data_9O9R
# 
_entry.id   9O9R 
# 
_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   9O9R         pdb_00009o9r 10.2210/pdb9o9r/pdb 
WWPDB D_1000295159 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9O9R 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-18 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu                    Scott    Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 isabelle.phan@seattlechildrens.org Isabelle Phan   ? 'principal investigator/group leader' 0000-0001-6873-3401 
4 julie.early@seattlechildrens.org   Julie    Early  ? 'principal investigator/group leader' 0000-0003-1224-2747 
5 peter.myler@seattlechildrens.org   Peter    Myler  ? 'principal investigator/group leader' 0000-0002-0056-0513 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Seattle Structural Genomics Center for Infectious Disease'          1 ? 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of nucleoside-diphosphate kinase Cryptosporidium parvum' 
_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 'SULFATE ION'                   96.063    11  ?       ? ? ? 
3 water       nat water                           18.015    574 ?       ? ? ? 
# 
_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 'SULFATE ION' SO4 
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 
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 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   18  ?   ?   ?   A . n 
A 1 2   ALA 2   19  ?   ?   ?   A . n 
A 1 3   HIS 3   20  ?   ?   ?   A . n 
A 1 4   HIS 4   21  ?   ?   ?   A . n 
A 1 5   HIS 5   22  ?   ?   ?   A . n 
A 1 6   HIS 6   23  ?   ?   ?   A . n 
A 1 7   HIS 7   24  ?   ?   ?   A . n 
A 1 8   HIS 8   25  25  HIS HIS A . n 
A 1 9   VAL 9   26  26  VAL VAL A . n 
A 1 10  GLU 10  27  27  GLU GLU A . n 
A 1 11  GLN 11  28  28  GLN GLN A . n 
A 1 12  THR 12  29  29  THR THR A . n 
A 1 13  TYR 13  30  30  TYR TYR A . n 
A 1 14  LEU 14  31  31  LEU LEU A . n 
A 1 15  MET 15  32  32  MET MET A . n 
A 1 16  ILE 16  33  33  ILE ILE A . n 
A 1 17  LYS 17  34  34  LYS LYS A . n 
A 1 18  PRO 18  35  35  PRO PRO A . n 
A 1 19  ASP 19  36  36  ASP ASP A . n 
A 1 20  GLY 20  37  37  GLY GLY A . n 
A 1 21  ILE 21  38  38  ILE ILE A . n 
A 1 22  GLN 22  39  39  GLN GLN A . n 
A 1 23  ARG 23  40  40  ARG ARG A . n 
A 1 24  GLN 24  41  41  GLN GLN A . n 
A 1 25  VAL 25  42  42  VAL VAL A . n 
A 1 26  VAL 26  43  43  VAL VAL A . n 
A 1 27  GLY 27  44  44  GLY GLY A . n 
A 1 28  GLU 28  45  45  GLU GLU A . n 
A 1 29  ILE 29  46  46  ILE ILE A . n 
A 1 30  ILE 30  47  47  ILE ILE A . n 
A 1 31  SER 31  48  48  SER SER A . n 
A 1 32  ARG 32  49  49  ARG ARG A . n 
A 1 33  PHE 33  50  50  PHE PHE A . n 
A 1 34  GLU 34  51  51  GLU GLU A . n 
A 1 35  LYS 35  52  52  LYS LYS A . n 
A 1 36  ARG 36  53  53  ARG ARG A . n 
A 1 37  GLY 37  54  54  GLY GLY A . n 
A 1 38  TYR 38  55  55  TYR TYR A . n 
A 1 39  ARG 39  56  56  ARG ARG A . n 
A 1 40  ILE 40  57  57  ILE ILE A . n 
A 1 41  ALA 41  58  58  ALA ALA A . n 
A 1 42  ALA 42  59  59  ALA ALA A . n 
A 1 43  MET 43  60  60  MET MET A . n 
A 1 44  LYS 44  61  61  LYS LYS A . n 
A 1 45  LEU 45  62  62  LEU LEU A . n 
A 1 46  THR 46  63  63  THR THR A . n 
A 1 47  ILE 47  64  64  ILE ILE A . n 
A 1 48  ALA 48  65  65  ALA ALA A . n 
A 1 49  THR 49  66  66  THR THR A . n 
A 1 50  PRO 50  67  67  PRO PRO A . n 
A 1 51  ALA 51  68  68  ALA ALA A . n 
A 1 52  ILE 52  69  69  ILE ILE A . n 
A 1 53  LEU 53  70  70  LEU LEU A . n 
A 1 54  GLU 54  71  71  GLU GLU A . n 
A 1 55  GLU 55  72  72  GLU GLU A . n 
A 1 56  HIS 56  73  73  HIS HIS A . n 
A 1 57  TYR 57  74  74  TYR TYR A . n 
A 1 58  ALA 58  75  75  ALA ALA A . n 
A 1 59  GLU 59  76  76  GLU GLU A . n 
A 1 60  HIS 60  77  77  HIS HIS A . n 
A 1 61  LYS 61  78  78  LYS LYS A . n 
A 1 62  GLY 62  79  79  GLY GLY A . n 
A 1 63  LYS 63  80  80  LYS LYS A . n 
A 1 64  PRO 64  81  81  PRO PRO A . n 
A 1 65  PHE 65  82  82  PHE PHE A . n 
A 1 66  LEU 66  83  83  LEU LEU A . n 
A 1 67  PRO 67  84  84  PRO PRO A . n 
A 1 68  GLY 68  85  85  GLY GLY A . n 
A 1 69  LEU 69  86  86  LEU LEU A . n 
A 1 70  ILE 70  87  87  ILE ILE A . n 
A 1 71  GLU 71  88  88  GLU GLU A . n 
A 1 72  LYS 72  89  89  LYS LYS A . n 
A 1 73  MET 73  90  90  MET MET A . n 
A 1 74  THR 74  91  91  THR THR A . n 
A 1 75  GLY 75  92  92  GLY GLY A . n 
A 1 76  PRO 76  93  93  PRO PRO A . n 
A 1 77  VAL 77  94  94  VAL VAL A . n 
A 1 78  LEU 78  95  95  LEU LEU A . n 
A 1 79  CYS 79  96  96  CYS CYS A . n 
A 1 80  MET 80  97  97  MET MET A . n 
A 1 81  VAL 81  98  98  VAL VAL A . n 
A 1 82  PHE 82  99  99  PHE PHE A . n 
A 1 83  GLU 83  100 100 GLU GLU A . n 
A 1 84  GLY 84  101 101 GLY GLY A . n 
A 1 85  VAL 85  102 102 VAL VAL A . n 
A 1 86  ASP 86  103 103 ASP ASP A . n 
A 1 87  VAL 87  104 104 VAL VAL A . n 
A 1 88  ILE 88  105 105 ILE ILE A . n 
A 1 89  ALA 89  106 106 ALA ALA A . n 
A 1 90  GLN 90  107 107 GLN GLN A . n 
A 1 91  ALA 91  108 108 ALA ALA A . n 
A 1 92  ARG 92  109 109 ARG ARG A . n 
A 1 93  LYS 93  110 110 LYS LYS A . n 
A 1 94  MET 94  111 111 MET MET A . n 
A 1 95  MET 95  112 112 MET MET A . n 
A 1 96  GLY 96  113 113 GLY GLY A . n 
A 1 97  SER 97  114 114 SER SER A . n 
A 1 98  THR 98  115 115 THR THR A . n 
A 1 99  ARG 99  116 116 ARG ARG A . n 
A 1 100 PRO 100 117 117 PRO PRO A . n 
A 1 101 GLY 101 118 118 GLY GLY A . n 
A 1 102 GLU 102 119 119 GLU GLU A . n 
A 1 103 ALA 103 120 120 ALA ALA A . n 
A 1 104 ALA 104 121 121 ALA ALA A . n 
A 1 105 PRO 105 122 122 PRO PRO A . n 
A 1 106 GLY 106 123 123 GLY GLY A . n 
A 1 107 THR 107 124 124 THR THR A . n 
A 1 108 ILE 108 125 125 ILE ILE A . n 
A 1 109 ARG 109 126 126 ARG ARG A . n 
A 1 110 ALA 110 127 127 ALA ALA A . n 
A 1 111 ASP 111 128 128 ASP ASP A . n 
A 1 112 PHE 112 129 129 PHE PHE A . n 
A 1 113 CYS 113 130 130 CYS CYS A . n 
A 1 114 GLN 114 131 131 GLN GLN A . n 
A 1 115 GLN 115 132 132 GLN GLN A . n 
A 1 116 ALA 116 133 133 ALA ALA A . n 
A 1 117 GLY 117 134 134 GLY GLY A . n 
A 1 118 ARG 118 135 135 ARG ARG A . n 
A 1 119 ASN 119 136 136 ASN ASN A . n 
A 1 120 LEU 120 137 137 LEU LEU A . n 
A 1 121 ILE 121 138 138 ILE ILE A . n 
A 1 122 HIS 122 139 139 HIS HIS A . n 
A 1 123 GLY 123 140 140 GLY GLY A . n 
A 1 124 SER 124 141 141 SER SER A . n 
A 1 125 ASP 125 142 142 ASP ASP A . n 
A 1 126 SER 126 143 143 SER SER A . n 
A 1 127 ALA 127 144 144 ALA ALA A . n 
A 1 128 GLU 128 145 145 GLU GLU A . n 
A 1 129 SER 129 146 146 SER SER A . n 
A 1 130 ALA 130 147 147 ALA ALA A . n 
A 1 131 LYS 131 148 148 LYS LYS A . n 
A 1 132 ARG 132 149 149 ARG ARG A . n 
A 1 133 GLU 133 150 150 GLU GLU A . n 
A 1 134 ILE 134 151 151 ILE ILE A . n 
A 1 135 SER 135 152 152 SER SER A . n 
A 1 136 LEU 136 153 153 LEU LEU A . n 
A 1 137 TRP 137 154 154 TRP TRP A . n 
A 1 138 PHE 138 155 155 PHE PHE A . n 
A 1 139 LYS 139 156 156 LYS LYS A . n 
A 1 140 PRO 140 157 157 PRO PRO A . n 
A 1 141 GLU 141 158 158 GLU GLU A . n 
A 1 142 GLU 142 159 159 GLU GLU A . n 
A 1 143 ILE 143 160 160 ILE ILE A . n 
A 1 144 GLN 144 161 161 GLN GLN A . n 
A 1 145 SER 145 162 162 SER SER A . n 
A 1 146 TYR 146 163 163 TYR TYR A . n 
A 1 147 LYS 147 164 164 LYS LYS A . n 
A 1 148 LEU 148 165 165 LEU LEU A . n 
A 1 149 ALA 149 166 166 ALA ALA A . n 
A 1 150 LEU 150 167 167 LEU LEU A . n 
A 1 151 SER 151 168 168 SER SER A . n 
A 1 152 ASP 152 169 169 ASP ASP A . n 
A 1 153 TYR 153 170 170 TYR TYR A . n 
A 1 154 ILE 154 171 171 ILE ILE A . n 
A 1 155 PHE 155 172 172 PHE PHE A . n 
A 1 156 GLU 156 173 173 GLU GLU A . n 
B 1 1   MET 1   18  ?   ?   ?   B . n 
B 1 2   ALA 2   19  ?   ?   ?   B . n 
B 1 3   HIS 3   20  ?   ?   ?   B . n 
B 1 4   HIS 4   21  ?   ?   ?   B . n 
B 1 5   HIS 5   22  ?   ?   ?   B . n 
B 1 6   HIS 6   23  ?   ?   ?   B . n 
B 1 7   HIS 7   24  ?   ?   ?   B . n 
B 1 8   HIS 8   25  25  HIS HIS B . n 
B 1 9   VAL 9   26  26  VAL VAL B . n 
B 1 10  GLU 10  27  27  GLU GLU B . n 
B 1 11  GLN 11  28  28  GLN GLN B . n 
B 1 12  THR 12  29  29  THR THR B . n 
B 1 13  TYR 13  30  30  TYR TYR B . n 
B 1 14  LEU 14  31  31  LEU LEU B . n 
B 1 15  MET 15  32  32  MET MET B . n 
B 1 16  ILE 16  33  33  ILE ILE B . n 
B 1 17  LYS 17  34  34  LYS LYS B . n 
B 1 18  PRO 18  35  35  PRO PRO B . n 
B 1 19  ASP 19  36  36  ASP ASP B . n 
B 1 20  GLY 20  37  37  GLY GLY B . n 
B 1 21  ILE 21  38  38  ILE ILE B . n 
B 1 22  GLN 22  39  39  GLN GLN B . n 
B 1 23  ARG 23  40  40  ARG ARG B . n 
B 1 24  GLN 24  41  41  GLN GLN B . n 
B 1 25  VAL 25  42  42  VAL VAL B . n 
B 1 26  VAL 26  43  43  VAL VAL B . n 
B 1 27  GLY 27  44  44  GLY GLY B . n 
B 1 28  GLU 28  45  45  GLU GLU B . n 
B 1 29  ILE 29  46  46  ILE ILE B . n 
B 1 30  ILE 30  47  47  ILE ILE B . n 
B 1 31  SER 31  48  48  SER SER B . n 
B 1 32  ARG 32  49  49  ARG ARG B . n 
B 1 33  PHE 33  50  50  PHE PHE B . n 
B 1 34  GLU 34  51  51  GLU GLU B . n 
B 1 35  LYS 35  52  52  LYS LYS B . n 
B 1 36  ARG 36  53  53  ARG ARG B . n 
B 1 37  GLY 37  54  54  GLY GLY B . n 
B 1 38  TYR 38  55  55  TYR TYR B . n 
B 1 39  ARG 39  56  56  ARG ARG B . n 
B 1 40  ILE 40  57  57  ILE ILE B . n 
B 1 41  ALA 41  58  58  ALA ALA B . n 
B 1 42  ALA 42  59  59  ALA ALA B . n 
B 1 43  MET 43  60  60  MET MET B . n 
B 1 44  LYS 44  61  61  LYS LYS B . n 
B 1 45  LEU 45  62  62  LEU LEU B . n 
B 1 46  THR 46  63  63  THR THR B . n 
B 1 47  ILE 47  64  64  ILE ILE B . n 
B 1 48  ALA 48  65  65  ALA ALA B . n 
B 1 49  THR 49  66  66  THR THR B . n 
B 1 50  PRO 50  67  67  PRO PRO B . n 
B 1 51  ALA 51  68  68  ALA ALA B . n 
B 1 52  ILE 52  69  69  ILE ILE B . n 
B 1 53  LEU 53  70  70  LEU LEU B . n 
B 1 54  GLU 54  71  71  GLU GLU B . n 
B 1 55  GLU 55  72  72  GLU GLU B . n 
B 1 56  HIS 56  73  73  HIS HIS B . n 
B 1 57  TYR 57  74  74  TYR TYR B . n 
B 1 58  ALA 58  75  75  ALA ALA B . n 
B 1 59  GLU 59  76  76  GLU GLU B . n 
B 1 60  HIS 60  77  77  HIS HIS B . n 
B 1 61  LYS 61  78  78  LYS LYS B . n 
B 1 62  GLY 62  79  79  GLY GLY B . n 
B 1 63  LYS 63  80  80  LYS LYS B . n 
B 1 64  PRO 64  81  81  PRO PRO B . n 
B 1 65  PHE 65  82  82  PHE PHE B . n 
B 1 66  LEU 66  83  83  LEU LEU B . n 
B 1 67  PRO 67  84  84  PRO PRO B . n 
B 1 68  GLY 68  85  85  GLY GLY B . n 
B 1 69  LEU 69  86  86  LEU LEU B . n 
B 1 70  ILE 70  87  87  ILE ILE B . n 
B 1 71  GLU 71  88  88  GLU GLU B . n 
B 1 72  LYS 72  89  89  LYS LYS B . n 
B 1 73  MET 73  90  90  MET MET B . n 
B 1 74  THR 74  91  91  THR THR B . n 
B 1 75  GLY 75  92  92  GLY GLY B . n 
B 1 76  PRO 76  93  93  PRO PRO B . n 
B 1 77  VAL 77  94  94  VAL VAL B . n 
B 1 78  LEU 78  95  95  LEU LEU B . n 
B 1 79  CYS 79  96  96  CYS CYS B . n 
B 1 80  MET 80  97  97  MET MET B . n 
B 1 81  VAL 81  98  98  VAL VAL B . n 
B 1 82  PHE 82  99  99  PHE PHE B . n 
B 1 83  GLU 83  100 100 GLU GLU B . n 
B 1 84  GLY 84  101 101 GLY GLY B . n 
B 1 85  VAL 85  102 102 VAL VAL B . n 
B 1 86  ASP 86  103 103 ASP ASP B . n 
B 1 87  VAL 87  104 104 VAL VAL B . n 
B 1 88  ILE 88  105 105 ILE ILE B . n 
B 1 89  ALA 89  106 106 ALA ALA B . n 
B 1 90  GLN 90  107 107 GLN GLN B . n 
B 1 91  ALA 91  108 108 ALA ALA B . n 
B 1 92  ARG 92  109 109 ARG ARG B . n 
B 1 93  LYS 93  110 110 LYS LYS B . n 
B 1 94  MET 94  111 111 MET MET B . n 
B 1 95  MET 95  112 112 MET MET B . n 
B 1 96  GLY 96  113 113 GLY GLY B . n 
B 1 97  SER 97  114 114 SER SER B . n 
B 1 98  THR 98  115 115 THR THR B . n 
B 1 99  ARG 99  116 116 ARG ARG B . n 
B 1 100 PRO 100 117 117 PRO PRO B . n 
B 1 101 GLY 101 118 118 GLY GLY B . n 
B 1 102 GLU 102 119 119 GLU GLU B . n 
B 1 103 ALA 103 120 120 ALA ALA B . n 
B 1 104 ALA 104 121 121 ALA ALA B . n 
B 1 105 PRO 105 122 122 PRO PRO B . n 
B 1 106 GLY 106 123 123 GLY GLY B . n 
B 1 107 THR 107 124 124 THR THR B . n 
B 1 108 ILE 108 125 125 ILE ILE B . n 
B 1 109 ARG 109 126 126 ARG ARG B . n 
B 1 110 ALA 110 127 127 ALA ALA B . n 
B 1 111 ASP 111 128 128 ASP ASP B . n 
B 1 112 PHE 112 129 129 PHE PHE B . n 
B 1 113 CYS 113 130 130 CYS CYS B . n 
B 1 114 GLN 114 131 131 GLN GLN B . n 
B 1 115 GLN 115 132 132 GLN GLN B . n 
B 1 116 ALA 116 133 133 ALA ALA B . n 
B 1 117 GLY 117 134 134 GLY GLY B . n 
B 1 118 ARG 118 135 135 ARG ARG B . n 
B 1 119 ASN 119 136 136 ASN ASN B . n 
B 1 120 LEU 120 137 137 LEU LEU B . n 
B 1 121 ILE 121 138 138 ILE ILE B . n 
B 1 122 HIS 122 139 139 HIS HIS B . n 
B 1 123 GLY 123 140 140 GLY GLY B . n 
B 1 124 SER 124 141 141 SER SER B . n 
B 1 125 ASP 125 142 142 ASP ASP B . n 
B 1 126 SER 126 143 143 SER SER B . n 
B 1 127 ALA 127 144 144 ALA ALA B . n 
B 1 128 GLU 128 145 145 GLU GLU B . n 
B 1 129 SER 129 146 146 SER SER B . n 
B 1 130 ALA 130 147 147 ALA ALA B . n 
B 1 131 LYS 131 148 148 LYS LYS B . n 
B 1 132 ARG 132 149 149 ARG ARG B . n 
B 1 133 GLU 133 150 150 GLU GLU B . n 
B 1 134 ILE 134 151 151 ILE ILE B . n 
B 1 135 SER 135 152 152 SER SER B . n 
B 1 136 LEU 136 153 153 LEU LEU B . n 
B 1 137 TRP 137 154 154 TRP TRP B . n 
B 1 138 PHE 138 155 155 PHE PHE B . n 
B 1 139 LYS 139 156 156 LYS LYS B . n 
B 1 140 PRO 140 157 157 PRO PRO B . n 
B 1 141 GLU 141 158 158 GLU GLU B . n 
B 1 142 GLU 142 159 159 GLU GLU B . n 
B 1 143 ILE 143 160 160 ILE ILE B . n 
B 1 144 GLN 144 161 161 GLN GLN B . n 
B 1 145 SER 145 162 162 SER SER B . n 
B 1 146 TYR 146 163 163 TYR TYR B . n 
B 1 147 LYS 147 164 164 LYS LYS B . n 
B 1 148 LEU 148 165 165 LEU LEU B . n 
B 1 149 ALA 149 166 166 ALA ALA B . n 
B 1 150 LEU 150 167 167 LEU LEU B . n 
B 1 151 SER 151 168 168 SER SER B . n 
B 1 152 ASP 152 169 169 ASP ASP B . n 
B 1 153 TYR 153 170 170 TYR TYR B . n 
B 1 154 ILE 154 171 171 ILE ILE B . n 
B 1 155 PHE 155 172 172 PHE PHE B . n 
B 1 156 GLU 156 173 173 GLU GLU B . n 
C 1 1   MET 1   18  ?   ?   ?   C . n 
C 1 2   ALA 2   19  ?   ?   ?   C . n 
C 1 3   HIS 3   20  ?   ?   ?   C . n 
C 1 4   HIS 4   21  ?   ?   ?   C . n 
C 1 5   HIS 5   22  ?   ?   ?   C . n 
C 1 6   HIS 6   23  ?   ?   ?   C . n 
C 1 7   HIS 7   24  ?   ?   ?   C . n 
C 1 8   HIS 8   25  25  HIS HIS C . n 
C 1 9   VAL 9   26  26  VAL VAL C . n 
C 1 10  GLU 10  27  27  GLU GLU C . n 
C 1 11  GLN 11  28  28  GLN GLN C . n 
C 1 12  THR 12  29  29  THR THR C . n 
C 1 13  TYR 13  30  30  TYR TYR C . n 
C 1 14  LEU 14  31  31  LEU LEU C . n 
C 1 15  MET 15  32  32  MET MET C . n 
C 1 16  ILE 16  33  33  ILE ILE C . n 
C 1 17  LYS 17  34  34  LYS LYS C . n 
C 1 18  PRO 18  35  35  PRO PRO C . n 
C 1 19  ASP 19  36  36  ASP ASP C . n 
C 1 20  GLY 20  37  37  GLY GLY C . n 
C 1 21  ILE 21  38  38  ILE ILE C . n 
C 1 22  GLN 22  39  39  GLN GLN C . n 
C 1 23  ARG 23  40  40  ARG ARG C . n 
C 1 24  GLN 24  41  41  GLN GLN C . n 
C 1 25  VAL 25  42  42  VAL VAL C . n 
C 1 26  VAL 26  43  43  VAL VAL C . n 
C 1 27  GLY 27  44  44  GLY GLY C . n 
C 1 28  GLU 28  45  45  GLU GLU C . n 
C 1 29  ILE 29  46  46  ILE ILE C . n 
C 1 30  ILE 30  47  47  ILE ILE C . n 
C 1 31  SER 31  48  48  SER SER C . n 
C 1 32  ARG 32  49  49  ARG ARG C . n 
C 1 33  PHE 33  50  50  PHE PHE C . n 
C 1 34  GLU 34  51  51  GLU GLU C . n 
C 1 35  LYS 35  52  52  LYS LYS C . n 
C 1 36  ARG 36  53  53  ARG ARG C . n 
C 1 37  GLY 37  54  54  GLY GLY C . n 
C 1 38  TYR 38  55  55  TYR TYR C . n 
C 1 39  ARG 39  56  56  ARG ARG C . n 
C 1 40  ILE 40  57  57  ILE ILE C . n 
C 1 41  ALA 41  58  58  ALA ALA C . n 
C 1 42  ALA 42  59  59  ALA ALA C . n 
C 1 43  MET 43  60  60  MET MET C . n 
C 1 44  LYS 44  61  61  LYS LYS C . n 
C 1 45  LEU 45  62  62  LEU LEU C . n 
C 1 46  THR 46  63  63  THR THR C . n 
C 1 47  ILE 47  64  64  ILE ILE C . n 
C 1 48  ALA 48  65  65  ALA ALA C . n 
C 1 49  THR 49  66  66  THR THR C . n 
C 1 50  PRO 50  67  67  PRO PRO C . n 
C 1 51  ALA 51  68  68  ALA ALA C . n 
C 1 52  ILE 52  69  69  ILE ILE C . n 
C 1 53  LEU 53  70  70  LEU LEU C . n 
C 1 54  GLU 54  71  71  GLU GLU C . n 
C 1 55  GLU 55  72  72  GLU GLU C . n 
C 1 56  HIS 56  73  73  HIS HIS C . n 
C 1 57  TYR 57  74  74  TYR TYR C . n 
C 1 58  ALA 58  75  75  ALA ALA C . n 
C 1 59  GLU 59  76  76  GLU GLU C . n 
C 1 60  HIS 60  77  77  HIS HIS C . n 
C 1 61  LYS 61  78  78  LYS LYS C . n 
C 1 62  GLY 62  79  79  GLY GLY C . n 
C 1 63  LYS 63  80  80  LYS LYS C . n 
C 1 64  PRO 64  81  81  PRO PRO C . n 
C 1 65  PHE 65  82  82  PHE PHE C . n 
C 1 66  LEU 66  83  83  LEU LEU C . n 
C 1 67  PRO 67  84  84  PRO PRO C . n 
C 1 68  GLY 68  85  85  GLY GLY C . n 
C 1 69  LEU 69  86  86  LEU LEU C . n 
C 1 70  ILE 70  87  87  ILE ILE C . n 
C 1 71  GLU 71  88  88  GLU GLU C . n 
C 1 72  LYS 72  89  89  LYS LYS C . n 
C 1 73  MET 73  90  90  MET MET C . n 
C 1 74  THR 74  91  91  THR THR C . n 
C 1 75  GLY 75  92  92  GLY GLY C . n 
C 1 76  PRO 76  93  93  PRO PRO C . n 
C 1 77  VAL 77  94  94  VAL VAL C . n 
C 1 78  LEU 78  95  95  LEU LEU C . n 
C 1 79  CYS 79  96  96  CYS CYS C . n 
C 1 80  MET 80  97  97  MET MET C . n 
C 1 81  VAL 81  98  98  VAL VAL C . n 
C 1 82  PHE 82  99  99  PHE PHE C . n 
C 1 83  GLU 83  100 100 GLU GLU C . n 
C 1 84  GLY 84  101 101 GLY GLY C . n 
C 1 85  VAL 85  102 102 VAL VAL C . n 
C 1 86  ASP 86  103 103 ASP ASP C . n 
C 1 87  VAL 87  104 104 VAL VAL C . n 
C 1 88  ILE 88  105 105 ILE ILE C . n 
C 1 89  ALA 89  106 106 ALA ALA C . n 
C 1 90  GLN 90  107 107 GLN GLN C . n 
C 1 91  ALA 91  108 108 ALA ALA C . n 
C 1 92  ARG 92  109 109 ARG ARG C . n 
C 1 93  LYS 93  110 110 LYS LYS C . n 
C 1 94  MET 94  111 111 MET MET C . n 
C 1 95  MET 95  112 112 MET MET C . n 
C 1 96  GLY 96  113 113 GLY GLY C . n 
C 1 97  SER 97  114 114 SER SER C . n 
C 1 98  THR 98  115 115 THR THR C . n 
C 1 99  ARG 99  116 116 ARG ARG C . n 
C 1 100 PRO 100 117 117 PRO PRO C . n 
C 1 101 GLY 101 118 118 GLY GLY C . n 
C 1 102 GLU 102 119 119 GLU GLU C . n 
C 1 103 ALA 103 120 120 ALA ALA C . n 
C 1 104 ALA 104 121 121 ALA ALA C . n 
C 1 105 PRO 105 122 122 PRO PRO C . n 
C 1 106 GLY 106 123 123 GLY GLY C . n 
C 1 107 THR 107 124 124 THR THR C . n 
C 1 108 ILE 108 125 125 ILE ILE C . n 
C 1 109 ARG 109 126 126 ARG ARG C . n 
C 1 110 ALA 110 127 127 ALA ALA C . n 
C 1 111 ASP 111 128 128 ASP ASP C . n 
C 1 112 PHE 112 129 129 PHE PHE C . n 
C 1 113 CYS 113 130 130 CYS CYS C . n 
C 1 114 GLN 114 131 131 GLN GLN C . n 
C 1 115 GLN 115 132 132 GLN GLN C . n 
C 1 116 ALA 116 133 133 ALA ALA C . n 
C 1 117 GLY 117 134 134 GLY GLY C . n 
C 1 118 ARG 118 135 135 ARG ARG C . n 
C 1 119 ASN 119 136 136 ASN ASN C . n 
C 1 120 LEU 120 137 137 LEU LEU C . n 
C 1 121 ILE 121 138 138 ILE ILE C . n 
C 1 122 HIS 122 139 139 HIS HIS C . n 
C 1 123 GLY 123 140 140 GLY GLY C . n 
C 1 124 SER 124 141 141 SER SER C . n 
C 1 125 ASP 125 142 142 ASP ASP C . n 
C 1 126 SER 126 143 143 SER SER C . n 
C 1 127 ALA 127 144 144 ALA ALA C . n 
C 1 128 GLU 128 145 145 GLU GLU C . n 
C 1 129 SER 129 146 146 SER SER C . n 
C 1 130 ALA 130 147 147 ALA ALA C . n 
C 1 131 LYS 131 148 148 LYS LYS C . n 
C 1 132 ARG 132 149 149 ARG ARG C . n 
C 1 133 GLU 133 150 150 GLU GLU C . n 
C 1 134 ILE 134 151 151 ILE ILE C . n 
C 1 135 SER 135 152 152 SER SER C . n 
C 1 136 LEU 136 153 153 LEU LEU C . n 
C 1 137 TRP 137 154 154 TRP TRP C . n 
C 1 138 PHE 138 155 155 PHE PHE C . n 
C 1 139 LYS 139 156 156 LYS LYS C . n 
C 1 140 PRO 140 157 157 PRO PRO C . n 
C 1 141 GLU 141 158 158 GLU GLU C . n 
C 1 142 GLU 142 159 159 GLU GLU C . n 
C 1 143 ILE 143 160 160 ILE ILE C . n 
C 1 144 GLN 144 161 161 GLN GLN C . n 
C 1 145 SER 145 162 162 SER SER C . n 
C 1 146 TYR 146 163 163 TYR TYR C . n 
C 1 147 LYS 147 164 164 LYS LYS C . n 
C 1 148 LEU 148 165 165 LEU LEU C . n 
C 1 149 ALA 149 166 166 ALA ALA C . n 
C 1 150 LEU 150 167 167 LEU LEU C . n 
C 1 151 SER 151 168 168 SER SER C . n 
C 1 152 ASP 152 169 169 ASP ASP C . n 
C 1 153 TYR 153 170 170 TYR TYR C . n 
C 1 154 ILE 154 171 171 ILE ILE C . n 
C 1 155 PHE 155 172 172 PHE PHE C . n 
C 1 156 GLU 156 173 173 GLU GLU C . n 
# 
loop_
_pdbx_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 SO4 1   201 2   SO4 SO4 A . 
E 2 SO4 1   202 4   SO4 SO4 A . 
F 2 SO4 1   203 10  SO4 SO4 A . 
G 2 SO4 1   201 3   SO4 SO4 B . 
H 2 SO4 1   202 5   SO4 SO4 B . 
I 2 SO4 1   203 7   SO4 SO4 B . 
J 2 SO4 1   204 11  SO4 SO4 B . 
K 2 SO4 1   201 1   SO4 SO4 C . 
L 2 SO4 1   202 6   SO4 SO4 C . 
M 2 SO4 1   203 8   SO4 SO4 C . 
N 2 SO4 1   204 9   SO4 SO4 C . 
O 3 HOH 1   301 549 HOH HOH A . 
O 3 HOH 2   302 540 HOH HOH A . 
O 3 HOH 3   303 80  HOH HOH A . 
O 3 HOH 4   304 169 HOH HOH A . 
O 3 HOH 5   305 99  HOH HOH A . 
O 3 HOH 6   306 199 HOH HOH A . 
O 3 HOH 7   307 266 HOH HOH A . 
O 3 HOH 8   308 6   HOH HOH A . 
O 3 HOH 9   309 431 HOH HOH A . 
O 3 HOH 10  310 113 HOH HOH A . 
O 3 HOH 11  311 360 HOH HOH A . 
O 3 HOH 12  312 458 HOH HOH A . 
O 3 HOH 13  313 182 HOH HOH A . 
O 3 HOH 14  314 1   HOH HOH A . 
O 3 HOH 15  315 473 HOH HOH A . 
O 3 HOH 16  316 248 HOH HOH A . 
O 3 HOH 17  317 432 HOH HOH A . 
O 3 HOH 18  318 36  HOH HOH A . 
O 3 HOH 19  319 258 HOH HOH A . 
O 3 HOH 20  320 371 HOH HOH A . 
O 3 HOH 21  321 500 HOH HOH A . 
O 3 HOH 22  322 259 HOH HOH A . 
O 3 HOH 23  323 112 HOH HOH A . 
O 3 HOH 24  324 178 HOH HOH A . 
O 3 HOH 25  325 316 HOH HOH A . 
O 3 HOH 26  326 125 HOH HOH A . 
O 3 HOH 27  327 272 HOH HOH A . 
O 3 HOH 28  328 442 HOH HOH A . 
O 3 HOH 29  329 312 HOH HOH A . 
O 3 HOH 30  330 309 HOH HOH A . 
O 3 HOH 31  331 85  HOH HOH A . 
O 3 HOH 32  332 357 HOH HOH A . 
O 3 HOH 33  333 541 HOH HOH A . 
O 3 HOH 34  334 63  HOH HOH A . 
O 3 HOH 35  335 206 HOH HOH A . 
O 3 HOH 36  336 135 HOH HOH A . 
O 3 HOH 37  337 349 HOH HOH A . 
O 3 HOH 38  338 115 HOH HOH A . 
O 3 HOH 39  339 117 HOH HOH A . 
O 3 HOH 40  340 301 HOH HOH A . 
O 3 HOH 41  341 27  HOH HOH A . 
O 3 HOH 42  342 130 HOH HOH A . 
O 3 HOH 43  343 83  HOH HOH A . 
O 3 HOH 44  344 306 HOH HOH A . 
O 3 HOH 45  345 19  HOH HOH A . 
O 3 HOH 46  346 294 HOH HOH A . 
O 3 HOH 47  347 507 HOH HOH A . 
O 3 HOH 48  348 232 HOH HOH A . 
O 3 HOH 49  349 76  HOH HOH A . 
O 3 HOH 50  350 71  HOH HOH A . 
O 3 HOH 51  351 15  HOH HOH A . 
O 3 HOH 52  352 546 HOH HOH A . 
O 3 HOH 53  353 75  HOH HOH A . 
O 3 HOH 54  354 142 HOH HOH A . 
O 3 HOH 55  355 426 HOH HOH A . 
O 3 HOH 56  356 13  HOH HOH A . 
O 3 HOH 57  357 8   HOH HOH A . 
O 3 HOH 58  358 9   HOH HOH A . 
O 3 HOH 59  359 194 HOH HOH A . 
O 3 HOH 60  360 11  HOH HOH A . 
O 3 HOH 61  361 264 HOH HOH A . 
O 3 HOH 62  362 154 HOH HOH A . 
O 3 HOH 63  363 438 HOH HOH A . 
O 3 HOH 64  364 121 HOH HOH A . 
O 3 HOH 65  365 118 HOH HOH A . 
O 3 HOH 66  366 102 HOH HOH A . 
O 3 HOH 67  367 213 HOH HOH A . 
O 3 HOH 68  368 238 HOH HOH A . 
O 3 HOH 69  369 58  HOH HOH A . 
O 3 HOH 70  370 343 HOH HOH A . 
O 3 HOH 71  371 445 HOH HOH A . 
O 3 HOH 72  372 203 HOH HOH A . 
O 3 HOH 73  373 100 HOH HOH A . 
O 3 HOH 74  374 231 HOH HOH A . 
O 3 HOH 75  375 180 HOH HOH A . 
O 3 HOH 76  376 141 HOH HOH A . 
O 3 HOH 77  377 193 HOH HOH A . 
O 3 HOH 78  378 35  HOH HOH A . 
O 3 HOH 79  379 236 HOH HOH A . 
O 3 HOH 80  380 251 HOH HOH A . 
O 3 HOH 81  381 327 HOH HOH A . 
O 3 HOH 82  382 171 HOH HOH A . 
O 3 HOH 83  383 234 HOH HOH A . 
O 3 HOH 84  384 23  HOH HOH A . 
O 3 HOH 85  385 262 HOH HOH A . 
O 3 HOH 86  386 198 HOH HOH A . 
O 3 HOH 87  387 131 HOH HOH A . 
O 3 HOH 88  388 81  HOH HOH A . 
O 3 HOH 89  389 46  HOH HOH A . 
O 3 HOH 90  390 260 HOH HOH A . 
O 3 HOH 91  391 202 HOH HOH A . 
O 3 HOH 92  392 544 HOH HOH A . 
O 3 HOH 93  393 420 HOH HOH A . 
O 3 HOH 94  394 536 HOH HOH A . 
O 3 HOH 95  395 34  HOH HOH A . 
O 3 HOH 96  396 157 HOH HOH A . 
O 3 HOH 97  397 446 HOH HOH A . 
O 3 HOH 98  398 84  HOH HOH A . 
O 3 HOH 99  399 377 HOH HOH A . 
O 3 HOH 100 400 572 HOH HOH A . 
O 3 HOH 101 401 207 HOH HOH A . 
O 3 HOH 102 402 341 HOH HOH A . 
O 3 HOH 103 403 57  HOH HOH A . 
O 3 HOH 104 404 451 HOH HOH A . 
O 3 HOH 105 405 164 HOH HOH A . 
O 3 HOH 106 406 73  HOH HOH A . 
O 3 HOH 107 407 16  HOH HOH A . 
O 3 HOH 108 408 212 HOH HOH A . 
O 3 HOH 109 409 336 HOH HOH A . 
O 3 HOH 110 410 436 HOH HOH A . 
O 3 HOH 111 411 339 HOH HOH A . 
O 3 HOH 112 412 317 HOH HOH A . 
O 3 HOH 113 413 324 HOH HOH A . 
O 3 HOH 114 414 150 HOH HOH A . 
O 3 HOH 115 415 521 HOH HOH A . 
O 3 HOH 116 416 181 HOH HOH A . 
O 3 HOH 117 417 444 HOH HOH A . 
O 3 HOH 118 418 552 HOH HOH A . 
O 3 HOH 119 419 417 HOH HOH A . 
O 3 HOH 120 420 401 HOH HOH A . 
O 3 HOH 121 421 2   HOH HOH A . 
O 3 HOH 122 422 147 HOH HOH A . 
O 3 HOH 123 423 568 HOH HOH A . 
O 3 HOH 124 424 227 HOH HOH A . 
O 3 HOH 125 425 518 HOH HOH A . 
O 3 HOH 126 426 196 HOH HOH A . 
O 3 HOH 127 427 296 HOH HOH A . 
O 3 HOH 128 428 133 HOH HOH A . 
O 3 HOH 129 429 353 HOH HOH A . 
O 3 HOH 130 430 302 HOH HOH A . 
O 3 HOH 131 431 25  HOH HOH A . 
O 3 HOH 132 432 314 HOH HOH A . 
O 3 HOH 133 433 108 HOH HOH A . 
O 3 HOH 134 434 484 HOH HOH A . 
O 3 HOH 135 435 461 HOH HOH A . 
O 3 HOH 136 436 128 HOH HOH A . 
O 3 HOH 137 437 18  HOH HOH A . 
O 3 HOH 138 438 359 HOH HOH A . 
O 3 HOH 139 439 220 HOH HOH A . 
O 3 HOH 140 440 472 HOH HOH A . 
O 3 HOH 141 441 116 HOH HOH A . 
O 3 HOH 142 442 365 HOH HOH A . 
O 3 HOH 143 443 320 HOH HOH A . 
O 3 HOH 144 444 397 HOH HOH A . 
O 3 HOH 145 445 509 HOH HOH A . 
O 3 HOH 146 446 134 HOH HOH A . 
O 3 HOH 147 447 208 HOH HOH A . 
O 3 HOH 148 448 176 HOH HOH A . 
O 3 HOH 149 449 535 HOH HOH A . 
O 3 HOH 150 450 510 HOH HOH A . 
O 3 HOH 151 451 563 HOH HOH A . 
O 3 HOH 152 452 523 HOH HOH A . 
O 3 HOH 153 453 478 HOH HOH A . 
O 3 HOH 154 454 233 HOH HOH A . 
O 3 HOH 155 455 358 HOH HOH A . 
O 3 HOH 156 456 485 HOH HOH A . 
O 3 HOH 157 457 333 HOH HOH A . 
O 3 HOH 158 458 373 HOH HOH A . 
O 3 HOH 159 459 242 HOH HOH A . 
O 3 HOH 160 460 149 HOH HOH A . 
O 3 HOH 161 461 162 HOH HOH A . 
O 3 HOH 162 462 172 HOH HOH A . 
O 3 HOH 163 463 560 HOH HOH A . 
O 3 HOH 164 464 483 HOH HOH A . 
O 3 HOH 165 465 318 HOH HOH A . 
O 3 HOH 166 466 249 HOH HOH A . 
O 3 HOH 167 467 334 HOH HOH A . 
O 3 HOH 168 468 37  HOH HOH A . 
O 3 HOH 169 469 512 HOH HOH A . 
O 3 HOH 170 470 313 HOH HOH A . 
O 3 HOH 171 471 190 HOH HOH A . 
O 3 HOH 172 472 235 HOH HOH A . 
O 3 HOH 173 473 571 HOH HOH A . 
O 3 HOH 174 474 496 HOH HOH A . 
O 3 HOH 175 475 230 HOH HOH A . 
O 3 HOH 176 476 537 HOH HOH A . 
O 3 HOH 177 477 330 HOH HOH A . 
O 3 HOH 178 478 167 HOH HOH A . 
O 3 HOH 179 479 400 HOH HOH A . 
O 3 HOH 180 480 457 HOH HOH A . 
O 3 HOH 181 481 340 HOH HOH A . 
O 3 HOH 182 482 465 HOH HOH A . 
O 3 HOH 183 483 393 HOH HOH A . 
O 3 HOH 184 484 538 HOH HOH A . 
O 3 HOH 185 485 285 HOH HOH A . 
O 3 HOH 186 486 403 HOH HOH A . 
O 3 HOH 187 487 511 HOH HOH A . 
O 3 HOH 188 488 383 HOH HOH A . 
O 3 HOH 189 489 527 HOH HOH A . 
O 3 HOH 190 490 77  HOH HOH A . 
O 3 HOH 191 491 391 HOH HOH A . 
O 3 HOH 192 492 344 HOH HOH A . 
O 3 HOH 193 493 250 HOH HOH A . 
O 3 HOH 194 494 508 HOH HOH A . 
O 3 HOH 195 495 411 HOH HOH A . 
O 3 HOH 196 496 382 HOH HOH A . 
O 3 HOH 197 497 323 HOH HOH A . 
O 3 HOH 198 498 315 HOH HOH A . 
O 3 HOH 199 499 137 HOH HOH A . 
O 3 HOH 200 500 574 HOH HOH A . 
O 3 HOH 201 501 539 HOH HOH A . 
O 3 HOH 202 502 160 HOH HOH A . 
P 3 HOH 1   301 221 HOH HOH B . 
P 3 HOH 2   302 453 HOH HOH B . 
P 3 HOH 3   303 430 HOH HOH B . 
P 3 HOH 4   304 165 HOH HOH B . 
P 3 HOH 5   305 554 HOH HOH B . 
P 3 HOH 6   306 424 HOH HOH B . 
P 3 HOH 7   307 516 HOH HOH B . 
P 3 HOH 8   308 419 HOH HOH B . 
P 3 HOH 9   309 241 HOH HOH B . 
P 3 HOH 10  310 398 HOH HOH B . 
P 3 HOH 11  311 486 HOH HOH B . 
P 3 HOH 12  312 288 HOH HOH B . 
P 3 HOH 13  313 261 HOH HOH B . 
P 3 HOH 14  314 54  HOH HOH B . 
P 3 HOH 15  315 425 HOH HOH B . 
P 3 HOH 16  316 361 HOH HOH B . 
P 3 HOH 17  317 163 HOH HOH B . 
P 3 HOH 18  318 543 HOH HOH B . 
P 3 HOH 19  319 345 HOH HOH B . 
P 3 HOH 20  320 381 HOH HOH B . 
P 3 HOH 21  321 243 HOH HOH B . 
P 3 HOH 22  322 522 HOH HOH B . 
P 3 HOH 23  323 464 HOH HOH B . 
P 3 HOH 24  324 326 HOH HOH B . 
P 3 HOH 25  325 267 HOH HOH B . 
P 3 HOH 26  326 525 HOH HOH B . 
P 3 HOH 27  327 276 HOH HOH B . 
P 3 HOH 28  328 416 HOH HOH B . 
P 3 HOH 29  329 386 HOH HOH B . 
P 3 HOH 30  330 104 HOH HOH B . 
P 3 HOH 31  331 201 HOH HOH B . 
P 3 HOH 32  332 448 HOH HOH B . 
P 3 HOH 33  333 89  HOH HOH B . 
P 3 HOH 34  334 32  HOH HOH B . 
P 3 HOH 35  335 452 HOH HOH B . 
P 3 HOH 36  336 447 HOH HOH B . 
P 3 HOH 37  337 278 HOH HOH B . 
P 3 HOH 38  338 434 HOH HOH B . 
P 3 HOH 39  339 124 HOH HOH B . 
P 3 HOH 40  340 43  HOH HOH B . 
P 3 HOH 41  341 45  HOH HOH B . 
P 3 HOH 42  342 214 HOH HOH B . 
P 3 HOH 43  343 91  HOH HOH B . 
P 3 HOH 44  344 346 HOH HOH B . 
P 3 HOH 45  345 153 HOH HOH B . 
P 3 HOH 46  346 107 HOH HOH B . 
P 3 HOH 47  347 96  HOH HOH B . 
P 3 HOH 48  348 462 HOH HOH B . 
P 3 HOH 49  349 51  HOH HOH B . 
P 3 HOH 50  350 191 HOH HOH B . 
P 3 HOH 51  351 513 HOH HOH B . 
P 3 HOH 52  352 39  HOH HOH B . 
P 3 HOH 53  353 161 HOH HOH B . 
P 3 HOH 54  354 151 HOH HOH B . 
P 3 HOH 55  355 114 HOH HOH B . 
P 3 HOH 56  356 31  HOH HOH B . 
P 3 HOH 57  357 69  HOH HOH B . 
P 3 HOH 58  358 372 HOH HOH B . 
P 3 HOH 59  359 50  HOH HOH B . 
P 3 HOH 60  360 412 HOH HOH B . 
P 3 HOH 61  361 72  HOH HOH B . 
P 3 HOH 62  362 379 HOH HOH B . 
P 3 HOH 63  363 188 HOH HOH B . 
P 3 HOH 64  364 263 HOH HOH B . 
P 3 HOH 65  365 30  HOH HOH B . 
P 3 HOH 66  366 3   HOH HOH B . 
P 3 HOH 67  367 335 HOH HOH B . 
P 3 HOH 68  368 450 HOH HOH B . 
P 3 HOH 69  369 173 HOH HOH B . 
P 3 HOH 70  370 105 HOH HOH B . 
P 3 HOH 71  371 59  HOH HOH B . 
P 3 HOH 72  372 205 HOH HOH B . 
P 3 HOH 73  373 7   HOH HOH B . 
P 3 HOH 74  374 487 HOH HOH B . 
P 3 HOH 75  375 168 HOH HOH B . 
P 3 HOH 76  376 362 HOH HOH B . 
P 3 HOH 77  377 187 HOH HOH B . 
P 3 HOH 78  378 223 HOH HOH B . 
P 3 HOH 79  379 437 HOH HOH B . 
P 3 HOH 80  380 129 HOH HOH B . 
P 3 HOH 81  381 303 HOH HOH B . 
P 3 HOH 82  382 392 HOH HOH B . 
P 3 HOH 83  383 93  HOH HOH B . 
P 3 HOH 84  384 90  HOH HOH B . 
P 3 HOH 85  385 459 HOH HOH B . 
P 3 HOH 86  386 364 HOH HOH B . 
P 3 HOH 87  387 174 HOH HOH B . 
P 3 HOH 88  388 252 HOH HOH B . 
P 3 HOH 89  389 337 HOH HOH B . 
P 3 HOH 90  390 183 HOH HOH B . 
P 3 HOH 91  391 159 HOH HOH B . 
P 3 HOH 92  392 82  HOH HOH B . 
P 3 HOH 93  393 555 HOH HOH B . 
P 3 HOH 94  394 177 HOH HOH B . 
P 3 HOH 95  395 428 HOH HOH B . 
P 3 HOH 96  396 254 HOH HOH B . 
P 3 HOH 97  397 470 HOH HOH B . 
P 3 HOH 98  398 140 HOH HOH B . 
P 3 HOH 99  399 64  HOH HOH B . 
P 3 HOH 100 400 240 HOH HOH B . 
P 3 HOH 101 401 545 HOH HOH B . 
P 3 HOH 102 402 491 HOH HOH B . 
P 3 HOH 103 403 98  HOH HOH B . 
P 3 HOH 104 404 68  HOH HOH B . 
P 3 HOH 105 405 380 HOH HOH B . 
P 3 HOH 106 406 268 HOH HOH B . 
P 3 HOH 107 407 475 HOH HOH B . 
P 3 HOH 108 408 126 HOH HOH B . 
P 3 HOH 109 409 210 HOH HOH B . 
P 3 HOH 110 410 255 HOH HOH B . 
P 3 HOH 111 411 148 HOH HOH B . 
P 3 HOH 112 412 331 HOH HOH B . 
P 3 HOH 113 413 123 HOH HOH B . 
P 3 HOH 114 414 332 HOH HOH B . 
P 3 HOH 115 415 569 HOH HOH B . 
P 3 HOH 116 416 146 HOH HOH B . 
P 3 HOH 117 417 402 HOH HOH B . 
P 3 HOH 118 418 505 HOH HOH B . 
P 3 HOH 119 419 455 HOH HOH B . 
P 3 HOH 120 420 454 HOH HOH B . 
P 3 HOH 121 421 506 HOH HOH B . 
P 3 HOH 122 422 352 HOH HOH B . 
P 3 HOH 123 423 499 HOH HOH B . 
P 3 HOH 124 424 519 HOH HOH B . 
P 3 HOH 125 425 556 HOH HOH B . 
P 3 HOH 126 426 280 HOH HOH B . 
P 3 HOH 127 427 440 HOH HOH B . 
P 3 HOH 128 428 477 HOH HOH B . 
P 3 HOH 129 429 517 HOH HOH B . 
P 3 HOH 130 430 48  HOH HOH B . 
P 3 HOH 131 431 65  HOH HOH B . 
P 3 HOH 132 432 561 HOH HOH B . 
P 3 HOH 133 433 367 HOH HOH B . 
P 3 HOH 134 434 413 HOH HOH B . 
P 3 HOH 135 435 405 HOH HOH B . 
P 3 HOH 136 436 217 HOH HOH B . 
P 3 HOH 137 437 407 HOH HOH B . 
P 3 HOH 138 438 222 HOH HOH B . 
P 3 HOH 139 439 476 HOH HOH B . 
P 3 HOH 140 440 308 HOH HOH B . 
P 3 HOH 141 441 529 HOH HOH B . 
P 3 HOH 142 442 562 HOH HOH B . 
P 3 HOH 143 443 14  HOH HOH B . 
P 3 HOH 144 444 136 HOH HOH B . 
P 3 HOH 145 445 328 HOH HOH B . 
P 3 HOH 146 446 482 HOH HOH B . 
P 3 HOH 147 447 110 HOH HOH B . 
P 3 HOH 148 448 497 HOH HOH B . 
P 3 HOH 149 449 421 HOH HOH B . 
P 3 HOH 150 450 49  HOH HOH B . 
P 3 HOH 151 451 530 HOH HOH B . 
P 3 HOH 152 452 558 HOH HOH B . 
P 3 HOH 153 453 374 HOH HOH B . 
P 3 HOH 154 454 299 HOH HOH B . 
P 3 HOH 155 455 480 HOH HOH B . 
P 3 HOH 156 456 514 HOH HOH B . 
P 3 HOH 157 457 369 HOH HOH B . 
P 3 HOH 158 458 166 HOH HOH B . 
P 3 HOH 159 459 498 HOH HOH B . 
P 3 HOH 160 460 573 HOH HOH B . 
P 3 HOH 161 461 311 HOH HOH B . 
P 3 HOH 162 462 564 HOH HOH B . 
P 3 HOH 163 463 247 HOH HOH B . 
P 3 HOH 164 464 559 HOH HOH B . 
P 3 HOH 165 465 495 HOH HOH B . 
P 3 HOH 166 466 502 HOH HOH B . 
P 3 HOH 167 467 281 HOH HOH B . 
P 3 HOH 168 468 423 HOH HOH B . 
P 3 HOH 169 469 418 HOH HOH B . 
P 3 HOH 170 470 566 HOH HOH B . 
Q 3 HOH 1   301 138 HOH HOH C . 
Q 3 HOH 2   302 52  HOH HOH C . 
Q 3 HOH 3   303 427 HOH HOH C . 
Q 3 HOH 4   304 279 HOH HOH C . 
Q 3 HOH 5   305 489 HOH HOH C . 
Q 3 HOH 6   306 226 HOH HOH C . 
Q 3 HOH 7   307 47  HOH HOH C . 
Q 3 HOH 8   308 474 HOH HOH C . 
Q 3 HOH 9   309 225 HOH HOH C . 
Q 3 HOH 10  310 277 HOH HOH C . 
Q 3 HOH 11  311 119 HOH HOH C . 
Q 3 HOH 12  312 79  HOH HOH C . 
Q 3 HOH 13  313 348 HOH HOH C . 
Q 3 HOH 14  314 4   HOH HOH C . 
Q 3 HOH 15  315 156 HOH HOH C . 
Q 3 HOH 16  316 300 HOH HOH C . 
Q 3 HOH 17  317 87  HOH HOH C . 
Q 3 HOH 18  318 275 HOH HOH C . 
Q 3 HOH 19  319 111 HOH HOH C . 
Q 3 HOH 20  320 120 HOH HOH C . 
Q 3 HOH 21  321 388 HOH HOH C . 
Q 3 HOH 22  322 469 HOH HOH C . 
Q 3 HOH 23  323 211 HOH HOH C . 
Q 3 HOH 24  324 195 HOH HOH C . 
Q 3 HOH 25  325 351 HOH HOH C . 
Q 3 HOH 26  326 282 HOH HOH C . 
Q 3 HOH 27  327 456 HOH HOH C . 
Q 3 HOH 28  328 5   HOH HOH C . 
Q 3 HOH 29  329 297 HOH HOH C . 
Q 3 HOH 30  330 449 HOH HOH C . 
Q 3 HOH 31  331 292 HOH HOH C . 
Q 3 HOH 32  332 257 HOH HOH C . 
Q 3 HOH 33  333 139 HOH HOH C . 
Q 3 HOH 34  334 61  HOH HOH C . 
Q 3 HOH 35  335 550 HOH HOH C . 
Q 3 HOH 36  336 355 HOH HOH C . 
Q 3 HOH 37  337 158 HOH HOH C . 
Q 3 HOH 38  338 78  HOH HOH C . 
Q 3 HOH 39  339 56  HOH HOH C . 
Q 3 HOH 40  340 12  HOH HOH C . 
Q 3 HOH 41  341 41  HOH HOH C . 
Q 3 HOH 42  342 396 HOH HOH C . 
Q 3 HOH 43  343 70  HOH HOH C . 
Q 3 HOH 44  344 488 HOH HOH C . 
Q 3 HOH 45  345 10  HOH HOH C . 
Q 3 HOH 46  346 92  HOH HOH C . 
Q 3 HOH 47  347 17  HOH HOH C . 
Q 3 HOH 48  348 229 HOH HOH C . 
Q 3 HOH 49  349 60  HOH HOH C . 
Q 3 HOH 50  350 548 HOH HOH C . 
Q 3 HOH 51  351 145 HOH HOH C . 
Q 3 HOH 52  352 329 HOH HOH C . 
Q 3 HOH 53  353 88  HOH HOH C . 
Q 3 HOH 54  354 55  HOH HOH C . 
Q 3 HOH 55  355 356 HOH HOH C . 
Q 3 HOH 56  356 132 HOH HOH C . 
Q 3 HOH 57  357 28  HOH HOH C . 
Q 3 HOH 58  358 94  HOH HOH C . 
Q 3 HOH 59  359 95  HOH HOH C . 
Q 3 HOH 60  360 155 HOH HOH C . 
Q 3 HOH 61  361 410 HOH HOH C . 
Q 3 HOH 62  362 350 HOH HOH C . 
Q 3 HOH 63  363 216 HOH HOH C . 
Q 3 HOH 64  364 307 HOH HOH C . 
Q 3 HOH 65  365 408 HOH HOH C . 
Q 3 HOH 66  366 467 HOH HOH C . 
Q 3 HOH 67  367 22  HOH HOH C . 
Q 3 HOH 68  368 209 HOH HOH C . 
Q 3 HOH 69  369 322 HOH HOH C . 
Q 3 HOH 70  370 284 HOH HOH C . 
Q 3 HOH 71  371 97  HOH HOH C . 
Q 3 HOH 72  372 143 HOH HOH C . 
Q 3 HOH 73  373 441 HOH HOH C . 
Q 3 HOH 74  374 186 HOH HOH C . 
Q 3 HOH 75  375 144 HOH HOH C . 
Q 3 HOH 76  376 224 HOH HOH C . 
Q 3 HOH 77  377 26  HOH HOH C . 
Q 3 HOH 78  378 406 HOH HOH C . 
Q 3 HOH 79  379 304 HOH HOH C . 
Q 3 HOH 80  380 273 HOH HOH C . 
Q 3 HOH 81  381 86  HOH HOH C . 
Q 3 HOH 82  382 439 HOH HOH C . 
Q 3 HOH 83  383 366 HOH HOH C . 
Q 3 HOH 84  384 354 HOH HOH C . 
Q 3 HOH 85  385 200 HOH HOH C . 
Q 3 HOH 86  386 21  HOH HOH C . 
Q 3 HOH 87  387 290 HOH HOH C . 
Q 3 HOH 88  388 215 HOH HOH C . 
Q 3 HOH 89  389 185 HOH HOH C . 
Q 3 HOH 90  390 298 HOH HOH C . 
Q 3 HOH 91  391 342 HOH HOH C . 
Q 3 HOH 92  392 20  HOH HOH C . 
Q 3 HOH 93  393 435 HOH HOH C . 
Q 3 HOH 94  394 422 HOH HOH C . 
Q 3 HOH 95  395 29  HOH HOH C . 
Q 3 HOH 96  396 245 HOH HOH C . 
Q 3 HOH 97  397 429 HOH HOH C . 
Q 3 HOH 98  398 253 HOH HOH C . 
Q 3 HOH 99  399 265 HOH HOH C . 
Q 3 HOH 100 400 551 HOH HOH C . 
Q 3 HOH 101 401 283 HOH HOH C . 
Q 3 HOH 102 402 376 HOH HOH C . 
Q 3 HOH 103 403 122 HOH HOH C . 
Q 3 HOH 104 404 228 HOH HOH C . 
Q 3 HOH 105 405 101 HOH HOH C . 
Q 3 HOH 106 406 74  HOH HOH C . 
Q 3 HOH 107 407 394 HOH HOH C . 
Q 3 HOH 108 408 24  HOH HOH C . 
Q 3 HOH 109 409 44  HOH HOH C . 
Q 3 HOH 110 410 557 HOH HOH C . 
Q 3 HOH 111 411 319 HOH HOH C . 
Q 3 HOH 112 412 53  HOH HOH C . 
Q 3 HOH 113 413 291 HOH HOH C . 
Q 3 HOH 114 414 287 HOH HOH C . 
Q 3 HOH 115 415 293 HOH HOH C . 
Q 3 HOH 116 416 38  HOH HOH C . 
Q 3 HOH 117 417 433 HOH HOH C . 
Q 3 HOH 118 418 62  HOH HOH C . 
Q 3 HOH 119 419 67  HOH HOH C . 
Q 3 HOH 120 420 404 HOH HOH C . 
Q 3 HOH 121 421 109 HOH HOH C . 
Q 3 HOH 122 422 40  HOH HOH C . 
Q 3 HOH 123 423 390 HOH HOH C . 
Q 3 HOH 124 424 66  HOH HOH C . 
Q 3 HOH 125 425 414 HOH HOH C . 
Q 3 HOH 126 426 192 HOH HOH C . 
Q 3 HOH 127 427 42  HOH HOH C . 
Q 3 HOH 128 428 269 HOH HOH C . 
Q 3 HOH 129 429 271 HOH HOH C . 
Q 3 HOH 130 430 515 HOH HOH C . 
Q 3 HOH 131 431 106 HOH HOH C . 
Q 3 HOH 132 432 460 HOH HOH C . 
Q 3 HOH 133 433 567 HOH HOH C . 
Q 3 HOH 134 434 479 HOH HOH C . 
Q 3 HOH 135 435 471 HOH HOH C . 
Q 3 HOH 136 436 103 HOH HOH C . 
Q 3 HOH 137 437 387 HOH HOH C . 
Q 3 HOH 138 438 152 HOH HOH C . 
Q 3 HOH 139 439 524 HOH HOH C . 
Q 3 HOH 140 440 175 HOH HOH C . 
Q 3 HOH 141 441 503 HOH HOH C . 
Q 3 HOH 142 442 325 HOH HOH C . 
Q 3 HOH 143 443 338 HOH HOH C . 
Q 3 HOH 144 444 463 HOH HOH C . 
Q 3 HOH 145 445 468 HOH HOH C . 
Q 3 HOH 146 446 553 HOH HOH C . 
Q 3 HOH 147 447 305 HOH HOH C . 
Q 3 HOH 148 448 466 HOH HOH C . 
Q 3 HOH 149 449 218 HOH HOH C . 
Q 3 HOH 150 450 534 HOH HOH C . 
Q 3 HOH 151 451 443 HOH HOH C . 
Q 3 HOH 152 452 310 HOH HOH C . 
Q 3 HOH 153 453 256 HOH HOH C . 
Q 3 HOH 154 454 570 HOH HOH C . 
Q 3 HOH 155 455 565 HOH HOH C . 
Q 3 HOH 156 456 493 HOH HOH C . 
Q 3 HOH 157 457 520 HOH HOH C . 
Q 3 HOH 158 458 237 HOH HOH C . 
Q 3 HOH 159 459 399 HOH HOH C . 
Q 3 HOH 160 460 347 HOH HOH C . 
Q 3 HOH 161 461 197 HOH HOH C . 
Q 3 HOH 162 462 368 HOH HOH C . 
Q 3 HOH 163 463 409 HOH HOH C . 
Q 3 HOH 164 464 375 HOH HOH C . 
Q 3 HOH 165 465 189 HOH HOH C . 
Q 3 HOH 166 466 219 HOH HOH C . 
Q 3 HOH 167 467 395 HOH HOH C . 
Q 3 HOH 168 468 389 HOH HOH C . 
Q 3 HOH 169 469 415 HOH HOH C . 
Q 3 HOH 170 470 33  HOH HOH C . 
Q 3 HOH 171 471 295 HOH HOH C . 
Q 3 HOH 172 472 547 HOH HOH C . 
Q 3 HOH 173 473 378 HOH HOH C . 
Q 3 HOH 174 474 481 HOH HOH C . 
Q 3 HOH 175 475 501 HOH HOH C . 
Q 3 HOH 176 476 286 HOH HOH C . 
Q 3 HOH 177 477 184 HOH HOH C . 
Q 3 HOH 178 478 170 HOH HOH C . 
Q 3 HOH 179 479 239 HOH HOH C . 
Q 3 HOH 180 480 532 HOH HOH C . 
Q 3 HOH 181 481 270 HOH HOH C . 
Q 3 HOH 182 482 526 HOH HOH C . 
Q 3 HOH 183 483 542 HOH HOH C . 
Q 3 HOH 184 484 533 HOH HOH C . 
Q 3 HOH 185 485 492 HOH HOH C . 
Q 3 HOH 186 486 244 HOH HOH C . 
Q 3 HOH 187 487 179 HOH HOH C . 
Q 3 HOH 188 488 204 HOH HOH C . 
Q 3 HOH 189 489 490 HOH HOH C . 
Q 3 HOH 190 490 289 HOH HOH C . 
Q 3 HOH 191 491 127 HOH HOH C . 
Q 3 HOH 192 492 370 HOH HOH C . 
Q 3 HOH 193 493 531 HOH HOH C . 
Q 3 HOH 194 494 504 HOH HOH C . 
Q 3 HOH 195 495 494 HOH HOH C . 
Q 3 HOH 196 496 246 HOH HOH C . 
Q 3 HOH 197 497 321 HOH HOH C . 
Q 3 HOH 198 498 363 HOH HOH C . 
Q 3 HOH 199 499 274 HOH HOH C . 
Q 3 HOH 200 500 384 HOH HOH C . 
Q 3 HOH 201 501 528 HOH HOH C . 
Q 3 HOH 202 502 385 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      ? ? ? '(1.21rc1_5156: ???)' ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .                     ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .                     ? 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? SHELX       ? ? ? .                     ? 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                     9O9R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.985 
_cell.length_a_esd                 ? 
_cell.length_b                     69.985 
_cell.length_b_esd                 ? 
_cell.length_c                     315.415 
_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                         9O9R 
_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                   9O9R 
_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             2.11 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.71 
_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              6.5 
_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    
;Index HT C6: 1.5M ammonium sufate, 0.1M sodium chloride, 0.1 M Bis-Tris pH 6.5. CrpaA.01302.a.B2.PW39348 at 8.9 mg/mL. plate 19658 C6 drop 1, Puck: PSL-0601, Cryo:  Paratone-N and parafin oil (1:1)
;
_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                                       9O9R 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.31 
_reflns.d_resolution_low                               48.05 
_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                                     111176 
_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                                36.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.98 
_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                                0.158 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       4047371 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.156 
_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                                    1.31 
_reflns_shell.d_res_low                                     1.34 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           168206 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8057 
_reflns_shell.percent_possible_obs                          99.6 
_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                               20.9 
_reflns_shell.pdbx_chi_squared                              0.76 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.5 
_reflns_shell.pdbx_Rrim_I_all                               1.336 
_reflns_shell.pdbx_Rpim_I_all                               0.289 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.564 
_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                                  1.304 
_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                                 9O9R 
_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                            1.31 
_refine.ls_d_res_low                             48.05 
_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                     110988 
_refine.ls_number_reflns_R_free                  5522 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1494 
_refine.ls_R_factor_R_free                       0.1871 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1475 
_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          SAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.33 
_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                            0.14 
_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                       1.31 
_refine_hist.d_res_low                        48.05 
_refine_hist.number_atoms_solvent             574 
_refine_hist.number_atoms_total               4126 
_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         55 
_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  ? 3700 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.933  ? 5019 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 14.909 ? 1432 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.075  ? 546  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 643  ? 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' 1.31 1.32  . . 184 3437 99.00  . . . . 0.2724 . . . . . . . . . . . . . . . 0.3514 
'X-RAY DIFFRACTION' 1.32 1.34  . . 193 3405 100.00 . . . . 0.2345 . . . . . . . . . . . . . . . 0.2715 
'X-RAY DIFFRACTION' 1.34 1.36  . . 193 3435 100.00 . . . . 0.2244 . . . . . . . . . . . . . . . 0.3095 
'X-RAY DIFFRACTION' 1.36 1.37  . . 170 3497 100.00 . . . . 0.2124 . . . . . . . . . . . . . . . 0.2583 
'X-RAY DIFFRACTION' 1.37 1.39  . . 173 3431 100.00 . . . . 0.2118 . . . . . . . . . . . . . . . 0.2730 
'X-RAY DIFFRACTION' 1.39 1.41  . . 189 3454 100.00 . . . . 0.1912 . . . . . . . . . . . . . . . 0.2755 
'X-RAY DIFFRACTION' 1.41 1.43  . . 183 3444 100.00 . . . . 0.1837 . . . . . . . . . . . . . . . 0.2527 
'X-RAY DIFFRACTION' 1.43 1.45  . . 193 3442 100.00 . . . . 0.1772 . . . . . . . . . . . . . . . 0.2361 
'X-RAY DIFFRACTION' 1.45 1.48  . . 194 3447 100.00 . . . . 0.1722 . . . . . . . . . . . . . . . 0.2134 
'X-RAY DIFFRACTION' 1.48 1.50  . . 166 3467 100.00 . . . . 0.1640 . . . . . . . . . . . . . . . 0.2344 
'X-RAY DIFFRACTION' 1.50 1.53  . . 193 3481 100.00 . . . . 0.1606 . . . . . . . . . . . . . . . 0.2176 
'X-RAY DIFFRACTION' 1.53 1.55  . . 175 3475 100.00 . . . . 0.1607 . . . . . . . . . . . . . . . 0.2172 
'X-RAY DIFFRACTION' 1.55 1.58  . . 173 3472 100.00 . . . . 0.1502 . . . . . . . . . . . . . . . 0.2005 
'X-RAY DIFFRACTION' 1.58 1.62  . . 197 3445 100.00 . . . . 0.1439 . . . . . . . . . . . . . . . 0.1939 
'X-RAY DIFFRACTION' 1.62 1.65  . . 179 3477 100.00 . . . . 0.1400 . . . . . . . . . . . . . . . 0.2039 
'X-RAY DIFFRACTION' 1.65 1.69  . . 217 3447 100.00 . . . . 0.1402 . . . . . . . . . . . . . . . 0.2046 
'X-RAY DIFFRACTION' 1.69 1.73  . . 212 3466 100.00 . . . . 0.1346 . . . . . . . . . . . . . . . 0.1869 
'X-RAY DIFFRACTION' 1.73 1.78  . . 175 3509 100.00 . . . . 0.1342 . . . . . . . . . . . . . . . 0.1744 
'X-RAY DIFFRACTION' 1.78 1.83  . . 193 3477 100.00 . . . . 0.1324 . . . . . . . . . . . . . . . 0.2039 
'X-RAY DIFFRACTION' 1.83 1.89  . . 183 3535 100.00 . . . . 0.1321 . . . . . . . . . . . . . . . 0.1773 
'X-RAY DIFFRACTION' 1.89 1.96  . . 172 3512 100.00 . . . . 0.1295 . . . . . . . . . . . . . . . 0.1612 
'X-RAY DIFFRACTION' 1.96 2.04  . . 179 3511 100.00 . . . . 0.1246 . . . . . . . . . . . . . . . 0.1609 
'X-RAY DIFFRACTION' 2.04 2.13  . . 170 3562 100.00 . . . . 0.1222 . . . . . . . . . . . . . . . 0.1590 
'X-RAY DIFFRACTION' 2.13 2.24  . . 186 3529 100.00 . . . . 0.1229 . . . . . . . . . . . . . . . 0.1662 
'X-RAY DIFFRACTION' 2.24 2.38  . . 169 3574 100.00 . . . . 0.1266 . . . . . . . . . . . . . . . 0.1488 
'X-RAY DIFFRACTION' 2.38 2.56  . . 176 3585 100.00 . . . . 0.1304 . . . . . . . . . . . . . . . 0.1560 
'X-RAY DIFFRACTION' 2.56 2.82  . . 197 3589 100.00 . . . . 0.1403 . . . . . . . . . . . . . . . 0.1539 
'X-RAY DIFFRACTION' 2.82 3.23  . . 159 3659 100.00 . . . . 0.1538 . . . . . . . . . . . . . . . 0.1770 
'X-RAY DIFFRACTION' 3.23 4.07  . . 177 3729 100.00 . . . . 0.1318 . . . . . . . . . . . . . . . 0.1409 
'X-RAY DIFFRACTION' 4.07 48.05 . . 202 3973 100.00 . . . . 0.1555 . . . . . . . . . . . . . . . 0.1961 
# 
_struct.entry_id                     9O9R 
_struct.title                        'Crystal structure of nucleoside-diphosphate kinase Cryptosporidium parvum' 
_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        9O9R 
_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 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 3 ? 
P N N 3 ? 
Q 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 9O9R A 9 ? 156 ? Q5CR64 26 ? 173 ? 26 173 
2 1 9O9R B 9 ? 156 ? Q5CR64 26 ? 173 ? 26 173 
3 1 9O9R 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 9O9R MET A 1 ? UNP Q5CR64 ? ? 'expression tag' 18 1  
1 9O9R ALA A 2 ? UNP Q5CR64 ? ? 'expression tag' 19 2  
1 9O9R HIS A 3 ? UNP Q5CR64 ? ? 'expression tag' 20 3  
1 9O9R HIS A 4 ? UNP Q5CR64 ? ? 'expression tag' 21 4  
1 9O9R HIS A 5 ? UNP Q5CR64 ? ? 'expression tag' 22 5  
1 9O9R HIS A 6 ? UNP Q5CR64 ? ? 'expression tag' 23 6  
1 9O9R HIS A 7 ? UNP Q5CR64 ? ? 'expression tag' 24 7  
1 9O9R HIS A 8 ? UNP Q5CR64 ? ? 'expression tag' 25 8  
2 9O9R MET B 1 ? UNP Q5CR64 ? ? 'expression tag' 18 9  
2 9O9R ALA B 2 ? UNP Q5CR64 ? ? 'expression tag' 19 10 
2 9O9R HIS B 3 ? UNP Q5CR64 ? ? 'expression tag' 20 11 
2 9O9R HIS B 4 ? UNP Q5CR64 ? ? 'expression tag' 21 12 
2 9O9R HIS B 5 ? UNP Q5CR64 ? ? 'expression tag' 22 13 
2 9O9R HIS B 6 ? UNP Q5CR64 ? ? 'expression tag' 23 14 
2 9O9R HIS B 7 ? UNP Q5CR64 ? ? 'expression tag' 24 15 
2 9O9R HIS B 8 ? UNP Q5CR64 ? ? 'expression tag' 25 16 
3 9O9R MET C 1 ? UNP Q5CR64 ? ? 'expression tag' 18 17 
3 9O9R ALA C 2 ? UNP Q5CR64 ? ? 'expression tag' 19 18 
3 9O9R HIS C 3 ? UNP Q5CR64 ? ? 'expression tag' 20 19 
3 9O9R HIS C 4 ? UNP Q5CR64 ? ? 'expression tag' 21 20 
3 9O9R HIS C 5 ? UNP Q5CR64 ? ? 'expression tag' 22 21 
3 9O9R HIS C 6 ? UNP Q5CR64 ? ? 'expression tag' 23 22 
3 9O9R HIS C 7 ? UNP Q5CR64 ? ? 'expression tag' 24 23 
3 9O9R 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)' 6730  ? 
1 MORE         -108  ? 
1 'SSA (A^2)'  21070 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
# 
_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  ? ILE A 47  ? ARG A 56  ILE A 64  
AA1 2 PRO A 76  ? GLY A 84  ? PRO A 93  GLY A 101 
AA1 3 GLU A 10  ? ILE A 16  ? GLU A 27  ILE A 33  
AA1 4 ILE A 121 ? GLY A 123 ? ILE A 138 GLY A 140 
AA2 1 ARG B 39  ? ILE B 47  ? ARG B 56  ILE B 64  
AA2 2 PRO B 76  ? GLY B 84  ? PRO B 93  GLY B 101 
AA2 3 GLU B 10  ? ILE B 16  ? GLU B 27  ILE B 33  
AA2 4 ILE B 121 ? GLY B 123 ? ILE B 138 GLY B 140 
AA3 1 ARG C 39  ? ILE C 47  ? ARG C 56  ILE C 64  
AA3 2 PRO C 76  ? GLY C 84  ? PRO C 93  GLY C 101 
AA3 3 GLU C 10  ? ILE C 16  ? GLU C 27  ILE C 33  
AA3 4 ILE C 121 ? GLY C 123 ? ILE C 138 GLY C 140 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 44 ? N LYS A 61  O CYS A 79  ? O CYS A 96  
AA1 2 3 O 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 LEU C 78 ? O LEU C 95  N ILE C 16  ? N ILE C 33  
AA3 3 4 N MET C 15 ? N MET C 32  O HIS C 122 ? O HIS C 139 
# 
_pdbx_entry_details.entry_id                   9O9R 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 74  ? ? -99.19 34.47  
2 1 LEU A 137 ? ? 73.12  -27.23 
3 1 TYR B 74  ? ? -97.37 34.94  
4 1 LEU B 137 ? ? 75.07  -28.27 
5 1 TYR C 74  ? ? -98.73 31.84  
6 1 LEU C 137 ? ? 75.83  -30.00 
# 
_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 384 ? O HOH . 
2 1 A HOH 459 ? O HOH . 
3 1 C HOH 496 ? Q 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  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
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                    9O9R 
_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]   0.014289 
_atom_sites.fract_transf_matrix[1][2]   0.008250 
_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]   0.016499 
_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]   0.003170 
_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   ? 11.472  53.517  7.027  1.00 35.96 ? 25  HIS A N   1 
ATOM   2    C CA  . HIS A 1 8   ? 10.177  53.621  7.690  1.00 30.79 ? 25  HIS A CA  1 
ATOM   3    C C   . HIS A 1 8   ? 9.791   52.255  8.240  1.00 28.61 ? 25  HIS A C   1 
ATOM   4    O O   . HIS A 1 8   ? 10.135  51.221  7.671  1.00 33.17 ? 25  HIS A O   1 
ATOM   5    C CB  . HIS A 1 8   ? 9.104   54.098  6.714  1.00 30.58 ? 25  HIS A CB  1 
ATOM   6    N N   . VAL A 1 9   ? 9.083   52.246  9.350  1.00 21.57 ? 26  VAL A N   1 
ATOM   7    C CA  . VAL A 1 9   ? 8.663   51.004  9.957  1.00 16.08 ? 26  VAL A CA  1 
ATOM   8    C C   . VAL A 1 9   ? 7.226   50.721  9.550  1.00 13.33 ? 26  VAL A C   1 
ATOM   9    O O   . VAL A 1 9   ? 6.502   51.593  9.062  1.00 15.63 ? 26  VAL A O   1 
ATOM   10   C CB  . VAL A 1 9   ? 8.832   51.024  11.498 1.00 16.36 ? 26  VAL A CB  1 
ATOM   11   C CG1 . VAL A 1 9   ? 10.312  51.157  11.856 1.00 18.70 ? 26  VAL A CG1 1 
ATOM   12   C CG2 . VAL A 1 9   ? 8.030   52.144  12.129 1.00 20.28 ? 26  VAL A CG2 1 
ATOM   13   N N   . GLU A 1 10  ? 6.807   49.476  9.736  1.00 11.42 ? 27  GLU A N   1 
ATOM   14   C CA  . GLU A 1 10  ? 5.405   49.100  9.603  1.00 10.99 ? 27  GLU A CA  1 
ATOM   15   C C   . GLU A 1 10  ? 5.030   48.234  10.801 1.00 9.39  ? 27  GLU A C   1 
ATOM   16   O O   . GLU A 1 10  ? 5.869   47.939  11.660 1.00 8.94  ? 27  GLU A O   1 
ATOM   17   C CB  . GLU A 1 10  ? 5.153   48.396  8.268  1.00 14.95 ? 27  GLU A CB  1 
ATOM   18   C CG  . GLU A 1 10  ? 5.986   47.165  8.104  1.00 13.73 ? 27  GLU A CG  1 
ATOM   19   C CD  . GLU A 1 10  ? 5.930   46.592  6.694  1.00 16.36 ? 27  GLU A CD  1 
ATOM   20   O OE1 . GLU A 1 10  ? 5.522   47.284  5.743  1.00 22.75 ? 27  GLU A OE1 1 
ATOM   21   O OE2 . GLU A 1 10  ? 6.268   45.413  6.553  1.00 13.34 ? 27  GLU A OE2 1 
ATOM   22   N N   . GLN A 1 11  ? 3.750   47.846  10.861 1.00 8.91  ? 28  GLN A N   1 
ATOM   23   C CA  . GLN A 1 11  ? 3.215   47.020  11.929 1.00 7.30  ? 28  GLN A CA  1 
ATOM   24   C C   . GLN A 1 11  ? 2.532   45.804  11.336 1.00 9.43  ? 28  GLN A C   1 
ATOM   25   O O   . GLN A 1 11  ? 1.832   45.899  10.323 1.00 10.18 ? 28  GLN A O   1 
ATOM   26   C CB  . GLN A 1 11  ? 2.220   47.791  12.786 1.00 9.98  ? 28  GLN A CB  1 
ATOM   27   C CG  . GLN A 1 11  ? 2.908   48.869  13.606 1.00 11.93 ? 28  GLN A CG  1 
ATOM   28   C CD  . GLN A 1 11  ? 2.003   49.553  14.607 1.00 14.04 ? 28  GLN A CD  1 
ATOM   29   O OE1 . GLN A 1 11  ? 0.799   49.318  14.658 1.00 17.40 ? 28  GLN A OE1 1 
ATOM   30   N NE2 . GLN A 1 11  ? 2.590   50.416  15.415 1.00 15.32 ? 28  GLN A NE2 1 
ATOM   31   N N   . THR A 1 12  ? 2.766   44.651  11.950 1.00 7.83  ? 29  THR A N   1 
ATOM   32   C CA  . THR A 1 12  ? 2.122   43.424  11.531 1.00 7.08  ? 29  THR A CA  1 
ATOM   33   C C   . THR A 1 12  ? 1.326   42.844  12.695 1.00 6.41  ? 29  THR A C   1 
ATOM   34   O O   . THR A 1 12  ? 1.610   43.125  13.863 1.00 7.59  ? 29  THR A O   1 
ATOM   35   C CB  . THR A 1 12  ? 3.150   42.402  11.016 1.00 8.92  ? 29  THR A CB  1 
ATOM   36   O OG1 . THR A 1 12  ? 2.438   41.355  10.351 1.00 9.11  ? 29  THR A OG1 1 
ATOM   37   C CG2 . THR A 1 12  ? 3.995   41.845  12.150 1.00 7.85  ? 29  THR A CG2 1 
ATOM   38   N N   . TYR A 1 13  ? 0.309   42.044  12.357 1.00 7.78  ? 30  TYR A N   1 
ATOM   39   C CA  . TYR A 1 13  ? -0.481  41.305  13.335 1.00 7.66  ? 30  TYR A CA  1 
ATOM   40   C C   . TYR A 1 13  ? 0.060   39.879  13.435 1.00 8.13  ? 30  TYR A C   1 
ATOM   41   O O   . TYR A 1 13  ? 0.104   39.148  12.442 1.00 8.96  ? 30  TYR A O   1 
ATOM   42   C CB  . TYR A 1 13  ? -1.966  41.287  12.956 1.00 8.74  ? 30  TYR A CB  1 
ATOM   43   C CG  . TYR A 1 13  ? -2.789  40.501  13.964 1.00 7.56  ? 30  TYR A CG  1 
ATOM   44   C CD1 . TYR A 1 13  ? -2.973  40.984  15.239 1.00 6.14  ? 30  TYR A CD1 1 
ATOM   45   C CD2 . TYR A 1 13  ? -3.333  39.269  13.647 1.00 7.81  ? 30  TYR A CD2 1 
ATOM   46   C CE1 . TYR A 1 13  ? -3.674  40.289  16.180 1.00 7.19  ? 30  TYR A CE1 1 
ATOM   47   C CE2 . TYR A 1 13  ? -4.047  38.537  14.594 1.00 7.06  ? 30  TYR A CE2 1 
ATOM   48   C CZ  . TYR A 1 13  ? -4.203  39.066  15.863 1.00 8.29  ? 30  TYR A CZ  1 
ATOM   49   O OH  . TYR A 1 13  ? -4.875  38.410  16.852 1.00 9.73  ? 30  TYR A OH  1 
ATOM   50   N N   . LEU A 1 14  ? 0.481   39.495  14.629 1.00 7.21  ? 31  LEU A N   1 
ATOM   51   C CA  . LEU A 1 14  ? 0.932   38.146  14.929 1.00 6.28  ? 31  LEU A CA  1 
ATOM   52   C C   . LEU A 1 14  ? 0.072   37.607  16.057 1.00 7.45  ? 31  LEU A C   1 
ATOM   53   O O   . LEU A 1 14  ? -0.211  38.321  17.028 1.00 9.69  ? 31  LEU A O   1 
ATOM   54   C CB  . LEU A 1 14  ? 2.395   38.154  15.361 1.00 7.95  ? 31  LEU A CB  1 
ATOM   55   C CG  . LEU A 1 14  ? 3.384   38.454  14.226 1.00 8.47  ? 31  LEU A CG  1 
ATOM   56   C CD1 . LEU A 1 14  ? 4.697   39.066  14.694 1.00 10.65 ? 31  LEU A CD1 1 
ATOM   57   C CD2 . LEU A 1 14  ? 3.697   37.148  13.452 1.00 12.42 ? 31  LEU A CD2 1 
ATOM   58   N N   . MET A 1 15  ? -0.343  36.349  15.939 1.00 7.70  ? 32  MET A N   1 
ATOM   59   C CA  . MET A 1 15  ? -1.242  35.745  16.911 1.00 7.46  ? 32  MET A CA  1 
ATOM   60   C C   . MET A 1 15  ? -0.727  34.364  17.258 1.00 7.17  ? 32  MET A C   1 
ATOM   61   O O   . MET A 1 15  ? -0.597  33.506  16.384 1.00 8.85  ? 32  MET A O   1 
ATOM   62   C CB  . MET A 1 15  ? -2.664  35.656  16.337 1.00 8.36  ? 32  MET A CB  1 
ATOM   63   C CG  . MET A 1 15  ? -3.673  34.993  17.264 1.00 10.26 ? 32  MET A CG  1 
ATOM   64   S SD  . MET A 1 15  ? -5.378  35.226  16.700 1.00 10.19 ? 32  MET A SD  1 
ATOM   65   C CE  . MET A 1 15  ? -5.292  34.587  15.044 1.00 12.28 ? 32  MET A CE  1 
ATOM   66   N N   . ILE A 1 16  ? -0.467  34.140  18.533 1.00 5.00  ? 33  ILE A N   1 
ATOM   67   C CA  . ILE A 1 16  ? -0.094  32.814  19.010 1.00 5.01  ? 33  ILE A CA  1 
ATOM   68   C C   . ILE A 1 16  ? -1.367  31.989  19.099 1.00 6.82  ? 33  ILE A C   1 
ATOM   69   O O   . ILE A 1 16  ? -2.325  32.387  19.770 1.00 6.23  ? 33  ILE A O   1 
ATOM   70   C CB  . ILE A 1 16  ? 0.624   32.890  20.362 1.00 7.13  ? 33  ILE A CB  1 
ATOM   71   C CG1 . ILE A 1 16  ? 1.866   33.802  20.213 1.00 9.15  ? 33  ILE A CG1 1 
ATOM   72   C CG2 . ILE A 1 16  ? 1.004   31.478  20.820 1.00 6.53  ? 33  ILE A CG2 1 
ATOM   73   C CD1 . ILE A 1 16  ? 2.719   33.974  21.458 1.00 9.24  ? 33  ILE A CD1 1 
ATOM   74   N N   . LYS A 1 17  ? -1.381  30.852  18.407 1.00 7.20  ? 34  LYS A N   1 
ATOM   75   C CA  . LYS A 1 17  ? -2.550  29.987  18.330 1.00 6.39  ? 34  LYS A CA  1 
ATOM   76   C C   . LYS A 1 17  ? -2.659  29.151  19.602 1.00 5.81  ? 34  LYS A C   1 
ATOM   77   O O   . LYS A 1 17  ? -1.760  29.134  20.448 1.00 6.46  ? 34  LYS A O   1 
ATOM   78   C CB  . LYS A 1 17  ? -2.447  29.095  17.091 1.00 7.41  ? 34  LYS A CB  1 
ATOM   79   C CG  . LYS A 1 17  ? -2.309  29.847  15.773 1.00 6.86  ? 34  LYS A CG  1 
ATOM   80   C CD  . LYS A 1 17  ? -2.310  28.900  14.575 1.00 8.31  ? 34  LYS A CD  1 
ATOM   81   C CE  . LYS A 1 17  ? -2.243  29.645  13.276 1.00 9.15  ? 34  LYS A CE  1 
ATOM   82   N NZ  . LYS A 1 17  ? -2.283  28.680  12.143 1.00 10.91 ? 34  LYS A NZ  1 
ATOM   83   N N   . PRO A 1 18  ? -3.776  28.450  19.796 1.00 6.01  ? 35  PRO A N   1 
ATOM   84   C CA  . PRO A 1 18  ? -3.953  27.741  21.072 1.00 7.23  ? 35  PRO A CA  1 
ATOM   85   C C   . PRO A 1 18  ? -2.854  26.737  21.366 1.00 6.48  ? 35  PRO A C   1 
ATOM   86   O O   . PRO A 1 18  ? -2.543  26.501  22.543 1.00 7.34  ? 35  PRO A O   1 
ATOM   87   C CB  . PRO A 1 18  ? -5.330  27.078  20.907 1.00 7.32  ? 35  PRO A CB  1 
ATOM   88   C CG  . PRO A 1 18  ? -6.071  28.016  19.971 1.00 8.93  ? 35  PRO A CG  1 
ATOM   89   C CD  . PRO A 1 18  ? -5.001  28.405  18.971 1.00 7.12  ? 35  PRO A CD  1 
ATOM   90   N N   . ASP A 1 19  ? -2.271  26.122  20.339 1.00 7.18  ? 36  ASP A N   1 
ATOM   91   C CA  . ASP A 1 19  ? -1.156  25.210  20.580 1.00 7.50  ? 36  ASP A CA  1 
ATOM   92   C C   . ASP A 1 19  ? 0.049   25.930  21.184 1.00 8.57  ? 36  ASP A C   1 
ATOM   93   O O   . ASP A 1 19  ? 0.768   25.357  22.009 1.00 9.14  ? 36  ASP A O   1 
ATOM   94   C CB  . ASP A 1 19  ? -0.788  24.404  19.327 1.00 7.93  ? 36  ASP A CB  1 
ATOM   95   C CG  . ASP A 1 19  ? -0.560  25.239  18.079 1.00 8.51  ? 36  ASP A CG  1 
ATOM   96   O OD1 . ASP A 1 19  ? -1.261  26.242  17.880 1.00 10.48 ? 36  ASP A OD1 1 
ATOM   97   O OD2 . ASP A 1 19  ? 0.280   24.831  17.251 1.00 9.13  ? 36  ASP A OD2 1 
ATOM   98   N N   . GLY A 1 20  ? 0.297   27.179  20.790 1.00 7.38  ? 37  GLY A N   1 
ATOM   99   C CA  . GLY A 1 20  ? 1.389   27.926  21.402 1.00 7.74  ? 37  GLY A CA  1 
ATOM   100  C C   . GLY A 1 20  ? 1.136   28.238  22.866 1.00 7.12  ? 37  GLY A C   1 
ATOM   101  O O   . GLY A 1 20  ? 2.062   28.221  23.681 1.00 7.92  ? 37  GLY A O   1 
ATOM   102  N N   . ILE A 1 21  ? -0.107  28.578  23.206 1.00 6.41  ? 38  ILE A N   1 
ATOM   103  C CA  . ILE A 1 21  ? -0.475  28.803  24.601 1.00 7.02  ? 38  ILE A CA  1 
ATOM   104  C C   . ILE A 1 21  ? -0.323  27.519  25.395 1.00 6.47  ? 38  ILE A C   1 
ATOM   105  O O   . ILE A 1 21  ? 0.286   27.496  26.471 1.00 7.58  ? 38  ILE A O   1 
ATOM   106  C CB  . ILE A 1 21  ? -1.928  29.314  24.698 1.00 6.66  ? 38  ILE A CB  1 
ATOM   107  C CG1 . ILE A 1 21  ? -2.180  30.542  23.819 1.00 8.70  ? 38  ILE A CG1 1 
ATOM   108  C CG2 . ILE A 1 21  ? -2.292  29.569  26.150 1.00 7.35  ? 38  ILE A CG2 1 
ATOM   109  C CD1 . ILE A 1 21  ? -1.337  31.728  24.121 1.00 10.57 ? 38  ILE A CD1 1 
ATOM   110  N N   . GLN A 1 22  ? -0.905  26.431  24.880 1.00 7.04  ? 39  GLN A N   1 
ATOM   111  C CA  . GLN A 1 22  ? -0.996  25.183  25.627 1.00 7.37  ? 39  GLN A CA  1 
ATOM   112  C C   . GLN A 1 22  ? 0.350   24.505  25.764 1.00 7.34  ? 39  GLN A C   1 
ATOM   113  O O   . GLN A 1 22  ? 0.601   23.839  26.764 1.00 8.06  ? 39  GLN A O   1 
ATOM   114  C CB  . GLN A 1 22  ? -1.972  24.235  24.936 1.00 8.44  ? 39  GLN A CB  1 
ATOM   115  C CG  . GLN A 1 22  ? -3.420  24.619  25.111 1.00 10.42 ? 39  GLN A CG  1 
ATOM   116  C CD  . GLN A 1 22  ? -3.911  24.343  26.517 1.00 10.99 ? 39  GLN A CD  1 
ATOM   117  O OE1 . GLN A 1 22  ? -3.144  23.930  27.384 1.00 12.48 ? 39  GLN A OE1 1 
ATOM   118  N NE2 . GLN A 1 22  ? -5.197  24.551  26.747 1.00 10.98 ? 39  GLN A NE2 1 
ATOM   119  N N   . ARG A 1 23  ? 1.217   24.640  24.768 1.00 6.84  ? 40  ARG A N   1 
ATOM   120  C CA  . ARG A 1 23  ? 2.575   24.129  24.868 1.00 6.60  ? 40  ARG A CA  1 
ATOM   121  C C   . ARG A 1 23  ? 3.474   25.050  25.685 1.00 7.35  ? 40  ARG A C   1 
ATOM   122  O O   . ARG A 1 23  ? 4.641   24.708  25.933 1.00 7.85  ? 40  ARG A O   1 
ATOM   123  C CB  . ARG A 1 23  ? 3.116   23.837  23.464 1.00 6.66  ? 40  ARG A CB  1 
ATOM   124  C CG  . ARG A 1 23  ? 2.322   22.742  22.758 1.00 6.31  ? 40  ARG A CG  1 
ATOM   125  C CD  . ARG A 1 23  ? 2.788   22.506  21.336 1.00 7.44  ? 40  ARG A CD  1 
ATOM   126  N NE  . ARG A 1 23  ? 4.134   21.947  21.313 1.00 8.39  ? 40  ARG A NE  1 
ATOM   127  C CZ  . ARG A 1 23  ? 4.941   21.967  20.264 1.00 8.00  ? 40  ARG A CZ  1 
ATOM   128  N NH1 . ARG A 1 23  ? 4.564   22.487  19.111 1.00 9.24  ? 40  ARG A NH1 1 
ATOM   129  N NH2 . ARG A 1 23  ? 6.165   21.461  20.377 1.00 10.54 ? 40  ARG A NH2 1 
ATOM   130  N N   . GLN A 1 24  ? 2.954   26.208  26.089 1.00 7.42  ? 41  GLN A N   1 
ATOM   131  C CA  . GLN A 1 24  ? 3.637   27.146  26.981 1.00 7.29  ? 41  GLN A CA  1 
ATOM   132  C C   . GLN A 1 24  ? 4.972   27.597  26.405 1.00 7.32  ? 41  GLN A C   1 
ATOM   133  O O   . GLN A 1 24  ? 5.999   27.617  27.083 1.00 8.78  ? 41  GLN A O   1 
ATOM   134  C CB  . GLN A 1 24  ? 3.762   26.604  28.405 1.00 9.61  ? 41  GLN A CB  1 
ATOM   135  C CG  . GLN A 1 24  ? 2.412   26.178  28.973 1.00 9.56  ? 41  GLN A CG  1 
ATOM   136  C CD  . GLN A 1 24  ? 2.325   26.451  30.453 1.00 9.34  ? 41  GLN A CD  1 
ATOM   137  O OE1 . GLN A 1 24  ? 2.594   25.583  31.274 1.00 9.55  ? 41  GLN A OE1 1 
ATOM   138  N NE2 . GLN A 1 24  ? 1.984   27.683  30.802 1.00 10.02 ? 41  GLN A NE2 1 
ATOM   139  N N   . VAL A 1 25  ? 4.923   28.052  25.157 1.00 7.89  ? 42  VAL A N   1 
ATOM   140  C CA  . VAL A 1 25  ? 6.069   28.621  24.464 1.00 7.99  ? 42  VAL A CA  1 
ATOM   141  C C   . VAL A 1 25  ? 5.852   30.100  24.134 1.00 6.89  ? 42  VAL A C   1 
ATOM   142  O O   . VAL A 1 25  ? 6.518   30.652  23.246 1.00 6.13  ? 42  VAL A O   1 
ATOM   143  C CB  . VAL A 1 25  ? 6.438   27.780  23.226 1.00 8.52  ? 42  VAL A CB  1 
ATOM   144  C CG1 . VAL A 1 25  ? 6.929   26.393  23.674 1.00 11.67 ? 42  VAL A CG1 1 
ATOM   145  C CG2 . VAL A 1 25  ? 5.258   27.675  22.267 1.00 9.82  ? 42  VAL A CG2 1 
ATOM   146  N N   . VAL A 1 26  ? 4.936   30.753  24.844 1.00 6.87  ? 43  VAL A N   1 
ATOM   147  C CA  . VAL A 1 26  ? 4.616   32.151  24.554 1.00 5.99  ? 43  VAL A CA  1 
ATOM   148  C C   . VAL A 1 26  ? 5.843   33.038  24.698 1.00 5.89  ? 43  VAL A C   1 
ATOM   149  O O   . VAL A 1 26  ? 6.140   33.862  23.821 1.00 6.25  ? 43  VAL A O   1 
ATOM   150  C CB  . VAL A 1 26  ? 3.465   32.633  25.452 1.00 7.79  ? 43  VAL A CB  1 
ATOM   151  C CG1 . VAL A 1 26  ? 3.296   34.137  25.361 1.00 7.66  ? 43  VAL A CG1 1 
ATOM   152  C CG2 . VAL A 1 26  ? 2.179   31.933  25.057 1.00 7.56  ? 43  VAL A CG2 1 
ATOM   153  N N   . GLY A 1 27  ? 6.554   32.913  25.822 1.00 5.62  ? 44  GLY A N   1 
ATOM   154  C CA  . GLY A 1 27  ? 7.728   33.752  26.023 1.00 5.85  ? 44  GLY A CA  1 
ATOM   155  C C   . GLY A 1 27  ? 8.816   33.520  24.991 1.00 7.81  ? 44  GLY A C   1 
ATOM   156  O O   . GLY A 1 27  ? 9.461   34.462  24.538 1.00 7.18  ? 44  GLY A O   1 
ATOM   157  N N   . GLU A 1 28  ? 9.042   32.264  24.611 1.00 7.11  ? 45  GLU A N   1 
ATOM   158  C CA  . GLU A 1 28  ? 10.048  31.994  23.590 1.00 6.64  ? 45  GLU A CA  1 
ATOM   159  C C   . GLU A 1 28  ? 9.684   32.657  22.269 1.00 6.94  ? 45  GLU A C   1 
ATOM   160  O O   . GLU A 1 28  ? 10.555  33.172  21.559 1.00 7.24  ? 45  GLU A O   1 
ATOM   161  C CB  . GLU A 1 28  ? 10.184  30.499  23.360 1.00 9.32  ? 45  GLU A CB  1 
ATOM   162  C CG  . GLU A 1 28  ? 10.942  29.725  24.370 1.00 13.50 ? 45  GLU A CG  1 
ATOM   163  C CD  . GLU A 1 28  ? 11.241  28.349  23.805 1.00 19.19 ? 45  GLU A CD  1 
ATOM   164  O OE1 . GLU A 1 28  ? 12.153  28.223  22.942 1.00 20.58 ? 45  GLU A OE1 1 
ATOM   165  O OE2 . GLU A 1 28  ? 10.500  27.423  24.145 1.00 19.91 ? 45  GLU A OE2 1 
ATOM   166  N N   . ILE A 1 29  ? 8.407   32.604  21.893 1.00 6.18  ? 46  ILE A N   1 
ATOM   167  C CA  . ILE A 1 29  ? 7.978   33.249  20.654 1.00 6.86  ? 46  ILE A CA  1 
ATOM   168  C C   . ILE A 1 29  ? 8.219   34.751  20.724 1.00 6.37  ? 46  ILE A C   1 
ATOM   169  O O   . ILE A 1 29  ? 8.809   35.347  19.816 1.00 7.05  ? 46  ILE A O   1 
ATOM   170  C CB  . ILE A 1 29  ? 6.498   32.935  20.367 1.00 6.72  ? 46  ILE A CB  1 
ATOM   171  C CG1 . ILE A 1 29  ? 6.332   31.448  20.047 1.00 6.08  ? 46  ILE A CG1 1 
ATOM   172  C CG2 . ILE A 1 29  ? 5.994   33.823  19.235 1.00 7.93  ? 46  ILE A CG2 1 
ATOM   173  C CD1 . ILE A 1 29  ? 4.879   30.971  20.010 1.00 9.07  ? 46  ILE A CD1 1 
ATOM   174  N N   . ILE A 1 30  ? 7.757   35.389  21.803 1.00 7.08  ? 47  ILE A N   1 
ATOM   175  C CA  . ILE A 1 30  ? 7.948   36.826  21.945 1.00 5.97  ? 47  ILE A CA  1 
ATOM   176  C C   . ILE A 1 30  ? 9.435   37.177  21.884 1.00 5.74  ? 47  ILE A C   1 
ATOM   177  O O   . ILE A 1 30  ? 9.831   38.147  21.224 1.00 6.64  ? 47  ILE A O   1 
ATOM   178  C CB  . ILE A 1 30  ? 7.290   37.306  23.252 1.00 6.45  ? 47  ILE A CB  1 
ATOM   179  C CG1 . ILE A 1 30  ? 5.757   37.242  23.151 1.00 8.01  ? 47  ILE A CG1 1 
ATOM   180  C CG2 . ILE A 1 30  ? 7.755   38.707  23.603 1.00 8.08  ? 47  ILE A CG2 1 
ATOM   181  C CD1 . ILE A 1 30  ? 5.044   37.415  24.453 1.00 9.15  ? 47  ILE A CD1 1 
ATOM   182  N N   . SER A 1 31  ? 10.284  36.375  22.541 1.00 6.53  ? 48  SER A N   1 
ATOM   183  C CA  . SER A 1 31  ? 11.719  36.669  22.572 1.00 5.81  ? 48  SER A CA  1 
ATOM   184  C C   . SER A 1 31  ? 12.323  36.681  21.174 1.00 5.78  ? 48  SER A C   1 
ATOM   185  O O   . SER A 1 31  ? 13.256  37.441  20.914 1.00 6.75  ? 48  SER A O   1 
ATOM   186  C CB  . SER A 1 31  ? 12.448  35.662  23.452 1.00 6.99  ? 48  SER A CB  1 
ATOM   187  O OG  . SER A 1 31  ? 12.185  35.884  24.829 1.00 7.08  ? 48  SER A OG  1 
ATOM   188  N N   . ARG A 1 32  ? 11.847  35.811  20.279 1.00 5.81  ? 49  ARG A N   1 
ATOM   189  C CA  . ARG A 1 32  ? 12.397  35.794  18.925 1.00 5.79  ? 49  ARG A CA  1 
ATOM   190  C C   . ARG A 1 32  ? 12.176  37.116  18.208 1.00 6.31  ? 49  ARG A C   1 
ATOM   191  O O   . ARG A 1 32  ? 13.035  37.562  17.441 1.00 7.84  ? 49  ARG A O   1 
ATOM   192  C CB  . ARG A 1 32  ? 11.765  34.673  18.121 1.00 7.89  ? 49  ARG A CB  1 
ATOM   193  C CG  . ARG A 1 32  ? 12.219  33.303  18.563 1.00 11.05 ? 49  ARG A CG  1 
ATOM   194  C CD  . ARG A 1 32  ? 11.884  32.268  17.511 1.00 15.46 ? 49  ARG A CD  1 
ATOM   195  N NE  . ARG A 1 32  ? 12.377  30.964  17.914 1.00 13.88 ? 49  ARG A NE  1 
ATOM   196  C CZ  . ARG A 1 32  ? 12.771  30.016  17.082 1.00 12.09 ? 49  ARG A CZ  1 
ATOM   197  N NH1 . ARG A 1 32  ? 12.754  30.193  15.772 1.00 13.77 ? 49  ARG A NH1 1 
ATOM   198  N NH2 . ARG A 1 32  ? 13.223  28.872  17.583 1.00 13.53 ? 49  ARG A NH2 1 
ATOM   199  N N   . PHE A 1 33  ? 11.014  37.745  18.424 1.00 6.07  ? 50  PHE A N   1 
ATOM   200  C CA  . PHE A 1 33  ? 10.739  39.034  17.796 1.00 6.37  ? 50  PHE A CA  1 
ATOM   201  C C   . PHE A 1 33  ? 11.451  40.183  18.497 1.00 6.13  ? 50  PHE A C   1 
ATOM   202  O O   . PHE A 1 33  ? 12.030  41.052  17.823 1.00 6.85  ? 50  PHE A O   1 
ATOM   203  C CB  . PHE A 1 33  ? 9.227   39.250  17.688 1.00 6.90  ? 50  PHE A CB  1 
ATOM   204  C CG  . PHE A 1 33  ? 8.566   38.249  16.776 1.00 7.75  ? 50  PHE A CG  1 
ATOM   205  C CD1 . PHE A 1 33  ? 8.778   38.291  15.399 1.00 8.26  ? 50  PHE A CD1 1 
ATOM   206  C CD2 . PHE A 1 33  ? 7.792   37.229  17.290 1.00 9.46  ? 50  PHE A CD2 1 
ATOM   207  C CE1 . PHE A 1 33  ? 8.201   37.352  14.569 1.00 8.93  ? 50  PHE A CE1 1 
ATOM   208  C CE2 . PHE A 1 33  ? 7.226   36.295  16.463 1.00 8.96  ? 50  PHE A CE2 1 
ATOM   209  C CZ  . PHE A 1 33  ? 7.417   36.364  15.099 1.00 7.56  ? 50  PHE A CZ  1 
ATOM   210  N N   . GLU A 1 34  ? 11.481  40.169  19.837 1.00 6.83  ? 51  GLU A N   1 
ATOM   211  C CA  . GLU A 1 34  ? 12.232  41.180  20.575 1.00 6.91  ? 51  GLU A CA  1 
ATOM   212  C C   . GLU A 1 34  ? 13.703  41.149  20.196 1.00 8.54  ? 51  GLU A C   1 
ATOM   213  O O   . GLU A 1 34  ? 14.361  42.186  20.208 1.00 7.78  ? 51  GLU A O   1 
ATOM   214  C CB  . GLU A 1 34  ? 12.122  40.949  22.084 1.00 6.52  ? 51  GLU A CB  1 
ATOM   215  C CG  . GLU A 1 34  ? 10.788  41.299  22.717 1.00 6.17  ? 51  GLU A CG  1 
ATOM   216  C CD  . GLU A 1 34  ? 10.844  41.087  24.202 1.00 7.55  ? 51  GLU A CD  1 
ATOM   217  O OE1 . GLU A 1 34  ? 11.017  39.908  24.598 1.00 8.84  ? 51  GLU A OE1 1 
ATOM   218  O OE2 . GLU A 1 34  ? 10.743  42.078  24.964 1.00 8.38  ? 51  GLU A OE2 1 
ATOM   219  N N   . LYS A 1 35  ? 14.231  39.967  19.867 1.00 6.80  ? 52  LYS A N   1 
ATOM   220  C CA  . LYS A 1 35  ? 15.662  39.829  19.617 1.00 6.98  ? 52  LYS A CA  1 
ATOM   221  C C   . LYS A 1 35  ? 16.120  40.691  18.450 1.00 7.13  ? 52  LYS A C   1 
ATOM   222  O O   . LYS A 1 35  ? 17.288  41.099  18.405 1.00 7.62  ? 52  LYS A O   1 
ATOM   223  C CB  . LYS A 1 35  ? 15.977  38.359  19.347 1.00 9.02  ? 52  LYS A CB  1 
ATOM   224  C CG  . LYS A 1 35  ? 17.447  38.023  19.415 1.00 11.17 ? 52  LYS A CG  1 
ATOM   225  C CD  . LYS A 1 35  ? 17.666  36.558  19.079 1.00 14.53 ? 52  LYS A CD  1 
ATOM   226  C CE  . LYS A 1 35  ? 19.014  36.091  19.545 1.00 21.09 ? 52  LYS A CE  1 
ATOM   227  N NZ  . LYS A 1 35  ? 18.999  35.891  21.015 1.00 25.84 ? 52  LYS A NZ  1 
ATOM   228  N N   . ARG A 1 36  ? 15.230  40.970  17.493 1.00 6.28  ? 53  ARG A N   1 
ATOM   229  C CA  . ARG A 1 36  ? 15.565  41.789  16.336 1.00 6.24  ? 53  ARG A CA  1 
ATOM   230  C C   . ARG A 1 36  ? 15.296  43.268  16.577 1.00 5.62  ? 53  ARG A C   1 
ATOM   231  O O   . ARG A 1 36  ? 15.430  44.068  15.656 1.00 7.66  ? 53  ARG A O   1 
ATOM   232  C CB  . ARG A 1 36  ? 14.833  41.320  15.077 1.00 6.78  ? 53  ARG A CB  1 
ATOM   233  C CG  . ARG A 1 36  ? 15.189  39.900  14.645 1.00 7.38  ? 53  ARG A CG  1 
ATOM   234  C CD  . ARG A 1 36  ? 14.574  39.499  13.322 1.00 6.45  ? 53  ARG A CD  1 
ATOM   235  N NE  . ARG A 1 36  ? 15.157  40.221  12.199 1.00 6.61  ? 53  ARG A NE  1 
ATOM   236  C CZ  . ARG A 1 36  ? 14.830  40.007  10.933 1.00 7.26  ? 53  ARG A CZ  1 
ATOM   237  N NH1 . ARG A 1 36  ? 13.881  39.150  10.604 1.00 7.80  ? 53  ARG A NH1 1 
ATOM   238  N NH2 . ARG A 1 36  ? 15.474  40.666  9.971  1.00 8.01  ? 53  ARG A NH2 1 
ATOM   239  N N   . GLY A 1 37  ? 14.910  43.646  17.791 1.00 5.64  ? 54  GLY A N   1 
ATOM   240  C CA  . GLY A 1 37  ? 14.561  45.023  18.058 1.00 6.67  ? 54  GLY A CA  1 
ATOM   241  C C   . GLY A 1 37  ? 13.191  45.397  17.559 1.00 6.41  ? 54  GLY A C   1 
ATOM   242  O O   . GLY A 1 37  ? 12.910  46.585  17.370 1.00 8.33  ? 54  GLY A O   1 
ATOM   243  N N   . TYR A 1 38  ? 12.328  44.413  17.326 1.00 6.04  ? 55  TYR A N   1 
ATOM   244  C CA  . TYR A 1 38  ? 10.955  44.728  16.990 1.00 5.81  ? 55  TYR A CA  1 
ATOM   245  C C   . TYR A 1 38  ? 10.244  45.177  18.260 1.00 6.89  ? 55  TYR A C   1 
ATOM   246  O O   . TYR A 1 38  ? 10.484  44.644  19.351 1.00 8.19  ? 55  TYR A O   1 
ATOM   247  C CB  . TYR A 1 38  ? 10.242  43.527  16.382 1.00 5.98  ? 55  TYR A CB  1 
ATOM   248  C CG  . TYR A 1 38  ? 10.766  43.084  15.026 1.00 5.84  ? 55  TYR A CG  1 
ATOM   249  C CD1 . TYR A 1 38  ? 11.302  43.992  14.108 1.00 7.41  ? 55  TYR A CD1 1 
ATOM   250  C CD2 . TYR A 1 38  ? 10.701  41.750  14.647 1.00 5.71  ? 55  TYR A CD2 1 
ATOM   251  C CE1 . TYR A 1 38  ? 11.755  43.572  12.867 1.00 8.49  ? 55  TYR A CE1 1 
ATOM   252  C CE2 . TYR A 1 38  ? 11.169  41.326  13.422 1.00 6.84  ? 55  TYR A CE2 1 
ATOM   253  C CZ  . TYR A 1 38  ? 11.688  42.233  12.540 1.00 6.98  ? 55  TYR A CZ  1 
ATOM   254  O OH  . TYR A 1 38  ? 12.121  41.775  11.335 1.00 8.13  ? 55  TYR A OH  1 
ATOM   255  N N   . ARG A 1 39  ? 9.380   46.169  18.113 1.00 5.97  ? 56  ARG A N   1 
ATOM   256  C CA  . ARG A 1 39  ? 8.718   46.807  19.235 1.00 5.86  ? 56  ARG A CA  1 
ATOM   257  C C   . ARG A 1 39  ? 7.320   46.241  19.408 1.00 6.23  ? 56  ARG A C   1 
ATOM   258  O O   . ARG A 1 39  ? 6.575   46.128  18.433 1.00 7.05  ? 56  ARG A O   1 
ATOM   259  C CB  . ARG A 1 39  ? 8.621   48.306  18.966 1.00 6.22  ? 56  ARG A CB  1 
ATOM   260  C CG  . ARG A 1 39  ? 8.061   49.074  20.132 1.00 7.55  ? 56  ARG A CG  1 
ATOM   261  C CD  . ARG A 1 39  ? 8.041   50.595  19.875 1.00 6.69  ? 56  ARG A CD  1 
ATOM   262  N NE  . ARG A 1 39  ? 7.093   50.969  18.827 1.00 6.83  ? 56  ARG A NE  1 
ATOM   263  C CZ  . ARG A 1 39  ? 5.804   51.188  19.036 1.00 8.14  ? 56  ARG A CZ  1 
ATOM   264  N NH1 . ARG A 1 39  ? 5.267   51.020  20.229 1.00 10.55 ? 56  ARG A NH1 1 
ATOM   265  N NH2 . ARG A 1 39  ? 5.039   51.593  18.025 1.00 10.49 ? 56  ARG A NH2 1 
ATOM   266  N N   . ILE A 1 40  ? 6.987   45.858  20.642 1.00 6.69  ? 57  ILE A N   1 
ATOM   267  C CA  . ILE A 1 40  ? 5.628   45.439  20.974 1.00 7.32  ? 57  ILE A CA  1 
ATOM   268  C C   . ILE A 1 40  ? 4.744   46.677  20.993 1.00 7.13  ? 57  ILE A C   1 
ATOM   269  O O   . ILE A 1 40  ? 4.855   47.517  21.887 1.00 8.10  ? 57  ILE A O   1 
ATOM   270  C CB  . ILE A 1 40  ? 5.558   44.711  22.319 1.00 7.37  ? 57  ILE A CB  1 
ATOM   271  C CG1 . ILE A 1 40  ? 6.566   43.556  22.406 1.00 7.80  ? 57  ILE A CG1 1 
ATOM   272  C CG2 . ILE A 1 40  ? 4.135   44.142  22.521 1.00 7.10  ? 57  ILE A CG2 1 
ATOM   273  C CD1 . ILE A 1 40  ? 6.700   42.966  23.797 1.00 8.43  ? 57  ILE A CD1 1 
ATOM   274  N N   . ALA A 1 41  ? 3.852   46.780  20.022 1.00 5.86  ? 58  ALA A N   1 
ATOM   275  C CA  . ALA A 1 41  ? 2.922   47.897  19.980 1.00 5.95  ? 58  ALA A CA  1 
ATOM   276  C C   . ALA A 1 41  ? 1.565   47.548  20.573 1.00 6.99  ? 58  ALA A C   1 
ATOM   277  O O   . ALA A 1 41  ? 0.828   48.450  20.960 1.00 9.06  ? 58  ALA A O   1 
ATOM   278  C CB  . ALA A 1 41  ? 2.721   48.381  18.537 1.00 7.41  ? 58  ALA A CB  1 
ATOM   279  N N   . ALA A 1 42  ? 1.222   46.271  20.661 1.00 6.76  ? 59  ALA A N   1 
ATOM   280  C CA  . ALA A 1 42  ? -0.040  45.860  21.265 1.00 8.51  ? 59  ALA A CA  1 
ATOM   281  C C   . ALA A 1 42  ? 0.092   44.401  21.650 1.00 7.08  ? 59  ALA A C   1 
ATOM   282  O O   . ALA A 1 42  ? 0.811   43.642  20.998 1.00 6.92  ? 59  ALA A O   1 
ATOM   283  C CB  . ALA A 1 42  ? -1.211  46.024  20.296 1.00 9.18  ? 59  ALA A CB  1 
ATOM   284  N N   . MET A 1 43  ? -0.640  44.004  22.685 1.00 7.35  ? 60  MET A N   1 
ATOM   285  C CA  . MET A 1 43  ? -0.647  42.620  23.131 1.00 7.42  ? 60  MET A CA  1 
ATOM   286  C C   . MET A 1 43  ? -1.887  42.414  23.989 1.00 8.48  ? 60  MET A C   1 
ATOM   287  O O   . MET A 1 43  ? -2.211  43.256  24.834 1.00 9.17  ? 60  MET A O   1 
ATOM   288  C CB  . MET A 1 43  ? 0.636   42.329  23.914 1.00 7.04  ? 60  MET A CB  1 
ATOM   289  C CG  . MET A 1 43  ? 0.849   40.871  24.289 1.00 10.31 ? 60  MET A CG  1 
ATOM   290  S SD  . MET A 1 43  ? 2.558   40.548  24.800 1.00 12.02 ? 60  MET A SD  1 
ATOM   291  C CE  . MET A 1 43  ? 3.394   40.419  23.222 1.00 11.34 ? 60  MET A CE  1 
ATOM   292  N N   . LYS A 1 44  ? -2.580  41.298  23.763 1.00 7.70  ? 61  LYS A N   1 
ATOM   293  C CA  . LYS A 1 44  ? -3.813  40.995  24.482 1.00 9.83  ? 61  LYS A CA  1 
ATOM   294  C C   . LYS A 1 44  ? -4.038  39.490  24.438 1.00 6.70  ? 61  LYS A C   1 
ATOM   295  O O   . LYS A 1 44  ? -4.058  38.907  23.355 1.00 9.12  ? 61  LYS A O   1 
ATOM   296  C CB  . LYS A 1 44  ? -4.997  41.708  23.797 1.00 11.88 ? 61  LYS A CB  1 
ATOM   297  C CG  . LYS A 1 44  ? -6.380  41.231  24.227 1.00 18.16 ? 61  LYS A CG  1 
ATOM   298  C CD  . LYS A 1 44  ? -7.533  42.158  23.791 1.00 21.54 ? 61  LYS A CD  1 
ATOM   299  C CE  . LYS A 1 44  ? -7.419  42.634  22.376 1.00 24.25 ? 61  LYS A CE  1 
ATOM   300  N NZ  . LYS A 1 44  ? -8.585  43.521  22.004 1.00 23.77 ? 61  LYS A NZ  1 
ATOM   301  N N   . LEU A 1 45  ? -4.250  38.867  25.601 1.00 7.39  ? 62  LEU A N   1 
ATOM   302  C CA  . LEU A 1 45  ? -4.722  37.490  25.643 1.00 6.73  ? 62  LEU A CA  1 
ATOM   303  C C   . LEU A 1 45  ? -6.235  37.501  25.581 1.00 7.66  ? 62  LEU A C   1 
ATOM   304  O O   . LEU A 1 45  ? -6.874  38.238  26.326 1.00 7.74  ? 62  LEU A O   1 
ATOM   305  C CB  . LEU A 1 45  ? -4.306  36.790  26.936 1.00 7.68  ? 62  LEU A CB  1 
ATOM   306  C CG  . LEU A 1 45  ? -4.685  35.311  27.009 1.00 8.29  ? 62  LEU A CG  1 
ATOM   307  C CD1 . LEU A 1 45  ? -3.680  34.453  26.296 1.00 10.88 ? 62  LEU A CD1 1 
ATOM   308  C CD2 . LEU A 1 45  ? -4.845  34.856  28.429 1.00 9.33  ? 62  LEU A CD2 1 
ATOM   309  N N   . THR A 1 46  ? -6.794  36.671  24.719 1.00 8.20  ? 63  THR A N   1 
ATOM   310  C CA  . THR A 1 46  ? -8.234  36.504  24.633 1.00 7.17  ? 63  THR A CA  1 
ATOM   311  C C   . THR A 1 46  ? -8.500  35.035  24.357 1.00 9.80  ? 63  THR A C   1 
ATOM   312  O O   . THR A 1 46  ? -7.573  34.237  24.221 1.00 8.36  ? 63  THR A O   1 
ATOM   313  C CB  . THR A 1 46  ? -8.866  37.425  23.580 1.00 9.88  ? 63  THR A CB  1 
ATOM   314  O OG1 . THR A 1 46  ? -10.292 37.364  23.695 1.00 10.92 ? 63  THR A OG1 1 
ATOM   315  C CG2 . THR A 1 46  ? -8.475  37.042  22.174 1.00 9.60  ? 63  THR A CG2 1 
ATOM   316  N N   . ILE A 1 47  ? -9.773  34.672  24.307 1.00 8.93  ? 64  ILE A N   1 
ATOM   317  C CA  . ILE A 1 47  ? -10.201 33.366  23.821 1.00 9.63  ? 64  ILE A CA  1 
ATOM   318  C C   . ILE A 1 47  ? -10.936 33.620  22.516 1.00 8.72  ? 64  ILE A C   1 
ATOM   319  O O   . ILE A 1 47  ? -11.948 34.335  22.491 1.00 10.06 ? 64  ILE A O   1 
ATOM   320  C CB  . ILE A 1 47  ? -11.052 32.601  24.847 1.00 8.54  ? 64  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 47  ? -10.168 32.149  26.015 1.00 12.33 ? 64  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 47  ? -11.706 31.392  24.174 1.00 12.01 ? 64  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 47  ? -10.915 31.542  27.191 1.00 13.60 ? 64  ILE A CD1 1 
ATOM   324  N N   . ALA A 1 48  ? -10.422 33.038  21.435 1.00 8.63  ? 65  ALA A N   1 
ATOM   325  C CA  . ALA A 1 48  ? -11.004 33.248  20.125 1.00 8.43  ? 65  ALA A CA  1 
ATOM   326  C C   . ALA A 1 48  ? -12.302 32.468  20.028 1.00 8.25  ? 65  ALA A C   1 
ATOM   327  O O   . ALA A 1 48  ? -12.392 31.326  20.484 1.00 10.10 ? 65  ALA A O   1 
ATOM   328  C CB  . ALA A 1 48  ? -10.022 32.822  19.038 1.00 9.54  ? 65  ALA A CB  1 
ATOM   329  N N   . THR A 1 49  ? -13.313 33.096  19.444 1.00 9.82  ? 66  THR A N   1 
ATOM   330  C CA  . THR A 1 49  ? -14.625 32.499  19.277 1.00 11.65 ? 66  THR A CA  1 
ATOM   331  C C   . THR A 1 49  ? -14.950 32.415  17.792 1.00 10.71 ? 66  THR A C   1 
ATOM   332  O O   . THR A 1 49  ? -14.324 33.095  16.968 1.00 10.26 ? 66  THR A O   1 
ATOM   333  C CB  . THR A 1 49  ? -15.724 33.302  19.995 1.00 13.28 ? 66  THR A CB  1 
ATOM   334  O OG1 . THR A 1 49  ? -15.841 34.600  19.398 1.00 15.79 ? 66  THR A OG1 1 
ATOM   335  C CG2 . THR A 1 49  ? -15.416 33.443  21.493 1.00 16.59 ? 66  THR A CG2 1 
ATOM   336  N N   . PRO A 1 50  ? -15.915 31.572  17.414 1.00 11.78 ? 67  PRO A N   1 
ATOM   337  C CA  . PRO A 1 50  ? -16.199 31.389  15.981 1.00 10.96 ? 67  PRO A CA  1 
ATOM   338  C C   . PRO A 1 50  ? -16.518 32.669  15.227 1.00 10.57 ? 67  PRO A C   1 
ATOM   339  O O   . PRO A 1 50  ? -16.055 32.831  14.090 1.00 12.36 ? 67  PRO A O   1 
ATOM   340  C CB  . PRO A 1 50  ? -17.369 30.390  15.982 1.00 11.11 ? 67  PRO A CB  1 
ATOM   341  C CG  . PRO A 1 50  ? -17.134 29.577  17.196 1.00 12.78 ? 67  PRO A CG  1 
ATOM   342  C CD  . PRO A 1 50  ? -16.560 30.526  18.233 1.00 10.70 ? 67  PRO A CD  1 
ATOM   343  N N   . ALA A 1 51  ? -17.256 33.608  15.823 1.00 12.02 ? 68  ALA A N   1 
ATOM   344  C CA  . ALA A 1 51  ? -17.684 34.774  15.057 1.00 10.71 ? 68  ALA A CA  1 
ATOM   345  C C   . ALA A 1 51  ? -16.498 35.633  14.643 1.00 10.25 ? 68  ALA A C   1 
ATOM   346  O O   . ALA A 1 51  ? -16.416 36.080  13.494 1.00 13.14 ? 68  ALA A O   1 
ATOM   347  C CB  . ALA A 1 51  ? -18.698 35.602  15.838 1.00 14.72 ? 68  ALA A CB  1 
ATOM   348  N N   . ILE A 1 52  ? -15.582 35.897  15.573 1.00 8.78  ? 69  ILE A N   1 
ATOM   349  C CA  . ILE A 1 52  ? -14.409 36.678  15.210 1.00 10.08 ? 69  ILE A CA  1 
ATOM   350  C C   . ILE A 1 52  ? -13.482 35.869  14.307 1.00 8.80  ? 69  ILE A C   1 
ATOM   351  O O   . ILE A 1 52  ? -12.856 36.420  13.410 1.00 9.75  ? 69  ILE A O   1 
ATOM   352  C CB  . ILE A 1 52  ? -13.690 37.241  16.453 1.00 13.73 ? 69  ILE A CB  1 
ATOM   353  C CG1 . ILE A 1 52  ? -12.709 38.336  16.034 1.00 13.22 ? 69  ILE A CG1 1 
ATOM   354  C CG2 . ILE A 1 52  ? -12.957 36.153  17.194 1.00 12.67 ? 69  ILE A CG2 1 
ATOM   355  C CD1 . ILE A 1 52  ? -12.293 39.264  17.150 1.00 14.21 ? 69  ILE A CD1 1 
ATOM   356  N N   . LEU A 1 53  ? -13.394 34.556  14.507 1.00 9.37  ? 70  LEU A N   1 
ATOM   357  C CA  . LEU A 1 53  ? -12.550 33.740  13.643 1.00 10.14 ? 70  LEU A CA  1 
ATOM   358  C C   . LEU A 1 53  ? -13.071 33.697  12.213 1.00 8.90  ? 70  LEU A C   1 
ATOM   359  O O   . LEU A 1 53  ? -12.269 33.675  11.270 1.00 9.94  ? 70  LEU A O   1 
ATOM   360  C CB  . LEU A 1 53  ? -12.402 32.338  14.219 1.00 9.17  ? 70  LEU A CB  1 
ATOM   361  C CG  . LEU A 1 53  ? -11.530 32.259  15.472 1.00 9.16  ? 70  LEU A CG  1 
ATOM   362  C CD1 . LEU A 1 53  ? -11.750 30.911  16.169 1.00 9.22  ? 70  LEU A CD1 1 
ATOM   363  C CD2 . LEU A 1 53  ? -10.038 32.490  15.157 1.00 9.78  ? 70  LEU A CD2 1 
ATOM   364  N N   . GLU A 1 54  ? -14.396 33.707  12.027 1.00 9.84  ? 71  GLU A N   1 
ATOM   365  C CA  . GLU A 1 54  ? -14.945 33.766  10.675 1.00 12.69 ? 71  GLU A CA  1 
ATOM   366  C C   . GLU A 1 54  ? -14.509 35.038  9.963  1.00 14.77 ? 71  GLU A C   1 
ATOM   367  O O   . GLU A 1 54  ? -14.236 35.025  8.758  1.00 15.22 ? 71  GLU A O   1 
ATOM   368  C CB  . GLU A 1 54  ? -16.465 33.721  10.730 1.00 18.76 ? 71  GLU A CB  1 
ATOM   369  C CG  . GLU A 1 54  ? -17.029 32.358  10.987 1.00 30.80 ? 71  GLU A CG  1 
ATOM   370  C CD  . GLU A 1 54  ? -18.495 32.409  11.353 1.00 37.23 ? 71  GLU A CD  1 
ATOM   371  O OE1 . GLU A 1 54  ? -19.196 33.364  10.922 1.00 40.03 ? 71  GLU A OE1 1 
ATOM   372  O OE2 . GLU A 1 54  ? -18.938 31.502  12.084 1.00 37.26 ? 71  GLU A OE2 1 
ATOM   373  N N   . GLU A 1 55  ? -14.459 36.152  10.692 1.00 13.31 ? 72  GLU A N   1 
ATOM   374  C CA  . GLU A 1 55  ? -13.983 37.401  10.116 1.00 12.54 ? 72  GLU A CA  1 
ATOM   375  C C   . GLU A 1 55  ? -12.492 37.343  9.825  1.00 9.42  ? 72  GLU A C   1 
ATOM   376  O O   . GLU A 1 55  ? -12.030 37.794  8.770  1.00 10.87 ? 72  GLU A O   1 
ATOM   377  C CB  . GLU A 1 55  ? -14.237 38.518  11.115 1.00 19.55 ? 72  GLU A CB  1 
ATOM   378  C CG  . GLU A 1 55  ? -15.676 38.774  11.360 1.00 28.44 ? 72  GLU A CG  1 
ATOM   379  C CD  . GLU A 1 55  ? -16.101 40.032  10.683 1.00 38.95 ? 72  GLU A CD  1 
ATOM   380  O OE1 . GLU A 1 55  ? -16.153 40.028  9.435  1.00 42.01 ? 72  GLU A OE1 1 
ATOM   381  O OE2 . GLU A 1 55  ? -16.327 41.025  11.405 1.00 42.52 ? 72  GLU A OE2 1 
ATOM   382  N N   . HIS A 1 56  ? -11.720 36.807  10.759 1.00 10.05 ? 73  HIS A N   1 
ATOM   383  C CA  . HIS A 1 56  ? -10.276 36.730  10.570 1.00 8.32  ? 73  HIS A CA  1 
ATOM   384  C C   . HIS A 1 56  ? -9.949  35.913  9.330  1.00 8.81  ? 73  HIS A C   1 
ATOM   385  O O   . HIS A 1 56  ? -9.086  36.288  8.528  1.00 12.54 ? 73  HIS A O   1 
ATOM   386  C CB  . HIS A 1 56  ? -9.670  36.084  11.808 1.00 9.47  ? 73  HIS A CB  1 
ATOM   387  C CG  . HIS A 1 56  ? -8.194  35.895  11.720 1.00 9.04  ? 73  HIS A CG  1 
ATOM   388  N ND1 . HIS A 1 56  ? -7.303  36.920  11.926 1.00 9.92  ? 73  HIS A ND1 1 
ATOM   389  C CD2 . HIS A 1 56  ? -7.454  34.803  11.423 1.00 12.01 ? 73  HIS A CD2 1 
ATOM   390  C CE1 . HIS A 1 56  ? -6.076  36.467  11.777 1.00 11.36 ? 73  HIS A CE1 1 
ATOM   391  N NE2 . HIS A 1 56  ? -6.137  35.185  11.473 1.00 12.18 ? 73  HIS A NE2 1 
ATOM   392  N N   . TYR A 1 57  ? -10.647 34.795  9.152  1.00 9.51  ? 74  TYR A N   1 
ATOM   393  C CA  . TYR A 1 57  ? -10.429 33.882  8.039  1.00 9.98  ? 74  TYR A CA  1 
ATOM   394  C C   . TYR A 1 57  ? -11.441 34.092  6.917  1.00 10.94 ? 74  TYR A C   1 
ATOM   395  O O   . TYR A 1 57  ? -11.842 33.137  6.242  1.00 14.63 ? 74  TYR A O   1 
ATOM   396  C CB  . TYR A 1 57  ? -10.467 32.442  8.548  1.00 10.11 ? 74  TYR A CB  1 
ATOM   397  C CG  . TYR A 1 57  ? -9.288  32.047  9.407  1.00 11.16 ? 74  TYR A CG  1 
ATOM   398  C CD1 . TYR A 1 57  ? -7.995  32.067  8.893  1.00 11.12 ? 74  TYR A CD1 1 
ATOM   399  C CD2 . TYR A 1 57  ? -9.461  31.654  10.730 1.00 14.00 ? 74  TYR A CD2 1 
ATOM   400  C CE1 . TYR A 1 57  ? -6.922  31.705  9.665  1.00 12.23 ? 74  TYR A CE1 1 
ATOM   401  C CE2 . TYR A 1 57  ? -8.383  31.310  11.511 1.00 16.11 ? 74  TYR A CE2 1 
ATOM   402  C CZ  . TYR A 1 57  ? -7.118  31.337  10.973 1.00 13.99 ? 74  TYR A CZ  1 
ATOM   403  O OH  . TYR A 1 57  ? -6.056  30.981  11.771 1.00 15.64 ? 74  TYR A OH  1 
ATOM   404  N N   . ALA A 1 58  ? -11.857 35.338  6.696  1.00 11.81 ? 75  ALA A N   1 
ATOM   405  C CA  . ALA A 1 58  ? -12.881 35.616  5.695  1.00 13.84 ? 75  ALA A CA  1 
ATOM   406  C C   . ALA A 1 58  ? -12.448 35.163  4.304  1.00 14.98 ? 75  ALA A C   1 
ATOM   407  O O   . ALA A 1 58  ? -13.291 34.793  3.481  1.00 17.27 ? 75  ALA A O   1 
ATOM   408  C CB  . ALA A 1 58  ? -13.184 37.112  5.711  1.00 16.01 ? 75  ALA A CB  1 
ATOM   409  N N   . GLU A 1 59  ? -11.143 35.166  4.025  1.00 17.14 ? 76  GLU A N   1 
ATOM   410  C CA  . GLU A 1 59  ? -10.674 34.728  2.712  1.00 18.39 ? 76  GLU A CA  1 
ATOM   411  C C   . GLU A 1 59  ? -11.010 33.269  2.436  1.00 19.43 ? 76  GLU A C   1 
ATOM   412  O O   . GLU A 1 59  ? -10.979 32.843  1.273  1.00 19.62 ? 76  GLU A O   1 
ATOM   413  C CB  . GLU A 1 59  ? -9.160  34.913  2.589  1.00 19.88 ? 76  GLU A CB  1 
ATOM   414  C CG  . GLU A 1 59  ? -8.347  34.021  3.505  1.00 22.37 ? 76  GLU A CG  1 
ATOM   415  C CD  . GLU A 1 59  ? -6.895  34.449  3.588  1.00 27.80 ? 76  GLU A CD  1 
ATOM   416  O OE1 . GLU A 1 59  ? -6.131  34.183  2.633  1.00 28.99 ? 76  GLU A OE1 1 
ATOM   417  O OE2 . GLU A 1 59  ? -6.526  35.079  4.601  1.00 29.05 ? 76  GLU A OE2 1 
ATOM   418  N N   . HIS A 1 60  ? -11.304 32.490  3.474  1.00 15.60 ? 77  HIS A N   1 
ATOM   419  C CA  . HIS A 1 60  ? -11.608 31.072  3.334  1.00 15.81 ? 77  HIS A CA  1 
ATOM   420  C C   . HIS A 1 60  ? -13.099 30.771  3.420  1.00 16.35 ? 77  HIS A C   1 
ATOM   421  O O   . HIS A 1 60  ? -13.477 29.599  3.527  1.00 15.81 ? 77  HIS A O   1 
ATOM   422  C CB  . HIS A 1 60  ? -10.873 30.264  4.396  1.00 18.09 ? 77  HIS A CB  1 
ATOM   423  C CG  . HIS A 1 60  ? -9.388  30.412  4.350  1.00 18.84 ? 77  HIS A CG  1 
ATOM   424  N ND1 . HIS A 1 60  ? -8.677  30.424  3.170  1.00 19.77 ? 77  HIS A ND1 1 
ATOM   425  C CD2 . HIS A 1 60  ? -8.477  30.547  5.343  1.00 19.09 ? 77  HIS A CD2 1 
ATOM   426  C CE1 . HIS A 1 60  ? -7.390  30.561  3.439  1.00 20.33 ? 77  HIS A CE1 1 
ATOM   427  N NE2 . HIS A 1 60  ? -7.244  30.635  4.750  1.00 19.37 ? 77  HIS A NE2 1 
ATOM   428  N N   . LYS A 1 61  ? -13.953 31.788  3.376  1.00 17.38 ? 78  LYS A N   1 
ATOM   429  C CA  . LYS A 1 61  ? -15.387 31.557  3.472  1.00 16.76 ? 78  LYS A CA  1 
ATOM   430  C C   . LYS A 1 61  ? -15.844 30.557  2.417  1.00 18.12 ? 78  LYS A C   1 
ATOM   431  O O   . LYS A 1 61  ? -15.482 30.659  1.239  1.00 20.04 ? 78  LYS A O   1 
ATOM   432  C CB  . LYS A 1 61  ? -16.151 32.870  3.298  1.00 21.13 ? 78  LYS A CB  1 
ATOM   433  C CG  . LYS A 1 61  ? -17.658 32.706  3.455  1.00 28.76 ? 78  LYS A CG  1 
ATOM   434  C CD  . LYS A 1 61  ? -18.380 34.025  3.298  1.00 34.46 ? 78  LYS A CD  1 
ATOM   435  C CE  . LYS A 1 61  ? -19.849 33.900  3.664  1.00 37.82 ? 78  LYS A CE  1 
ATOM   436  N NZ  . LYS A 1 61  ? -20.701 34.517  2.614  1.00 41.05 ? 78  LYS A NZ  1 
ATOM   437  N N   . GLY A 1 62  ? -16.609 29.560  2.863  1.00 16.43 ? 79  GLY A N   1 
ATOM   438  C CA  . GLY A 1 62  ? -17.186 28.562  1.990  1.00 16.88 ? 79  GLY A CA  1 
ATOM   439  C C   . GLY A 1 62  ? -16.273 27.411  1.648  1.00 19.69 ? 79  GLY A C   1 
ATOM   440  O O   . GLY A 1 62  ? -16.726 26.447  1.017  1.00 21.04 ? 79  GLY A O   1 
ATOM   441  N N   . LYS A 1 63  ? -15.029 27.470  2.031  1.00 17.53 ? 80  LYS A N   1 
ATOM   442  C CA  . LYS A 1 63  ? -14.115 26.396  1.694  1.00 15.66 ? 80  LYS A CA  1 
ATOM   443  C C   . LYS A 1 63  ? -14.327 25.210  2.635  1.00 15.15 ? 80  LYS A C   1 
ATOM   444  O O   . LYS A 1 63  ? -14.682 25.388  3.804  1.00 16.49 ? 80  LYS A O   1 
ATOM   445  C CB  . LYS A 1 63  ? -12.680 26.893  1.777  1.00 16.59 ? 80  LYS A CB  1 
ATOM   446  C CG  . LYS A 1 63  ? -12.322 27.905  0.678  1.00 18.62 ? 80  LYS A CG  1 
ATOM   447  C CD  . LYS A 1 63  ? -10.869 28.344  0.781  1.00 21.29 ? 80  LYS A CD  1 
ATOM   448  C CE  . LYS A 1 63  ? -10.567 29.523  -0.121 1.00 23.91 ? 80  LYS A CE  1 
ATOM   449  N NZ  . LYS A 1 63  ? -9.213  30.115  0.167  1.00 27.13 ? 80  LYS A NZ  1 
ATOM   450  N N   . PRO A 1 64  ? -14.132 23.984  2.144  1.00 16.80 ? 81  PRO A N   1 
ATOM   451  C CA  . PRO A 1 64  ? -14.504 22.812  2.958  1.00 15.30 ? 81  PRO A CA  1 
ATOM   452  C C   . PRO A 1 64  ? -13.720 22.670  4.245  1.00 16.64 ? 81  PRO A C   1 
ATOM   453  O O   . PRO A 1 64  ? -14.255 22.129  5.223  1.00 17.28 ? 81  PRO A O   1 
ATOM   454  C CB  . PRO A 1 64  ? -14.288 21.626  2.003  1.00 17.62 ? 81  PRO A CB  1 
ATOM   455  C CG  . PRO A 1 64  ? -13.372 22.147  0.933  1.00 16.09 ? 81  PRO A CG  1 
ATOM   456  C CD  . PRO A 1 64  ? -13.648 23.605  0.801  1.00 17.96 ? 81  PRO A CD  1 
ATOM   457  N N   . PHE A 1 65  ? -12.469 23.138  4.277  1.00 14.97 ? 82  PHE A N   1 
ATOM   458  C CA  . PHE A 1 65  ? -11.632 23.002  5.461  1.00 15.61 ? 82  PHE A CA  1 
ATOM   459  C C   . PHE A 1 65  ? -11.937 24.038  6.533  1.00 15.87 ? 82  PHE A C   1 
ATOM   460  O O   . PHE A 1 65  ? -11.431 23.903  7.651  1.00 15.70 ? 82  PHE A O   1 
ATOM   461  C CB  . PHE A 1 65  ? -10.152 23.078  5.080  1.00 18.48 ? 82  PHE A CB  1 
ATOM   462  C CG  . PHE A 1 65  ? -9.748  24.373  4.433  1.00 19.40 ? 82  PHE A CG  1 
ATOM   463  C CD1 . PHE A 1 65  ? -9.475  25.497  5.202  1.00 20.24 ? 82  PHE A CD1 1 
ATOM   464  C CD2 . PHE A 1 65  ? -9.613  24.464  3.060  1.00 21.11 ? 82  PHE A CD2 1 
ATOM   465  C CE1 . PHE A 1 65  ? -9.082  26.684  4.603  1.00 20.70 ? 82  PHE A CE1 1 
ATOM   466  C CE2 . PHE A 1 65  ? -9.226  25.651  2.464  1.00 19.82 ? 82  PHE A CE2 1 
ATOM   467  C CZ  . PHE A 1 65  ? -8.959  26.754  3.237  1.00 17.48 ? 82  PHE A CZ  1 
ATOM   468  N N   . LEU A 1 66  ? -12.736 25.062  6.238  1.00 15.37 ? 83  LEU A N   1 
ATOM   469  C CA  . LEU A 1 66  ? -12.900 26.146  7.207  1.00 13.79 ? 83  LEU A CA  1 
ATOM   470  C C   . LEU A 1 66  ? -13.508 25.706  8.535  1.00 14.32 ? 83  LEU A C   1 
ATOM   471  O O   . LEU A 1 66  ? -13.017 26.153  9.583  1.00 14.57 ? 83  LEU A O   1 
ATOM   472  C CB  . LEU A 1 66  ? -13.678 27.322  6.602  1.00 13.57 ? 83  LEU A CB  1 
ATOM   473  C CG  . LEU A 1 66  ? -13.819 28.544  7.514  1.00 13.31 ? 83  LEU A CG  1 
ATOM   474  C CD1 . LEU A 1 66  ? -12.459 29.062  7.907  1.00 14.48 ? 83  LEU A CD1 1 
ATOM   475  C CD2 . LEU A 1 66  ? -14.621 29.637  6.840  1.00 15.13 ? 83  LEU A CD2 1 
ATOM   476  N N   . PRO A 1 67  ? -14.578 24.901  8.583  1.00 14.41 ? 84  PRO A N   1 
ATOM   477  C CA  . PRO A 1 67  ? -15.132 24.545  9.903  1.00 15.84 ? 84  PRO A CA  1 
ATOM   478  C C   . PRO A 1 67  ? -14.125 23.901  10.848 1.00 16.13 ? 84  PRO A C   1 
ATOM   479  O O   . PRO A 1 67  ? -14.094 24.234  12.038 1.00 15.31 ? 84  PRO A O   1 
ATOM   480  C CB  . PRO A 1 67  ? -16.296 23.605  9.544  1.00 17.76 ? 84  PRO A CB  1 
ATOM   481  C CG  . PRO A 1 67  ? -16.684 24.013  8.173  1.00 18.66 ? 84  PRO A CG  1 
ATOM   482  C CD  . PRO A 1 67  ? -15.414 24.395  7.479  1.00 17.88 ? 84  PRO A CD  1 
ATOM   483  N N   . GLY A 1 68  ? -13.286 22.992  10.351 1.00 17.31 ? 85  GLY A N   1 
ATOM   484  C CA  . GLY A 1 68  ? -12.278 22.384  11.208 1.00 17.62 ? 85  GLY A CA  1 
ATOM   485  C C   . GLY A 1 68  ? -11.209 23.373  11.627 1.00 15.42 ? 85  GLY A C   1 
ATOM   486  O O   . GLY A 1 68  ? -10.694 23.307  12.746 1.00 17.41 ? 85  GLY A O   1 
ATOM   487  N N   . LEU A 1 69  ? -10.840 24.279  10.722 1.00 14.45 ? 86  LEU A N   1 
ATOM   488  C CA  . LEU A 1 69  ? -9.869  25.320  11.037 1.00 15.30 ? 86  LEU A CA  1 
ATOM   489  C C   . LEU A 1 69  ? -10.371 26.204  12.171 1.00 14.39 ? 86  LEU A C   1 
ATOM   490  O O   . LEU A 1 69  ? -9.625  26.516  13.110 1.00 14.07 ? 86  LEU A O   1 
ATOM   491  C CB  . LEU A 1 69  ? -9.646  26.144  9.770  1.00 16.13 ? 86  LEU A CB  1 
ATOM   492  C CG  . LEU A 1 69  ? -8.469  27.108  9.684  1.00 18.20 ? 86  LEU A CG  1 
ATOM   493  C CD1 . LEU A 1 69  ? -8.259  27.546  8.253  1.00 20.51 ? 86  LEU A CD1 1 
ATOM   494  C CD2 . LEU A 1 69  ? -8.711  28.300  10.537 1.00 22.60 ? 86  LEU A CD2 1 
ATOM   495  N N   . ILE A 1 70  ? -11.643 26.600  12.107 1.00 12.98 ? 87  ILE A N   1 
ATOM   496  C CA  A ILE A 1 70  ? -12.213 27.424  13.166 0.67 13.77 ? 87  ILE A CA  1 
ATOM   497  C CA  B ILE A 1 70  ? -12.231 27.418  13.163 0.33 13.43 ? 87  ILE A CA  1 
ATOM   498  C C   . ILE A 1 70  ? -12.250 26.657  14.482 1.00 12.56 ? 87  ILE A C   1 
ATOM   499  O O   . ILE A 1 70  ? -11.930 27.210  15.539 1.00 14.29 ? 87  ILE A O   1 
ATOM   500  C CB  A ILE A 1 70  ? -13.591 27.958  12.736 0.67 15.59 ? 87  ILE A CB  1 
ATOM   501  C CB  B ILE A 1 70  ? -13.639 27.883  12.746 0.33 13.97 ? 87  ILE A CB  1 
ATOM   502  C CG1 A ILE A 1 70  ? -13.393 29.027  11.655 0.67 18.73 ? 87  ILE A CG1 1 
ATOM   503  C CG1 B ILE A 1 70  ? -13.562 28.793  11.516 0.33 15.29 ? 87  ILE A CG1 1 
ATOM   504  C CG2 A ILE A 1 70  ? -14.370 28.504  13.936 0.67 14.43 ? 87  ILE A CG2 1 
ATOM   505  C CG2 B ILE A 1 70  ? -14.345 28.576  13.908 0.33 13.35 ? 87  ILE A CG2 1 
ATOM   506  C CD1 A ILE A 1 70  ? -14.673 29.570  11.075 0.67 21.19 ? 87  ILE A CD1 1 
ATOM   507  C CD1 B ILE A 1 70  ? -12.607 29.937  11.662 0.33 16.80 ? 87  ILE A CD1 1 
ATOM   508  N N   . GLU A 1 71  ? -12.623 25.373  14.446 1.00 14.54 ? 88  GLU A N   1 
ATOM   509  C CA  . GLU A 1 71  ? -12.668 24.610  15.692 1.00 15.41 ? 88  GLU A CA  1 
ATOM   510  C C   . GLU A 1 71  ? -11.293 24.563  16.359 1.00 14.09 ? 88  GLU A C   1 
ATOM   511  O O   . GLU A 1 71  ? -11.176 24.776  17.572 1.00 14.42 ? 88  GLU A O   1 
ATOM   512  C CB  . GLU A 1 71  ? -13.223 23.202  15.452 1.00 19.10 ? 88  GLU A CB  1 
ATOM   513  C CG  . GLU A 1 71  ? -14.747 23.157  15.297 1.00 29.01 ? 88  GLU A CG  1 
ATOM   514  C CD  . GLU A 1 71  ? -15.262 21.867  14.657 1.00 38.76 ? 88  GLU A CD  1 
ATOM   515  O OE1 . GLU A 1 71  ? -14.444 20.957  14.371 1.00 40.61 ? 88  GLU A OE1 1 
ATOM   516  O OE2 . GLU A 1 71  ? -16.495 21.771  14.429 1.00 39.75 ? 88  GLU A OE2 1 
ATOM   517  N N   . LYS A 1 72  ? -10.238 24.310  15.583 1.00 13.36 ? 89  LYS A N   1 
ATOM   518  C CA  . LYS A 1 72  ? -8.907  24.219  16.177 1.00 15.95 ? 89  LYS A CA  1 
ATOM   519  C C   . LYS A 1 72  ? -8.455  25.555  16.753 1.00 11.09 ? 89  LYS A C   1 
ATOM   520  O O   . LYS A 1 72  ? -7.661  25.584  17.701 1.00 12.32 ? 89  LYS A O   1 
ATOM   521  C CB  . LYS A 1 72  ? -7.884  23.738  15.141 1.00 19.06 ? 89  LYS A CB  1 
ATOM   522  C CG  . LYS A 1 72  ? -8.040  22.282  14.676 1.00 22.33 ? 89  LYS A CG  1 
ATOM   523  C CD  . LYS A 1 72  ? -7.977  21.293  15.822 1.00 26.06 ? 89  LYS A CD  1 
ATOM   524  C CE  . LYS A 1 72  ? -8.260  19.868  15.342 1.00 28.33 ? 89  LYS A CE  1 
ATOM   525  N NZ  . LYS A 1 72  ? -8.030  18.851  16.404 1.00 27.08 ? 89  LYS A NZ  1 
ATOM   526  N N   . MET A 1 73  ? -8.926  26.661  16.193 1.00 10.65 ? 90  MET A N   1 
ATOM   527  C CA  . MET A 1 73  ? -8.524  27.979  16.638 1.00 11.08 ? 90  MET A CA  1 
ATOM   528  C C   . MET A 1 73  ? -9.405  28.496  17.763 1.00 9.72  ? 90  MET A C   1 
ATOM   529  O O   . MET A 1 73  ? -9.150  29.584  18.282 1.00 9.68  ? 90  MET A O   1 
ATOM   530  C CB  . MET A 1 73  ? -8.571  28.951  15.453 1.00 10.24 ? 90  MET A CB  1 
ATOM   531  C CG  . MET A 1 73  ? -7.362  28.860  14.529 1.00 11.24 ? 90  MET A CG  1 
ATOM   532  S SD  . MET A 1 73  ? -5.790  29.359  15.312 1.00 11.51 ? 90  MET A SD  1 
ATOM   533  C CE  . MET A 1 73  ? -6.171  31.054  15.750 1.00 12.33 ? 90  MET A CE  1 
ATOM   534  N N   . THR A 1 74  ? -10.449 27.758  18.132 1.00 8.96  ? 91  THR A N   1 
ATOM   535  C CA  . THR A 1 74  ? -11.332 28.175  19.220 1.00 9.90  ? 91  THR A CA  1 
ATOM   536  C C   . THR A 1 74  ? -10.655 27.798  20.531 1.00 9.79  ? 91  THR A C   1 
ATOM   537  O O   . THR A 1 74  ? -10.639 26.634  20.934 1.00 12.94 ? 91  THR A O   1 
ATOM   538  C CB  . THR A 1 74  ? -12.703 27.530  19.069 1.00 12.20 ? 91  THR A CB  1 
ATOM   539  O OG1 . THR A 1 74  ? -13.286 27.953  17.836 1.00 12.23 ? 91  THR A OG1 1 
ATOM   540  C CG2 . THR A 1 74  ? -13.594 27.954  20.191 1.00 11.66 ? 91  THR A CG2 1 
ATOM   541  N N   . GLY A 1 75  ? -10.075 28.784  21.190 1.00 8.77  ? 92  GLY A N   1 
ATOM   542  C CA  . GLY A 1 75  ? -9.276  28.563  22.365 1.00 8.66  ? 92  GLY A CA  1 
ATOM   543  C C   . GLY A 1 75  ? -8.482  29.815  22.659 1.00 8.25  ? 92  GLY A C   1 
ATOM   544  O O   . GLY A 1 75  ? -8.639  30.847  21.992 1.00 7.42  ? 92  GLY A O   1 
ATOM   545  N N   . PRO A 1 76  ? -7.651  29.766  23.694 1.00 8.53  ? 93  PRO A N   1 
ATOM   546  C CA  . PRO A 1 76  ? -6.862  30.943  24.050 1.00 8.22  ? 93  PRO A CA  1 
ATOM   547  C C   . PRO A 1 76  ? -5.881  31.279  22.940 1.00 8.01  ? 93  PRO A C   1 
ATOM   548  O O   . PRO A 1 76  ? -5.271  30.395  22.339 1.00 7.75  ? 93  PRO A O   1 
ATOM   549  C CB  . PRO A 1 76  ? -6.150  30.506  25.334 1.00 7.17  ? 93  PRO A CB  1 
ATOM   550  C CG  . PRO A 1 76  ? -6.046  29.008  25.196 1.00 7.77  ? 93  PRO A CG  1 
ATOM   551  C CD  . PRO A 1 76  ? -7.339  28.611  24.550 1.00 8.61  ? 93  PRO A CD  1 
ATOM   552  N N   . VAL A 1 77  ? -5.725  32.571  22.687 1.00 6.94  ? 94  VAL A N   1 
ATOM   553  C CA  . VAL A 1 77  ? -4.757  33.081  21.728 1.00 7.14  ? 94  VAL A CA  1 
ATOM   554  C C   . VAL A 1 77  ? -4.120  34.330  22.316 1.00 6.43  ? 94  VAL A C   1 
ATOM   555  O O   . VAL A 1 77  ? -4.729  35.042  23.117 1.00 8.04  ? 94  VAL A O   1 
ATOM   556  C CB  . VAL A 1 77  ? -5.406  33.416  20.356 1.00 8.77  ? 94  VAL A CB  1 
ATOM   557  C CG1 . VAL A 1 77  ? -5.936  32.146  19.687 1.00 8.95  ? 94  VAL A CG1 1 
ATOM   558  C CG2 . VAL A 1 77  ? -6.490  34.466  20.512 1.00 8.69  ? 94  VAL A CG2 1 
ATOM   559  N N   . LEU A 1 78  ? -2.889  34.612  21.893 1.00 6.70  ? 95  LEU A N   1 
ATOM   560  C CA  . LEU A 1 78  ? -2.241  35.873  22.230 1.00 5.75  ? 95  LEU A CA  1 
ATOM   561  C C   . LEU A 1 78  ? -2.187  36.741  20.977 1.00 6.57  ? 95  LEU A C   1 
ATOM   562  O O   . LEU A 1 78  ? -1.470  36.427  20.026 1.00 7.67  ? 95  LEU A O   1 
ATOM   563  C CB  . LEU A 1 78  ? -0.858  35.680  22.851 1.00 7.27  ? 95  LEU A CB  1 
ATOM   564  C CG  . LEU A 1 78  ? -0.323  36.981  23.453 1.00 7.84  ? 95  LEU A CG  1 
ATOM   565  C CD1 . LEU A 1 78  ? -1.076  37.414  24.725 1.00 8.96  ? 95  LEU A CD1 1 
ATOM   566  C CD2 . LEU A 1 78  ? 1.156   36.879  23.753 1.00 8.88  ? 95  LEU A CD2 1 
ATOM   567  N N   . CYS A 1 79  ? -2.929  37.839  21.003 1.00 7.09  ? 96  CYS A N   1 
ATOM   568  C CA  . CYS A 1 79  ? -2.956  38.820  19.930 1.00 6.63  ? 96  CYS A CA  1 
ATOM   569  C C   . CYS A 1 79  ? -1.792  39.768  20.140 1.00 6.22  ? 96  CYS A C   1 
ATOM   570  O O   . CYS A 1 79  ? -1.569  40.229  21.257 1.00 8.01  ? 96  CYS A O   1 
ATOM   571  C CB  . CYS A 1 79  ? -4.257  39.618  20.026 1.00 7.17  ? 96  CYS A CB  1 
ATOM   572  S SG  . CYS A 1 79  ? -5.779  38.637  20.073 1.00 9.52  ? 96  CYS A SG  1 
ATOM   573  N N   . MET A 1 80  ? -1.049  40.058  19.076 1.00 6.81  ? 97  MET A N   1 
ATOM   574  C CA  . MET A 1 80  ? 0.136   40.885  19.199 1.00 5.99  ? 97  MET A CA  1 
ATOM   575  C C   . MET A 1 80  ? 0.280   41.765  17.970 1.00 6.28  ? 97  MET A C   1 
ATOM   576  O O   . MET A 1 80  ? -0.082  41.376  16.857 1.00 8.68  ? 97  MET A O   1 
ATOM   577  C CB  . MET A 1 80  ? 1.406   40.018  19.290 1.00 7.33  ? 97  MET A CB  1 
ATOM   578  C CG  . MET A 1 80  ? 1.275   38.811  20.234 1.00 8.33  ? 97  MET A CG  1 
ATOM   579  S SD  . MET A 1 80  ? 2.839   37.884  20.467 1.00 8.56  ? 97  MET A SD  1 
ATOM   580  C CE  . MET A 1 80  ? 3.039   37.161  18.835 1.00 9.48  ? 97  MET A CE  1 
ATOM   581  N N   . VAL A 1 81  ? 0.834   42.952  18.174 1.00 6.49  ? 98  VAL A N   1 
ATOM   582  C CA  . VAL A 1 81  ? 1.283   43.811  17.085 1.00 7.78  ? 98  VAL A CA  1 
ATOM   583  C C   . VAL A 1 81  ? 2.748   44.126  17.326 1.00 7.25  ? 98  VAL A C   1 
ATOM   584  O O   . VAL A 1 81  ? 3.104   44.631  18.391 1.00 7.84  ? 98  VAL A O   1 
ATOM   585  C CB  . VAL A 1 81  ? 0.465   45.102  16.967 1.00 7.25  ? 98  VAL A CB  1 
ATOM   586  C CG1 . VAL A 1 81  ? 1.007   45.952  15.825 1.00 8.15  ? 98  VAL A CG1 1 
ATOM   587  C CG2 . VAL A 1 81  ? -0.983  44.760  16.743 1.00 8.73  ? 98  VAL A CG2 1 
ATOM   588  N N   . PHE A 1 82  ? 3.588   43.834  16.336 1.00 7.51  ? 99  PHE A N   1 
ATOM   589  C CA  . PHE A 1 82  ? 5.005   44.171  16.366 1.00 7.18  ? 99  PHE A CA  1 
ATOM   590  C C   . PHE A 1 82  ? 5.309   45.173  15.269 1.00 7.54  ? 99  PHE A C   1 
ATOM   591  O O   . PHE A 1 82  ? 4.729   45.109  14.185 1.00 8.08  ? 99  PHE A O   1 
ATOM   592  C CB  . PHE A 1 82  ? 5.881   42.922  16.182 1.00 6.96  ? 99  PHE A CB  1 
ATOM   593  C CG  . PHE A 1 82  ? 6.109   42.160  17.455 1.00 8.09  ? 99  PHE A CG  1 
ATOM   594  C CD1 . PHE A 1 82  ? 7.150   42.500  18.298 1.00 8.40  ? 99  PHE A CD1 1 
ATOM   595  C CD2 . PHE A 1 82  ? 5.280   41.118  17.811 1.00 8.48  ? 99  PHE A CD2 1 
ATOM   596  C CE1 . PHE A 1 82  ? 7.366   41.792  19.472 1.00 9.52  ? 99  PHE A CE1 1 
ATOM   597  C CE2 . PHE A 1 82  ? 5.486   40.405  18.981 1.00 9.46  ? 99  PHE A CE2 1 
ATOM   598  C CZ  . PHE A 1 82  ? 6.521   40.750  19.821 1.00 8.56  ? 99  PHE A CZ  1 
ATOM   599  N N   . GLU A 1 83  ? 6.217   46.092  15.572 1.00 6.76  ? 100 GLU A N   1 
ATOM   600  C CA  . GLU A 1 83  ? 6.631   47.147  14.663 1.00 7.07  ? 100 GLU A CA  1 
ATOM   601  C C   . GLU A 1 83  ? 8.108   47.013  14.320 1.00 6.77  ? 100 GLU A C   1 
ATOM   602  O O   . GLU A 1 83  ? 8.947   46.792  15.195 1.00 7.40  ? 100 GLU A O   1 
ATOM   603  C CB  . GLU A 1 83  ? 6.398   48.496  15.328 1.00 9.20  ? 100 GLU A CB  1 
ATOM   604  C CG  . GLU A 1 83  ? 6.856   49.670  14.511 1.00 8.84  ? 100 GLU A CG  1 
ATOM   605  C CD  . GLU A 1 83  ? 6.650   50.958  15.248 1.00 13.89 ? 100 GLU A CD  1 
ATOM   606  O OE1 . GLU A 1 83  ? 5.553   51.530  15.110 1.00 16.27 ? 100 GLU A OE1 1 
ATOM   607  O OE2 . GLU A 1 83  ? 7.578   51.382  15.981 1.00 13.82 ? 100 GLU A OE2 1 
ATOM   608  N N   . GLY A 1 84  ? 8.432   47.173  13.046 1.00 7.38  ? 101 GLY A N   1 
ATOM   609  C CA  . GLY A 1 84  ? 9.823   47.206  12.631 1.00 7.24  ? 101 GLY A CA  1 
ATOM   610  C C   . GLY A 1 84  ? 9.930   47.400  11.134 1.00 8.33  ? 101 GLY A C   1 
ATOM   611  O O   . GLY A 1 84  ? 8.927   47.491  10.417 1.00 8.56  ? 101 GLY A O   1 
ATOM   612  N N   . VAL A 1 85  ? 11.170  47.494  10.664 1.00 8.09  ? 102 VAL A N   1 
ATOM   613  C CA  . VAL A 1 85  ? 11.410  47.623  9.231  1.00 9.08  ? 102 VAL A CA  1 
ATOM   614  C C   . VAL A 1 85  ? 10.964  46.351  8.531  1.00 9.87  ? 102 VAL A C   1 
ATOM   615  O O   . VAL A 1 85  ? 11.419  45.250  8.862  1.00 9.71  ? 102 VAL A O   1 
ATOM   616  C CB  . VAL A 1 85  ? 12.892  47.900  8.961  1.00 9.80  ? 102 VAL A CB  1 
ATOM   617  C CG1 . VAL A 1 85  ? 13.167  47.965  7.452  1.00 12.91 ? 102 VAL A CG1 1 
ATOM   618  C CG2 . VAL A 1 85  ? 13.336  49.196  9.632  1.00 11.30 ? 102 VAL A CG2 1 
ATOM   619  N N   . ASP A 1 86  ? 10.074  46.492  7.544  1.00 9.63  ? 103 ASP A N   1 
ATOM   620  C CA  . ASP A 1 86  ? 9.701   45.346  6.703  1.00 8.53  ? 103 ASP A CA  1 
ATOM   621  C C   . ASP A 1 86  ? 9.151   44.203  7.554  1.00 9.49  ? 103 ASP A C   1 
ATOM   622  O O   . ASP A 1 86  ? 9.256   43.038  7.180  1.00 8.51  ? 103 ASP A O   1 
ATOM   623  C CB  . ASP A 1 86  ? 10.913  44.902  5.853  1.00 9.48  ? 103 ASP A CB  1 
ATOM   624  C CG  . ASP A 1 86  ? 10.565  43.899  4.756  1.00 10.56 ? 103 ASP A CG  1 
ATOM   625  O OD1 . ASP A 1 86  ? 9.509   44.033  4.092  1.00 11.27 ? 103 ASP A OD1 1 
ATOM   626  O OD2 . ASP A 1 86  ? 11.411  42.997  4.526  1.00 12.52 ? 103 ASP A OD2 1 
ATOM   627  N N   . VAL A 1 87  ? 8.524   44.525  8.691  1.00 7.22  ? 104 VAL A N   1 
ATOM   628  C CA  . VAL A 1 87  ? 8.212   43.489  9.681  1.00 6.85  ? 104 VAL A CA  1 
ATOM   629  C C   . VAL A 1 87  ? 7.134   42.522  9.193  1.00 7.57  ? 104 VAL A C   1 
ATOM   630  O O   . VAL A 1 87  ? 7.085   41.374  9.642  1.00 7.45  ? 104 VAL A O   1 
ATOM   631  C CB  . VAL A 1 87  ? 7.889   44.108  11.058 1.00 8.45  ? 104 VAL A CB  1 
ATOM   632  C CG1 . VAL A 1 87  ? 6.499   44.771  11.074 1.00 8.69  ? 104 VAL A CG1 1 
ATOM   633  C CG2 . VAL A 1 87  ? 7.993   43.063  12.160 1.00 8.74  ? 104 VAL A CG2 1 
ATOM   634  N N   . ILE A 1 88  ? 6.241   42.950  8.295  1.00 8.06  ? 105 ILE A N   1 
ATOM   635  C CA  . ILE A 1 88  ? 5.229   42.020  7.797  1.00 7.91  ? 105 ILE A CA  1 
ATOM   636  C C   . ILE A 1 88  ? 5.911   40.837  7.099  1.00 7.20  ? 105 ILE A C   1 
ATOM   637  O O   . ILE A 1 88  ? 5.759   39.678  7.497  1.00 8.89  ? 105 ILE A O   1 
ATOM   638  C CB  . ILE A 1 88  ? 4.216   42.735  6.891  1.00 7.57  ? 105 ILE A CB  1 
ATOM   639  C CG1 . ILE A 1 88  ? 3.433   43.808  7.672  1.00 8.18  ? 105 ILE A CG1 1 
ATOM   640  C CG2 . ILE A 1 88  ? 3.243   41.717  6.308  1.00 9.79  ? 105 ILE A CG2 1 
ATOM   641  C CD1 . ILE A 1 88  ? 2.695   44.775  6.775  1.00 9.00  ? 105 ILE A CD1 1 
ATOM   642  N N   . ALA A 1 89  ? 6.724   41.125  6.080  1.00 7.39  ? 106 ALA A N   1 
ATOM   643  C CA  . ALA A 1 89  ? 7.413   40.057  5.357  1.00 7.60  ? 106 ALA A CA  1 
ATOM   644  C C   . ALA A 1 89  ? 8.439   39.350  6.234  1.00 7.28  ? 106 ALA A C   1 
ATOM   645  O O   . ALA A 1 89  ? 8.630   38.129  6.136  1.00 7.61  ? 106 ALA A O   1 
ATOM   646  C CB  . ALA A 1 89  ? 8.091   40.630  4.109  1.00 9.30  ? 106 ALA A CB  1 
ATOM   647  N N   . GLN A 1 90  ? 9.154   40.101  7.068  1.00 7.04  ? 107 GLN A N   1 
ATOM   648  C CA  . GLN A 1 90  ? 10.174  39.477  7.906  1.00 7.81  ? 107 GLN A CA  1 
ATOM   649  C C   . GLN A 1 90  ? 9.568   38.504  8.910  1.00 8.03  ? 107 GLN A C   1 
ATOM   650  O O   . GLN A 1 90  ? 10.123  37.425  9.142  1.00 6.70  ? 107 GLN A O   1 
ATOM   651  C CB  . GLN A 1 90  ? 11.009  40.554  8.598  1.00 8.70  ? 107 GLN A CB  1 
ATOM   652  C CG  . GLN A 1 90  ? 11.941  41.282  7.654  1.00 7.35  ? 107 GLN A CG  1 
ATOM   653  C CD  . GLN A 1 90  ? 12.968  40.374  7.013  1.00 8.17  ? 107 GLN A CD  1 
ATOM   654  O OE1 . GLN A 1 90  ? 13.710  39.690  7.700  1.00 8.51  ? 107 GLN A OE1 1 
ATOM   655  N NE2 . GLN A 1 90  ? 13.010  40.363  5.679  1.00 9.55  ? 107 GLN A NE2 1 
ATOM   656  N N   . ALA A 1 91  ? 8.453   38.873  9.539  1.00 7.43  ? 108 ALA A N   1 
ATOM   657  C CA  . ALA A 1 91  ? 7.796   37.947  10.464 1.00 5.63  ? 108 ALA A CA  1 
ATOM   658  C C   . ALA A 1 91  ? 7.335   36.671  9.755  1.00 7.21  ? 108 ALA A C   1 
ATOM   659  O O   . ALA A 1 91  ? 7.435   35.573  10.312 1.00 8.17  ? 108 ALA A O   1 
ATOM   660  C CB  . ALA A 1 91  ? 6.623   38.633  11.172 1.00 7.45  ? 108 ALA A CB  1 
ATOM   661  N N   . ARG A 1 92  ? 6.825   36.796  8.526  1.00 7.18  ? 109 ARG A N   1 
ATOM   662  C CA  . ARG A 1 92  ? 6.454   35.600  7.764  1.00 7.99  ? 109 ARG A CA  1 
ATOM   663  C C   . ARG A 1 92  ? 7.672   34.725  7.501  1.00 7.73  ? 109 ARG A C   1 
ATOM   664  O O   . ARG A 1 92  ? 7.593   33.491  7.567  1.00 8.52  ? 109 ARG A O   1 
ATOM   665  C CB  . ARG A 1 92  ? 5.789   35.998  6.446  1.00 8.25  ? 109 ARG A CB  1 
ATOM   666  C CG  . ARG A 1 92  ? 4.459   36.705  6.616  1.00 10.78 ? 109 ARG A CG  1 
ATOM   667  C CD  . ARG A 1 92  ? 3.318   35.751  6.930  1.00 10.02 ? 109 ARG A CD  1 
ATOM   668  N NE  . ARG A 1 92  ? 2.955   34.923  5.790  1.00 10.38 ? 109 ARG A NE  1 
ATOM   669  C CZ  . ARG A 1 92  ? 1.971   34.036  5.805  1.00 11.79 ? 109 ARG A CZ  1 
ATOM   670  N NH1 . ARG A 1 92  ? 1.230   33.839  6.886  1.00 13.88 ? 109 ARG A NH1 1 
ATOM   671  N NH2 . ARG A 1 92  ? 1.724   33.330  4.713  1.00 13.58 ? 109 ARG A NH2 1 
ATOM   672  N N   . LYS A 1 93  ? 8.811   35.350  7.212  1.00 9.02  ? 110 LYS A N   1 
ATOM   673  C CA  . LYS A 1 93  ? 10.045  34.602  6.998  1.00 8.16  ? 110 LYS A CA  1 
ATOM   674  C C   . LYS A 1 93  ? 10.491  33.897  8.272  1.00 8.29  ? 110 LYS A C   1 
ATOM   675  O O   . LYS A 1 93  ? 10.970  32.760  8.221  1.00 7.75  ? 110 LYS A O   1 
ATOM   676  C CB  . LYS A 1 93  ? 11.121  35.559  6.495  1.00 9.58  ? 110 LYS A CB  1 
ATOM   677  C CG  . LYS A 1 93  ? 12.390  34.904  6.102  1.00 9.07  ? 110 LYS A CG  1 
ATOM   678  C CD  . LYS A 1 93  ? 13.369  35.946  5.566  1.00 11.58 ? 110 LYS A CD  1 
ATOM   679  C CE  . LYS A 1 93  ? 14.728  35.336  5.326  1.00 12.76 ? 110 LYS A CE  1 
ATOM   680  N NZ  . LYS A 1 93  ? 15.667  36.301  4.723  1.00 11.97 ? 110 LYS A NZ  1 
ATOM   681  N N   . MET A 1 94  ? 10.324  34.558  9.423  1.00 7.18  ? 111 MET A N   1 
ATOM   682  C CA  . MET A 1 94  ? 10.692  33.963  10.707 1.00 8.21  ? 111 MET A CA  1 
ATOM   683  C C   . MET A 1 94  ? 9.760   32.821  11.090 1.00 7.10  ? 111 MET A C   1 
ATOM   684  O O   . MET A 1 94  ? 10.196  31.855  11.734 1.00 8.13  ? 111 MET A O   1 
ATOM   685  C CB  . MET A 1 94  ? 10.680  35.030  11.795 1.00 7.57  ? 111 MET A CB  1 
ATOM   686  C CG  . MET A 1 94  ? 11.767  36.075  11.598 1.00 6.73  ? 111 MET A CG  1 
ATOM   687  S SD  . MET A 1 94  ? 11.519  37.570  12.589 1.00 8.66  ? 111 MET A SD  1 
ATOM   688  C CE  . MET A 1 94  ? 11.916  36.986  14.226 1.00 11.94 ? 111 MET A CE  1 
ATOM   689  N N   . MET A 1 95  ? 8.481   32.913  10.713 1.00 7.09  ? 112 MET A N   1 
ATOM   690  C CA  . MET A 1 95  ? 7.549   31.840  11.008 1.00 6.49  ? 112 MET A CA  1 
ATOM   691  C C   . MET A 1 95  ? 7.889   30.588  10.220 1.00 6.18  ? 112 MET A C   1 
ATOM   692  O O   . MET A 1 95  ? 7.791   29.465  10.733 1.00 8.04  ? 112 MET A O   1 
ATOM   693  C CB  . MET A 1 95  ? 6.137   32.284  10.649 1.00 8.05  ? 112 MET A CB  1 
ATOM   694  C CG  . MET A 1 95  ? 5.546   33.329  11.571 1.00 8.17  ? 112 MET A CG  1 
ATOM   695  S SD  . MET A 1 95  ? 4.079   34.146  10.850 1.00 10.83 ? 112 MET A SD  1 
ATOM   696  C CE  . MET A 1 95  ? 3.103   32.757  10.285 1.00 9.27  ? 112 MET A CE  1 
ATOM   697  N N   . GLY A 1 96  ? 8.260   30.763  8.961  1.00 8.02  ? 113 GLY A N   1 
ATOM   698  C CA  . GLY A 1 96  ? 8.480   29.650  8.071  1.00 6.92  ? 113 GLY A CA  1 
ATOM   699  C C   . GLY A 1 96  ? 7.211   29.199  7.386  1.00 6.52  ? 113 GLY A C   1 
ATOM   700  O O   . GLY A 1 96  ? 6.100   29.638  7.694  1.00 8.05  ? 113 GLY A O   1 
ATOM   701  N N   . SER A 1 97  ? 7.393   28.224  6.490  1.00 7.59  ? 114 SER A N   1 
ATOM   702  C CA  . SER A 1 97  ? 6.310   27.701  5.675  1.00 8.92  ? 114 SER A CA  1 
ATOM   703  C C   . SER A 1 97  ? 5.166   27.190  6.538  1.00 8.75  ? 114 SER A C   1 
ATOM   704  O O   . SER A 1 97  ? 5.371   26.700  7.656  1.00 8.76  ? 114 SER A O   1 
ATOM   705  C CB  . SER A 1 97  ? 6.832   26.534  4.833  1.00 12.27 ? 114 SER A CB  1 
ATOM   706  O OG  . SER A 1 97  ? 8.035   26.899  4.181  1.00 18.02 ? 114 SER A OG  1 
ATOM   707  N N   . THR A 1 98  ? 3.952   27.253  5.967  1.00 10.03 ? 115 THR A N   1 
ATOM   708  C CA  A THR A 1 98  ? 2.785   26.758  6.685  0.64 10.61 ? 115 THR A CA  1 
ATOM   709  C CA  B THR A 1 98  ? 2.754   26.737  6.630  0.36 9.46  ? 115 THR A CA  1 
ATOM   710  C C   . THR A 1 98  ? 2.953   25.299  7.101  1.00 8.15  ? 115 THR A C   1 
ATOM   711  O O   . THR A 1 98  ? 2.516   24.920  8.190  1.00 8.16  ? 115 THR A O   1 
ATOM   712  C CB  A THR A 1 98  ? 1.505   26.981  5.873  0.64 12.48 ? 115 THR A CB  1 
ATOM   713  C CB  B THR A 1 98  ? 1.563   26.792  5.658  0.36 10.48 ? 115 THR A CB  1 
ATOM   714  O OG1 A THR A 1 98  ? 0.365   26.589  6.654  0.64 16.89 ? 115 THR A OG1 1 
ATOM   715  O OG1 B THR A 1 98  ? 1.364   28.128  5.174  0.36 10.37 ? 115 THR A OG1 1 
ATOM   716  C CG2 A THR A 1 98  ? 1.533   26.194  4.580  0.64 13.79 ? 115 THR A CG2 1 
ATOM   717  C CG2 B THR A 1 98  ? 0.284   26.303  6.334  0.36 11.64 ? 115 THR A CG2 1 
ATOM   718  N N   . ARG A 1 99  ? 3.599   24.475  6.268  1.00 8.65  ? 116 ARG A N   1 
ATOM   719  C CA  . ARG A 1 99  ? 3.899   23.099  6.639  1.00 10.64 ? 116 ARG A CA  1 
ATOM   720  C C   . ARG A 1 99  ? 5.224   23.071  7.384  1.00 8.10  ? 116 ARG A C   1 
ATOM   721  O O   . ARG A 1 99  ? 6.271   23.376  6.778  1.00 8.31  ? 116 ARG A O   1 
ATOM   722  C CB  . ARG A 1 99  ? 3.996   22.233  5.395  1.00 10.28 ? 116 ARG A CB  1 
ATOM   723  C CG  . ARG A 1 99  ? 2.670   22.041  4.704  1.00 10.95 ? 116 ARG A CG  1 
ATOM   724  C CD  . ARG A 1 99  ? 2.888   21.373  3.408  1.00 15.31 ? 116 ARG A CD  1 
ATOM   725  N NE  . ARG A 1 99  ? 1.669   20.804  2.864  1.00 21.44 ? 116 ARG A NE  1 
ATOM   726  C CZ  . ARG A 1 99  ? 1.608   20.244  1.669  1.00 26.57 ? 116 ARG A CZ  1 
ATOM   727  N NH1 . ARG A 1 99  ? 2.648   20.280  0.841  1.00 28.01 ? 116 ARG A NH1 1 
ATOM   728  N NH2 . ARG A 1 99  ? 0.489   19.627  1.301  1.00 27.33 ? 116 ARG A NH2 1 
ATOM   729  N N   . PRO A 1 100 ? 5.246   22.728  8.678  1.00 7.58  ? 117 PRO A N   1 
ATOM   730  C CA  . PRO A 1 100 ? 6.528   22.717  9.409  1.00 7.46  ? 117 PRO A CA  1 
ATOM   731  C C   . PRO A 1 100 ? 7.578   21.821  8.780  1.00 6.85  ? 117 PRO A C   1 
ATOM   732  O O   . PRO A 1 100 ? 8.776   22.134  8.863  1.00 7.61  ? 117 PRO A O   1 
ATOM   733  C CB  . PRO A 1 100 ? 6.124   22.242  10.817 1.00 7.23  ? 117 PRO A CB  1 
ATOM   734  C CG  . PRO A 1 100 ? 4.712   22.747  10.971 1.00 7.20  ? 117 PRO A CG  1 
ATOM   735  C CD  . PRO A 1 100 ? 4.104   22.507  9.589  1.00 8.38  ? 117 PRO A CD  1 
ATOM   736  N N   . GLY A 1 101 ? 7.167   20.738  8.122  1.00 7.79  ? 118 GLY A N   1 
ATOM   737  C CA  . GLY A 1 101 ? 8.124   19.843  7.482  1.00 7.77  ? 118 GLY A CA  1 
ATOM   738  C C   . GLY A 1 101 ? 8.820   20.448  6.282  1.00 7.89  ? 118 GLY A C   1 
ATOM   739  O O   . GLY A 1 101 ? 9.877   19.955  5.875  1.00 9.11  ? 118 GLY A O   1 
ATOM   740  N N   . GLU A 1 102 ? 8.255   21.514  5.710  1.00 6.91  ? 119 GLU A N   1 
ATOM   741  C CA  . GLU A 1 102 ? 8.861   22.246  4.609  1.00 7.31  ? 119 GLU A CA  1 
ATOM   742  C C   . GLU A 1 102 ? 9.562   23.516  5.061  1.00 8.17  ? 119 GLU A C   1 
ATOM   743  O O   . GLU A 1 102 ? 10.298  24.110  4.273  1.00 9.59  ? 119 GLU A O   1 
ATOM   744  C CB  . GLU A 1 102 ? 7.794   22.625  3.577  1.00 9.09  ? 119 GLU A CB  1 
ATOM   745  C CG  . GLU A 1 102 ? 7.037   21.402  3.035  1.00 10.38 ? 119 GLU A CG  1 
ATOM   746  C CD  . GLU A 1 102 ? 6.048   21.750  1.947  1.00 14.02 ? 119 GLU A CD  1 
ATOM   747  O OE1 . GLU A 1 102 ? 5.694   22.943  1.826  1.00 13.77 ? 119 GLU A OE1 1 
ATOM   748  O OE2 . GLU A 1 102 ? 5.603   20.826  1.233  1.00 16.69 ? 119 GLU A OE2 1 
ATOM   749  N N   . ALA A 1 103 ? 9.361   23.936  6.303  1.00 7.66  ? 120 ALA A N   1 
ATOM   750  C CA  . ALA A 1 103 ? 9.886   25.210  6.776  1.00 6.76  ? 120 ALA A CA  1 
ATOM   751  C C   . ALA A 1 103 ? 11.398  25.123  6.964  1.00 7.75  ? 120 ALA A C   1 
ATOM   752  O O   . ALA A 1 103 ? 11.949  24.071  7.291  1.00 9.22  ? 120 ALA A O   1 
ATOM   753  C CB  . ALA A 1 103 ? 9.215   25.594  8.094  1.00 9.02  ? 120 ALA A CB  1 
ATOM   754  N N   . ALA A 1 104 ? 12.068  26.259  6.747  1.00 8.76  ? 121 ALA A N   1 
ATOM   755  C CA  . ALA A 1 104 ? 13.518  26.311  6.828  1.00 10.22 ? 121 ALA A CA  1 
ATOM   756  C C   . ALA A 1 104 ? 13.979  26.089  8.264  1.00 10.02 ? 121 ALA A C   1 
ATOM   757  O O   . ALA A 1 104 ? 13.374  26.612  9.203  1.00 9.40  ? 121 ALA A O   1 
ATOM   758  C CB  . ALA A 1 104 ? 13.998  27.687  6.368  1.00 11.58 ? 121 ALA A CB  1 
ATOM   759  N N   . PRO A 1 105 ? 15.086  25.386  8.471  1.00 11.85 ? 122 PRO A N   1 
ATOM   760  C CA  . PRO A 1 105 ? 15.623  25.298  9.830  1.00 10.85 ? 122 PRO A CA  1 
ATOM   761  C C   . PRO A 1 105 ? 15.871  26.696  10.388 1.00 10.48 ? 122 PRO A C   1 
ATOM   762  O O   . PRO A 1 105 ? 16.270  27.607  9.670  1.00 12.74 ? 122 PRO A O   1 
ATOM   763  C CB  . PRO A 1 105 ? 16.932  24.512  9.655  1.00 16.46 ? 122 PRO A CB  1 
ATOM   764  C CG  . PRO A 1 105 ? 16.797  23.797  8.337  1.00 19.33 ? 122 PRO A CG  1 
ATOM   765  C CD  . PRO A 1 105 ? 15.886  24.639  7.484  1.00 18.79 ? 122 PRO A CD  1 
ATOM   766  N N   . GLY A 1 106 ? 15.609  26.863  11.681 1.00 10.35 ? 123 GLY A N   1 
ATOM   767  C CA  . GLY A 1 106 ? 15.727  28.152  12.318 1.00 10.49 ? 123 GLY A CA  1 
ATOM   768  C C   . GLY A 1 106 ? 14.458  28.974  12.329 1.00 8.90  ? 123 GLY A C   1 
ATOM   769  O O   . GLY A 1 106 ? 14.416  30.006  13.010 1.00 10.64 ? 123 GLY A O   1 
ATOM   770  N N   . THR A 1 107 ? 13.419  28.546  11.624 1.00 7.53  ? 124 THR A N   1 
ATOM   771  C CA  . THR A 1 107 ? 12.129  29.210  11.689 1.00 6.84  ? 124 THR A CA  1 
ATOM   772  C C   . THR A 1 107 ? 11.303  28.643  12.841 1.00 7.07  ? 124 THR A C   1 
ATOM   773  O O   . THR A 1 107 ? 11.569  27.566  13.359 1.00 7.89  ? 124 THR A O   1 
ATOM   774  C CB  . THR A 1 107 ? 11.360  29.064  10.368 1.00 7.46  ? 124 THR A CB  1 
ATOM   775  O OG1 . THR A 1 107 ? 11.088  27.682  10.111 1.00 8.19  ? 124 THR A OG1 1 
ATOM   776  C CG2 . THR A 1 107 ? 12.119  29.667  9.165  1.00 6.96  ? 124 THR A CG2 1 
ATOM   777  N N   . ILE A 1 108 ? 10.292  29.403  13.247 1.00 6.59  ? 125 ILE A N   1 
ATOM   778  C CA  . ILE A 1 108 ? 9.432   28.972  14.348 1.00 6.92  ? 125 ILE A CA  1 
ATOM   779  C C   . ILE A 1 108 ? 8.791   27.628  14.024 1.00 7.30  ? 125 ILE A C   1 
ATOM   780  O O   . ILE A 1 108 ? 8.818   26.691  14.831 1.00 8.11  ? 125 ILE A O   1 
ATOM   781  C CB  . ILE A 1 108 ? 8.382   30.057  14.658 1.00 8.45  ? 125 ILE A CB  1 
ATOM   782  C CG1 . ILE A 1 108 ? 9.073   31.319  15.182 1.00 9.64  ? 125 ILE A CG1 1 
ATOM   783  C CG2 . ILE A 1 108 ? 7.339   29.539  15.649 1.00 7.51  ? 125 ILE A CG2 1 
ATOM   784  C CD1 . ILE A 1 108 ? 8.174   32.541  15.267 1.00 10.86 ? 125 ILE A CD1 1 
ATOM   785  N N   . ARG A 1 109 ? 8.210   27.508  12.831 1.00 7.77  ? 126 ARG A N   1 
ATOM   786  C CA  . ARG A 1 109 ? 7.475   26.280  12.524 1.00 8.24  ? 126 ARG A CA  1 
ATOM   787  C C   . ARG A 1 109 ? 8.413   25.076  12.464 1.00 7.07  ? 126 ARG A C   1 
ATOM   788  O O   . ARG A 1 109 ? 8.069   23.996  12.947 1.00 6.74  ? 126 ARG A O   1 
ATOM   789  C CB  . ARG A 1 109 ? 6.687   26.407  11.215 1.00 7.95  ? 126 ARG A CB  1 
ATOM   790  C CG  . ARG A 1 109 ? 5.230   26.806  11.334 1.00 14.01 ? 126 ARG A CG  1 
ATOM   791  C CD  . ARG A 1 109 ? 5.026   28.267  11.132 1.00 15.58 ? 126 ARG A CD  1 
ATOM   792  N NE  . ARG A 1 109 ? 3.631   28.699  11.157 1.00 11.46 ? 126 ARG A NE  1 
ATOM   793  C CZ  . ARG A 1 109 ? 2.968   29.201  10.129 1.00 10.20 ? 126 ARG A CZ  1 
ATOM   794  N NH1 . ARG A 1 109 ? 3.490   29.242  8.915  1.00 10.96 ? 126 ARG A NH1 1 
ATOM   795  N NH2 . ARG A 1 109 ? 1.757   29.711  10.328 1.00 9.23  ? 126 ARG A NH2 1 
ATOM   796  N N   . ALA A 1 110 ? 9.598   25.235  11.857 1.00 6.88  ? 127 ALA A N   1 
ATOM   797  C CA  . ALA A 1 110 ? 10.550  24.130  11.783 1.00 8.01  ? 127 ALA A CA  1 
ATOM   798  C C   . ALA A 1 110 ? 11.090  23.752  13.155 1.00 6.57  ? 127 ALA A C   1 
ATOM   799  O O   . ALA A 1 110 ? 11.357  22.571  13.413 1.00 8.51  ? 127 ALA A O   1 
ATOM   800  C CB  . ALA A 1 110 ? 11.710  24.490  10.860 1.00 6.51  ? 127 ALA A CB  1 
ATOM   801  N N   . ASP A 1 111 ? 11.257  24.728  14.048 1.00 7.36  ? 128 ASP A N   1 
ATOM   802  C CA  . ASP A 1 111 ? 11.878  24.456  15.338 1.00 8.15  ? 128 ASP A CA  1 
ATOM   803  C C   . ASP A 1 111 ? 10.898  23.839  16.327 1.00 6.71  ? 128 ASP A C   1 
ATOM   804  O O   . ASP A 1 111 ? 11.320  23.100  17.225 1.00 7.80  ? 128 ASP A O   1 
ATOM   805  C CB  . ASP A 1 111 ? 12.466  25.741  15.928 1.00 9.70  ? 128 ASP A CB  1 
ATOM   806  C CG  . ASP A 1 111 ? 13.737  26.201  15.211 1.00 13.90 ? 128 ASP A CG  1 
ATOM   807  O OD1 . ASP A 1 111 ? 14.286  25.433  14.388 1.00 16.19 ? 128 ASP A OD1 1 
ATOM   808  O OD2 . ASP A 1 111 ? 14.188  27.342  15.460 1.00 13.71 ? 128 ASP A OD2 1 
ATOM   809  N N   . PHE A 1 112 ? 9.602   24.125  16.179 1.00 6.83  ? 129 PHE A N   1 
ATOM   810  C CA  . PHE A 1 112 ? 8.615   23.772  17.190 1.00 5.66  ? 129 PHE A CA  1 
ATOM   811  C C   . PHE A 1 112 ? 7.563   22.760  16.752 1.00 5.97  ? 129 PHE A C   1 
ATOM   812  O O   . PHE A 1 112 ? 6.923   22.172  17.628 1.00 7.75  ? 129 PHE A O   1 
ATOM   813  C CB  . PHE A 1 112 ? 7.821   25.010  17.648 1.00 6.86  ? 129 PHE A CB  1 
ATOM   814  C CG  . PHE A 1 112 ? 8.564   25.965  18.538 1.00 7.65  ? 129 PHE A CG  1 
ATOM   815  C CD1 . PHE A 1 112 ? 8.493   25.835  19.916 1.00 7.88  ? 129 PHE A CD1 1 
ATOM   816  C CD2 . PHE A 1 112 ? 9.275   27.041  18.008 1.00 8.04  ? 129 PHE A CD2 1 
ATOM   817  C CE1 . PHE A 1 112 ? 9.131   26.750  20.745 1.00 10.41 ? 129 PHE A CE1 1 
ATOM   818  C CE2 . PHE A 1 112 ? 9.910   27.957  18.833 1.00 9.16  ? 129 PHE A CE2 1 
ATOM   819  C CZ  . PHE A 1 112 ? 9.846   27.814  20.200 1.00 9.71  ? 129 PHE A CZ  1 
ATOM   820  N N   . CYS A 1 113 ? 7.324   22.561  15.452 1.00 6.04  ? 130 CYS A N   1 
ATOM   821  C CA  . CYS A 1 113 ? 6.078   21.932  15.014 1.00 5.93  ? 130 CYS A CA  1 
ATOM   822  C C   . CYS A 1 113 ? 6.299   20.790  14.029 1.00 6.41  ? 130 CYS A C   1 
ATOM   823  O O   . CYS A 1 113 ? 7.381   20.608  13.476 1.00 7.30  ? 130 CYS A O   1 
ATOM   824  C CB  . CYS A 1 113 ? 5.131   22.982  14.405 1.00 7.75  ? 130 CYS A CB  1 
ATOM   825  S SG  . CYS A 1 113 ? 4.700   24.315  15.565 1.00 8.41  ? 130 CYS A SG  1 
ATOM   826  N N   . GLN A 1 114 ? 5.205   20.054  13.774 1.00 6.37  ? 131 GLN A N   1 
ATOM   827  C CA  . GLN A 1 114 ? 5.190   18.904  12.878 1.00 7.81  ? 131 GLN A CA  1 
ATOM   828  C C   . GLN A 1 114 ? 4.233   19.033  11.709 1.00 7.38  ? 131 GLN A C   1 
ATOM   829  O O   . GLN A 1 114 ? 4.571   18.617  10.595 1.00 8.07  ? 131 GLN A O   1 
ATOM   830  C CB  . GLN A 1 114 ? 4.852   17.616  13.644 1.00 8.03  ? 131 GLN A CB  1 
ATOM   831  C CG  . GLN A 1 114 ? 5.929   17.231  14.642 1.00 8.88  ? 131 GLN A CG  1 
ATOM   832  C CD  . GLN A 1 114 ? 5.669   15.903  15.299 1.00 7.74  ? 131 GLN A CD  1 
ATOM   833  O OE1 . GLN A 1 114 ? 5.375   14.916  14.636 1.00 9.75  ? 131 GLN A OE1 1 
ATOM   834  N NE2 . GLN A 1 114 ? 5.780   15.871  16.618 1.00 7.73  ? 131 GLN A NE2 1 
ATOM   835  N N   . GLN A 1 115 ? 3.046   19.605  11.915 1.00 7.03  ? 132 GLN A N   1 
ATOM   836  C CA  . GLN A 1 115 ? 1.990   19.601  10.911 1.00 8.16  ? 132 GLN A CA  1 
ATOM   837  C C   . GLN A 1 115 ? 1.351   20.976  10.776 1.00 8.16  ? 132 GLN A C   1 
ATOM   838  O O   . GLN A 1 115 ? 1.294   21.756  11.726 1.00 9.74  ? 132 GLN A O   1 
ATOM   839  C CB  . GLN A 1 115 ? 0.905   18.583  11.276 1.00 10.20 ? 132 GLN A CB  1 
ATOM   840  C CG  . GLN A 1 115 ? 1.437   17.161  11.337 1.00 12.12 ? 132 GLN A CG  1 
ATOM   841  C CD  . GLN A 1 115 ? 0.333   16.139  11.443 1.00 11.74 ? 132 GLN A CD  1 
ATOM   842  O OE1 . GLN A 1 115 ? -0.251  15.956  12.500 1.00 13.68 ? 132 GLN A OE1 1 
ATOM   843  N NE2 . GLN A 1 115 ? 0.044   15.462  10.340 1.00 18.05 ? 132 GLN A NE2 1 
ATOM   844  N N   . ALA A 1 116 ? 0.818   21.242  9.581  1.00 8.68  ? 133 ALA A N   1 
ATOM   845  C CA  . ALA A 1 116 ? 0.226   22.547  9.304  1.00 9.23  ? 133 ALA A CA  1 
ATOM   846  C C   . ALA A 1 116 ? -0.964  22.842  10.203 1.00 7.78  ? 133 ALA A C   1 
ATOM   847  O O   . ALA A 1 116 ? -1.198  24.004  10.551 1.00 9.80  ? 133 ALA A O   1 
ATOM   848  C CB  . ALA A 1 116 ? -0.222  22.624  7.843  1.00 9.91  ? 133 ALA A CB  1 
ATOM   849  N N   . GLY A 1 117 ? -1.731  21.822  10.579 1.00 8.75  ? 134 GLY A N   1 
ATOM   850  C CA  . GLY A 1 117 ? -2.885  22.045  11.423 1.00 10.43 ? 134 GLY A CA  1 
ATOM   851  C C   . GLY A 1 117 ? -2.564  22.460  12.845 1.00 8.68  ? 134 GLY A C   1 
ATOM   852  O O   . GLY A 1 117 ? -3.491  22.838  13.572 1.00 10.58 ? 134 GLY A O   1 
ATOM   853  N N   . ARG A 1 118 ? -1.303  22.322  13.289 1.00 7.88  ? 135 ARG A N   1 
ATOM   854  C CA  . ARG A 1 118 ? -0.882  22.836  14.597 1.00 7.48  ? 135 ARG A CA  1 
ATOM   855  C C   . ARG A 1 118 ? 0.479   23.486  14.371 1.00 6.57  ? 135 ARG A C   1 
ATOM   856  O O   . ARG A 1 118 ? 1.515   22.899  14.687 1.00 9.10  ? 135 ARG A O   1 
ATOM   857  C CB  . ARG A 1 118 ? -0.796  21.707  15.626 1.00 7.96  ? 135 ARG A CB  1 
ATOM   858  C CG  . ARG A 1 118 ? -2.129  21.156  16.079 1.00 9.58  ? 135 ARG A CG  1 
ATOM   859  C CD  . ARG A 1 118 ? -2.949  22.187  16.812 1.00 11.72 ? 135 ARG A CD  1 
ATOM   860  N NE  . ARG A 1 118 ? -4.062  21.606  17.557 1.00 10.43 ? 135 ARG A NE  1 
ATOM   861  C CZ  . ARG A 1 118 ? -5.009  22.312  18.161 1.00 13.65 ? 135 ARG A CZ  1 
ATOM   862  N NH1 . ARG A 1 118 ? -5.047  23.630  18.080 1.00 13.99 ? 135 ARG A NH1 1 
ATOM   863  N NH2 . ARG A 1 118 ? -5.941  21.679  18.868 1.00 15.09 ? 135 ARG A NH2 1 
ATOM   864  N N   . ASN A 1 119 ? 0.472   24.716  13.858 1.00 7.24  ? 136 ASN A N   1 
ATOM   865  C CA  . ASN A 1 119 ? 1.707   25.395  13.467 1.00 7.38  ? 136 ASN A CA  1 
ATOM   866  C C   . ASN A 1 119 ? 1.932   26.700  14.221 1.00 5.92  ? 136 ASN A C   1 
ATOM   867  O O   . ASN A 1 119 ? 2.646   27.584  13.749 1.00 5.74  ? 136 ASN A O   1 
ATOM   868  C CB  . ASN A 1 119 ? 1.834   25.564  11.950 1.00 8.46  ? 136 ASN A CB  1 
ATOM   869  C CG  . ASN A 1 119 ? 0.835   26.524  11.370 1.00 7.95  ? 136 ASN A CG  1 
ATOM   870  O OD1 . ASN A 1 119 ? 0.087   27.177  12.094 1.00 10.17 ? 136 ASN A OD1 1 
ATOM   871  N ND2 . ASN A 1 119 ? 0.833   26.635  10.043 1.00 8.75  ? 136 ASN A ND2 1 
ATOM   872  N N   . LEU A 1 120 ? 1.353   26.787  15.415 1.00 7.74  ? 137 LEU A N   1 
ATOM   873  C CA  . LEU A 1 120 ? 1.740   27.634  16.530 1.00 7.51  ? 137 LEU A CA  1 
ATOM   874  C C   . LEU A 1 120 ? 1.454   29.121  16.420 1.00 6.89  ? 137 LEU A C   1 
ATOM   875  O O   . LEU A 1 120 ? 1.140   29.738  17.446 1.00 7.85  ? 137 LEU A O   1 
ATOM   876  C CB  . LEU A 1 120 ? 3.275   27.582  16.726 1.00 8.67  ? 137 LEU A CB  1 
ATOM   877  C CG  . LEU A 1 120 ? 3.809   27.542  18.160 1.00 8.17  ? 137 LEU A CG  1 
ATOM   878  C CD1 . LEU A 1 120 ? 3.499   26.171  18.780 1.00 8.65  ? 137 LEU A CD1 1 
ATOM   879  C CD2 . LEU A 1 120 ? 5.305   27.816  18.205 1.00 9.48  ? 137 LEU A CD2 1 
ATOM   880  N N   . ILE A 1 121 ? 1.395   29.685  15.216 1.00 6.34  ? 138 ILE A N   1 
ATOM   881  C CA  . ILE A 1 121 ? 1.424   31.145  15.100 1.00 6.80  ? 138 ILE A CA  1 
ATOM   882  C C   . ILE A 1 121 ? 0.835   31.552  13.760 1.00 7.11  ? 138 ILE A C   1 
ATOM   883  O O   . ILE A 1 121 ? 1.017   30.880  12.745 1.00 8.02  ? 138 ILE A O   1 
ATOM   884  C CB  . ILE A 1 121 ? 2.864   31.684  15.300 1.00 7.67  ? 138 ILE A CB  1 
ATOM   885  C CG1 . ILE A 1 121 ? 2.878   33.222  15.317 1.00 8.45  ? 138 ILE A CG1 1 
ATOM   886  C CG2 . ILE A 1 121 ? 3.804   31.126  14.239 1.00 7.95  ? 138 ILE A CG2 1 
ATOM   887  C CD1 . ILE A 1 121 ? 4.174   33.837  15.865 1.00 10.41 ? 138 ILE A CD1 1 
ATOM   888  N N   . HIS A 1 122 ? 0.089   32.648  13.790 1.00 7.32  ? 139 HIS A N   1 
ATOM   889  C CA  . HIS A 1 122 ? -0.402  33.323  12.610 1.00 7.71  ? 139 HIS A CA  1 
ATOM   890  C C   . HIS A 1 122 ? 0.339   34.643  12.442 1.00 6.56  ? 139 HIS A C   1 
ATOM   891  O O   . HIS A 1 122 ? 0.602   35.338  13.426 1.00 6.68  ? 139 HIS A O   1 
ATOM   892  C CB  . HIS A 1 122 ? -1.877  33.688  12.812 1.00 8.01  ? 139 HIS A CB  1 
ATOM   893  C CG  . HIS A 1 122 ? -2.362  34.714  11.846 1.00 7.78  ? 139 HIS A CG  1 
ATOM   894  N ND1 . HIS A 1 122 ? -2.881  34.390  10.614 1.00 10.64 ? 139 HIS A ND1 1 
ATOM   895  C CD2 . HIS A 1 122 ? -2.328  36.069  11.898 1.00 9.90  ? 139 HIS A CD2 1 
ATOM   896  C CE1 . HIS A 1 122 ? -3.179  35.501  9.965  1.00 9.65  ? 139 HIS A CE1 1 
ATOM   897  N NE2 . HIS A 1 122 ? -2.834  36.530  10.713 1.00 9.22  ? 139 HIS A NE2 1 
ATOM   898  N N   . GLY A 1 123 ? 0.613   35.028  11.201 1.00 7.10  ? 140 GLY A N   1 
ATOM   899  C CA  . GLY A 1 123 ? 1.120   36.359  10.927 1.00 8.26  ? 140 GLY A CA  1 
ATOM   900  C C   . GLY A 1 123 ? 0.527   36.909  9.651  1.00 7.43  ? 140 GLY A C   1 
ATOM   901  O O   . GLY A 1 123 ? 0.353   36.165  8.686  1.00 9.70  ? 140 GLY A O   1 
ATOM   902  N N   . SER A 1 124 ? 0.237   38.209  9.624  1.00 7.96  ? 141 SER A N   1 
ATOM   903  C CA  . SER A 1 124 ? -0.303  38.837  8.421  1.00 7.88  ? 141 SER A CA  1 
ATOM   904  C C   . SER A 1 124 ? 0.576   38.573  7.206  1.00 9.03  ? 141 SER A C   1 
ATOM   905  O O   . SER A 1 124 ? 1.806   38.615  7.282  1.00 8.37  ? 141 SER A O   1 
ATOM   906  C CB  . SER A 1 124 ? -0.359  40.355  8.612  1.00 9.15  ? 141 SER A CB  1 
ATOM   907  O OG  . SER A 1 124 ? -1.006  40.695  9.808  1.00 9.91  ? 141 SER A OG  1 
ATOM   908  N N   . ASP A 1 125 ? -0.057  38.373  6.055  1.00 9.21  ? 142 ASP A N   1 
ATOM   909  C CA  . ASP A 1 125 ? 0.694   38.076  4.841  1.00 11.00 ? 142 ASP A CA  1 
ATOM   910  C C   . ASP A 1 125 ? 0.894   39.267  3.908  1.00 11.78 ? 142 ASP A C   1 
ATOM   911  O O   . ASP A 1 125 ? 1.535   39.105  2.868  1.00 15.78 ? 142 ASP A O   1 
ATOM   912  C CB  . ASP A 1 125 ? 0.061   36.905  4.084  1.00 12.81 ? 142 ASP A CB  1 
ATOM   913  C CG  . ASP A 1 125 ? -1.331  37.213  3.543  1.00 18.69 ? 142 ASP A CG  1 
ATOM   914  O OD1 . ASP A 1 125 ? -1.798  38.366  3.623  1.00 19.87 ? 142 ASP A OD1 1 
ATOM   915  O OD2 . ASP A 1 125 ? -1.958  36.279  3.007  1.00 21.00 ? 142 ASP A OD2 1 
ATOM   916  N N   . SER A 1 126 ? 0.395   40.449  4.252  1.00 9.64  ? 143 SER A N   1 
ATOM   917  C CA  . SER A 1 126 ? 0.492   41.603  3.367  1.00 11.39 ? 143 SER A CA  1 
ATOM   918  C C   . SER A 1 126 ? 0.176   42.856  4.171  1.00 12.08 ? 143 SER A C   1 
ATOM   919  O O   . SER A 1 126 ? -0.349  42.785  5.285  1.00 11.44 ? 143 SER A O   1 
ATOM   920  C CB  . SER A 1 126 ? -0.493  41.496  2.198  1.00 13.15 ? 143 SER A CB  1 
ATOM   921  O OG  . SER A 1 126 ? -1.822  41.520  2.685  1.00 16.32 ? 143 SER A OG  1 
ATOM   922  N N   . ALA A 1 127 ? 0.474   44.015  3.575  1.00 12.11 ? 144 ALA A N   1 
ATOM   923  C CA  . ALA A 1 127 ? 0.104   45.276  4.207  1.00 10.69 ? 144 ALA A CA  1 
ATOM   924  C C   . ALA A 1 127 ? -1.405  45.373  4.418  1.00 12.52 ? 144 ALA A C   1 
ATOM   925  O O   . ALA A 1 127 ? -1.869  45.825  5.471  1.00 13.17 ? 144 ALA A O   1 
ATOM   926  C CB  . ALA A 1 127 ? 0.603   46.456  3.368  1.00 13.90 ? 144 ALA A CB  1 
ATOM   927  N N   . GLU A 1 128 ? -2.188  44.960  3.424  1.00 11.74 ? 145 GLU A N   1 
ATOM   928  C CA  . GLU A 1 128 ? -3.636  45.032  3.549  1.00 14.01 ? 145 GLU A CA  1 
ATOM   929  C C   . GLU A 1 128 ? -4.148  44.097  4.637  1.00 11.63 ? 145 GLU A C   1 
ATOM   930  O O   . GLU A 1 128 ? -5.002  44.485  5.440  1.00 13.92 ? 145 GLU A O   1 
ATOM   931  C CB  . GLU A 1 128 ? -4.280  44.727  2.201  1.00 18.83 ? 145 GLU A CB  1 
ATOM   932  C CG  . GLU A 1 128 ? -3.951  45.769  1.117  1.00 21.10 ? 145 GLU A CG  1 
ATOM   933  C CD  . GLU A 1 128 ? -2.597  45.541  0.404  1.00 22.61 ? 145 GLU A CD  1 
ATOM   934  O OE1 . GLU A 1 128 ? -1.890  44.537  0.683  1.00 20.54 ? 145 GLU A OE1 1 
ATOM   935  O OE2 . GLU A 1 128 ? -2.246  46.380  -0.459 1.00 26.25 ? 145 GLU A OE2 1 
ATOM   936  N N   . SER A 1 129 ? -3.614  42.874  4.714  1.00 12.39 ? 146 SER A N   1 
ATOM   937  C CA  A SER A 1 129 ? -4.096  41.972  5.752  0.49 10.40 ? 146 SER A CA  1 
ATOM   938  C CA  B SER A 1 129 ? -4.064  41.951  5.750  0.51 10.48 ? 146 SER A CA  1 
ATOM   939  C C   . SER A 1 129 ? -3.661  42.439  7.134  1.00 9.49  ? 146 SER A C   1 
ATOM   940  O O   . SER A 1 129 ? -4.418  42.283  8.099  1.00 9.37  ? 146 SER A O   1 
ATOM   941  C CB  A SER A 1 129 ? -3.680  40.525  5.467  0.49 13.06 ? 146 SER A CB  1 
ATOM   942  C CB  B SER A 1 129 ? -3.508  40.554  5.481  0.51 13.35 ? 146 SER A CB  1 
ATOM   943  O OG  A SER A 1 129 ? -2.279  40.391  5.344  0.49 11.95 ? 146 SER A OG  1 
ATOM   944  O OG  B SER A 1 129 ? -4.167  39.959  4.379  0.51 12.42 ? 146 SER A OG  1 
ATOM   945  N N   . ALA A 1 130 ? -2.475  43.038  7.252  1.00 10.80 ? 147 ALA A N   1 
ATOM   946  C CA  . ALA A 1 130 ? -2.041  43.542  8.550  1.00 11.31 ? 147 ALA A CA  1 
ATOM   947  C C   . ALA A 1 130 ? -2.983  44.630  9.047  1.00 10.06 ? 147 ALA A C   1 
ATOM   948  O O   . ALA A 1 130 ? -3.395  44.623  10.210 1.00 10.54 ? 147 ALA A O   1 
ATOM   949  C CB  . ALA A 1 130 ? -0.599  44.052  8.469  1.00 12.78 ? 147 ALA A CB  1 
ATOM   950  N N   . LYS A 1 131 ? -3.330  45.586  8.182  1.00 11.20 ? 148 LYS A N   1 
ATOM   951  C CA  . LYS A 1 131 ? -4.210  46.670  8.610  1.00 11.93 ? 148 LYS A CA  1 
ATOM   952  C C   . LYS A 1 131 ? -5.573  46.128  9.031  1.00 11.96 ? 148 LYS A C   1 
ATOM   953  O O   . LYS A 1 131 ? -6.113  46.510  10.079 1.00 11.84 ? 148 LYS A O   1 
ATOM   954  C CB  . LYS A 1 131 ? -4.358  47.686  7.483  1.00 12.41 ? 148 LYS A CB  1 
ATOM   955  C CG  . LYS A 1 131 ? -5.155  48.896  7.833  1.00 14.84 ? 148 LYS A CG  1 
ATOM   956  C CD  . LYS A 1 131 ? -5.144  49.854  6.649  1.00 19.42 ? 148 LYS A CD  1 
ATOM   957  C CE  . LYS A 1 131 ? -5.847  51.142  6.986  1.00 23.44 ? 148 LYS A CE  1 
ATOM   958  N NZ  . LYS A 1 131 ? -7.230  50.879  7.444  1.00 25.81 ? 148 LYS A NZ  1 
ATOM   959  N N   . ARG A 1 132 ? -6.126  45.208  8.243  1.00 10.44 ? 149 ARG A N   1 
ATOM   960  C CA  . ARG A 1 132 ? -7.441  44.653  8.547  1.00 11.16 ? 149 ARG A CA  1 
ATOM   961  C C   . ARG A 1 132 ? -7.416  43.841  9.835  1.00 9.89  ? 149 ARG A C   1 
ATOM   962  O O   . ARG A 1 132 ? -8.334  43.944  10.659 1.00 11.16 ? 149 ARG A O   1 
ATOM   963  C CB  . ARG A 1 132 ? -7.886  43.777  7.382  1.00 13.20 ? 149 ARG A CB  1 
ATOM   964  C CG  . ARG A 1 132 ? -9.282  43.238  7.493  1.00 16.87 ? 149 ARG A CG  1 
ATOM   965  C CD  . ARG A 1 132 ? -9.585  42.363  6.281  1.00 21.67 ? 149 ARG A CD  1 
ATOM   966  N NE  . ARG A 1 132 ? -9.019  41.033  6.441  1.00 24.64 ? 149 ARG A NE  1 
ATOM   967  C CZ  . ARG A 1 132 ? -9.580  40.084  7.178  1.00 29.89 ? 149 ARG A CZ  1 
ATOM   968  N NH1 . ARG A 1 132 ? -10.735 40.280  7.799  1.00 31.88 ? 149 ARG A NH1 1 
ATOM   969  N NH2 . ARG A 1 132 ? -8.966  38.915  7.302  1.00 31.07 ? 149 ARG A NH2 1 
ATOM   970  N N   . GLU A 1 133 ? -6.380  43.014  10.012 1.00 8.75  ? 150 GLU A N   1 
ATOM   971  C CA  . GLU A 1 133 ? -6.305  42.121  11.168 1.00 8.56  ? 150 GLU A CA  1 
ATOM   972  C C   . GLU A 1 133 ? -6.058  42.894  12.456 1.00 9.87  ? 150 GLU A C   1 
ATOM   973  O O   . GLU A 1 133 ? -6.650  42.580  13.493 1.00 10.59 ? 150 GLU A O   1 
ATOM   974  C CB  . GLU A 1 133 ? -5.218  41.063  10.951 1.00 8.67  ? 150 GLU A CB  1 
ATOM   975  C CG  . GLU A 1 133 ? -5.591  40.065  9.876  1.00 11.88 ? 150 GLU A CG  1 
ATOM   976  C CD  . GLU A 1 133 ? -4.461  39.142  9.465  1.00 10.55 ? 150 GLU A CD  1 
ATOM   977  O OE1 . GLU A 1 133 ? -3.356  39.224  10.043 1.00 10.71 ? 150 GLU A OE1 1 
ATOM   978  O OE2 . GLU A 1 133 ? -4.690  38.321  8.545  1.00 11.29 ? 150 GLU A OE2 1 
ATOM   979  N N   . ILE A 1 134 ? -5.177  43.897  12.418 1.00 9.29  ? 151 ILE A N   1 
ATOM   980  C CA  . ILE A 1 134 ? -4.949  44.717  13.602 1.00 10.81 ? 151 ILE A CA  1 
ATOM   981  C C   . ILE A 1 134 ? -6.252  45.379  14.023 1.00 11.48 ? 151 ILE A C   1 
ATOM   982  O O   . ILE A 1 134 ? -6.600  45.416  15.206 1.00 12.00 ? 151 ILE A O   1 
ATOM   983  C CB  . ILE A 1 134 ? -3.836  45.745  13.323 1.00 11.05 ? 151 ILE A CB  1 
ATOM   984  C CG1 . ILE A 1 134 ? -2.488  45.044  13.150 1.00 10.72 ? 151 ILE A CG1 1 
ATOM   985  C CG2 . ILE A 1 134 ? -3.803  46.807  14.423 1.00 11.44 ? 151 ILE A CG2 1 
ATOM   986  C CD1 . ILE A 1 134 ? -1.357  45.962  12.712 1.00 9.68  ? 151 ILE A CD1 1 
ATOM   987  N N   . SER A 1 135 ? -7.004  45.893  13.056 1.00 8.83  ? 152 SER A N   1 
ATOM   988  C CA  . SER A 1 135 ? -8.280  46.520  13.374 1.00 10.47 ? 152 SER A CA  1 
ATOM   989  C C   . SER A 1 135 ? -9.309  45.518  13.887 1.00 11.60 ? 152 SER A C   1 
ATOM   990  O O   . SER A 1 135 ? -10.133 45.869  14.731 1.00 11.37 ? 152 SER A O   1 
ATOM   991  C CB  . SER A 1 135 ? -8.805  47.272  12.156 1.00 12.77 ? 152 SER A CB  1 
ATOM   992  O OG  . SER A 1 135 ? -7.914  48.324  11.826 1.00 16.48 ? 152 SER A OG  1 
ATOM   993  N N   . LEU A 1 136 ? -9.285  44.281  13.396 1.00 10.56 ? 153 LEU A N   1 
ATOM   994  C CA  . LEU A 1 136 ? -10.253 43.290  13.856 1.00 8.95  ? 153 LEU A CA  1 
ATOM   995  C C   . LEU A 1 136 ? -10.025 42.915  15.319 1.00 10.57 ? 153 LEU A C   1 
ATOM   996  O O   . LEU A 1 136 ? -10.983 42.771  16.085 1.00 10.77 ? 153 LEU A O   1 
ATOM   997  C CB  . LEU A 1 136 ? -10.175 42.040  12.983 1.00 10.59 ? 153 LEU A CB  1 
ATOM   998  C CG  . LEU A 1 136 ? -11.080 40.876  13.372 1.00 11.38 ? 153 LEU A CG  1 
ATOM   999  C CD1 . LEU A 1 136 ? -12.562 41.266  13.283 1.00 15.77 ? 153 LEU A CD1 1 
ATOM   1000 C CD2 . LEU A 1 136 ? -10.778 39.673  12.479 1.00 11.61 ? 153 LEU A CD2 1 
ATOM   1001 N N   . TRP A 1 137 ? -8.770  42.706  15.711 1.00 9.55  ? 154 TRP A N   1 
ATOM   1002 C CA  . TRP A 1 137 ? -8.455  42.165  17.025 1.00 8.09  ? 154 TRP A CA  1 
ATOM   1003 C C   . TRP A 1 137 ? -8.160  43.225  18.078 1.00 10.68 ? 154 TRP A C   1 
ATOM   1004 O O   . TRP A 1 137 ? -8.198  42.905  19.275 1.00 11.56 ? 154 TRP A O   1 
ATOM   1005 C CB  . TRP A 1 137 ? -7.276  41.197  16.930 1.00 9.68  ? 154 TRP A CB  1 
ATOM   1006 C CG  . TRP A 1 137 ? -7.577  39.966  16.129 1.00 8.69  ? 154 TRP A CG  1 
ATOM   1007 C CD1 . TRP A 1 137 ? -7.338  39.767  14.798 1.00 8.45  ? 154 TRP A CD1 1 
ATOM   1008 C CD2 . TRP A 1 137 ? -8.156  38.749  16.617 1.00 9.81  ? 154 TRP A CD2 1 
ATOM   1009 N NE1 . TRP A 1 137 ? -7.733  38.503  14.433 1.00 9.82  ? 154 TRP A NE1 1 
ATOM   1010 C CE2 . TRP A 1 137 ? -8.230  37.858  15.532 1.00 9.67  ? 154 TRP A CE2 1 
ATOM   1011 C CE3 . TRP A 1 137 ? -8.606  38.326  17.869 1.00 9.60  ? 154 TRP A CE3 1 
ATOM   1012 C CZ2 . TRP A 1 137 ? -8.735  36.569  15.659 1.00 10.00 ? 154 TRP A CZ2 1 
ATOM   1013 C CZ3 . TRP A 1 137 ? -9.080  37.044  17.995 1.00 8.72  ? 154 TRP A CZ3 1 
ATOM   1014 C CH2 . TRP A 1 137 ? -9.169  36.189  16.891 1.00 10.60 ? 154 TRP A CH2 1 
ATOM   1015 N N   . PHE A 1 138 ? -7.887  44.470  17.672 1.00 9.51  ? 155 PHE A N   1 
ATOM   1016 C CA  . PHE A 1 138 ? -7.563  45.548  18.593 1.00 9.96  ? 155 PHE A CA  1 
ATOM   1017 C C   . PHE A 1 138 ? -8.377  46.798  18.273 1.00 10.34 ? 155 PHE A C   1 
ATOM   1018 O O   . PHE A 1 138 ? -8.670  47.090  17.114 1.00 13.87 ? 155 PHE A O   1 
ATOM   1019 C CB  . PHE A 1 138 ? -6.082  45.929  18.490 1.00 9.36  ? 155 PHE A CB  1 
ATOM   1020 C CG  . PHE A 1 138 ? -5.139  44.907  19.059 1.00 7.79  ? 155 PHE A CG  1 
ATOM   1021 C CD1 . PHE A 1 138 ? -4.935  44.837  20.425 1.00 6.99  ? 155 PHE A CD1 1 
ATOM   1022 C CD2 . PHE A 1 138 ? -4.425  44.070  18.237 1.00 8.90  ? 155 PHE A CD2 1 
ATOM   1023 C CE1 . PHE A 1 138 ? -4.055  43.932  20.973 1.00 8.62  ? 155 PHE A CE1 1 
ATOM   1024 C CE2 . PHE A 1 138 ? -3.553  43.138  18.783 1.00 7.75  ? 155 PHE A CE2 1 
ATOM   1025 C CZ  . PHE A 1 138 ? -3.356  43.082  20.148 1.00 8.38  ? 155 PHE A CZ  1 
ATOM   1026 N N   . LYS A 1 139 ? -8.719  47.543  19.308 1.00 10.48 ? 156 LYS A N   1 
ATOM   1027 C CA  . LYS A 1 139 ? -9.233  48.886  19.129 1.00 11.43 ? 156 LYS A CA  1 
ATOM   1028 C C   . LYS A 1 139 ? -8.062  49.844  18.984 1.00 9.68  ? 156 LYS A C   1 
ATOM   1029 O O   . LYS A 1 139 ? -6.956  49.561  19.462 1.00 10.60 ? 156 LYS A O   1 
ATOM   1030 C CB  . LYS A 1 139 ? -10.041 49.281  20.355 1.00 17.88 ? 156 LYS A CB  1 
ATOM   1031 C CG  . LYS A 1 139 ? -11.192 48.330  20.680 1.00 22.11 ? 156 LYS A CG  1 
ATOM   1032 C CD  . LYS A 1 139 ? -11.896 48.746  21.977 1.00 27.18 ? 156 LYS A CD  1 
ATOM   1033 C CE  . LYS A 1 139 ? -13.170 47.932  22.222 1.00 33.13 ? 156 LYS A CE  1 
ATOM   1034 N NZ  . LYS A 1 139 ? -14.247 48.273  21.233 1.00 37.64 ? 156 LYS A NZ  1 
ATOM   1035 N N   . PRO A 1 140 ? -8.269  51.002  18.350 1.00 12.18 ? 157 PRO A N   1 
ATOM   1036 C CA  . PRO A 1 140 ? -7.139  51.929  18.205 1.00 13.61 ? 157 PRO A CA  1 
ATOM   1037 C C   . PRO A 1 140 ? -6.521  52.336  19.533 1.00 13.30 ? 157 PRO A C   1 
ATOM   1038 O O   . PRO A 1 140 ? -5.303  52.527  19.613 1.00 13.45 ? 157 PRO A O   1 
ATOM   1039 C CB  . PRO A 1 140 ? -7.747  53.127  17.463 1.00 16.33 ? 157 PRO A CB  1 
ATOM   1040 C CG  . PRO A 1 140 ? -8.913  52.570  16.743 1.00 16.79 ? 157 PRO A CG  1 
ATOM   1041 C CD  . PRO A 1 140 ? -9.450  51.448  17.588 1.00 14.94 ? 157 PRO A CD  1 
ATOM   1042 N N   . GLU A 1 141 ? -7.324  52.441  20.587 1.00 13.54 ? 158 GLU A N   1 
ATOM   1043 C CA  . GLU A 1 141 ? -6.839  52.823  21.905 1.00 15.78 ? 158 GLU A CA  1 
ATOM   1044 C C   . GLU A 1 141 ? -5.924  51.777  22.522 1.00 13.52 ? 158 GLU A C   1 
ATOM   1045 O O   . GLU A 1 141 ? -5.267  52.067  23.523 1.00 14.47 ? 158 GLU A O   1 
ATOM   1046 C CB  . GLU A 1 141 ? -8.052  53.041  22.811 1.00 20.07 ? 158 GLU A CB  1 
ATOM   1047 C CG  . GLU A 1 141 ? -8.889  54.251  22.410 1.00 27.38 ? 158 GLU A CG  1 
ATOM   1048 C CD  . GLU A 1 141 ? -10.011 53.989  21.385 1.00 30.61 ? 158 GLU A CD  1 
ATOM   1049 O OE1 . GLU A 1 141 ? -10.112 52.905  20.753 1.00 21.16 ? 158 GLU A OE1 1 
ATOM   1050 O OE2 . GLU A 1 141 ? -10.818 54.924  21.213 1.00 38.66 ? 158 GLU A OE2 1 
ATOM   1051 N N   . GLU A 1 142 ? -5.876  50.576  21.960 1.00 10.31 ? 159 GLU A N   1 
ATOM   1052 C CA  . GLU A 1 142 ? -5.044  49.507  22.489 1.00 9.80  ? 159 GLU A CA  1 
ATOM   1053 C C   . GLU A 1 142 ? -3.668  49.475  21.847 1.00 9.10  ? 159 GLU A C   1 
ATOM   1054 O O   . GLU A 1 142 ? -2.781  48.772  22.343 1.00 9.47  ? 159 GLU A O   1 
ATOM   1055 C CB  . GLU A 1 142 ? -5.767  48.155  22.340 1.00 10.24 ? 159 GLU A CB  1 
ATOM   1056 C CG  . GLU A 1 142 ? -7.030  48.070  23.235 1.00 12.84 ? 159 GLU A CG  1 
ATOM   1057 C CD  . GLU A 1 142 ? -7.925  46.882  22.968 1.00 14.66 ? 159 GLU A CD  1 
ATOM   1058 O OE1 . GLU A 1 142 ? -7.964  46.400  21.822 1.00 14.45 ? 159 GLU A OE1 1 
ATOM   1059 O OE2 . GLU A 1 142 ? -8.615  46.448  23.926 1.00 18.13 ? 159 GLU A OE2 1 
ATOM   1060 N N   . ILE A 1 143 ? -3.464  50.251  20.792 1.00 10.00 ? 160 ILE A N   1 
ATOM   1061 C CA  . ILE A 1 143 ? -2.181  50.311  20.102 1.00 9.75  ? 160 ILE A CA  1 
ATOM   1062 C C   . ILE A 1 143 ? -1.347  51.406  20.760 1.00 11.19 ? 160 ILE A C   1 
ATOM   1063 O O   . ILE A 1 143 ? -1.738  52.579  20.766 1.00 10.06 ? 160 ILE A O   1 
ATOM   1064 C CB  . ILE A 1 143 ? -2.369  50.601  18.606 1.00 10.17 ? 160 ILE A CB  1 
ATOM   1065 C CG1 . ILE A 1 143 ? -3.412  49.663  17.985 1.00 11.10 ? 160 ILE A CG1 1 
ATOM   1066 C CG2 . ILE A 1 143 ? -1.014  50.538  17.897 1.00 11.16 ? 160 ILE A CG2 1 
ATOM   1067 C CD1 . ILE A 1 143 ? -3.071  48.184  18.060 1.00 13.68 ? 160 ILE A CD1 1 
ATOM   1068 N N   . GLN A 1 144 ? -0.189  51.026  21.289 1.00 8.55  ? 161 GLN A N   1 
ATOM   1069 C CA  . GLN A 1 144 ? 0.650   51.890  22.110 1.00 8.50  ? 161 GLN A CA  1 
ATOM   1070 C C   . GLN A 1 144 ? 1.831   52.401  21.298 1.00 9.02  ? 161 GLN A C   1 
ATOM   1071 O O   . GLN A 1 144 ? 2.537   51.613  20.651 1.00 9.81  ? 161 GLN A O   1 
ATOM   1072 C CB  . GLN A 1 144 ? 1.177   51.095  23.311 1.00 9.89  ? 161 GLN A CB  1 
ATOM   1073 C CG  . GLN A 1 144 ? 0.116   50.346  24.079 1.00 10.65 ? 161 GLN A CG  1 
ATOM   1074 C CD  . GLN A 1 144 ? -0.955  51.264  24.620 1.00 11.22 ? 161 GLN A CD  1 
ATOM   1075 O OE1 . GLN A 1 144 ? -0.668  52.396  25.026 1.00 10.98 ? 161 GLN A OE1 1 
ATOM   1076 N NE2 . GLN A 1 144 ? -2.194  50.787  24.634 1.00 11.69 ? 161 GLN A NE2 1 
ATOM   1077 N N   . SER A 1 145 ? 2.062   53.713  21.365 1.00 8.58  ? 162 SER A N   1 
ATOM   1078 C CA  A SER A 1 145 ? 3.159   54.369  20.664 0.55 9.01  ? 162 SER A CA  1 
ATOM   1079 C CA  B SER A 1 145 ? 3.165   54.354  20.666 0.45 9.75  ? 162 SER A CA  1 
ATOM   1080 C C   . SER A 1 145 ? 4.194   54.812  21.686 1.00 9.16  ? 162 SER A C   1 
ATOM   1081 O O   . SER A 1 145 ? 3.877   55.587  22.591 1.00 11.69 ? 162 SER A O   1 
ATOM   1082 C CB  A SER A 1 145 ? 2.649   55.591  19.895 0.55 9.63  ? 162 SER A CB  1 
ATOM   1083 C CB  B SER A 1 145 ? 2.649   55.534  19.843 0.45 11.33 ? 162 SER A CB  1 
ATOM   1084 O OG  A SER A 1 145 ? 3.711   56.308  19.282 0.55 12.98 ? 162 SER A OG  1 
ATOM   1085 O OG  B SER A 1 145 ? 1.794   55.065  18.812 0.45 11.59 ? 162 SER A OG  1 
ATOM   1086 N N   . TYR A 1 146 ? 5.419   54.327  21.528 1.00 8.40  ? 163 TYR A N   1 
ATOM   1087 C CA  . TYR A 1 146 ? 6.575   54.697  22.336 1.00 9.34  ? 163 TYR A CA  1 
ATOM   1088 C C   . TYR A 1 146 ? 7.804   54.349  21.507 1.00 7.63  ? 163 TYR A C   1 
ATOM   1089 O O   . TYR A 1 146 ? 7.714   53.610  20.528 1.00 10.23 ? 163 TYR A O   1 
ATOM   1090 C CB  . TYR A 1 146 ? 6.586   53.999  23.706 1.00 9.89  ? 163 TYR A CB  1 
ATOM   1091 C CG  . TYR A 1 146 ? 6.649   52.501  23.633 1.00 9.34  ? 163 TYR A CG  1 
ATOM   1092 C CD1 . TYR A 1 146 ? 5.497   51.744  23.492 1.00 7.90  ? 163 TYR A CD1 1 
ATOM   1093 C CD2 . TYR A 1 146 ? 7.865   51.841  23.697 1.00 8.25  ? 163 TYR A CD2 1 
ATOM   1094 C CE1 . TYR A 1 146 ? 5.559   50.348  23.421 1.00 9.12  ? 163 TYR A CE1 1 
ATOM   1095 C CE2 . TYR A 1 146 ? 7.934   50.464  23.630 1.00 7.60  ? 163 TYR A CE2 1 
ATOM   1096 C CZ  . TYR A 1 146 ? 6.786   49.719  23.476 1.00 8.98  ? 163 TYR A CZ  1 
ATOM   1097 O OH  . TYR A 1 146 ? 6.901   48.347  23.396 1.00 7.57  ? 163 TYR A OH  1 
ATOM   1098 N N   . LYS A 1 147 ? 8.941   54.920  21.880 1.00 8.68  ? 164 LYS A N   1 
ATOM   1099 C CA  . LYS A 1 147 ? 10.184  54.763  21.132 1.00 8.66  ? 164 LYS A CA  1 
ATOM   1100 C C   . LYS A 1 147 ? 11.116  53.847  21.910 1.00 8.94  ? 164 LYS A C   1 
ATOM   1101 O O   . LYS A 1 147 ? 11.317  54.041  23.113 1.00 10.62 ? 164 LYS A O   1 
ATOM   1102 C CB  . LYS A 1 147 ? 10.861  56.118  20.909 1.00 10.94 ? 164 LYS A CB  1 
ATOM   1103 C CG  . LYS A 1 147 ? 12.168  56.082  20.130 1.00 15.27 ? 164 LYS A CG  1 
ATOM   1104 C CD  . LYS A 1 147 ? 12.723  57.518  19.949 1.00 17.63 ? 164 LYS A CD  1 
ATOM   1105 C CE  . LYS A 1 147 ? 14.068  57.543  19.239 1.00 26.52 ? 164 LYS A CE  1 
ATOM   1106 N NZ  . LYS A 1 147 ? 13.953  57.076  17.839 1.00 33.35 ? 164 LYS A NZ  1 
ATOM   1107 N N   . LEU A 1 148 ? 11.685  52.859  21.229 1.00 10.79 ? 165 LEU A N   1 
ATOM   1108 C CA  . LEU A 1 148 ? 12.691  52.012  21.859 1.00 7.93  ? 165 LEU A CA  1 
ATOM   1109 C C   . LEU A 1 148 ? 13.942  52.812  22.166 1.00 8.46  ? 165 LEU A C   1 
ATOM   1110 O O   . LEU A 1 148 ? 14.482  53.517  21.307 1.00 9.22  ? 165 LEU A O   1 
ATOM   1111 C CB  . LEU A 1 148 ? 13.065  50.827  20.966 1.00 10.31 ? 165 LEU A CB  1 
ATOM   1112 C CG  . LEU A 1 148 ? 12.020  49.703  20.865 1.00 12.61 ? 165 LEU A CG  1 
ATOM   1113 C CD1 . LEU A 1 148 ? 12.401  48.654  19.820 1.00 11.13 ? 165 LEU A CD1 1 
ATOM   1114 C CD2 . LEU A 1 148 ? 11.811  49.049  22.224 1.00 12.46 ? 165 LEU A CD2 1 
ATOM   1115 N N   . ALA A 1 149 ? 14.441  52.643  23.386 1.00 9.49  ? 166 ALA A N   1 
ATOM   1116 C CA  . ALA A 1 149 ? 15.615  53.384  23.828 1.00 12.78 ? 166 ALA A CA  1 
ATOM   1117 C C   . ALA A 1 149 ? 16.847  53.085  22.982 1.00 13.18 ? 166 ALA A C   1 
ATOM   1118 O O   . ALA A 1 149 ? 17.705  53.959  22.823 1.00 12.48 ? 166 ALA A O   1 
ATOM   1119 C CB  . ALA A 1 149 ? 15.885  53.051  25.298 1.00 17.71 ? 166 ALA A CB  1 
ATOM   1120 N N   . LEU A 1 150 ? 16.952  51.876  22.417 1.00 11.05 ? 167 LEU A N   1 
ATOM   1121 C CA  . LEU A 1 150 ? 18.100  51.515  21.590 1.00 9.76  ? 167 LEU A CA  1 
ATOM   1122 C C   . LEU A 1 150 ? 17.881  51.784  20.108 1.00 9.73  ? 167 LEU A C   1 
ATOM   1123 O O   . LEU A 1 150 ? 18.643  51.279  19.283 1.00 9.30  ? 167 LEU A O   1 
ATOM   1124 C CB  . LEU A 1 150 ? 18.501  50.057  21.821 1.00 12.33 ? 167 LEU A CB  1 
ATOM   1125 C CG  . LEU A 1 150 ? 19.258  49.750  23.119 1.00 14.62 ? 167 LEU A CG  1 
ATOM   1126 C CD1 . LEU A 1 150 ? 19.376  48.237  23.359 1.00 14.77 ? 167 LEU A CD1 1 
ATOM   1127 C CD2 . LEU A 1 150 ? 20.621  50.383  23.086 1.00 22.01 ? 167 LEU A CD2 1 
ATOM   1128 N N   . SER A 1 151 ? 16.903  52.625  19.770 1.00 10.51 ? 168 SER A N   1 
ATOM   1129 C CA  A SER A 1 151 ? 16.588  52.898  18.371 0.48 11.24 ? 168 SER A CA  1 
ATOM   1130 C CA  B SER A 1 151 ? 16.593  52.890  18.368 0.52 11.44 ? 168 SER A CA  1 
ATOM   1131 C C   . SER A 1 151 ? 17.826  53.280  17.567 1.00 10.73 ? 168 SER A C   1 
ATOM   1132 O O   . SER A 1 151 ? 17.980  52.860  16.415 1.00 10.73 ? 168 SER A O   1 
ATOM   1133 C CB  A SER A 1 151 ? 15.543  54.017  18.320 0.48 13.15 ? 168 SER A CB  1 
ATOM   1134 C CB  B SER A 1 151 ? 15.554  54.003  18.269 0.52 12.22 ? 168 SER A CB  1 
ATOM   1135 O OG  A SER A 1 151 ? 15.319  54.489  17.006 0.48 15.32 ? 168 SER A OG  1 
ATOM   1136 O OG  B SER A 1 151 ? 14.270  53.514  18.591 0.52 13.40 ? 168 SER A OG  1 
ATOM   1137 N N   . ASP A 1 152 ? 18.716  54.081  18.153 1.00 10.44 ? 169 ASP A N   1 
ATOM   1138 C CA  . ASP A 1 152 ? 19.882  54.557  17.417 1.00 14.07 ? 169 ASP A CA  1 
ATOM   1139 C C   . ASP A 1 152 ? 20.804  53.421  16.995 1.00 11.03 ? 169 ASP A C   1 
ATOM   1140 O O   . ASP A 1 152 ? 21.595  53.598  16.063 1.00 13.62 ? 169 ASP A O   1 
ATOM   1141 C CB  . ASP A 1 152 ? 20.685  55.541  18.269 1.00 14.96 ? 169 ASP A CB  1 
ATOM   1142 C CG  . ASP A 1 152 ? 20.034  56.913  18.374 1.00 22.94 ? 169 ASP A CG  1 
ATOM   1143 O OD1 . ASP A 1 152 ? 19.042  57.175  17.668 1.00 26.93 ? 169 ASP A OD1 1 
ATOM   1144 O OD2 . ASP A 1 152 ? 20.527  57.728  19.185 1.00 26.26 ? 169 ASP A OD2 1 
ATOM   1145 N N   . TYR A 1 153 ? 20.747  52.279  17.681 1.00 10.66 ? 170 TYR A N   1 
ATOM   1146 C CA  . TYR A 1 153 ? 21.587  51.125  17.384 1.00 10.02 ? 170 TYR A CA  1 
ATOM   1147 C C   . TYR A 1 153 ? 20.834  50.015  16.662 1.00 9.26  ? 170 TYR A C   1 
ATOM   1148 O O   . TYR A 1 153 ? 21.411  48.965  16.389 1.00 9.53  ? 170 TYR A O   1 
ATOM   1149 C CB  . TYR A 1 153 ? 22.253  50.618  18.674 1.00 9.53  ? 170 TYR A CB  1 
ATOM   1150 C CG  . TYR A 1 153 ? 23.164  51.672  19.241 1.00 10.62 ? 170 TYR A CG  1 
ATOM   1151 C CD1 . TYR A 1 153 ? 24.425  51.884  18.697 1.00 10.03 ? 170 TYR A CD1 1 
ATOM   1152 C CD2 . TYR A 1 153 ? 22.743  52.517  20.259 1.00 11.52 ? 170 TYR A CD2 1 
ATOM   1153 C CE1 . TYR A 1 153 ? 25.239  52.890  19.156 1.00 10.54 ? 170 TYR A CE1 1 
ATOM   1154 C CE2 . TYR A 1 153 ? 23.572  53.523  20.743 1.00 12.03 ? 170 TYR A CE2 1 
ATOM   1155 C CZ  . TYR A 1 153 ? 24.809  53.702  20.185 1.00 11.52 ? 170 TYR A CZ  1 
ATOM   1156 O OH  . TYR A 1 153 ? 25.634  54.690  20.652 1.00 15.69 ? 170 TYR A OH  1 
ATOM   1157 N N   . ILE A 1 154 ? 19.576  50.242  16.306 1.00 10.88 ? 171 ILE A N   1 
ATOM   1158 C CA  . ILE A 1 154 ? 18.769  49.276  15.574 1.00 10.25 ? 171 ILE A CA  1 
ATOM   1159 C C   . ILE A 1 154 ? 18.496  49.749  14.151 1.00 12.84 ? 171 ILE A C   1 
ATOM   1160 O O   . ILE A 1 154 ? 18.602  48.974  13.195 1.00 12.81 ? 171 ILE A O   1 
ATOM   1161 C CB  . ILE A 1 154 ? 17.449  49.040  16.344 1.00 11.64 ? 171 ILE A CB  1 
ATOM   1162 C CG1 . ILE A 1 154 ? 17.719  48.369  17.696 1.00 13.92 ? 171 ILE A CG1 1 
ATOM   1163 C CG2 . ILE A 1 154 ? 16.458  48.227  15.494 1.00 12.69 ? 171 ILE A CG2 1 
ATOM   1164 C CD1 . ILE A 1 154 ? 16.567  48.460  18.675 1.00 14.16 ? 171 ILE A CD1 1 
ATOM   1165 N N   . PHE A 1 155 ? 18.182  51.030  13.992 1.00 12.39 ? 172 PHE A N   1 
ATOM   1166 C CA  . PHE A 1 155 ? 17.806  51.609  12.711 1.00 12.74 ? 172 PHE A CA  1 
ATOM   1167 C C   . PHE A 1 155 ? 18.947  52.437  12.141 1.00 15.76 ? 172 PHE A C   1 
ATOM   1168 O O   . PHE A 1 155 ? 19.667  53.116  12.877 1.00 16.88 ? 172 PHE A O   1 
ATOM   1169 C CB  . PHE A 1 155 ? 16.575  52.495  12.892 1.00 12.15 ? 172 PHE A CB  1 
ATOM   1170 C CG  . PHE A 1 155 ? 15.448  51.780  13.548 1.00 10.88 ? 172 PHE A CG  1 
ATOM   1171 C CD1 . PHE A 1 155 ? 14.807  50.743  12.894 1.00 11.78 ? 172 PHE A CD1 1 
ATOM   1172 C CD2 . PHE A 1 155 ? 15.069  52.085  14.842 1.00 12.30 ? 172 PHE A CD2 1 
ATOM   1173 C CE1 . PHE A 1 155 ? 13.781  50.049  13.499 1.00 14.20 ? 172 PHE A CE1 1 
ATOM   1174 C CE2 . PHE A 1 155 ? 14.037  51.392  15.448 1.00 13.34 ? 172 PHE A CE2 1 
ATOM   1175 C CZ  . PHE A 1 155 ? 13.401  50.375  14.774 1.00 13.27 ? 172 PHE A CZ  1 
ATOM   1176 N N   . GLU A 1 156 ? 19.099  52.371  10.823 1.00 21.18 ? 173 GLU A N   1 
ATOM   1177 C CA  . GLU A 1 156 ? 20.023  53.213  10.074 1.00 25.91 ? 173 GLU A CA  1 
ATOM   1178 C C   . GLU A 1 156 ? 19.755  54.678  10.276 1.00 30.24 ? 173 GLU A C   1 
ATOM   1179 O O   . GLU A 1 156 ? 20.676  55.490  10.173 1.00 35.47 ? 173 GLU A O   1 
ATOM   1180 C CB  . GLU A 1 156 ? 19.864  52.933  8.588  1.00 26.70 ? 173 GLU A CB  1 
ATOM   1181 C CG  . GLU A 1 156 ? 20.610  51.740  8.150  1.00 28.55 ? 173 GLU A CG  1 
ATOM   1182 C CD  . GLU A 1 156 ? 20.330  51.367  6.722  1.00 24.82 ? 173 GLU A CD  1 
ATOM   1183 O OE1 . GLU A 1 156 ? 19.614  52.111  6.006  1.00 27.70 ? 173 GLU A OE1 1 
ATOM   1184 O OE2 . GLU A 1 156 ? 20.849  50.318  6.319  1.00 18.46 ? 173 GLU A OE2 1 
ATOM   1185 O OXT . GLU A 1 156 ? 18.611  55.072  10.499 1.00 29.98 ? 173 GLU A OXT 1 
ATOM   1186 N N   . HIS B 1 8   ? -0.483  9.150   11.110 1.00 33.71 ? 25  HIS B N   1 
ATOM   1187 C CA  . HIS B 1 8   ? 0.649   8.271   10.848 1.00 27.98 ? 25  HIS B CA  1 
ATOM   1188 C C   . HIS B 1 8   ? 1.955   8.895   11.330 1.00 25.74 ? 25  HIS B C   1 
ATOM   1189 O O   . HIS B 1 8   ? 2.425   9.906   10.808 1.00 29.42 ? 25  HIS B O   1 
ATOM   1190 C CB  . HIS B 1 8   ? 0.757   7.942   9.359  1.00 31.26 ? 25  HIS B CB  1 
ATOM   1191 N N   . VAL B 1 9   ? 2.536   8.277   12.339 1.00 21.05 ? 26  VAL B N   1 
ATOM   1192 C CA  . VAL B 1 9   ? 3.874   8.620   12.784 1.00 15.91 ? 26  VAL B CA  1 
ATOM   1193 C C   . VAL B 1 9   ? 4.800   7.490   12.377 1.00 16.45 ? 26  VAL B C   1 
ATOM   1194 O O   . VAL B 1 9   ? 4.372   6.384   12.045 1.00 16.43 ? 26  VAL B O   1 
ATOM   1195 C CB  . VAL B 1 9   ? 3.954   8.889   14.305 1.00 17.31 ? 26  VAL B CB  1 
ATOM   1196 C CG1 . VAL B 1 9   ? 3.139   10.128  14.663 1.00 17.01 ? 26  VAL B CG1 1 
ATOM   1197 C CG2 . VAL B 1 9   ? 3.478   7.679   15.095 1.00 16.29 ? 26  VAL B CG2 1 
ATOM   1198 N N   . GLU B 1 10  ? 6.085   7.782   12.392 1.00 12.45 ? 27  GLU B N   1 
ATOM   1199 C CA  . GLU B 1 10  ? 7.115   6.771   12.214 1.00 11.37 ? 27  GLU B CA  1 
ATOM   1200 C C   . GLU B 1 10  ? 8.183   6.958   13.280 1.00 9.33  ? 27  GLU B C   1 
ATOM   1201 O O   . GLU B 1 10  ? 8.112   7.881   14.097 1.00 10.01 ? 27  GLU B O   1 
ATOM   1202 C CB  . GLU B 1 10  ? 7.713   6.824   10.811 1.00 18.74 ? 27  GLU B CB  1 
ATOM   1203 C CG  . GLU B 1 10  ? 8.257   8.159   10.471 1.00 16.45 ? 27  GLU B CG  1 
ATOM   1204 C CD  . GLU B 1 10  ? 8.565   8.313   8.993  1.00 18.41 ? 27  GLU B CD  1 
ATOM   1205 O OE1 . GLU B 1 10  ? 7.935   7.661   8.139  1.00 23.92 ? 27  GLU B OE1 1 
ATOM   1206 O OE2 . GLU B 1 10  ? 9.464   9.097   8.690  1.00 13.72 ? 27  GLU B OE2 1 
ATOM   1207 N N   . GLN B 1 11  ? 9.162   6.051   13.279 1.00 10.63 ? 28  GLN B N   1 
ATOM   1208 C CA  . GLN B 1 11  ? 10.253  6.043   14.242 1.00 8.66  ? 28  GLN B CA  1 
ATOM   1209 C C   . GLN B 1 11  ? 11.579  6.006   13.504 1.00 10.02 ? 28  GLN B C   1 
ATOM   1210 O O   . GLN B 1 11  ? 11.725  5.307   12.496 1.00 11.60 ? 28  GLN B O   1 
ATOM   1211 C CB  . GLN B 1 11  ? 10.137  4.834   15.164 1.00 10.41 ? 28  GLN B CB  1 
ATOM   1212 C CG  . GLN B 1 11  ? 8.997   4.987   16.159 1.00 11.44 ? 28  GLN B CG  1 
ATOM   1213 C CD  . GLN B 1 11  ? 8.882   3.845   17.142 1.00 11.95 ? 28  GLN B CD  1 
ATOM   1214 O OE1 . GLN B 1 11  ? 9.649   2.878   17.096 1.00 14.94 ? 28  GLN B OE1 1 
ATOM   1215 N NE2 . GLN B 1 11  ? 7.929   3.959   18.064 1.00 15.01 ? 28  GLN B NE2 1 
ATOM   1216 N N   . THR B 1 12  ? 12.537  6.779   13.994 1.00 9.26  ? 29  THR B N   1 
ATOM   1217 C CA  . THR B 1 12  ? 13.868  6.786   13.422 1.00 8.93  ? 29  THR B CA  1 
ATOM   1218 C C   . THR B 1 12  ? 14.888  6.476   14.505 1.00 9.01  ? 29  THR B C   1 
ATOM   1219 O O   . THR B 1 12  ? 14.636  6.686   15.696 1.00 8.31  ? 29  THR B O   1 
ATOM   1220 C CB  . THR B 1 12  ? 14.171  8.132   12.755 1.00 9.46  ? 29  THR B CB  1 
ATOM   1221 O OG1 . THR B 1 12  ? 15.340  7.986   11.953 1.00 10.93 ? 29  THR B OG1 1 
ATOM   1222 C CG2 . THR B 1 12  ? 14.374  9.237   13.778 1.00 8.80  ? 29  THR B CG2 1 
ATOM   1223 N N   . TYR B 1 13  ? 16.032  5.946   14.069 1.00 8.49  ? 30  TYR B N   1 
ATOM   1224 C CA  . TYR B 1 13  ? 17.162  5.690   14.951 1.00 7.54  ? 30  TYR B CA  1 
ATOM   1225 C C   . TYR B 1 13  ? 18.108  6.884   14.895 1.00 8.22  ? 30  TYR B C   1 
ATOM   1226 O O   . TYR B 1 13  ? 18.601  7.249   13.823 1.00 8.82  ? 30  TYR B O   1 
ATOM   1227 C CB  . TYR B 1 13  ? 17.909  4.407   14.574 1.00 8.43  ? 30  TYR B CB  1 
ATOM   1228 C CG  . TYR B 1 13  ? 19.079  4.160   15.496 1.00 10.12 ? 30  TYR B CG  1 
ATOM   1229 C CD1 . TYR B 1 13  ? 18.876  3.825   16.826 1.00 9.97  ? 30  TYR B CD1 1 
ATOM   1230 C CD2 . TYR B 1 13  ? 20.382  4.305   15.051 1.00 10.80 ? 30  TYR B CD2 1 
ATOM   1231 C CE1 . TYR B 1 13  ? 19.930  3.626   17.674 1.00 9.83  ? 30  TYR B CE1 1 
ATOM   1232 C CE2 . TYR B 1 13  ? 21.446  4.112   15.904 1.00 9.81  ? 30  TYR B CE2 1 
ATOM   1233 C CZ  . TYR B 1 13  ? 21.211  3.780   17.217 1.00 9.68  ? 30  TYR B CZ  1 
ATOM   1234 O OH  . TYR B 1 13  ? 22.256  3.587   18.100 1.00 11.82 ? 30  TYR B OH  1 
ATOM   1235 N N   . LEU B 1 14  ? 18.344  7.492   16.044 1.00 8.19  ? 31  LEU B N   1 
ATOM   1236 C CA  . LEU B 1 14  ? 19.305  8.575   16.187 1.00 8.44  ? 31  LEU B CA  1 
ATOM   1237 C C   . LEU B 1 14  ? 20.338  8.176   17.230 1.00 7.78  ? 31  LEU B C   1 
ATOM   1238 O O   . LEU B 1 14  ? 19.997  7.604   18.263 1.00 10.17 ? 31  LEU B O   1 
ATOM   1239 C CB  . LEU B 1 14  ? 18.602  9.867   16.625 1.00 8.36  ? 31  LEU B CB  1 
ATOM   1240 C CG  . LEU B 1 14  ? 17.724  10.508  15.535 1.00 10.13 ? 31  LEU B CG  1 
ATOM   1241 C CD1 . LEU B 1 14  ? 16.642  11.416  16.115 1.00 11.28 ? 31  LEU B CD1 1 
ATOM   1242 C CD2 . LEU B 1 14  ? 18.604  11.302  14.580 1.00 12.51 ? 31  LEU B CD2 1 
ATOM   1243 N N   . MET B 1 15  ? 21.605  8.484   16.968 1.00 8.04  ? 32  MET B N   1 
ATOM   1244 C CA  . MET B 1 15  ? 22.675  8.067   17.862 1.00 7.97  ? 32  MET B CA  1 
ATOM   1245 C C   . MET B 1 15  ? 23.627  9.234   18.058 1.00 7.67  ? 32  MET B C   1 
ATOM   1246 O O   . MET B 1 15  ? 24.199  9.743   17.093 1.00 9.19  ? 32  MET B O   1 
ATOM   1247 C CB  . MET B 1 15  ? 23.406  6.859   17.275 1.00 8.81  ? 32  MET B CB  1 
ATOM   1248 C CG  . MET B 1 15  ? 24.535  6.361   18.132 1.00 10.37 ? 32  MET B CG  1 
ATOM   1249 S SD  . MET B 1 15  ? 25.239  4.776   17.606 1.00 12.70 ? 32  MET B SD  1 
ATOM   1250 C CE  . MET B 1 15  ? 25.586  5.101   15.881 1.00 13.65 ? 32  MET B CE  1 
ATOM   1251 N N   . ILE B 1 16  ? 23.801  9.656   19.302 1.00 6.66  ? 33  ILE B N   1 
ATOM   1252 C CA  . ILE B 1 16  ? 24.814  10.661  19.611 1.00 6.79  ? 33  ILE B CA  1 
ATOM   1253 C C   . ILE B 1 16  ? 26.166  9.962   19.616 1.00 6.63  ? 33  ILE B C   1 
ATOM   1254 O O   . ILE B 1 16  ? 26.370  8.989   20.351 1.00 8.39  ? 33  ILE B O   1 
ATOM   1255 C CB  . ILE B 1 16  ? 24.536  11.355  20.951 1.00 7.49  ? 33  ILE B CB  1 
ATOM   1256 C CG1 . ILE B 1 16  ? 23.120  11.932  20.937 1.00 8.85  ? 33  ILE B CG1 1 
ATOM   1257 C CG2 . ILE B 1 16  ? 25.626  12.411  21.211 1.00 8.58  ? 33  ILE B CG2 1 
ATOM   1258 C CD1 . ILE B 1 16  ? 22.769  12.706  22.183 1.00 9.02  ? 33  ILE B CD1 1 
ATOM   1259 N N   . LYS B 1 17  ? 27.087  10.465  18.797 1.00 6.98  ? 34  LYS B N   1 
ATOM   1260 C CA  . LYS B 1 17  ? 28.417  9.890   18.621 1.00 6.97  ? 34  LYS B CA  1 
ATOM   1261 C C   . LYS B 1 17  ? 29.313  10.308  19.780 1.00 7.98  ? 34  LYS B C   1 
ATOM   1262 O O   . LYS B 1 17  ? 28.957  11.169  20.576 1.00 7.97  ? 34  LYS B O   1 
ATOM   1263 C CB  . LYS B 1 17  ? 28.996  10.354  17.285 1.00 7.80  ? 34  LYS B CB  1 
ATOM   1264 C CG  . LYS B 1 17  ? 28.150  9.988   16.065 1.00 7.27  ? 34  LYS B CG  1 
ATOM   1265 C CD  . LYS B 1 17  ? 28.821  10.409  14.748 1.00 8.60  ? 34  LYS B CD  1 
ATOM   1266 C CE  . LYS B 1 17  ? 28.022  9.944   13.553 1.00 9.41  ? 34  LYS B CE  1 
ATOM   1267 N NZ  . LYS B 1 17  ? 28.617  10.349  12.263 1.00 10.30 ? 34  LYS B NZ  1 
ATOM   1268 N N   . PRO B 1 18  ? 30.497  9.697   19.911 1.00 8.53  ? 35  PRO B N   1 
ATOM   1269 C CA  . PRO B 1 18  ? 31.349  9.995   21.079 1.00 7.28  ? 35  PRO B CA  1 
ATOM   1270 C C   . PRO B 1 18  ? 31.705  11.463  21.223 1.00 7.95  ? 35  PRO B C   1 
ATOM   1271 O O   . PRO B 1 18  ? 31.881  11.936  22.351 1.00 8.87  ? 35  PRO B O   1 
ATOM   1272 C CB  . PRO B 1 18  ? 32.573  9.103   20.851 1.00 8.77  ? 35  PRO B CB  1 
ATOM   1273 C CG  . PRO B 1 18  ? 32.029  7.953   20.059 1.00 9.02  ? 35  PRO B CG  1 
ATOM   1274 C CD  . PRO B 1 18  ? 31.031  8.578   19.116 1.00 8.43  ? 35  PRO B CD  1 
ATOM   1275 N N   . ASP B 1 19  ? 31.810  12.205  20.120 1.00 7.36  ? 36  ASP B N   1 
ATOM   1276 C CA  . ASP B 1 19  ? 32.051  13.644  20.221 1.00 9.02  ? 36  ASP B CA  1 
ATOM   1277 C C   . ASP B 1 19  ? 30.885  14.374  20.876 1.00 8.39  ? 36  ASP B C   1 
ATOM   1278 O O   . ASP B 1 19  ? 31.098  15.360  21.587 1.00 9.41  ? 36  ASP B O   1 
ATOM   1279 C CB  . ASP B 1 19  ? 32.433  14.280  18.875 1.00 8.85  ? 36  ASP B CB  1 
ATOM   1280 C CG  . ASP B 1 19  ? 31.490  13.950  17.711 1.00 10.77 ? 36  ASP B CG  1 
ATOM   1281 O OD1 . ASP B 1 19  ? 30.938  12.823  17.623 1.00 11.54 ? 36  ASP B OD1 1 
ATOM   1282 O OD2 . ASP B 1 19  ? 31.353  14.842  16.829 1.00 9.85  ? 36  ASP B OD2 1 
ATOM   1283 N N   . GLY B 1 20  ? 29.644  13.937  20.630 1.00 8.23  ? 37  GLY B N   1 
ATOM   1284 C CA  . GLY B 1 20  ? 28.522  14.545  21.324 1.00 8.70  ? 37  GLY B CA  1 
ATOM   1285 C C   . GLY B 1 20  ? 28.550  14.266  22.817 1.00 7.74  ? 37  GLY B C   1 
ATOM   1286 O O   . GLY B 1 20  ? 28.186  15.129  23.628 1.00 7.06  ? 37  GLY B O   1 
ATOM   1287 N N   . ILE B 1 21  ? 28.960  13.049  23.199 1.00 7.74  ? 38  ILE B N   1 
ATOM   1288 C CA  . ILE B 1 21  ? 29.104  12.714  24.614 1.00 7.87  ? 38  ILE B CA  1 
ATOM   1289 C C   . ILE B 1 21  ? 30.219  13.540  25.232 1.00 7.76  ? 38  ILE B C   1 
ATOM   1290 O O   . ILE B 1 21  ? 30.046  14.156  26.279 1.00 8.15  ? 38  ILE B O   1 
ATOM   1291 C CB  . ILE B 1 21  ? 29.384  11.208  24.799 1.00 9.79  ? 38  ILE B CB  1 
ATOM   1292 C CG1 . ILE B 1 21  ? 28.373  10.334  24.056 1.00 11.21 ? 38  ILE B CG1 1 
ATOM   1293 C CG2 . ILE B 1 21  ? 29.448  10.863  26.275 1.00 9.49  ? 38  ILE B CG2 1 
ATOM   1294 C CD1 . ILE B 1 21  ? 26.975  10.447  24.544 1.00 11.66 ? 38  ILE B CD1 1 
ATOM   1295 N N   . GLN B 1 22  ? 31.388  13.552  24.597 1.00 8.33  ? 39  GLN B N   1 
ATOM   1296 C CA  . GLN B 1 22  ? 32.560  14.163  25.215 1.00 8.22  ? 39  GLN B CA  1 
ATOM   1297 C C   . GLN B 1 22  ? 32.478  15.683  25.251 1.00 8.06  ? 39  GLN B C   1 
ATOM   1298 O O   . GLN B 1 22  ? 33.023  16.312  26.168 1.00 9.09  ? 39  GLN B O   1 
ATOM   1299 C CB  . GLN B 1 22  ? 33.821  13.723  24.467 1.00 8.17  ? 39  GLN B CB  1 
ATOM   1300 C CG  . GLN B 1 22  ? 34.209  12.276  24.679 1.00 9.22  ? 39  GLN B CG  1 
ATOM   1301 C CD  . GLN B 1 22  ? 34.819  12.053  26.027 1.00 10.62 ? 39  GLN B CD  1 
ATOM   1302 O OE1 . GLN B 1 22  ? 34.921  12.978  26.828 1.00 12.41 ? 39  GLN B OE1 1 
ATOM   1303 N NE2 . GLN B 1 22  ? 35.235  10.815  26.293 1.00 11.34 ? 39  GLN B NE2 1 
ATOM   1304 N N   . ARG B 1 23  ? 31.816  16.294  24.270 1.00 8.90  ? 40  ARG B N   1 
ATOM   1305 C CA  . ARG B 1 23  ? 31.592  17.735  24.282 1.00 9.73  ? 40  ARG B CA  1 
ATOM   1306 C C   . ARG B 1 23  ? 30.437  18.111  25.193 1.00 7.53  ? 40  ARG B C   1 
ATOM   1307 O O   . ARG B 1 23  ? 30.181  19.307  25.402 1.00 8.39  ? 40  ARG B O   1 
ATOM   1308 C CB  . ARG B 1 23  ? 31.397  18.235  22.847 1.00 7.95  ? 40  ARG B CB  1 
ATOM   1309 C CG  . ARG B 1 23  ? 32.656  18.058  22.000 1.00 7.31  ? 40  ARG B CG  1 
ATOM   1310 C CD  . ARG B 1 23  ? 32.451  18.462  20.565 1.00 9.20  ? 40  ARG B CD  1 
ATOM   1311 N NE  . ARG B 1 23  ? 32.241  19.899  20.472 1.00 9.29  ? 40  ARG B NE  1 
ATOM   1312 C CZ  . ARG B 1 23  ? 31.728  20.510  19.415 1.00 9.15  ? 40  ARG B CZ  1 
ATOM   1313 N NH1 . ARG B 1 23  ? 31.390  19.839  18.333 1.00 9.25  ? 40  ARG B NH1 1 
ATOM   1314 N NH2 . ARG B 1 23  ? 31.539  21.827  19.450 1.00 10.94 ? 40  ARG B NH2 1 
ATOM   1315 N N   . GLN B 1 24  ? 29.749  17.117  25.743 1.00 7.77  ? 41  GLN B N   1 
ATOM   1316 C CA  . GLN B 1 24  ? 28.715  17.300  26.764 1.00 8.12  ? 41  GLN B CA  1 
ATOM   1317 C C   . GLN B 1 24  ? 27.544  18.148  26.267 1.00 8.73  ? 41  GLN B C   1 
ATOM   1318 O O   . GLN B 1 24  ? 27.072  19.072  26.936 1.00 8.70  ? 41  GLN B O   1 
ATOM   1319 C CB  . GLN B 1 24  ? 29.302  17.798  28.084 1.00 8.03  ? 41  GLN B CB  1 
ATOM   1320 C CG  . GLN B 1 24  ? 30.396  16.838  28.591 1.00 9.55  ? 41  GLN B CG  1 
ATOM   1321 C CD  . GLN B 1 24  ? 30.375  16.677  30.085 1.00 10.08 ? 41  GLN B CD  1 
ATOM   1322 O OE1 . GLN B 1 24  ? 31.088  17.367  30.803 1.00 11.36 ? 41  GLN B OE1 1 
ATOM   1323 N NE2 . GLN B 1 24  ? 29.548  15.768  30.564 1.00 10.32 ? 41  GLN B NE2 1 
ATOM   1324 N N   . VAL B 1 25  ? 27.051  17.790  25.082 1.00 8.16  ? 42  VAL B N   1 
ATOM   1325 C CA  . VAL B 1 25  ? 25.908  18.442  24.454 1.00 6.65  ? 42  VAL B CA  1 
ATOM   1326 C C   . VAL B 1 25  ? 24.735  17.472  24.295 1.00 5.51  ? 42  VAL B C   1 
ATOM   1327 O O   . VAL B 1 25  ? 23.832  17.700  23.473 1.00 7.52  ? 42  VAL B O   1 
ATOM   1328 C CB  . VAL B 1 25  ? 26.299  19.090  23.110 1.00 8.04  ? 42  VAL B CB  1 
ATOM   1329 C CG1 . VAL B 1 25  ? 27.270  20.242  23.354 1.00 9.23  ? 42  VAL B CG1 1 
ATOM   1330 C CG2 . VAL B 1 25  ? 26.875  18.080  22.139 1.00 9.46  ? 42  VAL B CG2 1 
ATOM   1331 N N   . VAL B 1 26  ? 24.717  16.395  25.087 1.00 6.73  ? 43  VAL B N   1 
ATOM   1332 C CA  . VAL B 1 26  ? 23.648  15.403  24.965 1.00 7.10  ? 43  VAL B CA  1 
ATOM   1333 C C   . VAL B 1 26  ? 22.291  16.040  25.217 1.00 8.08  ? 43  VAL B C   1 
ATOM   1334 O O   . VAL B 1 26  ? 21.338  15.839  24.453 1.00 6.88  ? 43  VAL B O   1 
ATOM   1335 C CB  . VAL B 1 26  ? 23.904  14.221  25.923 1.00 7.22  ? 43  VAL B CB  1 
ATOM   1336 C CG1 . VAL B 1 26  ? 22.648  13.334  26.050 1.00 8.56  ? 43  VAL B CG1 1 
ATOM   1337 C CG2 . VAL B 1 26  ? 25.123  13.420  25.490 1.00 8.81  ? 43  VAL B CG2 1 
ATOM   1338 N N   . GLY B 1 27  ? 22.177  16.797  26.305 1.00 7.06  ? 44  GLY B N   1 
ATOM   1339 C CA  . GLY B 1 27  ? 20.892  17.383  26.628 1.00 7.35  ? 44  GLY B CA  1 
ATOM   1340 C C   . GLY B 1 27  ? 20.428  18.364  25.576 1.00 7.20  ? 44  GLY B C   1 
ATOM   1341 O O   . GLY B 1 27  ? 19.240  18.407  25.242 1.00 6.81  ? 44  GLY B O   1 
ATOM   1342 N N   . GLU B 1 28  ? 21.353  19.162  25.032 1.00 8.30  ? 45  GLU B N   1 
ATOM   1343 C CA  . GLU B 1 28  ? 20.961  20.107  23.992 1.00 8.09  ? 45  GLU B CA  1 
ATOM   1344 C C   . GLU B 1 28  ? 20.434  19.387  22.764 1.00 6.03  ? 45  GLU B C   1 
ATOM   1345 O O   . GLU B 1 28  ? 19.454  19.824  22.145 1.00 8.34  ? 45  GLU B O   1 
ATOM   1346 C CB  . GLU B 1 28  ? 22.157  20.938  23.568 1.00 8.91  ? 45  GLU B CB  1 
ATOM   1347 C CG  . GLU B 1 28  ? 22.553  22.019  24.503 1.00 11.37 ? 45  GLU B CG  1 
ATOM   1348 C CD  . GLU B 1 28  ? 23.480  22.964  23.800 1.00 16.94 ? 45  GLU B CD  1 
ATOM   1349 O OE1 . GLU B 1 28  ? 23.000  23.809  23.005 1.00 20.56 ? 45  GLU B OE1 1 
ATOM   1350 O OE2 . GLU B 1 28  ? 24.688  22.784  23.971 1.00 20.69 ? 45  GLU B OE2 1 
ATOM   1351 N N   . ILE B 1 29  ? 21.075  18.285  22.388 1.00 6.04  ? 46  ILE B N   1 
ATOM   1352 C CA  . ILE B 1 29  ? 20.612  17.543  21.225 1.00 7.40  ? 46  ILE B CA  1 
ATOM   1353 C C   . ILE B 1 29  ? 19.208  17.009  21.482 1.00 6.58  ? 46  ILE B C   1 
ATOM   1354 O O   . ILE B 1 29  ? 18.308  17.143  20.651 1.00 8.72  ? 46  ILE B O   1 
ATOM   1355 C CB  . ILE B 1 29  ? 21.611  16.419  20.894 1.00 8.09  ? 46  ILE B CB  1 
ATOM   1356 C CG1 . ILE B 1 29  ? 22.947  17.007  20.411 1.00 8.28  ? 46  ILE B CG1 1 
ATOM   1357 C CG2 . ILE B 1 29  ? 21.006  15.454  19.875 1.00 9.08  ? 46  ILE B CG2 1 
ATOM   1358 C CD1 . ILE B 1 29  ? 24.080  15.981  20.308 1.00 11.21 ? 46  ILE B CD1 1 
ATOM   1359 N N   . ILE B 1 30  ? 19.006  16.383  22.640 1.00 6.87  ? 47  ILE B N   1 
ATOM   1360 C CA  . ILE B 1 30  ? 17.701  15.821  22.955 1.00 5.93  ? 47  ILE B CA  1 
ATOM   1361 C C   . ILE B 1 30  ? 16.647  16.919  22.940 1.00 5.53  ? 47  ILE B C   1 
ATOM   1362 O O   . ILE B 1 30  ? 15.543  16.739  22.414 1.00 7.15  ? 47  ILE B O   1 
ATOM   1363 C CB  . ILE B 1 30  ? 17.754  15.068  24.298 1.00 6.21  ? 47  ILE B CB  1 
ATOM   1364 C CG1 . ILE B 1 30  ? 18.587  13.797  24.183 1.00 7.24  ? 47  ILE B CG1 1 
ATOM   1365 C CG2 . ILE B 1 30  ? 16.341  14.749  24.777 1.00 8.33  ? 47  ILE B CG2 1 
ATOM   1366 C CD1 . ILE B 1 30  ? 18.946  13.197  25.523 1.00 8.38  ? 47  ILE B CD1 1 
ATOM   1367 N N   . SER B 1 31  ? 16.963  18.065  23.532 1.00 5.78  ? 48  SER B N   1 
ATOM   1368 C CA  . SER B 1 31  ? 15.999  19.168  23.568 1.00 6.42  ? 48  SER B CA  1 
ATOM   1369 C C   . SER B 1 31  ? 15.548  19.590  22.176 1.00 4.56  ? 48  SER B C   1 
ATOM   1370 O O   . SER B 1 31  ? 14.405  20.012  22.009 1.00 7.72  ? 48  SER B O   1 
ATOM   1371 C CB  . SER B 1 31  ? 16.570  20.365  24.323 1.00 7.31  ? 48  SER B CB  1 
ATOM   1372 O OG  . SER B 1 31  ? 16.677  20.080  25.705 1.00 6.67  ? 48  SER B OG  1 
ATOM   1373 N N   . ARG B 1 32  ? 16.430  19.530  21.174 1.00 6.57  ? 49  ARG B N   1 
ATOM   1374 C CA  . ARG B 1 32  ? 16.027  19.958  19.839 1.00 7.02  ? 49  ARG B CA  1 
ATOM   1375 C C   . ARG B 1 32  ? 14.911  19.088  19.294 1.00 7.53  ? 49  ARG B C   1 
ATOM   1376 O O   . ARG B 1 32  ? 14.044  19.577  18.570 1.00 7.34  ? 49  ARG B O   1 
ATOM   1377 C CB  . ARG B 1 32  ? 17.211  19.934  18.875 1.00 9.36  ? 49  ARG B CB  1 
ATOM   1378 C CG  . ARG B 1 32  ? 18.201  21.033  19.132 1.00 10.10 ? 49  ARG B CG  1 
ATOM   1379 C CD  . ARG B 1 32  ? 19.077  21.226  17.950 1.00 14.52 ? 49  ARG B CD  1 
ATOM   1380 N NE  . ARG B 1 32  ? 19.970  22.344  18.184 1.00 14.72 ? 49  ARG B NE  1 
ATOM   1381 C CZ  . ARG B 1 32  ? 20.509  23.080  17.231 1.00 13.01 ? 49  ARG B CZ  1 
ATOM   1382 N NH1 . ARG B 1 32  ? 20.239  22.858  15.950 1.00 13.76 ? 49  ARG B NH1 1 
ATOM   1383 N NH2 . ARG B 1 32  ? 21.318  24.078  17.574 1.00 14.46 ? 49  ARG B NH2 1 
ATOM   1384 N N   . PHE B 1 33  ? 14.959  17.780  19.582 1.00 7.28  ? 50  PHE B N   1 
ATOM   1385 C CA  . PHE B 1 33  ? 13.920  16.859  19.123 1.00 7.34  ? 50  PHE B CA  1 
ATOM   1386 C C   . PHE B 1 33  ? 12.664  16.958  19.982 1.00 6.76  ? 50  PHE B C   1 
ATOM   1387 O O   . PHE B 1 33  ? 11.549  16.983  19.454 1.00 6.56  ? 50  PHE B O   1 
ATOM   1388 C CB  . PHE B 1 33  ? 14.506  15.447  19.054 1.00 8.13  ? 50  PHE B CB  1 
ATOM   1389 C CG  . PHE B 1 33  ? 15.593  15.316  18.020 1.00 7.09  ? 50  PHE B CG  1 
ATOM   1390 C CD1 . PHE B 1 33  ? 15.286  15.330  16.677 1.00 9.18  ? 50  PHE B CD1 1 
ATOM   1391 C CD2 . PHE B 1 33  ? 16.917  15.221  18.386 1.00 10.57 ? 50  PHE B CD2 1 
ATOM   1392 C CE1 . PHE B 1 33  ? 16.271  15.264  15.731 1.00 9.18  ? 50  PHE B CE1 1 
ATOM   1393 C CE2 . PHE B 1 33  ? 17.903  15.123  17.436 1.00 10.48 ? 50  PHE B CE2 1 
ATOM   1394 C CZ  . PHE B 1 33  ? 17.581  15.136  16.113 1.00 9.11  ? 50  PHE B CZ  1 
ATOM   1395 N N   . GLU B 1 34  ? 12.829  17.069  21.297 1.00 7.18  ? 51  GLU B N   1 
ATOM   1396 C CA  . GLU B 1 34  ? 11.681  17.280  22.162 1.00 7.46  ? 51  GLU B CA  1 
ATOM   1397 C C   . GLU B 1 34  ? 10.932  18.541  21.780 1.00 7.61  ? 51  GLU B C   1 
ATOM   1398 O O   . GLU B 1 34  ? 9.714   18.601  21.947 1.00 7.70  ? 51  GLU B O   1 
ATOM   1399 C CB  . GLU B 1 34  ? 12.114  17.391  23.626 1.00 6.81  ? 51  GLU B CB  1 
ATOM   1400 C CG  . GLU B 1 34  ? 12.443  16.078  24.299 1.00 8.33  ? 51  GLU B CG  1 
ATOM   1401 C CD  . GLU B 1 34  ? 12.825  16.282  25.749 1.00 8.70  ? 51  GLU B CD  1 
ATOM   1402 O OE1 . GLU B 1 34  ? 13.806  17.023  25.973 1.00 8.14  ? 51  GLU B OE1 1 
ATOM   1403 O OE2 . GLU B 1 34  ? 12.113  15.764  26.646 1.00 8.18  ? 51  GLU B OE2 1 
ATOM   1404 N N   . LYS B 1 35  ? 11.648  19.563  21.299 1.00 6.93  ? 52  LYS B N   1 
ATOM   1405 C CA  . LYS B 1 35  ? 11.025  20.855  21.037 1.00 8.06  ? 52  LYS B CA  1 
ATOM   1406 C C   . LYS B 1 35  ? 9.935   20.763  19.981 1.00 6.40  ? 52  LYS B C   1 
ATOM   1407 O O   . LYS B 1 35  ? 8.989   21.557  19.999 1.00 7.79  ? 52  LYS B O   1 
ATOM   1408 C CB  . LYS B 1 35  ? 12.086  21.844  20.566 1.00 9.62  ? 52  LYS B CB  1 
ATOM   1409 C CG  . LYS B 1 35  ? 11.666  23.299  20.648 1.00 11.50 ? 52  LYS B CG  1 
ATOM   1410 C CD  . LYS B 1 35  ? 12.801  24.166  20.149 1.00 13.88 ? 52  LYS B CD  1 
ATOM   1411 C CE  . LYS B 1 35  ? 12.593  25.634  20.463 1.00 17.02 ? 52  LYS B CE  1 
ATOM   1412 N NZ  . LYS B 1 35  ? 12.732  25.872  21.920 1.00 20.23 ? 52  LYS B NZ  1 
ATOM   1413 N N   . ARG B 1 36  ? 10.031  19.798  19.072 1.00 6.44  ? 53  ARG B N   1 
ATOM   1414 C CA  . ARG B 1 36  ? 9.030   19.616  18.028 1.00 7.01  ? 53  ARG B CA  1 
ATOM   1415 C C   . ARG B 1 36  ? 7.933   18.649  18.442 1.00 6.71  ? 53  ARG B C   1 
ATOM   1416 O O   . ARG B 1 36  ? 7.071   18.329  17.626 1.00 6.85  ? 53  ARG B O   1 
ATOM   1417 C CB  . ARG B 1 36  ? 9.683   19.131  16.724 1.00 6.96  ? 53  ARG B CB  1 
ATOM   1418 C CG  . ARG B 1 36  ? 10.704  20.104  16.151 1.00 9.01  ? 53  ARG B CG  1 
ATOM   1419 C CD  . ARG B 1 36  ? 11.191  19.687  14.792 1.00 7.69  ? 53  ARG B CD  1 
ATOM   1420 N NE  . ARG B 1 36  ? 10.134  19.728  13.786 1.00 6.99  ? 53  ARG B NE  1 
ATOM   1421 C CZ  . ARG B 1 36  ? 10.335  19.458  12.503 1.00 6.31  ? 53  ARG B CZ  1 
ATOM   1422 N NH1 . ARG B 1 36  ? 11.498  19.006  12.067 1.00 7.45  ? 53  ARG B NH1 1 
ATOM   1423 N NH2 . ARG B 1 36  ? 9.358   19.661  11.634 1.00 7.47  ? 53  ARG B NH2 1 
ATOM   1424 N N   . GLY B 1 37  ? 7.942   18.189  19.686 1.00 6.73  ? 54  GLY B N   1 
ATOM   1425 C CA  . GLY B 1 37  ? 6.970   17.209  20.118 1.00 7.12  ? 54  GLY B CA  1 
ATOM   1426 C C   . GLY B 1 37  ? 7.256   15.802  19.658 1.00 7.72  ? 54  GLY B C   1 
ATOM   1427 O O   . GLY B 1 37  ? 6.345   14.965  19.632 1.00 7.66  ? 54  GLY B O   1 
ATOM   1428 N N   . TYR B 1 38  ? 8.494   15.504  19.291 1.00 7.06  ? 55  TYR B N   1 
ATOM   1429 C CA  . TYR B 1 38  ? 8.858   14.121  19.022 1.00 6.41  ? 55  TYR B CA  1 
ATOM   1430 C C   . TYR B 1 38  ? 8.943   13.364  20.341 1.00 7.37  ? 55  TYR B C   1 
ATOM   1431 O O   . TYR B 1 38  ? 9.398   13.895  21.359 1.00 9.17  ? 55  TYR B O   1 
ATOM   1432 C CB  . TYR B 1 38  ? 10.193  14.075  18.294 1.00 7.16  ? 55  TYR B CB  1 
ATOM   1433 C CG  . TYR B 1 38  ? 10.186  14.670  16.893 1.00 6.41  ? 55  TYR B CG  1 
ATOM   1434 C CD1 . TYR B 1 38  ? 9.054   14.636  16.085 1.00 8.47  ? 55  TYR B CD1 1 
ATOM   1435 C CD2 . TYR B 1 38  ? 11.335  15.239  16.363 1.00 7.75  ? 55  TYR B CD2 1 
ATOM   1436 C CE1 . TYR B 1 38  ? 9.068   15.174  14.806 1.00 8.27  ? 55  TYR B CE1 1 
ATOM   1437 C CE2 . TYR B 1 38  ? 11.350  15.777  15.088 1.00 7.91  ? 55  TYR B CE2 1 
ATOM   1438 C CZ  . TYR B 1 38  ? 10.221  15.738  14.321 1.00 8.48  ? 55  TYR B CZ  1 
ATOM   1439 O OH  . TYR B 1 38  ? 10.269  16.282  13.056 1.00 8.71  ? 55  TYR B OH  1 
ATOM   1440 N N   . ARG B 1 39  ? 8.508   12.114  20.318 1.00 6.44  ? 56  ARG B N   1 
ATOM   1441 C CA  . ARG B 1 39  ? 8.444   11.276  21.506 1.00 8.06  ? 56  ARG B CA  1 
ATOM   1442 C C   . ARG B 1 39  ? 9.692   10.411  21.598 1.00 8.57  ? 56  ARG B C   1 
ATOM   1443 O O   . ARG B 1 39  ? 10.074  9.751   20.628 1.00 8.77  ? 56  ARG B O   1 
ATOM   1444 C CB  . ARG B 1 39  ? 7.211   10.380  21.452 1.00 9.01  ? 56  ARG B CB  1 
ATOM   1445 C CG  . ARG B 1 39  ? 6.987   9.576   22.715 1.00 9.45  ? 56  ARG B CG  1 
ATOM   1446 C CD  . ARG B 1 39  ? 5.698   8.782   22.625 1.00 8.79  ? 56  ARG B CD  1 
ATOM   1447 N NE  . ARG B 1 39  ? 5.765   7.704   21.643 1.00 10.24 ? 56  ARG B NE  1 
ATOM   1448 C CZ  . ARG B 1 39  ? 6.199   6.482   21.915 1.00 9.60  ? 56  ARG B CZ  1 
ATOM   1449 N NH1 . ARG B 1 39  ? 6.700   6.175   23.104 1.00 12.16 ? 56  ARG B NH1 1 
ATOM   1450 N NH2 . ARG B 1 39  ? 6.109   5.537   20.979 1.00 13.58 ? 56  ARG B NH2 1 
ATOM   1451 N N   . ILE B 1 40  ? 10.321  10.410  22.770 1.00 6.50  ? 57  ILE B N   1 
ATOM   1452 C CA  . ILE B 1 40  ? 11.405  9.477   23.060 1.00 8.58  ? 57  ILE B CA  1 
ATOM   1453 C C   . ILE B 1 40  ? 10.771  8.100   23.233 1.00 7.27  ? 57  ILE B C   1 
ATOM   1454 O O   . ILE B 1 40  ? 10.148  7.826   24.257 1.00 8.19  ? 57  ILE B O   1 
ATOM   1455 C CB  . ILE B 1 40  ? 12.187  9.883   24.314 1.00 8.85  ? 57  ILE B CB  1 
ATOM   1456 C CG1 . ILE B 1 40  ? 12.690  11.324  24.236 1.00 10.79 ? 57  ILE B CG1 1 
ATOM   1457 C CG2 . ILE B 1 40  ? 13.378  8.937   24.518 1.00 9.36  ? 57  ILE B CG2 1 
ATOM   1458 C CD1 . ILE B 1 40  ? 13.250  11.883  25.577 1.00 9.77  ? 57  ILE B CD1 1 
ATOM   1459 N N   . ALA B 1 41  ? 10.955  7.227   22.249 1.00 9.78  ? 58  ALA B N   1 
ATOM   1460 C CA  . ALA B 1 41  ? 10.467  5.860   22.343 1.00 9.64  ? 58  ALA B CA  1 
ATOM   1461 C C   . ALA B 1 41  ? 11.509  4.893   22.898 1.00 9.95  ? 58  ALA B C   1 
ATOM   1462 O O   . ALA B 1 41  ? 11.144  3.840   23.423 1.00 9.79  ? 58  ALA B O   1 
ATOM   1463 C CB  . ALA B 1 41  ? 9.985   5.380   20.971 1.00 10.85 ? 58  ALA B CB  1 
ATOM   1464 N N   . ALA B 1 42  ? 12.794  5.211   22.790 1.00 8.58  ? 59  ALA B N   1 
ATOM   1465 C CA  . ALA B 1 42  ? 13.820  4.347   23.354 1.00 9.56  ? 59  ALA B CA  1 
ATOM   1466 C C   . ALA B 1 42  ? 15.057  5.196   23.573 1.00 9.12  ? 59  ALA B C   1 
ATOM   1467 O O   . ALA B 1 42  ? 15.278  6.178   22.861 1.00 8.21  ? 59  ALA B O   1 
ATOM   1468 C CB  . ALA B 1 42  ? 14.161  3.181   22.423 1.00 11.76 ? 59  ALA B CB  1 
ATOM   1469 N N   . MET B 1 43  ? 15.861  4.815   24.568 1.00 8.94  ? 60  MET B N   1 
ATOM   1470 C CA  . MET B 1 43  ? 17.080  5.549   24.878 1.00 8.97  ? 60  MET B CA  1 
ATOM   1471 C C   . MET B 1 43  ? 17.975  4.642   25.709 1.00 8.44  ? 60  MET B C   1 
ATOM   1472 O O   . MET B 1 43  ? 17.517  4.010   26.669 1.00 9.95  ? 60  MET B O   1 
ATOM   1473 C CB  . MET B 1 43  ? 16.767  6.851   25.633 1.00 10.56 ? 60  MET B CB  1 
ATOM   1474 C CG  . MET B 1 43  ? 17.950  7.809   25.787 1.00 11.44 ? 60  MET B CG  1 
ATOM   1475 S SD  . MET B 1 43  ? 17.454  9.484   26.289 1.00 11.94 ? 60  MET B SD  1 
ATOM   1476 C CE  . MET B 1 43  ? 16.945  10.171  24.707 1.00 11.72 ? 60  MET B CE  1 
ATOM   1477 N N   . LYS B 1 44  ? 19.256  4.596   25.355 1.00 9.01  ? 61  LYS B N   1 
ATOM   1478 C CA  . LYS B 1 44  ? 20.210  3.725   26.027 1.00 10.84 ? 61  LYS B CA  1 
ATOM   1479 C C   . LYS B 1 44  ? 21.614  4.251   25.794 1.00 8.50  ? 61  LYS B C   1 
ATOM   1480 O O   . LYS B 1 44  ? 22.008  4.465   24.644 1.00 11.02 ? 61  LYS B O   1 
ATOM   1481 C CB  . LYS B 1 44  ? 20.103  2.300   25.457 1.00 13.49 ? 61  LYS B CB  1 
ATOM   1482 C CG  . LYS B 1 44  ? 21.252  1.388   25.812 1.00 19.50 ? 61  LYS B CG  1 
ATOM   1483 C CD  . LYS B 1 44  ? 20.954  -0.050  25.426 1.00 23.06 ? 61  LYS B CD  1 
ATOM   1484 C CE  . LYS B 1 44  ? 20.992  -0.263  23.935 1.00 22.62 ? 61  LYS B CE  1 
ATOM   1485 N NZ  . LYS B 1 44  ? 20.640  -1.683  23.615 1.00 24.86 ? 61  LYS B NZ  1 
ATOM   1486 N N   . LEU B 1 45  ? 22.364  4.460   26.874 1.00 7.34  ? 62  LEU B N   1 
ATOM   1487 C CA  . LEU B 1 45  ? 23.788  4.731   26.766 1.00 7.33  ? 62  LEU B CA  1 
ATOM   1488 C C   . LEU B 1 45  ? 24.549  3.412   26.706 1.00 8.81  ? 62  LEU B C   1 
ATOM   1489 O O   . LEU B 1 45  ? 24.335  2.503   27.524 1.00 9.43  ? 62  LEU B O   1 
ATOM   1490 C CB  . LEU B 1 45  ? 24.288  5.558   27.950 1.00 8.78  ? 62  LEU B CB  1 
ATOM   1491 C CG  . LEU B 1 45  ? 25.753  6.016   27.832 1.00 9.94  ? 62  LEU B CG  1 
ATOM   1492 C CD1 . LEU B 1 45  ? 25.882  7.257   26.972 1.00 11.50 ? 62  LEU B CD1 1 
ATOM   1493 C CD2 . LEU B 1 45  ? 26.388  6.221   29.198 1.00 10.17 ? 62  LEU B CD2 1 
ATOM   1494 N N   . THR B 1 46  ? 25.447  3.311   25.743 1.00 7.86  ? 63  THR B N   1 
ATOM   1495 C CA  . THR B 1 46  ? 26.317  2.159   25.650 1.00 8.58  ? 63  THR B CA  1 
ATOM   1496 C C   . THR B 1 46  ? 27.691  2.651   25.225 1.00 8.38  ? 63  THR B C   1 
ATOM   1497 O O   . THR B 1 46  ? 27.907  3.841   25.008 1.00 10.21 ? 63  THR B O   1 
ATOM   1498 C CB  . THR B 1 46  ? 25.737  1.105   24.704 1.00 12.49 ? 63  THR B CB  1 
ATOM   1499 O OG1 . THR B 1 46  ? 26.491  -0.099  24.847 1.00 12.68 ? 63  THR B OG1 1 
ATOM   1500 C CG2 . THR B 1 46  ? 25.801  1.549   23.259 1.00 13.08 ? 63  THR B CG2 1 
ATOM   1501 N N   . ILE B 1 47  ? 28.636  1.732   25.145 1.00 9.23  ? 64  ILE B N   1 
ATOM   1502 C CA  . ILE B 1 47  ? 29.921  1.981   24.500 1.00 9.00  ? 64  ILE B CA  1 
ATOM   1503 C C   . ILE B 1 47  ? 29.937  1.141   23.229 1.00 10.16 ? 64  ILE B C   1 
ATOM   1504 O O   . ILE B 1 47  ? 29.788  -0.090  23.274 1.00 10.30 ? 64  ILE B O   1 
ATOM   1505 C CB  . ILE B 1 47  ? 31.115  1.701   25.432 1.00 8.40  ? 64  ILE B CB  1 
ATOM   1506 C CG1 . ILE B 1 47  ? 31.212  2.791   26.512 1.00 10.72 ? 64  ILE B CG1 1 
ATOM   1507 C CG2 . ILE B 1 47  ? 32.440  1.618   24.639 1.00 10.23 ? 64  ILE B CG2 1 
ATOM   1508 C CD1 . ILE B 1 47  ? 32.187  2.481   27.623 1.00 12.68 ? 64  ILE B CD1 1 
ATOM   1509 N N   . ALA B 1 48  ? 30.060  1.813   22.092 1.00 10.63 ? 65  ALA B N   1 
ATOM   1510 C CA  . ALA B 1 48  ? 30.099  1.115   20.822 1.00 9.60  ? 65  ALA B CA  1 
ATOM   1511 C C   . ALA B 1 48  ? 31.425  0.388   20.686 1.00 8.89  ? 65  ALA B C   1 
ATOM   1512 O O   . ALA B 1 48  ? 32.480  0.927   21.025 1.00 9.91  ? 65  ALA B O   1 
ATOM   1513 C CB  . ALA B 1 48  ? 29.960  2.117   19.681 1.00 10.29 ? 65  ALA B CB  1 
ATOM   1514 N N   . THR B 1 49  ? 31.362  -0.847  20.198 1.00 9.94  ? 66  THR B N   1 
ATOM   1515 C CA  . THR B 1 49  ? 32.522  -1.691  19.987 1.00 11.23 ? 66  THR B CA  1 
ATOM   1516 C C   . THR B 1 49  ? 32.669  -1.969  18.499 1.00 10.07 ? 66  THR B C   1 
ATOM   1517 O O   . THR B 1 49  ? 31.698  -1.856  17.745 1.00 11.24 ? 66  THR B O   1 
ATOM   1518 C CB  . THR B 1 49  ? 32.328  -3.029  20.710 1.00 12.44 ? 66  THR B CB  1 
ATOM   1519 O OG1 . THR B 1 49  ? 31.212  -3.712  20.120 1.00 15.17 ? 66  THR B OG1 1 
ATOM   1520 C CG2 . THR B 1 49  ? 32.089  -2.833  22.200 1.00 14.04 ? 66  THR B CG2 1 
ATOM   1521 N N   . PRO B 1 50  ? 33.864  -2.377  18.047 1.00 13.55 ? 67  PRO B N   1 
ATOM   1522 C CA  . PRO B 1 50  ? 34.050  -2.646  16.612 1.00 12.08 ? 67  PRO B CA  1 
ATOM   1523 C C   . PRO B 1 50  ? 33.066  -3.638  16.018 1.00 12.32 ? 67  PRO B C   1 
ATOM   1524 O O   . PRO B 1 50  ? 32.602  -3.416  14.901 1.00 14.36 ? 67  PRO B O   1 
ATOM   1525 C CB  . PRO B 1 50  ? 35.498  -3.151  16.551 1.00 14.54 ? 67  PRO B CB  1 
ATOM   1526 C CG  . PRO B 1 50  ? 36.162  -2.431  17.644 1.00 15.14 ? 67  PRO B CG  1 
ATOM   1527 C CD  . PRO B 1 50  ? 35.148  -2.394  18.767 1.00 13.76 ? 67  PRO B CD  1 
ATOM   1528 N N   . ALA B 1 51  ? 32.723  -4.720  16.718 1.00 12.46 ? 68  ALA B N   1 
ATOM   1529 C CA  . ALA B 1 51  ? 31.837  -5.715  16.118 1.00 13.05 ? 68  ALA B CA  1 
ATOM   1530 C C   . ALA B 1 51  ? 30.469  -5.126  15.774 1.00 14.01 ? 68  ALA B C   1 
ATOM   1531 O O   . ALA B 1 51  ? 29.925  -5.378  14.692 1.00 15.42 ? 68  ALA B O   1 
ATOM   1532 C CB  . ALA B 1 51  ? 31.705  -6.920  17.044 1.00 12.57 ? 68  ALA B CB  1 
ATOM   1533 N N   . ILE B 1 52  ? 29.879  -4.360  16.691 1.00 11.14 ? 69  ILE B N   1 
ATOM   1534 C CA  . ILE B 1 52  ? 28.573  -3.781  16.388 1.00 10.91 ? 69  ILE B CA  1 
ATOM   1535 C C   . ILE B 1 52  ? 28.707  -2.648  15.380 1.00 11.10 ? 69  ILE B C   1 
ATOM   1536 O O   . ILE B 1 52  ? 27.851  -2.484  14.515 1.00 12.67 ? 69  ILE B O   1 
ATOM   1537 C CB  . ILE B 1 52  ? 27.822  -3.383  17.675 1.00 11.75 ? 69  ILE B CB  1 
ATOM   1538 C CG1 . ILE B 1 52  ? 26.323  -3.209  17.392 1.00 15.11 ? 69  ILE B CG1 1 
ATOM   1539 C CG2 . ILE B 1 52  ? 28.427  -2.109  18.286 1.00 14.59 ? 69  ILE B CG2 1 
ATOM   1540 C CD1 . ILE B 1 52  ? 25.474  -3.028  18.626 1.00 17.07 ? 69  ILE B CD1 1 
ATOM   1541 N N   . LEU B 1 53  ? 29.793  -1.881  15.441 1.00 9.85  ? 70  LEU B N   1 
ATOM   1542 C CA  . LEU B 1 53  ? 29.989  -0.811  14.469 1.00 13.25 ? 70  LEU B CA  1 
ATOM   1543 C C   . LEU B 1 53  ? 30.167  -1.353  13.057 1.00 12.44 ? 70  LEU B C   1 
ATOM   1544 O O   . LEU B 1 53  ? 29.705  -0.728  12.098 1.00 15.13 ? 70  LEU B O   1 
ATOM   1545 C CB  . LEU B 1 53  ? 31.186  0.029   14.875 1.00 12.60 ? 70  LEU B CB  1 
ATOM   1546 C CG  . LEU B 1 53  ? 30.962  0.888   16.116 1.00 11.79 ? 70  LEU B CG  1 
ATOM   1547 C CD1 . LEU B 1 53  ? 32.291  1.390   16.620 1.00 11.84 ? 70  LEU B CD1 1 
ATOM   1548 C CD2 . LEU B 1 53  ? 30.017  2.063   15.817 1.00 11.97 ? 70  LEU B CD2 1 
ATOM   1549 N N   . GLU B 1 54  ? 30.807  -2.518  12.905 1.00 16.97 ? 71  GLU B N   1 
ATOM   1550 C CA  . GLU B 1 54  ? 30.933  -3.117  11.579 1.00 19.22 ? 71  GLU B CA  1 
ATOM   1551 C C   . GLU B 1 54  ? 29.568  -3.469  10.999 1.00 17.41 ? 71  GLU B C   1 
ATOM   1552 O O   . GLU B 1 54  ? 29.362  -3.371  9.784  1.00 19.60 ? 71  GLU B O   1 
ATOM   1553 C CB  . GLU B 1 54  ? 31.838  -4.345  11.648 1.00 26.77 ? 71  GLU B CB  1 
ATOM   1554 C CG  . GLU B 1 54  ? 33.301  -4.008  11.826 1.00 33.23 ? 71  GLU B CG  1 
ATOM   1555 C CD  . GLU B 1 54  ? 34.113  -5.201  12.283 1.00 42.23 ? 71  GLU B CD  1 
ATOM   1556 O OE1 . GLU B 1 54  ? 33.696  -6.343  11.988 1.00 43.40 ? 71  GLU B OE1 1 
ATOM   1557 O OE2 . GLU B 1 54  ? 35.156  -4.998  12.949 1.00 47.47 ? 71  GLU B OE2 1 
ATOM   1558 N N   . GLU B 1 55  ? 28.631  -3.913  11.842 1.00 18.30 ? 72  GLU B N   1 
ATOM   1559 C CA  A GLU B 1 55  ? 27.271  -4.165  11.372 0.50 19.44 ? 72  GLU B CA  1 
ATOM   1560 C CA  B GLU B 1 55  ? 27.273  -4.167  11.366 0.50 17.84 ? 72  GLU B CA  1 
ATOM   1561 C C   . GLU B 1 55  ? 26.555  -2.863  11.032 1.00 18.39 ? 72  GLU B C   1 
ATOM   1562 O O   . GLU B 1 55  ? 25.861  -2.771  10.015 1.00 18.36 ? 72  GLU B O   1 
ATOM   1563 C CB  A GLU B 1 55  ? 26.476  -4.898  12.449 0.50 23.15 ? 72  GLU B CB  1 
ATOM   1564 C CB  B GLU B 1 55  ? 26.482  -4.936  12.423 0.50 17.92 ? 72  GLU B CB  1 
ATOM   1565 C CG  A GLU B 1 55  ? 27.123  -6.147  12.974 0.50 30.71 ? 72  GLU B CG  1 
ATOM   1566 C CG  B GLU B 1 55  ? 27.129  -6.220  12.888 0.50 24.01 ? 72  GLU B CG  1 
ATOM   1567 C CD  A GLU B 1 55  ? 26.464  -7.390  12.430 0.50 35.08 ? 72  GLU B CD  1 
ATOM   1568 C CD  B GLU B 1 55  ? 26.888  -7.371  11.938 0.50 24.55 ? 72  GLU B CD  1 
ATOM   1569 O OE1 A GLU B 1 55  ? 26.850  -7.842  11.329 0.50 38.22 ? 72  GLU B OE1 1 
ATOM   1570 O OE1 B GLU B 1 55  ? 26.083  -7.210  10.989 0.50 25.12 ? 72  GLU B OE1 1 
ATOM   1571 O OE2 A GLU B 1 55  ? 25.547  -7.900  13.103 0.50 36.30 ? 72  GLU B OE2 1 
ATOM   1572 O OE2 B GLU B 1 55  ? 27.496  -8.446  12.148 0.50 22.40 ? 72  GLU B OE2 1 
ATOM   1573 N N   . HIS B 1 56  ? 26.694  -1.849  11.889 1.00 15.10 ? 73  HIS B N   1 
ATOM   1574 C CA  . HIS B 1 56  ? 26.030  -0.578  11.643 1.00 15.88 ? 73  HIS B CA  1 
ATOM   1575 C C   . HIS B 1 56  ? 26.502  0.025   10.335 1.00 17.03 ? 73  HIS B C   1 
ATOM   1576 O O   . HIS B 1 56  ? 25.689  0.477   9.521  1.00 17.48 ? 73  HIS B O   1 
ATOM   1577 C CB  . HIS B 1 56  ? 26.339  0.360   12.799 1.00 14.74 ? 73  HIS B CB  1 
ATOM   1578 C CG  . HIS B 1 56  ? 25.736  1.718   12.642 1.00 14.19 ? 73  HIS B CG  1 
ATOM   1579 N ND1 . HIS B 1 56  ? 24.426  1.987   12.968 1.00 17.12 ? 73  HIS B ND1 1 
ATOM   1580 C CD2 . HIS B 1 56  ? 26.256  2.875   12.173 1.00 17.17 ? 73  HIS B CD2 1 
ATOM   1581 C CE1 . HIS B 1 56  ? 24.170  3.260   12.731 1.00 18.10 ? 73  HIS B CE1 1 
ATOM   1582 N NE2 . HIS B 1 56  ? 25.260  3.819   12.237 1.00 19.44 ? 73  HIS B NE2 1 
ATOM   1583 N N   . TYR B 1 57  ? 27.816  0.005   10.104 1.00 16.64 ? 74  TYR B N   1 
ATOM   1584 C CA  . TYR B 1 57  ? 28.445  0.551   8.910  1.00 18.94 ? 74  TYR B CA  1 
ATOM   1585 C C   . TYR B 1 57  ? 28.720  -0.528  7.875  1.00 19.56 ? 74  TYR B C   1 
ATOM   1586 O O   . TYR B 1 57  ? 29.727  -0.470  7.166  1.00 20.58 ? 74  TYR B O   1 
ATOM   1587 C CB  . TYR B 1 57  ? 29.737  1.281   9.282  1.00 20.07 ? 74  TYR B CB  1 
ATOM   1588 C CG  . TYR B 1 57  ? 29.493  2.540   10.069 1.00 20.31 ? 74  TYR B CG  1 
ATOM   1589 C CD1 . TYR B 1 57  ? 28.853  3.619   9.489  1.00 18.93 ? 74  TYR B CD1 1 
ATOM   1590 C CD2 . TYR B 1 57  ? 29.896  2.655   11.393 1.00 21.69 ? 74  TYR B CD2 1 
ATOM   1591 C CE1 . TYR B 1 57  ? 28.606  4.775   10.199 1.00 21.22 ? 74  TYR B CE1 1 
ATOM   1592 C CE2 . TYR B 1 57  ? 29.657  3.810   12.116 1.00 22.42 ? 74  TYR B CE2 1 
ATOM   1593 C CZ  . TYR B 1 57  ? 29.014  4.870   11.510 1.00 22.52 ? 74  TYR B CZ  1 
ATOM   1594 O OH  . TYR B 1 57  ? 28.769  6.032   12.209 1.00 21.44 ? 74  TYR B OH  1 
ATOM   1595 N N   . ALA B 1 58  ? 27.835  -1.522  7.781  1.00 20.72 ? 75  ALA B N   1 
ATOM   1596 C CA  . ALA B 1 58  ? 28.033  -2.613  6.834  1.00 25.14 ? 75  ALA B CA  1 
ATOM   1597 C C   . ALA B 1 58  ? 28.181  -2.093  5.413  1.00 27.12 ? 75  ALA B C   1 
ATOM   1598 O O   . ALA B 1 58  ? 28.926  -2.670  4.611  1.00 29.15 ? 75  ALA B O   1 
ATOM   1599 C CB  . ALA B 1 58  ? 26.842  -3.566  6.910  1.00 28.03 ? 75  ALA B CB  1 
ATOM   1600 N N   . GLU B 1 59  ? 27.476  -1.015  5.078  1.00 27.72 ? 76  GLU B N   1 
ATOM   1601 C CA  . GLU B 1 59  ? 27.533  -0.490  3.717  1.00 29.88 ? 76  GLU B CA  1 
ATOM   1602 C C   . GLU B 1 59  ? 28.948  -0.080  3.325  1.00 30.57 ? 76  GLU B C   1 
ATOM   1603 O O   . GLU B 1 59  ? 29.265  -0.036  2.127  1.00 31.52 ? 76  GLU B O   1 
ATOM   1604 C CB  . GLU B 1 59  ? 26.565  0.688   3.583  1.00 30.74 ? 76  GLU B CB  1 
ATOM   1605 C CG  . GLU B 1 59  ? 26.950  1.922   4.389  1.00 33.57 ? 76  GLU B CG  1 
ATOM   1606 C CD  . GLU B 1 59  ? 25.820  2.931   4.469  1.00 37.42 ? 76  GLU B CD  1 
ATOM   1607 O OE1 . GLU B 1 59  ? 25.705  3.781   3.556  1.00 40.02 ? 76  GLU B OE1 1 
ATOM   1608 O OE2 . GLU B 1 59  ? 25.034  2.859   5.438  1.00 38.08 ? 76  GLU B OE2 1 
ATOM   1609 N N   . HIS B 1 60  ? 29.806  0.209   4.303  1.00 29.98 ? 77  HIS B N   1 
ATOM   1610 C CA  . HIS B 1 60  ? 31.167  0.666   4.060  1.00 29.37 ? 77  HIS B CA  1 
ATOM   1611 C C   . HIS B 1 60  ? 32.207  -0.432  4.208  1.00 29.69 ? 77  HIS B C   1 
ATOM   1612 O O   . HIS B 1 60  ? 33.406  -0.131  4.213  1.00 28.75 ? 77  HIS B O   1 
ATOM   1613 C CB  . HIS B 1 60  ? 31.517  1.824   4.996  1.00 30.71 ? 77  HIS B CB  1 
ATOM   1614 C CG  . HIS B 1 60  ? 30.599  2.995   4.860  1.00 32.17 ? 77  HIS B CG  1 
ATOM   1615 N ND1 . HIS B 1 60  ? 30.243  3.522   3.637  1.00 33.49 ? 77  HIS B ND1 1 
ATOM   1616 C CD2 . HIS B 1 60  ? 29.950  3.732   5.792  1.00 35.12 ? 77  HIS B CD2 1 
ATOM   1617 C CE1 . HIS B 1 60  ? 29.418  4.538   3.822  1.00 35.10 ? 77  HIS B CE1 1 
ATOM   1618 N NE2 . HIS B 1 60  ? 29.225  4.687   5.120  1.00 35.99 ? 77  HIS B NE2 1 
ATOM   1619 N N   . LYS B 1 61  ? 31.783  -1.691  4.320  1.00 31.87 ? 78  LYS B N   1 
ATOM   1620 C CA  . LYS B 1 61  ? 32.723  -2.787  4.519  1.00 33.69 ? 78  LYS B CA  1 
ATOM   1621 C C   . LYS B 1 61  ? 33.802  -2.769  3.445  1.00 32.98 ? 78  LYS B C   1 
ATOM   1622 O O   . LYS B 1 61  ? 33.513  -2.637  2.252  1.00 34.33 ? 78  LYS B O   1 
ATOM   1623 C CB  . LYS B 1 61  ? 31.968  -4.119  4.482  1.00 37.27 ? 78  LYS B CB  1 
ATOM   1624 C CG  . LYS B 1 61  ? 32.856  -5.345  4.329  1.00 40.63 ? 78  LYS B CG  1 
ATOM   1625 C CD  . LYS B 1 61  ? 32.034  -6.628  4.316  1.00 42.27 ? 78  LYS B CD  1 
ATOM   1626 C CE  . LYS B 1 61  ? 32.420  -7.529  3.155  1.00 45.11 ? 78  LYS B CE  1 
ATOM   1627 N NZ  . LYS B 1 61  ? 31.492  -8.694  3.027  1.00 46.94 ? 78  LYS B NZ  1 
ATOM   1628 N N   . GLY B 1 62  ? 35.057  -2.883  3.879  1.00 33.19 ? 79  GLY B N   1 
ATOM   1629 C CA  . GLY B 1 62  ? 36.176  -2.960  2.970  1.00 34.66 ? 79  GLY B CA  1 
ATOM   1630 C C   . GLY B 1 62  ? 36.661  -1.636  2.431  1.00 36.18 ? 79  GLY B C   1 
ATOM   1631 O O   . GLY B 1 62  ? 37.707  -1.600  1.766  1.00 37.38 ? 79  GLY B O   1 
ATOM   1632 N N   . LYS B 1 63  ? 35.937  -0.552  2.670  1.00 35.71 ? 80  LYS B N   1 
ATOM   1633 C CA  . LYS B 1 63  ? 36.379  0.746   2.192  1.00 34.54 ? 80  LYS B CA  1 
ATOM   1634 C C   . LYS B 1 63  ? 37.549  1.238   3.040  1.00 35.37 ? 80  LYS B C   1 
ATOM   1635 O O   . LYS B 1 63  ? 37.583  1.003   4.253  1.00 34.98 ? 80  LYS B O   1 
ATOM   1636 C CB  . LYS B 1 63  ? 35.226  1.748   2.243  1.00 34.60 ? 80  LYS B CB  1 
ATOM   1637 C CG  . LYS B 1 63  ? 34.140  1.466   1.218  1.00 35.34 ? 80  LYS B CG  1 
ATOM   1638 C CD  . LYS B 1 63  ? 32.997  2.479   1.269  1.00 34.95 ? 80  LYS B CD  1 
ATOM   1639 C CE  . LYS B 1 63  ? 31.813  1.983   0.455  1.00 35.04 ? 80  LYS B CE  1 
ATOM   1640 N NZ  . LYS B 1 63  ? 30.558  2.755   0.707  1.00 35.18 ? 80  LYS B NZ  1 
ATOM   1641 N N   . PRO B 1 64  ? 38.523  1.921   2.438  1.00 36.41 ? 81  PRO B N   1 
ATOM   1642 C CA  . PRO B 1 64  ? 39.720  2.305   3.203  1.00 36.38 ? 81  PRO B CA  1 
ATOM   1643 C C   . PRO B 1 64  ? 39.448  3.252   4.366  1.00 34.40 ? 81  PRO B C   1 
ATOM   1644 O O   . PRO B 1 64  ? 40.227  3.254   5.327  1.00 32.74 ? 81  PRO B O   1 
ATOM   1645 C CB  . PRO B 1 64  ? 40.638  2.919   2.132  1.00 39.60 ? 81  PRO B CB  1 
ATOM   1646 C CG  . PRO B 1 64  ? 39.703  3.392   1.070  1.00 40.71 ? 81  PRO B CG  1 
ATOM   1647 C CD  . PRO B 1 64  ? 38.599  2.373   1.035  1.00 39.75 ? 81  PRO B CD  1 
ATOM   1648 N N   . PHE B 1 65  ? 38.381  4.058   4.319  1.00 33.01 ? 82  PHE B N   1 
ATOM   1649 C CA  . PHE B 1 65  ? 38.084  4.954   5.435  1.00 30.43 ? 82  PHE B CA  1 
ATOM   1650 C C   . PHE B 1 65  ? 37.475  4.231   6.629  1.00 28.72 ? 82  PHE B C   1 
ATOM   1651 O O   . PHE B 1 65  ? 37.394  4.820   7.714  1.00 27.65 ? 82  PHE B O   1 
ATOM   1652 C CB  . PHE B 1 65  ? 37.183  6.126   5.000  1.00 30.67 ? 82  PHE B CB  1 
ATOM   1653 C CG  . PHE B 1 65  ? 35.783  5.727   4.576  1.00 31.36 ? 82  PHE B CG  1 
ATOM   1654 C CD1 . PHE B 1 65  ? 34.842  5.332   5.510  1.00 29.63 ? 82  PHE B CD1 1 
ATOM   1655 C CD2 . PHE B 1 65  ? 35.404  5.791   3.239  1.00 32.28 ? 82  PHE B CD2 1 
ATOM   1656 C CE1 . PHE B 1 65  ? 33.554  4.977   5.121  1.00 29.15 ? 82  PHE B CE1 1 
ATOM   1657 C CE2 . PHE B 1 65  ? 34.117  5.440   2.847  1.00 32.48 ? 82  PHE B CE2 1 
ATOM   1658 C CZ  . PHE B 1 65  ? 33.195  5.036   3.790  1.00 30.55 ? 82  PHE B CZ  1 
ATOM   1659 N N   . LEU B 1 66  ? 37.050  2.981   6.458  1.00 26.34 ? 83  LEU B N   1 
ATOM   1660 C CA  . LEU B 1 66  ? 36.290  2.317   7.513  1.00 24.63 ? 83  LEU B CA  1 
ATOM   1661 C C   . LEU B 1 66  ? 37.079  2.154   8.801  1.00 24.35 ? 83  LEU B C   1 
ATOM   1662 O O   . LEU B 1 66  ? 36.519  2.435   9.870  1.00 21.17 ? 83  LEU B O   1 
ATOM   1663 C CB  . LEU B 1 66  ? 35.698  0.992   7.021  1.00 25.14 ? 83  LEU B CB  1 
ATOM   1664 C CG  . LEU B 1 66  ? 34.748  0.317   8.024  1.00 26.40 ? 83  LEU B CG  1 
ATOM   1665 C CD1 . LEU B 1 66  ? 33.572  1.229   8.378  1.00 27.23 ? 83  LEU B CD1 1 
ATOM   1666 C CD2 . LEU B 1 66  ? 34.243  -1.023  7.488  1.00 26.66 ? 83  LEU B CD2 1 
ATOM   1667 N N   . PRO B 1 67  ? 38.338  1.698   8.796  1.00 24.73 ? 84  PRO B N   1 
ATOM   1668 C CA  . PRO B 1 67  ? 39.018  1.481   10.088 1.00 27.24 ? 84  PRO B CA  1 
ATOM   1669 C C   . PRO B 1 67  ? 39.117  2.730   10.954 1.00 24.96 ? 84  PRO B C   1 
ATOM   1670 O O   . PRO B 1 67  ? 38.849  2.667   12.163 1.00 25.20 ? 84  PRO B O   1 
ATOM   1671 C CB  . PRO B 1 67  ? 40.393  0.936   9.671  1.00 28.30 ? 84  PRO B CB  1 
ATOM   1672 C CG  . PRO B 1 67  ? 40.156  0.331   8.331  1.00 28.80 ? 84  PRO B CG  1 
ATOM   1673 C CD  . PRO B 1 67  ? 39.167  1.240   7.664  1.00 27.85 ? 84  PRO B CD  1 
ATOM   1674 N N   . GLY B 1 68  ? 39.484  3.874   10.371 1.00 24.73 ? 85  GLY B N   1 
ATOM   1675 C CA  . GLY B 1 68  ? 39.533  5.105   11.144 1.00 22.24 ? 85  GLY B CA  1 
ATOM   1676 C C   . GLY B 1 68  ? 38.169  5.564   11.614 1.00 21.16 ? 85  GLY B C   1 
ATOM   1677 O O   . GLY B 1 68  ? 38.040  6.119   12.708 1.00 23.50 ? 85  GLY B O   1 
ATOM   1678 N N   . LEU B 1 69  ? 37.137  5.336   10.804 1.00 20.30 ? 86  LEU B N   1 
ATOM   1679 C CA  . LEU B 1 69  ? 35.772  5.630   11.228 1.00 19.63 ? 86  LEU B CA  1 
ATOM   1680 C C   . LEU B 1 69  ? 35.399  4.812   12.451 1.00 20.97 ? 86  LEU B C   1 
ATOM   1681 O O   . LEU B 1 69  ? 34.840  5.337   13.419 1.00 19.43 ? 86  LEU B O   1 
ATOM   1682 C CB  . LEU B 1 69  ? 34.813  5.324   10.078 1.00 19.63 ? 86  LEU B CB  1 
ATOM   1683 C CG  . LEU B 1 69  ? 33.317  5.269   10.383 1.00 23.97 ? 86  LEU B CG  1 
ATOM   1684 C CD1 . LEU B 1 69  ? 32.872  6.502   11.125 1.00 26.43 ? 86  LEU B CD1 1 
ATOM   1685 C CD2 . LEU B 1 69  ? 32.568  5.128   9.074  1.00 25.50 ? 86  LEU B CD2 1 
ATOM   1686 N N   . ILE B 1 70  ? 35.724  3.517   12.433 1.00 22.64 ? 87  ILE B N   1 
ATOM   1687 C CA  A ILE B 1 70  ? 35.377  2.659   13.560 0.75 21.19 ? 87  ILE B CA  1 
ATOM   1688 C CA  B ILE B 1 70  ? 35.389  2.647   13.556 0.25 22.10 ? 87  ILE B CA  1 
ATOM   1689 C C   . ILE B 1 70  ? 36.124  3.098   14.812 1.00 19.93 ? 87  ILE B C   1 
ATOM   1690 O O   . ILE B 1 70  ? 35.561  3.104   15.910 1.00 19.66 ? 87  ILE B O   1 
ATOM   1691 C CB  A ILE B 1 70  ? 35.617  1.180   13.206 0.75 24.29 ? 87  ILE B CB  1 
ATOM   1692 C CB  B ILE B 1 70  ? 35.697  1.180   13.202 0.25 24.16 ? 87  ILE B CB  1 
ATOM   1693 C CG1 A ILE B 1 70  ? 34.567  0.731   12.187 0.75 26.49 ? 87  ILE B CG1 1 
ATOM   1694 C CG1 B ILE B 1 70  ? 34.869  0.727   11.994 0.25 25.37 ? 87  ILE B CG1 1 
ATOM   1695 C CG2 A ILE B 1 70  ? 35.580  0.315   14.458 0.75 25.47 ? 87  ILE B CG2 1 
ATOM   1696 C CG2 B ILE B 1 70  ? 35.449  0.280   14.403 0.25 24.56 ? 87  ILE B CG2 1 
ATOM   1697 C CD1 A ILE B 1 70  ? 34.719  -0.695  11.733 0.75 27.42 ? 87  ILE B CD1 1 
ATOM   1698 C CD1 B ILE B 1 70  ? 33.383  0.867   12.171 0.25 26.12 ? 87  ILE B CD1 1 
ATOM   1699 N N   . GLU B 1 71  ? 37.395  3.483   14.666 1.00 19.80 ? 88  GLU B N   1 
ATOM   1700 C CA  . GLU B 1 71  ? 38.155  3.955   15.821 1.00 22.48 ? 88  GLU B CA  1 
ATOM   1701 C C   . GLU B 1 71  ? 37.514  5.194   16.434 1.00 20.22 ? 88  GLU B C   1 
ATOM   1702 O O   . GLU B 1 71  ? 37.373  5.285   17.660 1.00 18.17 ? 88  GLU B O   1 
ATOM   1703 C CB  . GLU B 1 71  ? 39.609  4.233   15.427 1.00 30.93 ? 88  GLU B CB  1 
ATOM   1704 C CG  . GLU B 1 71  ? 40.573  3.130   15.874 1.00 42.18 ? 88  GLU B CG  1 
ATOM   1705 C CD  . GLU B 1 71  ? 41.847  3.080   15.051 1.00 50.43 ? 88  GLU B CD  1 
ATOM   1706 O OE1 . GLU B 1 71  ? 42.549  4.114   14.977 1.00 53.26 ? 88  GLU B OE1 1 
ATOM   1707 O OE2 . GLU B 1 71  ? 42.143  2.009   14.471 1.00 52.46 ? 88  GLU B OE2 1 
ATOM   1708 N N   . LYS B 1 72  ? 37.090  6.150   15.601 1.00 16.90 ? 89  LYS B N   1 
ATOM   1709 C CA  A LYS B 1 72  ? 36.471  7.352   16.146 0.63 17.59 ? 89  LYS B CA  1 
ATOM   1710 C CA  B LYS B 1 72  ? 36.455  7.358   16.118 0.37 17.65 ? 89  LYS B CA  1 
ATOM   1711 C C   . LYS B 1 72  ? 35.130  7.053   16.798 1.00 15.70 ? 89  LYS B C   1 
ATOM   1712 O O   . LYS B 1 72  ? 34.738  7.753   17.736 1.00 14.34 ? 89  LYS B O   1 
ATOM   1713 C CB  A LYS B 1 72  ? 36.344  8.418   15.060 0.63 19.16 ? 89  LYS B CB  1 
ATOM   1714 C CB  B LYS B 1 72  ? 36.212  8.353   14.984 0.37 19.49 ? 89  LYS B CB  1 
ATOM   1715 C CG  A LYS B 1 72  ? 37.705  8.872   14.537 0.63 23.36 ? 89  LYS B CG  1 
ATOM   1716 C CG  B LYS B 1 72  ? 37.479  8.931   14.375 0.37 23.58 ? 89  LYS B CG  1 
ATOM   1717 C CD  A LYS B 1 72  ? 37.651  10.262  13.923 0.63 24.21 ? 89  LYS B CD  1 
ATOM   1718 C CD  B LYS B 1 72  ? 37.447  10.454  14.346 0.37 25.40 ? 89  LYS B CD  1 
ATOM   1719 C CE  A LYS B 1 72  ? 39.025  10.707  13.399 0.63 25.14 ? 89  LYS B CE  1 
ATOM   1720 C CE  B LYS B 1 72  ? 38.054  11.007  13.067 0.37 25.76 ? 89  LYS B CE  1 
ATOM   1721 N NZ  A LYS B 1 72  ? 40.116  10.602  14.424 0.63 21.89 ? 89  LYS B NZ  1 
ATOM   1722 N NZ  B LYS B 1 72  ? 37.097  10.937  11.940 0.37 26.31 ? 89  LYS B NZ  1 
ATOM   1723 N N   . MET B 1 73  ? 34.417  6.052   16.318 1.00 13.09 ? 90  MET B N   1 
ATOM   1724 C CA  . MET B 1 73  ? 33.126  5.686   16.874 1.00 12.47 ? 90  MET B CA  1 
ATOM   1725 C C   . MET B 1 73  ? 33.240  4.723   18.043 1.00 11.50 ? 90  MET B C   1 
ATOM   1726 O O   . MET B 1 73  ? 32.222  4.408   18.660 1.00 11.69 ? 90  MET B O   1 
ATOM   1727 C CB  . MET B 1 73  ? 32.225  5.090   15.787 1.00 12.23 ? 90  MET B CB  1 
ATOM   1728 C CG  . MET B 1 73  ? 31.684  6.119   14.826 1.00 13.67 ? 90  MET B CG  1 
ATOM   1729 S SD  . MET B 1 73  ? 30.477  7.224   15.598 1.00 13.39 ? 90  MET B SD  1 
ATOM   1730 C CE  . MET B 1 73  ? 29.198  6.062   16.064 1.00 14.74 ? 90  MET B CE  1 
ATOM   1731 N N   . THR B 1 74  ? 34.443  4.266   18.372 1.00 10.69 ? 91  THR B N   1 
ATOM   1732 C CA  . THR B 1 74  ? 34.625  3.343   19.494 1.00 10.56 ? 91  THR B CA  1 
ATOM   1733 C C   . THR B 1 74  ? 34.693  4.165   20.775 1.00 11.18 ? 91  THR B C   1 
ATOM   1734 O O   . THR B 1 74  ? 35.732  4.727   21.123 1.00 14.63 ? 91  THR B O   1 
ATOM   1735 C CB  . THR B 1 74  ? 35.866  2.474   19.302 1.00 14.64 ? 91  THR B CB  1 
ATOM   1736 O OG1 . THR B 1 74  ? 35.694  1.644   18.147 1.00 14.21 ? 91  THR B OG1 1 
ATOM   1737 C CG2 . THR B 1 74  ? 36.066  1.577   20.507 1.00 15.56 ? 91  THR B CG2 1 
ATOM   1738 N N   . GLY B 1 75  ? 33.577  4.241   21.477 1.00 10.28 ? 92  GLY B N   1 
ATOM   1739 C CA  . GLY B 1 75  ? 33.455  5.086   22.633 1.00 10.25 ? 92  GLY B CA  1 
ATOM   1740 C C   . GLY B 1 75  ? 32.003  5.159   23.036 1.00 9.01  ? 92  GLY B C   1 
ATOM   1741 O O   . GLY B 1 75  ? 31.145  4.503   22.441 1.00 9.29  ? 92  GLY B O   1 
ATOM   1742 N N   . PRO B 1 76  ? 31.697  5.973   24.045 1.00 8.98  ? 93  PRO B N   1 
ATOM   1743 C CA  . PRO B 1 76  ? 30.304  6.096   24.484 1.00 9.04  ? 93  PRO B CA  1 
ATOM   1744 C C   . PRO B 1 76  ? 29.445  6.684   23.374 1.00 9.22  ? 93  PRO B C   1 
ATOM   1745 O O   . PRO B 1 76  ? 29.854  7.612   22.674 1.00 8.82  ? 93  PRO B O   1 
ATOM   1746 C CB  . PRO B 1 76  ? 30.400  7.044   25.688 1.00 10.20 ? 93  PRO B CB  1 
ATOM   1747 C CG  . PRO B 1 76  ? 31.619  7.843   25.421 1.00 11.10 ? 93  PRO B CG  1 
ATOM   1748 C CD  . PRO B 1 76  ? 32.590  6.870   24.795 1.00 9.49  ? 93  PRO B CD  1 
ATOM   1749 N N   . VAL B 1 77  ? 28.234  6.143   23.241 1.00 8.01  ? 94  VAL B N   1 
ATOM   1750 C CA  . VAL B 1 77  ? 27.219  6.658   22.333 1.00 7.59  ? 94  VAL B CA  1 
ATOM   1751 C C   . VAL B 1 77  ? 25.879  6.599   23.057 1.00 7.63  ? 94  VAL B C   1 
ATOM   1752 O O   . VAL B 1 77  ? 25.661  5.752   23.930 1.00 8.53  ? 94  VAL B O   1 
ATOM   1753 C CB  . VAL B 1 77  ? 27.141  5.857   21.009 1.00 9.73  ? 94  VAL B CB  1 
ATOM   1754 C CG1 . VAL B 1 77  ? 28.474  5.917   20.247 1.00 8.22  ? 94  VAL B CG1 1 
ATOM   1755 C CG2 . VAL B 1 77  ? 26.704  4.401   21.266 1.00 10.73 ? 94  VAL B CG2 1 
ATOM   1756 N N   . LEU B 1 78  ? 24.963  7.502   22.686 1.00 6.62  ? 95  LEU B N   1 
ATOM   1757 C CA  . LEU B 1 78  ? 23.591  7.466   23.182 1.00 7.61  ? 95  LEU B CA  1 
ATOM   1758 C C   . LEU B 1 78  ? 22.709  6.994   22.032 1.00 7.83  ? 95  LEU B C   1 
ATOM   1759 O O   . LEU B 1 78  ? 22.521  7.709   21.044 1.00 8.70  ? 95  LEU B O   1 
ATOM   1760 C CB  . LEU B 1 78  ? 23.132  8.817   23.743 1.00 7.37  ? 95  LEU B CB  1 
ATOM   1761 C CG  . LEU B 1 78  ? 21.815  8.713   24.525 1.00 7.67  ? 95  LEU B CG  1 
ATOM   1762 C CD1 . LEU B 1 78  ? 21.946  7.903   25.828 1.00 10.43 ? 95  LEU B CD1 1 
ATOM   1763 C CD2 . LEU B 1 78  ? 21.207  10.074  24.812 1.00 8.11  ? 95  LEU B CD2 1 
ATOM   1764 N N   . CYS B 1 79  ? 22.183  5.784   22.168 1.00 7.26  ? 96  CYS B N   1 
ATOM   1765 C CA  . CYS B 1 79  ? 21.228  5.224   21.227 1.00 8.83  ? 96  CYS B CA  1 
ATOM   1766 C C   . CYS B 1 79  ? 19.844  5.778   21.545 1.00 7.22  ? 96  CYS B C   1 
ATOM   1767 O O   . CYS B 1 79  ? 19.421  5.796   22.710 1.00 8.24  ? 96  CYS B O   1 
ATOM   1768 C CB  . CYS B 1 79  ? 21.196  3.705   21.401 1.00 9.62  ? 96  CYS B CB  1 
ATOM   1769 S SG  . CYS B 1 79  ? 22.805  2.885   21.363 1.00 11.31 ? 96  CYS B SG  1 
ATOM   1770 N N   . MET B 1 80  ? 19.115  6.197   20.515 1.00 7.48  ? 97  MET B N   1 
ATOM   1771 C CA  . MET B 1 80  ? 17.810  6.814   20.720 1.00 7.67  ? 97  MET B CA  1 
ATOM   1772 C C   . MET B 1 80  ? 16.863  6.396   19.612 1.00 7.25  ? 97  MET B C   1 
ATOM   1773 O O   . MET B 1 80  ? 17.280  6.207   18.470 1.00 9.06  ? 97  MET B O   1 
ATOM   1774 C CB  . MET B 1 80  ? 17.921  8.360   20.702 1.00 8.99  ? 97  MET B CB  1 
ATOM   1775 C CG  . MET B 1 80  ? 19.045  8.923   21.563 1.00 9.37  ? 97  MET B CG  1 
ATOM   1776 S SD  . MET B 1 80  ? 19.138  10.740  21.613 1.00 9.50  ? 97  MET B SD  1 
ATOM   1777 C CE  . MET B 1 80  ? 19.551  11.134  19.914 1.00 10.07 ? 97  MET B CE  1 
ATOM   1778 N N   . VAL B 1 81  ? 15.580  6.280   19.951 1.00 7.34  ? 98  VAL B N   1 
ATOM   1779 C CA  . VAL B 1 81  ? 14.512  6.202   18.964 1.00 8.45  ? 98  VAL B CA  1 
ATOM   1780 C C   . VAL B 1 81  ? 13.541  7.335   19.243 1.00 7.67  ? 98  VAL B C   1 
ATOM   1781 O O   . VAL B 1 81  ? 13.014  7.450   20.354 1.00 8.23  ? 98  VAL B O   1 
ATOM   1782 C CB  . VAL B 1 81  ? 13.788  4.843   18.989 1.00 8.83  ? 98  VAL B CB  1 
ATOM   1783 C CG1 . VAL B 1 81  ? 12.646  4.813   17.982 1.00 9.08  ? 98  VAL B CG1 1 
ATOM   1784 C CG2 . VAL B 1 81  ? 14.773  3.737   18.674 1.00 10.13 ? 98  VAL B CG2 1 
ATOM   1785 N N   . PHE B 1 82  ? 13.284  8.145   18.229 1.00 8.91  ? 99  PHE B N   1 
ATOM   1786 C CA  . PHE B 1 82  ? 12.303  9.210   18.303 1.00 8.96  ? 99  PHE B CA  1 
ATOM   1787 C C   . PHE B 1 82  ? 11.169  8.939   17.329 1.00 7.43  ? 99  PHE B C   1 
ATOM   1788 O O   . PHE B 1 82  ? 11.369  8.397   16.237 1.00 8.48  ? 99  PHE B O   1 
ATOM   1789 C CB  . PHE B 1 82  ? 12.916  10.582  17.972 1.00 8.67  ? 99  PHE B CB  1 
ATOM   1790 C CG  . PHE B 1 82  ? 13.586  11.252  19.148 1.00 10.03 ? 99  PHE B CG  1 
ATOM   1791 C CD1 . PHE B 1 82  ? 12.849  12.050  20.003 1.00 10.47 ? 99  PHE B CD1 1 
ATOM   1792 C CD2 . PHE B 1 82  ? 14.942  11.099  19.391 1.00 12.91 ? 99  PHE B CD2 1 
ATOM   1793 C CE1 . PHE B 1 82  ? 13.438  12.686  21.087 1.00 11.30 ? 99  PHE B CE1 1 
ATOM   1794 C CE2 . PHE B 1 82  ? 15.547  11.727  20.490 1.00 11.08 ? 99  PHE B CE2 1 
ATOM   1795 C CZ  . PHE B 1 82  ? 14.790  12.520  21.338 1.00 11.32 ? 99  PHE B CZ  1 
ATOM   1796 N N   . GLU B 1 83  ? 9.972   9.336   17.742 1.00 7.70  ? 100 GLU B N   1 
ATOM   1797 C CA  . GLU B 1 83  ? 8.749   9.096   16.991 1.00 9.13  ? 100 GLU B CA  1 
ATOM   1798 C C   . GLU B 1 83  ? 8.087   10.422  16.640 1.00 8.57  ? 100 GLU B C   1 
ATOM   1799 O O   . GLU B 1 83  ? 7.961   11.310  17.489 1.00 8.21  ? 100 GLU B O   1 
ATOM   1800 C CB  . GLU B 1 83  ? 7.777   8.282   17.834 1.00 10.44 ? 100 GLU B CB  1 
ATOM   1801 C CG  . GLU B 1 83  ? 6.422   8.061   17.202 1.00 9.78  ? 100 GLU B CG  1 
ATOM   1802 C CD  . GLU B 1 83  ? 5.517   7.268   18.116 1.00 11.39 ? 100 GLU B CD  1 
ATOM   1803 O OE1 . GLU B 1 83  ? 5.563   6.017   18.076 1.00 13.31 ? 100 GLU B OE1 1 
ATOM   1804 O OE2 . GLU B 1 83  ? 4.782   7.889   18.913 1.00 13.64 ? 100 GLU B OE2 1 
ATOM   1805 N N   . GLY B 1 84  ? 7.605   10.523  15.407 1.00 9.15  ? 101 GLY B N   1 
ATOM   1806 C CA  . GLY B 1 84  ? 6.889   11.705  14.980 1.00 9.93  ? 101 GLY B CA  1 
ATOM   1807 C C   . GLY B 1 84  ? 6.471   11.572  13.537 1.00 8.65  ? 101 GLY B C   1 
ATOM   1808 O O   . GLY B 1 84  ? 6.799   10.601  12.853 1.00 8.99  ? 101 GLY B O   1 
ATOM   1809 N N   . VAL B 1 85  ? 5.701   12.565  13.091 1.00 7.96  ? 102 VAL B N   1 
ATOM   1810 C CA  . VAL B 1 85  ? 5.308   12.621  11.692 1.00 8.51  ? 102 VAL B CA  1 
ATOM   1811 C C   . VAL B 1 85  ? 6.551   12.822  10.841 1.00 7.11  ? 102 VAL B C   1 
ATOM   1812 O O   . VAL B 1 85  ? 7.315   13.777  11.038 1.00 8.00  ? 102 VAL B O   1 
ATOM   1813 C CB  . VAL B 1 85  ? 4.318   13.779  11.476 1.00 8.28  ? 102 VAL B CB  1 
ATOM   1814 C CG1 . VAL B 1 85  ? 4.054   13.968  9.963  1.00 10.62 ? 102 VAL B CG1 1 
ATOM   1815 C CG2 . VAL B 1 85  ? 3.050   13.558  12.284 1.00 12.93 ? 102 VAL B CG2 1 
ATOM   1816 N N   . ASP B 1 86  ? 6.736   11.955  9.850  1.00 8.74  ? 103 ASP B N   1 
ATOM   1817 C CA  . ASP B 1 86  ? 7.815   12.127  8.881  1.00 10.61 ? 103 ASP B CA  1 
ATOM   1818 C C   . ASP B 1 86  ? 9.179   12.217  9.575  1.00 8.67  ? 103 ASP B C   1 
ATOM   1819 O O   . ASP B 1 86  ? 10.104  12.849  9.065  1.00 9.07  ? 103 ASP B O   1 
ATOM   1820 C CB  . ASP B 1 86  ? 7.535   13.374  8.024  1.00 10.67 ? 103 ASP B CB  1 
ATOM   1821 C CG  . ASP B 1 86  ? 8.423   13.485  6.787  1.00 13.20 ? 103 ASP B CG  1 
ATOM   1822 O OD1 . ASP B 1 86  ? 8.709   12.470  6.123  1.00 11.15 ? 103 ASP B OD1 1 
ATOM   1823 O OD2 . ASP B 1 86  ? 8.785   14.627  6.440  1.00 12.81 ? 103 ASP B OD2 1 
ATOM   1824 N N   . VAL B 1 87  ? 9.346   11.565  10.733 1.00 8.76  ? 104 VAL B N   1 
ATOM   1825 C CA  . VAL B 1 87  ? 10.496  11.889  11.581 1.00 7.71  ? 104 VAL B CA  1 
ATOM   1826 C C   . VAL B 1 87  ? 11.807  11.410  10.970 1.00 7.93  ? 104 VAL B C   1 
ATOM   1827 O O   . VAL B 1 87  ? 12.873  11.941  11.292 1.00 8.27  ? 104 VAL B O   1 
ATOM   1828 C CB  . VAL B 1 87  ? 10.316  11.375  13.025 1.00 8.24  ? 104 VAL B CB  1 
ATOM   1829 C CG1 . VAL B 1 87  ? 10.470  9.842   13.101 1.00 10.16 ? 104 VAL B CG1 1 
ATOM   1830 C CG2 . VAL B 1 87  ? 11.304  12.053  13.977 1.00 9.44  ? 104 VAL B CG2 1 
ATOM   1831 N N   . ILE B 1 88  ? 11.779  10.375  10.133 1.00 7.93  ? 105 ILE B N   1 
ATOM   1832 C CA  . ILE B 1 88  ? 13.031  9.925   9.521  1.00 8.10  ? 105 ILE B CA  1 
ATOM   1833 C C   . ILE B 1 88  ? 13.635  11.039  8.674  1.00 9.40  ? 105 ILE B C   1 
ATOM   1834 O O   . ILE B 1 88  ? 14.768  11.479  8.906  1.00 8.53  ? 105 ILE B O   1 
ATOM   1835 C CB  . ILE B 1 88  ? 12.820  8.631   8.718  1.00 10.20 ? 105 ILE B CB  1 
ATOM   1836 C CG1 . ILE B 1 88  ? 12.417  7.483   9.647  1.00 10.55 ? 105 ILE B CG1 1 
ATOM   1837 C CG2 . ILE B 1 88  ? 14.090  8.272   7.981  1.00 13.83 ? 105 ILE B CG2 1 
ATOM   1838 C CD1 . ILE B 1 88  ? 11.808  6.297   8.907  1.00 10.89 ? 105 ILE B CD1 1 
ATOM   1839 N N   . ALA B 1 89  ? 12.857  11.559  7.722  1.00 8.82  ? 106 ALA B N   1 
ATOM   1840 C CA  . ALA B 1 89  ? 13.346  12.640  6.868  1.00 10.16 ? 106 ALA B CA  1 
ATOM   1841 C C   . ALA B 1 89  ? 13.547  13.930  7.659  1.00 9.65  ? 106 ALA B C   1 
ATOM   1842 O O   . ALA B 1 89  ? 14.494  14.680  7.403  1.00 9.56  ? 106 ALA B O   1 
ATOM   1843 C CB  . ALA B 1 89  ? 12.382  12.869  5.707  1.00 11.88 ? 106 ALA B CB  1 
ATOM   1844 N N   . GLN B 1 90  ? 12.664  14.215  8.616  1.00 7.93  ? 107 GLN B N   1 
ATOM   1845 C CA  . GLN B 1 90  ? 12.786  15.460  9.365  1.00 5.78  ? 107 GLN B CA  1 
ATOM   1846 C C   . GLN B 1 90  ? 14.034  15.474  10.242 1.00 6.71  ? 107 GLN B C   1 
ATOM   1847 O O   . GLN B 1 90  ? 14.702  16.501  10.357 1.00 6.57  ? 107 GLN B O   1 
ATOM   1848 C CB  . GLN B 1 90  ? 11.531  15.721  10.196 1.00 8.05  ? 107 GLN B CB  1 
ATOM   1849 C CG  . GLN B 1 90  ? 10.322  16.106  9.359  1.00 7.30  ? 107 GLN B CG  1 
ATOM   1850 C CD  . GLN B 1 90  ? 10.524  17.408  8.631  1.00 8.44  ? 107 GLN B CD  1 
ATOM   1851 O OE1 . GLN B 1 90  ? 10.794  18.454  9.238  1.00 8.39  ? 107 GLN B OE1 1 
ATOM   1852 N NE2 . GLN B 1 90  ? 10.414  17.357  7.318  1.00 9.47  ? 107 GLN B NE2 1 
ATOM   1853 N N   . ALA B 1 91  ? 14.355  14.357  10.888 1.00 7.75  ? 108 ALA B N   1 
ATOM   1854 C CA  . ALA B 1 91  ? 15.559  14.319  11.709 1.00 8.93  ? 108 ALA B CA  1 
ATOM   1855 C C   . ALA B 1 91  ? 16.799  14.514  10.854 1.00 7.84  ? 108 ALA B C   1 
ATOM   1856 O O   . ALA B 1 91  ? 17.747  15.177  11.279 1.00 7.99  ? 108 ALA B O   1 
ATOM   1857 C CB  . ALA B 1 91  ? 15.633  13.017  12.505 1.00 9.10  ? 108 ALA B CB  1 
ATOM   1858 N N   . ARG B 1 92  ? 16.812  13.938  9.643  1.00 8.10  ? 109 ARG B N   1 
ATOM   1859 C CA  . ARG B 1 92  ? 17.937  14.155  8.731  1.00 8.75  ? 109 ARG B CA  1 
ATOM   1860 C C   . ARG B 1 92  ? 18.069  15.631  8.372  1.00 8.79  ? 109 ARG B C   1 
ATOM   1861 O O   . ARG B 1 92  ? 19.178  16.178  8.318  1.00 9.16  ? 109 ARG B O   1 
ATOM   1862 C CB  . ARG B 1 92  ? 17.774  13.306  7.461  1.00 11.06 ? 109 ARG B CB  1 
ATOM   1863 C CG  . ARG B 1 92  ? 17.850  11.802  7.715  1.00 12.16 ? 109 ARG B CG  1 
ATOM   1864 C CD  . ARG B 1 92  ? 19.292  11.323  7.917  1.00 12.01 ? 109 ARG B CD  1 
ATOM   1865 N NE  . ARG B 1 92  ? 20.110  11.383  6.707  1.00 13.00 ? 109 ARG B NE  1 
ATOM   1866 C CZ  . ARG B 1 92  ? 21.356  10.929  6.646  1.00 15.15 ? 109 ARG B CZ  1 
ATOM   1867 N NH1 . ARG B 1 92  ? 21.925  10.345  7.686  1.00 15.83 ? 109 ARG B NH1 1 
ATOM   1868 N NH2 . ARG B 1 92  ? 22.046  11.062  5.516  1.00 20.66 ? 109 ARG B NH2 1 
ATOM   1869 N N   . LYS B 1 93  ? 16.941  16.292  8.137  1.00 7.30  ? 110 LYS B N   1 
ATOM   1870 C CA  . LYS B 1 93  ? 16.961  17.717  7.834  1.00 7.52  ? 110 LYS B CA  1 
ATOM   1871 C C   . LYS B 1 93  ? 17.468  18.531  9.018  1.00 7.57  ? 110 LYS B C   1 
ATOM   1872 O O   . LYS B 1 93  ? 18.229  19.490  8.847  1.00 9.07  ? 110 LYS B O   1 
ATOM   1873 C CB  . LYS B 1 93  ? 15.547  18.138  7.456  1.00 9.42  ? 110 LYS B CB  1 
ATOM   1874 C CG  . LYS B 1 93  ? 15.392  19.580  7.101  1.00 9.33  ? 110 LYS B CG  1 
ATOM   1875 C CD  . LYS B 1 93  ? 13.977  19.881  6.646  1.00 9.88  ? 110 LYS B CD  1 
ATOM   1876 C CE  . LYS B 1 93  ? 13.796  21.366  6.404  1.00 11.00 ? 110 LYS B CE  1 
ATOM   1877 N NZ  . LYS B 1 93  ? 12.404  21.657  6.020  1.00 10.65 ? 110 LYS B NZ  1 
ATOM   1878 N N   . MET B 1 94  ? 17.072  18.147  10.232 1.00 7.64  ? 111 MET B N   1 
ATOM   1879 C CA  . MET B 1 94  ? 17.528  18.833  11.439 1.00 6.49  ? 111 MET B CA  1 
ATOM   1880 C C   . MET B 1 94  ? 19.012  18.620  11.687 1.00 7.63  ? 111 MET B C   1 
ATOM   1881 O O   . MET B 1 94  ? 19.681  19.499  12.235 1.00 8.35  ? 111 MET B O   1 
ATOM   1882 C CB  . MET B 1 94  ? 16.737  18.321  12.639 1.00 6.99  ? 111 MET B CB  1 
ATOM   1883 C CG  . MET B 1 94  ? 15.290  18.726  12.570 1.00 8.13  ? 111 MET B CG  1 
ATOM   1884 S SD  . MET B 1 94  ? 14.263  17.880  13.785 1.00 9.34  ? 111 MET B SD  1 
ATOM   1885 C CE  . MET B 1 94  ? 14.713  18.728  15.289 1.00 9.24  ? 111 MET B CE  1 
ATOM   1886 N N   . MET B 1 95  ? 19.528  17.436  11.363 1.00 6.92  ? 112 MET B N   1 
ATOM   1887 C CA  . MET B 1 95  ? 20.962  17.190  11.493 1.00 8.06  ? 112 MET B CA  1 
ATOM   1888 C C   . MET B 1 95  ? 21.759  18.063  10.540 1.00 7.65  ? 112 MET B C   1 
ATOM   1889 O O   . MET B 1 95  ? 22.823  18.587  10.899 1.00 8.45  ? 112 MET B O   1 
ATOM   1890 C CB  . MET B 1 95  ? 21.269  15.721  11.195 1.00 9.08  ? 112 MET B CB  1 
ATOM   1891 C CG  . MET B 1 95  ? 20.779  14.770  12.256 1.00 10.55 ? 112 MET B CG  1 
ATOM   1892 S SD  . MET B 1 95  ? 20.752  13.040  11.693 1.00 12.92 ? 112 MET B SD  1 
ATOM   1893 C CE  . MET B 1 95  ? 22.381  12.829  10.980 1.00 15.49 ? 112 MET B CE  1 
ATOM   1894 N N   . GLY B 1 96  ? 21.270  18.213  9.316  1.00 8.47  ? 113 GLY B N   1 
ATOM   1895 C CA  . GLY B 1 96  ? 22.012  18.894  8.278  1.00 9.50  ? 113 GLY B CA  1 
ATOM   1896 C C   . GLY B 1 96  ? 22.993  17.982  7.570  1.00 8.92  ? 113 GLY B C   1 
ATOM   1897 O O   . GLY B 1 96  ? 23.197  16.821  7.927  1.00 9.03  ? 113 GLY B O   1 
ATOM   1898 N N   . SER B 1 97  ? 23.650  18.556  6.563  1.00 9.65  ? 114 SER B N   1 
ATOM   1899 C CA  . SER B 1 97  ? 24.572  17.808  5.721  1.00 10.57 ? 114 SER B CA  1 
ATOM   1900 C C   . SER B 1 97  ? 25.653  17.118  6.543  1.00 9.74  ? 114 SER B C   1 
ATOM   1901 O O   . SER B 1 97  ? 26.085  17.614  7.586  1.00 9.03  ? 114 SER B O   1 
ATOM   1902 C CB  . SER B 1 97  ? 25.278  18.769  4.764  1.00 12.57 ? 114 SER B CB  1 
ATOM   1903 O OG  . SER B 1 97  ? 24.347  19.591  4.089  1.00 17.40 ? 114 SER B OG  1 
ATOM   1904 N N   . THR B 1 98  ? 26.113  15.971  6.024  1.00 11.47 ? 115 THR B N   1 
ATOM   1905 C CA  A THR B 1 98  ? 27.196  15.259  6.684  0.41 11.59 ? 115 THR B CA  1 
ATOM   1906 C CA  B THR B 1 98  ? 27.227  15.238  6.618  0.59 11.87 ? 115 THR B CA  1 
ATOM   1907 C C   . THR B 1 98  ? 28.418  16.153  6.850  1.00 9.76  ? 115 THR B C   1 
ATOM   1908 O O   . THR B 1 98  ? 29.110  16.061  7.869  1.00 12.00 ? 115 THR B O   1 
ATOM   1909 C CB  A THR B 1 98  ? 27.548  13.979  5.924  0.41 13.29 ? 115 THR B CB  1 
ATOM   1910 C CB  B THR B 1 98  ? 27.644  14.112  5.659  0.59 13.35 ? 115 THR B CB  1 
ATOM   1911 O OG1 A THR B 1 98  ? 28.532  13.231  6.661  0.41 13.28 ? 115 THR B OG1 1 
ATOM   1912 O OG1 B THR B 1 98  ? 26.628  13.104  5.620  0.59 15.43 ? 115 THR B OG1 1 
ATOM   1913 C CG2 A THR B 1 98  ? 28.082  14.309  4.542  0.41 15.45 ? 115 THR B CG2 1 
ATOM   1914 C CG2 B THR B 1 98  ? 28.972  13.476  6.074  0.59 14.55 ? 115 THR B CG2 1 
ATOM   1915 N N   . ARG B 1 99  ? 28.686  17.035  5.884  1.00 10.23 ? 116 ARG B N   1 
ATOM   1916 C CA  . ARG B 1 99  ? 29.782  17.985  5.997  1.00 10.65 ? 116 ARG B CA  1 
ATOM   1917 C C   . ARG B 1 99  ? 29.244  19.226  6.688  1.00 9.16  ? 116 ARG B C   1 
ATOM   1918 O O   . ARG B 1 99  ? 28.425  19.950  6.094  1.00 8.58  ? 116 ARG B O   1 
ATOM   1919 C CB  . ARG B 1 99  ? 30.310  18.347  4.616  1.00 14.52 ? 116 ARG B CB  1 
ATOM   1920 C CG  . ARG B 1 99  ? 31.208  17.290  3.991  1.00 17.70 ? 116 ARG B CG  1 
ATOM   1921 C CD  . ARG B 1 99  ? 31.205  17.380  2.468  1.00 24.33 ? 116 ARG B CD  1 
ATOM   1922 N NE  . ARG B 1 99  ? 30.002  16.720  1.983  1.00 35.77 ? 116 ARG B NE  1 
ATOM   1923 C CZ  . ARG B 1 99  ? 29.843  15.401  1.946  1.00 43.39 ? 116 ARG B CZ  1 
ATOM   1924 N NH1 . ARG B 1 99  ? 30.851  14.571  2.181  1.00 46.57 ? 116 ARG B NH1 1 
ATOM   1925 N NH2 . ARG B 1 99  ? 28.641  14.899  1.674  1.00 42.74 ? 116 ARG B NH2 1 
ATOM   1926 N N   . PRO B 1 100 ? 29.673  19.529  7.912  1.00 10.57 ? 117 PRO B N   1 
ATOM   1927 C CA  . PRO B 1 100 ? 29.087  20.681  8.619  1.00 7.82  ? 117 PRO B CA  1 
ATOM   1928 C C   . PRO B 1 100 ? 29.222  22.002  7.878  1.00 9.29  ? 117 PRO B C   1 
ATOM   1929 O O   . PRO B 1 100 ? 28.349  22.869  8.022  1.00 8.28  ? 117 PRO B O   1 
ATOM   1930 C CB  . PRO B 1 100 ? 29.850  20.686  9.952  1.00 9.60  ? 117 PRO B CB  1 
ATOM   1931 C CG  . PRO B 1 100 ? 30.196  19.223  10.165 1.00 8.36  ? 117 PRO B CG  1 
ATOM   1932 C CD  . PRO B 1 100 ? 30.533  18.720  8.789  1.00 8.14  ? 117 PRO B CD  1 
ATOM   1933 N N   . GLY B 1 101 ? 30.294  22.185  7.097  1.00 9.10  ? 118 GLY B N   1 
ATOM   1934 C CA  . GLY B 1 101 ? 30.470  23.423  6.358  1.00 9.75  ? 118 GLY B CA  1 
ATOM   1935 C C   . GLY B 1 101 ? 29.430  23.640  5.282  1.00 10.09 ? 118 GLY B C   1 
ATOM   1936 O O   . GLY B 1 101 ? 29.255  24.772  4.828  1.00 11.93 ? 118 GLY B O   1 
ATOM   1937 N N   . GLU B 1 102 ? 28.762  22.573  4.844  1.00 8.97  ? 119 GLU B N   1 
ATOM   1938 C CA  . GLU B 1 102 ? 27.703  22.654  3.851  1.00 9.74  ? 119 GLU B CA  1 
ATOM   1939 C C   . GLU B 1 102 ? 26.317  22.639  4.473  1.00 9.87  ? 119 GLU B C   1 
ATOM   1940 O O   . GLU B 1 102 ? 25.336  22.897  3.768  1.00 11.21 ? 119 GLU B O   1 
ATOM   1941 C CB  . GLU B 1 102 ? 27.790  21.466  2.897  1.00 11.95 ? 119 GLU B CB  1 
ATOM   1942 C CG  . GLU B 1 102 ? 29.137  21.320  2.234  1.00 17.74 ? 119 GLU B CG  1 
ATOM   1943 C CD  . GLU B 1 102 ? 29.525  22.545  1.445  1.00 30.86 ? 119 GLU B CD  1 
ATOM   1944 O OE1 . GLU B 1 102 ? 28.765  22.922  0.531  1.00 36.32 ? 119 GLU B OE1 1 
ATOM   1945 O OE2 . GLU B 1 102 ? 30.584  23.137  1.754  1.00 36.98 ? 119 GLU B OE2 1 
ATOM   1946 N N   . ALA B 1 103 ? 26.220  22.330  5.762  1.00 9.83  ? 120 ALA B N   1 
ATOM   1947 C CA  . ALA B 1 103 ? 24.936  22.212  6.420  1.00 9.24  ? 120 ALA B CA  1 
ATOM   1948 C C   . ALA B 1 103 ? 24.284  23.582  6.580  1.00 9.61  ? 120 ALA B C   1 
ATOM   1949 O O   . ALA B 1 103 ? 24.954  24.610  6.732  1.00 11.05 ? 120 ALA B O   1 
ATOM   1950 C CB  . ALA B 1 103 ? 25.105  21.533  7.782  1.00 10.31 ? 120 ALA B CB  1 
ATOM   1951 N N   . ALA B 1 104 ? 22.954  23.583  6.534  1.00 10.81 ? 121 ALA B N   1 
ATOM   1952 C CA  . ALA B 1 104 ? 22.219  24.830  6.584  1.00 14.30 ? 121 ALA B CA  1 
ATOM   1953 C C   . ALA B 1 104 ? 22.297  25.440  7.979  1.00 10.31 ? 121 ALA B C   1 
ATOM   1954 O O   . ALA B 1 104 ? 22.303  24.726  8.984  1.00 11.28 ? 121 ALA B O   1 
ATOM   1955 C CB  . ALA B 1 104 ? 20.762  24.583  6.226  1.00 13.65 ? 121 ALA B CB  1 
ATOM   1956 N N   . PRO B 1 105 ? 22.314  26.762  8.082  1.00 14.92 ? 122 PRO B N   1 
ATOM   1957 C CA  . PRO B 1 105 ? 22.289  27.367  9.416  1.00 14.70 ? 122 PRO B CA  1 
ATOM   1958 C C   . PRO B 1 105 ? 21.058  26.883  10.173 1.00 12.04 ? 122 PRO B C   1 
ATOM   1959 O O   . PRO B 1 105 ? 19.988  26.686  9.594  1.00 14.44 ? 122 PRO B O   1 
ATOM   1960 C CB  . PRO B 1 105 ? 22.231  28.873  9.132  1.00 20.34 ? 122 PRO B CB  1 
ATOM   1961 C CG  . PRO B 1 105 ? 22.749  29.035  7.742  1.00 22.31 ? 122 PRO B CG  1 
ATOM   1962 C CD  . PRO B 1 105 ? 22.410  27.765  7.005  1.00 20.86 ? 122 PRO B CD  1 
ATOM   1963 N N   . GLY B 1 106 ? 21.226  26.670  11.475 1.00 12.83 ? 123 GLY B N   1 
ATOM   1964 C CA  . GLY B 1 106 ? 20.159  26.182  12.309 1.00 13.19 ? 123 GLY B CA  1 
ATOM   1965 C C   . GLY B 1 106 ? 20.085  24.675  12.421 1.00 10.44 ? 123 GLY B C   1 
ATOM   1966 O O   . GLY B 1 106 ? 19.278  24.170  13.201 1.00 13.69 ? 123 GLY B O   1 
ATOM   1967 N N   . THR B 1 107 ? 20.879  23.945  11.650 1.00 8.92  ? 124 THR B N   1 
ATOM   1968 C CA  . THR B 1 107 ? 20.962  22.503  11.807 1.00 8.09  ? 124 THR B CA  1 
ATOM   1969 C C   . THR B 1 107 ? 22.005  22.165  12.866 1.00 6.77  ? 124 THR B C   1 
ATOM   1970 O O   . THR B 1 107 ? 22.838  22.991  13.235 1.00 9.00  ? 124 THR B O   1 
ATOM   1971 C CB  . THR B 1 107 ? 21.313  21.815  10.481 1.00 9.34  ? 124 THR B CB  1 
ATOM   1972 O OG1 . THR B 1 107 ? 22.631  22.204  10.035 1.00 8.09  ? 124 THR B OG1 1 
ATOM   1973 C CG2 . THR B 1 107 ? 20.258  22.120  9.428  1.00 10.85 ? 124 THR B CG2 1 
ATOM   1974 N N   . ILE B 1 108 ? 21.938  20.923  13.352 1.00 7.82  ? 125 ILE B N   1 
ATOM   1975 C CA  . ILE B 1 108 ? 22.859  20.486  14.392 1.00 7.73  ? 125 ILE B CA  1 
ATOM   1976 C C   . ILE B 1 108 ? 24.294  20.567  13.899 1.00 8.56  ? 125 ILE B C   1 
ATOM   1977 O O   . ILE B 1 108 ? 25.167  21.098  14.583 1.00 7.72  ? 125 ILE B O   1 
ATOM   1978 C CB  . ILE B 1 108 ? 22.505  19.068  14.867 1.00 7.79  ? 125 ILE B CB  1 
ATOM   1979 C CG1 . ILE B 1 108 ? 21.157  19.074  15.583 1.00 9.22  ? 125 ILE B CG1 1 
ATOM   1980 C CG2 . ILE B 1 108 ? 23.608  18.529  15.783 1.00 7.58  ? 125 ILE B CG2 1 
ATOM   1981 C CD1 . ILE B 1 108 ? 20.589  17.704  15.825 1.00 10.73 ? 125 ILE B CD1 1 
ATOM   1982 N N   . ARG B 1 109 ? 24.564  20.051  12.700 1.00 7.28  ? 126 ARG B N   1 
ATOM   1983 C CA  . ARG B 1 109 ? 25.948  20.011  12.246 1.00 8.15  ? 126 ARG B CA  1 
ATOM   1984 C C   . ARG B 1 109 ? 26.494  21.416  12.025 1.00 7.17  ? 126 ARG B C   1 
ATOM   1985 O O   . ARG B 1 109 ? 27.646  21.692  12.349 1.00 8.30  ? 126 ARG B O   1 
ATOM   1986 C CB  . ARG B 1 109 ? 26.070  19.187  10.967 1.00 9.63  ? 126 ARG B CB  1 
ATOM   1987 C CG  . ARG B 1 109 ? 26.498  17.734  11.125 1.00 14.94 ? 126 ARG B CG  1 
ATOM   1988 C CD  . ARG B 1 109 ? 25.326  16.836  11.311 1.00 14.62 ? 126 ARG B CD  1 
ATOM   1989 N NE  . ARG B 1 109 ? 25.654  15.409  11.347 1.00 9.89  ? 126 ARG B NE  1 
ATOM   1990 C CZ  . ARG B 1 109 ? 25.388  14.531  10.384 1.00 9.22  ? 126 ARG B CZ  1 
ATOM   1991 N NH1 . ARG B 1 109 ? 24.897  14.902  9.213  1.00 11.65 ? 126 ARG B NH1 1 
ATOM   1992 N NH2 . ARG B 1 109 ? 25.600  13.237  10.607 1.00 10.17 ? 126 ARG B NH2 1 
ATOM   1993 N N   . ALA B 1 110 ? 25.682  22.322  11.475 1.00 6.92  ? 127 ALA B N   1 
ATOM   1994 C CA  . ALA B 1 110 ? 26.148  23.684  11.232 1.00 7.81  ? 127 ALA B CA  1 
ATOM   1995 C C   . ALA B 1 110 ? 26.357  24.442  12.533 1.00 7.56  ? 127 ALA B C   1 
ATOM   1996 O O   . ALA B 1 110 ? 27.233  25.310  12.618 1.00 9.89  ? 127 ALA B O   1 
ATOM   1997 C CB  . ALA B 1 110 ? 25.120  24.444  10.393 1.00 10.37 ? 127 ALA B CB  1 
ATOM   1998 N N   . ASP B 1 111 ? 25.522  24.176  13.538 1.00 6.53  ? 128 ASP B N   1 
ATOM   1999 C CA  . ASP B 1 111 ? 25.583  24.916  14.790 1.00 7.06  ? 128 ASP B CA  1 
ATOM   2000 C C   . ASP B 1 111 ? 26.707  24.434  15.705 1.00 6.82  ? 128 ASP B C   1 
ATOM   2001 O O   . ASP B 1 111 ? 27.221  25.222  16.514 1.00 7.69  ? 128 ASP B O   1 
ATOM   2002 C CB  . ASP B 1 111 ? 24.246  24.803  15.518 1.00 9.06  ? 128 ASP B CB  1 
ATOM   2003 C CG  . ASP B 1 111 ? 23.131  25.675  14.901 1.00 10.24 ? 128 ASP B CG  1 
ATOM   2004 O OD1 . ASP B 1 111 ? 23.378  26.540  14.041 1.00 13.54 ? 128 ASP B OD1 1 
ATOM   2005 O OD2 . ASP B 1 111 ? 21.968  25.469  15.291 1.00 11.30 ? 128 ASP B OD2 1 
ATOM   2006 N N   . PHE B 1 112 ? 27.114  23.165  15.597 1.00 7.09  ? 129 PHE B N   1 
ATOM   2007 C CA  . PHE B 1 112 ? 28.027  22.569  16.558 1.00 7.16  ? 129 PHE B CA  1 
ATOM   2008 C C   . PHE B 1 112 ? 29.369  22.128  15.980 1.00 7.29  ? 129 PHE B C   1 
ATOM   2009 O O   . PHE B 1 112 ? 30.284  21.869  16.764 1.00 7.04  ? 129 PHE B O   1 
ATOM   2010 C CB  . PHE B 1 112 ? 27.410  21.300  17.179 1.00 7.91  ? 129 PHE B CB  1 
ATOM   2011 C CG  . PHE B 1 112 ? 26.307  21.536  18.168 1.00 7.78  ? 129 PHE B CG  1 
ATOM   2012 C CD1 . PHE B 1 112 ? 24.993  21.610  17.754 1.00 9.11  ? 129 PHE B CD1 1 
ATOM   2013 C CD2 . PHE B 1 112 ? 26.575  21.591  19.530 1.00 7.92  ? 129 PHE B CD2 1 
ATOM   2014 C CE1 . PHE B 1 112 ? 23.976  21.786  18.683 1.00 9.95  ? 129 PHE B CE1 1 
ATOM   2015 C CE2 . PHE B 1 112 ? 25.562  21.765  20.450 1.00 10.19 ? 129 PHE B CE2 1 
ATOM   2016 C CZ  . PHE B 1 112 ? 24.270  21.850  20.030 1.00 10.24 ? 129 PHE B CZ  1 
ATOM   2017 N N   . CYS B 1 113 ? 29.498  21.935  14.662 1.00 7.53  ? 130 CYS B N   1 
ATOM   2018 C CA  . CYS B 1 113 ? 30.592  21.113  14.144 1.00 7.91  ? 130 CYS B CA  1 
ATOM   2019 C C   . CYS B 1 113 ? 31.363  21.789  13.021 1.00 8.53  ? 130 CYS B C   1 
ATOM   2020 O O   . CYS B 1 113 ? 30.959  22.815  12.478 1.00 7.28  ? 130 CYS B O   1 
ATOM   2021 C CB  . CYS B 1 113 ? 30.079  19.742  13.679 1.00 7.14  ? 130 CYS B CB  1 
ATOM   2022 S SG  . CYS B 1 113 ? 29.326  18.778  15.011 1.00 9.30  ? 130 CYS B SG  1 
ATOM   2023 N N   . GLN B 1 114 ? 32.514  21.203  12.698 1.00 6.94  ? 131 GLN B N   1 
ATOM   2024 C CA  . GLN B 1 114 ? 33.394  21.697  11.645 1.00 7.88  ? 131 GLN B CA  1 
ATOM   2025 C C   . GLN B 1 114 ? 33.623  20.710  10.511 1.00 8.75  ? 131 GLN B C   1 
ATOM   2026 O O   . GLN B 1 114 ? 33.677  21.135  9.349  1.00 9.84  ? 131 GLN B O   1 
ATOM   2027 C CB  . GLN B 1 114 ? 34.759  22.111  12.235 1.00 7.15  ? 131 GLN B CB  1 
ATOM   2028 C CG  . GLN B 1 114 ? 34.660  23.308  13.189 1.00 8.01  ? 131 GLN B CG  1 
ATOM   2029 C CD  . GLN B 1 114 ? 36.014  23.772  13.676 1.00 8.58  ? 131 GLN B CD  1 
ATOM   2030 O OE1 . GLN B 1 114 ? 36.939  23.929  12.885 1.00 8.32  ? 131 GLN B OE1 1 
ATOM   2031 N NE2 . GLN B 1 114 ? 36.148  23.957  14.981 1.00 8.97  ? 131 GLN B NE2 1 
ATOM   2032 N N   . GLN B 1 115 ? 33.767  19.406  10.807 1.00 8.54  ? 132 GLN B N   1 
ATOM   2033 C CA  . GLN B 1 115 ? 34.178  18.410  9.828  1.00 10.07 ? 132 GLN B CA  1 
ATOM   2034 C C   . GLN B 1 115 ? 33.316  17.160  9.918  1.00 8.77  ? 132 GLN B C   1 
ATOM   2035 O O   . GLN B 1 115 ? 32.837  16.788  10.989 1.00 9.97  ? 132 GLN B O   1 
ATOM   2036 C CB  . GLN B 1 115 ? 35.655  18.024  10.027 1.00 12.45 ? 132 GLN B CB  1 
ATOM   2037 C CG  . GLN B 1 115 ? 36.601  19.205  9.912  1.00 13.99 ? 132 GLN B CG  1 
ATOM   2038 C CD  . GLN B 1 115 ? 38.046  18.790  9.804  1.00 15.75 ? 132 GLN B CD  1 
ATOM   2039 O OE1 . GLN B 1 115 ? 38.688  18.462  10.804 1.00 15.59 ? 132 GLN B OE1 1 
ATOM   2040 N NE2 . GLN B 1 115 ? 38.566  18.811  8.590  1.00 19.16 ? 132 GLN B NE2 1 
ATOM   2041 N N   . ALA B 1 116 ? 33.178  16.480  8.778  1.00 8.92  ? 133 ALA B N   1 
ATOM   2042 C CA  . ALA B 1 116 ? 32.339  15.286  8.719  1.00 9.62  ? 133 ALA B CA  1 
ATOM   2043 C C   . ALA B 1 116 ? 32.830  14.174  9.647  1.00 10.26 ? 133 ALA B C   1 
ATOM   2044 O O   . ALA B 1 116 ? 32.019  13.383  10.150 1.00 10.90 ? 133 ALA B O   1 
ATOM   2045 C CB  . ALA B 1 116 ? 32.289  14.770  7.281  1.00 11.75 ? 133 ALA B CB  1 
ATOM   2046 N N   . GLY B 1 117 ? 34.145  14.067  9.860  1.00 9.66  ? 134 GLY B N   1 
ATOM   2047 C CA  . GLY B 1 117 ? 34.653  13.011  10.722 1.00 9.51  ? 134 GLY B CA  1 
ATOM   2048 C C   . GLY B 1 117 ? 34.312  13.183  12.187 1.00 9.56  ? 134 GLY B C   1 
ATOM   2049 O O   . GLY B 1 117 ? 34.497  12.238  12.961 1.00 11.43 ? 134 GLY B O   1 
ATOM   2050 N N   . ARG B 1 118 ? 33.875  14.379  12.601 1.00 10.40 ? 135 ARG B N   1 
ATOM   2051 C CA  . ARG B 1 118 ? 33.339  14.600  13.954 1.00 8.67  ? 135 ARG B CA  1 
ATOM   2052 C C   . ARG B 1 118 ? 32.065  15.441  13.794 1.00 7.91  ? 135 ARG B C   1 
ATOM   2053 O O   . ARG B 1 118 ? 32.072  16.655  14.018 1.00 9.42  ? 135 ARG B O   1 
ATOM   2054 C CB  . ARG B 1 118 ? 34.373  15.282  14.864 1.00 9.25  ? 135 ARG B CB  1 
ATOM   2055 C CG  . ARG B 1 118 ? 35.571  14.414  15.239 1.00 9.48  ? 135 ARG B CG  1 
ATOM   2056 C CD  . ARG B 1 118 ? 35.138  13.226  16.073 1.00 10.74 ? 135 ARG B CD  1 
ATOM   2057 N NE  . ARG B 1 118 ? 36.263  12.653  16.801 1.00 9.88  ? 135 ARG B NE  1 
ATOM   2058 C CZ  . ARG B 1 118 ? 36.206  11.527  17.498 1.00 11.52 ? 135 ARG B CZ  1 
ATOM   2059 N NH1 . ARG B 1 118 ? 35.088  10.834  17.596 1.00 12.86 ? 135 ARG B NH1 1 
ATOM   2060 N NH2 . ARG B 1 118 ? 37.294  11.103  18.132 1.00 12.96 ? 135 ARG B NH2 1 
ATOM   2061 N N   . ASN B 1 119 ? 30.953  14.786  13.455 1.00 7.59  ? 136 ASN B N   1 
ATOM   2062 C CA  . ASN B 1 119 ? 29.712  15.499  13.169 1.00 8.34  ? 136 ASN B CA  1 
ATOM   2063 C C   . ASN B 1 119 ? 28.559  15.119  14.098 1.00 7.25  ? 136 ASN B C   1 
ATOM   2064 O O   . ASN B 1 119 ? 27.386  15.248  13.738 1.00 8.36  ? 136 ASN B O   1 
ATOM   2065 C CB  . ASN B 1 119 ? 29.338  15.419  11.690 1.00 8.35  ? 136 ASN B CB  1 
ATOM   2066 C CG  . ASN B 1 119 ? 28.941  14.048  11.246 1.00 8.91  ? 136 ASN B CG  1 
ATOM   2067 O OD1 . ASN B 1 119 ? 28.801  13.113  12.038 1.00 12.14 ? 136 ASN B OD1 1 
ATOM   2068 N ND2 . ASN B 1 119 ? 28.738  13.920  9.951  1.00 9.99  ? 136 ASN B ND2 1 
ATOM   2069 N N   . LEU B 1 120 ? 28.903  14.654  15.290 1.00 7.12  ? 137 LEU B N   1 
ATOM   2070 C CA  . LEU B 1 120 ? 28.103  14.661  16.509 1.00 6.24  ? 137 LEU B CA  1 
ATOM   2071 C C   . LEU B 1 120 ? 26.971  13.645  16.596 1.00 6.49  ? 137 LEU B C   1 
ATOM   2072 O O   . LEU B 1 120 ? 26.687  13.141  17.693 1.00 7.78  ? 137 LEU B O   1 
ATOM   2073 C CB  . LEU B 1 120 ? 27.412  16.035  16.652 1.00 8.68  ? 137 LEU B CB  1 
ATOM   2074 C CG  . LEU B 1 120 ? 27.338  16.594  18.072 1.00 8.49  ? 137 LEU B CG  1 
ATOM   2075 C CD1 . LEU B 1 120 ? 28.722  17.028  18.516 1.00 9.04  ? 137 LEU B CD1 1 
ATOM   2076 C CD2 . LEU B 1 120 ? 26.341  17.752  18.112 1.00 8.18  ? 137 LEU B CD2 1 
ATOM   2077 N N   . ILE B 1 121 ? 26.401  13.236  15.470 1.00 7.45  ? 138 ILE B N   1 
ATOM   2078 C CA  . ILE B 1 121 ? 25.125  12.524  15.521 1.00 7.68  ? 138 ILE B CA  1 
ATOM   2079 C C   . ILE B 1 121 ? 24.921  11.747  14.236 1.00 7.84  ? 138 ILE B C   1 
ATOM   2080 O O   . ILE B 1 121 ? 25.305  12.187  13.155 1.00 9.32  ? 138 ILE B O   1 
ATOM   2081 C CB  . ILE B 1 121 ? 23.952  13.495  15.820 1.00 7.19  ? 138 ILE B CB  1 
ATOM   2082 C CG1 . ILE B 1 121 ? 22.638  12.740  15.986 1.00 10.28 ? 138 ILE B CG1 1 
ATOM   2083 C CG2 . ILE B 1 121 ? 23.807  14.573  14.710 1.00 8.94  ? 138 ILE B CG2 1 
ATOM   2084 C CD1 . ILE B 1 121 ? 21.490  13.587  16.513 1.00 10.36 ? 138 ILE B CD1 1 
ATOM   2085 N N   . HIS B 1 122 ? 24.335  10.569  14.384 1.00 8.00  ? 139 HIS B N   1 
ATOM   2086 C CA  . HIS B 1 122 ? 23.899  9.727   13.294 1.00 8.36  ? 139 HIS B CA  1 
ATOM   2087 C C   . HIS B 1 122 ? 22.377  9.677   13.282 1.00 8.12  ? 139 HIS B C   1 
ATOM   2088 O O   . HIS B 1 122 ? 21.742  9.625   14.341 1.00 7.88  ? 139 HIS B O   1 
ATOM   2089 C CB  . HIS B 1 122 ? 24.410  8.299   13.504 1.00 9.34  ? 139 HIS B CB  1 
ATOM   2090 C CG  . HIS B 1 122 ? 23.668  7.296   12.687 1.00 10.92 ? 139 HIS B CG  1 
ATOM   2091 N ND1 . HIS B 1 122 ? 24.080  6.916   11.431 1.00 12.51 ? 139 HIS B ND1 1 
ATOM   2092 C CD2 . HIS B 1 122 ? 22.502  6.649   12.916 1.00 10.18 ? 139 HIS B CD2 1 
ATOM   2093 C CE1 . HIS B 1 122 ? 23.209  6.060   10.929 1.00 12.95 ? 139 HIS B CE1 1 
ATOM   2094 N NE2 . HIS B 1 122 ? 22.233  5.896   11.804 1.00 11.92 ? 139 HIS B NE2 1 
ATOM   2095 N N   . GLY B 1 123 ? 21.798  9.666   12.085 1.00 8.14  ? 140 GLY B N   1 
ATOM   2096 C CA  . GLY B 1 123 ? 20.379  9.398   11.950 1.00 7.52  ? 140 GLY B CA  1 
ATOM   2097 C C   . GLY B 1 123 ? 20.069  8.516   10.756 1.00 7.13  ? 140 GLY B C   1 
ATOM   2098 O O   . GLY B 1 123 ? 20.704  8.633   9.704  1.00 8.69  ? 140 GLY B O   1 
ATOM   2099 N N   . SER B 1 124 ? 19.070  7.646   10.895 1.00 8.39  ? 141 SER B N   1 
ATOM   2100 C CA  . SER B 1 124 ? 18.682  6.756   9.808  1.00 8.91  ? 141 SER B CA  1 
ATOM   2101 C C   . SER B 1 124 ? 18.320  7.554   8.567  1.00 11.93 ? 141 SER B C   1 
ATOM   2102 O O   . SER B 1 124 ? 17.652  8.583   8.657  1.00 11.33 ? 141 SER B O   1 
ATOM   2103 C CB  . SER B 1 124 ? 17.451  5.933   10.211 1.00 11.73 ? 141 SER B CB  1 
ATOM   2104 O OG  . SER B 1 124 ? 17.645  5.260   11.430 1.00 11.83 ? 141 SER B OG  1 
ATOM   2105 N N   . ASP B 1 125 ? 18.736  7.063   7.397  1.00 13.56 ? 142 ASP B N   1 
ATOM   2106 C CA  . ASP B 1 125 ? 18.470  7.782   6.152  1.00 14.17 ? 142 ASP B CA  1 
ATOM   2107 C C   . ASP B 1 125 ? 17.242  7.292   5.383  1.00 14.62 ? 142 ASP B C   1 
ATOM   2108 O O   . ASP B 1 125 ? 16.916  7.870   4.341  1.00 16.32 ? 142 ASP B O   1 
ATOM   2109 C CB  . ASP B 1 125 ? 19.719  7.813   5.242  1.00 18.47 ? 142 ASP B CB  1 
ATOM   2110 C CG  . ASP B 1 125 ? 20.098  6.450   4.684  1.00 23.12 ? 142 ASP B CG  1 
ATOM   2111 O OD1 . ASP B 1 125 ? 19.428  5.454   4.992  1.00 19.20 ? 142 ASP B OD1 1 
ATOM   2112 O OD2 . ASP B 1 125 ? 21.086  6.375   3.915  1.00 28.39 ? 142 ASP B OD2 1 
ATOM   2113 N N   . SER B 1 126 ? 16.546  6.266   5.865  1.00 12.79 ? 143 SER B N   1 
ATOM   2114 C CA  . SER B 1 126 ? 15.415  5.712   5.138  1.00 15.33 ? 143 SER B CA  1 
ATOM   2115 C C   . SER B 1 126 ? 14.619  4.835   6.090  1.00 12.74 ? 143 SER B C   1 
ATOM   2116 O O   . SER B 1 126 ? 15.091  4.479   7.177  1.00 12.10 ? 143 SER B O   1 
ATOM   2117 C CB  . SER B 1 126 ? 15.870  4.873   3.941  1.00 16.02 ? 143 SER B CB  1 
ATOM   2118 O OG  . SER B 1 126 ? 16.578  3.727   4.388  1.00 16.36 ? 143 SER B OG  1 
ATOM   2119 N N   . ALA B 1 127 ? 13.401  4.479   5.664  1.00 14.79 ? 144 ALA B N   1 
ATOM   2120 C CA  . ALA B 1 127 ? 12.604  3.555   6.463  1.00 16.05 ? 144 ALA B CA  1 
ATOM   2121 C C   . ALA B 1 127 ? 13.318  2.217   6.617  1.00 14.65 ? 144 ALA B C   1 
ATOM   2122 O O   . ALA B 1 127 ? 13.312  1.617   7.700  1.00 15.26 ? 144 ALA B O   1 
ATOM   2123 C CB  . ALA B 1 127 ? 11.229  3.352   5.831  1.00 18.91 ? 144 ALA B CB  1 
ATOM   2124 N N   . GLU B 1 128 ? 13.936  1.732   5.539  1.00 16.64 ? 145 GLU B N   1 
ATOM   2125 C CA  . GLU B 1 128 ? 14.653  0.465   5.602  1.00 17.40 ? 145 GLU B CA  1 
ATOM   2126 C C   . GLU B 1 128 ? 15.810  0.539   6.591  1.00 15.83 ? 145 GLU B C   1 
ATOM   2127 O O   . GLU B 1 128 ? 16.010  -0.379  7.394  1.00 16.34 ? 145 GLU B O   1 
ATOM   2128 C CB  . GLU B 1 128 ? 15.146  0.097   4.203  1.00 20.15 ? 145 GLU B CB  1 
ATOM   2129 C CG  . GLU B 1 128 ? 15.873  -1.227  4.127  1.00 27.08 ? 145 GLU B CG  1 
ATOM   2130 C CD  . GLU B 1 128 ? 16.001  -1.765  2.706  1.00 37.81 ? 145 GLU B CD  1 
ATOM   2131 O OE1 . GLU B 1 128 ? 15.302  -1.272  1.788  1.00 41.02 ? 145 GLU B OE1 1 
ATOM   2132 O OE2 . GLU B 1 128 ? 16.812  -2.693  2.504  1.00 42.03 ? 145 GLU B OE2 1 
ATOM   2133 N N   . SER B 1 129 ? 16.576  1.631   6.561  1.00 14.11 ? 146 SER B N   1 
ATOM   2134 C CA  A SER B 1 129 ? 17.711  1.730   7.469  0.47 13.73 ? 146 SER B CA  1 
ATOM   2135 C CA  B SER B 1 129 ? 17.713  1.760   7.467  0.53 14.97 ? 146 SER B CA  1 
ATOM   2136 C C   . SER B 1 129 ? 17.254  1.939   8.906  1.00 13.40 ? 146 SER B C   1 
ATOM   2137 O O   . SER B 1 129 ? 17.897  1.443   9.835  1.00 13.00 ? 146 SER B O   1 
ATOM   2138 C CB  A SER B 1 129 ? 18.661  2.837   7.027  0.47 11.55 ? 146 SER B CB  1 
ATOM   2139 C CB  B SER B 1 129 ? 18.597  2.932   7.051  0.53 15.56 ? 146 SER B CB  1 
ATOM   2140 O OG  A SER B 1 129 ? 18.056  4.107   7.118  0.47 11.81 ? 146 SER B OG  1 
ATOM   2141 O OG  B SER B 1 129 ? 19.329  2.624   5.882  0.53 18.56 ? 146 SER B OG  1 
ATOM   2142 N N   . ALA B 1 130 ? 16.145  2.647   9.110  1.00 11.93 ? 147 ALA B N   1 
ATOM   2143 C CA  . ALA B 1 130 ? 15.637  2.835   10.464 1.00 11.92 ? 147 ALA B CA  1 
ATOM   2144 C C   . ALA B 1 130 ? 15.250  1.498   11.074 1.00 11.46 ? 147 ALA B C   1 
ATOM   2145 O O   . ALA B 1 130 ? 15.599  1.204   12.219 1.00 12.56 ? 147 ALA B O   1 
ATOM   2146 C CB  . ALA B 1 130 ? 14.441  3.784   10.455 1.00 12.32 ? 147 ALA B CB  1 
ATOM   2147 N N   . LYS B 1 131 ? 14.541  0.659   10.314 1.00 12.66 ? 148 LYS B N   1 
ATOM   2148 C CA  . LYS B 1 131 ? 14.170  -0.659  10.825 1.00 14.03 ? 148 LYS B CA  1 
ATOM   2149 C C   . LYS B 1 131 ? 15.413  -1.479  11.176 1.00 15.67 ? 148 LYS B C   1 
ATOM   2150 O O   . LYS B 1 131 ? 15.494  -2.091  12.251 1.00 15.23 ? 148 LYS B O   1 
ATOM   2151 C CB  . LYS B 1 131 ? 13.282  -1.373  9.799  1.00 18.97 ? 148 LYS B CB  1 
ATOM   2152 C CG  . LYS B 1 131 ? 12.732  -2.708  10.248 1.00 27.36 ? 148 LYS B CG  1 
ATOM   2153 C CD  . LYS B 1 131 ? 11.949  -3.384  9.124  1.00 36.64 ? 148 LYS B CD  1 
ATOM   2154 C CE  . LYS B 1 131 ? 11.676  -4.848  9.444  1.00 42.98 ? 148 LYS B CE  1 
ATOM   2155 N NZ  . LYS B 1 131 ? 12.751  -5.744  8.918  1.00 47.92 ? 148 LYS B NZ  1 
ATOM   2156 N N   . ARG B 1 132 ? 16.407  -1.482  10.288 1.00 13.82 ? 149 ARG B N   1 
ATOM   2157 C CA  . ARG B 1 132 ? 17.618  -2.270  10.512 1.00 13.98 ? 149 ARG B CA  1 
ATOM   2158 C C   . ARG B 1 132 ? 18.415  -1.746  11.708 1.00 12.71 ? 149 ARG B C   1 
ATOM   2159 O O   . ARG B 1 132 ? 18.927  -2.535  12.523 1.00 13.68 ? 149 ARG B O   1 
ATOM   2160 C CB  . ARG B 1 132 ? 18.464  -2.221  9.237  1.00 18.26 ? 149 ARG B CB  1 
ATOM   2161 C CG  . ARG B 1 132 ? 19.694  -3.111  9.245  1.00 20.21 ? 149 ARG B CG  1 
ATOM   2162 C CD  . ARG B 1 132 ? 20.527  -2.898  7.999  1.00 24.45 ? 149 ARG B CD  1 
ATOM   2163 N NE  . ARG B 1 132 ? 21.458  -1.796  8.177  1.00 32.22 ? 149 ARG B NE  1 
ATOM   2164 C CZ  . ARG B 1 132 ? 22.597  -1.887  8.854  1.00 35.80 ? 149 ARG B CZ  1 
ATOM   2165 N NH1 . ARG B 1 132 ? 22.997  -3.030  9.396  1.00 35.44 ? 149 ARG B NH1 1 
ATOM   2166 N NH2 . ARG B 1 132 ? 23.353  -0.804  8.994  1.00 38.73 ? 149 ARG B NH2 1 
ATOM   2167 N N   . GLU B 1 133 ? 18.531  -0.418  11.823 1.00 12.61 ? 150 GLU B N   1 
ATOM   2168 C CA  . GLU B 1 133 ? 19.359  0.179   12.868 1.00 11.91 ? 150 GLU B CA  1 
ATOM   2169 C C   . GLU B 1 133 ? 18.699  0.047   14.229 1.00 11.06 ? 150 GLU B C   1 
ATOM   2170 O O   . GLU B 1 133 ? 19.374  -0.250  15.222 1.00 14.08 ? 150 GLU B O   1 
ATOM   2171 C CB  . GLU B 1 133 ? 19.675  1.638   12.517 1.00 12.64 ? 150 GLU B CB  1 
ATOM   2172 C CG  . GLU B 1 133 ? 20.646  1.763   11.336 1.00 11.90 ? 150 GLU B CG  1 
ATOM   2173 C CD  . GLU B 1 133 ? 20.759  3.183   10.808 1.00 11.58 ? 150 GLU B CD  1 
ATOM   2174 O OE1 . GLU B 1 133 ? 20.113  4.100   11.369 1.00 12.65 ? 150 GLU B OE1 1 
ATOM   2175 O OE2 . GLU B 1 133 ? 21.487  3.378   9.812  1.00 14.32 ? 150 GLU B OE2 1 
ATOM   2176 N N   . ILE B 1 134 ? 17.379  0.244   14.293 1.00 12.05 ? 151 ILE B N   1 
ATOM   2177 C CA  . ILE B 1 134 ? 16.663  0.052   15.552 1.00 13.79 ? 151 ILE B CA  1 
ATOM   2178 C C   . ILE B 1 134 ? 16.835  -1.380  16.037 1.00 13.88 ? 151 ILE B C   1 
ATOM   2179 O O   . ILE B 1 134 ? 17.118  -1.621  17.217 1.00 15.56 ? 151 ILE B O   1 
ATOM   2180 C CB  . ILE B 1 134 ? 15.182  0.438   15.396 1.00 14.74 ? 151 ILE B CB  1 
ATOM   2181 C CG1 . ILE B 1 134 ? 15.055  1.950   15.168 1.00 11.92 ? 151 ILE B CG1 1 
ATOM   2182 C CG2 . ILE B 1 134 ? 14.387  -0.001  16.636 1.00 15.18 ? 151 ILE B CG2 1 
ATOM   2183 C CD1 . ILE B 1 134 ? 13.658  2.421   14.861 1.00 12.65 ? 151 ILE B CD1 1 
ATOM   2184 N N   . SER B 1 135 ? 16.731  -2.348  15.123 1.00 14.01 ? 152 SER B N   1 
ATOM   2185 C CA  . SER B 1 135 ? 16.889  -3.748  15.502 1.00 16.59 ? 152 SER B CA  1 
ATOM   2186 C C   . SER B 1 135 ? 18.311  -4.035  15.963 1.00 15.06 ? 152 SER B C   1 
ATOM   2187 O O   . SER B 1 135 ? 18.524  -4.860  16.862 1.00 18.89 ? 152 SER B O   1 
ATOM   2188 C CB  . SER B 1 135 ? 16.528  -4.660  14.331 1.00 18.83 ? 152 SER B CB  1 
ATOM   2189 O OG  . SER B 1 135 ? 15.129  -4.686  14.126 1.00 20.33 ? 152 SER B OG  1 
ATOM   2190 N N   . LEU B 1 136 ? 19.297  -3.398  15.330 1.00 14.85 ? 153 LEU B N   1 
ATOM   2191 C CA  . LEU B 1 136 ? 20.690  -3.659  15.678 1.00 15.05 ? 153 LEU B CA  1 
ATOM   2192 C C   . LEU B 1 136 ? 21.012  -3.162  17.083 1.00 15.05 ? 153 LEU B C   1 
ATOM   2193 O O   . LEU B 1 136 ? 21.658  -3.864  17.871 1.00 15.57 ? 153 LEU B O   1 
ATOM   2194 C CB  . LEU B 1 136 ? 21.615  -2.989  14.661 1.00 17.10 ? 153 LEU B CB  1 
ATOM   2195 C CG  . LEU B 1 136 ? 23.111  -3.123  14.956 1.00 16.71 ? 153 LEU B CG  1 
ATOM   2196 C CD1 . LEU B 1 136 ? 23.503  -4.593  15.006 1.00 18.44 ? 153 LEU B CD1 1 
ATOM   2197 C CD2 . LEU B 1 136 ? 23.974  -2.384  13.946 1.00 17.33 ? 153 LEU B CD2 1 
ATOM   2198 N N   . TRP B 1 137 ? 20.582  -1.938  17.415 1.00 15.48 ? 154 TRP B N   1 
ATOM   2199 C CA  . TRP B 1 137 ? 21.031  -1.315  18.649 1.00 12.92 ? 154 TRP B CA  1 
ATOM   2200 C C   . TRP B 1 137 ? 20.105  -1.528  19.836 1.00 15.11 ? 154 TRP B C   1 
ATOM   2201 O O   . TRP B 1 137 ? 20.533  -1.302  20.973 1.00 17.43 ? 154 TRP B O   1 
ATOM   2202 C CB  . TRP B 1 137 ? 21.236  0.182   18.431 1.00 14.23 ? 154 TRP B CB  1 
ATOM   2203 C CG  . TRP B 1 137 ? 22.364  0.514   17.510 1.00 13.71 ? 154 TRP B CG  1 
ATOM   2204 C CD1 . TRP B 1 137 ? 22.277  0.731   16.172 1.00 13.66 ? 154 TRP B CD1 1 
ATOM   2205 C CD2 . TRP B 1 137 ? 23.746  0.693   17.858 1.00 13.99 ? 154 TRP B CD2 1 
ATOM   2206 N NE1 . TRP B 1 137 ? 23.515  1.038   15.658 1.00 14.23 ? 154 TRP B NE1 1 
ATOM   2207 C CE2 . TRP B 1 137 ? 24.436  1.014   16.674 1.00 14.14 ? 154 TRP B CE2 1 
ATOM   2208 C CE3 . TRP B 1 137 ? 24.467  0.611   19.056 1.00 15.08 ? 154 TRP B CE3 1 
ATOM   2209 C CZ2 . TRP B 1 137 ? 25.811  1.257   16.652 1.00 16.63 ? 154 TRP B CZ2 1 
ATOM   2210 C CZ3 . TRP B 1 137 ? 25.834  0.844   19.032 1.00 17.49 ? 154 TRP B CZ3 1 
ATOM   2211 C CH2 . TRP B 1 137 ? 26.491  1.161   17.841 1.00 16.52 ? 154 TRP B CH2 1 
ATOM   2212 N N   . PHE B 1 138 ? 18.857  -1.920  19.607 1.00 16.30 ? 155 PHE B N   1 
ATOM   2213 C CA  . PHE B 1 138 ? 17.878  -2.108  20.661 1.00 16.39 ? 155 PHE B CA  1 
ATOM   2214 C C   . PHE B 1 138 ? 17.232  -3.478  20.511 1.00 17.28 ? 155 PHE B C   1 
ATOM   2215 O O   . PHE B 1 138 ? 17.075  -3.983  19.395 1.00 18.20 ? 155 PHE B O   1 
ATOM   2216 C CB  . PHE B 1 138 ? 16.742  -1.068  20.573 1.00 14.38 ? 155 PHE B CB  1 
ATOM   2217 C CG  . PHE B 1 138 ? 17.117  0.312   21.045 1.00 13.32 ? 155 PHE B CG  1 
ATOM   2218 C CD1 . PHE B 1 138 ? 17.208  0.597   22.394 1.00 13.13 ? 155 PHE B CD1 1 
ATOM   2219 C CD2 . PHE B 1 138 ? 17.374  1.324   20.141 1.00 12.30 ? 155 PHE B CD2 1 
ATOM   2220 C CE1 . PHE B 1 138 ? 17.548  1.854   22.827 1.00 10.92 ? 155 PHE B CE1 1 
ATOM   2221 C CE2 . PHE B 1 138 ? 17.699  2.607   20.575 1.00 11.48 ? 155 PHE B CE2 1 
ATOM   2222 C CZ  . PHE B 1 138 ? 17.794  2.863   21.917 1.00 11.86 ? 155 PHE B CZ  1 
ATOM   2223 N N   . LYS B 1 139 ? 16.854  -4.068  21.639 1.00 19.59 ? 156 LYS B N   1 
ATOM   2224 C CA  . LYS B 1 139 ? 15.912  -5.168  21.575 1.00 23.99 ? 156 LYS B CA  1 
ATOM   2225 C C   . LYS B 1 139 ? 14.519  -4.587  21.341 1.00 22.77 ? 156 LYS B C   1 
ATOM   2226 O O   . LYS B 1 139 ? 14.244  -3.450  21.729 1.00 21.95 ? 156 LYS B O   1 
ATOM   2227 C CB  . LYS B 1 139 ? 15.909  -5.944  22.886 1.00 28.36 ? 156 LYS B CB  1 
ATOM   2228 C CG  . LYS B 1 139 ? 17.266  -6.439  23.326 1.00 36.46 ? 156 LYS B CG  1 
ATOM   2229 C CD  . LYS B 1 139 ? 17.154  -7.345  24.550 1.00 41.16 ? 156 LYS B CD  1 
ATOM   2230 C CE  . LYS B 1 139 ? 18.463  -7.383  25.322 1.00 44.22 ? 156 LYS B CE  1 
ATOM   2231 N NZ  . LYS B 1 139 ? 19.649  -7.521  24.415 1.00 46.02 ? 156 LYS B NZ  1 
ATOM   2232 N N   . PRO B 1 140 ? 13.618  -5.326  20.702 1.00 24.31 ? 157 PRO B N   1 
ATOM   2233 C CA  . PRO B 1 140 ? 12.270  -4.775  20.511 1.00 25.03 ? 157 PRO B CA  1 
ATOM   2234 C C   . PRO B 1 140 ? 11.626  -4.388  21.825 1.00 27.06 ? 157 PRO B C   1 
ATOM   2235 O O   . PRO B 1 140 ? 10.834  -3.441  21.866 1.00 29.00 ? 157 PRO B O   1 
ATOM   2236 C CB  . PRO B 1 140 ? 11.519  -5.902  19.787 1.00 27.53 ? 157 PRO B CB  1 
ATOM   2237 C CG  . PRO B 1 140 ? 12.343  -7.133  20.018 1.00 28.76 ? 157 PRO B CG  1 
ATOM   2238 C CD  . PRO B 1 140 ? 13.759  -6.659  20.094 1.00 25.53 ? 157 PRO B CD  1 
ATOM   2239 N N   . GLU B 1 141 ? 12.001  -5.072  22.909 1.00 26.93 ? 158 GLU B N   1 
ATOM   2240 C CA  . GLU B 1 141 ? 11.434  -4.811  24.223 1.00 28.91 ? 158 GLU B CA  1 
ATOM   2241 C C   . GLU B 1 141 ? 11.820  -3.444  24.763 1.00 27.82 ? 158 GLU B C   1 
ATOM   2242 O O   . GLU B 1 141 ? 11.122  -2.904  25.629 1.00 29.32 ? 158 GLU B O   1 
ATOM   2243 C CB  . GLU B 1 141 ? 11.950  -5.866  25.195 1.00 31.36 ? 158 GLU B CB  1 
ATOM   2244 N N   . GLU B 1 142 ? 12.945  -2.903  24.307 1.00 22.30 ? 159 GLU B N   1 
ATOM   2245 C CA  . GLU B 1 142 ? 13.445  -1.626  24.787 1.00 22.39 ? 159 GLU B CA  1 
ATOM   2246 C C   . GLU B 1 142 ? 12.734  -0.439  24.157 1.00 18.02 ? 159 GLU B C   1 
ATOM   2247 O O   . GLU B 1 142 ? 12.957  0.685   24.608 1.00 15.71 ? 159 GLU B O   1 
ATOM   2248 C CB  . GLU B 1 142 ? 14.962  -1.567  24.579 1.00 24.19 ? 159 GLU B CB  1 
ATOM   2249 C CG  . GLU B 1 142 ? 15.676  -2.694  25.335 1.00 27.42 ? 159 GLU B CG  1 
ATOM   2250 C CD  . GLU B 1 142 ? 17.177  -2.747  25.128 1.00 29.70 ? 159 GLU B CD  1 
ATOM   2251 O OE1 . GLU B 1 142 ? 17.648  -2.465  24.015 1.00 29.81 ? 159 GLU B OE1 1 
ATOM   2252 O OE2 . GLU B 1 142 ? 17.890  -3.103  26.089 1.00 33.71 ? 159 GLU B OE2 1 
ATOM   2253 N N   . ILE B 1 143 ? 11.874  -0.664  23.166 1.00 17.91 ? 160 ILE B N   1 
ATOM   2254 C CA  . ILE B 1 143 ? 11.033  0.378   22.587 1.00 17.66 ? 160 ILE B CA  1 
ATOM   2255 C C   . ILE B 1 143 ? 9.768   0.476   23.432 1.00 17.46 ? 160 ILE B C   1 
ATOM   2256 O O   . ILE B 1 143 ? 9.040   -0.508  23.586 1.00 18.46 ? 160 ILE B O   1 
ATOM   2257 C CB  . ILE B 1 143 ? 10.679  0.065   21.126 1.00 18.64 ? 160 ILE B CB  1 
ATOM   2258 C CG1 . ILE B 1 143 ? 11.903  -0.411  20.348 1.00 21.77 ? 160 ILE B CG1 1 
ATOM   2259 C CG2 . ILE B 1 143 ? 10.048  1.281   20.485 1.00 18.90 ? 160 ILE B CG2 1 
ATOM   2260 C CD1 . ILE B 1 143 ? 13.049  0.544   20.339 1.00 24.23 ? 160 ILE B CD1 1 
ATOM   2261 N N   . GLN B 1 144 ? 9.496   1.663   23.963 1.00 14.25 ? 161 GLN B N   1 
ATOM   2262 C CA  . GLN B 1 144 ? 8.437   1.866   24.943 1.00 13.33 ? 161 GLN B CA  1 
ATOM   2263 C C   . GLN B 1 144 ? 7.224   2.506   24.283 1.00 12.16 ? 161 GLN B C   1 
ATOM   2264 O O   . GLN B 1 144 ? 7.357   3.452   23.502 1.00 14.15 ? 161 GLN B O   1 
ATOM   2265 C CB  . GLN B 1 144 ? 8.927   2.793   26.061 1.00 13.74 ? 161 GLN B CB  1 
ATOM   2266 C CG  . GLN B 1 144 ? 10.273  2.398   26.667 1.00 14.92 ? 161 GLN B CG  1 
ATOM   2267 C CD  . GLN B 1 144 ? 10.223  1.058   27.336 1.00 14.60 ? 161 GLN B CD  1 
ATOM   2268 O OE1 . GLN B 1 144 ? 9.209   0.693   27.922 1.00 17.95 ? 161 GLN B OE1 1 
ATOM   2269 N NE2 . GLN B 1 144 ? 11.301  0.296   27.227 1.00 16.93 ? 161 GLN B NE2 1 
ATOM   2270 N N   . SER B 1 145 ? 6.040   2.014   24.638 1.00 13.24 ? 162 SER B N   1 
ATOM   2271 C CA  A SER B 1 145 ? 4.788   2.526   24.100 0.31 14.54 ? 162 SER B CA  1 
ATOM   2272 C CA  B SER B 1 145 ? 4.776   2.510   24.105 0.69 13.90 ? 162 SER B CA  1 
ATOM   2273 C C   . SER B 1 145 ? 4.107   3.391   25.152 1.00 13.77 ? 162 SER B C   1 
ATOM   2274 O O   . SER B 1 145 ? 3.778   2.915   26.241 1.00 16.51 ? 162 SER B O   1 
ATOM   2275 C CB  A SER B 1 145 ? 3.864   1.382   23.688 0.31 17.10 ? 162 SER B CB  1 
ATOM   2276 C CB  B SER B 1 145 ? 3.836   1.347   23.777 0.69 16.22 ? 162 SER B CB  1 
ATOM   2277 O OG  A SER B 1 145 ? 2.756   1.889   22.965 0.31 17.87 ? 162 SER B OG  1 
ATOM   2278 O OG  B SER B 1 145 ? 4.387   0.455   22.830 0.69 16.76 ? 162 SER B OG  1 
ATOM   2279 N N   . TYR B 1 146 ? 3.903   4.655   24.820 1.00 9.82  ? 163 TYR B N   1 
ATOM   2280 C CA  . TYR B 1 146 ? 3.133   5.587   25.639 1.00 10.38 ? 163 TYR B CA  1 
ATOM   2281 C C   . TYR B 1 146 ? 2.773   6.770   24.750 1.00 10.87 ? 163 TYR B C   1 
ATOM   2282 O O   . TYR B 1 146 ? 3.364   6.968   23.688 1.00 13.30 ? 163 TYR B O   1 
ATOM   2283 C CB  . TYR B 1 146 ? 3.901   6.040   26.889 1.00 11.30 ? 163 TYR B CB  1 
ATOM   2284 C CG  . TYR B 1 146 ? 5.141   6.880   26.614 1.00 9.06  ? 163 TYR B CG  1 
ATOM   2285 C CD1 . TYR B 1 146 ? 6.382   6.283   26.393 1.00 11.20 ? 163 TYR B CD1 1 
ATOM   2286 C CD2 . TYR B 1 146 ? 5.075   8.262   26.591 1.00 10.41 ? 163 TYR B CD2 1 
ATOM   2287 C CE1 . TYR B 1 146 ? 7.523   7.046   26.143 1.00 9.56  ? 163 TYR B CE1 1 
ATOM   2288 C CE2 . TYR B 1 146 ? 6.220   9.036   26.339 1.00 9.32  ? 163 TYR B CE2 1 
ATOM   2289 C CZ  . TYR B 1 146 ? 7.423   8.422   26.118 1.00 7.76  ? 163 TYR B CZ  1 
ATOM   2290 O OH  . TYR B 1 146 ? 8.525   9.207   25.860 1.00 9.18  ? 163 TYR B OH  1 
ATOM   2291 N N   . LYS B 1 147 ? 1.794   7.553   25.189 1.00 10.92 ? 164 LYS B N   1 
ATOM   2292 C CA  . LYS B 1 147 ? 1.262   8.656   24.399 1.00 10.57 ? 164 LYS B CA  1 
ATOM   2293 C C   . LYS B 1 147 ? 1.614   9.988   25.047 1.00 11.86 ? 164 LYS B C   1 
ATOM   2294 O O   . LYS B 1 147 ? 1.461   10.151  26.259 1.00 13.06 ? 164 LYS B O   1 
ATOM   2295 C CB  . LYS B 1 147 ? -0.259  8.532   24.287 1.00 14.70 ? 164 LYS B CB  1 
ATOM   2296 C CG  . LYS B 1 147 ? -0.967  9.660   23.561 1.00 20.16 ? 164 LYS B CG  1 
ATOM   2297 C CD  . LYS B 1 147 ? -2.480  9.448   23.660 1.00 24.53 ? 164 LYS B CD  1 
ATOM   2298 C CE  . LYS B 1 147 ? -3.286  10.626  23.127 1.00 30.55 ? 164 LYS B CE  1 
ATOM   2299 N NZ  . LYS B 1 147 ? -3.920  10.299  21.830 1.00 34.36 ? 164 LYS B NZ  1 
ATOM   2300 N N   . LEU B 1 148 ? 2.071   10.938  24.237 1.00 11.80 ? 165 LEU B N   1 
ATOM   2301 C CA  . LEU B 1 148 ? 2.342   12.275  24.743 1.00 10.82 ? 165 LEU B CA  1 
ATOM   2302 C C   . LEU B 1 148 ? 1.038   12.980  25.093 1.00 10.60 ? 165 LEU B C   1 
ATOM   2303 O O   . LEU B 1 148 ? 0.116   13.043  24.277 1.00 10.55 ? 165 LEU B O   1 
ATOM   2304 C CB  . LEU B 1 148 ? 3.098   13.097  23.702 1.00 12.32 ? 165 LEU B CB  1 
ATOM   2305 C CG  . LEU B 1 148 ? 4.563   12.755  23.485 1.00 12.38 ? 165 LEU B CG  1 
ATOM   2306 C CD1 . LEU B 1 148 ? 5.131   13.653  22.380 1.00 12.14 ? 165 LEU B CD1 1 
ATOM   2307 C CD2 . LEU B 1 148 ? 5.349   12.910  24.767 1.00 12.93 ? 165 LEU B CD2 1 
ATOM   2308 N N   . ALA B 1 149 ? 0.987   13.547  26.302 1.00 11.80 ? 166 ALA B N   1 
ATOM   2309 C CA  . ALA B 1 149 ? -0.214  14.223  26.773 1.00 12.40 ? 166 ALA B CA  1 
ATOM   2310 C C   . ALA B 1 149 ? -0.570  15.448  25.938 1.00 11.99 ? 166 ALA B C   1 
ATOM   2311 O O   . ALA B 1 149 ? -1.744  15.837  25.892 1.00 13.72 ? 166 ALA B O   1 
ATOM   2312 C CB  . ALA B 1 149 ? -0.019  14.629  28.234 1.00 16.76 ? 166 ALA B CB  1 
ATOM   2313 N N   . LEU B 1 150 ? 0.408   16.077  25.286 1.00 11.58 ? 167 LEU B N   1 
ATOM   2314 C CA  . LEU B 1 150 ? 0.147   17.247  24.451 1.00 11.97 ? 167 LEU B CA  1 
ATOM   2315 C C   . LEU B 1 150 ? -0.197  16.881  23.007 1.00 10.89 ? 167 LEU B C   1 
ATOM   2316 O O   . LEU B 1 150 ? -0.222  17.771  22.156 1.00 10.12 ? 167 LEU B O   1 
ATOM   2317 C CB  . LEU B 1 150 ? 1.335   18.223  24.501 1.00 17.07 ? 167 LEU B CB  1 
ATOM   2318 C CG  . LEU B 1 150 ? 1.342   19.235  25.666 1.00 18.49 ? 167 LEU B CG  1 
ATOM   2319 C CD1 . LEU B 1 150 ? 2.668   19.979  25.761 1.00 19.71 ? 167 LEU B CD1 1 
ATOM   2320 C CD2 . LEU B 1 150 ? 0.193   20.228  25.545 1.00 22.84 ? 167 LEU B CD2 1 
ATOM   2321 N N   . SER B 1 151 ? -0.524  15.606  22.745 1.00 11.53 ? 168 SER B N   1 
ATOM   2322 C CA  A SER B 1 151 ? -0.772  15.146  21.381 0.40 12.25 ? 168 SER B CA  1 
ATOM   2323 C CA  B SER B 1 151 ? -0.778  15.144  21.380 0.60 11.82 ? 168 SER B CA  1 
ATOM   2324 C C   . SER B 1 151 ? -1.805  16.003  20.657 1.00 11.29 ? 168 SER B C   1 
ATOM   2325 O O   . SER B 1 151 ? -1.648  16.292  19.462 1.00 10.75 ? 168 SER B O   1 
ATOM   2326 C CB  A SER B 1 151 ? -1.221  13.681  21.419 0.40 13.04 ? 168 SER B CB  1 
ATOM   2327 C CB  B SER B 1 151 ? -1.257  13.686  21.389 0.60 12.06 ? 168 SER B CB  1 
ATOM   2328 O OG  A SER B 1 151 ? -1.726  13.265  20.167 0.40 13.28 ? 168 SER B OG  1 
ATOM   2329 O OG  B SER B 1 151 ? -0.171  12.781  21.505 0.60 10.88 ? 168 SER B OG  1 
ATOM   2330 N N   . ASP B 1 152 ? -2.873  16.404  21.353 1.00 11.95 ? 169 ASP B N   1 
ATOM   2331 C CA  . ASP B 1 152 ? -3.941  17.161  20.703 1.00 14.23 ? 169 ASP B CA  1 
ATOM   2332 C C   . ASP B 1 152 ? -3.453  18.497  20.153 1.00 12.52 ? 169 ASP B C   1 
ATOM   2333 O O   . ASP B 1 152 ? -4.087  19.052  19.250 1.00 14.08 ? 169 ASP B O   1 
ATOM   2334 C CB  . ASP B 1 152 ? -5.094  17.443  21.677 1.00 17.54 ? 169 ASP B CB  1 
ATOM   2335 C CG  . ASP B 1 152 ? -5.928  16.218  21.987 1.00 22.65 ? 169 ASP B CG  1 
ATOM   2336 O OD1 . ASP B 1 152 ? -5.794  15.214  21.268 1.00 23.80 ? 169 ASP B OD1 1 
ATOM   2337 O OD2 . ASP B 1 152 ? -6.712  16.267  22.965 1.00 25.40 ? 169 ASP B OD2 1 
ATOM   2338 N N   . TYR B 1 153 ? -2.358  19.032  20.681 1.00 10.93 ? 170 TYR B N   1 
ATOM   2339 C CA  . TYR B 1 153 ? -1.813  20.307  20.245 1.00 9.15  ? 170 TYR B CA  1 
ATOM   2340 C C   . TYR B 1 153 ? -0.569  20.162  19.388 1.00 8.79  ? 170 TYR B C   1 
ATOM   2341 O O   . TYR B 1 153 ? -0.021  21.167  18.950 1.00 9.75  ? 170 TYR B O   1 
ATOM   2342 C CB  . TYR B 1 153 ? -1.569  21.217  21.460 1.00 11.20 ? 170 TYR B CB  1 
ATOM   2343 C CG  . TYR B 1 153 ? -2.875  21.536  22.135 1.00 11.01 ? 170 TYR B CG  1 
ATOM   2344 C CD1 . TYR B 1 153 ? -3.715  22.514  21.618 1.00 11.60 ? 170 TYR B CD1 1 
ATOM   2345 C CD2 . TYR B 1 153 ? -3.312  20.811  23.233 1.00 12.88 ? 170 TYR B CD2 1 
ATOM   2346 C CE1 . TYR B 1 153 ? -4.930  22.782  22.199 1.00 13.61 ? 170 TYR B CE1 1 
ATOM   2347 C CE2 . TYR B 1 153 ? -4.527  21.069  23.821 1.00 13.54 ? 170 TYR B CE2 1 
ATOM   2348 C CZ  . TYR B 1 153 ? -5.333  22.058  23.298 1.00 14.01 ? 170 TYR B CZ  1 
ATOM   2349 O OH  . TYR B 1 153 ? -6.556  22.329  23.860 1.00 17.33 ? 170 TYR B OH  1 
ATOM   2350 N N   . ILE B 1 154 ? -0.118  18.942  19.132 1.00 10.10 ? 171 ILE B N   1 
ATOM   2351 C CA  . ILE B 1 154 ? 1.000   18.691  18.231 1.00 10.82 ? 171 ILE B CA  1 
ATOM   2352 C C   . ILE B 1 154 ? 0.524   18.178  16.880 1.00 11.19 ? 171 ILE B C   1 
ATOM   2353 O O   . ILE B 1 154 ? 1.063   18.547  15.836 1.00 12.75 ? 171 ILE B O   1 
ATOM   2354 C CB  . ILE B 1 154 ? 1.954   17.674  18.894 1.00 12.99 ? 171 ILE B CB  1 
ATOM   2355 C CG1 . ILE B 1 154 ? 2.563   18.269  20.162 1.00 17.23 ? 171 ILE B CG1 1 
ATOM   2356 C CG2 . ILE B 1 154 ? 3.030   17.201  17.918 1.00 13.47 ? 171 ILE B CG2 1 
ATOM   2357 C CD1 . ILE B 1 154 ? 3.145   17.202  21.100 1.00 15.89 ? 171 ILE B CD1 1 
ATOM   2358 N N   . PHE B 1 155 ? -0.488  17.320  16.886 1.00 12.51 ? 172 PHE B N   1 
ATOM   2359 C CA  . PHE B 1 155 ? -0.930  16.617  15.692 1.00 13.76 ? 172 PHE B CA  1 
ATOM   2360 C C   . PHE B 1 155 ? -2.268  17.166  15.225 1.00 16.84 ? 172 PHE B C   1 
ATOM   2361 O O   . PHE B 1 155 ? -3.108  17.563  16.037 1.00 18.44 ? 172 PHE B O   1 
ATOM   2362 C CB  . PHE B 1 155 ? -1.069  15.127  15.987 1.00 11.40 ? 172 PHE B CB  1 
ATOM   2363 C CG  . PHE B 1 155 ? 0.199   14.499  16.487 1.00 11.08 ? 172 PHE B CG  1 
ATOM   2364 C CD1 . PHE B 1 155 ? 1.317   14.441  15.680 1.00 10.93 ? 172 PHE B CD1 1 
ATOM   2365 C CD2 . PHE B 1 155 ? 0.278   13.984  17.761 1.00 13.09 ? 172 PHE B CD2 1 
ATOM   2366 C CE1 . PHE B 1 155 ? 2.487   13.880  16.127 1.00 14.12 ? 172 PHE B CE1 1 
ATOM   2367 C CE2 . PHE B 1 155 ? 1.449   13.414  18.217 1.00 13.70 ? 172 PHE B CE2 1 
ATOM   2368 C CZ  . PHE B 1 155 ? 2.558   13.359  17.397 1.00 14.25 ? 172 PHE B CZ  1 
ATOM   2369 N N   . GLU B 1 156 ? -2.459  17.181  13.903 1.00 22.83 ? 173 GLU B N   1 
ATOM   2370 C CA  . GLU B 1 156 ? -3.728  17.595  13.295 1.00 27.76 ? 173 GLU B CA  1 
ATOM   2371 C C   . GLU B 1 156 ? -4.850  16.651  13.695 1.00 31.24 ? 173 GLU B C   1 
ATOM   2372 O O   . GLU B 1 156 ? -6.027  17.003  13.592 1.00 33.57 ? 173 GLU B O   1 
ATOM   2373 C CB  . GLU B 1 156 ? -3.639  17.585  11.767 1.00 29.98 ? 173 GLU B CB  1 
ATOM   2374 C CG  . GLU B 1 156 ? -2.466  18.316  11.213 1.00 32.06 ? 173 GLU B CG  1 
ATOM   2375 C CD  . GLU B 1 156 ? -2.444  18.319  9.700  1.00 27.35 ? 173 GLU B CD  1 
ATOM   2376 O OE1 . GLU B 1 156 ? -2.953  17.348  9.073  1.00 26.35 ? 173 GLU B OE1 1 
ATOM   2377 O OE2 . GLU B 1 156 ? -1.904  19.298  9.145  1.00 18.39 ? 173 GLU B OE2 1 
ATOM   2378 O OXT . GLU B 1 156 ? -4.606  15.514  14.108 1.00 30.31 ? 173 GLU B OXT 1 
ATOM   2379 N N   . HIS C 1 8   ? 43.641  21.218  8.698  1.00 35.47 ? 25  HIS C N   1 
ATOM   2380 C CA  . HIS C 1 8   ? 44.251  22.522  8.466  1.00 31.19 ? 25  HIS C CA  1 
ATOM   2381 C C   . HIS C 1 8   ? 43.279  23.637  8.828  1.00 26.33 ? 25  HIS C C   1 
ATOM   2382 O O   . HIS C 1 8   ? 42.228  23.799  8.209  1.00 29.35 ? 25  HIS C O   1 
ATOM   2383 C CB  . HIS C 1 8   ? 44.679  22.666  7.005  1.00 33.58 ? 25  HIS C CB  1 
ATOM   2384 N N   . VAL C 1 9   ? 43.647  24.421  9.830  1.00 15.97 ? 26  VAL C N   1 
ATOM   2385 C CA  . VAL C 1 9   ? 42.827  25.512  10.284 1.00 13.48 ? 26  VAL C CA  1 
ATOM   2386 C C   . VAL C 1 9   ? 43.359  26.822  9.717  1.00 14.09 ? 26  VAL C C   1 
ATOM   2387 O O   . VAL C 1 9   ? 44.477  26.906  9.207  1.00 16.52 ? 26  VAL C O   1 
ATOM   2388 C CB  . VAL C 1 9   ? 42.724  25.566  11.830 1.00 11.41 ? 26  VAL C CB  1 
ATOM   2389 C CG1 . VAL C 1 9   ? 42.096  24.284  12.352 1.00 14.90 ? 26  VAL C CG1 1 
ATOM   2390 C CG2 . VAL C 1 9   ? 44.086  25.783  12.448 1.00 13.19 ? 26  VAL C CG2 1 
ATOM   2391 N N   . GLU C 1 10  ? 42.534  27.860  9.804  1.00 10.66 ? 27  GLU C N   1 
ATOM   2392 C CA  . GLU C 1 10  ? 42.920  29.216  9.467  1.00 10.18 ? 27  GLU C CA  1 
ATOM   2393 C C   . GLU C 1 10  ? 42.328  30.142  10.522 1.00 7.29  ? 27  GLU C C   1 
ATOM   2394 O O   . GLU C 1 10  ? 41.621  29.700  11.430 1.00 8.71  ? 27  GLU C O   1 
ATOM   2395 C CB  . GLU C 1 10  ? 42.462  29.573  8.045  1.00 13.32 ? 27  GLU C CB  1 
ATOM   2396 C CG  . GLU C 1 10  ? 40.966  29.546  7.906  1.00 10.17 ? 27  GLU C CG  1 
ATOM   2397 C CD  . GLU C 1 10  ? 40.457  29.756  6.490  1.00 14.63 ? 27  GLU C CD  1 
ATOM   2398 O OE1 . GLU C 1 10  ? 41.250  29.714  5.528  1.00 20.54 ? 27  GLU C OE1 1 
ATOM   2399 O OE2 . GLU C 1 10  ? 39.233  29.984  6.346  1.00 10.26 ? 27  GLU C OE2 1 
ATOM   2400 N N   . GLN C 1 11  ? 42.630  31.433  10.405 1.00 7.96  ? 28  GLN C N   1 
ATOM   2401 C CA  . GLN C 1 11  ? 42.176  32.464  11.330 1.00 8.08  ? 28  GLN C CA  1 
ATOM   2402 C C   . GLN C 1 11  ? 41.440  33.565  10.585 1.00 7.36  ? 28  GLN C C   1 
ATOM   2403 O O   . GLN C 1 11  ? 41.855  33.992  9.501  1.00 8.55  ? 28  GLN C O   1 
ATOM   2404 C CB  . GLN C 1 11  ? 43.350  33.056  12.124 1.00 9.61  ? 28  GLN C CB  1 
ATOM   2405 C CG  . GLN C 1 11  ? 43.944  32.031  13.069 1.00 10.69 ? 28  GLN C CG  1 
ATOM   2406 C CD  . GLN C 1 11  ? 44.971  32.619  14.006 1.00 13.24 ? 28  GLN C CD  1 
ATOM   2407 O OE1 . GLN C 1 11  ? 45.331  33.788  13.912 1.00 14.77 ? 28  GLN C OE1 1 
ATOM   2408 N NE2 . GLN C 1 11  ? 45.442  31.809  14.921 1.00 14.06 ? 28  GLN C NE2 1 
ATOM   2409 N N   . THR C 1 12  ? 40.355  34.041  11.187 1.00 6.92  ? 29  THR C N   1 
ATOM   2410 C CA  . THR C 1 12  ? 39.587  35.140  10.632 1.00 6.70  ? 29  THR C CA  1 
ATOM   2411 C C   . THR C 1 12  ? 39.495  36.275  11.637 1.00 7.35  ? 29  THR C C   1 
ATOM   2412 O O   . THR C 1 12  ? 39.561  36.048  12.845 1.00 7.87  ? 29  THR C O   1 
ATOM   2413 C CB  . THR C 1 12  ? 38.185  34.708  10.175 1.00 8.33  ? 29  THR C CB  1 
ATOM   2414 O OG1 . THR C 1 12  ? 37.656  35.743  9.349  1.00 8.65  ? 29  THR C OG1 1 
ATOM   2415 C CG2 . THR C 1 12  ? 37.257  34.440  11.331 1.00 8.97  ? 29  THR C CG2 1 
ATOM   2416 N N   . TYR C 1 13  ? 39.319  37.497  11.129 1.00 7.91  ? 30  TYR C N   1 
ATOM   2417 C CA  . TYR C 1 13  ? 39.074  38.673  11.960 1.00 7.22  ? 30  TYR C CA  1 
ATOM   2418 C C   . TYR C 1 13  ? 37.576  38.927  12.041 1.00 8.20  ? 30  TYR C C   1 
ATOM   2419 O O   . TYR C 1 13  ? 36.902  39.066  11.018 1.00 8.28  ? 30  TYR C O   1 
ATOM   2420 C CB  . TYR C 1 13  ? 39.805  39.910  11.426 1.00 6.96  ? 30  TYR C CB  1 
ATOM   2421 C CG  . TYR C 1 13  ? 39.536  41.123  12.284 1.00 6.22  ? 30  TYR C CG  1 
ATOM   2422 C CD1 . TYR C 1 13  ? 40.047  41.196  13.574 1.00 7.71  ? 30  TYR C CD1 1 
ATOM   2423 C CD2 . TYR C 1 13  ? 38.742  42.177  11.829 1.00 6.99  ? 30  TYR C CD2 1 
ATOM   2424 C CE1 . TYR C 1 13  ? 39.784  42.278  14.381 1.00 8.09  ? 30  TYR C CE1 1 
ATOM   2425 C CE2 . TYR C 1 13  ? 38.466  43.274  12.647 1.00 6.97  ? 30  TYR C CE2 1 
ATOM   2426 C CZ  . TYR C 1 13  ? 38.998  43.310  13.917 1.00 8.42  ? 30  TYR C CZ  1 
ATOM   2427 O OH  . TYR C 1 13  ? 38.753  44.350  14.782 1.00 9.09  ? 30  TYR C OH  1 
ATOM   2428 N N   . LEU C 1 14  ? 37.057  38.954  13.255 1.00 6.93  ? 31  LEU C N   1 
ATOM   2429 C CA  . LEU C 1 14  ? 35.659  39.247  13.520 1.00 8.03  ? 31  LEU C CA  1 
ATOM   2430 C C   . LEU C 1 14  ? 35.617  40.412  14.498 1.00 6.19  ? 31  LEU C C   1 
ATOM   2431 O O   . LEU C 1 14  ? 36.371  40.449  15.468 1.00 8.30  ? 31  LEU C O   1 
ATOM   2432 C CB  . LEU C 1 14  ? 34.941  38.021  14.101 1.00 8.61  ? 31  LEU C CB  1 
ATOM   2433 C CG  . LEU C 1 14  ? 34.695  36.884  13.093 1.00 8.87  ? 31  LEU C CG  1 
ATOM   2434 C CD1 . LEU C 1 14  ? 34.592  35.538  13.746 1.00 11.84 ? 31  LEU C CD1 1 
ATOM   2435 C CD2 . LEU C 1 14  ? 33.423  37.216  12.345 1.00 9.14  ? 31  LEU C CD2 1 
ATOM   2436 N N   . MET C 1 15  ? 34.725  41.360  14.263 1.00 7.37  ? 32  MET C N   1 
ATOM   2437 C CA  . MET C 1 15  ? 34.663  42.553  15.094 1.00 7.83  ? 32  MET C CA  1 
ATOM   2438 C C   . MET C 1 15  ? 33.208  42.822  15.430 1.00 6.52  ? 32  MET C C   1 
ATOM   2439 O O   . MET C 1 15  ? 32.388  42.998  14.525 1.00 8.98  ? 32  MET C O   1 
ATOM   2440 C CB  . MET C 1 15  ? 35.285  43.739  14.355 1.00 8.57  ? 32  MET C CB  1 
ATOM   2441 C CG  . MET C 1 15  ? 35.204  45.037  15.110 1.00 9.46  ? 32  MET C CG  1 
ATOM   2442 S SD  . MET C 1 15  ? 36.245  46.325  14.373 1.00 10.84 ? 32  MET C SD  1 
ATOM   2443 C CE  . MET C 1 15  ? 35.694  46.308  12.674 1.00 10.94 ? 32  MET C CE  1 
ATOM   2444 N N   . ILE C 1 16  ? 32.901  42.884  16.722 1.00 7.01  ? 33  ILE C N   1 
ATOM   2445 C CA  . ILE C 1 16  ? 31.566  43.287  17.157 1.00 7.34  ? 33  ILE C CA  1 
ATOM   2446 C C   . ILE C 1 16  ? 31.492  44.803  17.040 1.00 7.03  ? 33  ILE C C   1 
ATOM   2447 O O   . ILE C 1 16  ? 32.319  45.519  17.617 1.00 8.40  ? 33  ILE C O   1 
ATOM   2448 C CB  . ILE C 1 16  ? 31.266  42.799  18.581 1.00 6.50  ? 33  ILE C CB  1 
ATOM   2449 C CG1 . ILE C 1 16  ? 31.410  41.272  18.613 1.00 7.36  ? 33  ILE C CG1 1 
ATOM   2450 C CG2 . ILE C 1 16  ? 29.876  43.245  19.016 1.00 7.83  ? 33  ILE C CG2 1 
ATOM   2451 C CD1 . ILE C 1 16  ? 31.146  40.649  19.961 1.00 9.45  ? 33  ILE C CD1 1 
ATOM   2452 N N   . LYS C 1 17  ? 30.515  45.291  16.273 1.00 7.20  ? 34  LYS C N   1 
ATOM   2453 C CA  . LYS C 1 17  ? 30.332  46.711  16.012 1.00 6.02  ? 34  LYS C CA  1 
ATOM   2454 C C   . LYS C 1 17  ? 29.669  47.385  17.214 1.00 6.86  ? 34  LYS C C   1 
ATOM   2455 O O   . LYS C 1 17  ? 29.174  46.728  18.137 1.00 7.22  ? 34  LYS C O   1 
ATOM   2456 C CB  . LYS C 1 17  ? 29.478  46.884  14.757 1.00 7.10  ? 34  LYS C CB  1 
ATOM   2457 C CG  . LYS C 1 17  ? 30.052  46.232  13.501 1.00 8.29  ? 34  LYS C CG  1 
ATOM   2458 C CD  . LYS C 1 17  ? 29.204  46.533  12.273 1.00 9.20  ? 34  LYS C CD  1 
ATOM   2459 C CE  . LYS C 1 17  ? 29.840  45.968  11.013 1.00 10.97 ? 34  LYS C CE  1 
ATOM   2460 N NZ  . LYS C 1 17  ? 29.061  46.320  9.804  1.00 8.88  ? 34  LYS C NZ  1 
ATOM   2461 N N   . PRO C 1 18  ? 29.642  48.716  17.243 1.00 6.86  ? 35  PRO C N   1 
ATOM   2462 C CA  . PRO C 1 18  ? 29.107  49.390  18.440 1.00 6.05  ? 35  PRO C CA  1 
ATOM   2463 C C   . PRO C 1 18  ? 27.699  48.980  18.792 1.00 8.00  ? 35  PRO C C   1 
ATOM   2464 O O   . PRO C 1 18  ? 27.349  48.994  19.976 1.00 7.84  ? 35  PRO C O   1 
ATOM   2465 C CB  . PRO C 1 18  ? 29.221  50.880  18.087 1.00 8.14  ? 35  PRO C CB  1 
ATOM   2466 C CG  . PRO C 1 18  ? 30.440  50.939  17.161 1.00 7.98  ? 35  PRO C CG  1 
ATOM   2467 C CD  . PRO C 1 18  ? 30.300  49.667  16.323 1.00 7.51  ? 35  PRO C CD  1 
ATOM   2468 N N   . ASP C 1 19  ? 26.872  48.638  17.805 1.00 6.89  ? 36  ASP C N   1 
ATOM   2469 C CA  . ASP C 1 19  ? 25.523  48.170  18.111 1.00 6.83  ? 36  ASP C CA  1 
ATOM   2470 C C   . ASP C 1 19  ? 25.527  46.854  18.893 1.00 7.81  ? 36  ASP C C   1 
ATOM   2471 O O   . ASP C 1 19  ? 24.680  46.646  19.773 1.00 8.36  ? 36  ASP C O   1 
ATOM   2472 C CB  . ASP C 1 19  ? 24.630  48.099  16.859 1.00 8.59  ? 36  ASP C CB  1 
ATOM   2473 C CG  . ASP C 1 19  ? 25.223  47.320  15.701 1.00 9.17  ? 36  ASP C CG  1 
ATOM   2474 O OD1 . ASP C 1 19  ? 26.441  47.387  15.438 1.00 10.12 ? 36  ASP C OD1 1 
ATOM   2475 O OD2 . ASP C 1 19  ? 24.417  46.689  14.977 1.00 9.04  ? 36  ASP C OD2 1 
ATOM   2476 N N   . GLY C 1 20  ? 26.451  45.949  18.592 1.00 9.01  ? 37  GLY C N   1 
ATOM   2477 C CA  . GLY C 1 20  ? 26.541  44.731  19.379 1.00 7.25  ? 37  GLY C CA  1 
ATOM   2478 C C   . GLY C 1 20  ? 26.955  45.008  20.812 1.00 6.37  ? 37  GLY C C   1 
ATOM   2479 O O   . GLY C 1 20  ? 26.492  44.336  21.744 1.00 7.79  ? 37  GLY C O   1 
ATOM   2480 N N   . ILE C 1 21  ? 27.857  45.971  21.007 1.00 6.43  ? 38  ILE C N   1 
ATOM   2481 C CA  . ILE C 1 21  ? 28.249  46.359  22.358 1.00 8.31  ? 38  ILE C CA  1 
ATOM   2482 C C   . ILE C 1 21  ? 27.069  46.961  23.104 1.00 6.75  ? 38  ILE C C   1 
ATOM   2483 O O   . ILE C 1 21  ? 26.766  46.580  24.239 1.00 7.77  ? 38  ILE C O   1 
ATOM   2484 C CB  . ILE C 1 21  ? 29.431  47.345  22.325 1.00 7.56  ? 38  ILE C CB  1 
ATOM   2485 C CG1 . ILE C 1 21  ? 30.633  46.805  21.520 1.00 9.88  ? 38  ILE C CG1 1 
ATOM   2486 C CG2 . ILE C 1 21  ? 29.811  47.728  23.764 1.00 10.58 ? 38  ILE C CG2 1 
ATOM   2487 C CD1 . ILE C 1 21  ? 31.250  45.556  22.043 1.00 9.80  ? 38  ILE C CD1 1 
ATOM   2488 N N   . GLN C 1 22  ? 26.399  47.934  22.480 1.00 7.72  ? 39  GLN C N   1 
ATOM   2489 C CA  . GLN C 1 22  ? 25.354  48.697  23.162 1.00 8.56  ? 39  GLN C CA  1 
ATOM   2490 C C   . GLN C 1 22  ? 24.105  47.870  23.416 1.00 8.39  ? 39  GLN C C   1 
ATOM   2491 O O   . GLN C 1 22  ? 23.395  48.110  24.406 1.00 9.02  ? 39  GLN C O   1 
ATOM   2492 C CB  . GLN C 1 22  ? 25.005  49.938  22.339 1.00 8.12  ? 39  GLN C CB  1 
ATOM   2493 C CG  . GLN C 1 22  ? 26.093  51.011  22.343 1.00 9.69  ? 39  GLN C CG  1 
ATOM   2494 C CD  . GLN C 1 22  ? 26.155  51.747  23.659 1.00 10.30 ? 39  GLN C CD  1 
ATOM   2495 O OE1 . GLN C 1 22  ? 25.385  51.466  24.563 1.00 14.20 ? 39  GLN C OE1 1 
ATOM   2496 N NE2 . GLN C 1 22  ? 27.075  52.683  23.778 1.00 10.53 ? 39  GLN C NE2 1 
ATOM   2497 N N   . ARG C 1 23  ? 23.788  46.930  22.523 1.00 6.66  ? 40  ARG C N   1 
ATOM   2498 C CA  . ARG C 1 23  ? 22.661  46.026  22.732 1.00 6.27  ? 40  ARG C CA  1 
ATOM   2499 C C   . ARG C 1 23  ? 23.025  44.896  23.679 1.00 7.61  ? 40  ARG C C   1 
ATOM   2500 O O   . ARG C 1 23  ? 22.156  44.115  24.067 1.00 8.44  ? 40  ARG C O   1 
ATOM   2501 C CB  . ARG C 1 23  ? 22.141  45.512  21.387 1.00 7.87  ? 40  ARG C CB  1 
ATOM   2502 C CG  . ARG C 1 23  ? 21.650  46.630  20.509 1.00 7.45  ? 40  ARG C CG  1 
ATOM   2503 C CD  . ARG C 1 23  ? 21.204  46.140  19.154 1.00 7.85  ? 40  ARG C CD  1 
ATOM   2504 N NE  . ARG C 1 23  ? 20.048  45.256  19.268 1.00 8.65  ? 40  ARG C NE  1 
ATOM   2505 C CZ  . ARG C 1 23  ? 19.660  44.418  18.320 1.00 7.28  ? 40  ARG C CZ  1 
ATOM   2506 N NH1 . ARG C 1 23  ? 20.261  44.383  17.141 1.00 7.35  ? 40  ARG C NH1 1 
ATOM   2507 N NH2 . ARG C 1 23  ? 18.637  43.595  18.556 1.00 9.21  ? 40  ARG C NH2 1 
ATOM   2508 N N   . GLN C 1 24  ? 24.295  44.818  24.075 1.00 7.22  ? 41  GLN C N   1 
ATOM   2509 C CA  . GLN C 1 24  ? 24.763  43.925  25.120 1.00 7.22  ? 41  GLN C CA  1 
ATOM   2510 C C   . GLN C 1 24  ? 24.514  42.467  24.752 1.00 6.60  ? 41  GLN C C   1 
ATOM   2511 O O   . GLN C 1 24  ? 24.011  41.675  25.547 1.00 8.26  ? 41  GLN C O   1 
ATOM   2512 C CB  . GLN C 1 24  ? 24.190  44.297  26.489 1.00 9.77  ? 41  GLN C CB  1 
ATOM   2513 C CG  . GLN C 1 24  ? 24.519  45.735  26.884 1.00 9.52  ? 41  GLN C CG  1 
ATOM   2514 C CD  . GLN C 1 24  ? 24.859  45.856  28.341 1.00 10.25 ? 41  GLN C CD  1 
ATOM   2515 O OE1 . GLN C 1 24  ? 24.003  46.144  29.175 1.00 12.00 ? 41  GLN C OE1 1 
ATOM   2516 N NE2 . GLN C 1 24  ? 26.121  45.621  28.666 1.00 10.84 ? 41  GLN C NE2 1 
ATOM   2517 N N   . VAL C 1 25  ? 24.958  42.102  23.551 1.00 6.84  ? 42  VAL C N   1 
ATOM   2518 C CA  . VAL C 1 25  ? 24.873  40.754  23.009 1.00 6.28  ? 42  VAL C CA  1 
ATOM   2519 C C   . VAL C 1 25  ? 26.258  40.183  22.718 1.00 6.73  ? 42  VAL C C   1 
ATOM   2520 O O   . VAL C 1 25  ? 26.389  39.226  21.964 1.00 7.30  ? 42  VAL C O   1 
ATOM   2521 C CB  . VAL C 1 25  ? 23.957  40.699  21.770 1.00 7.22  ? 42  VAL C CB  1 
ATOM   2522 C CG1 . VAL C 1 25  ? 22.478  41.039  22.136 1.00 9.75  ? 42  VAL C CG1 1 
ATOM   2523 C CG2 . VAL C 1 25  ? 24.471  41.633  20.667 1.00 11.31 ? 42  VAL C CG2 1 
ATOM   2524 N N   . VAL C 1 26  ? 27.297  40.769  23.311 1.00 6.01  ? 43  VAL C N   1 
ATOM   2525 C CA  . VAL C 1 26  ? 28.658  40.290  23.074 1.00 6.60  ? 43  VAL C CA  1 
ATOM   2526 C C   . VAL C 1 26  ? 28.777  38.814  23.424 1.00 6.82  ? 43  VAL C C   1 
ATOM   2527 O O   . VAL C 1 26  ? 29.367  38.011  22.676 1.00 7.37  ? 43  VAL C O   1 
ATOM   2528 C CB  . VAL C 1 26  ? 29.645  41.142  23.892 1.00 6.18  ? 43  VAL C CB  1 
ATOM   2529 C CG1 . VAL C 1 26  ? 31.056  40.535  23.901 1.00 8.71  ? 43  VAL C CG1 1 
ATOM   2530 C CG2 . VAL C 1 26  ? 29.672  42.577  23.367 1.00 6.76  ? 43  VAL C CG2 1 
ATOM   2531 N N   . GLY C 1 27  ? 28.287  38.439  24.604 1.00 6.31  ? 44  GLY C N   1 
ATOM   2532 C CA  . GLY C 1 27  ? 28.437  37.053  25.024 1.00 6.00  ? 44  GLY C CA  1 
ATOM   2533 C C   . GLY C 1 27  ? 27.720  36.094  24.099 1.00 5.82  ? 44  GLY C C   1 
ATOM   2534 O O   . GLY C 1 27  ? 28.234  35.017  23.787 1.00 7.44  ? 44  GLY C O   1 
ATOM   2535 N N   . GLU C 1 28  ? 26.509  36.460  23.668 1.00 7.44  ? 45  GLU C N   1 
ATOM   2536 C CA  . GLU C 1 28  ? 25.774  35.591  22.765 1.00 6.38  ? 45  GLU C CA  1 
ATOM   2537 C C   . GLU C 1 28  ? 26.522  35.410  21.449 1.00 5.73  ? 45  GLU C C   1 
ATOM   2538 O O   . GLU C 1 28  ? 26.530  34.311  20.879 1.00 7.56  ? 45  GLU C O   1 
ATOM   2539 C CB  . GLU C 1 28  ? 24.388  36.152  22.470 1.00 8.83  ? 45  GLU C CB  1 
ATOM   2540 C CG  . GLU C 1 28  ? 23.405  36.101  23.568 1.00 12.03 ? 45  GLU C CG  1 
ATOM   2541 C CD  . GLU C 1 28  ? 22.046  36.383  22.973 1.00 18.98 ? 45  GLU C CD  1 
ATOM   2542 O OE1 . GLU C 1 28  ? 21.531  35.512  22.234 1.00 24.83 ? 45  GLU C OE1 1 
ATOM   2543 O OE2 . GLU C 1 28  ? 21.551  37.507  23.134 1.00 20.33 ? 45  GLU C OE2 1 
ATOM   2544 N N   . ILE C 1 29  ? 27.121  36.483  20.923 1.00 5.68  ? 46  ILE C N   1 
ATOM   2545 C CA  . ILE C 1 29  ? 27.881  36.364  19.680 1.00 6.20  ? 46  ILE C CA  1 
ATOM   2546 C C   . ILE C 1 29  ? 29.065  35.422  19.866 1.00 6.45  ? 46  ILE C C   1 
ATOM   2547 O O   . ILE C 1 29  ? 29.292  34.506  19.059 1.00 7.29  ? 46  ILE C O   1 
ATOM   2548 C CB  . ILE C 1 29  ? 28.346  37.751  19.209 1.00 7.64  ? 46  ILE C CB  1 
ATOM   2549 C CG1 . ILE C 1 29  ? 27.146  38.606  18.804 1.00 8.65  ? 46  ILE C CG1 1 
ATOM   2550 C CG2 . ILE C 1 29  ? 29.348  37.609  18.090 1.00 8.88  ? 46  ILE C CG2 1 
ATOM   2551 C CD1 . ILE C 1 29  ? 27.463  40.076  18.628 1.00 11.13 ? 46  ILE C CD1 1 
ATOM   2552 N N   . ILE C 1 30  ? 29.836  35.629  20.938 1.00 6.59  ? 47  ILE C N   1 
ATOM   2553 C CA  . ILE C 1 30  ? 30.988  34.771  21.203 1.00 5.98  ? 47  ILE C CA  1 
ATOM   2554 C C   . ILE C 1 30  ? 30.557  33.315  21.335 1.00 6.26  ? 47  ILE C C   1 
ATOM   2555 O O   . ILE C 1 30  ? 31.202  32.414  20.789 1.00 6.42  ? 47  ILE C O   1 
ATOM   2556 C CB  . ILE C 1 30  ? 31.777  35.266  22.429 1.00 6.65  ? 47  ILE C CB  1 
ATOM   2557 C CG1 . ILE C 1 30  ? 32.432  36.629  22.140 1.00 6.96  ? 47  ILE C CG1 1 
ATOM   2558 C CG2 . ILE C 1 30  ? 32.815  34.234  22.874 1.00 7.01  ? 47  ILE C CG2 1 
ATOM   2559 C CD1 . ILE C 1 30  ? 32.953  37.331  23.379 1.00 8.77  ? 47  ILE C CD1 1 
ATOM   2560 N N   . SER C 1 31  ? 29.439  33.064  22.032 1.00 5.99  ? 48  SER C N   1 
ATOM   2561 C CA  . SER C 1 31  ? 28.977  31.692  22.221 1.00 6.02  ? 48  SER C CA  1 
ATOM   2562 C C   . SER C 1 31  ? 28.666  31.007  20.897 1.00 6.77  ? 48  SER C C   1 
ATOM   2563 O O   . SER C 1 31  ? 28.838  29.788  20.778 1.00 8.03  ? 48  SER C O   1 
ATOM   2564 C CB  . SER C 1 31  ? 27.738  31.668  23.129 1.00 7.65  ? 48  SER C CB  1 
ATOM   2565 O OG  . SER C 1 31  ? 28.049  31.997  24.472 1.00 7.21  ? 48  SER C OG  1 
ATOM   2566 N N   . ARG C 1 32  ? 28.179  31.742  19.900 1.00 6.50  ? 49  ARG C N   1 
ATOM   2567 C CA  . ARG C 1 32  ? 27.864  31.083  18.635 1.00 7.17  ? 49  ARG C CA  1 
ATOM   2568 C C   . ARG C 1 32  ? 29.119  30.502  17.991 1.00 7.79  ? 49  ARG C C   1 
ATOM   2569 O O   . ARG C 1 32  ? 29.070  29.445  17.356 1.00 8.48  ? 49  ARG C O   1 
ATOM   2570 C CB  . ARG C 1 32  ? 27.193  32.049  17.674 1.00 9.92  ? 49  ARG C CB  1 
ATOM   2571 C CG  . ARG C 1 32  ? 25.801  32.431  18.071 1.00 10.44 ? 49  ARG C CG  1 
ATOM   2572 C CD  . ARG C 1 32  ? 25.075  33.001  16.918 1.00 14.65 ? 49  ARG C CD  1 
ATOM   2573 N NE  . ARG C 1 32  ? 23.705  33.282  17.305 1.00 16.10 ? 49  ARG C NE  1 
ATOM   2574 C CZ  . ARG C 1 32  ? 22.687  33.298  16.465 1.00 12.97 ? 49  ARG C CZ  1 
ATOM   2575 N NH1 . ARG C 1 32  ? 22.855  33.070  15.171 1.00 13.77 ? 49  ARG C NH1 1 
ATOM   2576 N NH2 . ARG C 1 32  ? 21.467  33.505  16.942 1.00 15.28 ? 49  ARG C NH2 1 
ATOM   2577 N N   . PHE C 1 33  ? 30.246  31.200  18.106 1.00 7.36  ? 50  PHE C N   1 
ATOM   2578 C CA  . PHE C 1 33  ? 31.473  30.695  17.500 1.00 6.58  ? 50  PHE C CA  1 
ATOM   2579 C C   . PHE C 1 33  ? 32.121  29.618  18.364 1.00 6.98  ? 50  PHE C C   1 
ATOM   2580 O O   . PHE C 1 33  ? 32.609  28.617  17.839 1.00 7.92  ? 50  PHE C O   1 
ATOM   2581 C CB  . PHE C 1 33  ? 32.408  31.876  17.224 1.00 8.47  ? 50  PHE C CB  1 
ATOM   2582 C CG  . PHE C 1 33  ? 31.861  32.829  16.194 1.00 6.49  ? 50  PHE C CG  1 
ATOM   2583 C CD1 . PHE C 1 33  ? 31.797  32.476  14.868 1.00 8.29  ? 50  PHE C CD1 1 
ATOM   2584 C CD2 . PHE C 1 33  ? 31.397  34.074  16.565 1.00 9.62  ? 50  PHE C CD2 1 
ATOM   2585 C CE1 . PHE C 1 33  ? 31.280  33.335  13.924 1.00 9.09  ? 50  PHE C CE1 1 
ATOM   2586 C CE2 . PHE C 1 33  ? 30.876  34.942  15.632 1.00 10.06 ? 50  PHE C CE2 1 
ATOM   2587 C CZ  . PHE C 1 33  ? 30.817  34.580  14.318 1.00 9.12  ? 50  PHE C CZ  1 
ATOM   2588 N N   . GLU C 1 34  ? 32.119  29.797  19.682 1.00 7.50  ? 51  GLU C N   1 
ATOM   2589 C CA  . GLU C 1 34  ? 32.603  28.756  20.577 1.00 7.53  ? 51  GLU C CA  1 
ATOM   2590 C C   . GLU C 1 34  ? 31.832  27.464  20.374 1.00 5.80  ? 51  GLU C C   1 
ATOM   2591 O O   . GLU C 1 34  ? 32.393  26.370  20.539 1.00 7.69  ? 51  GLU C O   1 
ATOM   2592 C CB  . GLU C 1 34  ? 32.434  29.195  22.035 1.00 8.57  ? 51  GLU C CB  1 
ATOM   2593 C CG  . GLU C 1 34  ? 33.456  30.182  22.558 1.00 9.23  ? 51  GLU C CG  1 
ATOM   2594 C CD  . GLU C 1 34  ? 33.256  30.460  24.025 1.00 8.79  ? 51  GLU C CD  1 
ATOM   2595 O OE1 . GLU C 1 34  ? 32.181  31.005  24.361 1.00 8.15  ? 51  GLU C OE1 1 
ATOM   2596 O OE2 . GLU C 1 34  ? 34.155  30.120  24.845 1.00 9.45  ? 51  GLU C OE2 1 
ATOM   2597 N N   . LYS C 1 35  ? 30.546  27.564  20.025 1.00 7.50  ? 52  LYS C N   1 
ATOM   2598 C CA  . LYS C 1 35  ? 29.712  26.375  19.941 1.00 8.30  ? 52  LYS C CA  1 
ATOM   2599 C C   . LYS C 1 35  ? 30.201  25.406  18.881 1.00 7.36  ? 52  LYS C C   1 
ATOM   2600 O O   . LYS C 1 35  ? 29.951  24.209  18.988 1.00 8.51  ? 52  LYS C O   1 
ATOM   2601 C CB  . LYS C 1 35  ? 28.284  26.779  19.617 1.00 8.50  ? 52  LYS C CB  1 
ATOM   2602 C CG  . LYS C 1 35  ? 27.274  25.672  19.780 1.00 10.15 ? 52  LYS C CG  1 
ATOM   2603 C CD  . LYS C 1 35  ? 25.883  26.221  19.478 1.00 14.26 ? 52  LYS C CD  1 
ATOM   2604 C CE  . LYS C 1 35  ? 24.794  25.363  20.063 1.00 17.46 ? 52  LYS C CE  1 
ATOM   2605 N NZ  . LYS C 1 35  ? 24.758  25.572  21.519 1.00 21.43 ? 52  LYS C NZ  1 
ATOM   2606 N N   . ARG C 1 36  ? 30.895  25.899  17.859 1.00 6.87  ? 53  ARG C N   1 
ATOM   2607 C CA  . ARG C 1 36  ? 31.435  25.054  16.801 1.00 7.05  ? 53  ARG C CA  1 
ATOM   2608 C C   . ARG C 1 36  ? 32.849  24.574  17.096 1.00 6.76  ? 53  ARG C C   1 
ATOM   2609 O O   . ARG C 1 36  ? 33.468  23.924  16.243 1.00 8.19  ? 53  ARG C O   1 
ATOM   2610 C CB  . ARG C 1 36  ? 31.402  25.791  15.462 1.00 7.46  ? 53  ARG C CB  1 
ATOM   2611 C CG  . ARG C 1 36  ? 30.003  26.119  14.999 1.00 8.49  ? 53  ARG C CG  1 
ATOM   2612 C CD  . ARG C 1 36  ? 29.965  26.624  13.591 1.00 8.53  ? 53  ARG C CD  1 
ATOM   2613 N NE  . ARG C 1 36  ? 30.278  25.601  12.595 1.00 8.45  ? 53  ARG C NE  1 
ATOM   2614 C CZ  . ARG C 1 36  ? 30.274  25.830  11.289 1.00 8.93  ? 53  ARG C CZ  1 
ATOM   2615 N NH1 . ARG C 1 36  ? 29.980  27.024  10.806 1.00 8.46  ? 53  ARG C NH1 1 
ATOM   2616 N NH2 . ARG C 1 36  ? 30.580  24.842  10.453 1.00 9.01  ? 53  ARG C NH2 1 
ATOM   2617 N N   . GLY C 1 37  ? 33.365  24.876  18.281 1.00 5.93  ? 54  GLY C N   1 
ATOM   2618 C CA  . GLY C 1 37  ? 34.732  24.542  18.586 1.00 8.89  ? 54  GLY C CA  1 
ATOM   2619 C C   . GLY C 1 37  ? 35.728  25.464  17.945 1.00 9.24  ? 54  GLY C C   1 
ATOM   2620 O O   . GLY C 1 37  ? 36.887  25.083  17.803 1.00 8.25  ? 54  GLY C O   1 
ATOM   2621 N N   . TYR C 1 38  ? 35.316  26.662  17.537 1.00 6.51  ? 55  TYR C N   1 
ATOM   2622 C CA  . TYR C 1 38  ? 36.283  27.647  17.092 1.00 7.45  ? 55  TYR C CA  1 
ATOM   2623 C C   . TYR C 1 38  ? 37.042  28.197  18.294 1.00 6.38  ? 55  TYR C C   1 
ATOM   2624 O O   . TYR C 1 38  ? 36.479  28.398  19.376 1.00 8.63  ? 55  TYR C O   1 
ATOM   2625 C CB  . TYR C 1 38  ? 35.600  28.778  16.330 1.00 6.39  ? 55  TYR C CB  1 
ATOM   2626 C CG  . TYR C 1 38  ? 34.966  28.366  15.013 1.00 5.90  ? 55  TYR C CG  1 
ATOM   2627 C CD1 . TYR C 1 38  ? 35.478  27.342  14.234 1.00 7.55  ? 55  TYR C CD1 1 
ATOM   2628 C CD2 . TYR C 1 38  ? 33.845  29.015  14.561 1.00 7.98  ? 55  TYR C CD2 1 
ATOM   2629 C CE1 . TYR C 1 38  ? 34.880  26.992  13.050 1.00 6.44  ? 55  TYR C CE1 1 
ATOM   2630 C CE2 . TYR C 1 38  ? 33.244  28.673  13.373 1.00 7.57  ? 55  TYR C CE2 1 
ATOM   2631 C CZ  . TYR C 1 38  ? 33.762  27.664  12.616 1.00 7.09  ? 55  TYR C CZ  1 
ATOM   2632 O OH  . TYR C 1 38  ? 33.142  27.316  11.437 1.00 9.11  ? 55  TYR C OH  1 
ATOM   2633 N N   . ARG C 1 39  ? 38.327  28.447  18.101 1.00 7.34  ? 56  ARG C N   1 
ATOM   2634 C CA  . ARG C 1 39  ? 39.216  28.832  19.184 1.00 7.39  ? 56  ARG C CA  1 
ATOM   2635 C C   . ARG C 1 39  ? 39.435  30.335  19.167 1.00 7.31  ? 56  ARG C C   1 
ATOM   2636 O O   . ARG C 1 39  ? 39.729  30.915  18.119 1.00 7.91  ? 56  ARG C O   1 
ATOM   2637 C CB  . ARG C 1 39  ? 40.551  28.110  19.024 1.00 6.85  ? 56  ARG C CB  1 
ATOM   2638 C CG  . ARG C 1 39  ? 41.572  28.426  20.112 1.00 8.34  ? 56  ARG C CG  1 
ATOM   2639 C CD  . ARG C 1 39  ? 42.872  27.651  19.925 1.00 8.59  ? 56  ARG C CD  1 
ATOM   2640 N NE  . ARG C 1 39  ? 43.705  28.127  18.822 1.00 8.47  ? 56  ARG C NE  1 
ATOM   2641 C CZ  . ARG C 1 39  ? 44.507  29.181  18.887 1.00 9.02  ? 56  ARG C CZ  1 
ATOM   2642 N NH1 . ARG C 1 39  ? 44.591  29.926  19.976 1.00 10.38 ? 56  ARG C NH1 1 
ATOM   2643 N NH2 . ARG C 1 39  ? 45.272  29.479  17.847 1.00 11.74 ? 56  ARG C NH2 1 
ATOM   2644 N N   . ILE C 1 40  ? 39.284  30.966  20.331 1.00 7.97  ? 57  ILE C N   1 
ATOM   2645 C CA  . ILE C 1 40  ? 39.586  32.387  20.475 1.00 6.86  ? 57  ILE C CA  1 
ATOM   2646 C C   . ILE C 1 40  ? 41.103  32.549  20.478 1.00 8.06  ? 57  ILE C C   1 
ATOM   2647 O O   . ILE C 1 40  ? 41.779  32.132  21.423 1.00 8.36  ? 57  ILE C O   1 
ATOM   2648 C CB  . ILE C 1 40  ? 38.980  32.970  21.754 1.00 8.17  ? 57  ILE C CB  1 
ATOM   2649 C CG1 . ILE C 1 40  ? 37.486  32.665  21.845 1.00 8.82  ? 57  ILE C CG1 1 
ATOM   2650 C CG2 . ILE C 1 40  ? 39.225  34.483  21.777 1.00 9.08  ? 57  ILE C CG2 1 
ATOM   2651 C CD1 . ILE C 1 40  ? 36.920  32.929  23.222 1.00 9.85  ? 57  ILE C CD1 1 
ATOM   2652 N N   . ALA C 1 41  ? 41.642  33.138  19.418 1.00 7.25  ? 58  ALA C N   1 
ATOM   2653 C CA  . ALA C 1 41  ? 43.076  33.385  19.315 1.00 9.21  ? 58  ALA C CA  1 
ATOM   2654 C C   . ALA C 1 41  ? 43.459  34.785  19.761 1.00 7.09  ? 58  ALA C C   1 
ATOM   2655 O O   . ALA C 1 41  ? 44.622  35.017  20.098 1.00 8.91  ? 58  ALA C O   1 
ATOM   2656 C CB  . ALA C 1 41  ? 43.562  33.165  17.879 1.00 10.21 ? 58  ALA C CB  1 
ATOM   2657 N N   . ALA C 1 42  ? 42.531  35.737  19.724 1.00 6.31  ? 59  ALA C N   1 
ATOM   2658 C CA  . ALA C 1 42  ? 42.818  37.090  20.171 1.00 7.62  ? 59  ALA C CA  1 
ATOM   2659 C C   . ALA C 1 42  ? 41.498  37.780  20.482 1.00 5.77  ? 59  ALA C C   1 
ATOM   2660 O O   . ALA C 1 42  ? 40.467  37.465  19.885 1.00 7.55  ? 59  ALA C O   1 
ATOM   2661 C CB  . ALA C 1 42  ? 43.571  37.866  19.086 1.00 9.46  ? 59  ALA C CB  1 
ATOM   2662 N N   . MET C 1 43  ? 41.542  38.747  21.399 1.00 8.39  ? 60  MET C N   1 
ATOM   2663 C CA  . MET C 1 43  ? 40.338  39.496  21.744 1.00 7.70  ? 60  MET C CA  1 
ATOM   2664 C C   . MET C 1 43  ? 40.785  40.771  22.446 1.00 7.25  ? 60  MET C C   1 
ATOM   2665 O O   . MET C 1 43  ? 41.685  40.738  23.294 1.00 9.39  ? 60  MET C O   1 
ATOM   2666 C CB  . MET C 1 43  ? 39.410  38.641  22.628 1.00 8.37  ? 60  MET C CB  1 
ATOM   2667 C CG  . MET C 1 43  ? 38.015  39.226  22.864 1.00 10.65 ? 60  MET C CG  1 
ATOM   2668 S SD  . MET C 1 43  ? 36.911  37.999  23.628 1.00 12.86 ? 60  MET C SD  1 
ATOM   2669 C CE  . MET C 1 43  ? 36.381  37.111  22.172 1.00 12.61 ? 60  MET C CE  1 
ATOM   2670 N N   . LYS C 1 44  ? 40.152  41.888  22.095 1.00 7.14  ? 61  LYS C N   1 
ATOM   2671 C CA  . LYS C 1 44  ? 40.507  43.200  22.630 1.00 10.71 ? 61  LYS C CA  1 
ATOM   2672 C C   . LYS C 1 44  ? 39.302  44.109  22.480 1.00 8.64  ? 61  LYS C C   1 
ATOM   2673 O O   . LYS C 1 44  ? 38.751  44.210  21.387 1.00 9.96  ? 61  LYS C O   1 
ATOM   2674 C CB  . LYS C 1 44  ? 41.705  43.776  21.839 1.00 12.89 ? 61  LYS C CB  1 
ATOM   2675 C CG  . LYS C 1 44  ? 41.967  45.251  21.993 1.00 21.26 ? 61  LYS C CG  1 
ATOM   2676 C CD  . LYS C 1 44  ? 43.378  45.594  21.530 1.00 23.43 ? 61  LYS C CD  1 
ATOM   2677 C CE  . LYS C 1 44  ? 43.590  45.253  20.093 1.00 24.62 ? 61  LYS C CE  1 
ATOM   2678 N NZ  . LYS C 1 44  ? 44.975  45.639  19.650 1.00 26.37 ? 61  LYS C NZ  1 
ATOM   2679 N N   . LEU C 1 45  ? 38.908  44.785  23.559 1.00 8.14  ? 62  LEU C N   1 
ATOM   2680 C CA  . LEU C 1 45  ? 37.940  45.863  23.461 1.00 7.49  ? 62  LEU C CA  1 
ATOM   2681 C C   . LEU C 1 45  ? 38.705  47.162  23.226 1.00 8.80  ? 62  LEU C C   1 
ATOM   2682 O O   . LEU C 1 45  ? 39.687  47.441  23.914 1.00 9.97  ? 62  LEU C O   1 
ATOM   2683 C CB  . LEU C 1 45  ? 37.112  45.997  24.741 1.00 9.18  ? 62  LEU C CB  1 
ATOM   2684 C CG  . LEU C 1 45  ? 36.018  47.070  24.713 1.00 11.60 ? 62  LEU C CG  1 
ATOM   2685 C CD1 . LEU C 1 45  ? 34.770  46.530  24.038 1.00 12.93 ? 62  LEU C CD1 1 
ATOM   2686 C CD2 . LEU C 1 45  ? 35.698  47.585  26.104 1.00 12.25 ? 62  LEU C CD2 1 
ATOM   2687 N N   . THR C 1 46  ? 38.236  47.963  22.280 1.00 8.56  ? 63  THR C N   1 
ATOM   2688 C CA  . THR C 1 46  ? 38.842  49.255  22.012 1.00 10.01 ? 63  THR C CA  1 
ATOM   2689 C C   . THR C 1 46  ? 37.730  50.199  21.585 1.00 10.31 ? 63  THR C C   1 
ATOM   2690 O O   . THR C 1 46  ? 36.578  49.798  21.426 1.00 10.64 ? 63  THR C O   1 
ATOM   2691 C CB  . THR C 1 46  ? 39.961  49.136  20.974 1.00 11.91 ? 63  THR C CB  1 
ATOM   2692 O OG1 . THR C 1 46  ? 40.678  50.372  20.938 1.00 12.14 ? 63  THR C OG1 1 
ATOM   2693 C CG2 . THR C 1 46  ? 39.418  48.824  19.596 1.00 12.97 ? 63  THR C CG2 1 
ATOM   2694 N N   . ILE C 1 47  ? 38.063  51.474  21.462 1.00 9.83  ? 64  ILE C N   1 
ATOM   2695 C CA  . ILE C 1 47  ? 37.197  52.434  20.790 1.00 11.05 ? 64  ILE C CA  1 
ATOM   2696 C C   . ILE C 1 47  ? 37.818  52.721  19.436 1.00 10.68 ? 64  ILE C C   1 
ATOM   2697 O O   . ILE C 1 47  ? 38.951  53.200  19.352 1.00 11.11 ? 64  ILE C O   1 
ATOM   2698 C CB  . ILE C 1 47  ? 36.981  53.699  21.632 1.00 11.34 ? 64  ILE C CB  1 
ATOM   2699 C CG1 . ILE C 1 47  ? 36.162  53.335  22.888 1.00 13.86 ? 64  ILE C CG1 1 
ATOM   2700 C CG2 . ILE C 1 47  ? 36.278  54.769  20.814 1.00 11.59 ? 64  ILE C CG2 1 
ATOM   2701 C CD1 . ILE C 1 47  ? 35.996  54.469  23.859 1.00 16.48 ? 64  ILE C CD1 1 
ATOM   2702 N N   . ALA C 1 48  ? 37.098  52.393  18.376 1.00 9.66  ? 65  ALA C N   1 
ATOM   2703 C CA  . ALA C 1 48  ? 37.650  52.513  17.038 1.00 10.58 ? 65  ALA C CA  1 
ATOM   2704 C C   . ALA C 1 48  ? 37.786  53.983  16.689 1.00 11.74 ? 65  ALA C C   1 
ATOM   2705 O O   . ALA C 1 48  ? 36.926  54.797  17.031 1.00 13.21 ? 65  ALA C O   1 
ATOM   2706 C CB  . ALA C 1 48  ? 36.732  51.819  16.032 1.00 11.68 ? 65  ALA C CB  1 
ATOM   2707 N N   . THR C 1 49  ? 38.881  54.322  16.030 1.00 11.92 ? 66  THR C N   1 
ATOM   2708 C CA  . THR C 1 49  ? 39.153  55.670  15.587 1.00 13.69 ? 66  THR C CA  1 
ATOM   2709 C C   . THR C 1 49  ? 38.953  55.780  14.082 1.00 13.18 ? 66  THR C C   1 
ATOM   2710 O O   . THR C 1 49  ? 39.061  54.786  13.355 1.00 12.78 ? 66  THR C O   1 
ATOM   2711 C CB  . THR C 1 49  ? 40.607  56.044  15.899 1.00 15.14 ? 66  THR C CB  1 
ATOM   2712 O OG1 . THR C 1 49  ? 41.480  55.149  15.190 1.00 13.54 ? 66  THR C OG1 1 
ATOM   2713 C CG2 . THR C 1 49  ? 40.870  55.967  17.403 1.00 18.40 ? 66  THR C CG2 1 
ATOM   2714 N N   . PRO C 1 50  ? 38.647  56.974  13.584 1.00 15.44 ? 67  PRO C N   1 
ATOM   2715 C CA  . PRO C 1 50  ? 38.596  57.150  12.127 1.00 17.60 ? 67  PRO C CA  1 
ATOM   2716 C C   . PRO C 1 50  ? 39.880  56.749  11.435 1.00 17.30 ? 67  PRO C C   1 
ATOM   2717 O O   . PRO C 1 50  ? 39.827  56.223  10.320 1.00 19.98 ? 67  PRO C O   1 
ATOM   2718 C CB  . PRO C 1 50  ? 38.300  58.649  11.969 1.00 18.31 ? 67  PRO C CB  1 
ATOM   2719 C CG  . PRO C 1 50  ? 37.564  59.003  13.185 1.00 20.13 ? 67  PRO C CG  1 
ATOM   2720 C CD  . PRO C 1 50  ? 38.165  58.170  14.297 1.00 18.55 ? 67  PRO C CD  1 
ATOM   2721 N N   . ALA C 1 51  ? 41.036  56.961  12.064 1.00 15.74 ? 68  ALA C N   1 
ATOM   2722 C CA  . ALA C 1 51  ? 42.294  56.626  11.405 1.00 17.83 ? 68  ALA C CA  1 
ATOM   2723 C C   . ALA C 1 51  ? 42.397  55.131  11.130 1.00 18.30 ? 68  ALA C C   1 
ATOM   2724 O O   . ALA C 1 51  ? 42.829  54.720  10.049 1.00 21.24 ? 68  ALA C O   1 
ATOM   2725 C CB  . ALA C 1 51  ? 43.469  57.089  12.260 1.00 20.16 ? 68  ALA C CB  1 
ATOM   2726 N N   . ILE C 1 52  ? 42.027  54.297  12.101 1.00 15.71 ? 69  ILE C N   1 
ATOM   2727 C CA  . ILE C 1 52  ? 42.087  52.857  11.877 1.00 12.99 ? 69  ILE C CA  1 
ATOM   2728 C C   . ILE C 1 52  ? 40.952  52.409  10.971 1.00 11.28 ? 69  ILE C C   1 
ATOM   2729 O O   . ILE C 1 52  ? 41.134  51.538  10.115 1.00 11.77 ? 69  ILE C O   1 
ATOM   2730 C CB  . ILE C 1 52  ? 42.137  52.093  13.211 1.00 13.90 ? 69  ILE C CB  1 
ATOM   2731 C CG1 . ILE C 1 52  ? 42.489  50.630  12.980 1.00 18.68 ? 69  ILE C CG1 1 
ATOM   2732 C CG2 . ILE C 1 52  ? 40.816  52.193  13.953 1.00 17.53 ? 69  ILE C CG2 1 
ATOM   2733 C CD1 . ILE C 1 52  ? 43.116  49.971  14.219 1.00 22.37 ? 69  ILE C CD1 1 
ATOM   2734 N N   . LEU C 1 53  ? 39.773  53.016  11.122 1.00 10.23 ? 70  LEU C N   1 
ATOM   2735 C CA  . LEU C 1 53  ? 38.622  52.606  10.316 1.00 10.22 ? 70  LEU C CA  1 
ATOM   2736 C C   . LEU C 1 53  ? 38.832  52.929  8.842  1.00 11.28 ? 70  LEU C C   1 
ATOM   2737 O O   . LEU C 1 53  ? 38.394  52.171  7.974  1.00 11.39 ? 70  LEU C O   1 
ATOM   2738 C CB  . LEU C 1 53  ? 37.342  53.255  10.834 1.00 11.83 ? 70  LEU C CB  1 
ATOM   2739 C CG  . LEU C 1 53  ? 36.873  52.768  12.198 1.00 10.18 ? 70  LEU C CG  1 
ATOM   2740 C CD1 . LEU C 1 53  ? 35.822  53.700  12.747 1.00 12.19 ? 70  LEU C CD1 1 
ATOM   2741 C CD2 . LEU C 1 53  ? 36.309  51.362  12.070 1.00 11.99 ? 70  LEU C CD2 1 
ATOM   2742 N N   . GLU C 1 54  ? 39.490  54.050  8.540  1.00 13.11 ? 71  GLU C N   1 
ATOM   2743 C CA  . GLU C 1 54  ? 39.778  54.390  7.151  1.00 14.80 ? 71  GLU C CA  1 
ATOM   2744 C C   . GLU C 1 54  ? 40.648  53.325  6.491  1.00 13.93 ? 71  GLU C C   1 
ATOM   2745 O O   . GLU C 1 54  ? 40.471  53.016  5.303  1.00 15.91 ? 71  GLU C O   1 
ATOM   2746 C CB  . GLU C 1 54  ? 40.479  55.746  7.092  1.00 19.35 ? 71  GLU C CB  1 
ATOM   2747 C CG  . GLU C 1 54  ? 39.580  56.943  7.315  1.00 29.47 ? 71  GLU C CG  1 
ATOM   2748 C CD  . GLU C 1 54  ? 40.352  58.258  7.227  1.00 36.86 ? 71  GLU C CD  1 
ATOM   2749 O OE1 . GLU C 1 54  ? 41.490  58.247  6.705  1.00 35.19 ? 71  GLU C OE1 1 
ATOM   2750 O OE2 . GLU C 1 54  ? 39.821  59.299  7.679  1.00 42.96 ? 71  GLU C OE2 1 
ATOM   2751 N N   . GLU C 1 55  ? 41.621  52.771  7.234  1.00 13.56 ? 72  GLU C N   1 
ATOM   2752 C CA  A GLU C 1 55  ? 42.429  51.684  6.688  0.59 14.26 ? 72  GLU C CA  1 
ATOM   2753 C CA  B GLU C 1 55  ? 42.437  51.679  6.705  0.41 14.21 ? 72  GLU C CA  1 
ATOM   2754 C C   . GLU C 1 55  ? 41.641  50.380  6.636  1.00 13.38 ? 72  GLU C C   1 
ATOM   2755 O O   . GLU C 1 55  ? 41.754  49.616  5.667  1.00 13.81 ? 72  GLU C O   1 
ATOM   2756 C CB  A GLU C 1 55  ? 43.705  51.512  7.510  0.59 15.48 ? 72  GLU C CB  1 
ATOM   2757 C CB  B GLU C 1 55  ? 43.670  51.459  7.586  0.41 15.46 ? 72  GLU C CB  1 
ATOM   2758 C CG  A GLU C 1 55  ? 44.652  50.463  6.942  0.59 18.94 ? 72  GLU C CG  1 
ATOM   2759 C CG  B GLU C 1 55  ? 44.481  52.700  7.942  0.41 17.35 ? 72  GLU C CG  1 
ATOM   2760 C CD  A GLU C 1 55  ? 46.075  50.615  7.449  0.59 19.69 ? 72  GLU C CD  1 
ATOM   2761 C CD  B GLU C 1 55  ? 45.548  52.403  8.989  0.41 19.24 ? 72  GLU C CD  1 
ATOM   2762 O OE1 A GLU C 1 55  ? 46.317  51.520  8.272  0.59 22.13 ? 72  GLU C OE1 1 
ATOM   2763 O OE1 B GLU C 1 55  ? 46.504  51.661  8.673  0.41 22.32 ? 72  GLU C OE1 1 
ATOM   2764 O OE2 A GLU C 1 55  ? 46.951  49.832  7.014  0.59 18.92 ? 72  GLU C OE2 1 
ATOM   2765 O OE2 B GLU C 1 55  ? 45.422  52.892  10.137 0.41 18.16 ? 72  GLU C OE2 1 
ATOM   2766 N N   . HIS C 1 56  ? 40.845  50.099  7.667  1.00 10.71 ? 73  HIS C N   1 
ATOM   2767 C CA  . HIS C 1 56  ? 40.010  48.907  7.662  1.00 10.43 ? 73  HIS C CA  1 
ATOM   2768 C C   . HIS C 1 56  ? 39.119  48.883  6.426  1.00 9.72  ? 73  HIS C C   1 
ATOM   2769 O O   . HIS C 1 56  ? 38.985  47.853  5.755  1.00 10.78 ? 73  HIS C O   1 
ATOM   2770 C CB  . HIS C 1 56  ? 39.142  48.898  8.922  1.00 9.55  ? 73  HIS C CB  1 
ATOM   2771 C CG  . HIS C 1 56  ? 38.254  47.699  9.032  1.00 10.48 ? 73  HIS C CG  1 
ATOM   2772 N ND1 . HIS C 1 56  ? 38.723  46.450  9.375  1.00 10.63 ? 73  HIS C ND1 1 
ATOM   2773 C CD2 . HIS C 1 56  ? 36.918  47.562  8.842  1.00 13.23 ? 73  HIS C CD2 1 
ATOM   2774 C CE1 . HIS C 1 56  ? 37.717  45.592  9.393  1.00 12.11 ? 73  HIS C CE1 1 
ATOM   2775 N NE2 . HIS C 1 56  ? 36.612  46.240  9.069  1.00 13.10 ? 73  HIS C NE2 1 
ATOM   2776 N N   . TYR C 1 57  ? 38.500  50.021  6.115  1.00 9.96  ? 74  TYR C N   1 
ATOM   2777 C CA  . TYR C 1 57  ? 37.582  50.156  4.993  1.00 11.58 ? 74  TYR C CA  1 
ATOM   2778 C C   . TYR C 1 57  ? 38.257  50.768  3.773  1.00 14.45 ? 74  TYR C C   1 
ATOM   2779 O O   . TYR C 1 57  ? 37.608  51.465  3.000  1.00 16.16 ? 74  TYR C O   1 
ATOM   2780 C CB  . TYR C 1 57  ? 36.349  50.959  5.417  1.00 9.70  ? 74  TYR C CB  1 
ATOM   2781 C CG  . TYR C 1 57  ? 35.437  50.251  6.397  1.00 12.69 ? 74  TYR C CG  1 
ATOM   2782 C CD1 . TYR C 1 57  ? 34.748  49.103  6.035  1.00 14.57 ? 74  TYR C CD1 1 
ATOM   2783 C CD2 . TYR C 1 57  ? 35.249  50.741  7.691  1.00 14.72 ? 74  TYR C CD2 1 
ATOM   2784 C CE1 . TYR C 1 57  ? 33.899  48.452  6.940  1.00 15.04 ? 74  TYR C CE1 1 
ATOM   2785 C CE2 . TYR C 1 57  ? 34.419  50.096  8.602  1.00 15.83 ? 74  TYR C CE2 1 
ATOM   2786 C CZ  . TYR C 1 57  ? 33.743  48.950  8.217  1.00 17.07 ? 74  TYR C CZ  1 
ATOM   2787 O OH  . TYR C 1 57  ? 32.904  48.305  9.110  1.00 16.29 ? 74  TYR C OH  1 
ATOM   2788 N N   . ALA C 1 58  ? 39.559  50.509  3.587  1.00 13.65 ? 75  ALA C N   1 
ATOM   2789 C CA  . ALA C 1 58  ? 40.292  51.095  2.467  1.00 15.10 ? 75  ALA C CA  1 
ATOM   2790 C C   . ALA C 1 58  ? 39.662  50.768  1.119  1.00 15.62 ? 75  ALA C C   1 
ATOM   2791 O O   . ALA C 1 58  ? 39.765  51.573  0.188  1.00 17.37 ? 75  ALA C O   1 
ATOM   2792 C CB  . ALA C 1 58  ? 41.750  50.622  2.482  1.00 17.10 ? 75  ALA C CB  1 
ATOM   2793 N N   . GLU C 1 59  ? 39.024  49.603  0.978  1.00 16.38 ? 76  GLU C N   1 
ATOM   2794 C CA  . GLU C 1 59  ? 38.410  49.264  -0.304 1.00 19.56 ? 76  GLU C CA  1 
ATOM   2795 C C   . GLU C 1 59  ? 37.339  50.265  -0.710 1.00 20.45 ? 76  GLU C C   1 
ATOM   2796 O O   . GLU C 1 59  ? 37.009  50.360  -1.898 1.00 21.13 ? 76  GLU C O   1 
ATOM   2797 C CB  . GLU C 1 59  ? 37.782  47.875  -0.238 1.00 21.23 ? 76  GLU C CB  1 
ATOM   2798 C CG  . GLU C 1 59  ? 36.581  47.795  0.694  1.00 24.74 ? 76  GLU C CG  1 
ATOM   2799 C CD  . GLU C 1 59  ? 36.144  46.365  0.966  1.00 27.42 ? 76  GLU C CD  1 
ATOM   2800 O OE1 . GLU C 1 59  ? 35.496  45.761  0.076  1.00 27.66 ? 76  GLU C OE1 1 
ATOM   2801 O OE2 . GLU C 1 59  ? 36.471  45.839  2.060  1.00 25.84 ? 76  GLU C OE2 1 
ATOM   2802 N N   . HIS C 1 60  ? 36.787  51.005  0.245  1.00 19.90 ? 77  HIS C N   1 
ATOM   2803 C CA  . HIS C 1 60  ? 35.732  51.974  -0.017 1.00 19.48 ? 77  HIS C CA  1 
ATOM   2804 C C   . HIS C 1 60  ? 36.246  53.406  -0.123 1.00 20.44 ? 77  HIS C C   1 
ATOM   2805 O O   . HIS C 1 60  ? 35.441  54.338  -0.151 1.00 17.58 ? 77  HIS C O   1 
ATOM   2806 C CB  . HIS C 1 60  ? 34.678  51.901  1.086  1.00 19.07 ? 77  HIS C CB  1 
ATOM   2807 C CG  . HIS C 1 60  ? 34.033  50.559  1.212  1.00 19.64 ? 77  HIS C CG  1 
ATOM   2808 N ND1 . HIS C 1 60  ? 33.546  49.868  0.124  1.00 22.02 ? 77  HIS C ND1 1 
ATOM   2809 C CD2 . HIS C 1 60  ? 33.793  49.783  2.292  1.00 21.54 ? 77  HIS C CD2 1 
ATOM   2810 C CE1 . HIS C 1 60  ? 33.031  48.722  0.531  1.00 22.90 ? 77  HIS C CE1 1 
ATOM   2811 N NE2 . HIS C 1 60  ? 33.166  48.648  1.841  1.00 22.25 ? 77  HIS C NE2 1 
ATOM   2812 N N   . LYS C 1 61  ? 37.558  53.605  -0.176 1.00 21.11 ? 78  LYS C N   1 
ATOM   2813 C CA  . LYS C 1 61  ? 38.096  54.957  -0.221 1.00 22.54 ? 78  LYS C CA  1 
ATOM   2814 C C   . LYS C 1 61  ? 37.456  55.745  -1.355 1.00 24.17 ? 78  LYS C C   1 
ATOM   2815 O O   . LYS C 1 61  ? 37.293  55.241  -2.469 1.00 24.63 ? 78  LYS C O   1 
ATOM   2816 C CB  . LYS C 1 61  ? 39.612  54.912  -0.414 1.00 26.29 ? 78  LYS C CB  1 
ATOM   2817 C CG  . LYS C 1 61  ? 40.262  56.283  -0.351 1.00 31.27 ? 78  LYS C CG  1 
ATOM   2818 C CD  . LYS C 1 61  ? 41.773  56.183  -0.255 1.00 36.49 ? 78  LYS C CD  1 
ATOM   2819 C CE  . LYS C 1 61  ? 42.452  57.328  -0.975 1.00 40.24 ? 78  LYS C CE  1 
ATOM   2820 N NZ  . LYS C 1 61  ? 43.905  57.044  -1.153 1.00 41.97 ? 78  LYS C NZ  1 
ATOM   2821 N N   . GLY C 1 62  ? 37.052  56.976  -1.047 1.00 27.38 ? 79  GLY C N   1 
ATOM   2822 C CA  . GLY C 1 62  ? 36.517  57.882  -2.036 1.00 27.99 ? 79  GLY C CA  1 
ATOM   2823 C C   . GLY C 1 62  ? 35.072  57.653  -2.400 1.00 26.36 ? 79  GLY C C   1 
ATOM   2824 O O   . GLY C 1 62  ? 34.545  58.386  -3.248 1.00 26.81 ? 79  GLY C O   1 
ATOM   2825 N N   . LYS C 1 63  ? 34.401  56.665  -1.785 1.00 24.61 ? 80  LYS C N   1 
ATOM   2826 C CA  . LYS C 1 63  ? 33.004  56.426  -2.110 1.00 22.80 ? 80  LYS C CA  1 
ATOM   2827 C C   . LYS C 1 63  ? 32.091  57.303  -1.255 1.00 22.45 ? 80  LYS C C   1 
ATOM   2828 O O   . LYS C 1 63  ? 32.437  57.655  -0.119 1.00 19.78 ? 80  LYS C O   1 
ATOM   2829 C CB  . LYS C 1 63  ? 32.657  54.954  -1.887 1.00 24.75 ? 80  LYS C CB  1 
ATOM   2830 C CG  . LYS C 1 63  ? 33.318  54.025  -2.888 1.00 26.86 ? 80  LYS C CG  1 
ATOM   2831 C CD  . LYS C 1 63  ? 33.084  52.563  -2.566 1.00 28.55 ? 80  LYS C CD  1 
ATOM   2832 C CE  . LYS C 1 63  ? 34.039  51.686  -3.357 1.00 32.16 ? 80  LYS C CE  1 
ATOM   2833 N NZ  . LYS C 1 63  ? 33.771  50.243  -3.127 1.00 31.73 ? 80  LYS C NZ  1 
ATOM   2834 N N   . PRO C 1 64  ? 30.916  57.656  -1.791 1.00 21.38 ? 81  PRO C N   1 
ATOM   2835 C CA  . PRO C 1 64  ? 30.038  58.608  -1.085 1.00 21.97 ? 81  PRO C CA  1 
ATOM   2836 C C   . PRO C 1 64  ? 29.597  58.142  0.292  1.00 21.78 ? 81  PRO C C   1 
ATOM   2837 O O   . PRO C 1 64  ? 29.381  58.979  1.179  1.00 19.71 ? 81  PRO C O   1 
ATOM   2838 C CB  . PRO C 1 64  ? 28.832  58.752  -2.028 1.00 23.58 ? 81  PRO C CB  1 
ATOM   2839 C CG  . PRO C 1 64  ? 29.259  58.232  -3.337 1.00 25.32 ? 81  PRO C CG  1 
ATOM   2840 C CD  . PRO C 1 64  ? 30.353  57.236  -3.089 1.00 21.13 ? 81  PRO C CD  1 
ATOM   2841 N N   . PHE C 1 65  ? 29.438  56.839  0.500  1.00 19.45 ? 82  PHE C N   1 
ATOM   2842 C CA  . PHE C 1 65  ? 28.910  56.332  1.757  1.00 20.52 ? 82  PHE C CA  1 
ATOM   2843 C C   . PHE C 1 65  ? 29.975  56.158  2.832  1.00 21.37 ? 82  PHE C C   1 
ATOM   2844 O O   . PHE C 1 65  ? 29.626  55.882  3.983  1.00 21.81 ? 82  PHE C O   1 
ATOM   2845 C CB  . PHE C 1 65  ? 28.199  54.996  1.512  1.00 20.35 ? 82  PHE C CB  1 
ATOM   2846 C CG  . PHE C 1 65  ? 29.089  53.927  0.938  1.00 22.21 ? 82  PHE C CG  1 
ATOM   2847 C CD1 . PHE C 1 65  ? 29.955  53.219  1.753  1.00 22.41 ? 82  PHE C CD1 1 
ATOM   2848 C CD2 . PHE C 1 65  ? 29.057  53.631  -0.417 1.00 24.01 ? 82  PHE C CD2 1 
ATOM   2849 C CE1 . PHE C 1 65  ? 30.776  52.226  1.229  1.00 21.73 ? 82  PHE C CE1 1 
ATOM   2850 C CE2 . PHE C 1 65  ? 29.873  52.651  -0.945 1.00 25.23 ? 82  PHE C CE2 1 
ATOM   2851 C CZ  . PHE C 1 65  ? 30.733  51.941  -0.115 1.00 22.05 ? 82  PHE C CZ  1 
ATOM   2852 N N   . LEU C 1 66  ? 31.255  56.301  2.493  1.00 16.68 ? 83  LEU C N   1 
ATOM   2853 C CA  . LEU C 1 66  ? 32.300  55.985  3.461  1.00 14.15 ? 83  LEU C CA  1 
ATOM   2854 C C   . LEU C 1 66  ? 32.273  56.881  4.693  1.00 18.85 ? 83  LEU C C   1 
ATOM   2855 O O   . LEU C 1 66  ? 32.452  56.350  5.801  1.00 18.53 ? 83  LEU C O   1 
ATOM   2856 C CB  . LEU C 1 66  ? 33.681  55.980  2.791  1.00 14.82 ? 83  LEU C CB  1 
ATOM   2857 C CG  . LEU C 1 66  ? 34.836  55.600  3.718  1.00 15.33 ? 83  LEU C CG  1 
ATOM   2858 C CD1 . LEU C 1 66  ? 34.619  54.226  4.348  1.00 16.11 ? 83  LEU C CD1 1 
ATOM   2859 C CD2 . LEU C 1 66  ? 36.165  55.652  2.966  1.00 21.48 ? 83  LEU C CD2 1 
ATOM   2860 N N   . PRO C 1 67  ? 32.099  58.204  4.590  1.00 18.83 ? 84  PRO C N   1 
ATOM   2861 C CA  . PRO C 1 67  ? 32.104  59.021  5.812  1.00 16.98 ? 84  PRO C CA  1 
ATOM   2862 C C   . PRO C 1 67  ? 31.047  58.603  6.815  1.00 19.02 ? 84  PRO C C   1 
ATOM   2863 O O   . PRO C 1 67  ? 31.327  58.531  8.018  1.00 20.01 ? 84  PRO C O   1 
ATOM   2864 C CB  . PRO C 1 67  ? 31.877  60.446  5.285  1.00 17.30 ? 84  PRO C CB  1 
ATOM   2865 C CG  . PRO C 1 67  ? 32.364  60.415  3.894  1.00 20.37 ? 84  PRO C CG  1 
ATOM   2866 C CD  . PRO C 1 67  ? 32.005  59.040  3.382  1.00 17.05 ? 84  PRO C CD  1 
ATOM   2867 N N   . GLY C 1 68  ? 29.833  58.310  6.354  1.00 21.53 ? 85  GLY C N   1 
ATOM   2868 C CA  . GLY C 1 68  ? 28.792  57.898  7.284  1.00 22.64 ? 85  GLY C CA  1 
ATOM   2869 C C   . GLY C 1 68  ? 29.086  56.535  7.875  1.00 20.16 ? 85  GLY C C   1 
ATOM   2870 O O   . GLY C 1 68  ? 28.799  56.273  9.048  1.00 21.41 ? 85  GLY C O   1 
ATOM   2871 N N   . LEU C 1 69  ? 29.656  55.648  7.062  1.00 18.40 ? 86  LEU C N   1 
ATOM   2872 C CA  . LEU C 1 69  ? 30.054  54.329  7.535  1.00 17.38 ? 86  LEU C CA  1 
ATOM   2873 C C   . LEU C 1 69  ? 31.076  54.442  8.658  1.00 17.64 ? 86  LEU C C   1 
ATOM   2874 O O   . LEU C 1 69  ? 30.956  53.766  9.688  1.00 18.21 ? 86  LEU C O   1 
ATOM   2875 C CB  . LEU C 1 69  ? 30.611  53.562  6.341  1.00 18.89 ? 86  LEU C CB  1 
ATOM   2876 C CG  . LEU C 1 69  ? 30.904  52.068  6.423  1.00 23.52 ? 86  LEU C CG  1 
ATOM   2877 C CD1 . LEU C 1 69  ? 31.044  51.504  5.020  1.00 24.66 ? 86  LEU C CD1 1 
ATOM   2878 C CD2 . LEU C 1 69  ? 32.152  51.820  7.206  1.00 29.20 ? 86  LEU C CD2 1 
ATOM   2879 N N   . ILE C 1 70  ? 32.077  55.312  8.490  1.00 15.96 ? 87  ILE C N   1 
ATOM   2880 C CA  A ILE C 1 70  ? 33.080  55.503  9.534  0.61 16.07 ? 87  ILE C CA  1 
ATOM   2881 C CA  B ILE C 1 70  ? 33.082  55.509  9.532  0.39 16.08 ? 87  ILE C CA  1 
ATOM   2882 C C   . ILE C 1 70  ? 32.446  56.087  10.791 1.00 16.46 ? 87  ILE C C   1 
ATOM   2883 O O   . ILE C 1 70  ? 32.802  55.709  11.910 1.00 16.31 ? 87  ILE C O   1 
ATOM   2884 C CB  A ILE C 1 70  ? 34.243  56.369  9.013  0.61 18.09 ? 87  ILE C CB  1 
ATOM   2885 C CB  B ILE C 1 70  ? 34.227  56.406  9.020  0.39 17.03 ? 87  ILE C CB  1 
ATOM   2886 C CG1 A ILE C 1 70  ? 35.128  55.565  8.055  0.61 21.49 ? 87  ILE C CG1 1 
ATOM   2887 C CG1 B ILE C 1 70  ? 34.994  55.742  7.867  0.39 19.51 ? 87  ILE C CG1 1 
ATOM   2888 C CG2 A ILE C 1 70  ? 35.078  56.902  10.177 0.61 18.38 ? 87  ILE C CG2 1 
ATOM   2889 C CG2 B ILE C 1 70  ? 35.166  56.777  10.169 0.39 16.68 ? 87  ILE C CG2 1 
ATOM   2890 C CD1 A ILE C 1 70  ? 36.027  56.422  7.189  0.61 22.92 ? 87  ILE C CD1 1 
ATOM   2891 C CD1 B ILE C 1 70  ? 35.289  54.275  8.056  0.39 19.15 ? 87  ILE C CD1 1 
ATOM   2892 N N   . GLU C 1 71  ? 31.514  57.035  10.629 1.00 17.68 ? 88  GLU C N   1 
ATOM   2893 C CA  . GLU C 1 71  ? 30.899  57.668  11.796 1.00 18.71 ? 88  GLU C CA  1 
ATOM   2894 C C   . GLU C 1 71  ? 30.142  56.652  12.638 1.00 17.28 ? 88  GLU C C   1 
ATOM   2895 O O   . GLU C 1 71  ? 30.255  56.651  13.870 1.00 18.86 ? 88  GLU C O   1 
ATOM   2896 C CB  . GLU C 1 71  ? 29.976  58.810  11.368 1.00 26.43 ? 88  GLU C CB  1 
ATOM   2897 C CG  . GLU C 1 71  ? 30.749  60.047  10.912 1.00 36.20 ? 88  GLU C CG  1 
ATOM   2898 C CD  . GLU C 1 71  ? 29.858  61.186  10.421 1.00 43.75 ? 88  GLU C CD  1 
ATOM   2899 O OE1 . GLU C 1 71  ? 28.667  60.936  10.112 1.00 46.76 ? 88  GLU C OE1 1 
ATOM   2900 O OE2 . GLU C 1 71  ? 30.360  62.335  10.339 1.00 44.42 ? 88  GLU C OE2 1 
ATOM   2901 N N   . LYS C 1 72  ? 29.387  55.756  11.992 1.00 17.61 ? 89  LYS C N   1 
ATOM   2902 C CA  . LYS C 1 72  ? 28.641  54.756  12.744 1.00 16.84 ? 89  LYS C CA  1 
ATOM   2903 C C   . LYS C 1 72  ? 29.569  53.783  13.459 1.00 13.63 ? 89  LYS C C   1 
ATOM   2904 O O   . LYS C 1 72  ? 29.201  53.241  14.505 1.00 15.96 ? 89  LYS C O   1 
ATOM   2905 C CB  . LYS C 1 72  ? 27.671  53.994  11.838 1.00 17.67 ? 89  LYS C CB  1 
ATOM   2906 C CG  . LYS C 1 72  ? 26.599  54.865  11.211 1.00 22.49 ? 89  LYS C CG  1 
ATOM   2907 C CD  . LYS C 1 72  ? 25.519  55.281  12.210 1.00 27.50 ? 89  LYS C CD  1 
ATOM   2908 C CE  . LYS C 1 72  ? 24.560  56.301  11.600 1.00 30.98 ? 89  LYS C CE  1 
ATOM   2909 N NZ  . LYS C 1 72  ? 23.597  56.836  12.601 1.00 32.45 ? 89  LYS C NZ  1 
ATOM   2910 N N   . MET C 1 73  ? 30.768  53.565  12.926 1.00 12.63 ? 90  MET C N   1 
ATOM   2911 C CA  . MET C 1 73  ? 31.720  52.632  13.519 1.00 11.96 ? 90  MET C CA  1 
ATOM   2912 C C   . MET C 1 73  ? 32.643  53.290  14.534 1.00 13.16 ? 90  MET C C   1 
ATOM   2913 O O   . MET C 1 73  ? 33.463  52.592  15.144 1.00 11.14 ? 90  MET C O   1 
ATOM   2914 C CB  . MET C 1 73  ? 32.570  51.983  12.421 1.00 12.68 ? 90  MET C CB  1 
ATOM   2915 C CG  . MET C 1 73  ? 31.834  50.926  11.633 1.00 10.14 ? 90  MET C CG  1 
ATOM   2916 S SD  . MET C 1 73  ? 31.431  49.467  12.609 1.00 13.42 ? 90  MET C SD  1 
ATOM   2917 C CE  . MET C 1 73  ? 33.067  48.860  13.006 1.00 14.26 ? 90  MET C CE  1 
ATOM   2918 N N   . THR C 1 74  ? 32.529  54.600  14.747 1.00 14.34 ? 91  THR C N   1 
ATOM   2919 C CA  . THR C 1 74  ? 33.400  55.298  15.690 1.00 13.81 ? 91  THR C CA  1 
ATOM   2920 C C   . THR C 1 74  ? 32.772  55.150  17.068 1.00 13.03 ? 91  THR C C   1 
ATOM   2921 O O   . THR C 1 74  ? 31.920  55.940  17.481 1.00 17.65 ? 91  THR C O   1 
ATOM   2922 C CB  . THR C 1 74  ? 33.569  56.764  15.306 1.00 15.64 ? 91  THR C CB  1 
ATOM   2923 O OG1 . THR C 1 74  ? 34.179  56.876  14.010 1.00 17.27 ? 91  THR C OG1 1 
ATOM   2924 C CG2 . THR C 1 74  ? 34.450  57.480  16.329 1.00 16.19 ? 91  THR C CG2 1 
ATOM   2925 N N   . GLY C 1 75  ? 33.188  54.114  17.784 1.00 10.06 ? 92  GLY C N   1 
ATOM   2926 C CA  . GLY C 1 75  ? 32.626  53.792  19.075 1.00 10.87 ? 92  GLY C CA  1 
ATOM   2927 C C   . GLY C 1 75  ? 33.272  52.514  19.572 1.00 8.69  ? 92  GLY C C   1 
ATOM   2928 O O   . GLY C 1 75  ? 34.216  52.001  18.963 1.00 9.07  ? 92  GLY C O   1 
ATOM   2929 N N   . PRO C 1 76  ? 32.776  51.976  20.680 1.00 8.03  ? 93  PRO C N   1 
ATOM   2930 C CA  . PRO C 1 76  ? 33.362  50.752  21.223 1.00 7.78  ? 93  PRO C CA  1 
ATOM   2931 C C   . PRO C 1 76  ? 33.148  49.588  20.267 1.00 7.74  ? 93  PRO C C   1 
ATOM   2932 O O   . PRO C 1 76  ? 32.074  49.450  19.679 1.00 8.09  ? 93  PRO C O   1 
ATOM   2933 C CB  . PRO C 1 76  ? 32.589  50.549  22.532 1.00 8.53  ? 93  PRO C CB  1 
ATOM   2934 C CG  . PRO C 1 76  ? 31.256  51.140  22.256 1.00 11.29 ? 93  PRO C CG  1 
ATOM   2935 C CD  . PRO C 1 76  ? 31.570  52.369  21.421 1.00 9.51  ? 93  PRO C CD  1 
ATOM   2936 N N   . VAL C 1 77  ? 34.196  48.773  20.096 1.00 7.74  ? 94  VAL C N   1 
ATOM   2937 C CA  . VAL C 1 77  ? 34.144  47.565  19.276 1.00 7.33  ? 94  VAL C CA  1 
ATOM   2938 C C   . VAL C 1 77  ? 34.910  46.469  20.004 1.00 6.63  ? 94  VAL C C   1 
ATOM   2939 O O   . VAL C 1 77  ? 35.822  46.735  20.797 1.00 8.29  ? 94  VAL C O   1 
ATOM   2940 C CB  . VAL C 1 77  ? 34.719  47.770  17.857 1.00 8.71  ? 94  VAL C CB  1 
ATOM   2941 C CG1 . VAL C 1 77  ? 33.942  48.829  17.105 1.00 9.61  ? 94  VAL C CG1 1 
ATOM   2942 C CG2 . VAL C 1 77  ? 36.196  48.161  17.923 1.00 10.77 ? 94  VAL C CG2 1 
ATOM   2943 N N   . LEU C 1 78  ? 34.518  45.229  19.767 1.00 6.32  ? 95  LEU C N   1 
ATOM   2944 C CA  . LEU C 1 78  ? 35.292  44.087  20.256 1.00 6.17  ? 95  LEU C CA  1 
ATOM   2945 C C   . LEU C 1 78  ? 35.996  43.443  19.077 1.00 7.10  ? 95  LEU C C   1 
ATOM   2946 O O   . LEU C 1 78  ? 35.347  42.859  18.202 1.00 8.28  ? 95  LEU C O   1 
ATOM   2947 C CB  . LEU C 1 78  ? 34.432  43.074  21.001 1.00 7.66  ? 95  LEU C CB  1 
ATOM   2948 C CG  . LEU C 1 78  ? 35.257  42.045  21.784 1.00 6.91  ? 95  LEU C CG  1 
ATOM   2949 C CD1 . LEU C 1 78  ? 35.948  42.684  23.020 1.00 10.02 ? 95  LEU C CD1 1 
ATOM   2950 C CD2 . LEU C 1 78  ? 34.424  40.845  22.205 1.00 9.60  ? 95  LEU C CD2 1 
ATOM   2951 N N   . CYS C 1 79  ? 37.322  43.540  19.084 1.00 6.71  ? 96  CYS C N   1 
ATOM   2952 C CA  . CYS C 1 79  ? 38.171  42.931  18.067 1.00 7.23  ? 96  CYS C CA  1 
ATOM   2953 C C   . CYS C 1 79  ? 38.420  41.491  18.468 1.00 6.96  ? 96  CYS C C   1 
ATOM   2954 O O   . CYS C 1 79  ? 38.713  41.221  19.630 1.00 7.76  ? 96  CYS C O   1 
ATOM   2955 C CB  . CYS C 1 79  ? 39.530  43.640  18.057 1.00 8.57  ? 96  CYS C CB  1 
ATOM   2956 S SG  . CYS C 1 79  ? 39.482  45.437  17.884 1.00 10.13 ? 96  CYS C SG  1 
ATOM   2957 N N   . MET C 1 80  ? 38.293  40.569  17.520 1.00 7.43  ? 97  MET C N   1 
ATOM   2958 C CA  . MET C 1 80  ? 38.418  39.148  17.810 1.00 7.79  ? 97  MET C CA  1 
ATOM   2959 C C   . MET C 1 80  ? 39.134  38.450  16.666 1.00 5.70  ? 97  MET C C   1 
ATOM   2960 O O   . MET C 1 80  ? 38.978  38.818  15.502 1.00 7.16  ? 97  MET C O   1 
ATOM   2961 C CB  . MET C 1 80  ? 37.032  38.484  18.001 1.00 8.76  ? 97  MET C CB  1 
ATOM   2962 C CG  . MET C 1 80  ? 36.075  39.277  18.880 1.00 9.42  ? 97  MET C CG  1 
ATOM   2963 S SD  . MET C 1 80  ? 34.480  38.450  19.195 1.00 9.05  ? 97  MET C SD  1 
ATOM   2964 C CE  . MET C 1 80  ? 33.754  38.483  17.552 1.00 8.82  ? 97  MET C CE  1 
ATOM   2965 N N   . VAL C 1 81  ? 39.881  37.400  17.002 1.00 6.77  ? 98  VAL C N   1 
ATOM   2966 C CA  . VAL C 1 81  ? 40.372  36.442  16.020 1.00 6.57  ? 98  VAL C CA  1 
ATOM   2967 C C   . VAL C 1 81  ? 39.890  35.061  16.443 1.00 6.91  ? 98  VAL C C   1 
ATOM   2968 O O   . VAL C 1 81  ? 40.107  34.652  17.587 1.00 7.91  ? 98  VAL C O   1 
ATOM   2969 C CB  . VAL C 1 81  ? 41.904  36.481  15.895 1.00 7.15  ? 98  VAL C CB  1 
ATOM   2970 C CG1 . VAL C 1 81  ? 42.374  35.442  14.886 1.00 9.17  ? 98  VAL C CG1 1 
ATOM   2971 C CG2 . VAL C 1 81  ? 42.367  37.859  15.512 1.00 7.38  ? 98  VAL C CG2 1 
ATOM   2972 N N   . PHE C 1 82  ? 39.226  34.358  15.532 1.00 7.44  ? 99  PHE C N   1 
ATOM   2973 C CA  . PHE C 1 82  ? 38.816  32.978  15.750 1.00 7.34  ? 99  PHE C CA  1 
ATOM   2974 C C   . PHE C 1 82  ? 39.549  32.063  14.776 1.00 6.90  ? 99  PHE C C   1 
ATOM   2975 O O   . PHE C 1 82  ? 39.790  32.412  13.617 1.00 7.23  ? 99  PHE C O   1 
ATOM   2976 C CB  . PHE C 1 82  ? 37.300  32.782  15.604 1.00 7.52  ? 99  PHE C CB  1 
ATOM   2977 C CG  . PHE C 1 82  ? 36.519  33.156  16.840 1.00 8.90  ? 99  PHE C CG  1 
ATOM   2978 C CD1 . PHE C 1 82  ? 36.087  34.448  17.046 1.00 8.55  ? 99  PHE C CD1 1 
ATOM   2979 C CD2 . PHE C 1 82  ? 36.250  32.207  17.806 1.00 9.36  ? 99  PHE C CD2 1 
ATOM   2980 C CE1 . PHE C 1 82  ? 35.369  34.781  18.183 1.00 10.10 ? 99  PHE C CE1 1 
ATOM   2981 C CE2 . PHE C 1 82  ? 35.563  32.541  18.951 1.00 8.91  ? 99  PHE C CE2 1 
ATOM   2982 C CZ  . PHE C 1 82  ? 35.113  33.833  19.132 1.00 10.61 ? 99  PHE C CZ  1 
ATOM   2983 N N   . GLU C 1 83  ? 39.832  30.854  15.240 1.00 8.28  ? 100 GLU C N   1 
ATOM   2984 C CA  . GLU C 1 83  ? 40.546  29.864  14.453 1.00 7.83  ? 100 GLU C CA  1 
ATOM   2985 C C   . GLU C 1 83  ? 39.696  28.622  14.278 1.00 7.54  ? 100 GLU C C   1 
ATOM   2986 O O   . GLU C 1 83  ? 39.073  28.148  15.232 1.00 8.96  ? 100 GLU C O   1 
ATOM   2987 C CB  . GLU C 1 83  ? 41.827  29.453  15.162 1.00 9.14  ? 100 GLU C CB  1 
ATOM   2988 C CG  . GLU C 1 83  ? 42.617  28.365  14.456 1.00 10.09 ? 100 GLU C CG  1 
ATOM   2989 C CD  . GLU C 1 83  ? 43.857  28.011  15.225 1.00 12.15 ? 100 GLU C CD  1 
ATOM   2990 O OE1 . GLU C 1 83  ? 43.787  27.111  16.093 1.00 12.67 ? 100 GLU C OE1 1 
ATOM   2991 O OE2 . GLU C 1 83  ? 44.877  28.671  14.985 1.00 14.63 ? 100 GLU C OE2 1 
ATOM   2992 N N   . GLY C 1 84  ? 39.711  28.076  13.070 1.00 7.30  ? 101 GLY C N   1 
ATOM   2993 C CA  . GLY C 1 84  ? 39.037  26.817  12.809 1.00 7.36  ? 101 GLY C CA  1 
ATOM   2994 C C   . GLY C 1 84  ? 39.183  26.415  11.359 1.00 7.02  ? 101 GLY C C   1 
ATOM   2995 O O   . GLY C 1 84  ? 39.750  27.136  10.537 1.00 8.33  ? 101 GLY C O   1 
ATOM   2996 N N   . VAL C 1 85  ? 38.612  25.252  11.045 1.00 8.38  ? 102 VAL C N   1 
ATOM   2997 C CA  . VAL C 1 85  ? 38.592  24.793  9.663  1.00 8.39  ? 102 VAL C CA  1 
ATOM   2998 C C   . VAL C 1 85  ? 37.683  25.708  8.858  1.00 8.98  ? 102 VAL C C   1 
ATOM   2999 O O   . VAL C 1 85  ? 36.499  25.872  9.181  1.00 8.67  ? 102 VAL C O   1 
ATOM   3000 C CB  . VAL C 1 85  ? 38.143  23.327  9.572  1.00 9.67  ? 102 VAL C CB  1 
ATOM   3001 C CG1 . VAL C 1 85  ? 38.065  22.893  8.114  1.00 10.84 ? 102 VAL C CG1 1 
ATOM   3002 C CG2 . VAL C 1 85  ? 39.107  22.431  10.329 1.00 12.87 ? 102 VAL C CG2 1 
ATOM   3003 N N   . ASP C 1 86  ? 38.227  26.292  7.782  1.00 8.31  ? 103 ASP C N   1 
ATOM   3004 C CA  . ASP C 1 86  ? 37.423  27.069  6.842  1.00 7.88  ? 103 ASP C CA  1 
ATOM   3005 C C   . ASP C 1 86  ? 36.728  28.228  7.553  1.00 7.57  ? 103 ASP C C   1 
ATOM   3006 O O   . ASP C 1 86  ? 35.666  28.681  7.134  1.00 8.34  ? 103 ASP C O   1 
ATOM   3007 C CB  . ASP C 1 86  ? 36.423  26.148  6.128  1.00 9.78  ? 103 ASP C CB  1 
ATOM   3008 C CG  . ASP C 1 86  ? 35.721  26.791  4.943  1.00 11.43 ? 103 ASP C CG  1 
ATOM   3009 O OD1 . ASP C 1 86  ? 36.371  27.531  4.175  1.00 12.34 ? 103 ASP C OD1 1 
ATOM   3010 O OD2 . ASP C 1 86  ? 34.518  26.469  4.734  1.00 13.38 ? 103 ASP C OD2 1 
ATOM   3011 N N   . VAL C 1 87  ? 37.329  28.740  8.638  1.00 6.78  ? 104 VAL C N   1 
ATOM   3012 C CA  . VAL C 1 87  ? 36.584  29.648  9.518  1.00 7.24  ? 104 VAL C CA  1 
ATOM   3013 C C   . VAL C 1 87  ? 36.283  30.985  8.848  1.00 6.78  ? 104 VAL C C   1 
ATOM   3014 O O   . VAL C 1 87  ? 35.309  31.656  9.220  1.00 6.59  ? 104 VAL C O   1 
ATOM   3015 C CB  . VAL C 1 87  ? 37.271  29.828  10.887 1.00 7.11  ? 104 VAL C CB  1 
ATOM   3016 C CG1 . VAL C 1 87  ? 38.526  30.646  10.754 1.00 7.23  ? 104 VAL C CG1 1 
ATOM   3017 C CG2 . VAL C 1 87  ? 36.317  30.473  11.913 1.00 8.91  ? 104 VAL C CG2 1 
ATOM   3018 N N   . ILE C 1 88  ? 37.074  31.397  7.858  1.00 7.73  ? 105 ILE C N   1 
ATOM   3019 C CA  . ILE C 1 88  ? 36.780  32.671  7.199  1.00 8.89  ? 105 ILE C CA  1 
ATOM   3020 C C   . ILE C 1 88  ? 35.427  32.606  6.496  1.00 7.49  ? 105 ILE C C   1 
ATOM   3021 O O   . ILE C 1 88  ? 34.531  33.420  6.755  1.00 8.49  ? 105 ILE C O   1 
ATOM   3022 C CB  . ILE C 1 88  ? 37.910  33.057  6.227  1.00 7.46  ? 105 ILE C CB  1 
ATOM   3023 C CG1 . ILE C 1 88  ? 39.213  33.280  6.986  1.00 8.17  ? 105 ILE C CG1 1 
ATOM   3024 C CG2 . ILE C 1 88  ? 37.511  34.307  5.419  1.00 9.34  ? 105 ILE C CG2 1 
ATOM   3025 C CD1 . ILE C 1 88  ? 40.447  33.373  6.067  1.00 9.11  ? 105 ILE C CD1 1 
ATOM   3026 N N   . ALA C 1 89  ? 35.241  31.600  5.630  1.00 7.62  ? 106 ALA C N   1 
ATOM   3027 C CA  . ALA C 1 89  ? 33.980  31.473  4.912  1.00 8.51  ? 106 ALA C CA  1 
ATOM   3028 C C   . ALA C 1 89  ? 32.860  31.050  5.853  1.00 7.80  ? 106 ALA C C   1 
ATOM   3029 O O   . ALA C 1 89  ? 31.718  31.484  5.701  1.00 8.36  ? 106 ALA C O   1 
ATOM   3030 C CB  . ALA C 1 89  ? 34.131  30.476  3.770  1.00 9.48  ? 106 ALA C CB  1 
ATOM   3031 N N   . GLN C 1 90  ? 33.164  30.194  6.824  1.00 7.10  ? 107 GLN C N   1 
ATOM   3032 C CA  . GLN C 1 90  ? 32.124  29.729  7.733  1.00 7.53  ? 107 GLN C CA  1 
ATOM   3033 C C   . GLN C 1 90  ? 31.599  30.867  8.601  1.00 7.08  ? 107 GLN C C   1 
ATOM   3034 O O   . GLN C 1 90  ? 30.396  30.949  8.851  1.00 6.73  ? 107 GLN C O   1 
ATOM   3035 C CB  . GLN C 1 90  ? 32.616  28.560  8.576  1.00 7.79  ? 107 GLN C CB  1 
ATOM   3036 C CG  . GLN C 1 90  ? 32.787  27.296  7.760  1.00 8.03  ? 107 GLN C CG  1 
ATOM   3037 C CD  . GLN C 1 90  ? 31.484  26.780  7.208  1.00 9.54  ? 107 GLN C CD  1 
ATOM   3038 O OE1 . GLN C 1 90  ? 30.540  26.552  7.954  1.00 9.46  ? 107 GLN C OE1 1 
ATOM   3039 N NE2 . GLN C 1 90  ? 31.428  26.577  5.892  1.00 10.96 ? 107 GLN C NE2 1 
ATOM   3040 N N   . ALA C 1 91  ? 32.485  31.739  9.090  1.00 7.31  ? 108 ALA C N   1 
ATOM   3041 C CA  . ALA C 1 91  ? 32.013  32.867  9.887  1.00 6.35  ? 108 ALA C CA  1 
ATOM   3042 C C   . ALA C 1 91  ? 31.125  33.786  9.064  1.00 7.39  ? 108 ALA C C   1 
ATOM   3043 O O   . ALA C 1 91  ? 30.123  34.305  9.569  1.00 7.30  ? 108 ALA C O   1 
ATOM   3044 C CB  . ALA C 1 91  ? 33.179  33.647  10.491 1.00 8.13  ? 108 ALA C CB  1 
ATOM   3045 N N   . ARG C 1 92  ? 31.492  34.031  7.800  1.00 8.17  ? 109 ARG C N   1 
ATOM   3046 C CA  . ARG C 1 92  ? 30.644  34.838  6.926  1.00 8.00  ? 109 ARG C CA  1 
ATOM   3047 C C   . ARG C 1 92  ? 29.275  34.203  6.749  1.00 6.35  ? 109 ARG C C   1 
ATOM   3048 O O   . ARG C 1 92  ? 28.250  34.900  6.775  1.00 8.87  ? 109 ARG C O   1 
ATOM   3049 C CB  . ARG C 1 92  ? 31.321  35.031  5.570  1.00 8.96  ? 109 ARG C CB  1 
ATOM   3050 C CG  . ARG C 1 92  ? 32.613  35.841  5.662  1.00 10.32 ? 109 ARG C CG  1 
ATOM   3051 C CD  . ARG C 1 92  ? 32.312  37.328  5.786  1.00 10.64 ? 109 ARG C CD  1 
ATOM   3052 N NE  . ARG C 1 92  ? 31.764  37.859  4.549  1.00 10.62 ? 109 ARG C NE  1 
ATOM   3053 C CZ  . ARG C 1 92  ? 31.477  39.138  4.359  1.00 12.20 ? 109 ARG C CZ  1 
ATOM   3054 N NH1 . ARG C 1 92  ? 31.693  40.042  5.303  1.00 15.32 ? 109 ARG C NH1 1 
ATOM   3055 N NH2 . ARG C 1 92  ? 30.975  39.521  3.190  1.00 17.92 ? 109 ARG C NH2 1 
ATOM   3056 N N   . LYS C 1 93  ? 29.240  32.882  6.583  1.00 7.24  ? 110 LYS C N   1 
ATOM   3057 C CA  . LYS C 1 93  ? 27.972  32.168  6.469  1.00 9.31  ? 110 LYS C CA  1 
ATOM   3058 C C   . LYS C 1 93  ? 27.137  32.304  7.741  1.00 5.95  ? 110 LYS C C   1 
ATOM   3059 O O   . LYS C 1 93  ? 25.913  32.501  7.678  1.00 8.62  ? 110 LYS C O   1 
ATOM   3060 C CB  . LYS C 1 93  ? 28.272  30.699  6.178  1.00 7.48  ? 110 LYS C CB  1 
ATOM   3061 C CG  . LYS C 1 93  ? 27.061  29.845  5.973  1.00 9.02  ? 110 LYS C CG  1 
ATOM   3062 C CD  . LYS C 1 93  ? 27.478  28.422  5.634  1.00 10.76 ? 110 LYS C CD  1 
ATOM   3063 C CE  . LYS C 1 93  ? 26.265  27.507  5.629  1.00 11.90 ? 110 LYS C CE  1 
ATOM   3064 N NZ  . LYS C 1 93  ? 26.648  26.143  5.192  1.00 11.70 ? 110 LYS C NZ  1 
ATOM   3065 N N   . MET C 1 94  ? 27.790  32.244  8.905  1.00 6.74  ? 111 MET C N   1 
ATOM   3066 C CA  . MET C 1 94  ? 27.090  32.367  10.177 1.00 6.77  ? 111 MET C CA  1 
ATOM   3067 C C   . MET C 1 94  ? 26.588  33.780  10.409 1.00 6.70  ? 111 MET C C   1 
ATOM   3068 O O   . MET C 1 94  ? 25.552  33.968  11.055 1.00 8.23  ? 111 MET C O   1 
ATOM   3069 C CB  . MET C 1 94  ? 28.022  31.965  11.319 1.00 7.81  ? 111 MET C CB  1 
ATOM   3070 C CG  . MET C 1 94  ? 28.397  30.511  11.308 1.00 7.95  ? 111 MET C CG  1 
ATOM   3071 S SD  . MET C 1 94  ? 29.812  30.128  12.365 1.00 8.69  ? 111 MET C SD  1 
ATOM   3072 C CE  . MET C 1 94  ? 29.066  30.228  13.994 1.00 10.96 ? 111 MET C CE  1 
ATOM   3073 N N   . MET C 1 95  ? 27.313  34.782  9.911  1.00 7.77  ? 112 MET C N   1 
ATOM   3074 C CA  . MET C 1 95  ? 26.872  36.161  10.040 1.00 7.23  ? 112 MET C CA  1 
ATOM   3075 C C   . MET C 1 95  ? 25.636  36.409  9.204  1.00 7.21  ? 112 MET C C   1 
ATOM   3076 O O   . MET C 1 95  ? 24.704  37.105  9.644  1.00 8.84  ? 112 MET C O   1 
ATOM   3077 C CB  . MET C 1 95  ? 27.979  37.087  9.546  1.00 8.04  ? 112 MET C CB  1 
ATOM   3078 C CG  . MET C 1 95  ? 29.189  37.191  10.446 1.00 10.99 ? 112 MET C CG  1 
ATOM   3079 S SD  . MET C 1 95  ? 30.593  38.006  9.647  1.00 12.35 ? 112 MET C SD  1 
ATOM   3080 C CE  . MET C 1 95  ? 29.867  39.469  8.926  1.00 12.15 ? 112 MET C CE  1 
ATOM   3081 N N   . GLY C 1 96  ? 25.602  35.851  7.997  1.00 8.18  ? 113 GLY C N   1 
ATOM   3082 C CA  . GLY C 1 96  ? 24.521  36.103  7.064  1.00 9.17  ? 113 GLY C CA  1 
ATOM   3083 C C   . GLY C 1 96  ? 24.785  37.323  6.204  1.00 9.16  ? 113 GLY C C   1 
ATOM   3084 O O   . GLY C 1 96  ? 25.720  38.098  6.423  1.00 10.31 ? 113 GLY C O   1 
ATOM   3085 N N   . SER C 1 97  ? 23.899  37.516  5.233  1.00 8.69  ? 114 SER C N   1 
ATOM   3086 C CA  . SER C 1 97  ? 23.979  38.627  4.294  1.00 11.14 ? 114 SER C CA  1 
ATOM   3087 C C   . SER C 1 97  ? 24.094  39.977  4.992  1.00 9.40  ? 114 SER C C   1 
ATOM   3088 O O   . SER C 1 97  ? 23.530  40.197  6.067  1.00 9.52  ? 114 SER C O   1 
ATOM   3089 C CB  . SER C 1 97  ? 22.699  38.688  3.444  1.00 12.71 ? 114 SER C CB  1 
ATOM   3090 O OG  . SER C 1 97  ? 22.380  37.454  2.867  1.00 16.32 ? 114 SER C OG  1 
ATOM   3091 N N   . THR C 1 98  ? 24.730  40.921  4.281  1.00 9.27  ? 115 THR C N   1 
ATOM   3092 C CA  A THR C 1 98  ? 24.895  42.272  4.804  0.22 9.95  ? 115 THR C CA  1 
ATOM   3093 C CA  B THR C 1 98  ? 24.891  42.289  4.761  0.78 10.48 ? 115 THR C CA  1 
ATOM   3094 C C   . THR C 1 98  ? 23.557  42.895  5.187  1.00 7.84  ? 115 THR C C   1 
ATOM   3095 O O   . THR C 1 98  ? 23.464  43.566  6.218  1.00 8.84  ? 115 THR C O   1 
ATOM   3096 C CB  A THR C 1 98  ? 25.652  43.154  3.801  0.22 12.46 ? 115 THR C CB  1 
ATOM   3097 C CB  B THR C 1 98  ? 25.507  43.121  3.627  0.78 13.25 ? 115 THR C CB  1 
ATOM   3098 O OG1 A THR C 1 98  ? 25.608  44.525  4.226  0.22 14.94 ? 115 THR C OG1 1 
ATOM   3099 O OG1 B THR C 1 98  ? 26.734  42.513  3.186  0.78 14.44 ? 115 THR C OG1 1 
ATOM   3100 C CG2 A THR C 1 98  ? 25.063  43.049  2.403  0.22 12.24 ? 115 THR C CG2 1 
ATOM   3101 C CG2 B THR C 1 98  ? 25.763  44.565  4.069  0.78 15.53 ? 115 THR C CG2 1 
ATOM   3102 N N   . ARG C 1 99  ? 22.516  42.713  4.359  1.00 9.17  ? 116 ARG C N   1 
ATOM   3103 C CA  . ARG C 1 99  ? 21.180  43.186  4.691  1.00 8.03  ? 116 ARG C CA  1 
ATOM   3104 C C   . ARG C 1 99  ? 20.474  42.134  5.533  1.00 7.58  ? 116 ARG C C   1 
ATOM   3105 O O   . ARG C 1 99  ? 20.239  41.023  5.041  1.00 9.16  ? 116 ARG C O   1 
ATOM   3106 C CB  . ARG C 1 99  ? 20.376  43.433  3.420  1.00 9.44  ? 116 ARG C CB  1 
ATOM   3107 C CG  . ARG C 1 99  ? 20.884  44.612  2.618  1.00 14.31 ? 116 ARG C CG  1 
ATOM   3108 C CD  . ARG C 1 99  ? 20.124  44.707  1.309  1.00 20.80 ? 116 ARG C CD  1 
ATOM   3109 N NE  . ARG C 1 99  ? 20.326  45.962  0.604  1.00 35.19 ? 116 ARG C NE  1 
ATOM   3110 C CZ  . ARG C 1 99  ? 19.876  46.197  -0.623 1.00 46.31 ? 116 ARG C CZ  1 
ATOM   3111 N NH1 . ARG C 1 99  ? 19.268  45.254  -1.331 1.00 49.01 ? 116 ARG C NH1 1 
ATOM   3112 N NH2 . ARG C 1 99  ? 20.043  47.406  -1.157 1.00 49.79 ? 116 ARG C NH2 1 
ATOM   3113 N N   . PRO C 1 100 ? 20.130  42.422  6.793  1.00 7.92  ? 117 PRO C N   1 
ATOM   3114 C CA  . PRO C 1 100 ? 19.506  41.385  7.625  1.00 8.35  ? 117 PRO C CA  1 
ATOM   3115 C C   . PRO C 1 100 ? 18.238  40.807  7.033  1.00 8.36  ? 117 PRO C C   1 
ATOM   3116 O O   . PRO C 1 100 ? 17.947  39.626  7.255  1.00 9.03  ? 117 PRO C O   1 
ATOM   3117 C CB  . PRO C 1 100 ? 19.246  42.118  8.947  1.00 8.56  ? 117 PRO C CB  1 
ATOM   3118 C CG  . PRO C 1 100 ? 20.328  43.160  9.003  1.00 9.44  ? 117 PRO C CG  1 
ATOM   3119 C CD  . PRO C 1 100 ? 20.449  43.625  7.580  1.00 9.69  ? 117 PRO C CD  1 
ATOM   3120 N N   . GLY C 1 101 ? 17.494  41.594  6.259  1.00 9.19  ? 118 GLY C N   1 
ATOM   3121 C CA  . GLY C 1 101 ? 16.257  41.103  5.681  1.00 8.79  ? 118 GLY C CA  1 
ATOM   3122 C C   . GLY C 1 101 ? 16.468  40.057  4.613  1.00 8.97  ? 118 GLY C C   1 
ATOM   3123 O O   . GLY C 1 101 ? 15.528  39.325  4.283  1.00 10.91 ? 118 GLY C O   1 
ATOM   3124 N N   . GLU C 1 102 ? 17.681  39.981  4.061  1.00 8.82  ? 119 GLU C N   1 
ATOM   3125 C CA  . GLU C 1 102 ? 18.046  38.979  3.075  1.00 8.47  ? 119 GLU C CA  1 
ATOM   3126 C C   . GLU C 1 102 ? 18.836  37.830  3.676  1.00 9.48  ? 119 GLU C C   1 
ATOM   3127 O O   . GLU C 1 102 ? 19.109  36.849  2.978  1.00 11.37 ? 119 GLU C O   1 
ATOM   3128 C CB  . GLU C 1 102 ? 18.893  39.633  1.973  1.00 11.36 ? 119 GLU C CB  1 
ATOM   3129 C CG  . GLU C 1 102 ? 18.146  40.740  1.223  1.00 14.91 ? 119 GLU C CG  1 
ATOM   3130 C CD  . GLU C 1 102 ? 18.959  41.468  0.154  1.00 17.10 ? 119 GLU C CD  1 
ATOM   3131 O OE1 . GLU C 1 102 ? 20.206  41.451  0.194  1.00 17.41 ? 119 GLU C OE1 1 
ATOM   3132 O OE2 . GLU C 1 102 ? 18.329  42.098  -0.726 1.00 21.87 ? 119 GLU C OE2 1 
ATOM   3133 N N   . ALA C 1 103 ? 19.222  37.936  4.936  1.00 9.03  ? 120 ALA C N   1 
ATOM   3134 C CA  . ALA C 1 103 ? 20.038  36.919  5.577  1.00 8.52  ? 120 ALA C CA  1 
ATOM   3135 C C   . ALA C 1 103 ? 19.201  35.688  5.911  1.00 10.74 ? 120 ALA C C   1 
ATOM   3136 O O   . ALA C 1 103 ? 18.008  35.786  6.220  1.00 11.03 ? 120 ALA C O   1 
ATOM   3137 C CB  . ALA C 1 103 ? 20.640  37.473  6.866  1.00 8.55  ? 120 ALA C CB  1 
ATOM   3138 N N   . ALA C 1 104 ? 19.850  34.527  5.875  1.00 10.42 ? 121 ALA C N   1 
ATOM   3139 C CA  . ALA C 1 104 ? 19.133  33.280  6.055  1.00 10.35 ? 121 ALA C CA  1 
ATOM   3140 C C   . ALA C 1 104 ? 18.708  33.092  7.513  1.00 10.74 ? 121 ALA C C   1 
ATOM   3141 O O   . ALA C 1 104 ? 19.407  33.504  8.438  1.00 9.75  ? 121 ALA C O   1 
ATOM   3142 C CB  . ALA C 1 104 ? 20.003  32.101  5.628  1.00 10.41 ? 121 ALA C CB  1 
ATOM   3143 N N   . PRO C 1 105 ? 17.577  32.440  7.749  1.00 14.62 ? 122 PRO C N   1 
ATOM   3144 C CA  . PRO C 1 105 ? 17.180  32.171  9.135  1.00 13.87 ? 122 PRO C CA  1 
ATOM   3145 C C   . PRO C 1 105 ? 18.301  31.437  9.855  1.00 11.77 ? 122 PRO C C   1 
ATOM   3146 O O   . PRO C 1 105 ? 19.005  30.622  9.267  1.00 12.78 ? 122 PRO C O   1 
ATOM   3147 C CB  . PRO C 1 105 ? 15.927  31.289  8.985  1.00 17.85 ? 122 PRO C CB  1 
ATOM   3148 C CG  . PRO C 1 105 ? 15.453  31.545  7.588  1.00 20.58 ? 122 PRO C CG  1 
ATOM   3149 C CD  . PRO C 1 105 ? 16.645  31.842  6.772  1.00 18.40 ? 122 PRO C CD  1 
ATOM   3150 N N   . GLY C 1 106 ? 18.494  31.769  11.118 1.00 10.59 ? 123 GLY C N   1 
ATOM   3151 C CA  . GLY C 1 106 ? 19.541  31.169  11.915 1.00 11.08 ? 123 GLY C CA  1 
ATOM   3152 C C   . GLY C 1 106 ? 20.901  31.838  11.831 1.00 10.08 ? 123 GLY C C   1 
ATOM   3153 O O   . GLY C 1 106 ? 21.823  31.402  12.528 1.00 13.24 ? 123 GLY C O   1 
ATOM   3154 N N   . THR C 1 107 ? 21.072  32.842  10.985 1.00 7.53  ? 124 THR C N   1 
ATOM   3155 C CA  . THR C 1 107 ? 22.306  33.617  10.949 1.00 7.30  ? 124 THR C CA  1 
ATOM   3156 C C   . THR C 1 107 ? 22.230  34.741  11.974 1.00 6.75  ? 124 THR C C   1 
ATOM   3157 O O   . THR C 1 107 ? 21.158  35.116  12.441 1.00 7.03  ? 124 THR C O   1 
ATOM   3158 C CB  . THR C 1 107 ? 22.561  34.192  9.556  1.00 7.88  ? 124 THR C CB  1 
ATOM   3159 O OG1 . THR C 1 107 ? 21.511  35.088  9.189  1.00 8.14  ? 124 THR C OG1 1 
ATOM   3160 C CG2 . THR C 1 107 ? 22.715  33.073  8.519  1.00 9.28  ? 124 THR C CG2 1 
ATOM   3161 N N   . ILE C 1 108 ? 23.388  35.294  12.311 1.00 7.28  ? 125 ILE C N   1 
ATOM   3162 C CA  . ILE C 1 108 ? 23.410  36.364  13.305 1.00 6.97  ? 125 ILE C CA  1 
ATOM   3163 C C   . ILE C 1 108 ? 22.562  37.540  12.837 1.00 7.87  ? 125 ILE C C   1 
ATOM   3164 O O   . ILE C 1 108 ? 21.744  38.076  13.587 1.00 9.15  ? 125 ILE C O   1 
ATOM   3165 C CB  . ILE C 1 108 ? 24.863  36.792  13.599 1.00 7.63  ? 125 ILE C CB  1 
ATOM   3166 C CG1 . ILE C 1 108 ? 25.586  35.667  14.331 1.00 9.93  ? 125 ILE C CG1 1 
ATOM   3167 C CG2 . ILE C 1 108 ? 24.875  38.068  14.417 1.00 8.48  ? 125 ILE C CG2 1 
ATOM   3168 C CD1 . ILE C 1 108 ? 27.101  35.841  14.414 1.00 12.28 ? 125 ILE C CD1 1 
ATOM   3169 N N   . ARG C 1 109 ? 22.745  37.970  11.593 1.00 7.39  ? 126 ARG C N   1 
ATOM   3170 C CA  . ARG C 1 109 ? 22.045  39.172  11.157 1.00 8.02  ? 126 ARG C CA  1 
ATOM   3171 C C   . ARG C 1 109 ? 20.541  38.963  11.080 1.00 7.33  ? 126 ARG C C   1 
ATOM   3172 O O   . ARG C 1 109 ? 19.774  39.860  11.454 1.00 7.75  ? 126 ARG C O   1 
ATOM   3173 C CB  . ARG C 1 109 ? 22.639  39.671  9.853  1.00 9.62  ? 126 ARG C CB  1 
ATOM   3174 C CG  . ARG C 1 109 ? 23.859  40.512  10.148 1.00 12.77 ? 126 ARG C CG  1 
ATOM   3175 C CD  . ARG C 1 109 ? 24.834  40.390  9.120  1.00 12.59 ? 126 ARG C CD  1 
ATOM   3176 N NE  . ARG C 1 109 ? 26.035  41.169  9.353  1.00 8.99  ? 126 ARG C NE  1 
ATOM   3177 C CZ  . ARG C 1 109 ? 26.913  41.355  8.388  1.00 9.11  ? 126 ARG C CZ  1 
ATOM   3178 N NH1 . ARG C 1 109 ? 26.768  40.766  7.216  1.00 12.46 ? 126 ARG C NH1 1 
ATOM   3179 N NH2 . ARG C 1 109 ? 27.944  42.157  8.592  1.00 9.42  ? 126 ARG C NH2 1 
ATOM   3180 N N   . ALA C 1 110 ? 20.103  37.788  10.636 1.00 6.86  ? 127 ALA C N   1 
ATOM   3181 C CA  . ALA C 1 110 ? 18.674  37.499  10.587 1.00 7.42  ? 127 ALA C CA  1 
ATOM   3182 C C   . ALA C 1 110 ? 18.082  37.398  11.980 1.00 7.92  ? 127 ALA C C   1 
ATOM   3183 O O   . ALA C 1 110 ? 16.920  37.769  12.190 1.00 9.23  ? 127 ALA C O   1 
ATOM   3184 C CB  . ALA C 1 110 ? 18.424  36.199  9.814  1.00 9.27  ? 127 ALA C CB  1 
ATOM   3185 N N   . ASP C 1 111 ? 18.844  36.862  12.937 1.00 7.17  ? 128 ASP C N   1 
ATOM   3186 C CA  . ASP C 1 111 ? 18.314  36.622  14.279 1.00 6.43  ? 128 ASP C CA  1 
ATOM   3187 C C   . ASP C 1 111 ? 18.287  37.890  15.127 1.00 6.74  ? 128 ASP C C   1 
ATOM   3188 O O   . ASP C 1 111 ? 17.446  37.998  16.025 1.00 7.61  ? 128 ASP C O   1 
ATOM   3189 C CB  . ASP C 1 111 ? 19.139  35.551  15.000 1.00 8.14  ? 128 ASP C CB  1 
ATOM   3190 C CG  . ASP C 1 111 ? 18.852  34.138  14.504 1.00 12.00 ? 128 ASP C CG  1 
ATOM   3191 O OD1 . ASP C 1 111 ? 17.865  33.922  13.766 1.00 15.59 ? 128 ASP C OD1 1 
ATOM   3192 O OD2 . ASP C 1 111 ? 19.657  33.235  14.829 1.00 13.25 ? 128 ASP C OD2 1 
ATOM   3193 N N   . PHE C 1 112 ? 19.184  38.847  14.860 1.00 6.04  ? 129 PHE C N   1 
ATOM   3194 C CA  . PHE C 1 112 ? 19.366  40.006  15.723 1.00 6.94  ? 129 PHE C CA  1 
ATOM   3195 C C   . PHE C 1 112 ? 19.033  41.360  15.097 1.00 6.61  ? 129 PHE C C   1 
ATOM   3196 O O   . PHE C 1 112 ? 18.866  42.323  15.853 1.00 7.52  ? 129 PHE C O   1 
ATOM   3197 C CB  . PHE C 1 112 ? 20.836  40.113  16.163 1.00 6.87  ? 129 PHE C CB  1 
ATOM   3198 C CG  . PHE C 1 112 ? 21.276  39.128  17.205 1.00 8.19  ? 129 PHE C CG  1 
ATOM   3199 C CD1 . PHE C 1 112 ? 21.214  39.430  18.560 1.00 8.16  ? 129 PHE C CD1 1 
ATOM   3200 C CD2 . PHE C 1 112 ? 21.863  37.927  16.823 1.00 9.15  ? 129 PHE C CD2 1 
ATOM   3201 C CE1 . PHE C 1 112 ? 21.689  38.530  19.511 1.00 10.16 ? 129 PHE C CE1 1 
ATOM   3202 C CE2 . PHE C 1 112 ? 22.336  37.027  17.759 1.00 8.40  ? 129 PHE C CE2 1 
ATOM   3203 C CZ  . PHE C 1 112 ? 22.252  37.323  19.095 1.00 9.55  ? 129 PHE C CZ  1 
ATOM   3204 N N   . CYS C 1 113 ? 18.971  41.487  13.774 1.00 6.68  ? 130 CYS C N   1 
ATOM   3205 C CA  . CYS C 1 113 ? 19.075  42.798  13.153 1.00 6.30  ? 130 CYS C CA  1 
ATOM   3206 C C   . CYS C 1 113 ? 17.967  43.058  12.140 1.00 7.25  ? 130 CYS C C   1 
ATOM   3207 O O   . CYS C 1 113 ? 17.237  42.160  11.719 1.00 7.33  ? 130 CYS C O   1 
ATOM   3208 C CB  . CYS C 1 113 ? 20.458  42.976  12.517 1.00 7.14  ? 130 CYS C CB  1 
ATOM   3209 S SG  . CYS C 1 113 ? 21.801  42.883  13.690 1.00 8.44  ? 130 CYS C SG  1 
ATOM   3210 N N   . GLN C 1 114 ? 17.867  44.329  11.742 1.00 7.74  ? 131 GLN C N   1 
ATOM   3211 C CA  . GLN C 1 114 ? 16.879  44.801  10.773 1.00 6.32  ? 131 GLN C CA  1 
ATOM   3212 C C   . GLN C 1 114 ? 17.482  45.440  9.530  1.00 7.47  ? 131 GLN C C   1 
ATOM   3213 O O   . GLN C 1 114 ? 16.928  45.278  8.438  1.00 9.00  ? 131 GLN C O   1 
ATOM   3214 C CB  . GLN C 1 114 ? 15.932  45.806  11.441 1.00 9.08  ? 131 GLN C CB  1 
ATOM   3215 C CG  . GLN C 1 114 ? 15.080  45.212  12.540 1.00 8.36  ? 131 GLN C CG  1 
ATOM   3216 C CD  . GLN C 1 114 ? 14.048  46.175  13.073 1.00 7.49  ? 131 GLN C CD  1 
ATOM   3217 O OE1 . GLN C 1 114 ? 13.361  46.839  12.311 1.00 8.33  ? 131 GLN C OE1 1 
ATOM   3218 N NE2 . GLN C 1 114 ? 13.933  46.251  14.391 1.00 8.15  ? 131 GLN C NE2 1 
ATOM   3219 N N   . GLN C 1 115 ? 18.556  46.219  9.664  1.00 7.05  ? 132 GLN C N   1 
ATOM   3220 C CA  . GLN C 1 115 ? 19.078  47.013  8.560  1.00 9.24  ? 132 GLN C CA  1 
ATOM   3221 C C   . GLN C 1 115 ? 20.590  46.889  8.462  1.00 7.08  ? 132 GLN C C   1 
ATOM   3222 O O   . GLN C 1 115 ? 21.276  46.692  9.466  1.00 8.17  ? 132 GLN C O   1 
ATOM   3223 C CB  . GLN C 1 115 ? 18.713  48.493  8.735  1.00 9.06  ? 132 GLN C CB  1 
ATOM   3224 C CG  . GLN C 1 115 ? 17.229  48.731  8.741  1.00 11.33 ? 132 GLN C CG  1 
ATOM   3225 C CD  . GLN C 1 115 ? 16.888  50.195  8.587  1.00 12.53 ? 132 GLN C CD  1 
ATOM   3226 O OE1 . GLN C 1 115 ? 16.973  50.957  9.538  1.00 12.90 ? 132 GLN C OE1 1 
ATOM   3227 N NE2 . GLN C 1 115 ? 16.514  50.594  7.381  1.00 17.73 ? 132 GLN C NE2 1 
ATOM   3228 N N   . ALA C 1 116 ? 21.092  47.027  7.230  1.00 8.55  ? 133 ALA C N   1 
ATOM   3229 C CA  . ALA C 1 116 ? 22.523  46.877  6.970  1.00 9.22  ? 133 ALA C CA  1 
ATOM   3230 C C   . ALA C 1 116 ? 23.374  47.869  7.755  1.00 9.87  ? 133 ALA C C   1 
ATOM   3231 O O   . ALA C 1 116 ? 24.503  47.540  8.132  1.00 10.96 ? 133 ALA C O   1 
ATOM   3232 C CB  . ALA C 1 116 ? 22.823  47.025  5.477  1.00 9.85  ? 133 ALA C CB  1 
ATOM   3233 N N   . GLY C 1 117 ? 22.874  49.079  8.006  1.00 10.18 ? 134 GLY C N   1 
ATOM   3234 C CA  . GLY C 1 117 ? 23.677  50.056  8.733  1.00 11.18 ? 134 GLY C CA  1 
ATOM   3235 C C   . GLY C 1 117 ? 23.849  49.758  10.202 1.00 10.55 ? 134 GLY C C   1 
ATOM   3236 O O   . GLY C 1 117 ? 24.642  50.434  10.860 1.00 10.80 ? 134 GLY C O   1 
ATOM   3237 N N   . ARG C 1 118 ? 23.076  48.810  10.750 1.00 8.72  ? 135 ARG C N   1 
ATOM   3238 C CA  . ARG C 1 118 ? 23.279  48.313  12.106 1.00 9.14  ? 135 ARG C CA  1 
ATOM   3239 C C   . ARG C 1 118 ? 23.174  46.793  12.057 1.00 8.49  ? 135 ARG C C   1 
ATOM   3240 O O   . ARG C 1 118 ? 22.173  46.207  12.490 1.00 8.75  ? 135 ARG C O   1 
ATOM   3241 C CB  . ARG C 1 118 ? 22.257  48.910  13.054 1.00 9.30  ? 135 ARG C CB  1 
ATOM   3242 C CG  . ARG C 1 118 ? 22.422  50.399  13.296 1.00 8.68  ? 135 ARG C CG  1 
ATOM   3243 C CD  . ARG C 1 118 ? 23.746  50.735  13.968 1.00 9.13  ? 135 ARG C CD  1 
ATOM   3244 N NE  . ARG C 1 118 ? 23.771  52.094  14.499 1.00 11.08 ? 135 ARG C NE  1 
ATOM   3245 C CZ  . ARG C 1 118 ? 24.821  52.664  15.077 1.00 12.09 ? 135 ARG C CZ  1 
ATOM   3246 N NH1 . ARG C 1 118 ? 25.988  52.043  15.161 1.00 14.30 ? 135 ARG C NH1 1 
ATOM   3247 N NH2 . ARG C 1 118 ? 24.702  53.892  15.578 1.00 14.99 ? 135 ARG C NH2 1 
ATOM   3248 N N   . ASN C 1 119 ? 24.245  46.141  11.601 1.00 6.82  ? 136 ASN C N   1 
ATOM   3249 C CA  . ASN C 1 119 ? 24.217  44.695  11.383 1.00 6.30  ? 136 ASN C CA  1 
ATOM   3250 C C   . ASN C 1 119 ? 25.225  43.950  12.252 1.00 6.23  ? 136 ASN C C   1 
ATOM   3251 O O   . ASN C 1 119 ? 25.640  42.836  11.906 1.00 6.82  ? 136 ASN C O   1 
ATOM   3252 C CB  . ASN C 1 119 ? 24.297  44.339  9.899  1.00 5.77  ? 136 ASN C CB  1 
ATOM   3253 C CG  . ASN C 1 119 ? 25.620  44.650  9.290  1.00 6.88  ? 136 ASN C CG  1 
ATOM   3254 O OD1 . ASN C 1 119 ? 26.562  45.056  9.978  1.00 8.46  ? 136 ASN C OD1 1 
ATOM   3255 N ND2 . ASN C 1 119 ? 25.721  44.444  7.974  1.00 9.57  ? 136 ASN C ND2 1 
ATOM   3256 N N   . LEU C 1 120 ? 25.599  44.552  13.388 1.00 7.35  ? 137 LEU C N   1 
ATOM   3257 C CA  . LEU C 1 120 ? 26.132  43.934  14.597 1.00 6.46  ? 137 LEU C CA  1 
ATOM   3258 C C   . LEU C 1 120 ? 27.583  43.478  14.542 1.00 6.40  ? 137 LEU C C   1 
ATOM   3259 O O   . LEU C 1 120 ? 28.276  43.570  15.560 1.00 6.82  ? 137 LEU C O   1 
ATOM   3260 C CB  . LEU C 1 120 ? 25.316  42.660  14.942 1.00 7.24  ? 137 LEU C CB  1 
ATOM   3261 C CG  . LEU C 1 120 ? 25.042  42.425  16.424 1.00 8.09  ? 137 LEU C CG  1 
ATOM   3262 C CD1 . LEU C 1 120 ? 24.041  43.479  16.934 1.00 8.47  ? 137 LEU C CD1 1 
ATOM   3263 C CD2 . LEU C 1 120 ? 24.543  40.990  16.632 1.00 7.95  ? 137 LEU C CD2 1 
ATOM   3264 N N   . ILE C 1 121 ? 28.079  43.093  13.373 1.00 7.00  ? 138 ILE C N   1 
ATOM   3265 C CA  . ILE C 1 121 ? 29.331  42.341  13.339 1.00 7.32  ? 138 ILE C CA  1 
ATOM   3266 C C   . ILE C 1 121 ? 29.963  42.469  11.966 1.00 7.02  ? 138 ILE C C   1 
ATOM   3267 O O   . ILE C 1 121 ? 29.267  42.553  10.951 1.00 8.23  ? 138 ILE C O   1 
ATOM   3268 C CB  . ILE C 1 121 ? 29.113  40.864  13.753 1.00 8.56  ? 138 ILE C CB  1 
ATOM   3269 C CG1 . ILE C 1 121 ? 30.451  40.119  13.846 1.00 10.23 ? 138 ILE C CG1 1 
ATOM   3270 C CG2 . ILE C 1 121 ? 28.155  40.144  12.809 1.00 8.42  ? 138 ILE C CG2 1 
ATOM   3271 C CD1 . ILE C 1 121 ? 30.346  38.742  14.534 1.00 12.57 ? 138 ILE C CD1 1 
ATOM   3272 N N   . HIS C 1 122 ? 31.296  42.533  11.962 1.00 8.07  ? 139 HIS C N   1 
ATOM   3273 C CA  . HIS C 1 122 ? 32.127  42.460  10.780 1.00 7.19  ? 139 HIS C CA  1 
ATOM   3274 C C   . HIS C 1 122 ? 32.898  41.148  10.782 1.00 6.75  ? 139 HIS C C   1 
ATOM   3275 O O   . HIS C 1 122 ? 33.342  40.689  11.834 1.00 7.70  ? 139 HIS C O   1 
ATOM   3276 C CB  . HIS C 1 122 ? 33.158  43.596  10.813 1.00 8.67  ? 139 HIS C CB  1 
ATOM   3277 C CG  . HIS C 1 122 ? 34.269  43.395  9.844  1.00 8.82  ? 139 HIS C CG  1 
ATOM   3278 N ND1 . HIS C 1 122 ? 34.213  43.863  8.551  1.00 9.01  ? 139 HIS C ND1 1 
ATOM   3279 C CD2 . HIS C 1 122 ? 35.412  42.675  9.939  1.00 10.04 ? 139 HIS C CD2 1 
ATOM   3280 C CE1 . HIS C 1 122 ? 35.297  43.475  7.901  1.00 12.20 ? 139 HIS C CE1 1 
ATOM   3281 N NE2 . HIS C 1 122 ? 36.043  42.755  8.722  1.00 10.28 ? 139 HIS C NE2 1 
ATOM   3282 N N   . GLY C 1 123 ? 33.092  40.573  9.600  1.00 6.96  ? 140 GLY C N   1 
ATOM   3283 C CA  . GLY C 1 123 ? 34.010  39.455  9.444  1.00 7.17  ? 140 GLY C CA  1 
ATOM   3284 C C   . GLY C 1 123 ? 34.762  39.532  8.136  1.00 6.49  ? 140 GLY C C   1 
ATOM   3285 O O   . GLY C 1 123 ? 34.205  39.947  7.118  1.00 7.16  ? 140 GLY C O   1 
ATOM   3286 N N   . SER C 1 124 ? 36.025  39.093  8.159  1.00 7.91  ? 141 SER C N   1 
ATOM   3287 C CA  . SER C 1 124 ? 36.859  39.089  6.968  1.00 7.54  ? 141 SER C CA  1 
ATOM   3288 C C   . SER C 1 124 ? 36.179  38.293  5.863  1.00 7.29  ? 141 SER C C   1 
ATOM   3289 O O   . SER C 1 124 ? 35.558  37.261  6.113  1.00 8.49  ? 141 SER C O   1 
ATOM   3290 C CB  . SER C 1 124 ? 38.210  38.431  7.281  1.00 9.16  ? 141 SER C CB  1 
ATOM   3291 O OG  . SER C 1 124 ? 38.809  39.000  8.423  1.00 9.62  ? 141 SER C OG  1 
ATOM   3292 N N   . ASP C 1 125 ? 36.331  38.746  4.616  1.00 8.96  ? 142 ASP C N   1 
ATOM   3293 C CA  . ASP C 1 125 ? 35.648  38.095  3.495  1.00 8.74  ? 142 ASP C CA  1 
ATOM   3294 C C   . ASP C 1 125 ? 36.539  37.195  2.652  1.00 9.45  ? 142 ASP C C   1 
ATOM   3295 O O   . ASP C 1 125 ? 36.032  36.577  1.710  1.00 12.28 ? 142 ASP C O   1 
ATOM   3296 C CB  . ASP C 1 125 ? 34.903  39.119  2.625  1.00 11.68 ? 142 ASP C CB  1 
ATOM   3297 C CG  . ASP C 1 125 ? 35.811  40.085  1.912  1.00 13.69 ? 142 ASP C CG  1 
ATOM   3298 O OD1 . ASP C 1 125 ? 37.047  39.884  1.870  1.00 13.54 ? 142 ASP C OD1 1 
ATOM   3299 O OD2 . ASP C 1 125 ? 35.253  41.078  1.380  1.00 17.53 ? 142 ASP C OD2 1 
ATOM   3300 N N   . SER C 1 126 ? 37.826  37.072  2.973  1.00 7.21  ? 143 SER C N   1 
ATOM   3301 C CA  . SER C 1 126 ? 38.736  36.253  2.176  1.00 7.19  ? 143 SER C CA  1 
ATOM   3302 C C   . SER C 1 126 ? 40.013  36.005  2.965  1.00 7.67  ? 143 SER C C   1 
ATOM   3303 O O   . SER C 1 126 ? 40.261  36.627  3.996  1.00 8.24  ? 143 SER C O   1 
ATOM   3304 C CB  . SER C 1 126 ? 39.071  36.926  0.849  1.00 8.52  ? 143 SER C CB  1 
ATOM   3305 O OG  . SER C 1 126 ? 39.940  38.031  1.085  1.00 8.88  ? 143 SER C OG  1 
ATOM   3306 N N   . ALA C 1 127 ? 40.835  35.087  2.455  1.00 8.43  ? 144 ALA C N   1 
ATOM   3307 C CA  . ALA C 1 127 ? 42.128  34.841  3.096  1.00 7.89  ? 144 ALA C CA  1 
ATOM   3308 C C   . ALA C 1 127 ? 42.980  36.113  3.132  1.00 8.22  ? 144 ALA C C   1 
ATOM   3309 O O   . ALA C 1 127 ? 43.584  36.454  4.157  1.00 9.12  ? 144 ALA C O   1 
ATOM   3310 C CB  . ALA C 1 127 ? 42.863  33.719  2.358  1.00 9.24  ? 144 ALA C CB  1 
ATOM   3311 N N   . GLU C 1 128 ? 43.026  36.838  2.023  1.00 8.13  ? 145 GLU C N   1 
ATOM   3312 C CA  . GLU C 1 128 ? 43.843  38.042  1.999  1.00 8.61  ? 145 GLU C CA  1 
ATOM   3313 C C   . GLU C 1 128 ? 43.322  39.093  2.973  1.00 8.98  ? 145 GLU C C   1 
ATOM   3314 O O   . GLU C 1 128 ? 44.107  39.736  3.689  1.00 8.74  ? 145 GLU C O   1 
ATOM   3315 C CB  . GLU C 1 128 ? 43.903  38.606  0.585  1.00 9.26  ? 145 GLU C CB  1 
ATOM   3316 C CG  . GLU C 1 128 ? 44.825  39.817  0.475  1.00 10.65 ? 145 GLU C CG  1 
ATOM   3317 C CD  . GLU C 1 128 ? 44.971  40.301  -0.949 1.00 12.99 ? 145 GLU C CD  1 
ATOM   3318 O OE1 . GLU C 1 128 ? 45.382  39.498  -1.813 1.00 13.53 ? 145 GLU C OE1 1 
ATOM   3319 O OE2 . GLU C 1 128 ? 44.651  41.472  -1.205 1.00 14.84 ? 145 GLU C OE2 1 
ATOM   3320 N N   . SER C 1 129 ? 42.007  39.287  3.023  1.00 9.28  ? 146 SER C N   1 
ATOM   3321 C CA  A SER C 1 129 ? 41.493  40.323  3.908  0.55 7.29  ? 146 SER C CA  1 
ATOM   3322 C CA  B SER C 1 129 ? 41.433  40.298  3.909  0.45 9.32  ? 146 SER C CA  1 
ATOM   3323 C C   . SER C 1 129 ? 41.622  39.927  5.371  1.00 6.73  ? 146 SER C C   1 
ATOM   3324 O O   . SER C 1 129 ? 41.844  40.795  6.214  1.00 8.48  ? 146 SER C O   1 
ATOM   3325 C CB  A SER C 1 129 ? 40.060  40.696  3.541  0.55 7.39  ? 146 SER C CB  1 
ATOM   3326 C CB  B SER C 1 129 ? 39.945  40.470  3.613  0.45 12.95 ? 146 SER C CB  1 
ATOM   3327 O OG  A SER C 1 129 ? 39.196  39.587  3.620  0.55 8.17  ? 146 SER C OG  1 
ATOM   3328 O OG  B SER C 1 129 ? 39.742  41.232  2.444  0.45 18.07 ? 146 SER C OG  1 
ATOM   3329 N N   . ALA C 1 130 ? 41.512  38.639  5.685  1.00 6.90  ? 147 ALA C N   1 
ATOM   3330 C CA  . ALA C 1 130 ? 41.701  38.196  7.064  1.00 7.76  ? 147 ALA C CA  1 
ATOM   3331 C C   . ALA C 1 130 ? 43.112  38.495  7.534  1.00 8.97  ? 147 ALA C C   1 
ATOM   3332 O O   . ALA C 1 130 ? 43.314  39.034  8.624  1.00 10.03 ? 147 ALA C O   1 
ATOM   3333 C CB  . ALA C 1 130 ? 41.371  36.699  7.184  1.00 8.23  ? 147 ALA C CB  1 
ATOM   3334 N N   . LYS C 1 131 ? 44.106  38.181  6.716  1.00 8.54  ? 148 LYS C N   1 
ATOM   3335 C CA  . LYS C 1 131 ? 45.481  38.436  7.125  1.00 9.93  ? 148 LYS C CA  1 
ATOM   3336 C C   . LYS C 1 131 ? 45.715  39.924  7.319  1.00 10.18 ? 148 LYS C C   1 
ATOM   3337 O O   . LYS C 1 131 ? 46.351  40.337  8.296  1.00 9.18  ? 148 LYS C O   1 
ATOM   3338 C CB  . LYS C 1 131 ? 46.428  37.880  6.075  1.00 11.36 ? 148 LYS C CB  1 
ATOM   3339 C CG  . LYS C 1 131 ? 47.898  37.997  6.417  1.00 15.49 ? 148 LYS C CG  1 
ATOM   3340 C CD  . LYS C 1 131 ? 48.696  37.221  5.372  1.00 18.48 ? 148 LYS C CD  1 
ATOM   3341 C CE  . LYS C 1 131 ? 50.168  37.172  5.699  1.00 21.26 ? 148 LYS C CE  1 
ATOM   3342 N NZ  . LYS C 1 131 ? 50.731  38.541  5.768  1.00 27.11 ? 148 LYS C NZ  1 
ATOM   3343 N N   . ARG C 1 132 ? 45.201  40.747  6.400  1.00 8.37  ? 149 ARG C N   1 
ATOM   3344 C CA  . ARG C 1 132 ? 45.370  42.196  6.508  1.00 9.10  ? 149 ARG C CA  1 
ATOM   3345 C C   . ARG C 1 132 ? 44.673  42.748  7.747  1.00 7.95  ? 149 ARG C C   1 
ATOM   3346 O O   . ARG C 1 132 ? 45.231  43.581  8.474  1.00 9.35  ? 149 ARG C O   1 
ATOM   3347 C CB  . ARG C 1 132 ? 44.819  42.858  5.246  1.00 11.78 ? 149 ARG C CB  1 
ATOM   3348 C CG  . ARG C 1 132 ? 45.126  44.333  5.156  1.00 14.11 ? 149 ARG C CG  1 
ATOM   3349 C CD  . ARG C 1 132 ? 44.485  44.942  3.919  1.00 18.85 ? 149 ARG C CD  1 
ATOM   3350 N NE  . ARG C 1 132 ? 43.096  45.299  4.157  1.00 25.62 ? 149 ARG C NE  1 
ATOM   3351 C CZ  . ARG C 1 132 ? 42.693  46.463  4.660  1.00 25.67 ? 149 ARG C CZ  1 
ATOM   3352 N NH1 . ARG C 1 132 ? 43.543  47.444  4.917  1.00 24.56 ? 149 ARG C NH1 1 
ATOM   3353 N NH2 . ARG C 1 132 ? 41.407  46.642  4.925  1.00 25.30 ? 149 ARG C NH2 1 
ATOM   3354 N N   . GLU C 1 133 ? 43.444  42.298  7.998  1.00 7.05  ? 150 GLU C N   1 
ATOM   3355 C CA  . GLU C 1 133 ? 42.653  42.844  9.098  1.00 7.26  ? 150 GLU C CA  1 
ATOM   3356 C C   . GLU C 1 133 ? 43.193  42.415  10.454 1.00 6.56  ? 150 GLU C C   1 
ATOM   3357 O O   . GLU C 1 133 ? 43.240  43.227  11.390 1.00 7.81  ? 150 GLU C O   1 
ATOM   3358 C CB  . GLU C 1 133 ? 41.189  42.433  8.937  1.00 8.02  ? 150 GLU C CB  1 
ATOM   3359 C CG  . GLU C 1 133 ? 40.514  43.149  7.762  1.00 8.87  ? 150 GLU C CG  1 
ATOM   3360 C CD  . GLU C 1 133 ? 39.135  42.627  7.444  1.00 9.60  ? 150 GLU C CD  1 
ATOM   3361 O OE1 . GLU C 1 133 ? 38.626  41.750  8.170  1.00 10.71 ? 150 GLU C OE1 1 
ATOM   3362 O OE2 . GLU C 1 133 ? 38.550  43.105  6.460  1.00 10.18 ? 150 GLU C OE2 1 
ATOM   3363 N N   . ILE C 1 134 ? 43.596  41.151  10.586 1.00 7.88  ? 151 ILE C N   1 
ATOM   3364 C CA  . ILE C 1 134 ? 44.199  40.708  11.838 1.00 7.93  ? 151 ILE C CA  1 
ATOM   3365 C C   . ILE C 1 134 ? 45.410  41.575  12.157 1.00 8.07  ? 151 ILE C C   1 
ATOM   3366 O O   . ILE C 1 134 ? 45.575  42.046  13.284 1.00 10.19 ? 151 ILE C O   1 
ATOM   3367 C CB  . ILE C 1 134 ? 44.552  39.211  11.773 1.00 9.47  ? 151 ILE C CB  1 
ATOM   3368 C CG1 . ILE C 1 134 ? 43.279  38.343  11.712 1.00 9.42  ? 151 ILE C CG1 1 
ATOM   3369 C CG2 . ILE C 1 134 ? 45.380  38.818  12.977 1.00 10.17 ? 151 ILE C CG2 1 
ATOM   3370 C CD1 . ILE C 1 134 ? 43.541  36.871  11.356 1.00 10.86 ? 151 ILE C CD1 1 
ATOM   3371 N N   . SER C 1 135 ? 46.258  41.825  11.154 1.00 9.13  ? 152 SER C N   1 
ATOM   3372 C CA  . SER C 1 135 ? 47.460  42.626  11.375 1.00 10.10 ? 152 SER C CA  1 
ATOM   3373 C C   . SER C 1 135 ? 47.125  44.084  11.665 1.00 10.21 ? 152 SER C C   1 
ATOM   3374 O O   . SER C 1 135 ? 47.850  44.743  12.412 1.00 10.23 ? 152 SER C O   1 
ATOM   3375 C CB  . SER C 1 135 ? 48.384  42.527  10.162 1.00 11.34 ? 152 SER C CB  1 
ATOM   3376 O OG  . SER C 1 135 ? 48.831  41.198  10.025 1.00 15.44 ? 152 SER C OG  1 
ATOM   3377 N N   . LEU C 1 136 ? 46.053  44.610  11.071 1.00 10.14 ? 153 LEU C N   1 
ATOM   3378 C CA  . LEU C 1 136 ? 45.670  45.996  11.317 1.00 9.37  ? 153 LEU C CA  1 
ATOM   3379 C C   . LEU C 1 136 ? 45.250  46.208  12.767 1.00 10.20 ? 153 LEU C C   1 
ATOM   3380 O O   . LEU C 1 136 ? 45.635  47.200  13.394 1.00 11.05 ? 153 LEU C O   1 
ATOM   3381 C CB  . LEU C 1 136 ? 44.533  46.391  10.372 1.00 9.92  ? 153 LEU C CB  1 
ATOM   3382 C CG  . LEU C 1 136 ? 43.926  47.769  10.597 1.00 11.01 ? 153 LEU C CG  1 
ATOM   3383 C CD1 . LEU C 1 136 ? 44.974  48.882  10.400 1.00 14.85 ? 153 LEU C CD1 1 
ATOM   3384 C CD2 . LEU C 1 136 ? 42.763  47.971  9.652  1.00 12.10 ? 153 LEU C CD2 1 
ATOM   3385 N N   . TRP C 1 137 ? 44.457  45.293  13.319 1.00 9.28  ? 154 TRP C N   1 
ATOM   3386 C CA  . TRP C 1 137 ? 43.848  45.502  14.626 1.00 9.08  ? 154 TRP C CA  1 
ATOM   3387 C C   . TRP C 1 137 ? 44.602  44.862  15.787 1.00 7.87  ? 154 TRP C C   1 
ATOM   3388 O O   . TRP C 1 137 ? 44.340  45.227  16.938 1.00 10.67 ? 154 TRP C O   1 
ATOM   3389 C CB  . TRP C 1 137 ? 42.413  44.980  14.627 1.00 9.40  ? 154 TRP C CB  1 
ATOM   3390 C CG  . TRP C 1 137 ? 41.468  45.733  13.733 1.00 7.70  ? 154 TRP C CG  1 
ATOM   3391 C CD1 . TRP C 1 137 ? 41.168  45.435  12.433 1.00 9.06  ? 154 TRP C CD1 1 
ATOM   3392 C CD2 . TRP C 1 137 ? 40.678  46.885  14.075 1.00 7.64  ? 154 TRP C CD2 1 
ATOM   3393 N NE1 . TRP C 1 137 ? 40.231  46.322  11.943 1.00 8.30  ? 154 TRP C NE1 1 
ATOM   3394 C CE2 . TRP C 1 137 ? 39.924  47.229  12.926 1.00 8.38  ? 154 TRP C CE2 1 
ATOM   3395 C CE3 . TRP C 1 137 ? 40.530  47.653  15.238 1.00 9.07  ? 154 TRP C CE3 1 
ATOM   3396 C CZ2 . TRP C 1 137 ? 39.012  48.285  12.919 1.00 8.65  ? 154 TRP C CZ2 1 
ATOM   3397 C CZ3 . TRP C 1 137 ? 39.634  48.725  15.224 1.00 11.01 ? 154 TRP C CZ3 1 
ATOM   3398 C CH2 . TRP C 1 137 ? 38.897  49.033  14.069 1.00 10.83 ? 154 TRP C CH2 1 
ATOM   3399 N N   . PHE C 1 138 ? 45.520  43.930  15.520 1.00 7.55  ? 155 PHE C N   1 
ATOM   3400 C CA  . PHE C 1 138 ? 46.268  43.227  16.548 1.00 7.52  ? 155 PHE C CA  1 
ATOM   3401 C C   . PHE C 1 138 ? 47.757  43.269  16.242 1.00 9.69  ? 155 PHE C C   1 
ATOM   3402 O O   . PHE C 1 138 ? 48.160  43.169  15.083 1.00 11.65 ? 155 PHE C O   1 
ATOM   3403 C CB  . PHE C 1 138 ? 45.832  41.760  16.636 1.00 8.03  ? 155 PHE C CB  1 
ATOM   3404 C CG  . PHE C 1 138 ? 44.519  41.575  17.288 1.00 6.73  ? 155 PHE C CG  1 
ATOM   3405 C CD1 . PHE C 1 138 ? 44.405  41.679  18.658 1.00 9.22  ? 155 PHE C CD1 1 
ATOM   3406 C CD2 . PHE C 1 138 ? 43.387  41.298  16.546 1.00 8.82  ? 155 PHE C CD2 1 
ATOM   3407 C CE1 . PHE C 1 138 ? 43.194  41.502  19.283 1.00 8.84  ? 155 PHE C CE1 1 
ATOM   3408 C CE2 . PHE C 1 138 ? 42.166  41.123  17.176 1.00 8.78  ? 155 PHE C CE2 1 
ATOM   3409 C CZ  . PHE C 1 138 ? 42.074  41.221  18.534 1.00 8.89  ? 155 PHE C CZ  1 
ATOM   3410 N N   . LYS C 1 139 ? 48.564  43.409  17.283 1.00 9.65  ? 156 LYS C N   1 
ATOM   3411 C CA  . LYS C 1 139 ? 49.995  43.172  17.160 1.00 10.23 ? 156 LYS C CA  1 
ATOM   3412 C C   . LYS C 1 139 ? 50.262  41.667  17.215 1.00 9.44  ? 156 LYS C C   1 
ATOM   3413 O O   . LYS C 1 139 ? 49.476  40.907  17.796 1.00 10.74 ? 156 LYS C O   1 
ATOM   3414 C CB  . LYS C 1 139 ? 50.730  43.820  18.324 1.00 14.39 ? 156 LYS C CB  1 
ATOM   3415 C CG  . LYS C 1 139 ? 50.535  45.315  18.458 1.00 21.18 ? 156 LYS C CG  1 
ATOM   3416 C CD  . LYS C 1 139 ? 51.185  45.780  19.763 1.00 30.36 ? 156 LYS C CD  1 
ATOM   3417 C CE  . LYS C 1 139 ? 51.093  47.288  19.976 1.00 36.66 ? 156 LYS C CE  1 
ATOM   3418 N NZ  . LYS C 1 139 ? 51.799  48.043  18.904 1.00 39.90 ? 156 LYS C NZ  1 
ATOM   3419 N N   . PRO C 1 140 ? 51.361  41.199  16.623 1.00 11.67 ? 157 PRO C N   1 
ATOM   3420 C CA  . PRO C 1 140 ? 51.636  39.751  16.670 1.00 12.86 ? 157 PRO C CA  1 
ATOM   3421 C C   . PRO C 1 140 ? 51.679  39.195  18.087 1.00 10.96 ? 157 PRO C C   1 
ATOM   3422 O O   . PRO C 1 140 ? 51.220  38.074  18.328 1.00 12.22 ? 157 PRO C O   1 
ATOM   3423 C CB  . PRO C 1 140 ? 52.984  39.629  15.949 1.00 16.04 ? 157 PRO C CB  1 
ATOM   3424 C CG  . PRO C 1 140 ? 53.039  40.800  15.061 1.00 16.63 ? 157 PRO C CG  1 
ATOM   3425 C CD  . PRO C 1 140 ? 52.328  41.911  15.773 1.00 12.34 ? 157 PRO C CD  1 
ATOM   3426 N N   . GLU C 1 141 ? 52.171  39.978  19.044 1.00 11.69 ? 158 GLU C N   1 
ATOM   3427 C CA  . GLU C 1 141 ? 52.250  39.546  20.433 1.00 15.17 ? 158 GLU C CA  1 
ATOM   3428 C C   . GLU C 1 141 ? 50.878  39.356  21.071 1.00 14.56 ? 158 GLU C C   1 
ATOM   3429 O O   . GLU C 1 141 ? 50.778  38.718  22.121 1.00 16.37 ? 158 GLU C O   1 
ATOM   3430 C CB  . GLU C 1 141 ? 53.075  40.554  21.226 1.00 21.32 ? 158 GLU C CB  1 
ATOM   3431 C CG  . GLU C 1 141 ? 54.544  40.570  20.831 1.00 27.76 ? 158 GLU C CG  1 
ATOM   3432 C CD  . GLU C 1 141 ? 54.882  41.569  19.731 1.00 30.99 ? 158 GLU C CD  1 
ATOM   3433 O OE1 . GLU C 1 141 ? 53.988  42.026  18.980 1.00 25.14 ? 158 GLU C OE1 1 
ATOM   3434 O OE2 . GLU C 1 141 ? 56.074  41.897  19.622 1.00 34.67 ? 158 GLU C OE2 1 
ATOM   3435 N N   . GLU C 1 142 ? 49.820  39.894  20.473 1.00 11.48 ? 159 GLU C N   1 
ATOM   3436 C CA  . GLU C 1 142 ? 48.477  39.749  21.010 1.00 12.25 ? 159 GLU C CA  1 
ATOM   3437 C C   . GLU C 1 142 ? 47.760  38.511  20.500 1.00 10.45 ? 159 GLU C C   1 
ATOM   3438 O O   . GLU C 1 142 ? 46.670  38.204  20.995 1.00 10.89 ? 159 GLU C O   1 
ATOM   3439 C CB  . GLU C 1 142 ? 47.671  41.003  20.676 1.00 10.65 ? 159 GLU C CB  1 
ATOM   3440 C CG  . GLU C 1 142 ? 48.215  42.229  21.385 1.00 12.11 ? 159 GLU C CG  1 
ATOM   3441 C CD  . GLU C 1 142 ? 47.566  43.531  20.981 1.00 15.13 ? 159 GLU C CD  1 
ATOM   3442 O OE1 . GLU C 1 142 ? 47.162  43.700  19.819 1.00 14.06 ? 159 GLU C OE1 1 
ATOM   3443 O OE2 . GLU C 1 142 ? 47.489  44.416  21.844 1.00 23.12 ? 159 GLU C OE2 1 
ATOM   3444 N N   . ILE C 1 143 ? 48.361  37.782  19.554 1.00 9.42  ? 160 ILE C N   1 
ATOM   3445 C CA  . ILE C 1 143 ? 47.767  36.573  18.994 1.00 7.66  ? 160 ILE C CA  1 
ATOM   3446 C C   . ILE C 1 143 ? 48.269  35.395  19.816 1.00 9.76  ? 160 ILE C C   1 
ATOM   3447 O O   . ILE C 1 143 ? 49.477  35.150  19.887 1.00 11.50 ? 160 ILE C O   1 
ATOM   3448 C CB  . ILE C 1 143 ? 48.136  36.399  17.513 1.00 9.48  ? 160 ILE C CB  1 
ATOM   3449 C CG1 . ILE C 1 143 ? 47.812  37.660  16.694 1.00 11.64 ? 160 ILE C CG1 1 
ATOM   3450 C CG2 . ILE C 1 143 ? 47.427  35.190  16.937 1.00 12.68 ? 160 ILE C CG2 1 
ATOM   3451 C CD1 . ILE C 1 143 ? 46.352  38.023  16.641 1.00 14.29 ? 160 ILE C CD1 1 
ATOM   3452 N N   . GLN C 1 144 ? 47.345  34.650  20.414 1.00 7.66  ? 161 GLN C N   1 
ATOM   3453 C CA  . GLN C 1 144 ? 47.674  33.638  21.407 1.00 9.69  ? 161 GLN C CA  1 
ATOM   3454 C C   . GLN C 1 144 ? 47.557  32.251  20.795 1.00 9.53  ? 161 GLN C C   1 
ATOM   3455 O O   . GLN C 1 144 ? 46.502  31.891  20.261 1.00 11.89 ? 161 GLN C O   1 
ATOM   3456 C CB  . GLN C 1 144 ? 46.741  33.750  22.612 1.00 9.02  ? 161 GLN C CB  1 
ATOM   3457 C CG  . GLN C 1 144 ? 46.629  35.127  23.173 1.00 11.19 ? 161 GLN C CG  1 
ATOM   3458 C CD  . GLN C 1 144 ? 47.935  35.638  23.700 1.00 11.23 ? 161 GLN C CD  1 
ATOM   3459 O OE1 . GLN C 1 144 ? 48.753  34.865  24.176 1.00 11.47 ? 161 GLN C OE1 1 
ATOM   3460 N NE2 . GLN C 1 144 ? 48.153  36.945  23.593 1.00 11.58 ? 161 GLN C NE2 1 
ATOM   3461 N N   . SER C 1 145 ? 48.628  31.465  20.903 1.00 10.30 ? 162 SER C N   1 
ATOM   3462 C CA  A SER C 1 145 ? 48.661  30.111  20.367 0.60 9.53  ? 162 SER C CA  1 
ATOM   3463 C CA  B SER C 1 145 ? 48.668  30.110  20.367 0.40 10.33 ? 162 SER C CA  1 
ATOM   3464 C C   . SER C 1 145 ? 48.526  29.115  21.514 1.00 9.82  ? 162 SER C C   1 
ATOM   3465 O O   . SER C 1 145 ? 49.363  29.089  22.429 1.00 12.11 ? 162 SER C O   1 
ATOM   3466 C CB  A SER C 1 145 ? 49.953  29.856  19.593 0.60 11.56 ? 162 SER C CB  1 
ATOM   3467 C CB  B SER C 1 145 ? 49.983  29.862  19.626 0.40 12.62 ? 162 SER C CB  1 
ATOM   3468 O OG  A SER C 1 145 ? 49.993  28.512  19.150 0.60 12.07 ? 162 SER C OG  1 
ATOM   3469 O OG  B SER C 1 145 ? 50.154  30.782  18.563 0.40 13.16 ? 162 SER C OG  1 
ATOM   3470 N N   . TYR C 1 146 ? 47.469  28.311  21.463 1.00 9.60  ? 163 TYR C N   1 
ATOM   3471 C CA  . TYR C 1 146 ? 47.211  27.235  22.414 1.00 10.13 ? 163 TYR C CA  1 
ATOM   3472 C C   . TYR C 1 146 ? 46.312  26.243  21.686 1.00 8.71  ? 163 TYR C C   1 
ATOM   3473 O O   . TYR C 1 146 ? 45.733  26.566  20.646 1.00 10.01 ? 163 TYR C O   1 
ATOM   3474 C CB  . TYR C 1 146 ? 46.590  27.740  23.734 1.00 8.99  ? 163 TYR C CB  1 
ATOM   3475 C CG  . TYR C 1 146 ? 45.234  28.382  23.590 1.00 9.11  ? 163 TYR C CG  1 
ATOM   3476 C CD1 . TYR C 1 146 ? 45.121  29.734  23.306 1.00 7.30  ? 163 TYR C CD1 1 
ATOM   3477 C CD2 . TYR C 1 146 ? 44.071  27.638  23.728 1.00 9.71  ? 163 TYR C CD2 1 
ATOM   3478 C CE1 . TYR C 1 146 ? 43.869  30.332  23.166 1.00 7.95  ? 163 TYR C CE1 1 
ATOM   3479 C CE2 . TYR C 1 146 ? 42.836  28.219  23.600 1.00 9.72  ? 163 TYR C CE2 1 
ATOM   3480 C CZ  . TYR C 1 146 ? 42.741  29.559  23.315 1.00 7.40  ? 163 TYR C CZ  1 
ATOM   3481 O OH  . TYR C 1 146 ? 41.496  30.112  23.172 1.00 7.82  ? 163 TYR C OH  1 
ATOM   3482 N N   . LYS C 1 147 ? 46.225  25.030  22.219 1.00 9.98  ? 164 LYS C N   1 
ATOM   3483 C CA  . LYS C 1 147 ? 45.443  23.952  21.625 1.00 10.18 ? 164 LYS C CA  1 
ATOM   3484 C C   . LYS C 1 147 ? 44.198  23.706  22.470 1.00 9.59  ? 164 LYS C C   1 
ATOM   3485 O O   . LYS C 1 147 ? 44.282  23.628  23.698 1.00 9.94  ? 164 LYS C O   1 
ATOM   3486 C CB  . LYS C 1 147 ? 46.298  22.686  21.595 1.00 15.20 ? 164 LYS C CB  1 
ATOM   3487 C CG  . LYS C 1 147 ? 45.621  21.450  21.050 1.00 20.18 ? 164 LYS C CG  1 
ATOM   3488 C CD  . LYS C 1 147 ? 46.533  20.232  21.273 1.00 29.68 ? 164 LYS C CD  1 
ATOM   3489 C CE  . LYS C 1 147 ? 45.891  18.945  20.816 1.00 37.56 ? 164 LYS C CE  1 
ATOM   3490 N NZ  . LYS C 1 147 ? 45.597  19.012  19.380 1.00 43.47 ? 164 LYS C NZ  1 
ATOM   3491 N N   . LEU C 1 148 ? 43.046  23.564  21.820 1.00 10.44 ? 165 LEU C N   1 
ATOM   3492 C CA  . LEU C 1 148 ? 41.826  23.189  22.533 1.00 9.07  ? 165 LEU C CA  1 
ATOM   3493 C C   . LEU C 1 148 ? 41.906  21.742  23.012 1.00 9.69  ? 165 LEU C C   1 
ATOM   3494 O O   . LEU C 1 148 ? 42.265  20.830  22.255 1.00 10.25 ? 165 LEU C O   1 
ATOM   3495 C CB  . LEU C 1 148 ? 40.594  23.367  21.641 1.00 10.10 ? 165 LEU C CB  1 
ATOM   3496 C CG  . LEU C 1 148 ? 40.184  24.806  21.307 1.00 13.25 ? 165 LEU C CG  1 
ATOM   3497 C CD1 . LEU C 1 148 ? 39.056  24.804  20.265 1.00 13.18 ? 165 LEU C CD1 1 
ATOM   3498 C CD2 . LEU C 1 148 ? 39.759  25.563  22.559 1.00 11.84 ? 165 LEU C CD2 1 
ATOM   3499 N N   . ALA C 1 149 ? 41.539  21.542  24.275 1.00 11.15 ? 166 ALA C N   1 
ATOM   3500 C CA  . ALA C 1 149 ? 41.574  20.221  24.890 1.00 13.67 ? 166 ALA C CA  1 
ATOM   3501 C C   . ALA C 1 149 ? 40.661  19.218  24.192 1.00 13.62 ? 166 ALA C C   1 
ATOM   3502 O O   . ALA C 1 149 ? 40.965  18.019  24.184 1.00 12.31 ? 166 ALA C O   1 
ATOM   3503 C CB  . ALA C 1 149 ? 41.193  20.347  26.366 1.00 16.77 ? 166 ALA C CB  1 
ATOM   3504 N N   . LEU C 1 150 ? 39.541  19.667  23.616 1.00 10.42 ? 167 LEU C N   1 
ATOM   3505 C CA  . LEU C 1 150 ? 38.609  18.786  22.914 1.00 9.78  ? 167 LEU C CA  1 
ATOM   3506 C C   . LEU C 1 150 ? 38.962  18.606  21.437 1.00 8.84  ? 167 LEU C C   1 
ATOM   3507 O O   . LEU C 1 150 ? 38.134  18.105  20.671 1.00 9.40  ? 167 LEU C O   1 
ATOM   3508 C CB  . LEU C 1 150 ? 37.173  19.294  23.062 1.00 15.29 ? 167 LEU C CB  1 
ATOM   3509 C CG  . LEU C 1 150 ? 36.464  18.911  24.367 1.00 15.78 ? 167 LEU C CG  1 
ATOM   3510 C CD1 . LEU C 1 150 ? 35.249  19.786  24.559 1.00 18.77 ? 167 LEU C CD1 1 
ATOM   3511 C CD2 . LEU C 1 150 ? 36.058  17.433  24.385 1.00 18.84 ? 167 LEU C CD2 1 
ATOM   3512 N N   . SER C 1 151 ? 40.201  18.944  21.045 1.00 10.40 ? 168 SER C N   1 
ATOM   3513 C CA  A SER C 1 151 ? 40.599  18.894  19.638 0.45 11.69 ? 168 SER C CA  1 
ATOM   3514 C CA  B SER C 1 151 ? 40.589  18.897  19.636 0.55 10.82 ? 168 SER C CA  1 
ATOM   3515 C C   . SER C 1 151 ? 40.295  17.547  18.990 1.00 11.73 ? 168 SER C C   1 
ATOM   3516 O O   . SER C 1 151 ? 39.857  17.490  17.837 1.00 11.40 ? 168 SER C O   1 
ATOM   3517 C CB  A SER C 1 151 ? 42.094  19.204  19.532 0.45 13.65 ? 168 SER C CB  1 
ATOM   3518 C CB  B SER C 1 151 ? 42.078  19.226  19.492 0.55 12.22 ? 168 SER C CB  1 
ATOM   3519 O OG  A SER C 1 151 ? 42.570  19.039  18.208 0.45 15.87 ? 168 SER C OG  1 
ATOM   3520 O OG  B SER C 1 151 ? 42.323  20.618  19.631 0.55 14.71 ? 168 SER C OG  1 
ATOM   3521 N N   . ASP C 1 152 ? 40.540  16.447  19.705 1.00 11.21 ? 169 ASP C N   1 
ATOM   3522 C CA  . ASP C 1 152 ? 40.327  15.129  19.120 1.00 12.59 ? 169 ASP C CA  1 
ATOM   3523 C C   . ASP C 1 152 ? 38.865  14.890  18.769 1.00 11.11 ? 169 ASP C C   1 
ATOM   3524 O O   . ASP C 1 152 ? 38.577  14.016  17.937 1.00 11.59 ? 169 ASP C O   1 
ATOM   3525 C CB  . ASP C 1 152 ? 40.758  14.026  20.090 1.00 15.46 ? 169 ASP C CB  1 
ATOM   3526 C CG  . ASP C 1 152 ? 42.258  13.984  20.323 1.00 26.42 ? 169 ASP C CG  1 
ATOM   3527 O OD1 . ASP C 1 152 ? 43.022  14.495  19.476 1.00 29.88 ? 169 ASP C OD1 1 
ATOM   3528 O OD2 . ASP C 1 152 ? 42.666  13.410  21.358 1.00 30.56 ? 169 ASP C OD2 1 
ATOM   3529 N N   . TYR C 1 153 ? 37.937  15.614  19.405 1.00 10.42 ? 170 TYR C N   1 
ATOM   3530 C CA  . TYR C 1 153 ? 36.504  15.454  19.185 1.00 9.33  ? 170 TYR C CA  1 
ATOM   3531 C C   . TYR C 1 153 ? 35.927  16.536  18.294 1.00 9.15  ? 170 TYR C C   1 
ATOM   3532 O O   . TYR C 1 153 ? 34.725  16.519  18.021 1.00 11.62 ? 170 TYR C O   1 
ATOM   3533 C CB  . TYR C 1 153 ? 35.758  15.355  20.533 1.00 9.87  ? 170 TYR C CB  1 
ATOM   3534 C CG  . TYR C 1 153 ? 36.190  14.094  21.253 1.00 9.68  ? 170 TYR C CG  1 
ATOM   3535 C CD1 . TYR C 1 153 ? 35.674  12.864  20.895 1.00 10.58 ? 170 TYR C CD1 1 
ATOM   3536 C CD2 . TYR C 1 153 ? 37.207  14.124  22.201 1.00 10.90 ? 170 TYR C CD2 1 
ATOM   3537 C CE1 . TYR C 1 153 ? 36.133  11.707  21.476 1.00 11.45 ? 170 TYR C CE1 1 
ATOM   3538 C CE2 . TYR C 1 153 ? 37.641  12.983  22.803 1.00 13.12 ? 170 TYR C CE2 1 
ATOM   3539 C CZ  . TYR C 1 153 ? 37.106  11.775  22.441 1.00 11.39 ? 170 TYR C CZ  1 
ATOM   3540 O OH  . TYR C 1 153 ? 37.553  10.613  23.053 1.00 15.17 ? 170 TYR C OH  1 
ATOM   3541 N N   . ILE C 1 154 ? 36.765  17.447  17.815 1.00 10.55 ? 171 ILE C N   1 
ATOM   3542 C CA  . ILE C 1 154 ? 36.356  18.505  16.904 1.00 12.21 ? 171 ILE C CA  1 
ATOM   3543 C C   . ILE C 1 154 ? 36.903  18.281  15.499 1.00 13.30 ? 171 ILE C C   1 
ATOM   3544 O O   . ILE C 1 154 ? 36.207  18.512  14.508 1.00 13.86 ? 171 ILE C O   1 
ATOM   3545 C CB  . ILE C 1 154 ? 36.801  19.880  17.455 1.00 12.33 ? 171 ILE C CB  1 
ATOM   3546 C CG1 . ILE C 1 154 ? 36.167  20.162  18.819 1.00 12.75 ? 171 ILE C CG1 1 
ATOM   3547 C CG2 . ILE C 1 154 ? 36.476  21.014  16.475 1.00 15.63 ? 171 ILE C CG2 1 
ATOM   3548 C CD1 . ILE C 1 154 ? 36.827  21.303  19.564 1.00 15.32 ? 171 ILE C CD1 1 
ATOM   3549 N N   . PHE C 1 155 ? 38.142  17.835  15.388 1.00 12.89 ? 172 PHE C N   1 
ATOM   3550 C CA  . PHE C 1 155 ? 38.817  17.735  14.104 1.00 13.10 ? 172 PHE C CA  1 
ATOM   3551 C C   . PHE C 1 155 ? 38.932  16.283  13.680 1.00 16.58 ? 172 PHE C C   1 
ATOM   3552 O O   . PHE C 1 155 ? 39.107  15.393  14.515 1.00 19.67 ? 172 PHE C O   1 
ATOM   3553 C CB  . PHE C 1 155 ? 40.201  18.373  14.175 1.00 12.89 ? 172 PHE C CB  1 
ATOM   3554 C CG  . PHE C 1 155 ? 40.163  19.800  14.616 1.00 11.74 ? 172 PHE C CG  1 
ATOM   3555 C CD1 . PHE C 1 155 ? 39.625  20.765  13.794 1.00 11.89 ? 172 PHE C CD1 1 
ATOM   3556 C CD2 . PHE C 1 155 ? 40.624  20.173  15.865 1.00 13.83 ? 172 PHE C CD2 1 
ATOM   3557 C CE1 . PHE C 1 155 ? 39.559  22.082  14.207 1.00 13.38 ? 172 PHE C CE1 1 
ATOM   3558 C CE2 . PHE C 1 155 ? 40.568  21.477  16.270 1.00 15.57 ? 172 PHE C CE2 1 
ATOM   3559 C CZ  . PHE C 1 155 ? 40.025  22.432  15.442 1.00 13.77 ? 172 PHE C CZ  1 
ATOM   3560 N N   . GLU C 1 156 ? 38.792  16.065  12.377 1.00 21.15 ? 173 GLU C N   1 
ATOM   3561 C CA  . GLU C 1 156 ? 39.001  14.768  11.756 1.00 29.22 ? 173 GLU C CA  1 
ATOM   3562 C C   . GLU C 1 156 ? 40.380  14.215  12.068 1.00 35.72 ? 173 GLU C C   1 
ATOM   3563 O O   . GLU C 1 156 ? 40.601  13.005  11.985 1.00 37.85 ? 173 GLU C O   1 
ATOM   3564 C CB  . GLU C 1 156 ? 38.860  14.900  10.240 1.00 31.30 ? 173 GLU C CB  1 
ATOM   3565 C CG  . GLU C 1 156 ? 37.560  14.407  9.717  1.00 35.67 ? 173 GLU C CG  1 
ATOM   3566 C CD  . GLU C 1 156 ? 37.300  14.859  8.305  1.00 34.41 ? 173 GLU C CD  1 
ATOM   3567 O OE1 . GLU C 1 156 ? 38.234  14.830  7.461  1.00 37.96 ? 173 GLU C OE1 1 
ATOM   3568 O OE2 . GLU C 1 156 ? 36.156  15.255  8.047  1.00 26.53 ? 173 GLU C OE2 1 
ATOM   3569 O OXT . GLU C 1 156 ? 41.304  14.964  12.394 1.00 36.61 ? 173 GLU C OXT 1 
HETATM 3570 S S   . SO4 D 2 .   ? -1.404  29.641  8.434  1.00 14.06 ? 201 SO4 A S   1 
HETATM 3571 O O1  . SO4 D 2 .   ? -0.236  30.578  8.379  1.00 19.30 ? 201 SO4 A O1  1 
HETATM 3572 O O2  . SO4 D 2 .   ? -2.233  29.961  7.232  1.00 18.03 ? 201 SO4 A O2  1 
HETATM 3573 O O3  . SO4 D 2 .   ? -0.960  28.229  8.504  1.00 19.91 ? 201 SO4 A O3  1 
HETATM 3574 O O4  . SO4 D 2 .   ? -2.133  29.998  9.693  1.00 23.68 ? 201 SO4 A O4  1 
HETATM 3575 S S   . SO4 E 2 .   ? 4.119   34.443  2.199  1.00 24.03 ? 202 SO4 A S   1 
HETATM 3576 O O1  . SO4 E 2 .   ? 5.505   34.301  1.635  1.00 23.80 ? 202 SO4 A O1  1 
HETATM 3577 O O2  . SO4 E 2 .   ? 3.222   34.960  1.101  1.00 29.44 ? 202 SO4 A O2  1 
HETATM 3578 O O3  . SO4 E 2 .   ? 3.610   33.101  2.652  1.00 21.43 ? 202 SO4 A O3  1 
HETATM 3579 O O4  . SO4 E 2 .   ? 4.140   35.453  3.295  1.00 22.85 ? 202 SO4 A O4  1 
HETATM 3580 S S   . SO4 F 2 .   ? 8.128   58.208  23.466 1.00 44.88 ? 203 SO4 A S   1 
HETATM 3581 O O1  . SO4 F 2 .   ? 7.990   58.115  21.972 1.00 49.49 ? 203 SO4 A O1  1 
HETATM 3582 O O2  . SO4 F 2 .   ? 6.786   58.543  24.051 1.00 45.27 ? 203 SO4 A O2  1 
HETATM 3583 O O3  . SO4 F 2 .   ? 8.666   56.910  24.021 1.00 36.30 ? 203 SO4 A O3  1 
HETATM 3584 O O4  . SO4 F 2 .   ? 9.093   59.319  23.797 1.00 46.12 ? 203 SO4 A O4  1 
HETATM 3585 S S   . SO4 G 2 .   ? 27.010  10.417  8.747  1.00 15.48 ? 201 SO4 B S   1 
HETATM 3586 O O1  . SO4 G 2 .   ? 28.151  11.369  8.668  1.00 22.70 ? 201 SO4 B O1  1 
HETATM 3587 O O2  . SO4 G 2 .   ? 27.001  9.489   7.582  1.00 20.01 ? 201 SO4 B O2  1 
HETATM 3588 O O3  . SO4 G 2 .   ? 27.031  9.676   10.050 1.00 23.33 ? 201 SO4 B O3  1 
HETATM 3589 O O4  . SO4 G 2 .   ? 25.693  11.150  8.677  1.00 19.88 ? 201 SO4 B O4  1 
HETATM 3590 S S   . SO4 H 2 .   ? 19.398  12.513  3.193  1.00 45.39 ? 202 SO4 B S   1 
HETATM 3591 O O1  . SO4 H 2 .   ? 20.848  12.159  3.073  1.00 47.81 ? 202 SO4 B O1  1 
HETATM 3592 O O2  . SO4 H 2 .   ? 18.690  12.151  1.920  1.00 47.30 ? 202 SO4 B O2  1 
HETATM 3593 O O3  . SO4 H 2 .   ? 18.763  11.779  4.327  1.00 40.34 ? 202 SO4 B O3  1 
HETATM 3594 O O4  . SO4 H 2 .   ? 19.268  13.991  3.433  1.00 46.72 ? 202 SO4 B O4  1 
HETATM 3595 S S   . SO4 I 2 .   ? 12.155  5.942   2.655  1.00 58.73 ? 203 SO4 B S   1 
HETATM 3596 O O1  . SO4 I 2 .   ? 12.697  6.770   1.621  1.00 60.05 ? 203 SO4 B O1  1 
HETATM 3597 O O2  . SO4 I 2 .   ? 10.772  5.669   2.397  1.00 57.09 ? 203 SO4 B O2  1 
HETATM 3598 O O3  . SO4 I 2 .   ? 12.877  4.717   2.697  1.00 58.36 ? 203 SO4 B O3  1 
HETATM 3599 O O4  . SO4 I 2 .   ? 12.262  6.604   3.914  1.00 59.61 ? 203 SO4 B O4  1 
HETATM 3600 S S   . SO4 J 2 .   ? -0.493  5.343   27.279 1.00 49.35 ? 204 SO4 B S   1 
HETATM 3601 O O1  . SO4 J 2 .   ? -0.536  5.007   25.815 1.00 52.77 ? 204 SO4 B O1  1 
HETATM 3602 O O2  . SO4 J 2 .   ? -1.890  5.627   27.751 1.00 55.06 ? 204 SO4 B O2  1 
HETATM 3603 O O3  . SO4 J 2 .   ? 0.032   4.149   28.029 1.00 47.15 ? 204 SO4 B O3  1 
HETATM 3604 O O4  . SO4 J 2 .   ? 0.386   6.551   27.515 1.00 36.72 ? 204 SO4 B O4  1 
HETATM 3605 S S   . SO4 K 2 .   ? 29.407  44.587  6.303  1.00 16.84 ? 201 SO4 C S   1 
HETATM 3606 O O1  . SO4 K 2 .   ? 29.549  43.089  6.385  1.00 18.43 ? 201 SO4 C O1  1 
HETATM 3607 O O2  . SO4 K 2 .   ? 27.988  45.033  6.362  1.00 22.03 ? 201 SO4 C O2  1 
HETATM 3608 O O3  . SO4 K 2 .   ? 30.145  45.163  7.470  1.00 22.39 ? 201 SO4 C O3  1 
HETATM 3609 O O4  . SO4 K 2 .   ? 30.067  45.060  5.051  1.00 22.04 ? 201 SO4 C O4  1 
HETATM 3610 S S   . SO4 L 2 .   ? 31.058  36.401  1.223  1.00 60.72 ? 202 SO4 C S   1 
HETATM 3611 O O1  . SO4 L 2 .   ? 32.164  36.218  2.216  1.00 58.48 ? 202 SO4 C O1  1 
HETATM 3612 O O2  . SO4 L 2 .   ? 29.739  36.247  1.922  1.00 63.02 ? 202 SO4 C O2  1 
HETATM 3613 O O3  . SO4 L 2 .   ? 31.142  37.764  0.595  1.00 61.05 ? 202 SO4 C O3  1 
HETATM 3614 O O4  . SO4 L 2 .   ? 31.188  35.357  0.149  1.00 62.26 ? 202 SO4 C O4  1 
HETATM 3615 S S   . SO4 M 2 .   ? 39.704  33.042  -0.907 1.00 27.99 ? 203 SO4 C S   1 
HETATM 3616 O O1  . SO4 M 2 .   ? 39.793  31.554  -0.981 1.00 28.41 ? 203 SO4 C O1  1 
HETATM 3617 O O2  . SO4 M 2 .   ? 39.421  33.407  0.518  1.00 26.62 ? 203 SO4 C O2  1 
HETATM 3618 O O3  . SO4 M 2 .   ? 40.997  33.646  -1.364 1.00 31.03 ? 203 SO4 C O3  1 
HETATM 3619 O O4  . SO4 M 2 .   ? 38.584  33.511  -1.793 1.00 33.83 ? 203 SO4 C O4  1 
HETATM 3620 S S   . SO4 N 2 .   ? 49.482  24.194  23.989 1.00 44.05 ? 204 SO4 C S   1 
HETATM 3621 O O1  . SO4 N 2 .   ? 50.398  25.097  24.759 1.00 47.47 ? 204 SO4 C O1  1 
HETATM 3622 O O2  . SO4 N 2 .   ? 48.057  24.415  24.423 1.00 30.33 ? 204 SO4 C O2  1 
HETATM 3623 O O3  . SO4 N 2 .   ? 49.655  24.475  22.522 1.00 44.89 ? 204 SO4 C O3  1 
HETATM 3624 O O4  . SO4 N 2 .   ? 49.847  22.762  24.261 1.00 48.22 ? 204 SO4 C O4  1 
HETATM 3625 O O   . HOH O 3 .   ? -6.830  39.053  6.415  1.00 25.24 ? 301 HOH A O   1 
HETATM 3626 O O   . HOH O 3 .   ? 14.898  23.962  12.668 1.00 26.64 ? 302 HOH A O   1 
HETATM 3627 O O   . HOH O 3 .   ? -3.601  31.638  10.659 1.00 15.93 ? 303 HOH A O   1 
HETATM 3628 O O   . HOH O 3 .   ? 9.253   49.101  6.782  1.00 17.92 ? 304 HOH A O   1 
HETATM 3629 O O   . HOH O 3 .   ? -12.615 56.554  20.527 1.00 28.62 ? 305 HOH A O   1 
HETATM 3630 O O   . HOH O 3 .   ? -17.831 36.082  19.915 1.00 20.51 ? 306 HOH A O   1 
HETATM 3631 O O   . HOH O 3 .   ? 6.866   43.696  4.784  1.00 9.92  ? 307 HOH A O   1 
HETATM 3632 O O   . HOH O 3 .   ? 4.778   57.083  24.626 1.00 12.67 ? 308 HOH A O   1 
HETATM 3633 O O   . HOH O 3 .   ? 18.949  55.065  20.878 1.00 22.24 ? 309 HOH A O   1 
HETATM 3634 O O   . HOH O 3 .   ? -17.084 25.883  4.551  1.00 28.60 ? 310 HOH A O   1 
HETATM 3635 O O   . HOH O 3 .   ? -4.949  37.100  4.536  1.00 24.67 ? 311 HOH A O   1 
HETATM 3636 O O   . HOH O 3 .   ? 16.634  27.710  16.176 1.00 27.29 ? 312 HOH A O   1 
HETATM 3637 O O   . HOH O 3 .   ? -14.610 32.988  7.172  1.00 24.69 ? 313 HOH A O   1 
HETATM 3638 O O   . HOH O 3 .   ? 19.451  46.612  12.463 1.00 8.03  ? 314 HOH A O   1 
HETATM 3639 O O   . HOH O 3 .   ? -16.556 20.865  5.222  1.00 29.98 ? 315 HOH A O   1 
HETATM 3640 O O   . HOH O 3 .   ? 9.233   27.601  26.448 1.00 18.57 ? 316 HOH A O   1 
HETATM 3641 O O   . HOH O 3 .   ? 17.008  56.318  16.141 1.00 27.00 ? 317 HOH A O   1 
HETATM 3642 O O   . HOH O 3 .   ? -0.514  33.069  9.215  1.00 10.80 ? 318 HOH A O   1 
HETATM 3643 O O   . HOH O 3 .   ? -13.507 35.401  24.340 1.00 14.97 ? 319 HOH A O   1 
HETATM 3644 O O   . HOH O 3 .   ? 10.530  24.825  23.654 1.00 20.59 ? 320 HOH A O   1 
HETATM 3645 O O   . HOH O 3 .   ? 9.223   42.985  1.669  1.00 28.86 ? 321 HOH A O   1 
HETATM 3646 O O   . HOH O 3 .   ? 13.309  43.719  9.960  1.00 7.91  ? 322 HOH A O   1 
HETATM 3647 O O   . HOH O 3 .   ? -0.313  47.608  6.688  1.00 14.45 ? 323 HOH A O   1 
HETATM 3648 O O   . HOH O 3 .   ? 5.451   22.173  25.981 1.00 17.52 ? 324 HOH A O   1 
HETATM 3649 O O   . HOH O 3 .   ? 5.034   31.506  4.241  1.00 22.93 ? 325 HOH A O   1 
HETATM 3650 O O   . HOH O 3 .   ? -7.607  23.961  19.816 1.00 18.68 ? 326 HOH A O   1 
HETATM 3651 O O   . HOH O 3 .   ? -3.936  54.343  21.013 1.00 15.63 ? 327 HOH A O   1 
HETATM 3652 O O   . HOH O 3 .   ? -16.378 25.161  13.065 1.00 24.40 ? 328 HOH A O   1 
HETATM 3653 O O   . HOH O 3 .   ? -13.388 43.897  15.787 1.00 27.14 ? 329 HOH A O   1 
HETATM 3654 O O   . HOH O 3 .   ? 16.579  43.316  21.195 1.00 19.82 ? 330 HOH A O   1 
HETATM 3655 O O   . HOH O 3 .   ? 12.893  38.336  25.690 1.00 8.15  ? 331 HOH A O   1 
HETATM 3656 O O   . HOH O 3 .   ? 13.798  21.773  12.619 1.00 17.32 ? 332 HOH A O   1 
HETATM 3657 O O   . HOH O 3 .   ? -1.575  49.993  13.593 1.00 27.85 ? 333 HOH A O   1 
HETATM 3658 O O   . HOH O 3 .   ? 5.184   32.038  6.899  1.00 15.95 ? 334 HOH A O   1 
HETATM 3659 O O   . HOH O 3 .   ? 24.507  56.276  22.517 1.00 28.46 ? 335 HOH A O   1 
HETATM 3660 O O   . HOH O 3 .   ? -0.874  54.829  19.115 1.00 15.53 ? 336 HOH A O   1 
HETATM 3661 O O   . HOH O 3 .   ? 3.600   55.436  16.732 1.00 26.58 ? 337 HOH A O   1 
HETATM 3662 O O   . HOH O 3 .   ? 8.432   36.908  3.736  1.00 12.86 ? 338 HOH A O   1 
HETATM 3663 O O   . HOH O 3 .   ? 15.041  38.252  22.778 1.00 14.14 ? 339 HOH A O   1 
HETATM 3664 O O   . HOH O 3 .   ? -18.583 36.993  12.144 1.00 22.79 ? 340 HOH A O   1 
HETATM 3665 O O   . HOH O 3 .   ? 3.636   39.148  9.323  1.00 8.75  ? 341 HOH A O   1 
HETATM 3666 O O   . HOH O 3 .   ? -3.611  25.690  16.639 1.00 13.44 ? 342 HOH A O   1 
HETATM 3667 O O   . HOH O 3 .   ? 2.165   22.994  30.578 1.00 15.34 ? 343 HOH A O   1 
HETATM 3668 O O   . HOH O 3 .   ? -6.239  36.108  8.268  1.00 18.64 ? 344 HOH A O   1 
HETATM 3669 O O   . HOH O 3 .   ? -10.877 44.781  10.182 1.00 14.14 ? 345 HOH A O   1 
HETATM 3670 O O   . HOH O 3 .   ? 18.739  55.417  14.000 1.00 24.02 ? 346 HOH A O   1 
HETATM 3671 O O   . HOH O 3 .   ? 8.794   46.487  3.147  1.00 34.01 ? 347 HOH A O   1 
HETATM 3672 O O   . HOH O 3 .   ? 2.010   30.493  6.830  1.00 23.03 ? 348 HOH A O   1 
HETATM 3673 O O   . HOH O 3 .   ? 15.234  36.362  16.327 1.00 10.42 ? 349 HOH A O   1 
HETATM 3674 O O   . HOH O 3 .   ? 10.219  50.822  16.472 1.00 15.66 ? 350 HOH A O   1 
HETATM 3675 O O   . HOH O 3 .   ? -4.185  54.548  23.979 1.00 17.18 ? 351 HOH A O   1 
HETATM 3676 O O   . HOH O 3 .   ? 11.552  40.873  2.780  1.00 32.66 ? 352 HOH A O   1 
HETATM 3677 O O   . HOH O 3 .   ? 15.678  37.803  7.308  1.00 11.36 ? 353 HOH A O   1 
HETATM 3678 O O   . HOH O 3 .   ? 13.199  32.469  21.910 1.00 10.54 ? 354 HOH A O   1 
HETATM 3679 O O   . HOH O 3 .   ? 22.185  54.243  13.016 1.00 22.42 ? 355 HOH A O   1 
HETATM 3680 O O   . HOH O 3 .   ? 11.303  31.217  5.953  1.00 13.19 ? 356 HOH A O   1 
HETATM 3681 O O   . HOH O 3 .   ? 10.180  44.723  24.387 1.00 8.85  ? 357 HOH A O   1 
HETATM 3682 O O   . HOH O 3 .   ? 11.167  48.254  15.962 1.00 10.84 ? 358 HOH A O   1 
HETATM 3683 O O   . HOH O 3 .   ? 5.835   37.605  2.850  1.00 17.19 ? 359 HOH A O   1 
HETATM 3684 O O   . HOH O 3 .   ? 7.136   17.887  9.826  1.00 10.43 ? 360 HOH A O   1 
HETATM 3685 O O   . HOH O 3 .   ? 14.000  43.663  5.278  1.00 11.60 ? 361 HOH A O   1 
HETATM 3686 O O   . HOH O 3 .   ? 12.547  54.561  16.681 1.00 19.07 ? 362 HOH A O   1 
HETATM 3687 O O   . HOH O 3 .   ? -9.616  21.957  8.455  1.00 26.18 ? 363 HOH A O   1 
HETATM 3688 O O   . HOH O 3 .   ? -6.259  39.328  28.811 1.00 8.33  ? 364 HOH A O   1 
HETATM 3689 O O   . HOH O 3 .   ? 5.058   51.749  6.685  1.00 35.77 ? 365 HOH A O   1 
HETATM 3690 O O   . HOH O 3 .   ? -1.642  54.907  24.309 1.00 15.96 ? 366 HOH A O   1 
HETATM 3691 O O   . HOH O 3 .   ? 8.316   56.117  26.670 1.00 18.98 ? 367 HOH A O   1 
HETATM 3692 O O   . HOH O 3 .   ? -12.479 52.174  19.469 1.00 25.86 ? 368 HOH A O   1 
HETATM 3693 O O   . HOH O 3 .   ? -2.942  37.372  6.588  1.00 13.47 ? 369 HOH A O   1 
HETATM 3694 O O   . HOH O 3 .   ? -15.562 26.339  17.773 1.00 22.99 ? 370 HOH A O   1 
HETATM 3695 O O   . HOH O 3 .   ? -17.753 41.703  7.878  1.00 29.58 ? 371 HOH A O   1 
HETATM 3696 O O   . HOH O 3 .   ? 6.498   54.287  9.793  1.00 44.30 ? 372 HOH A O   1 
HETATM 3697 O O   . HOH O 3 .   ? 8.836   46.448  22.731 1.00 7.85  ? 373 HOH A O   1 
HETATM 3698 O O   . HOH O 3 .   ? 13.931  32.506  11.865 1.00 20.12 ? 374 HOH A O   1 
HETATM 3699 O O   . HOH O 3 .   ? 23.212  50.906  4.947  1.00 33.01 ? 375 HOH A O   1 
HETATM 3700 O O   . HOH O 3 .   ? 3.587   29.197  3.858  1.00 20.37 ? 376 HOH A O   1 
HETATM 3701 O O   . HOH O 3 .   ? 16.552  31.255  14.325 1.00 18.79 ? 377 HOH A O   1 
HETATM 3702 O O   . HOH O 3 .   ? -0.129  47.692  9.419  1.00 13.53 ? 378 HOH A O   1 
HETATM 3703 O O   . HOH O 3 .   ? -8.915  40.105  26.806 1.00 13.61 ? 379 HOH A O   1 
HETATM 3704 O O   . HOH O 3 .   ? 28.214  53.843  21.365 1.00 15.52 ? 380 HOH A O   1 
HETATM 3705 O O   . HOH O 3 .   ? -3.376  32.517  7.512  1.00 46.76 ? 381 HOH A O   1 
HETATM 3706 O O   . HOH O 3 .   ? -6.884  46.463  4.726  1.00 18.73 ? 382 HOH A O   1 
HETATM 3707 O O   . HOH O 3 .   ? 7.415   26.533  29.271 1.00 15.84 ? 383 HOH A O   1 
HETATM 3708 O O   . HOH O 3 .   ? 12.028  33.462  26.285 0.50 8.42  ? 384 HOH A O   1 
HETATM 3709 O O   . HOH O 3 .   ? 0.004   55.529  22.134 1.00 14.72 ? 385 HOH A O   1 
HETATM 3710 O O   . HOH O 3 .   ? 12.816  56.220  24.195 1.00 27.12 ? 386 HOH A O   1 
HETATM 3711 O O   . HOH O 3 .   ? 5.241   20.594  23.594 1.00 21.81 ? 387 HOH A O   1 
HETATM 3712 O O   . HOH O 3 .   ? -4.987  48.791  11.417 1.00 15.69 ? 388 HOH A O   1 
HETATM 3713 O O   . HOH O 3 .   ? -5.109  28.248  11.823 1.00 17.13 ? 389 HOH A O   1 
HETATM 3714 O O   . HOH O 3 .   ? 2.113   52.448  17.652 1.00 22.32 ? 390 HOH A O   1 
HETATM 3715 O O   . HOH O 3 .   ? -13.479 32.034  -0.313 1.00 28.31 ? 391 HOH A O   1 
HETATM 3716 O O   . HOH O 3 .   ? -2.262  25.710  12.899 1.00 15.20 ? 392 HOH A O   1 
HETATM 3717 O O   . HOH O 3 .   ? -1.184  32.278  5.870  1.00 23.54 ? 393 HOH A O   1 
HETATM 3718 O O   . HOH O 3 .   ? -10.997 42.304  23.039 1.00 31.01 ? 394 HOH A O   1 
HETATM 3719 O O   . HOH O 3 .   ? 15.450  49.607  23.401 1.00 12.40 ? 395 HOH A O   1 
HETATM 3720 O O   . HOH O 3 .   ? -8.985  36.287  5.636  1.00 16.73 ? 396 HOH A O   1 
HETATM 3721 O O   . HOH O 3 .   ? 17.597  56.382  24.415 1.00 27.73 ? 397 HOH A O   1 
HETATM 3722 O O   . HOH O 3 .   ? 4.518   19.584  7.818  1.00 10.79 ? 398 HOH A O   1 
HETATM 3723 O O   . HOH O 3 .   ? 8.438   54.294  17.795 1.00 29.52 ? 399 HOH A O   1 
HETATM 3724 O O   . HOH O 3 .   ? -1.843  28.884  4.554  1.00 35.47 ? 400 HOH A O   1 
HETATM 3725 O O   . HOH O 3 .   ? -8.770  48.834  9.089  1.00 28.86 ? 401 HOH A O   1 
HETATM 3726 O O   . HOH O 3 .   ? 18.988  40.924  20.768 1.00 16.10 ? 402 HOH A O   1 
HETATM 3727 O O   . HOH O 3 .   ? 11.156  52.673  18.367 1.00 14.56 ? 403 HOH A O   1 
HETATM 3728 O O   . HOH O 3 .   ? -5.462  33.794  6.994  1.00 35.80 ? 404 HOH A O   1 
HETATM 3729 O O   . HOH O 3 .   ? -17.913 29.731  5.475  1.00 20.61 ? 405 HOH A O   1 
HETATM 3730 O O   . HOH O 3 .   ? -13.513 21.291  7.977  1.00 18.94 ? 406 HOH A O   1 
HETATM 3731 O O   . HOH O 3 .   ? 10.444  28.451  5.678  1.00 11.86 ? 407 HOH A O   1 
HETATM 3732 O O   . HOH O 3 .   ? 1.918   49.644  9.429  1.00 17.08 ? 408 HOH A O   1 
HETATM 3733 O O   . HOH O 3 .   ? -23.439 35.535  2.217  1.00 30.87 ? 409 HOH A O   1 
HETATM 3734 O O   . HOH O 3 .   ? -10.052 40.880  20.362 1.00 24.48 ? 410 HOH A O   1 
HETATM 3735 O O   . HOH O 3 .   ? -10.928 40.002  24.882 1.00 34.13 ? 411 HOH A O   1 
HETATM 3736 O O   . HOH O 3 .   ? 7.296   29.351  2.689  1.00 27.01 ? 412 HOH A O   1 
HETATM 3737 O O   . HOH O 3 .   ? -4.571  25.522  14.225 1.00 25.25 ? 413 HOH A O   1 
HETATM 3738 O O   . HOH O 3 .   ? -14.283 30.193  22.476 1.00 18.29 ? 414 HOH A O   1 
HETATM 3739 O O   . HOH O 3 .   ? 17.195  34.231  3.237  1.00 23.60 ? 415 HOH A O   1 
HETATM 3740 O O   . HOH O 3 .   ? -6.986  49.177  15.828 1.00 21.71 ? 416 HOH A O   1 
HETATM 3741 O O   . HOH O 3 .   ? 4.411   39.743  3.320  1.00 23.83 ? 417 HOH A O   1 
HETATM 3742 O O   . HOH O 3 .   ? 1.524   23.616  1.880  1.00 29.11 ? 418 HOH A O   1 
HETATM 3743 O O   . HOH O 3 .   ? -16.355 38.461  6.905  1.00 38.31 ? 419 HOH A O   1 
HETATM 3744 O O   . HOH O 3 .   ? 14.649  36.924  1.983  1.00 29.39 ? 420 HOH A O   1 
HETATM 3745 O O   . HOH O 3 .   ? 13.161  29.938  20.621 1.00 17.80 ? 421 HOH A O   1 
HETATM 3746 O O   . HOH O 3 .   ? 12.338  32.677  14.141 1.00 18.10 ? 422 HOH A O   1 
HETATM 3747 O O   . HOH O 3 .   ? 6.635   54.230  16.115 1.00 33.21 ? 423 HOH A O   1 
HETATM 3748 O O   . HOH O 3 .   ? -12.837 25.217  22.431 1.00 33.90 ? 424 HOH A O   1 
HETATM 3749 O O   . HOH O 3 .   ? -12.291 42.685  8.792  1.00 27.75 ? 425 HOH A O   1 
HETATM 3750 O O   . HOH O 3 .   ? 7.604   24.993  26.577 1.00 23.62 ? 426 HOH A O   1 
HETATM 3751 O O   . HOH O 3 .   ? -6.640  26.070  12.632 1.00 20.03 ? 427 HOH A O   1 
HETATM 3752 O O   . HOH O 3 .   ? 9.619   25.699  1.746  1.00 21.29 ? 428 HOH A O   1 
HETATM 3753 O O   . HOH O 3 .   ? -23.031 34.064  4.563  1.00 23.10 ? 429 HOH A O   1 
HETATM 3754 O O   . HOH O 3 .   ? 3.388   59.051  20.640 1.00 23.34 ? 430 HOH A O   1 
HETATM 3755 O O   . HOH O 3 .   ? 2.319   43.648  1.125  1.00 29.25 ? 431 HOH A O   1 
HETATM 3756 O O   . HOH O 3 .   ? -8.209  25.106  22.109 1.00 20.23 ? 432 HOH A O   1 
HETATM 3757 O O   . HOH O 3 .   ? 8.065   31.500  5.231  1.00 24.39 ? 433 HOH A O   1 
HETATM 3758 O O   . HOH O 3 .   ? -6.899  41.078  3.386  1.00 31.50 ? 434 HOH A O   1 
HETATM 3759 O O   . HOH O 3 .   ? 13.882  33.322  9.184  1.00 27.96 ? 435 HOH A O   1 
HETATM 3760 O O   . HOH O 3 .   ? -1.928  34.878  6.987  1.00 20.01 ? 436 HOH A O   1 
HETATM 3761 O O   . HOH O 3 .   ? -11.050 48.774  15.467 1.00 21.79 ? 437 HOH A O   1 
HETATM 3762 O O   . HOH O 3 .   ? 0.926   19.089  7.299  1.00 24.92 ? 438 HOH A O   1 
HETATM 3763 O O   . HOH O 3 .   ? -3.933  52.733  26.384 1.00 20.61 ? 439 HOH A O   1 
HETATM 3764 O O   . HOH O 3 .   ? 14.978  26.473  18.619 1.00 39.41 ? 440 HOH A O   1 
HETATM 3765 O O   . HOH O 3 .   ? 4.419   51.746  12.173 1.00 29.66 ? 441 HOH A O   1 
HETATM 3766 O O   . HOH O 3 .   ? -11.732 46.362  17.449 1.00 22.27 ? 442 HOH A O   1 
HETATM 3767 O O   . HOH O 3 .   ? -4.857  28.470  9.075  1.00 27.97 ? 443 HOH A O   1 
HETATM 3768 O O   . HOH O 3 .   ? 1.737   16.917  8.014  1.00 30.03 ? 444 HOH A O   1 
HETATM 3769 O O   . HOH O 3 .   ? 12.501  26.079  2.979  1.00 25.30 ? 445 HOH A O   1 
HETATM 3770 O O   . HOH O 3 .   ? -15.449 26.811  -1.923 1.00 32.28 ? 446 HOH A O   1 
HETATM 3771 O O   . HOH O 3 .   ? 21.382  56.294  21.994 1.00 28.20 ? 447 HOH A O   1 
HETATM 3772 O O   . HOH O 3 .   ? 2.413   48.426  5.684  1.00 22.63 ? 448 HOH A O   1 
HETATM 3773 O O   . HOH O 3 .   ? 2.055   17.827  4.310  1.00 40.75 ? 449 HOH A O   1 
HETATM 3774 O O   . HOH O 3 .   ? 13.058  25.871  25.613 1.00 40.44 ? 450 HOH A O   1 
HETATM 3775 O O   . HOH O 3 .   ? 15.523  31.788  17.123 1.00 31.10 ? 451 HOH A O   1 
HETATM 3776 O O   . HOH O 3 .   ? -9.406  38.476  3.973  1.00 29.51 ? 452 HOH A O   1 
HETATM 3777 O O   . HOH O 3 .   ? 14.292  36.074  9.118  1.00 25.69 ? 453 HOH A O   1 
HETATM 3778 O O   . HOH O 3 .   ? -4.813  45.546  24.718 1.00 15.86 ? 454 HOH A O   1 
HETATM 3779 O O   . HOH O 3 .   ? 8.159   34.161  3.975  1.00 28.81 ? 455 HOH A O   1 
HETATM 3780 O O   . HOH O 3 .   ? -0.793  19.406  4.956  1.00 36.05 ? 456 HOH A O   1 
HETATM 3781 O O   . HOH O 3 .   ? 15.614  22.218  15.113 1.00 25.98 ? 457 HOH A O   1 
HETATM 3782 O O   . HOH O 3 .   ? -11.225 44.813  19.772 1.00 28.84 ? 458 HOH A O   1 
HETATM 3783 O O   . HOH O 3 .   ? -6.811  44.338  26.285 0.50 18.86 ? 459 HOH A O   1 
HETATM 3784 O O   . HOH O 3 .   ? 15.112  34.272  20.781 1.00 13.76 ? 460 HOH A O   1 
HETATM 3785 O O   . HOH O 3 .   ? -12.656 45.628  12.101 1.00 27.97 ? 461 HOH A O   1 
HETATM 3786 O O   . HOH O 3 .   ? -8.522  47.494  6.681  1.00 27.83 ? 462 HOH A O   1 
HETATM 3787 O O   . HOH O 3 .   ? -17.059 27.586  9.052  1.00 35.30 ? 463 HOH A O   1 
HETATM 3788 O O   . HOH O 3 .   ? -21.162 37.970  1.310  1.00 23.70 ? 464 HOH A O   1 
HETATM 3789 O O   . HOH O 3 .   ? 1.206   58.235  22.414 1.00 19.06 ? 465 HOH A O   1 
HETATM 3790 O O   . HOH O 3 .   ? -13.024 27.568  23.857 1.00 30.37 ? 466 HOH A O   1 
HETATM 3791 O O   . HOH O 3 .   ? 15.990  36.629  24.531 1.00 33.98 ? 467 HOH A O   1 
HETATM 3792 O O   . HOH O 3 .   ? 13.888  32.336  24.522 1.00 13.25 ? 468 HOH A O   1 
HETATM 3793 O O   . HOH O 3 .   ? -14.845 43.900  13.690 1.00 32.63 ? 469 HOH A O   1 
HETATM 3794 O O   . HOH O 3 .   ? 4.988   42.728  2.837  1.00 23.22 ? 470 HOH A O   1 
HETATM 3795 O O   . HOH O 3 .   ? 2.447   58.388  25.104 1.00 23.70 ? 471 HOH A O   1 
HETATM 3796 O O   . HOH O 3 .   ? -10.748 27.789  25.418 1.00 15.44 ? 472 HOH A O   1 
HETATM 3797 O O   . HOH O 3 .   ? 12.169  46.949  3.020  1.00 43.85 ? 473 HOH A O   1 
HETATM 3798 O O   . HOH O 3 .   ? -8.439  44.312  3.125  1.00 29.59 ? 474 HOH A O   1 
HETATM 3799 O O   . HOH O 3 .   ? 1.997   51.634  11.238 1.00 34.99 ? 475 HOH A O   1 
HETATM 3800 O O   . HOH O 3 .   ? 15.986  34.117  24.787 1.00 25.55 ? 476 HOH A O   1 
HETATM 3801 O O   . HOH O 3 .   ? 11.174  53.113  14.695 1.00 21.97 ? 477 HOH A O   1 
HETATM 3802 O O   . HOH O 3 .   ? 8.232   22.710  24.885 1.00 35.99 ? 478 HOH A O   1 
HETATM 3803 O O   . HOH O 3 .   ? -21.593 34.365  7.546  1.00 40.36 ? 479 HOH A O   1 
HETATM 3804 O O   . HOH O 3 .   ? -10.694 19.701  7.466  1.00 40.27 ? 480 HOH A O   1 
HETATM 3805 O O   . HOH O 3 .   ? -20.654 30.262  4.075  1.00 31.69 ? 481 HOH A O   1 
HETATM 3806 O O   . HOH O 3 .   ? -24.209 33.649  0.265  1.00 31.20 ? 482 HOH A O   1 
HETATM 3807 O O   . HOH O 3 .   ? 18.499  28.551  14.443 1.00 26.45 ? 483 HOH A O   1 
HETATM 3808 O O   . HOH O 3 .   ? -18.536 34.047  6.650  1.00 29.66 ? 484 HOH A O   1 
HETATM 3809 O O   . HOH O 3 .   ? -14.633 33.691  25.918 1.00 18.00 ? 485 HOH A O   1 
HETATM 3810 O O   . HOH O 3 .   ? 4.181   18.413  5.579  1.00 35.79 ? 486 HOH A O   1 
HETATM 3811 O O   . HOH O 3 .   ? -15.193 24.027  19.218 1.00 32.17 ? 487 HOH A O   1 
HETATM 3812 O O   . HOH O 3 .   ? -13.237 50.038  17.308 1.00 33.72 ? 488 HOH A O   1 
HETATM 3813 O O   . HOH O 3 .   ? -12.660 43.857  5.979  1.00 43.07 ? 489 HOH A O   1 
HETATM 3814 O O   . HOH O 3 .   ? -2.142  49.069  10.722 1.00 19.28 ? 490 HOH A O   1 
HETATM 3815 O O   . HOH O 3 .   ? 2.564   50.875  7.036  1.00 21.83 ? 491 HOH A O   1 
HETATM 3816 O O   . HOH O 3 .   ? -17.251 31.781  7.182  1.00 22.25 ? 492 HOH A O   1 
HETATM 3817 O O   . HOH O 3 .   ? -17.161 26.112  15.464 1.00 22.58 ? 493 HOH A O   1 
HETATM 3818 O O   . HOH O 3 .   ? 12.370  35.912  1.654  1.00 36.23 ? 494 HOH A O   1 
HETATM 3819 O O   . HOH O 3 .   ? -17.980 27.152  6.602  1.00 25.87 ? 495 HOH A O   1 
HETATM 3820 O O   . HOH O 3 .   ? -17.963 26.484  11.204 1.00 35.24 ? 496 HOH A O   1 
HETATM 3821 O O   . HOH O 3 .   ? 15.850  33.990  18.136 1.00 19.51 ? 497 HOH A O   1 
HETATM 3822 O O   . HOH O 3 .   ? 4.301   15.833  6.883  1.00 20.16 ? 498 HOH A O   1 
HETATM 3823 O O   . HOH O 3 .   ? 13.651  31.560  4.315  1.00 27.33 ? 499 HOH A O   1 
HETATM 3824 O O   . HOH O 3 .   ? 13.005  53.708  12.152 1.00 30.38 ? 500 HOH A O   1 
HETATM 3825 O O   . HOH O 3 .   ? 12.118  33.329  2.358  1.00 30.97 ? 501 HOH A O   1 
HETATM 3826 O O   . HOH O 3 .   ? -14.853 30.912  25.339 1.00 30.61 ? 502 HOH A O   1 
HETATM 3827 O O   . HOH P 3 .   ? 13.368  2.484   2.724  1.00 24.53 ? 301 HOH B O   1 
HETATM 3828 O O   . HOH P 3 .   ? 23.751  -7.013  11.857 1.00 35.85 ? 302 HOH B O   1 
HETATM 3829 O O   . HOH P 3 .   ? -3.983  13.612  19.460 1.00 28.52 ? 303 HOH B O   1 
HETATM 3830 O O   . HOH P 3 .   ? 10.339  10.346  6.726  1.00 10.52 ? 304 HOH B O   1 
HETATM 3831 O O   . HOH P 3 .   ? 28.824  -9.551  10.359 1.00 33.71 ? 305 HOH B O   1 
HETATM 3832 O O   . HOH P 3 .   ? 26.783  7.461   11.196 1.00 17.79 ? 306 HOH B O   1 
HETATM 3833 O O   . HOH P 3 .   ? -2.289  8.103   27.525 1.00 33.31 ? 307 HOH B O   1 
HETATM 3834 O O   . HOH P 3 .   ? 22.495  12.706  1.244  1.00 39.80 ? 308 HOH B O   1 
HETATM 3835 O O   . HOH P 3 .   ? 12.293  8.984   4.768  1.00 22.13 ? 309 HOH B O   1 
HETATM 3836 O O   . HOH P 3 .   ? 0.825   3.861   24.016 1.00 43.76 ? 310 HOH B O   1 
HETATM 3837 O O   . HOH P 3 .   ? 9.180   -3.247  19.959 1.00 30.54 ? 311 HOH B O   1 
HETATM 3838 O O   . HOH P 3 .   ? 8.049   -1.425  28.726 1.00 23.80 ? 312 HOH B O   1 
HETATM 3839 O O   . HOH P 3 .   ? 26.368  15.757  2.455  1.00 34.21 ? 313 HOH B O   1 
HETATM 3840 O O   . HOH P 3 .   ? 2.379   2.966   28.378 1.00 18.18 ? 314 HOH B O   1 
HETATM 3841 O O   . HOH P 3 .   ? 6.737   0.217   21.790 1.00 21.24 ? 315 HOH B O   1 
HETATM 3842 O O   . HOH P 3 .   ? 26.576  27.692  11.844 1.00 22.01 ? 316 HOH B O   1 
HETATM 3843 O O   . HOH P 3 .   ? 31.885  21.222  25.015 1.00 17.61 ? 317 HOH B O   1 
HETATM 3844 O O   . HOH P 3 .   ? 20.311  27.300  16.081 1.00 27.29 ? 318 HOH B O   1 
HETATM 3845 O O   . HOH P 3 .   ? 30.765  11.464  8.538  1.00 22.32 ? 319 HOH B O   1 
HETATM 3846 O O   . HOH P 3 .   ? -5.367  18.815  16.480 1.00 24.40 ? 320 HOH B O   1 
HETATM 3847 O O   . HOH P 3 .   ? 25.448  21.810  26.282 1.00 22.10 ? 321 HOH B O   1 
HETATM 3848 O O   . HOH P 3 .   ? 9.222   12.612  3.554  1.00 24.25 ? 322 HOH B O   1 
HETATM 3849 O O   . HOH P 3 .   ? 34.802  9.667   11.872 1.00 28.58 ? 323 HOH B O   1 
HETATM 3850 O O   . HOH P 3 .   ? 30.233  -7.672  13.442 1.00 31.63 ? 324 HOH B O   1 
HETATM 3851 O O   . HOH P 3 .   ? 26.750  24.130  23.032 1.00 17.61 ? 325 HOH B O   1 
HETATM 3852 O O   . HOH P 3 .   ? 18.087  26.906  7.766  1.00 29.49 ? 326 HOH B O   1 
HETATM 3853 O O   . HOH P 3 .   ? -7.258  20.760  25.900 1.00 25.60 ? 327 HOH B O   1 
HETATM 3854 O O   . HOH P 3 .   ? 21.270  -6.511  17.966 1.00 33.93 ? 328 HOH B O   1 
HETATM 3855 O O   . HOH P 3 .   ? 7.720   19.979  23.085 1.00 24.63 ? 329 HOH B O   1 
HETATM 3856 O O   . HOH P 3 .   ? 16.481  10.046  10.669 1.00 9.65  ? 330 HOH B O   1 
HETATM 3857 O O   . HOH P 3 .   ? 24.271  20.774  1.679  1.00 35.70 ? 331 HOH B O   1 
HETATM 3858 O O   . HOH P 3 .   ? 14.396  -5.406  11.641 1.00 26.63 ? 332 HOH B O   1 
HETATM 3859 O O   . HOH P 3 .   ? 2.619   20.446  14.738 1.00 9.11  ? 333 HOH B O   1 
HETATM 3860 O O   . HOH P 3 .   ? 32.503  10.992  16.422 1.00 15.93 ? 334 HOH B O   1 
HETATM 3861 O O   . HOH P 3 .   ? 14.664  -3.622  18.240 1.00 28.76 ? 335 HOH B O   1 
HETATM 3862 O O   . HOH P 3 .   ? 24.320  12.999  7.263  1.00 25.16 ? 336 HOH B O   1 
HETATM 3863 O O   . HOH P 3 .   ? 21.176  5.140   7.784  1.00 14.38 ? 337 HOH B O   1 
HETATM 3864 O O   . HOH P 3 .   ? 26.283  -10.421 13.756 1.00 25.10 ? 338 HOH B O   1 
HETATM 3865 O O   . HOH P 3 .   ? 32.186  17.383  17.253 1.00 9.71  ? 339 HOH B O   1 
HETATM 3866 O O   . HOH P 3 .   ? 14.292  19.515  26.916 1.00 8.94  ? 340 HOH B O   1 
HETATM 3867 O O   . HOH P 3 .   ? 10.134  13.935  26.337 1.00 9.76  ? 341 HOH B O   1 
HETATM 3868 O O   . HOH P 3 .   ? 17.400  25.463  14.674 1.00 22.00 ? 342 HOH B O   1 
HETATM 3869 O O   . HOH P 3 .   ? 33.498  18.185  29.856 1.00 18.86 ? 343 HOH B O   1 
HETATM 3870 O O   . HOH P 3 .   ? 29.879  -1.973  25.232 1.00 16.74 ? 344 HOH B O   1 
HETATM 3871 O O   . HOH P 3 .   ? 15.497  14.927  4.885  1.00 15.73 ? 345 HOH B O   1 
HETATM 3872 O O   . HOH P 3 .   ? 1.973   22.762  17.976 1.00 10.47 ? 346 HOH B O   1 
HETATM 3873 O O   . HOH P 3 .   ? 7.738   16.318  11.958 1.00 9.59  ? 347 HOH B O   1 
HETATM 3874 O O   . HOH P 3 .   ? 16.767  -4.298  28.280 1.00 29.36 ? 348 HOH B O   1 
HETATM 3875 O O   . HOH P 3 .   ? 11.351  21.069  8.645  1.00 11.23 ? 349 HOH B O   1 
HETATM 3876 O O   . HOH P 3 .   ? 4.785   9.903   9.413  1.00 17.81 ? 350 HOH B O   1 
HETATM 3877 O O   . HOH P 3 .   ? 35.528  -4.090  6.297  1.00 34.21 ? 351 HOH B O   1 
HETATM 3878 O O   . HOH P 3 .   ? 23.807  9.566   9.886  1.00 15.81 ? 352 HOH B O   1 
HETATM 3879 O O   . HOH P 3 .   ? 23.789  -0.081  28.270 1.00 14.69 ? 353 HOH B O   1 
HETATM 3880 O O   . HOH P 3 .   ? 19.706  -5.138  12.123 1.00 18.70 ? 354 HOH B O   1 
HETATM 3881 O O   . HOH P 3 .   ? 25.268  0.485   6.802  1.00 27.22 ? 355 HOH B O   1 
HETATM 3882 O O   . HOH P 3 .   ? 5.682   12.563  18.382 1.00 9.94  ? 356 HOH B O   1 
HETATM 3883 O O   . HOH P 3 .   ? 13.932  22.053  17.373 1.00 10.10 ? 357 HOH B O   1 
HETATM 3884 O O   . HOH P 3 .   ? -0.491  10.512  19.980 1.00 20.52 ? 358 HOH B O   1 
HETATM 3885 O O   . HOH P 3 .   ? 11.270  2.646   11.914 1.00 21.17 ? 359 HOH B O   1 
HETATM 3886 O O   . HOH P 3 .   ? -3.468  14.673  27.709 1.00 32.52 ? 360 HOH B O   1 
HETATM 3887 O O   . HOH P 3 .   ? 19.128  20.388  6.390  1.00 12.38 ? 361 HOH B O   1 
HETATM 3888 O O   . HOH P 3 .   ? 38.707  5.096   20.076 1.00 31.85 ? 362 HOH B O   1 
HETATM 3889 O O   . HOH P 3 .   ? 15.247  -3.033  7.174  1.00 24.49 ? 363 HOH B O   1 
HETATM 3890 O O   . HOH P 3 .   ? 32.916  23.643  8.444  1.00 10.64 ? 364 HOH B O   1 
HETATM 3891 O O   . HOH P 3 .   ? 3.912   10.517  19.090 1.00 12.75 ? 365 HOH B O   1 
HETATM 3892 O O   . HOH P 3 .   ? 18.773  22.503  22.387 1.00 10.84 ? 366 HOH B O   1 
HETATM 3893 O O   . HOH P 3 .   ? 17.988  16.097  4.709  1.00 22.32 ? 367 HOH B O   1 
HETATM 3894 O O   . HOH P 3 .   ? 3.127   4.366   21.765 1.00 27.00 ? 368 HOH B O   1 
HETATM 3895 O O   . HOH P 3 .   ? 39.658  0.260   13.312 1.00 31.69 ? 369 HOH B O   1 
HETATM 3896 O O   . HOH P 3 .   ? 27.540  20.903  28.988 1.00 14.90 ? 370 HOH B O   1 
HETATM 3897 O O   . HOH P 3 .   ? 14.668  2.432   25.957 1.00 11.66 ? 371 HOH B O   1 
HETATM 3898 O O   . HOH P 3 .   ? 36.697  8.644   19.524 1.00 27.11 ? 372 HOH B O   1 
HETATM 3899 O O   . HOH P 3 .   ? 18.977  21.230  26.822 1.00 7.50  ? 373 HOH B O   1 
HETATM 3900 O O   . HOH P 3 .   ? 1.533   6.864   30.056 1.00 20.31 ? 374 HOH B O   1 
HETATM 3901 O O   . HOH P 3 .   ? 12.867  21.300  23.973 1.00 14.50 ? 375 HOH B O   1 
HETATM 3902 O O   . HOH P 3 .   ? 10.998  2.097   9.216  1.00 22.14 ? 376 HOH B O   1 
HETATM 3903 O O   . HOH P 3 .   ? 2.286   7.094   21.098 1.00 28.46 ? 377 HOH B O   1 
HETATM 3904 O O   . HOH P 3 .   ? 26.278  24.105  1.081  1.00 43.52 ? 378 HOH B O   1 
HETATM 3905 O O   . HOH P 3 .   ? 22.031  -5.282  10.778 1.00 27.69 ? 379 HOH B O   1 
HETATM 3906 O O   . HOH P 3 .   ? 9.123   11.799  24.944 1.00 8.29  ? 380 HOH B O   1 
HETATM 3907 O O   . HOH P 3 .   ? 38.248  0.459   18.082 1.00 23.57 ? 381 HOH B O   1 
HETATM 3908 O O   . HOH P 3 .   ? -1.054  10.445  27.493 1.00 21.48 ? 382 HOH B O   1 
HETATM 3909 O O   . HOH P 3 .   ? 30.560  8.200   12.030 1.00 17.76 ? 383 HOH B O   1 
HETATM 3910 O O   . HOH P 3 .   ? 5.959   -0.258  26.304 1.00 22.50 ? 384 HOH B O   1 
HETATM 3911 O O   . HOH P 3 .   ? 17.131  22.539  12.374 1.00 27.38 ? 385 HOH B O   1 
HETATM 3912 O O   . HOH P 3 .   ? 35.674  7.508   21.633 1.00 34.90 ? 386 HOH B O   1 
HETATM 3913 O O   . HOH P 3 .   ? 21.702  14.823  4.622  1.00 44.54 ? 387 HOH B O   1 
HETATM 3914 O O   . HOH P 3 .   ? -7.062  25.049  24.493 1.00 16.20 ? 388 HOH B O   1 
HETATM 3915 O O   . HOH P 3 .   ? 24.432  9.203   6.410  1.00 31.16 ? 389 HOH B O   1 
HETATM 3916 O O   . HOH P 3 .   ? 16.003  12.364  3.949  1.00 20.13 ? 390 HOH B O   1 
HETATM 3917 O O   . HOH P 3 .   ? 21.489  14.597  7.437  1.00 16.98 ? 391 HOH B O   1 
HETATM 3918 O O   . HOH P 3 .   ? 23.334  2.688   30.183 1.00 9.77  ? 392 HOH B O   1 
HETATM 3919 O O   . HOH P 3 .   ? 22.293  3.600   5.680  1.00 29.88 ? 393 HOH B O   1 
HETATM 3920 O O   . HOH P 3 .   ? 34.865  16.236  28.346 1.00 13.78 ? 394 HOH B O   1 
HETATM 3921 O O   . HOH P 3 .   ? 6.943   16.633  7.299  1.00 12.24 ? 395 HOH B O   1 
HETATM 3922 O O   . HOH P 3 .   ? 32.562  20.522  6.554  1.00 14.53 ? 396 HOH B O   1 
HETATM 3923 O O   . HOH P 3 .   ? 24.459  3.067   9.344  1.00 30.99 ? 397 HOH B O   1 
HETATM 3924 O O   . HOH P 3 .   ? 33.225  21.706  22.499 1.00 15.63 ? 398 HOH B O   1 
HETATM 3925 O O   . HOH P 3 .   ? 2.338   10.310  21.422 1.00 15.53 ? 399 HOH B O   1 
HETATM 3926 O O   . HOH P 3 .   ? 10.521  15.716  4.388  1.00 21.09 ? 400 HOH B O   1 
HETATM 3927 O O   . HOH P 3 .   ? 31.375  11.861  12.647 1.00 17.75 ? 401 HOH B O   1 
HETATM 3928 O O   . HOH P 3 .   ? 7.037   10.099  5.716  1.00 29.40 ? 402 HOH B O   1 
HETATM 3929 O O   . HOH P 3 .   ? 21.825  20.985  5.728  1.00 11.27 ? 403 HOH B O   1 
HETATM 3930 O O   . HOH P 3 .   ? 34.480  -0.195  22.874 1.00 16.90 ? 404 HOH B O   1 
HETATM 3931 O O   . HOH P 3 .   ? 28.684  21.767  26.054 1.00 25.46 ? 405 HOH B O   1 
HETATM 3932 O O   . HOH P 3 .   ? 18.133  21.214  14.687 1.00 17.77 ? 406 HOH B O   1 
HETATM 3933 O O   . HOH P 3 .   ? 15.607  -5.017  9.139  1.00 29.17 ? 407 HOH B O   1 
HETATM 3934 O O   . HOH P 3 .   ? 8.478   23.283  22.345 1.00 15.85 ? 408 HOH B O   1 
HETATM 3935 O O   . HOH P 3 .   ? 14.860  9.973   4.698  1.00 24.24 ? 409 HOH B O   1 
HETATM 3936 O O   . HOH P 3 .   ? 34.085  17.811  6.284  1.00 24.95 ? 410 HOH B O   1 
HETATM 3937 O O   . HOH P 3 .   ? 12.986  -2.132  13.870 1.00 22.80 ? 411 HOH B O   1 
HETATM 3938 O O   . HOH P 3 .   ? 8.458   3.489   11.916 1.00 20.85 ? 412 HOH B O   1 
HETATM 3939 O O   . HOH P 3 .   ? 6.565   2.642   20.373 1.00 17.24 ? 413 HOH B O   1 
HETATM 3940 O O   . HOH P 3 .   ? 14.356  -6.685  16.208 1.00 33.33 ? 414 HOH B O   1 
HETATM 3941 O O   . HOH P 3 .   ? 41.156  4.628   7.991  1.00 32.67 ? 415 HOH B O   1 
HETATM 3942 O O   . HOH P 3 .   ? 20.951  23.635  20.802 1.00 16.45 ? 416 HOH B O   1 
HETATM 3943 O O   . HOH P 3 .   ? 24.409  14.925  3.766  1.00 30.75 ? 417 HOH B O   1 
HETATM 3944 O O   . HOH P 3 .   ? 27.608  -1.587  21.779 1.00 27.99 ? 418 HOH B O   1 
HETATM 3945 O O   . HOH P 3 .   ? 22.772  7.421   7.826  1.00 23.59 ? 419 HOH B O   1 
HETATM 3946 O O   . HOH P 3 .   ? 16.250  -6.715  17.825 1.00 30.08 ? 420 HOH B O   1 
HETATM 3947 O O   . HOH P 3 .   ? 14.321  23.732  23.486 1.00 27.68 ? 421 HOH B O   1 
HETATM 3948 O O   . HOH P 3 .   ? 32.014  -11.723 3.537  1.00 35.67 ? 422 HOH B O   1 
HETATM 3949 O O   . HOH P 3 .   ? 8.563   -3.571  27.287 1.00 39.87 ? 423 HOH B O   1 
HETATM 3950 O O   . HOH P 3 .   ? 23.543  -1.682  21.743 1.00 27.99 ? 424 HOH B O   1 
HETATM 3951 O O   . HOH P 3 .   ? 16.469  21.853  9.932  1.00 27.16 ? 425 HOH B O   1 
HETATM 3952 O O   . HOH P 3 .   ? 19.153  -6.331  19.635 1.00 29.68 ? 426 HOH B O   1 
HETATM 3953 O O   . HOH P 3 .   ? 13.556  23.924  4.158  1.00 25.07 ? 427 HOH B O   1 
HETATM 3954 O O   . HOH P 3 .   ? 32.657  9.796   13.817 1.00 20.72 ? 428 HOH B O   1 
HETATM 3955 O O   . HOH P 3 .   ? -5.612  17.903  25.521 1.00 29.68 ? 429 HOH B O   1 
HETATM 3956 O O   . HOH P 3 .   ? 1.473   5.240   12.913 1.00 35.79 ? 430 HOH B O   1 
HETATM 3957 O O   . HOH P 3 .   ? 17.045  0.732   26.821 1.00 19.74 ? 431 HOH B O   1 
HETATM 3958 O O   . HOH P 3 .   ? 18.004  25.009  17.832 1.00 33.97 ? 432 HOH B O   1 
HETATM 3959 O O   . HOH P 3 .   ? 25.476  29.133  14.271 1.00 21.14 ? 433 HOH B O   1 
HETATM 3960 O O   . HOH P 3 .   ? 20.463  -4.598  21.670 1.00 36.81 ? 434 HOH B O   1 
HETATM 3961 O O   . HOH P 3 .   ? 22.458  27.185  18.390 1.00 30.89 ? 435 HOH B O   1 
HETATM 3962 O O   . HOH P 3 .   ? 18.926  -0.513  28.136 1.00 20.14 ? 436 HOH B O   1 
HETATM 3963 O O   . HOH P 3 .   ? 8.739   4.236   8.117  1.00 31.60 ? 437 HOH B O   1 
HETATM 3964 O O   . HOH P 3 .   ? 13.731  20.977  10.139 1.00 22.11 ? 438 HOH B O   1 
HETATM 3965 O O   . HOH P 3 .   ? 12.734  -3.336  16.422 1.00 18.32 ? 439 HOH B O   1 
HETATM 3966 O O   . HOH P 3 .   ? 16.186  23.117  21.506 1.00 15.80 ? 440 HOH B O   1 
HETATM 3967 O O   . HOH P 3 .   ? 17.882  -3.886  5.898  1.00 40.75 ? 441 HOH B O   1 
HETATM 3968 O O   . HOH P 3 .   ? 31.621  11.162  6.038  1.00 29.82 ? 442 HOH B O   1 
HETATM 3969 O O   . HOH P 3 .   ? 26.271  20.071  -0.021 1.00 39.56 ? 443 HOH B O   1 
HETATM 3970 O O   . HOH P 3 .   ? 2.893   4.588   30.576 1.00 17.19 ? 444 HOH B O   1 
HETATM 3971 O O   . HOH P 3 .   ? 33.526  -10.843 5.566  1.00 26.73 ? 445 HOH B O   1 
HETATM 3972 O O   . HOH P 3 .   ? 30.756  8.486   9.348  1.00 33.31 ? 446 HOH B O   1 
HETATM 3973 O O   . HOH P 3 .   ? 18.845  23.377  24.910 1.00 14.10 ? 447 HOH B O   1 
HETATM 3974 O O   . HOH P 3 .   ? 30.451  -10.522 14.049 1.00 26.30 ? 448 HOH B O   1 
HETATM 3975 O O   . HOH P 3 .   ? 29.175  -12.132 3.253  1.00 31.14 ? 449 HOH B O   1 
HETATM 3976 O O   . HOH P 3 .   ? 1.343   10.011  17.880 1.00 18.68 ? 450 HOH B O   1 
HETATM 3977 O O   . HOH P 3 .   ? 39.156  -0.612  15.834 1.00 37.83 ? 451 HOH B O   1 
HETATM 3978 O O   . HOH P 3 .   ? 9.871   -8.700  22.695 1.00 25.77 ? 452 HOH B O   1 
HETATM 3979 O O   . HOH P 3 .   ? 29.919  23.311  24.044 1.00 33.10 ? 453 HOH B O   1 
HETATM 3980 O O   . HOH P 3 .   ? 28.898  -4.154  24.201 1.00 16.92 ? 454 HOH B O   1 
HETATM 3981 O O   . HOH P 3 .   ? 33.807  9.448   9.493  1.00 32.47 ? 455 HOH B O   1 
HETATM 3982 O O   . HOH P 3 .   ? 40.125  2.180   19.181 1.00 38.53 ? 456 HOH B O   1 
HETATM 3983 O O   . HOH P 3 .   ? 6.743   3.229   10.053 1.00 37.86 ? 457 HOH B O   1 
HETATM 3984 O O   . HOH P 3 .   ? 18.851  18.486  4.543  1.00 28.08 ? 458 HOH B O   1 
HETATM 3985 O O   . HOH P 3 .   ? 16.328  24.537  25.428 1.00 26.19 ? 459 HOH B O   1 
HETATM 3986 O O   . HOH P 3 .   ? 0.616   7.363   17.334 1.00 36.19 ? 460 HOH B O   1 
HETATM 3987 O O   . HOH P 3 .   ? 15.769  23.841  18.672 1.00 20.35 ? 461 HOH B O   1 
HETATM 3988 O O   . HOH P 3 .   ? 17.541  -6.350  10.588 1.00 34.56 ? 462 HOH B O   1 
HETATM 3989 O O   . HOH P 3 .   ? 20.432  28.907  4.573  1.00 40.41 ? 463 HOH B O   1 
HETATM 3990 O O   . HOH P 3 .   ? 8.680   -1.320  15.622 1.00 32.33 ? 464 HOH B O   1 
HETATM 3991 O O   . HOH P 3 .   ? 35.945  1.474   24.369 1.00 25.96 ? 465 HOH B O   1 
HETATM 3992 O O   . HOH P 3 .   ? 11.034  0.225   13.327 1.00 29.06 ? 466 HOH B O   1 
HETATM 3993 O O   . HOH P 3 .   ? 17.520  22.319  5.097  1.00 23.81 ? 467 HOH B O   1 
HETATM 3994 O O   . HOH P 3 .   ? 11.194  14.050  2.273  1.00 31.85 ? 468 HOH B O   1 
HETATM 3995 O O   . HOH P 3 .   ? -0.236  11.111  15.630 1.00 30.76 ? 469 HOH B O   1 
HETATM 3996 O O   . HOH P 3 .   ? 7.065   -0.970  18.880 1.00 36.54 ? 470 HOH B O   1 
HETATM 3997 O O   . HOH Q 3 .   ? 32.229  45.881  8.347  1.00 16.47 ? 301 HOH C O   1 
HETATM 3998 O O   . HOH Q 3 .   ? 58.314  42.273  18.723 1.00 17.69 ? 302 HOH C O   1 
HETATM 3999 O O   . HOH Q 3 .   ? 39.437  13.086  15.408 1.00 29.52 ? 303 HOH C O   1 
HETATM 4000 O O   . HOH Q 3 .   ? 46.468  37.253  -1.493 1.00 19.34 ? 304 HOH C O   1 
HETATM 4001 O O   . HOH Q 3 .   ? 49.362  31.962  16.447 1.00 27.58 ? 305 HOH C O   1 
HETATM 4002 O O   . HOH Q 3 .   ? 44.587  42.393  -3.590 1.00 18.85 ? 306 HOH C O   1 
HETATM 4003 O O   . HOH Q 3 .   ? 37.453  29.999  4.493  1.00 9.18  ? 307 HOH C O   1 
HETATM 4004 O O   . HOH Q 3 .   ? 18.904  30.982  15.839 1.00 36.23 ? 308 HOH C O   1 
HETATM 4005 O O   . HOH Q 3 .   ? 19.760  28.762  7.631  1.00 39.28 ? 309 HOH C O   1 
HETATM 4006 O O   . HOH Q 3 .   ? 19.329  38.633  22.407 1.00 18.29 ? 310 HOH C O   1 
HETATM 4007 O O   . HOH Q 3 .   ? 18.112  36.397  0.624  1.00 26.27 ? 311 HOH C O   1 
HETATM 4008 O O   . HOH Q 3 .   ? 50.196  27.682  24.627 1.00 14.71 ? 312 HOH C O   1 
HETATM 4009 O O   . HOH Q 3 .   ? 41.377  16.195  22.379 1.00 23.30 ? 313 HOH C O   1 
HETATM 4010 O O   . HOH Q 3 .   ? 42.241  35.816  -0.649 1.00 10.18 ? 314 HOH C O   1 
HETATM 4011 O O   . HOH Q 3 .   ? 51.033  33.214  18.256 1.00 14.12 ? 315 HOH C O   1 
HETATM 4012 O O   . HOH Q 3 .   ? 28.425  41.216  4.964  1.00 21.81 ? 316 HOH C O   1 
HETATM 4013 O O   . HOH Q 3 .   ? 32.252  24.134  21.872 1.00 18.95 ? 317 HOH C O   1 
HETATM 4014 O O   . HOH Q 3 .   ? 22.010  47.638  28.384 1.00 22.67 ? 318 HOH C O   1 
HETATM 4015 O O   . HOH Q 3 .   ? 47.203  40.329  -3.494 1.00 15.72 ? 319 HOH C O   1 
HETATM 4016 O O   . HOH Q 3 .   ? 42.393  27.449  4.895  1.00 32.81 ? 320 HOH C O   1 
HETATM 4017 O O   . HOH Q 3 .   ? 44.646  43.352  0.614  1.00 24.59 ? 321 HOH C O   1 
HETATM 4018 O O   . HOH Q 3 .   ? 26.628  47.275  6.420  1.00 25.34 ? 322 HOH C O   1 
HETATM 4019 O O   . HOH Q 3 .   ? 52.460  36.880  22.950 1.00 20.76 ? 323 HOH C O   1 
HETATM 4020 O O   . HOH Q 3 .   ? 27.744  54.027  16.549 1.00 15.29 ? 324 HOH C O   1 
HETATM 4021 O O   . HOH Q 3 .   ? 21.764  42.378  -1.730 1.00 26.88 ? 325 HOH C O   1 
HETATM 4022 O O   . HOH Q 3 .   ? 40.600  54.501  20.966 1.00 21.49 ? 326 HOH C O   1 
HETATM 4023 O O   . HOH Q 3 .   ? 43.436  16.578  17.734 1.00 36.61 ? 327 HOH C O   1 
HETATM 4024 O O   . HOH Q 3 .   ? 42.044  25.242  16.818 1.00 14.74 ? 328 HOH C O   1 
HETATM 4025 O O   . HOH Q 3 .   ? 27.197  55.302  4.898  1.00 28.88 ? 329 HOH C O   1 
HETATM 4026 O O   . HOH Q 3 .   ? 36.046  33.519  -0.987 1.00 35.71 ? 330 HOH C O   1 
HETATM 4027 O O   . HOH Q 3 .   ? 15.084  35.945  11.562 1.00 19.16 ? 331 HOH C O   1 
HETATM 4028 O O   . HOH Q 3 .   ? 34.229  25.127  10.361 1.00 8.79  ? 332 HOH C O   1 
HETATM 4029 O O   . HOH Q 3 .   ? 27.001  49.643  14.126 1.00 14.67 ? 333 HOH C O   1 
HETATM 4030 O O   . HOH Q 3 .   ? 33.667  18.792  13.715 1.00 9.76  ? 334 HOH C O   1 
HETATM 4031 O O   . HOH Q 3 .   ? 21.500  34.992  2.286  1.00 30.59 ? 335 HOH C O   1 
HETATM 4032 O O   . HOH Q 3 .   ? 32.706  27.013  2.833  1.00 28.47 ? 336 HOH C O   1 
HETATM 4033 O O   . HOH Q 3 .   ? 27.268  50.237  11.394 1.00 21.31 ? 337 HOH C O   1 
HETATM 4034 O O   . HOH Q 3 .   ? 19.510  44.591  23.920 1.00 15.84 ? 338 HOH C O   1 
HETATM 4035 O O   . HOH Q 3 .   ? 21.870  46.305  15.764 1.00 8.85  ? 339 HOH C O   1 
HETATM 4036 O O   . HOH Q 3 .   ? 35.149  35.643  8.361  1.00 7.84  ? 340 HOH C O   1 
HETATM 4037 O O   . HOH Q 3 .   ? 36.663  29.299  24.267 1.00 9.95  ? 341 HOH C O   1 
HETATM 4038 O O   . HOH Q 3 .   ? 33.843  59.514  13.519 1.00 22.22 ? 342 HOH C O   1 
HETATM 4039 O O   . HOH Q 3 .   ? 39.067  35.822  -3.124 1.00 16.12 ? 343 HOH C O   1 
HETATM 4040 O O   . HOH Q 3 .   ? 46.245  47.321  6.243  1.00 22.98 ? 344 HOH C O   1 
HETATM 4041 O O   . HOH Q 3 .   ? 24.640  32.432  21.426 1.00 10.73 ? 345 HOH C O   1 
HETATM 4042 O O   . HOH Q 3 .   ? 51.351  34.425  23.498 1.00 19.60 ? 346 HOH C O   1 
HETATM 4043 O O   . HOH Q 3 .   ? 37.023  41.800  4.624  1.00 10.57 ? 347 HOH C O   1 
HETATM 4044 O O   . HOH Q 3 .   ? 39.481  11.007  24.936 1.00 22.46 ? 348 HOH C O   1 
HETATM 4045 O O   . HOH Q 3 .   ? 31.903  42.150  7.389  1.00 11.46 ? 349 HOH C O   1 
HETATM 4046 O O   . HOH Q 3 .   ? 51.674  30.358  23.145 1.00 25.47 ? 350 HOH C O   1 
HETATM 4047 O O   . HOH Q 3 .   ? 33.808  36.449  0.045  1.00 32.51 ? 351 HOH C O   1 
HETATM 4048 O O   . HOH Q 3 .   ? 45.280  21.427  24.977 1.00 24.03 ? 352 HOH C O   1 
HETATM 4049 O O   . HOH Q 3 .   ? 33.348  60.231  8.746  1.00 29.27 ? 353 HOH C O   1 
HETATM 4050 O O   . HOH Q 3 .   ? 46.757  40.306  3.267  1.00 13.79 ? 354 HOH C O   1 
HETATM 4051 O O   . HOH Q 3 .   ? 24.183  30.378  11.565 1.00 24.84 ? 355 HOH C O   1 
HETATM 4052 O O   . HOH Q 3 .   ? 29.819  30.214  25.601 1.00 9.28  ? 356 HOH C O   1 
HETATM 4053 O O   . HOH Q 3 .   ? 47.122  35.451  12.635 1.00 25.20 ? 357 HOH C O   1 
HETATM 4054 O O   . HOH Q 3 .   ? 22.582  41.498  1.596  1.00 16.76 ? 358 HOH C O   1 
HETATM 4055 O O   . HOH Q 3 .   ? 24.500  32.650  5.312  1.00 11.98 ? 359 HOH C O   1 
HETATM 4056 O O   . HOH Q 3 .   ? 30.641  31.888  3.185  1.00 14.31 ? 360 HOH C O   1 
HETATM 4057 O O   . HOH Q 3 .   ? 39.887  54.555  3.079  1.00 34.78 ? 361 HOH C O   1 
HETATM 4058 O O   . HOH Q 3 .   ? 44.128  56.182  8.089  1.00 28.80 ? 362 HOH C O   1 
HETATM 4059 O O   . HOH Q 3 .   ? 37.855  58.473  1.140  1.00 30.13 ? 363 HOH C O   1 
HETATM 4060 O O   . HOH Q 3 .   ? 44.060  21.298  17.581 1.00 19.93 ? 364 HOH C O   1 
HETATM 4061 O O   . HOH Q 3 .   ? 49.154  28.820  16.526 1.00 23.65 ? 365 HOH C O   1 
HETATM 4062 O O   . HOH Q 3 .   ? 35.504  13.189  6.317  1.00 37.36 ? 366 HOH C O   1 
HETATM 4063 O O   . HOH Q 3 .   ? 26.867  28.017  16.462 1.00 10.03 ? 367 HOH C O   1 
HETATM 4064 O O   . HOH Q 3 .   ? 22.353  41.271  27.734 1.00 16.22 ? 368 HOH C O   1 
HETATM 4065 O O   . HOH Q 3 .   ? 54.583  44.245  17.419 1.00 25.91 ? 369 HOH C O   1 
HETATM 4066 O O   . HOH Q 3 .   ? 40.284  44.200  4.224  1.00 21.83 ? 370 HOH C O   1 
HETATM 4067 O O   . HOH Q 3 .   ? 40.804  25.743  6.819  1.00 21.74 ? 371 HOH C O   1 
HETATM 4068 O O   . HOH Q 3 .   ? 38.879  29.377  22.580 1.00 9.65  ? 372 HOH C O   1 
HETATM 4069 O O   . HOH Q 3 .   ? 50.798  41.143  11.992 1.00 22.52 ? 373 HOH C O   1 
HETATM 4070 O O   . HOH Q 3 .   ? 49.702  40.952  7.392  1.00 19.82 ? 374 HOH C O   1 
HETATM 4071 O O   . HOH Q 3 .   ? 27.890  25.715  7.765  1.00 10.99 ? 375 HOH C O   1 
HETATM 4072 O O   . HOH Q 3 .   ? 37.622  32.158  2.244  1.00 21.19 ? 376 HOH C O   1 
HETATM 4073 O O   . HOH Q 3 .   ? 21.807  29.184  14.219 1.00 22.08 ? 377 HOH C O   1 
HETATM 4074 O O   . HOH Q 3 .   ? 42.309  51.236  23.033 1.00 24.86 ? 378 HOH C O   1 
HETATM 4075 O O   . HOH Q 3 .   ? 44.125  54.925  16.059 1.00 25.03 ? 379 HOH C O   1 
HETATM 4076 O O   . HOH Q 3 .   ? 38.799  47.380  3.005  1.00 17.73 ? 380 HOH C O   1 
HETATM 4077 O O   . HOH Q 3 .   ? 39.236  25.570  16.308 1.00 10.25 ? 381 HOH C O   1 
HETATM 4078 O O   . HOH Q 3 .   ? 35.376  27.858  1.579  1.00 23.70 ? 382 HOH C O   1 
HETATM 4079 O O   . HOH Q 3 .   ? 47.082  31.571  17.393 1.00 22.59 ? 383 HOH C O   1 
HETATM 4080 O O   . HOH Q 3 .   ? 37.169  45.491  5.944  1.00 16.24 ? 384 HOH C O   1 
HETATM 4081 O O   . HOH Q 3 .   ? 34.659  59.263  0.482  1.00 27.63 ? 385 HOH C O   1 
HETATM 4082 O O   . HOH Q 3 .   ? 44.310  34.207  5.682  1.00 11.37 ? 386 HOH C O   1 
HETATM 4083 O O   . HOH Q 3 .   ? 26.647  39.822  2.344  1.00 28.73 ? 387 HOH C O   1 
HETATM 4084 O O   . HOH Q 3 .   ? 40.143  30.592  3.086  1.00 26.95 ? 388 HOH C O   1 
HETATM 4085 O O   . HOH Q 3 .   ? 28.654  27.911  22.877 1.00 14.75 ? 389 HOH C O   1 
HETATM 4086 O O   . HOH Q 3 .   ? 28.552  59.116  3.873  1.00 23.17 ? 390 HOH C O   1 
HETATM 4087 O O   . HOH Q 3 .   ? 37.691  43.159  2.199  1.00 18.96 ? 391 HOH C O   1 
HETATM 4088 O O   . HOH Q 3 .   ? 47.319  45.360  7.783  1.00 13.50 ? 392 HOH C O   1 
HETATM 4089 O O   . HOH Q 3 .   ? 31.175  42.709  3.934  1.00 25.15 ? 393 HOH C O   1 
HETATM 4090 O O   . HOH Q 3 .   ? 22.426  38.979  25.393 1.00 20.47 ? 394 HOH C O   1 
HETATM 4091 O O   . HOH Q 3 .   ? 44.425  34.558  8.444  1.00 12.40 ? 395 HOH C O   1 
HETATM 4092 O O   . HOH Q 3 .   ? 32.494  33.423  1.854  1.00 26.65 ? 396 HOH C O   1 
HETATM 4093 O O   . HOH Q 3 .   ? 33.813  23.935  5.808  1.00 13.50 ? 397 HOH C O   1 
HETATM 4094 O O   . HOH Q 3 .   ? 15.011  43.262  7.850  1.00 9.80  ? 398 HOH C O   1 
HETATM 4095 O O   . HOH Q 3 .   ? 51.198  32.471  21.590 1.00 15.53 ? 399 HOH C O   1 
HETATM 4096 O O   . HOH Q 3 .   ? 47.985  48.727  12.909 1.00 27.14 ? 400 HOH C O   1 
HETATM 4097 O O   . HOH Q 3 .   ? 30.126  48.978  9.098  1.00 20.15 ? 401 HOH C O   1 
HETATM 4098 O O   . HOH Q 3 .   ? 14.004  40.011  1.964  1.00 31.27 ? 402 HOH C O   1 
HETATM 4099 O O   . HOH Q 3 .   ? 22.930  49.947  26.548 1.00 15.97 ? 403 HOH C O   1 
HETATM 4100 O O   . HOH Q 3 .   ? 35.430  33.803  2.084  1.00 25.46 ? 404 HOH C O   1 
HETATM 4101 O O   . HOH Q 3 .   ? 43.151  23.776  18.966 1.00 15.22 ? 405 HOH C O   1 
HETATM 4102 O O   . HOH Q 3 .   ? 45.517  48.534  15.932 1.00 17.02 ? 406 HOH C O   1 
HETATM 4103 O O   . HOH Q 3 .   ? 27.264  26.500  2.406  1.00 27.83 ? 407 HOH C O   1 
HETATM 4104 O O   . HOH Q 3 .   ? 25.083  31.979  13.683 1.00 18.04 ? 408 HOH C O   1 
HETATM 4105 O O   . HOH Q 3 .   ? 18.293  45.363  21.566 1.00 16.60 ? 409 HOH C O   1 
HETATM 4106 O O   . HOH Q 3 .   ? 46.497  26.098  16.021 1.00 36.97 ? 410 HOH C O   1 
HETATM 4107 O O   . HOH Q 3 .   ? 26.500  47.922  10.415 1.00 18.92 ? 411 HOH C O   1 
HETATM 4108 O O   . HOH Q 3 .   ? 37.333  57.220  18.578 1.00 17.40 ? 412 HOH C O   1 
HETATM 4109 O O   . HOH Q 3 .   ? 35.510  8.805   24.051 1.00 19.42 ? 413 HOH C O   1 
HETATM 4110 O O   . HOH Q 3 .   ? 41.062  51.910  17.826 1.00 21.82 ? 414 HOH C O   1 
HETATM 4111 O O   . HOH Q 3 .   ? 47.470  25.636  26.995 1.00 22.02 ? 415 HOH C O   1 
HETATM 4112 O O   . HOH Q 3 .   ? 22.565  34.752  4.821  1.00 10.77 ? 416 HOH C O   1 
HETATM 4113 O O   . HOH Q 3 .   ? 43.143  17.113  25.908 1.00 24.85 ? 417 HOH C O   1 
HETATM 4114 O O   . HOH Q 3 .   ? 17.736  44.444  5.634  1.00 14.01 ? 418 HOH C O   1 
HETATM 4115 O O   . HOH Q 3 .   ? 45.073  31.933  8.865  1.00 13.82 ? 419 HOH C O   1 
HETATM 4116 O O   . HOH Q 3 .   ? 20.778  48.298  2.316  1.00 39.29 ? 420 HOH C O   1 
HETATM 4117 O O   . HOH Q 3 .   ? 34.269  41.979  5.006  1.00 15.75 ? 421 HOH C O   1 
HETATM 4118 O O   . HOH Q 3 .   ? 28.519  37.787  5.593  1.00 20.83 ? 422 HOH C O   1 
HETATM 4119 O O   . HOH Q 3 .   ? 41.678  30.319  0.907  1.00 24.58 ? 423 HOH C O   1 
HETATM 4120 O O   . HOH Q 3 .   ? 47.806  38.435  10.021 1.00 14.19 ? 424 HOH C O   1 
HETATM 4121 O O   . HOH Q 3 .   ? 52.611  27.443  20.044 1.00 24.33 ? 425 HOH C O   1 
HETATM 4122 O O   . HOH Q 3 .   ? 42.522  48.083  24.504 1.00 19.91 ? 426 HOH C O   1 
HETATM 4123 O O   . HOH Q 3 .   ? 22.442  33.445  19.992 1.00 15.49 ? 427 HOH C O   1 
HETATM 4124 O O   . HOH Q 3 .   ? 41.497  59.152  14.027 1.00 20.62 ? 428 HOH C O   1 
HETATM 4125 O O   . HOH Q 3 .   ? 29.075  22.983  21.564 1.00 15.37 ? 429 HOH C O   1 
HETATM 4126 O O   . HOH Q 3 .   ? 16.608  48.494  5.251  1.00 39.93 ? 430 HOH C O   1 
HETATM 4127 O O   . HOH Q 3 .   ? 43.633  31.482  5.112  1.00 16.77 ? 431 HOH C O   1 
HETATM 4128 O O   . HOH Q 3 .   ? 47.056  27.120  10.720 1.00 33.72 ? 432 HOH C O   1 
HETATM 4129 O O   . HOH Q 3 .   ? 23.574  53.207  10.455 1.00 33.23 ? 433 HOH C O   1 
HETATM 4130 O O   . HOH Q 3 .   ? 45.662  29.085  12.109 1.00 28.37 ? 434 HOH C O   1 
HETATM 4131 O O   . HOH Q 3 .   ? 26.560  58.790  10.336 1.00 35.23 ? 435 HOH C O   1 
HETATM 4132 O O   . HOH Q 3 .   ? 43.481  48.055  17.556 1.00 23.69 ? 436 HOH C O   1 
HETATM 4133 O O   . HOH Q 3 .   ? 41.096  13.681  23.956 1.00 28.32 ? 437 HOH C O   1 
HETATM 4134 O O   . HOH Q 3 .   ? 29.012  51.397  9.558  1.00 22.34 ? 438 HOH C O   1 
HETATM 4135 O O   . HOH Q 3 .   ? 26.041  28.162  22.571 1.00 24.47 ? 439 HOH C O   1 
HETATM 4136 O O   . HOH Q 3 .   ? 50.767  44.513  13.396 1.00 22.84 ? 440 HOH C O   1 
HETATM 4137 O O   . HOH Q 3 .   ? 24.569  37.007  0.732  1.00 38.49 ? 441 HOH C O   1 
HETATM 4138 O O   . HOH Q 3 .   ? 50.586  37.681  25.355 1.00 25.31 ? 442 HOH C O   1 
HETATM 4139 O O   . HOH Q 3 .   ? 53.391  43.920  21.353 1.00 43.02 ? 443 HOH C O   1 
HETATM 4140 O O   . HOH Q 3 .   ? 32.438  40.559  0.194  1.00 36.09 ? 444 HOH C O   1 
HETATM 4141 O O   . HOH Q 3 .   ? 33.157  44.896  5.217  1.00 31.67 ? 445 HOH C O   1 
HETATM 4142 O O   . HOH Q 3 .   ? 20.822  41.548  25.183 1.00 31.36 ? 446 HOH C O   1 
HETATM 4143 O O   . HOH Q 3 .   ? 49.139  40.403  14.067 1.00 20.32 ? 447 HOH C O   1 
HETATM 4144 O O   . HOH Q 3 .   ? 42.183  43.221  2.011  1.00 36.12 ? 448 HOH C O   1 
HETATM 4145 O O   . HOH Q 3 .   ? 28.581  33.506  2.977  1.00 23.96 ? 449 HOH C O   1 
HETATM 4146 O O   . HOH Q 3 .   ? 35.769  61.244  -2.578 1.00 29.77 ? 450 HOH C O   1 
HETATM 4147 O O   . HOH Q 3 .   ? 21.599  56.629  15.076 1.00 31.75 ? 451 HOH C O   1 
HETATM 4148 O O   . HOH Q 3 .   ? 48.889  46.370  14.975 1.00 32.83 ? 452 HOH C O   1 
HETATM 4149 O O   . HOH Q 3 .   ? 18.946  47.424  4.836  1.00 25.33 ? 453 HOH C O   1 
HETATM 4150 O O   . HOH Q 3 .   ? 14.494  53.048  9.698  1.00 35.88 ? 454 HOH C O   1 
HETATM 4151 O O   . HOH Q 3 .   ? 18.487  33.014  18.186 1.00 32.07 ? 455 HOH C O   1 
HETATM 4152 O O   . HOH Q 3 .   ? 50.350  38.115  9.012  1.00 22.72 ? 456 HOH C O   1 
HETATM 4153 O O   . HOH Q 3 .   ? 30.093  48.270  6.369  1.00 32.51 ? 457 HOH C O   1 
HETATM 4154 O O   . HOH Q 3 .   ? 44.957  41.793  23.075 1.00 14.33 ? 458 HOH C O   1 
HETATM 4155 O O   . HOH Q 3 .   ? 37.806  29.081  1.438  1.00 28.05 ? 459 HOH C O   1 
HETATM 4156 O O   . HOH Q 3 .   ? 26.995  27.933  9.295  1.00 22.03 ? 460 HOH C O   1 
HETATM 4157 O O   . HOH Q 3 .   ? 29.170  54.318  18.892 1.00 16.79 ? 461 HOH C O   1 
HETATM 4158 O O   . HOH Q 3 .   ? 14.422  34.353  14.371 1.00 24.84 ? 462 HOH C O   1 
HETATM 4159 O O   . HOH Q 3 .   ? 48.425  41.597  5.172  1.00 21.57 ? 463 HOH C O   1 
HETATM 4160 O O   . HOH Q 3 .   ? 40.919  46.140  1.392  1.00 26.82 ? 464 HOH C O   1 
HETATM 4161 O O   . HOH Q 3 .   ? 48.600  46.778  9.532  1.00 24.59 ? 465 HOH C O   1 
HETATM 4162 O O   . HOH Q 3 .   ? 25.113  29.779  20.664 1.00 13.35 ? 466 HOH C O   1 
HETATM 4163 O O   . HOH Q 3 .   ? 47.535  47.276  17.276 1.00 26.37 ? 467 HOH C O   1 
HETATM 4164 O O   . HOH Q 3 .   ? 26.835  52.122  8.232  1.00 37.62 ? 468 HOH C O   1 
HETATM 4165 O O   . HOH Q 3 .   ? 26.710  28.430  24.793 1.00 28.46 ? 469 HOH C O   1 
HETATM 4166 O O   . HOH Q 3 .   ? 24.142  32.145  24.123 1.00 14.66 ? 470 HOH C O   1 
HETATM 4167 O O   . HOH Q 3 .   ? 48.882  27.903  27.061 1.00 18.04 ? 471 HOH C O   1 
HETATM 4168 O O   . HOH Q 3 .   ? 15.630  43.175  2.730  1.00 36.17 ? 472 HOH C O   1 
HETATM 4169 O O   . HOH Q 3 .   ? 39.528  57.265  3.298  1.00 28.73 ? 473 HOH C O   1 
HETATM 4170 O O   . HOH Q 3 .   ? 46.862  31.450  10.919 1.00 25.05 ? 474 HOH C O   1 
HETATM 4171 O O   . HOH Q 3 .   ? 43.577  23.081  15.379 1.00 24.48 ? 475 HOH C O   1 
HETATM 4172 O O   . HOH Q 3 .   ? 47.052  42.643  1.920  1.00 24.13 ? 476 HOH C O   1 
HETATM 4173 O O   . HOH Q 3 .   ? 39.251  57.195  20.549 1.00 21.59 ? 477 HOH C O   1 
HETATM 4174 O O   . HOH Q 3 .   ? 53.459  29.515  21.702 1.00 26.24 ? 478 HOH C O   1 
HETATM 4175 O O   . HOH Q 3 .   ? 50.742  27.550  15.044 1.00 33.26 ? 479 HOH C O   1 
HETATM 4176 O O   . HOH Q 3 .   ? 48.615  42.195  -2.802 1.00 37.37 ? 480 HOH C O   1 
HETATM 4177 O O   . HOH Q 3 .   ? 48.735  37.826  12.749 1.00 20.21 ? 481 HOH C O   1 
HETATM 4178 O O   . HOH Q 3 .   ? 45.492  18.776  24.309 1.00 42.86 ? 482 HOH C O   1 
HETATM 4179 O O   . HOH Q 3 .   ? 44.776  57.388  16.984 1.00 28.32 ? 483 HOH C O   1 
HETATM 4180 O O   . HOH Q 3 .   ? 48.810  44.013  5.945  1.00 29.34 ? 484 HOH C O   1 
HETATM 4181 O O   . HOH Q 3 .   ? 47.723  47.065  3.578  1.00 31.46 ? 485 HOH C O   1 
HETATM 4182 O O   . HOH Q 3 .   ? 54.926  37.517  23.094 1.00 19.71 ? 486 HOH C O   1 
HETATM 4183 O O   . HOH Q 3 .   ? 52.833  45.614  15.330 1.00 31.99 ? 487 HOH C O   1 
HETATM 4184 O O   . HOH Q 3 .   ? 52.699  33.653  25.889 1.00 18.10 ? 488 HOH C O   1 
HETATM 4185 O O   . HOH Q 3 .   ? 48.935  41.993  0.006  1.00 31.63 ? 489 HOH C O   1 
HETATM 4186 O O   . HOH Q 3 .   ? 46.590  35.778  9.597  1.00 15.15 ? 490 HOH C O   1 
HETATM 4187 O O   . HOH Q 3 .   ? 45.742  30.438  6.703  1.00 17.27 ? 491 HOH C O   1 
HETATM 4188 O O   . HOH Q 3 .   ? 24.277  29.541  24.848 1.00 27.58 ? 492 HOH C O   1 
HETATM 4189 O O   . HOH Q 3 .   ? 44.992  30.324  3.061  1.00 34.35 ? 493 HOH C O   1 
HETATM 4190 O O   . HOH Q 3 .   ? 35.822  22.154  5.331  1.00 25.54 ? 494 HOH C O   1 
HETATM 4191 O O   . HOH Q 3 .   ? 24.601  28.831  18.088 1.00 19.05 ? 495 HOH C O   1 
HETATM 4192 O O   . HOH Q 3 .   ? 39.626  60.609  0.000  0.50 38.00 ? 496 HOH C O   1 
HETATM 4193 O O   . HOH Q 3 .   ? 14.731  46.213  4.522  1.00 24.63 ? 497 HOH C O   1 
HETATM 4194 O O   . HOH Q 3 .   ? 34.578  60.751  11.271 1.00 26.07 ? 498 HOH C O   1 
HETATM 4195 O O   . HOH Q 3 .   ? 35.165  58.199  19.884 1.00 23.11 ? 499 HOH C O   1 
HETATM 4196 O O   . HOH Q 3 .   ? 35.476  61.152  15.639 1.00 30.89 ? 500 HOH C O   1 
HETATM 4197 O O   . HOH Q 3 .   ? 52.492  30.685  25.678 1.00 31.26 ? 501 HOH C O   1 
HETATM 4198 O O   . HOH Q 3 .   ? 23.234  30.212  4.421  1.00 27.26 ? 502 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   ? 0.6275 0.4434 0.2955 0.0545  0.1304  0.1285  25  HIS A N   
2    C CA  . HIS A 8   ? 0.5563 0.3302 0.2835 0.0071  0.1181  0.1309  25  HIS A CA  
3    C C   . HIS A 8   ? 0.4655 0.3544 0.2672 -0.0045 0.0866  0.0968  25  HIS A C   
4    O O   . HIS A 8   ? 0.5571 0.4324 0.2709 0.0576  0.0820  0.0984  25  HIS A O   
5    C CB  . HIS A 8   ? 0.5556 0.3190 0.2873 0.0354  0.1090  0.1297  25  HIS A CB  
6    N N   . VAL A 9   ? 0.2734 0.2952 0.2508 -0.0523 0.0296  0.0545  26  VAL A N   
7    C CA  . VAL A 9   ? 0.1782 0.2044 0.2283 -0.0299 -0.0119 0.0448  26  VAL A CA  
8    C C   . VAL A 9   ? 0.1638 0.1346 0.2082 -0.0017 -0.0226 0.0310  26  VAL A C   
9    O O   . VAL A 9   ? 0.2347 0.1380 0.2210 0.0584  -0.0379 0.0386  26  VAL A O   
10   C CB  . VAL A 9   ? 0.1776 0.2164 0.2277 -0.0375 -0.0367 -0.0246 26  VAL A CB  
11   C CG1 . VAL A 9   ? 0.2279 0.2505 0.2323 -0.0132 -0.0424 -0.0450 26  VAL A CG1 
12   C CG2 . VAL A 9   ? 0.2761 0.2628 0.2317 0.0038  -0.0322 -0.0120 26  VAL A CG2 
13   N N   . GLU A 10  ? 0.1234 0.1375 0.1731 -0.0093 -0.0117 0.0350  27  GLU A N   
14   C CA  . GLU A 10  ? 0.1394 0.1265 0.1519 -0.0155 -0.0053 0.0244  27  GLU A CA  
15   C C   . GLU A 10  ? 0.1143 0.1163 0.1262 0.0104  -0.0193 0.0145  27  GLU A C   
16   O O   . GLU A 10  ? 0.0868 0.1284 0.1246 -0.0127 -0.0109 0.0112  27  GLU A O   
17   C CB  . GLU A 10  ? 0.1797 0.2301 0.1585 0.0037  -0.0119 0.0153  27  GLU A CB  
18   C CG  . GLU A 10  ? 0.1965 0.1640 0.1613 0.0405  -0.0427 -0.0087 27  GLU A CG  
19   C CD  . GLU A 10  ? 0.2263 0.2341 0.1613 0.0064  -0.0574 0.0005  27  GLU A CD  
20   O OE1 . GLU A 10  ? 0.4485 0.2315 0.1843 0.1061  -0.0553 0.0266  27  GLU A OE1 
21   O OE2 . GLU A 10  ? 0.1690 0.1845 0.1533 0.0162  -0.0444 -0.0169 27  GLU A OE2 
22   N N   . GLN A 11  ? 0.1140 0.1113 0.1133 -0.0025 -0.0241 0.0267  28  GLN A N   
23   C CA  . GLN A 11  ? 0.0891 0.0773 0.1109 0.0036  -0.0180 0.0019  28  GLN A CA  
24   C C   . GLN A 11  ? 0.1327 0.1184 0.1071 0.0311  0.0082  0.0018  28  GLN A C   
25   O O   . GLN A 11  ? 0.1503 0.1185 0.1179 0.0378  -0.0139 -0.0004 28  GLN A O   
26   C CB  . GLN A 11  ? 0.1530 0.1089 0.1171 0.0514  -0.0201 -0.0140 28  GLN A CB  
27   C CG  . GLN A 11  ? 0.1874 0.1327 0.1332 0.0137  -0.0220 -0.0156 28  GLN A CG  
28   C CD  . GLN A 11  ? 0.1991 0.1842 0.1501 0.0219  -0.0110 -0.0288 28  GLN A CD  
29   O OE1 . GLN A 11  ? 0.2166 0.2757 0.1689 0.0283  -0.0074 -0.0320 28  GLN A OE1 
30   N NE2 . GLN A 11  ? 0.2509 0.1879 0.1432 0.0604  -0.0215 -0.0517 28  GLN A NE2 
31   N N   . THR A 12  ? 0.1385 0.0663 0.0927 0.0065  -0.0101 -0.0035 29  THR A N   
32   C CA  . THR A 12  ? 0.0846 0.0931 0.0912 0.0130  -0.0049 -0.0135 29  THR A CA  
33   C C   . THR A 12  ? 0.0334 0.1170 0.0932 0.0080  -0.0099 0.0025  29  THR A C   
34   O O   . THR A 12  ? 0.0668 0.1219 0.0996 0.0111  -0.0168 0.0019  29  THR A O   
35   C CB  . THR A 12  ? 0.1335 0.1153 0.0900 0.0151  0.0053  -0.0101 29  THR A CB  
36   O OG1 . THR A 12  ? 0.1248 0.1260 0.0954 0.0166  0.0009  -0.0109 29  THR A OG1 
37   C CG2 . THR A 12  ? 0.0964 0.0986 0.1034 -0.0264 0.0244  0.0057  29  THR A CG2 
38   N N   . TYR A 13  ? 0.0849 0.1160 0.0948 -0.0024 -0.0275 0.0204  30  TYR A N   
39   C CA  . TYR A 13  ? 0.1006 0.0875 0.1028 0.0159  -0.0134 0.0186  30  TYR A CA  
40   C C   . TYR A 13  ? 0.0849 0.1232 0.1009 -0.0123 -0.0019 0.0154  30  TYR A C   
41   O O   . TYR A 13  ? 0.1106 0.1306 0.0992 0.0009  -0.0094 0.0102  30  TYR A O   
42   C CB  . TYR A 13  ? 0.1104 0.1179 0.1039 0.0428  -0.0196 0.0209  30  TYR A CB  
43   C CG  . TYR A 13  ? 0.0861 0.0941 0.1072 0.0097  -0.0189 0.0067  30  TYR A CG  
44   C CD1 . TYR A 13  ? 0.0524 0.0689 0.1119 -0.0121 -0.0249 -0.0006 30  TYR A CD1 
45   C CD2 . TYR A 13  ? 0.0759 0.1125 0.1085 0.0096  -0.0136 0.0099  30  TYR A CD2 
46   C CE1 . TYR A 13  ? 0.0918 0.0631 0.1182 -0.0054 -0.0039 0.0049  30  TYR A CE1 
47   C CE2 . TYR A 13  ? 0.0801 0.0753 0.1126 0.0021  -0.0086 0.0250  30  TYR A CE2 
48   C CZ  . TYR A 13  ? 0.1055 0.0921 0.1174 0.0162  -0.0049 0.0094  30  TYR A CZ  
49   O OH  . TYR A 13  ? 0.1285 0.1143 0.1270 -0.0175 0.0054  0.0090  30  TYR A OH  
50   N N   . LEU A 14  ? 0.0806 0.0957 0.0974 0.0409  -0.0019 -0.0063 31  LEU A N   
51   C CA  . LEU A 14  ? 0.0459 0.0897 0.1031 0.0135  0.0027  0.0103  31  LEU A CA  
52   C C   . LEU A 14  ? 0.0863 0.0953 0.1014 0.0107  -0.0017 -0.0128 31  LEU A C   
53   O O   . LEU A 14  ? 0.1499 0.1062 0.1119 0.0279  0.0148  -0.0189 31  LEU A O   
54   C CB  . LEU A 14  ? 0.0741 0.1137 0.1143 0.0232  -0.0148 0.0216  31  LEU A CB  
55   C CG  . LEU A 14  ? 0.0562 0.1361 0.1296 -0.0218 0.0012  0.0045  31  LEU A CG  
56   C CD1 . LEU A 14  ? 0.1164 0.1550 0.1331 0.0114  -0.0157 0.0154  31  LEU A CD1 
57   C CD2 . LEU A 14  ? 0.1009 0.2407 0.1303 -0.0110 0.0120  -0.0259 31  LEU A CD2 
58   N N   . MET A 15  ? 0.0944 0.1078 0.0903 0.0408  -0.0065 0.0039  32  MET A N   
59   C CA  . MET A 15  ? 0.1126 0.0855 0.0855 0.0413  -0.0035 0.0135  32  MET A CA  
60   C C   . MET A 15  ? 0.1001 0.0936 0.0787 -0.0041 -0.0068 0.0024  32  MET A C   
61   O O   . MET A 15  ? 0.1413 0.1142 0.0805 0.0137  0.0009  0.0127  32  MET A O   
62   C CB  . MET A 15  ? 0.0747 0.1412 0.1018 0.0337  0.0074  0.0205  32  MET A CB  
63   C CG  . MET A 15  ? 0.1310 0.1436 0.1151 0.0511  -0.0042 0.0031  32  MET A CG  
64   S SD  . MET A 15  ? 0.0993 0.1567 0.1312 -0.0007 -0.0058 0.0170  32  MET A SD  
65   C CE  . MET A 15  ? 0.1176 0.2100 0.1389 -0.0026 -0.0255 -0.0074 32  MET A CE  
66   N N   . ILE A 16  ? 0.0622 0.0530 0.0749 0.0185  0.0008  0.0064  33  ILE A N   
67   C CA  . ILE A 16  ? 0.0310 0.0790 0.0806 -0.0007 0.0081  -0.0035 33  ILE A CA  
68   C C   . ILE A 16  ? 0.0841 0.0892 0.0860 -0.0042 0.0135  0.0163  33  ILE A C   
69   O O   . ILE A 16  ? 0.0571 0.0864 0.0935 -0.0174 0.0052  -0.0121 33  ILE A O   
70   C CB  . ILE A 16  ? 0.0758 0.1118 0.0834 0.0239  -0.0065 -0.0019 33  ILE A CB  
71   C CG1 . ILE A 16  ? 0.0963 0.1542 0.0972 0.0188  -0.0171 -0.0041 33  ILE A CG1 
72   C CG2 . ILE A 16  ? 0.0907 0.0757 0.0819 0.0221  -0.0178 -0.0025 33  ILE A CG2 
73   C CD1 . ILE A 16  ? 0.1202 0.1287 0.1023 0.0540  -0.0007 0.0228  33  ILE A CD1 
74   N N   . LYS A 17  ? 0.0868 0.0956 0.0912 0.0211  0.0036  0.0102  34  LYS A N   
75   C CA  . LYS A 17  ? 0.0541 0.0966 0.0923 -0.0157 -0.0097 -0.0109 34  LYS A CA  
76   C C   . LYS A 17  ? 0.0416 0.0881 0.0910 -0.0125 0.0025  -0.0027 34  LYS A C   
77   O O   . LYS A 17  ? 0.0652 0.0843 0.0958 -0.0038 -0.0074 -0.0077 34  LYS A O   
78   C CB  . LYS A 17  ? 0.0818 0.1104 0.0894 -0.0035 -0.0031 -0.0022 34  LYS A CB  
79   C CG  . LYS A 17  ? 0.0845 0.0822 0.0940 -0.0200 -0.0043 -0.0011 34  LYS A CG  
80   C CD  . LYS A 17  ? 0.0729 0.1454 0.0975 -0.0159 0.0102  -0.0013 34  LYS A CD  
81   C CE  . LYS A 17  ? 0.1197 0.1313 0.0967 0.0068  -0.0198 -0.0274 34  LYS A CE  
82   N NZ  . LYS A 17  ? 0.1239 0.2000 0.0906 0.0522  -0.0206 -0.0107 34  LYS A NZ  
83   N N   . PRO A 18  ? 0.0685 0.0663 0.0934 -0.0048 -0.0218 0.0020  35  PRO A N   
84   C CA  . PRO A 18  ? 0.0878 0.0901 0.0966 -0.0178 0.0175  0.0301  35  PRO A CA  
85   C C   . PRO A 18  ? 0.1082 0.0476 0.0905 -0.0028 0.0018  0.0133  35  PRO A C   
86   O O   . PRO A 18  ? 0.0995 0.1023 0.0772 -0.0047 -0.0143 0.0112  35  PRO A O   
87   C CB  . PRO A 18  ? 0.1003 0.0750 0.1030 0.0367  0.0294  0.0210  35  PRO A CB  
88   C CG  . PRO A 18  ? 0.1270 0.1107 0.1017 0.0135  0.0114  0.0005  35  PRO A CG  
89   C CD  . PRO A 18  ? 0.0799 0.0938 0.0969 -0.0059 -0.0044 0.0096  35  PRO A CD  
90   N N   . ASP A 19  ? 0.0914 0.0838 0.0976 0.0266  0.0224  -0.0023 36  ASP A N   
91   C CA  . ASP A 19  ? 0.1128 0.0729 0.0994 0.0059  0.0238  0.0027  36  ASP A CA  
92   C C   . ASP A 19  ? 0.1231 0.1095 0.0931 -0.0022 0.0097  -0.0047 36  ASP A C   
93   O O   . ASP A 19  ? 0.1376 0.1225 0.0871 0.0062  0.0103  0.0043  36  ASP A O   
94   C CB  . ASP A 19  ? 0.1261 0.0768 0.0985 0.0278  0.0235  0.0011  36  ASP A CB  
95   C CG  . ASP A 19  ? 0.1194 0.0987 0.1053 0.0054  0.0223  -0.0015 36  ASP A CG  
96   O OD1 . ASP A 19  ? 0.1473 0.1415 0.1095 0.0547  0.0126  0.0107  36  ASP A OD1 
97   O OD2 . ASP A 19  ? 0.1176 0.1314 0.0980 0.0128  -0.0122 0.0055  36  ASP A OD2 
98   N N   . GLY A 20  ? 0.0795 0.1058 0.0951 0.0320  -0.0101 -0.0111 37  GLY A N   
99   C CA  . GLY A 20  ? 0.0981 0.1038 0.0922 0.0210  0.0156  0.0210  37  GLY A CA  
100  C C   . GLY A 20  ? 0.0744 0.0987 0.0973 -0.0122 0.0055  0.0045  37  GLY A C   
101  O O   . GLY A 20  ? 0.0786 0.1257 0.0967 0.0001  0.0044  0.0105  37  GLY A O   
102  N N   . ILE A 21  ? 0.0490 0.0963 0.0983 0.0183  0.0075  -0.0075 38  ILE A N   
103  C CA  . ILE A 21  ? 0.0605 0.1126 0.0937 0.0044  0.0231  -0.0103 38  ILE A CA  
104  C C   . ILE A 21  ? 0.0496 0.1048 0.0915 -0.0327 0.0077  -0.0200 38  ILE A C   
105  O O   . ILE A 21  ? 0.0811 0.1203 0.0868 -0.0045 -0.0047 -0.0257 38  ILE A O   
106  C CB  . ILE A 21  ? 0.0594 0.0915 0.1020 -0.0072 0.0216  0.0015  38  ILE A CB  
107  C CG1 . ILE A 21  ? 0.0774 0.1473 0.1059 0.0072  0.0024  -0.0179 38  ILE A CG1 
108  C CG2 . ILE A 21  ? 0.0911 0.0869 0.1012 0.0229  0.0093  -0.0075 38  ILE A CG2 
109  C CD1 . ILE A 21  ? 0.1304 0.1570 0.1144 0.0086  -0.0176 -0.0170 38  ILE A CD1 
110  N N   . GLN A 22  ? 0.0780 0.0915 0.0979 0.0190  -0.0004 -0.0139 39  GLN A N   
111  C CA  . GLN A 22  ? 0.0938 0.0815 0.1048 0.0331  0.0042  -0.0015 39  GLN A CA  
112  C C   . GLN A 22  ? 0.1014 0.0689 0.1088 -0.0341 0.0182  0.0222  39  GLN A C   
113  O O   . GLN A 22  ? 0.1037 0.0931 0.1096 -0.0188 0.0125  0.0137  39  GLN A O   
114  C CB  . GLN A 22  ? 0.1186 0.0923 0.1099 -0.0472 0.0121  0.0010  39  GLN A CB  
115  C CG  . GLN A 22  ? 0.1194 0.1636 0.1127 -0.0349 0.0018  0.0265  39  GLN A CG  
116  C CD  . GLN A 22  ? 0.1079 0.1924 0.1172 -0.0347 -0.0016 0.0314  39  GLN A CD  
117  O OE1 . GLN A 22  ? 0.1207 0.2306 0.1230 -0.0053 -0.0003 0.0616  39  GLN A OE1 
118  N NE2 . GLN A 22  ? 0.1010 0.1980 0.1182 -0.0275 0.0001  0.0015  39  GLN A NE2 
119  N N   . ARG A 23  ? 0.0862 0.0736 0.1001 -0.0226 0.0120  0.0158  40  ARG A N   
120  C CA  . ARG A 23  ? 0.0679 0.0818 0.1012 -0.0094 0.0066  0.0105  40  ARG A CA  
121  C C   . ARG A 23  ? 0.0645 0.1128 0.1019 0.0397  0.0036  0.0081  40  ARG A C   
122  O O   . ARG A 23  ? 0.0886 0.1062 0.1032 0.0285  0.0056  0.0067  40  ARG A O   
123  C CB  . ARG A 23  ? 0.0856 0.0604 0.1070 0.0024  0.0025  0.0105  40  ARG A CB  
124  C CG  . ARG A 23  ? 0.0680 0.0643 0.1074 0.0096  0.0110  0.0010  40  ARG A CG  
125  C CD  . ARG A 23  ? 0.0676 0.1089 0.1063 0.0049  0.0143  -0.0046 40  ARG A CD  
126  N NE  . ARG A 23  ? 0.0959 0.1172 0.1057 0.0454  0.0281  0.0117  40  ARG A NE  
127  C CZ  . ARG A 23  ? 0.0948 0.1027 0.1064 -0.0056 0.0018  -0.0092 40  ARG A CZ  
128  N NH1 . ARG A 23  ? 0.0818 0.1664 0.1026 0.0432  -0.0208 0.0105  40  ARG A NH1 
129  N NH2 . ARG A 23  ? 0.1143 0.1816 0.1048 0.0712  0.0182  -0.0053 40  ARG A NH2 
130  N N   . GLN A 24  ? 0.0824 0.0961 0.1034 0.0201  0.0018  0.0049  41  GLN A N   
131  C CA  . GLN A 24  ? 0.0831 0.0978 0.0963 -0.0019 -0.0045 -0.0126 41  GLN A CA  
132  C C   . GLN A 24  ? 0.0765 0.1071 0.0943 -0.0089 -0.0008 -0.0245 41  GLN A C   
133  O O   . GLN A 24  ? 0.0865 0.1402 0.1070 -0.0211 0.0040  -0.0087 41  GLN A O   
134  C CB  . GLN A 24  ? 0.0822 0.1895 0.0933 -0.0540 0.0082  -0.0021 41  GLN A CB  
135  C CG  . GLN A 24  ? 0.1013 0.1707 0.0914 -0.0629 0.0009  -0.0156 41  GLN A CG  
136  C CD  . GLN A 24  ? 0.1114 0.1487 0.0947 -0.0619 0.0092  0.0016  41  GLN A CD  
137  O OE1 . GLN A 24  ? 0.1334 0.1326 0.0967 -0.0141 0.0201  0.0245  41  GLN A OE1 
138  N NE2 . GLN A 24  ? 0.1236 0.1553 0.1018 -0.0232 0.0040  0.0005  41  GLN A NE2 
139  N N   . VAL A 25  ? 0.0993 0.1171 0.0835 -0.0165 -0.0005 -0.0047 42  VAL A N   
140  C CA  . VAL A 25  ? 0.0878 0.1363 0.0796 -0.0073 0.0196  0.0160  42  VAL A CA  
141  C C   . VAL A 25  ? 0.0687 0.1202 0.0729 0.0308  0.0158  0.0221  42  VAL A C   
142  O O   . VAL A 25  ? 0.0870 0.0764 0.0696 0.0021  0.0115  0.0215  42  VAL A O   
143  C CB  . VAL A 25  ? 0.1139 0.1226 0.0871 -0.0178 0.0111  -0.0017 42  VAL A CB  
144  C CG1 . VAL A 25  ? 0.1446 0.2025 0.0962 0.0691  0.0123  -0.0084 42  VAL A CG1 
145  C CG2 . VAL A 25  ? 0.1238 0.1713 0.0779 -0.0600 0.0259  -0.0105 42  VAL A CG2 
146  N N   . VAL A 26  ? 0.0691 0.1187 0.0732 -0.0151 0.0078  0.0244  43  VAL A N   
147  C CA  . VAL A 26  ? 0.0488 0.0994 0.0792 0.0160  -0.0035 0.0216  43  VAL A CA  
148  C C   . VAL A 26  ? 0.0554 0.0935 0.0748 0.0165  -0.0101 0.0060  43  VAL A C   
149  O O   . VAL A 26  ? 0.0879 0.0697 0.0799 0.0119  0.0109  0.0134  43  VAL A O   
150  C CB  . VAL A 26  ? 0.0604 0.1496 0.0861 0.0222  -0.0082 0.0221  43  VAL A CB  
151  C CG1 . VAL A 26  ? 0.0963 0.1059 0.0890 0.0190  0.0013  0.0128  43  VAL A CG1 
152  C CG2 . VAL A 26  ? 0.0612 0.1356 0.0906 0.0025  -0.0034 0.0123  43  VAL A CG2 
153  N N   . GLY A 27  ? 0.0457 0.0960 0.0717 0.0043  -0.0231 0.0177  44  GLY A N   
154  C CA  . GLY A 27  ? 0.0572 0.0878 0.0772 0.0055  -0.0057 -0.0158 44  GLY A CA  
155  C C   . GLY A 27  ? 0.0728 0.1334 0.0907 0.0155  -0.0094 -0.0041 44  GLY A C   
156  O O   . GLY A 27  ? 0.0850 0.0917 0.0961 -0.0188 0.0023  -0.0040 44  GLY A O   
157  N N   . GLU A 28  ? 0.0866 0.0866 0.0967 0.0154  -0.0067 -0.0009 45  GLU A N   
158  C CA  . GLU A 28  ? 0.0528 0.0897 0.1097 -0.0105 0.0042  -0.0003 45  GLU A CA  
159  C C   . GLU A 28  ? 0.0730 0.0976 0.0930 0.0212  0.0050  -0.0007 45  GLU A C   
160  O O   . GLU A 28  ? 0.0787 0.0954 0.1011 0.0253  0.0195  0.0000  45  GLU A O   
161  C CB  . GLU A 28  ? 0.1228 0.0967 0.1346 -0.0052 -0.0093 -0.0095 45  GLU A CB  
162  C CG  . GLU A 28  ? 0.2189 0.1249 0.1692 0.0506  0.0121  -0.0023 45  GLU A CG  
163  C CD  . GLU A 28  ? 0.3222 0.2050 0.2021 0.0806  0.0237  -0.0088 45  GLU A CD  
164  O OE1 . GLU A 28  ? 0.3206 0.2421 0.2191 0.0267  -0.0056 -0.0461 45  GLU A OE1 
165  O OE2 . GLU A 28  ? 0.2653 0.2774 0.2137 0.0144  0.0341  0.0194  45  GLU A OE2 
166  N N   . ILE A 29  ? 0.0661 0.0875 0.0813 -0.0005 0.0102  0.0192  46  ILE A N   
167  C CA  . ILE A 29  ? 0.0913 0.0996 0.0697 0.0075  -0.0078 0.0224  46  ILE A CA  
168  C C   . ILE A 29  ? 0.0915 0.0736 0.0770 0.0459  0.0069  0.0141  46  ILE A C   
169  O O   . ILE A 29  ? 0.0844 0.1058 0.0777 0.0003  -0.0197 0.0053  46  ILE A O   
170  C CB  . ILE A 29  ? 0.0940 0.0880 0.0735 -0.0518 -0.0151 0.0174  46  ILE A CB  
171  C CG1 . ILE A 29  ? 0.0688 0.0811 0.0813 -0.0401 0.0002  0.0174  46  ILE A CG1 
172  C CG2 . ILE A 29  ? 0.0835 0.1432 0.0747 -0.0190 -0.0258 -0.0010 46  ILE A CG2 
173  C CD1 . ILE A 29  ? 0.1356 0.1166 0.0923 0.0001  -0.0196 -0.0025 46  ILE A CD1 
174  N N   . ILE A 30  ? 0.0638 0.1147 0.0904 -0.0017 0.0020  0.0098  47  ILE A N   
175  C CA  . ILE A 30  ? 0.0563 0.0839 0.0868 -0.0042 0.0073  0.0117  47  ILE A CA  
176  C C   . ILE A 30  ? 0.0581 0.0795 0.0804 -0.0052 0.0078  0.0041  47  ILE A C   
177  O O   . ILE A 30  ? 0.0709 0.1013 0.0802 0.0048  0.0223  0.0150  47  ILE A O   
178  C CB  . ILE A 30  ? 0.0628 0.0964 0.0861 -0.0346 0.0071  0.0050  47  ILE A CB  
179  C CG1 . ILE A 30  ? 0.0797 0.1419 0.0826 -0.0295 0.0040  0.0015  47  ILE A CG1 
180  C CG2 . ILE A 30  ? 0.1170 0.1028 0.0873 0.0109  0.0093  0.0207  47  ILE A CG2 
181  C CD1 . ILE A 30  ? 0.1252 0.1361 0.0865 0.0496  0.0015  0.0301  47  ILE A CD1 
182  N N   . SER A 31  ? 0.0628 0.1037 0.0814 0.0029  -0.0077 0.0023  48  SER A N   
183  C CA  . SER A 31  ? 0.0724 0.0678 0.0804 0.0403  -0.0012 -0.0069 48  SER A CA  
184  C C   . SER A 31  ? 0.0362 0.1022 0.0811 0.0124  -0.0071 -0.0219 48  SER A C   
185  O O   . SER A 31  ? 0.0562 0.1223 0.0780 -0.0191 0.0057  -0.0077 48  SER A O   
186  C CB  . SER A 31  ? 0.0779 0.1049 0.0827 0.0263  0.0030  -0.0041 48  SER A CB  
187  O OG  . SER A 31  ? 0.0959 0.0962 0.0767 0.0186  0.0168  -0.0034 48  SER A OG  
188  N N   . ARG A 32  ? 0.0766 0.0641 0.0801 -0.0039 -0.0010 -0.0071 49  ARG A N   
189  C CA  . ARG A 32  ? 0.0486 0.0809 0.0903 0.0337  -0.0011 -0.0048 49  ARG A CA  
190  C C   . ARG A 32  ? 0.0611 0.0894 0.0893 0.0036  -0.0138 0.0068  49  ARG A C   
191  O O   . ARG A 32  ? 0.0895 0.1170 0.0914 0.0183  0.0042  0.0153  49  ARG A O   
192  C CB  . ARG A 32  ? 0.0844 0.1091 0.1064 0.0346  -0.0134 -0.0131 49  ARG A CB  
193  C CG  . ARG A 32  ? 0.2080 0.0844 0.1273 0.0332  0.0009  -0.0076 49  ARG A CG  
194  C CD  . ARG A 32  ? 0.2837 0.1578 0.1461 0.0608  -0.0274 -0.0253 49  ARG A CD  
195  N NE  . ARG A 32  ? 0.2370 0.1329 0.1573 0.0146  -0.0265 -0.0444 49  ARG A NE  
196  C CZ  . ARG A 32  ? 0.1202 0.1765 0.1625 0.0157  -0.0237 -0.0322 49  ARG A CZ  
197  N NH1 . ARG A 32  ? 0.1723 0.1835 0.1674 0.0218  -0.0389 -0.0415 49  ARG A NH1 
198  N NH2 . ARG A 32  ? 0.1593 0.1840 0.1707 -0.0312 -0.0050 -0.0218 49  ARG A NH2 
199  N N   . PHE A 33  ? 0.0732 0.0731 0.0842 0.0088  -0.0004 0.0163  50  PHE A N   
200  C CA  . PHE A 33  ? 0.0817 0.0794 0.0808 0.0133  0.0014  0.0131  50  PHE A CA  
201  C C   . PHE A 33  ? 0.0893 0.0636 0.0800 -0.0125 0.0408  0.0130  50  PHE A C   
202  O O   . PHE A 33  ? 0.0786 0.0998 0.0817 -0.0151 0.0277  -0.0091 50  PHE A O   
203  C CB  . PHE A 33  ? 0.0973 0.0832 0.0815 0.0289  0.0099  0.0016  50  PHE A CB  
204  C CG  . PHE A 33  ? 0.1134 0.1008 0.0803 -0.0096 -0.0152 -0.0182 50  PHE A CG  
205  C CD1 . PHE A 33  ? 0.1158 0.1116 0.0864 -0.0277 0.0019  -0.0236 50  PHE A CD1 
206  C CD2 . PHE A 33  ? 0.1696 0.1055 0.0841 0.0291  -0.0308 -0.0059 50  PHE A CD2 
207  C CE1 . PHE A 33  ? 0.0907 0.1580 0.0905 -0.0504 0.0094  -0.0331 50  PHE A CE1 
208  C CE2 . PHE A 33  ? 0.1477 0.1019 0.0909 -0.0490 -0.0181 -0.0010 50  PHE A CE2 
209  C CZ  . PHE A 33  ? 0.1077 0.0878 0.0916 -0.0374 -0.0081 -0.0282 50  PHE A CZ  
210  N N   . GLU A 34  ? 0.0932 0.0859 0.0805 -0.0103 0.0432  0.0150  51  GLU A N   
211  C CA  . GLU A 34  ? 0.1100 0.0695 0.0831 -0.0005 0.0272  0.0022  51  GLU A CA  
212  C C   . GLU A 34  ? 0.1080 0.1319 0.0847 0.0209  0.0290  0.0008  51  GLU A C   
213  O O   . GLU A 34  ? 0.1235 0.0849 0.0871 -0.0092 0.0300  0.0060  51  GLU A O   
214  C CB  . GLU A 34  ? 0.1163 0.0455 0.0858 0.0081  0.0089  -0.0155 51  GLU A CB  
215  C CG  . GLU A 34  ? 0.0789 0.0738 0.0815 0.0160  0.0172  0.0034  51  GLU A CG  
216  C CD  . GLU A 34  ? 0.1059 0.0958 0.0851 0.0039  0.0095  0.0137  51  GLU A CD  
217  O OE1 . GLU A 34  ? 0.1583 0.0961 0.0817 0.0002  -0.0019 0.0198  51  GLU A OE1 
218  O OE2 . GLU A 34  ? 0.1090 0.1101 0.0992 0.0122  0.0029  0.0095  51  GLU A OE2 
219  N N   . LYS A 35  ? 0.0564 0.1111 0.0909 -0.0144 0.0200  0.0147  52  LYS A N   
220  C CA  . LYS A 35  ? 0.0909 0.0714 0.1028 0.0293  0.0244  0.0065  52  LYS A CA  
221  C C   . LYS A 35  ? 0.0568 0.1233 0.0909 0.0137  0.0202  0.0172  52  LYS A C   
222  O O   . LYS A 35  ? 0.0869 0.1177 0.0848 0.0105  0.0186  0.0208  52  LYS A O   
223  C CB  . LYS A 35  ? 0.0801 0.1416 0.1209 0.0461  0.0336  0.0054  52  LYS A CB  
224  C CG  . LYS A 35  ? 0.1148 0.1687 0.1411 0.0118  0.0357  0.0180  52  LYS A CG  
225  C CD  . LYS A 35  ? 0.2037 0.1860 0.1625 0.0169  0.0410  0.0451  52  LYS A CD  
226  C CE  . LYS A 35  ? 0.3038 0.3228 0.1749 0.0361  0.0555  0.0461  52  LYS A CE  
227  N NZ  . LYS A 35  ? 0.4131 0.3883 0.1804 0.1198  0.0474  0.0521  52  LYS A NZ  
228  N N   . ARG A 36  ? 0.0738 0.0736 0.0913 0.0040  0.0092  0.0006  53  ARG A N   
229  C CA  . ARG A 36  ? 0.0458 0.1008 0.0904 0.0093  0.0118  0.0061  53  ARG A CA  
230  C C   . ARG A 36  ? 0.0551 0.0771 0.0811 -0.0163 0.0096  0.0028  53  ARG A C   
231  O O   . ARG A 36  ? 0.1032 0.1003 0.0877 0.0089  0.0098  0.0158  53  ARG A O   
232  C CB  . ARG A 36  ? 0.0449 0.1174 0.0953 0.0296  -0.0017 -0.0106 53  ARG A CB  
233  C CG  . ARG A 36  ? 0.0530 0.1338 0.0937 0.0327  0.0156  0.0183  53  ARG A CG  
234  C CD  . ARG A 36  ? 0.0888 0.0631 0.0933 0.0014  0.0033  0.0097  53  ARG A CD  
235  N NE  . ARG A 36  ? 0.0997 0.0670 0.0845 0.0123  -0.0144 0.0103  53  ARG A NE  
236  C CZ  . ARG A 36  ? 0.0944 0.0980 0.0834 -0.0014 -0.0060 0.0011  53  ARG A CZ  
237  N NH1 . ARG A 36  ? 0.0920 0.1167 0.0877 -0.0090 -0.0045 -0.0176 53  ARG A NH1 
238  N NH2 . ARG A 36  ? 0.1078 0.1159 0.0806 -0.0151 -0.0039 -0.0010 53  ARG A NH2 
239  N N   . GLY A 37  ? 0.0555 0.0829 0.0757 0.0044  0.0050  0.0101  54  GLY A N   
240  C CA  . GLY A 37  ? 0.0666 0.0950 0.0919 -0.0267 0.0001  -0.0033 54  GLY A CA  
241  C C   . GLY A 37  ? 0.0676 0.0787 0.0972 0.0067  -0.0030 -0.0157 54  GLY A C   
242  O O   . GLY A 37  ? 0.1161 0.0926 0.1077 0.0175  -0.0076 -0.0074 54  GLY A O   
243  N N   . TYR A 38  ? 0.0342 0.1081 0.0870 -0.0071 0.0068  -0.0257 55  TYR A N   
244  C CA  . TYR A 38  ? 0.0485 0.0929 0.0793 -0.0160 -0.0033 -0.0220 55  TYR A CA  
245  C C   . TYR A 38  ? 0.0693 0.1107 0.0817 0.0059  0.0021  -0.0210 55  TYR A C   
246  O O   . TYR A 38  ? 0.1073 0.1100 0.0939 0.0321  -0.0178 -0.0106 55  TYR A O   
247  C CB  . TYR A 38  ? 0.0718 0.0707 0.0846 0.0144  0.0159  0.0004  55  TYR A CB  
248  C CG  . TYR A 38  ? 0.0615 0.0835 0.0770 0.0049  0.0152  -0.0031 55  TYR A CG  
249  C CD1 . TYR A 38  ? 0.1039 0.1038 0.0740 0.0098  0.0283  0.0074  55  TYR A CD1 
250  C CD2 . TYR A 38  ? 0.0698 0.0708 0.0765 0.0084  0.0058  -0.0085 55  TYR A CD2 
251  C CE1 . TYR A 38  ? 0.1081 0.1308 0.0839 -0.0123 0.0108  0.0039  55  TYR A CE1 
252  C CE2 . TYR A 38  ? 0.1075 0.0707 0.0817 0.0306  -0.0165 -0.0067 55  TYR A CE2 
253  C CZ  . TYR A 38  ? 0.0844 0.0968 0.0838 0.0152  -0.0156 -0.0069 55  TYR A CZ  
254  O OH  . TYR A 38  ? 0.1045 0.1135 0.0908 0.0216  -0.0055 0.0062  55  TYR A OH  
255  N N   . ARG A 39  ? 0.0613 0.0822 0.0833 0.0078  0.0067  -0.0029 56  ARG A N   
256  C CA  . ARG A 39  ? 0.0596 0.0807 0.0823 0.0156  0.0120  0.0125  56  ARG A CA  
257  C C   . ARG A 39  ? 0.0816 0.0721 0.0830 0.0334  -0.0153 0.0051  56  ARG A C   
258  O O   . ARG A 39  ? 0.0781 0.0942 0.0956 0.0119  -0.0008 0.0112  56  ARG A O   
259  C CB  . ARG A 39  ? 0.0639 0.0851 0.0872 -0.0026 0.0193  -0.0011 56  ARG A CB  
260  C CG  . ARG A 39  ? 0.0904 0.1075 0.0889 0.0297  0.0070  -0.0008 56  ARG A CG  
261  C CD  . ARG A 39  ? 0.0903 0.0596 0.1045 0.0104  0.0011  -0.0002 56  ARG A CD  
262  N NE  . ARG A 39  ? 0.0760 0.0731 0.1104 -0.0006 0.0028  0.0036  56  ARG A NE  
263  C CZ  . ARG A 39  ? 0.1144 0.0751 0.1198 0.0183  -0.0214 -0.0029 56  ARG A CZ  
264  N NH1 . ARG A 39  ? 0.1195 0.1589 0.1222 0.0383  -0.0029 0.0015  56  ARG A NH1 
265  N NH2 . ARG A 39  ? 0.1615 0.1011 0.1361 0.0369  -0.0332 0.0040  56  ARG A NH2 
266  N N   . ILE A 40  ? 0.0688 0.1043 0.0809 0.0259  -0.0144 0.0047  57  ILE A N   
267  C CA  . ILE A 40  ? 0.0589 0.1283 0.0909 0.0223  0.0172  0.0177  57  ILE A CA  
268  C C   . ILE A 40  ? 0.0765 0.1031 0.0912 0.0366  0.0133  0.0110  57  ILE A C   
269  O O   . ILE A 40  ? 0.1022 0.1100 0.0954 0.0200  0.0091  -0.0129 57  ILE A O   
270  C CB  . ILE A 40  ? 0.1026 0.0718 0.1058 0.0192  -0.0107 0.0142  57  ILE A CB  
271  C CG1 . ILE A 40  ? 0.1102 0.0706 0.1154 0.0212  -0.0074 0.0255  57  ILE A CG1 
272  C CG2 . ILE A 40  ? 0.0991 0.0550 0.1157 -0.0009 0.0142  0.0151  57  ILE A CG2 
273  C CD1 . ILE A 40  ? 0.1285 0.0657 0.1262 0.0270  -0.0174 0.0305  57  ILE A CD1 
274  N N   . ALA A 41  ? 0.0683 0.0615 0.0929 0.0351  -0.0136 -0.0036 58  ALA A N   
275  C CA  . ALA A 41  ? 0.0702 0.0510 0.1049 -0.0152 -0.0164 0.0029  58  ALA A CA  
276  C C   . ALA A 41  ? 0.0757 0.0792 0.1107 -0.0245 -0.0254 -0.0116 58  ALA A C   
277  O O   . ALA A 41  ? 0.1345 0.0807 0.1289 0.0441  -0.0149 0.0027  58  ALA A O   
278  C CB  . ALA A 41  ? 0.1209 0.0523 0.1084 0.0091  -0.0030 -0.0147 58  ALA A CB  
279  N N   . ALA A 42  ? 0.0949 0.0560 0.1061 -0.0135 0.0030  0.0063  59  ALA A N   
280  C CA  . ALA A 42  ? 0.0895 0.1328 0.1009 0.0091  -0.0089 0.0055  59  ALA A CA  
281  C C   . ALA A 42  ? 0.0726 0.0966 0.1000 0.0091  0.0057  -0.0034 59  ALA A C   
282  O O   . ALA A 42  ? 0.0955 0.0662 0.1012 -0.0045 0.0252  -0.0219 59  ALA A O   
283  C CB  . ALA A 42  ? 0.1209 0.1281 0.0999 -0.0211 -0.0177 0.0115  59  ALA A CB  
284  N N   . MET A 43  ? 0.0992 0.0716 0.1085 0.0141  0.0110  0.0065  60  MET A N   
285  C CA  . MET A 43  ? 0.1198 0.0490 0.1133 0.0170  0.0004  0.0147  60  MET A CA  
286  C C   . MET A 43  ? 0.1156 0.0965 0.1100 -0.0145 0.0153  0.0103  60  MET A C   
287  O O   . MET A 43  ? 0.1438 0.0972 0.1075 0.0038  0.0145  -0.0194 60  MET A O   
288  C CB  . MET A 43  ? 0.1062 0.0430 0.1182 0.0228  -0.0186 -0.0081 60  MET A CB  
289  C CG  . MET A 43  ? 0.1563 0.1061 0.1293 0.0218  -0.0222 -0.0194 60  MET A CG  
290  S SD  . MET A 43  ? 0.1797 0.1521 0.1251 0.0579  -0.0280 -0.0212 60  MET A SD  
291  C CE  . MET A 43  ? 0.1789 0.1221 0.1298 0.0386  -0.0319 -0.0261 60  MET A CE  
292  N N   . LYS A 44  ? 0.1009 0.0756 0.1163 -0.0423 0.0193  -0.0013 61  LYS A N   
293  C CA  . LYS A 44  ? 0.1178 0.1175 0.1382 0.0228  0.0359  0.0076  61  LYS A CA  
294  C C   . LYS A 44  ? 0.0752 0.0636 0.1157 -0.0287 0.0233  0.0118  61  LYS A C   
295  O O   . LYS A 44  ? 0.1454 0.0854 0.1158 -0.0168 0.0394  -0.0086 61  LYS A O   
296  C CB  . LYS A 44  ? 0.1187 0.1483 0.1845 0.0378  0.0570  0.0258  61  LYS A CB  
297  C CG  . LYS A 44  ? 0.1839 0.2885 0.2176 0.0993  0.0118  0.0189  61  LYS A CG  
298  C CD  . LYS A 44  ? 0.2169 0.3676 0.2339 0.1143  0.0123  0.0195  61  LYS A CD  
299  C CE  . LYS A 44  ? 0.2172 0.4586 0.2457 0.1580  0.0262  0.0208  61  LYS A CE  
300  N NZ  . LYS A 44  ? 0.2254 0.4271 0.2507 0.0689  0.0411  0.0179  61  LYS A NZ  
301  N N   . LEU A 45  ? 0.1079 0.0558 0.1170 -0.0087 0.0133  0.0102  62  LEU A N   
302  C CA  . LEU A 45  ? 0.0803 0.0637 0.1116 -0.0152 0.0134  0.0105  62  LEU A CA  
303  C C   . LEU A 45  ? 0.1063 0.0688 0.1160 -0.0398 -0.0040 -0.0112 62  LEU A C   
304  O O   . LEU A 45  ? 0.0896 0.0889 0.1156 0.0044  0.0146  -0.0332 62  LEU A O   
305  C CB  . LEU A 45  ? 0.0861 0.0997 0.1060 -0.0026 0.0111  0.0147  62  LEU A CB  
306  C CG  . LEU A 45  ? 0.0526 0.1552 0.1071 -0.0281 -0.0103 0.0256  62  LEU A CG  
307  C CD1 . LEU A 45  ? 0.1938 0.1169 0.1027 0.0450  -0.0058 0.0171  62  LEU A CD1 
308  C CD2 . LEU A 45  ? 0.1218 0.1246 0.1082 -0.0186 -0.0170 0.0087  62  LEU A CD2 
309  N N   . THR A 46  ? 0.0903 0.1039 0.1175 0.0016  0.0066  -0.0087 63  THR A N   
310  C CA  . THR A 46  ? 0.0530 0.0921 0.1274 -0.0175 -0.0079 -0.0201 63  THR A CA  
311  C C   . THR A 46  ? 0.1236 0.1166 0.1321 0.0371  0.0102  -0.0166 63  THR A C   
312  O O   . THR A 46  ? 0.0963 0.0741 0.1470 0.0320  0.0283  -0.0149 63  THR A O   
313  C CB  . THR A 46  ? 0.0936 0.1496 0.1321 0.0063  -0.0019 -0.0063 63  THR A CB  
314  O OG1 . THR A 46  ? 0.1338 0.1439 0.1372 0.0106  0.0006  0.0019  63  THR A OG1 
315  C CG2 . THR A 46  ? 0.0883 0.1471 0.1292 0.0056  -0.0170 0.0059  63  THR A CG2 
316  N N   . ILE A 47  ? 0.0883 0.1130 0.1381 0.0117  -0.0015 -0.0162 64  ILE A N   
317  C CA  . ILE A 47  ? 0.0674 0.1599 0.1385 0.0092  0.0150  -0.0134 64  ILE A CA  
318  C C   . ILE A 47  ? 0.0554 0.1375 0.1382 -0.0330 0.0041  -0.0241 64  ILE A C   
319  O O   . ILE A 47  ? 0.0719 0.1685 0.1418 0.0434  -0.0099 -0.0317 64  ILE A O   
320  C CB  . ILE A 47  ? 0.0950 0.0932 0.1363 -0.0022 0.0067  -0.0125 64  ILE A CB  
321  C CG1 . ILE A 47  ? 0.1449 0.1939 0.1297 0.0255  0.0427  -0.0212 64  ILE A CG1 
322  C CG2 . ILE A 47  ? 0.1249 0.1895 0.1417 -0.0102 0.0201  0.0094  64  ILE A CG2 
323  C CD1 . ILE A 47  ? 0.1524 0.2272 0.1370 -0.0370 0.0687  -0.0215 64  ILE A CD1 
324  N N   . ALA A 48  ? 0.0654 0.1157 0.1467 0.0063  0.0046  -0.0400 65  ALA A N   
325  C CA  . ALA A 48  ? 0.0653 0.1056 0.1496 0.0138  0.0009  -0.0311 65  ALA A CA  
326  C C   . ALA A 48  ? 0.0607 0.0973 0.1555 -0.0015 0.0062  -0.0065 65  ALA A C   
327  O O   . ALA A 48  ? 0.1136 0.1128 0.1573 -0.0157 -0.0082 -0.0093 65  ALA A O   
328  C CB  . ALA A 48  ? 0.1272 0.0880 0.1473 0.0235  -0.0162 -0.0325 65  ALA A CB  
329  N N   . THR A 49  ? 0.0644 0.1501 0.1585 0.0243  0.0066  0.0138  66  THR A N   
330  C CA  . THR A 49  ? 0.0642 0.2113 0.1673 -0.0342 0.0053  -0.0070 66  THR A CA  
331  C C   . THR A 49  ? 0.0737 0.1653 0.1681 0.0019  0.0104  -0.0179 66  THR A C   
332  O O   . THR A 49  ? 0.0692 0.1575 0.1629 -0.0210 -0.0187 -0.0226 66  THR A O   
333  C CB  . THR A 49  ? 0.0795 0.2449 0.1800 -0.0450 -0.0106 -0.0170 66  THR A CB  
334  O OG1 . THR A 49  ? 0.1569 0.2419 0.2013 0.0699  -0.0162 -0.0421 66  THR A OG1 
335  C CG2 . THR A 49  ? 0.1102 0.3376 0.1826 -0.0652 -0.0070 -0.0246 66  THR A CG2 
336  N N   . PRO A 50  ? 0.1044 0.1679 0.1754 -0.0076 0.0224  -0.0138 67  PRO A N   
337  C CA  . PRO A 50  ? 0.0883 0.1559 0.1722 -0.0256 0.0139  -0.0290 67  PRO A CA  
338  C C   . PRO A 50  ? 0.0866 0.1478 0.1671 -0.0186 0.0281  -0.0211 67  PRO A C   
339  O O   . PRO A 50  ? 0.0923 0.2172 0.1601 -0.0200 0.0382  -0.0207 67  PRO A O   
340  C CB  . PRO A 50  ? 0.0741 0.1724 0.1757 -0.0089 0.0226  -0.0343 67  PRO A CB  
341  C CG  . PRO A 50  ? 0.1424 0.1631 0.1801 -0.0021 0.0165  -0.0374 67  PRO A CG  
342  C CD  . PRO A 50  ? 0.1059 0.1224 0.1783 -0.0506 0.0191  -0.0148 67  PRO A CD  
343  N N   . ALA A 51  ? 0.1026 0.1833 0.1708 -0.0229 0.0242  -0.0208 68  ALA A N   
344  C CA  . ALA A 51  ? 0.0543 0.1837 0.1691 0.0023  -0.0003 -0.0184 68  ALA A CA  
345  C C   . ALA A 51  ? 0.0532 0.1693 0.1667 -0.0214 -0.0092 -0.0123 68  ALA A C   
346  O O   . ALA A 51  ? 0.1273 0.1948 0.1770 -0.0202 0.0032  -0.0087 68  ALA A O   
347  C CB  . ALA A 51  ? 0.1044 0.2783 0.1766 0.0614  0.0194  -0.0139 68  ALA A CB  
348  N N   . ILE A 52  ? 0.0749 0.0962 0.1626 0.0000  -0.0082 -0.0036 69  ILE A N   
349  C CA  . ILE A 52  ? 0.0776 0.1416 0.1638 0.0278  -0.0030 0.0017  69  ILE A CA  
350  C C   . ILE A 52  ? 0.0748 0.1027 0.1567 0.0130  -0.0001 -0.0128 69  ILE A C   
351  O O   . ILE A 52  ? 0.1115 0.1026 0.1563 0.0137  0.0182  -0.0028 69  ILE A O   
352  C CB  . ILE A 52  ? 0.1306 0.2209 0.1702 -0.0302 -0.0233 -0.0036 69  ILE A CB  
353  C CG1 . ILE A 52  ? 0.1242 0.2054 0.1726 -0.0470 -0.0539 -0.0250 69  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.1415 0.1712 0.1689 0.0018  -0.0415 -0.0100 69  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.1508 0.2146 0.1745 -0.0450 -0.0787 -0.0250 69  ILE A CD1 
356  N N   . LEU A 53  ? 0.0883 0.1166 0.1510 0.0079  0.0103  -0.0215 70  LEU A N   
357  C CA  . LEU A 53  ? 0.0942 0.1391 0.1519 0.0274  0.0108  -0.0233 70  LEU A CA  
358  C C   . LEU A 53  ? 0.0804 0.1067 0.1512 -0.0015 0.0183  -0.0003 70  LEU A C   
359  O O   . LEU A 53  ? 0.1032 0.1280 0.1464 0.0338  0.0215  -0.0003 70  LEU A O   
360  C CB  . LEU A 53  ? 0.0825 0.1185 0.1476 0.0530  0.0064  -0.0169 70  LEU A CB  
361  C CG  . LEU A 53  ? 0.0497 0.1408 0.1574 -0.0094 -0.0153 -0.0144 70  LEU A CG  
362  C CD1 . LEU A 53  ? 0.0701 0.1112 0.1690 0.0406  -0.0050 -0.0035 70  LEU A CD1 
363  C CD2 . LEU A 53  ? 0.0624 0.1523 0.1567 0.0136  -0.0244 -0.0601 70  LEU A CD2 
364  N N   . GLU A 54  ? 0.1007 0.1201 0.1531 -0.0356 0.0080  -0.0100 71  GLU A N   
365  C CA  . GLU A 54  ? 0.1156 0.1977 0.1690 -0.0153 0.0115  0.0192  71  GLU A CA  
366  C C   . GLU A 54  ? 0.1196 0.2742 0.1676 0.0076  -0.0012 0.0124  71  GLU A C   
367  O O   . GLU A 54  ? 0.1405 0.2784 0.1595 -0.0849 0.0031  0.0231  71  GLU A O   
368  C CB  . GLU A 54  ? 0.1792 0.3426 0.1908 -0.0339 0.0185  0.0590  71  GLU A CB  
369  C CG  . GLU A 54  ? 0.3443 0.6133 0.2129 0.0762  0.0219  0.1041  71  GLU A CG  
370  C CD  . GLU A 54  ? 0.4126 0.7682 0.2338 0.0221  0.0182  0.1301  71  GLU A CD  
371  O OE1 . GLU A 54  ? 0.4346 0.8429 0.2434 0.0369  0.0120  0.1228  71  GLU A OE1 
372  O OE2 . GLU A 54  ? 0.4156 0.7560 0.2440 -0.0808 0.0193  0.1368  71  GLU A OE2 
373  N N   . GLU A 55  ? 0.0847 0.2477 0.1734 0.0277  -0.0210 -0.0087 72  GLU A N   
374  C CA  . GLU A 55  ? 0.1323 0.1672 0.1771 0.0314  0.0110  0.0258  72  GLU A CA  
375  C C   . GLU A 55  ? 0.1171 0.0816 0.1592 0.0002  0.0016  0.0246  72  GLU A C   
376  O O   . GLU A 55  ? 0.1385 0.1139 0.1606 0.0204  0.0096  0.0470  72  GLU A O   
377  C CB  . GLU A 55  ? 0.2408 0.2922 0.2100 0.0991  0.0383  0.0320  72  GLU A CB  
378  C CG  . GLU A 55  ? 0.3863 0.4598 0.2343 0.1969  0.0358  0.0419  72  GLU A CG  
379  C CD  . GLU A 55  ? 0.5869 0.6396 0.2536 0.3647  0.0391  0.0428  72  GLU A CD  
380  O OE1 . GLU A 55  ? 0.6126 0.7135 0.2702 0.3928  0.0323  0.0365  72  GLU A OE1 
381  O OE2 . GLU A 55  ? 0.6797 0.6629 0.2731 0.3945  0.0402  0.0367  72  GLU A OE2 
382  N N   . HIS A 56  ? 0.0923 0.1432 0.1463 -0.0079 -0.0130 0.0063  73  HIS A N   
383  C CA  . HIS A 56  ? 0.0807 0.0960 0.1393 -0.0001 -0.0119 -0.0026 73  HIS A CA  
384  C C   . HIS A 56  ? 0.0934 0.1134 0.1280 -0.0095 0.0069  0.0165  73  HIS A C   
385  O O   . HIS A 56  ? 0.1450 0.2114 0.1201 -0.0241 0.0171  0.0080  73  HIS A O   
386  C CB  . HIS A 56  ? 0.0479 0.1735 0.1385 -0.0115 -0.0007 -0.0104 73  HIS A CB  
387  C CG  . HIS A 56  ? 0.0519 0.1519 0.1398 -0.0220 -0.0046 -0.0266 73  HIS A CG  
388  N ND1 . HIS A 56  ? 0.0827 0.1585 0.1356 0.0350  -0.0185 -0.0063 73  HIS A ND1 
389  C CD2 . HIS A 56  ? 0.1217 0.1872 0.1474 0.0312  -0.0014 -0.0300 73  HIS A CD2 
390  C CE1 . HIS A 56  ? 0.0934 0.1991 0.1390 -0.0014 -0.0304 -0.0418 73  HIS A CE1 
391  N NE2 . HIS A 56  ? 0.0963 0.2171 0.1494 0.0413  -0.0143 -0.0245 73  HIS A NE2 
392  N N   . TYR A 57  ? 0.0863 0.1480 0.1271 -0.0150 -0.0126 -0.0122 74  TYR A N   
393  C CA  . TYR A 57  ? 0.0935 0.1492 0.1365 -0.0561 -0.0044 -0.0230 74  TYR A CA  
394  C C   . TYR A 57  ? 0.1274 0.1410 0.1473 0.0186  -0.0248 0.0046  74  TYR A C   
395  O O   . TYR A 57  ? 0.1958 0.2143 0.1457 -0.0077 -0.0456 -0.0320 74  TYR A O   
396  C CB  . TYR A 57  ? 0.1344 0.1078 0.1420 -0.0636 -0.0143 -0.0237 74  TYR A CB  
397  C CG  . TYR A 57  ? 0.1248 0.1544 0.1449 -0.0179 0.0066  -0.0119 74  TYR A CG  
398  C CD1 . TYR A 57  ? 0.1035 0.1712 0.1479 -0.0197 -0.0067 -0.0280 74  TYR A CD1 
399  C CD2 . TYR A 57  ? 0.1420 0.2329 0.1571 0.0602  0.0295  0.0290  74  TYR A CD2 
400  C CE1 . TYR A 57  ? 0.0974 0.2114 0.1558 -0.0053 0.0147  0.0040  74  TYR A CE1 
401  C CE2 . TYR A 57  ? 0.1571 0.2961 0.1588 0.0949  0.0342  0.0472  74  TYR A CE2 
402  C CZ  . TYR A 57  ? 0.1658 0.2044 0.1615 0.0293  0.0330  0.0470  74  TYR A CZ  
403  O OH  . TYR A 57  ? 0.1849 0.2373 0.1723 0.0273  0.0258  0.0558  74  TYR A OH  
404  N N   . ALA A 58  ? 0.1540 0.1339 0.1607 0.0175  -0.0264 -0.0009 75  ALA A N   
405  C CA  . ALA A 58  ? 0.2137 0.1509 0.1611 -0.0155 -0.0318 0.0164  75  ALA A CA  
406  C C   . ALA A 58  ? 0.2531 0.1539 0.1622 -0.0148 -0.0492 0.0032  75  ALA A C   
407  O O   . ALA A 58  ? 0.2615 0.2245 0.1702 -0.0638 -0.0781 -0.0146 75  ALA A O   
408  C CB  . ALA A 58  ? 0.2010 0.2456 0.1619 0.0100  -0.0398 0.0222  75  ALA A CB  
409  N N   . GLU A 59  ? 0.2855 0.2018 0.1638 0.0036  -0.0186 0.0015  76  GLU A N   
410  C CA  . GLU A 59  ? 0.2757 0.2491 0.1739 -0.0668 -0.0024 -0.0044 76  GLU A CA  
411  C C   . GLU A 59  ? 0.3222 0.2412 0.1749 -0.0307 -0.0200 -0.0115 76  GLU A C   
412  O O   . GLU A 59  ? 0.3570 0.2196 0.1689 -0.0552 -0.0289 -0.0174 76  GLU A O   
413  C CB  . GLU A 59  ? 0.2827 0.2825 0.1903 -0.1214 0.0036  -0.0054 76  GLU A CB  
414  C CG  . GLU A 59  ? 0.2889 0.3506 0.2104 -0.0865 0.0033  -0.0029 76  GLU A CG  
415  C CD  . GLU A 59  ? 0.3803 0.4453 0.2306 -0.0685 0.0002  -0.0098 76  GLU A CD  
416  O OE1 . GLU A 59  ? 0.3642 0.4896 0.2476 -0.0877 0.0047  -0.0202 76  GLU A OE1 
417  O OE2 . GLU A 59  ? 0.4063 0.4616 0.2358 -0.0807 -0.0136 -0.0212 76  GLU A OE2 
418  N N   . HIS A 60  ? 0.2001 0.2150 0.1776 -0.0614 -0.0166 -0.0139 77  HIS A N   
419  C CA  . HIS A 60  ? 0.2031 0.2014 0.1962 -0.0272 -0.0202 -0.0053 77  HIS A CA  
420  C C   . HIS A 60  ? 0.1854 0.2214 0.2143 -0.0033 -0.0301 -0.0050 77  HIS A C   
421  O O   . HIS A 60  ? 0.1633 0.2186 0.2187 0.0257  -0.0150 -0.0091 77  HIS A O   
422  C CB  . HIS A 60  ? 0.2385 0.2507 0.1982 0.0092  -0.0186 -0.0253 77  HIS A CB  
423  C CG  . HIS A 60  ? 0.2472 0.2607 0.2080 0.0144  -0.0010 -0.0373 77  HIS A CG  
424  N ND1 . HIS A 60  ? 0.2598 0.2707 0.2207 -0.0156 0.0076  -0.0405 77  HIS A ND1 
425  C CD2 . HIS A 60  ? 0.1971 0.3123 0.2158 0.0298  0.0045  -0.0452 77  HIS A CD2 
426  C CE1 . HIS A 60  ? 0.2193 0.3316 0.2216 -0.0125 0.0144  -0.0376 77  HIS A CE1 
427  N NE2 . HIS A 60  ? 0.1927 0.3223 0.2208 -0.0514 0.0092  -0.0363 77  HIS A NE2 
428  N N   . LYS A 61  ? 0.2295 0.1986 0.2321 0.0533  -0.0354 -0.0137 78  LYS A N   
429  C CA  . LYS A 61  ? 0.1756 0.2084 0.2527 0.0402  -0.0617 -0.0143 78  LYS A CA  
430  C C   . LYS A 61  ? 0.1908 0.2432 0.2546 0.0271  -0.0643 -0.0127 78  LYS A C   
431  O O   . LYS A 61  ? 0.2510 0.2561 0.2544 0.0028  -0.0747 -0.0141 78  LYS A O   
432  C CB  . LYS A 61  ? 0.2377 0.2939 0.2712 0.1068  -0.0652 -0.0049 78  LYS A CB  
433  C CG  . LYS A 61  ? 0.3830 0.4242 0.2857 0.1807  -0.0735 -0.0122 78  LYS A CG  
434  C CD  . LYS A 61  ? 0.5043 0.5087 0.2962 0.2470  -0.0747 -0.0273 78  LYS A CD  
435  C CE  . LYS A 61  ? 0.5432 0.5923 0.3015 0.2411  -0.0854 -0.0427 78  LYS A CE  
436  N NZ  . LYS A 61  ? 0.6059 0.6503 0.3033 0.2518  -0.0892 -0.0500 78  LYS A NZ  
437  N N   . GLY A 62  ? 0.1716 0.1975 0.2553 0.0064  -0.0544 -0.0251 79  GLY A N   
438  C CA  . GLY A 62  ? 0.1690 0.2230 0.2492 -0.0226 -0.0544 -0.0466 79  GLY A CA  
439  C C   . GLY A 62  ? 0.2022 0.3011 0.2449 0.0207  -0.0409 -0.0593 79  GLY A C   
440  O O   . GLY A 62  ? 0.2092 0.3348 0.2556 -0.0244 -0.0536 -0.0690 79  GLY A O   
441  N N   . LYS A 63  ? 0.2058 0.2285 0.2317 0.0067  -0.0228 -0.0656 80  LYS A N   
442  C CA  . LYS A 63  ? 0.1717 0.2055 0.2180 0.0243  0.0001  -0.0600 80  LYS A CA  
443  C C   . LYS A 63  ? 0.1824 0.1883 0.2050 -0.0222 -0.0040 -0.0457 80  LYS A C   
444  O O   . LYS A 63  ? 0.1915 0.2261 0.2091 0.0126  -0.0032 -0.0449 80  LYS A O   
445  C CB  . LYS A 63  ? 0.1989 0.2092 0.2221 0.0070  0.0160  -0.0394 80  LYS A CB  
446  C CG  . LYS A 63  ? 0.2341 0.2481 0.2252 -0.0862 0.0262  -0.0478 80  LYS A CG  
447  C CD  . LYS A 63  ? 0.2996 0.2803 0.2290 -0.1335 0.0224  -0.0541 80  LYS A CD  
448  C CE  . LYS A 63  ? 0.3459 0.3301 0.2324 -0.1487 0.0401  -0.0472 80  LYS A CE  
449  N NZ  . LYS A 63  ? 0.3417 0.4556 0.2334 -0.1285 0.0511  -0.0369 80  LYS A NZ  
450  N N   . PRO A 64  ? 0.2195 0.2282 0.1908 0.0210  -0.0119 -0.0350 81  PRO A N   
451  C CA  . PRO A 64  ? 0.2491 0.1464 0.1857 -0.0535 -0.0250 -0.0340 81  PRO A CA  
452  C C   . PRO A 64  ? 0.2649 0.1858 0.1815 -0.0498 -0.0202 -0.0260 81  PRO A C   
453  O O   . PRO A 64  ? 0.2824 0.2001 0.1740 -0.0483 -0.0061 -0.0042 81  PRO A O   
454  C CB  . PRO A 64  ? 0.2948 0.1853 0.1895 0.0300  -0.0352 -0.0493 81  PRO A CB  
455  C CG  . PRO A 64  ? 0.2369 0.1915 0.1830 0.0077  -0.0400 -0.0760 81  PRO A CG  
456  C CD  . PRO A 64  ? 0.2567 0.2420 0.1837 0.0286  -0.0440 -0.0690 81  PRO A CD  
457  N N   . PHE A 65  ? 0.2006 0.1899 0.1781 -0.0569 -0.0459 -0.0448 82  PHE A N   
458  C CA  . PHE A 65  ? 0.2668 0.1474 0.1788 -0.0175 -0.0444 -0.0238 82  PHE A CA  
459  C C   . PHE A 65  ? 0.3147 0.1206 0.1676 -0.0033 -0.0594 -0.0091 82  PHE A C   
460  O O   . PHE A 65  ? 0.3054 0.1316 0.1597 0.0108  -0.0828 -0.0059 82  PHE A O   
461  C CB  . PHE A 65  ? 0.3052 0.2085 0.1886 0.0542  -0.0100 -0.0259 82  PHE A CB  
462  C CG  . PHE A 65  ? 0.2988 0.2348 0.2034 0.0777  -0.0082 -0.0161 82  PHE A CG  
463  C CD1 . PHE A 65  ? 0.2763 0.2801 0.2125 0.0909  0.0007  -0.0022 82  PHE A CD1 
464  C CD2 . PHE A 65  ? 0.3133 0.2770 0.2116 0.0511  -0.0214 -0.0041 82  PHE A CD2 
465  C CE1 . PHE A 65  ? 0.2952 0.2734 0.2180 0.0886  0.0007  0.0025  82  PHE A CE1 
466  C CE2 . PHE A 65  ? 0.2902 0.2465 0.2165 0.0474  -0.0156 0.0018  82  PHE A CE2 
467  C CZ  . PHE A 65  ? 0.2909 0.1539 0.2194 -0.0107 -0.0055 0.0023  82  PHE A CZ  
468  N N   . LEU A 66  ? 0.2964 0.1265 0.1610 0.0035  -0.0596 -0.0184 83  LEU A N   
469  C CA  . LEU A 66  ? 0.2364 0.1317 0.1558 -0.0212 -0.0350 -0.0317 83  LEU A CA  
470  C C   . LEU A 66  ? 0.2060 0.1801 0.1578 -0.0803 -0.0262 -0.0425 83  LEU A C   
471  O O   . LEU A 66  ? 0.2232 0.1681 0.1621 -0.0257 -0.0386 -0.0549 83  LEU A O   
472  C CB  . LEU A 66  ? 0.2391 0.1145 0.1621 -0.0191 -0.0416 -0.0355 83  LEU A CB  
473  C CG  . LEU A 66  ? 0.1972 0.1428 0.1658 -0.0219 -0.0252 -0.0131 83  LEU A CG  
474  C CD1 . LEU A 66  ? 0.2253 0.1587 0.1662 -0.0668 -0.0263 -0.0035 83  LEU A CD1 
475  C CD2 . LEU A 66  ? 0.2400 0.1632 0.1716 0.0374  -0.0283 -0.0363 83  LEU A CD2 
476  N N   . PRO A 67  ? 0.1657 0.2231 0.1586 -0.0731 -0.0230 -0.0547 84  PRO A N   
477  C CA  . PRO A 67  ? 0.1945 0.2462 0.1611 -0.0547 -0.0263 -0.0446 84  PRO A CA  
478  C C   . PRO A 67  ? 0.2209 0.2329 0.1593 -0.0632 -0.0329 -0.0439 84  PRO A C   
479  O O   . PRO A 67  ? 0.2430 0.1761 0.1627 -0.0371 -0.0224 -0.0392 84  PRO A O   
480  C CB  . PRO A 67  ? 0.2774 0.2337 0.1638 -0.0548 -0.0198 -0.0274 84  PRO A CB  
481  C CG  . PRO A 67  ? 0.2201 0.3238 0.1651 -0.0799 -0.0287 -0.0375 84  PRO A CG  
482  C CD  . PRO A 67  ? 0.1931 0.3231 0.1633 -0.0458 -0.0205 -0.0463 84  PRO A CD  
483  N N   . GLY A 68  ? 0.2512 0.2445 0.1619 -0.0369 -0.0489 -0.0521 85  GLY A N   
484  C CA  . GLY A 68  ? 0.2615 0.2433 0.1647 0.0098  -0.0468 -0.0557 85  GLY A CA  
485  C C   . GLY A 68  ? 0.2387 0.1772 0.1697 -0.0094 -0.0514 -0.0465 85  GLY A C   
486  O O   . GLY A 68  ? 0.3065 0.1840 0.1708 -0.0035 -0.0710 -0.0574 85  GLY A O   
487  N N   . LEU A 69  ? 0.1966 0.1782 0.1740 0.0087  -0.0450 -0.0482 86  LEU A N   
488  C CA  . LEU A 69  ? 0.1886 0.2170 0.1756 0.0092  -0.0315 -0.0565 86  LEU A CA  
489  C C   . LEU A 69  ? 0.1714 0.2077 0.1676 -0.0315 -0.0321 -0.0521 86  LEU A C   
490  O O   . LEU A 69  ? 0.1743 0.1969 0.1636 0.0134  -0.0512 -0.0677 86  LEU A O   
491  C CB  . LEU A 69  ? 0.1626 0.2645 0.1860 -0.0638 -0.0200 -0.0266 86  LEU A CB  
492  C CG  . LEU A 69  ? 0.1780 0.3196 0.1938 -0.1064 -0.0338 -0.0132 86  LEU A CG  
493  C CD1 . LEU A 69  ? 0.1961 0.3807 0.2024 -0.1085 -0.0388 -0.0009 86  LEU A CD1 
494  C CD2 . LEU A 69  ? 0.2425 0.4199 0.1961 -0.0061 -0.0273 -0.0014 86  LEU A CD2 
495  N N   . ILE A 70  ? 0.1676 0.1620 0.1637 -0.0102 -0.0312 -0.0370 87  ILE A N   
496  C CA  A ILE A 70  ? 0.2014 0.1551 0.1668 0.0156  -0.0242 -0.0200 87  ILE A CA  
497  C CA  B ILE A 70  ? 0.2072 0.1389 0.1642 0.0044  -0.0347 -0.0407 87  ILE A CA  
498  C C   . ILE A 70  ? 0.2017 0.1102 0.1654 -0.0083 -0.0436 -0.0376 87  ILE A C   
499  O O   . ILE A 70  ? 0.2472 0.1445 0.1515 0.0074  -0.0561 -0.0601 87  ILE A O   
500  C CB  A ILE A 70  ? 0.2056 0.2153 0.1713 0.0632  -0.0226 -0.0178 87  ILE A CB  
501  C CB  B ILE A 70  ? 0.2307 0.1366 0.1635 0.0156  -0.0425 -0.0636 87  ILE A CB  
502  C CG1 A ILE A 70  ? 0.2100 0.3260 0.1758 0.0805  -0.0223 -0.0097 87  ILE A CG1 
503  C CG1 B ILE A 70  ? 0.2674 0.1488 0.1646 0.0515  -0.0511 -0.0737 87  ILE A CG1 
504  C CG2 A ILE A 70  ? 0.1624 0.2100 0.1757 0.0393  -0.0165 -0.0262 87  ILE A CG2 
505  C CG2 B ILE A 70  ? 0.2100 0.1316 0.1654 0.0113  -0.0383 -0.0664 87  ILE A CG2 
506  C CD1 A ILE A 70  ? 0.1900 0.4328 0.1821 0.1268  -0.0108 0.0056  87  ILE A CD1 
507  C CD1 B ILE A 70  ? 0.2855 0.1892 0.1636 0.0500  -0.0559 -0.0746 87  ILE A CD1 
508  N N   . GLU A 71  ? 0.2077 0.1661 0.1785 -0.0161 -0.0219 0.0017  88  GLU A N   
509  C CA  . GLU A 71  ? 0.2277 0.1596 0.1981 -0.0370 -0.0037 -0.0026 88  GLU A CA  
510  C C   . GLU A 71  ? 0.2120 0.1416 0.1818 -0.0522 -0.0065 -0.0053 88  GLU A C   
511  O O   . GLU A 71  ? 0.2028 0.1738 0.1715 -0.0512 -0.0187 -0.0327 88  GLU A O   
512  C CB  . GLU A 71  ? 0.2859 0.2032 0.2364 -0.0673 0.0109  -0.0092 88  GLU A CB  
513  C CG  . GLU A 71  ? 0.4846 0.3452 0.2724 0.0117  0.0050  -0.0386 88  GLU A CG  
514  C CD  . GLU A 71  ? 0.5881 0.5809 0.3038 0.0732  0.0134  -0.0461 88  GLU A CD  
515  O OE1 . GLU A 71  ? 0.5985 0.6306 0.3140 0.1090  0.0319  -0.0351 88  GLU A OE1 
516  O OE2 . GLU A 71  ? 0.5751 0.6191 0.3162 -0.0007 0.0104  -0.0554 88  GLU A OE2 
517  N N   . LYS A 72  ? 0.2165 0.1194 0.1720 -0.0249 0.0048  -0.0205 89  LYS A N   
518  C CA  . LYS A 72  ? 0.2488 0.1898 0.1675 0.0154  -0.0191 -0.0365 89  LYS A CA  
519  C C   . LYS A 72  ? 0.1428 0.1241 0.1544 0.0572  -0.0226 -0.0066 89  LYS A C   
520  O O   . LYS A 72  ? 0.1681 0.1505 0.1496 0.0342  -0.0207 0.0153  89  LYS A O   
521  C CB  . LYS A 72  ? 0.3735 0.1698 0.1810 0.0710  -0.0341 -0.0678 89  LYS A CB  
522  C CG  . LYS A 72  ? 0.4376 0.2194 0.1914 0.1196  -0.0677 -0.0705 89  LYS A CG  
523  C CD  . LYS A 72  ? 0.4999 0.2871 0.2032 0.1148  -0.0795 -0.0438 89  LYS A CD  
524  C CE  . LYS A 72  ? 0.5280 0.3365 0.2121 0.0812  -0.0868 -0.0200 89  LYS A CE  
525  N NZ  . LYS A 72  ? 0.5197 0.2881 0.2212 -0.0242 -0.0946 -0.0135 89  LYS A NZ  
526  N N   . MET A 73  ? 0.1172 0.1393 0.1481 0.0136  -0.0152 -0.0339 90  MET A N   
527  C CA  . MET A 73  ? 0.1028 0.1732 0.1448 0.0079  -0.0131 -0.0036 90  MET A CA  
528  C C   . MET A 73  ? 0.0580 0.1664 0.1450 -0.0237 -0.0123 -0.0019 90  MET A C   
529  O O   . MET A 73  ? 0.0626 0.1544 0.1509 -0.0198 -0.0193 0.0092  90  MET A O   
530  C CB  . MET A 73  ? 0.1114 0.1314 0.1463 -0.0107 -0.0185 0.0015  90  MET A CB  
531  C CG  . MET A 73  ? 0.0782 0.2021 0.1466 0.0455  -0.0102 0.0007  90  MET A CG  
532  S SD  . MET A 73  ? 0.1017 0.1937 0.1419 0.0155  -0.0148 -0.0020 90  MET A SD  
533  C CE  . MET A 73  ? 0.1250 0.1930 0.1507 0.0195  -0.0003 0.0053  90  MET A CE  
534  N N   . THR A 74  ? 0.0756 0.1171 0.1478 -0.0177 -0.0021 -0.0175 91  THR A N   
535  C CA  . THR A 74  ? 0.1056 0.1207 0.1498 0.0086  -0.0068 -0.0158 91  THR A CA  
536  C C   . THR A 74  ? 0.0875 0.1297 0.1547 0.0098  -0.0296 0.0032  91  THR A C   
537  O O   . THR A 74  ? 0.2064 0.1187 0.1666 -0.0180 -0.0665 0.0078  91  THR A O   
538  C CB  . THR A 74  ? 0.1053 0.2031 0.1554 -0.0162 -0.0034 -0.0164 91  THR A CB  
539  O OG1 . THR A 74  ? 0.1023 0.2027 0.1599 -0.0105 -0.0128 -0.0292 91  THR A OG1 
540  C CG2 . THR A 74  ? 0.0906 0.1911 0.1613 -0.0553 0.0281  0.0152  91  THR A CG2 
541  N N   . GLY A 75  ? 0.0573 0.1303 0.1456 -0.0259 -0.0234 -0.0016 92  GLY A N   
542  C CA  . GLY A 75  ? 0.0662 0.1238 0.1389 -0.0411 -0.0154 0.0134  92  GLY A CA  
543  C C   . GLY A 75  ? 0.0762 0.1121 0.1252 -0.0010 -0.0029 -0.0028 92  GLY A C   
544  O O   . GLY A 75  ? 0.0635 0.1015 0.1171 0.0103  -0.0030 -0.0109 92  GLY A O   
545  N N   . PRO A 76  ? 0.0803 0.1183 0.1254 0.0013  0.0205  0.0122  93  PRO A N   
546  C CA  . PRO A 76  ? 0.0763 0.1172 0.1188 0.0009  0.0218  0.0081  93  PRO A CA  
547  C C   . PRO A 76  ? 0.0675 0.1211 0.1157 -0.0266 0.0258  -0.0098 93  PRO A C   
548  O O   . PRO A 76  ? 0.0768 0.1004 0.1173 -0.0040 0.0254  -0.0145 93  PRO A O   
549  C CB  . PRO A 76  ? 0.0615 0.0920 0.1188 0.0105  0.0023  -0.0024 93  PRO A CB  
550  C CG  . PRO A 76  ? 0.0873 0.0882 0.1195 0.0063  -0.0251 -0.0019 93  PRO A CG  
551  C CD  . PRO A 76  ? 0.1130 0.0895 0.1246 -0.0033 -0.0073 0.0188  93  PRO A CD  
552  N N   . VAL A 77  ? 0.0694 0.0842 0.1102 -0.0096 0.0149  -0.0209 94  VAL A N   
553  C CA  . VAL A 77  ? 0.0527 0.1065 0.1123 -0.0217 0.0117  -0.0023 94  VAL A CA  
554  C C   . VAL A 77  ? 0.0461 0.0929 0.1051 -0.0196 0.0261  -0.0020 94  VAL A C   
555  O O   . VAL A 77  ? 0.0831 0.1107 0.1118 0.0059  0.0226  -0.0201 94  VAL A O   
556  C CB  . VAL A 77  ? 0.0962 0.1205 0.1165 0.0182  0.0155  -0.0089 94  VAL A CB  
557  C CG1 . VAL A 77  ? 0.1105 0.1201 0.1095 0.0199  -0.0088 -0.0252 94  VAL A CG1 
558  C CG2 . VAL A 77  ? 0.0881 0.1230 0.1192 0.0041  0.0233  0.0149  94  VAL A CG2 
559  N N   . LEU A 78  ? 0.0420 0.1085 0.1041 0.0132  0.0087  -0.0008 95  LEU A N   
560  C CA  . LEU A 78  ? 0.0625 0.0637 0.0923 -0.0089 0.0078  -0.0090 95  LEU A CA  
561  C C   . LEU A 78  ? 0.0628 0.1012 0.0855 -0.0285 0.0237  -0.0064 95  LEU A C   
562  O O   . LEU A 78  ? 0.0905 0.1143 0.0868 0.0002  0.0107  0.0011  95  LEU A O   
563  C CB  . LEU A 78  ? 0.0888 0.0978 0.0895 0.0248  0.0081  -0.0081 95  LEU A CB  
564  C CG  . LEU A 78  ? 0.1108 0.1003 0.0866 -0.0258 -0.0013 0.0005  95  LEU A CG  
565  C CD1 . LEU A 78  ? 0.0999 0.1474 0.0929 -0.0117 0.0051  -0.0327 95  LEU A CD1 
566  C CD2 . LEU A 78  ? 0.1055 0.1439 0.0882 -0.0002 -0.0023 0.0101  95  LEU A CD2 
567  N N   . CYS A 79  ? 0.0603 0.1224 0.0867 0.0117  0.0118  -0.0033 96  CYS A N   
568  C CA  . CYS A 79  ? 0.0747 0.0815 0.0955 -0.0062 0.0206  -0.0049 96  CYS A CA  
569  C C   . CYS A 79  ? 0.0621 0.0802 0.0941 0.0314  0.0116  -0.0057 96  CYS A C   
570  O O   . CYS A 79  ? 0.1126 0.1013 0.0903 0.0267  -0.0120 -0.0225 96  CYS A O   
571  C CB  . CYS A 79  ? 0.0805 0.0861 0.1060 -0.0050 0.0027  -0.0178 96  CYS A CB  
572  S SG  . CYS A 79  ? 0.0898 0.1409 0.1310 0.0027  -0.0063 -0.0013 96  CYS A SG  
573  N N   . MET A 80  ? 0.0892 0.0802 0.0894 0.0302  0.0040  0.0236  97  MET A N   
574  C CA  . MET A 80  ? 0.0693 0.0704 0.0880 0.0024  -0.0011 -0.0068 97  MET A CA  
575  C C   . MET A 80  ? 0.0413 0.1132 0.0841 0.0225  -0.0140 -0.0053 97  MET A C   
576  O O   . MET A 80  ? 0.1126 0.1376 0.0797 -0.0047 -0.0170 0.0067  97  MET A O   
577  C CB  . MET A 80  ? 0.0974 0.0891 0.0921 0.0211  -0.0099 -0.0105 97  MET A CB  
578  C CG  . MET A 80  ? 0.1399 0.0761 0.1006 0.0196  -0.0249 -0.0071 97  MET A CG  
579  S SD  . MET A 80  ? 0.0979 0.1195 0.1079 0.0054  -0.0128 0.0132  97  MET A SD  
580  C CE  . MET A 80  ? 0.0872 0.1631 0.1098 0.0261  0.0125  0.0456  97  MET A CE  
581  N N   . VAL A 81  ? 0.0658 0.0941 0.0868 0.0238  -0.0055 -0.0099 98  VAL A N   
582  C CA  . VAL A 81  ? 0.1068 0.1033 0.0855 0.0200  -0.0064 -0.0015 98  VAL A CA  
583  C C   . VAL A 81  ? 0.0944 0.0890 0.0919 -0.0278 0.0120  -0.0004 98  VAL A C   
584  O O   . VAL A 81  ? 0.1319 0.0633 0.1026 0.0009  0.0036  -0.0211 98  VAL A O   
585  C CB  . VAL A 81  ? 0.0804 0.1057 0.0892 0.0024  -0.0056 0.0048  98  VAL A CB  
586  C CG1 . VAL A 81  ? 0.0997 0.1188 0.0912 0.0349  -0.0107 0.0078  98  VAL A CG1 
587  C CG2 . VAL A 81  ? 0.1156 0.1239 0.0921 0.0228  -0.0230 0.0044  98  VAL A CG2 
588  N N   . PHE A 82  ? 0.0962 0.1025 0.0867 0.0078  0.0185  -0.0039 99  PHE A N   
589  C CA  . PHE A 82  ? 0.0703 0.1104 0.0919 -0.0085 -0.0079 0.0098  99  PHE A CA  
590  C C   . PHE A 82  ? 0.0835 0.1055 0.0976 0.0185  -0.0165 0.0145  99  PHE A C   
591  O O   . PHE A 82  ? 0.0911 0.1214 0.0946 0.0182  -0.0140 0.0109  99  PHE A O   
592  C CB  . PHE A 82  ? 0.0768 0.0949 0.0927 0.0326  0.0098  0.0133  99  PHE A CB  
593  C CG  . PHE A 82  ? 0.1020 0.1104 0.0952 0.0076  0.0010  0.0085  99  PHE A CG  
594  C CD1 . PHE A 82  ? 0.0925 0.1212 0.1055 0.0222  0.0084  0.0008  99  PHE A CD1 
595  C CD2 . PHE A 82  ? 0.0945 0.1228 0.1048 -0.0334 -0.0198 0.0079  99  PHE A CD2 
596  C CE1 . PHE A 82  ? 0.1119 0.1391 0.1108 0.0282  0.0239  0.0276  99  PHE A CE1 
597  C CE2 . PHE A 82  ? 0.1319 0.1151 0.1124 0.0352  -0.0017 0.0238  99  PHE A CE2 
598  C CZ  . PHE A 82  ? 0.0951 0.1166 0.1136 0.0521  0.0109  0.0370  99  PHE A CZ  
599  N N   . GLU A 83  ? 0.0716 0.0884 0.0969 0.0055  -0.0053 0.0267  100 GLU A N   
600  C CA  . GLU A 83  ? 0.0719 0.0968 0.1000 0.0146  -0.0252 0.0307  100 GLU A CA  
601  C C   . GLU A 83  ? 0.0863 0.0843 0.0867 0.0159  -0.0240 0.0100  100 GLU A C   
602  O O   . GLU A 83  ? 0.0731 0.1221 0.0859 0.0240  -0.0170 0.0014  100 GLU A O   
603  C CB  . GLU A 83  ? 0.1101 0.1138 0.1256 -0.0050 -0.0289 0.0272  100 GLU A CB  
604  C CG  . GLU A 83  ? 0.1217 0.0697 0.1445 -0.0032 -0.0124 0.0305  100 GLU A CG  
605  C CD  . GLU A 83  ? 0.2349 0.1325 0.1605 0.0376  -0.0053 0.0202  100 GLU A CD  
606  O OE1 . GLU A 83  ? 0.2502 0.1901 0.1779 0.0526  -0.0200 0.0273  100 GLU A OE1 
607  O OE2 . GLU A 83  ? 0.2317 0.1345 0.1589 -0.0047 -0.0056 0.0006  100 GLU A OE2 
608  N N   . GLY A 84  ? 0.0989 0.1008 0.0806 0.0271  -0.0117 0.0025  101 GLY A N   
609  C CA  . GLY A 84  ? 0.0884 0.0987 0.0880 -0.0013 -0.0284 -0.0081 101 GLY A CA  
610  C C   . GLY A 84  ? 0.0884 0.1376 0.0904 -0.0328 -0.0071 0.0146  101 GLY A C   
611  O O   . GLY A 84  ? 0.0809 0.1479 0.0965 0.0128  -0.0180 0.0260  101 GLY A O   
612  N N   . VAL A 85  ? 0.0947 0.1234 0.0892 -0.0231 -0.0028 0.0303  102 VAL A N   
613  C CA  . VAL A 85  ? 0.1191 0.1309 0.0949 -0.0443 -0.0215 0.0230  102 VAL A CA  
614  C C   . VAL A 85  ? 0.1196 0.1557 0.0998 -0.0068 -0.0135 0.0191  102 VAL A C   
615  O O   . VAL A 85  ? 0.1315 0.1296 0.1081 0.0200  -0.0005 0.0272  102 VAL A O   
616  C CB  . VAL A 85  ? 0.0775 0.1967 0.0981 -0.0519 -0.0003 0.0091  102 VAL A CB  
617  C CG1 . VAL A 85  ? 0.1473 0.2456 0.0977 0.0116  0.0151  0.0190  102 VAL A CG1 
618  C CG2 . VAL A 85  ? 0.1394 0.1813 0.1087 -0.0756 0.0044  0.0116  102 VAL A CG2 
619  N N   . ASP A 86  ? 0.1347 0.1364 0.0948 -0.0134 0.0087  0.0134  103 ASP A N   
620  C CA  . ASP A 86  ? 0.1130 0.1063 0.1048 -0.0117 0.0010  0.0055  103 ASP A CA  
621  C C   . ASP A 86  ? 0.1259 0.1325 0.1023 0.0062  -0.0024 -0.0071 103 ASP A C   
622  O O   . ASP A 86  ? 0.0985 0.1212 0.1037 -0.0007 -0.0108 -0.0108 103 ASP A O   
623  C CB  . ASP A 86  ? 0.1146 0.1310 0.1145 0.0181  -0.0006 0.0081  103 ASP A CB  
624  C CG  . ASP A 86  ? 0.1042 0.1684 0.1287 0.0063  -0.0049 0.0116  103 ASP A CG  
625  O OD1 . ASP A 86  ? 0.0956 0.2003 0.1324 -0.0193 0.0034  -0.0238 103 ASP A OD1 
626  O OD2 . ASP A 86  ? 0.1553 0.1863 0.1340 0.0100  -0.0180 0.0215  103 ASP A OD2 
627  N N   . VAL A 87  ? 0.1065 0.0654 0.1024 0.0310  -0.0005 0.0001  104 VAL A N   
628  C CA  . VAL A 87  ? 0.0763 0.0734 0.1107 0.0230  0.0060  0.0195  104 VAL A CA  
629  C C   . VAL A 87  ? 0.0760 0.1055 0.1060 0.0220  0.0091  0.0168  104 VAL A C   
630  O O   . VAL A 87  ? 0.0900 0.0822 0.1110 0.0165  0.0015  0.0033  104 VAL A O   
631  C CB  . VAL A 87  ? 0.1240 0.0828 0.1143 0.0306  0.0331  0.0353  104 VAL A CB  
632  C CG1 . VAL A 87  ? 0.1252 0.0867 0.1183 0.0534  -0.0063 0.0116  104 VAL A CG1 
633  C CG2 . VAL A 87  ? 0.0589 0.1600 0.1130 0.0166  0.0145  0.0118  104 VAL A CG2 
634  N N   . ILE A 88  ? 0.0923 0.1115 0.1024 0.0085  -0.0097 0.0236  105 ILE A N   
635  C CA  . ILE A 88  ? 0.0774 0.1234 0.0998 0.0315  -0.0021 0.0144  105 ILE A CA  
636  C C   . ILE A 88  ? 0.0560 0.1229 0.0944 0.0100  0.0047  0.0006  105 ILE A C   
637  O O   . ILE A 88  ? 0.0939 0.1418 0.1022 -0.0107 0.0063  -0.0090 105 ILE A O   
638  C CB  . ILE A 88  ? 0.0784 0.1124 0.0970 -0.0202 0.0053  -0.0019 105 ILE A CB  
639  C CG1 . ILE A 88  ? 0.0711 0.1440 0.0959 -0.0045 0.0011  0.0050  105 ILE A CG1 
640  C CG2 . ILE A 88  ? 0.1312 0.1504 0.0902 0.0079  -0.0264 0.0129  105 ILE A CG2 
641  C CD1 . ILE A 88  ? 0.0889 0.1530 0.1003 0.0424  -0.0102 0.0093  105 ILE A CD1 
642  N N   . ALA A 89  ? 0.0809 0.1138 0.0859 0.0439  -0.0023 0.0007  106 ALA A N   
643  C CA  . ALA A 89  ? 0.1105 0.0974 0.0808 -0.0072 0.0002  0.0122  106 ALA A CA  
644  C C   . ALA A 89  ? 0.1185 0.0732 0.0848 -0.0090 -0.0069 0.0096  106 ALA A C   
645  O O   . ALA A 89  ? 0.1230 0.0818 0.0844 -0.0222 -0.0177 0.0079  106 ALA A O   
646  C CB  . ALA A 89  ? 0.1385 0.1404 0.0745 0.0103  -0.0136 0.0139  106 ALA A CB  
647  N N   . GLN A 90  ? 0.0992 0.0729 0.0953 -0.0022 -0.0022 -0.0087 107 GLN A N   
648  C CA  . GLN A 90  ? 0.1164 0.0826 0.0978 0.0392  -0.0086 -0.0031 107 GLN A CA  
649  C C   . GLN A 90  ? 0.0803 0.1269 0.0981 0.0052  -0.0097 0.0035  107 GLN A C   
650  O O   . GLN A 90  ? 0.0792 0.0729 0.1024 -0.0064 0.0018  0.0124  107 GLN A O   
651  C CB  . GLN A 90  ? 0.1313 0.0994 0.0999 0.0222  -0.0120 -0.0127 107 GLN A CB  
652  C CG  . GLN A 90  ? 0.0525 0.1152 0.1116 0.0054  -0.0007 0.0044  107 GLN A CG  
653  C CD  . GLN A 90  ? 0.0960 0.1079 0.1065 -0.0201 0.0068  0.0146  107 GLN A CD  
654  O OE1 . GLN A 90  ? 0.0819 0.1365 0.1050 0.0054  -0.0063 -0.0218 107 GLN A OE1 
655  N NE2 . GLN A 90  ? 0.1228 0.1391 0.1010 0.0122  -0.0129 0.0049  107 GLN A NE2 
656  N N   . ALA A 91  ? 0.1221 0.0580 0.1021 -0.0076 -0.0139 0.0039  108 ALA A N   
657  C CA  . ALA A 91  ? 0.0840 0.0317 0.0983 -0.0115 -0.0012 0.0136  108 ALA A CA  
658  C C   . ALA A 91  ? 0.0808 0.0832 0.1101 0.0058  -0.0169 -0.0081 108 ALA A C   
659  O O   . ALA A 91  ? 0.1009 0.0960 0.1137 0.0157  0.0097  0.0110  108 ALA A O   
660  C CB  . ALA A 91  ? 0.0905 0.0903 0.1024 0.0096  -0.0079 0.0204  108 ALA A CB  
661  N N   . ARG A 92  ? 0.0918 0.0770 0.1039 -0.0216 -0.0391 -0.0138 109 ARG A N   
662  C CA  . ARG A 92  ? 0.0870 0.1073 0.1095 -0.0180 -0.0293 -0.0083 109 ARG A CA  
663  C C   . ARG A 92  ? 0.1192 0.0718 0.1025 0.0123  -0.0012 0.0077  109 ARG A C   
664  O O   . ARG A 92  ? 0.1112 0.1124 0.1001 -0.0034 -0.0082 0.0052  109 ARG A O   
665  C CB  . ARG A 92  ? 0.0984 0.0935 0.1215 -0.0087 -0.0289 -0.0258 109 ARG A CB  
666  C CG  . ARG A 92  ? 0.1116 0.1661 0.1321 0.0312  -0.0219 -0.0151 109 ARG A CG  
667  C CD  . ARG A 92  ? 0.1052 0.1379 0.1376 0.0078  -0.0085 -0.0511 109 ARG A CD  
668  N NE  . ARG A 92  ? 0.1021 0.1450 0.1473 -0.0004 0.0030  -0.0345 109 ARG A NE  
669  C CZ  . ARG A 92  ? 0.1477 0.1480 0.1524 -0.0327 0.0047  -0.0427 109 ARG A CZ  
670  N NH1 . ARG A 92  ? 0.1356 0.2299 0.1621 -0.0353 0.0232  -0.0340 109 ARG A NH1 
671  N NH2 . ARG A 92  ? 0.2070 0.1533 0.1557 -0.0294 0.0036  -0.0453 109 ARG A NH2 
672  N N   . LYS A 93  ? 0.1107 0.1303 0.1019 -0.0072 0.0016  0.0122  110 LYS A N   
673  C CA  . LYS A 93  ? 0.0858 0.1216 0.1025 0.0073  -0.0031 0.0142  110 LYS A CA  
674  C C   . LYS A 93  ? 0.1156 0.1058 0.0938 0.0149  0.0127  0.0089  110 LYS A C   
675  O O   . LYS A 93  ? 0.0970 0.1107 0.0867 0.0174  0.0125  0.0100  110 LYS A O   
676  C CB  . LYS A 93  ? 0.0990 0.1550 0.1100 0.0242  0.0254  -0.0048 110 LYS A CB  
677  C CG  . LYS A 93  ? 0.0695 0.1545 0.1207 -0.0076 0.0083  -0.0155 110 LYS A CG  
678  C CD  . LYS A 93  ? 0.0932 0.2208 0.1260 -0.0449 0.0307  -0.0179 110 LYS A CD  
679  C CE  . LYS A 93  ? 0.1186 0.2318 0.1343 -0.0564 0.0468  0.0034  110 LYS A CE  
680  N NZ  . LYS A 93  ? 0.1164 0.2070 0.1313 -0.0439 0.0564  0.0003  110 LYS A NZ  
681  N N   . MET A 94  ? 0.1014 0.0804 0.0908 -0.0099 0.0233  0.0028  111 MET A N   
682  C CA  . MET A 94  ? 0.1164 0.1047 0.0907 0.0176  0.0061  0.0111  111 MET A CA  
683  C C   . MET A 94  ? 0.0495 0.1236 0.0966 -0.0056 0.0078  0.0219  111 MET A C   
684  O O   . MET A 94  ? 0.0877 0.1141 0.1072 0.0042  -0.0037 0.0230  111 MET A O   
685  C CB  . MET A 94  ? 0.0754 0.1164 0.0957 -0.0001 -0.0034 0.0091  111 MET A CB  
686  C CG  . MET A 94  ? 0.0556 0.0988 0.1013 -0.0274 -0.0101 0.0020  111 MET A CG  
687  S SD  . MET A 94  ? 0.1057 0.1213 0.1021 -0.0025 0.0053  -0.0215 111 MET A SD  
688  C CE  . MET A 94  ? 0.1533 0.2007 0.0996 -0.0075 -0.0094 -0.0372 111 MET A CE  
689  N N   . MET A 95  ? 0.0863 0.0883 0.0948 0.0154  0.0006  -0.0103 112 MET A N   
690  C CA  . MET A 95  ? 0.0743 0.0668 0.1055 0.0249  -0.0075 -0.0069 112 MET A CA  
691  C C   . MET A 95  ? 0.0475 0.0839 0.1033 -0.0139 -0.0038 0.0185  112 MET A C   
692  O O   . MET A 95  ? 0.1094 0.0984 0.0976 -0.0042 -0.0138 0.0254  112 MET A O   
693  C CB  . MET A 95  ? 0.0685 0.1127 0.1248 0.0146  0.0091  -0.0019 112 MET A CB  
694  C CG  . MET A 95  ? 0.0744 0.0869 0.1490 0.0113  0.0042  -0.0191 112 MET A CG  
695  S SD  . MET A 95  ? 0.1058 0.1346 0.1709 0.0167  -0.0057 -0.0269 112 MET A SD  
696  C CE  . MET A 95  ? 0.0940 0.0958 0.1624 -0.0130 0.0144  -0.0112 112 MET A CE  
697  N N   . GLY A 96  ? 0.0885 0.1140 0.1022 -0.0163 0.0118  0.0120  113 GLY A N   
698  C CA  . GLY A 96  ? 0.0792 0.0856 0.0982 0.0126  -0.0040 0.0094  113 GLY A CA  
699  C C   . GLY A 96  ? 0.0811 0.0645 0.1022 0.0264  -0.0012 -0.0051 113 GLY A C   
700  O O   . GLY A 96  ? 0.1102 0.0934 0.1021 0.0224  -0.0012 -0.0122 113 GLY A O   
701  N N   . SER A 97  ? 0.1093 0.0729 0.1061 0.0195  0.0030  -0.0086 114 SER A N   
702  C CA  . SER A 97  ? 0.1229 0.1037 0.1123 0.0172  -0.0180 -0.0278 114 SER A CA  
703  C C   . SER A 97  ? 0.1123 0.0994 0.1209 -0.0165 -0.0179 -0.0053 114 SER A C   
704  O O   . SER A 97  ? 0.0929 0.1327 0.1071 0.0114  -0.0085 -0.0196 114 SER A O   
705  C CB  . SER A 97  ? 0.1801 0.1734 0.1128 -0.0178 0.0066  -0.0271 114 SER A CB  
706  O OG  . SER A 97  ? 0.2801 0.2797 0.1250 0.0499  -0.0135 -0.0197 114 SER A OG  
707  N N   . THR A 98  ? 0.1099 0.1348 0.1361 0.0012  -0.0220 0.0054  115 THR A N   
708  C CA  A THR A 98  ? 0.1389 0.1222 0.1422 -0.0045 -0.0027 0.0195  115 THR A CA  
709  C CA  B THR A 98  ? 0.1112 0.1045 0.1436 -0.0180 -0.0134 0.0275  115 THR A CA  
710  C C   . THR A 98  ? 0.0959 0.0792 0.1344 -0.0130 -0.0029 0.0215  115 THR A C   
711  O O   . THR A 98  ? 0.0880 0.0943 0.1276 -0.0038 -0.0159 -0.0002 115 THR A O   
712  C CB  A THR A 98  ? 0.1286 0.1904 0.1552 0.0382  0.0268  0.0456  115 THR A CB  
713  C CB  B THR A 98  ? 0.0776 0.1596 0.1609 0.0053  -0.0100 0.0612  115 THR A CB  
714  O OG1 A THR A 98  ? 0.1944 0.2764 0.1710 0.0647  0.0302  0.0536  115 THR A OG1 
715  O OG1 B THR A 98  ? 0.0719 0.1622 0.1598 0.0023  -0.0195 0.0762  115 THR A OG1 
716  C CG2 A THR A 98  ? 0.1012 0.2742 0.1485 0.0309  0.0216  0.0400  115 THR A CG2 
717  C CG2 B THR A 98  ? 0.0654 0.2118 0.1651 -0.0104 -0.0063 0.0589  115 THR A CG2 
718  N N   . ARG A 99  ? 0.0947 0.1110 0.1229 0.0102  -0.0201 -0.0027 116 ARG A N   
719  C CA  . ARG A 99  ? 0.1607 0.1209 0.1227 0.0237  -0.0082 -0.0137 116 ARG A CA  
720  C C   . ARG A 99  ? 0.1206 0.0834 0.1039 -0.0029 -0.0103 -0.0098 116 ARG A C   
721  O O   . ARG A 99  ? 0.0768 0.1475 0.0913 -0.0012 -0.0045 0.0277  116 ARG A O   
722  C CB  . ARG A 99  ? 0.1089 0.1445 0.1371 0.0436  0.0003  -0.0106 116 ARG A CB  
723  C CG  . ARG A 99  ? 0.0974 0.1699 0.1489 0.0034  0.0066  -0.0177 116 ARG A CG  
724  C CD  . ARG A 99  ? 0.1157 0.3022 0.1639 -0.0414 0.0085  -0.0346 116 ARG A CD  
725  N NE  . ARG A 99  ? 0.2098 0.4281 0.1767 -0.0787 0.0238  -0.0366 116 ARG A NE  
726  C CZ  . ARG A 99  ? 0.2709 0.5524 0.1863 -0.1528 0.0052  0.0181  116 ARG A CZ  
727  N NH1 . ARG A 99  ? 0.2630 0.6084 0.1930 -0.1675 -0.0240 0.0130  116 ARG A NH1 
728  N NH2 . ARG A 99  ? 0.2984 0.5465 0.1936 -0.2124 -0.0040 0.0307  116 ARG A NH2 
729  N N   . PRO A 100 ? 0.0934 0.1016 0.0932 0.0168  -0.0082 0.0008  117 PRO A N   
730  C CA  . PRO A 100 ? 0.0893 0.1078 0.0861 0.0052  -0.0025 0.0218  117 PRO A CA  
731  C C   . PRO A 100 ? 0.0879 0.0863 0.0862 0.0178  -0.0091 0.0134  117 PRO A C   
732  O O   . PRO A 100 ? 0.0738 0.1211 0.0944 0.0185  -0.0280 0.0005  117 PRO A O   
733  C CB  . PRO A 100 ? 0.0851 0.1062 0.0836 -0.0003 -0.0176 0.0128  117 PRO A CB  
734  C CG  . PRO A 100 ? 0.0750 0.1103 0.0883 -0.0042 -0.0198 0.0038  117 PRO A CG  
735  C CD  . PRO A 100 ? 0.1050 0.1236 0.0898 -0.0088 -0.0138 -0.0086 117 PRO A CD  
736  N N   . GLY A 101 ? 0.1252 0.0852 0.0857 0.0152  -0.0206 -0.0011 118 GLY A N   
737  C CA  . GLY A 101 ? 0.1277 0.0815 0.0858 0.0038  0.0094  0.0028  118 GLY A CA  
738  C C   . GLY A 101 ? 0.0944 0.1235 0.0820 0.0367  0.0012  -0.0024 118 GLY A C   
739  O O   . GLY A 101 ? 0.1093 0.1467 0.0900 0.0231  -0.0020 0.0125  118 GLY A O   
740  N N   . GLU A 102 ? 0.0872 0.0893 0.0861 0.0232  -0.0125 -0.0031 119 GLU A N   
741  C CA  . GLU A 102 ? 0.0793 0.1094 0.0890 -0.0313 -0.0090 0.0054  119 GLU A CA  
742  C C   . GLU A 102 ? 0.1277 0.0985 0.0842 0.0185  0.0001  0.0143  119 GLU A C   
743  O O   . GLU A 102 ? 0.1320 0.1519 0.0803 -0.0302 0.0112  -0.0113 119 GLU A O   
744  C CB  . GLU A 102 ? 0.1473 0.1067 0.0913 0.0358  -0.0128 -0.0039 119 GLU A CB  
745  C CG  . GLU A 102 ? 0.1204 0.1706 0.1034 -0.0192 -0.0197 -0.0248 119 GLU A CG  
746  C CD  . GLU A 102 ? 0.1836 0.2307 0.1184 0.0354  -0.0137 -0.0287 119 GLU A CD  
747  O OE1 . GLU A 102 ? 0.1215 0.2703 0.1315 -0.0338 -0.0341 0.0446  119 GLU A OE1 
748  O OE2 . GLU A 102 ? 0.1883 0.3269 0.1190 0.0187  0.0164  -0.0555 119 GLU A OE2 
749  N N   . ALA A 103 ? 0.0908 0.1158 0.0845 0.0070  -0.0082 0.0117  120 ALA A N   
750  C CA  . ALA A 103 ? 0.0740 0.0907 0.0921 -0.0119 -0.0129 -0.0041 120 ALA A CA  
751  C C   . ALA A 103 ? 0.0929 0.0946 0.1070 -0.0549 0.0005  0.0037  120 ALA A C   
752  O O   . ALA A 103 ? 0.1392 0.1071 0.1040 -0.0077 -0.0155 -0.0063 120 ALA A O   
753  C CB  . ALA A 103 ? 0.1009 0.1504 0.0916 0.0507  -0.0024 -0.0062 120 ALA A CB  
754  N N   . ALA A 104 ? 0.0862 0.1173 0.1293 -0.0213 0.0070  -0.0132 121 ALA A N   
755  C CA  . ALA A 104 ? 0.0939 0.1374 0.1569 -0.0299 0.0198  -0.0059 121 ALA A CA  
756  C C   . ALA A 104 ? 0.0573 0.1426 0.1809 0.0002  0.0088  -0.0176 121 ALA A C   
757  O O   . ALA A 104 ? 0.0589 0.1194 0.1788 0.0190  0.0127  0.0011  121 ALA A O   
758  C CB  . ALA A 104 ? 0.1586 0.1192 0.1620 -0.0447 0.0279  0.0132  121 ALA A CB  
759  N N   . PRO A 105 ? 0.0890 0.1579 0.2034 0.0226  -0.0130 -0.0668 122 PRO A N   
760  C CA  . PRO A 105 ? 0.0884 0.1265 0.1973 0.0407  -0.0242 -0.0565 122 PRO A CA  
761  C C   . PRO A 105 ? 0.1185 0.1069 0.1728 0.0239  -0.0053 -0.0517 122 PRO A C   
762  O O   . PRO A 105 ? 0.1445 0.1687 0.1709 -0.0221 0.0172  -0.0273 122 PRO A O   
763  C CB  . PRO A 105 ? 0.1386 0.2748 0.2119 0.0867  -0.0385 -0.0927 122 PRO A CB  
764  C CG  . PRO A 105 ? 0.1875 0.3237 0.2232 0.0851  -0.0515 -0.1126 122 PRO A CG  
765  C CD  . PRO A 105 ? 0.2051 0.2937 0.2153 0.1018  -0.0452 -0.1111 122 PRO A CD  
766  N N   . GLY A 106 ? 0.1196 0.1199 0.1539 0.0314  -0.0035 -0.0129 123 GLY A N   
767  C CA  . GLY A 106 ? 0.1088 0.1542 0.1355 0.0421  -0.0281 -0.0110 123 GLY A CA  
768  C C   . GLY A 106 ? 0.0935 0.1177 0.1271 0.0153  -0.0297 -0.0138 123 GLY A C   
769  O O   . GLY A 106 ? 0.1269 0.1368 0.1404 0.0194  -0.0264 -0.0318 123 GLY A O   
770  N N   . THR A 107 ? 0.0648 0.1082 0.1129 -0.0272 -0.0162 -0.0033 124 THR A N   
771  C CA  . THR A 107 ? 0.0655 0.0911 0.1033 -0.0037 0.0051  -0.0019 124 THR A CA  
772  C C   . THR A 107 ? 0.0991 0.0698 0.0998 -0.0132 0.0127  -0.0108 124 THR A C   
773  O O   . THR A 107 ? 0.1059 0.1000 0.0938 0.0230  0.0119  0.0227  124 THR A O   
774  C CB  . THR A 107 ? 0.0536 0.1339 0.0961 0.0152  -0.0072 -0.0055 124 THR A CB  
775  O OG1 . THR A 107 ? 0.0798 0.1352 0.0961 -0.0066 -0.0111 -0.0075 124 THR A OG1 
776  C CG2 . THR A 107 ? 0.1068 0.0615 0.0962 0.0020  -0.0020 0.0015  124 THR A CG2 
777  N N   . ILE A 108 ? 0.0973 0.0603 0.0928 0.0011  -0.0019 -0.0043 125 ILE A N   
778  C CA  . ILE A 108 ? 0.0702 0.1077 0.0850 -0.0097 0.0028  0.0207  125 ILE A CA  
779  C C   . ILE A 108 ? 0.0917 0.1003 0.0852 0.0243  0.0102  0.0303  125 ILE A C   
780  O O   . ILE A 108 ? 0.1221 0.1051 0.0809 0.0041  0.0079  0.0241  125 ILE A O   
781  C CB  . ILE A 108 ? 0.0955 0.1312 0.0943 0.0023  0.0048  0.0218  125 ILE A CB  
782  C CG1 . ILE A 108 ? 0.0751 0.1851 0.1062 0.0050  -0.0196 0.0001  125 ILE A CG1 
783  C CG2 . ILE A 108 ? 0.0683 0.1216 0.0955 0.0347  0.0159  0.0190  125 ILE A CG2 
784  C CD1 . ILE A 108 ? 0.1223 0.1780 0.1122 -0.0059 -0.0278 -0.0097 125 ILE A CD1 
785  N N   . ARG A 109 ? 0.1110 0.0868 0.0975 0.0213  -0.0093 0.0055  126 ARG A N   
786  C CA  . ARG A 109 ? 0.1191 0.0908 0.1031 -0.0061 0.0030  -0.0013 126 ARG A CA  
787  C C   . ARG A 109 ? 0.0966 0.0808 0.0912 -0.0054 0.0162  -0.0026 126 ARG A C   
788  O O   . ARG A 109 ? 0.1012 0.0710 0.0839 -0.0022 -0.0088 0.0057  126 ARG A O   
789  C CB  . ARG A 109 ? 0.0785 0.0976 0.1260 -0.0354 0.0176  0.0159  126 ARG A CB  
790  C CG  . ARG A 109 ? 0.1205 0.2548 0.1569 0.0355  0.0295  0.0730  126 ARG A CG  
791  C CD  . ARG A 109 ? 0.1547 0.2662 0.1711 0.0272  0.0551  0.0504  126 ARG A CD  
792  N NE  . ARG A 109 ? 0.1057 0.1677 0.1619 0.0246  0.0093  -0.0131 126 ARG A NE  
793  C CZ  . ARG A 109 ? 0.0993 0.1448 0.1433 -0.0217 0.0244  -0.0277 126 ARG A CZ  
794  N NH1 . ARG A 109 ? 0.1289 0.1509 0.1366 0.0068  0.0419  -0.0287 126 ARG A NH1 
795  N NH2 . ARG A 109 ? 0.0976 0.1190 0.1342 0.0215  0.0047  -0.0236 126 ARG A NH2 
796  N N   . ALA A 110 ? 0.0726 0.1046 0.0843 -0.0117 -0.0033 -0.0001 127 ALA A N   
797  C CA  . ALA A 110 ? 0.1207 0.0888 0.0947 0.0340  0.0108  0.0090  127 ALA A CA  
798  C C   . ALA A 110 ? 0.0860 0.0620 0.1017 -0.0017 -0.0039 0.0032  127 ALA A C   
799  O O   . ALA A 110 ? 0.1436 0.0709 0.1090 0.0225  -0.0147 -0.0005 127 ALA A O   
800  C CB  . ALA A 110 ? 0.0529 0.0962 0.0982 0.0350  0.0132  0.0101  127 ALA A CB  
801  N N   . ASP A 111 ? 0.1080 0.0724 0.0994 0.0292  -0.0216 0.0077  128 ASP A N   
802  C CA  . ASP A 111 ? 0.1120 0.0886 0.1092 0.0168  -0.0084 0.0248  128 ASP A CA  
803  C C   . ASP A 111 ? 0.0699 0.0824 0.1026 -0.0074 -0.0018 0.0071  128 ASP A C   
804  O O   . ASP A 111 ? 0.0737 0.1092 0.1133 0.0098  -0.0101 0.0169  128 ASP A O   
805  C CB  . ASP A 111 ? 0.1167 0.1184 0.1333 0.0212  -0.0153 0.0250  128 ASP A CB  
806  C CG  . ASP A 111 ? 0.1593 0.1973 0.1716 -0.0360 0.0004  -0.0129 128 ASP A CG  
807  O OD1 . ASP A 111 ? 0.1808 0.2419 0.1925 -0.0607 0.0374  -0.0178 128 ASP A OD1 
808  O OD2 . ASP A 111 ? 0.1219 0.2140 0.1851 -0.0430 -0.0058 -0.0064 128 ASP A OD2 
809  N N   . PHE A 112 ? 0.0621 0.1030 0.0943 0.0059  -0.0131 0.0101  129 PHE A N   
810  C CA  . PHE A 112 ? 0.0637 0.0546 0.0968 -0.0179 -0.0127 -0.0128 129 PHE A CA  
811  C C   . PHE A 112 ? 0.0898 0.0492 0.0878 0.0172  -0.0089 -0.0176 129 PHE A C   
812  O O   . PHE A 112 ? 0.0755 0.1321 0.0870 0.0108  -0.0102 0.0206  129 PHE A O   
813  C CB  . PHE A 112 ? 0.0919 0.0681 0.1008 -0.0004 -0.0029 -0.0167 129 PHE A CB  
814  C CG  . PHE A 112 ? 0.1120 0.0747 0.1040 -0.0068 0.0156  0.0022  129 PHE A CG  
815  C CD1 . PHE A 112 ? 0.0877 0.1062 0.1054 -0.0171 0.0094  -0.0108 129 PHE A CD1 
816  C CD2 . PHE A 112 ? 0.1076 0.0852 0.1124 0.0082  -0.0104 0.0069  129 PHE A CD2 
817  C CE1 . PHE A 112 ? 0.1025 0.1798 0.1133 0.0000  -0.0161 -0.0086 129 PHE A CE1 
818  C CE2 . PHE A 112 ? 0.1478 0.0855 0.1149 -0.0480 -0.0192 0.0223  129 PHE A CE2 
819  C CZ  . PHE A 112 ? 0.1554 0.0987 0.1150 -0.0021 -0.0230 -0.0036 129 PHE A CZ  
820  N N   . CYS A 113 ? 0.0685 0.0784 0.0825 -0.0084 -0.0147 -0.0210 130 CYS A N   
821  C CA  . CYS A 113 ? 0.0654 0.0768 0.0832 -0.0030 -0.0090 -0.0056 130 CYS A CA  
822  C C   . CYS A 113 ? 0.0570 0.0975 0.0890 -0.0366 -0.0113 0.0042  130 CYS A C   
823  O O   . CYS A 113 ? 0.0845 0.1009 0.0918 -0.0005 0.0014  0.0063  130 CYS A O   
824  C CB  . CYS A 113 ? 0.1087 0.0981 0.0878 -0.0096 -0.0173 -0.0114 130 CYS A CB  
825  S SG  . CYS A 113 ? 0.1192 0.1002 0.1000 0.0170  -0.0177 -0.0190 130 CYS A SG  
826  N N   . GLN A 114 ? 0.0786 0.0692 0.0943 -0.0063 -0.0045 0.0002  131 GLN A N   
827  C CA  . GLN A 114 ? 0.1333 0.0673 0.0963 0.0016  -0.0111 -0.0117 131 GLN A CA  
828  C C   . GLN A 114 ? 0.0901 0.0855 0.1048 0.0353  -0.0110 -0.0137 131 GLN A C   
829  O O   . GLN A 114 ? 0.0742 0.1250 0.1073 0.0457  -0.0114 -0.0186 131 GLN A O   
830  C CB  . GLN A 114 ? 0.1097 0.0965 0.0988 0.0142  -0.0175 -0.0169 131 GLN A CB  
831  C CG  . GLN A 114 ? 0.1463 0.0977 0.0935 -0.0040 -0.0086 -0.0019 131 GLN A CG  
832  C CD  . GLN A 114 ? 0.1070 0.0904 0.0968 0.0033  -0.0157 0.0115  131 GLN A CD  
833  O OE1 . GLN A 114 ? 0.1496 0.1142 0.1064 0.0161  0.0036  0.0102  131 GLN A OE1 
834  N NE2 . GLN A 114 ? 0.1085 0.0891 0.0962 0.0103  -0.0247 0.0151  131 GLN A NE2 
835  N N   . GLN A 115 ? 0.0789 0.0789 0.1094 -0.0023 0.0019  -0.0113 132 GLN A N   
836  C CA  . GLN A 115 ? 0.0867 0.1043 0.1192 -0.0211 -0.0167 0.0130  132 GLN A CA  
837  C C   . GLN A 115 ? 0.1095 0.0926 0.1079 -0.0194 -0.0022 -0.0002 132 GLN A C   
838  O O   . GLN A 115 ? 0.1585 0.1075 0.1039 0.0426  -0.0091 0.0024  132 GLN A O   
839  C CB  . GLN A 115 ? 0.1310 0.1101 0.1463 0.0046  -0.0387 0.0090  132 GLN A CB  
840  C CG  . GLN A 115 ? 0.1412 0.1510 0.1681 -0.0102 -0.0566 -0.0105 132 GLN A CG  
841  C CD  . GLN A 115 ? 0.1419 0.1264 0.1777 0.0041  -0.0443 -0.0120 132 GLN A CD  
842  O OE1 . GLN A 115 ? 0.1701 0.1611 0.1886 0.0024  -0.0249 0.0004  132 GLN A OE1 
843  N NE2 . GLN A 115 ? 0.2119 0.2930 0.1807 0.0012  -0.0336 -0.0308 132 GLN A NE2 
844  N N   . ALA A 116 ? 0.1055 0.1151 0.1092 -0.0044 -0.0109 -0.0010 133 ALA A N   
845  C CA  . ALA A 116 ? 0.1114 0.1257 0.1137 0.0226  -0.0253 -0.0229 133 ALA A CA  
846  C C   . ALA A 116 ? 0.1151 0.0596 0.1211 -0.0150 -0.0167 -0.0057 133 ALA A C   
847  O O   . ALA A 116 ? 0.1258 0.1152 0.1314 0.0217  -0.0025 -0.0147 133 ALA A O   
848  C CB  . ALA A 116 ? 0.1208 0.1457 0.1102 -0.0216 -0.0163 -0.0040 133 ALA A CB  
849  N N   . GLY A 117 ? 0.0932 0.1167 0.1225 0.0010  -0.0300 0.0005  134 GLY A N   
850  C CA  . GLY A 117 ? 0.1242 0.1526 0.1196 -0.0188 -0.0257 -0.0145 134 GLY A CA  
851  C C   . GLY A 117 ? 0.0898 0.1144 0.1256 -0.0225 -0.0070 -0.0168 134 GLY A C   
852  O O   . GLY A 117 ? 0.1128 0.1537 0.1353 0.0118  0.0013  0.0095  134 GLY A O   
853  N N   . ARG A 118 ? 0.0769 0.1041 0.1183 -0.0374 0.0054  -0.0129 135 ARG A N   
854  C CA  . ARG A 118 ? 0.0918 0.0786 0.1139 0.0063  -0.0042 0.0008  135 ARG A CA  
855  C C   . ARG A 118 ? 0.0744 0.0740 0.1013 -0.0080 -0.0191 0.0030  135 ARG A C   
856  O O   . ARG A 118 ? 0.1385 0.1005 0.1068 0.0177  -0.0174 0.0158  135 ARG A O   
857  C CB  . ARG A 118 ? 0.0946 0.0783 0.1296 -0.0008 -0.0031 -0.0221 135 ARG A CB  
858  C CG  . ARG A 118 ? 0.0883 0.1359 0.1399 -0.0236 0.0277  0.0063  135 ARG A CG  
859  C CD  . ARG A 118 ? 0.1134 0.1856 0.1463 -0.0009 0.0313  -0.0040 135 ARG A CD  
860  N NE  . ARG A 118 ? 0.1076 0.1255 0.1630 -0.0124 0.0184  -0.0323 135 ARG A NE  
861  C CZ  . ARG A 118 ? 0.1548 0.1882 0.1755 0.0074  0.0074  -0.0246 135 ARG A CZ  
862  N NH1 . ARG A 118 ? 0.1153 0.2300 0.1865 -0.0010 0.0144  -0.0407 135 ARG A NH1 
863  N NH2 . ARG A 118 ? 0.1360 0.2660 0.1716 -0.0601 0.0252  -0.0067 135 ARG A NH2 
864  N N   . ASN A 119 ? 0.0852 0.0916 0.0984 0.0131  -0.0195 -0.0046 136 ASN A N   
865  C CA  . ASN A 119 ? 0.0760 0.1090 0.0953 -0.0198 -0.0327 -0.0128 136 ASN A CA  
866  C C   . ASN A 119 ? 0.0445 0.0840 0.0966 -0.0142 -0.0011 -0.0065 136 ASN A C   
867  O O   . ASN A 119 ? 0.0485 0.0684 0.1012 0.0015  0.0040  -0.0060 136 ASN A O   
868  C CB  . ASN A 119 ? 0.1458 0.0823 0.0931 0.0015  -0.0116 -0.0238 136 ASN A CB  
869  C CG  . ASN A 119 ? 0.1221 0.0872 0.0926 -0.0045 -0.0033 -0.0075 136 ASN A CG  
870  O OD1 . ASN A 119 ? 0.1607 0.1300 0.0957 0.0375  -0.0185 -0.0209 136 ASN A OD1 
871  N ND2 . ASN A 119 ? 0.1243 0.1021 0.1061 0.0382  0.0044  0.0098  136 ASN A ND2 
872  N N   . LEU A 120 ? 0.0741 0.1218 0.0981 0.0105  0.0067  -0.0143 137 LEU A N   
873  C CA  . LEU A 120 ? 0.0877 0.1007 0.0968 0.0027  -0.0018 -0.0008 137 LEU A CA  
874  C C   . LEU A 120 ? 0.0868 0.0842 0.0909 0.0226  -0.0035 0.0132  137 LEU A C   
875  O O   . LEU A 120 ? 0.0750 0.1229 0.1005 0.0048  0.0142  -0.0050 137 LEU A O   
876  C CB  . LEU A 120 ? 0.1174 0.1076 0.1046 0.0283  0.0097  -0.0100 137 LEU A CB  
877  C CG  . LEU A 120 ? 0.0849 0.1134 0.1123 -0.0251 0.0039  -0.0080 137 LEU A CG  
878  C CD1 . LEU A 120 ? 0.1293 0.0860 0.1135 0.0383  -0.0002 -0.0204 137 LEU A CD1 
879  C CD2 . LEU A 120 ? 0.0971 0.1513 0.1119 -0.0147 0.0054  0.0102  137 LEU A CD2 
880  N N   . ILE A 121 ? 0.0936 0.0650 0.0824 -0.0110 -0.0169 0.0046  138 ILE A N   
881  C CA  . ILE A 121 ? 0.0989 0.0764 0.0831 -0.0200 -0.0055 0.0080  138 ILE A CA  
882  C C   . ILE A 121 ? 0.1113 0.0708 0.0879 0.0334  -0.0062 -0.0029 138 ILE A C   
883  O O   . ILE A 121 ? 0.1270 0.0823 0.0955 0.0237  -0.0076 -0.0230 138 ILE A O   
884  C CB  . ILE A 121 ? 0.1159 0.0829 0.0928 0.0053  -0.0131 -0.0044 138 ILE A CB  
885  C CG1 . ILE A 121 ? 0.0979 0.1196 0.1036 0.0283  -0.0210 0.0299  138 ILE A CG1 
886  C CG2 . ILE A 121 ? 0.0960 0.1063 0.0996 -0.0451 -0.0011 0.0398  138 ILE A CG2 
887  C CD1 . ILE A 121 ? 0.1785 0.1045 0.1127 -0.0022 -0.0292 0.0256  138 ILE A CD1 
888  N N   . HIS A 122 ? 0.0784 0.1129 0.0869 0.0172  0.0035  0.0143  139 HIS A N   
889  C CA  . HIS A 122 ? 0.0536 0.1426 0.0967 0.0179  -0.0128 0.0154  139 HIS A CA  
890  C C   . HIS A 122 ? 0.0410 0.1122 0.0961 -0.0218 -0.0122 0.0165  139 HIS A C   
891  O O   . HIS A 122 ? 0.0801 0.0867 0.0872 0.0110  -0.0180 0.0110  139 HIS A O   
892  C CB  . HIS A 122 ? 0.0880 0.1000 0.1163 -0.0038 -0.0261 0.0121  139 HIS A CB  
893  C CG  . HIS A 122 ? 0.0502 0.1151 0.1304 0.0105  -0.0284 0.0124  139 HIS A CG  
894  N ND1 . HIS A 122 ? 0.1021 0.1626 0.1397 0.0438  -0.0518 0.0012  139 HIS A ND1 
895  C CD2 . HIS A 122 ? 0.0907 0.1499 0.1356 0.0565  -0.0187 0.0184  139 HIS A CD2 
896  C CE1 . HIS A 122 ? 0.0875 0.1344 0.1449 0.0581  -0.0187 0.0011  139 HIS A CE1 
897  N NE2 . HIS A 122 ? 0.0722 0.1331 0.1452 0.0385  -0.0081 0.0291  139 HIS A NE2 
898  N N   . GLY A 123 ? 0.0846 0.0796 0.1057 0.0147  -0.0009 0.0147  140 GLY A N   
899  C CA  . GLY A 123 ? 0.0928 0.1182 0.1030 0.0435  0.0059  0.0465  140 GLY A CA  
900  C C   . GLY A 123 ? 0.0963 0.0819 0.1040 -0.0100 -0.0047 0.0294  140 GLY A C   
901  O O   . GLY A 123 ? 0.1501 0.1090 0.1096 -0.0371 -0.0111 -0.0058 140 GLY A O   
902  N N   . SER A 124 ? 0.0871 0.1133 0.1021 0.0184  -0.0171 0.0207  141 SER A N   
903  C CA  . SER A 124 ? 0.0879 0.1111 0.1006 0.0023  -0.0373 0.0308  141 SER A CA  
904  C C   . SER A 124 ? 0.1010 0.1327 0.1093 -0.0088 -0.0290 0.0135  141 SER A C   
905  O O   . SER A 124 ? 0.1095 0.0968 0.1119 -0.0080 -0.0024 0.0112  141 SER A O   
906  C CB  . SER A 124 ? 0.1391 0.1090 0.0997 0.0378  -0.0161 0.0195  141 SER A CB  
907  O OG  . SER A 124 ? 0.1225 0.1473 0.1067 0.0195  -0.0155 -0.0089 141 SER A OG  
908  N N   . ASP A 125 ? 0.1139 0.1206 0.1154 0.0147  -0.0180 0.0093  142 ASP A N   
909  C CA  . ASP A 125 ? 0.1500 0.1450 0.1231 0.0255  -0.0103 0.0103  142 ASP A CA  
910  C C   . ASP A 125 ? 0.1775 0.1446 0.1256 0.0070  -0.0090 0.0071  142 ASP A C   
911  O O   . ASP A 125 ? 0.2856 0.1846 0.1293 0.0415  0.0405  0.0033  142 ASP A O   
912  C CB  . ASP A 125 ? 0.1982 0.1477 0.1409 0.0253  -0.0206 -0.0161 142 ASP A CB  
913  C CG  . ASP A 125 ? 0.2632 0.2850 0.1619 -0.0269 -0.0363 -0.0457 142 ASP A CG  
914  O OD1 . ASP A 125 ? 0.2010 0.3880 0.1658 -0.0996 -0.0355 -0.0454 142 ASP A OD1 
915  O OD2 . ASP A 125 ? 0.3052 0.3104 0.1824 -0.0424 -0.0393 -0.0516 142 ASP A OD2 
916  N N   . SER A 126 ? 0.1373 0.1035 0.1256 0.0161  -0.0215 0.0240  143 SER A N   
917  C CA  . SER A 126 ? 0.1599 0.1407 0.1322 0.0149  -0.0471 0.0119  143 SER A CA  
918  C C   . SER A 126 ? 0.1715 0.1529 0.1348 0.0052  -0.0385 0.0042  143 SER A C   
919  O O   . SER A 126 ? 0.1548 0.1541 0.1258 0.0144  -0.0229 -0.0036 143 SER A O   
920  C CB  . SER A 126 ? 0.1585 0.2088 0.1325 0.0000  -0.0541 0.0081  143 SER A CB  
921  O OG  . SER A 126 ? 0.1712 0.3086 0.1403 0.0048  -0.0672 -0.0248 143 SER A OG  
922  N N   . ALA A 127 ? 0.1802 0.1313 0.1487 0.0228  -0.0540 0.0240  144 ALA A N   
923  C CA  . ALA A 127 ? 0.1512 0.1016 0.1532 0.0079  -0.0502 0.0332  144 ALA A CA  
924  C C   . ALA A 127 ? 0.1823 0.1398 0.1535 0.0235  -0.0456 0.0339  144 ALA A C   
925  O O   . ALA A 127 ? 0.1931 0.1457 0.1617 0.0154  -0.0420 0.0222  144 ALA A O   
926  C CB  . ALA A 127 ? 0.2104 0.1537 0.1643 0.0374  -0.0305 0.0479  144 ALA A CB  
927  N N   . GLU A 128 ? 0.1336 0.1629 0.1495 0.0510  -0.0498 0.0266  145 GLU A N   
928  C CA  . GLU A 128 ? 0.2096 0.1762 0.1467 0.0274  -0.0687 0.0267  145 GLU A CA  
929  C C   . GLU A 128 ? 0.1437 0.1582 0.1400 0.0252  -0.0561 0.0301  145 GLU A C   
930  O O   . GLU A 128 ? 0.1761 0.2077 0.1454 0.0341  -0.0560 0.0257  145 GLU A O   
931  C CB  . GLU A 128 ? 0.2896 0.2732 0.1528 0.0354  -0.0662 0.0306  145 GLU A CB  
932  C CG  . GLU A 128 ? 0.3859 0.2513 0.1646 0.0837  -0.0473 0.0573  145 GLU A CG  
933  C CD  . GLU A 128 ? 0.4333 0.2483 0.1777 0.0610  -0.0321 0.0794  145 GLU A CD  
934  O OE1 . GLU A 128 ? 0.4262 0.1762 0.1782 0.0283  -0.0291 0.0626  145 GLU A OE1 
935  O OE2 . GLU A 128 ? 0.4868 0.3109 0.1996 0.1229  -0.0071 0.0847  145 GLU A OE2 
936  N N   . SER A 129 ? 0.1630 0.1762 0.1316 0.0625  -0.0372 0.0451  146 SER A N   
937  C CA  A SER A 129 ? 0.1427 0.1221 0.1303 0.0249  -0.0512 0.0409  146 SER A CA  
938  C CA  B SER A 129 ? 0.1553 0.1146 0.1284 0.0130  -0.0602 0.0265  146 SER A CA  
939  C C   . SER A 129 ? 0.1169 0.1159 0.1278 -0.0564 -0.0431 0.0419  146 SER A C   
940  O O   . SER A 129 ? 0.1351 0.0857 0.1352 0.0146  -0.0294 0.0279  146 SER A O   
941  C CB  A SER A 129 ? 0.1739 0.1841 0.1380 0.0736  -0.0476 0.0279  146 SER A CB  
942  C CB  B SER A 129 ? 0.2176 0.1606 0.1290 0.0442  -0.0766 -0.0144 146 SER A CB  
943  O OG  A SER A 129 ? 0.1137 0.1978 0.1425 0.0452  -0.0442 0.0372  146 SER A OG  
944  O OG  B SER A 129 ? 0.1829 0.1545 0.1347 -0.0289 -0.0755 -0.0301 146 SER A OG  
945  N N   . ALA A 130 ? 0.1325 0.1548 0.1232 -0.0476 -0.0382 0.0187  147 ALA A N   
946  C CA  . ALA A 130 ? 0.1200 0.1818 0.1278 -0.0231 -0.0400 0.0343  147 ALA A CA  
947  C C   . ALA A 130 ? 0.1031 0.1471 0.1322 0.0279  -0.0418 0.0219  147 ALA A C   
948  O O   . ALA A 130 ? 0.1392 0.1302 0.1308 -0.0254 -0.0290 0.0313  147 ALA A O   
949  C CB  . ALA A 130 ? 0.1133 0.2421 0.1302 0.0313  -0.0258 0.0637  147 ALA A CB  
950  N N   . LYS A 131 ? 0.1509 0.1316 0.1430 0.0021  -0.0329 0.0142  148 LYS A N   
951  C CA  . LYS A 131 ? 0.1730 0.1192 0.1612 -0.0027 -0.0313 0.0243  148 LYS A CA  
952  C C   . LYS A 131 ? 0.1646 0.1266 0.1633 0.0461  -0.0497 0.0164  148 LYS A C   
953  O O   . LYS A 131 ? 0.1580 0.1297 0.1623 0.0188  -0.0559 0.0285  148 LYS A O   
954  C CB  . LYS A 131 ? 0.1770 0.1167 0.1778 0.0003  -0.0256 0.0330  148 LYS A CB  
955  C CG  . LYS A 131 ? 0.2503 0.1229 0.1906 0.0625  -0.0351 0.0364  148 LYS A CG  
956  C CD  . LYS A 131 ? 0.2905 0.2388 0.2086 0.1442  -0.0201 0.0327  148 LYS A CD  
957  C CE  . LYS A 131 ? 0.2995 0.3728 0.2183 0.1969  0.0078  0.0131  148 LYS A CE  
958  N NZ  . LYS A 131 ? 0.2777 0.4767 0.2264 0.1897  0.0140  0.0258  148 LYS A NZ  
959  N N   . ARG A 132 ? 0.1264 0.1082 0.1622 0.0316  -0.0562 -0.0042 149 ARG A N   
960  C CA  . ARG A 132 ? 0.1398 0.1207 0.1636 0.0070  -0.0588 0.0010  149 ARG A CA  
961  C C   . ARG A 132 ? 0.1397 0.0791 0.1569 0.0393  -0.0232 -0.0085 149 ARG A C   
962  O O   . ARG A 132 ? 0.1356 0.1290 0.1593 0.0396  -0.0281 0.0025  149 ARG A O   
963  C CB  . ARG A 132 ? 0.1696 0.1555 0.1765 -0.0375 -0.0663 0.0062  149 ARG A CB  
964  C CG  . ARG A 132 ? 0.2664 0.1907 0.1839 -0.0506 -0.0742 0.0013  149 ARG A CG  
965  C CD  . ARG A 132 ? 0.3575 0.2739 0.1919 -0.0854 -0.0873 0.0096  149 ARG A CD  
966  N NE  . ARG A 132 ? 0.4502 0.2857 0.2003 -0.1608 -0.0796 0.0240  149 ARG A NE  
967  C CZ  . ARG A 132 ? 0.5744 0.3525 0.2087 -0.0506 -0.0630 0.0433  149 ARG A CZ  
968  N NH1 . ARG A 132 ? 0.6416 0.3598 0.2100 -0.0147 -0.0489 0.0635  149 ARG A NH1 
969  N NH2 . ARG A 132 ? 0.5881 0.3788 0.2137 -0.0149 -0.0663 0.0397  149 ARG A NH2 
970  N N   . GLU A 133 ? 0.1154 0.0687 0.1483 0.0251  -0.0209 -0.0027 150 GLU A N   
971  C CA  . GLU A 133 ? 0.0933 0.0886 0.1434 -0.0170 -0.0154 0.0114  150 GLU A CA  
972  C C   . GLU A 133 ? 0.1078 0.1359 0.1313 -0.0023 -0.0174 0.0012  150 GLU A C   
973  O O   . GLU A 133 ? 0.1181 0.1650 0.1194 0.0125  -0.0198 0.0018  150 GLU A O   
974  C CB  . GLU A 133 ? 0.1394 0.0433 0.1466 0.0141  -0.0140 0.0045  150 GLU A CB  
975  C CG  . GLU A 133 ? 0.1392 0.1595 0.1529 0.0591  -0.0128 -0.0089 150 GLU A CG  
976  C CD  . GLU A 133 ? 0.1270 0.1132 0.1605 -0.0102 -0.0019 -0.0052 150 GLU A CD  
977  O OE1 . GLU A 133 ? 0.1126 0.1377 0.1566 -0.0040 0.0010  0.0102  150 GLU A OE1 
978  O OE2 . GLU A 133 ? 0.1510 0.1060 0.1718 -0.0016 0.0110  -0.0106 150 GLU A OE2 
979  N N   . ILE A 134 ? 0.1272 0.0990 0.1269 -0.0119 -0.0052 0.0035  151 ILE A N   
980  C CA  . ILE A 134 ? 0.1611 0.1188 0.1308 0.0510  -0.0223 -0.0150 151 ILE A CA  
981  C C   . ILE A 134 ? 0.1638 0.1368 0.1356 0.0076  -0.0308 -0.0145 151 ILE A C   
982  O O   . ILE A 134 ? 0.1573 0.1706 0.1282 -0.0162 -0.0211 0.0101  151 ILE A O   
983  C CB  . ILE A 134 ? 0.1356 0.1463 0.1381 0.0041  -0.0340 -0.0140 151 ILE A CB  
984  C CG1 . ILE A 134 ? 0.1284 0.1388 0.1400 -0.0059 -0.0374 0.0033  151 ILE A CG1 
985  C CG2 . ILE A 134 ? 0.1137 0.1720 0.1489 -0.0501 -0.0269 -0.0074 151 ILE A CG2 
986  C CD1 . ILE A 134 ? 0.0792 0.1468 0.1417 -0.0069 -0.0390 -0.0074 151 ILE A CD1 
987  N N   . SER A 135 ? 0.1216 0.0666 0.1471 0.0066  -0.0380 -0.0232 152 SER A N   
988  C CA  . SER A 135 ? 0.1313 0.1066 0.1600 0.0202  -0.0271 -0.0029 152 SER A CA  
989  C C   . SER A 135 ? 0.1166 0.1653 0.1588 0.0013  -0.0222 -0.0122 152 SER A C   
990  O O   . SER A 135 ? 0.1303 0.1448 0.1568 0.0295  0.0010  -0.0343 152 SER A O   
991  C CB  . SER A 135 ? 0.1771 0.1310 0.1769 0.0517  -0.0006 0.0285  152 SER A CB  
992  O OG  . SER A 135 ? 0.2119 0.2258 0.1884 0.0384  0.0342  0.0413  152 SER A OG  
993  N N   . LEU A 136 ? 0.1112 0.1279 0.1619 0.0084  -0.0280 -0.0068 153 LEU A N   
994  C CA  . LEU A 136 ? 0.0737 0.1050 0.1613 0.0253  -0.0346 -0.0181 153 LEU A CA  
995  C C   . LEU A 136 ? 0.1211 0.1175 0.1629 0.0194  -0.0241 -0.0252 153 LEU A C   
996  O O   . LEU A 136 ? 0.1165 0.1238 0.1687 0.0128  -0.0225 -0.0085 153 LEU A O   
997  C CB  . LEU A 136 ? 0.1133 0.1248 0.1642 0.0082  -0.0477 -0.0211 153 LEU A CB  
998  C CG  . LEU A 136 ? 0.1068 0.1528 0.1728 -0.0115 -0.0346 -0.0222 153 LEU A CG  
999  C CD1 . LEU A 136 ? 0.1873 0.2301 0.1819 -0.0430 -0.0254 -0.0090 153 LEU A CD1 
1000 C CD2 . LEU A 136 ? 0.1026 0.1598 0.1789 -0.0177 -0.0232 -0.0023 153 LEU A CD2 
1001 N N   . TRP A 137 ? 0.0814 0.1221 0.1594 0.0147  -0.0129 -0.0026 154 TRP A N   
1002 C CA  . TRP A 137 ? 0.0792 0.0713 0.1570 0.0007  -0.0238 0.0085  154 TRP A CA  
1003 C C   . TRP A 137 ? 0.1138 0.1447 0.1471 0.0417  -0.0351 0.0083  154 TRP A C   
1004 O O   . TRP A 137 ? 0.1523 0.1503 0.1367 0.0146  -0.0174 0.0239  154 TRP A O   
1005 C CB  . TRP A 137 ? 0.0855 0.1254 0.1570 0.0017  -0.0165 0.0143  154 TRP A CB  
1006 C CG  . TRP A 137 ? 0.0593 0.1186 0.1524 0.0266  -0.0290 0.0041  154 TRP A CG  
1007 C CD1 . TRP A 137 ? 0.0805 0.0817 0.1587 -0.0196 -0.0165 0.0328  154 TRP A CD1 
1008 C CD2 . TRP A 137 ? 0.1143 0.1043 0.1540 0.0156  -0.0187 0.0133  154 TRP A CD2 
1009 N NE1 . TRP A 137 ? 0.0975 0.1188 0.1568 0.0105  -0.0153 0.0315  154 TRP A NE1 
1010 C CE2 . TRP A 137 ? 0.1160 0.0951 0.1564 -0.0051 -0.0123 0.0245  154 TRP A CE2 
1011 C CE3 . TRP A 137 ? 0.1166 0.0974 0.1507 -0.0340 -0.0237 0.0045  154 TRP A CE3 
1012 C CZ2 . TRP A 137 ? 0.1027 0.1201 0.1571 0.0126  -0.0167 -0.0004 154 TRP A CZ2 
1013 C CZ3 . TRP A 137 ? 0.0692 0.1133 0.1490 -0.0395 -0.0044 0.0302  154 TRP A CZ3 
1014 C CH2 . TRP A 137 ? 0.1108 0.1352 0.1568 -0.0215 -0.0154 0.0218  154 TRP A CH2 
1015 N N   . PHE A 138 ? 0.1325 0.0756 0.1533 0.0124  -0.0272 -0.0168 155 PHE A N   
1016 C CA  . PHE A 138 ? 0.1362 0.0834 0.1590 0.0205  -0.0181 -0.0027 155 PHE A CA  
1017 C C   . PHE A 138 ? 0.1422 0.0794 0.1714 0.0339  -0.0181 0.0050  155 PHE A C   
1018 O O   . PHE A 138 ? 0.2176 0.1349 0.1745 0.0925  -0.0254 0.0052  155 PHE A O   
1019 C CB  . PHE A 138 ? 0.1361 0.0739 0.1458 -0.0017 -0.0055 0.0122  155 PHE A CB  
1020 C CG  . PHE A 138 ? 0.0811 0.0817 0.1333 -0.0111 -0.0022 -0.0093 155 PHE A CG  
1021 C CD1 . PHE A 138 ? 0.0605 0.0756 0.1296 -0.0075 -0.0213 -0.0127 155 PHE A CD1 
1022 C CD2 . PHE A 138 ? 0.1146 0.0912 0.1323 -0.0264 0.0046  0.0063  155 PHE A CD2 
1023 C CE1 . PHE A 138 ? 0.0871 0.1082 0.1321 0.0122  -0.0093 0.0036  155 PHE A CE1 
1024 C CE2 . PHE A 138 ? 0.0764 0.0892 0.1290 0.0048  -0.0160 -0.0023 155 PHE A CE2 
1025 C CZ  . PHE A 138 ? 0.1000 0.0871 0.1311 0.0108  -0.0004 0.0046  155 PHE A CZ  
1026 N N   . LYS A 139 ? 0.1106 0.0992 0.1883 -0.0109 -0.0229 -0.0094 156 LYS A N   
1027 C CA  . LYS A 139 ? 0.1446 0.0935 0.1961 -0.0093 -0.0106 0.0150  156 LYS A CA  
1028 C C   . LYS A 139 ? 0.0892 0.0835 0.1951 0.0099  -0.0341 -0.0104 156 LYS A C   
1029 O O   . LYS A 139 ? 0.1065 0.1059 0.1905 0.0122  -0.0249 0.0010  156 LYS A O   
1030 C CB  . LYS A 139 ? 0.2461 0.2237 0.2095 0.0908  0.0312  0.0380  156 LYS A CB  
1031 C CG  . LYS A 139 ? 0.3139 0.3024 0.2237 0.0335  0.0500  0.0433  156 LYS A CG  
1032 C CD  . LYS A 139 ? 0.3703 0.4264 0.2359 0.0173  0.0427  0.0370  156 LYS A CD  
1033 C CE  . LYS A 139 ? 0.4507 0.5639 0.2443 0.0637  0.0263  0.0318  156 LYS A CE  
1034 N NZ  . LYS A 139 ? 0.5309 0.6485 0.2506 0.1344  0.0148  0.0315  156 LYS A NZ  
1035 N N   . PRO A 140 ? 0.1301 0.1348 0.1979 0.0671  -0.0416 -0.0042 157 PRO A N   
1036 C CA  . PRO A 140 ? 0.1842 0.1233 0.2098 0.0047  -0.0449 0.0147  157 PRO A CA  
1037 C C   . PRO A 140 ? 0.1927 0.1001 0.2125 -0.0045 -0.0069 0.0067  157 PRO A C   
1038 O O   . PRO A 140 ? 0.1927 0.1027 0.2156 0.0052  0.0044  0.0037  157 PRO A O   
1039 C CB  . PRO A 140 ? 0.2721 0.1380 0.2102 0.0644  -0.0585 0.0441  157 PRO A CB  
1040 C CG  . PRO A 140 ? 0.2223 0.2024 0.2132 0.0705  -0.0658 0.0098  157 PRO A CG  
1041 C CD  . PRO A 140 ? 0.1901 0.1708 0.2067 0.0555  -0.0561 0.0024  157 PRO A CD  
1042 N N   . GLU A 141 ? 0.1701 0.1287 0.2155 0.0470  0.0009  -0.0044 158 GLU A N   
1043 C CA  . GLU A 141 ? 0.1541 0.2220 0.2233 0.0663  -0.0011 -0.0374 158 GLU A CA  
1044 C C   . GLU A 141 ? 0.1063 0.2059 0.2017 0.0214  -0.0188 -0.0553 158 GLU A C   
1045 O O   . GLU A 141 ? 0.1708 0.1758 0.2033 0.0028  -0.0224 -0.0821 158 GLU A O   
1046 C CB  . GLU A 141 ? 0.2010 0.3124 0.2493 0.1308  0.0051  -0.0591 158 GLU A CB  
1047 C CG  . GLU A 141 ? 0.3218 0.4445 0.2741 0.1864  -0.0127 -0.0660 158 GLU A CG  
1048 C CD  . GLU A 141 ? 0.3619 0.5038 0.2972 0.2082  -0.0281 -0.0745 158 GLU A CD  
1049 O OE1 . GLU A 141 ? 0.2118 0.2905 0.3018 0.0512  -0.0326 -0.0982 158 GLU A OE1 
1050 O OE2 . GLU A 141 ? 0.5238 0.6358 0.3094 0.3161  -0.0381 -0.0587 158 GLU A OE2 
1051 N N   . GLU A 142 ? 0.0757 0.1359 0.1801 0.0055  -0.0220 -0.0211 159 GLU A N   
1052 C CA  . GLU A 142 ? 0.0839 0.1226 0.1658 0.0347  -0.0094 0.0049  159 GLU A CA  
1053 C C   . GLU A 142 ? 0.0498 0.1459 0.1502 0.0127  -0.0105 -0.0130 159 GLU A C   
1054 O O   . GLU A 142 ? 0.0873 0.1325 0.1399 0.0057  0.0131  0.0139  159 GLU A O   
1055 C CB  . GLU A 142 ? 0.1171 0.1003 0.1718 -0.0196 -0.0183 0.0119  159 GLU A CB  
1056 C CG  . GLU A 142 ? 0.1771 0.1289 0.1819 -0.0560 -0.0096 -0.0022 159 GLU A CG  
1057 C CD  . GLU A 142 ? 0.2303 0.1416 0.1849 -0.0170 0.0124  0.0281  159 GLU A CD  
1058 O OE1 . GLU A 142 ? 0.2332 0.1360 0.1799 0.0166  0.0139  0.0320  159 GLU A OE1 
1059 O OE2 . GLU A 142 ? 0.2802 0.2161 0.1927 -0.0672 0.0205  0.0343  159 GLU A OE2 
1060 N N   . ILE A 143 ? 0.1036 0.1189 0.1573 -0.0029 -0.0213 -0.0076 160 ILE A N   
1061 C CA  . ILE A 143 ? 0.0795 0.1317 0.1593 0.0073  -0.0225 0.0004  160 ILE A CA  
1062 C C   . ILE A 143 ? 0.1501 0.1177 0.1573 0.0690  -0.0241 -0.0144 160 ILE A C   
1063 O O   . ILE A 143 ? 0.1068 0.1017 0.1737 0.0384  -0.0414 -0.0217 160 ILE A O   
1064 C CB  . ILE A 143 ? 0.1208 0.0994 0.1660 0.0211  0.0030  -0.0093 160 ILE A CB  
1065 C CG1 . ILE A 143 ? 0.0730 0.1712 0.1777 -0.0092 0.0049  -0.0064 160 ILE A CG1 
1066 C CG2 . ILE A 143 ? 0.1046 0.1542 0.1652 -0.0143 0.0114  0.0151  160 ILE A CG2 
1067 C CD1 . ILE A 143 ? 0.2161 0.1223 0.1813 0.0361  -0.0106 0.0025  160 ILE A CD1 
1068 N N   . GLN A 144 ? 0.1284 0.0589 0.1376 0.0424  -0.0034 -0.0006 161 GLN A N   
1069 C CA  . GLN A 144 ? 0.1237 0.0606 0.1386 -0.0177 0.0139  0.0107  161 GLN A CA  
1070 C C   . GLN A 144 ? 0.1206 0.0798 0.1423 -0.0390 0.0201  -0.0324 161 GLN A C   
1071 O O   . GLN A 144 ? 0.1359 0.0851 0.1518 0.0116  0.0255  -0.0331 161 GLN A O   
1072 C CB  . GLN A 144 ? 0.1528 0.0910 0.1320 0.0316  0.0058  0.0307  161 GLN A CB  
1073 C CG  . GLN A 144 ? 0.1122 0.1665 0.1259 0.0498  0.0086  0.0294  161 GLN A CG  
1074 C CD  . GLN A 144 ? 0.1372 0.1585 0.1305 0.0389  -0.0033 0.0189  161 GLN A CD  
1075 O OE1 . GLN A 144 ? 0.1301 0.1521 0.1348 0.0157  -0.0051 -0.0096 161 GLN A OE1 
1076 N NE2 . GLN A 144 ? 0.1384 0.1718 0.1341 0.0413  -0.0335 0.0060  161 GLN A NE2 
1077 N N   . SER A 145 ? 0.1047 0.0846 0.1367 -0.0399 -0.0066 -0.0018 162 SER A N   
1078 C CA  A SER A 145 ? 0.1314 0.0731 0.1380 -0.0165 -0.0074 0.0151  162 SER A CA  
1079 C CA  B SER A 145 ? 0.1266 0.1062 0.1378 0.0274  -0.0177 0.0035  162 SER A CA  
1080 C C   . SER A 145 ? 0.1224 0.0924 0.1333 0.0162  -0.0016 -0.0024 162 SER A C   
1081 O O   . SER A 145 ? 0.1219 0.1878 0.1346 0.0367  0.0132  -0.0445 162 SER A O   
1082 C CB  A SER A 145 ? 0.1527 0.0763 0.1369 -0.0281 0.0157  0.0460  162 SER A CB  
1083 C CB  B SER A 145 ? 0.1437 0.1451 0.1416 0.0788  -0.0191 0.0182  162 SER A CB  
1084 O OG  A SER A 145 ? 0.2009 0.1467 0.1456 0.0092  0.0192  0.0841  162 SER A OG  
1085 O OG  B SER A 145 ? 0.1612 0.1338 0.1454 0.0429  -0.0215 0.0210  162 SER A OG  
1086 N N   . TYR A 146 ? 0.1146 0.0736 0.1311 0.0046  0.0048  -0.0029 163 TYR A N   
1087 C CA  . TYR A 146 ? 0.1232 0.1028 0.1288 0.0254  0.0093  0.0265  163 TYR A CA  
1088 C C   . TYR A 146 ? 0.0929 0.0641 0.1328 0.0242  0.0185  0.0178  163 TYR A C   
1089 O O   . TYR A 146 ? 0.1685 0.0855 0.1347 -0.0049 0.0240  -0.0129 163 TYR A O   
1090 C CB  . TYR A 146 ? 0.1459 0.1088 0.1210 -0.0084 -0.0014 0.0151  163 TYR A CB  
1091 C CG  . TYR A 146 ? 0.1598 0.0788 0.1162 0.0357  0.0135  0.0158  163 TYR A CG  
1092 C CD1 . TYR A 146 ? 0.0996 0.0819 0.1188 0.0006  0.0124  0.0080  163 TYR A CD1 
1093 C CD2 . TYR A 146 ? 0.1174 0.0852 0.1110 0.0090  0.0009  -0.0256 163 TYR A CD2 
1094 C CE1 . TYR A 146 ? 0.1303 0.1062 0.1102 -0.0573 0.0214  0.0165  163 TYR A CE1 
1095 C CE2 . TYR A 146 ? 0.0809 0.1031 0.1049 0.0417  -0.0007 -0.0128 163 TYR A CE2 
1096 C CZ  . TYR A 146 ? 0.1010 0.1323 0.1078 0.0225  0.0165  0.0047  163 TYR A CZ  
1097 O OH  . TYR A 146 ? 0.0815 0.0967 0.1095 -0.0040 -0.0099 -0.0107 163 TYR A OH  
1098 N N   . LYS A 147 ? 0.0870 0.1011 0.1416 -0.0171 0.0018  0.0247  164 LYS A N   
1099 C CA  . LYS A 147 ? 0.0994 0.0848 0.1448 -0.0203 0.0304  0.0129  164 LYS A CA  
1100 C C   . LYS A 147 ? 0.1091 0.0985 0.1319 -0.0050 0.0109  0.0283  164 LYS A C   
1101 O O   . LYS A 147 ? 0.1578 0.1229 0.1227 0.0257  0.0161  0.0194  164 LYS A O   
1102 C CB  . LYS A 147 ? 0.0926 0.1581 0.1652 -0.0283 0.0247  0.0313  164 LYS A CB  
1103 C CG  . LYS A 147 ? 0.2333 0.1596 0.1873 -0.0061 0.0296  0.0475  164 LYS A CG  
1104 C CD  . LYS A 147 ? 0.3158 0.1483 0.2057 0.0303  0.0523  0.0500  164 LYS A CD  
1105 C CE  . LYS A 147 ? 0.4058 0.3856 0.2163 0.0500  0.0542  0.0490  164 LYS A CE  
1106 N NZ  . LYS A 147 ? 0.4865 0.5509 0.2297 0.0903  0.0575  0.0478  164 LYS A NZ  
1107 N N   . LEU A 148 ? 0.1502 0.1273 0.1325 0.0204  -0.0166 0.0126  165 LEU A N   
1108 C CA  . LEU A 148 ? 0.0564 0.1122 0.1329 -0.0405 -0.0040 -0.0019 165 LEU A CA  
1109 C C   . LEU A 148 ? 0.1048 0.0893 0.1272 0.0168  0.0058  -0.0176 165 LEU A C   
1110 O O   . LEU A 148 ? 0.1030 0.1116 0.1358 0.0090  0.0273  0.0158  165 LEU A O   
1111 C CB  . LEU A 148 ? 0.1266 0.1156 0.1494 0.0082  -0.0203 -0.0248 165 LEU A CB  
1112 C CG  . LEU A 148 ? 0.1538 0.1621 0.1633 0.0214  -0.0090 -0.0270 165 LEU A CG  
1113 C CD1 . LEU A 148 ? 0.1298 0.1205 0.1727 0.0098  -0.0098 -0.0178 165 LEU A CD1 
1114 C CD2 . LEU A 148 ? 0.1164 0.1873 0.1696 0.0181  0.0225  -0.0150 165 LEU A CD2 
1115 N N   . ALA A 149 ? 0.1225 0.1220 0.1161 0.0141  -0.0121 -0.0099 166 ALA A N   
1116 C CA  . ALA A 149 ? 0.1631 0.2003 0.1222 0.0352  -0.0012 -0.0181 166 ALA A CA  
1117 C C   . ALA A 149 ? 0.1741 0.1940 0.1327 0.0137  0.0040  -0.0186 166 ALA A C   
1118 O O   . ALA A 149 ? 0.1908 0.1377 0.1458 0.0183  -0.0079 -0.0241 166 ALA A O   
1119 C CB  . ALA A 149 ? 0.2060 0.3467 0.1202 0.0028  0.0028  -0.0429 166 ALA A CB  
1120 N N   . LEU A 150 ? 0.1494 0.1432 0.1274 0.0323  0.0102  -0.0213 167 LEU A N   
1121 C CA  . LEU A 150 ? 0.1153 0.1220 0.1337 0.0109  0.0025  -0.0193 167 LEU A CA  
1122 C C   . LEU A 150 ? 0.0918 0.1358 0.1422 0.0099  -0.0024 -0.0141 167 LEU A C   
1123 O O   . LEU A 150 ? 0.1212 0.0871 0.1449 0.0150  0.0204  0.0035  167 LEU A O   
1124 C CB  . LEU A 150 ? 0.1589 0.1693 0.1401 0.0430  0.0060  0.0008  167 LEU A CB  
1125 C CG  . LEU A 150 ? 0.1782 0.2248 0.1526 -0.0175 -0.0133 0.0210  167 LEU A CG  
1126 C CD1 . LEU A 150 ? 0.1890 0.2194 0.1526 0.0675  -0.0215 0.0130  167 LEU A CD1 
1127 C CD2 . LEU A 150 ? 0.3133 0.3599 0.1632 0.0430  -0.0421 0.0244  167 LEU A CD2 
1128 N N   . SER A 151 ? 0.1232 0.1310 0.1453 -0.0282 -0.0064 -0.0022 168 SER A N   
1129 C CA  A SER A 151 ? 0.1378 0.1423 0.1470 -0.0498 -0.0016 0.0082  168 SER A CA  
1130 C CA  B SER A 151 ? 0.1250 0.1607 0.1490 -0.0007 0.0020  0.0136  168 SER A CA  
1131 C C   . SER A 151 ? 0.1259 0.1358 0.1460 -0.0178 0.0074  0.0213  168 SER A C   
1132 O O   . SER A 151 ? 0.1274 0.1438 0.1364 0.0342  0.0098  0.0094  168 SER A O   
1133 C CB  A SER A 151 ? 0.1587 0.1880 0.1532 -0.0337 0.0056  0.0042  168 SER A CB  
1134 C CB  B SER A 151 ? 0.1104 0.1949 0.1591 0.0703  0.0178  0.0196  168 SER A CB  
1135 O OG  A SER A 151 ? 0.2003 0.2238 0.1579 -0.0379 0.0164  0.0132  168 SER A OG  
1136 O OG  B SER A 151 ? 0.1637 0.1769 0.1685 0.0804  0.0378  0.0313  168 SER A OG  
1137 N N   . ASP A 152 ? 0.1248 0.1173 0.1547 -0.0082 0.0201  0.0323  169 ASP A N   
1138 C CA  . ASP A 152 ? 0.1879 0.1773 0.1693 0.0662  0.0100  0.0132  169 ASP A CA  
1139 C C   . ASP A 152 ? 0.1096 0.1573 0.1521 0.0272  0.0207  0.0000  169 ASP A C   
1140 O O   . ASP A 152 ? 0.1713 0.1906 0.1556 0.0292  0.0329  0.0118  169 ASP A O   
1141 C CB  . ASP A 152 ? 0.2193 0.1526 0.1965 -0.0810 -0.0028 0.0043  169 ASP A CB  
1142 C CG  . ASP A 152 ? 0.3759 0.2782 0.2175 0.0081  -0.0113 -0.0216 169 ASP A CG  
1143 O OD1 . ASP A 152 ? 0.4878 0.3097 0.2257 0.0690  -0.0038 0.0051  169 ASP A OD1 
1144 O OD2 . ASP A 152 ? 0.4149 0.3504 0.2326 0.0279  -0.0151 -0.0426 169 ASP A OD2 
1145 N N   . TYR A 153 ? 0.1063 0.1600 0.1386 0.0153  0.0048  -0.0166 170 TYR A N   
1146 C CA  . TYR A 153 ? 0.1045 0.1384 0.1379 -0.0066 0.0108  0.0096  170 TYR A CA  
1147 C C   . TYR A 153 ? 0.1233 0.0777 0.1509 -0.0230 0.0079  0.0004  170 TYR A C   
1148 O O   . TYR A 153 ? 0.1068 0.1019 0.1535 0.0281  -0.0013 -0.0233 170 TYR A O   
1149 C CB  . TYR A 153 ? 0.0822 0.1522 0.1277 -0.0237 -0.0030 0.0073  170 TYR A CB  
1150 C CG  . TYR A 153 ? 0.1572 0.1155 0.1308 0.0361  0.0046  0.0109  170 TYR A CG  
1151 C CD1 . TYR A 153 ? 0.1225 0.1193 0.1392 0.0365  0.0163  0.0046  170 TYR A CD1 
1152 C CD2 . TYR A 153 ? 0.1534 0.1494 0.1347 0.0076  0.0016  -0.0123 170 TYR A CD2 
1153 C CE1 . TYR A 153 ? 0.1366 0.1215 0.1423 -0.0173 0.0172  -0.0014 170 TYR A CE1 
1154 C CE2 . TYR A 153 ? 0.1507 0.1675 0.1387 0.0337  -0.0049 0.0181  170 TYR A CE2 
1155 C CZ  . TYR A 153 ? 0.1466 0.1460 0.1451 -0.0364 -0.0251 -0.0163 170 TYR A CZ  
1156 O OH  . TYR A 153 ? 0.2200 0.2239 0.1522 -0.0344 -0.0412 -0.0378 170 TYR A OH  
1157 N N   . ILE A 154 ? 0.1059 0.1442 0.1633 -0.0377 -0.0053 -0.0307 171 ILE A N   
1158 C CA  . ILE A 154 ? 0.0969 0.1237 0.1690 0.0086  -0.0072 -0.0236 171 ILE A CA  
1159 C C   . ILE A 154 ? 0.1153 0.1921 0.1806 0.0114  0.0014  -0.0164 171 ILE A C   
1160 O O   . ILE A 154 ? 0.1288 0.1668 0.1909 0.0245  -0.0039 -0.0247 171 ILE A O   
1161 C CB  . ILE A 154 ? 0.1610 0.1111 0.1702 -0.0110 -0.0036 -0.0040 171 ILE A CB  
1162 C CG1 . ILE A 154 ? 0.1532 0.1992 0.1764 -0.0205 -0.0021 0.0100  171 ILE A CG1 
1163 C CG2 . ILE A 154 ? 0.1472 0.1616 0.1734 -0.0762 -0.0120 -0.0111 171 ILE A CG2 
1164 C CD1 . ILE A 154 ? 0.1799 0.1786 0.1793 -0.0612 -0.0113 -0.0017 171 ILE A CD1 
1165 N N   . PHE A 155 ? 0.1493 0.1375 0.1842 0.0230  0.0112  0.0102  172 PHE A N   
1166 C CA  . PHE A 155 ? 0.1586 0.1406 0.1848 0.0000  0.0138  0.0091  172 PHE A CA  
1167 C C   . PHE A 155 ? 0.1658 0.2255 0.2075 -0.0634 0.0308  0.0179  172 PHE A C   
1168 O O   . PHE A 155 ? 0.1670 0.2673 0.2073 -0.0436 0.0354  0.0330  172 PHE A O   
1169 C CB  . PHE A 155 ? 0.1688 0.1131 0.1797 0.0168  0.0019  0.0288  172 PHE A CB  
1170 C CG  . PHE A 155 ? 0.1342 0.1038 0.1754 -0.0587 0.0070  0.0339  172 PHE A CG  
1171 C CD1 . PHE A 155 ? 0.1676 0.1088 0.1712 -0.0148 -0.0369 0.0141  172 PHE A CD1 
1172 C CD2 . PHE A 155 ? 0.1151 0.1752 0.1772 -0.0155 0.0258  0.0199  172 PHE A CD2 
1173 C CE1 . PHE A 155 ? 0.1478 0.2177 0.1739 -0.0374 -0.0065 0.0385  172 PHE A CE1 
1174 C CE2 . PHE A 155 ? 0.1745 0.1538 0.1787 -0.0167 0.0306  0.0168  172 PHE A CE2 
1175 C CZ  . PHE A 155 ? 0.1589 0.1642 0.1811 -0.0785 0.0290  0.0416  172 PHE A CZ  
1176 N N   . GLU A 156 ? 0.3098 0.2644 0.2307 -0.0734 0.0493  0.0309  173 GLU A N   
1177 C CA  . GLU A 156 ? 0.4028 0.3249 0.2568 -0.1196 0.0665  0.0413  173 GLU A CA  
1178 C C   . GLU A 156 ? 0.5197 0.3548 0.2744 -0.1431 0.0829  0.0387  173 GLU A C   
1179 O O   . GLU A 156 ? 0.5694 0.4993 0.2789 -0.1175 0.0957  0.0493  173 GLU A O   
1180 C CB  . GLU A 156 ? 0.4071 0.3401 0.2672 -0.1021 0.0625  0.0593  173 GLU A CB  
1181 C CG  . GLU A 156 ? 0.4385 0.3668 0.2792 -0.0238 0.0425  0.0610  173 GLU A CG  
1182 C CD  . GLU A 156 ? 0.3762 0.2818 0.2851 -0.0075 0.0133  0.0559  173 GLU A CD  
1183 O OE1 . GLU A 156 ? 0.3976 0.3656 0.2895 0.0734  -0.0009 0.0501  173 GLU A OE1 
1184 O OE2 . GLU A 156 ? 0.2854 0.1244 0.2915 0.0157  0.0141  0.0689  173 GLU A OE2 
1185 O OXT . GLU A 156 ? 0.5741 0.2775 0.2874 -0.1153 0.0759  0.0243  173 GLU A OXT 
1186 N N   . HIS B 8   ? 0.3201 0.6950 0.2658 -0.0412 -0.0987 -0.0100 25  HIS B N   
1187 C CA  . HIS B 8   ? 0.2494 0.5467 0.2672 -0.1091 -0.0916 -0.0041 25  HIS B CA  
1188 C C   . HIS B 8   ? 0.2495 0.4830 0.2455 -0.1148 -0.0742 0.0110  25  HIS B C   
1189 O O   . HIS B 8   ? 0.2990 0.5712 0.2478 -0.0668 -0.0847 0.0109  25  HIS B O   
1190 C CB  . HIS B 8   ? 0.2866 0.6383 0.2629 -0.0896 -0.0896 0.0096  25  HIS B CB  
1191 N N   . VAL B 9   ? 0.1906 0.3805 0.2286 -0.1045 -0.0554 -0.0006 26  VAL B N   
1192 C CA  . VAL B 9   ? 0.1549 0.2389 0.2106 -0.0648 -0.0369 -0.0052 26  VAL B CA  
1193 C C   . VAL B 9   ? 0.2028 0.2268 0.1956 -0.0101 -0.0352 -0.0277 26  VAL B C   
1194 O O   . VAL B 9   ? 0.2499 0.1680 0.2064 -0.0354 -0.0333 -0.0287 26  VAL B O   
1195 C CB  . VAL B 9   ? 0.1764 0.2701 0.2112 -0.0089 -0.0040 0.0044  26  VAL B CB  
1196 C CG1 . VAL B 9   ? 0.2031 0.2300 0.2134 -0.0255 0.0279  0.0052  26  VAL B CG1 
1197 C CG2 . VAL B 9   ? 0.1460 0.2661 0.2069 -0.0461 0.0167  0.0088  26  VAL B CG2 
1198 N N   . GLU B 10  ? 0.1312 0.1654 0.1763 -0.0353 -0.0340 -0.0095 27  GLU B N   
1199 C CA  . GLU B 10  ? 0.1139 0.1525 0.1657 0.0251  -0.0391 -0.0356 27  GLU B CA  
1200 C C   . GLU B 10  ? 0.1438 0.0559 0.1549 -0.0213 -0.0191 -0.0206 27  GLU B C   
1201 O O   . GLU B 10  ? 0.1104 0.1166 0.1532 0.0211  0.0037  -0.0235 27  GLU B O   
1202 C CB  . GLU B 10  ? 0.2732 0.2617 0.1772 0.1035  -0.0175 -0.0092 27  GLU B CB  
1203 C CG  . GLU B 10  ? 0.2538 0.1918 0.1793 0.0205  -0.0028 -0.0024 27  GLU B CG  
1204 C CD  . GLU B 10  ? 0.2988 0.2249 0.1758 0.0497  -0.0207 -0.0382 27  GLU B CD  
1205 O OE1 . GLU B 10  ? 0.3970 0.3119 0.2000 -0.0069 -0.0025 -0.0398 27  GLU B OE1 
1206 O OE2 . GLU B 10  ? 0.2367 0.1195 0.1651 0.0037  -0.0129 -0.0230 27  GLU B OE2 
1207 N N   . GLN B 11  ? 0.1858 0.0790 0.1390 -0.0005 -0.0210 -0.0461 28  GLN B N   
1208 C CA  . GLN B 11  ? 0.1159 0.0717 0.1416 -0.0338 -0.0148 -0.0238 28  GLN B CA  
1209 C C   . GLN B 11  ? 0.1330 0.1164 0.1314 0.0056  -0.0129 -0.0113 28  GLN B C   
1210 O O   . GLN B 11  ? 0.1430 0.1721 0.1254 0.0084  0.0084  -0.0338 28  GLN B O   
1211 C CB  . GLN B 11  ? 0.1578 0.0922 0.1454 0.0203  -0.0064 -0.0199 28  GLN B CB  
1212 C CG  . GLN B 11  ? 0.1691 0.1096 0.1560 0.0179  -0.0153 -0.0072 28  GLN B CG  
1213 C CD  . GLN B 11  ? 0.1976 0.0914 0.1652 0.0376  -0.0138 -0.0003 28  GLN B CD  
1214 O OE1 . GLN B 11  ? 0.2348 0.1570 0.1760 0.0591  -0.0006 0.0388  28  GLN B OE1 
1215 N NE2 . GLN B 11  ? 0.2204 0.1787 0.1712 0.0205  -0.0198 -0.0150 28  GLN B NE2 
1216 N N   . THR B 12  ? 0.1017 0.1248 0.1254 0.0069  -0.0278 -0.0168 29  THR B N   
1217 C CA  . THR B 12  ? 0.1133 0.1031 0.1229 -0.0337 -0.0143 -0.0376 29  THR B CA  
1218 C C   . THR B 12  ? 0.1384 0.0958 0.1083 0.0157  -0.0082 -0.0176 29  THR B C   
1219 O O   . THR B 12  ? 0.0945 0.1100 0.1112 0.0167  -0.0100 -0.0031 29  THR B O   
1220 C CB  . THR B 12  ? 0.1177 0.1067 0.1351 -0.0480 -0.0026 -0.0130 29  THR B CB  
1221 O OG1 . THR B 12  ? 0.1513 0.1229 0.1409 0.0404  -0.0009 0.0125  29  THR B OG1 
1222 C CG2 . THR B 12  ? 0.1085 0.0799 0.1460 -0.0294 -0.0023 -0.0023 29  THR B CG2 
1223 N N   . TYR B 13  ? 0.1236 0.1002 0.0987 -0.0049 -0.0157 -0.0084 30  TYR B N   
1224 C CA  . TYR B 13  ? 0.1020 0.0849 0.0997 0.0121  -0.0057 -0.0294 30  TYR B CA  
1225 C C   . TYR B 13  ? 0.1134 0.1017 0.0973 0.0219  -0.0097 -0.0134 30  TYR B C   
1226 O O   . TYR B 13  ? 0.1570 0.0844 0.0936 0.0079  -0.0080 -0.0243 30  TYR B O   
1227 C CB  . TYR B 13  ? 0.1284 0.0846 0.1074 -0.0152 -0.0200 -0.0296 30  TYR B CB  
1228 C CG  . TYR B 13  ? 0.1967 0.0749 0.1129 0.0336  -0.0124 -0.0063 30  TYR B CG  
1229 C CD1 . TYR B 13  ? 0.1833 0.0841 0.1115 0.0046  0.0002  0.0022  30  TYR B CD1 
1230 C CD2 . TYR B 13  ? 0.2176 0.0758 0.1168 0.0292  0.0097  -0.0096 30  TYR B CD2 
1231 C CE1 . TYR B 13  ? 0.1820 0.0759 0.1158 0.0352  -0.0062 0.0097  30  TYR B CE1 
1232 C CE2 . TYR B 13  ? 0.1579 0.1006 0.1142 0.0197  -0.0043 -0.0235 30  TYR B CE2 
1233 C CZ  . TYR B 13  ? 0.1695 0.0873 0.1112 0.0357  -0.0244 -0.0057 30  TYR B CZ  
1234 O OH  . TYR B 13  ? 0.1972 0.1485 0.1034 0.0505  -0.0542 -0.0091 30  TYR B OH  
1235 N N   . LEU B 14  ? 0.1260 0.0918 0.0936 0.0339  -0.0077 -0.0148 31  LEU B N   
1236 C CA  . LEU B 14  ? 0.1476 0.0800 0.0930 0.0368  -0.0148 -0.0311 31  LEU B CA  
1237 C C   . LEU B 14  ? 0.1232 0.0879 0.0845 0.0255  0.0067  -0.0110 31  LEU B C   
1238 O O   . LEU B 14  ? 0.1350 0.1679 0.0835 -0.0057 0.0109  0.0315  31  LEU B O   
1239 C CB  . LEU B 14  ? 0.1216 0.0963 0.0997 -0.0116 -0.0182 -0.0269 31  LEU B CB  
1240 C CG  . LEU B 14  ? 0.1386 0.1361 0.1103 0.0092  -0.0104 -0.0103 31  LEU B CG  
1241 C CD1 . LEU B 14  ? 0.1415 0.1639 0.1233 0.0554  -0.0209 0.0030  31  LEU B CD1 
1242 C CD2 . LEU B 14  ? 0.1582 0.2114 0.1056 0.0987  0.0154  0.0054  31  LEU B CD2 
1243 N N   . MET B 15  ? 0.1058 0.1177 0.0819 0.0208  -0.0048 0.0179  32  MET B N   
1244 C CA  . MET B 15  ? 0.1032 0.1079 0.0917 0.0182  -0.0035 -0.0020 32  MET B CA  
1245 C C   . MET B 15  ? 0.0861 0.1181 0.0871 0.0194  -0.0142 -0.0017 32  MET B C   
1246 O O   . MET B 15  ? 0.1401 0.1282 0.0808 0.0212  0.0161  0.0005  32  MET B O   
1247 C CB  . MET B 15  ? 0.0920 0.1363 0.1064 0.0080  0.0092  -0.0067 32  MET B CB  
1248 C CG  . MET B 15  ? 0.0997 0.1718 0.1224 0.0640  -0.0134 -0.0207 32  MET B CG  
1249 S SD  . MET B 15  ? 0.2117 0.1314 0.1395 0.0712  -0.0122 -0.0091 32  MET B SD  
1250 C CE  . MET B 15  ? 0.2322 0.1481 0.1384 0.0699  -0.0198 -0.0247 32  MET B CE  
1251 N N   . ILE B 16  ? 0.0686 0.1015 0.0828 0.0352  -0.0186 -0.0089 33  ILE B N   
1252 C CA  . ILE B 16  ? 0.0542 0.1174 0.0865 0.0069  -0.0026 0.0031  33  ILE B CA  
1253 C C   . ILE B 16  ? 0.0783 0.0806 0.0931 -0.0016 -0.0074 0.0114  33  ILE B C   
1254 O O   . ILE B 16  ? 0.1032 0.1106 0.1050 0.0448  0.0126  0.0292  33  ILE B O   
1255 C CB  . ILE B 16  ? 0.0793 0.1142 0.0909 0.0122  0.0147  -0.0030 33  ILE B CB  
1256 C CG1 . ILE B 16  ? 0.0953 0.1416 0.0994 -0.0116 0.0129  -0.0215 33  ILE B CG1 
1257 C CG2 . ILE B 16  ? 0.0991 0.1421 0.0846 0.0364  0.0017  0.0074  33  ILE B CG2 
1258 C CD1 . ILE B 16  ? 0.1091 0.1375 0.0963 0.0614  0.0227  -0.0073 33  ILE B CD1 
1259 N N   . LYS B 17  ? 0.0944 0.0774 0.0933 0.0330  -0.0036 -0.0073 34  LYS B N   
1260 C CA  . LYS B 17  ? 0.0789 0.0903 0.0958 0.0489  0.0066  0.0038  34  LYS B CA  
1261 C C   . LYS B 17  ? 0.0867 0.1231 0.0934 0.0187  0.0136  0.0187  34  LYS B C   
1262 O O   . LYS B 17  ? 0.1054 0.1066 0.0910 0.0483  0.0171  0.0017  34  LYS B O   
1263 C CB  . LYS B 17  ? 0.0752 0.1180 0.1030 0.0503  -0.0029 -0.0031 34  LYS B CB  
1264 C CG  . LYS B 17  ? 0.0877 0.0864 0.1022 0.0113  0.0081  -0.0007 34  LYS B CG  
1265 C CD  . LYS B 17  ? 0.1580 0.0701 0.0988 0.0222  0.0084  0.0086  34  LYS B CD  
1266 C CE  . LYS B 17  ? 0.1680 0.0979 0.0917 0.0003  0.0229  0.0088  34  LYS B CE  
1267 N NZ  . LYS B 17  ? 0.2251 0.0789 0.0872 0.0172  0.0001  0.0043  34  LYS B NZ  
1268 N N   . PRO B 18  ? 0.0926 0.1387 0.0927 0.0144  0.0105  0.0082  35  PRO B N   
1269 C CA  . PRO B 18  ? 0.0678 0.1114 0.0975 0.0098  -0.0176 0.0144  35  PRO B CA  
1270 C C   . PRO B 18  ? 0.0950 0.1147 0.0924 0.0220  0.0068  0.0054  35  PRO B C   
1271 O O   . PRO B 18  ? 0.1324 0.1208 0.0836 0.0334  0.0093  0.0130  35  PRO B O   
1272 C CB  . PRO B 18  ? 0.1282 0.1019 0.1031 0.0555  -0.0265 -0.0029 35  PRO B CB  
1273 C CG  . PRO B 18  ? 0.1308 0.1123 0.0997 0.0291  -0.0226 -0.0023 35  PRO B CG  
1274 C CD  . PRO B 18  ? 0.1195 0.0989 0.1021 0.0264  0.0092  0.0207  35  PRO B CD  
1275 N N   . ASP B 19  ? 0.0990 0.0888 0.0918 0.0206  -0.0015 0.0253  36  ASP B N   
1276 C CA  . ASP B 19  ? 0.1253 0.1197 0.0977 0.0048  0.0208  0.0217  36  ASP B CA  
1277 C C   . ASP B 19  ? 0.1129 0.1054 0.1003 -0.0179 0.0235  0.0232  36  ASP B C   
1278 O O   . ASP B 19  ? 0.1137 0.1279 0.1159 0.0073  0.0179  0.0133  36  ASP B O   
1279 C CB  . ASP B 19  ? 0.1351 0.1048 0.0965 -0.0199 0.0123  -0.0053 36  ASP B CB  
1280 C CG  . ASP B 19  ? 0.1454 0.1634 0.1005 0.0173  0.0157  0.0176  36  ASP B CG  
1281 O OD1 . ASP B 19  ? 0.1687 0.1685 0.1013 -0.0154 -0.0001 0.0024  36  ASP B OD1 
1282 O OD2 . ASP B 19  ? 0.1382 0.1305 0.1054 -0.0019 0.0144  0.0299  36  ASP B OD2 
1283 N N   . GLY B 20  ? 0.1206 0.1039 0.0879 0.0228  0.0304  0.0133  37  GLY B N   
1284 C CA  . GLY B 20  ? 0.0825 0.1509 0.0973 -0.0182 0.0137  0.0150  37  GLY B CA  
1285 C C   . GLY B 20  ? 0.1067 0.0903 0.0971 0.0130  0.0159  -0.0119 37  GLY B C   
1286 O O   . GLY B 20  ? 0.0829 0.0882 0.0972 0.0132  0.0110  0.0021  37  GLY B O   
1287 N N   . ILE B 21  ? 0.1363 0.0591 0.0985 0.0267  -0.0053 0.0207  38  ILE B N   
1288 C CA  . ILE B 21  ? 0.0718 0.1291 0.0980 0.0256  0.0099  0.0249  38  ILE B CA  
1289 C C   . ILE B 21  ? 0.1046 0.0963 0.0939 0.0444  0.0084  0.0075  38  ILE B C   
1290 O O   . ILE B 21  ? 0.1291 0.0940 0.0865 0.0319  0.0308  0.0241  38  ILE B O   
1291 C CB  . ILE B 21  ? 0.1449 0.1238 0.1031 0.0604  0.0019  0.0258  38  ILE B CB  
1292 C CG1 . ILE B 21  ? 0.1468 0.1553 0.1239 0.0685  0.0250  0.0411  38  ILE B CG1 
1293 C CG2 . ILE B 21  ? 0.1392 0.1217 0.0997 0.0204  -0.0094 0.0183  38  ILE B CG2 
1294 C CD1 . ILE B 21  ? 0.1690 0.1430 0.1311 0.0873  0.0370  0.0172  38  ILE B CD1 
1295 N N   . GLN B 22  ? 0.0988 0.1210 0.0969 -0.0009 -0.0024 0.0074  39  GLN B N   
1296 C CA  . GLN B 22  ? 0.0917 0.1247 0.0957 0.0266  0.0072  0.0070  39  GLN B CA  
1297 C C   . GLN B 22  ? 0.1117 0.1047 0.0899 0.0300  0.0101  0.0179  39  GLN B C   
1298 O O   . GLN B 22  ? 0.1247 0.1290 0.0916 0.0076  0.0033  -0.0091 39  GLN B O   
1299 C CB  . GLN B 22  ? 0.0784 0.1364 0.0956 0.0255  0.0062  -0.0105 39  GLN B CB  
1300 C CG  . GLN B 22  ? 0.1020 0.1420 0.1065 0.0532  -0.0127 -0.0187 39  GLN B CG  
1301 C CD  . GLN B 22  ? 0.1402 0.1435 0.1198 0.0654  -0.0124 -0.0180 39  GLN B CD  
1302 O OE1 . GLN B 22  ? 0.2000 0.1427 0.1287 0.0647  -0.0204 -0.0207 39  GLN B OE1 
1303 N NE2 . GLN B 22  ? 0.1537 0.1532 0.1240 0.0734  -0.0394 -0.0031 39  GLN B NE2 
1304 N N   . ARG B 23  ? 0.1205 0.1222 0.0957 0.0683  0.0104  0.0249  40  ARG B N   
1305 C CA  . ARG B 23  ? 0.1401 0.1334 0.0962 0.0234  0.0067  0.0214  40  ARG B CA  
1306 C C   . ARG B 23  ? 0.0791 0.1023 0.1045 0.0017  0.0146  -0.0013 40  ARG B C   
1307 O O   . ARG B 23  ? 0.1189 0.0876 0.1122 0.0093  -0.0028 -0.0004 40  ARG B O   
1308 C CB  . ARG B 23  ? 0.1604 0.0473 0.0943 0.0199  0.0096  0.0089  40  ARG B CB  
1309 C CG  . ARG B 23  ? 0.0858 0.1034 0.0887 0.0236  0.0104  0.0150  40  ARG B CG  
1310 C CD  . ARG B 23  ? 0.1533 0.1099 0.0864 0.0350  0.0183  0.0305  40  ARG B CD  
1311 N NE  . ARG B 23  ? 0.1746 0.0936 0.0848 0.0249  0.0066  0.0344  40  ARG B NE  
1312 C CZ  . ARG B 23  ? 0.1595 0.1043 0.0838 0.0332  0.0040  0.0250  40  ARG B CZ  
1313 N NH1 . ARG B 23  ? 0.1618 0.1089 0.0807 0.0157  -0.0145 0.0136  40  ARG B NH1 
1314 N NH2 . ARG B 23  ? 0.2277 0.1046 0.0834 0.0250  -0.0220 0.0003  40  ARG B NH2 
1315 N N   . GLN B 24  ? 0.1054 0.0895 0.1003 -0.0050 0.0153  -0.0068 41  GLN B N   
1316 C CA  . GLN B 24  ? 0.0812 0.1281 0.0991 0.0410  0.0113  0.0060  41  GLN B CA  
1317 C C   . GLN B 24  ? 0.1211 0.1084 0.1021 0.0400  0.0035  0.0047  41  GLN B C   
1318 O O   . GLN B 24  ? 0.0982 0.1242 0.1081 0.0119  0.0023  -0.0039 41  GLN B O   
1319 C CB  . GLN B 24  ? 0.0570 0.1406 0.1075 0.0215  0.0084  0.0189  41  GLN B CB  
1320 C CG  . GLN B 24  ? 0.0873 0.1684 0.1072 0.0106  -0.0047 -0.0049 41  GLN B CG  
1321 C CD  . GLN B 24  ? 0.1220 0.1549 0.1059 0.0138  -0.0063 -0.0080 41  GLN B CD  
1322 O OE1 . GLN B 24  ? 0.1376 0.1843 0.1096 0.0253  -0.0237 -0.0108 41  GLN B OE1 
1323 N NE2 . GLN B 24  ? 0.1843 0.1030 0.1047 0.0373  -0.0087 -0.0075 41  GLN B NE2 
1324 N N   . VAL B 25  ? 0.1087 0.1103 0.0909 0.0436  0.0142  0.0267  42  VAL B N   
1325 C CA  . VAL B 25  ? 0.0948 0.0680 0.0897 0.0169  0.0074  0.0388  42  VAL B CA  
1326 C C   . VAL B 25  ? 0.0648 0.0605 0.0839 -0.0079 0.0156  0.0143  42  VAL B C   
1327 O O   . VAL B 25  ? 0.0844 0.1116 0.0898 0.0211  -0.0073 0.0111  42  VAL B O   
1328 C CB  . VAL B 25  ? 0.1050 0.0999 0.1006 0.0235  -0.0072 0.0177  42  VAL B CB  
1329 C CG1 . VAL B 25  ? 0.1237 0.1152 0.1117 -0.0325 -0.0145 0.0447  42  VAL B CG1 
1330 C CG2 . VAL B 25  ? 0.1073 0.1566 0.0956 0.0696  0.0127  0.0339  42  VAL B CG2 
1331 N N   . VAL B 26  ? 0.0889 0.0823 0.0846 0.0098  0.0133  0.0159  43  VAL B N   
1332 C CA  . VAL B 26  ? 0.1114 0.0774 0.0809 0.0418  0.0216  0.0186  43  VAL B CA  
1333 C C   . VAL B 26  ? 0.0861 0.1402 0.0806 0.0018  0.0100  -0.0005 43  VAL B C   
1334 O O   . VAL B 26  ? 0.0716 0.1068 0.0829 0.0223  -0.0071 0.0157  43  VAL B O   
1335 C CB  . VAL B 26  ? 0.1304 0.0569 0.0869 0.0014  0.0068  0.0129  43  VAL B CB  
1336 C CG1 . VAL B 26  ? 0.1399 0.0911 0.0941 0.0107  -0.0154 -0.0061 43  VAL B CG1 
1337 C CG2 . VAL B 26  ? 0.1437 0.1034 0.0877 0.0537  0.0093  0.0044  43  VAL B CG2 
1338 N N   . GLY B 27  ? 0.0680 0.1146 0.0855 0.0426  0.0089  -0.0124 44  GLY B N   
1339 C CA  . GLY B 27  ? 0.1006 0.1038 0.0749 0.0382  0.0155  -0.0051 44  GLY B CA  
1340 C C   . GLY B 27  ? 0.1191 0.0789 0.0755 0.0204  0.0109  0.0132  44  GLY B C   
1341 O O   . GLY B 27  ? 0.0956 0.0961 0.0672 0.0039  -0.0088 -0.0007 44  GLY B O   
1342 N N   . GLU B 28  ? 0.1082 0.1196 0.0876 0.0341  -0.0121 -0.0137 45  GLU B N   
1343 C CA  . GLU B 28  ? 0.0750 0.1316 0.1009 0.0525  -0.0119 -0.0068 45  GLU B CA  
1344 C C   . GLU B 28  ? 0.0432 0.0990 0.0868 0.0284  0.0001  0.0145  45  GLU B C   
1345 O O   . GLU B 28  ? 0.0795 0.1536 0.0836 0.0332  -0.0142 0.0177  45  GLU B O   
1346 C CB  . GLU B 28  ? 0.0702 0.1285 0.1397 -0.0103 -0.0172 -0.0052 45  GLU B CB  
1347 C CG  . GLU B 28  ? 0.1374 0.1137 0.1810 -0.0302 -0.0066 0.0310  45  GLU B CG  
1348 C CD  . GLU B 28  ? 0.2409 0.1846 0.2182 -0.0930 -0.0239 0.0136  45  GLU B CD  
1349 O OE1 . GLU B 28  ? 0.3095 0.2320 0.2398 -0.0794 -0.0089 0.0214  45  GLU B OE1 
1350 O OE2 . GLU B 28  ? 0.2315 0.3246 0.2301 -0.0241 -0.0339 0.0211  45  GLU B OE2 
1351 N N   . ILE B 29  ? 0.0698 0.0860 0.0736 0.0250  -0.0001 0.0090  46  ILE B N   
1352 C CA  . ILE B 29  ? 0.1002 0.1170 0.0639 0.0002  0.0038  -0.0006 46  ILE B CA  
1353 C C   . ILE B 29  ? 0.0897 0.0910 0.0695 0.0226  -0.0041 0.0050  46  ILE B C   
1354 O O   . ILE B 29  ? 0.1104 0.1482 0.0729 0.0471  -0.0035 -0.0017 46  ILE B O   
1355 C CB  . ILE B 29  ? 0.1530 0.0850 0.0693 0.0218  0.0172  0.0085  46  ILE B CB  
1356 C CG1 . ILE B 29  ? 0.1118 0.1305 0.0724 0.0532  0.0291  0.0127  46  ILE B CG1 
1357 C CG2 . ILE B 29  ? 0.1382 0.1261 0.0806 0.0325  0.0052  -0.0122 46  ILE B CG2 
1358 C CD1 . ILE B 29  ? 0.1466 0.2049 0.0743 -0.0223 0.0214  0.0020  46  ILE B CD1 
1359 N N   . ILE B 30  ? 0.0926 0.0921 0.0762 0.0240  -0.0090 0.0061  47  ILE B N   
1360 C CA  . ILE B 30  ? 0.0567 0.0954 0.0733 -0.0065 -0.0173 -0.0135 47  ILE B CA  
1361 C C   . ILE B 30  ? 0.0639 0.0727 0.0734 0.0056  0.0058  0.0034  47  ILE B C   
1362 O O   . ILE B 30  ? 0.0940 0.0973 0.0804 0.0158  -0.0110 -0.0016 47  ILE B O   
1363 C CB  . ILE B 30  ? 0.0732 0.0843 0.0785 -0.0167 -0.0145 -0.0123 47  ILE B CB  
1364 C CG1 . ILE B 30  ? 0.1107 0.0819 0.0825 0.0105  0.0037  -0.0095 47  ILE B CG1 
1365 C CG2 . ILE B 30  ? 0.1144 0.1236 0.0784 -0.0134 -0.0162 0.0057  47  ILE B CG2 
1366 C CD1 . ILE B 30  ? 0.1333 0.0995 0.0857 -0.0102 -0.0031 -0.0093 47  ILE B CD1 
1367 N N   . SER B 31  ? 0.0887 0.0522 0.0787 0.0111  -0.0131 0.0059  48  SER B N   
1368 C CA  . SER B 31  ? 0.1004 0.0639 0.0798 0.0045  0.0116  0.0269  48  SER B CA  
1369 C C   . SER B 31  ? 0.0468 0.0451 0.0812 0.0099  0.0056  0.0154  48  SER B C   
1370 O O   . SER B 31  ? 0.1154 0.0976 0.0804 0.0159  -0.0297 0.0294  48  SER B O   
1371 C CB  . SER B 31  ? 0.1111 0.0910 0.0756 0.0074  0.0046  -0.0015 48  SER B CB  
1372 O OG  . SER B 31  ? 0.0739 0.1027 0.0768 0.0145  0.0055  0.0145  48  SER B OG  
1373 N N   . ARG B 32  ? 0.0747 0.0996 0.0754 0.0057  -0.0117 0.0116  49  ARG B N   
1374 C CA  . ARG B 32  ? 0.0970 0.0908 0.0790 0.0102  -0.0098 -0.0044 49  ARG B CA  
1375 C C   . ARG B 32  ? 0.1245 0.0883 0.0735 0.0097  -0.0059 0.0023  49  ARG B C   
1376 O O   . ARG B 32  ? 0.1038 0.0951 0.0801 0.0075  -0.0105 0.0095  49  ARG B O   
1377 C CB  . ARG B 32  ? 0.1404 0.1255 0.0899 0.0320  -0.0109 -0.0263 49  ARG B CB  
1378 C CG  . ARG B 32  ? 0.1790 0.0918 0.1129 -0.0004 -0.0178 -0.0225 49  ARG B CG  
1379 C CD  . ARG B 32  ? 0.2527 0.1590 0.1399 0.0259  0.0042  -0.0389 49  ARG B CD  
1380 N NE  . ARG B 32  ? 0.2520 0.1504 0.1569 -0.0018 0.0132  -0.0125 49  ARG B NE  
1381 C CZ  . ARG B 32  ? 0.1962 0.1292 0.1690 0.0231  0.0186  -0.0053 49  ARG B CZ  
1382 N NH1 . ARG B 32  ? 0.2126 0.1394 0.1708 0.0046  0.0151  0.0127  49  ARG B NH1 
1383 N NH2 . ARG B 32  ? 0.1697 0.1987 0.1810 0.0005  0.0170  0.0056  49  ARG B NH2 
1384 N N   . PHE B 33  ? 0.1212 0.0804 0.0751 -0.0028 -0.0110 -0.0031 50  PHE B N   
1385 C CA  . PHE B 33  ? 0.1329 0.0657 0.0805 -0.0115 -0.0108 0.0032  50  PHE B CA  
1386 C C   . PHE B 33  ? 0.1063 0.0692 0.0816 0.0141  -0.0241 0.0238  50  PHE B C   
1387 O O   . PHE B 33  ? 0.0939 0.0756 0.0796 -0.0072 -0.0167 0.0123  50  PHE B O   
1388 C CB  . PHE B 33  ? 0.1419 0.0824 0.0847 0.0434  -0.0140 0.0041  50  PHE B CB  
1389 C CG  . PHE B 33  ? 0.0735 0.1128 0.0830 0.0119  -0.0235 -0.0115 50  PHE B CG  
1390 C CD1 . PHE B 33  ? 0.1143 0.1494 0.0851 0.0392  -0.0069 -0.0126 50  PHE B CD1 
1391 C CD2 . PHE B 33  ? 0.1051 0.2146 0.0817 -0.0066 -0.0197 -0.0294 50  PHE B CD2 
1392 C CE1 . PHE B 33  ? 0.1449 0.1169 0.0869 0.0632  -0.0020 -0.0039 50  PHE B CE1 
1393 C CE2 . PHE B 33  ? 0.0771 0.2311 0.0901 -0.0255 -0.0143 -0.0171 50  PHE B CE2 
1394 C CZ  . PHE B 33  ? 0.1298 0.1294 0.0871 0.0325  0.0061  -0.0073 50  PHE B CZ  
1395 N N   . GLU B 34  ? 0.0817 0.1120 0.0793 -0.0198 -0.0094 0.0315  51  GLU B N   
1396 C CA  . GLU B 34  ? 0.0977 0.1116 0.0741 -0.0079 -0.0112 0.0258  51  GLU B CA  
1397 C C   . GLU B 34  ? 0.1263 0.0808 0.0822 0.0108  -0.0228 0.0082  51  GLU B C   
1398 O O   . GLU B 34  ? 0.0741 0.1264 0.0920 0.0084  -0.0386 0.0216  51  GLU B O   
1399 C CB  . GLU B 34  ? 0.1040 0.0843 0.0704 -0.0424 0.0048  0.0184  51  GLU B CB  
1400 C CG  . GLU B 34  ? 0.1607 0.0830 0.0727 0.0145  0.0027  0.0238  51  GLU B CG  
1401 C CD  . GLU B 34  ? 0.1472 0.1026 0.0808 -0.0130 0.0068  0.0097  51  GLU B CD  
1402 O OE1 . GLU B 34  ? 0.1006 0.1205 0.0882 -0.0043 0.0120  0.0149  51  GLU B OE1 
1403 O OE2 . GLU B 34  ? 0.1352 0.0948 0.0811 -0.0169 -0.0047 0.0115  51  GLU B OE2 
1404 N N   . LYS B 35  ? 0.0950 0.0892 0.0790 -0.0049 -0.0145 0.0254  52  LYS B N   
1405 C CA  . LYS B 35  ? 0.0999 0.1180 0.0881 0.0162  -0.0172 0.0296  52  LYS B CA  
1406 C C   . LYS B 35  ? 0.0838 0.0711 0.0880 0.0150  -0.0017 -0.0062 52  LYS B C   
1407 O O   . LYS B 35  ? 0.0969 0.1028 0.0963 0.0466  -0.0101 -0.0282 52  LYS B O   
1408 C CB  . LYS B 35  ? 0.1510 0.1104 0.1043 -0.0169 -0.0230 0.0354  52  LYS B CB  
1409 C CG  . LYS B 35  ? 0.2196 0.0955 0.1221 -0.0498 -0.0048 0.0349  52  LYS B CG  
1410 C CD  . LYS B 35  ? 0.2735 0.1033 0.1503 0.0110  -0.0173 0.0360  52  LYS B CD  
1411 C CE  . LYS B 35  ? 0.2266 0.2514 0.1685 -0.0024 -0.0262 0.0116  52  LYS B CE  
1412 N NZ  . LYS B 35  ? 0.2425 0.3479 0.1783 -0.0051 -0.0307 -0.0088 52  LYS B NZ  
1413 N N   . ARG B 36  ? 0.0875 0.0741 0.0829 0.0285  -0.0003 -0.0045 53  ARG B N   
1414 C CA  . ARG B 36  ? 0.1046 0.0869 0.0748 0.0404  -0.0167 0.0135  53  ARG B CA  
1415 C C   . ARG B 36  ? 0.1030 0.0802 0.0717 0.0157  -0.0060 0.0214  53  ARG B C   
1416 O O   . ARG B 36  ? 0.0823 0.1007 0.0771 0.0031  -0.0095 0.0121  53  ARG B O   
1417 C CB  . ARG B 36  ? 0.0525 0.1393 0.0725 0.0221  -0.0129 0.0091  53  ARG B CB  
1418 C CG  . ARG B 36  ? 0.1337 0.1323 0.0761 0.0046  -0.0032 0.0016  53  ARG B CG  
1419 C CD  . ARG B 36  ? 0.1240 0.0832 0.0851 0.0210  0.0046  0.0034  53  ARG B CD  
1420 N NE  . ARG B 36  ? 0.0763 0.1045 0.0847 0.0194  0.0044  0.0084  53  ARG B NE  
1421 C CZ  . ARG B 36  ? 0.0876 0.0708 0.0814 -0.0010 0.0119  0.0020  53  ARG B CZ  
1422 N NH1 . ARG B 36  ? 0.0871 0.1142 0.0818 0.0365  -0.0018 -0.0069 53  ARG B NH1 
1423 N NH2 . ARG B 36  ? 0.0969 0.1103 0.0765 0.0405  0.0120  -0.0090 53  ARG B NH2 
1424 N N   . GLY B 37  ? 0.1071 0.0741 0.0745 0.0039  -0.0108 0.0211  54  GLY B N   
1425 C CA  . GLY B 37  ? 0.0987 0.0913 0.0806 -0.0286 0.0055  0.0246  54  GLY B CA  
1426 C C   . GLY B 37  ? 0.1028 0.1029 0.0877 -0.0378 -0.0048 0.0136  54  GLY B C   
1427 O O   . GLY B 37  ? 0.0924 0.0943 0.1045 -0.0270 0.0000  -0.0033 54  GLY B O   
1428 N N   . TYR B 38  ? 0.0839 0.1042 0.0800 -0.0085 -0.0095 0.0148  55  TYR B N   
1429 C CA  . TYR B 38  ? 0.0861 0.0837 0.0738 -0.0050 -0.0065 0.0173  55  TYR B CA  
1430 C C   . TYR B 38  ? 0.1231 0.0818 0.0750 0.0134  -0.0127 -0.0014 55  TYR B C   
1431 O O   . TYR B 38  ? 0.1340 0.1370 0.0773 0.0222  -0.0296 0.0036  55  TYR B O   
1432 C CB  . TYR B 38  ? 0.1123 0.0891 0.0706 0.0016  -0.0074 0.0070  55  TYR B CB  
1433 C CG  . TYR B 38  ? 0.0667 0.1122 0.0646 -0.0231 0.0017  0.0019  55  TYR B CG  
1434 C CD1 . TYR B 38  ? 0.1080 0.1520 0.0619 0.0369  0.0096  0.0192  55  TYR B CD1 
1435 C CD2 . TYR B 38  ? 0.0959 0.1339 0.0646 -0.0071 0.0187  0.0045  55  TYR B CD2 
1436 C CE1 . TYR B 38  ? 0.1173 0.1347 0.0624 0.0221  -0.0001 0.0018  55  TYR B CE1 
1437 C CE2 . TYR B 38  ? 0.1301 0.1034 0.0670 -0.0090 0.0138  0.0005  55  TYR B CE2 
1438 C CZ  . TYR B 38  ? 0.1505 0.1027 0.0690 0.0331  0.0158  0.0064  55  TYR B CZ  
1439 O OH  . TYR B 38  ? 0.1330 0.1206 0.0774 -0.0119 0.0067  0.0004  55  TYR B OH  
1440 N N   . ARG B 39  ? 0.1019 0.0638 0.0791 -0.0015 -0.0223 0.0062  56  ARG B N   
1441 C CA  . ARG B 39  ? 0.1112 0.1069 0.0881 -0.0067 -0.0180 0.0051  56  ARG B CA  
1442 C C   . ARG B 39  ? 0.1203 0.1156 0.0897 -0.0165 -0.0192 -0.0034 56  ARG B C   
1443 O O   . ARG B 39  ? 0.1730 0.0619 0.0982 0.0081  -0.0301 -0.0075 56  ARG B O   
1444 C CB  . ARG B 39  ? 0.1495 0.0934 0.0992 0.0011  -0.0069 0.0175  56  ARG B CB  
1445 C CG  . ARG B 39  ? 0.1140 0.1452 0.0999 -0.0628 -0.0088 0.0178  56  ARG B CG  
1446 C CD  . ARG B 39  ? 0.1277 0.1067 0.0995 -0.0340 0.0040  0.0083  56  ARG B CD  
1447 N NE  . ARG B 39  ? 0.1451 0.1456 0.0983 -0.0491 0.0044  0.0125  56  ARG B NE  
1448 C CZ  . ARG B 39  ? 0.1655 0.1035 0.0959 -0.0727 -0.0114 0.0100  56  ARG B CZ  
1449 N NH1 . ARG B 39  ? 0.1772 0.1805 0.1043 -0.0448 -0.0233 0.0598  56  ARG B NH1 
1450 N NH2 . ARG B 39  ? 0.2375 0.1826 0.0960 -0.0719 0.0015  0.0060  56  ARG B NH2 
1451 N N   . ILE B 40  ? 0.0827 0.0812 0.0831 -0.0004 -0.0307 0.0067  57  ILE B N   
1452 C CA  . ILE B 40  ? 0.1354 0.1002 0.0904 0.0124  -0.0329 0.0125  57  ILE B CA  
1453 C C   . ILE B 40  ? 0.1139 0.0708 0.0915 -0.0060 -0.0044 0.0133  57  ILE B C   
1454 O O   . ILE B 40  ? 0.1300 0.0937 0.0873 -0.0017 0.0092  0.0092  57  ILE B O   
1455 C CB  . ILE B 40  ? 0.0984 0.1442 0.0936 -0.0254 -0.0261 0.0206  57  ILE B CB  
1456 C CG1 . ILE B 40  ? 0.1612 0.1567 0.0923 0.0248  -0.0258 -0.0140 57  ILE B CG1 
1457 C CG2 . ILE B 40  ? 0.1046 0.1462 0.1047 0.0031  -0.0213 0.0072  57  ILE B CG2 
1458 C CD1 . ILE B 40  ? 0.1126 0.1633 0.0951 -0.0113 -0.0119 -0.0115 57  ILE B CD1 
1459 N N   . ALA B 41  ? 0.1700 0.1018 0.0997 -0.0017 0.0072  -0.0072 58  ALA B N   
1460 C CA  . ALA B 41  ? 0.1617 0.0967 0.1080 -0.0038 -0.0048 -0.0034 58  ALA B CA  
1461 C C   . ALA B 41  ? 0.1442 0.1180 0.1157 -0.0015 -0.0079 0.0109  58  ALA B C   
1462 O O   . ALA B 41  ? 0.1563 0.0920 0.1237 -0.0056 -0.0168 0.0051  58  ALA B O   
1463 C CB  . ALA B 41  ? 0.1808 0.1232 0.1083 -0.0153 0.0065  -0.0027 58  ALA B CB  
1464 N N   . ALA B 42  ? 0.1099 0.0980 0.1180 -0.0144 -0.0144 0.0070  59  ALA B N   
1465 C CA  . ALA B 42  ? 0.1564 0.0809 0.1259 0.0316  -0.0090 0.0060  59  ALA B CA  
1466 C C   . ALA B 42  ? 0.1087 0.1185 0.1191 0.0044  0.0078  0.0042  59  ALA B C   
1467 O O   . ALA B 42  ? 0.1076 0.0890 0.1153 -0.0124 -0.0093 0.0065  59  ALA B O   
1468 C CB  . ALA B 42  ? 0.2022 0.1087 0.1358 0.0305  -0.0036 0.0206  59  ALA B CB  
1469 N N   . MET B 43  ? 0.1100 0.1095 0.1202 0.0226  -0.0137 -0.0114 60  MET B N   
1470 C CA  . MET B 43  ? 0.0916 0.1235 0.1256 -0.0238 -0.0152 -0.0223 60  MET B CA  
1471 C C   . MET B 43  ? 0.0874 0.1077 0.1255 0.0170  -0.0283 0.0082  60  MET B C   
1472 O O   . MET B 43  ? 0.0986 0.1523 0.1273 -0.0132 -0.0103 0.0613  60  MET B O   
1473 C CB  . MET B 43  ? 0.1212 0.1463 0.1339 -0.0719 0.0119  -0.0231 60  MET B CB  
1474 C CG  . MET B 43  ? 0.1445 0.1574 0.1329 0.0448  0.0145  -0.0185 60  MET B CG  
1475 S SD  . MET B 43  ? 0.1700 0.1515 0.1321 -0.0369 0.0179  0.0044  60  MET B SD  
1476 C CE  . MET B 43  ? 0.1648 0.1487 0.1316 0.0031  -0.0017 0.0085  60  MET B CE  
1477 N N   . LYS B 44  ? 0.0672 0.1434 0.1318 0.0263  -0.0108 0.0193  61  LYS B N   
1478 C CA  . LYS B 44  ? 0.1466 0.1211 0.1442 0.0021  -0.0251 0.0359  61  LYS B CA  
1479 C C   . LYS B 44  ? 0.1008 0.0981 0.1242 -0.0166 -0.0215 0.0181  61  LYS B C   
1480 O O   . LYS B 44  ? 0.1471 0.1483 0.1233 -0.0023 -0.0082 0.0347  61  LYS B O   
1481 C CB  . LYS B 44  ? 0.2461 0.0851 0.1813 0.0168  -0.0327 0.0401  61  LYS B CB  
1482 C CG  . LYS B 44  ? 0.3783 0.1595 0.2031 0.0764  -0.0164 0.0019  61  LYS B CG  
1483 C CD  . LYS B 44  ? 0.4548 0.2016 0.2196 0.0432  -0.0179 -0.0263 61  LYS B CD  
1484 C CE  . LYS B 44  ? 0.4690 0.1605 0.2300 0.0309  -0.0352 -0.0423 61  LYS B CE  
1485 N NZ  . LYS B 44  ? 0.5111 0.1964 0.2371 0.0131  -0.0348 -0.0384 61  LYS B NZ  
1486 N N   . LEU B 45  ? 0.0949 0.0785 0.1055 0.0361  0.0040  0.0102  62  LEU B N   
1487 C CA  . LEU B 45  ? 0.1086 0.0703 0.0997 0.0318  0.0001  -0.0001 62  LEU B CA  
1488 C C   . LEU B 45  ? 0.1146 0.1226 0.0977 0.0080  0.0217  0.0262  62  LEU B C   
1489 O O   . LEU B 45  ? 0.1537 0.1011 0.1035 0.0208  0.0159  0.0254  62  LEU B O   
1490 C CB  . LEU B 45  ? 0.1258 0.1017 0.1059 -0.0200 0.0179  0.0024  62  LEU B CB  
1491 C CG  . LEU B 45  ? 0.1857 0.0716 0.1206 0.0120  -0.0068 -0.0259 62  LEU B CG  
1492 C CD1 . LEU B 45  ? 0.1912 0.1163 0.1295 0.0041  0.0009  -0.0124 62  LEU B CD1 
1493 C CD2 . LEU B 45  ? 0.1571 0.1027 0.1266 0.0006  -0.0202 -0.0156 62  LEU B CD2 
1494 N N   . THR B 46  ? 0.1097 0.0934 0.0956 0.0448  0.0188  0.0130  63  THR B N   
1495 C CA  . THR B 46  ? 0.1272 0.0826 0.1161 0.0407  0.0174  0.0114  63  THR B CA  
1496 C C   . THR B 46  ? 0.1187 0.0716 0.1280 0.0109  0.0063  0.0294  63  THR B C   
1497 O O   . THR B 46  ? 0.1120 0.1357 0.1405 0.0035  0.0040  0.0395  63  THR B O   
1498 C CB  . THR B 46  ? 0.2028 0.1454 0.1264 0.0622  0.0020  -0.0097 63  THR B CB  
1499 O OG1 . THR B 46  ? 0.2245 0.1191 0.1383 0.0504  -0.0192 -0.0097 63  THR B OG1 
1500 C CG2 . THR B 46  ? 0.2363 0.1281 0.1326 0.0922  -0.0222 -0.0053 63  THR B CG2 
1501 N N   . ILE B 47  ? 0.1074 0.1051 0.1382 0.0579  -0.0056 0.0052  64  ILE B N   
1502 C CA  . ILE B 47  ? 0.0954 0.1049 0.1417 0.0578  0.0053  -0.0091 64  ILE B CA  
1503 C C   . ILE B 47  ? 0.1292 0.1110 0.1456 0.0192  0.0094  -0.0090 64  ILE B C   
1504 O O   . ILE B 47  ? 0.1546 0.0925 0.1442 0.0324  0.0308  -0.0107 64  ILE B O   
1505 C CB  . ILE B 47  ? 0.1060 0.0765 0.1368 0.0404  -0.0006 -0.0072 64  ILE B CB  
1506 C CG1 . ILE B 47  ? 0.1524 0.1269 0.1280 0.0505  -0.0182 0.0141  64  ILE B CG1 
1507 C CG2 . ILE B 47  ? 0.0990 0.1418 0.1480 0.0674  -0.0064 -0.0059 64  ILE B CG2 
1508 C CD1 . ILE B 47  ? 0.2144 0.1371 0.1303 0.0779  -0.0127 0.0007  64  ILE B CD1 
1509 N N   . ALA B 48  ? 0.1536 0.0952 0.1552 0.0461  0.0034  0.0039  65  ALA B N   
1510 C CA  . ALA B 48  ? 0.1311 0.0723 0.1612 0.0519  0.0023  -0.0040 65  ALA B CA  
1511 C C   . ALA B 48  ? 0.1057 0.0626 0.1696 0.0099  0.0132  0.0082  65  ALA B C   
1512 O O   . ALA B 48  ? 0.0922 0.1123 0.1723 0.0098  0.0195  -0.0127 65  ALA B O   
1513 C CB  . ALA B 48  ? 0.1734 0.0574 0.1600 0.0160  -0.0270 0.0009  65  ALA B CB  
1514 N N   . THR B 49  ? 0.1143 0.0892 0.1741 0.0053  -0.0051 -0.0055 66  THR B N   
1515 C CA  . THR B 49  ? 0.1317 0.1187 0.1762 0.0533  0.0005  -0.0204 66  THR B CA  
1516 C C   . THR B 49  ? 0.1225 0.0903 0.1699 0.0437  -0.0085 0.0046  66  THR B C   
1517 O O   . THR B 49  ? 0.1719 0.0901 0.1651 0.0594  -0.0224 0.0164  66  THR B O   
1518 C CB  . THR B 49  ? 0.1777 0.1076 0.1874 -0.0043 0.0163  -0.0086 66  THR B CB  
1519 O OG1 . THR B 49  ? 0.2673 0.1100 0.1992 0.0141  0.0149  0.0088  66  THR B OG1 
1520 C CG2 . THR B 49  ? 0.1588 0.1877 0.1871 0.0464  0.0384  0.0228  66  THR B CG2 
1521 N N   . PRO B 50  ? 0.1956 0.1493 0.1701 0.0964  -0.0002 0.0230  67  PRO B N   
1522 C CA  . PRO B 50  ? 0.1825 0.1067 0.1698 0.0279  0.0227  0.0296  67  PRO B CA  
1523 C C   . PRO B 50  ? 0.2011 0.1123 0.1546 0.0390  0.0189  0.0085  67  PRO B C   
1524 O O   . PRO B 50  ? 0.2350 0.1679 0.1427 0.0289  -0.0168 -0.0106 67  PRO B O   
1525 C CB  . PRO B 50  ? 0.1934 0.1855 0.1737 0.0812  0.0350  0.0570  67  PRO B CB  
1526 C CG  . PRO B 50  ? 0.2137 0.1870 0.1745 0.0629  0.0329  0.0411  67  PRO B CG  
1527 C CD  . PRO B 50  ? 0.1968 0.1505 0.1754 0.0258  0.0146  0.0281  67  PRO B CD  
1528 N N   . ALA B 51  ? 0.1922 0.1300 0.1511 0.0495  0.0277  -0.0024 68  ALA B N   
1529 C CA  . ALA B 51  ? 0.2209 0.1181 0.1570 0.0806  0.0267  0.0047  68  ALA B CA  
1530 C C   . ALA B 51  ? 0.2137 0.1634 0.1551 0.0784  0.0311  0.0201  68  ALA B C   
1531 O O   . ALA B 51  ? 0.2382 0.1852 0.1625 0.0961  0.0085  0.0287  68  ALA B O   
1532 C CB  . ALA B 51  ? 0.2422 0.0763 0.1589 0.0030  0.0003  -0.0043 68  ALA B CB  
1533 N N   . ILE B 52  ? 0.1512 0.1240 0.1481 0.0375  0.0271  0.0216  69  ILE B N   
1534 C CA  . ILE B 52  ? 0.1772 0.0835 0.1538 0.0174  0.0039  -0.0017 69  ILE B CA  
1535 C C   . ILE B 52  ? 0.1712 0.0962 0.1544 0.0414  -0.0160 -0.0074 69  ILE B C   
1536 O O   . ILE B 52  ? 0.2169 0.1097 0.1550 0.0761  -0.0377 -0.0251 69  ILE B O   
1537 C CB  . ILE B 52  ? 0.1815 0.1046 0.1603 0.0534  0.0202  -0.0038 69  ILE B CB  
1538 C CG1 . ILE B 52  ? 0.2509 0.1584 0.1648 0.0980  -0.0024 -0.0054 69  ILE B CG1 
1539 C CG2 . ILE B 52  ? 0.2478 0.1441 0.1623 0.0249  0.0163  0.0124  69  ILE B CG2 
1540 C CD1 . ILE B 52  ? 0.2647 0.2083 0.1756 0.0685  0.0026  -0.0089 69  ILE B CD1 
1541 N N   . LEU B 53  ? 0.1633 0.0640 0.1472 0.0368  -0.0231 0.0137  70  LEU B N   
1542 C CA  . LEU B 53  ? 0.2574 0.0930 0.1531 0.0411  -0.0173 0.0154  70  LEU B CA  
1543 C C   . LEU B 53  ? 0.2367 0.0790 0.1569 0.0483  -0.0217 -0.0025 70  LEU B C   
1544 O O   . LEU B 53  ? 0.2998 0.1157 0.1593 0.0515  -0.0309 0.0067  70  LEU B O   
1545 C CB  . LEU B 53  ? 0.2074 0.1169 0.1546 -0.0048 -0.0149 0.0174  70  LEU B CB  
1546 C CG  . LEU B 53  ? 0.2163 0.0741 0.1575 0.0473  0.0072  0.0084  70  LEU B CG  
1547 C CD1 . LEU B 53  ? 0.2333 0.0627 0.1538 0.0071  0.0299  0.0017  70  LEU B CD1 
1548 C CD2 . LEU B 53  ? 0.2143 0.0759 0.1647 0.0309  0.0014  0.0045  70  LEU B CD2 
1549 N N   . GLU B 54  ? 0.3308 0.1550 0.1589 0.1057  -0.0202 -0.0243 71  GLU B N   
1550 C CA  . GLU B 54  ? 0.3862 0.1698 0.1744 0.1179  -0.0296 -0.0323 71  GLU B CA  
1551 C C   . GLU B 54  ? 0.3736 0.1149 0.1731 0.0335  -0.0278 -0.0286 71  GLU B C   
1552 O O   . GLU B 54  ? 0.3775 0.2061 0.1611 0.0422  -0.0266 -0.0345 71  GLU B O   
1553 C CB  . GLU B 54  ? 0.5159 0.2981 0.2031 0.1951  -0.0342 -0.0529 71  GLU B CB  
1554 C CG  . GLU B 54  ? 0.6246 0.4035 0.2346 0.2595  -0.0487 -0.0625 71  GLU B CG  
1555 C CD  . GLU B 54  ? 0.7603 0.5766 0.2679 0.3104  -0.0611 -0.0705 71  GLU B CD  
1556 O OE1 . GLU B 54  ? 0.7653 0.5969 0.2866 0.3548  -0.0632 -0.0764 71  GLU B OE1 
1557 O OE2 . GLU B 54  ? 0.8461 0.6701 0.2875 0.3307  -0.0609 -0.0567 71  GLU B OE2 
1558 N N   . GLU B 55  ? 0.3728 0.1371 0.1854 0.0401  -0.0508 -0.0140 72  GLU B N   
1559 C CA  A GLU B 55  ? 0.3808 0.1657 0.1922 0.0042  -0.0690 -0.0208 72  GLU B CA  
1560 C CA  B GLU B 55  ? 0.3557 0.1292 0.1930 0.0177  -0.0728 -0.0178 72  GLU B CA  
1561 C C   . GLU B 55  ? 0.3646 0.1447 0.1895 0.0216  -0.0871 -0.0275 72  GLU B C   
1562 O O   . GLU B 55  ? 0.3386 0.1695 0.1896 0.0021  -0.1083 -0.0167 72  GLU B O   
1563 C CB  A GLU B 55  ? 0.4477 0.2275 0.2043 0.0085  -0.0686 -0.0041 72  GLU B CB  
1564 C CB  B GLU B 55  ? 0.3614 0.1135 0.2060 0.0407  -0.0794 0.0095  72  GLU B CB  
1565 C CG  A GLU B 55  ? 0.5591 0.3920 0.2159 0.0383  -0.0586 -0.0012 72  GLU B CG  
1566 C CG  B GLU B 55  ? 0.4683 0.2236 0.2204 0.0831  -0.0802 0.0131  72  GLU B CG  
1567 C CD  A GLU B 55  ? 0.6483 0.4623 0.2223 0.0379  -0.0546 0.0020  72  GLU B CD  
1568 C CD  B GLU B 55  ? 0.5249 0.1797 0.2283 0.0683  -0.0817 0.0090  72  GLU B CD  
1569 O OE1 A GLU B 55  ? 0.6955 0.5303 0.2264 0.0742  -0.0627 0.0116  72  GLU B OE1 
1570 O OE1 B GLU B 55  ? 0.5236 0.1961 0.2347 0.1153  -0.0753 0.0117  72  GLU B OE1 
1571 O OE2 A GLU B 55  ? 0.6651 0.4899 0.2241 0.0280  -0.0358 0.0111  72  GLU B OE2 
1572 O OE2 B GLU B 55  ? 0.4890 0.1293 0.2330 0.0088  -0.0706 0.0068  72  GLU B OE2 
1573 N N   . HIS B 56  ? 0.2766 0.1177 0.1794 0.0742  -0.0786 -0.0281 73  HIS B N   
1574 C CA  . HIS B 56  ? 0.2933 0.1258 0.1845 0.0790  -0.0637 -0.0052 73  HIS B CA  
1575 C C   . HIS B 56  ? 0.3270 0.1412 0.1787 0.0557  -0.0621 -0.0018 73  HIS B C   
1576 O O   . HIS B 56  ? 0.2957 0.1971 0.1714 -0.0155 -0.0752 -0.0225 73  HIS B O   
1577 C CB  . HIS B 56  ? 0.2735 0.0914 0.1953 0.0405  -0.0574 0.0090  73  HIS B CB  
1578 C CG  . HIS B 56  ? 0.2472 0.0841 0.2077 0.0384  -0.0539 0.0025  73  HIS B CG  
1579 N ND1 . HIS B 56  ? 0.2940 0.1413 0.2149 0.0872  -0.0761 -0.0022 73  HIS B ND1 
1580 C CD2 . HIS B 56  ? 0.2950 0.1337 0.2238 0.0787  -0.0391 0.0141  73  HIS B CD2 
1581 C CE1 . HIS B 56  ? 0.3133 0.1534 0.2208 0.1047  -0.0458 0.0086  73  HIS B CE1 
1582 N NE2 . HIS B 56  ? 0.3293 0.1811 0.2281 0.1258  -0.0361 0.0121  73  HIS B NE2 
1583 N N   . TYR B 57  ? 0.3086 0.1473 0.1764 0.0521  -0.0699 -0.0085 74  TYR B N   
1584 C CA  . TYR B 57  ? 0.3825 0.1566 0.1806 0.0347  -0.0433 -0.0078 74  TYR B CA  
1585 C C   . TYR B 57  ? 0.4109 0.1494 0.1831 0.0497  -0.0431 -0.0088 74  TYR B C   
1586 O O   . TYR B 57  ? 0.4162 0.1814 0.1844 0.0497  -0.0117 0.0027  74  TYR B O   
1587 C CB  . TYR B 57  ? 0.4234 0.1623 0.1768 0.0352  -0.0303 0.0114  74  TYR B CB  
1588 C CG  . TYR B 57  ? 0.4353 0.1621 0.1743 0.0325  -0.0329 0.0207  74  TYR B CG  
1589 C CD1 . TYR B 57  ? 0.4270 0.1180 0.1742 0.0207  -0.0321 0.0188  74  TYR B CD1 
1590 C CD2 . TYR B 57  ? 0.4830 0.1650 0.1761 0.0240  -0.0366 0.0343  74  TYR B CD2 
1591 C CE1 . TYR B 57  ? 0.4818 0.1529 0.1715 0.0444  -0.0365 0.0054  74  TYR B CE1 
1592 C CE2 . TYR B 57  ? 0.5135 0.1608 0.1774 0.0372  -0.0427 0.0237  74  TYR B CE2 
1593 C CZ  . TYR B 57  ? 0.5155 0.1680 0.1721 0.0614  -0.0421 0.0144  74  TYR B CZ  
1594 O OH  . TYR B 57  ? 0.4994 0.1507 0.1646 0.0786  -0.0425 -0.0164 74  TYR B OH  
1595 N N   . ALA B 58  ? 0.4540 0.1426 0.1909 -0.0071 -0.0552 -0.0386 75  ALA B N   
1596 C CA  . ALA B 58  ? 0.5713 0.1882 0.1959 0.0317  -0.0239 -0.0426 75  ALA B CA  
1597 C C   . ALA B 58  ? 0.6079 0.2240 0.1987 0.0355  -0.0153 -0.0396 75  ALA B C   
1598 O O   . ALA B 58  ? 0.6547 0.2557 0.1970 0.0435  -0.0020 -0.0379 75  ALA B O   
1599 C CB  . ALA B 58  ? 0.5893 0.2742 0.2014 0.0017  -0.0100 -0.0322 75  ALA B CB  
1600 N N   . GLU B 59  ? 0.5857 0.2642 0.2033 0.0749  -0.0017 -0.0148 76  GLU B N   
1601 C CA  . GLU B 59  ? 0.6240 0.2972 0.2140 0.0445  0.0175  0.0149  76  GLU B CA  
1602 C C   . GLU B 59  ? 0.6460 0.3004 0.2151 0.0524  0.0258  0.0185  76  GLU B C   
1603 O O   . GLU B 59  ? 0.6516 0.3338 0.2122 0.0573  0.0208  0.0481  76  GLU B O   
1604 C CB  . GLU B 59  ? 0.6323 0.3090 0.2266 -0.0295 0.0195  0.0401  76  GLU B CB  
1605 C CG  . GLU B 59  ? 0.6511 0.3846 0.2399 0.0286  0.0244  0.0500  76  GLU B CG  
1606 C CD  . GLU B 59  ? 0.6858 0.4858 0.2502 0.0728  0.0333  0.0462  76  GLU B CD  
1607 O OE1 . GLU B 59  ? 0.6892 0.5772 0.2541 0.1554  0.0351  0.0500  76  GLU B OE1 
1608 O OE2 . GLU B 59  ? 0.6987 0.4923 0.2559 0.0503  0.0254  0.0379  76  GLU B OE2 
1609 N N   . HIS B 60  ? 0.6513 0.2662 0.2218 0.0715  0.0318  -0.0027 77  HIS B N   
1610 C CA  . HIS B 60  ? 0.6437 0.2417 0.2304 0.0598  0.0494  -0.0082 77  HIS B CA  
1611 C C   . HIS B 60  ? 0.6585 0.2330 0.2366 0.0938  0.0324  -0.0276 77  HIS B C   
1612 O O   . HIS B 60  ? 0.6313 0.2238 0.2372 0.1340  0.0303  -0.0228 77  HIS B O   
1613 C CB  . HIS B 60  ? 0.6723 0.2556 0.2388 0.0471  0.0790  0.0001  77  HIS B CB  
1614 C CG  . HIS B 60  ? 0.7139 0.2611 0.2472 0.0635  0.0892  0.0010  77  HIS B CG  
1615 N ND1 . HIS B 60  ? 0.7351 0.2834 0.2538 0.0549  0.1007  0.0010  77  HIS B ND1 
1616 C CD2 . HIS B 60  ? 0.7528 0.3300 0.2517 0.0860  0.0901  0.0006  77  HIS B CD2 
1617 C CE1 . HIS B 60  ? 0.7499 0.3274 0.2562 0.0557  0.0895  0.0065  77  HIS B CE1 
1618 N NE2 . HIS B 60  ? 0.7509 0.3614 0.2551 0.0856  0.0914  -0.0024 77  HIS B NE2 
1619 N N   . LYS B 61  ? 0.6914 0.2741 0.2454 0.0652  0.0260  -0.0441 78  LYS B N   
1620 C CA  . LYS B 61  ? 0.7613 0.2612 0.2577 0.0452  0.0246  -0.0586 78  LYS B CA  
1621 C C   . LYS B 61  ? 0.7349 0.2628 0.2555 0.0372  0.0379  -0.0674 78  LYS B C   
1622 O O   . LYS B 61  ? 0.7465 0.3115 0.2466 0.0392  0.0203  -0.0796 78  LYS B O   
1623 C CB  . LYS B 61  ? 0.8308 0.3124 0.2730 0.0354  0.0058  -0.0651 78  LYS B CB  
1624 C CG  . LYS B 61  ? 0.8922 0.3640 0.2874 0.0643  -0.0084 -0.0634 78  LYS B CG  
1625 C CD  . LYS B 61  ? 0.9485 0.3583 0.2992 0.1041  -0.0149 -0.0673 78  LYS B CD  
1626 C CE  . LYS B 61  ? 0.9874 0.4175 0.3092 0.1655  -0.0191 -0.0693 78  LYS B CE  
1627 N NZ  . LYS B 61  ? 0.9970 0.4713 0.3153 0.2147  -0.0214 -0.0782 78  LYS B NZ  
1628 N N   . GLY B 62  ? 0.7265 0.2774 0.2572 0.0496  0.0674  -0.0673 79  GLY B N   
1629 C CA  . GLY B 62  ? 0.7353 0.3219 0.2597 0.0601  0.0902  -0.0563 79  GLY B CA  
1630 C C   . GLY B 62  ? 0.7419 0.3700 0.2626 0.1034  0.1116  -0.0486 79  GLY B C   
1631 O O   . GLY B 62  ? 0.7662 0.3843 0.2698 0.1118  0.1083  -0.0456 79  GLY B O   
1632 N N   . LYS B 63  ? 0.7196 0.3774 0.2597 0.0971  0.1336  -0.0467 80  LYS B N   
1633 C CA  . LYS B 63  ? 0.6874 0.3708 0.2542 0.0628  0.1586  -0.0159 80  LYS B CA  
1634 C C   . LYS B 63  ? 0.6538 0.4359 0.2540 0.0479  0.1755  -0.0204 80  LYS B C   
1635 O O   . LYS B 63  ? 0.6744 0.3889 0.2659 0.1168  0.1534  -0.0314 80  LYS B O   
1636 C CB  . LYS B 63  ? 0.7076 0.3513 0.2557 0.1021  0.1475  -0.0022 80  LYS B CB  
1637 C CG  . LYS B 63  ? 0.7003 0.3863 0.2561 0.1156  0.1499  0.0077  80  LYS B CG  
1638 C CD  . LYS B 63  ? 0.6556 0.4150 0.2572 0.0467  0.1618  0.0226  80  LYS B CD  
1639 C CE  . LYS B 63  ? 0.6490 0.4220 0.2602 0.0461  0.1664  0.0401  80  LYS B CE  
1640 N NZ  . LYS B 63  ? 0.6639 0.4102 0.2625 0.0378  0.1630  0.0498  80  LYS B NZ  
1641 N N   . PRO B 64  ? 0.5965 0.5291 0.2577 -0.0166 0.1895  -0.0182 81  PRO B N   
1642 C CA  . PRO B 64  ? 0.5382 0.5823 0.2617 -0.0132 0.1912  -0.0296 81  PRO B CA  
1643 C C   . PRO B 64  ? 0.5036 0.5433 0.2603 -0.0243 0.1806  -0.0568 81  PRO B C   
1644 O O   . PRO B 64  ? 0.4635 0.5178 0.2626 -0.0475 0.1676  -0.0820 81  PRO B O   
1645 C CB  . PRO B 64  ? 0.5785 0.6662 0.2599 0.0103  0.1918  -0.0225 81  PRO B CB  
1646 C CG  . PRO B 64  ? 0.6022 0.6833 0.2613 0.0098  0.1925  -0.0167 81  PRO B CG  
1647 C CD  . PRO B 64  ? 0.6238 0.6288 0.2579 0.0046  0.1884  -0.0189 81  PRO B CD  
1648 N N   . PHE B 65  ? 0.5244 0.4665 0.2633 -0.0185 0.1733  -0.0582 82  PHE B N   
1649 C CA  . PHE B 65  ? 0.4846 0.4074 0.2643 -0.0292 0.1747  -0.0420 82  PHE B CA  
1650 C C   . PHE B 65  ? 0.4713 0.3619 0.2582 -0.0090 0.1716  -0.0347 82  PHE B C   
1651 O O   . PHE B 65  ? 0.4290 0.3620 0.2597 -0.0596 0.1811  -0.0077 82  PHE B O   
1652 C CB  . PHE B 65  ? 0.5017 0.3926 0.2711 -0.0377 0.1478  -0.0527 82  PHE B CB  
1653 C CG  . PHE B 65  ? 0.5106 0.4034 0.2777 -0.0134 0.1218  -0.0674 82  PHE B CG  
1654 C CD1 . PHE B 65  ? 0.4905 0.3581 0.2772 -0.0046 0.1191  -0.0773 82  PHE B CD1 
1655 C CD2 . PHE B 65  ? 0.5212 0.4223 0.2830 0.0008  0.1004  -0.0779 82  PHE B CD2 
1656 C CE1 . PHE B 65  ? 0.4857 0.3422 0.2795 0.0005  0.1078  -0.0827 82  PHE B CE1 
1657 C CE2 . PHE B 65  ? 0.5194 0.4296 0.2851 0.0173  0.0960  -0.0785 82  PHE B CE2 
1658 C CZ  . PHE B 65  ? 0.4916 0.3851 0.2840 -0.0006 0.0997  -0.0787 82  PHE B CZ  
1659 N N   . LEU B 66  ? 0.4520 0.2912 0.2578 0.0588  0.1636  -0.0381 83  LEU B N   
1660 C CA  . LEU B 66  ? 0.4330 0.2468 0.2560 0.0486  0.1585  -0.0381 83  LEU B CA  
1661 C C   . LEU B 66  ? 0.4198 0.2510 0.2545 0.0578  0.1557  -0.0345 83  LEU B C   
1662 O O   . LEU B 66  ? 0.3700 0.1816 0.2528 0.0046  0.1629  -0.0334 83  LEU B O   
1663 C CB  . LEU B 66  ? 0.4462 0.2479 0.2610 0.0150  0.1524  -0.0207 83  LEU B CB  
1664 C CG  . LEU B 66  ? 0.4630 0.2694 0.2706 0.0390  0.1357  -0.0437 83  LEU B CG  
1665 C CD1 . LEU B 66  ? 0.4523 0.3071 0.2751 0.0430  0.1262  -0.0586 83  LEU B CD1 
1666 C CD2 . LEU B 66  ? 0.5023 0.2362 0.2746 0.0134  0.1110  -0.0498 83  LEU B CD2 
1667 N N   . PRO B 67  ? 0.3600 0.3243 0.2551 0.0496  0.1621  -0.0329 84  PRO B N   
1668 C CA  . PRO B 67  ? 0.3910 0.3877 0.2562 0.1027  0.1481  -0.0310 84  PRO B CA  
1669 C C   . PRO B 67  ? 0.3589 0.3394 0.2500 0.0769  0.1507  -0.0303 84  PRO B C   
1670 O O   . PRO B 67  ? 0.3728 0.3371 0.2475 0.0773  0.1254  -0.0339 84  PRO B O   
1671 C CB  . PRO B 67  ? 0.3885 0.4291 0.2576 0.0985  0.1451  -0.0292 84  PRO B CB  
1672 C CG  . PRO B 67  ? 0.3919 0.4438 0.2586 0.0987  0.1496  -0.0391 84  PRO B CG  
1673 C CD  . PRO B 67  ? 0.3975 0.4024 0.2583 0.0803  0.1609  -0.0335 84  PRO B CD  
1674 N N   . GLY B 68  ? 0.3713 0.3173 0.2512 0.0951  0.1360  -0.0412 85  GLY B N   
1675 C CA  . GLY B 68  ? 0.3352 0.2687 0.2412 -0.0023 0.1513  -0.0478 85  GLY B CA  
1676 C C   . GLY B 68  ? 0.3618 0.2048 0.2375 0.0064  0.1536  -0.0316 85  GLY B C   
1677 O O   . GLY B 68  ? 0.4267 0.2383 0.2279 -0.0523 0.1546  -0.0533 85  GLY B O   
1678 N N   . LEU B 69  ? 0.3418 0.1871 0.2425 0.0259  0.1505  -0.0057 86  LEU B N   
1679 C CA  . LEU B 69  ? 0.3541 0.1434 0.2483 0.0033  0.1332  -0.0012 86  LEU B CA  
1680 C C   . LEU B 69  ? 0.3935 0.1556 0.2476 0.0077  0.1385  -0.0045 86  LEU B C   
1681 O O   . LEU B 69  ? 0.3764 0.1171 0.2446 0.0040  0.1248  -0.0117 86  LEU B O   
1682 C CB  . LEU B 69  ? 0.3268 0.1611 0.2580 0.0531  0.1065  -0.0024 86  LEU B CB  
1683 C CG  . LEU B 69  ? 0.3950 0.2492 0.2665 0.0946  0.0823  -0.0157 86  LEU B CG  
1684 C CD1 . LEU B 69  ? 0.4357 0.2978 0.2706 0.1205  0.0680  -0.0070 86  LEU B CD1 
1685 C CD2 . LEU B 69  ? 0.3736 0.3259 0.2692 0.1073  0.0859  -0.0065 86  LEU B CD2 
1686 N N   . ILE B 70  ? 0.4273 0.1847 0.2480 0.0641  0.1546  -0.0023 87  ILE B N   
1687 C CA  A ILE B 70  ? 0.4129 0.1431 0.2491 0.0262  0.1611  -0.0025 87  ILE B CA  
1688 C CA  B ILE B 70  ? 0.4024 0.1881 0.2492 0.0273  0.1568  -0.0098 87  ILE B CA  
1689 C C   . ILE B 70  ? 0.3420 0.1661 0.2491 -0.0236 0.1624  -0.0160 87  ILE B C   
1690 O O   . ILE B 70  ? 0.2908 0.2090 0.2472 0.0090  0.1561  -0.0162 87  ILE B O   
1691 C CB  A ILE B 70  ? 0.4848 0.1878 0.2505 0.0454  0.1568  0.0067  87  ILE B CB  
1692 C CB  B ILE B 70  ? 0.4337 0.2331 0.2510 0.0268  0.1493  -0.0123 87  ILE B CB  
1693 C CG1 A ILE B 70  ? 0.5201 0.2327 0.2538 0.0613  0.1602  -0.0054 87  ILE B CG1 
1694 C CG1 B ILE B 70  ? 0.4412 0.2700 0.2526 0.0205  0.1457  -0.0184 87  ILE B CG1 
1695 C CG2 A ILE B 70  ? 0.5017 0.2159 0.2503 0.0208  0.1521  0.0175  87  ILE B CG2 
1696 C CG2 B ILE B 70  ? 0.4444 0.2373 0.2515 0.0117  0.1462  -0.0103 87  ILE B CG2 
1697 C CD1 A ILE B 70  ? 0.5572 0.2295 0.2553 0.0518  0.1614  -0.0136 87  ILE B CD1 
1698 C CD1 B ILE B 70  ? 0.4390 0.3011 0.2524 0.0124  0.1455  -0.0200 87  ILE B CD1 
1699 N N   . GLU B 71  ? 0.2734 0.2232 0.2557 -0.0274 0.1525  -0.0249 88  GLU B N   
1700 C CA  . GLU B 71  ? 0.2478 0.3438 0.2624 -0.0332 0.1135  -0.0299 88  GLU B CA  
1701 C C   . GLU B 71  ? 0.2524 0.2751 0.2407 0.0181  0.0891  -0.0149 88  GLU B C   
1702 O O   . GLU B 71  ? 0.2038 0.2527 0.2339 0.0034  0.0747  -0.0148 88  GLU B O   
1703 C CB  . GLU B 71  ? 0.3302 0.5572 0.2875 0.0596  0.1219  -0.0313 88  GLU B CB  
1704 C CG  . GLU B 71  ? 0.5065 0.7857 0.3105 0.1186  0.1177  -0.0423 88  GLU B CG  
1705 C CD  . GLU B 71  ? 0.6337 0.9549 0.3274 0.1885  0.1163  -0.0603 88  GLU B CD  
1706 O OE1 . GLU B 71  ? 0.6730 1.0135 0.3372 0.1786  0.1126  -0.0662 88  GLU B OE1 
1707 O OE2 . GLU B 71  ? 0.6801 0.9732 0.3398 0.2306  0.1124  -0.0703 88  GLU B OE2 
1708 N N   . LYS B 72  ? 0.2558 0.1603 0.2259 -0.0282 0.0850  0.0011  89  LYS B N   
1709 C CA  A LYS B 72  ? 0.2576 0.1929 0.2180 0.0415  0.0823  0.0087  89  LYS B CA  
1710 C CA  B LYS B 72  ? 0.2722 0.1797 0.2188 0.0042  0.0693  0.0039  89  LYS B CA  
1711 C C   . LYS B 72  ? 0.2275 0.1638 0.2051 0.0294  0.0512  -0.0018 89  LYS B C   
1712 O O   . LYS B 72  ? 0.1974 0.1513 0.1962 0.0378  0.0369  0.0014  89  LYS B O   
1713 C CB  A LYS B 72  ? 0.2553 0.2447 0.2278 0.1100  0.1060  0.0221  89  LYS B CB  
1714 C CB  B LYS B 72  ? 0.3164 0.1966 0.2276 0.0026  0.0702  0.0110  89  LYS B CB  
1715 C CG  A LYS B 72  ? 0.3262 0.3210 0.2402 0.1008  0.1271  0.0227  89  LYS B CG  
1716 C CG  B LYS B 72  ? 0.3742 0.2842 0.2377 -0.0019 0.0692  0.0088  89  LYS B CG  
1717 C CD  A LYS B 72  ? 0.3438 0.3278 0.2484 0.0961  0.1494  0.0196  89  LYS B CD  
1718 C CD  B LYS B 72  ? 0.4041 0.3175 0.2435 -0.0133 0.0702  0.0085  89  LYS B CD  
1719 C CE  A LYS B 72  ? 0.3791 0.3209 0.2553 0.1034  0.1405  0.0034  89  LYS B CE  
1720 C CE  B LYS B 72  ? 0.4166 0.3146 0.2476 -0.0234 0.0665  0.0118  89  LYS B CE  
1721 N NZ  A LYS B 72  ? 0.3341 0.2400 0.2574 0.0044  0.1439  -0.0193 89  LYS B NZ  
1722 N NZ  B LYS B 72  ? 0.4215 0.3278 0.2502 -0.0088 0.0659  0.0143  89  LYS B NZ  
1723 N N   . MET B 73  ? 0.1831 0.1299 0.1843 0.0578  0.0373  0.0041  90  MET B N   
1724 C CA  . MET B 73  ? 0.1915 0.1254 0.1570 0.0489  0.0299  -0.0093 90  MET B CA  
1725 C C   . MET B 73  ? 0.1823 0.1079 0.1467 0.0407  0.0301  -0.0055 90  MET B C   
1726 O O   . MET B 73  ? 0.1594 0.1424 0.1425 0.0573  0.0000  -0.0133 90  MET B O   
1727 C CB  . MET B 73  ? 0.2363 0.0763 0.1521 0.0444  0.0160  -0.0048 90  MET B CB  
1728 C CG  . MET B 73  ? 0.2544 0.1197 0.1454 0.0867  0.0176  -0.0015 90  MET B CG  
1729 S SD  . MET B 73  ? 0.2405 0.1284 0.1397 0.0578  -0.0060 -0.0140 90  MET B SD  
1730 C CE  . MET B 73  ? 0.2594 0.1530 0.1476 -0.0611 -0.0070 -0.0410 90  MET B CE  
1731 N N   . THR B 74  ? 0.1394 0.1219 0.1450 0.0437  0.0400  -0.0084 91  THR B N   
1732 C CA  . THR B 74  ? 0.1246 0.1286 0.1479 0.0678  0.0358  0.0079  91  THR B CA  
1733 C C   . THR B 74  ? 0.1377 0.1355 0.1518 0.0281  0.0189  0.0084  91  THR B C   
1734 O O   . THR B 74  ? 0.1462 0.2444 0.1652 -0.0068 0.0243  -0.0114 91  THR B O   
1735 C CB  . THR B 74  ? 0.1796 0.2202 0.1562 0.1028  0.0342  -0.0162 91  THR B CB  
1736 O OG1 . THR B 74  ? 0.2058 0.1736 0.1605 0.0727  0.0491  -0.0243 91  THR B OG1 
1737 C CG2 . THR B 74  ? 0.2048 0.2270 0.1593 0.1184  0.0364  -0.0017 91  THR B CG2 
1738 N N   . GLY B 75  ? 0.1366 0.1151 0.1388 0.0661  0.0113  -0.0110 92  GLY B N   
1739 C CA  . GLY B 75  ? 0.1164 0.1416 0.1314 0.0741  0.0059  -0.0087 92  GLY B CA  
1740 C C   . GLY B 75  ? 0.0875 0.1313 0.1236 0.0423  -0.0030 0.0041  92  GLY B C   
1741 O O   . GLY B 75  ? 0.1081 0.1122 0.1327 0.0371  -0.0060 0.0230  92  GLY B O   
1742 N N   . PRO B 76  ? 0.1146 0.1133 0.1134 0.0408  0.0004  -0.0141 93  PRO B N   
1743 C CA  . PRO B 76  ? 0.1364 0.0993 0.1077 0.0437  -0.0047 -0.0092 93  PRO B CA  
1744 C C   . PRO B 76  ? 0.1400 0.1022 0.1080 0.0534  0.0041  -0.0042 93  PRO B C   
1745 O O   . PRO B 76  ? 0.1132 0.1126 0.1093 0.0202  0.0182  0.0100  93  PRO B O   
1746 C CB  . PRO B 76  ? 0.1335 0.1483 0.1056 0.0653  0.0017  -0.0036 93  PRO B CB  
1747 C CG  . PRO B 76  ? 0.1603 0.1498 0.1117 0.0870  -0.0026 -0.0070 93  PRO B CG  
1748 C CD  . PRO B 76  ? 0.1424 0.1024 0.1156 0.0509  -0.0012 0.0062  93  PRO B CD  
1749 N N   . VAL B 77  ? 0.1167 0.0778 0.1099 0.0138  -0.0012 0.0079  94  VAL B N   
1750 C CA  . VAL B 77  ? 0.0888 0.0940 0.1057 0.0240  -0.0085 -0.0083 94  VAL B CA  
1751 C C   . VAL B 77  ? 0.1030 0.0800 0.1070 0.0464  -0.0048 0.0130  94  VAL B C   
1752 O O   . VAL B 77  ? 0.1145 0.0927 0.1169 0.0214  0.0123  0.0341  94  VAL B O   
1753 C CB  . VAL B 77  ? 0.1519 0.1179 0.1000 0.0307  0.0013  -0.0111 94  VAL B CB  
1754 C CG1 . VAL B 77  ? 0.1250 0.0917 0.0956 0.0171  0.0198  -0.0414 94  VAL B CG1 
1755 C CG2 . VAL B 77  ? 0.1454 0.1634 0.0987 0.0391  -0.0124 0.0086  94  VAL B CG2 
1756 N N   . LEU B 78  ? 0.0784 0.0769 0.0963 0.0321  0.0054  -0.0087 95  LEU B N   
1757 C CA  . LEU B 78  ? 0.1153 0.0872 0.0868 0.0281  0.0078  0.0001  95  LEU B CA  
1758 C C   . LEU B 78  ? 0.0998 0.1108 0.0869 0.0181  0.0018  -0.0019 95  LEU B C   
1759 O O   . LEU B 78  ? 0.1435 0.0946 0.0923 0.0212  0.0013  0.0041  95  LEU B O   
1760 C CB  . LEU B 78  ? 0.0880 0.1113 0.0807 0.0167  0.0140  0.0208  95  LEU B CB  
1761 C CG  . LEU B 78  ? 0.1117 0.1063 0.0733 -0.0158 -0.0244 -0.0146 95  LEU B CG  
1762 C CD1 . LEU B 78  ? 0.1658 0.1586 0.0720 0.0379  0.0005  0.0166  95  LEU B CD1 
1763 C CD2 . LEU B 78  ? 0.1516 0.0786 0.0781 -0.0190 -0.0113 -0.0285 95  LEU B CD2 
1764 N N   . CYS B 79  ? 0.1170 0.0682 0.0908 0.0029  0.0040  0.0101  96  CYS B N   
1765 C CA  . CYS B 79  ? 0.1767 0.0624 0.0964 0.0130  -0.0039 0.0073  96  CYS B CA  
1766 C C   . CYS B 79  ? 0.1332 0.0496 0.0918 0.0319  -0.0093 0.0049  96  CYS B C   
1767 O O   . CYS B 79  ? 0.1181 0.1116 0.0836 0.0196  -0.0021 -0.0008 96  CYS B O   
1768 C CB  . CYS B 79  ? 0.1546 0.0999 0.1110 0.0040  0.0023  -0.0073 96  CYS B CB  
1769 S SG  . CYS B 79  ? 0.1663 0.1299 0.1335 0.0513  -0.0059 -0.0067 96  CYS B SG  
1770 N N   . MET B 80  ? 0.1068 0.0846 0.0929 0.0409  -0.0256 0.0013  97  MET B N   
1771 C CA  . MET B 80  ? 0.0744 0.1156 0.1014 0.0253  -0.0110 0.0221  97  MET B CA  
1772 C C   . MET B 80  ? 0.0768 0.0986 0.1001 0.0410  0.0157  0.0248  97  MET B C   
1773 O O   . MET B 80  ? 0.1397 0.1129 0.0915 0.0228  0.0220  0.0213  97  MET B O   
1774 C CB  . MET B 80  ? 0.1086 0.1245 0.1086 0.0028  -0.0135 0.0028  97  MET B CB  
1775 C CG  . MET B 80  ? 0.1463 0.1027 0.1070 0.0233  -0.0073 -0.0002 97  MET B CG  
1776 S SD  . MET B 80  ? 0.1468 0.1068 0.1072 0.0204  -0.0109 -0.0038 97  MET B SD  
1777 C CE  . MET B 80  ? 0.1401 0.1294 0.1130 -0.0177 -0.0210 0.0125  97  MET B CE  
1778 N N   . VAL B 81  ? 0.0754 0.1042 0.0993 0.0295  0.0010  0.0057  98  VAL B N   
1779 C CA  . VAL B 81  ? 0.1211 0.1029 0.0972 -0.0028 -0.0106 0.0004  98  VAL B CA  
1780 C C   . VAL B 81  ? 0.1307 0.0624 0.0985 0.0274  -0.0097 -0.0038 98  VAL B C   
1781 O O   . VAL B 81  ? 0.0898 0.1163 0.1067 0.0215  -0.0017 -0.0157 98  VAL B O   
1782 C CB  . VAL B 81  ? 0.1451 0.0935 0.0967 -0.0009 -0.0256 -0.0117 98  VAL B CB  
1783 C CG1 . VAL B 81  ? 0.1260 0.1147 0.1042 0.0343  -0.0195 -0.0256 98  VAL B CG1 
1784 C CG2 . VAL B 81  ? 0.1569 0.1346 0.0934 0.0260  -0.0215 -0.0186 98  VAL B CG2 
1785 N N   . PHE B 82  ? 0.1359 0.1096 0.0930 0.0261  -0.0133 0.0109  99  PHE B N   
1786 C CA  . PHE B 82  ? 0.1414 0.1060 0.0932 0.0045  -0.0049 0.0158  99  PHE B CA  
1787 C C   . PHE B 82  ? 0.1291 0.0613 0.0918 0.0240  -0.0099 -0.0120 99  PHE B C   
1788 O O   . PHE B 82  ? 0.1265 0.0976 0.0982 0.0203  -0.0015 -0.0335 99  PHE B O   
1789 C CB  . PHE B 82  ? 0.1431 0.0979 0.0884 -0.0263 -0.0238 0.0279  99  PHE B CB  
1790 C CG  . PHE B 82  ? 0.1812 0.1120 0.0879 -0.0024 -0.0246 -0.0012 99  PHE B CG  
1791 C CD1 . PHE B 82  ? 0.1794 0.1314 0.0870 0.0368  -0.0198 -0.0033 99  PHE B CD1 
1792 C CD2 . PHE B 82  ? 0.1785 0.2228 0.0892 -0.0134 -0.0116 -0.0207 99  PHE B CD2 
1793 C CE1 . PHE B 82  ? 0.2214 0.1117 0.0964 -0.0061 -0.0247 -0.0078 99  PHE B CE1 
1794 C CE2 . PHE B 82  ? 0.1510 0.1772 0.0926 -0.0501 -0.0011 -0.0135 99  PHE B CE2 
1795 C CZ  . PHE B 82  ? 0.1640 0.1742 0.0921 -0.0297 -0.0252 -0.0223 99  PHE B CZ  
1796 N N   . GLU B 83  ? 0.1322 0.0616 0.0987 0.0289  -0.0140 -0.0232 100 GLU B N   
1797 C CA  . GLU B 83  ? 0.1297 0.1103 0.1069 -0.0049 -0.0309 -0.0141 100 GLU B CA  
1798 C C   . GLU B 83  ? 0.1239 0.0950 0.1069 -0.0066 -0.0400 -0.0223 100 GLU B C   
1799 O O   . GLU B 83  ? 0.0955 0.1116 0.1047 -0.0226 -0.0281 -0.0108 100 GLU B O   
1800 C CB  . GLU B 83  ? 0.1548 0.1180 0.1239 0.0038  -0.0367 -0.0187 100 GLU B CB  
1801 C CG  . GLU B 83  ? 0.1386 0.0942 0.1387 0.0080  -0.0316 -0.0155 100 GLU B CG  
1802 C CD  . GLU B 83  ? 0.1720 0.1148 0.1461 -0.0557 -0.0167 0.0203  100 GLU B CD  
1803 O OE1 . GLU B 83  ? 0.1816 0.1682 0.1557 -0.0620 0.0095  0.0279  100 GLU B OE1 
1804 O OE2 . GLU B 83  ? 0.1981 0.1770 0.1431 -0.0276 -0.0024 0.0322  100 GLU B OE2 
1805 N N   . GLY B 84  ? 0.1214 0.1216 0.1045 -0.0098 -0.0387 0.0119  101 GLY B N   
1806 C CA  . GLY B 84  ? 0.0990 0.1797 0.0988 0.0199  -0.0308 0.0039  101 GLY B CA  
1807 C C   . GLY B 84  ? 0.1172 0.1102 0.1015 0.0318  -0.0153 0.0021  101 GLY B C   
1808 O O   . GLY B 84  ? 0.1073 0.1272 0.1070 0.0054  -0.0080 -0.0254 101 GLY B O   
1809 N N   . VAL B 85  ? 0.1281 0.0733 0.1009 0.0205  -0.0298 0.0049  102 VAL B N   
1810 C CA  . VAL B 85  ? 0.1335 0.0898 0.1000 0.0255  -0.0244 -0.0044 102 VAL B CA  
1811 C C   . VAL B 85  ? 0.1156 0.0581 0.0963 0.0152  -0.0276 -0.0007 102 VAL B C   
1812 O O   . VAL B 85  ? 0.1312 0.0727 0.1002 -0.0017 -0.0130 -0.0236 102 VAL B O   
1813 C CB  . VAL B 85  ? 0.1313 0.0793 0.1042 -0.0099 -0.0145 -0.0152 102 VAL B CB  
1814 C CG1 . VAL B 85  ? 0.1594 0.1380 0.1060 0.0544  -0.0169 0.0205  102 VAL B CG1 
1815 C CG2 . VAL B 85  ? 0.1781 0.2011 0.1122 0.0266  -0.0208 -0.0035 102 VAL B CG2 
1816 N N   . ASP B 86  ? 0.1317 0.0987 0.1017 0.0066  -0.0287 -0.0062 103 ASP B N   
1817 C CA  . ASP B 86  ? 0.1534 0.1524 0.0974 -0.0058 -0.0210 -0.0049 103 ASP B CA  
1818 C C   . ASP B 86  ? 0.1558 0.0843 0.0894 0.0170  -0.0300 -0.0002 103 ASP B C   
1819 O O   . ASP B 86  ? 0.1739 0.0827 0.0882 -0.0051 -0.0282 -0.0061 103 ASP B O   
1820 C CB  . ASP B 86  ? 0.1057 0.1929 0.1067 -0.0050 -0.0344 -0.0063 103 ASP B CB  
1821 C CG  . ASP B 86  ? 0.1737 0.2048 0.1230 0.0294  -0.0320 -0.0144 103 ASP B CG  
1822 O OD1 . ASP B 86  ? 0.1462 0.1460 0.1315 0.0182  -0.0437 -0.0073 103 ASP B OD1 
1823 O OD2 . ASP B 86  ? 0.1986 0.1645 0.1235 0.0163  -0.0275 -0.0126 103 ASP B OD2 
1824 N N   . VAL B 87  ? 0.1260 0.1136 0.0933 -0.0115 -0.0332 0.0077  104 VAL B N   
1825 C CA  . VAL B 87  ? 0.1255 0.0734 0.0942 -0.0082 -0.0088 -0.0070 104 VAL B CA  
1826 C C   . VAL B 87  ? 0.1376 0.0604 0.1034 0.0065  -0.0223 0.0018  104 VAL B C   
1827 O O   . VAL B 87  ? 0.1359 0.0678 0.1105 -0.0025 -0.0194 -0.0059 104 VAL B O   
1828 C CB  . VAL B 87  ? 0.1266 0.1002 0.0862 -0.0287 -0.0012 -0.0202 104 VAL B CB  
1829 C CG1 . VAL B 87  ? 0.1681 0.1315 0.0865 -0.0128 -0.0059 -0.0047 104 VAL B CG1 
1830 C CG2 . VAL B 87  ? 0.1993 0.0678 0.0916 0.0195  -0.0410 -0.0125 104 VAL B CG2 
1831 N N   . ILE B 88  ? 0.1344 0.0671 0.0999 -0.0121 -0.0177 -0.0092 105 ILE B N   
1832 C CA  . ILE B 88  ? 0.1154 0.0874 0.1050 0.0392  -0.0145 -0.0173 105 ILE B CA  
1833 C C   . ILE B 88  ? 0.1243 0.1358 0.0971 0.0179  -0.0212 -0.0235 105 ILE B C   
1834 O O   . ILE B 88  ? 0.1103 0.1140 0.0998 -0.0021 -0.0049 0.0023  105 ILE B O   
1835 C CB  . ILE B 88  ? 0.1537 0.1200 0.1137 0.0298  -0.0322 -0.0176 105 ILE B CB  
1836 C CG1 . ILE B 88  ? 0.1783 0.0997 0.1229 0.0001  -0.0157 -0.0068 105 ILE B CG1 
1837 C CG2 . ILE B 88  ? 0.2090 0.1994 0.1172 0.0830  -0.0271 -0.0142 105 ILE B CG2 
1838 C CD1 . ILE B 88  ? 0.1961 0.0916 0.1260 0.0120  -0.0054 -0.0323 105 ILE B CD1 
1839 N N   . ALA B 89  ? 0.1270 0.1177 0.0906 -0.0216 -0.0202 -0.0168 106 ALA B N   
1840 C CA  . ALA B 89  ? 0.1600 0.1361 0.0901 -0.0201 -0.0108 -0.0262 106 ALA B CA  
1841 C C   . ALA B 89  ? 0.1457 0.1306 0.0904 0.0353  0.0031  -0.0167 106 ALA B C   
1842 O O   . ALA B 89  ? 0.1423 0.1336 0.0874 0.0041  -0.0047 -0.0102 106 ALA B O   
1843 C CB  . ALA B 89  ? 0.1664 0.1967 0.0883 0.0628  -0.0106 -0.0373 106 ALA B CB  
1844 N N   . GLN B 90  ? 0.1398 0.0737 0.0878 0.0458  -0.0028 0.0133  107 GLN B N   
1845 C CA  . GLN B 90  ? 0.0823 0.0518 0.0856 -0.0090 -0.0147 -0.0142 107 GLN B CA  
1846 C C   . GLN B 90  ? 0.0901 0.0793 0.0857 -0.0175 -0.0208 0.0066  107 GLN B C   
1847 O O   . GLN B 90  ? 0.1050 0.0570 0.0875 -0.0190 -0.0147 0.0046  107 GLN B O   
1848 C CB  . GLN B 90  ? 0.1010 0.1202 0.0847 -0.0086 0.0023  -0.0089 107 GLN B CB  
1849 C CG  . GLN B 90  ? 0.0964 0.0964 0.0847 -0.0033 0.0036  -0.0051 107 GLN B CG  
1850 C CD  . GLN B 90  ? 0.0920 0.1430 0.0858 0.0104  -0.0021 -0.0094 107 GLN B CD  
1851 O OE1 . GLN B 90  ? 0.1158 0.1200 0.0829 0.0211  -0.0150 -0.0048 107 GLN B OE1 
1852 N NE2 . GLN B 90  ? 0.1541 0.1154 0.0903 0.0476  0.0041  -0.0196 107 GLN B NE2 
1853 N N   . ALA B 91  ? 0.1292 0.0840 0.0813 -0.0100 -0.0318 -0.0012 108 ALA B N   
1854 C CA  . ALA B 91  ? 0.1259 0.1280 0.0852 0.0079  -0.0238 -0.0017 108 ALA B CA  
1855 C C   . ALA B 91  ? 0.1367 0.0651 0.0962 0.0183  -0.0166 -0.0096 108 ALA B C   
1856 O O   . ALA B 91  ? 0.0982 0.1044 0.1011 -0.0092 -0.0201 -0.0109 108 ALA B O   
1857 C CB  . ALA B 91  ? 0.1054 0.1605 0.0800 0.0162  -0.0152 -0.0154 108 ALA B CB  
1858 N N   . ARG B 92  ? 0.1492 0.0584 0.1003 0.0118  -0.0254 -0.0110 109 ARG B N   
1859 C CA  . ARG B 92  ? 0.1154 0.1107 0.1064 0.0200  -0.0192 0.0047  109 ARG B CA  
1860 C C   . ARG B 92  ? 0.1039 0.1304 0.0996 -0.0009 -0.0029 0.0120  109 ARG B C   
1861 O O   . ARG B 92  ? 0.1142 0.1231 0.1107 0.0316  -0.0057 -0.0003 109 ARG B O   
1862 C CB  . ARG B 92  ? 0.1558 0.1409 0.1235 0.0319  -0.0070 0.0226  109 ARG B CB  
1863 C CG  . ARG B 92  ? 0.1660 0.1574 0.1387 0.0610  -0.0095 0.0267  109 ARG B CG  
1864 C CD  . ARG B 92  ? 0.1773 0.1247 0.1544 0.0215  0.0251  0.0426  109 ARG B CD  
1865 N NE  . ARG B 92  ? 0.1681 0.1573 0.1685 0.0245  0.0347  0.0305  109 ARG B NE  
1866 C CZ  . ARG B 92  ? 0.2049 0.1924 0.1785 0.0756  0.0530  0.0747  109 ARG B CZ  
1867 N NH1 . ARG B 92  ? 0.2239 0.1946 0.1831 0.0601  0.0422  0.0766  109 ARG B NH1 
1868 N NH2 . ARG B 92  ? 0.3040 0.2923 0.1888 0.1694  0.0697  0.0771  109 ARG B NH2 
1869 N N   . LYS B 93  ? 0.0729 0.1225 0.0819 -0.0249 -0.0045 0.0236  110 LYS B N   
1870 C CA  . LYS B 93  ? 0.1100 0.0902 0.0856 0.0132  -0.0064 0.0196  110 LYS B CA  
1871 C C   . LYS B 93  ? 0.0938 0.1080 0.0857 0.0145  -0.0168 0.0084  110 LYS B C   
1872 O O   . LYS B 93  ? 0.1520 0.1081 0.0845 -0.0218 -0.0242 0.0100  110 LYS B O   
1873 C CB  . LYS B 93  ? 0.1228 0.1378 0.0972 0.0187  -0.0117 0.0105  110 LYS B CB  
1874 C CG  . LYS B 93  ? 0.0988 0.1423 0.1132 -0.0002 -0.0264 -0.0066 110 LYS B CG  
1875 C CD  . LYS B 93  ? 0.1217 0.1272 0.1266 0.0226  -0.0253 0.0258  110 LYS B CD  
1876 C CE  . LYS B 93  ? 0.1151 0.1555 0.1475 -0.0034 -0.0325 0.0446  110 LYS B CE  
1877 N NZ  . LYS B 93  ? 0.1232 0.1193 0.1620 0.0027  -0.0452 0.0280  110 LYS B NZ  
1878 N N   . MET B 94  ? 0.1058 0.0981 0.0865 0.0021  -0.0194 0.0051  111 MET B N   
1879 C CA  . MET B 94  ? 0.0684 0.0802 0.0979 -0.0216 -0.0134 -0.0129 111 MET B CA  
1880 C C   . MET B 94  ? 0.0803 0.1073 0.1022 0.0207  -0.0205 0.0148  111 MET B C   
1881 O O   . MET B 94  ? 0.0882 0.1117 0.1172 0.0073  -0.0068 0.0178  111 MET B O   
1882 C CB  . MET B 94  ? 0.0945 0.0717 0.0994 0.0138  -0.0217 -0.0128 111 MET B CB  
1883 C CG  . MET B 94  ? 0.1160 0.0923 0.1006 0.0501  -0.0132 -0.0006 111 MET B CG  
1884 S SD  . MET B 94  ? 0.1192 0.1294 0.1064 0.0197  0.0073  0.0062  111 MET B SD  
1885 C CE  . MET B 94  ? 0.0918 0.1470 0.1123 0.0148  0.0241  -0.0214 111 MET B CE  
1886 N N   . MET B 95  ? 0.0846 0.0700 0.1085 0.0174  -0.0065 0.0032  112 MET B N   
1887 C CA  . MET B 95  ? 0.0805 0.1068 0.1190 0.0154  -0.0173 -0.0044 112 MET B CA  
1888 C C   . MET B 95  ? 0.0688 0.1055 0.1164 0.0065  -0.0247 -0.0174 112 MET B C   
1889 O O   . MET B 95  ? 0.0958 0.1119 0.1132 0.0205  -0.0156 -0.0178 112 MET B O   
1890 C CB  . MET B 95  ? 0.1306 0.0833 0.1310 0.0348  0.0001  -0.0064 112 MET B CB  
1891 C CG  . MET B 95  ? 0.1345 0.1123 0.1542 -0.0014 0.0179  0.0104  112 MET B CG  
1892 S SD  . MET B 95  ? 0.1842 0.1223 0.1845 0.0126  0.0374  0.0157  112 MET B SD  
1893 C CE  . MET B 95  ? 0.2142 0.1818 0.1924 -0.0280 0.0302  0.0327  112 MET B CE  
1894 N N   . GLY B 96  ? 0.0790 0.1314 0.1114 0.0066  -0.0121 -0.0066 113 GLY B N   
1895 C CA  . GLY B 96  ? 0.0992 0.1514 0.1103 -0.0109 0.0071  0.0044  113 GLY B CA  
1896 C C   . GLY B 96  ? 0.1125 0.1151 0.1115 0.0338  -0.0184 -0.0061 113 GLY B C   
1897 O O   . GLY B 96  ? 0.1069 0.1235 0.1126 0.0246  -0.0087 -0.0008 113 GLY B O   
1898 N N   . SER B 97  ? 0.1370 0.1128 0.1168 0.0471  -0.0213 0.0242  114 SER B N   
1899 C CA  . SER B 97  ? 0.1577 0.1142 0.1296 0.0292  -0.0200 0.0154  114 SER B CA  
1900 C C   . SER B 97  ? 0.1461 0.0959 0.1280 -0.0267 -0.0176 -0.0061 114 SER B C   
1901 O O   . SER B 97  ? 0.1273 0.0950 0.1206 -0.0026 -0.0135 0.0033  114 SER B O   
1902 C CB  . SER B 97  ? 0.2417 0.0986 0.1373 0.0313  -0.0196 0.0371  114 SER B CB  
1903 O OG  . SER B 97  ? 0.2886 0.2104 0.1622 0.0448  0.0102  0.0296  114 SER B OG  
1904 N N   . THR B 98  ? 0.1706 0.1230 0.1422 0.0017  0.0008  -0.0055 115 THR B N   
1905 C CA  A THR B 98  ? 0.1732 0.1166 0.1506 0.0334  0.0077  -0.0204 115 THR B CA  
1906 C CA  B THR B 98  ? 0.1597 0.1421 0.1491 0.0190  0.0154  -0.0039 115 THR B CA  
1907 C C   . THR B 98  ? 0.1320 0.0976 0.1411 -0.0121 0.0157  -0.0131 115 THR B C   
1908 O O   . THR B 98  ? 0.1611 0.1620 0.1326 0.0080  0.0059  -0.0035 115 THR B O   
1909 C CB  A THR B 98  ? 0.2173 0.1177 0.1700 0.0712  -0.0072 -0.0428 115 THR B CB  
1910 C CB  B THR B 98  ? 0.1373 0.2024 0.1675 -0.0191 0.0181  0.0022  115 THR B CB  
1911 O OG1 A THR B 98  ? 0.2339 0.0849 0.1860 0.0364  -0.0038 -0.0426 115 THR B OG1 
1912 O OG1 B THR B 98  ? 0.1446 0.2532 0.1884 -0.1046 0.0098  -0.0085 115 THR B OG1 
1913 C CG2 A THR B 98  ? 0.2692 0.1436 0.1744 0.0935  -0.0130 -0.0418 115 THR B CG2 
1914 C CG2 B THR B 98  ? 0.1503 0.2341 0.1683 0.0329  0.0205  0.0114  115 THR B CG2 
1915 N N   . ARG B 99  ? 0.1561 0.0967 0.1358 0.0445  0.0154  -0.0067 116 ARG B N   
1916 C CA  . ARG B 99  ? 0.1444 0.1242 0.1360 0.0073  0.0223  -0.0106 116 ARG B CA  
1917 C C   . ARG B 99  ? 0.1531 0.0681 0.1271 0.0460  0.0046  -0.0063 116 ARG B C   
1918 O O   . ARG B 99  ? 0.1109 0.0900 0.1249 0.0116  0.0062  0.0129  116 ARG B O   
1919 C CB  . ARG B 99  ? 0.1954 0.2034 0.1531 -0.0122 0.0740  -0.0015 116 ARG B CB  
1920 C CG  . ARG B 99  ? 0.3102 0.1862 0.1762 0.0144  0.0884  -0.0501 116 ARG B CG  
1921 C CD  . ARG B 99  ? 0.4237 0.2907 0.2100 0.0137  0.0916  -0.1027 116 ARG B CD  
1922 N NE  . ARG B 99  ? 0.5818 0.5260 0.2512 0.1124  0.0627  -0.1358 116 ARG B NE  
1923 C CZ  . ARG B 99  ? 0.7029 0.6625 0.2832 0.1251  0.0344  -0.1674 116 ARG B CZ  
1924 N NH1 . ARG B 99  ? 0.7258 0.7406 0.3030 0.1978  0.0279  -0.1527 116 ARG B NH1 
1925 N NH2 . ARG B 99  ? 0.7221 0.6162 0.2858 0.0233  0.0201  -0.2070 116 ARG B NH2 
1926 N N   . PRO B 100 ? 0.1566 0.1262 0.1187 -0.0035 0.0048  0.0039  117 PRO B N   
1927 C CA  . PRO B 100 ? 0.0851 0.0985 0.1134 0.0252  0.0126  0.0083  117 PRO B CA  
1928 C C   . PRO B 100 ? 0.1446 0.0957 0.1126 0.0140  0.0149  -0.0039 117 PRO B C   
1929 O O   . PRO B 100 ? 0.1086 0.0947 0.1112 0.0172  0.0142  0.0098  117 PRO B O   
1930 C CB  . PRO B 100 ? 0.1250 0.1290 0.1106 0.0614  -0.0075 -0.0094 117 PRO B CB  
1931 C CG  . PRO B 100 ? 0.1047 0.1020 0.1108 0.0163  0.0074  -0.0133 117 PRO B CG  
1932 C CD  . PRO B 100 ? 0.1229 0.0710 0.1154 -0.0364 0.0017  -0.0120 117 PRO B CD  
1933 N N   . GLY B 101 ? 0.1419 0.0906 0.1134 -0.0121 0.0102  -0.0209 118 GLY B N   
1934 C CA  . GLY B 101 ? 0.1070 0.1541 0.1093 -0.0086 0.0014  -0.0143 118 GLY B CA  
1935 C C   . GLY B 101 ? 0.1145 0.1605 0.1085 -0.0047 0.0164  0.0014  118 GLY B C   
1936 O O   . GLY B 101 ? 0.2126 0.1324 0.1082 -0.0207 0.0028  0.0081  118 GLY B O   
1937 N N   . GLU B 102 ? 0.1139 0.1121 0.1149 -0.0290 0.0003  0.0155  119 GLU B N   
1938 C CA  . GLU B 102 ? 0.0995 0.1515 0.1190 -0.0324 0.0011  0.0127  119 GLU B CA  
1939 C C   . GLU B 102 ? 0.1189 0.1406 0.1155 -0.0057 -0.0030 0.0190  119 GLU B C   
1940 O O   . GLU B 102 ? 0.1544 0.1526 0.1189 0.0228  0.0023  0.0203  119 GLU B O   
1941 C CB  . GLU B 102 ? 0.1456 0.1771 0.1312 -0.0265 -0.0083 0.0090  119 GLU B CB  
1942 C CG  . GLU B 102 ? 0.1947 0.3209 0.1587 -0.0796 -0.0125 -0.0216 119 GLU B CG  
1943 C CD  . GLU B 102 ? 0.4045 0.5849 0.1832 0.0982  -0.0026 -0.0277 119 GLU B CD  
1944 O OE1 . GLU B 102 ? 0.5159 0.6708 0.1932 0.1329  0.0111  -0.0379 119 GLU B OE1 
1945 O OE2 . GLU B 102 ? 0.5091 0.6963 0.1998 0.1434  0.0113  -0.0137 119 GLU B OE2 
1946 N N   . ALA B 103 ? 0.1474 0.1149 0.1112 0.0191  0.0023  0.0095  120 ALA B N   
1947 C CA  . ALA B 103 ? 0.1531 0.0763 0.1217 0.0056  -0.0023 -0.0008 120 ALA B CA  
1948 C C   . ALA B 103 ? 0.1141 0.1181 0.1330 -0.0081 0.0183  0.0435  120 ALA B C   
1949 O O   . ALA B 103 ? 0.1037 0.1809 0.1354 -0.0041 0.0386  0.0403  120 ALA B O   
1950 C CB  . ALA B 103 ? 0.1578 0.1166 0.1174 0.0079  0.0105  0.0363  120 ALA B CB  
1951 N N   . ALA B 104 ? 0.1144 0.1548 0.1415 0.0254  0.0063  0.0475  121 ALA B N   
1952 C CA  . ALA B 104 ? 0.1532 0.2261 0.1641 0.0854  -0.0013 0.0646  121 ALA B CA  
1953 C C   . ALA B 104 ? 0.1363 0.0742 0.1811 0.0244  0.0134  0.0464  121 ALA B C   
1954 O O   . ALA B 104 ? 0.1538 0.1017 0.1730 0.0077  -0.0123 0.0358  121 ALA B O   
1955 C CB  . ALA B 104 ? 0.1249 0.2330 0.1609 0.0546  -0.0278 0.0621  121 ALA B CB  
1956 N N   . PRO B 105 ? 0.2217 0.1387 0.2066 0.0529  0.0614  0.0545  122 PRO B N   
1957 C CA  . PRO B 105 ? 0.2305 0.1195 0.2084 0.0507  0.0685  0.0412  122 PRO B CA  
1958 C C   . PRO B 105 ? 0.1399 0.1214 0.1963 0.0217  0.0238  0.0202  122 PRO B C   
1959 O O   . PRO B 105 ? 0.1223 0.2253 0.2011 0.0450  0.0130  0.0116  122 PRO B O   
1960 C CB  . PRO B 105 ? 0.3948 0.1576 0.2204 0.1011  0.0955  0.0402  122 PRO B CB  
1961 C CG  . PRO B 105 ? 0.4476 0.1758 0.2241 0.1157  0.0956  0.0263  122 PRO B CG  
1962 C CD  . PRO B 105 ? 0.3784 0.1967 0.2173 0.1355  0.0898  0.0365  122 PRO B CD  
1963 N N   . GLY B 106 ? 0.2038 0.0993 0.1843 0.0571  -0.0095 -0.0354 123 GLY B N   
1964 C CA  . GLY B 106 ? 0.2180 0.1112 0.1719 0.0079  -0.0294 -0.0519 123 GLY B CA  
1965 C C   . GLY B 106 ? 0.1838 0.0583 0.1545 0.0002  -0.0140 -0.0309 123 GLY B C   
1966 O O   . GLY B 106 ? 0.1752 0.1860 0.1591 0.0253  -0.0143 -0.0324 123 GLY B O   
1967 N N   . THR B 107 ? 0.1169 0.0932 0.1287 0.0560  -0.0116 -0.0170 124 THR B N   
1968 C CA  . THR B 107 ? 0.1001 0.0982 0.1090 0.0569  -0.0102 -0.0153 124 THR B CA  
1969 C C   . THR B 107 ? 0.0975 0.0588 0.1008 0.0133  -0.0013 -0.0191 124 THR B C   
1970 O O   . THR B 107 ? 0.1453 0.0993 0.0974 0.0008  -0.0080 0.0001  124 THR B O   
1971 C CB  . THR B 107 ? 0.1614 0.0899 0.1037 0.0441  0.0038  0.0114  124 THR B CB  
1972 O OG1 . THR B 107 ? 0.1252 0.0772 0.1050 0.0285  -0.0008 0.0110  124 THR B OG1 
1973 C CG2 . THR B 107 ? 0.1717 0.1378 0.1027 0.0184  -0.0177 -0.0053 124 THR B CG2 
1974 N N   . ILE B 108 ? 0.1529 0.0514 0.0927 -0.0065 -0.0068 0.0225  125 ILE B N   
1975 C CA  . ILE B 108 ? 0.1288 0.0783 0.0866 -0.0157 -0.0033 -0.0096 125 ILE B CA  
1976 C C   . ILE B 108 ? 0.0982 0.1374 0.0896 0.0048  -0.0018 0.0096  125 ILE B C   
1977 O O   . ILE B 108 ? 0.0807 0.1213 0.0914 -0.0117 -0.0187 0.0049  125 ILE B O   
1978 C CB  . ILE B 108 ? 0.1356 0.0742 0.0863 0.0032  -0.0112 0.0030  125 ILE B CB  
1979 C CG1 . ILE B 108 ? 0.1542 0.1050 0.0913 -0.0238 0.0101  0.0126  125 ILE B CG1 
1980 C CG2 . ILE B 108 ? 0.0798 0.1258 0.0823 -0.0300 -0.0136 0.0048  125 ILE B CG2 
1981 C CD1 . ILE B 108 ? 0.1577 0.1578 0.0922 -0.0325 0.0244  0.0139  125 ILE B CD1 
1982 N N   . ARG B 109 ? 0.0759 0.1026 0.0981 0.0189  -0.0013 0.0089  126 ARG B N   
1983 C CA  . ARG B 109 ? 0.0761 0.1220 0.1115 0.0175  -0.0102 0.0306  126 ARG B CA  
1984 C C   . ARG B 109 ? 0.0770 0.0903 0.1052 -0.0038 0.0114  0.0207  126 ARG B C   
1985 O O   . ARG B 109 ? 0.1147 0.0954 0.1052 0.0272  0.0033  0.0040  126 ARG B O   
1986 C CB  . ARG B 109 ? 0.1100 0.1206 0.1352 -0.0104 -0.0009 0.0354  126 ARG B CB  
1987 C CG  . ARG B 109 ? 0.2228 0.1808 0.1640 0.0560  -0.0379 0.0540  126 ARG B CG  
1988 C CD  . ARG B 109 ? 0.1540 0.2238 0.1776 0.0498  -0.0256 0.0845  126 ARG B CD  
1989 N NE  . ARG B 109 ? 0.0990 0.1090 0.1678 0.0155  -0.0027 0.0425  126 ARG B NE  
1990 C CZ  . ARG B 109 ? 0.1183 0.0833 0.1488 0.0248  -0.0155 0.0385  126 ARG B CZ  
1991 N NH1 . ARG B 109 ? 0.1914 0.1018 0.1494 0.0316  -0.0062 0.0614  126 ARG B NH1 
1992 N NH2 . ARG B 109 ? 0.1351 0.1202 0.1312 0.0345  -0.0169 0.0126  126 ARG B NH2 
1993 N N   . ALA B 110 ? 0.0729 0.0894 0.1005 -0.0079 -0.0093 0.0045  127 ALA B N   
1994 C CA  . ALA B 110 ? 0.1071 0.0834 0.1062 -0.0504 0.0121  0.0138  127 ALA B CA  
1995 C C   . ALA B 110 ? 0.1242 0.0433 0.1196 -0.0100 0.0065  -0.0099 127 ALA B C   
1996 O O   . ALA B 110 ? 0.1214 0.1239 0.1306 -0.0505 0.0276  -0.0336 127 ALA B O   
1997 C CB  . ALA B 110 ? 0.1693 0.1287 0.0960 -0.0084 0.0182  0.0283  127 ALA B CB  
1998 N N   . ASP B 111 ? 0.0737 0.0544 0.1202 0.0164  -0.0031 -0.0082 128 ASP B N   
1999 C CA  . ASP B 111 ? 0.0963 0.0518 0.1202 0.0051  -0.0164 -0.0032 128 ASP B CA  
2000 C C   . ASP B 111 ? 0.0604 0.0906 0.1080 -0.0271 0.0003  -0.0061 128 ASP B C   
2001 O O   . ASP B 111 ? 0.0982 0.0803 0.1136 0.0039  0.0076  0.0081  128 ASP B O   
2002 C CB  . ASP B 111 ? 0.1007 0.1056 0.1380 -0.0063 -0.0219 -0.0168 128 ASP B CB  
2003 C CG  . ASP B 111 ? 0.0817 0.1328 0.1747 -0.0204 0.0092  0.0318  128 ASP B CG  
2004 O OD1 . ASP B 111 ? 0.1500 0.1659 0.1985 0.0351  0.0041  0.0613  128 ASP B OD1 
2005 O OD2 . ASP B 111 ? 0.0885 0.1456 0.1954 -0.0081 -0.0066 -0.0048 128 ASP B OD2 
2006 N N   . PHE B 112 ? 0.0789 0.0950 0.0953 0.0256  -0.0068 -0.0198 129 PHE B N   
2007 C CA  . PHE B 112 ? 0.1239 0.0577 0.0903 0.0190  -0.0017 -0.0008 129 PHE B CA  
2008 C C   . PHE B 112 ? 0.0874 0.0985 0.0913 0.0208  -0.0145 0.0004  129 PHE B C   
2009 O O   . PHE B 112 ? 0.0753 0.1003 0.0919 0.0044  -0.0161 0.0014  129 PHE B O   
2010 C CB  . PHE B 112 ? 0.1037 0.1076 0.0894 -0.0027 0.0045  0.0072  129 PHE B CB  
2011 C CG  . PHE B 112 ? 0.1259 0.0672 0.1024 -0.0047 0.0102  -0.0003 129 PHE B CG  
2012 C CD1 . PHE B 112 ? 0.1443 0.0941 0.1077 0.0122  0.0187  0.0016  129 PHE B CD1 
2013 C CD2 . PHE B 112 ? 0.0902 0.1043 0.1065 -0.0207 0.0064  -0.0003 129 PHE B CD2 
2014 C CE1 . PHE B 112 ? 0.1014 0.1647 0.1118 -0.0215 0.0245  -0.0050 129 PHE B CE1 
2015 C CE2 . PHE B 112 ? 0.1411 0.1373 0.1089 0.0682  0.0224  0.0133  129 PHE B CE2 
2016 C CZ  . PHE B 112 ? 0.1321 0.1437 0.1133 0.0688  0.0526  0.0364  129 PHE B CZ  
2017 N N   . CYS B 113 ? 0.1056 0.0875 0.0928 0.0040  0.0048  0.0317  130 CYS B N   
2018 C CA  . CYS B 113 ? 0.1289 0.0693 0.1023 0.0443  0.0174  0.0241  130 CYS B CA  
2019 C C   . CYS B 113 ? 0.1457 0.0694 0.1088 0.0265  0.0144  -0.0104 130 CYS B C   
2020 O O   . CYS B 113 ? 0.0880 0.0717 0.1170 0.0198  0.0215  0.0083  130 CYS B O   
2021 C CB  . CYS B 113 ? 0.0972 0.0636 0.1106 0.0221  0.0226  0.0198  130 CYS B CB  
2022 S SG  . CYS B 113 ? 0.1394 0.0980 0.1160 -0.0030 0.0318  0.0043  130 CYS B SG  
2023 N N   . GLN B 114 ? 0.1129 0.0451 0.1057 0.0171  0.0187  -0.0056 131 GLN B N   
2024 C CA  . GLN B 114 ? 0.1037 0.0956 0.1001 0.0009  -0.0010 -0.0030 131 GLN B CA  
2025 C C   . GLN B 114 ? 0.1171 0.1145 0.1006 -0.0005 0.0006  -0.0109 131 GLN B C   
2026 O O   . GLN B 114 ? 0.1524 0.1262 0.0954 0.0254  -0.0085 0.0084  131 GLN B O   
2027 C CB  . GLN B 114 ? 0.0891 0.0833 0.0995 0.0116  0.0297  0.0085  131 GLN B CB  
2028 C CG  . GLN B 114 ? 0.0825 0.1209 0.1009 0.0095  0.0116  -0.0089 131 GLN B CG  
2029 C CD  . GLN B 114 ? 0.1100 0.1196 0.0964 0.0494  -0.0031 0.0119  131 GLN B CD  
2030 O OE1 . GLN B 114 ? 0.1016 0.1155 0.0991 0.0061  0.0125  0.0165  131 GLN B OE1 
2031 N NE2 . GLN B 114 ? 0.1249 0.1235 0.0925 0.0302  -0.0143 0.0171  131 GLN B NE2 
2032 N N   . GLN B 115 ? 0.1089 0.1067 0.1088 0.0072  0.0064  -0.0142 132 GLN B N   
2033 C CA  . GLN B 115 ? 0.1119 0.1379 0.1328 -0.0032 0.0068  -0.0319 132 GLN B CA  
2034 C C   . GLN B 115 ? 0.0855 0.1154 0.1325 0.0075  0.0102  -0.0316 132 GLN B C   
2035 O O   . GLN B 115 ? 0.1207 0.1243 0.1337 0.0029  0.0273  0.0005  132 GLN B O   
2036 C CB  . GLN B 115 ? 0.1538 0.1639 0.1553 0.0200  0.0211  -0.0479 132 GLN B CB  
2037 C CG  . GLN B 115 ? 0.1302 0.2263 0.1753 0.0072  0.0163  -0.0486 132 GLN B CG  
2038 C CD  . GLN B 115 ? 0.1473 0.2655 0.1855 0.0684  0.0382  -0.0419 132 GLN B CD  
2039 O OE1 . GLN B 115 ? 0.1476 0.2530 0.1919 0.0810  0.0364  -0.0315 132 GLN B OE1 
2040 N NE2 . GLN B 115 ? 0.2071 0.3269 0.1940 0.0936  0.0577  -0.0258 132 GLN B NE2 
2041 N N   . ALA B 116 ? 0.0907 0.1195 0.1285 0.0156  -0.0119 -0.0391 133 ALA B N   
2042 C CA  . ALA B 116 ? 0.1389 0.0949 0.1316 0.0293  -0.0051 -0.0373 133 ALA B CA  
2043 C C   . ALA B 116 ? 0.1123 0.1408 0.1366 0.0665  0.0206  -0.0174 133 ALA B C   
2044 O O   . ALA B 116 ? 0.1429 0.1278 0.1433 0.0353  0.0056  -0.0301 133 ALA B O   
2045 C CB  . ALA B 116 ? 0.1880 0.1240 0.1346 0.0290  -0.0123 -0.0410 133 ALA B CB  
2046 N N   . GLY B 117 ? 0.1200 0.1124 0.1347 0.0415  0.0307  0.0055  134 GLY B N   
2047 C CA  . GLY B 117 ? 0.1310 0.1066 0.1236 0.0311  0.0152  -0.0024 134 GLY B CA  
2048 C C   . GLY B 117 ? 0.1496 0.1022 0.1112 0.0332  0.0114  0.0145  134 GLY B C   
2049 O O   . GLY B 117 ? 0.1936 0.1248 0.1160 0.0164  0.0071  0.0033  134 GLY B O   
2050 N N   . ARG B 118 ? 0.1675 0.1253 0.1025 0.0507  0.0087  0.0126  135 ARG B N   
2051 C CA  . ARG B 118 ? 0.1154 0.1060 0.1082 0.0140  0.0229  0.0076  135 ARG B CA  
2052 C C   . ARG B 118 ? 0.0968 0.0948 0.1088 -0.0032 0.0242  0.0213  135 ARG B C   
2053 O O   . ARG B 118 ? 0.1426 0.0930 0.1224 0.0016  0.0018  0.0155  135 ARG B O   
2054 C CB  . ARG B 118 ? 0.0898 0.1472 0.1145 0.0209  0.0145  -0.0044 135 ARG B CB  
2055 C CG  . ARG B 118 ? 0.1235 0.1162 0.1205 0.0189  0.0303  -0.0138 135 ARG B CG  
2056 C CD  . ARG B 118 ? 0.1447 0.1300 0.1332 0.0256  0.0124  -0.0081 135 ARG B CD  
2057 N NE  . ARG B 118 ? 0.1461 0.0792 0.1502 -0.0044 0.0057  -0.0060 135 ARG B NE  
2058 C CZ  . ARG B 118 ? 0.1544 0.1258 0.1575 0.0094  -0.0058 -0.0034 135 ARG B CZ  
2059 N NH1 . ARG B 118 ? 0.1398 0.1896 0.1592 0.0128  0.0064  0.0093  135 ARG B NH1 
2060 N NH2 . ARG B 118 ? 0.1747 0.1528 0.1648 0.0635  -0.0287 -0.0040 135 ARG B NH2 
2061 N N   . ASN B 119 ? 0.0807 0.1041 0.1037 0.0057  0.0250  0.0091  136 ASN B N   
2062 C CA  . ASN B 119 ? 0.1083 0.1007 0.1079 0.0509  -0.0043 -0.0055 136 ASN B CA  
2063 C C   . ASN B 119 ? 0.0994 0.0696 0.1066 0.0124  0.0050  -0.0152 136 ASN B C   
2064 O O   . ASN B 119 ? 0.0974 0.1185 0.1017 0.0162  0.0037  -0.0031 136 ASN B O   
2065 C CB  . ASN B 119 ? 0.1159 0.0955 0.1058 0.0085  -0.0027 -0.0109 136 ASN B CB  
2066 C CG  . ASN B 119 ? 0.1174 0.1110 0.1103 0.0333  0.0021  0.0113  136 ASN B CG  
2067 O OD1 . ASN B 119 ? 0.2336 0.1072 0.1206 0.0512  0.0068  -0.0005 136 ASN B OD1 
2068 N ND2 . ASN B 119 ? 0.1546 0.1155 0.1094 0.0087  0.0072  -0.0076 136 ASN B ND2 
2069 N N   . LEU B 120 ? 0.0791 0.0846 0.1068 0.0146  0.0123  0.0050  137 LEU B N   
2070 C CA  . LEU B 120 ? 0.0427 0.0904 0.1039 0.0104  0.0172  0.0125  137 LEU B CA  
2071 C C   . LEU B 120 ? 0.0863 0.0603 0.1000 0.0271  0.0194  0.0248  137 LEU B C   
2072 O O   . LEU B 120 ? 0.1085 0.0882 0.0990 0.0328  0.0177  0.0387  137 LEU B O   
2073 C CB  . LEU B 120 ? 0.1290 0.0979 0.1027 -0.0188 0.0205  0.0060  137 LEU B CB  
2074 C CG  . LEU B 120 ? 0.1109 0.0982 0.1135 -0.0306 0.0269  -0.0023 137 LEU B CG  
2075 C CD1 . LEU B 120 ? 0.1080 0.1207 0.1149 -0.0383 -0.0024 -0.0137 137 LEU B CD1 
2076 C CD2 . LEU B 120 ? 0.1181 0.0747 0.1182 0.0098  0.0163  0.0032  137 LEU B CD2 
2077 N N   . ILE B 121 ? 0.1109 0.0778 0.0941 0.0162  0.0128  0.0179  138 ILE B N   
2078 C CA  . ILE B 121 ? 0.1166 0.0775 0.0978 0.0150  0.0030  -0.0019 138 ILE B CA  
2079 C C   . ILE B 121 ? 0.0934 0.1117 0.0928 0.0309  -0.0096 0.0020  138 ILE B C   
2080 O O   . ILE B 121 ? 0.1548 0.1048 0.0944 0.0207  0.0076  0.0059  138 ILE B O   
2081 C CB  . ILE B 121 ? 0.1156 0.0498 0.1079 -0.0118 0.0106  0.0004  138 ILE B CB  
2082 C CG1 . ILE B 121 ? 0.1654 0.1057 0.1194 0.0489  0.0120  -0.0140 138 ILE B CG1 
2083 C CG2 . ILE B 121 ? 0.1271 0.1056 0.1069 0.0233  -0.0101 -0.0363 138 ILE B CG2 
2084 C CD1 . ILE B 121 ? 0.1532 0.1065 0.1340 0.0026  0.0054  -0.0053 138 ILE B CD1 
2085 N N   . HIS B 122 ? 0.1137 0.1076 0.0826 -0.0153 -0.0124 -0.0118 139 HIS B N   
2086 C CA  . HIS B 122 ? 0.0840 0.1489 0.0849 0.0111  -0.0325 -0.0085 139 HIS B CA  
2087 C C   . HIS B 122 ? 0.1449 0.0814 0.0821 0.0197  -0.0056 0.0008  139 HIS B C   
2088 O O   . HIS B 122 ? 0.1155 0.1103 0.0736 0.0133  0.0034  -0.0060 139 HIS B O   
2089 C CB  . HIS B 122 ? 0.1145 0.1385 0.1019 0.0337  -0.0224 -0.0139 139 HIS B CB  
2090 C CG  . HIS B 122 ? 0.1702 0.1221 0.1227 0.0484  -0.0010 -0.0041 139 HIS B CG  
2091 N ND1 . HIS B 122 ? 0.2089 0.1407 0.1257 0.0346  0.0043  -0.0261 139 HIS B ND1 
2092 C CD2 . HIS B 122 ? 0.1763 0.0806 0.1299 0.0449  0.0209  -0.0094 139 HIS B CD2 
2093 C CE1 . HIS B 122 ? 0.2572 0.1063 0.1287 0.0195  0.0000  -0.0059 139 HIS B CE1 
2094 N NE2 . HIS B 122 ? 0.2093 0.1131 0.1307 -0.0002 -0.0026 -0.0142 139 HIS B NE2 
2095 N N   . GLY B 123 ? 0.1145 0.1108 0.0841 0.0044  -0.0104 -0.0041 140 GLY B N   
2096 C CA  . GLY B 123 ? 0.1233 0.0762 0.0861 0.0224  -0.0049 0.0031  140 GLY B CA  
2097 C C   . GLY B 123 ? 0.1351 0.0447 0.0911 -0.0265 -0.0054 -0.0030 140 GLY B C   
2098 O O   . GLY B 123 ? 0.1248 0.1117 0.0936 0.0222  0.0170  0.0056  140 GLY B O   
2099 N N   . SER B 124 ? 0.1574 0.0641 0.0972 0.0006  -0.0128 -0.0144 141 SER B N   
2100 C CA  . SER B 124 ? 0.1774 0.0539 0.1071 -0.0170 -0.0123 -0.0153 141 SER B CA  
2101 C C   . SER B 124 ? 0.2038 0.1304 0.1190 0.0113  -0.0092 -0.0095 141 SER B C   
2102 O O   . SER B 124 ? 0.2013 0.1013 0.1278 0.0363  -0.0540 -0.0051 141 SER B O   
2103 C CB  . SER B 124 ? 0.2086 0.1304 0.1068 -0.0017 -0.0103 0.0037  141 SER B CB  
2104 O OG  . SER B 124 ? 0.1911 0.1507 0.1078 -0.0161 0.0002  0.0113  141 SER B OG  
2105 N N   . ASP B 125 ? 0.2664 0.1241 0.1246 -0.0060 0.0026  -0.0060 142 ASP B N   
2106 C CA  . ASP B 125 ? 0.2716 0.1320 0.1347 -0.0155 -0.0046 0.0039  142 ASP B CA  
2107 C C   . ASP B 125 ? 0.2532 0.1609 0.1413 -0.0093 -0.0072 0.0070  142 ASP B C   
2108 O O   . ASP B 125 ? 0.2752 0.1942 0.1509 0.0131  -0.0048 0.0518  142 ASP B O   
2109 C CB  . ASP B 125 ? 0.3187 0.2398 0.1433 0.0227  0.0141  0.0008  142 ASP B CB  
2110 C CG  . ASP B 125 ? 0.4067 0.3169 0.1551 0.0541  0.0365  -0.0072 142 ASP B CG  
2111 O OD1 . ASP B 125 ? 0.3825 0.1876 0.1593 0.0942  0.0288  -0.0186 142 ASP B OD1 
2112 O OD2 . ASP B 125 ? 0.4769 0.4349 0.1668 0.0537  0.0469  -0.0268 142 ASP B OD2 
2113 N N   . SER B 126 ? 0.2133 0.1299 0.1428 -0.0087 -0.0149 -0.0455 143 SER B N   
2114 C CA  . SER B 126 ? 0.2612 0.1671 0.1541 0.0330  -0.0227 -0.0405 143 SER B CA  
2115 C C   . SER B 126 ? 0.2105 0.1194 0.1542 -0.0305 -0.0272 -0.0208 143 SER B C   
2116 O O   . SER B 126 ? 0.1889 0.1311 0.1397 0.0312  -0.0253 -0.0158 143 SER B O   
2117 C CB  . SER B 126 ? 0.3014 0.1497 0.1577 0.0547  -0.0218 -0.0557 143 SER B CB  
2118 O OG  . SER B 126 ? 0.3189 0.1448 0.1580 0.0609  -0.0248 -0.0454 143 SER B OG  
2119 N N   . ALA B 127 ? 0.2736 0.1187 0.1697 0.0110  -0.0321 -0.0383 144 ALA B N   
2120 C CA  . ALA B 127 ? 0.2312 0.1972 0.1813 0.0198  -0.0278 -0.0320 144 ALA B CA  
2121 C C   . ALA B 127 ? 0.2161 0.1558 0.1847 0.0658  -0.0404 -0.0589 144 ALA B C   
2122 O O   . ALA B 127 ? 0.2276 0.1619 0.1902 -0.0104 -0.0553 -0.0588 144 ALA B O   
2123 C CB  . ALA B 127 ? 0.2951 0.2362 0.1873 0.0463  -0.0278 -0.0331 144 ALA B CB  
2124 N N   . GLU B 128 ? 0.2949 0.1488 0.1886 0.0466  -0.0515 -0.0783 145 GLU B N   
2125 C CA  . GLU B 128 ? 0.3061 0.1610 0.1940 0.0483  -0.0441 -0.0852 145 GLU B CA  
2126 C C   . GLU B 128 ? 0.2460 0.1728 0.1827 0.0594  -0.0367 -0.0663 145 GLU B C   
2127 O O   . GLU B 128 ? 0.2612 0.1749 0.1846 0.0635  -0.0470 -0.0722 145 GLU B O   
2128 C CB  . GLU B 128 ? 0.3560 0.1846 0.2248 0.0641  -0.0360 -0.0968 145 GLU B CB  
2129 C CG  . GLU B 128 ? 0.5105 0.2721 0.2464 0.1521  -0.0338 -0.0862 145 GLU B CG  
2130 C CD  . GLU B 128 ? 0.6712 0.4984 0.2670 0.2498  -0.0375 -0.0560 145 GLU B CD  
2131 O OE1 . GLU B 128 ? 0.7545 0.5342 0.2701 0.2829  -0.0368 -0.0319 145 GLU B OE1 
2132 O OE2 . GLU B 128 ? 0.6993 0.6189 0.2787 0.3090  -0.0306 -0.0581 145 GLU B OE2 
2133 N N   . SER B 129 ? 0.2376 0.1274 0.1713 0.0574  -0.0193 -0.0456 146 SER B N   
2134 C CA  A SER B 129 ? 0.1898 0.1612 0.1707 0.0809  -0.0212 -0.0417 146 SER B CA  
2135 C CA  B SER B 129 ? 0.2297 0.1723 0.1669 0.0809  -0.0108 -0.0438 146 SER B CA  
2136 C C   . SER B 129 ? 0.2039 0.1400 0.1653 0.0191  -0.0142 -0.0438 146 SER B C   
2137 O O   . SER B 129 ? 0.2085 0.1201 0.1653 0.0296  -0.0092 -0.0204 146 SER B O   
2138 C CB  A SER B 129 ? 0.0991 0.1652 0.1747 0.0565  -0.0236 -0.0251 146 SER B CB  
2139 C CB  B SER B 129 ? 0.2191 0.2087 0.1635 0.0791  0.0111  -0.0337 146 SER B CB  
2140 O OG  A SER B 129 ? 0.1205 0.1479 0.1802 0.0459  -0.0281 -0.0112 146 SER B OG  
2141 O OG  B SER B 129 ? 0.2998 0.2433 0.1623 0.1198  0.0331  -0.0215 146 SER B OG  
2142 N N   . ALA B 130 ? 0.1830 0.1096 0.1606 0.0467  -0.0192 -0.0539 147 ALA B N   
2143 C CA  . ALA B 130 ? 0.1696 0.1179 0.1654 0.0188  -0.0278 -0.0670 147 ALA B CA  
2144 C C   . ALA B 130 ? 0.1264 0.1457 0.1633 -0.0404 -0.0288 -0.0569 147 ALA B C   
2145 O O   . ALA B 130 ? 0.1640 0.1545 0.1589 0.0204  -0.0368 -0.0499 147 ALA B O   
2146 C CB  . ALA B 130 ? 0.1914 0.1028 0.1738 0.0037  -0.0422 -0.0644 147 ALA B CB  
2147 N N   . LYS B 131 ? 0.1586 0.1585 0.1639 0.0050  -0.0368 -0.0530 148 LYS B N   
2148 C CA  . LYS B 131 ? 0.2421 0.1184 0.1727 -0.0643 -0.0233 -0.0350 148 LYS B CA  
2149 C C   . LYS B 131 ? 0.2467 0.1767 0.1721 -0.0385 -0.0150 -0.0267 148 LYS B C   
2150 O O   . LYS B 131 ? 0.2796 0.1209 0.1781 -0.0644 -0.0249 -0.0249 148 LYS B O   
2151 C CB  . LYS B 131 ? 0.3835 0.1474 0.1898 -0.0716 -0.0165 -0.0113 148 LYS B CB  
2152 C CG  . LYS B 131 ? 0.5166 0.3158 0.2073 -0.0003 -0.0139 -0.0321 148 LYS B CG  
2153 C CD  . LYS B 131 ? 0.6770 0.4881 0.2270 0.1204  -0.0051 -0.0199 148 LYS B CD  
2154 C CE  . LYS B 131 ? 0.7776 0.6154 0.2402 0.2051  0.0085  -0.0070 148 LYS B CE  
2155 N NZ  . LYS B 131 ? 0.8469 0.7150 0.2588 0.2375  0.0120  0.0126  148 LYS B NZ  
2156 N N   . ARG B 132 ? 0.2142 0.1427 0.1682 0.0003  -0.0023 -0.0532 149 ARG B N   
2157 C CA  . ARG B 132 ? 0.2383 0.1234 0.1696 0.0264  -0.0091 -0.0638 149 ARG B CA  
2158 C C   . ARG B 132 ? 0.2220 0.0935 0.1675 0.0356  -0.0199 -0.0280 149 ARG B C   
2159 O O   . ARG B 132 ? 0.2779 0.0727 0.1692 -0.0001 -0.0260 -0.0048 149 ARG B O   
2160 C CB  . ARG B 132 ? 0.3219 0.1944 0.1776 0.0260  -0.0056 -0.0560 149 ARG B CB  
2161 C CG  . ARG B 132 ? 0.3203 0.2616 0.1862 -0.0260 0.0089  -0.0613 149 ARG B CG  
2162 C CD  . ARG B 132 ? 0.3582 0.3721 0.1987 -0.0318 0.0187  -0.0701 149 ARG B CD  
2163 N NE  . ARG B 132 ? 0.4408 0.5687 0.2147 0.0100  0.0105  -0.0534 149 ARG B NE  
2164 C CZ  . ARG B 132 ? 0.5085 0.6242 0.2275 -0.0192 -0.0026 -0.0374 149 ARG B CZ  
2165 N NH1 . ARG B 132 ? 0.4968 0.6157 0.2341 -0.0509 0.0065  -0.0347 149 ARG B NH1 
2166 N NH2 . ARG B 132 ? 0.5591 0.6811 0.2312 0.0174  -0.0151 -0.0308 149 ARG B NH2 
2167 N N   . GLU B 133 ? 0.1967 0.1181 0.1644 0.0126  -0.0297 -0.0363 150 GLU B N   
2168 C CA  . GLU B 133 ? 0.2062 0.0871 0.1593 -0.0062 -0.0144 -0.0149 150 GLU B CA  
2169 C C   . GLU B 133 ? 0.1958 0.0712 0.1530 0.0145  -0.0133 -0.0351 150 GLU B C   
2170 O O   . GLU B 133 ? 0.2687 0.1153 0.1510 -0.0150 -0.0063 -0.0170 150 GLU B O   
2171 C CB  . GLU B 133 ? 0.2553 0.0676 0.1572 -0.0094 0.0004  -0.0124 150 GLU B CB  
2172 C CG  . GLU B 133 ? 0.2075 0.0869 0.1579 -0.0213 -0.0014 -0.0185 150 GLU B CG  
2173 C CD  . GLU B 133 ? 0.1926 0.0930 0.1546 -0.0076 0.0029  -0.0196 150 GLU B CD  
2174 O OE1 . GLU B 133 ? 0.2236 0.1100 0.1471 0.0486  -0.0222 -0.0364 150 GLU B OE1 
2175 O OE2 . GLU B 133 ? 0.2493 0.1304 0.1644 0.0167  0.0275  0.0047  150 GLU B OE2 
2176 N N   . ILE B 134 ? 0.2107 0.0927 0.1544 0.0072  -0.0011 -0.0183 151 ILE B N   
2177 C CA  . ILE B 134 ? 0.2031 0.1549 0.1658 -0.0123 0.0066  -0.0158 151 ILE B CA  
2178 C C   . ILE B 134 ? 0.2654 0.0929 0.1690 -0.0346 0.0046  -0.0086 151 ILE B C   
2179 O O   . ILE B 134 ? 0.2868 0.1429 0.1615 -0.0397 0.0020  -0.0218 151 ILE B O   
2180 C CB  . ILE B 134 ? 0.1856 0.1981 0.1764 0.0037  0.0197  -0.0148 151 ILE B CB  
2181 C CG1 . ILE B 134 ? 0.1487 0.1189 0.1854 0.0276  0.0577  -0.0195 151 ILE B CG1 
2182 C CG2 . ILE B 134 ? 0.1930 0.2040 0.1798 -0.0437 0.0161  -0.0266 151 ILE B CG2 
2183 C CD1 . ILE B 134 ? 0.1805 0.1035 0.1965 0.0117  0.0332  -0.0259 151 ILE B CD1 
2184 N N   . SER B 135 ? 0.2270 0.1264 0.1790 -0.0654 -0.0190 -0.0080 152 SER B N   
2185 C CA  . SER B 135 ? 0.2577 0.1809 0.1920 -0.0379 -0.0419 -0.0065 152 SER B CA  
2186 C C   . SER B 135 ? 0.2542 0.1242 0.1937 -0.0017 -0.0415 -0.0155 152 SER B C   
2187 O O   . SER B 135 ? 0.3718 0.1435 0.2026 0.0157  -0.0189 -0.0066 152 SER B O   
2188 C CB  . SER B 135 ? 0.3179 0.1954 0.2022 -0.0503 -0.0474 -0.0089 152 SER B CB  
2189 O OG  . SER B 135 ? 0.3698 0.1938 0.2089 -0.0404 -0.0434 -0.0328 152 SER B OG  
2190 N N   . LEU B 136 ? 0.2523 0.1200 0.1920 -0.0367 -0.0459 -0.0329 153 LEU B N   
2191 C CA  . LEU B 136 ? 0.2776 0.1012 0.1929 0.0197  -0.0266 -0.0202 153 LEU B CA  
2192 C C   . LEU B 136 ? 0.2927 0.0842 0.1949 0.0203  -0.0403 -0.0224 153 LEU B C   
2193 O O   . LEU B 136 ? 0.2909 0.0921 0.2086 0.0499  -0.0177 -0.0199 153 LEU B O   
2194 C CB  . LEU B 136 ? 0.3241 0.1335 0.1922 0.0550  -0.0154 -0.0067 153 LEU B CB  
2195 C CG  . LEU B 136 ? 0.3048 0.1394 0.1908 0.0556  -0.0017 -0.0002 153 LEU B CG  
2196 C CD1 . LEU B 136 ? 0.3704 0.1394 0.1908 0.0445  -0.0044 -0.0030 153 LEU B CD1 
2197 C CD2 . LEU B 136 ? 0.3221 0.1424 0.1939 0.0094  -0.0091 -0.0105 153 LEU B CD2 
2198 N N   . TRP B 137 ? 0.2999 0.0979 0.1905 0.0260  -0.0678 -0.0350 154 TRP B N   
2199 C CA  . TRP B 137 ? 0.2272 0.0800 0.1838 -0.0100 -0.0618 -0.0262 154 TRP B CA  
2200 C C   . TRP B 137 ? 0.2863 0.1026 0.1851 0.0134  -0.0633 -0.0080 154 TRP B C   
2201 O O   . TRP B 137 ? 0.2802 0.1972 0.1849 0.0377  -0.0798 -0.0055 154 TRP B O   
2202 C CB  . TRP B 137 ? 0.2553 0.1025 0.1830 0.0542  -0.0749 -0.0220 154 TRP B CB  
2203 C CG  . TRP B 137 ? 0.2489 0.0915 0.1806 0.0462  -0.0599 -0.0302 154 TRP B CG  
2204 C CD1 . TRP B 137 ? 0.2124 0.1247 0.1820 0.0035  -0.0745 -0.0462 154 TRP B CD1 
2205 C CD2 . TRP B 137 ? 0.2307 0.1219 0.1789 0.0499  -0.0476 -0.0226 154 TRP B CD2 
2206 N NE1 . TRP B 137 ? 0.2357 0.1237 0.1814 0.0848  -0.0482 -0.0210 154 TRP B NE1 
2207 C CE2 . TRP B 137 ? 0.2291 0.1283 0.1799 0.0847  -0.0603 -0.0214 154 TRP B CE2 
2208 C CE3 . TRP B 137 ? 0.2310 0.1592 0.1829 0.0870  -0.0491 -0.0212 154 TRP B CE3 
2209 C CZ2 . TRP B 137 ? 0.2731 0.1773 0.1816 0.0884  -0.0701 -0.0210 154 TRP B CZ2 
2210 C CZ3 . TRP B 137 ? 0.2848 0.1967 0.1830 0.1127  -0.0493 -0.0332 154 TRP B CZ3 
2211 C CH2 . TRP B 137 ? 0.2420 0.2031 0.1825 0.1000  -0.0565 -0.0249 154 TRP B CH2 
2212 N N   . PHE B 138 ? 0.3179 0.1142 0.1874 0.0346  -0.0348 -0.0176 155 PHE B N   
2213 C CA  . PHE B 138 ? 0.3245 0.1082 0.1900 0.0412  -0.0196 -0.0422 155 PHE B CA  
2214 C C   . PHE B 138 ? 0.3470 0.0973 0.2122 0.0062  0.0110  -0.0324 155 PHE B C   
2215 O O   . PHE B 138 ? 0.3784 0.1000 0.2133 -0.0089 0.0235  -0.0182 155 PHE B O   
2216 C CB  . PHE B 138 ? 0.2382 0.1386 0.1697 0.0131  -0.0335 -0.0209 155 PHE B CB  
2217 C CG  . PHE B 138 ? 0.2258 0.1286 0.1517 0.0628  -0.0291 -0.0258 155 PHE B CG  
2218 C CD1 . PHE B 138 ? 0.2473 0.1064 0.1451 0.0433  -0.0266 -0.0163 155 PHE B CD1 
2219 C CD2 . PHE B 138 ? 0.1555 0.1639 0.1481 0.0719  -0.0339 -0.0334 155 PHE B CD2 
2220 C CE1 . PHE B 138 ? 0.1688 0.0992 0.1469 0.0337  -0.0166 -0.0109 155 PHE B CE1 
2221 C CE2 . PHE B 138 ? 0.1843 0.1088 0.1433 0.0378  -0.0430 -0.0250 155 PHE B CE2 
2222 C CZ  . PHE B 138 ? 0.1829 0.1246 0.1433 0.0630  -0.0181 -0.0222 155 PHE B CZ  
2223 N N   . LYS B 139 ? 0.3529 0.1595 0.2320 0.0021  0.0293  -0.0286 156 LYS B N   
2224 C CA  . LYS B 139 ? 0.4591 0.2006 0.2516 -0.0221 0.0440  -0.0389 156 LYS B CA  
2225 C C   . LYS B 139 ? 0.4511 0.1477 0.2664 -0.0583 0.0754  -0.0515 156 LYS B C   
2226 O O   . LYS B 139 ? 0.4159 0.1526 0.2653 -0.0760 0.0909  -0.0577 156 LYS B O   
2227 C CB  . LYS B 139 ? 0.5501 0.2672 0.2603 0.0141  0.0180  -0.0306 156 LYS B CB  
2228 C CG  . LYS B 139 ? 0.6565 0.4615 0.2673 0.0762  0.0000  -0.0330 156 LYS B CG  
2229 C CD  . LYS B 139 ? 0.7165 0.5730 0.2742 0.1125  -0.0198 -0.0468 156 LYS B CD  
2230 C CE  . LYS B 139 ? 0.7510 0.6499 0.2790 0.1331  -0.0282 -0.0620 156 LYS B CE  
2231 N NZ  . LYS B 139 ? 0.7724 0.6939 0.2824 0.1565  -0.0283 -0.0736 156 LYS B NZ  
2232 N N   . PRO B 140 ? 0.4790 0.1631 0.2815 -0.0769 0.0893  -0.0557 157 PRO B N   
2233 C CA  . PRO B 140 ? 0.4536 0.2154 0.2821 -0.1458 0.1042  -0.0628 157 PRO B CA  
2234 C C   . PRO B 140 ? 0.4990 0.2430 0.2863 -0.1404 0.1244  -0.0892 157 PRO B C   
2235 O O   . PRO B 140 ? 0.4674 0.3414 0.2930 -0.1880 0.1156  -0.1253 157 PRO B O   
2236 C CB  . PRO B 140 ? 0.5239 0.2266 0.2956 -0.1377 0.0971  -0.0671 157 PRO B CB  
2237 C CG  . PRO B 140 ? 0.5341 0.2618 0.2970 -0.0967 0.0927  -0.0666 157 PRO B CG  
2238 C CD  . PRO B 140 ? 0.5013 0.1794 0.2895 -0.0893 0.0922  -0.0649 157 PRO B CD  
2239 N N   . GLU B 141 ? 0.5548 0.1930 0.2756 -0.1017 0.1455  -0.0525 158 GLU B N   
2240 C CA  . GLU B 141 ? 0.6250 0.2053 0.2681 -0.0659 0.1492  -0.0467 158 GLU B CA  
2241 C C   . GLU B 141 ? 0.5958 0.2052 0.2562 -0.0561 0.1346  -0.0364 158 GLU B C   
2242 O O   . GLU B 141 ? 0.6314 0.2244 0.2583 -0.1201 0.1478  -0.0194 158 GLU B O   
2243 C CB  . GLU B 141 ? 0.6733 0.2478 0.2705 -0.0137 0.1502  -0.0349 158 GLU B CB  
2244 N N   . GLU B 142 ? 0.4698 0.1411 0.2364 -0.0590 0.0971  -0.0227 159 GLU B N   
2245 C CA  . GLU B 142 ? 0.4551 0.1786 0.2172 -0.0073 0.0556  -0.0252 159 GLU B CA  
2246 C C   . GLU B 142 ? 0.3442 0.1392 0.2013 -0.0369 0.0556  -0.0096 159 GLU B C   
2247 O O   . GLU B 142 ? 0.2635 0.1398 0.1936 -0.0402 0.0296  0.0007  159 GLU B O   
2248 C CB  . GLU B 142 ? 0.4921 0.2147 0.2121 0.0238  0.0344  -0.0001 159 GLU B CB  
2249 C CG  . GLU B 142 ? 0.5624 0.2659 0.2137 0.1019  -0.0005 0.0257  159 GLU B CG  
2250 C CD  . GLU B 142 ? 0.6007 0.3118 0.2161 0.1688  -0.0192 0.0406  159 GLU B CD  
2251 O OE1 . GLU B 142 ? 0.5984 0.3194 0.2151 0.1877  -0.0324 0.0262  159 GLU B OE1 
2252 O OE2 . GLU B 142 ? 0.6677 0.3891 0.2241 0.1989  -0.0229 0.0468  159 GLU B OE2 
2253 N N   . ILE B 143 ? 0.3280 0.1505 0.2019 -0.0349 0.0601  -0.0266 160 ILE B N   
2254 C CA  . ILE B 143 ? 0.2531 0.2217 0.1962 -0.1224 0.0412  -0.0313 160 ILE B CA  
2255 C C   . ILE B 143 ? 0.2609 0.2103 0.1923 -0.0645 0.0512  0.0089  160 ILE B C   
2256 O O   . ILE B 143 ? 0.3157 0.1871 0.1988 -0.0780 0.0652  -0.0210 160 ILE B O   
2257 C CB  . ILE B 143 ? 0.3100 0.1984 0.1999 -0.1123 0.0383  -0.0466 160 ILE B CB  
2258 C CG1 . ILE B 143 ? 0.3285 0.2921 0.2065 -0.0964 0.0324  -0.0528 160 ILE B CG1 
2259 C CG2 . ILE B 143 ? 0.3121 0.2092 0.1967 -0.0574 0.0393  -0.0337 160 ILE B CG2 
2260 C CD1 . ILE B 143 ? 0.3694 0.3409 0.2103 -0.0498 0.0312  -0.0598 160 ILE B CD1 
2261 N N   . GLN B 144 ? 0.1899 0.1659 0.1857 -0.0327 0.0186  0.0225  161 GLN B N   
2262 C CA  . GLN B 144 ? 0.1900 0.1350 0.1813 -0.0153 -0.0101 0.0110  161 GLN B CA  
2263 C C   . GLN B 144 ? 0.1939 0.0901 0.1780 -0.0635 -0.0223 0.0054  161 GLN B C   
2264 O O   . GLN B 144 ? 0.2358 0.1125 0.1895 -0.0321 -0.0310 0.0166  161 GLN B O   
2265 C CB  . GLN B 144 ? 0.2119 0.1264 0.1839 -0.0009 -0.0257 -0.0023 161 GLN B CB  
2266 C CG  . GLN B 144 ? 0.2370 0.1408 0.1893 -0.0512 -0.0073 0.0142  161 GLN B CG  
2267 C CD  . GLN B 144 ? 0.2177 0.1398 0.1973 -0.0757 0.0034  0.0354  161 GLN B CD  
2268 O OE1 . GLN B 144 ? 0.2117 0.2683 0.2021 -0.0372 0.0144  0.0865  161 GLN B OE1 
2269 N NE2 . GLN B 144 ? 0.2339 0.2063 0.2028 0.0310  0.0102  0.0378  161 GLN B NE2 
2270 N N   . SER B 145 ? 0.2122 0.1145 0.1765 -0.0165 -0.0049 0.0143  162 SER B N   
2271 C CA  A SER B 145 ? 0.2073 0.1669 0.1782 -0.0408 0.0033  0.0059  162 SER B CA  
2272 C CA  B SER B 145 ? 0.2037 0.1444 0.1799 -0.0255 0.0160  0.0172  162 SER B CA  
2273 C C   . SER B 145 ? 0.1884 0.1626 0.1723 -0.0337 0.0079  0.0066  162 SER B C   
2274 O O   . SER B 145 ? 0.2763 0.1744 0.1767 0.0196  0.0248  0.0325  162 SER B O   
2275 C CB  A SER B 145 ? 0.2409 0.2241 0.1846 -0.0605 -0.0088 -0.0237 162 SER B CB  
2276 C CB  B SER B 145 ? 0.2655 0.1617 0.1888 0.0057  0.0106  -0.0131 162 SER B CB  
2277 O OG  A SER B 145 ? 0.2422 0.2475 0.1891 -0.1147 -0.0170 -0.0358 162 SER B OG  
2278 O OG  B SER B 145 ? 0.2746 0.1680 0.1943 0.0253  0.0164  -0.0112 162 SER B OG  
2279 N N   . TYR B 146 ? 0.1164 0.0997 0.1571 -0.0368 -0.0028 0.0169  163 TYR B N   
2280 C CA  . TYR B 146 ? 0.1134 0.1391 0.1421 -0.0089 -0.0265 -0.0028 163 TYR B CA  
2281 C C   . TYR B 146 ? 0.1320 0.1444 0.1364 -0.0505 -0.0151 0.0125  163 TYR B C   
2282 O O   . TYR B 146 ? 0.1847 0.1882 0.1326 -0.0444 0.0074  0.0287  163 TYR B O   
2283 C CB  . TYR B 146 ? 0.1428 0.1538 0.1327 0.0126  -0.0344 -0.0091 163 TYR B CB  
2284 C CG  . TYR B 146 ? 0.0919 0.1254 0.1268 -0.0567 -0.0241 -0.0013 163 TYR B CG  
2285 C CD1 . TYR B 146 ? 0.1535 0.1431 0.1292 -0.0313 -0.0106 0.0326  163 TYR B CD1 
2286 C CD2 . TYR B 146 ? 0.1139 0.1584 0.1234 -0.0325 -0.0172 -0.0114 163 TYR B CD2 
2287 C CE1 . TYR B 146 ? 0.1488 0.0921 0.1224 -0.0407 -0.0054 0.0156  163 TYR B CE1 
2288 C CE2 . TYR B 146 ? 0.0941 0.1436 0.1165 0.0096  -0.0155 -0.0182 163 TYR B CE2 
2289 C CZ  . TYR B 146 ? 0.0808 0.0988 0.1154 -0.0492 -0.0168 -0.0007 163 TYR B CZ  
2290 O OH  . TYR B 146 ? 0.1186 0.1149 0.1153 -0.0179 -0.0261 -0.0004 163 TYR B OH  
2291 N N   . LYS B 147 ? 0.1695 0.1055 0.1399 -0.0251 -0.0114 0.0110  164 LYS B N   
2292 C CA  . LYS B 147 ? 0.1739 0.0772 0.1506 -0.0229 -0.0282 0.0089  164 LYS B CA  
2293 C C   . LYS B 147 ? 0.1785 0.1261 0.1461 -0.0782 -0.0173 0.0005  164 LYS B C   
2294 O O   . LYS B 147 ? 0.1976 0.1660 0.1325 -0.0666 -0.0139 0.0088  164 LYS B O   
2295 C CB  . LYS B 147 ? 0.2402 0.1459 0.1725 -0.0808 -0.0513 0.0156  164 LYS B CB  
2296 C CG  . LYS B 147 ? 0.3107 0.2568 0.1985 -0.0795 -0.0687 0.0237  164 LYS B CG  
2297 C CD  . LYS B 147 ? 0.3952 0.3206 0.2162 0.0002  -0.0673 0.0598  164 LYS B CD  
2298 C CE  . LYS B 147 ? 0.5472 0.3839 0.2297 0.1332  -0.0570 0.0734  164 LYS B CE  
2299 N NZ  . LYS B 147 ? 0.6486 0.4156 0.2413 0.2012  -0.0497 0.0541  164 LYS B NZ  
2300 N N   . LEU B 148 ? 0.1362 0.1619 0.1503 -0.0089 -0.0196 0.0081  165 LEU B N   
2301 C CA  . LEU B 148 ? 0.1014 0.1585 0.1513 -0.0336 -0.0151 0.0114  165 LEU B CA  
2302 C C   . LEU B 148 ? 0.1259 0.1340 0.1427 -0.0185 -0.0191 0.0252  165 LEU B C   
2303 O O   . LEU B 148 ? 0.1503 0.1012 0.1491 -0.0267 -0.0333 0.0283  165 LEU B O   
2304 C CB  . LEU B 148 ? 0.1506 0.1546 0.1628 -0.0422 -0.0188 0.0086  165 LEU B CB  
2305 C CG  . LEU B 148 ? 0.1691 0.1325 0.1689 0.0254  -0.0165 0.0229  165 LEU B CG  
2306 C CD1 . LEU B 148 ? 0.1290 0.1602 0.1721 -0.0026 -0.0424 0.0189  165 LEU B CD1 
2307 C CD2 . LEU B 148 ? 0.1137 0.2026 0.1751 -0.0049 -0.0123 0.0075  165 LEU B CD2 
2308 N N   . ALA B 149 ? 0.1278 0.1917 0.1290 0.0152  -0.0065 0.0511  166 ALA B N   
2309 C CA  . ALA B 149 ? 0.1822 0.1545 0.1345 -0.0364 -0.0118 0.0369  166 ALA B CA  
2310 C C   . ALA B 149 ? 0.1512 0.1678 0.1366 -0.0193 -0.0111 0.0118  166 ALA B C   
2311 O O   . ALA B 149 ? 0.1534 0.2227 0.1455 -0.0119 -0.0095 0.0213  166 ALA B O   
2312 C CB  . ALA B 149 ? 0.2671 0.2365 0.1334 0.0395  0.0042  0.0320  166 ALA B CB  
2313 N N   . LEU B 150 ? 0.1691 0.1384 0.1324 0.0264  -0.0108 0.0229  167 LEU B N   
2314 C CA  . LEU B 150 ? 0.1709 0.1404 0.1434 0.0062  -0.0050 0.0034  167 LEU B CA  
2315 C C   . LEU B 150 ? 0.1383 0.1312 0.1445 -0.0328 -0.0019 0.0061  167 LEU B C   
2316 O O   . LEU B 150 ? 0.1301 0.1141 0.1403 -0.0273 -0.0237 0.0072  167 LEU B O   
2317 C CB  . LEU B 150 ? 0.2468 0.2479 0.1539 -0.0074 -0.0406 -0.0171 167 LEU B CB  
2318 C CG  . LEU B 150 ? 0.2725 0.2583 0.1716 -0.1114 -0.0624 -0.0300 167 LEU B CG  
2319 C CD1 . LEU B 150 ? 0.3522 0.2218 0.1750 -0.0778 -0.0584 -0.0200 167 LEU B CD1 
2320 C CD2 . LEU B 150 ? 0.3371 0.3580 0.1725 -0.0768 -0.0369 -0.0160 167 LEU B CD2 
2321 N N   . SER B 151 ? 0.1644 0.1235 0.1502 -0.0362 0.0082  0.0052  168 SER B N   
2322 C CA  A SER B 151 ? 0.1988 0.1102 0.1565 -0.0104 0.0029  0.0112  168 SER B CA  
2323 C CA  B SER B 151 ? 0.1885 0.1091 0.1516 0.0254  0.0083  0.0240  168 SER B CA  
2324 C C   . SER B 151 ? 0.1585 0.1105 0.1600 -0.0348 0.0010  0.0341  168 SER B C   
2325 O O   . SER B 151 ? 0.1399 0.1081 0.1603 -0.0333 -0.0087 0.0331  168 SER B O   
2326 C CB  A SER B 151 ? 0.2407 0.0938 0.1609 -0.0463 -0.0027 -0.0154 168 SER B CB  
2327 C CB  B SER B 151 ? 0.1992 0.1119 0.1472 0.0351  0.0124  0.0143  168 SER B CB  
2328 O OG  A SER B 151 ? 0.2377 0.1022 0.1649 -0.0728 0.0027  -0.0142 168 SER B OG  
2329 O OG  B SER B 151 ? 0.1603 0.1118 0.1414 0.0359  0.0326  0.0345  168 SER B OG  
2330 N N   . ASP B 152 ? 0.1410 0.1437 0.1694 -0.0517 -0.0157 0.0229  169 ASP B N   
2331 C CA  . ASP B 152 ? 0.1635 0.1892 0.1879 0.0194  -0.0103 0.0291  169 ASP B CA  
2332 C C   . ASP B 152 ? 0.1478 0.1502 0.1776 -0.0173 -0.0230 0.0210  169 ASP B C   
2333 O O   . ASP B 152 ? 0.1420 0.2060 0.1870 0.0037  -0.0489 0.0316  169 ASP B O   
2334 C CB  . ASP B 152 ? 0.1721 0.2741 0.2203 -0.0443 0.0043  0.0298  169 ASP B CB  
2335 C CG  . ASP B 152 ? 0.2465 0.3690 0.2450 -0.0613 0.0145  0.0290  169 ASP B CG  
2336 O OD1 . ASP B 152 ? 0.2604 0.3893 0.2546 -0.1395 0.0058  0.0326  169 ASP B OD1 
2337 O OD2 . ASP B 152 ? 0.2932 0.4075 0.2645 -0.0515 0.0379  0.0443  169 ASP B OD2 
2338 N N   . TYR B 153 ? 0.1273 0.1216 0.1664 -0.0244 -0.0058 0.0036  170 TYR B N   
2339 C CA  . TYR B 153 ? 0.1050 0.0852 0.1576 0.0090  -0.0015 0.0010  170 TYR B CA  
2340 C C   . TYR B 153 ? 0.0886 0.0815 0.1639 -0.0417 -0.0004 -0.0084 170 TYR B C   
2341 O O   . TYR B 153 ? 0.1165 0.0964 0.1576 -0.0022 0.0237  0.0015  170 TYR B O   
2342 C CB  . TYR B 153 ? 0.1345 0.1372 0.1538 0.0334  -0.0011 -0.0130 170 TYR B CB  
2343 C CG  . TYR B 153 ? 0.1123 0.1585 0.1476 -0.0105 0.0057  -0.0193 170 TYR B CG  
2344 C CD1 . TYR B 153 ? 0.1253 0.1705 0.1449 0.0477  0.0140  -0.0309 170 TYR B CD1 
2345 C CD2 . TYR B 153 ? 0.1772 0.1627 0.1494 0.0471  -0.0032 -0.0068 170 TYR B CD2 
2346 C CE1 . TYR B 153 ? 0.1179 0.2549 0.1443 0.0035  0.0301  -0.0379 170 TYR B CE1 
2347 C CE2 . TYR B 153 ? 0.1724 0.1917 0.1502 -0.0014 0.0095  -0.0256 170 TYR B CE2 
2348 C CZ  . TYR B 153 ? 0.1304 0.2487 0.1532 -0.0445 0.0365  -0.0270 170 TYR B CZ  
2349 O OH  . TYR B 153 ? 0.1479 0.3463 0.1641 -0.0581 0.0533  -0.0267 170 TYR B OH  
2350 N N   . ILE B 154 ? 0.1179 0.0858 0.1801 -0.0069 0.0265  0.0100  171 ILE B N   
2351 C CA  . ILE B 154 ? 0.1146 0.1107 0.1859 -0.0217 0.0315  0.0064  171 ILE B CA  
2352 C C   . ILE B 154 ? 0.1318 0.1093 0.1839 -0.0090 0.0175  0.0190  171 ILE B C   
2353 O O   . ILE B 154 ? 0.1826 0.1162 0.1858 -0.0057 0.0246  0.0262  171 ILE B O   
2354 C CB  . ILE B 154 ? 0.0729 0.2307 0.1900 -0.0199 0.0152  -0.0172 171 ILE B CB  
2355 C CG1 . ILE B 154 ? 0.1751 0.2871 0.1924 0.0630  -0.0052 -0.0251 171 ILE B CG1 
2356 C CG2 . ILE B 154 ? 0.1294 0.1903 0.1921 -0.0197 0.0323  -0.0058 171 ILE B CG2 
2357 C CD1 . ILE B 154 ? 0.1271 0.2800 0.1967 0.0017  -0.0201 -0.0045 171 ILE B CD1 
2358 N N   . PHE B 155 ? 0.1340 0.1598 0.1814 -0.0146 0.0073  0.0404  172 PHE B N   
2359 C CA  . PHE B 155 ? 0.1400 0.2017 0.1812 -0.0008 0.0084  0.0322  172 PHE B CA  
2360 C C   . PHE B 155 ? 0.1127 0.3273 0.1998 -0.0134 -0.0055 0.0377  172 PHE B C   
2361 O O   . PHE B 155 ? 0.1508 0.3430 0.2068 0.0695  -0.0116 0.0123  172 PHE B O   
2362 C CB  . PHE B 155 ? 0.1085 0.1533 0.1714 -0.0319 0.0048  0.0133  172 PHE B CB  
2363 C CG  . PHE B 155 ? 0.1320 0.1310 0.1579 0.0035  -0.0083 0.0247  172 PHE B CG  
2364 C CD1 . PHE B 155 ? 0.1196 0.1381 0.1574 -0.0413 0.0084  0.0217  172 PHE B CD1 
2365 C CD2 . PHE B 155 ? 0.1704 0.1701 0.1569 0.0229  0.0035  0.0305  172 PHE B CD2 
2366 C CE1 . PHE B 155 ? 0.1594 0.2206 0.1564 0.0204  -0.0054 0.0042  172 PHE B CE1 
2367 C CE2 . PHE B 155 ? 0.1379 0.2236 0.1589 0.0565  -0.0117 0.0366  172 PHE B CE2 
2368 C CZ  . PHE B 155 ? 0.1469 0.2358 0.1586 0.0818  -0.0262 0.0317  172 PHE B CZ  
2369 N N   . GLU B 156 ? 0.1634 0.4833 0.2209 0.0167  -0.0322 0.0504  173 GLU B N   
2370 C CA  . GLU B 156 ? 0.1957 0.6126 0.2465 0.0325  -0.0510 0.0546  173 GLU B CA  
2371 C C   . GLU B 156 ? 0.2300 0.6937 0.2633 -0.0141 -0.0643 0.0340  173 GLU B C   
2372 O O   . GLU B 156 ? 0.2517 0.7472 0.2767 0.0058  -0.0746 0.0115  173 GLU B O   
2373 C CB  . GLU B 156 ? 0.2637 0.6185 0.2568 0.0882  -0.0583 0.0676  173 GLU B CB  
2374 C CG  . GLU B 156 ? 0.3631 0.5901 0.2650 0.1541  -0.0652 0.0548  173 GLU B CG  
2375 C CD  . GLU B 156 ? 0.3324 0.4394 0.2673 0.0493  -0.0781 0.0188  173 GLU B CD  
2376 O OE1 . GLU B 156 ? 0.3486 0.3808 0.2718 -0.0508 -0.0694 0.0191  173 GLU B OE1 
2377 O OE2 . GLU B 156 ? 0.2471 0.1835 0.2680 -0.0637 -0.0870 0.0093  173 GLU B OE2 
2378 O OXT . GLU B 156 ? 0.2292 0.6492 0.2733 -0.1220 -0.0501 0.0409  173 GLU B OXT 
2379 N N   . HIS C 8   ? 0.6381 0.4254 0.2843 0.2519  0.0331  -0.0366 25  HIS C N   
2380 C CA  . HIS C 8   ? 0.5281 0.3845 0.2727 0.2371  0.0267  -0.0478 25  HIS C CA  
2381 C C   . HIS C 8   ? 0.3776 0.3698 0.2528 0.1835  0.0123  -0.0515 25  HIS C C   
2382 O O   . HIS C 8   ? 0.3500 0.5032 0.2621 0.2145  0.0191  -0.0677 25  HIS C O   
2383 C CB  . HIS C 8   ? 0.5687 0.4343 0.2728 0.2640  0.0189  -0.0503 25  HIS C CB  
2384 N N   . VAL C 9   ? 0.2609 0.1186 0.2274 0.0743  0.0266  -0.0243 26  VAL C N   
2385 C CA  . VAL C 9   ? 0.2230 0.0944 0.1947 0.0352  0.0539  -0.0020 26  VAL C CA  
2386 C C   . VAL C 9   ? 0.2042 0.1528 0.1785 0.0349  0.0648  0.0168  26  VAL C C   
2387 O O   . VAL C 9   ? 0.1553 0.2817 0.1908 0.0363  0.0672  0.0095  26  VAL C O   
2388 C CB  . VAL C 9   ? 0.1589 0.0837 0.1908 -0.0099 0.0459  -0.0052 26  VAL C CB  
2389 C CG1 . VAL C 9   ? 0.2055 0.1644 0.1960 0.0143  0.0385  -0.0010 26  VAL C CG1 
2390 C CG2 . VAL C 9   ? 0.1780 0.1273 0.1960 -0.0278 0.0431  -0.0169 26  VAL C CG2 
2391 N N   . GLU C 10  ? 0.1431 0.1035 0.1582 0.0044  0.0324  0.0045  27  GLU C N   
2392 C CA  . GLU C 10  ? 0.1282 0.1223 0.1362 0.0443  0.0245  0.0031  27  GLU C CA  
2393 C C   . GLU C 10  ? 0.0454 0.1175 0.1139 0.0099  0.0277  0.0113  27  GLU C C   
2394 O O   . GLU C 10  ? 0.1235 0.1041 0.1034 0.0122  0.0525  -0.0032 27  GLU C O   
2395 C CB  . GLU C 10  ? 0.1749 0.1995 0.1315 0.0834  0.0230  0.0258  27  GLU C CB  
2396 C CG  . GLU C 10  ? 0.1084 0.1472 0.1309 0.0548  0.0055  0.0197  27  GLU C CG  
2397 C CD  . GLU C 10  ? 0.1509 0.2667 0.1385 0.0434  -0.0043 0.0106  27  GLU C CD  
2398 O OE1 . GLU C 10  ? 0.2249 0.4022 0.1532 0.1225  -0.0001 -0.0044 27  GLU C OE1 
2399 O OE2 . GLU C 10  ? 0.1383 0.1164 0.1352 -0.0013 -0.0007 0.0036  27  GLU C OE2 
2400 N N   . GLN C 11  ? 0.0747 0.1079 0.1197 0.0252  0.0386  0.0240  28  GLN C N   
2401 C CA  . GLN C 11  ? 0.0834 0.1079 0.1155 0.0216  0.0274  0.0239  28  GLN C CA  
2402 C C   . GLN C 11  ? 0.0968 0.0851 0.0976 -0.0017 0.0350  0.0249  28  GLN C C   
2403 O O   . GLN C 11  ? 0.1091 0.1195 0.0965 0.0244  0.0271  0.0480  28  GLN C O   
2404 C CB  . GLN C 11  ? 0.1057 0.1321 0.1275 -0.0356 0.0384  0.0240  28  GLN C CB  
2405 C CG  . GLN C 11  ? 0.1490 0.1207 0.1365 0.0237  0.0027  0.0350  28  GLN C CG  
2406 C CD  . GLN C 11  ? 0.1699 0.1827 0.1507 0.0236  -0.0404 0.0183  28  GLN C CD  
2407 O OE1 . GLN C 11  ? 0.1803 0.2201 0.1606 -0.0121 -0.0529 0.0104  28  GLN C OE1 
2408 N NE2 . GLN C 11  ? 0.1901 0.1891 0.1551 0.0514  -0.0485 0.0089  28  GLN C NE2 
2409 N N   . THR C 12  ? 0.0709 0.1058 0.0860 0.0162  0.0270  0.0090  29  THR C N   
2410 C CA  . THR C 12  ? 0.0563 0.1116 0.0866 0.0210  0.0134  0.0119  29  THR C CA  
2411 C C   . THR C 12  ? 0.0756 0.1179 0.0858 -0.0242 0.0109  0.0155  29  THR C C   
2412 O O   . THR C 12  ? 0.1148 0.1025 0.0817 -0.0066 0.0120  0.0141  29  THR C O   
2413 C CB  . THR C 12  ? 0.0992 0.1317 0.0855 0.0038  0.0120  0.0143  29  THR C CB  
2414 O OG1 . THR C 12  ? 0.1405 0.1006 0.0874 0.0020  -0.0139 0.0009  29  THR C OG1 
2415 C CG2 . THR C 12  ? 0.1468 0.1062 0.0878 0.0339  0.0004  -0.0228 29  THR C CG2 
2416 N N   . TYR C 13  ? 0.1100 0.1045 0.0861 0.0133  0.0275  0.0197  30  TYR C N   
2417 C CA  . TYR C 13  ? 0.0627 0.1302 0.0813 -0.0142 0.0180  0.0270  30  TYR C CA  
2418 C C   . TYR C 13  ? 0.0878 0.1401 0.0836 -0.0172 0.0205  0.0371  30  TYR C C   
2419 O O   . TYR C 13  ? 0.1009 0.1287 0.0849 -0.0065 0.0221  0.0286  30  TYR C O   
2420 C CB  . TYR C 13  ? 0.0521 0.1338 0.0786 0.0029  0.0213  0.0296  30  TYR C CB  
2421 C CG  . TYR C 13  ? 0.0979 0.0613 0.0771 -0.0136 0.0191  0.0007  30  TYR C CG  
2422 C CD1 . TYR C 13  ? 0.1055 0.1086 0.0787 0.0142  -0.0010 -0.0033 30  TYR C CD1 
2423 C CD2 . TYR C 13  ? 0.0822 0.1089 0.0744 -0.0027 0.0378  0.0046  30  TYR C CD2 
2424 C CE1 . TYR C 13  ? 0.1203 0.1059 0.0813 0.0196  0.0059  0.0053  30  TYR C CE1 
2425 C CE2 . TYR C 13  ? 0.0936 0.0929 0.0783 0.0143  0.0248  0.0078  30  TYR C CE2 
2426 C CZ  . TYR C 13  ? 0.1072 0.1282 0.0845 -0.0152 0.0113  -0.0025 30  TYR C CZ  
2427 O OH  . TYR C 13  ? 0.1214 0.1300 0.0939 0.0065  0.0069  -0.0144 30  TYR C OH  
2428 N N   . LEU C 14  ? 0.0532 0.1284 0.0816 0.0043  0.0007  0.0121  31  LEU C N   
2429 C CA  . LEU C 14  ? 0.0866 0.1291 0.0893 0.0502  0.0134  0.0250  31  LEU C CA  
2430 C C   . LEU C 14  ? 0.0682 0.0793 0.0877 0.0229  0.0018  -0.0088 31  LEU C C   
2431 O O   . LEU C 14  ? 0.0863 0.1366 0.0926 0.0354  -0.0198 -0.0260 31  LEU C O   
2432 C CB  . LEU C 14  ? 0.0847 0.1476 0.0947 -0.0026 0.0245  0.0333  31  LEU C CB  
2433 C CG  . LEU C 14  ? 0.1286 0.0975 0.1111 0.0026  0.0157  0.0206  31  LEU C CG  
2434 C CD1 . LEU C 14  ? 0.1695 0.1669 0.1135 -0.0008 -0.0175 0.0008  31  LEU C CD1 
2435 C CD2 . LEU C 14  ? 0.1670 0.0655 0.1147 0.0293  0.0114  0.0307  31  LEU C CD2 
2436 N N   . MET C 15  ? 0.0839 0.1097 0.0865 0.0104  0.0230  0.0009  32  MET C N   
2437 C CA  . MET C 15  ? 0.0848 0.1201 0.0925 0.0088  0.0319  0.0054  32  MET C CA  
2438 C C   . MET C 15  ? 0.0646 0.0994 0.0838 0.0019  0.0276  0.0149  32  MET C C   
2439 O O   . MET C 15  ? 0.1079 0.1560 0.0771 -0.0075 0.0184  -0.0079 32  MET C O   
2440 C CB  . MET C 15  ? 0.1228 0.0938 0.1089 -0.0225 0.0372  0.0093  32  MET C CB  
2441 C CG  . MET C 15  ? 0.1447 0.0851 0.1297 0.0377  0.0376  0.0095  32  MET C CG  
2442 S SD  . MET C 15  ? 0.1414 0.1245 0.1462 -0.0218 0.0227  -0.0025 32  MET C SD  
2443 C CE  . MET C 15  ? 0.1311 0.1381 0.1467 -0.0228 0.0189  0.0316  32  MET C CE  
2444 N N   . ILE C 16  ? 0.0938 0.0900 0.0827 0.0203  0.0280  0.0125  33  ILE C N   
2445 C CA  . ILE C 16  ? 0.0890 0.1093 0.0806 0.0080  0.0188  0.0089  33  ILE C CA  
2446 C C   . ILE C 16  ? 0.0635 0.1256 0.0780 0.0138  0.0114  0.0004  33  ILE C C   
2447 O O   . ILE C 16  ? 0.0959 0.1449 0.0782 -0.0040 0.0018  0.0023  33  ILE C O   
2448 C CB  . ILE C 16  ? 0.0739 0.0827 0.0905 -0.0076 0.0058  -0.0012 33  ILE C CB  
2449 C CG1 . ILE C 16  ? 0.0740 0.1128 0.0930 -0.0088 0.0102  0.0159  33  ILE C CG1 
2450 C CG2 . ILE C 16  ? 0.0509 0.1544 0.0922 0.0156  0.0030  0.0050  33  ILE C CG2 
2451 C CD1 . ILE C 16  ? 0.1273 0.1395 0.0921 0.0227  0.0261  0.0174  33  ILE C CD1 
2452 N N   . LYS C 17  ? 0.0789 0.1155 0.0792 0.0078  0.0092  -0.0163 34  LYS C N   
2453 C CA  . LYS C 17  ? 0.0864 0.0594 0.0831 -0.0063 0.0048  -0.0223 34  LYS C CA  
2454 C C   . LYS C 17  ? 0.0671 0.1030 0.0906 -0.0256 0.0151  -0.0211 34  LYS C C   
2455 O O   . LYS C 17  ? 0.0843 0.0921 0.0977 -0.0174 0.0287  0.0128  34  LYS C O   
2456 C CB  . LYS C 17  ? 0.1331 0.0555 0.0810 -0.0143 0.0206  -0.0049 34  LYS C CB  
2457 C CG  . LYS C 17  ? 0.1369 0.0883 0.0900 0.0388  0.0119  0.0137  34  LYS C CG  
2458 C CD  . LYS C 17  ? 0.0967 0.1547 0.0981 -0.0197 0.0082  0.0181  34  LYS C CD  
2459 C CE  . LYS C 17  ? 0.1433 0.1754 0.0982 -0.0101 0.0166  0.0205  34  LYS C CE  
2460 N NZ  . LYS C 17  ? 0.0704 0.1626 0.1043 -0.0402 0.0022  0.0203  34  LYS C NZ  
2461 N N   . PRO C 18  ? 0.1233 0.0477 0.0896 -0.0142 0.0210  0.0090  35  PRO C N   
2462 C CA  . PRO C 18  ? 0.0723 0.0720 0.0858 -0.0070 0.0028  0.0048  35  PRO C CA  
2463 C C   . PRO C 18  ? 0.1224 0.1009 0.0808 0.0109  0.0091  0.0028  35  PRO C C   
2464 O O   . PRO C 18  ? 0.1008 0.1185 0.0784 -0.0052 -0.0028 -0.0017 35  PRO C O   
2465 C CB  . PRO C 18  ? 0.1090 0.1062 0.0940 0.0221  0.0064  0.0026  35  PRO C CB  
2466 C CG  . PRO C 18  ? 0.1259 0.0865 0.0909 0.0011  -0.0012 0.0118  35  PRO C CG  
2467 C CD  . PRO C 18  ? 0.1193 0.0740 0.0919 -0.0219 0.0085  0.0074  35  PRO C CD  
2468 N N   . ASP C 19  ? 0.0932 0.0884 0.0801 -0.0218 -0.0031 0.0062  36  ASP C N   
2469 C CA  . ASP C 19  ? 0.0888 0.0908 0.0799 0.0298  0.0033  0.0095  36  ASP C CA  
2470 C C   . ASP C 19  ? 0.0722 0.1383 0.0861 -0.0074 -0.0074 -0.0185 36  ASP C C   
2471 O O   . ASP C 19  ? 0.1041 0.1234 0.0902 -0.0086 0.0252  -0.0030 36  ASP C O   
2472 C CB  . ASP C 19  ? 0.1225 0.1185 0.0854 0.0183  0.0047  0.0185  36  ASP C CB  
2473 C CG  . ASP C 19  ? 0.1144 0.1380 0.0962 0.0161  0.0035  0.0072  36  ASP C CG  
2474 O OD1 . ASP C 19  ? 0.1043 0.1801 0.1002 0.0217  -0.0006 -0.0333 36  ASP C OD1 
2475 O OD2 . ASP C 19  ? 0.1263 0.1246 0.0926 0.0088  0.0037  0.0184  36  ASP C OD2 
2476 N N   . GLY C 20  ? 0.1140 0.1441 0.0843 -0.0247 0.0058  -0.0240 37  GLY C N   
2477 C CA  . GLY C 20  ? 0.0474 0.1369 0.0912 0.0170  -0.0003 -0.0185 37  GLY C CA  
2478 C C   . GLY C 20  ? 0.0526 0.0954 0.0942 -0.0134 0.0229  -0.0060 37  GLY C C   
2479 O O   . GLY C 20  ? 0.0958 0.1012 0.0988 -0.0193 0.0204  -0.0109 37  GLY C O   
2480 N N   . ILE C 21  ? 0.0599 0.0903 0.0943 -0.0335 0.0019  0.0112  38  ILE C N   
2481 C CA  . ILE C 21  ? 0.1028 0.1214 0.0916 0.0379  -0.0158 -0.0089 38  ILE C CA  
2482 C C   . ILE C 21  ? 0.0727 0.0991 0.0847 -0.0338 0.0058  0.0008  38  ILE C C   
2483 O O   . ILE C 21  ? 0.0950 0.1144 0.0858 -0.0180 0.0082  0.0135  38  ILE C O   
2484 C CB  . ILE C 21  ? 0.0934 0.0962 0.0977 -0.0084 -0.0025 -0.0072 38  ILE C CB  
2485 C CG1 . ILE C 21  ? 0.1399 0.1248 0.1109 0.0042  -0.0109 -0.0136 38  ILE C CG1 
2486 C CG2 . ILE C 21  ? 0.1482 0.1597 0.0942 -0.0488 0.0050  0.0057  38  ILE C CG2 
2487 C CD1 . ILE C 21  ? 0.1562 0.0978 0.1183 -0.0073 0.0056  -0.0071 38  ILE C CD1 
2488 N N   . GLN C 22  ? 0.1031 0.1008 0.0893 0.0118  0.0205  -0.0121 39  GLN C N   
2489 C CA  . GLN C 22  ? 0.1438 0.0818 0.0997 -0.0146 0.0239  -0.0145 39  GLN C CA  
2490 C C   . GLN C 22  ? 0.1487 0.0697 0.1005 0.0065  0.0037  -0.0110 39  GLN C C   
2491 O O   . GLN C 22  ? 0.1402 0.0984 0.1042 0.0101  -0.0132 -0.0288 39  GLN C O   
2492 C CB  . GLN C 22  ? 0.1486 0.0458 0.1142 -0.0015 0.0199  -0.0160 39  GLN C CB  
2493 C CG  . GLN C 22  ? 0.1894 0.0535 0.1251 0.0138  0.0246  0.0021  39  GLN C CG  
2494 C CD  . GLN C 22  ? 0.1840 0.0745 0.1328 -0.0334 0.0398  -0.0130 39  GLN C CD  
2495 O OE1 . GLN C 22  ? 0.2627 0.1500 0.1268 -0.0673 0.0492  -0.0323 39  GLN C OE1 
2496 N NE2 . GLN C 22  ? 0.1575 0.1042 0.1385 -0.0228 0.0330  -0.0230 39  GLN C NE2 
2497 N N   . ARG C 23  ? 0.0800 0.0733 0.0998 0.0245  0.0039  -0.0064 40  ARG C N   
2498 C CA  . ARG C 23  ? 0.0780 0.0560 0.1041 -0.0045 0.0023  -0.0193 40  ARG C CA  
2499 C C   . ARG C 23  ? 0.0872 0.0929 0.1088 -0.0378 0.0094  0.0018  40  ARG C C   
2500 O O   . ARG C 23  ? 0.0888 0.1125 0.1192 0.0072  0.0118  0.0306  40  ARG C O   
2501 C CB  . ARG C 23  ? 0.1181 0.0755 0.1056 0.0010  0.0160  -0.0164 40  ARG C CB  
2502 C CG  . ARG C 23  ? 0.0811 0.0976 0.1044 -0.0159 0.0107  -0.0250 40  ARG C CG  
2503 C CD  . ARG C 23  ? 0.0969 0.0951 0.1064 -0.0231 0.0103  -0.0381 40  ARG C CD  
2504 N NE  . ARG C 23  ? 0.0913 0.1264 0.1108 -0.0387 0.0037  -0.0311 40  ARG C NE  
2505 C CZ  . ARG C 23  ? 0.0792 0.0875 0.1100 -0.0009 -0.0096 -0.0195 40  ARG C CZ  
2506 N NH1 . ARG C 23  ? 0.0745 0.0879 0.1169 0.0090  0.0148  -0.0073 40  ARG C NH1 
2507 N NH2 . ARG C 23  ? 0.0896 0.1551 0.1052 -0.0638 0.0046  -0.0124 40  ARG C NH2 
2508 N N   . GLN C 24  ? 0.0972 0.0744 0.1028 -0.0059 0.0056  0.0067  41  GLN C N   
2509 C CA  . GLN C 24  ? 0.0952 0.0844 0.0946 -0.0145 0.0099  0.0070  41  GLN C CA  
2510 C C   . GLN C 24  ? 0.0952 0.0667 0.0890 0.0017  0.0159  -0.0019 41  GLN C C   
2511 O O   . GLN C 24  ? 0.1121 0.1140 0.0878 -0.0180 0.0094  -0.0031 41  GLN C O   
2512 C CB  . GLN C 24  ? 0.1531 0.1253 0.0927 0.0076  -0.0141 0.0002  41  GLN C CB  
2513 C CG  . GLN C 24  ? 0.1654 0.1031 0.0930 -0.0178 0.0063  -0.0058 41  GLN C CG  
2514 C CD  . GLN C 24  ? 0.1745 0.1216 0.0934 0.0120  0.0079  0.0017  41  GLN C CD  
2515 O OE1 . GLN C 24  ? 0.1996 0.1600 0.0964 0.0214  0.0192  -0.0212 41  GLN C OE1 
2516 N NE2 . GLN C 24  ? 0.1834 0.1373 0.0913 -0.0037 0.0006  0.0241  41  GLN C NE2 
2517 N N   . VAL C 25  ? 0.0844 0.0912 0.0844 0.0047  0.0130  0.0000  42  VAL C N   
2518 C CA  . VAL C 25  ? 0.0649 0.0857 0.0878 -0.0117 0.0024  -0.0144 42  VAL C CA  
2519 C C   . VAL C 25  ? 0.0738 0.0992 0.0826 -0.0122 -0.0043 -0.0065 42  VAL C C   
2520 O O   . VAL C 25  ? 0.1005 0.0906 0.0862 0.0066  -0.0154 -0.0162 42  VAL C O   
2521 C CB  . VAL C 25  ? 0.0717 0.1039 0.0988 0.0110  -0.0363 -0.0088 42  VAL C CB  
2522 C CG1 . VAL C 25  ? 0.1136 0.1467 0.1101 -0.0120 -0.0521 -0.0116 42  VAL C CG1 
2523 C CG2 . VAL C 25  ? 0.1592 0.1744 0.0960 0.0595  -0.0235 -0.0107 42  VAL C CG2 
2524 N N   . VAL C 26  ? 0.0935 0.0603 0.0747 0.0017  0.0072  -0.0059 43  VAL C N   
2525 C CA  . VAL C 26  ? 0.0747 0.1034 0.0728 0.0108  0.0041  0.0034  43  VAL C CA  
2526 C C   . VAL C 26  ? 0.1160 0.0681 0.0752 0.0165  0.0206  0.0087  43  VAL C C   
2527 O O   . VAL C 26  ? 0.1025 0.1017 0.0759 -0.0067 0.0091  -0.0170 43  VAL C O   
2528 C CB  . VAL C 26  ? 0.0926 0.0710 0.0711 0.0049  0.0024  -0.0102 43  VAL C CB  
2529 C CG1 . VAL C 26  ? 0.1281 0.1246 0.0785 -0.0146 0.0165  -0.0237 43  VAL C CG1 
2530 C CG2 . VAL C 26  ? 0.1078 0.0763 0.0728 -0.0203 -0.0113 -0.0166 43  VAL C CG2 
2531 N N   . GLY C 27  ? 0.0806 0.0785 0.0807 0.0197  0.0188  0.0009  44  GLY C N   
2532 C CA  . GLY C 27  ? 0.0637 0.0739 0.0904 -0.0015 0.0085  -0.0004 44  GLY C CA  
2533 C C   . GLY C 27  ? 0.0632 0.0587 0.0993 0.0164  0.0146  0.0013  44  GLY C C   
2534 O O   . GLY C 27  ? 0.0778 0.1047 0.1001 0.0240  0.0091  0.0078  44  GLY C O   
2535 N N   . GLU C 28  ? 0.0739 0.1046 0.1040 0.0133  0.0044  0.0028  45  GLU C N   
2536 C CA  . GLU C 28  ? 0.0973 0.0337 0.1114 -0.0004 -0.0009 0.0028  45  GLU C CA  
2537 C C   . GLU C 28  ? 0.0724 0.0520 0.0932 -0.0011 -0.0034 0.0114  45  GLU C C   
2538 O O   . GLU C 28  ? 0.1118 0.0859 0.0896 -0.0035 -0.0143 -0.0016 45  GLU C O   
2539 C CB  . GLU C 28  ? 0.1176 0.0772 0.1406 0.0485  0.0121  -0.0030 45  GLU C CB  
2540 C CG  . GLU C 28  ? 0.1385 0.1365 0.1819 -0.0114 -0.0028 -0.0004 45  GLU C CG  
2541 C CD  . GLU C 28  ? 0.2009 0.2983 0.2221 0.0074  0.0078  0.0057  45  GLU C CD  
2542 O OE1 . GLU C 28  ? 0.3128 0.3979 0.2326 0.0740  -0.0072 0.0288  45  GLU C OE1 
2543 O OE2 . GLU C 28  ? 0.2672 0.2630 0.2424 0.0806  0.0114  0.0217  45  GLU C OE2 
2544 N N   . ILE C 29  ? 0.0571 0.0699 0.0890 0.0052  0.0013  -0.0023 46  ILE C N   
2545 C CA  . ILE C 29  ? 0.0703 0.0841 0.0813 -0.0304 0.0069  -0.0231 46  ILE C CA  
2546 C C   . ILE C 29  ? 0.0953 0.0763 0.0733 0.0144  0.0159  -0.0108 46  ILE C C   
2547 O O   . ILE C 29  ? 0.1009 0.1020 0.0743 0.0168  0.0221  -0.0142 46  ILE C O   
2548 C CB  . ILE C 29  ? 0.0967 0.1128 0.0807 0.0026  0.0160  0.0216  46  ILE C CB  
2549 C CG1 . ILE C 29  ? 0.1070 0.1259 0.0957 0.0094  -0.0064 0.0489  46  ILE C CG1 
2550 C CG2 . ILE C 29  ? 0.1472 0.1169 0.0731 -0.0050 0.0098  0.0034  46  ILE C CG2 
2551 C CD1 . ILE C 29  ? 0.1274 0.1878 0.1078 -0.0067 -0.0078 0.0470  46  ILE C CD1 
2552 N N   . ILE C 30  ? 0.1039 0.0769 0.0697 0.0063  0.0084  -0.0015 47  ILE C N   
2553 C CA  . ILE C 30  ? 0.0899 0.0653 0.0721 0.0002  0.0211  -0.0006 47  ILE C CA  
2554 C C   . ILE C 30  ? 0.0641 0.1022 0.0715 0.0002  0.0120  -0.0125 47  ILE C C   
2555 O O   . ILE C 30  ? 0.0865 0.0930 0.0643 0.0112  -0.0037 -0.0141 47  ILE C O   
2556 C CB  . ILE C 30  ? 0.0867 0.0871 0.0790 0.0002  0.0210  0.0170  47  ILE C CB  
2557 C CG1 . ILE C 30  ? 0.0648 0.1175 0.0821 0.0221  0.0122  -0.0002 47  ILE C CG1 
2558 C CG2 . ILE C 30  ? 0.0637 0.1153 0.0872 -0.0070 0.0114  -0.0087 47  ILE C CG2 
2559 C CD1 . ILE C 30  ? 0.1019 0.1449 0.0864 0.0069  -0.0003 -0.0166 47  ILE C CD1 
2560 N N   . SER C 31  ? 0.0673 0.0901 0.0702 -0.0019 0.0119  0.0036  48  SER C N   
2561 C CA  . SER C 31  ? 0.0629 0.0908 0.0749 0.0199  0.0010  0.0094  48  SER C CA  
2562 C C   . SER C 31  ? 0.0609 0.1157 0.0805 0.0434  0.0013  0.0094  48  SER C C   
2563 O O   . SER C 31  ? 0.1089 0.1172 0.0788 0.0523  0.0161  0.0173  48  SER C O   
2564 C CB  . SER C 31  ? 0.0922 0.1194 0.0791 -0.0443 -0.0056 -0.0003 48  SER C CB  
2565 O OG  . SER C 31  ? 0.1089 0.0825 0.0824 -0.0026 -0.0065 -0.0121 48  SER C OG  
2566 N N   . ARG C 32  ? 0.0849 0.0780 0.0841 0.0075  -0.0179 -0.0016 49  ARG C N   
2567 C CA  . ARG C 32  ? 0.1062 0.0769 0.0894 0.0180  -0.0254 -0.0108 49  ARG C CA  
2568 C C   . ARG C 32  ? 0.1254 0.0834 0.0872 0.0139  0.0011  -0.0092 49  ARG C C   
2569 O O   . ARG C 32  ? 0.1060 0.1346 0.0817 -0.0288 0.0034  -0.0120 49  ARG C O   
2570 C CB  . ARG C 32  ? 0.1276 0.1480 0.1014 0.0228  -0.0131 0.0057  49  ARG C CB  
2571 C CG  . ARG C 32  ? 0.1039 0.1715 0.1215 0.0527  -0.0003 -0.0066 49  ARG C CG  
2572 C CD  . ARG C 32  ? 0.1317 0.2839 0.1410 0.0503  0.0303  0.0035  49  ARG C CD  
2573 N NE  . ARG C 32  ? 0.1570 0.3048 0.1499 0.0381  0.0209  0.0250  49  ARG C NE  
2574 C CZ  . ARG C 32  ? 0.1714 0.1637 0.1576 -0.0434 0.0196  0.0361  49  ARG C CZ  
2575 N NH1 . ARG C 32  ? 0.1304 0.2353 0.1575 -0.0015 0.0173  0.0402  49  ARG C NH1 
2576 N NH2 . ARG C 32  ? 0.2705 0.1443 0.1658 0.0217  0.0199  0.0033  49  ARG C NH2 
2577 N N   . PHE C 33  ? 0.1057 0.0870 0.0870 0.0085  0.0190  -0.0252 50  PHE C N   
2578 C CA  . PHE C 33  ? 0.0860 0.0746 0.0892 -0.0046 0.0105  -0.0257 50  PHE C CA  
2579 C C   . PHE C 33  ? 0.0898 0.0899 0.0855 -0.0103 0.0157  -0.0078 50  PHE C C   
2580 O O   . PHE C 33  ? 0.1015 0.1125 0.0870 0.0153  0.0184  -0.0099 50  PHE C O   
2581 C CB  . PHE C 33  ? 0.1181 0.1057 0.0980 -0.0003 0.0092  -0.0263 50  PHE C CB  
2582 C CG  . PHE C 33  ? 0.0605 0.0947 0.0915 -0.0230 0.0332  -0.0030 50  PHE C CG  
2583 C CD1 . PHE C 33  ? 0.1443 0.0784 0.0922 0.0053  0.0261  0.0029  50  PHE C CD1 
2584 C CD2 . PHE C 33  ? 0.1520 0.1161 0.0976 0.0660  0.0251  0.0120  50  PHE C CD2 
2585 C CE1 . PHE C 33  ? 0.1599 0.0898 0.0956 0.0040  0.0278  0.0368  50  PHE C CE1 
2586 C CE2 . PHE C 33  ? 0.1295 0.1527 0.0999 0.0574  0.0309  0.0260  50  PHE C CE2 
2587 C CZ  . PHE C 33  ? 0.1358 0.1171 0.0936 0.0334  0.0094  0.0278  50  PHE C CZ  
2588 N N   . GLU C 34  ? 0.1147 0.0882 0.0822 0.0128  0.0158  -0.0118 51  GLU C N   
2589 C CA  . GLU C 34  ? 0.1105 0.0926 0.0828 0.0206  -0.0039 -0.0119 51  GLU C CA  
2590 C C   . GLU C 34  ? 0.0816 0.0537 0.0850 0.0315  0.0117  -0.0147 51  GLU C C   
2591 O O   . GLU C 34  ? 0.1228 0.0791 0.0902 0.0250  0.0128  -0.0064 51  GLU C O   
2592 C CB  . GLU C 34  ? 0.0944 0.1455 0.0858 -0.0027 -0.0188 0.0008  51  GLU C CB  
2593 C CG  . GLU C 34  ? 0.0955 0.1675 0.0877 0.0154  0.0024  -0.0190 51  GLU C CG  
2594 C CD  . GLU C 34  ? 0.0927 0.1489 0.0926 0.0067  0.0129  0.0081  51  GLU C CD  
2595 O OE1 . GLU C 34  ? 0.1005 0.1090 0.0999 0.0044  0.0165  0.0003  51  GLU C OE1 
2596 O OE2 . GLU C 34  ? 0.1155 0.1585 0.0851 0.0121  0.0046  0.0022  51  GLU C OE2 
2597 N N   . LYS C 35  ? 0.1053 0.0918 0.0878 0.0160  -0.0001 -0.0209 52  LYS C N   
2598 C CA  . LYS C 35  ? 0.1167 0.1012 0.0975 0.0549  0.0119  -0.0218 52  LYS C CA  
2599 C C   . LYS C 35  ? 0.1043 0.0794 0.0961 0.0252  0.0083  -0.0258 52  LYS C C   
2600 O O   . LYS C 35  ? 0.1109 0.1121 0.1003 0.0156  0.0282  -0.0201 52  LYS C O   
2601 C CB  . LYS C 35  ? 0.0918 0.1175 0.1138 0.0173  0.0135  -0.0236 52  LYS C CB  
2602 C CG  . LYS C 35  ? 0.0924 0.1607 0.1325 -0.0223 0.0476  -0.0200 52  LYS C CG  
2603 C CD  . LYS C 35  ? 0.1752 0.2177 0.1487 -0.0416 0.0545  -0.0076 52  LYS C CD  
2604 C CE  . LYS C 35  ? 0.2685 0.2320 0.1629 0.0506  0.0719  0.0076  52  LYS C CE  
2605 N NZ  . LYS C 35  ? 0.3491 0.2965 0.1685 0.1214  0.0864  0.0137  52  LYS C NZ  
2606 N N   . ARG C 36  ? 0.0576 0.1118 0.0915 0.0394  0.0060  -0.0084 53  ARG C N   
2607 C CA  . ARG C 36  ? 0.0922 0.0833 0.0921 0.0042  0.0229  0.0021  53  ARG C CA  
2608 C C   . ARG C 36  ? 0.0754 0.0912 0.0902 0.0119  0.0109  0.0010  53  ARG C C   
2609 O O   . ARG C 36  ? 0.0755 0.1480 0.0877 0.0136  -0.0035 0.0040  53  ARG C O   
2610 C CB  . ARG C 36  ? 0.0966 0.0940 0.0927 -0.0215 0.0208  0.0139  53  ARG C CB  
2611 C CG  . ARG C 36  ? 0.1245 0.1044 0.0935 0.0219  -0.0144 -0.0048 53  ARG C CG  
2612 C CD  . ARG C 36  ? 0.1570 0.0743 0.0930 0.0117  -0.0080 -0.0119 53  ARG C CD  
2613 N NE  . ARG C 36  ? 0.1098 0.1265 0.0848 0.0312  -0.0096 -0.0028 53  ARG C NE  
2614 C CZ  . ARG C 36  ? 0.0944 0.1526 0.0922 0.0223  -0.0072 -0.0038 53  ARG C CZ  
2615 N NH1 . ARG C 36  ? 0.1226 0.1013 0.0976 0.0243  -0.0070 0.0014  53  ARG C NH1 
2616 N NH2 . ARG C 36  ? 0.1607 0.0949 0.0868 0.0049  -0.0019 -0.0092 53  ARG C NH2 
2617 N N   . GLY C 37  ? 0.0634 0.0672 0.0948 0.0236  0.0075  0.0060  54  GLY C N   
2618 C CA  . GLY C 37  ? 0.0926 0.1533 0.0919 0.0545  0.0115  0.0094  54  GLY C CA  
2619 C C   . GLY C 37  ? 0.1086 0.1493 0.0931 0.0593  0.0162  0.0107  54  GLY C C   
2620 O O   . GLY C 37  ? 0.1048 0.1078 0.1008 0.0361  0.0049  0.0086  54  GLY C O   
2621 N N   . TYR C 38  ? 0.0675 0.0855 0.0945 -0.0028 0.0106  -0.0044 55  TYR C N   
2622 C CA  . TYR C 38  ? 0.0626 0.1282 0.0922 0.0272  0.0103  -0.0008 55  TYR C CA  
2623 C C   . TYR C 38  ? 0.0732 0.0823 0.0871 -0.0107 -0.0065 -0.0022 55  TYR C C   
2624 O O   . TYR C 38  ? 0.0704 0.1661 0.0914 -0.0189 0.0168  0.0030  55  TYR C O   
2625 C CB  . TYR C 38  ? 0.0875 0.0556 0.0995 0.0108  0.0253  -0.0084 55  TYR C CB  
2626 C CG  . TYR C 38  ? 0.0519 0.0725 0.0998 -0.0045 0.0185  -0.0168 55  TYR C CG  
2627 C CD1 . TYR C 38  ? 0.0765 0.1151 0.0952 -0.0072 -0.0067 -0.0269 55  TYR C CD1 
2628 C CD2 . TYR C 38  ? 0.0853 0.1165 0.1015 0.0563  0.0119  0.0102  55  TYR C CD2 
2629 C CE1 . TYR C 38  ? 0.0596 0.0918 0.0932 0.0061  0.0067  -0.0163 55  TYR C CE1 
2630 C CE2 . TYR C 38  ? 0.0677 0.1221 0.0978 -0.0027 0.0096  0.0070  55  TYR C CE2 
2631 C CZ  . TYR C 38  ? 0.0623 0.1121 0.0952 0.0014  -0.0038 0.0106  55  TYR C CZ  
2632 O OH  . TYR C 38  ? 0.0874 0.1471 0.1117 0.0292  -0.0119 0.0013  55  TYR C OH  
2633 N N   . ARG C 39  ? 0.0517 0.1431 0.0839 0.0001  0.0001  0.0113  56  ARG C N   
2634 C CA  . ARG C 39  ? 0.0534 0.1412 0.0863 0.0008  0.0092  0.0106  56  ARG C CA  
2635 C C   . ARG C 39  ? 0.0476 0.1423 0.0878 -0.0031 0.0197  0.0187  56  ARG C C   
2636 O O   . ARG C 39  ? 0.0522 0.1640 0.0842 0.0151  0.0074  0.0108  56  ARG C O   
2637 C CB  . ARG C 39  ? 0.0492 0.1185 0.0927 -0.0040 0.0012  -0.0024 56  ARG C CB  
2638 C CG  . ARG C 39  ? 0.0669 0.1558 0.0941 -0.0007 -0.0027 -0.0107 56  ARG C CG  
2639 C CD  . ARG C 39  ? 0.0855 0.1383 0.1027 0.0167  0.0120  -0.0023 56  ARG C CD  
2640 N NE  . ARG C 39  ? 0.0747 0.1433 0.1040 -0.0084 0.0106  0.0191  56  ARG C NE  
2641 C CZ  . ARG C 39  ? 0.0854 0.1550 0.1021 0.0105  0.0253  0.0217  56  ARG C CZ  
2642 N NH1 . ARG C 39  ? 0.1207 0.1661 0.1076 0.0223  0.0057  0.0072  56  ARG C NH1 
2643 N NH2 . ARG C 39  ? 0.1209 0.2182 0.1071 0.0198  0.0426  0.0374  56  ARG C NH2 
2644 N N   . ILE C 40  ? 0.0517 0.1569 0.0943 -0.0093 0.0163  0.0197  57  ILE C N   
2645 C CA  . ILE C 40  ? 0.0639 0.0938 0.1030 0.0086  -0.0010 0.0054  57  ILE C CA  
2646 C C   . ILE C 40  ? 0.0836 0.1094 0.1134 0.0031  -0.0055 -0.0058 57  ILE C C   
2647 O O   . ILE C 40  ? 0.0669 0.1332 0.1175 0.0003  0.0063  0.0335  57  ILE C O   
2648 C CB  . ILE C 40  ? 0.0924 0.1151 0.1029 0.0126  0.0040  -0.0199 57  ILE C CB  
2649 C CG1 . ILE C 40  ? 0.1165 0.1175 0.1011 0.0312  0.0205  -0.0123 57  ILE C CG1 
2650 C CG2 . ILE C 40  ? 0.0865 0.1523 0.1062 0.0091  0.0063  -0.0336 57  ILE C CG2 
2651 C CD1 . ILE C 40  ? 0.1560 0.1164 0.1020 0.0172  0.0265  0.0011  57  ILE C CD1 
2652 N N   . ALA C 41  ? 0.0636 0.0937 0.1181 -0.0082 0.0116  -0.0013 58  ALA C N   
2653 C CA  . ALA C 41  ? 0.0827 0.1484 0.1190 -0.0073 0.0118  0.0102  58  ALA C CA  
2654 C C   . ALA C 41  ? 0.0614 0.0868 0.1211 0.0005  -0.0053 0.0126  58  ALA C C   
2655 O O   . ALA C 41  ? 0.0621 0.1356 0.1409 0.0141  -0.0082 0.0247  58  ALA C O   
2656 C CB  . ALA C 41  ? 0.1072 0.1559 0.1248 0.0259  0.0122  0.0093  58  ALA C CB  
2657 N N   . ALA C 42  ? 0.0574 0.0780 0.1042 0.0313  -0.0021 0.0221  59  ALA C N   
2658 C CA  . ALA C 42  ? 0.0636 0.1245 0.1013 0.0438  0.0096  0.0208  59  ALA C CA  
2659 C C   . ALA C 42  ? 0.0550 0.0664 0.0977 -0.0131 0.0082  0.0073  59  ALA C C   
2660 O O   . ALA C 42  ? 0.0828 0.1073 0.0966 -0.0182 -0.0065 0.0042  59  ALA C O   
2661 C CB  . ALA C 42  ? 0.0749 0.1844 0.1002 0.0103  0.0058  0.0066  59  ALA C CB  
2662 N N   . MET C 43  ? 0.1228 0.0907 0.1053 0.0316  0.0085  -0.0069 60  MET C N   
2663 C CA  . MET C 43  ? 0.0751 0.1078 0.1098 0.0151  0.0100  0.0149  60  MET C CA  
2664 C C   . MET C 43  ? 0.0575 0.0986 0.1194 0.0241  -0.0033 0.0099  60  MET C C   
2665 O O   . MET C 43  ? 0.0974 0.1393 0.1200 0.0202  -0.0330 0.0061  60  MET C O   
2666 C CB  . MET C 43  ? 0.0828 0.1259 0.1094 0.0210  0.0099  0.0054  60  MET C CB  
2667 C CG  . MET C 43  ? 0.1192 0.1797 0.1058 0.0524  0.0275  0.0158  60  MET C CG  
2668 S SD  . MET C 43  ? 0.1193 0.2572 0.1120 0.0315  0.0190  0.0380  60  MET C SD  
2669 C CE  . MET C 43  ? 0.1496 0.2214 0.1083 -0.0131 0.0034  0.0234  60  MET C CE  
2670 N N   . LYS C 44  ? 0.0488 0.0827 0.1397 0.0093  -0.0047 -0.0198 61  LYS C N   
2671 C CA  . LYS C 44  ? 0.1050 0.1422 0.1596 0.0468  -0.0085 -0.0310 61  LYS C CA  
2672 C C   . LYS C 44  ? 0.1108 0.0804 0.1371 -0.0098 -0.0088 -0.0237 61  LYS C C   
2673 O O   . LYS C 44  ? 0.1219 0.1274 0.1291 0.0326  -0.0151 -0.0340 61  LYS C O   
2674 C CB  . LYS C 44  ? 0.0795 0.1995 0.2110 -0.0091 -0.0051 -0.0719 61  LYS C CB  
2675 C CG  . LYS C 44  ? 0.1493 0.4192 0.2393 0.0088  -0.0018 -0.0453 61  LYS C CG  
2676 C CD  . LYS C 44  ? 0.1887 0.4485 0.2529 -0.0048 -0.0077 -0.0371 61  LYS C CD  
2677 C CE  . LYS C 44  ? 0.2494 0.4243 0.2619 -0.0284 -0.0303 -0.0744 61  LYS C CE  
2678 N NZ  . LYS C 44  ? 0.3548 0.3834 0.2636 0.0267  -0.0511 -0.1137 61  LYS C NZ  
2679 N N   . LEU C 45  ? 0.0583 0.1260 0.1249 -0.0082 0.0012  -0.0011 62  LEU C N   
2680 C CA  . LEU C 45  ? 0.0593 0.1094 0.1157 -0.0098 0.0229  0.0070  62  LEU C CA  
2681 C C   . LEU C 45  ? 0.0807 0.1311 0.1226 0.0078  0.0095  0.0110  62  LEU C C   
2682 O O   . LEU C 45  ? 0.1257 0.1317 0.1215 -0.0273 -0.0308 0.0116  62  LEU C O   
2683 C CB  . LEU C 45  ? 0.1151 0.1208 0.1127 0.0197  0.0264  0.0082  62  LEU C CB  
2684 C CG  . LEU C 45  ? 0.1844 0.1375 0.1187 0.0262  0.0191  -0.0020 62  LEU C CG  
2685 C CD1 . LEU C 45  ? 0.1522 0.2164 0.1227 0.0549  0.0054  -0.0041 62  LEU C CD1 
2686 C CD2 . LEU C 45  ? 0.2062 0.1341 0.1251 0.0586  0.0291  0.0052  62  LEU C CD2 
2687 N N   . THR C 46  ? 0.0708 0.1318 0.1224 -0.0480 0.0033  -0.0087 63  THR C N   
2688 C CA  . THR C 46  ? 0.0767 0.1669 0.1369 -0.0245 -0.0118 -0.0045 63  THR C CA  
2689 C C   . THR C 46  ? 0.1084 0.1373 0.1460 -0.0083 -0.0163 0.0088  63  THR C C   
2690 O O   . THR C 46  ? 0.1273 0.1124 0.1644 0.0019  -0.0452 -0.0063 63  THR C O   
2691 C CB  . THR C 46  ? 0.1541 0.1469 0.1514 -0.0407 -0.0134 -0.0064 63  THR C CB  
2692 O OG1 . THR C 46  ? 0.1676 0.1346 0.1589 -0.0623 0.0076  0.0007  63  THR C OG1 
2693 C CG2 . THR C 46  ? 0.1852 0.1511 0.1566 -0.0008 -0.0061 0.0122  63  THR C CG2 
2694 N N   . ILE C 47  ? 0.0955 0.1353 0.1428 -0.0424 -0.0237 0.0128  64  ILE C N   
2695 C CA  . ILE C 47  ? 0.1578 0.1143 0.1477 -0.0269 -0.0179 -0.0088 64  ILE C CA  
2696 C C   . ILE C 47  ? 0.1535 0.1008 0.1513 -0.0410 -0.0194 0.0036  64  ILE C C   
2697 O O   . ILE C 47  ? 0.1415 0.1278 0.1528 -0.0691 -0.0232 0.0235  64  ILE C O   
2698 C CB  . ILE C 47  ? 0.2165 0.0710 0.1433 -0.0047 -0.0116 -0.0093 64  ILE C CB  
2699 C CG1 . ILE C 47  ? 0.2609 0.1162 0.1494 0.0293  -0.0199 -0.0173 64  ILE C CG1 
2700 C CG2 . ILE C 47  ? 0.1578 0.1368 0.1458 -0.0261 -0.0038 -0.0046 64  ILE C CG2 
2701 C CD1 . ILE C 47  ? 0.2834 0.1848 0.1582 0.0067  -0.0206 -0.0131 64  ILE C CD1 
2702 N N   . ALA C 48  ? 0.0998 0.1192 0.1480 -0.0480 0.0049  0.0307  65  ALA C N   
2703 C CA  . ALA C 48  ? 0.1358 0.1175 0.1486 0.0050  0.0314  0.0505  65  ALA C CA  
2704 C C   . ALA C 48  ? 0.1487 0.1378 0.1596 -0.0014 0.0310  0.0532  65  ALA C C   
2705 O O   . ALA C 48  ? 0.1943 0.1415 0.1661 0.0436  0.0301  0.0470  65  ALA C O   
2706 C CB  . ALA C 48  ? 0.1196 0.1808 0.1435 0.0056  0.0211  0.0539  65  ALA C CB  
2707 N N   . THR C 49  ? 0.1456 0.1385 0.1686 -0.0519 0.0377  0.0228  66  THR C N   
2708 C CA  . THR C 49  ? 0.1802 0.1665 0.1733 -0.0437 0.0383  0.0163  66  THR C CA  
2709 C C   . THR C 49  ? 0.1960 0.1338 0.1712 -0.0816 0.0133  -0.0089 66  THR C C   
2710 O O   . THR C 49  ? 0.1982 0.1262 0.1614 -0.0630 0.0070  -0.0052 66  THR C O   
2711 C CB  . THR C 49  ? 0.1875 0.2063 0.1816 -0.0431 0.0503  -0.0115 66  THR C CB  
2712 O OG1 . THR C 49  ? 0.1583 0.1700 0.1863 -0.0644 0.0504  -0.0134 66  THR C OG1 
2713 C CG2 . THR C 49  ? 0.2441 0.2709 0.1841 -0.0527 0.0595  0.0185  66  THR C CG2 
2714 N N   . PRO C 50  ? 0.2608 0.1521 0.1737 -0.0852 0.0207  0.0016  67  PRO C N   
2715 C CA  . PRO C 50  ? 0.3335 0.1567 0.1787 -0.0091 0.0325  -0.0037 67  PRO C CA  
2716 C C   . PRO C 50  ? 0.3339 0.1396 0.1840 -0.0470 0.0475  -0.0034 67  PRO C C   
2717 O O   . PRO C 50  ? 0.4055 0.1753 0.1782 -0.0667 0.0671  0.0170  67  PRO C O   
2718 C CB  . PRO C 50  ? 0.3869 0.1267 0.1822 0.0480  0.0155  -0.0042 67  PRO C CB  
2719 C CG  . PRO C 50  ? 0.3931 0.1854 0.1863 0.0376  0.0219  0.0023  67  PRO C CG  
2720 C CD  . PRO C 50  ? 0.3491 0.1720 0.1837 -0.0173 0.0274  0.0069  67  PRO C CD  
2721 N N   . ALA C 51  ? 0.2425 0.1681 0.1873 -0.0917 0.0610  -0.0084 68  ALA C N   
2722 C CA  . ALA C 51  ? 0.2982 0.1843 0.1951 -0.0426 0.0749  0.0026  68  ALA C CA  
2723 C C   . ALA C 51  ? 0.3474 0.1537 0.1943 -0.0675 0.0702  -0.0021 68  ALA C C   
2724 O O   . ALA C 51  ? 0.4392 0.1657 0.2022 -0.0631 0.0936  0.0053  68  ALA C O   
2725 C CB  . ALA C 51  ? 0.3042 0.2581 0.2036 -0.0446 0.0663  -0.0121 68  ALA C CB  
2726 N N   . ILE C 52  ? 0.2548 0.1522 0.1901 -0.0933 0.0553  -0.0093 69  ILE C N   
2727 C CA  . ILE C 52  ? 0.1729 0.1376 0.1829 -0.0487 0.0362  -0.0017 69  ILE C CA  
2728 C C   . ILE C 52  ? 0.1730 0.0835 0.1722 0.0099  0.0230  0.0090  69  ILE C C   
2729 O O   . ILE C 52  ? 0.1555 0.1245 0.1674 0.0046  0.0199  0.0174  69  ILE C O   
2730 C CB  . ILE C 52  ? 0.1952 0.1398 0.1931 -0.0409 0.0281  0.0076  69  ILE C CB  
2731 C CG1 . ILE C 52  ? 0.2575 0.2574 0.1948 0.0701  0.0178  0.0364  69  ILE C CG1 
2732 C CG2 . ILE C 52  ? 0.2363 0.2304 0.1993 0.0050  0.0255  -0.0156 69  ILE C CG2 
2733 C CD1 . ILE C 52  ? 0.3240 0.3261 0.1999 0.0977  0.0184  0.0750  69  ILE C CD1 
2734 N N   . LEU C 53  ? 0.1051 0.1162 0.1676 -0.0110 0.0297  0.0006  70  LEU C N   
2735 C CA  . LEU C 53  ? 0.1212 0.0993 0.1678 -0.0321 0.0368  0.0009  70  LEU C CA  
2736 C C   . LEU C 53  ? 0.1647 0.0928 0.1712 0.0365  0.0359  -0.0191 70  LEU C C   
2737 O O   . LEU C 53  ? 0.1842 0.0744 0.1742 -0.0080 0.0335  -0.0139 70  LEU C O   
2738 C CB  . LEU C 53  ? 0.1911 0.0961 0.1624 0.0092  0.0309  -0.0132 70  LEU C CB  
2739 C CG  . LEU C 53  ? 0.0778 0.1485 0.1604 -0.0515 0.0219  -0.0090 70  LEU C CG  
2740 C CD1 . LEU C 53  ? 0.1380 0.1627 0.1627 0.0078  0.0298  0.0042  70  LEU C CD1 
2741 C CD2 . LEU C 53  ? 0.1214 0.1762 0.1578 -0.0251 0.0012  0.0002  70  LEU C CD2 
2742 N N   . GLU C 54  ? 0.2158 0.1066 0.1757 -0.0090 0.0581  -0.0023 71  GLU C N   
2743 C CA  . GLU C 54  ? 0.2778 0.0950 0.1895 -0.0233 0.0601  0.0285  71  GLU C CA  
2744 C C   . GLU C 54  ? 0.2230 0.1250 0.1814 -0.0012 0.0516  0.0304  71  GLU C C   
2745 O O   . GLU C 54  ? 0.2484 0.1801 0.1758 0.0377  0.0304  0.0182  71  GLU C O   
2746 C CB  . GLU C 54  ? 0.4003 0.1187 0.2163 -0.0253 0.0721  0.0215  71  GLU C CB  
2747 C CG  . GLU C 54  ? 0.6032 0.2724 0.2441 -0.0377 0.0971  0.0191  71  GLU C CG  
2748 C CD  . GLU C 54  ? 0.7603 0.3705 0.2698 -0.0198 0.1169  -0.0147 71  GLU C CD  
2749 O OE1 . GLU C 54  ? 0.7599 0.2978 0.2794 -0.1345 0.1250  -0.0110 71  GLU C OE1 
2750 O OE2 . GLU C 54  ? 0.8519 0.5017 0.2785 0.0323  0.1167  -0.0458 71  GLU C OE2 
2751 N N   . GLU C 55  ? 0.1973 0.1359 0.1818 -0.0440 0.0480  0.0403  72  GLU C N   
2752 C CA  A GLU C 55  ? 0.1819 0.1762 0.1838 -0.0570 0.0525  0.0235  72  GLU C CA  
2753 C CA  B GLU C 55  ? 0.1882 0.1659 0.1859 -0.0352 0.0447  0.0199  72  GLU C CA  
2754 C C   . GLU C 55  ? 0.1443 0.1857 0.1782 -0.0423 0.0455  0.0216  72  GLU C C   
2755 O O   . GLU C 55  ? 0.1369 0.2165 0.1714 -0.0076 0.0595  0.0127  72  GLU C O   
2756 C CB  A GLU C 55  ? 0.2139 0.1823 0.1921 -0.0613 0.0641  0.0347  72  GLU C CB  
2757 C CB  B GLU C 55  ? 0.2327 0.1568 0.1980 0.0029  0.0385  0.0149  72  GLU C CB  
2758 C CG  A GLU C 55  ? 0.2624 0.2557 0.2013 -0.0225 0.0677  0.0241  72  GLU C CG  
2759 C CG  B GLU C 55  ? 0.2678 0.1812 0.2101 0.0199  0.0365  0.0028  72  GLU C CG  
2760 C CD  A GLU C 55  ? 0.2708 0.2694 0.2080 -0.0209 0.0735  0.0180  72  GLU C CD  
2761 C CD  B GLU C 55  ? 0.2578 0.2506 0.2226 -0.0373 0.0449  -0.0185 72  GLU C CD  
2762 O OE1 A GLU C 55  ? 0.3303 0.3005 0.2099 -0.0616 0.0795  0.0194  72  GLU C OE1 
2763 O OE1 B GLU C 55  ? 0.3315 0.2885 0.2280 -0.0040 0.0473  -0.0149 72  GLU C OE1 
2764 O OE2 A GLU C 55  ? 0.2152 0.2908 0.2127 0.0693  0.0520  0.0032  72  GLU C OE2 
2765 O OE2 B GLU C 55  ? 0.2114 0.2502 0.2283 -0.0715 0.0452  -0.0325 72  GLU C OE2 
2766 N N   . HIS C 56  ? 0.1101 0.1277 0.1691 -0.0218 0.0076  0.0304  73  HIS C N   
2767 C CA  . HIS C 56  ? 0.1531 0.0815 0.1618 0.0077  0.0043  0.0310  73  HIS C CA  
2768 C C   . HIS C 56  ? 0.1486 0.0667 0.1540 0.0000  -0.0120 0.0209  73  HIS C C   
2769 O O   . HIS C 56  ? 0.1668 0.0875 0.1553 0.0207  -0.0260 0.0081  73  HIS C O   
2770 C CB  . HIS C 56  ? 0.1076 0.0943 0.1610 -0.0152 0.0166  0.0357  73  HIS C CB  
2771 C CG  . HIS C 56  ? 0.1464 0.0961 0.1558 -0.0219 -0.0050 0.0429  73  HIS C CG  
2772 N ND1 . HIS C 56  ? 0.1697 0.0861 0.1481 -0.0526 0.0016  0.0328  73  HIS C ND1 
2773 C CD2 . HIS C 56  ? 0.1745 0.1705 0.1577 -0.0231 -0.0143 0.0655  73  HIS C CD2 
2774 C CE1 . HIS C 56  ? 0.2044 0.1047 0.1510 -0.0588 -0.0079 0.0445  73  HIS C CE1 
2775 N NE2 . HIS C 56  ? 0.2000 0.1387 0.1592 -0.0341 -0.0166 0.0410  73  HIS C NE2 
2776 N N   . TYR C 57  ? 0.1187 0.1058 0.1540 0.0081  -0.0036 0.0267  74  TYR C N   
2777 C CA  . TYR C 57  ? 0.1668 0.1136 0.1597 0.0367  0.0067  0.0139  74  TYR C CA  
2778 C C   . TYR C 57  ? 0.2132 0.1807 0.1551 0.0864  0.0269  0.0045  74  TYR C C   
2779 O O   . TYR C 57  ? 0.2656 0.2053 0.1430 0.0749  0.0409  -0.0050 74  TYR C O   
2780 C CB  . TYR C 57  ? 0.1472 0.0552 0.1663 0.0202  -0.0212 0.0188  74  TYR C CB  
2781 C CG  . TYR C 57  ? 0.1401 0.1624 0.1798 -0.0188 -0.0258 0.0167  74  TYR C CG  
2782 C CD1 . TYR C 57  ? 0.2023 0.1718 0.1795 0.0203  -0.0354 -0.0028 74  TYR C CD1 
2783 C CD2 . TYR C 57  ? 0.1854 0.1904 0.1836 -0.0818 -0.0195 0.0171  74  TYR C CD2 
2784 C CE1 . TYR C 57  ? 0.2312 0.1571 0.1832 0.0363  0.0007  0.0136  74  TYR C CE1 
2785 C CE2 . TYR C 57  ? 0.2319 0.1844 0.1853 -0.0628 0.0101  0.0137  74  TYR C CE2 
2786 C CZ  . TYR C 57  ? 0.2497 0.2084 0.1906 -0.0478 0.0061  0.0136  74  TYR C CZ  
2787 O OH  . TYR C 57  ? 0.1790 0.2393 0.2004 -0.0788 0.0054  -0.0034 74  TYR C OH  
2788 N N   . ALA C 58  ? 0.1801 0.1794 0.1590 0.0122  0.0399  0.0214  75  ALA C N   
2789 C CA  . ALA C 58  ? 0.2084 0.2012 0.1639 0.0099  0.0477  0.0405  75  ALA C CA  
2790 C C   . ALA C 58  ? 0.2322 0.1908 0.1706 -0.0411 0.0350  0.0439  75  ALA C C   
2791 O O   . ALA C 58  ? 0.2964 0.1889 0.1745 0.0185  0.0397  0.0425  75  ALA C O   
2792 C CB  . ALA C 58  ? 0.2053 0.2811 0.1633 0.0710  0.0589  0.0594  75  ALA C CB  
2793 N N   . GLU C 59  ? 0.2985 0.1517 0.1722 0.0445  0.0169  0.0195  76  GLU C N   
2794 C CA  . GLU C 59  ? 0.3507 0.2063 0.1860 0.0496  -0.0031 0.0209  76  GLU C CA  
2795 C C   . GLU C 59  ? 0.3326 0.2540 0.1904 0.0762  -0.0091 0.0527  76  GLU C C   
2796 O O   . GLU C 59  ? 0.3228 0.3001 0.1800 0.0826  -0.0042 0.0519  76  GLU C O   
2797 C CB  . GLU C 59  ? 0.4295 0.1804 0.1967 0.0435  -0.0389 -0.0018 76  GLU C CB  
2798 C CG  . GLU C 59  ? 0.4829 0.2466 0.2107 0.0846  -0.0550 -0.0056 76  GLU C CG  
2799 C CD  . GLU C 59  ? 0.5716 0.2499 0.2205 0.0635  -0.0666 0.0046  76  GLU C CD  
2800 O OE1 . GLU C 59  ? 0.5914 0.2316 0.2278 0.0595  -0.0843 -0.0115 76  GLU C OE1 
2801 O OE2 . GLU C 59  ? 0.5920 0.1666 0.2233 -0.0320 -0.0552 0.0317  76  GLU C OE2 
2802 N N   . HIS C 60  ? 0.2944 0.2593 0.2025 0.1207  -0.0008 0.0862  77  HIS C N   
2803 C CA  . HIS C 60  ? 0.2635 0.2534 0.2231 0.0513  0.0069  0.0839  77  HIS C CA  
2804 C C   . HIS C 60  ? 0.2501 0.2829 0.2437 0.0236  0.0246  0.1076  77  HIS C C   
2805 O O   . HIS C 60  ? 0.2190 0.2042 0.2446 -0.0304 0.0113  0.0901  77  HIS C O   
2806 C CB  . HIS C 60  ? 0.2838 0.2122 0.2287 0.0248  -0.0067 0.0749  77  HIS C CB  
2807 C CG  . HIS C 60  ? 0.2962 0.2125 0.2376 -0.0431 -0.0362 0.0823  77  HIS C CG  
2808 N ND1 . HIS C 60  ? 0.3506 0.2410 0.2451 -0.0067 -0.0463 0.0717  77  HIS C ND1 
2809 C CD2 . HIS C 60  ? 0.3375 0.2368 0.2441 0.0149  -0.0578 0.0814  77  HIS C CD2 
2810 C CE1 . HIS C 60  ? 0.3657 0.2590 0.2454 -0.0108 -0.0575 0.0805  77  HIS C CE1 
2811 N NE2 . HIS C 60  ? 0.3741 0.2254 0.2460 -0.0042 -0.0598 0.0832  77  HIS C NE2 
2812 N N   . LYS C 61  ? 0.2804 0.2526 0.2689 -0.0159 0.0542  0.1283  78  LYS C N   
2813 C CA  . LYS C 61  ? 0.3079 0.2524 0.2960 0.0365  0.0824  0.1377  78  LYS C CA  
2814 C C   . LYS C 61  ? 0.2930 0.3195 0.3059 0.0633  0.0927  0.1579  78  LYS C C   
2815 O O   . LYS C 61  ? 0.2757 0.3537 0.3066 0.0295  0.1040  0.1650  78  LYS C O   
2816 C CB  . LYS C 61  ? 0.3386 0.3454 0.3148 0.1032  0.0982  0.1254  78  LYS C CB  
2817 C CG  . LYS C 61  ? 0.3788 0.4780 0.3312 0.0903  0.0984  0.1126  78  LYS C CG  
2818 C CD  . LYS C 61  ? 0.4538 0.5913 0.3414 0.1481  0.1064  0.1006  78  LYS C CD  
2819 C CE  . LYS C 61  ? 0.4909 0.6891 0.3488 0.1990  0.1071  0.0888  78  LYS C CE  
2820 N NZ  . LYS C 61  ? 0.5109 0.7296 0.3543 0.2288  0.0964  0.0735  78  LYS C NZ  
2821 N N   . GLY C 62  ? 0.3572 0.3665 0.3165 0.0919  0.0739  0.1644  79  GLY C N   
2822 C CA  . GLY C 62  ? 0.3569 0.3891 0.3174 0.1066  0.0660  0.1791  79  GLY C CA  
2823 C C   . GLY C 62  ? 0.3445 0.3399 0.3173 0.0701  0.0445  0.1820  79  GLY C C   
2824 O O   . GLY C 62  ? 0.3708 0.3231 0.3247 0.0698  0.0341  0.1844  79  GLY C O   
2825 N N   . LYS C 63  ? 0.3096 0.3139 0.3117 0.0493  0.0275  0.1665  80  LYS C N   
2826 C CA  . LYS C 63  ? 0.2866 0.2748 0.3048 0.0316  0.0001  0.1477  80  LYS C CA  
2827 C C   . LYS C 63  ? 0.2597 0.3002 0.2931 0.0115  -0.0045 0.1585  80  LYS C C   
2828 O O   . LYS C 63  ? 0.2069 0.2528 0.2919 -0.0418 -0.0148 0.1478  80  LYS C O   
2829 C CB  . LYS C 63  ? 0.3224 0.3094 0.3086 0.0505  -0.0047 0.1260  80  LYS C CB  
2830 C CG  . LYS C 63  ? 0.3629 0.3399 0.3176 0.0314  -0.0050 0.0886  80  LYS C CG  
2831 C CD  . LYS C 63  ? 0.3742 0.3869 0.3237 0.0575  -0.0109 0.0548  80  LYS C CD  
2832 C CE  . LYS C 63  ? 0.4830 0.4101 0.3287 0.1262  -0.0174 0.0276  80  LYS C CE  
2833 N NZ  . LYS C 63  ? 0.4946 0.3791 0.3318 0.1152  -0.0249 0.0075  80  LYS C NZ  
2834 N N   . PRO C 64  ? 0.2298 0.2987 0.2839 -0.0220 -0.0018 0.1718  81  PRO C N   
2835 C CA  . PRO C 64  ? 0.2548 0.3064 0.2734 0.0136  -0.0021 0.1712  81  PRO C CA  
2836 C C   . PRO C 64  ? 0.2711 0.2931 0.2633 0.0049  0.0016  0.1597  81  PRO C C   
2837 O O   . PRO C 64  ? 0.2433 0.2421 0.2633 0.0097  0.0057  0.1498  81  PRO C O   
2838 C CB  . PRO C 64  ? 0.2324 0.3861 0.2776 0.0409  0.0029  0.1714  81  PRO C CB  
2839 C CG  . PRO C 64  ? 0.2750 0.4039 0.2832 0.0601  -0.0079 0.1422  81  PRO C CG  
2840 C CD  . PRO C 64  ? 0.2241 0.2966 0.2823 0.0159  -0.0163 0.1511  81  PRO C CD  
2841 N N   . PHE C 65  ? 0.2534 0.2324 0.2531 -0.0463 -0.0078 0.1376  82  PHE C N   
2842 C CA  . PHE C 65  ? 0.2475 0.2780 0.2541 -0.0138 -0.0289 0.1309  82  PHE C CA  
2843 C C   . PHE C 65  ? 0.2706 0.2954 0.2460 -0.0111 -0.0261 0.1234  82  PHE C C   
2844 O O   . PHE C 65  ? 0.2620 0.3277 0.2390 -0.0296 -0.0151 0.1468  82  PHE C O   
2845 C CB  . PHE C 65  ? 0.2235 0.2849 0.2647 -0.0562 -0.0313 0.1057  82  PHE C CB  
2846 C CG  . PHE C 65  ? 0.2590 0.3100 0.2750 -0.0566 -0.0114 0.0960  82  PHE C CG  
2847 C CD1 . PHE C 65  ? 0.2584 0.3141 0.2788 -0.0496 -0.0022 0.1034  82  PHE C CD1 
2848 C CD2 . PHE C 65  ? 0.3023 0.3281 0.2817 -0.0201 -0.0092 0.0822  82  PHE C CD2 
2849 C CE1 . PHE C 65  ? 0.2923 0.2512 0.2821 -0.0646 0.0028  0.0943  82  PHE C CE1 
2850 C CE2 . PHE C 65  ? 0.3511 0.3236 0.2841 0.0379  -0.0089 0.0755  82  PHE C CE2 
2851 C CZ  . PHE C 65  ? 0.3435 0.2100 0.2844 -0.0067 -0.0140 0.0860  82  PHE C CZ  
2852 N N   . LEU C 66  ? 0.2037 0.1939 0.2362 -0.0101 -0.0303 0.1213  83  LEU C N   
2853 C CA  . LEU C 66  ? 0.1423 0.1725 0.2228 -0.0586 -0.0239 0.0937  83  LEU C CA  
2854 C C   . LEU C 66  ? 0.2323 0.2672 0.2166 0.0024  0.0019  0.1208  83  LEU C C   
2855 O O   . LEU C 66  ? 0.2422 0.2495 0.2124 0.0387  -0.0049 0.1303  83  LEU C O   
2856 C CB  . LEU C 66  ? 0.1330 0.2046 0.2256 0.0110  -0.0170 0.0743  83  LEU C CB  
2857 C CG  . LEU C 66  ? 0.1919 0.1684 0.2222 -0.0062 -0.0256 0.0252  83  LEU C CG  
2858 C CD1 . LEU C 66  ? 0.2613 0.1338 0.2168 0.0113  -0.0554 0.0020  83  LEU C CD1 
2859 C CD2 . LEU C 66  ? 0.2454 0.3460 0.2247 0.0087  -0.0204 0.0200  83  LEU C CD2 
2860 N N   . PRO C 67  ? 0.2528 0.2475 0.2153 0.0030  0.0063  0.1092  84  PRO C N   
2861 C CA  . PRO C 67  ? 0.2492 0.1766 0.2192 0.0432  0.0023  0.0830  84  PRO C CA  
2862 C C   . PRO C 67  ? 0.2541 0.2519 0.2168 0.0475  0.0203  0.1097  84  PRO C C   
2863 O O   . PRO C 67  ? 0.2619 0.2781 0.2203 0.0920  0.0274  0.1191  84  PRO C O   
2864 C CB  . PRO C 67  ? 0.2941 0.1438 0.2192 0.0160  -0.0016 0.0784  84  PRO C CB  
2865 C CG  . PRO C 67  ? 0.3400 0.2170 0.2170 0.0432  -0.0009 0.0985  84  PRO C CG  
2866 C CD  . PRO C 67  ? 0.2822 0.1454 0.2203 0.0032  -0.0094 0.1009  84  PRO C CD  
2867 N N   . GLY C 68  ? 0.3028 0.3010 0.2141 0.0446  0.0236  0.1146  85  GLY C N   
2868 C CA  . GLY C 68  ? 0.2922 0.3529 0.2150 0.0703  0.0260  0.1018  85  GLY C CA  
2869 C C   . GLY C 68  ? 0.2477 0.3057 0.2127 0.0756  0.0201  0.1066  85  GLY C C   
2870 O O   . GLY C 68  ? 0.2328 0.3699 0.2107 0.0680  0.0104  0.1121  85  GLY C O   
2871 N N   . LEU C 69  ? 0.2282 0.2553 0.2157 0.0926  0.0232  0.0979  86  LEU C N   
2872 C CA  . LEU C 69  ? 0.2165 0.2219 0.2220 0.0400  0.0364  0.0753  86  LEU C CA  
2873 C C   . LEU C 69  ? 0.2204 0.2305 0.2194 0.0926  0.0449  0.0798  86  LEU C C   
2874 O O   . LEU C 69  ? 0.2363 0.2388 0.2168 0.0262  0.0635  0.0888  86  LEU C O   
2875 C CB  . LEU C 69  ? 0.2903 0.1949 0.2326 0.0076  0.0465  0.0609  86  LEU C CB  
2876 C CG  . LEU C 69  ? 0.3538 0.2953 0.2447 0.0520  0.0297  0.0516  86  LEU C CG  
2877 C CD1 . LEU C 69  ? 0.3887 0.2957 0.2524 0.0618  0.0204  0.0414  86  LEU C CD1 
2878 C CD2 . LEU C 69  ? 0.4664 0.3918 0.2512 0.0637  0.0283  0.0457  86  LEU C CD2 
2879 N N   . ILE C 70  ? 0.1739 0.2142 0.2182 0.0330  0.0440  0.0755  87  ILE C N   
2880 C CA  A ILE C 70  ? 0.1893 0.2039 0.2172 0.0593  0.0449  0.0822  87  ILE C CA  
2881 C CA  B ILE C 70  ? 0.1881 0.2051 0.2175 0.0439  0.0365  0.0756  87  ILE C CA  
2882 C C   . ILE C 70  ? 0.2186 0.1884 0.2182 0.0250  0.0305  0.0815  87  ILE C C   
2883 O O   . ILE C 70  ? 0.2165 0.1919 0.2111 0.0126  0.0168  0.0877  87  ILE C O   
2884 C CB  A ILE C 70  ? 0.2327 0.2372 0.2174 0.0477  0.0543  0.0798  87  ILE C CB  
2885 C CB  B ILE C 70  ? 0.2030 0.2266 0.2174 0.0256  0.0315  0.0653  87  ILE C CB  
2886 C CG1 A ILE C 70  ? 0.2903 0.3088 0.2173 0.0357  0.0688  0.0888  87  ILE C CG1 
2887 C CG1 B ILE C 70  ? 0.2481 0.2757 0.2173 0.0090  0.0357  0.0646  87  ILE C CG1 
2888 C CG2 A ILE C 70  ? 0.2300 0.2520 0.2164 0.0687  0.0660  0.0845  87  ILE C CG2 
2889 C CG2 B ILE C 70  ? 0.1864 0.2307 0.2168 0.0332  0.0348  0.0657  87  ILE C CG2 
2890 C CD1 A ILE C 70  ? 0.2979 0.3554 0.2176 0.0521  0.0815  0.0835  87  ILE C CD1 
2891 C CD1 B ILE C 70  ? 0.2396 0.2722 0.2158 0.0077  0.0369  0.0585  87  ILE C CD1 
2892 N N   . GLU C 71  ? 0.2495 0.1938 0.2283 0.0908  0.0243  0.0735  88  GLU C N   
2893 C CA  . GLU C 71  ? 0.1981 0.2760 0.2367 0.1057  0.0323  0.0801  88  GLU C CA  
2894 C C   . GLU C 71  ? 0.2048 0.2383 0.2133 0.0803  0.0651  0.0622  88  GLU C C   
2895 O O   . GLU C 71  ? 0.2938 0.2139 0.2088 0.0775  0.0831  0.0378  88  GLU C O   
2896 C CB  . GLU C 71  ? 0.3409 0.3940 0.2693 0.1654  0.0232  0.0940  88  GLU C CB  
2897 C CG  . GLU C 71  ? 0.5097 0.5640 0.3016 0.2658  0.0083  0.0834  88  GLU C CG  
2898 C CD  . GLU C 71  ? 0.6662 0.6644 0.3317 0.2864  -0.0038 0.0745  88  GLU C CD  
2899 O OE1 . GLU C 71  ? 0.7099 0.7258 0.3411 0.3063  -0.0191 0.0546  88  GLU C OE1 
2900 O OE2 . GLU C 71  ? 0.7106 0.6340 0.3431 0.2155  0.0065  0.0823  88  GLU C OE2 
2901 N N   . LYS C 72  ? 0.2141 0.2576 0.1973 0.0640  0.0541  0.0436  89  LYS C N   
2902 C CA  . LYS C 72  ? 0.1888 0.2619 0.1894 0.0242  0.0335  0.0130  89  LYS C CA  
2903 C C   . LYS C 72  ? 0.1646 0.1868 0.1665 0.0479  0.0320  0.0328  89  LYS C C   
2904 O O   . LYS C 72  ? 0.1665 0.2852 0.1548 0.0211  0.0575  0.0588  89  LYS C O   
2905 C CB  . LYS C 72  ? 0.1730 0.2983 0.2000 -0.0038 0.0156  -0.0084 89  LYS C CB  
2906 C CG  . LYS C 72  ? 0.2390 0.3996 0.2160 0.0933  0.0287  -0.0038 89  LYS C CG  
2907 C CD  . LYS C 72  ? 0.3458 0.4722 0.2271 0.1578  0.0190  0.0057  89  LYS C CD  
2908 C CE  . LYS C 72  ? 0.4336 0.5101 0.2333 0.2107  0.0285  0.0228  89  LYS C CE  
2909 N NZ  . LYS C 72  ? 0.4654 0.5318 0.2357 0.2294  0.0270  0.0182  89  LYS C NZ  
2910 N N   . MET C 73  ? 0.1667 0.1582 0.1550 0.0312  0.0216  0.0221  90  MET C N   
2911 C CA  . MET C 73  ? 0.2052 0.1023 0.1469 0.0528  0.0313  0.0297  90  MET C CA  
2912 C C   . MET C 73  ? 0.2192 0.1409 0.1398 0.0649  0.0315  0.0228  90  MET C C   
2913 O O   . MET C 73  ? 0.1748 0.1203 0.1281 0.0046  0.0278  0.0165  90  MET C O   
2914 C CB  . MET C 73  ? 0.1974 0.1325 0.1519 -0.0010 0.0264  0.0327  90  MET C CB  
2915 C CG  . MET C 73  ? 0.1255 0.0946 0.1653 0.0107  0.0113  0.0208  90  MET C CG  
2916 S SD  . MET C 73  ? 0.1589 0.1784 0.1725 -0.0405 0.0209  0.0229  90  MET C SD  
2917 C CE  . MET C 73  ? 0.1450 0.2187 0.1782 -0.0456 0.0018  0.0275  90  MET C CE  
2918 N N   . THR C 74  ? 0.2338 0.1682 0.1428 0.0900  0.0391  0.0380  91  THR C N   
2919 C CA  . THR C 74  ? 0.2353 0.1349 0.1544 0.0271  0.0356  0.0172  91  THR C CA  
2920 C C   . THR C 74  ? 0.2211 0.1224 0.1515 0.0433  0.0453  0.0197  91  THR C C   
2921 O O   . THR C 74  ? 0.2909 0.2160 0.1636 0.1271  0.0752  0.0386  91  THR C O   
2922 C CB  . THR C 74  ? 0.3057 0.1228 0.1658 0.0611  0.0370  0.0164  91  THR C CB  
2923 O OG1 . THR C 74  ? 0.3231 0.1689 0.1643 0.0481  0.0256  0.0153  91  THR C OG1 
2924 C CG2 . THR C 74  ? 0.3065 0.1338 0.1747 0.0132  0.0346  0.0010  91  THR C CG2 
2925 N N   . GLY C 75  ? 0.1418 0.1041 0.1364 0.0112  0.0370  0.0101  92  GLY C N   
2926 C CA  . GLY C 75  ? 0.1654 0.1119 0.1355 0.0049  0.0240  -0.0076 92  GLY C CA  
2927 C C   . GLY C 75  ? 0.1055 0.0899 0.1349 0.0143  0.0186  -0.0030 92  GLY C C   
2928 O O   . GLY C 75  ? 0.0964 0.1111 0.1370 0.0354  0.0128  -0.0091 92  GLY C O   
2929 N N   . PRO C 76  ? 0.0931 0.0806 0.1315 -0.0122 0.0167  -0.0179 93  PRO C N   
2930 C CA  . PRO C 76  ? 0.1272 0.0430 0.1252 -0.0155 0.0267  -0.0001 93  PRO C CA  
2931 C C   . PRO C 76  ? 0.1152 0.0546 0.1242 -0.0165 0.0184  0.0054  93  PRO C C   
2932 O O   . PRO C 76  ? 0.0678 0.1200 0.1197 -0.0083 -0.0007 0.0125  93  PRO C O   
2933 C CB  . PRO C 76  ? 0.0952 0.1024 0.1265 -0.0206 0.0106  -0.0116 93  PRO C CB  
2934 C CG  . PRO C 76  ? 0.1110 0.1864 0.1317 -0.0448 0.0144  -0.0305 93  PRO C CG  
2935 C CD  . PRO C 76  ? 0.1195 0.1044 0.1373 -0.0164 0.0261  -0.0321 93  PRO C CD  
2936 N N   . VAL C 77  ? 0.0946 0.0791 0.1206 0.0003  -0.0053 -0.0153 94  VAL C N   
2937 C CA  . VAL C 77  ? 0.0972 0.0659 0.1155 -0.0158 0.0065  0.0039  94  VAL C CA  
2938 C C   . VAL C 77  ? 0.0846 0.0573 0.1100 0.0064  -0.0046 -0.0098 94  VAL C C   
2939 O O   . VAL C 77  ? 0.1196 0.0845 0.1108 0.0042  0.0029  -0.0007 94  VAL C O   
2940 C CB  . VAL C 77  ? 0.1047 0.1150 0.1113 -0.0070 0.0019  0.0075  94  VAL C CB  
2941 C CG1 . VAL C 77  ? 0.1310 0.1309 0.1034 -0.0097 0.0156  0.0131  94  VAL C CG1 
2942 C CG2 . VAL C 77  ? 0.1372 0.1589 0.1132 0.0193  0.0186  0.0516  94  VAL C CG2 
2943 N N   . LEU C 78  ? 0.0527 0.0829 0.1048 0.0055  0.0249  0.0044  95  LEU C N   
2944 C CA  . LEU C 78  ? 0.0745 0.0638 0.0960 0.0249  0.0274  0.0061  95  LEU C CA  
2945 C C   . LEU C 78  ? 0.0797 0.1015 0.0886 0.0055  0.0190  0.0078  95  LEU C C   
2946 O O   . LEU C 78  ? 0.1000 0.1189 0.0958 -0.0226 0.0051  -0.0302 95  LEU C O   
2947 C CB  . LEU C 78  ? 0.1187 0.0693 0.1032 0.0079  0.0329  0.0313  95  LEU C CB  
2948 C CG  . LEU C 78  ? 0.0484 0.1049 0.1093 -0.0285 0.0200  0.0039  95  LEU C CG  
2949 C CD1 . LEU C 78  ? 0.1824 0.0859 0.1126 -0.0151 -0.0038 -0.0039 95  LEU C CD1 
2950 C CD2 . LEU C 78  ? 0.0626 0.1797 0.1223 -0.0219 0.0089  -0.0009 95  LEU C CD2 
2951 N N   . CYS C 79  ? 0.0577 0.1086 0.0885 0.0117  0.0042  0.0003  96  CYS C N   
2952 C CA  . CYS C 79  ? 0.0726 0.1076 0.0945 0.0235  0.0182  0.0109  96  CYS C CA  
2953 C C   . CYS C 79  ? 0.0752 0.0989 0.0903 0.0210  0.0105  0.0063  96  CYS C C   
2954 O O   . CYS C 79  ? 0.0883 0.1214 0.0853 0.0198  -0.0030 0.0106  96  CYS C O   
2955 C CB  . CYS C 79  ? 0.0870 0.1303 0.1082 0.0136  0.0259  0.0273  96  CYS C CB  
2956 S SG  . CYS C 79  ? 0.1341 0.1273 0.1235 -0.0022 0.0258  0.0146  96  CYS C SG  
2957 N N   . MET C 80  ? 0.0947 0.0987 0.0888 0.0176  0.0184  -0.0053 97  MET C N   
2958 C CA  . MET C 80  ? 0.0799 0.1277 0.0885 0.0176  0.0176  -0.0160 97  MET C CA  
2959 C C   . MET C 80  ? 0.0723 0.0689 0.0752 0.0113  -0.0050 0.0073  97  MET C C   
2960 O O   . MET C 80  ? 0.1082 0.1025 0.0614 0.0171  -0.0064 0.0118  97  MET C O   
2961 C CB  . MET C 80  ? 0.0891 0.1501 0.0936 0.0117  0.0389  0.0136  97  MET C CB  
2962 C CG  . MET C 80  ? 0.0953 0.1666 0.0961 -0.0175 0.0349  0.0157  97  MET C CG  
2963 S SD  . MET C 80  ? 0.1052 0.1407 0.0978 -0.0033 0.0137  0.0077  97  MET C SD  
2964 C CE  . MET C 80  ? 0.1038 0.1397 0.0916 0.0166  0.0246  -0.0007 97  MET C CE  
2965 N N   . VAL C 81  ? 0.0754 0.1046 0.0774 0.0224  -0.0033 0.0199  98  VAL C N   
2966 C CA  . VAL C 81  ? 0.0879 0.0883 0.0733 -0.0248 -0.0098 -0.0004 98  VAL C CA  
2967 C C   . VAL C 81  ? 0.0687 0.1253 0.0686 -0.0094 0.0073  0.0087  98  VAL C C   
2968 O O   . VAL C 81  ? 0.1321 0.1038 0.0645 0.0079  0.0041  -0.0037 98  VAL C O   
2969 C CB  . VAL C 81  ? 0.1031 0.0868 0.0817 -0.0190 0.0018  -0.0058 98  VAL C CB  
2970 C CG1 . VAL C 81  ? 0.1206 0.1444 0.0835 0.0163  -0.0008 -0.0038 98  VAL C CG1 
2971 C CG2 . VAL C 81  ? 0.0987 0.0904 0.0915 0.0089  0.0246  0.0035  98  VAL C CG2 
2972 N N   . PHE C 82  ? 0.1039 0.1028 0.0758 0.0221  0.0116  0.0151  99  PHE C N   
2973 C CA  . PHE C 82  ? 0.0855 0.1148 0.0784 -0.0310 -0.0013 0.0008  99  PHE C CA  
2974 C C   . PHE C 82  ? 0.1104 0.0715 0.0802 -0.0178 0.0128  0.0240  99  PHE C C   
2975 O O   . PHE C 82  ? 0.1147 0.0649 0.0950 -0.0073 0.0147  0.0121  99  PHE C O   
2976 C CB  . PHE C 82  ? 0.0819 0.1265 0.0775 -0.0226 0.0138  0.0051  99  PHE C CB  
2977 C CG  . PHE C 82  ? 0.1160 0.1443 0.0779 -0.0016 0.0234  0.0130  99  PHE C CG  
2978 C CD1 . PHE C 82  ? 0.1516 0.0945 0.0786 0.0349  0.0162  0.0202  99  PHE C CD1 
2979 C CD2 . PHE C 82  ? 0.1312 0.1382 0.0863 -0.0494 0.0154  0.0056  99  PHE C CD2 
2980 C CE1 . PHE C 82  ? 0.1619 0.1288 0.0931 0.0199  0.0252  0.0101  99  PHE C CE1 
2981 C CE2 . PHE C 82  ? 0.0985 0.1551 0.0849 -0.0108 0.0150  -0.0129 99  PHE C CE2 
2982 C CZ  . PHE C 82  ? 0.0765 0.2408 0.0861 0.0075  0.0094  -0.0148 99  PHE C CZ  
2983 N N   . GLU C 83  ? 0.1111 0.1237 0.0798 0.0127  0.0088  0.0222  100 GLU C N   
2984 C CA  . GLU C 83  ? 0.0882 0.1297 0.0796 0.0231  0.0290  0.0264  100 GLU C CA  
2985 C C   . GLU C 83  ? 0.1064 0.1008 0.0794 -0.0170 0.0197  0.0186  100 GLU C C   
2986 O O   . GLU C 83  ? 0.1077 0.1514 0.0815 -0.0096 0.0252  0.0085  100 GLU C O   
2987 C CB  . GLU C 83  ? 0.1136 0.1436 0.0899 0.0162  0.0152  -0.0081 100 GLU C CB  
2988 C CG  . GLU C 83  ? 0.1108 0.1685 0.1042 0.0316  0.0006  0.0001  100 GLU C CG  
2989 C CD  . GLU C 83  ? 0.1023 0.2339 0.1257 0.0464  0.0153  0.0101  100 GLU C CD  
2990 O OE1 . GLU C 83  ? 0.1661 0.1916 0.1238 0.0057  0.0046  0.0051  100 GLU C OE1 
2991 O OE2 . GLU C 83  ? 0.1352 0.2750 0.1456 0.0284  0.0201  0.0025  100 GLU C OE2 
2992 N N   . GLY C 84  ? 0.0883 0.1100 0.0791 -0.0128 -0.0007 -0.0006 101 GLY C N   
2993 C CA  . GLY C 84  ? 0.0867 0.1079 0.0850 -0.0163 0.0025  -0.0068 101 GLY C CA  
2994 C C   . GLY C 84  ? 0.1120 0.0577 0.0970 -0.0072 0.0113  0.0160  101 GLY C C   
2995 O O   . GLY C 84  ? 0.1313 0.0842 0.1012 0.0010  0.0191  0.0208  101 GLY C O   
2996 N N   . VAL C 85  ? 0.1096 0.1102 0.0988 0.0030  0.0061  0.0032  102 VAL C N   
2997 C CA  . VAL C 85  ? 0.0766 0.1424 0.0996 -0.0138 -0.0139 -0.0273 102 VAL C CA  
2998 C C   . VAL C 85  ? 0.0885 0.1493 0.1035 -0.0145 0.0160  -0.0026 102 VAL C C   
2999 O O   . VAL C 85  ? 0.0789 0.1429 0.1075 0.0019  0.0180  0.0071  102 VAL C O   
3000 C CB  . VAL C 85  ? 0.1361 0.1244 0.1070 0.0104  -0.0204 -0.0182 102 VAL C CB  
3001 C CG1 . VAL C 85  ? 0.2069 0.0942 0.1106 0.0105  0.0057  -0.0286 102 VAL C CG1 
3002 C CG2 . VAL C 85  ? 0.2416 0.1294 0.1181 0.0144  -0.0505 -0.0182 102 VAL C CG2 
3003 N N   . ASP C 86  ? 0.0933 0.1170 0.1057 0.0032  0.0222  -0.0194 103 ASP C N   
3004 C CA  . ASP C 86  ? 0.0770 0.1198 0.1028 0.0102  0.0172  -0.0134 103 ASP C CA  
3005 C C   . ASP C 86  ? 0.1188 0.0711 0.0976 0.0021  0.0060  -0.0088 103 ASP C C   
3006 O O   . ASP C 86  ? 0.0793 0.1333 0.1043 0.0121  0.0070  0.0091  103 ASP C O   
3007 C CB  . ASP C 86  ? 0.1471 0.1069 0.1177 0.0289  0.0253  -0.0115 103 ASP C CB  
3008 C CG  . ASP C 86  ? 0.1534 0.1471 0.1340 -0.0312 0.0429  0.0000  103 ASP C CG  
3009 O OD1 . ASP C 86  ? 0.1575 0.1750 0.1365 -0.0184 0.0433  0.0171  103 ASP C OD1 
3010 O OD2 . ASP C 86  ? 0.2205 0.1441 0.1438 -0.0209 0.0236  -0.0182 103 ASP C OD2 
3011 N N   . VAL C 87  ? 0.1079 0.0548 0.0951 -0.0320 0.0088  0.0084  104 VAL C N   
3012 C CA  . VAL C 87  ? 0.0745 0.1048 0.0957 0.0212  0.0173  0.0158  104 VAL C CA  
3013 C C   . VAL C 87  ? 0.0637 0.0959 0.0979 0.0126  0.0188  0.0132  104 VAL C C   
3014 O O   . VAL C 87  ? 0.0634 0.0769 0.1102 0.0116  0.0202  0.0129  104 VAL C O   
3015 C CB  . VAL C 87  ? 0.1039 0.0713 0.0950 0.0282  0.0116  0.0019  104 VAL C CB  
3016 C CG1 . VAL C 87  ? 0.1023 0.0734 0.0992 0.0075  -0.0033 0.0007  104 VAL C CG1 
3017 C CG2 . VAL C 87  ? 0.1334 0.1118 0.0934 0.0158  0.0059  -0.0008 104 VAL C CG2 
3018 N N   . ILE C 88  ? 0.0608 0.1387 0.0942 0.0117  0.0098  0.0083  105 ILE C N   
3019 C CA  . ILE C 88  ? 0.1038 0.1362 0.0980 0.0384  0.0152  0.0026  105 ILE C CA  
3020 C C   . ILE C 88  ? 0.0984 0.0888 0.0974 0.0313  0.0097  0.0044  105 ILE C C   
3021 O O   . ILE C 88  ? 0.1162 0.1077 0.0986 0.0094  0.0132  0.0169  105 ILE C O   
3022 C CB  . ILE C 88  ? 0.0954 0.0887 0.0992 0.0031  0.0128  0.0059  105 ILE C CB  
3023 C CG1 . ILE C 88  ? 0.1018 0.1112 0.0975 -0.0293 0.0162  -0.0076 105 ILE C CG1 
3024 C CG2 . ILE C 88  ? 0.1245 0.1304 0.1001 0.0049  0.0112  -0.0001 105 ILE C CG2 
3025 C CD1 . ILE C 88  ? 0.1381 0.1035 0.1045 0.0389  0.0249  0.0011  105 ILE C CD1 
3026 N N   . ALA C 89  ? 0.1047 0.0922 0.0929 -0.0113 0.0172  0.0067  106 ALA C N   
3027 C CA  . ALA C 89  ? 0.1170 0.1095 0.0969 -0.0220 0.0127  0.0024  106 ALA C CA  
3028 C C   . ALA C 89  ? 0.0681 0.1369 0.0914 -0.0019 0.0138  0.0079  106 ALA C C   
3029 O O   . ALA C 89  ? 0.1000 0.1208 0.0969 0.0377  0.0124  0.0083  106 ALA C O   
3030 C CB  . ALA C 89  ? 0.0852 0.1746 0.1003 0.0096  0.0029  0.0110  106 ALA C CB  
3031 N N   . GLN C 90  ? 0.0788 0.1060 0.0850 0.0230  0.0117  0.0088  107 GLN C N   
3032 C CA  . GLN C 90  ? 0.0941 0.1028 0.0890 0.0031  0.0178  0.0282  107 GLN C CA  
3033 C C   . GLN C 90  ? 0.1033 0.0824 0.0832 -0.0411 0.0061  0.0116  107 GLN C C   
3034 O O   . GLN C 90  ? 0.0736 0.0960 0.0861 0.0029  0.0040  0.0088  107 GLN C O   
3035 C CB  . GLN C 90  ? 0.1050 0.0852 0.1057 0.0165  0.0248  0.0052  107 GLN C CB  
3036 C CG  . GLN C 90  ? 0.1191 0.0691 0.1171 0.0342  0.0231  -0.0023 107 GLN C CG  
3037 C CD  . GLN C 90  ? 0.1625 0.0883 0.1118 -0.0146 -0.0011 -0.0193 107 GLN C CD  
3038 O OE1 . GLN C 90  ? 0.1069 0.1375 0.1150 0.0027  -0.0084 -0.0077 107 GLN C OE1 
3039 N NE2 . GLN C 90  ? 0.1510 0.1573 0.1080 -0.0210 0.0127  0.0013  107 GLN C NE2 
3040 N N   . ALA C 91  ? 0.0933 0.1048 0.0796 -0.0007 0.0179  0.0141  108 ALA C N   
3041 C CA  . ALA C 91  ? 0.0892 0.0705 0.0817 0.0098  0.0267  -0.0166 108 ALA C CA  
3042 C C   . ALA C 91  ? 0.0876 0.1065 0.0868 0.0236  0.0250  -0.0157 108 ALA C C   
3043 O O   . ALA C 91  ? 0.0952 0.0878 0.0946 0.0183  0.0278  -0.0033 108 ALA C O   
3044 C CB  . ALA C 91  ? 0.1193 0.1065 0.0833 0.0092  0.0229  -0.0215 108 ALA C CB  
3045 N N   . ARG C 92  ? 0.1059 0.1122 0.0925 0.0248  0.0336  -0.0145 109 ARG C N   
3046 C CA  . ARG C 92  ? 0.1279 0.0705 0.1054 -0.0061 0.0240  -0.0047 109 ARG C CA  
3047 C C   . ARG C 92  ? 0.0847 0.0583 0.0982 0.0084  0.0127  0.0011  109 ARG C C   
3048 O O   . ARG C 92  ? 0.0854 0.1563 0.0954 0.0211  0.0062  0.0013  109 ARG C O   
3049 C CB  . ARG C 92  ? 0.1087 0.1114 0.1201 0.0198  0.0241  0.0016  109 ARG C CB  
3050 C CG  . ARG C 92  ? 0.1194 0.1383 0.1344 -0.0178 0.0223  0.0430  109 ARG C CG  
3051 C CD  . ARG C 92  ? 0.0899 0.1669 0.1475 -0.0003 0.0000  0.0476  109 ARG C CD  
3052 N NE  . ARG C 92  ? 0.1105 0.1366 0.1562 -0.0148 0.0108  0.0525  109 ARG C NE  
3053 C CZ  . ARG C 92  ? 0.1653 0.1342 0.1643 -0.0331 -0.0010 0.0598  109 ARG C CZ  
3054 N NH1 . ARG C 92  ? 0.2050 0.2068 0.1704 0.0047  -0.0339 0.0098  109 ARG C NH1 
3055 N NH2 . ARG C 92  ? 0.3127 0.1991 0.1690 0.0111  -0.0213 0.0842  109 ARG C NH2 
3056 N N   . LYS C 93  ? 0.0924 0.0844 0.0984 0.0037  0.0048  0.0060  110 LYS C N   
3057 C CA  . LYS C 93  ? 0.1325 0.1109 0.1103 0.0231  0.0064  -0.0141 110 LYS C CA  
3058 C C   . LYS C 93  ? 0.0499 0.0677 0.1084 0.0275  -0.0093 -0.0024 110 LYS C C   
3059 O O   . LYS C 93  ? 0.0796 0.1387 0.1091 0.0300  -0.0306 -0.0044 110 LYS C O   
3060 C CB  . LYS C 93  ? 0.0851 0.0774 0.1218 0.0009  0.0090  -0.0240 110 LYS C CB  
3061 C CG  . LYS C 93  ? 0.1369 0.0734 0.1325 0.0030  0.0169  -0.0087 110 LYS C CG  
3062 C CD  . LYS C 93  ? 0.1369 0.1261 0.1457 0.0061  0.0116  0.0008  110 LYS C CD  
3063 C CE  . LYS C 93  ? 0.1509 0.1454 0.1558 -0.0011 0.0147  0.0109  110 LYS C CE  
3064 N NZ  . LYS C 93  ? 0.1686 0.1093 0.1667 0.0033  -0.0184 -0.0068 110 LYS C NZ  
3065 N N   . MET C 94  ? 0.0608 0.0947 0.1007 -0.0041 0.0020  0.0097  111 MET C N   
3066 C CA  . MET C 94  ? 0.0842 0.0739 0.0990 -0.0039 0.0129  0.0227  111 MET C CA  
3067 C C   . MET C 94  ? 0.1055 0.0455 0.1037 -0.0055 0.0100  0.0288  111 MET C C   
3068 O O   . MET C 94  ? 0.1010 0.1013 0.1102 -0.0024 0.0255  0.0102  111 MET C O   
3069 C CB  . MET C 94  ? 0.0826 0.1146 0.0995 0.0523  0.0228  0.0200  111 MET C CB  
3070 C CG  . MET C 94  ? 0.0606 0.1314 0.1101 0.0106  0.0032  0.0048  111 MET C CG  
3071 S SD  . MET C 94  ? 0.1240 0.0978 0.1085 0.0114  0.0015  0.0083  111 MET C SD  
3072 C CE  . MET C 94  ? 0.1954 0.1218 0.0991 0.0383  0.0135  0.0238  111 MET C CE  
3073 N N   . MET C 95  ? 0.0824 0.1067 0.1061 0.0110  0.0272  0.0124  112 MET C N   
3074 C CA  . MET C 95  ? 0.0854 0.0778 0.1115 0.0103  0.0116  -0.0029 112 MET C CA  
3075 C C   . MET C 95  ? 0.0844 0.0717 0.1176 -0.0368 0.0081  0.0115  112 MET C C   
3076 O O   . MET C 95  ? 0.0965 0.1179 0.1214 0.0026  0.0111  0.0082  112 MET C O   
3077 C CB  . MET C 95  ? 0.1058 0.0692 0.1303 -0.0088 -0.0023 0.0091  112 MET C CB  
3078 C CG  . MET C 95  ? 0.1364 0.1372 0.1441 0.0385  -0.0098 0.0089  112 MET C CG  
3079 S SD  . MET C 95  ? 0.1225 0.1761 0.1708 -0.0365 -0.0232 0.0391  112 MET C SD  
3080 C CE  . MET C 95  ? 0.1597 0.1313 0.1705 0.0186  -0.0060 0.0200  112 MET C CE  
3081 N N   . GLY C 96  ? 0.1060 0.0871 0.1178 -0.0134 -0.0038 -0.0192 113 GLY C N   
3082 C CA  . GLY C 96  ? 0.0850 0.1413 0.1222 -0.0047 -0.0042 -0.0089 113 GLY C CA  
3083 C C   . GLY C 96  ? 0.1174 0.1038 0.1267 0.0047  0.0182  -0.0087 113 GLY C C   
3084 O O   . GLY C 96  ? 0.1003 0.1616 0.1298 -0.0080 0.0168  0.0016  113 GLY C O   
3085 N N   . SER C 97  ? 0.0808 0.1240 0.1254 -0.0351 0.0083  -0.0079 114 SER C N   
3086 C CA  . SER C 97  ? 0.1430 0.1529 0.1275 -0.0242 0.0084  0.0285  114 SER C CA  
3087 C C   . SER C 97  ? 0.1541 0.0791 0.1240 -0.0085 0.0150  0.0094  114 SER C C   
3088 O O   . SER C 97  ? 0.1276 0.1182 0.1160 0.0232  0.0227  0.0042  114 SER C O   
3089 C CB  . SER C 97  ? 0.1977 0.1491 0.1363 -0.0259 -0.0299 0.0143  114 SER C CB  
3090 O OG  . SER C 97  ? 0.1678 0.2951 0.1574 0.0082  -0.0312 0.0152  114 SER C OG  
3091 N N   . THR C 98  ? 0.1187 0.1052 0.1282 -0.0104 0.0089  -0.0112 115 THR C N   
3092 C CA  A THR C 98  ? 0.1268 0.1268 0.1244 -0.0068 0.0172  0.0051  115 THR C CA  
3093 C CA  B THR C 98  ? 0.1166 0.1443 0.1372 -0.0176 0.0265  0.0092  115 THR C CA  
3094 C C   . THR C 98  ? 0.0771 0.1040 0.1167 0.0006  0.0171  0.0057  115 THR C C   
3095 O O   . THR C 98  ? 0.1153 0.1101 0.1103 0.0127  0.0244  -0.0072 115 THR C O   
3096 C CB  A THR C 98  ? 0.1690 0.1774 0.1270 -0.0045 0.0219  0.0084  115 THR C CB  
3097 C CB  B THR C 98  ? 0.1198 0.2210 0.1625 -0.0198 0.0443  0.0028  115 THR C CB  
3098 O OG1 A THR C 98  ? 0.1917 0.2445 0.1314 0.0250  0.0253  0.0176  115 THR C OG1 
3099 O OG1 B THR C 98  ? 0.1159 0.2530 0.1799 -0.0162 0.0492  0.0161  115 THR C OG1 
3100 C CG2 A THR C 98  ? 0.1796 0.1593 0.1261 -0.0404 0.0179  0.0108  115 THR C CG2 
3101 C CG2 B THR C 98  ? 0.1589 0.2593 0.1717 -0.0121 0.0566  0.0299  115 THR C CG2 
3102 N N   . ARG C 99  ? 0.0924 0.1461 0.1100 0.0324  -0.0113 0.0012  116 ARG C N   
3103 C CA  . ARG C 99  ? 0.1228 0.0758 0.1066 0.0045  -0.0149 -0.0110 116 ARG C CA  
3104 C C   . ARG C 99  ? 0.1008 0.0875 0.0997 -0.0370 0.0131  0.0091  116 ARG C C   
3105 O O   . ARG C 99  ? 0.1298 0.1222 0.0960 -0.0130 0.0041  0.0033  116 ARG C O   
3106 C CB  . ARG C 99  ? 0.1619 0.0704 0.1264 0.0189  -0.0242 -0.0035 116 ARG C CB  
3107 C CG  . ARG C 99  ? 0.2367 0.1636 0.1435 -0.0997 -0.0339 0.0421  116 ARG C CG  
3108 C CD  . ARG C 99  ? 0.3834 0.2424 0.1643 -0.0777 -0.0680 0.0679  116 ARG C CD  
3109 N NE  . ARG C 99  ? 0.5906 0.5531 0.1934 -0.0114 -0.0809 0.0505  116 ARG C NE  
3110 C CZ  . ARG C 99  ? 0.7871 0.7473 0.2252 0.0604  -0.0675 0.0578  116 ARG C CZ  
3111 N NH1 . ARG C 99  ? 0.8375 0.7956 0.2289 0.0243  -0.0709 0.0470  116 ARG C NH1 
3112 N NH2 . ARG C 99  ? 0.8572 0.7850 0.2495 0.1060  -0.0554 0.0629  116 ARG C NH2 
3113 N N   . PRO C 100 ? 0.0806 0.1202 0.1001 -0.0314 0.0200  0.0108  117 PRO C N   
3114 C CA  . PRO C 100 ? 0.0899 0.1234 0.1040 -0.0142 0.0144  0.0072  117 PRO C CA  
3115 C C   . PRO C 100 ? 0.1014 0.1101 0.1061 -0.0172 0.0109  0.0086  117 PRO C C   
3116 O O   . PRO C 100 ? 0.1150 0.1185 0.1095 -0.0176 0.0014  0.0054  117 PRO C O   
3117 C CB  . PRO C 100 ? 0.0786 0.1427 0.1037 0.0032  0.0271  0.0175  117 PRO C CB  
3118 C CG  . PRO C 100 ? 0.1343 0.1187 0.1058 0.0443  0.0192  0.0015  117 PRO C CG  
3119 C CD  . PRO C 100 ? 0.1645 0.1015 0.1022 -0.0169 0.0310  0.0052  117 PRO C CD  
3120 N N   . GLY C 101 ? 0.1114 0.1266 0.1110 0.0232  0.0150  0.0097  118 GLY C N   
3121 C CA  . GLY C 101 ? 0.0891 0.1281 0.1168 -0.0168 -0.0081 -0.0070 118 GLY C CA  
3122 C C   . GLY C 101 ? 0.0936 0.1305 0.1166 -0.0300 -0.0017 0.0104  118 GLY C C   
3123 O O   . GLY C 101 ? 0.1113 0.1777 0.1254 -0.0061 0.0092  -0.0069 118 GLY C O   
3124 N N   . GLU C 102 ? 0.1095 0.1134 0.1121 0.0060  -0.0147 0.0134  119 GLU C N   
3125 C CA  . GLU C 102 ? 0.1411 0.0703 0.1106 -0.0329 -0.0049 0.0038  119 GLU C CA  
3126 C C   . GLU C 102 ? 0.1091 0.1335 0.1176 0.0371  0.0041  -0.0044 119 GLU C C   
3127 O O   . GLU C 102 ? 0.1200 0.1876 0.1243 0.0290  0.0025  0.0036  119 GLU C O   
3128 C CB  . GLU C 102 ? 0.1883 0.1357 0.1075 -0.0287 0.0035  0.0350  119 GLU C CB  
3129 C CG  . GLU C 102 ? 0.2490 0.2081 0.1094 0.0480  -0.0086 0.0435  119 GLU C CG  
3130 C CD  . GLU C 102 ? 0.2602 0.2710 0.1185 0.1093  -0.0080 0.0263  119 GLU C CD  
3131 O OE1 . GLU C 102 ? 0.3424 0.1999 0.1191 0.1179  -0.0042 0.0036  119 GLU C OE1 
3132 O OE2 . GLU C 102 ? 0.2966 0.4004 0.1339 0.0815  -0.0094 0.0495  119 GLU C OE2 
3133 N N   . ALA C 103 ? 0.1082 0.1132 0.1218 0.0455  0.0049  -0.0264 120 ALA C N   
3134 C CA  . ALA C 103 ? 0.0923 0.0976 0.1340 0.0300  -0.0062 0.0052  120 ALA C CA  
3135 C C   . ALA C 103 ? 0.1153 0.1424 0.1504 -0.0026 -0.0212 -0.0150 120 ALA C C   
3136 O O   . ALA C 103 ? 0.1217 0.1322 0.1651 0.0204  -0.0060 -0.0054 120 ALA C O   
3137 C CB  . ALA C 103 ? 0.1024 0.0898 0.1326 -0.0133 -0.0060 -0.0014 120 ALA C CB  
3138 N N   . ALA C 104 ? 0.1264 0.1090 0.1606 0.0093  -0.0277 -0.0245 121 ALA C N   
3139 C CA  . ALA C 104 ? 0.1422 0.0770 0.1741 0.0051  -0.0268 -0.0049 121 ALA C CA  
3140 C C   . ALA C 104 ? 0.1106 0.1037 0.1937 -0.0155 -0.0298 0.0011  121 ALA C C   
3141 O O   . ALA C 104 ? 0.0874 0.0891 0.1939 -0.0046 -0.0022 -0.0298 121 ALA C O   
3142 C CB  . ALA C 104 ? 0.1409 0.0823 0.1722 0.0062  -0.0099 -0.0143 121 ALA C CB  
3143 N N   . PRO C 105 ? 0.1439 0.2009 0.2107 -0.0427 -0.0658 0.0282  122 PRO C N   
3144 C CA  . PRO C 105 ? 0.0984 0.2225 0.2061 -0.0482 -0.0503 0.0380  122 PRO C CA  
3145 C C   . PRO C 105 ? 0.1035 0.1560 0.1878 -0.0273 -0.0347 0.0238  122 PRO C C   
3146 O O   . PRO C 105 ? 0.1745 0.1230 0.1882 -0.0238 -0.0305 -0.0012 122 PRO C O   
3147 C CB  . PRO C 105 ? 0.1399 0.3194 0.2191 -0.0700 -0.0644 0.0621  122 PRO C CB  
3148 C CG  . PRO C 105 ? 0.1608 0.3984 0.2229 -0.0801 -0.0611 0.0637  122 PRO C CG  
3149 C CD  . PRO C 105 ? 0.1787 0.3019 0.2186 -0.0838 -0.0741 0.0545  122 PRO C CD  
3150 N N   . GLY C 106 ? 0.0997 0.1274 0.1752 -0.0540 0.0024  0.0270  123 GLY C N   
3151 C CA  . GLY C 106 ? 0.1148 0.1512 0.1548 -0.0590 0.0183  0.0443  123 GLY C CA  
3152 C C   . GLY C 106 ? 0.1159 0.1313 0.1356 -0.0419 0.0277  0.0191  123 GLY C C   
3153 O O   . GLY C 106 ? 0.1982 0.1678 0.1369 0.0315  0.0023  0.0375  123 GLY C O   
3154 N N   . THR C 107 ? 0.0822 0.0837 0.1202 -0.0139 0.0157  -0.0035 124 THR C N   
3155 C CA  . THR C 107 ? 0.0919 0.0783 0.1074 -0.0103 0.0070  -0.0058 124 THR C CA  
3156 C C   . THR C 107 ? 0.0440 0.1137 0.0988 -0.0131 0.0087  -0.0047 124 THR C C   
3157 O O   . THR C 107 ? 0.0620 0.1063 0.0988 0.0096  0.0208  -0.0003 124 THR C O   
3158 C CB  . THR C 107 ? 0.1075 0.0787 0.1132 0.0105  0.0129  0.0016  124 THR C CB  
3159 O OG1 . THR C 107 ? 0.1199 0.0780 0.1114 -0.0218 0.0064  0.0110  124 THR C OG1 
3160 C CG2 . THR C 107 ? 0.1170 0.1185 0.1170 0.0070  0.0300  0.0069  124 THR C CG2 
3161 N N   . ILE C 108 ? 0.0947 0.0850 0.0969 -0.0010 0.0114  -0.0055 125 ILE C N   
3162 C CA  . ILE C 108 ? 0.0835 0.0903 0.0911 0.0436  0.0004  -0.0148 125 ILE C CA  
3163 C C   . ILE C 108 ? 0.0980 0.1081 0.0927 0.0008  0.0098  -0.0154 125 ILE C C   
3164 O O   . ILE C 108 ? 0.1014 0.1544 0.0918 0.0118  0.0118  -0.0384 125 ILE C O   
3165 C CB  . ILE C 108 ? 0.0667 0.1284 0.0947 0.0000  -0.0085 -0.0104 125 ILE C CB  
3166 C CG1 . ILE C 108 ? 0.1182 0.1608 0.0982 0.0591  -0.0069 0.0139  125 ILE C CG1 
3167 C CG2 . ILE C 108 ? 0.0638 0.1537 0.1050 -0.0124 -0.0084 -0.0247 125 ILE C CG2 
3168 C CD1 . ILE C 108 ? 0.1015 0.2637 0.1012 0.0419  0.0026  0.0267  125 ILE C CD1 
3169 N N   . ARG C 109 ? 0.0800 0.1038 0.0970 0.0359  0.0251  -0.0189 126 ARG C N   
3170 C CA  . ARG C 109 ? 0.0889 0.1080 0.1077 0.0508  0.0145  -0.0180 126 ARG C CA  
3171 C C   . ARG C 109 ? 0.1021 0.0766 0.0998 0.0214  -0.0027 0.0125  126 ARG C C   
3172 O O   . ARG C 109 ? 0.0996 0.0884 0.1066 0.0243  0.0200  0.0078  126 ARG C O   
3173 C CB  . ARG C 109 ? 0.1163 0.1246 0.1247 0.0433  0.0221  -0.0184 126 ARG C CB  
3174 C CG  . ARG C 109 ? 0.1925 0.1563 0.1364 -0.0947 0.0466  -0.0262 126 ARG C CG  
3175 C CD  . ARG C 109 ? 0.2139 0.1167 0.1478 -0.0833 0.0185  -0.0187 126 ARG C CD  
3176 N NE  . ARG C 109 ? 0.1446 0.0596 0.1374 -0.0220 0.0091  -0.0132 126 ARG C NE  
3177 C CZ  . ARG C 109 ? 0.1102 0.1112 0.1247 -0.0170 -0.0040 -0.0017 126 ARG C CZ  
3178 N NH1 . ARG C 109 ? 0.1655 0.1784 0.1294 -0.0183 -0.0019 -0.0305 126 ARG C NH1 
3179 N NH2 . ARG C 109 ? 0.1138 0.1255 0.1184 -0.0029 0.0117  0.0036  126 ARG C NH2 
3180 N N   . ALA C 110 ? 0.0638 0.1022 0.0948 0.0187  0.0070  0.0104  127 ALA C N   
3181 C CA  . ALA C 110 ? 0.0747 0.1083 0.0990 -0.0017 0.0151  -0.0052 127 ALA C CA  
3182 C C   . ALA C 110 ? 0.0499 0.1474 0.1036 0.0116  -0.0054 -0.0012 127 ALA C C   
3183 O O   . ALA C 110 ? 0.0887 0.1570 0.1050 0.0304  0.0175  0.0288  127 ALA C O   
3184 C CB  . ALA C 110 ? 0.0954 0.1678 0.0889 -0.0262 0.0071  -0.0123 127 ALA C CB  
3185 N N   . ASP C 111 ? 0.0869 0.0805 0.1050 0.0222  -0.0037 -0.0068 128 ASP C N   
3186 C CA  . ASP C 111 ? 0.0521 0.0737 0.1185 0.0040  0.0157  0.0014  128 ASP C CA  
3187 C C   . ASP C 111 ? 0.1093 0.0459 0.1008 0.0069  0.0016  -0.0126 128 ASP C C   
3188 O O   . ASP C 111 ? 0.0859 0.1163 0.0868 0.0219  0.0179  0.0079  128 ASP C O   
3189 C CB  . ASP C 111 ? 0.0772 0.0880 0.1440 0.0427  -0.0016 0.0053  128 ASP C CB  
3190 C CG  . ASP C 111 ? 0.1483 0.1278 0.1799 0.0434  -0.0303 0.0145  128 ASP C CG  
3191 O OD1 . ASP C 111 ? 0.2179 0.1675 0.2071 0.0905  -0.0360 -0.0062 128 ASP C OD1 
3192 O OD2 . ASP C 111 ? 0.1805 0.1331 0.1899 0.0450  -0.0025 0.0130  128 ASP C OD2 
3193 N N   . PHE C 112 ? 0.0897 0.0435 0.0961 -0.0023 0.0123  -0.0007 129 PHE C N   
3194 C CA  . PHE C 112 ? 0.0608 0.1136 0.0894 0.0142  0.0108  0.0230  129 PHE C CA  
3195 C C   . PHE C 112 ? 0.0637 0.1015 0.0861 -0.0236 -0.0081 0.0050  129 PHE C C   
3196 O O   . PHE C 112 ? 0.0878 0.1124 0.0857 -0.0021 0.0113  0.0117  129 PHE C O   
3197 C CB  . PHE C 112 ? 0.0718 0.0984 0.0907 0.0115  0.0196  0.0282  129 PHE C CB  
3198 C CG  . PHE C 112 ? 0.1033 0.1199 0.0880 -0.0397 0.0036  0.0045  129 PHE C CG  
3199 C CD1 . PHE C 112 ? 0.0938 0.1274 0.0888 -0.0059 -0.0343 0.0068  129 PHE C CD1 
3200 C CD2 . PHE C 112 ? 0.1299 0.1235 0.0944 -0.0191 0.0011  0.0051  129 PHE C CD2 
3201 C CE1 . PHE C 112 ? 0.1495 0.1453 0.0912 0.0016  -0.0336 0.0032  129 PHE C CE1 
3202 C CE2 . PHE C 112 ? 0.1083 0.1147 0.0963 -0.0255 -0.0048 0.0082  129 PHE C CE2 
3203 C CZ  . PHE C 112 ? 0.1157 0.1525 0.0947 -0.0243 -0.0138 0.0243  129 PHE C CZ  
3204 N N   . CYS C 113 ? 0.0518 0.1086 0.0935 -0.0042 -0.0198 0.0108  130 CYS C N   
3205 C CA  . CYS C 113 ? 0.0915 0.0605 0.0873 0.0135  0.0078  0.0028  130 CYS C CA  
3206 C C   . CYS C 113 ? 0.0819 0.1001 0.0937 -0.0221 0.0006  0.0127  130 CYS C C   
3207 O O   . CYS C 113 ? 0.0695 0.1082 0.1008 -0.0071 0.0034  0.0161  130 CYS C O   
3208 C CB  . CYS C 113 ? 0.0840 0.0913 0.0960 0.0147  -0.0066 0.0209  130 CYS C CB  
3209 S SG  . CYS C 113 ? 0.0853 0.1325 0.1029 0.0007  -0.0010 0.0284  130 CYS C SG  
3210 N N   . GLN C 114 ? 0.1293 0.0778 0.0869 0.0061  -0.0043 0.0196  131 GLN C N   
3211 C CA  . GLN C 114 ? 0.0769 0.0738 0.0893 -0.0328 -0.0049 0.0163  131 GLN C CA  
3212 C C   . GLN C 114 ? 0.1348 0.0560 0.0928 -0.0037 -0.0034 0.0042  131 GLN C C   
3213 O O   . GLN C 114 ? 0.1088 0.1496 0.0835 -0.0252 -0.0140 -0.0025 131 GLN C O   
3214 C CB  . GLN C 114 ? 0.1375 0.1180 0.0897 0.0102  -0.0131 0.0168  131 GLN C CB  
3215 C CG  . GLN C 114 ? 0.1284 0.0961 0.0930 0.0429  0.0209  0.0269  131 GLN C CG  
3216 C CD  . GLN C 114 ? 0.1312 0.0532 0.1003 -0.0048 0.0061  0.0320  131 GLN C CD  
3217 O OE1 . GLN C 114 ? 0.1056 0.1011 0.1097 0.0189  0.0138  0.0262  131 GLN C OE1 
3218 N NE2 . GLN C 114 ? 0.1067 0.1050 0.0978 0.0084  0.0048  0.0244  131 GLN C NE2 
3219 N N   . GLN C 115 ? 0.1018 0.0687 0.0973 -0.0210 0.0115  0.0158  132 GLN C N   
3220 C CA  . GLN C 115 ? 0.0999 0.1438 0.1073 0.0161  0.0224  0.0257  132 GLN C CA  
3221 C C   . GLN C 115 ? 0.0833 0.0859 0.0999 -0.0067 0.0322  0.0397  132 GLN C C   
3222 O O   . GLN C 115 ? 0.1093 0.1058 0.0952 0.0141  0.0136  0.0380  132 GLN C O   
3223 C CB  . GLN C 115 ? 0.1376 0.0782 0.1286 -0.0017 -0.0027 0.0231  132 GLN C CB  
3224 C CG  . GLN C 115 ? 0.1695 0.1153 0.1457 0.0152  0.0050  0.0199  132 GLN C CG  
3225 C CD  . GLN C 115 ? 0.1529 0.1689 0.1541 0.0088  0.0013  0.0372  132 GLN C CD  
3226 O OE1 . GLN C 115 ? 0.1269 0.1975 0.1658 -0.0147 0.0107  0.0135  132 GLN C OE1 
3227 N NE2 . GLN C 115 ? 0.2107 0.3055 0.1576 0.0815  -0.0094 0.0666  132 GLN C NE2 
3228 N N   . ALA C 116 ? 0.1020 0.1175 0.1054 0.0173  0.0560  0.0048  133 ALA C N   
3229 C CA  . ALA C 116 ? 0.0723 0.1655 0.1124 -0.0204 0.0345  0.0127  133 ALA C CA  
3230 C C   . ALA C 116 ? 0.1174 0.1393 0.1184 0.0007  0.0348  0.0199  133 ALA C C   
3231 O O   . ALA C 116 ? 0.1316 0.1555 0.1292 0.0530  0.0117  0.0148  133 ALA C O   
3232 C CB  . ALA C 116 ? 0.1112 0.1477 0.1154 0.0148  0.0271  0.0001  133 ALA C CB  
3233 N N   . GLY C 117 ? 0.1159 0.1509 0.1200 -0.0131 0.0197  0.0337  134 GLY C N   
3234 C CA  . GLY C 117 ? 0.1253 0.1730 0.1264 0.0268  0.0145  0.0244  134 GLY C CA  
3235 C C   . GLY C 117 ? 0.1484 0.1221 0.1304 0.0138  -0.0056 0.0117  134 GLY C C   
3236 O O   . GLY C 117 ? 0.1592 0.1237 0.1274 -0.0479 -0.0058 0.0057  134 GLY C O   
3237 N N   . ARG C 118 ? 0.1127 0.0891 0.1293 -0.0182 -0.0045 0.0006  135 ARG C N   
3238 C CA  . ARG C 118 ? 0.0940 0.1268 0.1266 0.0036  0.0073  0.0172  135 ARG C CA  
3239 C C   . ARG C 118 ? 0.1060 0.0992 0.1172 0.0169  0.0093  -0.0024 135 ARG C C   
3240 O O   . ARG C 118 ? 0.0976 0.1108 0.1239 0.0019  0.0167  -0.0107 135 ARG C O   
3241 C CB  . ARG C 118 ? 0.1054 0.1133 0.1347 -0.0196 0.0139  0.0293  135 ARG C CB  
3242 C CG  . ARG C 118 ? 0.1053 0.0813 0.1434 -0.0169 0.0251  0.0357  135 ARG C CG  
3243 C CD  . ARG C 118 ? 0.1225 0.0794 0.1451 -0.0001 0.0164  0.0381  135 ARG C CD  
3244 N NE  . ARG C 118 ? 0.1520 0.1066 0.1622 -0.0134 0.0032  0.0315  135 ARG C NE  
3245 C CZ  . ARG C 118 ? 0.2030 0.0764 0.1798 -0.0470 -0.0202 0.0206  135 ARG C CZ  
3246 N NH1 . ARG C 118 ? 0.2183 0.1401 0.1851 -0.0360 -0.0625 0.0382  135 ARG C NH1 
3247 N NH2 . ARG C 118 ? 0.2603 0.1184 0.1908 -0.0466 -0.0230 -0.0102 135 ARG C NH2 
3248 N N   . ASN C 119 ? 0.0617 0.0962 0.1014 0.0214  0.0006  -0.0016 136 ASN C N   
3249 C CA  . ASN C 119 ? 0.0780 0.0618 0.0997 0.0168  0.0144  0.0255  136 ASN C CA  
3250 C C   . ASN C 119 ? 0.1015 0.0451 0.0903 -0.0174 0.0148  0.0169  136 ASN C C   
3251 O O   . ASN C 119 ? 0.0929 0.0730 0.0932 0.0134  0.0065  -0.0007 136 ASN C O   
3252 C CB  . ASN C 119 ? 0.0402 0.0737 0.1055 -0.0084 0.0038  0.0090  136 ASN C CB  
3253 C CG  . ASN C 119 ? 0.0593 0.0936 0.1087 -0.0206 -0.0060 -0.0094 136 ASN C CG  
3254 O OD1 . ASN C 119 ? 0.0900 0.1233 0.1082 0.0139  -0.0190 0.0044  136 ASN C OD1 
3255 N ND2 . ASN C 119 ? 0.1189 0.1261 0.1188 0.0204  0.0166  -0.0098 136 ASN C ND2 
3256 N N   . LEU C 120 ? 0.0730 0.1115 0.0949 -0.0117 -0.0194 0.0010  137 LEU C N   
3257 C CA  . LEU C 120 ? 0.0533 0.0968 0.0954 -0.0296 0.0088  0.0052  137 LEU C CA  
3258 C C   . LEU C 120 ? 0.0377 0.1064 0.0991 -0.0197 0.0143  0.0025  137 LEU C C   
3259 O O   . LEU C 120 ? 0.0653 0.0866 0.1074 0.0076  0.0082  -0.0170 137 LEU C O   
3260 C CB  . LEU C 120 ? 0.0869 0.1008 0.0876 0.0008  0.0082  0.0028  137 LEU C CB  
3261 C CG  . LEU C 120 ? 0.1147 0.0956 0.0972 -0.0275 0.0172  0.0159  137 LEU C CG  
3262 C CD1 . LEU C 120 ? 0.0903 0.1384 0.0932 -0.0218 0.0134  -0.0060 137 LEU C CD1 
3263 C CD2 . LEU C 120 ? 0.1006 0.1029 0.0985 -0.0451 0.0167  0.0192  137 LEU C CD2 
3264 N N   . ILE C 121 ? 0.0560 0.1186 0.0914 0.0057  0.0318  0.0255  138 ILE C N   
3265 C CA  . ILE C 121 ? 0.0954 0.0890 0.0938 -0.0160 0.0162  -0.0137 138 ILE C CA  
3266 C C   . ILE C 121 ? 0.0633 0.1119 0.0917 -0.0078 0.0030  -0.0014 138 ILE C C   
3267 O O   . ILE C 121 ? 0.0613 0.1579 0.0933 0.0149  0.0075  -0.0054 138 ILE C O   
3268 C CB  . ILE C 121 ? 0.0997 0.1250 0.1006 0.0171  0.0259  -0.0081 138 ILE C CB  
3269 C CG1 . ILE C 121 ? 0.1477 0.1291 0.1118 -0.0304 0.0462  0.0154  138 ILE C CG1 
3270 C CG2 . ILE C 121 ? 0.1337 0.0802 0.1058 -0.0185 0.0317  -0.0091 138 ILE C CG2 
3271 C CD1 . ILE C 121 ? 0.1628 0.1978 0.1171 -0.0612 0.0438  0.0168  138 ILE C CD1 
3272 N N   . HIS C 122 ? 0.0805 0.1385 0.0876 -0.0087 0.0084  0.0135  139 HIS C N   
3273 C CA  . HIS C 122 ? 0.0695 0.1108 0.0927 0.0053  0.0155  0.0108  139 HIS C CA  
3274 C C   . HIS C 122 ? 0.0575 0.1131 0.0859 -0.0260 0.0190  0.0162  139 HIS C C   
3275 O O   . HIS C 122 ? 0.0948 0.1117 0.0861 0.0158  0.0240  0.0286  139 HIS C O   
3276 C CB  . HIS C 122 ? 0.0936 0.1350 0.1006 0.0027  0.0380  0.0301  139 HIS C CB  
3277 C CG  . HIS C 122 ? 0.1186 0.1160 0.1007 -0.0287 0.0512  0.0044  139 HIS C CG  
3278 N ND1 . HIS C 122 ? 0.1031 0.1378 0.1016 -0.0166 0.0525  0.0249  139 HIS C ND1 
3279 C CD2 . HIS C 122 ? 0.1244 0.1557 0.1013 -0.0134 0.0275  -0.0036 139 HIS C CD2 
3280 C CE1 . HIS C 122 ? 0.1706 0.1843 0.1086 -0.0147 0.0421  -0.0002 139 HIS C CE1 
3281 N NE2 . HIS C 122 ? 0.1359 0.1480 0.1069 -0.0036 0.0397  -0.0009 139 HIS C NE2 
3282 N N   . GLY C 123 ? 0.0606 0.1215 0.0823 0.0095  0.0269  -0.0024 140 GLY C N   
3283 C CA  . GLY C 123 ? 0.0514 0.1417 0.0791 0.0134  0.0222  -0.0029 140 GLY C CA  
3284 C C   . GLY C 123 ? 0.0990 0.0662 0.0816 0.0253  0.0080  -0.0039 140 GLY C C   
3285 O O   . GLY C 123 ? 0.0680 0.1150 0.0891 0.0104  0.0163  0.0123  140 GLY C O   
3286 N N   . SER C 124 ? 0.0908 0.1306 0.0790 0.0352  0.0269  0.0231  141 SER C N   
3287 C CA  . SER C 124 ? 0.0713 0.1290 0.0861 0.0156  0.0321  0.0201  141 SER C CA  
3288 C C   . SER C 124 ? 0.0562 0.1314 0.0896 -0.0003 0.0213  0.0049  141 SER C C   
3289 O O   . SER C 124 ? 0.0866 0.1430 0.0930 -0.0071 0.0233  0.0003  141 SER C O   
3290 C CB  . SER C 124 ? 0.0848 0.1731 0.0900 0.0331  0.0177  -0.0045 141 SER C CB  
3291 O OG  . SER C 124 ? 0.0877 0.1784 0.0995 0.0010  0.0016  -0.0323 141 SER C OG  
3292 N N   . ASP C 125 ? 0.1043 0.1492 0.0870 -0.0226 0.0305  0.0013  142 ASP C N   
3293 C CA  . ASP C 125 ? 0.0918 0.1457 0.0947 -0.0152 0.0259  -0.0033 142 ASP C CA  
3294 C C   . ASP C 125 ? 0.0838 0.1803 0.0951 -0.0138 0.0161  -0.0030 142 ASP C C   
3295 O O   . ASP C 125 ? 0.1406 0.2199 0.1063 -0.0502 0.0144  -0.0358 142 ASP C O   
3296 C CB  . ASP C 125 ? 0.1297 0.2100 0.1042 0.0178  0.0179  -0.0013 142 ASP C CB  
3297 C CG  . ASP C 125 ? 0.1162 0.2847 0.1192 0.0774  0.0002  0.0239  142 ASP C CG  
3298 O OD1 . ASP C 125 ? 0.1287 0.2613 0.1245 0.0217  -0.0032 0.0439  142 ASP C OD1 
3299 O OD2 . ASP C 125 ? 0.1862 0.3472 0.1328 0.0995  -0.0166 0.0415  142 ASP C OD2 
3300 N N   . SER C 126 ? 0.0517 0.1287 0.0937 0.0140  0.0160  0.0171  143 SER C N   
3301 C CA  . SER C 126 ? 0.0572 0.1254 0.0907 0.0014  0.0196  0.0230  143 SER C CA  
3302 C C   . SER C 126 ? 0.0686 0.1307 0.0923 -0.0085 0.0198  0.0120  143 SER C C   
3303 O O   . SER C 126 ? 0.0765 0.1426 0.0938 -0.0193 -0.0013 0.0144  143 SER C O   
3304 C CB  . SER C 126 ? 0.0885 0.1439 0.0912 0.0209  0.0279  0.0075  143 SER C CB  
3305 O OG  . SER C 126 ? 0.0944 0.1521 0.0911 -0.0109 0.0278  0.0036  143 SER C OG  
3306 N N   . ALA C 127 ? 0.0939 0.1334 0.0929 -0.0266 0.0323  -0.0046 144 ALA C N   
3307 C CA  . ALA C 127 ? 0.1016 0.1088 0.0896 -0.0160 0.0210  -0.0055 144 ALA C CA  
3308 C C   . ALA C 127 ? 0.1072 0.1204 0.0847 -0.0287 0.0109  -0.0211 144 ALA C C   
3309 O O   . ALA C 127 ? 0.1271 0.1370 0.0826 0.0057  0.0125  -0.0041 144 ALA C O   
3310 C CB  . ALA C 127 ? 0.1202 0.1372 0.0936 0.0295  0.0252  0.0074  144 ALA C CB  
3311 N N   . GLU C 128 ? 0.0958 0.1296 0.0833 -0.0215 0.0253  0.0149  145 GLU C N   
3312 C CA  . GLU C 128 ? 0.1353 0.1078 0.0841 -0.0185 0.0222  0.0090  145 GLU C CA  
3313 C C   . GLU C 128 ? 0.1439 0.1152 0.0821 0.0086  0.0234  0.0107  145 GLU C C   
3314 O O   . GLU C 128 ? 0.0991 0.1478 0.0853 -0.0307 0.0173  -0.0058 145 GLU C O   
3315 C CB  . GLU C 128 ? 0.1424 0.1181 0.0913 -0.0265 -0.0092 -0.0070 145 GLU C CB  
3316 C CG  . GLU C 128 ? 0.1600 0.1413 0.1032 -0.0505 -0.0026 0.0146  145 GLU C CG  
3317 C CD  . GLU C 128 ? 0.1923 0.1768 0.1243 -0.0731 0.0126  0.0243  145 GLU C CD  
3318 O OE1 . GLU C 128 ? 0.1679 0.2137 0.1324 -0.0517 0.0146  0.0129  145 GLU C OE1 
3319 O OE2 . GLU C 128 ? 0.2464 0.1780 0.1395 -0.0248 0.0262  -0.0110 145 GLU C OE2 
3320 N N   . SER C 129 ? 0.1371 0.1305 0.0849 -0.0099 0.0206  -0.0022 146 SER C N   
3321 C CA  A SER C 129 ? 0.0849 0.1010 0.0912 0.0003  0.0178  -0.0112 146 SER C CA  
3322 C CA  B SER C 129 ? 0.1439 0.1225 0.0877 0.0082  0.0212  -0.0088 146 SER C CA  
3323 C C   . SER C 129 ? 0.0658 0.1015 0.0884 -0.0209 0.0225  -0.0028 146 SER C C   
3324 O O   . SER C 129 ? 0.1149 0.1238 0.0834 -0.0068 0.0038  -0.0060 146 SER C O   
3325 C CB  A SER C 129 ? 0.0992 0.0807 0.1010 -0.0046 0.0019  -0.0059 146 SER C CB  
3326 C CB  B SER C 129 ? 0.2493 0.1533 0.0895 0.0420  0.0106  -0.0050 146 SER C CB  
3327 O OG  A SER C 129 ? 0.0830 0.1167 0.1108 -0.0261 0.0106  0.0232  146 SER C OG  
3328 O OG  B SER C 129 ? 0.3371 0.2527 0.0968 0.0666  0.0097  0.0157  146 SER C OG  
3329 N N   . ALA C 130 ? 0.0879 0.0848 0.0894 -0.0107 -0.0010 -0.0168 147 ALA C N   
3330 C CA  . ALA C 130 ? 0.0940 0.1167 0.0840 -0.0081 0.0219  0.0004  147 ALA C CA  
3331 C C   . ALA C 130 ? 0.1134 0.1474 0.0802 0.0031  0.0269  0.0094  147 ALA C C   
3332 O O   . ALA C 130 ? 0.1357 0.1692 0.0761 0.0124  0.0049  -0.0075 147 ALA C O   
3333 C CB  . ALA C 130 ? 0.0768 0.1533 0.0826 0.0033  0.0396  0.0035  147 ALA C CB  
3334 N N   . LYS C 131 ? 0.0901 0.1507 0.0836 0.0122  0.0240  0.0107  148 LYS C N   
3335 C CA  . LYS C 131 ? 0.0901 0.1904 0.0966 0.0389  0.0128  0.0026  148 LYS C CA  
3336 C C   . LYS C 131 ? 0.0955 0.1941 0.0971 0.0261  0.0194  0.0083  148 LYS C C   
3337 O O   . LYS C 131 ? 0.0866 0.1663 0.0958 0.0016  -0.0008 0.0056  148 LYS C O   
3338 C CB  . LYS C 131 ? 0.1202 0.1917 0.1196 0.0484  0.0004  -0.0085 148 LYS C CB  
3339 C CG  . LYS C 131 ? 0.1494 0.2973 0.1418 0.0073  0.0247  -0.0036 148 LYS C CG  
3340 C CD  . LYS C 131 ? 0.1302 0.4107 0.1612 0.0076  0.0373  -0.0170 148 LYS C CD  
3341 C CE  . LYS C 131 ? 0.1713 0.4579 0.1788 -0.0296 0.0573  -0.0117 148 LYS C CE  
3342 N NZ  . LYS C 131 ? 0.2760 0.5708 0.1833 0.0076  0.0636  -0.0025 148 LYS C NZ  
3343 N N   . ARG C 132 ? 0.1045 0.1128 0.1009 -0.0078 0.0163  0.0029  149 ARG C N   
3344 C CA  . ARG C 132 ? 0.0738 0.1709 0.1012 -0.0217 0.0182  0.0032  149 ARG C CA  
3345 C C   . ARG C 132 ? 0.0746 0.1364 0.0913 -0.0143 0.0084  -0.0094 149 ARG C C   
3346 O O   . ARG C 132 ? 0.1134 0.1527 0.0891 -0.0259 0.0148  -0.0151 149 ARG C O   
3347 C CB  . ARG C 132 ? 0.1438 0.1873 0.1164 -0.0594 0.0150  -0.0044 149 ARG C CB  
3348 C CG  . ARG C 132 ? 0.2376 0.1626 0.1358 -0.0028 0.0120  -0.0241 149 ARG C CG  
3349 C CD  . ARG C 132 ? 0.3092 0.2508 0.1562 0.0716  -0.0107 -0.0304 149 ARG C CD  
3350 N NE  . ARG C 132 ? 0.4199 0.3689 0.1847 0.2121  -0.0410 -0.0266 149 ARG C NE  
3351 C CZ  . ARG C 132 ? 0.3873 0.3792 0.2087 0.2244  -0.0480 -0.0356 149 ARG C CZ  
3352 N NH1 . ARG C 132 ? 0.3435 0.3670 0.2226 0.1717  -0.0594 -0.0471 149 ARG C NH1 
3353 N NH2 . ARG C 132 ? 0.3894 0.3560 0.2160 0.1632  -0.0458 -0.0143 149 ARG C NH2 
3354 N N   . GLU C 133 ? 0.0614 0.1184 0.0882 -0.0170 0.0066  -0.0006 150 GLU C N   
3355 C CA  . GLU C 133 ? 0.0651 0.1204 0.0905 0.0102  0.0112  0.0136  150 GLU C CA  
3356 C C   . GLU C 133 ? 0.0581 0.1027 0.0883 -0.0088 0.0014  0.0047  150 GLU C C   
3357 O O   . GLU C 133 ? 0.1014 0.1155 0.0797 0.0028  0.0061  -0.0167 150 GLU C O   
3358 C CB  . GLU C 133 ? 0.0616 0.1421 0.1010 -0.0044 -0.0046 0.0109  150 GLU C CB  
3359 C CG  . GLU C 133 ? 0.1142 0.1216 0.1013 0.0183  0.0041  -0.0011 150 GLU C CG  
3360 C CD  . GLU C 133 ? 0.1484 0.1086 0.1077 -0.0115 -0.0011 -0.0102 150 GLU C CD  
3361 O OE1 . GLU C 133 ? 0.0881 0.2015 0.1172 -0.0035 0.0105  0.0152  150 GLU C OE1 
3362 O OE2 . GLU C 133 ? 0.1243 0.1493 0.1132 -0.0166 -0.0155 0.0075  150 GLU C OE2 
3363 N N   . ILE C 134 ? 0.1039 0.1053 0.0901 -0.0099 0.0080  0.0125  151 ILE C N   
3364 C CA  . ILE C 134 ? 0.0866 0.1151 0.0997 0.0069  -0.0066 0.0145  151 ILE C CA  
3365 C C   . ILE C 134 ? 0.0828 0.1090 0.1148 0.0020  -0.0152 0.0032  151 ILE C C   
3366 O O   . ILE C 134 ? 0.1333 0.1371 0.1167 -0.0193 -0.0214 -0.0161 151 ILE C O   
3367 C CB  . ILE C 134 ? 0.0912 0.1739 0.0949 0.0168  -0.0153 0.0264  151 ILE C CB  
3368 C CG1 . ILE C 134 ? 0.0763 0.1863 0.0952 0.0331  -0.0060 0.0187  151 ILE C CG1 
3369 C CG2 . ILE C 134 ? 0.0887 0.2019 0.0959 -0.0118 -0.0294 0.0342  151 ILE C CG2 
3370 C CD1 . ILE C 134 ? 0.1028 0.2079 0.1021 -0.0005 -0.0086 0.0210  151 ILE C CD1 
3371 N N   . SER C 135 ? 0.0846 0.1311 0.1312 -0.0117 0.0031  0.0145  152 SER C N   
3372 C CA  . SER C 135 ? 0.1106 0.1323 0.1409 -0.0212 0.0205  -0.0027 152 SER C CA  
3373 C C   . SER C 135 ? 0.0963 0.1569 0.1349 -0.0217 0.0019  -0.0148 152 SER C C   
3374 O O   . SER C 135 ? 0.1138 0.1377 0.1372 -0.0304 -0.0253 -0.0241 152 SER C O   
3375 C CB  . SER C 135 ? 0.1810 0.0934 0.1566 -0.0310 0.0133  -0.0253 152 SER C CB  
3376 O OG  . SER C 135 ? 0.1649 0.2507 0.1710 -0.0212 0.0172  -0.0354 152 SER C OG  
3377 N N   . LEU C 136 ? 0.0839 0.1640 0.1372 -0.0195 0.0213  -0.0250 153 LEU C N   
3378 C CA  . LEU C 136 ? 0.0757 0.1423 0.1381 -0.0391 0.0183  -0.0239 153 LEU C CA  
3379 C C   . LEU C 136 ? 0.0890 0.1602 0.1384 -0.0194 0.0231  -0.0266 153 LEU C C   
3380 O O   . LEU C 136 ? 0.1305 0.1387 0.1505 -0.0276 0.0291  -0.0195 153 LEU C O   
3381 C CB  . LEU C 136 ? 0.0922 0.1488 0.1358 0.0052  0.0329  -0.0050 153 LEU C CB  
3382 C CG  . LEU C 136 ? 0.1550 0.1210 0.1422 0.0193  0.0224  0.0060  153 LEU C CG  
3383 C CD1 . LEU C 136 ? 0.2096 0.2078 0.1469 -0.0067 0.0191  0.0034  153 LEU C CD1 
3384 C CD2 . LEU C 136 ? 0.1961 0.1204 0.1433 0.0323  0.0056  -0.0055 153 LEU C CD2 
3385 N N   . TRP C 137 ? 0.1051 0.1140 0.1336 -0.0309 0.0202  -0.0102 154 TRP C N   
3386 C CA  . TRP C 137 ? 0.1266 0.0937 0.1247 0.0199  0.0157  -0.0124 154 TRP C CA  
3387 C C   . TRP C 137 ? 0.1030 0.0831 0.1131 0.0263  0.0136  -0.0031 154 TRP C C   
3388 O O   . TRP C 137 ? 0.1332 0.1620 0.1101 0.0525  -0.0077 -0.0083 154 TRP C O   
3389 C CB  . TRP C 137 ? 0.1204 0.1133 0.1233 0.0058  0.0319  0.0136  154 TRP C CB  
3390 C CG  . TRP C 137 ? 0.0565 0.1153 0.1207 0.0173  0.0218  0.0137  154 TRP C CG  
3391 C CD1 . TRP C 137 ? 0.0871 0.1390 0.1182 0.0063  0.0068  -0.0026 154 TRP C CD1 
3392 C CD2 . TRP C 137 ? 0.0594 0.1085 0.1225 0.0170  0.0201  0.0101  154 TRP C CD2 
3393 N NE1 . TRP C 137 ? 0.0959 0.1036 0.1157 0.0109  0.0015  0.0028  154 TRP C NE1 
3394 C CE2 . TRP C 137 ? 0.1219 0.0762 0.1202 0.0233  0.0138  0.0048  154 TRP C CE2 
3395 C CE3 . TRP C 137 ? 0.1015 0.1132 0.1297 0.0249  0.0301  0.0310  154 TRP C CE3 
3396 C CZ2 . TRP C 137 ? 0.0923 0.1133 0.1232 0.0042  0.0128  0.0158  154 TRP C CZ2 
3397 C CZ3 . TRP C 137 ? 0.1450 0.1416 0.1316 0.0044  0.0211  0.0112  154 TRP C CZ3 
3398 C CH2 . TRP C 137 ? 0.1370 0.1471 0.1275 0.0695  0.0236  0.0174  154 TRP C CH2 
3399 N N   . PHE C 138 ? 0.0873 0.0883 0.1113 -0.0007 0.0129  0.0004  155 PHE C N   
3400 C CA  . PHE C 138 ? 0.0558 0.1133 0.1165 -0.0375 0.0129  -0.0096 155 PHE C CA  
3401 C C   . PHE C 138 ? 0.0747 0.1670 0.1264 -0.0210 0.0072  0.0109  155 PHE C C   
3402 O O   . PHE C 138 ? 0.0982 0.2230 0.1216 -0.0452 0.0177  -0.0149 155 PHE C O   
3403 C CB  . PHE C 138 ? 0.0774 0.1180 0.1097 -0.0114 -0.0068 -0.0167 155 PHE C CB  
3404 C CG  . PHE C 138 ? 0.0486 0.0971 0.1099 -0.0104 -0.0109 -0.0074 155 PHE C CG  
3405 C CD1 . PHE C 138 ? 0.0899 0.1521 0.1082 -0.0223 -0.0163 -0.0090 155 PHE C CD1 
3406 C CD2 . PHE C 138 ? 0.1062 0.1184 0.1107 0.0091  -0.0105 -0.0187 155 PHE C CD2 
3407 C CE1 . PHE C 138 ? 0.1022 0.1251 0.1085 0.0177  -0.0168 0.0092  155 PHE C CE1 
3408 C CE2 . PHE C 138 ? 0.0557 0.1681 0.1099 -0.0065 -0.0196 -0.0191 155 PHE C CE2 
3409 C CZ  . PHE C 138 ? 0.0914 0.1379 0.1085 0.0117  -0.0033 0.0046  155 PHE C CZ  
3410 N N   . LYS C 139 ? 0.0948 0.1383 0.1336 -0.0105 -0.0003 0.0142  156 LYS C N   
3411 C CA  . LYS C 139 ? 0.0796 0.1587 0.1506 -0.0157 -0.0070 0.0005  156 LYS C CA  
3412 C C   . LYS C 139 ? 0.0844 0.1165 0.1577 -0.0308 0.0008  0.0201  156 LYS C C   
3413 O O   . LYS C 139 ? 0.1197 0.1392 0.1492 -0.0097 -0.0138 0.0340  156 LYS C O   
3414 C CB  . LYS C 139 ? 0.1285 0.2435 0.1746 -0.0760 -0.0261 -0.0214 156 LYS C CB  
3415 C CG  . LYS C 139 ? 0.2921 0.3206 0.1922 -0.0440 -0.0274 -0.0305 156 LYS C CG  
3416 C CD  . LYS C 139 ? 0.4908 0.4570 0.2059 0.0910  -0.0255 -0.0334 156 LYS C CD  
3417 C CE  . LYS C 139 ? 0.6183 0.5601 0.2145 0.1998  -0.0180 -0.0100 156 LYS C CE  
3418 N NZ  . LYS C 139 ? 0.6855 0.6131 0.2173 0.2090  -0.0067 0.0059  156 LYS C NZ  
3419 N N   . PRO C 140 ? 0.1039 0.1646 0.1748 -0.0193 0.0192  0.0339  157 PRO C N   
3420 C CA  . PRO C 140 ? 0.0968 0.2075 0.1845 -0.0130 0.0180  0.0353  157 PRO C CA  
3421 C C   . PRO C 140 ? 0.0782 0.1511 0.1872 -0.0322 0.0083  0.0226  157 PRO C C   
3422 O O   . PRO C 140 ? 0.0980 0.1759 0.1903 -0.0015 -0.0088 0.0045  157 PRO C O   
3423 C CB  . PRO C 140 ? 0.1350 0.2892 0.1851 0.0477  0.0266  0.0401  157 PRO C CB  
3424 C CG  . PRO C 140 ? 0.1740 0.2679 0.1900 0.0213  0.0270  0.0463  157 PRO C CG  
3425 C CD  . PRO C 140 ? 0.1193 0.1665 0.1829 -0.0085 0.0206  0.0458  157 PRO C CD  
3426 N N   . GLU C 141 ? 0.0871 0.1690 0.1881 -0.0132 0.0109  0.0134  158 GLU C N   
3427 C CA  . GLU C 141 ? 0.1489 0.2371 0.1903 -0.0515 0.0021  0.0261  158 GLU C CA  
3428 C C   . GLU C 141 ? 0.1546 0.2273 0.1713 -0.0054 -0.0234 0.0203  158 GLU C C   
3429 O O   . GLU C 141 ? 0.1666 0.2862 0.1691 0.0094  -0.0514 0.0388  158 GLU C O   
3430 C CB  . GLU C 141 ? 0.1715 0.4239 0.2148 -0.0513 0.0217  0.0291  158 GLU C CB  
3431 C CG  . GLU C 141 ? 0.2711 0.5473 0.2364 -0.0145 0.0291  0.0313  158 GLU C CG  
3432 C CD  . GLU C 141 ? 0.2578 0.6624 0.2573 -0.0053 0.0240  0.0195  158 GLU C CD  
3433 O OE1 . GLU C 141 ? 0.1517 0.5474 0.2562 -0.0616 0.0095  0.0208  158 GLU C OE1 
3434 O OE2 . GLU C 141 ? 0.2429 0.7996 0.2749 -0.0072 0.0312  0.0183  158 GLU C OE2 
3435 N N   . GLU C 142 ? 0.1155 0.1664 0.1543 -0.0316 -0.0252 0.0371  159 GLU C N   
3436 C CA  . GLU C 142 ? 0.1187 0.2092 0.1373 0.0081  -0.0020 -0.0033 159 GLU C CA  
3437 C C   . GLU C 142 ? 0.0574 0.2116 0.1282 -0.0027 0.0135  0.0118  159 GLU C C   
3438 O O   . GLU C 142 ? 0.1015 0.1927 0.1197 0.0133  0.0203  0.0247  159 GLU C O   
3439 C CB  . GLU C 142 ? 0.0971 0.1732 0.1345 -0.0039 0.0100  -0.0028 159 GLU C CB  
3440 C CG  . GLU C 142 ? 0.1566 0.1621 0.1415 0.0083  -0.0008 -0.0278 159 GLU C CG  
3441 C CD  . GLU C 142 ? 0.2642 0.1599 0.1507 0.0117  0.0127  -0.0203 159 GLU C CD  
3442 O OE1 . GLU C 142 ? 0.1948 0.1872 0.1524 -0.0044 0.0123  -0.0191 159 GLU C OE1 
3443 O OE2 . GLU C 142 ? 0.4243 0.2961 0.1581 0.1759  0.0172  -0.0159 159 GLU C OE2 
3444 N N   . ILE C 143 ? 0.0819 0.1481 0.1281 0.0218  0.0191  0.0069  160 ILE C N   
3445 C CA  . ILE C 143 ? 0.0595 0.1034 0.1282 -0.0097 0.0019  0.0223  160 ILE C CA  
3446 C C   . ILE C 143 ? 0.0951 0.1311 0.1445 0.0175  0.0089  0.0497  160 ILE C C   
3447 O O   . ILE C 143 ? 0.0732 0.1979 0.1659 0.0063  -0.0006 0.0617  160 ILE C O   
3448 C CB  . ILE C 143 ? 0.0922 0.1416 0.1262 -0.0347 -0.0119 0.0288  160 ILE C CB  
3449 C CG1 . ILE C 143 ? 0.1327 0.1730 0.1367 -0.0335 -0.0212 0.0137  160 ILE C CG1 
3450 C CG2 . ILE C 143 ? 0.1624 0.1942 0.1250 -0.0198 -0.0222 0.0307  160 ILE C CG2 
3451 C CD1 . ILE C 143 ? 0.1363 0.2707 0.1360 -0.0215 -0.0173 0.0520  160 ILE C CD1 
3452 N N   . GLN C 144 ? 0.0382 0.1245 0.1283 0.0019  -0.0044 0.0191  161 GLN C N   
3453 C CA  . GLN C 144 ? 0.0943 0.1330 0.1409 -0.0116 -0.0004 0.0230  161 GLN C CA  
3454 C C   . GLN C 144 ? 0.1063 0.1097 0.1461 0.0124  -0.0153 0.0081  161 GLN C C   
3455 O O   . GLN C 144 ? 0.0974 0.1941 0.1602 0.0409  -0.0247 -0.0137 161 GLN C O   
3456 C CB  . GLN C 144 ? 0.0601 0.1390 0.1434 0.0081  0.0196  0.0216  161 GLN C CB  
3457 C CG  . GLN C 144 ? 0.0843 0.1924 0.1485 0.0178  0.0259  0.0110  161 GLN C CG  
3458 C CD  . GLN C 144 ? 0.1184 0.1577 0.1505 -0.0093 0.0163  -0.0122 161 GLN C CD  
3459 O OE1 . GLN C 144 ? 0.1167 0.1696 0.1494 0.0200  0.0000  -0.0325 161 GLN C OE1 
3460 N NE2 . GLN C 144 ? 0.0852 0.1973 0.1574 -0.0043 0.0312  -0.0156 161 GLN C NE2 
3461 N N   . SER C 145 ? 0.1234 0.1289 0.1392 0.0123  -0.0039 0.0070  162 SER C N   
3462 C CA  A SER C 145 ? 0.0960 0.1235 0.1424 -0.0365 -0.0007 -0.0127 162 SER C CA  
3463 C CA  B SER C 145 ? 0.1019 0.1505 0.1400 -0.0171 -0.0078 0.0023  162 SER C CA  
3464 C C   . SER C 145 ? 0.0958 0.1378 0.1395 -0.0162 -0.0051 0.0130  162 SER C C   
3465 O O   . SER C 145 ? 0.1434 0.1817 0.1351 0.0261  -0.0238 0.0005  162 SER C O   
3466 C CB  A SER C 145 ? 0.1302 0.1575 0.1513 0.0423  0.0127  -0.0301 162 SER C CB  
3467 C CB  B SER C 145 ? 0.1328 0.2035 0.1433 0.0330  -0.0113 0.0030  162 SER C CB  
3468 O OG  A SER C 145 ? 0.1330 0.1695 0.1562 0.0055  0.0240  -0.0456 162 SER C OG  
3469 O OG  B SER C 145 ? 0.1386 0.2175 0.1440 -0.0060 -0.0153 0.0062  162 SER C OG  
3470 N N   . TYR C 146 ? 0.0814 0.1431 0.1401 -0.0296 0.0159  0.0195  163 TYR C N   
3471 C CA  . TYR C 146 ? 0.0933 0.1563 0.1351 0.0158  0.0124  0.0086  163 TYR C CA  
3472 C C   . TYR C 146 ? 0.0793 0.1070 0.1446 0.0000  0.0161  0.0175  163 TYR C C   
3473 O O   . TYR C 146 ? 0.0827 0.1594 0.1382 0.0209  -0.0045 0.0363  163 TYR C O   
3474 C CB  . TYR C 146 ? 0.0999 0.1113 0.1302 0.0131  0.0128  0.0115  163 TYR C CB  
3475 C CG  . TYR C 146 ? 0.0957 0.1288 0.1218 -0.0176 0.0134  0.0101  163 TYR C CG  
3476 C CD1 . TYR C 146 ? 0.0581 0.1018 0.1174 -0.0252 0.0150  -0.0024 163 TYR C CD1 
3477 C CD2 . TYR C 146 ? 0.1615 0.0850 0.1225 0.0292  0.0039  0.0207  163 TYR C CD2 
3478 C CE1 . TYR C 146 ? 0.0483 0.1425 0.1111 0.0081  0.0055  -0.0021 163 TYR C CE1 
3479 C CE2 . TYR C 146 ? 0.1384 0.1134 0.1175 0.0171  0.0099  0.0351  163 TYR C CE2 
3480 C CZ  . TYR C 146 ? 0.0695 0.1003 0.1113 -0.0198 0.0085  0.0334  163 TYR C CZ  
3481 O OH  . TYR C 146 ? 0.0790 0.1100 0.1082 0.0152  0.0071  0.0120  163 TYR C OH  
3482 N N   . LYS C 147 ? 0.0927 0.1299 0.1566 0.0260  0.0196  -0.0019 164 LYS C N   
3483 C CA  . LYS C 147 ? 0.0893 0.1301 0.1674 0.0048  0.0248  -0.0081 164 LYS C CA  
3484 C C   . LYS C 147 ? 0.0828 0.1302 0.1516 0.0149  0.0091  -0.0266 164 LYS C C   
3485 O O   . LYS C 147 ? 0.0712 0.1654 0.1409 0.0151  0.0131  0.0016  164 LYS C O   
3486 C CB  . LYS C 147 ? 0.1951 0.1856 0.1970 0.0450  0.0238  -0.0151 164 LYS C CB  
3487 C CG  . LYS C 147 ? 0.2757 0.2688 0.2221 0.0813  0.0182  -0.0197 164 LYS C CG  
3488 C CD  . LYS C 147 ? 0.4272 0.4564 0.2442 0.2046  0.0210  -0.0294 164 LYS C CD  
3489 C CE  . LYS C 147 ? 0.5552 0.6163 0.2556 0.2914  0.0262  -0.0424 164 LYS C CE  
3490 N NZ  . LYS C 147 ? 0.6356 0.7459 0.2702 0.3139  0.0281  -0.0346 164 LYS C NZ  
3491 N N   . LEU C 148 ? 0.0999 0.1515 0.1453 -0.0132 0.0001  -0.0192 165 LEU C N   
3492 C CA  . LEU C 148 ? 0.0477 0.1537 0.1434 -0.0158 -0.0054 -0.0229 165 LEU C CA  
3493 C C   . LEU C 148 ? 0.0725 0.1570 0.1388 0.0186  -0.0003 -0.0077 165 LEU C C   
3494 O O   . LEU C 148 ? 0.1270 0.1301 0.1325 0.0120  0.0128  0.0052  165 LEU C O   
3495 C CB  . LEU C 148 ? 0.1138 0.1207 0.1492 -0.0472 -0.0108 -0.0024 165 LEU C CB  
3496 C CG  . LEU C 148 ? 0.1676 0.1825 0.1535 -0.0095 -0.0012 0.0356  165 LEU C CG  
3497 C CD1 . LEU C 148 ? 0.1465 0.2027 0.1517 0.0376  0.0133  0.0327  165 LEU C CD1 
3498 C CD2 . LEU C 148 ? 0.1629 0.1252 0.1619 -0.0196 -0.0019 0.0235  165 LEU C CD2 
3499 N N   . ALA C 149 ? 0.1564 0.1293 0.1380 0.0032  0.0064  -0.0196 166 ALA C N   
3500 C CA  . ALA C 149 ? 0.1914 0.1892 0.1389 0.0370  0.0001  0.0008  166 ALA C CA  
3501 C C   . ALA C 149 ? 0.1978 0.1713 0.1483 0.0455  -0.0015 0.0003  166 ALA C C   
3502 O O   . ALA C 149 ? 0.1407 0.1614 0.1656 0.0268  -0.0407 0.0167  166 ALA C O   
3503 C CB  . ALA C 149 ? 0.2913 0.2065 0.1393 -0.0094 -0.0108 -0.0001 166 ALA C CB  
3504 N N   . LEU C 150 ? 0.1243 0.1260 0.1454 -0.0086 0.0011  -0.0045 167 LEU C N   
3505 C CA  . LEU C 150 ? 0.1232 0.0983 0.1501 0.0383  0.0041  0.0001  167 LEU C CA  
3506 C C   . LEU C 150 ? 0.0646 0.1274 0.1437 -0.0142 -0.0102 -0.0129 167 LEU C C   
3507 O O   . LEU C 150 ? 0.1129 0.1084 0.1358 -0.0027 0.0059  -0.0086 167 LEU C O   
3508 C CB  . LEU C 150 ? 0.1809 0.2415 0.1587 0.0795  0.0304  -0.0297 167 LEU C CB  
3509 C CG  . LEU C 150 ? 0.1731 0.2548 0.1716 0.0557  0.0334  -0.0386 167 LEU C CG  
3510 C CD1 . LEU C 150 ? 0.1387 0.3967 0.1777 0.0199  0.0166  -0.0568 167 LEU C CD1 
3511 C CD2 . LEU C 150 ? 0.2627 0.2695 0.1838 0.0897  0.0274  0.0078  167 LEU C CD2 
3512 N N   . SER C 151 ? 0.0969 0.1448 0.1533 0.0162  -0.0183 -0.0056 168 SER C N   
3513 C CA  A SER C 151 ? 0.1282 0.1585 0.1573 0.0341  -0.0093 -0.0237 168 SER C CA  
3514 C CA  B SER C 151 ? 0.1152 0.1361 0.1600 0.0034  -0.0074 -0.0153 168 SER C CA  
3515 C C   . SER C 151 ? 0.1100 0.1711 0.1646 0.0569  -0.0104 -0.0216 168 SER C C   
3516 O O   . SER C 151 ? 0.1221 0.1485 0.1624 -0.0026 0.0086  -0.0279 168 SER C O   
3517 C CB  A SER C 151 ? 0.1661 0.1960 0.1566 0.0446  -0.0016 -0.0473 168 SER C CB  
3518 C CB  B SER C 151 ? 0.1409 0.1582 0.1653 -0.0013 0.0031  -0.0276 168 SER C CB  
3519 O OG  A SER C 151 ? 0.2017 0.2436 0.1576 0.0439  0.0011  -0.0496 168 SER C OG  
3520 O OG  B SER C 151 ? 0.1857 0.2011 0.1723 0.0277  0.0100  -0.0103 168 SER C OG  
3521 N N   . ASP C 152 ? 0.0908 0.1550 0.1801 0.0357  0.0004  -0.0312 169 ASP C N   
3522 C CA  . ASP C 152 ? 0.0936 0.1944 0.1903 0.0356  0.0046  -0.0214 169 ASP C CA  
3523 C C   . ASP C 152 ? 0.1153 0.1291 0.1777 0.0498  0.0004  -0.0175 169 ASP C C   
3524 O O   . ASP C 152 ? 0.1158 0.1363 0.1881 0.0292  -0.0038 -0.0338 169 ASP C O   
3525 C CB  . ASP C 152 ? 0.1101 0.2590 0.2184 0.0370  -0.0176 -0.0292 169 ASP C CB  
3526 C CG  . ASP C 152 ? 0.3083 0.4529 0.2427 0.1115  -0.0123 -0.0135 169 ASP C CG  
3527 O OD1 . ASP C 152 ? 0.3933 0.4940 0.2480 0.2016  0.0060  -0.0045 169 ASP C OD1 
3528 O OD2 . ASP C 152 ? 0.3638 0.5341 0.2633 0.1510  -0.0181 0.0019  169 ASP C OD2 
3529 N N   . TYR C 153 ? 0.1365 0.1003 0.1592 0.0631  0.0062  0.0097  170 TYR C N   
3530 C CA  . TYR C 153 ? 0.1407 0.0654 0.1483 0.0256  0.0105  0.0156  170 TYR C CA  
3531 C C   . TYR C 153 ? 0.0994 0.0958 0.1524 0.0244  0.0039  0.0197  170 TYR C C   
3532 O O   . TYR C 153 ? 0.1423 0.1469 0.1524 0.0164  -0.0094 0.0394  170 TYR C O   
3533 C CB  . TYR C 153 ? 0.1030 0.1233 0.1487 -0.0188 0.0333  0.0309  170 TYR C CB  
3534 C CG  . TYR C 153 ? 0.0837 0.1364 0.1478 0.0013  0.0150  0.0125  170 TYR C CG  
3535 C CD1 . TYR C 153 ? 0.0696 0.1819 0.1506 0.0306  0.0272  0.0263  170 TYR C CD1 
3536 C CD2 . TYR C 153 ? 0.0992 0.1680 0.1471 0.0325  0.0100  0.0204  170 TYR C CD2 
3537 C CE1 . TYR C 153 ? 0.1601 0.1249 0.1502 0.0449  0.0297  0.0386  170 TYR C CE1 
3538 C CE2 . TYR C 153 ? 0.1281 0.2177 0.1526 0.0638  0.0152  0.0348  170 TYR C CE2 
3539 C CZ  . TYR C 153 ? 0.1441 0.1311 0.1577 0.0577  0.0233  0.0577  170 TYR C CZ  
3540 O OH  . TYR C 153 ? 0.1966 0.2116 0.1681 0.0531  0.0188  0.0659  170 TYR C OH  
3541 N N   . ILE C 154 ? 0.1303 0.1144 0.1561 0.0063  -0.0026 0.0203  171 ILE C N   
3542 C CA  . ILE C 154 ? 0.1548 0.1596 0.1496 0.0448  0.0097  0.0259  171 ILE C CA  
3543 C C   . ILE C 154 ? 0.2066 0.1469 0.1521 0.0519  0.0076  0.0140  171 ILE C C   
3544 O O   . ILE C 154 ? 0.1317 0.2431 0.1518 -0.0063 0.0051  0.0184  171 ILE C O   
3545 C CB  . ILE C 154 ? 0.1902 0.1292 0.1492 0.0458  0.0062  -0.0088 171 ILE C CB  
3546 C CG1 . ILE C 154 ? 0.1767 0.1571 0.1507 0.0295  0.0100  -0.0205 171 ILE C CG1 
3547 C CG2 . ILE C 154 ? 0.2314 0.2113 0.1511 0.1043  0.0121  -0.0345 171 ILE C CG2 
3548 C CD1 . ILE C 154 ? 0.2447 0.1878 0.1498 0.0559  0.0094  0.0225  171 ILE C CD1 
3549 N N   . PHE C 155 ? 0.1995 0.1313 0.1590 0.0356  0.0173  -0.0051 172 PHE C N   
3550 C CA  . PHE C 155 ? 0.1991 0.1248 0.1737 0.0110  0.0257  0.0036  172 PHE C CA  
3551 C C   . PHE C 155 ? 0.3001 0.1278 0.2020 0.0155  0.0421  -0.0097 172 PHE C C   
3552 O O   . PHE C 155 ? 0.3466 0.1925 0.2085 0.0820  0.0426  -0.0112 172 PHE C O   
3553 C CB  . PHE C 155 ? 0.1506 0.1687 0.1706 -0.0025 0.0249  0.0230  172 PHE C CB  
3554 C CG  . PHE C 155 ? 0.1735 0.1013 0.1712 0.0048  0.0077  0.0298  172 PHE C CG  
3555 C CD1 . PHE C 155 ? 0.1458 0.1347 0.1714 0.0301  -0.0078 0.0275  172 PHE C CD1 
3556 C CD2 . PHE C 155 ? 0.1762 0.1708 0.1783 -0.0205 -0.0145 0.0291  172 PHE C CD2 
3557 C CE1 . PHE C 155 ? 0.1512 0.1826 0.1746 0.0201  -0.0094 0.0271  172 PHE C CE1 
3558 C CE2 . PHE C 155 ? 0.2380 0.1744 0.1789 0.0006  -0.0199 0.0197  172 PHE C CE2 
3559 C CZ  . PHE C 155 ? 0.1884 0.1597 0.1753 -0.0066 -0.0146 0.0249  172 PHE C CZ  
3560 N N   . GLU C 156 ? 0.3834 0.1947 0.2254 0.0521  0.0494  -0.0535 173 GLU C N   
3561 C CA  . GLU C 156 ? 0.5178 0.3370 0.2553 0.0777  0.0401  -0.1016 173 GLU C CA  
3562 C C   . GLU C 156 ? 0.6169 0.4644 0.2758 0.1696  0.0492  -0.1121 173 GLU C C   
3563 O O   . GLU C 156 ? 0.6479 0.4983 0.2921 0.2039  0.0612  -0.1044 173 GLU C O   
3564 C CB  . GLU C 156 ? 0.5543 0.3723 0.2625 0.0797  0.0367  -0.1409 173 GLU C CB  
3565 C CG  . GLU C 156 ? 0.5699 0.5181 0.2672 0.0934  0.0612  -0.1276 173 GLU C CG  
3566 C CD  . GLU C 156 ? 0.4856 0.5619 0.2600 0.0365  0.1042  -0.1204 173 GLU C CD  
3567 O OE1 . GLU C 156 ? 0.5289 0.6461 0.2674 0.0909  0.1118  -0.1143 173 GLU C OE1 
3568 O OE2 . GLU C 156 ? 0.2866 0.4603 0.2610 -0.0867 0.1248  -0.1145 173 GLU C OE2 
3569 O OXT . GLU C 156 ? 0.6406 0.4670 0.2834 0.1453  0.0370  -0.1235 173 GLU C OXT 
3570 S S   . SO4 D .   ? 0.1695 0.1776 0.1871 0.0131  -0.0088 0.0043  201 SO4 A S   
3571 O O1  . SO4 D .   ? 0.2012 0.3283 0.2040 0.0423  -0.0183 0.0145  201 SO4 A O1  
3572 O O2  . SO4 D .   ? 0.2862 0.2066 0.1922 0.0557  -0.0778 0.0046  201 SO4 A O2  
3573 O O3  . SO4 D .   ? 0.3289 0.2295 0.1981 0.0851  -0.0662 -0.0287 201 SO4 A O3  
3574 O O4  . SO4 D .   ? 0.3709 0.3392 0.1896 0.0891  0.0376  0.0221  201 SO4 A O4  
3575 S S   . SO4 E .   ? 0.4340 0.2762 0.2027 0.0014  0.0487  -0.0018 202 SO4 A S   
3576 O O1  . SO4 E .   ? 0.4005 0.2857 0.2182 -0.0111 0.0644  -0.0298 202 SO4 A O1  
3577 O O2  . SO4 E .   ? 0.5610 0.3514 0.2063 0.0790  0.0254  0.0355  202 SO4 A O2  
3578 O O3  . SO4 E .   ? 0.3889 0.2216 0.2037 -0.0039 0.0578  -0.0195 202 SO4 A O3  
3579 O O4  . SO4 E .   ? 0.3610 0.3135 0.1936 -0.0865 0.0534  -0.0098 202 SO4 A O4  
3580 S S   . SO4 F .   ? 0.7937 0.4821 0.4295 -0.2903 0.1301  -0.1653 203 SO4 A S   
3581 O O1  . SO4 F .   ? 0.8763 0.5748 0.4292 -0.2227 0.1350  -0.1804 203 SO4 A O1  
3582 O O2  . SO4 F .   ? 0.8155 0.4742 0.4304 -0.2552 0.1531  -0.1493 203 SO4 A O2  
3583 O O3  . SO4 F .   ? 0.5978 0.3645 0.4171 -0.2148 0.1121  -0.1514 203 SO4 A O3  
3584 O O4  . SO4 F .   ? 0.8303 0.4881 0.4339 -0.2747 0.1170  -0.1742 203 SO4 A O4  
3585 S S   . SO4 G .   ? 0.2187 0.1694 0.2003 -0.0365 0.0113  -0.0220 201 SO4 B S   
3586 O O1  . SO4 G .   ? 0.3651 0.2882 0.2091 -0.0643 0.0535  -0.0836 201 SO4 B O1  
3587 O O2  . SO4 G .   ? 0.2764 0.2747 0.2093 -0.0377 0.0008  -0.0741 201 SO4 B O2  
3588 O O3  . SO4 G .   ? 0.3851 0.3062 0.1950 -0.0194 0.0013  0.0055  201 SO4 B O3  
3589 O O4  . SO4 G .   ? 0.2889 0.2519 0.2145 0.1120  -0.0201 -0.0659 201 SO4 B O4  
3590 S S   . SO4 H .   ? 0.5179 0.5511 0.6556 0.0783  0.0029  0.1952  202 SO4 B S   
3591 O O1  . SO4 H .   ? 0.5778 0.5865 0.6524 0.1822  -0.0095 0.1991  202 SO4 B O1  
3592 O O2  . SO4 H .   ? 0.5419 0.5982 0.6573 0.0198  0.0187  0.1830  202 SO4 B O2  
3593 O O3  . SO4 H .   ? 0.4482 0.4322 0.6525 0.0237  0.0027  0.2099  202 SO4 B O3  
3594 O O4  . SO4 H .   ? 0.5791 0.5356 0.6604 0.0598  0.0147  0.1919  202 SO4 B O4  
3595 S S   . SO4 I .   ? 0.8006 0.7914 0.6394 0.2478  -0.2528 0.0110  203 SO4 B S   
3596 O O1  . SO4 I .   ? 0.8211 0.8228 0.6377 0.2423  -0.2357 0.0127  203 SO4 B O1  
3597 O O2  . SO4 I .   ? 0.7785 0.7519 0.6387 0.2227  -0.2600 0.0007  203 SO4 B O2  
3598 O O3  . SO4 I .   ? 0.7807 0.7961 0.6405 0.1830  -0.2500 0.0082  203 SO4 B O3  
3599 O O4  . SO4 I .   ? 0.8132 0.8133 0.6383 0.2918  -0.2602 0.0229  203 SO4 B O4  
3600 S S   . SO4 J .   ? 0.4321 0.9738 0.4692 -0.0306 -0.0093 0.2152  204 SO4 B S   
3601 O O1  . SO4 J .   ? 0.4867 1.0469 0.4715 0.0243  -0.0180 0.2242  204 SO4 B O1  
3602 O O2  . SO4 J .   ? 0.5271 1.0894 0.4755 0.1035  0.0026  0.2211  204 SO4 B O2  
3603 O O3  . SO4 J .   ? 0.3850 0.9379 0.4686 -0.1158 -0.0317 0.2184  204 SO4 B O3  
3604 O O4  . SO4 J .   ? 0.3288 0.6109 0.4554 -0.1939 -0.0111 0.1876  204 SO4 B O4  
3605 S S   . SO4 K .   ? 0.1703 0.2509 0.2186 -0.0295 0.0110  0.0453  201 SO4 C S   
3606 O O1  . SO4 K .   ? 0.2621 0.2095 0.2286 -0.0796 0.0480  0.0456  201 SO4 C O1  
3607 O O2  . SO4 K .   ? 0.1712 0.4366 0.2293 0.0703  0.0588  0.0952  201 SO4 C O2  
3608 O O3  . SO4 K .   ? 0.2516 0.3770 0.2222 -0.0301 -0.0089 -0.0179 201 SO4 C O3  
3609 O O4  . SO4 K .   ? 0.2373 0.3781 0.2220 0.0368  0.0870  0.0859  201 SO4 C O4  
3610 S S   . SO4 L .   ? 0.9342 0.5799 0.7929 -0.1715 -0.2388 -0.1624 202 SO4 C S   
3611 O O1  . SO4 L .   ? 0.9354 0.4932 0.7932 -0.1883 -0.2316 -0.1552 202 SO4 C O1  
3612 O O2  . SO4 L .   ? 0.9506 0.6494 0.7944 -0.1108 -0.2336 -0.1456 202 SO4 C O2  
3613 O O3  . SO4 L .   ? 0.9405 0.5886 0.7907 -0.2091 -0.2494 -0.1789 202 SO4 C O3  
3614 O O4  . SO4 L .   ? 0.9297 0.6443 0.7917 -0.1513 -0.2373 -0.1608 202 SO4 C O4  
3615 S S   . SO4 M .   ? 0.5767 0.1992 0.2874 -0.0807 0.1312  0.0183  203 SO4 C S   
3616 O O1  . SO4 M .   ? 0.6079 0.1815 0.2903 -0.0786 0.1087  -0.0033 203 SO4 C O1  
3617 O O2  . SO4 M .   ? 0.5689 0.1610 0.2816 -0.0270 0.1197  -0.0270 203 SO4 C O2  
3618 O O3  . SO4 M .   ? 0.6275 0.2572 0.2945 -0.1466 0.1293  -0.0134 203 SO4 C O3  
3619 O O4  . SO4 M .   ? 0.6548 0.3403 0.2903 -0.0445 0.1214  0.0131  203 SO4 C O4  
3620 S S   . SO4 N .   ? 0.5433 0.5895 0.5407 0.2620  -0.2040 -0.0720 204 SO4 C S   
3621 O O1  . SO4 N .   ? 0.6120 0.6507 0.5409 0.2732  -0.2013 -0.0800 204 SO4 C O1  
3622 O O2  . SO4 N .   ? 0.3464 0.2876 0.5185 0.1246  -0.1820 -0.0563 204 SO4 C O2  
3623 O O3  . SO4 N .   ? 0.5435 0.6204 0.5417 0.2363  -0.2088 -0.0898 204 SO4 C O3  
3624 O O4  . SO4 N .   ? 0.6490 0.6386 0.5447 0.3446  -0.1935 -0.0669 204 SO4 C O4  
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