data_9OD6
# 
_entry.id   9OD6 
# 
_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   9OD6         pdb_00009od6 10.2210/pdb9od6/pdb 
WWPDB D_1000295354 ?            ?                   
# 
_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       2025-05-07 
_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                        9OD6 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-25 
_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 from Cryptosporidium parvum in complex with citrate' 
_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 'CITRIC ACID'                   192.124   3   ?       ? ? ? 
3 water       nat water                           18.015    457 ?       ? ? ? 
# 
_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 'CITRIC ACID' CIT 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   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 
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 
CIT non-polymer         . 'CITRIC ACID'   ? 'C6 H8 O7'       192.124 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CIT 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CIT 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 CIT 1   201 101 CIT CIT A . 
E 2 CIT 1   201 102 CIT CIT B . 
F 2 CIT 1   201 103 CIT CIT C . 
G 3 HOH 1   301 450 HOH HOH A . 
G 3 HOH 2   302 198 HOH HOH A . 
G 3 HOH 3   303 330 HOH HOH A . 
G 3 HOH 4   304 410 HOH HOH A . 
G 3 HOH 5   305 85  HOH HOH A . 
G 3 HOH 6   306 364 HOH HOH A . 
G 3 HOH 7   307 209 HOH HOH A . 
G 3 HOH 8   308 335 HOH HOH A . 
G 3 HOH 9   309 352 HOH HOH A . 
G 3 HOH 10  310 399 HOH HOH A . 
G 3 HOH 11  311 372 HOH HOH A . 
G 3 HOH 12  312 225 HOH HOH A . 
G 3 HOH 13  313 293 HOH HOH A . 
G 3 HOH 14  314 207 HOH HOH A . 
G 3 HOH 15  315 5   HOH HOH A . 
G 3 HOH 16  316 325 HOH HOH A . 
G 3 HOH 17  317 106 HOH HOH A . 
G 3 HOH 18  318 119 HOH HOH A . 
G 3 HOH 19  319 228 HOH HOH A . 
G 3 HOH 20  320 363 HOH HOH A . 
G 3 HOH 21  321 101 HOH HOH A . 
G 3 HOH 22  322 323 HOH HOH A . 
G 3 HOH 23  323 390 HOH HOH A . 
G 3 HOH 24  324 147 HOH HOH A . 
G 3 HOH 25  325 73  HOH HOH A . 
G 3 HOH 26  326 18  HOH HOH A . 
G 3 HOH 27  327 237 HOH HOH A . 
G 3 HOH 28  328 292 HOH HOH A . 
G 3 HOH 29  329 72  HOH HOH A . 
G 3 HOH 30  330 69  HOH HOH A . 
G 3 HOH 31  331 377 HOH HOH A . 
G 3 HOH 32  332 430 HOH HOH A . 
G 3 HOH 33  333 346 HOH HOH A . 
G 3 HOH 34  334 144 HOH HOH A . 
G 3 HOH 35  335 112 HOH HOH A . 
G 3 HOH 36  336 124 HOH HOH A . 
G 3 HOH 37  337 303 HOH HOH A . 
G 3 HOH 38  338 175 HOH HOH A . 
G 3 HOH 39  339 203 HOH HOH A . 
G 3 HOH 40  340 118 HOH HOH A . 
G 3 HOH 41  341 220 HOH HOH A . 
G 3 HOH 42  342 168 HOH HOH A . 
G 3 HOH 43  343 37  HOH HOH A . 
G 3 HOH 44  344 8   HOH HOH A . 
G 3 HOH 45  345 35  HOH HOH A . 
G 3 HOH 46  346 221 HOH HOH A . 
G 3 HOH 47  347 96  HOH HOH A . 
G 3 HOH 48  348 253 HOH HOH A . 
G 3 HOH 49  349 210 HOH HOH A . 
G 3 HOH 50  350 179 HOH HOH A . 
G 3 HOH 51  351 370 HOH HOH A . 
G 3 HOH 52  352 102 HOH HOH A . 
G 3 HOH 53  353 31  HOH HOH A . 
G 3 HOH 54  354 59  HOH HOH A . 
G 3 HOH 55  355 191 HOH HOH A . 
G 3 HOH 56  356 14  HOH HOH A . 
G 3 HOH 57  357 11  HOH HOH A . 
G 3 HOH 58  358 41  HOH HOH A . 
G 3 HOH 59  359 192 HOH HOH A . 
G 3 HOH 60  360 86  HOH HOH A . 
G 3 HOH 61  361 9   HOH HOH A . 
G 3 HOH 62  362 99  HOH HOH A . 
G 3 HOH 63  363 294 HOH HOH A . 
G 3 HOH 64  364 451 HOH HOH A . 
G 3 HOH 65  365 434 HOH HOH A . 
G 3 HOH 66  366 100 HOH HOH A . 
G 3 HOH 67  367 74  HOH HOH A . 
G 3 HOH 68  368 199 HOH HOH A . 
G 3 HOH 69  369 15  HOH HOH A . 
G 3 HOH 70  370 386 HOH HOH A . 
G 3 HOH 71  371 257 HOH HOH A . 
G 3 HOH 72  372 48  HOH HOH A . 
G 3 HOH 73  373 182 HOH HOH A . 
G 3 HOH 74  374 103 HOH HOH A . 
G 3 HOH 75  375 264 HOH HOH A . 
G 3 HOH 76  376 16  HOH HOH A . 
G 3 HOH 77  377 275 HOH HOH A . 
G 3 HOH 78  378 13  HOH HOH A . 
G 3 HOH 79  379 347 HOH HOH A . 
G 3 HOH 80  380 52  HOH HOH A . 
G 3 HOH 81  381 134 HOH HOH A . 
G 3 HOH 82  382 93  HOH HOH A . 
G 3 HOH 83  383 163 HOH HOH A . 
G 3 HOH 84  384 107 HOH HOH A . 
G 3 HOH 85  385 384 HOH HOH A . 
G 3 HOH 86  386 75  HOH HOH A . 
G 3 HOH 87  387 26  HOH HOH A . 
G 3 HOH 88  388 208 HOH HOH A . 
G 3 HOH 89  389 6   HOH HOH A . 
G 3 HOH 90  390 135 HOH HOH A . 
G 3 HOH 91  391 348 HOH HOH A . 
G 3 HOH 92  392 345 HOH HOH A . 
G 3 HOH 93  393 361 HOH HOH A . 
G 3 HOH 94  394 342 HOH HOH A . 
G 3 HOH 95  395 295 HOH HOH A . 
G 3 HOH 96  396 186 HOH HOH A . 
G 3 HOH 97  397 412 HOH HOH A . 
G 3 HOH 98  398 378 HOH HOH A . 
G 3 HOH 99  399 332 HOH HOH A . 
G 3 HOH 100 400 190 HOH HOH A . 
G 3 HOH 101 401 319 HOH HOH A . 
G 3 HOH 102 402 420 HOH HOH A . 
G 3 HOH 103 403 258 HOH HOH A . 
G 3 HOH 104 404 409 HOH HOH A . 
G 3 HOH 105 405 159 HOH HOH A . 
G 3 HOH 106 406 184 HOH HOH A . 
G 3 HOH 107 407 329 HOH HOH A . 
G 3 HOH 108 408 153 HOH HOH A . 
G 3 HOH 109 409 311 HOH HOH A . 
G 3 HOH 110 410 114 HOH HOH A . 
G 3 HOH 111 411 49  HOH HOH A . 
G 3 HOH 112 412 302 HOH HOH A . 
G 3 HOH 113 413 371 HOH HOH A . 
G 3 HOH 114 414 415 HOH HOH A . 
G 3 HOH 115 415 177 HOH HOH A . 
G 3 HOH 116 416 57  HOH HOH A . 
G 3 HOH 117 417 255 HOH HOH A . 
G 3 HOH 118 418 111 HOH HOH A . 
G 3 HOH 119 419 359 HOH HOH A . 
G 3 HOH 120 420 261 HOH HOH A . 
G 3 HOH 121 421 406 HOH HOH A . 
G 3 HOH 122 422 318 HOH HOH A . 
G 3 HOH 123 423 152 HOH HOH A . 
G 3 HOH 124 424 62  HOH HOH A . 
G 3 HOH 125 425 320 HOH HOH A . 
G 3 HOH 126 426 171 HOH HOH A . 
G 3 HOH 127 427 431 HOH HOH A . 
G 3 HOH 128 428 369 HOH HOH A . 
G 3 HOH 129 429 355 HOH HOH A . 
G 3 HOH 130 430 276 HOH HOH A . 
G 3 HOH 131 431 388 HOH HOH A . 
G 3 HOH 132 432 155 HOH HOH A . 
G 3 HOH 133 433 422 HOH HOH A . 
G 3 HOH 134 434 306 HOH HOH A . 
G 3 HOH 135 435 452 HOH HOH A . 
G 3 HOH 136 436 271 HOH HOH A . 
G 3 HOH 137 437 375 HOH HOH A . 
G 3 HOH 138 438 288 HOH HOH A . 
G 3 HOH 139 439 373 HOH HOH A . 
G 3 HOH 140 440 307 HOH HOH A . 
G 3 HOH 141 441 205 HOH HOH A . 
G 3 HOH 142 442 61  HOH HOH A . 
G 3 HOH 143 443 246 HOH HOH A . 
G 3 HOH 144 444 239 HOH HOH A . 
G 3 HOH 145 445 283 HOH HOH A . 
G 3 HOH 146 446 340 HOH HOH A . 
G 3 HOH 147 447 438 HOH HOH A . 
G 3 HOH 148 448 244 HOH HOH A . 
G 3 HOH 149 449 251 HOH HOH A . 
G 3 HOH 150 450 32  HOH HOH A . 
G 3 HOH 151 451 439 HOH HOH A . 
G 3 HOH 152 452 407 HOH HOH A . 
G 3 HOH 153 453 382 HOH HOH A . 
G 3 HOH 154 454 206 HOH HOH A . 
G 3 HOH 155 455 284 HOH HOH A . 
G 3 HOH 156 456 193 HOH HOH A . 
G 3 HOH 157 457 202 HOH HOH A . 
G 3 HOH 158 458 117 HOH HOH A . 
G 3 HOH 159 459 440 HOH HOH A . 
G 3 HOH 160 460 428 HOH HOH A . 
G 3 HOH 161 461 129 HOH HOH A . 
G 3 HOH 162 462 235 HOH HOH A . 
G 3 HOH 163 463 380 HOH HOH A . 
G 3 HOH 164 464 142 HOH HOH A . 
G 3 HOH 165 465 201 HOH HOH A . 
G 3 HOH 166 466 356 HOH HOH A . 
G 3 HOH 167 467 266 HOH HOH A . 
G 3 HOH 168 468 315 HOH HOH A . 
G 3 HOH 169 469 194 HOH HOH A . 
G 3 HOH 170 470 394 HOH HOH A . 
G 3 HOH 171 471 338 HOH HOH A . 
G 3 HOH 172 472 233 HOH HOH A . 
G 3 HOH 173 473 227 HOH HOH A . 
G 3 HOH 174 474 286 HOH HOH A . 
G 3 HOH 175 475 128 HOH HOH A . 
G 3 HOH 176 476 447 HOH HOH A . 
G 3 HOH 177 477 277 HOH HOH A . 
G 3 HOH 178 478 265 HOH HOH A . 
G 3 HOH 179 479 446 HOH HOH A . 
H 3 HOH 1   301 215 HOH HOH B . 
H 3 HOH 2   302 174 HOH HOH B . 
H 3 HOH 3   303 53  HOH HOH B . 
H 3 HOH 4   304 437 HOH HOH B . 
H 3 HOH 5   305 121 HOH HOH B . 
H 3 HOH 6   306 457 HOH HOH B . 
H 3 HOH 7   307 234 HOH HOH B . 
H 3 HOH 8   308 213 HOH HOH B . 
H 3 HOH 9   309 146 HOH HOH B . 
H 3 HOH 10  310 326 HOH HOH B . 
H 3 HOH 11  311 226 HOH HOH B . 
H 3 HOH 12  312 432 HOH HOH B . 
H 3 HOH 13  313 272 HOH HOH B . 
H 3 HOH 14  314 273 HOH HOH B . 
H 3 HOH 15  315 417 HOH HOH B . 
H 3 HOH 16  316 427 HOH HOH B . 
H 3 HOH 17  317 43  HOH HOH B . 
H 3 HOH 18  318 263 HOH HOH B . 
H 3 HOH 19  319 240 HOH HOH B . 
H 3 HOH 20  320 138 HOH HOH B . 
H 3 HOH 21  321 229 HOH HOH B . 
H 3 HOH 22  322 333 HOH HOH B . 
H 3 HOH 23  323 281 HOH HOH B . 
H 3 HOH 24  324 212 HOH HOH B . 
H 3 HOH 25  325 393 HOH HOH B . 
H 3 HOH 26  326 169 HOH HOH B . 
H 3 HOH 27  327 141 HOH HOH B . 
H 3 HOH 28  328 42  HOH HOH B . 
H 3 HOH 29  329 343 HOH HOH B . 
H 3 HOH 30  330 312 HOH HOH B . 
H 3 HOH 31  331 245 HOH HOH B . 
H 3 HOH 32  332 56  HOH HOH B . 
H 3 HOH 33  333 67  HOH HOH B . 
H 3 HOH 34  334 64  HOH HOH B . 
H 3 HOH 35  335 51  HOH HOH B . 
H 3 HOH 36  336 50  HOH HOH B . 
H 3 HOH 37  337 21  HOH HOH B . 
H 3 HOH 38  338 4   HOH HOH B . 
H 3 HOH 39  339 97  HOH HOH B . 
H 3 HOH 40  340 71  HOH HOH B . 
H 3 HOH 41  341 27  HOH HOH B . 
H 3 HOH 42  342 309 HOH HOH B . 
H 3 HOH 43  343 68  HOH HOH B . 
H 3 HOH 44  344 214 HOH HOH B . 
H 3 HOH 45  345 238 HOH HOH B . 
H 3 HOH 46  346 223 HOH HOH B . 
H 3 HOH 47  347 242 HOH HOH B . 
H 3 HOH 48  348 164 HOH HOH B . 
H 3 HOH 49  349 161 HOH HOH B . 
H 3 HOH 50  350 120 HOH HOH B . 
H 3 HOH 51  351 132 HOH HOH B . 
H 3 HOH 52  352 358 HOH HOH B . 
H 3 HOH 53  353 122 HOH HOH B . 
H 3 HOH 54  354 357 HOH HOH B . 
H 3 HOH 55  355 178 HOH HOH B . 
H 3 HOH 56  356 89  HOH HOH B . 
H 3 HOH 57  357 82  HOH HOH B . 
H 3 HOH 58  358 28  HOH HOH B . 
H 3 HOH 59  359 316 HOH HOH B . 
H 3 HOH 60  360 33  HOH HOH B . 
H 3 HOH 61  361 413 HOH HOH B . 
H 3 HOH 62  362 324 HOH HOH B . 
H 3 HOH 63  363 218 HOH HOH B . 
H 3 HOH 64  364 200 HOH HOH B . 
H 3 HOH 65  365 387 HOH HOH B . 
H 3 HOH 66  366 63  HOH HOH B . 
H 3 HOH 67  367 10  HOH HOH B . 
H 3 HOH 68  368 405 HOH HOH B . 
H 3 HOH 69  369 196 HOH HOH B . 
H 3 HOH 70  370 350 HOH HOH B . 
H 3 HOH 71  371 22  HOH HOH B . 
H 3 HOH 72  372 414 HOH HOH B . 
H 3 HOH 73  373 419 HOH HOH B . 
H 3 HOH 74  374 443 HOH HOH B . 
H 3 HOH 75  375 176 HOH HOH B . 
H 3 HOH 76  376 411 HOH HOH B . 
H 3 HOH 77  377 150 HOH HOH B . 
H 3 HOH 78  378 268 HOH HOH B . 
H 3 HOH 79  379 219 HOH HOH B . 
H 3 HOH 80  380 426 HOH HOH B . 
H 3 HOH 81  381 188 HOH HOH B . 
H 3 HOH 82  382 105 HOH HOH B . 
H 3 HOH 83  383 322 HOH HOH B . 
H 3 HOH 84  384 254 HOH HOH B . 
H 3 HOH 85  385 79  HOH HOH B . 
H 3 HOH 86  386 262 HOH HOH B . 
H 3 HOH 87  387 367 HOH HOH B . 
H 3 HOH 88  388 287 HOH HOH B . 
H 3 HOH 89  389 84  HOH HOH B . 
H 3 HOH 90  390 185 HOH HOH B . 
H 3 HOH 91  391 249 HOH HOH B . 
H 3 HOH 92  392 305 HOH HOH B . 
H 3 HOH 93  393 162 HOH HOH B . 
H 3 HOH 94  394 40  HOH HOH B . 
H 3 HOH 95  395 110 HOH HOH B . 
H 3 HOH 96  396 66  HOH HOH B . 
H 3 HOH 97  397 160 HOH HOH B . 
H 3 HOH 98  398 416 HOH HOH B . 
H 3 HOH 99  399 247 HOH HOH B . 
H 3 HOH 100 400 339 HOH HOH B . 
H 3 HOH 101 401 366 HOH HOH B . 
H 3 HOH 102 402 267 HOH HOH B . 
H 3 HOH 103 403 425 HOH HOH B . 
H 3 HOH 104 404 151 HOH HOH B . 
H 3 HOH 105 405 230 HOH HOH B . 
H 3 HOH 106 406 60  HOH HOH B . 
H 3 HOH 107 407 455 HOH HOH B . 
H 3 HOH 108 408 368 HOH HOH B . 
H 3 HOH 109 409 353 HOH HOH B . 
H 3 HOH 110 410 290 HOH HOH B . 
H 3 HOH 111 411 442 HOH HOH B . 
H 3 HOH 112 412 402 HOH HOH B . 
H 3 HOH 113 413 65  HOH HOH B . 
H 3 HOH 114 414 328 HOH HOH B . 
H 3 HOH 115 415 285 HOH HOH B . 
H 3 HOH 116 416 216 HOH HOH B . 
H 3 HOH 117 417 224 HOH HOH B . 
H 3 HOH 118 418 310 HOH HOH B . 
H 3 HOH 119 419 433 HOH HOH B . 
H 3 HOH 120 420 379 HOH HOH B . 
H 3 HOH 121 421 445 HOH HOH B . 
H 3 HOH 122 422 282 HOH HOH B . 
H 3 HOH 123 423 256 HOH HOH B . 
H 3 HOH 124 424 360 HOH HOH B . 
H 3 HOH 125 425 90  HOH HOH B . 
H 3 HOH 126 426 351 HOH HOH B . 
I 3 HOH 1   301 317 HOH HOH C . 
I 3 HOH 2   302 362 HOH HOH C . 
I 3 HOH 3   303 385 HOH HOH C . 
I 3 HOH 4   304 449 HOH HOH C . 
I 3 HOH 5   305 126 HOH HOH C . 
I 3 HOH 6   306 408 HOH HOH C . 
I 3 HOH 7   307 383 HOH HOH C . 
I 3 HOH 8   308 170 HOH HOH C . 
I 3 HOH 9   309 289 HOH HOH C . 
I 3 HOH 10  310 94  HOH HOH C . 
I 3 HOH 11  311 166 HOH HOH C . 
I 3 HOH 12  312 149 HOH HOH C . 
I 3 HOH 13  313 36  HOH HOH C . 
I 3 HOH 14  314 130 HOH HOH C . 
I 3 HOH 15  315 298 HOH HOH C . 
I 3 HOH 16  316 296 HOH HOH C . 
I 3 HOH 17  317 19  HOH HOH C . 
I 3 HOH 18  318 211 HOH HOH C . 
I 3 HOH 19  319 441 HOH HOH C . 
I 3 HOH 20  320 301 HOH HOH C . 
I 3 HOH 21  321 376 HOH HOH C . 
I 3 HOH 22  322 189 HOH HOH C . 
I 3 HOH 23  323 435 HOH HOH C . 
I 3 HOH 24  324 173 HOH HOH C . 
I 3 HOH 25  325 77  HOH HOH C . 
I 3 HOH 26  326 92  HOH HOH C . 
I 3 HOH 27  327 279 HOH HOH C . 
I 3 HOH 28  328 17  HOH HOH C . 
I 3 HOH 29  329 336 HOH HOH C . 
I 3 HOH 30  330 12  HOH HOH C . 
I 3 HOH 31  331 308 HOH HOH C . 
I 3 HOH 32  332 454 HOH HOH C . 
I 3 HOH 33  333 297 HOH HOH C . 
I 3 HOH 34  334 270 HOH HOH C . 
I 3 HOH 35  335 91  HOH HOH C . 
I 3 HOH 36  336 24  HOH HOH C . 
I 3 HOH 37  337 80  HOH HOH C . 
I 3 HOH 38  338 76  HOH HOH C . 
I 3 HOH 39  339 136 HOH HOH C . 
I 3 HOH 40  340 140 HOH HOH C . 
I 3 HOH 41  341 187 HOH HOH C . 
I 3 HOH 42  342 165 HOH HOH C . 
I 3 HOH 43  343 47  HOH HOH C . 
I 3 HOH 44  344 20  HOH HOH C . 
I 3 HOH 45  345 269 HOH HOH C . 
I 3 HOH 46  346 180 HOH HOH C . 
I 3 HOH 47  347 45  HOH HOH C . 
I 3 HOH 48  348 389 HOH HOH C . 
I 3 HOH 49  349 260 HOH HOH C . 
I 3 HOH 50  350 231 HOH HOH C . 
I 3 HOH 51  351 248 HOH HOH C . 
I 3 HOH 52  352 131 HOH HOH C . 
I 3 HOH 53  353 108 HOH HOH C . 
I 3 HOH 54  354 88  HOH HOH C . 
I 3 HOH 55  355 1   HOH HOH C . 
I 3 HOH 56  356 404 HOH HOH C . 
I 3 HOH 57  357 109 HOH HOH C . 
I 3 HOH 58  358 39  HOH HOH C . 
I 3 HOH 59  359 304 HOH HOH C . 
I 3 HOH 60  360 156 HOH HOH C . 
I 3 HOH 61  361 397 HOH HOH C . 
I 3 HOH 62  362 2   HOH HOH C . 
I 3 HOH 63  363 34  HOH HOH C . 
I 3 HOH 64  364 30  HOH HOH C . 
I 3 HOH 65  365 38  HOH HOH C . 
I 3 HOH 66  366 158 HOH HOH C . 
I 3 HOH 67  367 137 HOH HOH C . 
I 3 HOH 68  368 29  HOH HOH C . 
I 3 HOH 69  369 116 HOH HOH C . 
I 3 HOH 70  370 95  HOH HOH C . 
I 3 HOH 71  371 115 HOH HOH C . 
I 3 HOH 72  372 3   HOH HOH C . 
I 3 HOH 73  373 327 HOH HOH C . 
I 3 HOH 74  374 424 HOH HOH C . 
I 3 HOH 75  375 23  HOH HOH C . 
I 3 HOH 76  376 278 HOH HOH C . 
I 3 HOH 77  377 365 HOH HOH C . 
I 3 HOH 78  378 418 HOH HOH C . 
I 3 HOH 79  379 139 HOH HOH C . 
I 3 HOH 80  380 181 HOH HOH C . 
I 3 HOH 81  381 58  HOH HOH C . 
I 3 HOH 82  382 78  HOH HOH C . 
I 3 HOH 83  383 243 HOH HOH C . 
I 3 HOH 84  384 46  HOH HOH C . 
I 3 HOH 85  385 113 HOH HOH C . 
I 3 HOH 86  386 217 HOH HOH C . 
I 3 HOH 87  387 172 HOH HOH C . 
I 3 HOH 88  388 313 HOH HOH C . 
I 3 HOH 89  389 44  HOH HOH C . 
I 3 HOH 90  390 250 HOH HOH C . 
I 3 HOH 91  391 157 HOH HOH C . 
I 3 HOH 92  392 133 HOH HOH C . 
I 3 HOH 93  393 314 HOH HOH C . 
I 3 HOH 94  394 421 HOH HOH C . 
I 3 HOH 95  395 127 HOH HOH C . 
I 3 HOH 96  396 204 HOH HOH C . 
I 3 HOH 97  397 54  HOH HOH C . 
I 3 HOH 98  398 87  HOH HOH C . 
I 3 HOH 99  399 70  HOH HOH C . 
I 3 HOH 100 400 81  HOH HOH C . 
I 3 HOH 101 401 395 HOH HOH C . 
I 3 HOH 102 402 123 HOH HOH C . 
I 3 HOH 103 403 98  HOH HOH C . 
I 3 HOH 104 404 291 HOH HOH C . 
I 3 HOH 105 405 321 HOH HOH C . 
I 3 HOH 106 406 145 HOH HOH C . 
I 3 HOH 107 407 232 HOH HOH C . 
I 3 HOH 108 408 143 HOH HOH C . 
I 3 HOH 109 409 83  HOH HOH C . 
I 3 HOH 110 410 444 HOH HOH C . 
I 3 HOH 111 411 400 HOH HOH C . 
I 3 HOH 112 412 7   HOH HOH C . 
I 3 HOH 113 413 222 HOH HOH C . 
I 3 HOH 114 414 344 HOH HOH C . 
I 3 HOH 115 415 252 HOH HOH C . 
I 3 HOH 116 416 341 HOH HOH C . 
I 3 HOH 117 417 448 HOH HOH C . 
I 3 HOH 118 418 453 HOH HOH C . 
I 3 HOH 119 419 429 HOH HOH C . 
I 3 HOH 120 420 436 HOH HOH C . 
I 3 HOH 121 421 236 HOH HOH C . 
I 3 HOH 122 422 391 HOH HOH C . 
I 3 HOH 123 423 349 HOH HOH C . 
I 3 HOH 124 424 241 HOH HOH C . 
I 3 HOH 125 425 183 HOH HOH C . 
I 3 HOH 126 426 195 HOH HOH C . 
I 3 HOH 127 427 148 HOH HOH C . 
I 3 HOH 128 428 259 HOH HOH C . 
I 3 HOH 129 429 334 HOH HOH C . 
I 3 HOH 130 430 299 HOH HOH C . 
I 3 HOH 131 431 25  HOH HOH C . 
I 3 HOH 132 432 354 HOH HOH C . 
I 3 HOH 133 433 381 HOH HOH C . 
I 3 HOH 134 434 154 HOH HOH C . 
I 3 HOH 135 435 401 HOH HOH C . 
I 3 HOH 136 436 398 HOH HOH C . 
I 3 HOH 137 437 55  HOH HOH C . 
I 3 HOH 138 438 280 HOH HOH C . 
I 3 HOH 139 439 403 HOH HOH C . 
I 3 HOH 140 440 167 HOH HOH C . 
I 3 HOH 141 441 392 HOH HOH C . 
I 3 HOH 142 442 300 HOH HOH C . 
I 3 HOH 143 443 337 HOH HOH C . 
I 3 HOH 144 444 374 HOH HOH C . 
I 3 HOH 145 445 396 HOH HOH C . 
I 3 HOH 146 446 456 HOH HOH C . 
I 3 HOH 147 447 274 HOH HOH C . 
I 3 HOH 148 448 331 HOH HOH C . 
I 3 HOH 149 449 104 HOH HOH C . 
I 3 HOH 150 450 125 HOH HOH C . 
I 3 HOH 151 451 197 HOH HOH C . 
I 3 HOH 152 452 423 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 B GLU 158 ? CG  ? B GLU 141 CG  
12 1 Y 1 B GLU 158 ? CD  ? B GLU 141 CD  
13 1 Y 1 B GLU 158 ? OE1 ? B GLU 141 OE1 
14 1 Y 1 B GLU 158 ? OE2 ? B GLU 141 OE2 
15 1 Y 1 C HIS 25  ? CG  ? C HIS 8   CG  
16 1 Y 1 C HIS 25  ? ND1 ? C HIS 8   ND1 
17 1 Y 1 C HIS 25  ? CD2 ? C HIS 8   CD2 
18 1 Y 1 C HIS 25  ? CE1 ? C HIS 8   CE1 
19 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                     9OD6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.775 
_cell.length_a_esd                 ? 
_cell.length_b                     69.775 
_cell.length_b_esd                 ? 
_cell.length_c                     314.836 
_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                         9OD6 
_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                   9OD6 
_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             2.09 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.25 
_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. Citrate acquired from the crystallant. plate Liu-S-177 D2, Puck: PSL-0604, Cryo: 35% MPD, 0.1M sodium Formate, 0.1M Citrate pH 5.5
;
_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         2025-02-02 
_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                                       9OD6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.45 
_reflns.d_resolution_low                               47.93 
_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                                     81948 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                38.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.03 
_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                                0.136 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       3188737 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.134 
_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                                    1.45 
_reflns_shell.d_res_low                                     1.49 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           242693 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5933 
_reflns_shell.percent_possible_obs                          100.0 
_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                               40.9 
_reflns_shell.pdbx_chi_squared                              0.84 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               2.985 
_reflns_shell.pdbx_Rpim_I_all                               0.465 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.690 
_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                                  2.949 
_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                                 9OD6 
_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                            1.45 
_refine.ls_d_res_low                             47.93 
_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                     81770 
_refine.ls_number_reflns_R_free                  4131 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1339 
_refine.ls_R_factor_R_free                       0.1680 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1321 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_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                 15.39 
_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                            0.17 
_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                       1.45 
_refine_hist.d_res_low                        47.93 
_refine_hist.number_atoms_solvent             457 
_refine_hist.number_atoms_total               3993 
_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        3497 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_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  ? 3731 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.967  ? 5062 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 14.969 ? 1479 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.074  ? 551  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 660  ? 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' 1.45 1.47  . . 147 2511 100.00 . . . . 0.2639 . . . . . . . . . . . . . . . 0.3438 
'X-RAY DIFFRACTION' 1.47 1.48  . . 139 2551 100.00 . . . . 0.2363 . . . . . . . . . . . . . . . 0.2739 
'X-RAY DIFFRACTION' 1.48 1.50  . . 131 2500 100.00 . . . . 0.2081 . . . . . . . . . . . . . . . 0.3070 
'X-RAY DIFFRACTION' 1.50 1.52  . . 144 2564 100.00 . . . . 0.1778 . . . . . . . . . . . . . . . 0.2228 
'X-RAY DIFFRACTION' 1.52 1.54  . . 125 2504 100.00 . . . . 0.1651 . . . . . . . . . . . . . . . 0.2242 
'X-RAY DIFFRACTION' 1.54 1.56  . . 101 2580 100.00 . . . . 0.1630 . . . . . . . . . . . . . . . 0.2050 
'X-RAY DIFFRACTION' 1.56 1.58  . . 141 2548 100.00 . . . . 0.1507 . . . . . . . . . . . . . . . 0.2368 
'X-RAY DIFFRACTION' 1.58 1.61  . . 128 2533 100.00 . . . . 0.1416 . . . . . . . . . . . . . . . 0.2106 
'X-RAY DIFFRACTION' 1.61 1.63  . . 122 2565 100.00 . . . . 0.1370 . . . . . . . . . . . . . . . 0.2141 
'X-RAY DIFFRACTION' 1.63 1.66  . . 129 2553 100.00 . . . . 0.1282 . . . . . . . . . . . . . . . 0.1861 
'X-RAY DIFFRACTION' 1.66 1.69  . . 135 2541 100.00 . . . . 0.1259 . . . . . . . . . . . . . . . 0.1708 
'X-RAY DIFFRACTION' 1.69 1.72  . . 137 2532 100.00 . . . . 0.1258 . . . . . . . . . . . . . . . 0.1843 
'X-RAY DIFFRACTION' 1.72 1.75  . . 134 2583 100.00 . . . . 0.1287 . . . . . . . . . . . . . . . 0.2217 
'X-RAY DIFFRACTION' 1.75 1.79  . . 137 2553 100.00 . . . . 0.1328 . . . . . . . . . . . . . . . 0.2029 
'X-RAY DIFFRACTION' 1.79 1.83  . . 156 2522 100.00 . . . . 0.1252 . . . . . . . . . . . . . . . 0.1789 
'X-RAY DIFFRACTION' 1.83 1.87  . . 146 2526 100.00 . . . . 0.1270 . . . . . . . . . . . . . . . 0.1788 
'X-RAY DIFFRACTION' 1.87 1.92  . . 153 2562 100.00 . . . . 0.1290 . . . . . . . . . . . . . . . 0.1882 
'X-RAY DIFFRACTION' 1.92 1.97  . . 124 2580 100.00 . . . . 0.1311 . . . . . . . . . . . . . . . 0.1777 
'X-RAY DIFFRACTION' 1.97 2.03  . . 150 2572 100.00 . . . . 0.1177 . . . . . . . . . . . . . . . 0.1574 
'X-RAY DIFFRACTION' 2.03 2.09  . . 130 2573 100.00 . . . . 0.1163 . . . . . . . . . . . . . . . 0.1782 
'X-RAY DIFFRACTION' 2.09 2.17  . . 149 2601 100.00 . . . . 0.1130 . . . . . . . . . . . . . . . 0.1500 
'X-RAY DIFFRACTION' 2.17 2.25  . . 142 2590 100.00 . . . . 0.1103 . . . . . . . . . . . . . . . 0.1514 
'X-RAY DIFFRACTION' 2.25 2.36  . . 140 2577 100.00 . . . . 0.1115 . . . . . . . . . . . . . . . 0.1464 
'X-RAY DIFFRACTION' 2.36 2.48  . . 137 2618 100.00 . . . . 0.1178 . . . . . . . . . . . . . . . 0.1456 
'X-RAY DIFFRACTION' 2.48 2.63  . . 144 2610 100.00 . . . . 0.1266 . . . . . . . . . . . . . . . 0.1628 
'X-RAY DIFFRACTION' 2.63 2.84  . . 151 2623 100.00 . . . . 0.1314 . . . . . . . . . . . . . . . 0.1540 
'X-RAY DIFFRACTION' 2.84 3.12  . . 122 2682 100.00 . . . . 0.1369 . . . . . . . . . . . . . . . 0.1598 
'X-RAY DIFFRACTION' 3.12 3.58  . . 140 2684 100.00 . . . . 0.1296 . . . . . . . . . . . . . . . 0.1580 
'X-RAY DIFFRACTION' 3.58 4.50  . . 140 2750 100.00 . . . . 0.1168 . . . . . . . . . . . . . . . 0.1303 
'X-RAY DIFFRACTION' 4.50 47.93 . . 157 2951 100.00 . . . . 0.1559 . . . . . . . . . . . . . . . 0.1780 
# 
_struct.entry_id                     9OD6 
_struct.title                        
'Crystal structure of nucleoside-diphosphate kinase from Cryptosporidium parvum in complex with citrate' 
_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        9OD6 
_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 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
# 
_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 9OD6 A 9 ? 156 ? Q5CR64 26 ? 173 ? 26 173 
2 1 9OD6 B 9 ? 156 ? Q5CR64 26 ? 173 ? 26 173 
3 1 9OD6 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 9OD6 MET A 1 ? UNP Q5CR64 ? ? 'expression tag' 18 1  
1 9OD6 ALA A 2 ? UNP Q5CR64 ? ? 'expression tag' 19 2  
1 9OD6 HIS A 3 ? UNP Q5CR64 ? ? 'expression tag' 20 3  
1 9OD6 HIS A 4 ? UNP Q5CR64 ? ? 'expression tag' 21 4  
1 9OD6 HIS A 5 ? UNP Q5CR64 ? ? 'expression tag' 22 5  
1 9OD6 HIS A 6 ? UNP Q5CR64 ? ? 'expression tag' 23 6  
1 9OD6 HIS A 7 ? UNP Q5CR64 ? ? 'expression tag' 24 7  
1 9OD6 HIS A 8 ? UNP Q5CR64 ? ? 'expression tag' 25 8  
2 9OD6 MET B 1 ? UNP Q5CR64 ? ? 'expression tag' 18 9  
2 9OD6 ALA B 2 ? UNP Q5CR64 ? ? 'expression tag' 19 10 
2 9OD6 HIS B 3 ? UNP Q5CR64 ? ? 'expression tag' 20 11 
2 9OD6 HIS B 4 ? UNP Q5CR64 ? ? 'expression tag' 21 12 
2 9OD6 HIS B 5 ? UNP Q5CR64 ? ? 'expression tag' 22 13 
2 9OD6 HIS B 6 ? UNP Q5CR64 ? ? 'expression tag' 23 14 
2 9OD6 HIS B 7 ? UNP Q5CR64 ? ? 'expression tag' 24 15 
2 9OD6 HIS B 8 ? UNP Q5CR64 ? ? 'expression tag' 25 16 
3 9OD6 MET C 1 ? UNP Q5CR64 ? ? 'expression tag' 18 17 
3 9OD6 ALA C 2 ? UNP Q5CR64 ? ? 'expression tag' 19 18 
3 9OD6 HIS C 3 ? UNP Q5CR64 ? ? 'expression tag' 20 19 
3 9OD6 HIS C 4 ? UNP Q5CR64 ? ? 'expression tag' 21 20 
3 9OD6 HIS C 5 ? UNP Q5CR64 ? ? 'expression tag' 22 21 
3 9OD6 HIS C 6 ? UNP Q5CR64 ? ? 'expression tag' 23 22 
3 9OD6 HIS C 7 ? UNP Q5CR64 ? ? 'expression tag' 24 23 
3 9OD6 HIS C 8 ? UNP Q5CR64 ? ? 'expression tag' 25 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6330  ? 
1 MORE         5     ? 
1 'SSA (A^2)'  20050 ? 
# 
_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 
# 
_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 ARG A 99  ? ALA A 103 ? ARG A 116 ALA A 120 5 ? 5  
HELX_P HELX_P8  AA8 THR A 107 ? CYS A 113 ? THR A 124 CYS A 130 1 ? 7  
HELX_P HELX_P9  AA9 GLN A 115 ? ASN A 119 ? GLN A 132 ASN A 136 5 ? 5  
HELX_P HELX_P10 AB1 SER A 126 ? PHE A 138 ? SER A 143 PHE A 155 1 ? 13 
HELX_P HELX_P11 AB2 LYS A 139 ? ILE A 143 ? LYS A 156 ILE A 160 5 ? 5  
HELX_P HELX_P12 AB3 LEU A 150 ? PHE A 155 ? LEU A 167 PHE A 172 1 ? 6  
HELX_P HELX_P13 AB4 LYS B 17  ? ARG B 23  ? LYS B 34  ARG B 40  1 ? 7  
HELX_P HELX_P14 AB5 VAL B 25  ? LYS B 35  ? VAL B 42  LYS B 52  1 ? 11 
HELX_P HELX_P15 AB6 THR B 49  ? TYR B 57  ? THR B 66  TYR B 74  1 ? 9  
HELX_P HELX_P16 AB7 ALA B 58  ? LYS B 61  ? ALA B 75  LYS B 78  5 ? 4  
HELX_P HELX_P17 AB8 PHE B 65  ? THR B 74  ? PHE B 82  THR B 91  1 ? 10 
HELX_P HELX_P18 AB9 ASP B 86  ? GLY B 96  ? ASP B 103 GLY B 113 1 ? 11 
HELX_P HELX_P19 AC1 ARG B 99  ? ALA B 103 ? ARG B 116 ALA B 120 5 ? 5  
HELX_P HELX_P20 AC2 THR B 107 ? CYS B 113 ? THR B 124 CYS B 130 1 ? 7  
HELX_P HELX_P21 AC3 GLN B 115 ? ASN B 119 ? GLN B 132 ASN B 136 5 ? 5  
HELX_P HELX_P22 AC4 SER B 126 ? PHE B 138 ? SER B 143 PHE B 155 1 ? 13 
HELX_P HELX_P23 AC5 LYS B 139 ? ILE B 143 ? LYS B 156 ILE B 160 5 ? 5  
HELX_P HELX_P24 AC6 LEU B 150 ? PHE B 155 ? LEU B 167 PHE B 172 1 ? 6  
HELX_P HELX_P25 AC7 LYS C 17  ? ARG C 23  ? LYS C 34  ARG C 40  1 ? 7  
HELX_P HELX_P26 AC8 VAL C 25  ? LYS C 35  ? VAL C 42  LYS C 52  1 ? 11 
HELX_P HELX_P27 AC9 THR C 49  ? TYR C 57  ? THR C 66  TYR C 74  1 ? 9  
HELX_P HELX_P28 AD1 ALA C 58  ? LYS C 61  ? ALA C 75  LYS C 78  5 ? 4  
HELX_P HELX_P29 AD2 PHE C 65  ? THR C 74  ? PHE C 82  THR C 91  1 ? 10 
HELX_P HELX_P30 AD3 ASP C 86  ? GLY C 96  ? ASP C 103 GLY C 113 1 ? 11 
HELX_P HELX_P31 AD4 ARG C 99  ? ALA C 103 ? ARG C 116 ALA C 120 5 ? 5  
HELX_P HELX_P32 AD5 THR C 107 ? CYS C 113 ? THR C 124 CYS C 130 1 ? 7  
HELX_P HELX_P33 AD6 GLN C 115 ? ASN C 119 ? GLN C 132 ASN C 136 5 ? 5  
HELX_P HELX_P34 AD7 SER C 126 ? PHE C 138 ? SER C 143 PHE C 155 1 ? 13 
HELX_P HELX_P35 AD8 LYS C 139 ? ILE C 143 ? LYS C 156 ILE C 160 5 ? 5  
HELX_P HELX_P36 AD9 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_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  ? ALA A 48  ? ARG A 56  ALA A 65  
AA1 2 GLY A 75  ? GLY A 84  ? GLY A 92  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 MET A 80 ? O MET A 97  N LEU A 14  ? N LEU A 31  
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                   9OD6 
_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  ? ? -97.15 32.74  
2 1 LEU A 137 ? ? 72.76  -27.61 
3 1 LEU B 137 ? ? 73.15  -27.85 
4 1 TYR C 74  ? ? -98.84 31.53  
5 1 LEU C 137 ? ? 73.70  -27.30 
# 
_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 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 382 ? G HOH . 
2 1 C HOH 376 ? I HOH . 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
HIS N    N N N 158 
HIS CA   C N S 159 
HIS C    C N N 160 
HIS O    O N N 161 
HIS CB   C N N 162 
HIS CG   C Y N 163 
HIS ND1  N Y N 164 
HIS CD2  C Y N 165 
HIS CE1  C Y N 166 
HIS NE2  N Y N 167 
HIS OXT  O N N 168 
HIS H    H N N 169 
HIS H2   H N N 170 
HIS HA   H N N 171 
HIS HB2  H N N 172 
HIS HB3  H N N 173 
HIS HD1  H N N 174 
HIS HD2  H N N 175 
HIS HE1  H N N 176 
HIS HE2  H N N 177 
HIS HXT  H N N 178 
HOH O    O N N 179 
HOH H1   H N N 180 
HOH H2   H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
PHE N    N N N 271 
PHE CA   C N S 272 
PHE C    C N N 273 
PHE O    O N N 274 
PHE CB   C N N 275 
PHE CG   C Y N 276 
PHE CD1  C Y N 277 
PHE CD2  C Y N 278 
PHE CE1  C Y N 279 
PHE CE2  C Y N 280 
PHE CZ   C Y N 281 
PHE OXT  O N N 282 
PHE H    H N N 283 
PHE H2   H N N 284 
PHE HA   H N N 285 
PHE HB2  H N N 286 
PHE HB3  H N N 287 
PHE HD1  H N N 288 
PHE HD2  H N N 289 
PHE HE1  H N N 290 
PHE HE2  H N N 291 
PHE HZ   H N N 292 
PHE HXT  H N N 293 
PRO N    N N N 294 
PRO CA   C N S 295 
PRO C    C N N 296 
PRO O    O N N 297 
PRO CB   C N N 298 
PRO CG   C N N 299 
PRO CD   C N N 300 
PRO OXT  O N N 301 
PRO H    H N N 302 
PRO HA   H N N 303 
PRO HB2  H N N 304 
PRO HB3  H N N 305 
PRO HG2  H N N 306 
PRO HG3  H N N 307 
PRO HD2  H N N 308 
PRO HD3  H N N 309 
PRO HXT  H N N 310 
SER N    N N N 311 
SER CA   C N S 312 
SER C    C N N 313 
SER O    O N N 314 
SER CB   C N N 315 
SER OG   O N N 316 
SER OXT  O N N 317 
SER H    H N N 318 
SER H2   H N N 319 
SER HA   H N N 320 
SER HB2  H N N 321 
SER HB3  H N N 322 
SER HG   H N N 323 
SER HXT  H N N 324 
THR N    N N N 325 
THR CA   C N S 326 
THR C    C N N 327 
THR O    O N N 328 
THR CB   C N R 329 
THR OG1  O N N 330 
THR CG2  C N N 331 
THR OXT  O N N 332 
THR H    H N N 333 
THR H2   H N N 334 
THR HA   H N N 335 
THR HB   H N N 336 
THR HG1  H N N 337 
THR HG21 H N N 338 
THR HG22 H N N 339 
THR HG23 H N N 340 
THR HXT  H N N 341 
TRP N    N N N 342 
TRP CA   C N S 343 
TRP C    C N N 344 
TRP O    O N N 345 
TRP CB   C N N 346 
TRP CG   C Y N 347 
TRP CD1  C Y N 348 
TRP CD2  C Y N 349 
TRP NE1  N Y N 350 
TRP CE2  C Y N 351 
TRP CE3  C Y N 352 
TRP CZ2  C Y N 353 
TRP CZ3  C Y N 354 
TRP CH2  C Y N 355 
TRP OXT  O N N 356 
TRP H    H N N 357 
TRP H2   H N N 358 
TRP HA   H N N 359 
TRP HB2  H N N 360 
TRP HB3  H N N 361 
TRP HD1  H N N 362 
TRP HE1  H N N 363 
TRP HE3  H N N 364 
TRP HZ2  H N N 365 
TRP HZ3  H N N 366 
TRP HH2  H N N 367 
TRP HXT  H N N 368 
TYR N    N N N 369 
TYR CA   C N S 370 
TYR C    C N N 371 
TYR O    O N N 372 
TYR CB   C N N 373 
TYR CG   C Y N 374 
TYR CD1  C Y N 375 
TYR CD2  C Y N 376 
TYR CE1  C Y N 377 
TYR CE2  C Y N 378 
TYR CZ   C Y N 379 
TYR OH   O N N 380 
TYR OXT  O N N 381 
TYR H    H N N 382 
TYR H2   H N N 383 
TYR HA   H N N 384 
TYR HB2  H N N 385 
TYR HB3  H N N 386 
TYR HD1  H N N 387 
TYR HD2  H N N 388 
TYR HE1  H N N 389 
TYR HE2  H N N 390 
TYR HH   H N N 391 
TYR HXT  H N N 392 
VAL N    N N N 393 
VAL CA   C N S 394 
VAL C    C N N 395 
VAL O    O N N 396 
VAL CB   C N N 397 
VAL CG1  C N N 398 
VAL CG2  C N N 399 
VAL OXT  O N N 400 
VAL H    H N N 401 
VAL H2   H N N 402 
VAL HA   H N N 403 
VAL HB   H N N 404 
VAL HG11 H N N 405 
VAL HG12 H N N 406 
VAL HG13 H N N 407 
VAL HG21 H N N 408 
VAL HG22 H N N 409 
VAL HG23 H N N 410 
VAL HXT  H N N 411 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
VAL N   CA   sing N N 378 
VAL N   H    sing N N 379 
VAL N   H2   sing N N 380 
VAL CA  C    sing N N 381 
VAL CA  CB   sing N N 382 
VAL CA  HA   sing N N 383 
VAL C   O    doub N N 384 
VAL C   OXT  sing N N 385 
VAL CB  CG1  sing N N 386 
VAL CB  CG2  sing N N 387 
VAL CB  HB   sing N N 388 
VAL CG1 HG11 sing N N 389 
VAL CG1 HG12 sing N N 390 
VAL CG1 HG13 sing N N 391 
VAL CG2 HG21 sing N N 392 
VAL CG2 HG22 sing N N 393 
VAL CG2 HG23 sing N N 394 
VAL OXT HXT  sing N N 395 
# 
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                    9OD6 
_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]   0.014332 
_atom_sites.fract_transf_matrix[1][2]   0.008274 
_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]   0.016549 
_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]   0.003176 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . HIS A 1 8   ? 10.985  53.576 6.838  1.00 46.64 ? 25  HIS A N   1 
ATOM   2    C CA  . HIS A 1 8   ? 9.649   53.572 7.425  1.00 40.58 ? 25  HIS A CA  1 
ATOM   3    C C   . HIS A 1 8   ? 9.358   52.220 8.067  1.00 38.26 ? 25  HIS A C   1 
ATOM   4    O O   . HIS A 1 8   ? 9.590   51.171 7.478  1.00 39.46 ? 25  HIS A O   1 
ATOM   5    C CB  . HIS A 1 8   ? 8.600   53.845 6.349  1.00 44.87 ? 25  HIS A CB  1 
ATOM   6    N N   . VAL A 1 9   ? 8.851   52.225 9.285  1.00 31.38 ? 26  VAL A N   1 
ATOM   7    C CA  . VAL A 1 9   ? 8.446   50.959 9.861  1.00 24.51 ? 26  VAL A CA  1 
ATOM   8    C C   . VAL A 1 9   ? 7.012   50.678 9.440  1.00 20.41 ? 26  VAL A C   1 
ATOM   9    O O   . VAL A 1 9   ? 6.313   51.552 8.915  1.00 23.19 ? 26  VAL A O   1 
ATOM   10   C CB  . VAL A 1 9   ? 8.619   50.935 11.390 1.00 26.80 ? 26  VAL A CB  1 
ATOM   11   C CG1 . VAL A 1 9   ? 10.081  51.202 11.739 1.00 28.37 ? 26  VAL A CG1 1 
ATOM   12   C CG2 . VAL A 1 9   ? 7.709   51.920 12.045 1.00 27.98 ? 26  VAL A CG2 1 
ATOM   13   N N   . GLU A 1 10  ? 6.581   49.448 9.629  1.00 18.25 ? 27  GLU A N   1 
ATOM   14   C CA  . GLU A 1 10  ? 5.179   49.091 9.496  1.00 19.25 ? 27  GLU A CA  1 
ATOM   15   C C   . GLU A 1 10  ? 4.798   48.227 10.687 1.00 14.17 ? 27  GLU A C   1 
ATOM   16   O O   . GLU A 1 10  ? 5.636   47.916 11.537 1.00 14.90 ? 27  GLU A O   1 
ATOM   17   C CB  . GLU A 1 10  ? 4.926   48.387 8.167  1.00 22.33 ? 27  GLU A CB  1 
ATOM   18   C CG  . GLU A 1 10  ? 5.662   47.116 8.043  1.00 22.94 ? 27  GLU A CG  1 
ATOM   19   C CD  . GLU A 1 10  ? 5.710   46.593 6.606  1.00 25.19 ? 27  GLU A CD  1 
ATOM   20   O OE1 . GLU A 1 10  ? 5.441   47.327 5.638  1.00 31.83 ? 27  GLU A OE1 1 
ATOM   21   O OE2 . GLU A 1 10  ? 6.003   45.417 6.461  1.00 20.17 ? 27  GLU A OE2 1 
ATOM   22   N N   . GLN A 1 11  ? 3.517   47.857 10.753 1.00 15.46 ? 28  GLN A N   1 
ATOM   23   C CA  . GLN A 1 11  ? 2.978   47.037 11.822 1.00 16.39 ? 28  GLN A CA  1 
ATOM   24   C C   . GLN A 1 11  ? 2.294   45.820 11.222 1.00 15.40 ? 28  GLN A C   1 
ATOM   25   O O   . GLN A 1 11  ? 1.599   45.916 10.201 1.00 17.18 ? 28  GLN A O   1 
ATOM   26   C CB  . GLN A 1 11  ? 2.002   47.827 12.702 1.00 16.82 ? 28  GLN A CB  1 
ATOM   27   C CG  . GLN A 1 11  ? 2.694   48.915 13.490 1.00 19.18 ? 28  GLN A CG  1 
ATOM   28   C CD  . GLN A 1 11  ? 1.805   49.586 14.510 1.00 21.05 ? 28  GLN A CD  1 
ATOM   29   O OE1 . GLN A 1 11  ? 0.602   49.327 14.582 1.00 24.84 ? 28  GLN A OE1 1 
ATOM   30   N NE2 . GLN A 1 11  ? 2.392   50.454 15.312 1.00 21.17 ? 28  GLN A NE2 1 
ATOM   31   N N   . THR A 1 12  ? 2.504   44.670 11.857 1.00 14.08 ? 29  THR A N   1 
ATOM   32   C CA  . THR A 1 12  ? 1.860   43.436 11.450 1.00 15.34 ? 29  THR A CA  1 
ATOM   33   C C   . THR A 1 12  ? 1.074   42.850 12.612 1.00 15.23 ? 29  THR A C   1 
ATOM   34   O O   . THR A 1 12  ? 1.399   43.090 13.780 1.00 15.01 ? 29  THR A O   1 
ATOM   35   C CB  . THR A 1 12  ? 2.870   42.418 10.891 1.00 15.30 ? 29  THR A CB  1 
ATOM   36   O OG1 . THR A 1 12  ? 2.147   41.384 10.210 1.00 16.87 ? 29  THR A OG1 1 
ATOM   37   C CG2 . THR A 1 12  ? 3.745   41.809 11.965 1.00 14.95 ? 29  THR A CG2 1 
ATOM   38   N N   . TYR A 1 13  ? 0.025   42.086 12.275 1.00 15.07 ? 30  TYR A N   1 
ATOM   39   C CA  . TYR A 1 13  ? -0.763  41.348 13.259 1.00 14.41 ? 30  TYR A CA  1 
ATOM   40   C C   . TYR A 1 13  ? -0.199  39.933 13.371 1.00 14.61 ? 30  TYR A C   1 
ATOM   41   O O   . TYR A 1 13  ? -0.110  39.214 12.375 1.00 15.75 ? 30  TYR A O   1 
ATOM   42   C CB  . TYR A 1 13  ? -2.246  41.304 12.871 1.00 14.29 ? 30  TYR A CB  1 
ATOM   43   C CG  . TYR A 1 13  ? -3.059  40.527 13.877 1.00 13.32 ? 30  TYR A CG  1 
ATOM   44   C CD1 . TYR A 1 13  ? -3.245  41.015 15.156 1.00 14.84 ? 30  TYR A CD1 1 
ATOM   45   C CD2 . TYR A 1 13  ? -3.595  39.289 13.566 1.00 14.42 ? 30  TYR A CD2 1 
ATOM   46   C CE1 . TYR A 1 13  ? -3.949  40.291 16.094 1.00 15.46 ? 30  TYR A CE1 1 
ATOM   47   C CE2 . TYR A 1 13  ? -4.294  38.548 14.510 1.00 15.13 ? 30  TYR A CE2 1 
ATOM   48   C CZ  . TYR A 1 13  ? -4.480  39.070 15.770 1.00 14.14 ? 30  TYR A CZ  1 
ATOM   49   O OH  . TYR A 1 13  ? -5.167  38.378 16.748 1.00 17.43 ? 30  TYR A OH  1 
ATOM   50   N N   . LEU A 1 14  ? 0.200   39.543 14.584 1.00 13.83 ? 31  LEU A N   1 
ATOM   51   C CA  . LEU A 1 14  ? 0.671   38.199 14.890 1.00 13.65 ? 31  LEU A CA  1 
ATOM   52   C C   . LEU A 1 14  ? -0.190  37.633 16.005 1.00 14.97 ? 31  LEU A C   1 
ATOM   53   O O   . LEU A 1 14  ? -0.475  38.322 16.986 1.00 16.93 ? 31  LEU A O   1 
ATOM   54   C CB  . LEU A 1 14  ? 2.141   38.210 15.331 1.00 15.19 ? 31  LEU A CB  1 
ATOM   55   C CG  . LEU A 1 14  ? 3.100   38.507 14.181 1.00 16.18 ? 31  LEU A CG  1 
ATOM   56   C CD1 . LEU A 1 14  ? 4.400   39.113 14.662 1.00 19.29 ? 31  LEU A CD1 1 
ATOM   57   C CD2 . LEU A 1 14  ? 3.397   37.232 13.390 1.00 19.88 ? 31  LEU A CD2 1 
ATOM   58   N N   . MET A 1 15  ? -0.588  36.380 15.867 1.00 14.28 ? 32  MET A N   1 
ATOM   59   C CA  . MET A 1 15  ? -1.482  35.741 16.829 1.00 13.55 ? 32  MET A CA  1 
ATOM   60   C C   . MET A 1 15  ? -0.935  34.378 17.204 1.00 13.12 ? 32  MET A C   1 
ATOM   61   O O   . MET A 1 15  ? -0.753  33.515 16.342 1.00 14.52 ? 32  MET A O   1 
ATOM   62   C CB  . MET A 1 15  ? -2.890  35.594 16.243 1.00 15.36 ? 32  MET A CB  1 
ATOM   63   C CG  . MET A 1 15  ? -3.903  34.987 17.215 1.00 15.67 ? 32  MET A CG  1 
ATOM   64   S SD  . MET A 1 15  ? -5.608  35.194 16.674 1.00 18.91 ? 32  MET A SD  1 
ATOM   65   C CE  . MET A 1 15  ? -5.535  34.524 15.013 1.00 21.05 ? 32  MET A CE  1 
ATOM   66   N N   . ILE A 1 16  ? -0.685  34.174 18.495 1.00 12.78 ? 33  ILE A N   1 
ATOM   67   C CA  . ILE A 1 16  ? -0.310  32.854 18.987 1.00 13.13 ? 33  ILE A CA  1 
ATOM   68   C C   . ILE A 1 16  ? -1.585  32.031 19.104 1.00 12.46 ? 33  ILE A C   1 
ATOM   69   O O   . ILE A 1 16  ? -2.550  32.450 19.763 1.00 13.89 ? 33  ILE A O   1 
ATOM   70   C CB  . ILE A 1 16  ? 0.455   32.932 20.319 1.00 14.38 ? 33  ILE A CB  1 
ATOM   71   C CG1 . ILE A 1 16  ? 1.685   33.829 20.164 1.00 14.94 ? 33  ILE A CG1 1 
ATOM   72   C CG2 . ILE A 1 16  ? 0.838   31.532 20.776 1.00 14.16 ? 33  ILE A CG2 1 
ATOM   73   C CD1 . ILE A 1 16  ? 2.490   34.003 21.468 1.00 16.10 ? 33  ILE A CD1 1 
ATOM   74   N N   . LYS A 1 17  ? -1.614  30.908 18.412 1.00 13.77 ? 34  LYS A N   1 
ATOM   75   C CA  . LYS A 1 17  ? -2.787  30.038 18.341 1.00 13.10 ? 34  LYS A CA  1 
ATOM   76   C C   . LYS A 1 17  ? -2.889  29.203 19.618 1.00 13.32 ? 34  LYS A C   1 
ATOM   77   O O   . LYS A 1 17  ? -1.984  29.199 20.472 1.00 13.35 ? 34  LYS A O   1 
ATOM   78   C CB  . LYS A 1 17  ? -2.668  29.157 17.098 1.00 14.43 ? 34  LYS A CB  1 
ATOM   79   C CG  . LYS A 1 17  ? -2.578  29.928 15.783 1.00 15.11 ? 34  LYS A CG  1 
ATOM   80   C CD  . LYS A 1 17  ? -2.443  29.015 14.588 1.00 14.03 ? 34  LYS A CD  1 
ATOM   81   C CE  . LYS A 1 17  ? -2.509  29.820 13.307 1.00 18.94 ? 34  LYS A CE  1 
ATOM   82   N NZ  . LYS A 1 17  ? -2.375  28.956 12.100 1.00 21.13 ? 34  LYS A NZ  1 
ATOM   83   N N   . PRO A 1 18  ? -4.010  28.507 19.819 1.00 14.00 ? 35  PRO A N   1 
ATOM   84   C CA  . PRO A 1 18  ? -4.177  27.788 21.097 1.00 15.20 ? 35  PRO A CA  1 
ATOM   85   C C   . PRO A 1 18  ? -3.075  26.793 21.386 1.00 13.19 ? 35  PRO A C   1 
ATOM   86   O O   . PRO A 1 18  ? -2.787  26.535 22.562 1.00 14.65 ? 35  PRO A O   1 
ATOM   87   C CB  . PRO A 1 18  ? -5.541  27.112 20.927 1.00 15.26 ? 35  PRO A CB  1 
ATOM   88   C CG  . PRO A 1 18  ? -6.294  28.052 20.018 1.00 14.80 ? 35  PRO A CG  1 
ATOM   89   C CD  . PRO A 1 18  ? -5.237  28.464 19.008 1.00 14.18 ? 35  PRO A CD  1 
ATOM   90   N N   . ASP A 1 19  ? -2.494  26.162 20.358 1.00 15.20 ? 36  ASP A N   1 
ATOM   91   C CA  . ASP A 1 19  ? -1.368  25.263 20.593 1.00 14.23 ? 36  ASP A CA  1 
ATOM   92   C C   . ASP A 1 19  ? -0.151  25.987 21.179 1.00 14.77 ? 36  ASP A C   1 
ATOM   93   O O   . ASP A 1 19  ? 0.575   25.415 22.004 1.00 14.84 ? 36  ASP A O   1 
ATOM   94   C CB  . ASP A 1 19  ? -1.012  24.450 19.332 1.00 16.00 ? 36  ASP A CB  1 
ATOM   95   C CG  . ASP A 1 19  ? -0.801  25.295 18.076 1.00 15.35 ? 36  ASP A CG  1 
ATOM   96   O OD1 . ASP A 1 19  ? -1.431  26.361 17.898 1.00 17.33 ? 36  ASP A OD1 1 
ATOM   97   O OD2 . ASP A 1 19  ? -0.003  24.847 17.233 1.00 14.64 ? 36  ASP A OD2 1 
ATOM   98   N N   . GLY A 1 20  ? 0.095   27.232 20.773 1.00 14.52 ? 37  GLY A N   1 
ATOM   99   C CA  . GLY A 1 20  ? 1.168   27.997 21.403 1.00 14.03 ? 37  GLY A CA  1 
ATOM   100  C C   . GLY A 1 20  ? 0.900   28.286 22.872 1.00 14.71 ? 37  GLY A C   1 
ATOM   101  O O   . GLY A 1 20  ? 1.817   28.276 23.694 1.00 15.30 ? 37  GLY A O   1 
ATOM   102  N N   . ILE A 1 21  ? -0.351  28.593 23.208 1.00 14.24 ? 38  ILE A N   1 
ATOM   103  C CA  . ILE A 1 21  ? -0.721  28.834 24.603 1.00 13.95 ? 38  ILE A CA  1 
ATOM   104  C C   . ILE A 1 21  ? -0.568  27.550 25.403 1.00 14.38 ? 38  ILE A C   1 
ATOM   105  O O   . ILE A 1 21  ? 0.067   27.522 26.462 1.00 14.39 ? 38  ILE A O   1 
ATOM   106  C CB  . ILE A 1 21  ? -2.175  29.352 24.687 1.00 14.26 ? 38  ILE A CB  1 
ATOM   107  C CG1 . ILE A 1 21  ? -2.414  30.603 23.816 1.00 15.95 ? 38  ILE A CG1 1 
ATOM   108  C CG2 . ILE A 1 21  ? -2.553  29.593 26.145 1.00 17.42 ? 38  ILE A CG2 1 
ATOM   109  C CD1 . ILE A 1 21  ? -1.532  31.790 24.127 1.00 19.35 ? 38  ILE A CD1 1 
ATOM   110  N N   . GLN A 1 22  ? -1.140  26.460 24.889 1.00 14.19 ? 39  GLN A N   1 
ATOM   111  C CA  . GLN A 1 22  ? -1.228  25.216 25.640 1.00 13.62 ? 39  GLN A CA  1 
ATOM   112  C C   . GLN A 1 22  ? 0.123   24.539 25.798 1.00 14.97 ? 39  GLN A C   1 
ATOM   113  O O   . GLN A 1 22  ? 0.361   23.864 26.810 1.00 15.75 ? 39  GLN A O   1 
ATOM   114  C CB  . GLN A 1 22  ? -2.222  24.295 24.937 1.00 15.49 ? 39  GLN A CB  1 
ATOM   115  C CG  . GLN A 1 22  ? -3.680  24.678 25.145 1.00 16.51 ? 39  GLN A CG  1 
ATOM   116  C CD  . GLN A 1 22  ? -4.142  24.350 26.538 1.00 17.72 ? 39  GLN A CD  1 
ATOM   117  O OE1 . GLN A 1 22  ? -3.350  23.879 27.370 1.00 19.60 ? 39  GLN A OE1 1 
ATOM   118  N NE2 . GLN A 1 22  ? -5.427  24.560 26.805 1.00 18.01 ? 39  GLN A NE2 1 
ATOM   119  N N   . ARG A 1 23  ? 1.005   24.662 24.800 1.00 14.55 ? 40  ARG A N   1 
ATOM   120  C CA  . ARG A 1 23  ? 2.364   24.131 24.892 1.00 14.05 ? 40  ARG A CA  1 
ATOM   121  C C   . ARG A 1 23  ? 3.274   25.040 25.699 1.00 15.41 ? 40  ARG A C   1 
ATOM   122  O O   . ARG A 1 23  ? 4.430   24.679 25.973 1.00 16.97 ? 40  ARG A O   1 
ATOM   123  C CB  . ARG A 1 23  ? 2.895   23.851 23.484 1.00 15.07 ? 40  ARG A CB  1 
ATOM   124  C CG  . ARG A 1 23  ? 2.077   22.774 22.793 1.00 14.78 ? 40  ARG A CG  1 
ATOM   125  C CD  . ARG A 1 23  ? 2.515   22.541 21.362 1.00 17.07 ? 40  ARG A CD  1 
ATOM   126  N NE  . ARG A 1 23  ? 3.835   21.940 21.320 1.00 16.93 ? 40  ARG A NE  1 
ATOM   127  C CZ  . ARG A 1 23  ? 4.646   21.967 20.274 1.00 15.77 ? 40  ARG A CZ  1 
ATOM   128  N NH1 . ARG A 1 23  ? 4.276   22.515 19.127 1.00 17.37 ? 40  ARG A NH1 1 
ATOM   129  N NH2 . ARG A 1 23  ? 5.878   21.481 20.399 1.00 18.15 ? 40  ARG A NH2 1 
ATOM   130  N N   . GLN A 1 24  ? 2.759   26.203 26.095 1.00 14.37 ? 41  GLN A N   1 
ATOM   131  C CA  . GLN A 1 24  ? 3.434   27.128 27.002 1.00 15.46 ? 41  GLN A CA  1 
ATOM   132  C C   . GLN A 1 24  ? 4.771   27.595 26.443 1.00 14.97 ? 41  GLN A C   1 
ATOM   133  O O   . GLN A 1 24  ? 5.807   27.573 27.116 1.00 15.76 ? 41  GLN A O   1 
ATOM   134  C CB  . GLN A 1 24  ? 3.548   26.542 28.416 1.00 16.15 ? 41  GLN A CB  1 
ATOM   135  C CG  . GLN A 1 24  ? 2.201   26.120 28.985 1.00 17.39 ? 41  GLN A CG  1 
ATOM   136  C CD  . GLN A 1 24  ? 2.095   26.422 30.461 1.00 16.72 ? 41  GLN A CD  1 
ATOM   137  O OE1 . GLN A 1 24  ? 2.362   25.572 31.299 1.00 17.50 ? 41  GLN A OE1 1 
ATOM   138  N NE2 . GLN A 1 24  ? 1.706   27.637 30.775 1.00 17.32 ? 41  GLN A NE2 1 
ATOM   139  N N   . VAL A 1 25  ? 4.719   28.073 25.197 1.00 14.45 ? 42  VAL A N   1 
ATOM   140  C CA  . VAL A 1 25  ? 5.861   28.641 24.497 1.00 14.37 ? 42  VAL A CA  1 
ATOM   141  C C   . VAL A 1 25  ? 5.633   30.116 24.135 1.00 12.20 ? 42  VAL A C   1 
ATOM   142  O O   . VAL A 1 25  ? 6.316   30.673 23.273 1.00 14.60 ? 42  VAL A O   1 
ATOM   143  C CB  . VAL A 1 25  ? 6.255   27.785 23.278 1.00 14.99 ? 42  VAL A CB  1 
ATOM   144  C CG1 . VAL A 1 25  ? 6.708   26.397 23.733 1.00 16.67 ? 42  VAL A CG1 1 
ATOM   145  C CG2 . VAL A 1 25  ? 5.082   27.674 22.296 1.00 15.55 ? 42  VAL A CG2 1 
ATOM   146  N N   . VAL A 1 26  ? 4.690   30.773 24.808 1.00 13.22 ? 43  VAL A N   1 
ATOM   147  C CA  . VAL A 1 26  ? 4.386   32.165 24.490 1.00 13.55 ? 43  VAL A CA  1 
ATOM   148  C C   . VAL A 1 26  ? 5.628   33.029 24.637 1.00 13.31 ? 43  VAL A C   1 
ATOM   149  O O   . VAL A 1 26  ? 5.938   33.866 23.779 1.00 13.32 ? 43  VAL A O   1 
ATOM   150  C CB  . VAL A 1 26  ? 3.247   32.670 25.399 1.00 13.43 ? 43  VAL A CB  1 
ATOM   151  C CG1 . VAL A 1 26  ? 3.074   34.183 25.309 1.00 14.44 ? 43  VAL A CG1 1 
ATOM   152  C CG2 . VAL A 1 26  ? 1.979   31.925 25.091 1.00 14.66 ? 43  VAL A CG2 1 
ATOM   153  N N   . GLY A 1 27  ? 6.301   32.918 25.779 1.00 12.52 ? 44  GLY A N   1 
ATOM   154  C CA  . GLY A 1 27  ? 7.471   33.742 25.995 1.00 13.29 ? 44  GLY A CA  1 
ATOM   155  C C   . GLY A 1 27  ? 8.546   33.522 24.952 1.00 12.84 ? 44  GLY A C   1 
ATOM   156  O O   . GLY A 1 27  ? 9.182   34.476 24.494 1.00 13.07 ? 44  GLY A O   1 
ATOM   157  N N   . GLU A 1 28  ? 8.786   32.263 24.577 1.00 13.31 ? 45  GLU A N   1 
ATOM   158  C CA  . GLU A 1 28  ? 9.804   31.985 23.574 1.00 13.25 ? 45  GLU A CA  1 
ATOM   159  C C   . GLU A 1 28  ? 9.446   32.640 22.245 1.00 12.26 ? 45  GLU A C   1 
ATOM   160  O O   . GLU A 1 28  ? 10.333  33.123 21.523 1.00 13.71 ? 45  GLU A O   1 
ATOM   161  C CB  . GLU A 1 28  ? 9.951   30.486 23.347 1.00 14.42 ? 45  GLU A CB  1 
ATOM   162  C CG  . GLU A 1 28  ? 10.586  29.708 24.436 1.00 17.14 ? 45  GLU A CG  1 
ATOM   163  C CD  . GLU A 1 28  ? 10.898  28.302 23.931 1.00 26.33 ? 45  GLU A CD  1 
ATOM   164  O OE1 . GLU A 1 28  ? 11.775  28.156 23.050 1.00 30.21 ? 45  GLU A OE1 1 
ATOM   165  O OE2 . GLU A 1 28  ? 10.214  27.360 24.356 1.00 31.02 ? 45  GLU A OE2 1 
ATOM   166  N N   . ILE A 1 29  ? 8.161   32.605 21.874 1.00 12.55 ? 46  ILE A N   1 
ATOM   167  C CA  . ILE A 1 29  ? 7.734   33.237 20.629 1.00 13.20 ? 46  ILE A CA  1 
ATOM   168  C C   . ILE A 1 29  ? 7.977   34.734 20.691 1.00 13.87 ? 46  ILE A C   1 
ATOM   169  O O   . ILE A 1 29  ? 8.544   35.332 19.769 1.00 14.66 ? 46  ILE A O   1 
ATOM   170  C CB  . ILE A 1 29  ? 6.253   32.927 20.357 1.00 12.74 ? 46  ILE A CB  1 
ATOM   171  C CG1 . ILE A 1 29  ? 6.076   31.435 20.051 1.00 14.83 ? 46  ILE A CG1 1 
ATOM   172  C CG2 . ILE A 1 29  ? 5.705   33.818 19.223 1.00 15.25 ? 46  ILE A CG2 1 
ATOM   173  C CD1 . ILE A 1 29  ? 4.618   30.968 20.028 1.00 14.75 ? 46  ILE A CD1 1 
ATOM   174  N N   . ILE A 1 30  ? 7.534   35.371 21.777 1.00 13.85 ? 47  ILE A N   1 
ATOM   175  C CA  . ILE A 1 30  ? 7.714   36.816 21.896 1.00 13.15 ? 47  ILE A CA  1 
ATOM   176  C C   . ILE A 1 30  ? 9.194   37.170 21.843 1.00 13.03 ? 47  ILE A C   1 
ATOM   177  O O   . ILE A 1 30  ? 9.591   38.145 21.193 1.00 13.80 ? 47  ILE A O   1 
ATOM   178  C CB  . ILE A 1 30  ? 7.036   37.324 23.184 1.00 12.24 ? 47  ILE A CB  1 
ATOM   179  C CG1 . ILE A 1 30  ? 5.514   37.230 23.054 1.00 13.37 ? 47  ILE A CG1 1 
ATOM   180  C CG2 . ILE A 1 30  ? 7.467   38.741 23.516 1.00 13.74 ? 47  ILE A CG2 1 
ATOM   181  C CD1 . ILE A 1 30  ? 4.812   37.400 24.397 1.00 12.89 ? 47  ILE A CD1 1 
ATOM   182  N N   . SER A 1 31  ? 10.033  36.375 22.511 1.00 13.41 ? 48  SER A N   1 
ATOM   183  C CA  . SER A 1 31  ? 11.465  36.645 22.526 1.00 13.50 ? 48  SER A CA  1 
ATOM   184  C C   . SER A 1 31  ? 12.058  36.664 21.119 1.00 13.51 ? 48  SER A C   1 
ATOM   185  O O   . SER A 1 31  ? 12.981  37.436 20.844 1.00 14.10 ? 48  SER A O   1 
ATOM   186  C CB  . SER A 1 31  ? 12.206  35.629 23.401 1.00 12.65 ? 48  SER A CB  1 
ATOM   187  O OG  . SER A 1 31  ? 11.988  35.896 24.779 1.00 13.86 ? 48  SER A OG  1 
ATOM   188  N N   . ARG A 1 32  ? 11.561  35.816 20.214 1.00 14.03 ? 49  ARG A N   1 
ATOM   189  C CA  . ARG A 1 32  ? 12.135  35.792 18.874 1.00 14.47 ? 49  ARG A CA  1 
ATOM   190  C C   . ARG A 1 32  ? 11.922  37.112 18.144 1.00 12.29 ? 49  ARG A C   1 
ATOM   191  O O   . ARG A 1 32  ? 12.799  37.568 17.393 1.00 14.59 ? 49  ARG A O   1 
ATOM   192  C CB  . ARG A 1 32  ? 11.535  34.661 18.067 1.00 16.09 ? 49  ARG A CB  1 
ATOM   193  C CG  . ARG A 1 32  ? 11.997  33.329 18.518 1.00 17.38 ? 49  ARG A CG  1 
ATOM   194  C CD  . ARG A 1 32  ? 11.655  32.314 17.492 1.00 23.50 ? 49  ARG A CD  1 
ATOM   195  N NE  . ARG A 1 32  ? 12.121  31.008 17.911 1.00 23.33 ? 49  ARG A NE  1 
ATOM   196  C CZ  . ARG A 1 32  ? 12.535  30.070 17.078 1.00 19.82 ? 49  ARG A CZ  1 
ATOM   197  N NH1 . ARG A 1 32  ? 12.543  30.262 15.770 1.00 20.34 ? 49  ARG A NH1 1 
ATOM   198  N NH2 . ARG A 1 32  ? 12.942  28.910 17.570 1.00 21.33 ? 49  ARG A NH2 1 
ATOM   199  N N   . PHE A 1 33  ? 10.760  37.741 18.348 1.00 13.77 ? 50  PHE A N   1 
ATOM   200  C CA  . PHE A 1 33  ? 10.474  39.019 17.713 1.00 13.72 ? 50  PHE A CA  1 
ATOM   201  C C   . PHE A 1 33  ? 11.194  40.160 18.417 1.00 14.06 ? 50  PHE A C   1 
ATOM   202  O O   . PHE A 1 33  ? 11.755  41.048 17.759 1.00 14.51 ? 50  PHE A O   1 
ATOM   203  C CB  . PHE A 1 33  ? 8.967   39.229 17.610 1.00 13.35 ? 50  PHE A CB  1 
ATOM   204  C CG  . PHE A 1 33  ? 8.296   38.213 16.738 1.00 14.42 ? 50  PHE A CG  1 
ATOM   205  C CD1 . PHE A 1 33  ? 8.520   38.217 15.382 1.00 16.65 ? 50  PHE A CD1 1 
ATOM   206  C CD2 . PHE A 1 33  ? 7.501   37.221 17.261 1.00 16.19 ? 50  PHE A CD2 1 
ATOM   207  C CE1 . PHE A 1 33  ? 7.944   37.272 14.567 1.00 17.82 ? 50  PHE A CE1 1 
ATOM   208  C CE2 . PHE A 1 33  ? 6.911   36.266 16.434 1.00 16.51 ? 50  PHE A CE2 1 
ATOM   209  C CZ  . PHE A 1 33  ? 7.141   36.309 15.085 1.00 15.44 ? 50  PHE A CZ  1 
ATOM   210  N N   . GLU A 1 34  ? 11.226  40.134 19.754 1.00 13.57 ? 51  GLU A N   1 
ATOM   211  C CA  . GLU A 1 34  ? 11.978  41.144 20.486 1.00 13.39 ? 51  GLU A CA  1 
ATOM   212  C C   . GLU A 1 34  ? 13.453  41.138 20.109 1.00 14.36 ? 51  GLU A C   1 
ATOM   213  O O   . GLU A 1 34  ? 14.105  42.191 20.132 1.00 14.43 ? 51  GLU A O   1 
ATOM   214  C CB  . GLU A 1 34  ? 11.884  40.899 21.995 1.00 14.87 ? 51  GLU A CB  1 
ATOM   215  C CG  . GLU A 1 34  ? 10.562  41.313 22.653 1.00 13.09 ? 51  GLU A CG  1 
ATOM   216  C CD  . GLU A 1 34  ? 10.605  41.082 24.131 1.00 14.44 ? 51  GLU A CD  1 
ATOM   217  O OE1 . GLU A 1 34  ? 10.759  39.904 24.515 1.00 14.98 ? 51  GLU A OE1 1 
ATOM   218  O OE2 . GLU A 1 34  ? 10.496  42.068 24.885 1.00 15.12 ? 51  GLU A OE2 1 
ATOM   219  N N   . LYS A 1 35  ? 13.988  39.964 19.761 1.00 14.16 ? 52  LYS A N   1 
ATOM   220  C CA  . LYS A 1 35  ? 15.414  39.836 19.511 1.00 13.75 ? 52  LYS A CA  1 
ATOM   221  C C   . LYS A 1 35  ? 15.868  40.655 18.312 1.00 12.43 ? 52  LYS A C   1 
ATOM   222  O O   . LYS A 1 35  ? 17.034  41.039 18.237 1.00 13.56 ? 52  LYS A O   1 
ATOM   223  C CB  . LYS A 1 35  ? 15.748  38.360 19.289 1.00 15.22 ? 52  LYS A CB  1 
ATOM   224  C CG  . LYS A 1 35  ? 17.224  38.035 19.320 1.00 19.51 ? 52  LYS A CG  1 
ATOM   225  C CD  . LYS A 1 35  ? 17.408  36.547 19.100 1.00 25.21 ? 52  LYS A CD  1 
ATOM   226  C CE  . LYS A 1 35  ? 18.674  36.028 19.714 1.00 27.65 ? 52  LYS A CE  1 
ATOM   227  N NZ  . LYS A 1 35  ? 18.587  36.106 21.204 1.00 30.69 ? 52  LYS A NZ  1 
ATOM   228  N N   . ARG A 1 36  ? 14.972  40.935 17.376 1.00 14.10 ? 53  ARG A N   1 
ATOM   229  C CA  . ARG A 1 36  ? 15.292  41.765 16.217 1.00 14.49 ? 53  ARG A CA  1 
ATOM   230  C C   . ARG A 1 36  ? 15.033  43.246 16.468 1.00 14.40 ? 53  ARG A C   1 
ATOM   231  O O   . ARG A 1 36  ? 15.175  44.055 15.555 1.00 14.52 ? 53  ARG A O   1 
ATOM   232  C CB  . ARG A 1 36  ? 14.511  41.290 14.986 1.00 14.33 ? 53  ARG A CB  1 
ATOM   233  C CG  . ARG A 1 36  ? 14.900  39.893 14.536 1.00 14.63 ? 53  ARG A CG  1 
ATOM   234  C CD  . ARG A 1 36  ? 14.279  39.497 13.225 1.00 15.48 ? 53  ARG A CD  1 
ATOM   235  N NE  . ARG A 1 36  ? 14.851  40.231 12.108 1.00 13.49 ? 53  ARG A NE  1 
ATOM   236  C CZ  . ARG A 1 36  ? 14.535  39.991 10.845 1.00 15.44 ? 53  ARG A CZ  1 
ATOM   237  N NH1 . ARG A 1 36  ? 13.611  39.105 10.521 1.00 15.91 ? 53  ARG A NH1 1 
ATOM   238  N NH2 . ARG A 1 36  ? 15.173  40.648 9.889  1.00 16.32 ? 53  ARG A NH2 1 
ATOM   239  N N   . GLY A 1 37  ? 14.662  43.622 17.682 1.00 13.97 ? 54  GLY A N   1 
ATOM   240  C CA  . GLY A 1 37  ? 14.310  44.995 17.935 1.00 14.61 ? 54  GLY A CA  1 
ATOM   241  C C   . GLY A 1 37  ? 12.952  45.374 17.418 1.00 14.04 ? 54  GLY A C   1 
ATOM   242  O O   . GLY A 1 37  ? 12.685  46.565 17.224 1.00 16.39 ? 54  GLY A O   1 
ATOM   243  N N   . TYR A 1 38  ? 12.085  44.394 17.183 1.00 13.17 ? 55  TYR A N   1 
ATOM   244  C CA  . TYR A 1 38  ? 10.701  44.695 16.875 1.00 12.23 ? 55  TYR A CA  1 
ATOM   245  C C   . TYR A 1 38  ? 10.006  45.143 18.151 1.00 14.17 ? 55  TYR A C   1 
ATOM   246  O O   . TYR A 1 38  ? 10.248  44.604 19.231 1.00 14.54 ? 55  TYR A O   1 
ATOM   247  C CB  . TYR A 1 38  ? 9.999   43.474 16.282 1.00 14.44 ? 55  TYR A CB  1 
ATOM   248  C CG  . TYR A 1 38  ? 10.514  43.026 14.921 1.00 13.79 ? 55  TYR A CG  1 
ATOM   249  C CD1 . TYR A 1 38  ? 11.049  43.928 14.023 1.00 14.99 ? 55  TYR A CD1 1 
ATOM   250  C CD2 . TYR A 1 38  ? 10.414  41.699 14.521 1.00 13.69 ? 55  TYR A CD2 1 
ATOM   251  C CE1 . TYR A 1 38  ? 11.494  43.509 12.775 1.00 14.50 ? 55  TYR A CE1 1 
ATOM   252  C CE2 . TYR A 1 38  ? 10.852  41.276 13.283 1.00 12.81 ? 55  TYR A CE2 1 
ATOM   253  C CZ  . TYR A 1 38  ? 11.386  42.189 12.418 1.00 14.24 ? 55  TYR A CZ  1 
ATOM   254  O OH  . TYR A 1 38  ? 11.807  41.750 11.186 1.00 16.16 ? 55  TYR A OH  1 
ATOM   255  N N   . ARG A 1 39  ? 9.149   46.148 18.022 1.00 13.91 ? 56  ARG A N   1 
ATOM   256  C CA  . ARG A 1 39  ? 8.475   46.776 19.153 1.00 13.85 ? 56  ARG A CA  1 
ATOM   257  C C   . ARG A 1 39  ? 7.076   46.206 19.335 1.00 14.09 ? 56  ARG A C   1 
ATOM   258  O O   . ARG A 1 39  ? 6.315   46.118 18.371 1.00 13.90 ? 56  ARG A O   1 
ATOM   259  C CB  . ARG A 1 39  ? 8.378   48.273 18.880 1.00 14.10 ? 56  ARG A CB  1 
ATOM   260  C CG  . ARG A 1 39  ? 7.832   49.062 20.059 1.00 14.34 ? 56  ARG A CG  1 
ATOM   261  C CD  . ARG A 1 39  ? 7.799   50.574 19.772 1.00 13.82 ? 56  ARG A CD  1 
ATOM   262  N NE  . ARG A 1 39  ? 6.823   50.926 18.739 1.00 15.06 ? 56  ARG A NE  1 
ATOM   263  C CZ  . ARG A 1 39  ? 5.541   51.164 18.987 1.00 15.45 ? 56  ARG A CZ  1 
ATOM   264  N NH1 . ARG A 1 39  ? 5.039   51.037 20.205 1.00 17.44 ? 56  ARG A NH1 1 
ATOM   265  N NH2 . ARG A 1 39  ? 4.741   51.561 17.997 1.00 18.31 ? 56  ARG A NH2 1 
ATOM   266  N N   . ILE A 1 40  ? 6.737   45.852 20.573 1.00 13.27 ? 57  ILE A N   1 
ATOM   267  C CA  . ILE A 1 40  ? 5.385   45.422 20.908 1.00 12.35 ? 57  ILE A CA  1 
ATOM   268  C C   . ILE A 1 40  ? 4.505   46.673 20.929 1.00 14.17 ? 57  ILE A C   1 
ATOM   269  O O   . ILE A 1 40  ? 4.643   47.527 21.808 1.00 14.78 ? 57  ILE A O   1 
ATOM   270  C CB  . ILE A 1 40  ? 5.329   44.692 22.253 1.00 12.99 ? 57  ILE A CB  1 
ATOM   271  C CG1 . ILE A 1 40  ? 6.327   43.533 22.334 1.00 15.31 ? 57  ILE A CG1 1 
ATOM   272  C CG2 . ILE A 1 40  ? 3.934   44.181 22.471 1.00 14.71 ? 57  ILE A CG2 1 
ATOM   273  C CD1 . ILE A 1 40  ? 6.474   42.988 23.744 1.00 15.26 ? 57  ILE A CD1 1 
ATOM   274  N N   . ALA A 1 41  ? 3.619   46.799 19.948 1.00 14.21 ? 58  ALA A N   1 
ATOM   275  C CA  . ALA A 1 41  ? 2.664   47.906 19.888 1.00 14.00 ? 58  ALA A CA  1 
ATOM   276  C C   . ALA A 1 41  ? 1.309   47.540 20.484 1.00 14.77 ? 58  ALA A C   1 
ATOM   277  O O   . ALA A 1 41  ? 0.566   48.438 20.881 1.00 15.02 ? 58  ALA A O   1 
ATOM   278  C CB  . ALA A 1 41  ? 2.495   48.369 18.438 1.00 14.73 ? 58  ALA A CB  1 
ATOM   279  N N   . ALA A 1 42  ? 0.974   46.256 20.569 1.00 13.46 ? 59  ALA A N   1 
ATOM   280  C CA  . ALA A 1 42  ? -0.279  45.838 21.187 1.00 13.70 ? 59  ALA A CA  1 
ATOM   281  C C   . ALA A 1 42  ? -0.155  44.372 21.575 1.00 14.45 ? 59  ALA A C   1 
ATOM   282  O O   . ALA A 1 42  ? 0.566   43.611 20.934 1.00 13.80 ? 59  ALA A O   1 
ATOM   283  C CB  . ALA A 1 42  ? -1.466  46.062 20.242 1.00 14.99 ? 59  ALA A CB  1 
ATOM   284  N N   . MET A 1 43  ? -0.877  43.979 22.622 1.00 14.96 ? 60  MET A N   1 
ATOM   285  C CA  . MET A 1 43  ? -0.848  42.595 23.069 1.00 14.52 ? 60  MET A CA  1 
ATOM   286  C C   . MET A 1 43  ? -2.060  42.365 23.949 1.00 15.92 ? 60  MET A C   1 
ATOM   287  O O   . MET A 1 43  ? -2.345  43.194 24.820 1.00 16.10 ? 60  MET A O   1 
ATOM   288  C CB  . MET A 1 43  ? 0.450   42.334 23.844 1.00 15.10 ? 60  MET A CB  1 
ATOM   289  C CG  . MET A 1 43  ? 0.697   40.878 24.239 1.00 17.44 ? 60  MET A CG  1 
ATOM   290  S SD  . MET A 1 43  ? 2.416   40.584 24.743 1.00 17.83 ? 60  MET A SD  1 
ATOM   291  C CE  . MET A 1 43  ? 3.190   40.359 23.153 1.00 18.91 ? 60  MET A CE  1 
ATOM   292  N N   . LYS A 1 44  ? -2.776  41.263 23.706 1.00 13.87 ? 61  LYS A N   1 
ATOM   293  C CA  . LYS A 1 44  ? -4.011  40.960 24.417 1.00 16.13 ? 61  LYS A CA  1 
ATOM   294  C C   . LYS A 1 44  ? -4.251  39.468 24.398 1.00 15.42 ? 61  LYS A C   1 
ATOM   295  O O   . LYS A 1 44  ? -4.273  38.862 23.323 1.00 16.55 ? 61  LYS A O   1 
ATOM   296  C CB  . LYS A 1 44  ? -5.183  41.625 23.677 1.00 18.08 ? 61  LYS A CB  1 
ATOM   297  C CG  . LYS A 1 44  ? -6.556  41.241 24.172 1.00 23.43 ? 61  LYS A CG  1 
ATOM   298  C CD  . LYS A 1 44  ? -7.611  42.253 23.707 1.00 24.42 ? 61  LYS A CD  1 
ATOM   299  C CE  . LYS A 1 44  ? -7.712  42.338 22.204 1.00 22.32 ? 61  LYS A CE  1 
ATOM   300  N NZ  . LYS A 1 44  ? -8.703  43.393 21.805 1.00 20.44 ? 61  LYS A NZ  1 
ATOM   301  N N   . LEU A 1 45  ? -4.446  38.871 25.570 1.00 14.54 ? 62  LEU A N   1 
ATOM   302  C CA  . LEU A 1 45  ? -4.941  37.502 25.638 1.00 14.95 ? 62  LEU A CA  1 
ATOM   303  C C   . LEU A 1 45  ? -6.461  37.508 25.582 1.00 14.27 ? 62  LEU A C   1 
ATOM   304  O O   . LEU A 1 45  ? -7.118  38.235 26.331 1.00 16.04 ? 62  LEU A O   1 
ATOM   305  C CB  . LEU A 1 45  ? -4.509  36.809 26.926 1.00 14.31 ? 62  LEU A CB  1 
ATOM   306  C CG  . LEU A 1 45  ? -4.878  35.325 27.013 1.00 16.50 ? 62  LEU A CG  1 
ATOM   307  C CD1 . LEU A 1 45  ? -3.843  34.483 26.302 1.00 15.78 ? 62  LEU A CD1 1 
ATOM   308  C CD2 . LEU A 1 45  ? -5.041  34.869 28.446 1.00 16.56 ? 62  LEU A CD2 1 
ATOM   309  N N   . THR A 1 46  ? -7.018  36.700 24.691 1.00 14.66 ? 63  THR A N   1 
ATOM   310  C CA  . THR A 1 46  ? -8.459  36.524 24.623 1.00 14.69 ? 63  THR A CA  1 
ATOM   311  C C   . THR A 1 46  ? -8.739  35.065 24.310 1.00 16.05 ? 63  THR A C   1 
ATOM   312  O O   . THR A 1 46  ? -7.823  34.251 24.161 1.00 16.78 ? 63  THR A O   1 
ATOM   313  C CB  . THR A 1 46  ? -9.096  37.497 23.617 1.00 17.09 ? 63  THR A CB  1 
ATOM   314  O OG1 . THR A 1 46  ? -10.521 37.489 23.794 1.00 18.59 ? 63  THR A OG1 1 
ATOM   315  C CG2 . THR A 1 46  ? -8.755  37.145 22.171 1.00 17.09 ? 63  THR A CG2 1 
ATOM   316  N N   . ILE A 1 47  ? -10.020 34.715 24.243 1.00 15.52 ? 64  ILE A N   1 
ATOM   317  C CA  . ILE A 1 47  ? -10.431 33.414 23.737 1.00 17.11 ? 64  ILE A CA  1 
ATOM   318  C C   . ILE A 1 47  ? -11.152 33.654 22.425 1.00 15.65 ? 64  ILE A C   1 
ATOM   319  O O   . ILE A 1 47  ? -12.168 34.353 22.388 1.00 18.82 ? 64  ILE A O   1 
ATOM   320  C CB  . ILE A 1 47  ? -11.289 32.644 24.750 1.00 17.30 ? 64  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 47  ? -10.382 32.162 25.901 1.00 18.23 ? 64  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 47  ? -11.962 31.463 24.061 1.00 20.00 ? 64  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 47  ? -11.132 31.774 27.149 1.00 21.06 ? 64  ILE A CD1 1 
ATOM   324  N N   . ALA A 1 48  ? -10.603 33.091 21.348 1.00 16.09 ? 65  ALA A N   1 
ATOM   325  C CA  . ALA A 1 48  ? -11.174 33.281 20.022 1.00 16.35 ? 65  ALA A CA  1 
ATOM   326  C C   . ALA A 1 48  ? -12.459 32.483 19.926 1.00 17.15 ? 65  ALA A C   1 
ATOM   327  O O   . ALA A 1 48  ? -12.531 31.348 20.392 1.00 20.48 ? 65  ALA A O   1 
ATOM   328  C CB  . ALA A 1 48  ? -10.172 32.799 18.978 1.00 16.73 ? 65  ALA A CB  1 
ATOM   329  N N   . THR A 1 49  ? -13.489 33.097 19.356 1.00 16.57 ? 66  THR A N   1 
ATOM   330  C CA  . THR A 1 49  ? -14.798 32.485 19.215 1.00 17.27 ? 66  THR A CA  1 
ATOM   331  C C   . THR A 1 49  ? -15.119 32.323 17.734 1.00 18.32 ? 66  THR A C   1 
ATOM   332  O O   . THR A 1 49  ? -14.520 32.992 16.880 1.00 18.50 ? 66  THR A O   1 
ATOM   333  C CB  . THR A 1 49  ? -15.879 33.375 19.837 1.00 18.08 ? 66  THR A CB  1 
ATOM   334  O OG1 . THR A 1 49  ? -15.950 34.598 19.095 1.00 19.94 ? 66  THR A OG1 1 
ATOM   335  C CG2 . THR A 1 49  ? -15.553 33.694 21.277 1.00 19.90 ? 66  THR A CG2 1 
ATOM   336  N N   . PRO A 1 50  ? -16.074 31.449 17.393 1.00 17.29 ? 67  PRO A N   1 
ATOM   337  C CA  . PRO A 1 50  ? -16.390 31.256 15.971 1.00 19.02 ? 67  PRO A CA  1 
ATOM   338  C C   . PRO A 1 50  ? -16.749 32.537 15.244 1.00 17.90 ? 67  PRO A C   1 
ATOM   339  O O   . PRO A 1 50  ? -16.336 32.708 14.092 1.00 19.39 ? 67  PRO A O   1 
ATOM   340  C CB  . PRO A 1 50  ? -17.533 30.232 16.005 1.00 20.87 ? 67  PRO A CB  1 
ATOM   341  C CG  . PRO A 1 50  ? -17.263 29.440 17.269 1.00 21.39 ? 67  PRO A CG  1 
ATOM   342  C CD  . PRO A 1 50  ? -16.746 30.458 18.255 1.00 19.81 ? 67  PRO A CD  1 
ATOM   343  N N   . ALA A 1 51  ? -17.480 33.462 15.870 1.00 17.42 ? 68  ALA A N   1 
ATOM   344  C CA  . ALA A 1 51  ? -17.898 34.658 15.141 1.00 18.67 ? 68  ALA A CA  1 
ATOM   345  C C   . ALA A 1 51  ? -16.712 35.537 14.751 1.00 18.51 ? 68  ALA A C   1 
ATOM   346  O O   . ALA A 1 51  ? -16.663 36.061 13.633 1.00 20.36 ? 68  ALA A O   1 
ATOM   347  C CB  . ALA A 1 51  ? -18.931 35.444 15.942 1.00 21.73 ? 68  ALA A CB  1 
ATOM   348  N N   . ILE A 1 52  ? -15.760 35.747 15.657 1.00 16.90 ? 69  ILE A N   1 
ATOM   349  C CA  A ILE A 1 52  ? -14.606 36.558 15.289 0.50 17.72 ? 69  ILE A CA  1 
ATOM   350  C CA  B ILE A 1 52  ? -14.584 36.545 15.322 0.50 17.65 ? 69  ILE A CA  1 
ATOM   351  C C   . ILE A 1 52  ? -13.717 35.804 14.310 1.00 18.21 ? 69  ILE A C   1 
ATOM   352  O O   . ILE A 1 52  ? -13.144 36.406 13.404 1.00 17.46 ? 69  ILE A O   1 
ATOM   353  C CB  A ILE A 1 52  ? -13.833 37.070 16.519 0.50 22.07 ? 69  ILE A CB  1 
ATOM   354  C CB  B ILE A 1 52  ? -13.805 36.891 16.606 0.50 21.46 ? 69  ILE A CB  1 
ATOM   355  C CG1 A ILE A 1 52  ? -12.789 38.107 16.078 0.50 25.79 ? 69  ILE A CG1 1 
ATOM   356  C CG1 B ILE A 1 52  ? -14.733 37.543 17.645 0.50 22.62 ? 69  ILE A CG1 1 
ATOM   357  C CG2 A ILE A 1 52  ? -13.158 35.934 17.256 0.50 21.73 ? 69  ILE A CG2 1 
ATOM   358  C CG2 B ILE A 1 52  ? -12.656 37.835 16.288 0.50 25.44 ? 69  ILE A CG2 1 
ATOM   359  C CD1 A ILE A 1 52  ? -12.539 39.216 17.090 0.50 27.72 ? 69  ILE A CD1 1 
ATOM   360  C CD1 B ILE A 1 52  ? -14.146 37.662 19.055 0.50 25.33 ? 69  ILE A CD1 1 
ATOM   361  N N   . LEU A 1 53  ? -13.593 34.484 14.475 1.00 16.44 ? 70  LEU A N   1 
ATOM   362  C CA  . LEU A 1 53  ? -12.749 33.704 13.567 1.00 16.23 ? 70  LEU A CA  1 
ATOM   363  C C   . LEU A 1 53  ? -13.321 33.677 12.155 1.00 18.06 ? 70  LEU A C   1 
ATOM   364  O O   . LEU A 1 53  ? -12.557 33.633 11.198 1.00 18.55 ? 70  LEU A O   1 
ATOM   365  C CB  . LEU A 1 53  ? -12.519 32.294 14.108 1.00 16.73 ? 70  LEU A CB  1 
ATOM   366  C CG  . LEU A 1 53  ? -11.688 32.235 15.388 1.00 16.63 ? 70  LEU A CG  1 
ATOM   367  C CD1 . LEU A 1 53  ? -11.888 30.858 16.010 1.00 17.66 ? 70  LEU A CD1 1 
ATOM   368  C CD2 . LEU A 1 53  ? -10.230 32.538 15.101 1.00 18.92 ? 70  LEU A CD2 1 
ATOM   369  N N   . GLU A 1 54  ? -14.648 33.708 12.005 1.00 18.62 ? 71  GLU A N   1 
ATOM   370  C CA  A GLU A 1 54  ? -15.231 33.787 10.669 0.33 20.45 ? 71  GLU A CA  1 
ATOM   371  C CA  B GLU A 1 54  ? -15.242 33.792 10.672 0.67 20.07 ? 71  GLU A CA  1 
ATOM   372  C C   . GLU A 1 54  ? -14.786 35.057 9.954  1.00 19.78 ? 71  GLU A C   1 
ATOM   373  O O   . GLU A 1 54  ? -14.494 35.032 8.750  1.00 22.00 ? 71  GLU A O   1 
ATOM   374  C CB  A GLU A 1 54  ? -16.755 33.711 10.764 0.33 24.89 ? 71  GLU A CB  1 
ATOM   375  C CB  B GLU A 1 54  ? -16.770 33.757 10.774 0.67 26.04 ? 71  GLU A CB  1 
ATOM   376  C CG  A GLU A 1 54  ? -17.274 32.296 10.938 0.33 27.46 ? 71  GLU A CG  1 
ATOM   377  C CG  B GLU A 1 54  ? -17.464 33.809 9.409  0.67 28.37 ? 71  GLU A CG  1 
ATOM   378  C CD  A GLU A 1 54  ? -18.772 32.236 11.123 0.33 30.29 ? 71  GLU A CD  1 
ATOM   379  C CD  B GLU A 1 54  ? -18.972 33.919 9.506  0.67 36.46 ? 71  GLU A CD  1 
ATOM   380  O OE1 A GLU A 1 54  ? -19.487 32.947 10.385 0.33 32.46 ? 71  GLU A OE1 1 
ATOM   381  O OE1 B GLU A 1 54  ? -19.509 33.730 10.612 0.67 40.06 ? 71  GLU A OE1 1 
ATOM   382  O OE2 A GLU A 1 54  ? -19.230 31.477 12.007 0.33 30.89 ? 71  GLU A OE2 1 
ATOM   383  O OE2 B GLU A 1 54  ? -19.615 34.207 8.474  0.67 40.20 ? 71  GLU A OE2 1 
ATOM   384  N N   . GLU A 1 55  ? -14.737 36.180 10.669 1.00 18.51 ? 72  GLU A N   1 
ATOM   385  C CA  . GLU A 1 55  ? -14.231 37.414 10.077 1.00 20.41 ? 72  GLU A CA  1 
ATOM   386  C C   . GLU A 1 55  ? -12.731 37.333 9.819  1.00 20.08 ? 72  GLU A C   1 
ATOM   387  O O   . GLU A 1 55  ? -12.246 37.762 8.767  1.00 21.93 ? 72  GLU A O   1 
ATOM   388  C CB  . GLU A 1 55  ? -14.499 38.568 11.036 1.00 25.96 ? 72  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 55  ? -15.914 38.774 11.405 1.00 37.06 ? 72  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 55  ? -16.408 40.034 10.795 1.00 49.53 ? 72  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 55  ? -16.661 40.003 9.575  1.00 52.98 ? 72  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 55  ? -16.476 41.051 11.524 1.00 54.93 ? 72  GLU A OE2 1 
ATOM   393  N N   . HIS A 1 56  ? -11.972 36.798 10.777 1.00 19.56 ? 73  HIS A N   1 
ATOM   394  C CA  . HIS A 1 56  ? -10.531 36.673 10.590 1.00 18.67 ? 73  HIS A CA  1 
ATOM   395  C C   . HIS A 1 56  ? -10.221 35.884 9.324  1.00 18.64 ? 73  HIS A C   1 
ATOM   396  O O   . HIS A 1 56  ? -9.346  36.270 8.533  1.00 20.57 ? 73  HIS A O   1 
ATOM   397  C CB  . HIS A 1 56  ? -9.965  35.968 11.816 1.00 18.31 ? 73  HIS A CB  1 
ATOM   398  C CG  . HIS A 1 56  ? -8.502  35.709 11.745 1.00 16.68 ? 73  HIS A CG  1 
ATOM   399  N ND1 . HIS A 1 56  ? -7.567  36.707 11.910 1.00 19.54 ? 73  HIS A ND1 1 
ATOM   400  C CD2 . HIS A 1 56  ? -7.803  34.565 11.543 1.00 21.49 ? 73  HIS A CD2 1 
ATOM   401  C CE1 . HIS A 1 56  ? -6.357  36.194 11.798 1.00 21.03 ? 73  HIS A CE1 1 
ATOM   402  N NE2 . HIS A 1 56  ? -6.470  34.894 11.576 1.00 21.55 ? 73  HIS A NE2 1 
ATOM   403  N N   . TYR A 1 57  ? -10.945 34.791 9.110  1.00 18.97 ? 74  TYR A N   1 
ATOM   404  C CA  . TYR A 1 57  ? -10.775 33.908 7.967  1.00 19.32 ? 74  TYR A CA  1 
ATOM   405  C C   . TYR A 1 57  ? -11.763 34.204 6.842  1.00 21.31 ? 74  TYR A C   1 
ATOM   406  O O   . TYR A 1 57  ? -12.189 33.288 6.131  1.00 22.88 ? 74  TYR A O   1 
ATOM   407  C CB  . TYR A 1 57  ? -10.945 32.465 8.430  1.00 20.55 ? 74  TYR A CB  1 
ATOM   408  C CG  . TYR A 1 57  ? -9.824  31.921 9.272  1.00 19.24 ? 74  TYR A CG  1 
ATOM   409  C CD1 . TYR A 1 57  ? -8.498  32.017 8.858  1.00 23.97 ? 74  TYR A CD1 1 
ATOM   410  C CD2 . TYR A 1 57  ? -10.089 31.301 10.482 1.00 24.29 ? 74  TYR A CD2 1 
ATOM   411  C CE1 . TYR A 1 57  ? -7.471  31.494 9.608  1.00 24.42 ? 74  TYR A CE1 1 
ATOM   412  C CE2 . TYR A 1 57  ? -9.071  30.780 11.243 1.00 24.04 ? 74  TYR A CE2 1 
ATOM   413  C CZ  . TYR A 1 57  ? -7.755  30.882 10.802 1.00 28.19 ? 74  TYR A CZ  1 
ATOM   414  O OH  . TYR A 1 57  ? -6.725  30.377 11.564 1.00 33.15 ? 74  TYR A OH  1 
ATOM   415  N N   . ALA A 1 58  ? -12.142 35.467 6.670  1.00 22.87 ? 75  ALA A N   1 
ATOM   416  C CA  . ALA A 1 58  ? -13.153 35.813 5.675  1.00 26.14 ? 75  ALA A CA  1 
ATOM   417  C C   . ALA A 1 58  ? -12.765 35.342 4.280  1.00 28.03 ? 75  ALA A C   1 
ATOM   418  O O   . ALA A 1 58  ? -13.638 34.993 3.480  1.00 28.93 ? 75  ALA A O   1 
ATOM   419  C CB  . ALA A 1 58  ? -13.369 37.324 5.686  1.00 29.10 ? 75  ALA A CB  1 
ATOM   420  N N   . GLU A 1 59  ? -11.470 35.317 3.965  1.00 27.85 ? 76  GLU A N   1 
ATOM   421  C CA  . GLU A 1 59  ? -11.066 34.924 2.618  1.00 27.56 ? 76  GLU A CA  1 
ATOM   422  C C   . GLU A 1 59  ? -11.427 33.477 2.312  1.00 28.45 ? 76  GLU A C   1 
ATOM   423  O O   . GLU A 1 59  ? -11.518 33.103 1.137  1.00 30.70 ? 76  GLU A O   1 
ATOM   424  C CB  . GLU A 1 59  ? -9.560  35.131 2.439  1.00 33.33 ? 76  GLU A CB  1 
ATOM   425  C CG  . GLU A 1 59  ? -8.714  34.154 3.215  1.00 33.30 ? 76  GLU A CG  1 
ATOM   426  C CD  . GLU A 1 59  ? -7.255  34.571 3.273  1.00 40.36 ? 76  GLU A CD  1 
ATOM   427  O OE1 . GLU A 1 59  ? -6.533  34.342 2.278  1.00 41.80 ? 76  GLU A OE1 1 
ATOM   428  O OE2 . GLU A 1 59  ? -6.844  35.139 4.313  1.00 43.25 ? 76  GLU A OE2 1 
ATOM   429  N N   . HIS A 1 60  ? -11.632 32.655 3.342  1.00 26.18 ? 77  HIS A N   1 
ATOM   430  C CA  . HIS A 1 60  ? -11.925 31.240 3.185  1.00 28.73 ? 77  HIS A CA  1 
ATOM   431  C C   . HIS A 1 60  ? -13.410 30.934 3.253  1.00 29.68 ? 77  HIS A C   1 
ATOM   432  O O   . HIS A 1 60  ? -13.785 29.762 3.333  1.00 30.59 ? 77  HIS A O   1 
ATOM   433  C CB  . HIS A 1 60  ? -11.203 30.428 4.260  1.00 27.44 ? 77  HIS A CB  1 
ATOM   434  C CG  . HIS A 1 60  ? -9.719  30.557 4.212  1.00 28.71 ? 77  HIS A CG  1 
ATOM   435  N ND1 . HIS A 1 60  ? -9.008  30.565 3.029  1.00 27.79 ? 77  HIS A ND1 1 
ATOM   436  C CD2 . HIS A 1 60  ? -8.807  30.692 5.201  1.00 29.06 ? 77  HIS A CD2 1 
ATOM   437  C CE1 . HIS A 1 60  ? -7.719  30.693 3.296  1.00 29.54 ? 77  HIS A CE1 1 
ATOM   438  N NE2 . HIS A 1 60  ? -7.571  30.765 4.608  1.00 29.41 ? 77  HIS A NE2 1 
ATOM   439  N N   . LYS A 1 61  ? -14.265 31.945 3.228  1.00 28.70 ? 78  LYS A N   1 
ATOM   440  C CA  . LYS A 1 61  ? -15.692 31.684 3.306  1.00 33.87 ? 78  LYS A CA  1 
ATOM   441  C C   . LYS A 1 61  ? -16.104 30.664 2.251  1.00 35.11 ? 78  LYS A C   1 
ATOM   442  O O   . LYS A 1 61  ? -15.690 30.745 1.089  1.00 34.32 ? 78  LYS A O   1 
ATOM   443  C CB  . LYS A 1 61  ? -16.457 32.987 3.098  1.00 40.28 ? 78  LYS A CB  1 
ATOM   444  C CG  . LYS A 1 61  ? -17.934 32.869 3.414  1.00 47.05 ? 78  LYS A CG  1 
ATOM   445  C CD  . LYS A 1 61  ? -18.668 34.138 3.050  1.00 52.52 ? 78  LYS A CD  1 
ATOM   446  C CE  . LYS A 1 61  ? -20.141 34.045 3.413  1.00 57.35 ? 78  LYS A CE  1 
ATOM   447  N NZ  . LYS A 1 61  ? -20.925 35.135 2.766  1.00 61.32 ? 78  LYS A NZ  1 
ATOM   448  N N   . GLY A 1 62  ? -16.899 29.680 2.678  1.00 36.00 ? 79  GLY A N   1 
ATOM   449  C CA  . GLY A 1 62  ? -17.463 28.682 1.798  1.00 37.29 ? 79  GLY A CA  1 
ATOM   450  C C   . GLY A 1 62  ? -16.565 27.506 1.495  1.00 36.97 ? 79  GLY A C   1 
ATOM   451  O O   . GLY A 1 62  ? -17.011 26.559 0.821  1.00 38.50 ? 79  GLY A O   1 
ATOM   452  N N   . LYS A 1 63  ? -15.322 27.524 1.957  1.00 38.08 ? 80  LYS A N   1 
ATOM   453  C CA  . LYS A 1 63  ? -14.408 26.443 1.639  1.00 38.13 ? 80  LYS A CA  1 
ATOM   454  C C   . LYS A 1 63  ? -14.613 25.261 2.584  1.00 37.77 ? 80  LYS A C   1 
ATOM   455  O O   . LYS A 1 63  ? -14.931 25.444 3.764  1.00 35.91 ? 80  LYS A O   1 
ATOM   456  C CB  . LYS A 1 63  ? -12.975 26.936 1.742  1.00 41.23 ? 80  LYS A CB  1 
ATOM   457  C CG  . LYS A 1 63  ? -12.682 28.067 0.784  1.00 42.68 ? 80  LYS A CG  1 
ATOM   458  C CD  . LYS A 1 63  ? -11.213 28.396 0.763  1.00 44.86 ? 80  LYS A CD  1 
ATOM   459  C CE  . LYS A 1 63  ? -10.922 29.505 -0.229 1.00 47.29 ? 80  LYS A CE  1 
ATOM   460  N NZ  . LYS A 1 63  ? -9.609  30.164 0.049  1.00 47.65 ? 80  LYS A NZ  1 
ATOM   461  N N   . PRO A 1 64  ? -14.408 24.039 2.091  1.00 37.56 ? 81  PRO A N   1 
ATOM   462  C CA  . PRO A 1 64  ? -14.728 22.856 2.910  1.00 39.48 ? 81  PRO A CA  1 
ATOM   463  C C   . PRO A 1 64  ? -13.917 22.745 4.186  1.00 41.67 ? 81  PRO A C   1 
ATOM   464  O O   . PRO A 1 64  ? -14.394 22.143 5.157  1.00 42.08 ? 81  PRO A O   1 
ATOM   465  C CB  . PRO A 1 64  ? -14.475 21.675 1.956  1.00 37.64 ? 81  PRO A CB  1 
ATOM   466  C CG  . PRO A 1 64  ? -13.596 22.216 0.871  1.00 36.94 ? 81  PRO A CG  1 
ATOM   467  C CD  . PRO A 1 64  ? -13.925 23.676 0.743  1.00 38.54 ? 81  PRO A CD  1 
ATOM   468  N N   . PHE A 1 65  ? -12.713 23.312 4.222  1.00 41.25 ? 82  PHE A N   1 
ATOM   469  C CA  . PHE A 1 65  ? -11.840 23.178 5.378  1.00 41.13 ? 82  PHE A CA  1 
ATOM   470  C C   . PHE A 1 65  ? -12.103 24.223 6.457  1.00 36.77 ? 82  PHE A C   1 
ATOM   471  O O   . PHE A 1 65  ? -11.533 24.119 7.553  1.00 36.75 ? 82  PHE A O   1 
ATOM   472  C CB  . PHE A 1 65  ? -10.370 23.261 4.936  1.00 41.96 ? 82  PHE A CB  1 
ATOM   473  C CG  . PHE A 1 65  ? -9.996  24.576 4.303  1.00 42.84 ? 82  PHE A CG  1 
ATOM   474  C CD1 . PHE A 1 65  ? -9.721  25.688 5.092  1.00 41.56 ? 82  PHE A CD1 1 
ATOM   475  C CD2 . PHE A 1 65  ? -9.915  24.703 2.922  1.00 43.33 ? 82  PHE A CD2 1 
ATOM   476  C CE1 . PHE A 1 65  ? -9.380  26.902 4.518  1.00 40.87 ? 82  PHE A CE1 1 
ATOM   477  C CE2 . PHE A 1 65  ? -9.568  25.915 2.342  1.00 43.68 ? 82  PHE A CE2 1 
ATOM   478  C CZ  . PHE A 1 65  ? -9.302  27.017 3.147  1.00 41.44 ? 82  PHE A CZ  1 
ATOM   479  N N   . LEU A 1 66  ? -12.948 25.218 6.182  1.00 35.79 ? 83  LEU A N   1 
ATOM   480  C CA  . LEU A 1 66  ? -13.122 26.316 7.131  1.00 33.49 ? 83  LEU A CA  1 
ATOM   481  C C   . LEU A 1 66  ? -13.687 25.853 8.464  1.00 34.72 ? 83  LEU A C   1 
ATOM   482  O O   . LEU A 1 66  ? -13.176 26.294 9.508  1.00 33.69 ? 83  LEU A O   1 
ATOM   483  C CB  . LEU A 1 66  ? -13.949 27.450 6.512  1.00 31.89 ? 83  LEU A CB  1 
ATOM   484  C CG  . LEU A 1 66  ? -14.140 28.669 7.424  1.00 29.78 ? 83  LEU A CG  1 
ATOM   485  C CD1 . LEU A 1 66  ? -12.804 29.176 7.940  1.00 31.13 ? 83  LEU A CD1 1 
ATOM   486  C CD2 . LEU A 1 66  ? -14.890 29.790 6.708  1.00 33.42 ? 83  LEU A CD2 1 
ATOM   487  N N   . PRO A 1 67  ? -14.721 25.006 8.519  1.00 35.70 ? 84  PRO A N   1 
ATOM   488  C CA  . PRO A 1 67  ? -15.221 24.579 9.836  1.00 37.05 ? 84  PRO A CA  1 
ATOM   489  C C   . PRO A 1 67  ? -14.158 23.937 10.715 1.00 38.21 ? 84  PRO A C   1 
ATOM   490  O O   . PRO A 1 67  ? -14.080 24.257 11.905 1.00 35.17 ? 84  PRO A O   1 
ATOM   491  C CB  . PRO A 1 67  ? -16.366 23.617 9.489  1.00 40.11 ? 84  PRO A CB  1 
ATOM   492  C CG  . PRO A 1 67  ? -16.804 24.026 8.090  1.00 38.95 ? 84  PRO A CG  1 
ATOM   493  C CD  . PRO A 1 67  ? -15.550 24.499 7.405  1.00 36.19 ? 84  PRO A CD  1 
ATOM   494  N N   . GLY A 1 68  ? -13.317 23.055 10.172 1.00 39.16 ? 85  GLY A N   1 
ATOM   495  C CA  . GLY A 1 68  ? -12.293 22.436 11.003 1.00 39.21 ? 85  GLY A CA  1 
ATOM   496  C C   . GLY A 1 68  ? -11.259 23.443 11.463 1.00 40.65 ? 85  GLY A C   1 
ATOM   497  O O   . GLY A 1 68  ? -10.761 23.381 12.592 1.00 41.24 ? 85  GLY A O   1 
ATOM   498  N N   . LEU A 1 69  ? -10.930 24.395 10.595 1.00 37.14 ? 86  LEU A N   1 
ATOM   499  C CA  . LEU A 1 69  ? -10.008 25.451 10.971 1.00 36.76 ? 86  LEU A CA  1 
ATOM   500  C C   . LEU A 1 69  ? -10.563 26.264 12.137 1.00 33.88 ? 86  LEU A C   1 
ATOM   501  O O   . LEU A 1 69  ? -9.842  26.557 13.100 1.00 32.32 ? 86  LEU A O   1 
ATOM   502  C CB  . LEU A 1 69  ? -9.784  26.330 9.750  1.00 38.76 ? 86  LEU A CB  1 
ATOM   503  C CG  . LEU A 1 69  ? -8.886  27.540 9.893  1.00 40.99 ? 86  LEU A CG  1 
ATOM   504  C CD1 . LEU A 1 69  ? -7.534  27.141 10.464 1.00 45.05 ? 86  LEU A CD1 1 
ATOM   505  C CD2 . LEU A 1 69  ? -8.753  28.165 8.516  1.00 41.19 ? 86  LEU A CD2 1 
ATOM   506  N N   . ILE A 1 70  ? -11.848 26.617 12.075 1.00 29.34 ? 87  ILE A N   1 
ATOM   507  C CA  A ILE A 1 70  ? -12.433 27.408 13.154 0.75 27.91 ? 87  ILE A CA  1 
ATOM   508  C CA  B ILE A 1 70  ? -12.471 27.395 13.148 0.25 28.88 ? 87  ILE A CA  1 
ATOM   509  C C   . ILE A 1 70  ? -12.445 26.612 14.454 1.00 28.53 ? 87  ILE A C   1 
ATOM   510  O O   . ILE A 1 70  ? -12.211 27.171 15.531 1.00 28.11 ? 87  ILE A O   1 
ATOM   511  C CB  A ILE A 1 70  ? -13.813 27.950 12.738 0.75 25.77 ? 87  ILE A CB  1 
ATOM   512  C CB  B ILE A 1 70  ? -13.907 27.795 12.751 0.25 28.50 ? 87  ILE A CB  1 
ATOM   513  C CG1 A ILE A 1 70  ? -13.626 29.057 11.690 0.75 23.15 ? 87  ILE A CG1 1 
ATOM   514  C CG1 B ILE A 1 70  ? -13.908 28.666 11.489 0.25 27.75 ? 87  ILE A CG1 1 
ATOM   515  C CG2 A ILE A 1 70  ? -14.585 28.474 13.944 0.75 26.44 ? 87  ILE A CG2 1 
ATOM   516  C CG2 B ILE A 1 70  ? -14.603 28.523 13.896 0.25 28.64 ? 87  ILE A CG2 1 
ATOM   517  C CD1 A ILE A 1 70  ? -14.897 29.663 11.171 0.75 24.65 ? 87  ILE A CD1 1 
ATOM   518  C CD1 B ILE A 1 70  ? -13.290 30.034 11.667 0.25 27.07 ? 87  ILE A CD1 1 
ATOM   519  N N   . GLU A 1 71  ? -12.681 25.301 14.381 1.00 32.16 ? 88  GLU A N   1 
ATOM   520  C CA  . GLU A 1 71  ? -12.641 24.490 15.597 1.00 35.18 ? 88  GLU A CA  1 
ATOM   521  C C   . GLU A 1 71  ? -11.250 24.497 16.224 1.00 37.58 ? 88  GLU A C   1 
ATOM   522  O O   . GLU A 1 71  ? -11.104 24.689 17.438 1.00 38.99 ? 88  GLU A O   1 
ATOM   523  C CB  . GLU A 1 71  ? -13.092 23.064 15.291 1.00 45.13 ? 88  GLU A CB  1 
ATOM   524  C CG  . GLU A 1 71  ? -14.603 22.896 15.213 1.00 56.25 ? 88  GLU A CG  1 
ATOM   525  C CD  . GLU A 1 71  ? -15.014 21.509 14.735 1.00 66.93 ? 88  GLU A CD  1 
ATOM   526  O OE1 . GLU A 1 71  ? -14.135 20.749 14.267 1.00 69.11 ? 88  GLU A OE1 1 
ATOM   527  O OE2 . GLU A 1 71  ? -16.218 21.183 14.826 1.00 71.07 ? 88  GLU A OE2 1 
ATOM   528  N N   . LYS A 1 72  ? -10.208 24.284 15.413 1.00 34.48 ? 89  LYS A N   1 
ATOM   529  C CA  . LYS A 1 72  ? -8.853  24.267 15.956 1.00 33.50 ? 89  LYS A CA  1 
ATOM   530  C C   . LYS A 1 72  ? -8.512  25.585 16.629 1.00 29.40 ? 89  LYS A C   1 
ATOM   531  O O   . LYS A 1 72  ? -7.779  25.614 17.627 1.00 30.80 ? 89  LYS A O   1 
ATOM   532  C CB  . LYS A 1 72  ? -7.840  24.006 14.837 1.00 35.29 ? 89  LYS A CB  1 
ATOM   533  C CG  . LYS A 1 72  ? -7.810  22.587 14.324 1.00 38.55 ? 89  LYS A CG  1 
ATOM   534  C CD  . LYS A 1 72  ? -6.581  21.886 14.822 1.00 40.60 ? 89  LYS A CD  1 
ATOM   535  C CE  . LYS A 1 72  ? -6.405  20.548 14.133 1.00 42.48 ? 89  LYS A CE  1 
ATOM   536  N NZ  . LYS A 1 72  ? -7.547  19.644 14.428 1.00 43.79 ? 89  LYS A NZ  1 
ATOM   537  N N   . MET A 1 73  ? -9.022  26.682 16.095 1.00 27.16 ? 90  MET A N   1 
ATOM   538  C CA  . MET A 1 73  ? -8.653  28.006 16.557 1.00 23.46 ? 90  MET A CA  1 
ATOM   539  C C   . MET A 1 73  ? -9.544  28.506 17.675 1.00 20.58 ? 90  MET A C   1 
ATOM   540  O O   . MET A 1 73  ? -9.283  29.586 18.206 1.00 21.91 ? 90  MET A O   1 
ATOM   541  C CB  . MET A 1 73  ? -8.731  28.998 15.389 1.00 25.60 ? 90  MET A CB  1 
ATOM   542  C CG  . MET A 1 73  ? -7.531  28.928 14.451 1.00 28.18 ? 90  MET A CG  1 
ATOM   543  S SD  . MET A 1 73  ? -5.973  29.364 15.241 1.00 28.63 ? 90  MET A SD  1 
ATOM   544  C CE  . MET A 1 73  ? -6.349  31.001 15.868 1.00 30.30 ? 90  MET A CE  1 
ATOM   545  N N   . THR A 1 74  ? -10.601 27.771 18.017 1.00 20.60 ? 91  THR A N   1 
ATOM   546  C CA  . THR A 1 74  ? -11.469 28.155 19.124 1.00 19.52 ? 91  THR A CA  1 
ATOM   547  C C   . THR A 1 74  ? -10.761 27.776 20.413 1.00 21.02 ? 91  THR A C   1 
ATOM   548  O O   . THR A 1 74  ? -10.631 26.594 20.748 1.00 25.71 ? 91  THR A O   1 
ATOM   549  C CB  . THR A 1 74  ? -12.833 27.490 19.008 1.00 21.05 ? 91  THR A CB  1 
ATOM   550  O OG1 . THR A 1 74  ? -13.464 27.918 17.795 1.00 23.57 ? 91  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 74  ? -13.711 27.900 20.168 1.00 22.90 ? 91  THR A CG2 1 
ATOM   552  N N   . GLY A 1 75  ? -10.282 28.781 21.118 1.00 16.45 ? 92  GLY A N   1 
ATOM   553  C CA  . GLY A 1 75  ? -9.470  28.575 22.290 1.00 15.61 ? 92  GLY A CA  1 
ATOM   554  C C   . GLY A 1 75  ? -8.721  29.839 22.634 1.00 14.41 ? 92  GLY A C   1 
ATOM   555  O O   . GLY A 1 75  ? -8.871  30.878 21.973 1.00 15.45 ? 92  GLY A O   1 
ATOM   556  N N   . PRO A 1 76  ? -7.913  29.789 23.697 1.00 15.18 ? 93  PRO A N   1 
ATOM   557  C CA  . PRO A 1 76  ? -7.094  30.958 24.042 1.00 14.85 ? 93  PRO A CA  1 
ATOM   558  C C   . PRO A 1 76  ? -6.115  31.286 22.927 1.00 13.58 ? 93  PRO A C   1 
ATOM   559  O O   . PRO A 1 76  ? -5.531  30.393 22.311 1.00 15.27 ? 93  PRO A O   1 
ATOM   560  C CB  . PRO A 1 76  ? -6.374  30.515 25.322 1.00 15.65 ? 93  PRO A CB  1 
ATOM   561  C CG  . PRO A 1 76  ? -6.270  29.049 25.182 1.00 17.02 ? 93  PRO A CG  1 
ATOM   562  C CD  . PRO A 1 76  ? -7.555  28.618 24.521 1.00 15.81 ? 93  PRO A CD  1 
ATOM   563  N N   . VAL A 1 77  ? -5.957  32.583 22.676 1.00 15.24 ? 94  VAL A N   1 
ATOM   564  C CA  . VAL A 1 77  ? -5.000  33.106 21.713 1.00 14.32 ? 94  VAL A CA  1 
ATOM   565  C C   . VAL A 1 77  ? -4.348  34.348 22.309 1.00 15.43 ? 94  VAL A C   1 
ATOM   566  O O   . VAL A 1 77  ? -4.934  35.040 23.153 1.00 16.05 ? 94  VAL A O   1 
ATOM   567  C CB  . VAL A 1 77  ? -5.623  33.457 20.328 1.00 13.91 ? 94  VAL A CB  1 
ATOM   568  C CG1 . VAL A 1 77  ? -6.223  32.215 19.670 1.00 14.02 ? 94  VAL A CG1 1 
ATOM   569  C CG2 . VAL A 1 77  ? -6.677  34.558 20.457 1.00 16.26 ? 94  VAL A CG2 1 
ATOM   570  N N   . LEU A 1 78  ? -3.144  34.647 21.848 1.00 14.18 ? 95  LEU A N   1 
ATOM   571  C CA  . LEU A 1 78  ? -2.487  35.909 22.173 1.00 13.24 ? 95  LEU A CA  1 
ATOM   572  C C   . LEU A 1 78  ? -2.434  36.773 20.920 1.00 12.58 ? 95  LEU A C   1 
ATOM   573  O O   . LEU A 1 78  ? -1.695  36.472 19.974 1.00 13.17 ? 95  LEU A O   1 
ATOM   574  C CB  . LEU A 1 78  ? -1.104  35.722 22.795 1.00 13.43 ? 95  LEU A CB  1 
ATOM   575  C CG  . LEU A 1 78  ? -0.530  36.995 23.413 1.00 14.53 ? 95  LEU A CG  1 
ATOM   576  C CD1 . LEU A 1 78  ? -1.266  37.356 24.694 1.00 15.50 ? 95  LEU A CD1 1 
ATOM   577  C CD2 . LEU A 1 78  ? 0.964   36.917 23.699 1.00 13.07 ? 95  LEU A CD2 1 
ATOM   578  N N   . CYS A 1 79  ? -3.208  37.844 20.940 1.00 13.63 ? 96  CYS A N   1 
ATOM   579  C CA  . CYS A 1 79  ? -3.226  38.838 19.875 1.00 13.64 ? 96  CYS A CA  1 
ATOM   580  C C   . CYS A 1 79  ? -2.045  39.774 20.062 1.00 12.76 ? 96  CYS A C   1 
ATOM   581  O O   . CYS A 1 79  ? -1.802  40.260 21.170 1.00 14.13 ? 96  CYS A O   1 
ATOM   582  C CB  . CYS A 1 79  ? -4.502  39.652 19.982 1.00 14.63 ? 96  CYS A CB  1 
ATOM   583  S SG  . CYS A 1 79  ? -6.031  38.687 20.011 1.00 16.20 ? 96  CYS A SG  1 
ATOM   584  N N   . MET A 1 80  ? -1.311  40.049 18.989 1.00 14.99 ? 97  MET A N   1 
ATOM   585  C CA  . MET A 1 80  ? -0.120  40.883 19.094 1.00 14.32 ? 97  MET A CA  1 
ATOM   586  C C   . MET A 1 80  ? -0.002  41.777 17.866 1.00 12.41 ? 97  MET A C   1 
ATOM   587  O O   . MET A 1 80  ? -0.386  41.400 16.756 1.00 15.46 ? 97  MET A O   1 
ATOM   588  C CB  . MET A 1 80  ? 1.158   40.027 19.182 1.00 14.53 ? 97  MET A CB  1 
ATOM   589  C CG  . MET A 1 80  ? 1.061   38.873 20.177 1.00 15.10 ? 97  MET A CG  1 
ATOM   590  S SD  . MET A 1 80  ? 2.613   37.919 20.378 1.00 15.55 ? 97  MET A SD  1 
ATOM   591  C CE  . MET A 1 80  ? 2.824   37.220 18.745 1.00 16.28 ? 97  MET A CE  1 
ATOM   592  N N   . VAL A 1 81  ? 0.556   42.963 18.073 1.00 13.44 ? 98  VAL A N   1 
ATOM   593  C CA  . VAL A 1 81  ? 1.019   43.820 16.985 1.00 12.95 ? 98  VAL A CA  1 
ATOM   594  C C   . VAL A 1 81  ? 2.490   44.101 17.221 1.00 12.72 ? 98  VAL A C   1 
ATOM   595  O O   . VAL A 1 81  ? 2.863   44.595 18.290 1.00 14.48 ? 98  VAL A O   1 
ATOM   596  C CB  . VAL A 1 81  ? 0.226   45.134 16.881 1.00 15.22 ? 98  VAL A CB  1 
ATOM   597  C CG1 . VAL A 1 81  ? 0.766   45.988 15.724 1.00 14.20 ? 98  VAL A CG1 1 
ATOM   598  C CG2 . VAL A 1 81  ? -1.256  44.843 16.674 1.00 17.10 ? 98  VAL A CG2 1 
ATOM   599  N N   . PHE A 1 82  ? 3.325   43.784 16.236 1.00 13.81 ? 99  PHE A N   1 
ATOM   600  C CA  . PHE A 1 82  ? 4.738   44.130 16.261 1.00 13.85 ? 99  PHE A CA  1 
ATOM   601  C C   . PHE A 1 82  ? 5.047   45.148 15.171 1.00 13.60 ? 99  PHE A C   1 
ATOM   602  O O   . PHE A 1 82  ? 4.458   45.120 14.088 1.00 14.57 ? 99  PHE A O   1 
ATOM   603  C CB  . PHE A 1 82  ? 5.622   42.890 16.088 1.00 15.59 ? 99  PHE A CB  1 
ATOM   604  C CG  . PHE A 1 82  ? 5.857   42.135 17.370 1.00 13.64 ? 99  PHE A CG  1 
ATOM   605  C CD1 . PHE A 1 82  ? 6.912   42.465 18.190 1.00 14.15 ? 99  PHE A CD1 1 
ATOM   606  C CD2 . PHE A 1 82  ? 5.021   41.121 17.754 1.00 14.41 ? 99  PHE A CD2 1 
ATOM   607  C CE1 . PHE A 1 82  ? 7.141   41.781 19.378 1.00 16.55 ? 99  PHE A CE1 1 
ATOM   608  C CE2 . PHE A 1 82  ? 5.235   40.426 18.957 1.00 17.13 ? 99  PHE A CE2 1 
ATOM   609  C CZ  . PHE A 1 82  ? 6.287   40.762 19.759 1.00 17.42 ? 99  PHE A CZ  1 
ATOM   610  N N   . GLU A 1 83  ? 5.982   46.043 15.479 1.00 15.41 ? 100 GLU A N   1 
ATOM   611  C CA  . GLU A 1 83  ? 6.397   47.113 14.586 1.00 14.65 ? 100 GLU A CA  1 
ATOM   612  C C   . GLU A 1 83  ? 7.874   46.964 14.237 1.00 15.18 ? 100 GLU A C   1 
ATOM   613  O O   . GLU A 1 83  ? 8.720   46.699 15.108 1.00 15.16 ? 100 GLU A O   1 
ATOM   614  C CB  . GLU A 1 83  ? 6.188   48.472 15.242 1.00 14.57 ? 100 GLU A CB  1 
ATOM   615  C CG  . GLU A 1 83  ? 6.696   49.648 14.434 1.00 15.25 ? 100 GLU A CG  1 
ATOM   616  C CD  . GLU A 1 83  ? 6.457   50.945 15.170 1.00 17.74 ? 100 GLU A CD  1 
ATOM   617  O OE1 . GLU A 1 83  ? 5.334   51.475 15.059 1.00 19.26 ? 100 GLU A OE1 1 
ATOM   618  O OE2 . GLU A 1 83  ? 7.373   51.390 15.912 1.00 18.95 ? 100 GLU A OE2 1 
ATOM   619  N N   . GLY A 1 84  ? 8.188   47.153 12.962 1.00 14.04 ? 101 GLY A N   1 
ATOM   620  C CA  . GLY A 1 84  ? 9.575   47.151 12.532 1.00 15.25 ? 101 GLY A CA  1 
ATOM   621  C C   . GLY A 1 84  ? 9.660   47.355 11.033 1.00 14.78 ? 101 GLY A C   1 
ATOM   622  O O   . GLY A 1 84  ? 8.645   47.430 10.329 1.00 15.24 ? 101 GLY A O   1 
ATOM   623  N N   . VAL A 1 85  ? 10.893  47.470 10.552 1.00 15.37 ? 102 VAL A N   1 
ATOM   624  C CA  . VAL A 1 85  ? 11.114  47.630 9.114  1.00 15.96 ? 102 VAL A CA  1 
ATOM   625  C C   . VAL A 1 85  ? 10.700  46.340 8.416  1.00 15.32 ? 102 VAL A C   1 
ATOM   626  O O   . VAL A 1 85  ? 11.165  45.255 8.774  1.00 15.71 ? 102 VAL A O   1 
ATOM   627  C CB  . VAL A 1 85  ? 12.582  47.969 8.820  1.00 15.74 ? 102 VAL A CB  1 
ATOM   628  C CG1 . VAL A 1 85  ? 12.821  48.002 7.314  1.00 18.68 ? 102 VAL A CG1 1 
ATOM   629  C CG2 . VAL A 1 85  ? 12.968  49.270 9.481  1.00 18.70 ? 102 VAL A CG2 1 
ATOM   630  N N   . ASP A 1 86  ? 9.796   46.453 7.434  1.00 16.94 ? 103 ASP A N   1 
ATOM   631  C CA  . ASP A 1 86  ? 9.426   45.296 6.613  1.00 16.83 ? 103 ASP A CA  1 
ATOM   632  C C   . ASP A 1 86  ? 8.885   44.167 7.480  1.00 14.19 ? 103 ASP A C   1 
ATOM   633  O O   . ASP A 1 86  ? 8.995   42.993 7.131  1.00 16.16 ? 103 ASP A O   1 
ATOM   634  C CB  . ASP A 1 86  ? 10.634  44.848 5.778  1.00 17.86 ? 103 ASP A CB  1 
ATOM   635  C CG  . ASP A 1 86  ? 10.290  43.888 4.648  1.00 19.90 ? 103 ASP A CG  1 
ATOM   636  O OD1 . ASP A 1 86  ? 9.246   44.064 3.967  1.00 20.81 ? 103 ASP A OD1 1 
ATOM   637  O OD2 . ASP A 1 86  ? 11.137  42.980 4.394  1.00 21.96 ? 103 ASP A OD2 1 
ATOM   638  N N   . VAL A 1 87  ? 8.306   44.513 8.634  1.00 14.59 ? 104 VAL A N   1 
ATOM   639  C CA  . VAL A 1 87  ? 7.985   43.475 9.612  1.00 16.45 ? 104 VAL A CA  1 
ATOM   640  C C   . VAL A 1 87  ? 6.908   42.519 9.109  1.00 16.03 ? 104 VAL A C   1 
ATOM   641  O O   . VAL A 1 87  ? 6.837   41.368 9.567  1.00 14.83 ? 104 VAL A O   1 
ATOM   642  C CB  . VAL A 1 87  ? 7.633   44.083 10.989 1.00 13.36 ? 104 VAL A CB  1 
ATOM   643  C CG1 . VAL A 1 87  ? 6.251   44.718 10.979 1.00 14.72 ? 104 VAL A CG1 1 
ATOM   644  C CG2 . VAL A 1 87  ? 7.696   42.995 12.073 1.00 15.91 ? 104 VAL A CG2 1 
ATOM   645  N N   . ILE A 1 88  ? 6.038   42.951 8.191  1.00 14.40 ? 105 ILE A N   1 
ATOM   646  C CA  . ILE A 1 88  ? 5.007   42.034 7.706  1.00 15.63 ? 105 ILE A CA  1 
ATOM   647  C C   . ILE A 1 88  ? 5.657   40.841 7.001  1.00 14.49 ? 105 ILE A C   1 
ATOM   648  O O   . ILE A 1 88  ? 5.472   39.679 7.383  1.00 15.34 ? 105 ILE A O   1 
ATOM   649  C CB  . ILE A 1 88  ? 4.004   42.766 6.803  1.00 15.48 ? 105 ILE A CB  1 
ATOM   650  C CG1 . ILE A 1 88  ? 3.226   43.832 7.579  1.00 14.55 ? 105 ILE A CG1 1 
ATOM   651  C CG2 . ILE A 1 88  ? 3.050   41.776 6.202  1.00 16.50 ? 105 ILE A CG2 1 
ATOM   652  C CD1 . ILE A 1 88  ? 2.462   44.775 6.672  1.00 17.75 ? 105 ILE A CD1 1 
ATOM   653  N N   . ALA A 1 89  ? 6.455   41.118 5.975  1.00 14.94 ? 106 ALA A N   1 
ATOM   654  C CA  . ALA A 1 89  ? 7.147   40.045 5.266  1.00 15.81 ? 106 ALA A CA  1 
ATOM   655  C C   . ALA A 1 89  ? 8.157   39.331 6.156  1.00 15.66 ? 106 ALA A C   1 
ATOM   656  O O   . ALA A 1 89  ? 8.308   38.108 6.071  1.00 16.66 ? 106 ALA A O   1 
ATOM   657  C CB  . ALA A 1 89  ? 7.850   40.614 4.030  1.00 15.32 ? 106 ALA A CB  1 
ATOM   658  N N   . GLN A 1 90  ? 8.878   40.072 7.002  1.00 14.21 ? 107 GLN A N   1 
ATOM   659  C CA  . GLN A 1 90  ? 9.917   39.449 7.825  1.00 14.66 ? 107 GLN A CA  1 
ATOM   660  C C   . GLN A 1 90  ? 9.322   38.498 8.860  1.00 14.92 ? 107 GLN A C   1 
ATOM   661  O O   . GLN A 1 90  ? 9.862   37.415 9.088  1.00 15.48 ? 107 GLN A O   1 
ATOM   662  C CB  . GLN A 1 90  ? 10.778  40.522 8.498  1.00 17.13 ? 107 GLN A CB  1 
ATOM   663  C CG  . GLN A 1 90  ? 11.673  41.243 7.528  1.00 15.64 ? 107 GLN A CG  1 
ATOM   664  C CD  . GLN A 1 90  ? 12.685  40.311 6.881  1.00 16.10 ? 107 GLN A CD  1 
ATOM   665  O OE1 . GLN A 1 90  ? 13.425  39.645 7.569  1.00 16.16 ? 107 GLN A OE1 1 
ATOM   666  N NE2 . GLN A 1 90  ? 12.730  40.286 5.542  1.00 17.81 ? 107 GLN A NE2 1 
ATOM   667  N N   . ALA A 1 91  ? 8.201   38.875 9.472  1.00 16.17 ? 108 ALA A N   1 
ATOM   668  C CA  . ALA A 1 91  ? 7.564   37.976 10.427 1.00 14.18 ? 108 ALA A CA  1 
ATOM   669  C C   . ALA A 1 91  ? 7.098   36.699 9.742  1.00 16.12 ? 108 ALA A C   1 
ATOM   670  O O   . ALA A 1 91  ? 7.203   35.613 10.309 1.00 15.93 ? 108 ALA A O   1 
ATOM   671  C CB  . ALA A 1 91  ? 6.387   38.672 11.096 1.00 14.83 ? 108 ALA A CB  1 
ATOM   672  N N   . ARG A 1 92  ? 6.579   36.812 8.511  1.00 16.14 ? 109 ARG A N   1 
ATOM   673  C CA  . ARG A 1 92  ? 6.204   35.608 7.770  1.00 17.70 ? 109 ARG A CA  1 
ATOM   674  C C   . ARG A 1 92  ? 7.415   34.717 7.518  1.00 16.20 ? 109 ARG A C   1 
ATOM   675  O O   . ARG A 1 92  ? 7.329   33.484 7.601  1.00 17.02 ? 109 ARG A O   1 
ATOM   676  C CB  . ARG A 1 92  ? 5.559   35.985 6.441  1.00 22.82 ? 109 ARG A CB  1 
ATOM   677  C CG  . ARG A 1 92  ? 4.261   36.730 6.582  1.00 26.96 ? 109 ARG A CG  1 
ATOM   678  C CD  . ARG A 1 92  ? 3.119   35.797 6.917  1.00 33.96 ? 109 ARG A CD  1 
ATOM   679  N NE  . ARG A 1 92  ? 2.688   35.037 5.754  1.00 44.06 ? 109 ARG A NE  1 
ATOM   680  C CZ  . ARG A 1 92  ? 1.638   34.228 5.741  1.00 50.25 ? 109 ARG A CZ  1 
ATOM   681  N NH1 . ARG A 1 92  ? 0.893   34.046 6.819  1.00 50.19 ? 109 ARG A NH1 1 
ATOM   682  N NH2 . ARG A 1 92  ? 1.322   33.594 4.616  1.00 53.62 ? 109 ARG A NH2 1 
ATOM   683  N N   . LYS A 1 93  ? 8.543   35.328 7.159  1.00 16.88 ? 110 LYS A N   1 
ATOM   684  C CA  . LYS A 1 93  ? 9.769   34.566 6.964  1.00 18.72 ? 110 LYS A CA  1 
ATOM   685  C C   . LYS A 1 93  ? 10.195  33.875 8.252  1.00 17.17 ? 110 LYS A C   1 
ATOM   686  O O   . LYS A 1 93  ? 10.635  32.714 8.230  1.00 16.48 ? 110 LYS A O   1 
ATOM   687  C CB  . LYS A 1 93  ? 10.853  35.507 6.467  1.00 20.68 ? 110 LYS A CB  1 
ATOM   688  C CG  . LYS A 1 93  ? 12.127  34.826 6.125  1.00 20.51 ? 110 LYS A CG  1 
ATOM   689  C CD  . LYS A 1 93  ? 13.059  35.801 5.427  1.00 23.09 ? 110 LYS A CD  1 
ATOM   690  C CE  . LYS A 1 93  ? 14.427  35.223 5.240  1.00 23.52 ? 110 LYS A CE  1 
ATOM   691  N NZ  . LYS A 1 93  ? 15.284  36.257 4.644  1.00 22.88 ? 110 LYS A NZ  1 
ATOM   692  N N   . MET A 1 94  ? 10.033  34.560 9.392  1.00 14.70 ? 111 MET A N   1 
ATOM   693  C CA  . MET A 1 94  ? 10.418  33.984 10.680 1.00 14.31 ? 111 MET A CA  1 
ATOM   694  C C   . MET A 1 94  ? 9.500   32.839 11.088 1.00 14.57 ? 111 MET A C   1 
ATOM   695  O O   . MET A 1 94  ? 9.950   31.891 11.736 1.00 15.27 ? 111 MET A O   1 
ATOM   696  C CB  . MET A 1 94  ? 10.422  35.057 11.765 1.00 15.89 ? 111 MET A CB  1 
ATOM   697  C CG  . MET A 1 94  ? 11.469  36.120 11.519 1.00 14.83 ? 111 MET A CG  1 
ATOM   698  S SD  . MET A 1 94  ? 11.235  37.568 12.551 1.00 16.34 ? 111 MET A SD  1 
ATOM   699  C CE  . MET A 1 94  ? 11.717  36.969 14.178 1.00 20.55 ? 111 MET A CE  1 
ATOM   700  N N   . MET A 1 95  ? 8.213   32.928 10.743 1.00 16.02 ? 112 MET A N   1 
ATOM   701  C CA  A MET A 1 95  ? 7.277   31.855 11.053 0.52 15.07 ? 112 MET A CA  1 
ATOM   702  C CA  B MET A 1 95  ? 7.288   31.852 11.066 0.48 16.27 ? 112 MET A CA  1 
ATOM   703  C C   . MET A 1 95  ? 7.594   30.603 10.259 1.00 15.47 ? 112 MET A C   1 
ATOM   704  O O   . MET A 1 95  ? 7.478   29.485 10.772 1.00 15.15 ? 112 MET A O   1 
ATOM   705  C CB  A MET A 1 95  ? 5.847   32.302 10.725 0.52 13.13 ? 112 MET A CB  1 
ATOM   706  C CB  B MET A 1 95  ? 5.847   32.302 10.804 0.48 16.73 ? 112 MET A CB  1 
ATOM   707  C CG  A MET A 1 95  ? 5.309   33.389 11.645 0.52 15.25 ? 112 MET A CG  1 
ATOM   708  C CG  B MET A 1 95  ? 5.337   33.342 11.799 0.48 18.46 ? 112 MET A CG  1 
ATOM   709  S SD  A MET A 1 95  ? 3.787   34.143 11.037 0.52 17.27 ? 112 MET A SD  1 
ATOM   710  S SD  B MET A 1 95  ? 3.581   33.704 11.595 0.48 19.40 ? 112 MET A SD  1 
ATOM   711  C CE  A MET A 1 95  ? 2.893   32.772 10.342 0.52 18.43 ? 112 MET A CE  1 
ATOM   712  C CE  B MET A 1 95  ? 3.588   34.450 9.982  0.48 19.28 ? 112 MET A CE  1 
ATOM   713  N N   . GLY A 1 96  ? 7.968   30.779 8.990  1.00 14.54 ? 113 GLY A N   1 
ATOM   714  C CA  . GLY A 1 96  ? 8.201   29.665 8.106  1.00 16.47 ? 113 GLY A CA  1 
ATOM   715  C C   . GLY A 1 96  ? 6.952   29.228 7.381  1.00 15.09 ? 113 GLY A C   1 
ATOM   716  O O   . GLY A 1 96  ? 5.837   29.673 7.659  1.00 15.72 ? 113 GLY A O   1 
ATOM   717  N N   . SER A 1 97  ? 7.144   28.267 6.480  1.00 15.42 ? 114 SER A N   1 
ATOM   718  C CA  A SER A 1 97  ? 6.066   27.752 5.645  0.65 15.57 ? 114 SER A CA  1 
ATOM   719  C CA  B SER A 1 97  ? 6.043   27.820 5.644  0.35 16.67 ? 114 SER A CA  1 
ATOM   720  C C   . SER A 1 97  ? 4.906   27.246 6.488  1.00 16.76 ? 114 SER A C   1 
ATOM   721  O O   . SER A 1 97  ? 5.093   26.782 7.614  1.00 16.53 ? 114 SER A O   1 
ATOM   722  C CB  A SER A 1 97  ? 6.572   26.573 4.807  0.65 17.82 ? 114 SER A CB  1 
ATOM   723  C CB  B SER A 1 97  ? 6.522   26.776 4.637  0.35 18.12 ? 114 SER A CB  1 
ATOM   724  O OG  A SER A 1 97  ? 7.816   26.866 4.209  0.65 20.52 ? 114 SER A OG  1 
ATOM   725  O OG  B SER A 1 97  ? 7.043   25.649 5.304  0.35 16.56 ? 114 SER A OG  1 
ATOM   726  N N   . THR A 1 98  ? 3.700   27.290 5.906  1.00 17.13 ? 115 THR A N   1 
ATOM   727  C CA  . THR A 1 98  ? 2.504   26.791 6.574  1.00 17.51 ? 115 THR A CA  1 
ATOM   728  C C   . THR A 1 98  ? 2.698   25.382 7.110  1.00 15.74 ? 115 THR A C   1 
ATOM   729  O O   . THR A 1 98  ? 2.261   25.068 8.228  1.00 15.56 ? 115 THR A O   1 
ATOM   730  C CB  . THR A 1 98  ? 1.334   26.796 5.586  1.00 21.28 ? 115 THR A CB  1 
ATOM   731  O OG1 . THR A 1 98  ? 1.177   28.100 5.034  1.00 24.99 ? 115 THR A OG1 1 
ATOM   732  C CG2 . THR A 1 98  ? 0.057   26.404 6.291  1.00 23.38 ? 115 THR A CG2 1 
ATOM   733  N N   . ARG A 1 99  ? 3.306   24.509 6.320  1.00 16.50 ? 116 ARG A N   1 
ATOM   734  C CA  . ARG A 1 99  ? 3.620   23.161 6.746  1.00 17.40 ? 116 ARG A CA  1 
ATOM   735  C C   . ARG A 1 99  ? 4.945   23.157 7.480  1.00 15.93 ? 116 ARG A C   1 
ATOM   736  O O   . ARG A 1 99  ? 5.990   23.427 6.874  1.00 16.56 ? 116 ARG A O   1 
ATOM   737  C CB  . ARG A 1 99  ? 3.743   22.260 5.524  1.00 16.77 ? 116 ARG A CB  1 
ATOM   738  C CG  . ARG A 1 99  ? 2.435   22.027 4.850  1.00 18.78 ? 116 ARG A CG  1 
ATOM   739  C CD  . ARG A 1 99  ? 2.684   21.271 3.613  1.00 21.85 ? 116 ARG A CD  1 
ATOM   740  N NE  . ARG A 1 99  ? 1.453   20.733 3.079  1.00 27.02 ? 116 ARG A NE  1 
ATOM   741  C CZ  . ARG A 1 99  ? 1.322   20.321 1.832  1.00 29.89 ? 116 ARG A CZ  1 
ATOM   742  N NH1 . ARG A 1 99  ? 2.315   20.434 0.966  1.00 28.43 ? 116 ARG A NH1 1 
ATOM   743  N NH2 . ARG A 1 99  ? 0.169   19.791 1.445  1.00 30.57 ? 116 ARG A NH2 1 
ATOM   744  N N   . PRO A 1 100 ? 4.954   22.843 8.782  1.00 15.59 ? 117 PRO A N   1 
ATOM   745  C CA  . PRO A 1 100 ? 6.231   22.807 9.515  1.00 15.40 ? 117 PRO A CA  1 
ATOM   746  C C   . PRO A 1 100 ? 7.276   21.928 8.857  1.00 13.95 ? 117 PRO A C   1 
ATOM   747  O O   . PRO A 1 100 ? 8.470   22.239 8.938  1.00 15.03 ? 117 PRO A O   1 
ATOM   748  C CB  . PRO A 1 100 ? 5.807   22.278 10.897 1.00 15.68 ? 117 PRO A CB  1 
ATOM   749  C CG  . PRO A 1 100 ? 4.407   22.794 11.048 1.00 15.37 ? 117 PRO A CG  1 
ATOM   750  C CD  . PRO A 1 100 ? 3.797   22.647 9.673  1.00 14.51 ? 117 PRO A CD  1 
ATOM   751  N N   . GLY A 1 101 ? 6.858   20.838 8.208  1.00 14.59 ? 118 GLY A N   1 
ATOM   752  C CA  . GLY A 1 101 ? 7.807   19.941 7.566  1.00 17.10 ? 118 GLY A CA  1 
ATOM   753  C C   . GLY A 1 101 ? 8.497   20.539 6.359  1.00 15.20 ? 118 GLY A C   1 
ATOM   754  O O   . GLY A 1 101 ? 9.550   20.041 5.957  1.00 16.42 ? 118 GLY A O   1 
ATOM   755  N N   . GLU A 1 102 ? 7.930   21.601 5.781  1.00 15.86 ? 119 GLU A N   1 
ATOM   756  C CA  . GLU A 1 102 ? 8.561   22.314 4.678  1.00 15.77 ? 119 GLU A CA  1 
ATOM   757  C C   . GLU A 1 102 ? 9.287   23.572 5.126  1.00 16.96 ? 119 GLU A C   1 
ATOM   758  O O   . GLU A 1 102 ? 10.005  24.178 4.323  1.00 18.48 ? 119 GLU A O   1 
ATOM   759  C CB  . GLU A 1 102 ? 7.496   22.715 3.644  1.00 16.27 ? 119 GLU A CB  1 
ATOM   760  C CG  . GLU A 1 102 ? 6.767   21.535 3.054  1.00 16.85 ? 119 GLU A CG  1 
ATOM   761  C CD  . GLU A 1 102 ? 5.697   21.933 2.056  1.00 19.74 ? 119 GLU A CD  1 
ATOM   762  O OE1 . GLU A 1 102 ? 5.312   23.133 2.012  1.00 20.49 ? 119 GLU A OE1 1 
ATOM   763  O OE2 . GLU A 1 102 ? 5.235   21.028 1.325  1.00 20.99 ? 119 GLU A OE2 1 
ATOM   764  N N   . ALA A 1 103 ? 9.101   23.986 6.371  1.00 15.75 ? 120 ALA A N   1 
ATOM   765  C CA  . ALA A 1 103 ? 9.636   25.251 6.844  1.00 15.32 ? 120 ALA A CA  1 
ATOM   766  C C   . ALA A 1 103 ? 11.143  25.142 7.052  1.00 16.64 ? 120 ALA A C   1 
ATOM   767  O O   . ALA A 1 103 ? 11.678  24.077 7.362  1.00 17.74 ? 120 ALA A O   1 
ATOM   768  C CB  . ALA A 1 103 ? 8.932   25.654 8.145  1.00 16.48 ? 120 ALA A CB  1 
ATOM   769  N N   . ALA A 1 104 ? 11.832  26.269 6.875  1.00 18.74 ? 121 ALA A N   1 
ATOM   770  C CA  . ALA A 1 104 ? 13.286  26.277 6.979  1.00 19.92 ? 121 ALA A CA  1 
ATOM   771  C C   . ALA A 1 104 ? 13.722  26.081 8.428  1.00 18.22 ? 121 ALA A C   1 
ATOM   772  O O   . ALA A 1 104 ? 13.097  26.609 9.354  1.00 18.45 ? 121 ALA A O   1 
ATOM   773  C CB  . ALA A 1 104 ? 13.835  27.607 6.461  1.00 21.38 ? 121 ALA A CB  1 
ATOM   774  N N   . PRO A 1 105 ? 14.799  25.343 8.674  1.00 22.43 ? 122 PRO A N   1 
ATOM   775  C CA  . PRO A 1 105 ? 15.295  25.268 10.050 1.00 23.74 ? 122 PRO A CA  1 
ATOM   776  C C   . PRO A 1 105 ? 15.588  26.667 10.557 1.00 18.08 ? 122 PRO A C   1 
ATOM   777  O O   . PRO A 1 105 ? 16.022  27.538 9.807  1.00 21.79 ? 122 PRO A O   1 
ATOM   778  C CB  . PRO A 1 105 ? 16.570  24.425 9.923  1.00 28.71 ? 122 PRO A CB  1 
ATOM   779  C CG  . PRO A 1 105 ? 16.324  23.585 8.727  1.00 31.01 ? 122 PRO A CG  1 
ATOM   780  C CD  . PRO A 1 105 ? 15.558  24.456 7.767  1.00 29.36 ? 122 PRO A CD  1 
ATOM   781  N N   . GLY A 1 106 ? 15.318  26.889 11.836 1.00 18.49 ? 123 GLY A N   1 
ATOM   782  C CA  . GLY A 1 106 ? 15.446  28.202 12.423 1.00 18.24 ? 123 GLY A CA  1 
ATOM   783  C C   . GLY A 1 106 ? 14.188  29.026 12.396 1.00 16.20 ? 123 GLY A C   1 
ATOM   784  O O   . GLY A 1 106 ? 14.146  30.098 13.030 1.00 18.97 ? 123 GLY A O   1 
ATOM   785  N N   . THR A 1 107 ? 13.158  28.579 11.684 1.00 14.75 ? 124 THR A N   1 
ATOM   786  C CA  . THR A 1 107 ? 11.876  29.252 11.746 1.00 14.10 ? 124 THR A CA  1 
ATOM   787  C C   . THR A 1 107 ? 11.044  28.674 12.879 1.00 14.61 ? 124 THR A C   1 
ATOM   788  O O   . THR A 1 107 ? 11.298  27.571 13.368 1.00 14.98 ? 124 THR A O   1 
ATOM   789  C CB  . THR A 1 107 ? 11.097  29.121 10.430 1.00 14.93 ? 124 THR A CB  1 
ATOM   790  O OG1 . THR A 1 107 ? 10.767  27.743 10.157 1.00 14.85 ? 124 THR A OG1 1 
ATOM   791  C CG2 . THR A 1 107 ? 11.886  29.678 9.283  1.00 13.85 ? 124 THR A CG2 1 
ATOM   792  N N   . ILE A 1 108 ? 10.025  29.432 13.284 1.00 15.91 ? 125 ILE A N   1 
ATOM   793  C CA  . ILE A 1 108 ? 9.184   29.010 14.408 1.00 14.99 ? 125 ILE A CA  1 
ATOM   794  C C   . ILE A 1 108 ? 8.520   27.676 14.103 1.00 15.39 ? 125 ILE A C   1 
ATOM   795  O O   . ILE A 1 108 ? 8.561   26.736 14.904 1.00 15.11 ? 125 ILE A O   1 
ATOM   796  C CB  . ILE A 1 108 ? 8.148   30.102 14.740 1.00 15.25 ? 125 ILE A CB  1 
ATOM   797  C CG1 . ILE A 1 108 ? 8.868   31.334 15.278 1.00 16.81 ? 125 ILE A CG1 1 
ATOM   798  C CG2 . ILE A 1 108 ? 7.088   29.597 15.726 1.00 15.28 ? 125 ILE A CG2 1 
ATOM   799  C CD1 . ILE A 1 108 ? 8.017   32.563 15.350 1.00 16.84 ? 125 ILE A CD1 1 
ATOM   800  N N   . ARG A 1 109 ? 7.911   27.563 12.922 1.00 13.88 ? 126 ARG A N   1 
ATOM   801  C CA  . ARG A 1 109 ? 7.171   26.346 12.613 1.00 14.63 ? 126 ARG A CA  1 
ATOM   802  C C   . ARG A 1 109 ? 8.085   25.138 12.499 1.00 13.50 ? 126 ARG A C   1 
ATOM   803  O O   . ARG A 1 109 ? 7.741   24.059 12.992 1.00 15.00 ? 126 ARG A O   1 
ATOM   804  C CB  . ARG A 1 109 ? 6.294   26.563 11.381 1.00 16.67 ? 126 ARG A CB  1 
ATOM   805  C CG  . ARG A 1 109 ? 5.165   27.552 11.712 1.00 15.76 ? 126 ARG A CG  1 
ATOM   806  C CD  . ARG A 1 109 ? 4.418   27.975 10.512 1.00 16.39 ? 126 ARG A CD  1 
ATOM   807  N NE  . ARG A 1 109 ? 3.285   28.828 10.827 1.00 16.03 ? 126 ARG A NE  1 
ATOM   808  C CZ  . ARG A 1 109 ? 2.601   29.488 9.906  1.00 18.33 ? 126 ARG A CZ  1 
ATOM   809  N NH1 . ARG A 1 109 ? 3.014   29.536 8.647  1.00 21.76 ? 126 ARG A NH1 1 
ATOM   810  N NH2 . ARG A 1 109 ? 1.460   30.079 10.241 1.00 20.69 ? 126 ARG A NH2 1 
ATOM   811  N N   . ALA A 1 110 ? 9.271   25.302 11.899 1.00 13.33 ? 127 ALA A N   1 
ATOM   812  C CA  . ALA A 1 110 ? 10.203  24.176 11.812 1.00 15.53 ? 127 ALA A CA  1 
ATOM   813  C C   . ALA A 1 110 ? 10.722  23.766 13.186 1.00 14.00 ? 127 ALA A C   1 
ATOM   814  O O   . ALA A 1 110 ? 10.961  22.579 13.436 1.00 16.70 ? 127 ALA A O   1 
ATOM   815  C CB  . ALA A 1 110 ? 11.398  24.528 10.930 1.00 16.30 ? 127 ALA A CB  1 
ATOM   816  N N   . ASP A 1 111 ? 10.943  24.740 14.070 1.00 14.01 ? 128 ASP A N   1 
ATOM   817  C CA  . ASP A 1 111 ? 11.588  24.461 15.340 1.00 14.93 ? 128 ASP A CA  1 
ATOM   818  C C   . ASP A 1 111 ? 10.621  23.882 16.357 1.00 13.83 ? 128 ASP A C   1 
ATOM   819  O O   . ASP A 1 111 ? 11.065  23.169 17.270 1.00 14.77 ? 128 ASP A O   1 
ATOM   820  C CB  . ASP A 1 111 ? 12.198  25.735 15.911 1.00 18.30 ? 128 ASP A CB  1 
ATOM   821  C CG  . ASP A 1 111 ? 13.467  26.186 15.169 1.00 18.97 ? 128 ASP A CG  1 
ATOM   822  O OD1 . ASP A 1 111 ? 14.022  25.433 14.332 1.00 22.47 ? 128 ASP A OD1 1 
ATOM   823  O OD2 . ASP A 1 111 ? 13.906  27.332 15.421 1.00 20.96 ? 128 ASP A OD2 1 
ATOM   824  N N   . PHE A 1 112 ? 9.319   24.151 16.207 1.00 14.30 ? 129 PHE A N   1 
ATOM   825  C CA  . PHE A 1 112 ? 8.338   23.794 17.219 1.00 13.70 ? 129 PHE A CA  1 
ATOM   826  C C   . PHE A 1 112 ? 7.276   22.787 16.779 1.00 14.17 ? 129 PHE A C   1 
ATOM   827  O O   . PHE A 1 112 ? 6.627   22.193 17.643 1.00 13.82 ? 129 PHE A O   1 
ATOM   828  C CB  . PHE A 1 112 ? 7.560   25.026 17.701 1.00 14.73 ? 129 PHE A CB  1 
ATOM   829  C CG  . PHE A 1 112 ? 8.316   25.974 18.590 1.00 14.06 ? 129 PHE A CG  1 
ATOM   830  C CD1 . PHE A 1 112 ? 8.981   27.071 18.056 1.00 15.87 ? 129 PHE A CD1 1 
ATOM   831  C CD2 . PHE A 1 112 ? 8.300   25.821 19.972 1.00 15.12 ? 129 PHE A CD2 1 
ATOM   832  C CE1 . PHE A 1 112 ? 9.620   27.989 18.868 1.00 17.43 ? 129 PHE A CE1 1 
ATOM   833  C CE2 . PHE A 1 112 ? 8.946   26.727 20.791 1.00 15.64 ? 129 PHE A CE2 1 
ATOM   834  C CZ  . PHE A 1 112 ? 9.615   27.818 20.239 1.00 15.85 ? 129 PHE A CZ  1 
ATOM   835  N N   . CYS A 1 113 ? 7.042   22.590 15.479 1.00 13.69 ? 130 CYS A N   1 
ATOM   836  C CA  . CYS A 1 113 ? 5.790   21.976 15.041 1.00 13.01 ? 130 CYS A CA  1 
ATOM   837  C C   . CYS A 1 113 ? 6.029   20.823 14.073 1.00 13.92 ? 130 CYS A C   1 
ATOM   838  O O   . CYS A 1 113 ? 7.133   20.617 13.572 1.00 14.62 ? 130 CYS A O   1 
ATOM   839  C CB  . CYS A 1 113 ? 4.856   23.040 14.419 1.00 14.17 ? 130 CYS A CB  1 
ATOM   840  S SG  . CYS A 1 113 ? 4.404   24.327 15.605 1.00 14.91 ? 130 CYS A SG  1 
ATOM   841  N N   . GLN A 1 114 ? 4.948   20.082 13.810 1.00 14.05 ? 131 GLN A N   1 
ATOM   842  C CA  . GLN A 1 114 ? 4.933   18.935 12.900 1.00 13.32 ? 131 GLN A CA  1 
ATOM   843  C C   . GLN A 1 114 ? 3.961   19.066 11.742 1.00 14.05 ? 131 GLN A C   1 
ATOM   844  O O   . GLN A 1 114 ? 4.287   18.665 10.621 1.00 16.77 ? 131 GLN A O   1 
ATOM   845  C CB  . GLN A 1 114 ? 4.575   17.654 13.675 1.00 15.24 ? 131 GLN A CB  1 
ATOM   846  C CG  . GLN A 1 114 ? 5.631   17.270 14.704 1.00 15.29 ? 131 GLN A CG  1 
ATOM   847  C CD  . GLN A 1 114 ? 5.350   15.945 15.344 1.00 14.40 ? 131 GLN A CD  1 
ATOM   848  O OE1 . GLN A 1 114 ? 5.000   14.971 14.672 1.00 16.09 ? 131 GLN A OE1 1 
ATOM   849  N NE2 . GLN A 1 114 ? 5.493   15.895 16.665 1.00 16.04 ? 131 GLN A NE2 1 
ATOM   850  N N   . GLN A 1 115 ? 2.770   19.615 11.978 1.00 15.76 ? 132 GLN A N   1 
ATOM   851  C CA  . GLN A 1 115 ? 1.707   19.619 10.979 1.00 15.50 ? 132 GLN A CA  1 
ATOM   852  C C   . GLN A 1 115 ? 1.082   20.994 10.815 1.00 15.93 ? 132 GLN A C   1 
ATOM   853  O O   . GLN A 1 115 ? 1.036   21.788 11.749 1.00 15.73 ? 132 GLN A O   1 
ATOM   854  C CB  . GLN A 1 115 ? 0.606   18.618 11.334 1.00 16.78 ? 132 GLN A CB  1 
ATOM   855  C CG  . GLN A 1 115 ? 1.157   17.214 11.447 1.00 18.52 ? 132 GLN A CG  1 
ATOM   856  C CD  . GLN A 1 115 ? 0.068   16.166 11.512 1.00 19.85 ? 132 GLN A CD  1 
ATOM   857  O OE1 . GLN A 1 115 ? -0.558  15.966 12.547 1.00 22.01 ? 132 GLN A OE1 1 
ATOM   858  N NE2 . GLN A 1 115 ? -0.156  15.483 10.400 1.00 22.34 ? 132 GLN A NE2 1 
ATOM   859  N N   . ALA A 1 116 ? 0.559   21.244 9.607  1.00 16.41 ? 133 ALA A N   1 
ATOM   860  C CA  . ALA A 1 116 ? -0.018  22.546 9.282  1.00 16.61 ? 133 ALA A CA  1 
ATOM   861  C C   . ALA A 1 116 ? -1.199  22.900 10.176 1.00 18.84 ? 133 ALA A C   1 
ATOM   862  O O   . ALA A 1 116 ? -1.407  24.075 10.482 1.00 19.85 ? 133 ALA A O   1 
ATOM   863  C CB  . ALA A 1 116 ? -0.457  22.584 7.815  1.00 18.75 ? 133 ALA A CB  1 
ATOM   864  N N   . GLY A 1 117 ? -1.991  21.915 10.588 1.00 17.76 ? 134 GLY A N   1 
ATOM   865  C CA  . GLY A 1 117 ? -3.134  22.235 11.424 1.00 18.58 ? 134 GLY A CA  1 
ATOM   866  C C   . GLY A 1 117 ? -2.791  22.595 12.853 1.00 17.33 ? 134 GLY A C   1 
ATOM   867  O O   . GLY A 1 117 ? -3.673  23.077 13.573 1.00 19.08 ? 134 GLY A O   1 
ATOM   868  N N   . ARG A 1 118 ? -1.554  22.366 13.283 1.00 15.84 ? 135 ARG A N   1 
ATOM   869  C CA  . ARG A 1 118 ? -1.065  22.842 14.582 1.00 14.69 ? 135 ARG A CA  1 
ATOM   870  C C   . ARG A 1 118 ? 0.285   23.507 14.333 1.00 15.16 ? 135 ARG A C   1 
ATOM   871  O O   . ARG A 1 118 ? 1.343   22.949 14.645 1.00 15.37 ? 135 ARG A O   1 
ATOM   872  C CB  . ARG A 1 118 ? -0.964  21.671 15.582 1.00 15.76 ? 135 ARG A CB  1 
ATOM   873  C CG  . ARG A 1 118 ? -2.329  21.124 16.041 1.00 16.27 ? 135 ARG A CG  1 
ATOM   874  C CD  . ARG A 1 118 ? -3.120  22.207 16.773 1.00 17.66 ? 135 ARG A CD  1 
ATOM   875  N NE  . ARG A 1 118 ? -4.268  21.698 17.510 1.00 19.00 ? 135 ARG A NE  1 
ATOM   876  C CZ  . ARG A 1 118 ? -5.221  22.461 18.027 1.00 20.66 ? 135 ARG A CZ  1 
ATOM   877  N NH1 . ARG A 1 118 ? -5.198  23.775 17.899 1.00 21.40 ? 135 ARG A NH1 1 
ATOM   878  N NH2 . ARG A 1 118 ? -6.221  21.894 18.696 1.00 21.70 ? 135 ARG A NH2 1 
ATOM   879  N N   . ASN A 1 119 ? 0.246   24.738 13.824 1.00 14.96 ? 136 ASN A N   1 
ATOM   880  C CA  . ASN A 1 119 ? 1.467   25.425 13.430 1.00 14.42 ? 136 ASN A CA  1 
ATOM   881  C C   . ASN A 1 119 ? 1.699   26.724 14.199 1.00 15.07 ? 136 ASN A C   1 
ATOM   882  O O   . ASN A 1 119 ? 2.356   27.636 13.700 1.00 15.64 ? 136 ASN A O   1 
ATOM   883  C CB  . ASN A 1 119 ? 1.535   25.610 11.909 1.00 16.22 ? 136 ASN A CB  1 
ATOM   884  C CG  . ASN A 1 119 ? 0.508   26.559 11.382 1.00 17.76 ? 136 ASN A CG  1 
ATOM   885  O OD1 . ASN A 1 119 ? -0.298  27.097 12.126 1.00 17.12 ? 136 ASN A OD1 1 
ATOM   886  N ND2 . ASN A 1 119 ? 0.550   26.797 10.073 1.00 19.30 ? 136 ASN A ND2 1 
ATOM   887  N N   . LEU A 1 120 ? 1.148   26.801 15.414 1.00 15.15 ? 137 LEU A N   1 
ATOM   888  C CA  . LEU A 1 120 ? 1.538   27.661 16.528 1.00 14.10 ? 137 LEU A CA  1 
ATOM   889  C C   . LEU A 1 120 ? 1.219   29.147 16.430 1.00 13.88 ? 137 LEU A C   1 
ATOM   890  O O   . LEU A 1 120 ? 0.906   29.777 17.452 1.00 14.20 ? 137 LEU A O   1 
ATOM   891  C CB  . LEU A 1 120 ? 3.069   27.613 16.719 1.00 14.73 ? 137 LEU A CB  1 
ATOM   892  C CG  . LEU A 1 120 ? 3.556   27.576 18.166 1.00 15.43 ? 137 LEU A CG  1 
ATOM   893  C CD1 . LEU A 1 120 ? 3.211   26.235 18.814 1.00 15.59 ? 137 LEU A CD1 1 
ATOM   894  C CD2 . LEU A 1 120 ? 5.054   27.814 18.206 1.00 14.74 ? 137 LEU A CD2 1 
ATOM   895  N N   . ILE A 1 121 ? 1.137   29.702 15.225 1.00 14.12 ? 138 ILE A N   1 
ATOM   896  C CA  . ILE A 1 121 ? 1.182   31.152 15.090 1.00 13.64 ? 138 ILE A CA  1 
ATOM   897  C C   . ILE A 1 121 ? 0.615   31.541 13.745 1.00 14.05 ? 138 ILE A C   1 
ATOM   898  O O   . ILE A 1 121 ? 0.777   30.819 12.764 1.00 14.90 ? 138 ILE A O   1 
ATOM   899  C CB  . ILE A 1 121 ? 2.627   31.702 15.288 1.00 14.79 ? 138 ILE A CB  1 
ATOM   900  C CG1 . ILE A 1 121 ? 2.619   33.223 15.301 1.00 15.94 ? 138 ILE A CG1 1 
ATOM   901  C CG2 . ILE A 1 121 ? 3.584   31.142 14.231 1.00 16.64 ? 138 ILE A CG2 1 
ATOM   902  C CD1 . ILE A 1 121 ? 3.864   33.862 15.838 1.00 15.49 ? 138 ILE A CD1 1 
ATOM   903  N N   . HIS A 1 122 ? -0.061  32.694 13.713 1.00 13.08 ? 139 HIS A N   1 
ATOM   904  C CA  . HIS A 1 122 ? -0.533  33.357 12.502 1.00 14.20 ? 139 HIS A CA  1 
ATOM   905  C C   . HIS A 1 122 ? 0.161   34.708 12.356 1.00 13.89 ? 139 HIS A C   1 
ATOM   906  O O   . HIS A 1 122 ? 0.407   35.393 13.351 1.00 14.25 ? 139 HIS A O   1 
ATOM   907  C CB  . HIS A 1 122 ? -2.032  33.668 12.636 1.00 14.90 ? 139 HIS A CB  1 
ATOM   908  C CG  . HIS A 1 122 ? -2.519  34.687 11.658 1.00 17.95 ? 139 HIS A CG  1 
ATOM   909  N ND1 . HIS A 1 122 ? -2.955  34.356 10.393 1.00 21.22 ? 139 HIS A ND1 1 
ATOM   910  C CD2 . HIS A 1 122 ? -2.598  36.035 11.742 1.00 15.53 ? 139 HIS A CD2 1 
ATOM   911  C CE1 . HIS A 1 122 ? -3.289  35.456 9.745  1.00 21.25 ? 139 HIS A CE1 1 
ATOM   912  N NE2 . HIS A 1 122 ? -3.077  36.493 10.535 1.00 17.96 ? 139 HIS A NE2 1 
ATOM   913  N N   . GLY A 1 123 ? 0.456   35.103 11.128 1.00 15.94 ? 140 GLY A N   1 
ATOM   914  C CA  . GLY A 1 123 ? 0.906   36.458 10.852 1.00 14.18 ? 140 GLY A CA  1 
ATOM   915  C C   . GLY A 1 123 ? 0.282   36.967 9.569  1.00 13.72 ? 140 GLY A C   1 
ATOM   916  O O   . GLY A 1 123 ? 0.014   36.203 8.640  1.00 17.62 ? 140 GLY A O   1 
ATOM   917  N N   . SER A 1 124 ? 0.046   38.279 9.531  1.00 15.06 ? 141 SER A N   1 
ATOM   918  C CA  . SER A 1 124 ? -0.574  38.883 8.356  1.00 15.27 ? 141 SER A CA  1 
ATOM   919  C C   . SER A 1 124 ? 0.265   38.611 7.118  1.00 16.93 ? 141 SER A C   1 
ATOM   920  O O   . SER A 1 124 ? 1.494   38.619 7.171  1.00 17.35 ? 141 SER A O   1 
ATOM   921  C CB  . SER A 1 124 ? -0.678  40.394 8.534  1.00 15.54 ? 141 SER A CB  1 
ATOM   922  O OG  . SER A 1 124 ? -1.317  40.734 9.738  1.00 17.13 ? 141 SER A OG  1 
ATOM   923  N N   . ASP A 1 125 ? -0.400  38.401 5.985  1.00 18.32 ? 142 ASP A N   1 
ATOM   924  C CA  . ASP A 1 125 ? 0.314   38.055 4.760  1.00 19.94 ? 142 ASP A CA  1 
ATOM   925  C C   . ASP A 1 125 ? 0.612   39.250 3.848  1.00 21.18 ? 142 ASP A C   1 
ATOM   926  O O   . ASP A 1 125 ? 1.302   39.073 2.841  1.00 24.14 ? 142 ASP A O   1 
ATOM   927  C CB  . ASP A 1 125 ? -0.410  36.934 3.987  1.00 24.35 ? 142 ASP A CB  1 
ATOM   928  C CG  . ASP A 1 125 ? -1.751  37.360 3.417  1.00 28.56 ? 142 ASP A CG  1 
ATOM   929  O OD1 . ASP A 1 125 ? -2.137  38.537 3.539  1.00 27.78 ? 142 ASP A OD1 1 
ATOM   930  O OD2 . ASP A 1 125 ? -2.427  36.496 2.817  1.00 32.97 ? 142 ASP A OD2 1 
ATOM   931  N N   . SER A 1 126 ? 0.133   40.452 4.173  1.00 19.25 ? 143 SER A N   1 
ATOM   932  C CA  . SER A 1 126 ? 0.266   41.601 3.283  1.00 19.17 ? 143 SER A CA  1 
ATOM   933  C C   . SER A 1 126 ? -0.084  42.862 4.061  1.00 18.22 ? 143 SER A C   1 
ATOM   934  O O   . SER A 1 126 ? -0.644  42.804 5.154  1.00 19.06 ? 143 SER A O   1 
ATOM   935  C CB  . SER A 1 126 ? -0.682  41.475 2.091  1.00 22.87 ? 143 SER A CB  1 
ATOM   936  O OG  . SER A 1 126 ? -2.005  41.635 2.550  1.00 24.19 ? 143 SER A OG  1 
ATOM   937  N N   . ALA A 1 127 ? 0.244   44.015 3.475  1.00 20.33 ? 144 ALA A N   1 
ATOM   938  C CA  . ALA A 1 127 ? -0.123  45.283 4.095  1.00 19.55 ? 144 ALA A CA  1 
ATOM   939  C C   . ALA A 1 127 ? -1.623  45.375 4.329  1.00 20.44 ? 144 ALA A C   1 
ATOM   940  O O   . ALA A 1 127 ? -2.074  45.844 5.376  1.00 22.24 ? 144 ALA A O   1 
ATOM   941  C CB  . ALA A 1 127 ? 0.315   46.433 3.194  1.00 21.77 ? 144 ALA A CB  1 
ATOM   942  N N   . GLU A 1 128 ? -2.415  44.968 3.343  1.00 20.78 ? 145 GLU A N   1 
ATOM   943  C CA  . GLU A 1 128 ? -3.860  45.099 3.454  1.00 21.88 ? 145 GLU A CA  1 
ATOM   944  C C   . GLU A 1 128 ? -4.420  44.169 4.521  1.00 20.31 ? 145 GLU A C   1 
ATOM   945  O O   . GLU A 1 128 ? -5.312  44.561 5.287  1.00 22.08 ? 145 GLU A O   1 
ATOM   946  C CB  . GLU A 1 128 ? -4.483  44.852 2.081  1.00 26.05 ? 145 GLU A CB  1 
ATOM   947  C CG  . GLU A 1 128 ? -4.054  45.908 1.039  1.00 33.36 ? 145 GLU A CG  1 
ATOM   948  C CD  . GLU A 1 128 ? -2.746  45.568 0.278  1.00 36.95 ? 145 GLU A CD  1 
ATOM   949  O OE1 . GLU A 1 128 ? -2.014  44.603 0.647  1.00 32.87 ? 145 GLU A OE1 1 
ATOM   950  O OE2 . GLU A 1 128 ? -2.450  46.276 -0.706 1.00 43.68 ? 145 GLU A OE2 1 
ATOM   951  N N   . SER A 1 129 ? -3.907  42.937 4.601  1.00 18.68 ? 146 SER A N   1 
ATOM   952  C CA  A SER A 1 129 ? -4.400  42.031 5.631  0.52 17.88 ? 146 SER A CA  1 
ATOM   953  C CA  B SER A 1 129 ? -4.364  42.006 5.628  0.48 17.53 ? 146 SER A CA  1 
ATOM   954  C C   . SER A 1 129 ? -3.934  42.455 7.015  1.00 18.88 ? 146 SER A C   1 
ATOM   955  O O   . SER A 1 129 ? -4.671  42.283 7.984  1.00 18.65 ? 146 SER A O   1 
ATOM   956  C CB  A SER A 1 129 ? -4.023  40.579 5.330  0.52 20.58 ? 146 SER A CB  1 
ATOM   957  C CB  B SER A 1 129 ? -3.840  40.602 5.334  0.48 20.07 ? 146 SER A CB  1 
ATOM   958  O OG  A SER A 1 129 ? -2.631  40.420 5.210  0.52 21.30 ? 146 SER A OG  1 
ATOM   959  O OG  B SER A 1 129 ? -4.418  40.112 4.143  0.48 21.23 ? 146 SER A OG  1 
ATOM   960  N N   . ALA A 1 130 ? -2.738  43.026 7.128  1.00 18.18 ? 147 ALA A N   1 
ATOM   961  C CA  . ALA A 1 130 ? -2.315  43.545 8.421  1.00 16.93 ? 147 ALA A CA  1 
ATOM   962  C C   . ALA A 1 130 ? -3.251  44.654 8.903  1.00 18.13 ? 147 ALA A C   1 
ATOM   963  O O   . ALA A 1 130 ? -3.655  44.676 10.075 1.00 18.99 ? 147 ALA A O   1 
ATOM   964  C CB  . ALA A 1 130 ? -0.876  44.071 8.328  1.00 17.10 ? 147 ALA A CB  1 
ATOM   965  N N   . LYS A 1 131 ? -3.616  45.580 8.021  1.00 18.65 ? 148 LYS A N   1 
ATOM   966  C CA  . LYS A 1 131 ? -4.500  46.662 8.437  1.00 19.36 ? 148 LYS A CA  1 
ATOM   967  C C   . LYS A 1 131 ? -5.846  46.100 8.875  1.00 18.48 ? 148 LYS A C   1 
ATOM   968  O O   . LYS A 1 131 ? -6.388  46.479 9.919  1.00 19.35 ? 148 LYS A O   1 
ATOM   969  C CB  . LYS A 1 131 ? -4.666  47.664 7.292  1.00 23.90 ? 148 LYS A CB  1 
ATOM   970  C CG  . LYS A 1 131 ? -5.444  48.913 7.688  1.00 34.44 ? 148 LYS A CG  1 
ATOM   971  C CD  . LYS A 1 131 ? -5.575  49.886 6.514  1.00 41.80 ? 148 LYS A CD  1 
ATOM   972  C CE  . LYS A 1 131 ? -6.124  51.248 6.964  1.00 49.05 ? 148 LYS A CE  1 
ATOM   973  N NZ  . LYS A 1 131 ? -7.426  51.138 7.670  1.00 52.14 ? 148 LYS A NZ  1 
ATOM   974  N N   . ARG A 1 132 ? -6.381  45.158 8.105  1.00 18.51 ? 149 ARG A N   1 
ATOM   975  C CA  . ARG A 1 132 ? -7.688  44.607 8.416  1.00 19.00 ? 149 ARG A CA  1 
ATOM   976  C C   . ARG A 1 132 ? -7.658  43.782 9.694  1.00 17.57 ? 149 ARG A C   1 
ATOM   977  O O   . ARG A 1 132 ? -8.567  43.884 10.524 1.00 20.07 ? 149 ARG A O   1 
ATOM   978  C CB  . ARG A 1 132 ? -8.137  43.755 7.236  1.00 21.46 ? 149 ARG A CB  1 
ATOM   979  C CG  . ARG A 1 132 ? -9.522  43.165 7.371  1.00 23.72 ? 149 ARG A CG  1 
ATOM   980  C CD  . ARG A 1 132 ? -9.843  42.299 6.165  1.00 29.40 ? 149 ARG A CD  1 
ATOM   981  N NE  . ARG A 1 132 ? -9.360  40.948 6.381  1.00 32.96 ? 149 ARG A NE  1 
ATOM   982  C CZ  . ARG A 1 132 ? -9.981  40.069 7.160  1.00 38.92 ? 149 ARG A CZ  1 
ATOM   983  N NH1 . ARG A 1 132 ? -11.109 40.372 7.786  1.00 39.35 ? 149 ARG A NH1 1 
ATOM   984  N NH2 . ARG A 1 132 ? -9.449  38.871 7.335  1.00 39.16 ? 149 ARG A NH2 1 
ATOM   985  N N   . GLU A 1 133 ? -6.623  42.959 9.865  1.00 17.86 ? 150 GLU A N   1 
ATOM   986  C CA  . GLU A 1 133 ? -6.543  42.097 11.039 1.00 16.82 ? 150 GLU A CA  1 
ATOM   987  C C   . GLU A 1 133 ? -6.299  42.898 12.305 1.00 17.53 ? 150 GLU A C   1 
ATOM   988  O O   . GLU A 1 133 ? -6.900  42.611 13.344 1.00 17.74 ? 150 GLU A O   1 
ATOM   989  C CB  . GLU A 1 133 ? -5.454  41.044 10.833 1.00 16.37 ? 150 GLU A CB  1 
ATOM   990  C CG  . GLU A 1 133 ? -5.817  40.049 9.750  1.00 16.57 ? 150 GLU A CG  1 
ATOM   991  C CD  . GLU A 1 133 ? -4.706  39.094 9.383  1.00 17.13 ? 150 GLU A CD  1 
ATOM   992  O OE1 . GLU A 1 133 ? -3.603  39.180 9.971  1.00 18.87 ? 150 GLU A OE1 1 
ATOM   993  O OE2 . GLU A 1 133 ? -4.955  38.240 8.496  1.00 18.75 ? 150 GLU A OE2 1 
ATOM   994  N N   . ILE A 1 134 ? -5.429  43.912 12.237 1.00 17.91 ? 151 ILE A N   1 
ATOM   995  C CA  . ILE A 1 134 ? -5.218  44.752 13.412 1.00 18.36 ? 151 ILE A CA  1 
ATOM   996  C C   . ILE A 1 134 ? -6.536  45.398 13.822 1.00 17.70 ? 151 ILE A C   1 
ATOM   997  O O   . ILE A 1 134 ? -6.877  45.442 15.003 1.00 19.91 ? 151 ILE A O   1 
ATOM   998  C CB  . ILE A 1 134 ? -4.108  45.786 13.158 1.00 19.29 ? 151 ILE A CB  1 
ATOM   999  C CG1 . ILE A 1 134 ? -2.757  45.073 13.053 1.00 18.82 ? 151 ILE A CG1 1 
ATOM   1000 C CG2 . ILE A 1 134 ? -4.068  46.797 14.253 1.00 18.59 ? 151 ILE A CG2 1 
ATOM   1001 C CD1 . ILE A 1 134 ? -1.596  45.958 12.618 1.00 19.42 ? 151 ILE A CD1 1 
ATOM   1002 N N   . SER A 1 135 ? -7.307  45.888 12.851 1.00 20.27 ? 152 SER A N   1 
ATOM   1003 C CA  . SER A 1 135 ? -8.575  46.537 13.164 1.00 23.67 ? 152 SER A CA  1 
ATOM   1004 C C   . SER A 1 135 ? -9.619  45.561 13.693 1.00 21.81 ? 152 SER A C   1 
ATOM   1005 O O   . SER A 1 135 ? -10.484 45.955 14.481 1.00 24.05 ? 152 SER A O   1 
ATOM   1006 C CB  . SER A 1 135 ? -9.105  47.256 11.931 1.00 31.71 ? 152 SER A CB  1 
ATOM   1007 O OG  . SER A 1 135 ? -8.277  48.367 11.635 1.00 39.71 ? 152 SER A OG  1 
ATOM   1008 N N   . LEU A 1 136 ? -9.576  44.302 13.254 1.00 20.28 ? 153 LEU A N   1 
ATOM   1009 C CA  . LEU A 1 136 ? -10.542 43.315 13.717 1.00 19.37 ? 153 LEU A CA  1 
ATOM   1010 C C   . LEU A 1 136 ? -10.328 42.975 15.186 1.00 19.81 ? 153 LEU A C   1 
ATOM   1011 O O   . LEU A 1 136 ? -11.284 42.912 15.969 1.00 23.04 ? 153 LEU A O   1 
ATOM   1012 C CB  . LEU A 1 136 ? -10.417 42.047 12.874 1.00 20.65 ? 153 LEU A CB  1 
ATOM   1013 C CG  . LEU A 1 136 ? -11.274 40.851 13.275 1.00 21.44 ? 153 LEU A CG  1 
ATOM   1014 C CD1 . LEU A 1 136 ? -12.750 41.223 13.236 1.00 25.51 ? 153 LEU A CD1 1 
ATOM   1015 C CD2 . LEU A 1 136 ? -11.029 39.667 12.344 1.00 21.44 ? 153 LEU A CD2 1 
ATOM   1016 N N   . TRP A 1 137 ? -9.072  42.735 15.574 1.00 17.59 ? 154 TRP A N   1 
ATOM   1017 C CA  . TRP A 1 137 ? -8.759  42.212 16.895 1.00 16.70 ? 154 TRP A CA  1 
ATOM   1018 C C   . TRP A 1 137 ? -8.471  43.295 17.934 1.00 18.57 ? 154 TRP A C   1 
ATOM   1019 O O   . TRP A 1 137 ? -8.510  43.001 19.138 1.00 18.76 ? 154 TRP A O   1 
ATOM   1020 C CB  . TRP A 1 137 ? -7.560  41.270 16.806 1.00 16.86 ? 154 TRP A CB  1 
ATOM   1021 C CG  . TRP A 1 137 ? -7.831  40.007 16.029 1.00 17.03 ? 154 TRP A CG  1 
ATOM   1022 C CD1 . TRP A 1 137 ? -7.575  39.784 14.701 1.00 16.20 ? 154 TRP A CD1 1 
ATOM   1023 C CD2 . TRP A 1 137 ? -8.368  38.778 16.545 1.00 16.41 ? 154 TRP A CD2 1 
ATOM   1024 N NE1 . TRP A 1 137 ? -7.928  38.497 14.366 1.00 16.11 ? 154 TRP A NE1 1 
ATOM   1025 C CE2 . TRP A 1 137 ? -8.423  37.865 15.478 1.00 15.69 ? 154 TRP A CE2 1 
ATOM   1026 C CE3 . TRP A 1 137 ? -8.808  38.361 17.809 1.00 16.20 ? 154 TRP A CE3 1 
ATOM   1027 C CZ2 . TRP A 1 137 ? -8.876  36.557 15.639 1.00 17.03 ? 154 TRP A CZ2 1 
ATOM   1028 C CZ3 . TRP A 1 137 ? -9.273  37.081 17.959 1.00 18.94 ? 154 TRP A CZ3 1 
ATOM   1029 C CH2 . TRP A 1 137 ? -9.304  36.188 16.885 1.00 18.35 ? 154 TRP A CH2 1 
ATOM   1030 N N   . PHE A 1 138 ? -8.159  44.524 17.508 1.00 17.41 ? 155 PHE A N   1 
ATOM   1031 C CA  . PHE A 1 138 ? -7.808  45.602 18.424 1.00 17.33 ? 155 PHE A CA  1 
ATOM   1032 C C   . PHE A 1 138 ? -8.595  46.864 18.101 1.00 22.95 ? 155 PHE A C   1 
ATOM   1033 O O   . PHE A 1 138 ? -8.752  47.226 16.939 1.00 29.09 ? 155 PHE A O   1 
ATOM   1034 C CB  . PHE A 1 138 ? -6.308  45.956 18.333 1.00 18.06 ? 155 PHE A CB  1 
ATOM   1035 C CG  . PHE A 1 138 ? -5.383  44.930 18.931 1.00 16.21 ? 155 PHE A CG  1 
ATOM   1036 C CD1 . PHE A 1 138 ? -5.207  44.858 20.304 1.00 16.27 ? 155 PHE A CD1 1 
ATOM   1037 C CD2 . PHE A 1 138 ? -4.685  44.045 18.125 1.00 16.35 ? 155 PHE A CD2 1 
ATOM   1038 C CE1 . PHE A 1 138 ? -4.356  43.940 20.864 1.00 16.03 ? 155 PHE A CE1 1 
ATOM   1039 C CE2 . PHE A 1 138 ? -3.820  43.110 18.687 1.00 15.37 ? 155 PHE A CE2 1 
ATOM   1040 C CZ  . PHE A 1 138 ? -3.650  43.070 20.060 1.00 16.33 ? 155 PHE A CZ  1 
ATOM   1041 N N   . LYS A 1 139 ? -9.036  47.546 19.132 1.00 21.12 ? 156 LYS A N   1 
ATOM   1042 C CA  . LYS A 1 139 ? -9.521  48.910 19.013 1.00 22.23 ? 156 LYS A CA  1 
ATOM   1043 C C   . LYS A 1 139 ? -8.320  49.848 18.929 1.00 20.00 ? 156 LYS A C   1 
ATOM   1044 O O   . LYS A 1 139 ? -7.244  49.526 19.440 1.00 20.85 ? 156 LYS A O   1 
ATOM   1045 C CB  . LYS A 1 139 ? -10.328 49.283 20.254 1.00 24.94 ? 156 LYS A CB  1 
ATOM   1046 C CG  . LYS A 1 139 ? -11.428 48.301 20.665 1.00 32.74 ? 156 LYS A CG  1 
ATOM   1047 C CD  . LYS A 1 139 ? -11.920 48.628 22.080 1.00 40.90 ? 156 LYS A CD  1 
ATOM   1048 C CE  . LYS A 1 139 ? -12.654 47.467 22.734 1.00 49.66 ? 156 LYS A CE  1 
ATOM   1049 N NZ  . LYS A 1 139 ? -14.013 47.282 22.152 1.00 54.24 ? 156 LYS A NZ  1 
ATOM   1050 N N   . PRO A 1 140 ? -8.471  51.018 18.304 1.00 21.65 ? 157 PRO A N   1 
ATOM   1051 C CA  . PRO A 1 140 ? -7.320  51.933 18.205 1.00 22.21 ? 157 PRO A CA  1 
ATOM   1052 C C   . PRO A 1 140 ? -6.719  52.304 19.552 1.00 21.80 ? 157 PRO A C   1 
ATOM   1053 O O   . PRO A 1 140 ? -5.499  52.464 19.654 1.00 21.95 ? 157 PRO A O   1 
ATOM   1054 C CB  . PRO A 1 140 ? -7.899  53.149 17.466 1.00 25.58 ? 157 PRO A CB  1 
ATOM   1055 C CG  . PRO A 1 140 ? -9.035  52.609 16.695 1.00 27.33 ? 157 PRO A CG  1 
ATOM   1056 C CD  . PRO A 1 140 ? -9.617  51.485 17.507 1.00 25.68 ? 157 PRO A CD  1 
ATOM   1057 N N   . GLU A 1 141 ? -7.534  52.430 20.596 1.00 22.11 ? 158 GLU A N   1 
ATOM   1058 C CA  . GLU A 1 141 ? -7.012  52.802 21.907 1.00 21.76 ? 158 GLU A CA  1 
ATOM   1059 C C   . GLU A 1 141 ? -6.130  51.724 22.518 1.00 19.65 ? 158 GLU A C   1 
ATOM   1060 O O   . GLU A 1 141 ? -5.453  51.998 23.514 1.00 21.78 ? 158 GLU A O   1 
ATOM   1061 C CB  . GLU A 1 141 ? -8.160  53.135 22.861 1.00 28.27 ? 158 GLU A CB  1 
ATOM   1062 C CG  . GLU A 1 141 ? -9.177  52.032 23.008 1.00 36.13 ? 158 GLU A CG  1 
ATOM   1063 C CD  . GLU A 1 141 ? -10.486 52.310 22.247 1.00 41.38 ? 158 GLU A CD  1 
ATOM   1064 O OE1 . GLU A 1 141 ? -10.451 52.596 21.012 1.00 36.31 ? 158 GLU A OE1 1 
ATOM   1065 O OE2 . GLU A 1 141 ? -11.551 52.238 22.897 1.00 44.16 ? 158 GLU A OE2 1 
ATOM   1066 N N   . GLU A 1 142 ? -6.129  50.516 21.955 1.00 18.44 ? 159 GLU A N   1 
ATOM   1067 C CA  . GLU A 1 142 ? -5.286  49.439 22.446 1.00 17.23 ? 159 GLU A CA  1 
ATOM   1068 C C   . GLU A 1 142 ? -3.906  49.428 21.809 1.00 16.35 ? 159 GLU A C   1 
ATOM   1069 O O   . GLU A 1 142 ? -3.038  48.674 22.259 1.00 17.60 ? 159 GLU A O   1 
ATOM   1070 C CB  . GLU A 1 142 ? -5.946  48.080 22.179 1.00 18.26 ? 159 GLU A CB  1 
ATOM   1071 C CG  . GLU A 1 142 ? -7.263  47.843 22.903 1.00 21.28 ? 159 GLU A CG  1 
ATOM   1072 C CD  . GLU A 1 142 ? -7.867  46.500 22.522 1.00 23.65 ? 159 GLU A CD  1 
ATOM   1073 O OE1 . GLU A 1 142 ? -8.735  46.454 21.658 1.00 26.89 ? 159 GLU A OE1 1 
ATOM   1074 O OE2 . GLU A 1 142 ? -7.438  45.473 23.064 1.00 32.08 ? 159 GLU A OE2 1 
ATOM   1075 N N   . ILE A 1 143 ? -3.688  50.240 20.783 1.00 16.61 ? 160 ILE A N   1 
ATOM   1076 C CA  . ILE A 1 143 ? -2.409  50.292 20.085 1.00 16.23 ? 160 ILE A CA  1 
ATOM   1077 C C   . ILE A 1 143 ? -1.581  51.401 20.724 1.00 16.72 ? 160 ILE A C   1 
ATOM   1078 O O   . ILE A 1 143 ? -1.980  52.576 20.729 1.00 18.10 ? 160 ILE A O   1 
ATOM   1079 C CB  . ILE A 1 143 ? -2.617  50.556 18.585 1.00 17.54 ? 160 ILE A CB  1 
ATOM   1080 C CG1 . ILE A 1 143 ? -3.668  49.612 17.993 1.00 20.43 ? 160 ILE A CG1 1 
ATOM   1081 C CG2 . ILE A 1 143 ? -1.304  50.487 17.849 1.00 19.38 ? 160 ILE A CG2 1 
ATOM   1082 C CD1 . ILE A 1 143 ? -3.358  48.166 18.044 1.00 24.35 ? 160 ILE A CD1 1 
ATOM   1083 N N   . GLN A 1 144 ? -0.409  51.031 21.228 1.00 15.98 ? 161 GLN A N   1 
ATOM   1084 C CA  . GLN A 1 144 ? 0.421   51.887 22.055 1.00 16.93 ? 161 GLN A CA  1 
ATOM   1085 C C   . GLN A 1 144 ? 1.609   52.385 21.253 1.00 16.46 ? 161 GLN A C   1 
ATOM   1086 O O   . GLN A 1 144 ? 2.315   51.593 20.614 1.00 18.05 ? 161 GLN A O   1 
ATOM   1087 C CB  . GLN A 1 144 ? 0.917   51.095 23.266 1.00 16.47 ? 161 GLN A CB  1 
ATOM   1088 C CG  . GLN A 1 144 ? -0.190  50.341 24.001 1.00 15.29 ? 161 GLN A CG  1 
ATOM   1089 C CD  . GLN A 1 144 ? -1.257  51.237 24.532 1.00 18.25 ? 161 GLN A CD  1 
ATOM   1090 O OE1 . GLN A 1 144 ? -1.000  52.388 24.904 1.00 21.08 ? 161 GLN A OE1 1 
ATOM   1091 N NE2 . GLN A 1 144 ? -2.479  50.735 24.556 1.00 18.94 ? 161 GLN A NE2 1 
ATOM   1092 N N   . SER A 1 145 ? 1.833   53.691 21.300 1.00 16.64 ? 162 SER A N   1 
ATOM   1093 C CA  A SER A 1 145 ? 2.939   54.338 20.603 0.55 16.00 ? 162 SER A CA  1 
ATOM   1094 C CA  B SER A 1 145 ? 2.944   54.330 20.606 0.45 16.05 ? 162 SER A CA  1 
ATOM   1095 C C   . SER A 1 145 ? 3.993   54.751 21.624 1.00 15.80 ? 162 SER A C   1 
ATOM   1096 O O   . SER A 1 145 ? 3.689   55.493 22.567 1.00 18.52 ? 162 SER A O   1 
ATOM   1097 C CB  A SER A 1 145 ? 2.427   55.565 19.847 0.55 17.22 ? 162 SER A CB  1 
ATOM   1098 C CB  B SER A 1 145 ? 2.449   55.545 19.828 0.45 16.86 ? 162 SER A CB  1 
ATOM   1099 O OG  A SER A 1 145 ? 3.493   56.284 19.261 0.55 20.74 ? 162 SER A OG  1 
ATOM   1100 O OG  B SER A 1 145 ? 1.524   55.135 18.845 0.45 19.89 ? 162 SER A OG  1 
ATOM   1101 N N   . TYR A 1 146 ? 5.217   54.274 21.428 1.00 17.17 ? 163 TYR A N   1 
ATOM   1102 C CA  . TYR A 1 146 ? 6.372   54.667 22.213 1.00 15.91 ? 163 TYR A CA  1 
ATOM   1103 C C   . TYR A 1 146 ? 7.590   54.326 21.372 1.00 14.18 ? 163 TYR A C   1 
ATOM   1104 O O   . TYR A 1 146 ? 7.499   53.562 20.405 1.00 16.60 ? 163 TYR A O   1 
ATOM   1105 C CB  . TYR A 1 146 ? 6.410   53.979 23.584 1.00 15.63 ? 163 TYR A CB  1 
ATOM   1106 C CG  . TYR A 1 146 ? 6.475   52.468 23.534 1.00 13.70 ? 163 TYR A CG  1 
ATOM   1107 C CD1 . TYR A 1 146 ? 5.322   51.711 23.425 1.00 14.42 ? 163 TYR A CD1 1 
ATOM   1108 C CD2 . TYR A 1 146 ? 7.691   51.790 23.580 1.00 15.26 ? 163 TYR A CD2 1 
ATOM   1109 C CE1 . TYR A 1 146 ? 5.372   50.319 23.355 1.00 16.63 ? 163 TYR A CE1 1 
ATOM   1110 C CE2 . TYR A 1 146 ? 7.748   50.417 23.525 1.00 14.90 ? 163 TYR A CE2 1 
ATOM   1111 C CZ  . TYR A 1 146 ? 6.589   49.680 23.407 1.00 15.06 ? 163 TYR A CZ  1 
ATOM   1112 O OH  . TYR A 1 146 ? 6.650   48.313 23.334 1.00 15.57 ? 163 TYR A OH  1 
ATOM   1113 N N   . LYS A 1 147 ? 8.727   54.895 21.748 1.00 16.15 ? 164 LYS A N   1 
ATOM   1114 C CA  . LYS A 1 147 ? 9.980   54.722 21.024 1.00 16.24 ? 164 LYS A CA  1 
ATOM   1115 C C   . LYS A 1 147 ? 10.930  53.844 21.831 1.00 15.40 ? 164 LYS A C   1 
ATOM   1116 O O   . LYS A 1 147 ? 11.145  54.080 23.027 1.00 17.29 ? 164 LYS A O   1 
ATOM   1117 C CB  . LYS A 1 147 ? 10.629  56.082 20.754 1.00 19.98 ? 164 LYS A CB  1 
ATOM   1118 C CG  . LYS A 1 147 ? 11.991  56.015 20.103 1.00 23.88 ? 164 LYS A CG  1 
ATOM   1119 C CD  . LYS A 1 147 ? 12.557  57.439 19.945 1.00 31.11 ? 164 LYS A CD  1 
ATOM   1120 C CE  . LYS A 1 147 ? 14.004  57.448 19.471 1.00 40.73 ? 164 LYS A CE  1 
ATOM   1121 N NZ  . LYS A 1 147 ? 14.121  57.226 18.028 1.00 49.24 ? 164 LYS A NZ  1 
ATOM   1122 N N   . LEU A 1 148 ? 11.501  52.839 21.170 1.00 15.86 ? 165 LEU A N   1 
ATOM   1123 C CA  . LEU A 1 148 ? 12.510  51.999 21.807 1.00 16.74 ? 165 LEU A CA  1 
ATOM   1124 C C   . LEU A 1 148 ? 13.774  52.805 22.081 1.00 17.29 ? 165 LEU A C   1 
ATOM   1125 O O   . LEU A 1 148 ? 14.285  53.525 21.209 1.00 17.54 ? 165 LEU A O   1 
ATOM   1126 C CB  . LEU A 1 148 ? 12.828  50.796 20.924 1.00 17.53 ? 165 LEU A CB  1 
ATOM   1127 C CG  . LEU A 1 148 ? 11.743  49.727 20.806 1.00 17.39 ? 165 LEU A CG  1 
ATOM   1128 C CD1 . LEU A 1 148 ? 12.115  48.671 19.747 1.00 18.05 ? 165 LEU A CD1 1 
ATOM   1129 C CD2 . LEU A 1 148 ? 11.462  49.065 22.165 1.00 18.39 ? 165 LEU A CD2 1 
ATOM   1130 N N   . ALA A 1 149 ? 14.298  52.652 23.297 1.00 17.83 ? 166 ALA A N   1 
ATOM   1131 C CA  . ALA A 1 149 ? 15.484  53.391 23.706 1.00 18.38 ? 166 ALA A CA  1 
ATOM   1132 C C   . ALA A 1 149 ? 16.706  53.050 22.863 1.00 18.70 ? 166 ALA A C   1 
ATOM   1133 O O   . ALA A 1 149 ? 17.587  53.893 22.711 1.00 19.62 ? 166 ALA A O   1 
ATOM   1134 C CB  . ALA A 1 149 ? 15.760  53.126 25.182 1.00 22.95 ? 166 ALA A CB  1 
ATOM   1135 N N   . LEU A 1 150 ? 16.788  51.834 22.310 1.00 16.28 ? 167 LEU A N   1 
ATOM   1136 C CA  . LEU A 1 150 ? 17.912  51.437 21.467 1.00 16.37 ? 167 LEU A CA  1 
ATOM   1137 C C   . LEU A 1 150 ? 17.682  51.729 19.981 1.00 16.56 ? 167 LEU A C   1 
ATOM   1138 O O   . LEU A 1 150 ? 18.414  51.197 19.136 1.00 17.18 ? 167 LEU A O   1 
ATOM   1139 C CB  . LEU A 1 150 ? 18.223  49.953 21.672 1.00 19.76 ? 167 LEU A CB  1 
ATOM   1140 C CG  . LEU A 1 150 ? 18.998  49.649 22.952 1.00 21.04 ? 167 LEU A CG  1 
ATOM   1141 C CD1 . LEU A 1 150 ? 18.993  48.169 23.236 1.00 24.53 ? 167 LEU A CD1 1 
ATOM   1142 C CD2 . LEU A 1 150 ? 20.416  50.153 22.868 1.00 28.59 ? 167 LEU A CD2 1 
ATOM   1143 N N   . SER A 1 151 ? 16.726  52.609 19.658 1.00 17.60 ? 168 SER A N   1 
ATOM   1144 C CA  A SER A 1 151 ? 16.384  52.883 18.264 0.35 17.98 ? 168 SER A CA  1 
ATOM   1145 C CA  B SER A 1 151 ? 16.388  52.872 18.259 0.65 16.73 ? 168 SER A CA  1 
ATOM   1146 C C   . SER A 1 151 ? 17.607  53.256 17.433 1.00 16.47 ? 168 SER A C   1 
ATOM   1147 O O   . SER A 1 151 ? 17.733  52.834 16.280 1.00 18.45 ? 168 SER A O   1 
ATOM   1148 C CB  A SER A 1 151 ? 15.332  53.998 18.225 0.35 21.52 ? 168 SER A CB  1 
ATOM   1149 C CB  B SER A 1 151 ? 15.318  53.969 18.169 0.65 20.62 ? 168 SER A CB  1 
ATOM   1150 O OG  A SER A 1 151 ? 14.976  54.351 16.903 0.35 22.88 ? 168 SER A OG  1 
ATOM   1151 O OG  B SER A 1 151 ? 14.033  53.453 18.441 0.65 22.92 ? 168 SER A OG  1 
ATOM   1152 N N   . ASP A 1 152 ? 18.515  54.073 17.992 1.00 17.48 ? 169 ASP A N   1 
ATOM   1153 C CA  . ASP A 1 152 ? 19.687  54.513 17.231 1.00 19.59 ? 169 ASP A CA  1 
ATOM   1154 C C   . ASP A 1 152 ? 20.579  53.355 16.806 1.00 19.23 ? 169 ASP A C   1 
ATOM   1155 O O   . ASP A 1 152 ? 21.359  53.497 15.856 1.00 20.53 ? 169 ASP A O   1 
ATOM   1156 C CB  . ASP A 1 152 ? 20.543  55.474 18.061 1.00 23.80 ? 169 ASP A CB  1 
ATOM   1157 C CG  . ASP A 1 152 ? 19.897  56.820 18.254 1.00 30.97 ? 169 ASP A CG  1 
ATOM   1158 O OD1 . ASP A 1 152 ? 19.009  57.177 17.457 1.00 35.22 ? 169 ASP A OD1 1 
ATOM   1159 O OD2 . ASP A 1 152 ? 20.292  57.519 19.205 1.00 35.95 ? 169 ASP A OD2 1 
ATOM   1160 N N   . TYR A 1 153 ? 20.494  52.223 17.498 1.00 16.49 ? 170 TYR A N   1 
ATOM   1161 C CA  . TYR A 1 153 ? 21.311  51.057 17.210 1.00 15.16 ? 170 TYR A CA  1 
ATOM   1162 C C   . TYR A 1 153 ? 20.546  49.959 16.483 1.00 15.71 ? 170 TYR A C   1 
ATOM   1163 O O   . TYR A 1 153 ? 21.126  48.922 16.160 1.00 18.09 ? 170 TYR A O   1 
ATOM   1164 C CB  . TYR A 1 153 ? 21.949  50.549 18.508 1.00 15.32 ? 170 TYR A CB  1 
ATOM   1165 C CG  . TYR A 1 153 ? 22.889  51.586 19.075 1.00 17.43 ? 170 TYR A CG  1 
ATOM   1166 C CD1 . TYR A 1 153 ? 24.166  51.739 18.560 1.00 16.26 ? 170 TYR A CD1 1 
ATOM   1167 C CD2 . TYR A 1 153 ? 22.479  52.462 20.085 1.00 18.94 ? 170 TYR A CD2 1 
ATOM   1168 C CE1 . TYR A 1 153 ? 25.019  52.698 19.039 1.00 19.85 ? 170 TYR A CE1 1 
ATOM   1169 C CE2 . TYR A 1 153 ? 23.332  53.431 20.574 1.00 19.02 ? 170 TYR A CE2 1 
ATOM   1170 C CZ  . TYR A 1 153 ? 24.599  53.545 20.043 1.00 20.34 ? 170 TYR A CZ  1 
ATOM   1171 O OH  . TYR A 1 153 ? 25.447  54.505 20.509 1.00 21.70 ? 170 TYR A OH  1 
ATOM   1172 N N   . ILE A 1 154 ? 19.255  50.156 16.239 1.00 17.21 ? 171 ILE A N   1 
ATOM   1173 C CA  . ILE A 1 154 ? 18.437  49.206 15.499 1.00 17.57 ? 171 ILE A CA  1 
ATOM   1174 C C   . ILE A 1 154 ? 18.180  49.682 14.075 1.00 19.39 ? 171 ILE A C   1 
ATOM   1175 O O   . ILE A 1 154 ? 18.228  48.892 13.131 1.00 19.39 ? 171 ILE A O   1 
ATOM   1176 C CB  . ILE A 1 154 ? 17.111  48.982 16.260 1.00 18.82 ? 171 ILE A CB  1 
ATOM   1177 C CG1 . ILE A 1 154 ? 17.352  48.329 17.627 1.00 19.91 ? 171 ILE A CG1 1 
ATOM   1178 C CG2 . ILE A 1 154 ? 16.124  48.174 15.415 1.00 17.73 ? 171 ILE A CG2 1 
ATOM   1179 C CD1 . ILE A 1 154 ? 16.153  48.452 18.522 1.00 21.22 ? 171 ILE A CD1 1 
ATOM   1180 N N   . PHE A 1 155 ? 17.927  50.977 13.908 1.00 18.95 ? 172 PHE A N   1 
ATOM   1181 C CA  . PHE A 1 155 ? 17.560  51.569 12.625 1.00 18.13 ? 172 PHE A CA  1 
ATOM   1182 C C   . PHE A 1 155 ? 18.723  52.373 12.062 1.00 22.06 ? 172 PHE A C   1 
ATOM   1183 O O   . PHE A 1 155 ? 19.439  53.049 12.805 1.00 24.26 ? 172 PHE A O   1 
ATOM   1184 C CB  . PHE A 1 155 ? 16.334  52.472 12.818 1.00 20.31 ? 172 PHE A CB  1 
ATOM   1185 C CG  . PHE A 1 155 ? 15.178  51.762 13.438 1.00 19.41 ? 172 PHE A CG  1 
ATOM   1186 C CD1 . PHE A 1 155 ? 14.524  50.755 12.741 1.00 19.73 ? 172 PHE A CD1 1 
ATOM   1187 C CD2 . PHE A 1 155 ? 14.786  52.039 14.729 1.00 19.50 ? 172 PHE A CD2 1 
ATOM   1188 C CE1 . PHE A 1 155 ? 13.495  50.073 13.296 1.00 18.05 ? 172 PHE A CE1 1 
ATOM   1189 C CE2 . PHE A 1 155 ? 13.740  51.360 15.301 1.00 19.75 ? 172 PHE A CE2 1 
ATOM   1190 C CZ  . PHE A 1 155 ? 13.088  50.378 14.584 1.00 19.97 ? 172 PHE A CZ  1 
ATOM   1191 N N   . GLU A 1 156 ? 18.911  52.264 10.743 1.00 26.20 ? 173 GLU A N   1 
ATOM   1192 C CA  . GLU A 1 156 ? 19.787  53.139 9.961  1.00 32.94 ? 173 GLU A CA  1 
ATOM   1193 C C   . GLU A 1 156 ? 19.485  54.606 10.125 1.00 38.27 ? 173 GLU A C   1 
ATOM   1194 O O   . GLU A 1 156 ? 20.373  55.433 9.908  1.00 42.19 ? 173 GLU A O   1 
ATOM   1195 C CB  . GLU A 1 156 ? 19.616  52.855 8.471  1.00 36.83 ? 173 GLU A CB  1 
ATOM   1196 C CG  . GLU A 1 156 ? 20.245  51.598 8.072  1.00 37.79 ? 173 GLU A CG  1 
ATOM   1197 C CD  . GLU A 1 156 ? 20.033  51.251 6.626  1.00 32.94 ? 173 GLU A CD  1 
ATOM   1198 O OE1 . GLU A 1 156 ? 19.368  51.995 5.864  1.00 38.06 ? 173 GLU A OE1 1 
ATOM   1199 O OE2 . GLU A 1 156 ? 20.557  50.209 6.246  1.00 28.78 ? 173 GLU A OE2 1 
ATOM   1200 O OXT . GLU A 1 156 ? 18.348  54.979 10.421 1.00 42.99 ? 173 GLU A OXT 1 
ATOM   1201 N N   . HIS B 1 8   ? -0.607  9.633  11.102 1.00 42.94 ? 25  HIS B N   1 
ATOM   1202 C CA  . HIS B 1 8   ? 0.323   8.519  10.944 1.00 39.40 ? 25  HIS B CA  1 
ATOM   1203 C C   . HIS B 1 8   ? 1.729   8.949  11.350 1.00 34.72 ? 25  HIS B C   1 
ATOM   1204 O O   . HIS B 1 8   ? 2.386   9.703  10.651 1.00 38.71 ? 25  HIS B O   1 
ATOM   1205 C CB  . HIS B 1 8   ? 0.338   8.037  9.496  1.00 45.16 ? 25  HIS B CB  1 
ATOM   1206 N N   . VAL B 1 9   ? 2.194   8.462  12.481 1.00 28.81 ? 26  VAL B N   1 
ATOM   1207 C CA  . VAL B 1 9   ? 3.544   8.740  12.921 1.00 22.93 ? 26  VAL B CA  1 
ATOM   1208 C C   . VAL B 1 9   ? 4.458   7.594  12.509 1.00 22.21 ? 26  VAL B C   1 
ATOM   1209 O O   . VAL B 1 9   ? 4.023   6.482  12.208 1.00 25.12 ? 26  VAL B O   1 
ATOM   1210 C CB  . VAL B 1 9   ? 3.616   8.985  14.453 1.00 23.54 ? 26  VAL B CB  1 
ATOM   1211 C CG1 . VAL B 1 9   ? 2.805   10.227 14.842 1.00 25.77 ? 26  VAL B CG1 1 
ATOM   1212 C CG2 . VAL B 1 9   ? 3.143   7.757  15.208 1.00 26.16 ? 26  VAL B CG2 1 
ATOM   1213 N N   . GLU B 1 10  ? 5.757   7.865  12.513 1.00 20.29 ? 27  GLU B N   1 
ATOM   1214 C CA  . GLU B 1 10  ? 6.755   6.827  12.301 1.00 20.19 ? 27  GLU B CA  1 
ATOM   1215 C C   . GLU B 1 10  ? 7.830   6.974  13.367 1.00 17.67 ? 27  GLU B C   1 
ATOM   1216 O O   . GLU B 1 10  ? 7.766   7.867  14.211 1.00 17.99 ? 27  GLU B O   1 
ATOM   1217 C CB  . GLU B 1 10  ? 7.322   6.874  10.888 1.00 29.06 ? 27  GLU B CB  1 
ATOM   1218 C CG  . GLU B 1 10  ? 8.066   8.105  10.587 1.00 26.73 ? 27  GLU B CG  1 
ATOM   1219 C CD  . GLU B 1 10  ? 8.287   8.312  9.084  1.00 26.76 ? 27  GLU B CD  1 
ATOM   1220 O OE1 . GLU B 1 10  ? 7.692   7.631  8.226  1.00 32.37 ? 27  GLU B OE1 1 
ATOM   1221 O OE2 . GLU B 1 10  ? 9.104   9.171  8.776  1.00 23.15 ? 27  GLU B OE2 1 
ATOM   1222 N N   . GLN B 1 11  ? 8.793   6.058  13.349 1.00 18.60 ? 28  GLN B N   1 
ATOM   1223 C CA  . GLN B 1 11  ? 9.900   6.043  14.294 1.00 18.62 ? 28  GLN B CA  1 
ATOM   1224 C C   . GLN B 1 11  ? 11.226  6.022  13.551 1.00 17.59 ? 28  GLN B C   1 
ATOM   1225 O O   . GLN B 1 11  ? 11.360  5.370  12.513 1.00 19.94 ? 28  GLN B O   1 
ATOM   1226 C CB  . GLN B 1 11  ? 9.789   4.846  15.254 1.00 18.10 ? 28  GLN B CB  1 
ATOM   1227 C CG  . GLN B 1 11  ? 8.630   5.002  16.220 1.00 22.36 ? 28  GLN B CG  1 
ATOM   1228 C CD  . GLN B 1 11  ? 8.530   3.903  17.253 1.00 23.35 ? 28  GLN B CD  1 
ATOM   1229 O OE1 . GLN B 1 11  ? 9.247   2.904  17.198 1.00 26.57 ? 28  GLN B OE1 1 
ATOM   1230 N NE2 . GLN B 1 11  ? 7.614   4.079  18.203 1.00 25.10 ? 28  GLN B NE2 1 
ATOM   1231 N N   . THR B 1 12  ? 12.209  6.738  14.083 1.00 17.50 ? 29  THR B N   1 
ATOM   1232 C CA  . THR B 1 12  ? 13.539  6.774  13.504 1.00 17.15 ? 29  THR B CA  1 
ATOM   1233 C C   . THR B 1 12  ? 14.575  6.507  14.586 1.00 17.00 ? 29  THR B C   1 
ATOM   1234 O O   . THR B 1 12  ? 14.346  6.775  15.775 1.00 17.94 ? 29  THR B O   1 
ATOM   1235 C CB  . THR B 1 12  ? 13.830  8.114  12.807 1.00 18.04 ? 29  THR B CB  1 
ATOM   1236 O OG1 . THR B 1 12  ? 15.022  7.960  12.023 1.00 20.01 ? 29  THR B OG1 1 
ATOM   1237 C CG2 . THR B 1 12  ? 14.008  9.240  13.812 1.00 17.50 ? 29  THR B CG2 1 
ATOM   1238 N N   . TYR B 1 13  ? 15.699  5.935  14.164 1.00 15.72 ? 30  TYR B N   1 
ATOM   1239 C CA  . TYR B 1 13  ? 16.841  5.711  15.039 1.00 17.25 ? 30  TYR B CA  1 
ATOM   1240 C C   . TYR B 1 13  ? 17.780  6.918  14.974 1.00 17.40 ? 30  TYR B C   1 
ATOM   1241 O O   . TYR B 1 13  ? 18.254  7.289  13.900 1.00 17.16 ? 30  TYR B O   1 
ATOM   1242 C CB  . TYR B 1 13  ? 17.599  4.431  14.668 1.00 18.96 ? 30  TYR B CB  1 
ATOM   1243 C CG  . TYR B 1 13  ? 18.807  4.215  15.547 1.00 17.25 ? 30  TYR B CG  1 
ATOM   1244 C CD1 . TYR B 1 13  ? 18.647  3.944  16.895 1.00 17.12 ? 30  TYR B CD1 1 
ATOM   1245 C CD2 . TYR B 1 13  ? 20.104  4.333  15.054 1.00 16.73 ? 30  TYR B CD2 1 
ATOM   1246 C CE1 . TYR B 1 13  ? 19.723  3.774  17.717 1.00 18.19 ? 30  TYR B CE1 1 
ATOM   1247 C CE2 . TYR B 1 13  ? 21.198  4.159  15.879 1.00 18.43 ? 30  TYR B CE2 1 
ATOM   1248 C CZ  . TYR B 1 13  ? 20.992  3.899  17.218 1.00 17.66 ? 30  TYR B CZ  1 
ATOM   1249 O OH  . TYR B 1 13  ? 22.042  3.717  18.094 1.00 19.75 ? 30  TYR B OH  1 
ATOM   1250 N N   . LEU B 1 14  ? 18.017  7.551  16.114 1.00 15.02 ? 31  LEU B N   1 
ATOM   1251 C CA  . LEU B 1 14  ? 18.964  8.648  16.241 1.00 15.69 ? 31  LEU B CA  1 
ATOM   1252 C C   . LEU B 1 14  ? 20.006  8.240  17.271 1.00 17.10 ? 31  LEU B C   1 
ATOM   1253 O O   . LEU B 1 14  ? 19.666  7.667  18.315 1.00 21.05 ? 31  LEU B O   1 
ATOM   1254 C CB  . LEU B 1 14  ? 18.260  9.939  16.681 1.00 18.16 ? 31  LEU B CB  1 
ATOM   1255 C CG  . LEU B 1 14  ? 17.383  10.559 15.587 1.00 20.66 ? 31  LEU B CG  1 
ATOM   1256 C CD1 . LEU B 1 14  ? 16.330  11.459 16.189 1.00 22.33 ? 31  LEU B CD1 1 
ATOM   1257 C CD2 . LEU B 1 14  ? 18.266  11.356 14.649 1.00 27.09 ? 31  LEU B CD2 1 
ATOM   1258 N N   . MET B 1 15  ? 21.267  8.533  16.981 1.00 16.00 ? 32  MET B N   1 
ATOM   1259 C CA  . MET B 1 15  ? 22.371  8.144  17.849 1.00 14.98 ? 32  MET B CA  1 
ATOM   1260 C C   . MET B 1 15  ? 23.290  9.331  18.048 1.00 15.67 ? 32  MET B C   1 
ATOM   1261 O O   . MET B 1 15  ? 23.839  9.871  17.083 1.00 16.85 ? 32  MET B O   1 
ATOM   1262 C CB  . MET B 1 15  ? 23.148  6.970  17.240 1.00 17.64 ? 32  MET B CB  1 
ATOM   1263 C CG  . MET B 1 15  ? 24.324  6.505  18.103 1.00 20.27 ? 32  MET B CG  1 
ATOM   1264 S SD  . MET B 1 15  ? 24.980  4.915  17.550 1.00 21.37 ? 32  MET B SD  1 
ATOM   1265 C CE  . MET B 1 15  ? 25.198  5.190  15.789 1.00 21.71 ? 32  MET B CE  1 
ATOM   1266 N N   . ILE B 1 16  ? 23.457  9.751  19.291 1.00 15.14 ? 33  ILE B N   1 
ATOM   1267 C CA  . ILE B 1 16  ? 24.461  10.754 19.611 1.00 15.15 ? 33  ILE B CA  1 
ATOM   1268 C C   . ILE B 1 16  ? 25.819  10.055 19.652 1.00 13.48 ? 33  ILE B C   1 
ATOM   1269 O O   . ILE B 1 16  ? 26.014  9.081  20.385 1.00 15.75 ? 33  ILE B O   1 
ATOM   1270 C CB  . ILE B 1 16  ? 24.149  11.444 20.946 1.00 15.31 ? 33  ILE B CB  1 
ATOM   1271 C CG1 . ILE B 1 16  ? 22.756  12.074 20.873 1.00 15.98 ? 33  ILE B CG1 1 
ATOM   1272 C CG2 . ILE B 1 16  ? 25.216  12.492 21.248 1.00 15.11 ? 33  ILE B CG2 1 
ATOM   1273 C CD1 . ILE B 1 16  ? 22.313  12.779 22.153 1.00 18.09 ? 33  ILE B CD1 1 
ATOM   1274 N N   . LYS B 1 17  ? 26.752  10.552 18.852 1.00 15.09 ? 34  LYS B N   1 
ATOM   1275 C CA  . LYS B 1 17  ? 28.061  9.953  18.669 1.00 16.68 ? 34  LYS B CA  1 
ATOM   1276 C C   . LYS B 1 17  ? 28.976  10.369 19.815 1.00 14.71 ? 34  LYS B C   1 
ATOM   1277 O O   . LYS B 1 17  ? 28.630  11.237 20.613 1.00 16.25 ? 34  LYS B O   1 
ATOM   1278 C CB  . LYS B 1 17  ? 28.604  10.383 17.310 1.00 15.09 ? 34  LYS B CB  1 
ATOM   1279 C CG  . LYS B 1 17  ? 27.741  9.961  16.144 1.00 15.40 ? 34  LYS B CG  1 
ATOM   1280 C CD  . LYS B 1 17  ? 28.326  10.435 14.812 1.00 15.21 ? 34  LYS B CD  1 
ATOM   1281 C CE  . LYS B 1 17  ? 27.551  9.854  13.667 1.00 17.08 ? 34  LYS B CE  1 
ATOM   1282 N NZ  . LYS B 1 17  ? 28.016  10.344 12.346 1.00 20.92 ? 34  LYS B NZ  1 
ATOM   1283 N N   . PRO B 1 18  ? 30.169  9.774  19.925 1.00 15.28 ? 35  PRO B N   1 
ATOM   1284 C CA  . PRO B 1 18  ? 31.013  10.091 21.089 1.00 15.64 ? 35  PRO B CA  1 
ATOM   1285 C C   . PRO B 1 18  ? 31.364  11.558 21.203 1.00 15.70 ? 35  PRO B C   1 
ATOM   1286 O O   . PRO B 1 18  ? 31.592  12.032 22.323 1.00 15.74 ? 35  PRO B O   1 
ATOM   1287 C CB  . PRO B 1 18  ? 32.251  9.208  20.879 1.00 16.81 ? 35  PRO B CB  1 
ATOM   1288 C CG  . PRO B 1 18  ? 31.742  8.075  20.084 1.00 17.28 ? 35  PRO B CG  1 
ATOM   1289 C CD  . PRO B 1 18  ? 30.753  8.675  19.129 1.00 17.29 ? 35  PRO B CD  1 
ATOM   1290 N N   . ASP B 1 19  ? 31.432  12.294 20.088 1.00 15.53 ? 36  ASP B N   1 
ATOM   1291 C CA  . ASP B 1 19  ? 31.696  13.729 20.185 1.00 16.73 ? 36  ASP B CA  1 
ATOM   1292 C C   . ASP B 1 19  ? 30.559  14.478 20.878 1.00 17.16 ? 36  ASP B C   1 
ATOM   1293 O O   . ASP B 1 19  ? 30.805  15.445 21.609 1.00 16.08 ? 36  ASP B O   1 
ATOM   1294 C CB  . ASP B 1 19  ? 32.061  14.355 18.832 1.00 15.94 ? 36  ASP B CB  1 
ATOM   1295 C CG  . ASP B 1 19  ? 31.101  14.020 17.706 1.00 17.02 ? 36  ASP B CG  1 
ATOM   1296 O OD1 . ASP B 1 19  ? 30.490  12.939 17.690 1.00 17.72 ? 36  ASP B OD1 1 
ATOM   1297 O OD2 . ASP B 1 19  ? 31.005  14.865 16.791 1.00 17.33 ? 36  ASP B OD2 1 
ATOM   1298 N N   . GLY B 1 20  ? 29.312  14.060 20.646 1.00 15.10 ? 37  GLY B N   1 
ATOM   1299 C CA  . GLY B 1 20  ? 28.195  14.663 21.362 1.00 13.69 ? 37  GLY B CA  1 
ATOM   1300 C C   . GLY B 1 20  ? 28.248  14.402 22.854 1.00 14.76 ? 37  GLY B C   1 
ATOM   1301 O O   . GLY B 1 20  ? 27.910  15.276 23.658 1.00 16.45 ? 37  GLY B O   1 
ATOM   1302 N N   . ILE B 1 21  ? 28.636  13.178 23.242 1.00 15.51 ? 38  ILE B N   1 
ATOM   1303 C CA  . ILE B 1 21  ? 28.806  12.849 24.657 1.00 15.66 ? 38  ILE B CA  1 
ATOM   1304 C C   . ILE B 1 21  ? 29.934  13.681 25.262 1.00 14.61 ? 38  ILE B C   1 
ATOM   1305 O O   . ILE B 1 21  ? 29.767  14.318 26.309 1.00 17.30 ? 38  ILE B O   1 
ATOM   1306 C CB  . ILE B 1 21  ? 29.095  11.346 24.829 1.00 15.04 ? 38  ILE B CB  1 
ATOM   1307 C CG1 . ILE B 1 21  ? 28.054  10.461 24.126 1.00 19.57 ? 38  ILE B CG1 1 
ATOM   1308 C CG2 . ILE B 1 21  ? 29.247  11.007 26.310 1.00 16.90 ? 38  ILE B CG2 1 
ATOM   1309 C CD1 . ILE B 1 21  ? 26.642  10.640 24.588 1.00 21.20 ? 38  ILE B CD1 1 
ATOM   1310 N N   . GLN B 1 22  ? 31.097  13.692 24.597 1.00 15.16 ? 39  GLN B N   1 
ATOM   1311 C CA  . GLN B 1 22  ? 32.293  14.294 25.179 1.00 15.72 ? 39  GLN B CA  1 
ATOM   1312 C C   . GLN B 1 22  ? 32.204  15.810 25.212 1.00 15.75 ? 39  GLN B C   1 
ATOM   1313 O O   . GLN B 1 22  ? 32.772  16.456 26.104 1.00 15.97 ? 39  GLN B O   1 
ATOM   1314 C CB  . GLN B 1 22  ? 33.548  13.859 24.411 1.00 15.56 ? 39  GLN B CB  1 
ATOM   1315 C CG  . GLN B 1 22  ? 33.928  12.412 24.629 1.00 17.67 ? 39  GLN B CG  1 
ATOM   1316 C CD  . GLN B 1 22  ? 34.552  12.188 25.974 1.00 19.75 ? 39  GLN B CD  1 
ATOM   1317 O OE1 . GLN B 1 22  ? 34.686  13.131 26.762 1.00 21.05 ? 39  GLN B OE1 1 
ATOM   1318 N NE2 . GLN B 1 22  ? 34.935  10.947 26.260 1.00 20.16 ? 39  GLN B NE2 1 
ATOM   1319 N N   . ARG B 1 23  ? 31.520  16.400 24.246 1.00 15.37 ? 40  ARG B N   1 
ATOM   1320 C CA  . ARG B 1 23  ? 31.328  17.840 24.250 1.00 16.05 ? 40  ARG B CA  1 
ATOM   1321 C C   . ARG B 1 23  ? 30.184  18.240 25.166 1.00 16.58 ? 40  ARG B C   1 
ATOM   1322 O O   . ARG B 1 23  ? 29.956  19.436 25.372 1.00 18.26 ? 40  ARG B O   1 
ATOM   1323 C CB  . ARG B 1 23  ? 31.121  18.328 22.817 1.00 15.86 ? 40  ARG B CB  1 
ATOM   1324 C CG  . ARG B 1 23  ? 32.392  18.167 21.983 1.00 15.83 ? 40  ARG B CG  1 
ATOM   1325 C CD  . ARG B 1 23  ? 32.192  18.502 20.521 1.00 15.55 ? 40  ARG B CD  1 
ATOM   1326 N NE  . ARG B 1 23  ? 32.034  19.942 20.371 1.00 15.82 ? 40  ARG B NE  1 
ATOM   1327 C CZ  . ARG B 1 23  ? 31.446  20.515 19.337 1.00 17.20 ? 40  ARG B CZ  1 
ATOM   1328 N NH1 . ARG B 1 23  ? 31.017  19.795 18.300 1.00 17.22 ? 40  ARG B NH1 1 
ATOM   1329 N NH2 . ARG B 1 23  ? 31.281  21.837 19.336 1.00 17.29 ? 40  ARG B NH2 1 
ATOM   1330 N N   . GLN B 1 24  ? 29.479  17.261 25.715 1.00 15.52 ? 41  GLN B N   1 
ATOM   1331 C CA  . GLN B 1 24  ? 28.470  17.470 26.759 1.00 16.49 ? 41  GLN B CA  1 
ATOM   1332 C C   . GLN B 1 24  ? 27.311  18.332 26.273 1.00 16.79 ? 41  GLN B C   1 
ATOM   1333 O O   . GLN B 1 24  ? 26.875  19.269 26.936 1.00 17.25 ? 41  GLN B O   1 
ATOM   1334 C CB  . GLN B 1 24  ? 29.106  18.002 28.047 1.00 18.86 ? 41  GLN B CB  1 
ATOM   1335 C CG  . GLN B 1 24  ? 30.218  17.081 28.552 1.00 18.75 ? 41  GLN B CG  1 
ATOM   1336 C CD  . GLN B 1 24  ? 30.175  16.906 30.056 1.00 18.70 ? 41  GLN B CD  1 
ATOM   1337 O OE1 . GLN B 1 24  ? 30.873  17.592 30.774 1.00 20.91 ? 41  GLN B OE1 1 
ATOM   1338 N NE2 . GLN B 1 24  ? 29.353  15.990 30.529 1.00 19.03 ? 41  GLN B NE2 1 
ATOM   1339 N N   . VAL B 1 25  ? 26.809  17.982 25.087 1.00 15.19 ? 42  VAL B N   1 
ATOM   1340 C CA  . VAL B 1 25  ? 25.662  18.611 24.448 1.00 15.64 ? 42  VAL B CA  1 
ATOM   1341 C C   . VAL B 1 25  ? 24.491  17.632 24.297 1.00 14.29 ? 42  VAL B C   1 
ATOM   1342 O O   . VAL B 1 25  ? 23.597  17.864 23.492 1.00 15.42 ? 42  VAL B O   1 
ATOM   1343 C CB  . VAL B 1 25  ? 26.054  19.278 23.116 1.00 16.54 ? 42  VAL B CB  1 
ATOM   1344 C CG1 . VAL B 1 25  ? 27.036  20.428 23.376 1.00 19.42 ? 42  VAL B CG1 1 
ATOM   1345 C CG2 . VAL B 1 25  ? 26.651  18.272 22.143 1.00 17.58 ? 42  VAL B CG2 1 
ATOM   1346 N N   . VAL B 1 26  ? 24.477  16.540 25.079 1.00 12.76 ? 43  VAL B N   1 
ATOM   1347 C CA  . VAL B 1 26  ? 23.399  15.559 24.973 1.00 13.99 ? 43  VAL B CA  1 
ATOM   1348 C C   . VAL B 1 26  ? 22.046  16.209 25.223 1.00 13.38 ? 43  VAL B C   1 
ATOM   1349 O O   . VAL B 1 26  ? 21.099  16.030 24.452 1.00 14.98 ? 43  VAL B O   1 
ATOM   1350 C CB  . VAL B 1 26  ? 23.650  14.384 25.934 1.00 15.49 ? 43  VAL B CB  1 
ATOM   1351 C CG1 . VAL B 1 26  ? 22.436  13.481 26.026 1.00 15.97 ? 43  VAL B CG1 1 
ATOM   1352 C CG2 . VAL B 1 26  ? 24.888  13.611 25.504 1.00 15.22 ? 43  VAL B CG2 1 
ATOM   1353 N N   . GLY B 1 27  ? 21.924  16.954 26.323 1.00 13.61 ? 44  GLY B N   1 
ATOM   1354 C CA  . GLY B 1 27  ? 20.643  17.553 26.639 1.00 15.10 ? 44  GLY B CA  1 
ATOM   1355 C C   . GLY B 1 27  ? 20.174  18.518 25.567 1.00 15.37 ? 44  GLY B C   1 
ATOM   1356 O O   . GLY B 1 27  ? 18.984  18.581 25.262 1.00 14.94 ? 44  GLY B O   1 
ATOM   1357 N N   . GLU B 1 28  ? 21.093  19.309 25.010 1.00 14.14 ? 45  GLU B N   1 
ATOM   1358 C CA  . GLU B 1 28  ? 20.699  20.260 23.976 1.00 14.02 ? 45  GLU B CA  1 
ATOM   1359 C C   . GLU B 1 28  ? 20.187  19.541 22.746 1.00 15.31 ? 45  GLU B C   1 
ATOM   1360 O O   . GLU B 1 28  ? 19.247  20.007 22.092 1.00 15.48 ? 45  GLU B O   1 
ATOM   1361 C CB  . GLU B 1 28  ? 21.879  21.115 23.543 1.00 16.69 ? 45  GLU B CB  1 
ATOM   1362 C CG  . GLU B 1 28  ? 22.340  22.146 24.498 1.00 20.08 ? 45  GLU B CG  1 
ATOM   1363 C CD  . GLU B 1 28  ? 23.323  23.070 23.801 1.00 26.79 ? 45  GLU B CD  1 
ATOM   1364 O OE1 . GLU B 1 28  ? 22.908  23.811 22.881 1.00 28.75 ? 45  GLU B OE1 1 
ATOM   1365 O OE2 . GLU B 1 28  ? 24.516  23.013 24.136 1.00 28.15 ? 45  GLU B OE2 1 
ATOM   1366 N N   . ILE B 1 29  ? 20.822  18.424 22.396 1.00 14.61 ? 46  ILE B N   1 
ATOM   1367 C CA  . ILE B 1 29  ? 20.356  17.645 21.253 1.00 13.79 ? 46  ILE B CA  1 
ATOM   1368 C C   . ILE B 1 29  ? 18.948  17.129 21.501 1.00 14.65 ? 46  ILE B C   1 
ATOM   1369 O O   . ILE B 1 29  ? 18.052  17.280 20.670 1.00 15.55 ? 46  ILE B O   1 
ATOM   1370 C CB  . ILE B 1 29  ? 21.329  16.496 20.953 1.00 15.12 ? 46  ILE B CB  1 
ATOM   1371 C CG1 . ILE B 1 29  ? 22.667  17.069 20.469 1.00 16.01 ? 46  ILE B CG1 1 
ATOM   1372 C CG2 . ILE B 1 29  ? 20.706  15.545 19.930 1.00 17.45 ? 46  ILE B CG2 1 
ATOM   1373 C CD1 . ILE B 1 29  ? 23.805  16.041 20.382 1.00 16.94 ? 46  ILE B CD1 1 
ATOM   1374 N N   . ILE B 1 30  ? 18.738  16.491 22.656 1.00 14.61 ? 47  ILE B N   1 
ATOM   1375 C CA  . ILE B 1 30  ? 17.426  15.934 22.966 1.00 14.61 ? 47  ILE B CA  1 
ATOM   1376 C C   . ILE B 1 30  ? 16.375  17.035 22.966 1.00 13.97 ? 47  ILE B C   1 
ATOM   1377 O O   . ILE B 1 30  ? 15.267  16.854 22.450 1.00 14.61 ? 47  ILE B O   1 
ATOM   1378 C CB  . ILE B 1 30  ? 17.491  15.191 24.315 1.00 14.16 ? 47  ILE B CB  1 
ATOM   1379 C CG1 . ILE B 1 30  ? 18.388  13.955 24.184 1.00 14.71 ? 47  ILE B CG1 1 
ATOM   1380 C CG2 . ILE B 1 30  ? 16.082  14.858 24.822 1.00 15.29 ? 47  ILE B CG2 1 
ATOM   1381 C CD1 . ILE B 1 30  ? 18.678  13.303 25.520 1.00 17.03 ? 47  ILE B CD1 1 
ATOM   1382 N N   . SER B 1 31  ? 16.718  18.204 23.508 1.00 14.13 ? 48  SER B N   1 
ATOM   1383 C CA  . SER B 1 31  ? 15.758  19.302 23.558 1.00 13.16 ? 48  SER B CA  1 
ATOM   1384 C C   . SER B 1 31  ? 15.278  19.719 22.175 1.00 13.72 ? 48  SER B C   1 
ATOM   1385 O O   . SER B 1 31  ? 14.115  20.085 22.008 1.00 15.19 ? 48  SER B O   1 
ATOM   1386 C CB  . SER B 1 31  ? 16.332  20.507 24.293 1.00 13.46 ? 48  SER B CB  1 
ATOM   1387 O OG  . SER B 1 31  ? 16.441  20.236 25.687 1.00 14.93 ? 48  SER B OG  1 
ATOM   1388 N N   . ARG B 1 32  ? 16.151  19.666 21.166 1.00 14.87 ? 49  ARG B N   1 
ATOM   1389 C CA  . ARG B 1 32  ? 15.709  20.075 19.835 1.00 13.22 ? 49  ARG B CA  1 
ATOM   1390 C C   . ARG B 1 32  ? 14.606  19.161 19.321 1.00 14.26 ? 49  ARG B C   1 
ATOM   1391 O O   . ARG B 1 32  ? 13.698  19.609 18.617 1.00 15.18 ? 49  ARG B O   1 
ATOM   1392 C CB  . ARG B 1 32  ? 16.886  20.101 18.869 1.00 15.54 ? 49  ARG B CB  1 
ATOM   1393 C CG  . ARG B 1 32  ? 17.883  21.186 19.128 1.00 16.22 ? 49  ARG B CG  1 
ATOM   1394 C CD  . ARG B 1 32  ? 18.821  21.311 17.966 1.00 22.97 ? 49  ARG B CD  1 
ATOM   1395 N NE  . ARG B 1 32  ? 19.753  22.396 18.185 1.00 22.73 ? 49  ARG B NE  1 
ATOM   1396 C CZ  . ARG B 1 32  ? 20.287  23.140 17.227 1.00 20.93 ? 49  ARG B CZ  1 
ATOM   1397 N NH1 . ARG B 1 32  ? 20.001  22.941 15.948 1.00 20.46 ? 49  ARG B NH1 1 
ATOM   1398 N NH2 . ARG B 1 32  ? 21.125  24.113 17.560 1.00 21.27 ? 49  ARG B NH2 1 
ATOM   1399 N N   . PHE B 1 33  ? 14.700  17.863 19.609 1.00 13.69 ? 50  PHE B N   1 
ATOM   1400 C CA  . PHE B 1 33  ? 13.659  16.940 19.154 1.00 14.93 ? 50  PHE B CA  1 
ATOM   1401 C C   . PHE B 1 33  ? 12.400  17.031 20.008 1.00 14.05 ? 50  PHE B C   1 
ATOM   1402 O O   . PHE B 1 33  ? 11.283  17.032 19.483 1.00 15.15 ? 50  PHE B O   1 
ATOM   1403 C CB  . PHE B 1 33  ? 14.224  15.523 19.063 1.00 15.29 ? 50  PHE B CB  1 
ATOM   1404 C CG  . PHE B 1 33  ? 15.324  15.394 18.039 1.00 15.69 ? 50  PHE B CG  1 
ATOM   1405 C CD1 . PHE B 1 33  ? 15.026  15.405 16.700 1.00 17.82 ? 50  PHE B CD1 1 
ATOM   1406 C CD2 . PHE B 1 33  ? 16.652  15.302 18.407 1.00 16.03 ? 50  PHE B CD2 1 
ATOM   1407 C CE1 . PHE B 1 33  ? 16.027  15.314 15.752 1.00 17.31 ? 50  PHE B CE1 1 
ATOM   1408 C CE2 . PHE B 1 33  ? 17.649  15.203 17.443 1.00 18.17 ? 50  PHE B CE2 1 
ATOM   1409 C CZ  . PHE B 1 33  ? 17.319  15.222 16.126 1.00 17.57 ? 50  PHE B CZ  1 
ATOM   1410 N N   . GLU B 1 34  ? 12.554  17.134 21.321 1.00 14.09 ? 51  GLU B N   1 
ATOM   1411 C CA  . GLU B 1 34  ? 11.395  17.342 22.177 1.00 14.54 ? 51  GLU B CA  1 
ATOM   1412 C C   . GLU B 1 34  ? 10.629  18.604 21.807 1.00 14.63 ? 51  GLU B C   1 
ATOM   1413 O O   . GLU B 1 34  ? 9.399   18.658 21.987 1.00 15.20 ? 51  GLU B O   1 
ATOM   1414 C CB  . GLU B 1 34  ? 11.835  17.471 23.635 1.00 16.20 ? 51  GLU B CB  1 
ATOM   1415 C CG  . GLU B 1 34  ? 12.168  16.180 24.342 1.00 16.35 ? 51  GLU B CG  1 
ATOM   1416 C CD  . GLU B 1 34  ? 12.552  16.426 25.771 1.00 17.14 ? 51  GLU B CD  1 
ATOM   1417 O OE1 . GLU B 1 34  ? 13.543  17.169 25.985 1.00 15.44 ? 51  GLU B OE1 1 
ATOM   1418 O OE2 . GLU B 1 34  ? 11.847  15.915 26.671 1.00 15.60 ? 51  GLU B OE2 1 
ATOM   1419 N N   . LYS B 1 35  ? 11.335  19.630 21.303 1.00 14.37 ? 52  LYS B N   1 
ATOM   1420 C CA  . LYS B 1 35  ? 10.713  20.927 21.048 1.00 14.08 ? 52  LYS B CA  1 
ATOM   1421 C C   . LYS B 1 35  ? 9.620   20.826 20.002 1.00 12.87 ? 52  LYS B C   1 
ATOM   1422 O O   . LYS B 1 35  ? 8.687   21.633 20.007 1.00 14.83 ? 52  LYS B O   1 
ATOM   1423 C CB  . LYS B 1 35  ? 11.772  21.927 20.585 1.00 16.18 ? 52  LYS B CB  1 
ATOM   1424 C CG  . LYS B 1 35  ? 11.332  23.373 20.642 1.00 17.15 ? 52  LYS B CG  1 
ATOM   1425 C CD  . LYS B 1 35  ? 12.486  24.284 20.225 1.00 22.76 ? 52  LYS B CD  1 
ATOM   1426 C CE  . LYS B 1 35  ? 12.344  25.683 20.754 1.00 30.38 ? 52  LYS B CE  1 
ATOM   1427 N NZ  . LYS B 1 35  ? 12.331  25.676 22.232 1.00 32.27 ? 52  LYS B NZ  1 
ATOM   1428 N N   . ARG B 1 36  ? 9.726   19.845 19.096 1.00 12.70 ? 53  ARG B N   1 
ATOM   1429 C CA  . ARG B 1 36  ? 8.726   19.632 18.059 1.00 13.99 ? 53  ARG B CA  1 
ATOM   1430 C C   . ARG B 1 36  ? 7.631   18.676 18.481 1.00 12.99 ? 53  ARG B C   1 
ATOM   1431 O O   . ARG B 1 36  ? 6.776   18.337 17.662 1.00 15.20 ? 53  ARG B O   1 
ATOM   1432 C CB  . ARG B 1 36  ? 9.380   19.115 16.770 1.00 13.86 ? 53  ARG B CB  1 
ATOM   1433 C CG  . ARG B 1 36  ? 10.356  20.107 16.182 1.00 14.88 ? 53  ARG B CG  1 
ATOM   1434 C CD  . ARG B 1 36  ? 10.886  19.717 14.832 1.00 14.39 ? 53  ARG B CD  1 
ATOM   1435 N NE  . ARG B 1 36  ? 9.847   19.738 13.812 1.00 14.69 ? 53  ARG B NE  1 
ATOM   1436 C CZ  . ARG B 1 36  ? 10.048  19.474 12.531 1.00 14.36 ? 53  ARG B CZ  1 
ATOM   1437 N NH1 . ARG B 1 36  ? 11.221  19.059 12.091 1.00 15.50 ? 53  ARG B NH1 1 
ATOM   1438 N NH2 . ARG B 1 36  ? 9.048   19.653 11.675 1.00 16.12 ? 53  ARG B NH2 1 
ATOM   1439 N N   . GLY B 1 37  ? 7.635   18.232 19.738 1.00 13.82 ? 54  GLY B N   1 
ATOM   1440 C CA  . GLY B 1 37  ? 6.656   17.265 20.170 1.00 13.75 ? 54  GLY B CA  1 
ATOM   1441 C C   . GLY B 1 37  ? 6.954   15.865 19.716 1.00 13.87 ? 54  GLY B C   1 
ATOM   1442 O O   . GLY B 1 37  ? 6.040   15.044 19.647 1.00 15.80 ? 54  GLY B O   1 
ATOM   1443 N N   . TYR B 1 38  ? 8.196   15.576 19.342 1.00 14.07 ? 55  TYR B N   1 
ATOM   1444 C CA  . TYR B 1 38  ? 8.570   14.197 19.068 1.00 14.08 ? 55  TYR B CA  1 
ATOM   1445 C C   . TYR B 1 38  ? 8.670   13.444 20.390 1.00 15.08 ? 55  TYR B C   1 
ATOM   1446 O O   . TYR B 1 38  ? 9.138   13.979 21.404 1.00 16.09 ? 55  TYR B O   1 
ATOM   1447 C CB  . TYR B 1 38  ? 9.901   14.139 18.346 1.00 15.78 ? 55  TYR B CB  1 
ATOM   1448 C CG  . TYR B 1 38  ? 9.894   14.732 16.949 1.00 14.80 ? 55  TYR B CG  1 
ATOM   1449 C CD1 . TYR B 1 38  ? 8.754   14.699 16.145 1.00 15.77 ? 55  TYR B CD1 1 
ATOM   1450 C CD2 . TYR B 1 38  ? 11.037  15.297 16.419 1.00 14.07 ? 55  TYR B CD2 1 
ATOM   1451 C CE1 . TYR B 1 38  ? 8.764   15.238 14.864 1.00 15.06 ? 55  TYR B CE1 1 
ATOM   1452 C CE2 . TYR B 1 38  ? 11.049  15.827 15.124 1.00 14.82 ? 55  TYR B CE2 1 
ATOM   1453 C CZ  . TYR B 1 38  ? 9.922   15.795 14.373 1.00 15.45 ? 55  TYR B CZ  1 
ATOM   1454 O OH  . TYR B 1 38  ? 9.930   16.323 13.099 1.00 16.21 ? 55  TYR B OH  1 
ATOM   1455 N N   . ARG B 1 39  ? 8.203   12.200 20.376 1.00 13.98 ? 56  ARG B N   1 
ATOM   1456 C CA  . ARG B 1 39  ? 8.160   11.383 21.578 1.00 15.58 ? 56  ARG B CA  1 
ATOM   1457 C C   . ARG B 1 39  ? 9.405   10.512 21.674 1.00 14.92 ? 56  ARG B C   1 
ATOM   1458 O O   . ARG B 1 39  ? 9.781   9.836  20.716 1.00 15.42 ? 56  ARG B O   1 
ATOM   1459 C CB  . ARG B 1 39  ? 6.907   10.501 21.539 1.00 15.28 ? 56  ARG B CB  1 
ATOM   1460 C CG  . ARG B 1 39  ? 6.698   9.684  22.789 1.00 15.38 ? 56  ARG B CG  1 
ATOM   1461 C CD  . ARG B 1 39  ? 5.424   8.863  22.710 1.00 17.08 ? 56  ARG B CD  1 
ATOM   1462 N NE  . ARG B 1 39  ? 5.510   7.774  21.739 1.00 17.25 ? 56  ARG B NE  1 
ATOM   1463 C CZ  . ARG B 1 39  ? 5.963   6.555  22.013 1.00 18.58 ? 56  ARG B CZ  1 
ATOM   1464 N NH1 . ARG B 1 39  ? 6.458   6.254  23.195 1.00 19.63 ? 56  ARG B NH1 1 
ATOM   1465 N NH2 . ARG B 1 39  ? 5.915   5.615  21.076 1.00 19.40 ? 56  ARG B NH2 1 
ATOM   1466 N N   . ILE B 1 40  ? 10.021  10.493 22.858 1.00 16.27 ? 57  ILE B N   1 
ATOM   1467 C CA  . ILE B 1 40  ? 11.114  9.570  23.132 1.00 16.45 ? 57  ILE B CA  1 
ATOM   1468 C C   . ILE B 1 40  ? 10.501  8.186  23.328 1.00 15.99 ? 57  ILE B C   1 
ATOM   1469 O O   . ILE B 1 40  ? 9.852   7.937  24.340 1.00 18.02 ? 57  ILE B O   1 
ATOM   1470 C CB  . ILE B 1 40  ? 11.920  9.981  24.373 1.00 15.23 ? 57  ILE B CB  1 
ATOM   1471 C CG1 . ILE B 1 40  ? 12.451  11.404 24.267 1.00 17.00 ? 57  ILE B CG1 1 
ATOM   1472 C CG2 . ILE B 1 40  ? 13.065  9.005  24.564 1.00 15.82 ? 57  ILE B CG2 1 
ATOM   1473 C CD1 . ILE B 1 40  ? 12.978  11.967 25.624 1.00 17.52 ? 57  ILE B CD1 1 
ATOM   1474 N N   . ALA B 1 41  ? 10.692  7.295  22.359 1.00 17.21 ? 58  ALA B N   1 
ATOM   1475 C CA  . ALA B 1 41  ? 10.224  5.920  22.469 1.00 16.71 ? 58  ALA B CA  1 
ATOM   1476 C C   . ALA B 1 41  ? 11.284  4.978  23.022 1.00 17.62 ? 58  ALA B C   1 
ATOM   1477 O O   . ALA B 1 41  ? 10.934  3.915  23.547 1.00 18.87 ? 58  ALA B O   1 
ATOM   1478 C CB  . ALA B 1 41  ? 9.734   5.428  21.102 1.00 18.26 ? 58  ALA B CB  1 
ATOM   1479 N N   . ALA B 1 42  ? 12.559  5.340  22.929 1.00 17.19 ? 59  ALA B N   1 
ATOM   1480 C CA  . ALA B 1 42  ? 13.625  4.514  23.476 1.00 18.04 ? 59  ALA B CA  1 
ATOM   1481 C C   . ALA B 1 42  ? 14.843  5.391  23.673 1.00 16.12 ? 59  ALA B C   1 
ATOM   1482 O O   . ALA B 1 42  ? 15.059  6.349  22.930 1.00 17.53 ? 59  ALA B O   1 
ATOM   1483 C CB  . ALA B 1 42  ? 13.972  3.361  22.534 1.00 19.83 ? 59  ALA B CB  1 
ATOM   1484 N N   . MET B 1 43  ? 15.648  5.040  24.670 1.00 18.34 ? 60  MET B N   1 
ATOM   1485 C CA  . MET B 1 43  ? 16.859  5.794  24.955 1.00 17.65 ? 60  MET B CA  1 
ATOM   1486 C C   . MET B 1 43  ? 17.741  4.892  25.792 1.00 19.74 ? 60  MET B C   1 
ATOM   1487 O O   . MET B 1 43  ? 17.272  4.320  26.781 1.00 21.31 ? 60  MET B O   1 
ATOM   1488 C CB  . MET B 1 43  ? 16.508  7.088  25.708 1.00 19.34 ? 60  MET B CB  1 
ATOM   1489 C CG  . MET B 1 43  ? 17.676  8.060  25.938 1.00 20.88 ? 60  MET B CG  1 
ATOM   1490 S SD  . MET B 1 43  ? 17.125  9.751  26.349 1.00 21.08 ? 60  MET B SD  1 
ATOM   1491 C CE  . MET B 1 43  ? 16.658  10.355 24.743 1.00 18.86 ? 60  MET B CE  1 
ATOM   1492 N N   . LYS B 1 44  ? 18.997  4.751  25.388 1.00 18.51 ? 61  LYS B N   1 
ATOM   1493 C CA  . LYS B 1 44  ? 19.949  3.909  26.104 1.00 20.70 ? 61  LYS B CA  1 
ATOM   1494 C C   . LYS B 1 44  ? 21.352  4.443  25.866 1.00 18.38 ? 61  LYS B C   1 
ATOM   1495 O O   . LYS B 1 44  ? 21.736  4.669  24.715 1.00 20.18 ? 61  LYS B O   1 
ATOM   1496 C CB  . LYS B 1 44  ? 19.837  2.471  25.573 1.00 23.19 ? 61  LYS B CB  1 
ATOM   1497 C CG  . LYS B 1 44  ? 20.938  1.531  25.977 1.00 28.70 ? 61  LYS B CG  1 
ATOM   1498 C CD  . LYS B 1 44  ? 20.591  0.100  25.588 1.00 32.54 ? 61  LYS B CD  1 
ATOM   1499 C CE  . LYS B 1 44  ? 20.600  -0.096 24.084 1.00 30.29 ? 61  LYS B CE  1 
ATOM   1500 N NZ  . LYS B 1 44  ? 20.359  -1.529 23.748 1.00 31.75 ? 61  LYS B NZ  1 
ATOM   1501 N N   . LEU B 1 45  ? 22.125  4.620  26.940 1.00 17.98 ? 62  LEU B N   1 
ATOM   1502 C CA  . LEU B 1 45  ? 23.549  4.889  26.811 1.00 17.04 ? 62  LEU B CA  1 
ATOM   1503 C C   . LEU B 1 45  ? 24.300  3.564  26.746 1.00 18.03 ? 62  LEU B C   1 
ATOM   1504 O O   . LEU B 1 45  ? 24.092  2.669  27.572 1.00 18.16 ? 62  LEU B O   1 
ATOM   1505 C CB  . LEU B 1 45  ? 24.088  5.709  27.982 1.00 18.98 ? 62  LEU B CB  1 
ATOM   1506 C CG  . LEU B 1 45  ? 25.554  6.132  27.864 1.00 18.67 ? 62  LEU B CG  1 
ATOM   1507 C CD1 . LEU B 1 45  ? 25.708  7.375  27.001 1.00 20.37 ? 62  LEU B CD1 1 
ATOM   1508 C CD2 . LEU B 1 45  ? 26.186  6.317  29.263 1.00 21.50 ? 62  LEU B CD2 1 
ATOM   1509 N N   . THR B 1 46  ? 25.181  3.438  25.775 1.00 16.62 ? 63  THR B N   1 
ATOM   1510 C CA  . THR B 1 46  ? 26.055  2.281  25.706 1.00 16.48 ? 63  THR B CA  1 
ATOM   1511 C C   . THR B 1 46  ? 27.424  2.753  25.246 1.00 16.34 ? 63  THR B C   1 
ATOM   1512 O O   . THR B 1 46  ? 27.638  3.941  25.017 1.00 18.60 ? 63  THR B O   1 
ATOM   1513 C CB  . THR B 1 46  ? 25.442  1.190  24.833 1.00 19.51 ? 63  THR B CB  1 
ATOM   1514 O OG1 . THR B 1 46  ? 26.201  -0.011 24.998 1.00 22.25 ? 63  THR B OG1 1 
ATOM   1515 C CG2 . THR B 1 46  ? 25.420  1.596  23.358 1.00 21.27 ? 63  THR B CG2 1 
ATOM   1516 N N   . ILE B 1 47  ? 28.378  1.832  25.175 1.00 17.53 ? 64  ILE B N   1 
ATOM   1517 C CA  . ILE B 1 47  ? 29.652  2.091  24.511 1.00 18.52 ? 64  ILE B CA  1 
ATOM   1518 C C   . ILE B 1 47  ? 29.661  1.264  23.235 1.00 18.05 ? 64  ILE B C   1 
ATOM   1519 O O   . ILE B 1 47  ? 29.560  0.028  23.271 1.00 19.18 ? 64  ILE B O   1 
ATOM   1520 C CB  . ILE B 1 47  ? 30.865  1.816  25.415 1.00 19.54 ? 64  ILE B CB  1 
ATOM   1521 C CG1 . ILE B 1 47  ? 30.911  2.879  26.527 1.00 20.94 ? 64  ILE B CG1 1 
ATOM   1522 C CG2 . ILE B 1 47  ? 32.151  1.841  24.601 1.00 24.43 ? 64  ILE B CG2 1 
ATOM   1523 C CD1 . ILE B 1 47  ? 31.972  2.622  27.604 1.00 23.30 ? 64  ILE B CD1 1 
ATOM   1524 N N   . ALA B 1 48  ? 29.742  1.954  22.108 1.00 18.06 ? 65  ALA B N   1 
ATOM   1525 C CA  . ALA B 1 48  ? 29.797  1.270  20.828 1.00 17.03 ? 65  ALA B CA  1 
ATOM   1526 C C   . ALA B 1 48  ? 31.123  0.541  20.677 1.00 18.39 ? 65  ALA B C   1 
ATOM   1527 O O   . ALA B 1 48  ? 32.182  1.059  21.032 1.00 19.14 ? 65  ALA B O   1 
ATOM   1528 C CB  . ALA B 1 48  ? 29.623  2.303  19.717 1.00 16.99 ? 65  ALA B CB  1 
ATOM   1529 N N   . THR B 1 49  ? 31.055  -0.674 20.156 1.00 18.18 ? 66  THR B N   1 
ATOM   1530 C CA  . THR B 1 49  ? 32.219  -1.510 19.942 1.00 17.58 ? 66  THR B CA  1 
ATOM   1531 C C   . THR B 1 49  ? 32.398  -1.788 18.457 1.00 17.04 ? 66  THR B C   1 
ATOM   1532 O O   . THR B 1 49  ? 31.450  -1.658 17.671 1.00 18.36 ? 66  THR B O   1 
ATOM   1533 C CB  . THR B 1 49  ? 32.047  -2.861 20.645 1.00 19.42 ? 66  THR B CB  1 
ATOM   1534 O OG1 . THR B 1 49  ? 30.949  -3.550 20.026 1.00 22.44 ? 66  THR B OG1 1 
ATOM   1535 C CG2 . THR B 1 49  ? 31.792  -2.671 22.140 1.00 23.16 ? 66  THR B CG2 1 
ATOM   1536 N N   . PRO B 1 50  ? 33.602  -2.193 18.039 1.00 19.41 ? 67  PRO B N   1 
ATOM   1537 C CA  . PRO B 1 50  ? 33.807  -2.486 16.619 1.00 20.66 ? 67  PRO B CA  1 
ATOM   1538 C C   . PRO B 1 50  ? 32.821  -3.485 16.042 1.00 20.34 ? 67  PRO B C   1 
ATOM   1539 O O   . PRO B 1 50  ? 32.359  -3.275 14.919 1.00 21.95 ? 67  PRO B O   1 
ATOM   1540 C CB  . PRO B 1 50  ? 35.257  -2.985 16.582 1.00 22.37 ? 67  PRO B CB  1 
ATOM   1541 C CG  . PRO B 1 50  ? 35.915  -2.221 17.669 1.00 22.15 ? 67  PRO B CG  1 
ATOM   1542 C CD  . PRO B 1 50  ? 34.877  -2.170 18.777 1.00 22.54 ? 67  PRO B CD  1 
ATOM   1543 N N   . ALA B 1 51  ? 32.445  -4.539 16.770 1.00 19.82 ? 68  ALA B N   1 
ATOM   1544 C CA  . ALA B 1 51  ? 31.580  -5.547 16.163 1.00 19.83 ? 68  ALA B CA  1 
ATOM   1545 C C   . ALA B 1 51  ? 30.211  -4.977 15.849 1.00 19.38 ? 68  ALA B C   1 
ATOM   1546 O O   . ALA B 1 51  ? 29.630  -5.284 14.804 1.00 21.65 ? 68  ALA B O   1 
ATOM   1547 C CB  . ALA B 1 51  ? 31.453  -6.784 17.051 1.00 21.53 ? 68  ALA B CB  1 
ATOM   1548 N N   . ILE B 1 52  ? 29.665  -4.153 16.743 1.00 21.08 ? 69  ILE B N   1 
ATOM   1549 C CA  A ILE B 1 52  ? 28.352  -3.595 16.451 0.64 19.73 ? 69  ILE B CA  1 
ATOM   1550 C CA  B ILE B 1 52  ? 28.357  -3.550 16.497 0.36 21.44 ? 69  ILE B CA  1 
ATOM   1551 C C   . ILE B 1 52  ? 28.461  -2.507 15.392 1.00 19.66 ? 69  ILE B C   1 
ATOM   1552 O O   . ILE B 1 52  ? 27.578  -2.377 14.542 1.00 21.06 ? 69  ILE B O   1 
ATOM   1553 C CB  A ILE B 1 52  ? 27.605  -3.131 17.713 0.64 20.88 ? 69  ILE B CB  1 
ATOM   1554 C CB  B ILE B 1 52  ? 27.808  -2.941 17.802 0.36 25.05 ? 69  ILE B CB  1 
ATOM   1555 C CG1 A ILE B 1 52  ? 26.140  -2.835 17.360 0.64 28.54 ? 69  ILE B CG1 1 
ATOM   1556 C CG1 B ILE B 1 52  ? 27.779  -3.981 18.928 0.36 26.53 ? 69  ILE B CG1 1 
ATOM   1557 C CG2 A ILE B 1 52  ? 28.252  -1.899 18.313 0.64 21.98 ? 69  ILE B CG2 1 
ATOM   1558 C CG2 B ILE B 1 52  ? 26.410  -2.366 17.582 0.36 28.43 ? 69  ILE B CG2 1 
ATOM   1559 C CD1 A ILE B 1 52  ? 25.218  -2.800 18.551 0.64 30.17 ? 69  ILE B CD1 1 
ATOM   1560 C CD1 B ILE B 1 52  ? 27.695  -3.383 20.319 0.36 28.60 ? 69  ILE B CD1 1 
ATOM   1561 N N   . LEU B 1 53  ? 29.542  -1.731 15.411 1.00 18.55 ? 70  LEU B N   1 
ATOM   1562 C CA  . LEU B 1 53  ? 29.721  -0.690 14.413 1.00 19.44 ? 70  LEU B CA  1 
ATOM   1563 C C   . LEU B 1 53  ? 29.926  -1.275 13.027 1.00 22.64 ? 70  LEU B C   1 
ATOM   1564 O O   . LEU B 1 53  ? 29.517  -0.658 12.044 1.00 22.06 ? 70  LEU B O   1 
ATOM   1565 C CB  . LEU B 1 53  ? 30.885  0.216  14.804 1.00 19.41 ? 70  LEU B CB  1 
ATOM   1566 C CG  . LEU B 1 53  ? 30.632  1.047  16.061 1.00 19.02 ? 70  LEU B CG  1 
ATOM   1567 C CD1 . LEU B 1 53  ? 31.943  1.608  16.551 1.00 19.24 ? 70  LEU B CD1 1 
ATOM   1568 C CD2 . LEU B 1 53  ? 29.625  2.163  15.786 1.00 21.07 ? 70  LEU B CD2 1 
ATOM   1569 N N   . GLU B 1 54  ? 30.545  -2.453 12.920 1.00 23.60 ? 71  GLU B N   1 
ATOM   1570 C CA  A GLU B 1 54  ? 30.685  -3.077 11.609 0.47 26.65 ? 71  GLU B CA  1 
ATOM   1571 C CA  B GLU B 1 54  ? 30.690  -3.076 11.606 0.53 26.33 ? 71  GLU B CA  1 
ATOM   1572 C C   . GLU B 1 54  ? 29.325  -3.394 11.009 1.00 27.30 ? 71  GLU B C   1 
ATOM   1573 O O   . GLU B 1 54  ? 29.119  -3.236 9.799  1.00 27.07 ? 71  GLU B O   1 
ATOM   1574 C CB  A GLU B 1 54  ? 31.520  -4.347 11.724 0.47 32.55 ? 71  GLU B CB  1 
ATOM   1575 C CB  B GLU B 1 54  ? 31.560  -4.334 11.704 0.53 32.33 ? 71  GLU B CB  1 
ATOM   1576 C CG  A GLU B 1 54  ? 33.003  -4.106 11.705 0.47 38.28 ? 71  GLU B CG  1 
ATOM   1577 C CG  B GLU B 1 54  ? 31.979  -4.933 10.348 0.53 39.08 ? 71  GLU B CG  1 
ATOM   1578 C CD  A GLU B 1 54  ? 33.760  -5.349 12.078 0.47 43.18 ? 71  GLU B CD  1 
ATOM   1579 C CD  B GLU B 1 54  ? 33.235  -4.292 9.759  0.53 45.56 ? 71  GLU B CD  1 
ATOM   1580 O OE1 A GLU B 1 54  ? 33.442  -6.410 11.500 0.47 45.33 ? 71  GLU B OE1 1 
ATOM   1581 O OE1 B GLU B 1 54  ? 34.151  -3.945 10.535 0.53 48.91 ? 71  GLU B OE1 1 
ATOM   1582 O OE2 A GLU B 1 54  ? 34.642  -5.268 12.961 0.47 45.89 ? 71  GLU B OE2 1 
ATOM   1583 O OE2 B GLU B 1 54  ? 33.311  -4.145 8.515  0.53 46.72 ? 71  GLU B OE2 1 
ATOM   1584 N N   . GLU B 1 55  ? 28.384  -3.862 11.837 1.00 25.38 ? 72  GLU B N   1 
ATOM   1585 C CA  . GLU B 1 55  ? 27.030  -4.113 11.348 1.00 26.42 ? 72  GLU B CA  1 
ATOM   1586 C C   . GLU B 1 55  ? 26.312  -2.810 11.030 1.00 25.00 ? 72  GLU B C   1 
ATOM   1587 O O   . GLU B 1 55  ? 25.601  -2.708 10.024 1.00 27.71 ? 72  GLU B O   1 
ATOM   1588 C CB  . GLU B 1 55  ? 26.231  -4.879 12.397 1.00 31.76 ? 72  GLU B CB  1 
ATOM   1589 C CG  . GLU B 1 55  ? 26.682  -6.300 12.594 1.00 43.56 ? 72  GLU B CG  1 
ATOM   1590 C CD  . GLU B 1 55  ? 25.740  -7.271 11.936 1.00 52.59 ? 72  GLU B CD  1 
ATOM   1591 O OE1 . GLU B 1 55  ? 24.698  -7.567 12.565 1.00 55.98 ? 72  GLU B OE1 1 
ATOM   1592 O OE2 . GLU B 1 55  ? 26.029  -7.710 10.800 1.00 55.92 ? 72  GLU B OE2 1 
ATOM   1593 N N   . HIS B 1 56  ? 26.468  -1.806 11.893 1.00 23.08 ? 73  HIS B N   1 
ATOM   1594 C CA  . HIS B 1 56  ? 25.821  -0.522 11.645 1.00 23.30 ? 73  HIS B CA  1 
ATOM   1595 C C   . HIS B 1 56  ? 26.263  0.045  10.306 1.00 24.13 ? 73  HIS B C   1 
ATOM   1596 O O   . HIS B 1 56  ? 25.442  0.552  9.527  1.00 26.30 ? 73  HIS B O   1 
ATOM   1597 C CB  . HIS B 1 56  ? 26.193  0.430  12.778 1.00 21.30 ? 73  HIS B CB  1 
ATOM   1598 C CG  . HIS B 1 56  ? 25.614  1.797  12.636 1.00 24.24 ? 73  HIS B CG  1 
ATOM   1599 N ND1 . HIS B 1 56  ? 24.289  2.073  12.896 1.00 24.28 ? 73  HIS B ND1 1 
ATOM   1600 C CD2 . HIS B 1 56  ? 26.172  2.963  12.234 1.00 24.87 ? 73  HIS B CD2 1 
ATOM   1601 C CE1 . HIS B 1 56  ? 24.062  3.355  12.674 1.00 25.51 ? 73  HIS B CE1 1 
ATOM   1602 N NE2 . HIS B 1 56  ? 25.188  3.918  12.273 1.00 27.59 ? 73  HIS B NE2 1 
ATOM   1603 N N   . TYR B 1 57  ? 27.558  -0.051 10.015 1.00 24.18 ? 74  TYR B N   1 
ATOM   1604 C CA  . TYR B 1 57  ? 28.152  0.475  8.795  1.00 23.35 ? 74  TYR B CA  1 
ATOM   1605 C C   . TYR B 1 57  ? 28.390  -0.611 7.759  1.00 25.18 ? 74  TYR B C   1 
ATOM   1606 O O   . TYR B 1 57  ? 29.347  -0.527 6.982  1.00 28.75 ? 74  TYR B O   1 
ATOM   1607 C CB  . TYR B 1 57  ? 29.470  1.171  9.122  1.00 25.09 ? 74  TYR B CB  1 
ATOM   1608 C CG  . TYR B 1 57  ? 29.347  2.453  9.902  1.00 24.53 ? 74  TYR B CG  1 
ATOM   1609 C CD1 . TYR B 1 57  ? 28.630  3.533  9.405  1.00 27.83 ? 74  TYR B CD1 1 
ATOM   1610 C CD2 . TYR B 1 57  ? 29.988  2.600  11.120 1.00 27.44 ? 74  TYR B CD2 1 
ATOM   1611 C CE1 . TYR B 1 57  ? 28.543  4.722  10.105 1.00 29.02 ? 74  TYR B CE1 1 
ATOM   1612 C CE2 . TYR B 1 57  ? 29.905  3.768  11.830 1.00 27.30 ? 74  TYR B CE2 1 
ATOM   1613 C CZ  . TYR B 1 57  ? 29.183  4.834  11.323 1.00 28.74 ? 74  TYR B CZ  1 
ATOM   1614 O OH  . TYR B 1 57  ? 29.108  6.016  12.042 1.00 31.70 ? 74  TYR B OH  1 
ATOM   1615 N N   . ALA B 1 58  ? 27.539  -1.638 7.738  1.00 27.67 ? 75  ALA B N   1 
ATOM   1616 C CA  . ALA B 1 58  ? 27.754  -2.753 6.821  1.00 30.57 ? 75  ALA B CA  1 
ATOM   1617 C C   . ALA B 1 58  ? 27.852  -2.296 5.371  1.00 33.16 ? 75  ALA B C   1 
ATOM   1618 O O   . ALA B 1 58  ? 28.600  -2.887 4.583  1.00 33.60 ? 75  ALA B O   1 
ATOM   1619 C CB  . ALA B 1 58  ? 26.628  -3.779 6.975  1.00 31.69 ? 75  ALA B CB  1 
ATOM   1620 N N   . GLU B 1 59  ? 27.122  -1.251 4.995  1.00 34.70 ? 76  GLU B N   1 
ATOM   1621 C CA  . GLU B 1 59  ? 27.185  -0.798 3.609  1.00 37.49 ? 76  GLU B CA  1 
ATOM   1622 C C   . GLU B 1 59  ? 28.583  -0.335 3.219  1.00 37.47 ? 76  GLU B C   1 
ATOM   1623 O O   . GLU B 1 59  ? 28.918  -0.344 2.030  1.00 37.55 ? 76  GLU B O   1 
ATOM   1624 C CB  . GLU B 1 59  ? 26.164  0.318  3.380  1.00 44.43 ? 76  GLU B CB  1 
ATOM   1625 C CG  . GLU B 1 59  ? 26.374  1.549  4.235  1.00 49.96 ? 76  GLU B CG  1 
ATOM   1626 C CD  . GLU B 1 59  ? 25.129  2.428  4.318  1.00 53.17 ? 76  GLU B CD  1 
ATOM   1627 O OE1 . GLU B 1 59  ? 24.687  2.936  3.261  1.00 55.75 ? 76  GLU B OE1 1 
ATOM   1628 O OE2 . GLU B 1 59  ? 24.591  2.602  5.442  1.00 52.05 ? 76  GLU B OE2 1 
ATOM   1629 N N   . HIS B 1 60  ? 29.409  0.056  4.187  1.00 34.38 ? 77  HIS B N   1 
ATOM   1630 C CA  . HIS B 1 60  ? 30.737  0.594  3.922  1.00 35.82 ? 77  HIS B CA  1 
ATOM   1631 C C   . HIS B 1 60  ? 31.851  -0.425 4.124  1.00 34.85 ? 77  HIS B C   1 
ATOM   1632 O O   . HIS B 1 60  ? 33.028  -0.052 4.078  1.00 33.99 ? 77  HIS B O   1 
ATOM   1633 C CB  . HIS B 1 60  ? 30.991  1.811  4.807  1.00 35.42 ? 77  HIS B CB  1 
ATOM   1634 C CG  . HIS B 1 60  ? 29.985  2.898  4.626  1.00 36.85 ? 77  HIS B CG  1 
ATOM   1635 N ND1 . HIS B 1 60  ? 29.622  3.374  3.385  1.00 37.88 ? 77  HIS B ND1 1 
ATOM   1636 C CD2 . HIS B 1 60  ? 29.270  3.610  5.529  1.00 38.90 ? 77  HIS B CD2 1 
ATOM   1637 C CE1 . HIS B 1 60  ? 28.721  4.328  3.530  1.00 37.98 ? 77  HIS B CE1 1 
ATOM   1638 N NE2 . HIS B 1 60  ? 28.494  4.496  4.819  1.00 39.05 ? 77  HIS B NE2 1 
ATOM   1639 N N   . LYS B 1 61  ? 31.512  -1.696 4.331  1.00 35.88 ? 78  LYS B N   1 
ATOM   1640 C CA  . LYS B 1 61  ? 32.523  -2.723 4.556  1.00 39.26 ? 78  LYS B CA  1 
ATOM   1641 C C   . LYS B 1 61  ? 33.554  -2.714 3.437  1.00 38.86 ? 78  LYS B C   1 
ATOM   1642 O O   . LYS B 1 61  ? 33.206  -2.758 2.255  1.00 37.83 ? 78  LYS B O   1 
ATOM   1643 C CB  . LYS B 1 61  ? 31.846  -4.093 4.618  1.00 45.20 ? 78  LYS B CB  1 
ATOM   1644 C CG  . LYS B 1 61  ? 32.787  -5.240 4.975  1.00 51.76 ? 78  LYS B CG  1 
ATOM   1645 C CD  . LYS B 1 61  ? 32.026  -6.564 5.090  1.00 59.08 ? 78  LYS B CD  1 
ATOM   1646 C CE  . LYS B 1 61  ? 32.862  -7.755 4.625  1.00 64.18 ? 78  LYS B CE  1 
ATOM   1647 N NZ  . LYS B 1 61  ? 32.019  -8.810 3.975  1.00 67.62 ? 78  LYS B NZ  1 
ATOM   1648 N N   . GLY B 1 62  ? 34.832  -2.669 3.818  1.00 39.86 ? 79  GLY B N   1 
ATOM   1649 C CA  . GLY B 1 62  ? 35.920  -2.696 2.866  1.00 41.40 ? 79  GLY B CA  1 
ATOM   1650 C C   . GLY B 1 62  ? 36.374  -1.344 2.354  1.00 43.68 ? 79  GLY B C   1 
ATOM   1651 O O   . GLY B 1 62  ? 37.419  -1.271 1.692  1.00 45.37 ? 79  GLY B O   1 
ATOM   1652 N N   . LYS B 1 63  ? 35.642  -0.273 2.640  1.00 39.86 ? 80  LYS B N   1 
ATOM   1653 C CA  . LYS B 1 63  ? 36.060  1.025  2.142  1.00 38.20 ? 80  LYS B CA  1 
ATOM   1654 C C   . LYS B 1 63  ? 37.214  1.569  2.982  1.00 42.16 ? 80  LYS B C   1 
ATOM   1655 O O   . LYS B 1 63  ? 37.293  1.309  4.184  1.00 43.63 ? 80  LYS B O   1 
ATOM   1656 C CB  . LYS B 1 63  ? 34.887  1.995  2.165  1.00 36.91 ? 80  LYS B CB  1 
ATOM   1657 C CG  . LYS B 1 63  ? 33.719  1.519  1.308  1.00 38.93 ? 80  LYS B CG  1 
ATOM   1658 C CD  . LYS B 1 63  ? 32.524  2.455  1.364  1.00 40.95 ? 80  LYS B CD  1 
ATOM   1659 C CE  . LYS B 1 63  ? 31.429  1.966  0.427  1.00 42.90 ? 80  LYS B CE  1 
ATOM   1660 N NZ  . LYS B 1 63  ? 30.184  2.777  0.513  1.00 44.63 ? 80  LYS B NZ  1 
ATOM   1661 N N   . PRO B 1 64  ? 38.126  2.325  2.369  1.00 44.69 ? 81  PRO B N   1 
ATOM   1662 C CA  . PRO B 1 64  ? 39.339  2.734  3.097  1.00 43.69 ? 81  PRO B CA  1 
ATOM   1663 C C   . PRO B 1 64  ? 39.071  3.615  4.303  1.00 42.66 ? 81  PRO B C   1 
ATOM   1664 O O   . PRO B 1 64  ? 39.870  3.609  5.250  1.00 41.46 ? 81  PRO B O   1 
ATOM   1665 C CB  . PRO B 1 64  ? 40.171  3.457  2.026  1.00 48.48 ? 81  PRO B CB  1 
ATOM   1666 C CG  . PRO B 1 64  ? 39.183  3.861  0.978  1.00 50.88 ? 81  PRO B CG  1 
ATOM   1667 C CD  . PRO B 1 64  ? 38.136  2.790  0.968  1.00 48.98 ? 81  PRO B CD  1 
ATOM   1668 N N   . PHE B 1 65  ? 37.979  4.379  4.303  1.00 40.30 ? 82  PHE B N   1 
ATOM   1669 C CA  . PHE B 1 65  ? 37.700  5.254  5.433  1.00 37.87 ? 82  PHE B CA  1 
ATOM   1670 C C   . PHE B 1 65  ? 37.101  4.513  6.615  1.00 34.89 ? 82  PHE B C   1 
ATOM   1671 O O   . PHE B 1 65  ? 37.049  5.074  7.715  1.00 33.34 ? 82  PHE B O   1 
ATOM   1672 C CB  . PHE B 1 65  ? 36.747  6.385  5.028  1.00 36.43 ? 82  PHE B CB  1 
ATOM   1673 C CG  . PHE B 1 65  ? 35.371  5.916  4.632  1.00 36.71 ? 82  PHE B CG  1 
ATOM   1674 C CD1 . PHE B 1 65  ? 34.444  5.545  5.594  1.00 36.52 ? 82  PHE B CD1 1 
ATOM   1675 C CD2 . PHE B 1 65  ? 35.009  5.843  3.294  1.00 37.65 ? 82  PHE B CD2 1 
ATOM   1676 C CE1 . PHE B 1 65  ? 33.180  5.112  5.230  1.00 36.57 ? 82  PHE B CE1 1 
ATOM   1677 C CE2 . PHE B 1 65  ? 33.751  5.417  2.924  1.00 37.84 ? 82  PHE B CE2 1 
ATOM   1678 C CZ  . PHE B 1 65  ? 32.837  5.044  3.889  1.00 34.12 ? 82  PHE B CZ  1 
ATOM   1679 N N   . LEU B 1 66  ? 36.629  3.285  6.419  1.00 33.22 ? 83  LEU B N   1 
ATOM   1680 C CA  . LEU B 1 66  ? 35.883  2.622  7.487  1.00 32.14 ? 83  LEU B CA  1 
ATOM   1681 C C   . LEU B 1 66  ? 36.700  2.407  8.753  1.00 30.85 ? 83  LEU B C   1 
ATOM   1682 O O   . LEU B 1 66  ? 36.178  2.673  9.845  1.00 29.58 ? 83  LEU B O   1 
ATOM   1683 C CB  . LEU B 1 66  ? 35.245  1.325  6.982  1.00 32.74 ? 83  LEU B CB  1 
ATOM   1684 C CG  . LEU B 1 66  ? 34.345  0.646  8.020  1.00 32.58 ? 83  LEU B CG  1 
ATOM   1685 C CD1 . LEU B 1 66  ? 33.193  1.551  8.435  1.00 32.52 ? 83  LEU B CD1 1 
ATOM   1686 C CD2 . LEU B 1 66  ? 33.827  -0.680 7.502  1.00 32.93 ? 83  LEU B CD2 1 
ATOM   1687 N N   . PRO B 1 67  ? 37.936  1.916  8.708  1.00 31.12 ? 84  PRO B N   1 
ATOM   1688 C CA  . PRO B 1 67  ? 38.663  1.703  9.971  1.00 30.48 ? 84  PRO B CA  1 
ATOM   1689 C C   . PRO B 1 67  ? 38.746  2.957  10.832 1.00 30.02 ? 84  PRO B C   1 
ATOM   1690 O O   . PRO B 1 67  ? 38.526  2.895  12.050 1.00 30.15 ? 84  PRO B O   1 
ATOM   1691 C CB  . PRO B 1 67  ? 40.040  1.222  9.495  1.00 34.54 ? 84  PRO B CB  1 
ATOM   1692 C CG  . PRO B 1 67  ? 39.777  0.604  8.156  1.00 36.32 ? 84  PRO B CG  1 
ATOM   1693 C CD  . PRO B 1 67  ? 38.681  1.414  7.538  1.00 33.26 ? 84  PRO B CD  1 
ATOM   1694 N N   . GLY B 1 68  ? 39.036  4.110  10.226 1.00 31.03 ? 85  GLY B N   1 
ATOM   1695 C CA  . GLY B 1 68  ? 39.112  5.334  11.005 1.00 30.65 ? 85  GLY B CA  1 
ATOM   1696 C C   . GLY B 1 68  ? 37.763  5.788  11.525 1.00 27.81 ? 85  GLY B C   1 
ATOM   1697 O O   . GLY B 1 68  ? 37.674  6.367  12.610 1.00 28.65 ? 85  GLY B O   1 
ATOM   1698 N N   . LEU B 1 69  ? 36.706  5.563  10.748 1.00 26.91 ? 86  LEU B N   1 
ATOM   1699 C CA  . LEU B 1 69  ? 35.353  5.851  11.202 1.00 27.37 ? 86  LEU B CA  1 
ATOM   1700 C C   . LEU B 1 69  ? 34.994  4.996  12.409 1.00 27.22 ? 86  LEU B C   1 
ATOM   1701 O O   . LEU B 1 69  ? 34.414  5.488  13.382 1.00 26.51 ? 86  LEU B O   1 
ATOM   1702 C CB  . LEU B 1 69  ? 34.396  5.585  10.043 1.00 31.17 ? 86  LEU B CB  1 
ATOM   1703 C CG  . LEU B 1 69  ? 32.898  5.548  10.293 1.00 38.10 ? 86  LEU B CG  1 
ATOM   1704 C CD1 . LEU B 1 69  ? 32.453  6.831  10.930 1.00 41.85 ? 86  LEU B CD1 1 
ATOM   1705 C CD2 . LEU B 1 69  ? 32.208  5.332  8.965  1.00 39.29 ? 86  LEU B CD2 1 
ATOM   1706 N N   . ILE B 1 70  ? 35.356  3.715  12.374 1.00 26.34 ? 87  ILE B N   1 
ATOM   1707 C CA  A ILE B 1 70  ? 35.052  2.858  13.516 0.81 26.24 ? 87  ILE B CA  1 
ATOM   1708 C CA  B ILE B 1 70  ? 35.078  2.833  13.509 0.19 25.30 ? 87  ILE B CA  1 
ATOM   1709 C C   . ILE B 1 70  ? 35.820  3.316  14.746 1.00 23.68 ? 87  ILE B C   1 
ATOM   1710 O O   . ILE B 1 70  ? 35.281  3.306  15.862 1.00 23.72 ? 87  ILE B O   1 
ATOM   1711 C CB  A ILE B 1 70  ? 35.280  1.376  13.159 0.81 28.65 ? 87  ILE B CB  1 
ATOM   1712 C CB  B ILE B 1 70  ? 35.441  1.378  13.155 0.19 25.57 ? 87  ILE B CB  1 
ATOM   1713 C CG1 A ILE B 1 70  ? 34.163  0.917  12.211 0.81 32.28 ? 87  ILE B CG1 1 
ATOM   1714 C CG1 B ILE B 1 70  ? 34.629  0.883  11.951 0.19 25.18 ? 87  ILE B CG1 1 
ATOM   1715 C CG2 A ILE B 1 70  ? 35.342  0.518  14.426 0.81 28.44 ? 87  ILE B CG2 1 
ATOM   1716 C CG2 B ILE B 1 70  ? 35.233  0.466  14.360 0.19 25.97 ? 87  ILE B CG2 1 
ATOM   1717 C CD1 A ILE B 1 70  ? 34.254  -0.522 11.778 0.81 35.00 ? 87  ILE B CD1 1 
ATOM   1718 C CD1 B ILE B 1 70  ? 33.132  0.908  12.145 0.19 24.20 ? 87  ILE B CD1 1 
ATOM   1719 N N   . GLU B 1 71  ? 37.072  3.749  14.574 1.00 24.61 ? 88  GLU B N   1 
ATOM   1720 C CA  . GLU B 1 71  ? 37.842  4.260  15.705 1.00 28.64 ? 88  GLU B CA  1 
ATOM   1721 C C   . GLU B 1 71  ? 37.177  5.478  16.323 1.00 27.02 ? 88  GLU B C   1 
ATOM   1722 O O   . GLU B 1 71  ? 37.089  5.594  17.551 1.00 27.87 ? 88  GLU B O   1 
ATOM   1723 C CB  . GLU B 1 71  ? 39.245  4.643  15.255 1.00 35.11 ? 88  GLU B CB  1 
ATOM   1724 C CG  . GLU B 1 71  ? 40.213  3.505  15.192 1.00 45.51 ? 88  GLU B CG  1 
ATOM   1725 C CD  . GLU B 1 71  ? 41.624  4.002  14.953 1.00 50.92 ? 88  GLU B CD  1 
ATOM   1726 O OE1 . GLU B 1 71  ? 42.121  4.783  15.795 1.00 51.91 ? 88  GLU B OE1 1 
ATOM   1727 O OE2 . GLU B 1 71  ? 42.214  3.631  13.919 1.00 55.23 ? 88  GLU B OE2 1 
ATOM   1728 N N   . LYS B 1 72  ? 36.727  6.420  15.488 1.00 23.77 ? 89  LYS B N   1 
ATOM   1729 C CA  A LYS B 1 72  ? 36.092  7.611  16.035 0.60 24.93 ? 89  LYS B CA  1 
ATOM   1730 C CA  B LYS B 1 72  ? 36.077  7.615  16.013 0.40 23.97 ? 89  LYS B CA  1 
ATOM   1731 C C   . LYS B 1 72  ? 34.801  7.265  16.758 1.00 23.33 ? 89  LYS B C   1 
ATOM   1732 O O   . LYS B 1 72  ? 34.459  7.924  17.743 1.00 23.67 ? 89  LYS B O   1 
ATOM   1733 C CB  A LYS B 1 72  ? 35.865  8.646  14.934 0.60 28.63 ? 89  LYS B CB  1 
ATOM   1734 C CB  B LYS B 1 72  ? 35.738  8.583  14.880 0.40 25.82 ? 89  LYS B CB  1 
ATOM   1735 C CG  A LYS B 1 72  ? 37.178  9.200  14.410 0.60 30.32 ? 89  LYS B CG  1 
ATOM   1736 C CG  B LYS B 1 72  ? 36.933  9.296  14.283 0.40 25.98 ? 89  LYS B CG  1 
ATOM   1737 C CD  A LYS B 1 72  ? 37.016  10.245 13.326 0.60 32.39 ? 89  LYS B CD  1 
ATOM   1738 C CD  B LYS B 1 72  ? 36.510  10.627 13.700 0.40 30.11 ? 89  LYS B CD  1 
ATOM   1739 C CE  A LYS B 1 72  ? 38.378  10.587 12.713 0.60 36.03 ? 89  LYS B CE  1 
ATOM   1740 C CE  B LYS B 1 72  ? 37.624  11.278 12.904 0.40 31.30 ? 89  LYS B CE  1 
ATOM   1741 N NZ  A LYS B 1 72  ? 39.439  10.790 13.746 0.60 39.07 ? 89  LYS B NZ  1 
ATOM   1742 N NZ  B LYS B 1 72  ? 38.037  10.451 11.735 0.40 33.50 ? 89  LYS B NZ  1 
ATOM   1743 N N   . MET B 1 73  ? 34.091  6.236  16.296 1.00 21.76 ? 90  MET B N   1 
ATOM   1744 C CA  . MET B 1 73  ? 32.807  5.859  16.865 1.00 19.59 ? 90  MET B CA  1 
ATOM   1745 C C   . MET B 1 73  ? 32.915  4.878  18.023 1.00 18.99 ? 90  MET B C   1 
ATOM   1746 O O   . MET B 1 73  ? 31.891  4.602  18.650 1.00 20.20 ? 90  MET B O   1 
ATOM   1747 C CB  . MET B 1 73  ? 31.917  5.248  15.775 1.00 20.99 ? 90  MET B CB  1 
ATOM   1748 C CG  . MET B 1 73  ? 31.413  6.277  14.780 1.00 25.18 ? 90  MET B CG  1 
ATOM   1749 S SD  . MET B 1 73  ? 30.143  7.357  15.513 1.00 22.91 ? 90  MET B SD  1 
ATOM   1750 C CE  . MET B 1 73  ? 28.867  6.148  15.827 1.00 22.48 ? 90  MET B CE  1 
ATOM   1751 N N   . THR B 1 74  ? 34.099  4.340  18.315 1.00 18.51 ? 91  THR B N   1 
ATOM   1752 C CA  . THR B 1 74  ? 34.279  3.452  19.469 1.00 19.10 ? 91  THR B CA  1 
ATOM   1753 C C   . THR B 1 74  ? 34.364  4.321  20.717 1.00 20.11 ? 91  THR B C   1 
ATOM   1754 O O   . THR B 1 74  ? 35.402  4.923  21.020 1.00 23.64 ? 91  THR B O   1 
ATOM   1755 C CB  . THR B 1 74  ? 35.521  2.592  19.283 1.00 21.45 ? 91  THR B CB  1 
ATOM   1756 O OG1 . THR B 1 74  ? 35.369  1.811  18.093 1.00 24.22 ? 91  THR B OG1 1 
ATOM   1757 C CG2 . THR B 1 74  ? 35.724  1.645  20.463 1.00 22.78 ? 91  THR B CG2 1 
ATOM   1758 N N   . GLY B 1 75  ? 33.266  4.374  21.451 1.00 18.32 ? 92  GLY B N   1 
ATOM   1759 C CA  . GLY B 1 75  ? 33.141  5.274  22.566 1.00 18.54 ? 92  GLY B CA  1 
ATOM   1760 C C   . GLY B 1 75  ? 31.704  5.294  23.021 1.00 15.91 ? 92  GLY B C   1 
ATOM   1761 O O   . GLY B 1 75  ? 30.837  4.629  22.444 1.00 17.24 ? 92  GLY B O   1 
ATOM   1762 N N   . PRO B 1 76  ? 31.413  6.071  24.057 1.00 16.87 ? 93  PRO B N   1 
ATOM   1763 C CA  . PRO B 1 76  ? 30.023  6.207  24.496 1.00 15.74 ? 93  PRO B CA  1 
ATOM   1764 C C   . PRO B 1 76  ? 29.165  6.798  23.389 1.00 16.68 ? 93  PRO B C   1 
ATOM   1765 O O   . PRO B 1 76  ? 29.571  7.740  22.703 1.00 17.40 ? 93  PRO B O   1 
ATOM   1766 C CB  . PRO B 1 76  ? 30.129  7.162  25.692 1.00 17.73 ? 93  PRO B CB  1 
ATOM   1767 C CG  . PRO B 1 76  ? 31.350  7.959  25.416 1.00 17.55 ? 93  PRO B CG  1 
ATOM   1768 C CD  . PRO B 1 76  ? 32.313  7.001  24.768 1.00 19.44 ? 93  PRO B CD  1 
ATOM   1769 N N   . VAL B 1 77  ? 27.950  6.259  23.252 1.00 17.36 ? 94  VAL B N   1 
ATOM   1770 C CA  . VAL B 1 77  ? 26.926  6.806  22.370 1.00 17.16 ? 94  VAL B CA  1 
ATOM   1771 C C   . VAL B 1 77  ? 25.585  6.749  23.094 1.00 15.93 ? 94  VAL B C   1 
ATOM   1772 O O   . VAL B 1 77  ? 25.360  5.911  23.964 1.00 16.64 ? 94  VAL B O   1 
ATOM   1773 C CB  . VAL B 1 77  ? 26.826  6.031  21.035 1.00 16.70 ? 94  VAL B CB  1 
ATOM   1774 C CG1 . VAL B 1 77  ? 28.129  6.111  20.266 1.00 17.42 ? 94  VAL B CG1 1 
ATOM   1775 C CG2 . VAL B 1 77  ? 26.440  4.561  21.284 1.00 16.26 ? 94  VAL B CG2 1 
ATOM   1776 N N   . LEU B 1 78  ? 24.669  7.633  22.693 1.00 15.90 ? 95  LEU B N   1 
ATOM   1777 C CA  . LEU B 1 78  ? 23.299  7.599  23.200 1.00 15.49 ? 95  LEU B CA  1 
ATOM   1778 C C   . LEU B 1 78  ? 22.404  7.114  22.066 1.00 16.51 ? 95  LEU B C   1 
ATOM   1779 O O   . LEU B 1 78  ? 22.208  7.820  21.070 1.00 15.61 ? 95  LEU B O   1 
ATOM   1780 C CB  . LEU B 1 78  ? 22.843  8.946  23.758 1.00 15.71 ? 95  LEU B CB  1 
ATOM   1781 C CG  . LEU B 1 78  ? 21.526  8.850  24.559 1.00 16.34 ? 95  LEU B CG  1 
ATOM   1782 C CD1 . LEU B 1 78  ? 21.675  8.056  25.857 1.00 20.42 ? 95  LEU B CD1 1 
ATOM   1783 C CD2 . LEU B 1 78  ? 20.925  10.227 24.870 1.00 16.59 ? 95  LEU B CD2 1 
ATOM   1784 N N   . CYS B 1 79  ? 21.904  5.889  22.209 1.00 17.07 ? 96  CYS B N   1 
ATOM   1785 C CA  . CYS B 1 79  ? 20.938  5.324  21.285 1.00 16.65 ? 96  CYS B CA  1 
ATOM   1786 C C   . CYS B 1 79  ? 19.558  5.871  21.611 1.00 15.11 ? 96  CYS B C   1 
ATOM   1787 O O   . CYS B 1 79  ? 19.156  5.933  22.783 1.00 17.30 ? 96  CYS B O   1 
ATOM   1788 C CB  . CYS B 1 79  ? 20.916  3.806  21.452 1.00 18.35 ? 96  CYS B CB  1 
ATOM   1789 S SG  . CYS B 1 79  ? 22.538  3.016  21.381 1.00 19.37 ? 96  CYS B SG  1 
ATOM   1790 N N   . MET B 1 80  ? 18.818  6.272  20.575 1.00 16.91 ? 97  MET B N   1 
ATOM   1791 C CA  . MET B 1 80  ? 17.519  6.897  20.770 1.00 16.16 ? 97  MET B CA  1 
ATOM   1792 C C   . MET B 1 80  ? 16.561  6.464  19.671 1.00 16.59 ? 97  MET B C   1 
ATOM   1793 O O   . MET B 1 80  ? 16.956  6.253  18.522 1.00 17.14 ? 97  MET B O   1 
ATOM   1794 C CB  . MET B 1 80  ? 17.600  8.447  20.771 1.00 17.16 ? 97  MET B CB  1 
ATOM   1795 C CG  . MET B 1 80  ? 18.741  9.015  21.622 1.00 17.88 ? 97  MET B CG  1 
ATOM   1796 S SD  . MET B 1 80  ? 18.802  10.821 21.665 1.00 17.86 ? 97  MET B SD  1 
ATOM   1797 C CE  . MET B 1 80  ? 19.151  11.239 19.964 1.00 20.22 ? 97  MET B CE  1 
ATOM   1798 N N   . VAL B 1 81  ? 15.285  6.351  20.028 1.00 15.68 ? 98  VAL B N   1 
ATOM   1799 C CA  . VAL B 1 81  ? 14.209  6.262  19.048 1.00 16.64 ? 98  VAL B CA  1 
ATOM   1800 C C   . VAL B 1 81  ? 13.247  7.407  19.314 1.00 15.80 ? 98  VAL B C   1 
ATOM   1801 O O   . VAL B 1 81  ? 12.744  7.561  20.434 1.00 16.47 ? 98  VAL B O   1 
ATOM   1802 C CB  . VAL B 1 81  ? 13.481  4.908  19.082 1.00 18.82 ? 98  VAL B CB  1 
ATOM   1803 C CG1 . VAL B 1 81  ? 12.316  4.885  18.089 1.00 17.46 ? 98  VAL B CG1 1 
ATOM   1804 C CG2 . VAL B 1 81  ? 14.450  3.781  18.774 1.00 18.82 ? 98  VAL B CG2 1 
ATOM   1805 N N   . PHE B 1 82  ? 13.001  8.218  18.299 1.00 17.13 ? 99  PHE B N   1 
ATOM   1806 C CA  . PHE B 1 82  ? 12.005  9.281  18.369 1.00 15.33 ? 99  PHE B CA  1 
ATOM   1807 C C   . PHE B 1 82  ? 10.854  8.975  17.425 1.00 15.50 ? 99  PHE B C   1 
ATOM   1808 O O   . PHE B 1 82  ? 11.048  8.444  16.327 1.00 16.73 ? 99  PHE B O   1 
ATOM   1809 C CB  . PHE B 1 82  ? 12.599  10.652 18.020 1.00 17.04 ? 99  PHE B CB  1 
ATOM   1810 C CG  . PHE B 1 82  ? 13.269  11.332 19.186 1.00 16.04 ? 99  PHE B CG  1 
ATOM   1811 C CD1 . PHE B 1 82  ? 12.546  12.126 20.055 1.00 17.21 ? 99  PHE B CD1 1 
ATOM   1812 C CD2 . PHE B 1 82  ? 14.609  11.149 19.421 1.00 18.36 ? 99  PHE B CD2 1 
ATOM   1813 C CE1 . PHE B 1 82  ? 13.171  12.742 21.134 1.00 18.10 ? 99  PHE B CE1 1 
ATOM   1814 C CE2 . PHE B 1 82  ? 15.242  11.746 20.511 1.00 16.52 ? 99  PHE B CE2 1 
ATOM   1815 C CZ  . PHE B 1 82  ? 14.526  12.559 21.354 1.00 18.34 ? 99  PHE B CZ  1 
ATOM   1816 N N   . GLU B 1 83  ? 9.656   9.373  17.835 1.00 16.42 ? 100 GLU B N   1 
ATOM   1817 C CA  . GLU B 1 83  ? 8.436   9.139  17.075 1.00 15.97 ? 100 GLU B CA  1 
ATOM   1818 C C   . GLU B 1 83  ? 7.777   10.465 16.724 1.00 13.88 ? 100 GLU B C   1 
ATOM   1819 O O   . GLU B 1 83  ? 7.646   11.344 17.572 1.00 15.48 ? 100 GLU B O   1 
ATOM   1820 C CB  . GLU B 1 83  ? 7.460   8.330  17.919 1.00 16.39 ? 100 GLU B CB  1 
ATOM   1821 C CG  . GLU B 1 83  ? 6.106   8.093  17.304 1.00 20.26 ? 100 GLU B CG  1 
ATOM   1822 C CD  . GLU B 1 83  ? 5.212   7.299  18.235 1.00 18.52 ? 100 GLU B CD  1 
ATOM   1823 O OE1 . GLU B 1 83  ? 5.315   6.047  18.234 1.00 18.95 ? 100 GLU B OE1 1 
ATOM   1824 O OE2 . GLU B 1 83  ? 4.434   7.928  19.008 1.00 20.45 ? 100 GLU B OE2 1 
ATOM   1825 N N   . GLY B 1 84  ? 7.314   10.590 15.483 1.00 16.67 ? 101 GLY B N   1 
ATOM   1826 C CA  . GLY B 1 84  ? 6.577   11.771 15.070 1.00 17.38 ? 101 GLY B CA  1 
ATOM   1827 C C   . GLY B 1 84  ? 6.148   11.628 13.623 1.00 16.04 ? 101 GLY B C   1 
ATOM   1828 O O   . GLY B 1 84  ? 6.512   10.673 12.936 1.00 16.86 ? 101 GLY B O   1 
ATOM   1829 N N   . VAL B 1 85  ? 5.355   12.606 13.169 1.00 16.58 ? 102 VAL B N   1 
ATOM   1830 C CA  . VAL B 1 85  ? 4.985   12.655 11.751 1.00 16.28 ? 102 VAL B CA  1 
ATOM   1831 C C   . VAL B 1 85  ? 6.236   12.865 10.907 1.00 16.60 ? 102 VAL B C   1 
ATOM   1832 O O   . VAL B 1 85  ? 7.011   13.799 11.141 1.00 16.80 ? 102 VAL B O   1 
ATOM   1833 C CB  . VAL B 1 85  ? 3.969   13.783 11.523 1.00 16.98 ? 102 VAL B CB  1 
ATOM   1834 C CG1 . VAL B 1 85  ? 3.694   13.958 10.041 1.00 18.27 ? 102 VAL B CG1 1 
ATOM   1835 C CG2 . VAL B 1 85  ? 2.686   13.505 12.289 1.00 19.12 ? 102 VAL B CG2 1 
ATOM   1836 N N   . ASP B 1 86  ? 6.457   11.981 9.931  1.00 15.06 ? 103 ASP B N   1 
ATOM   1837 C CA  . ASP B 1 86  ? 7.540   12.166 8.954  1.00 15.78 ? 103 ASP B CA  1 
ATOM   1838 C C   . ASP B 1 86  ? 8.888   12.298 9.659  1.00 15.26 ? 103 ASP B C   1 
ATOM   1839 O O   . ASP B 1 86  ? 9.809   12.936 9.163  1.00 17.47 ? 103 ASP B O   1 
ATOM   1840 C CB  . ASP B 1 86  ? 7.232   13.400 8.092  1.00 17.53 ? 103 ASP B CB  1 
ATOM   1841 C CG  . ASP B 1 86  ? 8.112   13.534 6.849  1.00 18.51 ? 103 ASP B CG  1 
ATOM   1842 O OD1 . ASP B 1 86  ? 8.430   12.525 6.184  1.00 19.11 ? 103 ASP B OD1 1 
ATOM   1843 O OD2 . ASP B 1 86  ? 8.442   14.695 6.518  1.00 19.53 ? 103 ASP B OD2 1 
ATOM   1844 N N   . VAL B 1 87  ? 9.022   11.691 10.839 1.00 15.28 ? 104 VAL B N   1 
ATOM   1845 C CA  . VAL B 1 87  ? 10.187  11.970 11.663 1.00 16.23 ? 104 VAL B CA  1 
ATOM   1846 C C   . VAL B 1 87  ? 11.483  11.467 11.045 1.00 17.61 ? 104 VAL B C   1 
ATOM   1847 O O   . VAL B 1 87  ? 12.551  11.985 11.368 1.00 16.38 ? 104 VAL B O   1 
ATOM   1848 C CB  . VAL B 1 87  ? 9.980   11.416 13.087 1.00 14.84 ? 104 VAL B CB  1 
ATOM   1849 C CG1 . VAL B 1 87  ? 10.141  9.883  13.123 1.00 18.11 ? 104 VAL B CG1 1 
ATOM   1850 C CG2 . VAL B 1 87  ? 10.955  12.088 14.056 1.00 15.93 ? 104 VAL B CG2 1 
ATOM   1851 N N   . ILE B 1 88  ? 11.447  10.449 10.183 1.00 16.00 ? 105 ILE B N   1 
ATOM   1852 C CA  . ILE B 1 88  ? 12.697  9.993  9.579  1.00 15.25 ? 105 ILE B CA  1 
ATOM   1853 C C   . ILE B 1 88  ? 13.305  11.109 8.726  1.00 14.95 ? 105 ILE B C   1 
ATOM   1854 O O   . ILE B 1 88  ? 14.446  11.529 8.929  1.00 15.89 ? 105 ILE B O   1 
ATOM   1855 C CB  . ILE B 1 88  ? 12.485  8.699  8.775  1.00 16.64 ? 105 ILE B CB  1 
ATOM   1856 C CG1 . ILE B 1 88  ? 12.099  7.520  9.688  1.00 19.75 ? 105 ILE B CG1 1 
ATOM   1857 C CG2 . ILE B 1 88  ? 13.756  8.355  8.030  1.00 17.79 ? 105 ILE B CG2 1 
ATOM   1858 C CD1 . ILE B 1 88  ? 11.500  6.345  8.893  1.00 21.64 ? 105 ILE B CD1 1 
ATOM   1859 N N   . ALA B 1 89  ? 12.539  11.605 7.750  1.00 15.21 ? 106 ALA B N   1 
ATOM   1860 C CA  . ALA B 1 89  ? 13.033  12.698 6.929  1.00 18.86 ? 106 ALA B CA  1 
ATOM   1861 C C   . ALA B 1 89  ? 13.246  13.974 7.738  1.00 15.71 ? 106 ALA B C   1 
ATOM   1862 O O   . ALA B 1 89  ? 14.177  14.746 7.460  1.00 15.85 ? 106 ALA B O   1 
ATOM   1863 C CB  . ALA B 1 89  ? 12.040  12.967 5.808  1.00 19.41 ? 106 ALA B CB  1 
ATOM   1864 N N   . GLN B 1 90  ? 12.349  14.261 8.693  1.00 15.18 ? 107 GLN B N   1 
ATOM   1865 C CA  . GLN B 1 90  ? 12.463  15.516 9.430  1.00 14.64 ? 107 GLN B CA  1 
ATOM   1866 C C   . GLN B 1 90  ? 13.702  15.527 10.315 1.00 16.00 ? 107 GLN B C   1 
ATOM   1867 O O   . GLN B 1 90  ? 14.381  16.559 10.427 1.00 16.04 ? 107 GLN B O   1 
ATOM   1868 C CB  . GLN B 1 90  ? 11.192  15.769 10.240 1.00 15.49 ? 107 GLN B CB  1 
ATOM   1869 C CG  . GLN B 1 90  ? 9.991   16.157 9.416  1.00 16.77 ? 107 GLN B CG  1 
ATOM   1870 C CD  . GLN B 1 90  ? 10.195  17.458 8.684  1.00 15.41 ? 107 GLN B CD  1 
ATOM   1871 O OE1 . GLN B 1 90  ? 10.516  18.490 9.280  1.00 15.34 ? 107 GLN B OE1 1 
ATOM   1872 N NE2 . GLN B 1 90  ? 10.038  17.411 7.375  1.00 18.33 ? 107 GLN B NE2 1 
ATOM   1873 N N   . ALA B 1 91  ? 14.019  14.390 10.952 1.00 15.66 ? 108 ALA B N   1 
ATOM   1874 C CA  . ALA B 1 91  ? 15.233  14.335 11.760 1.00 16.97 ? 108 ALA B CA  1 
ATOM   1875 C C   . ALA B 1 91  ? 16.465  14.547 10.895 1.00 15.81 ? 108 ALA B C   1 
ATOM   1876 O O   . ALA B 1 91  ? 17.394  15.235 11.311 1.00 17.41 ? 108 ALA B O   1 
ATOM   1877 C CB  . ALA B 1 91  ? 15.338  13.021 12.538 1.00 16.25 ? 108 ALA B CB  1 
ATOM   1878 N N   . ARG B 1 92  ? 16.489  13.974 9.682  1.00 17.46 ? 109 ARG B N   1 
ATOM   1879 C CA  . ARG B 1 92  ? 17.609  14.217 8.774  1.00 18.17 ? 109 ARG B CA  1 
ATOM   1880 C C   . ARG B 1 92  ? 17.739  15.693 8.433  1.00 18.67 ? 109 ARG B C   1 
ATOM   1881 O O   . ARG B 1 92  ? 18.850  16.238 8.381  1.00 18.78 ? 109 ARG B O   1 
ATOM   1882 C CB  . ARG B 1 92  ? 17.428  13.419 7.481  1.00 20.15 ? 109 ARG B CB  1 
ATOM   1883 C CG  . ARG B 1 92  ? 17.402  11.916 7.653  1.00 24.53 ? 109 ARG B CG  1 
ATOM   1884 C CD  . ARG B 1 92  ? 18.767  11.324 7.808  1.00 32.27 ? 109 ARG B CD  1 
ATOM   1885 N NE  . ARG B 1 92  ? 19.518  11.332 6.556  1.00 33.88 ? 109 ARG B NE  1 
ATOM   1886 C CZ  . ARG B 1 92  ? 20.671  10.704 6.387  1.00 36.77 ? 109 ARG B CZ  1 
ATOM   1887 N NH1 . ARG B 1 92  ? 21.187  9.945  7.344  1.00 33.96 ? 109 ARG B NH1 1 
ATOM   1888 N NH2 . ARG B 1 92  ? 21.318  10.834 5.233  1.00 39.57 ? 109 ARG B NH2 1 
ATOM   1889 N N   . LYS B 1 93  ? 16.609  16.349 8.179  1.00 16.73 ? 110 LYS B N   1 
ATOM   1890 C CA  . LYS B 1 93  ? 16.633  17.780 7.884  1.00 15.50 ? 110 LYS B CA  1 
ATOM   1891 C C   . LYS B 1 93  ? 17.162  18.576 9.069  1.00 16.20 ? 110 LYS B C   1 
ATOM   1892 O O   . LYS B 1 93  ? 17.916  19.541 8.891  1.00 16.78 ? 110 LYS B O   1 
ATOM   1893 C CB  . LYS B 1 93  ? 15.228  18.222 7.489  1.00 16.58 ? 110 LYS B CB  1 
ATOM   1894 C CG  . LYS B 1 93  ? 15.091  19.665 7.161  1.00 17.54 ? 110 LYS B CG  1 
ATOM   1895 C CD  . LYS B 1 93  ? 13.680  19.960 6.731  1.00 17.30 ? 110 LYS B CD  1 
ATOM   1896 C CE  . LYS B 1 93  ? 13.496  21.416 6.479  1.00 18.12 ? 110 LYS B CE  1 
ATOM   1897 N NZ  . LYS B 1 93  ? 12.084  21.694 6.092  1.00 19.51 ? 110 LYS B NZ  1 
ATOM   1898 N N   . MET B 1 94  ? 16.777  18.181 10.284 1.00 15.51 ? 111 MET B N   1 
ATOM   1899 C CA  . MET B 1 94  ? 17.197  18.889 11.484 1.00 14.22 ? 111 MET B CA  1 
ATOM   1900 C C   . MET B 1 94  ? 18.678  18.708 11.747 1.00 14.59 ? 111 MET B C   1 
ATOM   1901 O O   . MET B 1 94  ? 19.329  19.633 12.246 1.00 15.71 ? 111 MET B O   1 
ATOM   1902 C CB  . MET B 1 94  ? 16.394  18.394 12.678 1.00 15.01 ? 111 MET B CB  1 
ATOM   1903 C CG  . MET B 1 94  ? 14.954  18.802 12.624 1.00 15.09 ? 111 MET B CG  1 
ATOM   1904 S SD  . MET B 1 94  ? 13.963  17.919 13.833 1.00 16.27 ? 111 MET B SD  1 
ATOM   1905 C CE  . MET B 1 94  ? 14.347  18.779 15.335 1.00 17.74 ? 111 MET B CE  1 
ATOM   1906 N N   . MET B 1 95  ? 19.217  17.519 11.428 1.00 15.54 ? 112 MET B N   1 
ATOM   1907 C CA  A MET B 1 95  ? 20.651  17.295 11.572 0.68 16.57 ? 112 MET B CA  1 
ATOM   1908 C CA  B MET B 1 95  ? 20.652  17.293 11.572 0.32 16.94 ? 112 MET B CA  1 
ATOM   1909 C C   . MET B 1 95  ? 21.441  18.110 10.562 1.00 16.25 ? 112 MET B C   1 
ATOM   1910 O O   . MET B 1 95  ? 22.525  18.613 10.872 1.00 16.70 ? 112 MET B O   1 
ATOM   1911 C CB  A MET B 1 95  ? 20.965  15.815 11.364 0.68 17.87 ? 112 MET B CB  1 
ATOM   1912 C CB  B MET B 1 95  ? 20.968  15.812 11.367 0.32 18.32 ? 112 MET B CB  1 
ATOM   1913 C CG  A MET B 1 95  ? 20.334  14.925 12.389 0.68 20.40 ? 112 MET B CG  1 
ATOM   1914 C CG  B MET B 1 95  ? 20.398  14.897 12.421 0.32 20.27 ? 112 MET B CG  1 
ATOM   1915 S SD  A MET B 1 95  ? 20.773  13.192 12.208 0.68 24.99 ? 112 MET B SD  1 
ATOM   1916 S SD  B MET B 1 95  ? 21.020  13.214 12.269 0.32 22.98 ? 112 MET B SD  1 
ATOM   1917 C CE  A MET B 1 95  ? 20.497  12.828 10.508 0.68 32.27 ? 112 MET B CE  1 
ATOM   1918 C CE  B MET B 1 95  ? 20.581  12.784 10.605 0.32 29.41 ? 112 MET B CE  1 
ATOM   1919 N N   . GLY B 1 96  ? 20.920  18.234 9.354  1.00 15.89 ? 113 GLY B N   1 
ATOM   1920 C CA  . GLY B 1 96  ? 21.639  18.893 8.289  1.00 15.50 ? 113 GLY B CA  1 
ATOM   1921 C C   . GLY B 1 96  ? 22.588  17.969 7.566  1.00 16.24 ? 113 GLY B C   1 
ATOM   1922 O O   . GLY B 1 96  ? 22.793  16.801 7.918  1.00 17.14 ? 113 GLY B O   1 
ATOM   1923 N N   . SER B 1 97  ? 23.197  18.534 6.518  1.00 16.91 ? 114 SER B N   1 
ATOM   1924 C CA  A SER B 1 97  ? 24.138  17.791 5.688  0.44 17.95 ? 114 SER B CA  1 
ATOM   1925 C CA  B SER B 1 97  ? 24.122  17.770 5.692  0.56 17.31 ? 114 SER B CA  1 
ATOM   1926 C C   . SER B 1 97  ? 25.191  17.089 6.536  1.00 18.17 ? 114 SER B C   1 
ATOM   1927 O O   . SER B 1 97  ? 25.647  17.613 7.561  1.00 17.18 ? 114 SER B O   1 
ATOM   1928 C CB  A SER B 1 97  ? 24.855  18.769 4.755  0.44 18.36 ? 114 SER B CB  1 
ATOM   1929 C CB  B SER B 1 97  ? 24.826  18.690 4.696  0.56 17.19 ? 114 SER B CB  1 
ATOM   1930 O OG  A SER B 1 97  ? 23.938  19.646 4.133  0.44 21.91 ? 114 SER B OG  1 
ATOM   1931 O OG  B SER B 1 97  ? 25.921  18.007 4.102  0.56 22.18 ? 114 SER B OG  1 
ATOM   1932 N N   . THR B 1 98  ? 25.609  15.907 6.071  1.00 19.01 ? 115 THR B N   1 
ATOM   1933 C CA  . THR B 1 98  ? 26.683  15.167 6.719  1.00 19.98 ? 115 THR B CA  1 
ATOM   1934 C C   . THR B 1 98  ? 27.937  16.011 6.884  1.00 18.57 ? 115 THR B C   1 
ATOM   1935 O O   . THR B 1 98  ? 28.663  15.864 7.869  1.00 18.56 ? 115 THR B O   1 
ATOM   1936 C CB  . THR B 1 98  ? 27.040  13.922 5.900  1.00 26.16 ? 115 THR B CB  1 
ATOM   1937 O OG1 . THR B 1 98  ? 25.869  13.162 5.610  1.00 39.46 ? 115 THR B OG1 1 
ATOM   1938 C CG2 . THR B 1 98  ? 28.003  13.066 6.677  1.00 26.45 ? 115 THR B CG2 1 
ATOM   1939 N N   . ARG B 1 99  ? 28.238  16.859 5.905  1.00 16.86 ? 116 ARG B N   1 
ATOM   1940 C CA  . ARG B 1 99  ? 29.368  17.770 5.986  1.00 17.43 ? 116 ARG B CA  1 
ATOM   1941 C C   . ARG B 1 99  ? 28.885  19.062 6.623  1.00 18.12 ? 116 ARG B C   1 
ATOM   1942 O O   . ARG B 1 99  ? 28.078  19.786 6.019  1.00 17.47 ? 116 ARG B O   1 
ATOM   1943 C CB  . ARG B 1 99  ? 29.910  18.028 4.586  1.00 22.09 ? 116 ARG B CB  1 
ATOM   1944 C CG  . ARG B 1 99  ? 30.584  16.792 4.028  1.00 29.13 ? 116 ARG B CG  1 
ATOM   1945 C CD  . ARG B 1 99  ? 30.820  16.805 2.516  1.00 37.30 ? 116 ARG B CD  1 
ATOM   1946 N NE  . ARG B 1 99  ? 29.587  16.649 1.749  1.00 45.13 ? 116 ARG B NE  1 
ATOM   1947 C CZ  . ARG B 1 99  ? 28.923  15.508 1.580  1.00 47.97 ? 116 ARG B CZ  1 
ATOM   1948 N NH1 . ARG B 1 99  ? 29.335  14.371 2.123  1.00 43.66 ? 116 ARG B NH1 1 
ATOM   1949 N NH2 . ARG B 1 99  ? 27.822  15.508 0.837  1.00 50.73 ? 116 ARG B NH2 1 
ATOM   1950 N N   . PRO B 1 100 ? 29.326  19.395 7.843  1.00 18.66 ? 117 PRO B N   1 
ATOM   1951 C CA  . PRO B 1 100 ? 28.755  20.561 8.528  1.00 16.59 ? 117 PRO B CA  1 
ATOM   1952 C C   . PRO B 1 100 ? 28.897  21.867 7.773  1.00 16.86 ? 117 PRO B C   1 
ATOM   1953 O O   . PRO B 1 100 ? 28.019  22.735 7.896  1.00 17.71 ? 117 PRO B O   1 
ATOM   1954 C CB  . PRO B 1 100 ? 29.506  20.579 9.868  1.00 16.89 ? 117 PRO B CB  1 
ATOM   1955 C CG  . PRO B 1 100 ? 29.895  19.160 10.094 1.00 17.58 ? 117 PRO B CG  1 
ATOM   1956 C CD  . PRO B 1 100 ? 30.214  18.609 8.710  1.00 17.49 ? 117 PRO B CD  1 
ATOM   1957 N N   . GLY B 1 101 ? 29.972  22.037 6.998  1.00 18.31 ? 118 GLY B N   1 
ATOM   1958 C CA  . GLY B 1 101 ? 30.154  23.254 6.221  1.00 18.84 ? 118 GLY B CA  1 
ATOM   1959 C C   . GLY B 1 101 ? 29.091  23.469 5.167  1.00 19.20 ? 118 GLY B C   1 
ATOM   1960 O O   . GLY B 1 101 ? 28.886  24.606 4.728  1.00 21.01 ? 118 GLY B O   1 
ATOM   1961 N N   . GLU B 1 102 ? 28.411  22.400 4.759  1.00 18.22 ? 119 GLU B N   1 
ATOM   1962 C CA  . GLU B 1 102 ? 27.341  22.454 3.774  1.00 17.30 ? 119 GLU B CA  1 
ATOM   1963 C C   . GLU B 1 102 ? 25.970  22.538 4.412  1.00 18.46 ? 119 GLU B C   1 
ATOM   1964 O O   . GLU B 1 102 ? 24.992  22.811 3.713  1.00 21.12 ? 119 GLU B O   1 
ATOM   1965 C CB  . GLU B 1 102 ? 27.368  21.212 2.864  1.00 21.39 ? 119 GLU B CB  1 
ATOM   1966 C CG  . GLU B 1 102 ? 28.643  21.036 2.064  1.00 30.88 ? 119 GLU B CG  1 
ATOM   1967 C CD  . GLU B 1 102 ? 28.639  19.739 1.243  1.00 44.55 ? 119 GLU B CD  1 
ATOM   1968 O OE1 . GLU B 1 102 ? 27.601  19.040 1.239  1.00 48.47 ? 119 GLU B OE1 1 
ATOM   1969 O OE2 . GLU B 1 102 ? 29.668  19.413 0.605  1.00 49.72 ? 119 GLU B OE2 1 
ATOM   1970 N N   . ALA B 1 103 ? 25.878  22.306 5.719  1.00 18.65 ? 120 ALA B N   1 
ATOM   1971 C CA  . ALA B 1 103 ? 24.609  22.232 6.411  1.00 18.54 ? 120 ALA B CA  1 
ATOM   1972 C C   . ALA B 1 103 ? 24.010  23.617 6.600  1.00 20.72 ? 120 ALA B C   1 
ATOM   1973 O O   . ALA B 1 103 ? 24.721  24.616 6.729  1.00 22.01 ? 120 ALA B O   1 
ATOM   1974 C CB  . ALA B 1 103 ? 24.796  21.552 7.772  1.00 17.14 ? 120 ALA B CB  1 
ATOM   1975 N N   . ALA B 1 104 ? 22.683  23.661 6.599  1.00 21.03 ? 121 ALA B N   1 
ATOM   1976 C CA  . ALA B 1 104 ? 21.982  24.928 6.656  1.00 23.28 ? 121 ALA B CA  1 
ATOM   1977 C C   . ALA B 1 104 ? 22.063  25.529 8.058  1.00 22.64 ? 121 ALA B C   1 
ATOM   1978 O O   . ALA B 1 104 ? 22.013  24.814 9.057  1.00 18.34 ? 121 ALA B O   1 
ATOM   1979 C CB  . ALA B 1 104 ? 20.514  24.710 6.290  1.00 27.04 ? 121 ALA B CB  1 
ATOM   1980 N N   . PRO B 1 105 ? 22.140  26.850 8.169  1.00 26.11 ? 122 PRO B N   1 
ATOM   1981 C CA  . PRO B 1 105 ? 22.088  27.454 9.502  1.00 25.06 ? 122 PRO B CA  1 
ATOM   1982 C C   . PRO B 1 105 ? 20.835  26.979 10.221 1.00 21.40 ? 122 PRO B C   1 
ATOM   1983 O O   . PRO B 1 105 ? 19.780  26.784 9.608  1.00 24.76 ? 122 PRO B O   1 
ATOM   1984 C CB  . PRO B 1 105 ? 22.024  28.952 9.206  1.00 29.97 ? 122 PRO B CB  1 
ATOM   1985 C CG  . PRO B 1 105 ? 22.674  29.089 7.868  1.00 35.45 ? 122 PRO B CG  1 
ATOM   1986 C CD  . PRO B 1 105 ? 22.271  27.861 7.103  1.00 34.13 ? 122 PRO B CD  1 
ATOM   1987 N N   . GLY B 1 106 ? 20.964  26.753 11.524 1.00 17.98 ? 123 GLY B N   1 
ATOM   1988 C CA  . GLY B 1 106 ? 19.864  26.243 12.314 1.00 17.74 ? 123 GLY B CA  1 
ATOM   1989 C C   . GLY B 1 106 ? 19.787  24.738 12.411 1.00 16.34 ? 123 GLY B C   1 
ATOM   1990 O O   . GLY B 1 106 ? 18.974  24.223 13.193 1.00 19.77 ? 123 GLY B O   1 
ATOM   1991 N N   . THR B 1 107 ? 20.584  24.011 11.640 1.00 16.02 ? 124 THR B N   1 
ATOM   1992 C CA  . THR B 1 107 ? 20.663  22.568 11.801 1.00 14.03 ? 124 THR B CA  1 
ATOM   1993 C C   . THR B 1 107 ? 21.707  22.211 12.859 1.00 15.99 ? 124 THR B C   1 
ATOM   1994 O O   . THR B 1 107 ? 22.587  23.006 13.190 1.00 17.50 ? 124 THR B O   1 
ATOM   1995 C CB  . THR B 1 107 ? 20.998  21.875 10.472 1.00 15.77 ? 124 THR B CB  1 
ATOM   1996 O OG1 . THR B 1 107 ? 22.309  22.266 10.035 1.00 16.02 ? 124 THR B OG1 1 
ATOM   1997 C CG2 . THR B 1 107 ? 19.956  22.181 9.410  1.00 16.85 ? 124 THR B CG2 1 
ATOM   1998 N N   . ILE B 1 108 ? 21.610  20.986 13.377 1.00 14.96 ? 125 ILE B N   1 
ATOM   1999 C CA  . ILE B 1 108 ? 22.541  20.555 14.420 1.00 16.61 ? 125 ILE B CA  1 
ATOM   2000 C C   . ILE B 1 108 ? 23.978  20.630 13.920 1.00 16.95 ? 125 ILE B C   1 
ATOM   2001 O O   . ILE B 1 108 ? 24.866  21.171 14.586 1.00 15.77 ? 125 ILE B O   1 
ATOM   2002 C CB  . ILE B 1 108 ? 22.189  19.143 14.911 1.00 15.93 ? 125 ILE B CB  1 
ATOM   2003 C CG1 . ILE B 1 108 ? 20.849  19.191 15.641 1.00 16.08 ? 125 ILE B CG1 1 
ATOM   2004 C CG2 . ILE B 1 108 ? 23.296  18.600 15.804 1.00 18.90 ? 125 ILE B CG2 1 
ATOM   2005 C CD1 . ILE B 1 108 ? 20.195  17.825 15.928 1.00 17.71 ? 125 ILE B CD1 1 
ATOM   2006 N N   . ARG B 1 109 ? 24.232  20.079 12.741 1.00 15.46 ? 126 ARG B N   1 
ATOM   2007 C CA  . ARG B 1 109 ? 25.618  20.020 12.289 1.00 15.13 ? 126 ARG B CA  1 
ATOM   2008 C C   . ARG B 1 109 ? 26.179  21.407 11.992 1.00 15.86 ? 126 ARG B C   1 
ATOM   2009 O O   . ARG B 1 109 ? 27.346  21.683 12.280 1.00 15.26 ? 126 ARG B O   1 
ATOM   2010 C CB  . ARG B 1 109 ? 25.724  19.059 11.111 1.00 17.19 ? 126 ARG B CB  1 
ATOM   2011 C CG  . ARG B 1 109 ? 25.659  17.621 11.647 1.00 24.17 ? 126 ARG B CG  1 
ATOM   2012 C CD  . ARG B 1 109 ? 25.245  16.693 10.616 1.00 24.20 ? 126 ARG B CD  1 
ATOM   2013 N NE  . ARG B 1 109 ? 25.220  15.308 11.058 1.00 17.84 ? 126 ARG B NE  1 
ATOM   2014 C CZ  . ARG B 1 109 ? 24.775  14.342 10.279 1.00 19.71 ? 126 ARG B CZ  1 
ATOM   2015 N NH1 . ARG B 1 109 ? 24.232  14.611 9.102  1.00 22.20 ? 126 ARG B NH1 1 
ATOM   2016 N NH2 . ARG B 1 109 ? 24.876  13.086 10.680 1.00 20.50 ? 126 ARG B NH2 1 
ATOM   2017 N N   . ALA B 1 110 ? 25.371  22.296 11.414 1.00 15.80 ? 127 ALA B N   1 
ATOM   2018 C CA  . ALA B 1 110 ? 25.855  23.650 11.166 1.00 16.07 ? 127 ALA B CA  1 
ATOM   2019 C C   . ALA B 1 110 ? 26.071  24.415 12.465 1.00 14.17 ? 127 ALA B C   1 
ATOM   2020 O O   . ALA B 1 110 ? 26.980  25.245 12.555 1.00 16.59 ? 127 ALA B O   1 
ATOM   2021 C CB  . ALA B 1 110 ? 24.845  24.425 10.329 1.00 16.78 ? 127 ALA B CB  1 
ATOM   2022 N N   . ASP B 1 111 ? 25.241  24.148 13.479 1.00 14.53 ? 128 ASP B N   1 
ATOM   2023 C CA  . ASP B 1 111 ? 25.307  24.915 14.715 1.00 15.72 ? 128 ASP B CA  1 
ATOM   2024 C C   . ASP B 1 111 ? 26.411  24.433 15.647 1.00 15.28 ? 128 ASP B C   1 
ATOM   2025 O O   . ASP B 1 111 ? 26.902  25.230 16.458 1.00 15.77 ? 128 ASP B O   1 
ATOM   2026 C CB  . ASP B 1 111 ? 23.962  24.853 15.437 1.00 16.97 ? 128 ASP B CB  1 
ATOM   2027 C CG  . ASP B 1 111 ? 22.870  25.699 14.766 1.00 20.74 ? 128 ASP B CG  1 
ATOM   2028 O OD1 . ASP B 1 111 ? 23.169  26.479 13.831 1.00 22.37 ? 128 ASP B OD1 1 
ATOM   2029 O OD2 . ASP B 1 111 ? 21.689  25.564 15.170 1.00 21.96 ? 128 ASP B OD2 1 
ATOM   2030 N N   . PHE B 1 112 ? 26.814  23.159 15.540 1.00 13.90 ? 129 PHE B N   1 
ATOM   2031 C CA  . PHE B 1 112 ? 27.740  22.548 16.483 1.00 14.36 ? 129 PHE B CA  1 
ATOM   2032 C C   . PHE B 1 112 ? 29.073  22.079 15.907 1.00 14.78 ? 129 PHE B C   1 
ATOM   2033 O O   . PHE B 1 112 ? 30.009  21.884 16.691 1.00 15.46 ? 129 PHE B O   1 
ATOM   2034 C CB  . PHE B 1 112 ? 27.111  21.303 17.144 1.00 16.36 ? 129 PHE B CB  1 
ATOM   2035 C CG  . PHE B 1 112 ? 26.021  21.584 18.154 1.00 15.70 ? 129 PHE B CG  1 
ATOM   2036 C CD1 . PHE B 1 112 ? 24.689  21.622 17.766 1.00 16.91 ? 129 PHE B CD1 1 
ATOM   2037 C CD2 . PHE B 1 112 ? 26.317  21.728 19.510 1.00 16.19 ? 129 PHE B CD2 1 
ATOM   2038 C CE1 . PHE B 1 112 ? 23.685  21.822 18.708 1.00 17.76 ? 129 PHE B CE1 1 
ATOM   2039 C CE2 . PHE B 1 112 ? 25.322  21.932 20.433 1.00 17.25 ? 129 PHE B CE2 1 
ATOM   2040 C CZ  . PHE B 1 112 ? 24.007  21.985 20.024 1.00 15.82 ? 129 PHE B CZ  1 
ATOM   2041 N N   . CYS B 1 113 ? 29.197  21.869 14.593 1.00 14.40 ? 130 CYS B N   1 
ATOM   2042 C CA  . CYS B 1 113 ? 30.288  21.043 14.074 1.00 15.08 ? 130 CYS B CA  1 
ATOM   2043 C C   . CYS B 1 113 ? 31.042  21.715 12.934 1.00 15.89 ? 130 CYS B C   1 
ATOM   2044 O O   . CYS B 1 113 ? 30.631  22.743 12.389 1.00 16.06 ? 130 CYS B O   1 
ATOM   2045 C CB  . CYS B 1 113 ? 29.776  19.669 13.604 1.00 14.99 ? 130 CYS B CB  1 
ATOM   2046 S SG  . CYS B 1 113 ? 28.995  18.750 14.964 1.00 16.88 ? 130 CYS B SG  1 
ATOM   2047 N N   . GLN B 1 114 ? 32.181  21.106 12.594 1.00 15.03 ? 131 GLN B N   1 
ATOM   2048 C CA  . GLN B 1 114 ? 33.077  21.598 11.546 1.00 15.21 ? 131 GLN B CA  1 
ATOM   2049 C C   . GLN B 1 114 ? 33.293  20.603 10.420 1.00 17.46 ? 131 GLN B C   1 
ATOM   2050 O O   . GLN B 1 114 ? 33.298  20.999 9.250  1.00 17.79 ? 131 GLN B O   1 
ATOM   2051 C CB  . GLN B 1 114 ? 34.440  21.984 12.140 1.00 17.25 ? 131 GLN B CB  1 
ATOM   2052 C CG  . GLN B 1 114 ? 34.346  23.148 13.117 1.00 16.60 ? 131 GLN B CG  1 
ATOM   2053 C CD  . GLN B 1 114 ? 35.692  23.649 13.584 1.00 15.15 ? 131 GLN B CD  1 
ATOM   2054 O OE1 . GLN B 1 114 ? 36.628  23.772 12.798 1.00 17.26 ? 131 GLN B OE1 1 
ATOM   2055 N NE2 . GLN B 1 114 ? 35.798  23.937 14.882 1.00 16.55 ? 131 GLN B NE2 1 
ATOM   2056 N N   . GLN B 1 115 ? 33.459  19.318 10.739 1.00 16.91 ? 132 GLN B N   1 
ATOM   2057 C CA  . GLN B 1 115 ? 33.861  18.319 9.766  1.00 17.66 ? 132 GLN B CA  1 
ATOM   2058 C C   . GLN B 1 115 ? 32.996  17.076 9.863  1.00 16.45 ? 132 GLN B C   1 
ATOM   2059 O O   . GLN B 1 115 ? 32.520  16.704 10.939 1.00 17.04 ? 132 GLN B O   1 
ATOM   2060 C CB  . GLN B 1 115 ? 35.319  17.920 9.959  1.00 20.27 ? 132 GLN B CB  1 
ATOM   2061 C CG  . GLN B 1 115 ? 36.251  19.094 9.803  1.00 21.33 ? 132 GLN B CG  1 
ATOM   2062 C CD  . GLN B 1 115 ? 37.689  18.683 9.751  1.00 20.76 ? 132 GLN B CD  1 
ATOM   2063 O OE1 . GLN B 1 115 ? 38.285  18.342 10.771 1.00 22.32 ? 132 GLN B OE1 1 
ATOM   2064 N NE2 . GLN B 1 115 ? 38.265  18.712 8.554  1.00 23.99 ? 132 GLN B NE2 1 
ATOM   2065 N N   . ALA B 1 116 ? 32.837  16.400 8.719  1.00 19.28 ? 133 ALA B N   1 
ATOM   2066 C CA  . ALA B 1 116 ? 31.968  15.232 8.651  1.00 20.03 ? 133 ALA B CA  1 
ATOM   2067 C C   . ALA B 1 116 ? 32.403  14.121 9.601  1.00 18.69 ? 133 ALA B C   1 
ATOM   2068 O O   . ALA B 1 116 ? 31.552  13.395 10.137 1.00 20.28 ? 133 ALA B O   1 
ATOM   2069 C CB  . ALA B 1 116 ? 31.946  14.695 7.217  1.00 20.64 ? 133 ALA B CB  1 
ATOM   2070 N N   . GLY B 1 117 ? 33.709  13.960 9.820  1.00 20.05 ? 134 GLY B N   1 
ATOM   2071 C CA  . GLY B 1 117 ? 34.168  12.893 10.697 1.00 19.92 ? 134 GLY B CA  1 
ATOM   2072 C C   . GLY B 1 117 ? 33.815  13.091 12.156 1.00 19.29 ? 134 GLY B C   1 
ATOM   2073 O O   . GLY B 1 117 ? 33.937  12.148 12.943 1.00 19.04 ? 134 GLY B O   1 
ATOM   2074 N N   . ARG B 1 118 ? 33.439  14.308 12.545 1.00 17.27 ? 135 ARG B N   1 
ATOM   2075 C CA  . ARG B 1 118 ? 32.936  14.591 13.893 1.00 18.19 ? 135 ARG B CA  1 
ATOM   2076 C C   . ARG B 1 118 ? 31.672  15.444 13.742 1.00 16.21 ? 135 ARG B C   1 
ATOM   2077 O O   . ARG B 1 118 ? 31.669  16.666 13.972 1.00 16.33 ? 135 ARG B O   1 
ATOM   2078 C CB  . ARG B 1 118 ? 34.013  15.308 14.684 1.00 17.04 ? 135 ARG B CB  1 
ATOM   2079 C CG  . ARG B 1 118 ? 35.190  14.444 15.091 1.00 18.16 ? 135 ARG B CG  1 
ATOM   2080 C CD  . ARG B 1 118 ? 34.751  13.314 16.018 1.00 18.67 ? 135 ARG B CD  1 
ATOM   2081 N NE  . ARG B 1 118 ? 35.874  12.679 16.701 1.00 19.39 ? 135 ARG B NE  1 
ATOM   2082 C CZ  . ARG B 1 118 ? 35.782  11.556 17.394 1.00 19.74 ? 135 ARG B CZ  1 
ATOM   2083 N NH1 . ARG B 1 118 ? 34.633  10.916 17.511 1.00 19.12 ? 135 ARG B NH1 1 
ATOM   2084 N NH2 . ARG B 1 118 ? 36.871  11.063 17.979 1.00 20.81 ? 135 ARG B NH2 1 
ATOM   2085 N N   . ASN B 1 119 ? 30.562  14.788 13.413 1.00 16.33 ? 136 ASN B N   1 
ATOM   2086 C CA  . ASN B 1 119 ? 29.320  15.486 13.083 1.00 13.49 ? 136 ASN B CA  1 
ATOM   2087 C C   . ASN B 1 119 ? 28.177  15.131 14.033 1.00 14.86 ? 136 ASN B C   1 
ATOM   2088 O O   . ASN B 1 119 ? 27.001  15.216 13.666 1.00 16.69 ? 136 ASN B O   1 
ATOM   2089 C CB  . ASN B 1 119 ? 28.941  15.302 11.606 1.00 16.12 ? 136 ASN B CB  1 
ATOM   2090 C CG  . ASN B 1 119 ? 28.589  13.876 11.252 1.00 18.44 ? 136 ASN B CG  1 
ATOM   2091 O OD1 . ASN B 1 119 ? 28.601  12.976 12.103 1.00 19.96 ? 136 ASN B OD1 1 
ATOM   2092 N ND2 . ASN B 1 119 ? 28.240  13.669 9.990  1.00 19.91 ? 136 ASN B ND2 1 
ATOM   2093 N N   . LEU B 1 120 ? 28.534  14.716 15.252 1.00 15.66 ? 137 LEU B N   1 
ATOM   2094 C CA  . LEU B 1 120 ? 27.733  14.726 16.472 1.00 15.25 ? 137 LEU B CA  1 
ATOM   2095 C C   . LEU B 1 120 ? 26.614  13.710 16.596 1.00 17.48 ? 137 LEU B C   1 
ATOM   2096 O O   . LEU B 1 120 ? 26.347  13.222 17.702 1.00 15.69 ? 137 LEU B O   1 
ATOM   2097 C CB  . LEU B 1 120 ? 27.044  16.101 16.620 1.00 16.06 ? 137 LEU B CB  1 
ATOM   2098 C CG  . LEU B 1 120 ? 26.953  16.633 18.051 1.00 14.64 ? 137 LEU B CG  1 
ATOM   2099 C CD1 . LEU B 1 120 ? 28.348  17.042 18.519 1.00 16.61 ? 137 LEU B CD1 1 
ATOM   2100 C CD2 . LEU B 1 120 ? 25.991  17.802 18.154 1.00 15.30 ? 137 LEU B CD2 1 
ATOM   2101 N N   . ILE B 1 121 ? 26.043  13.269 15.480 1.00 15.36 ? 138 ILE B N   1 
ATOM   2102 C CA  . ILE B 1 121 ? 24.770  12.568 15.547 1.00 15.03 ? 138 ILE B CA  1 
ATOM   2103 C C   . ILE B 1 121 ? 24.578  11.801 14.258 1.00 16.31 ? 138 ILE B C   1 
ATOM   2104 O O   . ILE B 1 121 ? 25.086  12.191 13.215 1.00 17.05 ? 138 ILE B O   1 
ATOM   2105 C CB  . ILE B 1 121 ? 23.602  13.554 15.816 1.00 15.68 ? 138 ILE B CB  1 
ATOM   2106 C CG1 . ILE B 1 121 ? 22.305  12.783 16.098 1.00 16.50 ? 138 ILE B CG1 1 
ATOM   2107 C CG2 . ILE B 1 121 ? 23.454  14.567 14.659 1.00 17.63 ? 138 ILE B CG2 1 
ATOM   2108 C CD1 . ILE B 1 121 ? 21.176  13.653 16.602 1.00 16.78 ? 138 ILE B CD1 1 
ATOM   2109 N N   . HIS B 1 122 ? 23.858  10.699 14.352 1.00 17.40 ? 139 HIS B N   1 
ATOM   2110 C CA  . HIS B 1 122 ? 23.407  9.910  13.219 1.00 16.35 ? 139 HIS B CA  1 
ATOM   2111 C C   . HIS B 1 122 ? 21.886  9.787  13.256 1.00 15.37 ? 139 HIS B C   1 
ATOM   2112 O O   . HIS B 1 122 ? 21.292  9.669  14.338 1.00 16.47 ? 139 HIS B O   1 
ATOM   2113 C CB  . HIS B 1 122 ? 23.972  8.486  13.311 1.00 18.45 ? 139 HIS B CB  1 
ATOM   2114 C CG  . HIS B 1 122 ? 23.219  7.503  12.479 1.00 19.47 ? 139 HIS B CG  1 
ATOM   2115 N ND1 . HIS B 1 122 ? 23.508  7.277  11.151 1.00 23.18 ? 139 HIS B ND1 1 
ATOM   2116 C CD2 . HIS B 1 122 ? 22.156  6.718  12.769 1.00 18.72 ? 139 HIS B CD2 1 
ATOM   2117 C CE1 . HIS B 1 122 ? 22.666  6.384  10.664 1.00 22.12 ? 139 HIS B CE1 1 
ATOM   2118 N NE2 . HIS B 1 122 ? 21.822  6.041  11.621 1.00 20.25 ? 139 HIS B NE2 1 
ATOM   2119 N N   . GLY B 1 123 ? 21.258  9.774  12.083 1.00 17.55 ? 140 GLY B N   1 
ATOM   2120 C CA  . GLY B 1 123 ? 19.846  9.451  11.984 1.00 16.76 ? 140 GLY B CA  1 
ATOM   2121 C C   . GLY B 1 123 ? 19.601  8.549  10.792 1.00 16.49 ? 140 GLY B C   1 
ATOM   2122 O O   . GLY B 1 123 ? 20.254  8.675  9.756  1.00 18.79 ? 140 GLY B O   1 
ATOM   2123 N N   . SER B 1 124 ? 18.624  7.653  10.944 1.00 16.86 ? 141 SER B N   1 
ATOM   2124 C CA  . SER B 1 124 ? 18.269  6.730  9.870  1.00 16.30 ? 141 SER B CA  1 
ATOM   2125 C C   . SER B 1 124 ? 17.917  7.499  8.602  1.00 18.75 ? 141 SER B C   1 
ATOM   2126 O O   . SER B 1 124 ? 17.259  8.539  8.649  1.00 18.24 ? 141 SER B O   1 
ATOM   2127 C CB  . SER B 1 124 ? 17.042  5.904  10.274 1.00 17.93 ? 141 SER B CB  1 
ATOM   2128 O OG  . SER B 1 124 ? 17.251  5.185  11.481 1.00 18.86 ? 141 SER B OG  1 
ATOM   2129 N N   . ASP B 1 125 ? 18.340  6.971  7.459  1.00 20.72 ? 142 ASP B N   1 
ATOM   2130 C CA  . ASP B 1 125 ? 18.088  7.656  6.195  1.00 22.91 ? 142 ASP B CA  1 
ATOM   2131 C C   . ASP B 1 125 ? 16.821  7.196  5.482  1.00 21.58 ? 142 ASP B C   1 
ATOM   2132 O O   . ASP B 1 125 ? 16.470  7.783  4.459  1.00 24.52 ? 142 ASP B O   1 
ATOM   2133 C CB  . ASP B 1 125 ? 19.303  7.551  5.253  1.00 23.23 ? 142 ASP B CB  1 
ATOM   2134 C CG  . ASP B 1 125 ? 19.552  6.143  4.729  1.00 28.96 ? 142 ASP B CG  1 
ATOM   2135 O OD1 . ASP B 1 125 ? 18.811  5.198  5.067  1.00 28.65 ? 142 ASP B OD1 1 
ATOM   2136 O OD2 . ASP B 1 125 ? 20.508  5.987  3.942  1.00 34.42 ? 142 ASP B OD2 1 
ATOM   2137 N N   . SER B 1 126 ? 16.112  6.197  5.999  1.00 22.21 ? 143 SER B N   1 
ATOM   2138 C CA  . SER B 1 126 ? 14.944  5.649  5.317  1.00 23.14 ? 143 SER B CA  1 
ATOM   2139 C C   . SER B 1 126 ? 14.189  4.771  6.300  1.00 23.88 ? 143 SER B C   1 
ATOM   2140 O O   . SER B 1 126 ? 14.689  4.447  7.376  1.00 21.58 ? 143 SER B O   1 
ATOM   2141 C CB  . SER B 1 126 ? 15.352  4.815  4.099  1.00 24.07 ? 143 SER B CB  1 
ATOM   2142 O OG  . SER B 1 126 ? 15.977  3.608  4.517  1.00 27.14 ? 143 SER B OG  1 
ATOM   2143 N N   . ALA B 1 127 ? 12.972  4.383  5.912  1.00 25.31 ? 144 ALA B N   1 
ATOM   2144 C CA  . ALA B 1 127 ? 12.193  3.466  6.741  1.00 26.00 ? 144 ALA B CA  1 
ATOM   2145 C C   . ALA B 1 127 ? 12.885  2.112  6.882  1.00 25.14 ? 144 ALA B C   1 
ATOM   2146 O O   . ALA B 1 127 ? 12.879  1.516  7.968  1.00 25.83 ? 144 ALA B O   1 
ATOM   2147 C CB  . ALA B 1 127 ? 10.789  3.302  6.164  1.00 24.11 ? 144 ALA B CB  1 
ATOM   2148 N N   . GLU B 1 128 ? 13.472  1.604  5.790  1.00 25.64 ? 145 GLU B N   1 
ATOM   2149 C CA  . GLU B 1 128 ? 14.180  0.327  5.857  1.00 26.79 ? 145 GLU B CA  1 
ATOM   2150 C C   . GLU B 1 128 ? 15.373  0.415  6.800  1.00 23.12 ? 145 GLU B C   1 
ATOM   2151 O O   . GLU B 1 128 ? 15.619  -0.503 7.586  1.00 25.46 ? 145 GLU B O   1 
ATOM   2152 C CB  . GLU B 1 128 ? 14.631  -0.111 4.457  1.00 34.05 ? 145 GLU B CB  1 
ATOM   2153 C CG  . GLU B 1 128 ? 15.454  -1.400 4.443  1.00 44.97 ? 145 GLU B CG  1 
ATOM   2154 C CD  . GLU B 1 128 ? 15.969  -1.789 3.056  1.00 55.63 ? 145 GLU B CD  1 
ATOM   2155 O OE1 . GLU B 1 128 ? 15.870  -0.976 2.109  1.00 57.76 ? 145 GLU B OE1 1 
ATOM   2156 O OE2 . GLU B 1 128 ? 16.480  -2.921 2.914  1.00 59.68 ? 145 GLU B OE2 1 
ATOM   2157 N N   . SER B 1 129 ? 16.139  1.502  6.725  1.00 21.83 ? 146 SER B N   1 
ATOM   2158 C CA  A SER B 1 129 ? 17.293  1.610  7.610  0.50 23.52 ? 146 SER B CA  1 
ATOM   2159 C CA  B SER B 1 129 ? 17.295  1.666  7.603  0.50 23.86 ? 146 SER B CA  1 
ATOM   2160 C C   . SER B 1 129 ? 16.874  1.872  9.053  1.00 21.94 ? 146 SER B C   1 
ATOM   2161 O O   . SER B 1 129 ? 17.554  1.416  9.970  1.00 21.29 ? 146 SER B O   1 
ATOM   2162 C CB  A SER B 1 129 ? 18.287  2.656  7.108  0.50 22.59 ? 146 SER B CB  1 
ATOM   2163 C CB  B SER B 1 129 ? 18.150  2.843  7.135  0.50 24.11 ? 146 SER B CB  1 
ATOM   2164 O OG  A SER B 1 129 ? 17.733  3.948  7.118  0.50 22.58 ? 146 SER B OG  1 
ATOM   2165 O OG  B SER B 1 129 ? 18.894  2.508  5.981  0.50 26.83 ? 146 SER B OG  1 
ATOM   2166 N N   . ALA B 1 130 ? 15.769  2.584  9.277  1.00 21.74 ? 147 ALA B N   1 
ATOM   2167 C CA  . ALA B 1 130 ? 15.278  2.756  10.641 1.00 21.70 ? 147 ALA B CA  1 
ATOM   2168 C C   . ALA B 1 130 ? 14.919  1.417  11.272 1.00 22.19 ? 147 ALA B C   1 
ATOM   2169 O O   . ALA B 1 130 ? 15.288  1.147  12.415 1.00 23.20 ? 147 ALA B O   1 
ATOM   2170 C CB  . ALA B 1 130 ? 14.065  3.685  10.652 1.00 23.34 ? 147 ALA B CB  1 
ATOM   2171 N N   . LYS B 1 131 ? 14.212  0.551  10.537 1.00 21.89 ? 148 LYS B N   1 
ATOM   2172 C CA  . LYS B 1 131 ? 13.883  -0.764 11.083 1.00 25.86 ? 148 LYS B CA  1 
ATOM   2173 C C   . LYS B 1 131 ? 15.151  -1.549 11.400 1.00 23.72 ? 148 LYS B C   1 
ATOM   2174 O O   . LYS B 1 131 ? 15.284  -2.135 12.481 1.00 26.66 ? 148 LYS B O   1 
ATOM   2175 C CB  . LYS B 1 131 ? 13.001  -1.552 10.110 1.00 36.15 ? 148 LYS B CB  1 
ATOM   2176 C CG  . LYS B 1 131 ? 11.537  -1.161 10.160 1.00 47.43 ? 148 LYS B CG  1 
ATOM   2177 C CD  . LYS B 1 131 ? 10.744  -1.805 9.037  1.00 56.16 ? 148 LYS B CD  1 
ATOM   2178 C CE  . LYS B 1 131 ? 9.340   -1.215 8.953  1.00 63.37 ? 148 LYS B CE  1 
ATOM   2179 N NZ  . LYS B 1 131 ? 8.537   -1.811 7.844  1.00 67.23 ? 148 LYS B NZ  1 
ATOM   2180 N N   . ARG B 1 132 ? 16.110  -1.535 10.473 1.00 23.06 ? 149 ARG B N   1 
ATOM   2181 C CA  A ARG B 1 132 ? 17.337  -2.299 10.663 0.49 22.76 ? 149 ARG B CA  1 
ATOM   2182 C CA  B ARG B 1 132 ? 17.344  -2.292 10.654 0.51 22.53 ? 149 ARG B CA  1 
ATOM   2183 C C   . ARG B 1 132 ? 18.158  -1.756 11.828 1.00 21.71 ? 149 ARG B C   1 
ATOM   2184 O O   . ARG B 1 132 ? 18.680  -2.533 12.644 1.00 23.78 ? 149 ARG B O   1 
ATOM   2185 C CB  A ARG B 1 132 ? 18.159  -2.274 9.374  0.49 26.55 ? 149 ARG B CB  1 
ATOM   2186 C CB  B ARG B 1 132 ? 18.152  -2.217 9.356  0.51 25.68 ? 149 ARG B CB  1 
ATOM   2187 C CG  A ARG B 1 132 ? 19.373  -3.181 9.391  0.49 29.18 ? 149 ARG B CG  1 
ATOM   2188 C CG  B ARG B 1 132 ? 19.467  -2.963 9.363  0.51 27.47 ? 149 ARG B CG  1 
ATOM   2189 C CD  A ARG B 1 132 ? 20.232  -2.983 8.152  0.49 31.22 ? 149 ARG B CD  1 
ATOM   2190 C CD  B ARG B 1 132 ? 20.230  -2.738 8.054  0.51 30.13 ? 149 ARG B CD  1 
ATOM   2191 N NE  A ARG B 1 132 ? 21.023  -1.759 8.229  0.49 34.62 ? 149 ARG B NE  1 
ATOM   2192 N NE  B ARG B 1 132 ? 20.842  -1.411 7.997  0.51 32.07 ? 149 ARG B NE  1 
ATOM   2193 C CZ  A ARG B 1 132 ? 22.180  -1.652 8.873  0.49 33.01 ? 149 ARG B CZ  1 
ATOM   2194 C CZ  B ARG B 1 132 ? 20.509  -0.440 7.155  0.51 32.50 ? 149 ARG B CZ  1 
ATOM   2195 N NH1 A ARG B 1 132 ? 22.735  -2.688 9.483  0.49 31.78 ? 149 ARG B NH1 1 
ATOM   2196 N NH1 B ARG B 1 132 ? 19.577  -0.607 6.228  0.51 34.72 ? 149 ARG B NH1 1 
ATOM   2197 N NH2 A ARG B 1 132 ? 22.797  -0.476 8.904  0.49 33.34 ? 149 ARG B NH2 1 
ATOM   2198 N NH2 B ARG B 1 132 ? 21.130  0.734  7.250  0.51 30.54 ? 149 ARG B NH2 1 
ATOM   2199 N N   . GLU B 1 133 ? 18.279  -0.429 11.930 1.00 20.47 ? 150 GLU B N   1 
ATOM   2200 C CA  . GLU B 1 133 ? 19.099  0.165  12.980 1.00 19.46 ? 150 GLU B CA  1 
ATOM   2201 C C   . GLU B 1 133 ? 18.450  0.007  14.347 1.00 21.11 ? 150 GLU B C   1 
ATOM   2202 O O   . GLU B 1 133 ? 19.138  -0.294 15.327 1.00 22.54 ? 150 GLU B O   1 
ATOM   2203 C CB  . GLU B 1 133 ? 19.390  1.636  12.654 1.00 20.15 ? 150 GLU B CB  1 
ATOM   2204 C CG  . GLU B 1 133 ? 20.295  1.795  11.434 1.00 21.15 ? 150 GLU B CG  1 
ATOM   2205 C CD  . GLU B 1 133 ? 20.437  3.206  10.929 1.00 21.59 ? 150 GLU B CD  1 
ATOM   2206 O OE1 . GLU B 1 133 ? 19.808  4.127  11.509 1.00 22.21 ? 150 GLU B OE1 1 
ATOM   2207 O OE2 . GLU B 1 133 ? 21.166  3.375  9.921  1.00 22.58 ? 150 GLU B OE2 1 
ATOM   2208 N N   . ILE B 1 134 ? 17.127  0.183  14.430 1.00 22.91 ? 151 ILE B N   1 
ATOM   2209 C CA  . ILE B 1 134 ? 16.442  -0.003 15.709 1.00 22.69 ? 151 ILE B CA  1 
ATOM   2210 C C   . ILE B 1 134 ? 16.610  -1.439 16.199 1.00 23.53 ? 151 ILE B C   1 
ATOM   2211 O O   . ILE B 1 134 ? 16.850  -1.677 17.388 1.00 24.76 ? 151 ILE B O   1 
ATOM   2212 C CB  . ILE B 1 134 ? 14.962  0.418  15.594 1.00 23.11 ? 151 ILE B CB  1 
ATOM   2213 C CG1 . ILE B 1 134 ? 14.866  1.929  15.349 1.00 22.52 ? 151 ILE B CG1 1 
ATOM   2214 C CG2 . ILE B 1 134 ? 14.181  0.020  16.853 1.00 25.32 ? 151 ILE B CG2 1 
ATOM   2215 C CD1 . ILE B 1 134 ? 13.457  2.413  15.128 1.00 24.40 ? 151 ILE B CD1 1 
ATOM   2216 N N   . SER B 1 135 ? 16.510  -2.415 15.287 1.00 24.82 ? 152 SER B N   1 
ATOM   2217 C CA  . SER B 1 135 ? 16.716  -3.819 15.652 1.00 25.97 ? 152 SER B CA  1 
ATOM   2218 C C   . SER B 1 135 ? 18.157  -4.100 16.063 1.00 26.18 ? 152 SER B C   1 
ATOM   2219 O O   . SER B 1 135 ? 18.402  -4.951 16.925 1.00 28.60 ? 152 SER B O   1 
ATOM   2220 C CB  . SER B 1 135 ? 16.352  -4.733 14.477 1.00 28.61 ? 152 SER B CB  1 
ATOM   2221 O OG  . SER B 1 135 ? 14.987  -4.601 14.113 1.00 34.74 ? 152 SER B OG  1 
ATOM   2222 N N   . LEU B 1 136 ? 19.125  -3.431 15.439 1.00 25.60 ? 153 LEU B N   1 
ATOM   2223 C CA  . LEU B 1 136 ? 20.521  -3.669 15.777 1.00 24.55 ? 153 LEU B CA  1 
ATOM   2224 C C   . LEU B 1 136 ? 20.853  -3.156 17.172 1.00 24.21 ? 153 LEU B C   1 
ATOM   2225 O O   . LEU B 1 136 ? 21.505  -3.848 17.963 1.00 28.05 ? 153 LEU B O   1 
ATOM   2226 C CB  . LEU B 1 136 ? 21.413  -2.981 14.748 1.00 28.35 ? 153 LEU B CB  1 
ATOM   2227 C CG  . LEU B 1 136 ? 22.909  -3.050 15.051 1.00 31.28 ? 153 LEU B CG  1 
ATOM   2228 C CD1 . LEU B 1 136 ? 23.358  -4.513 15.200 1.00 34.57 ? 153 LEU B CD1 1 
ATOM   2229 C CD2 . LEU B 1 136 ? 23.694  -2.340 13.962 1.00 32.78 ? 153 LEU B CD2 1 
ATOM   2230 N N   . TRP B 1 137 ? 20.426  -1.934 17.484 1.00 24.37 ? 154 TRP B N   1 
ATOM   2231 C CA  . TRP B 1 137 ? 20.899  -1.238 18.672 1.00 21.62 ? 154 TRP B CA  1 
ATOM   2232 C C   . TRP B 1 137 ? 19.997  -1.407 19.887 1.00 24.07 ? 154 TRP B C   1 
ATOM   2233 O O   . TRP B 1 137 ? 20.444  -1.133 21.005 1.00 27.42 ? 154 TRP B O   1 
ATOM   2234 C CB  . TRP B 1 137 ? 21.035  0.254  18.377 1.00 23.48 ? 154 TRP B CB  1 
ATOM   2235 C CG  . TRP B 1 137 ? 22.163  0.606  17.437 1.00 23.05 ? 154 TRP B CG  1 
ATOM   2236 C CD1 . TRP B 1 137 ? 22.076  0.815  16.085 1.00 22.41 ? 154 TRP B CD1 1 
ATOM   2237 C CD2 . TRP B 1 137 ? 23.538  0.826  17.787 1.00 22.98 ? 154 TRP B CD2 1 
ATOM   2238 N NE1 . TRP B 1 137 ? 23.312  1.140  15.580 1.00 21.42 ? 154 TRP B NE1 1 
ATOM   2239 C CE2 . TRP B 1 137 ? 24.223  1.160  16.603 1.00 22.87 ? 154 TRP B CE2 1 
ATOM   2240 C CE3 . TRP B 1 137 ? 24.253  0.787  18.990 1.00 24.20 ? 154 TRP B CE3 1 
ATOM   2241 C CZ2 . TRP B 1 137 ? 25.591  1.442  16.580 1.00 22.54 ? 154 TRP B CZ2 1 
ATOM   2242 C CZ3 . TRP B 1 137 ? 25.616  1.062  18.964 1.00 23.85 ? 154 TRP B CZ3 1 
ATOM   2243 C CH2 . TRP B 1 137 ? 26.266  1.390  17.765 1.00 23.19 ? 154 TRP B CH2 1 
ATOM   2244 N N   . PHE B 1 138 ? 18.746  -1.823 19.697 1.00 26.13 ? 155 PHE B N   1 
ATOM   2245 C CA  . PHE B 1 138 ? 17.790  -1.985 20.783 1.00 25.38 ? 155 PHE B CA  1 
ATOM   2246 C C   . PHE B 1 138 ? 17.202  -3.389 20.761 1.00 29.06 ? 155 PHE B C   1 
ATOM   2247 O O   . PHE B 1 138 ? 17.044  -3.994 19.698 1.00 32.77 ? 155 PHE B O   1 
ATOM   2248 C CB  . PHE B 1 138 ? 16.620  -0.983 20.672 1.00 24.82 ? 155 PHE B CB  1 
ATOM   2249 C CG  . PHE B 1 138 ? 16.961  0.415  21.098 1.00 20.31 ? 155 PHE B CG  1 
ATOM   2250 C CD1 . PHE B 1 138 ? 17.073  0.738  22.445 1.00 22.79 ? 155 PHE B CD1 1 
ATOM   2251 C CD2 . PHE B 1 138 ? 17.123  1.415  20.161 1.00 18.33 ? 155 PHE B CD2 1 
ATOM   2252 C CE1 . PHE B 1 138 ? 17.355  2.031  22.840 1.00 22.68 ? 155 PHE B CE1 1 
ATOM   2253 C CE2 . PHE B 1 138 ? 17.426  2.700  20.547 1.00 19.80 ? 155 PHE B CE2 1 
ATOM   2254 C CZ  . PHE B 1 138 ? 17.539  3.013  21.888 1.00 21.93 ? 155 PHE B CZ  1 
ATOM   2255 N N   . LYS B 1 139 ? 16.892  -3.909 21.954 1.00 34.02 ? 156 LYS B N   1 
ATOM   2256 C CA  . LYS B 1 139 ? 15.967  -5.025 22.062 1.00 38.15 ? 156 LYS B CA  1 
ATOM   2257 C C   . LYS B 1 139 ? 14.543  -4.480 21.981 1.00 37.08 ? 156 LYS B C   1 
ATOM   2258 O O   . LYS B 1 139 ? 14.283  -3.366 22.436 1.00 35.74 ? 156 LYS B O   1 
ATOM   2259 C CB  . LYS B 1 139 ? 16.106  -5.715 23.413 1.00 43.55 ? 156 LYS B CB  1 
ATOM   2260 C CG  . LYS B 1 139 ? 17.513  -5.911 23.926 1.00 49.61 ? 156 LYS B CG  1 
ATOM   2261 C CD  . LYS B 1 139 ? 17.474  -6.517 25.328 1.00 55.77 ? 156 LYS B CD  1 
ATOM   2262 C CE  . LYS B 1 139 ? 18.814  -6.385 26.038 1.00 58.36 ? 156 LYS B CE  1 
ATOM   2263 N NZ  . LYS B 1 139 ? 19.910  -7.037 25.273 1.00 58.67 ? 156 LYS B NZ  1 
ATOM   2264 N N   . PRO B 1 140 ? 13.593  -5.249 21.447 1.00 39.17 ? 157 PRO B N   1 
ATOM   2265 C CA  . PRO B 1 140 ? 12.206  -4.749 21.420 1.00 39.81 ? 157 PRO B CA  1 
ATOM   2266 C C   . PRO B 1 140 ? 11.682  -4.356 22.789 1.00 41.89 ? 157 PRO B C   1 
ATOM   2267 O O   . PRO B 1 140 ? 10.851  -3.444 22.887 1.00 44.39 ? 157 PRO B O   1 
ATOM   2268 C CB  . PRO B 1 140 ? 11.404  -5.909 20.808 1.00 40.67 ? 157 PRO B CB  1 
ATOM   2269 C CG  . PRO B 1 140 ? 12.334  -7.084 20.762 1.00 41.02 ? 157 PRO B CG  1 
ATOM   2270 C CD  . PRO B 1 140 ? 13.732  -6.561 20.787 1.00 40.50 ? 157 PRO B CD  1 
ATOM   2271 N N   . GLU B 1 141 ? 12.156  -5.009 23.853 1.00 43.24 ? 158 GLU B N   1 
ATOM   2272 C CA  . GLU B 1 141 ? 11.738  -4.649 25.204 1.00 45.94 ? 158 GLU B CA  1 
ATOM   2273 C C   . GLU B 1 141 ? 12.020  -3.188 25.510 1.00 43.27 ? 158 GLU B C   1 
ATOM   2274 O O   . GLU B 1 141 ? 11.331  -2.577 26.334 1.00 43.92 ? 158 GLU B O   1 
ATOM   2275 C CB  . GLU B 1 141 ? 12.492  -5.514 26.217 1.00 50.50 ? 158 GLU B CB  1 
ATOM   2276 N N   . GLU B 1 142 ? 13.045  -2.624 24.881 1.00 37.94 ? 159 GLU B N   1 
ATOM   2277 C CA  . GLU B 1 142 ? 13.494  -1.278 25.192 1.00 37.45 ? 159 GLU B CA  1 
ATOM   2278 C C   . GLU B 1 142 ? 12.698  -0.200 24.470 1.00 32.54 ? 159 GLU B C   1 
ATOM   2279 O O   . GLU B 1 142 ? 12.886  0.985  24.773 1.00 31.59 ? 159 GLU B O   1 
ATOM   2280 C CB  . GLU B 1 142 ? 14.992  -1.190 24.902 1.00 36.56 ? 159 GLU B CB  1 
ATOM   2281 C CG  . GLU B 1 142 ? 15.787  -2.214 25.728 1.00 36.64 ? 159 GLU B CG  1 
ATOM   2282 C CD  . GLU B 1 142 ? 17.262  -2.244 25.413 1.00 40.66 ? 159 GLU B CD  1 
ATOM   2283 O OE1 . GLU B 1 142 ? 17.626  -1.997 24.256 1.00 40.02 ? 159 GLU B OE1 1 
ATOM   2284 O OE2 . GLU B 1 142 ? 18.066  -2.530 26.330 1.00 44.82 ? 159 GLU B OE2 1 
ATOM   2285 N N   . ILE B 1 143 ? 11.799  -0.562 23.559 1.00 30.55 ? 160 ILE B N   1 
ATOM   2286 C CA  . ILE B 1 143 ? 10.934  0.415  22.898 1.00 27.75 ? 160 ILE B CA  1 
ATOM   2287 C C   . ILE B 1 143 ? 9.658   0.538  23.724 1.00 29.50 ? 160 ILE B C   1 
ATOM   2288 O O   . ILE B 1 143 ? 8.952   -0.451 23.931 1.00 30.35 ? 160 ILE B O   1 
ATOM   2289 C CB  . ILE B 1 143 ? 10.604  0.003  21.457 1.00 30.86 ? 160 ILE B CB  1 
ATOM   2290 C CG1 . ILE B 1 143 ? 11.831  -0.579 20.756 1.00 35.63 ? 160 ILE B CG1 1 
ATOM   2291 C CG2 . ILE B 1 143 ? 10.058  1.210  20.696 1.00 29.62 ? 160 ILE B CG2 1 
ATOM   2292 C CD1 . ILE B 1 143 ? 13.013  0.346  20.684 1.00 39.32 ? 160 ILE B CD1 1 
ATOM   2293 N N   . GLN B 1 144 ? 9.360   1.749  24.179 1.00 23.71 ? 161 GLN B N   1 
ATOM   2294 C CA  . GLN B 1 144 ? 8.265   1.993  25.105 1.00 22.60 ? 161 GLN B CA  1 
ATOM   2295 C C   . GLN B 1 144 ? 7.080   2.628  24.393 1.00 21.58 ? 161 GLN B C   1 
ATOM   2296 O O   . GLN B 1 144 ? 7.245   3.573  23.622 1.00 22.00 ? 161 GLN B O   1 
ATOM   2297 C CB  . GLN B 1 144 ? 8.735   2.948  26.201 1.00 21.99 ? 161 GLN B CB  1 
ATOM   2298 C CG  . GLN B 1 144 ? 10.036  2.550  26.886 1.00 28.23 ? 161 GLN B CG  1 
ATOM   2299 C CD  . GLN B 1 144 ? 10.026  1.149  27.453 1.00 29.73 ? 161 GLN B CD  1 
ATOM   2300 O OE1 . GLN B 1 144 ? 9.020   0.679  27.984 1.00 30.32 ? 161 GLN B OE1 1 
ATOM   2301 N NE2 . GLN B 1 144 ? 11.163  0.473  27.354 1.00 27.28 ? 161 GLN B NE2 1 
ATOM   2302 N N   . SER B 1 145 ? 5.879   2.136  24.702 1.00 21.45 ? 162 SER B N   1 
ATOM   2303 C CA  A SER B 1 145 ? 4.648   2.671  24.139 0.52 21.94 ? 162 SER B CA  1 
ATOM   2304 C CA  B SER B 1 145 ? 4.634   2.654  24.143 0.48 21.40 ? 162 SER B CA  1 
ATOM   2305 C C   . SER B 1 145 ? 3.919   3.505  25.187 1.00 21.46 ? 162 SER B C   1 
ATOM   2306 O O   . SER B 1 145 ? 3.535   2.993  26.247 1.00 24.31 ? 162 SER B O   1 
ATOM   2307 C CB  A SER B 1 145 ? 3.739   1.546  23.645 0.52 25.07 ? 162 SER B CB  1 
ATOM   2308 C CB  B SER B 1 145 ? 3.705   1.502  23.753 0.48 23.26 ? 162 SER B CB  1 
ATOM   2309 O OG  A SER B 1 145 ? 2.598   2.103  23.021 0.52 25.81 ? 162 SER B OG  1 
ATOM   2310 O OG  B SER B 1 145 ? 4.345   0.576  22.908 0.48 25.25 ? 162 SER B OG  1 
ATOM   2311 N N   . TYR B 1 146 ? 3.716   4.785  24.878 1.00 19.36 ? 163 TYR B N   1 
ATOM   2312 C CA  . TYR B 1 146 ? 2.899   5.693  25.681 1.00 20.52 ? 163 TYR B CA  1 
ATOM   2313 C C   . TYR B 1 146 ? 2.490   6.855  24.779 1.00 20.36 ? 163 TYR B C   1 
ATOM   2314 O O   . TYR B 1 146 ? 3.011   7.011  23.681 1.00 20.36 ? 163 TYR B O   1 
ATOM   2315 C CB  . TYR B 1 146 ? 3.631   6.166  26.947 1.00 20.17 ? 163 TYR B CB  1 
ATOM   2316 C CG  . TYR B 1 146 ? 4.872   6.989  26.685 1.00 18.48 ? 163 TYR B CG  1 
ATOM   2317 C CD1 . TYR B 1 146 ? 6.115   6.382  26.501 1.00 17.57 ? 163 TYR B CD1 1 
ATOM   2318 C CD2 . TYR B 1 146 ? 4.805   8.365  26.631 1.00 16.39 ? 163 TYR B CD2 1 
ATOM   2319 C CE1 . TYR B 1 146 ? 7.253   7.137  26.259 1.00 17.99 ? 163 TYR B CE1 1 
ATOM   2320 C CE2 . TYR B 1 146 ? 5.933   9.131  26.382 1.00 16.85 ? 163 TYR B CE2 1 
ATOM   2321 C CZ  . TYR B 1 146 ? 7.149   8.517  26.206 1.00 17.62 ? 163 TYR B CZ  1 
ATOM   2322 O OH  . TYR B 1 146 ? 8.253   9.295  25.966 1.00 17.76 ? 163 TYR B OH  1 
ATOM   2323 N N   . LYS B 1 147 ? 1.539   7.661  25.245 1.00 20.33 ? 164 LYS B N   1 
ATOM   2324 C CA  . LYS B 1 147 ? 0.969   8.749  24.460 1.00 19.29 ? 164 LYS B CA  1 
ATOM   2325 C C   . LYS B 1 147 ? 1.309   10.082 25.105 1.00 18.52 ? 164 LYS B C   1 
ATOM   2326 O O   . LYS B 1 147 ? 1.173   10.236 26.317 1.00 21.44 ? 164 LYS B O   1 
ATOM   2327 C CB  . LYS B 1 147 ? -0.555  8.588  24.376 1.00 20.94 ? 164 LYS B CB  1 
ATOM   2328 C CG  . LYS B 1 147 ? -1.303  9.710  23.649 1.00 29.93 ? 164 LYS B CG  1 
ATOM   2329 C CD  . LYS B 1 147 ? -2.805  9.698  24.000 1.00 36.60 ? 164 LYS B CD  1 
ATOM   2330 C CE  . LYS B 1 147 ? -3.515  10.994 23.592 1.00 41.86 ? 164 LYS B CE  1 
ATOM   2331 N NZ  . LYS B 1 147 ? -4.378  10.831 22.406 1.00 44.33 ? 164 LYS B NZ  1 
ATOM   2332 N N   . LEU B 1 148 ? 1.757   11.041 24.302 1.00 17.99 ? 165 LEU B N   1 
ATOM   2333 C CA  . LEU B 1 148 ? 2.020   12.379 24.819 1.00 16.89 ? 165 LEU B CA  1 
ATOM   2334 C C   . LEU B 1 148 ? 0.721   13.091 25.167 1.00 18.37 ? 165 LEU B C   1 
ATOM   2335 O O   . LEU B 1 148 ? -0.201  13.150 24.357 1.00 17.90 ? 165 LEU B O   1 
ATOM   2336 C CB  . LEU B 1 148 ? 2.779   13.204 23.776 1.00 17.98 ? 165 LEU B CB  1 
ATOM   2337 C CG  . LEU B 1 148 ? 4.243   12.807 23.560 1.00 17.90 ? 165 LEU B CG  1 
ATOM   2338 C CD1 . LEU B 1 148 ? 4.843   13.620 22.399 1.00 20.80 ? 165 LEU B CD1 1 
ATOM   2339 C CD2 . LEU B 1 148 ? 5.082   12.968 24.827 1.00 18.85 ? 165 LEU B CD2 1 
ATOM   2340 N N   . ALA B 1 149 ? 0.683   13.686 26.364 1.00 18.46 ? 166 ALA B N   1 
ATOM   2341 C CA  . ALA B 1 149 ? -0.505  14.375 26.837 1.00 19.67 ? 166 ALA B CA  1 
ATOM   2342 C C   . ALA B 1 149 ? -0.842  15.608 26.009 1.00 19.34 ? 166 ALA B C   1 
ATOM   2343 O O   . ALA B 1 149 ? -2.006  16.027 26.001 1.00 21.90 ? 166 ALA B O   1 
ATOM   2344 C CB  . ALA B 1 149 ? -0.323  14.785 28.307 1.00 23.99 ? 166 ALA B CB  1 
ATOM   2345 N N   . LEU B 1 150 ? 0.134   16.210 25.324 1.00 18.38 ? 167 LEU B N   1 
ATOM   2346 C CA  . LEU B 1 150 ? -0.129  17.372 24.476 1.00 18.66 ? 167 LEU B CA  1 
ATOM   2347 C C   . LEU B 1 150 ? -0.487  16.996 23.041 1.00 17.69 ? 167 LEU B C   1 
ATOM   2348 O O   . LEU B 1 150 ? -0.518  17.874 22.173 1.00 17.89 ? 167 LEU B O   1 
ATOM   2349 C CB  . LEU B 1 150 ? 1.065   18.331 24.474 1.00 24.28 ? 167 LEU B CB  1 
ATOM   2350 C CG  . LEU B 1 150 ? 1.141   19.307 25.653 1.00 28.44 ? 167 LEU B CG  1 
ATOM   2351 C CD1 . LEU B 1 150 ? 2.548   19.867 25.759 1.00 32.11 ? 167 LEU B CD1 1 
ATOM   2352 C CD2 . LEU B 1 150 ? 0.138   20.437 25.497 1.00 32.53 ? 167 LEU B CD2 1 
ATOM   2353 N N   . SER B 1 151 ? -0.818  15.729 22.804 1.00 17.56 ? 168 SER B N   1 
ATOM   2354 C CA  A SER B 1 151 ? -1.085  15.256 21.448 0.27 18.34 ? 168 SER B CA  1 
ATOM   2355 C CA  B SER B 1 151 ? -1.087  15.258 21.445 0.73 17.11 ? 168 SER B CA  1 
ATOM   2356 C C   . SER B 1 151 ? -2.114  16.110 20.713 1.00 17.14 ? 168 SER B C   1 
ATOM   2357 O O   . SER B 1 151 ? -1.979  16.343 19.504 1.00 18.44 ? 168 SER B O   1 
ATOM   2358 C CB  A SER B 1 151 ? -1.552  13.799 21.504 0.27 20.51 ? 168 SER B CB  1 
ATOM   2359 C CB  B SER B 1 151 ? -1.556  13.797 21.470 0.73 17.16 ? 168 SER B CB  1 
ATOM   2360 O OG  A SER B 1 151 ? -1.887  13.322 20.217 0.27 22.71 ? 168 SER B OG  1 
ATOM   2361 O OG  B SER B 1 151 ? -0.472  12.902 21.622 0.73 21.07 ? 168 SER B OG  1 
ATOM   2362 N N   . ASP B 1 152 ? -3.179  16.554 21.405 1.00 18.05 ? 169 ASP B N   1 
ATOM   2363 C CA  . ASP B 1 152 ? -4.243  17.295 20.720 1.00 20.35 ? 169 ASP B CA  1 
ATOM   2364 C C   . ASP B 1 152 ? -3.744  18.613 20.158 1.00 17.92 ? 169 ASP B C   1 
ATOM   2365 O O   . ASP B 1 152 ? -4.395  19.193 19.276 1.00 19.03 ? 169 ASP B O   1 
ATOM   2366 C CB  . ASP B 1 152 ? -5.404  17.631 21.673 1.00 23.01 ? 169 ASP B CB  1 
ATOM   2367 C CG  . ASP B 1 152 ? -6.160  16.411 22.154 1.00 28.57 ? 169 ASP B CG  1 
ATOM   2368 O OD1 . ASP B 1 152 ? -6.206  15.394 21.437 1.00 29.41 ? 169 ASP B OD1 1 
ATOM   2369 O OD2 . ASP B 1 152 ? -6.721  16.487 23.271 1.00 31.56 ? 169 ASP B OD2 1 
ATOM   2370 N N   . TYR B 1 153 ? -2.628  19.118 20.680 1.00 15.94 ? 170 TYR B N   1 
ATOM   2371 C CA  . TYR B 1 153 ? -2.045  20.377 20.241 1.00 15.57 ? 170 TYR B CA  1 
ATOM   2372 C C   . TYR B 1 153 ? -0.795  20.201 19.402 1.00 16.10 ? 170 TYR B C   1 
ATOM   2373 O O   . TYR B 1 153 ? -0.260  21.194 18.929 1.00 17.75 ? 170 TYR B O   1 
ATOM   2374 C CB  . TYR B 1 153 ? -1.771  21.282 21.463 1.00 16.22 ? 170 TYR B CB  1 
ATOM   2375 C CG  . TYR B 1 153 ? -3.066  21.616 22.137 1.00 18.44 ? 170 TYR B CG  1 
ATOM   2376 C CD1 . TYR B 1 153 ? -3.881  22.604 21.631 1.00 17.49 ? 170 TYR B CD1 1 
ATOM   2377 C CD2 . TYR B 1 153 ? -3.507  20.899 23.241 1.00 18.12 ? 170 TYR B CD2 1 
ATOM   2378 C CE1 . TYR B 1 153 ? -5.100  22.891 22.212 1.00 18.84 ? 170 TYR B CE1 1 
ATOM   2379 C CE2 . TYR B 1 153 ? -4.719  21.169 23.822 1.00 19.76 ? 170 TYR B CE2 1 
ATOM   2380 C CZ  . TYR B 1 153 ? -5.506  22.172 23.315 1.00 19.09 ? 170 TYR B CZ  1 
ATOM   2381 O OH  . TYR B 1 153 ? -6.721  22.442 23.881 1.00 22.00 ? 170 TYR B OH  1 
ATOM   2382 N N   . ILE B 1 154 ? -0.327  18.970 19.200 1.00 17.66 ? 171 ILE B N   1 
ATOM   2383 C CA  . ILE B 1 154 ? 0.803   18.676 18.329 1.00 17.63 ? 171 ILE B CA  1 
ATOM   2384 C C   . ILE B 1 154 ? 0.342   18.159 16.972 1.00 17.10 ? 171 ILE B C   1 
ATOM   2385 O O   . ILE B 1 154 ? 0.905   18.514 15.932 1.00 20.26 ? 171 ILE B O   1 
ATOM   2386 C CB  . ILE B 1 154 ? 1.699   17.636 19.038 1.00 18.36 ? 171 ILE B CB  1 
ATOM   2387 C CG1 . ILE B 1 154 ? 2.335   18.224 20.305 1.00 19.69 ? 171 ILE B CG1 1 
ATOM   2388 C CG2 . ILE B 1 154 ? 2.754   17.095 18.081 1.00 20.03 ? 171 ILE B CG2 1 
ATOM   2389 C CD1 . ILE B 1 154 ? 2.911   17.163 21.233 1.00 21.70 ? 171 ILE B CD1 1 
ATOM   2390 N N   . PHE B 1 155 ? -0.687  17.317 16.972 1.00 17.56 ? 172 PHE B N   1 
ATOM   2391 C CA  . PHE B 1 155 ? -1.184  16.642 15.778 1.00 19.43 ? 172 PHE B CA  1 
ATOM   2392 C C   . PHE B 1 155 ? -2.519  17.218 15.327 1.00 23.14 ? 172 PHE B C   1 
ATOM   2393 O O   . PHE B 1 155 ? -3.356  17.599 16.149 1.00 24.06 ? 172 PHE B O   1 
ATOM   2394 C CB  . PHE B 1 155 ? -1.335  15.138 16.049 1.00 18.83 ? 172 PHE B CB  1 
ATOM   2395 C CG  . PHE B 1 155 ? -0.084  14.513 16.553 1.00 17.17 ? 172 PHE B CG  1 
ATOM   2396 C CD1 . PHE B 1 155 ? 1.017   14.407 15.728 1.00 18.23 ? 172 PHE B CD1 1 
ATOM   2397 C CD2 . PHE B 1 155 ? 0.013   14.064 17.862 1.00 19.60 ? 172 PHE B CD2 1 
ATOM   2398 C CE1 . PHE B 1 155 ? 2.180   13.853 16.192 1.00 19.69 ? 172 PHE B CE1 1 
ATOM   2399 C CE2 . PHE B 1 155 ? 1.181   13.521 18.323 1.00 22.12 ? 172 PHE B CE2 1 
ATOM   2400 C CZ  . PHE B 1 155 ? 2.265   13.416 17.498 1.00 20.11 ? 172 PHE B CZ  1 
ATOM   2401 N N   . GLU B 1 156 ? -2.690  17.286 14.005 1.00 25.28 ? 173 GLU B N   1 
ATOM   2402 C CA  . GLU B 1 156 ? -3.951  17.612 13.351 1.00 32.15 ? 173 GLU B CA  1 
ATOM   2403 C C   . GLU B 1 156 ? -5.058  16.636 13.658 1.00 37.25 ? 173 GLU B C   1 
ATOM   2404 O O   . GLU B 1 156 ? -6.225  16.999 13.528 1.00 41.12 ? 173 GLU B O   1 
ATOM   2405 C CB  . GLU B 1 156 ? -3.781  17.534 11.836 1.00 36.76 ? 173 GLU B CB  1 
ATOM   2406 C CG  . GLU B 1 156 ? -2.997  18.619 11.286 1.00 36.16 ? 173 GLU B CG  1 
ATOM   2407 C CD  . GLU B 1 156 ? -2.767  18.480 9.802  1.00 31.98 ? 173 GLU B CD  1 
ATOM   2408 O OE1 . GLU B 1 156 ? -3.176  17.465 9.171  1.00 34.10 ? 173 GLU B OE1 1 
ATOM   2409 O OE2 . GLU B 1 156 ? -2.178  19.414 9.258  1.00 27.13 ? 173 GLU B OE2 1 
ATOM   2410 O OXT . GLU B 1 156 ? -4.799  15.477 13.984 1.00 41.16 ? 173 GLU B OXT 1 
ATOM   2411 N N   . HIS C 1 8   ? 43.680  21.183 8.762  1.00 44.12 ? 25  HIS C N   1 
ATOM   2412 C CA  . HIS C 1 8   ? 44.068  22.524 8.346  1.00 39.37 ? 25  HIS C CA  1 
ATOM   2413 C C   . HIS C 1 8   ? 43.027  23.558 8.778  1.00 33.98 ? 25  HIS C C   1 
ATOM   2414 O O   . HIS C 1 8   ? 41.928  23.624 8.220  1.00 39.42 ? 25  HIS C O   1 
ATOM   2415 C CB  . HIS C 1 8   ? 44.231  22.585 6.833  1.00 41.72 ? 25  HIS C CB  1 
ATOM   2416 N N   . VAL C 1 9   ? 43.376  24.374 9.761  1.00 27.77 ? 26  VAL C N   1 
ATOM   2417 C CA  . VAL C 1 9   ? 42.504  25.452 10.202 1.00 25.09 ? 26  VAL C CA  1 
ATOM   2418 C C   . VAL C 1 9   ? 42.978  26.766 9.620  1.00 22.23 ? 26  VAL C C   1 
ATOM   2419 O O   . VAL C 1 9   ? 44.096  26.903 9.111  1.00 24.04 ? 26  VAL C O   1 
ATOM   2420 C CB  . VAL C 1 9   ? 42.404  25.530 11.743 1.00 23.68 ? 26  VAL C CB  1 
ATOM   2421 C CG1 . VAL C 1 9   ? 41.738  24.266 12.287 1.00 25.79 ? 26  VAL C CG1 1 
ATOM   2422 C CG2 . VAL C 1 9   ? 43.772  25.778 12.369 1.00 25.23 ? 26  VAL C CG2 1 
ATOM   2423 N N   . GLU C 1 10  ? 42.107  27.770 9.673  1.00 19.04 ? 27  GLU C N   1 
ATOM   2424 C CA  . GLU C 1 10  ? 42.466  29.129 9.324  1.00 20.94 ? 27  GLU C CA  1 
ATOM   2425 C C   . GLU C 1 10  ? 41.896  30.059 10.383 1.00 17.78 ? 27  GLU C C   1 
ATOM   2426 O O   . GLU C 1 10  ? 41.234  29.623 11.329 1.00 16.44 ? 27  GLU C O   1 
ATOM   2427 C CB  . GLU C 1 10  ? 41.996  29.469 7.911  1.00 24.74 ? 27  GLU C CB  1 
ATOM   2428 C CG  . GLU C 1 10  ? 40.513  29.425 7.766  1.00 22.48 ? 27  GLU C CG  1 
ATOM   2429 C CD  . GLU C 1 10  ? 40.031  29.511 6.323  1.00 23.58 ? 27  GLU C CD  1 
ATOM   2430 O OE1 . GLU C 1 10  ? 40.786  29.314 5.354  1.00 32.66 ? 27  GLU C OE1 1 
ATOM   2431 O OE2 . GLU C 1 10  ? 38.856  29.806 6.163  1.00 20.36 ? 27  GLU C OE2 1 
ATOM   2432 N N   . GLN C 1 11  ? 42.187  31.342 10.239 1.00 17.96 ? 28  GLN C N   1 
ATOM   2433 C CA  . GLN C 1 11  ? 41.759  32.367 11.180 1.00 17.29 ? 28  GLN C CA  1 
ATOM   2434 C C   . GLN C 1 11  ? 41.043  33.484 10.434 1.00 17.56 ? 28  GLN C C   1 
ATOM   2435 O O   . GLN C 1 11  ? 41.448  33.880 9.336  1.00 19.10 ? 28  GLN C O   1 
ATOM   2436 C CB  . GLN C 1 11  ? 42.950  32.938 11.935 1.00 18.10 ? 28  GLN C CB  1 
ATOM   2437 C CG  . GLN C 1 11  ? 43.545  31.944 12.903 1.00 19.46 ? 28  GLN C CG  1 
ATOM   2438 C CD  . GLN C 1 11  ? 44.616  32.543 13.788 1.00 22.74 ? 28  GLN C CD  1 
ATOM   2439 O OE1 . GLN C 1 11  ? 45.035  33.685 13.613 1.00 26.91 ? 28  GLN C OE1 1 
ATOM   2440 N NE2 . GLN C 1 11  ? 45.062  31.769 14.748 1.00 26.03 ? 28  GLN C NE2 1 
ATOM   2441 N N   . THR C 1 12  ? 39.969  33.980 11.042 1.00 16.81 ? 29  THR C N   1 
ATOM   2442 C CA  . THR C 1 12  ? 39.192  35.069 10.484 1.00 16.65 ? 29  THR C CA  1 
ATOM   2443 C C   . THR C 1 12  ? 39.082  36.189 11.498 1.00 16.01 ? 29  THR C C   1 
ATOM   2444 O O   . THR C 1 12  ? 39.128  35.956 12.707 1.00 15.81 ? 29  THR C O   1 
ATOM   2445 C CB  . THR C 1 12  ? 37.790  34.632 10.025 1.00 16.37 ? 29  THR C CB  1 
ATOM   2446 O OG1 . THR C 1 12  ? 37.241  35.679 9.217  1.00 17.21 ? 29  THR C OG1 1 
ATOM   2447 C CG2 . THR C 1 12  ? 36.833  34.356 11.189 1.00 16.03 ? 29  THR C CG2 1 
ATOM   2448 N N   . TYR C 1 13  ? 38.927  37.410 10.991 1.00 15.26 ? 30  TYR C N   1 
ATOM   2449 C CA  . TYR C 1 13  ? 38.713  38.581 11.830 1.00 15.80 ? 30  TYR C CA  1 
ATOM   2450 C C   . TYR C 1 13  ? 37.214  38.846 11.920 1.00 17.03 ? 30  TYR C C   1 
ATOM   2451 O O   . TYR C 1 13  ? 36.534  39.002 10.899 1.00 17.49 ? 30  TYR C O   1 
ATOM   2452 C CB  . TYR C 1 13  ? 39.463  39.809 11.285 1.00 17.95 ? 30  TYR C CB  1 
ATOM   2453 C CG  . TYR C 1 13  ? 39.183  41.039 12.118 1.00 17.14 ? 30  TYR C CG  1 
ATOM   2454 C CD1 . TYR C 1 13  ? 39.690  41.150 13.408 1.00 17.64 ? 30  TYR C CD1 1 
ATOM   2455 C CD2 . TYR C 1 13  ? 38.381  42.066 11.640 1.00 15.68 ? 30  TYR C CD2 1 
ATOM   2456 C CE1 . TYR C 1 13  ? 39.407  42.226 14.197 1.00 18.17 ? 30  TYR C CE1 1 
ATOM   2457 C CE2 . TYR C 1 13  ? 38.081  43.180 12.434 1.00 17.35 ? 30  TYR C CE2 1 
ATOM   2458 C CZ  . TYR C 1 13  ? 38.604  43.251 13.714 1.00 15.37 ? 30  TYR C CZ  1 
ATOM   2459 O OH  . TYR C 1 13  ? 38.328  44.312 14.554 1.00 19.09 ? 30  TYR C OH  1 
ATOM   2460 N N   . LEU C 1 14  ? 36.688  38.840 13.142 1.00 15.33 ? 31  LEU C N   1 
ATOM   2461 C CA  . LEU C 1 14  ? 35.295  39.138 13.420 1.00 15.59 ? 31  LEU C CA  1 
ATOM   2462 C C   . LEU C 1 14  ? 35.249  40.303 14.395 1.00 15.17 ? 31  LEU C C   1 
ATOM   2463 O O   . LEU C 1 14  ? 36.012  40.341 15.363 1.00 17.38 ? 31  LEU C O   1 
ATOM   2464 C CB  . LEU C 1 14  ? 34.570  37.927 14.026 1.00 15.70 ? 31  LEU C CB  1 
ATOM   2465 C CG  . LEU C 1 14  ? 34.302  36.783 13.034 1.00 17.91 ? 31  LEU C CG  1 
ATOM   2466 C CD1 . LEU C 1 14  ? 34.165  35.441 13.720 1.00 19.76 ? 31  LEU C CD1 1 
ATOM   2467 C CD2 . LEU C 1 14  ? 33.040  37.111 12.251 1.00 19.25 ? 31  LEU C CD2 1 
ATOM   2468 N N   . MET C 1 15  ? 34.367  41.257 14.134 1.00 15.29 ? 32  MET C N   1 
ATOM   2469 C CA  . MET C 1 15  ? 34.283  42.468 14.935 1.00 15.43 ? 32  MET C CA  1 
ATOM   2470 C C   . MET C 1 15  ? 32.829  42.724 15.283 1.00 14.14 ? 32  MET C C   1 
ATOM   2471 O O   . MET C 1 15  ? 31.990  42.884 14.391 1.00 17.37 ? 32  MET C O   1 
ATOM   2472 C CB  . MET C 1 15  ? 34.859  43.664 14.180 1.00 16.98 ? 32  MET C CB  1 
ATOM   2473 C CG  . MET C 1 15  ? 34.840  44.955 14.968 1.00 17.81 ? 32  MET C CG  1 
ATOM   2474 S SD  . MET C 1 15  ? 35.844  46.245 14.179 1.00 20.68 ? 32  MET C SD  1 
ATOM   2475 C CE  . MET C 1 15  ? 35.213  46.252 12.514 1.00 21.13 ? 32  MET C CE  1 
ATOM   2476 N N   . ILE C 1 16  ? 32.533  42.796 16.574 1.00 15.28 ? 33  ILE C N   1 
ATOM   2477 C CA  . ILE C 1 16  ? 31.203  43.195 17.017 1.00 14.81 ? 33  ILE C CA  1 
ATOM   2478 C C   . ILE C 1 16  ? 31.141  44.713 16.938 1.00 15.07 ? 33  ILE C C   1 
ATOM   2479 O O   . ILE C 1 16  ? 32.006  45.404 17.481 1.00 15.73 ? 33  ILE C O   1 
ATOM   2480 C CB  . ILE C 1 16  ? 30.919  42.686 18.435 1.00 14.24 ? 33  ILE C CB  1 
ATOM   2481 C CG1 . ILE C 1 16  ? 31.104  41.169 18.455 1.00 16.85 ? 33  ILE C CG1 1 
ATOM   2482 C CG2 . ILE C 1 16  ? 29.502  43.116 18.863 1.00 15.79 ? 33  ILE C CG2 1 
ATOM   2483 C CD1 . ILE C 1 16  ? 30.825  40.530 19.813 1.00 16.73 ? 33  ILE C CD1 1 
ATOM   2484 N N   . LYS C 1 17  ? 30.166  45.224 16.196 1.00 14.49 ? 34  LYS C N   1 
ATOM   2485 C CA  . LYS C 1 17  ? 30.038  46.647 15.942 1.00 14.77 ? 34  LYS C CA  1 
ATOM   2486 C C   . LYS C 1 17  ? 29.372  47.328 17.137 1.00 14.58 ? 34  LYS C C   1 
ATOM   2487 O O   . LYS C 1 17  ? 28.886  46.671 18.063 1.00 14.60 ? 34  LYS C O   1 
ATOM   2488 C CB  . LYS C 1 17  ? 29.212  46.830 14.674 1.00 14.86 ? 34  LYS C CB  1 
ATOM   2489 C CG  . LYS C 1 17  ? 29.818  46.157 13.457 1.00 15.64 ? 34  LYS C CG  1 
ATOM   2490 C CD  . LYS C 1 17  ? 28.981  46.440 12.208 1.00 18.00 ? 34  LYS C CD  1 
ATOM   2491 C CE  . LYS C 1 17  ? 29.644  45.920 10.944 1.00 17.31 ? 34  LYS C CE  1 
ATOM   2492 N NZ  . LYS C 1 17  ? 28.816  46.145 9.729  1.00 20.73 ? 34  LYS C NZ  1 
ATOM   2493 N N   . PRO C 1 18  ? 29.313  48.660 17.147 1.00 15.28 ? 35  PRO C N   1 
ATOM   2494 C CA  . PRO C 1 18  ? 28.771  49.352 18.328 1.00 15.57 ? 35  PRO C CA  1 
ATOM   2495 C C   . PRO C 1 18  ? 27.356  48.948 18.678 1.00 13.75 ? 35  PRO C C   1 
ATOM   2496 O O   . PRO C 1 18  ? 26.985  48.978 19.863 1.00 15.53 ? 35  PRO C O   1 
ATOM   2497 C CB  . PRO C 1 18  ? 28.876  50.833 17.940 1.00 17.37 ? 35  PRO C CB  1 
ATOM   2498 C CG  . PRO C 1 18  ? 30.011  50.870 16.978 1.00 17.75 ? 35  PRO C CG  1 
ATOM   2499 C CD  . PRO C 1 18  ? 29.868  49.621 16.166 1.00 16.61 ? 35  PRO C CD  1 
ATOM   2500 N N   . ASP C 1 19  ? 26.543  48.576 17.692 1.00 14.49 ? 36  ASP C N   1 
ATOM   2501 C CA  . ASP C 1 19  ? 25.197  48.111 17.997 1.00 14.60 ? 36  ASP C CA  1 
ATOM   2502 C C   . ASP C 1 19  ? 25.208  46.794 18.774 1.00 14.84 ? 36  ASP C C   1 
ATOM   2503 O O   . ASP C 1 19  ? 24.359  46.577 19.655 1.00 15.43 ? 36  ASP C O   1 
ATOM   2504 C CB  . ASP C 1 19  ? 24.314  48.061 16.745 1.00 15.28 ? 36  ASP C CB  1 
ATOM   2505 C CG  . ASP C 1 19  ? 24.907  47.260 15.583 1.00 15.28 ? 36  ASP C CG  1 
ATOM   2506 O OD1 . ASP C 1 19  ? 26.138  47.258 15.381 1.00 17.72 ? 36  ASP C OD1 1 
ATOM   2507 O OD2 . ASP C 1 19  ? 24.108  46.667 14.827 1.00 15.34 ? 36  ASP C OD2 1 
ATOM   2508 N N   . GLY C 1 20  ? 26.155  45.910 18.483 1.00 15.53 ? 37  GLY C N   1 
ATOM   2509 C CA  . GLY C 1 20  ? 26.270  44.693 19.269 1.00 15.37 ? 37  GLY C CA  1 
ATOM   2510 C C   . GLY C 1 20  ? 26.645  44.975 20.709 1.00 16.65 ? 37  GLY C C   1 
ATOM   2511 O O   . GLY C 1 20  ? 26.159  44.312 21.632 1.00 15.39 ? 37  GLY C O   1 
ATOM   2512 N N   . ILE C 1 21  ? 27.532  45.947 20.915 1.00 15.09 ? 38  ILE C N   1 
ATOM   2513 C CA  . ILE C 1 21  ? 27.933  46.313 22.267 1.00 15.04 ? 38  ILE C CA  1 
ATOM   2514 C C   . ILE C 1 21  ? 26.758  46.920 23.009 1.00 13.94 ? 38  ILE C C   1 
ATOM   2515 O O   . ILE C 1 21  ? 26.448  46.540 24.146 1.00 15.80 ? 38  ILE C O   1 
ATOM   2516 C CB  . ILE C 1 21  ? 29.128  47.288 22.245 1.00 15.91 ? 38  ILE C CB  1 
ATOM   2517 C CG1 . ILE C 1 21  ? 30.321  46.752 21.430 1.00 17.85 ? 38  ILE C CG1 1 
ATOM   2518 C CG2 . ILE C 1 21  ? 29.510  47.686 23.689 1.00 16.73 ? 38  ILE C CG2 1 
ATOM   2519 C CD1 . ILE C 1 21  ? 30.860  45.448 21.892 1.00 19.66 ? 38  ILE C CD1 1 
ATOM   2520 N N   . GLN C 1 22  ? 26.082  47.889 22.373 1.00 14.34 ? 39  GLN C N   1 
ATOM   2521 C CA  . GLN C 1 22  ? 25.047  48.663 23.059 1.00 15.01 ? 39  GLN C CA  1 
ATOM   2522 C C   . GLN C 1 22  ? 23.798  47.841 23.312 1.00 14.14 ? 39  GLN C C   1 
ATOM   2523 O O   . GLN C 1 22  ? 23.089  48.087 24.295 1.00 15.82 ? 39  GLN C O   1 
ATOM   2524 C CB  . GLN C 1 22  ? 24.699  49.893 22.214 1.00 16.60 ? 39  GLN C CB  1 
ATOM   2525 C CG  . GLN C 1 22  ? 25.781  50.953 22.239 1.00 16.60 ? 39  GLN C CG  1 
ATOM   2526 C CD  . GLN C 1 22  ? 25.811  51.697 23.528 1.00 18.75 ? 39  GLN C CD  1 
ATOM   2527 O OE1 . GLN C 1 22  ? 25.010  51.423 24.418 1.00 19.97 ? 39  GLN C OE1 1 
ATOM   2528 N NE2 . GLN C 1 22  ? 26.707  52.668 23.637 1.00 20.19 ? 39  GLN C NE2 1 
ATOM   2529 N N   . ARG C 1 23  ? 23.465  46.916 22.403 1.00 13.83 ? 40  ARG C N   1 
ATOM   2530 C CA  . ARG C 1 23  ? 22.340  46.007 22.626 1.00 14.52 ? 40  ARG C CA  1 
ATOM   2531 C C   . ARG C 1 23  ? 22.697  44.878 23.583 1.00 15.64 ? 40  ARG C C   1 
ATOM   2532 O O   . ARG C 1 23  ? 21.819  44.095 23.966 1.00 16.74 ? 40  ARG C O   1 
ATOM   2533 C CB  . ARG C 1 23  ? 21.811  45.472 21.288 1.00 15.11 ? 40  ARG C CB  1 
ATOM   2534 C CG  . ARG C 1 23  ? 21.311  46.590 20.402 1.00 14.18 ? 40  ARG C CG  1 
ATOM   2535 C CD  . ARG C 1 23  ? 20.891  46.152 19.008 1.00 16.21 ? 40  ARG C CD  1 
ATOM   2536 N NE  . ARG C 1 23  ? 19.761  45.240 19.104 1.00 16.93 ? 40  ARG C NE  1 
ATOM   2537 C CZ  . ARG C 1 23  ? 19.376  44.414 18.150 1.00 15.95 ? 40  ARG C CZ  1 
ATOM   2538 N NH1 . ARG C 1 23  ? 20.009  44.352 16.993 1.00 15.48 ? 40  ARG C NH1 1 
ATOM   2539 N NH2 . ARG C 1 23  ? 18.343  43.617 18.370 1.00 17.32 ? 40  ARG C NH2 1 
ATOM   2540 N N   . GLN C 1 24  ? 23.966  44.795 23.968 1.00 15.54 ? 41  GLN C N   1 
ATOM   2541 C CA  . GLN C 1 24  ? 24.436  43.892 25.009 1.00 16.17 ? 41  GLN C CA  1 
ATOM   2542 C C   . GLN C 1 24  ? 24.190  42.430 24.656 1.00 14.98 ? 41  GLN C C   1 
ATOM   2543 O O   . GLN C 1 24  ? 23.698  41.633 25.456 1.00 15.51 ? 41  GLN C O   1 
ATOM   2544 C CB  . GLN C 1 24  ? 23.890  44.288 26.381 1.00 14.57 ? 41  GLN C CB  1 
ATOM   2545 C CG  . GLN C 1 24  ? 24.218  45.723 26.740 1.00 15.08 ? 41  GLN C CG  1 
ATOM   2546 C CD  . GLN C 1 24  ? 24.530  45.877 28.215 1.00 17.99 ? 41  GLN C CD  1 
ATOM   2547 O OE1 . GLN C 1 24  ? 23.662  46.198 29.009 1.00 19.26 ? 41  GLN C OE1 1 
ATOM   2548 N NE2 . GLN C 1 24  ? 25.781  45.660 28.577 1.00 18.18 ? 41  GLN C NE2 1 
ATOM   2549 N N   . VAL C 1 25  ? 24.619  42.068 23.450 1.00 14.04 ? 42  VAL C N   1 
ATOM   2550 C CA  . VAL C 1 25  ? 24.531  40.716 22.918 1.00 13.91 ? 42  VAL C CA  1 
ATOM   2551 C C   . VAL C 1 25  ? 25.918  40.144 22.615 1.00 13.29 ? 42  VAL C C   1 
ATOM   2552 O O   . VAL C 1 25  ? 26.039  39.180 21.865 1.00 15.24 ? 42  VAL C O   1 
ATOM   2553 C CB  . VAL C 1 25  ? 23.582  40.642 21.703 1.00 14.49 ? 42  VAL C CB  1 
ATOM   2554 C CG1 . VAL C 1 25  ? 22.143  40.960 22.114 1.00 16.81 ? 42  VAL C CG1 1 
ATOM   2555 C CG2 . VAL C 1 25  ? 24.040  41.587 20.596 1.00 15.76 ? 42  VAL C CG2 1 
ATOM   2556 N N   . VAL C 1 26  ? 26.966  40.724 23.217 1.00 13.97 ? 43  VAL C N   1 
ATOM   2557 C CA  . VAL C 1 26  ? 28.332  40.254 22.979 1.00 14.90 ? 43  VAL C CA  1 
ATOM   2558 C C   . VAL C 1 26  ? 28.458  38.776 23.322 1.00 13.87 ? 43  VAL C C   1 
ATOM   2559 O O   . VAL C 1 26  ? 28.997  37.974 22.542 1.00 14.45 ? 43  VAL C O   1 
ATOM   2560 C CB  . VAL C 1 26  ? 29.340  41.113 23.769 1.00 14.33 ? 43  VAL C CB  1 
ATOM   2561 C CG1 . VAL C 1 26  ? 30.728  40.461 23.760 1.00 15.32 ? 43  VAL C CG1 1 
ATOM   2562 C CG2 . VAL C 1 26  ? 29.383  42.523 23.230 1.00 15.82 ? 43  VAL C CG2 1 
ATOM   2563 N N   . GLY C 1 27  ? 27.976  38.389 24.501 1.00 13.72 ? 44  GLY C N   1 
ATOM   2564 C CA  . GLY C 1 27  ? 28.113  37.012 24.917 1.00 14.01 ? 44  GLY C CA  1 
ATOM   2565 C C   . GLY C 1 27  ? 27.372  36.053 24.009 1.00 14.76 ? 44  GLY C C   1 
ATOM   2566 O O   . GLY C 1 27  ? 27.865  34.966 23.709 1.00 14.91 ? 44  GLY C O   1 
ATOM   2567 N N   . GLU C 1 28  ? 26.161  36.432 23.583 1.00 13.87 ? 45  GLU C N   1 
ATOM   2568 C CA  . GLU C 1 28  ? 25.409  35.566 22.675 1.00 14.88 ? 45  GLU C CA  1 
ATOM   2569 C C   . GLU C 1 28  ? 26.160  35.372 21.357 1.00 12.82 ? 45  GLU C C   1 
ATOM   2570 O O   . GLU C 1 28  ? 26.167  34.273 20.798 1.00 14.24 ? 45  GLU C O   1 
ATOM   2571 C CB  . GLU C 1 28  ? 24.037  36.161 22.381 1.00 16.82 ? 45  GLU C CB  1 
ATOM   2572 C CG  . GLU C 1 28  ? 23.060  36.159 23.511 1.00 19.20 ? 45  GLU C CG  1 
ATOM   2573 C CD  . GLU C 1 28  ? 21.695  36.606 23.019 1.00 29.62 ? 45  GLU C CD  1 
ATOM   2574 O OE1 . GLU C 1 28  ? 21.115  35.909 22.158 1.00 34.08 ? 45  GLU C OE1 1 
ATOM   2575 O OE2 . GLU C 1 28  ? 21.226  37.666 23.461 1.00 34.03 ? 45  GLU C OE2 1 
ATOM   2576 N N   . ILE C 1 29  ? 26.790  36.431 20.849 1.00 14.65 ? 46  ILE C N   1 
ATOM   2577 C CA  . ILE C 1 29  ? 27.545  36.326 19.602 1.00 14.10 ? 46  ILE C CA  1 
ATOM   2578 C C   . ILE C 1 29  ? 28.724  35.388 19.782 1.00 12.22 ? 46  ILE C C   1 
ATOM   2579 O O   . ILE C 1 29  ? 28.953  34.488 18.971 1.00 14.45 ? 46  ILE C O   1 
ATOM   2580 C CB  . ILE C 1 29  ? 28.007  37.717 19.141 1.00 14.16 ? 46  ILE C CB  1 
ATOM   2581 C CG1 . ILE C 1 29  ? 26.806  38.567 18.734 1.00 15.99 ? 46  ILE C CG1 1 
ATOM   2582 C CG2 . ILE C 1 29  ? 29.020  37.604 17.997 1.00 16.19 ? 46  ILE C CG2 1 
ATOM   2583 C CD1 . ILE C 1 29  ? 27.131  40.028 18.514 1.00 16.97 ? 46  ILE C CD1 1 
ATOM   2584 N N   . ILE C 1 30  ? 29.479  35.571 20.870 1.00 14.35 ? 47  ILE C N   1 
ATOM   2585 C CA  . ILE C 1 30  ? 30.630  34.716 21.117 1.00 13.67 ? 47  ILE C CA  1 
ATOM   2586 C C   . ILE C 1 30  ? 30.189  33.267 21.249 1.00 13.73 ? 47  ILE C C   1 
ATOM   2587 O O   . ILE C 1 30  ? 30.829  32.358 20.710 1.00 13.71 ? 47  ILE C O   1 
ATOM   2588 C CB  . ILE C 1 30  ? 31.411  35.215 22.344 1.00 13.58 ? 47  ILE C CB  1 
ATOM   2589 C CG1 . ILE C 1 30  ? 32.072  36.566 22.047 1.00 15.78 ? 47  ILE C CG1 1 
ATOM   2590 C CG2 . ILE C 1 30  ? 32.429  34.176 22.792 1.00 14.42 ? 47  ILE C CG2 1 
ATOM   2591 C CD1 . ILE C 1 30  ? 32.558  37.276 23.293 1.00 16.41 ? 47  ILE C CD1 1 
ATOM   2592 N N   . SER C 1 31  ? 29.098  33.025 21.976 1.00 13.92 ? 48  SER C N   1 
ATOM   2593 C CA  . SER C 1 31  ? 28.615  31.660 22.157 1.00 13.20 ? 48  SER C CA  1 
ATOM   2594 C C   . SER C 1 31  ? 28.311  30.961 20.835 1.00 15.23 ? 48  SER C C   1 
ATOM   2595 O O   . SER C 1 31  ? 28.503  29.740 20.728 1.00 15.61 ? 48  SER C O   1 
ATOM   2596 C CB  . SER C 1 31  ? 27.373  31.644 23.055 1.00 13.43 ? 48  SER C CB  1 
ATOM   2597 O OG  . SER C 1 31  ? 27.720  31.922 24.403 1.00 15.51 ? 48  SER C OG  1 
ATOM   2598 N N   . ARG C 1 32  ? 27.832  31.692 19.821 1.00 13.93 ? 49  ARG C N   1 
ATOM   2599 C CA  . ARG C 1 32  ? 27.533  31.035 18.555 1.00 14.10 ? 49  ARG C CA  1 
ATOM   2600 C C   . ARG C 1 32  ? 28.790  30.463 17.901 1.00 14.59 ? 49  ARG C C   1 
ATOM   2601 O O   . ARG C 1 32  ? 28.748  29.392 17.287 1.00 15.05 ? 49  ARG C O   1 
ATOM   2602 C CB  . ARG C 1 32  ? 26.855  32.012 17.599 1.00 14.92 ? 49  ARG C CB  1 
ATOM   2603 C CG  . ARG C 1 32  ? 25.440  32.345 18.000 1.00 16.11 ? 49  ARG C CG  1 
ATOM   2604 C CD  . ARG C 1 32  ? 24.721  33.000 16.852 1.00 22.65 ? 49  ARG C CD  1 
ATOM   2605 N NE  . ARG C 1 32  ? 23.346  33.299 17.220 1.00 23.31 ? 49  ARG C NE  1 
ATOM   2606 C CZ  . ARG C 1 32  ? 22.334  33.281 16.375 1.00 20.26 ? 49  ARG C CZ  1 
ATOM   2607 N NH1 . ARG C 1 32  ? 22.513  33.018 15.086 1.00 19.26 ? 49  ARG C NH1 1 
ATOM   2608 N NH2 . ARG C 1 32  ? 21.114  33.546 16.827 1.00 21.50 ? 49  ARG C NH2 1 
ATOM   2609 N N   . PHE C 1 33  ? 29.907  31.172 18.000 1.00 14.05 ? 50  PHE C N   1 
ATOM   2610 C CA  . PHE C 1 33  ? 31.144  30.670 17.422 1.00 14.64 ? 50  PHE C CA  1 
ATOM   2611 C C   . PHE C 1 33  ? 31.779  29.598 18.290 1.00 14.58 ? 50  PHE C C   1 
ATOM   2612 O O   . PHE C 1 33  ? 32.274  28.594 17.768 1.00 15.05 ? 50  PHE C O   1 
ATOM   2613 C CB  . PHE C 1 33  ? 32.086  31.837 17.123 1.00 15.72 ? 50  PHE C CB  1 
ATOM   2614 C CG  . PHE C 1 33  ? 31.525  32.787 16.109 1.00 15.10 ? 50  PHE C CG  1 
ATOM   2615 C CD1 . PHE C 1 33  ? 31.420  32.401 14.787 1.00 15.98 ? 50  PHE C CD1 1 
ATOM   2616 C CD2 . PHE C 1 33  ? 31.069  34.038 16.471 1.00 17.45 ? 50  PHE C CD2 1 
ATOM   2617 C CE1 . PHE C 1 33  ? 30.873  33.241 13.849 1.00 16.85 ? 50  PHE C CE1 1 
ATOM   2618 C CE2 . PHE C 1 33  ? 30.527  34.904 15.531 1.00 17.11 ? 50  PHE C CE2 1 
ATOM   2619 C CZ  . PHE C 1 33  ? 30.439  34.510 14.223 1.00 16.55 ? 50  PHE C CZ  1 
ATOM   2620 N N   . GLU C 1 34  ? 31.765  29.775 19.614 1.00 14.05 ? 51  GLU C N   1 
ATOM   2621 C CA  . GLU C 1 34  ? 32.283  28.728 20.485 1.00 15.44 ? 51  GLU C CA  1 
ATOM   2622 C C   . GLU C 1 34  ? 31.524  27.426 20.296 1.00 15.31 ? 51  GLU C C   1 
ATOM   2623 O O   . GLU C 1 34  ? 32.099  26.338 20.452 1.00 16.10 ? 51  GLU C O   1 
ATOM   2624 C CB  . GLU C 1 34  ? 32.131  29.138 21.945 1.00 14.99 ? 51  GLU C CB  1 
ATOM   2625 C CG  . GLU C 1 34  ? 33.127  30.154 22.458 1.00 15.78 ? 51  GLU C CG  1 
ATOM   2626 C CD  . GLU C 1 34  ? 32.896  30.433 23.940 1.00 15.11 ? 51  GLU C CD  1 
ATOM   2627 O OE1 . GLU C 1 34  ? 31.795  30.956 24.251 1.00 15.85 ? 51  GLU C OE1 1 
ATOM   2628 O OE2 . GLU C 1 34  ? 33.806  30.126 24.760 1.00 17.07 ? 51  GLU C OE2 1 
ATOM   2629 N N   . LYS C 1 35  ? 30.233  27.520 19.949 1.00 14.46 ? 52  LYS C N   1 
ATOM   2630 C CA  . LYS C 1 35  ? 29.400  26.325 19.859 1.00 14.92 ? 52  LYS C CA  1 
ATOM   2631 C C   . LYS C 1 35  ? 29.905  25.356 18.800 1.00 14.40 ? 52  LYS C C   1 
ATOM   2632 O O   . LYS C 1 35  ? 29.675  24.151 18.911 1.00 15.61 ? 52  LYS C O   1 
ATOM   2633 C CB  . LYS C 1 35  ? 27.949  26.732 19.573 1.00 15.78 ? 52  LYS C CB  1 
ATOM   2634 C CG  . LYS C 1 35  ? 26.960  25.617 19.776 1.00 16.77 ? 52  LYS C CG  1 
ATOM   2635 C CD  . LYS C 1 35  ? 25.540  26.116 19.507 1.00 27.67 ? 52  LYS C CD  1 
ATOM   2636 C CE  . LYS C 1 35  ? 24.540  25.440 20.407 1.00 34.38 ? 52  LYS C CE  1 
ATOM   2637 N NZ  . LYS C 1 35  ? 24.802  25.693 21.843 1.00 40.75 ? 52  LYS C NZ  1 
ATOM   2638 N N   . ARG C 1 36  ? 30.567  25.859 17.757 1.00 15.11 ? 53  ARG C N   1 
ATOM   2639 C CA  . ARG C 1 36  ? 31.099  25.007 16.698 1.00 15.85 ? 53  ARG C CA  1 
ATOM   2640 C C   . ARG C 1 36  ? 32.503  24.528 16.991 1.00 14.45 ? 53  ARG C C   1 
ATOM   2641 O O   . ARG C 1 36  ? 33.117  23.890 16.136 1.00 16.85 ? 53  ARG C O   1 
ATOM   2642 C CB  . ARG C 1 36  ? 31.085  25.736 15.351 1.00 15.41 ? 53  ARG C CB  1 
ATOM   2643 C CG  . ARG C 1 36  ? 29.675  26.052 14.871 1.00 15.53 ? 53  ARG C CG  1 
ATOM   2644 C CD  . ARG C 1 36  ? 29.656  26.607 13.477 1.00 15.95 ? 53  ARG C CD  1 
ATOM   2645 N NE  . ARG C 1 36  ? 29.982  25.582 12.493 1.00 14.51 ? 53  ARG C NE  1 
ATOM   2646 C CZ  . ARG C 1 36  ? 29.918  25.772 11.186 1.00 13.69 ? 53  ARG C CZ  1 
ATOM   2647 N NH1 . ARG C 1 36  ? 29.631  26.959 10.679 1.00 16.16 ? 53  ARG C NH1 1 
ATOM   2648 N NH2 . ARG C 1 36  ? 30.140  24.747 10.378 1.00 17.06 ? 53  ARG C NH2 1 
ATOM   2649 N N   . GLY C 1 37  ? 33.024  24.821 18.178 1.00 14.04 ? 54  GLY C N   1 
ATOM   2650 C CA  . GLY C 1 37  ? 34.392  24.459 18.469 1.00 14.71 ? 54  GLY C CA  1 
ATOM   2651 C C   . GLY C 1 37  ? 35.412  25.386 17.861 1.00 14.91 ? 54  GLY C C   1 
ATOM   2652 O O   . GLY C 1 37  ? 36.574  24.996 17.722 1.00 17.87 ? 54  GLY C O   1 
ATOM   2653 N N   . TYR C 1 38  ? 35.002  26.589 17.455 1.00 14.63 ? 55  TYR C N   1 
ATOM   2654 C CA  . TYR C 1 38  ? 35.960  27.578 16.998 1.00 13.70 ? 55  TYR C CA  1 
ATOM   2655 C C   . TYR C 1 38  ? 36.704  28.153 18.197 1.00 15.38 ? 55  TYR C C   1 
ATOM   2656 O O   . TYR C 1 38  ? 36.130  28.357 19.280 1.00 16.11 ? 55  TYR C O   1 
ATOM   2657 C CB  . TYR C 1 38  ? 35.259  28.696 16.233 1.00 15.92 ? 55  TYR C CB  1 
ATOM   2658 C CG  . TYR C 1 38  ? 34.607  28.295 14.925 1.00 15.42 ? 55  TYR C CG  1 
ATOM   2659 C CD1 . TYR C 1 38  ? 35.116  27.267 14.149 1.00 16.13 ? 55  TYR C CD1 1 
ATOM   2660 C CD2 . TYR C 1 38  ? 33.490  28.948 14.481 1.00 15.64 ? 55  TYR C CD2 1 
ATOM   2661 C CE1 . TYR C 1 38  ? 34.534  26.916 12.966 1.00 15.37 ? 55  TYR C CE1 1 
ATOM   2662 C CE2 . TYR C 1 38  ? 32.892  28.624 13.265 1.00 14.77 ? 55  TYR C CE2 1 
ATOM   2663 C CZ  . TYR C 1 38  ? 33.406  27.599 12.531 1.00 14.74 ? 55  TYR C CZ  1 
ATOM   2664 O OH  . TYR C 1 38  ? 32.794  27.267 11.347 1.00 17.78 ? 55  TYR C OH  1 
ATOM   2665 N N   . ARG C 1 39  ? 37.990  28.412 18.000 1.00 14.61 ? 56  ARG C N   1 
ATOM   2666 C CA  . ARG C 1 39  ? 38.886  28.780 19.082 1.00 14.21 ? 56  ARG C CA  1 
ATOM   2667 C C   . ARG C 1 39  ? 39.088  30.285 19.079 1.00 13.90 ? 56  ARG C C   1 
ATOM   2668 O O   . ARG C 1 39  ? 39.391  30.873 18.033 1.00 15.68 ? 56  ARG C O   1 
ATOM   2669 C CB  . ARG C 1 39  ? 40.224  28.061 18.905 1.00 15.49 ? 56  ARG C CB  1 
ATOM   2670 C CG  . ARG C 1 39  ? 41.200  28.320 20.053 1.00 17.12 ? 56  ARG C CG  1 
ATOM   2671 C CD  . ARG C 1 39  ? 42.531  27.602 19.875 1.00 15.55 ? 56  ARG C CD  1 
ATOM   2672 N NE  . ARG C 1 39  ? 43.320  28.101 18.750 1.00 15.60 ? 56  ARG C NE  1 
ATOM   2673 C CZ  . ARG C 1 39  ? 44.134  29.143 18.817 1.00 15.90 ? 56  ARG C CZ  1 
ATOM   2674 N NH1 . ARG C 1 39  ? 44.242  29.866 19.920 1.00 17.93 ? 56  ARG C NH1 1 
ATOM   2675 N NH2 . ARG C 1 39  ? 44.868  29.464 17.759 1.00 20.21 ? 56  ARG C NH2 1 
ATOM   2676 N N   . ILE C 1 40  ? 38.924  30.909 20.248 1.00 15.09 ? 57  ILE C N   1 
ATOM   2677 C CA  . ILE C 1 40  ? 39.224  32.331 20.386 1.00 13.66 ? 57  ILE C CA  1 
ATOM   2678 C C   . ILE C 1 40  ? 40.739  32.487 20.375 1.00 13.68 ? 57  ILE C C   1 
ATOM   2679 O O   . ILE C 1 40  ? 41.424  32.075 21.317 1.00 15.82 ? 57  ILE C O   1 
ATOM   2680 C CB  . ILE C 1 40  ? 38.630  32.932 21.663 1.00 14.97 ? 57  ILE C CB  1 
ATOM   2681 C CG1 . ILE C 1 40  ? 37.130  32.642 21.793 1.00 16.05 ? 57  ILE C CG1 1 
ATOM   2682 C CG2 . ILE C 1 40  ? 38.858  34.418 21.639 1.00 17.27 ? 57  ILE C CG2 1 
ATOM   2683 C CD1 . ILE C 1 40  ? 36.576  32.966 23.187 1.00 17.43 ? 57  ILE C CD1 1 
ATOM   2684 N N   . ALA C 1 41  ? 41.270  33.071 19.305 1.00 15.36 ? 58  ALA C N   1 
ATOM   2685 C CA  . ALA C 1 41  ? 42.700  33.330 19.194 1.00 15.54 ? 58  ALA C CA  1 
ATOM   2686 C C   . ALA C 1 41  ? 43.075  34.752 19.591 1.00 16.22 ? 58  ALA C C   1 
ATOM   2687 O O   . ALA C 1 41  ? 44.229  34.999 19.943 1.00 18.36 ? 58  ALA C O   1 
ATOM   2688 C CB  . ALA C 1 41  ? 43.188  33.036 17.766 1.00 19.50 ? 58  ALA C CB  1 
ATOM   2689 N N   . ALA C 1 42  ? 42.133  35.687 19.561 1.00 16.99 ? 59  ALA C N   1 
ATOM   2690 C CA  . ALA C 1 42  ? 42.433  37.041 20.005 1.00 15.92 ? 59  ALA C CA  1 
ATOM   2691 C C   . ALA C 1 42  ? 41.118  37.727 20.310 1.00 15.78 ? 59  ALA C C   1 
ATOM   2692 O O   . ALA C 1 42  ? 40.083  37.385 19.729 1.00 16.00 ? 59  ALA C O   1 
ATOM   2693 C CB  . ALA C 1 42  ? 43.204  37.831 18.933 1.00 16.11 ? 59  ALA C CB  1 
ATOM   2694 N N   . MET C 1 43  ? 41.166  38.688 21.232 1.00 16.41 ? 60  MET C N   1 
ATOM   2695 C CA  . MET C 1 43  ? 39.972  39.431 21.609 1.00 16.90 ? 60  MET C CA  1 
ATOM   2696 C C   . MET C 1 43  ? 40.408  40.720 22.292 1.00 16.25 ? 60  MET C C   1 
ATOM   2697 O O   . MET C 1 43  ? 41.300  40.698 23.144 1.00 20.75 ? 60  MET C O   1 
ATOM   2698 C CB  . MET C 1 43  ? 39.087  38.574 22.533 1.00 18.54 ? 60  MET C CB  1 
ATOM   2699 C CG  . MET C 1 43  ? 37.695  39.110 22.761 1.00 19.60 ? 60  MET C CG  1 
ATOM   2700 S SD  . MET C 1 43  ? 36.566  37.887 23.498 1.00 20.42 ? 60  MET C SD  1 
ATOM   2701 C CE  . MET C 1 43  ? 35.984  37.027 22.033 1.00 19.84 ? 60  MET C CE  1 
ATOM   2702 N N   . LYS C 1 44  ? 39.775  41.833 21.920 1.00 16.63 ? 61  LYS C N   1 
ATOM   2703 C CA  . LYS C 1 44  ? 40.125  43.148 22.450 1.00 19.39 ? 61  LYS C CA  1 
ATOM   2704 C C   . LYS C 1 44  ? 38.928  44.077 22.297 1.00 17.52 ? 61  LYS C C   1 
ATOM   2705 O O   . LYS C 1 44  ? 38.390  44.223 21.193 1.00 20.68 ? 61  LYS C O   1 
ATOM   2706 C CB  . LYS C 1 44  ? 41.324  43.717 21.658 1.00 22.25 ? 61  LYS C CB  1 
ATOM   2707 C CG  . LYS C 1 44  ? 41.654  45.169 21.902 1.00 30.33 ? 61  LYS C CG  1 
ATOM   2708 C CD  . LYS C 1 44  ? 43.051  45.485 21.361 1.00 31.19 ? 61  LYS C CD  1 
ATOM   2709 C CE  . LYS C 1 44  ? 43.121  45.322 19.868 1.00 27.42 ? 61  LYS C CE  1 
ATOM   2710 N NZ  . LYS C 1 44  ? 44.497  45.640 19.352 1.00 26.66 ? 61  LYS C NZ  1 
ATOM   2711 N N   . LEU C 1 45  ? 38.532  44.732 23.387 1.00 17.57 ? 62  LEU C N   1 
ATOM   2712 C CA  . LEU C 1 45  ? 37.592  45.837 23.308 1.00 16.95 ? 62  LEU C CA  1 
ATOM   2713 C C   . LEU C 1 45  ? 38.361  47.127 23.054 1.00 18.19 ? 62  LEU C C   1 
ATOM   2714 O O   . LEU C 1 45  ? 39.358  47.414 23.732 1.00 19.09 ? 62  LEU C O   1 
ATOM   2715 C CB  . LEU C 1 45  ? 36.805  45.959 24.609 1.00 18.18 ? 62  LEU C CB  1 
ATOM   2716 C CG  . LEU C 1 45  ? 35.662  46.975 24.538 1.00 18.57 ? 62  LEU C CG  1 
ATOM   2717 C CD1 . LEU C 1 45  ? 34.418  46.395 23.854 1.00 21.41 ? 62  LEU C CD1 1 
ATOM   2718 C CD2 . LEU C 1 45  ? 35.321  47.494 25.900 1.00 23.76 ? 62  LEU C CD2 1 
ATOM   2719 N N   . THR C 1 46  ? 37.915  47.910 22.075 1.00 18.87 ? 63  THR C N   1 
ATOM   2720 C CA  . THR C 1 46  ? 38.518  49.204 21.814 1.00 19.71 ? 63  THR C CA  1 
ATOM   2721 C C   . THR C 1 46  ? 37.414  50.144 21.376 1.00 17.16 ? 63  THR C C   1 
ATOM   2722 O O   . THR C 1 46  ? 36.261  49.741 21.212 1.00 19.38 ? 63  THR C O   1 
ATOM   2723 C CB  . THR C 1 46  ? 39.657  49.112 20.783 1.00 22.06 ? 63  THR C CB  1 
ATOM   2724 O OG1 . THR C 1 46  ? 40.374  50.344 20.747 1.00 21.87 ? 63  THR C OG1 1 
ATOM   2725 C CG2 . THR C 1 46  ? 39.131  48.803 19.393 1.00 21.10 ? 63  THR C CG2 1 
ATOM   2726 N N   . ILE C 1 47  ? 37.751  51.418 21.230 1.00 19.01 ? 64  ILE C N   1 
ATOM   2727 C CA  . ILE C 1 47  ? 36.871  52.380 20.574 1.00 19.33 ? 64  ILE C CA  1 
ATOM   2728 C C   . ILE C 1 47  ? 37.474  52.674 19.213 1.00 19.23 ? 64  ILE C C   1 
ATOM   2729 O O   . ILE C 1 47  ? 38.593  53.184 19.120 1.00 21.82 ? 64  ILE C O   1 
ATOM   2730 C CB  . ILE C 1 47  ? 36.666  53.649 21.410 1.00 20.36 ? 64  ILE C CB  1 
ATOM   2731 C CG1 . ILE C 1 47  ? 35.880  53.299 22.684 1.00 23.10 ? 64  ILE C CG1 1 
ATOM   2732 C CG2 . ILE C 1 47  ? 35.903  54.682 20.613 1.00 21.02 ? 64  ILE C CG2 1 
ATOM   2733 C CD1 . ILE C 1 47  ? 35.784  54.421 23.697 1.00 29.92 ? 64  ILE C CD1 1 
ATOM   2734 N N   . ALA C 1 48  ? 36.756  52.304 18.159 1.00 19.03 ? 65  ALA C N   1 
ATOM   2735 C CA  . ALA C 1 48  ? 37.275  52.478 16.809 1.00 20.58 ? 65  ALA C CA  1 
ATOM   2736 C C   . ALA C 1 48  ? 37.390  53.955 16.475 1.00 22.92 ? 65  ALA C C   1 
ATOM   2737 O O   . ALA C 1 48  ? 36.513  54.754 16.813 1.00 27.47 ? 65  ALA C O   1 
ATOM   2738 C CB  . ALA C 1 48  ? 36.353  51.795 15.806 1.00 23.62 ? 65  ALA C CB  1 
ATOM   2739 N N   . THR C 1 49  ? 38.471  54.310 15.789 1.00 24.25 ? 66  THR C N   1 
ATOM   2740 C CA  . THR C 1 49  ? 38.741  55.670 15.380 1.00 27.39 ? 66  THR C CA  1 
ATOM   2741 C C   . THR C 1 49  ? 38.541  55.825 13.877 1.00 24.42 ? 66  THR C C   1 
ATOM   2742 O O   . THR C 1 49  ? 38.667  54.859 13.123 1.00 24.47 ? 66  THR C O   1 
ATOM   2743 C CB  . THR C 1 49  ? 40.197  56.022 15.703 1.00 28.93 ? 66  THR C CB  1 
ATOM   2744 O OG1 . THR C 1 49  ? 41.070  55.136 14.986 1.00 29.17 ? 66  THR C OG1 1 
ATOM   2745 C CG2 . THR C 1 49  ? 40.443  55.898 17.206 1.00 32.22 ? 66  THR C CG2 1 
ATOM   2746 N N   . PRO C 1 50  ? 38.238  57.031 13.409 1.00 29.30 ? 67  PRO C N   1 
ATOM   2747 C CA  . PRO C 1 50  ? 38.145  57.228 11.955 1.00 28.50 ? 67  PRO C CA  1 
ATOM   2748 C C   . PRO C 1 50  ? 39.398  56.789 11.217 1.00 29.30 ? 67  PRO C C   1 
ATOM   2749 O O   . PRO C 1 50  ? 39.291  56.245 10.116 1.00 28.68 ? 67  PRO C O   1 
ATOM   2750 C CB  . PRO C 1 50  ? 37.904  58.739 11.828 1.00 28.49 ? 67  PRO C CB  1 
ATOM   2751 C CG  . PRO C 1 50  ? 37.199  59.096 13.084 1.00 32.13 ? 67  PRO C CG  1 
ATOM   2752 C CD  . PRO C 1 50  ? 37.775  58.212 14.159 1.00 30.52 ? 67  PRO C CD  1 
ATOM   2753 N N   . ALA C 1 51  ? 40.585  56.994 11.798 1.00 29.48 ? 68  ALA C N   1 
ATOM   2754 C CA  . ALA C 1 51  ? 41.817  56.657 11.089 1.00 28.53 ? 68  ALA C CA  1 
ATOM   2755 C C   . ALA C 1 51  ? 41.929  55.161 10.833 1.00 25.75 ? 68  ALA C C   1 
ATOM   2756 O O   . ALA C 1 51  ? 42.323  54.738 9.739  1.00 30.04 ? 68  ALA C O   1 
ATOM   2757 C CB  . ALA C 1 51  ? 43.031  57.139 11.881 1.00 32.14 ? 68  ALA C CB  1 
ATOM   2758 N N   . ILE C 1 52  ? 41.616  54.338 11.834 1.00 25.26 ? 69  ILE C N   1 
ATOM   2759 C CA  . ILE C 1 52  ? 41.674  52.899 11.614 1.00 23.75 ? 69  ILE C CA  1 
ATOM   2760 C C   . ILE C 1 52  ? 40.522  52.450 10.724 1.00 20.68 ? 69  ILE C C   1 
ATOM   2761 O O   . ILE C 1 52  ? 40.668  51.540 9.905  1.00 20.82 ? 69  ILE C O   1 
ATOM   2762 C CB  . ILE C 1 52  ? 41.746  52.117 12.938 1.00 25.57 ? 69  ILE C CB  1 
ATOM   2763 C CG1 . ILE C 1 52  ? 42.117  50.665 12.646 1.00 31.89 ? 69  ILE C CG1 1 
ATOM   2764 C CG2 . ILE C 1 52  ? 40.423  52.183 13.676 1.00 26.70 ? 69  ILE C CG2 1 
ATOM   2765 C CD1 . ILE C 1 52  ? 42.703  49.943 13.830 1.00 37.24 ? 69  ILE C CD1 1 
ATOM   2766 N N   . LEU C 1 53  ? 39.359  53.086 10.869 1.00 20.47 ? 70  LEU C N   1 
ATOM   2767 C CA  . LEU C 1 53  ? 38.202  52.694 10.058 1.00 19.77 ? 70  LEU C CA  1 
ATOM   2768 C C   . LEU C 1 53  ? 38.410  53.025 8.582  1.00 21.10 ? 70  LEU C C   1 
ATOM   2769 O O   . LEU C 1 53  ? 37.941  52.284 7.713  1.00 21.25 ? 70  LEU C O   1 
ATOM   2770 C CB  . LEU C 1 53  ? 36.944  53.365 10.606 1.00 20.10 ? 70  LEU C CB  1 
ATOM   2771 C CG  . LEU C 1 53  ? 36.482  52.824 11.970 1.00 19.42 ? 70  LEU C CG  1 
ATOM   2772 C CD1 . LEU C 1 53  ? 35.487  53.788 12.570 1.00 19.86 ? 70  LEU C CD1 1 
ATOM   2773 C CD2 . LEU C 1 53  ? 35.915  51.382 11.877 1.00 21.41 ? 70  LEU C CD2 1 
ATOM   2774 N N   . GLU C 1 54  ? 39.123  54.113 8.284  1.00 22.40 ? 71  GLU C N   1 
ATOM   2775 C CA  . GLU C 1 54  ? 39.429  54.439 6.898  1.00 25.16 ? 71  GLU C CA  1 
ATOM   2776 C C   . GLU C 1 54  ? 40.250  53.333 6.259  1.00 24.12 ? 71  GLU C C   1 
ATOM   2777 O O   . GLU C 1 54  ? 40.069  53.019 5.077  1.00 25.26 ? 71  GLU C O   1 
ATOM   2778 C CB  . GLU C 1 54  ? 40.189  55.765 6.820  1.00 32.09 ? 71  GLU C CB  1 
ATOM   2779 C CG  . GLU C 1 54  ? 39.335  56.994 6.951  1.00 42.08 ? 71  GLU C CG  1 
ATOM   2780 C CD  . GLU C 1 54  ? 40.144  58.273 6.768  1.00 48.91 ? 71  GLU C CD  1 
ATOM   2781 O OE1 . GLU C 1 54  ? 41.271  58.190 6.228  1.00 47.84 ? 71  GLU C OE1 1 
ATOM   2782 O OE2 . GLU C 1 54  ? 39.654  59.356 7.162  1.00 55.23 ? 71  GLU C OE2 1 
ATOM   2783 N N   . GLU C 1 55  ? 41.197  52.764 7.014  1.00 22.46 ? 72  GLU C N   1 
ATOM   2784 C CA  A GLU C 1 55  ? 41.992  51.672 6.471  0.56 22.18 ? 72  GLU C CA  1 
ATOM   2785 C CA  B GLU C 1 55  ? 42.009  51.660 6.509  0.44 22.39 ? 72  GLU C CA  1 
ATOM   2786 C C   . GLU C 1 55  ? 41.196  50.374 6.434  1.00 21.62 ? 72  GLU C C   1 
ATOM   2787 O O   . GLU C 1 55  ? 41.315  49.601 5.479  1.00 22.64 ? 72  GLU C O   1 
ATOM   2788 C CB  A GLU C 1 55  ? 43.288  51.505 7.265  0.56 26.15 ? 72  GLU C CB  1 
ATOM   2789 C CB  B GLU C 1 55  ? 43.215  51.445 7.431  0.44 25.80 ? 72  GLU C CB  1 
ATOM   2790 C CG  A GLU C 1 55  ? 44.304  50.635 6.544  0.56 29.78 ? 72  GLU C CG  1 
ATOM   2791 C CG  B GLU C 1 55  ? 44.043  52.693 7.722  0.44 29.79 ? 72  GLU C CG  1 
ATOM   2792 C CD  A GLU C 1 55  ? 45.695  50.690 7.159  0.56 30.95 ? 72  GLU C CD  1 
ATOM   2793 C CD  B GLU C 1 55  ? 45.108  52.457 8.785  0.44 32.64 ? 72  GLU C CD  1 
ATOM   2794 O OE1 A GLU C 1 55  ? 45.959  51.590 7.980  0.56 32.85 ? 72  GLU C OE1 1 
ATOM   2795 O OE1 B GLU C 1 55  ? 45.968  51.574 8.576  0.44 33.52 ? 72  GLU C OE1 1 
ATOM   2796 O OE2 A GLU C 1 55  ? 46.527  49.828 6.814  0.56 31.00 ? 72  GLU C OE2 1 
ATOM   2797 O OE2 B GLU C 1 55  ? 45.075  53.143 9.837  0.44 31.72 ? 72  GLU C OE2 1 
ATOM   2798 N N   . HIS C 1 56  ? 40.372  50.127 7.452  1.00 19.59 ? 73  HIS C N   1 
ATOM   2799 C CA  . HIS C 1 56  ? 39.524  48.938 7.460  1.00 19.90 ? 73  HIS C CA  1 
ATOM   2800 C C   . HIS C 1 56  ? 38.618  48.922 6.237  1.00 20.76 ? 73  HIS C C   1 
ATOM   2801 O O   . HIS C 1 56  ? 38.442  47.886 5.584  1.00 21.37 ? 73  HIS C O   1 
ATOM   2802 C CB  . HIS C 1 56  ? 38.668  48.958 8.731  1.00 18.23 ? 73  HIS C CB  1 
ATOM   2803 C CG  . HIS C 1 56  ? 37.740  47.797 8.861  1.00 20.82 ? 73  HIS C CG  1 
ATOM   2804 N ND1 . HIS C 1 56  ? 38.170  46.532 9.200  1.00 20.89 ? 73  HIS C ND1 1 
ATOM   2805 C CD2 . HIS C 1 56  ? 36.394  47.711 8.714  1.00 22.88 ? 73  HIS C CD2 1 
ATOM   2806 C CE1 . HIS C 1 56  ? 37.133  45.715 9.252  1.00 21.67 ? 73  HIS C CE1 1 
ATOM   2807 N NE2 . HIS C 1 56  ? 36.042  46.405 8.955  1.00 23.23 ? 73  HIS C NE2 1 
ATOM   2808 N N   . TYR C 1 57  ? 38.044  50.076 5.914  1.00 19.13 ? 74  TYR C N   1 
ATOM   2809 C CA  . TYR C 1 57  ? 37.149  50.236 4.776  1.00 20.42 ? 74  TYR C CA  1 
ATOM   2810 C C   . TYR C 1 57  ? 37.857  50.825 3.556  1.00 22.18 ? 74  TYR C C   1 
ATOM   2811 O O   . TYR C 1 57  ? 37.230  51.551 2.783  1.00 23.71 ? 74  TYR C O   1 
ATOM   2812 C CB  . TYR C 1 57  ? 35.973  51.120 5.177  1.00 22.88 ? 74  TYR C CB  1 
ATOM   2813 C CG  . TYR C 1 57  ? 35.012  50.476 6.141  1.00 22.01 ? 74  TYR C CG  1 
ATOM   2814 C CD1 . TYR C 1 57  ? 34.401  49.270 5.843  1.00 22.62 ? 74  TYR C CD1 1 
ATOM   2815 C CD2 . TYR C 1 57  ? 34.683  51.093 7.332  1.00 24.09 ? 74  TYR C CD2 1 
ATOM   2816 C CE1 . TYR C 1 57  ? 33.502  48.688 6.713  1.00 26.10 ? 74  TYR C CE1 1 
ATOM   2817 C CE2 . TYR C 1 57  ? 33.791  50.526 8.202  1.00 26.96 ? 74  TYR C CE2 1 
ATOM   2818 C CZ  . TYR C 1 57  ? 33.201  49.327 7.890  1.00 26.13 ? 74  TYR C CZ  1 
ATOM   2819 O OH  . TYR C 1 57  ? 32.310  48.781 8.778  1.00 31.25 ? 74  TYR C OH  1 
ATOM   2820 N N   . ALA C 1 58  ? 39.154  50.536 3.384  1.00 21.95 ? 75  ALA C N   1 
ATOM   2821 C CA  . ALA C 1 58  ? 39.913  51.094 2.269  1.00 23.27 ? 75  ALA C CA  1 
ATOM   2822 C C   . ALA C 1 58  ? 39.266  50.794 0.926  1.00 26.62 ? 75  ALA C C   1 
ATOM   2823 O O   . ALA C 1 58  ? 39.399  51.585 -0.021 1.00 28.84 ? 75  ALA C O   1 
ATOM   2824 C CB  . ALA C 1 58  ? 41.328  50.504 2.264  1.00 26.20 ? 75  ALA C CB  1 
ATOM   2825 N N   . GLU C 1 59  ? 38.591  49.649 0.809  1.00 27.07 ? 76  GLU C N   1 
ATOM   2826 C CA  . GLU C 1 59  ? 37.965  49.288 -0.462 1.00 31.33 ? 76  GLU C CA  1 
ATOM   2827 C C   . GLU C 1 59  ? 36.925  50.312 -0.891 1.00 33.27 ? 76  GLU C C   1 
ATOM   2828 O O   . GLU C 1 59  ? 36.643  50.443 -2.086 1.00 38.73 ? 76  GLU C O   1 
ATOM   2829 C CB  . GLU C 1 59  ? 37.308  47.909 -0.357 1.00 36.55 ? 76  GLU C CB  1 
ATOM   2830 C CG  . GLU C 1 59  ? 36.209  47.824 0.696  1.00 42.31 ? 76  GLU C CG  1 
ATOM   2831 C CD  . GLU C 1 59  ? 35.779  46.392 0.990  1.00 47.35 ? 76  GLU C CD  1 
ATOM   2832 O OE1 . GLU C 1 59  ? 35.214  45.741 0.083  1.00 45.59 ? 76  GLU C OE1 1 
ATOM   2833 O OE2 . GLU C 1 59  ? 36.019  45.916 2.122  1.00 51.09 ? 76  GLU C OE2 1 
ATOM   2834 N N   . HIS C 1 60  ? 36.341  51.039 0.063  1.00 30.86 ? 77  HIS C N   1 
ATOM   2835 C CA  . HIS C 1 60  ? 35.268  51.985 -0.206 1.00 31.00 ? 77  HIS C CA  1 
ATOM   2836 C C   . HIS C 1 60  ? 35.751  53.426 -0.304 1.00 32.97 ? 77  HIS C C   1 
ATOM   2837 O O   . HIS C 1 60  ? 34.924  54.341 -0.328 1.00 33.06 ? 77  HIS C O   1 
ATOM   2838 C CB  . HIS C 1 60  ? 34.193  51.903 0.879  1.00 31.50 ? 77  HIS C CB  1 
ATOM   2839 C CG  . HIS C 1 60  ? 33.594  50.546 1.034  1.00 30.88 ? 77  HIS C CG  1 
ATOM   2840 N ND1 . HIS C 1 60  ? 33.133  49.807 -0.035 1.00 33.01 ? 77  HIS C ND1 1 
ATOM   2841 C CD2 . HIS C 1 60  ? 33.372  49.793 2.137  1.00 31.46 ? 77  HIS C CD2 1 
ATOM   2842 C CE1 . HIS C 1 60  ? 32.654  48.658 0.405  1.00 34.94 ? 77  HIS C CE1 1 
ATOM   2843 N NE2 . HIS C 1 60  ? 32.791  48.622 1.718  1.00 35.94 ? 77  HIS C NE2 1 
ATOM   2844 N N   . LYS C 1 61  ? 37.055  53.655 -0.345 1.00 34.96 ? 78  LYS C N   1 
ATOM   2845 C CA  . LYS C 1 61  ? 37.560  55.016 -0.440 1.00 39.97 ? 78  LYS C CA  1 
ATOM   2846 C C   . LYS C 1 61  ? 36.878  55.763 -1.581 1.00 42.56 ? 78  LYS C C   1 
ATOM   2847 O O   . LYS C 1 61  ? 36.739  55.245 -2.694 1.00 44.05 ? 78  LYS C O   1 
ATOM   2848 C CB  . LYS C 1 61  ? 39.070  54.992 -0.681 1.00 46.71 ? 78  LYS C CB  1 
ATOM   2849 C CG  . LYS C 1 61  ? 39.728  56.353 -0.533 1.00 52.99 ? 78  LYS C CG  1 
ATOM   2850 C CD  . LYS C 1 61  ? 41.178  56.322 -0.992 1.00 58.23 ? 78  LYS C CD  1 
ATOM   2851 C CE  . LYS C 1 61  ? 41.919  57.594 -0.602 1.00 62.73 ? 78  LYS C CE  1 
ATOM   2852 N NZ  . LYS C 1 61  ? 43.316  57.605 -1.129 1.00 63.98 ? 78  LYS C NZ  1 
ATOM   2853 N N   . GLY C 1 62  ? 36.447  56.987 -1.294 1.00 42.48 ? 79  GLY C N   1 
ATOM   2854 C CA  . GLY C 1 62  ? 35.835  57.822 -2.299 1.00 41.14 ? 79  GLY C CA  1 
ATOM   2855 C C   . GLY C 1 62  ? 34.375  57.541 -2.576 1.00 41.63 ? 79  GLY C C   1 
ATOM   2856 O O   . GLY C 1 62  ? 33.794  58.202 -3.441 1.00 44.99 ? 79  GLY C O   1 
ATOM   2857 N N   . LYS C 1 63  ? 33.748  56.563 -1.870 1.00 38.11 ? 80  LYS C N   1 
ATOM   2858 C CA  . LYS C 1 63  ? 32.342  56.319 -2.158 1.00 38.46 ? 80  LYS C CA  1 
ATOM   2859 C C   . LYS C 1 63  ? 31.462  57.218 -1.296 1.00 34.28 ? 80  LYS C C   1 
ATOM   2860 O O   . LYS C 1 63  ? 31.838  57.577 -0.175 1.00 31.57 ? 80  LYS C O   1 
ATOM   2861 C CB  . LYS C 1 63  ? 31.987  54.859 -1.891 1.00 41.96 ? 80  LYS C CB  1 
ATOM   2862 C CG  . LYS C 1 63  ? 32.706  53.878 -2.811 1.00 46.89 ? 80  LYS C CG  1 
ATOM   2863 C CD  . LYS C 1 63  ? 32.369  52.429 -2.482 1.00 51.02 ? 80  LYS C CD  1 
ATOM   2864 C CE  . LYS C 1 63  ? 33.149  51.454 -3.364 1.00 53.57 ? 80  LYS C CE  1 
ATOM   2865 N NZ  . LYS C 1 63  ? 32.879  50.031 -3.004 1.00 53.19 ? 80  LYS C NZ  1 
ATOM   2866 N N   . PRO C 1 64  ? 30.286  57.597 -1.803 1.00 34.40 ? 81  PRO C N   1 
ATOM   2867 C CA  . PRO C 1 64  ? 29.433  58.532 -1.053 1.00 32.02 ? 81  PRO C CA  1 
ATOM   2868 C C   . PRO C 1 64  ? 28.978  58.023 0.310  1.00 33.17 ? 81  PRO C C   1 
ATOM   2869 O O   . PRO C 1 64  ? 28.725  58.841 1.202  1.00 35.37 ? 81  PRO C O   1 
ATOM   2870 C CB  . PRO C 1 64  ? 28.245  58.777 -2.001 1.00 32.62 ? 81  PRO C CB  1 
ATOM   2871 C CG  . PRO C 1 64  ? 28.293  57.661 -2.997 1.00 34.88 ? 81  PRO C CG  1 
ATOM   2872 C CD  . PRO C 1 64  ? 29.722  57.263 -3.124 1.00 35.44 ? 81  PRO C CD  1 
ATOM   2873 N N   . PHE C 1 65  ? 28.844  56.709 0.500  1.00 32.89 ? 82  PHE C N   1 
ATOM   2874 C CA  . PHE C 1 65  ? 28.366  56.191 1.777  1.00 33.34 ? 82  PHE C CA  1 
ATOM   2875 C C   . PHE C 1 65  ? 29.468  56.027 2.812  1.00 31.36 ? 82  PHE C C   1 
ATOM   2876 O O   . PHE C 1 65  ? 29.159  55.716 3.966  1.00 35.80 ? 82  PHE C O   1 
ATOM   2877 C CB  . PHE C 1 65  ? 27.678  54.837 1.588  1.00 35.80 ? 82  PHE C CB  1 
ATOM   2878 C CG  . PHE C 1 65  ? 28.571  53.786 0.997  1.00 37.58 ? 82  PHE C CG  1 
ATOM   2879 C CD1 . PHE C 1 65  ? 29.459  53.073 1.795  1.00 39.20 ? 82  PHE C CD1 1 
ATOM   2880 C CD2 . PHE C 1 65  ? 28.536  53.522 -0.358 1.00 39.59 ? 82  PHE C CD2 1 
ATOM   2881 C CE1 . PHE C 1 65  ? 30.282  52.114 1.250  1.00 36.70 ? 82  PHE C CE1 1 
ATOM   2882 C CE2 . PHE C 1 65  ? 29.360  52.563 -0.909 1.00 38.64 ? 82  PHE C CE2 1 
ATOM   2883 C CZ  . PHE C 1 65  ? 30.234  51.856 -0.098 1.00 36.86 ? 82  PHE C CZ  1 
ATOM   2884 N N   . LEU C 1 66  ? 30.733  56.210 2.442  1.00 30.89 ? 83  LEU C N   1 
ATOM   2885 C CA  . LEU C 1 66  ? 31.800  55.936 3.401  1.00 28.44 ? 83  LEU C CA  1 
ATOM   2886 C C   . LEU C 1 66  ? 31.735  56.834 4.625  1.00 30.53 ? 83  LEU C C   1 
ATOM   2887 O O   . LEU C 1 66  ? 31.862  56.315 5.748  1.00 32.88 ? 83  LEU C O   1 
ATOM   2888 C CB  . LEU C 1 66  ? 33.169  55.993 2.722  1.00 27.16 ? 83  LEU C CB  1 
ATOM   2889 C CG  . LEU C 1 66  ? 34.373  55.677 3.630  1.00 27.28 ? 83  LEU C CG  1 
ATOM   2890 C CD1 . LEU C 1 66  ? 34.217  54.320 4.296  1.00 27.03 ? 83  LEU C CD1 1 
ATOM   2891 C CD2 . LEU C 1 66  ? 35.659  55.750 2.833  1.00 30.77 ? 83  LEU C CD2 1 
ATOM   2892 N N   . PRO C 1 67  ? 31.562  58.155 4.504  1.00 33.64 ? 84  PRO C N   1 
ATOM   2893 C CA  . PRO C 1 67  ? 31.559  58.980 5.723  1.00 38.73 ? 84  PRO C CA  1 
ATOM   2894 C C   . PRO C 1 67  ? 30.524  58.551 6.742  1.00 39.14 ? 84  PRO C C   1 
ATOM   2895 O O   . PRO C 1 67  ? 30.829  58.507 7.942  1.00 41.58 ? 84  PRO C O   1 
ATOM   2896 C CB  . PRO C 1 67  ? 31.288  60.389 5.186  1.00 38.21 ? 84  PRO C CB  1 
ATOM   2897 C CG  . PRO C 1 67  ? 31.810  60.359 3.794  1.00 35.37 ? 84  PRO C CG  1 
ATOM   2898 C CD  . PRO C 1 67  ? 31.505  58.984 3.283  1.00 33.41 ? 84  PRO C CD  1 
ATOM   2899 N N   . GLY C 1 68  ? 29.310  58.209 6.301  1.00 40.92 ? 85  GLY C N   1 
ATOM   2900 C CA  . GLY C 1 68  ? 28.294  57.769 7.242  1.00 39.97 ? 85  GLY C CA  1 
ATOM   2901 C C   . GLY C 1 68  ? 28.589  56.405 7.824  1.00 38.93 ? 85  GLY C C   1 
ATOM   2902 O O   . GLY C 1 68  ? 28.257  56.129 8.982  1.00 41.58 ? 85  GLY C O   1 
ATOM   2903 N N   . LEU C 1 69  ? 29.214  55.534 7.034  1.00 35.64 ? 86  LEU C N   1 
ATOM   2904 C CA  . LEU C 1 69  ? 29.636  54.236 7.542  1.00 34.13 ? 86  LEU C CA  1 
ATOM   2905 C C   . LEU C 1 69  ? 30.684  54.387 8.640  1.00 31.21 ? 86  LEU C C   1 
ATOM   2906 O O   . LEU C 1 69  ? 30.620  53.708 9.673  1.00 32.02 ? 86  LEU C O   1 
ATOM   2907 C CB  . LEU C 1 69  ? 30.186  53.433 6.373  1.00 37.16 ? 86  LEU C CB  1 
ATOM   2908 C CG  . LEU C 1 69  ? 30.847  52.105 6.677  1.00 37.87 ? 86  LEU C CG  1 
ATOM   2909 C CD1 . LEU C 1 69  ? 29.908  51.234 7.503  1.00 41.27 ? 86  LEU C CD1 1 
ATOM   2910 C CD2 . LEU C 1 69  ? 31.212  51.461 5.356  1.00 39.29 ? 86  LEU C CD2 1 
ATOM   2911 N N   . ILE C 1 70  ? 31.656  55.278 8.436  1.00 29.57 ? 87  ILE C N   1 
ATOM   2912 C CA  A ILE C 1 70  ? 32.668  55.509 9.465  0.73 30.51 ? 87  ILE C CA  1 
ATOM   2913 C CA  B ILE C 1 70  ? 32.669  55.518 9.462  0.27 30.31 ? 87  ILE C CA  1 
ATOM   2914 C C   . ILE C 1 70  ? 32.021  56.070 10.725 1.00 32.51 ? 87  ILE C C   1 
ATOM   2915 O O   . ILE C 1 70  ? 32.354  55.657 11.844 1.00 32.00 ? 87  ILE C O   1 
ATOM   2916 C CB  A ILE C 1 70  ? 33.791  56.411 8.916  0.73 28.73 ? 87  ILE C CB  1 
ATOM   2917 C CB  B ILE C 1 70  ? 33.763  56.456 8.919  0.27 28.42 ? 87  ILE C CB  1 
ATOM   2918 C CG1 A ILE C 1 70  ? 34.655  55.638 7.912  0.73 27.21 ? 87  ILE C CG1 1 
ATOM   2919 C CG1 B ILE C 1 70  ? 34.431  55.855 7.678  0.27 25.51 ? 87  ILE C CG1 1 
ATOM   2920 C CG2 A ILE C 1 70  ? 34.657  56.961 10.046 0.73 29.22 ? 87  ILE C CG2 1 
ATOM   2921 C CG2 B ILE C 1 70  ? 34.805  56.747 9.990  0.27 29.06 ? 87  ILE C CG2 1 
ATOM   2922 C CD1 A ILE C 1 70  ? 35.588  56.513 7.087  0.73 27.45 ? 87  ILE C CD1 1 
ATOM   2923 C CD1 B ILE C 1 70  ? 35.263  54.620 7.950  0.27 22.88 ? 87  ILE C CD1 1 
ATOM   2924 N N   . GLU C 1 71  ? 31.077  57.008 10.567 1.00 36.20 ? 88  GLU C N   1 
ATOM   2925 C CA  . GLU C 1 71  ? 30.412  57.604 11.726 1.00 41.45 ? 88  GLU C CA  1 
ATOM   2926 C C   . GLU C 1 71  ? 29.676  56.553 12.552 1.00 39.33 ? 88  GLU C C   1 
ATOM   2927 O O   . GLU C 1 71  ? 29.806  56.513 13.778 1.00 42.29 ? 88  GLU C O   1 
ATOM   2928 C CB  . GLU C 1 71  ? 29.442  58.696 11.272 1.00 51.53 ? 88  GLU C CB  1 
ATOM   2929 C CG  . GLU C 1 71  ? 30.091  60.059 11.041 1.00 61.63 ? 88  GLU C CG  1 
ATOM   2930 C CD  . GLU C 1 71  ? 29.086  61.135 10.636 1.00 68.49 ? 88  GLU C CD  1 
ATOM   2931 O OE1 . GLU C 1 71  ? 28.084  61.321 11.361 1.00 71.34 ? 88  GLU C OE1 1 
ATOM   2932 O OE2 . GLU C 1 71  ? 29.293  61.788 9.583  1.00 70.16 ? 88  GLU C OE2 1 
ATOM   2933 N N   . LYS C 1 72  ? 28.905  55.680 11.893 1.00 37.08 ? 89  LYS C N   1 
ATOM   2934 C CA  . LYS C 1 72  ? 28.212  54.606 12.602 1.00 36.97 ? 89  LYS C CA  1 
ATOM   2935 C C   . LYS C 1 72  ? 29.180  53.703 13.364 1.00 32.00 ? 89  LYS C C   1 
ATOM   2936 O O   . LYS C 1 72  ? 28.825  53.161 14.425 1.00 33.58 ? 89  LYS C O   1 
ATOM   2937 C CB  . LYS C 1 72  ? 27.409  53.766 11.603 1.00 43.10 ? 89  LYS C CB  1 
ATOM   2938 C CG  . LYS C 1 72  ? 25.913  54.068 11.584 1.00 47.18 ? 89  LYS C CG  1 
ATOM   2939 C CD  . LYS C 1 72  ? 25.263  53.682 10.264 1.00 49.82 ? 89  LYS C CD  1 
ATOM   2940 C CE  . LYS C 1 72  ? 23.757  53.998 10.257 1.00 50.30 ? 89  LYS C CE  1 
ATOM   2941 N NZ  . LYS C 1 72  ? 23.438  55.366 10.781 1.00 49.18 ? 89  LYS C NZ  1 
ATOM   2942 N N   . MET C 1 73  ? 30.394  53.518 12.839 1.00 29.60 ? 90  MET C N   1 
ATOM   2943 C CA  . MET C 1 73  ? 31.361  52.597 13.412 1.00 25.19 ? 90  MET C CA  1 
ATOM   2944 C C   . MET C 1 73  ? 32.287  53.243 14.429 1.00 23.87 ? 90  MET C C   1 
ATOM   2945 O O   . MET C 1 73  ? 33.080  52.528 15.064 1.00 23.28 ? 90  MET C O   1 
ATOM   2946 C CB  . MET C 1 73  ? 32.206  51.986 12.293 1.00 24.92 ? 90  MET C CB  1 
ATOM   2947 C CG  . MET C 1 73  ? 31.466  50.933 11.508 1.00 26.30 ? 90  MET C CG  1 
ATOM   2948 S SD  . MET C 1 73  ? 31.053  49.480 12.512 1.00 28.84 ? 90  MET C SD  1 
ATOM   2949 C CE  . MET C 1 73  ? 32.669  48.962 13.078 1.00 26.45 ? 90  MET C CE  1 
ATOM   2950 N N   . THR C 1 74  ? 32.222  54.558 14.594 1.00 25.85 ? 91  THR C N   1 
ATOM   2951 C CA  . THR C 1 74  ? 33.070  55.255 15.562 1.00 25.15 ? 91  THR C CA  1 
ATOM   2952 C C   . THR C 1 74  ? 32.419  55.106 16.931 1.00 26.06 ? 91  THR C C   1 
ATOM   2953 O O   . THR C 1 74  ? 31.563  55.884 17.335 1.00 33.74 ? 91  THR C O   1 
ATOM   2954 C CB  . THR C 1 74  ? 33.264  56.707 15.157 1.00 31.91 ? 91  THR C CB  1 
ATOM   2955 O OG1 . THR C 1 74  ? 33.879  56.745 13.866 1.00 33.18 ? 91  THR C OG1 1 
ATOM   2956 C CG2 . THR C 1 74  ? 34.162  57.425 16.149 1.00 34.08 ? 91  THR C CG2 1 
ATOM   2957 N N   . GLY C 1 75  ? 32.834  54.077 17.649 1.00 20.33 ? 92  GLY C N   1 
ATOM   2958 C CA  . GLY C 1 75  ? 32.249  53.729 18.922 1.00 20.20 ? 92  GLY C CA  1 
ATOM   2959 C C   . GLY C 1 75  ? 32.931  52.478 19.434 1.00 17.40 ? 92  GLY C C   1 
ATOM   2960 O O   . GLY C 1 75  ? 33.889  51.986 18.828 1.00 17.92 ? 92  GLY C O   1 
ATOM   2961 N N   . PRO C 1 76  ? 32.452  51.932 20.552 1.00 17.89 ? 93  PRO C N   1 
ATOM   2962 C CA  . PRO C 1 76  ? 33.036  50.690 21.071 1.00 17.19 ? 93  PRO C CA  1 
ATOM   2963 C C   . PRO C 1 76  ? 32.810  49.533 20.108 1.00 15.75 ? 93  PRO C C   1 
ATOM   2964 O O   . PRO C 1 76  ? 31.726  49.374 19.543 1.00 16.14 ? 93  PRO C O   1 
ATOM   2965 C CB  . PRO C 1 76  ? 32.282  50.476 22.399 1.00 18.27 ? 93  PRO C CB  1 
ATOM   2966 C CG  . PRO C 1 76  ? 30.986  51.153 22.195 1.00 20.63 ? 93  PRO C CG  1 
ATOM   2967 C CD  . PRO C 1 76  ? 31.293  52.371 21.351 1.00 18.83 ? 93  PRO C CD  1 
ATOM   2968 N N   . VAL C 1 77  ? 33.850  48.713 19.950 1.00 16.19 ? 94  VAL C N   1 
ATOM   2969 C CA  . VAL C 1 77  ? 33.805  47.498 19.142 1.00 15.61 ? 94  VAL C CA  1 
ATOM   2970 C C   . VAL C 1 77  ? 34.589  46.417 19.866 1.00 14.25 ? 94  VAL C C   1 
ATOM   2971 O O   . VAL C 1 77  ? 35.524  46.700 20.619 1.00 16.55 ? 94  VAL C O   1 
ATOM   2972 C CB  . VAL C 1 77  ? 34.376  47.705 17.718 1.00 16.60 ? 94  VAL C CB  1 
ATOM   2973 C CG1 . VAL C 1 77  ? 33.548  48.747 16.974 1.00 18.47 ? 94  VAL C CG1 1 
ATOM   2974 C CG2 . VAL C 1 77  ? 35.860  48.092 17.776 1.00 19.31 ? 94  VAL C CG2 1 
ATOM   2975 N N   . LEU C 1 78  ? 34.203  45.163 19.636 1.00 15.14 ? 95  LEU C N   1 
ATOM   2976 C CA  . LEU C 1 78  ? 34.975  44.018 20.121 1.00 15.60 ? 95  LEU C CA  1 
ATOM   2977 C C   . LEU C 1 78  ? 35.679  43.381 18.929 1.00 16.20 ? 95  LEU C C   1 
ATOM   2978 O O   . LEU C 1 78  ? 35.027  42.792 18.057 1.00 16.79 ? 95  LEU C O   1 
ATOM   2979 C CB  . LEU C 1 78  ? 34.113  42.992 20.857 1.00 16.68 ? 95  LEU C CB  1 
ATOM   2980 C CG  . LEU C 1 78  ? 34.974  41.986 21.630 1.00 16.28 ? 95  LEU C CG  1 
ATOM   2981 C CD1 . LEU C 1 78  ? 35.644  42.645 22.831 1.00 19.71 ? 95  LEU C CD1 1 
ATOM   2982 C CD2 . LEU C 1 78  ? 34.140  40.782 22.105 1.00 16.93 ? 95  LEU C CD2 1 
ATOM   2983 N N   . CYS C 1 79  ? 37.001  43.518 18.894 1.00 14.52 ? 96  CYS C N   1 
ATOM   2984 C CA  . CYS C 1 79  ? 37.825  42.871 17.878 1.00 16.13 ? 96  CYS C CA  1 
ATOM   2985 C C   . CYS C 1 79  ? 38.045  41.420 18.289 1.00 13.86 ? 96  CYS C C   1 
ATOM   2986 O O   . CYS C 1 79  ? 38.341  41.137 19.450 1.00 17.09 ? 96  CYS C O   1 
ATOM   2987 C CB  . CYS C 1 79  ? 39.186  43.570 17.787 1.00 17.78 ? 96  CYS C CB  1 
ATOM   2988 S SG  . CYS C 1 79  ? 39.107  45.381 17.679 1.00 18.67 ? 96  CYS C SG  1 
ATOM   2989 N N   . MET C 1 80  ? 37.927  40.499 17.335 1.00 16.04 ? 97  MET C N   1 
ATOM   2990 C CA  . MET C 1 80  ? 38.062  39.079 17.630 1.00 15.84 ? 97  MET C CA  1 
ATOM   2991 C C   . MET C 1 80  ? 38.761  38.364 16.483 1.00 15.43 ? 97  MET C C   1 
ATOM   2992 O O   . MET C 1 80  ? 38.608  38.728 15.311 1.00 17.39 ? 97  MET C O   1 
ATOM   2993 C CB  . MET C 1 80  ? 36.690  38.397 17.861 1.00 16.43 ? 97  MET C CB  1 
ATOM   2994 C CG  . MET C 1 80  ? 35.716  39.205 18.716 1.00 17.07 ? 97  MET C CG  1 
ATOM   2995 S SD  . MET C 1 80  ? 34.147  38.387 19.080 1.00 17.37 ? 97  MET C SD  1 
ATOM   2996 C CE  . MET C 1 80  ? 33.392  38.372 17.449 1.00 17.06 ? 97  MET C CE  1 
ATOM   2997 N N   . VAL C 1 81  ? 39.500  37.316 16.835 1.00 14.88 ? 98  VAL C N   1 
ATOM   2998 C CA  . VAL C 1 81  ? 40.017  36.347 15.868 1.00 16.30 ? 98  VAL C CA  1 
ATOM   2999 C C   . VAL C 1 81  ? 39.530  34.977 16.305 1.00 15.65 ? 98  VAL C C   1 
ATOM   3000 O O   . VAL C 1 81  ? 39.754  34.577 17.453 1.00 15.69 ? 98  VAL C O   1 
ATOM   3001 C CB  . VAL C 1 81  ? 41.542  36.371 15.750 1.00 16.73 ? 98  VAL C CB  1 
ATOM   3002 C CG1 . VAL C 1 81  ? 42.015  35.291 14.753 1.00 17.97 ? 98  VAL C CG1 1 
ATOM   3003 C CG2 . VAL C 1 81  ? 42.045  37.751 15.334 1.00 17.97 ? 98  VAL C CG2 1 
ATOM   3004 N N   . PHE C 1 82  ? 38.853  34.267 15.409 1.00 14.76 ? 99  PHE C N   1 
ATOM   3005 C CA  . PHE C 1 82  ? 38.437  32.892 15.642 1.00 13.51 ? 99  PHE C CA  1 
ATOM   3006 C C   . PHE C 1 82  ? 39.139  31.973 14.653 1.00 16.00 ? 99  PHE C C   1 
ATOM   3007 O O   . PHE C 1 82  ? 39.376  32.346 13.497 1.00 17.10 ? 99  PHE C O   1 
ATOM   3008 C CB  . PHE C 1 82  ? 36.919  32.707 15.490 1.00 15.69 ? 99  PHE C CB  1 
ATOM   3009 C CG  . PHE C 1 82  ? 36.145  33.064 16.725 1.00 14.46 ? 99  PHE C CG  1 
ATOM   3010 C CD1 . PHE C 1 82  ? 35.698  34.355 16.941 1.00 16.28 ? 99  PHE C CD1 1 
ATOM   3011 C CD2 . PHE C 1 82  ? 35.925  32.112 17.692 1.00 15.82 ? 99  PHE C CD2 1 
ATOM   3012 C CE1 . PHE C 1 82  ? 34.993  34.665 18.100 1.00 18.46 ? 99  PHE C CE1 1 
ATOM   3013 C CE2 . PHE C 1 82  ? 35.231  32.407 18.840 1.00 17.65 ? 99  PHE C CE2 1 
ATOM   3014 C CZ  . PHE C 1 82  ? 34.782  33.688 19.054 1.00 17.32 ? 99  PHE C CZ  1 
ATOM   3015 N N   . GLU C 1 83  ? 39.458  30.767 15.120 1.00 15.90 ? 100 GLU C N   1 
ATOM   3016 C CA  . GLU C 1 83  ? 40.162  29.764 14.337 1.00 15.45 ? 100 GLU C CA  1 
ATOM   3017 C C   . GLU C 1 83  ? 39.309  28.515 14.167 1.00 16.04 ? 100 GLU C C   1 
ATOM   3018 O O   . GLU C 1 83  ? 38.689  28.036 15.121 1.00 18.06 ? 100 GLU C O   1 
ATOM   3019 C CB  . GLU C 1 83  ? 41.457  29.384 15.048 1.00 15.06 ? 100 GLU C CB  1 
ATOM   3020 C CG  . GLU C 1 83  ? 42.240  28.265 14.373 1.00 17.45 ? 100 GLU C CG  1 
ATOM   3021 C CD  . GLU C 1 83  ? 43.467  27.940 15.168 1.00 20.24 ? 100 GLU C CD  1 
ATOM   3022 O OE1 . GLU C 1 83  ? 43.378  27.072 16.069 1.00 19.76 ? 100 GLU C OE1 1 
ATOM   3023 O OE2 . GLU C 1 83  ? 44.498  28.593 14.916 1.00 22.00 ? 100 GLU C OE2 1 
ATOM   3024 N N   . GLY C 1 84  ? 39.311  27.966 12.957 1.00 17.02 ? 101 GLY C N   1 
ATOM   3025 C CA  . GLY C 1 84  ? 38.613  26.721 12.706 1.00 15.98 ? 101 GLY C CA  1 
ATOM   3026 C C   . GLY C 1 84  ? 38.755  26.323 11.253 1.00 16.49 ? 101 GLY C C   1 
ATOM   3027 O O   . GLY C 1 84  ? 39.330  27.045 10.438 1.00 17.96 ? 101 GLY C O   1 
ATOM   3028 N N   . VAL C 1 85  ? 38.224  25.146 10.938 1.00 15.67 ? 102 VAL C N   1 
ATOM   3029 C CA  . VAL C 1 85  ? 38.254  24.676 9.554  1.00 18.18 ? 102 VAL C CA  1 
ATOM   3030 C C   . VAL C 1 85  ? 37.339  25.566 8.728  1.00 17.02 ? 102 VAL C C   1 
ATOM   3031 O O   . VAL C 1 85  ? 36.168  25.761 9.072  1.00 18.19 ? 102 VAL C O   1 
ATOM   3032 C CB  . VAL C 1 85  ? 37.813  23.206 9.490  1.00 18.41 ? 102 VAL C CB  1 
ATOM   3033 C CG1 . VAL C 1 85  ? 37.657  22.732 8.052  1.00 20.52 ? 102 VAL C CG1 1 
ATOM   3034 C CG2 . VAL C 1 85  ? 38.791  22.322 10.225 1.00 19.62 ? 102 VAL C CG2 1 
ATOM   3035 N N   . ASP C 1 86  ? 37.871  26.133 7.638  1.00 16.99 ? 103 ASP C N   1 
ATOM   3036 C CA  . ASP C 1 86  ? 37.049  26.927 6.722  1.00 16.88 ? 103 ASP C CA  1 
ATOM   3037 C C   . ASP C 1 86  ? 36.354  28.083 7.447  1.00 14.71 ? 103 ASP C C   1 
ATOM   3038 O O   . ASP C 1 86  ? 35.290  28.539 7.032  1.00 16.80 ? 103 ASP C O   1 
ATOM   3039 C CB  . ASP C 1 86  ? 36.015  26.014 6.031  1.00 16.62 ? 103 ASP C CB  1 
ATOM   3040 C CG  . ASP C 1 86  ? 35.357  26.640 4.806  1.00 19.80 ? 103 ASP C CG  1 
ATOM   3041 O OD1 . ASP C 1 86  ? 36.026  27.377 4.036  1.00 20.01 ? 103 ASP C OD1 1 
ATOM   3042 O OD2 . ASP C 1 86  ? 34.158  26.327 4.583  1.00 21.43 ? 103 ASP C OD2 1 
ATOM   3043 N N   . VAL C 1 87  ? 36.960  28.603 8.518  1.00 15.26 ? 104 VAL C N   1 
ATOM   3044 C CA  . VAL C 1 87  ? 36.208  29.508 9.395  1.00 15.45 ? 104 VAL C CA  1 
ATOM   3045 C C   . VAL C 1 87  ? 35.890  30.835 8.721  1.00 16.06 ? 104 VAL C C   1 
ATOM   3046 O O   . VAL C 1 87  ? 34.919  31.498 9.092  1.00 16.59 ? 104 VAL C O   1 
ATOM   3047 C CB  . VAL C 1 87  ? 36.925  29.695 10.749 1.00 16.22 ? 104 VAL C CB  1 
ATOM   3048 C CG1 . VAL C 1 87  ? 38.224  30.495 10.593 1.00 17.16 ? 104 VAL C CG1 1 
ATOM   3049 C CG2 . VAL C 1 87  ? 35.993  30.356 11.779 1.00 15.90 ? 104 VAL C CG2 1 
ATOM   3050 N N   . ILE C 1 88  ? 36.679  31.260 7.731  1.00 16.73 ? 105 ILE C N   1 
ATOM   3051 C CA  . ILE C 1 88  ? 36.379  32.528 7.069  1.00 16.00 ? 105 ILE C CA  1 
ATOM   3052 C C   . ILE C 1 88  ? 35.023  32.456 6.369  1.00 15.96 ? 105 ILE C C   1 
ATOM   3053 O O   . ILE C 1 88  ? 34.118  33.257 6.632  1.00 15.53 ? 105 ILE C O   1 
ATOM   3054 C CB  . ILE C 1 88  ? 37.503  32.916 6.091  1.00 17.41 ? 105 ILE C CB  1 
ATOM   3055 C CG1 . ILE C 1 88  ? 38.827  33.127 6.838  1.00 17.09 ? 105 ILE C CG1 1 
ATOM   3056 C CG2 . ILE C 1 88  ? 37.110  34.186 5.318  1.00 18.83 ? 105 ILE C CG2 1 
ATOM   3057 C CD1 . ILE C 1 88  ? 40.043  33.182 5.910  1.00 18.58 ? 105 ILE C CD1 1 
ATOM   3058 N N   . ALA C 1 89  ? 34.869  31.474 5.477  1.00 15.71 ? 106 ALA C N   1 
ATOM   3059 C CA  . ALA C 1 89  ? 33.597  31.295 4.783  1.00 16.06 ? 106 ALA C CA  1 
ATOM   3060 C C   . ALA C 1 89  ? 32.488  30.903 5.749  1.00 15.49 ? 106 ALA C C   1 
ATOM   3061 O O   . ALA C 1 89  ? 31.345  31.328 5.592  1.00 16.79 ? 106 ALA C O   1 
ATOM   3062 C CB  . ALA C 1 89  ? 33.747  30.238 3.685  1.00 18.36 ? 106 ALA C CB  1 
ATOM   3063 N N   . GLN C 1 90  ? 32.799  30.085 6.752  1.00 15.56 ? 107 GLN C N   1 
ATOM   3064 C CA  . GLN C 1 90  ? 31.745  29.601 7.630  1.00 14.93 ? 107 GLN C CA  1 
ATOM   3065 C C   . GLN C 1 90  ? 31.224  30.718 8.514  1.00 15.65 ? 107 GLN C C   1 
ATOM   3066 O O   . GLN C 1 90  ? 30.021  30.818 8.740  1.00 16.44 ? 107 GLN C O   1 
ATOM   3067 C CB  . GLN C 1 90  ? 32.247  28.419 8.447  1.00 15.68 ? 107 GLN C CB  1 
ATOM   3068 C CG  . GLN C 1 90  ? 32.440  27.153 7.624  1.00 17.47 ? 107 GLN C CG  1 
ATOM   3069 C CD  . GLN C 1 90  ? 31.133  26.613 7.066  1.00 18.25 ? 107 GLN C CD  1 
ATOM   3070 O OE1 . GLN C 1 90  ? 30.177  26.397 7.807  1.00 17.47 ? 107 GLN C OE1 1 
ATOM   3071 N NE2 . GLN C 1 90  ? 31.088  26.378 5.758  1.00 20.68 ? 107 GLN C NE2 1 
ATOM   3072 N N   . ALA C 1 91  ? 32.112  31.579 9.013  1.00 16.08 ? 108 ALA C N   1 
ATOM   3073 C CA  . ALA C 1 91  ? 31.641  32.710 9.810  1.00 16.94 ? 108 ALA C CA  1 
ATOM   3074 C C   . ALA C 1 91  ? 30.766  33.634 8.972  1.00 16.57 ? 108 ALA C C   1 
ATOM   3075 O O   . ALA C 1 91  ? 29.758  34.148 9.458  1.00 17.01 ? 108 ALA C O   1 
ATOM   3076 C CB  . ALA C 1 91  ? 32.817  33.476 10.410 1.00 16.79 ? 108 ALA C CB  1 
ATOM   3077 N N   . ARG C 1 92  ? 31.121  33.837 7.697  1.00 17.28 ? 109 ARG C N   1 
ATOM   3078 C CA  . ARG C 1 92  ? 30.264  34.637 6.827  1.00 17.30 ? 109 ARG C CA  1 
ATOM   3079 C C   . ARG C 1 92  ? 28.885  34.016 6.679  1.00 17.73 ? 109 ARG C C   1 
ATOM   3080 O O   . ARG C 1 92  ? 27.875  34.728 6.665  1.00 18.55 ? 109 ARG C O   1 
ATOM   3081 C CB  . ARG C 1 92  ? 30.902  34.779 5.447  1.00 20.96 ? 109 ARG C CB  1 
ATOM   3082 C CG  . ARG C 1 92  ? 32.183  35.557 5.451  1.00 21.97 ? 109 ARG C CG  1 
ATOM   3083 C CD  . ARG C 1 92  ? 31.934  37.039 5.636  1.00 28.63 ? 109 ARG C CD  1 
ATOM   3084 N NE  . ARG C 1 92  ? 31.385  37.626 4.420  1.00 34.89 ? 109 ARG C NE  1 
ATOM   3085 C CZ  . ARG C 1 92  ? 31.222  38.927 4.220  1.00 41.97 ? 109 ARG C CZ  1 
ATOM   3086 N NH1 . ARG C 1 92  ? 31.570  39.817 5.136  1.00 44.12 ? 109 ARG C NH1 1 
ATOM   3087 N NH2 . ARG C 1 92  ? 30.710  39.344 3.067  1.00 42.95 ? 109 ARG C NH2 1 
ATOM   3088 N N   . LYS C 1 93  ? 28.830  32.693 6.524  1.00 16.75 ? 110 LYS C N   1 
ATOM   3089 C CA  . LYS C 1 93  ? 27.554  32.001 6.430  1.00 16.61 ? 110 LYS C CA  1 
ATOM   3090 C C   . LYS C 1 93  ? 26.748  32.158 7.718  1.00 16.04 ? 110 LYS C C   1 
ATOM   3091 O O   . LYS C 1 93  ? 25.518  32.331 7.685  1.00 17.04 ? 110 LYS C O   1 
ATOM   3092 C CB  . LYS C 1 93  ? 27.825  30.535 6.143  1.00 18.55 ? 110 LYS C CB  1 
ATOM   3093 C CG  . LYS C 1 93  ? 26.611  29.695 5.901  1.00 22.28 ? 110 LYS C CG  1 
ATOM   3094 C CD  . LYS C 1 93  ? 27.065  28.308 5.481  1.00 23.87 ? 110 LYS C CD  1 
ATOM   3095 C CE  . LYS C 1 93  ? 25.924  27.345 5.451  1.00 25.46 ? 110 LYS C CE  1 
ATOM   3096 N NZ  . LYS C 1 93  ? 26.378  26.052 4.928  1.00 25.43 ? 110 LYS C NZ  1 
ATOM   3097 N N   . MET C 1 94  ? 27.421  32.089 8.868  1.00 15.15 ? 111 MET C N   1 
ATOM   3098 C CA  . MET C 1 94  ? 26.728  32.230 10.146 1.00 16.07 ? 111 MET C CA  1 
ATOM   3099 C C   . MET C 1 94  ? 26.233  33.647 10.369 1.00 14.50 ? 111 MET C C   1 
ATOM   3100 O O   . MET C 1 94  ? 25.206  33.842 11.034 1.00 15.58 ? 111 MET C O   1 
ATOM   3101 C CB  . MET C 1 94  ? 27.681  31.850 11.264 1.00 14.94 ? 111 MET C CB  1 
ATOM   3102 C CG  . MET C 1 94  ? 28.097  30.400 11.209 1.00 15.88 ? 111 MET C CG  1 
ATOM   3103 S SD  . MET C 1 94  ? 29.491  30.031 12.296 1.00 16.56 ? 111 MET C SD  1 
ATOM   3104 C CE  . MET C 1 94  ? 28.766  30.173 13.929 1.00 20.77 ? 111 MET C CE  1 
ATOM   3105 N N   . MET C 1 95  ? 26.967  34.646 9.860  1.00 14.98 ? 112 MET C N   1 
ATOM   3106 C CA  A MET C 1 95  ? 26.519  36.028 9.977  0.55 16.30 ? 112 MET C CA  1 
ATOM   3107 C CA  B MET C 1 95  ? 26.514  36.026 9.985  0.45 16.29 ? 112 MET C CA  1 
ATOM   3108 C C   . MET C 1 95  ? 25.277  36.277 9.137  1.00 16.34 ? 112 MET C C   1 
ATOM   3109 O O   . MET C 1 95  ? 24.386  37.029 9.548  1.00 16.51 ? 112 MET C O   1 
ATOM   3110 C CB  A MET C 1 95  ? 27.628  36.966 9.495  0.55 16.46 ? 112 MET C CB  1 
ATOM   3111 C CB  B MET C 1 95  ? 27.628  36.980 9.550  0.45 17.11 ? 112 MET C CB  1 
ATOM   3112 C CG  A MET C 1 95  ? 28.834  37.070 10.412 0.55 19.36 ? 112 MET C CG  1 
ATOM   3113 C CG  B MET C 1 95  ? 28.792  37.073 10.519 0.45 18.54 ? 112 MET C CG  1 
ATOM   3114 S SD  A MET C 1 95  ? 30.215  37.890 9.588  0.55 20.95 ? 112 MET C SD  1 
ATOM   3115 S SD  B MET C 1 95  ? 30.028  38.322 10.089 0.45 19.68 ? 112 MET C SD  1 
ATOM   3116 C CE  A MET C 1 95  ? 29.398  39.121 8.602  0.55 26.09 ? 112 MET C CE  1 
ATOM   3117 C CE  B MET C 1 95  ? 29.542  38.854 8.465  0.45 25.45 ? 112 MET C CE  1 
ATOM   3118 N N   . GLY C 1 96  ? 25.231  35.683 7.943  1.00 16.30 ? 113 GLY C N   1 
ATOM   3119 C CA  . GLY C 1 96  ? 24.172  35.921 6.992  1.00 16.75 ? 113 GLY C CA  1 
ATOM   3120 C C   . GLY C 1 96  ? 24.430  37.142 6.132  1.00 16.06 ? 113 GLY C C   1 
ATOM   3121 O O   . GLY C 1 96  ? 25.367  37.912 6.341  1.00 18.07 ? 113 GLY C O   1 
ATOM   3122 N N   . SER C 1 97  ? 23.538  37.316 5.159  1.00 17.39 ? 114 SER C N   1 
ATOM   3123 C CA  . SER C 1 97  ? 23.591  38.426 4.213  1.00 18.49 ? 114 SER C CA  1 
ATOM   3124 C C   . SER C 1 97  ? 23.745  39.765 4.916  1.00 18.48 ? 114 SER C C   1 
ATOM   3125 O O   . SER C 1 97  ? 23.186  39.984 5.993  1.00 17.26 ? 114 SER C O   1 
ATOM   3126 C CB  . SER C 1 97  ? 22.271  38.465 3.435  1.00 22.38 ? 114 SER C CB  1 
ATOM   3127 O OG  . SER C 1 97  ? 22.055  37.245 2.755  1.00 27.86 ? 114 SER C OG  1 
ATOM   3128 N N   . THR C 1 98  ? 24.448  40.692 4.247  1.00 18.77 ? 115 THR C N   1 
ATOM   3129 C CA  . THR C 1 98  ? 24.642  42.045 4.768  1.00 19.20 ? 115 THR C CA  1 
ATOM   3130 C C   . THR C 1 98  ? 23.321  42.698 5.139  1.00 17.80 ? 115 THR C C   1 
ATOM   3131 O O   . THR C 1 98  ? 23.224  43.375 6.168  1.00 19.39 ? 115 THR C O   1 
ATOM   3132 C CB  . THR C 1 98  ? 25.357  42.912 3.726  1.00 23.48 ? 115 THR C CB  1 
ATOM   3133 O OG1 . THR C 1 98  ? 26.549  42.247 3.281  1.00 32.37 ? 115 THR C OG1 1 
ATOM   3134 C CG2 . THR C 1 98  ? 25.748  44.245 4.321  1.00 23.72 ? 115 THR C CG2 1 
ATOM   3135 N N   . ARG C 1 99  ? 22.295  42.512 4.308  1.00 17.24 ? 116 ARG C N   1 
ATOM   3136 C CA  . ARG C 1 99  ? 20.968  43.038 4.576  1.00 17.66 ? 116 ARG C CA  1 
ATOM   3137 C C   . ARG C 1 99  ? 20.223  42.009 5.418  1.00 16.50 ? 116 ARG C C   1 
ATOM   3138 O O   . ARG C 1 99  ? 19.945  40.906 4.911  1.00 16.84 ? 116 ARG C O   1 
ATOM   3139 C CB  . ARG C 1 99  ? 20.219  43.264 3.264  1.00 19.95 ? 116 ARG C CB  1 
ATOM   3140 C CG  . ARG C 1 99  ? 20.816  44.384 2.412  1.00 26.77 ? 116 ARG C CG  1 
ATOM   3141 C CD  . ARG C 1 99  ? 20.027  44.626 1.129  1.00 34.24 ? 116 ARG C CD  1 
ATOM   3142 N NE  . ARG C 1 99  ? 20.464  45.857 0.473  1.00 50.52 ? 116 ARG C NE  1 
ATOM   3143 C CZ  . ARG C 1 99  ? 19.817  46.470 -0.511 1.00 65.40 ? 116 ARG C CZ  1 
ATOM   3144 N NH1 . ARG C 1 99  ? 18.696  45.978 -1.020 1.00 71.08 ? 116 ARG C NH1 1 
ATOM   3145 N NH2 . ARG C 1 99  ? 20.310  47.605 -1.006 1.00 69.72 ? 116 ARG C NH2 1 
ATOM   3146 N N   . PRO C 1 100 ? 19.896  42.306 6.673  1.00 17.10 ? 117 PRO C N   1 
ATOM   3147 C CA  . PRO C 1 100 ? 19.243  41.282 7.499  1.00 15.22 ? 117 PRO C CA  1 
ATOM   3148 C C   . PRO C 1 100 ? 17.968  40.741 6.897  1.00 15.88 ? 117 PRO C C   1 
ATOM   3149 O O   . PRO C 1 100 ? 17.643  39.573 7.117  1.00 16.43 ? 117 PRO C O   1 
ATOM   3150 C CB  . PRO C 1 100 ? 18.975  42.025 8.818  1.00 15.50 ? 117 PRO C CB  1 
ATOM   3151 C CG  . PRO C 1 100 ? 20.080  43.034 8.888  1.00 15.99 ? 117 PRO C CG  1 
ATOM   3152 C CD  . PRO C 1 100 ? 20.257  43.496 7.464  1.00 16.67 ? 117 PRO C CD  1 
ATOM   3153 N N   . GLY C 1 101 ? 17.217  41.549 6.148  1.00 18.00 ? 118 GLY C N   1 
ATOM   3154 C CA  . GLY C 1 101 ? 15.988  41.055 5.564  1.00 19.21 ? 118 GLY C CA  1 
ATOM   3155 C C   . GLY C 1 101 ? 16.201  39.977 4.523  1.00 17.23 ? 118 GLY C C   1 
ATOM   3156 O O   . GLY C 1 101 ? 15.276  39.214 4.241  1.00 18.22 ? 118 GLY C O   1 
ATOM   3157 N N   . GLU C 1 102 ? 17.409  39.897 3.957  1.00 15.78 ? 119 GLU C N   1 
ATOM   3158 C CA  . GLU C 1 102 ? 17.765  38.869 2.986  1.00 17.26 ? 119 GLU C CA  1 
ATOM   3159 C C   . GLU C 1 102 ? 18.505  37.693 3.606  1.00 17.05 ? 119 GLU C C   1 
ATOM   3160 O O   . GLU C 1 102 ? 18.717  36.687 2.932  1.00 18.78 ? 119 GLU C O   1 
ATOM   3161 C CB  . GLU C 1 102 ? 18.633  39.474 1.872  1.00 19.33 ? 119 GLU C CB  1 
ATOM   3162 C CG  . GLU C 1 102 ? 17.912  40.569 1.075  1.00 20.49 ? 119 GLU C CG  1 
ATOM   3163 C CD  . GLU C 1 102 ? 18.785  41.286 0.056  1.00 25.94 ? 119 GLU C CD  1 
ATOM   3164 O OE1 . GLU C 1 102 ? 20.026  41.144 0.082  1.00 26.86 ? 119 GLU C OE1 1 
ATOM   3165 O OE2 . GLU C 1 102 ? 18.217  42.009 -0.779 1.00 30.83 ? 119 GLU C OE2 1 
ATOM   3166 N N   . ALA C 1 103 ? 18.897  37.796 4.868  1.00 16.49 ? 120 ALA C N   1 
ATOM   3167 C CA  . ALA C 1 103 ? 19.668  36.758 5.524  1.00 16.66 ? 120 ALA C CA  1 
ATOM   3168 C C   . ALA C 1 103 ? 18.778  35.581 5.896  1.00 19.85 ? 120 ALA C C   1 
ATOM   3169 O O   . ALA C 1 103 ? 17.579  35.736 6.125  1.00 19.18 ? 120 ALA C O   1 
ATOM   3170 C CB  . ALA C 1 103 ? 20.295  37.339 6.782  1.00 16.97 ? 120 ALA C CB  1 
ATOM   3171 N N   . ALA C 1 104 ? 19.390  34.390 5.962  1.00 19.08 ? 121 ALA C N   1 
ATOM   3172 C CA  . ALA C 1 104 ? 18.656  33.159 6.209  1.00 23.03 ? 121 ALA C CA  1 
ATOM   3173 C C   . ALA C 1 104 ? 18.273  33.054 7.686  1.00 21.32 ? 121 ALA C C   1 
ATOM   3174 O O   . ALA C 1 104 ? 19.053  33.424 8.563  1.00 18.61 ? 121 ALA C O   1 
ATOM   3175 C CB  . ALA C 1 104 ? 19.521  31.956 5.824  1.00 25.20 ? 121 ALA C CB  1 
ATOM   3176 N N   . PRO C 1 105 ? 17.099  32.516 8.008  1.00 24.82 ? 122 PRO C N   1 
ATOM   3177 C CA  . PRO C 1 105 ? 16.790  32.289 9.420  1.00 21.95 ? 122 PRO C CA  1 
ATOM   3178 C C   . PRO C 1 105 ? 17.874  31.432 10.049 1.00 20.31 ? 122 PRO C C   1 
ATOM   3179 O O   . PRO C 1 105 ? 18.409  30.509 9.426  1.00 21.95 ? 122 PRO C O   1 
ATOM   3180 C CB  . PRO C 1 105 ? 15.439  31.561 9.372  1.00 27.02 ? 122 PRO C CB  1 
ATOM   3181 C CG  . PRO C 1 105 ? 14.814  32.056 8.133  1.00 30.22 ? 122 PRO C CG  1 
ATOM   3182 C CD  . PRO C 1 105 ? 15.941  32.213 7.143  1.00 30.33 ? 122 PRO C CD  1 
ATOM   3183 N N   . GLY C 1 106 ? 18.199  31.743 11.293 1.00 18.64 ? 123 GLY C N   1 
ATOM   3184 C CA  . GLY C 1 106 ? 19.271  31.083 11.990 1.00 18.66 ? 123 GLY C CA  1 
ATOM   3185 C C   . GLY C 1 106 ? 20.617  31.755 11.874 1.00 15.79 ? 123 GLY C C   1 
ATOM   3186 O O   . GLY C 1 106 ? 21.555  31.343 12.564 1.00 19.97 ? 123 GLY C O   1 
ATOM   3187 N N   . THR C 1 107 ? 20.756  32.759 11.016 1.00 15.14 ? 124 THR C N   1 
ATOM   3188 C CA  . THR C 1 107 ? 21.971  33.551 10.964 1.00 16.06 ? 124 THR C CA  1 
ATOM   3189 C C   . THR C 1 107 ? 21.884  34.708 11.952 1.00 13.36 ? 124 THR C C   1 
ATOM   3190 O O   . THR C 1 107 ? 20.802  35.085 12.405 1.00 14.77 ? 124 THR C O   1 
ATOM   3191 C CB  . THR C 1 107 ? 22.230  34.086 9.553  1.00 15.10 ? 124 THR C CB  1 
ATOM   3192 O OG1 . THR C 1 107 ? 21.198  35.011 9.167  1.00 15.92 ? 124 THR C OG1 1 
ATOM   3193 C CG2 . THR C 1 107 ? 22.303  32.936 8.548  1.00 17.64 ? 124 THR C CG2 1 
ATOM   3194 N N   . ILE C 1 108 ? 23.047  35.260 12.290 1.00 14.72 ? 125 ILE C N   1 
ATOM   3195 C CA  . ILE C 1 108 ? 23.090  36.349 13.258 1.00 14.88 ? 125 ILE C CA  1 
ATOM   3196 C C   . ILE C 1 108 ? 22.266  37.530 12.761 1.00 14.33 ? 125 ILE C C   1 
ATOM   3197 O O   . ILE C 1 108 ? 21.456  38.097 13.493 1.00 14.83 ? 125 ILE C O   1 
ATOM   3198 C CB  . ILE C 1 108 ? 24.548  36.747 13.561 1.00 14.83 ? 125 ILE C CB  1 
ATOM   3199 C CG1 . ILE C 1 108 ? 25.278  35.610 14.284 1.00 16.63 ? 125 ILE C CG1 1 
ATOM   3200 C CG2 . ILE C 1 108 ? 24.581  38.035 14.384 1.00 17.51 ? 125 ILE C CG2 1 
ATOM   3201 C CD1 . ILE C 1 108 ? 26.788  35.822 14.413 1.00 18.03 ? 125 ILE C CD1 1 
ATOM   3202 N N   . ARG C 1 109 ? 22.480  37.936 11.512 1.00 14.48 ? 126 ARG C N   1 
ATOM   3203 C CA  . ARG C 1 109 ? 21.792  39.135 11.046 1.00 15.98 ? 126 ARG C CA  1 
ATOM   3204 C C   . ARG C 1 109 ? 20.287  38.930 10.971 1.00 14.32 ? 126 ARG C C   1 
ATOM   3205 O O   . ARG C 1 109 ? 19.518  39.829 11.337 1.00 15.40 ? 126 ARG C O   1 
ATOM   3206 C CB  . ARG C 1 109 ? 22.416  39.622 9.742  1.00 17.26 ? 126 ARG C CB  1 
ATOM   3207 C CG  . ARG C 1 109 ? 23.750  40.314 10.059 1.00 21.15 ? 126 ARG C CG  1 
ATOM   3208 C CD  . ARG C 1 109 ? 24.582  40.425 8.889  1.00 23.08 ? 126 ARG C CD  1 
ATOM   3209 N NE  . ARG C 1 109 ? 25.866  41.049 9.163  1.00 19.26 ? 126 ARG C NE  1 
ATOM   3210 C CZ  . ARG C 1 109 ? 26.793  41.123 8.234  1.00 20.45 ? 126 ARG C CZ  1 
ATOM   3211 N NH1 . ARG C 1 109 ? 26.658  40.480 7.083  1.00 23.81 ? 126 ARG C NH1 1 
ATOM   3212 N NH2 . ARG C 1 109 ? 27.867  41.865 8.444  1.00 21.42 ? 126 ARG C NH2 1 
ATOM   3213 N N   . ALA C 1 110 ? 19.846  37.749 10.524 1.00 14.09 ? 127 ALA C N   1 
ATOM   3214 C CA  . ALA C 1 110 ? 18.411  37.482 10.474 1.00 16.88 ? 127 ALA C CA  1 
ATOM   3215 C C   . ALA C 1 110 ? 17.799  37.402 11.866 1.00 14.42 ? 127 ALA C C   1 
ATOM   3216 O O   . ALA C 1 110 ? 16.637  37.784 12.055 1.00 16.54 ? 127 ALA C O   1 
ATOM   3217 C CB  . ALA C 1 110 ? 18.131  36.177 9.727  1.00 16.05 ? 127 ALA C CB  1 
ATOM   3218 N N   . ASP C 1 111 ? 18.544  36.877 12.842 1.00 14.66 ? 128 ASP C N   1 
ATOM   3219 C CA  . ASP C 1 111 ? 17.962  36.638 14.156 1.00 14.04 ? 128 ASP C CA  1 
ATOM   3220 C C   . ASP C 1 111 ? 17.950  37.897 15.012 1.00 13.97 ? 128 ASP C C   1 
ATOM   3221 O O   . ASP C 1 111 ? 17.137  37.987 15.939 1.00 14.22 ? 128 ASP C O   1 
ATOM   3222 C CB  . ASP C 1 111 ? 18.741  35.552 14.901 1.00 16.11 ? 128 ASP C CB  1 
ATOM   3223 C CG  . ASP C 1 111 ? 18.538  34.161 14.318 1.00 20.58 ? 128 ASP C CG  1 
ATOM   3224 O OD1 . ASP C 1 111 ? 17.606  33.952 13.507 1.00 21.43 ? 128 ASP C OD1 1 
ATOM   3225 O OD2 . ASP C 1 111 ? 19.336  33.272 14.683 1.00 19.43 ? 128 ASP C OD2 1 
ATOM   3226 N N   . PHE C 1 112 ? 18.863  38.844 14.744 1.00 14.13 ? 129 PHE C N   1 
ATOM   3227 C CA  . PHE C 1 112 ? 19.059  40.001 15.603 1.00 13.07 ? 129 PHE C CA  1 
ATOM   3228 C C   . PHE C 1 112 ? 18.724  41.351 14.973 1.00 13.52 ? 129 PHE C C   1 
ATOM   3229 O O   . PHE C 1 112 ? 18.534  42.313 15.718 1.00 14.33 ? 129 PHE C O   1 
ATOM   3230 C CB  . PHE C 1 112 ? 20.520  40.117 16.068 1.00 14.49 ? 129 PHE C CB  1 
ATOM   3231 C CG  . PHE C 1 112 ? 20.943  39.119 17.114 1.00 14.08 ? 129 PHE C CG  1 
ATOM   3232 C CD1 . PHE C 1 112 ? 21.501  37.900 16.750 1.00 15.91 ? 129 PHE C CD1 1 
ATOM   3233 C CD2 . PHE C 1 112 ? 20.850  39.428 18.456 1.00 16.54 ? 129 PHE C CD2 1 
ATOM   3234 C CE1 . PHE C 1 112 ? 21.943  37.011 17.696 1.00 17.75 ? 129 PHE C CE1 1 
ATOM   3235 C CE2 . PHE C 1 112 ? 21.287  38.531 19.415 1.00 16.73 ? 129 PHE C CE2 1 
ATOM   3236 C CZ  . PHE C 1 112 ? 21.832  37.317 19.033 1.00 17.78 ? 129 PHE C CZ  1 
ATOM   3237 N N   . CYS C 1 113 ? 18.686  41.476 13.641 1.00 13.61 ? 130 CYS C N   1 
ATOM   3238 C CA  . CYS C 1 113 ? 18.771  42.797 13.029 1.00 15.15 ? 130 CYS C CA  1 
ATOM   3239 C C   . CYS C 1 113 ? 17.662  43.044 12.010 1.00 12.56 ? 130 CYS C C   1 
ATOM   3240 O O   . CYS C 1 113 ? 16.917  42.139 11.617 1.00 13.44 ? 130 CYS C O   1 
ATOM   3241 C CB  . CYS C 1 113 ? 20.151  42.997 12.381 1.00 14.61 ? 130 CYS C CB  1 
ATOM   3242 S SG  . CYS C 1 113 ? 21.484  42.869 13.585 1.00 16.14 ? 130 CYS C SG  1 
ATOM   3243 N N   . GLN C 1 114 ? 17.576  44.304 11.592 1.00 13.54 ? 131 GLN C N   1 
ATOM   3244 C CA  . GLN C 1 114 ? 16.569  44.759 10.633 1.00 14.78 ? 131 GLN C CA  1 
ATOM   3245 C C   . GLN C 1 114 ? 17.159  45.384 9.381  1.00 14.26 ? 131 GLN C C   1 
ATOM   3246 O O   . GLN C 1 114 ? 16.645  45.162 8.278  1.00 17.34 ? 131 GLN C O   1 
ATOM   3247 C CB  . GLN C 1 114 ? 15.646  45.789 11.289 1.00 14.46 ? 131 GLN C CB  1 
ATOM   3248 C CG  . GLN C 1 114 ? 14.790  45.189 12.383 1.00 15.63 ? 131 GLN C CG  1 
ATOM   3249 C CD  . GLN C 1 114 ? 13.786  46.163 12.942 1.00 14.97 ? 131 GLN C CD  1 
ATOM   3250 O OE1 . GLN C 1 114 ? 13.088  46.876 12.206 1.00 15.87 ? 131 GLN C OE1 1 
ATOM   3251 N NE2 . GLN C 1 114 ? 13.708  46.207 14.265 1.00 15.47 ? 131 GLN C NE2 1 
ATOM   3252 N N   . GLN C 1 115 ? 18.227  46.169 9.518  1.00 14.44 ? 132 GLN C N   1 
ATOM   3253 C CA  . GLN C 1 115 ? 18.757  46.950 8.411  1.00 16.36 ? 132 GLN C CA  1 
ATOM   3254 C C   . GLN C 1 115 ? 20.266  46.820 8.308  1.00 15.11 ? 132 GLN C C   1 
ATOM   3255 O O   . GLN C 1 115 ? 20.960  46.614 9.305  1.00 16.48 ? 132 GLN C O   1 
ATOM   3256 C CB  . GLN C 1 115 ? 18.400  48.421 8.576  1.00 16.80 ? 132 GLN C CB  1 
ATOM   3257 C CG  . GLN C 1 115 ? 16.916  48.662 8.528  1.00 19.57 ? 132 GLN C CG  1 
ATOM   3258 C CD  . GLN C 1 115 ? 16.596  50.140 8.488  1.00 19.14 ? 132 GLN C CD  1 
ATOM   3259 O OE1 . GLN C 1 115 ? 16.771  50.845 9.476  1.00 22.07 ? 132 GLN C OE1 1 
ATOM   3260 N NE2 . GLN C 1 115 ? 16.136  50.620 7.337  1.00 23.62 ? 132 GLN C NE2 1 
ATOM   3261 N N   . ALA C 1 116 ? 20.767  46.951 7.073  1.00 18.14 ? 133 ALA C N   1 
ATOM   3262 C CA  . ALA C 1 116 ? 22.190  46.742 6.807  1.00 19.58 ? 133 ALA C CA  1 
ATOM   3263 C C   . ALA C 1 116 ? 23.067  47.715 7.582  1.00 18.45 ? 133 ALA C C   1 
ATOM   3264 O O   . ALA C 1 116 ? 24.190  47.366 7.980  1.00 19.89 ? 133 ALA C O   1 
ATOM   3265 C CB  . ALA C 1 116 ? 22.459  46.882 5.299  1.00 20.69 ? 133 ALA C CB  1 
ATOM   3266 N N   . GLY C 1 117 ? 22.587  48.938 7.796  1.00 18.73 ? 134 GLY C N   1 
ATOM   3267 C CA  . GLY C 1 117 ? 23.384  49.917 8.508  1.00 20.03 ? 134 GLY C CA  1 
ATOM   3268 C C   . GLY C 1 117 ? 23.552  49.628 9.983  1.00 20.36 ? 134 GLY C C   1 
ATOM   3269 O O   . GLY C 1 117 ? 24.388  50.271 10.627 1.00 20.46 ? 134 GLY C O   1 
ATOM   3270 N N   . ARG C 1 118 ? 22.762  48.697 10.539 1.00 17.86 ? 135 ARG C N   1 
ATOM   3271 C CA  . ARG C 1 118 ? 22.931  48.216 11.916 1.00 17.62 ? 135 ARG C CA  1 
ATOM   3272 C C   . ARG C 1 118 ? 22.819  46.697 11.874 1.00 15.97 ? 135 ARG C C   1 
ATOM   3273 O O   . ARG C 1 118 ? 21.816  46.105 12.291 1.00 16.09 ? 135 ARG C O   1 
ATOM   3274 C CB  . ARG C 1 118 ? 21.866  48.843 12.825 1.00 15.95 ? 135 ARG C CB  1 
ATOM   3275 C CG  . ARG C 1 118 ? 22.066  50.341 13.067 1.00 16.62 ? 135 ARG C CG  1 
ATOM   3276 C CD  . ARG C 1 118 ? 23.402  50.602 13.766 1.00 17.87 ? 135 ARG C CD  1 
ATOM   3277 N NE  . ARG C 1 118 ? 23.487  51.960 14.281 1.00 20.16 ? 135 ARG C NE  1 
ATOM   3278 C CZ  . ARG C 1 118 ? 24.567  52.494 14.837 1.00 21.28 ? 135 ARG C CZ  1 
ATOM   3279 N NH1 . ARG C 1 118 ? 25.705  51.822 14.924 1.00 22.72 ? 135 ARG C NH1 1 
ATOM   3280 N NH2 . ARG C 1 118 ? 24.503  53.729 15.322 1.00 23.13 ? 135 ARG C NH2 1 
ATOM   3281 N N   . ASN C 1 119 ? 23.894  46.048 11.439 1.00 14.94 ? 136 ASN C N   1 
ATOM   3282 C CA  . ASN C 1 119 ? 23.883  44.603 11.230 1.00 16.07 ? 136 ASN C CA  1 
ATOM   3283 C C   . ASN C 1 119 ? 24.881  43.868 12.120 1.00 15.60 ? 136 ASN C C   1 
ATOM   3284 O O   . ASN C 1 119 ? 25.301  42.753 11.786 1.00 15.72 ? 136 ASN C O   1 
ATOM   3285 C CB  . ASN C 1 119 ? 24.038  44.258 9.745  1.00 16.55 ? 136 ASN C CB  1 
ATOM   3286 C CG  . ASN C 1 119 ? 25.389  44.632 9.192  1.00 17.10 ? 136 ASN C CG  1 
ATOM   3287 O OD1 . ASN C 1 119 ? 26.260  45.131 9.919  1.00 18.62 ? 136 ASN C OD1 1 
ATOM   3288 N ND2 . ASN C 1 119 ? 25.578  44.403 7.883  1.00 18.57 ? 136 ASN C ND2 1 
ATOM   3289 N N   . LEU C 1 120 ? 25.252  44.488 13.250 1.00 14.78 ? 137 LEU C N   1 
ATOM   3290 C CA  . LEU C 1 120 ? 25.800  43.895 14.469 1.00 13.75 ? 137 LEU C CA  1 
ATOM   3291 C C   . LEU C 1 120 ? 27.238  43.406 14.431 1.00 14.86 ? 137 LEU C C   1 
ATOM   3292 O O   . LEU C 1 120 ? 27.941  43.492 15.450 1.00 15.24 ? 137 LEU C O   1 
ATOM   3293 C CB  . LEU C 1 120 ? 24.967  42.643 14.842 1.00 16.70 ? 137 LEU C CB  1 
ATOM   3294 C CG  . LEU C 1 120 ? 24.677  42.399 16.322 1.00 16.51 ? 137 LEU C CG  1 
ATOM   3295 C CD1 . LEU C 1 120 ? 23.666  43.445 16.820 1.00 15.60 ? 137 LEU C CD1 1 
ATOM   3296 C CD2 . LEU C 1 120 ? 24.160  40.988 16.560 1.00 18.06 ? 137 LEU C CD2 1 
ATOM   3297 N N   . ILE C 1 121 ? 27.749  43.018 13.265 1.00 15.44 ? 138 ILE C N   1 
ATOM   3298 C CA  . ILE C 1 121 ? 28.991  42.258 13.237 1.00 15.22 ? 138 ILE C CA  1 
ATOM   3299 C C   . ILE C 1 121 ? 29.599  42.382 11.861 1.00 14.09 ? 138 ILE C C   1 
ATOM   3300 O O   . ILE C 1 121 ? 28.888  42.504 10.867 1.00 17.67 ? 138 ILE C O   1 
ATOM   3301 C CB  . ILE C 1 121 ? 28.743  40.782 13.651 1.00 15.65 ? 138 ILE C CB  1 
ATOM   3302 C CG1 . ILE C 1 121 ? 30.059  40.016 13.730 1.00 14.94 ? 138 ILE C CG1 1 
ATOM   3303 C CG2 . ILE C 1 121 ? 27.788  40.095 12.695 1.00 18.05 ? 138 ILE C CG2 1 
ATOM   3304 C CD1 . ILE C 1 121 ? 29.955  38.682 14.451 1.00 17.39 ? 138 ILE C CD1 1 
ATOM   3305 N N   . HIS C 1 122 ? 30.928  42.388 11.820 1.00 15.91 ? 139 HIS C N   1 
ATOM   3306 C CA  . HIS C 1 122 ? 31.717  42.291 10.609 1.00 15.55 ? 139 HIS C CA  1 
ATOM   3307 C C   . HIS C 1 122 ? 32.533  41.005 10.649 1.00 15.53 ? 139 HIS C C   1 
ATOM   3308 O O   . HIS C 1 122 ? 33.025  40.617 11.703 1.00 16.27 ? 139 HIS C O   1 
ATOM   3309 C CB  . HIS C 1 122 ? 32.714  43.447 10.541 1.00 17.06 ? 139 HIS C CB  1 
ATOM   3310 C CG  . HIS C 1 122 ? 33.829  43.193 9.589  1.00 18.44 ? 139 HIS C CG  1 
ATOM   3311 N ND1 . HIS C 1 122 ? 33.764  43.543 8.258  1.00 24.50 ? 139 HIS C ND1 1 
ATOM   3312 C CD2 . HIS C 1 122 ? 35.031  42.596 9.765  1.00 17.59 ? 139 HIS C CD2 1 
ATOM   3313 C CE1 . HIS C 1 122 ? 34.877  43.169 7.655  1.00 23.74 ? 139 HIS C CE1 1 
ATOM   3314 N NE2 . HIS C 1 122 ? 35.659  42.580 8.544  1.00 19.48 ? 139 HIS C NE2 1 
ATOM   3315 N N   . GLY C 1 123 ? 32.699  40.372 9.488  1.00 15.96 ? 140 GLY C N   1 
ATOM   3316 C CA  . GLY C 1 123 ? 33.609  39.250 9.335  1.00 16.03 ? 140 GLY C CA  1 
ATOM   3317 C C   . GLY C 1 123 ? 34.394  39.346 8.040  1.00 16.36 ? 140 GLY C C   1 
ATOM   3318 O O   . GLY C 1 123 ? 33.854  39.784 7.019  1.00 16.89 ? 140 GLY C O   1 
ATOM   3319 N N   . SER C 1 124 ? 35.651  38.914 8.055  1.00 16.87 ? 141 SER C N   1 
ATOM   3320 C CA  . SER C 1 124 ? 36.463  38.959 6.847  1.00 16.89 ? 141 SER C CA  1 
ATOM   3321 C C   . SER C 1 124 ? 35.790  38.153 5.751  1.00 18.03 ? 141 SER C C   1 
ATOM   3322 O O   . SER C 1 124 ? 35.174  37.115 6.003  1.00 19.08 ? 141 SER C O   1 
ATOM   3323 C CB  . SER C 1 124 ? 37.832  38.345 7.114  1.00 17.91 ? 141 SER C CB  1 
ATOM   3324 O OG  . SER C 1 124 ? 38.432  38.916 8.252  1.00 17.43 ? 141 SER C OG  1 
ATOM   3325 N N   . ASP C 1 125 ? 35.929  38.622 4.518  1.00 17.95 ? 142 ASP C N   1 
ATOM   3326 C CA  . ASP C 1 125 ? 35.240  37.975 3.408  1.00 19.55 ? 142 ASP C CA  1 
ATOM   3327 C C   . ASP C 1 125 ? 36.125  37.032 2.592  1.00 19.77 ? 142 ASP C C   1 
ATOM   3328 O O   . ASP C 1 125 ? 35.614  36.376 1.681  1.00 22.59 ? 142 ASP C O   1 
ATOM   3329 C CB  . ASP C 1 125 ? 34.481  38.983 2.524  1.00 25.49 ? 142 ASP C CB  1 
ATOM   3330 C CG  . ASP C 1 125 ? 35.367  40.008 1.863  1.00 27.84 ? 142 ASP C CG  1 
ATOM   3331 O OD1 . ASP C 1 125 ? 36.590  39.826 1.820  1.00 29.13 ? 142 ASP C OD1 1 
ATOM   3332 O OD2 . ASP C 1 125 ? 34.807  41.019 1.363  1.00 29.74 ? 142 ASP C OD2 1 
ATOM   3333 N N   . SER C 1 126 ? 37.410  36.910 2.913  1.00 16.05 ? 143 SER C N   1 
ATOM   3334 C CA  . SER C 1 126 ? 38.321  36.089 2.119  1.00 16.79 ? 143 SER C CA  1 
ATOM   3335 C C   . SER C 1 126 ? 39.609  35.882 2.907  1.00 16.24 ? 143 SER C C   1 
ATOM   3336 O O   . SER C 1 126 ? 39.865  36.563 3.898  1.00 16.91 ? 143 SER C O   1 
ATOM   3337 C CB  . SER C 1 126 ? 38.640  36.744 0.763  1.00 17.97 ? 143 SER C CB  1 
ATOM   3338 O OG  . SER C 1 126 ? 39.493  37.872 0.953  1.00 17.76 ? 143 SER C OG  1 
ATOM   3339 N N   . ALA C 1 127 ? 40.446  34.966 2.413  1.00 18.26 ? 144 ALA C N   1 
ATOM   3340 C CA  . ALA C 1 127 ? 41.743  34.735 3.038  1.00 16.56 ? 144 ALA C CA  1 
ATOM   3341 C C   . ALA C 1 127 ? 42.591  36.001 3.045  1.00 15.57 ? 144 ALA C C   1 
ATOM   3342 O O   . ALA C 1 127 ? 43.207  36.344 4.057  1.00 17.57 ? 144 ALA C O   1 
ATOM   3343 C CB  . ALA C 1 127 ? 42.477  33.596 2.341  1.00 17.43 ? 144 ALA C CB  1 
ATOM   3344 N N   . GLU C 1 128 ? 42.646  36.717 1.924  1.00 17.00 ? 145 GLU C N   1 
ATOM   3345 C CA  . GLU C 1 128 ? 43.455  37.926 1.878  1.00 15.97 ? 145 GLU C CA  1 
ATOM   3346 C C   . GLU C 1 128 ? 42.925  38.987 2.835  1.00 14.77 ? 145 GLU C C   1 
ATOM   3347 O O   . GLU C 1 128 ? 43.708  39.631 3.549  1.00 17.83 ? 145 GLU C O   1 
ATOM   3348 C CB  . GLU C 1 128 ? 43.508  38.476 0.459  1.00 17.21 ? 145 GLU C CB  1 
ATOM   3349 C CG  . GLU C 1 128 ? 44.377  39.728 0.358  1.00 20.72 ? 145 GLU C CG  1 
ATOM   3350 C CD  . GLU C 1 128 ? 44.470  40.260 -1.047 1.00 22.65 ? 145 GLU C CD  1 
ATOM   3351 O OE1 . GLU C 1 128 ? 44.942  39.512 -1.927 1.00 23.23 ? 145 GLU C OE1 1 
ATOM   3352 O OE2 . GLU C 1 128 ? 44.064  41.424 -1.265 1.00 25.91 ? 145 GLU C OE2 1 
ATOM   3353 N N   . SER C 1 129 ? 41.599  39.178 2.873  1.00 17.99 ? 146 SER C N   1 
ATOM   3354 C CA  A SER C 1 129 ? 41.051  40.188 3.768  0.41 17.51 ? 146 SER C CA  1 
ATOM   3355 C CA  B SER C 1 129 ? 41.002  40.164 3.769  0.59 18.67 ? 146 SER C CA  1 
ATOM   3356 C C   . SER C 1 129 ? 41.200  39.785 5.230  1.00 17.04 ? 146 SER C C   1 
ATOM   3357 O O   . SER C 1 129 ? 41.392  40.652 6.083  1.00 16.18 ? 146 SER C O   1 
ATOM   3358 C CB  A SER C 1 129 ? 39.602  40.509 3.405  0.41 16.03 ? 146 SER C CB  1 
ATOM   3359 C CB  B SER C 1 129 ? 39.513  40.321 3.466  0.59 21.44 ? 146 SER C CB  1 
ATOM   3360 O OG  A SER C 1 129 ? 38.789  39.358 3.468  0.41 15.62 ? 146 SER C OG  1 
ATOM   3361 O OG  B SER C 1 129 ? 39.301  41.016 2.258  0.59 24.90 ? 146 SER C OG  1 
ATOM   3362 N N   . ALA C 1 130 ? 41.134  38.489 5.543  1.00 16.71 ? 147 ALA C N   1 
ATOM   3363 C CA  . ALA C 1 130 ? 41.353  38.077 6.929  1.00 15.99 ? 147 ALA C CA  1 
ATOM   3364 C C   . ALA C 1 130 ? 42.760  38.421 7.376  1.00 16.36 ? 147 ALA C C   1 
ATOM   3365 O O   . ALA C 1 130 ? 42.958  38.966 8.458  1.00 17.21 ? 147 ALA C O   1 
ATOM   3366 C CB  . ALA C 1 130 ? 41.094  36.586 7.095  1.00 15.81 ? 147 ALA C CB  1 
ATOM   3367 N N   . LYS C 1 131 ? 43.757  38.098 6.554  1.00 16.64 ? 148 LYS C N   1 
ATOM   3368 C CA  . LYS C 1 131 ? 45.134  38.413 6.930  1.00 17.72 ? 148 LYS C CA  1 
ATOM   3369 C C   . LYS C 1 131 ? 45.325  39.914 7.109  1.00 16.88 ? 148 LYS C C   1 
ATOM   3370 O O   . LYS C 1 131 ? 45.952  40.362 8.083  1.00 18.81 ? 148 LYS C O   1 
ATOM   3371 C CB  . LYS C 1 131 ? 46.087  37.828 5.888  1.00 22.51 ? 148 LYS C CB  1 
ATOM   3372 C CG  . LYS C 1 131 ? 47.552  37.888 6.251  1.00 35.72 ? 148 LYS C CG  1 
ATOM   3373 C CD  . LYS C 1 131 ? 48.399  37.281 5.129  1.00 45.95 ? 148 LYS C CD  1 
ATOM   3374 C CE  . LYS C 1 131 ? 49.855  37.096 5.542  1.00 49.54 ? 148 LYS C CE  1 
ATOM   3375 N NZ  . LYS C 1 131 ? 50.407  38.325 6.171  1.00 52.81 ? 148 LYS C NZ  1 
ATOM   3376 N N   . ARG C 1 132 ? 44.776  40.712 6.192  1.00 16.59 ? 149 ARG C N   1 
ATOM   3377 C CA  . ARG C 1 132 ? 44.917  42.163 6.278  1.00 17.01 ? 149 ARG C CA  1 
ATOM   3378 C C   . ARG C 1 132 ? 44.230  42.723 7.517  1.00 16.39 ? 149 ARG C C   1 
ATOM   3379 O O   . ARG C 1 132 ? 44.791  43.570 8.227  1.00 19.05 ? 149 ARG C O   1 
ATOM   3380 C CB  . ARG C 1 132 ? 44.322  42.800 5.027  1.00 18.73 ? 149 ARG C CB  1 
ATOM   3381 C CG  . ARG C 1 132 ? 44.598  44.277 4.915  1.00 22.24 ? 149 ARG C CG  1 
ATOM   3382 C CD  . ARG C 1 132 ? 43.901  44.867 3.699  1.00 27.21 ? 149 ARG C CD  1 
ATOM   3383 N NE  . ARG C 1 132 ? 42.497  45.167 3.942  1.00 33.55 ? 149 ARG C NE  1 
ATOM   3384 C CZ  . ARG C 1 132 ? 42.061  46.284 4.520  1.00 40.01 ? 149 ARG C CZ  1 
ATOM   3385 N NH1 . ARG C 1 132 ? 42.897  47.211 4.965  1.00 37.61 ? 149 ARG C NH1 1 
ATOM   3386 N NH2 . ARG C 1 132 ? 40.754  46.473 4.666  1.00 43.67 ? 149 ARG C NH2 1 
ATOM   3387 N N   . GLU C 1 133 ? 43.000  42.273 7.781  1.00 15.70 ? 150 GLU C N   1 
ATOM   3388 C CA  . GLU C 1 133 ? 42.231  42.816 8.898  1.00 16.12 ? 150 GLU C CA  1 
ATOM   3389 C C   . GLU C 1 133 ? 42.805  42.392 10.239 1.00 16.23 ? 150 GLU C C   1 
ATOM   3390 O O   . GLU C 1 133 ? 42.857  43.202 11.171 1.00 17.09 ? 150 GLU C O   1 
ATOM   3391 C CB  . GLU C 1 133 ? 40.770  42.412 8.762  1.00 15.74 ? 150 GLU C CB  1 
ATOM   3392 C CG  . GLU C 1 133 ? 40.103  43.046 7.550  1.00 18.13 ? 150 GLU C CG  1 
ATOM   3393 C CD  . GLU C 1 133 ? 38.704  42.526 7.288  1.00 18.70 ? 150 GLU C CD  1 
ATOM   3394 O OE1 . GLU C 1 133 ? 38.236  41.643 8.039  1.00 19.40 ? 150 GLU C OE1 1 
ATOM   3395 O OE2 . GLU C 1 133 ? 38.080  43.014 6.318  1.00 21.13 ? 150 GLU C OE2 1 
ATOM   3396 N N   . ILE C 1 134 ? 43.260  41.140 10.363 1.00 16.58 ? 151 ILE C N   1 
ATOM   3397 C CA  . ILE C 1 134 ? 43.892  40.724 11.617 1.00 17.37 ? 151 ILE C CA  1 
ATOM   3398 C C   . ILE C 1 134 ? 45.108  41.596 11.902 1.00 17.40 ? 151 ILE C C   1 
ATOM   3399 O O   . ILE C 1 134 ? 45.306  42.064 13.033 1.00 19.47 ? 151 ILE C O   1 
ATOM   3400 C CB  . ILE C 1 134 ? 44.235  39.220 11.583 1.00 16.73 ? 151 ILE C CB  1 
ATOM   3401 C CG1 . ILE C 1 134 ? 42.954  38.386 11.523 1.00 16.79 ? 151 ILE C CG1 1 
ATOM   3402 C CG2 . ILE C 1 134 ? 45.067  38.800 12.783 1.00 17.26 ? 151 ILE C CG2 1 
ATOM   3403 C CD1 . ILE C 1 134 ? 43.178  36.902 11.304 1.00 17.29 ? 151 ILE C CD1 1 
ATOM   3404 N N   . SER C 1 135 ? 45.936  41.843 10.883 1.00 18.38 ? 152 SER C N   1 
ATOM   3405 C CA  . SER C 1 135 ? 47.132  42.652 11.080 1.00 19.45 ? 152 SER C CA  1 
ATOM   3406 C C   . SER C 1 135 ? 46.805  44.116 11.354 1.00 18.82 ? 152 SER C C   1 
ATOM   3407 O O   . SER C 1 135 ? 47.585  44.806 12.019 1.00 20.10 ? 152 SER C O   1 
ATOM   3408 C CB  . SER C 1 135 ? 48.035  42.557 9.854  1.00 25.13 ? 152 SER C CB  1 
ATOM   3409 O OG  . SER C 1 135 ? 48.523  41.239 9.699  1.00 31.50 ? 152 SER C OG  1 
ATOM   3410 N N   . LEU C 1 136 ? 45.672  44.604 10.838 1.00 19.55 ? 153 LEU C N   1 
ATOM   3411 C CA  . LEU C 1 136 ? 45.273  45.985 11.069 1.00 18.92 ? 153 LEU C CA  1 
ATOM   3412 C C   . LEU C 1 136 ? 44.873  46.211 12.519 1.00 17.64 ? 153 LEU C C   1 
ATOM   3413 O O   . LEU C 1 136 ? 45.277  47.199 13.135 1.00 19.91 ? 153 LEU C O   1 
ATOM   3414 C CB  . LEU C 1 136 ? 44.110  46.342 10.155 1.00 19.99 ? 153 LEU C CB  1 
ATOM   3415 C CG  . LEU C 1 136 ? 43.540  47.740 10.321 1.00 20.13 ? 153 LEU C CG  1 
ATOM   3416 C CD1 . LEU C 1 136 ? 44.645  48.790 10.119 1.00 23.83 ? 153 LEU C CD1 1 
ATOM   3417 C CD2 . LEU C 1 136 ? 42.388  47.946 9.351  1.00 21.07 ? 153 LEU C CD2 1 
ATOM   3418 N N   . TRP C 1 137 ? 44.076  45.303 13.078 1.00 17.72 ? 154 TRP C N   1 
ATOM   3419 C CA  . TRP C 1 137 ? 43.453  45.498 14.380 1.00 17.02 ? 154 TRP C CA  1 
ATOM   3420 C C   . TRP C 1 137 ? 44.218  44.862 15.526 1.00 17.60 ? 154 TRP C C   1 
ATOM   3421 O O   . TRP C 1 137 ? 43.990  45.241 16.678 1.00 18.50 ? 154 TRP C O   1 
ATOM   3422 C CB  . TRP C 1 137 ? 42.031  44.929 14.341 1.00 18.15 ? 154 TRP C CB  1 
ATOM   3423 C CG  . TRP C 1 137 ? 41.066  45.685 13.464 1.00 17.37 ? 154 TRP C CG  1 
ATOM   3424 C CD1 . TRP C 1 137 ? 40.768  45.419 12.166 1.00 17.10 ? 154 TRP C CD1 1 
ATOM   3425 C CD2 . TRP C 1 137 ? 40.259  46.808 13.838 1.00 16.40 ? 154 TRP C CD2 1 
ATOM   3426 N NE1 . TRP C 1 137 ? 39.823  46.305 11.700 1.00 17.99 ? 154 TRP C NE1 1 
ATOM   3427 C CE2 . TRP C 1 137 ? 39.497  47.169 12.707 1.00 16.37 ? 154 TRP C CE2 1 
ATOM   3428 C CE3 . TRP C 1 137 ? 40.111  47.544 15.016 1.00 18.70 ? 154 TRP C CE3 1 
ATOM   3429 C CZ2 . TRP C 1 137 ? 38.597  48.225 12.722 1.00 17.30 ? 154 TRP C CZ2 1 
ATOM   3430 C CZ3 . TRP C 1 137 ? 39.213  48.584 15.034 1.00 20.28 ? 154 TRP C CZ3 1 
ATOM   3431 C CH2 . TRP C 1 137 ? 38.464  48.919 13.892 1.00 18.09 ? 154 TRP C CH2 1 
ATOM   3432 N N   . PHE C 1 138 ? 45.116  43.912 15.246 1.00 17.74 ? 155 PHE C N   1 
ATOM   3433 C CA  . PHE C 1 138 ? 45.884  43.221 16.277 1.00 19.68 ? 155 PHE C CA  1 
ATOM   3434 C C   . PHE C 1 138 ? 47.387  43.267 15.997 1.00 20.98 ? 155 PHE C C   1 
ATOM   3435 O O   . PHE C 1 138 ? 47.825  43.117 14.856 1.00 23.24 ? 155 PHE C O   1 
ATOM   3436 C CB  . PHE C 1 138 ? 45.453  41.744 16.369 1.00 17.79 ? 155 PHE C CB  1 
ATOM   3437 C CG  . PHE C 1 138 ? 44.128  41.523 17.049 1.00 17.10 ? 155 PHE C CG  1 
ATOM   3438 C CD1 . PHE C 1 138 ? 44.026  41.615 18.433 1.00 18.08 ? 155 PHE C CD1 1 
ATOM   3439 C CD2 . PHE C 1 138 ? 42.988  41.201 16.313 1.00 18.40 ? 155 PHE C CD2 1 
ATOM   3440 C CE1 . PHE C 1 138 ? 42.815  41.413 19.066 1.00 17.44 ? 155 PHE C CE1 1 
ATOM   3441 C CE2 . PHE C 1 138 ? 41.775  40.988 16.949 1.00 18.19 ? 155 PHE C CE2 1 
ATOM   3442 C CZ  . PHE C 1 138 ? 41.693  41.093 18.334 1.00 17.27 ? 155 PHE C CZ  1 
ATOM   3443 N N   . LYS C 1 139 ? 48.177  43.474 17.047 1.00 21.05 ? 156 LYS C N   1 
ATOM   3444 C CA  . LYS C 1 139 ? 49.623  43.239 16.984 1.00 20.49 ? 156 LYS C CA  1 
ATOM   3445 C C   . LYS C 1 139 ? 49.894  41.737 17.102 1.00 19.84 ? 156 LYS C C   1 
ATOM   3446 O O   . LYS C 1 139 ? 49.097  41.004 17.689 1.00 19.27 ? 156 LYS C O   1 
ATOM   3447 C CB  . LYS C 1 139 ? 50.331  43.938 18.135 1.00 26.00 ? 156 LYS C CB  1 
ATOM   3448 C CG  . LYS C 1 139 ? 49.961  45.394 18.387 1.00 34.05 ? 156 LYS C CG  1 
ATOM   3449 C CD  . LYS C 1 139 ? 50.249  45.740 19.857 1.00 45.88 ? 156 LYS C CD  1 
ATOM   3450 C CE  . LYS C 1 139 ? 49.827  47.160 20.246 1.00 55.99 ? 156 LYS C CE  1 
ATOM   3451 N NZ  . LYS C 1 139 ? 50.596  48.203 19.500 1.00 61.54 ? 156 LYS C NZ  1 
ATOM   3452 N N   . PRO C 1 140 ? 51.009  41.241 16.545 1.00 19.99 ? 157 PRO C N   1 
ATOM   3453 C CA  . PRO C 1 140 ? 51.256  39.789 16.617 1.00 20.97 ? 157 PRO C CA  1 
ATOM   3454 C C   . PRO C 1 140 ? 51.273  39.246 18.029 1.00 21.36 ? 157 PRO C C   1 
ATOM   3455 O O   . PRO C 1 140 ? 50.831  38.111 18.253 1.00 22.97 ? 157 PRO C O   1 
ATOM   3456 C CB  . PRO C 1 140 ? 52.608  39.618 15.911 1.00 26.53 ? 157 PRO C CB  1 
ATOM   3457 C CG  . PRO C 1 140 ? 52.689  40.775 14.979 1.00 30.65 ? 157 PRO C CG  1 
ATOM   3458 C CD  . PRO C 1 140 ? 51.987  41.919 15.673 1.00 25.51 ? 157 PRO C CD  1 
ATOM   3459 N N   . GLU C 1 141 ? 51.772  40.019 18.993 1.00 21.06 ? 158 GLU C N   1 
ATOM   3460 C CA  . GLU C 1 141 ? 51.826  39.552 20.375 1.00 21.85 ? 158 GLU C CA  1 
ATOM   3461 C C   . GLU C 1 141 ? 50.442  39.371 20.998 1.00 22.00 ? 158 GLU C C   1 
ATOM   3462 O O   . GLU C 1 141 ? 50.333  38.718 22.043 1.00 22.67 ? 158 GLU C O   1 
ATOM   3463 C CB  . GLU C 1 141 ? 52.681  40.500 21.218 1.00 26.44 ? 158 GLU C CB  1 
ATOM   3464 C CG  . GLU C 1 141 ? 52.175  41.924 21.270 1.00 35.11 ? 158 GLU C CG  1 
ATOM   3465 C CD  . GLU C 1 141 ? 52.985  42.882 20.396 1.00 41.88 ? 158 GLU C CD  1 
ATOM   3466 O OE1 . GLU C 1 141 ? 53.247  42.575 19.196 1.00 38.26 ? 158 GLU C OE1 1 
ATOM   3467 O OE2 . GLU C 1 141 ? 53.362  43.952 20.924 1.00 45.53 ? 158 GLU C OE2 1 
ATOM   3468 N N   . GLU C 1 142 ? 49.393  39.912 20.388 1.00 18.74 ? 159 GLU C N   1 
ATOM   3469 C CA  . GLU C 1 142 ? 48.023  39.768 20.871 1.00 18.94 ? 159 GLU C CA  1 
ATOM   3470 C C   . GLU C 1 142 ? 47.341  38.497 20.370 1.00 18.36 ? 159 GLU C C   1 
ATOM   3471 O O   . GLU C 1 142 ? 46.250  38.155 20.855 1.00 18.62 ? 159 GLU C O   1 
ATOM   3472 C CB  . GLU C 1 142 ? 47.211  41.020 20.490 1.00 19.61 ? 159 GLU C CB  1 
ATOM   3473 C CG  . GLU C 1 142 ? 47.752  42.280 21.159 1.00 21.16 ? 159 GLU C CG  1 
ATOM   3474 C CD  . GLU C 1 142 ? 47.038  43.557 20.785 1.00 25.20 ? 159 GLU C CD  1 
ATOM   3475 O OE1 . GLU C 1 142 ? 46.784  43.773 19.602 1.00 26.85 ? 159 GLU C OE1 1 
ATOM   3476 O OE2 . GLU C 1 142 ? 46.752  44.367 21.693 1.00 35.99 ? 159 GLU C OE2 1 
ATOM   3477 N N   . ILE C 1 143 ? 47.945  37.785 19.424 1.00 18.08 ? 160 ILE C N   1 
ATOM   3478 C CA  . ILE C 1 143 ? 47.371  36.555 18.879 1.00 18.03 ? 160 ILE C CA  1 
ATOM   3479 C C   . ILE C 1 143 ? 47.900  35.380 19.703 1.00 16.97 ? 160 ILE C C   1 
ATOM   3480 O O   . ILE C 1 143 ? 49.112  35.154 19.778 1.00 19.88 ? 160 ILE C O   1 
ATOM   3481 C CB  . ILE C 1 143 ? 47.745  36.390 17.396 1.00 18.67 ? 160 ILE C CB  1 
ATOM   3482 C CG1 . ILE C 1 143 ? 47.416  37.644 16.577 1.00 20.59 ? 160 ILE C CG1 1 
ATOM   3483 C CG2 . ILE C 1 143 ? 47.069  35.171 16.811 1.00 19.64 ? 160 ILE C CG2 1 
ATOM   3484 C CD1 . ILE C 1 143 ? 45.995  38.107 16.628 1.00 25.91 ? 160 ILE C CD1 1 
ATOM   3485 N N   . GLN C 1 144 ? 46.986  34.621 20.302 1.00 16.51 ? 161 GLN C N   1 
ATOM   3486 C CA  . GLN C 1 144 ? 47.300  33.616 21.307 1.00 16.98 ? 161 GLN C CA  1 
ATOM   3487 C C   . GLN C 1 144 ? 47.168  32.234 20.697 1.00 17.50 ? 161 GLN C C   1 
ATOM   3488 O O   . GLN C 1 144 ? 46.119  31.900 20.133 1.00 19.67 ? 161 GLN C O   1 
ATOM   3489 C CB  . GLN C 1 144 ? 46.339  33.734 22.491 1.00 17.34 ? 161 GLN C CB  1 
ATOM   3490 C CG  . GLN C 1 144 ? 46.262  35.150 23.045 1.00 18.52 ? 161 GLN C CG  1 
ATOM   3491 C CD  . GLN C 1 144 ? 47.602  35.643 23.558 1.00 19.60 ? 161 GLN C CD  1 
ATOM   3492 O OE1 . GLN C 1 144 ? 48.432  34.866 24.066 1.00 22.05 ? 161 GLN C OE1 1 
ATOM   3493 N NE2 . GLN C 1 144 ? 47.836  36.934 23.404 1.00 20.59 ? 161 GLN C NE2 1 
ATOM   3494 N N   . SER C 1 145 ? 48.222  31.431 20.832 1.00 17.66 ? 162 SER C N   1 
ATOM   3495 C CA  A SER C 1 145 ? 48.258  30.077 20.297 0.65 17.83 ? 162 SER C CA  1 
ATOM   3496 C CA  B SER C 1 145 ? 48.256  30.075 20.297 0.35 17.08 ? 162 SER C CA  1 
ATOM   3497 C C   . SER C 1 145 ? 48.112  29.081 21.440 1.00 16.56 ? 162 SER C C   1 
ATOM   3498 O O   . SER C 1 145 ? 48.950  29.045 22.349 1.00 20.35 ? 162 SER C O   1 
ATOM   3499 C CB  A SER C 1 145 ? 49.577  29.828 19.568 0.65 21.44 ? 162 SER C CB  1 
ATOM   3500 C CB  B SER C 1 145 ? 49.565  29.825 19.551 0.35 18.59 ? 162 SER C CB  1 
ATOM   3501 O OG  A SER C 1 145 ? 49.623  28.502 19.071 0.65 23.05 ? 162 SER C OG  1 
ATOM   3502 O OG  B SER C 1 145 ? 49.633  30.617 18.381 0.35 19.10 ? 162 SER C OG  1 
ATOM   3503 N N   . TYR C 1 146 ? 47.062  28.271 21.379 1.00 16.42 ? 163 TYR C N   1 
ATOM   3504 C CA  . TYR C 1 146 ? 46.836  27.187 22.326 1.00 17.84 ? 163 TYR C CA  1 
ATOM   3505 C C   . TYR C 1 146 ? 45.933  26.189 21.623 1.00 16.98 ? 163 TYR C C   1 
ATOM   3506 O O   . TYR C 1 146 ? 45.352  26.481 20.575 1.00 17.94 ? 163 TYR C O   1 
ATOM   3507 C CB  . TYR C 1 146 ? 46.238  27.669 23.661 1.00 17.73 ? 163 TYR C CB  1 
ATOM   3508 C CG  . TYR C 1 146 ? 44.892  28.342 23.519 1.00 15.64 ? 163 TYR C CG  1 
ATOM   3509 C CD1 . TYR C 1 146 ? 44.796  29.696 23.228 1.00 16.02 ? 163 TYR C CD1 1 
ATOM   3510 C CD2 . TYR C 1 146 ? 43.721  27.619 23.654 1.00 16.31 ? 163 TYR C CD2 1 
ATOM   3511 C CE1 . TYR C 1 146 ? 43.560  30.311 23.078 1.00 15.32 ? 163 TYR C CE1 1 
ATOM   3512 C CE2 . TYR C 1 146 ? 42.492  28.220 23.507 1.00 16.36 ? 163 TYR C CE2 1 
ATOM   3513 C CZ  . TYR C 1 146 ? 42.411  29.565 23.228 1.00 15.70 ? 163 TYR C CZ  1 
ATOM   3514 O OH  . TYR C 1 146 ? 41.176  30.155 23.073 1.00 16.08 ? 163 TYR C OH  1 
ATOM   3515 N N   . LYS C 1 147 ? 45.851  24.997 22.181 1.00 17.24 ? 164 LYS C N   1 
ATOM   3516 C CA  . LYS C 1 147 ? 45.080  23.915 21.587 1.00 17.52 ? 164 LYS C CA  1 
ATOM   3517 C C   . LYS C 1 147 ? 43.842  23.655 22.429 1.00 16.28 ? 164 LYS C C   1 
ATOM   3518 O O   . LYS C 1 147 ? 43.923  23.579 23.661 1.00 18.26 ? 164 LYS C O   1 
ATOM   3519 C CB  . LYS C 1 147 ? 45.923  22.641 21.531 1.00 23.95 ? 164 LYS C CB  1 
ATOM   3520 C CG  . LYS C 1 147 ? 45.212  21.417 20.994 1.00 31.30 ? 164 LYS C CG  1 
ATOM   3521 C CD  . LYS C 1 147 ? 46.060  20.175 21.292 1.00 40.15 ? 164 LYS C CD  1 
ATOM   3522 C CE  . LYS C 1 147 ? 45.393  18.904 20.823 1.00 45.87 ? 164 LYS C CE  1 
ATOM   3523 N NZ  . LYS C 1 147 ? 45.174  18.946 19.384 1.00 50.50 ? 164 LYS C NZ  1 
ATOM   3524 N N   . LEU C 1 148 ? 42.705  23.492 21.762 1.00 17.19 ? 165 LEU C N   1 
ATOM   3525 C CA  . LEU C 1 148 ? 41.485  23.126 22.471 1.00 17.49 ? 165 LEU C CA  1 
ATOM   3526 C C   . LEU C 1 148 ? 41.566  21.682 22.967 1.00 15.83 ? 165 LEU C C   1 
ATOM   3527 O O   . LEU C 1 148 ? 41.920  20.762 22.223 1.00 17.03 ? 165 LEU C O   1 
ATOM   3528 C CB  . LEU C 1 148 ? 40.263  23.311 21.579 1.00 18.05 ? 165 LEU C CB  1 
ATOM   3529 C CG  . LEU C 1 148 ? 39.825  24.754 21.320 1.00 19.15 ? 165 LEU C CG  1 
ATOM   3530 C CD1 . LEU C 1 148 ? 38.738  24.735 20.267 1.00 20.90 ? 165 LEU C CD1 1 
ATOM   3531 C CD2 . LEU C 1 148 ? 39.355  25.459 22.582 1.00 20.18 ? 165 LEU C CD2 1 
ATOM   3532 N N   . ALA C 1 149 ? 41.224  21.494 24.242 1.00 17.44 ? 166 ALA C N   1 
ATOM   3533 C CA  . ALA C 1 149 ? 41.265  20.164 24.838 1.00 18.43 ? 166 ALA C CA  1 
ATOM   3534 C C   . ALA C 1 149 ? 40.308  19.188 24.166 1.00 18.67 ? 166 ALA C C   1 
ATOM   3535 O O   . ALA C 1 149 ? 40.540  17.975 24.212 1.00 20.44 ? 166 ALA C O   1 
ATOM   3536 C CB  . ALA C 1 149 ? 40.939  20.280 26.324 1.00 24.25 ? 166 ALA C CB  1 
ATOM   3537 N N   . LEU C 1 150 ? 39.232  19.682 23.549 1.00 17.73 ? 167 LEU C N   1 
ATOM   3538 C CA  . LEU C 1 150 ? 38.279  18.834 22.843 1.00 18.48 ? 167 LEU C CA  1 
ATOM   3539 C C   . LEU C 1 150 ? 38.640  18.618 21.368 1.00 16.82 ? 167 LEU C C   1 
ATOM   3540 O O   . LEU C 1 150 ? 37.816  18.099 20.618 1.00 17.25 ? 167 LEU C O   1 
ATOM   3541 C CB  . LEU C 1 150 ? 36.869  19.423 22.964 1.00 22.11 ? 167 LEU C CB  1 
ATOM   3542 C CG  . LEU C 1 150 ? 36.174  19.145 24.306 1.00 27.55 ? 167 LEU C CG  1 
ATOM   3543 C CD1 . LEU C 1 150 ? 34.958  20.018 24.482 1.00 31.84 ? 167 LEU C CD1 1 
ATOM   3544 C CD2 . LEU C 1 150 ? 35.776  17.679 24.394 1.00 30.50 ? 167 LEU C CD2 1 
ATOM   3545 N N   . SER C 1 151 ? 39.870  18.948 20.964 1.00 19.04 ? 168 SER C N   1 
ATOM   3546 C CA  A SER C 1 151 ? 40.250  18.874 19.553 0.39 20.88 ? 168 SER C CA  1 
ATOM   3547 C CA  B SER C 1 151 ? 40.233  18.879 19.549 0.61 19.65 ? 168 SER C CA  1 
ATOM   3548 C C   . SER C 1 151 ? 39.935  17.516 18.940 1.00 20.42 ? 168 SER C C   1 
ATOM   3549 O O   . SER C 1 151 ? 39.511  17.431 17.775 1.00 19.32 ? 168 SER C O   1 
ATOM   3550 C CB  A SER C 1 151 ? 41.745  19.169 19.408 0.39 23.34 ? 168 SER C CB  1 
ATOM   3551 C CB  B SER C 1 151 ? 41.713  19.228 19.376 0.61 18.46 ? 168 SER C CB  1 
ATOM   3552 O OG  A SER C 1 151 ? 42.211  18.813 18.118 0.39 25.88 ? 168 SER C OG  1 
ATOM   3553 O OG  B SER C 1 151 ? 41.915  20.619 19.528 0.61 19.09 ? 168 SER C OG  1 
ATOM   3554 N N   . ASP C 1 152 ? 40.178  16.426 19.685 1.00 19.11 ? 169 ASP C N   1 
ATOM   3555 C CA  . ASP C 1 152 ? 39.978  15.102 19.103 1.00 20.96 ? 169 ASP C CA  1 
ATOM   3556 C C   . ASP C 1 152 ? 38.521  14.856 18.739 1.00 20.60 ? 169 ASP C C   1 
ATOM   3557 O O   . ASP C 1 152 ? 38.233  13.965 17.938 1.00 20.96 ? 169 ASP C O   1 
ATOM   3558 C CB  . ASP C 1 152 ? 40.384  13.987 20.074 1.00 25.72 ? 169 ASP C CB  1 
ATOM   3559 C CG  . ASP C 1 152 ? 41.874  13.907 20.311 1.00 31.63 ? 169 ASP C CG  1 
ATOM   3560 O OD1 . ASP C 1 152 ? 42.657  14.382 19.466 1.00 31.02 ? 169 ASP C OD1 1 
ATOM   3561 O OD2 . ASP C 1 152 ? 42.252  13.328 21.352 1.00 35.62 ? 169 ASP C OD2 1 
ATOM   3562 N N   . TYR C 1 153 ? 37.601  15.602 19.345 1.00 17.87 ? 170 TYR C N   1 
ATOM   3563 C CA  . TYR C 1 153 ? 36.170  15.451 19.120 1.00 16.66 ? 170 TYR C CA  1 
ATOM   3564 C C   . TYR C 1 153 ? 35.596  16.539 18.234 1.00 16.64 ? 170 TYR C C   1 
ATOM   3565 O O   . TYR C 1 153 ? 34.395  16.516 17.950 1.00 18.60 ? 170 TYR C O   1 
ATOM   3566 C CB  . TYR C 1 153 ? 35.437  15.376 20.472 1.00 16.43 ? 170 TYR C CB  1 
ATOM   3567 C CG  . TYR C 1 153 ? 35.871  14.136 21.211 1.00 16.56 ? 170 TYR C CG  1 
ATOM   3568 C CD1 . TYR C 1 153 ? 35.359  12.895 20.874 1.00 16.72 ? 170 TYR C CD1 1 
ATOM   3569 C CD2 . TYR C 1 153 ? 36.851  14.198 22.180 1.00 18.21 ? 170 TYR C CD2 1 
ATOM   3570 C CE1 . TYR C 1 153 ? 35.799  11.749 21.501 1.00 18.30 ? 170 TYR C CE1 1 
ATOM   3571 C CE2 . TYR C 1 153 ? 37.284  13.068 22.821 1.00 22.63 ? 170 TYR C CE2 1 
ATOM   3572 C CZ  . TYR C 1 153 ? 36.761  11.848 22.483 1.00 21.69 ? 170 TYR C CZ  1 
ATOM   3573 O OH  . TYR C 1 153 ? 37.219  10.740 23.150 1.00 25.08 ? 170 TYR C OH  1 
ATOM   3574 N N   . ILE C 1 154 ? 36.430  17.467 17.773 1.00 18.92 ? 171 ILE C N   1 
ATOM   3575 C CA  . ILE C 1 154 ? 36.022  18.534 16.871 1.00 19.01 ? 171 ILE C CA  1 
ATOM   3576 C C   . ILE C 1 154 ? 36.549  18.305 15.462 1.00 19.79 ? 171 ILE C C   1 
ATOM   3577 O O   . ILE C 1 154 ? 35.825  18.504 14.478 1.00 21.69 ? 171 ILE C O   1 
ATOM   3578 C CB  . ILE C 1 154 ? 36.506  19.890 17.425 1.00 19.87 ? 171 ILE C CB  1 
ATOM   3579 C CG1 . ILE C 1 154 ? 35.786  20.217 18.731 1.00 20.16 ? 171 ILE C CG1 1 
ATOM   3580 C CG2 . ILE C 1 154 ? 36.267  21.011 16.426 1.00 18.22 ? 171 ILE C CG2 1 
ATOM   3581 C CD1 . ILE C 1 154 ? 36.510  21.291 19.562 1.00 22.30 ? 171 ILE C CD1 1 
ATOM   3582 N N   . PHE C 1 155 ? 37.796  17.862 15.347 1.00 19.00 ? 172 PHE C N   1 
ATOM   3583 C CA  . PHE C 1 155 ? 38.467  17.711 14.065 1.00 20.30 ? 172 PHE C CA  1 
ATOM   3584 C C   . PHE C 1 155 ? 38.588  16.248 13.675 1.00 23.04 ? 172 PHE C C   1 
ATOM   3585 O O   . PHE C 1 155 ? 38.751  15.371 14.529 1.00 26.33 ? 172 PHE C O   1 
ATOM   3586 C CB  . PHE C 1 155 ? 39.851  18.355 14.113 1.00 21.61 ? 172 PHE C CB  1 
ATOM   3587 C CG  . PHE C 1 155 ? 39.820  19.772 14.570 1.00 20.65 ? 172 PHE C CG  1 
ATOM   3588 C CD1 . PHE C 1 155 ? 39.274  20.755 13.775 1.00 19.91 ? 172 PHE C CD1 1 
ATOM   3589 C CD2 . PHE C 1 155 ? 40.317  20.120 15.809 1.00 20.32 ? 172 PHE C CD2 1 
ATOM   3590 C CE1 . PHE C 1 155 ? 39.234  22.057 14.206 1.00 19.60 ? 172 PHE C CE1 1 
ATOM   3591 C CE2 . PHE C 1 155 ? 40.277  21.406 16.238 1.00 23.16 ? 172 PHE C CE2 1 
ATOM   3592 C CZ  . PHE C 1 155 ? 39.738  22.382 15.439 1.00 21.63 ? 172 PHE C CZ  1 
ATOM   3593 N N   . GLU C 1 156 ? 38.482  15.996 12.372 1.00 26.06 ? 173 GLU C N   1 
ATOM   3594 C CA  . GLU C 1 156 ? 38.764  14.697 11.803 1.00 38.61 ? 173 GLU C CA  1 
ATOM   3595 C C   . GLU C 1 156 ? 40.213  14.326 11.981 1.00 43.78 ? 173 GLU C C   1 
ATOM   3596 O O   . GLU C 1 156 ? 40.546  13.141 12.033 1.00 47.07 ? 173 GLU C O   1 
ATOM   3597 C CB  . GLU C 1 156 ? 38.523  14.737 10.302 1.00 42.06 ? 173 GLU C CB  1 
ATOM   3598 C CG  . GLU C 1 156 ? 37.127  14.508 9.928  1.00 39.86 ? 173 GLU C CG  1 
ATOM   3599 C CD  . GLU C 1 156 ? 36.863  14.813 8.466  1.00 34.19 ? 173 GLU C CD  1 
ATOM   3600 O OE1 . GLU C 1 156 ? 37.796  15.101 7.682  1.00 37.76 ? 173 GLU C OE1 1 
ATOM   3601 O OE2 . GLU C 1 156 ? 35.697  14.750 8.090  1.00 31.47 ? 173 GLU C OE2 1 
ATOM   3602 O OXT . GLU C 1 156 ? 41.069  15.209 12.034 1.00 46.19 ? 173 GLU C OXT 1 
HETATM 3603 C C1  A CIT D 2 .   ? -4.329  29.014 9.405  0.95 47.28 ? 201 CIT A C1  1 
HETATM 3604 O O1  A CIT D 2 .   ? -4.623  29.975 10.160 0.95 47.88 ? 201 CIT A O1  1 
HETATM 3605 O O2  A CIT D 2 .   ? -4.480  27.800 9.660  0.95 48.95 ? 201 CIT A O2  1 
HETATM 3606 C C2  A CIT D 2 .   ? -3.694  29.322 8.039  0.95 42.89 ? 201 CIT A C2  1 
HETATM 3607 C C3  A CIT D 2 .   ? -2.265  29.854 8.172  0.95 40.63 ? 201 CIT A C3  1 
HETATM 3608 O O7  A CIT D 2 .   ? -1.536  28.859 8.877  0.95 34.81 ? 201 CIT A O7  1 
HETATM 3609 C C4  A CIT D 2 .   ? -1.645  30.152 6.791  0.95 43.49 ? 201 CIT A C4  1 
HETATM 3610 C C5  A CIT D 2 .   ? -0.158  30.528 6.830  0.95 46.48 ? 201 CIT A C5  1 
HETATM 3611 O O3  A CIT D 2 .   ? 0.550   30.373 5.829  0.95 52.23 ? 201 CIT A O3  1 
HETATM 3612 O O4  A CIT D 2 .   ? 0.262   30.997 7.906  0.95 46.80 ? 201 CIT A O4  1 
HETATM 3613 C C6  A CIT D 2 .   ? -2.388  31.183 8.985  0.95 44.20 ? 201 CIT A C6  1 
HETATM 3614 O O5  A CIT D 2 .   ? -2.140  31.075 10.208 0.95 40.83 ? 201 CIT A O5  1 
HETATM 3615 O O6  A CIT D 2 .   ? -2.725  32.227 8.384  0.95 46.85 ? 201 CIT A O6  1 
HETATM 3616 C C1  A CIT E 2 .   ? 28.925  8.692  9.603  0.91 43.47 ? 201 CIT B C1  1 
HETATM 3617 O O1  A CIT E 2 .   ? 28.437  7.988  10.518 0.91 38.35 ? 201 CIT B O1  1 
HETATM 3618 O O2  A CIT E 2 .   ? 30.019  9.296  9.624  0.91 47.48 ? 201 CIT B O2  1 
HETATM 3619 C C2  A CIT E 2 .   ? 28.091  8.843  8.324  0.91 40.77 ? 201 CIT B C2  1 
HETATM 3620 C C3  A CIT E 2 .   ? 26.801  9.655  8.526  0.91 37.63 ? 201 CIT B C3  1 
HETATM 3621 O O7  A CIT E 2 .   ? 27.133  10.940 9.026  0.91 33.53 ? 201 CIT B O7  1 
HETATM 3622 C C4  A CIT E 2 .   ? 26.023  9.707  7.203  0.91 37.21 ? 201 CIT B C4  1 
HETATM 3623 C C5  A CIT E 2 .   ? 24.946  10.787 7.118  0.91 40.73 ? 201 CIT B C5  1 
HETATM 3624 O O3  A CIT E 2 .   ? 24.297  10.881 6.061  0.91 43.92 ? 201 CIT B O3  1 
HETATM 3625 O O4  A CIT E 2 .   ? 24.804  11.508 8.138  0.91 41.30 ? 201 CIT B O4  1 
HETATM 3626 C C6  A CIT E 2 .   ? 25.920  8.923  9.572  0.91 40.47 ? 201 CIT B C6  1 
HETATM 3627 O O5  A CIT E 2 .   ? 25.801  9.537  10.650 0.91 39.50 ? 201 CIT B O5  1 
HETATM 3628 O O6  A CIT E 2 .   ? 25.416  7.829  9.267  0.91 43.22 ? 201 CIT B O6  1 
HETATM 3629 C C1  A CIT F 2 .   ? 29.721  47.580 6.844  0.89 50.97 ? 201 CIT C C1  1 
HETATM 3630 O O1  A CIT F 2 .   ? 30.602  47.428 7.721  0.89 51.11 ? 201 CIT C O1  1 
HETATM 3631 O O2  A CIT F 2 .   ? 28.763  48.382 6.873  0.89 52.47 ? 201 CIT C O2  1 
HETATM 3632 C C2  A CIT F 2 .   ? 29.813  46.677 5.609  0.89 47.43 ? 201 CIT C C2  1 
HETATM 3633 C C3  A CIT F 2 .   ? 29.641  45.191 5.942  0.89 43.10 ? 201 CIT C C3  1 
HETATM 3634 O O7  A CIT F 2 .   ? 28.408  45.055 6.654  0.89 35.75 ? 201 CIT C O7  1 
HETATM 3635 C C4  A CIT F 2 .   ? 29.648  44.415 4.616  0.89 45.07 ? 201 CIT C C4  1 
HETATM 3636 C C5  A CIT F 2 .   ? 29.598  42.890 4.740  0.89 47.26 ? 201 CIT C C5  1 
HETATM 3637 O O3  A CIT F 2 .   ? 30.129  42.215 3.841  0.89 51.84 ? 201 CIT C O3  1 
HETATM 3638 O O4  A CIT F 2 .   ? 29.016  42.424 5.759  0.89 43.93 ? 201 CIT C O4  1 
HETATM 3639 C C6  A CIT F 2 .   ? 30.901  44.757 6.764  0.89 49.27 ? 201 CIT C C6  1 
HETATM 3640 O O5  A CIT F 2 .   ? 30.775  44.714 8.005  0.89 49.93 ? 201 CIT C O5  1 
HETATM 3641 O O6  A CIT F 2 .   ? 31.942  44.489 6.136  0.89 52.36 ? 201 CIT C O6  1 
HETATM 3642 O O   . HOH G 3 .   ? 8.950   49.071 6.626  1.00 25.56 ? 301 HOH A O   1 
HETATM 3643 O O   . HOH G 3 .   ? -0.228  32.987 9.142  1.00 30.68 ? 302 HOH A O   1 
HETATM 3644 O O   . HOH G 3 .   ? -4.524  27.252 12.015 1.00 39.34 ? 303 HOH A O   1 
HETATM 3645 O O   . HOH G 3 .   ? 11.394  41.088 2.755  1.00 39.55 ? 304 HOH A O   1 
HETATM 3646 O O   . HOH G 3 .   ? 6.637   43.722 4.662  1.00 18.27 ? 305 HOH A O   1 
HETATM 3647 O O   . HOH G 3 .   ? -2.829  25.941 9.024  1.00 33.79 ? 306 HOH A O   1 
HETATM 3648 O O   . HOH G 3 .   ? 4.441   57.008 24.498 1.00 28.30 ? 307 HOH A O   1 
HETATM 3649 O O   . HOH G 3 .   ? -5.056  36.979 4.443  1.00 33.83 ? 308 HOH A O   1 
HETATM 3650 O O   . HOH G 3 .   ? -16.304 25.032 12.932 1.00 37.66 ? 309 HOH A O   1 
HETATM 3651 O O   . HOH G 3 .   ? -7.862  24.078 19.689 1.00 32.66 ? 310 HOH A O   1 
HETATM 3652 O O   . HOH G 3 .   ? -11.188 47.960 15.947 1.00 40.29 ? 311 HOH A O   1 
HETATM 3653 O O   . HOH G 3 .   ? 16.434  27.635 15.938 1.00 32.65 ? 312 HOH A O   1 
HETATM 3654 O O   . HOH G 3 .   ? 5.388   22.263 25.959 1.00 32.48 ? 313 HOH A O   1 
HETATM 3655 O O   . HOH G 3 .   ? -1.677  49.944 13.483 1.00 32.69 ? 314 HOH A O   1 
HETATM 3656 O O   . HOH G 3 .   ? 19.157  46.565 12.345 1.00 15.94 ? 315 HOH A O   1 
HETATM 3657 O O   . HOH G 3 .   ? 3.424   55.467 16.762 1.00 35.00 ? 316 HOH A O   1 
HETATM 3658 O O   . HOH G 3 .   ? 19.363  54.407 20.837 1.00 31.35 ? 317 HOH A O   1 
HETATM 3659 O O   . HOH G 3 .   ? 10.142  24.773 23.809 1.00 26.11 ? 318 HOH A O   1 
HETATM 3660 O O   . HOH G 3 .   ? 16.368  43.243 21.015 1.00 27.39 ? 319 HOH A O   1 
HETATM 3661 O O   . HOH G 3 .   ? -17.115 24.235 -0.443 1.00 43.79 ? 320 HOH A O   1 
HETATM 3662 O O   . HOH G 3 .   ? -1.078  54.824 19.230 1.00 21.81 ? 321 HOH A O   1 
HETATM 3663 O O   . HOH G 3 .   ? -13.616 31.794 -0.193 1.00 38.57 ? 322 HOH A O   1 
HETATM 3664 O O   . HOH G 3 .   ? 6.384   18.787 0.474  1.00 36.94 ? 323 HOH A O   1 
HETATM 3665 O O   . HOH G 3 .   ? -1.908  54.813 24.291 1.00 23.40 ? 324 HOH A O   1 
HETATM 3666 O O   . HOH G 3 .   ? 3.818   24.876 3.360  1.00 22.00 ? 325 HOH A O   1 
HETATM 3667 O O   . HOH G 3 .   ? 13.075  43.674 9.852  1.00 15.53 ? 326 HOH A O   1 
HETATM 3668 O O   . HOH G 3 .   ? 21.788  54.296 13.051 1.00 35.15 ? 327 HOH A O   1 
HETATM 3669 O O   . HOH G 3 .   ? -17.434 26.172 4.351  1.00 42.91 ? 328 HOH A O   1 
HETATM 3670 O O   . HOH G 3 .   ? -4.327  54.407 23.782 1.00 22.91 ? 329 HOH A O   1 
HETATM 3671 O O   . HOH G 3 .   ? -0.484  47.630 6.576  1.00 26.92 ? 330 HOH A O   1 
HETATM 3672 O O   . HOH G 3 .   ? 16.783  56.365 16.204 1.00 37.91 ? 331 HOH A O   1 
HETATM 3673 O O   . HOH G 3 .   ? -4.942  32.350 11.942 1.00 39.23 ? 332 HOH A O   1 
HETATM 3674 O O   . HOH G 3 .   ? 12.320  54.707 16.642 1.00 32.81 ? 333 HOH A O   1 
HETATM 3675 O O   . HOH G 3 .   ? 2.113   23.013 30.490 1.00 22.61 ? 334 HOH A O   1 
HETATM 3676 O O   . HOH G 3 .   ? -18.079 36.057 19.898 1.00 25.81 ? 335 HOH A O   1 
HETATM 3677 O O   . HOH G 3 .   ? -7.169  46.343 4.460  1.00 30.51 ? 336 HOH A O   1 
HETATM 3678 O O   . HOH G 3 .   ? -2.716  25.605 13.522 1.00 31.94 ? 337 HOH A O   1 
HETATM 3679 O O   . HOH G 3 .   ? 24.328  56.135 22.357 1.00 30.09 ? 338 HOH A O   1 
HETATM 3680 O O   . HOH G 3 .   ? 13.485  21.874 12.752 1.00 27.24 ? 339 HOH A O   1 
HETATM 3681 O O   . HOH G 3 .   ? -13.733 35.485 24.292 1.00 26.32 ? 340 HOH A O   1 
HETATM 3682 O O   . HOH G 3 .   ? -6.456  35.981 8.386  1.00 28.28 ? 341 HOH A O   1 
HETATM 3683 O O   . HOH G 3 .   ? -4.040  54.313 21.061 1.00 22.78 ? 342 HOH A O   1 
HETATM 3684 O O   . HOH G 3 .   ? 12.686  38.367 25.669 1.00 15.38 ? 343 HOH A O   1 
HETATM 3685 O O   . HOH G 3 .   ? 3.365   39.165 9.201  1.00 17.27 ? 344 HOH A O   1 
HETATM 3686 O O   . HOH G 3 .   ? 1.717   22.860 17.968 1.00 16.73 ? 345 HOH A O   1 
HETATM 3687 O O   . HOH G 3 .   ? -11.051 39.933 24.891 1.00 35.47 ? 346 HOH A O   1 
HETATM 3688 O O   . HOH G 3 .   ? 4.990   32.233 6.923  1.00 25.05 ? 347 HOH A O   1 
HETATM 3689 O O   . HOH G 3 .   ? 18.588  55.436 13.845 1.00 35.03 ? 348 HOH A O   1 
HETATM 3690 O O   . HOH G 3 .   ? 8.738   43.117 1.447  1.00 33.48 ? 349 HOH A O   1 
HETATM 3691 O O   . HOH G 3 .   ? 16.010  31.351 14.606 1.00 34.71 ? 350 HOH A O   1 
HETATM 3692 O O   . HOH G 3 .   ? -23.626 35.502 2.404  1.00 40.73 ? 351 HOH A O   1 
HETATM 3693 O O   . HOH G 3 .   ? 15.390  37.748 7.250  1.00 17.49 ? 352 HOH A O   1 
HETATM 3694 O O   . HOH G 3 .   ? -3.213  37.407 6.534  1.00 19.84 ? 353 HOH A O   1 
HETATM 3695 O O   . HOH G 3 .   ? 8.826   27.668 26.718 1.00 25.30 ? 354 HOH A O   1 
HETATM 3696 O O   . HOH G 3 .   ? 28.014  53.787 21.217 1.00 26.57 ? 355 HOH A O   1 
HETATM 3697 O O   . HOH G 3 .   ? 9.864   44.686 24.289 1.00 15.97 ? 356 HOH A O   1 
HETATM 3698 O O   . HOH G 3 .   ? 6.918   24.934 0.674  1.00 18.66 ? 357 HOH A O   1 
HETATM 3699 O O   . HOH G 3 .   ? 6.811   17.833 9.874  1.00 16.73 ? 358 HOH A O   1 
HETATM 3700 O O   . HOH G 3 .   ? -11.147 44.756 10.035 1.00 25.53 ? 359 HOH A O   1 
HETATM 3701 O O   . HOH G 3 .   ? 9.975   50.744 16.602 1.00 22.04 ? 360 HOH A O   1 
HETATM 3702 O O   . HOH G 3 .   ? 10.930  48.226 15.869 1.00 17.27 ? 361 HOH A O   1 
HETATM 3703 O O   . HOH G 3 .   ? -3.655  25.638 16.409 1.00 21.49 ? 362 HOH A O   1 
HETATM 3704 O O   . HOH G 3 .   ? 4.775   51.778 6.619  1.00 36.43 ? 363 HOH A O   1 
HETATM 3705 O O   . HOH G 3 .   ? -6.862  39.057 6.342  1.00 31.05 ? 364 HOH A O   1 
HETATM 3706 O O   . HOH G 3 .   ? -8.666  50.256 13.636 1.00 38.01 ? 365 HOH A O   1 
HETATM 3707 O O   . HOH G 3 .   ? 12.999  32.405 21.852 1.00 19.04 ? 366 HOH A O   1 
HETATM 3708 O O   . HOH G 3 .   ? -0.319  47.708 9.269  1.00 23.03 ? 367 HOH A O   1 
HETATM 3709 O O   . HOH G 3 .   ? -18.958 36.700 12.188 1.00 30.23 ? 368 HOH A O   1 
HETATM 3710 O O   . HOH G 3 .   ? 11.022  31.115 5.979  1.00 20.38 ? 369 HOH A O   1 
HETATM 3711 O O   . HOH G 3 .   ? 14.505  36.735 2.006  1.00 36.42 ? 370 HOH A O   1 
HETATM 3712 O O   . HOH G 3 .   ? 18.441  55.828 24.539 1.00 39.30 ? 371 HOH A O   1 
HETATM 3713 O O   . HOH G 3 .   ? -2.497  46.303 23.647 1.00 16.29 ? 372 HOH A O   1 
HETATM 3714 O O   . HOH G 3 .   ? 7.181   26.524 29.319 1.00 26.51 ? 373 HOH A O   1 
HETATM 3715 O O   . HOH G 3 .   ? -5.093  45.451 24.595 1.00 23.60 ? 374 HOH A O   1 
HETATM 3716 O O   . HOH G 3 .   ? 12.703  56.192 24.013 1.00 30.51 ? 375 HOH A O   1 
HETATM 3717 O O   . HOH G 3 .   ? 13.754  43.662 5.144  1.00 20.12 ? 376 HOH A O   1 
HETATM 3718 O O   . HOH G 3 .   ? -13.969 43.676 15.636 1.00 41.81 ? 377 HOH A O   1 
HETATM 3719 O O   . HOH G 3 .   ? 8.598   46.408 22.631 1.00 14.91 ? 378 HOH A O   1 
HETATM 3720 O O   . HOH G 3 .   ? 16.081  53.731 9.312  1.00 39.22 ? 379 HOH A O   1 
HETATM 3721 O O   . HOH G 3 .   ? -9.077  40.226 26.751 1.00 19.67 ? 380 HOH A O   1 
HETATM 3722 O O   . HOH G 3 .   ? 8.088   36.785 3.564  1.00 24.87 ? 381 HOH A O   1 
HETATM 3723 O O   . HOH G 3 .   ? 11.863  33.451 26.240 0.50 14.59 ? 382 HOH A O   1 
HETATM 3724 O O   . HOH G 3 .   ? -9.169  36.100 5.655  1.00 28.07 ? 383 HOH A O   1 
HETATM 3725 O O   . HOH G 3 .   ? 15.008  38.206 22.701 1.00 26.02 ? 384 HOH A O   1 
HETATM 3726 O O   . HOH G 3 .   ? 1.923   51.964 17.760 1.00 26.99 ? 385 HOH A O   1 
HETATM 3727 O O   . HOH G 3 .   ? 4.210   19.694 7.949  1.00 19.23 ? 386 HOH A O   1 
HETATM 3728 O O   . HOH G 3 .   ? -0.431  22.497 29.202 1.00 19.64 ? 387 HOH A O   1 
HETATM 3729 O O   . HOH G 3 .   ? 10.625  26.872 3.559  1.00 30.79 ? 388 HOH A O   1 
HETATM 3730 O O   . HOH G 3 .   ? -0.270  55.462 22.119 1.00 20.13 ? 389 HOH A O   1 
HETATM 3731 O O   . HOH G 3 .   ? -8.506  25.051 21.911 1.00 26.51 ? 390 HOH A O   1 
HETATM 3732 O O   . HOH G 3 .   ? 6.753   27.869 1.736  1.00 48.29 ? 391 HOH A O   1 
HETATM 3733 O O   . HOH G 3 .   ? -2.644  13.985 12.737 1.00 36.96 ? 392 HOH A O   1 
HETATM 3734 O O   . HOH G 3 .   ? 16.163  35.494 22.640 1.00 31.09 ? 393 HOH A O   1 
HETATM 3735 O O   . HOH G 3 .   ? 8.350   46.665 3.087  1.00 42.09 ? 394 HOH A O   1 
HETATM 3736 O O   . HOH G 3 .   ? 2.566   43.804 1.764  1.00 45.35 ? 395 HOH A O   1 
HETATM 3737 O O   . HOH G 3 .   ? -13.443 21.376 7.780  1.00 38.25 ? 396 HOH A O   1 
HETATM 3738 O O   . HOH G 3 .   ? 8.033   54.250 17.644 1.00 36.55 ? 397 HOH A O   1 
HETATM 3739 O O   . HOH G 3 .   ? -15.077 32.967 6.803  1.00 41.61 ? 398 HOH A O   1 
HETATM 3740 O O   . HOH G 3 .   ? 13.564  32.675 11.839 1.00 31.87 ? 399 HOH A O   1 
HETATM 3741 O O   . HOH G 3 .   ? 0.591   19.198 7.552  1.00 33.19 ? 400 HOH A O   1 
HETATM 3742 O O   . HOH G 3 .   ? -18.267 29.916 5.231  1.00 37.05 ? 401 HOH A O   1 
HETATM 3743 O O   . HOH G 3 .   ? -8.974  48.991 8.874  1.00 43.43 ? 402 HOH A O   1 
HETATM 3744 O O   . HOH G 3 .   ? -15.795 26.172 17.828 1.00 34.39 ? 403 HOH A O   1 
HETATM 3745 O O   . HOH G 3 .   ? -11.101 42.163 22.918 1.00 35.13 ? 404 HOH A O   1 
HETATM 3746 O O   . HOH G 3 .   ? 5.064   20.605 23.606 1.00 27.74 ? 405 HOH A O   1 
HETATM 3747 O O   . HOH G 3 .   ? -7.234  49.320 15.574 1.00 34.90 ? 406 HOH A O   1 
HETATM 3748 O O   . HOH G 3 .   ? 16.722  34.108 3.276  1.00 34.27 ? 407 HOH A O   1 
HETATM 3749 O O   . HOH G 3 .   ? 1.836   49.607 9.117  1.00 25.77 ? 408 HOH A O   1 
HETATM 3750 O O   . HOH G 3 .   ? 12.904  23.880 4.020  1.00 39.83 ? 409 HOH A O   1 
HETATM 3751 O O   . HOH G 3 .   ? 11.046  52.658 18.264 1.00 22.37 ? 410 HOH A O   1 
HETATM 3752 O O   . HOH G 3 .   ? 10.192  28.457 5.751  1.00 17.55 ? 411 HOH A O   1 
HETATM 3753 O O   . HOH G 3 .   ? 3.224   59.024 20.339 1.00 35.77 ? 412 HOH A O   1 
HETATM 3754 O O   . HOH G 3 .   ? -0.350  19.565 5.123  1.00 39.59 ? 413 HOH A O   1 
HETATM 3755 O O   . HOH G 3 .   ? 4.186   39.737 3.087  1.00 34.78 ? 414 HOH A O   1 
HETATM 3756 O O   . HOH G 3 .   ? 18.611  41.075 20.755 1.00 24.23 ? 415 HOH A O   1 
HETATM 3757 O O   . HOH G 3 .   ? 12.144  32.736 14.171 1.00 24.45 ? 416 HOH A O   1 
HETATM 3758 O O   . HOH G 3 .   ? -14.442 30.219 22.379 1.00 27.87 ? 417 HOH A O   1 
HETATM 3759 O O   . HOH G 3 .   ? 8.681   56.856 24.014 1.00 24.24 ? 418 HOH A O   1 
HETATM 3760 O O   . HOH G 3 .   ? 3.586   36.099 3.084  1.00 55.02 ? 419 HOH A O   1 
HETATM 3761 O O   . HOH G 3 .   ? 21.310  56.265 21.748 1.00 36.34 ? 420 HOH A O   1 
HETATM 3762 O O   . HOH G 3 .   ? -12.652 42.827 8.653  1.00 37.11 ? 421 HOH A O   1 
HETATM 3763 O O   . HOH G 3 .   ? -2.184  34.785 6.851  1.00 34.50 ? 422 HOH A O   1 
HETATM 3764 O O   . HOH G 3 .   ? -5.143  48.901 11.268 1.00 29.04 ? 423 HOH A O   1 
HETATM 3765 O O   . HOH G 3 .   ? 12.918  29.843 20.623 1.00 23.90 ? 424 HOH A O   1 
HETATM 3766 O O   . HOH G 3 .   ? 14.628  26.700 18.852 1.00 38.08 ? 425 HOH A O   1 
HETATM 3767 O O   . HOH G 3 .   ? 3.704   29.119 3.450  1.00 32.01 ? 426 HOH A O   1 
HETATM 3768 O O   . HOH G 3 .   ? 5.896   57.931 20.215 1.00 53.17 ? 427 HOH A O   1 
HETATM 3769 O O   . HOH G 3 .   ? -11.854 45.338 17.806 1.00 39.83 ? 428 HOH A O   1 
HETATM 3770 O O   . HOH G 3 .   ? 1.581   16.617 8.091  1.00 37.09 ? 429 HOH A O   1 
HETATM 3771 O O   . HOH G 3 .   ? -4.109  52.797 26.245 1.00 34.31 ? 430 HOH A O   1 
HETATM 3772 O O   . HOH G 3 .   ? -22.313 37.883 1.932  1.00 44.43 ? 431 HOH A O   1 
HETATM 3773 O O   . HOH G 3 .   ? 15.209  22.357 15.085 1.00 28.28 ? 432 HOH A O   1 
HETATM 3774 O O   . HOH G 3 .   ? -12.841 46.031 11.978 1.00 38.07 ? 433 HOH A O   1 
HETATM 3775 O O   . HOH G 3 .   ? 14.102  35.965 9.120  1.00 37.86 ? 434 HOH A O   1 
HETATM 3776 O O   . HOH G 3 .   ? 15.482  31.727 17.092 1.00 44.90 ? 435 HOH A O   1 
HETATM 3777 O O   . HOH G 3 .   ? 2.065   48.483 5.604  1.00 35.70 ? 436 HOH A O   1 
HETATM 3778 O O   . HOH G 3 .   ? -15.281 43.965 13.409 1.00 45.19 ? 437 HOH A O   1 
HETATM 3779 O O   . HOH G 3 .   ? 16.049  30.156 19.114 1.00 37.95 ? 438 HOH A O   1 
HETATM 3780 O O   . HOH G 3 .   ? 14.477  29.760 24.987 1.00 45.46 ? 439 HOH A O   1 
HETATM 3781 O O   . HOH G 3 .   ? -8.883  47.544 6.560  1.00 43.60 ? 440 HOH A O   1 
HETATM 3782 O O   . HOH G 3 .   ? 12.518  45.562 1.985  1.00 57.10 ? 441 HOH A O   1 
HETATM 3783 O O   . HOH G 3 .   ? 14.917  34.098 20.816 1.00 21.05 ? 442 HOH A O   1 
HETATM 3784 O O   . HOH G 3 .   ? 6.286   18.223 4.808  1.00 35.02 ? 443 HOH A O   1 
HETATM 3785 O O   . HOH G 3 .   ? -12.914 27.756 23.792 1.00 34.67 ? 444 HOH A O   1 
HETATM 3786 O O   . HOH G 3 .   ? 7.496   33.933 3.604  1.00 44.63 ? 445 HOH A O   1 
HETATM 3787 O O   . HOH G 3 .   ? 0.868   58.263 22.280 1.00 31.73 ? 446 HOH A O   1 
HETATM 3788 O O   . HOH G 3 .   ? 3.190   18.416 5.803  1.00 42.17 ? 447 HOH A O   1 
HETATM 3789 O O   . HOH G 3 .   ? 4.769   42.695 2.728  1.00 33.86 ? 448 HOH A O   1 
HETATM 3790 O O   . HOH G 3 .   ? 2.992   26.806 1.728  1.00 34.19 ? 449 HOH A O   1 
HETATM 3791 O O   . HOH G 3 .   ? 13.661  32.273 24.434 1.00 22.09 ? 450 HOH A O   1 
HETATM 3792 O O   . HOH G 3 .   ? -14.637 24.143 19.251 1.00 44.14 ? 451 HOH A O   1 
HETATM 3793 O O   . HOH G 3 .   ? 13.532  26.480 3.165  1.00 40.17 ? 452 HOH A O   1 
HETATM 3794 O O   . HOH G 3 .   ? 6.469   58.402 23.406 1.00 43.03 ? 453 HOH A O   1 
HETATM 3795 O O   . HOH G 3 .   ? -11.058 27.752 25.505 1.00 28.35 ? 454 HOH A O   1 
HETATM 3796 O O   . HOH G 3 .   ? 11.017  58.156 23.935 1.00 39.43 ? 455 HOH A O   1 
HETATM 3797 O O   . HOH G 3 .   ? 10.933  53.218 14.571 1.00 31.91 ? 456 HOH A O   1 
HETATM 3798 O O   . HOH G 3 .   ? 1.629   57.915 25.363 1.00 44.73 ? 457 HOH A O   1 
HETATM 3799 O O   . HOH G 3 .   ? 15.879  34.216 24.834 1.00 34.06 ? 458 HOH A O   1 
HETATM 3800 O O   . HOH G 3 .   ? -0.763  44.173 -4.024 1.00 39.84 ? 459 HOH A O   1 
HETATM 3801 O O   . HOH G 3 .   ? -8.939  44.123 3.048  1.00 44.99 ? 460 HOH A O   1 
HETATM 3802 O O   . HOH G 3 .   ? -2.358  48.923 10.523 1.00 29.60 ? 461 HOH A O   1 
HETATM 3803 O O   . HOH G 3 .   ? -6.107  56.224 24.394 1.00 32.62 ? 462 HOH A O   1 
HETATM 3804 O O   . HOH G 3 .   ? 5.889   37.882 2.429  1.00 37.61 ? 463 HOH A O   1 
HETATM 3805 O O   . HOH G 3 .   ? -9.675  25.439 25.910 1.00 27.98 ? 464 HOH A O   1 
HETATM 3806 O O   . HOH G 3 .   ? -1.642  56.448 26.556 1.00 30.66 ? 465 HOH A O   1 
HETATM 3807 O O   . HOH G 3 .   ? 17.159  25.362 4.920  1.00 41.53 ? 466 HOH A O   1 
HETATM 3808 O O   . HOH G 3 .   ? 2.508   50.711 6.795  1.00 36.00 ? 467 HOH A O   1 
HETATM 3809 O O   . HOH G 3 .   ? -23.538 35.952 9.595  1.00 32.24 ? 468 HOH A O   1 
HETATM 3810 O O   . HOH G 3 .   ? 11.766  47.707 3.325  1.00 47.30 ? 469 HOH A O   1 
HETATM 3811 O O   . HOH G 3 .   ? 9.298   32.108 3.794  1.00 36.61 ? 470 HOH A O   1 
HETATM 3812 O O   . HOH G 3 .   ? 3.884   16.018 6.963  1.00 34.53 ? 471 HOH A O   1 
HETATM 3813 O O   . HOH G 3 .   ? 15.785  34.083 18.180 1.00 27.81 ? 472 HOH A O   1 
HETATM 3814 O O   . HOH G 3 .   ? -4.647  50.189 13.784 1.00 39.71 ? 473 HOH A O   1 
HETATM 3815 O O   . HOH G 3 .   ? 14.365  46.291 4.307  1.00 50.56 ? 474 HOH A O   1 
HETATM 3816 O O   . HOH G 3 .   ? 15.356  23.961 18.830 1.00 26.78 ? 475 HOH A O   1 
HETATM 3817 O O   . HOH G 3 .   ? -12.711 50.009 16.559 1.00 42.75 ? 476 HOH A O   1 
HETATM 3818 O O   . HOH G 3 .   ? 13.318  31.433 4.556  1.00 38.59 ? 477 HOH A O   1 
HETATM 3819 O O   . HOH G 3 .   ? -11.720 30.517 -4.199 1.00 35.94 ? 478 HOH A O   1 
HETATM 3820 O O   . HOH G 3 .   ? -17.388 26.058 15.548 1.00 40.26 ? 479 HOH A O   1 
HETATM 3821 O O   . HOH H 3 .   ? 20.204  27.496 15.776 1.00 30.66 ? 301 HOH B O   1 
HETATM 3822 O O   . HOH H 3 .   ? 4.516   9.924  9.284  1.00 27.17 ? 302 HOH B O   1 
HETATM 3823 O O   . HOH H 3 .   ? 10.054  10.441 6.784  1.00 19.05 ? 303 HOH B O   1 
HETATM 3824 O O   . HOH H 3 .   ? 22.627  12.767 7.660  1.00 42.16 ? 304 HOH B O   1 
HETATM 3825 O O   . HOH H 3 .   ? 2.141   3.041  28.398 1.00 29.37 ? 305 HOH B O   1 
HETATM 3826 O O   . HOH H 3 .   ? 6.659   0.183  21.854 1.00 38.14 ? 306 HOH B O   1 
HETATM 3827 O O   . HOH H 3 .   ? 25.287  21.917 26.339 1.00 28.92 ? 307 HOH B O   1 
HETATM 3828 O O   . HOH H 3 .   ? 33.107  18.397 29.767 1.00 29.57 ? 308 HOH B O   1 
HETATM 3829 O O   . HOH H 3 .   ? 23.101  10.563 9.835  1.00 31.93 ? 309 HOH B O   1 
HETATM 3830 O O   . HOH H 3 .   ? 39.217  0.646  13.137 1.00 36.57 ? 310 HOH B O   1 
HETATM 3831 O O   . HOH H 3 .   ? 7.293   19.834 22.990 1.00 32.49 ? 311 HOH B O   1 
HETATM 3832 O O   . HOH H 3 .   ? 31.390  11.634 13.329 1.00 44.36 ? 312 HOH B O   1 
HETATM 3833 O O   . HOH H 3 .   ? -3.560  17.366 24.357 1.00 33.46 ? 313 HOH B O   1 
HETATM 3834 O O   . HOH H 3 .   ? 30.031  -7.425 13.322 1.00 35.20 ? 314 HOH B O   1 
HETATM 3835 O O   . HOH H 3 .   ? -4.399  13.916 19.681 1.00 42.34 ? 315 HOH B O   1 
HETATM 3836 O O   . HOH H 3 .   ? 31.209  -2.731 7.775  1.00 43.29 ? 316 HOH B O   1 
HETATM 3837 O O   . HOH H 3 .   ? 2.303   20.427 14.758 1.00 16.46 ? 317 HOH B O   1 
HETATM 3838 O O   . HOH H 3 .   ? 10.800  2.841  11.962 1.00 37.62 ? 318 HOH B O   1 
HETATM 3839 O O   . HOH H 3 .   ? 26.175  27.622 11.700 1.00 32.09 ? 319 HOH B O   1 
HETATM 3840 O O   . HOH H 3 .   ? 29.634  -1.799 25.201 1.00 25.33 ? 320 HOH B O   1 
HETATM 3841 O O   . HOH H 3 .   ? 31.561  21.528 24.960 1.00 31.99 ? 321 HOH B O   1 
HETATM 3842 O O   . HOH H 3 .   ? 30.635  9.114  12.221 1.00 39.57 ? 322 HOH B O   1 
HETATM 3843 O O   . HOH H 3 .   ? -5.630  18.927 16.652 1.00 38.23 ? 323 HOH B O   1 
HETATM 3844 O O   . HOH H 3 .   ? 9.067   12.196 3.598  1.00 31.71 ? 324 HOH B O   1 
HETATM 3845 O O   . HOH H 3 .   ? 40.566  4.582  7.663  1.00 36.59 ? 325 HOH B O   1 
HETATM 3846 O O   . HOH H 3 .   ? -7.363  20.730 25.864 1.00 30.54 ? 326 HOH B O   1 
HETATM 3847 O O   . HOH H 3 .   ? 26.701  24.207 23.083 1.00 27.13 ? 327 HOH B O   1 
HETATM 3848 O O   . HOH H 3 .   ? 7.427   16.336 11.985 1.00 16.88 ? 328 HOH B O   1 
HETATM 3849 O O   . HOH H 3 .   ? 26.481  6.689  12.118 1.00 38.72 ? 329 HOH B O   1 
HETATM 3850 O O   . HOH H 3 .   ? -5.999  18.016 25.396 1.00 36.44 ? 330 HOH B O   1 
HETATM 3851 O O   . HOH H 3 .   ? 9.097   -4.467 7.962  1.00 38.68 ? 331 HOH B O   1 
HETATM 3852 O O   . HOH H 3 .   ? 14.057  19.700 26.883 1.00 16.01 ? 332 HOH B O   1 
HETATM 3853 O O   . HOH H 3 .   ? 31.849  17.416 17.229 1.00 16.62 ? 333 HOH B O   1 
HETATM 3854 O O   . HOH H 3 .   ? 14.584  2.666  26.080 1.00 20.91 ? 334 HOH B O   1 
HETATM 3855 O O   . HOH H 3 .   ? 3.731   10.537 19.353 1.00 23.04 ? 335 HOH B O   1 
HETATM 3856 O O   . HOH H 3 .   ? 11.078  21.097 8.725  1.00 18.12 ? 336 HOH B O   1 
HETATM 3857 O O   . HOH H 3 .   ? 5.353   12.662 18.500 1.00 18.06 ? 337 HOH B O   1 
HETATM 3858 O O   . HOH H 3 .   ? 18.562  22.646 22.265 1.00 19.14 ? 338 HOH B O   1 
HETATM 3859 O O   . HOH H 3 .   ? 20.725  5.129  7.873  1.00 20.82 ? 339 HOH B O   1 
HETATM 3860 O O   . HOH H 3 .   ? 31.995  11.141 16.287 1.00 24.31 ? 340 HOH B O   1 
HETATM 3861 O O   . HOH H 3 .   ? 32.582  23.495 8.391  1.00 17.68 ? 341 HOH B O   1 
HETATM 3862 O O   . HOH H 3 .   ? 15.157  -3.183 7.248  1.00 31.40 ? 342 HOH B O   1 
HETATM 3863 O O   . HOH H 3 .   ? 16.176  10.060 10.692 1.00 17.84 ? 343 HOH B O   1 
HETATM 3864 O O   . HOH H 3 .   ? 19.453  -5.136 12.246 1.00 30.27 ? 344 HOH B O   1 
HETATM 3865 O O   . HOH H 3 .   ? -0.675  10.584 20.162 1.00 30.61 ? 345 HOH B O   1 
HETATM 3866 O O   . HOH H 3 .   ? 25.053  0.197  6.688  1.00 35.32 ? 346 HOH B O   1 
HETATM 3867 O O   . HOH H 3 .   ? 14.964  15.029 4.836  1.00 32.59 ? 347 HOH B O   1 
HETATM 3868 O O   . HOH H 3 .   ? 36.334  8.581  19.654 1.00 33.81 ? 348 HOH B O   1 
HETATM 3869 O O   . HOH H 3 .   ? -7.328  25.071 24.449 1.00 25.29 ? 349 HOH B O   1 
HETATM 3870 O O   . HOH H 3 .   ? 23.441  0.081  28.274 1.00 23.72 ? 350 HOH B O   1 
HETATM 3871 O O   . HOH H 3 .   ? 21.110  14.681 7.381  1.00 25.86 ? 351 HOH B O   1 
HETATM 3872 O O   . HOH H 3 .   ? 18.992  -7.644 17.133 1.00 46.55 ? 352 HOH B O   1 
HETATM 3873 O O   . HOH H 3 .   ? 34.589  16.225 28.178 1.00 21.90 ? 353 HOH B O   1 
HETATM 3874 O O   . HOH H 3 .   ? 38.196  5.133  20.052 1.00 42.12 ? 354 HOH B O   1 
HETATM 3875 O O   . HOH H 3 .   ? 37.967  0.850  17.919 1.00 29.68 ? 355 HOH B O   1 
HETATM 3876 O O   . HOH H 3 .   ? 27.328  21.097 28.977 1.00 25.21 ? 356 HOH B O   1 
HETATM 3877 O O   . HOH H 3 .   ? 9.848   14.004 26.360 1.00 17.00 ? 357 HOH B O   1 
HETATM 3878 O O   . HOH H 3 .   ? 13.647  22.104 17.384 1.00 18.35 ? 358 HOH B O   1 
HETATM 3879 O O   . HOH H 3 .   ? 24.969  23.647 1.049  1.00 35.77 ? 359 HOH B O   1 
HETATM 3880 O O   . HOH H 3 .   ? 6.579   16.627 7.314  1.00 20.87 ? 360 HOH B O   1 
HETATM 3881 O O   . HOH H 3 .   ? 12.968  -2.549 14.001 1.00 41.53 ? 361 HOH B O   1 
HETATM 3882 O O   . HOH H 3 .   ? 22.557  -6.446 18.063 1.00 35.72 ? 362 HOH B O   1 
HETATM 3883 O O   . HOH H 3 .   ? 10.021  15.774 4.464  1.00 27.89 ? 363 HOH B O   1 
HETATM 3884 O O   . HOH H 3 .   ? 17.073  25.179 15.042 1.00 30.42 ? 364 HOH B O   1 
HETATM 3885 O O   . HOH H 3 .   ? -1.270  10.701 27.652 1.00 33.90 ? 365 HOH B O   1 
HETATM 3886 O O   . HOH H 3 .   ? 18.769  20.484 6.370  1.00 18.82 ? 366 HOH B O   1 
HETATM 3887 O O   . HOH H 3 .   ? 8.841   11.896 25.038 1.00 16.74 ? 367 HOH B O   1 
HETATM 3888 O O   . HOH H 3 .   ? 10.595  2.248  9.474  1.00 40.83 ? 368 HOH B O   1 
HETATM 3889 O O   . HOH H 3 .   ? 12.748  21.561 24.005 1.00 27.03 ? 369 HOH B O   1 
HETATM 3890 O O   . HOH H 3 .   ? 6.712   10.280 5.935  1.00 39.93 ? 370 HOH B O   1 
HETATM 3891 O O   . HOH H 3 .   ? 18.725  21.521 26.780 1.00 14.58 ? 371 HOH B O   1 
HETATM 3892 O O   . HOH H 3 .   ? 16.900  22.434 12.399 1.00 34.36 ? 372 HOH B O   1 
HETATM 3893 O O   . HOH H 3 .   ? 35.535  7.682  21.771 1.00 38.39 ? 373 HOH B O   1 
HETATM 3894 O O   . HOH H 3 .   ? 24.444  -1.679 26.535 1.00 37.16 ? 374 HOH B O   1 
HETATM 3895 O O   . HOH H 3 .   ? 32.172  20.275 6.390  1.00 26.26 ? 375 HOH B O   1 
HETATM 3896 O O   . HOH H 3 .   ? 18.228  12.158 4.101  1.00 49.21 ? 376 HOH B O   1 
HETATM 3897 O O   . HOH H 3 .   ? 32.847  21.899 22.343 1.00 26.34 ? 377 HOH B O   1 
HETATM 3898 O O   . HOH H 3 .   ? 33.485  17.732 6.228  1.00 32.61 ? 378 HOH B O   1 
HETATM 3899 O O   . HOH H 3 .   ? 8.062   23.146 22.416 1.00 24.06 ? 379 HOH B O   1 
HETATM 3900 O O   . HOH H 3 .   ? 21.782  3.319  5.729  1.00 40.38 ? 380 HOH B O   1 
HETATM 3901 O O   . HOH H 3 .   ? 5.791   -0.277 26.333 1.00 31.86 ? 381 HOH B O   1 
HETATM 3902 O O   . HOH H 3 .   ? 0.083   6.802  27.622 1.00 26.13 ? 382 HOH B O   1 
HETATM 3903 O O   . HOH H 3 .   ? 31.265  13.137 3.936  1.00 42.23 ? 383 HOH B O   1 
HETATM 3904 O O   . HOH H 3 .   ? -4.921  15.543 17.556 1.00 33.19 ? 384 HOH B O   1 
HETATM 3905 O O   . HOH H 3 .   ? 1.901   10.428 21.426 1.00 23.63 ? 385 HOH B O   1 
HETATM 3906 O O   . HOH H 3 .   ? 2.092   6.977  20.879 1.00 41.10 ? 386 HOH B O   1 
HETATM 3907 O O   . HOH H 3 .   ? 29.109  21.953 26.675 1.00 39.66 ? 387 HOH B O   1 
HETATM 3908 O O   . HOH H 3 .   ? 22.077  21.792 3.298  1.00 38.22 ? 388 HOH B O   1 
HETATM 3909 O O   . HOH H 3 .   ? 6.449   2.740  20.605 1.00 27.81 ? 389 HOH B O   1 
HETATM 3910 O O   . HOH H 3 .   ? 12.750  2.440  3.036  1.00 30.48 ? 390 HOH B O   1 
HETATM 3911 O O   . HOH H 3 .   ? 34.311  0.014  22.833 1.00 30.96 ? 391 HOH B O   1 
HETATM 3912 O O   . HOH H 3 .   ? 14.305  23.843 23.511 1.00 31.16 ? 392 HOH B O   1 
HETATM 3913 O O   . HOH H 3 .   ? 23.878  14.687 3.965  1.00 32.39 ? 393 HOH B O   1 
HETATM 3914 O O   . HOH H 3 .   ? 21.486  21.031 5.779  1.00 21.53 ? 394 HOH B O   1 
HETATM 3915 O O   . HOH H 3 .   ? 8.164   3.522  11.843 1.00 31.41 ? 395 HOH B O   1 
HETATM 3916 O O   . HOH H 3 .   ? 17.854  21.164 14.756 1.00 24.47 ? 396 HOH B O   1 
HETATM 3917 O O   . HOH H 3 .   ? 20.681  23.772 20.727 1.00 26.55 ? 397 HOH B O   1 
HETATM 3918 O O   . HOH H 3 .   ? 36.273  19.503 6.387  1.00 41.33 ? 398 HOH B O   1 
HETATM 3919 O O   . HOH H 3 .   ? 14.454  10.130 4.723  1.00 37.08 ? 399 HOH B O   1 
HETATM 3920 O O   . HOH H 3 .   ? 22.176  26.929 18.350 1.00 35.21 ? 400 HOH B O   1 
HETATM 3921 O O   . HOH H 3 .   ? 18.746  -0.293 28.395 1.00 34.95 ? 401 HOH B O   1 
HETATM 3922 O O   . HOH H 3 .   ? 25.160  29.143 14.229 1.00 30.86 ? 402 HOH B O   1 
HETATM 3923 O O   . HOH H 3 .   ? 12.790  -3.631 16.604 1.00 42.17 ? 403 HOH B O   1 
HETATM 3924 O O   . HOH H 3 .   ? 16.770  0.872  27.036 1.00 28.98 ? 404 HOH B O   1 
HETATM 3925 O O   . HOH H 3 .   ? 13.562  21.038 10.214 1.00 32.03 ? 405 HOH B O   1 
HETATM 3926 O O   . HOH H 3 .   ? 15.987  23.328 21.547 1.00 21.36 ? 406 HOH B O   1 
HETATM 3927 O O   . HOH H 3 .   ? 17.914  15.927 4.748  1.00 47.62 ? 407 HOH B O   1 
HETATM 3928 O O   . HOH H 3 .   ? 12.352  16.980 4.332  1.00 46.74 ? 408 HOH B O   1 
HETATM 3929 O O   . HOH H 3 .   ? 11.666  9.202  4.819  1.00 35.18 ? 409 HOH B O   1 
HETATM 3930 O O   . HOH H 3 .   ? 35.864  2.395  23.963 1.00 39.55 ? 410 HOH B O   1 
HETATM 3931 O O   . HOH H 3 .   ? 30.223  11.077 6.046  1.00 47.77 ? 411 HOH B O   1 
HETATM 3932 O O   . HOH H 3 .   ? -4.446  14.126 28.569 1.00 40.10 ? 412 HOH B O   1 
HETATM 3933 O O   . HOH H 3 .   ? 18.620  23.540 24.860 1.00 22.87 ? 413 HOH B O   1 
HETATM 3934 O O   . HOH H 3 .   ? -0.200  4.013  27.752 1.00 40.12 ? 414 HOH B O   1 
HETATM 3935 O O   . HOH H 3 .   ? 0.956   10.006 18.037 1.00 31.66 ? 415 HOH B O   1 
HETATM 3936 O O   . HOH H 3 .   ? 35.064  4.540  25.544 1.00 28.10 ? 416 HOH B O   1 
HETATM 3937 O O   . HOH H 3 .   ? 39.577  2.611  19.303 1.00 44.79 ? 417 HOH B O   1 
HETATM 3938 O O   . HOH H 3 .   ? 15.923  24.475 25.655 1.00 39.21 ? 418 HOH B O   1 
HETATM 3939 O O   . HOH H 3 .   ? 21.956  -7.847 15.937 1.00 42.28 ? 419 HOH B O   1 
HETATM 3940 O O   . HOH H 3 .   ? -2.353  8.176  27.885 1.00 42.34 ? 420 HOH B O   1 
HETATM 3941 O O   . HOH H 3 .   ? 17.620  -6.373 10.755 1.00 45.32 ? 421 HOH B O   1 
HETATM 3942 O O   . HOH H 3 .   ? 36.266  6.789  25.533 1.00 33.02 ? 422 HOH B O   1 
HETATM 3943 O O   . HOH H 3 .   ? 18.481  18.373 4.498  1.00 36.56 ? 423 HOH B O   1 
HETATM 3944 O O   . HOH H 3 .   ? 17.133  22.355 5.270  1.00 33.98 ? 424 HOH B O   1 
HETATM 3945 O O   . HOH H 3 .   ? 24.225  28.647 18.133 1.00 27.54 ? 425 HOH B O   1 
HETATM 3946 O O   . HOH H 3 .   ? 10.752  14.055 2.436  1.00 34.23 ? 426 HOH B O   1 
HETATM 3947 O O   . HOH I 3 .   ? 28.556  48.796 9.301  1.00 43.52 ? 301 HOH C O   1 
HETATM 3948 O O   . HOH I 3 .   ? 40.538  30.347 3.068  1.00 40.69 ? 302 HOH C O   1 
HETATM 3949 O O   . HOH I 3 .   ? 22.158  38.935 25.451 1.00 27.47 ? 303 HOH C O   1 
HETATM 3950 O O   . HOH I 3 .   ? 26.398  47.488 6.556  1.00 42.45 ? 304 HOH C O   1 
HETATM 3951 O O   . HOH I 3 .   ? 27.354  54.001 16.358 1.00 29.09 ? 305 HOH C O   1 
HETATM 3952 O O   . HOH I 3 .   ? 39.195  13.014 15.457 1.00 37.21 ? 306 HOH C O   1 
HETATM 3953 O O   . HOH I 3 .   ? 49.721  27.915 24.541 1.00 28.43 ? 307 HOH C O   1 
HETATM 3954 O O   . HOH I 3 .   ? 38.787  54.238 3.178  1.00 31.99 ? 308 HOH C O   1 
HETATM 3955 O O   . HOH I 3 .   ? 40.199  15.932 22.637 1.00 34.35 ? 309 HOH C O   1 
HETATM 3956 O O   . HOH I 3 .   ? 50.626  33.029 18.376 1.00 22.61 ? 310 HOH C O   1 
HETATM 3957 O O   . HOH I 3 .   ? 40.176  54.631 20.611 1.00 31.81 ? 311 HOH C O   1 
HETATM 3958 O O   . HOH I 3 .   ? 33.863  59.146 0.350  1.00 37.22 ? 312 HOH C O   1 
HETATM 3959 O O   . HOH I 3 .   ? 37.015  29.869 4.304  1.00 18.45 ? 313 HOH C O   1 
HETATM 3960 O O   . HOH I 3 .   ? 31.682  24.128 21.798 1.00 30.03 ? 314 HOH C O   1 
HETATM 3961 O O   . HOH I 3 .   ? 18.379  31.012 15.616 1.00 31.37 ? 315 HOH C O   1 
HETATM 3962 O O   . HOH I 3 .   ? 26.129  48.328 10.957 1.00 33.82 ? 316 HOH C O   1 
HETATM 3963 O O   . HOH I 3 .   ? 33.346  18.762 13.633 1.00 16.53 ? 317 HOH C O   1 
HETATM 3964 O O   . HOH I 3 .   ? 51.890  36.677 22.635 1.00 24.87 ? 318 HOH C O   1 
HETATM 3965 O O   . HOH I 3 .   ? 45.903  26.366 16.429 1.00 46.82 ? 319 HOH C O   1 
HETATM 3966 O O   . HOH I 3 .   ? 46.033  37.104 -1.732 1.00 31.17 ? 320 HOH C O   1 
HETATM 3967 O O   . HOH I 3 .   ? 49.494  40.908 7.251  1.00 46.16 ? 321 HOH C O   1 
HETATM 3968 O O   . HOH I 3 .   ? 27.896  58.809 3.734  1.00 34.27 ? 322 HOH C O   1 
HETATM 3969 O O   . HOH I 3 .   ? 44.877  27.546 6.646  1.00 36.98 ? 323 HOH C O   1 
HETATM 3970 O O   . HOH I 3 .   ? 14.887  35.823 11.613 1.00 29.76 ? 324 HOH C O   1 
HETATM 3971 O O   . HOH I 3 .   ? 26.680  49.345 13.805 1.00 23.76 ? 325 HOH C O   1 
HETATM 3972 O O   . HOH I 3 .   ? 46.749  40.381 -3.695 1.00 24.37 ? 326 HOH C O   1 
HETATM 3973 O O   . HOH I 3 .   ? 42.124  50.978 22.671 1.00 37.39 ? 327 HOH C O   1 
HETATM 3974 O O   . HOH I 3 .   ? 21.571  46.244 15.578 1.00 17.54 ? 328 HOH C O   1 
HETATM 3975 O O   . HOH I 3 .   ? 32.288  27.144 2.845  1.00 34.17 ? 329 HOH C O   1 
HETATM 3976 O O   . HOH I 3 .   ? 34.776  35.549 8.159  1.00 17.52 ? 330 HOH C O   1 
HETATM 3977 O O   . HOH I 3 .   ? 44.406  43.292 0.636  1.00 35.20 ? 331 HOH C O   1 
HETATM 3978 O O   . HOH I 3 .   ? 23.915  36.818 0.863  1.00 39.24 ? 332 HOH C O   1 
HETATM 3979 O O   . HOH I 3 .   ? 27.105  26.121 2.340  1.00 41.25 ? 333 HOH C O   1 
HETATM 3980 O O   . HOH I 3 .   ? 47.495  48.612 12.572 1.00 41.94 ? 334 HOH C O   1 
HETATM 3981 O O   . HOH I 3 .   ? 31.138  41.737 7.263  1.00 26.53 ? 335 HOH C O   1 
HETATM 3982 O O   . HOH I 3 .   ? 33.873  25.018 10.266 1.00 16.47 ? 336 HOH C O   1 
HETATM 3983 O O   . HOH I 3 .   ? 43.814  42.287 -3.803 1.00 25.55 ? 337 HOH C O   1 
HETATM 3984 O O   . HOH I 3 .   ? 24.208  32.497 21.328 1.00 18.72 ? 338 HOH C O   1 
HETATM 3985 O O   . HOH I 3 .   ? 39.177  11.205 24.957 1.00 29.01 ? 339 HOH C O   1 
HETATM 3986 O O   . HOH I 3 .   ? 40.582  25.493 6.797  1.00 27.83 ? 340 HOH C O   1 
HETATM 3987 O O   . HOH I 3 .   ? 35.306  27.654 1.440  1.00 29.14 ? 341 HOH C O   1 
HETATM 3988 O O   . HOH I 3 .   ? 51.033  34.435 23.442 1.00 25.19 ? 342 HOH C O   1 
HETATM 3989 O O   . HOH I 3 .   ? 36.438  41.706 4.603  1.00 19.68 ? 343 HOH C O   1 
HETATM 3990 O O   . HOH I 3 .   ? 29.470  30.163 25.500 1.00 15.26 ? 344 HOH C O   1 
HETATM 3991 O O   . HOH I 3 .   ? 21.515  47.555 28.053 1.00 28.94 ? 345 HOH C O   1 
HETATM 3992 O O   . HOH I 3 .   ? 19.122  44.382 23.777 1.00 27.55 ? 346 HOH C O   1 
HETATM 3993 O O   . HOH I 3 .   ? 43.908  34.436 8.315  1.00 22.37 ? 347 HOH C O   1 
HETATM 3994 O O   . HOH I 3 .   ? 25.413  28.156 22.829 1.00 36.65 ? 348 HOH C O   1 
HETATM 3995 O O   . HOH I 3 .   ? 45.657  47.442 5.828  1.00 33.18 ? 349 HOH C O   1 
HETATM 3996 O O   . HOH I 3 .   ? 42.037  47.825 24.026 1.00 30.67 ? 350 HOH C O   1 
HETATM 3997 O O   . HOH I 3 .   ? 48.893  28.678 16.447 1.00 35.08 ? 351 HOH C O   1 
HETATM 3998 O O   . HOH I 3 .   ? 21.964  29.324 14.363 1.00 34.53 ? 352 HOH C O   1 
HETATM 3999 O O   . HOH I 3 .   ? 28.263  27.999 22.826 1.00 26.38 ? 353 HOH C O   1 
HETATM 4000 O O   . HOH I 3 .   ? 27.545  25.659 7.631  1.00 22.39 ? 354 HOH C O   1 
HETATM 4001 O O   . HOH I 3 .   ? 15.032  36.266 16.276 1.00 17.30 ? 355 HOH C O   1 
HETATM 4002 O O   . HOH I 3 .   ? 54.172  44.452 17.419 1.00 38.38 ? 356 HOH C O   1 
HETATM 4003 O O   . HOH I 3 .   ? 18.947  38.761 22.378 1.00 26.57 ? 357 HOH C O   1 
HETATM 4004 O O   . HOH I 3 .   ? 41.584  25.159 16.908 1.00 24.88 ? 358 HOH C O   1 
HETATM 4005 O O   . HOH I 3 .   ? 41.752  43.163 2.205  1.00 38.86 ? 359 HOH C O   1 
HETATM 4006 O O   . HOH I 3 .   ? 30.367  31.799 3.060  1.00 24.85 ? 360 HOH C O   1 
HETATM 4007 O O   . HOH I 3 .   ? 50.027  44.046 13.049 1.00 40.31 ? 361 HOH C O   1 
HETATM 4008 O O   . HOH I 3 .   ? 36.350  29.227 24.166 1.00 17.59 ? 362 HOH C O   1 
HETATM 4009 O O   . HOH I 3 .   ? 14.784  43.190 7.732  1.00 17.05 ? 363 HOH C O   1 
HETATM 4010 O O   . HOH I 3 .   ? 38.893  25.517 16.252 1.00 19.32 ? 364 HOH C O   1 
HETATM 4011 O O   . HOH I 3 .   ? 22.589  49.885 26.341 1.00 23.25 ? 365 HOH C O   1 
HETATM 4012 O O   . HOH I 3 .   ? 46.373  40.258 3.121  1.00 25.37 ? 366 HOH C O   1 
HETATM 4013 O O   . HOH I 3 .   ? 22.406  41.438 1.482  1.00 25.18 ? 367 HOH C O   1 
HETATM 4014 O O   . HOH I 3 .   ? 26.519  27.998 16.391 1.00 18.21 ? 368 HOH C O   1 
HETATM 4015 O O   . HOH I 3 .   ? 46.772  45.364 7.460  1.00 24.27 ? 369 HOH C O   1 
HETATM 4016 O O   . HOH I 3 .   ? 43.965  38.988 22.208 1.00 19.29 ? 370 HOH C O   1 
HETATM 4017 O O   . HOH I 3 .   ? 27.975  37.346 5.547  1.00 26.14 ? 371 HOH C O   1 
HETATM 4018 O O   . HOH I 3 .   ? 38.526  29.361 22.536 1.00 16.99 ? 372 HOH C O   1 
HETATM 4019 O O   . HOH I 3 .   ? 36.868  45.587 5.902  1.00 32.82 ? 373 HOH C O   1 
HETATM 4020 O O   . HOH I 3 .   ? 38.693  26.842 3.351  1.00 35.38 ? 374 HOH C O   1 
HETATM 4021 O O   . HOH I 3 .   ? 24.010  32.383 5.320  1.00 20.46 ? 375 HOH C O   1 
HETATM 4022 O O   . HOH I 3 .   ? 41.545  16.299 26.236 0.50 37.33 ? 376 HOH C O   1 
HETATM 4023 O O   . HOH I 3 .   ? 39.765  43.966 3.818  1.00 36.26 ? 377 HOH C O   1 
HETATM 4024 O O   . HOH I 3 .   ? 53.109  38.684 6.928  1.00 48.21 ? 378 HOH C O   1 
HETATM 4025 O O   . HOH I 3 .   ? 38.370  47.451 2.780  1.00 28.20 ? 379 HOH C O   1 
HETATM 4026 O O   . HOH I 3 .   ? 32.931  60.294 8.631  1.00 44.66 ? 380 HOH C O   1 
HETATM 4027 O O   . HOH I 3 .   ? 43.946  34.087 5.624  1.00 25.25 ? 381 HOH C O   1 
HETATM 4028 O O   . HOH I 3 .   ? 35.270  8.875  24.082 1.00 27.07 ? 382 HOH C O   1 
HETATM 4029 O O   . HOH I 3 .   ? 22.067  41.283 27.772 1.00 27.50 ? 383 HOH C O   1 
HETATM 4030 O O   . HOH I 3 .   ? 50.803  32.470 21.498 1.00 20.70 ? 384 HOH C O   1 
HETATM 4031 O O   . HOH I 3 .   ? 33.528  23.790 5.758  1.00 22.82 ? 385 HOH C O   1 
HETATM 4032 O O   . HOH I 3 .   ? 46.678  31.641 17.278 1.00 28.91 ? 386 HOH C O   1 
HETATM 4033 O O   . HOH I 3 .   ? 48.952  40.663 13.873 1.00 34.39 ? 387 HOH C O   1 
HETATM 4034 O O   . HOH I 3 .   ? 43.788  21.256 17.441 1.00 34.81 ? 388 HOH C O   1 
HETATM 4035 O O   . HOH I 3 .   ? 17.477  44.338 5.496  1.00 21.74 ? 389 HOH C O   1 
HETATM 4036 O O   . HOH I 3 .   ? 36.879  57.180 18.314 1.00 34.33 ? 390 HOH C O   1 
HETATM 4037 O O   . HOH I 3 .   ? 44.908  21.231 25.009 1.00 30.24 ? 391 HOH C O   1 
HETATM 4038 O O   . HOH I 3 .   ? 20.739  34.702 2.388  1.00 30.49 ? 392 HOH C O   1 
HETATM 4039 O O   . HOH I 3 .   ? 33.597  59.540 13.200 1.00 39.39 ? 393 HOH C O   1 
HETATM 4040 O O   . HOH I 3 .   ? 40.873  51.824 17.951 1.00 42.56 ? 394 HOH C O   1 
HETATM 4041 O O   . HOH I 3 .   ? 39.210  32.932 0.733  1.00 30.26 ? 395 HOH C O   1 
HETATM 4042 O O   . HOH I 3 .   ? 35.034  33.553 2.115  1.00 35.42 ? 396 HOH C O   1 
HETATM 4043 O O   . HOH I 3 .   ? 42.676  23.543 18.848 1.00 21.67 ? 397 HOH C O   1 
HETATM 4044 O O   . HOH I 3 .   ? 17.993  45.256 21.437 1.00 22.47 ? 398 HOH C O   1 
HETATM 4045 O O   . HOH I 3 .   ? 47.627  24.325 24.409 1.00 22.90 ? 399 HOH C O   1 
HETATM 4046 O O   . HOH I 3 .   ? 47.488  38.496 9.745  1.00 27.63 ? 400 HOH C O   1 
HETATM 4047 O O   . HOH I 3 .   ? 37.078  43.181 2.263  1.00 34.55 ? 401 HOH C O   1 
HETATM 4048 O O   . HOH I 3 .   ? 18.930  46.867 4.782  1.00 28.11 ? 402 HOH C O   1 
HETATM 4049 O O   . HOH I 3 .   ? 24.880  31.979 13.687 1.00 23.20 ? 403 HOH C O   1 
HETATM 4050 O O   . HOH I 3 .   ? 25.712  39.782 1.752  1.00 44.66 ? 404 HOH C O   1 
HETATM 4051 O O   . HOH I 3 .   ? 32.185  46.143 3.183  1.00 53.62 ? 405 HOH C O   1 
HETATM 4052 O O   . HOH I 3 .   ? 44.650  31.726 8.637  1.00 26.19 ? 406 HOH C O   1 
HETATM 4053 O O   . HOH I 3 .   ? 41.190  58.938 13.983 1.00 36.44 ? 407 HOH C O   1 
HETATM 4054 O O   . HOH I 3 .   ? 28.869  23.099 21.592 1.00 23.93 ? 408 HOH C O   1 
HETATM 4055 O O   . HOH I 3 .   ? 22.114  33.605 19.946 1.00 24.01 ? 409 HOH C O   1 
HETATM 4056 O O   . HOH I 3 .   ? 46.381  24.545 10.022 1.00 47.65 ? 410 HOH C O   1 
HETATM 4057 O O   . HOH I 3 .   ? 52.252  27.478 20.152 1.00 37.76 ? 411 HOH C O   1 
HETATM 4058 O O   . HOH I 3 .   ? 22.153  34.498 4.740  1.00 19.85 ? 412 HOH C O   1 
HETATM 4059 O O   . HOH I 3 .   ? 40.658  13.673 23.899 1.00 36.87 ? 413 HOH C O   1 
HETATM 4060 O O   . HOH I 3 .   ? 41.565  15.282 15.657 1.00 39.10 ? 414 HOH C O   1 
HETATM 4061 O O   . HOH I 3 .   ? 37.412  58.516 1.158  1.00 40.05 ? 415 HOH C O   1 
HETATM 4062 O O   . HOH I 3 .   ? 18.338  33.168 18.099 1.00 33.22 ? 416 HOH C O   1 
HETATM 4063 O O   . HOH I 3 .   ? 30.468  36.144 1.883  1.00 45.32 ? 417 HOH C O   1 
HETATM 4064 O O   . HOH I 3 .   ? 47.728  46.639 14.990 1.00 44.58 ? 418 HOH C O   1 
HETATM 4065 O O   . HOH I 3 .   ? 46.721  46.972 17.517 1.00 40.23 ? 419 HOH C O   1 
HETATM 4066 O O   . HOH I 3 .   ? 16.119  48.229 5.225  1.00 41.69 ? 420 HOH C O   1 
HETATM 4067 O O   . HOH I 3 .   ? 33.736  42.175 4.869  1.00 30.54 ? 421 HOH C O   1 
HETATM 4068 O O   . HOH I 3 .   ? 32.920  57.262 19.907 1.00 41.85 ? 422 HOH C O   1 
HETATM 4069 O O   . HOH I 3 .   ? 34.986  61.054 -2.474 1.00 46.81 ? 423 HOH C O   1 
HETATM 4070 O O   . HOH I 3 .   ? 14.405  34.354 14.374 1.00 30.78 ? 424 HOH C O   1 
HETATM 4071 O O   . HOH I 3 .   ? 43.415  31.406 5.002  1.00 29.80 ? 425 HOH C O   1 
HETATM 4072 O O   . HOH I 3 .   ? 48.461  46.612 9.260  1.00 36.28 ? 426 HOH C O   1 
HETATM 4073 O O   . HOH I 3 .   ? 44.596  41.707 22.874 1.00 28.24 ? 427 HOH C O   1 
HETATM 4074 O O   . HOH I 3 .   ? 28.731  54.242 18.569 1.00 33.47 ? 428 HOH C O   1 
HETATM 4075 O O   . HOH I 3 .   ? 26.591  27.814 9.124  1.00 34.33 ? 429 HOH C O   1 
HETATM 4076 O O   . HOH I 3 .   ? 48.137  41.240 5.166  1.00 36.40 ? 430 HOH C O   1 
HETATM 4077 O O   . HOH I 3 .   ? 24.784  29.823 20.706 1.00 22.06 ? 431 HOH C O   1 
HETATM 4078 O O   . HOH I 3 .   ? 15.705  42.988 2.736  1.00 47.71 ? 432 HOH C O   1 
HETATM 4079 O O   . HOH I 3 .   ? 42.340  47.327 0.738  1.00 45.39 ? 433 HOH C O   1 
HETATM 4080 O O   . HOH I 3 .   ? 37.074  31.589 2.183  1.00 31.06 ? 434 HOH C O   1 
HETATM 4081 O O   . HOH I 3 .   ? 39.065  56.887 20.484 1.00 43.61 ? 435 HOH C O   1 
HETATM 4082 O O   . HOH I 3 .   ? 52.771  30.009 21.740 1.00 42.32 ? 436 HOH C O   1 
HETATM 4083 O O   . HOH I 3 .   ? 23.685  32.248 24.029 1.00 22.78 ? 437 HOH C O   1 
HETATM 4084 O O   . HOH I 3 .   ? 32.250  55.789 21.909 1.00 27.96 ? 438 HOH C O   1 
HETATM 4085 O O   . HOH I 3 .   ? 43.891  17.157 26.556 1.00 43.34 ? 439 HOH C O   1 
HETATM 4086 O O   . HOH I 3 .   ? 24.234  29.630 24.815 1.00 34.45 ? 440 HOH C O   1 
HETATM 4087 O O   . HOH I 3 .   ? 46.787  42.549 1.809  1.00 39.79 ? 441 HOH C O   1 
HETATM 4088 O O   . HOH I 3 .   ? 48.505  38.075 12.595 1.00 44.57 ? 442 HOH C O   1 
HETATM 4089 O O   . HOH I 3 .   ? 43.353  22.863 15.227 1.00 33.02 ? 443 HOH C O   1 
HETATM 4090 O O   . HOH I 3 .   ? 47.632  21.817 24.987 1.00 40.79 ? 444 HOH C O   1 
HETATM 4091 O O   . HOH I 3 .   ? 48.369  43.811 5.816  1.00 39.40 ? 445 HOH C O   1 
HETATM 4092 O O   . HOH I 3 .   ? 57.176  41.130 20.464 1.00 47.63 ? 446 HOH C O   1 
HETATM 4093 O O   . HOH I 3 .   ? 45.274  30.319 6.598  1.00 31.98 ? 447 HOH C O   1 
HETATM 4094 O O   . HOH I 3 .   ? 52.279  33.655 25.838 1.00 30.38 ? 448 HOH C O   1 
HETATM 4095 O O   . HOH I 3 .   ? 29.592  55.810 22.332 1.00 29.24 ? 449 HOH C O   1 
HETATM 4096 O O   . HOH I 3 .   ? 54.423  37.417 23.326 1.00 28.79 ? 450 HOH C O   1 
HETATM 4097 O O   . HOH I 3 .   ? 44.779  45.883 0.040  1.00 36.06 ? 451 HOH C O   1 
HETATM 4098 O O   . HOH I 3 .   ? 36.487  30.039 0.141  1.00 39.72 ? 452 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   ? 0.7882 0.6199 0.3639 0.0908  0.0923  0.1769  25  HIS A N   
2    C CA  . HIS A 8   ? 0.6806 0.5197 0.3415 0.0661  0.0911  0.2122  25  HIS A CA  
3    C C   . HIS A 8   ? 0.5518 0.5785 0.3235 0.0690  0.0687  0.1610  25  HIS A C   
4    O O   . HIS A 8   ? 0.5829 0.5862 0.3302 0.1360  0.0539  0.1860  25  HIS A O   
5    C CB  . HIS A 8   ? 0.7324 0.6261 0.3465 0.1403  0.0731  0.1894  25  HIS A CB  
6    N N   . VAL A 9   ? 0.3832 0.5021 0.3071 -0.0392 0.0242  0.1088  26  VAL A N   
7    C CA  . VAL A 9   ? 0.3121 0.3445 0.2745 -0.0661 0.0071  0.1146  26  VAL A CA  
8    C C   . VAL A 9   ? 0.2506 0.2779 0.2469 -0.0195 -0.0258 0.0749  26  VAL A C   
9    O O   . VAL A 9   ? 0.3144 0.3049 0.2618 0.0113  -0.0291 0.0688  26  VAL A O   
10   C CB  . VAL A 9   ? 0.3788 0.3597 0.2797 -0.0350 0.0109  0.0600  26  VAL A CB  
11   C CG1 . VAL A 9   ? 0.3827 0.3978 0.2975 -0.0244 0.0219  -0.0013 26  VAL A CG1 
12   C CG2 . VAL A 9   ? 0.3888 0.4018 0.2723 -0.0944 0.0388  0.1096  26  VAL A CG2 
13   N N   . GLU A 10  ? 0.2468 0.2332 0.2135 0.0196  -0.0140 0.0615  27  GLU A N   
14   C CA  . GLU A 10  ? 0.2614 0.2682 0.2017 -0.0105 -0.0271 0.0596  27  GLU A CA  
15   C C   . GLU A 10  ? 0.1706 0.1926 0.1750 0.0367  -0.0558 0.0317  27  GLU A C   
16   O O   . GLU A 10  ? 0.1592 0.2322 0.1748 0.0473  -0.0130 0.0232  27  GLU A O   
17   C CB  . GLU A 10  ? 0.3257 0.3061 0.2168 -0.0073 -0.0128 0.0115  27  GLU A CB  
18   C CG  . GLU A 10  ? 0.3293 0.3254 0.2169 0.0240  -0.0347 -0.0044 27  GLU A CG  
19   C CD  . GLU A 10  ? 0.3588 0.3780 0.2201 -0.0392 -0.0554 0.0178  27  GLU A CD  
20   O OE1 . GLU A 10  ? 0.6134 0.3467 0.2493 0.0625  -0.0855 0.0335  27  GLU A OE1 
21   O OE2 . GLU A 10  ? 0.2563 0.3035 0.2066 0.0084  -0.0353 0.0416  27  GLU A OE2 
22   N N   . GLN A 11  ? 0.1999 0.2197 0.1678 0.0141  -0.0391 0.0470  28  GLN A N   
23   C CA  . GLN A 11  ? 0.2235 0.2174 0.1820 0.0340  -0.0290 0.0273  28  GLN A CA  
24   C C   . GLN A 11  ? 0.2264 0.1965 0.1624 0.0434  -0.0393 0.0000  28  GLN A C   
25   O O   . GLN A 11  ? 0.2362 0.2388 0.1778 0.0296  -0.0405 0.0134  28  GLN A O   
26   C CB  . GLN A 11  ? 0.2480 0.1965 0.1945 -0.0030 -0.0151 0.0165  28  GLN A CB  
27   C CG  . GLN A 11  ? 0.2565 0.2537 0.2184 -0.0138 -0.0154 -0.0082 28  GLN A CG  
28   C CD  . GLN A 11  ? 0.2644 0.3058 0.2297 -0.0075 -0.0240 -0.0126 28  GLN A CD  
29   O OE1 . GLN A 11  ? 0.3650 0.3348 0.2438 -0.0342 0.0107  -0.0237 28  GLN A OE1 
30   N NE2 . GLN A 11  ? 0.3046 0.2648 0.2351 -0.0039 -0.0007 0.0305  28  GLN A NE2 
31   N N   . THR A 12  ? 0.1865 0.2063 0.1423 0.0369  -0.0248 0.0113  29  THR A N   
32   C CA  . THR A 12  ? 0.1789 0.2493 0.1547 -0.0041 -0.0224 -0.0140 29  THR A CA  
33   C C   . THR A 12  ? 0.1807 0.2366 0.1615 0.0209  -0.0243 -0.0008 29  THR A C   
34   O O   . THR A 12  ? 0.1867 0.2134 0.1703 0.0192  -0.0329 0.0006  29  THR A O   
35   C CB  . THR A 12  ? 0.1750 0.2380 0.1684 0.0186  -0.0236 0.0019  29  THR A CB  
36   O OG1 . THR A 12  ? 0.1917 0.2689 0.1803 0.0090  -0.0048 0.0030  29  THR A OG1 
37   C CG2 . THR A 12  ? 0.1570 0.2380 0.1729 0.0050  -0.0096 -0.0350 29  THR A CG2 
38   N N   . TYR A 13  ? 0.1851 0.2288 0.1587 0.0251  -0.0127 0.0405  30  TYR A N   
39   C CA  . TYR A 13  ? 0.1729 0.2263 0.1481 0.0427  -0.0276 0.0140  30  TYR A CA  
40   C C   . TYR A 13  ? 0.1727 0.2388 0.1436 0.0320  -0.0113 0.0126  30  TYR A C   
41   O O   . TYR A 13  ? 0.1972 0.2505 0.1508 0.0447  -0.0198 -0.0074 30  TYR A O   
42   C CB  . TYR A 13  ? 0.1742 0.2182 0.1505 0.0131  -0.0233 0.0043  30  TYR A CB  
43   C CG  . TYR A 13  ? 0.1622 0.1890 0.1548 0.0229  -0.0246 -0.0083 30  TYR A CG  
44   C CD1 . TYR A 13  ? 0.1645 0.2376 0.1620 0.0203  0.0017  -0.0240 30  TYR A CD1 
45   C CD2 . TYR A 13  ? 0.1758 0.2113 0.1607 0.0030  -0.0458 -0.0108 30  TYR A CD2 
46   C CE1 . TYR A 13  ? 0.1669 0.2520 0.1686 0.0047  -0.0032 -0.0145 30  TYR A CE1 
47   C CE2 . TYR A 13  ? 0.1838 0.2136 0.1774 0.0353  -0.0114 0.0018  30  TYR A CE2 
48   C CZ  . TYR A 13  ? 0.1340 0.2291 0.1739 0.0422  0.0165  0.0182  30  TYR A CZ  
49   O OH  . TYR A 13  ? 0.1755 0.2962 0.1905 0.0337  0.0078  0.0109  30  TYR A OH  
50   N N   . LEU A 14  ? 0.1896 0.1974 0.1385 -0.0100 -0.0266 0.0045  31  LEU A N   
51   C CA  . LEU A 14  ? 0.1669 0.2003 0.1515 0.0157  -0.0028 0.0202  31  LEU A CA  
52   C C   . LEU A 14  ? 0.1954 0.2094 0.1638 0.0343  -0.0068 -0.0023 31  LEU A C   
53   O O   . LEU A 14  ? 0.2304 0.2367 0.1762 0.0196  0.0037  -0.0107 31  LEU A O   
54   C CB  . LEU A 14  ? 0.1902 0.2220 0.1649 0.0338  -0.0010 0.0016  31  LEU A CB  
55   C CG  . LEU A 14  ? 0.2034 0.2235 0.1879 0.0061  -0.0082 -0.0010 31  LEU A CG  
56   C CD1 . LEU A 14  ? 0.2378 0.3081 0.1870 -0.0160 -0.0133 -0.0376 31  LEU A CD1 
57   C CD2 . LEU A 14  ? 0.2596 0.2891 0.2068 -0.0459 -0.0108 -0.0246 31  LEU A CD2 
58   N N   . MET A 15  ? 0.1621 0.2117 0.1687 0.0376  0.0245  0.0050  32  MET A N   
59   C CA  . MET A 15  ? 0.1546 0.1927 0.1677 0.0434  0.0232  0.0068  32  MET A CA  
60   C C   . MET A 15  ? 0.1818 0.1656 0.1510 0.0346  0.0008  -0.0081 32  MET A C   
61   O O   . MET A 15  ? 0.2006 0.2028 0.1483 0.0378  -0.0111 -0.0048 32  MET A O   
62   C CB  . MET A 15  ? 0.1753 0.2284 0.1800 0.0612  0.0055  0.0364  32  MET A CB  
63   C CG  . MET A 15  ? 0.1929 0.2115 0.1910 -0.0126 -0.0322 0.0152  32  MET A CG  
64   S SD  . MET A 15  ? 0.2139 0.2816 0.2231 0.0172  -0.0307 0.0008  32  MET A SD  
65   C CE  . MET A 15  ? 0.2333 0.3324 0.2342 0.0000  -0.0048 -0.0430 32  MET A CE  
66   N N   . ILE A 16  ? 0.1543 0.1887 0.1426 0.0287  -0.0206 0.0080  33  ILE A N   
67   C CA  . ILE A 16  ? 0.1347 0.2205 0.1438 0.0379  -0.0043 -0.0049 33  ILE A CA  
68   C C   . ILE A 16  ? 0.1306 0.1934 0.1493 -0.0222 -0.0104 -0.0093 33  ILE A C   
69   O O   . ILE A 16  ? 0.1503 0.2210 0.1563 0.0259  0.0235  0.0012  33  ILE A O   
70   C CB  . ILE A 16  ? 0.1546 0.2374 0.1546 -0.0057 -0.0014 0.0096  33  ILE A CB  
71   C CG1 . ILE A 16  ? 0.1868 0.2204 0.1606 0.0211  -0.0034 0.0061  33  ILE A CG1 
72   C CG2 . ILE A 16  ? 0.2145 0.1687 0.1548 0.0071  0.0186  0.0203  33  ILE A CG2 
73   C CD1 . ILE A 16  ? 0.2539 0.1983 0.1596 0.0264  -0.0073 -0.0054 33  ILE A CD1 
74   N N   . LYS A 17  ? 0.1571 0.2082 0.1577 0.0006  -0.0294 -0.0073 34  LYS A N   
75   C CA  . LYS A 17  ? 0.1517 0.1878 0.1583 0.0042  -0.0089 -0.0076 34  LYS A CA  
76   C C   . LYS A 17  ? 0.1577 0.1906 0.1579 -0.0021 -0.0183 0.0066  34  LYS A C   
77   O O   . LYS A 17  ? 0.1607 0.1867 0.1600 0.0129  -0.0045 0.0034  34  LYS A O   
78   C CB  . LYS A 17  ? 0.1511 0.2391 0.1581 0.0224  -0.0145 -0.0105 34  LYS A CB  
79   C CG  . LYS A 17  ? 0.1943 0.2242 0.1558 0.0174  -0.0211 -0.0183 34  LYS A CG  
80   C CD  . LYS A 17  ? 0.1728 0.2077 0.1526 0.0073  -0.0082 -0.0098 34  LYS A CD  
81   C CE  . LYS A 17  ? 0.2746 0.2986 0.1463 0.0586  -0.0033 -0.0027 34  LYS A CE  
82   N NZ  . LYS A 17  ? 0.2862 0.3598 0.1569 0.1151  -0.0158 -0.0483 34  LYS A NZ  
83   N N   . PRO A 18  ? 0.1711 0.2087 0.1522 -0.0258 -0.0109 -0.0013 35  PRO A N   
84   C CA  . PRO A 18  ? 0.1902 0.2268 0.1606 0.0135  0.0074  0.0275  35  PRO A CA  
85   C C   . PRO A 18  ? 0.1573 0.1949 0.1488 -0.0114 -0.0028 -0.0040 35  PRO A C   
86   O O   . PRO A 18  ? 0.1969 0.2223 0.1375 0.0127  0.0131  0.0009  35  PRO A O   
87   C CB  . PRO A 18  ? 0.1920 0.2238 0.1641 0.0010  -0.0057 0.0402  35  PRO A CB  
88   C CG  . PRO A 18  ? 0.2015 0.2036 0.1571 -0.0132 0.0065  0.0166  35  PRO A CG  
89   C CD  . PRO A 18  ? 0.1870 0.1968 0.1550 -0.0266 0.0057  -0.0062 35  PRO A CD  
90   N N   . ASP A 19  ? 0.2222 0.2065 0.1488 0.0456  0.0132  -0.0135 36  ASP A N   
91   C CA  . ASP A 19  ? 0.1966 0.1898 0.1544 0.0305  0.0103  -0.0223 36  ASP A CA  
92   C C   . ASP A 19  ? 0.2077 0.1997 0.1538 0.0434  0.0114  -0.0150 36  ASP A C   
93   O O   . ASP A 19  ? 0.2032 0.2060 0.1545 0.0233  0.0040  -0.0021 36  ASP A O   
94   C CB  . ASP A 19  ? 0.2082 0.2436 0.1560 0.0337  0.0420  -0.0003 36  ASP A CB  
95   C CG  . ASP A 19  ? 0.1869 0.2287 0.1677 0.0206  0.0380  -0.0041 36  ASP A CG  
96   O OD1 . ASP A 19  ? 0.2491 0.2295 0.1799 0.0527  0.0196  -0.0149 36  ASP A OD1 
97   O OD2 . ASP A 19  ? 0.1870 0.2025 0.1668 0.0323  0.0176  0.0030  36  ASP A OD2 
98   N N   . GLY A 20  ? 0.2166 0.1870 0.1479 0.0302  0.0123  -0.0263 37  GLY A N   
99   C CA  . GLY A 20  ? 0.1672 0.2089 0.1569 0.0241  0.0266  -0.0058 37  GLY A CA  
100  C C   . GLY A 20  ? 0.1809 0.2052 0.1727 0.0367  0.0096  -0.0052 37  GLY A C   
101  O O   . GLY A 20  ? 0.1709 0.2264 0.1840 0.0289  0.0241  0.0202  37  GLY A O   
102  N N   . ILE A 21  ? 0.1766 0.1885 0.1758 0.0347  0.0168  -0.0104 38  ILE A N   
103  C CA  . ILE A 21  ? 0.2023 0.1621 0.1655 0.0216  0.0304  -0.0121 38  ILE A CA  
104  C C   . ILE A 21  ? 0.1782 0.2195 0.1487 0.0439  0.0082  -0.0107 38  ILE A C   
105  O O   . ILE A 21  ? 0.1523 0.2366 0.1578 0.0157  0.0091  0.0045  38  ILE A O   
106  C CB  . ILE A 21  ? 0.1678 0.2144 0.1596 0.0259  0.0363  0.0150  38  ILE A CB  
107  C CG1 . ILE A 21  ? 0.2131 0.2220 0.1708 0.0264  0.0024  -0.0067 38  ILE A CG1 
108  C CG2 . ILE A 21  ? 0.2203 0.2762 0.1653 0.0423  0.0469  0.0345  38  ILE A CG2 
109  C CD1 . ILE A 21  ? 0.2586 0.2935 0.1831 0.0616  -0.0177 -0.0054 38  ILE A CD1 
110  N N   . GLN A 22  ? 0.2056 0.1886 0.1450 0.0083  0.0072  -0.0112 39  GLN A N   
111  C CA  . GLN A 22  ? 0.1794 0.1881 0.1499 0.0268  0.0026  -0.0051 39  GLN A CA  
112  C C   . GLN A 22  ? 0.1682 0.2474 0.1530 0.0196  0.0134  0.0092  39  GLN A C   
113  O O   . GLN A 22  ? 0.2023 0.2229 0.1733 -0.0040 0.0180  0.0019  39  GLN A O   
114  C CB  . GLN A 22  ? 0.2049 0.2218 0.1619 0.0080  0.0029  -0.0152 39  GLN A CB  
115  C CG  . GLN A 22  ? 0.1953 0.2668 0.1653 0.0080  0.0364  -0.0147 39  GLN A CG  
116  C CD  . GLN A 22  ? 0.1465 0.3441 0.1828 -0.0523 0.0042  0.0015  39  GLN A CD  
117  O OE1 . GLN A 22  ? 0.2079 0.3503 0.1867 0.0175  -0.0159 0.0340  39  GLN A OE1 
118  N NE2 . GLN A 22  ? 0.1828 0.2957 0.2057 -0.0341 0.0060  0.0178  39  GLN A NE2 
119  N N   . ARG A 23  ? 0.2025 0.2014 0.1491 0.0124  0.0204  0.0234  40  ARG A N   
120  C CA  . ARG A 23  ? 0.1631 0.2236 0.1473 0.0459  0.0073  0.0259  40  ARG A CA  
121  C C   . ARG A 23  ? 0.1856 0.2356 0.1642 0.0296  0.0281  0.0125  40  ARG A C   
122  O O   . ARG A 23  ? 0.1995 0.2733 0.1719 0.0199  0.0026  -0.0065 40  ARG A O   
123  C CB  . ARG A 23  ? 0.2047 0.2128 0.1553 0.0237  0.0060  0.0125  40  ARG A CB  
124  C CG  . ARG A 23  ? 0.2009 0.2023 0.1582 0.0054  0.0048  0.0213  40  ARG A CG  
125  C CD  . ARG A 23  ? 0.2278 0.2655 0.1551 0.0531  0.0010  0.0007  40  ARG A CD  
126  N NE  . ARG A 23  ? 0.1976 0.2918 0.1537 0.0582  0.0367  -0.0147 40  ARG A NE  
127  C CZ  . ARG A 23  ? 0.1777 0.2684 0.1529 0.0492  0.0258  0.0010  40  ARG A CZ  
128  N NH1 . ARG A 23  ? 0.2003 0.2900 0.1696 0.0764  -0.0050 0.0153  40  ARG A NH1 
129  N NH2 . ARG A 23  ? 0.1992 0.3326 0.1577 0.0517  0.0105  -0.0042 40  ARG A NH2 
130  N N   . GLN A 24  ? 0.1789 0.2021 0.1650 0.0498  0.0071  0.0034  41  GLN A N   
131  C CA  . GLN A 24  ? 0.1940 0.2402 0.1534 -0.0036 0.0255  -0.0092 41  GLN A CA  
132  C C   . GLN A 24  ? 0.1887 0.2210 0.1592 0.0182  0.0223  -0.0010 41  GLN A C   
133  O O   . GLN A 24  ? 0.1692 0.2713 0.1584 -0.0038 0.0267  -0.0050 41  GLN A O   
134  C CB  . GLN A 24  ? 0.2342 0.2352 0.1444 0.0051  0.0380  0.0206  41  GLN A CB  
135  C CG  . GLN A 24  ? 0.2193 0.3050 0.1364 0.0198  0.0304  0.0348  41  GLN A CG  
136  C CD  . GLN A 24  ? 0.2078 0.2756 0.1518 0.0374  0.0227  0.0149  41  GLN A CD  
137  O OE1 . GLN A 24  ? 0.2432 0.2631 0.1586 -0.0137 -0.0074 0.0576  41  GLN A OE1 
138  N NE2 . GLN A 24  ? 0.1852 0.3169 0.1560 0.0335  0.0259  -0.0249 41  GLN A NE2 
139  N N   . VAL A 25  ? 0.1824 0.2060 0.1606 0.0216  0.0253  0.0033  42  VAL A N   
140  C CA  . VAL A 25  ? 0.1799 0.1976 0.1687 -0.0156 0.0088  -0.0078 42  VAL A CA  
141  C C   . VAL A 25  ? 0.1435 0.1730 0.1470 -0.0010 0.0024  0.0000  42  VAL A C   
142  O O   . VAL A 25  ? 0.1945 0.2172 0.1431 0.0105  0.0201  -0.0045 42  VAL A O   
143  C CB  . VAL A 25  ? 0.2009 0.1886 0.1799 -0.0089 0.0098  -0.0089 42  VAL A CB  
144  C CG1 . VAL A 25  ? 0.1906 0.2526 0.1901 0.0244  0.0334  -0.0025 42  VAL A CG1 
145  C CG2 . VAL A 25  ? 0.2340 0.1961 0.1608 0.0085  0.0066  -0.0112 42  VAL A CG2 
146  N N   . VAL A 26  ? 0.1360 0.2257 0.1405 0.0544  0.0021  0.0001  43  VAL A N   
147  C CA  . VAL A 26  ? 0.1539 0.2145 0.1463 0.0704  0.0076  -0.0018 43  VAL A CA  
148  C C   . VAL A 26  ? 0.1502 0.2180 0.1374 0.0610  -0.0062 0.0099  43  VAL A C   
149  O O   . VAL A 26  ? 0.1571 0.2190 0.1300 0.0321  0.0154  0.0370  43  VAL A O   
150  C CB  . VAL A 26  ? 0.1562 0.2054 0.1484 -0.0018 0.0131  -0.0039 43  VAL A CB  
151  C CG1 . VAL A 26  ? 0.1861 0.2147 0.1477 0.0313  0.0270  0.0104  43  VAL A CG1 
152  C CG2 . VAL A 26  ? 0.1622 0.2402 0.1546 0.0423  0.0093  -0.0092 43  VAL A CG2 
153  N N   . GLY A 27  ? 0.1424 0.1943 0.1388 0.0251  0.0002  0.0096  44  GLY A N   
154  C CA  . GLY A 27  ? 0.1442 0.2232 0.1376 0.0361  0.0057  -0.0114 44  GLY A CA  
155  C C   . GLY A 27  ? 0.1699 0.1818 0.1363 0.0293  0.0076  0.0049  44  GLY A C   
156  O O   . GLY A 27  ? 0.1728 0.1889 0.1351 0.0061  0.0081  0.0104  44  GLY A O   
157  N N   . GLU A 28  ? 0.1476 0.2086 0.1494 0.0280  0.0155  0.0338  45  GLU A N   
158  C CA  . GLU A 28  ? 0.1436 0.1998 0.1601 0.0049  0.0275  0.0159  45  GLU A CA  
159  C C   . GLU A 28  ? 0.1428 0.1847 0.1383 0.0229  0.0144  0.0064  45  GLU A C   
160  O O   . GLU A 28  ? 0.1703 0.2183 0.1321 0.0319  0.0033  0.0142  45  GLU A O   
161  C CB  . GLU A 28  ? 0.1707 0.1946 0.1827 0.0310  0.0180  0.0321  45  GLU A CB  
162  C CG  . GLU A 28  ? 0.2038 0.2426 0.2049 0.0445  0.0197  0.0335  45  GLU A CG  
163  C CD  . GLU A 28  ? 0.4014 0.3578 0.2414 0.1974  0.0179  0.0237  45  GLU A CD  
164  O OE1 . GLU A 28  ? 0.4662 0.4254 0.2563 0.1832  -0.0099 -0.0440 45  GLU A OE1 
165  O OE2 . GLU A 28  ? 0.4561 0.4556 0.2668 0.1571  0.0199  0.0278  45  GLU A OE2 
166  N N   . ILE A 29  ? 0.1689 0.1747 0.1331 -0.0025 0.0267  0.0220  46  ILE A N   
167  C CA  . ILE A 29  ? 0.1631 0.2095 0.1290 0.0180  0.0159  0.0089  46  ILE A CA  
168  C C   . ILE A 29  ? 0.1723 0.2262 0.1286 0.0183  -0.0010 -0.0004 46  ILE A C   
169  O O   . ILE A 29  ? 0.1973 0.2159 0.1439 0.0212  0.0027  0.0071  46  ILE A O   
170  C CB  . ILE A 29  ? 0.1876 0.1567 0.1399 0.0186  0.0094  0.0099  46  ILE A CB  
171  C CG1 . ILE A 29  ? 0.1879 0.2110 0.1647 0.0431  0.0226  0.0031  46  ILE A CG1 
172  C CG2 . ILE A 29  ? 0.2008 0.2321 0.1467 0.0250  -0.0024 0.0077  46  ILE A CG2 
173  C CD1 . ILE A 29  ? 0.1978 0.1965 0.1664 0.0301  -0.0002 -0.0028 46  ILE A CD1 
174  N N   . ILE A 30  ? 0.1708 0.2220 0.1335 0.0144  0.0030  -0.0073 47  ILE A N   
175  C CA  . ILE A 30  ? 0.1732 0.1940 0.1325 0.0139  0.0202  0.0008  47  ILE A CA  
176  C C   . ILE A 30  ? 0.1580 0.2009 0.1361 0.0302  0.0229  0.0320  47  ILE A C   
177  O O   . ILE A 30  ? 0.1744 0.2052 0.1448 0.0171  0.0060  0.0202  47  ILE A O   
178  C CB  . ILE A 30  ? 0.1288 0.1971 0.1393 0.0273  0.0216  0.0140  47  ILE A CB  
179  C CG1 . ILE A 30  ? 0.1752 0.1871 0.1456 0.0406  0.0056  0.0219  47  ILE A CG1 
180  C CG2 . ILE A 30  ? 0.1733 0.2057 0.1430 0.0400  -0.0117 0.0026  47  ILE A CG2 
181  C CD1 . ILE A 30  ? 0.1672 0.1748 0.1477 0.0309  -0.0044 -0.0096 47  ILE A CD1 
182  N N   . SER A 31  ? 0.1673 0.2169 0.1254 0.0162  0.0114  0.0225  48  SER A N   
183  C CA  . SER A 31  ? 0.1755 0.2034 0.1342 0.0324  0.0154  0.0329  48  SER A CA  
184  C C   . SER A 31  ? 0.1377 0.2321 0.1435 0.0249  0.0005  0.0117  48  SER A C   
185  O O   . SER A 31  ? 0.1564 0.2290 0.1503 0.0094  0.0166  0.0029  48  SER A O   
186  C CB  . SER A 31  ? 0.1473 0.2034 0.1300 0.0035  0.0313  0.0295  48  SER A CB  
187  O OG  . SER A 31  ? 0.1650 0.2376 0.1242 0.0353  0.0326  0.0222  48  SER A OG  
188  N N   . ARG A 32  ? 0.1830 0.2051 0.1451 0.0423  0.0108  0.0119  49  ARG A N   
189  C CA  . ARG A 32  ? 0.1725 0.2273 0.1499 0.0366  0.0094  0.0177  49  ARG A CA  
190  C C   . ARG A 32  ? 0.1487 0.1737 0.1444 0.0232  0.0203  0.0172  49  ARG A C   
191  O O   . ARG A 32  ? 0.1646 0.2441 0.1456 0.0309  0.0394  0.0326  49  ARG A O   
192  C CB  . ARG A 32  ? 0.2243 0.2302 0.1568 0.0649  -0.0010 0.0397  49  ARG A CB  
193  C CG  . ARG A 32  ? 0.2693 0.2157 0.1753 0.0503  -0.0094 0.0036  49  ARG A CG  
194  C CD  . ARG A 32  ? 0.3916 0.2870 0.2144 0.1082  -0.0507 -0.0110 49  ARG A CD  
195  N NE  . ARG A 32  ? 0.3540 0.3019 0.2307 0.0516  -0.0507 -0.0078 49  ARG A NE  
196  C CZ  . ARG A 32  ? 0.2809 0.2392 0.2332 0.0455  -0.0269 -0.0114 49  ARG A CZ  
197  N NH1 . ARG A 32  ? 0.2577 0.2839 0.2313 0.0517  -0.0357 -0.0051 49  ARG A NH1 
198  N NH2 . ARG A 32  ? 0.3340 0.2264 0.2499 0.0327  -0.0287 0.0081  49  ARG A NH2 
199  N N   . PHE A 33  ? 0.1762 0.2013 0.1458 0.0627  0.0225  0.0113  50  PHE A N   
200  C CA  . PHE A 33  ? 0.1845 0.1882 0.1486 0.0603  0.0133  0.0354  50  PHE A CA  
201  C C   . PHE A 33  ? 0.1935 0.1971 0.1437 0.0269  0.0018  -0.0003 50  PHE A C   
202  O O   . PHE A 33  ? 0.2052 0.2007 0.1453 0.0306  0.0074  0.0161  50  PHE A O   
203  C CB  . PHE A 33  ? 0.1876 0.1727 0.1470 0.0599  0.0216  0.0070  50  PHE A CB  
204  C CG  . PHE A 33  ? 0.1764 0.2284 0.1433 0.0315  0.0327  0.0061  50  PHE A CG  
205  C CD1 . PHE A 33  ? 0.2332 0.2555 0.1441 -0.0250 0.0327  0.0273  50  PHE A CD1 
206  C CD2 . PHE A 33  ? 0.1895 0.2817 0.1441 0.0051  -0.0113 0.0139  50  PHE A CD2 
207  C CE1 . PHE A 33  ? 0.2068 0.3202 0.1500 0.0402  0.0149  0.0156  50  PHE A CE1 
208  C CE2 . PHE A 33  ? 0.2566 0.2281 0.1425 -0.0257 -0.0124 0.0317  50  PHE A CE2 
209  C CZ  . PHE A 33  ? 0.2012 0.2377 0.1477 0.0286  0.0035  0.0171  50  PHE A CZ  
210  N N   . GLU A 34  ? 0.1828 0.1909 0.1418 0.0066  0.0090  0.0113  51  GLU A N   
211  C CA  . GLU A 34  ? 0.1775 0.1919 0.1396 0.0385  0.0017  0.0035  51  GLU A CA  
212  C C   . GLU A 34  ? 0.1843 0.2129 0.1484 0.0514  0.0072  0.0017  51  GLU A C   
213  O O   . GLU A 34  ? 0.2004 0.2021 0.1457 0.0332  0.0209  0.0143  51  GLU A O   
214  C CB  . GLU A 34  ? 0.1776 0.2559 0.1314 0.0163  0.0110  -0.0050 51  GLU A CB  
215  C CG  . GLU A 34  ? 0.1886 0.1796 0.1293 0.0073  0.0330  0.0053  51  GLU A CG  
216  C CD  . GLU A 34  ? 0.1950 0.2120 0.1414 -0.0060 0.0275  0.0188  51  GLU A CD  
217  O OE1 . GLU A 34  ? 0.1978 0.2201 0.1514 -0.0017 0.0181  0.0143  51  GLU A OE1 
218  O OE2 . GLU A 34  ? 0.2089 0.2153 0.1504 0.0518  0.0128  0.0232  51  GLU A OE2 
219  N N   . LYS A 35  ? 0.1575 0.2255 0.1551 0.0259  -0.0031 0.0210  52  LYS A N   
220  C CA  . LYS A 35  ? 0.1620 0.2005 0.1598 0.0064  0.0195  -0.0015 52  LYS A CA  
221  C C   . LYS A 35  ? 0.1216 0.1964 0.1544 0.0114  0.0089  -0.0059 52  LYS A C   
222  O O   . LYS A 35  ? 0.1459 0.2114 0.1579 0.0051  0.0200  0.0239  52  LYS A O   
223  C CB  . LYS A 35  ? 0.2184 0.1825 0.1772 0.0172  0.0542  -0.0134 52  LYS A CB  
224  C CG  . LYS A 35  ? 0.2500 0.2913 0.2001 0.0613  0.0523  0.0143  52  LYS A CG  
225  C CD  . LYS A 35  ? 0.3307 0.4019 0.2253 0.1132  0.0311  0.0312  52  LYS A CD  
226  C CE  . LYS A 35  ? 0.3301 0.4817 0.2388 0.0804  -0.0139 0.0218  52  LYS A CE  
227  N NZ  . LYS A 35  ? 0.3988 0.5244 0.2429 0.0429  -0.0321 0.0685  52  LYS A NZ  
228  N N   . ARG A 36  ? 0.1574 0.2268 0.1515 0.0261  -0.0225 0.0031  53  ARG A N   
229  C CA  . ARG A 36  ? 0.1748 0.2303 0.1456 0.0323  0.0026  0.0223  53  ARG A CA  
230  C C   . ARG A 36  ? 0.1690 0.2265 0.1516 0.0538  0.0230  0.0232  53  ARG A C   
231  O O   . ARG A 36  ? 0.2081 0.1869 0.1566 0.0057  0.0119  0.0299  53  ARG A O   
232  C CB  . ARG A 36  ? 0.1311 0.2706 0.1429 0.0356  -0.0058 -0.0136 53  ARG A CB  
233  C CG  . ARG A 36  ? 0.2303 0.1876 0.1380 0.0453  0.0157  0.0006  53  ARG A CG  
234  C CD  . ARG A 36  ? 0.2410 0.2107 0.1363 0.0345  0.0320  0.0352  53  ARG A CD  
235  N NE  . ARG A 36  ? 0.2050 0.1666 0.1409 0.0294  0.0053  -0.0078 53  ARG A NE  
236  C CZ  . ARG A 36  ? 0.1834 0.2514 0.1518 0.0172  0.0055  -0.0144 53  ARG A CZ  
237  N NH1 . ARG A 36  ? 0.2192 0.2300 0.1555 0.0075  0.0020  0.0004  53  ARG A NH1 
238  N NH2 . ARG A 36  ? 0.1874 0.2748 0.1578 0.0038  0.0026  0.0005  53  ARG A NH2 
239  N N   . GLY A 37  ? 0.1621 0.2061 0.1624 0.0404  0.0073  0.0095  54  GLY A N   
240  C CA  . GLY A 37  ? 0.1306 0.2593 0.1651 0.0336  -0.0132 0.0039  54  GLY A CA  
241  C C   . GLY A 37  ? 0.1560 0.2154 0.1619 -0.0169 -0.0141 0.0087  54  GLY A C   
242  O O   . GLY A 37  ? 0.2254 0.2180 0.1795 0.0189  -0.0025 -0.0048 54  GLY A O   
243  N N   . TYR A 38  ? 0.1227 0.2233 0.1545 0.0037  -0.0026 0.0068  55  TYR A N   
244  C CA  . TYR A 38  ? 0.1360 0.1862 0.1423 0.0051  -0.0223 -0.0032 55  TYR A CA  
245  C C   . TYR A 38  ? 0.2091 0.1982 0.1312 0.0343  0.0072  0.0097  55  TYR A C   
246  O O   . TYR A 38  ? 0.2037 0.2086 0.1401 0.0422  0.0183  0.0358  55  TYR A O   
247  C CB  . TYR A 38  ? 0.1627 0.2364 0.1494 0.0045  -0.0072 -0.0032 55  TYR A CB  
248  C CG  . TYR A 38  ? 0.2029 0.1808 0.1404 0.0297  0.0053  0.0088  55  TYR A CG  
249  C CD1 . TYR A 38  ? 0.2158 0.2115 0.1423 0.0445  -0.0110 -0.0049 55  TYR A CD1 
250  C CD2 . TYR A 38  ? 0.1719 0.2135 0.1347 0.0318  0.0192  0.0054  55  TYR A CD2 
251  C CE1 . TYR A 38  ? 0.1731 0.2388 0.1392 0.0085  0.0096  0.0177  55  TYR A CE1 
252  C CE2 . TYR A 38  ? 0.1728 0.1720 0.1420 0.0131  0.0245  0.0118  55  TYR A CE2 
253  C CZ  . TYR A 38  ? 0.1924 0.2132 0.1354 0.0195  0.0115  0.0113  55  TYR A CZ  
254  O OH  . TYR A 38  ? 0.2271 0.2429 0.1441 0.0469  0.0242  -0.0002 55  TYR A OH  
255  N N   . ARG A 39  ? 0.2118 0.1881 0.1287 0.0369  0.0122  -0.0137 56  ARG A N   
256  C CA  . ARG A 39  ? 0.1703 0.2074 0.1484 0.0427  -0.0147 -0.0006 56  ARG A CA  
257  C C   . ARG A 39  ? 0.2053 0.1837 0.1465 0.0601  -0.0235 0.0096  56  ARG A C   
258  O O   . ARG A 39  ? 0.1770 0.1997 0.1515 0.0080  -0.0188 0.0055  56  ARG A O   
259  C CB  . ARG A 39  ? 0.1885 0.1888 0.1585 0.0488  -0.0170 0.0206  56  ARG A CB  
260  C CG  . ARG A 39  ? 0.1587 0.2387 0.1474 0.0060  -0.0075 0.0016  56  ARG A CG  
261  C CD  . ARG A 39  ? 0.1909 0.1880 0.1461 0.0149  0.0123  0.0099  56  ARG A CD  
262  N NE  . ARG A 39  ? 0.2014 0.2249 0.1460 0.0239  0.0058  -0.0119 56  ARG A NE  
263  C CZ  . ARG A 39  ? 0.2404 0.1949 0.1516 0.0066  -0.0186 0.0057  56  ARG A CZ  
264  N NH1 . ARG A 39  ? 0.2314 0.2809 0.1502 0.0168  0.0021  -0.0008 56  ARG A NH1 
265  N NH2 . ARG A 39  ? 0.2800 0.2495 0.1661 0.0456  -0.0312 -0.0030 56  ARG A NH2 
266  N N   . ILE A 40  ? 0.1710 0.1850 0.1480 0.0316  -0.0190 0.0125  57  ILE A N   
267  C CA  . ILE A 40  ? 0.1448 0.1735 0.1508 0.0331  0.0020  0.0364  57  ILE A CA  
268  C C   . ILE A 40  ? 0.1890 0.1846 0.1648 0.0210  -0.0085 0.0341  57  ILE A C   
269  O O   . ILE A 40  ? 0.1760 0.2105 0.1752 0.0218  -0.0208 -0.0013 57  ILE A O   
270  C CB  . ILE A 40  ? 0.1767 0.1489 0.1680 0.0459  0.0039  0.0420  57  ILE A CB  
271  C CG1 . ILE A 40  ? 0.1993 0.2085 0.1741 0.0407  -0.0085 0.0447  57  ILE A CG1 
272  C CG2 . ILE A 40  ? 0.1779 0.2056 0.1755 -0.0064 -0.0045 0.0145  57  ILE A CG2 
273  C CD1 . ILE A 40  ? 0.2054 0.1979 0.1765 0.0388  -0.0334 0.0581  57  ILE A CD1 
274  N N   . ALA A 41  ? 0.1840 0.1931 0.1630 0.0257  0.0015  0.0188  58  ALA A N   
275  C CA  . ALA A 41  ? 0.1897 0.1719 0.1703 0.0133  -0.0037 -0.0039 58  ALA A CA  
276  C C   . ALA A 41  ? 0.1793 0.2030 0.1789 0.0548  0.0003  -0.0236 58  ALA A C   
277  O O   . ALA A 41  ? 0.1839 0.1886 0.1980 0.0533  0.0121  -0.0111 58  ALA A O   
278  C CB  . ALA A 41  ? 0.2062 0.1756 0.1780 0.0246  0.0074  0.0081  58  ALA A CB  
279  N N   . ALA A 42  ? 0.1605 0.1814 0.1693 0.0324  -0.0002 -0.0085 59  ALA A N   
280  C CA  . ALA A 42  ? 0.1727 0.1825 0.1651 0.0364  -0.0165 -0.0169 59  ALA A CA  
281  C C   . ALA A 42  ? 0.1749 0.2077 0.1664 0.0188  0.0001  -0.0052 59  ALA A C   
282  O O   . ALA A 42  ? 0.1771 0.1764 0.1709 0.0163  -0.0110 -0.0131 59  ALA A O   
283  C CB  . ALA A 42  ? 0.2118 0.1993 0.1584 -0.0096 -0.0109 0.0046  59  ALA A CB  
284  N N   . MET A 43  ? 0.1887 0.2254 0.1545 0.0361  -0.0152 -0.0311 60  MET A N   
285  C CA  . MET A 43  ? 0.2053 0.1818 0.1645 0.0439  -0.0095 0.0119  60  MET A CA  
286  C C   . MET A 43  ? 0.2282 0.2052 0.1714 0.0331  -0.0085 0.0113  60  MET A C   
287  O O   . MET A 43  ? 0.2205 0.2104 0.1808 0.0060  0.0030  -0.0232 60  MET A O   
288  C CB  . MET A 43  ? 0.2303 0.1830 0.1603 0.0603  -0.0244 -0.0348 60  MET A CB  
289  C CG  . MET A 43  ? 0.2320 0.2610 0.1696 0.0325  -0.0130 -0.0421 60  MET A CG  
290  S SD  . MET A 43  ? 0.2556 0.2393 0.1827 0.0649  -0.0260 -0.0127 60  MET A SD  
291  C CE  . MET A 43  ? 0.2918 0.2446 0.1821 0.0177  -0.0400 -0.0124 60  MET A CE  
292  N N   . LYS A 44  ? 0.1672 0.1852 0.1744 -0.0194 -0.0077 -0.0042 61  LYS A N   
293  C CA  . LYS A 44  ? 0.1853 0.2267 0.2007 0.0103  -0.0010 0.0169  61  LYS A CA  
294  C C   . LYS A 44  ? 0.1579 0.2449 0.1831 0.0252  0.0186  0.0153  61  LYS A C   
295  O O   . LYS A 44  ? 0.2284 0.2292 0.1713 0.0029  0.0340  -0.0016 61  LYS A O   
296  C CB  . LYS A 44  ? 0.1310 0.3130 0.2430 0.0578  0.0212  0.0411  61  LYS A CB  
297  C CG  . LYS A 44  ? 0.2662 0.3618 0.2621 0.0362  -0.0280 0.0243  61  LYS A CG  
298  C CD  . LYS A 44  ? 0.2347 0.4181 0.2752 0.0935  -0.0393 0.0095  61  LYS A CD  
299  C CE  . LYS A 44  ? 0.1905 0.3709 0.2866 0.0768  -0.0093 0.0060  61  LYS A CE  
300  N NZ  . LYS A 44  ? 0.1949 0.2877 0.2938 0.0303  -0.0155 0.0103  61  LYS A NZ  
301  N N   . LEU A 45  ? 0.1809 0.1961 0.1755 0.0305  -0.0086 0.0017  62  LEU A N   
302  C CA  . LEU A 45  ? 0.1860 0.2050 0.1770 0.0103  -0.0089 -0.0138 62  LEU A CA  
303  C C   . LEU A 45  ? 0.1839 0.1818 0.1763 -0.0148 -0.0128 -0.0242 62  LEU A C   
304  O O   . LEU A 45  ? 0.1640 0.2688 0.1767 0.0220  0.0141  -0.0272 62  LEU A O   
305  C CB  . LEU A 45  ? 0.1615 0.2122 0.1701 -0.0337 -0.0116 0.0050  62  LEU A CB  
306  C CG  . LEU A 45  ? 0.1801 0.2782 0.1685 0.0261  -0.0183 0.0025  62  LEU A CG  
307  C CD1 . LEU A 45  ? 0.1669 0.2635 0.1692 0.0414  -0.0013 0.0269  62  LEU A CD1 
308  C CD2 . LEU A 45  ? 0.2182 0.2326 0.1785 0.0338  -0.0034 0.0374  62  LEU A CD2 
309  N N   . THR A 46  ? 0.1461 0.2337 0.1773 0.0247  0.0191  -0.0203 63  THR A N   
310  C CA  . THR A 46  ? 0.1678 0.1980 0.1921 -0.0211 0.0094  -0.0066 63  THR A CA  
311  C C   . THR A 46  ? 0.1771 0.2386 0.1941 -0.0003 0.0242  0.0047  63  THR A C   
312  O O   . THR A 46  ? 0.1837 0.2515 0.2024 0.0342  0.0138  -0.0008 63  THR A O   
313  C CB  . THR A 46  ? 0.1647 0.2843 0.2006 0.0538  -0.0093 -0.0328 63  THR A CB  
314  O OG1 . THR A 46  ? 0.1710 0.3173 0.2182 0.0495  -0.0043 -0.0207 63  THR A OG1 
315  C CG2 . THR A 46  ? 0.1922 0.2586 0.1985 0.0736  -0.0071 0.0141  63  THR A CG2 
316  N N   . ILE A 47  ? 0.1872 0.2094 0.1933 -0.0203 0.0218  -0.0520 64  ILE A N   
317  C CA  . ILE A 47  ? 0.1780 0.2667 0.2053 0.0211  0.0160  -0.0398 64  ILE A CA  
318  C C   . ILE A 47  ? 0.1397 0.2468 0.2080 0.0396  0.0127  -0.0509 64  ILE A C   
319  O O   . ILE A 47  ? 0.1884 0.2975 0.2292 0.0467  -0.0065 -0.0770 64  ILE A O   
320  C CB  . ILE A 47  ? 0.1533 0.2888 0.2152 -0.0052 -0.0002 -0.0528 64  ILE A CB  
321  C CG1 . ILE A 47  ? 0.1979 0.2760 0.2186 -0.0134 0.0229  -0.0369 64  ILE A CG1 
322  C CG2 . ILE A 47  ? 0.2355 0.3015 0.2230 -0.0637 0.0515  -0.0367 64  ILE A CG2 
323  C CD1 . ILE A 47  ? 0.2360 0.3298 0.2345 -0.0356 0.0660  -0.0291 64  ILE A CD1 
324  N N   . ALA A 48  ? 0.1756 0.2448 0.1907 0.0401  0.0318  -0.0333 65  ALA A N   
325  C CA  . ALA A 48  ? 0.1697 0.2453 0.2063 0.0013  0.0217  0.0099  65  ALA A CA  
326  C C   . ALA A 48  ? 0.1612 0.2650 0.2254 0.0173  0.0012  0.0265  65  ALA A C   
327  O O   . ALA A 48  ? 0.2147 0.3023 0.2611 0.0177  -0.0139 -0.0035 65  ALA A O   
328  C CB  . ALA A 48  ? 0.2077 0.2308 0.1970 0.0175  0.0248  0.0087  65  ALA A CB  
329  N N   . THR A 49  ? 0.1727 0.2344 0.2226 0.0215  -0.0222 0.0262  66  THR A N   
330  C CA  . THR A 49  ? 0.1329 0.2970 0.2262 -0.0034 -0.0159 -0.0056 66  THR A CA  
331  C C   . THR A 49  ? 0.1668 0.3071 0.2221 0.0076  -0.0168 -0.0170 66  THR A C   
332  O O   . THR A 49  ? 0.1709 0.3085 0.2235 -0.0156 0.0029  -0.0068 66  THR A O   
333  C CB  . THR A 49  ? 0.1455 0.3009 0.2406 0.0595  -0.0258 -0.0204 66  THR A CB  
334  O OG1 . THR A 49  ? 0.1896 0.3102 0.2578 0.0179  -0.0167 -0.0095 66  THR A OG1 
335  C CG2 . THR A 49  ? 0.1891 0.3150 0.2521 0.0194  -0.0338 -0.0333 66  THR A CG2 
336  N N   . PRO A 50  ? 0.1533 0.2845 0.2191 -0.0107 -0.0039 -0.0131 67  PRO A N   
337  C CA  . PRO A 50  ? 0.2271 0.2773 0.2182 -0.0148 0.0184  -0.0001 67  PRO A CA  
338  C C   . PRO A 50  ? 0.1724 0.2901 0.2177 0.0094  0.0268  -0.0053 67  PRO A C   
339  O O   . PRO A 50  ? 0.1954 0.3370 0.2043 -0.0087 0.0057  -0.0458 67  PRO A O   
340  C CB  . PRO A 50  ? 0.2523 0.3209 0.2199 -0.0546 0.0125  -0.0152 67  PRO A CB  
341  C CG  . PRO A 50  ? 0.2661 0.3255 0.2213 -0.0416 0.0047  -0.0316 67  PRO A CG  
342  C CD  . PRO A 50  ? 0.1912 0.3444 0.2171 -0.0406 0.0036  -0.0210 67  PRO A CD  
343  N N   . ALA A 51  ? 0.1338 0.3022 0.2261 0.0148  -0.0091 -0.0189 68  ALA A N   
344  C CA  . ALA A 51  ? 0.1342 0.3454 0.2298 0.0546  0.0005  -0.0100 68  ALA A CA  
345  C C   . ALA A 51  ? 0.1782 0.2958 0.2293 -0.0143 -0.0119 -0.0513 68  ALA A C   
346  O O   . ALA A 51  ? 0.2160 0.3141 0.2436 0.0099  0.0036  -0.0166 68  ALA A O   
347  C CB  . ALA A 51  ? 0.1323 0.4463 0.2470 0.0652  0.0119  -0.0274 68  ALA A CB  
348  N N   . ILE A 52  ? 0.1478 0.2619 0.2323 -0.0023 -0.0004 -0.0237 69  ILE A N   
349  C CA  A ILE A 52  ? 0.1607 0.2838 0.2288 -0.0140 -0.0092 -0.0507 69  ILE A CA  
350  C CA  B ILE A 52  ? 0.1774 0.2592 0.2341 0.0082  -0.0196 -0.0621 69  ILE A CA  
351  C C   . ILE A 52  ? 0.1907 0.2777 0.2234 0.0253  -0.0196 -0.0486 69  ILE A C   
352  O O   . ILE A 52  ? 0.1957 0.2332 0.2343 0.0180  -0.0217 -0.0247 69  ILE A O   
353  C CB  A ILE A 52  ? 0.2289 0.3800 0.2298 0.0057  -0.0026 -0.0723 69  ILE A CB  
354  C CB  B ILE A 52  ? 0.2659 0.3043 0.2451 0.0345  -0.0359 -0.1024 69  ILE A CB  
355  C CG1 A ILE A 52  ? 0.2561 0.4886 0.2354 -0.0309 0.0121  -0.0993 69  ILE A CG1 
356  C CG1 B ILE A 52  ? 0.2775 0.3343 0.2476 0.0590  -0.0724 -0.1043 69  ILE A CG1 
357  C CG2 A ILE A 52  ? 0.2120 0.3923 0.2215 0.0168  -0.0154 -0.0624 69  ILE A CG2 
358  C CG2 B ILE A 52  ? 0.3051 0.4096 0.2517 -0.0007 -0.0293 -0.1254 69  ILE A CG2 
359  C CD1 A ILE A 52  ? 0.2802 0.5351 0.2380 0.0071  0.0117  -0.1038 69  ILE A CD1 
360  C CD1 B ILE A 52  ? 0.3449 0.3678 0.2499 0.0047  -0.0988 -0.1151 69  ILE A CD1 
361  N N   . LEU A 53  ? 0.1639 0.2477 0.2130 0.0105  0.0058  -0.0150 70  LEU A N   
362  C CA  . LEU A 53  ? 0.2177 0.1913 0.2078 0.0380  0.0171  -0.0173 70  LEU A CA  
363  C C   . LEU A 53  ? 0.1981 0.2794 0.2088 -0.0316 0.0002  0.0052  70  LEU A C   
364  O O   . LEU A 53  ? 0.1862 0.3085 0.2101 -0.0078 0.0253  -0.0085 70  LEU A O   
365  C CB  . LEU A 53  ? 0.1942 0.2333 0.2079 -0.0275 0.0079  -0.0357 70  LEU A CB  
366  C CG  . LEU A 53  ? 0.1388 0.2697 0.2233 -0.0279 0.0095  -0.0238 70  LEU A CG  
367  C CD1 . LEU A 53  ? 0.1976 0.2480 0.2253 0.0143  0.0058  -0.0343 70  LEU A CD1 
368  C CD2 . LEU A 53  ? 0.1632 0.3273 0.2282 0.0039  0.0053  -0.0372 70  LEU A CD2 
369  N N   . GLU A 54  ? 0.1852 0.3062 0.2162 -0.0352 -0.0312 -0.0218 71  GLU A N   
370  C CA  A GLU A 54  ? 0.1927 0.3553 0.2291 -0.0236 -0.0270 -0.0051 71  GLU A CA  
371  C CA  B GLU A 54  ? 0.1621 0.3717 0.2286 -0.0241 -0.0401 -0.0199 71  GLU A CA  
372  C C   . GLU A 54  ? 0.1955 0.3306 0.2255 -0.0321 -0.0197 -0.0004 71  GLU A C   
373  O O   . GLU A 54  ? 0.2263 0.3976 0.2119 -0.0282 -0.0043 0.0029  71  GLU A O   
374  C CB  A GLU A 54  ? 0.2585 0.4419 0.2452 -0.0126 -0.0272 0.0148  71  GLU A CB  
375  C CB  B GLU A 54  ? 0.2350 0.5088 0.2455 -0.0300 -0.0590 -0.0159 71  GLU A CB  
376  C CG  A GLU A 54  ? 0.2752 0.5061 0.2620 -0.0137 -0.0207 0.0334  71  GLU A CG  
377  C CG  B GLU A 54  ? 0.1939 0.6186 0.2654 -0.0738 -0.0481 -0.0071 71  GLU A CG  
378  C CD  A GLU A 54  ? 0.3028 0.5702 0.2778 -0.0102 -0.0118 0.0502  71  GLU A CD  
379  C CD  B GLU A 54  ? 0.2898 0.8132 0.2822 0.0326  -0.0552 0.0136  71  GLU A CD  
380  O OE1 A GLU A 54  ? 0.3284 0.6163 0.2887 0.0337  0.0005  0.0481  71  GLU A OE1 
381  O OE1 B GLU A 54  ? 0.3312 0.8920 0.2988 0.0717  -0.0243 0.0309  71  GLU A OE1 
382  O OE2 A GLU A 54  ? 0.3156 0.5742 0.2840 -0.0179 -0.0125 0.0584  71  GLU A OE2 
383  O OE2 B GLU A 54  ? 0.3757 0.8620 0.2895 0.0700  -0.0840 0.0130  71  GLU A OE2 
384  N N   . GLU A 55  ? 0.1858 0.2842 0.2332 -0.0120 -0.0178 0.0042  72  GLU A N   
385  C CA  . GLU A 55  ? 0.2192 0.2965 0.2598 -0.0034 -0.0175 0.0023  72  GLU A CA  
386  C C   . GLU A 55  ? 0.2209 0.2890 0.2529 0.0140  -0.0421 0.0108  72  GLU A C   
387  O O   . GLU A 55  ? 0.2796 0.2930 0.2608 0.0384  -0.0127 0.0294  72  GLU A O   
388  C CB  . GLU A 55  ? 0.2411 0.4557 0.2896 0.0281  -0.0040 0.0169  72  GLU A CB  
389  C CG  . GLU A 55  ? 0.4208 0.6679 0.3194 0.0937  -0.0290 0.0440  72  GLU A CG  
390  C CD  . GLU A 55  ? 0.6340 0.9001 0.3478 0.3281  -0.0319 0.0574  72  GLU A CD  
391  O OE1 . GLU A 55  ? 0.6986 0.9463 0.3681 0.3790  -0.0774 0.0373  72  GLU A OE1 
392  O OE2 . GLU A 55  ? 0.7493 0.9784 0.3592 0.3344  -0.0209 0.0420  72  GLU A OE2 
393  N N   . HIS A 56  ? 0.2057 0.2976 0.2399 0.0072  -0.0309 -0.0130 73  HIS A N   
394  C CA  . HIS A 56  ? 0.2417 0.2417 0.2258 0.0360  -0.0194 -0.0112 73  HIS A CA  
395  C C   . HIS A 56  ? 0.2475 0.2450 0.2159 -0.0348 0.0075  0.0325  73  HIS A C   
396  O O   . HIS A 56  ? 0.2204 0.3339 0.2272 -0.0381 0.0113  0.0716  73  HIS A O   
397  C CB  . HIS A 56  ? 0.2084 0.2535 0.2339 0.0138  -0.0324 0.0032  73  HIS A CB  
398  C CG  . HIS A 56  ? 0.1409 0.2526 0.2401 0.0218  -0.0370 -0.0228 73  HIS A CG  
399  N ND1 . HIS A 56  ? 0.1685 0.3306 0.2432 0.0025  -0.0582 -0.0227 73  HIS A ND1 
400  C CD2 . HIS A 56  ? 0.2211 0.3416 0.2539 0.0680  -0.0496 -0.0303 73  HIS A CD2 
401  C CE1 . HIS A 56  ? 0.1770 0.3718 0.2503 0.0214  -0.0228 -0.0193 73  HIS A CE1 
402  N NE2 . HIS A 56  ? 0.1985 0.3631 0.2572 0.0224  -0.0260 -0.0340 73  HIS A NE2 
403  N N   . TYR A 57  ? 0.2505 0.2666 0.2038 0.0084  -0.0135 0.0021  74  TYR A N   
404  C CA  . TYR A 57  ? 0.2746 0.2560 0.2034 0.0257  0.0030  -0.0177 74  TYR A CA  
405  C C   . TYR A 57  ? 0.2846 0.3106 0.2143 0.0030  0.0000  0.0001  74  TYR A C   
406  O O   . TYR A 57  ? 0.2849 0.3712 0.2132 -0.0403 -0.0160 -0.0344 74  TYR A O   
407  C CB  . TYR A 57  ? 0.2733 0.3007 0.2068 0.0482  -0.0064 -0.0440 74  TYR A CB  
408  C CG  . TYR A 57  ? 0.1920 0.3370 0.2022 -0.0190 -0.0013 -0.0198 74  TYR A CG  
409  C CD1 . TYR A 57  ? 0.2764 0.4279 0.2065 0.0017  -0.0055 -0.0295 74  TYR A CD1 
410  C CD2 . TYR A 57  ? 0.3266 0.3831 0.2131 0.0645  -0.0012 -0.0173 74  TYR A CD2 
411  C CE1 . TYR A 57  ? 0.2864 0.4328 0.2088 0.0459  0.0005  -0.0235 74  TYR A CE1 
412  C CE2 . TYR A 57  ? 0.3342 0.3575 0.2218 0.0657  -0.0068 0.0240  74  TYR A CE2 
413  C CZ  . TYR A 57  ? 0.3861 0.4577 0.2273 0.1301  -0.0178 0.0297  74  TYR A CZ  
414  O OH  . TYR A 57  ? 0.4878 0.5260 0.2458 0.2218  -0.0353 0.0470  74  TYR A OH  
415  N N   . ALA A 58  ? 0.2971 0.3495 0.2223 -0.0215 -0.0058 0.0312  75  ALA A N   
416  C CA  . ALA A 58  ? 0.3436 0.4235 0.2259 0.0758  -0.0166 0.0516  75  ALA A CA  
417  C C   . ALA A 58  ? 0.4065 0.4261 0.2323 0.0650  -0.0377 0.0199  75  ALA A C   
418  O O   . ALA A 58  ? 0.4064 0.4637 0.2290 0.0112  -0.0721 0.0170  75  ALA A O   
419  C CB  . ALA A 58  ? 0.3389 0.5336 0.2330 0.1056  -0.0253 0.0796  75  ALA A CB  
420  N N   . GLU A 59  ? 0.3616 0.4600 0.2364 0.0332  -0.0255 0.0156  76  GLU A N   
421  C CA  . GLU A 59  ? 0.3114 0.4915 0.2442 -0.0540 -0.0106 0.0023  76  GLU A CA  
422  C C   . GLU A 59  ? 0.3291 0.5114 0.2403 -0.0155 -0.0262 -0.0031 76  GLU A C   
423  O O   . GLU A 59  ? 0.3665 0.5681 0.2320 0.0252  -0.0315 -0.0215 76  GLU A O   
424  C CB  . GLU A 59  ? 0.4339 0.5664 0.2661 -0.0921 0.0110  0.0130  76  GLU A CB  
425  C CG  . GLU A 59  ? 0.4400 0.5332 0.2919 -0.2111 0.0065  0.0099  76  GLU A CG  
426  C CD  . GLU A 59  ? 0.5425 0.6785 0.3126 -0.1703 0.0188  0.0193  76  GLU A CD  
427  O OE1 . GLU A 59  ? 0.5565 0.7027 0.3290 -0.1155 0.0236  0.0085  76  GLU A OE1 
428  O OE2 . GLU A 59  ? 0.5728 0.7501 0.3205 -0.1671 0.0082  0.0274  76  GLU A OE2 
429  N N   . HIS A 60  ? 0.3093 0.4382 0.2472 -0.0610 -0.0105 0.0218  77  HIS A N   
430  C CA  . HIS A 60  ? 0.3190 0.5127 0.2600 0.0169  -0.0321 0.0184  77  HIS A CA  
431  C C   . HIS A 60  ? 0.3166 0.5318 0.2794 0.0388  -0.0069 0.0187  77  HIS A C   
432  O O   . HIS A 60  ? 0.3593 0.5241 0.2791 0.0911  0.0012  -0.0013 77  HIS A O   
433  C CB  . HIS A 60  ? 0.2960 0.4907 0.2557 0.0175  -0.0417 0.0272  77  HIS A CB  
434  C CG  . HIS A 60  ? 0.3104 0.5137 0.2666 0.0268  -0.0263 0.0389  77  HIS A CG  
435  N ND1 . HIS A 60  ? 0.2993 0.4827 0.2740 -0.0411 -0.0408 0.0386  77  HIS A ND1 
436  C CD2 . HIS A 60  ? 0.2825 0.5461 0.2756 -0.0291 -0.0143 0.0583  77  HIS A CD2 
437  C CE1 . HIS A 60  ? 0.3203 0.5252 0.2770 -0.0406 -0.0321 0.0421  77  HIS A CE1 
438  N NE2 . HIS A 60  ? 0.3252 0.5104 0.2819 -0.0788 -0.0173 0.0551  77  HIS A NE2 
439  N N   . LYS A 61  ? 0.2721 0.5109 0.3076 -0.0220 -0.0230 0.0044  78  LYS A N   
440  C CA  . LYS A 61  ? 0.3322 0.6074 0.3474 -0.0357 -0.0179 0.0054  78  LYS A CA  
441  C C   . LYS A 61  ? 0.3450 0.6332 0.3560 -0.0332 -0.0357 -0.0217 78  LYS A C   
442  O O   . LYS A 61  ? 0.3505 0.5863 0.3670 -0.0429 -0.0514 -0.0485 78  LYS A O   
443  C CB  . LYS A 61  ? 0.4264 0.7248 0.3792 0.0937  -0.0047 0.0158  78  LYS A CB  
444  C CG  . LYS A 61  ? 0.5614 0.8235 0.4027 0.1624  -0.0130 0.0049  78  LYS A CG  
445  C CD  . LYS A 61  ? 0.6733 0.9014 0.4208 0.2174  -0.0245 0.0035  78  LYS A CD  
446  C CE  . LYS A 61  ? 0.7777 0.9657 0.4358 0.2676  -0.0367 -0.0001 78  LYS A CE  
447  N NZ  . LYS A 61  ? 0.8684 1.0200 0.4416 0.2773  -0.0430 0.0034  78  LYS A NZ  
448  N N   . GLY A 62  ? 0.3477 0.6633 0.3569 -0.0946 -0.0576 -0.0645 79  GLY A N   
449  C CA  . GLY A 62  ? 0.3882 0.6719 0.3568 -0.1274 -0.0558 -0.1054 79  GLY A CA  
450  C C   . GLY A 62  ? 0.3820 0.6592 0.3636 -0.2152 -0.0401 -0.1289 79  GLY A C   
451  O O   . GLY A 62  ? 0.4253 0.6605 0.3772 -0.2209 -0.0439 -0.1492 79  GLY A O   
452  N N   . LYS A 63  ? 0.4437 0.6550 0.3481 -0.2067 -0.0533 -0.1465 80  LYS A N   
453  C CA  . LYS A 63  ? 0.4951 0.6217 0.3321 -0.2235 -0.0254 -0.1524 80  LYS A CA  
454  C C   . LYS A 63  ? 0.5680 0.5532 0.3137 -0.1232 -0.0302 -0.1602 80  LYS A C   
455  O O   . LYS A 63  ? 0.5872 0.4725 0.3047 -0.0898 -0.0173 -0.1564 80  LYS A O   
456  C CB  . LYS A 63  ? 0.5668 0.6577 0.3421 -0.2321 0.0185  -0.1268 80  LYS A CB  
457  C CG  . LYS A 63  ? 0.5910 0.6828 0.3480 -0.2874 0.0440  -0.1225 80  LYS A CG  
458  C CD  . LYS A 63  ? 0.6231 0.7282 0.3532 -0.2689 0.0664  -0.0993 80  LYS A CD  
459  C CE  . LYS A 63  ? 0.6427 0.7966 0.3575 -0.2206 0.0976  -0.0636 80  LYS A CE  
460  N NZ  . LYS A 63  ? 0.6620 0.7818 0.3666 -0.1978 0.1004  -0.0570 80  LYS A NZ  
461  N N   . PRO A 64  ? 0.6106 0.5161 0.3003 -0.1037 -0.0251 -0.1718 81  PRO A N   
462  C CA  . PRO A 64  ? 0.6551 0.5439 0.3011 -0.0928 -0.0431 -0.1575 81  PRO A CA  
463  C C   . PRO A 64  ? 0.7222 0.5579 0.3032 -0.0282 -0.0560 -0.1442 81  PRO A C   
464  O O   . PRO A 64  ? 0.7703 0.5253 0.3033 -0.0337 -0.0524 -0.1339 81  PRO A O   
465  C CB  . PRO A 64  ? 0.6679 0.4610 0.3013 -0.0809 -0.0249 -0.1573 81  PRO A CB  
466  C CG  . PRO A 64  ? 0.6067 0.5027 0.2940 -0.0224 -0.0114 -0.1592 81  PRO A CG  
467  C CD  . PRO A 64  ? 0.6191 0.5532 0.2920 -0.0115 -0.0095 -0.1562 81  PRO A CD  
468  N N   . PHE A 65  ? 0.6949 0.5651 0.3074 0.0031  -0.0763 -0.1346 82  PHE A N   
469  C CA  . PHE A 65  ? 0.7028 0.5435 0.3163 0.0523  -0.0872 -0.1254 82  PHE A CA  
470  C C   . PHE A 65  ? 0.6818 0.4146 0.3009 0.0400  -0.1232 -0.1362 82  PHE A C   
471  O O   . PHE A 65  ? 0.7108 0.3742 0.3113 0.1140  -0.1403 -0.1316 82  PHE A O   
472  C CB  . PHE A 65  ? 0.6779 0.5790 0.3376 0.0355  -0.0550 -0.1330 82  PHE A CB  
473  C CG  . PHE A 65  ? 0.6519 0.6174 0.3583 -0.0055 -0.0376 -0.1416 82  PHE A CG  
474  C CD1 . PHE A 65  ? 0.6370 0.5704 0.3717 -0.0732 -0.0419 -0.1387 82  PHE A CD1 
475  C CD2 . PHE A 65  ? 0.6550 0.6216 0.3696 0.0113  -0.0123 -0.1341 82  PHE A CD2 
476  C CE1 . PHE A 65  ? 0.6167 0.5587 0.3776 -0.0917 -0.0318 -0.1309 82  PHE A CE1 
477  C CE2 . PHE A 65  ? 0.6419 0.6431 0.3747 0.0047  -0.0051 -0.1230 82  PHE A CE2 
478  C CZ  . PHE A 65  ? 0.6123 0.5828 0.3794 -0.0877 -0.0176 -0.1338 82  PHE A CZ  
479  N N   . LEU A 66  ? 0.6581 0.4167 0.2852 0.1249  -0.1092 -0.1271 83  LEU A N   
480  C CA  . LEU A 66  ? 0.5558 0.4523 0.2645 0.0369  -0.0834 -0.1015 83  LEU A CA  
481  C C   . LEU A 66  ? 0.5748 0.4911 0.2532 -0.0303 -0.0808 -0.0745 83  LEU A C   
482  O O   . LEU A 66  ? 0.5646 0.4717 0.2437 -0.0686 -0.0635 -0.1059 83  LEU A O   
483  C CB  . LEU A 66  ? 0.5168 0.4301 0.2646 0.0813  -0.0513 -0.0775 83  LEU A CB  
484  C CG  . LEU A 66  ? 0.4585 0.4157 0.2573 -0.0334 -0.0219 -0.0533 83  LEU A CG  
485  C CD1 . LEU A 66  ? 0.4692 0.4604 0.2534 -0.0059 -0.0206 -0.0411 83  LEU A CD1 
486  C CD2 . LEU A 66  ? 0.5059 0.5044 0.2593 0.0203  -0.0151 -0.0595 83  LEU A CD2 
487  N N   . PRO A 67  ? 0.5696 0.5383 0.2485 -0.1421 -0.0680 -0.0277 84  PRO A N   
488  C CA  . PRO A 67  ? 0.6161 0.5477 0.2440 -0.1354 -0.0564 -0.0324 84  PRO A CA  
489  C C   . PRO A 67  ? 0.7160 0.4857 0.2500 -0.0475 -0.0564 -0.0358 84  PRO A C   
490  O O   . PRO A 67  ? 0.7154 0.3795 0.2413 -0.0855 -0.0738 -0.0272 84  PRO A O   
491  C CB  . PRO A 67  ? 0.6155 0.6627 0.2458 -0.1298 -0.0314 -0.0071 84  PRO A CB  
492  C CG  . PRO A 67  ? 0.5805 0.6551 0.2445 -0.1890 -0.0503 -0.0085 84  PRO A CG  
493  C CD  . PRO A 67  ? 0.5666 0.5619 0.2464 -0.1718 -0.0682 -0.0141 84  PRO A CD  
494  N N   . GLY A 68  ? 0.7672 0.4695 0.2513 -0.0009 -0.0683 -0.0389 85  GLY A N   
495  C CA  . GLY A 68  ? 0.7836 0.4497 0.2565 0.0715  -0.0620 -0.0667 85  GLY A CA  
496  C C   . GLY A 68  ? 0.7623 0.5292 0.2532 0.1811  -0.0621 -0.0756 85  GLY A C   
497  O O   . GLY A 68  ? 0.8169 0.4939 0.2562 0.2113  -0.0851 -0.0684 85  GLY A O   
498  N N   . LEU A 69  ? 0.6671 0.4857 0.2584 0.1335  -0.0338 -0.0845 86  LEU A N   
499  C CA  . LEU A 69  ? 0.6210 0.5155 0.2601 0.1713  -0.0050 -0.0674 86  LEU A CA  
500  C C   . LEU A 69  ? 0.5447 0.4912 0.2515 0.1203  0.0061  -0.0794 86  LEU A C   
501  O O   . LEU A 69  ? 0.5122 0.4662 0.2498 0.1357  -0.0407 -0.0778 86  LEU A O   
502  C CB  . LEU A 69  ? 0.6110 0.5907 0.2709 0.1504  -0.0038 -0.0135 86  LEU A CB  
503  C CG  . LEU A 69  ? 0.6188 0.6556 0.2830 0.1404  -0.0083 0.0040  86  LEU A CG  
504  C CD1 . LEU A 69  ? 0.6779 0.7447 0.2889 0.2701  0.0006  0.0060  86  LEU A CD1 
505  C CD2 . LEU A 69  ? 0.6260 0.6555 0.2835 0.0542  -0.0020 0.0146  86  LEU A CD2 
506  N N   . ILE A 70  ? 0.4732 0.3905 0.2509 -0.0084 0.0447  -0.0567 87  ILE A N   
507  C CA  A ILE A 70  ? 0.4384 0.3657 0.2564 -0.0223 0.0299  -0.0619 87  ILE A CA  
508  C CA  B ILE A 70  ? 0.4717 0.3668 0.2588 -0.0159 0.0224  -0.0600 87  ILE A CA  
509  C C   . ILE A 70  ? 0.5077 0.3092 0.2671 -0.0212 0.0054  -0.0517 87  ILE A C   
510  O O   . ILE A 70  ? 0.4988 0.3210 0.2481 0.0475  -0.0112 -0.0635 87  ILE A O   
511  C CB  A ILE A 70  ? 0.3400 0.3845 0.2547 0.0077  0.0375  -0.0712 87  ILE A CB  
512  C CB  B ILE A 70  ? 0.4361 0.3877 0.2589 -0.0083 0.0166  -0.0658 87  ILE A CB  
513  C CG1 A ILE A 70  ? 0.2653 0.3596 0.2548 -0.0466 0.0394  -0.1106 87  ILE A CG1 
514  C CG1 B ILE A 70  ? 0.4103 0.3861 0.2580 -0.0234 0.0189  -0.0695 87  ILE A CG1 
515  C CG2 A ILE A 70  ? 0.2973 0.4515 0.2557 0.0369  0.0300  -0.0593 87  ILE A CG2 
516  C CG2 B ILE A 70  ? 0.4254 0.4030 0.2598 -0.0086 0.0092  -0.0656 87  ILE A CG2 
517  C CD1 A ILE A 70  ? 0.3026 0.3746 0.2595 -0.0259 0.0360  -0.0927 87  ILE A CD1 
518  C CD1 B ILE A 70  ? 0.4097 0.3624 0.2566 -0.0218 0.0211  -0.0675 87  ILE A CD1 
519  N N   . GLU A 71  ? 0.6391 0.2952 0.2878 -0.0403 -0.0195 -0.0682 88  GLU A N   
520  C CA  . GLU A 71  ? 0.7823 0.2420 0.3123 -0.0770 -0.0497 -0.0502 88  GLU A CA  
521  C C   . GLU A 71  ? 0.8033 0.3111 0.3136 0.1238  -0.0474 -0.0309 88  GLU A C   
522  O O   . GLU A 71  ? 0.8927 0.2822 0.3067 0.1435  -0.0909 -0.0461 88  GLU A O   
523  C CB  . GLU A 71  ? 0.9639 0.4034 0.3474 -0.0572 -0.0434 -0.0683 88  GLU A CB  
524  C CG  . GLU A 71  ? 1.1424 0.6152 0.3798 -0.0417 -0.0343 -0.1001 88  GLU A CG  
525  C CD  . GLU A 71  ? 1.2820 0.8487 0.4123 0.0017  -0.0184 -0.1113 88  GLU A CD  
526  O OE1 . GLU A 71  ? 1.3203 0.8820 0.4233 0.0380  -0.0132 -0.1190 88  GLU A OE1 
527  O OE2 . GLU A 71  ? 1.3362 0.9373 0.4270 -0.0029 -0.0083 -0.1082 88  GLU A OE2 
528  N N   . LYS A 72  ? 0.6437 0.3529 0.3136 0.1178  -0.0313 -0.0375 89  LYS A N   
529  C CA  . LYS A 72  ? 0.5217 0.4330 0.3180 0.1250  -0.0403 -0.0527 89  LYS A CA  
530  C C   . LYS A 72  ? 0.4186 0.4087 0.2900 0.0749  -0.0438 -0.0408 89  LYS A C   
531  O O   . LYS A 72  ? 0.4856 0.3984 0.2864 0.1363  -0.0473 -0.0261 89  LYS A O   
532  C CB  . LYS A 72  ? 0.4841 0.5067 0.3499 0.1620  -0.0673 -0.1321 89  LYS A CB  
533  C CG  . LYS A 72  ? 0.5603 0.5188 0.3855 0.1643  -0.0795 -0.1455 89  LYS A CG  
534  C CD  . LYS A 72  ? 0.5947 0.5342 0.4137 0.1083  -0.0738 -0.1453 89  LYS A CD  
535  C CE  . LYS A 72  ? 0.6539 0.5213 0.4387 0.1410  -0.0591 -0.1245 89  LYS A CE  
536  N NZ  . LYS A 72  ? 0.6949 0.5147 0.4544 0.1284  -0.0451 -0.1046 89  LYS A NZ  
537  N N   . MET A 73  ? 0.4026 0.3579 0.2715 0.0776  -0.0045 -0.0127 90  MET A N   
538  C CA  . MET A 73  ? 0.2567 0.3708 0.2637 0.0774  -0.0071 0.0193  90  MET A CA  
539  C C   . MET A 73  ? 0.2502 0.2801 0.2515 0.0135  -0.0084 0.0137  90  MET A C   
540  O O   . MET A 73  ? 0.2452 0.3368 0.2506 0.0182  -0.0173 -0.0198 90  MET A O   
541  C CB  . MET A 73  ? 0.2045 0.5002 0.2681 0.0776  0.0059  0.0578  90  MET A CB  
542  C CG  . MET A 73  ? 0.2255 0.5561 0.2891 0.1202  0.0238  0.0381  90  MET A CG  
543  S SD  . MET A 73  ? 0.2480 0.5417 0.2982 0.0780  -0.0016 0.0255  90  MET A SD  
544  C CE  . MET A 73  ? 0.2487 0.5829 0.3195 0.1367  -0.0353 -0.0377 90  MET A CE  
545  N N   . THR A 74  ? 0.2826 0.2506 0.2494 0.0479  -0.0087 -0.0146 91  THR A N   
546  C CA  . THR A 74  ? 0.2558 0.2454 0.2404 0.0225  -0.0220 -0.0031 91  THR A CA  
547  C C   . THR A 74  ? 0.2928 0.2645 0.2415 0.0118  -0.0590 0.0027  91  THR A C   
548  O O   . THR A 74  ? 0.4242 0.2981 0.2544 0.0257  -0.0982 -0.0067 91  THR A O   
549  C CB  . THR A 74  ? 0.1986 0.3617 0.2395 -0.0233 -0.0120 0.0014  91  THR A CB  
550  O OG1 . THR A 74  ? 0.2700 0.3764 0.2491 -0.0109 -0.0732 -0.0108 91  THR A OG1 
551  C CG2 . THR A 74  ? 0.2323 0.3840 0.2538 -0.0255 0.0070  0.0039  91  THR A CG2 
552  N N   . GLY A 75  ? 0.1855 0.2233 0.2164 0.0068  -0.0396 -0.0195 92  GLY A N   
553  C CA  . GLY A 75  ? 0.1622 0.2436 0.1873 -0.0125 -0.0001 0.0091  92  GLY A CA  
554  C C   . GLY A 75  ? 0.1620 0.2069 0.1788 -0.0034 -0.0105 -0.0122 92  GLY A C   
555  O O   . GLY A 75  ? 0.1807 0.2273 0.1789 0.0036  -0.0061 0.0018  92  GLY A O   
556  N N   . PRO A 76  ? 0.1678 0.2356 0.1732 -0.0154 -0.0032 0.0199  93  PRO A N   
557  C CA  . PRO A 76  ? 0.1844 0.2083 0.1714 0.0040  0.0209  0.0216  93  PRO A CA  
558  C C   . PRO A 76  ? 0.1145 0.2243 0.1770 0.0124  -0.0098 0.0003  93  PRO A C   
559  O O   . PRO A 76  ? 0.1702 0.2203 0.1898 0.0175  0.0232  0.0069  93  PRO A O   
560  C CB  . PRO A 76  ? 0.2404 0.1783 0.1759 0.0438  0.0070  0.0469  93  PRO A CB  
561  C CG  . PRO A 76  ? 0.2178 0.2461 0.1830 0.0319  -0.0217 0.0574  93  PRO A CG  
562  C CD  . PRO A 76  ? 0.1989 0.2197 0.1823 0.0087  -0.0211 0.0375  93  PRO A CD  
563  N N   . VAL A 77  ? 0.2059 0.1978 0.1753 -0.0114 0.0053  0.0091  94  VAL A N   
564  C CA  . VAL A 77  ? 0.1927 0.1761 0.1753 0.0020  0.0047  0.0265  94  VAL A CA  
565  C C   . VAL A 77  ? 0.2071 0.2121 0.1670 -0.0129 0.0038  0.0013  94  VAL A C   
566  O O   . VAL A 77  ? 0.1827 0.2581 0.1689 0.0071  -0.0063 -0.0281 94  VAL A O   
567  C CB  . VAL A 77  ? 0.1272 0.2145 0.1868 0.0329  0.0055  0.0166  94  VAL A CB  
568  C CG1 . VAL A 77  ? 0.1491 0.1916 0.1919 -0.0082 -0.0034 0.0145  94  VAL A CG1 
569  C CG2 . VAL A 77  ? 0.1756 0.2449 0.1973 -0.0033 -0.0207 0.0015  94  VAL A CG2 
570  N N   . LEU A 78  ? 0.1724 0.1966 0.1699 0.0033  0.0062  0.0002  95  LEU A N   
571  C CA  . LEU A 78  ? 0.1425 0.2021 0.1586 0.0238  -0.0073 -0.0091 95  LEU A CA  
572  C C   . LEU A 78  ? 0.1171 0.2104 0.1507 0.0278  0.0126  0.0070  95  LEU A C   
573  O O   . LEU A 78  ? 0.1390 0.2065 0.1550 0.0264  0.0112  -0.0048 95  LEU A O   
574  C CB  . LEU A 78  ? 0.1346 0.2119 0.1639 -0.0153 0.0027  -0.0105 95  LEU A CB  
575  C CG  . LEU A 78  ? 0.1608 0.2334 0.1578 -0.0090 0.0110  -0.0087 95  LEU A CG  
576  C CD1 . LEU A 78  ? 0.1491 0.2789 0.1609 0.0003  0.0190  -0.0044 95  LEU A CD1 
577  C CD2 . LEU A 78  ? 0.1485 0.1894 0.1586 0.0233  -0.0075 -0.0074 95  LEU A CD2 
578  N N   . CYS A 79  ? 0.1671 0.1957 0.1553 0.0362  -0.0225 0.0127  96  CYS A N   
579  C CA  . CYS A 79  ? 0.1528 0.2049 0.1607 0.0313  -0.0019 0.0239  96  CYS A CA  
580  C C   . CYS A 79  ? 0.1379 0.1908 0.1562 0.0031  -0.0150 0.0028  96  CYS A C   
581  O O   . CYS A 79  ? 0.1873 0.2050 0.1444 0.0330  -0.0141 -0.0264 96  CYS A O   
582  C CB  . CYS A 79  ? 0.1623 0.2162 0.1774 -0.0125 -0.0115 -0.0032 96  CYS A CB  
583  S SG  . CYS A 79  ? 0.1752 0.2496 0.1908 0.0276  -0.0119 0.0045  96  CYS A SG  
584  N N   . MET A 80  ? 0.1702 0.2431 0.1563 -0.0019 -0.0025 0.0356  97  MET A N   
585  C CA  . MET A 80  ? 0.1839 0.2024 0.1578 0.0285  0.0053  0.0121  97  MET A CA  
586  C C   . MET A 80  ? 0.1497 0.1712 0.1506 0.0042  0.0104  -0.0023 97  MET A C   
587  O O   . MET A 80  ? 0.1882 0.2544 0.1447 0.0078  0.0042  0.0087  97  MET A O   
588  C CB  . MET A 80  ? 0.1904 0.2033 0.1584 0.0579  -0.0223 0.0128  97  MET A CB  
589  C CG  . MET A 80  ? 0.2090 0.2093 0.1553 0.0532  -0.0242 -0.0018 97  MET A CG  
590  S SD  . MET A 80  ? 0.1927 0.2419 0.1562 0.0375  0.0049  0.0218  97  MET A SD  
591  C CE  . MET A 80  ? 0.1975 0.2652 0.1558 0.0285  0.0360  0.0212  97  MET A CE  
592  N N   . VAL A 81  ? 0.1419 0.2129 0.1560 -0.0048 -0.0082 -0.0144 98  VAL A N   
593  C CA  . VAL A 81  ? 0.1694 0.1692 0.1536 -0.0032 0.0019  0.0170  98  VAL A CA  
594  C C   . VAL A 81  ? 0.1453 0.1856 0.1525 0.0018  -0.0161 -0.0141 98  VAL A C   
595  O O   . VAL A 81  ? 0.1565 0.2341 0.1595 0.0067  -0.0136 -0.0042 98  VAL A O   
596  C CB  . VAL A 81  ? 0.1945 0.2229 0.1610 0.0388  -0.0381 0.0329  98  VAL A CB  
597  C CG1 . VAL A 81  ? 0.2102 0.1720 0.1573 0.0116  -0.0358 0.0243  98  VAL A CG1 
598  C CG2 . VAL A 81  ? 0.2395 0.2397 0.1705 0.0812  -0.0583 0.0209  98  VAL A CG2 
599  N N   . PHE A 82  ? 0.1850 0.1903 0.1495 0.0267  0.0102  -0.0186 99  PHE A N   
600  C CA  . PHE A 82  ? 0.1767 0.2022 0.1475 0.0079  0.0138  0.0390  99  PHE A CA  
601  C C   . PHE A 82  ? 0.1231 0.2435 0.1502 0.0404  -0.0110 0.0326  99  PHE A C   
602  O O   . PHE A 82  ? 0.1906 0.2125 0.1504 0.0362  -0.0075 0.0070  99  PHE A O   
603  C CB  . PHE A 82  ? 0.2049 0.2345 0.1531 0.0041  0.0218  0.0411  99  PHE A CB  
604  C CG  . PHE A 82  ? 0.1925 0.1740 0.1518 -0.0110 0.0179  0.0056  99  PHE A CG  
605  C CD1 . PHE A 82  ? 0.1669 0.2248 0.1460 -0.0058 -0.0255 -0.0086 99  PHE A CD1 
606  C CD2 . PHE A 82  ? 0.2311 0.1605 0.1559 0.0155  0.0199  0.0119  99  PHE A CD2 
607  C CE1 . PHE A 82  ? 0.2177 0.2666 0.1446 0.0616  -0.0031 -0.0008 99  PHE A CE1 
608  C CE2 . PHE A 82  ? 0.2805 0.2159 0.1546 0.0088  0.0226  0.0384  99  PHE A CE2 
609  C CZ  . PHE A 82  ? 0.2719 0.2422 0.1477 0.0906  0.0062  0.0301  99  PHE A CZ  
610  N N   . GLU A 83  ? 0.1893 0.2453 0.1508 0.0038  -0.0204 0.0346  100 GLU A N   
611  C CA  . GLU A 83  ? 0.1956 0.2086 0.1525 0.0142  -0.0202 0.0050  100 GLU A CA  
612  C C   . GLU A 83  ? 0.2061 0.2171 0.1538 0.0298  -0.0051 0.0186  100 GLU A C   
613  O O   . GLU A 83  ? 0.2355 0.1961 0.1444 0.0312  -0.0087 0.0232  100 GLU A O   
614  C CB  . GLU A 83  ? 0.2066 0.1884 0.1585 0.0385  -0.0007 0.0236  100 GLU A CB  
615  C CG  . GLU A 83  ? 0.2180 0.1957 0.1659 0.0209  0.0081  0.0168  100 GLU A CG  
616  C CD  . GLU A 83  ? 0.2617 0.2306 0.1817 0.0790  -0.0275 -0.0016 100 GLU A CD  
617  O OE1 . GLU A 83  ? 0.2770 0.2517 0.2032 0.0494  -0.0169 0.0078  100 GLU A OE1 
618  O OE2 . GLU A 83  ? 0.2699 0.2750 0.1752 0.0073  -0.0041 0.0210  100 GLU A OE2 
619  N N   . GLY A 84  ? 0.1765 0.2027 0.1540 0.0049  -0.0086 0.0016  101 GLY A N   
620  C CA  . GLY A 84  ? 0.1874 0.2269 0.1652 0.0377  -0.0129 0.0243  101 GLY A CA  
621  C C   . GLY A 84  ? 0.2071 0.1918 0.1626 -0.0032 0.0050  0.0187  101 GLY A C   
622  O O   . GLY A 84  ? 0.2039 0.2039 0.1711 0.0138  -0.0159 0.0103  101 GLY A O   
623  N N   . VAL A 85  ? 0.1471 0.2857 0.1514 0.0033  -0.0023 0.0157  102 VAL A N   
624  C CA  . VAL A 85  ? 0.2102 0.2423 0.1537 0.0078  0.0049  0.0472  102 VAL A CA  
625  C C   . VAL A 85  ? 0.2133 0.2147 0.1538 0.0078  -0.0066 0.0407  102 VAL A C   
626  O O   . VAL A 85  ? 0.2242 0.2292 0.1435 0.0176  -0.0075 0.0509  102 VAL A O   
627  C CB  . VAL A 85  ? 0.1834 0.2520 0.1625 -0.0382 0.0034  0.0295  102 VAL A CB  
628  C CG1 . VAL A 85  ? 0.2371 0.3158 0.1567 -0.0244 0.0181  0.0371  102 VAL A CG1 
629  C CG2 . VAL A 85  ? 0.1832 0.3448 0.1824 -0.0008 0.0246  0.0461  102 VAL A CG2 
630  N N   . ASP A 86  ? 0.1962 0.2937 0.1539 0.0328  0.0053  0.0020  103 ASP A N   
631  C CA  . ASP A 86  ? 0.2397 0.2294 0.1704 0.0365  -0.0007 0.0286  103 ASP A CA  
632  C C   . ASP A 86  ? 0.1950 0.1918 0.1523 0.0290  0.0018  0.0439  103 ASP A C   
633  O O   . ASP A 86  ? 0.2410 0.2187 0.1542 0.0358  0.0016  0.0273  103 ASP A O   
634  C CB  . ASP A 86  ? 0.2387 0.2546 0.1853 0.0310  0.0042  0.0250  103 ASP A CB  
635  C CG  . ASP A 86  ? 0.2453 0.3000 0.2107 0.0453  0.0174  0.0143  103 ASP A CG  
636  O OD1 . ASP A 86  ? 0.2673 0.3106 0.2129 0.0177  0.0231  0.0093  103 ASP A OD1 
637  O OD2 . ASP A 86  ? 0.2752 0.3360 0.2231 0.0343  0.0353  0.0332  103 ASP A OD2 
638  N N   . VAL A 87  ? 0.1666 0.2257 0.1619 0.0188  -0.0073 0.0406  104 VAL A N   
639  C CA  . VAL A 87  ? 0.2328 0.2415 0.1508 0.0257  -0.0078 0.0212  104 VAL A CA  
640  C C   . VAL A 87  ? 0.1839 0.2748 0.1504 0.0450  -0.0040 0.0269  104 VAL A C   
641  O O   . VAL A 87  ? 0.2010 0.2053 0.1571 -0.0038 -0.0049 0.0172  104 VAL A O   
642  C CB  . VAL A 87  ? 0.1623 0.1930 0.1522 0.0679  -0.0037 0.0195  104 VAL A CB  
643  C CG1 . VAL A 87  ? 0.2170 0.1811 0.1611 0.0349  -0.0053 0.0273  104 VAL A CG1 
644  C CG2 . VAL A 87  ? 0.1835 0.2604 0.1607 0.0463  -0.0109 0.0209  104 VAL A CG2 
645  N N   . ILE A 88  ? 0.1810 0.2281 0.1381 0.0125  -0.0034 0.0311  105 ILE A N   
646  C CA  . ILE A 88  ? 0.2005 0.2459 0.1477 0.0325  -0.0219 0.0286  105 ILE A CA  
647  C C   . ILE A 88  ? 0.2034 0.1961 0.1511 0.0164  -0.0053 0.0259  105 ILE A C   
648  O O   . ILE A 88  ? 0.2365 0.1883 0.1581 0.0189  0.0008  0.0077  105 ILE A O   
649  C CB  . ILE A 88  ? 0.1958 0.2267 0.1658 0.0046  -0.0256 0.0097  105 ILE A CB  
650  C CG1 . ILE A 88  ? 0.1898 0.1872 0.1758 0.0043  -0.0087 0.0268  105 ILE A CG1 
651  C CG2 . ILE A 88  ? 0.2069 0.2446 0.1755 0.0087  -0.0012 0.0088  105 ILE A CG2 
652  C CD1 . ILE A 88  ? 0.2146 0.2785 0.1815 0.0754  -0.0243 0.0243  105 ILE A CD1 
653  N N   . ALA A 89  ? 0.1917 0.2399 0.1359 0.0440  -0.0035 0.0335  106 ALA A N   
654  C CA  . ALA A 89  ? 0.2188 0.2442 0.1378 0.0301  0.0051  0.0220  106 ALA A CA  
655  C C   . ALA A 89  ? 0.2013 0.2529 0.1409 0.0361  -0.0110 0.0062  106 ALA A C   
656  O O   . ALA A 89  ? 0.2333 0.2397 0.1601 0.0464  -0.0220 0.0110  106 ALA A O   
657  C CB  . ALA A 89  ? 0.2358 0.2142 0.1322 0.0061  -0.0267 0.0139  106 ALA A CB  
658  N N   . GLN A 90  ? 0.1772 0.2187 0.1438 0.0410  -0.0077 -0.0006 107 GLN A N   
659  C CA  . GLN A 90  ? 0.1891 0.2160 0.1517 0.0414  -0.0125 0.0126  107 GLN A CA  
660  C C   . GLN A 90  ? 0.1626 0.2537 0.1508 -0.0007 -0.0250 0.0267  107 GLN A C   
661  O O   . GLN A 90  ? 0.2116 0.2172 0.1595 0.0584  -0.0121 0.0282  107 GLN A O   
662  C CB  . GLN A 90  ? 0.2190 0.2780 0.1539 0.0301  0.0001  0.0036  107 GLN A CB  
663  C CG  . GLN A 90  ? 0.2006 0.2276 0.1661 0.0296  0.0249  0.0342  107 GLN A CG  
664  C CD  . GLN A 90  ? 0.1923 0.2580 0.1615 0.0100  0.0167  0.0290  107 GLN A CD  
665  O OE1 . GLN A 90  ? 0.1995 0.2487 0.1657 0.0310  -0.0321 0.0053  107 GLN A OE1 
666  N NE2 . GLN A 90  ? 0.2032 0.3184 0.1551 -0.0026 0.0093  0.0291  107 GLN A NE2 
667  N N   . ALA A 91  ? 0.2167 0.2552 0.1425 0.0117  -0.0155 0.0216  108 ALA A N   
668  C CA  . ALA A 91  ? 0.1765 0.2089 0.1533 0.0285  0.0061  0.0344  108 ALA A CA  
669  C C   . ALA A 91  ? 0.2045 0.2351 0.1729 0.0238  -0.0017 0.0275  108 ALA A C   
670  O O   . ALA A 91  ? 0.1727 0.2522 0.1802 0.0111  0.0175  0.0323  108 ALA A O   
671  C CB  . ALA A 91  ? 0.1926 0.2148 0.1563 0.0326  0.0434  0.0505  108 ALA A CB  
672  N N   . ARG A 92  ? 0.2306 0.2092 0.1734 0.0375  -0.0070 0.0050  109 ARG A N   
673  C CA  . ARG A 92  ? 0.2726 0.2112 0.1889 0.0141  -0.0189 -0.0102 109 ARG A CA  
674  C C   . ARG A 92  ? 0.2602 0.1765 0.1789 0.0143  -0.0411 -0.0127 109 ARG A C   
675  O O   . ARG A 92  ? 0.2655 0.2050 0.1762 0.0428  -0.0420 0.0057  109 ARG A O   
676  C CB  . ARG A 92  ? 0.3487 0.3063 0.2120 0.0734  -0.0126 -0.0073 109 ARG A CB  
677  C CG  . ARG A 92  ? 0.4141 0.3691 0.2411 0.0224  -0.0322 -0.0360 109 ARG A CG  
678  C CD  . ARG A 92  ? 0.5273 0.4910 0.2720 0.0248  -0.0524 -0.0886 109 ARG A CD  
679  N NE  . ARG A 92  ? 0.6982 0.6806 0.2953 0.1433  -0.0413 -0.1483 109 ARG A NE  
680  C CZ  . ARG A 92  ? 0.8192 0.7620 0.3282 0.1811  -0.0292 -0.1911 109 ARG A CZ  
681  N NH1 . ARG A 92  ? 0.8225 0.7185 0.3660 0.1717  0.0045  -0.2226 109 ARG A NH1 
682  N NH2 . ARG A 92  ? 0.8556 0.8209 0.3608 0.2862  -0.0285 -0.1789 109 ARG A NH2 
683  N N   . LYS A 93  ? 0.2651 0.2076 0.1688 -0.0127 -0.0020 -0.0032 110 LYS A N   
684  C CA  . LYS A 93  ? 0.2759 0.2597 0.1756 0.0460  0.0243  0.0311  110 LYS A CA  
685  C C   . LYS A 93  ? 0.2406 0.2428 0.1688 0.0685  0.0136  0.0332  110 LYS A C   
686  O O   . LYS A 93  ? 0.2270 0.2381 0.1612 0.0186  0.0215  -0.0004 110 LYS A O   
687  C CB  . LYS A 93  ? 0.2615 0.3256 0.1986 -0.0179 0.0526  0.0209  110 LYS A CB  
688  C CG  . LYS A 93  ? 0.2169 0.3398 0.2225 -0.0625 0.0478  0.0074  110 LYS A CG  
689  C CD  . LYS A 93  ? 0.2451 0.3958 0.2364 -0.0604 0.0390  -0.0195 110 LYS A CD  
690  C CE  . LYS A 93  ? 0.2542 0.3914 0.2481 -0.0315 0.0679  -0.0263 110 LYS A CE  
691  N NZ  . LYS A 93  ? 0.2372 0.3715 0.2607 -0.0511 0.0751  0.0236  110 LYS A NZ  
692  N N   . MET A 94  ? 0.1998 0.1919 0.1667 0.0314  0.0060  0.0075  111 MET A N   
693  C CA  . MET A 94  ? 0.2045 0.1861 0.1532 0.0264  0.0072  0.0148  111 MET A CA  
694  C C   . MET A 94  ? 0.2091 0.1925 0.1521 0.0778  0.0235  0.0382  111 MET A C   
695  O O   . MET A 94  ? 0.1915 0.2149 0.1740 0.0586  0.0061  0.0416  111 MET A O   
696  C CB  . MET A 94  ? 0.1926 0.2577 0.1536 0.0237  -0.0046 0.0144  111 MET A CB  
697  C CG  . MET A 94  ? 0.1844 0.2328 0.1462 0.0018  -0.0055 0.0226  111 MET A CG  
698  S SD  . MET A 94  ? 0.2095 0.2433 0.1681 0.0131  -0.0056 -0.0099 111 MET A SD  
699  C CE  . MET A 94  ? 0.2589 0.3558 0.1660 0.0161  -0.0340 -0.0137 111 MET A CE  
700  N N   . MET A 95  ? 0.2006 0.2536 0.1544 0.0409  0.0150  0.0344  112 MET A N   
701  C CA  A MET A 95  ? 0.2183 0.1972 0.1571 0.0610  0.0069  0.0100  112 MET A CA  
702  C CA  B MET A 95  ? 0.2218 0.2373 0.1592 0.0462  0.0042  0.0219  112 MET A CA  
703  C C   . MET A 95  ? 0.2414 0.1930 0.1533 0.0306  0.0003  0.0237  112 MET A C   
704  O O   . MET A 95  ? 0.2185 0.2085 0.1487 0.0318  -0.0496 0.0136  112 MET A O   
705  C CB  A MET A 95  ? 0.1649 0.1730 0.1611 0.0189  0.0076  -0.0132 112 MET A CB  
706  C CB  B MET A 95  ? 0.1882 0.2793 0.1681 -0.0029 -0.0007 0.0262  112 MET A CB  
707  C CG  A MET A 95  ? 0.1757 0.2376 0.1660 0.0335  0.0246  -0.0091 112 MET A CG  
708  C CG  B MET A 95  ? 0.2091 0.3156 0.1769 0.0164  0.0043  0.0328  112 MET A CG  
709  S SD  A MET A 95  ? 0.2212 0.2650 0.1700 0.0650  0.0205  0.0197  112 MET A SD  
710  S SD  B MET A 95  ? 0.2527 0.2991 0.1854 0.0461  -0.0072 0.0596  112 MET A SD  
711  C CE  A MET A 95  ? 0.2567 0.2770 0.1665 0.0557  0.0178  0.0034  112 MET A CE  
712  C CE  B MET A 95  ? 0.2802 0.2698 0.1826 0.0790  -0.0202 0.0415  112 MET A CE  
713  N N   . GLY A 96  ? 0.1974 0.2052 0.1500 0.0178  0.0206  0.0084  113 GLY A N   
714  C CA  . GLY A 96  ? 0.1876 0.2778 0.1604 0.0367  0.0050  -0.0152 113 GLY A CA  
715  C C   . GLY A 96  ? 0.2106 0.1994 0.1634 0.0613  -0.0206 0.0039  113 GLY A C   
716  O O   . GLY A 96  ? 0.1939 0.2387 0.1648 0.0276  -0.0215 0.0028  113 GLY A O   
717  N N   . SER A 97  ? 0.1968 0.2269 0.1620 0.0176  -0.0019 -0.0084 114 SER A N   
718  C CA  A SER A 97  ? 0.2110 0.2046 0.1761 0.0281  -0.0057 -0.0318 114 SER A CA  
719  C CA  B SER A 97  ? 0.2027 0.2643 0.1666 0.0298  -0.0153 -0.0268 114 SER A CA  
720  C C   . SER A 97  ? 0.1864 0.2885 0.1620 -0.0056 -0.0211 -0.0277 114 SER A C   
721  O O   . SER A 97  ? 0.2341 0.2616 0.1324 0.0132  -0.0110 -0.0343 114 SER A O   
722  C CB  A SER A 97  ? 0.2293 0.2507 0.1971 -0.0035 0.0317  -0.0115 114 SER A CB  
723  C CB  B SER A 97  ? 0.2014 0.3175 0.1695 0.0301  -0.0079 -0.0209 114 SER A CB  
724  O OG  A SER A 97  ? 0.2383 0.3300 0.2114 -0.0276 0.0435  -0.0068 114 SER A OG  
725  O OG  B SER A 97  ? 0.1629 0.2980 0.1683 -0.0049 -0.0306 -0.0316 114 SER A OG  
726  N N   . THR A 98  ? 0.2064 0.2742 0.1704 0.0461  -0.0096 -0.0139 115 THR A N   
727  C CA  . THR A 98  ? 0.1939 0.2812 0.1903 0.0035  -0.0077 0.0410  115 THR A CA  
728  C C   . THR A 98  ? 0.1688 0.2563 0.1728 -0.0030 0.0068  0.0476  115 THR A C   
729  O O   . THR A 98  ? 0.2099 0.2122 0.1691 0.0226  -0.0065 0.0213  115 THR A O   
730  C CB  . THR A 98  ? 0.2326 0.3508 0.2253 0.0525  -0.0081 0.1097  115 THR A CB  
731  O OG1 . THR A 98  ? 0.2999 0.4041 0.2456 0.0289  -0.0227 0.0745  115 THR A OG1 
732  C CG2 . THR A 98  ? 0.2080 0.4403 0.2402 0.0572  -0.0016 0.0982  115 THR A CG2 
733  N N   . ARG A 99  ? 0.2091 0.2573 0.1606 0.0465  -0.0179 -0.0004 116 ARG A N   
734  C CA  . ARG A 99  ? 0.2397 0.2567 0.1649 0.0470  -0.0069 0.0024  116 ARG A CA  
735  C C   . ARG A 99  ? 0.1917 0.2517 0.1621 0.0294  0.0008  -0.0003 116 ARG A C   
736  O O   . ARG A 99  ? 0.2235 0.2463 0.1595 0.0255  0.0030  0.0135  116 ARG A O   
737  C CB  . ARG A 99  ? 0.2289 0.2361 0.1722 0.0652  -0.0076 0.0160  116 ARG A CB  
738  C CG  . ARG A 99  ? 0.2440 0.2883 0.1811 0.0637  0.0225  -0.0284 116 ARG A CG  
739  C CD  . ARG A 99  ? 0.2332 0.4104 0.1868 -0.0341 0.0500  -0.0037 116 ARG A CD  
740  N NE  . ARG A 99  ? 0.3245 0.5060 0.1961 0.0031  0.0231  -0.0371 116 ARG A NE  
741  C CZ  . ARG A 99  ? 0.3387 0.5942 0.2029 -0.0378 -0.0202 -0.0223 116 ARG A CZ  
742  N NH1 . ARG A 99  ? 0.2919 0.5785 0.2099 -0.0902 -0.0346 0.0176  116 ARG A NH1 
743  N NH2 . ARG A 99  ? 0.3386 0.6083 0.2146 -0.1419 -0.0352 -0.0476 116 ARG A NH2 
744  N N   . PRO A 100 ? 0.1840 0.2445 0.1640 0.0397  -0.0093 0.0189  117 PRO A N   
745  C CA  . PRO A 100 ? 0.1861 0.2384 0.1606 0.0467  -0.0072 0.0110  117 PRO A CA  
746  C C   . PRO A 100 ? 0.1881 0.1807 0.1613 -0.0201 -0.0096 0.0000  117 PRO A C   
747  O O   . PRO A 100 ? 0.1895 0.2320 0.1495 0.0056  -0.0118 0.0074  117 PRO A O   
748  C CB  . PRO A 100 ? 0.1808 0.2579 0.1570 0.0133  -0.0066 0.0067  117 PRO A CB  
749  C CG  . PRO A 100 ? 0.1696 0.2607 0.1536 0.0211  -0.0175 -0.0077 117 PRO A CG  
750  C CD  . PRO A 100 ? 0.1387 0.2552 0.1575 0.0226  -0.0148 0.0026  117 PRO A CD  
751  N N   . GLY A 101 ? 0.1870 0.2003 0.1669 0.0377  -0.0281 0.0053  118 GLY A N   
752  C CA  . GLY A 101 ? 0.1966 0.2840 0.1691 0.0795  0.0184  0.0287  118 GLY A CA  
753  C C   . GLY A 101 ? 0.1598 0.2492 0.1686 0.0438  0.0116  0.0008  118 GLY A C   
754  O O   . GLY A 101 ? 0.1988 0.2376 0.1876 0.0677  0.0326  0.0211  118 GLY A O   
755  N N   . GLU A 102 ? 0.2109 0.2294 0.1623 0.0218  -0.0253 0.0023  119 GLU A N   
756  C CA  . GLU A 102 ? 0.1824 0.2617 0.1552 0.0258  -0.0265 0.0028  119 GLU A CA  
757  C C   . GLU A 102 ? 0.2229 0.2637 0.1577 0.0453  -0.0158 0.0153  119 GLU A C   
758  O O   . GLU A 102 ? 0.2737 0.2579 0.1707 -0.0289 0.0049  -0.0173 119 GLU A O   
759  C CB  . GLU A 102 ? 0.2282 0.2403 0.1498 0.0268  -0.0170 0.0083  119 GLU A CB  
760  C CG  . GLU A 102 ? 0.2181 0.2581 0.1641 0.0105  -0.0145 0.0058  119 GLU A CG  
761  C CD  . GLU A 102 ? 0.2659 0.3063 0.1779 0.0531  -0.0382 -0.0017 119 GLU A CD  
762  O OE1 . GLU A 102 ? 0.2492 0.3541 0.1753 0.0228  -0.0318 0.0408  119 GLU A OE1 
763  O OE2 . GLU A 102 ? 0.2479 0.3538 0.1959 0.0160  -0.0497 -0.0384 119 GLU A OE2 
764  N N   . ALA A 103 ? 0.1849 0.2633 0.1502 0.0023  -0.0202 0.0210  120 ALA A N   
765  C CA  . ALA A 103 ? 0.1848 0.2515 0.1458 -0.0326 -0.0063 0.0045  120 ALA A CA  
766  C C   . ALA A 103 ? 0.1772 0.2926 0.1625 -0.0236 0.0100  -0.0143 120 ALA A C   
767  O O   . ALA A 103 ? 0.2615 0.2626 0.1500 0.0253  -0.0174 -0.0080 120 ALA A O   
768  C CB  . ALA A 103 ? 0.2300 0.2601 0.1360 0.0066  0.0151  -0.0033 120 ALA A CB  
769  N N   . ALA A 104 ? 0.2005 0.3144 0.1973 0.0015  0.0133  -0.0323 121 ALA A N   
770  C CA  . ALA A 104 ? 0.2566 0.2793 0.2210 -0.0283 0.0287  -0.0766 121 ALA A CA  
771  C C   . ALA A 104 ? 0.1368 0.3088 0.2468 0.0093  0.0228  -0.0388 121 ALA A C   
772  O O   . ALA A 104 ? 0.1896 0.2866 0.2247 0.0338  0.0393  0.0086  121 ALA A O   
773  C CB  . ALA A 104 ? 0.3153 0.2836 0.2135 -0.0388 0.0644  -0.0423 121 ALA A CB  
774  N N   . PRO A 105 ? 0.2111 0.3634 0.2777 0.0470  -0.0123 -0.1309 122 PRO A N   
775  C CA  . PRO A 105 ? 0.2192 0.4016 0.2813 0.1060  -0.0066 -0.0917 122 PRO A CA  
776  C C   . PRO A 105 ? 0.1486 0.2820 0.2563 0.0293  0.0189  -0.0360 122 PRO A C   
777  O O   . PRO A 105 ? 0.2385 0.3378 0.2517 -0.0424 0.0280  -0.0504 122 PRO A O   
778  C CB  . PRO A 105 ? 0.2895 0.5024 0.2989 0.1278  -0.0330 -0.1328 122 PRO A CB  
779  C CG  . PRO A 105 ? 0.3924 0.4773 0.3087 0.1733  -0.0621 -0.1777 122 PRO A CG  
780  C CD  . PRO A 105 ? 0.3794 0.4350 0.3009 0.1307  -0.0535 -0.1783 122 PRO A CD  
781  N N   . GLY A 106 ? 0.2151 0.2518 0.2357 0.0252  -0.0038 0.0355  123 GLY A N   
782  C CA  . GLY A 106 ? 0.1811 0.2980 0.2139 0.0326  -0.0104 0.0321  123 GLY A CA  
783  C C   . GLY A 106 ? 0.1860 0.2238 0.2056 0.0781  0.0033  0.0021  123 GLY A C   
784  O O   . GLY A 106 ? 0.2086 0.2837 0.2285 0.0541  0.0113  -0.0111 123 GLY A O   
785  N N   . THR A 107 ? 0.1299 0.2502 0.1802 0.0263  -0.0103 0.0057  124 THR A N   
786  C CA  . THR A 107 ? 0.1686 0.1878 0.1795 0.0005  -0.0166 0.0191  124 THR A CA  
787  C C   . THR A 107 ? 0.2145 0.1691 0.1715 0.0139  0.0034  -0.0146 124 THR A C   
788  O O   . THR A 107 ? 0.1955 0.2021 0.1716 0.0476  0.0114  0.0072  124 THR A O   
789  C CB  . THR A 107 ? 0.1797 0.2221 0.1655 0.0216  -0.0106 0.0169  124 THR A CB  
790  O OG1 . THR A 107 ? 0.1776 0.2245 0.1622 0.0176  -0.0194 0.0281  124 THR A OG1 
791  C CG2 . THR A 107 ? 0.1606 0.1959 0.1698 0.0474  0.0092  0.0266  124 THR A CG2 
792  N N   . ILE A 108 ? 0.2258 0.2090 0.1697 0.0125  -0.0056 0.0024  125 ILE A N   
793  C CA  . ILE A 108 ? 0.2087 0.1986 0.1623 0.0017  0.0135  0.0337  125 ILE A CA  
794  C C   . ILE A 108 ? 0.1932 0.2418 0.1499 0.0434  0.0033  0.0099  125 ILE A C   
795  O O   . ILE A 108 ? 0.1853 0.2480 0.1407 0.0318  0.0036  0.0188  125 ILE A O   
796  C CB  . ILE A 108 ? 0.2405 0.1787 0.1600 0.0342  0.0149  0.0274  125 ILE A CB  
797  C CG1 . ILE A 108 ? 0.2541 0.2158 0.1688 0.0694  0.0151  0.0103  125 ILE A CG1 
798  C CG2 . ILE A 108 ? 0.1807 0.2384 0.1614 0.0234  0.0039  0.0091  125 ILE A CG2 
799  C CD1 . ILE A 108 ? 0.2517 0.2022 0.1860 0.0566  0.0000  -0.0257 125 ILE A CD1 
800  N N   . ARG A 109 ? 0.1711 0.2096 0.1466 0.0146  0.0018  0.0091  126 ARG A N   
801  C CA  . ARG A 109 ? 0.1865 0.2234 0.1460 0.0152  0.0026  0.0000  126 ARG A CA  
802  C C   . ARG A 109 ? 0.1799 0.1962 0.1369 0.0399  -0.0070 -0.0032 126 ARG A C   
803  O O   . ARG A 109 ? 0.2003 0.2249 0.1449 0.0268  -0.0030 0.0074  126 ARG A O   
804  C CB  . ARG A 109 ? 0.2200 0.2599 0.1534 0.0695  0.0031  0.0109  126 ARG A CB  
805  C CG  . ARG A 109 ? 0.1711 0.2684 0.1594 0.0355  -0.0071 -0.0040 126 ARG A CG  
806  C CD  . ARG A 109 ? 0.1644 0.2974 0.1609 0.0280  0.0005  -0.0250 126 ARG A CD  
807  N NE  . ARG A 109 ? 0.1736 0.2718 0.1637 0.0061  -0.0052 -0.0265 126 ARG A NE  
808  C CZ  . ARG A 109 ? 0.2283 0.3051 0.1630 0.0867  0.0061  -0.0131 126 ARG A CZ  
809  N NH1 . ARG A 109 ? 0.2926 0.3769 0.1572 0.0784  0.0478  -0.0173 126 ARG A NH1 
810  N NH2 . ARG A 109 ? 0.2762 0.3384 0.1714 0.0863  0.0274  -0.0027 126 ARG A NH2 
811  N N   . ALA A 110 ? 0.1761 0.2088 0.1216 0.0249  0.0152  -0.0065 127 ALA A N   
812  C CA  . ALA A 110 ? 0.2276 0.2248 0.1375 0.0537  0.0172  -0.0028 127 ALA A CA  
813  C C   . ALA A 110 ? 0.2234 0.1557 0.1530 -0.0001 0.0112  -0.0031 127 ALA A C   
814  O O   . ALA A 110 ? 0.2655 0.2119 0.1572 0.0196  0.0001  -0.0029 127 ALA A O   
815  C CB  . ALA A 110 ? 0.2321 0.2571 0.1301 0.0828  0.0015  0.0073  127 ALA A CB  
816  N N   . ASP A 111 ? 0.2025 0.1713 0.1587 0.0469  -0.0203 -0.0018 128 ASP A N   
817  C CA  . ASP A 111 ? 0.1751 0.2263 0.1659 0.0396  -0.0073 0.0283  128 ASP A CA  
818  C C   . ASP A 111 ? 0.1480 0.2268 0.1505 0.0370  -0.0259 0.0088  128 ASP A C   
819  O O   . ASP A 111 ? 0.1754 0.2432 0.1426 0.0521  -0.0296 -0.0080 128 ASP A O   
820  C CB  . ASP A 111 ? 0.2166 0.2749 0.2038 0.0014  0.0056  0.0198  128 ASP A CB  
821  C CG  . ASP A 111 ? 0.2458 0.2299 0.2449 -0.0271 0.0202  -0.0099 128 ASP A CG  
822  O OD1 . ASP A 111 ? 0.2418 0.3471 0.2647 0.0150  0.0373  -0.0088 128 ASP A OD1 
823  O OD2 . ASP A 111 ? 0.2852 0.2450 0.2661 -0.0157 0.0017  0.0071  128 ASP A OD2 
824  N N   . PHE A 112 ? 0.1821 0.2164 0.1449 0.0358  -0.0118 0.0152  129 PHE A N   
825  C CA  . PHE A 112 ? 0.1914 0.1936 0.1355 0.0615  -0.0141 0.0075  129 PHE A CA  
826  C C   . PHE A 112 ? 0.1936 0.2007 0.1440 0.0177  -0.0149 0.0093  129 PHE A C   
827  O O   . PHE A 112 ? 0.1708 0.2095 0.1449 0.0127  -0.0146 0.0252  129 PHE A O   
828  C CB  . PHE A 112 ? 0.2112 0.2068 0.1416 0.0549  -0.0086 -0.0041 129 PHE A CB  
829  C CG  . PHE A 112 ? 0.1848 0.2132 0.1362 0.0381  -0.0082 -0.0002 129 PHE A CG  
830  C CD1 . PHE A 112 ? 0.2235 0.2396 0.1398 0.0584  -0.0405 0.0003  129 PHE A CD1 
831  C CD2 . PHE A 112 ? 0.2495 0.1879 0.1372 0.0217  -0.0004 -0.0343 129 PHE A CD2 
832  C CE1 . PHE A 112 ? 0.2513 0.2732 0.1377 0.0133  -0.0421 -0.0139 129 PHE A CE1 
833  C CE2 . PHE A 112 ? 0.2084 0.2512 0.1346 0.0288  0.0084  -0.0198 129 PHE A CE2 
834  C CZ  . PHE A 112 ? 0.2492 0.2181 0.1350 0.0168  -0.0388 -0.0325 129 PHE A CZ  
835  N N   . CYS A 113 ? 0.1609 0.2125 0.1467 0.0412  -0.0013 -0.0095 130 CYS A N   
836  C CA  . CYS A 113 ? 0.1452 0.1981 0.1510 0.0104  0.0137  -0.0038 130 CYS A CA  
837  C C   . CYS A 113 ? 0.1814 0.1926 0.1551 0.0507  0.0154  -0.0082 130 CYS A C   
838  O O   . CYS A 113 ? 0.1806 0.2168 0.1583 0.0338  0.0086  -0.0029 130 CYS A O   
839  C CB  . CYS A 113 ? 0.1729 0.2155 0.1501 0.0378  -0.0074 -0.0013 130 CYS A CB  
840  S SG  . CYS A 113 ? 0.1933 0.2074 0.1657 0.0336  -0.0138 -0.0191 130 CYS A SG  
841  N N   . GLN A 114 ? 0.1552 0.2137 0.1648 0.0375  0.0057  -0.0157 131 GLN A N   
842  C CA  . GLN A 114 ? 0.1659 0.1843 0.1559 0.0197  0.0003  -0.0026 131 GLN A CA  
843  C C   . GLN A 114 ? 0.1842 0.1959 0.1539 0.0319  -0.0324 -0.0254 131 GLN A C   
844  O O   . GLN A 114 ? 0.1961 0.2707 0.1703 0.0266  -0.0273 -0.0313 131 GLN A O   
845  C CB  . GLN A 114 ? 0.2006 0.2164 0.1620 0.0351  0.0041  0.0029  131 GLN A CB  
846  C CG  . GLN A 114 ? 0.2363 0.1864 0.1581 0.0152  -0.0255 -0.0170 131 GLN A CG  
847  C CD  . GLN A 114 ? 0.1884 0.2014 0.1573 -0.0178 -0.0549 -0.0274 131 GLN A CD  
848  O OE1 . GLN A 114 ? 0.2243 0.2095 0.1777 0.0045  -0.0379 -0.0118 131 GLN A OE1 
849  N NE2 . GLN A 114 ? 0.2202 0.2379 0.1515 0.0392  -0.0513 0.0072  131 GLN A NE2 
850  N N   . GLN A 115 ? 0.1995 0.2407 0.1585 0.0433  -0.0472 -0.0234 132 GLN A N   
851  C CA  . GLN A 115 ? 0.1671 0.2368 0.1850 -0.0142 -0.0536 0.0140  132 GLN A CA  
852  C C   . GLN A 115 ? 0.2064 0.2201 0.1786 0.0172  -0.0136 0.0270  132 GLN A C   
853  O O   . GLN A 115 ? 0.2076 0.2240 0.1661 0.0083  -0.0201 0.0014  132 GLN A O   
854  C CB  . GLN A 115 ? 0.2316 0.1907 0.2152 -0.0132 -0.0309 0.0095  132 GLN A CB  
855  C CG  . GLN A 115 ? 0.2076 0.2540 0.2421 -0.0364 -0.0368 0.0036  132 GLN A CG  
856  C CD  . GLN A 115 ? 0.2308 0.2680 0.2554 -0.0172 -0.0164 -0.0044 132 GLN A CD  
857  O OE1 . GLN A 115 ? 0.2726 0.3042 0.2595 0.0123  -0.0138 -0.0142 132 GLN A OE1 
858  N NE2 . GLN A 115 ? 0.2857 0.2993 0.2637 -0.0216 -0.0138 -0.0214 132 GLN A NE2 
859  N N   . ALA A 116 ? 0.2010 0.2433 0.1792 0.0193  -0.0023 0.0265  133 ALA A N   
860  C CA  . ALA A 116 ? 0.2250 0.2236 0.1824 0.0208  -0.0204 0.0283  133 ALA A CA  
861  C C   . ALA A 116 ? 0.2203 0.3064 0.1892 0.0232  -0.0164 0.0245  133 ALA A C   
862  O O   . ALA A 116 ? 0.2430 0.3052 0.2061 0.0458  -0.0112 0.0117  133 ALA A O   
863  C CB  . ALA A 116 ? 0.2477 0.2787 0.1859 0.0061  -0.0340 0.0475  133 ALA A CB  
864  N N   . GLY A 117 ? 0.2094 0.2797 0.1856 -0.0153 -0.0001 0.0233  134 GLY A N   
865  C CA  . GLY A 117 ? 0.2240 0.3038 0.1781 0.0201  -0.0047 0.0331  134 GLY A CA  
866  C C   . GLY A 117 ? 0.2336 0.2426 0.1824 0.0550  -0.0135 0.0018  134 GLY A C   
867  O O   . GLY A 117 ? 0.2019 0.3335 0.1896 0.0481  0.0081  -0.0026 134 GLY A O   
868  N N   . ARG A 118 ? 0.1988 0.2243 0.1789 0.0486  -0.0149 -0.0253 135 ARG A N   
869  C CA  . ARG A 118 ? 0.1963 0.1933 0.1684 -0.0150 0.0195  -0.0036 135 ARG A CA  
870  C C   . ARG A 118 ? 0.1921 0.2154 0.1684 0.0046  0.0051  0.0007  135 ARG A C   
871  O O   . ARG A 118 ? 0.2044 0.2146 0.1649 0.0178  -0.0199 0.0026  135 ARG A O   
872  C CB  . ARG A 118 ? 0.2088 0.2072 0.1828 0.0186  -0.0071 -0.0136 135 ARG A CB  
873  C CG  . ARG A 118 ? 0.1867 0.2395 0.1919 0.0243  -0.0105 -0.0167 135 ARG A CG  
874  C CD  . ARG A 118 ? 0.1881 0.2822 0.2007 0.0077  0.0053  -0.0144 135 ARG A CD  
875  N NE  . ARG A 118 ? 0.1931 0.3038 0.2249 0.0173  0.0272  -0.0026 135 ARG A NE  
876  C CZ  . ARG A 118 ? 0.2586 0.2839 0.2424 0.0685  0.0377  -0.0020 135 ARG A CZ  
877  N NH1 . ARG A 118 ? 0.2023 0.3567 0.2540 -0.0140 0.0093  -0.0169 135 ARG A NH1 
878  N NH2 . ARG A 118 ? 0.2668 0.2999 0.2578 0.0293  0.0501  0.0007  135 ARG A NH2 
879  N N   . ASN A 119 ? 0.2028 0.1985 0.1671 0.0260  0.0079  -0.0029 136 ASN A N   
880  C CA  . ASN A 119 ? 0.1725 0.2147 0.1607 -0.0034 0.0271  0.0146  136 ASN A CA  
881  C C   . ASN A 119 ? 0.2207 0.1990 0.1528 0.0415  0.0072  0.0134  136 ASN A C   
882  O O   . ASN A 119 ? 0.2313 0.2098 0.1532 0.0450  -0.0092 0.0137  136 ASN A O   
883  C CB  . ASN A 119 ? 0.1811 0.2674 0.1677 0.0306  0.0178  0.0481  136 ASN A CB  
884  C CG  . ASN A 119 ? 0.2073 0.2932 0.1741 0.0282  -0.0111 0.0315  136 ASN A CG  
885  O OD1 . ASN A 119 ? 0.2241 0.2469 0.1794 0.0559  -0.0076 0.0058  136 ASN A OD1 
886  N ND2 . ASN A 119 ? 0.2550 0.3048 0.1736 0.0610  -0.0085 0.0237  136 ASN A ND2 
887  N N   . LEU A 120 ? 0.2069 0.2172 0.1514 0.0173  0.0045  -0.0263 137 LEU A N   
888  C CA  . LEU A 120 ? 0.1700 0.2112 0.1546 0.0239  0.0039  -0.0027 137 LEU A CA  
889  C C   . LEU A 120 ? 0.1755 0.2012 0.1506 0.0201  0.0082  -0.0098 137 LEU A C   
890  O O   . LEU A 120 ? 0.1905 0.2058 0.1431 0.0245  0.0145  0.0107  137 LEU A O   
891  C CB  . LEU A 120 ? 0.2246 0.1860 0.1491 0.0165  -0.0098 -0.0115 137 LEU A CB  
892  C CG  . LEU A 120 ? 0.1917 0.2549 0.1396 0.0011  -0.0017 -0.0028 137 LEU A CG  
893  C CD1 . LEU A 120 ? 0.2440 0.2185 0.1300 0.0268  0.0253  0.0002  137 LEU A CD1 
894  C CD2 . LEU A 120 ? 0.1674 0.2463 0.1462 0.0262  -0.0089 0.0043  137 LEU A CD2 
895  N N   . ILE A 121 ? 0.1993 0.1875 0.1498 0.0552  0.0022  0.0027  138 ILE A N   
896  C CA  . ILE A 121 ? 0.2039 0.1594 0.1550 0.0337  -0.0217 0.0118  138 ILE A CA  
897  C C   . ILE A 121 ? 0.1931 0.1907 0.1500 0.0094  -0.0170 0.0102  138 ILE A C   
898  O O   . ILE A 121 ? 0.2071 0.2130 0.1461 0.0013  -0.0016 -0.0045 138 ILE A O   
899  C CB  . ILE A 121 ? 0.2113 0.1816 0.1691 -0.0240 0.0038  0.0136  138 ILE A CB  
900  C CG1 . ILE A 121 ? 0.1635 0.2643 0.1778 -0.0163 -0.0049 0.0226  138 ILE A CG1 
901  C CG2 . ILE A 121 ? 0.2035 0.2606 0.1680 -0.0266 0.0205  0.0431  138 ILE A CG2 
902  C CD1 . ILE A 121 ? 0.2101 0.2005 0.1779 0.0265  0.0090  0.0467  138 ILE A CD1 
903  N N   . HIS A 122 ? 0.1785 0.1635 0.1549 0.0145  -0.0115 0.0201  139 HIS A N   
904  C CA  . HIS A 122 ? 0.2068 0.1847 0.1482 0.0596  0.0026  0.0060  139 HIS A CA  
905  C C   . HIS A 122 ? 0.2009 0.1791 0.1479 0.0575  -0.0167 0.0164  139 HIS A C   
906  O O   . HIS A 122 ? 0.2064 0.1989 0.1360 0.0197  -0.0159 0.0012  139 HIS A O   
907  C CB  . HIS A 122 ? 0.2002 0.1970 0.1688 0.0317  -0.0287 -0.0046 139 HIS A CB  
908  C CG  . HIS A 122 ? 0.2313 0.2614 0.1892 0.0172  -0.0323 0.0063  139 HIS A CG  
909  N ND1 . HIS A 122 ? 0.2927 0.3084 0.2051 0.0720  -0.0908 0.0082  139 HIS A ND1 
910  C CD2 . HIS A 122 ? 0.1533 0.2466 0.1901 0.0479  -0.0363 -0.0058 139 HIS A CD2 
911  C CE1 . HIS A 122 ? 0.3143 0.2907 0.2024 0.0818  -0.0866 0.0066  139 HIS A CE1 
912  N NE2 . HIS A 122 ? 0.2014 0.2846 0.1962 0.0473  -0.0572 -0.0032 139 HIS A NE2 
913  N N   . GLY A 123 ? 0.2414 0.2065 0.1578 0.0415  -0.0053 0.0002  140 GLY A N   
914  C CA  . GLY A 123 ? 0.1745 0.2067 0.1577 0.0252  -0.0025 0.0221  140 GLY A CA  
915  C C   . GLY A 123 ? 0.1744 0.1851 0.1619 0.0188  -0.0090 0.0158  140 GLY A C   
916  O O   . GLY A 123 ? 0.2495 0.2553 0.1646 0.0541  -0.0243 -0.0289 140 GLY A O   
917  N N   . SER A 124 ? 0.1920 0.2099 0.1702 0.0379  -0.0242 0.0123  141 SER A N   
918  C CA  . SER A 124 ? 0.1741 0.2334 0.1726 0.0330  -0.0090 0.0411  141 SER A CA  
919  C C   . SER A 124 ? 0.2323 0.2335 0.1773 0.0414  -0.0136 0.0234  141 SER A C   
920  O O   . SER A 124 ? 0.2167 0.2654 0.1771 0.0522  0.0175  -0.0015 141 SER A O   
921  C CB  . SER A 124 ? 0.1739 0.2392 0.1773 0.0397  0.0252  0.0341  141 SER A CB  
922  O OG  . SER A 124 ? 0.2003 0.2867 0.1637 0.0520  -0.0001 0.0306  141 SER A OG  
923  N N   . ASP A 125 ? 0.2196 0.2917 0.1847 0.0338  -0.0027 0.0133  142 ASP A N   
924  C CA  . ASP A 125 ? 0.2851 0.2749 0.1976 0.0791  0.0073  -0.0115 142 ASP A CA  
925  C C   . ASP A 125 ? 0.3171 0.2888 0.1990 0.0751  -0.0055 -0.0004 142 ASP A C   
926  O O   . ASP A 125 ? 0.3189 0.3854 0.2130 0.0728  0.0447  -0.0036 142 ASP A O   
927  C CB  . ASP A 125 ? 0.3303 0.3687 0.2263 0.0259  -0.0163 -0.0334 142 ASP A CB  
928  C CG  . ASP A 125 ? 0.4056 0.4301 0.2493 0.0023  -0.0329 -0.0759 142 ASP A CG  
929  O OD1 . ASP A 125 ? 0.3883 0.4164 0.2510 0.0218  -0.0431 -0.0462 142 ASP A OD1 
930  O OD2 . ASP A 125 ? 0.4532 0.5218 0.2779 0.0118  -0.0513 -0.0969 142 ASP A OD2 
931  N N   . SER A 126 ? 0.3071 0.2325 0.1919 0.0313  -0.0398 0.0245  143 SER A N   
932  C CA  . SER A 126 ? 0.2752 0.2511 0.2021 -0.0066 -0.0571 0.0399  143 SER A CA  
933  C C   . SER A 126 ? 0.2449 0.2449 0.2024 0.0068  -0.0386 0.0403  143 SER A C   
934  O O   . SER A 126 ? 0.2356 0.2973 0.1913 0.0254  -0.0342 0.0172  143 SER A O   
935  C CB  . SER A 126 ? 0.3545 0.3096 0.2048 0.0357  -0.0567 0.0120  143 SER A CB  
936  O OG  . SER A 126 ? 0.3480 0.3615 0.2098 0.0533  -0.0736 -0.0056 143 SER A OG  
937  N N   . ALA A 127 ? 0.2596 0.2982 0.2147 0.0372  -0.0355 0.0498  144 ALA A N   
938  C CA  . ALA A 127 ? 0.2547 0.2632 0.2249 -0.0218 -0.0368 0.0388  144 ALA A CA  
939  C C   . ALA A 127 ? 0.2769 0.2827 0.2171 -0.0114 -0.0571 0.0457  144 ALA A C   
940  O O   . ALA A 127 ? 0.3367 0.2848 0.2235 0.0581  -0.0729 0.0408  144 ALA A O   
941  C CB  . ALA A 127 ? 0.2380 0.3500 0.2393 0.0720  -0.0207 0.0408  144 ALA A CB  
942  N N   . GLU A 128 ? 0.2775 0.3015 0.2105 0.0055  -0.0403 0.0282  145 GLU A N   
943  C CA  . GLU A 128 ? 0.2657 0.3548 0.2108 0.0227  -0.0507 0.0428  145 GLU A CA  
944  C C   . GLU A 128 ? 0.2291 0.3338 0.2090 0.0434  -0.0409 0.0394  145 GLU A C   
945  O O   . GLU A 128 ? 0.2555 0.3680 0.2156 -0.0012 -0.0579 0.0295  145 GLU A O   
946  C CB  . GLU A 128 ? 0.2968 0.4723 0.2206 0.0011  -0.0591 0.0715  145 GLU A CB  
947  C CG  . GLU A 128 ? 0.4324 0.5962 0.2390 0.0257  -0.0425 0.0807  145 GLU A CG  
948  C CD  . GLU A 128 ? 0.5379 0.6144 0.2516 0.0328  -0.0601 0.1058  145 GLU A CD  
949  O OE1 . GLU A 128 ? 0.5051 0.4933 0.2505 0.0118  -0.1021 0.0926  145 GLU A OE1 
950  O OE2 . GLU A 128 ? 0.6791 0.7106 0.2699 0.1354  -0.0588 0.1096  145 GLU A OE2 
951  N N   . SER A 129 ? 0.1928 0.3158 0.2011 0.0427  -0.0324 0.0244  146 SER A N   
952  C CA  A SER A 129 ? 0.2034 0.2711 0.2050 0.0345  -0.0334 0.0362  146 SER A CA  
953  C CA  B SER A 129 ? 0.2141 0.2508 0.2013 -0.0044 -0.0288 0.0309  146 SER A CA  
954  C C   . SER A 129 ? 0.2377 0.2783 0.2013 0.0302  -0.0351 0.0238  146 SER A C   
955  O O   . SER A 129 ? 0.2279 0.2872 0.1933 0.0246  -0.0356 0.0084  146 SER A O   
956  C CB  A SER A 129 ? 0.2518 0.3173 0.2130 0.0904  -0.0436 0.0328  146 SER A CB  
957  C CB  B SER A 129 ? 0.2830 0.2772 0.2024 0.0041  -0.0294 0.0239  146 SER A CB  
958  O OG  A SER A 129 ? 0.2368 0.3521 0.2206 0.0696  -0.0608 0.0253  146 SER A OG  
959  O OG  B SER A 129 ? 0.3177 0.2857 0.2033 -0.0395 -0.0374 0.0116  146 SER A OG  
960  N N   . ALA A 130 ? 0.2524 0.2398 0.1986 0.0481  -0.0307 0.0200  147 ALA A N   
961  C CA  . ALA A 130 ? 0.2156 0.2224 0.2051 0.0246  -0.0748 0.0009  147 ALA A CA  
962  C C   . ALA A 130 ? 0.1854 0.2881 0.2153 -0.0026 -0.0765 0.0242  147 ALA A C   
963  O O   . ALA A 130 ? 0.2669 0.2398 0.2148 0.0175  -0.0517 -0.0061 147 ALA A O   
964  C CB  . ALA A 130 ? 0.1896 0.2466 0.2135 0.0273  -0.0651 0.0316  147 ALA A CB  
965  N N   . LYS A 131 ? 0.2134 0.2676 0.2277 0.0368  -0.0642 0.0331  148 LYS A N   
966  C CA  . LYS A 131 ? 0.2190 0.2787 0.2379 0.0015  -0.0730 0.0247  148 LYS A CA  
967  C C   . LYS A 131 ? 0.2542 0.2154 0.2328 0.0414  -0.0868 -0.0065 148 LYS A C   
968  O O   . LYS A 131 ? 0.2626 0.2392 0.2335 0.0513  -0.0475 0.0189  148 LYS A O   
969  C CB  . LYS A 131 ? 0.3015 0.3421 0.2644 0.0307  -0.0386 0.0527  148 LYS A CB  
970  C CG  . LYS A 131 ? 0.4751 0.5425 0.2908 0.2351  -0.0105 0.0820  148 LYS A CG  
971  C CD  . LYS A 131 ? 0.5203 0.7491 0.3189 0.3502  0.0149  0.0675  148 LYS A CD  
972  C CE  . LYS A 131 ? 0.6246 0.9014 0.3378 0.4327  0.0314  0.0548  148 LYS A CE  
973  N NZ  . LYS A 131 ? 0.6372 0.9942 0.3498 0.4501  0.0296  0.0586  148 LYS A NZ  
974  N N   . ARG A 132 ? 0.2286 0.2448 0.2297 0.0630  -0.0811 -0.0200 149 ARG A N   
975  C CA  . ARG A 132 ? 0.2321 0.2649 0.2249 0.0549  -0.0670 0.0246  149 ARG A CA  
976  C C   . ARG A 132 ? 0.2212 0.2309 0.2153 0.0509  -0.0598 -0.0066 149 ARG A C   
977  O O   . ARG A 132 ? 0.2814 0.2678 0.2135 0.0586  -0.0460 -0.0125 149 ARG A O   
978  C CB  . ARG A 132 ? 0.2938 0.2985 0.2232 0.0008  -0.0792 0.0287  149 ARG A CB  
979  C CG  . ARG A 132 ? 0.3173 0.3494 0.2343 -0.0669 -0.0910 0.0156  149 ARG A CG  
980  C CD  . ARG A 132 ? 0.4735 0.3944 0.2492 -0.1721 -0.1060 0.0096  149 ARG A CD  
981  N NE  . ARG A 132 ? 0.6486 0.3445 0.2592 -0.1788 -0.0851 0.0255  149 ARG A NE  
982  C CZ  . ARG A 132 ? 0.8055 0.3962 0.2771 -0.0212 -0.0701 0.0268  149 ARG A CZ  
983  N NH1 . ARG A 132 ? 0.8296 0.3735 0.2920 -0.1021 -0.0387 0.0553  149 ARG A NH1 
984  N NH2 . ARG A 132 ? 0.8214 0.3890 0.2775 0.1810  -0.0940 0.0211  149 ARG A NH2 
985  N N   . GLU A 133 ? 0.1890 0.2846 0.2050 0.0807  -0.0470 -0.0001 150 GLU A N   
986  C CA  . GLU A 133 ? 0.1935 0.2459 0.1997 0.0606  -0.0452 -0.0102 150 GLU A CA  
987  C C   . GLU A 133 ? 0.2505 0.2140 0.2017 0.0795  -0.0201 -0.0136 150 GLU A C   
988  O O   . GLU A 133 ? 0.2654 0.2123 0.1963 0.0378  -0.0074 -0.0146 150 GLU A O   
989  C CB  . GLU A 133 ? 0.1976 0.2260 0.1985 0.0331  -0.0331 -0.0166 150 GLU A CB  
990  C CG  . GLU A 133 ? 0.1581 0.2735 0.1979 0.0047  0.0092  -0.0336 150 GLU A CG  
991  C CD  . GLU A 133 ? 0.2277 0.2238 0.1994 -0.0094 0.0137  -0.0077 150 GLU A CD  
992  O OE1 . GLU A 133 ? 0.2378 0.2814 0.1977 0.0290  -0.0046 -0.0034 150 GLU A OE1 
993  O OE2 . GLU A 133 ? 0.2547 0.2492 0.2086 0.0206  0.0068  -0.0392 150 GLU A OE2 
994  N N   . ILE A 134 ? 0.2744 0.2094 0.1968 0.0111  -0.0417 -0.0017 151 ILE A N   
995  C CA  . ILE A 134 ? 0.2542 0.2374 0.2058 0.0115  -0.0512 0.0044  151 ILE A CA  
996  C C   . ILE A 134 ? 0.2532 0.2131 0.2061 0.0586  -0.0431 -0.0174 151 ILE A C   
997  O O   . ILE A 134 ? 0.2815 0.2840 0.1911 0.0507  -0.0294 -0.0179 151 ILE A O   
998  C CB  . ILE A 134 ? 0.2748 0.2347 0.2236 0.0344  -0.0703 -0.0057 151 ILE A CB  
999  C CG1 . ILE A 134 ? 0.2866 0.1905 0.2380 -0.0169 -0.1040 -0.0017 151 ILE A CG1 
1000 C CG2 . ILE A 134 ? 0.2660 0.2071 0.2334 0.0109  -0.0600 -0.0029 151 ILE A CG2 
1001 C CD1 . ILE A 134 ? 0.2993 0.1937 0.2450 0.0055  -0.0919 -0.0071 151 ILE A CD1 
1002 N N   . SER A 135 ? 0.3166 0.2362 0.2173 0.0719  -0.0576 -0.0014 152 SER A N   
1003 C CA  . SER A 135 ? 0.4201 0.2394 0.2396 0.1026  -0.0363 -0.0071 152 SER A CA  
1004 C C   . SER A 135 ? 0.3217 0.2651 0.2419 0.1008  -0.0349 -0.0268 152 SER A C   
1005 O O   . SER A 135 ? 0.3328 0.3406 0.2405 0.0784  -0.0129 -0.0710 152 SER A O   
1006 C CB  . SER A 135 ? 0.5844 0.3656 0.2546 0.1885  -0.0258 0.0363  152 SER A CB  
1007 O OG  . SER A 135 ? 0.7485 0.4903 0.2701 0.2409  -0.0176 0.0512  152 SER A OG  
1008 N N   . LEU A 136 ? 0.2633 0.2658 0.2414 0.0870  -0.0576 -0.0381 153 LEU A N   
1009 C CA  . LEU A 136 ? 0.2169 0.2640 0.2550 0.0667  -0.0619 -0.0379 153 LEU A CA  
1010 C C   . LEU A 136 ? 0.2344 0.2658 0.2525 0.1055  -0.0566 -0.0432 153 LEU A C   
1011 O O   . LEU A 136 ? 0.2571 0.3575 0.2606 0.1119  -0.0616 -0.0404 153 LEU A O   
1012 C CB  . LEU A 136 ? 0.2264 0.2867 0.2715 0.0428  -0.0710 -0.0563 153 LEU A CB  
1013 C CG  . LEU A 136 ? 0.1681 0.3575 0.2891 0.0124  -0.0474 -0.0778 153 LEU A CG  
1014 C CD1 . LEU A 136 ? 0.2416 0.4198 0.3080 0.0262  -0.0589 -0.0948 153 LEU A CD1 
1015 C CD2 . LEU A 136 ? 0.2602 0.2599 0.2945 0.0299  -0.0673 -0.0991 153 LEU A CD2 
1016 N N   . TRP A 137 ? 0.2000 0.2286 0.2397 0.0888  -0.0492 -0.0113 154 TRP A N   
1017 C CA  . TRP A 137 ? 0.1791 0.2244 0.2312 0.0979  -0.0508 -0.0380 154 TRP A CA  
1018 C C   . TRP A 137 ? 0.2637 0.2034 0.2383 0.0870  -0.0377 -0.0321 154 TRP A C   
1019 O O   . TRP A 137 ? 0.2228 0.2450 0.2451 0.0224  -0.0265 0.0068  154 TRP A O   
1020 C CB  . TRP A 137 ? 0.1888 0.2352 0.2166 0.0410  -0.0179 -0.0198 154 TRP A CB  
1021 C CG  . TRP A 137 ? 0.1951 0.2405 0.2116 0.0700  -0.0173 -0.0062 154 TRP A CG  
1022 C CD1 . TRP A 137 ? 0.2372 0.1663 0.2121 0.0329  -0.0247 0.0081  154 TRP A CD1 
1023 C CD2 . TRP A 137 ? 0.1543 0.2633 0.2059 0.0151  -0.0242 0.0036  154 TRP A CD2 
1024 N NE1 . TRP A 137 ? 0.2051 0.1993 0.2076 0.0318  -0.0131 0.0060  154 TRP A NE1 
1025 C CE2 . TRP A 137 ? 0.1478 0.2452 0.2031 0.0181  -0.0260 0.0056  154 TRP A CE2 
1026 C CE3 . TRP A 137 ? 0.1570 0.2564 0.2023 -0.0056 -0.0180 -0.0039 154 TRP A CE3 
1027 C CZ2 . TRP A 137 ? 0.2019 0.2473 0.1979 0.0240  -0.0343 0.0088  154 TRP A CZ2 
1028 C CZ3 . TRP A 137 ? 0.1686 0.3530 0.1982 -0.0449 -0.0383 0.0138  154 TRP A CZ3 
1029 C CH2 . TRP A 137 ? 0.2140 0.2805 0.2027 -0.0010 -0.0420 0.0087  154 TRP A CH2 
1030 N N   . PHE A 138 ? 0.2210 0.1994 0.2413 0.0326  -0.0597 -0.0229 155 PHE A N   
1031 C CA  . PHE A 138 ? 0.2264 0.1845 0.2477 -0.0138 -0.0256 -0.0203 155 PHE A CA  
1032 C C   . PHE A 138 ? 0.3183 0.2781 0.2754 0.1140  -0.0395 -0.0431 155 PHE A C   
1033 O O   . PHE A 138 ? 0.4534 0.3792 0.2727 0.2199  -0.0733 -0.0670 155 PHE A O   
1034 C CB  . PHE A 138 ? 0.2583 0.2036 0.2242 -0.0088 -0.0118 -0.0106 155 PHE A CB  
1035 C CG  . PHE A 138 ? 0.2147 0.1969 0.2041 0.0282  -0.0041 0.0056  155 PHE A CG  
1036 C CD1 . PHE A 138 ? 0.1987 0.2241 0.1954 0.0158  -0.0186 0.0004  155 PHE A CD1 
1037 C CD2 . PHE A 138 ? 0.2172 0.2070 0.1971 -0.0016 -0.0212 0.0122  155 PHE A CD2 
1038 C CE1 . PHE A 138 ? 0.2010 0.2142 0.1938 0.0050  0.0174  -0.0061 155 PHE A CE1 
1039 C CE2 . PHE A 138 ? 0.1995 0.1892 0.1954 0.0238  0.0020  0.0195  155 PHE A CE2 
1040 C CZ  . PHE A 138 ? 0.1681 0.2586 0.1939 0.0504  0.0084  -0.0178 155 PHE A CZ  
1041 N N   . LYS A 139 ? 0.2556 0.2439 0.3031 0.0531  -0.0247 -0.0521 156 LYS A N   
1042 C CA  . LYS A 139 ? 0.2353 0.2787 0.3306 0.0147  -0.0063 -0.0448 156 LYS A CA  
1043 C C   . LYS A 139 ? 0.2204 0.2137 0.3258 0.0845  0.0033  -0.0282 156 LYS A C   
1044 O O   . LYS A 139 ? 0.2135 0.2597 0.3189 0.0859  0.0146  -0.0037 156 LYS A O   
1045 C CB  . LYS A 139 ? 0.2844 0.3028 0.3605 0.0079  0.0415  -0.0166 156 LYS A CB  
1046 C CG  . LYS A 139 ? 0.4120 0.4470 0.3851 -0.0041 0.0560  0.0094  156 LYS A CG  
1047 C CD  . LYS A 139 ? 0.5490 0.5974 0.4077 0.0054  0.0640  0.0427  156 LYS A CD  
1048 C CE  . LYS A 139 ? 0.6744 0.7877 0.4249 0.0826  0.0448  0.0381  156 LYS A CE  
1049 N NZ  . LYS A 139 ? 0.7291 0.8993 0.4325 0.1216  0.0229  0.0312  156 LYS A NZ  
1050 N N   . PRO A 140 ? 0.2195 0.2737 0.3295 0.0785  -0.0432 -0.0139 157 PRO A N   
1051 C CA  . PRO A 140 ? 0.3088 0.2087 0.3263 0.0886  -0.0711 0.0086  157 PRO A CA  
1052 C C   . PRO A 140 ? 0.2791 0.2331 0.3162 0.0452  -0.0422 -0.0021 157 PRO A C   
1053 O O   . PRO A 140 ? 0.2715 0.2584 0.3042 0.0577  -0.0080 0.0020  157 PRO A O   
1054 C CB  . PRO A 140 ? 0.3536 0.2867 0.3315 0.0700  -0.1036 0.0213  157 PRO A CB  
1055 C CG  . PRO A 140 ? 0.3450 0.3600 0.3331 0.0807  -0.1383 0.0108  157 PRO A CG  
1056 C CD  . PRO A 140 ? 0.3446 0.2953 0.3360 0.1133  -0.1087 -0.0024 157 PRO A CD  
1057 N N   . GLU A 141 ? 0.2601 0.2563 0.3237 0.0908  -0.0459 -0.0328 158 GLU A N   
1058 C CA  . GLU A 141 ? 0.2456 0.2627 0.3186 0.1123  -0.0373 -0.0633 158 GLU A CA  
1059 C C   . GLU A 141 ? 0.2243 0.2358 0.2866 0.0349  -0.0043 -0.0721 158 GLU A C   
1060 O O   . GLU A 141 ? 0.2709 0.2844 0.2721 0.0401  0.0060  -0.1069 158 GLU A O   
1061 C CB  . GLU A 141 ? 0.3054 0.4165 0.3520 0.1545  -0.0387 -0.0830 158 GLU A CB  
1062 C CG  . GLU A 141 ? 0.3749 0.6099 0.3878 0.2033  -0.0381 -0.1124 158 GLU A CG  
1063 C CD  . GLU A 141 ? 0.4314 0.7175 0.4234 0.2485  -0.0305 -0.1397 158 GLU A CD  
1064 O OE1 . GLU A 141 ? 0.3440 0.5926 0.4432 0.1231  -0.0334 -0.1783 158 GLU A OE1 
1065 O OE2 . GLU A 141 ? 0.4486 0.7914 0.4381 0.1875  -0.0036 -0.1211 158 GLU A OE2 
1066 N N   . GLU A 142 ? 0.1894 0.2433 0.2682 0.0182  0.0275  -0.0280 159 GLU A N   
1067 C CA  . GLU A 142 ? 0.1806 0.2198 0.2543 0.0254  0.0047  -0.0122 159 GLU A CA  
1068 C C   . GLU A 142 ? 0.1857 0.2073 0.2280 0.0185  0.0127  -0.0222 159 GLU A C   
1069 O O   . GLU A 142 ? 0.1921 0.2622 0.2143 0.0533  0.0029  -0.0020 159 GLU A O   
1070 C CB  . GLU A 142 ? 0.1617 0.2592 0.2728 0.0017  0.0014  -0.0122 159 GLU A CB  
1071 C CG  . GLU A 142 ? 0.2164 0.2955 0.2965 -0.0268 0.0149  -0.0112 159 GLU A CG  
1072 C CD  . GLU A 142 ? 0.2940 0.2913 0.3133 -0.1004 0.0182  0.0138  159 GLU A CD  
1073 O OE1 . GLU A 142 ? 0.3779 0.3293 0.3144 -0.0197 0.0528  0.0228  159 GLU A OE1 
1074 O OE2 . GLU A 142 ? 0.5067 0.3806 0.3316 -0.0588 0.0328  0.0137  159 GLU A OE2 
1075 N N   . ILE A 143 ? 0.1911 0.2101 0.2300 -0.0005 -0.0105 0.0021  160 ILE A N   
1076 C CA  . ILE A 143 ? 0.1716 0.2178 0.2272 0.0196  -0.0314 0.0057  160 ILE A CA  
1077 C C   . ILE A 143 ? 0.1968 0.2077 0.2308 0.0543  -0.0209 0.0010  160 ILE A C   
1078 O O   . ILE A 143 ? 0.2351 0.1951 0.2574 0.0278  -0.0319 -0.0211 160 ILE A O   
1079 C CB  . ILE A 143 ? 0.1968 0.2377 0.2321 0.0584  -0.0169 0.0045  160 ILE A CB  
1080 C CG1 . ILE A 143 ? 0.2538 0.2683 0.2540 0.0735  0.0127  0.0139  160 ILE A CG1 
1081 C CG2 . ILE A 143 ? 0.2309 0.2750 0.2304 0.0980  -0.0006 0.0086  160 ILE A CG2 
1082 C CD1 . ILE A 143 ? 0.3140 0.3507 0.2606 0.0638  -0.0024 0.0068  160 ILE A CD1 
1083 N N   . GLN A 144 ? 0.1933 0.1988 0.2150 0.0720  -0.0022 -0.0014 161 GLN A N   
1084 C CA  . GLN A 144 ? 0.2198 0.2103 0.2131 0.0622  -0.0100 -0.0238 161 GLN A CA  
1085 C C   . GLN A 144 ? 0.2082 0.2159 0.2015 0.0261  0.0016  -0.0541 161 GLN A C   
1086 O O   . GLN A 144 ? 0.2168 0.2410 0.2279 0.0348  0.0351  -0.0248 161 GLN A O   
1087 C CB  . GLN A 144 ? 0.1743 0.2366 0.2148 0.0048  -0.0046 0.0024  161 GLN A CB  
1088 C CG  . GLN A 144 ? 0.1618 0.2082 0.2110 0.0531  -0.0062 0.0041  161 GLN A CG  
1089 C CD  . GLN A 144 ? 0.2506 0.2387 0.2039 0.0948  -0.0111 0.0029  161 GLN A CD  
1090 O OE1 . GLN A 144 ? 0.3222 0.2560 0.2228 0.0524  0.0123  0.0014  161 GLN A OE1 
1091 N NE2 . GLN A 144 ? 0.2421 0.2797 0.1980 0.0496  -0.0364 0.0160  161 GLN A NE2 
1092 N N   . SER A 145 ? 0.2381 0.2009 0.1931 0.0095  -0.0098 0.0028  162 SER A N   
1093 C CA  A SER A 145 ? 0.2098 0.1890 0.2092 0.0127  -0.0023 0.0126  162 SER A CA  
1094 C CA  B SER A 145 ? 0.2256 0.1830 0.2013 0.0042  -0.0114 -0.0141 162 SER A CA  
1095 C C   . SER A 145 ? 0.1902 0.1991 0.2111 0.0045  0.0082  -0.0147 162 SER A C   
1096 O O   . SER A 145 ? 0.2379 0.2400 0.2256 0.0401  0.0027  -0.0256 162 SER A O   
1097 C CB  A SER A 145 ? 0.2352 0.2005 0.2184 0.0280  0.0193  0.0670  162 SER A CB  
1098 C CB  B SER A 145 ? 0.2797 0.1648 0.1960 -0.0094 -0.0151 -0.0155 162 SER A CB  
1099 O OG  A SER A 145 ? 0.2550 0.2969 0.2360 0.0383  0.0140  0.0934  162 SER A OG  
1100 O OG  B SER A 145 ? 0.3224 0.2340 0.1994 -0.0045 -0.0418 -0.0272 162 SER A OG  
1101 N N   . TYR A 146 ? 0.2142 0.2357 0.2026 0.0199  -0.0034 -0.0053 163 TYR A N   
1102 C CA  . TYR A 146 ? 0.2315 0.1739 0.1988 0.0359  0.0209  -0.0008 163 TYR A CA  
1103 C C   . TYR A 146 ? 0.1696 0.1588 0.2105 0.0410  0.0239  0.0048  163 TYR A C   
1104 O O   . TYR A 146 ? 0.2447 0.1659 0.2201 0.0273  0.0126  -0.0051 163 TYR A O   
1105 C CB  . TYR A 146 ? 0.1814 0.2353 0.1773 0.0040  0.0189  0.0104  163 TYR A CB  
1106 C CG  . TYR A 146 ? 0.2059 0.1452 0.1693 0.0132  0.0266  0.0141  163 TYR A CG  
1107 C CD1 . TYR A 146 ? 0.1863 0.1936 0.1680 -0.0065 0.0170  -0.0005 163 TYR A CD1 
1108 C CD2 . TYR A 146 ? 0.1993 0.2186 0.1620 0.0687  0.0076  -0.0038 163 TYR A CD2 
1109 C CE1 . TYR A 146 ? 0.2624 0.1941 0.1753 0.0132  -0.0224 -0.0011 163 TYR A CE1 
1110 C CE2 . TYR A 146 ? 0.1796 0.2218 0.1646 0.0583  -0.0019 -0.0036 163 TYR A CE2 
1111 C CZ  . TYR A 146 ? 0.2143 0.1885 0.1694 0.0438  -0.0140 0.0061  163 TYR A CZ  
1112 O OH  . TYR A 146 ? 0.1997 0.2058 0.1862 0.0291  0.0062  0.0173  163 TYR A OH  
1113 N N   . LYS A 147 ? 0.1482 0.2459 0.2197 0.0010  -0.0015 0.0002  164 LYS A N   
1114 C CA  . LYS A 147 ? 0.1843 0.2168 0.2158 0.0157  0.0455  0.0435  164 LYS A CA  
1115 C C   . LYS A 147 ? 0.2130 0.1786 0.1934 0.0613  0.0048  0.0200  164 LYS A C   
1116 O O   . LYS A 147 ? 0.2299 0.2465 0.1806 0.0456  0.0218  -0.0078 164 LYS A O   
1117 C CB  . LYS A 147 ? 0.2481 0.2669 0.2440 -0.0124 0.0623  0.0347  164 LYS A CB  
1118 C CG  . LYS A 147 ? 0.3889 0.2364 0.2819 0.0030  0.0826  0.0739  164 LYS A CG  
1119 C CD  . LYS A 147 ? 0.5540 0.3145 0.3136 0.0613  0.1034  0.0749  164 LYS A CD  
1120 C CE  . LYS A 147 ? 0.7194 0.4976 0.3307 0.1638  0.1075  0.0819  164 LYS A CE  
1121 N NZ  . LYS A 147 ? 0.8507 0.6737 0.3465 0.2419  0.0778  0.0749  164 LYS A NZ  
1122 N N   . LEU A 148 ? 0.2003 0.2013 0.2009 0.0032  -0.0109 0.0230  165 LEU A N   
1123 C CA  . LEU A 148 ? 0.2039 0.2314 0.2007 0.0505  -0.0013 0.0167  165 LEU A CA  
1124 C C   . LEU A 148 ? 0.1952 0.2615 0.2003 0.0363  -0.0087 0.0353  165 LEU A C   
1125 O O   . LEU A 148 ? 0.2338 0.2317 0.2010 0.0069  0.0027  0.0238  165 LEU A O   
1126 C CB  . LEU A 148 ? 0.2081 0.2516 0.2061 0.0545  0.0069  -0.0134 165 LEU A CB  
1127 C CG  . LEU A 148 ? 0.1799 0.2662 0.2146 0.0492  0.0103  -0.0045 165 LEU A CG  
1128 C CD1 . LEU A 148 ? 0.1892 0.2825 0.2140 0.0387  -0.0021 0.0243  165 LEU A CD1 
1129 C CD2 . LEU A 148 ? 0.2089 0.2644 0.2254 0.0241  -0.0004 -0.0078 165 LEU A CD2 
1130 N N   . ALA A 149 ? 0.2251 0.2495 0.2031 0.0028  -0.0373 0.0162  166 ALA A N   
1131 C CA  . ALA A 149 ? 0.2238 0.2637 0.2107 0.0290  -0.0224 -0.0075 166 ALA A CA  
1132 C C   . ALA A 149 ? 0.2332 0.2625 0.2148 0.0675  -0.0258 -0.0170 166 ALA A C   
1133 O O   . ALA A 149 ? 0.2491 0.2601 0.2364 -0.0084 -0.0112 -0.0095 166 ALA A O   
1134 C CB  . ALA A 149 ? 0.2620 0.3965 0.2134 0.0310  -0.0134 -0.0536 166 ALA A CB  
1135 N N   . LEU A 150 ? 0.1804 0.2272 0.2110 0.0096  0.0085  0.0140  167 LEU A N   
1136 C CA  . LEU A 150 ? 0.1627 0.2514 0.2077 0.0325  0.0281  0.0164  167 LEU A CA  
1137 C C   . LEU A 150 ? 0.2280 0.1947 0.2066 -0.0073 0.0099  -0.0003 167 LEU A C   
1138 O O   . LEU A 150 ? 0.2060 0.2372 0.2096 0.0211  0.0035  0.0087  167 LEU A O   
1139 C CB  . LEU A 150 ? 0.2676 0.2755 0.2077 0.0853  0.0279  0.0185  167 LEU A CB  
1140 C CG  . LEU A 150 ? 0.2841 0.2997 0.2157 -0.0164 -0.0006 0.0432  167 LEU A CG  
1141 C CD1 . LEU A 150 ? 0.3225 0.3898 0.2196 0.0962  -0.0141 0.0391  167 LEU A CD1 
1142 C CD2 . LEU A 150 ? 0.4028 0.4496 0.2341 0.0133  -0.0416 0.0246  167 LEU A CD2 
1143 N N   . SER A 151 ? 0.2062 0.2630 0.1997 0.0283  0.0004  0.0029  168 SER A N   
1144 C CA  A SER A 151 ? 0.2343 0.2537 0.1951 0.0525  0.0062  0.0195  168 SER A CA  
1145 C CA  B SER A 151 ? 0.1803 0.2540 0.2012 0.0526  0.0075  0.0179  168 SER A CA  
1146 C C   . SER A 151 ? 0.2175 0.2086 0.1997 0.0042  0.0164  0.0116  168 SER A C   
1147 O O   . SER A 151 ? 0.2590 0.2582 0.1839 0.0604  0.0172  0.0416  168 SER A O   
1148 C CB  A SER A 151 ? 0.3075 0.3216 0.1886 0.0734  -0.0004 0.0273  168 SER A CB  
1149 C CB  B SER A 151 ? 0.2147 0.3609 0.2079 0.0664  -0.0001 0.0111  168 SER A CB  
1150 O OG  A SER A 151 ? 0.3721 0.3123 0.1849 0.0500  -0.0079 0.0215  168 SER A OG  
1151 O OG  B SER A 151 ? 0.2848 0.3675 0.2186 0.0495  0.0065  0.0009  168 SER A OG  
1152 N N   . ASP A 152 ? 0.2389 0.2073 0.2177 0.0080  0.0224  0.0002  169 ASP A N   
1153 C CA  . ASP A 152 ? 0.2587 0.2523 0.2332 0.0273  0.0286  0.0051  169 ASP A CA  
1154 C C   . ASP A 152 ? 0.2650 0.2526 0.2130 0.0153  0.0683  0.0620  169 ASP A C   
1155 O O   . ASP A 152 ? 0.2867 0.2612 0.2320 0.0481  0.0684  0.0685  169 ASP A O   
1156 C CB  . ASP A 152 ? 0.3809 0.2457 0.2774 -0.0164 0.0533  -0.0281 169 ASP A CB  
1157 C CG  . ASP A 152 ? 0.5150 0.3495 0.3121 0.0275  0.0595  -0.0050 169 ASP A CG  
1158 O OD1 . ASP A 152 ? 0.6630 0.3456 0.3296 0.0696  0.0623  0.0283  169 ASP A OD1 
1159 O OD2 . ASP A 152 ? 0.5760 0.4535 0.3366 0.0860  0.0697  -0.0277 169 ASP A OD2 
1160 N N   . TYR A 153 ? 0.2078 0.2259 0.1929 -0.0137 0.0096  0.0132  170 TYR A N   
1161 C CA  . TYR A 153 ? 0.2001 0.1870 0.1890 0.0205  0.0184  0.0264  170 TYR A CA  
1162 C C   . TYR A 153 ? 0.2020 0.1937 0.2012 0.0151  -0.0058 -0.0054 170 TYR A C   
1163 O O   . TYR A 153 ? 0.2229 0.2595 0.2048 0.0435  0.0104  -0.0014 170 TYR A O   
1164 C CB  . TYR A 153 ? 0.1644 0.2364 0.1812 -0.0082 0.0314  0.0304  170 TYR A CB  
1165 C CG  . TYR A 153 ? 0.2140 0.2611 0.1871 0.0072  0.0123  0.0432  170 TYR A CG  
1166 C CD1 . TYR A 153 ? 0.2058 0.2231 0.1888 -0.0185 0.0059  0.0610  170 TYR A CD1 
1167 C CD2 . TYR A 153 ? 0.2337 0.2936 0.1923 -0.0016 0.0145  0.0087  170 TYR A CD2 
1168 C CE1 . TYR A 153 ? 0.2266 0.3240 0.2036 0.0008  0.0045  0.0347  170 TYR A CE1 
1169 C CE2 . TYR A 153 ? 0.2641 0.2596 0.1989 0.0224  0.0212  0.0371  170 TYR A CE2 
1170 C CZ  . TYR A 153 ? 0.2595 0.2997 0.2137 -0.0500 -0.0016 0.0048  170 TYR A CZ  
1171 O OH  . TYR A 153 ? 0.2914 0.2875 0.2455 -0.0332 -0.0161 0.0015  170 TYR A OH  
1172 N N   . ILE A 154 ? 0.2028 0.2424 0.2088 0.0326  -0.0197 -0.0232 171 ILE A N   
1173 C CA  . ILE A 154 ? 0.1934 0.2641 0.2100 0.0403  -0.0392 -0.0385 171 ILE A CA  
1174 C C   . ILE A 154 ? 0.2017 0.3214 0.2139 0.0256  -0.0147 -0.0199 171 ILE A C   
1175 O O   . ILE A 154 ? 0.2353 0.2884 0.2132 0.0490  0.0078  -0.0321 171 ILE A O   
1176 C CB  . ILE A 154 ? 0.2452 0.2653 0.2045 0.0126  -0.0381 -0.0243 171 ILE A CB  
1177 C CG1 . ILE A 154 ? 0.2050 0.3379 0.2135 -0.0183 -0.0250 -0.0045 171 ILE A CG1 
1178 C CG2 . ILE A 154 ? 0.2303 0.2282 0.2153 0.0143  -0.0264 -0.0096 171 ILE A CG2 
1179 C CD1 . ILE A 154 ? 0.3061 0.2830 0.2172 -0.0454 -0.0286 -0.0143 171 ILE A CD1 
1180 N N   . PHE A 155 ? 0.2375 0.2654 0.2172 0.0277  -0.0041 0.0260  172 PHE A N   
1181 C CA  . PHE A 155 ? 0.2132 0.2422 0.2333 -0.0254 -0.0023 0.0474  172 PHE A CA  
1182 C C   . PHE A 155 ? 0.2855 0.2897 0.2632 -0.0491 0.0096  0.0542  172 PHE A C   
1183 O O   . PHE A 155 ? 0.3021 0.3589 0.2608 -0.0325 0.0155  0.0348  172 PHE A O   
1184 C CB  . PHE A 155 ? 0.2694 0.2754 0.2267 0.0332  -0.0280 0.0067  172 PHE A CB  
1185 C CG  . PHE A 155 ? 0.2625 0.2511 0.2238 0.0513  0.0079  -0.0057 172 PHE A CG  
1186 C CD1 . PHE A 155 ? 0.2317 0.2894 0.2285 0.0190  0.0030  0.0110  172 PHE A CD1 
1187 C CD2 . PHE A 155 ? 0.2415 0.2685 0.2310 0.0424  0.0365  0.0200  172 PHE A CD2 
1188 C CE1 . PHE A 155 ? 0.1839 0.2703 0.2316 -0.0283 0.0058  0.0185  172 PHE A CE1 
1189 C CE2 . PHE A 155 ? 0.2232 0.2921 0.2353 -0.0185 0.0336  0.0386  172 PHE A CE2 
1190 C CZ  . PHE A 155 ? 0.2674 0.2597 0.2317 -0.0154 0.0206  0.0237  172 PHE A CZ  
1191 N N   . GLU A 156 ? 0.3624 0.3418 0.2913 -0.0544 0.0338  0.0633  173 GLU A N   
1192 C CA  . GLU A 156 ? 0.4827 0.4427 0.3261 -0.1525 0.0707  0.0872  173 GLU A CA  
1193 C C   . GLU A 156 ? 0.6692 0.4336 0.3514 -0.1043 0.0896  0.1351  173 GLU A C   
1194 O O   . GLU A 156 ? 0.7090 0.5336 0.3605 -0.1381 0.1014  0.1397  173 GLU A O   
1195 C CB  . GLU A 156 ? 0.5250 0.5307 0.3436 -0.1128 0.0825  0.0718  173 GLU A CB  
1196 C CG  . GLU A 156 ? 0.5393 0.5478 0.3486 -0.0364 0.0873  0.0836  173 GLU A CG  
1197 C CD  . GLU A 156 ? 0.5043 0.4085 0.3389 -0.0268 0.0685  0.1155  173 GLU A CD  
1198 O OE1 . GLU A 156 ? 0.5504 0.5410 0.3547 0.1301  0.0632  0.0941  173 GLU A OE1 
1199 O OE2 . GLU A 156 ? 0.4451 0.3199 0.3284 0.0583  0.0666  0.0988  173 GLU A OE2 
1200 O OXT . GLU A 156 ? 0.7948 0.4715 0.3670 -0.0403 0.0705  0.1318  173 GLU A OXT 
1201 N N   . HIS B 8   ? 0.4009 0.8294 0.4012 -0.0172 -0.1069 0.0070  25  HIS B N   
1202 C CA  . HIS B 8   ? 0.3887 0.7213 0.3869 -0.0658 -0.1008 -0.0107 25  HIS B CA  
1203 C C   . HIS B 8   ? 0.3605 0.5899 0.3690 -0.0513 -0.0807 0.0153  25  HIS B C   
1204 O O   . HIS B 8   ? 0.4413 0.6467 0.3829 -0.0705 -0.0992 0.0272  25  HIS B O   
1205 C CB  . HIS B 8   ? 0.5295 0.7926 0.3937 0.0106  -0.0978 -0.0228 25  HIS B CB  
1206 N N   . VAL B 9   ? 0.3212 0.4318 0.3419 -0.0517 -0.0584 -0.0238 26  VAL B N   
1207 C CA  . VAL B 9   ? 0.2696 0.2883 0.3133 -0.0160 -0.0540 -0.0449 26  VAL B CA  
1208 C C   . VAL B 9   ? 0.2776 0.2644 0.3017 -0.0401 -0.0423 -0.0537 26  VAL B C   
1209 O O   . VAL B 9   ? 0.3403 0.2914 0.3227 -0.0107 -0.0377 -0.0389 26  VAL B O   
1210 C CB  . VAL B 9   ? 0.3022 0.2863 0.3059 0.0361  -0.0259 -0.0372 26  VAL B CB  
1211 C CG1 . VAL B 9   ? 0.3536 0.3140 0.3115 0.0950  -0.0069 -0.0242 26  VAL B CG1 
1212 C CG2 . VAL B 9   ? 0.3438 0.3454 0.3049 -0.0011 -0.0423 -0.0603 26  VAL B CG2 
1213 N N   . GLU B 10  ? 0.2382 0.2618 0.2710 -0.0074 -0.0512 -0.0147 27  GLU B N   
1214 C CA  . GLU B 10  ? 0.2268 0.2925 0.2477 0.0248  -0.0263 -0.0372 27  GLU B CA  
1215 C C   . GLU B 10  ? 0.2297 0.2331 0.2085 -0.0002 -0.0269 -0.0328 27  GLU B C   
1216 O O   . GLU B 10  ? 0.2409 0.2559 0.1868 0.0206  -0.0349 -0.0268 27  GLU B O   
1217 C CB  . GLU B 10  ? 0.4189 0.4117 0.2736 0.1712  0.0117  -0.0314 27  GLU B CB  
1218 C CG  . GLU B 10  ? 0.4088 0.3285 0.2784 0.0491  0.0149  -0.0507 27  GLU B CG  
1219 C CD  . GLU B 10  ? 0.4302 0.3104 0.2761 0.0790  -0.0163 -0.1122 27  GLU B CD  
1220 O OE1 . GLU B 10  ? 0.4452 0.4673 0.3173 -0.0410 -0.0109 -0.1130 27  GLU B OE1 
1221 O OE2 . GLU B 10  ? 0.3126 0.3026 0.2644 0.0175  0.0125  -0.0374 27  GLU B OE2 
1222 N N   . GLN B 11  ? 0.2323 0.2783 0.1963 0.0046  -0.0132 -0.0114 28  GLN B N   
1223 C CA  . GLN B 11  ? 0.2674 0.2424 0.1976 0.0335  -0.0107 -0.0213 28  GLN B CA  
1224 C C   . GLN B 11  ? 0.2976 0.1914 0.1795 0.0102  0.0157  -0.0131 28  GLN B C   
1225 O O   . GLN B 11  ? 0.2906 0.2949 0.1721 0.0404  0.0155  -0.0544 28  GLN B O   
1226 C CB  . GLN B 11  ? 0.2189 0.2501 0.2188 0.0317  -0.0087 -0.0279 28  GLN B CB  
1227 C CG  . GLN B 11  ? 0.3243 0.2834 0.2418 0.0868  0.0207  0.0117  28  GLN B CG  
1228 C CD  . GLN B 11  ? 0.3540 0.2786 0.2545 0.0414  0.0312  0.0062  28  GLN B CD  
1229 O OE1 . GLN B 11  ? 0.4260 0.3186 0.2649 0.1305  0.0354  0.0139  28  GLN B OE1 
1230 N NE2 . GLN B 11  ? 0.4020 0.2847 0.2671 0.0155  0.0425  -0.0103 28  GLN B NE2 
1231 N N   . THR B 12  ? 0.2791 0.2169 0.1692 0.0253  0.0136  -0.0286 29  THR B N   
1232 C CA  . THR B 12  ? 0.2697 0.2074 0.1747 0.0230  0.0048  -0.0139 29  THR B CA  
1233 C C   . THR B 12  ? 0.2684 0.2116 0.1661 0.0310  0.0096  -0.0162 29  THR B C   
1234 O O   . THR B 12  ? 0.2615 0.2548 0.1655 0.0704  0.0121  -0.0236 29  THR B O   
1235 C CB  . THR B 12  ? 0.2681 0.2244 0.1929 0.0128  0.0069  -0.0468 29  THR B CB  
1236 O OG1 . THR B 12  ? 0.2510 0.3022 0.2070 0.0671  0.0126  -0.0040 29  THR B OG1 
1237 C CG2 . THR B 12  ? 0.2177 0.2451 0.2023 0.0032  -0.0062 -0.0214 29  THR B CG2 
1238 N N   . TYR B 13  ? 0.2183 0.2161 0.1628 0.0499  -0.0034 -0.0109 30  TYR B N   
1239 C CA  . TYR B 13  ? 0.2400 0.2589 0.1566 0.1153  0.0041  0.0149  30  TYR B CA  
1240 C C   . TYR B 13  ? 0.2686 0.2315 0.1610 0.0668  -0.0004 -0.0156 30  TYR B C   
1241 O O   . TYR B 13  ? 0.2256 0.2599 0.1665 0.0192  0.0081  -0.0196 30  TYR B O   
1242 C CB  . TYR B 13  ? 0.3030 0.2577 0.1598 0.1097  0.0063  0.0268  30  TYR B CB  
1243 C CG  . TYR B 13  ? 0.2693 0.2391 0.1469 0.0288  0.0072  -0.0089 30  TYR B CG  
1244 C CD1 . TYR B 13  ? 0.2624 0.2397 0.1484 0.0487  -0.0055 0.0052  30  TYR B CD1 
1245 C CD2 . TYR B 13  ? 0.2743 0.2181 0.1432 0.0215  -0.0147 -0.0100 30  TYR B CD2 
1246 C CE1 . TYR B 13  ? 0.2627 0.2617 0.1668 0.1030  0.0061  0.0036  30  TYR B CE1 
1247 C CE2 . TYR B 13  ? 0.2879 0.2479 0.1643 0.0551  -0.0102 0.0006  30  TYR B CE2 
1248 C CZ  . TYR B 13  ? 0.2754 0.2280 0.1675 0.1270  0.0091  -0.0043 30  TYR B CZ  
1249 O OH  . TYR B 13  ? 0.3216 0.2475 0.1815 0.0973  -0.0090 0.0093  30  TYR B OH  
1250 N N   . LEU B 14  ? 0.2138 0.1968 0.1601 0.0153  -0.0084 -0.0232 31  LEU B N   
1251 C CA  . LEU B 14  ? 0.2278 0.1991 0.1693 0.0352  0.0043  0.0173  31  LEU B CA  
1252 C C   . LEU B 14  ? 0.2474 0.2303 0.1719 0.0980  -0.0133 0.0138  31  LEU B C   
1253 O O   . LEU B 14  ? 0.2648 0.3646 0.1705 0.0733  -0.0157 0.0659  31  LEU B O   
1254 C CB  . LEU B 14  ? 0.2757 0.2383 0.1757 0.0653  -0.0133 0.0043  31  LEU B CB  
1255 C CG  . LEU B 14  ? 0.2489 0.3488 0.1874 0.0969  -0.0053 0.0042  31  LEU B CG  
1256 C CD1 . LEU B 14  ? 0.2970 0.3663 0.1851 0.0540  0.0064  0.0194  31  LEU B CD1 
1257 C CD2 . LEU B 14  ? 0.4384 0.4023 0.1887 0.2002  0.0484  0.0307  31  LEU B CD2 
1258 N N   . MET B 15  ? 0.2142 0.2253 0.1685 0.0901  -0.0250 -0.0085 32  MET B N   
1259 C CA  . MET B 15  ? 0.1876 0.2125 0.1690 0.0743  -0.0127 0.0187  32  MET B CA  
1260 C C   . MET B 15  ? 0.2248 0.2249 0.1456 0.0350  0.0075  0.0401  32  MET B C   
1261 O O   . MET B 15  ? 0.2584 0.2334 0.1482 0.0367  0.0103  0.0297  32  MET B O   
1262 C CB  . MET B 15  ? 0.2401 0.2288 0.2014 0.0968  -0.0264 -0.0276 32  MET B CB  
1263 C CG  . MET B 15  ? 0.2538 0.3008 0.2156 0.1211  -0.0323 -0.0401 32  MET B CG  
1264 S SD  . MET B 15  ? 0.2862 0.2851 0.2406 0.1060  -0.0252 -0.0257 32  MET B SD  
1265 C CE  . MET B 15  ? 0.3044 0.2841 0.2363 0.1211  -0.0221 -0.0503 32  MET B CE  
1266 N N   . ILE B 16  ? 0.1809 0.2634 0.1310 0.0530  0.0073  0.0345  33  ILE B N   
1267 C CA  . ILE B 16  ? 0.1769 0.2558 0.1430 0.0558  0.0013  0.0138  33  ILE B CA  
1268 C C   . ILE B 16  ? 0.1984 0.1584 0.1555 0.0340  0.0050  0.0254  33  ILE B C   
1269 O O   . ILE B 16  ? 0.2411 0.1875 0.1700 0.0790  0.0059  0.0355  33  ILE B O   
1270 C CB  . ILE B 16  ? 0.1831 0.2491 0.1494 0.0335  -0.0018 -0.0066 33  ILE B CB  
1271 C CG1 . ILE B 16  ? 0.2263 0.2196 0.1613 0.0709  0.0044  -0.0015 33  ILE B CG1 
1272 C CG2 . ILE B 16  ? 0.1953 0.2318 0.1469 0.0762  0.0075  0.0177  33  ILE B CG2 
1273 C CD1 . ILE B 16  ? 0.2732 0.2476 0.1667 0.1163  0.0202  -0.0041 33  ILE B CD1 
1274 N N   . LYS B 17  ? 0.1989 0.2155 0.1589 0.0450  0.0165  0.0089  34  LYS B N   
1275 C CA  . LYS B 17  ? 0.2276 0.2480 0.1583 0.0817  0.0279  -0.0116 34  LYS B CA  
1276 C C   . LYS B 17  ? 0.1893 0.2134 0.1563 0.0434  0.0192  -0.0048 34  LYS B C   
1277 O O   . LYS B 17  ? 0.2299 0.2313 0.1562 0.0638  -0.0007 0.0191  34  LYS B O   
1278 C CB  . LYS B 17  ? 0.2033 0.2147 0.1553 0.0338  0.0238  -0.0282 34  LYS B CB  
1279 C CG  . LYS B 17  ? 0.2151 0.2241 0.1458 0.0498  0.0146  -0.0234 34  LYS B CG  
1280 C CD  . LYS B 17  ? 0.2278 0.2043 0.1457 0.0517  0.0217  -0.0280 34  LYS B CD  
1281 C CE  . LYS B 17  ? 0.2413 0.2671 0.1406 0.0555  0.0307  -0.0262 34  LYS B CE  
1282 N NZ  . LYS B 17  ? 0.3564 0.2961 0.1422 0.0280  0.0200  -0.0406 34  LYS B NZ  
1283 N N   . PRO B 18  ? 0.2017 0.2252 0.1538 0.0527  0.0261  -0.0112 35  PRO B N   
1284 C CA  . PRO B 18  ? 0.1640 0.2689 0.1615 0.0328  -0.0065 -0.0097 35  PRO B CA  
1285 C C   . PRO B 18  ? 0.1699 0.2674 0.1593 0.0329  0.0086  -0.0093 35  PRO B C   
1286 O O   . PRO B 18  ? 0.1943 0.2383 0.1656 0.0347  0.0052  -0.0165 35  PRO B O   
1287 C CB  . PRO B 18  ? 0.1892 0.2848 0.1647 0.1066  0.0038  0.0044  35  PRO B CB  
1288 C CG  . PRO B 18  ? 0.2314 0.2623 0.1630 0.0737  -0.0222 -0.0132 35  PRO B CG  
1289 C CD  . PRO B 18  ? 0.2393 0.2551 0.1624 0.0616  0.0094  0.0023  35  PRO B CD  
1290 N N   . ASP B 19  ? 0.1728 0.2580 0.1593 0.0634  0.0138  0.0163  36  ASP B N   
1291 C CA  . ASP B 19  ? 0.1994 0.2744 0.1617 0.0666  0.0286  0.0207  36  ASP B CA  
1292 C C   . ASP B 19  ? 0.2248 0.2672 0.1599 0.0506  0.0497  0.0239  36  ASP B C   
1293 O O   . ASP B 19  ? 0.2233 0.2318 0.1560 0.0303  0.0341  0.0191  36  ASP B O   
1294 C CB  . ASP B 19  ? 0.2366 0.2137 0.1553 0.0446  0.0182  0.0126  36  ASP B CB  
1295 C CG  . ASP B 19  ? 0.1993 0.2815 0.1660 0.0382  0.0275  0.0265  36  ASP B CG  
1296 O OD1 . ASP B 19  ? 0.2572 0.2502 0.1659 0.0230  0.0125  0.0227  36  ASP B OD1 
1297 O OD2 . ASP B 19  ? 0.2305 0.2622 0.1656 0.0445  0.0182  0.0144  36  ASP B OD2 
1298 N N   . GLY B 20  ? 0.1929 0.2245 0.1564 0.0396  0.0256  0.0294  37  GLY B N   
1299 C CA  . GLY B 20  ? 0.1610 0.1976 0.1616 0.0323  0.0288  0.0342  37  GLY B CA  
1300 C C   . GLY B 20  ? 0.1717 0.2276 0.1617 0.0262  0.0013  0.0108  37  GLY B C   
1301 O O   . GLY B 20  ? 0.2234 0.2346 0.1669 0.0683  -0.0167 0.0132  37  GLY B O   
1302 N N   . ILE B 21  ? 0.2326 0.2038 0.1530 0.0437  0.0086  0.0118  38  ILE B N   
1303 C CA  . ILE B 21  ? 0.2189 0.2339 0.1421 0.0428  0.0144  0.0328  38  ILE B CA  
1304 C C   . ILE B 21  ? 0.1929 0.2293 0.1328 0.0290  0.0225  0.0236  38  ILE B C   
1305 O O   . ILE B 21  ? 0.2411 0.2816 0.1346 0.0804  0.0174  0.0237  38  ILE B O   
1306 C CB  . ILE B 21  ? 0.2154 0.2047 0.1511 0.0248  -0.0186 0.0208  38  ILE B CB  
1307 C CG1 . ILE B 21  ? 0.3023 0.2729 0.1686 0.1057  0.0129  0.0206  38  ILE B CG1 
1308 C CG2 . ILE B 21  ? 0.2506 0.2386 0.1529 0.0482  0.0053  0.0556  38  ILE B CG2 
1309 C CD1 . ILE B 21  ? 0.3255 0.2957 0.1844 0.1060  0.0203  0.0339  38  ILE B CD1 
1310 N N   . GLN B 22  ? 0.1831 0.2592 0.1338 0.0566  0.0253  0.0210  39  GLN B N   
1311 C CA  . GLN B 22  ? 0.1882 0.2675 0.1416 0.0365  0.0109  0.0021  39  GLN B CA  
1312 C C   . GLN B 22  ? 0.1872 0.2633 0.1480 0.0779  -0.0137 -0.0069 39  GLN B C   
1313 O O   . GLN B 22  ? 0.2244 0.2282 0.1542 0.0487  0.0141  -0.0075 39  GLN B O   
1314 C CB  . GLN B 22  ? 0.1983 0.2416 0.1512 0.0560  0.0326  -0.0135 39  GLN B CB  
1315 C CG  . GLN B 22  ? 0.2264 0.2799 0.1653 0.0806  0.0018  0.0022  39  GLN B CG  
1316 C CD  . GLN B 22  ? 0.2929 0.2764 0.1810 0.1614  -0.0191 -0.0129 39  GLN B CD  
1317 O OE1 . GLN B 22  ? 0.3387 0.2587 0.2025 0.1224  -0.0421 -0.0300 39  GLN B OE1 
1318 N NE2 . GLN B 22  ? 0.2873 0.2934 0.1852 0.1093  -0.0199 0.0187  39  GLN B NE2 
1319 N N   . ARG B 23  ? 0.1956 0.2494 0.1389 0.0784  -0.0109 0.0020  40  ARG B N   
1320 C CA  . ARG B 23  ? 0.2121 0.2444 0.1533 0.0718  0.0002  -0.0019 40  ARG B CA  
1321 C C   . ARG B 23  ? 0.2153 0.2642 0.1506 0.0562  0.0096  -0.0091 40  ARG B C   
1322 O O   . ARG B 23  ? 0.2433 0.2842 0.1663 0.0545  -0.0078 0.0016  40  ARG B O   
1323 C CB  . ARG B 23  ? 0.1793 0.2635 0.1595 0.0824  -0.0259 0.0039  40  ARG B CB  
1324 C CG  . ARG B 23  ? 0.1921 0.2561 0.1535 0.0787  -0.0082 0.0032  40  ARG B CG  
1325 C CD  . ARG B 23  ? 0.2026 0.2312 0.1570 0.0456  0.0189  0.0203  40  ARG B CD  
1326 N NE  . ARG B 23  ? 0.2320 0.2038 0.1655 0.0226  -0.0051 0.0355  40  ARG B NE  
1327 C CZ  . ARG B 23  ? 0.2685 0.2235 0.1614 0.1174  0.0155  0.0388  40  ARG B CZ  
1328 N NH1 . ARG B 23  ? 0.2651 0.2396 0.1495 0.0378  0.0226  0.0082  40  ARG B NH1 
1329 N NH2 . ARG B 23  ? 0.2332 0.2508 0.1728 0.0769  0.0058  0.0144  40  ARG B NH2 
1330 N N   . GLN B 24  ? 0.2091 0.2414 0.1394 0.0606  0.0089  0.0009  41  GLN B N   
1331 C CA  . GLN B 24  ? 0.2009 0.2926 0.1330 0.1011  0.0081  -0.0114 41  GLN B CA  
1332 C C   . GLN B 24  ? 0.2235 0.2735 0.1409 0.0677  0.0084  0.0109  41  GLN B C   
1333 O O   . GLN B 24  ? 0.2282 0.2738 0.1534 0.0678  -0.0080 0.0126  41  GLN B O   
1334 C CB  . GLN B 24  ? 0.2304 0.3448 0.1415 0.0945  -0.0150 0.0216  41  GLN B CB  
1335 C CG  . GLN B 24  ? 0.2251 0.3375 0.1497 0.0852  0.0276  0.0175  41  GLN B CG  
1336 C CD  . GLN B 24  ? 0.2402 0.3154 0.1551 0.0751  0.0135  0.0138  41  GLN B CD  
1337 O OE1 . GLN B 24  ? 0.2736 0.3597 0.1611 0.1210  -0.0069 -0.0048 41  GLN B OE1 
1338 N NE2 . GLN B 24  ? 0.2620 0.3049 0.1561 0.0631  -0.0276 0.0001  41  GLN B NE2 
1339 N N   . VAL B 25  ? 0.2028 0.2359 0.1386 0.0466  -0.0009 0.0071  42  VAL B N   
1340 C CA  . VAL B 25  ? 0.1858 0.2701 0.1383 0.0533  -0.0028 0.0289  42  VAL B CA  
1341 C C   . VAL B 25  ? 0.1710 0.2322 0.1399 0.0336  0.0082  0.0410  42  VAL B C   
1342 O O   . VAL B 25  ? 0.1810 0.2606 0.1444 0.0432  0.0151  0.0177  42  VAL B O   
1343 C CB  . VAL B 25  ? 0.1694 0.3075 0.1516 0.0323  0.0298  0.0423  42  VAL B CB  
1344 C CG1 . VAL B 25  ? 0.2092 0.3699 0.1586 0.0664  0.0667  0.0791  42  VAL B CG1 
1345 C CG2 . VAL B 25  ? 0.2043 0.3031 0.1607 0.0669  0.0548  0.0523  42  VAL B CG2 
1346 N N   . VAL B 26  ? 0.1582 0.1875 0.1391 0.0352  -0.0004 0.0117  43  VAL B N   
1347 C CA  . VAL B 26  ? 0.1878 0.2010 0.1428 0.0204  -0.0054 0.0046  43  VAL B CA  
1348 C C   . VAL B 26  ? 0.1977 0.1736 0.1369 0.0464  0.0031  0.0079  43  VAL B C   
1349 O O   . VAL B 26  ? 0.1961 0.2331 0.1400 0.0434  0.0047  0.0480  43  VAL B O   
1350 C CB  . VAL B 26  ? 0.1971 0.2382 0.1532 0.0496  0.0047  0.0185  43  VAL B CB  
1351 C CG1 . VAL B 26  ? 0.2271 0.2084 0.1714 0.0166  0.0020  0.0139  43  VAL B CG1 
1352 C CG2 . VAL B 26  ? 0.2048 0.2241 0.1493 0.0926  0.0296  0.0330  43  VAL B CG2 
1353 N N   . GLY B 27  ? 0.1742 0.2030 0.1400 0.0493  0.0036  -0.0104 44  GLY B N   
1354 C CA  . GLY B 27  ? 0.1522 0.2776 0.1441 0.1040  0.0298  0.0203  44  GLY B CA  
1355 C C   . GLY B 27  ? 0.2042 0.2366 0.1431 0.0588  0.0217  0.0270  44  GLY B C   
1356 O O   . GLY B 27  ? 0.2125 0.2104 0.1447 0.0540  0.0229  0.0064  44  GLY B O   
1357 N N   . GLU B 28  ? 0.1735 0.2087 0.1549 0.0504  0.0194  0.0236  45  GLU B N   
1358 C CA  . GLU B 28  ? 0.2144 0.1550 0.1632 0.0427  0.0114  0.0326  45  GLU B CA  
1359 C C   . GLU B 28  ? 0.2392 0.1906 0.1519 0.0722  0.0222  0.0385  45  GLU B C   
1360 O O   . GLU B 28  ? 0.2067 0.2431 0.1385 0.0784  -0.0099 0.0209  45  GLU B O   
1361 C CB  . GLU B 28  ? 0.2568 0.1720 0.2052 0.0050  -0.0138 0.0050  45  GLU B CB  
1362 C CG  . GLU B 28  ? 0.2972 0.2226 0.2431 0.0329  -0.0091 0.0245  45  GLU B CG  
1363 C CD  . GLU B 28  ? 0.4169 0.3212 0.2797 -0.0094 -0.0016 0.0268  45  GLU B CD  
1364 O OE1 . GLU B 28  ? 0.4361 0.3834 0.2728 -0.0844 0.0461  0.0145  45  GLU B OE1 
1365 O OE2 . GLU B 28  ? 0.3989 0.3609 0.3098 0.0042  -0.0074 0.0389  45  GLU B OE2 
1366 N N   . ILE B 29  ? 0.2115 0.1908 0.1527 0.0406  -0.0010 0.0144  46  ILE B N   
1367 C CA  . ILE B 29  ? 0.2051 0.1871 0.1317 0.0227  0.0095  -0.0069 46  ILE B CA  
1368 C C   . ILE B 29  ? 0.2013 0.2243 0.1311 0.0318  0.0152  0.0208  46  ILE B C   
1369 O O   . ILE B 29  ? 0.2199 0.2464 0.1247 0.0571  0.0097  -0.0113 46  ILE B O   
1370 C CB  . ILE B 29  ? 0.1977 0.2410 0.1357 0.0541  0.0329  0.0119  46  ILE B CB  
1371 C CG1 . ILE B 29  ? 0.2074 0.2600 0.1410 0.0738  0.0251  0.0289  46  ILE B CG1 
1372 C CG2 . ILE B 29  ? 0.2403 0.2719 0.1509 0.0359  0.0120  -0.0229 46  ILE B CG2 
1373 C CD1 . ILE B 29  ? 0.2372 0.2528 0.1537 0.0700  -0.0049 0.0072  46  ILE B CD1 
1374 N N   . ILE B 30  ? 0.1687 0.2472 0.1391 0.0415  -0.0052 0.0172  47  ILE B N   
1375 C CA  . ILE B 30  ? 0.1796 0.2251 0.1502 0.0355  -0.0165 0.0161  47  ILE B CA  
1376 C C   . ILE B 30  ? 0.1514 0.2250 0.1545 0.0352  -0.0003 0.0160  47  ILE B C   
1377 O O   . ILE B 30  ? 0.1873 0.2034 0.1642 0.0340  -0.0091 0.0196  47  ILE B O   
1378 C CB  . ILE B 30  ? 0.1803 0.2057 0.1520 0.0280  -0.0036 0.0420  47  ILE B CB  
1379 C CG1 . ILE B 30  ? 0.2033 0.2013 0.1544 0.0562  -0.0125 0.0099  47  ILE B CG1 
1380 C CG2 . ILE B 30  ? 0.2085 0.2222 0.1502 0.0454  -0.0073 0.0123  47  ILE B CG2 
1381 C CD1 . ILE B 30  ? 0.2646 0.2228 0.1595 0.0736  -0.0167 0.0331  47  ILE B CD1 
1382 N N   . SER B 31  ? 0.1795 0.2176 0.1399 0.0430  -0.0027 0.0019  48  SER B N   
1383 C CA  . SER B 31  ? 0.1554 0.2097 0.1351 0.0428  -0.0099 0.0241  48  SER B CA  
1384 C C   . SER B 31  ? 0.1668 0.2133 0.1410 0.0405  -0.0145 0.0160  48  SER B C   
1385 O O   . SER B 31  ? 0.2142 0.2180 0.1451 0.0546  -0.0208 0.0242  48  SER B O   
1386 C CB  . SER B 31  ? 0.1788 0.2077 0.1248 0.0417  -0.0152 0.0234  48  SER B CB  
1387 O OG  . SER B 31  ? 0.2258 0.2185 0.1229 0.0451  -0.0015 0.0143  48  SER B OG  
1388 N N   . ARG B 32  ? 0.1943 0.2215 0.1491 0.0441  -0.0208 -0.0003 49  ARG B N   
1389 C CA  . ARG B 32  ? 0.1884 0.1622 0.1517 0.0240  0.0013  0.0090  49  ARG B CA  
1390 C C   . ARG B 32  ? 0.2033 0.1926 0.1458 0.0276  -0.0015 0.0034  49  ARG B C   
1391 O O   . ARG B 32  ? 0.1984 0.2383 0.1402 0.0527  -0.0023 0.0192  49  ARG B O   
1392 C CB  . ARG B 32  ? 0.2110 0.2115 0.1680 0.0376  0.0057  0.0160  49  ARG B CB  
1393 C CG  . ARG B 32  ? 0.1871 0.2443 0.1850 -0.0079 0.0177  0.0281  49  ARG B CG  
1394 C CD  . ARG B 32  ? 0.2795 0.3762 0.2169 -0.0329 0.0114  -0.0171 49  ARG B CD  
1395 N NE  . ARG B 32  ? 0.2714 0.3584 0.2340 -0.0078 0.0193  -0.0057 49  ARG B NE  
1396 C CZ  . ARG B 32  ? 0.2822 0.2800 0.2330 0.0202  0.0313  -0.0012 49  ARG B CZ  
1397 N NH1 . ARG B 32  ? 0.2843 0.2628 0.2301 0.0160  0.0389  -0.0004 49  ARG B NH1 
1398 N NH2 . ARG B 32  ? 0.2448 0.3189 0.2444 -0.0049 0.0286  -0.0192 49  ARG B NH2 
1399 N N   . PHE B 33  ? 0.1993 0.1791 0.1419 0.0384  -0.0039 0.0007  50  PHE B N   
1400 C CA  . PHE B 33  ? 0.1974 0.2157 0.1541 0.0270  -0.0056 -0.0087 50  PHE B CA  
1401 C C   . PHE B 33  ? 0.1860 0.2133 0.1347 0.0286  -0.0191 0.0001  50  PHE B C   
1402 O O   . PHE B 33  ? 0.2414 0.1954 0.1390 0.0121  -0.0071 -0.0229 50  PHE B O   
1403 C CB  . PHE B 33  ? 0.2200 0.1959 0.1649 0.0337  -0.0032 -0.0108 50  PHE B CB  
1404 C CG  . PHE B 33  ? 0.2163 0.2233 0.1566 0.0622  0.0046  -0.0143 50  PHE B CG  
1405 C CD1 . PHE B 33  ? 0.2524 0.2673 0.1574 0.1223  -0.0065 -0.0221 50  PHE B CD1 
1406 C CD2 . PHE B 33  ? 0.1687 0.2875 0.1529 0.0548  0.0112  0.0021  50  PHE B CD2 
1407 C CE1 . PHE B 33  ? 0.2250 0.2642 0.1683 0.0922  -0.0077 -0.0250 50  PHE B CE1 
1408 C CE2 . PHE B 33  ? 0.1968 0.3342 0.1594 0.0710  -0.0123 0.0017  50  PHE B CE2 
1409 C CZ  . PHE B 33  ? 0.2022 0.2990 0.1663 0.0525  -0.0054 0.0139  50  PHE B CZ  
1410 N N   . GLU B 34  ? 0.1817 0.2288 0.1248 0.0387  -0.0414 0.0092  51  GLU B N   
1411 C CA  . GLU B 34  ? 0.1689 0.2474 0.1362 0.0283  -0.0065 0.0278  51  GLU B CA  
1412 C C   . GLU B 34  ? 0.1869 0.2325 0.1363 0.0334  -0.0001 0.0107  51  GLU B C   
1413 O O   . GLU B 34  ? 0.2089 0.2230 0.1457 0.0479  -0.0174 0.0188  51  GLU B O   
1414 C CB  . GLU B 34  ? 0.2047 0.2669 0.1440 0.0506  -0.0220 0.0341  51  GLU B CB  
1415 C CG  . GLU B 34  ? 0.2038 0.2639 0.1535 0.0234  -0.0109 0.0355  51  GLU B CG  
1416 C CD  . GLU B 34  ? 0.2179 0.2794 0.1541 0.0530  -0.0034 0.0141  51  GLU B CD  
1417 O OE1 . GLU B 34  ? 0.1875 0.2463 0.1529 0.0402  -0.0025 0.0180  51  GLU B OE1 
1418 O OE2 . GLU B 34  ? 0.2155 0.2246 0.1528 0.0396  -0.0130 0.0036  51  GLU B OE2 
1419 N N   . LYS B 35  ? 0.1846 0.2123 0.1490 0.0223  0.0235  0.0364  52  LYS B N   
1420 C CA  . LYS B 35  ? 0.1770 0.2043 0.1537 0.0236  -0.0139 0.0061  52  LYS B CA  
1421 C C   . LYS B 35  ? 0.1414 0.1915 0.1560 0.0219  -0.0056 -0.0037 52  LYS B C   
1422 O O   . LYS B 35  ? 0.1660 0.2366 0.1611 0.0459  -0.0045 -0.0036 52  LYS B O   
1423 C CB  . LYS B 35  ? 0.2040 0.2443 0.1663 0.0517  -0.0383 0.0392  52  LYS B CB  
1424 C CG  . LYS B 35  ? 0.2053 0.2709 0.1754 -0.0397 -0.0126 0.0508  52  LYS B CG  
1425 C CD  . LYS B 35  ? 0.2984 0.3636 0.2029 0.0467  -0.0109 -0.0107 52  LYS B CD  
1426 C CE  . LYS B 35  ? 0.4150 0.5115 0.2279 0.0877  -0.0234 -0.0464 52  LYS B CE  
1427 N NZ  . LYS B 35  ? 0.4356 0.5531 0.2375 0.1029  -0.0482 -0.0993 52  LYS B NZ  
1428 N N   . ARG B 36  ? 0.1654 0.1682 0.1491 0.0239  -0.0102 0.0086  53  ARG B N   
1429 C CA  . ARG B 36  ? 0.1821 0.2015 0.1481 0.0169  -0.0346 -0.0070 53  ARG B CA  
1430 C C   . ARG B 36  ? 0.1639 0.1862 0.1433 0.0330  -0.0263 0.0255  53  ARG B C   
1431 O O   . ARG B 36  ? 0.1659 0.2572 0.1543 0.0409  -0.0103 -0.0143 53  ARG B O   
1432 C CB  . ARG B 36  ? 0.1726 0.2062 0.1478 0.0373  -0.0276 -0.0011 53  ARG B CB  
1433 C CG  . ARG B 36  ? 0.2044 0.2079 0.1532 0.0037  -0.0299 -0.0026 53  ARG B CG  
1434 C CD  . ARG B 36  ? 0.2253 0.1815 0.1400 0.0043  -0.0370 -0.0043 53  ARG B CD  
1435 N NE  . ARG B 36  ? 0.2016 0.2122 0.1445 0.0392  0.0144  -0.0069 53  ARG B NE  
1436 C CZ  . ARG B 36  ? 0.1930 0.1926 0.1599 0.0668  0.0221  -0.0017 53  ARG B CZ  
1437 N NH1 . ARG B 36  ? 0.1820 0.2411 0.1657 0.0488  0.0351  -0.0026 53  ARG B NH1 
1438 N NH2 . ARG B 36  ? 0.2090 0.2340 0.1696 0.0825  -0.0285 0.0003  53  ARG B NH2 
1439 N N   . GLY B 37  ? 0.1773 0.2031 0.1448 0.0432  -0.0001 0.0130  54  GLY B N   
1440 C CA  . GLY B 37  ? 0.1915 0.1759 0.1550 0.0188  0.0106  -0.0067 54  GLY B CA  
1441 C C   . GLY B 37  ? 0.1874 0.1807 0.1588 0.0395  0.0075  -0.0028 54  GLY B C   
1442 O O   . GLY B 37  ? 0.1940 0.2313 0.1751 -0.0060 0.0221  0.0053  54  GLY B O   
1443 N N   . TYR B 38  ? 0.1949 0.1828 0.1568 0.0469  0.0055  0.0203  55  TYR B N   
1444 C CA  . TYR B 38  ? 0.1779 0.2036 0.1535 0.0523  0.0008  0.0157  55  TYR B CA  
1445 C C   . TYR B 38  ? 0.1732 0.2500 0.1498 0.0112  -0.0068 -0.0014 55  TYR B C   
1446 O O   . TYR B 38  ? 0.2265 0.2220 0.1627 0.0192  -0.0133 0.0058  55  TYR B O   
1447 C CB  . TYR B 38  ? 0.1996 0.2487 0.1513 0.0384  -0.0076 -0.0098 55  TYR B CB  
1448 C CG  . TYR B 38  ? 0.1702 0.2463 0.1457 0.0414  -0.0167 -0.0110 55  TYR B CG  
1449 C CD1 . TYR B 38  ? 0.2088 0.2416 0.1489 0.0202  -0.0066 0.0049  55  TYR B CD1 
1450 C CD2 . TYR B 38  ? 0.1844 0.2067 0.1435 0.0166  0.0044  -0.0085 55  TYR B CD2 
1451 C CE1 . TYR B 38  ? 0.1880 0.2310 0.1533 0.0444  -0.0066 -0.0025 55  TYR B CE1 
1452 C CE2 . TYR B 38  ? 0.1961 0.2184 0.1487 0.0229  -0.0053 -0.0141 55  TYR B CE2 
1453 C CZ  . TYR B 38  ? 0.2035 0.2330 0.1504 0.0613  -0.0059 0.0017  55  TYR B CZ  
1454 O OH  . TYR B 38  ? 0.2421 0.2173 0.1566 -0.0011 -0.0232 0.0072  55  TYR B OH  
1455 N N   . ARG B 39  ? 0.1965 0.1904 0.1444 0.0059  -0.0221 0.0201  56  ARG B N   
1456 C CA  . ARG B 39  ? 0.2308 0.2043 0.1569 0.0056  -0.0083 0.0304  56  ARG B CA  
1457 C C   . ARG B 39  ? 0.2474 0.1619 0.1575 0.0376  0.0019  0.0115  56  ARG B C   
1458 O O   . ARG B 39  ? 0.2344 0.2036 0.1478 0.0415  -0.0069 -0.0030 56  ARG B O   
1459 C CB  . ARG B 39  ? 0.2097 0.2075 0.1635 0.0382  0.0161  0.0263  56  ARG B CB  
1460 C CG  . ARG B 39  ? 0.2040 0.2228 0.1577 -0.0295 0.0087  0.0231  56  ARG B CG  
1461 C CD  . ARG B 39  ? 0.2798 0.2073 0.1620 -0.0009 0.0102  -0.0085 56  ARG B CD  
1462 N NE  . ARG B 39  ? 0.2365 0.2544 0.1646 0.0025  0.0032  0.0026  56  ARG B NE  
1463 C CZ  . ARG B 39  ? 0.2518 0.2685 0.1858 -0.0434 -0.0062 0.0037  56  ARG B CZ  
1464 N NH1 . ARG B 39  ? 0.2959 0.2512 0.1987 0.0410  -0.0297 0.0348  56  ARG B NH1 
1465 N NH2 . ARG B 39  ? 0.2631 0.2764 0.1977 -0.0109 -0.0071 -0.0065 56  ARG B NH2 
1466 N N   . ILE B 40  ? 0.1982 0.2547 0.1653 0.0382  -0.0142 0.0213  57  ILE B N   
1467 C CA  . ILE B 40  ? 0.1773 0.2772 0.1705 0.0444  -0.0073 -0.0057 57  ILE B CA  
1468 C C   . ILE B 40  ? 0.1963 0.2225 0.1888 0.0326  0.0072  -0.0046 57  ILE B C   
1469 O O   . ILE B 40  ? 0.2376 0.2557 0.1915 0.0488  -0.0047 0.0398  57  ILE B O   
1470 C CB  . ILE B 40  ? 0.1710 0.2347 0.1728 0.0096  -0.0188 -0.0258 57  ILE B CB  
1471 C CG1 . ILE B 40  ? 0.2209 0.2581 0.1671 0.0401  -0.0156 -0.0268 57  ILE B CG1 
1472 C CG2 . ILE B 40  ? 0.2018 0.2175 0.1818 0.0218  -0.0058 0.0001  57  ILE B CG2 
1473 C CD1 . ILE B 40  ? 0.2308 0.2728 0.1620 0.0172  -0.0456 0.0005  57  ILE B CD1 
1474 N N   . ALA B 41  ? 0.2461 0.2055 0.2021 0.0513  0.0092  -0.0185 58  ALA B N   
1475 C CA  . ALA B 41  ? 0.1887 0.2388 0.2074 0.0469  0.0087  -0.0173 58  ALA B CA  
1476 C C   . ALA B 41  ? 0.1990 0.2527 0.2180 0.0283  0.0130  0.0150  58  ALA B C   
1477 O O   . ALA B 41  ? 0.2253 0.2593 0.2323 0.0423  0.0044  0.0185  58  ALA B O   
1478 C CB  . ALA B 41  ? 0.2146 0.2710 0.2081 0.0181  -0.0309 -0.0355 58  ALA B CB  
1479 N N   . ALA B 42  ? 0.1821 0.2535 0.2177 0.0269  -0.0035 0.0063  59  ALA B N   
1480 C CA  . ALA B 42  ? 0.2301 0.2537 0.2014 0.0344  0.0129  -0.0151 59  ALA B CA  
1481 C C   . ALA B 42  ? 0.2053 0.2151 0.1921 0.0494  0.0208  0.0098  59  ALA B C   
1482 O O   . ALA B 42  ? 0.2243 0.2449 0.1968 0.0621  0.0097  0.0361  59  ALA B O   
1483 C CB  . ALA B 42  ? 0.2784 0.2761 0.1990 0.0760  0.0223  -0.0036 59  ALA B CB  
1484 N N   . MET B 43  ? 0.1917 0.3121 0.1931 0.0731  0.0165  0.0300  60  MET B N   
1485 C CA  . MET B 43  ? 0.1898 0.2871 0.1936 0.0666  0.0062  0.0295  60  MET B CA  
1486 C C   . MET B 43  ? 0.2300 0.3365 0.1834 0.0635  -0.0012 0.0497  60  MET B C   
1487 O O   . MET B 43  ? 0.2988 0.3414 0.1695 0.0767  0.0369  0.0915  60  MET B O   
1488 C CB  . MET B 43  ? 0.2499 0.2837 0.2012 0.0369  0.0082  -0.0072 60  MET B CB  
1489 C CG  . MET B 43  ? 0.2392 0.3415 0.2128 0.0000  0.0148  0.0165  60  MET B CG  
1490 S SD  . MET B 43  ? 0.2864 0.3067 0.2077 0.0173  0.0037  0.0225  60  MET B SD  
1491 C CE  . MET B 43  ? 0.2528 0.2563 0.2075 0.0094  0.0283  0.0463  60  MET B CE  
1492 N N   . LYS B 44  ? 0.2092 0.2966 0.1974 0.0628  0.0052  0.0545  61  LYS B N   
1493 C CA  . LYS B 44  ? 0.2588 0.3066 0.2210 0.0156  -0.0202 0.0184  61  LYS B CA  
1494 C C   . LYS B 44  ? 0.2077 0.2902 0.2006 0.0237  -0.0228 0.0308  61  LYS B C   
1495 O O   . LYS B 44  ? 0.2465 0.3194 0.2010 0.0677  0.0163  0.0463  61  LYS B O   
1496 C CB  . LYS B 44  ? 0.3446 0.2655 0.2710 0.0525  -0.0396 0.0387  61  LYS B CB  
1497 C CG  . LYS B 44  ? 0.4622 0.3378 0.2905 0.1049  -0.0082 0.0083  61  LYS B CG  
1498 C CD  . LYS B 44  ? 0.5227 0.4203 0.2934 0.1248  0.0028  -0.0285 61  LYS B CD  
1499 C CE  . LYS B 44  ? 0.5151 0.3430 0.2927 0.1869  0.0072  -0.0092 61  LYS B CE  
1500 N NZ  . LYS B 44  ? 0.5412 0.3695 0.2958 0.1846  0.0077  -0.0064 61  LYS B NZ  
1501 N N   . LEU B 45  ? 0.2121 0.2852 0.1860 0.0870  0.0020  0.0119  62  LEU B N   
1502 C CA  . LEU B 45  ? 0.2649 0.2028 0.1798 0.0649  0.0129  0.0127  62  LEU B CA  
1503 C C   . LEU B 45  ? 0.2687 0.2386 0.1776 0.0861  0.0118  0.0192  62  LEU B C   
1504 O O   . LEU B 45  ? 0.2443 0.2522 0.1936 0.0253  0.0091  0.0295  62  LEU B O   
1505 C CB  . LEU B 45  ? 0.2718 0.2672 0.1822 0.0899  0.0110  0.0195  62  LEU B CB  
1506 C CG  . LEU B 45  ? 0.2655 0.2577 0.1863 0.0764  -0.0028 0.0111  62  LEU B CG  
1507 C CD1 . LEU B 45  ? 0.3266 0.2480 0.1994 0.0731  0.0010  0.0179  62  LEU B CD1 
1508 C CD2 . LEU B 45  ? 0.3046 0.3175 0.1950 0.0948  -0.0262 0.0170  62  LEU B CD2 
1509 N N   . THR B 46  ? 0.2282 0.2269 0.1763 0.0671  0.0207  0.0216  63  THR B N   
1510 C CA  . THR B 46  ? 0.2237 0.2052 0.1974 0.0633  0.0313  0.0252  63  THR B CA  
1511 C C   . THR B 46  ? 0.2307 0.1833 0.2070 0.0536  0.0050  0.0166  63  THR B C   
1512 O O   . THR B 46  ? 0.2538 0.2222 0.2308 0.0761  0.0234  0.0197  63  THR B O   
1513 C CB  . THR B 46  ? 0.2983 0.2279 0.2153 0.0865  0.0286  0.0338  63  THR B CB  
1514 O OG1 . THR B 46  ? 0.3547 0.2499 0.2407 0.1208  0.0181  -0.0085 63  THR B OG1 
1515 C CG2 . THR B 46  ? 0.2949 0.2973 0.2159 0.0426  -0.0119 0.0290  63  THR B CG2 
1516 N N   . ILE B 47  ? 0.2316 0.2381 0.1964 0.0607  0.0185  0.0418  64  ILE B N   
1517 C CA  . ILE B 47  ? 0.2628 0.2499 0.1909 0.1117  0.0273  0.0095  64  ILE B CA  
1518 C C   . ILE B 47  ? 0.2409 0.2498 0.1952 0.1040  0.0326  0.0281  64  ILE B C   
1519 O O   . ILE B 47  ? 0.2862 0.2357 0.2068 0.0698  0.0163  0.0078  64  ILE B O   
1520 C CB  . ILE B 47  ? 0.2634 0.2790 0.1998 0.1029  0.0329  0.0101  64  ILE B CB  
1521 C CG1 . ILE B 47  ? 0.2725 0.3352 0.1878 0.1179  0.0272  0.0184  64  ILE B CG1 
1522 C CG2 . ILE B 47  ? 0.2956 0.4217 0.2109 0.1324  -0.0189 -0.0148 64  ILE B CG2 
1523 C CD1 . ILE B 47  ? 0.3400 0.3477 0.1977 0.1551  0.0160  0.0021  64  ILE B CD1 
1524 N N   . ALA B 48  ? 0.2026 0.2846 0.1991 0.0934  0.0253  0.0403  65  ALA B N   
1525 C CA  . ALA B 48  ? 0.2350 0.2072 0.2050 0.0525  0.0143  0.0252  65  ALA B CA  
1526 C C   . ALA B 48  ? 0.2515 0.2328 0.2147 0.0621  0.0039  0.0049  65  ALA B C   
1527 O O   . ALA B 48  ? 0.2632 0.2363 0.2279 0.0670  0.0427  0.0110  65  ALA B O   
1528 C CB  . ALA B 48  ? 0.2537 0.2000 0.1918 0.0501  -0.0033 0.0245  65  ALA B CB  
1529 N N   . THR B 49  ? 0.2742 0.2081 0.2086 0.0828  -0.0316 -0.0139 66  THR B N   
1530 C CA  . THR B 49  ? 0.2555 0.2012 0.2112 0.0873  -0.0154 -0.0025 66  THR B CA  
1531 C C   . THR B 49  ? 0.2046 0.2289 0.2140 0.0343  -0.0301 0.0009  66  THR B C   
1532 O O   . THR B 49  ? 0.2687 0.1997 0.2294 0.0637  -0.0219 0.0038  66  THR B O   
1533 C CB  . THR B 49  ? 0.3271 0.1923 0.2184 0.0834  0.0180  0.0120  66  THR B CB  
1534 O OG1 . THR B 49  ? 0.3579 0.2581 0.2365 0.1087  0.0132  0.0072  66  THR B OG1 
1535 C CG2 . THR B 49  ? 0.3449 0.3175 0.2176 0.1407  0.0468  0.0417  66  THR B CG2 
1536 N N   . PRO B 50  ? 0.2784 0.2436 0.2157 0.0685  0.0153  0.0174  67  PRO B N   
1537 C CA  . PRO B 50  ? 0.3037 0.2646 0.2168 0.0421  0.0463  0.0492  67  PRO B CA  
1538 C C   . PRO B 50  ? 0.2960 0.2562 0.2207 0.0980  0.0431  0.0377  67  PRO B C   
1539 O O   . PRO B 50  ? 0.3606 0.2563 0.2172 0.1244  0.0340  0.0486  67  PRO B O   
1540 C CB  . PRO B 50  ? 0.3278 0.3047 0.2174 0.0925  0.0599  0.0410  67  PRO B CB  
1541 C CG  . PRO B 50  ? 0.2964 0.3190 0.2262 0.1019  0.0340  0.0047  67  PRO B CG  
1542 C CD  . PRO B 50  ? 0.3319 0.2975 0.2270 0.0903  0.0221  0.0191  67  PRO B CD  
1543 N N   . ALA B 51  ? 0.2725 0.2500 0.2304 0.0275  0.0359  0.0107  68  ALA B N   
1544 C CA  . ALA B 51  ? 0.2935 0.2227 0.2374 0.1403  0.0227  0.0015  68  ALA B CA  
1545 C C   . ALA B 51  ? 0.2869 0.2166 0.2328 0.1016  0.0162  0.0114  68  ALA B C   
1546 O O   . ALA B 51  ? 0.3081 0.2849 0.2296 0.0893  -0.0088 0.0124  68  ALA B O   
1547 C CB  . ALA B 51  ? 0.4108 0.1680 0.2392 0.1006  0.0032  0.0318  68  ALA B CB  
1548 N N   . ILE B 52  ? 0.3192 0.2522 0.2295 0.1101  0.0377  0.0091  69  ILE B N   
1549 C CA  A ILE B 52  ? 0.2834 0.2335 0.2328 0.0737  0.0219  0.0194  69  ILE B CA  
1550 C CA  B ILE B 52  ? 0.3294 0.2483 0.2369 0.0895  0.0346  0.0221  69  ILE B CA  
1551 C C   . ILE B 52  ? 0.2950 0.2184 0.2337 0.0507  0.0100  0.0128  69  ILE B C   
1552 O O   . ILE B 52  ? 0.3205 0.2458 0.2339 0.0774  -0.0255 -0.0227 69  ILE B O   
1553 C CB  A ILE B 52  ? 0.2563 0.2974 0.2395 0.1382  0.0149  0.0016  69  ILE B CB  
1554 C CB  B ILE B 52  ? 0.3803 0.3217 0.2496 0.1483  0.0551  0.0258  69  ILE B CB  
1555 C CG1 A ILE B 52  ? 0.3528 0.4777 0.2538 0.1951  0.0182  -0.0156 69  ILE B CG1 
1556 C CG1 B ILE B 52  ? 0.4134 0.3334 0.2614 0.1880  0.0692  0.0193  69  ILE B CG1 
1557 C CG2 A ILE B 52  ? 0.2859 0.3104 0.2390 0.0795  0.0194  0.0011  69  ILE B CG2 
1558 C CG2 B ILE B 52  ? 0.4062 0.4191 0.2547 0.1616  0.0623  0.0238  69  ILE B CG2 
1559 C CD1 A ILE B 52  ? 0.4109 0.4777 0.2578 0.2582  0.0033  -0.0296 69  ILE B CD1 
1560 C CD1 B ILE B 52  ? 0.4124 0.4049 0.2693 0.1338  0.0868  0.0148  69  ILE B CD1 
1561 N N   . LEU B 53  ? 0.2847 0.1872 0.2328 0.0754  0.0111  0.0081  70  LEU B N   
1562 C CA  . LEU B 53  ? 0.3145 0.2059 0.2182 0.0220  0.0051  0.0180  70  LEU B CA  
1563 C C   . LEU B 53  ? 0.3595 0.2810 0.2196 0.0601  -0.0020 0.0236  70  LEU B C   
1564 O O   . LEU B 53  ? 0.3594 0.2646 0.2141 0.0567  -0.0294 0.0545  70  LEU B O   
1565 C CB  . LEU B 53  ? 0.3232 0.2037 0.2108 0.0181  -0.0024 0.0244  70  LEU B CB  
1566 C CG  . LEU B 53  ? 0.2777 0.2296 0.2154 0.0434  0.0046  0.0077  70  LEU B CG  
1567 C CD1 . LEU B 53  ? 0.2837 0.2412 0.2060 0.0509  -0.0049 -0.0316 70  LEU B CD1 
1568 C CD2 . LEU B 53  ? 0.3150 0.2551 0.2305 0.1046  -0.0098 0.0357  70  LEU B CD2 
1569 N N   . GLU B 54  ? 0.3857 0.2935 0.2175 0.0776  -0.0168 -0.0069 71  GLU B N   
1570 C CA  A GLU B 54  ? 0.4548 0.3370 0.2210 0.1576  -0.0092 -0.0198 71  GLU B CA  
1571 C CA  B GLU B 54  ? 0.4445 0.3371 0.2190 0.1397  -0.0092 -0.0330 71  GLU B CA  
1572 C C   . GLU B 54  ? 0.4405 0.3720 0.2246 0.1709  -0.0115 -0.0218 71  GLU B C   
1573 O O   . GLU B 54  ? 0.4437 0.3791 0.2057 0.1028  -0.0318 -0.0325 71  GLU B O   
1574 C CB  A GLU B 54  ? 0.5618 0.4479 0.2271 0.2871  -0.0020 -0.0237 71  GLU B CB  
1575 C CB  B GLU B 54  ? 0.5381 0.4650 0.2251 0.2485  -0.0036 -0.0605 71  GLU B CB  
1576 C CG  A GLU B 54  ? 0.6459 0.5652 0.2434 0.3594  0.0027  0.0028  71  GLU B CG  
1577 C CG  B GLU B 54  ? 0.6241 0.6019 0.2587 0.3086  0.0000  -0.0575 71  GLU B CG  
1578 C CD  A GLU B 54  ? 0.6795 0.6873 0.2737 0.4040  0.0116  0.0111  71  GLU B CD  
1579 C CD  B GLU B 54  ? 0.6896 0.7589 0.2826 0.3506  0.0079  -0.0410 71  GLU B CD  
1580 O OE1 A GLU B 54  ? 0.7119 0.7222 0.2881 0.4252  0.0101  0.0129  71  GLU B OE1 
1581 O OE1 B GLU B 54  ? 0.7174 0.8412 0.2999 0.3815  0.0093  -0.0289 71  GLU B OE1 
1582 O OE2 A GLU B 54  ? 0.6986 0.7488 0.2962 0.4196  0.0218  0.0373  71  GLU B OE2 
1583 O OE2 B GLU B 54  ? 0.6994 0.7887 0.2871 0.3723  0.0124  -0.0202 71  GLU B OE2 
1584 N N   . GLU B 55  ? 0.4483 0.2712 0.2448 0.1261  -0.0199 -0.0188 72  GLU B N   
1585 C CA  . GLU B 55  ? 0.4281 0.3111 0.2647 0.1026  -0.0236 -0.0247 72  GLU B CA  
1586 C C   . GLU B 55  ? 0.4149 0.2845 0.2505 0.0438  -0.0567 -0.0176 72  GLU B C   
1587 O O   . GLU B 55  ? 0.4525 0.3598 0.2406 0.0673  -0.0932 -0.0121 72  GLU B O   
1588 C CB  . GLU B 55  ? 0.5334 0.3748 0.2986 0.0913  0.0322  0.0336  72  GLU B CB  
1589 C CG  . GLU B 55  ? 0.6754 0.6455 0.3343 0.0070  0.0517  0.0635  72  GLU B CG  
1590 C CD  . GLU B 55  ? 0.7983 0.8382 0.3617 -0.0991 0.0808  0.0960  72  GLU B CD  
1591 O OE1 . GLU B 55  ? 0.8510 0.8978 0.3783 -0.1304 0.1148  0.1234  72  GLU B OE1 
1592 O OE2 . GLU B 55  ? 0.8203 0.9379 0.3664 -0.1218 0.0864  0.1157  72  GLU B OE2 
1593 N N   . HIS B 56  ? 0.3627 0.2656 0.2486 0.0405  -0.0308 -0.0184 73  HIS B N   
1594 C CA  . HIS B 56  ? 0.3672 0.2702 0.2480 0.0479  -0.0359 -0.0088 73  HIS B CA  
1595 C C   . HIS B 56  ? 0.3605 0.3085 0.2479 0.0562  -0.0467 -0.0133 73  HIS B C   
1596 O O   . HIS B 56  ? 0.3886 0.3516 0.2592 0.0441  -0.0691 -0.0243 73  HIS B O   
1597 C CB  . HIS B 56  ? 0.3555 0.2016 0.2520 0.0460  -0.0086 -0.0018 73  HIS B CB  
1598 C CG  . HIS B 56  ? 0.4497 0.2070 0.2642 0.0941  0.0164  0.0002  73  HIS B CG  
1599 N ND1 . HIS B 56  ? 0.4152 0.2400 0.2673 0.0587  -0.0196 -0.0095 73  HIS B ND1 
1600 C CD2 . HIS B 56  ? 0.4263 0.2395 0.2792 0.0001  0.0271  -0.0074 73  HIS B CD2 
1601 C CE1 . HIS B 56  ? 0.4198 0.2802 0.2693 0.0465  -0.0090 -0.0045 73  HIS B CE1 
1602 N NE2 . HIS B 56  ? 0.4657 0.3075 0.2750 0.1003  -0.0037 -0.0030 73  HIS B NE2 
1603 N N   . TYR B 57  ? 0.3992 0.2815 0.2382 0.0485  -0.0258 -0.0020 74  TYR B N   
1604 C CA  . TYR B 57  ? 0.3971 0.2618 0.2284 0.0268  -0.0058 0.0149  74  TYR B CA  
1605 C C   . TYR B 57  ? 0.4166 0.3084 0.2317 0.0588  -0.0074 0.0027  74  TYR B C   
1606 O O   . TYR B 57  ? 0.4409 0.4300 0.2213 0.0858  0.0158  0.0217  74  TYR B O   
1607 C CB  . TYR B 57  ? 0.4201 0.3144 0.2188 0.0677  -0.0065 0.0304  74  TYR B CB  
1608 C CG  . TYR B 57  ? 0.4339 0.2870 0.2111 0.0418  -0.0187 0.0087  74  TYR B CG  
1609 C CD1 . TYR B 57  ? 0.5017 0.3428 0.2129 0.0733  -0.0005 -0.0021 74  TYR B CD1 
1610 C CD2 . TYR B 57  ? 0.4653 0.3615 0.2159 0.0692  -0.0445 0.0048  74  TYR B CD2 
1611 C CE1 . TYR B 57  ? 0.5228 0.3605 0.2194 0.0674  -0.0017 -0.0042 74  TYR B CE1 
1612 C CE2 . TYR B 57  ? 0.5027 0.3103 0.2242 0.0974  -0.0213 0.0097  74  TYR B CE2 
1613 C CZ  . TYR B 57  ? 0.4905 0.3724 0.2292 0.0892  -0.0229 -0.0310 74  TYR B CZ  
1614 O OH  . TYR B 57  ? 0.5745 0.3864 0.2437 0.1045  -0.0248 -0.0598 74  TYR B OH  
1615 N N   . ALA B 58  ? 0.4859 0.3185 0.2469 0.0233  -0.0301 -0.0229 75  ALA B N   
1616 C CA  . ALA B 58  ? 0.5862 0.3188 0.2566 0.0221  -0.0303 -0.0279 75  ALA B CA  
1617 C C   . ALA B 58  ? 0.6336 0.3619 0.2644 0.0421  -0.0347 -0.0360 75  ALA B C   
1618 O O   . ALA B 58  ? 0.6355 0.3792 0.2620 0.0071  -0.0164 -0.0625 75  ALA B O   
1619 C CB  . ALA B 58  ? 0.6077 0.3341 0.2621 -0.0007 -0.0331 -0.0167 75  ALA B CB  
1620 N N   . GLU B 59  ? 0.6210 0.4281 0.2695 0.0552  -0.0433 0.0022  76  GLU B N   
1621 C CA  . GLU B 59  ? 0.6660 0.4790 0.2796 0.0957  -0.0393 0.0253  76  GLU B CA  
1622 C C   . GLU B 59  ? 0.6688 0.4811 0.2738 0.1125  -0.0264 0.0225  76  GLU B C   
1623 O O   . GLU B 59  ? 0.6459 0.5184 0.2626 0.0882  -0.0066 0.0499  76  GLU B O   
1624 C CB  . GLU B 59  ? 0.7480 0.6376 0.3024 0.2093  -0.0393 0.0313  76  GLU B CB  
1625 C CG  . GLU B 59  ? 0.8135 0.7616 0.3234 0.3187  -0.0517 0.0431  76  GLU B CG  
1626 C CD  . GLU B 59  ? 0.8712 0.8117 0.3375 0.3395  -0.0467 0.0430  76  GLU B CD  
1627 O OE1 . GLU B 59  ? 0.8994 0.8729 0.3461 0.3555  -0.0393 0.0449  76  GLU B OE1 
1628 O OE2 . GLU B 59  ? 0.8619 0.7762 0.3396 0.3327  -0.0429 0.0512  76  GLU B OE2 
1629 N N   . HIS B 60  ? 0.6444 0.3884 0.2736 0.0659  -0.0231 -0.0003 77  HIS B N   
1630 C CA  . HIS B 60  ? 0.6806 0.3958 0.2845 0.0788  0.0044  -0.0027 77  HIS B CA  
1631 C C   . HIS B 60  ? 0.7005 0.3413 0.2823 0.0695  -0.0216 -0.0150 77  HIS B C   
1632 O O   . HIS B 60  ? 0.7127 0.3070 0.2718 0.0696  -0.0053 -0.0185 77  HIS B O   
1633 C CB  . HIS B 60  ? 0.6509 0.3908 0.3040 0.0908  0.0371  0.0269  77  HIS B CB  
1634 C CG  . HIS B 60  ? 0.6528 0.4239 0.3233 0.1483  0.0467  0.0556  77  HIS B CG  
1635 N ND1 . HIS B 60  ? 0.6318 0.4747 0.3327 0.1427  0.0443  0.0721  77  HIS B ND1 
1636 C CD2 . HIS B 60  ? 0.6491 0.4945 0.3345 0.1603  0.0519  0.0635  77  HIS B CD2 
1637 C CE1 . HIS B 60  ? 0.6351 0.4679 0.3398 0.1075  0.0424  0.0797  77  HIS B CE1 
1638 N NE2 . HIS B 60  ? 0.6111 0.5320 0.3405 0.1375  0.0489  0.0662  77  HIS B NE2 
1639 N N   . LYS B 61  ? 0.7230 0.3471 0.2930 0.0847  -0.0375 0.0010  78  LYS B N   
1640 C CA  . LYS B 61  ? 0.7910 0.3927 0.3080 0.0332  -0.0311 -0.0250 78  LYS B CA  
1641 C C   . LYS B 61  ? 0.7725 0.4174 0.2865 0.0503  -0.0296 -0.0679 78  LYS B C   
1642 O O   . LYS B 61  ? 0.7289 0.4391 0.2695 0.0195  -0.0757 -0.0652 78  LYS B O   
1643 C CB  . LYS B 61  ? 0.9001 0.4729 0.3442 0.0262  -0.0231 -0.0330 78  LYS B CB  
1644 C CG  . LYS B 61  ? 1.0032 0.5861 0.3775 0.0430  -0.0144 -0.0476 78  LYS B CG  
1645 C CD  . LYS B 61  ? 1.1157 0.7298 0.3995 0.0969  -0.0094 -0.0599 78  LYS B CD  
1646 C CE  . LYS B 61  ? 1.2025 0.8244 0.4118 0.1281  -0.0176 -0.0690 78  LYS B CE  
1647 N NZ  . LYS B 61  ? 1.2494 0.9015 0.4182 0.1471  -0.0245 -0.0618 78  LYS B NZ  
1648 N N   . GLY B 62  ? 0.7907 0.4505 0.2733 0.1371  0.0071  -0.0774 79  GLY B N   
1649 C CA  . GLY B 62  ? 0.7810 0.5225 0.2694 0.1188  0.0476  -0.0505 79  GLY B CA  
1650 C C   . GLY B 62  ? 0.7824 0.6146 0.2626 0.1547  0.0610  -0.0654 79  GLY B C   
1651 O O   . GLY B 62  ? 0.7977 0.6543 0.2718 0.2087  0.0697  -0.0658 79  GLY B O   
1652 N N   . LYS B 63  ? 0.6999 0.5650 0.2496 0.0727  0.0661  -0.0689 80  LYS B N   
1653 C CA  . LYS B 63  ? 0.6782 0.5237 0.2495 -0.0626 0.0723  -0.0709 80  LYS B CA  
1654 C C   . LYS B 63  ? 0.7081 0.6526 0.2412 -0.0626 0.1057  -0.0835 80  LYS B C   
1655 O O   . LYS B 63  ? 0.7206 0.6982 0.2388 -0.0068 0.0689  -0.1196 80  LYS B O   
1656 C CB  . LYS B 63  ? 0.6837 0.4637 0.2550 -0.0726 0.0724  -0.0374 80  LYS B CB  
1657 C CG  . LYS B 63  ? 0.7392 0.4783 0.2618 0.0456  0.0624  0.0122  80  LYS B CG  
1658 C CD  . LYS B 63  ? 0.7782 0.5072 0.2705 0.0983  0.0527  0.0182  80  LYS B CD  
1659 C CE  . LYS B 63  ? 0.8069 0.5469 0.2764 0.1454  0.0438  0.0477  80  LYS B CE  
1660 N NZ  . LYS B 63  ? 0.8512 0.5628 0.2818 0.1806  0.0212  0.0726  80  LYS B NZ  
1661 N N   . PRO B 64  ? 0.7212 0.7232 0.2535 -0.0887 0.1430  -0.0485 81  PRO B N   
1662 C CA  . PRO B 64  ? 0.6804 0.7187 0.2607 -0.1104 0.1511  -0.0416 81  PRO B CA  
1663 C C   . PRO B 64  ? 0.6420 0.7248 0.2543 -0.0197 0.1356  -0.0622 81  PRO B C   
1664 O O   . PRO B 64  ? 0.5992 0.7119 0.2641 -0.0368 0.1147  -0.0714 81  PRO B O   
1665 C CB  . PRO B 64  ? 0.7322 0.8366 0.2731 -0.1011 0.1475  -0.0154 81  PRO B CB  
1666 C CG  . PRO B 64  ? 0.7933 0.8704 0.2697 -0.0635 0.1474  -0.0107 81  PRO B CG  
1667 C CD  . PRO B 64  ? 0.7771 0.8183 0.2656 -0.0805 0.1453  -0.0305 81  PRO B CD  
1668 N N   . PHE B 65  ? 0.6273 0.6484 0.2555 0.0053  0.1249  -0.0711 82  PHE B N   
1669 C CA  . PHE B 65  ? 0.5760 0.6013 0.2617 0.0053  0.1257  -0.0510 82  PHE B CA  
1670 C C   . PHE B 65  ? 0.5695 0.4958 0.2604 -0.0167 0.1149  -0.0459 82  PHE B C   
1671 O O   . PHE B 65  ? 0.5719 0.4480 0.2468 -0.0290 0.0927  -0.0491 82  PHE B O   
1672 C CB  . PHE B 65  ? 0.5700 0.5434 0.2706 -0.0671 0.1213  -0.0408 82  PHE B CB  
1673 C CG  . PHE B 65  ? 0.5739 0.5429 0.2780 -0.0493 0.1100  -0.0412 82  PHE B CG  
1674 C CD1 . PHE B 65  ? 0.5299 0.5802 0.2776 -0.0382 0.1170  -0.0440 82  PHE B CD1 
1675 C CD2 . PHE B 65  ? 0.5825 0.5634 0.2844 -0.0064 0.1042  -0.0648 82  PHE B CD2 
1676 C CE1 . PHE B 65  ? 0.5322 0.5753 0.2821 0.0021  0.1083  -0.0443 82  PHE B CE1 
1677 C CE2 . PHE B 65  ? 0.5721 0.5789 0.2868 0.0639  0.0989  -0.0746 82  PHE B CE2 
1678 C CZ  . PHE B 65  ? 0.5011 0.5129 0.2824 -0.0122 0.1218  -0.0586 82  PHE B CZ  
1679 N N   . LEU B 66  ? 0.5464 0.4519 0.2640 0.0241  0.1128  -0.0543 83  LEU B N   
1680 C CA  . LEU B 66  ? 0.5541 0.4110 0.2561 0.0600  0.1016  -0.0414 83  LEU B CA  
1681 C C   . LEU B 66  ? 0.4978 0.4170 0.2575 0.0858  0.1060  -0.0506 83  LEU B C   
1682 O O   . LEU B 66  ? 0.4653 0.4060 0.2527 0.0483  0.0942  -0.0819 83  LEU B O   
1683 C CB  . LEU B 66  ? 0.5948 0.3937 0.2556 0.0529  0.0867  -0.0349 83  LEU B CB  
1684 C CG  . LEU B 66  ? 0.5465 0.4338 0.2578 -0.0038 0.0508  -0.0228 83  LEU B CG  
1685 C CD1 . LEU B 66  ? 0.5333 0.4481 0.2541 -0.0113 0.0481  -0.0339 83  LEU B CD1 
1686 C CD2 . LEU B 66  ? 0.5406 0.4555 0.2553 -0.0748 -0.0024 -0.0620 83  LEU B CD2 
1687 N N   . PRO B 67  ? 0.4630 0.4603 0.2593 0.0980  0.1163  -0.0658 84  PRO B N   
1688 C CA  . PRO B 67  ? 0.4607 0.4320 0.2653 0.0889  0.1235  -0.0524 84  PRO B CA  
1689 C C   . PRO B 67  ? 0.4474 0.4320 0.2612 0.0581  0.1166  -0.0476 84  PRO B C   
1690 O O   . PRO B 67  ? 0.4475 0.4362 0.2620 0.0592  0.0873  -0.0753 84  PRO B O   
1691 C CB  . PRO B 67  ? 0.5388 0.5040 0.2695 0.1714  0.1336  -0.0373 84  PRO B CB  
1692 C CG  . PRO B 67  ? 0.5603 0.5530 0.2667 0.1757  0.1231  -0.0487 84  PRO B CG  
1693 C CD  . PRO B 67  ? 0.5055 0.4972 0.2610 0.1298  0.1199  -0.0490 84  PRO B CD  
1694 N N   . GLY B 68  ? 0.4519 0.4658 0.2613 0.0620  0.1135  -0.0737 85  GLY B N   
1695 C CA  . GLY B 68  ? 0.4743 0.4419 0.2483 0.0693  0.1017  -0.0688 85  GLY B CA  
1696 C C   . GLY B 68  ? 0.4557 0.3626 0.2384 0.0063  0.0917  -0.0217 85  GLY B C   
1697 O O   . GLY B 68  ? 0.4816 0.3750 0.2321 0.0055  0.0640  -0.0359 85  GLY B O   
1698 N N   . LEU B 69  ? 0.4342 0.3466 0.2415 0.0138  0.0783  0.0066  86  LEU B N   
1699 C CA  . LEU B 69  ? 0.4307 0.3762 0.2329 0.0112  0.0640  0.0159  86  LEU B CA  
1700 C C   . LEU B 69  ? 0.4261 0.3793 0.2288 0.0523  0.0682  0.0188  86  LEU B C   
1701 O O   . LEU B 69  ? 0.4338 0.3580 0.2154 0.0373  0.0495  0.0319  86  LEU B O   
1702 C CB  . LEU B 69  ? 0.4134 0.5289 0.2420 0.0947  0.0413  0.0180  86  LEU B CB  
1703 C CG  . LEU B 69  ? 0.5572 0.6360 0.2545 0.1904  0.0262  0.0279  86  LEU B CG  
1704 C CD1 . LEU B 69  ? 0.6052 0.7272 0.2579 0.2938  0.0211  0.0434  86  LEU B CD1 
1705 C CD2 . LEU B 69  ? 0.5676 0.6642 0.2610 0.1728  0.0018  0.0226  86  LEU B CD2 
1706 N N   . ILE B 70  ? 0.4316 0.3452 0.2239 0.0912  0.0905  -0.0149 87  ILE B N   
1707 C CA  A ILE B 70  ? 0.4442 0.3274 0.2253 0.0724  0.0865  -0.0039 87  ILE B CA  
1708 C CA  B ILE B 70  ? 0.4126 0.3251 0.2237 0.0560  0.0926  -0.0041 87  ILE B CA  
1709 C C   . ILE B 70  ? 0.3844 0.2946 0.2206 0.0610  0.0873  -0.0110 87  ILE B C   
1710 O O   . ILE B 70  ? 0.3922 0.3036 0.2056 0.0642  0.0932  -0.0010 87  ILE B O   
1711 C CB  A ILE B 70  ? 0.5131 0.3490 0.2264 0.0355  0.0950  -0.0257 87  ILE B CB  
1712 C CB  B ILE B 70  ? 0.4206 0.3278 0.2234 -0.0010 0.1022  -0.0038 87  ILE B CB  
1713 C CG1 A ILE B 70  ? 0.5773 0.4149 0.2345 0.0243  0.1159  -0.0245 87  ILE B CG1 
1714 C CG1 B ILE B 70  ? 0.4117 0.3205 0.2247 -0.0656 0.1134  0.0051  87  ILE B CG1 
1715 C CG2 A ILE B 70  ? 0.5347 0.3241 0.2217 0.0857  0.0926  -0.0343 87  ILE B CG2 
1716 C CG2 B ILE B 70  ? 0.4411 0.3232 0.2224 0.0199  0.1035  -0.0060 87  ILE B CG2 
1717 C CD1 A ILE B 70  ? 0.6309 0.4593 0.2396 0.0571  0.1159  -0.0522 87  ILE B CD1 
1718 C CD1 B ILE B 70  ? 0.3812 0.3122 0.2262 -0.1319 0.1142  0.0127  87  ILE B CD1 
1719 N N   . GLU B 71  ? 0.3323 0.3747 0.2282 0.0823  0.0740  -0.0081 88  GLU B N   
1720 C CA  . GLU B 71  ? 0.3234 0.5013 0.2636 0.0468  0.0512  -0.0293 88  GLU B CA  
1721 C C   . GLU B 71  ? 0.3261 0.4424 0.2580 0.0485  0.0278  -0.0170 88  GLU B C   
1722 O O   . GLU B 71  ? 0.3056 0.4992 0.2542 0.0597  0.0147  -0.0431 88  GLU B O   
1723 C CB  . GLU B 71  ? 0.3466 0.6820 0.3053 0.0783  0.0821  -0.0246 88  GLU B CB  
1724 C CG  . GLU B 71  ? 0.4528 0.9311 0.3451 0.0496  0.0709  -0.0257 88  GLU B CG  
1725 C CD  . GLU B 71  ? 0.5152 1.0481 0.3713 -0.0742 0.0806  -0.0248 88  GLU B CD  
1726 O OE1 . GLU B 71  ? 0.5332 1.0520 0.3873 -0.1547 0.0609  -0.0441 88  GLU B OE1 
1727 O OE2 . GLU B 71  ? 0.5931 1.1222 0.3832 -0.0239 0.0909  -0.0138 88  GLU B OE2 
1728 N N   . LYS B 72  ? 0.3315 0.3075 0.2640 0.0427  0.0576  -0.0073 89  LYS B N   
1729 C CA  A LYS B 72  ? 0.3813 0.3034 0.2625 0.0430  0.0748  0.0054  89  LYS B CA  
1730 C CA  B LYS B 72  ? 0.3544 0.2959 0.2604 -0.0014 0.0733  0.0248  89  LYS B CA  
1731 C C   . LYS B 72  ? 0.3385 0.2972 0.2507 0.0045  0.0619  0.0239  89  LYS B C   
1732 O O   . LYS B 72  ? 0.3830 0.2687 0.2477 0.0340  0.0471  0.0235  89  LYS B O   
1733 C CB  A LYS B 72  ? 0.4516 0.3619 0.2743 0.1402  0.1097  0.0081  89  LYS B CB  
1734 C CB  B LYS B 72  ? 0.3870 0.3266 0.2673 -0.0104 0.1013  0.0599  89  LYS B CB  
1735 C CG  A LYS B 72  ? 0.4596 0.4029 0.2894 0.1052  0.1295  0.0276  89  LYS B CG  
1736 C CG  B LYS B 72  ? 0.3760 0.3352 0.2760 -0.0614 0.1215  0.0906  89  LYS B CG  
1737 C CD  A LYS B 72  ? 0.4721 0.4569 0.3017 0.1941  0.1501  0.0383  89  LYS B CD  
1738 C CD  B LYS B 72  ? 0.4385 0.4222 0.2834 -0.0136 0.1335  0.1087  89  LYS B CD  
1739 C CE  A LYS B 72  ? 0.5332 0.5234 0.3123 0.2138  0.1455  0.0502  89  LYS B CE  
1740 C CE  B LYS B 72  ? 0.4920 0.4086 0.2887 -0.0037 0.1379  0.1237  89  LYS B CE  
1741 N NZ  A LYS B 72  ? 0.5884 0.5719 0.3240 0.2355  0.1518  0.0501  89  LYS B NZ  
1742 N NZ  B LYS B 72  ? 0.5387 0.4414 0.2929 0.0002  0.1249  0.1187  89  LYS B NZ  
1743 N N   . MET B 73  ? 0.3292 0.2675 0.2302 0.0226  0.0406  -0.0036 90  MET B N   
1744 C CA  . MET B 73  ? 0.3185 0.2067 0.2191 0.0548  -0.0105 -0.0037 90  MET B CA  
1745 C C   . MET B 73  ? 0.3203 0.1959 0.2053 0.0947  -0.0178 0.0149  90  MET B C   
1746 O O   . MET B 73  ? 0.3077 0.2629 0.1970 0.0347  -0.0043 -0.0195 90  MET B O   
1747 C CB  . MET B 73  ? 0.3401 0.2176 0.2399 0.0939  -0.0204 -0.0131 90  MET B CB  
1748 C CG  . MET B 73  ? 0.3906 0.3195 0.2466 0.1267  -0.0108 -0.0098 90  MET B CG  
1749 S SD  . MET B 73  ? 0.3538 0.2687 0.2481 0.0710  -0.0286 -0.0005 90  MET B SD  
1750 C CE  . MET B 73  ? 0.3182 0.2601 0.2759 -0.0068 -0.0154 -0.0168 90  MET B CE  
1751 N N   . THR B 74  ? 0.2652 0.2406 0.1975 0.1300  0.0019  0.0100  91  THR B N   
1752 C CA  . THR B 74  ? 0.2743 0.2561 0.1952 0.0795  0.0118  -0.0066 91  THR B CA  
1753 C C   . THR B 74  ? 0.2531 0.2927 0.2184 0.0614  0.0069  -0.0461 91  THR B C   
1754 O O   . THR B 74  ? 0.2915 0.3596 0.2472 0.0397  0.0036  -0.0466 91  THR B O   
1755 C CB  . THR B 74  ? 0.3066 0.3103 0.1979 0.1314  0.0120  -0.0031 91  THR B CB  
1756 O OG1 . THR B 74  ? 0.3470 0.3600 0.2132 0.1022  0.0313  -0.0395 91  THR B OG1 
1757 C CG2 . THR B 74  ? 0.3016 0.3624 0.2015 0.1426  0.0330  0.0050  91  THR B CG2 
1758 N N   . GLY B 75  ? 0.2264 0.2767 0.1930 0.0637  0.0211  -0.0176 92  GLY B N   
1759 C CA  . GLY B 75  ? 0.2207 0.3047 0.1791 0.0801  0.0063  -0.0028 92  GLY B CA  
1760 C C   . GLY B 75  ? 0.1996 0.2285 0.1765 0.0926  -0.0185 0.0023  92  GLY B C   
1761 O O   . GLY B 75  ? 0.2022 0.2738 0.1791 0.0770  -0.0057 -0.0088 92  GLY B O   
1762 N N   . PRO B 76  ? 0.2285 0.2382 0.1743 0.0783  -0.0144 -0.0120 93  PRO B N   
1763 C CA  . PRO B 76  ? 0.1861 0.2469 0.1649 0.0515  -0.0077 0.0217  93  PRO B CA  
1764 C C   . PRO B 76  ? 0.2379 0.2317 0.1641 0.0773  -0.0013 0.0100  93  PRO B C   
1765 O O   . PRO B 76  ? 0.2651 0.2234 0.1727 0.0553  -0.0002 0.0167  93  PRO B O   
1766 C CB  . PRO B 76  ? 0.2155 0.2892 0.1691 0.0312  0.0165  0.0181  93  PRO B CB  
1767 C CG  . PRO B 76  ? 0.2164 0.2796 0.1709 0.0905  -0.0063 -0.0119 93  PRO B CG  
1768 C CD  . PRO B 76  ? 0.2659 0.2971 0.1755 0.1073  0.0041  -0.0093 93  PRO B CD  
1769 N N   . VAL B 77  ? 0.2441 0.2470 0.1684 0.0708  -0.0020 0.0041  94  VAL B N   
1770 C CA  . VAL B 77  ? 0.2360 0.2506 0.1654 0.0909  0.0208  0.0238  94  VAL B CA  
1771 C C   . VAL B 77  ? 0.2140 0.2292 0.1622 0.0246  0.0217  0.0089  94  VAL B C   
1772 O O   . VAL B 77  ? 0.2449 0.2225 0.1650 0.0694  0.0367  0.0128  94  VAL B O   
1773 C CB  . VAL B 77  ? 0.2587 0.2015 0.1742 0.0891  0.0025  0.0038  94  VAL B CB  
1774 C CG1 . VAL B 77  ? 0.2098 0.2868 0.1652 0.0765  0.0141  -0.0139 94  VAL B CG1 
1775 C CG2 . VAL B 77  ? 0.2191 0.2170 0.1817 0.0813  0.0257  -0.0057 94  VAL B CG2 
1776 N N   . LEU B 78  ? 0.2011 0.2396 0.1634 0.0868  0.0245  0.0345  95  LEU B N   
1777 C CA  . LEU B 78  ? 0.1944 0.2252 0.1690 0.0818  0.0065  0.0012  95  LEU B CA  
1778 C C   . LEU B 78  ? 0.2320 0.2305 0.1649 0.1031  -0.0005 0.0159  95  LEU B C   
1779 O O   . LEU B 78  ? 0.2401 0.1950 0.1581 0.0488  0.0042  0.0452  95  LEU B O   
1780 C CB  . LEU B 78  ? 0.2048 0.2233 0.1687 0.0929  0.0224  -0.0075 95  LEU B CB  
1781 C CG  . LEU B 78  ? 0.2276 0.2316 0.1616 0.0673  0.0487  0.0153  95  LEU B CG  
1782 C CD1 . LEU B 78  ? 0.3124 0.2922 0.1712 0.1083  0.0066  0.0107  95  LEU B CD1 
1783 C CD2 . LEU B 78  ? 0.2384 0.2311 0.1610 0.0935  0.0533  0.0140  95  LEU B CD2 
1784 N N   . CYS B 79  ? 0.2514 0.2216 0.1757 0.0785  -0.0033 0.0011  96  CYS B N   
1785 C CA  . CYS B 79  ? 0.2447 0.2120 0.1760 0.0941  0.0070  0.0062  96  CYS B CA  
1786 C C   . CYS B 79  ? 0.1982 0.2099 0.1659 0.0701  -0.0001 -0.0193 96  CYS B C   
1787 O O   . CYS B 79  ? 0.2500 0.2477 0.1596 0.0544  0.0051  -0.0189 96  CYS B O   
1788 C CB  . CYS B 79  ? 0.2426 0.2587 0.1961 0.1195  -0.0039 0.0069  96  CYS B CB  
1789 S SG  . CYS B 79  ? 0.2814 0.2354 0.2192 0.0875  -0.0054 -0.0086 96  CYS B SG  
1790 N N   . MET B 80  ? 0.2127 0.2597 0.1700 0.0395  -0.0088 0.0165  97  MET B N   
1791 C CA  . MET B 80  ? 0.2098 0.2286 0.1756 0.0471  -0.0007 0.0168  97  MET B CA  
1792 C C   . MET B 80  ? 0.2024 0.2529 0.1751 0.0707  0.0065  -0.0147 97  MET B C   
1793 O O   . MET B 80  ? 0.2189 0.2552 0.1772 0.0465  0.0131  -0.0231 97  MET B O   
1794 C CB  . MET B 80  ? 0.2327 0.2427 0.1765 0.0320  -0.0039 0.0217  97  MET B CB  
1795 C CG  . MET B 80  ? 0.2606 0.2342 0.1845 0.0438  -0.0029 -0.0032 97  MET B CG  
1796 S SD  . MET B 80  ? 0.2528 0.2454 0.1803 0.0625  -0.0116 -0.0109 97  MET B SD  
1797 C CE  . MET B 80  ? 0.2785 0.3123 0.1776 0.0603  -0.0116 0.0435  97  MET B CE  
1798 N N   . VAL B 81  ? 0.1982 0.2207 0.1770 0.0563  0.0194  0.0196  98  VAL B N   
1799 C CA  . VAL B 81  ? 0.2345 0.2148 0.1827 0.0605  -0.0121 -0.0027 98  VAL B CA  
1800 C C   . VAL B 81  ? 0.2154 0.2090 0.1758 0.0878  -0.0092 -0.0150 98  VAL B C   
1801 O O   . VAL B 81  ? 0.2334 0.2283 0.1642 0.0659  0.0065  -0.0171 98  VAL B O   
1802 C CB  . VAL B 81  ? 0.3036 0.2208 0.1907 0.0408  -0.0226 0.0003  98  VAL B CB  
1803 C CG1 . VAL B 81  ? 0.2523 0.2187 0.1923 0.0087  -0.0399 -0.0071 98  VAL B CG1 
1804 C CG2 . VAL B 81  ? 0.2435 0.2752 0.1963 0.0288  -0.0293 -0.0128 98  VAL B CG2 
1805 N N   . PHE B 82  ? 0.2291 0.2437 0.1779 0.0916  -0.0230 0.0102  99  PHE B N   
1806 C CA  . PHE B 82  ? 0.1981 0.2118 0.1727 0.0090  -0.0055 0.0104  99  PHE B CA  
1807 C C   . PHE B 82  ? 0.2104 0.2160 0.1627 0.0292  -0.0168 -0.0256 99  PHE B C   
1808 O O   . PHE B 82  ? 0.2557 0.2174 0.1624 0.0371  -0.0094 -0.0297 99  PHE B O   
1809 C CB  . PHE B 82  ? 0.2273 0.2519 0.1681 0.0702  -0.0302 -0.0030 99  PHE B CB  
1810 C CG  . PHE B 82  ? 0.2042 0.2441 0.1609 0.0379  -0.0230 0.0110  99  PHE B CG  
1811 C CD1 . PHE B 82  ? 0.2248 0.2548 0.1742 0.0431  -0.0220 0.0240  99  PHE B CD1 
1812 C CD2 . PHE B 82  ? 0.2016 0.3303 0.1659 0.0353  -0.0402 -0.0129 99  PHE B CD2 
1813 C CE1 . PHE B 82  ? 0.2234 0.2808 0.1834 0.0516  -0.0204 0.0042  99  PHE B CE1 
1814 C CE2 . PHE B 82  ? 0.1759 0.2846 0.1672 0.0272  -0.0176 0.0056  99  PHE B CE2 
1815 C CZ  . PHE B 82  ? 0.2622 0.2527 0.1819 -0.0050 -0.0103 0.0077  99  PHE B CZ  
1816 N N   . GLU B 83  ? 0.1986 0.2634 0.1620 0.0252  -0.0100 -0.0068 100 GLU B N   
1817 C CA  . GLU B 83  ? 0.2459 0.1888 0.1719 0.0282  -0.0342 0.0032  100 GLU B CA  
1818 C C   . GLU B 83  ? 0.1875 0.1726 0.1673 -0.0048 -0.0365 -0.0194 100 GLU B C   
1819 O O   . GLU B 83  ? 0.2335 0.1843 0.1704 0.0318  -0.0267 -0.0379 100 GLU B O   
1820 C CB  . GLU B 83  ? 0.2477 0.1885 0.1867 0.0008  -0.0380 0.0080  100 GLU B CB  
1821 C CG  . GLU B 83  ? 0.3317 0.2259 0.2120 -0.0012 -0.0386 -0.0002 100 GLU B CG  
1822 C CD  . GLU B 83  ? 0.2987 0.1880 0.2169 0.0033  -0.0076 0.0132  100 GLU B CD  
1823 O OE1 . GLU B 83  ? 0.3073 0.1882 0.2246 -0.0221 -0.0094 0.0141  100 GLU B OE1 
1824 O OE2 . GLU B 83  ? 0.2687 0.2830 0.2254 0.0064  0.0099  -0.0144 100 GLU B OE2 
1825 N N   . GLY B 84  ? 0.2397 0.2303 0.1633 0.0404  -0.0308 -0.0037 101 GLY B N   
1826 C CA  . GLY B 84  ? 0.2610 0.2362 0.1633 0.0408  -0.0365 -0.0034 101 GLY B CA  
1827 C C   . GLY B 84  ? 0.2206 0.2284 0.1604 0.0047  -0.0147 0.0014  101 GLY B C   
1828 O O   . GLY B 84  ? 0.2319 0.2395 0.1694 0.0136  -0.0281 -0.0423 101 GLY B O   
1829 N N   . VAL B 85  ? 0.2144 0.2602 0.1554 0.0422  -0.0260 -0.0180 102 VAL B N   
1830 C CA  . VAL B 85  ? 0.2152 0.2429 0.1604 -0.0111 -0.0461 -0.0222 102 VAL B CA  
1831 C C   . VAL B 85  ? 0.1952 0.2649 0.1704 0.0542  -0.0076 -0.0098 102 VAL B C   
1832 O O   . VAL B 85  ? 0.2087 0.2535 0.1760 0.0049  -0.0049 -0.0026 102 VAL B O   
1833 C CB  . VAL B 85  ? 0.2478 0.2437 0.1535 0.0438  -0.0242 0.0097  102 VAL B CB  
1834 C CG1 . VAL B 85  ? 0.2749 0.2664 0.1528 0.0625  -0.0156 0.0336  102 VAL B CG1 
1835 C CG2 . VAL B 85  ? 0.2584 0.3043 0.1639 0.0941  -0.0275 -0.0229 102 VAL B CG2 
1836 N N   . ASP B 86  ? 0.2075 0.1899 0.1750 0.0444  -0.0052 -0.0191 103 ASP B N   
1837 C CA  . ASP B 86  ? 0.1876 0.2275 0.1847 0.0652  -0.0071 -0.0169 103 ASP B CA  
1838 C C   . ASP B 86  ? 0.2241 0.1837 0.1721 0.0182  -0.0265 0.0089  103 ASP B C   
1839 O O   . ASP B 86  ? 0.2574 0.2323 0.1740 0.0155  -0.0054 -0.0077 103 ASP B O   
1840 C CB  . ASP B 86  ? 0.2491 0.2250 0.1920 0.0744  -0.0275 -0.0130 103 ASP B CB  
1841 C CG  . ASP B 86  ? 0.2833 0.2143 0.2058 0.0473  -0.0344 -0.0201 103 ASP B CG  
1842 O OD1 . ASP B 86  ? 0.2660 0.2452 0.2148 0.0671  -0.0329 -0.0197 103 ASP B OD1 
1843 O OD2 . ASP B 86  ? 0.3019 0.2372 0.2030 0.0121  -0.0340 -0.0107 103 ASP B OD2 
1844 N N   . VAL B 87  ? 0.2076 0.2052 0.1678 -0.0019 -0.0155 0.0094  104 VAL B N   
1845 C CA  . VAL B 87  ? 0.2178 0.2316 0.1672 0.0191  -0.0034 -0.0088 104 VAL B CA  
1846 C C   . VAL B 87  ? 0.2650 0.2332 0.1710 0.0619  0.0003  -0.0103 104 VAL B C   
1847 O O   . VAL B 87  ? 0.2097 0.2413 0.1715 0.0394  0.0000  -0.0004 104 VAL B O   
1848 C CB  . VAL B 87  ? 0.2025 0.1956 0.1656 0.0047  -0.0186 0.0070  104 VAL B CB  
1849 C CG1 . VAL B 87  ? 0.2999 0.2221 0.1660 0.0144  -0.0160 0.0178  104 VAL B CG1 
1850 C CG2 . VAL B 87  ? 0.2115 0.2313 0.1626 0.0111  -0.0348 0.0150  104 VAL B CG2 
1851 N N   . ILE B 88  ? 0.2127 0.2297 0.1656 0.0621  0.0053  -0.0092 105 ILE B N   
1852 C CA  . ILE B 88  ? 0.2231 0.1933 0.1632 0.0332  -0.0289 -0.0265 105 ILE B CA  
1853 C C   . ILE B 88  ? 0.1768 0.2330 0.1582 -0.0179 -0.0388 -0.0168 105 ILE B C   
1854 O O   . ILE B 88  ? 0.1989 0.2365 0.1683 0.0218  -0.0051 -0.0130 105 ILE B O   
1855 C CB  . ILE B 88  ? 0.2419 0.2271 0.1634 0.0577  -0.0375 -0.0182 105 ILE B CB  
1856 C CG1 . ILE B 88  ? 0.3419 0.2331 0.1756 0.0542  0.0005  -0.0232 105 ILE B CG1 
1857 C CG2 . ILE B 88  ? 0.2962 0.2246 0.1551 0.0914  -0.0451 -0.0311 105 ILE B CG2 
1858 C CD1 . ILE B 88  ? 0.3961 0.2348 0.1911 0.0011  0.0127  -0.0102 105 ILE B CD1 
1859 N N   . ALA B 89  ? 0.1986 0.2238 0.1556 0.0340  -0.0227 -0.0266 106 ALA B N   
1860 C CA  . ALA B 89  ? 0.2936 0.2690 0.1539 0.0202  0.0030  -0.0063 106 ALA B CA  
1861 C C   . ALA B 89  ? 0.2113 0.2283 0.1572 0.0480  0.0145  -0.0027 106 ALA B C   
1862 O O   . ALA B 89  ? 0.1959 0.2299 0.1764 0.0124  -0.0113 -0.0157 106 ALA B O   
1863 C CB  . ALA B 89  ? 0.2844 0.3001 0.1530 0.0426  -0.0179 0.0227  106 ALA B CB  
1864 N N   . GLN B 90  ? 0.2187 0.1942 0.1640 0.0339  0.0058  0.0300  107 GLN B N   
1865 C CA  . GLN B 90  ? 0.2011 0.1899 0.1654 0.0356  -0.0060 0.0217  107 GLN B CA  
1866 C C   . GLN B 90  ? 0.2561 0.1754 0.1764 0.1084  -0.0344 -0.0073 107 GLN B C   
1867 O O   . GLN B 90  ? 0.2250 0.2147 0.1698 0.0333  -0.0158 0.0073  107 GLN B O   
1868 C CB  . GLN B 90  ? 0.1964 0.2218 0.1702 0.0023  0.0030  0.0171  107 GLN B CB  
1869 C CG  . GLN B 90  ? 0.2172 0.2516 0.1682 0.0229  0.0053  0.0230  107 GLN B CG  
1870 C CD  . GLN B 90  ? 0.1839 0.2424 0.1593 -0.0332 -0.0289 0.0082  107 GLN B CD  
1871 O OE1 . GLN B 90  ? 0.1937 0.2250 0.1641 0.0039  -0.0142 0.0088  107 GLN B OE1 
1872 N NE2 . GLN B 90  ? 0.3127 0.2350 0.1487 0.0830  -0.0403 0.0095  107 GLN B NE2 
1873 N N   . ALA B 91  ? 0.1866 0.2211 0.1873 0.0518  -0.0458 -0.0250 108 ALA B N   
1874 C CA  . ALA B 91  ? 0.2170 0.2321 0.1957 0.0251  -0.0443 -0.0013 108 ALA B CA  
1875 C C   . ALA B 91  ? 0.1550 0.2434 0.2024 0.0169  -0.0239 -0.0104 108 ALA B C   
1876 O O   . ALA B 91  ? 0.2034 0.2419 0.2164 0.0508  -0.0117 -0.0055 108 ALA B O   
1877 C CB  . ALA B 91  ? 0.2251 0.1898 0.2027 -0.0010 -0.0293 0.0115  108 ALA B CB  
1878 N N   . ARG B 92  ? 0.2149 0.2518 0.1965 0.0224  -0.0041 -0.0010 109 ARG B N   
1879 C CA  . ARG B 92  ? 0.2248 0.2662 0.1995 0.0263  0.0151  -0.0116 109 ARG B CA  
1880 C C   . ARG B 92  ? 0.2369 0.2913 0.1814 0.0617  0.0100  -0.0184 109 ARG B C   
1881 O O   . ARG B 92  ? 0.2462 0.2823 0.1851 0.0492  -0.0224 -0.0187 109 ARG B O   
1882 C CB  . ARG B 92  ? 0.2701 0.2777 0.2180 -0.0336 0.0172  -0.0421 109 ARG B CB  
1883 C CG  . ARG B 92  ? 0.3692 0.3225 0.2402 -0.0026 0.0449  -0.0284 109 ARG B CG  
1884 C CD  . ARG B 92  ? 0.5604 0.4034 0.2623 0.1278  0.0717  -0.0026 109 ARG B CD  
1885 N NE  . ARG B 92  ? 0.6116 0.4017 0.2740 0.1747  0.0965  0.0025  109 ARG B NE  
1886 C CZ  . ARG B 92  ? 0.6416 0.4792 0.2761 0.2192  0.0979  0.0254  109 ARG B CZ  
1887 N NH1 . ARG B 92  ? 0.5601 0.4582 0.2718 0.0709  0.0987  0.0540  109 ARG B NH1 
1888 N NH2 . ARG B 92  ? 0.6735 0.5440 0.2861 0.2241  0.0958  0.0488  109 ARG B NH2 
1889 N N   . LYS B 93  ? 0.2082 0.2700 0.1575 0.0164  -0.0046 -0.0221 110 LYS B N   
1890 C CA  . LYS B 93  ? 0.2182 0.2082 0.1625 0.0434  -0.0275 -0.0127 110 LYS B CA  
1891 C C   . LYS B 93  ? 0.2427 0.2020 0.1707 0.0327  -0.0170 -0.0064 110 LYS B C   
1892 O O   . LYS B 93  ? 0.2520 0.2128 0.1728 -0.0072 -0.0185 0.0032  110 LYS B O   
1893 C CB  . LYS B 93  ? 0.2164 0.2512 0.1622 0.0359  -0.0365 -0.0193 110 LYS B CB  
1894 C CG  . LYS B 93  ? 0.2376 0.2615 0.1674 0.0933  -0.0466 -0.0307 110 LYS B CG  
1895 C CD  . LYS B 93  ? 0.2171 0.2649 0.1752 0.0504  -0.0259 0.0066  110 LYS B CD  
1896 C CE  . LYS B 93  ? 0.2074 0.2740 0.2072 0.0530  -0.0326 0.0303  110 LYS B CE  
1897 N NZ  . LYS B 93  ? 0.2128 0.3031 0.2255 0.0689  -0.0386 0.0210  110 LYS B NZ  
1898 N N   . MET B 94  ? 0.2114 0.2125 0.1653 0.0486  -0.0006 -0.0103 111 MET B N   
1899 C CA  . MET B 94  ? 0.1955 0.1844 0.1602 0.0372  0.0001  0.0062  111 MET B CA  
1900 C C   . MET B 94  ? 0.1600 0.2310 0.1633 0.0006  0.0012  0.0104  111 MET B C   
1901 O O   . MET B 94  ? 0.1959 0.2332 0.1676 0.0113  -0.0148 0.0207  111 MET B O   
1902 C CB  . MET B 94  ? 0.1820 0.2292 0.1592 0.0265  -0.0115 -0.0067 111 MET B CB  
1903 C CG  . MET B 94  ? 0.1968 0.2167 0.1599 0.0226  0.0105  0.0053  111 MET B CG  
1904 S SD  . MET B 94  ? 0.2043 0.2500 0.1638 0.0331  0.0141  0.0009  111 MET B SD  
1905 C CE  . MET B 94  ? 0.2418 0.2755 0.1569 0.0281  0.0352  -0.0015 111 MET B CE  
1906 N N   . MET B 95  ? 0.2183 0.2029 0.1694 0.0255  -0.0103 0.0105  112 MET B N   
1907 C CA  A MET B 95  ? 0.2084 0.2338 0.1872 0.0437  0.0050  0.0148  112 MET B CA  
1908 C CA  B MET B 95  ? 0.2223 0.2377 0.1837 0.0286  -0.0178 0.0077  112 MET B CA  
1909 C C   . MET B 95  ? 0.2380 0.2032 0.1763 0.0188  -0.0130 -0.0033 112 MET B C   
1910 O O   . MET B 95  ? 0.2219 0.2380 0.1746 0.0286  -0.0162 -0.0263 112 MET B O   
1911 C CB  A MET B 95  ? 0.2548 0.2076 0.2165 0.0564  0.0262  0.0219  112 MET B CB  
1912 C CB  B MET B 95  ? 0.2407 0.2506 0.2047 0.0067  -0.0367 0.0054  112 MET B CB  
1913 C CG  A MET B 95  ? 0.2944 0.2292 0.2516 0.0598  0.0404  0.0365  112 MET B CG  
1914 C CG  B MET B 95  ? 0.2356 0.3032 0.2315 -0.0184 -0.0579 0.0021  112 MET B CG  
1915 S SD  A MET B 95  ? 0.4267 0.2340 0.2886 0.0958  0.0389  0.0327  112 MET B SD  
1916 S SD  B MET B 95  ? 0.2732 0.3419 0.2581 -0.0411 -0.0905 -0.0138 112 MET B SD  
1917 C CE  A MET B 95  ? 0.5591 0.3636 0.3035 0.1660  0.0422  0.0295  112 MET B CE  
1918 C CE  B MET B 95  ? 0.4156 0.4365 0.2652 0.1038  -0.0797 -0.0027 112 MET B CE  
1919 N N   . GLY B 96  ? 0.2028 0.2440 0.1568 0.0546  0.0005  0.0057  113 GLY B N   
1920 C CA  . GLY B 96  ? 0.2190 0.2167 0.1530 0.0366  0.0076  0.0141  113 GLY B CA  
1921 C C   . GLY B 96  ? 0.2093 0.2525 0.1552 0.0390  -0.0085 0.0132  113 GLY B C   
1922 O O   . GLY B 96  ? 0.2520 0.2372 0.1619 0.0361  0.0039  0.0127  113 GLY B O   
1923 N N   . SER B 97  ? 0.2406 0.2517 0.1501 0.0188  0.0117  -0.0043 114 SER B N   
1924 C CA  A SER B 97  ? 0.2549 0.2645 0.1626 0.0597  0.0227  0.0067  114 SER B CA  
1925 C CA  B SER B 97  ? 0.2566 0.2378 0.1631 0.0377  0.0245  0.0015  114 SER B CA  
1926 C C   . SER B 97  ? 0.2636 0.2574 0.1694 0.0465  0.0210  0.0081  114 SER B C   
1927 O O   . SER B 97  ? 0.2509 0.2360 0.1658 0.0265  0.0135  -0.0051 114 SER B O   
1928 C CB  A SER B 97  ? 0.2297 0.3020 0.1659 0.1052  0.0405  0.0310  114 SER B CB  
1929 C CB  B SER B 97  ? 0.2397 0.2465 0.1668 0.0431  0.0491  0.0195  114 SER B CB  
1930 O OG  A SER B 97  ? 0.2724 0.3837 0.1763 0.1194  0.0303  0.0478  114 SER B OG  
1931 O OG  B SER B 97  ? 0.3133 0.3508 0.1788 0.0619  0.0496  0.0260  114 SER B OG  
1932 N N   . THR B 98  ? 0.2501 0.2802 0.1922 0.0298  0.0134  0.0017  115 THR B N   
1933 C CA  . THR B 98  ? 0.2765 0.2549 0.2279 0.0485  -0.0362 -0.0120 115 THR B CA  
1934 C C   . THR B 98  ? 0.2113 0.2963 0.1981 0.0278  -0.0429 -0.0140 115 THR B C   
1935 O O   . THR B 98  ? 0.2693 0.2576 0.1784 0.0432  -0.0119 -0.0199 115 THR B O   
1936 C CB  . THR B 98  ? 0.4051 0.2817 0.3071 0.1164  -0.1280 -0.0776 115 THR B CB  
1937 O OG1 . THR B 98  ? 0.5910 0.5615 0.3468 0.2071  -0.1339 -0.0775 115 THR B OG1 
1938 C CG2 . THR B 98  ? 0.4188 0.2623 0.3237 0.1255  -0.1663 -0.0947 115 THR B CG2 
1939 N N   . ARG B 99  ? 0.2219 0.2321 0.1865 0.0524  0.0125  -0.0229 116 ARG B N   
1940 C CA  . ARG B 99  ? 0.2020 0.2811 0.1791 0.0472  0.0245  0.0122  116 ARG B CA  
1941 C C   . ARG B 99  ? 0.2391 0.2739 0.1755 0.0649  0.0245  0.0272  116 ARG B C   
1942 O O   . ARG B 99  ? 0.2286 0.2544 0.1805 0.0230  0.0170  0.0384  116 ARG B O   
1943 C CB  . ARG B 99  ? 0.2616 0.3901 0.1876 0.0883  0.0316  0.0115  116 ARG B CB  
1944 C CG  . ARG B 99  ? 0.4076 0.4919 0.2072 0.2100  0.0571  -0.0100 116 ARG B CG  
1945 C CD  . ARG B 99  ? 0.5287 0.6454 0.2432 0.2244  0.0736  -0.0237 116 ARG B CD  
1946 N NE  . ARG B 99  ? 0.6528 0.7985 0.2634 0.2141  0.0616  -0.0496 116 ARG B NE  
1947 C CZ  . ARG B 99  ? 0.6956 0.8549 0.2721 0.0624  0.0493  -0.0663 116 ARG B CZ  
1948 N NH1 . ARG B 99  ? 0.6856 0.7041 0.2690 -0.1467 0.0748  -0.0262 116 ARG B NH1 
1949 N NH2 . ARG B 99  ? 0.6926 0.9434 0.2916 0.0473  0.0189  -0.0798 116 ARG B NH2 
1950 N N   . PRO B 100 ? 0.2586 0.2783 0.1722 0.0874  0.0180  0.0129  117 PRO B N   
1951 C CA  . PRO B 100 ? 0.1846 0.2746 0.1713 0.0018  0.0305  0.0041  117 PRO B CA  
1952 C C   . PRO B 100 ? 0.1753 0.2795 0.1857 0.0296  0.0261  0.0120  117 PRO B C   
1953 O O   . PRO B 100 ? 0.2164 0.2505 0.2061 0.0506  0.0138  0.0095  117 PRO B O   
1954 C CB  . PRO B 100 ? 0.1815 0.3062 0.1540 0.0085  0.0185  -0.0273 117 PRO B CB  
1955 C CG  . PRO B 100 ? 0.2178 0.2970 0.1532 0.0337  0.0052  -0.0242 117 PRO B CG  
1956 C CD  . PRO B 100 ? 0.2394 0.2638 0.1613 0.0495  -0.0040 -0.0125 117 PRO B CD  
1957 N N   . GLY B 101 ? 0.2098 0.2986 0.1872 0.0237  0.0049  0.0037  118 GLY B N   
1958 C CA  . GLY B 101 ? 0.2266 0.3082 0.1813 0.0457  0.0022  0.0220  118 GLY B CA  
1959 C C   . GLY B 101 ? 0.2686 0.2773 0.1835 0.0394  0.0128  0.0299  118 GLY B C   
1960 O O   . GLY B 101 ? 0.3034 0.3011 0.1938 -0.0091 -0.0038 0.0271  118 GLY B O   
1961 N N   . GLU B 102 ? 0.2515 0.2594 0.1815 0.0146  -0.0080 -0.0125 119 GLU B N   
1962 C CA  . GLU B 102 ? 0.2211 0.2632 0.1730 0.0363  0.0025  0.0256  119 GLU B CA  
1963 C C   . GLU B 102 ? 0.2325 0.3065 0.1623 0.0710  0.0068  0.0136  119 GLU B C   
1964 O O   . GLU B 102 ? 0.2915 0.3434 0.1674 0.0758  0.0093  0.0338  119 GLU B O   
1965 C CB  . GLU B 102 ? 0.3143 0.3049 0.1935 0.0903  0.0516  0.0032  119 GLU B CB  
1966 C CG  . GLU B 102 ? 0.5119 0.4275 0.2339 0.0931  0.0752  -0.0281 119 GLU B CG  
1967 C CD  . GLU B 102 ? 0.8047 0.5992 0.2886 0.2448  0.1072  -0.0279 119 GLU B CD  
1968 O OE1 . GLU B 102 ? 0.8962 0.6252 0.3201 0.2964  0.0756  -0.0528 119 GLU B OE1 
1969 O OE2 . GLU B 102 ? 0.9036 0.6741 0.3112 0.2687  0.1294  0.0053  119 GLU B OE2 
1970 N N   . ALA B 103 ? 0.2703 0.2852 0.1530 0.0702  0.0134  0.0179  120 ALA B N   
1971 C CA  . ALA B 103 ? 0.2562 0.2887 0.1594 0.0868  0.0001  0.0043  120 ALA B CA  
1972 C C   . ALA B 103 ? 0.2558 0.3576 0.1738 0.1147  0.0162  0.0321  120 ALA B C   
1973 O O   . ALA B 103 ? 0.3176 0.3435 0.1750 0.1118  0.0299  0.0165  120 ALA B O   
1974 C CB  . ALA B 103 ? 0.2557 0.2461 0.1494 0.0927  0.0099  0.0072  120 ALA B CB  
1975 N N   . ALA B 104 ? 0.2457 0.3620 0.1913 0.1398  0.0337  0.0945  121 ALA B N   
1976 C CA  . ALA B 104 ? 0.2696 0.3916 0.2232 0.1490  0.0210  0.1133  121 ALA B CA  
1977 C C   . ALA B 104 ? 0.2969 0.3134 0.2498 0.0981  0.0521  0.0825  121 ALA B C   
1978 O O   . ALA B 104 ? 0.2116 0.2541 0.2310 0.0583  0.0086  0.0442  121 ALA B O   
1979 C CB  . ALA B 104 ? 0.3019 0.5028 0.2225 0.1501  -0.0190 0.0897  121 ALA B CB  
1980 N N   . PRO B 105 ? 0.4227 0.2925 0.2770 0.1153  0.1375  0.1081  122 PRO B N   
1981 C CA  . PRO B 105 ? 0.4385 0.2280 0.2856 0.0496  0.1229  0.0740  122 PRO B CA  
1982 C C   . PRO B 105 ? 0.3192 0.2264 0.2675 0.0554  0.0746  0.0627  122 PRO B C   
1983 O O   . PRO B 105 ? 0.2750 0.4050 0.2608 0.1288  0.0717  0.0604  122 PRO B O   
1984 C CB  . PRO B 105 ? 0.6058 0.2313 0.3015 0.0947  0.1636  0.0679  122 PRO B CB  
1985 C CG  . PRO B 105 ? 0.6944 0.3460 0.3066 0.1095  0.1858  0.0630  122 PRO B CG  
1986 C CD  . PRO B 105 ? 0.6060 0.3956 0.2951 0.1244  0.1744  0.0944  122 PRO B CD  
1987 N N   . GLY B 106 ? 0.2068 0.2309 0.2455 0.0440  0.0148  -0.0004 123 GLY B N   
1988 C CA  . GLY B 106 ? 0.2577 0.2070 0.2094 0.0337  -0.0177 -0.0266 123 GLY B CA  
1989 C C   . GLY B 106 ? 0.2124 0.2175 0.1909 0.0061  -0.0151 -0.0272 123 GLY B C   
1990 O O   . GLY B 106 ? 0.2962 0.2521 0.2028 0.0414  0.0166  0.0062  123 GLY B O   
1991 N N   . THR B 107 ? 0.2170 0.2184 0.1732 0.0326  0.0015  -0.0334 124 THR B N   
1992 C CA  . THR B 107 ? 0.1628 0.2174 0.1530 -0.0025 -0.0015 -0.0119 124 THR B CA  
1993 C C   . THR B 107 ? 0.1840 0.2732 0.1503 0.0517  0.0121  0.0047  124 THR B C   
1994 O O   . THR B 107 ? 0.2149 0.2951 0.1548 0.0379  -0.0090 0.0202  124 THR B O   
1995 C CB  . THR B 107 ? 0.2149 0.2356 0.1486 -0.0005 -0.0126 -0.0099 124 THR B CB  
1996 O OG1 . THR B 107 ? 0.2420 0.2158 0.1510 0.0469  -0.0105 0.0037  124 THR B OG1 
1997 C CG2 . THR B 107 ? 0.2396 0.2472 0.1534 0.0035  -0.0555 0.0052  124 THR B CG2 
1998 N N   . ILE B 108 ? 0.1901 0.2259 0.1524 -0.0150 -0.0143 0.0209  125 ILE B N   
1999 C CA  . ILE B 108 ? 0.2313 0.2441 0.1558 0.0522  -0.0130 0.0129  125 ILE B CA  
2000 C C   . ILE B 108 ? 0.2060 0.2755 0.1624 0.0583  -0.0069 0.0216  125 ILE B C   
2001 O O   . ILE B 108 ? 0.1755 0.2751 0.1485 0.0169  -0.0199 0.0151  125 ILE B O   
2002 C CB  . ILE B 108 ? 0.2117 0.2278 0.1659 0.0358  -0.0199 0.0120  125 ILE B CB  
2003 C CG1 . ILE B 108 ? 0.1997 0.2355 0.1756 0.0260  0.0136  0.0220  125 ILE B CG1 
2004 C CG2 . ILE B 108 ? 0.2573 0.2939 0.1669 0.0254  -0.0138 -0.0095 125 ILE B CG2 
2005 C CD1 . ILE B 108 ? 0.2502 0.2429 0.1798 0.0281  0.0002  0.0303  125 ILE B CD1 
2006 N N   . ARG B 109 ? 0.1631 0.2530 0.1712 0.0396  -0.0095 0.0200  126 ARG B N   
2007 C CA  . ARG B 109 ? 0.1999 0.2107 0.1643 0.0482  0.0028  -0.0076 126 ARG B CA  
2008 C C   . ARG B 109 ? 0.2287 0.2167 0.1570 0.0517  -0.0061 0.0011  126 ARG B C   
2009 O O   . ARG B 109 ? 0.1788 0.2476 0.1534 0.0449  0.0193  0.0091  126 ARG B O   
2010 C CB  . ARG B 109 ? 0.2527 0.2153 0.1852 0.0750  -0.0189 -0.0105 126 ARG B CB  
2011 C CG  . ARG B 109 ? 0.3917 0.3229 0.2036 0.1703  -0.0664 -0.0121 126 ARG B CG  
2012 C CD  . ARG B 109 ? 0.3912 0.3021 0.2263 0.1491  -0.0696 0.0124  126 ARG B CD  
2013 N NE  . ARG B 109 ? 0.1919 0.2626 0.2232 0.0632  -0.0306 0.0222  126 ARG B NE  
2014 C CZ  . ARG B 109 ? 0.2627 0.2693 0.2170 0.0268  -0.0420 0.0166  126 ARG B CZ  
2015 N NH1 . ARG B 109 ? 0.3406 0.2945 0.2086 0.0841  -0.0156 0.0911  126 ARG B NH1 
2016 N NH2 . ARG B 109 ? 0.2972 0.2670 0.2149 0.0491  -0.0195 0.0085  126 ARG B NH2 
2017 N N   . ALA B 110 ? 0.1980 0.2483 0.1540 0.0275  -0.0115 0.0247  127 ALA B N   
2018 C CA  . ALA B 110 ? 0.2443 0.2108 0.1554 0.0383  0.0016  0.0127  127 ALA B CA  
2019 C C   . ALA B 110 ? 0.1778 0.2018 0.1586 -0.0008 0.0119  0.0282  127 ALA B C   
2020 O O   . ALA B 110 ? 0.1922 0.2594 0.1787 -0.0167 0.0191  -0.0003 127 ALA B O   
2021 C CB  . ALA B 110 ? 0.2589 0.2396 0.1392 0.0617  0.0186  0.0102  127 ALA B CB  
2022 N N   . ASP B 111 ? 0.1895 0.2141 0.1483 0.0222  0.0240  0.0061  128 ASP B N   
2023 C CA  . ASP B 111 ? 0.2160 0.2183 0.1631 0.0576  -0.0157 -0.0264 128 ASP B CA  
2024 C C   . ASP B 111 ? 0.1974 0.2281 0.1551 0.0276  0.0176  -0.0043 128 ASP B C   
2025 O O   . ASP B 111 ? 0.2345 0.1995 0.1651 0.0417  0.0132  0.0185  128 ASP B O   
2026 C CB  . ASP B 111 ? 0.1710 0.2763 0.1976 0.0567  -0.0156 -0.0291 128 ASP B CB  
2027 C CG  . ASP B 111 ? 0.2096 0.3360 0.2425 0.0550  0.0267  -0.0068 128 ASP B CG  
2028 O OD1 . ASP B 111 ? 0.2534 0.3280 0.2686 0.0754  0.0095  0.0298  128 ASP B OD1 
2029 O OD2 . ASP B 111 ? 0.2603 0.3131 0.2609 0.0501  0.0307  -0.0191 128 ASP B OD2 
2030 N N   . PHE B 112 ? 0.2125 0.1814 0.1342 0.0401  -0.0009 -0.0176 129 PHE B N   
2031 C CA  . PHE B 112 ? 0.1984 0.2035 0.1437 0.0511  0.0069  0.0017  129 PHE B CA  
2032 C C   . PHE B 112 ? 0.1757 0.2456 0.1403 0.0234  0.0028  -0.0084 129 PHE B C   
2033 O O   . PHE B 112 ? 0.2136 0.2427 0.1310 0.0241  -0.0115 0.0063  129 PHE B O   
2034 C CB  . PHE B 112 ? 0.2479 0.2263 0.1474 0.0125  0.0349  0.0335  129 PHE B CB  
2035 C CG  . PHE B 112 ? 0.2183 0.2303 0.1478 0.0075  0.0172  0.0150  129 PHE B CG  
2036 C CD1 . PHE B 112 ? 0.1873 0.2998 0.1555 -0.0135 0.0211  -0.0051 129 PHE B CD1 
2037 C CD2 . PHE B 112 ? 0.1877 0.2768 0.1506 0.0459  0.0315  -0.0013 129 PHE B CD2 
2038 C CE1 . PHE B 112 ? 0.1938 0.3206 0.1604 0.0022  0.0171  0.0043  129 PHE B CE1 
2039 C CE2 . PHE B 112 ? 0.2353 0.2614 0.1587 0.1089  0.0172  0.0155  129 PHE B CE2 
2040 C CZ  . PHE B 112 ? 0.1521 0.2879 0.1611 0.0520  0.0273  0.0011  129 PHE B CZ  
2041 N N   . CYS B 113 ? 0.1781 0.2183 0.1507 0.0615  0.0012  -0.0032 130 CYS B N   
2042 C CA  . CYS B 113 ? 0.1954 0.2195 0.1583 0.0738  0.0164  0.0038  130 CYS B CA  
2043 C C   . CYS B 113 ? 0.1662 0.2818 0.1559 0.0413  0.0018  -0.0007 130 CYS B C   
2044 O O   . CYS B 113 ? 0.1898 0.2602 0.1600 0.0657  -0.0157 -0.0045 130 CYS B O   
2045 C CB  . CYS B 113 ? 0.1814 0.2327 0.1556 0.0440  0.0397  0.0045  130 CYS B CB  
2046 S SG  . CYS B 113 ? 0.2426 0.2316 0.1674 0.0307  0.0384  0.0047  130 CYS B SG  
2047 N N   . GLN B 114 ? 0.1883 0.2270 0.1558 0.0414  0.0316  0.0094  131 GLN B N   
2048 C CA  . GLN B 114 ? 0.1707 0.2563 0.1508 0.0477  0.0266  -0.0073 131 GLN B CA  
2049 C C   . GLN B 114 ? 0.2162 0.2915 0.1555 0.0782  -0.0018 -0.0262 131 GLN B C   
2050 O O   . GLN B 114 ? 0.2169 0.2959 0.1631 0.0249  0.0117  0.0076  131 GLN B O   
2051 C CB  . GLN B 114 ? 0.2046 0.2958 0.1550 0.0286  0.0434  -0.0068 131 GLN B CB  
2052 C CG  . GLN B 114 ? 0.2063 0.2771 0.1472 0.0138  0.0226  -0.0221 131 GLN B CG  
2053 C CD  . GLN B 114 ? 0.2022 0.2320 0.1415 0.0046  0.0303  -0.0044 131 GLN B CD  
2054 O OE1 . GLN B 114 ? 0.2128 0.2876 0.1552 0.0307  0.0140  0.0225  131 GLN B OE1 
2055 N NE2 . GLN B 114 ? 0.2218 0.2740 0.1329 0.0304  0.0015  -0.0137 131 GLN B NE2 
2056 N N   . GLN B 115 ? 0.2288 0.2539 0.1598 0.0615  0.0193  -0.0004 132 GLN B N   
2057 C CA  . GLN B 115 ? 0.2037 0.2887 0.1785 0.0879  0.0313  -0.0152 132 GLN B CA  
2058 C C   . GLN B 115 ? 0.1652 0.2848 0.1751 0.0374  0.0475  -0.0161 132 GLN B C   
2059 O O   . GLN B 115 ? 0.2157 0.2667 0.1651 0.0561  0.0594  -0.0010 132 GLN B O   
2060 C CB  . GLN B 115 ? 0.2426 0.3159 0.2116 0.0758  0.0302  -0.0041 132 GLN B CB  
2061 C CG  . GLN B 115 ? 0.2127 0.3691 0.2286 0.0434  0.0155  -0.0175 132 GLN B CG  
2062 C CD  . GLN B 115 ? 0.2072 0.3491 0.2326 0.0329  -0.0031 -0.0304 132 GLN B CD  
2063 O OE1 . GLN B 115 ? 0.2609 0.3442 0.2429 0.0702  -0.0263 0.0141  132 GLN B OE1 
2064 N NE2 . GLN B 115 ? 0.2704 0.4070 0.2340 0.0795  0.0390  -0.0311 132 GLN B NE2 
2065 N N   . ALA B 116 ? 0.2186 0.3322 0.1819 0.0605  0.0068  -0.0301 133 ALA B N   
2066 C CA  . ALA B 116 ? 0.2495 0.3152 0.1961 0.0800  -0.0060 -0.0346 133 ALA B CA  
2067 C C   . ALA B 116 ? 0.2275 0.2710 0.2117 0.0646  -0.0140 -0.0295 133 ALA B C   
2068 O O   . ALA B 116 ? 0.2414 0.2976 0.2317 0.0527  -0.0067 -0.0159 133 ALA B O   
2069 C CB  . ALA B 116 ? 0.2540 0.3353 0.1949 0.0159  -0.0051 -0.0263 133 ALA B CB  
2070 N N   . GLY B 117 ? 0.2522 0.2976 0.2118 0.1240  -0.0140 -0.0128 134 GLY B N   
2071 C CA  . GLY B 117 ? 0.2654 0.2932 0.1981 0.0923  -0.0179 -0.0399 134 GLY B CA  
2072 C C   . GLY B 117 ? 0.3133 0.2315 0.1882 0.0832  -0.0120 -0.0010 134 GLY B C   
2073 O O   . GLY B 117 ? 0.2788 0.2461 0.1985 0.0784  -0.0134 -0.0060 134 GLY B O   
2074 N N   . ARG B 118 ? 0.2349 0.2462 0.1751 0.0476  -0.0063 -0.0123 135 ARG B N   
2075 C CA  . ARG B 118 ? 0.2349 0.2830 0.1733 0.0738  0.0187  0.0009  135 ARG B CA  
2076 C C   . ARG B 118 ? 0.1995 0.2506 0.1658 0.0716  0.0258  0.0142  135 ARG B C   
2077 O O   . ARG B 118 ? 0.2270 0.2144 0.1792 0.0486  0.0065  -0.0050 135 ARG B O   
2078 C CB  . ARG B 118 ? 0.2094 0.2506 0.1875 0.0834  0.0192  0.0006  135 ARG B CB  
2079 C CG  . ARG B 118 ? 0.2276 0.2725 0.1899 0.0419  0.0195  -0.0132 135 ARG B CG  
2080 C CD  . ARG B 118 ? 0.2346 0.2796 0.1953 0.0448  0.0017  0.0158  135 ARG B CD  
2081 N NE  . ARG B 118 ? 0.2626 0.2782 0.1961 0.1059  0.0120  0.0087  135 ARG B NE  
2082 C CZ  . ARG B 118 ? 0.2529 0.2904 0.2068 0.0752  0.0021  0.0052  135 ARG B CZ  
2083 N NH1 . ARG B 118 ? 0.2745 0.2481 0.2037 0.0902  0.0245  0.0106  135 ARG B NH1 
2084 N NH2 . ARG B 118 ? 0.2579 0.3196 0.2131 0.0673  -0.0055 0.0107  135 ARG B NH2 
2085 N N   . ASN B 119 ? 0.2022 0.2650 0.1534 0.0280  0.0022  0.0109  136 ASN B N   
2086 C CA  . ASN B 119 ? 0.1481 0.2187 0.1456 0.0187  0.0099  0.0030  136 ASN B CA  
2087 C C   . ASN B 119 ? 0.2103 0.2100 0.1443 0.0400  0.0145  0.0174  136 ASN B C   
2088 O O   . ASN B 119 ? 0.2033 0.2851 0.1458 0.0491  -0.0110 0.0166  136 ASN B O   
2089 C CB  . ASN B 119 ? 0.2428 0.2296 0.1400 0.0552  0.0090  0.0068  136 ASN B CB  
2090 C CG  . ASN B 119 ? 0.2838 0.2764 0.1404 0.0712  0.0275  -0.0090 136 ASN B CG  
2091 O OD1 . ASN B 119 ? 0.3245 0.2943 0.1395 0.0528  0.0220  -0.0034 136 ASN B OD1 
2092 N ND2 . ASN B 119 ? 0.2689 0.3297 0.1580 0.0365  0.0308  -0.0294 136 ASN B ND2 
2093 N N   . LEU B 120 ? 0.1887 0.2583 0.1481 0.0644  -0.0098 0.0092  137 LEU B N   
2094 C CA  . LEU B 120 ? 0.2109 0.2117 0.1569 0.0216  0.0054  -0.0059 137 LEU B CA  
2095 C C   . LEU B 120 ? 0.2413 0.2673 0.1557 0.0580  0.0047  -0.0059 137 LEU B C   
2096 O O   . LEU B 120 ? 0.2305 0.2084 0.1573 0.0630  -0.0071 0.0140  137 LEU B O   
2097 C CB  . LEU B 120 ? 0.2317 0.2308 0.1475 0.0338  0.0220  -0.0390 137 LEU B CB  
2098 C CG  . LEU B 120 ? 0.2048 0.2033 0.1481 0.0418  0.0114  -0.0161 137 LEU B CG  
2099 C CD1 . LEU B 120 ? 0.2400 0.2357 0.1555 0.0411  0.0062  -0.0138 137 LEU B CD1 
2100 C CD2 . LEU B 120 ? 0.2215 0.2122 0.1475 0.0390  0.0059  0.0197  137 LEU B CD2 
2101 N N   . ILE B 121 ? 0.2478 0.1830 0.1527 0.0312  0.0354  0.0056  138 ILE B N   
2102 C CA  . ILE B 121 ? 0.2174 0.2015 0.1521 0.0214  0.0019  0.0053  138 ILE B CA  
2103 C C   . ILE B 121 ? 0.2350 0.2371 0.1477 0.0403  0.0057  0.0111  138 ILE B C   
2104 O O   . ILE B 121 ? 0.2641 0.2367 0.1471 0.0525  0.0199  0.0055  138 ILE B O   
2105 C CB  . ILE B 121 ? 0.1673 0.2678 0.1606 -0.0033 0.0001  0.0102  138 ILE B CB  
2106 C CG1 . ILE B 121 ? 0.1657 0.2926 0.1686 0.0577  -0.0045 -0.0031 138 ILE B CG1 
2107 C CG2 . ILE B 121 ? 0.2302 0.2703 0.1692 0.0568  -0.0119 -0.0223 138 ILE B CG2 
2108 C CD1 . ILE B 121 ? 0.1901 0.2807 0.1667 0.0489  -0.0013 0.0057  138 ILE B CD1 
2109 N N   . HIS B 122 ? 0.2902 0.2138 0.1572 0.0138  0.0139  -0.0071 139 HIS B N   
2110 C CA  . HIS B 122 ? 0.2645 0.2118 0.1448 0.0585  0.0200  -0.0123 139 HIS B CA  
2111 C C   . HIS B 122 ? 0.2409 0.2094 0.1336 0.0398  0.0192  0.0027  139 HIS B C   
2112 O O   . HIS B 122 ? 0.2462 0.2539 0.1258 0.0186  0.0051  -0.0002 139 HIS B O   
2113 C CB  . HIS B 122 ? 0.2842 0.2517 0.1652 0.0471  0.0295  -0.0287 139 HIS B CB  
2114 C CG  . HIS B 122 ? 0.2805 0.2711 0.1883 0.0400  0.0224  -0.0416 139 HIS B CG  
2115 N ND1 . HIS B 122 ? 0.3219 0.3616 0.1972 0.0270  0.0381  -0.0825 139 HIS B ND1 
2116 C CD2 . HIS B 122 ? 0.3197 0.1998 0.1919 0.0723  0.0133  -0.0318 139 HIS B CD2 
2117 C CE1 . HIS B 122 ? 0.3310 0.3152 0.1941 0.0080  0.0428  -0.0664 139 HIS B CE1 
2118 N NE2 . HIS B 122 ? 0.3269 0.2497 0.1927 0.0332  0.0009  -0.0697 139 HIS B NE2 
2119 N N   . GLY B 123 ? 0.2914 0.2240 0.1514 0.0405  -0.0093 0.0122  140 GLY B N   
2120 C CA  . GLY B 123 ? 0.2709 0.2190 0.1471 0.0647  -0.0121 0.0126  140 GLY B CA  
2121 C C   . GLY B 123 ? 0.2296 0.2413 0.1558 0.0274  -0.0185 -0.0346 140 GLY B C   
2122 O O   . GLY B 123 ? 0.2860 0.2634 0.1646 0.0330  -0.0014 -0.0076 140 GLY B O   
2123 N N   . SER B 124 ? 0.2466 0.2372 0.1567 0.0530  -0.0115 -0.0391 141 SER B N   
2124 C CA  . SER B 124 ? 0.2323 0.2185 0.1683 0.0298  -0.0331 -0.0487 141 SER B CA  
2125 C C   . SER B 124 ? 0.2949 0.2439 0.1737 0.0334  -0.0199 -0.0403 141 SER B C   
2126 O O   . SER B 124 ? 0.2718 0.2461 0.1753 0.0433  -0.0324 -0.0107 141 SER B O   
2127 C CB  . SER B 124 ? 0.3033 0.1963 0.1814 -0.0016 -0.0302 -0.0232 141 SER B CB  
2128 O OG  . SER B 124 ? 0.2907 0.2482 0.1778 0.0438  -0.0122 0.0062  141 SER B OG  
2129 N N   . ASP B 125 ? 0.3514 0.2633 0.1725 0.0642  -0.0057 -0.0553 142 ASP B N   
2130 C CA  . ASP B 125 ? 0.3487 0.3379 0.1838 0.0195  -0.0218 -0.0312 142 ASP B CA  
2131 C C   . ASP B 125 ? 0.3233 0.2944 0.2022 0.0162  -0.0152 -0.0233 142 ASP B C   
2132 O O   . ASP B 125 ? 0.3673 0.3567 0.2076 0.0284  -0.0574 0.0091  142 ASP B O   
2133 C CB  . ASP B 125 ? 0.3574 0.3408 0.1846 -0.0651 -0.0121 -0.0226 142 ASP B CB  
2134 C CG  . ASP B 125 ? 0.4535 0.4519 0.1949 0.0133  0.0296  -0.0197 142 ASP B CG  
2135 O OD1 . ASP B 125 ? 0.4971 0.3923 0.1992 0.0869  0.0035  -0.0349 142 ASP B OD1 
2136 O OD2 . ASP B 125 ? 0.5656 0.5313 0.2109 -0.0052 0.0629  -0.0349 142 ASP B OD2 
2137 N N   . SER B 126 ? 0.3435 0.2815 0.2189 0.0576  -0.0203 -0.0707 143 SER B N   
2138 C CA  . SER B 126 ? 0.3342 0.3146 0.2304 0.0170  -0.0094 -0.0799 143 SER B CA  
2139 C C   . SER B 126 ? 0.3648 0.2968 0.2455 0.0350  -0.0197 -0.0479 143 SER B C   
2140 O O   . SER B 126 ? 0.3256 0.2636 0.2308 0.0271  -0.0179 -0.0173 143 SER B O   
2141 C CB  . SER B 126 ? 0.3689 0.3117 0.2339 0.0276  -0.0087 -0.0987 143 SER B CB  
2142 O OG  . SER B 126 ? 0.4075 0.3849 0.2390 0.0789  -0.0159 -0.1054 143 SER B OG  
2143 N N   . ALA B 127 ? 0.3774 0.3173 0.2671 0.0068  -0.0433 -0.0506 144 ALA B N   
2144 C CA  . ALA B 127 ? 0.3793 0.3197 0.2890 0.0125  -0.0603 -0.0558 144 ALA B CA  
2145 C C   . ALA B 127 ? 0.3698 0.2874 0.2978 0.0067  -0.0481 -0.0766 144 ALA B C   
2146 O O   . ALA B 127 ? 0.3986 0.2833 0.2995 0.0365  -0.0592 -0.0769 144 ALA B O   
2147 C CB  . ALA B 127 ? 0.3327 0.2818 0.3016 -0.0363 -0.0654 -0.0490 144 ALA B CB  
2148 N N   . GLU B 128 ? 0.3750 0.2932 0.3062 0.0272  -0.0339 -0.1112 145 GLU B N   
2149 C CA  . GLU B 128 ? 0.3829 0.3220 0.3130 -0.0072 -0.0269 -0.0996 145 GLU B CA  
2150 C C   . GLU B 128 ? 0.3331 0.2494 0.2960 0.0280  -0.0246 -0.1068 145 GLU B C   
2151 O O   . GLU B 128 ? 0.3693 0.3061 0.2920 0.0780  -0.0091 -0.0828 145 GLU B O   
2152 C CB  . GLU B 128 ? 0.5450 0.4120 0.3368 0.0994  -0.0147 -0.1023 145 GLU B CB  
2153 C CG  . GLU B 128 ? 0.7745 0.5746 0.3597 0.1850  -0.0009 -0.0869 145 GLU B CG  
2154 C CD  . GLU B 128 ? 0.9721 0.7570 0.3847 0.3176  0.0057  -0.0443 145 GLU B CD  
2155 O OE1 . GLU B 128 ? 1.0436 0.7608 0.3902 0.3551  0.0027  -0.0353 145 GLU B OE1 
2156 O OE2 . GLU B 128 ? 1.0203 0.8485 0.3988 0.3601  0.0147  -0.0280 145 GLU B OE2 
2157 N N   . SER B 129 ? 0.3139 0.2248 0.2908 0.0382  -0.0209 -0.0665 146 SER B N   
2158 C CA  A SER B 129 ? 0.3225 0.2883 0.2830 0.0573  -0.0234 -0.0570 146 SER B CA  
2159 C CA  B SER B 129 ? 0.3369 0.2874 0.2823 0.0676  -0.0126 -0.0638 146 SER B CA  
2160 C C   . SER B 129 ? 0.2894 0.2657 0.2786 0.0261  -0.0130 -0.0521 146 SER B C   
2161 O O   . SER B 129 ? 0.2474 0.2840 0.2775 0.0033  -0.0216 -0.0214 146 SER B O   
2162 C CB  A SER B 129 ? 0.3058 0.2712 0.2815 0.0315  -0.0350 -0.0450 146 SER B CB  
2163 C CB  B SER B 129 ? 0.3545 0.2820 0.2794 0.0611  -0.0018 -0.0750 146 SER B CB  
2164 O OG  A SER B 129 ? 0.2893 0.2867 0.2820 0.0310  -0.0582 -0.0238 146 SER B OG  
2165 O OG  B SER B 129 ? 0.3944 0.3450 0.2802 0.0744  0.0023  -0.0685 146 SER B OG  
2166 N N   . ALA B 130 ? 0.2804 0.2707 0.2749 0.0379  -0.0106 -0.0655 147 ALA B N   
2167 C CA  . ALA B 130 ? 0.3237 0.2156 0.2852 0.0032  0.0095  -0.0878 147 ALA B CA  
2168 C C   . ALA B 130 ? 0.3106 0.2472 0.2855 -0.0117 0.0174  -0.0644 147 ALA B C   
2169 O O   . ALA B 130 ? 0.3088 0.2918 0.2809 0.0225  0.0311  -0.0597 147 ALA B O   
2170 C CB  . ALA B 130 ? 0.3608 0.2340 0.2919 0.0279  0.0070  -0.0986 147 ALA B CB  
2171 N N   . LYS B 131 ? 0.3228 0.2226 0.2864 0.0265  -0.0029 -0.0768 148 LYS B N   
2172 C CA  . LYS B 131 ? 0.3780 0.3080 0.2965 -0.0080 -0.0285 -0.0536 148 LYS B CA  
2173 C C   . LYS B 131 ? 0.3590 0.2422 0.3000 0.0121  -0.0080 -0.0415 148 LYS B C   
2174 O O   . LYS B 131 ? 0.4049 0.3017 0.3064 0.0076  0.0119  -0.0295 148 LYS B O   
2175 C CB  . LYS B 131 ? 0.4852 0.5785 0.3098 -0.0055 -0.0391 -0.0563 148 LYS B CB  
2176 C CG  . LYS B 131 ? 0.6517 0.8279 0.3224 0.0078  -0.0571 -0.0566 148 LYS B CG  
2177 C CD  . LYS B 131 ? 0.7542 1.0482 0.3313 0.0447  -0.0668 -0.0544 148 LYS B CD  
2178 C CE  . LYS B 131 ? 0.8674 1.2054 0.3351 0.1176  -0.0694 -0.0406 148 LYS B CE  
2179 N NZ  . LYS B 131 ? 0.9271 1.2804 0.3470 0.1606  -0.0729 -0.0307 148 LYS B NZ  
2180 N N   . ARG B 132 ? 0.3560 0.2238 0.2963 0.0210  -0.0107 -0.0553 149 ARG B N   
2181 C CA  A ARG B 132 ? 0.3329 0.2396 0.2923 0.0228  -0.0049 -0.0373 149 ARG B CA  
2182 C CA  B ARG B 132 ? 0.3333 0.2272 0.2955 0.0357  0.0081  -0.0317 149 ARG B CA  
2183 C C   . ARG B 132 ? 0.3315 0.2104 0.2830 0.0906  -0.0023 -0.0262 149 ARG B C   
2184 O O   . ARG B 132 ? 0.3868 0.2370 0.2800 0.0533  -0.0179 -0.0188 149 ARG B O   
2185 C CB  A ARG B 132 ? 0.3677 0.3421 0.2989 0.0661  0.0005  -0.0367 149 ARG B CB  
2186 C CB  B ARG B 132 ? 0.3655 0.3017 0.3084 0.0949  0.0364  -0.0211 149 ARG B CB  
2187 C CG  A ARG B 132 ? 0.4058 0.3966 0.3061 0.0538  -0.0094 -0.0360 149 ARG B CG  
2188 C CG  B ARG B 132 ? 0.4094 0.3127 0.3217 0.1222  0.0475  -0.0133 149 ARG B CG  
2189 C CD  A ARG B 132 ? 0.4282 0.4477 0.3103 0.0130  -0.0010 -0.0468 149 ARG B CD  
2190 C CD  B ARG B 132 ? 0.4452 0.3667 0.3328 0.1428  0.0794  -0.0094 149 ARG B CD  
2191 N NE  A ARG B 132 ? 0.4545 0.5464 0.3146 -0.0222 -0.0042 -0.0299 149 ARG B NE  
2192 N NE  B ARG B 132 ? 0.4671 0.4091 0.3421 0.1796  0.1105  0.0256  149 ARG B NE  
2193 C CZ  A ARG B 132 ? 0.3945 0.5510 0.3088 -0.0933 -0.0156 -0.0164 149 ARG B CZ  
2194 C CZ  B ARG B 132 ? 0.4274 0.4619 0.3455 0.1533  0.1530  0.0393  149 ARG B CZ  
2195 N NH1 A ARG B 132 ? 0.3546 0.5471 0.3058 -0.1589 0.0052  -0.0080 149 ARG B NH1 
2196 N NH1 B ARG B 132 ? 0.5017 0.4797 0.3378 0.1807  0.1835  0.0338  149 ARG B NH1 
2197 N NH2 A ARG B 132 ? 0.3964 0.5644 0.3060 -0.0617 -0.0389 -0.0168 149 ARG B NH2 
2198 N NH2 B ARG B 132 ? 0.3609 0.4458 0.3535 0.1438  0.1565  0.0532  149 ARG B NH2 
2199 N N   . GLU B 133 ? 0.3166 0.1935 0.2675 0.0303  0.0053  -0.0510 150 GLU B N   
2200 C CA  . GLU B 133 ? 0.2855 0.2034 0.2506 0.0100  0.0039  -0.0211 150 GLU B CA  
2201 C C   . GLU B 133 ? 0.3168 0.2357 0.2495 0.0187  0.0216  0.0089  150 GLU B C   
2202 O O   . GLU B 133 ? 0.3817 0.2332 0.2414 0.0495  0.0062  0.0112  150 GLU B O   
2203 C CB  . GLU B 133 ? 0.3254 0.1947 0.2454 0.0653  -0.0097 -0.0136 150 GLU B CB  
2204 C CG  . GLU B 133 ? 0.3431 0.2093 0.2512 0.0514  -0.0119 -0.0192 150 GLU B CG  
2205 C CD  . GLU B 133 ? 0.3177 0.2468 0.2560 0.0208  0.0007  -0.0179 150 GLU B CD  
2206 O OE1 . GLU B 133 ? 0.3474 0.2425 0.2541 0.0456  -0.0379 -0.0352 150 GLU B OE1 
2207 O OE2 . GLU B 133 ? 0.3265 0.2619 0.2695 0.0316  0.0326  -0.0095 150 GLU B OE2 
2208 N N   . ILE B 134 ? 0.3900 0.2235 0.2570 0.0264  0.0361  -0.0176 151 ILE B N   
2209 C CA  . ILE B 134 ? 0.3143 0.2700 0.2779 -0.0351 0.0444  -0.0016 151 ILE B CA  
2210 C C   . ILE B 134 ? 0.3468 0.2529 0.2945 -0.0278 0.0377  0.0175  151 ILE B C   
2211 O O   . ILE B 134 ? 0.3729 0.2721 0.2956 -0.0047 0.0312  0.0077  151 ILE B O   
2212 C CB  . ILE B 134 ? 0.3603 0.2330 0.2847 -0.0494 0.0273  -0.0152 151 ILE B CB  
2213 C CG1 . ILE B 134 ? 0.3661 0.2056 0.2838 -0.0088 0.0265  -0.0495 151 ILE B CG1 
2214 C CG2 . ILE B 134 ? 0.4386 0.2344 0.2890 -0.0154 0.0196  0.0032  151 ILE B CG2 
2215 C CD1 . ILE B 134 ? 0.3678 0.2751 0.2843 0.0478  0.0521  -0.0112 151 ILE B CD1 
2216 N N   . SER B 135 ? 0.4149 0.2152 0.3130 0.0216  0.0099  0.0017  152 SER B N   
2217 C CA  . SER B 135 ? 0.4061 0.2513 0.3292 0.0146  -0.0160 -0.0053 152 SER B CA  
2218 C C   . SER B 135 ? 0.4334 0.2406 0.3207 0.0333  -0.0024 0.0401  152 SER B C   
2219 O O   . SER B 135 ? 0.4777 0.2851 0.3237 0.0230  0.0211  0.0808  152 SER B O   
2220 C CB  . SER B 135 ? 0.4364 0.3008 0.3498 -0.0360 -0.0448 -0.0231 152 SER B CB  
2221 O OG  . SER B 135 ? 0.5882 0.3634 0.3682 -0.0144 -0.0320 -0.0043 152 SER B OG  
2222 N N   . LEU B 136 ? 0.4275 0.2343 0.3108 0.0309  0.0083  0.0103  153 LEU B N   
2223 C CA  . LEU B 136 ? 0.4675 0.1604 0.3050 -0.0291 0.0214  -0.0144 153 LEU B CA  
2224 C C   . LEU B 136 ? 0.4649 0.1518 0.3031 0.0202  0.0305  -0.0150 153 LEU B C   
2225 O O   . LEU B 136 ? 0.5442 0.2188 0.3029 0.1211  0.0462  -0.0024 153 LEU B O   
2226 C CB  . LEU B 136 ? 0.5811 0.1856 0.3106 0.0626  0.0106  0.0055  153 LEU B CB  
2227 C CG  . LEU B 136 ? 0.6255 0.2490 0.3141 0.1618  0.0113  0.0125  153 LEU B CG  
2228 C CD1 . LEU B 136 ? 0.6725 0.3221 0.3188 0.1656  0.0051  -0.0274 153 LEU B CD1 
2229 C CD2 . LEU B 136 ? 0.6743 0.2557 0.3154 0.1635  0.0106  0.0268  153 LEU B CD2 
2230 N N   . TRP B 137 ? 0.4046 0.2176 0.3039 0.0774  0.0281  -0.0267 154 TRP B N   
2231 C CA  . TRP B 137 ? 0.3385 0.1826 0.3004 0.0739  0.0219  -0.0216 154 TRP B CA  
2232 C C   . TRP B 137 ? 0.3833 0.2180 0.3131 0.0909  0.0380  0.0034  154 TRP B C   
2233 O O   . TRP B 137 ? 0.4076 0.3253 0.3090 0.1073  0.0483  0.0018  154 TRP B O   
2234 C CB  . TRP B 137 ? 0.3364 0.2674 0.2882 0.1282  0.0019  -0.0240 154 TRP B CB  
2235 C CG  . TRP B 137 ? 0.3679 0.2384 0.2696 0.1132  -0.0212 -0.0250 154 TRP B CG  
2236 C CD1 . TRP B 137 ? 0.3474 0.2394 0.2646 0.0481  -0.0335 -0.0289 154 TRP B CD1 
2237 C CD2 . TRP B 137 ? 0.3417 0.2636 0.2678 0.1203  -0.0503 -0.0369 154 TRP B CD2 
2238 N NE1 . TRP B 137 ? 0.3481 0.2070 0.2589 0.0733  -0.0564 -0.0215 154 TRP B NE1 
2239 C CE2 . TRP B 137 ? 0.2975 0.3021 0.2694 0.1256  -0.0540 -0.0196 154 TRP B CE2 
2240 C CE3 . TRP B 137 ? 0.3326 0.3181 0.2686 0.1677  -0.0475 -0.0457 154 TRP B CE3 
2241 C CZ2 . TRP B 137 ? 0.3244 0.2612 0.2709 0.1225  -0.0618 -0.0103 154 TRP B CZ2 
2242 C CZ3 . TRP B 137 ? 0.3528 0.2857 0.2678 0.1656  -0.0541 -0.0599 154 TRP B CZ3 
2243 C CH2 . TRP B 137 ? 0.2937 0.3199 0.2675 0.1419  -0.0587 -0.0453 154 TRP B CH2 
2244 N N   . PHE B 138 ? 0.3643 0.2978 0.3307 0.0673  0.0161  -0.0061 155 PHE B N   
2245 C CA  . PHE B 138 ? 0.3356 0.2767 0.3521 0.0234  0.0243  -0.0004 155 PHE B CA  
2246 C C   . PHE B 138 ? 0.4553 0.2445 0.4045 0.0697  0.0514  0.0033  155 PHE B C   
2247 O O   . PHE B 138 ? 0.5541 0.2808 0.4102 0.0350  0.0558  0.0055  155 PHE B O   
2248 C CB  . PHE B 138 ? 0.3145 0.3085 0.3200 0.0549  0.0023  -0.0150 155 PHE B CB  
2249 C CG  . PHE B 138 ? 0.2815 0.2025 0.2877 0.0313  0.0089  0.0051  155 PHE B CG  
2250 C CD1 . PHE B 138 ? 0.3476 0.2385 0.2799 0.0769  -0.0001 -0.0140 155 PHE B CD1 
2251 C CD2 . PHE B 138 ? 0.2029 0.2215 0.2721 0.0058  0.0036  -0.0131 155 PHE B CD2 
2252 C CE1 . PHE B 138 ? 0.3256 0.2650 0.2710 0.1166  -0.0018 0.0150  155 PHE B CE1 
2253 C CE2 . PHE B 138 ? 0.2359 0.2479 0.2683 -0.0044 -0.0212 0.0039  155 PHE B CE2 
2254 C CZ  . PHE B 138 ? 0.3023 0.2601 0.2707 0.0750  -0.0263 -0.0032 155 PHE B CZ  
2255 N N   . LYS B 139 ? 0.4738 0.3651 0.4537 0.1373  0.0641  0.0240  156 LYS B N   
2256 C CA  . LYS B 139 ? 0.5430 0.4044 0.5020 0.1300  0.0547  0.0155  156 LYS B CA  
2257 C C   . LYS B 139 ? 0.5437 0.3246 0.5407 0.0779  0.0870  0.0083  156 LYS B C   
2258 O O   . LYS B 139 ? 0.5773 0.2357 0.5451 0.0878  0.1363  0.0384  156 LYS B O   
2259 C CB  . LYS B 139 ? 0.6208 0.5256 0.5083 0.1745  0.0431  0.0434  156 LYS B CB  
2260 C CG  . LYS B 139 ? 0.6967 0.6743 0.5140 0.2235  0.0090  0.0607  156 LYS B CG  
2261 C CD  . LYS B 139 ? 0.7730 0.8231 0.5229 0.2477  -0.0016 0.0588  156 LYS B CD  
2262 C CE  . LYS B 139 ? 0.7900 0.8991 0.5282 0.2594  -0.0050 0.0533  156 LYS B CE  
2263 N NZ  . LYS B 139 ? 0.7887 0.9097 0.5309 0.2762  -0.0006 0.0382  156 LYS B NZ  
2264 N N   . PRO B 140 ? 0.5874 0.3297 0.5713 0.0175  0.0750  -0.0251 157 PRO B N   
2265 C CA  . PRO B 140 ? 0.5793 0.3509 0.5824 -0.1176 0.0646  -0.0195 157 PRO B CA  
2266 C C   . PRO B 140 ? 0.5938 0.4186 0.5792 -0.0889 0.0767  0.0398  157 PRO B C   
2267 O O   . PRO B 140 ? 0.5829 0.5146 0.5890 -0.0287 0.0636  0.0502  157 PRO B O   
2268 C CB  . PRO B 140 ? 0.5850 0.3745 0.5859 -0.1387 0.0591  -0.0522 157 PRO B CB  
2269 C CG  . PRO B 140 ? 0.6003 0.3726 0.5856 -0.0937 0.0584  -0.0400 157 PRO B CG  
2270 C CD  . PRO B 140 ? 0.5889 0.3692 0.5806 -0.0224 0.0755  -0.0407 157 PRO B CD  
2271 N N   . GLU B 141 ? 0.6545 0.4208 0.5677 -0.0017 0.0943  0.0757  158 GLU B N   
2272 C CA  . GLU B 141 ? 0.7104 0.4847 0.5503 0.0759  0.1067  0.0963  158 GLU B CA  
2273 C C   . GLU B 141 ? 0.6808 0.4346 0.5285 0.0947  0.1316  0.1018  158 GLU B C   
2274 O O   . GLU B 141 ? 0.7036 0.4303 0.5348 0.0524  0.1527  0.0987  158 GLU B O   
2275 C CB  . GLU B 141 ? 0.7618 0.6031 0.5537 0.1380  0.0944  0.1041  158 GLU B CB  
2276 N N   . GLU B 142 ? 0.6276 0.3166 0.4974 0.1276  0.1243  0.1127  159 GLU B N   
2277 C CA  . GLU B 142 ? 0.5303 0.4286 0.4640 0.1014  0.1183  0.1010  159 GLU B CA  
2278 C C   . GLU B 142 ? 0.4469 0.3627 0.4269 0.0927  0.1120  0.0682  159 GLU B C   
2279 O O   . GLU B 142 ? 0.4299 0.3571 0.4132 0.1209  0.1103  0.0267  159 GLU B O   
2280 C CB  . GLU B 142 ? 0.4940 0.4318 0.4636 0.0801  0.1163  0.1490  159 GLU B CB  
2281 C CG  . GLU B 142 ? 0.5102 0.4147 0.4673 0.1647  0.0954  0.1659  159 GLU B CG  
2282 C CD  . GLU B 142 ? 0.5488 0.5256 0.4705 0.2196  0.0848  0.1962  159 GLU B CD  
2283 O OE1 . GLU B 142 ? 0.5071 0.5464 0.4671 0.2567  0.0770  0.2046  159 GLU B OE1 
2284 O OE2 . GLU B 142 ? 0.6252 0.6032 0.4747 0.2615  0.0943  0.2064  159 GLU B OE2 
2285 N N   . ILE B 143 ? 0.4162 0.3317 0.4129 0.0663  0.1156  0.0224  160 ILE B N   
2286 C CA  . ILE B 143 ? 0.3812 0.2807 0.3926 -0.0461 0.0942  -0.0003 160 ILE B CA  
2287 C C   . ILE B 143 ? 0.4046 0.3446 0.3716 0.0183  0.0888  0.0019  160 ILE B C   
2288 O O   . ILE B 143 ? 0.4529 0.3167 0.3837 -0.0086 0.1055  -0.0102 160 ILE B O   
2289 C CB  . ILE B 143 ? 0.4352 0.3387 0.3988 -0.0237 0.0794  -0.0272 160 ILE B CB  
2290 C CG1 . ILE B 143 ? 0.5337 0.4114 0.4086 0.0702  0.0522  -0.0449 160 ILE B CG1 
2291 C CG2 . ILE B 143 ? 0.4637 0.2703 0.3913 -0.0515 0.0821  -0.0441 160 ILE B CG2 
2292 C CD1 . ILE B 143 ? 0.5761 0.5032 0.4146 0.1465  0.0301  -0.0451 160 ILE B CD1 
2293 N N   . GLN B 144 ? 0.3072 0.2576 0.3360 -0.0027 0.0683  0.0289  161 GLN B N   
2294 C CA  . GLN B 144 ? 0.2947 0.2539 0.3101 -0.0069 0.0559  0.0215  161 GLN B CA  
2295 C C   . GLN B 144 ? 0.3132 0.2232 0.2835 -0.0219 0.0310  0.0029  161 GLN B C   
2296 O O   . GLN B 144 ? 0.3097 0.2406 0.2858 -0.0096 0.0360  0.0342  161 GLN B O   
2297 C CB  . GLN B 144 ? 0.2508 0.2707 0.3142 -0.0349 0.0571  0.0084  161 GLN B CB  
2298 C CG  . GLN B 144 ? 0.3511 0.3940 0.3274 0.0589  0.0487  0.0198  161 GLN B CG  
2299 C CD  . GLN B 144 ? 0.4043 0.3884 0.3368 0.0810  0.0572  0.0531  161 GLN B CD  
2300 O OE1 . GLN B 144 ? 0.4718 0.3366 0.3437 0.0821  0.0417  0.0657  161 GLN B OE1 
2301 N NE2 . GLN B 144 ? 0.3480 0.3487 0.3397 0.0371  0.0471  0.0709  161 GLN B NE2 
2302 N N   . SER B 145 ? 0.2883 0.2564 0.2702 -0.0259 0.0103  -0.0168 162 SER B N   
2303 C CA  A SER B 145 ? 0.3087 0.2570 0.2679 -0.0105 0.0002  -0.0205 162 SER B CA  
2304 C CA  B SER B 145 ? 0.2988 0.2471 0.2672 -0.0111 0.0192  -0.0183 162 SER B CA  
2305 C C   . SER B 145 ? 0.3180 0.2393 0.2582 0.0111  0.0139  -0.0023 162 SER B C   
2306 O O   . SER B 145 ? 0.3767 0.2678 0.2792 0.0440  0.0378  0.0413  162 SER B O   
2307 C CB  A SER B 145 ? 0.3567 0.3271 0.2689 -0.0310 -0.0166 -0.0341 162 SER B CB  
2308 C CB  B SER B 145 ? 0.3237 0.2928 0.2671 -0.0138 0.0424  -0.0216 162 SER B CB  
2309 O OG  A SER B 145 ? 0.3915 0.3188 0.2703 -0.0434 -0.0389 -0.0288 162 SER B OG  
2310 O OG  B SER B 145 ? 0.3944 0.2996 0.2655 0.0629  0.0619  -0.0070 162 SER B OG  
2311 N N   . TYR B 146 ? 0.2915 0.2012 0.2427 -0.0150 0.0060  0.0367  163 TYR B N   
2312 C CA  . TYR B 146 ? 0.3111 0.2405 0.2280 0.0067  -0.0193 0.0188  163 TYR B CA  
2313 C C   . TYR B 146 ? 0.2854 0.2591 0.2293 -0.0057 -0.0152 0.0170  163 TYR B C   
2314 O O   . TYR B 146 ? 0.2818 0.2763 0.2156 -0.0309 -0.0075 0.0234  163 TYR B O   
2315 C CB  . TYR B 146 ? 0.2710 0.2832 0.2124 0.0113  -0.0133 0.0064  163 TYR B CB  
2316 C CG  . TYR B 146 ? 0.2561 0.2389 0.2071 -0.0105 -0.0062 0.0231  163 TYR B CG  
2317 C CD1 . TYR B 146 ? 0.1968 0.2674 0.2034 0.0350  -0.0087 0.0101  163 TYR B CD1 
2318 C CD2 . TYR B 146 ? 0.2049 0.2164 0.2016 0.0080  -0.0055 -0.0101 163 TYR B CD2 
2319 C CE1 . TYR B 146 ? 0.2286 0.2643 0.1905 0.0111  0.0085  0.0278  163 TYR B CE1 
2320 C CE2 . TYR B 146 ? 0.1934 0.2513 0.1955 -0.0214 -0.0006 0.0003  163 TYR B CE2 
2321 C CZ  . TYR B 146 ? 0.1984 0.2778 0.1931 0.0061  0.0052  0.0154  163 TYR B CZ  
2322 O OH  . TYR B 146 ? 0.2331 0.2488 0.1930 0.0240  -0.0115 0.0061  163 TYR B OH  
2323 N N   . LYS B 147 ? 0.2822 0.2594 0.2310 -0.0264 0.0077  0.0185  164 LYS B N   
2324 C CA  . LYS B 147 ? 0.2463 0.2570 0.2295 -0.0459 -0.0328 0.0035  164 LYS B CA  
2325 C C   . LYS B 147 ? 0.2394 0.2455 0.2187 -0.0444 -0.0311 0.0279  164 LYS B C   
2326 O O   . LYS B 147 ? 0.2962 0.3117 0.2066 -0.0538 -0.0415 0.0323  164 LYS B O   
2327 C CB  . LYS B 147 ? 0.2695 0.2668 0.2593 -0.0729 -0.0522 -0.0084 164 LYS B CB  
2328 C CG  . LYS B 147 ? 0.4217 0.4257 0.2896 -0.0294 -0.0766 0.0276  164 LYS B CG  
2329 C CD  . LYS B 147 ? 0.5705 0.5045 0.3154 0.0077  -0.0930 0.0555  164 LYS B CD  
2330 C CE  . LYS B 147 ? 0.6669 0.5970 0.3265 0.0100  -0.0998 0.0790  164 LYS B CE  
2331 N NZ  . LYS B 147 ? 0.7568 0.5937 0.3339 0.0400  -0.0958 0.0624  164 LYS B NZ  
2332 N N   . LEU B 148 ? 0.2407 0.2346 0.2083 -0.0143 -0.0137 0.0240  165 LEU B N   
2333 C CA  . LEU B 148 ? 0.2070 0.2333 0.2013 0.0007  0.0068  0.0062  165 LEU B CA  
2334 C C   . LEU B 148 ? 0.2368 0.2690 0.1921 -0.0042 -0.0018 0.0164  165 LEU B C   
2335 O O   . LEU B 148 ? 0.2365 0.2564 0.1871 -0.0094 -0.0105 -0.0016 165 LEU B O   
2336 C CB  . LEU B 148 ? 0.2203 0.2586 0.2041 -0.0151 0.0025  -0.0023 165 LEU B CB  
2337 C CG  . LEU B 148 ? 0.2215 0.2438 0.2150 -0.0130 0.0008  0.0083  165 LEU B CG  
2338 C CD1 . LEU B 148 ? 0.2924 0.2745 0.2233 0.0451  0.0024  0.0111  165 LEU B CD1 
2339 C CD2 . LEU B 148 ? 0.1934 0.3040 0.2189 -0.0257 0.0182  0.0408  165 LEU B CD2 
2340 N N   . ALA B 149 ? 0.2613 0.2538 0.1863 0.0008  -0.0034 0.0152  166 ALA B N   
2341 C CA  . ALA B 149 ? 0.2975 0.2660 0.1840 0.0025  -0.0009 0.0038  166 ALA B CA  
2342 C C   . ALA B 149 ? 0.3026 0.2332 0.1992 0.0177  0.0062  0.0247  166 ALA B C   
2343 O O   . ALA B 149 ? 0.3040 0.2998 0.2282 0.0540  0.0079  0.0325  166 ALA B O   
2344 C CB  . ALA B 149 ? 0.3650 0.3662 0.1801 0.0232  0.0016  0.0313  166 ALA B CB  
2345 N N   . LEU B 150 ? 0.2502 0.2623 0.1860 0.0099  0.0165  0.0321  167 LEU B N   
2346 C CA  . LEU B 150 ? 0.2600 0.2718 0.1771 -0.0294 0.0091  0.0065  167 LEU B CA  
2347 C C   . LEU B 150 ? 0.1985 0.2948 0.1788 -0.0565 0.0173  0.0113  167 LEU B C   
2348 O O   . LEU B 150 ? 0.2403 0.2476 0.1918 -0.0275 0.0014  0.0059  167 LEU B O   
2349 C CB  . LEU B 150 ? 0.3874 0.3555 0.1798 -0.0561 -0.0066 -0.0006 167 LEU B CB  
2350 C CG  . LEU B 150 ? 0.4676 0.4331 0.1798 -0.0878 -0.0237 0.0374  167 LEU B CG  
2351 C CD1 . LEU B 150 ? 0.5489 0.4769 0.1943 -0.1166 -0.0653 0.0552  167 LEU B CD1 
2352 C CD2 . LEU B 150 ? 0.5499 0.5017 0.1844 -0.0978 0.0259  0.0147  167 LEU B CD2 
2353 N N   . SER B 151 ? 0.2372 0.2522 0.1779 -0.0452 0.0066  0.0161  168 SER B N   
2354 C CA  A SER B 151 ? 0.2702 0.2453 0.1814 0.0011  0.0119  -0.0050 168 SER B CA  
2355 C CA  B SER B 151 ? 0.2725 0.1885 0.1891 0.0029  -0.0050 -0.0094 168 SER B CA  
2356 C C   . SER B 151 ? 0.2187 0.2462 0.1863 -0.0289 0.0162  -0.0009 168 SER B C   
2357 O O   . SER B 151 ? 0.2536 0.2773 0.1697 -0.0035 0.0098  -0.0090 168 SER B O   
2358 C CB  A SER B 151 ? 0.3393 0.2548 0.1850 0.0683  0.0075  -0.0238 168 SER B CB  
2359 C CB  B SER B 151 ? 0.2839 0.1500 0.2179 0.0550  -0.0504 -0.0247 168 SER B CB  
2360 O OG  A SER B 151 ? 0.4000 0.2766 0.1862 0.1157  0.0144  -0.0430 168 SER B OG  
2361 O OG  B SER B 151 ? 0.3012 0.2585 0.2409 0.0084  -0.0378 -0.0175 168 SER B OG  
2362 N N   . ASP B 152 ? 0.2014 0.2801 0.2045 -0.0141 -0.0282 0.0093  169 ASP B N   
2363 C CA  . ASP B 152 ? 0.2561 0.2959 0.2212 0.0098  -0.0001 0.0171  169 ASP B CA  
2364 C C   . ASP B 152 ? 0.1986 0.2691 0.2133 -0.0108 -0.0193 -0.0026 169 ASP B C   
2365 O O   . ASP B 152 ? 0.2251 0.2744 0.2236 0.0010  -0.0302 0.0013  169 ASP B O   
2366 C CB  . ASP B 152 ? 0.2734 0.3481 0.2528 -0.0357 0.0460  0.0420  169 ASP B CB  
2367 C CG  . ASP B 152 ? 0.3526 0.4484 0.2847 -0.0404 0.0500  0.0113  169 ASP B CG  
2368 O OD1 . ASP B 152 ? 0.3796 0.4320 0.3059 -0.1130 0.0138  -0.0122 169 ASP B OD1 
2369 O OD2 . ASP B 152 ? 0.4033 0.4910 0.3046 0.0075  0.1004  0.0249  169 ASP B OD2 
2370 N N   . TYR B 153 ? 0.1742 0.2242 0.2071 -0.0150 -0.0045 -0.0040 170 TYR B N   
2371 C CA  . TYR B 153 ? 0.1672 0.2309 0.1936 0.0095  0.0004  -0.0235 170 TYR B CA  
2372 C C   . TYR B 153 ? 0.1699 0.2411 0.2008 0.0145  0.0317  -0.0193 170 TYR B C   
2373 O O   . TYR B 153 ? 0.2621 0.2203 0.1922 0.0141  0.0620  -0.0038 170 TYR B O   
2374 C CB  . TYR B 153 ? 0.2089 0.2139 0.1936 -0.0337 0.0150  -0.0331 170 TYR B CB  
2375 C CG  . TYR B 153 ? 0.2247 0.2860 0.1900 -0.0071 0.0169  -0.0073 170 TYR B CG  
2376 C CD1 . TYR B 153 ? 0.1838 0.2788 0.2018 0.0163  0.0213  0.0059  170 TYR B CD1 
2377 C CD2 . TYR B 153 ? 0.2343 0.2721 0.1820 0.0039  0.0238  -0.0002 170 TYR B CD2 
2378 C CE1 . TYR B 153 ? 0.2187 0.2949 0.2024 0.0102  0.0424  0.0082  170 TYR B CE1 
2379 C CE2 . TYR B 153 ? 0.2510 0.3086 0.1912 -0.0106 0.0249  -0.0284 170 TYR B CE2 
2380 C CZ  . TYR B 153 ? 0.2116 0.3036 0.2104 -0.0369 0.0659  0.0017  170 TYR B CZ  
2381 O OH  . TYR B 153 ? 0.2510 0.3468 0.2382 -0.0278 0.0730  -0.0393 170 TYR B OH  
2382 N N   . ILE B 154 ? 0.2176 0.2371 0.2163 0.0218  0.0432  0.0146  171 ILE B N   
2383 C CA  . ILE B 154 ? 0.2268 0.2118 0.2310 0.0249  0.0430  0.0082  171 ILE B CA  
2384 C C   . ILE B 154 ? 0.1928 0.2225 0.2346 0.0075  0.0485  0.0187  171 ILE B C   
2385 O O   . ILE B 154 ? 0.2713 0.2433 0.2551 0.0115  0.0508  0.0085  171 ILE B O   
2386 C CB  . ILE B 154 ? 0.2098 0.2437 0.2440 0.0348  0.0269  -0.0251 171 ILE B CB  
2387 C CG1 . ILE B 154 ? 0.2548 0.2386 0.2549 0.0272  0.0100  -0.0346 171 ILE B CG1 
2388 C CG2 . ILE B 154 ? 0.2423 0.2671 0.2517 0.0388  0.0133  -0.0224 171 ILE B CG2 
2389 C CD1 . ILE B 154 ? 0.2690 0.2926 0.2627 -0.0213 0.0048  -0.0402 171 ILE B CD1 
2390 N N   . PHE B 155 ? 0.1851 0.2483 0.2339 0.0128  0.0163  0.0329  172 PHE B N   
2391 C CA  . PHE B 155 ? 0.2510 0.2389 0.2484 0.0451  0.0005  0.0077  172 PHE B CA  
2392 C C   . PHE B 155 ? 0.2543 0.3518 0.2733 0.0263  -0.0278 -0.0032 172 PHE B C   
2393 O O   . PHE B 155 ? 0.2642 0.3736 0.2763 0.0496  -0.0189 0.0138  172 PHE B O   
2394 C CB  . PHE B 155 ? 0.2485 0.2319 0.2350 -0.0037 0.0094  0.0048  172 PHE B CB  
2395 C CG  . PHE B 155 ? 0.2060 0.2332 0.2133 0.0493  -0.0063 -0.0042 172 PHE B CG  
2396 C CD1 . PHE B 155 ? 0.2032 0.2747 0.2147 0.0143  0.0057  -0.0359 172 PHE B CD1 
2397 C CD2 . PHE B 155 ? 0.2371 0.2881 0.2195 0.0418  -0.0209 0.0182  172 PHE B CD2 
2398 C CE1 . PHE B 155 ? 0.2309 0.3026 0.2148 0.0247  0.0109  -0.0113 172 PHE B CE1 
2399 C CE2 . PHE B 155 ? 0.3269 0.2937 0.2200 0.1059  -0.0343 -0.0177 172 PHE B CE2 
2400 C CZ  . PHE B 155 ? 0.2722 0.2807 0.2111 0.0567  -0.0115 -0.0297 172 PHE B CZ  
2401 N N   . GLU B 156 ? 0.2027 0.4606 0.2973 -0.0278 -0.0606 -0.0023 173 GLU B N   
2402 C CA  . GLU B 156 ? 0.2070 0.6741 0.3406 0.0525  -0.0645 0.0214  173 GLU B CA  
2403 C C   . GLU B 156 ? 0.2818 0.7659 0.3677 -0.0760 -0.0613 -0.0229 173 GLU B C   
2404 O O   . GLU B 156 ? 0.3187 0.8678 0.3759 -0.0767 -0.0603 -0.0370 173 GLU B O   
2405 C CB  . GLU B 156 ? 0.3507 0.6860 0.3599 0.1677  -0.0925 0.0602  173 GLU B CB  
2406 C CG  . GLU B 156 ? 0.3688 0.6352 0.3700 0.0831  -0.1026 0.0624  173 GLU B CG  
2407 C CD  . GLU B 156 ? 0.3501 0.4940 0.3710 -0.0396 -0.1354 -0.0015 173 GLU B CD  
2408 O OE1 . GLU B 156 ? 0.4076 0.5063 0.3817 -0.0302 -0.1262 0.0427  173 GLU B OE1 
2409 O OE2 . GLU B 156 ? 0.3304 0.3259 0.3746 -0.0383 -0.1307 -0.0231 173 GLU B OE2 
2410 O OXT . GLU B 156 ? 0.3671 0.8136 0.3831 -0.0424 -0.0484 -0.0360 173 GLU B OXT 
2411 N N   . HIS C 8   ? 0.6845 0.6319 0.3598 0.2307  0.0298  -0.0165 25  HIS C N   
2412 C CA  . HIS C 8   ? 0.6028 0.5545 0.3387 0.2734  0.0504  -0.0215 25  HIS C CA  
2413 C C   . HIS C 8   ? 0.4945 0.4831 0.3135 0.1997  0.0403  -0.0337 25  HIS C C   
2414 O O   . HIS C 8   ? 0.5946 0.5897 0.3136 0.2100  0.0513  -0.0604 25  HIS C O   
2415 C CB  . HIS C 8   ? 0.6239 0.6231 0.3381 0.2759  0.0549  -0.0401 25  HIS C CB  
2416 N N   . VAL C 9   ? 0.3832 0.3858 0.2860 0.1336  0.0310  0.0035  26  VAL C N   
2417 C CA  . VAL C 9   ? 0.3188 0.3716 0.2629 0.0870  0.0352  0.0021  26  VAL C CA  
2418 C C   . VAL C 9   ? 0.2589 0.3382 0.2476 0.0635  0.0488  -0.0092 26  VAL C C   
2419 O O   . VAL C 9   ? 0.2735 0.3695 0.2702 0.0548  0.0472  -0.0211 26  VAL C O   
2420 C CB  . VAL C 9   ? 0.2749 0.3632 0.2617 0.0290  -0.0001 0.0115  26  VAL C CB  
2421 C CG1 . VAL C 9   ? 0.2968 0.4130 0.2702 0.1124  -0.0284 0.0069  26  VAL C CG1 
2422 C CG2 . VAL C 9   ? 0.3332 0.3586 0.2670 0.0759  0.0120  0.0130  26  VAL C CG2 
2423 N N   . GLU C 10  ? 0.2197 0.2923 0.2115 0.0013  0.0333  -0.0256 27  GLU C N   
2424 C CA  . GLU C 10  ? 0.2416 0.3586 0.1952 0.0500  0.0530  0.0296  27  GLU C CA  
2425 C C   . GLU C 10  ? 0.1790 0.3270 0.1694 0.0532  0.0505  0.0390  27  GLU C C   
2426 O O   . GLU C 10  ? 0.1846 0.2785 0.1616 0.0444  0.0303  0.0506  27  GLU C O   
2427 C CB  . GLU C 10  ? 0.3581 0.3801 0.2019 0.0786  0.0068  0.0472  27  GLU C CB  
2428 C CG  . GLU C 10  ? 0.2769 0.3701 0.2072 0.0175  0.0279  0.0434  27  GLU C CG  
2429 C CD  . GLU C 10  ? 0.2715 0.4158 0.2087 0.0199  0.0778  0.0781  27  GLU C CD  
2430 O OE1 . GLU C 10  ? 0.3108 0.6848 0.2454 0.1466  0.0805  0.0805  27  GLU C OE1 
2431 O OE2 . GLU C 10  ? 0.2001 0.3818 0.1918 0.0210  0.0523  0.0443  27  GLU C OE2 
2432 N N   . GLN C 11  ? 0.2178 0.2975 0.1671 0.0512  0.0286  0.0223  28  GLN C N   
2433 C CA  . GLN C 11  ? 0.1573 0.3301 0.1694 0.0234  0.0154  0.0414  28  GLN C CA  
2434 C C   . GLN C 11  ? 0.1804 0.3301 0.1566 0.0540  0.0027  0.0463  28  GLN C C   
2435 O O   . GLN C 11  ? 0.2250 0.3385 0.1624 0.0616  0.0228  0.0427  28  GLN C O   
2436 C CB  . GLN C 11  ? 0.1597 0.3447 0.1833 0.0043  0.0269  0.0651  28  GLN C CB  
2437 C CG  . GLN C 11  ? 0.2095 0.3243 0.2054 0.0076  -0.0311 0.0325  28  GLN C CG  
2438 C CD  . GLN C 11  ? 0.2399 0.3844 0.2398 0.0267  -0.0303 0.0460  28  GLN C CD  
2439 O OE1 . GLN C 11  ? 0.3458 0.4071 0.2696 0.0346  -0.0393 0.0765  28  GLN C OE1 
2440 N NE2 . GLN C 11  ? 0.2906 0.4704 0.2279 0.1133  0.0192  0.0415  28  GLN C NE2 
2441 N N   . THR C 12  ? 0.1662 0.3260 0.1464 0.0673  0.0097  0.0223  29  THR C N   
2442 C CA  . THR C 12  ? 0.1715 0.3077 0.1534 0.0368  0.0229  0.0394  29  THR C CA  
2443 C C   . THR C 12  ? 0.1578 0.2978 0.1528 0.0145  0.0018  0.0485  29  THR C C   
2444 O O   . THR C 12  ? 0.1899 0.2717 0.1389 0.0433  0.0060  0.0364  29  THR C O   
2445 C CB  . THR C 12  ? 0.1492 0.3108 0.1621 0.0133  0.0292  0.0498  29  THR C CB  
2446 O OG1 . THR C 12  ? 0.1881 0.2978 0.1680 0.0223  -0.0022 0.0439  29  THR C OG1 
2447 C CG2 . THR C 12  ? 0.1585 0.2727 0.1778 0.0435  0.0373  0.0555  29  THR C CG2 
2448 N N   . TYR C 13  ? 0.1738 0.2387 0.1675 0.0319  0.0168  0.0280  30  TYR C N   
2449 C CA  . TYR C 13  ? 0.1467 0.2978 0.1559 0.0285  0.0264  0.0315  30  TYR C CA  
2450 C C   . TYR C 13  ? 0.2004 0.2946 0.1521 0.0230  0.0340  0.0463  30  TYR C C   
2451 O O   . TYR C 13  ? 0.1878 0.3069 0.1699 0.0307  0.0206  0.0238  30  TYR C O   
2452 C CB  . TYR C 13  ? 0.1927 0.3316 0.1578 0.0105  0.0204  0.0559  30  TYR C CB  
2453 C CG  . TYR C 13  ? 0.1729 0.3209 0.1574 0.0313  0.0438  0.0361  30  TYR C CG  
2454 C CD1 . TYR C 13  ? 0.1801 0.3146 0.1755 -0.0245 0.0288  0.0447  30  TYR C CD1 
2455 C CD2 . TYR C 13  ? 0.1557 0.2864 0.1536 -0.0060 0.0450  0.0362  30  TYR C CD2 
2456 C CE1 . TYR C 13  ? 0.2145 0.2900 0.1857 0.0191  -0.0008 0.0167  30  TYR C CE1 
2457 C CE2 . TYR C 13  ? 0.1980 0.2910 0.1701 0.0012  0.0314  0.0191  30  TYR C CE2 
2458 C CZ  . TYR C 13  ? 0.1959 0.2028 0.1854 -0.0377 0.0036  0.0039  30  TYR C CZ  
2459 O OH  . TYR C 13  ? 0.2792 0.2476 0.1985 0.0142  0.0224  -0.0170 30  TYR C OH  
2460 N N   . LEU C 14  ? 0.1589 0.2764 0.1472 0.0333  0.0169  0.0360  31  LEU C N   
2461 C CA  . LEU C 14  ? 0.1560 0.2761 0.1602 0.0273  -0.0015 0.0299  31  LEU C CA  
2462 C C   . LEU C 14  ? 0.1729 0.2470 0.1564 0.0130  0.0002  0.0139  31  LEU C C   
2463 O O   . LEU C 14  ? 0.1900 0.3130 0.1575 0.0586  -0.0178 -0.0212 31  LEU C O   
2464 C CB  . LEU C 14  ? 0.1780 0.2445 0.1739 -0.0012 -0.0087 0.0231  31  LEU C CB  
2465 C CG  . LEU C 14  ? 0.2056 0.2771 0.1979 -0.0201 -0.0114 0.0305  31  LEU C CG  
2466 C CD1 . LEU C 14  ? 0.2015 0.3514 0.1978 0.0140  -0.0441 0.0069  31  LEU C CD1 
2467 C CD2 . LEU C 14  ? 0.2505 0.2649 0.2161 -0.0200 0.0033  0.0550  31  LEU C CD2 
2468 N N   . MET C 15  ? 0.1976 0.2313 0.1521 -0.0002 -0.0140 0.0122  32  MET C N   
2469 C CA  . MET C 15  ? 0.1881 0.2472 0.1510 -0.0011 -0.0034 0.0109  32  MET C CA  
2470 C C   . MET C 15  ? 0.1476 0.2460 0.1435 -0.0361 0.0052  0.0044  32  MET C C   
2471 O O   . MET C 15  ? 0.1845 0.3311 0.1442 0.0381  0.0012  0.0104  32  MET C O   
2472 C CB  . MET C 15  ? 0.1989 0.2686 0.1779 -0.0132 0.0469  0.0256  32  MET C CB  
2473 C CG  . MET C 15  ? 0.1977 0.2751 0.2040 -0.0306 0.0690  0.0298  32  MET C CG  
2474 S SD  . MET C 15  ? 0.2731 0.2926 0.2200 0.0063  0.0428  0.0199  32  MET C SD  
2475 C CE  . MET C 15  ? 0.2718 0.3122 0.2187 0.0062  0.0397  0.0723  32  MET C CE  
2476 N N   . ILE C 16  ? 0.1818 0.2533 0.1455 0.0576  0.0257  0.0017  33  ILE C N   
2477 C CA  . ILE C 16  ? 0.1773 0.2438 0.1418 0.0354  0.0202  0.0044  33  ILE C CA  
2478 C C   . ILE C 16  ? 0.1972 0.2290 0.1465 0.0382  0.0084  -0.0047 33  ILE C C   
2479 O O   . ILE C 16  ? 0.2222 0.2248 0.1508 0.0132  0.0048  0.0044  33  ILE C O   
2480 C CB  . ILE C 16  ? 0.1705 0.2164 0.1540 0.0231  0.0180  0.0351  33  ILE C CB  
2481 C CG1 . ILE C 16  ? 0.2153 0.2763 0.1484 0.0242  0.0141  0.0358  33  ILE C CG1 
2482 C CG2 . ILE C 16  ? 0.1765 0.2459 0.1776 0.0435  0.0002  0.0196  33  ILE C CG2 
2483 C CD1 . ILE C 16  ? 0.2383 0.2731 0.1242 0.0429  0.0101  0.0073  33  ILE C CD1 
2484 N N   . LYS C 17  ? 0.1750 0.2111 0.1642 0.0309  0.0089  0.0115  34  LYS C N   
2485 C CA  . LYS C 17  ? 0.1932 0.2096 0.1583 0.0103  -0.0027 0.0266  34  LYS C CA  
2486 C C   . LYS C 17  ? 0.2097 0.1864 0.1579 -0.0248 0.0047  0.0133  34  LYS C C   
2487 O O   . LYS C 17  ? 0.1674 0.2254 0.1620 -0.0026 0.0061  0.0361  34  LYS C O   
2488 C CB  . LYS C 17  ? 0.1437 0.2627 0.1582 0.0422  -0.0025 0.0087  34  LYS C CB  
2489 C CG  . LYS C 17  ? 0.2169 0.2176 0.1596 -0.0110 0.0224  0.0561  34  LYS C CG  
2490 C CD  . LYS C 17  ? 0.1930 0.3330 0.1580 0.0057  0.0259  0.0559  34  LYS C CD  
2491 C CE  . LYS C 17  ? 0.1936 0.3067 0.1573 0.0398  0.0417  0.0733  34  LYS C CE  
2492 N NZ  . LYS C 17  ? 0.2319 0.3920 0.1637 -0.0109 -0.0062 0.0584  34  LYS C NZ  
2493 N N   . PRO C 18  ? 0.1822 0.2371 0.1612 -0.0097 0.0007  0.0278  35  PRO C N   
2494 C CA  . PRO C 18  ? 0.2061 0.2269 0.1587 -0.0120 0.0181  0.0318  35  PRO C CA  
2495 C C   . PRO C 18  ? 0.1608 0.2063 0.1555 -0.0239 0.0233  0.0241  35  PRO C C   
2496 O O   . PRO C 18  ? 0.2122 0.2210 0.1567 0.0370  0.0210  0.0299  35  PRO C O   
2497 C CB  . PRO C 18  ? 0.2442 0.2585 0.1574 0.0324  0.0045  0.0112  35  PRO C CB  
2498 C CG  . PRO C 18  ? 0.2234 0.2875 0.1636 0.0217  0.0162  -0.0098 35  PRO C CG  
2499 C CD  . PRO C 18  ? 0.2178 0.2533 0.1598 0.0250  0.0350  0.0193  35  PRO C CD  
2500 N N   . ASP C 19  ? 0.1751 0.2141 0.1613 0.0152  0.0012  0.0281  36  ASP C N   
2501 C CA  . ASP C 19  ? 0.1406 0.2465 0.1676 0.0127  0.0161  0.0278  36  ASP C CA  
2502 C C   . ASP C 19  ? 0.1432 0.2625 0.1583 -0.0196 0.0102  0.0143  36  ASP C C   
2503 O O   . ASP C 19  ? 0.1891 0.2442 0.1530 0.0270  0.0099  -0.0058 36  ASP C O   
2504 C CB  . ASP C 19  ? 0.1736 0.2382 0.1688 0.0317  -0.0067 -0.0018 36  ASP C CB  
2505 C CG  . ASP C 19  ? 0.1633 0.2517 0.1655 -0.0025 -0.0082 -0.0059 36  ASP C CG  
2506 O OD1 . ASP C 19  ? 0.1691 0.3253 0.1790 0.0113  0.0146  -0.0064 36  ASP C OD1 
2507 O OD2 . ASP C 19  ? 0.2062 0.2286 0.1479 0.0199  0.0038  0.0034  36  ASP C OD2 
2508 N N   . GLY C 20  ? 0.1716 0.2697 0.1489 -0.0044 0.0211  0.0028  37  GLY C N   
2509 C CA  . GLY C 20  ? 0.2251 0.2024 0.1563 0.0144  0.0214  0.0346  37  GLY C CA  
2510 C C   . GLY C 20  ? 0.2447 0.2211 0.1668 0.0642  0.0167  0.0043  37  GLY C C   
2511 O O   . GLY C 20  ? 0.1812 0.2405 0.1632 -0.0145 -0.0119 0.0038  37  GLY C O   
2512 N N   . ILE C 21  ? 0.1873 0.2138 0.1723 0.0138  0.0195  0.0000  38  ILE C N   
2513 C CA  . ILE C 21  ? 0.1779 0.2299 0.1634 0.0117  0.0031  -0.0051 38  ILE C CA  
2514 C C   . ILE C 21  ? 0.1310 0.2386 0.1600 0.0003  0.0083  0.0194  38  ILE C C   
2515 O O   . ILE C 21  ? 0.2171 0.2273 0.1558 0.0156  0.0288  0.0124  38  ILE C O   
2516 C CB  . ILE C 21  ? 0.1974 0.2355 0.1717 0.0000  0.0304  0.0125  38  ILE C CB  
2517 C CG1 . ILE C 21  ? 0.2574 0.2262 0.1948 0.0086  0.0230  0.0081  38  ILE C CG1 
2518 C CG2 . ILE C 21  ? 0.2008 0.2678 0.1671 0.0038  -0.0296 0.0134  38  ILE C CG2 
2519 C CD1 . ILE C 21  ? 0.2368 0.2917 0.2184 0.0121  0.0346  0.0440  38  ILE C CD1 
2520 N N   . GLN C 22  ? 0.1673 0.2162 0.1612 0.0371  -0.0072 0.0007  39  GLN C N   
2521 C CA  . GLN C 22  ? 0.2153 0.1889 0.1663 0.0337  -0.0056 -0.0040 39  GLN C CA  
2522 C C   . GLN C 22  ? 0.1779 0.1959 0.1634 -0.0184 -0.0261 -0.0078 39  GLN C C   
2523 O O   . GLN C 22  ? 0.2042 0.2202 0.1769 0.0275  0.0025  -0.0092 39  GLN C O   
2524 C CB  . GLN C 22  ? 0.2460 0.2060 0.1788 0.0240  0.0198  -0.0042 39  GLN C CB  
2525 C CG  . GLN C 22  ? 0.2737 0.1707 0.1865 -0.0217 0.0371  0.0012  39  GLN C CG  
2526 C CD  . GLN C 22  ? 0.3347 0.1793 0.1986 -0.0307 0.0611  0.0214  39  GLN C CD  
2527 O OE1 . GLN C 22  ? 0.3367 0.2143 0.2079 -0.0389 0.0551  0.0089  39  GLN C OE1 
2528 N NE2 . GLN C 22  ? 0.3321 0.2301 0.2050 -0.0044 0.0628  -0.0245 39  GLN C NE2 
2529 N N   . ARG C 23  ? 0.1759 0.2026 0.1471 -0.0040 -0.0135 -0.0219 40  ARG C N   
2530 C CA  . ARG C 23  ? 0.1789 0.2136 0.1593 -0.0013 -0.0067 0.0036  40  ARG C CA  
2531 C C   . ARG C 23  ? 0.1882 0.2434 0.1625 0.0191  0.0224  0.0113  40  ARG C C   
2532 O O   . ARG C 23  ? 0.2107 0.2476 0.1776 0.0137  0.0079  0.0272  40  ARG C O   
2533 C CB  . ARG C 23  ? 0.1853 0.2331 0.1555 0.0126  -0.0024 0.0117  40  ARG C CB  
2534 C CG  . ARG C 23  ? 0.1842 0.2108 0.1438 0.0223  0.0004  0.0086  40  ARG C CG  
2535 C CD  . ARG C 23  ? 0.2269 0.2496 0.1394 0.0004  0.0176  -0.0024 40  ARG C CD  
2536 N NE  . ARG C 23  ? 0.2366 0.2544 0.1524 -0.0068 -0.0074 -0.0282 40  ARG C NE  
2537 C CZ  . ARG C 23  ? 0.1873 0.2676 0.1513 -0.0079 -0.0035 0.0028  40  ARG C CZ  
2538 N NH1 . ARG C 23  ? 0.1783 0.2587 0.1513 -0.0169 0.0061  0.0182  40  ARG C NH1 
2539 N NH2 . ARG C 23  ? 0.2254 0.2741 0.1588 -0.0217 0.0237  0.0134  40  ARG C NH2 
2540 N N   . GLN C 24  ? 0.1900 0.2370 0.1636 0.0117  0.0136  0.0026  41  GLN C N   
2541 C CA  . GLN C 24  ? 0.2232 0.2403 0.1510 0.0608  0.0226  0.0026  41  GLN C CA  
2542 C C   . GLN C 24  ? 0.2002 0.2159 0.1530 0.0146  0.0272  0.0253  41  GLN C C   
2543 O O   . GLN C 24  ? 0.1949 0.2355 0.1590 -0.0067 0.0169  -0.0012 41  GLN C O   
2544 C CB  . GLN C 24  ? 0.2443 0.1684 0.1408 0.0114  -0.0007 -0.0169 41  GLN C CB  
2545 C CG  . GLN C 24  ? 0.2210 0.2053 0.1467 0.0225  0.0028  -0.0210 41  GLN C CG  
2546 C CD  . GLN C 24  ? 0.2714 0.2533 0.1587 0.0516  -0.0015 -0.0031 41  GLN C CD  
2547 O OE1 . GLN C 24  ? 0.2850 0.2871 0.1597 0.0377  0.0232  -0.0205 41  GLN C OE1 
2548 N NE2 . GLN C 24  ? 0.2524 0.2694 0.1690 0.0394  0.0027  0.0065  41  GLN C NE2 
2549 N N   . VAL C 25  ? 0.1775 0.2118 0.1441 0.0431  0.0137  0.0066  42  VAL C N   
2550 C CA  . VAL C 25  ? 0.1734 0.1932 0.1618 0.0312  -0.0148 0.0198  42  VAL C CA  
2551 C C   . VAL C 25  ? 0.1558 0.1995 0.1498 0.0105  0.0003  0.0107  42  VAL C C   
2552 O O   . VAL C 25  ? 0.2046 0.2239 0.1506 0.0270  0.0008  0.0042  42  VAL C O   
2553 C CB  . VAL C 25  ? 0.1535 0.2039 0.1930 0.0189  -0.0415 0.0094  42  VAL C CB  
2554 C CG1 . VAL C 25  ? 0.1647 0.2574 0.2166 0.0290  -0.0709 0.0111  42  VAL C CG1 
2555 C CG2 . VAL C 25  ? 0.1869 0.2287 0.1832 0.0171  -0.0412 0.0133  42  VAL C CG2 
2556 N N   . VAL C 26  ? 0.1614 0.2195 0.1500 -0.0247 0.0075  0.0064  43  VAL C N   
2557 C CA  . VAL C 26  ? 0.1588 0.2547 0.1528 0.0269  -0.0077 0.0109  43  VAL C CA  
2558 C C   . VAL C 26  ? 0.1799 0.2060 0.1409 0.0212  -0.0068 0.0127  43  VAL C C   
2559 O O   . VAL C 26  ? 0.1982 0.2103 0.1407 0.0324  -0.0158 -0.0215 43  VAL C O   
2560 C CB  . VAL C 26  ? 0.1425 0.2517 0.1505 0.0147  0.0042  0.0429  43  VAL C CB  
2561 C CG1 . VAL C 26  ? 0.1812 0.2406 0.1605 0.0112  0.0070  -0.0044 43  VAL C CG1 
2562 C CG2 . VAL C 26  ? 0.2017 0.2515 0.1477 -0.0120 -0.0280 0.0338  43  VAL C CG2 
2563 N N   . GLY C 27  ? 0.1796 0.1948 0.1467 0.0073  -0.0176 0.0108  44  GLY C N   
2564 C CA  . GLY C 27  ? 0.1866 0.1974 0.1482 0.0306  -0.0056 0.0233  44  GLY C CA  
2565 C C   . GLY C 27  ? 0.1646 0.2472 0.1490 0.0315  0.0054  0.0088  44  GLY C C   
2566 O O   . GLY C 27  ? 0.1830 0.2367 0.1469 0.0342  0.0124  0.0079  44  GLY C O   
2567 N N   . GLU C 28  ? 0.1525 0.2174 0.1572 0.0485  0.0004  0.0145  45  GLU C N   
2568 C CA  . GLU C 28  ? 0.1469 0.2535 0.1652 0.0327  0.0130  0.0092  45  GLU C CA  
2569 C C   . GLU C 28  ? 0.1411 0.1968 0.1494 -0.0036 0.0054  0.0105  45  GLU C C   
2570 O O   . GLU C 28  ? 0.2049 0.1819 0.1543 -0.0028 -0.0048 0.0003  45  GLU C O   
2571 C CB  . GLU C 28  ? 0.1741 0.2691 0.1958 0.0650  0.0170  0.0067  45  GLU C CB  
2572 C CG  . GLU C 28  ? 0.1391 0.3599 0.2303 0.0512  0.0070  0.0166  45  GLU C CG  
2573 C CD  . GLU C 28  ? 0.2262 0.6224 0.2769 0.0386  0.0470  0.0254  45  GLU C CD  
2574 O OE1 . GLU C 28  ? 0.2789 0.7438 0.2721 0.0936  0.0610  0.1207  45  GLU C OE1 
2575 O OE2 . GLU C 28  ? 0.3252 0.6417 0.3260 0.0623  0.0281  -0.0148 45  GLU C OE2 
2576 N N   . ILE C 29  ? 0.1279 0.2816 0.1472 0.0213  0.0068  0.0014  46  ILE C N   
2577 C CA  . ILE C 29  ? 0.1846 0.2146 0.1367 0.0107  0.0260  -0.0024 46  ILE C CA  
2578 C C   . ILE C 29  ? 0.1595 0.1841 0.1206 0.0304  0.0256  0.0053  46  ILE C C   
2579 O O   . ILE C 29  ? 0.2168 0.2135 0.1187 0.0434  0.0186  -0.0072 46  ILE C O   
2580 C CB  . ILE C 29  ? 0.1924 0.1978 0.1477 0.0190  0.0341  0.0051  46  ILE C CB  
2581 C CG1 . ILE C 29  ? 0.1990 0.2453 0.1630 0.0142  0.0006  0.0034  46  ILE C CG1 
2582 C CG2 . ILE C 29  ? 0.1984 0.2752 0.1415 -0.0189 0.0367  -0.0061 46  ILE C CG2 
2583 C CD1 . ILE C 29  ? 0.2129 0.2537 0.1781 0.0094  0.0204  0.0053  46  ILE C CD1 
2584 N N   . ILE C 30  ? 0.2113 0.2093 0.1247 0.0392  0.0188  0.0199  47  ILE C N   
2585 C CA  . ILE C 30  ? 0.1771 0.2165 0.1257 0.0424  0.0164  0.0157  47  ILE C CA  
2586 C C   . ILE C 30  ? 0.1714 0.2206 0.1296 0.0548  0.0248  -0.0029 47  ILE C C   
2587 O O   . ILE C 30  ? 0.1654 0.2160 0.1394 0.0330  0.0286  -0.0033 47  ILE C O   
2588 C CB  . ILE C 30  ? 0.1707 0.2113 0.1338 0.0296  0.0153  0.0127  47  ILE C CB  
2589 C CG1 . ILE C 30  ? 0.1771 0.2884 0.1340 0.0646  0.0242  0.0223  47  ILE C CG1 
2590 C CG2 . ILE C 30  ? 0.1895 0.2272 0.1310 0.0251  0.0016  0.0017  47  ILE C CG2 
2591 C CD1 . ILE C 30  ? 0.2096 0.2651 0.1488 0.0088  -0.0121 -0.0079 47  ILE C CD1 
2592 N N   . SER C 31  ? 0.1701 0.2298 0.1291 0.0357  0.0259  0.0093  48  SER C N   
2593 C CA  . SER C 31  ? 0.1983 0.1767 0.1266 0.0497  0.0210  0.0016  48  SER C CA  
2594 C C   . SER C 31  ? 0.2022 0.2367 0.1399 0.0786  -0.0025 -0.0006 48  SER C C   
2595 O O   . SER C 31  ? 0.1852 0.2603 0.1475 0.0635  0.0049  -0.0066 48  SER C O   
2596 C CB  . SER C 31  ? 0.1830 0.2084 0.1188 0.0510  0.0286  -0.0065 48  SER C CB  
2597 O OG  . SER C 31  ? 0.2038 0.2721 0.1135 0.0120  0.0314  0.0305  48  SER C OG  
2598 N N   . ARG C 32  ? 0.1500 0.2279 0.1515 0.0679  0.0045  0.0001  49  ARG C N   
2599 C CA  . ARG C 32  ? 0.1589 0.2239 0.1529 -0.0067 0.0090  0.0168  49  ARG C CA  
2600 C C   . ARG C 32  ? 0.1974 0.2085 0.1483 0.0140  0.0234  0.0202  49  ARG C C   
2601 O O   . ARG C 32  ? 0.2175 0.2035 0.1506 0.0249  0.0199  -0.0073 49  ARG C O   
2602 C CB  . ARG C 32  ? 0.1878 0.2167 0.1623 0.0311  0.0250  0.0085  49  ARG C CB  
2603 C CG  . ARG C 32  ? 0.1813 0.2540 0.1768 0.0333  0.0291  0.0106  49  ARG C CG  
2604 C CD  . ARG C 32  ? 0.2508 0.4147 0.1952 0.0951  0.0237  0.0294  49  ARG C CD  
2605 N NE  . ARG C 32  ? 0.2575 0.4222 0.2059 0.1088  0.0048  0.0397  49  ARG C NE  
2606 C CZ  . ARG C 32  ? 0.2115 0.3572 0.2009 0.0269  -0.0013 0.0577  49  ARG C CZ  
2607 N NH1 . ARG C 32  ? 0.2109 0.3350 0.1858 0.0187  0.0047  0.0701  49  ARG C NH1 
2608 N NH2 . ARG C 32  ? 0.2659 0.3327 0.2183 0.0876  0.0077  0.0675  49  ARG C NH2 
2609 N N   . PHE C 33  ? 0.1823 0.2059 0.1457 0.0115  0.0037  -0.0005 50  PHE C N   
2610 C CA  . PHE C 33  ? 0.1900 0.2131 0.1532 0.0656  0.0258  0.0183  50  PHE C CA  
2611 C C   . PHE C 33  ? 0.1805 0.2274 0.1461 0.0327  0.0126  0.0182  50  PHE C C   
2612 O O   . PHE C 33  ? 0.1479 0.2674 0.1566 0.0234  -0.0039 0.0223  50  PHE C O   
2613 C CB  . PHE C 33  ? 0.1949 0.2442 0.1582 0.0024  0.0298  0.0060  50  PHE C CB  
2614 C CG  . PHE C 33  ? 0.1953 0.2281 0.1503 -0.0111 0.0088  0.0062  50  PHE C CG  
2615 C CD1 . PHE C 33  ? 0.2234 0.2336 0.1502 0.0094  -0.0030 0.0189  50  PHE C CD1 
2616 C CD2 . PHE C 33  ? 0.2430 0.2704 0.1497 0.0349  0.0140  0.0321  50  PHE C CD2 
2617 C CE1 . PHE C 33  ? 0.2276 0.2587 0.1538 -0.0373 0.0004  0.0283  50  PHE C CE1 
2618 C CE2 . PHE C 33  ? 0.2544 0.2453 0.1503 0.0878  0.0332  0.0346  50  PHE C CE2 
2619 C CZ  . PHE C 33  ? 0.2077 0.2677 0.1535 0.0209  0.0075  0.0249  50  PHE C CZ  
2620 N N   . GLU C 34  ? 0.1615 0.2332 0.1392 0.0404  0.0243  -0.0046 51  GLU C N   
2621 C CA  . GLU C 34  ? 0.1897 0.2521 0.1448 0.0422  -0.0095 -0.0040 51  GLU C CA  
2622 C C   . GLU C 34  ? 0.1620 0.2736 0.1462 0.0839  -0.0136 0.0022  51  GLU C C   
2623 O O   . GLU C 34  ? 0.1784 0.2823 0.1509 0.0575  -0.0119 -0.0021 51  GLU C O   
2624 C CB  . GLU C 34  ? 0.1783 0.2439 0.1473 0.0434  -0.0069 -0.0228 51  GLU C CB  
2625 C CG  . GLU C 34  ? 0.1833 0.2719 0.1445 0.0602  -0.0099 -0.0170 51  GLU C CG  
2626 C CD  . GLU C 34  ? 0.1749 0.2521 0.1473 0.0255  0.0152  0.0038  51  GLU C CD  
2627 O OE1 . GLU C 34  ? 0.1740 0.2840 0.1441 0.0339  0.0073  0.0037  51  GLU C OE1 
2628 O OE2 . GLU C 34  ? 0.1946 0.2924 0.1616 0.0524  0.0068  0.0158  51  GLU C OE2 
2629 N N   . LYS C 35  ? 0.1977 0.2020 0.1497 0.0555  -0.0121 0.0153  52  LYS C N   
2630 C CA  . LYS C 35  ? 0.1847 0.2237 0.1587 0.0662  0.0294  0.0055  52  LYS C CA  
2631 C C   . LYS C 35  ? 0.2095 0.1890 0.1485 0.0928  0.0285  0.0670  52  LYS C C   
2632 O O   . LYS C 35  ? 0.2287 0.1993 0.1649 0.0441  0.0432  0.0304  52  LYS C O   
2633 C CB  . LYS C 35  ? 0.1754 0.2518 0.1724 0.0759  0.0232  -0.0105 52  LYS C CB  
2634 C CG  . LYS C 35  ? 0.1777 0.2820 0.1775 0.0631  0.0102  0.0198  52  LYS C CG  
2635 C CD  . LYS C 35  ? 0.4000 0.4486 0.2026 0.1820  0.0196  0.0011  52  LYS C CD  
2636 C CE  . LYS C 35  ? 0.5693 0.5033 0.2335 0.2432  0.0189  0.0701  52  LYS C CE  
2637 N NZ  . LYS C 35  ? 0.6895 0.6098 0.2491 0.2562  0.0406  0.0805  52  LYS C NZ  
2638 N N   . ARG C 36  ? 0.1892 0.2526 0.1324 0.0191  0.0151  0.0226  53  ARG C N   
2639 C CA  . ARG C 36  ? 0.1782 0.2992 0.1250 0.0396  0.0032  0.0082  53  ARG C CA  
2640 C C   . ARG C 36  ? 0.1927 0.2324 0.1237 0.0130  0.0050  -0.0100 53  ARG C C   
2641 O O   . ARG C 36  ? 0.2366 0.2706 0.1330 0.0833  0.0206  0.0191  53  ARG C O   
2642 C CB  . ARG C 36  ? 0.1929 0.2667 0.1260 0.0509  -0.0092 -0.0016 53  ARG C CB  
2643 C CG  . ARG C 36  ? 0.2178 0.2400 0.1323 0.0383  -0.0017 0.0117  53  ARG C CG  
2644 C CD  . ARG C 36  ? 0.2064 0.2708 0.1289 0.0257  -0.0114 0.0083  53  ARG C CD  
2645 N NE  . ARG C 36  ? 0.1996 0.2281 0.1238 0.0190  0.0039  0.0315  53  ARG C NE  
2646 C CZ  . ARG C 36  ? 0.1919 0.1909 0.1373 0.0556  0.0301  0.0455  53  ARG C CZ  
2647 N NH1 . ARG C 36  ? 0.2419 0.2243 0.1480 0.0584  0.0109  0.0621  53  ARG C NH1 
2648 N NH2 . ARG C 36  ? 0.2332 0.2629 0.1522 0.0567  0.0375  0.0288  53  ARG C NH2 
2649 N N   . GLY C 37  ? 0.2000 0.2109 0.1225 0.0478  0.0251  -0.0078 54  GLY C N   
2650 C CA  . GLY C 37  ? 0.2242 0.2025 0.1322 0.0745  0.0044  0.0135  54  GLY C CA  
2651 C C   . GLY C 37  ? 0.2327 0.1912 0.1426 0.0039  0.0109  0.0430  54  GLY C C   
2652 O O   . GLY C 37  ? 0.2162 0.3003 0.1625 0.0907  -0.0010 0.0250  54  GLY C O   
2653 N N   . TYR C 38  ? 0.2034 0.2221 0.1304 0.0156  0.0064  0.0392  55  TYR C N   
2654 C CA  . TYR C 38  ? 0.1541 0.2400 0.1266 0.0076  -0.0028 0.0340  55  TYR C CA  
2655 C C   . TYR C 38  ? 0.1616 0.2998 0.1230 0.0231  0.0187  -0.0032 55  TYR C C   
2656 O O   . TYR C 38  ? 0.1718 0.3151 0.1252 0.0121  0.0185  -0.0154 55  TYR C O   
2657 C CB  . TYR C 38  ? 0.2000 0.2644 0.1407 0.0279  -0.0007 0.0393  55  TYR C CB  
2658 C CG  . TYR C 38  ? 0.1959 0.2487 0.1414 0.0550  0.0104  0.0530  55  TYR C CG  
2659 C CD1 . TYR C 38  ? 0.1965 0.2718 0.1447 0.0502  -0.0021 0.0201  55  TYR C CD1 
2660 C CD2 . TYR C 38  ? 0.2101 0.2410 0.1431 0.0794  0.0054  0.0562  55  TYR C CD2 
2661 C CE1 . TYR C 38  ? 0.2080 0.2336 0.1423 0.0465  0.0110  0.0197  55  TYR C CE1 
2662 C CE2 . TYR C 38  ? 0.1630 0.2605 0.1376 0.0277  0.0183  0.0335  55  TYR C CE2 
2663 C CZ  . TYR C 38  ? 0.1782 0.2409 0.1410 0.0482  0.0085  0.0432  55  TYR C CZ  
2664 O OH  . TYR C 38  ? 0.2181 0.3108 0.1467 0.0619  0.0306  0.0399  55  TYR C OH  
2665 N N   . ARG C 39  ? 0.1621 0.2755 0.1176 0.0146  -0.0012 0.0098  56  ARG C N   
2666 C CA  . ARG C 39  ? 0.1622 0.2506 0.1269 0.0028  0.0092  0.0176  56  ARG C CA  
2667 C C   . ARG C 39  ? 0.1655 0.2228 0.1397 0.0396  0.0283  0.0441  56  ARG C C   
2668 O O   . ARG C 39  ? 0.1988 0.2505 0.1466 0.0340  0.0241  0.0436  56  ARG C O   
2669 C CB  . ARG C 39  ? 0.1740 0.2885 0.1259 0.0361  0.0018  0.0386  56  ARG C CB  
2670 C CG  . ARG C 39  ? 0.1664 0.3461 0.1381 0.0542  -0.0092 0.0086  56  ARG C CG  
2671 C CD  . ARG C 39  ? 0.1627 0.2830 0.1453 0.0184  0.0128  0.0249  56  ARG C CD  
2672 N NE  . ARG C 39  ? 0.1589 0.2838 0.1500 0.0270  0.0043  0.0366  56  ARG C NE  
2673 C CZ  . ARG C 39  ? 0.1754 0.2780 0.1508 0.0265  0.0204  0.0531  56  ARG C CZ  
2674 N NH1 . ARG C 39  ? 0.2193 0.3004 0.1615 0.0331  -0.0192 -0.0019 56  ARG C NH1 
2675 N NH2 . ARG C 39  ? 0.2579 0.3429 0.1672 0.0618  0.0560  0.0652  56  ARG C NH2 
2676 N N   . ILE C 40  ? 0.1836 0.2447 0.1449 0.0442  0.0175  -0.0021 57  ILE C N   
2677 C CA  . ILE C 40  ? 0.1383 0.2267 0.1540 0.0380  0.0183  0.0157  57  ILE C CA  
2678 C C   . ILE C 40  ? 0.1421 0.2150 0.1629 0.0374  0.0123  0.0235  57  ILE C C   
2679 O O   . ILE C 40  ? 0.1619 0.2716 0.1675 0.0367  -0.0022 0.0225  57  ILE C O   
2680 C CB  . ILE C 40  ? 0.1536 0.2600 0.1550 0.0498  0.0162  0.0177  57  ILE C CB  
2681 C CG1 . ILE C 40  ? 0.1569 0.2862 0.1667 0.0159  0.0354  0.0020  57  ILE C CG1 
2682 C CG2 . ILE C 40  ? 0.2263 0.2742 0.1557 0.0662  0.0106  0.0140  57  ILE C CG2 
2683 C CD1 . ILE C 40  ? 0.2307 0.2568 0.1749 0.0342  0.0455  0.0160  57  ILE C CD1 
2684 N N   . ALA C 41  ? 0.1680 0.2501 0.1655 0.0226  0.0165  0.0490  58  ALA C N   
2685 C CA  . ALA C 41  ? 0.1376 0.2853 0.1675 0.0155  0.0079  0.0280  58  ALA C CA  
2686 C C   . ALA C 41  ? 0.1310 0.3082 0.1769 0.0220  -0.0052 0.0349  58  ALA C C   
2687 O O   . ALA C 41  ? 0.1377 0.3611 0.1989 0.0540  -0.0002 0.0071  58  ALA C O   
2688 C CB  . ALA C 41  ? 0.1857 0.3994 0.1558 0.0526  0.0169  0.0286  58  ALA C CB  
2689 N N   . ALA C 42  ? 0.1342 0.3386 0.1728 0.0290  0.0086  0.0350  59  ALA C N   
2690 C CA  . ALA C 42  ? 0.1688 0.2774 0.1589 0.0081  0.0082  0.0246  59  ALA C CA  
2691 C C   . ALA C 42  ? 0.1428 0.2924 0.1643 -0.0190 0.0166  0.0136  59  ALA C C   
2692 O O   . ALA C 42  ? 0.1675 0.2697 0.1706 0.0095  0.0111  0.0149  59  ALA C O   
2693 C CB  . ALA C 42  ? 0.1604 0.3014 0.1505 0.0278  -0.0049 0.0307  59  ALA C CB  
2694 N N   . MET C 43  ? 0.1931 0.2639 0.1667 0.0078  0.0166  0.0241  60  MET C N   
2695 C CA  . MET C 43  ? 0.1396 0.3329 0.1695 -0.0035 0.0151  0.0100  60  MET C CA  
2696 C C   . MET C 43  ? 0.1518 0.2843 0.1813 0.0329  0.0034  -0.0100 60  MET C C   
2697 O O   . MET C 43  ? 0.2189 0.3790 0.1904 0.0478  -0.0394 -0.0011 60  MET C O   
2698 C CB  . MET C 43  ? 0.1670 0.3762 0.1611 0.0471  0.0105  0.0349  60  MET C CB  
2699 C CG  . MET C 43  ? 0.1953 0.3690 0.1804 0.0471  0.0193  0.0285  60  MET C CG  
2700 S SD  . MET C 43  ? 0.1943 0.3934 0.1884 0.0097  0.0200  0.0482  60  MET C SD  
2701 C CE  . MET C 43  ? 0.1943 0.3838 0.1757 0.0152  -0.0263 0.0111  60  MET C CE  
2702 N N   . LYS C 44  ? 0.2077 0.2306 0.1937 0.0625  -0.0011 0.0006  61  LYS C N   
2703 C CA  . LYS C 44  ? 0.2292 0.2882 0.2192 0.0729  0.0280  -0.0203 61  LYS C CA  
2704 C C   . LYS C 44  ? 0.1946 0.2759 0.1952 0.0240  0.0142  -0.0404 61  LYS C C   
2705 O O   . LYS C 44  ? 0.2412 0.3430 0.2013 0.0284  -0.0224 -0.0513 61  LYS C O   
2706 C CB  . LYS C 44  ? 0.2028 0.3632 0.2793 0.0209  0.0184  -0.0608 61  LYS C CB  
2707 C CG  . LYS C 44  ? 0.3036 0.5501 0.2987 0.0890  0.0503  -0.0073 61  LYS C CG  
2708 C CD  . LYS C 44  ? 0.3764 0.5119 0.2967 0.0243  0.0899  0.0418  61  LYS C CD  
2709 C CE  . LYS C 44  ? 0.3532 0.3889 0.2997 0.0098  0.0975  0.0005  61  LYS C CE  
2710 N NZ  . LYS C 44  ? 0.3890 0.3219 0.3021 0.0443  0.0753  -0.0016 61  LYS C NZ  
2711 N N   . LEU C 45  ? 0.1551 0.3186 0.1941 0.0051  0.0334  -0.0202 62  LEU C N   
2712 C CA  . LEU C 45  ? 0.1425 0.3060 0.1955 0.0033  0.0179  -0.0259 62  LEU C CA  
2713 C C   . LEU C 45  ? 0.2162 0.2718 0.2033 0.0201  -0.0065 0.0179  62  LEU C C   
2714 O O   . LEU C 45  ? 0.2438 0.2718 0.2097 0.0014  -0.0310 0.0115  62  LEU C O   
2715 C CB  . LEU C 45  ? 0.1960 0.2969 0.1976 0.1135  0.0440  0.0080  62  LEU C CB  
2716 C CG  . LEU C 45  ? 0.1975 0.2949 0.2133 -0.0144 0.0496  0.0307  62  LEU C CG  
2717 C CD1 . LEU C 45  ? 0.1588 0.4267 0.2282 -0.0123 0.0182  0.0032  62  LEU C CD1 
2718 C CD2 . LEU C 45  ? 0.3079 0.3722 0.2228 0.1164  0.0876  0.0289  62  LEU C CD2 
2719 N N   . THR C 46  ? 0.2156 0.2811 0.2202 -0.0205 -0.0048 0.0112  63  THR C N   
2720 C CA  . THR C 46  ? 0.2213 0.2896 0.2380 0.0159  -0.0013 0.0026  63  THR C CA  
2721 C C   . THR C 46  ? 0.1868 0.2158 0.2494 -0.0736 -0.0060 0.0088  63  THR C C   
2722 O O   . THR C 46  ? 0.2109 0.2615 0.2638 -0.0244 -0.0121 0.0036  63  THR C O   
2723 C CB  . THR C 46  ? 0.2633 0.3197 0.2550 0.0061  0.0129  0.0376  63  THR C CB  
2724 O OG1 . THR C 46  ? 0.2452 0.3177 0.2681 -0.0207 0.0018  0.0502  63  THR C OG1 
2725 C CG2 . THR C 46  ? 0.2126 0.3305 0.2585 -0.0637 0.0265  0.0164  63  THR C CG2 
2726 N N   . ILE C 47  ? 0.2144 0.2532 0.2545 -0.0440 -0.0069 0.0190  64  ILE C N   
2727 C CA  . ILE C 47  ? 0.2261 0.2656 0.2427 -0.0226 -0.0097 0.0249  64  ILE C CA  
2728 C C   . ILE C 47  ? 0.2181 0.2649 0.2477 -0.0468 0.0091  0.0332  64  ILE C C   
2729 O O   . ILE C 47  ? 0.2285 0.3381 0.2623 -0.0426 0.0183  0.0537  64  ILE C O   
2730 C CB  . ILE C 47  ? 0.2602 0.2753 0.2379 0.0034  0.0109  0.0312  64  ILE C CB  
2731 C CG1 . ILE C 47  ? 0.3554 0.2977 0.2247 0.0601  0.0066  0.0068  64  ILE C CG1 
2732 C CG2 . ILE C 47  ? 0.3145 0.2470 0.2372 -0.0685 0.0115  0.0313  64  ILE C CG2 
2733 C CD1 . ILE C 47  ? 0.4285 0.4681 0.2402 0.1083  0.0008  0.0076  64  ILE C CD1 
2734 N N   . ALA C 48  ? 0.1852 0.3034 0.2344 -0.0233 0.0129  0.0214  65  ALA C N   
2735 C CA  . ALA C 48  ? 0.2825 0.2591 0.2405 -0.0275 0.0640  0.0671  65  ALA C CA  
2736 C C   . ALA C 48  ? 0.3683 0.2552 0.2474 -0.0462 0.0814  0.0501  65  ALA C C   
2737 O O   . ALA C 48  ? 0.4456 0.3471 0.2509 0.0519  0.0533  0.0512  65  ALA C O   
2738 C CB  . ALA C 48  ? 0.3290 0.3269 0.2416 0.0387  0.0676  0.0402  65  ALA C CB  
2739 N N   . THR C 49  ? 0.4047 0.2598 0.2567 -0.0572 0.0949  0.0195  66  THR C N   
2740 C CA  . THR C 49  ? 0.4559 0.3282 0.2564 -0.0224 0.0820  0.0052  66  THR C CA  
2741 C C   . THR C 49  ? 0.4545 0.2011 0.2722 -0.0705 0.0542  -0.0075 66  THR C C   
2742 O O   . THR C 49  ? 0.4092 0.2478 0.2728 -0.0467 0.0342  -0.0246 66  THR C O   
2743 C CB  . THR C 49  ? 0.4775 0.3727 0.2491 -0.0607 0.0810  -0.0061 66  THR C CB  
2744 O OG1 . THR C 49  ? 0.3881 0.4570 0.2632 -0.1746 0.0564  -0.0128 66  THR C OG1 
2745 C CG2 . THR C 49  ? 0.5501 0.4344 0.2398 0.0098  0.0934  0.0219  66  THR C CG2 
2746 N N   . PRO C 50  ? 0.5227 0.2968 0.2938 0.0011  0.0844  0.0162  67  PRO C N   
2747 C CA  . PRO C 50  ? 0.5220 0.2565 0.3045 -0.0606 0.0948  0.0070  67  PRO C CA  
2748 C C   . PRO C 50  ? 0.5067 0.2969 0.3097 -0.0148 0.0876  0.0195  67  PRO C C   
2749 O O   . PRO C 50  ? 0.5107 0.2717 0.3074 -0.0612 0.0749  0.0323  67  PRO C O   
2750 C CB  . PRO C 50  ? 0.5744 0.1998 0.3082 -0.0381 0.0916  -0.0068 67  PRO C CB  
2751 C CG  . PRO C 50  ? 0.6353 0.2792 0.3063 0.0427  0.0835  -0.0110 67  PRO C CG  
2752 C CD  . PRO C 50  ? 0.6011 0.2612 0.2974 0.0060  0.0902  0.0014  67  PRO C CD  
2753 N N   . ALA C 51  ? 0.4768 0.3301 0.3133 -0.0269 0.0721  0.0228  68  ALA C N   
2754 C CA  . ALA C 51  ? 0.4051 0.3615 0.3175 -0.1527 0.0487  -0.0017 68  ALA C CA  
2755 C C   . ALA C 51  ? 0.3811 0.2969 0.3002 -0.1061 0.0526  0.0227  68  ALA C C   
2756 O O   . ALA C 51  ? 0.4818 0.3553 0.3043 -0.0130 0.0662  0.0256  68  ALA C O   
2757 C CB  . ALA C 51  ? 0.4420 0.4498 0.3294 -0.2082 0.0256  -0.0131 68  ALA C CB  
2758 N N   . ILE C 52  ? 0.3231 0.3543 0.2823 -0.0600 0.0067  0.0019  69  ILE C N   
2759 C CA  . ILE C 52  ? 0.2966 0.3323 0.2735 -0.0403 0.0150  0.0242  69  ILE C CA  
2760 C C   . ILE C 52  ? 0.2928 0.2309 0.2619 -0.0448 0.0045  0.0250  69  ILE C C   
2761 O O   . ILE C 52  ? 0.2914 0.2570 0.2428 -0.0079 0.0003  0.0082  69  ILE C O   
2762 C CB  . ILE C 52  ? 0.3082 0.3881 0.2754 -0.0062 0.0484  0.0304  69  ILE C CB  
2763 C CG1 . ILE C 52  ? 0.4293 0.5021 0.2803 0.0886  0.0302  0.0460  69  ILE C CG1 
2764 C CG2 . ILE C 52  ? 0.3848 0.3501 0.2795 0.0652  0.0355  0.0230  69  ILE C CG2 
2765 C CD1 . ILE C 52  ? 0.4950 0.6294 0.2905 0.1056  0.0161  0.0479  69  ILE C CD1 
2766 N N   . LEU C 53  ? 0.2466 0.2697 0.2616 -0.0228 0.0369  0.0201  70  LEU C N   
2767 C CA  . LEU C 53  ? 0.2136 0.2762 0.2612 -0.0343 0.0387  0.0269  70  LEU C CA  
2768 C C   . LEU C 53  ? 0.2654 0.2650 0.2713 0.0098  0.0260  -0.0033 70  LEU C C   
2769 O O   . LEU C 53  ? 0.2647 0.2700 0.2726 -0.0102 0.0082  0.0182  70  LEU C O   
2770 C CB  . LEU C 53  ? 0.2409 0.2692 0.2536 0.0031  0.0326  0.0411  70  LEU C CB  
2771 C CG  . LEU C 53  ? 0.2732 0.2149 0.2496 0.0052  0.0190  0.0270  70  LEU C CG  
2772 C CD1 . LEU C 53  ? 0.2347 0.2767 0.2430 0.0541  0.0131  0.0363  70  LEU C CD1 
2773 C CD2 . LEU C 53  ? 0.2954 0.2668 0.2514 0.0206  -0.0066 0.0157  70  LEU C CD2 
2774 N N   . GLU C 54  ? 0.2962 0.2723 0.2827 -0.0062 0.0625  0.0017  71  GLU C N   
2775 C CA  . GLU C 54  ? 0.3825 0.2695 0.3038 -0.0080 0.0689  0.0218  71  GLU C CA  
2776 C C   . GLU C 54  ? 0.3399 0.2859 0.2907 -0.0079 0.0479  0.0057  71  GLU C C   
2777 O O   . GLU C 54  ? 0.3666 0.3057 0.2877 0.0460  0.0532  0.0015  71  GLU C O   
2778 C CB  . GLU C 54  ? 0.5507 0.3272 0.3413 0.0927  0.1114  0.0129  71  GLU C CB  
2779 C CG  . GLU C 54  ? 0.7859 0.4345 0.3783 0.0837  0.1379  0.0230  71  GLU C CG  
2780 C CD  . GLU C 54  ? 0.9541 0.4940 0.4101 0.0565  0.1596  -0.0007 71  GLU C CD  
2781 O OE1 . GLU C 54  ? 0.9942 0.4006 0.4229 -0.0569 0.1674  0.0189  71  GLU C OE1 
2782 O OE2 . GLU C 54  ? 1.0455 0.6308 0.4221 0.1085  0.1472  -0.0355 71  GLU C OE2 
2783 N N   . GLU C 55  ? 0.2879 0.2866 0.2789 -0.0263 0.0318  0.0196  72  GLU C N   
2784 C CA  A GLU C 55  ? 0.2319 0.3327 0.2781 -0.0261 0.0371  0.0044  72  GLU C CA  
2785 C CA  B GLU C 55  ? 0.2608 0.3154 0.2746 -0.0035 0.0291  0.0094  72  GLU C CA  
2786 C C   . GLU C 55  ? 0.2249 0.3322 0.2645 -0.0090 0.0367  -0.0022 72  GLU C C   
2787 O O   . GLU C 55  ? 0.2833 0.3217 0.2554 0.0292  0.0439  -0.0311 72  GLU C O   
2788 C CB  A GLU C 55  ? 0.2570 0.4411 0.2954 -0.0580 0.0375  -0.0223 72  GLU C CB  
2789 C CB  B GLU C 55  ? 0.3199 0.3765 0.2840 -0.0091 0.0167  -0.0021 72  GLU C CB  
2790 C CG  A GLU C 55  ? 0.2636 0.5577 0.3104 -0.0336 0.0498  -0.0338 72  GLU C CG  
2791 C CG  B GLU C 55  ? 0.3706 0.4674 0.2939 0.0050  0.0072  -0.0075 72  GLU C CG  
2792 C CD  A GLU C 55  ? 0.2888 0.5669 0.3202 -0.1143 0.0507  -0.0548 72  GLU C CD  
2793 C CD  B GLU C 55  ? 0.3768 0.5579 0.3056 0.0349  -0.0001 -0.0297 72  GLU C CD  
2794 O OE1 A GLU C 55  ? 0.3379 0.5918 0.3183 -0.1326 0.0520  -0.0544 72  GLU C OE1 
2795 O OE1 B GLU C 55  ? 0.3876 0.5746 0.3116 0.0271  -0.0255 -0.0298 72  GLU C OE1 
2796 O OE2 A GLU C 55  ? 0.2977 0.5494 0.3308 -0.0585 0.0560  -0.0499 72  GLU C OE2 
2797 O OE2 B GLU C 55  ? 0.3719 0.5282 0.3050 -0.0230 -0.0098 -0.0468 72  GLU C OE2 
2798 N N   . HIS C 56  ? 0.2879 0.2124 0.2439 0.0017  0.0428  0.0197  73  HIS C N   
2799 C CA  . HIS C 56  ? 0.2803 0.2379 0.2379 0.0131  0.0339  0.0320  73  HIS C CA  
2800 C C   . HIS C 56  ? 0.2717 0.2821 0.2350 -0.0048 0.0241  0.0183  73  HIS C C   
2801 O O   . HIS C 56  ? 0.2930 0.2797 0.2392 0.0132  0.0289  0.0054  73  HIS C O   
2802 C CB  . HIS C 56  ? 0.1945 0.2614 0.2368 0.0066  0.0531  0.0512  73  HIS C CB  
2803 C CG  . HIS C 56  ? 0.2362 0.3133 0.2417 0.0056  -0.0101 0.0641  73  HIS C CG  
2804 N ND1 . HIS C 56  ? 0.2481 0.3043 0.2413 -0.0182 -0.0183 0.0530  73  HIS C ND1 
2805 C CD2 . HIS C 56  ? 0.2830 0.3329 0.2533 -0.0344 -0.0438 0.0918  73  HIS C CD2 
2806 C CE1 . HIS C 56  ? 0.2860 0.2878 0.2496 -0.0382 -0.0369 0.0606  73  HIS C CE1 
2807 N NE2 . HIS C 56  ? 0.3045 0.3204 0.2576 -0.0820 -0.0481 0.0901  73  HIS C NE2 
2808 N N   . TYR C 57  ? 0.2342 0.2596 0.2332 -0.0106 0.0261  0.0353  74  TYR C N   
2809 C CA  . TYR C 57  ? 0.2245 0.3187 0.2326 0.0260  0.0104  0.0448  74  TYR C CA  
2810 C C   . TYR C 57  ? 0.3212 0.2804 0.2413 0.0392  0.0541  0.0635  74  TYR C C   
2811 O O   . TYR C 57  ? 0.3470 0.3156 0.2384 0.0462  0.0481  0.0529  74  TYR C O   
2812 C CB  . TYR C 57  ? 0.2711 0.3520 0.2463 0.0579  -0.0233 0.0464  74  TYR C CB  
2813 C CG  . TYR C 57  ? 0.2409 0.3424 0.2531 0.0356  -0.0062 0.0428  74  TYR C CG  
2814 C CD1 . TYR C 57  ? 0.2664 0.3357 0.2574 -0.0488 -0.0241 0.0520  74  TYR C CD1 
2815 C CD2 . TYR C 57  ? 0.2637 0.3889 0.2628 0.0249  0.0370  0.0513  74  TYR C CD2 
2816 C CE1 . TYR C 57  ? 0.3099 0.4198 0.2619 -0.0157 -0.0083 0.0608  74  TYR C CE1 
2817 C CE2 . TYR C 57  ? 0.3015 0.4512 0.2717 0.0410  0.0441  0.0609  74  TYR C CE2 
2818 C CZ  . TYR C 57  ? 0.3162 0.4006 0.2760 -0.0672 0.0404  0.0725  74  TYR C CZ  
2819 O OH  . TYR C 57  ? 0.4034 0.4900 0.2940 -0.0544 0.0617  0.0844  74  TYR C OH  
2820 N N   . ALA C 58  ? 0.3024 0.2831 0.2486 0.0381  0.0718  0.0486  75  ALA C N   
2821 C CA  . ALA C 58  ? 0.3158 0.3115 0.2566 -0.0127 0.0676  0.0455  75  ALA C CA  
2822 C C   . ALA C 58  ? 0.3615 0.3883 0.2618 0.0373  0.0700  0.0449  75  ALA C C   
2823 O O   . ALA C 58  ? 0.4562 0.3805 0.2590 0.0432  0.0861  0.0599  75  ALA C O   
2824 C CB  . ALA C 58  ? 0.3573 0.3783 0.2598 0.0394  0.0779  0.0483  75  ALA C CB  
2825 N N   . GLU C 59  ? 0.3870 0.3669 0.2747 -0.0073 0.0450  0.0261  76  GLU C N   
2826 C CA  . GLU C 59  ? 0.5259 0.3693 0.2950 0.0136  0.0328  0.0414  76  GLU C CA  
2827 C C   . GLU C 59  ? 0.4960 0.4685 0.2997 -0.0043 0.0261  0.0986  76  GLU C C   
2828 O O   . GLU C 59  ? 0.5526 0.6318 0.2872 0.0238  0.0175  0.0864  76  GLU C O   
2829 C CB  . GLU C 59  ? 0.6704 0.4005 0.3178 0.0055  0.0334  0.0228  76  GLU C CB  
2830 C CG  . GLU C 59  ? 0.7845 0.4756 0.3474 0.0777  0.0330  0.0067  76  GLU C CG  
2831 C CD  . GLU C 59  ? 0.9152 0.5199 0.3639 0.1473  0.0344  0.0066  76  GLU C CD  
2832 O OE1 . GLU C 59  ? 0.9089 0.4448 0.3784 0.0891  0.0270  -0.0090 76  GLU C OE1 
2833 O OE2 . GLU C 59  ? 1.0087 0.5647 0.3677 0.1792  0.0405  0.0326  76  GLU C OE2 
2834 N N   . HIS C 60  ? 0.4143 0.4409 0.3172 -0.0003 0.0353  0.1356  77  HIS C N   
2835 C CA  . HIS C 60  ? 0.3718 0.4635 0.3427 -0.0337 0.0225  0.1461  77  HIS C CA  
2836 C C   . HIS C 60  ? 0.3924 0.4901 0.3700 -0.0136 0.0417  0.2068  77  HIS C C   
2837 O O   . HIS C 60  ? 0.3976 0.4845 0.3740 0.0266  0.0392  0.2215  77  HIS C O   
2838 C CB  . HIS C 60  ? 0.3870 0.4567 0.3530 -0.0497 0.0070  0.1071  77  HIS C CB  
2839 C CG  . HIS C 60  ? 0.4043 0.4119 0.3571 -0.0840 -0.0196 0.0951  77  HIS C CG  
2840 N ND1 . HIS C 60  ? 0.4535 0.4427 0.3581 -0.0270 -0.0399 0.0898  77  HIS C ND1 
2841 C CD2 . HIS C 60  ? 0.4388 0.3939 0.3629 -0.0627 -0.0398 0.0897  77  HIS C CD2 
2842 C CE1 . HIS C 60  ? 0.5027 0.4609 0.3641 -0.0342 -0.0547 0.0699  77  HIS C CE1 
2843 N NE2 . HIS C 60  ? 0.5217 0.4758 0.3679 -0.0166 -0.0479 0.0802  77  HIS C NE2 
2844 N N   . LYS C 61  ? 0.4118 0.5163 0.4004 -0.0231 0.0602  0.2316  78  LYS C N   
2845 C CA  . LYS C 61  ? 0.4972 0.5820 0.4396 -0.0762 0.0667  0.2362  78  LYS C CA  
2846 C C   . LYS C 61  ? 0.4668 0.7014 0.4487 -0.0145 0.0654  0.2562  78  LYS C C   
2847 O O   . LYS C 61  ? 0.4870 0.7418 0.4451 -0.0028 0.0785  0.3052  78  LYS C O   
2848 C CB  . LYS C 61  ? 0.6172 0.6887 0.4690 -0.0586 0.0526  0.2083  78  LYS C CB  
2849 C CG  . LYS C 61  ? 0.7342 0.7905 0.4888 -0.0486 0.0533  0.2191  78  LYS C CG  
2850 C CD  . LYS C 61  ? 0.8534 0.8533 0.5060 -0.0392 0.0498  0.2158  78  LYS C CD  
2851 C CE  . LYS C 61  ? 0.9446 0.9216 0.5174 -0.0352 0.0498  0.2106  78  LYS C CE  
2852 N NZ  . LYS C 61  ? 0.9934 0.9148 0.5229 -0.0549 0.0535  0.2186  78  LYS C NZ  
2853 N N   . GLY C 62  ? 0.4558 0.7011 0.4570 -0.0118 0.0735  0.2658  79  GLY C N   
2854 C CA  . GLY C 62  ? 0.4538 0.6577 0.4518 -0.0191 0.0797  0.2854  79  GLY C CA  
2855 C C   . GLY C 62  ? 0.5255 0.6099 0.4461 0.0183  0.0650  0.2755  79  GLY C C   
2856 O O   . GLY C 62  ? 0.5932 0.6620 0.4542 0.1041  0.0789  0.2924  79  GLY C O   
2857 N N   . LYS C 63  ? 0.4760 0.5431 0.4290 -0.0390 0.0584  0.2618  80  LYS C N   
2858 C CA  . LYS C 63  ? 0.4709 0.5737 0.4168 0.0064  -0.0015 0.2048  80  LYS C CA  
2859 C C   . LYS C 63  ? 0.3610 0.5346 0.4068 -0.0242 -0.0005 0.2114  80  LYS C C   
2860 O O   . LYS C 63  ? 0.3146 0.4742 0.4109 -0.0171 0.0054  0.2241  80  LYS C O   
2861 C CB  . LYS C 63  ? 0.5615 0.6151 0.4177 0.0662  -0.0400 0.1700  80  LYS C CB  
2862 C CG  . LYS C 63  ? 0.6846 0.6751 0.4220 0.1312  -0.0616 0.1413  80  LYS C CG  
2863 C CD  . LYS C 63  ? 0.7892 0.7271 0.4223 0.2506  -0.0809 0.1216  80  LYS C CD  
2864 C CE  . LYS C 63  ? 0.8753 0.7353 0.4248 0.3002  -0.0936 0.0975  80  LYS C CE  
2865 N NZ  . LYS C 63  ? 0.9015 0.6942 0.4253 0.2718  -0.0983 0.0766  80  LYS C NZ  
2866 N N   . PRO C 64  ? 0.3957 0.5149 0.3964 0.0424  -0.0307 0.2139  81  PRO C N   
2867 C CA  . PRO C 64  ? 0.3284 0.4985 0.3896 0.0153  -0.0264 0.2267  81  PRO C CA  
2868 C C   . PRO C 64  ? 0.3414 0.5297 0.3893 0.0106  0.0001  0.2554  81  PRO C C   
2869 O O   . PRO C 64  ? 0.3645 0.5853 0.3939 0.0343  0.0091  0.2736  81  PRO C O   
2870 C CB  . PRO C 64  ? 0.3163 0.5285 0.3945 -0.0232 -0.0511 0.1761  81  PRO C CB  
2871 C CG  . PRO C 64  ? 0.3476 0.5796 0.3982 0.0824  -0.0544 0.1723  81  PRO C CG  
2872 C CD  . PRO C 64  ? 0.3662 0.5844 0.3960 0.0890  -0.0616 0.1850  81  PRO C CD  
2873 N N   . PHE C 65  ? 0.3145 0.5486 0.3867 -0.0032 0.0089  0.2629  82  PHE C N   
2874 C CA  . PHE C 65  ? 0.2864 0.5866 0.3937 -0.0190 -0.0072 0.2400  82  PHE C CA  
2875 C C   . PHE C 65  ? 0.2575 0.5501 0.3839 -0.0795 0.0058  0.2331  82  PHE C C   
2876 O O   . PHE C 65  ? 0.3292 0.6409 0.3903 0.0026  0.0432  0.2725  82  PHE C O   
2877 C CB  . PHE C 65  ? 0.3464 0.5991 0.4146 0.0014  0.0018  0.2436  82  PHE C CB  
2878 C CG  . PHE C 65  ? 0.3558 0.6354 0.4367 -0.0159 -0.0113 0.2126  82  PHE C CG  
2879 C CD1 . PHE C 65  ? 0.4004 0.6429 0.4462 0.0110  -0.0127 0.1996  82  PHE C CD1 
2880 C CD2 . PHE C 65  ? 0.3952 0.6594 0.4496 -0.0258 -0.0089 0.1829  82  PHE C CD2 
2881 C CE1 . PHE C 65  ? 0.3754 0.5659 0.4532 -0.0272 -0.0231 0.1941  82  PHE C CE1 
2882 C CE2 . PHE C 65  ? 0.4073 0.6034 0.4575 -0.0069 -0.0189 0.1663  82  PHE C CE2 
2883 C CZ  . PHE C 65  ? 0.3897 0.5547 0.4559 -0.0066 -0.0241 0.1813  82  PHE C CZ  
2884 N N   . LEU C 66  ? 0.2414 0.5605 0.3716 -0.0409 0.0154  0.2357  83  LEU C N   
2885 C CA  . LEU C 66  ? 0.2595 0.4558 0.3652 -0.0102 -0.0065 0.2065  83  LEU C CA  
2886 C C   . LEU C 66  ? 0.2667 0.5318 0.3616 0.0183  0.0358  0.2407  83  LEU C C   
2887 O O   . LEU C 66  ? 0.2853 0.6030 0.3609 0.0941  0.0507  0.2525  83  LEU C O   
2888 C CB  . LEU C 66  ? 0.2400 0.4285 0.3633 0.0266  -0.0269 0.1524  83  LEU C CB  
2889 C CG  . LEU C 66  ? 0.2527 0.4157 0.3681 -0.0365 -0.0241 0.1000  83  LEU C CG  
2890 C CD1 . LEU C 66  ? 0.2791 0.3859 0.3620 -0.0167 -0.0306 0.0706  83  LEU C CD1 
2891 C CD2 . LEU C 66  ? 0.3027 0.4904 0.3760 -0.0564 -0.0204 0.0601  83  LEU C CD2 
2892 N N   . PRO C 67  ? 0.3589 0.5575 0.3620 0.0410  0.0525  0.2366  84  PRO C N   
2893 C CA  . PRO C 67  ? 0.4407 0.6665 0.3646 0.1566  0.0492  0.2302  84  PRO C CA  
2894 C C   . PRO C 67  ? 0.4102 0.7164 0.3606 0.1461  0.0583  0.2540  84  PRO C C   
2895 O O   . PRO C 67  ? 0.4667 0.7430 0.3704 0.2072  0.0691  0.2464  84  PRO C O   
2896 C CB  . PRO C 67  ? 0.4888 0.5959 0.3671 0.1804  0.0582  0.2337  84  PRO C CB  
2897 C CG  . PRO C 67  ? 0.4048 0.5729 0.3664 0.0821  0.0794  0.2306  84  PRO C CG  
2898 C CD  . PRO C 67  ? 0.3923 0.5088 0.3685 0.0319  0.0757  0.2422  84  PRO C CD  
2899 N N   . GLY C 68  ? 0.3985 0.7952 0.3612 0.1634  0.0696  0.2545  85  GLY C N   
2900 C CA  . GLY C 68  ? 0.3343 0.8303 0.3542 0.1385  0.0628  0.2380  85  GLY C CA  
2901 C C   . GLY C 68  ? 0.3102 0.8157 0.3533 0.0507  0.0691  0.2290  85  GLY C C   
2902 O O   . GLY C 68  ? 0.3336 0.8798 0.3664 0.0837  0.0816  0.2298  85  GLY C O   
2903 N N   . LEU C 69  ? 0.3222 0.6884 0.3435 0.0069  0.0553  0.2114  86  LEU C N   
2904 C CA  . LEU C 69  ? 0.3111 0.6441 0.3417 -0.0790 0.0332  0.1625  86  LEU C CA  
2905 C C   . LEU C 69  ? 0.2694 0.5946 0.3221 -0.0191 0.0435  0.1858  86  LEU C C   
2906 O O   . LEU C 69  ? 0.2989 0.6008 0.3170 0.0097  0.0545  0.2186  86  LEU C O   
2907 C CB  . LEU C 69  ? 0.3935 0.6684 0.3501 -0.0449 0.0512  0.1583  86  LEU C CB  
2908 C CG  . LEU C 69  ? 0.4772 0.5997 0.3619 -0.0275 0.0622  0.1611  86  LEU C CG  
2909 C CD1 . LEU C 69  ? 0.5046 0.6940 0.3697 0.0093  0.0562  0.1530  86  LEU C CD1 
2910 C CD2 . LEU C 69  ? 0.5537 0.5719 0.3674 -0.0037 0.0559  0.1481  86  LEU C CD2 
2911 N N   . ILE C 70  ? 0.3069 0.4972 0.3194 0.0923  0.0336  0.1455  87  ILE C N   
2912 C CA  A ILE C 70  ? 0.3915 0.4503 0.3173 0.1329  0.0398  0.1221  87  ILE C CA  
2913 C CA  B ILE C 70  ? 0.3649 0.4671 0.3197 0.1066  0.0479  0.1237  87  ILE C CA  
2914 C C   . ILE C 70  ? 0.4048 0.5119 0.3186 0.1859  0.0615  0.1321  87  ILE C C   
2915 O O   . ILE C 70  ? 0.4166 0.4970 0.3024 0.1521  0.0667  0.1281  87  ILE C O   
2916 C CB  A ILE C 70  ? 0.3834 0.3895 0.3189 0.1069  0.0302  0.1096  87  ILE C CB  
2917 C CB  B ILE C 70  ? 0.3531 0.4051 0.3216 0.0307  0.0499  0.1005  87  ILE C CB  
2918 C CG1 A ILE C 70  ? 0.3755 0.3379 0.3205 0.0670  0.0533  0.1134  87  ILE C CG1 
2919 C CG1 B ILE C 70  ? 0.3260 0.3202 0.3230 -0.0547 0.0615  0.0912  87  ILE C CG1 
2920 C CG2 A ILE C 70  ? 0.3783 0.4102 0.3217 0.0888  0.0207  0.0996  87  ILE C CG2 
2921 C CG2 B ILE C 70  ? 0.3571 0.4244 0.3228 0.0327  0.0495  0.0933  87  ILE C CG2 
2922 C CD1 A ILE C 70  ? 0.3302 0.3863 0.3264 0.0215  0.0669  0.0888  87  ILE C CD1 
2923 C CD1 B ILE C 70  ? 0.2881 0.2540 0.3271 -0.1302 0.0572  0.0721  87  ILE C CD1 
2924 N N   . GLU C 71  ? 0.5148 0.5302 0.3304 0.2507  0.0867  0.1375  88  GLU C N   
2925 C CA  . GLU C 71  ? 0.6005 0.6236 0.3507 0.3529  0.0931  0.1265  88  GLU C CA  
2926 C C   . GLU C 71  ? 0.5584 0.5990 0.3369 0.3278  0.1091  0.1457  88  GLU C C   
2927 O O   . GLU C 71  ? 0.6386 0.6399 0.3281 0.3230  0.1345  0.1636  88  GLU C O   
2928 C CB  . GLU C 71  ? 0.7818 0.7928 0.3832 0.4369  0.0861  0.1407  88  GLU C CB  
2929 C CG  . GLU C 71  ? 0.9571 0.9752 0.4094 0.4961  0.0794  0.1363  88  GLU C CG  
2930 C CD  . GLU C 71  ? 1.0610 1.1020 0.4394 0.5380  0.0742  0.1317  88  GLU C CD  
2931 O OE1 . GLU C 71  ? 1.0930 1.1653 0.4523 0.5723  0.0724  0.1197  88  GLU C OE1 
2932 O OE2 . GLU C 71  ? 1.1109 1.1062 0.4486 0.5315  0.0604  0.1353  88  GLU C OE2 
2933 N N   . LYS C 72  ? 0.4700 0.6062 0.3327 0.2400  0.0777  0.1692  89  LYS C N   
2934 C CA  . LYS C 72  ? 0.4486 0.6226 0.3335 0.2031  0.0591  0.1444  89  LYS C CA  
2935 C C   . LYS C 72  ? 0.3359 0.5759 0.3039 0.1314  0.0883  0.1578  89  LYS C C   
2936 O O   . LYS C 72  ? 0.3489 0.6270 0.2999 0.1085  0.0994  0.1602  89  LYS C O   
2937 C CB  . LYS C 72  ? 0.6044 0.6659 0.3672 0.2514  0.0361  0.1121  89  LYS C CB  
2938 C CG  . LYS C 72  ? 0.6716 0.7298 0.3913 0.3068  0.0322  0.0751  89  LYS C CG  
2939 C CD  . LYS C 72  ? 0.6980 0.7816 0.4131 0.3019  0.0243  0.0566  89  LYS C CD  
2940 C CE  . LYS C 72  ? 0.6773 0.8070 0.4270 0.2841  0.0240  0.0475  89  LYS C CE  
2941 N NZ  . LYS C 72  ? 0.6486 0.7869 0.4331 0.2751  0.0135  0.0598  89  LYS C NZ  
2942 N N   . MET C 73  ? 0.3494 0.4856 0.2896 0.1068  0.0814  0.1160  90  MET C N   
2943 C CA  . MET C 73  ? 0.3044 0.3752 0.2776 0.0272  0.0809  0.0765  90  MET C CA  
2944 C C   . MET C 73  ? 0.2888 0.3573 0.2609 0.0570  0.0593  0.0570  90  MET C C   
2945 O O   . MET C 73  ? 0.2968 0.3334 0.2544 0.0599  0.0300  0.0610  90  MET C O   
2946 C CB  . MET C 73  ? 0.3130 0.3490 0.2849 -0.0120 0.0716  0.0474  90  MET C CB  
2947 C CG  . MET C 73  ? 0.3479 0.3664 0.2848 -0.0208 0.0719  0.0123  90  MET C CG  
2948 S SD  . MET C 73  ? 0.3574 0.4550 0.2834 -0.0916 0.0518  0.0371  90  MET C SD  
2949 C CE  . MET C 73  ? 0.3197 0.3908 0.2945 -0.0274 0.0485  0.0425  90  MET C CE  
2950 N N   . THR C 74  ? 0.3698 0.3549 0.2574 0.0940  0.0544  0.0277  91  THR C N   
2951 C CA  . THR C 74  ? 0.4550 0.2390 0.2614 0.0711  0.0428  0.0383  91  THR C CA  
2952 C C   . THR C 74  ? 0.4152 0.3122 0.2627 0.1258  0.0647  0.0618  91  THR C C   
2953 O O   . THR C 74  ? 0.5103 0.4908 0.2807 0.2661  0.0846  0.0881  91  THR C O   
2954 C CB  . THR C 74  ? 0.5859 0.3529 0.2738 0.1968  0.0489  0.0373  91  THR C CB  
2955 O OG1 . THR C 74  ? 0.5646 0.4143 0.2820 0.1423  0.0656  0.0599  91  THR C OG1 
2956 C CG2 . THR C 74  ? 0.6220 0.3897 0.2831 0.1871  0.0532  0.0409  91  THR C CG2 
2957 N N   . GLY C 75  ? 0.2664 0.2650 0.2409 -0.0123 0.0067  0.0382  92  GLY C N   
2958 C CA  . GLY C 75  ? 0.2533 0.2845 0.2298 -0.0350 -0.0046 0.0212  92  GLY C CA  
2959 C C   . GLY C 75  ? 0.2197 0.2257 0.2157 -0.0022 0.0197  0.0239  92  GLY C C   
2960 O O   . GLY C 75  ? 0.2048 0.2617 0.2146 0.0093  0.0256  0.0014  92  GLY C O   
2961 N N   . PRO C 76  ? 0.2373 0.2439 0.1986 0.0500  0.0221  0.0033  93  PRO C N   
2962 C CA  . PRO C 76  ? 0.1974 0.2670 0.1887 0.0321  0.0395  -0.0003 93  PRO C CA  
2963 C C   . PRO C 76  ? 0.1882 0.2180 0.1920 -0.0206 0.0241  0.0066  93  PRO C C   
2964 O O   . PRO C 76  ? 0.1623 0.2626 0.1883 0.0091  0.0279  -0.0062 93  PRO C O   
2965 C CB  . PRO C 76  ? 0.1950 0.3093 0.1897 0.0521  0.0287  -0.0238 93  PRO C CB  
2966 C CG  . PRO C 76  ? 0.2752 0.3121 0.1965 0.0767  0.0286  -0.0072 93  PRO C CG  
2967 C CD  . PRO C 76  ? 0.2579 0.2555 0.2022 0.0212  0.0192  0.0165  93  PRO C CD  
2968 N N   . VAL C 77  ? 0.2073 0.2131 0.1948 0.0227  0.0036  0.0096  94  VAL C N   
2969 C CA  . VAL C 77  ? 0.1852 0.2254 0.1824 0.0355  0.0127  -0.0022 94  VAL C CA  
2970 C C   . VAL C 77  ? 0.1653 0.1888 0.1875 0.0106  -0.0071 -0.0103 94  VAL C C   
2971 O O   . VAL C 77  ? 0.1872 0.2562 0.1855 -0.0196 -0.0114 -0.0088 94  VAL C O   
2972 C CB  . VAL C 77  ? 0.1676 0.2785 0.1847 -0.0325 0.0031  -0.0050 94  VAL C CB  
2973 C CG1 . VAL C 77  ? 0.2279 0.2940 0.1800 0.0091  0.0049  -0.0089 94  VAL C CG1 
2974 C CG2 . VAL C 77  ? 0.2418 0.2941 0.1980 0.0483  -0.0001 0.0163  94  VAL C CG2 
2975 N N   . LEU C 78  ? 0.1664 0.2236 0.1853 0.0083  0.0191  0.0024  95  LEU C N   
2976 C CA  . LEU C 78  ? 0.1691 0.2578 0.1658 0.0196  0.0342  0.0219  95  LEU C CA  
2977 C C   . LEU C 78  ? 0.1812 0.2780 0.1566 0.0244  0.0100  0.0024  95  LEU C C   
2978 O O   . LEU C 78  ? 0.1894 0.2931 0.1553 0.0081  0.0013  0.0073  95  LEU C O   
2979 C CB  . LEU C 78  ? 0.1729 0.3025 0.1583 0.0279  0.0414  0.0067  95  LEU C CB  
2980 C CG  . LEU C 78  ? 0.1543 0.2956 0.1685 0.0383  0.0122  0.0074  95  LEU C CG  
2981 C CD1 . LEU C 78  ? 0.2304 0.3508 0.1678 0.0189  -0.0154 0.0436  95  LEU C CD1 
2982 C CD2 . LEU C 78  ? 0.1591 0.3085 0.1755 -0.0101 0.0016  0.0227  95  LEU C CD2 
2983 N N   . CYS C 79  ? 0.1372 0.2542 0.1602 0.0023  0.0090  0.0275  96  CYS C N   
2984 C CA  . CYS C 79  ? 0.1880 0.2580 0.1667 -0.0027 0.0172  0.0018  96  CYS C CA  
2985 C C   . CYS C 79  ? 0.1510 0.2133 0.1623 0.0102  0.0271  0.0237  96  CYS C C   
2986 O O   . CYS C 79  ? 0.1897 0.3001 0.1597 0.0426  0.0135  0.0391  96  CYS C O   
2987 C CB  . CYS C 79  ? 0.2098 0.2838 0.1818 0.0250  0.0251  0.0111  96  CYS C CB  
2988 S SG  . CYS C 79  ? 0.2374 0.2782 0.1937 -0.0088 0.0198  0.0198  96  CYS C SG  
2989 N N   . MET C 80  ? 0.1767 0.2687 0.1641 0.0172  0.0261  0.0139  97  MET C N   
2990 C CA  . MET C 80  ? 0.1691 0.2718 0.1608 -0.0246 0.0222  0.0314  97  MET C CA  
2991 C C   . MET C 80  ? 0.1758 0.2546 0.1557 0.0298  0.0013  0.0101  97  MET C C   
2992 O O   . MET C 80  ? 0.2108 0.2866 0.1635 0.0397  -0.0077 0.0142  97  MET C O   
2993 C CB  . MET C 80  ? 0.2308 0.2330 0.1605 0.0305  0.0136  0.0518  97  MET C CB  
2994 C CG  . MET C 80  ? 0.1905 0.2869 0.1710 0.0214  0.0232  0.0340  97  MET C CG  
2995 S SD  . MET C 80  ? 0.2129 0.2683 0.1787 0.0166  0.0268  0.0247  97  MET C SD  
2996 C CE  . MET C 80  ? 0.1867 0.2857 0.1757 0.0208  0.0098  0.0133  97  MET C CE  
2997 N N   . VAL C 81  ? 0.1576 0.2629 0.1450 0.0409  0.0057  0.0285  98  VAL C N   
2998 C CA  . VAL C 81  ? 0.1638 0.3000 0.1557 0.0505  0.0328  0.0280  98  VAL C CA  
2999 C C   . VAL C 81  ? 0.1525 0.2873 0.1547 0.0276  0.0127  0.0382  98  VAL C C   
3000 O O   . VAL C 81  ? 0.1870 0.2518 0.1574 0.0335  0.0124  0.0416  98  VAL C O   
3001 C CB  . VAL C 81  ? 0.1894 0.2865 0.1598 0.0145  0.0353  0.0583  98  VAL C CB  
3002 C CG1 . VAL C 81  ? 0.1806 0.3292 0.1730 0.0215  0.0573  0.0333  98  VAL C CG1 
3003 C CG2 . VAL C 81  ? 0.2128 0.3186 0.1513 0.0255  0.0075  0.0684  98  VAL C CG2 
3004 N N   . PHE C 82  ? 0.1686 0.2398 0.1526 0.0296  0.0161  0.0158  99  PHE C N   
3005 C CA  . PHE C 82  ? 0.1329 0.2202 0.1603 0.0233  0.0147  0.0216  99  PHE C CA  
3006 C C   . PHE C 82  ? 0.1687 0.2815 0.1578 0.0181  0.0363  0.0363  99  PHE C C   
3007 O O   . PHE C 82  ? 0.1955 0.3000 0.1543 0.0523  0.0359  0.0359  99  PHE C O   
3008 C CB  . PHE C 82  ? 0.1607 0.2690 0.1665 0.0463  0.0123  0.0131  99  PHE C CB  
3009 C CG  . PHE C 82  ? 0.1564 0.2304 0.1628 0.0546  0.0140  0.0273  99  PHE C CG  
3010 C CD1 . PHE C 82  ? 0.1703 0.2939 0.1543 0.0778  0.0121  0.0127  99  PHE C CD1 
3011 C CD2 . PHE C 82  ? 0.1803 0.2573 0.1635 0.0396  0.0109  0.0321  99  PHE C CD2 
3012 C CE1 . PHE C 82  ? 0.2534 0.2939 0.1543 0.0953  0.0270  0.0385  99  PHE C CE1 
3013 C CE2 . PHE C 82  ? 0.1814 0.3253 0.1638 0.0029  0.0241  0.0337  99  PHE C CE2 
3014 C CZ  . PHE C 82  ? 0.1502 0.3441 0.1636 0.0346  -0.0071 0.0324  99  PHE C CZ  
3015 N N   . GLU C 83  ? 0.1765 0.2727 0.1550 0.0518  0.0095  0.0390  100 GLU C N   
3016 C CA  . GLU C 83  ? 0.1616 0.2617 0.1636 0.0828  0.0306  0.0378  100 GLU C CA  
3017 C C   . GLU C 83  ? 0.1807 0.2715 0.1571 0.0099  0.0157  0.0148  100 GLU C C   
3018 O O   . GLU C 83  ? 0.2000 0.3276 0.1587 0.0516  0.0426  0.0442  100 GLU C O   
3019 C CB  . GLU C 83  ? 0.1695 0.2403 0.1623 0.0508  0.0349  0.0202  100 GLU C CB  
3020 C CG  . GLU C 83  ? 0.1585 0.3301 0.1743 0.0696  0.0094  0.0147  100 GLU C CG  
3021 C CD  . GLU C 83  ? 0.1707 0.4054 0.1930 0.0994  0.0309  0.0236  100 GLU C CD  
3022 O OE1 . GLU C 83  ? 0.2336 0.3446 0.1725 0.0453  0.0231  0.0179  100 GLU C OE1 
3023 O OE2 . GLU C 83  ? 0.2267 0.3844 0.2246 0.0361  0.0359  0.0373  100 GLU C OE2 
3024 N N   . GLY C 84  ? 0.2122 0.2661 0.1684 0.0101  0.0338  0.0060  101 GLY C N   
3025 C CA  . GLY C 84  ? 0.1802 0.2594 0.1675 0.0473  0.0144  0.0267  101 GLY C CA  
3026 C C   . GLY C 84  ? 0.2038 0.2581 0.1646 -0.0029 0.0230  0.0254  101 GLY C C   
3027 O O   . GLY C 84  ? 0.2081 0.3013 0.1729 0.0369  0.0382  0.0219  101 GLY C O   
3028 N N   . VAL C 85  ? 0.2075 0.2333 0.1545 0.0190  0.0456  0.0200  102 VAL C N   
3029 C CA  . VAL C 85  ? 0.2379 0.3051 0.1480 0.0600  0.0562  0.0327  102 VAL C CA  
3030 C C   . VAL C 85  ? 0.2104 0.2819 0.1546 0.0547  0.0503  0.0250  102 VAL C C   
3031 O O   . VAL C 85  ? 0.1941 0.3372 0.1598 0.0593  0.0221  0.0202  102 VAL C O   
3032 C CB  . VAL C 85  ? 0.2445 0.2928 0.1621 0.0394  0.0079  0.0155  102 VAL C CB  
3033 C CG1 . VAL C 85  ? 0.3313 0.2721 0.1763 0.0507  -0.0254 0.0146  102 VAL C CG1 
3034 C CG2 . VAL C 85  ? 0.3241 0.2571 0.1641 0.0746  0.0329  -0.0048 102 VAL C CG2 
3035 N N   . ASP C 86  ? 0.1950 0.2860 0.1646 0.0268  0.0349  0.0059  103 ASP C N   
3036 C CA  . ASP C 86  ? 0.2102 0.2681 0.1629 0.0633  0.0295  0.0025  103 ASP C CA  
3037 C C   . ASP C 86  ? 0.1631 0.2381 0.1576 0.0206  0.0320  -0.0008 103 ASP C C   
3038 O O   . ASP C 86  ? 0.1895 0.2838 0.1650 0.0767  0.0230  0.0064  103 ASP C O   
3039 C CB  . ASP C 86  ? 0.2163 0.2441 0.1711 0.0221  0.0396  -0.0031 103 ASP C CB  
3040 C CG  . ASP C 86  ? 0.2288 0.3411 0.1827 0.0044  0.0420  0.0013  103 ASP C CG  
3041 O OD1 . ASP C 86  ? 0.2647 0.3100 0.1854 0.0240  0.0353  0.0182  103 ASP C OD1 
3042 O OD2 . ASP C 86  ? 0.2698 0.3528 0.1914 -0.0088 0.0237  0.0145  103 ASP C OD2 
3043 N N   . VAL C 87  ? 0.1766 0.2386 0.1647 0.0345  0.0142  -0.0164 104 VAL C N   
3044 C CA  . VAL C 87  ? 0.1627 0.2614 0.1627 0.0478  0.0276  0.0373  104 VAL C CA  
3045 C C   . VAL C 87  ? 0.1563 0.2970 0.1570 0.0465  0.0101  0.0154  104 VAL C C   
3046 O O   . VAL C 87  ? 0.1765 0.2982 0.1557 0.0389  0.0002  0.0284  104 VAL C O   
3047 C CB  . VAL C 87  ? 0.1660 0.2823 0.1680 0.0685  0.0141  0.0255  104 VAL C CB  
3048 C CG1 . VAL C 87  ? 0.1832 0.2893 0.1794 0.0520  0.0136  0.0387  104 VAL C CG1 
3049 C CG2 . VAL C 87  ? 0.1781 0.2545 0.1715 0.0173  -0.0025 0.0202  104 VAL C CG2 
3050 N N   . ILE C 88  ? 0.2180 0.2607 0.1569 0.0291  0.0469  0.0240  105 ILE C N   
3051 C CA  . ILE C 88  ? 0.2083 0.2406 0.1589 0.0233  0.0493  0.0339  105 ILE C CA  
3052 C C   . ILE C 88  ? 0.2226 0.2296 0.1542 0.0183  0.0343  0.0132  105 ILE C C   
3053 O O   . ILE C 88  ? 0.1941 0.2477 0.1481 0.0270  -0.0005 0.0130  105 ILE C O   
3054 C CB  . ILE C 88  ? 0.1963 0.2894 0.1757 0.0334  0.0325  0.0524  105 ILE C CB  
3055 C CG1 . ILE C 88  ? 0.1661 0.3044 0.1788 0.0272  0.0348  0.0525  105 ILE C CG1 
3056 C CG2 . ILE C 88  ? 0.2270 0.3006 0.1880 0.0247  0.0329  0.0532  105 ILE C CG2 
3057 C CD1 . ILE C 88  ? 0.2014 0.3227 0.1819 0.0248  0.0539  0.0289  105 ILE C CD1 
3058 N N   . ALA C 89  ? 0.1865 0.2535 0.1567 0.0591  0.0273  0.0151  106 ALA C N   
3059 C CA  . ALA C 89  ? 0.1473 0.3133 0.1495 0.0188  0.0224  0.0075  106 ALA C CA  
3060 C C   . ALA C 89  ? 0.1724 0.2618 0.1544 0.0485  0.0139  0.0405  106 ALA C C   
3061 O O   . ALA C 89  ? 0.1979 0.2712 0.1690 0.0372  0.0291  0.0408  106 ALA C O   
3062 C CB  . ALA C 89  ? 0.2133 0.3401 0.1444 0.0866  0.0228  -0.0034 106 ALA C CB  
3063 N N   . GLN C 90  ? 0.1572 0.2820 0.1518 0.0300  0.0192  0.0444  107 GLN C N   
3064 C CA  . GLN C 90  ? 0.1663 0.2451 0.1558 -0.0023 0.0078  0.0357  107 GLN C CA  
3065 C C   . GLN C 90  ? 0.1853 0.2581 0.1513 0.0225  0.0119  0.0367  107 GLN C C   
3066 O O   . GLN C 90  ? 0.1680 0.2951 0.1615 0.0144  0.0065  0.0173  107 GLN C O   
3067 C CB  . GLN C 90  ? 0.2165 0.2195 0.1598 0.0210  0.0099  0.0319  107 GLN C CB  
3068 C CG  . GLN C 90  ? 0.2503 0.2435 0.1699 0.0257  -0.0019 0.0073  107 GLN C CG  
3069 C CD  . GLN C 90  ? 0.2386 0.2839 0.1710 -0.0183 -0.0004 -0.0122 107 GLN C CD  
3070 O OE1 . GLN C 90  ? 0.1870 0.3071 0.1697 -0.0087 0.0227  0.0221  107 GLN C OE1 
3071 N NE2 . GLN C 90  ? 0.3073 0.3068 0.1718 -0.0599 -0.0034 0.0053  107 GLN C NE2 
3072 N N   . ALA C 91  ? 0.1738 0.2747 0.1626 0.0209  0.0245  0.0368  108 ALA C N   
3073 C CA  . ALA C 91  ? 0.2177 0.2542 0.1717 0.0696  0.0260  -0.0176 108 ALA C CA  
3074 C C   . ALA C 91  ? 0.1801 0.2686 0.1810 0.0346  0.0234  0.0003  108 ALA C C   
3075 O O   . ALA C 91  ? 0.2023 0.2513 0.1928 0.0139  0.0188  -0.0025 108 ALA C O   
3076 C CB  . ALA C 91  ? 0.1697 0.2844 0.1840 -0.0033 -0.0012 -0.0191 108 ALA C CB  
3077 N N   . ARG C 92  ? 0.1841 0.2843 0.1880 0.0029  0.0342  0.0131  109 ARG C N   
3078 C CA  . ARG C 92  ? 0.1897 0.2774 0.1903 0.0035  0.0095  0.0289  109 ARG C CA  
3079 C C   . ARG C 92  ? 0.2398 0.2679 0.1658 0.0712  0.0310  0.0325  109 ARG C C   
3080 O O   . ARG C 92  ? 0.2380 0.3044 0.1624 0.0626  0.0198  0.0257  109 ARG C O   
3081 C CB  . ARG C 92  ? 0.2539 0.3291 0.2133 0.0574  -0.0182 0.0256  109 ARG C CB  
3082 C CG  . ARG C 92  ? 0.2357 0.3526 0.2464 0.0413  -0.0485 0.0515  109 ARG C CG  
3083 C CD  . ARG C 92  ? 0.3105 0.5011 0.2762 0.0069  -0.0714 0.0560  109 ARG C CD  
3084 N NE  . ARG C 92  ? 0.4470 0.5822 0.2964 0.0175  -0.0635 0.1004  109 ARG C NE  
3085 C CZ  . ARG C 92  ? 0.5807 0.7038 0.3099 0.0877  -0.0698 0.1034  109 ARG C CZ  
3086 N NH1 . ARG C 92  ? 0.6280 0.7384 0.3101 0.1712  -0.0974 0.0885  109 ARG C NH1 
3087 N NH2 . ARG C 92  ? 0.5773 0.7312 0.3236 0.0057  -0.0674 0.1127  109 ARG C NH2 
3088 N N   . LYS C 93  ? 0.2099 0.2681 0.1583 0.0539  0.0120  0.0335  110 LYS C N   
3089 C CA  . LYS C 93  ? 0.2179 0.2371 0.1759 0.0440  -0.0017 0.0110  110 LYS C CA  
3090 C C   . LYS C 93  ? 0.1693 0.2582 0.1819 0.0289  0.0221  0.0059  110 LYS C C   
3091 O O   . LYS C 93  ? 0.1607 0.2836 0.2031 0.0327  0.0260  -0.0317 110 LYS C O   
3092 C CB  . LYS C 93  ? 0.2679 0.2446 0.1922 0.0221  0.0031  0.0210  110 LYS C CB  
3093 C CG  . LYS C 93  ? 0.3585 0.2649 0.2232 0.0351  0.0154  0.0258  110 LYS C CG  
3094 C CD  . LYS C 93  ? 0.4223 0.2396 0.2452 0.0299  0.0070  0.0037  110 LYS C CD  
3095 C CE  . LYS C 93  ? 0.4239 0.2798 0.2638 -0.0196 -0.0094 -0.0269 110 LYS C CE  
3096 N NZ  . LYS C 93  ? 0.4509 0.2380 0.2773 -0.0744 0.0192  -0.0058 110 LYS C NZ  
3097 N N   . MET C 94  ? 0.1624 0.2403 0.1728 0.0338  0.0033  0.0001  111 MET C N   
3098 C CA  . MET C 94  ? 0.2027 0.2311 0.1768 0.0796  0.0161  0.0027  111 MET C CA  
3099 C C   . MET C 94  ? 0.1424 0.2252 0.1832 0.0475  0.0027  0.0023  111 MET C C   
3100 O O   . MET C 94  ? 0.1707 0.2267 0.1944 0.0535  0.0216  0.0041  111 MET C O   
3101 C CB  . MET C 94  ? 0.1650 0.2395 0.1632 0.0040  0.0109  -0.0001 111 MET C CB  
3102 C CG  . MET C 94  ? 0.1896 0.2533 0.1603 0.0266  -0.0153 -0.0028 111 MET C CG  
3103 S SD  . MET C 94  ? 0.2231 0.2460 0.1602 0.0304  -0.0102 0.0112  111 MET C SD  
3104 C CE  . MET C 94  ? 0.2865 0.3581 0.1446 0.0437  0.0235  0.0368  111 MET C CE  
3105 N N   . MET C 95  ? 0.1934 0.1993 0.1764 -0.0017 0.0079  0.0000  112 MET C N   
3106 C CA  A MET C 95  ? 0.2023 0.2351 0.1819 -0.0064 -0.0188 -0.0036 112 MET C CA  
3107 C CA  B MET C 95  ? 0.1881 0.2527 0.1782 -0.0106 0.0013  -0.0132 112 MET C CA  
3108 C C   . MET C 95  ? 0.1957 0.2542 0.1708 0.0134  0.0161  0.0015  112 MET C C   
3109 O O   . MET C 95  ? 0.1867 0.2826 0.1581 0.0584  0.0326  0.0268  112 MET C O   
3110 C CB  A MET C 95  ? 0.2282 0.1943 0.2029 0.0243  -0.0343 0.0426  112 MET C CB  
3111 C CB  B MET C 95  ? 0.1849 0.2742 0.1909 0.0056  0.0158  0.0019  112 MET C CB  
3112 C CG  A MET C 95  ? 0.2508 0.2636 0.2210 -0.0006 -0.0492 0.0518  112 MET C CG  
3113 C CG  B MET C 95  ? 0.1806 0.3241 0.1998 0.0025  0.0213  -0.0128 112 MET C CG  
3114 S SD  A MET C 95  ? 0.2447 0.3073 0.2442 -0.0313 -0.0481 0.0620  112 MET C SD  
3115 S SD  B MET C 95  ? 0.1797 0.3538 0.2142 -0.0305 0.0398  -0.0242 112 MET C SD  
3116 C CE  A MET C 95  ? 0.3301 0.4094 0.2519 0.0243  -0.0282 0.0864  112 MET C CE  
3117 C CE  B MET C 95  ? 0.2928 0.4479 0.2261 -0.0436 0.0170  0.0141  112 MET C CE  
3118 N N   . GLY C 96  ? 0.2079 0.2493 0.1620 0.0519  -0.0009 -0.0274 113 GLY C N   
3119 C CA  . GLY C 96  ? 0.2315 0.2404 0.1644 0.0126  -0.0188 0.0150  113 GLY C CA  
3120 C C   . GLY C 96  ? 0.2069 0.2353 0.1682 0.0096  0.0027  0.0068  113 GLY C C   
3121 O O   . GLY C 96  ? 0.2248 0.2874 0.1743 0.0165  -0.0130 0.0232  113 GLY C O   
3122 N N   . SER C 97  ? 0.2316 0.2603 0.1688 0.0317  -0.0091 0.0026  114 SER C N   
3123 C CA  . SER C 97  ? 0.2817 0.2387 0.1821 0.0165  0.0048  0.0454  114 SER C CA  
3124 C C   . SER C 97  ? 0.2422 0.2821 0.1778 0.0332  0.0262  0.0309  114 SER C C   
3125 O O   . SER C 97  ? 0.2058 0.2959 0.1543 0.0072  0.0328  0.0119  114 SER C O   
3126 C CB  . SER C 97  ? 0.2817 0.3675 0.2009 0.0136  -0.0436 0.0171  114 SER C CB  
3127 O OG  . SER C 97  ? 0.3377 0.4908 0.2301 0.0749  -0.0526 0.0445  114 SER C OG  
3128 N N   . THR C 98  ? 0.2394 0.2777 0.1960 0.0057  0.0133  0.0242  115 THR C N   
3129 C CA  . THR C 98  ? 0.1895 0.3278 0.2123 -0.0106 0.0422  -0.0116 115 THR C CA  
3130 C C   . THR C 98  ? 0.1851 0.2995 0.1917 -0.0044 0.0494  0.0109  115 THR C C   
3131 O O   . THR C 98  ? 0.2532 0.2972 0.1863 0.0417  0.0292  0.0071  115 THR C O   
3132 C CB  . THR C 98  ? 0.2485 0.3773 0.2664 -0.0570 0.1297  -0.0271 115 THR C CB  
3133 O OG1 . THR C 98  ? 0.3955 0.5366 0.2977 -0.0146 0.1193  -0.0214 115 THR C OG1 
3134 C CG2 . THR C 98  ? 0.2745 0.3497 0.2770 -0.0345 0.1394  -0.0225 115 THR C CG2 
3135 N N   . ARG C 99  ? 0.2086 0.2611 0.1852 0.0047  0.0066  0.0173  116 ARG C N   
3136 C CA  . ARG C 99  ? 0.2494 0.2362 0.1853 0.0112  -0.0259 -0.0304 116 ARG C CA  
3137 C C   . ARG C 99  ? 0.2110 0.2430 0.1730 0.0331  0.0021  -0.0003 116 ARG C C   
3138 O O   . ARG C 99  ? 0.2081 0.2670 0.1647 0.0330  0.0148  -0.0150 116 ARG C O   
3139 C CB  . ARG C 99  ? 0.2742 0.2791 0.2048 -0.0286 -0.0736 -0.0069 116 ARG C CB  
3140 C CG  . ARG C 99  ? 0.4314 0.3486 0.2369 -0.0568 -0.0731 0.0077  116 ARG C CG  
3141 C CD  . ARG C 99  ? 0.6040 0.4287 0.2681 -0.0323 -0.1237 -0.0106 116 ARG C CD  
3142 N NE  . ARG C 99  ? 0.9046 0.7145 0.3004 0.0144  -0.1376 -0.0030 116 ARG C NE  
3143 C CZ  . ARG C 99  ? 1.1734 0.9713 0.3401 0.1215  -0.1366 0.0105  116 ARG C CZ  
3144 N NH1 . ARG C 99  ? 1.2586 1.0806 0.3614 0.1448  -0.1371 0.0082  116 ARG C NH1 
3145 N NH2 . ARG C 99  ? 1.2647 1.0244 0.3600 0.1613  -0.1235 0.0230  116 ARG C NH2 
3146 N N   . PRO C 100 ? 0.2283 0.2525 0.1688 0.0016  0.0137  0.0113  117 PRO C N   
3147 C CA  . PRO C 100 ? 0.1861 0.2235 0.1686 0.0165  0.0137  0.0106  117 PRO C CA  
3148 C C   . PRO C 100 ? 0.1636 0.2680 0.1717 0.0089  -0.0003 -0.0041 117 PRO C C   
3149 O O   . PRO C 100 ? 0.2267 0.2337 0.1639 0.0267  0.0143  0.0055  117 PRO C O   
3150 C CB  . PRO C 100 ? 0.1871 0.2417 0.1600 0.0344  0.0356  0.0382  117 PRO C CB  
3151 C CG  . PRO C 100 ? 0.2156 0.2275 0.1646 0.0405  0.0561  0.0517  117 PRO C CG  
3152 C CD  . PRO C 100 ? 0.2014 0.2689 0.1630 0.0044  0.0423  0.0322  117 PRO C CD  
3153 N N   . GLY C 101 ? 0.1687 0.3335 0.1818 0.0428  0.0048  0.0142  118 GLY C N   
3154 C CA  . GLY C 101 ? 0.2043 0.3387 0.1867 0.0339  -0.0122 0.0200  118 GLY C CA  
3155 C C   . GLY C 101 ? 0.2030 0.2809 0.1707 -0.0103 0.0043  0.0236  118 GLY C C   
3156 O O   . GLY C 101 ? 0.1992 0.3171 0.1759 0.0343  0.0105  0.0017  118 GLY C O   
3157 N N   . GLU C 102 ? 0.1819 0.2585 0.1593 0.0248  0.0109  0.0299  119 GLU C N   
3158 C CA  . GLU C 102 ? 0.2038 0.2897 0.1624 0.0388  0.0066  0.0108  119 GLU C CA  
3159 C C   . GLU C 102 ? 0.2219 0.2649 0.1612 0.0451  -0.0058 0.0054  119 GLU C C   
3160 O O   . GLU C 102 ? 0.2584 0.2736 0.1817 0.0561  -0.0139 0.0051  119 GLU C O   
3161 C CB  . GLU C 102 ? 0.2822 0.2889 0.1635 0.0382  0.0173  0.0350  119 GLU C CB  
3162 C CG  . GLU C 102 ? 0.3076 0.2915 0.1793 0.0013  0.0138  0.0528  119 GLU C CG  
3163 C CD  . GLU C 102 ? 0.3980 0.3831 0.2044 0.0175  -0.0108 0.0561  119 GLU C CD  
3164 O OE1 . GLU C 102 ? 0.4314 0.3812 0.2079 0.0006  0.0267  0.0445  119 GLU C OE1 
3165 O OE2 . GLU C 102 ? 0.4848 0.4631 0.2236 0.0245  -0.0367 0.0835  119 GLU C OE2 
3166 N N   . ALA C 103 ? 0.2351 0.2375 0.1539 0.0093  -0.0024 0.0157  120 ALA C N   
3167 C CA  . ALA C 103 ? 0.2273 0.2350 0.1709 0.0174  -0.0066 -0.0018 120 ALA C CA  
3168 C C   . ALA C 103 ? 0.2675 0.2807 0.2061 0.0287  -0.0368 0.0180  120 ALA C C   
3169 O O   . ALA C 103 ? 0.2525 0.2568 0.2195 0.0347  -0.0185 0.0299  120 ALA C O   
3170 C CB  . ALA C 103 ? 0.2355 0.2558 0.1536 -0.0082 -0.0204 -0.0121 120 ALA C CB  
3171 N N   . ALA C 104 ? 0.2892 0.2064 0.2292 0.0035  -0.0537 0.0219  121 ALA C N   
3172 C CA  . ALA C 104 ? 0.3281 0.2861 0.2608 0.0486  -0.0521 0.0153  121 ALA C CA  
3173 C C   . ALA C 104 ? 0.2631 0.2678 0.2790 0.0216  -0.0531 0.0205  121 ALA C C   
3174 O O   . ALA C 104 ? 0.2206 0.2362 0.2504 -0.0078 -0.0385 -0.0102 121 ALA C O   
3175 C CB  . ALA C 104 ? 0.4298 0.2728 0.2550 0.0752  -0.0311 -0.0190 121 ALA C CB  
3176 N N   . PRO C 105 ? 0.2886 0.3499 0.3046 -0.0196 -0.0913 0.0708  122 PRO C N   
3177 C CA  . PRO C 105 ? 0.2079 0.3190 0.3071 -0.1006 -0.0728 0.0661  122 PRO C CA  
3178 C C   . PRO C 105 ? 0.2139 0.2730 0.2847 -0.0552 -0.0424 0.0337  122 PRO C C   
3179 O O   . PRO C 105 ? 0.2889 0.2642 0.2808 0.0424  -0.0656 0.0247  122 PRO C O   
3180 C CB  . PRO C 105 ? 0.2851 0.4213 0.3200 -0.1149 -0.0920 0.0960  122 PRO C CB  
3181 C CG  . PRO C 105 ? 0.3439 0.4817 0.3226 -0.0412 -0.0901 0.1298  122 PRO C CG  
3182 C CD  . PRO C 105 ? 0.3269 0.5064 0.3190 -0.0071 -0.0957 0.1073  122 PRO C CD  
3183 N N   . GLY C 106 ? 0.2360 0.2075 0.2649 0.0041  0.0321  -0.0072 123 GLY C N   
3184 C CA  . GLY C 106 ? 0.2602 0.2189 0.2299 0.0404  0.0367  0.0083  123 GLY C CA  
3185 C C   . GLY C 106 ? 0.1759 0.2269 0.1970 -0.0135 0.0221  0.0416  123 GLY C C   
3186 O O   . GLY C 106 ? 0.2499 0.3152 0.1937 -0.0019 -0.0130 0.0040  123 GLY C O   
3187 N N   . THR C 107 ? 0.1850 0.2073 0.1827 0.0233  0.0259  0.0296  124 THR C N   
3188 C CA  . THR C 107 ? 0.2091 0.2281 0.1729 0.0408  0.0211  0.0133  124 THR C CA  
3189 C C   . THR C 107 ? 0.1331 0.2102 0.1643 0.0440  0.0140  0.0113  124 THR C C   
3190 O O   . THR C 107 ? 0.1616 0.2362 0.1634 0.0333  0.0045  0.0076  124 THR C O   
3191 C CB  . THR C 107 ? 0.1789 0.2347 0.1602 0.0209  0.0050  0.0051  124 THR C CB  
3192 O OG1 . THR C 107 ? 0.1827 0.2544 0.1676 0.0230  0.0077  -0.0044 124 THR C OG1 
3193 C CG2 . THR C 107 ? 0.2386 0.2862 0.1456 0.0187  0.0289  0.0036  124 THR C CG2 
3194 N N   . ILE C 108 ? 0.1794 0.2215 0.1584 0.0538  0.0287  0.0251  125 ILE C N   
3195 C CA  . ILE C 108 ? 0.1761 0.2306 0.1589 0.0555  -0.0012 0.0121  125 ILE C CA  
3196 C C   . ILE C 108 ? 0.1668 0.2229 0.1548 0.0114  -0.0017 -0.0217 125 ILE C C   
3197 O O   . ILE C 108 ? 0.1731 0.2297 0.1608 0.0430  0.0234  -0.0187 125 ILE C O   
3198 C CB  . ILE C 108 ? 0.1196 0.2750 0.1687 -0.0007 -0.0040 0.0136  125 ILE C CB  
3199 C CG1 . ILE C 108 ? 0.1691 0.2954 0.1674 -0.0181 -0.0320 0.0027  125 ILE C CG1 
3200 C CG2 . ILE C 108 ? 0.2178 0.2796 0.1680 0.0054  -0.0191 -0.0137 125 ILE C CG2 
3201 C CD1 . ILE C 108 ? 0.1607 0.3434 0.1810 -0.0331 -0.0317 -0.0210 125 ILE C CD1 
3202 N N   . ARG C 109 ? 0.1636 0.2266 0.1602 0.0368  0.0116  0.0061  126 ARG C N   
3203 C CA  . ARG C 109 ? 0.2223 0.2195 0.1652 0.0262  0.0200  0.0104  126 ARG C CA  
3204 C C   . ARG C 109 ? 0.1514 0.2385 0.1543 0.0150  0.0241  0.0121  126 ARG C C   
3205 O O   . ARG C 109 ? 0.1814 0.2508 0.1528 0.0361  -0.0019 0.0101  126 ARG C O   
3206 C CB  . ARG C 109 ? 0.2260 0.2459 0.1839 0.0183  0.0238  0.0068  126 ARG C CB  
3207 C CG  . ARG C 109 ? 0.2909 0.3029 0.2097 -0.0838 0.0550  0.0183  126 ARG C CG  
3208 C CD  . ARG C 109 ? 0.2931 0.3438 0.2401 -0.0792 -0.0084 0.0050  126 ARG C CD  
3209 N NE  . ARG C 109 ? 0.2244 0.2632 0.2444 -0.0149 -0.0220 0.0281  126 ARG C NE  
3210 C CZ  . ARG C 109 ? 0.2165 0.3385 0.2219 0.0199  -0.0031 0.0216  126 ARG C CZ  
3211 N NH1 . ARG C 109 ? 0.2944 0.3756 0.2347 -0.0026 -0.0234 -0.0209 126 ARG C NH1 
3212 N NH2 . ARG C 109 ? 0.2568 0.3529 0.2043 -0.0463 0.0069  0.0124  126 ARG C NH2 
3213 N N   . ALA C 110 ? 0.1641 0.2173 0.1540 0.0265  -0.0066 0.0070  127 ALA C N   
3214 C CA  . ALA C 110 ? 0.1974 0.2890 0.1551 0.0519  0.0225  0.0189  127 ALA C CA  
3215 C C   . ALA C 110 ? 0.1311 0.2653 0.1514 -0.0072 0.0016  0.0019  127 ALA C C   
3216 O O   . ALA C 110 ? 0.1870 0.2922 0.1493 0.0330  0.0259  0.0402  127 ALA C O   
3217 C CB  . ALA C 110 ? 0.1976 0.2715 0.1406 0.0482  0.0313  0.0037  127 ALA C CB  
3218 N N   . ASP C 111 ? 0.1691 0.2304 0.1575 0.0140  0.0063  0.0032  128 ASP C N   
3219 C CA  . ASP C 111 ? 0.1738 0.1917 0.1679 0.0376  0.0167  0.0171  128 ASP C CA  
3220 C C   . ASP C 111 ? 0.1612 0.2181 0.1516 0.0237  0.0000  -0.0040 128 ASP C C   
3221 O O   . ASP C 111 ? 0.1711 0.2298 0.1392 0.0160  0.0108  0.0000  128 ASP C O   
3222 C CB  . ASP C 111 ? 0.1783 0.2424 0.1916 0.0361  0.0112  0.0159  128 ASP C CB  
3223 C CG  . ASP C 111 ? 0.2210 0.3252 0.2359 0.0874  -0.0396 0.0059  128 ASP C CG  
3224 O OD1 . ASP C 111 ? 0.2335 0.3240 0.2566 0.0440  -0.0520 -0.0044 128 ASP C OD1 
3225 O OD2 . ASP C 111 ? 0.2113 0.2780 0.2490 0.0333  0.0016  0.0108  128 ASP C OD2 
3226 N N   . PHE C 112 ? 0.1841 0.2023 0.1503 0.0005  0.0172  0.0011  129 PHE C N   
3227 C CA  . PHE C 112 ? 0.1469 0.2007 0.1489 -0.0129 -0.0032 0.0232  129 PHE C CA  
3228 C C   . PHE C 112 ? 0.1721 0.1957 0.1459 0.0086  0.0114  0.0497  129 PHE C C   
3229 O O   . PHE C 112 ? 0.1790 0.2266 0.1387 0.0244  0.0117  0.0092  129 PHE C O   
3230 C CB  . PHE C 112 ? 0.1538 0.2426 0.1542 0.0170  -0.0024 0.0382  129 PHE C CB  
3231 C CG  . PHE C 112 ? 0.1371 0.2522 0.1454 0.0147  0.0009  0.0063  129 PHE C CG  
3232 C CD1 . PHE C 112 ? 0.2044 0.2491 0.1509 0.0493  0.0154  0.0184  129 PHE C CD1 
3233 C CD2 . PHE C 112 ? 0.2003 0.2869 0.1411 0.0277  -0.0107 0.0470  129 PHE C CD2 
3234 C CE1 . PHE C 112 ? 0.2403 0.2934 0.1408 0.0434  -0.0018 0.0159  129 PHE C CE1 
3235 C CE2 . PHE C 112 ? 0.2533 0.2368 0.1456 0.0105  -0.0133 0.0188  129 PHE C CE2 
3236 C CZ  . PHE C 112 ? 0.2306 0.3021 0.1429 0.0187  -0.0024 0.0108  129 PHE C CZ  
3237 N N   . CYS C 113 ? 0.1695 0.2013 0.1463 0.0115  -0.0002 0.0140  130 CYS C N   
3238 C CA  . CYS C 113 ? 0.1864 0.2321 0.1571 0.0614  -0.0089 0.0254  130 CYS C CA  
3239 C C   . CYS C 113 ? 0.1639 0.1547 0.1588 -0.0013 0.0012  0.0152  130 CYS C C   
3240 O O   . CYS C 113 ? 0.1555 0.1988 0.1563 0.0062  0.0008  0.0151  130 CYS C O   
3241 C CB  . CYS C 113 ? 0.2076 0.1924 0.1549 0.0089  0.0009  0.0136  130 CYS C CB  
3242 S SG  . CYS C 113 ? 0.1699 0.2825 0.1611 0.0077  -0.0080 0.0382  130 CYS C SG  
3243 N N   . GLN C 114 ? 0.1796 0.1741 0.1607 -0.0129 0.0014  0.0276  131 GLN C N   
3244 C CA  . GLN C 114 ? 0.1821 0.2308 0.1487 0.0450  -0.0004 0.0482  131 GLN C CA  
3245 C C   . GLN C 114 ? 0.1908 0.2060 0.1451 0.0050  0.0178  0.0536  131 GLN C C   
3246 O O   . GLN C 114 ? 0.2350 0.2837 0.1400 0.0406  0.0046  0.0426  131 GLN C O   
3247 C CB  . GLN C 114 ? 0.1836 0.2203 0.1457 0.0254  -0.0058 0.0388  131 GLN C CB  
3248 C CG  . GLN C 114 ? 0.2100 0.2362 0.1475 0.0141  0.0138  0.0105  131 GLN C CG  
3249 C CD  . GLN C 114 ? 0.1752 0.2389 0.1548 0.0005  0.0089  0.0305  131 GLN C CD  
3250 O OE1 . GLN C 114 ? 0.2012 0.2265 0.1755 0.0465  -0.0189 0.0244  131 GLN C OE1 
3251 N NE2 . GLN C 114 ? 0.1926 0.2473 0.1478 0.0398  0.0386  0.0364  131 GLN C NE2 
3252 N N   . GLN C 115 ? 0.1520 0.2412 0.1554 -0.0109 0.0038  0.0566  132 GLN C N   
3253 C CA  . GLN C 115 ? 0.2469 0.2119 0.1627 0.0507  0.0196  0.0518  132 GLN C CA  
3254 C C   . GLN C 115 ? 0.1900 0.2245 0.1595 0.0391  0.0107  0.0268  132 GLN C C   
3255 O O   . GLN C 115 ? 0.2338 0.2394 0.1530 0.0250  0.0067  0.0443  132 GLN C O   
3256 C CB  . GLN C 115 ? 0.1934 0.2589 0.1859 -0.0110 0.0341  0.0576  132 GLN C CB  
3257 C CG  . GLN C 115 ? 0.2674 0.2610 0.2152 0.0136  0.0012  0.0363  132 GLN C CG  
3258 C CD  . GLN C 115 ? 0.2225 0.2769 0.2278 0.0078  -0.0099 0.0400  132 GLN C CD  
3259 O OE1 . GLN C 115 ? 0.3013 0.2927 0.2445 0.0234  0.0192  0.0226  132 GLN C OE1 
3260 N NE2 . GLN C 115 ? 0.3011 0.3719 0.2244 0.0246  -0.0403 0.0540  132 GLN C NE2 
3261 N N   . ALA C 116 ? 0.2459 0.2622 0.1813 0.0235  0.0392  0.0363  133 ALA C N   
3262 C CA  . ALA C 116 ? 0.2582 0.3028 0.1831 -0.0137 0.0574  0.0245  133 ALA C CA  
3263 C C   . ALA C 116 ? 0.2354 0.2706 0.1950 0.0290  0.0322  0.0157  133 ALA C C   
3264 O O   . ALA C 116 ? 0.2377 0.3076 0.2105 0.0275  0.0502  0.0130  133 ALA C O   
3265 C CB  . ALA C 116 ? 0.3142 0.3000 0.1718 0.0069  0.0655  0.0409  133 ALA C CB  
3266 N N   . GLY C 117 ? 0.2803 0.2373 0.1939 -0.0217 0.0444  0.0411  134 GLY C N   
3267 C CA  . GLY C 117 ? 0.3005 0.2565 0.2039 0.0154  0.0453  0.0251  134 GLY C CA  
3268 C C   . GLY C 117 ? 0.2762 0.2882 0.2093 -0.0122 0.0320  0.0214  134 GLY C C   
3269 O O   . GLY C 117 ? 0.2708 0.2876 0.2191 -0.0470 0.0436  0.0233  134 GLY C O   
3270 N N   . ARG C 118 ? 0.2128 0.2601 0.2057 0.0134  0.0268  0.0268  135 ARG C N   
3271 C CA  . ARG C 118 ? 0.2314 0.2531 0.1849 0.0250  0.0084  0.0214  135 ARG C CA  
3272 C C   . ARG C 118 ? 0.1917 0.2467 0.1683 0.0141  0.0068  0.0434  135 ARG C C   
3273 O O   . ARG C 118 ? 0.1913 0.2570 0.1631 0.0174  0.0171  0.0184  135 ARG C O   
3274 C CB  . ARG C 118 ? 0.2544 0.1700 0.1817 -0.0057 0.0103  0.0235  135 ARG C CB  
3275 C CG  . ARG C 118 ? 0.2291 0.2151 0.1874 -0.0018 0.0250  0.0455  135 ARG C CG  
3276 C CD  . ARG C 118 ? 0.2803 0.2068 0.1918 -0.0021 -0.0003 0.0083  135 ARG C CD  
3277 N NE  . ARG C 118 ? 0.3098 0.2440 0.2122 0.0073  0.0079  0.0262  135 ARG C NE  
3278 C CZ  . ARG C 118 ? 0.2829 0.2884 0.2374 -0.0117 -0.0165 0.0015  135 ARG C CZ  
3279 N NH1 . ARG C 118 ? 0.2878 0.3340 0.2413 0.0115  -0.0611 0.0219  135 ARG C NH1 
3280 N NH2 . ARG C 118 ? 0.3132 0.3169 0.2486 -0.0112 -0.0259 -0.0125 135 ARG C NH2 
3281 N N   . ASN C 119 ? 0.1560 0.2469 0.1646 0.0355  -0.0103 0.0355  136 ASN C N   
3282 C CA  . ASN C 119 ? 0.2230 0.2273 0.1603 0.0188  -0.0004 0.0255  136 ASN C CA  
3283 C C   . ASN C 119 ? 0.2074 0.2323 0.1530 -0.0185 -0.0214 0.0043  136 ASN C C   
3284 O O   . ASN C 119 ? 0.2029 0.2422 0.1523 -0.0010 -0.0074 0.0109  136 ASN C O   
3285 C CB  . ASN C 119 ? 0.2161 0.2608 0.1519 0.0321  -0.0051 0.0214  136 ASN C CB  
3286 C CG  . ASN C 119 ? 0.2029 0.2932 0.1534 0.0118  -0.0050 0.0298  136 ASN C CG  
3287 O OD1 . ASN C 119 ? 0.2169 0.3269 0.1639 0.0017  0.0160  0.0152  136 ASN C OD1 
3288 N ND2 . ASN C 119 ? 0.2293 0.3165 0.1600 0.0113  -0.0002 0.0559  136 ASN C ND2 
3289 N N   . LEU C 120 ? 0.1771 0.2274 0.1572 0.0214  -0.0192 0.0158  137 LEU C N   
3290 C CA  . LEU C 120 ? 0.1364 0.2332 0.1530 -0.0022 -0.0080 0.0076  137 LEU C CA  
3291 C C   . LEU C 120 ? 0.1386 0.2711 0.1549 0.0007  0.0065  0.0052  137 LEU C C   
3292 O O   . LEU C 120 ? 0.1744 0.2216 0.1829 0.0155  -0.0067 -0.0179 137 LEU C O   
3293 C CB  . LEU C 120 ? 0.1685 0.3130 0.1530 0.0305  0.0048  -0.0034 137 LEU C CB  
3294 C CG  . LEU C 120 ? 0.1877 0.2782 0.1615 0.0103  0.0308  0.0074  137 LEU C CG  
3295 C CD1 . LEU C 120 ? 0.1588 0.2616 0.1722 0.0045  0.0155  -0.0032 137 LEU C CD1 
3296 C CD2 . LEU C 120 ? 0.1883 0.3388 0.1591 0.0313  0.0366  -0.0014 137 LEU C CD2 
3297 N N   . ILE C 121 ? 0.1669 0.2637 0.1561 0.0590  0.0162  0.0291  138 ILE C N   
3298 C CA  . ILE C 121 ? 0.1922 0.2328 0.1535 0.0230  0.0155  0.0397  138 ILE C CA  
3299 C C   . ILE C 121 ? 0.1381 0.2356 0.1617 0.0445  0.0180  0.0511  138 ILE C C   
3300 O O   . ILE C 121 ? 0.1782 0.3226 0.1708 0.0565  0.0010  0.0300  138 ILE C O   
3301 C CB  . ILE C 121 ? 0.1567 0.2838 0.1539 0.0345  -0.0032 0.0221  138 ILE C CB  
3302 C CG1 . ILE C 121 ? 0.1826 0.2334 0.1515 0.0119  0.0021  0.0250  138 ILE C CG1 
3303 C CG2 . ILE C 121 ? 0.1896 0.3376 0.1587 0.0616  0.0169  0.0231  138 ILE C CG2 
3304 C CD1 . ILE C 121 ? 0.2233 0.2785 0.1588 0.0460  0.0092  0.0206  138 ILE C CD1 
3305 N N   . HIS C 122 ? 0.1429 0.2952 0.1663 0.0484  0.0225  0.0005  139 HIS C N   
3306 C CA  . HIS C 122 ? 0.1615 0.2619 0.1677 0.0200  0.0018  -0.0107 139 HIS C CA  
3307 C C   . HIS C 122 ? 0.1546 0.2845 0.1508 0.0280  0.0109  0.0101  139 HIS C C   
3308 O O   . HIS C 122 ? 0.1745 0.3009 0.1429 0.0497  0.0113  0.0290  139 HIS C O   
3309 C CB  . HIS C 122 ? 0.1815 0.2770 0.1897 0.0112  0.0361  0.0201  139 HIS C CB  
3310 C CG  . HIS C 122 ? 0.1877 0.3129 0.1999 0.0317  0.0444  0.0136  139 HIS C CG  
3311 N ND1 . HIS C 122 ? 0.2696 0.4497 0.2115 0.1161  0.0752  0.0652  139 HIS C ND1 
3312 C CD2 . HIS C 122 ? 0.1600 0.3036 0.2049 0.0108  0.0403  0.0267  139 HIS C CD2 
3313 C CE1 . HIS C 122 ? 0.2822 0.4054 0.2144 0.1102  0.0599  0.0555  139 HIS C CE1 
3314 N NE2 . HIS C 122 ? 0.1961 0.3335 0.2107 -0.0017 0.0614  0.0305  139 HIS C NE2 
3315 N N   . GLY C 123 ? 0.1447 0.3023 0.1594 0.0305  0.0400  0.0006  140 GLY C N   
3316 C CA  . GLY C 123 ? 0.1428 0.3180 0.1482 0.0227  0.0453  0.0092  140 GLY C CA  
3317 C C   . GLY C 123 ? 0.1884 0.2866 0.1468 0.0757  0.0428  0.0226  140 GLY C C   
3318 O O   . GLY C 123 ? 0.1957 0.2863 0.1597 0.0531  0.0168  0.0252  140 GLY C O   
3319 N N   . SER C 124 ? 0.1759 0.3285 0.1364 0.0326  0.0370  0.0318  141 SER C N   
3320 C CA  . SER C 124 ? 0.1851 0.3111 0.1457 0.0624  0.0384  0.0360  141 SER C CA  
3321 C C   . SER C 124 ? 0.1941 0.3243 0.1665 0.0558  0.0428  0.0323  141 SER C C   
3322 O O   . SER C 124 ? 0.2313 0.3171 0.1765 0.0316  0.0349  -0.0128 141 SER C O   
3323 C CB  . SER C 124 ? 0.1948 0.3394 0.1464 0.0422  0.0333  0.0146  141 SER C CB  
3324 O OG  . SER C 124 ? 0.2033 0.3155 0.1436 -0.0045 0.0127  -0.0109 141 SER C OG  
3325 N N   . ASP C 125 ? 0.1661 0.3522 0.1637 -0.0321 0.0369  0.0202  142 ASP C N   
3326 C CA  . ASP C 125 ? 0.1978 0.3842 0.1607 -0.0044 0.0033  -0.0123 142 ASP C CA  
3327 C C   . ASP C 125 ? 0.1579 0.4334 0.1599 0.0142  0.0317  0.0252  142 ASP C C   
3328 O O   . ASP C 125 ? 0.1917 0.4875 0.1790 -0.0219 0.0249  -0.0198 142 ASP C O   
3329 C CB  . ASP C 125 ? 0.2628 0.5249 0.1806 0.0514  0.0009  0.0220  142 ASP C CB  
3330 C CG  . ASP C 125 ? 0.2983 0.5730 0.1865 0.1503  -0.0183 0.0471  142 ASP C CG  
3331 O OD1 . ASP C 125 ? 0.3445 0.5779 0.1845 0.1618  0.0007  0.0419  142 ASP C OD1 
3332 O OD2 . ASP C 125 ? 0.3932 0.5383 0.1985 0.1748  -0.0163 0.0496  142 ASP C OD2 
3333 N N   . SER C 126 ? 0.1459 0.3095 0.1543 0.0031  0.0139  0.0019  143 SER C N   
3334 C CA  . SER C 126 ? 0.1773 0.3034 0.1572 -0.0211 0.0173  0.0112  143 SER C CA  
3335 C C   . SER C 126 ? 0.1685 0.2904 0.1580 -0.0041 0.0207  -0.0306 143 SER C C   
3336 O O   . SER C 126 ? 0.2217 0.2505 0.1705 -0.0356 0.0366  0.0103  143 SER C O   
3337 C CB  . SER C 126 ? 0.2405 0.2850 0.1573 -0.0368 0.0327  0.0297  143 SER C CB  
3338 O OG  . SER C 126 ? 0.2413 0.2760 0.1574 -0.0007 0.0333  0.0193  143 SER C OG  
3339 N N   . ALA C 127 ? 0.2070 0.3190 0.1679 -0.0160 0.0450  0.0103  144 ALA C N   
3340 C CA  . ALA C 127 ? 0.2090 0.2624 0.1577 0.0083  0.0382  -0.0070 144 ALA C CA  
3341 C C   . ALA C 127 ? 0.1835 0.2587 0.1494 -0.0180 0.0434  0.0183  144 ALA C C   
3342 O O   . ALA C 127 ? 0.1962 0.3224 0.1490 -0.0048 0.0186  -0.0069 144 ALA C O   
3343 C CB  . ALA C 127 ? 0.2216 0.2719 0.1686 -0.0064 0.0218  0.0200  144 ALA C CB  
3344 N N   . GLU C 128 ? 0.2101 0.2839 0.1520 -0.0077 0.0354  0.0435  145 GLU C N   
3345 C CA  . GLU C 128 ? 0.1846 0.2658 0.1564 0.0186  0.0241  0.0216  145 GLU C CA  
3346 C C   . GLU C 128 ? 0.1474 0.2530 0.1609 -0.0168 0.0194  0.0238  145 GLU C C   
3347 O O   . GLU C 128 ? 0.2120 0.3006 0.1651 -0.0068 0.0052  0.0000  145 GLU C O   
3348 C CB  . GLU C 128 ? 0.2527 0.2338 0.1673 -0.0087 0.0129  0.0211  145 GLU C CB  
3349 C CG  . GLU C 128 ? 0.3076 0.3000 0.1798 -0.0297 0.0156  -0.0177 145 GLU C CG  
3350 C CD  . GLU C 128 ? 0.3242 0.3400 0.1966 -0.0034 0.0098  -0.0124 145 GLU C CD  
3351 O OE1 . GLU C 128 ? 0.2771 0.3913 0.2142 -0.0308 0.0290  0.0048  145 GLU C OE1 
3352 O OE2 . GLU C 128 ? 0.4297 0.3454 0.2093 -0.0080 0.0208  -0.0316 145 GLU C OE2 
3353 N N   . SER C 129 ? 0.2002 0.3106 0.1728 -0.0120 0.0222  0.0284  146 SER C N   
3354 C CA  A SER C 129 ? 0.1973 0.2904 0.1775 0.0062  0.0271  0.0377  146 SER C CA  
3355 C CA  B SER C 129 ? 0.2401 0.2929 0.1762 -0.0182 0.0377  0.0413  146 SER C CA  
3356 C C   . SER C 129 ? 0.2217 0.2537 0.1721 -0.0056 0.0334  0.0334  146 SER C C   
3357 O O   . SER C 129 ? 0.2170 0.2202 0.1778 0.0326  0.0194  -0.0023 146 SER C O   
3358 C CB  A SER C 129 ? 0.1610 0.2667 0.1813 0.0089  0.0222  0.0486  146 SER C CB  
3359 C CB  B SER C 129 ? 0.3062 0.3322 0.1761 0.0026  0.0419  0.0467  146 SER C CB  
3360 O OG  A SER C 129 ? 0.1073 0.2947 0.1915 -0.0044 0.0139  0.0350  146 SER C OG  
3361 O OG  B SER C 129 ? 0.3540 0.4125 0.1797 0.0306  0.0418  0.0332  146 SER C OG  
3362 N N   . ALA C 130 ? 0.2067 0.2710 0.1572 -0.0090 0.0490  0.0371  147 ALA C N   
3363 C CA  . ALA C 130 ? 0.2079 0.2353 0.1645 0.0067  0.0237  0.0220  147 ALA C CA  
3364 C C   . ALA C 130 ? 0.2044 0.2446 0.1725 0.0178  0.0339  0.0358  147 ALA C C   
3365 O O   . ALA C 130 ? 0.2021 0.2817 0.1701 0.0162  0.0066  0.0181  147 ALA C O   
3366 C CB  . ALA C 130 ? 0.1940 0.2421 0.1645 0.0477  0.0278  0.0080  147 ALA C CB  
3367 N N   . LYS C 131 ? 0.1821 0.2710 0.1791 0.0060  0.0251  0.0355  148 LYS C N   
3368 C CA  . LYS C 131 ? 0.1639 0.3192 0.1902 -0.0242 0.0386  0.0074  148 LYS C CA  
3369 C C   . LYS C 131 ? 0.1726 0.2897 0.1792 -0.0268 0.0329  0.0149  148 LYS C C   
3370 O O   . LYS C 131 ? 0.1782 0.3545 0.1819 0.0088  -0.0034 -0.0204 148 LYS C O   
3371 C CB  . LYS C 131 ? 0.2094 0.4394 0.2064 -0.0403 0.0442  -0.0339 148 LYS C CB  
3372 C CG  . LYS C 131 ? 0.4014 0.7252 0.2304 0.1383  0.0556  -0.0419 148 LYS C CG  
3373 C CD  . LYS C 131 ? 0.4865 0.9733 0.2860 0.2411  0.0223  -0.0520 148 LYS C CD  
3374 C CE  . LYS C 131 ? 0.4824 1.0932 0.3066 0.2080  0.0172  -0.0684 148 LYS C CE  
3375 N NZ  . LYS C 131 ? 0.5548 1.1365 0.3154 0.1967  0.0154  -0.0797 148 LYS C NZ  
3376 N N   . ARG C 132 ? 0.1924 0.2585 0.1795 -0.0034 0.0262  0.0420  149 ARG C N   
3377 C CA  . ARG C 132 ? 0.1927 0.2709 0.1827 -0.0240 0.0501  0.0601  149 ARG C CA  
3378 C C   . ARG C 132 ? 0.1687 0.2712 0.1831 -0.0178 0.0389  0.0180  149 ARG C C   
3379 O O   . ARG C 132 ? 0.2389 0.2886 0.1964 -0.0268 0.0223  -0.0174 149 ARG C O   
3380 C CB  . ARG C 132 ? 0.1917 0.3221 0.1979 -0.0262 0.0622  0.0959  149 ARG C CB  
3381 C CG  . ARG C 132 ? 0.3381 0.2867 0.2203 -0.0044 0.0542  0.0998  149 ARG C CG  
3382 C CD  . ARG C 132 ? 0.4474 0.3428 0.2437 0.1075  0.0543  0.0925  149 ARG C CD  
3383 N NE  . ARG C 132 ? 0.5204 0.4772 0.2770 0.2487  0.0523  0.0788  149 ARG C NE  
3384 C CZ  . ARG C 132 ? 0.5746 0.6412 0.3046 0.3359  0.0448  0.0549  149 ARG C CZ  
3385 N NH1 . ARG C 132 ? 0.5462 0.5743 0.3085 0.2586  0.0312  0.0482  149 ARG C NH1 
3386 N NH2 . ARG C 132 ? 0.6102 0.7301 0.3190 0.3954  0.0355  0.0449  149 ARG C NH2 
3387 N N   . GLU C 133 ? 0.1565 0.2622 0.1780 -0.0159 0.0170  0.0176  150 GLU C N   
3388 C CA  . GLU C 133 ? 0.1483 0.2883 0.1758 0.0051  0.0300  0.0204  150 GLU C CA  
3389 C C   . GLU C 133 ? 0.1888 0.2482 0.1797 -0.0148 0.0223  0.0270  150 GLU C C   
3390 O O   . GLU C 133 ? 0.1799 0.2829 0.1865 0.0300  0.0104  -0.0034 150 GLU C O   
3391 C CB  . GLU C 133 ? 0.1805 0.2452 0.1722 0.0175  0.0216  -0.0082 150 GLU C CB  
3392 C CG  . GLU C 133 ? 0.2056 0.3137 0.1696 0.0133  0.0137  0.0094  150 GLU C CG  
3393 C CD  . GLU C 133 ? 0.2046 0.3302 0.1758 -0.0133 0.0206  0.0481  150 GLU C CD  
3394 O OE1 . GLU C 133 ? 0.2067 0.3501 0.1804 -0.0161 0.0236  0.0235  150 GLU C OE1 
3395 O OE2 . GLU C 133 ? 0.2616 0.3611 0.1800 0.0067  -0.0007 0.0286  150 GLU C OE2 
3396 N N   . ILE C 134 ? 0.1966 0.2555 0.1779 -0.0183 0.0098  0.0439  151 ILE C N   
3397 C CA  . ILE C 134 ? 0.2076 0.2666 0.1857 0.0111  0.0058  0.0556  151 ILE C CA  
3398 C C   . ILE C 134 ? 0.1737 0.2941 0.1931 -0.0212 -0.0110 0.0284  151 ILE C C   
3399 O O   . ILE C 134 ? 0.2464 0.3049 0.1886 -0.0211 -0.0344 0.0125  151 ILE C O   
3400 C CB  . ILE C 134 ? 0.1627 0.2867 0.1862 0.0129  -0.0097 0.0262  151 ILE C CB  
3401 C CG1 . ILE C 134 ? 0.1890 0.2513 0.1976 -0.0205 0.0191  0.0441  151 ILE C CG1 
3402 C CG2 . ILE C 134 ? 0.1816 0.2839 0.1903 0.0255  -0.0241 0.0151  151 ILE C CG2 
3403 C CD1 . ILE C 134 ? 0.2135 0.2415 0.2020 -0.0087 0.0135  0.0520  151 ILE C CD1 
3404 N N   . SER C 135 ? 0.1814 0.3180 0.1990 0.0349  0.0052  0.0214  152 SER C N   
3405 C CA  . SER C 135 ? 0.1806 0.3256 0.2327 -0.0184 0.0005  -0.0081 152 SER C CA  
3406 C C   . SER C 135 ? 0.1561 0.3299 0.2289 -0.0635 -0.0166 -0.0316 152 SER C C   
3407 O O   . SER C 135 ? 0.1892 0.3405 0.2341 -0.0250 -0.0387 -0.0294 152 SER C O   
3408 C CB  . SER C 135 ? 0.2371 0.4450 0.2726 0.0225  0.0299  -0.0243 152 SER C CB  
3409 O OG  . SER C 135 ? 0.2972 0.5990 0.3007 0.0131  0.0134  -0.0216 152 SER C OG  
3410 N N   . LEU C 136 ? 0.1756 0.3494 0.2180 -0.0460 0.0143  0.0010  153 LEU C N   
3411 C CA  . LEU C 136 ? 0.1969 0.3109 0.2109 -0.0377 -0.0035 -0.0097 153 LEU C CA  
3412 C C   . LEU C 136 ? 0.1992 0.2646 0.2064 -0.0382 0.0213  -0.0024 153 LEU C C   
3413 O O   . LEU C 136 ? 0.2498 0.2975 0.2091 -0.0345 -0.0046 -0.0263 153 LEU C O   
3414 C CB  . LEU C 136 ? 0.2450 0.2942 0.2202 -0.0284 -0.0079 -0.0112 153 LEU C CB  
3415 C CG  . LEU C 136 ? 0.2113 0.3204 0.2331 -0.0282 0.0121  0.0024  153 LEU C CG  
3416 C CD1 . LEU C 136 ? 0.2365 0.4228 0.2461 -0.0095 0.0027  -0.0044 153 LEU C CD1 
3417 C CD2 . LEU C 136 ? 0.2273 0.3344 0.2389 0.0084  0.0009  0.0404  153 LEU C CD2 
3418 N N   . TRP C 137 ? 0.2160 0.2512 0.2058 -0.0018 0.0248  -0.0100 154 TRP C N   
3419 C CA  . TRP C 137 ? 0.1737 0.2631 0.2099 0.0265  0.0217  0.0125  154 TRP C CA  
3420 C C   . TRP C 137 ? 0.2199 0.2438 0.2052 0.0299  0.0091  -0.0172 154 TRP C C   
3421 O O   . TRP C 137 ? 0.2487 0.2567 0.1977 0.0251  0.0062  -0.0091 154 TRP C O   
3422 C CB  . TRP C 137 ? 0.2018 0.2785 0.2092 0.0428  0.0216  0.0130  154 TRP C CB  
3423 C CG  . TRP C 137 ? 0.1730 0.2835 0.2034 0.0312  0.0421  0.0182  154 TRP C CG  
3424 C CD1 . TRP C 137 ? 0.1929 0.2586 0.1983 -0.0007 0.0474  0.0290  154 TRP C CD1 
3425 C CD2 . TRP C 137 ? 0.1932 0.2268 0.2029 -0.0087 0.0393  -0.0006 154 TRP C CD2 
3426 N NE1 . TRP C 137 ? 0.2275 0.2595 0.1967 0.0520  0.0303  0.0141  154 TRP C NE1 
3427 C CE2 . TRP C 137 ? 0.1896 0.2316 0.2008 0.0376  0.0425  0.0169  154 TRP C CE2 
3428 C CE3 . TRP C 137 ? 0.2663 0.2382 0.2062 0.0000  0.0457  0.0090  154 TRP C CE3 
3429 C CZ2 . TRP C 137 ? 0.1898 0.2663 0.2014 0.0089  0.0261  -0.0039 154 TRP C CZ2 
3430 C CZ3 . TRP C 137 ? 0.3212 0.2393 0.2099 0.0397  0.0575  0.0163  154 TRP C CZ3 
3431 C CH2 . TRP C 137 ? 0.2399 0.2463 0.2012 0.0239  0.0471  -0.0026 154 TRP C CH2 
3432 N N   . PHE C 138 ? 0.1908 0.2712 0.2120 0.0211  0.0148  0.0108  155 PHE C N   
3433 C CA  . PHE C 138 ? 0.2073 0.3193 0.2213 0.0495  -0.0026 -0.0049 155 PHE C CA  
3434 C C   . PHE C 138 ? 0.1789 0.3795 0.2388 0.0260  0.0025  0.0033  155 PHE C C   
3435 O O   . PHE C 138 ? 0.1578 0.4913 0.2338 -0.0107 0.0150  -0.0053 155 PHE C O   
3436 C CB  . PHE C 138 ? 0.2131 0.2437 0.2191 0.0097  0.0142  -0.0033 155 PHE C CB  
3437 C CG  . PHE C 138 ? 0.1629 0.2759 0.2108 0.0150  0.0083  -0.0003 155 PHE C CG  
3438 C CD1 . PHE C 138 ? 0.1767 0.3061 0.2040 0.0261  0.0086  0.0134  155 PHE C CD1 
3439 C CD2 . PHE C 138 ? 0.1865 0.3047 0.2080 0.0647  0.0148  0.0094  155 PHE C CD2 
3440 C CE1 . PHE C 138 ? 0.2056 0.2612 0.1956 0.0478  -0.0120 0.0136  155 PHE C CE1 
3441 C CE2 . PHE C 138 ? 0.1615 0.3280 0.2016 0.0661  0.0010  0.0112  155 PHE C CE2 
3442 C CZ  . PHE C 138 ? 0.2091 0.2476 0.1996 0.0385  -0.0044 0.0107  155 PHE C CZ  
3443 N N   . LYS C 139 ? 0.1909 0.3581 0.2509 -0.0351 -0.0091 0.0140  156 LYS C N   
3444 C CA  . LYS C 139 ? 0.2065 0.2898 0.2824 -0.0963 -0.0152 0.0031  156 LYS C CA  
3445 C C   . LYS C 139 ? 0.1827 0.2929 0.2784 -0.0324 -0.0057 0.0244  156 LYS C C   
3446 O O   . LYS C 139 ? 0.2055 0.2621 0.2645 0.0019  -0.0307 0.0112  156 LYS C O   
3447 C CB  . LYS C 139 ? 0.2856 0.3924 0.3098 -0.0818 -0.0522 -0.0020 156 LYS C CB  
3448 C CG  . LYS C 139 ? 0.5334 0.4169 0.3436 -0.0153 -0.0772 -0.0157 156 LYS C CG  
3449 C CD  . LYS C 139 ? 0.8264 0.5453 0.3714 0.1802  -0.0754 -0.0109 156 LYS C CD  
3450 C CE  . LYS C 139 ? 1.0452 0.6934 0.3888 0.3342  -0.0638 0.0071  156 LYS C CE  
3451 N NZ  . LYS C 139 ? 1.1702 0.7687 0.3994 0.4215  -0.0656 0.0234  156 LYS C NZ  
3452 N N   . PRO C 140 ? 0.1626 0.3026 0.2944 0.0276  0.0289  0.0617  157 PRO C N   
3453 C CA  . PRO C 140 ? 0.1987 0.2963 0.3017 0.0014  0.0426  0.0759  157 PRO C CA  
3454 C C   . PRO C 140 ? 0.1887 0.3160 0.3070 -0.0116 0.0228  0.0656  157 PRO C C   
3455 O O   . PRO C 140 ? 0.2030 0.3536 0.3161 0.0360  0.0269  0.0266  157 PRO C O   
3456 C CB  . PRO C 140 ? 0.2452 0.4583 0.3046 0.0379  0.0671  0.0938  157 PRO C CB  
3457 C CG  . PRO C 140 ? 0.3505 0.5074 0.3066 0.0977  0.0630  0.0814  157 PRO C CG  
3458 C CD  . PRO C 140 ? 0.2188 0.4459 0.3046 0.0105  0.0610  0.0839  157 PRO C CD  
3459 N N   . GLU C 141 ? 0.1921 0.3046 0.3036 -0.0425 -0.0160 0.0686  158 GLU C N   
3460 C CA  . GLU C 141 ? 0.2127 0.3219 0.2957 -0.0205 -0.0351 0.0630  158 GLU C CA  
3461 C C   . GLU C 141 ? 0.1916 0.3749 0.2694 0.0078  -0.0278 0.0415  158 GLU C C   
3462 O O   . GLU C 141 ? 0.2130 0.3812 0.2670 0.0329  -0.0447 0.0175  158 GLU C O   
3463 C CB  . GLU C 141 ? 0.2840 0.3933 0.3274 -0.0938 -0.0824 0.0755  158 GLU C CB  
3464 C CG  . GLU C 141 ? 0.4238 0.5575 0.3526 -0.0240 -0.1202 0.0624  158 GLU C CG  
3465 C CD  . GLU C 141 ? 0.5219 0.6900 0.3795 -0.0303 -0.1314 0.0682  158 GLU C CD  
3466 O OE1 . GLU C 141 ? 0.3848 0.6743 0.3945 -0.1197 -0.1418 0.0845  158 GLU C OE1 
3467 O OE2 . GLU C 141 ? 0.6596 0.6799 0.3905 -0.0498 -0.1303 0.0613  158 GLU C OE2 
3468 N N   . GLU C 142 ? 0.1756 0.2897 0.2466 -0.0359 -0.0331 0.0463  159 GLU C N   
3469 C CA  . GLU C 142 ? 0.1375 0.3493 0.2327 0.0120  -0.0356 0.0251  159 GLU C CA  
3470 C C   . GLU C 142 ? 0.1617 0.3123 0.2236 0.0226  -0.0107 0.0064  159 GLU C C   
3471 O O   . GLU C 142 ? 0.2021 0.2975 0.2077 0.0302  0.0101  0.0221  159 GLU C O   
3472 C CB  . GLU C 142 ? 0.2056 0.3027 0.2369 0.0019  -0.0016 0.0162  159 GLU C CB  
3473 C CG  . GLU C 142 ? 0.2703 0.2798 0.2539 -0.0244 0.0072  -0.0101 159 GLU C CG  
3474 C CD  . GLU C 142 ? 0.4194 0.2636 0.2746 0.0108  0.0310  0.0000  159 GLU C CD  
3475 O OE1 . GLU C 142 ? 0.3715 0.3661 0.2827 0.0587  -0.0419 -0.0437 159 GLU C OE1 
3476 O OE2 . GLU C 142 ? 0.6025 0.4621 0.3029 0.1766  0.0432  -0.0098 159 GLU C OE2 
3477 N N   . ILE C 143 ? 0.1455 0.3111 0.2304 0.0139  -0.0006 0.0275  160 ILE C N   
3478 C CA  . ILE C 143 ? 0.1611 0.2911 0.2328 -0.0184 -0.0110 0.0292  160 ILE C CA  
3479 C C   . ILE C 143 ? 0.1346 0.2634 0.2467 -0.0212 -0.0169 0.0321  160 ILE C C   
3480 O O   . ILE C 143 ? 0.1778 0.3011 0.2766 0.0168  0.0182  0.0501  160 ILE C O   
3481 C CB  . ILE C 143 ? 0.1877 0.2894 0.2325 0.0039  0.0009  0.0442  160 ILE C CB  
3482 C CG1 . ILE C 143 ? 0.2362 0.2974 0.2487 0.0175  -0.0206 0.0268  160 ILE C CG1 
3483 C CG2 . ILE C 143 ? 0.2437 0.2755 0.2271 -0.0293 0.0036  0.0304  160 ILE C CG2 
3484 C CD1 . ILE C 143 ? 0.3481 0.3764 0.2600 0.0511  -0.0103 0.0511  160 ILE C CD1 
3485 N N   . GLN C 144 ? 0.1398 0.2522 0.2352 -0.0038 -0.0048 0.0513  161 GLN C N   
3486 C CA  . GLN C 144 ? 0.1732 0.2385 0.2335 0.0189  0.0011  0.0460  161 GLN C CA  
3487 C C   . GLN C 144 ? 0.1785 0.2628 0.2237 -0.0101 -0.0171 -0.0115 161 GLN C C   
3488 O O   . GLN C 144 ? 0.1838 0.3168 0.2468 0.0301  -0.0060 -0.0196 161 GLN C O   
3489 C CB  . GLN C 144 ? 0.1531 0.2661 0.2396 -0.0277 0.0138  0.0333  161 GLN C CB  
3490 C CG  . GLN C 144 ? 0.1936 0.2751 0.2350 -0.0393 0.0250  0.0215  161 GLN C CG  
3491 C CD  . GLN C 144 ? 0.2291 0.2917 0.2238 -0.0273 -0.0002 0.0146  161 GLN C CD  
3492 O OE1 . GLN C 144 ? 0.2432 0.3690 0.2255 0.0481  -0.0117 0.0297  161 GLN C OE1 
3493 N NE2 . GLN C 144 ? 0.2154 0.3443 0.2227 0.0200  0.0024  0.0257  161 GLN C NE2 
3494 N N   . SER C 145 ? 0.1822 0.2881 0.2008 0.0113  0.0160  0.0133  162 SER C N   
3495 C CA  A SER C 145 ? 0.1734 0.3008 0.2033 0.0517  0.0238  0.0050  162 SER C CA  
3496 C CA  B SER C 145 ? 0.1643 0.2895 0.1953 0.0481  0.0141  0.0048  162 SER C CA  
3497 C C   . SER C 145 ? 0.1558 0.2747 0.1987 -0.0020 0.0020  0.0170  162 SER C C   
3498 O O   . SER C 145 ? 0.2074 0.3440 0.2218 0.0125  -0.0049 -0.0075 162 SER C O   
3499 C CB  A SER C 145 ? 0.2334 0.3632 0.2179 0.0061  0.0397  -0.0259 162 SER C CB  
3500 C CB  B SER C 145 ? 0.1833 0.3323 0.1906 0.0582  0.0187  -0.0199 162 SER C CB  
3501 O OG  A SER C 145 ? 0.3179 0.3312 0.2268 0.0221  0.0338  -0.0476 162 SER C OG  
3502 O OG  B SER C 145 ? 0.1909 0.3522 0.1827 0.0933  0.0041  -0.0457 162 SER C OG  
3503 N N   . TYR C 146 ? 0.1560 0.2789 0.1891 0.0234  -0.0052 0.0383  163 TYR C N   
3504 C CA  . TYR C 146 ? 0.1507 0.3458 0.1813 0.0293  0.0036  0.0153  163 TYR C CA  
3505 C C   . TYR C 146 ? 0.1544 0.2949 0.1958 0.0101  0.0051  0.0069  163 TYR C C   
3506 O O   . TYR C 146 ? 0.1977 0.2867 0.1974 0.0341  -0.0120 -0.0104 163 TYR C O   
3507 C CB  . TYR C 146 ? 0.1731 0.3309 0.1697 0.0256  0.0126  0.0232  163 TYR C CB  
3508 C CG  . TYR C 146 ? 0.1636 0.2659 0.1648 0.0231  0.0224  0.0485  163 TYR C CG  
3509 C CD1 . TYR C 146 ? 0.1835 0.2695 0.1558 0.0259  -0.0177 0.0298  163 TYR C CD1 
3510 C CD2 . TYR C 146 ? 0.1735 0.2818 0.1645 0.0548  0.0368  0.0433  163 TYR C CD2 
3511 C CE1 . TYR C 146 ? 0.1741 0.2526 0.1554 0.0246  0.0127  0.0046  163 TYR C CE1 
3512 C CE2 . TYR C 146 ? 0.1761 0.2675 0.1781 0.0096  0.0279  0.0099  163 TYR C CE2 
3513 C CZ  . TYR C 146 ? 0.1721 0.2609 0.1634 0.0341  0.0406  0.0346  163 TYR C CZ  
3514 O OH  . TYR C 146 ? 0.1876 0.2550 0.1684 0.0205  0.0336  0.0118  163 TYR C OH  
3515 N N   . LYS C 147 ? 0.1903 0.2623 0.2025 0.0271  0.0217  0.0188  164 LYS C N   
3516 C CA  . LYS C 147 ? 0.1523 0.2973 0.2161 -0.0020 0.0187  -0.0022 164 LYS C CA  
3517 C C   . LYS C 147 ? 0.1389 0.2898 0.1898 -0.0053 0.0215  -0.0083 164 LYS C C   
3518 O O   . LYS C 147 ? 0.2091 0.3177 0.1668 -0.0080 0.0143  -0.0115 164 LYS C O   
3519 C CB  . LYS C 147 ? 0.2770 0.3815 0.2515 0.0828  0.0365  0.0002  164 LYS C CB  
3520 C CG  . LYS C 147 ? 0.3630 0.5351 0.2910 0.1772  0.0032  -0.0110 164 LYS C CG  
3521 C CD  . LYS C 147 ? 0.5092 0.6869 0.3293 0.2328  -0.0087 -0.0256 164 LYS C CD  
3522 C CE  . LYS C 147 ? 0.5737 0.8190 0.3501 0.2940  -0.0083 -0.0389 164 LYS C CE  
3523 N NZ  . LYS C 147 ? 0.6256 0.9276 0.3656 0.3171  0.0074  -0.0215 164 LYS C NZ  
3524 N N   . LEU C 148 ? 0.1437 0.3074 0.2020 0.0117  0.0333  0.0189  165 LEU C N   
3525 C CA  . LEU C 148 ? 0.1594 0.2979 0.2072 0.0181  0.0183  0.0101  165 LEU C CA  
3526 C C   . LEU C 148 ? 0.1657 0.2327 0.2030 0.0278  0.0068  -0.0035 165 LEU C C   
3527 O O   . LEU C 148 ? 0.2147 0.2280 0.2044 0.0284  -0.0052 -0.0290 165 LEU C O   
3528 C CB  . LEU C 148 ? 0.1823 0.2913 0.2122 0.0601  0.0180  0.0254  165 LEU C CB  
3529 C CG  . LEU C 148 ? 0.2078 0.2990 0.2207 0.0457  0.0314  0.0427  165 LEU C CG  
3530 C CD1 . LEU C 148 ? 0.2013 0.3791 0.2136 0.0459  0.0414  0.0778  165 LEU C CD1 
3531 C CD2 . LEU C 148 ? 0.2458 0.2828 0.2381 0.1036  0.0260  0.0454  165 LEU C CD2 
3532 N N   . ALA C 149 ? 0.2028 0.2581 0.2017 0.0148  0.0013  -0.0007 166 ALA C N   
3533 C CA  . ALA C 149 ? 0.2340 0.2612 0.2051 -0.0160 -0.0088 -0.0076 166 ALA C CA  
3534 C C   . ALA C 149 ? 0.2543 0.2484 0.2065 0.0450  -0.0177 0.0043  166 ALA C C   
3535 O O   . ALA C 149 ? 0.2844 0.2775 0.2148 0.0590  0.0060  0.0128  166 ALA C O   
3536 C CB  . ALA C 149 ? 0.3176 0.3962 0.2075 -0.0453 0.0112  -0.0051 166 ALA C CB  
3537 N N   . LEU C 150 ? 0.1979 0.2726 0.2033 0.0235  0.0214  0.0223  167 LEU C N   
3538 C CA  . LEU C 150 ? 0.1796 0.3257 0.1970 0.0426  0.0112  0.0076  167 LEU C CA  
3539 C C   . LEU C 150 ? 0.1969 0.2547 0.1876 0.0737  -0.0085 0.0126  167 LEU C C   
3540 O O   . LEU C 150 ? 0.1971 0.2638 0.1947 0.0327  -0.0010 0.0194  167 LEU C O   
3541 C CB  . LEU C 150 ? 0.1927 0.4438 0.2036 0.0506  0.0222  -0.0404 167 LEU C CB  
3542 C CG  . LEU C 150 ? 0.2585 0.5682 0.2199 0.0776  0.0350  -0.0473 167 LEU C CG  
3543 C CD1 . LEU C 150 ? 0.3066 0.6727 0.2304 0.0968  0.0186  -0.1078 167 LEU C CD1 
3544 C CD2 . LEU C 150 ? 0.3476 0.5839 0.2274 -0.0090 0.0499  -0.0120 167 LEU C CD2 
3545 N N   . SER C 151 ? 0.2217 0.3168 0.1848 0.0581  -0.0076 -0.0163 168 SER C N   
3546 C CA  A SER C 151 ? 0.2426 0.3596 0.1911 0.0289  0.0155  -0.0017 168 SER C CA  
3547 C CA  B SER C 151 ? 0.2369 0.3185 0.1912 0.0389  0.0206  -0.0005 168 SER C CA  
3548 C C   . SER C 151 ? 0.2478 0.3266 0.2013 0.0822  0.0177  0.0115  168 SER C C   
3549 O O   . SER C 151 ? 0.2161 0.3210 0.1970 0.0426  0.0142  -0.0070 168 SER C O   
3550 C CB  A SER C 151 ? 0.2855 0.4094 0.1920 -0.0087 0.0351  0.0063  168 SER C CB  
3551 C CB  B SER C 151 ? 0.2795 0.2268 0.1952 0.0133  0.0481  0.0094  168 SER C CB  
3552 O OG  A SER C 151 ? 0.2976 0.4898 0.1958 -0.0005 0.0291  0.0066  168 SER C OG  
3553 O OG  B SER C 151 ? 0.2633 0.2570 0.2052 0.0382  0.0467  0.0134  168 SER C OG  
3554 N N   . ASP C 152 ? 0.1994 0.3017 0.2252 0.0666  0.0097  0.0212  169 ASP C N   
3555 C CA  . ASP C 152 ? 0.2325 0.3172 0.2469 0.0608  0.0169  0.0283  169 ASP C CA  
3556 C C   . ASP C 152 ? 0.2475 0.3028 0.2325 0.0645  -0.0049 0.0124  169 ASP C C   
3557 O O   . ASP C 152 ? 0.2307 0.3064 0.2590 0.0751  0.0179  -0.0223 169 ASP C O   
3558 C CB  . ASP C 152 ? 0.2995 0.3927 0.2853 0.1268  -0.0213 0.0151  169 ASP C CB  
3559 C CG  . ASP C 152 ? 0.3242 0.5604 0.3171 0.1035  -0.0207 0.0264  169 ASP C CG  
3560 O OD1 . ASP C 152 ? 0.2777 0.5706 0.3302 0.1091  -0.0037 0.0060  169 ASP C OD1 
3561 O OD2 . ASP C 152 ? 0.3652 0.6445 0.3437 0.1212  -0.0302 0.0507  169 ASP C OD2 
3562 N N   . TYR C 153 ? 0.2078 0.2659 0.2055 0.0462  -0.0080 0.0104  170 TYR C N   
3563 C CA  . TYR C 153 ? 0.2353 0.2010 0.1968 0.0263  0.0217  0.0134  170 TYR C CA  
3564 C C   . TYR C 153 ? 0.1895 0.2377 0.2049 0.0364  0.0077  0.0425  170 TYR C C   
3565 O O   . TYR C 153 ? 0.2212 0.2734 0.2123 -0.0028 -0.0091 0.0506  170 TYR C O   
3566 C CB  . TYR C 153 ? 0.2148 0.2201 0.1893 0.0260  0.0373  0.0255  170 TYR C CB  
3567 C CG  . TYR C 153 ? 0.1976 0.2480 0.1837 0.0538  0.0248  0.0237  170 TYR C CG  
3568 C CD1 . TYR C 153 ? 0.2228 0.2304 0.1821 0.0427  0.0374  0.0163  170 TYR C CD1 
3569 C CD2 . TYR C 153 ? 0.1863 0.3155 0.1900 0.0672  -0.0141 0.0195  170 TYR C CD2 
3570 C CE1 . TYR C 153 ? 0.2399 0.2692 0.1864 0.0482  0.0028  0.0132  170 TYR C CE1 
3571 C CE2 . TYR C 153 ? 0.3176 0.3463 0.1960 0.0949  -0.0051 0.0333  170 TYR C CE2 
3572 C CZ  . TYR C 153 ? 0.2785 0.3489 0.1968 0.0954  -0.0193 0.0264  170 TYR C CZ  
3573 O OH  . TYR C 153 ? 0.3478 0.3872 0.2178 0.0827  -0.0299 0.0549  170 TYR C OH  
3574 N N   . ILE C 154 ? 0.2489 0.2617 0.2082 0.0605  -0.0016 0.0483  171 ILE C N   
3575 C CA  . ILE C 154 ? 0.2316 0.2838 0.2067 0.0402  0.0228  0.0634  171 ILE C CA  
3576 C C   . ILE C 154 ? 0.2235 0.3064 0.2222 0.0242  -0.0055 0.0244  171 ILE C C   
3577 O O   . ILE C 154 ? 0.2381 0.3625 0.2236 0.0368  0.0004  0.0258  171 ILE C O   
3578 C CB  . ILE C 154 ? 0.2767 0.2804 0.1980 0.0656  0.0263  0.0194  171 ILE C CB  
3579 C CG1 . ILE C 154 ? 0.2572 0.2997 0.2090 0.0433  0.0084  0.0171  171 ILE C CG1 
3580 C CG2 . ILE C 154 ? 0.2310 0.2635 0.1979 0.0533  0.0287  0.0060  171 ILE C CG2 
3581 C CD1 . ILE C 154 ? 0.3384 0.2863 0.2226 0.1207  -0.0070 0.0047  171 ILE C CD1 
3582 N N   . PHE C 155 ? 0.1872 0.3047 0.2298 0.0389  0.0052  0.0086  172 PHE C N   
3583 C CA  . PHE C 155 ? 0.2263 0.3034 0.2417 0.0582  0.0141  0.0027  172 PHE C CA  
3584 C C   . PHE C 155 ? 0.3068 0.3000 0.2688 0.0470  0.0196  -0.0044 172 PHE C C   
3585 O O   . PHE C 155 ? 0.3963 0.3364 0.2675 0.0530  0.0131  0.0139  172 PHE C O   
3586 C CB  . PHE C 155 ? 0.2854 0.3036 0.2321 0.0974  0.0187  0.0289  172 PHE C CB  
3587 C CG  . PHE C 155 ? 0.2794 0.2785 0.2267 0.0904  0.0256  0.0126  172 PHE C CG  
3588 C CD1 . PHE C 155 ? 0.2526 0.2853 0.2185 0.0762  0.0072  0.0047  172 PHE C CD1 
3589 C CD2 . PHE C 155 ? 0.2466 0.3007 0.2246 0.0711  0.0065  -0.0212 172 PHE C CD2 
3590 C CE1 . PHE C 155 ? 0.2106 0.3082 0.2257 0.0240  0.0186  0.0085  172 PHE C CE1 
3591 C CE2 . PHE C 155 ? 0.3389 0.3131 0.2282 0.0634  -0.0141 -0.0238 172 PHE C CE2 
3592 C CZ  . PHE C 155 ? 0.2465 0.3419 0.2334 0.0353  0.0056  -0.0006 172 PHE C CZ  
3593 N N   . GLU C 156 ? 0.3274 0.3695 0.2932 0.0711  0.0573  -0.0006 173 GLU C N   
3594 C CA  . GLU C 156 ? 0.6513 0.4750 0.3406 0.2584  0.0425  -0.0074 173 GLU C CA  
3595 C C   . GLU C 156 ? 0.7052 0.5824 0.3758 0.3406  0.1026  -0.0082 173 GLU C C   
3596 O O   . GLU C 156 ? 0.7747 0.6114 0.4022 0.3614  0.1185  -0.0077 173 GLU C O   
3597 C CB  . GLU C 156 ? 0.7148 0.5282 0.3553 0.2597  0.0068  -0.0276 173 GLU C CB  
3598 C CG  . GLU C 156 ? 0.6187 0.5319 0.3637 0.2145  0.0337  -0.0178 173 GLU C CG  
3599 C CD  . GLU C 156 ? 0.5128 0.4335 0.3528 0.0177  0.0987  0.0204  173 GLU C CD  
3600 O OE1 . GLU C 156 ? 0.5389 0.5165 0.3793 -0.0881 0.0478  -0.0392 173 GLU C OE1 
3601 O OE2 . GLU C 156 ? 0.4452 0.4083 0.3423 0.0149  0.1372  0.0354  173 GLU C OE2 
3602 O OXT . GLU C 156 ? 0.7868 0.5753 0.3929 0.3673  0.1061  0.0090  173 GLU C OXT 
3603 C C1  A CIT D .   ? 0.4394 0.8358 0.5212 0.1146  -0.0479 -0.0666 201 CIT A C1  
3604 O O1  A CIT D .   ? 0.3977 0.8983 0.5231 0.2891  -0.0604 -0.0849 201 CIT A O1  
3605 O O2  A CIT D .   ? 0.4406 0.8895 0.5296 0.0949  -0.0358 -0.0558 201 CIT A O2  
3606 C C2  A CIT D .   ? 0.4612 0.6634 0.5049 0.0380  -0.0350 -0.0501 201 CIT A C2  
3607 C C3  A CIT D .   ? 0.5201 0.5296 0.4941 0.0673  -0.0256 -0.0439 201 CIT A C3  
3608 O O7  A CIT D .   ? 0.3349 0.5093 0.4783 0.0555  -0.0716 -0.0403 201 CIT A O7  
3609 C C4  A CIT D .   ? 0.6322 0.5199 0.5004 0.0620  0.0035  -0.0448 201 CIT A C4  
3610 C C5  A CIT D .   ? 0.7210 0.5351 0.5100 0.0551  0.0339  -0.0404 201 CIT A C5  
3611 O O3  A CIT D .   ? 0.8484 0.6135 0.5227 0.1318  0.0534  -0.0353 201 CIT A O3  
3612 O O4  A CIT D .   ? 0.6817 0.5843 0.5120 0.0304  0.0242  -0.0227 201 CIT A O4  
3613 C C6  A CIT D .   ? 0.6932 0.4940 0.4923 0.0626  -0.0291 -0.0348 201 CIT A C6  
3614 O O5  A CIT D .   ? 0.7414 0.3301 0.4797 -0.0500 -0.0396 -0.0401 201 CIT A O5  
3615 O O6  A CIT D .   ? 0.7435 0.5383 0.4982 0.1341  -0.0298 -0.0215 201 CIT A O6  
3616 C C1  A CIT E .   ? 0.5889 0.6581 0.4047 0.0914  -0.0054 -0.1694 201 CIT B C1  
3617 O O1  A CIT E .   ? 0.5631 0.4941 0.4000 0.0456  -0.0049 -0.1735 201 CIT B O1  
3618 O O2  A CIT E .   ? 0.5935 0.8035 0.4069 0.0464  -0.0052 -0.1732 201 CIT B O2  
3619 C C2  A CIT E .   ? 0.5574 0.5883 0.4033 0.0786  0.0005  -0.1528 201 CIT B C2  
3620 C C3  A CIT E .   ? 0.5356 0.4867 0.4076 0.0092  0.0175  -0.1088 201 CIT B C3  
3621 O O7  A CIT E .   ? 0.5853 0.2897 0.3991 0.0542  0.0516  -0.0994 201 CIT B O7  
3622 C C4  A CIT E .   ? 0.4555 0.5482 0.4103 0.0727  -0.0218 -0.1136 201 CIT B C4  
3623 C C5  A CIT E .   ? 0.5093 0.6193 0.4189 0.1467  -0.0426 -0.1048 201 CIT B C5  
3624 O O3  A CIT E .   ? 0.5647 0.6751 0.4290 0.1654  -0.0590 -0.0794 201 CIT B O3  
3625 O O4  A CIT E .   ? 0.5434 0.6010 0.4249 0.1399  -0.0551 -0.0906 201 CIT B O4  
3626 C C6  A CIT E .   ? 0.5511 0.5686 0.4180 -0.0920 0.0190  -0.1000 201 CIT B C6  
3627 O O5  A CIT E .   ? 0.4406 0.6499 0.4104 -0.1666 0.0306  -0.0845 201 CIT B O5  
3628 O O6  A CIT E .   ? 0.6516 0.5559 0.4346 -0.1051 0.0127  -0.0848 201 CIT B O6  
3629 C C1  A CIT F .   ? 0.7339 0.6610 0.5419 0.0077  0.0824  0.0866  201 CIT C C1  
3630 O O1  A CIT F .   ? 0.7173 0.6853 0.5393 -0.0520 0.0691  0.0703  201 CIT C O1  
3631 O O2  A CIT F .   ? 0.7735 0.6714 0.5489 -0.0327 0.0630  0.0748  201 CIT C O2  
3632 C C2  A CIT F .   ? 0.6571 0.6111 0.5338 0.0752  0.1101  0.1073  201 CIT C C2  
3633 C C3  A CIT F .   ? 0.5445 0.5656 0.5276 0.1209  0.1278  0.1297  201 CIT C C3  
3634 O O7  A CIT F .   ? 0.3757 0.4669 0.5157 -0.0454 0.1643  0.1658  201 CIT C O7  
3635 C C4  A CIT F .   ? 0.6117 0.5691 0.5317 0.1717  0.1086  0.1286  201 CIT C C4  
3636 C C5  A CIT F .   ? 0.6192 0.6420 0.5344 0.1467  0.1050  0.1337  201 CIT C C5  
3637 O O3  A CIT F .   ? 0.7177 0.7124 0.5394 0.2065  0.0885  0.1330  201 CIT C O3  
3638 O O4  A CIT F .   ? 0.5035 0.6315 0.5341 -0.0175 0.1232  0.1286  201 CIT C O4  
3639 C C6  A CIT F .   ? 0.6705 0.6717 0.5299 0.3003  0.1249  0.1100  201 CIT C C6  
3640 O O5  A CIT F .   ? 0.7179 0.6632 0.5160 0.4056  0.0896  0.1018  201 CIT C O5  
3641 O O6  A CIT F .   ? 0.6783 0.7757 0.5355 0.3328  0.1385  0.0965  201 CIT C O6  
# 
