data_9MTO
# 
_entry.id   9MTO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9MTO         pdb_00009mto 10.2210/pdb9mto/pdb 
WWPDB D_1000291809 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_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                        9MTO 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-11 
_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 
# 
_pdbx_database_related.db_name        TargetTrack 
_pdbx_database_related.db_id          IDP96809 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexei.savchenko@ucalgary.ca 
_pdbx_contact_author.name_first         Alexei 
_pdbx_contact_author.name_last          Savchenko 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5256-9237 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Stogios, P.J.'                                                1 ? 
'Evdokimova, E.'                                               2 ? 
'Chang, C.'                                                    3 ? 
'Di Leo, R.'                                                   4 ? 
'Savchenko, A.'                                                5 ? 
'Joachimiak, A.'                                               6 ? 
'Satchell, K.J.F.'                                             7 ? 
'Center for Structural Biology of Infectious Diseases (CSBID)' 8 ? 
# 
_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 acetyltransferase CBU0801 from Coxiella burnetii' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Stogios, P.J.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   ? 
# 
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 '[Ribosomal protein bS18]-alanine N-acetyltransferase' 17163.795 2   2.3.1.266 ? ? ? 
2 non-polymer syn 'COENZYME A'                                           767.534   2   ?         ? ? ? 
3 water       nat water                                                  18.015    199 ?         ? ? ? 
# 
_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       
;QSMKIRNWIKDDVPQVSEIAEAAMPFPWSEKFFYDCLKSNYYGWVMESDHHLVGFIVILMQEKECQLMNIAVAPRYQRKG
VASQLLQHALHYAKTHHATRLLLEVRKSNRSAIEFYKKAGGVEIGVRKNYYPAEKGREDALVFNLNF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;QSMKIRNWIKDDVPQVSEIAEAAMPFPWSEKFFYDCLKSNYYGWVMESDHHLVGFIVILMQEKECQLMNIAVAPRYQRKG
VASQLLQHALHYAKTHHATRLLLEVRKSNRSAIEFYKKAGGVEIGVRKNYYPAEKGREDALVFNLNF
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         IDP96809 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COENZYME A' COA 
3 water        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   SER n 
1 3   MET n 
1 4   LYS n 
1 5   ILE n 
1 6   ARG n 
1 7   ASN n 
1 8   TRP n 
1 9   ILE n 
1 10  LYS n 
1 11  ASP n 
1 12  ASP n 
1 13  VAL n 
1 14  PRO n 
1 15  GLN n 
1 16  VAL n 
1 17  SER n 
1 18  GLU n 
1 19  ILE n 
1 20  ALA n 
1 21  GLU n 
1 22  ALA n 
1 23  ALA n 
1 24  MET n 
1 25  PRO n 
1 26  PHE n 
1 27  PRO n 
1 28  TRP n 
1 29  SER n 
1 30  GLU n 
1 31  LYS n 
1 32  PHE n 
1 33  PHE n 
1 34  TYR n 
1 35  ASP n 
1 36  CYS n 
1 37  LEU n 
1 38  LYS n 
1 39  SER n 
1 40  ASN n 
1 41  TYR n 
1 42  TYR n 
1 43  GLY n 
1 44  TRP n 
1 45  VAL n 
1 46  MET n 
1 47  GLU n 
1 48  SER n 
1 49  ASP n 
1 50  HIS n 
1 51  HIS n 
1 52  LEU n 
1 53  VAL n 
1 54  GLY n 
1 55  PHE n 
1 56  ILE n 
1 57  VAL n 
1 58  ILE n 
1 59  LEU n 
1 60  MET n 
1 61  GLN n 
1 62  GLU n 
1 63  LYS n 
1 64  GLU n 
1 65  CYS n 
1 66  GLN n 
1 67  LEU n 
1 68  MET n 
1 69  ASN n 
1 70  ILE n 
1 71  ALA n 
1 72  VAL n 
1 73  ALA n 
1 74  PRO n 
1 75  ARG n 
1 76  TYR n 
1 77  GLN n 
1 78  ARG n 
1 79  LYS n 
1 80  GLY n 
1 81  VAL n 
1 82  ALA n 
1 83  SER n 
1 84  GLN n 
1 85  LEU n 
1 86  LEU n 
1 87  GLN n 
1 88  HIS n 
1 89  ALA n 
1 90  LEU n 
1 91  HIS n 
1 92  TYR n 
1 93  ALA n 
1 94  LYS n 
1 95  THR n 
1 96  HIS n 
1 97  HIS n 
1 98  ALA n 
1 99  THR n 
1 100 ARG n 
1 101 LEU n 
1 102 LEU n 
1 103 LEU n 
1 104 GLU n 
1 105 VAL n 
1 106 ARG n 
1 107 LYS n 
1 108 SER n 
1 109 ASN n 
1 110 ARG n 
1 111 SER n 
1 112 ALA n 
1 113 ILE n 
1 114 GLU n 
1 115 PHE n 
1 116 TYR n 
1 117 LYS n 
1 118 LYS n 
1 119 ALA n 
1 120 GLY n 
1 121 GLY n 
1 122 VAL n 
1 123 GLU n 
1 124 ILE n 
1 125 GLY n 
1 126 VAL n 
1 127 ARG n 
1 128 LYS n 
1 129 ASN n 
1 130 TYR n 
1 131 TYR n 
1 132 PRO n 
1 133 ALA n 
1 134 GLU n 
1 135 LYS n 
1 136 GLY n 
1 137 ARG n 
1 138 GLU n 
1 139 ASP n 
1 140 ALA n 
1 141 LEU n 
1 142 VAL n 
1 143 PHE n 
1 144 ASN n 
1 145 LEU n 
1 146 ASN n 
1 147 PHE 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                   147 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rimI, CBU_0801' 
_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      'Coxiella burnetii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     777 
_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              -Gold 
_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                       pMCSG53 
_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 
COA non-polymer         . 'COENZYME A'    ? 'C21 H36 N7 O16 P3 S' 767.534 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'        121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER           ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLN 1   -1  -1  GLN GLN A . n 
A 1 2   SER 2   0   0   SER SER A . n 
A 1 3   MET 3   1   1   MET MET A . n 
A 1 4   LYS 4   2   2   LYS LYS A . n 
A 1 5   ILE 5   3   3   ILE ILE A . n 
A 1 6   ARG 6   4   4   ARG ARG A . n 
A 1 7   ASN 7   5   5   ASN ASN A . n 
A 1 8   TRP 8   6   6   TRP TRP A . n 
A 1 9   ILE 9   7   7   ILE ILE A . n 
A 1 10  LYS 10  8   8   LYS LYS A . n 
A 1 11  ASP 11  9   9   ASP ASP A . n 
A 1 12  ASP 12  10  10  ASP ASP A . n 
A 1 13  VAL 13  11  11  VAL VAL A . n 
A 1 14  PRO 14  12  12  PRO PRO A . n 
A 1 15  GLN 15  13  13  GLN GLN A . n 
A 1 16  VAL 16  14  14  VAL VAL A . n 
A 1 17  SER 17  15  15  SER SER A . n 
A 1 18  GLU 18  16  16  GLU GLU A . n 
A 1 19  ILE 19  17  17  ILE ILE A . n 
A 1 20  ALA 20  18  18  ALA ALA A . n 
A 1 21  GLU 21  19  19  GLU GLU A . n 
A 1 22  ALA 22  20  20  ALA ALA A . n 
A 1 23  ALA 23  21  21  ALA ALA A . n 
A 1 24  MET 24  22  22  MET MET A . n 
A 1 25  PRO 25  23  23  PRO PRO A . n 
A 1 26  PHE 26  24  24  PHE PHE A . n 
A 1 27  PRO 27  25  25  PRO PRO A . n 
A 1 28  TRP 28  26  26  TRP TRP A . n 
A 1 29  SER 29  27  27  SER SER A . n 
A 1 30  GLU 30  28  28  GLU GLU A . n 
A 1 31  LYS 31  29  29  LYS LYS A . n 
A 1 32  PHE 32  30  30  PHE PHE A . n 
A 1 33  PHE 33  31  31  PHE PHE A . n 
A 1 34  TYR 34  32  32  TYR TYR A . n 
A 1 35  ASP 35  33  33  ASP ASP A . n 
A 1 36  CYS 36  34  34  CYS CYS A . n 
A 1 37  LEU 37  35  35  LEU LEU A . n 
A 1 38  LYS 38  36  36  LYS LYS A . n 
A 1 39  SER 39  37  37  SER SER A . n 
A 1 40  ASN 40  38  38  ASN ASN A . n 
A 1 41  TYR 41  39  39  TYR TYR A . n 
A 1 42  TYR 42  40  40  TYR TYR A . n 
A 1 43  GLY 43  41  41  GLY GLY A . n 
A 1 44  TRP 44  42  42  TRP TRP A . n 
A 1 45  VAL 45  43  43  VAL VAL A . n 
A 1 46  MET 46  44  44  MET MET A . n 
A 1 47  GLU 47  45  45  GLU GLU A . n 
A 1 48  SER 48  46  46  SER SER A . n 
A 1 49  ASP 49  47  47  ASP ASP A . n 
A 1 50  HIS 50  48  48  HIS HIS A . n 
A 1 51  HIS 51  49  49  HIS HIS A . n 
A 1 52  LEU 52  50  50  LEU LEU A . n 
A 1 53  VAL 53  51  51  VAL VAL A . n 
A 1 54  GLY 54  52  52  GLY GLY A . n 
A 1 55  PHE 55  53  53  PHE PHE A . n 
A 1 56  ILE 56  54  54  ILE ILE A . n 
A 1 57  VAL 57  55  55  VAL VAL A . n 
A 1 58  ILE 58  56  56  ILE ILE A . n 
A 1 59  LEU 59  57  57  LEU LEU A . n 
A 1 60  MET 60  58  58  MET MET A . n 
A 1 61  GLN 61  59  59  GLN GLN A . n 
A 1 62  GLU 62  60  60  GLU GLU A . n 
A 1 63  LYS 63  61  61  LYS LYS A . n 
A 1 64  GLU 64  62  62  GLU GLU A . n 
A 1 65  CYS 65  63  63  CYS CYS A . n 
A 1 66  GLN 66  64  64  GLN GLN A . n 
A 1 67  LEU 67  65  65  LEU LEU A . n 
A 1 68  MET 68  66  66  MET MET A . n 
A 1 69  ASN 69  67  67  ASN ASN A . n 
A 1 70  ILE 70  68  68  ILE ILE A . n 
A 1 71  ALA 71  69  69  ALA ALA A . n 
A 1 72  VAL 72  70  70  VAL VAL A . n 
A 1 73  ALA 73  71  71  ALA ALA A . n 
A 1 74  PRO 74  72  72  PRO PRO A . n 
A 1 75  ARG 75  73  73  ARG ARG A . n 
A 1 76  TYR 76  74  74  TYR TYR A . n 
A 1 77  GLN 77  75  75  GLN GLN A . n 
A 1 78  ARG 78  76  76  ARG ARG A . n 
A 1 79  LYS 79  77  77  LYS LYS A . n 
A 1 80  GLY 80  78  78  GLY GLY A . n 
A 1 81  VAL 81  79  79  VAL VAL A . n 
A 1 82  ALA 82  80  80  ALA ALA A . n 
A 1 83  SER 83  81  81  SER SER A . n 
A 1 84  GLN 84  82  82  GLN GLN A . n 
A 1 85  LEU 85  83  83  LEU LEU A . n 
A 1 86  LEU 86  84  84  LEU LEU A . n 
A 1 87  GLN 87  85  85  GLN GLN A . n 
A 1 88  HIS 88  86  86  HIS HIS A . n 
A 1 89  ALA 89  87  87  ALA ALA A . n 
A 1 90  LEU 90  88  88  LEU LEU A . n 
A 1 91  HIS 91  89  89  HIS HIS A . n 
A 1 92  TYR 92  90  90  TYR TYR A . n 
A 1 93  ALA 93  91  91  ALA ALA A . n 
A 1 94  LYS 94  92  92  LYS LYS A . n 
A 1 95  THR 95  93  93  THR THR A . n 
A 1 96  HIS 96  94  94  HIS HIS A . n 
A 1 97  HIS 97  95  95  HIS HIS A . n 
A 1 98  ALA 98  96  96  ALA ALA A . n 
A 1 99  THR 99  97  97  THR THR A . n 
A 1 100 ARG 100 98  98  ARG ARG A . n 
A 1 101 LEU 101 99  99  LEU LEU A . n 
A 1 102 LEU 102 100 100 LEU LEU A . n 
A 1 103 LEU 103 101 101 LEU LEU A . n 
A 1 104 GLU 104 102 102 GLU GLU A . n 
A 1 105 VAL 105 103 103 VAL VAL A . n 
A 1 106 ARG 106 104 104 ARG ARG A . n 
A 1 107 LYS 107 105 105 LYS LYS A . n 
A 1 108 SER 108 106 106 SER SER A . n 
A 1 109 ASN 109 107 107 ASN ASN A . n 
A 1 110 ARG 110 108 108 ARG ARG A . n 
A 1 111 SER 111 109 109 SER SER A . n 
A 1 112 ALA 112 110 110 ALA ALA A . n 
A 1 113 ILE 113 111 111 ILE ILE A . n 
A 1 114 GLU 114 112 112 GLU GLU A . n 
A 1 115 PHE 115 113 113 PHE PHE A . n 
A 1 116 TYR 116 114 114 TYR TYR A . n 
A 1 117 LYS 117 115 115 LYS LYS A . n 
A 1 118 LYS 118 116 116 LYS LYS A . n 
A 1 119 ALA 119 117 117 ALA ALA A . n 
A 1 120 GLY 120 118 118 GLY GLY A . n 
A 1 121 GLY 121 119 119 GLY GLY A . n 
A 1 122 VAL 122 120 120 VAL VAL A . n 
A 1 123 GLU 123 121 121 GLU GLU A . n 
A 1 124 ILE 124 122 122 ILE ILE A . n 
A 1 125 GLY 125 123 123 GLY GLY A . n 
A 1 126 VAL 126 124 124 VAL VAL A . n 
A 1 127 ARG 127 125 125 ARG ARG A . n 
A 1 128 LYS 128 126 126 LYS LYS A . n 
A 1 129 ASN 129 127 127 ASN ASN A . n 
A 1 130 TYR 130 128 128 TYR TYR A . n 
A 1 131 TYR 131 129 129 TYR TYR A . n 
A 1 132 PRO 132 130 130 PRO PRO A . n 
A 1 133 ALA 133 131 131 ALA ALA A . n 
A 1 134 GLU 134 132 132 GLU GLU A . n 
A 1 135 LYS 135 133 133 LYS LYS A . n 
A 1 136 GLY 136 134 134 GLY GLY A . n 
A 1 137 ARG 137 135 135 ARG ARG A . n 
A 1 138 GLU 138 136 136 GLU GLU A . n 
A 1 139 ASP 139 137 137 ASP ASP A . n 
A 1 140 ALA 140 138 138 ALA ALA A . n 
A 1 141 LEU 141 139 139 LEU LEU A . n 
A 1 142 VAL 142 140 140 VAL VAL A . n 
A 1 143 PHE 143 141 141 PHE PHE A . n 
A 1 144 ASN 144 142 142 ASN ASN A . n 
A 1 145 LEU 145 143 143 LEU LEU A . n 
A 1 146 ASN 146 144 144 ASN ASN A . n 
A 1 147 PHE 147 145 145 PHE PHE A . n 
B 1 1   GLN 1   -1  ?   ?   ?   B . n 
B 1 2   SER 2   0   ?   ?   ?   B . n 
B 1 3   MET 3   1   1   MET MET B . n 
B 1 4   LYS 4   2   2   LYS LYS B . n 
B 1 5   ILE 5   3   3   ILE ILE B . n 
B 1 6   ARG 6   4   4   ARG ARG B . n 
B 1 7   ASN 7   5   5   ASN ASN B . n 
B 1 8   TRP 8   6   6   TRP TRP B . n 
B 1 9   ILE 9   7   7   ILE ILE B . n 
B 1 10  LYS 10  8   8   LYS LYS B . n 
B 1 11  ASP 11  9   9   ASP ASP B . n 
B 1 12  ASP 12  10  10  ASP ASP B . n 
B 1 13  VAL 13  11  11  VAL VAL B . n 
B 1 14  PRO 14  12  12  PRO PRO B . n 
B 1 15  GLN 15  13  13  GLN GLN B . n 
B 1 16  VAL 16  14  14  VAL VAL B . n 
B 1 17  SER 17  15  15  SER SER B . n 
B 1 18  GLU 18  16  16  GLU GLU B . n 
B 1 19  ILE 19  17  17  ILE ILE B . n 
B 1 20  ALA 20  18  18  ALA ALA B . n 
B 1 21  GLU 21  19  19  GLU GLU B . n 
B 1 22  ALA 22  20  20  ALA ALA B . n 
B 1 23  ALA 23  21  21  ALA ALA B . n 
B 1 24  MET 24  22  22  MET MET B . n 
B 1 25  PRO 25  23  23  PRO PRO B . n 
B 1 26  PHE 26  24  24  PHE PHE B . n 
B 1 27  PRO 27  25  25  PRO PRO B . n 
B 1 28  TRP 28  26  26  TRP TRP B . n 
B 1 29  SER 29  27  27  SER ALA B . n 
B 1 30  GLU 30  28  28  GLU GLU B . n 
B 1 31  LYS 31  29  29  LYS LYS B . n 
B 1 32  PHE 32  30  30  PHE PHE B . n 
B 1 33  PHE 33  31  31  PHE PHE B . n 
B 1 34  TYR 34  32  32  TYR TYR B . n 
B 1 35  ASP 35  33  33  ASP ASP B . n 
B 1 36  CYS 36  34  34  CYS CYS B . n 
B 1 37  LEU 37  35  35  LEU LEU B . n 
B 1 38  LYS 38  36  36  LYS LYS B . n 
B 1 39  SER 39  37  37  SER SER B . n 
B 1 40  ASN 40  38  38  ASN ASN B . n 
B 1 41  TYR 41  39  39  TYR TYR B . n 
B 1 42  TYR 42  40  40  TYR TYR B . n 
B 1 43  GLY 43  41  41  GLY GLY B . n 
B 1 44  TRP 44  42  42  TRP TRP B . n 
B 1 45  VAL 45  43  43  VAL VAL B . n 
B 1 46  MET 46  44  44  MET MET B . n 
B 1 47  GLU 47  45  45  GLU GLU B . n 
B 1 48  SER 48  46  46  SER SER B . n 
B 1 49  ASP 49  47  47  ASP ASP B . n 
B 1 50  HIS 50  48  48  HIS HIS B . n 
B 1 51  HIS 51  49  49  HIS HIS B . n 
B 1 52  LEU 52  50  50  LEU LEU B . n 
B 1 53  VAL 53  51  51  VAL VAL B . n 
B 1 54  GLY 54  52  52  GLY GLY B . n 
B 1 55  PHE 55  53  53  PHE PHE B . n 
B 1 56  ILE 56  54  54  ILE ILE B . n 
B 1 57  VAL 57  55  55  VAL VAL B . n 
B 1 58  ILE 58  56  56  ILE ILE B . n 
B 1 59  LEU 59  57  57  LEU LEU B . n 
B 1 60  MET 60  58  58  MET MET B . n 
B 1 61  GLN 61  59  59  GLN GLN B . n 
B 1 62  GLU 62  60  60  GLU GLU B . n 
B 1 63  LYS 63  61  61  LYS LYS B . n 
B 1 64  GLU 64  62  62  GLU GLU B . n 
B 1 65  CYS 65  63  63  CYS CYS B . n 
B 1 66  GLN 66  64  64  GLN GLN B . n 
B 1 67  LEU 67  65  65  LEU LEU B . n 
B 1 68  MET 68  66  66  MET MET B . n 
B 1 69  ASN 69  67  67  ASN ASN B . n 
B 1 70  ILE 70  68  68  ILE ILE B . n 
B 1 71  ALA 71  69  69  ALA ALA B . n 
B 1 72  VAL 72  70  70  VAL VAL B . n 
B 1 73  ALA 73  71  71  ALA ALA B . n 
B 1 74  PRO 74  72  72  PRO PRO B . n 
B 1 75  ARG 75  73  73  ARG ARG B . n 
B 1 76  TYR 76  74  74  TYR TYR B . n 
B 1 77  GLN 77  75  75  GLN GLN B . n 
B 1 78  ARG 78  76  76  ARG ARG B . n 
B 1 79  LYS 79  77  77  LYS LYS B . n 
B 1 80  GLY 80  78  78  GLY GLY B . n 
B 1 81  VAL 81  79  79  VAL VAL B . n 
B 1 82  ALA 82  80  80  ALA ALA B . n 
B 1 83  SER 83  81  81  SER SER B . n 
B 1 84  GLN 84  82  82  GLN GLN B . n 
B 1 85  LEU 85  83  83  LEU LEU B . n 
B 1 86  LEU 86  84  84  LEU LEU B . n 
B 1 87  GLN 87  85  85  GLN GLN B . n 
B 1 88  HIS 88  86  86  HIS HIS B . n 
B 1 89  ALA 89  87  87  ALA ALA B . n 
B 1 90  LEU 90  88  88  LEU LEU B . n 
B 1 91  HIS 91  89  89  HIS HIS B . n 
B 1 92  TYR 92  90  90  TYR TYR B . n 
B 1 93  ALA 93  91  91  ALA ALA B . n 
B 1 94  LYS 94  92  92  LYS LYS B . n 
B 1 95  THR 95  93  93  THR THR B . n 
B 1 96  HIS 96  94  94  HIS HIS B . n 
B 1 97  HIS 97  95  95  HIS HIS B . n 
B 1 98  ALA 98  96  96  ALA ALA B . n 
B 1 99  THR 99  97  97  THR THR B . n 
B 1 100 ARG 100 98  98  ARG ARG B . n 
B 1 101 LEU 101 99  99  LEU LEU B . n 
B 1 102 LEU 102 100 100 LEU LEU B . n 
B 1 103 LEU 103 101 101 LEU LEU B . n 
B 1 104 GLU 104 102 102 GLU GLU B . n 
B 1 105 VAL 105 103 103 VAL VAL B . n 
B 1 106 ARG 106 104 104 ARG ARG B . n 
B 1 107 LYS 107 105 105 LYS LYS B . n 
B 1 108 SER 108 106 106 SER SER B . n 
B 1 109 ASN 109 107 107 ASN ASN B . n 
B 1 110 ARG 110 108 108 ARG ARG B . n 
B 1 111 SER 111 109 109 SER SER B . n 
B 1 112 ALA 112 110 110 ALA ALA B . n 
B 1 113 ILE 113 111 111 ILE ILE B . n 
B 1 114 GLU 114 112 112 GLU GLU B . n 
B 1 115 PHE 115 113 113 PHE PHE B . n 
B 1 116 TYR 116 114 114 TYR TYR B . n 
B 1 117 LYS 117 115 115 LYS LYS B . n 
B 1 118 LYS 118 116 116 LYS LYS B . n 
B 1 119 ALA 119 117 117 ALA ALA B . n 
B 1 120 GLY 120 118 118 GLY GLY B . n 
B 1 121 GLY 121 119 119 GLY GLY B . n 
B 1 122 VAL 122 120 120 VAL VAL B . n 
B 1 123 GLU 123 121 121 GLU GLU B . n 
B 1 124 ILE 124 122 122 ILE ILE B . n 
B 1 125 GLY 125 123 123 GLY GLY B . n 
B 1 126 VAL 126 124 124 VAL VAL B . n 
B 1 127 ARG 127 125 125 ARG ARG B . n 
B 1 128 LYS 128 126 126 LYS LYS B . n 
B 1 129 ASN 129 127 127 ASN ASN B . n 
B 1 130 TYR 130 128 128 TYR TYR B . n 
B 1 131 TYR 131 129 129 TYR TYR B . n 
B 1 132 PRO 132 130 130 PRO PRO B . n 
B 1 133 ALA 133 131 131 ALA ALA B . n 
B 1 134 GLU 134 132 132 GLU GLU B . n 
B 1 135 LYS 135 133 133 LYS LYS B . n 
B 1 136 GLY 136 134 134 GLY GLY B . n 
B 1 137 ARG 137 135 135 ARG ARG B . n 
B 1 138 GLU 138 136 136 GLU GLU B . n 
B 1 139 ASP 139 137 137 ASP ASP B . n 
B 1 140 ALA 140 138 138 ALA ALA B . n 
B 1 141 LEU 141 139 139 LEU LEU B . n 
B 1 142 VAL 142 140 140 VAL VAL B . n 
B 1 143 PHE 143 141 141 PHE PHE B . n 
B 1 144 ASN 144 142 142 ASN ASN B . n 
B 1 145 LEU 145 143 143 LEU LEU B . n 
B 1 146 ASN 146 144 144 ASN ASN B . n 
B 1 147 PHE 147 145 145 PHE PHE B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        COA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   COA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 COA 1   201 1   COA COA A . 
D 2 COA 1   201 2   COA COA B . 
E 3 HOH 1   301 322 HOH HOH A . 
E 3 HOH 2   302 32  HOH HOH A . 
E 3 HOH 3   303 75  HOH HOH A . 
E 3 HOH 4   304 222 HOH HOH A . 
E 3 HOH 5   305 7   HOH HOH A . 
E 3 HOH 6   306 13  HOH HOH A . 
E 3 HOH 7   307 110 HOH HOH A . 
E 3 HOH 8   308 49  HOH HOH A . 
E 3 HOH 9   309 145 HOH HOH A . 
E 3 HOH 10  310 2   HOH HOH A . 
E 3 HOH 11  311 143 HOH HOH A . 
E 3 HOH 12  312 28  HOH HOH A . 
E 3 HOH 13  313 92  HOH HOH A . 
E 3 HOH 14  314 161 HOH HOH A . 
E 3 HOH 15  315 83  HOH HOH A . 
E 3 HOH 16  316 214 HOH HOH A . 
E 3 HOH 17  317 187 HOH HOH A . 
E 3 HOH 18  318 36  HOH HOH A . 
E 3 HOH 19  319 176 HOH HOH A . 
E 3 HOH 20  320 321 HOH HOH A . 
E 3 HOH 21  321 215 HOH HOH A . 
E 3 HOH 22  322 4   HOH HOH A . 
E 3 HOH 23  323 69  HOH HOH A . 
E 3 HOH 24  324 205 HOH HOH A . 
E 3 HOH 25  325 204 HOH HOH A . 
E 3 HOH 26  326 85  HOH HOH A . 
E 3 HOH 27  327 16  HOH HOH A . 
E 3 HOH 28  328 30  HOH HOH A . 
E 3 HOH 29  329 157 HOH HOH A . 
E 3 HOH 30  330 271 HOH HOH A . 
E 3 HOH 31  331 369 HOH HOH A . 
E 3 HOH 32  332 86  HOH HOH A . 
E 3 HOH 33  333 22  HOH HOH A . 
E 3 HOH 34  334 20  HOH HOH A . 
E 3 HOH 35  335 15  HOH HOH A . 
E 3 HOH 36  336 183 HOH HOH A . 
E 3 HOH 37  337 10  HOH HOH A . 
E 3 HOH 38  338 11  HOH HOH A . 
E 3 HOH 39  339 304 HOH HOH A . 
E 3 HOH 40  340 330 HOH HOH A . 
E 3 HOH 41  341 200 HOH HOH A . 
E 3 HOH 42  342 115 HOH HOH A . 
E 3 HOH 43  343 25  HOH HOH A . 
E 3 HOH 44  344 47  HOH HOH A . 
E 3 HOH 45  345 105 HOH HOH A . 
E 3 HOH 46  346 48  HOH HOH A . 
E 3 HOH 47  347 163 HOH HOH A . 
E 3 HOH 48  348 224 HOH HOH A . 
E 3 HOH 49  349 325 HOH HOH A . 
E 3 HOH 50  350 128 HOH HOH A . 
E 3 HOH 51  351 53  HOH HOH A . 
E 3 HOH 52  352 46  HOH HOH A . 
E 3 HOH 53  353 42  HOH HOH A . 
E 3 HOH 54  354 148 HOH HOH A . 
E 3 HOH 55  355 80  HOH HOH A . 
E 3 HOH 56  356 106 HOH HOH A . 
E 3 HOH 57  357 27  HOH HOH A . 
E 3 HOH 58  358 167 HOH HOH A . 
E 3 HOH 59  359 84  HOH HOH A . 
E 3 HOH 60  360 62  HOH HOH A . 
E 3 HOH 61  361 9   HOH HOH A . 
E 3 HOH 62  362 18  HOH HOH A . 
E 3 HOH 63  363 355 HOH HOH A . 
E 3 HOH 64  364 192 HOH HOH A . 
E 3 HOH 65  365 349 HOH HOH A . 
E 3 HOH 66  366 40  HOH HOH A . 
E 3 HOH 67  367 23  HOH HOH A . 
E 3 HOH 68  368 29  HOH HOH A . 
E 3 HOH 69  369 72  HOH HOH A . 
E 3 HOH 70  370 39  HOH HOH A . 
E 3 HOH 71  371 56  HOH HOH A . 
E 3 HOH 72  372 95  HOH HOH A . 
E 3 HOH 73  373 57  HOH HOH A . 
E 3 HOH 74  374 251 HOH HOH A . 
E 3 HOH 75  375 264 HOH HOH A . 
E 3 HOH 76  376 79  HOH HOH A . 
E 3 HOH 77  377 350 HOH HOH A . 
E 3 HOH 78  378 309 HOH HOH A . 
E 3 HOH 79  379 59  HOH HOH A . 
E 3 HOH 80  380 107 HOH HOH A . 
E 3 HOH 81  381 5   HOH HOH A . 
E 3 HOH 82  382 206 HOH HOH A . 
E 3 HOH 83  383 310 HOH HOH A . 
E 3 HOH 84  384 324 HOH HOH A . 
E 3 HOH 85  385 91  HOH HOH A . 
E 3 HOH 86  386 226 HOH HOH A . 
E 3 HOH 87  387 182 HOH HOH A . 
E 3 HOH 88  388 33  HOH HOH A . 
E 3 HOH 89  389 351 HOH HOH A . 
E 3 HOH 90  390 17  HOH HOH A . 
E 3 HOH 91  391 156 HOH HOH A . 
E 3 HOH 92  392 326 HOH HOH A . 
E 3 HOH 93  393 54  HOH HOH A . 
E 3 HOH 94  394 246 HOH HOH A . 
E 3 HOH 95  395 14  HOH HOH A . 
E 3 HOH 96  396 188 HOH HOH A . 
E 3 HOH 97  397 38  HOH HOH A . 
E 3 HOH 98  398 240 HOH HOH A . 
E 3 HOH 99  399 1   HOH HOH A . 
E 3 HOH 100 400 277 HOH HOH A . 
E 3 HOH 101 401 319 HOH HOH A . 
E 3 HOH 102 402 315 HOH HOH A . 
E 3 HOH 103 403 353 HOH HOH A . 
E 3 HOH 104 404 311 HOH HOH A . 
E 3 HOH 105 405 352 HOH HOH A . 
E 3 HOH 106 406 318 HOH HOH A . 
E 3 HOH 107 407 312 HOH HOH A . 
E 3 HOH 108 408 43  HOH HOH A . 
E 3 HOH 109 409 184 HOH HOH A . 
E 3 HOH 110 410 372 HOH HOH A . 
E 3 HOH 111 411 146 HOH HOH A . 
E 3 HOH 112 412 45  HOH HOH A . 
E 3 HOH 113 413 317 HOH HOH A . 
E 3 HOH 114 414 130 HOH HOH A . 
E 3 HOH 115 415 314 HOH HOH A . 
E 3 HOH 116 416 186 HOH HOH A . 
E 3 HOH 117 417 316 HOH HOH A . 
E 3 HOH 118 418 266 HOH HOH A . 
E 3 HOH 119 419 294 HOH HOH A . 
E 3 HOH 120 420 371 HOH HOH A . 
E 3 HOH 121 421 354 HOH HOH A . 
E 3 HOH 122 422 331 HOH HOH A . 
E 3 HOH 123 423 26  HOH HOH A . 
E 3 HOH 124 424 328 HOH HOH A . 
E 3 HOH 125 425 21  HOH HOH A . 
E 3 HOH 126 426 323 HOH HOH A . 
E 3 HOH 127 427 370 HOH HOH A . 
E 3 HOH 128 428 191 HOH HOH A . 
E 3 HOH 129 429 373 HOH HOH A . 
E 3 HOH 130 430 104 HOH HOH A . 
E 3 HOH 131 431 320 HOH HOH A . 
E 3 HOH 132 432 109 HOH HOH A . 
E 3 HOH 133 433 338 HOH HOH A . 
E 3 HOH 134 434 360 HOH HOH A . 
E 3 HOH 135 435 298 HOH HOH A . 
E 3 HOH 136 436 213 HOH HOH A . 
E 3 HOH 137 437 339 HOH HOH A . 
F 3 HOH 1   301 291 HOH HOH B . 
F 3 HOH 2   302 67  HOH HOH B . 
F 3 HOH 3   303 340 HOH HOH B . 
F 3 HOH 4   304 258 HOH HOH B . 
F 3 HOH 5   305 313 HOH HOH B . 
F 3 HOH 6   306 308 HOH HOH B . 
F 3 HOH 7   307 365 HOH HOH B . 
F 3 HOH 8   308 244 HOH HOH B . 
F 3 HOH 9   309 19  HOH HOH B . 
F 3 HOH 10  310 78  HOH HOH B . 
F 3 HOH 11  311 241 HOH HOH B . 
F 3 HOH 12  312 12  HOH HOH B . 
F 3 HOH 13  313 361 HOH HOH B . 
F 3 HOH 14  314 348 HOH HOH B . 
F 3 HOH 15  315 228 HOH HOH B . 
F 3 HOH 16  316 126 HOH HOH B . 
F 3 HOH 17  317 267 HOH HOH B . 
F 3 HOH 18  318 131 HOH HOH B . 
F 3 HOH 19  319 34  HOH HOH B . 
F 3 HOH 20  320 52  HOH HOH B . 
F 3 HOH 21  321 88  HOH HOH B . 
F 3 HOH 22  322 270 HOH HOH B . 
F 3 HOH 23  323 268 HOH HOH B . 
F 3 HOH 24  324 300 HOH HOH B . 
F 3 HOH 25  325 247 HOH HOH B . 
F 3 HOH 26  326 284 HOH HOH B . 
F 3 HOH 27  327 279 HOH HOH B . 
F 3 HOH 28  328 363 HOH HOH B . 
F 3 HOH 29  329 116 HOH HOH B . 
F 3 HOH 30  330 368 HOH HOH B . 
F 3 HOH 31  331 102 HOH HOH B . 
F 3 HOH 32  332 41  HOH HOH B . 
F 3 HOH 33  333 229 HOH HOH B . 
F 3 HOH 34  334 208 HOH HOH B . 
F 3 HOH 35  335 334 HOH HOH B . 
F 3 HOH 36  336 341 HOH HOH B . 
F 3 HOH 37  337 293 HOH HOH B . 
F 3 HOH 38  338 332 HOH HOH B . 
F 3 HOH 39  339 357 HOH HOH B . 
F 3 HOH 40  340 37  HOH HOH B . 
F 3 HOH 41  341 366 HOH HOH B . 
F 3 HOH 42  342 8   HOH HOH B . 
F 3 HOH 43  343 358 HOH HOH B . 
F 3 HOH 44  344 346 HOH HOH B . 
F 3 HOH 45  345 89  HOH HOH B . 
F 3 HOH 46  346 367 HOH HOH B . 
F 3 HOH 47  347 345 HOH HOH B . 
F 3 HOH 48  348 333 HOH HOH B . 
F 3 HOH 49  349 335 HOH HOH B . 
F 3 HOH 50  350 343 HOH HOH B . 
F 3 HOH 51  351 356 HOH HOH B . 
F 3 HOH 52  352 342 HOH HOH B . 
F 3 HOH 53  353 359 HOH HOH B . 
F 3 HOH 54  354 290 HOH HOH B . 
F 3 HOH 55  355 327 HOH HOH B . 
F 3 HOH 56  356 337 HOH HOH B . 
F 3 HOH 57  357 362 HOH HOH B . 
F 3 HOH 58  358 364 HOH HOH B . 
F 3 HOH 59  359 329 HOH HOH B . 
F 3 HOH 60  360 347 HOH HOH B . 
F 3 HOH 61  361 344 HOH HOH B . 
F 3 HOH 62  362 336 HOH HOH B . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      27 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     OG 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    B 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     29 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    OG 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.2_5419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BALBES   ? ? ? .           4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? ARP/wARP ? ? ? .           5 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .           6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MTO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.460 
_cell.length_a_esd                 ? 
_cell.length_b                     41.460 
_cell.length_b_esd                 ? 
_cell.length_c                     325.720 
_cell.length_c_esd                 ? 
_cell.volume                       484879.310 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9MTO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            
;P 32 2"
;
_symmetry.space_group_name_H-M             'P 32 2 1' 
_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                   9MTO 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.08 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.10% w/v n-Octyl-beta-D-glucoside, 0.1 M Sodium citrate tribasic dihydrate pH 5.5, 22% w/v Polyethylene glycol 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-07-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97940 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97940 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          25.29 
_reflns.entry_id                                       9MTO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.69 
_reflns.d_resolution_low                               46.53 
_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                                     38359 
_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 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.039 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.107 
_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                                    1.69 
_reflns_shell.d_res_low                                     1.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2775 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               9.9 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.482 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.602 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.002 
_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                               42.79 
_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                                 9MTO 
_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                            1.69 
_refine.ls_d_res_low                             36.19 
_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                     38236 
_refine.ls_number_reflns_R_free                  1984 
_refine.ls_number_reflns_R_work                  36252 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 5.19 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2327 
_refine.ls_R_factor_R_free                       0.2659 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2308 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 26.3464 
_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                            0.2026 
_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                       1.69 
_refine_hist.d_res_low                        36.19 
_refine_hist.number_atoms_solvent             199 
_refine_hist.number_atoms_total               2696 
_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        2401 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         96 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0157  ? 2567 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.8332  ? 3478 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.1002  ? 355  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0108  ? 431  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 18.9220 ? 1039 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.69 1.73  . . 155 2542 99.96  . . . . 0.2976 . . . . . . . . . . . 0.3628 
'X-RAY DIFFRACTION' 1.73 1.78  . . 118 2499 100.00 . . . . 0.2822 . . . . . . . . . . . 0.3590 
'X-RAY DIFFRACTION' 1.78 1.83  . . 138 2547 100.00 . . . . 0.2940 . . . . . . . . . . . 0.3481 
'X-RAY DIFFRACTION' 1.83 1.89  . . 149 2595 100.00 . . . . 0.2532 . . . . . . . . . . . 0.3444 
'X-RAY DIFFRACTION' 1.89 1.96  . . 133 2472 99.92  . . . . 0.2462 . . . . . . . . . . . 0.2332 
'X-RAY DIFFRACTION' 1.96 2.04  . . 150 2532 100.00 . . . . 0.2239 . . . . . . . . . . . 0.2527 
'X-RAY DIFFRACTION' 2.04 2.13  . . 128 2550 100.00 . . . . 0.2481 . . . . . . . . . . . 0.2706 
'X-RAY DIFFRACTION' 2.13 2.24  . . 120 2602 100.00 . . . . 0.2239 . . . . . . . . . . . 0.2610 
'X-RAY DIFFRACTION' 2.24 2.38  . . 129 2565 99.93  . . . . 0.2398 . . . . . . . . . . . 0.3186 
'X-RAY DIFFRACTION' 2.38 2.57  . . 125 2656 100.00 . . . . 0.2403 . . . . . . . . . . . 0.2772 
'X-RAY DIFFRACTION' 2.57 2.82  . . 147 2552 99.96  . . . . 0.2535 . . . . . . . . . . . 0.2992 
'X-RAY DIFFRACTION' 2.82 3.23  . . 164 2620 100.00 . . . . 0.2253 . . . . . . . . . . . 0.3026 
'X-RAY DIFFRACTION' 3.23 4.07  . . 140 2676 100.00 . . . . 0.2087 . . . . . . . . . . . 0.2258 
'X-RAY DIFFRACTION' 4.07 36.19 . . 188 2844 99.97  . . . . 0.2189 . . . . . . . . . . . 0.2356 
# 
_struct.entry_id                     9MTO 
_struct.title                        'Crystal structure of acetyltransferase CBU0801 from Coxiella burnetii' 
_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        9MTO 
_struct_keywords.text            
'acetyltransferase, Structural Genomics, Center for Structural Biology of Infectious Diseases, CSBID, 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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q83DD7_COXBU 
_struct_ref.pdbx_db_accession          Q83DD7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKIRNWIKDDVPQVSEIAEAAMPFPWSEKFFYDCLKSNYYGWVMESDHHLVGFIVILMQEKECQLMNIAVAPRYQRKGVA
SQLLQHALHYAKTHHATRLLLEVRKSNRSAIEFYKKAGGVEIGVRKNYYPAEKGREDALVFNLNF
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9MTO A 3 ? 147 ? Q83DD7 1 ? 145 ? 1 145 
2 1 9MTO B 3 ? 147 ? Q83DD7 1 ? 145 ? 1 145 
# 
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 9MTO GLN A 1 ? UNP Q83DD7 ? ? 'expression tag' -1 1 
1 9MTO SER A 2 ? UNP Q83DD7 ? ? 'expression tag' 0  2 
2 9MTO GLN B 1 ? UNP Q83DD7 ? ? 'expression tag' -1 3 
2 9MTO SER B 2 ? UNP Q83DD7 ? ? 'expression tag' 0  4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_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 ILE A 9   ? ASP A 11  ? ILE A 7   ASP A 9   5 ? 3  
HELX_P HELX_P2  AA2 ASP A 12  ? MET A 24  ? ASP A 10  MET A 22  1 ? 13 
HELX_P HELX_P3  AA3 SER A 29  ? CYS A 36  ? SER A 27  CYS A 34  1 ? 8  
HELX_P HELX_P4  AA4 PRO A 74  ? GLN A 77  ? PRO A 72  GLN A 75  5 ? 4  
HELX_P HELX_P5  AA5 GLY A 80  ? HIS A 96  ? GLY A 78  HIS A 94  1 ? 17 
HELX_P HELX_P6  AA6 ASN A 109 ? ALA A 119 ? ASN A 107 ALA A 117 1 ? 11 
HELX_P HELX_P7  AA7 ILE B 9   ? ASP B 11  ? ILE B 7   ASP B 9   5 ? 3  
HELX_P HELX_P8  AA8 ASP B 12  ? MET B 24  ? ASP B 10  MET B 22  1 ? 13 
HELX_P HELX_P9  AA9 SER B 29  ? CYS B 36  ? SER B 27  CYS B 34  1 ? 8  
HELX_P HELX_P10 AB1 PRO B 74  ? GLN B 77  ? PRO B 72  GLN B 75  5 ? 4  
HELX_P HELX_P11 AB2 GLY B 80  ? HIS B 96  ? GLY B 78  HIS B 94  1 ? 17 
HELX_P HELX_P12 AB3 ASN B 109 ? ALA B 119 ? ASN B 107 ALA B 117 1 ? 11 
# 
_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 ? 7 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? 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 MET A 3   ? ASN A 7   ? MET A 1   ASN A 5   
AA1 2 TYR A 41  ? SER A 48  ? TYR A 39  SER A 46  
AA1 3 HIS A 51  ? GLN A 61  ? HIS A 49  GLN A 59  
AA1 4 GLU A 64  ? VAL A 72  ? GLU A 62  VAL A 70  
AA1 5 ARG A 100 ? ARG A 106 ? ARG A 98  ARG A 104 
AA1 6 ARG A 137 ? ASN A 146 ? ARG A 135 ASN A 144 
AA1 7 VAL A 122 ? PRO A 132 ? VAL A 120 PRO A 130 
AA2 1 LYS B 4   ? ASN B 7   ? LYS B 2   ASN B 5   
AA2 2 TYR B 41  ? SER B 48  ? TYR B 39  SER B 46  
AA2 3 HIS B 51  ? GLN B 61  ? HIS B 49  GLN B 59  
AA2 4 GLU B 64  ? VAL B 72  ? GLU B 62  VAL B 70  
AA2 5 ARG B 100 ? ARG B 106 ? ARG B 98  ARG B 104 
AA2 6 ARG B 137 ? ASN B 146 ? ARG B 135 ASN B 144 
AA2 7 VAL B 122 ? PRO B 132 ? VAL B 120 PRO B 130 
# 
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 4   ? N LYS A 2   O GLU A 47  ? O GLU A 45  
AA1 2 3 N TYR A 42  ? N TYR A 40  O ILE A 58  ? O ILE A 56  
AA1 3 4 N VAL A 57  ? N VAL A 55  O ASN A 69  ? O ASN A 67  
AA1 4 5 N LEU A 67  ? N LEU A 65  O LEU A 102 ? O LEU A 100 
AA1 5 6 N LEU A 101 ? N LEU A 99  O LEU A 145 ? O LEU A 143 
AA1 6 7 O VAL A 142 ? O VAL A 140 N ILE A 124 ? N ILE A 122 
AA2 1 2 N ARG B 6   ? N ARG B 4   O VAL B 45  ? O VAL B 43  
AA2 2 3 N TYR B 42  ? N TYR B 40  O ILE B 58  ? O ILE B 56  
AA2 3 4 N VAL B 57  ? N VAL B 55  O ASN B 69  ? O ASN B 67  
AA2 4 5 N LEU B 67  ? N LEU B 65  O LEU B 102 ? O LEU B 100 
AA2 5 6 N LEU B 103 ? N LEU B 101 O PHE B 143 ? O PHE B 141 
AA2 6 7 O VAL B 142 ? O VAL B 140 N ILE B 124 ? N ILE B 122 
# 
_pdbx_entry_details.entry_id                   9MTO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NE2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HIS 
_pdbx_validate_symm_contact.auth_seq_id_1     86 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O8A 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    COA 
_pdbx_validate_symm_contact.auth_seq_id_2     201 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   6_664 
_pdbx_validate_symm_contact.dist              1.94 
# 
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 GLU A 60 ? ? 56.11   -129.20 
2 1 ASN A 67 ? ? -171.42 144.64  
3 1 LEU B 35 ? ? -68.38  5.09    
4 1 ASN B 38 ? ? 66.15   -12.47  
5 1 ASP B 47 ? ? 29.55   59.40   
6 1 GLU B 60 ? ? 49.21   -111.76 
7 1 HIS B 94 ? ? -111.35 59.67   
# 
_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   'Center for Structural Biology of Infectious Diseases' 
_pdbx_SG_project.initial_of_center     CSBID 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+2/3   
3 -x+y,-x,z+1/3  
4 x-y,-y,-z+1/3  
5 -x,-x+y,-z+2/3 
6 y,x,-z         
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 17.5917213091 -6.67824425416 -53.528987663  0.411362424701  ? -0.0309526296749  ? 0.0330748420424 
? 0.150337039072 ? 0.00942449408576 ? 0.272122300048 ? 6.41283867373  ? 0.735804277975   ? 1.64845602464   ? 6.59889109418  ? 
4.26117810231    ? 4.30083199809  ? -0.170035717286  ? 0.36245650063    ? -0.363900177233 ? -1.04222176304   ? -0.124030641537  ? 
-0.470798162459  ? -0.337087610523  ? 0.907842822929  ? 0.198768871508    ? 
2  'X-RAY DIFFRACTION' ? refined 11.8775934053 -11.8723877959 -42.7352591123 0.126647693822  ? 0.0449284844594   ? 
0.00871407348772  ? 0.317132454984 ? 0.0418187339499  ? 0.295796534861 ? 4.74959184556  ? 0.0304380001353  ? 0.71753630978   ? 
2.27392731724  ? -0.132599553005  ? 4.36778228571  ? 0.236298324591   ? -0.301203877921  ? -0.150584468876 ? -0.0475902527378 ? 
-0.0528190142466 ? 1.07213684193    ? -0.0847263616897 ? -0.999729201561 ? -0.0976102166346  ? 
3  'X-RAY DIFFRACTION' ? refined 17.2852081267 -9.23538030476 -35.1726179011 0.608673414782  ? -0.229328828709   ? 0.210591332606 
? 0.479913804879 ? -0.265865158519  ? 0.138445061628 ? 3.69984807513  ? 1.93942252619    ? -1.09666742706  ? 3.40635540391  ? 
0.101703708172   ? 0.475527018189 ? 0.471216256474   ? -1.41715968626   ? 0.213550818689  ? 1.35440393083    ? -0.583281909723  ? 
-0.313274111247  ? -1.14414688936   ? 0.378338399568  ? -0.0569113262382  ? 
4  'X-RAY DIFFRACTION' ? refined 20.4871845225 -8.11008313812 -46.8881659329 0.129030826934  ? -0.0448957962188  ? 
-0.0109405804872  ? 0.146058870251 ? 0.00843729849517 ? 0.194477749157 ? 4.9360220205   ? 1.31443850927    ? 2.54590457125   ? 
3.57583097536  ? 1.13736930559    ? 4.69470443212  ? -0.273291125688  ? -0.113222719397  ? 0.40691611303   ? 0.0514566784415  ? 
0.12003900417    ? 0.0160965665425  ? -0.47076640129   ? 0.307296857378  ? 0.153935619893    ? 
5  'X-RAY DIFFRACTION' ? refined 25.1884743941 -14.4362280233 -44.9820221836 0.114147112711  ? -0.0205769129434  ? 
-0.0114091850692  ? 0.134912991362 ? 0.0443943368737  ? 0.148508144528 ? 5.84409917874  ? -0.0024412676317 ? 0.187642101546  ? 
4.22442046994  ? 0.0893759849408  ? 4.10976787553  ? -0.0662751116885 ? 0.15484651174    ? 0.29006530367   ? 0.227488598023   ? 
-0.0314093096206 ? -0.0553808001678 ? -0.173930456498  ? 0.432838333669  ? 0.0129498277503   ? 
6  'X-RAY DIFFRACTION' ? refined 29.7863102399 -7.06395547379 -50.3414181206 0.27660969846   ? -0.163352906753   ? 
-0.0173797786798  ? 0.350176726457 ? 0.138758840725   ? 0.313832851719 ? 5.01529676982  ? 4.70110335593    ? -0.779078004336 ? 
8.4920218691   ? -0.0572994203746 ? 0.257504714072 ? -0.19652337268   ? 1.08226756731    ? 0.803457945635  ? -0.529027341685  ? 
-0.0491944529563 ? 0.138690400414   ? -0.784905869053  ? 0.706270665571  ? -0.144657378256   ? 
7  'X-RAY DIFFRACTION' ? refined 32.8201121191 -12.4525028959 -38.385973837  0.186989887361  ? -0.0815276595812  ? 
-0.0461808438347  ? 0.256391263654 ? 0.0301677229     ? 0.26781663979  ? 3.68072321314  ? 1.25429294926    ? -0.280214239224 ? 
6.63467689867  ? -1.15997405354   ? 3.20185094623  ? -0.0704696862911 ? -0.0238350067006 ? 0.449209544251  ? -0.230528180098  ? 
-0.0186127872304 ? -0.13740222931   ? -0.415374955584  ? 0.436607894145  ? 0.0462263380809   ? 
8  'X-RAY DIFFRACTION' ? refined 30.7104311507 -21.5652775722 -34.0522016926 0.131566444023  ? 0.000701932899013 ? 
-0.0040187837168  ? 0.343520699853 ? 0.0511784972097  ? 0.282371590045 ? 4.38972130901  ? -0.107491751272  ? -0.157254885176 ? 
0.944061463081 ? -0.760642263227  ? 3.39414181821  ? -0.0639150594738 ? -0.66805821341   ? -0.353658175548 ? 0.0457407617704  ? 
-0.222975370713  ? -0.0340996590059 ? 0.131585531344   ? 0.751802057231  ? 0.233051655455    ? 
9  'X-RAY DIFFRACTION' ? refined 36.9419042386 -14.3319599978 -39.7684912117 0.0829323121729 ? -0.0190185890683  ? 
-0.00728380183095 ? 0.492241242579 ? 0.0127360127641  ? 0.305672174915 ? 1.86778321184  ? -0.82925188492   ? 2.33517507301   ? 
1.11613325442  ? 0.172603344337   ? 4.86782759567  ? -0.230567134709  ? -0.360873107454  ? 0.321821666618  ? 0.0288770420504  ? 
-0.115182366125  ? -0.424679789594  ? -0.579355920386  ? 0.749304433294  ? 0.279714040348    ? 
10 'X-RAY DIFFRACTION' ? refined 21.5917884369 -17.5673123183 -6.74798068057 0.386385105267  ? -0.17810766204    ? -0.165076747287 
? 1.23919748062  ? -0.097371100668  ? 0.28962590409  ? 0.701441392712 ? 0.045825497333   ? -0.217412496064 ? 2.11492991732  ? 
0.78476552209    ? 0.397465134999 ? 0.252608344014   ? -0.56014369189   ? -0.221628558586 ? 0.533480365523   ? 0.224615859683   ? 
-0.45647690907   ? 0.111531985144   ? 1.06005108888   ? -0.00810028664542 ? 
11 'X-RAY DIFFRACTION' ? refined 19.4431926088 -13.1972921503 -16.733873715  0.536941717303  ? -0.27020104684    ? 
-0.0292062930281  ? 0.572205740892 ? -0.0723385722695 ? 0.546645010807 ? 8.04776127487  ? 0.050934772757   ? 1.11259103826   ? 
0.596088248308 ? -1.8683828729    ? 5.98969957672  ? -0.458181232534  ? 0.0238795163926  ? 1.42788825453   ? 0.0196605486712  ? 
0.102861973973   ? 0.226439554337   ? -1.88510942855   ? 1.44728001931   ? 0.175620982942    ? 
12 'X-RAY DIFFRACTION' ? refined 17.1827006387 -16.9314633329 -2.91064706954 0.62483826288   ? -0.0468365711596  ? -0.133748391645 
? 0.972287923552 ? 0.0672011728893  ? 0.292957930157 ? 4.57393371776  ? 1.83483600708    ? -1.02076288345  ? 3.16203727627  ? 
2.25230183066    ? 3.13387527888  ? 0.229705409367   ? -0.632460509637  ? 0.0940336869521 ? -0.644198574348  ? 0.503370210009   ? 
-0.0249447264977 ? 1.26370329901    ? -0.110824561043 ? -0.547935485864   ? 
13 'X-RAY DIFFRACTION' ? refined 9.63766664262 -15.0249377887 -10.8260579542 0.418114498269  ? -0.00155425561711 ? 
-0.0183959625615  ? 0.578471550949 ? -0.0220628814977 ? 0.217258440066 ? 3.1725211635   ? 3.90708193229    ? -0.743502492967 ? 
5.53087411347  ? 1.40046632439    ? 7.02679968247  ? 0.366234039967   ? -0.90573919375   ? 0.0154213764812 ? 0.556034972905   ? 
-0.238071569863  ? 0.718676724306   ? -1.10174288233   ? -0.483855023376 ? -0.0280614114394  ? 
14 'X-RAY DIFFRACTION' ? refined 7.05537557131 -19.8345195183 -7.28149858612 0.579843690074  ? 0.0683707967981   ? 0.0331743508364 
? 0.840470804184 ? 0.00500467847709 ? 0.191464701513 ? 2.84320500848  ? 2.31442079151    ? 0.0136386912275 ? 2.04169968021  ? 
-0.811318464242  ? 5.01408927761  ? 0.149723712295   ? -1.4771189059    ? 0.0163774468962 ? 0.916102346628   ? -0.280878057329  ? 
-0.0721082033513 ? -0.124775541333  ? -0.158249492044 ? 0.0939947448242   ? 
15 'X-RAY DIFFRACTION' ? refined 4.82071404641 -28.1060521423 -16.5055760261 0.318411098283  ? -0.161571407142   ? 
5.77573773455e-05 ? 0.416802378094 ? 0.10871580689    ? 0.312669450416 ? 7.36410675607  ? -0.615306200127  ? -4.24246667906  ? 
4.53247951977  ? -0.744577236606  ? 5.7424702547   ? -0.468214914835  ? -0.502507346834  ? -0.817444516577 ? -0.420222779249  ? 
0.42571406478    ? -0.10442461633   ? 0.791512511966   ? -0.301053949988 ? 0.0951707061613   ? 
16 'X-RAY DIFFRACTION' ? refined 3.69181881875 -20.9180008378 -24.1473986087 0.147575518629  ? 0.0283991339002   ? 
-0.0259795396924  ? 0.423447527983 ? 0.0762377487187  ? 0.207463814469 ? 3.79742689669  ? 1.12501012113    ? -0.887507495217 ? 
2.42974179867  ? -0.119466494918  ? 5.95172790859  ? -0.058734165606  ? -0.313364902891  ? 0.240724489029  ? 0.152491679929   ? 
0.109265752043   ? 0.128628056575   ? -0.174297881336  ? -0.46912582522  ? 0.01578511581     ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A -1  ? A 9   A 7   ? ? 
;chain 'A' and (resid -1 through 7 )
;
2  'X-RAY DIFFRACTION' 2  A 10  A 8   ? A 23  A 21  ? ? 
;chain 'A' and (resid 8 through 21 )
;
3  'X-RAY DIFFRACTION' 3  A 24  A 22  ? A 40  A 38  ? ? 
;chain 'A' and (resid 22 through 38 )
;
4  'X-RAY DIFFRACTION' 4  A 41  A 39  ? A 61  A 59  ? ? 
;chain 'A' and (resid 39 through 59 )
;
5  'X-RAY DIFFRACTION' 5  A 62  A 60  ? A 80  A 78  ? ? 
;chain 'A' and (resid 60 through 78 )
;
6  'X-RAY DIFFRACTION' 6  A 81  A 79  ? A 95  A 93  ? ? 
;chain 'A' and (resid 79 through 93 )
;
7  'X-RAY DIFFRACTION' 7  A 96  A 94  ? A 109 A 107 ? ? 
;chain 'A' and (resid 94 through 107 )
;
8  'X-RAY DIFFRACTION' 8  A 110 A 108 ? A 139 A 137 ? ? 
;chain 'A' and (resid 108 through 137 )
;
9  'X-RAY DIFFRACTION' 9  A 140 A 138 ? A 147 A 145 ? ? 
;chain 'A' and (resid 138 through 145 )
;
10 'X-RAY DIFFRACTION' 10 B 1   B 1   ? B 21  B 21  ? ? 
;chain 'B' and (resid 1 through 21 )
;
11 'X-RAY DIFFRACTION' 11 B 22  B 22  ? B 38  B 38  ? ? 
;chain 'B' and (resid 22 through 38 )
;
12 'X-RAY DIFFRACTION' 12 B 39  B 39  ? B 48  B 48  ? ? 
;chain 'B' and (resid 39 through 48 )
;
13 'X-RAY DIFFRACTION' 13 B 49  B 49  ? B 70  B 70  ? ? 
;chain 'B' and (resid 49 through 70 )
;
14 'X-RAY DIFFRACTION' 14 B 71  B 71  ? B 104 B 104 ? ? 
;chain 'B' and (resid 71 through 104 )
;
15 'X-RAY DIFFRACTION' 15 B 105 B 105 ? B 116 B 116 ? ? 
;chain 'B' and (resid 105 through 116 )
;
16 'X-RAY DIFFRACTION' 16 B 117 B 117 ? B 145 B 145 ? ? 
;chain 'B' and (resid 117 through 145 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      A 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       362 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.99 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 B GLN -1 ? B GLN 1 
2 1 Y 1 B SER 0  ? B SER 2 
# 
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  
COA N1A  N Y N 74  
COA C2A  C Y N 75  
COA N3A  N Y N 76  
COA C4A  C Y N 77  
COA C5A  C Y N 78  
COA C6A  C Y N 79  
COA N6A  N N N 80  
COA N7A  N Y N 81  
COA C8A  C Y N 82  
COA N9A  N Y N 83  
COA C1B  C N R 84  
COA C2B  C N R 85  
COA O2B  O N N 86  
COA C3B  C N S 87  
COA O3B  O N N 88  
COA P3B  P N N 89  
COA O7A  O N N 90  
COA O8A  O N N 91  
COA O9A  O N N 92  
COA C4B  C N R 93  
COA O4B  O N N 94  
COA C5B  C N N 95  
COA O5B  O N N 96  
COA P1A  P N S 97  
COA O1A  O N N 98  
COA O2A  O N N 99  
COA O3A  O N N 100 
COA P2A  P N S 101 
COA O4A  O N N 102 
COA O5A  O N N 103 
COA O6A  O N N 104 
COA CBP  C N N 105 
COA CCP  C N N 106 
COA CDP  C N N 107 
COA CEP  C N N 108 
COA CAP  C N R 109 
COA OAP  O N N 110 
COA C9P  C N N 111 
COA O9P  O N N 112 
COA N8P  N N N 113 
COA C7P  C N N 114 
COA C6P  C N N 115 
COA C5P  C N N 116 
COA O5P  O N N 117 
COA N4P  N N N 118 
COA C3P  C N N 119 
COA C2P  C N N 120 
COA S1P  S N N 121 
COA H2A  H N N 122 
COA H61A H N N 123 
COA H62A H N N 124 
COA H8A  H N N 125 
COA H1B  H N N 126 
COA H2B  H N N 127 
COA HO2A H N N 128 
COA H3B  H N N 129 
COA HOA8 H N N 130 
COA HOA9 H N N 131 
COA H4B  H N N 132 
COA H51A H N N 133 
COA H52A H N N 134 
COA HOA2 H N N 135 
COA HOA5 H N N 136 
COA H121 H N N 137 
COA H122 H N N 138 
COA H131 H N N 139 
COA H132 H N N 140 
COA H133 H N N 141 
COA H141 H N N 142 
COA H142 H N N 143 
COA H143 H N N 144 
COA H10  H N N 145 
COA HO1  H N N 146 
COA HN8  H N N 147 
COA H71  H N N 148 
COA H72  H N N 149 
COA H61  H N N 150 
COA H62  H N N 151 
COA HN4  H N N 152 
COA H31  H N N 153 
COA H32  H N N 154 
COA H21  H N N 155 
COA H22  H N N 156 
COA HS1  H N N 157 
CYS N    N N N 158 
CYS CA   C N R 159 
CYS C    C N N 160 
CYS O    O N N 161 
CYS CB   C N N 162 
CYS SG   S N N 163 
CYS OXT  O N N 164 
CYS H    H N N 165 
CYS H2   H N N 166 
CYS HA   H N N 167 
CYS HB2  H N N 168 
CYS HB3  H N N 169 
CYS HG   H N N 170 
CYS HXT  H N N 171 
GLN N    N N N 172 
GLN CA   C N S 173 
GLN C    C N N 174 
GLN O    O N N 175 
GLN CB   C N N 176 
GLN CG   C N N 177 
GLN CD   C N N 178 
GLN OE1  O N N 179 
GLN NE2  N N N 180 
GLN OXT  O N N 181 
GLN H    H N N 182 
GLN H2   H N N 183 
GLN HA   H N N 184 
GLN HB2  H N N 185 
GLN HB3  H N N 186 
GLN HG2  H N N 187 
GLN HG3  H N N 188 
GLN HE21 H N N 189 
GLN HE22 H N N 190 
GLN HXT  H N N 191 
GLU N    N N N 192 
GLU CA   C N S 193 
GLU C    C N N 194 
GLU O    O N N 195 
GLU CB   C N N 196 
GLU CG   C N N 197 
GLU CD   C N N 198 
GLU OE1  O N N 199 
GLU OE2  O N N 200 
GLU OXT  O N N 201 
GLU H    H N N 202 
GLU H2   H N N 203 
GLU HA   H N N 204 
GLU HB2  H N N 205 
GLU HB3  H N N 206 
GLU HG2  H N N 207 
GLU HG3  H N N 208 
GLU HE2  H N N 209 
GLU HXT  H N N 210 
GLY N    N N N 211 
GLY CA   C N N 212 
GLY C    C N N 213 
GLY O    O N N 214 
GLY OXT  O N N 215 
GLY H    H N N 216 
GLY H2   H N N 217 
GLY HA2  H N N 218 
GLY HA3  H N N 219 
GLY HXT  H N N 220 
HIS N    N N N 221 
HIS CA   C N S 222 
HIS C    C N N 223 
HIS O    O N N 224 
HIS CB   C N N 225 
HIS CG   C Y N 226 
HIS ND1  N Y N 227 
HIS CD2  C Y N 228 
HIS CE1  C Y N 229 
HIS NE2  N Y N 230 
HIS OXT  O N N 231 
HIS H    H N N 232 
HIS H2   H N N 233 
HIS HA   H N N 234 
HIS HB2  H N N 235 
HIS HB3  H N N 236 
HIS HD1  H N N 237 
HIS HD2  H N N 238 
HIS HE1  H N N 239 
HIS HE2  H N N 240 
HIS HXT  H N N 241 
HOH O    O N N 242 
HOH H1   H N N 243 
HOH H2   H N N 244 
ILE N    N N N 245 
ILE CA   C N S 246 
ILE C    C N N 247 
ILE O    O N N 248 
ILE CB   C N S 249 
ILE CG1  C N N 250 
ILE CG2  C N N 251 
ILE CD1  C N N 252 
ILE OXT  O N N 253 
ILE H    H N N 254 
ILE H2   H N N 255 
ILE HA   H N N 256 
ILE HB   H N N 257 
ILE HG12 H N N 258 
ILE HG13 H N N 259 
ILE HG21 H N N 260 
ILE HG22 H N N 261 
ILE HG23 H N N 262 
ILE HD11 H N N 263 
ILE HD12 H N N 264 
ILE HD13 H N N 265 
ILE HXT  H N N 266 
LEU N    N N N 267 
LEU CA   C N S 268 
LEU C    C N N 269 
LEU O    O N N 270 
LEU CB   C N N 271 
LEU CG   C N N 272 
LEU CD1  C N N 273 
LEU CD2  C N N 274 
LEU OXT  O N N 275 
LEU H    H N N 276 
LEU H2   H N N 277 
LEU HA   H N N 278 
LEU HB2  H N N 279 
LEU HB3  H N N 280 
LEU HG   H N N 281 
LEU HD11 H N N 282 
LEU HD12 H N N 283 
LEU HD13 H N N 284 
LEU HD21 H N N 285 
LEU HD22 H N N 286 
LEU HD23 H N N 287 
LEU HXT  H N N 288 
LYS N    N N N 289 
LYS CA   C N S 290 
LYS C    C N N 291 
LYS O    O N N 292 
LYS CB   C N N 293 
LYS CG   C N N 294 
LYS CD   C N N 295 
LYS CE   C N N 296 
LYS NZ   N N N 297 
LYS OXT  O N N 298 
LYS H    H N N 299 
LYS H2   H N N 300 
LYS HA   H N N 301 
LYS HB2  H N N 302 
LYS HB3  H N N 303 
LYS HG2  H N N 304 
LYS HG3  H N N 305 
LYS HD2  H N N 306 
LYS HD3  H N N 307 
LYS HE2  H N N 308 
LYS HE3  H N N 309 
LYS HZ1  H N N 310 
LYS HZ2  H N N 311 
LYS HZ3  H N N 312 
LYS HXT  H N N 313 
MET N    N N N 314 
MET CA   C N S 315 
MET C    C N N 316 
MET O    O N N 317 
MET CB   C N N 318 
MET CG   C N N 319 
MET SD   S N N 320 
MET CE   C N N 321 
MET OXT  O N N 322 
MET H    H N N 323 
MET H2   H N N 324 
MET HA   H N N 325 
MET HB2  H N N 326 
MET HB3  H N N 327 
MET HG2  H N N 328 
MET HG3  H N N 329 
MET HE1  H N N 330 
MET HE2  H N N 331 
MET HE3  H N N 332 
MET HXT  H N N 333 
PHE N    N N N 334 
PHE CA   C N S 335 
PHE C    C N N 336 
PHE O    O N N 337 
PHE CB   C N N 338 
PHE CG   C Y N 339 
PHE CD1  C Y N 340 
PHE CD2  C Y N 341 
PHE CE1  C Y N 342 
PHE CE2  C Y N 343 
PHE CZ   C Y N 344 
PHE OXT  O N N 345 
PHE H    H N N 346 
PHE H2   H N N 347 
PHE HA   H N N 348 
PHE HB2  H N N 349 
PHE HB3  H N N 350 
PHE HD1  H N N 351 
PHE HD2  H N N 352 
PHE HE1  H N N 353 
PHE HE2  H N N 354 
PHE HZ   H N N 355 
PHE HXT  H N N 356 
PRO N    N N N 357 
PRO CA   C N S 358 
PRO C    C N N 359 
PRO O    O N N 360 
PRO CB   C N N 361 
PRO CG   C N N 362 
PRO CD   C N N 363 
PRO OXT  O N N 364 
PRO H    H N N 365 
PRO HA   H N N 366 
PRO HB2  H N N 367 
PRO HB3  H N N 368 
PRO HG2  H N N 369 
PRO HG3  H N N 370 
PRO HD2  H N N 371 
PRO HD3  H N N 372 
PRO HXT  H N N 373 
SER N    N N N 374 
SER CA   C N S 375 
SER C    C N N 376 
SER O    O N N 377 
SER CB   C N N 378 
SER OG   O N N 379 
SER OXT  O N N 380 
SER H    H N N 381 
SER H2   H N N 382 
SER HA   H N N 383 
SER HB2  H N N 384 
SER HB3  H N N 385 
SER HG   H N N 386 
SER HXT  H N N 387 
THR N    N N N 388 
THR CA   C N S 389 
THR C    C N N 390 
THR O    O N N 391 
THR CB   C N R 392 
THR OG1  O N N 393 
THR CG2  C N N 394 
THR OXT  O N N 395 
THR H    H N N 396 
THR H2   H N N 397 
THR HA   H N N 398 
THR HB   H N N 399 
THR HG1  H N N 400 
THR HG21 H N N 401 
THR HG22 H N N 402 
THR HG23 H N N 403 
THR HXT  H N N 404 
TRP N    N N N 405 
TRP CA   C N S 406 
TRP C    C N N 407 
TRP O    O N N 408 
TRP CB   C N N 409 
TRP CG   C Y N 410 
TRP CD1  C Y N 411 
TRP CD2  C Y N 412 
TRP NE1  N Y N 413 
TRP CE2  C Y N 414 
TRP CE3  C Y N 415 
TRP CZ2  C Y N 416 
TRP CZ3  C Y N 417 
TRP CH2  C Y N 418 
TRP OXT  O N N 419 
TRP H    H N N 420 
TRP H2   H N N 421 
TRP HA   H N N 422 
TRP HB2  H N N 423 
TRP HB3  H N N 424 
TRP HD1  H N N 425 
TRP HE1  H N N 426 
TRP HE3  H N N 427 
TRP HZ2  H N N 428 
TRP HZ3  H N N 429 
TRP HH2  H N N 430 
TRP HXT  H N N 431 
TYR N    N N N 432 
TYR CA   C N S 433 
TYR C    C N N 434 
TYR O    O N N 435 
TYR CB   C N N 436 
TYR CG   C Y N 437 
TYR CD1  C Y N 438 
TYR CD2  C Y N 439 
TYR CE1  C Y N 440 
TYR CE2  C Y N 441 
TYR CZ   C Y N 442 
TYR OH   O N N 443 
TYR OXT  O N N 444 
TYR H    H N N 445 
TYR H2   H N N 446 
TYR HA   H N N 447 
TYR HB2  H N N 448 
TYR HB3  H N N 449 
TYR HD1  H N N 450 
TYR HD2  H N N 451 
TYR HE1  H N N 452 
TYR HE2  H N N 453 
TYR HH   H N N 454 
TYR HXT  H N N 455 
VAL N    N N N 456 
VAL CA   C N S 457 
VAL C    C N N 458 
VAL O    O N N 459 
VAL CB   C N N 460 
VAL CG1  C N N 461 
VAL CG2  C N N 462 
VAL OXT  O N N 463 
VAL H    H N N 464 
VAL H2   H N N 465 
VAL HA   H N N 466 
VAL HB   H N N 467 
VAL HG11 H N N 468 
VAL HG12 H N N 469 
VAL HG13 H N N 470 
VAL HG21 H N N 471 
VAL HG22 H N N 472 
VAL HG23 H N N 473 
VAL HXT  H N N 474 
# 
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  
COA N1A C2A  sing Y N 70  
COA N1A C6A  doub Y N 71  
COA C2A N3A  doub Y N 72  
COA C2A H2A  sing N N 73  
COA N3A C4A  sing Y N 74  
COA C4A C5A  doub Y N 75  
COA C4A N9A  sing Y N 76  
COA C5A C6A  sing Y N 77  
COA C5A N7A  sing Y N 78  
COA C6A N6A  sing N N 79  
COA N6A H61A sing N N 80  
COA N6A H62A sing N N 81  
COA N7A C8A  doub Y N 82  
COA C8A N9A  sing Y N 83  
COA C8A H8A  sing N N 84  
COA N9A C1B  sing N N 85  
COA C1B C2B  sing N N 86  
COA C1B O4B  sing N N 87  
COA C1B H1B  sing N N 88  
COA C2B O2B  sing N N 89  
COA C2B C3B  sing N N 90  
COA C2B H2B  sing N N 91  
COA O2B HO2A sing N N 92  
COA C3B O3B  sing N N 93  
COA C3B C4B  sing N N 94  
COA C3B H3B  sing N N 95  
COA O3B P3B  sing N N 96  
COA P3B O7A  doub N N 97  
COA P3B O8A  sing N N 98  
COA P3B O9A  sing N N 99  
COA O8A HOA8 sing N N 100 
COA O9A HOA9 sing N N 101 
COA C4B O4B  sing N N 102 
COA C4B C5B  sing N N 103 
COA C4B H4B  sing N N 104 
COA C5B O5B  sing N N 105 
COA C5B H51A sing N N 106 
COA C5B H52A sing N N 107 
COA O5B P1A  sing N N 108 
COA P1A O1A  doub N N 109 
COA P1A O2A  sing N N 110 
COA P1A O3A  sing N N 111 
COA O2A HOA2 sing N N 112 
COA O3A P2A  sing N N 113 
COA P2A O4A  doub N N 114 
COA P2A O5A  sing N N 115 
COA P2A O6A  sing N N 116 
COA O5A HOA5 sing N N 117 
COA O6A CCP  sing N N 118 
COA CBP CCP  sing N N 119 
COA CBP CDP  sing N N 120 
COA CBP CEP  sing N N 121 
COA CBP CAP  sing N N 122 
COA CCP H121 sing N N 123 
COA CCP H122 sing N N 124 
COA CDP H131 sing N N 125 
COA CDP H132 sing N N 126 
COA CDP H133 sing N N 127 
COA CEP H141 sing N N 128 
COA CEP H142 sing N N 129 
COA CEP H143 sing N N 130 
COA CAP OAP  sing N N 131 
COA CAP C9P  sing N N 132 
COA CAP H10  sing N N 133 
COA OAP HO1  sing N N 134 
COA C9P O9P  doub N N 135 
COA C9P N8P  sing N N 136 
COA N8P C7P  sing N N 137 
COA N8P HN8  sing N N 138 
COA C7P C6P  sing N N 139 
COA C7P H71  sing N N 140 
COA C7P H72  sing N N 141 
COA C6P C5P  sing N N 142 
COA C6P H61  sing N N 143 
COA C6P H62  sing N N 144 
COA C5P O5P  doub N N 145 
COA C5P N4P  sing N N 146 
COA N4P C3P  sing N N 147 
COA N4P HN4  sing N N 148 
COA C3P C2P  sing N N 149 
COA C3P H31  sing N N 150 
COA C3P H32  sing N N 151 
COA C2P S1P  sing N N 152 
COA C2P H21  sing N N 153 
COA C2P H22  sing N N 154 
COA S1P HS1  sing N N 155 
CYS N   CA   sing N N 156 
CYS N   H    sing N N 157 
CYS N   H2   sing N N 158 
CYS CA  C    sing N N 159 
CYS CA  CB   sing N N 160 
CYS CA  HA   sing N N 161 
CYS C   O    doub N N 162 
CYS C   OXT  sing N N 163 
CYS CB  SG   sing N N 164 
CYS CB  HB2  sing N N 165 
CYS CB  HB3  sing N N 166 
CYS SG  HG   sing N N 167 
CYS OXT HXT  sing N N 168 
GLN N   CA   sing N N 169 
GLN N   H    sing N N 170 
GLN N   H2   sing N N 171 
GLN CA  C    sing N N 172 
GLN CA  CB   sing N N 173 
GLN CA  HA   sing N N 174 
GLN C   O    doub N N 175 
GLN C   OXT  sing N N 176 
GLN CB  CG   sing N N 177 
GLN CB  HB2  sing N N 178 
GLN CB  HB3  sing N N 179 
GLN CG  CD   sing N N 180 
GLN CG  HG2  sing N N 181 
GLN CG  HG3  sing N N 182 
GLN CD  OE1  doub N N 183 
GLN CD  NE2  sing N N 184 
GLN NE2 HE21 sing N N 185 
GLN NE2 HE22 sing N N 186 
GLN OXT HXT  sing N N 187 
GLU N   CA   sing N N 188 
GLU N   H    sing N N 189 
GLU N   H2   sing N N 190 
GLU CA  C    sing N N 191 
GLU CA  CB   sing N N 192 
GLU CA  HA   sing N N 193 
GLU C   O    doub N N 194 
GLU C   OXT  sing N N 195 
GLU CB  CG   sing N N 196 
GLU CB  HB2  sing N N 197 
GLU CB  HB3  sing N N 198 
GLU CG  CD   sing N N 199 
GLU CG  HG2  sing N N 200 
GLU CG  HG3  sing N N 201 
GLU CD  OE1  doub N N 202 
GLU CD  OE2  sing N N 203 
GLU OE2 HE2  sing N N 204 
GLU OXT HXT  sing N N 205 
GLY N   CA   sing N N 206 
GLY N   H    sing N N 207 
GLY N   H2   sing N N 208 
GLY CA  C    sing N N 209 
GLY CA  HA2  sing N N 210 
GLY CA  HA3  sing N N 211 
GLY C   O    doub N N 212 
GLY C   OXT  sing N N 213 
GLY OXT HXT  sing N N 214 
HIS N   CA   sing N N 215 
HIS N   H    sing N N 216 
HIS N   H2   sing N N 217 
HIS CA  C    sing N N 218 
HIS CA  CB   sing N N 219 
HIS CA  HA   sing N N 220 
HIS C   O    doub N N 221 
HIS C   OXT  sing N N 222 
HIS CB  CG   sing N N 223 
HIS CB  HB2  sing N N 224 
HIS CB  HB3  sing N N 225 
HIS CG  ND1  sing Y N 226 
HIS CG  CD2  doub Y N 227 
HIS ND1 CE1  doub Y N 228 
HIS ND1 HD1  sing N N 229 
HIS CD2 NE2  sing Y N 230 
HIS CD2 HD2  sing N N 231 
HIS CE1 NE2  sing Y N 232 
HIS CE1 HE1  sing N N 233 
HIS NE2 HE2  sing N N 234 
HIS OXT HXT  sing N N 235 
HOH O   H1   sing N N 236 
HOH O   H2   sing N N 237 
ILE N   CA   sing N N 238 
ILE N   H    sing N N 239 
ILE N   H2   sing N N 240 
ILE CA  C    sing N N 241 
ILE CA  CB   sing N N 242 
ILE CA  HA   sing N N 243 
ILE C   O    doub N N 244 
ILE C   OXT  sing N N 245 
ILE CB  CG1  sing N N 246 
ILE CB  CG2  sing N N 247 
ILE CB  HB   sing N N 248 
ILE CG1 CD1  sing N N 249 
ILE CG1 HG12 sing N N 250 
ILE CG1 HG13 sing N N 251 
ILE CG2 HG21 sing N N 252 
ILE CG2 HG22 sing N N 253 
ILE CG2 HG23 sing N N 254 
ILE CD1 HD11 sing N N 255 
ILE CD1 HD12 sing N N 256 
ILE CD1 HD13 sing N N 257 
ILE OXT HXT  sing N N 258 
LEU N   CA   sing N N 259 
LEU N   H    sing N N 260 
LEU N   H2   sing N N 261 
LEU CA  C    sing N N 262 
LEU CA  CB   sing N N 263 
LEU CA  HA   sing N N 264 
LEU C   O    doub N N 265 
LEU C   OXT  sing N N 266 
LEU CB  CG   sing N N 267 
LEU CB  HB2  sing N N 268 
LEU CB  HB3  sing N N 269 
LEU CG  CD1  sing N N 270 
LEU CG  CD2  sing N N 271 
LEU CG  HG   sing N N 272 
LEU CD1 HD11 sing N N 273 
LEU CD1 HD12 sing N N 274 
LEU CD1 HD13 sing N N 275 
LEU CD2 HD21 sing N N 276 
LEU CD2 HD22 sing N N 277 
LEU CD2 HD23 sing N N 278 
LEU OXT HXT  sing N N 279 
LYS N   CA   sing N N 280 
LYS N   H    sing N N 281 
LYS N   H2   sing N N 282 
LYS CA  C    sing N N 283 
LYS CA  CB   sing N N 284 
LYS CA  HA   sing N N 285 
LYS C   O    doub N N 286 
LYS C   OXT  sing N N 287 
LYS CB  CG   sing N N 288 
LYS CB  HB2  sing N N 289 
LYS CB  HB3  sing N N 290 
LYS CG  CD   sing N N 291 
LYS CG  HG2  sing N N 292 
LYS CG  HG3  sing N N 293 
LYS CD  CE   sing N N 294 
LYS CD  HD2  sing N N 295 
LYS CD  HD3  sing N N 296 
LYS CE  NZ   sing N N 297 
LYS CE  HE2  sing N N 298 
LYS CE  HE3  sing N N 299 
LYS NZ  HZ1  sing N N 300 
LYS NZ  HZ2  sing N N 301 
LYS NZ  HZ3  sing N N 302 
LYS OXT HXT  sing N N 303 
MET N   CA   sing N N 304 
MET N   H    sing N N 305 
MET N   H2   sing N N 306 
MET CA  C    sing N N 307 
MET CA  CB   sing N N 308 
MET CA  HA   sing N N 309 
MET C   O    doub N N 310 
MET C   OXT  sing N N 311 
MET CB  CG   sing N N 312 
MET CB  HB2  sing N N 313 
MET CB  HB3  sing N N 314 
MET CG  SD   sing N N 315 
MET CG  HG2  sing N N 316 
MET CG  HG3  sing N N 317 
MET SD  CE   sing N N 318 
MET CE  HE1  sing N N 319 
MET CE  HE2  sing N N 320 
MET CE  HE3  sing N N 321 
MET OXT HXT  sing N N 322 
PHE N   CA   sing N N 323 
PHE N   H    sing N N 324 
PHE N   H2   sing N N 325 
PHE CA  C    sing N N 326 
PHE CA  CB   sing N N 327 
PHE CA  HA   sing N N 328 
PHE C   O    doub N N 329 
PHE C   OXT  sing N N 330 
PHE CB  CG   sing N N 331 
PHE CB  HB2  sing N N 332 
PHE CB  HB3  sing N N 333 
PHE CG  CD1  doub Y N 334 
PHE CG  CD2  sing Y N 335 
PHE CD1 CE1  sing Y N 336 
PHE CD1 HD1  sing N N 337 
PHE CD2 CE2  doub Y N 338 
PHE CD2 HD2  sing N N 339 
PHE CE1 CZ   doub Y N 340 
PHE CE1 HE1  sing N N 341 
PHE CE2 CZ   sing Y N 342 
PHE CE2 HE2  sing N N 343 
PHE CZ  HZ   sing N N 344 
PHE OXT HXT  sing N N 345 
PRO N   CA   sing N N 346 
PRO N   CD   sing N N 347 
PRO N   H    sing N N 348 
PRO CA  C    sing N N 349 
PRO CA  CB   sing N N 350 
PRO CA  HA   sing N N 351 
PRO C   O    doub N N 352 
PRO C   OXT  sing N N 353 
PRO CB  CG   sing N N 354 
PRO CB  HB2  sing N N 355 
PRO CB  HB3  sing N N 356 
PRO CG  CD   sing N N 357 
PRO CG  HG2  sing N N 358 
PRO CG  HG3  sing N N 359 
PRO CD  HD2  sing N N 360 
PRO CD  HD3  sing N N 361 
PRO OXT HXT  sing N N 362 
SER N   CA   sing N N 363 
SER N   H    sing N N 364 
SER N   H2   sing N N 365 
SER CA  C    sing N N 366 
SER CA  CB   sing N N 367 
SER CA  HA   sing N N 368 
SER C   O    doub N N 369 
SER C   OXT  sing N N 370 
SER CB  OG   sing N N 371 
SER CB  HB2  sing N N 372 
SER CB  HB3  sing N N 373 
SER OG  HG   sing N N 374 
SER OXT HXT  sing N N 375 
THR N   CA   sing N N 376 
THR N   H    sing N N 377 
THR N   H2   sing N N 378 
THR CA  C    sing N N 379 
THR CA  CB   sing N N 380 
THR CA  HA   sing N N 381 
THR C   O    doub N N 382 
THR C   OXT  sing N N 383 
THR CB  OG1  sing N N 384 
THR CB  CG2  sing N N 385 
THR CB  HB   sing N N 386 
THR OG1 HG1  sing N N 387 
THR CG2 HG21 sing N N 388 
THR CG2 HG22 sing N N 389 
THR CG2 HG23 sing N N 390 
THR OXT HXT  sing N N 391 
TRP N   CA   sing N N 392 
TRP N   H    sing N N 393 
TRP N   H2   sing N N 394 
TRP CA  C    sing N N 395 
TRP CA  CB   sing N N 396 
TRP CA  HA   sing N N 397 
TRP C   O    doub N N 398 
TRP C   OXT  sing N N 399 
TRP CB  CG   sing N N 400 
TRP CB  HB2  sing N N 401 
TRP CB  HB3  sing N N 402 
TRP CG  CD1  doub Y N 403 
TRP CG  CD2  sing Y N 404 
TRP CD1 NE1  sing Y N 405 
TRP CD1 HD1  sing N N 406 
TRP CD2 CE2  doub Y N 407 
TRP CD2 CE3  sing Y N 408 
TRP NE1 CE2  sing Y N 409 
TRP NE1 HE1  sing N N 410 
TRP CE2 CZ2  sing Y N 411 
TRP CE3 CZ3  doub Y N 412 
TRP CE3 HE3  sing N N 413 
TRP CZ2 CH2  doub Y N 414 
TRP CZ2 HZ2  sing N N 415 
TRP CZ3 CH2  sing Y N 416 
TRP CZ3 HZ3  sing N N 417 
TRP CH2 HH2  sing N N 418 
TRP OXT HXT  sing N N 419 
TYR N   CA   sing N N 420 
TYR N   H    sing N N 421 
TYR N   H2   sing N N 422 
TYR CA  C    sing N N 423 
TYR CA  CB   sing N N 424 
TYR CA  HA   sing N N 425 
TYR C   O    doub N N 426 
TYR C   OXT  sing N N 427 
TYR CB  CG   sing N N 428 
TYR CB  HB2  sing N N 429 
TYR CB  HB3  sing N N 430 
TYR CG  CD1  doub Y N 431 
TYR CG  CD2  sing Y N 432 
TYR CD1 CE1  sing Y N 433 
TYR CD1 HD1  sing N N 434 
TYR CD2 CE2  doub Y N 435 
TYR CD2 HD2  sing N N 436 
TYR CE1 CZ   doub Y N 437 
TYR CE1 HE1  sing N N 438 
TYR CE2 CZ   sing Y N 439 
TYR CE2 HE2  sing N N 440 
TYR CZ  OH   sing N N 441 
TYR OH  HH   sing N N 442 
TYR OXT HXT  sing N N 443 
VAL N   CA   sing N N 444 
VAL N   H    sing N N 445 
VAL N   H2   sing N N 446 
VAL CA  C    sing N N 447 
VAL CA  CB   sing N N 448 
VAL CA  HA   sing N N 449 
VAL C   O    doub N N 450 
VAL C   OXT  sing N N 451 
VAL CB  CG1  sing N N 452 
VAL CB  CG2  sing N N 453 
VAL CB  HB   sing N N 454 
VAL CG1 HG11 sing N N 455 
VAL CG1 HG12 sing N N 456 
VAL CG1 HG13 sing N N 457 
VAL CG2 HG21 sing N N 458 
VAL CG2 HG22 sing N N 459 
VAL CG2 HG23 sing N N 460 
VAL OXT HXT  sing N N 461 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           75N93022C00035 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2CNT 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 32 2 1' 
_space_group.name_Hall        
;P 32 2"
;
_space_group.IT_number        154 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9MTO 
_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]   0.024120 
_atom_sites.fract_transf_matrix[1][2]   0.013925 
_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]   0.027851 
_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]   0.003070 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLN A 1 1   ? 14.46100 -14.48100 -64.08700 1.000 51.36116  ? -1  GLN A N   1 
ATOM   2    C CA  . GLN A 1 1   ? 15.91300 -14.41800 -64.13100 1.000 58.44648  ? -1  GLN A CA  1 
ATOM   3    C C   . GLN A 1 1   ? 16.40300 -13.10200 -63.58500 1.000 54.70218  ? -1  GLN A C   1 
ATOM   4    O O   . GLN A 1 1   ? 17.60200 -12.91500 -63.37600 1.000 68.01730  ? -1  GLN A O   1 
ATOM   5    C CB  . GLN A 1 1   ? 16.41500 -14.58900 -65.55500 1.000 72.96321  ? -1  GLN A CB  1 
ATOM   6    C CG  . GLN A 1 1   ? 15.90500 -15.85600 -66.22000 1.000 80.77161  ? -1  GLN A CG  1 
ATOM   7    C CD  . GLN A 1 1   ? 16.50600 -17.11400 -65.62900 1.000 91.46187  ? -1  GLN A CD  1 
ATOM   8    O OE1 . GLN A 1 1   ? 17.73100 -17.28000 -65.57700 1.000 100.84038 ? -1  GLN A OE1 1 
ATOM   9    N NE2 . GLN A 1 1   ? 15.63900 -18.02300 -65.19500 1.000 92.76495  ? -1  GLN A NE2 1 
ATOM   10   N N   . SER A 1 2   ? 15.48300 -12.17500 -63.36400 1.000 41.99300  ? 0   SER A N   1 
ATOM   11   C CA  . SER A 1 2   ? 15.86900 -10.92500 -62.72200 1.000 39.18359  ? 0   SER A CA  1 
ATOM   12   C C   . SER A 1 2   ? 16.41500 -11.22200 -61.31800 1.000 46.25833  ? 0   SER A C   1 
ATOM   13   O O   . SER A 1 2   ? 16.02900 -12.20700 -60.67200 1.000 36.53726  ? 0   SER A O   1 
ATOM   14   C CB  . SER A 1 2   ? 14.67000 -9.96600  -62.62800 1.000 37.51905  ? 0   SER A CB  1 
ATOM   15   O OG  . SER A 1 2   ? 14.10700 -9.99300  -61.34000 1.000 54.15075  ? 0   SER A OG  1 
ATOM   16   N N   . MET A 1 3   ? 17.38700 -10.42500 -60.88300 1.000 36.18828  ? 1   MET A N   1 
ATOM   17   C CA  . MET A 1 3   ? 17.87500 -10.48800 -59.50900 1.000 33.60018  ? 1   MET A CA  1 
ATOM   18   C C   . MET A 1 3   ? 18.16100 -9.06500  -59.06800 1.000 32.78747  ? 1   MET A C   1 
ATOM   19   O O   . MET A 1 3   ? 18.69200 -8.26500  -59.83700 1.000 35.51156  ? 1   MET A O   1 
ATOM   20   C CB  . MET A 1 3   ? 19.15900 -11.32100 -59.34100 1.000 35.61797  ? 1   MET A CB  1 
ATOM   21   C CG  . MET A 1 3   ? 19.26500 -12.57700 -60.23200 1.000 45.36375  ? 1   MET A CG  1 
ATOM   22   S SD  . MET A 1 3   ? 20.14400 -14.00000 -59.48300 1.000 94.33616  ? 1   MET A SD  1 
ATOM   23   C CE  . MET A 1 3   ? 21.83300 -13.88200 -60.11600 1.000 49.55650  ? 1   MET A CE  1 
ATOM   24   N N   . LYS A 1 4   ? 17.77600 -8.74200  -57.85000 1.000 29.53859  ? 2   LYS A N   1 
ATOM   25   C CA  . LYS A 1 4   ? 17.90700 -7.39500  -57.33200 1.000 28.67976  ? 2   LYS A CA  1 
ATOM   26   C C   . LYS A 1 4   ? 18.67400 -7.50300  -56.02400 1.000 27.30773  ? 2   LYS A C   1 
ATOM   27   O O   . LYS A 1 4   ? 18.36900 -8.37100  -55.20000 1.000 25.57476  ? 2   LYS A O   1 
ATOM   28   C CB  . LYS A 1 4   ? 16.50900 -6.79200  -57.12400 1.000 28.29220  ? 2   LYS A CB  1 
ATOM   29   C CG  . LYS A 1 4   ? 16.45200 -5.39000  -56.61000 1.000 34.78238  ? 2   LYS A CG  1 
ATOM   30   C CD  . LYS A 1 4   ? 15.00200 -4.81500  -56.73300 1.000 39.58454  ? 2   LYS A CD  1 
ATOM   31   C CE  . LYS A 1 4   ? 14.92000 -3.40100  -56.14900 1.000 51.94354  ? 2   LYS A CE  1 
ATOM   32   N NZ  . LYS A 1 4   ? 13.53500 -2.80000  -56.12300 1.000 43.97936  ? 2   LYS A NZ  1 
ATOM   33   N N   . ILE A 1 5   ? 19.68300 -6.65700  -55.83600 1.000 28.63854  ? 3   ILE A N   1 
ATOM   34   C CA  . ILE A 1 5   ? 20.31600 -6.55100  -54.52700 1.000 27.51094  ? 3   ILE A CA  1 
ATOM   35   C C   . ILE A 1 5   ? 20.20100 -5.10200  -54.06300 1.000 26.78443  ? 3   ILE A C   1 
ATOM   36   O O   . ILE A 1 5   ? 20.41300 -4.17700  -54.85400 1.000 28.82508  ? 3   ILE A O   1 
ATOM   37   C CB  . ILE A 1 5   ? 21.77300 -7.02600  -54.55000 1.000 30.32005  ? 3   ILE A CB  1 
ATOM   38   C CG1 . ILE A 1 5   ? 21.82900 -8.47500  -55.05400 1.000 31.48671  ? 3   ILE A CG1 1 
ATOM   39   C CG2 . ILE A 1 5   ? 22.37100 -6.83900  -53.13700 1.000 30.25470  ? 3   ILE A CG2 1 
ATOM   40   C CD1 . ILE A 1 5   ? 23.20300 -8.99200  -55.40600 1.000 35.24533  ? 3   ILE A CD1 1 
ATOM   41   N N   . ARG A 1 6   ? 19.78600 -4.90400  -52.81900 1.000 24.33519  ? 4   ARG A N   1 
ATOM   42   C CA  . ARG A 1 6   ? 19.63000 -3.53400  -52.34700 1.000 23.88895  ? 4   ARG A CA  1 
ATOM   43   C C   . ARG A 1 6   ? 19.76000 -3.51600  -50.83300 1.000 22.34469  ? 4   ARG A C   1 
ATOM   44   O O   . ARG A 1 6   ? 19.62200 -4.53200  -50.15800 1.000 21.32843  ? 4   ARG A O   1 
ATOM   45   C CB  . ARG A 1 6   ? 18.28500 -2.90900  -52.77800 1.000 22.84463  ? 4   ARG A CB  1 
ATOM   46   C CG  . ARG A 1 6   ? 16.99800 -3.69500  -52.28700 1.000 23.93613  ? 4   ARG A CG  1 
ATOM   47   C CD  . ARG A 1 6   ? 15.69900 -2.86900  -52.35300 1.000 27.45391  ? 4   ARG A CD  1 
ATOM   48   N NE  . ARG A 1 6   ? 14.54700 -3.72400  -52.05000 1.000 22.97163  ? 4   ARG A NE  1 
ATOM   49   C CZ  . ARG A 1 6   ? 14.20000 -4.05800  -50.80600 1.000 24.19807  ? 4   ARG A CZ  1 
ATOM   50   N NH1 . ARG A 1 6   ? 14.86000 -3.59100  -49.75600 1.000 21.85309  ? 4   ARG A NH1 1 
ATOM   51   N NH2 . ARG A 1 6   ? 13.16700 -4.89200  -50.61600 1.000 24.69891  ? 4   ARG A NH2 1 
ATOM   52   N N   . ASN A 1 7   ? 19.99400 -2.32300  -50.30200 1.000 25.03797  ? 5   ASN A N   1 
ATOM   53   C CA  . ASN A 1 7   ? 19.91200 -2.18100  -48.86600 1.000 21.38986  ? 5   ASN A CA  1 
ATOM   54   C C   . ASN A 1 7   ? 18.50600 -2.50400  -48.39300 1.000 20.41092  ? 5   ASN A C   1 
ATOM   55   O O   . ASN A 1 7   ? 17.50600 -2.28700  -49.11500 1.000 22.90908  ? 5   ASN A O   1 
ATOM   56   C CB  . ASN A 1 7   ? 20.33300 -0.78300  -48.44300 1.000 27.05428  ? 5   ASN A CB  1 
ATOM   57   C CG  . ASN A 1 7   ? 21.79600 -0.59900  -48.58200 1.000 40.31769  ? 5   ASN A CG  1 
ATOM   58   O OD1 . ASN A 1 7   ? 22.25800 -0.03900  -49.56900 1.000 38.87041  ? 5   ASN A OD1 1 
ATOM   59   N ND2 . ASN A 1 7   ? 22.56500 -1.12700  -47.61100 1.000 38.67257  ? 5   ASN A ND2 1 
ATOM   60   N N   . TRP A 1 8   ? 18.45600 -3.11100  -47.20800 1.000 20.38452  ? 6   TRP A N   1 
ATOM   61   C CA  . TRP A 1 8   ? 17.20200 -3.49400  -46.59400 1.000 20.86393  ? 6   TRP A CA  1 
ATOM   62   C C   . TRP A 1 8   ? 16.53900 -2.26400  -45.99500 1.000 20.07171  ? 6   TRP A C   1 
ATOM   63   O O   . TRP A 1 8   ? 17.15700 -1.20700  -45.82400 1.000 22.73722  ? 6   TRP A O   1 
ATOM   64   C CB  . TRP A 1 8   ? 17.39200 -4.58900  -45.53000 1.000 19.72428  ? 6   TRP A CB  1 
ATOM   65   C CG  . TRP A 1 8   ? 18.05500 -4.21500  -44.22400 1.000 19.04681  ? 6   TRP A CG  1 
ATOM   66   C CD1 . TRP A 1 8   ? 18.71800 -3.04800  -43.90300 1.000 19.04673  ? 6   TRP A CD1 1 
ATOM   67   C CD2 . TRP A 1 8   ? 18.09600 -5.04000  -43.06300 1.000 19.39619  ? 6   TRP A CD2 1 
ATOM   68   N NE1 . TRP A 1 8   ? 19.18900 -3.12600  -42.58400 1.000 21.56630  ? 6   TRP A NE1 1 
ATOM   69   C CE2 . TRP A 1 8   ? 18.80600 -4.33700  -42.06000 1.000 20.71021  ? 6   TRP A CE2 1 
ATOM   70   C CE3 . TRP A 1 8   ? 17.57300 -6.29900  -42.76500 1.000 31.46757  ? 6   TRP A CE3 1 
ATOM   71   C CZ2 . TRP A 1 8   ? 19.01300 -4.87900  -40.77400 1.000 32.54520  ? 6   TRP A CZ2 1 
ATOM   72   C CZ3 . TRP A 1 8   ? 17.79200 -6.83700  -41.51500 1.000 26.63343  ? 6   TRP A CZ3 1 
ATOM   73   C CH2 . TRP A 1 8   ? 18.50300 -6.12100  -40.52500 1.000 36.90799  ? 6   TRP A CH2 1 
ATOM   74   N N   . ILE A 1 9   ? 15.23800 -2.40700  -45.74900 1.000 26.63651  ? 7   ILE A N   1 
ATOM   75   C CA  . ILE A 1 9   ? 14.40400 -1.33500  -45.21600 1.000 26.34899  ? 7   ILE A CA  1 
ATOM   76   C C   . ILE A 1 9   ? 13.43800 -1.98500  -44.22700 1.000 28.78771  ? 7   ILE A C   1 
ATOM   77   O O   . ILE A 1 9   ? 13.19900 -3.19200  -44.26100 1.000 30.43458  ? 7   ILE A O   1 
ATOM   78   C CB  . ILE A 1 9   ? 13.63200 -0.60200  -46.34100 1.000 29.86249  ? 7   ILE A CB  1 
ATOM   79   C CG1 . ILE A 1 9   ? 12.74300 -1.56800  -47.10400 1.000 25.26238  ? 7   ILE A CG1 1 
ATOM   80   C CG2 . ILE A 1 9   ? 14.59500 0.01300   -47.32400 1.000 28.38748  ? 7   ILE A CG2 1 
ATOM   81   C CD1 . ILE A 1 9   ? 11.99300 -0.97100  -48.28200 1.000 41.89437  ? 7   ILE A CD1 1 
ATOM   82   N N   . LYS A 1 10  ? 12.82900 -1.17100  -43.37100 1.000 34.21270  ? 8   LYS A N   1 
ATOM   83   C CA  . LYS A 1 10  ? 11.98100 -1.76100  -42.33800 1.000 37.21731  ? 8   LYS A CA  1 
ATOM   84   C C   . LYS A 1 10  ? 10.88500 -2.65900  -42.92000 1.000 33.48695  ? 8   LYS A C   1 
ATOM   85   O O   . LYS A 1 10  ? 10.56900 -3.70200  -42.32800 1.000 35.03207  ? 8   LYS A O   1 
ATOM   86   C CB  . LYS A 1 10  ? 11.38500 -0.66400  -41.48200 1.000 32.80493  ? 8   LYS A CB  1 
ATOM   87   C CG  . LYS A 1 10  ? 10.25000 -1.15900  -40.62000 1.000 39.12750  ? 8   LYS A CG  1 
ATOM   88   C CD  . LYS A 1 10  ? 10.65700 -1.29200  -39.17500 1.000 61.34862  ? 8   LYS A CD  1 
ATOM   89   C CE  . LYS A 1 10  ? 10.70600 0.06800   -38.46600 1.000 58.28214  ? 8   LYS A CE  1 
ATOM   90   N NZ  . LYS A 1 10  ? 10.63500 -0.03700  -36.96700 1.000 60.76908  ? 8   LYS A NZ  1 
ATOM   91   N N   . ASP A 1 11  ? 10.35300 -2.33800  -44.10200 1.000 32.49907  ? 9   ASP A N   1 
ATOM   92   C CA  . ASP A 1 11  ? 9.28700  -3.16800  -44.67700 1.000 35.00601  ? 9   ASP A CA  1 
ATOM   93   C C   . ASP A 1 11  ? 9.75900  -4.59600  -44.97000 1.000 37.85247  ? 9   ASP A C   1 
ATOM   94   O O   . ASP A 1 11  ? 8.92400  -5.50500  -45.08700 1.000 29.69237  ? 9   ASP A O   1 
ATOM   95   C CB  . ASP A 1 11  ? 8.72600  -2.54200  -45.96600 1.000 42.07154  ? 9   ASP A CB  1 
ATOM   96   C CG  . ASP A 1 11  ? 7.51700  -1.61800  -45.71800 1.000 51.57018  ? 9   ASP A CG  1 
ATOM   97   O OD1 . ASP A 1 11  ? 7.00500  -1.55500  -44.57800 1.000 55.96481  ? 9   ASP A OD1 1 
ATOM   98   O OD2 . ASP A 1 11  ? 7.06300  -0.94300  -46.66900 1.000 45.50929  ? 9   ASP A OD2 1 
ATOM   99   N N   . ASP A 1 12  ? 11.07400 -4.81500  -45.08100 1.000 27.57595  ? 10  ASP A N   1 
ATOM   100  C CA  . ASP A 1 12  ? 11.62100 -6.14000  -45.37200 1.000 21.74992  ? 10  ASP A CA  1 
ATOM   101  C C   . ASP A 1 12  ? 11.60400 -7.09100  -44.18600 1.000 29.06523  ? 10  ASP A C   1 
ATOM   102  O O   . ASP A 1 12  ? 11.83900 -8.29200  -44.37900 1.000 26.27127  ? 10  ASP A O   1 
ATOM   103  C CB  . ASP A 1 12  ? 13.08400 -6.07000  -45.81700 1.000 19.73480  ? 10  ASP A CB  1 
ATOM   104  C CG  . ASP A 1 12  ? 13.24700 -5.34300  -47.11700 1.000 25.92905  ? 10  ASP A CG  1 
ATOM   105  O OD1 . ASP A 1 12  ? 12.33000 -5.41600  -47.95500 1.000 28.51524  ? 10  ASP A OD1 1 
ATOM   106  O OD2 . ASP A 1 12  ? 14.29700 -4.68900  -47.31000 1.000 25.43984  ? 10  ASP A OD2 1 
ATOM   107  N N   . VAL A 1 13  ? 11.42500 -6.58000  -42.96200 1.000 32.42627  ? 11  VAL A N   1 
ATOM   108  C CA  . VAL A 1 13  ? 11.74700 -7.38300  -41.77500 1.000 26.10635  ? 11  VAL A CA  1 
ATOM   109  C C   . VAL A 1 13  ? 10.88300 -8.63200  -41.68700 1.000 26.64917  ? 11  VAL A C   1 
ATOM   110  O O   . VAL A 1 13  ? 11.40300 -9.68000  -41.26900 1.000 29.68706  ? 11  VAL A O   1 
ATOM   111  C CB  . VAL A 1 13  ? 11.69100 -6.51500  -40.51100 1.000 35.06015  ? 11  VAL A CB  1 
ATOM   112  C CG1 . VAL A 1 13  ? 11.71500 -7.41000  -39.29100 1.000 32.09066  ? 11  VAL A CG1 1 
ATOM   113  C CG2 . VAL A 1 13  ? 12.91800 -5.60900  -40.45300 1.000 32.12538  ? 11  VAL A CG2 1 
ATOM   114  N N   . PRO A 1 14  ? 9.61000  -8.62700  -42.08300 1.000 29.55113  ? 12  PRO A N   1 
ATOM   115  C CA  . PRO A 1 14  ? 8.84900  -9.88000  -41.95700 1.000 37.23684  ? 12  PRO A CA  1 
ATOM   116  C C   . PRO A 1 14  ? 9.39100  -10.98100 -42.84000 1.000 27.71919  ? 12  PRO A C   1 
ATOM   117  O O   . PRO A 1 14  ? 9.49700  -12.13300 -42.39200 1.000 25.84648  ? 12  PRO A O   1 
ATOM   118  C CB  . PRO A 1 14  ? 7.42800  -9.45700  -42.34800 1.000 41.41272  ? 12  PRO A CB  1 
ATOM   119  C CG  . PRO A 1 14  ? 7.35200  -8.10100  -41.88500 1.000 39.44755  ? 12  PRO A CG  1 
ATOM   120  C CD  . PRO A 1 14  ? 8.66300  -7.49100  -42.25800 1.000 32.96548  ? 12  PRO A CD  1 
ATOM   121  N N   . GLN A 1 15  ? 9.74200  -10.66700 -44.08500 1.000 27.07308  ? 13  GLN A N   1 
ATOM   122  C CA  . GLN A 1 15  ? 10.33200 -11.68800 -44.93900 1.000 24.58847  ? 13  GLN A CA  1 
ATOM   123  C C   . GLN A 1 15  ? 11.72200 -12.08700 -44.47700 1.000 24.13207  ? 13  GLN A C   1 
ATOM   124  O O   . GLN A 1 15  ? 12.10800 -13.25300 -44.59300 1.000 22.22760  ? 13  GLN A O   1 
ATOM   125  C CB  . GLN A 1 15  ? 10.36700 -11.18700 -46.38100 1.000 23.50617  ? 13  GLN A CB  1 
ATOM   126  C CG  . GLN A 1 15  ? 9.03700  -11.27500 -47.10400 1.000 34.60839  ? 13  GLN A CG  1 
ATOM   127  C CD  . GLN A 1 15  ? 9.19100  -10.86000 -48.54300 1.000 32.13617  ? 13  GLN A CD  1 
ATOM   128  O OE1 . GLN A 1 15  ? 9.48500  -11.67800 -49.42200 1.000 34.60319  ? 13  GLN A OE1 1 
ATOM   129  N NE2 . GLN A 1 15  ? 9.04100  -9.57400  -48.79400 1.000 47.72100  ? 13  GLN A NE2 1 
ATOM   130  N N   . VAL A 1 16  ? 12.53900 -11.13200 -44.01300 1.000 23.61680  ? 14  VAL A N   1 
ATOM   131  C CA  . VAL A 1 16  ? 13.85100 -11.48000 -43.48000 1.000 16.80233  ? 14  VAL A CA  1 
ATOM   132  C C   . VAL A 1 16  ? 13.71200 -12.44900 -42.31000 1.000 18.54126  ? 14  VAL A C   1 
ATOM   133  O O   . VAL A 1 16  ? 14.46300 -13.42900 -42.18400 1.000 21.67711  ? 14  VAL A O   1 
ATOM   134  C CB  . VAL A 1 16  ? 14.58100 -10.18700 -43.09200 1.000 24.03438  ? 14  VAL A CB  1 
ATOM   135  C CG1 . VAL A 1 16  ? 15.86100 -10.51900 -42.25800 1.000 21.50482  ? 14  VAL A CG1 1 
ATOM   136  C CG2 . VAL A 1 16  ? 14.94800 -9.42300  -44.40700 1.000 23.09975  ? 14  VAL A CG2 1 
ATOM   137  N N   . SER A 1 17  ? 12.75700 -12.16700 -41.43600 1.000 20.91419  ? 15  SER A N   1 
ATOM   138  C CA  A SER A 1 17  ? 12.54300 -13.04500 -40.29300 0.500 20.77246  ? 15  SER A CA  1 
ATOM   139  C CA  B SER A 1 17  ? 12.49300 -13.02500 -40.28800 0.500 20.80980  ? 15  SER A CA  1 
ATOM   140  C C   . SER A 1 17  ? 12.03800 -14.40500 -40.73800 1.000 23.08482  ? 15  SER A C   1 
ATOM   141  O O   . SER A 1 17  ? 12.38700 -15.41200 -40.13000 1.000 23.56401  ? 15  SER A O   1 
ATOM   142  C CB  A SER A 1 17  ? 11.57600 -12.40300 -39.28800 0.500 25.53446  ? 15  SER A CB  1 
ATOM   143  C CB  B SER A 1 17  ? 11.44600 -12.35000 -39.39300 0.500 25.52557  ? 15  SER A CB  1 
ATOM   144  O OG  A SER A 1 17  ? 10.43000 -11.88700 -39.93000 0.500 33.44791  ? 15  SER A OG  1 
ATOM   145  O OG  B SER A 1 17  ? 10.96700 -13.20800 -38.38000 0.500 23.56908  ? 15  SER A OG  1 
ATOM   146  N N   . GLU A 1 18  ? 11.25300 -14.45800 -41.82300 1.000 24.15923  ? 16  GLU A N   1 
ATOM   147  C CA  . GLU A 1 18  ? 10.83200 -15.74600 -42.37100 1.000 22.93630  ? 16  GLU A CA  1 
ATOM   148  C C   . GLU A 1 18  ? 12.01300 -16.51900 -42.93500 1.000 21.02585  ? 16  GLU A C   1 
ATOM   149  O O   . GLU A 1 18  ? 12.09900 -17.74300 -42.75500 1.000 21.91687  ? 16  GLU A O   1 
ATOM   150  C CB  . GLU A 1 18  ? 9.76700  -15.52000 -43.43200 1.000 24.76249  ? 16  GLU A CB  1 
ATOM   151  C CG  . GLU A 1 18  ? 8.37800  -15.23400 -42.84100 1.000 30.74066  ? 16  GLU A CG  1 
ATOM   152  C CD  . GLU A 1 18  ? 7.44700  -14.65300 -43.86000 1.000 34.08696  ? 16  GLU A CD  1 
ATOM   153  O OE1 . GLU A 1 18  ? 7.89100  -14.53700 -45.02100 1.000 31.80301  ? 16  GLU A OE1 1 
ATOM   154  O OE2 . GLU A 1 18  ? 6.30100  -14.29400 -43.50700 1.000 32.11231  ? 16  GLU A OE2 1 
ATOM   155  N N   . ILE A 1 19  ? 12.92700 -15.83600 -43.64100 1.000 18.77005  ? 17  ILE A N   1 
ATOM   156  C CA  . ILE A 1 19  ? 14.15400 -16.50600 -44.10300 1.000 17.09876  ? 17  ILE A CA  1 
ATOM   157  C C   . ILE A 1 19  ? 14.94300 -17.07200 -42.93700 1.000 20.27723  ? 17  ILE A C   1 
ATOM   158  O O   . ILE A 1 19  ? 15.40900 -18.21100 -42.97000 1.000 16.69960  ? 17  ILE A O   1 
ATOM   159  C CB  . ILE A 1 19  ? 15.01800 -15.53700 -44.93400 1.000 15.76912  ? 17  ILE A CB  1 
ATOM   160  C CG1 . ILE A 1 19  ? 14.29600 -15.14500 -46.19600 1.000 18.39044  ? 17  ILE A CG1 1 
ATOM   161  C CG2 . ILE A 1 19  ? 16.43700 -16.14700 -45.13600 1.000 15.70753  ? 17  ILE A CG2 1 
ATOM   162  C CD1 . ILE A 1 19  ? 14.89400 -13.88200 -46.82600 1.000 17.56014  ? 17  ILE A CD1 1 
ATOM   163  N N   . ALA A 1 20  ? 15.11300 -16.27700 -41.88500 1.000 15.79707  ? 18  ALA A N   1 
ATOM   164  C CA  . ALA A 1 20  ? 15.74800 -16.76300 -40.66200 1.000 20.94008  ? 18  ALA A CA  1 
ATOM   165  C C   . ALA A 1 20  ? 15.06400 -18.01400 -40.09900 1.000 22.21063  ? 18  ALA A C   1 
ATOM   166  O O   . ALA A 1 20  ? 15.71700 -19.00300 -39.73800 1.000 20.25995  ? 18  ALA A O   1 
ATOM   167  C CB  . ALA A 1 20  ? 15.70100 -15.59600 -39.67100 1.000 20.91989  ? 18  ALA A CB  1 
ATOM   168  N N   . GLU A 1 21  ? 13.74900 -17.97900 -39.94800 1.000 20.18087  ? 19  GLU A N   1 
ATOM   169  C CA  . GLU A 1 21  ? 13.03700 -19.13700 -39.41700 1.000 22.92857  ? 19  GLU A CA  1 
ATOM   170  C C   . GLU A 1 21  ? 13.28700 -20.38200 -40.25900 1.000 24.15491  ? 19  GLU A C   1 
ATOM   171  O O   . GLU A 1 21  ? 13.37300 -21.49400 -39.72600 1.000 25.19140  ? 19  GLU A O   1 
ATOM   172  C CB  . GLU A 1 21  ? 11.53300 -18.86600 -39.36000 1.000 25.51543  ? 19  GLU A CB  1 
ATOM   173  C CG  . GLU A 1 21  ? 10.72900 -19.93000 -38.69200 1.000 31.19193  ? 19  GLU A CG  1 
ATOM   174  C CD  . GLU A 1 21  ? 9.25500  -19.56500 -38.72600 1.000 31.49892  ? 19  GLU A CD  1 
ATOM   175  O OE1 . GLU A 1 21  ? 8.90800  -18.63600 -39.50300 1.000 39.30684  ? 19  GLU A OE1 1 
ATOM   176  O OE2 . GLU A 1 21  ? 8.46800  -20.20800 -38.01800 1.000 34.59683  ? 19  GLU A OE2 1 
ATOM   177  N N   . ALA A 1 22  ? 13.37700 -20.20200 -41.58000 1.000 22.61623  ? 20  ALA A N   1 
ATOM   178  C CA  . ALA A 1 22  ? 13.53600 -21.30800 -42.51500 1.000 23.58649  ? 20  ALA A CA  1 
ATOM   179  C C   . ALA A 1 22  ? 14.97800 -21.81600 -42.51700 1.000 21.96059  ? 20  ALA A C   1 
ATOM   180  O O   . ALA A 1 22  ? 15.20100 -23.02500 -42.65400 1.000 23.52606  ? 20  ALA A O   1 
ATOM   181  C CB  . ALA A 1 22  ? 13.17400 -20.84100 -43.92100 1.000 23.35787  ? 20  ALA A CB  1 
ATOM   182  N N   . ALA A 1 23  ? 15.95500 -20.91200 -42.37800 1.000 24.17871  ? 21  ALA A N   1 
ATOM   183  C CA  . ALA A 1 23  ? 17.36600 -21.24900 -42.63700 1.000 20.21133  ? 21  ALA A CA  1 
ATOM   184  C C   . ALA A 1 23  ? 18.28500 -21.30600 -41.42300 1.000 18.02499  ? 21  ALA A C   1 
ATOM   185  O O   . ALA A 1 23  ? 19.20100 -22.15400 -41.40200 1.000 22.73786  ? 21  ALA A O   1 
ATOM   186  C CB  . ALA A 1 23  ? 17.98200 -20.25800 -43.63100 1.000 20.14329  ? 21  ALA A CB  1 
ATOM   187  N N   . MET A 1 24  ? 18.00700 -20.52000 -40.35600 1.000 25.70255  ? 22  MET A N   1 
ATOM   188  C CA  . MET A 1 24  ? 19.09100 -20.33000 -39.40200 1.000 26.57757  ? 22  MET A CA  1 
ATOM   189  C C   . MET A 1 24  ? 18.85700 -21.18500 -38.17300 1.000 20.67270  ? 22  MET A C   1 
ATOM   190  O O   . MET A 1 24  ? 17.77300 -21.12000 -37.61000 1.000 20.21415  ? 22  MET A O   1 
ATOM   191  C CB  . MET A 1 24  ? 19.11800 -18.86000 -39.01200 1.000 28.27142  ? 22  MET A CB  1 
ATOM   192  C CG  . MET A 1 24  ? 20.06000 -18.44200 -37.99000 1.000 28.10977  ? 22  MET A CG  1 
ATOM   193  S SD  . MET A 1 24  ? 19.62800 -16.76100 -37.40600 1.000 30.48799  ? 22  MET A SD  1 
ATOM   194  C CE  . MET A 1 24  ? 18.44500 -16.24200 -38.51400 1.000 41.59890  ? 22  MET A CE  1 
ATOM   195  N N   . PRO A 1 25  ? 19.82600 -21.94600 -37.65000 1.000 22.42588  ? 23  PRO A N   1 
ATOM   196  C CA  . PRO A 1 25  ? 19.55900 -22.64400 -36.38800 1.000 23.45088  ? 23  PRO A CA  1 
ATOM   197  C C   . PRO A 1 25  ? 19.35100 -21.59100 -35.30600 1.000 27.73952  ? 23  PRO A C   1 
ATOM   198  O O   . PRO A 1 25  ? 19.95700 -20.51700 -35.32800 1.000 26.92785  ? 23  PRO A O   1 
ATOM   199  C CB  . PRO A 1 25  ? 20.82200 -23.48100 -36.15100 1.000 28.48251  ? 23  PRO A CB  1 
ATOM   200  C CG  . PRO A 1 25  ? 21.91700 -22.75400 -36.93300 1.000 37.26356  ? 23  PRO A CG  1 
ATOM   201  C CD  . PRO A 1 25  ? 21.20500 -22.14900 -38.15000 1.000 27.33601  ? 23  PRO A CD  1 
ATOM   202  N N   . PHE A 1 26  ? 18.45100 -21.87600 -34.38200 1.000 29.08596  ? 24  PHE A N   1 
ATOM   203  C CA  . PHE A 1 26  ? 18.13100 -20.95700 -33.29800 1.000 30.00372  ? 24  PHE A CA  1 
ATOM   204  C C   . PHE A 1 26  ? 17.87200 -19.53500 -33.80000 1.000 28.50941  ? 24  PHE A C   1 
ATOM   205  O O   . PHE A 1 26  ? 18.58700 -18.59000 -33.43600 1.000 29.47390  ? 24  PHE A O   1 
ATOM   206  C CB  . PHE A 1 26  ? 19.22500 -20.99100 -32.23900 1.000 44.38896  ? 24  PHE A CB  1 
ATOM   207  C CG  . PHE A 1 26  ? 19.50600 -22.39000 -31.75300 1.000 36.57743  ? 24  PHE A CG  1 
ATOM   208  C CD1 . PHE A 1 26  ? 20.38500 -23.21300 -32.45300 1.000 43.36166  ? 24  PHE A CD1 1 
ATOM   209  C CD2 . PHE A 1 26  ? 18.82700 -22.91400 -30.66200 1.000 49.05474  ? 24  PHE A CD2 1 
ATOM   210  C CE1 . PHE A 1 26  ? 20.62900 -24.50800 -32.04700 1.000 45.93928  ? 24  PHE A CE1 1 
ATOM   211  C CE2 . PHE A 1 26  ? 19.06100 -24.21100 -30.24200 1.000 44.26012  ? 24  PHE A CE2 1 
ATOM   212  C CZ  . PHE A 1 26  ? 19.94800 -25.01200 -30.93300 1.000 38.37251  ? 24  PHE A CZ  1 
ATOM   213  N N   . PRO A 1 27  ? 16.84000 -19.34300 -34.60700 1.000 29.03934  ? 25  PRO A N   1 
ATOM   214  C CA  . PRO A 1 27  ? 16.72400 -18.10900 -35.38100 1.000 28.53677  ? 25  PRO A CA  1 
ATOM   215  C C   . PRO A 1 27  ? 16.35700 -16.88800 -34.55700 1.000 31.07398  ? 25  PRO A C   1 
ATOM   216  O O   . PRO A 1 27  ? 15.66100 -16.95700 -33.54200 1.000 35.45907  ? 25  PRO A O   1 
ATOM   217  C CB  . PRO A 1 27  ? 15.62400 -18.43700 -36.40200 1.000 25.90610  ? 25  PRO A CB  1 
ATOM   218  C CG  . PRO A 1 27  ? 14.81700 -19.45300 -35.74700 1.000 24.05913  ? 25  PRO A CG  1 
ATOM   219  C CD  . PRO A 1 27  ? 15.81400 -20.31900 -34.99700 1.000 27.32398  ? 25  PRO A CD  1 
ATOM   220  N N   . TRP A 1 28  ? 16.89600 -15.75300 -35.00400 1.000 33.27482  ? 26  TRP A N   1 
ATOM   221  C CA  . TRP A 1 28  ? 16.50400 -14.45200 -34.49800 1.000 36.12209  ? 26  TRP A CA  1 
ATOM   222  C C   . TRP A 1 28  ? 15.00200 -14.24000 -34.63200 1.000 34.07544  ? 26  TRP A C   1 
ATOM   223  O O   . TRP A 1 28  ? 14.40600 -14.58500 -35.65600 1.000 38.37756  ? 26  TRP A O   1 
ATOM   224  C CB  . TRP A 1 28  ? 17.21800 -13.37300 -35.29600 1.000 40.27371  ? 26  TRP A CB  1 
ATOM   225  C CG  . TRP A 1 28  ? 18.65800 -13.20400 -34.98800 1.000 36.61319  ? 26  TRP A CG  1 
ATOM   226  C CD1 . TRP A 1 28  ? 19.44500 -13.97500 -34.18600 1.000 36.21442  ? 26  TRP A CD1 1 
ATOM   227  C CD2 . TRP A 1 28  ? 19.49000 -12.18300 -35.51600 1.000 32.92491  ? 26  TRP A CD2 1 
ATOM   228  N NE1 . TRP A 1 28  ? 20.73400 -13.47500 -34.17800 1.000 35.37611  ? 26  TRP A NE1 1 
ATOM   229  C CE2 . TRP A 1 28  ? 20.77500 -12.37200 -34.99000 1.000 35.94895  ? 26  TRP A CE2 1 
ATOM   230  C CE3 . TRP A 1 28  ? 19.26100 -11.10600 -36.36900 1.000 28.56001  ? 26  TRP A CE3 1 
ATOM   231  C CZ2 . TRP A 1 28  ? 21.83500 -11.51300 -35.28900 1.000 33.17907  ? 26  TRP A CZ2 1 
ATOM   232  C CZ3 . TRP A 1 28  ? 20.31800 -10.26000 -36.66900 1.000 32.79698  ? 26  TRP A CZ3 1 
ATOM   233  C CH2 . TRP A 1 28  ? 21.58400 -10.46100 -36.10900 1.000 34.86736  ? 26  TRP A CH2 1 
ATOM   234  N N   . SER A 1 29  ? 14.41800 -13.62700 -33.61800 1.000 38.41872  ? 27  SER A N   1 
ATOM   235  C CA  . SER A 1 29  ? 13.02500 -13.22300 -33.66100 1.000 38.48398  ? 27  SER A CA  1 
ATOM   236  C C   . SER A 1 29  ? 12.84300 -12.05400 -34.63200 1.000 38.81863  ? 27  SER A C   1 
ATOM   237  O O   . SER A 1 29  ? 13.80400 -11.38500 -35.03200 1.000 41.73795  ? 27  SER A O   1 
ATOM   238  C CB  . SER A 1 29  ? 12.53800 -12.84600 -32.26300 1.000 40.83216  ? 27  SER A CB  1 
ATOM   239  O OG  . SER A 1 29  ? 13.11600 -11.63000 -31.81300 1.000 53.42048  ? 27  SER A OG  1 
ATOM   240  N N   . GLU A 1 30  ? 11.58500 -11.82700 -35.03200 1.000 37.38429  ? 28  GLU A N   1 
ATOM   241  C CA  . GLU A 1 30  ? 11.25600 -10.63400 -35.80400 1.000 43.57867  ? 28  GLU A CA  1 
ATOM   242  C C   . GLU A 1 30  ? 11.71200 -9.38300  -35.08200 1.000 43.86959  ? 28  GLU A C   1 
ATOM   243  O O   . GLU A 1 30  ? 12.17000 -8.43400  -35.72100 1.000 47.96363  ? 28  GLU A O   1 
ATOM   244  C CB  . GLU A 1 30  ? 9.75200  -10.56100 -36.07400 1.000 42.44802  ? 28  GLU A CB  1 
ATOM   245  C CG  . GLU A 1 30  ? 9.37600  -9.86200  -37.37100 1.000 31.07181  ? 28  GLU A CG  1 
ATOM   246  C CD  . GLU A 1 30  ? 7.86400  -9.83400  -37.60000 1.000 33.69452  ? 28  GLU A CD  1 
ATOM   247  O OE1 . GLU A 1 30  ? 7.13500  -9.53700  -36.63400 1.000 58.73618  ? 28  GLU A OE1 1 
ATOM   248  O OE2 . GLU A 1 30  ? 7.40100  -10.13400 -38.72800 1.000 37.14474  ? 28  GLU A OE2 1 
ATOM   249  N N   . LYS A 1 31  ? 11.59800 -9.36000  -33.74200 1.000 39.58046  ? 29  LYS A N   1 
ATOM   250  C CA  . LYS A 1 31  ? 12.03000 -8.18900  -32.98700 1.000 42.43667  ? 29  LYS A CA  1 
ATOM   251  C C   . LYS A 1 31  ? 13.55700 -8.02400  -32.99200 1.000 41.11647  ? 29  LYS A C   1 
ATOM   252  O O   . LYS A 1 31  ? 14.04200 -6.89200  -32.94200 1.000 43.53925  ? 29  LYS A O   1 
ATOM   253  C CB  . LYS A 1 31  ? 11.48200 -8.27400  -31.56100 1.000 44.58134  ? 29  LYS A CB  1 
ATOM   254  C CG  . LYS A 1 31  ? 11.32700 -6.93700  -30.87800 1.000 48.71108  ? 29  LYS A CG  1 
ATOM   255  C CD  . LYS A 1 31  ? 12.53300 -6.63000  -29.99600 1.000 53.69131  ? 29  LYS A CD  1 
ATOM   256  C CE  . LYS A 1 31  ? 12.24000 -5.49100  -29.02700 1.000 56.20661  ? 29  LYS A CE  1 
ATOM   257  N NZ  . LYS A 1 31  ? 11.39900 -4.42400  -29.64100 1.000 60.10783  ? 29  LYS A NZ  1 
ATOM   258  N N   . PHE A 1 32  ? 14.33200 -9.12000  -33.06900 1.000 38.50376  ? 30  PHE A N   1 
ATOM   259  C CA  . PHE A 1 32  ? 15.79100 -8.99400  -33.14300 1.000 41.32991  ? 30  PHE A CA  1 
ATOM   260  C C   . PHE A 1 32  ? 16.23900 -8.28200  -34.42400 1.000 46.69122  ? 30  PHE A C   1 
ATOM   261  O O   . PHE A 1 32  ? 17.27300 -7.60400  -34.41900 1.000 46.55554  ? 30  PHE A O   1 
ATOM   262  C CB  . PHE A 1 32  ? 16.47100 -10.37100 -33.08000 1.000 48.76620  ? 30  PHE A CB  1 
ATOM   263  C CG  . PHE A 1 32  ? 16.70300 -10.88100 -31.68100 1.000 55.75305  ? 30  PHE A CG  1 
ATOM   264  C CD1 . PHE A 1 32  ? 16.02100 -10.32900 -30.61700 1.000 46.42975  ? 30  PHE A CD1 1 
ATOM   265  C CD2 . PHE A 1 32  ? 17.61400 -11.90500 -31.43000 1.000 51.89833  ? 30  PHE A CD2 1 
ATOM   266  C CE1 . PHE A 1 32  ? 16.21300 -10.78400 -29.32200 1.000 54.39836  ? 30  PHE A CE1 1 
ATOM   267  C CE2 . PHE A 1 32  ? 17.83200 -12.35700 -30.12900 1.000 50.95613  ? 30  PHE A CE2 1 
ATOM   268  C CZ  . PHE A 1 32  ? 17.12500 -11.79200 -29.07400 1.000 49.99675  ? 30  PHE A CZ  1 
ATOM   269  N N   . PHE A 1 33  ? 15.50000 -8.44600  -35.53600 1.000 41.34494  ? 31  PHE A N   1 
ATOM   270  C CA  . PHE A 1 33  ? 15.84100 -7.76000  -36.78600 1.000 31.93035  ? 31  PHE A CA  1 
ATOM   271  C C   . PHE A 1 33  ? 15.47300 -6.27800  -36.76300 1.000 37.11237  ? 31  PHE A C   1 
ATOM   272  O O   . PHE A 1 33  ? 16.17300 -5.47000  -37.38400 1.000 44.76554  ? 31  PHE A O   1 
ATOM   273  C CB  . PHE A 1 33  ? 15.16200 -8.46000  -37.97300 1.000 36.49959  ? 31  PHE A CB  1 
ATOM   274  C CG  . PHE A 1 33  ? 15.78000 -9.78600  -38.31700 1.000 29.45826  ? 31  PHE A CG  1 
ATOM   275  C CD1 . PHE A 1 33  ? 16.99700 -9.84300  -38.96200 1.000 32.21688  ? 31  PHE A CD1 1 
ATOM   276  C CD2 . PHE A 1 33  ? 15.16100 -10.97500 -37.96100 1.000 27.59326  ? 31  PHE A CD2 1 
ATOM   277  C CE1 . PHE A 1 33  ? 17.58000 -11.05900 -39.28400 1.000 31.91092  ? 31  PHE A CE1 1 
ATOM   278  C CE2 . PHE A 1 33  ? 15.73500 -12.18600 -38.26700 1.000 28.29479  ? 31  PHE A CE2 1 
ATOM   279  C CZ  . PHE A 1 33  ? 16.95700 -12.23500 -38.91500 1.000 25.18474  ? 31  PHE A CZ  1 
ATOM   280  N N   . TYR A 1 34  ? 14.41300 -5.88800  -36.04300 1.000 47.60046  ? 32  TYR A N   1 
ATOM   281  C CA  . TYR A 1 34  ? 14.24100 -4.45700  -35.76700 1.000 43.79298  ? 32  TYR A CA  1 
ATOM   282  C C   . TYR A 1 34  ? 15.38400 -3.90300  -34.92600 1.000 55.84885  ? 32  TYR A C   1 
ATOM   283  O O   . TYR A 1 34  ? 15.78200 -2.74600  -35.10600 1.000 49.81749  ? 32  TYR A O   1 
ATOM   284  C CB  . TYR A 1 34  ? 12.90200 -4.18300  -35.08200 1.000 57.10887  ? 32  TYR A CB  1 
ATOM   285  C CG  . TYR A 1 34  ? 11.70400 -4.55800  -35.92500 1.000 40.67093  ? 32  TYR A CG  1 
ATOM   286  C CD1 . TYR A 1 34  ? 11.48800 -3.96100  -37.14600 1.000 47.96161  ? 32  TYR A CD1 1 
ATOM   287  C CD2 . TYR A 1 34  ? 10.75700 -5.48300  -35.46600 1.000 55.06281  ? 32  TYR A CD2 1 
ATOM   288  C CE1 . TYR A 1 34  ? 10.39400 -4.30900  -37.93300 1.000 45.94361  ? 32  TYR A CE1 1 
ATOM   289  C CE2 . TYR A 1 34  ? 9.64900  -5.83500  -36.25400 1.000 41.98658  ? 32  TYR A CE2 1 
ATOM   290  C CZ  . TYR A 1 34  ? 9.47600  -5.23300  -37.48400 1.000 46.25199  ? 32  TYR A CZ  1 
ATOM   291  O OH  . TYR A 1 34  ? 8.40600  -5.53900  -38.28900 1.000 48.86343  ? 32  TYR A OH  1 
ATOM   292  N N   . ASP A 1 35  ? 15.94000 -4.71200  -34.02200 1.000 55.70984  ? 33  ASP A N   1 
ATOM   293  C CA  . ASP A 1 35  ? 16.96300 -4.21600  -33.10600 1.000 56.04360  ? 33  ASP A CA  1 
ATOM   294  C C   . ASP A 1 35  ? 18.20500 -3.71100  -33.84800 1.000 58.48566  ? 33  ASP A C   1 
ATOM   295  O O   . ASP A 1 35  ? 18.85000 -2.75600  -33.39500 1.000 57.30041  ? 33  ASP A O   1 
ATOM   296  C CB  . ASP A 1 35  ? 17.35300 -5.30500  -32.10700 1.000 53.13804  ? 33  ASP A CB  1 
ATOM   297  C CG  . ASP A 1 35  ? 16.34300 -5.46900  -30.97200 1.000 56.04224  ? 33  ASP A CG  1 
ATOM   298  O OD1 . ASP A 1 35  ? 15.38200 -4.67200  -30.86800 1.000 55.88798  ? 33  ASP A OD1 1 
ATOM   299  O OD2 . ASP A 1 35  ? 16.51900 -6.42000  -30.18100 1.000 63.54051  ? 33  ASP A OD2 1 
ATOM   300  N N   . CYS A 1 36  ? 18.58100 -4.34100  -34.97900 1.000 64.07071  ? 34  CYS A N   1 
ATOM   301  C CA  . CYS A 1 36  ? 19.71700 -3.84300  -35.75900 1.000 57.65172  ? 34  CYS A CA  1 
ATOM   302  C C   . CYS A 1 36  ? 19.28900 -2.96300  -36.92800 1.000 46.84599  ? 34  CYS A C   1 
ATOM   303  O O   . CYS A 1 36  ? 20.02100 -2.82400  -37.90800 1.000 54.78624  ? 34  CYS A O   1 
ATOM   304  C CB  . CYS A 1 36  ? 20.62600 -4.97700  -36.25700 1.000 51.09223  ? 34  CYS A CB  1 
ATOM   305  S SG  . CYS A 1 36  ? 19.97800 -6.63000  -36.30200 1.000 48.06090  ? 34  CYS A SG  1 
ATOM   306  N N   . LEU A 1 37  ? 18.12900 -2.34200  -36.84800 1.000 56.05310  ? 35  LEU A N   1 
ATOM   307  C CA  . LEU A 1 37  ? 17.88800 -1.24000  -37.76100 1.000 57.33833  ? 35  LEU A CA  1 
ATOM   308  C C   . LEU A 1 37  ? 18.62700 0.02000   -37.35600 1.000 60.92102  ? 35  LEU A C   1 
ATOM   309  O O   . LEU A 1 37  ? 18.70400 0.95800   -38.15600 1.000 63.48112  ? 35  LEU A O   1 
ATOM   310  C CB  . LEU A 1 37  ? 16.39000 -0.97000  -37.86500 1.000 54.46553  ? 35  LEU A CB  1 
ATOM   311  C CG  . LEU A 1 37  ? 15.80900 -1.85100  -38.98100 1.000 42.82855  ? 35  LEU A CG  1 
ATOM   312  C CD1 . LEU A 1 37  ? 14.28700 -1.83700  -38.96300 1.000 47.70884  ? 35  LEU A CD1 1 
ATOM   313  C CD2 . LEU A 1 37  ? 16.33000 -1.42300  -40.32800 1.000 42.58027  ? 35  LEU A CD2 1 
ATOM   314  N N   . LYS A 1 38  ? 19.20700 0.04800   -36.16400 1.000 50.54054  ? 36  LYS A N   1 
ATOM   315  C CA  . LYS A 1 38  ? 19.71900 1.27900   -35.59300 1.000 55.83436  ? 36  LYS A CA  1 
ATOM   316  C C   . LYS A 1 38  ? 21.09700 1.60200   -36.16700 1.000 56.34275  ? 36  LYS A C   1 
ATOM   317  O O   . LYS A 1 38  ? 21.61600 0.89700   -37.03300 1.000 50.14152  ? 36  LYS A O   1 
ATOM   318  C CB  . LYS A 1 38  ? 19.71800 1.17600   -34.07400 1.000 65.63099  ? 36  LYS A CB  1 
ATOM   319  C CG  . LYS A 1 38  ? 20.47100 -0.01800  -33.51600 1.000 64.90846  ? 36  LYS A CG  1 
ATOM   320  C CD  . LYS A 1 38  ? 20.28900 -0.09800  -32.00200 1.000 57.65691  ? 36  LYS A CD  1 
ATOM   321  C CE  . LYS A 1 38  ? 21.59200 -0.46200  -31.31300 1.000 59.18674  ? 36  LYS A CE  1 
ATOM   322  N NZ  . LYS A 1 38  ? 21.42700 -0.67700  -29.86900 1.000 67.50508  ? 36  LYS A NZ  1 
ATOM   323  N N   . SER A 1 39  ? 21.68700 2.69400   -35.68200 1.000 73.08605  ? 37  SER A N   1 
ATOM   324  C CA  . SER A 1 39  ? 22.89900 3.25400   -36.26700 1.000 73.08371  ? 37  SER A CA  1 
ATOM   325  C C   . SER A 1 39  ? 24.03200 2.23300   -36.27000 1.000 66.58630  ? 37  SER A C   1 
ATOM   326  O O   . SER A 1 39  ? 24.09600 1.33400   -35.42600 1.000 72.12278  ? 37  SER A O   1 
ATOM   327  C CB  . SER A 1 39  ? 23.33600 4.50600   -35.49600 1.000 84.35244  ? 37  SER A CB  1 
ATOM   328  O OG  . SER A 1 39  ? 22.25600 5.39800   -35.25200 1.000 91.50777  ? 37  SER A OG  1 
ATOM   329  N N   . ASN A 1 40  ? 24.93600 2.39000   -37.23900 1.000 63.00410  ? 38  ASN A N   1 
ATOM   330  C CA  . ASN A 1 40  ? 26.10500 1.55200   -37.50000 1.000 55.66788  ? 38  ASN A CA  1 
ATOM   331  C C   . ASN A 1 40  ? 25.77500 0.12000   -37.91000 1.000 45.90621  ? 38  ASN A C   1 
ATOM   332  O O   . ASN A 1 40  ? 26.71400 -0.68700  -38.02400 1.000 44.83279  ? 38  ASN A O   1 
ATOM   333  C CB  . ASN A 1 40  ? 27.06300 1.43700   -36.30300 1.000 55.31396  ? 38  ASN A CB  1 
ATOM   334  C CG  . ASN A 1 40  ? 27.49300 2.77000   -35.75400 1.000 65.99695  ? 38  ASN A CG  1 
ATOM   335  O OD1 . ASN A 1 40  ? 28.18400 3.55000   -36.42400 1.000 57.68241  ? 38  ASN A OD1 1 
ATOM   336  N ND2 . ASN A 1 40  ? 27.11300 3.03400   -34.51000 1.000 63.97382  ? 38  ASN A ND2 1 
ATOM   337  N N   . TYR A 1 41  ? 24.50300 -0.24900  -38.09800 1.000 29.68411  ? 39  TYR A N   1 
ATOM   338  C CA  . TYR A 1 41  ? 24.14100 -1.58200  -38.57600 1.000 31.77118  ? 39  TYR A CA  1 
ATOM   339  C C   . TYR A 1 41  ? 23.67600 -1.43800  -40.01300 1.000 33.11142  ? 39  TYR A C   1 
ATOM   340  O O   . TYR A 1 41  ? 22.89200 -0.53700  -40.31300 1.000 32.04500  ? 39  TYR A O   1 
ATOM   341  C CB  . TYR A 1 41  ? 23.02600 -2.20800  -37.73800 1.000 40.66624  ? 39  TYR A CB  1 
ATOM   342  C CG  . TYR A 1 41  ? 23.43500 -2.71200  -36.37300 1.000 45.44207  ? 39  TYR A CG  1 
ATOM   343  C CD1 . TYR A 1 41  ? 23.93200 -4.00900  -36.20600 1.000 30.09357  ? 39  TYR A CD1 1 
ATOM   344  C CD2 . TYR A 1 41  ? 23.29900 -1.91300  -35.24700 1.000 48.20058  ? 39  TYR A CD2 1 
ATOM   345  C CE1 . TYR A 1 41  ? 24.32200 -4.47100  -34.94200 1.000 26.90549  ? 39  TYR A CE1 1 
ATOM   346  C CE2 . TYR A 1 41  ? 23.66400 -2.36900  -33.98900 1.000 51.31706  ? 39  TYR A CE2 1 
ATOM   347  C CZ  . TYR A 1 41  ? 24.16200 -3.64900  -33.84500 1.000 45.29445  ? 39  TYR A CZ  1 
ATOM   348  O OH  . TYR A 1 41  ? 24.52100 -4.09000  -32.58900 1.000 51.43609  ? 39  TYR A OH  1 
ATOM   349  N N   . TYR A 1 42  ? 24.17100 -2.29500  -40.90900 1.000 25.60482  ? 40  TYR A N   1 
ATOM   350  C CA  . TYR A 1 42  ? 23.86800 -2.15100  -42.32900 1.000 26.67807  ? 40  TYR A CA  1 
ATOM   351  C C   . TYR A 1 42  ? 23.42100 -3.49700  -42.84000 1.000 21.97688  ? 40  TYR A C   1 
ATOM   352  O O   . TYR A 1 42  ? 24.02200 -4.52600  -42.51600 1.000 21.39901  ? 40  TYR A O   1 
ATOM   353  C CB  . TYR A 1 42  ? 25.08400 -1.65700  -43.12200 1.000 26.58069  ? 40  TYR A CB  1 
ATOM   354  C CG  . TYR A 1 42  ? 25.58900 -0.31400  -42.64100 1.000 34.17832  ? 40  TYR A CG  1 
ATOM   355  C CD1 . TYR A 1 42  ? 25.08800 0.87500   -43.15600 1.000 39.84733  ? 40  TYR A CD1 1 
ATOM   356  C CD2 . TYR A 1 42  ? 26.57000 -0.23800  -41.65900 1.000 33.43297  ? 40  TYR A CD2 1 
ATOM   357  C CE1 . TYR A 1 42  ? 25.56000 2.10600   -42.69700 1.000 43.76629  ? 40  TYR A CE1 1 
ATOM   358  C CE2 . TYR A 1 42  ? 27.04400 0.99400   -41.18300 1.000 34.14025  ? 40  TYR A CE2 1 
ATOM   359  C CZ  . TYR A 1 42  ? 26.54900 2.15100   -41.71100 1.000 45.55407  ? 40  TYR A CZ  1 
ATOM   360  O OH  . TYR A 1 42  ? 27.04100 3.35500   -41.23300 1.000 47.41099  ? 40  TYR A OH  1 
ATOM   361  N N   . GLY A 1 43  ? 22.36200 -3.49600  -43.64900 1.000 24.13231  ? 41  GLY A N   1 
ATOM   362  C CA  . GLY A 1 43  ? 21.83000 -4.72500  -44.18800 1.000 18.71026  ? 41  GLY A CA  1 
ATOM   363  C C   . GLY A 1 43  ? 21.52100 -4.57300  -45.66600 1.000 18.91362  ? 41  GLY A C   1 
ATOM   364  O O   . GLY A 1 43  ? 21.29600 -3.46700  -46.18100 1.000 22.70880  ? 41  GLY A O   1 
ATOM   365  N N   . TRP A 1 44  ? 21.51500 -5.72300  -46.33100 1.000 18.87442  ? 42  TRP A N   1 
ATOM   366  C CA  . TRP A 1 44  ? 21.15500 -5.88100  -47.73700 1.000 18.71624  ? 42  TRP A CA  1 
ATOM   367  C C   . TRP A 1 44  ? 20.26900 -7.11400  -47.91500 1.000 18.92689  ? 42  TRP A C   1 
ATOM   368  O O   . TRP A 1 44  ? 20.38200 -8.10800  -47.17100 1.000 17.92810  ? 42  TRP A O   1 
ATOM   369  C CB  . TRP A 1 44  ? 22.43100 -6.02200  -48.59400 1.000 15.20476  ? 42  TRP A CB  1 
ATOM   370  C CG  . TRP A 1 44  ? 23.30700 -4.78100  -48.65500 1.000 18.19983  ? 42  TRP A CG  1 
ATOM   371  C CD1 . TRP A 1 44  ? 23.30700 -3.80800  -49.65300 1.000 30.21284  ? 42  TRP A CD1 1 
ATOM   372  C CD2 . TRP A 1 44  ? 24.34500 -4.42600  -47.75100 1.000 24.05605  ? 42  TRP A CD2 1 
ATOM   373  N NE1 . TRP A 1 44  ? 24.28600 -2.88300  -49.39500 1.000 23.94808  ? 42  TRP A NE1 1 
ATOM   374  C CE2 . TRP A 1 44  ? 24.92400 -3.22900  -48.22300 1.000 25.37394  ? 42  TRP A CE2 1 
ATOM   375  C CE3 . TRP A 1 44  ? 24.82300 -5.00100  -46.55700 1.000 21.21296  ? 42  TRP A CE3 1 
ATOM   376  C CZ2 . TRP A 1 44  ? 25.97400 -2.57900  -47.54200 1.000 28.20686  ? 42  TRP A CZ2 1 
ATOM   377  C CZ3 . TRP A 1 44  ? 25.85100 -4.35300  -45.87800 1.000 24.43165  ? 42  TRP A CZ3 1 
ATOM   378  C CH2 . TRP A 1 44  ? 26.43200 -3.16700  -46.39000 1.000 28.03112  ? 42  TRP A CH2 1 
ATOM   379  N N   . VAL A 1 45  ? 19.43600 -7.09000  -48.94900 1.000 16.91991  ? 43  VAL A N   1 
ATOM   380  C CA  . VAL A 1 45  ? 18.57000 -8.22300  -49.24300 1.000 13.30352  ? 43  VAL A CA  1 
ATOM   381  C C   . VAL A 1 45  ? 18.73800 -8.52100  -50.72300 1.000 18.38079  ? 43  VAL A C   1 
ATOM   382  O O   . VAL A 1 45  ? 19.07000 -7.62400  -51.51100 1.000 15.88794  ? 43  VAL A O   1 
ATOM   383  C CB  . VAL A 1 45  ? 17.07400 -7.97600  -48.92000 1.000 17.40473  ? 43  VAL A CB  1 
ATOM   384  C CG1 . VAL A 1 45  ? 16.81000 -7.82600  -47.37300 1.000 18.58167  ? 43  VAL A CG1 1 
ATOM   385  C CG2 . VAL A 1 45  ? 16.53600 -6.78500  -49.70300 1.000 19.20009  ? 43  VAL A CG2 1 
ATOM   386  N N   . MET A 1 46  ? 18.56600 -9.78700  -51.08900 1.000 16.07099  ? 44  MET A N   1 
ATOM   387  C CA  . MET A 1 46  ? 18.48700 -10.19800 -52.50300 1.000 16.37019  ? 44  MET A CA  1 
ATOM   388  C C   . MET A 1 46  ? 17.04900 -10.55200 -52.83600 1.000 20.72539  ? 44  MET A C   1 
ATOM   389  O O   . MET A 1 46  ? 16.39500 -11.28400 -52.08500 1.000 17.48563  ? 44  MET A O   1 
ATOM   390  C CB  . MET A 1 46  ? 19.36600 -11.41500 -52.84100 1.000 14.64108  ? 44  MET A CB  1 
ATOM   391  C CG  . MET A 1 46  ? 19.28700 -11.66600 -54.33300 1.000 21.22250  ? 44  MET A CG  1 
ATOM   392  S SD  . MET A 1 46  ? 20.11900 -13.16900 -54.89600 1.000 26.60929  ? 44  MET A SD  1 
ATOM   393  C CE  . MET A 1 46  ? 21.73400 -12.55000 -54.72400 1.000 20.28102  ? 44  MET A CE  1 
ATOM   394  N N   . GLU A 1 47  ? 16.54800 -10.02900 -53.94500 1.000 18.23397  ? 45  GLU A N   1 
ATOM   395  C CA  . GLU A 1 47  ? 15.25900 -10.47400 -54.45900 1.000 16.82707  ? 45  GLU A CA  1 
ATOM   396  C C   . GLU A 1 47  ? 15.48500 -11.33300 -55.70000 1.000 20.82923  ? 45  GLU A C   1 
ATOM   397  O O   . GLU A 1 47  ? 16.19500 -10.92200 -56.64200 1.000 20.78501  ? 45  GLU A O   1 
ATOM   398  C CB  . GLU A 1 47  ? 14.36500 -9.27500  -54.77700 1.000 21.38000  ? 45  GLU A CB  1 
ATOM   399  C CG  . GLU A 1 47  ? 13.07700 -9.71400  -55.36600 1.000 22.87887  ? 45  GLU A CG  1 
ATOM   400  C CD  . GLU A 1 47  ? 12.24700 -8.59700  -55.83600 1.000 27.38690  ? 45  GLU A CD  1 
ATOM   401  O OE1 . GLU A 1 47  ? 12.40300 -7.47400  -55.32600 1.000 33.16565  ? 45  GLU A OE1 1 
ATOM   402  O OE2 . GLU A 1 47  ? 11.44500 -8.82300  -56.75000 1.000 42.18190  ? 45  GLU A OE2 1 
ATOM   403  N N   . SER A 1 48  ? 14.90100 -12.53300 -55.69000 1.000 15.74821  ? 46  SER A N   1 
ATOM   404  C CA  . SER A 1 48  ? 14.90300 -13.41400 -56.86400 1.000 17.28902  ? 46  SER A CA  1 
ATOM   405  C C   . SER A 1 48  ? 13.52000 -14.03700 -56.96700 1.000 18.18599  ? 46  SER A C   1 
ATOM   406  O O   . SER A 1 48  ? 12.87300 -14.26300 -55.93700 1.000 15.98262  ? 46  SER A O   1 
ATOM   407  C CB  . SER A 1 48  ? 16.01100 -14.48500 -56.71400 1.000 17.01777  ? 46  SER A CB  1 
ATOM   408  O OG  . SER A 1 48  ? 16.10300 -15.33300 -57.86600 1.000 25.13753  ? 46  SER A OG  1 
ATOM   409  N N   . ASP A 1 49  ? 13.02600 -14.29000 -58.18900 1.000 15.96271  ? 47  ASP A N   1 
ATOM   410  C CA  . ASP A 1 49  ? 11.65700 -14.81800 -58.32900 1.000 13.70586  ? 47  ASP A CA  1 
ATOM   411  C C   . ASP A 1 49  ? 10.63700 -13.95600 -57.54700 1.000 17.77858  ? 47  ASP A C   1 
ATOM   412  O O   . ASP A 1 49  ? 9.75000  -14.45700 -56.86000 1.000 19.59366  ? 47  ASP A O   1 
ATOM   413  C CB  . ASP A 1 49  ? 11.61900 -16.28200 -57.86700 1.000 15.95620  ? 47  ASP A CB  1 
ATOM   414  C CG  . ASP A 1 49  ? 12.32900 -17.23300 -58.81800 1.000 21.40257  ? 47  ASP A CG  1 
ATOM   415  O OD1 . ASP A 1 49  ? 12.39600 -16.93000 -60.05200 1.000 19.83907  ? 47  ASP A OD1 1 
ATOM   416  O OD2 . ASP A 1 49  ? 12.73200 -18.33200 -58.32800 1.000 19.48743  ? 47  ASP A OD2 1 
ATOM   417  N N   . HIS A 1 50  ? 10.80800 -12.63800 -57.58200 1.000 17.93439  ? 48  HIS A N   1 
ATOM   418  C CA  . HIS A 1 50  ? 9.80400  -11.69600 -57.06900 1.000 16.82325  ? 48  HIS A CA  1 
ATOM   419  C C   . HIS A 1 50  ? 9.60500  -11.80600 -55.55100 1.000 18.95891  ? 48  HIS A C   1 
ATOM   420  O O   . HIS A 1 50  ? 8.51200  -11.50100 -55.04600 1.000 20.60690  ? 48  HIS A O   1 
ATOM   421  C CB  . HIS A 1 50  ? 8.43500  -11.85800 -57.76300 1.000 20.81580  ? 48  HIS A CB  1 
ATOM   422  C CG  . HIS A 1 50  ? 8.50600  -11.85700 -59.26000 1.000 21.28750  ? 48  HIS A CG  1 
ATOM   423  N ND1 . HIS A 1 50  ? 8.54100  -10.69400 -60.00100 1.000 29.06480  ? 48  HIS A ND1 1 
ATOM   424  C CD2 . HIS A 1 50  ? 8.60900  -12.87000 -60.14300 1.000 25.73621  ? 48  HIS A CD2 1 
ATOM   425  C CE1 . HIS A 1 50  ? 8.62100  -10.99500 -61.28700 1.000 26.07995  ? 48  HIS A CE1 1 
ATOM   426  N NE2 . HIS A 1 50  ? 8.68100  -12.31200 -61.39800 1.000 24.59536  ? 48  HIS A NE2 1 
ATOM   427  N N   . HIS A 1 51  ? 10.62200 -12.20700 -54.79600 1.000 20.36913  ? 49  HIS A N   1 
ATOM   428  C CA  . HIS A 1 51  ? 10.47500 -12.23700 -53.34000 1.000 15.22633  ? 49  HIS A CA  1 
ATOM   429  C C   . HIS A 1 51  ? 11.87600 -12.23200 -52.73200 1.000 16.80889  ? 49  HIS A C   1 
ATOM   430  O O   . HIS A 1 51  ? 12.88000 -12.45700 -53.42800 1.000 15.52533  ? 49  HIS A O   1 
ATOM   431  C CB  . HIS A 1 51  ? 9.64000  -13.45900 -52.87100 1.000 17.51745  ? 49  HIS A CB  1 
ATOM   432  C CG  . HIS A 1 51  ? 10.34300 -14.78500 -52.95900 1.000 19.76899  ? 49  HIS A CG  1 
ATOM   433  N ND1 . HIS A 1 51  ? 10.70300 -15.35200 -54.16600 1.000 15.92442  ? 49  HIS A ND1 1 
ATOM   434  C CD2 . HIS A 1 51  ? 10.74700 -15.66300 -52.00200 1.000 18.35821  ? 49  HIS A CD2 1 
ATOM   435  C CE1 . HIS A 1 51  ? 11.30200 -16.50800 -53.95200 1.000 12.25874  ? 49  HIS A CE1 1 
ATOM   436  N NE2 . HIS A 1 51  ? 11.32000 -16.73700 -52.64800 1.000 19.46624  ? 49  HIS A NE2 1 
ATOM   437  N N   . LEU A 1 52  ? 11.96800 -11.95400 -51.43000 1.000 15.85485  ? 50  LEU A N   1 
ATOM   438  C CA  . LEU A 1 52  ? 13.31800 -11.94200 -50.83800 1.000 14.79268  ? 50  LEU A CA  1 
ATOM   439  C C   . LEU A 1 52  ? 13.81500 -13.35900 -50.58300 1.000 13.69894  ? 50  LEU A C   1 
ATOM   440  O O   . LEU A 1 52  ? 13.07200 -14.17600 -50.00800 1.000 17.13432  ? 50  LEU A O   1 
ATOM   441  C CB  . LEU A 1 52  ? 13.30300 -11.14100 -49.52900 1.000 19.84485  ? 50  LEU A CB  1 
ATOM   442  C CG  . LEU A 1 52  ? 12.99200 -9.64600  -49.69300 1.000 22.60379  ? 50  LEU A CG  1 
ATOM   443  C CD1 . LEU A 1 52  ? 13.23500 -8.94200  -48.33800 1.000 24.15358  ? 50  LEU A CD1 1 
ATOM   444  C CD2 . LEU A 1 52  ? 13.81400 -8.91600  -50.78000 1.000 21.67714  ? 50  LEU A CD2 1 
ATOM   445  N N   . VAL A 1 53  ? 15.07500 -13.64100 -50.95200 1.000 14.94775  ? 51  VAL A N   1 
ATOM   446  C CA  . VAL A 1 53  ? 15.62700 -14.98800 -50.76000 1.000 18.12492  ? 51  VAL A CA  1 
ATOM   447  C C   . VAL A 1 53  ? 16.86400 -15.02200 -49.87900 1.000 16.07952  ? 51  VAL A C   1 
ATOM   448  O O   . VAL A 1 53  ? 17.33300 -16.10900 -49.54900 1.000 16.18399  ? 51  VAL A O   1 
ATOM   449  C CB  . VAL A 1 53  ? 15.91500 -15.68100 -52.09500 1.000 15.03363  ? 51  VAL A CB  1 
ATOM   450  C CG1 . VAL A 1 53  ? 14.60100 -15.71900 -52.97900 1.000 14.50158  ? 51  VAL A CG1 1 
ATOM   451  C CG2 . VAL A 1 53  ? 17.07300 -14.99200 -52.82900 1.000 15.59491  ? 51  VAL A CG2 1 
ATOM   452  N N   . GLY A 1 54  ? 17.36500 -13.89400 -49.43900 1.000 16.54524  ? 52  GLY A N   1 
ATOM   453  C CA  . GLY A 1 54  ? 18.54600 -13.93100 -48.58100 1.000 18.24180  ? 52  GLY A CA  1 
ATOM   454  C C   . GLY A 1 54  ? 18.82200 -12.53700 -48.09300 1.000 17.55983  ? 52  GLY A C   1 
ATOM   455  O O   . GLY A 1 54  ? 18.30500 -11.56200 -48.65000 1.000 15.68870  ? 52  GLY A O   1 
ATOM   456  N N   . PHE A 1 55  ? 19.54900 -12.45900 -46.97900 1.000 14.22736  ? 53  PHE A N   1 
ATOM   457  C CA  . PHE A 1 55  ? 19.90200 -11.16100 -46.40700 1.000 16.53366  ? 53  PHE A CA  1 
ATOM   458  C C   . PHE A 1 55  ? 21.26200 -11.27800 -45.74500 1.000 17.00443  ? 53  PHE A C   1 
ATOM   459  O O   . PHE A 1 55  ? 21.79500 -12.37800 -45.50200 1.000 13.45302  ? 53  PHE A O   1 
ATOM   460  C CB  . PHE A 1 55  ? 18.84700 -10.69900 -45.37100 1.000 16.49111  ? 53  PHE A CB  1 
ATOM   461  C CG  . PHE A 1 55  ? 18.77300 -11.57900 -44.14500 1.000 13.72917  ? 53  PHE A CG  1 
ATOM   462  C CD1 . PHE A 1 55  ? 19.64700 -11.37900 -43.07800 1.000 17.58782  ? 53  PHE A CD1 1 
ATOM   463  C CD2 . PHE A 1 55  ? 17.89100 -12.65400 -44.09100 1.000 18.76313  ? 53  PHE A CD2 1 
ATOM   464  C CE1 . PHE A 1 55  ? 19.62100 -12.22400 -41.95600 1.000 20.06268  ? 53  PHE A CE1 1 
ATOM   465  C CE2 . PHE A 1 55  ? 17.86400 -13.49100 -42.96700 1.000 17.09502  ? 53  PHE A CE2 1 
ATOM   466  C CZ  . PHE A 1 55  ? 18.71800 -13.25800 -41.89200 1.000 19.16303  ? 53  PHE A CZ  1 
ATOM   467  N N   . ILE A 1 56  ? 21.87600 -10.12800 -45.50400 1.000 14.87059  ? 54  ILE A N   1 
ATOM   468  C CA  . ILE A 1 56  ? 23.12900 -10.10300 -44.75200 1.000 16.55451  ? 54  ILE A CA  1 
ATOM   469  C C   . ILE A 1 56  ? 23.12400 -8.83100  -43.92800 1.000 19.25517  ? 54  ILE A C   1 
ATOM   470  O O   . ILE A 1 56  ? 22.60000 -7.80300  -44.38500 1.000 18.03428  ? 54  ILE A O   1 
ATOM   471  C CB  . ILE A 1 56  ? 24.33600 -10.17000 -45.71800 1.000 15.52070  ? 54  ILE A CB  1 
ATOM   472  C CG1 . ILE A 1 56  ? 25.60500 -10.26000 -44.90900 1.000 15.48199  ? 54  ILE A CG1 1 
ATOM   473  C CG2 . ILE A 1 56  ? 24.42400 -8.92200  -46.66700 1.000 19.57912  ? 54  ILE A CG2 1 
ATOM   474  C CD1 . ILE A 1 56  ? 26.83100 -10.27900 -45.78500 1.000 17.33288  ? 54  ILE A CD1 1 
ATOM   475  N N   . VAL A 1 57  ? 23.68100 -8.89500  -42.71700 1.000 16.19259  ? 55  VAL A N   1 
ATOM   476  C CA  . VAL A 1 57  ? 23.67400 -7.78300  -41.76800 1.000 18.52070  ? 55  VAL A CA  1 
ATOM   477  C C   . VAL A 1 57  ? 25.08300 -7.66600  -41.24600 1.000 19.67322  ? 55  VAL A C   1 
ATOM   478  O O   . VAL A 1 57  ? 25.63500 -8.66300  -40.73800 1.000 18.18832  ? 55  VAL A O   1 
ATOM   479  C CB  . VAL A 1 57  ? 22.69800 -7.99300  -40.59600 1.000 18.73468  ? 55  VAL A CB  1 
ATOM   480  C CG1 . VAL A 1 57  ? 22.72700 -6.75600  -39.63100 1.000 22.55945  ? 55  VAL A CG1 1 
ATOM   481  C CG2 . VAL A 1 57  ? 21.21700 -8.28700  -41.13900 1.000 25.11054  ? 55  VAL A CG2 1 
ATOM   482  N N   . ILE A 1 58  ? 25.66900 -6.44800  -41.30400 1.000 19.35818  ? 56  ILE A N   1 
ATOM   483  C CA  . ILE A 1 58  ? 26.98200 -6.22600  -40.70900 1.000 20.87139  ? 56  ILE A CA  1 
ATOM   484  C C   . ILE A 1 58  ? 26.89300 -5.11800  -39.67100 1.000 21.85839  ? 56  ILE A C   1 
ATOM   485  O O   . ILE A 1 58  ? 25.95500 -4.30600  -39.67400 1.000 22.08232  ? 56  ILE A O   1 
ATOM   486  C CB  . ILE A 1 58  ? 28.09400 -5.83700  -41.72200 1.000 21.58466  ? 56  ILE A CB  1 
ATOM   487  C CG1 . ILE A 1 58  ? 27.72700 -4.52200  -42.45300 1.000 23.36411  ? 56  ILE A CG1 1 
ATOM   488  C CG2 . ILE A 1 58  ? 28.38700 -6.98200  -42.69400 1.000 21.71627  ? 56  ILE A CG2 1 
ATOM   489  C CD1 . ILE A 1 58  ? 28.83900 -3.98300  -43.35000 1.000 31.50658  ? 56  ILE A CD1 1 
ATOM   490  N N   . LEU A 1 59  ? 27.91100 -5.07500  -38.82800 1.000 23.44668  ? 57  LEU A N   1 
ATOM   491  C CA  . LEU A 1 59  ? 28.09300 -4.02000  -37.84100 1.000 29.13078  ? 57  LEU A CA  1 
ATOM   492  C C   . LEU A 1 59  ? 29.43600 -3.36300  -38.11200 1.000 30.07512  ? 57  LEU A C   1 
ATOM   493  O O   . LEU A 1 59  ? 30.47300 -4.03300  -38.01900 1.000 27.78973  ? 57  LEU A O   1 
ATOM   494  C CB  . LEU A 1 59  ? 28.04600 -4.59800  -36.41900 1.000 30.44618  ? 57  LEU A CB  1 
ATOM   495  C CG  . LEU A 1 59  ? 28.41600 -3.67100  -35.26200 1.000 33.58411  ? 57  LEU A CG  1 
ATOM   496  C CD1 . LEU A 1 59  ? 27.44200 -2.48700  -35.30400 1.000 32.14005  ? 57  LEU A CD1 1 
ATOM   497  C CD2 . LEU A 1 59  ? 28.30800 -4.44200  -33.93600 1.000 32.05532  ? 57  LEU A CD2 1 
ATOM   498  N N   . MET A 1 60  ? 29.44100 -2.04700  -38.38000 1.000 33.13020  ? 58  MET A N   1 
ATOM   499  C CA  . MET A 1 60  ? 30.69900 -1.29700  -38.47800 1.000 38.14137  ? 58  MET A CA  1 
ATOM   500  C C   . MET A 1 60  ? 31.07600 -0.76800  -37.09500 1.000 47.62360  ? 58  MET A C   1 
ATOM   501  O O   . MET A 1 60  ? 30.39800 0.10800   -36.55500 1.000 45.52557  ? 58  MET A O   1 
ATOM   502  C CB  . MET A 1 60  ? 30.59900 -0.13000  -39.45900 1.000 41.44582  ? 58  MET A CB  1 
ATOM   503  C CG  . MET A 1 60  ? 30.24700 -0.48500  -40.87000 1.000 40.24485  ? 58  MET A CG  1 
ATOM   504  S SD  . MET A 1 60  ? 31.46700 -1.43100  -41.82600 1.000 38.94013  ? 58  MET A SD  1 
ATOM   505  C CE  . MET A 1 60  ? 32.89900 -0.40000  -41.74500 1.000 36.10903  ? 58  MET A CE  1 
ATOM   506  N N   . GLN A 1 61  ? 32.17100 -1.27000  -36.52900 1.000 42.42986  ? 59  GLN A N   1 
ATOM   507  C CA  . GLN A 1 61  ? 32.54700 -0.88600  -35.17500 1.000 58.35835  ? 59  GLN A CA  1 
ATOM   508  C C   . GLN A 1 61  ? 34.05000 -0.69100  -35.11100 1.000 64.09524  ? 59  GLN A C   1 
ATOM   509  O O   . GLN A 1 61  ? 34.81100 -1.48400  -35.67800 1.000 48.62954  ? 59  GLN A O   1 
ATOM   510  C CB  . GLN A 1 61  ? 32.09600 -1.93100  -34.13500 1.000 65.40925  ? 59  GLN A CB  1 
ATOM   511  C CG  . GLN A 1 61  ? 32.60100 -3.36500  -34.36800 1.000 61.44426  ? 59  GLN A CG  1 
ATOM   512  C CD  . GLN A 1 61  ? 32.20600 -4.32100  -33.23800 1.000 64.78976  ? 59  GLN A CD  1 
ATOM   513  O OE1 . GLN A 1 61  ? 31.78200 -3.88700  -32.14900 1.000 65.32728  ? 59  GLN A OE1 1 
ATOM   514  N NE2 . GLN A 1 61  ? 32.34400 -5.63400  -33.49400 1.000 49.26642  ? 59  GLN A NE2 1 
ATOM   515  N N   . GLU A 1 62  ? 34.46400 0.36600   -34.41000 1.000 78.61845  ? 60  GLU A N   1 
ATOM   516  C CA  . GLU A 1 62  ? 35.86900 0.76200   -34.30900 1.000 72.77378  ? 60  GLU A CA  1 
ATOM   517  C C   . GLU A 1 62  ? 36.36600 0.95200   -35.73600 1.000 70.92969  ? 60  GLU A C   1 
ATOM   518  O O   . GLU A 1 62  ? 35.69400 1.64200   -36.51900 1.000 78.16536  ? 60  GLU A O   1 
ATOM   519  C CB  . GLU A 1 62  ? 36.63800 -0.26100  -33.49200 1.000 82.94538  ? 60  GLU A CB  1 
ATOM   520  C CG  . GLU A 1 62  ? 36.47800 -0.15300  -31.99800 1.000 91.60968  ? 60  GLU A CG  1 
ATOM   521  C CD  . GLU A 1 62  ? 37.23800 -1.25200  -31.27500 1.000 107.60279 ? 60  GLU A CD  1 
ATOM   522  O OE1 . GLU A 1 62  ? 37.76100 -2.16300  -31.96000 1.000 111.33592 ? 60  GLU A OE1 1 
ATOM   523  O OE2 . GLU A 1 62  ? 37.31000 -1.20800  -30.02800 1.000 100.30899 ? 60  GLU A OE2 1 
ATOM   524  N N   . LYS A 1 63  ? 37.48700 0.34800   -36.11700 1.000 69.46750  ? 61  LYS A N   1 
ATOM   525  C CA  . LYS A 1 63  ? 37.99900 0.40500   -37.47400 1.000 72.53836  ? 61  LYS A CA  1 
ATOM   526  C C   . LYS A 1 63  ? 37.64000 -0.82800  -38.31200 1.000 69.93938  ? 61  LYS A C   1 
ATOM   527  O O   . LYS A 1 63  ? 37.91200 -0.83400  -39.51600 1.000 72.53147  ? 61  LYS A O   1 
ATOM   528  C CB  . LYS A 1 63  ? 39.52600 0.60700   -37.42400 1.000 65.37503  ? 61  LYS A CB  1 
ATOM   529  C CG  . LYS A 1 63  ? 40.19500 0.85200   -38.76500 1.000 72.07313  ? 61  LYS A CG  1 
ATOM   530  C CD  . LYS A 1 63  ? 41.07100 -0.32700  -39.14700 1.000 78.98934  ? 61  LYS A CD  1 
ATOM   531  C CE  . LYS A 1 63  ? 41.40100 -0.31500  -40.62900 1.000 69.93960  ? 61  LYS A CE  1 
ATOM   532  N NZ  . LYS A 1 63  ? 41.30800 -1.67600  -41.23200 1.000 61.25166  ? 61  LYS A NZ  1 
ATOM   533  N N   . GLU A 1 64  ? 37.00000 -1.85400  -37.73900 1.000 55.65745  ? 62  GLU A N   1 
ATOM   534  C CA  . GLU A 1 64  ? 36.76200 -3.09800  -38.47200 1.000 52.41984  ? 62  GLU A CA  1 
ATOM   535  C C   . GLU A 1 64  ? 35.25900 -3.40400  -38.54500 1.000 39.65419  ? 62  GLU A C   1 
ATOM   536  O O   . GLU A 1 64  ? 34.40600 -2.58900  -38.16800 1.000 48.81811  ? 62  GLU A O   1 
ATOM   537  C CB  . GLU A 1 64  ? 37.56900 -4.23700  -37.83800 1.000 48.98057  ? 62  GLU A CB  1 
ATOM   538  C CG  . GLU A 1 64  ? 39.06300 -3.90000  -37.65400 1.000 50.79706  ? 62  GLU A CG  1 
ATOM   539  C CD  . GLU A 1 64  ? 39.85400 -3.93600  -38.97100 1.000 55.47287  ? 62  GLU A CD  1 
ATOM   540  O OE1 . GLU A 1 64  ? 39.23200 -4.01300  -40.08300 1.000 46.68942  ? 62  GLU A OE1 1 
ATOM   541  O OE2 . GLU A 1 64  ? 41.09900 -3.89900  -38.89600 1.000 60.50771  ? 62  GLU A OE2 1 
ATOM   542  N N   . CYS A 1 65  ? 34.93000 -4.59900  -39.03300 1.000 39.69881  ? 63  CYS A N   1 
ATOM   543  C CA  . CYS A 1 65  ? 33.56600 -4.93800  -39.39300 1.000 35.16615  ? 63  CYS A CA  1 
ATOM   544  C C   . CYS A 1 65  ? 33.18900 -6.28500  -38.76700 1.000 31.97415  ? 63  CYS A C   1 
ATOM   545  O O   . CYS A 1 65  ? 34.04600 -7.14300  -38.59300 1.000 30.51927  ? 63  CYS A O   1 
ATOM   546  C CB  . CYS A 1 65  ? 33.45600 -4.94700  -40.94800 1.000 31.40049  ? 63  CYS A CB  1 
ATOM   547  S SG  . CYS A 1 65  ? 31.79600 -5.16800  -41.47800 1.000 40.43273  ? 63  CYS A SG  1 
ATOM   548  N N   . GLN A 1 66  ? 31.91100 -6.47100  -38.40100 1.000 28.68603  ? 64  GLN A N   1 
ATOM   549  C CA  . GLN A 1 66  ? 31.44900 -7.76600  -37.90400 1.000 26.60146  ? 64  GLN A CA  1 
ATOM   550  C C   . GLN A 1 66  ? 30.25700 -8.24500  -38.71200 1.000 24.01574  ? 64  GLN A C   1 
ATOM   551  O O   . GLN A 1 66  ? 29.31400 -7.47900  -38.97200 1.000 23.46303  ? 64  GLN A O   1 
ATOM   552  C CB  . GLN A 1 66  ? 31.09100 -7.69400  -36.40300 1.000 30.65639  ? 64  GLN A CB  1 
ATOM   553  C CG  . GLN A 1 66  ? 30.55400 -9.02400  -35.86100 1.000 26.54583  ? 64  GLN A CG  1 
ATOM   554  C CD  . GLN A 1 66  ? 30.41600 -9.06400  -34.36500 1.000 29.29886  ? 64  GLN A CD  1 
ATOM   555  O OE1 . GLN A 1 66  ? 30.75800 -8.10600  -33.66000 1.000 36.75688  ? 64  GLN A OE1 1 
ATOM   556  N NE2 . GLN A 1 66  ? 29.91100 -10.18700 -33.85900 1.000 31.49512  ? 64  GLN A NE2 1 
ATOM   557  N N   . LEU A 1 67  ? 30.28000 -9.52600  -39.11600 1.000 21.53562  ? 65  LEU A N   1 
ATOM   558  C CA  . LEU A 1 67  ? 29.15100 -10.15400 -39.79400 1.000 21.43390  ? 65  LEU A CA  1 
ATOM   559  C C   . LEU A 1 67  ? 28.15100 -10.62200 -38.73400 1.000 23.06878  ? 65  LEU A C   1 
ATOM   560  O O   . LEU A 1 67  ? 28.44400 -11.53700 -37.95800 1.000 21.94794  ? 65  LEU A O   1 
ATOM   561  C CB  . LEU A 1 67  ? 29.63100 -11.33300 -40.64900 1.000 19.53963  ? 65  LEU A CB  1 
ATOM   562  C CG  . LEU A 1 67  ? 28.56400 -12.13200 -41.40400 1.000 19.80421  ? 65  LEU A CG  1 
ATOM   563  C CD1 . LEU A 1 67  ? 27.65100 -11.21400 -42.24100 1.000 20.59593  ? 65  LEU A CD1 1 
ATOM   564  C CD2 . LEU A 1 67  ? 29.21900 -13.26500 -42.29500 1.000 19.42117  ? 65  LEU A CD2 1 
ATOM   565  N N   . MET A 1 68  ? 27.00000 -9.94800  -38.64500 1.000 18.60575  ? 66  MET A N   1 
ATOM   566  C CA  . MET A 1 68  ? 26.07400 -10.29200 -37.57400 1.000 20.38952  ? 66  MET A CA  1 
ATOM   567  C C   . MET A 1 68  ? 25.20400 -11.45900 -37.96800 1.000 20.03868  ? 66  MET A C   1 
ATOM   568  O O   . MET A 1 68  ? 24.87300 -12.30900 -37.12000 1.000 21.26101  ? 66  MET A O   1 
ATOM   569  C CB  . MET A 1 68  ? 25.19600 -9.08900  -37.21500 1.000 21.52864  ? 66  MET A CB  1 
ATOM   570  C CG  . MET A 1 68  ? 25.98100 -7.86900  -36.77000 1.000 22.99730  ? 66  MET A CG  1 
ATOM   571  S SD  . MET A 1 68  ? 27.09700 -8.16200  -35.38200 1.000 28.03167  ? 66  MET A SD  1 
ATOM   572  C CE  . MET A 1 68  ? 25.90400 -8.66800  -34.14200 1.000 31.88445  ? 66  MET A CE  1 
ATOM   573  N N   . ASN A 1 69  ? 24.91200 -11.57300 -39.25000 1.000 19.03709  ? 67  ASN A N   1 
ATOM   574  C CA  . ASN A 1 69  ? 24.00400 -12.61700 -39.69700 1.000 18.45312  ? 67  ASN A CA  1 
ATOM   575  C C   . ASN A 1 69  ? 24.01900 -12.64800 -41.20300 1.000 18.35964  ? 67  ASN A C   1 
ATOM   576  O O   . ASN A 1 69  ? 24.13600 -11.60500 -41.84100 1.000 19.09387  ? 67  ASN A O   1 
ATOM   577  C CB  . ASN A 1 69  ? 22.57300 -12.34900 -39.20700 1.000 19.31049  ? 67  ASN A CB  1 
ATOM   578  C CG  . ASN A 1 69  ? 21.70300 -13.60100 -39.22900 1.000 21.31801  ? 67  ASN A CG  1 
ATOM   579  O OD1 . ASN A 1 69  ? 22.12900 -14.68600 -39.71600 1.000 20.69648  ? 67  ASN A OD1 1 
ATOM   580  N ND2 . ASN A 1 69  ? 20.51500 -13.48100 -38.65100 1.000 22.39310  ? 67  ASN A ND2 1 
ATOM   581  N N   . ILE A 1 70  ? 23.89900 -13.84500 -41.76000 1.000 18.19376  ? 68  ILE A N   1 
ATOM   582  C CA  . ILE A 1 70  ? 23.71200 -14.02000 -43.20300 1.000 16.95303  ? 68  ILE A CA  1 
ATOM   583  C C   . ILE A 1 70  ? 22.88500 -15.27100 -43.36300 1.000 14.71402  ? 68  ILE A C   1 
ATOM   584  O O   . ILE A 1 70  ? 23.08700 -16.23400 -42.62500 1.000 16.43444  ? 68  ILE A O   1 
ATOM   585  C CB  . ILE A 1 70  ? 25.05000 -14.10900 -43.97000 1.000 15.35499  ? 68  ILE A CB  1 
ATOM   586  C CG1 . ILE A 1 70  ? 24.80200 -14.28800 -45.44500 1.000 13.82445  ? 68  ILE A CG1 1 
ATOM   587  C CG2 . ILE A 1 70  ? 25.88200 -15.27600 -43.49000 1.000 18.27214  ? 68  ILE A CG2 1 
ATOM   588  C CD1 . ILE A 1 70  ? 26.14200 -14.31100 -46.28300 1.000 21.25978  ? 68  ILE A CD1 1 
ATOM   589  N N   . ALA A 1 71  ? 21.86800 -15.22600 -44.23100 1.000 15.90986  ? 69  ALA A N   1 
ATOM   590  C CA  . ALA A 1 71  ? 20.99500 -16.39600 -44.33900 1.000 13.71584  ? 69  ALA A CA  1 
ATOM   591  C C   . ALA A 1 71  ? 20.34500 -16.37900 -45.72200 1.000 12.02899  ? 69  ALA A C   1 
ATOM   592  O O   . ALA A 1 71  ? 20.06300 -15.30200 -46.26500 1.000 14.15525  ? 69  ALA A O   1 
ATOM   593  C CB  . ALA A 1 71  ? 19.92200 -16.43100 -43.22100 1.000 17.07527  ? 69  ALA A CB  1 
ATOM   594  N N   . VAL A 1 72  ? 20.12300 -17.58100 -46.27000 1.000 13.05008  ? 70  VAL A N   1 
ATOM   595  C CA  . VAL A 1 72  ? 19.48500 -17.78000 -47.58600 1.000 13.94404  ? 70  VAL A CA  1 
ATOM   596  C C   . VAL A 1 72  ? 18.40400 -18.83300 -47.43800 1.000 17.26525  ? 70  VAL A C   1 
ATOM   597  O O   . VAL A 1 72  ? 18.61900 -19.86600 -46.80200 1.000 15.76295  ? 70  VAL A O   1 
ATOM   598  C CB  . VAL A 1 72  ? 20.51200 -18.18700 -48.65200 1.000 14.08242  ? 70  VAL A CB  1 
ATOM   599  C CG1 . VAL A 1 72  ? 19.87900 -18.56400 -49.97500 1.000 14.35902  ? 70  VAL A CG1 1 
ATOM   600  C CG2 . VAL A 1 72  ? 21.55600 -17.02200 -48.82700 1.000 12.39784  ? 70  VAL A CG2 1 
ATOM   601  N N   . ALA A 1 73  ? 17.23800 -18.55400 -47.98200 1.000 13.99669  ? 71  ALA A N   1 
ATOM   602  C CA  . ALA A 1 73  ? 16.14300 -19.49800 -47.87100 1.000 15.08126  ? 71  ALA A CA  1 
ATOM   603  C C   . ALA A 1 73  ? 16.57600 -20.84500 -48.44000 1.000 15.84816  ? 71  ALA A C   1 
ATOM   604  O O   . ALA A 1 73  ? 17.26400 -20.90700 -49.47300 1.000 14.93045  ? 71  ALA A O   1 
ATOM   605  C CB  . ALA A 1 73  ? 14.92600 -18.93800 -48.60800 1.000 18.68896  ? 71  ALA A CB  1 
ATOM   606  N N   . PRO A 1 74  ? 16.20300 -21.96100 -47.80900 1.000 15.70980  ? 72  PRO A N   1 
ATOM   607  C CA  . PRO A 1 74  ? 16.77000 -23.25300 -48.22900 1.000 19.81443  ? 72  PRO A CA  1 
ATOM   608  C C   . PRO A 1 74  ? 16.55800 -23.61300 -49.69600 1.000 15.77917  ? 72  PRO A C   1 
ATOM   609  O O   . PRO A 1 74  ? 17.43600 -24.20800 -50.31500 1.000 21.02083  ? 72  PRO A O   1 
ATOM   610  C CB  . PRO A 1 74  ? 16.07800 -24.25700 -47.30700 1.000 23.44439  ? 72  PRO A CB  1 
ATOM   611  C CG  . PRO A 1 74  ? 15.70100 -23.46200 -46.09000 1.000 23.56467  ? 72  PRO A CG  1 
ATOM   612  C CD  . PRO A 1 74  ? 15.40300 -22.05400 -46.57100 1.000 19.35826  ? 72  PRO A CD  1 
ATOM   613  N N   . ARG A 1 75  ? 15.40800 -23.27200 -50.26400 1.000 17.01046  ? 73  ARG A N   1 
ATOM   614  C CA  . ARG A 1 75  ? 15.19700 -23.54600 -51.67800 1.000 20.92932  ? 73  ARG A CA  1 
ATOM   615  C C   . ARG A 1 75  ? 16.10900 -22.76400 -52.60400 1.000 23.74711  ? 73  ARG A C   1 
ATOM   616  O O   . ARG A 1 75  ? 16.23000 -23.14900 -53.78900 1.000 21.38922  ? 73  ARG A O   1 
ATOM   617  C CB  . ARG A 1 75  ? 13.75000 -23.24700 -52.03400 1.000 19.73051  ? 73  ARG A CB  1 
ATOM   618  C CG  . ARG A 1 75  ? 12.88300 -24.27700 -51.40600 1.000 32.02270  ? 73  ARG A CG  1 
ATOM   619  C CD  . ARG A 1 75  ? 11.49700 -24.16100 -51.83400 1.000 25.86162  ? 73  ARG A CD  1 
ATOM   620  N NE  . ARG A 1 75  ? 10.74100 -25.12200 -51.03400 1.000 30.25894  ? 73  ARG A NE  1 
ATOM   621  C CZ  . ARG A 1 75  ? 10.66000 -26.41800 -51.27200 1.000 30.22515  ? 73  ARG A CZ  1 
ATOM   622  N NH1 . ARG A 1 75  ? 11.10400 -26.95100 -52.40100 1.000 38.34375  ? 73  ARG A NH1 1 
ATOM   623  N NH2 . ARG A 1 75  ? 10.10500 -27.21000 -50.35500 1.000 53.12475  ? 73  ARG A NH2 1 
ATOM   624  N N   . TYR A 1 76  ? 16.75100 -21.69800 -52.11300 1.000 17.79238  ? 74  TYR A N   1 
ATOM   625  C CA  . TYR A 1 76  ? 17.66200 -20.88800 -52.91400 1.000 16.93304  ? 74  TYR A CA  1 
ATOM   626  C C   . TYR A 1 76  ? 19.13700 -21.06300 -52.54600 1.000 18.43471  ? 74  TYR A C   1 
ATOM   627  O O   . TYR A 1 76  ? 19.99100 -20.37200 -53.10900 1.000 19.06379  ? 74  TYR A O   1 
ATOM   628  C CB  . TYR A 1 76  ? 17.25800 -19.41100 -52.81800 1.000 16.19550  ? 74  TYR A CB  1 
ATOM   629  C CG  . TYR A 1 76  ? 15.95800 -19.17400 -53.58200 1.000 16.88879  ? 74  TYR A CG  1 
ATOM   630  C CD1 . TYR A 1 76  ? 14.68700 -19.47700 -53.02700 1.000 17.37834  ? 74  TYR A CD1 1 
ATOM   631  C CD2 . TYR A 1 76  ? 15.99100 -18.79600 -54.94600 1.000 21.34921  ? 74  TYR A CD2 1 
ATOM   632  C CE1 . TYR A 1 76  ? 13.52400 -19.30800 -53.78100 1.000 19.43462  ? 74  TYR A CE1 1 
ATOM   633  C CE2 . TYR A 1 76  ? 14.83800 -18.63900 -55.69600 1.000 20.75192  ? 74  TYR A CE2 1 
ATOM   634  C CZ  . TYR A 1 76  ? 13.60000 -18.89900 -55.11300 1.000 21.11879  ? 74  TYR A CZ  1 
ATOM   635  O OH  . TYR A 1 76  ? 12.44000 -18.74600 -55.79200 1.000 23.48211  ? 74  TYR A OH  1 
ATOM   636  N N   . GLN A 1 77  ? 19.46100 -22.01600 -51.69100 1.000 16.69560  ? 75  GLN A N   1 
ATOM   637  C CA  . GLN A 1 77  ? 20.82900 -22.26100 -51.27200 1.000 19.33933  ? 75  GLN A CA  1 
ATOM   638  C C   . GLN A 1 77  ? 21.63400 -22.97200 -52.35500 1.000 23.44519  ? 75  GLN A C   1 
ATOM   639  O O   . GLN A 1 77  ? 21.08700 -23.60400 -53.27400 1.000 26.40307  ? 75  GLN A O   1 
ATOM   640  C CB  . GLN A 1 77  ? 20.80600 -23.08500 -49.97000 1.000 24.39206  ? 75  GLN A CB  1 
ATOM   641  C CG  . GLN A 1 77  ? 20.31700 -22.28000 -48.80900 1.000 16.88892  ? 75  GLN A CG  1 
ATOM   642  C CD  . GLN A 1 77  ? 20.32200 -23.02100 -47.48100 1.000 15.54450  ? 75  GLN A CD  1 
ATOM   643  O OE1 . GLN A 1 77  ? 20.61800 -24.23400 -47.43000 1.000 18.68794  ? 75  GLN A OE1 1 
ATOM   644  N NE2 . GLN A 1 77  ? 19.97300 -22.33400 -46.43700 1.000 16.01845  ? 75  GLN A NE2 1 
ATOM   645  N N   . ARG A 1 78  ? 22.95900 -22.85700 -52.22900 1.000 22.88907  ? 76  ARG A N   1 
ATOM   646  C CA  . ARG A 1 78  ? 23.93200 -23.49200 -53.10000 1.000 23.46049  ? 76  ARG A CA  1 
ATOM   647  C C   . ARG A 1 78  ? 23.79100 -22.99100 -54.52700 1.000 23.60842  ? 76  ARG A C   1 
ATOM   648  O O   . ARG A 1 78  ? 24.04600 -23.73300 -55.48200 1.000 25.80682  ? 76  ARG A O   1 
ATOM   649  C CB  . ARG A 1 78  ? 23.84800 -25.02000 -53.03100 1.000 28.10925  ? 76  ARG A CB  1 
ATOM   650  C CG  . ARG A 1 78  ? 23.91400 -25.54300 -51.56900 1.000 29.54083  ? 76  ARG A CG  1 
ATOM   651  C CD  . ARG A 1 78  ? 25.21700 -25.19100 -50.87700 1.000 29.10645  ? 76  ARG A CD  1 
ATOM   652  N NE  . ARG A 1 78  ? 26.39400 -25.83500 -51.47600 1.000 27.06492  ? 76  ARG A NE  1 
ATOM   653  C CZ  . ARG A 1 78  ? 26.87500 -27.02600 -51.12700 1.000 27.09749  ? 76  ARG A CZ  1 
ATOM   654  N NH1 . ARG A 1 78  ? 26.26800 -27.78400 -50.22400 1.000 34.51337  ? 76  ARG A NH1 1 
ATOM   655  N NH2 . ARG A 1 78  ? 27.96500 -27.48300 -51.72500 1.000 30.73171  ? 76  ARG A NH2 1 
ATOM   656  N N   . LYS A 1 79  ? 23.42400 -21.70800 -54.68300 1.000 24.27273  ? 77  LYS A N   1 
ATOM   657  C CA  . LYS A 1 79  ? 23.42200 -21.06900 -55.99400 1.000 28.29760  ? 77  LYS A CA  1 
ATOM   658  C C   . LYS A 1 79  ? 24.25100 -19.78200 -56.03500 1.000 27.23857  ? 77  LYS A C   1 
ATOM   659  O O   . LYS A 1 79  ? 24.20000 -19.05800 -57.04200 1.000 28.17934  ? 77  LYS A O   1 
ATOM   660  C CB  . LYS A 1 79  ? 21.97300 -20.78900 -56.43200 1.000 33.08408  ? 77  LYS A CB  1 
ATOM   661  C CG  . LYS A 1 79  ? 21.08400 -22.03100 -56.38100 1.000 42.08338  ? 77  LYS A CG  1 
ATOM   662  C CD  . LYS A 1 79  ? 21.62900 -23.17400 -57.26200 1.000 50.84186  ? 77  LYS A CD  1 
ATOM   663  C CE  . LYS A 1 79  ? 21.68600 -22.80900 -58.75000 1.000 53.42762  ? 77  LYS A CE  1 
ATOM   664  N NZ  . LYS A 1 79  ? 22.66300 -23.61000 -59.54300 1.000 51.59850  ? 77  LYS A NZ  1 
ATOM   665  N N   . GLY A 1 80  ? 25.04000 -19.49700 -54.99600 1.000 20.09466  ? 78  GLY A N   1 
ATOM   666  C CA  . GLY A 1 80  ? 25.80800 -18.27600 -54.93900 1.000 24.06142  ? 78  GLY A CA  1 
ATOM   667  C C   . GLY A 1 80  ? 25.11700 -17.07200 -54.31200 1.000 22.45821  ? 78  GLY A C   1 
ATOM   668  O O   . GLY A 1 80  ? 25.70600 -15.96100 -54.35200 1.000 20.61227  ? 78  GLY A O   1 
ATOM   669  N N   . VAL A 1 81  ? 23.88500 -17.21800 -53.80500 1.000 19.63894  ? 79  VAL A N   1 
ATOM   670  C CA  . VAL A 1 81  ? 23.19600 -16.07500 -53.19900 1.000 23.26251  ? 79  VAL A CA  1 
ATOM   671  C C   . VAL A 1 81  ? 24.02000 -15.45400 -52.06600 1.000 22.60853  ? 79  VAL A C   1 
ATOM   672  O O   . VAL A 1 81  ? 24.21300 -14.22500 -52.02300 1.000 18.81588  ? 79  VAL A O   1 
ATOM   673  C CB  . VAL A 1 81  ? 21.80300 -16.47000 -52.69200 1.000 16.23631  ? 79  VAL A CB  1 
ATOM   674  C CG1 . VAL A 1 81  ? 21.21700 -15.29600 -51.92700 1.000 15.47555  ? 79  VAL A CG1 1 
ATOM   675  C CG2 . VAL A 1 81  ? 20.87200 -16.80700 -53.89100 1.000 18.87549  ? 79  VAL A CG2 1 
ATOM   676  N N   . ALA A 1 82  ? 24.44400 -16.27300 -51.06700 1.000 15.30968  ? 80  ALA A N   1 
ATOM   677  C CA  . ALA A 1 82  ? 25.20100 -15.69500 -49.96000 1.000 13.16275  ? 80  ALA A CA  1 
ATOM   678  C C   . ALA A 1 82  ? 26.51600 -15.11200 -50.44100 1.000 17.42689  ? 80  ALA A C   1 
ATOM   679  O O   . ALA A 1 82  ? 26.99600 -14.10100 -49.89600 1.000 19.80342  ? 80  ALA A O   1 
ATOM   680  C CB  . ALA A 1 82  ? 25.48000 -16.75400 -48.90600 1.000 16.25906  ? 80  ALA A CB  1 
ATOM   681  N N   . SER A 1 83  ? 27.14400 -15.75900 -51.43700 1.000 17.70673  ? 81  SER A N   1 
ATOM   682  C CA  . SER A 1 83  ? 28.39400 -15.23900 -51.98900 1.000 16.97794  ? 81  SER A CA  1 
ATOM   683  C C   . SER A 1 83  ? 28.21200 -13.82900 -52.52900 1.000 21.44041  ? 81  SER A C   1 
ATOM   684  O O   . SER A 1 83  ? 29.05000 -12.94800 -52.28400 1.000 21.47494  ? 81  SER A O   1 
ATOM   685  C CB  . SER A 1 83  ? 28.90800 -16.15800 -53.09300 1.000 20.83057  ? 81  SER A CB  1 
ATOM   686  O OG  . SER A 1 83  ? 29.26700 -17.38600 -52.44000 1.000 20.78578  ? 81  SER A OG  1 
ATOM   687  N N   . GLN A 1 84  ? 27.11700 -13.59200 -53.24100 1.000 22.20947  ? 82  GLN A N   1 
ATOM   688  C CA  . GLN A 1 84  ? 26.86900 -12.27200 -53.81300 1.000 22.82078  ? 82  GLN A CA  1 
ATOM   689  C C   . GLN A 1 84  ? 26.58100 -11.26400 -52.70300 1.000 21.61104  ? 82  GLN A C   1 
ATOM   690  O O   . GLN A 1 84  ? 27.06900 -10.11200 -52.75800 1.000 23.47630  ? 82  GLN A O   1 
ATOM   691  C CB  . GLN A 1 84  ? 25.69300 -12.34400 -54.79800 1.000 24.63900  ? 82  GLN A CB  1 
ATOM   692  C CG  . GLN A 1 84  ? 25.96400 -13.13200 -55.99700 1.000 26.87873  ? 82  GLN A CG  1 
ATOM   693  C CD  . GLN A 1 84  ? 24.94500 -12.89300 -57.04300 1.000 34.13100  ? 82  GLN A CD  1 
ATOM   694  O OE1 . GLN A 1 84  ? 24.72400 -11.75800 -57.45000 1.000 36.13733  ? 82  GLN A OE1 1 
ATOM   695  N NE2 . GLN A 1 84  ? 24.31000 -13.95700 -57.50400 1.000 39.73095  ? 82  GLN A NE2 1 
ATOM   696  N N   . LEU A 1 85  ? 25.80600 -11.68200 -51.69300 1.000 18.84068  ? 83  LEU A N   1 
ATOM   697  C CA  . LEU A 1 85  ? 25.44000 -10.78300 -50.59800 1.000 18.15599  ? 83  LEU A CA  1 
ATOM   698  C C   . LEU A 1 85  ? 26.67600 -10.37700 -49.82300 1.000 20.21340  ? 83  LEU A C   1 
ATOM   699  O O   . LEU A 1 85  ? 26.89400 -9.19400  -49.54200 1.000 19.30937  ? 83  LEU A O   1 
ATOM   700  C CB  . LEU A 1 85  ? 24.42200 -11.46200 -49.69000 1.000 15.63443  ? 83  LEU A CB  1 
ATOM   701  C CG  . LEU A 1 85  ? 22.99300 -11.34300 -50.19700 1.000 18.11780  ? 83  LEU A CG  1 
ATOM   702  C CD1 . LEU A 1 85  ? 22.09800 -12.15000 -49.22800 1.000 19.32047  ? 83  LEU A CD1 1 
ATOM   703  C CD2 . LEU A 1 85  ? 22.58000 -9.88600  -50.19000 1.000 21.39349  ? 83  LEU A CD2 1 
ATOM   704  N N   . LEU A 1 86  ? 27.55800 -11.34000 -49.57700 1.000 16.66493  ? 84  LEU A N   1 
ATOM   705  C CA  . LEU A 1 86  ? 28.80300 -11.05900 -48.87100 1.000 19.44500  ? 84  LEU A CA  1 
ATOM   706  C C   . LEU A 1 86  ? 29.71800 -10.14000 -49.68800 1.000 20.89678  ? 84  LEU A C   1 
ATOM   707  O O   . LEU A 1 86  ? 30.32700 -9.20800  -49.14800 1.000 25.11429  ? 84  LEU A O   1 
ATOM   708  C CB  . LEU A 1 86  ? 29.48700 -12.38400 -48.55500 1.000 19.00638  ? 84  LEU A CB  1 
ATOM   709  C CG  . LEU A 1 86  ? 30.84000 -12.10700 -47.87600 1.000 19.17716  ? 84  LEU A CG  1 
ATOM   710  C CD1 . LEU A 1 86  ? 30.59800 -11.41100 -46.55600 1.000 22.78899  ? 84  LEU A CD1 1 
ATOM   711  C CD2 . LEU A 1 86  ? 31.48000 -13.45100 -47.64800 1.000 19.24550  ? 84  LEU A CD2 1 
ATOM   712  N N   . GLN A 1 87  ? 29.80500 -10.35800 -51.00900 1.000 21.46085  ? 85  GLN A N   1 
ATOM   713  C CA  . GLN A 1 87  ? 30.61100 -9.48100  -51.84800 1.000 24.56792  ? 85  GLN A CA  1 
ATOM   714  C C   . GLN A 1 87  ? 30.10900 -8.04600  -51.74600 1.000 25.85183  ? 85  GLN A C   1 
ATOM   715  O O   . GLN A 1 87  ? 30.90300 -7.11500  -51.65200 1.000 27.63802  ? 85  GLN A O   1 
ATOM   716  C CB  . GLN A 1 87  ? 30.57200 -9.99700  -53.29200 1.000 26.75607  ? 85  GLN A CB  1 
ATOM   717  C CG  . GLN A 1 87  ? 31.53300 -9.39000  -54.24800 1.000 39.00099  ? 85  GLN A CG  1 
ATOM   718  C CD  . GLN A 1 87  ? 31.56600 -10.19900 -55.53700 1.000 44.54177  ? 85  GLN A CD  1 
ATOM   719  O OE1 . GLN A 1 87  ? 30.53100 -10.41600 -56.16400 1.000 46.93735  ? 85  GLN A OE1 1 
ATOM   720  N NE2 . GLN A 1 87  ? 32.74500 -10.70500 -55.89800 1.000 56.16720  ? 85  GLN A NE2 1 
ATOM   721  N N   . HIS A 1 88  ? 28.77500 -7.86000  -51.73500 1.000 25.39694  ? 86  HIS A N   1 
ATOM   722  C CA  . HIS A 1 88  ? 28.20700 -6.51800  -51.67700 1.000 27.31959  ? 86  HIS A CA  1 
ATOM   723  C C   . HIS A 1 88  ? 28.51700 -5.88000  -50.33400 1.000 26.09646  ? 86  HIS A C   1 
ATOM   724  O O   . HIS A 1 88  ? 28.87600 -4.69500  -50.26700 1.000 28.08605  ? 86  HIS A O   1 
ATOM   725  C CB  . HIS A 1 88  ? 26.68800 -6.58700  -51.88800 1.000 27.23860  ? 86  HIS A CB  1 
ATOM   726  C CG  . HIS A 1 88  ? 26.16700 -5.56600  -52.83400 1.000 37.68310  ? 86  HIS A CG  1 
ATOM   727  N ND1 . HIS A 1 88  ? 26.06300 -5.81000  -54.18800 1.000 55.57369  ? 86  HIS A ND1 1 
ATOM   728  C CD2 . HIS A 1 88  ? 25.78600 -4.27700  -52.65400 1.000 43.30158  ? 86  HIS A CD2 1 
ATOM   729  C CE1 . HIS A 1 88  ? 25.58500 -4.74000  -54.78500 1.000 48.23728  ? 86  HIS A CE1 1 
ATOM   730  N NE2 . HIS A 1 88  ? 25.47600 -3.77000  -53.89400 1.000 49.25463  ? 86  HIS A NE2 1 
ATOM   731  N N   . ALA A 1 89  ? 28.33000 -6.65200  -49.26500 1.000 24.04139  ? 87  ALA A N   1 
ATOM   732  C CA  . ALA A 1 89  ? 28.66000 -6.18800  -47.92600 1.000 27.13983  ? 87  ALA A CA  1 
ATOM   733  C C   . ALA A 1 89  ? 30.12500 -5.82000  -47.80100 1.000 23.74166  ? 87  ALA A C   1 
ATOM   734  O O   . ALA A 1 89  ? 30.46700 -4.82700  -47.14500 1.000 28.76589  ? 87  ALA A O   1 
ATOM   735  C CB  . ALA A 1 89  ? 28.31900 -7.26500  -46.91800 1.000 19.96627  ? 87  ALA A CB  1 
ATOM   736  N N   . LEU A 1 90  ? 31.02400 -6.62800  -48.37200 1.000 24.73747  ? 88  LEU A N   1 
ATOM   737  C CA  . LEU A 1 90  ? 32.44700 -6.32900  -48.21400 1.000 26.91109  ? 88  LEU A CA  1 
ATOM   738  C C   . LEU A 1 90  ? 32.88200 -5.12800  -49.04600 1.000 31.70308  ? 88  LEU A C   1 
ATOM   739  O O   . LEU A 1 90  ? 33.81600 -4.40600  -48.67600 1.000 32.81555  ? 88  LEU A O   1 
ATOM   740  C CB  . LEU A 1 90  ? 33.29300 -7.53700  -48.58900 1.000 24.70596  ? 88  LEU A CB  1 
ATOM   741  C CG  . LEU A 1 90  ? 33.20700 -8.73700  -47.66200 1.000 24.54703  ? 88  LEU A CG  1 
ATOM   742  C CD1 . LEU A 1 90  ? 34.25000 -9.69400  -48.19000 1.000 30.45709  ? 88  LEU A CD1 1 
ATOM   743  C CD2 . LEU A 1 90  ? 33.47500 -8.31500  -46.20400 1.000 24.18770  ? 88  LEU A CD2 1 
ATOM   744  N N   . HIS A 1 91  ? 32.24600 -4.89600  -50.18800 1.000 29.94327  ? 89  HIS A N   1 
ATOM   745  C CA  . HIS A 1 91  ? 32.50100 -3.66500  -50.90200 1.000 32.28450  ? 89  HIS A CA  1 
ATOM   746  C C   . HIS A 1 91  ? 32.13100 -2.44900  -50.04700 1.000 32.76685  ? 89  HIS A C   1 
ATOM   747  O O   . HIS A 1 91  ? 32.91100 -1.49700  -49.95900 1.000 34.65940  ? 89  HIS A O   1 
ATOM   748  C CB  . HIS A 1 91  ? 31.77800 -3.67100  -52.24800 1.000 34.16396  ? 89  HIS A CB  1 
ATOM   749  C CG  . HIS A 1 91  ? 32.08100 -2.47600  -53.08400 1.000 37.89745  ? 89  HIS A CG  1 
ATOM   750  N ND1 . HIS A 1 91  ? 31.37800 -1.29900  -52.96800 1.000 40.36565  ? 89  HIS A ND1 1 
ATOM   751  C CD2 . HIS A 1 91  ? 33.02200 -2.26400  -54.03100 1.000 41.15984  ? 89  HIS A CD2 1 
ATOM   752  C CE1 . HIS A 1 91  ? 31.86100 -0.41400  -53.82500 1.000 43.03257  ? 89  HIS A CE1 1 
ATOM   753  N NE2 . HIS A 1 91  ? 32.86500 -0.97300  -54.47800 1.000 47.55371  ? 89  HIS A NE2 1 
ATOM   754  N N   . TYR A 1 92  ? 30.99600 -2.48100  -49.35500 1.000 33.27706  ? 90  TYR A N   1 
ATOM   755  C CA  . TYR A 1 92  ? 30.65500 -1.37500  -48.45800 1.000 32.18563  ? 90  TYR A CA  1 
ATOM   756  C C   . TYR A 1 92  ? 31.69900 -1.21400  -47.36300 1.000 35.13882  ? 90  TYR A C   1 
ATOM   757  O O   . TYR A 1 92  ? 32.19000 -0.10500  -47.12700 1.000 38.84022  ? 90  TYR A O   1 
ATOM   758  C CB  . TYR A 1 92  ? 29.26800 -1.57400  -47.82900 1.000 36.37717  ? 90  TYR A CB  1 
ATOM   759  C CG  . TYR A 1 92  ? 28.92500 -0.45600  -46.84100 1.000 32.40535  ? 90  TYR A CG  1 
ATOM   760  C CD1 . TYR A 1 92  ? 29.30000 -0.52600  -45.48400 1.000 37.69101  ? 90  TYR A CD1 1 
ATOM   761  C CD2 . TYR A 1 92  ? 28.25200 0.68200   -47.26900 1.000 36.68700  ? 90  TYR A CD2 1 
ATOM   762  C CE1 . TYR A 1 92  ? 29.01600 0.52900   -44.59500 1.000 34.24182  ? 90  TYR A CE1 1 
ATOM   763  C CE2 . TYR A 1 92  ? 27.95100 1.71500   -46.40400 1.000 42.36804  ? 90  TYR A CE2 1 
ATOM   764  C CZ  . TYR A 1 92  ? 28.32800 1.63600   -45.07000 1.000 48.95557  ? 90  TYR A CZ  1 
ATOM   765  O OH  . TYR A 1 92  ? 28.03000 2.69000   -44.22900 1.000 59.29239  ? 90  TYR A OH  1 
ATOM   766  N N   . ALA A 1 93  ? 32.03900 -2.31300  -46.67900 1.000 39.32103  ? 91  ALA A N   1 
ATOM   767  C CA  . ALA A 1 93  ? 32.99800 -2.25700  -45.57500 1.000 35.61501  ? 91  ALA A CA  1 
ATOM   768  C C   . ALA A 1 93  ? 34.35600 -1.72800  -46.04100 1.000 35.03205  ? 91  ALA A C   1 
ATOM   769  O O   . ALA A 1 93  ? 34.95400 -0.86700  -45.38700 1.000 33.27361  ? 91  ALA A O   1 
ATOM   770  C CB  . ALA A 1 93  ? 33.12800 -3.64800  -44.92700 1.000 30.44015  ? 91  ALA A CB  1 
ATOM   771  N N   . LYS A 1 94  ? 34.84400 -2.20800  -47.18800 1.000 33.95305  ? 92  LYS A N   1 
ATOM   772  C CA  . LYS A 1 94  ? 36.13800 -1.76100  -47.69900 1.000 34.35335  ? 92  LYS A CA  1 
ATOM   773  C C   . LYS A 1 94  ? 36.12500 -0.26700  -48.03000 1.000 36.85797  ? 92  LYS A C   1 
ATOM   774  O O   . LYS A 1 94  ? 37.15100 0.41400   -47.90100 1.000 43.22304  ? 92  LYS A O   1 
ATOM   775  C CB  . LYS A 1 94  ? 36.51000 -2.60900  -48.92800 1.000 34.76384  ? 92  LYS A CB  1 
ATOM   776  C CG  . LYS A 1 94  ? 37.89500 -2.36300  -49.58600 1.000 37.54055  ? 92  LYS A CG  1 
ATOM   777  C CD  . LYS A 1 94  ? 39.03700 -2.66500  -48.61400 1.000 39.40100  ? 92  LYS A CD  1 
ATOM   778  C CE  . LYS A 1 94  ? 40.41900 -2.65400  -49.30200 1.000 50.02757  ? 92  LYS A CE  1 
ATOM   779  N NZ  . LYS A 1 94  ? 40.65600 -3.93000  -50.06900 1.000 44.55728  ? 92  LYS A NZ  1 
ATOM   780  N N   . THR A 1 95  ? 34.98600 0.26100   -48.48200 1.000 37.20524  ? 93  THR A N   1 
ATOM   781  C CA  . THR A 1 95  ? 34.91800 1.69200   -48.77400 1.000 39.96914  ? 93  THR A CA  1 
ATOM   782  C C   . THR A 1 95  ? 34.90700 2.51600   -47.49700 1.000 40.29945  ? 93  THR A C   1 
ATOM   783  O O   . THR A 1 95  ? 35.29000 3.69600   -47.50200 1.000 45.84089  ? 93  THR A O   1 
ATOM   784  C CB  . THR A 1 95  ? 33.68700 1.96700   -49.63300 1.000 48.03785  ? 93  THR A CB  1 
ATOM   785  O OG1 . THR A 1 95  ? 33.98800 1.59800   -50.98800 1.000 51.61145  ? 93  THR A OG1 1 
ATOM   786  C CG2 . THR A 1 95  ? 33.26300 3.44700   -49.58100 1.000 54.41812  ? 93  THR A CG2 1 
ATOM   787  N N   . HIS A 1 96  ? 34.53400 1.90000   -46.38400 1.000 46.73784  ? 94  HIS A N   1 
ATOM   788  C CA  . HIS A 1 96  ? 34.48400 2.55900   -45.08700 1.000 46.73438  ? 94  HIS A CA  1 
ATOM   789  C C   . HIS A 1 96  ? 35.64300 2.11400   -44.20700 1.000 45.88809  ? 94  HIS A C   1 
ATOM   790  O O   . HIS A 1 96  ? 35.49200 1.85900   -43.00800 1.000 43.94893  ? 94  HIS A O   1 
ATOM   791  C CB  . HIS A 1 96  ? 33.13000 2.29600   -44.44000 1.000 45.02582  ? 94  HIS A CB  1 
ATOM   792  C CG  . HIS A 1 96  ? 32.01500 3.03000   -45.11900 1.000 47.23299  ? 94  HIS A CG  1 
ATOM   793  N ND1 . HIS A 1 96  ? 31.62100 4.29500   -44.74100 1.000 50.22701  ? 94  HIS A ND1 1 
ATOM   794  C CD2 . HIS A 1 96  ? 31.24200 2.69500   -46.17900 1.000 47.61730  ? 94  HIS A CD2 1 
ATOM   795  C CE1 . HIS A 1 96  ? 30.64200 4.70400   -45.52900 1.000 51.93076  ? 94  HIS A CE1 1 
ATOM   796  N NE2 . HIS A 1 96  ? 30.38900 3.74800   -46.40400 1.000 52.22818  ? 94  HIS A NE2 1 
ATOM   797  N N   . HIS A 1 97  ? 36.79500 1.93000   -44.84800 1.000 49.35851  ? 95  HIS A N   1 
ATOM   798  C CA  . HIS A 1 97  ? 38.08900 1.76900   -44.18700 1.000 50.80926  ? 95  HIS A CA  1 
ATOM   799  C C   . HIS A 1 97  ? 38.17000 0.52400   -43.29900 1.000 48.87462  ? 95  HIS A C   1 
ATOM   800  O O   . HIS A 1 97  ? 38.88600 0.52700   -42.29600 1.000 46.03406  ? 95  HIS A O   1 
ATOM   801  C CB  . HIS A 1 97  ? 38.42800 3.02900   -43.39700 1.000 49.39041  ? 95  HIS A CB  1 
ATOM   802  C CG  . HIS A 1 97  ? 38.27500 4.27800   -44.20500 1.000 52.79186  ? 95  HIS A CG  1 
ATOM   803  N ND1 . HIS A 1 97  ? 39.25300 4.72900   -45.06200 1.000 59.64722  ? 95  HIS A ND1 1 
ATOM   804  C CD2 . HIS A 1 97  ? 37.23800 5.14000   -44.33200 1.000 56.01398  ? 95  HIS A CD2 1 
ATOM   805  C CE1 . HIS A 1 97  ? 38.83600 5.82700   -45.66700 1.000 58.58438  ? 95  HIS A CE1 1 
ATOM   806  N NE2 . HIS A 1 97  ? 37.61800 6.10100   -45.23600 1.000 57.67447  ? 95  HIS A NE2 1 
ATOM   807  N N   . ALA A 1 98  ? 37.47900 -0.56200  -43.65200 1.000 41.03700  ? 96  ALA A N   1 
ATOM   808  C CA  . ALA A 1 98  ? 37.63300 -1.83300  -42.95400 1.000 38.30480  ? 96  ALA A CA  1 
ATOM   809  C C   . ALA A 1 98  ? 38.39300 -2.83700  -43.82500 1.000 38.13812  ? 96  ALA A C   1 
ATOM   810  O O   . ALA A 1 98  ? 38.39700 -2.73100  -45.05800 1.000 39.53282  ? 96  ALA A O   1 
ATOM   811  C CB  . ALA A 1 98  ? 36.26200 -2.39900  -42.55600 1.000 35.71970  ? 96  ALA A CB  1 
ATOM   812  N N   . THR A 1 99  ? 39.08200 -3.79000  -43.16500 1.000 36.93459  ? 97  THR A N   1 
ATOM   813  C CA  . THR A 1 99  ? 39.88300 -4.81200  -43.83500 1.000 37.12429  ? 97  THR A CA  1 
ATOM   814  C C   . THR A 1 99  ? 39.68000 -6.21100  -43.25300 1.000 34.46092  ? 97  THR A C   1 
ATOM   815  O O   . THR A 1 99  ? 40.12500 -7.19000  -43.85700 1.000 36.13828  ? 97  THR A O   1 
ATOM   816  C CB  . THR A 1 99  ? 41.38600 -4.44600  -43.78000 1.000 44.53659  ? 97  THR A CB  1 
ATOM   817  O OG1 . THR A 1 99  ? 42.13600 -5.32400  -44.62300 1.000 61.46026  ? 97  THR A OG1 1 
ATOM   818  C CG2 . THR A 1 99  ? 41.91000 -4.57900  -42.39000 1.000 39.59907  ? 97  THR A CG2 1 
ATOM   819  N N   . ARG A 1 100 ? 38.98300 -6.34900  -42.13400 1.000 32.45454  ? 98  ARG A N   1 
ATOM   820  C CA  . ARG A 1 100 ? 38.84400 -7.63700  -41.48200 1.000 30.75097  ? 98  ARG A CA  1 
ATOM   821  C C   . ARG A 1 100 ? 37.39400 -7.79800  -41.06800 1.000 28.06108  ? 98  ARG A C   1 
ATOM   822  O O   . ARG A 1 100 ? 36.84000 -6.90400  -40.41900 1.000 33.48392  ? 98  ARG A O   1 
ATOM   823  C CB  . ARG A 1 100 ? 39.74300 -7.74900  -40.24500 1.000 32.66378  ? 98  ARG A CB  1 
ATOM   824  C CG  . ARG A 1 100 ? 41.22200 -7.61500  -40.50700 1.000 33.53588  ? 98  ARG A CG  1 
ATOM   825  C CD  . ARG A 1 100 ? 41.95600 -7.44900  -39.19000 1.000 37.71152  ? 98  ARG A CD  1 
ATOM   826  N NE  . ARG A 1 100 ? 41.74200 -8.58000  -38.30400 1.000 48.25108  ? 98  ARG A NE  1 
ATOM   827  C CZ  . ARG A 1 100 ? 42.47000 -9.68700  -38.32900 1.000 56.10468  ? 98  ARG A CZ  1 
ATOM   828  N NH1 . ARG A 1 100 ? 43.44100 -9.85400  -39.21700 1.000 47.75683  ? 98  ARG A NH1 1 
ATOM   829  N NH2 . ARG A 1 100 ? 42.22900 -10.64500 -37.43100 1.000 38.32746  ? 98  ARG A NH2 1 
ATOM   830  N N   . LEU A 1 101 ? 36.77500 -8.91200  -41.45900 1.000 27.99784  ? 99  LEU A N   1 
ATOM   831  C CA  . LEU A 1 101 ? 35.40100 -9.22800  -41.09800 1.000 24.50109  ? 99  LEU A CA  1 
ATOM   832  C C   . LEU A 1 101 ? 35.37100 -10.35100 -40.06200 1.000 22.84735  ? 99  LEU A C   1 
ATOM   833  O O   . LEU A 1 101 ? 35.77600 -11.47700 -40.36600 1.000 25.13710  ? 99  LEU A O   1 
ATOM   834  C CB  . LEU A 1 101 ? 34.61700 -9.66200  -42.34100 1.000 24.27302  ? 99  LEU A CB  1 
ATOM   835  C CG  . LEU A 1 101 ? 33.12200 -9.90600  -42.14200 1.000 22.94644  ? 99  LEU A CG  1 
ATOM   836  C CD1 . LEU A 1 101 ? 32.38600 -8.63100  -41.87200 1.000 29.68181  ? 99  LEU A CD1 1 
ATOM   837  C CD2 . LEU A 1 101 ? 32.50700 -10.62200 -43.35000 1.000 23.95985  ? 99  LEU A CD2 1 
ATOM   838  N N   . LEU A 1 102 ? 34.80700 -10.06200 -38.87400 1.000 27.82754  ? 100 LEU A N   1 
ATOM   839  C CA  . LEU A 1 102 ? 34.63500 -11.01700 -37.76700 1.000 24.85143  ? 100 LEU A CA  1 
ATOM   840  C C   . LEU A 1 102 ? 33.31400 -11.77200 -37.84300 1.000 21.35790  ? 100 LEU A C   1 
ATOM   841  O O   . LEU A 1 102 ? 32.25800 -11.19100 -38.10700 1.000 23.07025  ? 100 LEU A O   1 
ATOM   842  C CB  . LEU A 1 102 ? 34.66500 -10.26200 -36.43200 1.000 22.43998  ? 100 LEU A CB  1 
ATOM   843  C CG  . LEU A 1 102 ? 34.69600 -10.99000 -35.07800 1.000 34.32346  ? 100 LEU A CG  1 
ATOM   844  C CD1 . LEU A 1 102 ? 36.01300 -11.68200 -34.92300 1.000 32.23358  ? 100 LEU A CD1 1 
ATOM   845  C CD2 . LEU A 1 102 ? 34.53300 -9.99300  -33.92100 1.000 36.66493  ? 100 LEU A CD2 1 
ATOM   846  N N   . LEU A 1 103 ? 33.35500 -13.07900 -37.62400 1.000 19.16632  ? 101 LEU A N   1 
ATOM   847  C CA  . LEU A 1 103 ? 32.11800 -13.85400 -37.54600 1.000 17.29317  ? 101 LEU A CA  1 
ATOM   848  C C   . LEU A 1 103 ? 32.18400 -14.72700 -36.31400 1.000 18.84830  ? 101 LEU A C   1 
ATOM   849  O O   . LEU A 1 103 ? 33.18600 -15.42200 -36.12600 1.000 22.38733  ? 101 LEU A O   1 
ATOM   850  C CB  . LEU A 1 103 ? 31.93000 -14.78000 -38.73500 1.000 18.60171  ? 101 LEU A CB  1 
ATOM   851  C CG  . LEU A 1 103 ? 30.76100 -15.75500 -38.65200 1.000 18.87706  ? 101 LEU A CG  1 
ATOM   852  C CD1 . LEU A 1 103 ? 29.45200 -14.90400 -38.60600 1.000 20.35483  ? 101 LEU A CD1 1 
ATOM   853  C CD2 . LEU A 1 103 ? 30.72800 -16.65100 -39.90500 1.000 17.90064  ? 101 LEU A CD2 1 
ATOM   854  N N   . GLU A 1 104 ? 31.11700 -14.74500 -35.51900 1.000 21.82469  ? 102 GLU A N   1 
ATOM   855  C CA  . GLU A 1 104 ? 30.94900 -15.70100 -34.43500 1.000 21.05558  ? 102 GLU A CA  1 
ATOM   856  C C   . GLU A 1 104 ? 29.73200 -16.54200 -34.73600 1.000 25.49471  ? 102 GLU A C   1 
ATOM   857  O O   . GLU A 1 104 ? 28.65900 -16.00400 -35.05400 1.000 24.74767  ? 102 GLU A O   1 
ATOM   858  C CB  . GLU A 1 104 ? 30.79400 -14.99600 -33.08300 1.000 18.82424  ? 102 GLU A CB  1 
ATOM   859  C CG  . GLU A 1 104 ? 31.89900 -14.05600 -32.74800 1.000 30.12014  ? 102 GLU A CG  1 
ATOM   860  C CD  . GLU A 1 104 ? 31.70500 -13.43400 -31.37700 1.000 43.14485  ? 102 GLU A CD  1 
ATOM   861  O OE1 . GLU A 1 104 ? 30.57700 -13.53500 -30.83400 1.000 49.97606  ? 102 GLU A OE1 1 
ATOM   862  O OE2 . GLU A 1 104 ? 32.67800 -12.85000 -30.85400 1.000 45.15299  ? 102 GLU A OE2 1 
ATOM   863  N N   . VAL A 1 105 ? 29.90600 -17.85000 -34.67500 1.000 19.28580  ? 103 VAL A N   1 
ATOM   864  C CA  . VAL A 1 105 ? 28.90900 -18.79100 -35.13900 1.000 19.83440  ? 103 VAL A CA  1 
ATOM   865  C C   . VAL A 1 105 ? 28.90900 -19.98100 -34.18700 1.000 21.94439  ? 103 VAL A C   1 
ATOM   866  O O   . VAL A 1 105 ? 29.94000 -20.32000 -33.60200 1.000 21.93658  ? 103 VAL A O   1 
ATOM   867  C CB  . VAL A 1 105 ? 29.20700 -19.19800 -36.61300 1.000 22.78424  ? 103 VAL A CB  1 
ATOM   868  C CG1 . VAL A 1 105 ? 30.52100 -19.93100 -36.68900 1.000 23.98839  ? 103 VAL A CG1 1 
ATOM   869  C CG2 . VAL A 1 105 ? 28.13200 -20.04200 -37.18700 1.000 31.29864  ? 103 VAL A CG2 1 
ATOM   870  N N   . ARG A 1 106 ? 27.74900 -20.60400 -33.99800 1.000 22.70466  ? 104 ARG A N   1 
ATOM   871  C CA  . ARG A 1 106 ? 27.68100 -21.82500 -33.17900 1.000 18.68020  ? 104 ARG A CA  1 
ATOM   872  C C   . ARG A 1 106 ? 28.56300 -22.92500 -33.75500 1.000 22.84879  ? 104 ARG A C   1 
ATOM   873  O O   . ARG A 1 106 ? 28.64600 -23.10500 -34.97200 1.000 20.91035  ? 104 ARG A O   1 
ATOM   874  C CB  . ARG A 1 106 ? 26.23500 -22.35500 -33.10600 1.000 19.31978  ? 104 ARG A CB  1 
ATOM   875  C CG  . ARG A 1 106 ? 25.30400 -21.58400 -32.21700 1.000 22.41390  ? 104 ARG A CG  1 
ATOM   876  C CD  . ARG A 1 106 ? 23.83000 -21.98200 -32.47600 1.000 23.23331  ? 104 ARG A CD  1 
ATOM   877  N NE  . ARG A 1 106 ? 22.92000 -21.20600 -31.63800 1.000 22.98878  ? 104 ARG A NE  1 
ATOM   878  C CZ  . ARG A 1 106 ? 22.54700 -21.52900 -30.40400 1.000 26.76037  ? 104 ARG A CZ  1 
ATOM   879  N NH1 . ARG A 1 106 ? 23.00400 -22.61700 -29.79200 1.000 24.92363  ? 104 ARG A NH1 1 
ATOM   880  N NH2 . ARG A 1 106 ? 21.72100 -20.72100 -29.74600 1.000 25.29314  ? 104 ARG A NH2 1 
ATOM   881  N N   . LYS A 1 107 ? 29.20900 -23.68100 -32.86100 1.000 20.56020  ? 105 LYS A N   1 
ATOM   882  C CA  . LYS A 1 107 ? 30.09900 -24.75400 -33.29100 1.000 25.48219  ? 105 LYS A CA  1 
ATOM   883  C C   . LYS A 1 107 ? 29.40000 -25.75800 -34.19500 1.000 22.48570  ? 105 LYS A C   1 
ATOM   884  O O   . LYS A 1 107 ? 30.03900 -26.32900 -35.09600 1.000 23.70912  ? 105 LYS A O   1 
ATOM   885  C CB  . LYS A 1 107 ? 30.65000 -25.45600 -32.06400 1.000 26.68559  ? 105 LYS A CB  1 
ATOM   886  C CG  . LYS A 1 107 ? 31.80600 -26.38000 -32.34900 1.000 24.94149  ? 105 LYS A CG  1 
ATOM   887  C CD  . LYS A 1 107 ? 32.60300 -26.63500 -31.07700 1.000 27.67477  ? 105 LYS A CD  1 
ATOM   888  C CE  . LYS A 1 107 ? 31.87000 -27.57700 -30.18800 1.000 40.44674  ? 105 LYS A CE  1 
ATOM   889  N NZ  . LYS A 1 107 ? 31.38000 -28.67900 -31.04500 1.000 48.30495  ? 105 LYS A NZ  1 
ATOM   890  N N   . SER A 1 108 ? 28.09600 -25.97900 -33.99000 1.000 20.62633  ? 106 SER A N   1 
ATOM   891  C CA  . SER A 1 108 ? 27.34200 -26.97000 -34.73900 1.000 21.57327  ? 106 SER A CA  1 
ATOM   892  C C   . SER A 1 108 ? 26.81500 -26.43100 -36.06600 1.000 21.73372  ? 106 SER A C   1 
ATOM   893  O O   . SER A 1 108 ? 26.22100 -27.19700 -36.84400 1.000 24.23986  ? 106 SER A O   1 
ATOM   894  C CB  . SER A 1 108 ? 26.15300 -27.49800 -33.88400 1.000 22.88664  ? 106 SER A CB  1 
ATOM   895  O OG  . SER A 1 108 ? 25.20000 -26.48000 -33.63200 1.000 24.45321  ? 106 SER A OG  1 
ATOM   896  N N   . ASN A 1 109 ? 27.03200 -25.14500 -36.36400 1.000 18.84537  ? 107 ASN A N   1 
ATOM   897  C CA  . ASN A 1 109 ? 26.42600 -24.51700 -37.53800 1.000 18.05600  ? 107 ASN A CA  1 
ATOM   898  C C   . ASN A 1 109 ? 27.32700 -24.78000 -38.73400 1.000 23.95458  ? 107 ASN A C   1 
ATOM   899  O O   . ASN A 1 109 ? 27.98000 -23.88300 -39.26600 1.000 22.85472  ? 107 ASN A O   1 
ATOM   900  C CB  . ASN A 1 109 ? 26.21700 -23.02800 -37.31100 1.000 17.55775  ? 107 ASN A CB  1 
ATOM   901  C CG  . ASN A 1 109 ? 25.31500 -22.38900 -38.35600 1.000 18.91684  ? 107 ASN A CG  1 
ATOM   902  O OD1 . ASN A 1 109 ? 25.06400 -22.97700 -39.42600 1.000 19.67612  ? 107 ASN A OD1 1 
ATOM   903  N ND2 . ASN A 1 109 ? 24.80900 -21.21600 -38.04700 1.000 18.30074  ? 107 ASN A ND2 1 
ATOM   904  N N   . ARG A 1 110 ? 27.25700 -26.00900 -39.20500 1.000 27.27484  ? 108 ARG A N   1 
ATOM   905  C CA  . ARG A 1 110 ? 28.16000 -26.51200 -40.23100 1.000 28.62389  ? 108 ARG A CA  1 
ATOM   906  C C   . ARG A 1 110 ? 28.06700 -25.70400 -41.51500 1.000 28.51542  ? 108 ARG A C   1 
ATOM   907  O O   . ARG A 1 110 ? 29.09700 -25.41300 -42.14700 1.000 28.82473  ? 108 ARG A O   1 
ATOM   908  C CB  . ARG A 1 110 ? 27.83900 -27.98100 -40.51200 1.000 35.00734  ? 108 ARG A CB  1 
ATOM   909  C CG  . ARG A 1 110 ? 28.11500 -28.89200 -39.31200 1.000 46.06001  ? 108 ARG A CG  1 
ATOM   910  C CD  . ARG A 1 110 ? 29.48200 -28.57700 -38.66100 1.000 42.39947  ? 108 ARG A CD  1 
ATOM   911  N NE  . ARG A 1 110 ? 30.48900 -28.30900 -39.68200 1.000 54.33557  ? 108 ARG A NE  1 
ATOM   912  C CZ  . ARG A 1 110 ? 31.79400 -28.46000 -39.53100 1.000 51.05600  ? 108 ARG A CZ  1 
ATOM   913  N NH1 . ARG A 1 110 ? 32.31200 -28.99700 -38.43300 1.000 64.56721  ? 108 ARG A NH1 1 
ATOM   914  N NH2 . ARG A 1 110 ? 32.59900 -28.07500 -40.51200 1.000 56.17750  ? 108 ARG A NH2 1 
ATOM   915  N N   . SER A 1 111 ? 26.84500 -25.38100 -41.94900 1.000 25.33723  ? 109 SER A N   1 
ATOM   916  C CA  . SER A 1 111 ? 26.72700 -24.72700 -43.25300 1.000 21.65013  ? 109 SER A CA  1 
ATOM   917  C C   . SER A 1 111 ? 27.36100 -23.34100 -43.23100 1.000 22.40145  ? 109 SER A C   1 
ATOM   918  O O   . SER A 1 111 ? 28.04100 -22.95800 -44.20100 1.000 24.50922  ? 109 SER A O   1 
ATOM   919  C CB  . SER A 1 111 ? 25.26400 -24.65300 -43.72200 1.000 23.16392  ? 109 SER A CB  1 
ATOM   920  O OG  . SER A 1 111 ? 24.46700 -23.72500 -42.98500 1.000 25.41094  ? 109 SER A OG  1 
ATOM   921  N N   . ALA A 1 112 ? 27.10500 -22.55500 -42.17200 1.000 20.38698  ? 110 ALA A N   1 
ATOM   922  C CA  . ALA A 1 112 ? 27.69900 -21.22200 -42.09300 1.000 19.51035  ? 110 ALA A CA  1 
ATOM   923  C C   . ALA A 1 112 ? 29.21300 -21.32100 -41.98700 1.000 18.05597  ? 110 ALA A C   1 
ATOM   924  O O   . ALA A 1 112 ? 29.94000 -20.52600 -42.58900 1.000 17.41859  ? 110 ALA A O   1 
ATOM   925  C CB  . ALA A 1 112 ? 27.10800 -20.42100 -40.91100 1.000 23.42727  ? 110 ALA A CB  1 
ATOM   926  N N   . ILE A 1 113 ? 29.71200 -22.33700 -41.27100 1.000 17.56757  ? 111 ILE A N   1 
ATOM   927  C CA  . ILE A 1 113 ? 31.15300 -22.51900 -41.13200 1.000 22.14470  ? 111 ILE A CA  1 
ATOM   928  C C   . ILE A 1 113 ? 31.78900 -22.81700 -42.49500 1.000 22.35234  ? 111 ILE A C   1 
ATOM   929  O O   . ILE A 1 113 ? 32.79000 -22.21400 -42.88700 1.000 21.03853  ? 111 ILE A O   1 
ATOM   930  C CB  . ILE A 1 113 ? 31.45100 -23.64900 -40.13300 1.000 24.54772  ? 111 ILE A CB  1 
ATOM   931  C CG1 . ILE A 1 113 ? 31.09900 -23.19100 -38.70300 1.000 25.42160  ? 111 ILE A CG1 1 
ATOM   932  C CG2 . ILE A 1 113 ? 32.90700 -24.06600 -40.26800 1.000 27.22991  ? 111 ILE A CG2 1 
ATOM   933  C CD1 . ILE A 1 113 ? 30.94400 -24.32100 -37.67400 1.000 23.93810  ? 111 ILE A CD1 1 
ATOM   934  N N   . GLU A 1 114 ? 31.23800 -23.79900 -43.21200 1.000 23.81929  ? 112 GLU A N   1 
ATOM   935  C CA  . GLU A 1 114 ? 31.81900 -24.17700 -44.49900 1.000 20.48344  ? 112 GLU A CA  1 
ATOM   936  C C   . GLU A 1 114 ? 31.68600 -23.05100 -45.51200 1.000 23.39654  ? 112 GLU A C   1 
ATOM   937  O O   . GLU A 1 114 ? 32.62300 -22.81500 -46.27500 1.000 21.70291  ? 112 GLU A O   1 
ATOM   938  C CB  . GLU A 1 114 ? 31.16400 -25.44700 -45.01600 1.000 33.06306  ? 112 GLU A CB  1 
ATOM   939  C CG  . GLU A 1 114 ? 31.45300 -26.64700 -44.11400 1.000 35.11386  ? 112 GLU A CG  1 
ATOM   940  C CD  . GLU A 1 114 ? 32.95700 -26.94300 -43.96300 1.000 47.10399  ? 112 GLU A CD  1 
ATOM   941  O OE1 . GLU A 1 114 ? 33.69600 -26.86600 -44.95700 1.000 44.79770  ? 112 GLU A OE1 1 
ATOM   942  O OE2 . GLU A 1 114 ? 33.40900 -27.24600 -42.83400 1.000 49.63525  ? 112 GLU A OE2 1 
ATOM   943  N N   . PHE A 1 115 ? 30.59900 -22.29400 -45.47200 1.000 20.12953  ? 113 PHE A N   1 
ATOM   944  C CA  . PHE A 1 115 ? 30.46500 -21.13600 -46.35300 1.000 17.92745  ? 113 PHE A CA  1 
ATOM   945  C C   . PHE A 1 115 ? 31.56600 -20.12200 -46.08300 1.000 22.50078  ? 113 PHE A C   1 
ATOM   946  O O   . PHE A 1 115 ? 32.23200 -19.62700 -46.99800 1.000 18.81164  ? 113 PHE A O   1 
ATOM   947  C CB  . PHE A 1 115 ? 29.10300 -20.47200 -46.16500 1.000 19.50449  ? 113 PHE A CB  1 
ATOM   948  C CG  . PHE A 1 115 ? 29.02600 -19.13000 -46.81100 1.000 19.04826  ? 113 PHE A CG  1 
ATOM   949  C CD1 . PHE A 1 115 ? 28.84600 -19.02100 -48.18900 1.000 17.55074  ? 113 PHE A CD1 1 
ATOM   950  C CD2 . PHE A 1 115 ? 29.15600 -17.96600 -46.03100 1.000 15.89333  ? 113 PHE A CD2 1 
ATOM   951  C CE1 . PHE A 1 115 ? 28.79800 -17.75100 -48.80000 1.000 18.60758  ? 113 PHE A CE1 1 
ATOM   952  C CE2 . PHE A 1 115 ? 29.10700 -16.66700 -46.63900 1.000 18.71514  ? 113 PHE A CE2 1 
ATOM   953  C CZ  . PHE A 1 115 ? 28.97900 -16.59100 -48.03600 1.000 18.32339  ? 113 PHE A CZ  1 
ATOM   954  N N   . TYR A 1 116 ? 31.77600 -19.80500 -44.81200 1.000 19.80683  ? 114 TYR A N   1 
ATOM   955  C CA  . TYR A 1 116 ? 32.73300 -18.76200 -44.50100 1.000 18.19478  ? 114 TYR A CA  1 
ATOM   956  C C   . TYR A 1 116 ? 34.13400 -19.19600 -44.84100 1.000 19.62073  ? 114 TYR A C   1 
ATOM   957  O O   . TYR A 1 116 ? 34.93100 -18.39500 -45.33900 1.000 20.72401  ? 114 TYR A O   1 
ATOM   958  C CB  . TYR A 1 116 ? 32.60000 -18.41000 -43.03400 1.000 19.21015  ? 114 TYR A CB  1 
ATOM   959  C CG  . TYR A 1 116 ? 32.98500 -16.96900 -42.73000 1.000 18.03846  ? 114 TYR A CG  1 
ATOM   960  C CD1 . TYR A 1 116 ? 32.24300 -15.91600 -43.26600 1.000 17.53920  ? 114 TYR A CD1 1 
ATOM   961  C CD2 . TYR A 1 116 ? 34.01800 -16.67700 -41.89200 1.000 20.03854  ? 114 TYR A CD2 1 
ATOM   962  C CE1 . TYR A 1 116 ? 32.57500 -14.58700 -42.93700 1.000 22.78588  ? 114 TYR A CE1 1 
ATOM   963  C CE2 . TYR A 1 116 ? 34.37300 -15.36200 -41.58500 1.000 20.09927  ? 114 TYR A CE2 1 
ATOM   964  C CZ  . TYR A 1 116 ? 33.64400 -14.34200 -42.10000 1.000 22.08795  ? 114 TYR A CZ  1 
ATOM   965  O OH  . TYR A 1 116 ? 33.98200 -13.05700 -41.77400 1.000 23.06271  ? 114 TYR A OH  1 
ATOM   966  N N   . LYS A 1 117 ? 34.44900 -20.45800 -44.60800 1.000 20.31155  ? 115 LYS A N   1 
ATOM   967  C CA  . LYS A 1 117 ? 35.77900 -20.95200 -44.92900 1.000 21.95002  ? 115 LYS A CA  1 
ATOM   968  C C   . LYS A 1 117 ? 36.05100 -20.87800 -46.43400 1.000 25.03874  ? 115 LYS A C   1 
ATOM   969  O O   . LYS A 1 117 ? 37.15600 -20.50900 -46.84500 1.000 24.98055  ? 115 LYS A O   1 
ATOM   970  C CB  . LYS A 1 117 ? 35.93300 -22.38300 -44.42800 1.000 26.69535  ? 115 LYS A CB  1 
ATOM   971  C CG  . LYS A 1 117 ? 36.16600 -22.45300 -42.92000 1.000 31.06274  ? 115 LYS A CG  1 
ATOM   972  C CD  . LYS A 1 117 ? 36.39800 -23.88900 -42.44600 1.000 28.66652  ? 115 LYS A CD  1 
ATOM   973  C CE  . LYS A 1 117 ? 37.60900 -24.53800 -43.11300 1.000 42.05804  ? 115 LYS A CE  1 
ATOM   974  N NZ  . LYS A 1 117 ? 38.80400 -23.64700 -43.16300 1.000 53.59594  ? 115 LYS A NZ  1 
ATOM   975  N N   . LYS A 1 118 ? 35.06200 -21.20800 -47.26000 1.000 27.35444  ? 116 LYS A N   1 
ATOM   976  C CA  . LYS A 1 118 ? 35.28700 -21.13800 -48.71100 1.000 24.03106  ? 116 LYS A CA  1 
ATOM   977  C C   . LYS A 1 118 ? 35.32700 -19.71500 -49.24100 1.000 24.74209  ? 116 LYS A C   1 
ATOM   978  O O   . LYS A 1 118 ? 35.70800 -19.52100 -50.40400 1.000 26.04801  ? 116 LYS A O   1 
ATOM   979  C CB  . LYS A 1 118 ? 34.20300 -21.92900 -49.45500 1.000 29.34469  ? 116 LYS A CB  1 
ATOM   980  C CG  . LYS A 1 118 ? 34.37700 -23.44600 -49.32300 1.000 41.76378  ? 116 LYS A CG  1 
ATOM   981  C CD  . LYS A 1 118 ? 35.86900 -23.79000 -49.27500 1.000 45.48070  ? 116 LYS A CD  1 
ATOM   982  C CE  . LYS A 1 118 ? 36.14500 -25.29300 -49.14200 1.000 54.27697  ? 116 LYS A CE  1 
ATOM   983  N NZ  . LYS A 1 118 ? 37.25100 -25.63100 -48.17300 1.000 51.80435  ? 116 LYS A NZ  1 
ATOM   984  N N   . ALA A 1 119 ? 34.96600 -18.72700 -48.42900 1.000 21.65504  ? 117 ALA A N   1 
ATOM   985  C CA  . ALA A 1 119 ? 35.09500 -17.30200 -48.73500 1.000 24.20243  ? 117 ALA A CA  1 
ATOM   986  C C   . ALA A 1 119 ? 36.40600 -16.69700 -48.24500 1.000 25.64386  ? 117 ALA A C   1 
ATOM   987  O O   . ALA A 1 119 ? 36.64800 -15.49400 -48.45200 1.000 23.82487  ? 117 ALA A O   1 
ATOM   988  C CB  . ALA A 1 119 ? 33.92600 -16.54300 -48.10200 1.000 20.23301  ? 117 ALA A CB  1 
ATOM   989  N N   . GLY A 1 120 ? 37.26600 -17.49400 -47.62400 1.000 23.50718  ? 118 GLY A N   1 
ATOM   990  C CA  . GLY A 1 120 ? 38.51300 -17.01400 -47.08900 1.000 24.74995  ? 118 GLY A CA  1 
ATOM   991  C C   . GLY A 1 120 ? 38.57200 -16.86300 -45.58400 1.000 24.34306  ? 118 GLY A C   1 
ATOM   992  O O   . GLY A 1 120 ? 39.58700 -16.35000 -45.09000 1.000 27.24129  ? 118 GLY A O   1 
ATOM   993  N N   . GLY A 1 121 ? 37.51400 -17.25800 -44.85700 1.000 23.47937  ? 119 GLY A N   1 
ATOM   994  C CA  . GLY A 1 121 ? 37.52700 -17.11400 -43.40100 1.000 22.71625  ? 119 GLY A CA  1 
ATOM   995  C C   . GLY A 1 121 ? 38.45300 -18.10600 -42.72600 1.000 23.85549  ? 119 GLY A C   1 
ATOM   996  O O   . GLY A 1 121 ? 38.64400 -19.21900 -43.18800 1.000 24.31637  ? 119 GLY A O   1 
ATOM   997  N N   . VAL A 1 122 ? 39.04300 -17.68800 -41.61000 1.000 24.60223  ? 120 VAL A N   1 
ATOM   998  C CA  . VAL A 1 122 ? 40.00500 -18.50400 -40.86100 1.000 34.02976  ? 120 VAL A CA  1 
ATOM   999  C C   . VAL A 1 122 ? 39.59100 -18.49600 -39.40200 1.000 28.92556  ? 120 VAL A C   1 
ATOM   1000 O O   . VAL A 1 122 ? 39.29700 -17.42500 -38.85500 1.000 26.21715  ? 120 VAL A O   1 
ATOM   1001 C CB  . VAL A 1 122 ? 41.44400 -17.98000 -40.99000 1.000 27.98009  ? 120 VAL A CB  1 
ATOM   1002 C CG1 . VAL A 1 122 ? 42.40600 -18.75400 -40.08400 1.000 29.64964  ? 120 VAL A CG1 1 
ATOM   1003 C CG2 . VAL A 1 122 ? 41.90800 -18.04100 -42.41700 1.000 28.56426  ? 120 VAL A CG2 1 
ATOM   1004 N N   . GLU A 1 123 ? 39.58900 -19.67200 -38.77100 1.000 26.13950  ? 121 GLU A N   1 
ATOM   1005 C CA  . GLU A 1 123 ? 39.24200 -19.70200 -37.35500 1.000 26.19496  ? 121 GLU A CA  1 
ATOM   1006 C C   . GLU A 1 123 ? 40.36600 -19.09200 -36.54300 1.000 27.96604  ? 121 GLU A C   1 
ATOM   1007 O O   . GLU A 1 123 ? 41.54500 -19.46700 -36.69000 1.000 29.64777  ? 121 GLU A O   1 
ATOM   1008 C CB  . GLU A 1 123 ? 38.94600 -21.12100 -36.87200 1.000 26.51180  ? 121 GLU A CB  1 
ATOM   1009 C CG  . GLU A 1 123 ? 38.52100 -21.15000 -35.40600 1.000 27.63969  ? 121 GLU A CG  1 
ATOM   1010 C CD  . GLU A 1 123 ? 38.37800 -22.54500 -34.85900 1.000 36.65721  ? 121 GLU A CD  1 
ATOM   1011 O OE1 . GLU A 1 123 ? 37.99100 -23.44200 -35.63000 1.000 43.45588  ? 121 GLU A OE1 1 
ATOM   1012 O OE2 . GLU A 1 123 ? 38.63200 -22.74600 -33.65100 1.000 32.74060  ? 121 GLU A OE2 1 
ATOM   1013 N N   . ILE A 1 124 ? 40.00000 -18.18800 -35.63100 1.000 27.87371  ? 122 ILE A N   1 
ATOM   1014 C CA  . ILE A 1 124 ? 40.96900 -17.52900 -34.76400 1.000 29.79273  ? 122 ILE A CA  1 
ATOM   1015 C C   . ILE A 1 124 ? 40.71700 -17.80000 -33.28900 1.000 30.49388  ? 122 ILE A C   1 
ATOM   1016 O O   . ILE A 1 124 ? 41.61300 -17.53000 -32.47100 1.000 32.49976  ? 122 ILE A O   1 
ATOM   1017 C CB  . ILE A 1 124 ? 41.03100 -16.01100 -35.02700 1.000 30.39207  ? 122 ILE A CB  1 
ATOM   1018 C CG1 . ILE A 1 124 ? 39.66300 -15.34500 -34.81900 1.000 28.37142  ? 122 ILE A CG1 1 
ATOM   1019 C CG2 . ILE A 1 124 ? 41.57700 -15.77800 -36.46100 1.000 29.93934  ? 122 ILE A CG2 1 
ATOM   1020 C CD1 . ILE A 1 124 ? 39.71100 -13.82800 -34.72700 1.000 29.15631  ? 122 ILE A CD1 1 
ATOM   1021 N N   . GLY A 1 125 ? 39.57500 -18.35700 -32.92000 1.000 31.29692  ? 123 GLY A N   1 
ATOM   1022 C CA  . GLY A 1 125 ? 39.36400 -18.64100 -31.50300 1.000 30.15782  ? 123 GLY A CA  1 
ATOM   1023 C C   . GLY A 1 125 ? 38.06000 -19.36200 -31.25700 1.000 28.76343  ? 123 GLY A C   1 
ATOM   1024 O O   . GLY A 1 125 ? 37.23100 -19.53700 -32.15400 1.000 27.22967  ? 123 GLY A O   1 
ATOM   1025 N N   . VAL A 1 126 ? 37.87100 -19.75400 -29.99400 1.000 29.83697  ? 124 VAL A N   1 
ATOM   1026 C CA  . VAL A 1 126 ? 36.61900 -20.34100 -29.51800 1.000 28.96389  ? 124 VAL A CA  1 
ATOM   1027 C C   . VAL A 1 126 ? 36.19700 -19.57100 -28.27000 1.000 29.76407  ? 124 VAL A C   1 
ATOM   1028 O O   . VAL A 1 126 ? 37.03100 -19.24600 -27.42400 1.000 31.73397  ? 124 VAL A O   1 
ATOM   1029 C CB  . VAL A 1 126 ? 36.77800 -21.84400 -29.18900 1.000 36.15337  ? 124 VAL A CB  1 
ATOM   1030 C CG1 . VAL A 1 126 ? 35.50700 -22.40100 -28.63500 1.000 33.00014  ? 124 VAL A CG1 1 
ATOM   1031 C CG2 . VAL A 1 126 ? 37.25900 -22.64300 -30.42300 1.000 32.07295  ? 124 VAL A CG2 1 
ATOM   1032 N N   . ARG A 1 127 ? 34.90500 -19.23400 -28.18400 1.000 28.44246  ? 125 ARG A N   1 
ATOM   1033 C CA  . ARG A 1 127 ? 34.29500 -18.78200 -26.93100 1.000 31.89845  ? 125 ARG A CA  1 
ATOM   1034 C C   . ARG A 1 127 ? 33.48900 -19.95400 -26.39500 1.000 29.39445  ? 125 ARG A C   1 
ATOM   1035 O O   . ARG A 1 127 ? 32.45600 -20.30500 -26.95800 1.000 27.78753  ? 125 ARG A O   1 
ATOM   1036 C CB  . ARG A 1 127 ? 33.39900 -17.55300 -27.14200 1.000 28.32116  ? 125 ARG A CB  1 
ATOM   1037 C CG  . ARG A 1 127 ? 34.08200 -16.33000 -27.79800 1.000 36.68216  ? 125 ARG A CG  1 
ATOM   1038 C CD  . ARG A 1 127 ? 33.17300 -15.08600 -27.71600 1.000 40.63971  ? 125 ARG A CD  1 
ATOM   1039 N NE  . ARG A 1 127 ? 33.73300 -13.95400 -28.43800 1.000 49.15616  ? 125 ARG A NE  1 
ATOM   1040 C CZ  . ARG A 1 127 ? 34.66200 -13.13800 -27.96500 1.000 53.22950  ? 125 ARG A CZ  1 
ATOM   1041 N NH1 . ARG A 1 127 ? 35.11700 -13.25100 -26.72600 1.000 61.77100  ? 125 ARG A NH1 1 
ATOM   1042 N NH2 . ARG A 1 127 ? 35.16800 -12.20100 -28.76300 1.000 59.89351  ? 125 ARG A NH2 1 
ATOM   1043 N N   . LYS A 1 128 ? 33.92100 -20.52400 -25.27700 1.000 31.45125  ? 126 LYS A N   1 
ATOM   1044 C CA  . LYS A 1 128 ? 33.26200 -21.70200 -24.74100 1.000 31.92360  ? 126 LYS A CA  1 
ATOM   1045 C C   . LYS A 1 128 ? 31.91900 -21.31900 -24.12900 1.000 36.63473  ? 126 LYS A C   1 
ATOM   1046 O O   . LYS A 1 128 ? 31.80800 -20.30600 -23.41900 1.000 33.72693  ? 126 LYS A O   1 
ATOM   1047 C CB  . LYS A 1 128 ? 34.13200 -22.35500 -23.66500 1.000 34.61445  ? 126 LYS A CB  1 
ATOM   1048 C CG  . LYS A 1 128 ? 35.43500 -22.88500 -24.12700 1.000 36.69694  ? 126 LYS A CG  1 
ATOM   1049 C CD  . LYS A 1 128 ? 35.31100 -24.12600 -24.98600 1.000 34.85100  ? 126 LYS A CD  1 
ATOM   1050 C CE  . LYS A 1 128 ? 34.60000 -25.27000 -24.31600 1.000 45.57195  ? 126 LYS A CE  1 
ATOM   1051 N NZ  . LYS A 1 128 ? 34.75300 -26.44900 -25.21800 1.000 41.76371  ? 126 LYS A NZ  1 
ATOM   1052 N N   . ASN A 1 129 ? 30.90600 -22.14800 -24.39000 1.000 30.62336  ? 127 ASN A N   1 
ATOM   1053 C CA  . ASN A 1 129 ? 29.62100 -22.04700 -23.71500 1.000 30.67958  ? 127 ASN A CA  1 
ATOM   1054 C C   . ASN A 1 129 ? 29.06800 -20.63800 -23.84900 1.000 33.94172  ? 127 ASN A C   1 
ATOM   1055 O O   . ASN A 1 129 ? 28.63600 -20.01000 -22.88100 1.000 34.79102  ? 127 ASN A O   1 
ATOM   1056 C CB  . ASN A 1 129 ? 29.75000 -22.45100 -22.24500 1.000 33.26764  ? 127 ASN A CB  1 
ATOM   1057 C CG  . ASN A 1 129 ? 30.05600 -23.92100 -22.06500 1.000 39.93381  ? 127 ASN A CG  1 
ATOM   1058 O OD1 . ASN A 1 129 ? 29.37900 -24.78700 -22.62700 1.000 37.42577  ? 127 ASN A OD1 1 
ATOM   1059 N ND2 . ASN A 1 129 ? 31.11100 -24.21400 -21.29600 1.000 46.87137  ? 127 ASN A ND2 1 
ATOM   1060 N N   . TYR A 1 130 ? 29.08900 -20.13800 -25.07400 1.000 29.11865  ? 128 TYR A N   1 
ATOM   1061 C CA  . TYR A 1 130 ? 28.69300 -18.77000 -25.33800 1.000 29.20429  ? 128 TYR A CA  1 
ATOM   1062 C C   . TYR A 1 130 ? 27.21400 -18.64900 -25.66100 1.000 30.88781  ? 128 TYR A C   1 
ATOM   1063 O O   . TYR A 1 130 ? 26.61100 -17.62700 -25.33700 1.000 35.02551  ? 128 TYR A O   1 
ATOM   1064 C CB  . TYR A 1 130 ? 29.52500 -18.22200 -26.49100 1.000 30.59536  ? 128 TYR A CB  1 
ATOM   1065 C CG  . TYR A 1 130 ? 29.19800 -16.81600 -26.93200 1.000 36.27351  ? 128 TYR A CG  1 
ATOM   1066 C CD1 . TYR A 1 130 ? 29.75200 -15.71100 -26.28200 1.000 31.33430  ? 128 TYR A CD1 1 
ATOM   1067 C CD2 . TYR A 1 130 ? 28.35500 -16.59000 -28.01200 1.000 32.93610  ? 128 TYR A CD2 1 
ATOM   1068 C CE1 . TYR A 1 130 ? 29.46000 -14.41500 -26.71900 1.000 48.40576  ? 128 TYR A CE1 1 
ATOM   1069 C CE2 . TYR A 1 130 ? 28.05500 -15.32400 -28.45200 1.000 40.47078  ? 128 TYR A CE2 1 
ATOM   1070 C CZ  . TYR A 1 130 ? 28.60500 -14.23200 -27.80400 1.000 50.86361  ? 128 TYR A CZ  1 
ATOM   1071 O OH  . TYR A 1 130 ? 28.30500 -12.95400 -28.24000 1.000 57.57227  ? 128 TYR A OH  1 
ATOM   1072 N N   . TYR A 1 131 ? 26.60500 -19.66900 -26.30100 1.000 27.35107  ? 129 TYR A N   1 
ATOM   1073 C CA  . TYR A 1 131 ? 25.19300 -19.59300 -26.70700 1.000 23.55385  ? 129 TYR A CA  1 
ATOM   1074 C C   . TYR A 1 131 ? 24.35200 -20.50300 -25.83500 1.000 30.54833  ? 129 TYR A C   1 
ATOM   1075 O O   . TYR A 1 131 ? 24.85700 -21.52200 -25.36400 1.000 26.88645  ? 129 TYR A O   1 
ATOM   1076 C CB  . TYR A 1 131 ? 25.01000 -20.07000 -28.14000 1.000 25.12018  ? 129 TYR A CB  1 
ATOM   1077 C CG  . TYR A 1 131 ? 25.72200 -19.32300 -29.21600 1.000 20.73728  ? 129 TYR A CG  1 
ATOM   1078 C CD1 . TYR A 1 131 ? 25.11200 -18.22500 -29.81600 1.000 27.95502  ? 129 TYR A CD1 1 
ATOM   1079 C CD2 . TYR A 1 131 ? 26.92000 -19.78200 -29.75700 1.000 26.01272  ? 129 TYR A CD2 1 
ATOM   1080 C CE1 . TYR A 1 131 ? 25.70300 -17.55500 -30.84400 1.000 34.82316  ? 129 TYR A CE1 1 
ATOM   1081 C CE2 . TYR A 1 131 ? 27.53500 -19.09200 -30.78500 1.000 25.90182  ? 129 TYR A CE2 1 
ATOM   1082 C CZ  . TYR A 1 131 ? 26.90100 -17.96500 -31.33300 1.000 28.91620  ? 129 TYR A CZ  1 
ATOM   1083 O OH  . TYR A 1 131 ? 27.41600 -17.24100 -32.38800 1.000 29.42930  ? 129 TYR A OH  1 
ATOM   1084 N N   . PRO A 1 132 ? 23.06100 -20.20400 -25.64100 1.000 24.75184  ? 130 PRO A N   1 
ATOM   1085 C CA  . PRO A 1 132 ? 22.18500 -21.16900 -24.97100 1.000 26.55998  ? 130 PRO A CA  1 
ATOM   1086 C C   . PRO A 1 132 ? 21.89000 -22.32800 -25.91200 1.000 24.57584  ? 130 PRO A C   1 
ATOM   1087 O O   . PRO A 1 132 ? 21.82000 -22.15800 -27.13500 1.000 27.01826  ? 130 PRO A O   1 
ATOM   1088 C CB  . PRO A 1 132 ? 20.91600 -20.35800 -24.67500 1.000 32.26248  ? 130 PRO A CB  1 
ATOM   1089 C CG  . PRO A 1 132 ? 20.90800 -19.29800 -25.71800 1.000 31.06322  ? 130 PRO A CG  1 
ATOM   1090 C CD  . PRO A 1 132 ? 22.34500 -18.97800 -26.03700 1.000 28.74116  ? 130 PRO A CD  1 
ATOM   1091 N N   . ALA A 1 133 ? 21.80500 -23.51900 -25.34700 1.000 27.72643  ? 131 ALA A N   1 
ATOM   1092 C CA  . ALA A 1 133 ? 21.50500 -24.71300 -26.11500 1.000 30.95282  ? 131 ALA A CA  1 
ATOM   1093 C C   . ALA A 1 133 ? 20.32000 -25.39500 -25.45300 1.000 31.67485  ? 131 ALA A C   1 
ATOM   1094 O O   . ALA A 1 133 ? 19.91600 -25.04600 -24.33500 1.000 32.71346  ? 131 ALA A O   1 
ATOM   1095 C CB  . ALA A 1 133 ? 22.73400 -25.64000 -26.20500 1.000 27.65414  ? 131 ALA A CB  1 
ATOM   1096 N N   . GLU A 1 134 ? 19.73700 -26.38000 -26.14200 1.000 31.75401  ? 132 GLU A N   1 
ATOM   1097 C CA  . GLU A 1 134 ? 18.59100 -27.09300 -25.57800 1.000 40.37378  ? 132 GLU A CA  1 
ATOM   1098 C C   . GLU A 1 134 ? 18.88700 -27.59700 -24.17600 1.000 32.87113  ? 132 GLU A C   1 
ATOM   1099 O O   . GLU A 1 134 ? 18.01900 -27.56700 -23.29800 1.000 36.87482  ? 132 GLU A O   1 
ATOM   1100 C CB  . GLU A 1 134 ? 18.21000 -28.25700 -26.48100 1.000 38.92307  ? 132 GLU A CB  1 
ATOM   1101 C CG  . GLU A 1 134 ? 16.75600 -28.50500 -26.57700 1.000 55.38304  ? 132 GLU A CG  1 
ATOM   1102 C CD  . GLU A 1 134 ? 16.43700 -29.49800 -27.68000 1.000 62.71307  ? 132 GLU A CD  1 
ATOM   1103 O OE1 . GLU A 1 134 ? 16.58300 -29.13000 -28.87600 1.000 56.95329  ? 132 GLU A OE1 1 
ATOM   1104 O OE2 . GLU A 1 134 ? 16.05400 -30.64200 -27.34500 1.000 61.27769  ? 132 GLU A OE2 1 
ATOM   1105 N N   . LYS A 1 135 ? 20.12000 -28.04000 -23.93700 1.000 35.45330  ? 133 LYS A N   1 
ATOM   1106 C CA  . LYS A 1 135 ? 20.62500 -28.33500 -22.59800 1.000 38.13913  ? 133 LYS A CA  1 
ATOM   1107 C C   . LYS A 1 135 ? 22.03900 -27.77600 -22.45900 1.000 36.19405  ? 133 LYS A C   1 
ATOM   1108 O O   . LYS A 1 135 ? 22.89300 -28.01000 -23.31900 1.000 32.87818  ? 133 LYS A O   1 
ATOM   1109 C CB  . LYS A 1 135 ? 20.60400 -29.84300 -22.30200 1.000 39.77686  ? 133 LYS A CB  1 
ATOM   1110 C CG  . LYS A 1 135 ? 19.25600 -30.38700 -21.84800 1.000 50.26728  ? 133 LYS A CG  1 
ATOM   1111 C CD  . LYS A 1 135 ? 18.87400 -29.94100 -20.41900 1.000 56.01473  ? 133 LYS A CD  1 
ATOM   1112 C CE  . LYS A 1 135 ? 17.37000 -29.95500 -20.28700 1.000 52.88366  ? 133 LYS A CE  1 
ATOM   1113 N NZ  . LYS A 1 135 ? 16.83200 -29.48600 -21.61200 1.000 48.89170  ? 133 LYS A NZ  1 
ATOM   1114 N N   . GLY A 1 136 ? 22.28300 -27.02700 -21.38300 1.000 35.35331  ? 134 GLY A N   1 
ATOM   1115 C CA  . GLY A 1 136 ? 23.56200 -26.34900 -21.26000 1.000 34.58061  ? 134 GLY A CA  1 
ATOM   1116 C C   . GLY A 1 136 ? 23.75200 -25.26200 -22.30800 1.000 32.46518  ? 134 GLY A C   1 
ATOM   1117 O O   . GLY A 1 136 ? 22.79500 -24.65100 -22.79800 1.000 30.71358  ? 134 GLY A O   1 
ATOM   1118 N N   . ARG A 1 137 ? 25.01500 -25.00000 -22.63900 1.000 31.66539  ? 135 ARG A N   1 
ATOM   1119 C CA  . ARG A 1 137 ? 25.41100 -23.93300 -23.54400 1.000 29.68209  ? 135 ARG A CA  1 
ATOM   1120 C C   . ARG A 1 137 ? 26.28400 -24.52000 -24.66200 1.000 32.45786  ? 135 ARG A C   1 
ATOM   1121 O O   . ARG A 1 137 ? 26.77100 -25.65200 -24.56300 1.000 30.95413  ? 135 ARG A O   1 
ATOM   1122 C CB  . ARG A 1 137 ? 26.14500 -22.83200 -22.75000 1.000 30.60837  ? 135 ARG A CB  1 
ATOM   1123 C CG  . ARG A 1 137 ? 25.27600 -22.23500 -21.62100 1.000 39.51322  ? 135 ARG A CG  1 
ATOM   1124 C CD  . ARG A 1 137 ? 25.90400 -20.98700 -20.99500 1.000 40.36530  ? 135 ARG A CD  1 
ATOM   1125 N NE  . ARG A 1 137 ? 25.05000 -20.40400 -19.95500 1.000 43.42126  ? 135 ARG A NE  1 
ATOM   1126 C CZ  . ARG A 1 137 ? 25.26900 -20.46000 -18.64800 1.000 50.27666  ? 135 ARG A CZ  1 
ATOM   1127 N NH1 . ARG A 1 137 ? 26.35600 -21.02800 -18.14600 1.000 51.90009  ? 135 ARG A NH1 1 
ATOM   1128 N NH2 . ARG A 1 137 ? 24.38200 -19.91900 -17.82100 1.000 50.96299  ? 135 ARG A NH2 1 
ATOM   1129 N N   . GLU A 1 138 ? 26.49100 -23.73400 -25.72600 1.000 26.90019  ? 136 GLU A N   1 
ATOM   1130 C CA  . GLU A 1 138 ? 27.20100 -24.17000 -26.92100 1.000 31.26039  ? 136 GLU A CA  1 
ATOM   1131 C C   . GLU A 1 138 ? 28.33800 -23.20600 -27.23000 1.000 28.12323  ? 136 GLU A C   1 
ATOM   1132 O O   . GLU A 1 138 ? 28.16800 -21.98200 -27.15000 1.000 25.00731  ? 136 GLU A O   1 
ATOM   1133 C CB  . GLU A 1 138 ? 26.22600 -24.27100 -28.13000 1.000 24.20217  ? 136 GLU A CB  1 
ATOM   1134 C CG  . GLU A 1 138 ? 26.97300 -24.67100 -29.39300 1.000 24.97843  ? 136 GLU A CG  1 
ATOM   1135 C CD  . GLU A 1 138 ? 26.08400 -25.02600 -30.55500 1.000 27.29745  ? 136 GLU A CD  1 
ATOM   1136 O OE1 . GLU A 1 138 ? 24.89500 -24.69400 -30.51300 1.000 23.79931  ? 136 GLU A OE1 1 
ATOM   1137 O OE2 . GLU A 1 138 ? 26.60900 -25.64800 -31.50700 1.000 28.48367  ? 136 GLU A OE2 1 
ATOM   1138 N N   . ASP A 1 139 ? 29.49400 -23.75400 -27.61100 1.000 26.19445  ? 137 ASP A N   1 
ATOM   1139 C CA  . ASP A 1 139 ? 30.64800 -22.94100 -27.94200 1.000 26.12211  ? 137 ASP A CA  1 
ATOM   1140 C C   . ASP A 1 139 ? 30.38000 -22.09900 -29.18800 1.000 27.60217  ? 137 ASP A C   1 
ATOM   1141 O O   . ASP A 1 139 ? 29.67400 -22.50800 -30.10000 1.000 26.54133  ? 137 ASP A O   1 
ATOM   1142 C CB  . ASP A 1 139 ? 31.85200 -23.83700 -28.23700 1.000 27.25057  ? 137 ASP A CB  1 
ATOM   1143 C CG  . ASP A 1 139 ? 32.29800 -24.66900 -27.04300 1.000 31.06461  ? 137 ASP A CG  1 
ATOM   1144 O OD1 . ASP A 1 139 ? 31.76300 -24.49400 -25.93100 1.000 30.47033  ? 137 ASP A OD1 1 
ATOM   1145 O OD2 . ASP A 1 139 ? 33.18700 -25.52100 -27.25500 1.000 35.10733  ? 137 ASP A OD2 1 
ATOM   1146 N N   . ALA A 1 140 ? 31.07100 -20.97300 -29.28200 1.000 26.26837  ? 138 ALA A N   1 
ATOM   1147 C CA  . ALA A 1 140 ? 31.07200 -20.16500 -30.48600 1.000 23.54346  ? 138 ALA A CA  1 
ATOM   1148 C C   . ALA A 1 140 ? 32.44100 -20.26300 -31.12300 1.000 27.33371  ? 138 ALA A C   1 
ATOM   1149 O O   . ALA A 1 140 ? 33.45400 -20.07300 -30.45300 1.000 27.21178  ? 138 ALA A O   1 
ATOM   1150 C CB  . ALA A 1 140 ? 30.73200 -18.70600 -30.16800 1.000 25.31682  ? 138 ALA A CB  1 
ATOM   1151 N N   . LEU A 1 141 ? 32.48300 -20.57000 -32.41200 1.000 22.23495  ? 139 LEU A N   1 
ATOM   1152 C CA  . LEU A 1 141 ? 33.72800 -20.44600 -33.15500 1.000 24.31895  ? 139 LEU A CA  1 
ATOM   1153 C C   . LEU A 1 141 ? 33.87300 -19.01300 -33.66800 1.000 21.98430  ? 139 LEU A C   1 
ATOM   1154 O O   . LEU A 1 141 ? 32.90200 -18.40800 -34.10300 1.000 21.39924  ? 139 LEU A O   1 
ATOM   1155 C CB  . LEU A 1 141 ? 33.75700 -21.45200 -34.31200 1.000 27.45378  ? 139 LEU A CB  1 
ATOM   1156 C CG  . LEU A 1 141 ? 33.52800 -22.92500 -33.95300 1.000 29.79652  ? 139 LEU A CG  1 
ATOM   1157 C CD1 . LEU A 1 141 ? 33.78100 -23.79000 -35.16600 1.000 31.52054  ? 139 LEU A CD1 1 
ATOM   1158 C CD2 . LEU A 1 141 ? 34.41100 -23.36800 -32.75600 1.000 31.25542  ? 139 LEU A CD2 1 
ATOM   1159 N N   . VAL A 1 142 ? 35.10400 -18.49400 -33.67800 1.000 22.51159  ? 140 VAL A N   1 
ATOM   1160 C CA  . VAL A 1 142 ? 35.33100 -17.10300 -34.04600 1.000 23.69422  ? 140 VAL A CA  1 
ATOM   1161 C C   . VAL A 1 142 ? 36.23700 -17.10000 -35.27100 1.000 23.80096  ? 140 VAL A C   1 
ATOM   1162 O O   . VAL A 1 142 ? 37.33300 -17.64300 -35.23100 1.000 23.53808  ? 140 VAL A O   1 
ATOM   1163 C CB  . VAL A 1 142 ? 35.97700 -16.30200 -32.90700 1.000 26.93380  ? 140 VAL A CB  1 
ATOM   1164 C CG1 . VAL A 1 142 ? 36.11300 -14.85300 -33.32100 1.000 27.46737  ? 140 VAL A CG1 1 
ATOM   1165 C CG2 . VAL A 1 142 ? 35.08900 -16.38800 -31.65400 1.000 27.02547  ? 140 VAL A CG2 1 
ATOM   1166 N N   . PHE A 1 143 ? 35.75300 -16.52300 -36.36900 1.000 22.11406  ? 141 PHE A N   1 
ATOM   1167 C CA  . PHE A 1 143 ? 36.51200 -16.49700 -37.61900 1.000 22.12890  ? 141 PHE A CA  1 
ATOM   1168 C C   . PHE A 1 143 ? 36.87100 -15.05700 -37.98200 1.000 23.25993  ? 141 PHE A C   1 
ATOM   1169 O O   . PHE A 1 143 ? 36.12400 -14.12000 -37.65600 1.000 23.43519  ? 141 PHE A O   1 
ATOM   1170 C CB  . PHE A 1 143 ? 35.64600 -17.10200 -38.77600 1.000 22.33116  ? 141 PHE A CB  1 
ATOM   1171 C CG  . PHE A 1 143 ? 35.39800 -18.59600 -38.63900 1.000 22.34717  ? 141 PHE A CG  1 
ATOM   1172 C CD1 . PHE A 1 143 ? 34.32400 -19.06100 -37.90400 1.000 24.82901  ? 141 PHE A CD1 1 
ATOM   1173 C CD2 . PHE A 1 143 ? 36.23400 -19.50500 -39.27100 1.000 27.70787  ? 141 PHE A CD2 1 
ATOM   1174 C CE1 . PHE A 1 143 ? 34.09800 -20.44200 -37.78200 1.000 24.69260  ? 141 PHE A CE1 1 
ATOM   1175 C CE2 . PHE A 1 143 ? 36.00900 -20.89200 -39.16100 1.000 24.34101  ? 141 PHE A CE2 1 
ATOM   1176 C CZ  . PHE A 1 143 ? 34.95100 -21.33700 -38.41500 1.000 23.58150  ? 141 PHE A CZ  1 
ATOM   1177 N N   . ASN A 1 144 ? 37.96800 -14.89400 -38.72400 1.000 24.70893  ? 142 ASN A N   1 
ATOM   1178 C CA  . ASN A 1 144 ? 38.34000 -13.63200 -39.37300 1.000 25.52755  ? 142 ASN A CA  1 
ATOM   1179 C C   . ASN A 1 144 ? 38.39600 -13.84300 -40.87900 1.000 26.29989  ? 142 ASN A C   1 
ATOM   1180 O O   . ASN A 1 144 ? 38.92500 -14.85200 -41.35000 1.000 27.07347  ? 142 ASN A O   1 
ATOM   1181 C CB  . ASN A 1 144 ? 39.70400 -13.10000 -38.94100 1.000 27.89950  ? 142 ASN A CB  1 
ATOM   1182 C CG  . ASN A 1 144 ? 40.05600 -11.80800 -39.67200 1.000 35.38748  ? 142 ASN A CG  1 
ATOM   1183 O OD1 . ASN A 1 144 ? 39.34600 -10.81600 -39.55000 1.000 35.99465  ? 142 ASN A OD1 1 
ATOM   1184 N ND2 . ASN A 1 144 ? 41.11300 -11.83400 -40.47200 1.000 38.68093  ? 142 ASN A ND2 1 
ATOM   1185 N N   . LEU A 1 145 ? 37.85200 -12.89100 -41.62800 1.000 25.01456  ? 143 LEU A N   1 
ATOM   1186 C CA  . LEU A 1 145 ? 38.01600 -12.87200 -43.07700 1.000 24.96512  ? 143 LEU A CA  1 
ATOM   1187 C C   . LEU A 1 145 ? 38.69300 -11.57000 -43.47300 1.000 27.25472  ? 143 LEU A C   1 
ATOM   1188 O O   . LEU A 1 145 ? 38.15400 -10.48800 -43.20800 1.000 30.12601  ? 143 LEU A O   1 
ATOM   1189 C CB  . LEU A 1 145 ? 36.66900 -12.99500 -43.76400 1.000 24.06471  ? 143 LEU A CB  1 
ATOM   1190 C CG  . LEU A 1 145 ? 36.52500 -12.74700 -45.26100 1.000 30.35026  ? 143 LEU A CG  1 
ATOM   1191 C CD1 . LEU A 1 145 ? 37.38600 -13.69700 -45.98400 1.000 32.16210  ? 143 LEU A CD1 1 
ATOM   1192 C CD2 . LEU A 1 145 ? 35.03100 -12.98600 -45.61700 1.000 27.58138  ? 143 LEU A CD2 1 
ATOM   1193 N N   . ASN A 1 146 ? 39.84700 -11.66900 -44.10900 1.000 30.01036  ? 144 ASN A N   1 
ATOM   1194 C CA  . ASN A 1 146 ? 40.53400 -10.49800 -44.64400 1.000 31.35775  ? 144 ASN A CA  1 
ATOM   1195 C C   . ASN A 1 146 ? 40.01600 -10.19600 -46.04200 1.000 34.92755  ? 144 ASN A C   1 
ATOM   1196 O O   . ASN A 1 146 ? 39.62800 -11.09600 -46.78300 1.000 32.17933  ? 144 ASN A O   1 
ATOM   1197 C CB  . ASN A 1 146 ? 42.02700 -10.74100 -44.66300 1.000 35.31917  ? 144 ASN A CB  1 
ATOM   1198 C CG  . ASN A 1 146 ? 42.58100 -10.91500 -43.27500 1.000 43.38298  ? 144 ASN A CG  1 
ATOM   1199 O OD1 . ASN A 1 146 ? 42.32500 -10.08900 -42.38900 1.000 35.36028  ? 144 ASN A OD1 1 
ATOM   1200 N ND2 . ASN A 1 146 ? 43.32000 -12.00800 -43.05900 1.000 38.34036  ? 144 ASN A ND2 1 
ATOM   1201 N N   . PHE A 1 147 ? 39.99300 -8.91000  -46.39000 1.000 32.87519  ? 145 PHE A N   1 
ATOM   1202 C CA  . PHE A 1 147 ? 39.38800 -8.47900  -47.67300 1.000 32.51072  ? 145 PHE A CA  1 
ATOM   1203 C C   . PHE A 1 147 ? 39.91000 -7.12200  -48.03400 1.000 35.62610  ? 145 PHE A C   1 
ATOM   1204 O O   . PHE A 1 147 ? 40.66100 -6.54000  -47.24400 1.000 37.86173  ? 145 PHE A O   1 
ATOM   1205 C CB  . PHE A 1 147 ? 37.84800 -8.47000  -47.61200 1.000 30.03571  ? 145 PHE A CB  1 
ATOM   1206 C CG  . PHE A 1 147 ? 37.25900 -7.46600  -46.63600 1.000 30.67017  ? 145 PHE A CG  1 
ATOM   1207 C CD1 . PHE A 1 147 ? 36.88400 -6.20100  -47.05800 1.000 32.22563  ? 145 PHE A CD1 1 
ATOM   1208 C CD2 . PHE A 1 147 ? 37.00700 -7.83100  -45.33000 1.000 29.78568  ? 145 PHE A CD2 1 
ATOM   1209 C CE1 . PHE A 1 147 ? 36.32600 -5.30100  -46.15900 1.000 36.94799  ? 145 PHE A CE1 1 
ATOM   1210 C CE2 . PHE A 1 147 ? 36.45800 -6.96000  -44.43400 1.000 30.52380  ? 145 PHE A CE2 1 
ATOM   1211 C CZ  . PHE A 1 147 ? 36.10500 -5.67900  -44.84700 1.000 41.15278  ? 145 PHE A CZ  1 
ATOM   1212 O OXT . PHE A 1 147 ? 39.61500 -6.59500  -49.13400 1.000 36.20472  ? 145 PHE A OXT 1 
ATOM   1213 N N   . MET B 1 3   ? 17.84500 -23.14100 6.46500   1.000 69.69765  ? 1   MET B N   1 
ATOM   1214 C CA  . MET B 1 3   ? 17.11000 -23.10300 5.19800   1.000 77.28820  ? 1   MET B CA  1 
ATOM   1215 C C   . MET B 1 3   ? 16.08500 -21.95200 5.16600   1.000 78.69606  ? 1   MET B C   1 
ATOM   1216 O O   . MET B 1 3   ? 15.06600 -22.00900 5.85400   1.000 81.94482  ? 1   MET B O   1 
ATOM   1217 C CB  . MET B 1 3   ? 16.41300 -24.45900 4.95300   1.000 83.68504  ? 1   MET B CB  1 
ATOM   1218 C CG  . MET B 1 3   ? 15.49800 -24.53200 3.71000   1.000 83.85030  ? 1   MET B CG  1 
ATOM   1219 S SD  . MET B 1 3   ? 14.49200 -26.05000 3.51600   1.000 93.82803  ? 1   MET B SD  1 
ATOM   1220 C CE  . MET B 1 3   ? 13.75400 -26.22100 5.14800   1.000 73.70495  ? 1   MET B CE  1 
ATOM   1221 N N   . LYS B 1 4   ? 16.35100 -20.90900 4.37000   1.000 66.78226  ? 2   LYS B N   1 
ATOM   1222 C CA  . LYS B 1 4   ? 15.41900 -19.79300 4.21400   1.000 59.77026  ? 2   LYS B CA  1 
ATOM   1223 C C   . LYS B 1 4   ? 15.35000 -19.40000 2.74300   1.000 63.78709  ? 2   LYS B C   1 
ATOM   1224 O O   . LYS B 1 4   ? 16.03800 -19.96700 1.89000   1.000 57.83382  ? 2   LYS B O   1 
ATOM   1225 C CB  . LYS B 1 4   ? 15.81600 -18.57400 5.06700   1.000 72.51995  ? 2   LYS B CB  1 
ATOM   1226 C CG  . LYS B 1 4   ? 16.96800 -17.72000 4.49100   1.000 70.00996  ? 2   LYS B CG  1 
ATOM   1227 C CD  . LYS B 1 4   ? 17.13300 -16.39900 5.26200   1.000 72.07496  ? 2   LYS B CD  1 
ATOM   1228 C CE  . LYS B 1 4   ? 18.60200 -16.08500 5.61000   1.000 68.15394  ? 2   LYS B CE  1 
ATOM   1229 N NZ  . LYS B 1 4   ? 19.40300 -15.52300 4.48500   1.000 60.62810  ? 2   LYS B NZ  1 
ATOM   1230 N N   . ILE B 1 5   ? 14.50900 -18.41100 2.45600   1.000 68.04095  ? 3   ILE B N   1 
ATOM   1231 C CA  . ILE B 1 5   ? 14.32800 -17.87000 1.11300   1.000 65.52384  ? 3   ILE B CA  1 
ATOM   1232 C C   . ILE B 1 5   ? 14.49400 -16.36100 1.21000   1.000 71.25914  ? 3   ILE B C   1 
ATOM   1233 O O   . ILE B 1 5   ? 13.81200 -15.70800 2.01300   1.000 69.38309  ? 3   ILE B O   1 
ATOM   1234 C CB  . ILE B 1 5   ? 12.95900 -18.24200 0.52300   1.000 54.88800  ? 3   ILE B CB  1 
ATOM   1235 C CG1 . ILE B 1 5   ? 12.84000 -19.76600 0.40900   1.000 57.63797  ? 3   ILE B CG1 1 
ATOM   1236 C CG2 . ILE B 1 5   ? 12.77300 -17.57100 -0.80300  1.000 56.17952  ? 3   ILE B CG2 1 
ATOM   1237 C CD1 . ILE B 1 5   ? 11.44500 -20.27200 0.10000   1.000 53.17852  ? 3   ILE B CD1 1 
ATOM   1238 N N   . ARG B 1 6   ? 15.42200 -15.81400 0.42800   1.000 61.82010  ? 4   ARG B N   1 
ATOM   1239 C CA  . ARG B 1 6   ? 15.86100 -14.44000 0.59500   1.000 59.98991  ? 4   ARG B CA  1 
ATOM   1240 C C   . ARG B 1 6   ? 16.02600 -13.77000 -0.76100  1.000 58.66095  ? 4   ARG B C   1 
ATOM   1241 O O   . ARG B 1 6   ? 16.14100 -14.43400 -1.79700  1.000 60.09264  ? 4   ARG B O   1 
ATOM   1242 C CB  . ARG B 1 6   ? 17.18700 -14.36400 1.38300   1.000 59.57512  ? 4   ARG B CB  1 
ATOM   1243 C CG  . ARG B 1 6   ? 18.37100 -15.11300 0.73700   1.000 63.45441  ? 4   ARG B CG  1 
ATOM   1244 C CD  . ARG B 1 6   ? 19.72900 -14.58800 1.22400   1.000 57.80486  ? 4   ARG B CD  1 
ATOM   1245 N NE  . ARG B 1 6   ? 20.85000 -15.33600 0.65600   1.000 57.19573  ? 4   ARG B NE  1 
ATOM   1246 C CZ  . ARG B 1 6   ? 21.44400 -15.04600 -0.49700  1.000 63.21154  ? 4   ARG B CZ  1 
ATOM   1247 N NH1 . ARG B 1 6   ? 21.07200 -14.00600 -1.22800  1.000 54.68732  ? 4   ARG B NH1 1 
ATOM   1248 N NH2 . ARG B 1 6   ? 22.42900 -15.82600 -0.93300  1.000 57.57504  ? 4   ARG B NH2 1 
ATOM   1249 N N   . ASN B 1 7   ? 16.01100 -12.43600 -0.73900  1.000 66.55335  ? 5   ASN B N   1 
ATOM   1250 C CA  . ASN B 1 7   ? 16.29900 -11.65100 -1.93400  1.000 53.79759  ? 5   ASN B CA  1 
ATOM   1251 C C   . ASN B 1 7   ? 17.64800 -12.05700 -2.50900  1.000 58.91930  ? 5   ASN B C   1 
ATOM   1252 O O   . ASN B 1 7   ? 18.64000 -12.17600 -1.78900  1.000 59.78479  ? 5   ASN B O   1 
ATOM   1253 C CB  . ASN B 1 7   ? 16.27900 -10.14100 -1.62000  1.000 70.72042  ? 5   ASN B CB  1 
ATOM   1254 C CG  . ASN B 1 7   ? 17.33300 -9.70000  -0.55000  1.000 81.41662  ? 5   ASN B CG  1 
ATOM   1255 O OD1 . ASN B 1 7   ? 17.37900 -10.21000 0.58100   1.000 79.50044  ? 5   ASN B OD1 1 
ATOM   1256 N ND2 . ASN B 1 7   ? 18.15300 -8.71300  -0.91500  1.000 80.75726  ? 5   ASN B ND2 1 
ATOM   1257 N N   . TRP B 1 8   ? 17.66500 -12.32600 -3.80600  1.000 53.22299  ? 6   TRP B N   1 
ATOM   1258 C CA  . TRP B 1 8   ? 18.91000 -12.49800 -4.53800  1.000 62.44261  ? 6   TRP B CA  1 
ATOM   1259 C C   . TRP B 1 8   ? 19.78200 -11.24300 -4.47000  1.000 60.52376  ? 6   TRP B C   1 
ATOM   1260 O O   . TRP B 1 8   ? 19.28900 -10.11000 -4.44100  1.000 59.67647  ? 6   TRP B O   1 
ATOM   1261 C CB  . TRP B 1 8   ? 18.60300 -12.80200 -5.99600  1.000 65.55345  ? 6   TRP B CB  1 
ATOM   1262 C CG  . TRP B 1 8   ? 17.81800 -11.68900 -6.60700  1.000 63.93873  ? 6   TRP B CG  1 
ATOM   1263 C CD1 . TRP B 1 8   ? 16.87200 -10.90700 -5.99000  1.000 74.05134  ? 6   TRP B CD1 1 
ATOM   1264 C CD2 . TRP B 1 8   ? 17.93800 -11.19500 -7.92500  1.000 66.29562  ? 6   TRP B CD2 1 
ATOM   1265 N NE1 . TRP B 1 8   ? 16.38400 -9.97700  -6.85600  1.000 75.57371  ? 6   TRP B NE1 1 
ATOM   1266 C CE2 . TRP B 1 8   ? 17.02300 -10.13000 -8.05700  1.000 69.85513  ? 6   TRP B CE2 1 
ATOM   1267 C CE3 . TRP B 1 8   ? 18.71600 -11.55700 -9.01900  1.000 73.88079  ? 6   TRP B CE3 1 
ATOM   1268 C CZ2 . TRP B 1 8   ? 16.87600 -9.42500  -9.23100  1.000 74.61691  ? 6   TRP B CZ2 1 
ATOM   1269 C CZ3 . TRP B 1 8   ? 18.56600 -10.86200 -10.18100 1.000 83.21388  ? 6   TRP B CZ3 1 
ATOM   1270 C CH2 . TRP B 1 8   ? 17.65100 -9.80900  -10.28200 1.000 84.17884  ? 6   TRP B CH2 1 
ATOM   1271 N N   . ILE B 1 9   ? 21.09800 -11.45900 -4.50800  1.000 52.97695  ? 7   ILE B N   1 
ATOM   1272 C CA  . ILE B 1 9   ? 22.09700 -10.40100 -4.49200  1.000 55.15288  ? 7   ILE B CA  1 
ATOM   1273 C C   . ILE B 1 9   ? 23.10300 -10.68300 -5.60100  1.000 63.02107  ? 7   ILE B C   1 
ATOM   1274 O O   . ILE B 1 9   ? 23.21900 -11.81200 -6.08000  1.000 67.41030  ? 7   ILE B O   1 
ATOM   1275 C CB  . ILE B 1 9   ? 22.76400 -10.30400 -3.09800  1.000 55.77706  ? 7   ILE B CB  1 
ATOM   1276 C CG1 . ILE B 1 9   ? 21.75700 -9.68400  -2.14600  1.000 63.21038  ? 7   ILE B CG1 1 
ATOM   1277 C CG2 . ILE B 1 9   ? 24.01500 -9.43200  -3.10000  1.000 75.38690  ? 7   ILE B CG2 1 
ATOM   1278 C CD1 . ILE B 1 9   ? 21.13700 -8.42500  -2.73800  1.000 64.90497  ? 7   ILE B CD1 1 
ATOM   1279 N N   . LYS B 1 10  ? 23.79500 -9.62100  -6.04900  1.000 63.40289  ? 8   LYS B N   1 
ATOM   1280 C CA  . LYS B 1 10  ? 24.77800 -9.74200  -7.12400  1.000 64.52473  ? 8   LYS B CA  1 
ATOM   1281 C C   . LYS B 1 10  ? 25.75600 -10.88400 -6.88100  1.000 66.98815  ? 8   LYS B C   1 
ATOM   1282 O O   . LYS B 1 10  ? 26.18200 -11.54800 -7.83200  1.000 63.28270  ? 8   LYS B O   1 
ATOM   1283 C CB  . LYS B 1 10  ? 25.54500 -8.42100  -7.29600  1.000 60.77339  ? 8   LYS B CB  1 
ATOM   1284 C CG  . LYS B 1 10  ? 26.46200 -8.37000  -8.53000  1.000 66.95915  ? 8   LYS B CG  1 
ATOM   1285 C CD  . LYS B 1 10  ? 27.14300 -6.99600  -8.72100  1.000 68.41335  ? 8   LYS B CD  1 
ATOM   1286 C CE  . LYS B 1 10  ? 26.51200 -6.17200  -9.87100  1.000 81.16070  ? 8   LYS B CE  1 
ATOM   1287 N NZ  . LYS B 1 10  ? 27.25800 -4.90600  -10.23100 1.000 74.28113  ? 8   LYS B NZ  1 
ATOM   1288 N N   . ASP B 1 11  ? 26.11100 -11.14000 -5.61900  1.000 65.95263  ? 9   ASP B N   1 
ATOM   1289 C CA  . ASP B 1 11  ? 27.01300 -12.24200 -5.30700  1.000 61.64844  ? 9   ASP B CA  1 
ATOM   1290 C C   . ASP B 1 11  ? 26.42600 -13.60300 -5.66100  1.000 61.91712  ? 9   ASP B C   1 
ATOM   1291 O O   . ASP B 1 11  ? 27.18800 -14.56000 -5.83500  1.000 66.23891  ? 9   ASP B O   1 
ATOM   1292 C CB  . ASP B 1 11  ? 27.39300 -12.19600 -3.82500  1.000 60.74520  ? 9   ASP B CB  1 
ATOM   1293 C CG  . ASP B 1 11  ? 28.37400 -11.07400 -3.51800  1.000 63.56598  ? 9   ASP B CG  1 
ATOM   1294 O OD1 . ASP B 1 11  ? 29.04000 -10.61700 -4.47200  1.000 71.02767  ? 9   ASP B OD1 1 
ATOM   1295 O OD2 . ASP B 1 11  ? 28.49500 -10.65200 -2.34500  1.000 63.83799  ? 9   ASP B OD2 1 
ATOM   1296 N N   . ASP B 1 12  ? 25.09600 -13.71000 -5.78600  1.000 55.71129  ? 10  ASP B N   1 
ATOM   1297 C CA  . ASP B 1 12  ? 24.45600 -14.98600 -6.10100  1.000 54.47025  ? 10  ASP B CA  1 
ATOM   1298 C C   . ASP B 1 12  ? 24.58200 -15.34500 -7.57600  1.000 59.78704  ? 10  ASP B C   1 
ATOM   1299 O O   . ASP B 1 12  ? 24.53200 -16.53000 -7.92800  1.000 54.52669  ? 10  ASP B O   1 
ATOM   1300 C CB  . ASP B 1 12  ? 22.96100 -14.95800 -5.74800  1.000 58.01090  ? 10  ASP B CB  1 
ATOM   1301 C CG  . ASP B 1 12  ? 22.69700 -14.88100 -4.25600  1.000 59.35819  ? 10  ASP B CG  1 
ATOM   1302 O OD1 . ASP B 1 12  ? 23.47500 -15.45600 -3.47300  1.000 55.95878  ? 10  ASP B OD1 1 
ATOM   1303 O OD2 . ASP B 1 12  ? 21.68800 -14.25700 -3.87100  1.000 54.32888  ? 10  ASP B OD2 1 
ATOM   1304 N N   . VAL B 1 13  ? 24.72100 -14.34600 -8.44200  1.000 54.43517  ? 11  VAL B N   1 
ATOM   1305 C CA  . VAL B 1 13  ? 24.58700 -14.54000 -9.88500  1.000 52.86312  ? 11  VAL B CA  1 
ATOM   1306 C C   . VAL B 1 13  ? 25.48300 -15.66600 -10.39700 1.000 58.41956  ? 11  VAL B C   1 
ATOM   1307 O O   . VAL B 1 13  ? 25.05600 -16.41200 -11.29700 1.000 59.89851  ? 11  VAL B O   1 
ATOM   1308 C CB  . VAL B 1 13  ? 24.84400 -13.22900 -10.64000 1.000 50.57809  ? 11  VAL B CB  1 
ATOM   1309 C CG1 . VAL B 1 13  ? 24.87300 -13.48200 -12.13900 1.000 55.22307  ? 11  VAL B CG1 1 
ATOM   1310 C CG2 . VAL B 1 13  ? 23.72900 -12.26100 -10.34800 1.000 52.29025  ? 11  VAL B CG2 1 
ATOM   1311 N N   . PRO B 1 14  ? 26.70200 -15.86300 -9.87700  1.000 57.06372  ? 12  PRO B N   1 
ATOM   1312 C CA  . PRO B 1 14  ? 27.43800 -17.06900 -10.28700 1.000 58.29876  ? 12  PRO B CA  1 
ATOM   1313 C C   . PRO B 1 14  ? 26.68200 -18.36100 -10.00200 1.000 57.88130  ? 12  PRO B C   1 
ATOM   1314 O O   . PRO B 1 14  ? 26.45100 -19.15000 -10.92500 1.000 54.20743  ? 12  PRO B O   1 
ATOM   1315 C CB  . PRO B 1 14  ? 28.74400 -16.94400 -9.50400  1.000 58.56622  ? 12  PRO B CB  1 
ATOM   1316 C CG  . PRO B 1 14  ? 28.97200 -15.48500 -9.48500  1.000 58.59595  ? 12  PRO B CG  1 
ATOM   1317 C CD  . PRO B 1 14  ? 27.60700 -14.92200 -9.18400  1.000 56.47257  ? 12  PRO B CD  1 
ATOM   1318 N N   . GLN B 1 15  ? 26.24000 -18.58500 -8.76400  1.000 56.98752  ? 13  GLN B N   1 
ATOM   1319 C CA  . GLN B 1 15  ? 25.61000 -19.86400 -8.45200  1.000 55.36651  ? 13  GLN B CA  1 
ATOM   1320 C C   . GLN B 1 15  ? 24.20500 -19.99800 -9.03000  1.000 52.98235  ? 13  GLN B C   1 
ATOM   1321 O O   . GLN B 1 15  ? 23.75600 -21.12300 -9.30500  1.000 52.16616  ? 13  GLN B O   1 
ATOM   1322 C CB  . GLN B 1 15  ? 25.59500 -20.07000 -6.94300  1.000 56.93119  ? 13  GLN B CB  1 
ATOM   1323 C CG  . GLN B 1 15  ? 26.98100 -20.40500 -6.42800  1.000 59.79179  ? 13  GLN B CG  1 
ATOM   1324 C CD  . GLN B 1 15  ? 27.06900 -20.31500 -4.93900  1.000 61.64183  ? 13  GLN B CD  1 
ATOM   1325 O OE1 . GLN B 1 15  ? 26.20200 -19.73000 -4.29300  1.000 66.52887  ? 13  GLN B OE1 1 
ATOM   1326 N NE2 . GLN B 1 15  ? 28.09900 -20.91900 -4.37100  1.000 67.09327  ? 13  GLN B NE2 1 
ATOM   1327 N N   . VAL B 1 16  ? 23.49900 -18.88600 -9.23300  1.000 51.27174  ? 14  VAL B N   1 
ATOM   1328 C CA  . VAL B 1 16  ? 22.21600 -18.96400 -9.93100  1.000 48.69705  ? 14  VAL B CA  1 
ATOM   1329 C C   . VAL B 1 16  ? 22.43000 -19.41000 -11.37300 1.000 47.89878  ? 14  VAL B C   1 
ATOM   1330 O O   . VAL B 1 16  ? 21.68000 -20.24600 -11.90600 1.000 46.65561  ? 14  VAL B O   1 
ATOM   1331 C CB  . VAL B 1 16  ? 21.48500 -17.61100 -9.85400  1.000 47.36779  ? 14  VAL B CB  1 
ATOM   1332 C CG1 . VAL B 1 16  ? 20.42700 -17.51700 -10.91100 1.000 45.08238  ? 14  VAL B CG1 1 
ATOM   1333 C CG2 . VAL B 1 16  ? 20.85800 -17.43300 -8.47300  1.000 49.43059  ? 14  VAL B CG2 1 
ATOM   1334 N N   . SER B 1 17  ? 23.45200 -18.85400 -12.02600 1.000 48.68435  ? 15  SER B N   1 
ATOM   1335 C CA  . SER B 1 17  ? 23.77600 -19.23500 -13.39700 1.000 48.21088  ? 15  SER B CA  1 
ATOM   1336 C C   . SER B 1 17  ? 24.15300 -20.70400 -13.49900 1.000 49.07899  ? 15  SER B C   1 
ATOM   1337 O O   . SER B 1 17  ? 23.88900 -21.33800 -14.52100 1.000 48.19036  ? 15  SER B O   1 
ATOM   1338 C CB  . SER B 1 17  ? 24.92700 -18.36800 -13.91900 1.000 54.54673  ? 15  SER B CB  1 
ATOM   1339 O OG  . SER B 1 17  ? 25.35000 -18.80200 -15.19900 1.000 59.61168  ? 15  SER B OG  1 
ATOM   1340 N N   . GLU B 1 18  ? 24.79400 -21.25500 -12.46300 1.000 50.99805  ? 16  GLU B N   1 
ATOM   1341 C CA  . GLU B 1 18  ? 25.15500 -22.67000 -12.47300 1.000 51.98039  ? 16  GLU B CA  1 
ATOM   1342 C C   . GLU B 1 18  ? 23.91700 -23.56200 -12.42700 1.000 50.46449  ? 16  GLU B C   1 
ATOM   1343 O O   . GLU B 1 18  ? 23.82100 -24.54200 -13.17700 1.000 52.05628  ? 16  GLU B O   1 
ATOM   1344 C CB  . GLU B 1 18  ? 26.08200 -22.98300 -11.29700 1.000 54.51785  ? 16  GLU B CB  1 
ATOM   1345 C CG  . GLU B 1 18  ? 27.29000 -22.09700 -11.22700 1.000 56.19407  ? 16  GLU B CG  1 
ATOM   1346 C CD  . GLU B 1 18  ? 28.24100 -22.55400 -10.15900 1.000 65.76980  ? 16  GLU B CD  1 
ATOM   1347 O OE1 . GLU B 1 18  ? 27.81400 -23.38600 -9.33200  1.000 61.18279  ? 16  GLU B OE1 1 
ATOM   1348 O OE2 . GLU B 1 18  ? 29.40300 -22.09400 -10.15100 1.000 68.06493  ? 16  GLU B OE2 1 
ATOM   1349 N N   . ILE B 1 19  ? 22.96400 -23.25600 -11.54500 1.000 49.72172  ? 17  ILE B N   1 
ATOM   1350 C CA  . ILE B 1 19  ? 21.73700 -24.04700 -11.49900 1.000 48.30941  ? 17  ILE B CA  1 
ATOM   1351 C C   . ILE B 1 19  ? 20.97500 -23.90900 -12.81300 1.000 48.58094  ? 17  ILE B C   1 
ATOM   1352 O O   . ILE B 1 19  ? 20.36300 -24.86800 -13.30600 1.000 49.36394  ? 17  ILE B O   1 
ATOM   1353 C CB  . ILE B 1 19  ? 20.85300 -23.62600 -10.31500 1.000 48.00325  ? 17  ILE B CB  1 
ATOM   1354 C CG1 . ILE B 1 19  ? 21.56100 -23.79700 -8.96000  1.000 50.32687  ? 17  ILE B CG1 1 
ATOM   1355 C CG2 . ILE B 1 19  ? 19.50200 -24.37700 -10.38200 1.000 46.42721  ? 17  ILE B CG2 1 
ATOM   1356 C CD1 . ILE B 1 19  ? 20.84300 -23.02000 -7.88300  1.000 50.11608  ? 17  ILE B CD1 1 
ATOM   1357 N N   . ALA B 1 20  ? 20.98300 -22.70400 -13.38600 1.000 48.05162  ? 18  ALA B N   1 
ATOM   1358 C CA  . ALA B 1 20  ? 20.32800 -22.48200 -14.66700 1.000 50.36297  ? 18  ALA B CA  1 
ATOM   1359 C C   . ALA B 1 20  ? 20.96500 -23.33500 -15.75200 1.000 43.74704  ? 18  ALA B C   1 
ATOM   1360 O O   . ALA B 1 20  ? 20.26000 -23.99700 -16.52400 1.000 42.50271  ? 18  ALA B O   1 
ATOM   1361 C CB  . ALA B 1 20  ? 20.38400 -21.00300 -15.03800 1.000 44.60636  ? 18  ALA B CB  1 
ATOM   1362 N N   . GLU B 1 21  ? 22.29700 -23.34500 -15.82300 1.000 45.52404  ? 19  GLU B N   1 
ATOM   1363 C CA  . GLU B 1 21  ? 22.95000 -24.13800 -16.86200 1.000 45.99775  ? 19  GLU B CA  1 
ATOM   1364 C C   . GLU B 1 21  ? 22.62000 -25.62100 -16.70500 1.000 49.80256  ? 19  GLU B C   1 
ATOM   1365 O O   . GLU B 1 21  ? 22.53500 -26.35000 -17.69900 1.000 45.57112  ? 19  GLU B O   1 
ATOM   1366 C CB  . GLU B 1 21  ? 24.47100 -23.91000 -16.86300 1.000 48.40890  ? 19  GLU B CB  1 
ATOM   1367 C CG  . GLU B 1 21  ? 25.19400 -24.47000 -18.14300 1.000 48.58750  ? 19  GLU B CG  1 
ATOM   1368 C CD  . GLU B 1 21  ? 26.70800 -24.21900 -18.14000 1.000 50.84030  ? 19  GLU B CD  1 
ATOM   1369 O OE1 . GLU B 1 21  ? 27.17600 -23.51600 -17.23100 1.000 59.96774  ? 19  GLU B OE1 1 
ATOM   1370 O OE2 . GLU B 1 21  ? 27.43600 -24.71700 -19.04000 1.000 54.58739  ? 19  GLU B OE2 1 
ATOM   1371 N N   . ALA B 1 22  ? 22.37800 -26.06600 -15.47200 1.000 52.64758  ? 20  ALA B N   1 
ATOM   1372 C CA  . ALA B 1 22  ? 22.19200 -27.47500 -15.15200 1.000 50.52662  ? 20  ALA B CA  1 
ATOM   1373 C C   . ALA B 1 22  ? 20.75500 -27.93800 -15.34500 1.000 46.12232  ? 20  ALA B C   1 
ATOM   1374 O O   . ALA B 1 22  ? 20.51200 -29.07200 -15.78200 1.000 51.49899  ? 20  ALA B O   1 
ATOM   1375 C CB  . ALA B 1 22  ? 22.63000 -27.73100 -13.70500 1.000 58.36969  ? 20  ALA B CB  1 
ATOM   1376 N N   . ALA B 1 23  ? 19.79500 -27.07500 -15.04800 1.000 44.62630  ? 21  ALA B N   1 
ATOM   1377 C CA  . ALA B 1 23  ? 18.40100 -27.47100 -14.95300 1.000 44.61093  ? 21  ALA B CA  1 
ATOM   1378 C C   . ALA B 1 23  ? 17.49700 -26.91200 -16.04800 1.000 40.36917  ? 21  ALA B C   1 
ATOM   1379 O O   . ALA B 1 23  ? 16.52400 -27.56800 -16.43200 1.000 44.76882  ? 21  ALA B O   1 
ATOM   1380 C CB  . ALA B 1 23  ? 17.85100 -27.03000 -13.59600 1.000 42.58801  ? 21  ALA B CB  1 
ATOM   1381 N N   . MET B 1 24  ? 17.80000 -25.76200 -16.56700 1.000 34.86868  ? 22  MET B N   1 
ATOM   1382 C CA  . MET B 1 24  ? 16.88200 -24.98000 -17.39200 1.000 36.53313  ? 22  MET B CA  1 
ATOM   1383 C C   . MET B 1 24  ? 17.12200 -25.20400 -18.88500 1.000 39.86627  ? 22  MET B C   1 
ATOM   1384 O O   . MET B 1 24  ? 18.25000 -25.03300 -19.36700 1.000 36.12972  ? 22  MET B O   1 
ATOM   1385 C CB  . MET B 1 24  ? 17.05900 -23.50100 -17.04300 1.000 37.01511  ? 22  MET B CB  1 
ATOM   1386 C CG  . MET B 1 24  ? 16.54100 -22.51500 -18.03300 1.000 37.76893  ? 22  MET B CG  1 
ATOM   1387 S SD  . MET B 1 24  ? 16.93700 -20.81300 -17.54300 1.000 38.12121  ? 22  MET B SD  1 
ATOM   1388 C CE  . MET B 1 24  ? 15.66400 -20.01300 -18.52700 1.000 42.79570  ? 22  MET B CE  1 
ATOM   1389 N N   . PRO B 1 25  ? 16.11400 -25.57000 -19.66900 1.000 39.07692  ? 23  PRO B N   1 
ATOM   1390 C CA  . PRO B 1 25  ? 16.30700 -25.57700 -21.12500 1.000 36.53761  ? 23  PRO B CA  1 
ATOM   1391 C C   . PRO B 1 25  ? 16.69800 -24.18000 -21.59900 1.000 31.30652  ? 23  PRO B C   1 
ATOM   1392 O O   . PRO B 1 25  ? 16.17600 -23.17400 -21.11400 1.000 29.60504  ? 23  PRO B O   1 
ATOM   1393 C CB  . PRO B 1 25  ? 14.92800 -25.99400 -21.66500 1.000 32.44460  ? 23  PRO B CB  1 
ATOM   1394 C CG  . PRO B 1 25  ? 13.97200 -25.74200 -20.56900 1.000 35.57045  ? 23  PRO B CG  1 
ATOM   1395 C CD  . PRO B 1 25  ? 14.73900 -25.93200 -19.29100 1.000 39.02638  ? 23  PRO B CD  1 
ATOM   1396 N N   . PHE B 1 26  ? 17.59800 -24.12800 -22.57500 1.000 37.31258  ? 24  PHE B N   1 
ATOM   1397 C CA  . PHE B 1 26  ? 18.01700 -22.87600 -23.19200 1.000 29.82592  ? 24  PHE B CA  1 
ATOM   1398 C C   . PHE B 1 26  ? 18.37900 -21.85300 -22.11600 1.000 31.73144  ? 24  PHE B C   1 
ATOM   1399 O O   . PHE B 1 26  ? 17.72200 -20.81800 -21.98600 1.000 31.65133  ? 24  PHE B O   1 
ATOM   1400 C CB  . PHE B 1 26  ? 16.93000 -22.33800 -24.11100 1.000 32.75994  ? 24  PHE B CB  1 
ATOM   1401 C CG  . PHE B 1 26  ? 16.57600 -23.27400 -25.18000 1.000 36.48318  ? 24  PHE B CG  1 
ATOM   1402 C CD1 . PHE B 1 26  ? 15.64600 -24.27800 -24.95600 1.000 45.29891  ? 24  PHE B CD1 1 
ATOM   1403 C CD2 . PHE B 1 26  ? 17.19200 -23.18300 -26.42000 1.000 47.78054  ? 24  PHE B CD2 1 
ATOM   1404 C CE1 . PHE B 1 26  ? 15.33600 -25.17500 -25.94800 1.000 50.39637  ? 24  PHE B CE1 1 
ATOM   1405 C CE2 . PHE B 1 26  ? 16.88000 -24.06800 -27.41800 1.000 46.98427  ? 24  PHE B CE2 1 
ATOM   1406 C CZ  . PHE B 1 26  ? 15.95800 -25.06700 -27.18300 1.000 40.64952  ? 24  PHE B CZ  1 
ATOM   1407 N N   . PRO B 1 27  ? 19.37000 -22.15400 -21.30300 1.000 30.78895  ? 25  PRO B N   1 
ATOM   1408 C CA  . PRO B 1 27  ? 19.62000 -21.34500 -20.10900 1.000 35.96696  ? 25  PRO B CA  1 
ATOM   1409 C C   . PRO B 1 27  ? 19.97200 -19.90900 -20.45500 1.000 37.86026  ? 25  PRO B C   1 
ATOM   1410 O O   . PRO B 1 27  ? 20.65900 -19.63300 -21.44400 1.000 39.24732  ? 25  PRO B O   1 
ATOM   1411 C CB  . PRO B 1 27  ? 20.79000 -22.07300 -19.44900 1.000 40.21879  ? 25  PRO B CB  1 
ATOM   1412 C CG  . PRO B 1 27  ? 21.51700 -22.72800 -20.60300 1.000 35.15820  ? 25  PRO B CG  1 
ATOM   1413 C CD  . PRO B 1 27  ? 20.42900 -23.14500 -21.55300 1.000 36.79951  ? 25  PRO B CD  1 
ATOM   1414 N N   . TRP B 1 28  ? 19.46200 -18.99700 -19.64200 1.000 34.31526  ? 26  TRP B N   1 
ATOM   1415 C CA  . TRP B 1 28  ? 19.92600 -17.61700 -19.61700 1.000 36.19473  ? 26  TRP B CA  1 
ATOM   1416 C C   . TRP B 1 28  ? 21.43100 -17.54700 -19.34200 1.000 42.30831  ? 26  TRP B C   1 
ATOM   1417 O O   . TRP B 1 28  ? 21.97200 -18.32400 -18.54800 1.000 49.38918  ? 26  TRP B O   1 
ATOM   1418 C CB  . TRP B 1 28  ? 19.20000 -16.85000 -18.51100 1.000 39.94475  ? 26  TRP B CB  1 
ATOM   1419 C CG  . TRP B 1 28  ? 17.74800 -16.63900 -18.69500 1.000 36.48016  ? 26  TRP B CG  1 
ATOM   1420 C CD1 . TRP B 1 28  ? 16.98200 -17.01400 -19.76000 1.000 40.46848  ? 26  TRP B CD1 1 
ATOM   1421 C CD2 . TRP B 1 28  ? 16.87800 -15.93800 -17.79800 1.000 34.24492  ? 26  TRP B CD2 1 
ATOM   1422 N NE1 . TRP B 1 28  ? 15.68200 -16.60300 -19.56800 1.000 40.19290  ? 26  TRP B NE1 1 
ATOM   1423 C CE2 . TRP B 1 28  ? 15.60100 -15.93000 -18.37400 1.000 32.77790  ? 26  TRP B CE2 1 
ATOM   1424 C CE3 . TRP B 1 28  ? 17.06700 -15.30300 -16.56400 1.000 35.29547  ? 26  TRP B CE3 1 
ATOM   1425 C CZ2 . TRP B 1 28  ? 14.50400 -15.35200 -17.74500 1.000 40.99696  ? 26  TRP B CZ2 1 
ATOM   1426 C CZ3 . TRP B 1 28  ? 15.98900 -14.70600 -15.95400 1.000 36.04641  ? 26  TRP B CZ3 1 
ATOM   1427 C CH2 . TRP B 1 28  ? 14.71900 -14.74200 -16.53400 1.000 38.67719  ? 26  TRP B CH2 1 
ATOM   1428 N N   . SER B 1 29  ? 22.09700 -16.56000 -19.96600 1.000 44.09376  ? 27  SER B N   1 
ATOM   1429 C CA  . SER B 1 29  ? 23.51900 -16.26800 -19.75800 1.000 41.89607  ? 27  SER B CA  1 
ATOM   1430 C C   . SER B 1 29  ? 23.78600 -15.77500 -18.34300 1.000 52.05558  ? 27  SER B C   1 
ATOM   1431 O O   . SER B 1 29  ? 22.89500 -15.28500 -17.64500 1.000 45.13707  ? 27  SER B O   1 
ATOM   1432 C CB  . SER B 1 29  ? 24.02700 -15.18600 -20.71800 1.000 45.90754  ? 27  SER B CB  1 
ATOM   1433 N N   . GLU B 1 30  ? 25.05000 -15.88500 -17.93400 1.000 44.49310  ? 28  GLU B N   1 
ATOM   1434 C CA  . GLU B 1 30  ? 25.45600 -15.23400 -16.69600 1.000 50.89966  ? 28  GLU B CA  1 
ATOM   1435 C C   . GLU B 1 30  ? 25.33400 -13.72300 -16.82600 1.000 54.41904  ? 28  GLU B C   1 
ATOM   1436 O O   . GLU B 1 30  ? 24.93700 -13.04600 -15.87400 1.000 57.82713  ? 28  GLU B O   1 
ATOM   1437 C CB  . GLU B 1 30  ? 26.87900 -15.64100 -16.32000 1.000 54.39426  ? 28  GLU B CB  1 
ATOM   1438 C CG  . GLU B 1 30  ? 27.12600 -15.61300 -14.83000 1.000 60.98126  ? 28  GLU B CG  1 
ATOM   1439 C CD  . GLU B 1 30  ? 28.49600 -16.12700 -14.45200 1.000 72.47927  ? 28  GLU B CD  1 
ATOM   1440 O OE1 . GLU B 1 30  ? 29.49300 -15.55900 -14.92900 1.000 68.13131  ? 28  GLU B OE1 1 
ATOM   1441 O OE2 . GLU B 1 30  ? 28.57700 -17.10400 -13.67800 1.000 68.97029  ? 28  GLU B OE2 1 
ATOM   1442 N N   . LYS B 1 31  ? 25.64200 -13.17700 -18.00900 1.000 57.57805  ? 29  LYS B N   1 
ATOM   1443 C CA  . LYS B 1 31  ? 25.47900 -11.73800 -18.21400 1.000 61.13957  ? 29  LYS B CA  1 
ATOM   1444 C C   . LYS B 1 31  ? 24.01900 -11.32800 -18.03200 1.000 62.38726  ? 29  LYS B C   1 
ATOM   1445 O O   . LYS B 1 31  ? 23.72700 -10.35300 -17.32800 1.000 69.72217  ? 29  LYS B O   1 
ATOM   1446 C CB  . LYS B 1 31  ? 25.99200 -11.32700 -19.60300 1.000 60.77790  ? 29  LYS B CB  1 
ATOM   1447 C CG  . LYS B 1 31  ? 26.68100 -9.95400  -19.69600 1.000 67.25383  ? 29  LYS B CG  1 
ATOM   1448 C CD  . LYS B 1 31  ? 25.75900 -8.77400  -19.35300 1.000 73.40937  ? 29  LYS B CD  1 
ATOM   1449 C CE  . LYS B 1 31  ? 26.31000 -7.44300  -19.88200 1.000 81.15640  ? 29  LYS B CE  1 
ATOM   1450 N NZ  . LYS B 1 31  ? 25.55600 -6.23400  -19.41400 1.000 79.26515  ? 29  LYS B NZ  1 
ATOM   1451 N N   . PHE B 1 32  ? 23.08700 -12.07200 -18.63800 1.000 55.04397  ? 30  PHE B N   1 
ATOM   1452 C CA  . PHE B 1 32  ? 21.67700 -11.70700 -18.52400 1.000 59.50936  ? 30  PHE B CA  1 
ATOM   1453 C C   . PHE B 1 32  ? 21.20500 -11.76500 -17.07500 1.000 63.55236  ? 30  PHE B C   1 
ATOM   1454 O O   . PHE B 1 32  ? 20.33400 -10.98200 -16.66800 1.000 61.79045  ? 30  PHE B O   1 
ATOM   1455 C CB  . PHE B 1 32  ? 20.79900 -12.61700 -19.38900 1.000 48.08081  ? 30  PHE B CB  1 
ATOM   1456 C CG  . PHE B 1 32  ? 19.35200 -12.19600 -19.42600 1.000 52.27874  ? 30  PHE B CG  1 
ATOM   1457 C CD1 . PHE B 1 32  ? 18.92500 -11.21000 -20.31100 1.000 58.49379  ? 30  PHE B CD1 1 
ATOM   1458 C CD2 . PHE B 1 32  ? 18.41800 -12.76400 -18.56500 1.000 45.95306  ? 30  PHE B CD2 1 
ATOM   1459 C CE1 . PHE B 1 32  ? 17.59200 -10.81900 -20.34600 1.000 55.00486  ? 30  PHE B CE1 1 
ATOM   1460 C CE2 . PHE B 1 32  ? 17.08400 -12.36800 -18.59000 1.000 43.95141  ? 30  PHE B CE2 1 
ATOM   1461 C CZ  . PHE B 1 32  ? 16.67600 -11.39800 -19.48100 1.000 49.84314  ? 30  PHE B CZ  1 
ATOM   1462 N N   . PHE B 1 33  ? 21.75000 -12.69400 -16.28800 1.000 57.87826  ? 31  PHE B N   1 
ATOM   1463 C CA  . PHE B 1 33  ? 21.35800 -12.76600 -14.88600 1.000 61.48058  ? 31  PHE B CA  1 
ATOM   1464 C C   . PHE B 1 33  ? 21.77800 -11.50500 -14.14600 1.000 52.73095  ? 31  PHE B C   1 
ATOM   1465 O O   . PHE B 1 33  ? 21.03500 -11.00200 -13.29600 1.000 62.07666  ? 31  PHE B O   1 
ATOM   1466 C CB  . PHE B 1 33  ? 21.95100 -14.01400 -14.24300 1.000 48.37502  ? 31  PHE B CB  1 
ATOM   1467 C CG  . PHE B 1 33  ? 21.05400 -15.19300 -14.31300 1.000 46.49112  ? 31  PHE B CG  1 
ATOM   1468 C CD1 . PHE B 1 33  ? 19.75600 -15.10500 -13.82500 1.000 39.89991  ? 31  PHE B CD1 1 
ATOM   1469 C CD2 . PHE B 1 33  ? 21.47600 -16.38100 -14.89400 1.000 41.40055  ? 31  PHE B CD2 1 
ATOM   1470 C CE1 . PHE B 1 33  ? 18.88500 -16.18100 -13.87000 1.000 43.74422  ? 31  PHE B CE1 1 
ATOM   1471 C CE2 . PHE B 1 33  ? 20.60200 -17.47400 -14.94100 1.000 47.52176  ? 31  PHE B CE2 1 
ATOM   1472 C CZ  . PHE B 1 33  ? 19.30500 -17.36500 -14.43300 1.000 50.25602  ? 31  PHE B CZ  1 
ATOM   1473 N N   . TYR B 1 34  ? 22.94900 -10.95700 -14.48600 1.000 57.91157  ? 32  TYR B N   1 
ATOM   1474 C CA  . TYR B 1 34  ? 23.35000 -9.67100  -13.92600 1.000 61.52396  ? 32  TYR B CA  1 
ATOM   1475 C C   . TYR B 1 34  ? 22.39900 -8.55900  -14.35800 1.000 71.71071  ? 32  TYR B C   1 
ATOM   1476 O O   . TYR B 1 34  ? 22.08400 -7.66200  -13.56300 1.000 79.10127  ? 32  TYR B O   1 
ATOM   1477 C CB  . TYR B 1 34  ? 24.78500 -9.34300  -14.33100 1.000 65.74390  ? 32  TYR B CB  1 
ATOM   1478 C CG  . TYR B 1 34  ? 25.85200 -10.10900 -13.56800 1.000 67.05233  ? 32  TYR B CG  1 
ATOM   1479 C CD1 . TYR B 1 34  ? 26.11700 -9.83700  -12.22400 1.000 73.40882  ? 32  TYR B CD1 1 
ATOM   1480 C CD2 . TYR B 1 34  ? 26.61700 -11.08200 -14.19900 1.000 61.54323  ? 32  TYR B CD2 1 
ATOM   1481 C CE1 . TYR B 1 34  ? 27.10000 -10.53400 -11.53400 1.000 66.73747  ? 32  TYR B CE1 1 
ATOM   1482 C CE2 . TYR B 1 34  ? 27.60500 -11.77300 -13.52500 1.000 61.17496  ? 32  TYR B CE2 1 
ATOM   1483 C CZ  . TYR B 1 34  ? 27.83600 -11.50300 -12.19400 1.000 70.20537  ? 32  TYR B CZ  1 
ATOM   1484 O OH  . TYR B 1 34  ? 28.81500 -12.20800 -11.53800 1.000 73.22888  ? 32  TYR B OH  1 
ATOM   1485 N N   . ASP B 1 35  ? 21.93600 -8.59800  -15.61100 1.000 66.69210  ? 33  ASP B N   1 
ATOM   1486 C CA  . ASP B 1 35  ? 20.97300 -7.60700  -16.08400 1.000 77.75497  ? 33  ASP B CA  1 
ATOM   1487 C C   . ASP B 1 35  ? 19.67500 -7.65500  -15.29400 1.000 78.87358  ? 33  ASP B C   1 
ATOM   1488 O O   . ASP B 1 35  ? 19.02500 -6.61900  -15.10900 1.000 80.34195  ? 33  ASP B O   1 
ATOM   1489 C CB  . ASP B 1 35  ? 20.66500 -7.81600  -17.57100 1.000 76.08035  ? 33  ASP B CB  1 
ATOM   1490 C CG  . ASP B 1 35  ? 21.84300 -7.51900  -18.45700 1.000 75.70356  ? 33  ASP B CG  1 
ATOM   1491 O OD1 . ASP B 1 35  ? 22.71200 -6.72900  -18.03400 1.000 90.27869  ? 33  ASP B OD1 1 
ATOM   1492 O OD2 . ASP B 1 35  ? 21.89900 -8.07200  -19.57600 1.000 77.62919  ? 33  ASP B OD2 1 
ATOM   1493 N N   . CYS B 1 36  ? 19.27100 -8.83500  -14.82500 1.000 62.76395  ? 34  CYS B N   1 
ATOM   1494 C CA  . CYS B 1 36  ? 17.97000 -8.92300  -14.17800 1.000 64.90447  ? 34  CYS B CA  1 
ATOM   1495 C C   . CYS B 1 36  ? 17.88500 -8.09600  -12.89000 1.000 75.35407  ? 34  CYS B C   1 
ATOM   1496 O O   . CYS B 1 36  ? 16.77600 -7.86800  -12.39400 1.000 79.13567  ? 34  CYS B O   1 
ATOM   1497 C CB  . CYS B 1 36  ? 17.63400 -10.40200 -13.95000 1.000 62.91784  ? 34  CYS B CB  1 
ATOM   1498 S SG  . CYS B 1 36  ? 17.29400 -11.27200 -15.52000 1.000 54.04462  ? 34  CYS B SG  1 
ATOM   1499 N N   . LEU B 1 37  ? 19.00500 -7.58000  -12.37800 1.000 81.46995  ? 35  LEU B N   1 
ATOM   1500 C CA  . LEU B 1 37  ? 19.01000 -6.75900  -11.16400 1.000 91.91377  ? 35  LEU B CA  1 
ATOM   1501 C C   . LEU B 1 37  ? 18.33600 -5.39200  -11.33900 1.000 96.65309  ? 35  LEU B C   1 
ATOM   1502 O O   . LEU B 1 37  ? 18.34400 -4.57200  -10.41000 1.000 96.35603  ? 35  LEU B O   1 
ATOM   1503 C CB  . LEU B 1 37  ? 20.44900 -6.56000  -10.66900 1.000 91.87372  ? 35  LEU B CB  1 
ATOM   1504 C CG  . LEU B 1 37  ? 21.15300 -7.64900  -9.84200  1.000 89.49507  ? 35  LEU B CG  1 
ATOM   1505 C CD1 . LEU B 1 37  ? 20.42600 -7.90500  -8.53100  1.000 89.09014  ? 35  LEU B CD1 1 
ATOM   1506 C CD2 . LEU B 1 37  ? 21.34200 -8.94900  -10.60800 1.000 77.30644  ? 35  LEU B CD2 1 
ATOM   1507 N N   . LYS B 1 38  ? 17.74000 -5.14300  -12.50800 1.000 94.97321  ? 36  LYS B N   1 
ATOM   1508 C CA  . LYS B 1 38  ? 17.13100 -3.85900  -12.82700 1.000 104.84644 ? 36  LYS B CA  1 
ATOM   1509 C C   . LYS B 1 38  ? 15.73400 -3.74500  -12.21500 1.000 108.31132 ? 36  LYS B C   1 
ATOM   1510 O O   . LYS B 1 38  ? 15.25400 -4.63900  -11.51200 1.000 103.07364 ? 36  LYS B O   1 
ATOM   1511 C CB  . LYS B 1 38  ? 17.06400 -3.66300  -14.33900 1.000 106.91858 ? 36  LYS B CB  1 
ATOM   1512 C CG  . LYS B 1 38  ? 18.41700 -3.59600  -15.02700 1.000 112.31660 ? 36  LYS B CG  1 
ATOM   1513 C CD  . LYS B 1 38  ? 18.26800 -3.77300  -16.53600 1.000 107.78965 ? 36  LYS B CD  1 
ATOM   1514 C CE  . LYS B 1 38  ? 17.75100 -2.50600  -17.20100 1.000 111.03214 ? 36  LYS B CE  1 
ATOM   1515 N NZ  . LYS B 1 38  ? 17.01900 -2.81500  -18.45600 1.000 111.90771 ? 36  LYS B NZ  1 
ATOM   1516 N N   . SER B 1 39  ? 15.06700 -2.62600  -12.50800 1.000 109.98232 ? 37  SER B N   1 
ATOM   1517 C CA  . SER B 1 39  ? 13.76700 -2.31200  -11.93500 1.000 103.98576 ? 37  SER B CA  1 
ATOM   1518 C C   . SER B 1 39  ? 12.71000 -3.32100  -12.38900 1.000 101.31885 ? 37  SER B C   1 
ATOM   1519 O O   . SER B 1 39  ? 12.88000 -4.04000  -13.37800 1.000 100.40888 ? 37  SER B O   1 
ATOM   1520 C CB  . SER B 1 39  ? 13.35200 -0.88800  -12.32100 1.000 107.40311 ? 37  SER B CB  1 
ATOM   1521 O OG  . SER B 1 39  ? 12.33800 -0.38700  -11.46800 1.000 106.84131 ? 37  SER B OG  1 
ATOM   1522 N N   . ASN B 1 40  ? 11.62100 -3.38800  -11.61600 1.000 97.29087  ? 38  ASN B N   1 
ATOM   1523 C CA  . ASN B 1 40  ? 10.46700 -4.25600  -11.85900 1.000 99.82692  ? 38  ASN B CA  1 
ATOM   1524 C C   . ASN B 1 40  ? 10.75600 -5.75700  -11.73900 1.000 94.26810  ? 38  ASN B C   1 
ATOM   1525 O O   . ASN B 1 40  ? 9.81500  -6.55900  -11.67500 1.000 84.12980  ? 38  ASN B O   1 
ATOM   1526 C CB  . ASN B 1 40  ? 9.84800  -3.95200  -13.23200 1.000 97.53157  ? 38  ASN B CB  1 
ATOM   1527 C CG  . ASN B 1 40  ? 8.75200  -2.89400  -13.15800 1.000 91.57295  ? 38  ASN B CG  1 
ATOM   1528 O OD1 . ASN B 1 40  ? 8.87500  -1.91200  -12.42500 1.000 98.34623  ? 38  ASN B OD1 1 
ATOM   1529 N ND2 . ASN B 1 40  ? 7.66600  -3.10300  -13.90300 1.000 81.97636  ? 38  ASN B ND2 1 
ATOM   1530 N N   . TYR B 1 41  ? 12.02800 -6.15600  -11.68500 1.000 92.98630  ? 39  TYR B N   1 
ATOM   1531 C CA  . TYR B 1 41  ? 12.40600 -7.56400  -11.58800 1.000 88.41558  ? 39  TYR B CA  1 
ATOM   1532 C C   . TYR B 1 41  ? 12.72900 -7.93500  -10.14600 1.000 80.38338  ? 39  TYR B C   1 
ATOM   1533 O O   . TYR B 1 41  ? 13.48700 -7.22900  -9.47300  1.000 81.38188  ? 39  TYR B O   1 
ATOM   1534 C CB  . TYR B 1 41  ? 13.60600 -7.87200  -12.48200 1.000 82.72414  ? 39  TYR B CB  1 
ATOM   1535 C CG  . TYR B 1 41  ? 13.22400 -8.47500  -13.80700 1.000 84.16757  ? 39  TYR B CG  1 
ATOM   1536 C CD1 . TYR B 1 41  ? 12.40900 -7.78300  -14.68900 1.000 86.63071  ? 39  TYR B CD1 1 
ATOM   1537 C CD2 . TYR B 1 41  ? 13.68100 -9.73200  -14.18100 1.000 76.89733  ? 39  TYR B CD2 1 
ATOM   1538 C CE1 . TYR B 1 41  ? 12.05500 -8.32200  -15.90500 1.000 85.17783  ? 39  TYR B CE1 1 
ATOM   1539 C CE2 . TYR B 1 41  ? 13.33400 -10.28000 -15.40100 1.000 76.33002  ? 39  TYR B CE2 1 
ATOM   1540 C CZ  . TYR B 1 41  ? 12.51700 -9.57100  -16.25800 1.000 74.55112  ? 39  TYR B CZ  1 
ATOM   1541 O OH  . TYR B 1 41  ? 12.15600 -10.10900 -17.47000 1.000 75.87306  ? 39  TYR B OH  1 
ATOM   1542 N N   . TYR B 1 42  ? 12.17200 -9.05500  -9.68800  1.000 67.62597  ? 40  TYR B N   1 
ATOM   1543 C CA  . TYR B 1 42  ? 12.36500 -9.53000  -8.32600  1.000 68.29267  ? 40  TYR B CA  1 
ATOM   1544 C C   . TYR B 1 42  ? 12.75600 -10.99800 -8.35000  1.000 59.02034  ? 40  TYR B C   1 
ATOM   1545 O O   . TYR B 1 42  ? 12.06600 -11.82000 -8.96700  1.000 56.92082  ? 40  TYR B O   1 
ATOM   1546 C CB  . TYR B 1 42  ? 11.09600 -9.33000  -7.48200  1.000 72.01635  ? 40  TYR B CB  1 
ATOM   1547 C CG  . TYR B 1 42  ? 10.74400 -7.87500  -7.23200  1.000 82.25512  ? 40  TYR B CG  1 
ATOM   1548 C CD1 . TYR B 1 42  ? 11.57000 -7.06000  -6.44500  1.000 83.09352  ? 40  TYR B CD1 1 
ATOM   1549 C CD2 . TYR B 1 42  ? 9.59500  -7.31000  -7.78400  1.000 80.26732  ? 40  TYR B CD2 1 
ATOM   1550 C CE1 . TYR B 1 42  ? 11.25600 -5.72200  -6.21600  1.000 81.44250  ? 40  TYR B CE1 1 
ATOM   1551 C CE2 . TYR B 1 42  ? 9.26800  -5.97400  -7.55600  1.000 82.93730  ? 40  TYR B CE2 1 
ATOM   1552 C CZ  . TYR B 1 42  ? 10.10500 -5.18600  -6.77300  1.000 84.68248  ? 40  TYR B CZ  1 
ATOM   1553 O OH  . TYR B 1 42  ? 9.80400  -3.86300  -6.53800  1.000 78.28103  ? 40  TYR B OH  1 
ATOM   1554 N N   . GLY B 1 43  ? 13.85300 -11.32100 -7.66800  1.000 58.81042  ? 41  GLY B N   1 
ATOM   1555 C CA  . GLY B 1 43  ? 14.30300 -12.69000 -7.53800  1.000 60.92571  ? 41  GLY B CA  1 
ATOM   1556 C C   . GLY B 1 43  ? 14.41600 -13.14500 -6.09700  1.000 56.25978  ? 41  GLY B C   1 
ATOM   1557 O O   . GLY B 1 43  ? 14.46600 -12.32700 -5.17000  1.000 61.53717  ? 41  GLY B O   1 
ATOM   1558 N N   . TRP B 1 44  ? 14.44900 -14.45700 -5.89100  1.000 54.49868  ? 42  TRP B N   1 
ATOM   1559 C CA  . TRP B 1 44  ? 14.75000 -15.00200 -4.57700  1.000 49.47385  ? 42  TRP B CA  1 
ATOM   1560 C C   . TRP B 1 44  ? 15.53300 -16.28500 -4.77300  1.000 58.39734  ? 42  TRP B C   1 
ATOM   1561 O O   . TRP B 1 44  ? 15.40900 -16.94900 -5.81000  1.000 57.24359  ? 42  TRP B O   1 
ATOM   1562 C CB  . TRP B 1 44  ? 13.48700 -15.27400 -3.75600  1.000 51.18254  ? 42  TRP B CB  1 
ATOM   1563 C CG  . TRP B 1 44  ? 12.70100 -14.02700 -3.45300  1.000 60.90112  ? 42  TRP B CG  1 
ATOM   1564 C CD1 . TRP B 1 44  ? 12.83800 -13.20700 -2.36500  1.000 66.45689  ? 42  TRP B CD1 1 
ATOM   1565 C CD2 . TRP B 1 44  ? 11.65700 -13.46100 -4.24800  1.000 58.00432  ? 42  TRP B CD2 1 
ATOM   1566 N NE1 . TRP B 1 44  ? 11.94300 -12.16700 -2.43800  1.000 64.78914  ? 42  TRP B NE1 1 
ATOM   1567 C CE2 . TRP B 1 44  ? 11.21100 -12.30000 -3.58800  1.000 65.61137  ? 42  TRP B CE2 1 
ATOM   1568 C CE3 . TRP B 1 44  ? 11.05400 -13.81900 -5.46300  1.000 60.49962  ? 42  TRP B CE3 1 
ATOM   1569 C CZ2 . TRP B 1 44  ? 10.19100 -11.50300 -4.09600  1.000 62.49412  ? 42  TRP B CZ2 1 
ATOM   1570 C CZ3 . TRP B 1 44  ? 10.04400 -13.02000 -5.96100  1.000 57.00788  ? 42  TRP B CZ3 1 
ATOM   1571 C CH2 . TRP B 1 44  ? 9.62300  -11.87900 -5.27800  1.000 59.19703  ? 42  TRP B CH2 1 
ATOM   1572 N N   . VAL B 1 45  ? 16.35700 -16.61100 -3.78500  1.000 49.59320  ? 43  VAL B N   1 
ATOM   1573 C CA  . VAL B 1 45  ? 17.10200 -17.86100 -3.77900  1.000 50.82997  ? 43  VAL B CA  1 
ATOM   1574 C C   . VAL B 1 45  ? 16.72100 -18.64300 -2.54300  1.000 60.86563  ? 43  VAL B C   1 
ATOM   1575 O O   . VAL B 1 45  ? 16.27400 -18.08000 -1.54000  1.000 59.17989  ? 43  VAL B O   1 
ATOM   1576 C CB  . VAL B 1 45  ? 18.62200 -17.62900 -3.83800  1.000 50.56340  ? 43  VAL B CB  1 
ATOM   1577 C CG1 . VAL B 1 45  ? 18.95100 -16.76800 -5.09000  1.000 49.84877  ? 43  VAL B CG1 1 
ATOM   1578 C CG2 . VAL B 1 45  ? 19.10400 -16.98500 -2.56900  1.000 53.69221  ? 43  VAL B CG2 1 
ATOM   1579 N N   . MET B 1 46  ? 16.88500 -19.95200 -2.61500  1.000 59.02465  ? 44  MET B N   1 
ATOM   1580 C CA  . MET B 1 46  ? 16.76200 -20.77600 -1.43200  1.000 58.13259  ? 44  MET B CA  1 
ATOM   1581 C C   . MET B 1 46  ? 18.16600 -21.16700 -1.01100  1.000 61.65905  ? 44  MET B C   1 
ATOM   1582 O O   . MET B 1 46  ? 18.91700 -21.73700 -1.80900  1.000 56.88212  ? 44  MET B O   1 
ATOM   1583 C CB  . MET B 1 46  ? 15.90000 -22.00900 -1.67100  1.000 57.07035  ? 44  MET B CB  1 
ATOM   1584 C CG  . MET B 1 46  ? 15.67600 -22.72200 -0.36400  1.000 58.86081  ? 44  MET B CG  1 
ATOM   1585 S SD  . MET B 1 46  ? 14.99900 -24.37600 -0.45400  1.000 62.02480  ? 44  MET B SD  1 
ATOM   1586 C CE  . MET B 1 46  ? 13.26700 -23.92400 -0.59700  1.000 61.30100  ? 44  MET B CE  1 
ATOM   1587 N N   . GLU B 1 47  ? 18.53300 -20.80800 0.21100   1.000 60.38815  ? 45  GLU B N   1 
ATOM   1588 C CA  . GLU B 1 47  ? 19.83100 -21.12800 0.77600   1.000 60.91308  ? 45  GLU B CA  1 
ATOM   1589 C C   . GLU B 1 47  ? 19.67700 -22.32400 1.70000   1.000 71.76895  ? 45  GLU B C   1 
ATOM   1590 O O   . GLU B 1 47  ? 18.96400 -22.24900 2.70500   1.000 74.49065  ? 45  GLU B O   1 
ATOM   1591 C CB  . GLU B 1 47  ? 20.40000 -19.94400 1.55300   1.000 66.01054  ? 45  GLU B CB  1 
ATOM   1592 C CG  . GLU B 1 47  ? 21.66400 -19.37300 0.94800   1.000 71.59760  ? 45  GLU B CG  1 
ATOM   1593 C CD  . GLU B 1 47  ? 22.48000 -18.55300 1.92600   1.000 75.72184  ? 45  GLU B CD  1 
ATOM   1594 O OE1 . GLU B 1 47  ? 22.08000 -17.40800 2.22500   1.000 75.72025  ? 45  GLU B OE1 1 
ATOM   1595 O OE2 . GLU B 1 47  ? 23.51900 -19.06200 2.40300   1.000 84.29380  ? 45  GLU B OE2 1 
ATOM   1596 N N   . SER B 1 48  ? 20.33700 -23.41800 1.35700   1.000 70.52437  ? 46  SER B N   1 
ATOM   1597 C CA  . SER B 1 48  ? 20.50800 -24.54600 2.25600   1.000 77.91381  ? 46  SER B CA  1 
ATOM   1598 C C   . SER B 1 48  ? 22.00000 -24.71800 2.45200   1.000 72.75016  ? 46  SER B C   1 
ATOM   1599 O O   . SER B 1 48  ? 22.77000 -24.45700 1.53200   1.000 80.54722  ? 46  SER B O   1 
ATOM   1600 C CB  . SER B 1 48  ? 19.87900 -25.82400 1.69000   1.000 82.12347  ? 46  SER B CB  1 
ATOM   1601 O OG  . SER B 1 48  ? 19.95700 -26.89500 2.61300   1.000 78.86771  ? 46  SER B OG  1 
ATOM   1602 N N   . ASP B 1 49  ? 22.39600 -25.09400 3.66500   1.000 86.00542  ? 47  ASP B N   1 
ATOM   1603 C CA  . ASP B 1 49  ? 23.78900 -25.34500 4.01800   1.000 79.59151  ? 47  ASP B CA  1 
ATOM   1604 C C   . ASP B 1 49  ? 24.78500 -24.51600 3.21200   1.000 70.97121  ? 47  ASP B C   1 
ATOM   1605 O O   . ASP B 1 49  ? 25.61600 -25.07000 2.48700   1.000 71.60767  ? 47  ASP B O   1 
ATOM   1606 C CB  . ASP B 1 49  ? 24.08300 -26.83600 3.86700   1.000 86.04042  ? 47  ASP B CB  1 
ATOM   1607 C CG  . ASP B 1 49  ? 23.30400 -27.68500 4.86800   1.000 96.74804  ? 47  ASP B CG  1 
ATOM   1608 O OD1 . ASP B 1 49  ? 22.96600 -27.17100 5.96200   1.000 83.10333  ? 47  ASP B OD1 1 
ATOM   1609 O OD2 . ASP B 1 49  ? 23.02600 -28.86400 4.55800   1.000 102.86929 ? 47  ASP B OD2 1 
ATOM   1610 N N   . HIS B 1 50  ? 24.67000 -23.18800 3.30300   1.000 70.21221  ? 48  HIS B N   1 
ATOM   1611 C CA  . HIS B 1 50  ? 25.65900 -22.25600 2.75700   1.000 68.72096  ? 48  HIS B CA  1 
ATOM   1612 C C   . HIS B 1 50  ? 25.87100 -22.43400 1.26200   1.000 66.64761  ? 48  HIS B C   1 
ATOM   1613 O O   . HIS B 1 50  ? 26.98300 -22.23500 0.76400   1.000 64.87733  ? 48  HIS B O   1 
ATOM   1614 C CB  . HIS B 1 50  ? 27.00600 -22.38400 3.47700   1.000 67.85954  ? 48  HIS B CB  1 
ATOM   1615 C CG  . HIS B 1 50  ? 26.91300 -22.29900 4.96600   1.000 69.38534  ? 48  HIS B CG  1 
ATOM   1616 N ND1 . HIS B 1 50  ? 26.84300 -21.09900 5.64000   1.000 70.27269  ? 48  HIS B ND1 1 
ATOM   1617 C CD2 . HIS B 1 50  ? 26.89100 -23.26400 5.91200   1.000 72.98022  ? 48  HIS B CD2 1 
ATOM   1618 C CE1 . HIS B 1 50  ? 26.77400 -21.32900 6.93800   1.000 69.81294  ? 48  HIS B CE1 1 
ATOM   1619 N NE2 . HIS B 1 50  ? 26.79700 -22.63500 7.13000   1.000 73.19717  ? 48  HIS B NE2 1 
ATOM   1620 N N   . HIS B 1 51  ? 24.82200 -22.81900 0.54100   1.000 71.09502  ? 49  HIS B N   1 
ATOM   1621 C CA  . HIS B 1 51  ? 24.87300 -22.85200 -0.91200  1.000 66.64670  ? 49  HIS B CA  1 
ATOM   1622 C C   . HIS B 1 51  ? 23.44500 -22.74300 -1.42600  1.000 62.26339  ? 49  HIS B C   1 
ATOM   1623 O O   . HIS B 1 51  ? 22.48500 -23.03200 -0.70900  1.000 61.93733  ? 49  HIS B O   1 
ATOM   1624 C CB  . HIS B 1 51  ? 25.60600 -24.10200 -1.44200  1.000 68.92497  ? 49  HIS B CB  1 
ATOM   1625 C CG  . HIS B 1 51  ? 24.83400 -25.38400 -1.33800  1.000 73.49195  ? 49  HIS B CG  1 
ATOM   1626 N ND1 . HIS B 1 51  ? 24.01500 -25.68500 -0.27300  1.000 83.80242  ? 49  HIS B ND1 1 
ATOM   1627 C CD2 . HIS B 1 51  ? 24.77100 -26.45600 -2.16600  1.000 83.56674  ? 49  HIS B CD2 1 
ATOM   1628 C CE1 . HIS B 1 51  ? 23.46800 -26.87500 -0.45300  1.000 81.21636  ? 49  HIS B CE1 1 
ATOM   1629 N NE2 . HIS B 1 51  ? 23.91400 -27.36700 -1.59400  1.000 79.82760  ? 49  HIS B NE2 1 
ATOM   1630 N N   . LEU B 1 52  ? 23.32200 -22.27500 -2.66800  1.000 57.01335  ? 50  LEU B N   1 
ATOM   1631 C CA  . LEU B 1 52  ? 22.03100 -22.07700 -3.30300  1.000 59.76220  ? 50  LEU B CA  1 
ATOM   1632 C C   . LEU B 1 52  ? 21.54900 -23.36600 -3.95700  1.000 59.25552  ? 50  LEU B C   1 
ATOM   1633 O O   . LEU B 1 52  ? 22.34200 -24.13900 -4.51400  1.000 55.68017  ? 50  LEU B O   1 
ATOM   1634 C CB  . LEU B 1 52  ? 22.12000 -20.97100 -4.35200  1.000 48.72827  ? 50  LEU B CB  1 
ATOM   1635 C CG  . LEU B 1 52  ? 22.56300 -19.62100 -3.79200  1.000 59.63083  ? 50  LEU B CG  1 
ATOM   1636 C CD1 . LEU B 1 52  ? 22.30300 -18.51600 -4.79600  1.000 50.09827  ? 50  LEU B CD1 1 
ATOM   1637 C CD2 . LEU B 1 52  ? 21.82800 -19.33200 -2.52800  1.000 51.78340  ? 50  LEU B CD2 1 
ATOM   1638 N N   . VAL B 1 53  ? 20.23800 -23.59600 -3.88400  1.000 52.36094  ? 51  VAL B N   1 
ATOM   1639 C CA  . VAL B 1 53  ? 19.66000 -24.84500 -4.36100  1.000 49.97080  ? 51  VAL B CA  1 
ATOM   1640 C C   . VAL B 1 53  ? 18.53400 -24.56100 -5.34200  1.000 44.26953  ? 51  VAL B C   1 
ATOM   1641 O O   . VAL B 1 53  ? 18.04900 -25.48300 -6.00700  1.000 46.97735  ? 51  VAL B O   1 
ATOM   1642 C CB  . VAL B 1 53  ? 19.14800 -25.71100 -3.20200  1.000 52.27145  ? 51  VAL B CB  1 
ATOM   1643 C CG1 . VAL B 1 53  ? 20.30800 -26.04800 -2.25500  1.000 57.46085  ? 51  VAL B CG1 1 
ATOM   1644 C CG2 . VAL B 1 53  ? 18.03800 -24.99400 -2.46300  1.000 51.73327  ? 51  VAL B CG2 1 
ATOM   1645 N N   . GLY B 1 54  ? 18.12300 -23.29400 -5.44400  1.000 48.40868  ? 52  GLY B N   1 
ATOM   1646 C CA  . GLY B 1 54  ? 17.05300 -22.90700 -6.35500  1.000 43.12478  ? 52  GLY B CA  1 
ATOM   1647 C C   . GLY B 1 54  ? 16.88700 -21.40300 -6.38600  1.000 40.37094  ? 52  GLY B C   1 
ATOM   1648 O O   . GLY B 1 54  ? 17.44100 -20.67500 -5.54900  1.000 43.39606  ? 52  GLY B O   1 
ATOM   1649 N N   . PHE B 1 55  ? 16.12300 -20.94000 -7.37400  1.000 40.39084  ? 53  PHE B N   1 
ATOM   1650 C CA  . PHE B 1 55  ? 15.83600 -19.51600 -7.50100  1.000 40.84519  ? 53  PHE B CA  1 
ATOM   1651 C C   . PHE B 1 55  ? 14.51600 -19.35200 -8.23300  1.000 42.20959  ? 53  PHE B C   1 
ATOM   1652 O O   . PHE B 1 55  ? 14.04500 -20.27000 -8.91400  1.000 36.65951  ? 53  PHE B O   1 
ATOM   1653 C CB  . PHE B 1 55  ? 16.95900 -18.75400 -8.22700  1.000 40.60716  ? 53  PHE B CB  1 
ATOM   1654 C CG  . PHE B 1 55  ? 17.11600 -19.12100 -9.68600  1.000 33.57196  ? 53  PHE B CG  1 
ATOM   1655 C CD1 . PHE B 1 55  ? 17.94600 -20.16700 -10.07500 1.000 43.08853  ? 53  PHE B CD1 1 
ATOM   1656 C CD2 . PHE B 1 55  ? 16.44400 -18.41300 -10.66300 1.000 40.74617  ? 53  PHE B CD2 1 
ATOM   1657 C CE1 . PHE B 1 55  ? 18.09200 -20.48900 -11.44200 1.000 35.86164  ? 53  PHE B CE1 1 
ATOM   1658 C CE2 . PHE B 1 55  ? 16.59100 -18.73700 -12.02200 1.000 43.25600  ? 53  PHE B CE2 1 
ATOM   1659 C CZ  . PHE B 1 55  ? 17.41300 -19.77200 -12.39900 1.000 38.19696  ? 53  PHE B CZ  1 
ATOM   1660 N N   . ILE B 1 56  ? 13.90800 -18.17600 -8.06300  1.000 41.47587  ? 54  ILE B N   1 
ATOM   1661 C CA  . ILE B 1 56  ? 12.65800 -17.81800 -8.74400  1.000 44.32622  ? 54  ILE B CA  1 
ATOM   1662 C C   . ILE B 1 56  ? 12.70500 -16.32300 -9.04000  1.000 52.55283  ? 54  ILE B C   1 
ATOM   1663 O O   . ILE B 1 56  ? 13.26700 -15.54000 -8.26100  1.000 44.52147  ? 54  ILE B O   1 
ATOM   1664 C CB  . ILE B 1 56  ? 11.41200 -18.20200 -7.90600  1.000 35.91943  ? 54  ILE B CB  1 
ATOM   1665 C CG1 . ILE B 1 56  ? 10.12100 -17.75800 -8.59200  1.000 37.11917  ? 54  ILE B CG1 1 
ATOM   1666 C CG2 . ILE B 1 56  ? 11.54700 -17.64800 -6.49900  1.000 36.39884  ? 54  ILE B CG2 1 
ATOM   1667 C CD1 . ILE B 1 56  ? 8.87800  -18.42700 -8.04300  1.000 35.87503  ? 54  ILE B CD1 1 
ATOM   1668 N N   . VAL B 1 57  ? 12.14700 -15.94400 -10.18800 1.000 40.51709  ? 55  VAL B N   1 
ATOM   1669 C CA  . VAL B 1 57  ? 12.20700 -14.58300 -10.72100 1.000 36.41010  ? 55  VAL B CA  1 
ATOM   1670 C C   . VAL B 1 57  ? 10.82000 -14.21700 -11.23300 1.000 44.93563  ? 55  VAL B C   1 
ATOM   1671 O O   . VAL B 1 57  ? 10.26000 -14.92900 -12.07600 1.000 37.22306  ? 55  VAL B O   1 
ATOM   1672 C CB  . VAL B 1 57  ? 13.23300 -14.45700 -11.86100 1.000 38.76690  ? 55  VAL B CB  1 
ATOM   1673 C CG1 . VAL B 1 57  ? 13.29500 -13.03100 -12.33800 1.000 38.96075  ? 55  VAL B CG1 1 
ATOM   1674 C CG2 . VAL B 1 57  ? 14.59400 -14.94100 -11.43200 1.000 44.99198  ? 55  VAL B CG2 1 
ATOM   1675 N N   . ILE B 1 58  ? 10.26800 -13.10300 -10.74600 1.000 37.51145  ? 56  ILE B N   1 
ATOM   1676 C CA  . ILE B 1 58  ? 8.96100  -12.62900 -11.19600 1.000 46.32904  ? 56  ILE B CA  1 
ATOM   1677 C C   . ILE B 1 58  ? 9.06900  -11.18300 -11.66300 1.000 44.96620  ? 56  ILE B C   1 
ATOM   1678 O O   . ILE B 1 58  ? 10.03600 -10.48100 -11.36400 1.000 54.39636  ? 56  ILE B O   1 
ATOM   1679 C CB  . ILE B 1 58  ? 7.88700  -12.73200 -10.09100 1.000 40.29363  ? 56  ILE B CB  1 
ATOM   1680 C CG1 . ILE B 1 58  ? 8.28200  -11.84100 -8.91200  1.000 45.39173  ? 56  ILE B CG1 1 
ATOM   1681 C CG2 . ILE B 1 58  ? 7.71200  -14.17300 -9.63800  1.000 42.30980  ? 56  ILE B CG2 1 
ATOM   1682 C CD1 . ILE B 1 58  ? 7.14200  -11.54000 -7.97800  1.000 47.03576  ? 56  ILE B CD1 1 
ATOM   1683 N N   . LEU B 1 59  ? 8.03700  -10.73500 -12.37700 1.000 51.06147  ? 57  LEU B N   1 
ATOM   1684 C CA  . LEU B 1 59  ? 7.90400  -9.35500  -12.84100 1.000 56.38650  ? 57  LEU B CA  1 
ATOM   1685 C C   . LEU B 1 59  ? 6.51600  -8.84300  -12.47200 1.000 64.64219  ? 57  LEU B C   1 
ATOM   1686 O O   . LEU B 1 59  ? 5.52100  -9.51200  -12.76300 1.000 65.41231  ? 57  LEU B O   1 
ATOM   1687 C CB  . LEU B 1 59  ? 8.13200  -9.27800  -14.36200 1.000 58.72446  ? 57  LEU B CB  1 
ATOM   1688 C CG  . LEU B 1 59  ? 7.67400  -8.09600  -15.22800 1.000 64.06564  ? 57  LEU B CG  1 
ATOM   1689 C CD1 . LEU B 1 59  ? 8.63800  -7.86600  -16.38600 1.000 66.07684  ? 57  LEU B CD1 1 
ATOM   1690 C CD2 . LEU B 1 59  ? 6.29700  -8.36600  -15.79600 1.000 63.27625  ? 57  LEU B CD2 1 
ATOM   1691 N N   . MET B 1 60  ? 6.43400  -7.65300  -11.85300 1.000 68.56136  ? 58  MET B N   1 
ATOM   1692 C CA  . MET B 1 60  ? 5.16000  -7.09900  -11.38200 1.000 71.84949  ? 58  MET B CA  1 
ATOM   1693 C C   . MET B 1 60  ? 4.71000  -5.93300  -12.26200 1.000 81.28358  ? 58  MET B C   1 
ATOM   1694 O O   . MET B 1 60  ? 5.28600  -4.83900  -12.19900 1.000 80.19163  ? 58  MET B O   1 
ATOM   1695 C CB  . MET B 1 60  ? 5.27600  -6.66700  -9.92700  1.000 75.65794  ? 58  MET B CB  1 
ATOM   1696 C CG  . MET B 1 60  ? 5.62000  -7.81900  -9.02700  1.000 75.25160  ? 58  MET B CG  1 
ATOM   1697 S SD  . MET B 1 60  ? 4.35900  -8.10600  -7.77400  1.000 88.98328  ? 58  MET B SD  1 
ATOM   1698 C CE  . MET B 1 60  ? 4.66200  -6.69500  -6.72600  1.000 84.16531  ? 58  MET B CE  1 
ATOM   1699 N N   . GLN B 1 61  ? 3.64300  -6.16500  -13.04100 1.000 95.14135  ? 59  GLN B N   1 
ATOM   1700 C CA  . GLN B 1 61  ? 3.13400  -5.24000  -14.05100 1.000 99.33966  ? 59  GLN B CA  1 
ATOM   1701 C C   . GLN B 1 61  ? 1.64600  -4.99200  -13.83500 1.000 101.38119 ? 59  GLN B C   1 
ATOM   1702 O O   . GLN B 1 61  ? 0.89600  -5.90600  -13.48500 1.000 95.71723  ? 59  GLN B O   1 
ATOM   1703 C CB  . GLN B 1 61  ? 3.36000  -5.78200  -15.49000 1.000 97.00998  ? 59  GLN B CB  1 
ATOM   1704 C CG  . GLN B 1 61  ? 2.26800  -6.73800  -16.05100 1.000 101.46870 ? 59  GLN B CG  1 
ATOM   1705 C CD  . GLN B 1 61  ? 2.38300  -8.19100  -15.56400 1.000 94.87043  ? 59  GLN B CD  1 
ATOM   1706 O OE1 . GLN B 1 61  ? 3.10000  -8.48900  -14.61100 1.000 92.97845  ? 59  GLN B OE1 1 
ATOM   1707 N NE2 . GLN B 1 61  ? 1.67200  -9.09600  -16.23100 1.000 87.60244  ? 59  GLN B NE2 1 
ATOM   1708 N N   . GLU B 1 62  ? 1.22000  -3.74900  -14.07200 1.000 104.44517 ? 60  GLU B N   1 
ATOM   1709 C CA  . GLU B 1 62  ? -0.17900 -3.37600  -13.88800 1.000 110.51898 ? 60  GLU B CA  1 
ATOM   1710 C C   . GLU B 1 62  ? -0.68600 -3.84400  -12.52700 1.000 108.09609 ? 60  GLU B C   1 
ATOM   1711 O O   . GLU B 1 62  ? -0.25500 -3.33000  -11.48900 1.000 104.89498 ? 60  GLU B O   1 
ATOM   1712 C CB  . GLU B 1 62  ? -1.04000 -3.94900  -15.02100 1.000 113.94152 ? 60  GLU B CB  1 
ATOM   1713 C CG  . GLU B 1 62  ? -0.97900 -3.13200  -16.30800 1.000 119.37791 ? 60  GLU B CG  1 
ATOM   1714 C CD  . GLU B 1 62  ? -0.86600 -3.99000  -17.55700 1.000 126.41992 ? 60  GLU B CD  1 
ATOM   1715 O OE1 . GLU B 1 62  ? -1.68000 -4.92600  -17.72400 1.000 133.27136 ? 60  GLU B OE1 1 
ATOM   1716 O OE2 . GLU B 1 62  ? 0.04800  -3.72700  -18.36900 1.000 128.15451 ? 60  GLU B OE2 1 
ATOM   1717 N N   . LYS B 1 63  ? -1.59900 -4.81900  -12.52700 1.000 107.97152 ? 61  LYS B N   1 
ATOM   1718 C CA  . LYS B 1 63  ? -2.01100 -5.52900  -11.32000 1.000 107.29783 ? 61  LYS B CA  1 
ATOM   1719 C C   . LYS B 1 63  ? -1.63600 -7.00500  -11.36800 1.000 101.43692 ? 61  LYS B C   1 
ATOM   1720 O O   . LYS B 1 63  ? -1.85500 -7.73000  -10.38700 1.000 87.75134  ? 61  LYS B O   1 
ATOM   1721 C CB  . LYS B 1 63  ? -3.52500 -5.38600  -11.09800 1.000 102.37591 ? 61  LYS B CB  1 
ATOM   1722 C CG  . LYS B 1 63  ? -3.96600 -4.03700  -10.54400 1.000 105.55345 ? 61  LYS B CG  1 
ATOM   1723 C CD  . LYS B 1 63  ? -3.82100 -3.97000  -9.02800  1.000 103.33801 ? 61  LYS B CD  1 
ATOM   1724 C CE  . LYS B 1 63  ? -4.76000 -2.93200  -8.43800  1.000 106.54670 ? 61  LYS B CE  1 
ATOM   1725 N NZ  . LYS B 1 63  ? -5.39700 -3.40100  -7.17200  1.000 110.46884 ? 61  LYS B NZ  1 
ATOM   1726 N N   . GLU B 1 64  ? -1.07600 -7.46800  -12.47700 1.000 103.07542 ? 62  GLU B N   1 
ATOM   1727 C CA  . GLU B 1 64  ? -0.66900 -8.85000  -12.62800 1.000 100.99285 ? 62  GLU B CA  1 
ATOM   1728 C C   . GLU B 1 64  ? 0.81000  -9.01100  -12.28800 1.000 99.11350  ? 62  GLU B C   1 
ATOM   1729 O O   . GLU B 1 64  ? 1.53800  -8.05700  -11.99600 1.000 94.53677  ? 62  GLU B O   1 
ATOM   1730 C CB  . GLU B 1 64  ? -0.95200 -9.33600  -14.05100 1.000 97.73167  ? 62  GLU B CB  1 
ATOM   1731 C CG  . GLU B 1 64  ? -2.32500 -8.95500  -14.58500 1.000 103.39195 ? 62  GLU B CG  1 
ATOM   1732 C CD  . GLU B 1 64  ? -3.45000 -9.80400  -14.01300 1.000 100.97929 ? 62  GLU B CD  1 
ATOM   1733 O OE1 . GLU B 1 64  ? -3.66900 -9.77600  -12.78200 1.000 100.37860 ? 62  GLU B OE1 1 
ATOM   1734 O OE2 . GLU B 1 64  ? -4.11700 -10.50600 -14.80200 1.000 94.12044  ? 62  GLU B OE2 1 
ATOM   1735 N N   . CYS B 1 65  ? 1.25000  -10.25800 -12.31000 1.000 77.13344  ? 63  CYS B N   1 
ATOM   1736 C CA  . CYS B 1 65  ? 2.65600  -10.57000 -12.21900 1.000 63.83833  ? 63  CYS B CA  1 
ATOM   1737 C C   . CYS B 1 65  ? 2.91300  -11.72400 -13.16400 1.000 52.64728  ? 63  CYS B C   1 
ATOM   1738 O O   . CYS B 1 65  ? 1.98900  -12.41700 -13.59600 1.000 51.10583  ? 63  CYS B O   1 
ATOM   1739 C CB  . CYS B 1 65  ? 3.08800  -10.90500 -10.78400 1.000 69.95434  ? 63  CYS B CB  1 
ATOM   1740 S SG  . CYS B 1 65  ? 1.94300  -11.95700 -9.89300  1.000 74.03243  ? 63  CYS B SG  1 
ATOM   1741 N N   . GLN B 1 66  ? 4.18200  -11.89800 -13.50000 1.000 45.95460  ? 64  GLN B N   1 
ATOM   1742 C CA  . GLN B 1 66  ? 4.61000  -12.89000 -14.46900 1.000 45.79421  ? 64  GLN B CA  1 
ATOM   1743 C C   . GLN B 1 66  ? 5.79400  -13.63700 -13.89000 1.000 37.79696  ? 64  GLN B C   1 
ATOM   1744 O O   . GLN B 1 66  ? 6.73500  -13.02200 -13.38000 1.000 43.13990  ? 64  GLN B O   1 
ATOM   1745 C CB  . GLN B 1 66  ? 4.98900  -12.24100 -15.80200 1.000 47.72460  ? 64  GLN B CB  1 
ATOM   1746 C CG  . GLN B 1 66  ? 5.27800  -13.24900 -16.92600 1.000 41.88108  ? 64  GLN B CG  1 
ATOM   1747 C CD  . GLN B 1 66  ? 5.56800  -12.56700 -18.27100 1.000 48.04345  ? 64  GLN B CD  1 
ATOM   1748 O OE1 . GLN B 1 66  ? 5.18200  -11.41800 -18.49700 1.000 50.35132  ? 64  GLN B OE1 1 
ATOM   1749 N NE2 . GLN B 1 66  ? 6.27700  -13.27100 -19.15400 1.000 38.41858  ? 64  GLN B NE2 1 
ATOM   1750 N N   . LEU B 1 67  ? 5.71900  -14.96000 -13.93100 1.000 36.00322  ? 65  LEU B N   1 
ATOM   1751 C CA  . LEU B 1 67  ? 6.82000  -15.80300 -13.50900 1.000 31.91545  ? 65  LEU B CA  1 
ATOM   1752 C C   . LEU B 1 67  ? 7.81800  -15.82100 -14.65400 1.000 34.36445  ? 65  LEU B C   1 
ATOM   1753 O O   . LEU B 1 67  ? 7.51900  -16.33900 -15.72700 1.000 33.13231  ? 65  LEU B O   1 
ATOM   1754 C CB  . LEU B 1 67  ? 6.30800  -17.20600 -13.19800 1.000 31.62257  ? 65  LEU B CB  1 
ATOM   1755 C CG  . LEU B 1 67  ? 7.34100  -18.27600 -12.82300 1.000 29.58068  ? 65  LEU B CG  1 
ATOM   1756 C CD1 . LEU B 1 67  ? 8.20400  -17.80400 -11.68600 1.000 35.03060  ? 65  LEU B CD1 1 
ATOM   1757 C CD2 . LEU B 1 67  ? 6.63000  -19.56200 -12.44400 1.000 36.16349  ? 65  LEU B CD2 1 
ATOM   1758 N N   . MET B 1 68  ? 8.98500  -15.21900 -14.45900 1.000 32.12955  ? 66  MET B N   1 
ATOM   1759 C CA  . MET B 1 68  ? 9.91100  -15.19300 -15.58200 1.000 36.98056  ? 66  MET B CA  1 
ATOM   1760 C C   . MET B 1 68  ? 10.79100 -16.44000 -15.61400 1.000 39.25221  ? 66  MET B C   1 
ATOM   1761 O O   . MET B 1 68  ? 11.18100 -16.89100 -16.70300 1.000 31.88962  ? 66  MET B O   1 
ATOM   1762 C CB  . MET B 1 68  ? 10.76600 -13.92200 -15.54300 1.000 40.76621  ? 66  MET B CB  1 
ATOM   1763 C CG  . MET B 1 68  ? 10.00100 -12.58900 -15.55900 1.000 33.53977  ? 66  MET B CG  1 
ATOM   1764 S SD  . MET B 1 68  ? 8.68700  -12.48100 -16.75600 1.000 40.54673  ? 66  MET B SD  1 
ATOM   1765 C CE  . MET B 1 68  ? 9.57700  -12.66200 -18.29000 1.000 34.86973  ? 66  MET B CE  1 
ATOM   1766 N N   . ASN B 1 69  ? 11.09700 -17.02200 -14.45600 1.000 32.25792  ? 67  ASN B N   1 
ATOM   1767 C CA  . ASN B 1 69  ? 12.01300 -18.15000 -14.37200 1.000 25.64036  ? 67  ASN B CA  1 
ATOM   1768 C C   . ASN B 1 69  ? 11.91000 -18.76700 -12.98100 1.000 30.10038  ? 67  ASN B C   1 
ATOM   1769 O O   . ASN B 1 69  ? 11.71700 -18.05600 -11.99200 1.000 35.66368  ? 67  ASN B O   1 
ATOM   1770 C CB  . ASN B 1 69  ? 13.45600 -17.72300 -14.67900 1.000 34.89695  ? 67  ASN B CB  1 
ATOM   1771 C CG  . ASN B 1 69  ? 14.35700 -18.89200 -15.10900 1.000 29.96355  ? 67  ASN B CG  1 
ATOM   1772 O OD1 . ASN B 1 69  ? 13.96600 -20.05500 -15.06200 1.000 37.51962  ? 67  ASN B OD1 1 
ATOM   1773 N ND2 . ASN B 1 69  ? 15.59000 -18.57300 -15.48800 1.000 34.48489  ? 67  ASN B ND2 1 
ATOM   1774 N N   . ILE B 1 70  ? 11.99300 -20.08900 -12.92100 1.000 32.52664  ? 68  ILE B N   1 
ATOM   1775 C CA  . ILE B 1 70  ? 12.07900 -20.83500 -11.67000 1.000 33.10905  ? 68  ILE B CA  1 
ATOM   1776 C C   . ILE B 1 70  ? 12.88500 -22.08700 -11.96400 1.000 33.97953  ? 68  ILE B C   1 
ATOM   1777 O O   . ILE B 1 70  ? 12.64700 -22.74800 -12.97800 1.000 35.68096  ? 68  ILE B O   1 
ATOM   1778 C CB  . ILE B 1 70  ? 10.68500 -21.18000 -11.11000 1.000 32.72502  ? 68  ILE B CB  1 
ATOM   1779 C CG1 . ILE B 1 70  ? 10.82900 -21.94900 -9.79800  1.000 29.73332  ? 68  ILE B CG1 1 
ATOM   1780 C CG2 . ILE B 1 70  ? 9.88600  -21.97700 -12.11000 1.000 33.66376  ? 68  ILE B CG2 1 
ATOM   1781 C CD1 . ILE B 1 70  ? 9.61600  -21.88500 -8.89500  1.000 41.69057  ? 68  ILE B CD1 1 
ATOM   1782 N N   . ALA B 1 71  ? 13.88200 -22.38100 -11.13400 1.000 31.59869  ? 69  ALA B N   1 
ATOM   1783 C CA  . ALA B 1 71  ? 14.78900 -23.48000 -11.45300 1.000 34.44002  ? 69  ALA B CA  1 
ATOM   1784 C C   . ALA B 1 71  ? 15.40500 -24.03800 -10.17500 1.000 32.56213  ? 69  ALA B C   1 
ATOM   1785 O O   . ALA B 1 71  ? 15.72700 -23.28300 -9.25800  1.000 34.43897  ? 69  ALA B O   1 
ATOM   1786 C CB  . ALA B 1 71  ? 15.88100 -23.02500 -12.42800 1.000 35.92463  ? 69  ALA B CB  1 
ATOM   1787 N N   . VAL B 1 72  ? 15.55800 -25.37000 -10.12900 1.000 38.67945  ? 70  VAL B N   1 
ATOM   1788 C CA  . VAL B 1 72  ? 16.12500 -26.08600 -8.97800  1.000 43.95534  ? 70  VAL B CA  1 
ATOM   1789 C C   . VAL B 1 72  ? 17.21100 -27.03900 -9.47000  1.000 37.34618  ? 70  VAL B C   1 
ATOM   1790 O O   . VAL B 1 72  ? 17.06500 -27.65900 -10.52900 1.000 49.41949  ? 70  VAL B O   1 
ATOM   1791 C CB  . VAL B 1 72  ? 15.03600 -26.86200 -8.20100  1.000 38.95038  ? 70  VAL B CB  1 
ATOM   1792 C CG1 . VAL B 1 72  ? 15.64000 -27.59000 -6.98400  1.000 41.23056  ? 70  VAL B CG1 1 
ATOM   1793 C CG2 . VAL B 1 72  ? 13.97100 -25.91300 -7.73100  1.000 36.26663  ? 70  VAL B CG2 1 
ATOM   1794 N N   . ALA B 1 73  ? 18.30300 -27.15900 -8.69600  1.000 51.28015  ? 71  ALA B N   1 
ATOM   1795 C CA  . ALA B 1 73  ? 19.38400 -28.06500 -9.07000  1.000 53.39756  ? 71  ALA B CA  1 
ATOM   1796 C C   . ALA B 1 73  ? 18.85500 -29.49900 -9.17800  1.000 58.25644  ? 71  ALA B C   1 
ATOM   1797 O O   . ALA B 1 73  ? 18.11000 -29.94900 -8.29500  1.000 60.16472  ? 71  ALA B O   1 
ATOM   1798 C CB  . ALA B 1 73  ? 20.51700 -27.99400 -8.04000  1.000 57.25563  ? 71  ALA B CB  1 
ATOM   1799 N N   . PRO B 1 74  ? 19.22200 -30.24500 -10.23200 1.000 59.48399  ? 72  PRO B N   1 
ATOM   1800 C CA  . PRO B 1 74  ? 18.62800 -31.58400 -10.43200 1.000 57.44539  ? 72  PRO B CA  1 
ATOM   1801 C C   . PRO B 1 74  ? 18.85900 -32.56600 -9.28800  1.000 70.96861  ? 72  PRO B C   1 
ATOM   1802 O O   . PRO B 1 74  ? 17.99000 -33.40700 -9.02500  1.000 74.77059  ? 72  PRO B O   1 
ATOM   1803 C CB  . PRO B 1 74  ? 19.28800 -32.05700 -11.73600 1.000 70.48064  ? 72  PRO B CB  1 
ATOM   1804 C CG  . PRO B 1 74  ? 19.58400 -30.77500 -12.49000 1.000 51.88233  ? 72  PRO B CG  1 
ATOM   1805 C CD  . PRO B 1 74  ? 20.03100 -29.82500 -11.39400 1.000 64.26549  ? 72  PRO B CD  1 
ATOM   1806 N N   . ARG B 1 75  ? 20.00200 -32.50100 -8.59900  1.000 67.24726  ? 73  ARG B N   1 
ATOM   1807 C CA  . ARG B 1 75  ? 20.20100 -33.36000 -7.43600  1.000 70.15990  ? 73  ARG B CA  1 
ATOM   1808 C C   . ARG B 1 75  ? 19.21400 -33.04600 -6.31800  1.000 67.05036  ? 73  ARG B C   1 
ATOM   1809 O O   . ARG B 1 75  ? 18.95200 -33.91100 -5.47200  1.000 70.12679  ? 73  ARG B O   1 
ATOM   1810 C CB  . ARG B 1 75  ? 21.63400 -33.22500 -6.92600  1.000 74.20383  ? 73  ARG B CB  1 
ATOM   1811 C CG  . ARG B 1 75  ? 22.66600 -33.79800 -7.88300  1.000 87.22852  ? 73  ARG B CG  1 
ATOM   1812 C CD  . ARG B 1 75  ? 22.36400 -35.26500 -8.18700  1.000 88.80442  ? 73  ARG B CD  1 
ATOM   1813 N NE  . ARG B 1 75  ? 23.47800 -35.94800 -8.83900  1.000 89.55028  ? 73  ARG B NE  1 
ATOM   1814 C CZ  . ARG B 1 75  ? 23.66300 -37.26200 -8.82600  1.000 91.96179  ? 73  ARG B CZ  1 
ATOM   1815 N NH1 . ARG B 1 75  ? 22.83600 -38.07200 -8.18500  1.000 96.80473  ? 73  ARG B NH1 1 
ATOM   1816 N NH2 . ARG B 1 75  ? 24.70800 -37.77600 -9.46900  1.000 87.50474  ? 73  ARG B NH2 1 
ATOM   1817 N N   . TYR B 1 76  ? 18.64500 -31.83700 -6.30900  1.000 66.30213  ? 74  TYR B N   1 
ATOM   1818 C CA  . TYR B 1 76  ? 17.75700 -31.39000 -5.24100  1.000 63.89197  ? 74  TYR B CA  1 
ATOM   1819 C C   . TYR B 1 76  ? 16.32200 -31.18700 -5.72300  1.000 67.42897  ? 74  TYR B C   1 
ATOM   1820 O O   . TYR B 1 76  ? 15.49900 -30.64100 -4.97900  1.000 60.06848  ? 74  TYR B O   1 
ATOM   1821 C CB  . TYR B 1 76  ? 18.30300 -30.10600 -4.60100  1.000 64.09816  ? 74  TYR B CB  1 
ATOM   1822 C CG  . TYR B 1 76  ? 19.71900 -30.22900 -4.00300  1.000 68.76901  ? 74  TYR B CG  1 
ATOM   1823 C CD1 . TYR B 1 76  ? 20.28300 -31.47000 -3.69500  1.000 80.26018  ? 74  TYR B CD1 1 
ATOM   1824 C CD2 . TYR B 1 76  ? 20.48200 -29.09300 -3.74600  1.000 69.96146  ? 74  TYR B CD2 1 
ATOM   1825 C CE1 . TYR B 1 76  ? 21.57300 -31.57000 -3.14900  1.000 77.22236  ? 74  TYR B CE1 1 
ATOM   1826 C CE2 . TYR B 1 76  ? 21.76800 -29.18100 -3.20300  1.000 77.57278  ? 74  TYR B CE2 1 
ATOM   1827 C CZ  . TYR B 1 76  ? 22.30900 -30.42000 -2.90500  1.000 82.29041  ? 74  TYR B CZ  1 
ATOM   1828 O OH  . TYR B 1 76  ? 23.58100 -30.49900 -2.36500  1.000 80.34085  ? 74  TYR B OH  1 
ATOM   1829 N N   . GLN B 1 77  ? 16.00300 -31.62300 -6.94000  1.000 58.08325  ? 75  GLN B N   1 
ATOM   1830 C CA  . GLN B 1 77  ? 14.63400 -31.58900 -7.43200  1.000 55.24818  ? 75  GLN B CA  1 
ATOM   1831 C C   . GLN B 1 77  ? 13.75900 -32.61200 -6.72500  1.000 58.57183  ? 75  GLN B C   1 
ATOM   1832 O O   . GLN B 1 77  ? 14.23100 -33.61300 -6.18900  1.000 65.22669  ? 75  GLN B O   1 
ATOM   1833 C CB  . GLN B 1 77  ? 14.60000 -31.87500 -8.92200  1.000 54.21712  ? 75  GLN B CB  1 
ATOM   1834 C CG  . GLN B 1 77  ? 15.29100 -30.82200 -9.71400  1.000 50.37906  ? 75  GLN B CG  1 
ATOM   1835 C CD  . GLN B 1 77  ? 15.07000 -31.00400 -11.18700 1.000 53.39195  ? 75  GLN B CD  1 
ATOM   1836 O OE1 . GLN B 1 77  ? 14.39900 -31.94400 -11.61300 1.000 57.82443  ? 75  GLN B OE1 1 
ATOM   1837 N NE2 . GLN B 1 77  ? 15.62100 -30.10600 -11.97800 1.000 52.58895  ? 75  GLN B NE2 1 
ATOM   1838 N N   . ARG B 1 78  ? 12.45400 -32.35000 -6.75900  1.000 57.90405  ? 76  ARG B N   1 
ATOM   1839 C CA  . ARG B 1 78  ? 11.42000 -33.22400 -6.20900  1.000 66.01368  ? 76  ARG B CA  1 
ATOM   1840 C C   . ARG B 1 78  ? 11.58300 -33.43900 -4.71300  1.000 60.85083  ? 76  ARG B C   1 
ATOM   1841 O O   . ARG B 1 78  ? 11.05200 -34.40800 -4.15600  1.000 71.51208  ? 76  ARG B O   1 
ATOM   1842 C CB  . ARG B 1 78  ? 11.38000 -34.55500 -6.96500  1.000 64.21208  ? 76  ARG B CB  1 
ATOM   1843 C CG  . ARG B 1 78  ? 11.50500 -34.30300 -8.46000  1.000 72.01366  ? 76  ARG B CG  1 
ATOM   1844 C CD  . ARG B 1 78  ? 10.99900 -35.43500 -9.27300  1.000 72.23556  ? 76  ARG B CD  1 
ATOM   1845 N NE  . ARG B 1 78  ? 9.55200  -35.39400 -9.41500  1.000 69.59351  ? 76  ARG B NE  1 
ATOM   1846 C CZ  . ARG B 1 78  ? 8.92100  -35.76300 -10.51900 1.000 70.21078  ? 76  ARG B CZ  1 
ATOM   1847 N NH1 . ARG B 1 78  ? 9.58800  -36.10800 -11.60900 1.000 68.82116  ? 76  ARG B NH1 1 
ATOM   1848 N NH2 . ARG B 1 78  ? 7.59100  -35.80700 -10.52400 1.000 73.26143  ? 76  ARG B NH2 1 
ATOM   1849 N N   . LYS B 1 79  ? 12.34500 -32.55900 -4.06500  1.000 63.68717  ? 77  LYS B N   1 
ATOM   1850 C CA  . LYS B 1 79  ? 12.34800 -32.41300 -2.61600  1.000 64.73375  ? 77  LYS B CA  1 
ATOM   1851 C C   . LYS B 1 79  ? 11.23800 -31.48600 -2.14800  1.000 63.46452  ? 77  LYS B C   1 
ATOM   1852 O O   . LYS B 1 79  ? 10.69800 -31.67000 -1.05600  1.000 66.95930  ? 77  LYS B O   1 
ATOM   1853 C CB  . LYS B 1 79  ? 13.71100 -31.88000 -2.14000  1.000 69.64168  ? 77  LYS B CB  1 
ATOM   1854 C CG  . LYS B 1 79  ? 13.64000 -30.83800 -0.99800  1.000 76.88519  ? 77  LYS B CG  1 
ATOM   1855 C CD  . LYS B 1 79  ? 15.00700 -30.51400 -0.38200  1.000 78.44818  ? 77  LYS B CD  1 
ATOM   1856 C CE  . LYS B 1 79  ? 14.96600 -29.20100 0.41600   1.000 70.68926  ? 77  LYS B CE  1 
ATOM   1857 N NZ  . LYS B 1 79  ? 13.74400 -29.06400 1.26600   1.000 76.00935  ? 77  LYS B NZ  1 
ATOM   1858 N N   . GLY B 1 80  ? 10.86500 -30.51100 -2.96900  1.000 59.85278  ? 78  GLY B N   1 
ATOM   1859 C CA  . GLY B 1 80  ? 9.85400  -29.54500 -2.59300  1.000 58.90532  ? 78  GLY B CA  1 
ATOM   1860 C C   . GLY B 1 80  ? 10.35100 -28.12200 -2.73000  1.000 57.36394  ? 78  GLY B C   1 
ATOM   1861 O O   . GLY B 1 80  ? 9.66100  -27.17100 -2.34400  1.000 57.08345  ? 78  GLY B O   1 
ATOM   1862 N N   . VAL B 1 81  ? 11.53700 -27.96800 -3.32700  1.000 56.55188  ? 79  VAL B N   1 
ATOM   1863 C CA  . VAL B 1 81  ? 12.20000 -26.66900 -3.35400  1.000 55.75718  ? 79  VAL B CA  1 
ATOM   1864 C C   . VAL B 1 81  ? 11.38100 -25.66500 -4.15100  1.000 52.48412  ? 79  VAL B C   1 
ATOM   1865 O O   . VAL B 1 81  ? 11.09700 -24.55300 -3.68100  1.000 52.72268  ? 79  VAL B O   1 
ATOM   1866 C CB  . VAL B 1 81  ? 13.62400 -26.80900 -3.91200  1.000 55.74368  ? 79  VAL B CB  1 
ATOM   1867 C CG1 . VAL B 1 81  ? 14.24900 -25.44100 -4.09300  1.000 54.69913  ? 79  VAL B CG1 1 
ATOM   1868 C CG2 . VAL B 1 81  ? 14.46700 -27.66700 -2.98300  1.000 59.67400  ? 79  VAL B CG2 1 
ATOM   1869 N N   . ALA B 1 82  ? 10.99300 -26.03600 -5.37500  1.000 49.68915  ? 80  ALA B N   1 
ATOM   1870 C CA  . ALA B 1 82  ? 10.26100 -25.09700 -6.21700  1.000 46.74737  ? 80  ALA B CA  1 
ATOM   1871 C C   . ALA B 1 82  ? 8.92000  -24.71700 -5.60900  1.000 47.35580  ? 80  ALA B C   1 
ATOM   1872 O O   . ALA B 1 82  ? 8.52000  -23.54600 -5.66200  1.000 46.59875  ? 80  ALA B O   1 
ATOM   1873 C CB  . ALA B 1 82  ? 10.06100 -25.66900 -7.61800  1.000 44.02246  ? 80  ALA B CB  1 
ATOM   1874 N N   . SER B 1 83  ? 8.18900  -25.69200 -5.07200  1.000 48.93176  ? 81  SER B N   1 
ATOM   1875 C CA  . SER B 1 83  ? 6.93600  -25.38000 -4.39400  1.000 50.09110  ? 81  SER B CA  1 
ATOM   1876 C C   . SER B 1 83  ? 7.14000  -24.29700 -3.33500  1.000 52.16169  ? 81  SER B C   1 
ATOM   1877 O O   . SER B 1 83  ? 6.41900  -23.28800 -3.31200  1.000 51.88247  ? 81  SER B O   1 
ATOM   1878 C CB  . SER B 1 83  ? 6.34900  -26.65700 -3.78900  1.000 52.22017  ? 81  SER B CB  1 
ATOM   1879 O OG  . SER B 1 83  ? 6.04300  -27.59800 -4.81200  1.000 61.05789  ? 81  SER B OG  1 
ATOM   1880 N N   . GLN B 1 84  ? 8.14600  -24.48400 -2.46400  1.000 54.55684  ? 82  GLN B N   1 
ATOM   1881 C CA  . GLN B 1 84  ? 8.47500  -23.48600 -1.44900  1.000 56.85792  ? 82  GLN B CA  1 
ATOM   1882 C C   . GLN B 1 84  ? 8.85100  -22.14400 -2.07000  1.000 55.01446  ? 82  GLN B C   1 
ATOM   1883 O O   . GLN B 1 84  ? 8.45400  -21.09100 -1.56000  1.000 56.18851  ? 82  GLN B O   1 
ATOM   1884 C CB  . GLN B 1 84  ? 9.60800  -24.00400 -0.55000  1.000 59.74241  ? 82  GLN B CB  1 
ATOM   1885 C CG  . GLN B 1 84  ? 9.33000  -25.35400 0.17000   1.000 62.22143  ? 82  GLN B CG  1 
ATOM   1886 C CD  . GLN B 1 84  ? 10.48700 -25.81600 1.09800   1.000 68.68512  ? 82  GLN B CD  1 
ATOM   1887 O OE1 . GLN B 1 84  ? 10.83800 -25.13100 2.06000   1.000 68.05920  ? 82  GLN B OE1 1 
ATOM   1888 N NE2 . GLN B 1 84  ? 11.06900 -26.98200 0.80000   1.000 66.97283  ? 82  GLN B NE2 1 
ATOM   1889 N N   . LEU B 1 85  ? 9.65100  -22.15500 -3.14100  1.000 52.50553  ? 83  LEU B N   1 
ATOM   1890 C CA  . LEU B 1 85  ? 10.04800 -20.90500 -3.78500  1.000 50.85787  ? 83  LEU B CA  1 
ATOM   1891 C C   . LEU B 1 85  ? 8.84200  -20.20100 -4.38900  1.000 49.11719  ? 83  LEU B C   1 
ATOM   1892 O O   . LEU B 1 85  ? 8.68300  -18.98100 -4.26200  1.000 49.57485  ? 83  LEU B O   1 
ATOM   1893 C CB  . LEU B 1 85  ? 11.08100 -21.17200 -4.89000  1.000 48.59901  ? 83  LEU B CB  1 
ATOM   1894 C CG  . LEU B 1 85  ? 12.49200 -21.44100 -4.37000  1.000 53.43288  ? 83  LEU B CG  1 
ATOM   1895 C CD1 . LEU B 1 85  ? 13.30700 -22.13000 -5.44900  1.000 48.93738  ? 83  LEU B CD1 1 
ATOM   1896 C CD2 . LEU B 1 85  ? 13.15100 -20.14200 -3.95000  1.000 51.81726  ? 83  LEU B CD2 1 
ATOM   1897 N N   . LEU B 1 86  ? 7.99200  -20.96300 -5.08000  1.000 47.36641  ? 84  LEU B N   1 
ATOM   1898 C CA  . LEU B 1 86  ? 6.77900  -20.38600 -5.64100  1.000 48.88049  ? 84  LEU B CA  1 
ATOM   1899 C C   . LEU B 1 86  ? 5.91700  -19.75500 -4.56000  1.000 49.34380  ? 84  LEU B C   1 
ATOM   1900 O O   . LEU B 1 86  ? 5.41600  -18.64000 -4.73200  1.000 49.93953  ? 84  LEU B O   1 
ATOM   1901 C CB  . LEU B 1 86  ? 5.99200  -21.45300 -6.38900  1.000 44.43470  ? 84  LEU B CB  1 
ATOM   1902 C CG  . LEU B 1 86  ? 4.64900  -20.99100 -6.95300  1.000 50.99893  ? 84  LEU B CG  1 
ATOM   1903 C CD1 . LEU B 1 86  ? 4.78000  -19.74100 -7.81700  1.000 47.04852  ? 84  LEU B CD1 1 
ATOM   1904 C CD2 . LEU B 1 86  ? 4.05600  -22.13600 -7.73400  1.000 41.97208  ? 84  LEU B CD2 1 
ATOM   1905 N N   . GLN B 1 87  ? 5.73900  -20.44600 -3.43300  1.000 51.54908  ? 85  GLN B N   1 
ATOM   1906 C CA  . GLN B 1 87  ? 4.86900  -19.89100 -2.41000  1.000 59.02781  ? 85  GLN B CA  1 
ATOM   1907 C C   . GLN B 1 87  ? 5.45000  -18.61300 -1.82200  1.000 56.27799  ? 85  GLN B C   1 
ATOM   1908 O O   . GLN B 1 87  ? 4.69900  -17.68200 -1.51900  1.000 60.24207  ? 85  GLN B O   1 
ATOM   1909 C CB  . GLN B 1 87  ? 4.59300  -20.90700 -1.31100  1.000 57.95290  ? 85  GLN B CB  1 
ATOM   1910 C CG  . GLN B 1 87  ? 3.65100  -20.33900 -0.26900  1.000 69.34295  ? 85  GLN B CG  1 
ATOM   1911 C CD  . GLN B 1 87  ? 2.39700  -19.72300 -0.90100  1.000 74.55830  ? 85  GLN B CD  1 
ATOM   1912 O OE1 . GLN B 1 87  ? 2.03800  -18.57000 -0.62700  1.000 61.22368  ? 85  GLN B OE1 1 
ATOM   1913 N NE2 . GLN B 1 87  ? 1.73500  -20.49600 -1.76800  1.000 70.55348  ? 85  GLN B NE2 1 
ATOM   1914 N N   . HIS B 1 88  ? 6.77700  -18.53500 -1.66900  1.000 56.40401  ? 86  HIS B N   1 
ATOM   1915 C CA  . HIS B 1 88  ? 7.37500  -17.28700 -1.20000  1.000 58.13058  ? 86  HIS B CA  1 
ATOM   1916 C C   . HIS B 1 88  ? 7.13900  -16.15800 -2.19300  1.000 62.93317  ? 86  HIS B C   1 
ATOM   1917 O O   . HIS B 1 88  ? 6.89800  -15.01100 -1.79500  1.000 61.07202  ? 86  HIS B O   1 
ATOM   1918 C CB  . HIS B 1 88  ? 8.87300  -17.45700 -0.93600  1.000 61.85017  ? 86  HIS B CB  1 
ATOM   1919 C CG  . HIS B 1 88  ? 9.47900  -16.33400 -0.13700  1.000 68.26409  ? 86  HIS B CG  1 
ATOM   1920 N ND1 . HIS B 1 88  ? 9.31600  -16.21600 1.22500   1.000 74.28099  ? 86  HIS B ND1 1 
ATOM   1921 C CD2 . HIS B 1 88  ? 10.23500 -15.27300 -0.51700  1.000 62.18748  ? 86  HIS B CD2 1 
ATOM   1922 C CE1 . HIS B 1 88  ? 9.95200  -15.13700 1.65200   1.000 72.80223  ? 86  HIS B CE1 1 
ATOM   1923 N NE2 . HIS B 1 88  ? 10.52000 -14.54800 0.61300   1.000 70.56498  ? 86  HIS B NE2 1 
ATOM   1924 N N   . ALA B 1 89  ? 7.20800  -16.46200 -3.49100  1.000 53.03654  ? 87  ALA B N   1 
ATOM   1925 C CA  . ALA B 1 89  ? 6.86900  -15.46500 -4.49900  1.000 57.38085  ? 87  ALA B CA  1 
ATOM   1926 C C   . ALA B 1 89  ? 5.39400  -15.08900 -4.42100  1.000 62.83566  ? 87  ALA B C   1 
ATOM   1927 O O   . ALA B 1 89  ? 5.04700  -13.90200 -4.47300  1.000 63.67542  ? 87  ALA B O   1 
ATOM   1928 C CB  . ALA B 1 89  ? 7.22200  -15.99000 -5.88800  1.000 47.02416  ? 87  ALA B CB  1 
ATOM   1929 N N   . LEU B 1 90  ? 4.51400  -16.08800 -4.27700  1.000 53.48836  ? 88  LEU B N   1 
ATOM   1930 C CA  . LEU B 1 90  ? 3.08300  -15.82400 -4.18700  1.000 53.56274  ? 88  LEU B CA  1 
ATOM   1931 C C   . LEU B 1 90  ? 2.75100  -14.97600 -2.97000  1.000 61.63218  ? 88  LEU B C   1 
ATOM   1932 O O   . LEU B 1 90  ? 1.88200  -14.10000 -3.04500  1.000 70.39575  ? 88  LEU B O   1 
ATOM   1933 C CB  . LEU B 1 90  ? 2.30000  -17.13500 -4.15000  1.000 58.29734  ? 88  LEU B CB  1 
ATOM   1934 C CG  . LEU B 1 90  ? 2.18200  -17.82500 -5.51300  1.000 50.69056  ? 88  LEU B CG  1 
ATOM   1935 C CD1 . LEU B 1 90  ? 1.36600  -19.11100 -5.43100  1.000 55.77966  ? 88  LEU B CD1 1 
ATOM   1936 C CD2 . LEU B 1 90  ? 1.57900  -16.86800 -6.53600  1.000 47.78277  ? 88  LEU B CD2 1 
ATOM   1937 N N   . HIS B 1 91  ? 3.41000  -15.23300 -1.83600  1.000 60.53770  ? 89  HIS B N   1 
ATOM   1938 C CA  . HIS B 1 91  ? 3.16000  -14.43100 -0.64100  1.000 68.34773  ? 89  HIS B CA  1 
ATOM   1939 C C   . HIS B 1 91  ? 3.40500  -12.95700 -0.92800  1.000 75.27956  ? 89  HIS B C   1 
ATOM   1940 O O   . HIS B 1 91  ? 2.50900  -12.12100 -0.77600  1.000 82.14748  ? 89  HIS B O   1 
ATOM   1941 C CB  . HIS B 1 91  ? 4.03700  -14.90300 0.52500   1.000 65.95504  ? 89  HIS B CB  1 
ATOM   1942 C CG  . HIS B 1 91  ? 3.71300  -14.24200 1.83300   1.000 71.04367  ? 89  HIS B CG  1 
ATOM   1943 N ND1 . HIS B 1 91  ? 4.04900  -12.93400 2.11200   1.000 76.87948  ? 89  HIS B ND1 1 
ATOM   1944 C CD2 . HIS B 1 91  ? 3.07600  -14.70800 2.93400   1.000 86.00917  ? 89  HIS B CD2 1 
ATOM   1945 C CE1 . HIS B 1 91  ? 3.63400  -12.62300 3.32700   1.000 85.57854  ? 89  HIS B CE1 1 
ATOM   1946 N NE2 . HIS B 1 91  ? 3.03900  -13.68100 3.84800   1.000 83.60924  ? 89  HIS B NE2 1 
ATOM   1947 N N   . TYR B 1 92  ? 4.62000  -12.62200 -1.35400  1.000 74.31188  ? 90  TYR B N   1 
ATOM   1948 C CA  . TYR B 1 92  ? 4.93200  -11.23700 -1.67600  1.000 79.78617  ? 90  TYR B CA  1 
ATOM   1949 C C   . TYR B 1 92  ? 3.99900  -10.69300 -2.74900  1.000 82.61093  ? 90  TYR B C   1 
ATOM   1950 O O   . TYR B 1 92  ? 3.52100  -9.55900  -2.64600  1.000 89.04451  ? 90  TYR B O   1 
ATOM   1951 C CB  . TYR B 1 92  ? 6.39100  -11.13100 -2.11100  1.000 86.79159  ? 90  TYR B CB  1 
ATOM   1952 C CG  . TYR B 1 92  ? 6.79200  -9.78100  -2.64400  1.000 92.39932  ? 90  TYR B CG  1 
ATOM   1953 C CD1 . TYR B 1 92  ? 6.36400  -8.60800  -2.04000  1.000 101.73320 ? 90  TYR B CD1 1 
ATOM   1954 C CD2 . TYR B 1 92  ? 7.62000  -9.68100  -3.74400  1.000 93.26368  ? 90  TYR B CD2 1 
ATOM   1955 C CE1 . TYR B 1 92  ? 6.74200  -7.37500  -2.53400  1.000 107.07258 ? 90  TYR B CE1 1 
ATOM   1956 C CE2 . TYR B 1 92  ? 8.00900  -8.46000  -4.24200  1.000 98.47063  ? 90  TYR B CE2 1 
ATOM   1957 C CZ  . TYR B 1 92  ? 7.56700  -7.30700  -3.63700  1.000 101.16871 ? 90  TYR B CZ  1 
ATOM   1958 O OH  . TYR B 1 92  ? 7.95300  -6.08200  -4.13800  1.000 103.99465 ? 90  TYR B OH  1 
ATOM   1959 N N   . ALA B 1 93  ? 3.72200  -11.49000 -3.78500  1.000 75.63655  ? 91  ALA B N   1 
ATOM   1960 C CA  . ALA B 1 93  ? 2.82000  -11.04300 -4.84200  1.000 75.40903  ? 91  ALA B CA  1 
ATOM   1961 C C   . ALA B 1 93  ? 1.45500  -10.65900 -4.27700  1.000 83.71079  ? 91  ALA B C   1 
ATOM   1962 O O   . ALA B 1 93  ? 0.96700  -9.54600  -4.50900  1.000 85.15459  ? 91  ALA B O   1 
ATOM   1963 C CB  . ALA B 1 93  ? 2.68600  -12.12800 -5.90800  1.000 64.33889  ? 91  ALA B CB  1 
ATOM   1964 N N   . LYS B 1 94  ? 0.82800  -11.56300 -3.51300  1.000 80.58243  ? 92  LYS B N   1 
ATOM   1965 C CA  . LYS B 1 94  ? -0.44900 -11.23400 -2.88200  1.000 70.98926  ? 92  LYS B CA  1 
ATOM   1966 C C   . LYS B 1 94  ? -0.31800 -10.02200 -1.96700  1.000 80.10478  ? 92  LYS B C   1 
ATOM   1967 O O   . LYS B 1 94  ? -1.27900 -9.26300  -1.80400  1.000 78.78757  ? 92  LYS B O   1 
ATOM   1968 C CB  . LYS B 1 94  ? -0.98600 -12.44100 -2.10600  1.000 67.68992  ? 92  LYS B CB  1 
ATOM   1969 C CG  . LYS B 1 94  ? -2.30700 -12.18200 -1.37500  1.000 74.07198  ? 92  LYS B CG  1 
ATOM   1970 C CD  . LYS B 1 94  ? -3.44900 -13.06800 -1.87200  1.000 76.04283  ? 92  LYS B CD  1 
ATOM   1971 C CE  . LYS B 1 94  ? -3.36200 -14.46900 -1.30000  1.000 71.77815  ? 92  LYS B CE  1 
ATOM   1972 N NZ  . LYS B 1 94  ? -3.46500 -14.45800 0.18600   1.000 79.96089  ? 92  LYS B NZ  1 
ATOM   1973 N N   . THR B 1 95  ? 0.86300  -9.81600  -1.37500  1.000 82.27310  ? 93  THR B N   1 
ATOM   1974 C CA  . THR B 1 95  ? 1.07400  -8.65200  -0.51800  1.000 86.15134  ? 93  THR B CA  1 
ATOM   1975 C C   . THR B 1 95  ? 1.03200  -7.35900  -1.32700  1.000 89.04298  ? 93  THR B C   1 
ATOM   1976 O O   . THR B 1 95  ? 0.52200  -6.33800  -0.85000  1.000 91.91212  ? 93  THR B O   1 
ATOM   1977 C CB  . THR B 1 95  ? 2.40800  -8.78500  0.24000   1.000 86.91799  ? 93  THR B CB  1 
ATOM   1978 O OG1 . THR B 1 95  ? 2.31700  -9.83300  1.21800   1.000 80.30990  ? 93  THR B OG1 1 
ATOM   1979 C CG2 . THR B 1 95  ? 2.77200  -7.48800  0.95500   1.000 79.06017  ? 93  THR B CG2 1 
ATOM   1980 N N   . HIS B 1 96  ? 1.53500  -7.38700  -2.56200  1.000 96.61212  ? 94  HIS B N   1 
ATOM   1981 C CA  . HIS B 1 96  ? 1.64700  -6.16500  -3.35200  1.000 103.65585 ? 94  HIS B CA  1 
ATOM   1982 C C   . HIS B 1 96  ? 0.69500  -6.13900  -4.54300  1.000 105.95368 ? 94  HIS B C   1 
ATOM   1983 O O   . HIS B 1 96  ? 1.13800  -6.04800  -5.69300  1.000 100.35689 ? 94  HIS B O   1 
ATOM   1984 C CB  . HIS B 1 96  ? 3.08500  -5.98200  -3.84100  1.000 104.34846 ? 94  HIS B CB  1 
ATOM   1985 C CG  . HIS B 1 96  ? 4.01900  -5.42800  -2.80900  1.000 111.27245 ? 94  HIS B CG  1 
ATOM   1986 N ND1 . HIS B 1 96  ? 3.90000  -5.70900  -1.46500  1.000 115.87299 ? 94  HIS B ND1 1 
ATOM   1987 C CD2 . HIS B 1 96  ? 5.09100  -4.60700  -2.92600  1.000 118.03448 ? 94  HIS B CD2 1 
ATOM   1988 C CE1 . HIS B 1 96  ? 4.85500  -5.08400  -0.79900  1.000 109.96328 ? 94  HIS B CE1 1 
ATOM   1989 N NE2 . HIS B 1 96  ? 5.59300  -4.41000  -1.66200  1.000 110.76219 ? 94  HIS B NE2 1 
ATOM   1990 N N   . HIS B 1 97  ? -0.61000 -6.22700  -4.27600  1.000 101.22555 ? 95  HIS B N   1 
ATOM   1991 C CA  . HIS B 1 97  ? -1.64400 -5.92000  -5.26600  1.000 99.83957  ? 95  HIS B CA  1 
ATOM   1992 C C   . HIS B 1 97  ? -1.59000 -6.87300  -6.46000  1.000 100.68055 ? 95  HIS B C   1 
ATOM   1993 O O   . HIS B 1 97  ? -1.53500 -6.44900  -7.61600  1.000 109.89538 ? 95  HIS B O   1 
ATOM   1994 C CB  . HIS B 1 97  ? -1.53500 -4.46200  -5.73100  1.000 101.36795 ? 95  HIS B CB  1 
ATOM   1995 C CG  . HIS B 1 97  ? -1.34100 -3.48000  -4.61500  1.000 112.50483 ? 95  HIS B CG  1 
ATOM   1996 N ND1 . HIS B 1 97  ? -2.31800 -3.21100  -3.67800  1.000 118.00464 ? 95  HIS B ND1 1 
ATOM   1997 C CD2 . HIS B 1 97  ? -0.28400 -2.70000  -4.28700  1.000 109.80514 ? 95  HIS B CD2 1 
ATOM   1998 C CE1 . HIS B 1 97  ? -1.86900 -2.31100  -2.82100  1.000 112.74273 ? 95  HIS B CE1 1 
ATOM   1999 N NE2 . HIS B 1 97  ? -0.63800 -1.98400  -3.16800  1.000 110.12948 ? 95  HIS B NE2 1 
ATOM   2000 N N   . ALA B 1 98  ? -1.61700 -8.17600  -6.17700  1.000 91.14627  ? 96  ALA B N   1 
ATOM   2001 C CA  . ALA B 1 98  ? -1.59300 -9.17900  -7.23300  1.000 88.21446  ? 96  ALA B CA  1 
ATOM   2002 C C   . ALA B 1 98  ? -2.51700 -10.33300 -6.87700  1.000 79.41742  ? 96  ALA B C   1 
ATOM   2003 O O   . ALA B 1 98  ? -2.63100 -10.71300 -5.70600  1.000 78.34308  ? 96  ALA B O   1 
ATOM   2004 C CB  . ALA B 1 98  ? -0.17000 -9.70700  -7.48700  1.000 80.80052  ? 96  ALA B CB  1 
ATOM   2005 N N   . THR B 1 99  ? -3.18600 -10.87300 -7.89800  1.000 65.46842  ? 97  THR B N   1 
ATOM   2006 C CA  . THR B 1 99  ? -4.03000 -12.05700 -7.75500  1.000 65.98448  ? 97  THR B CA  1 
ATOM   2007 C C   . THR B 1 99  ? -3.84000 -13.07500 -8.87200  1.000 66.50849  ? 97  THR B C   1 
ATOM   2008 O O   . THR B 1 99  ? -4.40700 -14.17300 -8.78900  1.000 63.06762  ? 97  THR B O   1 
ATOM   2009 C CB  . THR B 1 99  ? -5.51100 -11.66400 -7.69900  1.000 80.67314  ? 97  THR B CB  1 
ATOM   2010 O OG1 . THR B 1 99  ? -6.31100 -12.84300 -7.54200  1.000 86.93016  ? 97  THR B OG1 1 
ATOM   2011 C CG2 . THR B 1 99  ? -5.92900 -10.93000 -8.97600  1.000 72.99185  ? 97  THR B CG2 1 
ATOM   2012 N N   . ARG B 1 100 ? -3.07300 -12.76100 -9.90900  1.000 67.68084  ? 98  ARG B N   1 
ATOM   2013 C CA  . ARG B 1 100 ? -2.83000 -13.68600 -11.00100 1.000 53.60438  ? 98  ARG B CA  1 
ATOM   2014 C C   . ARG B 1 100 ? -1.33800 -13.76700 -11.27600 1.000 52.29248  ? 98  ARG B C   1 
ATOM   2015 O O   . ARG B 1 100 ? -0.64300 -12.75100 -11.28600 1.000 48.64710  ? 98  ARG B O   1 
ATOM   2016 C CB  . ARG B 1 100 ? -3.56800 -13.25200 -12.27900 1.000 61.64707  ? 98  ARG B CB  1 
ATOM   2017 C CG  . ARG B 1 100 ? -5.00700 -12.75400 -12.05700 1.000 73.76548  ? 98  ARG B CG  1 
ATOM   2018 C CD  . ARG B 1 100 ? -6.03500 -13.88500 -11.94300 1.000 65.03396  ? 98  ARG B CD  1 
ATOM   2019 N NE  . ARG B 1 100 ? -6.31300 -14.56200 -13.21000 1.000 77.03896  ? 98  ARG B NE  1 
ATOM   2020 C CZ  . ARG B 1 100 ? -6.97900 -14.02300 -14.22500 1.000 78.91625  ? 98  ARG B CZ  1 
ATOM   2021 N NH1 . ARG B 1 100 ? -7.36300 -12.75500 -14.20500 1.000 80.02790  ? 98  ARG B NH1 1 
ATOM   2022 N NH2 . ARG B 1 100 ? -7.27600 -14.77800 -15.28000 1.000 73.86519  ? 98  ARG B NH2 1 
ATOM   2023 N N   . LEU B 1 101 ? -0.84600 -14.97600 -11.49900 1.000 42.34421  ? 99  LEU B N   1 
ATOM   2024 C CA  . LEU B 1 101 ? 0.53900  -15.18600 -11.89000 1.000 40.74334  ? 99  LEU B CA  1 
ATOM   2025 C C   . LEU B 1 101 ? 0.52500  -15.77400 -13.29400 1.000 42.87817  ? 99  LEU B C   1 
ATOM   2026 O O   . LEU B 1 101 ? -0.01300 -16.86200 -13.50800 1.000 41.30373  ? 99  LEU B O   1 
ATOM   2027 C CB  . LEU B 1 101 ? 1.29100  -16.10600 -10.91100 1.000 41.04923  ? 99  LEU B CB  1 
ATOM   2028 C CG  . LEU B 1 101 ? 2.78900  -16.25300 -11.20400 1.000 47.02843  ? 99  LEU B CG  1 
ATOM   2029 C CD1 . LEU B 1 101 ? 3.48900  -14.90900 -11.14600 1.000 40.32549  ? 99  LEU B CD1 1 
ATOM   2030 C CD2 . LEU B 1 101 ? 3.47500  -17.27100 -10.28500 1.000 43.01548  ? 99  LEU B CD2 1 
ATOM   2031 N N   . LEU B 1 102 ? 1.11600  -15.05300 -14.24000 1.000 38.91387  ? 100 LEU B N   1 
ATOM   2032 C CA  . LEU B 1 102 ? 1.18700  -15.47600 -15.63100 1.000 34.27992  ? 100 LEU B CA  1 
ATOM   2033 C C   . LEU B 1 102 ? 2.47900  -16.24300 -15.86600 1.000 33.41882  ? 100 LEU B C   1 
ATOM   2034 O O   . LEU B 1 102 ? 3.52800  -15.87100 -15.34700 1.000 38.85867  ? 100 LEU B O   1 
ATOM   2035 C CB  . LEU B 1 102 ? 1.13400  -14.25100 -16.54400 1.000 35.24522  ? 100 LEU B CB  1 
ATOM   2036 C CG  . LEU B 1 102 ? 1.23000  -14.41300 -18.06100 1.000 42.98295  ? 100 LEU B CG  1 
ATOM   2037 C CD1 . LEU B 1 102 ? -0.07500 -14.96600 -18.59500 1.000 40.01284  ? 100 LEU B CD1 1 
ATOM   2038 C CD2 . LEU B 1 102 ? 1.54100  -13.08600 -18.73100 1.000 43.97312  ? 100 LEU B CD2 1 
ATOM   2039 N N   . LEU B 1 103 ? 2.41200  -17.31700 -16.64100 1.000 32.48525  ? 101 LEU B N   1 
ATOM   2040 C CA  . LEU B 1 103 ? 3.62100  -18.00600 -17.07700 1.000 32.07355  ? 101 LEU B CA  1 
ATOM   2041 C C   . LEU B 1 103 ? 3.56700  -18.28400 -18.56700 1.000 29.30257  ? 101 LEU B C   1 
ATOM   2042 O O   . LEU B 1 103 ? 2.57300  -18.81200 -19.05900 1.000 26.46505  ? 101 LEU B O   1 
ATOM   2043 C CB  . LEU B 1 103 ? 3.83200  -19.31000 -16.32700 1.000 28.24256  ? 101 LEU B CB  1 
ATOM   2044 C CG  . LEU B 1 103 ? 4.90400  -20.22900 -16.89800 1.000 32.47939  ? 101 LEU B CG  1 
ATOM   2045 C CD1 . LEU B 1 103 ? 6.27500  -19.60900 -16.68200 1.000 27.02902  ? 101 LEU B CD1 1 
ATOM   2046 C CD2 . LEU B 1 103 ? 4.79800  -21.59800 -16.23200 1.000 27.51191  ? 101 LEU B CD2 1 
ATOM   2047 N N   . GLU B 1 104 ? 4.64100  -17.94100 -19.26800 1.000 25.87054  ? 102 GLU B N   1 
ATOM   2048 C CA  . GLU B 1 104 ? 4.86400  -18.32200 -20.65500 1.000 26.13610  ? 102 GLU B CA  1 
ATOM   2049 C C   . GLU B 1 104 ? 6.06000  -19.26600 -20.71000 1.000 28.91454  ? 102 GLU B C   1 
ATOM   2050 O O   . GLU B 1 104 ? 7.11800  -18.94700 -20.16700 1.000 25.07141  ? 102 GLU B O   1 
ATOM   2051 C CB  . GLU B 1 104 ? 5.09100  -17.07800 -21.52200 1.000 27.86458  ? 102 GLU B CB  1 
ATOM   2052 C CG  . GLU B 1 104 ? 3.89300  -16.12000 -21.48000 1.000 37.11572  ? 102 GLU B CG  1 
ATOM   2053 C CD  . GLU B 1 104 ? 3.84700  -15.12000 -22.61700 1.000 48.66865  ? 102 GLU B CD  1 
ATOM   2054 O OE1 . GLU B 1 104 ? 4.78500  -15.12500 -23.43500 1.000 50.04432  ? 102 GLU B OE1 1 
ATOM   2055 O OE2 . GLU B 1 104 ? 2.86100  -14.33600 -22.68600 1.000 44.20124  ? 102 GLU B OE2 1 
ATOM   2056 N N   . VAL B 1 105 ? 5.89900  -20.42200 -21.35300 1.000 21.15095  ? 103 VAL B N   1 
ATOM   2057 C CA  . VAL B 1 105 ? 6.92100  -21.46500 -21.30500 1.000 23.30500  ? 103 VAL B CA  1 
ATOM   2058 C C   . VAL B 1 105 ? 6.93400  -22.27200 -22.59900 1.000 24.93136  ? 103 VAL B C   1 
ATOM   2059 O O   . VAL B 1 105 ? 5.90800  -22.42500 -23.26400 1.000 23.87060  ? 103 VAL B O   1 
ATOM   2060 C CB  . VAL B 1 105 ? 6.68200  -22.35800 -20.06700 1.000 33.03555  ? 103 VAL B CB  1 
ATOM   2061 C CG1 . VAL B 1 105 ? 5.37200  -23.12500 -20.20900 1.000 35.21394  ? 103 VAL B CG1 1 
ATOM   2062 C CG2 . VAL B 1 105 ? 7.83600  -23.28300 -19.85900 1.000 37.32877  ? 103 VAL B CG2 1 
ATOM   2063 N N   . ARG B 1 106 ? 8.10900  -22.81100 -22.95100 1.000 21.88731  ? 104 ARG B N   1 
ATOM   2064 C CA  . ARG B 1 106 ? 8.21900  -23.62900 -24.15100 1.000 23.53420  ? 104 ARG B CA  1 
ATOM   2065 C C   . ARG B 1 106 ? 7.28500  -24.81500 -24.02200 1.000 23.89703  ? 104 ARG B C   1 
ATOM   2066 O O   . ARG B 1 106 ? 7.12200  -25.38400 -22.93900 1.000 27.23420  ? 104 ARG B O   1 
ATOM   2067 C CB  . ARG B 1 106 ? 9.66000  -24.11600 -24.35900 1.000 26.06131  ? 104 ARG B CB  1 
ATOM   2068 C CG  . ARG B 1 106 ? 10.60200 -23.01500 -24.76400 1.000 20.90082  ? 104 ARG B CG  1 
ATOM   2069 C CD  . ARG B 1 106 ? 12.02800 -23.52400 -24.81600 1.000 23.50012  ? 104 ARG B CD  1 
ATOM   2070 N NE  . ARG B 1 106 ? 12.91100 -22.42500 -25.18200 1.000 26.56171  ? 104 ARG B NE  1 
ATOM   2071 C CZ  . ARG B 1 106 ? 13.34200 -22.18400 -26.41200 1.000 30.83263  ? 104 ARG B CZ  1 
ATOM   2072 N NH1 . ARG B 1 106 ? 13.09200 -23.02200 -27.41000 1.000 31.61970  ? 104 ARG B NH1 1 
ATOM   2073 N NH2 . ARG B 1 106 ? 14.05100 -21.08300 -26.64700 1.000 26.91996  ? 104 ARG B NH2 1 
ATOM   2074 N N   . LYS B 1 107 ? 6.66200  -25.18100 -25.14000 1.000 29.22936  ? 105 LYS B N   1 
ATOM   2075 C CA  . LYS B 1 107 ? 5.78500  -26.32500 -25.14400 1.000 32.37903  ? 105 LYS B CA  1 
ATOM   2076 C C   . LYS B 1 107 ? 6.51500  -27.58200 -24.70800 1.000 32.51953  ? 105 LYS B C   1 
ATOM   2077 O O   . LYS B 1 107 ? 5.89300  -28.48600 -24.14600 1.000 38.81059  ? 105 LYS B O   1 
ATOM   2078 C CB  . LYS B 1 107 ? 5.20400  -26.51100 -26.55000 1.000 33.84794  ? 105 LYS B CB  1 
ATOM   2079 C CG  . LYS B 1 107 ? 4.32400  -27.70600 -26.70500 1.000 36.55966  ? 105 LYS B CG  1 
ATOM   2080 C CD  . LYS B 1 107 ? 3.24200  -27.42300 -27.72800 1.000 42.86835  ? 105 LYS B CD  1 
ATOM   2081 C CE  . LYS B 1 107 ? 3.80100  -27.16600 -29.08000 1.000 51.02231  ? 105 LYS B CE  1 
ATOM   2082 N NZ  . LYS B 1 107 ? 4.57300  -28.31300 -29.61700 1.000 64.72960  ? 105 LYS B NZ  1 
ATOM   2083 N N   . SER B 1 108 ? 7.82500  -27.66700 -24.98200 1.000 32.67140  ? 106 SER B N   1 
ATOM   2084 C CA  . SER B 1 108 ? 8.56400  -28.88100 -24.66200 1.000 36.62079  ? 106 SER B CA  1 
ATOM   2085 C C   . SER B 1 108 ? 9.04600  -28.92800 -23.21300 1.000 33.03707  ? 106 SER B C   1 
ATOM   2086 O O   . SER B 1 108 ? 9.64300  -29.93900 -22.82000 1.000 41.23997  ? 106 SER B O   1 
ATOM   2087 C CB  . SER B 1 108 ? 9.77200  -29.05200 -25.59300 1.000 34.38167  ? 106 SER B CB  1 
ATOM   2088 O OG  . SER B 1 108 ? 10.71900 -28.02600 -25.44600 1.000 38.33007  ? 106 SER B OG  1 
ATOM   2089 N N   . ASN B 1 109 ? 8.80200  -27.88900 -22.41500 1.000 33.16572  ? 107 ASN B N   1 
ATOM   2090 C CA  . ASN B 1 109 ? 9.31700  -27.88500 -21.03800 1.000 30.90506  ? 107 ASN B CA  1 
ATOM   2091 C C   . ASN B 1 109 ? 8.34900  -28.62100 -20.11800 1.000 35.87239  ? 107 ASN B C   1 
ATOM   2092 O O   . ASN B 1 109 ? 7.59100  -28.03200 -19.34100 1.000 31.49026  ? 107 ASN B O   1 
ATOM   2093 C CB  . ASN B 1 109 ? 9.57000  -26.48000 -20.55600 1.000 26.74725  ? 107 ASN B CB  1 
ATOM   2094 C CG  . ASN B 1 109 ? 10.44000 -26.45100 -19.32100 1.000 34.13568  ? 107 ASN B CG  1 
ATOM   2095 O OD1 . ASN B 1 109 ? 10.68600 -27.49000 -18.65800 1.000 34.23552  ? 107 ASN B OD1 1 
ATOM   2096 N ND2 . ASN B 1 109 ? 10.90100 -25.26900 -18.98700 1.000 31.12585  ? 107 ASN B ND2 1 
ATOM   2097 N N   . ARG B 1 110 ? 8.43300  -29.94400 -20.18200 1.000 36.40094  ? 108 ARG B N   1 
ATOM   2098 C CA  . ARG B 1 110 ? 7.52700  -30.80800 -19.43700 1.000 37.62206  ? 108 ARG B CA  1 
ATOM   2099 C C   . ARG B 1 110 ? 7.58700  -30.54000 -17.94100 1.000 33.94392  ? 108 ARG B C   1 
ATOM   2100 O O   . ARG B 1 110 ? 6.55000  -30.54100 -17.27100 1.000 43.44142  ? 108 ARG B O   1 
ATOM   2101 C CB  . ARG B 1 110 ? 7.84700  -32.27300 -19.73700 1.000 38.84395  ? 108 ARG B CB  1 
ATOM   2102 C CG  . ARG B 1 110 ? 6.80500  -33.30600 -19.26900 1.000 49.94670  ? 108 ARG B CG  1 
ATOM   2103 C CD  . ARG B 1 110 ? 5.46100  -33.28100 -20.05100 1.000 60.81473  ? 108 ARG B CD  1 
ATOM   2104 N NE  . ARG B 1 110 ? 4.52600  -34.31200 -19.58500 1.000 60.97643  ? 108 ARG B NE  1 
ATOM   2105 C CZ  . ARG B 1 110 ? 3.20900  -34.30000 -19.77800 1.000 71.43057  ? 108 ARG B CZ  1 
ATOM   2106 N NH1 . ARG B 1 110 ? 2.59900  -33.27300 -20.35600 1.000 57.61172  ? 108 ARG B NH1 1 
ATOM   2107 N NH2 . ARG B 1 110 ? 2.48400  -35.34700 -19.37700 1.000 70.18814  ? 108 ARG B NH2 1 
ATOM   2108 N N   . SER B 1 111 ? 8.77900  -30.35200 -17.37700 1.000 37.04837  ? 109 SER B N   1 
ATOM   2109 C CA  . SER B 1 111 ? 8.81500  -30.33600 -15.91500 1.000 32.62260  ? 109 SER B CA  1 
ATOM   2110 C C   . SER B 1 111 ? 8.23600  -29.03300 -15.39400 1.000 36.57123  ? 109 SER B C   1 
ATOM   2111 O O   . SER B 1 111 ? 7.49400  -29.03600 -14.39700 1.000 33.45106  ? 109 SER B O   1 
ATOM   2112 C CB  . SER B 1 111 ? 10.24000 -30.57700 -15.39000 1.000 33.76285  ? 109 SER B CB  1 
ATOM   2113 O OG  . SER B 1 111 ? 11.09200 -29.49400 -15.68600 1.000 38.08827  ? 109 SER B OG  1 
ATOM   2114 N N   . ALA B 1 112 ? 8.52300  -27.92200 -16.08600 1.000 35.67029  ? 110 ALA B N   1 
ATOM   2115 C CA  . ALA B 1 112 ? 7.93500  -26.63400 -15.73300 1.000 28.85497  ? 110 ALA B CA  1 
ATOM   2116 C C   . ALA B 1 112 ? 6.41900  -26.69300 -15.81800 1.000 36.81878  ? 110 ALA B C   1 
ATOM   2117 O O   . ALA B 1 112 ? 5.71500  -26.20200 -14.92300 1.000 31.31283  ? 110 ALA B O   1 
ATOM   2118 C CB  . ALA B 1 112 ? 8.47000  -25.53900 -16.65500 1.000 28.50815  ? 110 ALA B CB  1 
ATOM   2119 N N   . ILE B 1 113 ? 5.90200  -27.28500 -16.90000 1.000 30.93913  ? 111 ILE B N   1 
ATOM   2120 C CA  . ILE B 1 113 ? 4.45900  -27.33100 -17.12100 1.000 26.56913  ? 111 ILE B CA  1 
ATOM   2121 C C   . ILE B 1 113 ? 3.78400  -28.19500 -16.07500 1.000 31.49202  ? 111 ILE B C   1 
ATOM   2122 O O   . ILE B 1 113 ? 2.72800  -27.83500 -15.53600 1.000 37.37592  ? 111 ILE B O   1 
ATOM   2123 C CB  . ILE B 1 113 ? 4.15600  -27.83200 -18.53900 1.000 34.89590  ? 111 ILE B CB  1 
ATOM   2124 C CG1 . ILE B 1 113 ? 4.50200  -26.74200 -19.55300 1.000 26.49196  ? 111 ILE B CG1 1 
ATOM   2125 C CG2 . ILE B 1 113 ? 2.71700  -28.29600 -18.63600 1.000 37.93866  ? 111 ILE B CG2 1 
ATOM   2126 C CD1 . ILE B 1 113 ? 4.81300  -27.33800 -20.94900 1.000 31.32158  ? 111 ILE B CD1 1 
ATOM   2127 N N   . GLU B 1 114 ? 4.34100  -29.38100 -15.80800 1.000 38.13480  ? 112 GLU B N   1 
ATOM   2128 C CA  . GLU B 1 114 ? 3.70500  -30.26500 -14.84200 1.000 34.49154  ? 112 GLU B CA  1 
ATOM   2129 C C   . GLU B 1 114 ? 3.76900  -29.66200 -13.44600 1.000 38.37745  ? 112 GLU B C   1 
ATOM   2130 O O   . GLU B 1 114 ? 2.80800  -29.76100 -12.67100 1.000 37.35392  ? 112 GLU B O   1 
ATOM   2131 C CB  . GLU B 1 114 ? 4.38000  -31.63400 -14.85400 1.000 45.77559  ? 112 GLU B CB  1 
ATOM   2132 C CG  . GLU B 1 114 ? 4.28900  -32.37200 -16.16700 1.000 48.78737  ? 112 GLU B CG  1 
ATOM   2133 C CD  . GLU B 1 114 ? 2.92500  -32.22600 -16.80700 1.000 55.53656  ? 112 GLU B CD  1 
ATOM   2134 O OE1 . GLU B 1 114 ? 1.94600  -32.75100 -16.23300 1.000 47.67353  ? 112 GLU B OE1 1 
ATOM   2135 O OE2 . GLU B 1 114 ? 2.84200  -31.57100 -17.87700 1.000 65.00151  ? 112 GLU B OE2 1 
ATOM   2136 N N   . PHE B 1 115 ? 4.90400  -29.04600 -13.10800 1.000 39.24930  ? 113 PHE B N   1 
ATOM   2137 C CA  . PHE B 1 115 ? 5.02200  -28.30600 -11.85700 1.000 39.81818  ? 113 PHE B CA  1 
ATOM   2138 C C   . PHE B 1 115 ? 3.96100  -27.21400 -11.74100 1.000 42.31298  ? 113 PHE B C   1 
ATOM   2139 O O   . PHE B 1 115 ? 3.31500  -27.08000 -10.69900 1.000 38.31308  ? 113 PHE B O   1 
ATOM   2140 C CB  . PHE B 1 115 ? 6.41600  -27.69700 -11.73000 1.000 32.42598  ? 113 PHE B CB  1 
ATOM   2141 C CG  . PHE B 1 115 ? 6.51400  -26.69000 -10.61800 1.000 41.74972  ? 113 PHE B CG  1 
ATOM   2142 C CD1 . PHE B 1 115 ? 6.56000  -27.11500 -9.29400  1.000 38.61004  ? 113 PHE B CD1 1 
ATOM   2143 C CD2 . PHE B 1 115 ? 6.51900  -25.32800 -10.88100 1.000 33.07307  ? 113 PHE B CD2 1 
ATOM   2144 C CE1 . PHE B 1 115 ? 6.63300  -26.20400 -8.25300  1.000 46.46195  ? 113 PHE B CE1 1 
ATOM   2145 C CE2 . PHE B 1 115 ? 6.59300  -24.40800 -9.85200  1.000 37.77474  ? 113 PHE B CE2 1 
ATOM   2146 C CZ  . PHE B 1 115 ? 6.64100  -24.85200 -8.52800  1.000 34.39629  ? 113 PHE B CZ  1 
ATOM   2147 N N   . TYR B 1 116 ? 3.79500  -26.39000 -12.78400 1.000 34.72538  ? 114 TYR B N   1 
ATOM   2148 C CA  . TYR B 1 116 ? 2.88300  -25.24900 -12.66500 1.000 32.44440  ? 114 TYR B CA  1 
ATOM   2149 C C   . TYR B 1 116 ? 1.42900  -25.69900 -12.63000 1.000 32.96305  ? 114 TYR B C   1 
ATOM   2150 O O   . TYR B 1 116 ? 0.62200  -25.12400 -11.89800 1.000 34.49726  ? 114 TYR B O   1 
ATOM   2151 C CB  . TYR B 1 116 ? 3.08400  -24.26200 -13.81900 1.000 34.74641  ? 114 TYR B CB  1 
ATOM   2152 C CG  . TYR B 1 116 ? 2.72200  -22.80800 -13.50100 1.000 33.01664  ? 114 TYR B CG  1 
ATOM   2153 C CD1 . TYR B 1 116 ? 3.47600  -22.06200 -12.59100 1.000 40.32451  ? 114 TYR B CD1 1 
ATOM   2154 C CD2 . TYR B 1 116 ? 1.63600  -22.18200 -14.12900 1.000 30.55266  ? 114 TYR B CD2 1 
ATOM   2155 C CE1 . TYR B 1 116 ? 3.17400  -20.73900 -12.32200 1.000 31.43934  ? 114 TYR B CE1 1 
ATOM   2156 C CE2 . TYR B 1 116 ? 1.32800  -20.85800 -13.86700 1.000 26.05029  ? 114 TYR B CE2 1 
ATOM   2157 C CZ  . TYR B 1 116 ? 2.10300  -20.15700 -12.96000 1.000 36.44154  ? 114 TYR B CZ  1 
ATOM   2158 O OH  . TYR B 1 116 ? 1.82000  -18.85600 -12.69400 1.000 30.55796  ? 114 TYR B OH  1 
ATOM   2159 N N   . LYS B 1 117 ? 1.05300  -26.70900 -13.42100 1.000 29.40529  ? 115 LYS B N   1 
ATOM   2160 C CA  . LYS B 1 117 ? -0.32900 -27.18600 -13.32300 1.000 30.93545  ? 115 LYS B CA  1 
ATOM   2161 C C   . LYS B 1 117 ? -0.59800 -27.81200 -11.95600 1.000 40.23672  ? 115 LYS B C   1 
ATOM   2162 O O   . LYS B 1 117 ? -1.68500 -27.64400 -11.38600 1.000 38.08280  ? 115 LYS B O   1 
ATOM   2163 C CB  . LYS B 1 117 ? -0.62200 -28.16700 -14.45300 1.000 39.49059  ? 115 LYS B CB  1 
ATOM   2164 C CG  . LYS B 1 117 ? -0.64900 -27.49200 -15.82100 1.000 32.69079  ? 115 LYS B CG  1 
ATOM   2165 C CD  . LYS B 1 117 ? -0.95200 -28.46600 -16.95200 1.000 48.58272  ? 115 LYS B CD  1 
ATOM   2166 C CE  . LYS B 1 117 ? -0.23800 -29.80200 -16.77300 1.000 46.86382  ? 115 LYS B CE  1 
ATOM   2167 N NZ  . LYS B 1 117 ? -0.14600 -30.58500 -18.05700 1.000 57.94522  ? 115 LYS B NZ  1 
ATOM   2168 N N   . LYS B 1 118 ? 0.38200  -28.52500 -11.41500 1.000 32.28583  ? 116 LYS B N   1 
ATOM   2169 C CA  . LYS B 1 118 ? 0.23700  -29.10200 -10.08700 1.000 43.84805  ? 116 LYS B CA  1 
ATOM   2170 C C   . LYS B 1 118 ? -0.01600 -28.01300 -9.05200  1.000 51.79491  ? 116 LYS B C   1 
ATOM   2171 O O   . LYS B 1 118 ? -0.82800 -28.19100 -8.13600  1.000 45.28187  ? 116 LYS B O   1 
ATOM   2172 C CB  . LYS B 1 118 ? 1.49100  -29.91200 -9.76300  1.000 48.43790  ? 116 LYS B CB  1 
ATOM   2173 C CG  . LYS B 1 118 ? 1.44600  -30.79400 -8.54200  1.000 57.04928  ? 116 LYS B CG  1 
ATOM   2174 C CD  . LYS B 1 118 ? 2.86500  -30.94800 -8.04000  1.000 60.51395  ? 116 LYS B CD  1 
ATOM   2175 C CE  . LYS B 1 118 ? 3.39400  -29.54600 -7.59600  1.000 64.55956  ? 116 LYS B CE  1 
ATOM   2176 N NZ  . LYS B 1 118 ? 2.88400  -29.06600 -6.26300  1.000 64.13993  ? 116 LYS B NZ  1 
ATOM   2177 N N   . ALA B 1 119 ? 0.64700  -26.86400 -9.20100  1.000 39.68562  ? 117 ALA B N   1 
ATOM   2178 C CA  . ALA B 1 119 ? 0.42100  -25.73900 -8.29800  1.000 41.13853  ? 117 ALA B CA  1 
ATOM   2179 C C   . ALA B 1 119 ? -0.92200 -25.04700 -8.51000  1.000 42.32051  ? 117 ALA B C   1 
ATOM   2180 O O   . ALA B 1 119 ? -1.27000 -24.16000 -7.72800  1.000 45.54675  ? 117 ALA B O   1 
ATOM   2181 C CB  . ALA B 1 119 ? 1.54700  -24.71800 -8.44300  1.000 39.94913  ? 117 ALA B CB  1 
ATOM   2182 N N   . GLY B 1 120 ? -1.68600 -25.40700 -9.52700  1.000 40.49801  ? 118 GLY B N   1 
ATOM   2183 C CA  . GLY B 1 120 ? -2.98700 -24.79400 -9.76600  1.000 41.39056  ? 118 GLY B CA  1 
ATOM   2184 C C   . GLY B 1 120 ? -3.10000 -24.00900 -11.05300 1.000 39.32931  ? 118 GLY B C   1 
ATOM   2185 O O   . GLY B 1 120 ? -4.22100 -23.65600 -11.43600 1.000 42.73551  ? 118 GLY B O   1 
ATOM   2186 N N   . GLY B 1 121 ? -1.98900 -23.70900 -11.72900 1.000 38.59376  ? 119 GLY B N   1 
ATOM   2187 C CA  . GLY B 1 121 ? -2.06800 -22.98800 -12.99200 1.000 37.81366  ? 119 GLY B CA  1 
ATOM   2188 C C   . GLY B 1 121 ? -2.88200 -23.71900 -14.04700 1.000 41.60623  ? 119 GLY B C   1 
ATOM   2189 O O   . GLY B 1 121 ? -2.88900 -24.95400 -14.12400 1.000 37.07225  ? 119 GLY B O   1 
ATOM   2190 N N   . VAL B 1 122 ? -3.56000 -22.93100 -14.89500 1.000 36.05789  ? 120 VAL B N   1 
ATOM   2191 C CA  . VAL B 1 122 ? -4.41300 -23.42700 -15.97700 1.000 34.40070  ? 120 VAL B CA  1 
ATOM   2192 C C   . VAL B 1 122 ? -3.95400 -22.81200 -17.30800 1.000 36.87576  ? 120 VAL B C   1 
ATOM   2193 O O   . VAL B 1 122 ? -3.61100 -21.62300 -17.38500 1.000 35.00753  ? 120 VAL B O   1 
ATOM   2194 C CB  . VAL B 1 122 ? -5.90500 -23.13200 -15.70700 1.000 48.84097  ? 120 VAL B CB  1 
ATOM   2195 C CG1 . VAL B 1 122 ? -6.15000 -21.63400 -15.47300 1.000 54.44523  ? 120 VAL B CG1 1 
ATOM   2196 C CG2 . VAL B 1 122 ? -6.76100 -23.65500 -16.83700 1.000 43.84508  ? 120 VAL B CG2 1 
ATOM   2197 N N   . GLU B 1 123 ? -3.91900 -23.62700 -18.35500 1.000 33.92576  ? 121 GLU B N   1 
ATOM   2198 C CA  . GLU B 1 123 ? -3.48300 -23.10800 -19.65700 1.000 29.59585  ? 121 GLU B CA  1 
ATOM   2199 C C   . GLU B 1 123 ? -4.55900 -22.18400 -20.21400 1.000 31.03309  ? 121 GLU B C   1 
ATOM   2200 O O   . GLU B 1 123 ? -5.76000 -22.52900 -20.23100 1.000 34.10957  ? 121 GLU B O   1 
ATOM   2201 C CB  . GLU B 1 123 ? -3.18700 -24.25000 -20.62500 1.000 34.42341  ? 121 GLU B CB  1 
ATOM   2202 C CG  . GLU B 1 123 ? -2.68800 -23.75500 -22.00600 1.000 32.49491  ? 121 GLU B CG  1 
ATOM   2203 C CD  . GLU B 1 123 ? -2.52200 -24.87700 -23.04000 1.000 45.00072  ? 121 GLU B CD  1 
ATOM   2204 O OE1 . GLU B 1 123 ? -2.02900 -25.98200 -22.69300 1.000 43.78848  ? 121 GLU B OE1 1 
ATOM   2205 O OE2 . GLU B 1 123 ? -2.85700 -24.62800 -24.21900 1.000 39.81684  ? 121 GLU B OE2 1 
ATOM   2206 N N   . ILE B 1 124 ? -4.16000 -20.96400 -20.58800 1.000 30.89120  ? 122 ILE B N   1 
ATOM   2207 C CA  . ILE B 1 124 ? -5.09100 -20.00600 -21.17900 1.000 32.39730  ? 122 ILE B CA  1 
ATOM   2208 C C   . ILE B 1 124 ? -4.83100 -19.78100 -22.66200 1.000 31.32876  ? 122 ILE B C   1 
ATOM   2209 O O   . ILE B 1 124 ? -5.72500 -19.26200 -23.35600 1.000 33.01255  ? 122 ILE B O   1 
ATOM   2210 C CB  . ILE B 1 124 ? -5.09300 -18.65600 -20.43400 1.000 33.94942  ? 122 ILE B CB  1 
ATOM   2211 C CG1 . ILE B 1 124 ? -3.70400 -18.03000 -20.37800 1.000 33.69806  ? 122 ILE B CG1 1 
ATOM   2212 C CG2 . ILE B 1 124 ? -5.62200 -18.84100 -18.98600 1.000 35.78636  ? 122 ILE B CG2 1 
ATOM   2213 C CD1 . ILE B 1 124 ? -3.73100 -16.62200 -19.81000 1.000 34.29655  ? 122 ILE B CD1 1 
ATOM   2214 N N   . GLY B 1 125 ? -3.67000 -20.15300 -23.17600 1.000 28.97515  ? 123 GLY B N   1 
ATOM   2215 C CA  . GLY B 1 125 ? -3.49900 -19.97600 -24.61100 1.000 28.32214  ? 123 GLY B CA  1 
ATOM   2216 C C   . GLY B 1 125 ? -2.14800 -20.46800 -25.07900 1.000 25.94368  ? 123 GLY B C   1 
ATOM   2217 O O   . GLY B 1 125 ? -1.32200 -20.95700 -24.30600 1.000 28.45968  ? 123 GLY B O   1 
ATOM   2218 N N   . VAL B 1 126 ? -1.93600 -20.32000 -26.38100 1.000 26.42176  ? 124 VAL B N   1 
ATOM   2219 C CA  . VAL B 1 126 ? -0.70000 -20.73200 -27.03300 1.000 23.64531  ? 124 VAL B CA  1 
ATOM   2220 C C   . VAL B 1 126 ? -0.28700 -19.60100 -27.95700 1.000 23.77026  ? 124 VAL B C   1 
ATOM   2221 O O   . VAL B 1 126 ? -1.13000 -19.03800 -28.66300 1.000 25.55881  ? 124 VAL B O   1 
ATOM   2222 C CB  . VAL B 1 126 ? -0.89200 -22.01900 -27.86000 1.000 27.34690  ? 124 VAL B CB  1 
ATOM   2223 C CG1 . VAL B 1 126 ? 0.36600  -22.34500 -28.64300 1.000 22.10711  ? 124 VAL B CG1 1 
ATOM   2224 C CG2 . VAL B 1 126 ? -1.27700 -23.18400 -26.96200 1.000 33.15508  ? 124 VAL B CG2 1 
ATOM   2225 N N   . ARG B 1 127 ? 0.99800  -19.26700 -27.94500 1.000 22.60702  ? 125 ARG B N   1 
ATOM   2226 C CA  . ARG B 1 127 ? 1.60100  -18.41500 -28.98200 1.000 24.32895  ? 125 ARG B CA  1 
ATOM   2227 C C   . ARG B 1 127 ? 2.42200  -19.30800 -29.90300 1.000 23.61949  ? 125 ARG B C   1 
ATOM   2228 O O   . ARG B 1 127 ? 3.45000  -19.86100 -29.48100 1.000 24.41588  ? 125 ARG B O   1 
ATOM   2229 C CB  . ARG B 1 127 ? 2.49000  -17.34000 -28.34700 1.000 28.99082  ? 125 ARG B CB  1 
ATOM   2230 C CG  . ARG B 1 127 ? 1.80300  -16.56000 -27.27200 1.000 26.28272  ? 125 ARG B CG  1 
ATOM   2231 C CD  . ARG B 1 127 ? 2.67500  -15.46400 -26.71800 1.000 36.27152  ? 125 ARG B CD  1 
ATOM   2232 N NE  . ARG B 1 127 ? 2.07700  -14.85300 -25.53700 1.000 45.19054  ? 125 ARG B NE  1 
ATOM   2233 C CZ  . ARG B 1 127 ? 1.24800  -13.81800 -25.55600 1.000 50.84251  ? 125 ARG B CZ  1 
ATOM   2234 N NH1 . ARG B 1 127 ? 0.91400  -13.21500 -26.68900 1.000 54.82813  ? 125 ARG B NH1 1 
ATOM   2235 N NH2 . ARG B 1 127 ? 0.73700  -13.37600 -24.40800 1.000 57.01131  ? 125 ARG B NH2 1 
ATOM   2236 N N   . LYS B 1 128 ? 1.98400  -19.43500 -31.17400 1.000 22.15764  ? 126 LYS B N   1 
ATOM   2237 C CA  . LYS B 1 128 ? 2.68200  -20.30700 -32.10800 1.000 23.52710  ? 126 LYS B CA  1 
ATOM   2238 C C   . LYS B 1 128 ? 4.05500  -19.71600 -32.43800 1.000 26.50004  ? 126 LYS B C   1 
ATOM   2239 O O   . LYS B 1 128 ? 4.19600  -18.50700 -32.61700 1.000 25.35346  ? 126 LYS B O   1 
ATOM   2240 C CB  . LYS B 1 128 ? 1.86300  -20.46000 -33.40800 1.000 24.32108  ? 126 LYS B CB  1 
ATOM   2241 C CG  . LYS B 1 128 ? 0.48300  -21.11700 -33.19700 1.000 31.43093  ? 126 LYS B CG  1 
ATOM   2242 C CD  . LYS B 1 128 ? 0.61400  -22.58800 -32.77000 1.000 25.31943  ? 126 LYS B CD  1 
ATOM   2243 C CE  . LYS B 1 128 ? 1.33300  -23.38700 -33.87400 1.000 38.34581  ? 126 LYS B CE  1 
ATOM   2244 N NZ  . LYS B 1 128 ? 1.42500  -24.85600 -33.52500 1.000 46.65567  ? 126 LYS B NZ  1 
ATOM   2245 N N   . ASN B 1 129 ? 5.07800  -20.56400 -32.50800 1.000 24.41398  ? 127 ASN B N   1 
ATOM   2246 C CA  . ASN B 1 129 ? 6.35900  -20.17600 -33.12600 1.000 23.42405  ? 127 ASN B CA  1 
ATOM   2247 C C   . ASN B 1 129 ? 6.93600  -18.94000 -32.44800 1.000 26.75430  ? 127 ASN B C   1 
ATOM   2248 O O   . ASN B 1 129 ? 7.39500  -17.98900 -33.08900 1.000 25.69850  ? 127 ASN B O   1 
ATOM   2249 C CB  . ASN B 1 129 ? 6.18900  -19.96200 -34.62100 1.000 22.52768  ? 127 ASN B CB  1 
ATOM   2250 C CG  . ASN B 1 129 ? 5.72100  -21.21600 -35.31800 1.000 29.51000  ? 127 ASN B CG  1 
ATOM   2251 O OD1 . ASN B 1 129 ? 6.32400  -22.27300 -35.18000 1.000 31.85630  ? 127 ASN B OD1 1 
ATOM   2252 N ND2 . ASN B 1 129 ? 4.59500  -21.12700 -35.99500 1.000 27.80842  ? 127 ASN B ND2 1 
ATOM   2253 N N   . TYR B 1 130 ? 6.95000  -19.00100 -31.13700 1.000 24.78311  ? 128 TYR B N   1 
ATOM   2254 C CA  . TYR B 1 130 ? 7.27800  -17.89400 -30.26300 1.000 25.93654  ? 128 TYR B CA  1 
ATOM   2255 C C   . TYR B 1 130 ? 8.74900  -17.89500 -29.87900 1.000 25.33480  ? 128 TYR B C   1 
ATOM   2256 O O   . TYR B 1 130 ? 9.36900  -16.82200 -29.80200 1.000 34.18248  ? 128 TYR B O   1 
ATOM   2257 C CB  . TYR B 1 130 ? 6.39700  -17.97300 -29.01700 1.000 30.53558  ? 128 TYR B CB  1 
ATOM   2258 C CG  . TYR B 1 130 ? 6.59500  -16.81700 -28.08200 1.000 27.78488  ? 128 TYR B CG  1 
ATOM   2259 C CD1 . TYR B 1 130 ? 6.17500  -15.55500 -28.42400 1.000 29.68681  ? 128 TYR B CD1 1 
ATOM   2260 C CD2 . TYR B 1 130 ? 7.23500  -16.99000 -26.88800 1.000 29.46494  ? 128 TYR B CD2 1 
ATOM   2261 C CE1 . TYR B 1 130 ? 6.37800  -14.51400 -27.58800 1.000 33.05222  ? 128 TYR B CE1 1 
ATOM   2262 C CE2 . TYR B 1 130 ? 7.43300  -15.95400 -26.04800 1.000 42.77495  ? 128 TYR B CE2 1 
ATOM   2263 C CZ  . TYR B 1 130 ? 6.99700  -14.71500 -26.40300 1.000 34.78607  ? 128 TYR B CZ  1 
ATOM   2264 O OH  . TYR B 1 130 ? 7.20600  -13.65000 -25.55400 1.000 51.69339  ? 128 TYR B OH  1 
ATOM   2265 N N   . TYR B 1 131 ? 9.36000  -19.14600 -29.58700 1.000 20.09312  ? 129 TYR B N   1 
ATOM   2266 C CA  . TYR B 1 131 ? 10.73800 -19.17900 -29.12100 1.000 25.79443  ? 129 TYR B CA  1 
ATOM   2267 C C   . TYR B 1 131 ? 11.67800 -19.67500 -30.20800 1.000 23.36133  ? 129 TYR B C   1 
ATOM   2268 O O   . TYR B 1 131 ? 11.26600 -20.41400 -31.09600 1.000 23.30272  ? 129 TYR B O   1 
ATOM   2269 C CB  . TYR B 1 131 ? 10.90000 -20.13400 -27.95300 1.000 22.24776  ? 129 TYR B CB  1 
ATOM   2270 C CG  . TYR B 1 131 ? 10.15900 -19.80300 -26.70000 1.000 22.36808  ? 129 TYR B CG  1 
ATOM   2271 C CD1 . TYR B 1 131 ? 10.70100 -18.92500 -25.78100 1.000 26.03165  ? 129 TYR B CD1 1 
ATOM   2272 C CD2 . TYR B 1 131 ? 8.95100  -20.39200 -26.41300 1.000 23.56316  ? 129 TYR B CD2 1 
ATOM   2273 C CE1 . TYR B 1 131 ? 10.07700 -18.64300 -24.62000 1.000 29.69324  ? 129 TYR B CE1 1 
ATOM   2274 C CE2 . TYR B 1 131 ? 8.32000  -20.09400 -25.23100 1.000 26.32898  ? 129 TYR B CE2 1 
ATOM   2275 C CZ  . TYR B 1 131 ? 8.87600  -19.21700 -24.35800 1.000 34.43833  ? 129 TYR B CZ  1 
ATOM   2276 O OH  . TYR B 1 131 ? 8.22000  -18.91000 -23.20100 1.000 33.44131  ? 129 TYR B OH  1 
ATOM   2277 N N   . PRO B 1 132 ? 12.96100 -19.33600 -30.17000 1.000 29.39254  ? 130 PRO B N   1 
ATOM   2278 C CA  . PRO B 1 132 ? 13.89700 -19.94800 -31.12700 1.000 26.14878  ? 130 PRO B CA  1 
ATOM   2279 C C   . PRO B 1 132 ? 14.17000 -21.39600 -30.76700 1.000 32.13346  ? 130 PRO B C   1 
ATOM   2280 O O   . PRO B 1 132 ? 14.23900 -21.76700 -29.58700 1.000 27.06739  ? 130 PRO B O   1 
ATOM   2281 C CB  . PRO B 1 132 ? 15.16100 -19.07700 -31.01100 1.000 28.58322  ? 130 PRO B CB  1 
ATOM   2282 C CG  . PRO B 1 132 ? 15.05900 -18.44600 -29.67900 1.000 36.42482  ? 130 PRO B CG  1 
ATOM   2283 C CD  . PRO B 1 132 ? 13.60700 -18.35200 -29.29200 1.000 28.72323  ? 130 PRO B CD  1 
ATOM   2284 N N   . ALA B 1 133 ? 14.27300 -22.23700 -31.78700 1.000 25.77344  ? 131 ALA B N   1 
ATOM   2285 C CA  . ALA B 1 133 ? 14.58600 -23.63400 -31.56700 1.000 27.54650  ? 131 ALA B CA  1 
ATOM   2286 C C   . ALA B 1 133 ? 15.66700 -24.05900 -32.53500 1.000 31.67443  ? 131 ALA B C   1 
ATOM   2287 O O   . ALA B 1 133 ? 16.04000 -23.31100 -33.44500 1.000 31.04418  ? 131 ALA B O   1 
ATOM   2288 C CB  . ALA B 1 133 ? 13.37400 -24.52900 -31.73800 1.000 23.62951  ? 131 ALA B CB  1 
ATOM   2289 N N   . GLU B 1 134 ? 16.19700 -25.26900 -32.31300 1.000 28.93261  ? 132 GLU B N   1 
ATOM   2290 C CA  . GLU B 1 134 ? 17.32000 -25.72100 -33.12400 1.000 31.14938  ? 132 GLU B CA  1 
ATOM   2291 C C   . GLU B 1 134 ? 16.95300 -25.69500 -34.59600 1.000 29.24372  ? 132 GLU B C   1 
ATOM   2292 O O   . GLU B 1 134 ? 17.73400 -25.23800 -35.43200 1.000 31.28446  ? 132 GLU B O   1 
ATOM   2293 C CB  . GLU B 1 134 ? 17.75800 -27.12600 -32.72700 1.000 31.53248  ? 132 GLU B CB  1 
ATOM   2294 C CG  . GLU B 1 134 ? 18.90000 -27.62300 -33.61400 1.000 36.22051  ? 132 GLU B CG  1 
ATOM   2295 C CD  . GLU B 1 134 ? 19.60600 -28.84100 -33.03600 1.000 53.45010  ? 132 GLU B CD  1 
ATOM   2296 O OE1 . GLU B 1 134 ? 19.01700 -29.55000 -32.20200 1.000 56.68954  ? 132 GLU B OE1 1 
ATOM   2297 O OE2 . GLU B 1 134 ? 20.76800 -29.09800 -33.44100 1.000 60.83236  ? 132 GLU B OE2 1 
ATOM   2298 N N   . LYS B 1 135 ? 15.75600 -26.14900 -34.92600 1.000 27.98198  ? 133 LYS B N   1 
ATOM   2299 C CA  . LYS B 1 135 ? 15.19600 -25.97400 -36.26600 1.000 39.95467  ? 133 LYS B CA  1 
ATOM   2300 C C   . LYS B 1 135 ? 13.91400 -25.15600 -36.13800 1.000 23.21530  ? 133 LYS B C   1 
ATOM   2301 O O   . LYS B 1 135 ? 12.96000 -25.59400 -35.48900 1.000 25.01141  ? 133 LYS B O   1 
ATOM   2302 C CB  . LYS B 1 135 ? 14.91700 -27.32900 -36.91300 1.000 32.18233  ? 133 LYS B CB  1 
ATOM   2303 C CG  . LYS B 1 135 ? 14.30000 -27.25900 -38.29100 1.000 44.94559  ? 133 LYS B CG  1 
ATOM   2304 C CD  . LYS B 1 135 ? 15.36000 -26.91100 -39.28500 1.000 40.41259  ? 133 LYS B CD  1 
ATOM   2305 C CE  . LYS B 1 135 ? 14.97000 -27.29500 -40.69700 1.000 41.96912  ? 133 LYS B CE  1 
ATOM   2306 N NZ  . LYS B 1 135 ? 13.63700 -26.72400 -41.04300 1.000 51.45569  ? 133 LYS B NZ  1 
ATOM   2307 N N   . GLY B 1 136 ? 13.89500 -23.94800 -36.72100 1.000 24.59668  ? 134 GLY B N   1 
ATOM   2308 C CA  . GLY B 1 136 ? 12.66100 -23.15600 -36.67300 1.000 22.20795  ? 134 GLY B CA  1 
ATOM   2309 C C   . GLY B 1 136 ? 12.34100 -22.56500 -35.29600 1.000 21.94772  ? 134 GLY B C   1 
ATOM   2310 O O   . GLY B 1 136 ? 13.22100 -22.22000 -34.53300 1.000 25.73818  ? 134 GLY B O   1 
ATOM   2311 N N   . ARG B 1 137 ? 11.04300 -22.40000 -34.99600 1.000 21.11189  ? 135 ARG B N   1 
ATOM   2312 C CA  . ARG B 1 137 ? 10.64100 -21.83100 -33.70800 1.000 23.11744  ? 135 ARG B CA  1 
ATOM   2313 C C   . ARG B 1 137 ? 9.72600  -22.78200 -32.95700 1.000 29.41952  ? 135 ARG B C   1 
ATOM   2314 O O   . ARG B 1 137 ? 9.18800  -23.73300 -33.52300 1.000 22.63818  ? 135 ARG B O   1 
ATOM   2315 C CB  . ARG B 1 137 ? 9.97400  -20.47400 -33.91500 1.000 28.34128  ? 135 ARG B CB  1 
ATOM   2316 C CG  . ARG B 1 137 ? 10.92700 -19.51900 -34.64400 1.000 29.78366  ? 135 ARG B CG  1 
ATOM   2317 C CD  . ARG B 1 137 ? 10.25900 -18.22800 -35.02000 1.000 35.03661  ? 135 ARG B CD  1 
ATOM   2318 N NE  . ARG B 1 137 ? 11.25100 -17.24700 -35.44700 1.000 30.57222  ? 135 ARG B NE  1 
ATOM   2319 C CZ  . ARG B 1 137 ? 11.03700 -16.31900 -36.37000 1.000 33.75010  ? 135 ARG B CZ  1 
ATOM   2320 N NH1 . ARG B 1 137 ? 9.89600  -16.25600 -37.04600 1.000 31.20219  ? 135 ARG B NH1 1 
ATOM   2321 N NH2 . ARG B 1 137 ? 11.99500 -15.43400 -36.63200 1.000 29.71535  ? 135 ARG B NH2 1 
ATOM   2322 N N   . GLU B 1 138 ? 9.55500  -22.51200 -31.66300 1.000 23.25365  ? 136 GLU B N   1 
ATOM   2323 C CA  . GLU B 1 138 ? 8.79900  -23.39200 -30.79000 1.000 21.87848  ? 136 GLU B CA  1 
ATOM   2324 C C   . GLU B 1 138 ? 7.62600  -22.64600 -30.15400 1.000 20.43100  ? 136 GLU B C   1 
ATOM   2325 O O   . GLU B 1 138 ? 7.76300  -21.48800 -29.74500 1.000 23.98209  ? 136 GLU B O   1 
ATOM   2326 C CB  . GLU B 1 138 ? 9.71500  -23.97700 -29.69600 1.000 21.93519  ? 136 GLU B CB  1 
ATOM   2327 C CG  . GLU B 1 138 ? 8.92600  -24.82400 -28.65900 1.000 25.08444  ? 136 GLU B CG  1 
ATOM   2328 C CD  . GLU B 1 138 ? 9.78800  -25.68100 -27.73500 1.000 26.81757  ? 136 GLU B CD  1 
ATOM   2329 O OE1 . GLU B 1 138 ? 10.99200 -25.37200 -27.51500 1.000 26.85402  ? 136 GLU B OE1 1 
ATOM   2330 O OE2 . GLU B 1 138 ? 9.25000  -26.69900 -27.19400 1.000 26.84035  ? 136 GLU B OE2 1 
ATOM   2331 N N   . ASP B 1 139 ? 6.48700  -23.32700 -30.01000 1.000 22.39161  ? 137 ASP B N   1 
ATOM   2332 C CA  . ASP B 1 139 ? 5.30400  -22.67500 -29.46200 1.000 24.34909  ? 137 ASP B CA  1 
ATOM   2333 C C   . ASP B 1 139 ? 5.50500  -22.39700 -27.97700 1.000 21.28610  ? 137 ASP B C   1 
ATOM   2334 O O   . ASP B 1 139 ? 6.23400  -23.10400 -27.28800 1.000 21.69844  ? 137 ASP B O   1 
ATOM   2335 C CB  . ASP B 1 139 ? 4.05600  -23.54600 -29.58900 1.000 25.73139  ? 137 ASP B CB  1 
ATOM   2336 C CG  . ASP B 1 139 ? 3.70000  -23.87200 -31.01800 1.000 25.62666  ? 137 ASP B CG  1 
ATOM   2337 O OD1 . ASP B 1 139 ? 4.18300  -23.15700 -31.91600 1.000 24.09710  ? 137 ASP B OD1 1 
ATOM   2338 O OD2 . ASP B 1 139 ? 2.89400  -24.83100 -31.21000 1.000 33.74821  ? 137 ASP B OD2 1 
ATOM   2339 N N   . ALA B 1 140 ? 4.87000  -21.34100 -27.50800 1.000 20.07957  ? 138 ALA B N   1 
ATOM   2340 C CA  . ALA B 1 140 ? 4.78500  -21.03300 -26.08600 1.000 25.46558  ? 138 ALA B CA  1 
ATOM   2341 C C   . ALA B 1 140 ? 3.40300  -21.42900 -25.58500 1.000 24.40933  ? 138 ALA B C   1 
ATOM   2342 O O   . ALA B 1 140 ? 2.41400  -21.19300 -26.25600 1.000 23.30888  ? 138 ALA B O   1 
ATOM   2343 C CB  . ALA B 1 140 ? 5.03000  -19.54400 -25.84900 1.000 27.89596  ? 138 ALA B CB  1 
ATOM   2344 N N   . LEU B 1 141 ? 3.34400  -22.08100 -24.44100 1.000 20.80816  ? 139 LEU B N   1 
ATOM   2345 C CA  . LEU B 1 141 ? 2.09000  -22.21500 -23.72800 1.000 23.19036  ? 139 LEU B CA  1 
ATOM   2346 C C   . LEU B 1 141 ? 2.01500  -21.12600 -22.66600 1.000 26.74056  ? 139 LEU B C   1 
ATOM   2347 O O   . LEU B 1 141 ? 3.01800  -20.78800 -22.03800 1.000 23.79071  ? 139 LEU B O   1 
ATOM   2348 C CB  . LEU B 1 141 ? 1.97700  -23.57900 -23.07000 1.000 28.02467  ? 139 LEU B CB  1 
ATOM   2349 C CG  . LEU B 1 141 ? 2.19000  -24.79900 -23.92600 1.000 36.11780  ? 139 LEU B CG  1 
ATOM   2350 C CD1 . LEU B 1 141 ? 2.09000  -25.97800 -23.00600 1.000 37.95492  ? 139 LEU B CD1 1 
ATOM   2351 C CD2 . LEU B 1 141 ? 1.10600  -24.87500 -24.97800 1.000 38.12257  ? 139 LEU B CD2 1 
ATOM   2352 N N   . VAL B 1 142 ? 0.82000  -20.57400 -22.48900 1.000 27.41723  ? 140 VAL B N   1 
ATOM   2353 C CA  . VAL B 1 142 ? 0.55700  -19.47100 -21.56000 1.000 25.51260  ? 140 VAL B CA  1 
ATOM   2354 C C   . VAL B 1 142 ? -0.38000 -19.98500 -20.47700 1.000 29.38079  ? 140 VAL B C   1 
ATOM   2355 O O   . VAL B 1 142 ? -1.46600 -20.49200 -20.77900 1.000 28.81308  ? 140 VAL B O   1 
ATOM   2356 C CB  . VAL B 1 142 ? -0.03600 -18.25000 -22.29000 1.000 27.18588  ? 140 VAL B CB  1 
ATOM   2357 C CG1 . VAL B 1 142 ? -0.22400 -17.08400 -21.31700 1.000 32.55792  ? 140 VAL B CG1 1 
ATOM   2358 C CG2 . VAL B 1 142 ? 0.84200  -17.85900 -23.53400 1.000 27.08606  ? 140 VAL B CG2 1 
ATOM   2359 N N   . PHE B 1 143 ? 0.04100  -19.85100 -19.21800 1.000 27.03241  ? 141 PHE B N   1 
ATOM   2360 C CA  . PHE B 1 143 ? -0.69200 -20.32500 -18.05100 1.000 34.04278  ? 141 PHE B CA  1 
ATOM   2361 C C   . PHE B 1 143 ? -1.03200 -19.16300 -17.13700 1.000 30.64826  ? 141 PHE B C   1 
ATOM   2362 O O   . PHE B 1 143 ? -0.32600 -18.15000 -17.08400 1.000 33.59153  ? 141 PHE B O   1 
ATOM   2363 C CB  . PHE B 1 143 ? 0.11500  -21.34100 -17.24000 1.000 29.07848  ? 141 PHE B CB  1 
ATOM   2364 C CG  . PHE B 1 143 ? 0.35400  -22.61400 -17.95500 1.000 29.54867  ? 141 PHE B CG  1 
ATOM   2365 C CD1 . PHE B 1 143 ? 1.42400  -22.74200 -18.82700 1.000 28.62518  ? 141 PHE B CD1 1 
ATOM   2366 C CD2 . PHE B 1 143 ? -0.53100 -23.67700 -17.80900 1.000 31.53314  ? 141 PHE B CD2 1 
ATOM   2367 C CE1 . PHE B 1 143 ? 1.64600  -23.91000 -19.49900 1.000 28.76370  ? 141 PHE B CE1 1 
ATOM   2368 C CE2 . PHE B 1 143 ? -0.32700 -24.85900 -18.50900 1.000 30.55232  ? 141 PHE B CE2 1 
ATOM   2369 C CZ  . PHE B 1 143 ? 0.75800  -24.95800 -19.37900 1.000 31.95069  ? 141 PHE B CZ  1 
ATOM   2370 N N   . ASN B 1 144 ? -2.08600 -19.34800 -16.35900 1.000 33.01690  ? 142 ASN B N   1 
ATOM   2371 C CA  . ASN B 1 144 ? -2.46400 -18.37900 -15.35800 1.000 35.06113  ? 142 ASN B CA  1 
ATOM   2372 C C   . ASN B 1 144 ? -2.67000 -19.12900 -14.05800 1.000 36.87981  ? 142 ASN B C   1 
ATOM   2373 O O   . ASN B 1 144 ? -3.22000 -20.23400 -14.05400 1.000 38.53448  ? 142 ASN B O   1 
ATOM   2374 C CB  . ASN B 1 144 ? -3.75300 -17.62300 -15.76300 1.000 38.50941  ? 142 ASN B CB  1 
ATOM   2375 C CG  . ASN B 1 144 ? -4.26600 -16.74800 -14.66400 1.000 49.71326  ? 142 ASN B CG  1 
ATOM   2376 O OD1 . ASN B 1 144 ? -3.90500 -15.57200 -14.56500 1.000 52.60212  ? 142 ASN B OD1 1 
ATOM   2377 N ND2 . ASN B 1 144 ? -5.12400 -17.30800 -13.82500 1.000 52.64264  ? 142 ASN B ND2 1 
ATOM   2378 N N   . LEU B 1 145 ? -2.22900 -18.53100 -12.96200 1.000 37.91336  ? 143 LEU B N   1 
ATOM   2379 C CA  . LEU B 1 145 ? -2.40200 -19.11300 -11.64100 1.000 39.59203  ? 143 LEU B CA  1 
ATOM   2380 C C   . LEU B 1 145 ? -3.08900 -18.08200 -10.76200 1.000 47.43831  ? 143 LEU B C   1 
ATOM   2381 O O   . LEU B 1 145 ? -2.61900 -16.94800 -10.64400 1.000 53.82403  ? 143 LEU B O   1 
ATOM   2382 C CB  . LEU B 1 145 ? -1.05800 -19.53800 -11.04600 1.000 38.73233  ? 143 LEU B CB  1 
ATOM   2383 C CG  . LEU B 1 145 ? -1.04700 -19.97600 -9.56900  1.000 41.00239  ? 143 LEU B CG  1 
ATOM   2384 C CD1 . LEU B 1 145 ? -1.89600 -21.21700 -9.33200  1.000 47.81105  ? 143 LEU B CD1 1 
ATOM   2385 C CD2 . LEU B 1 145 ? 0.40600  -20.19200 -9.07200  1.000 46.56674  ? 143 LEU B CD2 1 
ATOM   2386 N N   . ASN B 1 146 ? -4.21200 -18.46400 -10.17100 1.000 45.01110  ? 144 ASN B N   1 
ATOM   2387 C CA  . ASN B 1 146 ? -4.91100 -17.58700 -9.25200  1.000 50.27708  ? 144 ASN B CA  1 
ATOM   2388 C C   . ASN B 1 146 ? -4.35900 -17.79100 -7.85200  1.000 52.83945  ? 144 ASN B C   1 
ATOM   2389 O O   . ASN B 1 146 ? -4.07500 -18.92100 -7.44900  1.000 53.46923  ? 144 ASN B O   1 
ATOM   2390 C CB  . ASN B 1 146 ? -6.41200 -17.87000 -9.28600  1.000 57.84403  ? 144 ASN B CB  1 
ATOM   2391 C CG  . ASN B 1 146 ? -6.99800 -17.68200 -10.67100 1.000 51.58324  ? 144 ASN B CG  1 
ATOM   2392 O OD1 . ASN B 1 146 ? -6.45600 -16.93800 -11.47300 1.000 55.13817  ? 144 ASN B OD1 1 
ATOM   2393 N ND2 . ASN B 1 146 ? -8.11800 -18.34300 -10.94900 1.000 66.40830  ? 144 ASN B ND2 1 
ATOM   2394 N N   . PHE B 1 147 ? -4.17600 -16.69400 -7.12600  1.000 58.22751  ? 145 PHE B N   1 
ATOM   2395 C CA  . PHE B 1 147 ? -3.77000 -16.77900 -5.71600  1.000 54.83990  ? 145 PHE B CA  1 
ATOM   2396 C C   . PHE B 1 147 ? -4.35600 -15.63700 -4.86600  1.000 71.06246  ? 145 PHE B C   1 
ATOM   2397 O O   . PHE B 1 147 ? -4.54900 -14.51000 -5.34500  1.000 69.47992  ? 145 PHE B O   1 
ATOM   2398 C CB  . PHE B 1 147 ? -2.25000 -16.78800 -5.60000  1.000 59.32722  ? 145 PHE B CB  1 
ATOM   2399 C CG  . PHE B 1 147 ? -1.59600 -15.55300 -6.15400  1.000 59.73963  ? 145 PHE B CG  1 
ATOM   2400 C CD1 . PHE B 1 147 ? -1.37000 -15.42100 -7.51500  1.000 55.34152  ? 145 PHE B CD1 1 
ATOM   2401 C CD2 . PHE B 1 147 ? -1.20800 -14.52500 -5.31900  1.000 60.17870  ? 145 PHE B CD2 1 
ATOM   2402 C CE1 . PHE B 1 147 ? -0.77600 -14.29400 -8.02100  1.000 51.45135  ? 145 PHE B CE1 1 
ATOM   2403 C CE2 . PHE B 1 147 ? -0.61300 -13.39200 -5.82800  1.000 65.02291  ? 145 PHE B CE2 1 
ATOM   2404 C CZ  . PHE B 1 147 ? -0.39700 -13.27900 -7.18200  1.000 64.67353  ? 145 PHE B CZ  1 
HETATM 2405 N N1A . COA C 2 .   ? 27.62100 -27.36200 -46.70800 1.000 34.93147  ? 201 COA A N1A 1 
HETATM 2406 C C2A . COA C 2 .   ? 28.89200 -27.50000 -47.17200 1.000 31.67097  ? 201 COA A C2A 1 
HETATM 2407 N N3A . COA C 2 .   ? 29.45400 -26.50200 -47.88200 1.000 36.57299  ? 201 COA A N3A 1 
HETATM 2408 C C4A . COA C 2 .   ? 28.71500 -25.37500 -48.10000 1.000 30.82208  ? 201 COA A C4A 1 
HETATM 2409 C C5A . COA C 2 .   ? 27.47000 -25.22200 -47.65700 1.000 29.15833  ? 201 COA A C5A 1 
HETATM 2410 C C6A . COA C 2 .   ? 26.91400 -26.25300 -46.94500 1.000 32.27375  ? 201 COA A C6A 1 
HETATM 2411 N N6A . COA C 2 .   ? 25.59100 -26.25200 -46.37700 1.000 31.81812  ? 201 COA A N6A 1 
HETATM 2412 N N7A . COA C 2 .   ? 26.98900 -24.01600 -48.05200 1.000 22.62454  ? 201 COA A N7A 1 
HETATM 2413 C C8A . COA C 2 .   ? 28.00500 -23.44100 -48.73900 1.000 24.92550  ? 201 COA A C8A 1 
HETATM 2414 N N9A . COA C 2 .   ? 29.05800 -24.29300 -48.74100 1.000 31.36242  ? 201 COA A N9A 1 
HETATM 2415 C C1B . COA C 2 .   ? 30.10100 -23.61800 -49.54900 1.000 30.16531  ? 201 COA A C1B 1 
HETATM 2416 C C2B . COA C 2 .   ? 30.09600 -24.18500 -50.92900 1.000 42.55475  ? 201 COA A C2B 1 
HETATM 2417 O O2B . COA C 2 .   ? 31.48700 -24.70400 -51.18700 1.000 44.73373  ? 201 COA A O2B 1 
HETATM 2418 C C3B . COA C 2 .   ? 29.46000 -23.07500 -51.72200 1.000 33.44637  ? 201 COA A C3B 1 
HETATM 2419 O O3B . COA C 2 .   ? 30.12100 -23.16100 -52.99800 1.000 50.68850  ? 201 COA A O3B 1 
HETATM 2420 P P3B . COA C 2 .   ? 29.35500 -23.97300 -54.16400 1.000 66.96716  ? 201 COA A P3B 1 
HETATM 2421 O O7A . COA C 2 .   ? 27.97400 -23.54600 -54.26400 1.000 32.54161  ? 201 COA A O7A 1 
HETATM 2422 O O8A . COA C 2 .   ? 30.24900 -23.51200 -55.41800 1.000 56.73462  ? 201 COA A O8A 1 
HETATM 2423 O O9A . COA C 2 .   ? 29.26500 -25.47700 -53.82300 1.000 35.53488  ? 201 COA A O9A 1 
HETATM 2424 C C4B . COA C 2 .   ? 30.01200 -21.87100 -51.33300 1.000 21.90070  ? 201 COA A C4B 1 
HETATM 2425 O O4B . COA C 2 .   ? 29.92700 -22.20600 -49.79800 1.000 23.91319  ? 201 COA A O4B 1 
HETATM 2426 C C5B . COA C 2 .   ? 29.09500 -20.75400 -51.54000 1.000 28.19060  ? 201 COA A C5B 1 
HETATM 2427 O O5B . COA C 2 .   ? 28.01100 -20.74100 -51.00700 1.000 20.70616  ? 201 COA A O5B 1 
HETATM 2428 P P1A . COA C 2 .   ? 26.65900 -19.99300 -51.55500 1.000 18.66161  ? 201 COA A P1A 1 
HETATM 2429 O O1A . COA C 2 .   ? 25.88600 -20.81600 -52.57300 1.000 21.59278  ? 201 COA A O1A 1 
HETATM 2430 O O2A . COA C 2 .   ? 27.00400 -18.56000 -51.91100 1.000 19.22771  ? 201 COA A O2A 1 
HETATM 2431 O O3A . COA C 2 .   ? 25.86200 -19.96800 -50.14200 1.000 16.02560  ? 201 COA A O3A 1 
HETATM 2432 P P2A . COA C 2 .   ? 24.26300 -20.07200 -49.86400 1.000 17.57928  ? 201 COA A P2A 1 
HETATM 2433 O O4A . COA C 2 .   ? 23.56000 -19.06200 -50.72100 1.000 16.09685  ? 201 COA A O4A 1 
HETATM 2434 O O5A . COA C 2 .   ? 23.86200 -21.52000 -49.98200 1.000 18.26381  ? 201 COA A O5A 1 
HETATM 2435 O O6A . COA C 2 .   ? 24.25700 -19.62800 -48.31200 1.000 16.79361  ? 201 COA A O6A 1 
HETATM 2436 C CBP . COA C 2 .   ? 24.54400 -19.99800 -46.04000 1.000 16.80760  ? 201 COA A CBP 1 
HETATM 2437 C CCP . COA C 2 .   ? 25.17200 -20.21500 -47.40900 1.000 18.83115  ? 201 COA A CCP 1 
HETATM 2438 C CDP . COA C 2 .   ? 25.58700 -20.32600 -44.95600 1.000 16.62608  ? 201 COA A CDP 1 
HETATM 2439 C CEP . COA C 2 .   ? 24.14100 -18.48800 -45.91300 1.000 18.71387  ? 201 COA A CEP 1 
HETATM 2440 C CAP . COA C 2 .   ? 23.30100 -20.89200 -45.89100 1.000 14.34038  ? 201 COA A CAP 1 
HETATM 2441 O OAP . COA C 2 .   ? 23.72900 -22.23000 -45.62500 1.000 20.88630  ? 201 COA A OAP 1 
HETATM 2442 C C9P . COA C 2 .   ? 22.45700 -20.44700 -44.70500 1.000 19.28966  ? 201 COA A C9P 1 
HETATM 2443 O O9P . COA C 2 .   ? 21.57500 -19.61700 -44.78300 1.000 14.86325  ? 201 COA A O9P 1 
HETATM 2444 N N8P . COA C 2 .   ? 22.76900 -21.15800 -43.53000 1.000 17.91169  ? 201 COA A N8P 1 
HETATM 2445 C C7P . COA C 2 .   ? 22.02800 -20.88000 -42.26900 1.000 22.02339  ? 201 COA A C7P 1 
HETATM 2446 C C6P . COA C 2 .   ? 22.34200 -19.42800 -41.94900 1.000 19.38390  ? 201 COA A C6P 1 
HETATM 2447 C C5P . COA C 2 .   ? 22.90000 -19.17500 -40.57700 1.000 19.78893  ? 201 COA A C5P 1 
HETATM 2448 O O5P . COA C 2 .   ? 23.00300 -20.07500 -39.82400 1.000 21.09508  ? 201 COA A O5P 1 
HETATM 2449 N N4P . COA C 2 .   ? 23.20100 -17.83300 -40.17400 1.000 17.47409  ? 201 COA A N4P 1 
HETATM 2450 C C3P . COA C 2 .   ? 23.69400 -17.51700 -38.81700 1.000 25.91188  ? 201 COA A C3P 1 
HETATM 2451 C C2P . COA C 2 .   ? 25.20900 -17.61900 -38.74000 1.000 27.50730  ? 201 COA A C2P 1 
HETATM 2452 S S1P . COA C 2 .   ? 25.94000 -16.40200 -39.88700 1.000 29.53453  ? 201 COA A S1P 1 
HETATM 2453 N N1A . COA D 2 .   ? 8.13600  -34.15900 -13.86000 1.000 56.60543  ? 201 COA B N1A 1 
HETATM 2454 C C2A . COA D 2 .   ? 6.80600  -34.32300 -13.63100 1.000 63.64733  ? 201 COA B C2A 1 
HETATM 2455 N N3A . COA D 2 .   ? 6.17000  -33.59800 -12.67100 1.000 57.30049  ? 201 COA B N3A 1 
HETATM 2456 C C4A . COA D 2 .   ? 6.85500  -32.71000 -11.92700 1.000 53.35877  ? 201 COA B C4A 1 
HETATM 2457 C C5A . COA D 2 .   ? 8.17000  -32.54300 -12.14400 1.000 54.44163  ? 201 COA B C5A 1 
HETATM 2458 C C6A . COA D 2 .   ? 8.80900  -33.28400 -13.13300 1.000 51.94082  ? 201 COA B C6A 1 
HETATM 2459 N N6A . COA D 2 .   ? 10.19800 -33.06500 -13.16700 1.000 57.49800  ? 201 COA B N6A 1 
HETATM 2460 N N7A . COA D 2 .   ? 8.60900  -31.62100 -11.28100 1.000 45.03428  ? 201 COA B N7A 1 
HETATM 2461 C C8A . COA D 2 .   ? 7.56600  -31.21000 -10.55400 1.000 47.34808  ? 201 COA B C8A 1 
HETATM 2462 N N9A . COA D 2 .   ? 6.46300  -31.88800 -10.93700 1.000 57.75826  ? 201 COA B N9A 1 
HETATM 2463 C C1B . COA D 2 .   ? 5.31000  -31.48100 -10.10600 1.000 59.90934  ? 201 COA B C1B 1 
HETATM 2464 C C2B . COA D 2 .   ? 5.44600  -33.00400 -9.68700  1.000 66.88679  ? 201 COA B C2B 1 
HETATM 2465 O O2B . COA D 2 .   ? 4.10800  -33.49600 -10.04100 1.000 81.30980  ? 201 COA B O2B 1 
HETATM 2466 C C3B . COA D 2 .   ? 5.91800  -32.85800 -8.26500  1.000 67.48889  ? 201 COA B C3B 1 
HETATM 2467 O O3B . COA D 2 .   ? 5.21900  -33.57600 -7.18500  1.000 73.56544  ? 201 COA B O3B 1 
HETATM 2468 P P3B . COA D 2 .   ? 5.79700  -34.84800 -6.74700  1.000 99.48397  ? 201 COA B P3B 1 
HETATM 2469 O O7A . COA D 2 .   ? 6.06100  -35.57200 -8.05700  1.000 79.30351  ? 201 COA B O7A 1 
HETATM 2470 O O8A . COA D 2 .   ? 7.10900  -34.58700 -6.03300  1.000 76.70278  ? 201 COA B O8A 1 
HETATM 2471 O O9A . COA D 2 .   ? 4.90700  -35.67400 -5.84800  1.000 99.81227  ? 201 COA B O9A 1 
HETATM 2472 C C4B . COA D 2 .   ? 6.08400  -31.67000 -7.79100  1.000 65.98230  ? 201 COA B C4B 1 
HETATM 2473 O O4B . COA D 2 .   ? 6.04100  -30.84300 -8.98800  1.000 61.70080  ? 201 COA B O4B 1 
HETATM 2474 C C5B . COA D 2 .   ? 7.40600  -31.40100 -7.13100  1.000 61.67771  ? 201 COA B C5B 1 
HETATM 2475 O O5B . COA D 2 .   ? 7.36500  -30.05600 -6.80500  1.000 54.05103  ? 201 COA B O5B 1 
HETATM 2476 P P1A . COA D 2 .   ? 8.80000  -29.46300 -6.37100  1.000 48.06027  ? 201 COA B P1A 1 
HETATM 2477 O O1A . COA D 2 .   ? 9.65700  -30.57300 -5.81300  1.000 51.46757  ? 201 COA B O1A 1 
HETATM 2478 O O2A . COA D 2 .   ? 8.55000  -28.30300 -5.45700  1.000 39.23755  ? 201 COA B O2A 1 
HETATM 2479 O O3A . COA D 2 .   ? 9.58800  -28.87700 -7.67900  1.000 46.09732  ? 201 COA B O3A 1 
HETATM 2480 P P2A . COA D 2 .   ? 11.19500 -29.05800 -7.96200  1.000 39.80458  ? 201 COA B P2A 1 
HETATM 2481 O O4A . COA D 2 .   ? 12.12700 -28.59800 -6.86900  1.000 41.34846  ? 201 COA B O4A 1 
HETATM 2482 O O5A . COA D 2 .   ? 11.45400 -30.47700 -8.42400  1.000 38.58433  ? 201 COA B O5A 1 
HETATM 2483 O O6A . COA D 2 .   ? 11.41000 -28.02400 -9.21300  1.000 31.63124  ? 201 COA B O6A 1 
HETATM 2484 C CBP . COA D 2 .   ? 11.13400 -27.47400 -11.40400 1.000 29.86076  ? 201 COA B CBP 1 
HETATM 2485 C CCP . COA D 2 .   ? 10.50200 -28.23400 -10.25100 1.000 32.52854  ? 201 COA B CCP 1 
HETATM 2486 C CDP . COA D 2 .   ? 10.08900 -27.28900 -12.51200 1.000 29.94612  ? 201 COA B CDP 1 
HETATM 2487 C CEP . COA D 2 .   ? 11.58600 -26.09700 -10.90200 1.000 28.00372  ? 201 COA B CEP 1 
HETATM 2488 C CAP . COA D 2 .   ? 12.33200 -28.31500 -11.82400 1.000 31.70030  ? 201 COA B CAP 1 
HETATM 2489 O OAP . COA D 2 .   ? 11.86800 -29.44900 -12.50300 1.000 35.84474  ? 201 COA B OAP 1 
HETATM 2490 C C9P . COA D 2 .   ? 13.18300 -27.46000 -12.76000 1.000 40.12488  ? 201 COA B C9P 1 
HETATM 2491 O O9P . COA D 2 .   ? 14.08900 -26.78600 -12.36200 1.000 35.16139  ? 201 COA B O9P 1 
HETATM 2492 N N8P . COA D 2 .   ? 12.83200 -27.48200 -14.16600 1.000 29.85729  ? 201 COA B N8P 1 
HETATM 2493 C C7P . COA D 2 .   ? 13.60700 -26.66100 -15.07500 1.000 28.57376  ? 201 COA B C7P 1 
HETATM 2494 C C6P . COA D 2 .   ? 13.19900 -25.22100 -14.79700 1.000 35.04717  ? 201 COA B C6P 1 
HETATM 2495 C C5P . COA D 2 .   ? 12.81500 -24.48000 -16.09400 1.000 28.81573  ? 201 COA B C5P 1 
HETATM 2496 O O5P . COA D 2 .   ? 12.66800 -25.07900 -17.12000 1.000 29.52341  ? 201 COA B O5P 1 
HETATM 2497 N N4P . COA D 2 .   ? 12.62300 -23.03700 -16.01700 1.000 27.41842  ? 201 COA B N4P 1 
HETATM 2498 C C3P . COA D 2 .   ? 12.27000 -22.24200 -17.19400 1.000 28.47265  ? 201 COA B C3P 1 
HETATM 2499 C C2P . COA D 2 .   ? 10.75500 -22.17900 -17.39400 1.000 30.46633  ? 201 COA B C2P 1 
HETATM 2500 S S1P . COA D 2 .   ? 9.96200  -21.26600 -16.04300 1.000 40.80297  ? 201 COA B S1P 1 
HETATM 2501 O O   . HOH E 3 .   ? 26.84800 -7.34000  -55.78900 1.000 42.39367  ? 301 HOH A O   1 
HETATM 2502 O O   . HOH E 3 .   ? 29.626   -26.632   -55.924   1.000 46.05235  ? 302 HOH A O   1 
HETATM 2503 O O   . HOH E 3 .   ? 33.91500 -25.65000 -47.07900 1.000 40.30267  ? 303 HOH A O   1 
HETATM 2504 O O   . HOH E 3 .   ? 23.21200 -25.57400 -46.66500 1.000 35.29445  ? 304 HOH A O   1 
HETATM 2505 O O   . HOH E 3 .   ? 14.59500 -14.27000 -60.60300 1.000 24.85264  ? 305 HOH A O   1 
HETATM 2506 O O   . HOH E 3 .   ? 10.32600 -14.06400 -49.01200 1.000 20.61311  ? 306 HOH A O   1 
HETATM 2507 O O   . HOH E 3 .   ? 23.32600 -19.43400 -21.63900 1.000 41.01176  ? 307 HOH A O   1 
HETATM 2508 O O   . HOH E 3 .   ? 21.93800 1.85200   -51.32400 1.000 30.21026  ? 308 HOH A O   1 
HETATM 2509 O O   . HOH E 3 .   ? 33.44300 -6.89700  -52.16300 1.000 30.89208  ? 309 HOH A O   1 
HETATM 2510 O O   . HOH E 3 .   ? 22.58700 -19.71800 -53.04200 1.000 17.47468  ? 310 HOH A O   1 
HETATM 2511 O O   . HOH E 3 .   ? 36.23600 0.86000   -40.55900 1.000 38.23248  ? 311 HOH A O   1 
HETATM 2512 O O   . HOH E 3 .   ? 4.11300  -15.25100 -44.54600 1.000 37.36089  ? 312 HOH A O   1 
HETATM 2513 O O   . HOH E 3 .   ? 26.57100 4.73000   -44.96700 1.000 47.11345  ? 313 HOH A O   1 
HETATM 2514 O O   . HOH E 3 .   ? 30.94500 -26.31700 -24.23400 1.000 39.79921  ? 314 HOH A O   1 
HETATM 2515 O O   . HOH E 3 .   ? 28.24000 -27.50700 -30.60600 1.000 29.60633  ? 315 HOH A O   1 
HETATM 2516 O O   . HOH E 3 .   ? 7.88500  -12.51700 -40.24600 1.000 38.11274  ? 316 HOH A O   1 
HETATM 2517 O O   . HOH E 3 .   ? 21.85300 -2.56900  -56.38200 1.000 27.47128  ? 317 HOH A O   1 
HETATM 2518 O O   . HOH E 3 .   ? 11.23400 -15.28800 -61.76900 1.000 33.06548  ? 318 HOH A O   1 
HETATM 2519 O O   . HOH E 3 .   ? 25.57200 -2.46000  -30.77600 1.000 38.25748  ? 319 HOH A O   1 
HETATM 2520 O O   . HOH E 3 .   ? 24.06700 -23.49000 -48.21200 1.000 18.25594  ? 320 HOH A O   1 
HETATM 2521 O O   . HOH E 3 .   ? 43.14100 -15.54900 -31.57600 1.000 32.99722  ? 321 HOH A O   1 
HETATM 2522 O O   . HOH E 3 .   ? 15.74900 -22.62600 -38.45700 1.000 18.42466  ? 322 HOH A O   1 
HETATM 2523 O O   . HOH E 3 .   ? 40.70000 -22.73200 -44.79800 1.000 38.03754  ? 323 HOH A O   1 
HETATM 2524 O O   . HOH E 3 .   ? 29.33600 -29.53400 -32.52800 1.000 38.40299  ? 324 HOH A O   1 
HETATM 2525 O O   . HOH E 3 .   ? 9.03700  -8.48400  -58.58500 1.000 39.79549  ? 325 HOH A O   1 
HETATM 2526 O O   . HOH E 3 .   ? 25.46200 -28.22100 -24.04900 1.000 39.96222  ? 326 HOH A O   1 
HETATM 2527 O O   . HOH E 3 .   ? 12.49400 -11.29800 -59.64100 1.000 23.29732  ? 327 HOH A O   1 
HETATM 2528 O O   . HOH E 3 .   ? 41.14100 -14.24200 -44.49400 1.000 32.55360  ? 328 HOH A O   1 
HETATM 2529 O O   . HOH E 3 .   ? 37.86800 -7.22100  -51.08800 1.000 40.87604  ? 329 HOH A O   1 
HETATM 2530 O O   . HOH E 3 .   ? 23.61600 -25.13100 -35.35000 1.000 30.34081  ? 330 HOH A O   1 
HETATM 2531 O O   . HOH E 3 .   ? 23.35400 -28.06300 -32.44300 1.000 45.42956  ? 331 HOH A O   1 
HETATM 2532 O O   . HOH E 3 .   ? 12.144   -15.860   -64.367   1.000 34.43908  ? 332 HOH A O   1 
HETATM 2533 O O   . HOH E 3 .   ? 31.54900 -13.76700 -51.61600 1.000 27.49026  ? 333 HOH A O   1 
HETATM 2534 O O   . HOH E 3 .   ? 29.68100 -26.47200 -27.69300 1.000 32.30528  ? 334 HOH A O   1 
HETATM 2535 O O   . HOH E 3 .   ? 39.59700 -20.18600 -45.66900 1.000 25.37649  ? 335 HOH A O   1 
HETATM 2536 O O   . HOH E 3 .   ? 29.483   -24.905   -57.638   1.000 33.33989  ? 336 HOH A O   1 
HETATM 2537 O O   . HOH E 3 .   ? 29.25500 -12.50700 -35.53700 1.000 19.58199  ? 337 HOH A O   1 
HETATM 2538 O O   . HOH E 3 .   ? 8.86000  -8.14500  -45.82400 1.000 29.75273  ? 338 HOH A O   1 
HETATM 2539 O O   . HOH E 3 .   ? 30.85500 -27.70800 -53.60500 1.000 47.09930  ? 339 HOH A O   1 
HETATM 2540 O O   . HOH E 3 .   ? 29.33900 -19.09700 -20.38400 1.000 38.37581  ? 340 HOH A O   1 
HETATM 2541 O O   . HOH E 3 .   ? 12.13700 -23.90800 -40.21600 1.000 36.30750  ? 341 HOH A O   1 
HETATM 2542 O O   . HOH E 3 .   ? 40.25000 -22.04200 -40.01500 1.000 38.39057  ? 342 HOH A O   1 
HETATM 2543 O O   . HOH E 3 .   ? 16.75200 0.12200   -50.23000 1.000 22.27053  ? 343 HOH A O   1 
HETATM 2544 O O   . HOH E 3 .   ? 5.28000  -11.78700 -44.05500 1.000 31.20592  ? 344 HOH A O   1 
HETATM 2545 O O   . HOH E 3 .   ? 26.40500 -15.34500 -36.51000 1.000 31.51066  ? 345 HOH A O   1 
HETATM 2546 O O   . HOH E 3 .   ? 44.20500 -18.74400 -36.47100 1.000 28.98002  ? 346 HOH A O   1 
HETATM 2547 O O   . HOH E 3 .   ? 25.41000 -0.61800  -50.51700 1.000 36.37844  ? 347 HOH A O   1 
HETATM 2548 O O   . HOH E 3 .   ? 9.51900  -13.40100 -34.07500 1.000 40.37180  ? 348 HOH A O   1 
HETATM 2549 O O   . HOH E 3 .   ? 32.46800 -27.43400 -35.84800 1.000 36.64833  ? 349 HOH A O   1 
HETATM 2550 O O   . HOH E 3 .   ? 38.36900 -25.37900 -32.81300 1.000 34.03188  ? 350 HOH A O   1 
HETATM 2551 O O   . HOH E 3 .   ? 20.20700 -1.48200  -40.34000 1.000 29.71631  ? 351 HOH A O   1 
HETATM 2552 O O   . HOH E 3 .   ? 20.85700 -27.40800 -28.47800 1.000 40.13383  ? 352 HOH A O   1 
HETATM 2553 O O   . HOH E 3 .   ? 9.83800  -15.40400 -46.82400 1.000 25.27390  ? 353 HOH A O   1 
HETATM 2554 O O   . HOH E 3 .   ? 9.65400  -6.67400  -56.85700 1.000 38.88325  ? 354 HOH A O   1 
HETATM 2555 O O   . HOH E 3 .   ? 27.58400 -15.86700 -23.38500 1.000 35.69805  ? 355 HOH A O   1 
HETATM 2556 O O   . HOH E 3 .   ? 13.25100 -24.93700 -43.30500 1.000 34.86670  ? 356 HOH A O   1 
HETATM 2557 O O   . HOH E 3 .   ? 35.74000 -13.22200 -49.84200 1.000 27.72023  ? 357 HOH A O   1 
HETATM 2558 O O   . HOH E 3 .   ? 13.39200 -2.84800  -31.67800 1.000 49.12065  ? 358 HOH A O   1 
HETATM 2559 O O   . HOH E 3 .   ? 36.92900 -7.44100  -37.65200 1.000 32.86354  ? 359 HOH A O   1 
HETATM 2560 O O   . HOH E 3 .   ? 32.11400 -26.62500 -49.21000 1.000 41.40545  ? 360 HOH A O   1 
HETATM 2561 O O   . HOH E 3 .   ? 9.64300  -19.14500 -42.57500 1.000 28.12001  ? 361 HOH A O   1 
HETATM 2562 O O   . HOH E 3 .   ? 12.50300 -16.80400 -49.10100 1.000 20.44984  ? 362 HOH A O   1 
HETATM 2563 O O   . HOH E 3 .   ? 42.70900 -14.07300 -41.17900 1.000 39.66799  ? 363 HOH A O   1 
HETATM 2564 O O   . HOH E 3 .   ? 6.40700  -21.75100 -39.21500 1.000 32.59798  ? 364 HOH A O   1 
HETATM 2565 O O   . HOH E 3 .   ? 14.356   -16.989   -62.745   1.000 65.07859  ? 365 HOH A O   1 
HETATM 2566 O O   . HOH E 3 .   ? 31.93500 -19.30000 -49.82900 1.000 22.85903  ? 366 HOH A O   1 
HETATM 2567 O O   . HOH E 3 .   ? 19.62200 -23.75100 -43.75100 1.000 20.38280  ? 367 HOH A O   1 
HETATM 2568 O O   . HOH E 3 .   ? 31.74300 -16.73300 -51.09200 1.000 25.21725  ? 368 HOH A O   1 
HETATM 2569 O O   . HOH E 3 .   ? 15.11200 -19.23100 -59.71200 1.000 29.26743  ? 369 HOH A O   1 
HETATM 2570 O O   . HOH E 3 .   ? 28.83000 -7.35600  -31.62500 1.000 37.04945  ? 370 HOH A O   1 
HETATM 2571 O O   . HOH E 3 .   ? 11.26900 -8.91900  -59.65000 1.000 35.15530  ? 371 HOH A O   1 
HETATM 2572 O O   . HOH E 3 .   ? 22.06200 -24.80900 -44.23100 1.000 38.10472  ? 372 HOH A O   1 
HETATM 2573 O O   . HOH E 3 .   ? 12.02600 -19.26700 -61.76200 1.000 32.22268  ? 373 HOH A O   1 
HETATM 2574 O O   . HOH E 3 .   ? 24.30200 -17.94200 -23.55700 1.000 40.87795  ? 374 HOH A O   1 
HETATM 2575 O O   . HOH E 3 .   ? 13.99300 -0.51900  -54.32700 1.000 37.15255  ? 375 HOH A O   1 
HETATM 2576 O O   . HOH E 3 .   ? 23.57000 -27.22800 -29.81000 1.000 38.76018  ? 376 HOH A O   1 
HETATM 2577 O O   . HOH E 3 .   ? 16.85600 1.08500   -43.97100 1.000 49.68012  ? 377 HOH A O   1 
HETATM 2578 O O   . HOH E 3 .   ? 7.53700  -10.43200 -52.45500 1.000 35.54472  ? 378 HOH A O   1 
HETATM 2579 O O   . HOH E 3 .   ? 23.34600 -14.66300 -33.39300 1.000 35.50455  ? 379 HOH A O   1 
HETATM 2580 O O   . HOH E 3 .   ? 35.34800 -26.35400 -29.13700 1.000 36.42651  ? 380 HOH A O   1 
HETATM 2581 O O   . HOH E 3 .   ? 20.32300 -0.02900  -52.23200 1.000 23.76178  ? 381 HOH A O   1 
HETATM 2582 O O   . HOH E 3 .   ? 38.09600 -11.51800 -49.36700 1.000 31.68362  ? 382 HOH A O   1 
HETATM 2583 O O   . HOH E 3 .   ? 6.47700  -17.94300 -37.66200 1.000 30.82954  ? 383 HOH A O   1 
HETATM 2584 O O   . HOH E 3 .   ? 43.30200 -7.72100  -46.28000 1.000 32.30805  ? 384 HOH A O   1 
HETATM 2585 O O   . HOH E 3 .   ? 31.05300 -19.23000 -54.09200 1.000 29.76449  ? 385 HOH A O   1 
HETATM 2586 O O   . HOH E 3 .   ? 17.13600 -18.19000 -58.24400 1.000 37.01169  ? 386 HOH A O   1 
HETATM 2587 O O   . HOH E 3 .   ? 18.514   -2.223    -56.266   1.000 25.14824  ? 387 HOH A O   1 
HETATM 2588 O O   . HOH E 3 .   ? 21.78200 -29.20800 -26.24000 1.000 32.75583  ? 388 HOH A O   1 
HETATM 2589 O O   . HOH E 3 .   ? 24.90100 -15.47000 -26.70700 1.000 39.82870  ? 389 HOH A O   1 
HETATM 2590 O O   . HOH E 3 .   ? 27.84000 -15.66900 -56.54700 1.000 30.34758  ? 390 HOH A O   1 
HETATM 2591 O O   . HOH E 3 .   ? 8.62200  1.53700   -47.64500 1.000 47.24680  ? 391 HOH A O   1 
HETATM 2592 O O   . HOH E 3 .   ? 36.95200 -26.35000 -35.46900 1.000 53.27849  ? 392 HOH A O   1 
HETATM 2593 O O   . HOH E 3 .   ? 29.64000 -13.35100 -55.73600 1.000 33.62593  ? 393 HOH A O   1 
HETATM 2594 O O   . HOH E 3 .   ? 22.830   -1.741    -52.096   1.000 36.59486  ? 394 HOH A O   1 
HETATM 2595 O O   . HOH E 3 .   ? 12.35500 -18.94600 -50.72500 1.000 23.39532  ? 395 HOH A O   1 
HETATM 2596 O O   . HOH E 3 .   ? 23.43100 -27.97300 -48.90500 1.000 32.28368  ? 396 HOH A O   1 
HETATM 2597 O O   . HOH E 3 .   ? 21.22700 -0.56100  -43.94300 1.000 29.39486  ? 397 HOH A O   1 
HETATM 2598 O O   . HOH E 3 .   ? 9.10600  -11.00300 -32.59300 1.000 48.94629  ? 398 HOH A O   1 
HETATM 2599 O O   . HOH E 3 .   ? 24.95300 -19.57800 -35.29500 1.000 13.87751  ? 399 HOH A O   1 
HETATM 2600 O O   . HOH E 3 .   ? 14.11000 -19.95700 -63.14000 1.000 47.61754  ? 400 HOH A O   1 
HETATM 2601 O O   . HOH E 3 .   ? 12.860   -21.828   -48.941   1.000 21.84807  ? 401 HOH A O   1 
HETATM 2602 O O   . HOH E 3 .   ? 17.73400 -16.20900 -31.15400 1.000 37.17742  ? 402 HOH A O   1 
HETATM 2603 O O   . HOH E 3 .   ? 32.55600 -28.67100 -24.30800 1.000 44.73998  ? 403 HOH A O   1 
HETATM 2604 O O   . HOH E 3 .   ? 6.16400  -18.67200 -41.28900 1.000 40.73435  ? 404 HOH A O   1 
HETATM 2605 O O   . HOH E 3 .   ? 28.95400 -27.92200 -25.47300 1.000 41.10097  ? 405 HOH A O   1 
HETATM 2606 O O   . HOH E 3 .   ? 20.33800 3.18700   -39.92900 1.000 56.24694  ? 406 HOH A O   1 
HETATM 2607 O O   . HOH E 3 .   ? 35.896   8.980     -44.775   1.000 53.32695  ? 407 HOH A O   1 
HETATM 2608 O O   . HOH E 3 .   ? 16.84700 -24.49300 -40.07800 1.000 29.44900  ? 408 HOH A O   1 
HETATM 2609 O O   . HOH E 3 .   ? 12.252   -12.755   -62.012   1.000 27.48047  ? 409 HOH A O   1 
HETATM 2610 O O   . HOH E 3 .   ? 43.523   -14.110   -45.720   1.000 35.04775  ? 410 HOH A O   1 
HETATM 2611 O O   . HOH E 3 .   ? 28.59000 -20.42400 -55.59800 1.000 41.88195  ? 411 HOH A O   1 
HETATM 2612 O O   . HOH E 3 .   ? 11.84400 -17.46500 -46.50000 1.000 24.60556  ? 412 HOH A O   1 
HETATM 2613 O O   . HOH E 3 .   ? 19.82500 -8.59100  -32.26700 1.000 46.59303  ? 413 HOH A O   1 
HETATM 2614 O O   . HOH E 3 .   ? 21.86600 -17.60000 -35.64900 1.000 45.94320  ? 414 HOH A O   1 
HETATM 2615 O O   . HOH E 3 .   ? 21.33100 -16.66400 -32.41800 1.000 51.71583  ? 415 HOH A O   1 
HETATM 2616 O O   . HOH E 3 .   ? 10.551   -1.050    -57.337   1.000 29.62351  ? 416 HOH A O   1 
HETATM 2617 O O   . HOH E 3 .   ? 18.58200 -3.88200  -28.52000 1.000 47.54486  ? 417 HOH A O   1 
HETATM 2618 O O   . HOH E 3 .   ? 31.492   -22.658   -17.917   1.000 47.97507  ? 418 HOH A O   1 
HETATM 2619 O O   . HOH E 3 .   ? 30.743   -6.547    -55.794   1.000 51.88052  ? 419 HOH A O   1 
HETATM 2620 O O   . HOH E 3 .   ? 20.87600 -12.56700 -30.35300 1.000 53.40821  ? 420 HOH A O   1 
HETATM 2621 O O   . HOH E 3 .   ? 36.54800 -29.71700 -26.62000 1.000 45.52469  ? 421 HOH A O   1 
HETATM 2622 O O   . HOH E 3 .   ? 16.11800 -33.18400 -23.12700 1.000 53.76214  ? 422 HOH A O   1 
HETATM 2623 O O   . HOH E 3 .   ? 12.321   1.063     -56.419   1.000 30.40252  ? 423 HOH A O   1 
HETATM 2624 O O   . HOH E 3 .   ? 38.52500 -15.67300 -26.11600 1.000 39.58637  ? 424 HOH A O   1 
HETATM 2625 O O   . HOH E 3 .   ? 33.52700 -12.05000 -50.66800 1.000 25.46947  ? 425 HOH A O   1 
HETATM 2626 O O   . HOH E 3 .   ? 43.87300 -2.69200  -47.41900 1.000 52.68718  ? 426 HOH A O   1 
HETATM 2627 O O   . HOH E 3 .   ? 22.06800 -10.12800 -31.98700 1.000 51.30708  ? 427 HOH A O   1 
HETATM 2628 O O   . HOH E 3 .   ? 31.81200 -14.82300 -56.03600 1.000 26.66245  ? 428 HOH A O   1 
HETATM 2629 O O   . HOH E 3 .   ? 16.505   0.002     -54.925   1.000 38.98965  ? 429 HOH A O   1 
HETATM 2630 O O   . HOH E 3 .   ? 17.11600 2.17000   -48.72800 1.000 34.30423  ? 430 HOH A O   1 
HETATM 2631 O O   . HOH E 3 .   ? 13.92800 -27.08300 -48.05300 1.000 40.53311  ? 431 HOH A O   1 
HETATM 2632 O O   . HOH E 3 .   ? 30.06200 -15.73700 -22.31900 1.000 33.75756  ? 432 HOH A O   1 
HETATM 2633 O O   . HOH E 3 .   ? 24.56300 -32.03600 -25.15000 1.000 52.86768  ? 433 HOH A O   1 
HETATM 2634 O O   . HOH E 3 .   ? 18.43700 -32.81500 -18.47700 1.000 54.88337  ? 434 HOH A O   1 
HETATM 2635 O O   . HOH E 3 .   ? 34.83600 -27.40500 -34.24200 1.000 38.83496  ? 435 HOH A O   1 
HETATM 2636 O O   . HOH E 3 .   ? 44.493   -14.133   -34.742   1.000 43.94250  ? 436 HOH A O   1 
HETATM 2637 O O   . HOH E 3 .   ? 23.86600 -32.96500 -22.62300 1.000 57.38954  ? 437 HOH A O   1 
HETATM 2638 O O   . HOH F 3 .   ? 25.41400 -22.30200 -3.99600  1.000 62.68588  ? 301 HOH B O   1 
HETATM 2639 O O   . HOH F 3 .   ? 7.35200  -24.54500 -35.30400 1.000 40.64553  ? 302 HOH B O   1 
HETATM 2640 O O   . HOH F 3 .   ? 28.21700 -22.48600 -15.19900 1.000 47.95612  ? 303 HOH B O   1 
HETATM 2641 O O   . HOH F 3 .   ? 27.70100 -19.75700 -15.14100 1.000 50.96812  ? 304 HOH B O   1 
HETATM 2642 O O   . HOH F 3 .   ? 18.89800 -26.46200 -37.34800 1.000 40.93986  ? 305 HOH B O   1 
HETATM 2643 O O   . HOH F 3 .   ? 18.97400 -28.66100 -29.77600 1.000 41.76250  ? 306 HOH B O   1 
HETATM 2644 O O   . HOH F 3 .   ? 4.22300  -16.14000 -31.51800 1.000 38.14316  ? 307 HOH B O   1 
HETATM 2645 O O   . HOH F 3 .   ? 15.42600 -19.60800 -22.29800 1.000 39.77902  ? 308 HOH B O   1 
HETATM 2646 O O   . HOH F 3 .   ? 12.91500 -30.10200 -4.84100  1.000 42.86230  ? 309 HOH B O   1 
HETATM 2647 O O   . HOH F 3 .   ? 20.36400 -26.67600 -19.34100 1.000 33.30213  ? 310 HOH B O   1 
HETATM 2648 O O   . HOH F 3 .   ? 10.45500 -8.54100  -18.86800 1.000 53.35018  ? 311 HOH B O   1 
HETATM 2649 O O   . HOH F 3 .   ? 6.60700  -16.12200 -18.26500 1.000 28.37730  ? 312 HOH B O   1 
HETATM 2650 O O   . HOH F 3 .   ? 19.00300 -18.10400 -22.96200 1.000 34.49458  ? 313 HOH B O   1 
HETATM 2651 O O   . HOH F 3 .   ? -6.09400 -14.80400 -17.73400 1.000 58.11151  ? 314 HOH B O   1 
HETATM 2652 O O   . HOH F 3 .   ? 7.06000  -16.61400 -35.41700 1.000 39.33420  ? 315 HOH B O   1 
HETATM 2653 O O   . HOH F 3 .   ? 27.11500 -14.34300 -19.98500 1.000 48.57072  ? 316 HOH B O   1 
HETATM 2654 O O   . HOH F 3 .   ? -2.33200 -26.73900 -25.86800 1.000 35.25782  ? 317 HOH B O   1 
HETATM 2655 O O   . HOH F 3 .   ? -6.64800 -25.11000 -20.08300 1.000 37.11574  ? 318 HOH B O   1 
HETATM 2656 O O   . HOH F 3 .   ? -8.42800 -21.93500 -20.07800 1.000 34.25758  ? 319 HOH B O   1 
HETATM 2657 O O   . HOH F 3 .   ? 12.69400 -27.15900 -28.72500 1.000 35.01053  ? 320 HOH B O   1 
HETATM 2658 O O   . HOH F 3 .   ? 27.20800 -26.22500 -21.33400 1.000 35.45630  ? 321 HOH B O   1 
HETATM 2659 O O   . HOH F 3 .   ? 12.23800 -10.38100 -0.35100  1.000 58.22448  ? 322 HOH B O   1 
HETATM 2660 O O   . HOH F 3 .   ? 21.76400 -30.69600 -17.63900 1.000 61.78399  ? 323 HOH B O   1 
HETATM 2661 O O   . HOH F 3 .   ? 10.24200 -26.06900 -35.15500 1.000 36.89216  ? 324 HOH B O   1 
HETATM 2662 O O   . HOH F 3 .   ? 16.23800 -29.76400 -14.75200 1.000 48.35089  ? 325 HOH B O   1 
HETATM 2663 O O   . HOH F 3 .   ? 11.69500 -15.92400 -31.03300 1.000 33.03126  ? 326 HOH B O   1 
HETATM 2664 O O   . HOH F 3 .   ? 12.84100 -17.07100 -33.16100 1.000 39.92246  ? 327 HOH B O   1 
HETATM 2665 O O   . HOH F 3 .   ? 15.01200 -18.87800 -25.22200 1.000 39.00359  ? 328 HOH B O   1 
HETATM 2666 O O   . HOH F 3 .   ? 10.22300 -32.31900 -24.20300 1.000 45.47699  ? 329 HOH B O   1 
HETATM 2667 O O   A HOH F 3 .   ? -3.85900 -28.09700 -13.12200 0.500 33.27236  ? 330 HOH B O   1 
HETATM 2668 O O   B HOH F 3 .   ? -3.84400 -29.91000 -14.20900 0.500 36.63726  ? 330 HOH B O   1 
HETATM 2669 O O   . HOH F 3 .   ? 14.98000 -27.00400 -30.44200 1.000 36.58013  ? 331 HOH B O   1 
HETATM 2670 O O   . HOH F 3 .   ? 9.03000  -22.97000 -36.92800 1.000 25.54241  ? 332 HOH B O   1 
HETATM 2671 O O   . HOH F 3 .   ? 8.34300  -14.58100 -38.75500 1.000 44.53545  ? 333 HOH B O   1 
HETATM 2672 O O   . HOH F 3 .   ? 0.79000  -25.81800 -29.50400 1.000 36.39153  ? 334 HOH B O   1 
HETATM 2673 O O   . HOH F 3 .   ? 11.23400 -15.36300 -19.15500 1.000 36.92664  ? 335 HOH B O   1 
HETATM 2674 O O   . HOH F 3 .   ? 19.129   -6.148    -1.839    1.000 51.42038  ? 336 HOH B O   1 
HETATM 2675 O O   . HOH F 3 .   ? 32.078   -15.991   -13.683   1.000 65.39071  ? 337 HOH B O   1 
HETATM 2676 O O   . HOH F 3 .   ? 12.99000 -27.66600 -23.57800 1.000 39.57012  ? 338 HOH B O   1 
HETATM 2677 O O   . HOH F 3 .   ? -2.765   -20.863   -5.584    1.000 39.46606  ? 339 HOH B O   1 
HETATM 2678 O O   . HOH F 3 .   ? 3.37800  -16.61800 -34.83500 1.000 29.13666  ? 340 HOH B O   1 
HETATM 2679 O O   . HOH F 3 .   ? 28.10300 -20.35900 -1.36200  1.000 52.12057  ? 341 HOH B O   1 
HETATM 2680 O O   . HOH F 3 .   ? 6.34200  -26.19600 -31.03800 1.000 28.30101  ? 342 HOH B O   1 
HETATM 2681 O O   . HOH F 3 .   ? 30.54400 -10.79900 -7.17300  1.000 57.53299  ? 343 HOH B O   1 
HETATM 2682 O O   . HOH F 3 .   ? 14.50600 -28.79700 -33.72400 1.000 37.61392  ? 344 HOH B O   1 
HETATM 2683 O O   . HOH F 3 .   ? 20.69100 -3.98300  -12.54600 1.000 77.95131  ? 345 HOH B O   1 
HETATM 2684 O O   . HOH F 3 .   ? 3.65800  -24.48600 -4.32200  1.000 41.10734  ? 346 HOH B O   1 
HETATM 2685 O O   . HOH F 3 .   ? 1.69500  -33.22800 -13.03000 1.000 46.78997  ? 347 HOH B O   1 
HETATM 2686 O O   . HOH F 3 .   ? 10.92300 -22.53300 -21.17500 1.000 20.41297  ? 348 HOH B O   1 
HETATM 2687 O O   . HOH F 3 .   ? 8.92600  -16.11700 -20.03500 1.000 37.87570  ? 349 HOH B O   1 
HETATM 2688 O O   . HOH F 3 .   ? 6.67500  -30.52400 -27.68400 1.000 39.22467  ? 350 HOH B O   1 
HETATM 2689 O O   . HOH F 3 .   ? 21.13000 -12.35000 4.01600   1.000 45.56997  ? 351 HOH B O   1 
HETATM 2690 O O   . HOH F 3 .   ? 7.83500  -12.02900 0.59600   1.000 56.82648  ? 352 HOH B O   1 
HETATM 2691 O O   . HOH F 3 .   ? 17.78300 -31.91000 -15.93100 1.000 52.46997  ? 353 HOH B O   1 
HETATM 2692 O O   . HOH F 3 .   ? 7.36500  -13.48000 -35.68100 1.000 35.07589  ? 354 HOH B O   1 
HETATM 2693 O O   . HOH F 3 .   ? -2.619   -15.271   -28.772   1.000 38.34446  ? 355 HOH B O   1 
HETATM 2694 O O   . HOH F 3 .   ? 15.59900 -7.67100  -17.79900 1.000 57.19392  ? 356 HOH B O   1 
HETATM 2695 O O   . HOH F 3 .   ? 17.66900 -18.91100 -26.13200 1.000 49.23963  ? 357 HOH B O   1 
HETATM 2696 O O   . HOH F 3 .   ? 5.89900  -14.02600 -32.05400 1.000 40.81969  ? 358 HOH B O   1 
HETATM 2697 O O   . HOH F 3 .   ? -7.315   -15.602   -20.762   1.000 41.50274  ? 359 HOH B O   1 
HETATM 2698 O O   . HOH F 3 .   ? 17.87200 -29.70400 -37.37800 1.000 40.67574  ? 360 HOH B O   1 
HETATM 2699 O O   . HOH F 3 .   ? 1.10800  -28.95300 -25.55400 1.000 40.52345  ? 361 HOH B O   1 
HETATM 2700 O O   A HOH F 3 .   ? 14.63100 -11.53300 -22.73700 0.500 43.43236  ? 362 HOH B O   1 
HETATM 2701 O O   B HOH F 3 .   ? 13.98900 -12.27600 -21.01900 0.500 39.88038  ? 362 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLN A 1   ? 0.82549 0.53238 0.59362 0.09187  0.06836  -0.24145 -1  GLN A N   
2    C CA  . GLN A 1   ? 0.91917 0.64119 0.66034 0.09695  0.09874  -0.24541 -1  GLN A CA  
3    C C   . GLN A 1   ? 0.90643 0.59277 0.57923 0.07701  0.10999  -0.20783 -1  GLN A C   
4    O O   . GLN A 1   ? 1.07084 0.77534 0.73817 0.06650  0.14871  -0.20350 -1  GLN A O   
5    C CB  . GLN A 1   ? 1.11854 0.85615 0.79757 0.09825  0.11971  -0.27597 -1  GLN A CB  
6    C CG  . GLN A 1   ? 1.18478 0.95307 0.93110 0.10634  0.11505  -0.31343 -1  GLN A CG  
7    C CD  . GLN A 1   ? 1.33594 1.05207 1.08713 0.14448  0.12912  -0.28410 -1  GLN A CD  
8    O OE1 . GLN A 1   ? 1.42605 1.19569 1.20974 0.15389  0.15233  -0.30398 -1  GLN A OE1 
9    N NE2 . GLN A 1   ? 1.33938 1.03598 1.14928 0.14207  0.12211  -0.27563 -1  GLN A NE2 
10   N N   . SER A 2   ? 0.77210 0.41715 0.40630 0.06786  0.07822  -0.18348 0   SER A N   
11   C CA  . SER A 2   ? 0.76589 0.37520 0.34771 0.04706  0.08237  -0.15015 0   SER A CA  
12   C C   . SER A 2   ? 0.82019 0.45484 0.48258 0.04950  0.09587  -0.14010 0   SER A C   
13   O O   . SER A 2   ? 0.65488 0.32256 0.41080 0.06660  0.08254  -0.14649 0   SER A O   
14   C CB  . SER A 2   ? 0.76768 0.33732 0.32055 0.04351  0.03658  -0.12977 0   SER A CB  
15   O OG  . SER A 2   ? 0.94194 0.53642 0.57913 0.04674  0.01785  -0.11787 0   SER A OG  
16   N N   . MET A 3   ? 0.69039 0.34108 0.34352 0.02638  0.11722  -0.11564 1   MET A N   
17   C CA  . MET A 3   ? 0.61585 0.30664 0.35417 0.02558  0.11805  -0.09612 1   MET A CA  
18   C C   . MET A 3   ? 0.61961 0.30198 0.32419 -0.00348 0.11295  -0.06433 1   MET A C   
19   O O   . MET A 3   ? 0.67948 0.35130 0.31850 -0.02796 0.13044  -0.05620 1   MET A O   
20   C CB  . MET A 3   ? 0.59427 0.35189 0.40716 0.03241  0.15104  -0.10702 1   MET A CB  
21   C CG  . MET A 3   ? 0.70610 0.47791 0.53961 0.05544  0.16749  -0.14660 1   MET A CG  
22   S SD  . MET A 3   ? 1.26392 1.09338 1.22705 0.08396  0.17687  -0.16249 1   MET A SD  
23   C CE  . MET A 3   ? 0.66347 0.56968 0.64977 0.07082  0.22378  -0.18468 1   MET A CE  
24   N N   . LYS A 4   ? 0.56424 0.24817 0.30993 -0.00305 0.08962  -0.04756 2   LYS A N   
25   C CA  . LYS A 4   ? 0.56395 0.23803 0.28771 -0.02764 0.07833  -0.02280 2   LYS A CA  
26   C C   . LYS A 4   ? 0.50049 0.23261 0.30447 -0.02895 0.08433  -0.01034 2   LYS A C   
27   O O   . LYS A 4   ? 0.45426 0.20366 0.31380 -0.00921 0.07475  -0.01349 2   LYS A O   
28   C CB  . LYS A 4   ? 0.58799 0.20663 0.28035 -0.02347 0.03626  -0.02342 2   LYS A CB  
29   C CG  . LYS A 4   ? 0.68282 0.28257 0.35619 -0.04477 0.01654  -0.00419 2   LYS A CG  
30   C CD  . LYS A 4   ? 0.75587 0.33408 0.41408 -0.03280 -0.02701 -0.01236 2   LYS A CD  
31   C CE  . LYS A 4   ? 0.90753 0.49482 0.57127 -0.04665 -0.04827 0.00043  2   LYS A CE  
32   N NZ  . LYS A 4   ? 0.79607 0.39855 0.47639 -0.03030 -0.08409 -0.00678 2   LYS A NZ  
33   N N   . ILE A 5   ? 0.50637 0.26677 0.31499 -0.05298 0.09964  0.00353  3   ILE A N   
34   C CA  . ILE A 5   ? 0.45152 0.26370 0.33007 -0.05407 0.09568  0.01395  3   ILE A CA  
35   C C   . ILE A 5   ? 0.45535 0.25066 0.31168 -0.07939 0.07886  0.02960  3   ILE A C   
36   O O   . ILE A 5   ? 0.50933 0.27412 0.31177 -0.10440 0.08781  0.03627  3   ILE A O   
37   C CB  . ILE A 5   ? 0.44575 0.32499 0.38129 -0.05455 0.12705  0.00618  3   ILE A CB  
38   C CG1 . ILE A 5   ? 0.44749 0.33847 0.41039 -0.02620 0.13934  -0.01464 3   ILE A CG1 
39   C CG2 . ILE A 5   ? 0.40559 0.33505 0.40889 -0.05284 0.11330  0.01628  3   ILE A CG2 
40   C CD1 . ILE A 5   ? 0.45525 0.41062 0.47330 -0.02408 0.17191  -0.03442 3   ILE A CD1 
41   N N   . ARG A 6   ? 0.40828 0.21662 0.29973 -0.07396 0.05341  0.03476  4   ARG A N   
42   C CA  . ARG A 6   ? 0.41147 0.20573 0.29047 -0.09553 0.03432  0.04280  4   ARG A CA  
43   C C   . ARG A 6   ? 0.35607 0.19943 0.29350 -0.09039 0.01879  0.04437  4   ARG A C   
44   O O   . ARG A 6   ? 0.32407 0.19275 0.29356 -0.06994 0.01613  0.04347  4   ARG A O   
45   C CB  . ARG A 6   ? 0.44079 0.16401 0.26319 -0.09560 0.00483  0.03837  4   ARG A CB  
46   C CG  . ARG A 6   ? 0.44914 0.17039 0.28993 -0.06897 -0.01618 0.02243  4   ARG A CG  
47   C CD  . ARG A 6   ? 0.49553 0.21707 0.33052 -0.05818 -0.04540 0.00835  4   ARG A CD  
48   N NE  . ARG A 6   ? 0.42052 0.16640 0.28590 -0.03779 -0.04996 -0.00699 4   ARG A NE  
49   C CZ  . ARG A 6   ? 0.40949 0.19200 0.31793 -0.03508 -0.04903 -0.01182 4   ARG A CZ  
50   N NH1 . ARG A 6   ? 0.36920 0.16786 0.29326 -0.04722 -0.05136 -0.00445 4   ARG A NH1 
51   N NH2 . ARG A 6   ? 0.40169 0.20285 0.33391 -0.02416 -0.04437 -0.02399 4   ARG A NH2 
52   N N   . ASN A 7   ? 0.38478 0.23603 0.33052 -0.11042 0.00660  0.04705  5   ASN A N   
53   C CA  . ASN A 7   ? 0.31040 0.20353 0.29878 -0.10609 -0.01312 0.04413  5   ASN A CA  
54   C C   . ASN A 7   ? 0.31093 0.17935 0.28524 -0.09240 -0.03474 0.03513  5   ASN A C   
55   O O   . ASN A 7   ? 0.37294 0.18790 0.30960 -0.09048 -0.04508 0.02628  5   ASN A O   
56   C CB  . ASN A 7   ? 0.37382 0.27766 0.37647 -0.13022 -0.02438 0.04194  5   ASN A CB  
57   C CG  . ASN A 7   ? 0.51516 0.46376 0.55297 -0.14491 -0.00079 0.04578  5   ASN A CG  
58   O OD1 . ASN A 7   ? 0.51353 0.43581 0.52756 -0.16734 0.01847  0.05070  5   ASN A OD1 
59   N ND2 . ASN A 7   ? 0.45264 0.47009 0.54665 -0.13274 -0.00149 0.04260  5   ASN A ND2 
60   N N   . TRP A 8   ? 0.28696 0.19643 0.29113 -0.08207 -0.04035 0.03620  6   TRP A N   
61   C CA  . TRP A 8   ? 0.29934 0.19728 0.29611 -0.07512 -0.05311 0.02621  6   TRP A CA  
62   C C   . TRP A 8   ? 0.28753 0.18905 0.28605 -0.08698 -0.07465 0.00696  6   TRP A C   
63   O O   . TRP A 8   ? 0.31138 0.23126 0.32127 -0.09521 -0.07877 0.00510  6   TRP A O   
64   C CB  . TRP A 8   ? 0.26689 0.20045 0.28209 -0.06394 -0.04899 0.03872  6   TRP A CB  
65   C CG  . TRP A 8   ? 0.23324 0.22130 0.26914 -0.06903 -0.06000 0.04397  6   TRP A CG  
66   C CD1 . TRP A 8   ? 0.21669 0.23602 0.27098 -0.08188 -0.07021 0.03632  6   TRP A CD1 
67   C CD2 . TRP A 8   ? 0.22907 0.24291 0.26498 -0.06165 -0.06406 0.05771  6   TRP A CD2 
68   N NE1 . TRP A 8   ? 0.22647 0.29737 0.29558 -0.07991 -0.08198 0.04057  6   TRP A NE1 
69   C CE2 . TRP A 8   ? 0.22355 0.28861 0.27474 -0.06763 -0.07908 0.05612  6   TRP A CE2 
70   C CE3 . TRP A 8   ? 0.39390 0.38727 0.41446 -0.05238 -0.05755 0.07203  6   TRP A CE3 
71   C CZ2 . TRP A 8   ? 0.36628 0.46234 0.40795 -0.06234 -0.09006 0.07008  6   TRP A CZ2 
72   C CZ3 . TRP A 8   ? 0.32839 0.34513 0.33843 -0.05011 -0.06603 0.09038  6   TRP A CZ3 
73   C CH2 . TRP A 8   ? 0.43958 0.50745 0.45530 -0.05425 -0.08341 0.08987  6   TRP A CH2 
74   N N   . ILE A 9   ? 0.37257 0.27328 0.36621 -0.07315 -0.07338 -0.01065 7   ILE A N   
75   C CA  . ILE A 9   ? 0.35725 0.28234 0.36155 -0.06721 -0.07263 -0.03211 7   ILE A CA  
76   C C   . ILE A 9   ? 0.37685 0.32759 0.38936 -0.06789 -0.06467 -0.04642 7   ILE A C   
77   O O   . ILE A 9   ? 0.40447 0.33999 0.41192 -0.06878 -0.06235 -0.04000 7   ILE A O   
78   C CB  . ILE A 9   ? 0.41530 0.31244 0.40689 -0.05640 -0.07515 -0.03709 7   ILE A CB  
79   C CG1 . ILE A 9   ? 0.36690 0.24496 0.34800 -0.04551 -0.07181 -0.03856 7   ILE A CG1 
80   C CG2 . ILE A 9   ? 0.41226 0.27990 0.38643 -0.06254 -0.08126 -0.02309 7   ILE A CG2 
81   C CD1 . ILE A 9   ? 0.59302 0.44099 0.55778 -0.03353 -0.08878 -0.03888 7   ILE A CD1 
82   N N   . LYS A 10  ? 0.42141 0.39685 0.48167 0.17272  0.03917  -0.00842 8   LYS A N   
83   C CA  . LYS A 10  ? 0.43374 0.45572 0.52463 0.17387  0.05343  -0.01800 8   LYS A CA  
84   C C   . LYS A 10  ? 0.35737 0.42644 0.48854 0.17753  0.04235  -0.00829 8   LYS A C   
85   O O   . LYS A 10  ? 0.35810 0.46744 0.50552 0.16725  0.05027  -0.00828 8   LYS A O   
86   C CB  . LYS A 10  ? 0.37230 0.39323 0.48091 0.18815  0.06675  -0.03484 8   LYS A CB  
87   C CG  . LYS A 10  ? 0.42068 0.49748 0.56851 0.19175  0.08033  -0.04282 8   LYS A CG  
88   C CD  . LYS A 10  ? 0.70440 0.79072 0.83586 0.17821  0.10184  -0.05811 8   LYS A CD  
89   C CE  . LYS A 10  ? 0.67557 0.73628 0.80261 0.18952  0.11260  -0.07938 8   LYS A CE  
90   N NZ  . LYS A 10  ? 0.69898 0.78581 0.82416 0.17925  0.13516  -0.09727 8   LYS A NZ  
91   N N   . ASP A 11  ? 0.34063 0.40666 0.48753 0.18809  0.02256  0.00173  9   ASP A N   
92   C CA  . ASP A 11  ? 0.34326 0.45639 0.53042 0.18883  0.00901  0.00947  9   ASP A CA  
93   C C   . ASP A 11  ? 0.37766 0.50572 0.55484 0.16888  0.00092  0.01637  9   ASP A C   
94   O O   . ASP A 11  ? 0.24732 0.42042 0.46043 0.16312  -0.00644 0.01948  9   ASP A O   
95   C CB  . ASP A 11  ? 0.43094 0.53596 0.63163 0.20133  -0.01304 0.02021  9   ASP A CB  
96   C CG  . ASP A 11  ? 0.53081 0.65447 0.77415 0.22403  -0.00949 0.01559  9   ASP A CG  
97   O OD1 . ASP A 11  ? 0.57041 0.71984 0.83616 0.22927  0.01009  0.00246  9   ASP A OD1 
98   O OD2 . ASP A 11  ? 0.45314 0.56773 0.70827 0.23692  -0.02586 0.02570  9   ASP A OD2 
99   N N   . ASP A 12  ? 0.27469 0.36675 0.40632 0.15741  0.00146  0.01815  10  ASP A N   
100  C CA  . ASP A 12  ? 0.20164 0.30235 0.32242 0.14055  -0.00714 0.02330  10  ASP A CA  
101  C C   . ASP A 12  ? 0.27878 0.41164 0.41393 0.12945  0.01009  0.02142  10  ASP A C   
102  O O   . ASP A 12  ? 0.23766 0.38432 0.37621 0.11462  0.00126  0.02725  10  ASP A O   
103  C CB  . ASP A 12  ? 0.20913 0.26387 0.27683 0.13193  -0.01039 0.02497  10  ASP A CB  
104  C CG  . ASP A 12  ? 0.30166 0.33092 0.35261 0.13457  -0.02679 0.03116  10  ASP A CG  
105  O OD1 . ASP A 12  ? 0.31905 0.36843 0.39598 0.13892  -0.04271 0.03668  10  ASP A OD1 
106  O OD2 . ASP A 12  ? 0.32020 0.31312 0.33328 0.13071  -0.02312 0.03186  10  ASP A OD2 
107  N N   . VAL A 13  ? 0.31733 0.45819 0.45653 0.13224  0.03393  0.01336  11  VAL A N   
108  C CA  . VAL A 13  ? 0.23183 0.39231 0.36778 0.11534  0.05293  0.01333  11  VAL A CA  
109  C C   . VAL A 13  ? 0.20681 0.41933 0.38641 0.10062  0.04881  0.02327  11  VAL A C   
110  O O   . VAL A 13  ? 0.24789 0.46187 0.41821 0.07858  0.05132  0.03035  11  VAL A O   
111  C CB  . VAL A 13  ? 0.35014 0.50636 0.47563 0.11736  0.07536  -0.00032 11  VAL A CB  
112  C CG1 . VAL A 13  ? 0.30328 0.48681 0.42921 0.09610  0.09100  0.00152  11  VAL A CG1 
113  C CG2 . VAL A 13  ? 0.34728 0.44897 0.42437 0.11855  0.07757  -0.00830 11  VAL A CG2 
114  N N   . PRO A 14  ? 0.21717 0.46498 0.44065 0.10578  0.03932  0.02393  12  PRO A N   
115  C CA  . PRO A 14  ? 0.28622 0.57940 0.54921 0.08422  0.03432  0.03328  12  PRO A CA  
116  C C   . PRO A 14  ? 0.17122 0.45164 0.43035 0.06761  0.01095  0.04243  12  PRO A C   
117  O O   . PRO A 14  ? 0.14361 0.43003 0.40841 0.04136  0.01178  0.05001  12  PRO A O   
118  C CB  . PRO A 14  ? 0.31261 0.64149 0.61939 0.09604  0.02654  0.02886  12  PRO A CB  
119  C CG  . PRO A 14  ? 0.29648 0.61039 0.59196 0.11911  0.04186  0.01740  12  PRO A CG  
120  C CD  . PRO A 14  ? 0.25115 0.50592 0.49547 0.12750  0.03907  0.01526  12  PRO A CD  
121  N N   . GLN A 15  ? 0.18003 0.42942 0.41920 0.07887  -0.01171 0.03881  13  GLN A N   
122  C CA  . GLN A 15  ? 0.16391 0.38629 0.38405 0.06166  -0.03481 0.03924  13  GLN A CA  
123  C C   . GLN A 15  ? 0.18924 0.36669 0.36097 0.05020  -0.02578 0.03819  13  GLN A C   
124  O O   . GLN A 15  ? 0.17136 0.33538 0.33780 0.03084  -0.03606 0.03989  13  GLN A O   
125  C CB  . GLN A 15  ? 0.15982 0.36684 0.36647 0.07800  -0.05964 0.03561  13  GLN A CB  
126  C CG  . GLN A 15  ? 0.27548 0.51887 0.52062 0.08036  -0.07754 0.03261  13  GLN A CG  
127  C CD  . GLN A 15  ? 0.26164 0.48483 0.47455 0.08848  -0.09394 0.03797  13  GLN A CD  
128  O OE1 . GLN A 15  ? 0.30211 0.51654 0.49611 0.07688  -0.11141 0.03303  13  GLN A OE1 
129  N NE2 . GLN A 15  ? 0.46542 0.66768 0.68008 0.10553  -0.09319 0.04033  13  GLN A NE2 
130  N N   . VAL A 16  ? 0.20355 0.35474 0.33904 0.06248  -0.00878 0.03455  14  VAL A N   
131  C CA  . VAL A 16  ? 0.14260 0.26005 0.23577 0.05157  0.00024  0.03403  14  VAL A CA  
132  C C   . VAL A 16  ? 0.15302 0.29022 0.26124 0.03133  0.01340  0.04205  14  VAL A C   
133  O O   . VAL A 16  ? 0.20526 0.32218 0.29620 0.01627  0.00841  0.04620  14  VAL A O   
134  C CB  . VAL A 16  ? 0.25369 0.34701 0.31250 0.06598  0.01649  0.02801  14  VAL A CB  
135  C CG1 . VAL A 16  ? 0.24173 0.31298 0.26237 0.05313  0.02894  0.02778  14  VAL A CG1 
136  C CG2 . VAL A 16  ? 0.25863 0.32361 0.29545 0.08084  -0.00017 0.02545  14  VAL A CG2 
137  N N   . SER A 17  ? 0.15874 0.33694 0.29897 0.03213  0.03079  0.04532  15  SER A N   
138  C CA  A SER A 17  ? 0.14383 0.34708 0.29835 0.01145  0.04495  0.05689  15  SER A CA  
139  C CA  B SER A 17  ? 0.14316 0.34820 0.29932 0.01177  0.04524  0.05686  15  SER A CA  
140  C C   . SER A 17  ? 0.15999 0.37146 0.34567 -0.01019 0.02601  0.06725  15  SER A C   
141  O O   . SER A 17  ? 0.17009 0.37394 0.35129 -0.03047 0.02828  0.07908  15  SER A O   
142  C CB  A SER A 17  ? 0.17885 0.43107 0.36027 0.01789  0.06929  0.05656  15  SER A CB  
143  C CB  B SER A 17  ? 0.17591 0.43152 0.36243 0.01959  0.06803  0.05611  15  SER A CB  
144  O OG  A SER A 17  ? 0.25641 0.53735 0.47711 0.03207  0.06172  0.05140  15  SER A OG  
145  O OG  B SER A 17  ? 0.14239 0.41541 0.33771 -0.00230 0.07656  0.06448  15  SER A OG  
146  N N   . GLU A 18  ? 0.15943 0.38316 0.37534 -0.00652 0.00517  0.06301  16  GLU A N   
147  C CA  . GLU A 18  ? 0.13453 0.35926 0.37768 -0.02864 -0.01691 0.06849  16  GLU A CA  
148  C C   . GLU A 18  ? 0.14207 0.31040 0.34642 -0.03430 -0.03362 0.06393  16  GLU A C   
149  O O   . GLU A 18  ? 0.15518 0.30927 0.36829 -0.05598 -0.04196 0.07167  16  GLU A O   
150  C CB  . GLU A 18  ? 0.13526 0.38945 0.41615 -0.02183 -0.03702 0.06218  16  GLU A CB  
151  C CG  . GLU A 18  ? 0.17309 0.49027 0.50465 -0.02319 -0.02357 0.06798  16  GLU A CG  
152  C CD  . GLU A 18  ? 0.20078 0.54034 0.55403 -0.00671 -0.04019 0.05754  16  GLU A CD  
153  O OE1 . GLU A 18  ? 0.18770 0.49969 0.52099 0.00291  -0.06317 0.04989  16  GLU A OE1 
154  O OE2 . GLU A 18  ? 0.15043 0.53369 0.53600 -0.00225 -0.03038 0.05606  16  GLU A OE2 
155  N N   . ILE A 19  ? 0.13819 0.27406 0.30093 -0.01486 -0.03898 0.05181  17  ILE A N   
156  C CA  . ILE A 19  ? 0.14559 0.23428 0.26981 -0.01686 -0.05099 0.04610  17  ILE A CA  
157  C C   . ILE A 19  ? 0.19688 0.27005 0.30351 -0.02785 -0.03544 0.05700  17  ILE A C   
158  O O   . ILE A 19  ? 0.16191 0.20846 0.26414 -0.03957 -0.04647 0.05992  17  ILE A O   
159  C CB  . ILE A 19  ? 0.15008 0.21631 0.23276 0.00474  -0.05428 0.03430  17  ILE A CB  
160  C CG1 . ILE A 19  ? 0.17460 0.25354 0.27061 0.01495  -0.07413 0.02645  17  ILE A CG1 
161  C CG2 . ILE A 19  ? 0.17623 0.20266 0.21793 0.00428  -0.05927 0.02921  17  ILE A CG2 
162  C CD1 . ILE A 19  ? 0.18039 0.24583 0.24099 0.03625  -0.07207 0.02179  17  ILE A CD1 
163  N N   . ALA A 20  ? 0.13876 0.22747 0.23399 -0.02298 -0.01056 0.06258  18  ALA A N   
164  C CA  . ALA A 20  ? 0.21086 0.29464 0.29012 -0.03399 0.00478  0.07536  18  ALA A CA  
165  C C   . ALA A 20  ? 0.21172 0.30747 0.32472 -0.05815 0.00227  0.09340  18  ALA A C   
166  O O   . ALA A 20  ? 0.19971 0.26922 0.30085 -0.06909 -0.00243 0.10407  18  ALA A O   
167  C CB  . ALA A 20  ? 0.20581 0.31508 0.27397 -0.02527 0.03127  0.07482  18  ALA A CB  
168  N N   . GLU A 21  ? 0.15758 0.29475 0.31445 -0.06725 0.00622  0.09930  19  GLU A N   
169  C CA  . GLU A 21  ? 0.17792 0.32686 0.36640 -0.09254 0.00421  0.11694  19  GLU A CA  
170  C C   . GLU A 21  ? 0.20492 0.31174 0.40112 -0.10599 -0.02399 0.11695  19  GLU A C   
171  O O   . GLU A 21  ? 0.22716 0.31153 0.41846 -0.11804 -0.02633 0.12701  19  GLU A O   
172  C CB  . GLU A 21  ? 0.18043 0.37834 0.41071 -0.09591 0.00940  0.11586  19  GLU A CB  
173  C CG  . GLU A 21  ? 0.24333 0.44965 0.49217 -0.11693 0.01111  0.12820  19  GLU A CG  
174  C CD  . GLU A 21  ? 0.21548 0.47486 0.50647 -0.11931 0.01651  0.12532  19  GLU A CD  
175  O OE1 . GLU A 21  ? 0.30157 0.58319 0.60872 -0.10319 0.01199  0.11255  19  GLU A OE1 
176  O OE2 . GLU A 21  ? 0.24241 0.52139 0.55072 -0.13592 0.02401  0.13585  19  GLU A OE2 
177  N N   . ALA A 22  ? 0.19256 0.28112 0.38564 -0.09403 -0.04540 0.09652  20  ALA A N   
178  C CA  . ALA A 22  ? 0.21670 0.26515 0.41434 -0.10292 -0.07402 0.08792  20  ALA A CA  
179  C C   . ALA A 22  ? 0.22829 0.22380 0.38232 -0.09374 -0.07833 0.08439  20  ALA A C   
180  O O   . ALA A 22  ? 0.25895 0.21660 0.41834 -0.10589 -0.09460 0.08674  20  ALA A O   
181  C CB  . ALA A 22  ? 0.21095 0.26437 0.41218 -0.08965 -0.09405 0.06502  20  ALA A CB  
182  N N   . ALA A 23  ? 0.27100 0.26340 0.38428 -0.07236 -0.06485 0.07828  21  ALA A N   
183  C CA  . ALA A 23  ? 0.24802 0.19885 0.32106 -0.05904 -0.07111 0.07016  21  ALA A CA  
184  C C   . ALA A 23  ? 0.23018 0.17578 0.27891 -0.05841 -0.05347 0.08668  21  ALA A C   
185  O O   . ALA A 23  ? 0.30701 0.21746 0.33947 -0.05525 -0.06254 0.08830  21  ALA A O   
186  C CB  . ALA A 23  ? 0.25791 0.20767 0.29977 -0.03593 -0.07386 0.04903  21  ALA A CB  
187  N N   . MET A 24  ? 0.25616 0.36500 0.35542 -0.04559 0.09202  -0.01881 22  MET A N   
188  C CA  . MET A 24  ? 0.25225 0.39420 0.36338 -0.06089 0.08889  0.00116  22  MET A CA  
189  C C   . MET A 24  ? 0.16412 0.32958 0.29177 -0.06147 0.09386  0.02392  22  MET A C   
190  O O   . MET A 24  ? 0.17090 0.33101 0.26613 -0.05692 0.10184  0.01488  22  MET A O   
191  C CB  . MET A 24  ? 0.29473 0.41838 0.36107 -0.07776 0.09192  -0.02287 22  MET A CB  
192  C CG  . MET A 24  ? 0.28899 0.43216 0.34690 -0.10314 0.08586  -0.01274 22  MET A CG  
193  S SD  . MET A 24  ? 0.35471 0.47162 0.33208 -0.13043 0.09408  -0.05045 22  MET A SD  
194  C CE  . MET A 24  ? 0.50980 0.58192 0.48886 -0.10325 0.10084  -0.07088 22  MET A CE  
195  N N   . PRO A 25  ? 0.16939 0.34502 0.33767 -0.07372 0.09211  0.03346  23  PRO A N   
196  C CA  . PRO A 25  ? 0.17783 0.37953 0.33366 -0.08565 0.09050  0.04267  23  PRO A CA  
197  C C   . PRO A 25  ? 0.24957 0.45918 0.34523 -0.10463 0.08689  0.04356  23  PRO A C   
198  O O   . PRO A 25  ? 0.24846 0.45634 0.31834 -0.12348 0.07881  0.03532  23  PRO A O   
199  C CB  . PRO A 25  ? 0.21994 0.45231 0.40996 -0.09841 0.06984  0.06233  23  PRO A CB  
200  C CG  . PRO A 25  ? 0.32942 0.55081 0.53561 -0.10550 0.06432  0.05272  23  PRO A CG  
201  C CD  . PRO A 25  ? 0.22043 0.39925 0.41896 -0.08542 0.08261  0.02650  23  PRO A CD  
202  N N   . PHE A 26  ? 0.27593 0.49103 0.33817 -0.10441 0.09439  0.04669  24  PHE A N   
203  C CA  . PHE A 26  ? 0.31001 0.53929 0.29070 -0.13466 0.09199  0.03743  24  PHE A CA  
204  C C   . PHE A 26  ? 0.31695 0.51019 0.25608 -0.13644 0.09967  0.00308  24  PHE A C   
205  O O   . PHE A 26  ? 0.34307 0.54068 0.23612 -0.17469 0.08960  -0.00821 24  PHE A O   
206  C CB  . PHE A 26  ? 0.48379 0.76368 0.43911 -0.18313 0.06318  0.06374  24  PHE A CB  
207  C CG  . PHE A 26  ? 0.35668 0.67307 0.36002 -0.17867 0.04900  0.10249  24  PHE A CG  
208  C CD1 . PHE A 26  ? 0.41572 0.73371 0.49811 -0.16094 0.03852  0.11843  24  PHE A CD1 
209  C CD2 . PHE A 26  ? 0.52033 0.85464 0.48888 -0.18590 0.04995  0.11635  24  PHE A CD2 
210  C CE1 . PHE A 26  ? 0.42693 0.76831 0.55024 -0.15365 0.02639  0.14893  24  PHE A CE1 
211  C CE2 . PHE A 26  ? 0.43295 0.80067 0.44806 -0.18078 0.03610  0.15311  24  PHE A CE2 
212  C CZ  . PHE A 26  ? 0.33089 0.70290 0.42420 -0.16403 0.02347  0.17029  24  PHE A CZ  
213  N N   . PRO A 27  ? 0.33242 0.48569 0.28525 -0.09730 0.11262  -0.01031 25  PRO A N   
214  C CA  . PRO A 27  ? 0.34209 0.46335 0.27883 -0.09688 0.11317  -0.03721 25  PRO A CA  
215  C C   . PRO A 27  ? 0.40378 0.49938 0.27751 -0.11446 0.11760  -0.05980 25  PRO A C   
216  O O   . PRO A 27  ? 0.47212 0.56394 0.31123 -0.11388 0.12282  -0.06016 25  PRO A O   
217  C CB  . PRO A 27  ? 0.30511 0.40823 0.27097 -0.07068 0.11752  -0.04484 25  PRO A CB  
218  C CG  . PRO A 27  ? 0.27562 0.39331 0.24521 -0.05804 0.12389  -0.03123 25  PRO A CG  
219  C CD  . PRO A 27  ? 0.30071 0.45267 0.28481 -0.07000 0.12081  -0.00479 25  PRO A CD  
220  N N   . TRP A 28  ? 0.44298 0.51745 0.30387 -0.13077 0.11579  -0.07789 26  TRP A N   
221  C CA  . TRP A 28  ? 0.50557 0.54479 0.32212 -0.13738 0.12050  -0.09618 26  TRP A CA  
222  C C   . TRP A 28  ? 0.48509 0.50166 0.30796 -0.11259 0.13205  -0.10284 26  TRP A C   
223  O O   . TRP A 28  ? 0.52661 0.54059 0.39098 -0.09472 0.13411  -0.09964 26  TRP A O   
224  C CB  . TRP A 28  ? 0.56325 0.58189 0.38507 -0.14947 0.11936  -0.10809 26  TRP A CB  
225  C CG  . TRP A 28  ? 0.51925 0.55426 0.31762 -0.19412 0.11120  -0.11120 26  TRP A CG  
226  C CD1 . TRP A 28  ? 0.50782 0.58329 0.28487 -0.22729 0.09779  -0.09804 26  TRP A CD1 
227  C CD2 . TRP A 28  ? 0.47981 0.49634 0.27485 -0.21076 0.11104  -0.12075 26  TRP A CD2 
228  N NE1 . TRP A 28  ? 0.50078 0.58424 0.25911 -0.26663 0.08462  -0.09824 26  TRP A NE1 
229  C CE2 . TRP A 28  ? 0.51756 0.56133 0.28700 -0.25393 0.09627  -0.11478 26  TRP A CE2 
230  C CE3 . TRP A 28  ? 0.43051 0.41378 0.24086 -0.19183 0.11887  -0.12774 26  TRP A CE3 
231  C CZ2 . TRP A 28  ? 0.48982 0.52081 0.25003 -0.27056 0.09031  -0.11834 26  TRP A CZ2 
232  C CZ3 . TRP A 28  ? 0.49067 0.46411 0.29135 -0.21111 0.11749  -0.13260 26  TRP A CZ3 
233  C CH2 . TRP A 28  ? 0.51855 0.51255 0.29370 -0.24714 0.10393  -0.12969 26  TRP A CH2 
234  N N   . SER A 29  ? 0.56039 0.55971 0.33963 -0.11892 0.13931  -0.11400 27  SER A N   
235  C CA  . SER A 29  ? 0.56812 0.54493 0.34917 -0.10452 0.15294  -0.12366 27  SER A CA  
236  C C   . SER A 29  ? 0.57633 0.52559 0.37302 -0.10148 0.15750  -0.13254 27  SER A C   
237  O O   . SER A 29  ? 0.61596 0.55890 0.41099 -0.11289 0.15230  -0.13514 27  SER A O   
238  C CB  . SER A 29  ? 0.61890 0.58453 0.34800 -0.11558 0.16123  -0.13497 27  SER A CB  
239  O OG  . SER A 29  ? 0.79797 0.74225 0.48952 -0.13589 0.16114  -0.14956 27  SER A OG  
240  N N   . GLU A 30  ? 0.55789 0.49223 0.37031 -0.08640 0.16721  -0.13502 28  GLU A N   
241  C CA  . GLU A 30  ? 0.64217 0.55086 0.46276 -0.08404 0.17353  -0.14129 28  GLU A CA  
242  C C   . GLU A 30  ? 0.66669 0.55342 0.44674 -0.10063 0.17976  -0.15744 28  GLU A C   
243  O O   . GLU A 30  ? 0.72225 0.59396 0.50619 -0.10457 0.18021  -0.16054 28  GLU A O   
244  C CB  . GLU A 30  ? 0.62666 0.52435 0.46183 -0.06846 0.18352  -0.14165 28  GLU A CB  
245  C CG  . GLU A 30  ? 0.47809 0.36267 0.33983 -0.06049 0.18451  -0.13722 28  GLU A CG  
246  C CD  . GLU A 30  ? 0.50962 0.38628 0.38433 -0.04671 0.19321  -0.13664 28  GLU A CD  
247  O OE1 . GLU A 30  ? 0.83767 0.70305 0.69099 -0.04736 0.20573  -0.14853 28  GLU A OE1 
248  O OE2 . GLU A 30  ? 0.54152 0.42346 0.44635 -0.03709 0.18778  -0.12484 28  GLU A OE2 
249  N N   . LYS A 31  ? 0.62703 0.51103 0.36582 -0.11197 0.18477  -0.16807 29  LYS A N   
250  C CA  . LYS A 31  ? 0.68459 0.54648 0.38133 -0.13124 0.19008  -0.18534 29  LYS A CA  
251  C C   . LYS A 31  ? 0.66976 0.53942 0.35305 -0.14910 0.17547  -0.18325 29  LYS A C   
252  O O   . LYS A 31  ? 0.71351 0.56254 0.37824 -0.16133 0.17783  -0.19507 29  LYS A O   
253  C CB  . LYS A 31  ? 0.72741 0.58507 0.38141 -0.14200 0.19908  -0.19716 29  LYS A CB  
254  C CG  . LYS A 31  ? 0.80202 0.62899 0.41979 -0.15770 0.21260  -0.21941 29  LYS A CG  
255  C CD  . LYS A 31  ? 0.87988 0.70863 0.45151 -0.18581 0.20224  -0.22647 29  LYS A CD  
256  C CE  . LYS A 31  ? 0.93548 0.73594 0.46417 -0.20500 0.21789  -0.25108 29  LYS A CE  
257  N NZ  . LYS A 31  ? 0.98686 0.75850 0.53846 -0.19254 0.23695  -0.26286 29  LYS A NZ  
258  N N   . PHE A 32  ? 0.62314 0.52243 0.31740 -0.15124 0.16062  -0.16838 30  PHE A N   
259  C CA  . PHE A 32  ? 0.65867 0.56701 0.34467 -0.16894 0.14560  -0.16500 30  PHE A CA  
260  C C   . PHE A 32  ? 0.72010 0.61618 0.43778 -0.16365 0.14640  -0.16428 30  PHE A C   
261  O O   . PHE A 32  ? 0.72561 0.61471 0.42858 -0.17947 0.13946  -0.16901 30  PHE A O   
262  C CB  . PHE A 32  ? 0.73620 0.68151 0.43519 -0.17114 0.13062  -0.14688 30  PHE A CB  
263  C CG  . PHE A 32  ? 0.83549 0.79596 0.48691 -0.19519 0.12431  -0.14546 30  PHE A CG  
264  C CD1 . PHE A 32  ? 0.73710 0.67990 0.34712 -0.19711 0.13120  -0.15786 30  PHE A CD1 
265  C CD2 . PHE A 32  ? 0.77609 0.77238 0.42343 -0.22146 0.11076  -0.13017 30  PHE A CD2 
266  C CE1 . PHE A 32  ? 0.84944 0.80595 0.41149 -0.22352 0.12529  -0.15545 30  PHE A CE1 
267  C CE2 . PHE A 32  ? 0.77358 0.78827 0.37426 -0.24845 0.10039  -0.12287 30  PHE A CE2 
268  C CZ  . PHE A 32  ? 0.78365 0.77615 0.33984 -0.24906 0.10818  -0.13619 30  PHE A CZ  
269  N N   . PHE A 33  ? 0.63880 0.53321 0.39892 -0.14298 0.15331  -0.15705 31  PHE A N   
270  C CA  . PHE A 33  ? 0.51416 0.39761 0.30144 -0.13884 0.15491  -0.15409 31  PHE A CA  
271  C C   . PHE A 33  ? 0.59732 0.44790 0.36488 -0.14021 0.16645  -0.16787 31  PHE A C   
272  O O   . PHE A 33  ? 0.69687 0.53621 0.46781 -0.14528 0.16607  -0.16932 31  PHE A O   
273  C CB  . PHE A 33  ? 0.55264 0.44667 0.38750 -0.12006 0.15569  -0.14021 31  PHE A CB  
274  C CG  . PHE A 33  ? 0.44379 0.36782 0.30767 -0.12034 0.14458  -0.12789 31  PHE A CG  
275  C CD1 . PHE A 33  ? 0.46949 0.40368 0.35093 -0.13082 0.13805  -0.12329 31  PHE A CD1 
276  C CD2 . PHE A 33  ? 0.41077 0.35290 0.28475 -0.11043 0.14177  -0.12191 31  PHE A CD2 
277  C CE1 . PHE A 33  ? 0.44677 0.40741 0.35829 -0.13214 0.12849  -0.11476 31  PHE A CE1 
278  C CE2 . PHE A 33  ? 0.40176 0.37014 0.30317 -0.10965 0.13180  -0.11217 31  PHE A CE2 
279  C CZ  . PHE A 33  ? 0.35326 0.33020 0.27345 -0.12074 0.12448  -0.10990 31  PHE A CZ  
280  N N   . TYR A 34  ? 0.74210 0.57689 0.48961 -0.13648 0.17792  -0.17890 32  TYR A N   
281  C CA  . TYR A 34  ? 0.71214 0.51583 0.43596 -0.14287 0.18954  -0.19583 32  TYR A CA  
282  C C   . TYR A 34  ? 0.87982 0.67707 0.56511 -0.16687 0.18353  -0.20811 32  TYR A C   
283  O O   . TYR A 34  ? 0.81379 0.58921 0.48984 -0.17382 0.18802  -0.21846 32  TYR A O   
284  C CB  . TYR A 34  ? 0.89003 0.67876 0.60109 -0.13686 0.20513  -0.20722 32  TYR A CB  
285  C CG  . TYR A 34  ? 0.66838 0.46059 0.41634 -0.11425 0.21040  -0.19625 32  TYR A CG  
286  C CD1 . TYR A 34  ? 0.75462 0.53771 0.52999 -0.10288 0.21248  -0.18946 32  TYR A CD1 
287  C CD2 . TYR A 34  ? 0.84512 0.64945 0.59756 -0.10552 0.21309  -0.19292 32  TYR A CD2 
288  C CE1 . TYR A 34  ? 0.71723 0.50514 0.52328 -0.08457 0.21485  -0.17866 32  TYR A CE1 
289  C CE2 . TYR A 34  ? 0.66705 0.47515 0.45309 -0.08626 0.21613  -0.18275 32  TYR A CE2 
290  C CZ  . TYR A 34  ? 0.71518 0.51531 0.52688 -0.07667 0.21631  -0.17570 32  TYR A CZ  
291  O OH  . TYR A 34  ? 0.73695 0.54161 0.57802 -0.06023 0.21742  -0.16543 32  TYR A OH  
292  N N   . ASP A 35  ? 0.87921 0.69598 0.54153 -0.18054 0.17206  -0.20639 33  ASP A N   
293  C CA  . ASP A 35  ? 0.89873 0.71117 0.51950 -0.20656 0.16339  -0.21758 33  ASP A CA  
294  C C   . ASP A 35  ? 0.92639 0.73682 0.55899 -0.21369 0.15307  -0.21467 33  ASP A C   
295  O O   . ASP A 35  ? 0.92607 0.72001 0.53107 -0.23144 0.15136  -0.22856 33  ASP A O   
296  C CB  . ASP A 35  ? 0.86121 0.70042 0.45738 -0.22008 0.14897  -0.21073 33  ASP A CB  
297  C CG  . ASP A 35  ? 0.91001 0.74506 0.47428 -0.22331 0.15992  -0.22011 33  ASP A CG  
298  O OD1 . ASP A 35  ? 0.91801 0.72771 0.47777 -0.21746 0.17935  -0.23480 33  ASP A OD1 
299  O OD2 . ASP A 35  ? 1.00395 0.86215 0.54815 -0.23248 0.14919  -0.21180 33  ASP A OD2 
300  N N   . CYS A 36  ? 0.97783 0.80506 0.65151 -0.20154 0.14670  -0.19766 34  CYS A N   
301  C CA  . CYS A 36  ? 0.89299 0.71727 0.58025 -0.20739 0.13945  -0.19513 34  CYS A CA  
302  C C   . CYS A 36  ? 0.75457 0.55837 0.46700 -0.19209 0.15322  -0.19516 34  CYS A C   
303  O O   . CYS A 36  ? 0.84653 0.65323 0.58186 -0.19030 0.14993  -0.18750 34  CYS A O   
304  C CB  . CYS A 36  ? 0.79061 0.64597 0.50469 -0.20877 0.12422  -0.17808 34  CYS A CB  
305  S SG  . CYS A 36  ? 0.73317 0.62052 0.47241 -0.19718 0.12344  -0.16241 34  CYS A SG  
306  N N   . LEU A 37  ? 0.87941 0.66292 0.58743 -0.18187 0.16846  -0.20330 35  LEU A N   
307  C CA  . LEU A 37  ? 0.89885 0.65913 0.62061 -0.17291 0.17920  -0.20593 35  LEU A CA  
308  C C   . LEU A 37  ? 0.96119 0.69706 0.65647 -0.18906 0.18082  -0.22326 35  LEU A C   
309  O O   . LEU A 37  ? 0.99602 0.71324 0.70274 -0.18385 0.18760  -0.22493 35  LEU A O   
310  C CB  . LEU A 37  ? 0.86420 0.61122 0.59402 -0.15638 0.19409  -0.20830 35  LEU A CB  
311  C CG  . LEU A 37  ? 0.69726 0.46337 0.46666 -0.13752 0.19193  -0.18784 35  LEU A CG  
312  C CD1 . LEU A 37  ? 0.75875 0.51742 0.53655 -0.12174 0.20286  -0.18861 35  LEU A CD1 
313  C CD2 . LEU A 37  ? 0.68723 0.45102 0.47961 -0.13294 0.19074  -0.17771 35  LEU A CD2 
314  N N   . LYS A 38  ? 0.84117 0.57771 0.50143 -0.20963 0.17366  -0.23558 36  LYS A N   
315  C CA  . LYS A 38  ? 0.92594 0.63771 0.55781 -0.22703 0.17709  -0.25574 36  LYS A CA  
316  C C   . LYS A 38  ? 0.92919 0.64218 0.56940 -0.23623 0.16438  -0.25249 36  LYS A C   
317  O O   . LYS A 38  ? 0.83485 0.56710 0.50320 -0.22872 0.15493  -0.23503 36  LYS A O   
318  C CB  . LYS A 38  ? 1.06401 0.77731 0.65236 -0.24776 0.17453  -0.27042 36  LYS A CB  
319  C CG  . LYS A 38  ? 1.04806 0.79285 0.62531 -0.26001 0.15290  -0.25909 36  LYS A CG  
320  C CD  . LYS A 38  ? 0.97155 0.71791 0.50124 -0.28094 0.15168  -0.27238 36  LYS A CD  
321  C CE  . LYS A 38  ? 0.99255 0.75832 0.49796 -0.30651 0.12635  -0.26947 36  LYS A CE  
322  N NZ  . LYS A 38  ? 1.11182 0.88427 0.56880 -0.32854 0.12266  -0.27823 36  LYS A NZ  
323  N N   . SER A 39  ? 1.15600 0.84788 0.77306 -0.25333 0.16546  -0.27071 37  SER A N   
324  C CA  . SER A 39  ? 1.15446 0.84091 0.78148 -0.26109 0.15644  -0.27073 37  SER A CA  
325  C C   . SER A 39  ? 1.05964 0.77586 0.69448 -0.27034 0.13283  -0.25708 37  SER A C   
326  O O   . SER A 39  ? 1.12800 0.86543 0.74691 -0.27972 0.12061  -0.25350 37  SER A O   
327  C CB  . SER A 39  ? 1.31553 0.97659 0.91289 -0.28161 0.16037  -0.29509 37  SER A CB  
328  O OG  . SER A 39  ? 1.41816 1.05242 1.00630 -0.27623 0.18315  -0.31065 37  SER A OG  
329  N N   . ASN A 40  ? 1.00504 0.72267 0.66616 -0.26804 0.12645  -0.24914 38  ASN A N   
330  C CA  . ASN A 40  ? 0.89717 0.64039 0.57757 -0.27482 0.10539  -0.23595 38  ASN A CA  
331  C C   . ASN A 40  ? 0.75534 0.52861 0.46028 -0.26126 0.10154  -0.21595 38  ASN A C   
332  O O   . ASN A 40  ? 0.72755 0.52421 0.45168 -0.26748 0.08337  -0.20495 38  ASN A O   
333  C CB  . ASN A 40  ? 0.89766 0.65097 0.55304 -0.30161 0.08298  -0.24357 38  ASN A CB  
334  C CG  . ASN A 40  ? 1.05035 0.77755 0.67967 -0.31921 0.08512  -0.26530 38  ASN A CG  
335  O OD1 . ASN A 40  ? 0.94449 0.65711 0.59007 -0.32010 0.08623  -0.26910 38  ASN A OD1 
336  N ND2 . ASN A 40  ? 1.04029 0.76201 0.62842 -0.33479 0.08631  -0.28042 38  ASN A ND2 
337  N N   . TYR A 41  ? 0.40924 0.31895 0.39967 -0.06997 -0.11837 -0.13807 39  TYR A N   
338  C CA  . TYR A 41  ? 0.42273 0.36687 0.41756 -0.06204 -0.09663 -0.11693 39  TYR A CA  
339  C C   . TYR A 41  ? 0.43979 0.36445 0.45384 -0.06587 -0.09421 -0.09894 39  TYR A C   
340  O O   . TYR A 41  ? 0.43737 0.32407 0.45612 -0.05939 -0.10309 -0.10825 39  TYR A O   
341  C CB  . TYR A 41  ? 0.53480 0.49729 0.51304 -0.03962 -0.08009 -0.12925 39  TYR A CB  
342  C CG  . TYR A 41  ? 0.59518 0.58561 0.54581 -0.03815 -0.07894 -0.13881 39  TYR A CG  
343  C CD1 . TYR A 41  ? 0.39208 0.41517 0.33617 -0.04103 -0.07225 -0.11783 39  TYR A CD1 
344  C CD2 . TYR A 41  ? 0.64006 0.62227 0.56907 -0.03321 -0.08685 -0.16945 39  TYR A CD2 
345  C CE1 . TYR A 41  ? 0.35455 0.39896 0.26877 -0.04142 -0.07605 -0.12267 39  TYR A CE1 
346  C CE2 . TYR A 41  ? 0.68156 0.69012 0.57814 -0.03431 -0.08714 -0.17697 39  TYR A CE2 
347  C CZ  . TYR A 41  ? 0.59811 0.63669 0.48618 -0.03931 -0.08245 -0.15114 39  TYR A CZ  
348  O OH  . TYR A 41  ? 0.68082 0.74113 0.53239 -0.04193 -0.08720 -0.15512 39  TYR A OH  
349  N N   . TYR A 42  ? 0.33275 0.28242 0.35769 -0.07566 -0.08473 -0.07493 40  TYR A N   
350  C CA  . TYR A 42  ? 0.34739 0.28168 0.38458 -0.08406 -0.08353 -0.05677 40  TYR A CA  
351  C C   . TYR A 42  ? 0.27633 0.24093 0.31776 -0.07327 -0.06405 -0.04354 40  TYR A C   
352  O O   . TYR A 42  ? 0.25707 0.25685 0.29914 -0.07141 -0.05570 -0.03952 40  TYR A O   
353  C CB  . TYR A 42  ? 0.34319 0.27814 0.38862 -0.11468 -0.09320 -0.04232 40  TYR A CB  
354  C CG  . TYR A 42  ? 0.45074 0.35635 0.49153 -0.12507 -0.10975 -0.05236 40  TYR A CG  
355  C CD1 . TYR A 42  ? 0.53875 0.39927 0.57600 -0.12573 -0.11953 -0.04894 40  TYR A CD1 
356  C CD2 . TYR A 42  ? 0.43522 0.36019 0.47489 -0.13155 -0.11570 -0.06424 40  TYR A CD2 
357  C CE1 . TYR A 42  ? 0.59883 0.43191 0.63218 -0.13374 -0.13460 -0.05731 40  TYR A CE1 
358  C CE2 . TYR A 42  ? 0.45396 0.35361 0.48960 -0.14025 -0.12925 -0.07419 40  TYR A CE2 
359  C CZ  . TYR A 42  ? 0.61501 0.46803 0.64781 -0.14198 -0.13831 -0.07050 40  TYR A CZ  
360  O OH  . TYR A 42  ? 0.64869 0.47451 0.67821 -0.15137 -0.15390 -0.07978 40  TYR A OH  
361  N N   . GLY A 43  ? 0.30769 0.25585 0.35337 -0.06569 -0.06021 -0.03715 41  GLY A N   
362  C CA  . GLY A 43  ? 0.22983 0.20138 0.27969 -0.05662 -0.04419 -0.02604 41  GLY A CA  
363  C C   . GLY A 43  ? 0.23513 0.19305 0.29044 -0.06601 -0.04594 -0.01016 41  GLY A C   
364  O O   . GLY A 43  ? 0.29527 0.21790 0.34966 -0.07442 -0.06076 -0.00731 41  GLY A O   
365  N N   . TRP A 44  ? 0.22495 0.20850 0.28369 -0.06472 -0.03314 0.00013  42  TRP A N   
366  C CA  . TRP A 44  ? 0.22427 0.20340 0.28346 -0.07225 -0.03185 0.01407  42  TRP A CA  
367  C C   . TRP A 44  ? 0.22046 0.21459 0.28409 -0.05632 -0.01995 0.01508  42  TRP A C   
368  O O   . TRP A 44  ? 0.20000 0.21526 0.26593 -0.04601 -0.01097 0.01039  42  TRP A O   
369  C CB  . TRP A 44  ? 0.17215 0.17509 0.23047 -0.09466 -0.02850 0.02342  42  TRP A CB  
370  C CG  . TRP A 44  ? 0.21650 0.20623 0.26878 -0.11390 -0.03899 0.02594  42  TRP A CG  
371  C CD1 . TRP A 44  ? 0.38092 0.34803 0.41899 -0.12510 -0.04608 0.03725  42  TRP A CD1 
372  C CD2 . TRP A 44  ? 0.28504 0.28625 0.34273 -0.12109 -0.04308 0.01759  42  TRP A CD2 
373  N NE1 . TRP A 44  ? 0.30365 0.26683 0.33943 -0.13979 -0.05311 0.03730  42  TRP A NE1 
374  C CE2 . TRP A 44  ? 0.31054 0.29402 0.35954 -0.13693 -0.05113 0.02407  42  TRP A CE2 
375  C CE3 . TRP A 44  ? 0.23826 0.26301 0.30473 -0.11295 -0.04187 0.00542  42  TRP A CE3 
376  C CZ2 . TRP A 44  ? 0.34329 0.33171 0.39673 -0.14822 -0.05784 0.01807  42  TRP A CZ2 
377  C CZ3 . TRP A 44  ? 0.27603 0.30647 0.34579 -0.12566 -0.05137 -0.00105 42  TRP A CZ3 
378  C CH2 . TRP A 44  ? 0.32909 0.34188 0.39408 -0.14165 -0.05745 0.00454  42  TRP A CH2 
379  N N   . VAL A 45  ? 0.19926 0.18084 0.26278 -0.05692 -0.02255 0.02326  43  VAL A N   
380  C CA  . VAL A 45  ? 0.14751 0.14147 0.21649 -0.04546 -0.01379 0.02458  43  VAL A CA  
381  C C   . VAL A 45  ? 0.21288 0.21055 0.27496 -0.05802 -0.01395 0.03528  43  VAL A C   
382  O O   . VAL A 45  ? 0.18958 0.17312 0.24097 -0.07464 -0.02304 0.04426  43  VAL A O   
383  C CB  . VAL A 45  ? 0.20033 0.18156 0.27941 -0.03033 -0.01728 0.01942  43  VAL A CB  
384  C CG1 . VAL A 45  ? 0.21157 0.19990 0.29454 -0.01762 -0.01231 0.00461  43  VAL A CG1 
385  C CG2 . VAL A 45  ? 0.23319 0.18325 0.31307 -0.03359 -0.03483 0.02411  43  VAL A CG2 
386  N N   . MET A 46  ? 0.17655 0.19240 0.24167 -0.05237 -0.00495 0.03433  44  MET A N   
387  C CA  . MET A 46  ? 0.18151 0.20254 0.23794 -0.06142 -0.00465 0.04000  44  MET A CA  
388  C C   . MET A 46  ? 0.23900 0.24784 0.30063 -0.05220 -0.00952 0.04228  44  MET A C   
389  O O   . MET A 46  ? 0.19212 0.20538 0.26687 -0.03915 -0.00497 0.03723  44  MET A O   
390  C CB  . MET A 46  ? 0.14910 0.19972 0.20747 -0.06074 0.00642  0.03212  44  MET A CB  
391  C CG  . MET A 46  ? 0.23464 0.29260 0.27911 -0.07174 0.00706  0.03423  44  MET A CG  
392  S SD  . MET A 46  ? 0.28945 0.38206 0.33952 -0.06561 0.01861  0.01676  44  MET A SD  
393  C CE  . MET A 46  ? 0.19818 0.32147 0.25093 -0.07700 0.02577  0.01235  44  MET A CE  
394  N N   . GLU A 47  ? 0.21567 0.21059 0.26654 -0.06130 -0.02019 0.05132  45  GLU A N   
395  C CA  . GLU A 47  ? 0.19751 0.18683 0.25501 -0.05426 -0.02677 0.05290  45  GLU A CA  
396  C C   . GLU A 47  ? 0.24940 0.25114 0.29087 -0.06385 -0.02404 0.05327  45  GLU A C   
397  O O   . GLU A 47  ? 0.25568 0.26037 0.27368 -0.08109 -0.02546 0.05928  45  GLU A O   
398  C CB  . GLU A 47  ? 0.26350 0.22589 0.32295 -0.05376 -0.04650 0.06128  45  GLU A CB  
399  C CG  . GLU A 47  ? 0.27901 0.24124 0.34904 -0.04707 -0.05559 0.06242  45  GLU A CG  
400  C CD  . GLU A 47  ? 0.34361 0.27955 0.41742 -0.04488 -0.07979 0.07073  45  GLU A CD  
401  O OE1 . GLU A 47  ? 0.42261 0.33714 0.50040 -0.04149 -0.08933 0.07117  45  GLU A OE1 
402  O OE2 . GLU A 47  ? 0.53216 0.46570 0.60486 -0.04629 -0.09276 0.07645  45  GLU A OE2 
403  N N   . SER A 48  ? 0.17853 0.18881 0.23102 -0.05483 -0.02005 0.04595  46  SER A N   
404  C CA  . SER A 48  ? 0.19979 0.21842 0.23869 -0.06092 -0.02029 0.04144  46  SER A CA  
405  C C   . SER A 48  ? 0.20849 0.22020 0.26230 -0.05412 -0.02890 0.04119  46  SER A C   
406  O O   . SER A 48  ? 0.17280 0.18416 0.25030 -0.04419 -0.02672 0.04057  46  SER A O   
407  C CB  . SER A 48  ? 0.18942 0.22773 0.22944 -0.05703 -0.00668 0.02684  46  SER A CB  
408  O OG  . SER A 48  ? 0.29339 0.34152 0.32020 -0.06087 -0.00648 0.01608  46  SER A OG  
409  N N   . ASP A 49  ? 0.18576 0.19547 0.22528 -0.06173 -0.03893 0.04181  47  ASP A N   
410  C CA  . ASP A 49  ? 0.15257 0.15831 0.20988 -0.05750 -0.04997 0.04181  47  ASP A CA  
411  C C   . ASP A 49  ? 0.19637 0.19810 0.28103 -0.04892 -0.05754 0.04937  47  ASP A C   
412  O O   . ASP A 49  ? 0.20684 0.21774 0.31989 -0.04218 -0.05576 0.04619  47  ASP A O   
413  C CB  . ASP A 49  ? 0.17463 0.18522 0.24641 -0.05216 -0.04204 0.03046  47  ASP A CB  
414  C CG  . ASP A 49  ? 0.24957 0.26287 0.30077 -0.05613 -0.04024 0.01645  47  ASP A CG  
415  O OD1 . ASP A 49  ? 0.23757 0.25378 0.26244 -0.06598 -0.04685 0.01540  47  ASP A OD1 
416  O OD2 . ASP A 49  ? 0.22258 0.23396 0.28390 -0.04923 -0.03447 0.00572  47  ASP A OD2 
417  N N   . HIS A 50  ? 0.20473 0.19433 0.28236 -0.04955 -0.06562 0.05789  48  HIS A N   
418  C CA  . HIS A 50  ? 0.18357 0.16735 0.28828 -0.03807 -0.07806 0.06046  48  HIS A CA  
419  C C   . HIS A 50  ? 0.19584 0.19508 0.32943 -0.02520 -0.06261 0.05072  48  HIS A C   
420  O O   . HIS A 50  ? 0.20227 0.21283 0.36787 -0.01374 -0.06742 0.04546  48  HIS A O   
421  C CB  . HIS A 50  ? 0.22694 0.21442 0.34955 -0.03536 -0.09696 0.06199  48  HIS A CB  
422  C CG  . HIS A 50  ? 0.24833 0.22258 0.33792 -0.04947 -0.11400 0.07149  48  HIS A CG  
423  N ND1 . HIS A 50  ? 0.36203 0.31140 0.43090 -0.05534 -0.13621 0.08602  48  HIS A ND1 
424  C CD2 . HIS A 50  ? 0.30932 0.29026 0.37828 -0.06049 -0.11278 0.06823  48  HIS A CD2 
425  C CE1 . HIS A 50  ? 0.33725 0.28249 0.37118 -0.07133 -0.14692 0.09324  48  HIS A CE1 
426  N NE2 . HIS A 50  ? 0.31156 0.27757 0.34538 -0.07357 -0.13182 0.08004  48  HIS A NE2 
427  N N   . HIS A 51  ? 0.21546 0.21948 0.33900 -0.02684 -0.04482 0.04713  49  HIS A N   
428  C CA  . HIS A 51  ? 0.13939 0.15743 0.28171 -0.01752 -0.03163 0.03975  49  HIS A CA  
429  C C   . HIS A 51  ? 0.16709 0.18142 0.29015 -0.02047 -0.02021 0.03886  49  HIS A C   
430  O O   . HIS A 51  ? 0.15964 0.16839 0.26185 -0.02910 -0.01959 0.04183  49  HIS A O   
431  C CB  . HIS A 51  ? 0.15500 0.19437 0.31620 -0.01816 -0.02302 0.03731  49  HIS A CB  
432  C CG  . HIS A 51  ? 0.18968 0.22577 0.33568 -0.02625 -0.01579 0.03945  49  HIS A CG  
433  N ND1 . HIS A 51  ? 0.14979 0.17510 0.28016 -0.03262 -0.02287 0.03981  49  HIS A ND1 
434  C CD2 . HIS A 51  ? 0.17121 0.21128 0.31504 -0.02793 -0.00494 0.04009  49  HIS A CD2 
435  C CE1 . HIS A 51  ? 0.10649 0.12871 0.23057 -0.03468 -0.01705 0.03725  49  HIS A CE1 
436  N NE2 . HIS A 51  ? 0.19314 0.22121 0.32528 -0.03240 -0.00804 0.03972  49  HIS A NE2 
437  N N   . LEU A 52  ? 0.14987 0.17218 0.28037 -0.01361 -0.01122 0.03284  50  LEU A N   
438  C CA  . LEU A 52  ? 0.14276 0.16287 0.25643 -0.01654 -0.00374 0.03198  50  LEU A CA  
439  C C   . LEU A 52  ? 0.12769 0.15655 0.23626 -0.01926 0.00477  0.03363  50  LEU A C   
440  O O   . LEU A 52  ? 0.16516 0.20288 0.28299 -0.01838 0.00943  0.03492  50  LEU A O   
441  C CB  . LEU A 52  ? 0.20395 0.22771 0.32234 -0.00889 0.00029  0.02358  50  LEU A CB  
442  C CG  . LEU A 52  ? 0.24258 0.24900 0.36726 -0.00332 -0.01258 0.01845  50  LEU A CG  
443  C CD1 . LEU A 52  ? 0.26110 0.27050 0.38613 0.00431  -0.00806 0.00503  50  LEU A CD1 
444  C CD2 . LEU A 52  ? 0.24484 0.22606 0.35274 -0.01479 -0.02571 0.02823  50  LEU A CD2 
445  N N   . VAL A 53  ? 0.14817 0.17572 0.24406 -0.02303 0.00564  0.03317  51  VAL A N   
446  C CA  . VAL A 53  ? 0.18749 0.21866 0.28251 -0.02129 0.00860  0.03194  51  VAL A CA  
447  C C   . VAL A 53  ? 0.16113 0.19810 0.25172 -0.01820 0.01103  0.02937  51  VAL A C   
448  O O   . VAL A 53  ? 0.16214 0.19844 0.25434 -0.01385 0.00919  0.02879  51  VAL A O   
449  C CB  . VAL A 53  ? 0.14973 0.18045 0.24102 -0.02401 0.00546  0.02759  51  VAL A CB  
450  C CG1 . VAL A 53  ? 0.14403 0.16845 0.23852 -0.02808 -0.00060 0.03072  51  VAL A CG1 
451  C CG2 . VAL A 53  ? 0.15693 0.19805 0.23755 -0.02972 0.00738  0.02308  51  VAL A CG2 
452  N N   . GLY A 54  ? 0.16749 0.20724 0.25392 -0.01996 0.01175  0.02781  52  GLY A N   
453  C CA  . GLY A 54  ? 0.18708 0.23514 0.27088 -0.01787 0.01167  0.02479  52  GLY A CA  
454  C C   . GLY A 54  ? 0.18056 0.22700 0.25964 -0.02203 0.01048  0.02232  52  GLY A C   
455  O O   . GLY A 54  ? 0.16062 0.19647 0.23901 -0.02651 0.00784  0.02309  52  GLY A O   
456  N N   . PHE A 55  ? 0.13760 0.19019 0.21278 -0.01999 0.00906  0.01943  53  PHE A N   
457  C CA  . PHE A 55  ? 0.16984 0.21846 0.23991 -0.02430 0.00555  0.01407  53  PHE A CA  
458  C C   . PHE A 55  ? 0.17121 0.23423 0.24065 -0.02594 0.00122  0.01072  53  PHE A C   
459  O O   . PHE A 55  ? 0.12116 0.19562 0.19437 -0.01998 -0.00036 0.01248  53  PHE A O   
460  C CB  . PHE A 55  ? 0.17359 0.21519 0.23780 -0.01802 0.00764  0.00910  53  PHE A CB  
461  C CG  . PHE A 55  ? 0.13851 0.19088 0.19226 -0.01390 0.01123  0.01084  53  PHE A CG  
462  C CD1 . PHE A 55  ? 0.18965 0.24768 0.23093 -0.01481 0.00638  0.00668  53  PHE A CD1 
463  C CD2 . PHE A 55  ? 0.20104 0.25673 0.25514 -0.01237 0.01690  0.01906  53  PHE A CD2 
464  C CE1 . PHE A 55  ? 0.22397 0.28946 0.24886 -0.01391 0.00649  0.01234  53  PHE A CE1 
465  C CE2 . PHE A 55  ? 0.18293 0.24484 0.22176 -0.01383 0.01777  0.02587  53  PHE A CE2 
466  C CZ  . PHE A 55  ? 0.21330 0.27952 0.23529 -0.01448 0.01231  0.02321  53  PHE A CZ  
467  N N   . ILE A 56  ? 0.14561 0.20649 0.21291 -0.03424 -0.00412 0.00553  54  ILE A N   
468  C CA  . ILE A 56  ? 0.16101 0.23822 0.22977 -0.03689 -0.01063 0.00090  54  ILE A CA  
469  C C   . ILE A 56  ? 0.20349 0.26627 0.26185 -0.04211 -0.01753 -0.00718 54  ILE A C   
470  O O   . ILE A 56  ? 0.19562 0.23684 0.25276 -0.04773 -0.01972 -0.00880 54  ILE A O   
471  C CB  . ILE A 56  ? 0.13420 0.23591 0.21961 -0.04696 -0.01064 0.00058  54  ILE A CB  
472  C CG1 . ILE A 56  ? 0.12288 0.24821 0.21715 -0.04745 -0.01911 -0.00556 54  ILE A CG1 
473  C CG2 . ILE A 56  ? 0.18904 0.28188 0.27300 -0.06666 -0.01101 0.00352  54  ILE A CG2 
474  C CD1 . ILE A 56  ? 0.12657 0.28848 0.24352 -0.05805 -0.01718 -0.00965 54  ILE A CD1 
475  N N   . VAL A 57  ? 0.16474 0.23591 0.21460 -0.03960 -0.02396 -0.01301 55  VAL A N   
476  C CA  . VAL A 57  ? 0.20306 0.26102 0.23963 -0.04272 -0.03162 -0.02542 55  VAL A CA  
477  C C   . VAL A 57  ? 0.21049 0.28632 0.25068 -0.05104 -0.04348 -0.02897 55  VAL A C   
478  O O   . VAL A 57  ? 0.18482 0.28108 0.22517 -0.04475 -0.04679 -0.02476 55  VAL A O   
479  C CB  . VAL A 57  ? 0.21400 0.26869 0.22914 -0.03133 -0.02681 -0.03223 55  VAL A CB  
480  C CG1 . VAL A 57  ? 0.27133 0.31375 0.27208 -0.03291 -0.03514 -0.05213 55  VAL A CG1 
481  C CG2 . VAL A 57  ? 0.29588 0.34324 0.31496 -0.02286 -0.01371 -0.02870 55  VAL A CG2 
482  N N   . ILE A 58  ? 0.20848 0.27474 0.25230 -0.06563 -0.05336 -0.03650 56  ILE A N   
483  C CA  . ILE A 58  ? 0.21923 0.30517 0.26861 -0.07580 -0.06663 -0.04197 56  ILE A CA  
484  C C   . ILE A 58  ? 0.24574 0.30859 0.27619 -0.07953 -0.07896 -0.05833 56  ILE A C   
485  O O   . ILE A 58  ? 0.26287 0.29305 0.28311 -0.07633 -0.07814 -0.06684 56  ILE A O   
486  C CB  . ILE A 58  ? 0.21288 0.31890 0.28834 -0.09681 -0.06936 -0.03690 56  ILE A CB  
487  C CG1 . ILE A 58  ? 0.24809 0.31930 0.32034 -0.11474 -0.07250 -0.03504 56  ILE A CG1 
488  C CG2 . ILE A 58  ? 0.19674 0.33562 0.29276 -0.09170 -0.05735 -0.02756 56  ILE A CG2 
489  C CD1 . ILE A 58  ? 0.33985 0.42738 0.42988 -0.13722 -0.07263 -0.02757 56  ILE A CD1 
490  N N   . LEU A 59  ? 0.26037 0.34124 0.28926 -0.08537 -0.09266 -0.06495 57  LEU A N   
491  C CA  . LEU A 59  ? 0.34423 0.40676 0.35585 -0.09194 -0.10801 -0.08349 57  LEU A CA  
492  C C   . LEU A 59  ? 0.34454 0.41973 0.37845 -0.11571 -0.12348 -0.08408 57  LEU A C   
493  O O   . LEU A 59  ? 0.29637 0.41171 0.34781 -0.11887 -0.12852 -0.07869 57  LEU A O   
494  C CB  . LEU A 59  ? 0.36636 0.44155 0.34890 -0.07989 -0.11278 -0.09128 57  LEU A CB  
495  C CG  . LEU A 59  ? 0.41695 0.48166 0.37743 -0.08653 -0.13068 -0.11348 57  LEU A CG  
496  C CD1 . LEU A 59  ? 0.41546 0.43939 0.36632 -0.08390 -0.12844 -0.13303 57  LEU A CD1 
497  C CD2 . LEU A 59  ? 0.40380 0.48591 0.32824 -0.07617 -0.13344 -0.11608 57  LEU A CD2 
498  N N   . MET A 60  ? 0.39374 0.43562 0.42944 -0.13093 -0.13200 -0.09133 58  MET A N   
499  C CA  . MET A 60  ? 0.44658 0.49947 0.50314 -0.14765 -0.13919 -0.09186 58  MET A CA  
500  C C   . MET A 60  ? 0.57373 0.62246 0.61329 -0.14726 -0.15516 -0.11283 58  MET A C   
501  O O   . MET A 60  ? 0.56816 0.57824 0.58337 -0.14586 -0.15995 -0.12818 58  MET A O   
502  C CB  . MET A 60  ? 0.49719 0.51675 0.56082 -0.16351 -0.13692 -0.08479 58  MET A CB  
503  C CG  . MET A 60  ? 0.47786 0.49963 0.55163 -0.16625 -0.12162 -0.06408 58  MET A CG  
504  S SD  . MET A 60  ? 0.43111 0.51332 0.53512 -0.17373 -0.10749 -0.04797 58  MET A SD  
505  C CE  . MET A 60  ? 0.38600 0.47908 0.50690 -0.19765 -0.11763 -0.05006 58  MET A CE  
506  N N   . GLN A 61  ? 0.49123 0.57746 0.54346 -0.14699 -0.16440 -0.11367 59  GLN A N   
507  C CA  . GLN A 61  ? 0.69887 0.78689 0.73159 -0.14634 -0.17974 -0.13324 59  GLN A CA  
508  C C   . GLN A 61  ? 0.75091 0.86871 0.81571 -0.15805 -0.19222 -0.13288 59  GLN A C   
509  O O   . GLN A 61  ? 0.53417 0.68427 0.62926 -0.15665 -0.19078 -0.11729 59  GLN A O   
510  C CB  . GLN A 61  ? 0.79743 0.89003 0.79779 -0.12461 -0.18481 -0.13288 59  GLN A CB  
511  C CG  . GLN A 61  ? 0.73097 0.85821 0.74543 -0.11738 -0.18514 -0.11113 59  GLN A CG  
512  C CD  . GLN A 61  ? 0.78439 0.91783 0.75950 -0.10264 -0.18916 -0.10873 59  GLN A CD  
513  O OE1 . GLN A 61  ? 0.81197 0.92518 0.74499 -0.10160 -0.19537 -0.12194 59  GLN A OE1 
514  N NE2 . GLN A 61  ? 0.57456 0.73516 0.56218 -0.09095 -0.18537 -0.09196 59  GLN A NE2 
515  N N   . GLU A 62  ? 1.00491 0.88062 1.10161 -0.26917 -0.16494 -0.19934 60  GLU A N   
516  C CA  . GLU A 62  ? 0.90630 0.82069 1.03808 -0.29578 -0.17999 -0.20596 60  GLU A CA  
517  C C   . GLU A 62  ? 0.86193 0.78777 1.04530 -0.30416 -0.16875 -0.17024 60  GLU A C   
518  O O   . GLU A 62  ? 0.96811 0.84496 1.15685 -0.30475 -0.15192 -0.15457 60  GLU A O   
519  C CB  . GLU A 62  ? 1.01645 0.99601 1.13909 -0.28593 -0.20147 -0.21499 60  GLU A CB  
520  C CG  . GLU A 62  ? 1.14559 1.11884 1.21632 -0.28394 -0.21439 -0.24945 60  GLU A CG  
521  C CD  . GLU A 62  ? 1.32861 1.36800 1.39180 -0.26725 -0.23753 -0.25157 60  GLU A CD  
522  O OE1 . GLU A 62  ? 1.35215 1.43293 1.44518 -0.25531 -0.24227 -0.22417 60  GLU A OE1 
523  O OE2 . GLU A 62  ? 1.24718 1.29440 1.26971 -0.26615 -0.25059 -0.27812 60  GLU A OE2 
524  N N   . LYS A 63  ? 0.81065 0.79978 1.02902 -0.30806 -0.17662 -0.15527 61  LYS A N   
525  C CA  . LYS A 63  ? 0.82939 0.83681 1.08993 -0.31485 -0.16310 -0.12060 61  LYS A CA  
526  C C   . LYS A 63  ? 0.79013 0.82334 1.04390 -0.28805 -0.15273 -0.08884 61  LYS A C   
527  O O   . LYS A 63  ? 0.81010 0.85676 1.08901 -0.29063 -0.13808 -0.05938 61  LYS A O   
528  C CB  . LYS A 63  ? 0.70501 0.76694 1.01201 -0.33858 -0.17491 -0.12556 61  LYS A CB  
529  C CG  . LYS A 63  ? 0.76817 0.85032 1.11995 -0.35138 -0.15886 -0.09327 61  LYS A CG  
530  C CD  . LYS A 63  ? 0.82346 0.97937 1.19841 -0.33816 -0.16143 -0.07663 61  LYS A CD  
531  C CE  . LYS A 63  ? 0.69408 0.86629 1.09703 -0.34208 -0.13870 -0.04070 61  LYS A CE  
532  N NZ  . LYS A 63  ? 0.57506 0.78514 0.96708 -0.31327 -0.13067 -0.01913 61  LYS A NZ  
533  N N   . GLU A 64  ? 0.62002 0.65812 0.83658 -0.26345 -0.15847 -0.09380 62  GLU A N   
534  C CA  . GLU A 64  ? 0.57216 0.63747 0.78209 -0.24102 -0.14989 -0.06616 62  GLU A CA  
535  C C   . GLU A 64  ? 0.43829 0.45871 0.60967 -0.22163 -0.13911 -0.06218 62  GLU A C   
536  O O   . GLU A 64  ? 0.57753 0.54536 0.73197 -0.22372 -0.13539 -0.07791 62  GLU A O   
537  C CB  . GLU A 64  ? 0.51043 0.63253 0.71808 -0.22926 -0.16676 -0.06991 62  GLU A CB  
538  C CG  . GLU A 64  ? 0.50306 0.67280 0.75419 -0.24722 -0.18004 -0.07790 62  GLU A CG  
539  C CD  . GLU A 64  ? 0.53561 0.74007 0.83204 -0.25438 -0.16427 -0.05117 62  GLU A CD  
540  O OE1 . GLU A 64  ? 0.43197 0.61826 0.72376 -0.24837 -0.14268 -0.02717 62  GLU A OE1 
541  O OE2 . GLU A 64  ? 0.57022 0.82275 0.90605 -0.26522 -0.17349 -0.05493 62  GLU A OE2 
542  N N   . CYS A 65  ? 0.43558 0.47768 0.59511 -0.20214 -0.13303 -0.04251 63  CYS A N   
543  C CA  . CYS A 65  ? 0.39840 0.40568 0.53208 -0.18577 -0.12044 -0.03374 63  CYS A CA  
544  C C   . CYS A 65  ? 0.36381 0.38738 0.46368 -0.16692 -0.12701 -0.03608 63  CYS A C   
545  O O   . CYS A 65  ? 0.32813 0.39852 0.43294 -0.16172 -0.13566 -0.03104 63  CYS A O   
546  C CB  . CYS A 65  ? 0.34111 0.35575 0.49622 -0.18367 -0.10208 -0.00283 63  CYS A CB  
547  S SG  . CYS A 65  ? 0.47677 0.45099 0.60850 -0.16490 -0.08805 0.00709  63  CYS A SG  
548  N N   . GLN A 66  ? 0.34675 0.33089 0.41229 -0.15520 -0.12201 -0.04372 64  GLN A N   
549  C CA  . GLN A 66  ? 0.32845 0.32443 0.35785 -0.13400 -0.12066 -0.04207 64  GLN A CA  
550  C C   . GLN A 66  ? 0.30334 0.28147 0.32769 -0.11509 -0.09757 -0.02723 64  GLN A C   
551  O O   . GLN A 66  ? 0.30891 0.24754 0.33504 -0.11484 -0.08743 -0.03121 64  GLN A O   
552  C CB  . GLN A 66  ? 0.40253 0.37742 0.38485 -0.12929 -0.12915 -0.06920 64  GLN A CB  
553  C CG  . GLN A 66  ? 0.36047 0.34523 0.30292 -0.10434 -0.12091 -0.06211 64  GLN A CG  
554  C CD  . GLN A 66  ? 0.41563 0.39152 0.30607 -0.10087 -0.13015 -0.08378 64  GLN A CD  
555  O OE1 . GLN A 66  ? 0.51721 0.48120 0.39818 -0.11664 -0.14511 -0.10973 64  GLN A OE1 
556  N NE2 . GLN A 66  ? 0.45395 0.43475 0.30797 -0.08114 -0.12119 -0.07343 64  GLN A NE2 
557  N N   . LEU A 67  ? 0.26344 0.27043 0.28439 -0.09837 -0.09050 -0.01114 65  LEU A N   
558  C CA  . LEU A 67  ? 0.26849 0.26273 0.28317 -0.08119 -0.07147 -0.00039 65  LEU A CA  
559  C C   . LEU A 67  ? 0.31010 0.28030 0.28610 -0.06683 -0.06449 -0.01229 65  LEU A C   
560  O O   . LEU A 67  ? 0.29913 0.28332 0.25147 -0.05808 -0.06909 -0.01201 65  LEU A O   
561  C CB  . LEU A 67  ? 0.22752 0.25918 0.25572 -0.07082 -0.06707 0.01715  65  LEU A CB  
562  C CG  . LEU A 67  ? 0.23539 0.25842 0.25866 -0.05498 -0.05050 0.02556  65  LEU A CG  
563  C CD1 . LEU A 67  ? 0.24939 0.24923 0.28393 -0.05997 -0.04213 0.02933  65  LEU A CD1 
564  C CD2 . LEU A 67  ? 0.21334 0.27315 0.25142 -0.04545 -0.04725 0.03725  65  LEU A CD2 
565  N N   . MET A 68  ? 0.26707 0.20232 0.23755 -0.06434 -0.05329 -0.02174 66  MET A N   
566  C CA  . MET A 68  ? 0.30731 0.22490 0.24250 -0.05268 -0.04329 -0.03438 66  MET A CA  
567  C C   . MET A 68  ? 0.30150 0.22511 0.23477 -0.03767 -0.02743 -0.02021 66  MET A C   
568  O O   . MET A 68  ? 0.32656 0.25087 0.23039 -0.02913 -0.02094 -0.02018 66  MET A O   
569  C CB  . MET A 68  ? 0.33430 0.21528 0.26841 -0.05390 -0.03599 -0.05439 66  MET A CB  
570  C CG  . MET A 68  ? 0.35707 0.22260 0.29413 -0.07080 -0.05203 -0.07338 66  MET A CG  
571  S SD  . MET A 68  ? 0.42744 0.31276 0.32488 -0.07891 -0.07177 -0.08961 66  MET A SD  
572  C CE  . MET A 68  ? 0.49887 0.37024 0.34236 -0.06102 -0.05305 -0.10438 66  MET A CE  
573  N N   . ASN A 69  ? 0.27685 0.20667 0.23981 -0.03597 -0.02251 -0.00677 67  ASN A N   
574  C CA  . ASN A 69  ? 0.26720 0.20112 0.23281 -0.02441 -0.00922 0.00261  67  ASN A CA  
575  C C   . ASN A 69  ? 0.25179 0.19922 0.24657 -0.02534 -0.01009 0.01528  67  ASN A C   
576  O O   . ASN A 69  ? 0.25678 0.19962 0.26909 -0.03270 -0.01466 0.01774  67  ASN A O   
577  C CB  . ASN A 69  ? 0.28651 0.19996 0.24725 -0.01775 0.00645  -0.00704 67  ASN A CB  
578  C CG  . ASN A 69  ? 0.31051 0.22998 0.26950 -0.00941 0.02016  0.00064  67  ASN A CG  
579  O OD1 . ASN A 69  ? 0.29719 0.23006 0.25913 -0.00765 0.01711  0.01231  67  ASN A OD1 
580  N ND2 . ASN A 69  ? 0.32834 0.23789 0.28460 -0.00459 0.03619  -0.00720 67  ASN A ND2 
581  N N   . ILE A 70  ? 0.24383 0.20587 0.24158 -0.01821 -0.00579 0.02330  68  ILE A N   
582  C CA  . ILE A 70  ? 0.21654 0.19314 0.23447 -0.01741 -0.00510 0.03178  68  ILE A CA  
583  C C   . ILE A 70  ? 0.18827 0.16511 0.20569 -0.00888 0.00337  0.03113  68  ILE A C   
584  O O   . ILE A 70  ? 0.21570 0.18873 0.22001 -0.00428 0.00610  0.03051  68  ILE A O   
585  C CB  . ILE A 70  ? 0.18455 0.18816 0.21071 -0.02194 -0.01260 0.03925  68  ILE A CB  
586  C CG1 . ILE A 70  ? 0.15567 0.17611 0.19348 -0.02073 -0.01008 0.04638  68  ILE A CG1 
587  C CG2 . ILE A 70  ? 0.21956 0.23662 0.23807 -0.01474 -0.01459 0.03832  68  ILE A CG2 
588  C CD1 . ILE A 70  ? 0.23596 0.28982 0.28199 -0.02540 -0.01270 0.05374  68  ILE A CD1 
589  N N   . ALA A 71  ? 0.19768 0.17660 0.23022 -0.00746 0.00655  0.03188  69  ALA A N   
590  C CA  . ALA A 71  ? 0.16850 0.14687 0.20577 -0.00308 0.01370  0.02863  69  ALA A CA  
591  C C   . ALA A 71  ? 0.13621 0.13005 0.19078 -0.00325 0.00952  0.02931  69  ALA A C   
592  O O   . ALA A 71  ? 0.15893 0.15670 0.22221 -0.00457 0.00427  0.03456  69  ALA A O   
593  C CB  . ALA A 71  ? 0.21703 0.17898 0.25277 -0.00205 0.02550  0.02433  69  ALA A CB  
594  N N   . VAL A 72  ? 0.14563 0.14618 0.20403 -0.00176 0.01042  0.02400  70  VAL A N   
595  C CA  . VAL A 72  ? 0.14710 0.16560 0.21711 -0.00256 0.00408  0.02038  70  VAL A CA  
596  C C   . VAL A 72  ? 0.18598 0.19880 0.27122 -0.00453 0.00874  0.01088  70  VAL A C   
597  O O   . VAL A 72  ? 0.17356 0.17025 0.25511 -0.00449 0.01586  0.00739  70  VAL A O   
598  C CB  . VAL A 72  ? 0.14658 0.18364 0.20485 -0.00097 -0.00098 0.01819  70  VAL A CB  
599  C CG1 . VAL A 72  ? 0.14254 0.19913 0.20390 -0.00183 -0.00820 0.01033  70  VAL A CG1 
600  C CG2 . VAL A 72  ? 0.12478 0.17207 0.17421 -0.00315 -0.00398 0.03116  70  VAL A CG2 
601  N N   . ALA A 73  ? 0.13343 0.15940 0.23899 -0.00678 0.00406  0.00868  71  ALA A N   
602  C CA  . ALA A 73  ? 0.13970 0.16537 0.26795 -0.01240 0.00793  -0.00070 71  ALA A CA  
603  C C   . ALA A 73  ? 0.15302 0.17387 0.27527 -0.01513 0.00528  -0.01316 71  ALA A C   
604  O O   . ALA A 73  ? 0.14209 0.17601 0.24919 -0.01192 -0.00390 -0.01875 71  ALA A O   
605  C CB  . ALA A 73  ? 0.16791 0.21894 0.32325 -0.01350 -0.00207 -0.00185 71  ALA A CB  
606  N N   . PRO A 74  ? 0.15412 0.15493 0.28784 -0.02091 0.01443  -0.01810 72  PRO A N   
607  C CA  . PRO A 74  ? 0.21296 0.19844 0.34146 -0.02092 0.01277  -0.03063 72  PRO A CA  
608  C C   . PRO A 74  ? 0.15397 0.15946 0.28610 -0.02347 -0.00137 -0.05053 72  PRO A C   
609  O O   . PRO A 74  ? 0.22682 0.22880 0.34307 -0.01718 -0.00415 -0.06259 72  PRO A O   
610  C CB  . PRO A 74  ? 0.26159 0.22002 0.40917 -0.03027 0.02476  -0.02871 72  PRO A CB  
611  C CG  . PRO A 74  ? 0.26383 0.22149 0.41003 -0.03061 0.03730  -0.01113 72  PRO A CG  
612  C CD  . PRO A 74  ? 0.19974 0.18747 0.34832 -0.02649 0.02947  -0.01010 72  PRO A CD  
613  N N   . ARG A 75  ? 0.15469 0.18424 0.30738 -0.03144 -0.01081 -0.05557 73  ARG A N   
614  C CA  . ARG A 75  ? 0.19750 0.25086 0.34686 -0.03411 -0.02760 -0.07499 73  ARG A CA  
615  C C   . ARG A 75  ? 0.23691 0.31336 0.35201 -0.02384 -0.03517 -0.07095 73  ARG A C   
616  O O   . ARG A 75  ? 0.20615 0.30087 0.30567 -0.02404 -0.04619 -0.08913 73  ARG A O   
617  C CB  . ARG A 75  ? 0.16245 0.24332 0.34390 -0.04397 -0.03950 -0.07796 73  ARG A CB  
618  C CG  . ARG A 75  ? 0.31169 0.37511 0.52992 -0.05859 -0.03219 -0.08720 73  ARG A CG  
619  C CD  . ARG A 75  ? 0.21142 0.30654 0.46466 -0.06879 -0.04438 -0.09270 73  ARG A CD  
620  N NE  . ARG A 75  ? 0.26681 0.33940 0.54349 -0.08042 -0.03010 -0.09190 73  ARG A NE  
621  C CZ  . ARG A 75  ? 0.27296 0.32326 0.55219 -0.09038 -0.03083 -0.10765 73  ARG A CZ  
622  N NH1 . ARG A 75  ? 0.38170 0.43216 0.64303 -0.09031 -0.04613 -0.13096 73  ARG A NH1 
623  N NH2 . ARG A 75  ? 0.56444 0.59189 0.86216 -0.10012 -0.01535 -0.09961 73  ARG A NH2 
624  N N   . TYR A 76  ? 0.16572 0.24240 0.26790 -0.01651 -0.02905 -0.04881 74  TYR A N   
625  C CA  . TYR A 76  ? 0.15735 0.25524 0.23078 -0.01001 -0.03332 -0.03976 74  TYR A CA  
626  C C   . TYR A 76  ? 0.18599 0.27310 0.24134 -0.00280 -0.02147 -0.03683 74  TYR A C   
627  O O   . TYR A 76  ? 0.19389 0.30072 0.22973 0.00043  -0.02150 -0.02710 74  TYR A O   
628  C CB  . TYR A 76  ? 0.14277 0.25156 0.22103 -0.00911 -0.03845 -0.01615 74  TYR A CB  
629  C CG  . TYR A 76  ? 0.13815 0.27119 0.23236 -0.01220 -0.05516 -0.01808 74  TYR A CG  
630  C CD1 . TYR A 76  ? 0.13255 0.26335 0.26440 -0.01712 -0.05627 -0.02439 74  TYR A CD1 
631  C CD2 . TYR A 76  ? 0.19178 0.35601 0.26338 -0.01093 -0.07074 -0.01508 74  TYR A CD2 
632  C CE1 . TYR A 76  ? 0.14171 0.30267 0.29406 -0.01956 -0.07457 -0.02735 74  TYR A CE1 
633  C CE2 . TYR A 76  ? 0.17093 0.36223 0.25532 -0.01271 -0.09049 -0.01672 74  TYR A CE2 
634  C CZ  . TYR A 76  ? 0.16115 0.35200 0.28926 -0.01674 -0.09368 -0.02376 74  TYR A CZ  
635  O OH  . TYR A 76  ? 0.17323 0.39647 0.32252 -0.01818 -0.11495 -0.02557 74  TYR A OH  
636  N N   . GLN A 77  ? 0.17051 0.23002 0.23382 -0.00037 -0.01208 -0.04400 75  GLN A N   
637  C CA  . GLN A 77  ? 0.20982 0.26238 0.26260 0.00883  -0.00352 -0.04094 75  GLN A CA  
638  C C   . GLN A 77  ? 0.26066 0.32980 0.30036 0.01658  -0.00285 -0.06002 75  GLN A C   
639  O O   . GLN A 77  ? 0.29706 0.37220 0.33394 0.01433  -0.00848 -0.08131 75  GLN A O   
640  C CB  . GLN A 77  ? 0.28186 0.29801 0.34692 0.01066  0.00416  -0.03877 75  GLN A CB  
641  C CG  . GLN A 77  ? 0.18900 0.19428 0.25842 0.00554  0.00759  -0.02032 75  GLN A CG  
642  C CD  . GLN A 77  ? 0.18169 0.15464 0.25429 0.00679  0.01615  -0.01358 75  GLN A CD  
643  O OE1 . GLN A 77  ? 0.22691 0.17973 0.30341 0.01144  0.01846  -0.02070 75  GLN A OE1 
644  N NE2 . GLN A 77  ? 0.19093 0.15703 0.26067 0.00333  0.02109  -0.00018 75  GLN A NE2 
645  N N   . ARG A 78  ? 0.25228 0.33204 0.28536 0.02586  0.00417  -0.05441 76  ARG A N   
646  C CA  . ARG A 78  ? 0.25579 0.35556 0.28005 0.03699  0.00978  -0.07208 76  ARG A CA  
647  C C   . ARG A 78  ? 0.25272 0.39040 0.25390 0.03262  0.00676  -0.07830 76  ARG A C   
648  O O   . ARG A 78  ? 0.28002 0.43187 0.26866 0.03943  0.00972  -0.10336 76  ARG A O   
649  C CB  . ARG A 78  ? 0.32096 0.39054 0.35652 0.04600  0.01202  -0.09738 76  ARG A CB  
650  C CG  . ARG A 78  ? 0.34631 0.37519 0.40092 0.04991  0.01428  -0.08463 76  ARG A CG  
651  C CD  . ARG A 78  ? 0.33582 0.37680 0.39329 0.06102  0.01850  -0.06764 76  ARG A CD  
652  N NE  . ARG A 78  ? 0.30210 0.36184 0.36440 0.07918  0.02492  -0.08342 76  ARG A NE  
653  C CZ  . ARG A 78  ? 0.30579 0.33964 0.38415 0.09642  0.02750  -0.09373 76  ARG A CZ  
654  N NH1 . ARG A 78  ? 0.41294 0.39745 0.50096 0.09570  0.02422  -0.08812 76  ARG A NH1 
655  N NH2 . ARG A 78  ? 0.34112 0.39896 0.42758 0.11536  0.03473  -0.10935 76  ARG A NH2 
656  N N   . LYS A 79  ? 0.25844 0.41218 0.25164 0.02232  0.00103  -0.05507 77  LYS A N   
657  C CA  . LYS A 79  ? 0.30558 0.49731 0.27229 0.01832  -0.00205 -0.05122 77  LYS A CA  
658  C C   . LYS A 79  ? 0.28662 0.50082 0.24751 0.01340  0.00342  -0.02114 77  LYS A C   
659  O O   . LYS A 79  ? 0.29668 0.53943 0.23458 0.00790  0.00092  -0.00827 77  LYS A O   
660  C CB  . LYS A 79  ? 0.36780 0.55822 0.33103 0.00989  -0.01858 -0.05069 77  LYS A CB  
661  C CG  . LYS A 79  ? 0.48459 0.65394 0.46045 0.00961  -0.02508 -0.08050 77  LYS A CG  
662  C CD  . LYS A 79  ? 0.59809 0.77754 0.55613 0.01726  -0.02025 -0.11469 77  LYS A CD  
663  C CE  . LYS A 79  ? 0.62917 0.85348 0.54736 0.01626  -0.02558 -0.12033 77  LYS A CE  
664  N NZ  . LYS A 79  ? 0.60750 0.85041 0.50260 0.02732  -0.01265 -0.14902 77  LYS A NZ  
665  N N   . GLY A 80  ? 0.19341 0.39633 0.17376 0.01408  0.00995  -0.00910 78  GLY A N   
666  C CA  . GLY A 80  ? 0.23744 0.45749 0.21929 0.00556  0.01375  0.01762  78  GLY A CA  
667  C C   . GLY A 80  ? 0.22232 0.41805 0.21294 -0.00487 0.00417  0.04058  78  GLY A C   
668  O O   . GLY A 80  ? 0.19508 0.40005 0.18804 -0.01459 0.00603  0.06339  78  GLY A O   
669  N N   . VAL A 81  ? 0.15505 0.40773 0.18341 0.00230  0.01568  -0.07032 79  VAL A N   
670  C CA  . VAL A 81  ? 0.20861 0.41820 0.25706 0.00787  -0.00920 -0.05101 79  VAL A CA  
671  C C   . VAL A 81  ? 0.19905 0.39179 0.26818 0.00297  0.00082  -0.04398 79  VAL A C   
672  O O   . VAL A 81  ? 0.16316 0.32745 0.22431 -0.01326 -0.01316 -0.01552 79  VAL A O   
673  C CB  . VAL A 81  ? 0.11680 0.29521 0.20490 0.03620  -0.02117 -0.07023 79  VAL A CB  
674  C CG1 . VAL A 81  ? 0.11416 0.23641 0.23743 0.03897  -0.03841 -0.05455 79  VAL A CG1 
675  C CG2 . VAL A 81  ? 0.15318 0.34172 0.22228 0.03612  -0.04439 -0.06813 79  VAL A CG2 
676  N N   . ALA A 82  ? 0.11737 0.27629 0.18804 0.01063  0.01413  -0.05632 80  ALA A N   
677  C CA  . ALA A 82  ? 0.09233 0.23400 0.17379 0.00269  0.01786  -0.04813 80  ALA A CA  
678  C C   . ALA A 82  ? 0.13282 0.31778 0.21154 -0.01934 0.02533  -0.03182 80  ALA A C   
679  O O   . ALA A 82  ? 0.15955 0.34397 0.24892 -0.03817 0.02231  -0.01624 80  ALA A O   
680  C CB  . ALA A 82  ? 0.14826 0.25284 0.21667 0.00430  0.01547  -0.05492 80  ALA A CB  
681  N N   . SER A 83  ? 0.13510 0.34254 0.19514 -0.02336 0.03401  -0.03299 81  SER A N   
682  C CA  . SER A 83  ? 0.12011 0.35299 0.17198 -0.04561 0.04382  -0.01727 81  SER A CA  
683  C C   . SER A 83  ? 0.17709 0.43128 0.20628 -0.07504 0.03775  0.01332  81  SER A C   
684  O O   . SER A 83  ? 0.18129 0.42445 0.21020 -0.09241 0.03613  0.03388  81  SER A O   
685  C CB  . SER A 83  ? 0.16823 0.41446 0.20878 -0.04734 0.05750  -0.02812 81  SER A CB  
686  O OG  . SER A 83  ? 0.16764 0.38708 0.23504 -0.02874 0.05875  -0.03932 81  SER A OG  
687  N N   . GLN A 84  ? 0.20322 0.43716 0.20347 -0.07181 0.01824  0.02053  82  GLN A N   
688  C CA  . GLN A 84  ? 0.23196 0.43329 0.20183 -0.09103 -0.00666 0.05747  82  GLN A CA  
689  C C   . GLN A 84  ? 0.22130 0.37329 0.22653 -0.08527 -0.02170 0.06871  82  GLN A C   
690  O O   . GLN A 84  ? 0.25382 0.38710 0.25108 -0.10564 -0.02917 0.09740  82  GLN A O   
691  C CB  . GLN A 84  ? 0.26863 0.45794 0.20960 -0.08969 -0.03246 0.06579  82  GLN A CB  
692  C CG  . GLN A 84  ? 0.30162 0.52987 0.18977 -0.10688 -0.01797 0.05705  82  GLN A CG  
693  C CD  . GLN A 84  ? 0.41440 0.62338 0.25904 -0.11878 -0.05373 0.07820  82  GLN A CD  
694  O OE1 . GLN A 84  ? 0.45667 0.63400 0.28238 -0.13719 -0.08559 0.11908  82  GLN A OE1 
695  N NE2 . GLN A 84  ? 0.48393 0.71085 0.31482 -0.11061 -0.05222 0.05312  82  GLN A NE2 
696  N N   . LEU A 85  ? 0.18166 0.30970 0.22450 -0.06101 -0.02200 0.04408  83  LEU A N   
697  C CA  . LEU A 85  ? 0.18074 0.25483 0.25427 -0.06024 -0.02794 0.04637  83  LEU A CA  
698  C C   . LEU A 85  ? 0.20699 0.28354 0.27748 -0.07933 -0.01513 0.05094  83  LEU A C   
699  O O   . LEU A 85  ? 0.20544 0.24921 0.27902 -0.09637 -0.02120 0.07040  83  LEU A O   
700  C CB  . LEU A 85  ? 0.14660 0.19457 0.25287 -0.03569 -0.02227 0.01321  83  LEU A CB  
701  C CG  . LEU A 85  ? 0.17783 0.20009 0.31047 -0.01932 -0.04124 0.01439  83  LEU A CG  
702  C CD1 . LEU A 85  ? 0.18923 0.18853 0.35633 0.00418  -0.02692 -0.02435 83  LEU A CD1 
703  C CD2 . LEU A 85  ? 0.22632 0.19954 0.38699 -0.03096 -0.05802 0.04141  83  LEU A CD2 
704  N N   . LEU A 86  ? 0.14817 0.26684 0.21818 -0.07893 0.00080  0.03618  84  LEU A N   
705  C CA  . LEU A 86  ? 0.17895 0.30539 0.25449 -0.09884 0.00698  0.04360  84  LEU A CA  
706  C C   . LEU A 86  ? 0.19979 0.33729 0.25690 -0.11857 0.00623  0.07158  84  LEU A C   
707  O O   . LEU A 86  ? 0.26340 0.37245 0.31838 -0.12781 0.00177  0.08045  84  LEU A O   
708  C CB  . LEU A 86  ? 0.16031 0.31350 0.24835 -0.08160 0.01797  0.02226  84  LEU A CB  
709  C CG  . LEU A 86  ? 0.16316 0.30790 0.25759 -0.09079 0.01614  0.02983  84  LEU A CG  
710  C CD1 . LEU A 86  ? 0.22780 0.32410 0.31398 -0.09888 0.00639  0.02836  84  LEU A CD1 
711  C CD2 . LEU A 86  ? 0.15050 0.31033 0.27041 -0.07418 0.02183  0.01649  84  LEU A CD2 
712  N N   . GLN A 87  ? 0.20161 0.37554 0.23826 -0.12445 0.01198  0.08174  85  GLN A N   
713  C CA  . GLN A 87  ? 0.24877 0.42429 0.26041 -0.14316 0.01225  0.10471  85  GLN A CA  
714  C C   . GLN A 87  ? 0.28293 0.41089 0.28844 -0.15417 -0.00833 0.13195  85  GLN A C   
715  O O   . GLN A 87  ? 0.31029 0.42494 0.31488 -0.16324 -0.00911 0.14203  85  GLN A O   
716  C CB  . GLN A 87  ? 0.27768 0.48565 0.25328 -0.15056 0.02187  0.10573  85  GLN A CB  
717  C CG  . GLN A 87  ? 0.44029 0.65251 0.38907 -0.17031 0.02978  0.11888  85  GLN A CG  
718  C CD  . GLN A 87  ? 0.51398 0.75152 0.42688 -0.17777 0.04620  0.10576  85  GLN A CD  
719  O OE1 . GLN A 87  ? 0.55690 0.79200 0.43450 -0.18097 0.03325  0.11029  85  GLN A OE1 
720  N NE2 . GLN A 87  ? 0.65059 0.90671 0.57680 -0.18021 0.07477  0.08799  85  GLN A NE2 
721  N N   . HIS A 88  ? 0.28565 0.38161 0.29771 -0.14640 -0.02587 0.13821  86  HIS A N   
722  C CA  . HIS A 88  ? 0.32271 0.36747 0.34784 -0.15291 -0.04580 0.16270  86  HIS A CA  
723  C C   . HIS A 88  ? 0.31033 0.32093 0.36029 -0.14663 -0.03654 0.14223  86  HIS A C   
724  O O   . HIS A 88  ? 0.34188 0.33121 0.39405 -0.15342 -0.03885 0.15281  86  HIS A O   
725  C CB  . HIS A 88  ? 0.32442 0.33890 0.37162 -0.13398 -0.06678 0.16202  86  HIS A CB  
726  C CG  . HIS A 88  ? 0.46509 0.45520 0.51150 -0.14639 -0.09645 0.20352  86  HIS A CG  
727  N ND1 . HIS A 88  ? 0.69972 0.71368 0.69815 -0.15762 -0.11425 0.22645  86  HIS A ND1 
728  C CD2 . HIS A 88  ? 0.53617 0.48873 0.62036 -0.14414 -0.10911 0.21407  86  HIS A CD2 
729  C CE1 . HIS A 88  ? 0.61085 0.59906 0.62289 -0.16492 -0.14288 0.25470  86  HIS A CE1 
730  N NE2 . HIS A 88  ? 0.61597 0.57156 0.68392 -0.15596 -0.13877 0.24855  86  HIS A NE2 
731  N N   . ALA A 89  ? 0.28221 0.28609 0.34516 -0.13502 -0.02502 0.11133  87  ALA A N   
732  C CA  . ALA A 89  ? 0.33089 0.30274 0.39756 -0.13298 -0.01280 0.08842  87  ALA A CA  
733  C C   . ALA A 89  ? 0.28521 0.27790 0.33896 -0.14483 -0.00976 0.09587  87  ALA A C   
734  O O   . ALA A 89  ? 0.35733 0.32307 0.41257 -0.15068 -0.00553 0.09302  87  ALA A O   
735  C CB  . ALA A 89  ? 0.24061 0.20743 0.31059 -0.12140 -0.00244 0.05692  87  ALA A CB  
736  N N   . LEU A 90  ? 0.28384 0.32484 0.33124 -0.14763 -0.00826 0.10145  88  LEU A N   
737  C CA  . LEU A 90  ? 0.30557 0.36324 0.35369 -0.15698 -0.00537 0.10619  88  LEU A CA  
738  C C   . LEU A 90  ? 0.36966 0.42510 0.40981 -0.17051 -0.00728 0.12953  88  LEU A C   
739  O O   . LEU A 90  ? 0.38407 0.43407 0.42870 -0.17946 -0.00609 0.13305  88  LEU A O   
740  C CB  . LEU A 90  ? 0.25806 0.36353 0.31712 -0.15331 0.00280  0.10066  88  LEU A CB  
741  C CG  . LEU A 90  ? 0.24980 0.35924 0.32363 -0.14006 0.00292  0.07956  88  LEU A CG  
742  C CD1 . LEU A 90  ? 0.30169 0.45452 0.40102 -0.13636 0.01399  0.07611  88  LEU A CD1 
743  C CD2 . LEU A 90  ? 0.25808 0.33240 0.32854 -0.14432 -0.00624 0.07295  88  LEU A CD2 
744  N N   . HIS A 91  ? 0.35046 0.40986 0.37739 -0.17395 -0.01222 0.14764  89  HIS A N   
745  C CA  . HIS A 91  ? 0.38691 0.43512 0.40463 -0.18705 -0.01752 0.17150  89  HIS A CA  
746  C C   . HIS A 91  ? 0.40294 0.40419 0.43786 -0.18602 -0.02173 0.17000  89  HIS A C   
747  O O   . HIS A 91  ? 0.42857 0.42265 0.46568 -0.19602 -0.01859 0.17739  89  HIS A O   
748  C CB  . HIS A 91  ? 0.41596 0.47161 0.41051 -0.19306 -0.02849 0.19383  89  HIS A CB  
749  C CG  . HIS A 91  ? 0.47137 0.51652 0.45204 -0.20873 -0.03627 0.22065  89  HIS A CG  
750  N ND1 . HIS A 91  ? 0.50931 0.51570 0.50870 -0.20829 -0.05300 0.23677  89  HIS A ND1 
751  C CD2 . HIS A 91  ? 0.51461 0.58064 0.46863 -0.22556 -0.02704 0.23238  89  HIS A CD2 
752  C CE1 . HIS A 91  ? 0.54867 0.55489 0.53147 -0.22453 -0.05797 0.26086  89  HIS A CE1 
753  N NE2 . HIS A 91  ? 0.60518 0.64545 0.55620 -0.23619 -0.04154 0.25815  89  HIS A NE2 
754  N N   . TYR A 92  ? 0.41528 0.38362 0.46547 -0.17436 -0.02310 0.15563  90  TYR A N   
755  C CA  . TYR A 92  ? 0.41067 0.33374 0.47849 -0.17413 -0.01508 0.14415  90  TYR A CA  
756  C C   . TYR A 92  ? 0.45002 0.37156 0.51353 -0.18053 -0.00213 0.12651  90  TYR A C   
757  O O   . TYR A 92  ? 0.50065 0.40569 0.56941 -0.19052 0.00332  0.13053  90  TYR A O   
758  C CB  . TYR A 92  ? 0.46971 0.35770 0.55476 -0.16074 -0.00852 0.12189  90  TYR A CB  
759  C CG  . TYR A 92  ? 0.43224 0.27272 0.52630 -0.16541 0.01232  0.10099  90  TYR A CG  
760  C CD1 . TYR A 92  ? 0.50609 0.33237 0.59363 -0.17024 0.03617  0.07091  90  TYR A CD1 
761  C CD2 . TYR A 92  ? 0.48852 0.30211 0.60331 -0.16723 0.00621  0.11474  90  TYR A CD2 
762  C CE1 . TYR A 92  ? 0.47544 0.26466 0.56093 -0.18031 0.05099  0.05472  90  TYR A CE1 
763  C CE2 . TYR A 92  ? 0.57551 0.34589 0.68840 -0.17810 0.02350  0.09668  90  TYR A CE2 
764  C CZ  . TYR A 92  ? 0.67484 0.42811 0.75714 -0.19189 0.04284  0.06781  90  TYR A CZ  
765  O OH  . TYR A 92  ? 0.82272 0.53852 0.89161 -0.20951 0.03942  0.06122  90  TYR A OH  
766  N N   . ALA A 93  ? 0.49953 0.43818 0.55631 -0.17553 -0.00024 0.10922  91  ALA A N   
767  C CA  . ALA A 93  ? 0.45355 0.39167 0.50798 -0.18236 0.00240  0.09766  91  ALA A CA  
768  C C   . ALA A 93  ? 0.43875 0.39993 0.49238 -0.19618 -0.00289 0.11634  91  ALA A C   
769  O O   . ALA A 93  ? 0.42074 0.36634 0.47717 -0.20702 -0.00087 0.11500  91  ALA A O   
770  C CB  . ALA A 93  ? 0.38430 0.34015 0.43214 -0.17504 -0.00231 0.08337  91  ALA A CB  
771  N N   . LYS A 94  ? 0.41295 0.41146 0.46565 -0.19727 -0.00632 0.13277  92  LYS A N   
772  C CA  . LYS A 94  ? 0.40848 0.42965 0.46714 -0.21015 -0.00484 0.14799  92  LYS A CA  
773  C C   . LYS A 94  ? 0.44873 0.44515 0.50655 -0.22000 -0.00278 0.16229  92  LYS A C   
774  O O   . LYS A 94  ? 0.52597 0.52491 0.59140 -0.23200 -0.00040 0.16849  92  LYS A O   
775  C CB  . LYS A 94  ? 0.39962 0.46288 0.45837 -0.20975 0.00118  0.15753  92  LYS A CB  
776  C CG  . LYS A 94  ? 0.42180 0.51148 0.49309 -0.22320 0.01209  0.16898  92  LYS A CG  
777  C CD  . LYS A 94  ? 0.43217 0.53237 0.53252 -0.22676 0.01000  0.16018  92  LYS A CD  
778  C CE  . LYS A 94  ? 0.54760 0.67723 0.67599 -0.23890 0.02612  0.16763  92  LYS A CE  
779  N NZ  . LYS A 94  ? 0.46000 0.62521 0.60777 -0.23344 0.04490  0.15897  92  LYS A NZ  
780  N N   . THR A 95  ? 0.46239 0.43472 0.51652 -0.21564 -0.00461 0.16934  93  THR A N   
781  C CA  . THR A 95  ? 0.50399 0.45033 0.56432 -0.22449 -0.00350 0.18426  93  THR A CA  
782  C C   . THR A 95  ? 0.51587 0.42586 0.58946 -0.22768 0.00722  0.16524  93  THR A C   
783  O O   . THR A 95  ? 0.58888 0.48176 0.67111 -0.23844 0.01265  0.17315  93  THR A O   
784  C CB  . THR A 95  ? 0.61081 0.54232 0.67209 -0.21943 -0.01349 0.20084  93  THR A CB  
785  O OG1 . THR A 95  ? 0.65204 0.61611 0.69286 -0.22596 -0.02173 0.22471  93  THR A OG1 
786  C CG2 . THR A 95  ? 0.69807 0.59073 0.77884 -0.22466 -0.01267 0.21042  93  THR A CG2 
787  N N   . HIS A 96  ? 0.69464 0.37641 0.70477 -0.21260 -0.05309 0.18444  94  HIS A N   
788  C CA  . HIS A 96  ? 0.68589 0.35780 0.73200 -0.21203 -0.05501 0.16154  94  HIS A CA  
789  C C   . HIS A 96  ? 0.65570 0.36730 0.72054 -0.22743 -0.04315 0.14135  94  HIS A C   
790  O O   . HIS A 96  ? 0.62083 0.34473 0.70430 -0.22301 -0.04756 0.11718  94  HIS A O   
791  C CB  . HIS A 96  ? 0.66244 0.32595 0.72238 -0.18772 -0.07021 0.15033  94  HIS A CB  
792  C CG  . HIS A 96  ? 0.70382 0.32882 0.76201 -0.17194 -0.08380 0.16870  94  HIS A CG  
793  N ND1 . HIS A 96  ? 0.74879 0.33213 0.82748 -0.16717 -0.08446 0.16524  94  HIS A ND1 
794  C CD2 . HIS A 96  ? 0.71616 0.33863 0.75445 -0.16077 -0.09824 0.19107  94  HIS A CD2 
795  C CE1 . HIS A 96  ? 0.77829 0.33873 0.85611 -0.15181 -0.09873 0.18647  94  HIS A CE1 
796  N NE2 . HIS A 96  ? 0.78198 0.36716 0.83530 -0.14850 -0.10925 0.20227  94  HIS A NE2 
797  N N   . HIS A 97  ? 0.69361 0.42867 0.75311 -0.24446 -0.02760 0.15231  95  HIS A N   
798  C CA  . HIS A 97  ? 0.68981 0.46357 0.77715 -0.26148 -0.01641 0.13872  95  HIS A CA  
799  C C   . HIS A 97  ? 0.64528 0.46634 0.74539 -0.25355 -0.02006 0.12019  95  HIS A C   
800  O O   . HIS A 97  ? 0.59198 0.43830 0.71880 -0.26236 -0.02166 0.10229  95  HIS A O   
801  C CB  . HIS A 97  ? 0.67290 0.42060 0.78312 -0.27483 -0.01971 0.12539  95  HIS A CB  
802  C CG  . HIS A 97  ? 0.73632 0.43356 0.83597 -0.28135 -0.01651 0.14377  95  HIS A CG  
803  N ND1 . HIS A 97  ? 0.82254 0.52077 0.92301 -0.30009 -0.00046 0.16222  95  HIS A ND1 
804  C CD2 . HIS A 97  ? 0.79809 0.44261 0.88757 -0.27012 -0.02611 0.14859  95  HIS A CD2 
805  C CE1 . HIS A 97  ? 0.83074 0.47725 0.91795 -0.30161 -0.00168 0.17793  95  HIS A CE1 
806  N NE2 . HIS A 97  ? 0.83193 0.44565 0.91379 -0.28285 -0.01800 0.17015  95  HIS A NE2 
807  N N   . ALA A 98  ? 0.54840 0.38209 0.62873 -0.23784 -0.02271 0.12481  96  ALA A N   
808  C CA  . ALA A 98  ? 0.49461 0.37456 0.58624 -0.23071 -0.02327 0.11098  96  ALA A CA  
809  C C   . ALA A 98  ? 0.48290 0.39896 0.56721 -0.23303 -0.00427 0.12351  96  ALA A C   
810  O O   . ALA A 98  ? 0.51655 0.41401 0.57151 -0.23576 0.00717  0.14253  96  ALA A O   
811  C CB  . ALA A 98  ? 0.46970 0.33760 0.54989 -0.21097 -0.03840 0.10359  96  ALA A CB  
812  N N   . THR A 99  ? 0.44227 0.40857 0.55250 -0.23110 0.00059  0.11224  97  THR A N   
813  C CA  . THR A 99  ? 0.43097 0.43510 0.54448 -0.22995 0.02298  0.12034  97  THR A CA  
814  C C   . THR A 99  ? 0.38219 0.42334 0.50383 -0.21462 0.02015  0.10993  97  THR A C   
815  O O   . THR A 99  ? 0.39583 0.46207 0.51519 -0.20906 0.04023  0.11542  97  THR A O   
816  C CB  . THR A 99  ? 0.50062 0.53558 0.65599 -0.24425 0.03886  0.12179  97  THR A CB  
817  O OG1 . THR A 99  ? 0.70409 0.76789 0.86323 -0.24124 0.06778  0.13102  97  THR A OG1 
818  C CG2 . THR A 99  ? 0.41274 0.48211 0.60973 -0.24452 0.02310  0.10413  97  THR A CG2 
819  N N   . ARG A 100 ? 0.35459 0.39602 0.48251 -0.20644 -0.00134 0.09476  98  ARG A N   
820  C CA  . ARG A 100 ? 0.31893 0.39433 0.45514 -0.18879 -0.00420 0.08370  98  ARG A CA  
821  C C   . ARG A 100 ? 0.30291 0.35024 0.41304 -0.17070 -0.01996 0.07274  98  ARG A C   
822  O O   . ARG A 100 ? 0.38048 0.40124 0.49051 -0.17427 -0.03363 0.06469  98  ARG A O   
823  C CB  . ARG A 100 ? 0.31738 0.43070 0.49300 -0.19237 -0.01302 0.07250  98  ARG A CB  
824  C CG  . ARG A 100 ? 0.30615 0.45032 0.51775 -0.20193 0.00109  0.07918  98  ARG A CG  
825  C CD  . ARG A 100 ? 0.34110 0.50897 0.58280 -0.20604 -0.01680 0.06703  98  ARG A CD  
826  N NE  . ARG A 100 ? 0.46584 0.65786 0.70963 -0.18931 -0.02789 0.05930  98  ARG A NE  
827  C CZ  . ARG A 100 ? 0.54259 0.77466 0.81448 -0.17761 -0.01966 0.06455  98  ARG A CZ  
828  N NH1 . ARG A 100 ? 0.41942 0.67413 0.72100 -0.18003 0.00300  0.07548  98  ARG A NH1 
829  N NH2 . ARG A 100 ? 0.31301 0.56007 0.58319 -0.16264 -0.03247 0.05876  98  ARG A NH2 
830  N N   . LEU A 101 ? 0.30733 0.35853 0.39792 -0.15200 -0.01623 0.07211  99  LEU A N   
831  C CA  . LEU A 101 ? 0.27439 0.30702 0.34952 -0.13497 -0.02952 0.06371  99  LEU A CA  
832  C C   . LEU A 101 ? 0.23844 0.30264 0.32701 -0.12204 -0.03197 0.05139  99  LEU A C   
833  O O   . LEU A 101 ? 0.25956 0.34672 0.34882 -0.11426 -0.02210 0.05361  99  LEU A O   
834  C CB  . LEU A 101 ? 0.29069 0.29996 0.33162 -0.12681 -0.02820 0.07376  99  LEU A CB  
835  C CG  . LEU A 101 ? 0.28222 0.27358 0.31606 -0.11144 -0.04413 0.06938  99  LEU A CG  
836  C CD1 . LEU A 101 ? 0.37428 0.33538 0.41812 -0.11308 -0.05653 0.07082  99  LEU A CD1 
837  C CD2 . LEU A 101 ? 0.31191 0.28726 0.31119 -0.10633 -0.04676 0.07860  99  LEU A CD2 
838  N N   . LEU A 102 ? 0.30104 0.36045 0.39582 -0.11887 -0.04335 0.03866  100 LEU A N   
839  C CA  . LEU A 102 ? 0.25410 0.33627 0.35387 -0.10822 -0.04704 0.02850  100 LEU A CA  
840  C C   . LEU A 102 ? 0.21750 0.28869 0.30532 -0.09037 -0.04787 0.02630  100 LEU A C   
841  O O   . LEU A 102 ? 0.25009 0.29352 0.33296 -0.08613 -0.05179 0.02612  100 LEU A O   
842  C CB  . LEU A 102 ? 0.22499 0.30089 0.32673 -0.11687 -0.05621 0.01484  100 LEU A CB  
843  C CG  . LEU A 102 ? 0.37029 0.46559 0.46825 -0.11274 -0.06212 0.00511  100 LEU A CG  
844  C CD1 . LEU A 102 ? 0.32364 0.45985 0.44124 -0.11853 -0.06593 0.01332  100 LEU A CD1 
845  C CD2 . LEU A 102 ? 0.41254 0.48460 0.49596 -0.12401 -0.06908 -0.01136 100 LEU A CD2 
846  N N   . LEU A 103 ? 0.18207 0.27525 0.27091 -0.07994 -0.04497 0.02628  101 LEU A N   
847  C CA  . LEU A 103 ? 0.16314 0.24828 0.24564 -0.06592 -0.04656 0.02403  101 LEU A CA  
848  C C   . LEU A 103 ? 0.17453 0.28020 0.26141 -0.05989 -0.04658 0.01847  101 LEU A C   
849  O O   . LEU A 103 ? 0.20888 0.33879 0.30294 -0.06012 -0.04496 0.02235  101 LEU A O   
850  C CB  . LEU A 103 ? 0.18482 0.26616 0.25580 -0.05990 -0.04303 0.03151  101 LEU A CB  
851  C CG  . LEU A 103 ? 0.19056 0.26701 0.25967 -0.04860 -0.04687 0.02990  101 LEU A CG  
852  C CD1 . LEU A 103 ? 0.21327 0.26983 0.29029 -0.04701 -0.05607 0.02956  101 LEU A CD1 
853  C CD2 . LEU A 103 ? 0.18835 0.25429 0.23750 -0.04686 -0.04485 0.03475  101 LEU A CD2 
854  N N   . GLU A 104 ? 0.21609 0.31235 0.30079 -0.05378 -0.04710 0.01164  102 GLU A N   
855  C CA  . GLU A 104 ? 0.20292 0.31287 0.28422 -0.04782 -0.04535 0.00931  102 GLU A CA  
856  C C   . GLU A 104 ? 0.25959 0.36326 0.34583 -0.03682 -0.04193 0.01217  102 GLU A C   
857  O O   . GLU A 104 ? 0.25256 0.34022 0.34752 -0.03403 -0.04167 0.01053  102 GLU A O   
858  C CB  . GLU A 104 ? 0.18129 0.28387 0.25007 -0.05348 -0.04467 -0.00213 102 GLU A CB  
859  C CG  . GLU A 104 ? 0.32585 0.42974 0.38884 -0.06851 -0.05220 -0.00677 102 GLU A CG  
860  C CD  . GLU A 104 ? 0.50424 0.59271 0.54236 -0.07611 -0.05188 -0.02140 102 GLU A CD  
861  O OE1 . GLU A 104 ? 0.59900 0.67230 0.62756 -0.06766 -0.03995 -0.02854 102 GLU A OE1 
862  O OE2 . GLU A 104 ? 0.53241 0.62303 0.56017 -0.09175 -0.06270 -0.02604 102 GLU A OE2 
863  N N   . VAL A 105 ? 0.17691 0.29290 0.26297 -0.03098 -0.04064 0.01782  103 VAL A N   
864  C CA  . VAL A 105 ? 0.18423 0.29338 0.27601 -0.02390 -0.03958 0.02151  103 VAL A CA  
865  C C   . VAL A 105 ? 0.20796 0.32751 0.29832 -0.01896 -0.03548 0.02509  103 VAL A C   
866  O O   . VAL A 105 ? 0.20501 0.33844 0.29005 -0.01913 -0.03659 0.02845  103 VAL A O   
867  C CB  . VAL A 105 ? 0.22621 0.32698 0.31251 -0.02401 -0.04254 0.02578  103 VAL A CB  
868  C CG1 . VAL A 105 ? 0.23793 0.35211 0.32141 -0.02174 -0.03694 0.02879  103 VAL A CG1 
869  C CG2 . VAL A 105 ? 0.33765 0.42572 0.42583 -0.02111 -0.04656 0.02790  103 VAL A CG2 
870  N N   . ARG A 106 ? 0.21678 0.33048 0.31541 -0.01543 -0.03204 0.02678  104 ARG A N   
871  C CA  . ARG A 106 ? 0.16496 0.28377 0.26104 -0.01185 -0.02733 0.03330  104 ARG A CA  
872  C C   . ARG A 106 ? 0.21785 0.33765 0.31265 -0.00724 -0.03033 0.03966  104 ARG A C   
873  O O   . ARG A 106 ? 0.19641 0.30605 0.29204 -0.00668 -0.03262 0.03768  104 ARG A O   
874  C CB  . ARG A 106 ? 0.16974 0.28182 0.28250 -0.01105 -0.02214 0.03561  104 ARG A CB  
875  C CG  . ARG A 106 ? 0.20592 0.31937 0.32634 -0.01216 -0.01074 0.03102  104 ARG A CG  
876  C CD  . ARG A 106 ? 0.20527 0.31787 0.35962 -0.01171 -0.00665 0.03499  104 ARG A CD  
877  N NE  . ARG A 106 ? 0.19594 0.31152 0.36600 -0.01022 0.01055  0.03023  104 ARG A NE  
878  C CZ  . ARG A 106 ? 0.24582 0.36358 0.40738 -0.01079 0.03075  0.03129  104 ARG A CZ  
879  N NH1 . ARG A 106 ? 0.23083 0.34840 0.36776 -0.01340 0.03270  0.03981  104 ARG A NH1 
880  N NH2 . ARG A 106 ? 0.22266 0.33992 0.39845 -0.00828 0.05139  0.02416  104 ARG A NH2 
881  N N   . LYS A 107 ? 0.18721 0.31616 0.27783 -0.00365 -0.02964 0.04781  105 LYS A N   
882  C CA  . LYS A 107 ? 0.24698 0.37671 0.34452 0.00423  -0.02993 0.05496  105 LYS A CA  
883  C C   . LYS A 107 ? 0.21534 0.32264 0.31637 0.00718  -0.02625 0.05371  105 LYS A C   
884  O O   . LYS A 107 ? 0.23351 0.33163 0.33570 0.01271  -0.02277 0.05205  105 LYS A O   
885  C CB  . LYS A 107 ? 0.25920 0.39966 0.35507 0.00809  -0.03308 0.06812  105 LYS A CB  
886  C CG  . LYS A 107 ? 0.22912 0.37599 0.34255 0.01906  -0.03414 0.07781  105 LYS A CG  
887  C CD  . LYS A 107 ? 0.25730 0.42270 0.37152 0.02073  -0.04541 0.09373  105 LYS A CD  
888  C CE  . LYS A 107 ? 0.42860 0.57920 0.52899 0.02167  -0.04473 0.10554  105 LYS A CE  
889  N NZ  . LYS A 107 ? 0.53151 0.65852 0.64535 0.02973  -0.03432 0.10491  105 LYS A NZ  
890  N N   . SER A 108 ? 0.19442 0.29138 0.29791 0.00248  -0.02577 0.05362  106 SER A N   
891  C CA  . SER A 108 ? 0.21241 0.28695 0.32032 0.00104  -0.02650 0.05286  106 SER A CA  
892  C C   . SER A 108 ? 0.22029 0.28174 0.32375 -0.00561 -0.03420 0.04312  106 SER A C   
893  O O   . SER A 108 ? 0.26042 0.29935 0.36123 -0.01021 -0.03932 0.04049  106 SER A O   
894  C CB  . SER A 108 ? 0.22539 0.29838 0.34581 -0.00366 -0.02324 0.06022  106 SER A CB  
895  O OG  . SER A 108 ? 0.23771 0.32190 0.36950 -0.00949 -0.02242 0.05673  106 SER A OG  
896  N N   . ASN A 109 ? 0.18186 0.25304 0.28114 -0.00791 -0.03733 0.03859  107 ASN A N   
897  C CA  . ASN A 109 ? 0.17821 0.23619 0.27164 -0.01520 -0.04813 0.03378  107 ASN A CA  
898  C C   . ASN A 109 ? 0.26840 0.30813 0.33364 -0.01522 -0.04630 0.02850  107 ASN A C   
899  O O   . ASN A 109 ? 0.25800 0.29989 0.31048 -0.01675 -0.04488 0.02663  107 ASN A O   
900  C CB  . ASN A 109 ? 0.16472 0.23559 0.26680 -0.01717 -0.05100 0.03321  107 ASN A CB  
901  C CG  . ASN A 109 ? 0.18526 0.24343 0.29006 -0.02400 -0.06636 0.03374  107 ASN A CG  
902  O OD1 . ASN A 109 ? 0.20716 0.24502 0.29542 -0.02985 -0.07710 0.03322  107 ASN A OD1 
903  N ND2 . ASN A 109 ? 0.16828 0.23488 0.29219 -0.02367 -0.06872 0.03508  107 ASN A ND2 
904  N N   . ARG A 110 ? 0.28497 0.28483 0.46652 0.04517  0.02054  0.01128  108 ARG A N   
905  C CA  . ARG A 110 ? 0.30323 0.30016 0.48419 0.06000  0.02470  0.00754  108 ARG A CA  
906  C C   . ARG A 110 ? 0.30573 0.30274 0.47498 0.05412  0.01947  -0.01100 108 ARG A C   
907  O O   . ARG A 110 ? 0.30404 0.32312 0.46805 0.06117  0.02014  -0.01005 108 ARG A O   
908  C CB  . ARG A 110 ? 0.39290 0.35204 0.58519 0.07226  0.03241  0.00556  108 ARG A CB  
909  C CG  . ARG A 110 ? 0.52788 0.48776 0.73443 0.08172  0.03902  0.02972  108 ARG A CG  
910  C CD  . ARG A 110 ? 0.46637 0.47236 0.67225 0.09161  0.04031  0.05009  108 ARG A CD  
911  N NE  . ARG A 110 ? 0.61460 0.63630 0.81360 0.10170  0.04103  0.04222  108 ARG A NE  
912  C CZ  . ARG A 110 ? 0.56076 0.61596 0.76318 0.11714  0.04507  0.05771  108 ARG A CZ  
913  N NH1 . ARG A 110 ? 0.72174 0.79636 0.93516 0.12706  0.04917  0.08290  108 ARG A NH1 
914  N NH2 . ARG A 110 ? 0.62159 0.69590 0.81700 0.12328  0.04519  0.04960  108 ARG A NH2 
915  N N   . SER A 111 ? 0.27342 0.24968 0.43960 0.04209  0.01464  -0.02601 109 SER A N   
916  C CA  . SER A 111 ? 0.22959 0.20757 0.38545 0.03845  0.01006  -0.04122 109 SER A CA  
917  C C   . SER A 111 ? 0.23148 0.24015 0.37951 0.03050  0.00439  -0.03507 109 SER A C   
918  O O   . SER A 111 ? 0.25511 0.27967 0.39645 0.03359  0.00366  -0.03730 109 SER A O   
919  C CB  . SER A 111 ? 0.25656 0.21151 0.41205 0.02759  0.00543  -0.05656 109 SER A CB  
920  O OG  . SER A 111 ? 0.28324 0.24302 0.43924 0.01433  -0.00007 -0.05357 109 SER A OG  
921  N N   . ALA A 112 ? 0.20292 0.22004 0.35166 0.01925  0.00029  -0.02835 110 ALA A N   
922  C CA  . ALA A 112 ? 0.18603 0.22658 0.32869 0.00931  -0.00556 -0.02421 110 ALA A CA  
923  C C   . ALA A 112 ? 0.15701 0.22880 0.30024 0.01587  -0.00286 -0.01123 110 ALA A C   
924  O O   . ALA A 112 ? 0.14366 0.23545 0.28272 0.01111  -0.00605 -0.00866 110 ALA A O   
925  C CB  . ALA A 112 ? 0.23548 0.27660 0.37805 -0.00309 -0.00990 -0.02367 110 ALA A CB  
926  N N   . ILE A 113 ? 0.14627 0.22488 0.29634 0.02755  0.00339  -0.00076 111 ILE A N   
927  C CA  . ILE A 113 ? 0.19159 0.30543 0.34438 0.03637  0.00650  0.01368  111 ILE A CA  
928  C C   . ILE A 113 ? 0.19298 0.31272 0.34358 0.04838  0.01047  0.00976  111 ILE A C   
929  O O   . ILE A 113 ? 0.16587 0.31904 0.31446 0.04645  0.00898  0.01672  111 ILE A O   
930  C CB  . ILE A 113 ? 0.21733 0.33564 0.37974 0.04987  0.01321  0.02794  111 ILE A CB  
931  C CG1 . ILE A 113 ? 0.22448 0.35458 0.38685 0.03726  0.00894  0.03490  111 ILE A CG1 
932  C CG2 . ILE A 113 ? 0.23787 0.39152 0.40521 0.06518  0.01823  0.04256  111 ILE A CG2 
933  C CD1 . ILE A 113 ? 0.20314 0.33116 0.37525 0.04826  0.01525  0.04976  111 ILE A CD1 
934  N N   . GLU A 114 ? 0.22131 0.31112 0.37259 0.06076  0.01592  -0.00170 112 GLU A N   
935  C CA  . GLU A 114 ? 0.17796 0.27509 0.32522 0.07446  0.02074  -0.00867 112 GLU A CA  
936  C C   . GLU A 114 ? 0.21421 0.32358 0.35118 0.06182  0.01422  -0.01566 112 GLU A C   
937  O O   . GLU A 114 ? 0.18348 0.32403 0.31710 0.06747  0.01623  -0.01137 112 GLU A O   
938  C CB  . GLU A 114 ? 0.34954 0.40800 0.49870 0.08798  0.02708  -0.02381 112 GLU A CB  
939  C CG  . GLU A 114 ? 0.37561 0.42086 0.53769 0.10352  0.03508  -0.01289 112 GLU A CG  
940  C CD  . GLU A 114 ? 0.51325 0.59575 0.68073 0.12225  0.04185  0.00391  112 GLU A CD  
941  O OE1 . GLU A 114 ? 0.47868 0.58282 0.64060 0.13242  0.04503  -0.00116 112 GLU A OE1 
942  O OE2 . GLU A 114 ? 0.53754 0.63318 0.71520 0.12729  0.04411  0.02371  112 GLU A OE2 
943  N N   . PHE A 115 ? 0.18041 0.27064 0.31378 0.04520  0.00670  -0.02298 113 PHE A N   
944  C CA  . PHE A 115 ? 0.15121 0.25291 0.27704 0.03327  0.00021  -0.02496 113 PHE A CA  
945  C C   . PHE A 115 ? 0.19682 0.33410 0.32401 0.02381  -0.00304 -0.00863 113 PHE A C   
946  O O   . PHE A 115 ? 0.14245 0.30617 0.26614 0.02291  -0.00341 -0.00320 113 PHE A O   
947  C CB  . PHE A 115 ? 0.18043 0.25553 0.30512 0.01904  -0.00692 -0.03289 113 PHE A CB  
948  C CG  . PHE A 115 ? 0.17254 0.25844 0.29277 0.00638  -0.01392 -0.02926 113 PHE A CG  
949  C CD1 . PHE A 115 ? 0.15336 0.24684 0.26665 0.00935  -0.01469 -0.03407 113 PHE A CD1 
950  C CD2 . PHE A 115 ? 0.13059 0.21954 0.25374 -0.00861 -0.01971 -0.02069 113 PHE A CD2 
951  C CE1 . PHE A 115 ? 0.16376 0.26847 0.27477 -0.00197 -0.02095 -0.02585 113 PHE A CE1 
952  C CE2 . PHE A 115 ? 0.16532 0.25891 0.28686 -0.02073 -0.02605 -0.01514 113 PHE A CE2 
953  C CZ  . PHE A 115 ? 0.15899 0.26191 0.27531 -0.01669 -0.02627 -0.01522 113 PHE A CZ  
954  N N   . TYR A 116 ? 0.15955 0.30099 0.29203 0.01534  -0.00561 -0.00040 114 TYR A N   
955  C CA  . TYR A 116 ? 0.12796 0.30113 0.26223 0.00158  -0.01048 0.01253  114 TYR A CA  
956  C C   . TYR A 116 ? 0.13089 0.34600 0.26861 0.01263  -0.00499 0.02514  114 TYR A C   
957  O O   . TYR A 116 ? 0.13443 0.38028 0.27270 0.00322  -0.00783 0.03500  114 TYR A O   
958  C CB  . TYR A 116 ? 0.14070 0.31120 0.27800 -0.00966 -0.01460 0.01476  114 TYR A CB  
959  C CG  . TYR A 116 ? 0.12162 0.30500 0.25876 -0.03215 -0.02324 0.01894  114 TYR A CG  
960  C CD1 . TYR A 116 ? 0.12432 0.28359 0.25850 -0.04473 -0.02906 0.01227  114 TYR A CD1 
961  C CD2 . TYR A 116 ? 0.13439 0.35169 0.27529 -0.04094 -0.02581 0.02908  114 TYR A CD2 
962  C CE1 . TYR A 116 ? 0.18894 0.35212 0.32470 -0.06597 -0.03683 0.01520  114 TYR A CE1 
963  C CE2 . TYR A 116 ? 0.13221 0.35780 0.27367 -0.06437 -0.03440 0.03035  114 TYR A CE2 
964  C CZ  . TYR A 116 ? 0.16839 0.36330 0.30755 -0.07653 -0.03951 0.02287  114 TYR A CZ  
965  O OH  . TYR A 116 ? 0.18263 0.37310 0.32054 -0.09693 -0.04635 0.02226  114 TYR A OH  
966  N N   . LYS A 117 ? 0.13752 0.35514 0.27908 0.03314  0.00333  0.02634  115 LYS A N   
967  C CA  . LYS A 117 ? 0.14270 0.40237 0.28893 0.04824  0.01002  0.03852  115 LYS A CA  
968  C C   . LYS A 117 ? 0.17917 0.45298 0.31921 0.05528  0.01335  0.03424  115 LYS A C   
969  O O   . LYS A 117 ? 0.16217 0.48216 0.30481 0.05523  0.01461  0.04733  115 LYS A O   
970  C CB  . LYS A 117 ? 0.20342 0.45466 0.35622 0.07232  0.01932  0.04010  115 LYS A CB  
971  C CG  . LYS A 117 ? 0.25235 0.51498 0.41291 0.06791  0.01715  0.05353  115 LYS A CG  
972  C CD  . LYS A 117 ? 0.22101 0.47741 0.39077 0.09366  0.02708  0.06068  115 LYS A CD  
973  C CE  . LYS A 117 ? 0.37831 0.66698 0.55273 0.11714  0.03614  0.06899  115 LYS A CE  
974  N NZ  . LYS A 117 ? 0.51090 0.84669 0.67881 0.10344  0.03108  0.08129  115 LYS A NZ  
975  N N   . LYS A 118 ? 0.22244 0.46255 0.35435 0.06032  0.01451  0.01672  116 LYS A N   
976  C CA  . LYS A 118 ? 0.17678 0.43585 0.30044 0.06716  0.01749  0.01177  116 LYS A CA  
977  C C   . LYS A 118 ? 0.18029 0.45889 0.30090 0.04551  0.00928  0.02134  116 LYS A C   
978  O O   . LYS A 118 ? 0.18929 0.49639 0.30403 0.04948  0.01163  0.02356  116 LYS A O   
979  C CB  . LYS A 118 ? 0.25962 0.48071 0.37464 0.07753  0.02017  -0.01142 116 LYS A CB  
980  C CG  . LYS A 118 ? 0.42148 0.62563 0.53973 0.10256  0.03059  -0.02165 116 LYS A CG  
981  C CD  . LYS A 118 ? 0.45155 0.70039 0.57612 0.12003  0.03891  -0.00694 116 LYS A CD  
982  C CE  . LYS A 118 ? 0.56709 0.79799 0.69719 0.14870  0.05055  -0.01486 116 LYS A CE  
983  N NZ  . LYS A 118 ? 0.52186 0.78055 0.66592 0.16065  0.05559  0.00705  116 LYS A NZ  
984  N N   . ALA A 119 ? 0.14444 0.40919 0.26917 0.02356  0.00028  0.02740  117 ALA A N   
985  C CA  . ALA A 119 ? 0.17201 0.44986 0.29771 0.00124  -0.00778 0.03923  117 ALA A CA  
986  C C   . ALA A 119 ? 0.17307 0.49328 0.30800 -0.01073 -0.00971 0.05872  117 ALA A C   
987  O O   . ALA A 119 ? 0.14524 0.47640 0.28360 -0.03183 -0.01650 0.07049  117 ALA A O   
988  C CB  . ALA A 119 ? 0.13621 0.37059 0.26196 -0.01519 -0.01621 0.03197  117 ALA A CB  
989  N N   . GLY A 120 ? 0.13570 0.48128 0.27619 0.00171  -0.00410 0.06375  118 GLY A N   
990  C CA  . GLY A 120 ? 0.13689 0.52086 0.28264 -0.00946 -0.00622 0.08096  118 GLY A CA  
991  C C   . GLY A 120 ? 0.13512 0.50707 0.28274 -0.02045 -0.01135 0.08094  118 GLY A C   
992  O O   . GLY A 120 ? 0.16682 0.55815 0.31008 -0.03228 -0.01429 0.09180  118 GLY A O   
993  N N   . GLY A 121 ? 0.13306 0.47437 0.28468 -0.01741 -0.01263 0.06877  119 GLY A N   
994  C CA  . GLY A 121 ? 0.12485 0.46110 0.27716 -0.02750 -0.01728 0.06858  119 GLY A CA  
995  C C   . GLY A 121 ? 0.13068 0.49269 0.28303 -0.01063 -0.01090 0.07850  119 GLY A C   
996  O O   . GLY A 121 ? 0.13308 0.50201 0.28882 0.01426  -0.00162 0.08060  119 GLY A O   
997  N N   . VAL A 122 ? 0.13774 0.51207 0.28496 -0.02365 -0.01580 0.08400  120 VAL A N   
998  C CA  . VAL A 122 ? 0.24794 0.65131 0.39373 -0.01044 -0.01125 0.09675  120 VAL A CA  
999  C C   . VAL A 122 ? 0.18585 0.58331 0.32988 -0.01788 -0.01553 0.09398  120 VAL A C   
1000 O O   . VAL A 122 ? 0.15698 0.54394 0.29521 -0.04092 -0.02399 0.08521  120 VAL A O   
1001 C CB  . VAL A 122 ? 0.16119 0.60203 0.29990 -0.01927 -0.01289 0.11034  120 VAL A CB  
1002 C CG1 . VAL A 122 ? 0.17234 0.64549 0.30872 -0.00741 -0.00933 0.12462  120 VAL A CG1 
1003 C CG2 . VAL A 122 ? 0.16436 0.61758 0.30337 -0.01048 -0.00784 0.11502  120 VAL A CG2 
1004 N N   . GLU A 123 ? 0.14728 0.55046 0.29545 0.00223  -0.00920 0.10156  121 GLU A N   
1005 C CA  . GLU A 123 ? 0.14836 0.55342 0.29351 -0.00415 -0.01273 0.10186  121 GLU A CA  
1006 C C   . GLU A 123 ? 0.16246 0.60357 0.29655 -0.01883 -0.01790 0.11026  121 GLU A C   
1007 O O   . GLU A 123 ? 0.17365 0.64680 0.30603 -0.01012 -0.01420 0.12560  121 GLU A O   
1008 C CB  . GLU A 123 ? 0.15111 0.55201 0.30421 0.02086  -0.00419 0.11169  121 GLU A CB  
1009 C CG  . GLU A 123 ? 0.16452 0.57192 0.31375 0.01409  -0.00752 0.11422  121 GLU A CG  
1010 C CD  . GLU A 123 ? 0.27663 0.68239 0.43378 0.03791  0.00130  0.12982  121 GLU A CD  
1011 O OE1 . GLU A 123 ? 0.36816 0.74647 0.53649 0.05779  0.00949  0.12996  121 GLU A OE1 
1012 O OE2 . GLU A 123 ? 0.22077 0.65079 0.37243 0.03656  0.00040  0.14183  121 GLU A OE2 
1013 N N   . ILE A 124 ? 0.16524 0.60244 0.29139 -0.04023 -0.02588 0.09953  122 ILE A N   
1014 C CA  . ILE A 124 ? 0.18219 0.65243 0.29737 -0.05655 -0.03107 0.10373  122 ILE A CA  
1015 C C   . ILE A 124 ? 0.18802 0.67399 0.29662 -0.05753 -0.03220 0.10462  122 ILE A C   
1016 O O   . ILE A 124 ? 0.20414 0.72694 0.30377 -0.06683 -0.03461 0.11136  122 ILE A O   
1017 C CB  . ILE A 124 ? 0.19646 0.65198 0.30632 -0.08363 -0.03938 0.08914  122 ILE A CB  
1018 C CG1 . ILE A 124 ? 0.18574 0.59740 0.29485 -0.09420 -0.04384 0.06724  122 ILE A CG1 
1019 C CG2 . ILE A 124 ? 0.18947 0.64350 0.30459 -0.08259 -0.03766 0.09541  122 ILE A CG2 
1020 C CD1 . ILE A 124 ? 0.20362 0.59703 0.30717 -0.11963 -0.05190 0.05216  122 ILE A CD1 
1021 N N   . GLY A 125 ? 0.20395 0.66848 0.31671 -0.04817 -0.02997 0.09983  123 GLY A N   
1022 C CA  . GLY A 125 ? 0.18485 0.67069 0.29032 -0.04852 -0.03038 0.10347  123 GLY A CA  
1023 C C   . GLY A 125 ? 0.17277 0.63438 0.28573 -0.03619 -0.02666 0.10151  123 GLY A C   
1024 O O   . GLY A 125 ? 0.16169 0.58735 0.28556 -0.02992 -0.02441 0.09391  123 GLY A O   
1025 N N   . VAL A 126 ? 0.18057 0.66571 0.28738 -0.03390 -0.02574 0.10915  124 VAL A N   
1026 C CA  . VAL A 126 ? 0.17301 0.64199 0.28550 -0.02549 -0.02249 0.10890  124 VAL A CA  
1027 C C   . VAL A 126 ? 0.18224 0.66977 0.27889 -0.04268 -0.02793 0.09534  124 VAL A C   
1028 O O   . VAL A 126 ? 0.19863 0.72505 0.28206 -0.05137 -0.03030 0.09908  124 VAL A O   
1029 C CB  . VAL A 126 ? 0.25677 0.73774 0.37915 -0.00053 -0.01315 0.13778  124 VAL A CB  
1030 C CG1 . VAL A 126 ? 0.21952 0.68574 0.34860 0.00570  -0.00944 0.14010  124 VAL A CG1 
1031 C CG2 . VAL A 126 ? 0.20683 0.66780 0.34399 0.01881  -0.00612 0.14823  124 VAL A CG2 
1032 N N   . ARG A 127 ? 0.17388 0.63511 0.27169 -0.04799 -0.02919 0.07774  125 ARG A N   
1033 C CA  . ARG A 127 ? 0.21591 0.69618 0.29990 -0.05811 -0.03157 0.06631  125 ARG A CA  
1034 C C   . ARG A 127 ? 0.17887 0.66626 0.27172 -0.04114 -0.02426 0.08531  125 ARG A C   
1035 O O   . ARG A 127 ? 0.16486 0.61912 0.27182 -0.03448 -0.02039 0.08244  125 ARG A O   
1036 C CB  . ARG A 127 ? 0.18380 0.63034 0.26193 -0.07476 -0.03702 0.03331  125 ARG A CB  
1037 C CG  . ARG A 127 ? 0.29850 0.72435 0.37090 -0.09152 -0.04346 0.01595  125 ARG A CG  
1038 C CD  . ARG A 127 ? 0.36332 0.75348 0.42733 -0.10577 -0.04781 -0.01551 125 ARG A CD  
1039 N NE  . ARG A 127 ? 0.48127 0.84251 0.54393 -0.11937 -0.05309 -0.02768 125 ARG A NE  
1040 C CZ  . ARG A 127 ? 0.53069 0.90735 0.58444 -0.13371 -0.05754 -0.03367 125 ARG A CZ  
1041 N NH1 . ARG A 127 ? 0.62750 1.04924 0.67028 -0.13760 -0.05731 -0.03215 125 ARG A NH1 
1042 N NH2 . ARG A 127 ? 0.62308 0.97225 0.68035 -0.14470 -0.06220 -0.03972 125 ARG A NH2 
1043 N N   . LYS A 128 ? 0.19308 0.72411 0.27782 -0.03545 -0.02164 0.10541  126 LYS A N   
1044 C CA  . LYS A 128 ? 0.19383 0.73124 0.28787 -0.01889 -0.01398 0.12961  126 LYS A CA  
1045 C C   . LYS A 128 ? 0.25570 0.79095 0.34531 -0.02617 -0.01392 0.11349  126 LYS A C   
1046 O O   . LYS A 128 ? 0.21781 0.77490 0.28876 -0.04186 -0.01931 0.09088  126 LYS A O   
1047 C CB  . LYS A 128 ? 0.21379 0.80278 0.29862 -0.01164 -0.01104 0.15805  126 LYS A CB  
1048 C CG  . LYS A 128 ? 0.23546 0.83320 0.32566 -0.00147 -0.00838 0.17803  126 LYS A CG  
1049 C CD  . LYS A 128 ? 0.21606 0.77798 0.33014 0.02125  0.00013  0.19942  126 LYS A CD  
1050 C CE  . LYS A 128 ? 0.34772 0.91096 0.47285 0.03587  0.00864  0.22631  126 LYS A CE  
1051 N NZ  . LYS A 128 ? 0.30370 0.82987 0.45325 0.05735  0.01857  0.24517  126 LYS A NZ  
1052 N N   . ASN A 129 ? 0.18239 0.69150 0.28965 -0.01463 -0.00632 0.12469  127 ASN A N   
1053 C CA  . ASN A 129 ? 0.18255 0.69567 0.28747 -0.01812 -0.00308 0.11728  127 ASN A CA  
1054 C C   . ASN A 129 ? 0.23257 0.73251 0.32456 -0.03515 -0.00955 0.07733  127 ASN A C   
1055 O O   . ASN A 129 ? 0.23855 0.76854 0.31481 -0.04352 -0.01157 0.06222  127 ASN A O   
1056 C CB  . ASN A 129 ? 0.20207 0.76918 0.29277 -0.01517 -0.00173 0.13747  127 ASN A CB  
1057 C CG  . ASN A 129 ? 0.28014 0.85182 0.38535 0.00335  0.00541  0.17988  127 ASN A CG  
1058 O OD1 . ASN A 129 ? 0.25326 0.78777 0.38098 0.01333  0.01343  0.19362  127 ASN A OD1 
1059 N ND2 . ASN A 129 ? 0.35673 0.97405 0.45013 0.00751  0.00345  0.20143  127 ASN A ND2 
1060 N N   . TYR A 130 ? 0.18731 0.63618 0.28289 -0.03888 -0.01241 0.05959  128 TYR A N   
1061 C CA  . TYR A 130 ? 0.20092 0.62493 0.28378 -0.05358 -0.01877 0.02364  128 TYR A CA  
1062 C C   . TYR A 130 ? 0.23655 0.61602 0.32102 -0.05041 -0.01367 0.00942  128 TYR A C   
1063 O O   . TYR A 130 ? 0.29503 0.66854 0.36724 -0.05877 -0.01641 -0.01749 128 TYR A O   
1064 C CB  . TYR A 130 ? 0.22597 0.62376 0.31276 -0.06004 -0.02484 0.01533  128 TYR A CB  
1065 C CG  . TYR A 130 ? 0.31211 0.67641 0.38971 -0.07489 -0.03139 -0.01770 128 TYR A CG  
1066 C CD1 . TYR A 130 ? 0.24716 0.63361 0.30979 -0.09179 -0.03946 -0.03742 128 TYR A CD1 
1067 C CD2 . TYR A 130 ? 0.28679 0.59414 0.37049 -0.07159 -0.02919 -0.02838 128 TYR A CD2 
1068 C CE1 . TYR A 130 ? 0.48072 0.82272 0.53576 -0.10274 -0.04346 -0.06523 128 TYR A CE1 
1069 C CE2 . TYR A 130 ? 0.39498 0.66988 0.47284 -0.08290 -0.03461 -0.05448 128 TYR A CE2 
1070 C CZ  . TYR A 130 ? 0.52459 0.81790 0.59009 -0.09951 -0.04246 -0.07350 128 TYR A CZ  
1071 O OH  . TYR A 130 ? 0.62762 0.87319 0.68668 -0.10631 -0.04517 -0.09522 128 TYR A OH  
1072 N N   . TYR A 131 ? 0.19694 0.54516 0.29712 -0.03844 -0.00632 0.02604  129 TYR A N   
1073 C CA  . TYR A 131 ? 0.16049 0.46975 0.26470 -0.03653 -0.00217 0.01395  129 TYR A CA  
1074 C C   . TYR A 131 ? 0.23994 0.57087 0.34989 -0.02977 0.00602  0.03266  129 TYR A C   
1075 O O   . TYR A 131 ? 0.18237 0.53925 0.29995 -0.02293 0.00989  0.06133  129 TYR A O   
1076 C CB  . TYR A 131 ? 0.19261 0.45092 0.31092 -0.03108 -0.00066 0.01673  129 TYR A CB  
1077 C CG  . TYR A 131 ? 0.14594 0.38008 0.26190 -0.03620 -0.00723 0.00309  129 TYR A CG  
1078 C CD1 . TYR A 131 ? 0.24932 0.45259 0.36025 -0.04301 -0.01130 -0.02143 129 TYR A CD1 
1079 C CD2 . TYR A 131 ? 0.20905 0.44885 0.33046 -0.03233 -0.00832 0.01711  129 TYR A CD2 
1080 C CE1 . TYR A 131 ? 0.34379 0.52505 0.45428 -0.04812 -0.01686 -0.03024 129 TYR A CE1 
1081 C CE2 . TYR A 131 ? 0.21419 0.43571 0.33425 -0.03763 -0.01374 0.00650  129 TYR A CE2 
1082 C CZ  . TYR A 131 ? 0.26423 0.45566 0.37880 -0.04648 -0.01818 -0.01665 129 TYR A CZ  
1083 O OH  . TYR A 131 ? 0.27710 0.44955 0.39153 -0.05248 -0.02332 -0.02453 129 TYR A OH  
1084 N N   . PRO A 132 ? 0.17004 0.49159 0.27882 -0.03064 0.00938  0.02001  130 PRO A N   
1085 C CA  . PRO A 132 ? 0.18365 0.52342 0.30208 -0.02533 0.01789  0.04147  130 PRO A CA  
1086 C C   . PRO A 132 ? 0.16485 0.46404 0.30488 -0.02000 0.02217  0.06018  130 PRO A C   
1087 O O   . PRO A 132 ? 0.20924 0.46301 0.35433 -0.02058 0.01921  0.04723  130 PRO A O   
1088 C CB  . PRO A 132 ? 0.25807 0.59816 0.36960 -0.02782 0.01968  0.01849  130 PRO A CB  
1089 C CG  . PRO A 132 ? 0.25883 0.55535 0.36609 -0.03142 0.01324  -0.01031 130 PRO A CG  
1090 C CD  . PRO A 132 ? 0.23205 0.52729 0.33269 -0.03569 0.00599  -0.01224 130 PRO A CD  
1091 N N   . ALA A 133 ? 0.19480 0.51123 0.34745 -0.01501 0.02887  0.09127  131 ALA A N   
1092 C CA  . ALA A 133 ? 0.24178 0.51819 0.41609 -0.01094 0.03347  0.10900  131 ALA A CA  
1093 C C   . ALA A 133 ? 0.24258 0.53185 0.42907 -0.01322 0.04086  0.12652  131 ALA A C   
1094 O O   . ALA A 133 ? 0.24297 0.57943 0.42056 -0.01522 0.04327  0.12955  131 ALA A O   
1095 C CB  . ALA A 133 ? 0.19712 0.47356 0.38005 -0.00149 0.03494  0.13414  131 ALA A CB  
1096 N N   . GLU A 134 ? 0.25002 0.49926 0.45723 -0.01392 0.04459  0.13763  132 GLU A N   
1097 C CA  . GLU A 134 ? 0.35042 0.61053 0.57307 -0.01900 0.05147  0.15691  132 GLU A CA  
1098 C C   . GLU A 134 ? 0.23718 0.55141 0.46036 -0.01536 0.05722  0.18971  132 GLU A C   
1099 O O   . GLU A 134 ? 0.27489 0.62735 0.49883 -0.01980 0.06190  0.19905  132 GLU A O   
1100 C CB  . GLU A 134 ? 0.34157 0.54905 0.58827 -0.02147 0.05407  0.16774  132 GLU A CB  
1101 C CG  . GLU A 134 ? 0.54761 0.74811 0.80858 -0.03268 0.05673  0.16732  132 GLU A CG  
1102 C CD  . GLU A 134 ? 0.65286 0.79513 0.93483 -0.03792 0.05674  0.16834  132 GLU A CD  
1103 O OE1 . GLU A 134 ? 0.59402 0.69937 0.87057 -0.03765 0.05079  0.14149  132 GLU A OE1 
1104 O OE2 . GLU A 134 ? 0.63008 0.76435 0.93384 -0.04286 0.06265  0.19601  132 GLU A OE2 
1105 N N   . LYS A 135 ? 0.26677 0.59089 0.48940 -0.00633 0.05713  0.20865  133 LYS A N   
1106 C CA  . LYS A 135 ? 0.28164 0.66701 0.50046 -0.00124 0.06080  0.23883  133 LYS A CA  
1107 C C   . LYS A 135 ? 0.25439 0.66476 0.45607 0.00556  0.05467  0.23240  133 LYS A C   
1108 O O   . LYS A 135 ? 0.22232 0.59786 0.42904 0.01195  0.05200  0.23000  133 LYS A O   
1109 C CB  . LYS A 135 ? 0.29911 0.67132 0.54090 0.00468  0.06682  0.28075  133 LYS A CB  
1110 C CG  . LYS A 135 ? 0.42913 0.79964 0.68116 -0.00270 0.06993  0.29233  133 LYS A CG  
1111 C CD  . LYS A 135 ? 0.48789 0.92191 0.71850 -0.00238 0.06722  0.29604  133 LYS A CD  
1112 C CE  . LYS A 135 ? 0.44702 0.87945 0.68287 -0.01247 0.07001  0.29107  133 LYS A CE  
1113 N NZ  . LYS A 135 ? 0.40952 0.79493 0.65322 -0.02126 0.07061  0.26143  133 LYS A NZ  
1114 N N   . GLY A 136 ? 0.23486 0.69804 0.41037 0.00448  0.04945  0.22474  134 GLY A N   
1115 C CA  . GLY A 136 ? 0.22233 0.71132 0.38025 0.00647  0.04195  0.21387  134 GLY A CA  
1116 C C   . GLY A 136 ? 0.20681 0.66728 0.35944 -0.00044 0.03680  0.17557  134 GLY A C   
1117 O O   . GLY A 136 ? 0.19583 0.62580 0.34534 -0.00703 0.03605  0.14889  134 GLY A O   
1118 N N   . ARG A 137 ? 0.19706 0.66170 0.34438 0.00198  0.03077  0.17212  135 ARG A N   
1119 C CA  . ARG A 137 ? 0.18524 0.62085 0.32169 -0.00484 0.02265  0.13749  135 ARG A CA  
1120 C C   . ARG A 137 ? 0.22810 0.62696 0.37819 0.00356  0.02227  0.14658  135 ARG A C   
1121 O O   . ARG A 137 ? 0.20240 0.60601 0.36770 0.01576  0.02759  0.17825  135 ARG A O   
1122 C CB  . ARG A 137 ? 0.18719 0.67469 0.30109 -0.01369 0.01470  0.12047  135 ARG A CB  
1123 C CG  . ARG A 137 ? 0.29246 0.81843 0.39043 -0.02015 0.01590  0.10737  135 ARG A CG  
1124 C CD  . ARG A 137 ? 0.29827 0.86337 0.37206 -0.03154 0.00697  0.07970  135 ARG A CD  
1125 N NE  . ARG A 137 ? 0.33091 0.93098 0.38792 -0.03566 0.00900  0.06274  135 ARG A NE  
1126 C CZ  . ARG A 137 ? 0.40216 1.06580 0.44232 -0.03593 0.00824  0.07152  135 ARG A CZ  
1127 N NH1 . ARG A 137 ? 0.41367 1.11025 0.44805 -0.03259 0.00338  0.09761  135 ARG A NH1 
1128 N NH2 . ARG A 137 ? 0.40627 1.09822 0.43187 -0.03809 0.01105  0.05284  135 ARG A NH2 
1129 N N   . GLU A 138 ? 0.17125 0.53470 0.31613 -0.00183 0.01647  0.11929  136 GLU A N   
1130 C CA  . GLU A 138 ? 0.23468 0.56279 0.39029 0.00593  0.01650  0.12241  136 GLU A CA  
1131 C C   . GLU A 138 ? 0.19279 0.53867 0.33709 -0.00037 0.00811  0.10792  136 GLU A C   
1132 O O   . GLU A 138 ? 0.15705 0.50646 0.28665 -0.01416 0.00136  0.08188  136 GLU A O   
1133 C CB  . GLU A 138 ? 0.16368 0.42909 0.32680 0.00499  0.01830  0.10575  136 GLU A CB  
1134 C CG  . GLU A 138 ? 0.18160 0.41471 0.35276 0.01337  0.01846  0.10549  136 GLU A CG  
1135 C CD  . GLU A 138 ? 0.22682 0.40408 0.40629 0.01395  0.02070  0.09285  136 GLU A CD  
1136 O OE1 . GLU A 138 ? 0.18779 0.35079 0.36569 0.00547  0.02021  0.08020  136 GLU A OE1 
1137 O OE2 . GLU A 138 ? 0.24772 0.39935 0.43517 0.02360  0.02300  0.09533  136 GLU A OE2 
1138 N N   . ASP A 139 ? 0.16226 0.51806 0.31495 0.00984  0.00885  0.12496  137 ASP A N   
1139 C CA  . ASP A 139 ? 0.15644 0.53426 0.30182 0.00327  0.00127  0.11563  137 ASP A CA  
1140 C C   . ASP A 139 ? 0.19175 0.52395 0.33306 -0.00547 -0.00286 0.08803  137 ASP A C   
1141 O O   . ASP A 139 ? 0.19193 0.47613 0.34038 0.00035  0.00134  0.08266  137 ASP A O   
1142 C CB  . ASP A 139 ? 0.16023 0.55629 0.31888 0.01987  0.00489  0.14159  137 ASP A CB  
1143 C CG  . ASP A 139 ? 0.19500 0.63199 0.35332 0.03004  0.00870  0.17214  137 ASP A CG  
1144 O OD1 . ASP A 139 ? 0.18222 0.64503 0.33049 0.02284  0.00764  0.17410  137 ASP A OD1 
1145 O OD2 . ASP A 139 ? 0.24289 0.68264 0.40838 0.04611  0.01362  0.19395  137 ASP A OD2 
1146 N N   . ALA A 140 ? 0.17247 0.60626 0.21935 0.04695  -0.00087 0.02375  138 ALA A N   
1147 C CA  . ALA A 140 ? 0.14391 0.54909 0.20155 0.04580  -0.00125 0.01356  138 ALA A CA  
1148 C C   . ALA A 140 ? 0.19163 0.58090 0.26602 0.04342  -0.00256 0.01723  138 ALA A C   
1149 O O   . ALA A 140 ? 0.18360 0.58745 0.26288 0.04403  -0.00667 0.01589  138 ALA A O   
1150 C CB  . ALA A 140 ? 0.16445 0.57934 0.21814 0.05063  -0.00571 -0.00653 138 ALA A CB  
1151 N N   . LEU A 141 ? 0.13317 0.49564 0.21602 0.04133  0.00069  0.02141  139 LEU A N   
1152 C CA  . LEU A 141 ? 0.15795 0.51008 0.25598 0.03964  0.00000  0.02245  139 LEU A CA  
1153 C C   . LEU A 141 ? 0.12635 0.47460 0.23435 0.03583  -0.00272 0.01035  139 LEU A C   
1154 O O   . LEU A 141 ? 0.12355 0.46198 0.22754 0.03642  -0.00203 0.00285  139 LEU A O   
1155 C CB  . LEU A 141 ? 0.20415 0.53409 0.30488 0.04130  0.00446  0.03182  139 LEU A CB  
1156 C CG  . LEU A 141 ? 0.23490 0.57036 0.32688 0.04562  0.00510  0.04554  139 LEU A CG  
1157 C CD1 . LEU A 141 ? 0.26197 0.57771 0.35795 0.04999  0.00723  0.05235  139 LEU A CD1 
1158 C CD2 . LEU A 141 ? 0.24537 0.60702 0.33517 0.04878  0.00130  0.05097  139 LEU A CD2 
1159 N N   . VAL A 142 ? 0.12492 0.48369 0.24673 0.03165  -0.00677 0.00918  140 VAL A N   
1160 C CA  . VAL A 142 ? 0.13466 0.49770 0.26792 0.02532  -0.01267 -0.00054 140 VAL A CA  
1161 C C   . VAL A 142 ? 0.13328 0.48903 0.28202 0.01903  -0.00919 0.00628  140 VAL A C   
1162 O O   . VAL A 142 ? 0.12435 0.49012 0.27987 0.01813  -0.00822 0.01335  140 VAL A O   
1163 C CB  . VAL A 142 ? 0.16578 0.55440 0.30319 0.02217  -0.02407 -0.00848 140 VAL A CB  
1164 C CG1 . VAL A 142 ? 0.16817 0.55933 0.31614 0.01319  -0.03576 -0.01929 140 VAL A CG1 
1165 C CG2 . VAL A 142 ? 0.16957 0.56893 0.28834 0.03133  -0.02612 -0.01568 140 VAL A CG2 
1166 N N   . PHE A 143 ? 0.11548 0.45668 0.26808 0.01619  -0.00702 0.00368  141 PHE A N   
1167 C CA  . PHE A 143 ? 0.11305 0.44978 0.27796 0.01049  -0.00218 0.01055  141 PHE A CA  
1168 C C   . PHE A 143 ? 0.11795 0.46891 0.29690 -0.00429 -0.01051 0.00592  141 PHE A C   
1169 O O   . PHE A 143 ? 0.12090 0.47306 0.29648 -0.00653 -0.02073 -0.00598 141 PHE A O   
1170 C CB  . PHE A 143 ? 0.12824 0.43497 0.28527 0.01774  0.00688  0.01299  141 PHE A CB  
1171 C CG  . PHE A 143 ? 0.13716 0.42985 0.28209 0.02730  0.01121  0.01890  141 PHE A CG  
1172 C CD1 . PHE A 143 ? 0.17515 0.46139 0.30685 0.03180  0.01039  0.01721  141 PHE A CD1 
1173 C CD2 . PHE A 143 ? 0.20496 0.49634 0.35147 0.03126  0.01460  0.02616  141 PHE A CD2 
1174 C CE1 . PHE A 143 ? 0.17891 0.45800 0.30129 0.03762  0.01226  0.02482  141 PHE A CE1 
1175 C CE2 . PHE A 143 ? 0.16892 0.45146 0.30447 0.04016  0.01536  0.03170  141 PHE A CE2 
1176 C CZ  . PHE A 143 ? 0.16487 0.44152 0.28960 0.04206  0.01395  0.03191  141 PHE A CZ  
1177 N N   . ASN A 144 ? 0.12832 0.49010 0.32041 -0.01509 -0.00823 0.01420  142 ASN A N   
1178 C CA  . ASN A 144 ? 0.13147 0.50290 0.33556 -0.03621 -0.01587 0.01471  142 ASN A CA  
1179 C C   . ASN A 144 ? 0.14431 0.50499 0.34998 -0.03655 -0.00345 0.02361  142 ASN A C   
1180 O O   . ASN A 144 ? 0.15535 0.51456 0.35875 -0.02549 0.00740  0.03051  142 ASN A O   
1181 C CB  . ASN A 144 ? 0.14863 0.54597 0.36546 -0.05500 -0.02473 0.01934  142 ASN A CB  
1182 C CG  . ASN A 144 ? 0.24131 0.63867 0.46458 -0.08452 -0.03523 0.02296  142 ASN A CG  
1183 O OD1 . ASN A 144 ? 0.25769 0.63729 0.47266 -0.09730 -0.05250 0.01316  142 ASN A OD1 
1184 N ND2 . ASN A 144 ? 0.27540 0.68714 0.50717 -0.09597 -0.02727 0.03618  142 ASN A ND2 
1185 N N   . LEU A 145 ? 0.13025 0.48304 0.33715 -0.04956 -0.00793 0.02202  143 LEU A N   
1186 C CA  . LEU A 145 ? 0.13159 0.47721 0.33977 -0.05421 0.00290  0.03228  143 LEU A CA  
1187 C C   . LEU A 145 ? 0.15645 0.50888 0.37022 -0.08949 -0.00863 0.03990  143 LEU A C   
1188 O O   . LEU A 145 ? 0.21339 0.52432 0.40694 -0.10202 -0.02657 0.02941  143 LEU A O   
1189 C CB  . LEU A 145 ? 0.13116 0.45252 0.33068 -0.04016 0.00859  0.02641  143 LEU A CB  
1190 C CG  . LEU A 145 ? 0.21903 0.52100 0.41314 -0.04406 0.01729  0.03415  143 LEU A CG  
1191 C CD1 . LEU A 145 ? 0.23819 0.54963 0.43420 -0.03412 0.03088  0.04418  143 LEU A CD1 
1192 C CD2 . LEU A 145 ? 0.20526 0.46342 0.37929 -0.02163 0.02026  0.02137  143 LEU A CD2 
1193 N N   . ASN A 146 ? 0.18433 0.55271 0.40322 -0.09805 -0.00058 0.05304  144 ASN A N   
1194 C CA  . ASN A 146 ? 0.20205 0.56918 0.42023 -0.13380 -0.00978 0.06407  144 ASN A CA  
1195 C C   . ASN A 146 ? 0.25840 0.60209 0.46660 -0.14029 -0.00221 0.07226  144 ASN A C   
1196 O O   . ASN A 146 ? 0.22373 0.56785 0.43109 -0.11378 0.01521  0.07257  144 ASN A O   
1197 C CB  . ASN A 146 ? 0.23676 0.64032 0.46488 -0.13880 -0.00437 0.07418  144 ASN A CB  
1198 C CG  . ASN A 146 ? 0.32925 0.75308 0.56602 -0.13622 -0.01348 0.06717  144 ASN A CG  
1199 O OD1 . ASN A 146 ? 0.23294 0.64330 0.46729 -0.15257 -0.03246 0.05977  144 ASN A OD1 
1200 N ND2 . ASN A 146 ? 0.25408 0.70545 0.49723 -0.11486 -0.00291 0.06789  144 ASN A ND2 
1201 N N   . PHE A 147 ? 0.24976 0.55771 0.44164 -0.17417 -0.01838 0.07713  145 PHE A N   
1202 C CA  . PHE A 147 ? 0.27024 0.52858 0.43644 -0.17559 -0.01416 0.08102  145 PHE A CA  
1203 C C   . PHE A 147 ? 0.32699 0.55259 0.47405 -0.21812 -0.03250 0.09249  145 PHE A C   
1204 O O   . PHE A 147 ? 0.34883 0.58728 0.50246 -0.24469 -0.04951 0.09539  145 PHE A O   
1205 C CB  . PHE A 147 ? 0.27028 0.46347 0.40747 -0.14605 -0.01870 0.05885  145 PHE A CB  
1206 C CG  . PHE A 147 ? 0.30576 0.44411 0.41546 -0.15082 -0.04637 0.03954  145 PHE A CG  
1207 C CD1 . PHE A 147 ? 0.36235 0.42854 0.43353 -0.16747 -0.06723 0.03528  145 PHE A CD1 
1208 C CD2 . PHE A 147 ? 0.28578 0.44201 0.40393 -0.13445 -0.05227 0.02452  145 PHE A CD2 
1209 C CE1 . PHE A 147 ? 0.44945 0.46326 0.49115 -0.16605 -0.09551 0.01466  145 PHE A CE1 
1210 C CE2 . PHE A 147 ? 0.31892 0.43033 0.41051 -0.13349 -0.07754 0.00507  145 PHE A CE2 
1211 C CZ  . PHE A 147 ? 0.49079 0.52961 0.54322 -0.14773 -0.10024 -0.00123 145 PHE A CZ  
1212 O OXT . PHE A 147 ? 0.35616 0.54030 0.47915 -0.22746 -0.03171 0.10000  145 PHE A OXT 
1213 N N   . MET B 3   ? 0.87577 1.30845 0.46397 -0.07265 -0.21352 0.04752  1   MET B N   
1214 C CA  . MET B 3   ? 0.96059 1.39604 0.57998 -0.07739 -0.19701 0.04901  1   MET B CA  
1215 C C   . MET B 3   ? 0.98305 1.40850 0.59854 -0.10068 -0.17110 0.04671  1   MET B C   
1216 O O   . MET B 3   ? 1.04612 1.43781 0.62960 -0.10577 -0.16108 0.05739  1   MET B O   
1217 C CB  . MET B 3   ? 1.05320 1.46137 0.66507 -0.06037 -0.20167 0.06630  1   MET B CB  
1218 C CG  . MET B 3   ? 1.04723 1.45213 0.68657 -0.06389 -0.18575 0.06994  1   MET B CG  
1219 S SD  . MET B 3   ? 1.18919 1.55815 0.81770 -0.04577 -0.18810 0.09157  1   MET B SD  
1220 C CE  . MET B 3   ? 0.96900 1.29447 0.53699 -0.04791 -0.18449 0.10581  1   MET B CE  
1221 N N   . LYS B 4   ? 0.81228 1.26491 0.46024 -0.11510 -0.15945 0.03280  2   LYS B N   
1222 C CA  . LYS B 4   ? 0.72579 1.16952 0.37569 -0.13751 -0.13556 0.02963  2   LYS B CA  
1223 C C   . LYS B 4   ? 0.75688 1.21903 0.44771 -0.14319 -0.12489 0.02249  2   LYS B C   
1224 O O   . LYS B 4   ? 0.66650 1.14831 0.38261 -0.13020 -0.13480 0.01960  2   LYS B O   
1225 C CB  . LYS B 4   ? 0.88743 1.34152 0.52647 -0.15421 -0.12997 0.01843  2   LYS B CB  
1226 C CG  . LYS B 4   ? 0.83066 1.32640 0.50300 -0.16052 -0.13074 0.00107  2   LYS B CG  
1227 C CD  . LYS B 4   ? 0.85719 1.36042 0.52092 -0.17996 -0.12090 -0.00928 2   LYS B CD  
1228 C CE  . LYS B 4   ? 0.79361 1.33062 0.46531 -0.17644 -0.13532 -0.02236 2   LYS B CE  
1229 N NZ  . LYS B 4   ? 0.67254 1.24523 0.38582 -0.18047 -0.13011 -0.03572 2   LYS B NZ  
1230 N N   . ILE B 5   ? 0.81181 1.26518 0.50826 -0.16289 -0.10436 0.01932  3   ILE B N   
1231 C CA  . ILE B 5   ? 0.76466 1.23007 0.49488 -0.17093 -0.09228 0.01240  3   ILE B CA  
1232 C C   . ILE B 5   ? 0.82988 1.30870 0.56894 -0.19293 -0.07750 -0.00058 3   ILE B C   
1233 O O   . ILE B 5   ? 0.81853 1.27862 0.53909 -0.20748 -0.06700 0.00049  3   ILE B O   
1234 C CB  . ILE B 5   ? 0.64009 1.07542 0.36999 -0.17236 -0.08222 0.02294  3   ILE B CB  
1235 C CG1 . ILE B 5   ? 0.68110 1.10466 0.40422 -0.14969 -0.09686 0.03636  3   ILE B CG1 
1236 C CG2 . ILE B 5   ? 0.64291 1.08788 0.40378 -0.18176 -0.07036 0.01492  3   ILE B CG2 
1237 C CD1 . ILE B 5   ? 0.63823 1.02809 0.35422 -0.14966 -0.08822 0.04924  3   ILE B CD1 
1238 N N   . ARG B 6   ? 0.69066 1.20077 0.45745 -0.19522 -0.07608 -0.01289 4   ARG B N   
1239 C CA  . ARG B 6   ? 0.65851 1.18676 0.43408 -0.21363 -0.06438 -0.02570 4   ARG B CA  
1240 C C   . ARG B 6   ? 0.62634 1.16961 0.43289 -0.22110 -0.05159 -0.03437 4   ARG B C   
1241 O O   . ARG B 6   ? 0.63830 1.18481 0.46014 -0.20929 -0.05541 -0.03274 4   ARG B O   
1242 C CB  . ARG B 6   ? 0.64586 1.20111 0.41661 -0.20840 -0.07764 -0.03397 4   ARG B CB  
1243 C CG  . ARG B 6   ? 0.67975 1.26146 0.46976 -0.19047 -0.09275 -0.03883 4   ARG B CG  
1244 C CD  . ARG B 6   ? 0.59551 1.20943 0.39138 -0.19171 -0.10019 -0.05240 4   ARG B CD  
1245 N NE  . ARG B 6   ? 0.57350 1.21090 0.38878 -0.17486 -0.11514 -0.05769 4   ARG B NE  
1246 C CZ  . ARG B 6   ? 0.63271 1.29184 0.47720 -0.17592 -0.10766 -0.06758 4   ARG B CZ  
1247 N NH1 . ARG B 6   ? 0.52023 1.18092 0.37672 -0.19246 -0.08592 -0.07311 4   ARG B NH1 
1248 N NH2 . ARG B 6   ? 0.54955 1.22737 0.41067 -0.16004 -0.12213 -0.07200 4   ARG B NH2 
1249 N N   . ASN B 7   ? 0.72144 1.27164 0.53564 -0.24096 -0.03584 -0.04333 5   ASN B N   
1250 C CA  . ASN B 7   ? 0.54653 1.11128 0.38625 -0.24920 -0.02234 -0.05240 5   ASN B CA  
1251 C C   . ASN B 7   ? 0.59611 1.19188 0.45067 -0.23565 -0.03148 -0.06043 5   ASN B C   
1252 O O   . ASN B 7   ? 0.60131 1.21824 0.45200 -0.23005 -0.04270 -0.06597 5   ASN B O   
1253 C CB  . ASN B 7   ? 0.75736 1.32823 0.60146 -0.27190 -0.00553 -0.06123 5   ASN B CB  
1254 C CG  . ASN B 7   ? 0.88681 1.48304 0.72361 -0.27453 -0.01106 -0.06980 5   ASN B CG  
1255 O OD1 . ASN B 7   ? 0.87144 1.46228 0.68693 -0.26836 -0.02396 -0.06541 5   ASN B OD1 
1256 N ND2 . ASN B 7   ? 0.86467 1.48655 0.71718 -0.28402 -0.00056 -0.08227 5   ASN B ND2 
1257 N N   . TRP B 8   ? 0.51831 1.11468 0.38924 -0.22973 -0.02785 -0.06130 6   TRP B N   
1258 C CA  . TRP B 8   ? 0.61996 1.24461 0.50796 -0.22063 -0.03185 -0.07145 6   TRP B CA  
1259 C C   . TRP B 8   ? 0.58456 1.23458 0.48048 -0.23480 -0.01980 -0.08596 6   TRP B C   
1260 O O   . TRP B 8   ? 0.57670 1.21962 0.47112 -0.25291 -0.00258 -0.08822 6   TRP B O   
1261 C CB  . TRP B 8   ? 0.65811 1.27349 0.55914 -0.21555 -0.02601 -0.07027 6   TRP B CB  
1262 C CG  . TRP B 8   ? 0.64239 1.24197 0.54503 -0.23339 -0.00529 -0.07156 6   TRP B CG  
1263 C CD1 . TRP B 8   ? 0.77969 1.36080 0.67312 -0.24954 0.00482  -0.06752 6   TRP B CD1 
1264 C CD2 . TRP B 8   ? 0.66871 1.26824 0.58198 -0.23731 0.00761  -0.07780 6   TRP B CD2 
1265 N NE1 . TRP B 8   ? 0.80075 1.37023 0.70048 -0.26262 0.02245  -0.07031 6   TRP B NE1 
1266 C CE2 . TRP B 8   ? 0.72186 1.30119 0.63113 -0.25499 0.02468  -0.07629 6   TRP B CE2 
1267 C CE3 . TRP B 8   ? 0.75658 1.36930 0.68125 -0.22771 0.00630  -0.08469 6   TRP B CE3 
1268 C CZ2 . TRP B 8   ? 0.78997 1.34386 0.70127 -0.25537 0.03334  -0.08102 6   TRP B CZ2 
1269 C CZ3 . TRP B 8   ? 0.87670 1.48092 0.80412 -0.23555 0.02177  -0.08959 6   TRP B CZ3 
1270 C CH2 . TRP B 8   ? 0.90255 1.47393 0.82193 -0.24790 0.03370  -0.08724 6   TRP B CH2 
1271 N N   . ILE B 9   ? 0.47568 1.15533 0.38187 -0.22623 -0.02874 -0.09638 7   ILE B N   
1272 C CA  . ILE B 9   ? 0.49109 1.19827 0.40620 -0.23703 -0.01908 -0.11195 7   ILE B CA  
1273 C C   . ILE B 9   ? 0.57761 1.30548 0.51143 -0.22836 -0.01960 -0.12258 7   ILE B C   
1274 O O   . ILE B 9   ? 0.63180 1.35752 0.57196 -0.21205 -0.03241 -0.11815 7   ILE B O   
1275 C CB  . ILE B 9   ? 0.49618 1.22011 0.40299 -0.23689 -0.03172 -0.11626 7   ILE B CB  
1276 C CG1 . ILE B 9   ? 0.60339 1.30661 0.49171 -0.25086 -0.02462 -0.10871 7   ILE B CG1 
1277 C CG2 . ILE B 9   ? 0.72929 1.48637 0.64870 -0.24391 -0.02614 -0.13423 7   ILE B CG2 
1278 C CD1 . ILE B 9   ? 0.62613 1.32063 0.51933 -0.27068 0.00074  -0.11136 7   ILE B CD1 
1279 N N   . LYS B 10  ? 0.57357 1.31988 0.51557 -0.24006 -0.00414 -0.13701 8   LYS B N   
1280 C CA  . LYS B 10  ? 0.57592 1.34155 0.53418 -0.23456 -0.00175 -0.14956 8   LYS B CA  
1281 C C   . LYS B 10  ? 0.59595 1.38234 0.56695 -0.21624 -0.02452 -0.15294 8   LYS B C   
1282 O O   . LYS B 10  ? 0.54273 1.33473 0.52700 -0.20597 -0.02801 -0.15636 8   LYS B O   
1283 C CB  . LYS B 10  ? 0.52069 1.30595 0.48247 -0.24958 0.01573  -0.16660 8   LYS B CB  
1284 C CG  . LYS B 10  ? 0.58941 1.39022 0.56451 -0.24726 0.02274  -0.18126 8   LYS B CG  
1285 C CD  . LYS B 10  ? 0.60345 1.41877 0.57717 -0.26286 0.04186  -0.19882 8   LYS B CD  
1286 C CE  . LYS B 10  ? 0.77918 1.56563 0.73893 -0.27298 0.06275  -0.19908 8   LYS B CE  
1287 N NZ  . LYS B 10  ? 0.69469 1.47317 0.65449 -0.28164 0.07186  -0.21455 8   LYS B NZ  
1288 N N   . ASP B 11  ? 0.58099 1.37738 0.54753 -0.21175 -0.04078 -0.15195 9   ASP B N   
1289 C CA  . ASP B 11  ? 0.51723 1.33046 0.49467 -0.19361 -0.06443 -0.15416 9   ASP B CA  
1290 C C   . ASP B 11  ? 0.52788 1.32093 0.50376 -0.17663 -0.07745 -0.13961 9   ASP B C   
1291 O O   . ASP B 11  ? 0.57359 1.37956 0.56363 -0.16097 -0.09365 -0.14217 9   ASP B O   
1292 C CB  . ASP B 11  ? 0.50605 1.32846 0.47353 -0.19268 -0.08005 -0.15477 9   ASP B CB  
1293 C CG  . ASP B 11  ? 0.52921 1.38026 0.50575 -0.20485 -0.07262 -0.17297 9   ASP B CG  
1294 O OD1 . ASP B 11  ? 0.61192 1.48043 0.60637 -0.20928 -0.06014 -0.18665 9   ASP B OD1 
1295 O OD2 . ASP B 11  ? 0.53498 1.39050 0.50008 -0.20995 -0.07906 -0.17435 9   ASP B OD2 
1296 N N   . ASP B 12  ? 0.46484 1.22646 0.42548 -0.17939 -0.07065 -0.12494 10  ASP B N   
1297 C CA  . ASP B 12  ? 0.45689 1.19749 0.41523 -0.16353 -0.08223 -0.11096 10  ASP B CA  
1298 C C   . ASP B 12  ? 0.51834 1.25964 0.49365 -0.15809 -0.07583 -0.11436 10  ASP B C   
1299 O O   . ASP B 12  ? 0.45198 1.18641 0.43338 -0.14164 -0.08866 -0.10737 10  ASP B O   
1300 C CB  . ASP B 12  ? 0.52010 1.22650 0.45755 -0.16896 -0.07671 -0.09533 10  ASP B CB  
1301 C CG  . ASP B 12  ? 0.54640 1.24607 0.46287 -0.17156 -0.08554 -0.08933 10  ASP B CG  
1302 O OD1 . ASP B 12  ? 0.49972 1.21231 0.41415 -0.16063 -0.10424 -0.09088 10  ASP B OD1 
1303 O OD2 . ASP B 12  ? 0.49446 1.17406 0.39573 -0.18459 -0.07414 -0.08304 10  ASP B OD2 
1304 N N   . VAL B 13  ? 0.44651 1.19403 0.42775 -0.17165 -0.05602 -0.12477 11  VAL B N   
1305 C CA  . VAL B 13  ? 0.42577 1.16649 0.41630 -0.16944 -0.04704 -0.12676 11  VAL B CA  
1306 C C   . VAL B 13  ? 0.48432 1.24134 0.49402 -0.15189 -0.06156 -0.13122 11  VAL B C   
1307 O O   . VAL B 13  ? 0.50643 1.24905 0.52040 -0.14286 -0.06302 -0.12520 11  VAL B O   
1308 C CB  . VAL B 13  ? 0.39420 1.14196 0.38558 -0.18691 -0.02439 -0.13990 11  VAL B CB  
1309 C CG1 . VAL B 13  ? 0.45219 1.19458 0.45145 -0.18383 -0.01702 -0.14388 11  VAL B CG1 
1310 C CG2 . VAL B 13  ? 0.42973 1.15386 0.40320 -0.20266 -0.00967 -0.13252 11  VAL B CG2 
1311 N N   . PRO B 14  ? 0.45311 1.23897 0.47607 -0.14612 -0.07320 -0.14159 12  PRO B N   
1312 C CA  . PRO B 14  ? 0.45838 1.25607 0.50063 -0.12807 -0.08893 -0.14352 12  PRO B CA  
1313 C C   . PRO B 14  ? 0.46312 1.23730 0.49880 -0.11153 -0.10534 -0.12538 12  PRO B C   
1314 O O   . PRO B 14  ? 0.41708 1.18139 0.46116 -0.10167 -0.10673 -0.12123 12  PRO B O   
1315 C CB  . PRO B 14  ? 0.44679 1.27645 0.50201 -0.12629 -0.10006 -0.15642 12  PRO B CB  
1316 C CG  . PRO B 14  ? 0.44462 1.28597 0.49579 -0.14595 -0.08115 -0.16905 12  PRO B CG  
1317 C CD  . PRO B 14  ? 0.43593 1.24771 0.46205 -0.15659 -0.07013 -0.15558 12  PRO B CD  
1318 N N   . GLN B 15  ? 0.46107 1.22401 0.48019 -0.10868 -0.11696 -0.11447 13  GLN B N   
1319 C CA  . GLN B 15  ? 0.45027 1.19101 0.46240 -0.09219 -0.13300 -0.09806 13  GLN B CA  
1320 C C   . GLN B 15  ? 0.43481 1.14314 0.43514 -0.09394 -0.12308 -0.08522 13  GLN B C   
1321 O O   . GLN B 15  ? 0.42950 1.12095 0.43163 -0.07931 -0.13267 -0.07441 13  GLN B O   
1322 C CB  . GLN B 15  ? 0.47708 1.21423 0.47182 -0.08872 -0.14860 -0.09096 13  GLN B CB  
1323 C CG  . GLN B 15  ? 0.49913 1.26426 0.50843 -0.08011 -0.16590 -0.10090 13  GLN B CG  
1324 C CD  . GLN B 15  ? 0.52967 1.29331 0.51913 -0.08022 -0.17966 -0.09705 13  GLN B CD  
1325 O OE1 . GLN B 15  ? 0.60530 1.35177 0.57073 -0.09062 -0.17222 -0.09025 13  GLN B OE1 
1326 N NE2 . GLN B 15  ? 0.59021 1.37024 0.58879 -0.06856 -0.20052 -0.10116 13  GLN B NE2 
1327 N N   . VAL B 16  ? 0.42001 1.11853 0.40955 -0.11136 -0.10439 -0.08633 14  VAL B N   
1328 C CA  . VAL B 16  ? 0.39989 1.06853 0.38184 -0.11346 -0.09509 -0.07609 14  VAL B CA  
1329 C C   . VAL B 16  ? 0.38372 1.05355 0.38266 -0.10657 -0.09174 -0.08053 14  VAL B C   
1330 O O   . VAL B 16  ? 0.37504 1.02327 0.37439 -0.09636 -0.09593 -0.07042 14  VAL B O   
1331 C CB  . VAL B 16  ? 0.39101 1.04909 0.35967 -0.13447 -0.07597 -0.07741 14  VAL B CB  
1332 C CG1 . VAL B 16  ? 0.37126 1.00358 0.33809 -0.13806 -0.06484 -0.07195 14  VAL B CG1 
1333 C CG2 . VAL B 16  ? 0.42769 1.07393 0.37652 -0.13940 -0.07999 -0.06840 14  VAL B CG2 
1334 N N   . SER B 17  ? 0.38078 1.07554 0.39347 -0.11232 -0.08382 -0.09631 15  SER B N   
1335 C CA  . SER B 17  ? 0.36854 1.06689 0.39637 -0.10686 -0.08004 -0.10260 15  SER B CA  
1336 C C   . SER B 17  ? 0.37394 1.07470 0.41613 -0.08576 -0.09824 -0.09772 15  SER B C   
1337 O O   . SER B 17  ? 0.36361 1.05387 0.41354 -0.07786 -0.09797 -0.09548 15  SER B O   
1338 C CB  . SER B 17  ? 0.43532 1.16279 0.47442 -0.11740 -0.06850 -0.12205 15  SER B CB  
1339 O OG  . SER B 17  ? 0.49267 1.22599 0.54632 -0.11183 -0.06567 -0.12949 15  SER B OG  
1340 N N   . GLU B 18  ? 0.39262 1.10649 0.43858 -0.07648 -0.11446 -0.09633 16  GLU B N   
1341 C CA  . GLU B 18  ? 0.40058 1.11452 0.45993 -0.05633 -0.13250 -0.09071 16  GLU B CA  
1342 C C   . GLU B 18  ? 0.39643 1.07635 0.44465 -0.04610 -0.13861 -0.07243 16  GLU B C   
1343 O O   . GLU B 18  ? 0.41562 1.08666 0.47562 -0.03318 -0.14377 -0.06836 16  GLU B O   
1344 C CB  . GLU B 18  ? 0.42507 1.15803 0.48832 -0.04969 -0.14945 -0.09291 16  GLU B CB  
1345 C CG  . GLU B 18  ? 0.43101 1.19776 0.50634 -0.05960 -0.14457 -0.11141 16  GLU B CG  
1346 C CD  . GLU B 18  ? 0.54396 1.32877 0.62622 -0.05065 -0.16446 -0.11374 16  GLU B CD  
1347 O OE1 . GLU B 18  ? 0.49550 1.26302 0.56614 -0.03944 -0.18037 -0.09950 16  GLU B OE1 
1348 O OE2 . GLU B 18  ? 0.55737 1.37252 0.65627 -0.05472 -0.16452 -0.12990 16  GLU B OE2 
1349 N N   . ILE B 19  ? 0.40080 1.06135 0.42705 -0.05172 -0.13788 -0.06174 17  ILE B N   
1350 C CA  . ILE B 19  ? 0.39720 1.02530 0.41304 -0.04306 -0.14222 -0.04530 17  ILE B CA  
1351 C C   . ILE B 19  ? 0.40471 1.01642 0.42473 -0.04627 -0.12973 -0.04499 17  ILE B C   
1352 O O   . ILE B 19  ? 0.41987 1.01157 0.44417 -0.03393 -0.13509 -0.03585 17  ILE B O   
1353 C CB  . ILE B 19  ? 0.40716 1.01884 0.39790 -0.05083 -0.14160 -0.03551 17  ILE B CB  
1354 C CG1 . ILE B 19  ? 0.43504 1.05973 0.41742 -0.04702 -0.15573 -0.03509 17  ILE B CG1 
1355 C CG2 . ILE B 19  ? 0.40168 0.97954 0.38280 -0.04320 -0.14359 -0.01955 17  ILE B CG2 
1356 C CD1 . ILE B 19  ? 0.44464 1.05818 0.40136 -0.05996 -0.15051 -0.02993 17  ILE B CD1 
1357 N N   . ALA B 20  ? 0.39649 1.01478 0.41447 -0.06300 -0.11317 -0.05494 18  ALA B N   
1358 C CA  . ALA B 20  ? 0.43034 1.03290 0.45032 -0.06699 -0.10197 -0.05587 18  ALA B CA  
1359 C C   . ALA B 20  ? 0.33726 0.94810 0.37683 -0.05419 -0.10662 -0.06105 18  ALA B C   
1360 O O   . ALA B 20  ? 0.32749 0.91736 0.37006 -0.04577 -0.10837 -0.05438 18  ALA B O   
1361 C CB  . ALA B 20  ? 0.35744 0.96667 0.37073 -0.08768 -0.08363 -0.06659 18  ALA B CB  
1362 N N   . GLU B 21  ? 0.34473 0.98613 0.39885 -0.05253 -0.10886 -0.07347 19  GLU B N   
1363 C CA  . GLU B 21  ? 0.34092 0.99191 0.41488 -0.04136 -0.11227 -0.07963 19  GLU B CA  
1364 C C   . GLU B 21  ? 0.39229 1.02668 0.47330 -0.02138 -0.12824 -0.06654 19  GLU B C   
1365 O O   . GLU B 21  ? 0.33746 0.96418 0.42985 -0.01204 -0.12937 -0.06610 19  GLU B O   
1366 C CB  . GLU B 21  ? 0.35355 1.04167 0.44410 -0.04315 -0.11249 -0.09609 19  GLU B CB  
1367 C CG  . GLU B 21  ? 0.34446 1.04569 0.45596 -0.03604 -0.11093 -0.10653 19  GLU B CG  
1368 C CD  . GLU B 21  ? 0.35414 1.09311 0.48445 -0.03854 -0.11046 -0.12446 19  GLU B CD  
1369 O OE1 . GLU B 21  ? 0.46583 1.22033 0.59234 -0.04672 -0.11042 -0.12942 19  GLU B OE1 
1370 O OE2 . GLU B 21  ? 0.39029 1.14369 0.54010 -0.03252 -0.11006 -0.13436 19  GLU B OE2 
1371 N N   . ALA B 22  ? 0.43362 1.06033 0.50642 -0.01524 -0.14001 -0.05565 20  ALA B N   
1372 C CA  . ALA B 22  ? 0.40969 1.02171 0.48838 0.00328  -0.15568 -0.04350 20  ALA B CA  
1373 C C   . ALA B 22  ? 0.36928 0.94537 0.43779 0.00788  -0.15492 -0.02919 20  ALA B C   
1374 O O   . ALA B 22  ? 0.43900 0.99990 0.51783 0.02220  -0.16219 -0.02220 20  ALA B O   
1375 C CB  . ALA B 22  ? 0.50861 1.12847 0.58070 0.00749  -0.16930 -0.03885 20  ALA B CB  
1376 N N   . ALA B 23  ? 0.36122 0.92320 0.41118 -0.00444 -0.14585 -0.02524 21  ALA B N   
1377 C CA  . ALA B 23  ? 0.37546 0.90448 0.41508 -0.00062 -0.14649 -0.01133 21  ALA B CA  
1378 C C   . ALA B 23  ? 0.32805 0.83990 0.36590 -0.00853 -0.13446 -0.01276 21  ALA B C   
1379 O O   . ALA B 23  ? 0.39202 0.87765 0.43134 -0.00024 -0.13707 -0.00353 21  ALA B O   
1380 C CB  . ALA B 23  ? 0.35904 0.88171 0.37741 -0.00778 -0.14738 -0.00357 21  ALA B CB  
1381 N N   . MET B 24  ? 0.28400 0.56296 0.47789 0.03761  0.05213  -0.03777 22  MET B N   
1382 C CA  . MET B 24  ? 0.31155 0.57027 0.50627 0.03361  0.04936  -0.03761 22  MET B CA  
1383 C C   . MET B 24  ? 0.34914 0.62677 0.53883 0.02922  0.04736  -0.04860 22  MET B C   
1384 O O   . MET B 24  ? 0.29421 0.61103 0.46752 0.01678  0.04886  -0.05662 22  MET B O   
1385 C CB  . MET B 24  ? 0.31257 0.59542 0.49841 0.01594  0.04894  -0.04892 22  MET B CB  
1386 C CG  . MET B 24  ? 0.31572 0.61201 0.50731 0.00070  0.04611  -0.06048 22  MET B CG  
1387 S SD  . MET B 24  ? 0.31910 0.62885 0.50049 -0.03720 0.04579  -0.07142 22  MET B SD  
1388 C CE  . MET B 24  ? 0.41146 0.63711 0.57747 -0.03802 0.03033  -0.06014 22  MET B CE  
1389 N N   . PRO B 25  ? 0.34175 0.60193 0.54107 0.03766  0.04296  -0.04994 23  PRO B N   
1390 C CA  . PRO B 25  ? 0.30106 0.59289 0.49431 0.03061  0.04012  -0.06661 23  PRO B CA  
1391 C C   . PRO B 25  ? 0.22504 0.55870 0.40577 0.00396  0.03983  -0.07018 23  PRO B C   
1392 O O   . PRO B 25  ? 0.20294 0.52862 0.39330 -0.00615 0.03851  -0.06563 23  PRO B O   
1393 C CB  . PRO B 25  ? 0.25322 0.51772 0.46181 0.04184  0.03305  -0.06732 23  PRO B CB  
1394 C CG  . PRO B 25  ? 0.30357 0.52933 0.51861 0.04990  0.03170  -0.04819 23  PRO B CG  
1395 C CD  . PRO B 25  ? 0.35073 0.57200 0.56010 0.05143  0.03934  -0.03502 23  PRO B CD  
1396 N N   . PHE B 26  ? 0.29221 0.67368 0.45182 -0.01101 0.04051  -0.07532 24  PHE B N   
1397 C CA  . PHE B 26  ? 0.18985 0.61253 0.33087 -0.04804 0.03820  -0.06497 24  PHE B CA  
1398 C C   . PHE B 26  ? 0.21837 0.63086 0.35642 -0.07055 0.03923  -0.05494 24  PHE B C   
1399 O O   . PHE B 26  ? 0.23332 0.60145 0.36783 -0.08844 0.03066  -0.04406 24  PHE B O   
1400 C CB  . PHE B 26  ? 0.22792 0.64220 0.37461 -0.05932 0.02857  -0.05701 24  PHE B CB  
1401 C CG  . PHE B 26  ? 0.26364 0.70648 0.41607 -0.04263 0.02738  -0.07227 24  PHE B CG  
1402 C CD1 . PHE B 26  ? 0.38066 0.78303 0.55747 -0.01035 0.02597  -0.08694 24  PHE B CD1 
1403 C CD2 . PHE B 26  ? 0.39654 0.89731 0.52158 -0.05995 0.02537  -0.07061 24  PHE B CD2 
1404 C CE1 . PHE B 26  ? 0.43991 0.85796 0.61696 0.00172  0.02227  -0.10544 24  PHE B CE1 
1405 C CE2 . PHE B 26  ? 0.37845 0.90440 0.50234 -0.04355 0.02341  -0.09134 24  PHE B CE2 
1406 C CZ  . PHE B 26  ? 0.30319 0.78682 0.45449 -0.01357 0.02167  -0.11188 24  PHE B CZ  
1407 N N   . PRO B 27  ? 0.20817 0.62748 0.33419 -0.06506 0.04366  -0.05701 25  PRO B N   
1408 C CA  . PRO B 27  ? 0.27736 0.68707 0.40216 -0.08175 0.04462  -0.05449 25  PRO B CA  
1409 C C   . PRO B 27  ? 0.30483 0.72300 0.41069 -0.13433 0.03707  -0.04163 25  PRO B C   
1410 O O   . PRO B 27  ? 0.32104 0.76818 0.40200 -0.15695 0.03201  -0.02791 25  PRO B O   
1411 C CB  . PRO B 27  ? 0.32975 0.75738 0.44100 -0.06812 0.04717  -0.05536 25  PRO B CB  
1412 C CG  . PRO B 27  ? 0.25880 0.72161 0.35544 -0.06412 0.04561  -0.05517 25  PRO B CG  
1413 C CD  . PRO B 27  ? 0.28021 0.72610 0.39190 -0.04998 0.04532  -0.06147 25  PRO B CD  
1414 N N   . TRP B 28  ? 0.27947 0.64041 0.38394 -0.14698 0.03057  -0.04358 26  TRP B N   
1415 C CA  . TRP B 28  ? 0.32518 0.65014 0.39992 -0.19380 0.01703  -0.03205 26  TRP B CA  
1416 C C   . TRP B 28  ? 0.38384 0.78013 0.44355 -0.22412 0.02073  -0.02863 26  TRP B C   
1417 O O   . TRP B 28  ? 0.46074 0.89281 0.52301 -0.19668 0.03166  -0.04029 26  TRP B O   
1418 C CB  . TRP B 28  ? 0.40163 0.64292 0.47316 -0.18705 0.01071  -0.04622 26  TRP B CB  
1419 C CG  . TRP B 28  ? 0.38194 0.54344 0.46070 -0.15700 0.00466  -0.04525 26  TRP B CG  
1420 C CD1 . TRP B 28  ? 0.43220 0.58594 0.51948 -0.14005 0.00241  -0.03093 26  TRP B CD1 
1421 C CD2 . TRP B 28  ? 0.38040 0.46374 0.45701 -0.14040 -0.00062 -0.05924 26  TRP B CD2 
1422 N NE1 . TRP B 28  ? 0.45203 0.53036 0.54476 -0.11447 -0.00377 -0.03080 26  TRP B NE1 
1423 C CE2 . TRP B 28  ? 0.37521 0.40873 0.46147 -0.11209 -0.00515 -0.04846 26  TRP B CE2 
1424 C CE3 . TRP B 28  ? 0.40619 0.46267 0.47221 -0.14619 -0.00210 -0.08214 26  TRP B CE3 
1425 C CZ2 . TRP B 28  ? 0.50266 0.46421 0.59083 -0.08471 -0.00942 -0.05757 26  TRP B CZ2 
1426 C CZ3 . TRP B 28  ? 0.44113 0.42214 0.50634 -0.11919 -0.00678 -0.09622 26  TRP B CZ3 
1427 C CH2 . TRP B 28  ? 0.48565 0.42104 0.56287 -0.08668 -0.00966 -0.08286 26  TRP B CH2 
1428 N N   . SER B 29  ? 0.41915 0.80673 0.44948 -0.26758 0.00743  -0.00717 27  SER B N   
1429 C CA  . SER B 29  ? 0.38702 0.81688 0.38796 -0.29002 0.00584  0.00132  27  SER B CA  
1430 C C   . SER B 29  ? 0.52371 0.93295 0.52121 -0.30401 0.00513  -0.01610 27  SER B C   
1431 O O   . SER B 29  ? 0.45306 0.79875 0.46319 -0.30794 -0.00020 -0.03388 27  SER B O   
1432 C CB  . SER B 29  ? 0.45047 0.86881 0.42500 -0.33538 -0.01129 0.03210  27  SER B CB  
1433 N N   . GLU B 30  ? 0.41652 0.88179 0.39222 -0.31228 0.00827  -0.01300 28  GLU B N   
1434 C CA  . GLU B 30  ? 0.50521 0.95825 0.47050 -0.33582 0.00539  -0.02679 28  GLU B CA  
1435 C C   . GLU B 30  ? 0.58145 0.95415 0.53207 -0.38549 -0.01585 -0.02056 28  GLU B C   
1436 O O   . GLU B 30  ? 0.64423 0.95787 0.59507 -0.39771 -0.02350 -0.04440 28  GLU B O   
1437 C CB  . GLU B 30  ? 0.53092 1.06376 0.47205 -0.33722 0.01049  -0.02047 28  GLU B CB  
1438 C CG  . GLU B 30  ? 0.61001 1.15775 0.54925 -0.33760 0.01624  -0.04127 28  GLU B CG  
1439 C CD  . GLU B 30  ? 0.73728 1.36489 0.65170 -0.33460 0.01763  -0.03333 28  GLU B CD  
1440 O OE1 . GLU B 30  ? 0.68285 1.33689 0.56894 -0.37015 0.00880  -0.01407 28  GLU B OE1 
1441 O OE2 . GLU B 30  ? 0.67829 1.33912 0.60314 -0.29615 0.02219  -0.04392 28  GLU B OE2 
1442 N N   . LYS B 31  ? 0.62894 0.99311 0.56565 -0.41095 -0.02804 0.01010  29  LYS B N   
1443 C CA  . LYS B 31  ? 0.70745 0.98186 0.63372 -0.45339 -0.05141 0.02129  29  LYS B CA  
1444 C C   . LYS B 31  ? 0.75312 0.92048 0.69683 -0.44064 -0.05929 0.00347  29  LYS B C   
1445 O O   . LYS B 31  ? 0.87732 0.95643 0.81538 -0.45687 -0.07325 -0.01530 29  LYS B O   
1446 C CB  . LYS B 31  ? 0.70017 0.99659 0.61252 -0.47821 -0.06297 0.06365  29  LYS B CB  
1447 C CG  . LYS B 31  ? 0.80245 1.05656 0.69633 -0.53059 -0.08595 0.08487  29  LYS B CG  
1448 C CD  . LYS B 31  ? 0.92225 1.04040 0.82657 -0.54494 -0.10433 0.07397  29  LYS B CD  
1449 C CE  . LYS B 31  ? 1.03891 1.11178 0.93288 -0.59328 -0.12928 0.10596  29  LYS B CE  
1450 N NZ  . LYS B 31  ? 1.05799 0.99133 0.96240 -0.60386 -0.14708 0.08986  29  LYS B NZ  
1451 N N   . PHE B 32  ? 0.65238 0.82401 0.61503 -0.40887 -0.05096 0.00644  30  PHE B N   
1452 C CA  . PHE B 32  ? 0.73941 0.80872 0.71296 -0.39503 -0.05883 -0.00650 30  PHE B CA  
1453 C C   . PHE B 32  ? 0.80185 0.83554 0.77731 -0.37212 -0.05352 -0.05167 30  PHE B C   
1454 O O   . PHE B 32  ? 0.81694 0.74363 0.78719 -0.35841 -0.06350 -0.06837 30  PHE B O   
1455 C CB  . PHE B 32  ? 0.58059 0.67313 0.57313 -0.35548 -0.04834 0.00508  30  PHE B CB  
1456 C CG  . PHE B 32  ? 0.66709 0.65349 0.66577 -0.31985 -0.05441 0.00135  30  PHE B CG  
1457 C CD1 . PHE B 32  ? 0.77224 0.68516 0.76510 -0.34016 -0.07258 0.03261  30  PHE B CD1 
1458 C CD2 . PHE B 32  ? 0.58889 0.55545 0.60166 -0.26593 -0.04241 -0.02862 30  PHE B CD2 
1459 C CE1 . PHE B 32  ? 0.75594 0.57747 0.75652 -0.30363 -0.07737 0.03214  30  PHE B CE1 
1460 C CE2 . PHE B 32  ? 0.59037 0.47020 0.60939 -0.23120 -0.04745 -0.02978 30  PHE B CE2 
1461 C CZ  . PHE B 32  ? 0.69144 0.49835 0.70402 -0.24854 -0.06438 -0.00041 30  PHE B CZ  
1462 N N   . PHE B 33  ? 0.69614 0.82290 0.68007 -0.35708 -0.03631 -0.07019 31  PHE B N   
1463 C CA  . PHE B 33  ? 0.74624 0.85785 0.73189 -0.32930 -0.02985 -0.10931 31  PHE B CA  
1464 C C   . PHE B 33  ? 0.66529 0.71396 0.62428 -0.37290 -0.04795 -0.13176 31  PHE B C   
1465 O O   . PHE B 33  ? 0.80997 0.78633 0.76233 -0.35148 -0.05183 -0.16588 31  PHE B O   
1466 C CB  . PHE B 33  ? 0.53323 0.76756 0.53724 -0.30829 -0.00885 -0.11574 31  PHE B CB  
1467 C CG  . PHE B 33  ? 0.49129 0.74920 0.52596 -0.24716 0.00784  -0.11411 31  PHE B CG  
1468 C CD1 . PHE B 33  ? 0.42754 0.61816 0.47032 -0.20526 0.00812  -0.13078 31  PHE B CD1 
1469 C CD2 . PHE B 33  ? 0.39032 0.73585 0.44687 -0.23101 0.02205  -0.09598 31  PHE B CD2 
1470 C CE1 . PHE B 33  ? 0.45856 0.67136 0.53216 -0.15358 0.02086  -0.12575 31  PHE B CE1 
1471 C CE2 . PHE B 33  ? 0.45395 0.81014 0.54152 -0.17753 0.03433  -0.09578 31  PHE B CE2 
1472 C CZ  . PHE B 33  ? 0.50747 0.79799 0.60403 -0.14205 0.03280  -0.10832 31  PHE B CZ  
1473 N N   . TYR B 34  ? 0.72832 0.79919 0.67287 -0.41138 -0.05658 -0.10739 32  TYR B N   
1474 C CA  . TYR B 34  ? 0.80404 0.80469 0.72890 -0.44446 -0.07571 -0.12214 32  TYR B CA  
1475 C C   . TYR B 34  ? 0.98009 0.84063 0.90396 -0.44624 -0.09550 -0.12397 32  TYR B C   
1476 O O   . TYR B 34  ? 1.10465 0.88066 1.02018 -0.44633 -0.10804 -0.15843 32  TYR B O   
1477 C CB  . TYR B 34  ? 0.84280 0.90070 0.75447 -0.48697 -0.08071 -0.09068 32  TYR B CB  
1478 C CG  . TYR B 34  ? 0.82233 0.99849 0.72686 -0.48705 -0.06355 -0.09487 32  TYR B CG  
1479 C CD1 . TYR B 34  ? 0.90417 1.08588 0.79915 -0.49317 -0.06403 -0.12989 32  TYR B CD1 
1480 C CD2 . TYR B 34  ? 0.71710 0.99939 0.62187 -0.47813 -0.04690 -0.06375 32  TYR B CD2 
1481 C CE1 . TYR B 34  ? 0.78429 1.07851 0.67292 -0.49292 -0.04669 -0.12782 32  TYR B CE1 
1482 C CE2 . TYR B 34  ? 0.68159 1.06547 0.57731 -0.47336 -0.03055 -0.06396 32  TYR B CE2 
1483 C CZ  . TYR B 34  ? 0.79557 1.18725 0.68466 -0.48209 -0.02957 -0.09309 32  TYR B CZ  
1484 O OH  . TYR B 34  ? 0.80222 1.29883 0.68131 -0.47655 -0.01222 -0.08845 32  TYR B OH  
1485 N N   . ASP B 35  ? 0.92096 0.75853 0.85451 -0.44331 -0.09798 -0.08689 33  ASP B N   
1486 C CA  . ASP B 35  ? 1.10252 0.81245 1.03936 -0.43677 -0.11368 -0.08022 33  ASP B CA  
1487 C C   . ASP B 35  ? 1.14254 0.77545 1.07884 -0.38978 -0.10985 -0.12139 33  ASP B C   
1488 O O   . ASP B 35  ? 1.19800 0.71992 1.13471 -0.37709 -0.12182 -0.13531 33  ASP B O   
1489 C CB  . ASP B 35  ? 1.07401 0.79536 1.02133 -0.43691 -0.11438 -0.02914 33  ASP B CB  
1490 C CG  . ASP B 35  ? 1.05022 0.83347 0.99271 -0.47949 -0.12112 0.01310  33  ASP B CG  
1491 O OD1 . ASP B 35  ? 1.24197 1.01370 1.17451 -0.51350 -0.13210 0.00868  33  ASP B OD1 
1492 O OD2 . ASP B 35  ? 1.05205 0.89846 0.99905 -0.47829 -0.11620 0.04954  33  ASP B OD2 
1493 N N   . CYS B 36  ? 0.91394 0.61491 0.85589 -0.35171 -0.08937 -0.13951 34  CYS B N   
1494 C CA  . CYS B 36  ? 0.95500 0.60627 0.90480 -0.28744 -0.08104 -0.16848 34  CYS B CA  
1495 C C   . CYS B 36  ? 1.11530 0.70255 1.04526 -0.28582 -0.08881 -0.22235 34  CYS B C   
1496 O O   . CYS B 36  ? 1.18186 0.71053 1.11440 -0.23450 -0.08588 -0.24767 34  CYS B O   
1497 C CB  . CYS B 36  ? 0.88606 0.64561 0.85892 -0.23941 -0.05601 -0.16753 34  CYS B CB  
1498 S SG  . CYS B 36  ? 0.75190 0.55417 0.74739 -0.22643 -0.04940 -0.11580 34  CYS B SG  
1499 N N   . LEU B 37  ? 1.19324 0.79550 1.10675 -0.33577 -0.09986 -0.23842 35  LEU B N   
1500 C CA  . LEU B 37  ? 1.34503 0.90189 1.24539 -0.32859 -0.11015 -0.28876 35  LEU B CA  
1501 C C   . LEU B 37  ? 1.44750 0.86780 1.35708 -0.31725 -0.12786 -0.30002 35  LEU B C   
1502 O O   . LEU B 37  ? 1.46020 0.83561 1.36528 -0.31239 -0.13893 -0.34600 35  LEU B O   
1503 C CB  . LEU B 37  ? 1.32468 0.95011 1.21599 -0.37805 -0.11779 -0.29150 35  LEU B CB  
1504 C CG  . LEU B 37  ? 1.24920 1.01582 1.13539 -0.37825 -0.09790 -0.30082 35  LEU B CG  
1505 C CD1 . LEU B 37  ? 1.24197 1.02363 1.11942 -0.33205 -0.08652 -0.35143 35  LEU B CD1 
1506 C CD2 . LEU B 37  ? 1.05439 0.92317 0.95973 -0.37369 -0.07716 -0.26133 35  LEU B CD2 
1507 N N   . LYS B 38  ? 1.44003 0.80339 1.36513 -0.31084 -0.12691 -0.25850 36  LYS B N   
1508 C CA  . LYS B 38  ? 1.60041 0.84795 1.53533 -0.30241 -0.13206 -0.25638 36  LYS B CA  
1509 C C   . LYS B 38  ? 1.66571 0.85713 1.59250 -0.23561 -0.11545 -0.28851 36  LYS B C   
1510 O O   . LYS B 38  ? 1.58674 0.82956 1.50003 -0.19651 -0.10164 -0.31277 36  LYS B O   
1511 C CB  . LYS B 38  ? 1.62972 0.85518 1.57752 -0.31954 -0.13812 -0.18940 36  LYS B CB  
1512 C CG  . LYS B 38  ? 1.67899 0.96091 1.62763 -0.38432 -0.15031 -0.15095 36  LYS B CG  
1513 C CD  . LYS B 38  ? 1.61327 0.91056 1.57169 -0.39272 -0.15224 -0.08478 36  LYS B CD  
1514 C CE  . LYS B 38  ? 1.68500 0.87867 1.65505 -0.39210 -0.16264 -0.05851 36  LYS B CE  
1515 N NZ  . LYS B 38  ? 1.68948 0.89235 1.67016 -0.37233 -0.16076 -0.00554 36  LYS B NZ  
1516 N N   . SER B 39  ? 1.71994 0.80910 1.64979 -0.22018 -0.11650 -0.28171 37  SER B N   
1517 C CA  . SER B 39  ? 1.66576 0.70156 1.58366 -0.15563 -0.10192 -0.30607 37  SER B CA  
1518 C C   . SER B 39  ? 1.61210 0.69535 1.54221 -0.10077 -0.09095 -0.27578 37  SER B C   
1519 O O   . SER B 39  ? 1.58008 0.70779 1.52720 -0.11471 -0.09577 -0.23131 37  SER B O   
1520 C CB  . SER B 39  ? 1.74518 0.66513 1.67051 -0.15386 -0.10743 -0.29689 37  SER B CB  
1521 O OG  . SER B 39  ? 1.75999 0.62974 1.66975 -0.09893 -0.09430 -0.33490 37  SER B OG  
1522 N N   . ASN B 40  ? 1.56338 0.64694 1.48629 -0.03850 -0.07602 -0.30091 38  ASN B N   
1523 C CA  . ASN B 40  ? 1.57117 0.70869 1.51311 0.01935  -0.06331 -0.27649 38  ASN B CA  
1524 C C   . ASN B 40  ? 1.46123 0.70845 1.41208 0.02236  -0.05968 -0.27299 38  ASN B C   
1525 O O   . ASN B 40  ? 1.30686 0.61362 1.27607 0.07107  -0.04685 -0.26041 38  ASN B O   
1526 C CB  . ASN B 40  ? 1.54717 0.64585 1.51273 0.02512  -0.06693 -0.21969 38  ASN B CB  
1527 C CG  . ASN B 40  ? 1.49450 0.52078 1.46407 0.06683  -0.05894 -0.21991 38  ASN B CG  
1528 O OD1 . ASN B 40  ? 1.60757 0.56762 1.56152 0.06524  -0.05915 -0.25798 38  ASN B OD1 
1529 N ND2 . ASN B 40  ? 1.36066 0.40274 1.35133 0.10420  -0.05117 -0.17868 38  ASN B ND2 
1530 N N   . TYR B 41  ? 1.10787 1.40559 1.01961 -0.11117 -0.10523 0.22995  39  TYR B N   
1531 C CA  . TYR B 41  ? 1.08103 1.35811 0.92025 -0.12117 -0.11504 0.21580  39  TYR B CA  
1532 C C   . TYR B 41  ? 0.94421 1.27821 0.83178 -0.11088 -0.09924 0.18343  39  TYR B C   
1533 O O   . TYR B 41  ? 0.92753 1.29423 0.87039 -0.09433 -0.06368 0.15467  39  TYR B O   
1534 C CB  . TYR B 41  ? 1.05891 1.26886 0.81537 -0.12374 -0.09571 0.20134  39  TYR B CB  
1535 C CG  . TYR B 41  ? 1.12870 1.27706 0.79222 -0.14599 -0.12520 0.22932  39  TYR B CG  
1536 C CD1 . TYR B 41  ? 1.16656 1.29977 0.82524 -0.15445 -0.14689 0.26807  39  TYR B CD1 
1537 C CD2 . TYR B 41  ? 1.07782 1.18421 0.65971 -0.15860 -0.13178 0.21633  39  TYR B CD2 
1538 C CE1 . TYR B 41  ? 1.19432 1.27720 0.76485 -0.17708 -0.17502 0.29295  39  TYR B CE1 
1539 C CE2 . TYR B 41  ? 1.11634 1.17036 0.61350 -0.18246 -0.15636 0.23775  39  TYR B CE2 
1540 C CZ  . TYR B 41  ? 1.09792 1.14252 0.59216 -0.19109 -0.17670 0.27344  39  TYR B CZ  
1541 O OH  . TYR B 41  ? 1.14601 1.14539 0.59143 -0.20389 -0.18998 0.27578  39  TYR B OH  
1542 N N   . TYR B 42  ? 0.78739 1.13201 0.65007 -0.12259 -0.12511 0.18791  40  TYR B N   
1543 C CA  . TYR B 42  ? 0.76798 1.16292 0.66391 -0.11663 -0.11615 0.16394  40  TYR B CA  
1544 C C   . TYR B 42  ? 0.69201 1.04443 0.50607 -0.12388 -0.12975 0.15931  40  TYR B C   
1545 O O   . TYR B 42  ? 0.69648 1.01193 0.45432 -0.14338 -0.15972 0.18176  40  TYR B O   
1546 C CB  . TYR B 42  ? 0.76989 1.23129 0.73512 -0.12583 -0.13246 0.17508  40  TYR B CB  
1547 C CG  . TYR B 42  ? 0.84972 1.36191 0.91369 -0.11548 -0.11526 0.17304  40  TYR B CG  
1548 C CD1 . TYR B 42  ? 0.82549 1.37948 0.95221 -0.09805 -0.07576 0.14047  40  TYR B CD1 
1549 C CD2 . TYR B 42  ? 0.81064 1.33014 0.90902 -0.12249 -0.13839 0.20193  40  TYR B CD2 
1550 C CE1 . TYR B 42  ? 0.75851 1.35568 0.98026 -0.08938 -0.05667 0.13592  40  TYR B CE1 
1551 C CE2 . TYR B 42  ? 0.79798 1.35987 0.99339 -0.11061 -0.12262 0.20013  40  TYR B CE2 
1552 C CZ  . TYR B 42  ? 0.78753 1.38564 1.04438 -0.09479 -0.08010 0.16659  40  TYR B CZ  
1553 O OH  . TYR B 42  ? 0.66013 1.29714 1.01705 -0.08382 -0.06086 0.16177  40  TYR B OH  
1554 N N   . GLY B 43  ? 0.68804 1.04735 0.49913 -0.10780 -0.10804 0.12918  41  GLY B N   
1555 C CA  . GLY B 43  ? 0.74985 1.07064 0.49441 -0.10931 -0.11943 0.12302  41  GLY B CA  
1556 C C   . GLY B 43  ? 0.66499 1.03509 0.43754 -0.10163 -0.11781 0.11008  41  GLY B C   
1557 O O   . GLY B 43  ? 0.68494 1.12387 0.52932 -0.09211 -0.09965 0.09546  41  GLY B O   
1558 N N   . TRP B 44  ? 0.67384 1.00826 0.38861 -0.10720 -0.13631 0.11558  42  TRP B N   
1559 C CA  . TRP B 44  ? 0.59507 0.96413 0.32058 -0.09800 -0.13570 0.10527  42  TRP B CA  
1560 C C   . TRP B 44  ? 0.75371 1.04993 0.41519 -0.08713 -0.14186 0.09832  42  TRP B C   
1561 O O   . TRP B 44  ? 0.78056 1.00387 0.39057 -0.09593 -0.15176 0.10631  42  TRP B O   
1562 C CB  . TRP B 44  ? 0.59895 0.99045 0.35531 -0.11666 -0.14651 0.12099  42  TRP B CB  
1563 C CG  . TRP B 44  ? 0.67071 1.14419 0.49907 -0.12691 -0.14190 0.12499  42  TRP B CG  
1564 C CD1 . TRP B 44  ? 0.68933 1.24842 0.58731 -0.11983 -0.12362 0.10688  42  TRP B CD1 
1565 C CD2 . TRP B 44  ? 0.62704 1.10165 0.47521 -0.14350 -0.15389 0.14463  42  TRP B CD2 
1566 N NE1 . TRP B 44  ? 0.62979 1.23493 0.59697 -0.12962 -0.11923 0.11131  42  TRP B NE1 
1567 C CE2 . TRP B 44  ? 0.66639 1.22303 0.60351 -0.14293 -0.14073 0.13682  42  TRP B CE2 
1568 C CE3 . TRP B 44  ? 0.69402 1.10278 0.50191 -0.15592 -0.17047 0.16346  42  TRP B CE3 
1569 C CZ2 . TRP B 44  ? 0.60433 1.18092 0.58924 -0.15307 -0.14908 0.15197  42  TRP B CZ2 
1570 C CZ3 . TRP B 44  ? 0.62781 1.06333 0.47490 -0.16776 -0.18203 0.18096  42  TRP B CZ3 
1571 C CH2 . TRP B 44  ? 0.59765 1.11903 0.53254 -0.16578 -0.17501 0.17779  42  TRP B CH2 
1572 N N   . VAL B 45  ? 0.63182 0.95328 0.29921 -0.06703 -0.13636 0.08204  43  VAL B N   
1573 C CA  . VAL B 45  ? 0.68601 0.94759 0.29771 -0.05354 -0.14663 0.07770  43  VAL B CA  
1574 C C   . VAL B 45  ? 0.81124 1.07554 0.42583 -0.05383 -0.15798 0.08938  43  VAL B C   
1575 O O   . VAL B 45  ? 0.75192 1.08028 0.41636 -0.05899 -0.15116 0.09004  43  VAL B O   
1576 C CB  . VAL B 45  ? 0.67687 0.94859 0.29572 -0.02151 -0.12777 0.04261  43  VAL B CB  
1577 C CG1 . VAL B 45  ? 0.67172 0.92454 0.29776 -0.02339 -0.10645 0.02692  43  VAL B CG1 
1578 C CG2 . VAL B 45  ? 0.66825 1.02509 0.34672 -0.00244 -0.11391 0.02366  43  VAL B CG2 
1579 N N   . MET B 46  ? 0.82951 1.02543 0.38773 -0.05026 -0.17420 0.09853  44  MET B N   
1580 C CA  . MET B 46  ? 0.82251 1.01499 0.37128 -0.04625 -0.18481 0.10966  44  MET B CA  
1581 C C   . MET B 46  ? 0.87321 1.06681 0.40275 -0.01395 -0.18964 0.09522  44  MET B C   
1582 O O   . MET B 46  ? 0.84278 0.99035 0.32813 -0.00127 -0.19680 0.08828  44  MET B O   
1583 C CB  . MET B 46  ? 0.84604 0.97176 0.35062 -0.06436 -0.19873 0.13231  44  MET B CB  
1584 C CG  . MET B 46  ? 0.87008 0.99978 0.36659 -0.06404 -0.20635 0.14592  44  MET B CG  
1585 S SD  . MET B 46  ? 0.95548 1.00701 0.39417 -0.08240 -0.22087 0.17197  44  MET B SD  
1586 C CE  . MET B 46  ? 0.92554 1.00454 0.39908 -0.12615 -0.21447 0.18051  44  MET B CE  
1587 N N   . GLU B 47  ? 0.82403 1.07931 0.39114 -0.00126 -0.18453 0.08765  45  GLU B N   
1588 C CA  . GLU B 47  ? 0.82606 1.09900 0.38936 0.03347  -0.18929 0.07212  45  GLU B CA  
1589 C C   . GLU B 47  ? 0.99189 1.22188 0.51312 0.03397  -0.21289 0.09828  45  GLU B C   
1590 O O   . GLU B 47  ? 1.01328 1.26742 0.54961 0.01754  -0.21153 0.11086  45  GLU B O   
1591 C CB  . GLU B 47  ? 0.83339 1.20719 0.46753 0.04835  -0.16696 0.04387  45  GLU B CB  
1592 C CG  . GLU B 47  ? 0.88662 1.29254 0.54122 0.08138  -0.15163 0.00351  45  GLU B CG  
1593 C CD  . GLU B 47  ? 0.88675 1.38711 0.60323 0.10308  -0.13419 -0.02798 45  GLU B CD  
1594 O OE1 . GLU B 47  ? 0.84545 1.41465 0.61693 0.08833  -0.11159 -0.03903 45  GLU B OE1 
1595 O OE2 . GLU B 47  ? 0.99415 1.50266 0.70597 0.13565  -0.14389 -0.04283 45  GLU B OE2 
1596 N N   . SER B 48  ? 1.01425 1.18335 0.48200 0.05399  -0.23322 0.10558  46  SER B N   
1597 C CA  . SER B 48  ? 1.13381 1.26473 0.56183 0.06315  -0.25769 0.13040  46  SER B CA  
1598 C C   . SER B 48  ? 1.05668 1.20980 0.49770 0.11443  -0.26346 0.10756  46  SER B C   
1599 O O   . SER B 48  ? 1.15385 1.29949 0.60709 0.13959  -0.25315 0.07452  46  SER B O   
1600 C CB  . SER B 48  ? 1.23292 1.28531 0.60208 0.05371  -0.26946 0.16016  46  SER B CB  
1601 O OG  . SER B 48  ? 1.21000 1.23479 0.55182 0.06163  -0.28588 0.18798  46  SER B OG  
1602 N N   . ASP B 49  ? 1.21656 1.39022 0.66103 0.12764  -0.27716 0.11946  47  ASP B N   
1603 C CA  . ASP B 49  ? 1.12409 1.31728 0.58274 0.18061  -0.28811 0.09863  47  ASP B CA  
1604 C C   . ASP B 49  ? 0.98653 1.22370 0.48635 0.21511  -0.27018 0.04577  47  ASP B C   
1605 O O   . ASP B 49  ? 1.01404 1.19562 0.51110 0.24333  -0.27293 0.02538  47  ASP B O   
1606 C CB  . ASP B 49  ? 1.25919 1.35237 0.65758 0.20444  -0.31899 0.12377  47  ASP B CB  
1607 C CG  . ASP B 49  ? 1.41671 1.48039 0.77889 0.17391  -0.33586 0.17534  47  ASP B CG  
1608 O OD1 . ASP B 49  ? 1.21657 1.34175 0.59922 0.14956  -0.33223 0.18391  47  ASP B OD1 
1609 O OD2 . ASP B 49  ? 1.54285 1.51268 0.85303 0.17325  -0.35149 0.20344  47  ASP B OD2 
1610 N N   . HIS B 50  ? 0.92941 1.25152 0.48681 0.19938  -0.24048 0.02069  48  HIS B N   
1611 C CA  . HIS B 50  ? 0.87486 1.25102 0.48520 0.22436  -0.21568 -0.03261 48  HIS B CA  
1612 C C   . HIS B 50  ? 0.87789 1.17664 0.47778 0.22200  -0.20148 -0.05107 48  HIS B C   
1613 O O   . HIS B 50  ? 0.84276 1.14840 0.47389 0.24945  -0.18677 -0.09423 48  HIS B O   
1614 C CB  . HIS B 50  ? 0.83720 1.26330 0.47786 0.27199  -0.22511 -0.06103 48  HIS B CB  
1615 C CG  . HIS B 50  ? 0.83078 1.31665 0.48889 0.26683  -0.23213 -0.04253 48  HIS B CG  
1616 N ND1 . HIS B 50  ? 0.79097 1.37138 0.50769 0.25097  -0.20364 -0.06273 48  HIS B ND1 
1617 C CD2 . HIS B 50  ? 0.89709 1.35311 0.52271 0.27123  -0.26037 -0.00671 48  HIS B CD2 
1618 C CE1 . HIS B 50  ? 0.77629 1.38371 0.49257 0.24531  -0.21395 -0.04226 48  HIS B CE1 
1619 N NE2 . HIS B 50  ? 0.86302 1.39543 0.52271 0.25593  -0.24917 -0.00675 48  HIS B NE2 
1620 N N   . HIS B 51  ? 0.80267 1.22852 0.67010 -0.20888 -0.35339 0.24709  49  HIS B N   
1621 C CA  . HIS B 51  ? 0.72384 1.15659 0.65184 -0.17673 -0.33786 0.22113  49  HIS B CA  
1622 C C   . HIS B 51  ? 0.69014 1.08179 0.59379 -0.17612 -0.30308 0.21218  49  HIS B C   
1623 O O   . HIS B 51  ? 0.71025 1.07333 0.56976 -0.19111 -0.29773 0.22987  49  HIS B O   
1624 C CB  . HIS B 51  ? 0.71735 1.17195 0.72953 -0.13586 -0.36800 0.23197  49  HIS B CB  
1625 C CG  . HIS B 51  ? 0.78430 1.20321 0.80485 -0.11818 -0.37635 0.26080  49  HIS B CG  
1626 N ND1 . HIS B 51  ? 0.94766 1.33149 0.90496 -0.14184 -0.37984 0.28909  49  HIS B ND1 
1627 C CD2 . HIS B 51  ? 0.89417 1.30449 0.97649 -0.08290 -0.38034 0.26480  49  HIS B CD2 
1628 C CE1 . HIS B 51  ? 0.91861 1.27198 0.89526 -0.12262 -0.38655 0.31008  49  HIS B CE1 
1629 N NE2 . HIS B 51  ? 0.87118 1.23840 0.92350 -0.08608 -0.38676 0.29703  49  HIS B NE2 
1630 N N   . LEU B 52  ? 0.61457 1.00590 0.54577 -0.16160 -0.27982 0.18262  50  LEU B N   
1631 C CA  . LEU B 52  ? 0.66544 1.02507 0.58018 -0.15823 -0.24904 0.17111  50  LEU B CA  
1632 C C   . LEU B 52  ? 0.64604 0.99455 0.61085 -0.13009 -0.25501 0.18496  50  LEU B C   
1633 O O   . LEU B 52  ? 0.57421 0.93930 0.60209 -0.10573 -0.27277 0.18682  50  LEU B O   
1634 C CB  . LEU B 52  ? 0.52604 0.88437 0.44104 -0.15805 -0.22378 0.13497  50  LEU B CB  
1635 C CG  . LEU B 52  ? 0.68160 1.04186 0.54224 -0.18819 -0.21232 0.11873  50  LEU B CG  
1636 C CD1 . LEU B 52  ? 0.57311 0.91224 0.41816 -0.18928 -0.18259 0.08545  50  LEU B CD1 
1637 C CD2 . LEU B 52  ? 0.60955 0.95129 0.40669 -0.21387 -0.20516 0.13133  50  LEU B CD2 
1638 N N   . VAL B 53  ? 0.57645 0.89863 0.51440 -0.13481 -0.23848 0.19267  51  VAL B N   
1639 C CA  . VAL B 53  ? 0.53909 0.84616 0.51341 -0.11597 -0.24245 0.20953  51  VAL B CA  
1640 C C   . VAL B 53  ? 0.47003 0.76553 0.44648 -0.11112 -0.21368 0.19177  51  VAL B C   
1641 O O   . VAL B 53  ? 0.49619 0.78122 0.50751 -0.09697 -0.21231 0.20010  51  VAL B O   
1642 C CB  . VAL B 53  ? 0.58601 0.87396 0.52610 -0.13036 -0.25702 0.24379  51  VAL B CB  
1643 C CG1 . VAL B 53  ? 0.64830 0.94714 0.58781 -0.13330 -0.29122 0.26440  51  VAL B CG1 
1644 C CG2 . VAL B 53  ? 0.60547 0.88316 0.47700 -0.16035 -0.23451 0.23906  51  VAL B CG2 
1645 N N   . GLY B 54  ? 0.53472 0.83079 0.47380 -0.12290 -0.19169 0.16782  52  GLY B N   
1646 C CA  . GLY B 54  ? 0.47031 0.75858 0.40966 -0.11635 -0.16775 0.15053  52  GLY B CA  
1647 C C   . GLY B 54  ? 0.45160 0.73511 0.34720 -0.12625 -0.14844 0.12315  52  GLY B C   
1648 O O   . GLY B 54  ? 0.50275 0.78603 0.36007 -0.14361 -0.14931 0.11866  52  GLY B O   
1649 N N   . PHE B 55  ? 0.45293 0.72876 0.35297 -0.11551 -0.13153 0.10485  53  PHE B N   
1650 C CA  . PHE B 55  ? 0.47923 0.73833 0.33437 -0.11998 -0.11276 0.07824  53  PHE B CA  
1651 C C   . PHE B 55  ? 0.49717 0.75341 0.35319 -0.10607 -0.09805 0.06974  53  PHE B C   
1652 O O   . PHE B 55  ? 0.40764 0.67725 0.30800 -0.09482 -0.10310 0.08075  53  PHE B O   
1653 C CB  . PHE B 55  ? 0.47893 0.72606 0.33790 -0.12067 -0.11385 0.05675  53  PHE B CB  
1654 C CG  . PHE B 55  ? 0.37506 0.61985 0.28067 -0.10603 -0.11614 0.04756  53  PHE B CG  
1655 C CD1 . PHE B 55  ? 0.47083 0.73347 0.43287 -0.09924 -0.13090 0.05630  53  PHE B CD1 
1656 C CD2 . PHE B 55  ? 0.47908 0.69890 0.37019 -0.09901 -0.10328 0.02852  53  PHE B CD2 
1657 C CE1 . PHE B 55  ? 0.36785 0.62397 0.37076 -0.08995 -0.12804 0.04279  53  PHE B CE1 
1658 C CE2 . PHE B 55  ? 0.50093 0.71373 0.42888 -0.09193 -0.10463 0.01911  53  PHE B CE2 
1659 C CZ  . PHE B 55  ? 0.41236 0.64357 0.39538 -0.08958 -0.11460 0.02496  53  PHE B CZ  
1660 N N   . ILE B 56  ? 0.51053 0.74770 0.31767 -0.10589 -0.07869 0.04951  54  ILE B N   
1661 C CA  . ILE B 56  ? 0.54715 0.78638 0.35067 -0.08809 -0.06484 0.03836  54  ILE B CA  
1662 C C   . ILE B 56  ? 0.68276 0.87555 0.43846 -0.08181 -0.04967 0.00940  54  ILE B C   
1663 O O   . ILE B 56  ? 0.60473 0.76765 0.31923 -0.09461 -0.04068 -0.00047 54  ILE B O   
1664 C CB  . ILE B 56  ? 0.43337 0.69502 0.23639 -0.08707 -0.04629 0.04584  54  ILE B CB  
1665 C CG1 . ILE B 56  ? 0.44038 0.70116 0.26882 -0.05876 -0.02661 0.02885  54  ILE B CG1 
1666 C CG2 . ILE B 56  ? 0.46374 0.71748 0.20178 -0.11077 -0.03299 0.04195  54  ILE B CG2 
1667 C CD1 . ILE B 56  ? 0.40331 0.70317 0.25661 -0.05854 -0.00945 0.03531  54  ILE B CD1 
1668 N N   . VAL B 57  ? 0.53139 0.70410 0.30397 -0.05903 -0.04686 -0.00258 55  VAL B N   
1669 C CA  . VAL B 57  ? 0.51473 0.62985 0.23884 -0.05068 -0.03807 -0.02695 55  VAL B CA  
1670 C C   . VAL B 57  ? 0.61884 0.72417 0.36434 -0.01555 -0.02703 -0.03352 55  VAL B C   
1671 O O   . VAL B 57  ? 0.49409 0.62422 0.29600 -0.00182 -0.03809 -0.02304 55  VAL B O   
1672 C CB  . VAL B 57  ? 0.55309 0.63872 0.28116 -0.05963 -0.05374 -0.03297 55  VAL B CB  
1673 C CG1 . VAL B 57  ? 0.59697 0.61116 0.27221 -0.05133 -0.04403 -0.05428 55  VAL B CG1 
1674 C CG2 . VAL B 57  ? 0.61861 0.72040 0.37048 -0.08032 -0.06145 -0.02522 55  VAL B CG2 
1675 N N   . ILE B 58  ? 0.55098 0.62084 0.25344 -0.00090 -0.00547 -0.05179 56  ILE B N   
1676 C CA  . ILE B 58  ? 0.65595 0.71903 0.38530 0.03921  0.00334  -0.05981 56  ILE B CA  
1677 C C   . ILE B 58  ? 0.68733 0.66539 0.35579 0.05543  0.00756  -0.07963 56  ILE B C   
1678 O O   . ILE B 58  ? 0.84811 0.77417 0.44454 0.03108  0.01310  -0.09136 56  ILE B O   
1679 C CB  . ILE B 58  ? 0.55785 0.66434 0.30878 0.05074  0.03125  -0.06542 56  ILE B CB  
1680 C CG1 . ILE B 58  ? 0.66037 0.72817 0.33614 0.03361  0.05832  -0.08429 56  ILE B CG1 
1681 C CG2 . ILE B 58  ? 0.54263 0.72245 0.34250 0.03076  0.02707  -0.04446 56  ILE B CG2 
1682 C CD1 . ILE B 58  ? 0.67036 0.76037 0.35642 0.04951  0.09445  -0.10145 56  ILE B CD1 
1683 N N   . LEU B 59  ? 0.76025 0.72354 0.45631 0.09621  0.00384  -0.08269 57  LEU B N   
1684 C CA  . LEU B 59  ? 0.87601 0.74954 0.51688 0.12120  0.00568  -0.09833 57  LEU B CA  
1685 C C   . LEU B 59  ? 0.96363 0.84963 0.64285 0.17062  0.02425  -0.10917 57  LEU B C   
1686 O O   . LEU B 59  ? 0.92190 0.87915 0.68432 0.19452  0.01589  -0.09887 57  LEU B O   
1687 C CB  . LEU B 59  ? 0.92151 0.75337 0.55637 0.12374  -0.02791 -0.08788 57  LEU B CB  
1688 C CG  . LEU B 59  ? 1.03216 0.77494 0.62711 0.15780  -0.04056 -0.09298 57  LEU B CG  
1689 C CD1 . LEU B 59  ? 1.10153 0.77437 0.63471 0.12668  -0.06484 -0.08938 57  LEU B CD1 
1690 C CD2 . LEU B 59  ? 0.97897 0.76951 0.65572 0.20413  -0.05766 -0.08038 57  LEU B CD2 
1691 N N   . MET B 60  ? 1.05510 0.87344 0.67647 0.18555  0.05110  -0.13227 58  MET B N   
1692 C CA  . MET B 60  ? 1.07935 0.90932 0.74128 0.23500  0.07613  -0.14909 58  MET B CA  
1693 C C   . MET B 60  ? 1.23488 0.97689 0.87663 0.28454  0.06202  -0.15403 58  MET B C   
1694 O O   . MET B 60  ? 1.28816 0.92140 0.83736 0.28097  0.07239  -0.16848 58  MET B O   
1695 C CB  . MET B 60  ? 1.14660 0.96542 0.76264 0.21711  0.12315  -0.17458 58  MET B CB  
1696 C CG  . MET B 60  ? 1.10826 1.01018 0.74078 0.16968  0.13236  -0.16563 58  MET B CG  
1697 S SD  . MET B 60  ? 1.23637 1.21825 0.92634 0.18162  0.17835  -0.18558 58  MET B SD  
1698 C CE  . MET B 60  ? 1.24109 1.12748 0.82933 0.17350  0.22625  -0.22285 58  MET B CE  
1699 N N   . GLN B 61  ? 1.36670 1.15518 1.09306 0.32986  0.03784  -0.14156 59  GLN B N   
1700 C CA  . GLN B 61  ? 1.44650 1.16173 1.16623 0.38008  0.01034  -0.13653 59  GLN B CA  
1701 C C   . GLN B 61  ? 1.42085 1.19348 1.23769 0.44652  0.02014  -0.14648 59  GLN B C   
1702 O O   . GLN B 61  ? 1.27637 1.17155 1.18890 0.44921  0.02858  -0.14572 59  GLN B O   
1703 C CB  . GLN B 61  ? 1.41405 1.13039 1.14150 0.36697  -0.04226 -0.10613 59  GLN B CB  
1704 C CG  . GLN B 61  ? 1.39278 1.22528 1.23729 0.38971  -0.06782 -0.08746 59  GLN B CG  
1705 C CD  . GLN B 61  ? 1.25252 1.19925 1.15288 0.34703  -0.05547 -0.08176 59  GLN B CD  
1706 O OE1 . GLN B 61  ? 1.23753 1.19060 1.10463 0.30985  -0.02571 -0.09210 59  GLN B OE1 
1707 N NE2 . GLN B 61  ? 1.10510 1.13775 1.08565 0.35064  -0.08059 -0.06378 59  GLN B NE2 
1708 N N   . GLU B 62  ? 1.49777 1.18012 1.29056 0.50034  0.01859  -0.15643 60  GLU B N   
1709 C CA  . GLU B 62  ? 1.52186 1.26019 1.41717 0.56089  0.02757  -0.16589 60  GLU B CA  
1710 C C   . GLU B 62  ? 1.43810 1.27494 1.39413 0.55505  0.08291  -0.19509 60  GLU B C   
1711 O O   . GLU B 62  ? 1.43539 1.22162 1.32852 0.53594  0.12988  -0.22242 60  GLU B O   
1712 C CB  . GLU B 62  ? 1.50599 1.32593 1.49735 0.58055  -0.02372 -0.13476 60  GLU B CB  
1713 C CG  . GLU B 62  ? 1.62287 1.34458 1.56837 0.59482  -0.07340 -0.10856 60  GLU B CG  
1714 C CD  . GLU B 62  ? 1.69582 1.45392 1.65364 0.56983  -0.12681 -0.07477 60  GLU B CD  
1715 O OE1 . GLU B 62  ? 1.70551 1.59081 1.76738 0.56858  -0.13701 -0.06422 60  GLU B OE1 
1716 O OE2 . GLU B 62  ? 1.78477 1.44161 1.64291 0.54311  -0.15507 -0.06041 60  GLU B OE2 
1717 N N   . LYS B 63  ? 1.35150 1.32770 1.42323 0.56040  0.07837  -0.18894 61  LYS B N   
1718 C CA  . LYS B 63  ? 1.29134 1.37135 1.41414 0.53852  0.12721  -0.21250 61  LYS B CA  
1719 C C   . LYS B 63  ? 1.18240 1.35134 1.32040 0.48544  0.11395  -0.19259 61  LYS B C   
1720 O O   . LYS B 63  ? 0.97381 1.22220 1.13814 0.45276  0.15019  -0.20601 61  LYS B O   
1721 C CB  . LYS B 63  ? 1.15831 1.32516 1.40635 0.57158  0.14315  -0.22390 61  LYS B CB  
1722 C CG  . LYS B 63  ? 1.22256 1.31884 1.46915 0.60758  0.17905  -0.25244 61  LYS B CG  
1723 C CD  . LYS B 63  ? 1.20392 1.30402 1.41844 0.57647  0.24895  -0.29243 61  LYS B CD  
1724 C CE  . LYS B 63  ? 1.23150 1.31506 1.50172 0.61360  0.29203  -0.32534 61  LYS B CE  
1725 N NZ  . LYS B 63  ? 1.23761 1.40564 1.55406 0.58758  0.35650  -0.35627 61  LYS B NZ  
1726 N N   . GLU B 64  ? 1.21660 1.36599 1.33381 0.46612  0.06382  -0.15915 62  GLU B N   
1727 C CA  . GLU B 64  ? 1.16357 1.38088 1.29282 0.41059  0.04926  -0.13701 62  GLU B CA  
1728 C C   . GLU B 64  ? 1.19811 1.34463 1.22313 0.35299  0.05417  -0.13104 62  GLU B C   
1729 O O   . GLU B 64  ? 1.20159 1.24935 1.14102 0.35044  0.06691  -0.14348 62  GLU B O   
1730 C CB  . GLU B 64  ? 1.09879 1.34295 1.27162 0.41943  -0.00473 -0.10726 62  GLU B CB  
1731 C CG  . GLU B 64  ? 1.11996 1.41991 1.38856 0.48024  -0.02245 -0.10846 62  GLU B CG  
1732 C CD  . GLU B 64  ? 1.01238 1.44281 1.38156 0.46545  0.00159  -0.11544 62  GLU B CD  
1733 O OE1 . GLU B 64  ? 0.99040 1.45339 1.37014 0.46150  0.05139  -0.14322 62  GLU B OE1 
1734 O OE2 . GLU B 64  ? 0.88485 1.37783 1.31346 0.45127  -0.02746 -0.09384 62  GLU B OE2 
1735 N N   . CYS B 65  ? 0.89843 1.09898 0.93331 0.30552  0.04422  -0.11242 63  CYS B N   
1736 C CA  . CYS B 65  ? 0.77312 0.92263 0.72981 0.25483  0.03778  -0.10168 63  CYS B CA  
1737 C C   . CYS B 65  ? 0.60778 0.79631 0.59627 0.22975  0.00335  -0.07461 63  CYS B C   
1738 O O   . CYS B 65  ? 0.53764 0.80165 0.60250 0.24100  -0.00767 -0.06546 63  CYS B O   
1739 C CB  . CYS B 65  ? 0.85542 1.02398 0.77855 0.21634  0.07425  -0.11245 63  CYS B CB  
1740 S SG  . CYS B 65  ? 0.84014 1.12901 0.84374 0.20826  0.10202  -0.11680 63  CYS B SG  
1741 N N   . GLN B 66  ? 0.55997 0.69669 0.48940 0.19409  -0.01160 -0.06463 64  GLN B N   
1742 C CA  . GLN B 66  ? 0.54533 0.70050 0.49414 0.16833  -0.04054 -0.04351 64  GLN B CA  
1743 C C   . GLN B 66  ? 0.45362 0.61058 0.37191 0.12263  -0.03429 -0.03752 64  GLN B C   
1744 O O   . GLN B 66  ? 0.56021 0.66514 0.41376 0.10712  -0.02513 -0.04712 64  GLN B O   
1745 C CB  . GLN B 66  ? 0.60679 0.68839 0.51814 0.17507  -0.07090 -0.03902 64  GLN B CB  
1746 C CG  . GLN B 66  ? 0.51856 0.61979 0.45294 0.14770  -0.09756 -0.02109 64  GLN B CG  
1747 C CD  . GLN B 66  ? 0.63759 0.66209 0.52575 0.14849  -0.12680 -0.01778 64  GLN B CD  
1748 O OE1 . GLN B 66  ? 0.69630 0.66381 0.55302 0.18071  -0.13468 -0.02298 64  GLN B OE1 
1749 N NE2 . GLN B 66  ? 0.52168 0.53766 0.40039 0.11104  -0.14146 -0.01005 64  GLN B NE2 
1750 N N   . LEU B 67  ? 0.39508 0.61249 0.36039 0.10140  -0.03960 -0.02159 65  LEU B N   
1751 C CA  . LEU B 67  ? 0.34776 0.56861 0.29627 0.06385  -0.04060 -0.01135 65  LEU B CA  
1752 C C   . LEU B 67  ? 0.40039 0.57633 0.32897 0.04883  -0.06297 -0.00833 65  LEU B C   
1753 O O   . LEU B 67  ? 0.37066 0.55637 0.33185 0.04820  -0.07890 -0.00045 65  LEU B O   
1754 C CB  . LEU B 67  ? 0.30345 0.59246 0.30560 0.04903  -0.03763 0.00469  65  LEU B CB  
1755 C CG  . LEU B 67  ? 0.27813 0.57135 0.27445 0.01597  -0.04363 0.02071  65  LEU B CG  
1756 C CD1 . LEU B 67  ? 0.37241 0.64330 0.31530 0.00219  -0.03503 0.01673  65  LEU B CD1 
1757 C CD2 . LEU B 67  ? 0.32926 0.67704 0.36775 0.00312  -0.03763 0.03607  65  LEU B CD2 
1758 N N   . MET B 68  ? 0.40704 0.53456 0.27917 0.03255  -0.06240 -0.01734 66  MET B N   
1759 C CA  . MET B 68  ? 0.48775 0.57584 0.34150 0.01437  -0.07903 -0.01994 66  MET B CA  
1760 C C   . MET B 68  ? 0.49382 0.61604 0.38155 -0.01286 -0.08473 -0.00951 66  MET B C   
1761 O O   . MET B 68  ? 0.39869 0.51108 0.30189 -0.02630 -0.09530 -0.00978 66  MET B O   
1762 C CB  . MET B 68  ? 0.58465 0.60324 0.36104 0.00558  -0.07541 -0.03820 66  MET B CB  
1763 C CG  . MET B 68  ? 0.52588 0.48951 0.25897 0.03527  -0.06937 -0.04976 66  MET B CG  
1764 S SD  . MET B 68  ? 0.60424 0.56293 0.37342 0.06990  -0.08862 -0.04106 66  MET B SD  
1765 C CE  . MET B 68  ? 0.55716 0.46975 0.29798 0.03648  -0.11159 -0.03991 66  MET B CE  
1766 N N   . ASN B 69  ? 0.38952 0.54807 0.28807 -0.02154 -0.07811 -0.00028 67  ASN B N   
1767 C CA  . ASN B 69  ? 0.28615 0.47106 0.21701 -0.04140 -0.08647 0.01139  67  ASN B CA  
1768 C C   . ASN B 69  ? 0.32809 0.55008 0.26551 -0.04536 -0.08238 0.02813  67  ASN B C   
1769 O O   . ASN B 69  ? 0.41339 0.63150 0.31017 -0.04480 -0.07167 0.02344  67  ASN B O   
1770 C CB  . ASN B 69  ? 0.42044 0.58020 0.32528 -0.06137 -0.09265 -0.00249 67  ASN B CB  
1771 C CG  . ASN B 69  ? 0.33452 0.51029 0.29367 -0.07127 -0.09743 0.00350  67  ASN B CG  
1772 O OD1 . ASN B 69  ? 0.40635 0.60791 0.41131 -0.06649 -0.09934 0.02027  67  ASN B OD1 
1773 N ND2 . ASN B 69  ? 0.40041 0.55645 0.35340 -0.08311 -0.09504 -0.01185 67  ASN B ND2 
1774 N N   . ILE B 70  ? 0.33448 0.58488 0.31651 -0.05172 -0.08957 0.04728  68  ILE B N   
1775 C CA  . ILE B 70  ? 0.33358 0.60908 0.31533 -0.06114 -0.09191 0.06817  68  ILE B CA  
1776 C C   . ILE B 70  ? 0.33106 0.60403 0.35598 -0.06549 -0.10297 0.08205  68  ILE B C   
1777 O O   . ILE B 70  ? 0.34283 0.60866 0.40423 -0.06152 -0.10075 0.08049  68  ILE B O   
1778 C CB  . ILE B 70  ? 0.31970 0.61816 0.30554 -0.05750 -0.07682 0.07627  68  ILE B CB  
1779 C CG1 . ILE B 70  ? 0.28226 0.59547 0.25200 -0.07524 -0.08001 0.09900  68  ILE B CG1 
1780 C CG2 . ILE B 70  ? 0.31150 0.62232 0.34526 -0.05192 -0.07553 0.08002  68  ILE B CG2 
1781 C CD1 . ILE B 70  ? 0.43384 0.76723 0.38299 -0.08121 -0.05813 0.09854  68  ILE B CD1 
1782 N N   . ALA B 71  ? 0.30334 0.57496 0.32231 -0.07215 -0.11275 0.09233  69  ALA B N   
1783 C CA  . ALA B 71  ? 0.32667 0.59241 0.38948 -0.06863 -0.12332 0.10111  69  ALA B CA  
1784 C C   . ALA B 71  ? 0.30319 0.57633 0.35769 -0.07412 -0.13886 0.12445  69  ALA B C   
1785 O O   . ALA B 71  ? 0.33873 0.61647 0.35332 -0.08382 -0.14147 0.12339  69  ALA B O   
1786 C CB  . ALA B 71  ? 0.34325 0.59820 0.42352 -0.06600 -0.12337 0.07629  69  ALA B CB  
1787 N N   . VAL B 72  ? 0.37026 0.64004 0.45934 -0.06968 -0.15005 0.14633  70  VAL B N   
1788 C CA  . VAL B 72  ? 0.43926 0.70857 0.52227 -0.07307 -0.17046 0.17358  70  VAL B CA  
1789 C C   . VAL B 72  ? 0.33759 0.60297 0.47842 -0.05629 -0.18570 0.17814  70  VAL B C   
1790 O O   . VAL B 72  ? 0.47892 0.73604 0.66276 -0.04759 -0.17864 0.17276  70  VAL B O   
1791 C CB  . VAL B 72  ? 0.38664 0.64976 0.44354 -0.08659 -0.17189 0.20294  70  VAL B CB  
1792 C CG1 . VAL B 72  ? 0.42527 0.67618 0.46512 -0.09294 -0.19565 0.23197  70  VAL B CG1 
1793 C CG2 . VAL B 72  ? 0.36466 0.64204 0.37126 -0.10200 -0.15390 0.19373  70  VAL B CG2 
1794 N N   . ALA B 73  ? 0.59481 0.88464 0.46896 0.15246  -0.10315 0.26792  71  ALA B N   
1795 C CA  . ALA B 73  ? 0.60580 0.89606 0.52700 0.17527  -0.10642 0.29004  71  ALA B CA  
1796 C C   . ALA B 73  ? 0.68497 0.92349 0.60501 0.18924  -0.09315 0.31175  71  ALA B C   
1797 O O   . ALA B 73  ? 0.72715 0.94987 0.60897 0.17737  -0.09499 0.32303  71  ALA B O   
1798 C CB  . ALA B 73  ? 0.63670 0.97309 0.56567 0.17097  -0.13059 0.30607  71  ALA B CB  
1799 N N   . PRO B 74  ? 0.69779 0.90644 0.65589 0.21166  -0.07903 0.31605  72  PRO B N   
1800 C CA  . PRO B 74  ? 0.69510 0.84263 0.64493 0.22095  -0.06397 0.33181  72  PRO B CA  
1801 C C   . PRO B 74  ? 0.87304 1.01403 0.80941 0.22342  -0.07928 0.36197  72  PRO B C   
1802 O O   . PRO B 74  ? 0.94723 1.04200 0.85171 0.21675  -0.07233 0.37289  72  PRO B O   
1803 C CB  . PRO B 74  ? 0.85212 0.97662 0.84920 0.24419  -0.04754 0.32627  72  PRO B CB  
1804 C CG  . PRO B 74  ? 0.59756 0.75940 0.61433 0.23934  -0.04626 0.29993  72  PRO B CG  
1805 C CD  . PRO B 74  ? 0.73815 0.96144 0.74221 0.22478  -0.07250 0.30078  72  PRO B CD  
1806 N N   . ARG B 75  ? 0.80386 0.98938 0.76185 0.23070  -0.10077 0.37658  73  ARG B N   
1807 C CA  . ARG B 75  ? 0.84744 1.02912 0.78920 0.23108  -0.11807 0.40673  73  ARG B CA  
1808 C C   . ARG B 75  ? 0.82587 1.01217 0.70957 0.20117  -0.12573 0.40737  73  ARG B C   
1809 O O   . ARG B 75  ? 0.88102 1.04531 0.73817 0.19671  -0.13430 0.43051  73  ARG B O   
1810 C CB  . ARG B 75  ? 0.86867 1.10502 0.84571 0.24227  -0.13984 0.42161  73  ARG B CB  
1811 C CG  . ARG B 75  ? 1.01582 1.24739 1.05107 0.27461  -0.13219 0.42531  73  ARG B CG  
1812 C CD  . ARG B 75  ? 1.05909 1.22041 1.09467 0.29462  -0.12026 0.44168  73  ARG B CD  
1813 N NE  . ARG B 75  ? 1.05128 1.21030 1.14093 0.32780  -0.11583 0.44879  73  ARG B NE  
1814 C CZ  . ARG B 75  ? 1.09546 1.20592 1.19275 0.35023  -0.11399 0.46923  73  ARG B CZ  
1815 N NH1 . ARG B 75  ? 1.18895 1.24734 1.24185 0.34136  -0.11814 0.48680  73  ARG B NH1 
1816 N NH2 . ARG B 75  ? 1.02077 1.13429 1.16971 0.38162  -0.10802 0.47142  73  ARG B NH2 
1817 N N   . TYR B 76  ? 0.81504 1.02728 0.67686 0.18043  -0.12195 0.38100  74  TYR B N   
1818 C CA  . TYR B 76  ? 0.79857 1.02216 0.60688 0.15163  -0.12664 0.37530  74  TYR B CA  
1819 C C   . TYR B 76  ? 0.86397 1.05614 0.64188 0.13864  -0.10431 0.35435  74  TYR B C   
1820 O O   . TYR B 76  ? 0.78011 0.98555 0.51667 0.11520  -0.10330 0.34155  74  TYR B O   
1821 C CB  . TYR B 76  ? 0.78383 1.06584 0.58577 0.13539  -0.14181 0.36013  74  TYR B CB  
1822 C CG  . TYR B 76  ? 0.82059 1.14272 0.64960 0.14236  -0.16511 0.38144  74  TYR B CG  
1823 C CD1 . TYR B 76  ? 0.96482 1.27285 0.81186 0.15996  -0.17452 0.41532  74  TYR B CD1 
1824 C CD2 . TYR B 76  ? 0.81685 1.18974 0.65163 0.13006  -0.17766 0.36734  74  TYR B CD2 
1825 C CE1 . TYR B 76  ? 0.90324 1.25323 0.77763 0.16708  -0.19568 0.43591  74  TYR B CE1 
1826 C CE2 . TYR B 76  ? 0.89112 1.30566 0.75063 0.13343  -0.19830 0.38737  74  TYR B CE2 
1827 C CZ  . TYR B 76  ? 0.94640 1.35257 0.82768 0.15287  -0.20719 0.42232  74  TYR B CZ  
1828 O OH  . TYR B 76  ? 0.89734 1.34977 0.80547 0.15697  -0.22764 0.44352  74  TYR B OH  
1829 N N   . GLN B 77  ? 0.75247 0.90424 0.55019 0.15245  -0.08505 0.34956  75  GLN B N   
1830 C CA  . GLN B 77  ? 0.73602 0.85643 0.50673 0.13908  -0.06341 0.33336  75  GLN B CA  
1831 C C   . GLN B 77  ? 0.80280 0.88889 0.53377 0.12406  -0.06122 0.34993  75  GLN B C   
1832 O O   . GLN B 77  ? 0.89391 0.96120 0.62321 0.13056  -0.07313 0.37690  75  GLN B O   
1833 C CB  . GLN B 77  ? 0.72534 0.80827 0.52640 0.15485  -0.04349 0.32560  75  GLN B CB  
1834 C CG  . GLN B 77  ? 0.65515 0.76878 0.49024 0.16579  -0.04355 0.30616  75  GLN B CG  
1835 C CD  . GLN B 77  ? 0.69871 0.77372 0.55622 0.17571  -0.02109 0.29472  75  GLN B CD  
1836 O OE1 . GLN B 77  ? 0.77572 0.79913 0.62221 0.17284  -0.00469 0.30044  75  GLN B OE1 
1837 N NE2 . GLN B 77  ? 0.67144 0.76929 0.55741 0.18351  -0.02056 0.27717  75  GLN B NE2 
1838 N N   . ARG B 78  ? 0.80775 0.88555 0.50679 0.10342  -0.04574 0.33259  76  ARG B N   
1839 C CA  . ARG B 78  ? 0.93464 0.98102 0.59256 0.08370  -0.04017 0.34223  76  ARG B CA  
1840 C C   . ARG B 78  ? 0.87266 0.93962 0.49977 0.07211  -0.05866 0.35866  76  ARG B C   
1841 O O   . ARG B 78  ? 1.02884 1.06492 0.62338 0.06024  -0.05924 0.37527  76  ARG B O   
1842 C CB  . ARG B 78  ? 0.93121 0.91345 0.59510 0.09149  -0.03197 0.35947  76  ARG B CB  
1843 C CG  . ARG B 78  ? 1.02331 0.98887 0.72401 0.10543  -0.01464 0.34345  76  ARG B CG  
1844 C CD  . ARG B 78  ? 1.04963 0.95079 0.74420 0.10089  0.00042  0.34874  76  ARG B CD  
1845 N NE  . ARG B 78  ? 1.03041 0.92190 0.69193 0.07090  0.01489  0.33324  76  ARG B NE  
1846 C CZ  . ARG B 78  ? 1.04919 0.90464 0.71386 0.06056  0.03270  0.32197  76  ARG B CZ  
1847 N NH1 . ARG B 78  ? 1.03127 0.85506 0.72855 0.07868  0.04160  0.32089  76  ARG B NH1 
1848 N NH2 . ARG B 78  ? 1.09884 0.95140 0.73336 0.02985  0.04198  0.30980  76  ARG B NH2 
1849 N N   . LYS B 79  ? 0.88925 1.00630 0.52427 0.07377  -0.07406 0.35420  77  LYS B N   
1850 C CA  . LYS B 79  ? 0.90335 1.05088 0.50535 0.05611  -0.08837 0.36071  77  LYS B CA  
1851 C C   . LYS B 79  ? 0.88939 1.06248 0.45949 0.03316  -0.07519 0.33055  77  LYS B C   
1852 O O   . LYS B 79  ? 0.94242 1.12537 0.47637 0.01385  -0.07703 0.33387  77  LYS B O   
1853 C CB  . LYS B 79  ? 0.94406 1.13355 0.56846 0.06478  -0.11072 0.36823  77  LYS B CB  
1854 C CG  . LYS B 79  ? 1.02945 1.26725 0.62458 0.04198  -0.11827 0.35156  77  LYS B CG  
1855 C CD  . LYS B 79  ? 1.03076 1.30753 0.64238 0.04472  -0.14264 0.36453  77  LYS B CD  
1856 C CE  . LYS B 79  ? 0.92701 1.24637 0.51249 0.02176  -0.14553 0.33788  77  LYS B CE  
1857 N NZ  . LYS B 79  ? 1.01055 1.32948 0.54798 -0.00249 -0.13322 0.32355  77  LYS B NZ  
1858 N N   . GLY B 80  ? 0.83544 1.01881 0.41988 0.03613  -0.06082 0.30072  78  GLY B N   
1859 C CA  . GLY B 80  ? 0.82343 1.03056 0.38415 0.01942  -0.04713 0.26911  78  GLY B CA  
1860 C C   . GLY B 80  ? 0.78928 1.02900 0.36129 0.02327  -0.05014 0.24203  78  GLY B C   
1861 O O   . GLY B 80  ? 0.78577 1.04451 0.33862 0.01207  -0.04000 0.21294  78  GLY B O   
1862 N N   . VAL B 81  ? 0.76699 1.01048 0.37124 0.03997  -0.06301 0.24998  79  VAL B N   
1863 C CA  . VAL B 81  ? 0.74485 1.01769 0.35598 0.04043  -0.07063 0.22697  79  VAL B CA  
1864 C C   . VAL B 81  ? 0.70410 0.97323 0.31683 0.04185  -0.05178 0.19136  79  VAL B C   
1865 O O   . VAL B 81  ? 0.70863 0.99404 0.30055 0.03137  -0.04870 0.16237  79  VAL B O   
1866 C CB  . VAL B 81  ? 0.72932 1.00884 0.37984 0.05792  -0.08757 0.24399  79  VAL B CB  
1867 C CG1 . VAL B 81  ? 0.70549 1.01086 0.36197 0.05510  -0.09459 0.21754  79  VAL B CG1 
1868 C CG2 . VAL B 81  ? 0.77592 1.06511 0.42632 0.05697  -0.10769 0.27754  79  VAL B CG2 
1869 N N   . ALA B 82  ? 0.66881 0.91308 0.30607 0.05501  -0.03837 0.19252  80  ALA B N   
1870 C CA  . ALA B 82  ? 0.63061 0.87160 0.27398 0.05795  -0.02193 0.16084  80  ALA B CA  
1871 C C   . ALA B 82  ? 0.64544 0.89191 0.26195 0.04399  -0.00568 0.13951  80  ALA B C   
1872 O O   . ALA B 82  ? 0.63438 0.89005 0.24611 0.04349  0.00171  0.10755  80  ALA B O   
1873 C CB  . ALA B 82  ? 0.59595 0.80786 0.26885 0.07141  -0.00991 0.16881  80  ALA B CB  
1874 N N   . SER B 83  ? 0.67338 0.91173 0.27407 0.03352  0.00068  0.15585  81  SER B N   
1875 C CA  . SER B 83  ? 0.69190 0.94155 0.26978 0.02019  0.01579  0.13708  81  SER B CA  
1876 C C   . SER B 83  ? 0.71788 0.99317 0.27086 0.01264  0.01102  0.11471  81  SER B C   
1877 O O   . SER B 83  ? 0.71295 0.99624 0.26211 0.01318  0.02472  0.08334  81  SER B O   
1878 C CB  . SER B 83  ? 0.72868 0.96746 0.28798 0.00703  0.01807  0.16136  81  SER B CB  
1879 O OG  . SER B 83  ? 0.84522 1.05192 0.42278 0.01099  0.02517  0.17707  81  SER B OG  
1880 N N   . GLN B 84  ? 0.75004 1.03598 0.28689 0.00572  -0.00851 0.13073  82  GLN B N   
1881 C CA  . GLN B 84  ? 0.78147 1.08767 0.29121 -0.00532 -0.01456 0.11071  82  GLN B CA  
1882 C C   . GLN B 84  ? 0.75559 1.05937 0.27534 0.00315  -0.01415 0.07987  82  GLN B C   
1883 O O   . GLN B 84  ? 0.77655 1.08367 0.27468 -0.00283 -0.00556 0.04903  82  GLN B O   
1884 C CB  . GLN B 84  ? 0.81788 1.13689 0.31517 -0.01487 -0.03846 0.13807  82  GLN B CB  
1885 C CG  . GLN B 84  ? 0.85443 1.17164 0.33806 -0.02423 -0.04222 0.17065  82  GLN B CG  
1886 C CD  . GLN B 84  ? 0.93423 1.26683 0.40866 -0.03273 -0.06762 0.19898  82  GLN B CD  
1887 O OE1 . GLN B 84  ? 0.92664 1.28232 0.37697 -0.04807 -0.07516 0.18828  82  GLN B OE1 
1888 N NE2 . GLN B 84  ? 0.91071 1.22881 0.40514 -0.02252 -0.08019 0.23510  82  GLN B NE2 
1889 N N   . LEU B 85  ? 0.71633 1.01154 0.26710 0.01678  -0.02358 0.08741  83  LEU B N   
1890 C CA  . LEU B 85  ? 0.69444 0.98403 0.25390 0.02291  -0.02531 0.05883  83  LEU B CA  
1891 C C   . LEU B 85  ? 0.67514 0.95102 0.24007 0.03103  -0.00275 0.02854  83  LEU B C   
1892 O O   . LEU B 85  ? 0.68765 0.95608 0.23988 0.02999  0.00187  -0.00381 83  LEU B O   
1893 C CB  . LEU B 85  ? 0.65520 0.94090 0.25044 0.03606  -0.03874 0.07478  83  LEU B CB  
1894 C CG  . LEU B 85  ? 0.70934 1.01323 0.30764 0.03035  -0.06362 0.09753  83  LEU B CG  
1895 C CD1 . LEU B 85  ? 0.63887 0.94042 0.28011 0.04768  -0.07192 0.12126  83  LEU B CD1 
1896 C CD2 . LEU B 85  ? 0.69276 1.00326 0.27280 0.01718  -0.07454 0.07216  83  LEU B CD2 
1897 N N   . LEU B 86  ? 0.64832 0.91753 0.23386 0.03910  0.01116  0.03968  84  LEU B N   
1898 C CA  . LEU B 86  ? 0.66603 0.92784 0.26337 0.04670  0.03188  0.01544  84  LEU B CA  
1899 C C   . LEU B 86  ? 0.67743 0.94946 0.24795 0.03893  0.04463  -0.00716 84  LEU B C   
1900 O O   . LEU B 86  ? 0.68677 0.95126 0.25945 0.04657  0.05511  -0.03776 84  LEU B O   
1901 C CB  . LEU B 86  ? 0.60417 0.85984 0.22431 0.04983  0.04336  0.03561  84  LEU B CB  
1902 C CG  . LEU B 86  ? 0.68160 0.93657 0.31956 0.05554  0.06343  0.01637  84  LEU B CG  
1903 C CD1 . LEU B 86  ? 0.62943 0.87263 0.28557 0.06965  0.06398  -0.01059 84  LEU B CD1 
1904 C CD2 . LEU B 86  ? 0.56355 0.80945 0.22175 0.05263  0.07086  0.03975  84  LEU B CD2 
1905 N N   . GLN B 87  ? 0.70897 0.99586 0.25380 0.02451  0.04410  0.00762  85  GLN B N   
1906 C CA  . GLN B 87  ? 0.80840 1.10691 0.32748 0.01734  0.05863  -0.01396 85  GLN B CA  
1907 C C   . GLN B 87  ? 0.78468 1.07591 0.27771 0.01449  0.05419  -0.04212 85  GLN B C   
1908 O O   . GLN B 87  ? 0.83960 1.12673 0.32259 0.01874  0.07069  -0.07190 85  GLN B O   
1909 C CB  . GLN B 87  ? 0.79716 1.11310 0.29168 0.00021  0.05773  0.00802  85  GLN B CB  
1910 C CG  . GLN B 87  ? 0.94476 1.27651 0.41345 -0.00700 0.07474  -0.01520 85  GLN B CG  
1911 C CD  . GLN B 87  ? 1.00228 1.33510 0.49549 0.00804  0.09773  -0.03882 85  GLN B CD  
1912 O OE1 . GLN B 87  ? 0.83714 1.16732 0.32176 0.01521  0.10995  -0.07055 85  GLN B OE1 
1913 N NE2 . GLN B 87  ? 0.94067 1.27513 0.46492 0.01289  0.10323  -0.02232 85  GLN B NE2 
1914 N N   . HIS B 88  ? 0.79103 1.07865 0.27341 0.00728  0.03225  -0.03298 86  HIS B N   
1915 C CA  . HIS B 88  ? 0.82618 1.10062 0.28189 0.00120  0.02662  -0.05988 86  HIS B CA  
1916 C C   . HIS B 88  ? 0.89030 1.13699 0.36388 0.01699  0.03478  -0.08962 86  HIS B C   
1917 O O   . HIS B 88  ? 0.88116 1.10776 0.33153 0.01668  0.04359  -0.12091 86  HIS B O   
1918 C CB  . HIS B 88  ? 0.87415 1.15458 0.32129 -0.01120 -0.00070 -0.04098 86  HIS B CB  
1919 C CG  . HIS B 88  ? 0.97131 1.24123 0.38119 -0.02552 -0.00780 -0.06399 86  HIS B CG  
1920 N ND1 . HIS B 88  ? 1.05735 1.33838 0.42661 -0.04251 -0.00463 -0.06937 86  HIS B ND1 
1921 C CD2 . HIS B 88  ? 0.90367 1.15040 0.30877 -0.02718 -0.01777 -0.08311 86  HIS B CD2 
1922 C CE1 . HIS B 88  ? 1.05370 1.31833 0.39413 -0.05340 -0.01178 -0.09082 86  HIS B CE1 
1923 N NE2 . HIS B 88  ? 1.02615 1.26800 0.38700 -0.04469 -0.02031 -0.09907 86  HIS B NE2 
1924 N N   . ALA B 89  ? 0.75341 0.99487 0.26687 0.03096  0.03199  -0.07993 87  ALA B N   
1925 C CA  . ALA B 89  ? 0.80997 1.02549 0.34475 0.04643  0.03937  -0.10550 87  ALA B CA  
1926 C C   . ALA B 89  ? 0.87686 1.09183 0.41878 0.05809  0.06484  -0.12431 87  ALA B C   
1927 O O   . ALA B 89  ? 0.89730 1.08770 0.43437 0.06620  0.07371  -0.15414 87  ALA B O   
1928 C CB  . ALA B 89  ? 0.66610 0.87935 0.24125 0.05750  0.03117  -0.08841 87  ALA B CB  
1929 N N   . LEU B 90  ? 0.74593 0.98678 0.29960 0.05840  0.07643  -0.10596 88  LEU B N   
1930 C CA  . LEU B 90  ? 0.73999 0.98997 0.30517 0.06831  0.09979  -0.12000 88  LEU B CA  
1931 C C   . LEU B 90  ? 0.85566 1.10251 0.38357 0.06398  0.11183  -0.14638 88  LEU B C   
1932 O O   . LEU B 90  ? 0.96659 1.20502 0.50311 0.07841  0.12942  -0.17096 88  LEU B O   
1933 C CB  . LEU B 90  ? 0.78591 1.06463 0.36449 0.06269  0.10693  -0.09279 88  LEU B CB  
1934 C CG  . LEU B 90  ? 0.67704 0.95299 0.29598 0.07000  0.10367  -0.07238 88  LEU B CG  
1935 C CD1 . LEU B 90  ? 0.73235 1.02863 0.35840 0.05998  0.11085  -0.04639 88  LEU B CD1 
1936 C CD2 . LEU B 90  ? 0.63316 0.89727 0.28510 0.08915  0.11209  -0.09229 88  LEU B CD2 
1937 N N   . HIS B 91  ? 0.85337 1.10680 0.33999 0.04474  0.10306  -0.14061 89  HIS B N   
1938 C CA  . HIS B 91  ? 0.96824 1.21563 0.41303 0.03838  0.11472  -0.16613 89  HIS B CA  
1939 C C   . HIS B 91  ? 1.07344 1.27788 0.50896 0.04870  0.11760  -0.19948 89  HIS B C   
1940 O O   . HIS B 91  ? 1.16514 1.35682 0.59926 0.06224  0.13901  -0.22577 89  HIS B O   
1941 C CB  . HIS B 91  ? 0.94804 1.20761 0.35034 0.01384  0.09931  -0.15207 89  HIS B CB  
1942 C CG  . HIS B 91  ? 1.02822 1.28664 0.38448 0.00451  0.11218  -0.17567 89  HIS B CG  
1943 N ND1 . HIS B 91  ? 1.12442 1.34636 0.45030 0.00608  0.11495  -0.20728 89  HIS B ND1 
1944 C CD2 . HIS B 91  ? 1.21567 1.50319 0.54910 -0.00729 0.12336  -0.17269 89  HIS B CD2 
1945 C CE1 . HIS B 91  ? 1.24564 1.47432 0.53164 -0.00290 0.12843  -0.22350 89  HIS B CE1 
1946 N NE2 . HIS B 91  ? 1.20482 1.47605 0.49590 -0.01162 0.13377  -0.20323 89  HIS B NE2 
1947 N N   . TYR B 92  ? 1.07130 1.25146 0.50075 0.04229  0.09594  -0.19787 90  TYR B N   
1948 C CA  . TYR B 92  ? 1.16081 1.29265 0.57804 0.04824  0.09564  -0.22739 90  TYR B CA  
1949 C C   . TYR B 92  ? 1.18689 1.30403 0.64792 0.07353  0.11055  -0.24107 90  TYR B C   
1950 O O   . TYR B 92  ? 1.28318 1.36637 0.73374 0.08421  0.12518  -0.26998 90  TYR B O   
1951 C CB  . TYR B 92  ? 1.25699 1.37245 0.66825 0.03496  0.06711  -0.21766 90  TYR B CB  
1952 C CG  . TYR B 92  ? 1.34924 1.41070 0.75081 0.03764  0.06272  -0.24349 90  TYR B CG  
1953 C CD1 . TYR B 92  ? 1.49366 1.51370 0.85804 0.04051  0.07815  -0.27544 90  TYR B CD1 
1954 C CD2 . TYR B 92  ? 1.35602 1.40461 0.78297 0.03627  0.04305  -0.23524 90  TYR B CD2 
1955 C CE1 . TYR B 92  ? 1.58482 1.54720 0.93625 0.04071  0.07356  -0.29707 90  TYR B CE1 
1956 C CE2 . TYR B 92  ? 1.44273 1.43945 0.85925 0.03422  0.03727  -0.25644 90  TYR B CE2 
1957 C CZ  . TYR B 92  ? 1.50485 1.45632 0.88278 0.03549  0.05236  -0.28673 90  TYR B CZ  
1958 O OH  . TYR B 92  ? 1.56440 1.45801 0.92891 0.03016  0.04707  -0.30637 90  TYR B OH  
1959 N N   . ALA B 93  ? 1.07435 1.21514 0.58436 0.08390  0.10683  -0.21931 91  ALA B N   
1960 C CA  . ALA B 93  ? 1.05911 1.19159 0.61451 0.10778  0.11776  -0.22747 91  ALA B CA  
1961 C C   . ALA B 93  ? 1.15952 1.30332 0.71779 0.12157  0.14517  -0.24419 91  ALA B C   
1962 O O   . ALA B 93  ? 1.18480 1.29937 0.75132 0.13842  0.15642  -0.26836 91  ALA B O   
1963 C CB  . ALA B 93  ? 0.89514 1.05458 0.49487 0.11281  0.11039  -0.19798 91  ALA B CB  
1964 N N   . LYS B 94  ? 1.10818 1.29387 0.65971 0.11435  0.15612  -0.23104 92  LYS B N   
1965 C CA  . LYS B 94  ? 0.98077 1.18341 0.53309 0.12566  0.18276  -0.24691 92  LYS B CA  
1966 C C   . LYS B 94  ? 1.12373 1.28868 0.63121 0.12635  0.19476  -0.28089 92  LYS B C   
1967 O O   . LYS B 94  ? 1.10613 1.26541 0.62203 0.14499  0.21772  -0.30273 92  LYS B O   
1968 C CB  . LYS B 94  ? 0.92535 1.17725 0.46930 0.11131  0.18920  -0.22625 92  LYS B CB  
1969 C CG  . LYS B 94  ? 0.99790 1.27528 0.54122 0.12050  0.21697  -0.24174 92  LYS B CG  
1970 C CD  . LYS B 94  ? 0.99244 1.31761 0.57924 0.12541  0.22476  -0.22037 92  LYS B CD  
1971 C CE  . LYS B 94  ? 0.93313 1.29141 0.50271 0.10000  0.21686  -0.19162 92  LYS B CE  
1972 N NZ  . LYS B 94  ? 1.04825 1.41941 0.57050 0.08555  0.22739  -0.20272 92  LYS B NZ  
1973 N N   . THR B 95  ? 1.17649 1.31418 0.63533 0.10636  0.17963  -0.28507 93  THR B N   
1974 C CA  . THR B 95  ? 1.25782 1.35086 0.66468 0.10388  0.18943  -0.31679 93  THR B CA  
1975 C C   . THR B 95  ? 1.30762 1.34653 0.72907 0.12183  0.19360  -0.34079 93  THR B C   
1976 O O   . THR B 95  ? 1.36275 1.36759 0.76190 0.13309  0.21482  -0.36997 93  THR B O   
1977 C CB  . THR B 95  ? 1.29021 1.37001 0.64227 0.07612  0.16707  -0.31095 93  THR B CB  
1978 O OG1 . THR B 95  ? 1.19629 1.32436 0.53076 0.05971  0.16652  -0.29244 93  THR B OG1 
1979 C CG2 . THR B 95  ? 1.22927 1.25192 0.52274 0.07335  0.17201  -0.34314 93  THR B CG2 
1980 N N   . HIS B 96  ? 1.39408 1.42331 0.85344 0.12529  0.17419  -0.32861 94  HIS B N   
1981 C CA  . HIS B 96  ? 1.49688 1.47253 0.96904 0.13767  0.17275  -0.34864 94  HIS B CA  
1982 C C   . HIS B 96  ? 1.49762 1.48882 1.03932 0.16647  0.17763  -0.34157 94  HIS B C   
1983 O O   . HIS B 96  ? 1.42147 1.39799 0.99364 0.16999  0.15833  -0.33119 94  HIS B O   
1984 C CB  . HIS B 96  ? 1.52205 1.46591 0.97681 0.11673  0.14323  -0.34251 94  HIS B CB  
1985 C CG  . HIS B 96  ? 1.64738 1.55202 1.02844 0.09131  0.13738  -0.35692 94  HIS B CG  
1986 N ND1 . HIS B 96  ? 1.71796 1.63540 1.04929 0.08301  0.14695  -0.36020 94  HIS B ND1 
1987 C CD2 . HIS B 96  ? 1.76248 1.61460 1.10770 0.07217  0.12028  -0.36675 94  HIS B CD2 
1988 C CE1 . HIS B 96  ? 1.67903 1.55296 0.94611 0.06586  0.13305  -0.37069 94  HIS B CE1 
1989 N NE2 . HIS B 96  ? 1.70234 1.53270 0.97342 0.05836  0.11674  -0.37391 94  HIS B NE2 
1990 N N   . HIS B 97  ? 1.41940 1.44176 0.98495 0.18625  0.20218  -0.34536 95  HIS B N   
1991 C CA  . HIS B 97  ? 1.37832 1.41014 1.00499 0.21604  0.20952  -0.34268 95  HIS B CA  
1992 C C   . HIS B 97  ? 1.36285 1.42707 1.03548 0.21653  0.18997  -0.30984 95  HIS B C   
1993 O O   . HIS B 97  ? 1.47568 1.51774 1.18210 0.22883  0.17734  -0.30500 95  HIS B O   
1994 C CB  . HIS B 97  ? 1.41792 1.38567 1.04793 0.23108  0.20966  -0.36692 95  HIS B CB  
1995 C CG  . HIS B 97  ? 1.59278 1.51439 1.16750 0.22454  0.22730  -0.40093 95  HIS B CG  
1996 N ND1 . HIS B 97  ? 1.66225 1.59530 1.22609 0.23771  0.25926  -0.41983 95  HIS B ND1 
1997 C CD2 . HIS B 97  ? 1.59515 1.45790 1.11905 0.20374  0.21854  -0.41979 95  HIS B CD2 
1998 C CE1 . HIS B 97  ? 1.63346 1.51152 1.13874 0.22652  0.27068  -0.44957 95  HIS B CE1 
1999 N NE2 . HIS B 97  ? 1.62328 1.45825 1.10289 0.20413  0.24589  -0.44994 95  HIS B NE2 
2000 N N   . ALA B 98  ? 1.22611 1.33988 0.89716 0.20164  0.18788  -0.28650 96  ALA B N   
2001 C CA  . ALA B 98  ? 1.16701 1.30941 0.87533 0.19916  0.17311  -0.25552 96  ALA B CA  
2002 C C   . ALA B 98  ? 1.03120 1.23365 0.75264 0.19439  0.18554  -0.23554 96  ALA B C   
2003 O O   . ALA B 98  ? 1.02189 1.24419 0.71060 0.18194  0.19612  -0.23877 96  ALA B O   
2004 C CB  . ALA B 98  ? 1.08543 1.21211 0.77251 0.17782  0.14855  -0.24219 96  ALA B CB  
2005 N N   . THR B 99  ? 0.83046 1.05995 0.59710 0.20166  0.18353  -0.21426 97  THR B N   
2006 C CA  . THR B 99  ? 0.81464 1.09809 0.59438 0.19213  0.19176  -0.19102 97  THR B CA  
2007 C C   . THR B 99  ? 0.80955 1.10414 0.61333 0.18153  0.17736  -0.16013 97  THR B C   
2008 O O   . THR B 99  ? 0.75211 1.08350 0.56068 0.16783  0.18146  -0.13817 97  THR B O   
2009 C CB  . THR B 99  ? 0.97913 1.29598 0.79010 0.21109  0.21241  -0.19779 97  THR B CB  
2010 O OG1 . THR B 99  ? 1.03806 1.40735 0.85754 0.19705  0.21853  -0.17452 97  THR B OG1 
2011 C CG2 . THR B 99  ? 0.87013 1.17492 0.72831 0.23373  0.20798  -0.19732 97  THR B CG2 
2012 N N   . ARG B 100 ? 0.83134 1.09260 0.64762 0.18526  0.16127  -0.15794 98  ARG B N   
2013 C CA  . ARG B 100 ? 0.64471 0.91148 0.48053 0.17429  0.14997  -0.13078 98  ARG B CA  
2014 C C   . ARG B 100 ? 0.64701 0.87746 0.46241 0.16488  0.13165  -0.12989 98  ARG B C   
2015 O O   . ARG B 100 ? 0.61670 0.81046 0.42121 0.17265  0.12327  -0.15060 98  ARG B O   
2016 C CB  . ARG B 100 ? 0.73027 1.00050 0.61154 0.18879  0.14974  -0.12543 98  ARG B CB  
2017 C CG  . ARG B 100 ? 0.86408 1.16736 0.77131 0.20588  0.16657  -0.13198 98  ARG B CG  
2018 C CD  . ARG B 100 ? 0.73224 1.08896 0.64980 0.19169  0.17653  -0.10894 98  ARG B CD  
2019 N NE  . ARG B 100 ? 0.87067 1.24040 0.81606 0.18098  0.16935  -0.08230 98  ARG B NE  
2020 C CZ  . ARG B 100 ? 0.87758 1.25771 0.86317 0.19428  0.16829  -0.07741 98  ARG B CZ  
2021 N NH1 . ARG B 100 ? 0.88760 1.25947 0.89362 0.22226  0.17209  -0.09723 98  ARG B NH1 
2022 N NH2 . ARG B 100 ? 0.80153 1.19836 0.80665 0.17772  0.16313  -0.05093 98  ARG B NH2 
2023 N N   . LEU B 101 ? 0.52017 0.75898 0.32973 0.14724  0.12526  -0.10550 99  LEU B N   
2024 C CA  . LEU B 101 ? 0.51342 0.72482 0.30982 0.13951  0.10860  -0.10075 99  LEU B CA  
2025 C C   . LEU B 101 ? 0.53181 0.74011 0.35726 0.13549  0.10503  -0.08071 99  LEU B C   
2026 O O   . LEU B 101 ? 0.50239 0.73078 0.33619 0.12317  0.11167  -0.05721 99  LEU B O   
2027 C CB  . LEU B 101 ? 0.52573 0.74560 0.28835 0.12330  0.10408  -0.08817 99  LEU B CB  
2028 C CG  . LEU B 101 ? 0.61333 0.81089 0.36265 0.11770  0.08602  -0.08350 99  LEU B CG  
2029 C CD1 . LEU B 101 ? 0.54202 0.71063 0.27954 0.12454  0.07539  -0.11150 99  LEU B CD1 
2030 C CD2 . LEU B 101 ? 0.56746 0.77818 0.28875 0.10343  0.08026  -0.06446 99  LEU B CD2 
2031 N N   . LEU B 102 ? 0.48717 0.66643 0.32495 0.14256  0.09424  -0.09050 100 LEU B N   
2032 C CA  . LEU B 102 ? 0.42228 0.59101 0.28919 0.13360  0.08904  -0.07271 100 LEU B CA  
2033 C C   . LEU B 102 ? 0.42144 0.56878 0.27954 0.11608  0.07615  -0.05854 100 LEU B C   
2034 O O   . LEU B 102 ? 0.50234 0.63370 0.34041 0.11594  0.06417  -0.06948 100 LEU B O   
2035 C CB  . LEU B 102 ? 0.43591 0.57553 0.32771 0.14254  0.07879  -0.08689 100 LEU B CB  
2036 C CG  . LEU B 102 ? 0.52914 0.65091 0.45311 0.12760  0.06907  -0.07043 100 LEU B CG  
2037 C CD1 . LEU B 102 ? 0.47141 0.62793 0.42096 0.12499  0.08248  -0.05155 100 LEU B CD1 
2038 C CD2 . LEU B 102 ? 0.55016 0.63419 0.48643 0.13356  0.05321  -0.08657 100 LEU B CD2 
2039 N N   . LEU B 103 ? 0.40459 0.55254 0.27716 0.10103  0.07923  -0.03429 101 LEU B N   
2040 C CA  . LEU B 103 ? 0.40716 0.53188 0.27961 0.08807  0.06899  -0.02191 101 LEU B CA  
2041 C C   . LEU B 103 ? 0.36866 0.47513 0.26957 0.07373  0.06816  -0.01093 101 LEU B C   
2042 O O   . LEU B 103 ? 0.32525 0.44401 0.23629 0.06558  0.07980  0.00237  101 LEU B O   
2043 C CB  . LEU B 103 ? 0.36188 0.49842 0.21278 0.08249  0.07520  -0.00189 101 LEU B CB  
2044 C CG  . LEU B 103 ? 0.42113 0.53440 0.27854 0.07265  0.06914  0.01490  101 LEU B CG  
2045 C CD1 . LEU B 103 ? 0.35587 0.45915 0.21196 0.07749  0.05154  0.00342  101 LEU B CD1 
2046 C CD2 . LEU B 103 ? 0.36283 0.48296 0.19954 0.06820  0.07753  0.03864  101 LEU B CD2 
2047 N N   . GLU B 104 ? 0.33042 0.41088 0.24166 0.06738  0.05459  -0.01627 102 GLU B N   
2048 C CA  . GLU B 104 ? 0.33286 0.39437 0.26582 0.04947  0.05386  -0.00657 102 GLU B CA  
2049 C C   . GLU B 104 ? 0.37334 0.42273 0.30255 0.04343  0.05262  0.00331  102 GLU B C   
2050 O O   . GLU B 104 ? 0.32709 0.37616 0.24935 0.05054  0.04110  -0.00441 102 GLU B O   
2051 C CB  . GLU B 104 ? 0.35508 0.39865 0.30500 0.04551  0.03963  -0.02147 102 GLU B CB  
2052 C CG  . GLU B 104 ? 0.46642 0.51940 0.42441 0.05672  0.04055  -0.02968 102 GLU B CG  
2053 C CD  . GLU B 104 ? 0.61285 0.64487 0.59146 0.04847  0.02737  -0.03544 102 GLU B CD  
2054 O OE1 . GLU B 104 ? 0.63552 0.64684 0.61910 0.03071  0.01744  -0.03515 102 GLU B OE1 
2055 O OE2 . GLU B 104 ? 0.55023 0.58837 0.54084 0.06007  0.02708  -0.03935 102 GLU B OE2 
2056 N N   . VAL B 105 ? 0.27689 0.31654 0.21021 0.03040  0.06472  0.02050  103 VAL B N   
2057 C CA  . VAL B 105 ? 0.30958 0.33609 0.23981 0.03020  0.06733  0.03161  103 VAL B CA  
2058 C C   . VAL B 105 ? 0.33464 0.33635 0.27629 0.01085  0.07867  0.04033  103 VAL B C   
2059 O O   . VAL B 105 ? 0.32191 0.32068 0.26439 -0.00516 0.08782  0.04551  103 VAL B O   
2060 C CB  . VAL B 105 ? 0.43716 0.47487 0.34317 0.04057  0.07394  0.04649  103 VAL B CB  
2061 C CG1 . VAL B 105 ? 0.46814 0.50663 0.36320 0.02862  0.09033  0.06065  103 VAL B CG1 
2062 C CG2 . VAL B 105 ? 0.49598 0.52104 0.40130 0.04686  0.07271  0.05877  103 VAL B CG2 
2063 N N   . ARG B 106 ? 0.29847 0.28457 0.24858 0.01158  0.07897  0.04202  104 ARG B N   
2064 C CA  . ARG B 106 ? 0.32616 0.28460 0.28343 -0.00663 0.09294  0.04706  104 ARG B CA  
2065 C C   . ARG B 106 ? 0.34307 0.28573 0.27918 -0.01461 0.11031  0.06493  104 ARG B C   
2066 O O   . ARG B 106 ? 0.38962 0.33731 0.30784 -0.00108 0.11189  0.07704  104 ARG B O   
2067 C CB  . ARG B 106 ? 0.35706 0.30531 0.32784 0.00194  0.09353  0.04594  104 ARG B CB  
2068 C CG  . ARG B 106 ? 0.27970 0.24364 0.27080 0.00056  0.07795  0.02869  104 ARG B CG  
2069 C CD  . ARG B 106 ? 0.30613 0.27277 0.31400 0.01221  0.07885  0.02943  104 ARG B CD  
2070 N NE  . ARG B 106 ? 0.33242 0.31974 0.35707 0.00635  0.06284  0.01337  104 ARG B NE  
2071 C CZ  . ARG B 106 ? 0.38331 0.36487 0.42332 -0.01358 0.06609  0.00224  104 ARG B CZ  
2072 N NH1 . ARG B 106 ? 0.40138 0.35672 0.44331 -0.02826 0.08647  0.00404  104 ARG B NH1 
2073 N NH2 . ARG B 106 ? 0.32393 0.32522 0.37368 -0.02225 0.04874  -0.01136 104 ARG B NH2 
2074 N N   . LYS B 107 ? 0.47069 0.37808 0.26181 -0.21468 0.03975  0.00100  105 LYS B N   
2075 C CA  . LYS B 107 ? 0.51608 0.42120 0.29297 -0.24091 0.02509  -0.00253 105 LYS B CA  
2076 C C   . LYS B 107 ? 0.52766 0.38714 0.32079 -0.24362 0.04291  -0.01249 105 LYS B C   
2077 O O   . LYS B 107 ? 0.60282 0.46297 0.40884 -0.25820 0.03628  -0.00832 105 LYS B O   
2078 C CB  . LYS B 107 ? 0.55816 0.45322 0.27469 -0.26519 0.01843  -0.01524 105 LYS B CB  
2079 C CG  . LYS B 107 ? 0.59903 0.49000 0.30007 -0.30149 0.00546  -0.02847 105 LYS B CG  
2080 C CD  . LYS B 107 ? 0.67961 0.61345 0.33574 -0.32350 -0.01933 -0.03099 105 LYS B CD  
2081 C CE  . LYS B 107 ? 0.81319 0.71842 0.40700 -0.32322 -0.00701 -0.04652 105 LYS B CE  
2082 N NZ  . LYS B 107 ? 1.02274 0.85119 0.58550 -0.34276 0.01903  -0.08162 105 LYS B NZ  
2083 N N   . SER B 108 ? 0.54204 0.36127 0.33806 -0.22827 0.06943  -0.02270 106 SER B N   
2084 C CA  . SER B 108 ? 0.60154 0.37554 0.41434 -0.22489 0.09169  -0.02742 106 SER B CA  
2085 C C   . SER B 108 ? 0.52528 0.33362 0.39636 -0.19836 0.09036  -0.00655 106 SER B C   
2086 O O   . SER B 108 ? 0.63233 0.41125 0.52335 -0.18822 0.10949  -0.00111 106 SER B O   
2087 C CB  . SER B 108 ? 0.59733 0.31721 0.39181 -0.21716 0.12410  -0.04499 106 SER B CB  
2088 O OG  . SER B 108 ? 0.62972 0.37420 0.45245 -0.19212 0.13174  -0.04022 106 SER B OG  
2089 N N   . ASN B 109 ? 0.49797 0.36772 0.39446 -0.18560 0.07068  0.00564  107 ASN B N   
2090 C CA  . ASN B 109 ? 0.43928 0.35132 0.38365 -0.16098 0.06749  0.02141  107 ASN B CA  
2091 C C   . ASN B 109 ? 0.49370 0.42321 0.44607 -0.16579 0.05511  0.04148  107 ASN B C   
2092 O O   . ASN B 109 ? 0.41799 0.39813 0.38036 -0.16395 0.03573  0.05250  107 ASN B O   
2093 C CB  . ASN B 109 ? 0.36157 0.32677 0.32794 -0.14817 0.05724  0.01842  107 ASN B CB  
2094 C CG  . ASN B 109 ? 0.42419 0.43707 0.43574 -0.12435 0.05580  0.02501  107 ASN B CG  
2095 O OD1 . ASN B 109 ? 0.41937 0.43530 0.44612 -0.11177 0.05886  0.04185  107 ASN B OD1 
2096 N ND2 . ASN B 109 ? 0.36532 0.41837 0.39895 -0.11788 0.05253  0.01248  107 ASN B ND2 
2097 N N   . ARG B 110 ? 0.51667 0.39909 0.46730 -0.17026 0.07258  0.04709  108 ARG B N   
2098 C CA  . ARG B 110 ? 0.52871 0.41295 0.48780 -0.17815 0.06990  0.06732  108 ARG B CA  
2099 C C   . ARG B 110 ? 0.44963 0.39842 0.44166 -0.14999 0.05867  0.09443  108 ARG B C   
2100 O O   . ARG B 110 ? 0.55861 0.53800 0.55397 -0.15705 0.04594  0.10977  108 ARG B O   
2101 C CB  . ARG B 110 ? 0.56920 0.37985 0.52684 -0.18324 0.10156  0.06892  108 ARG B CB  
2102 C CG  . ARG B 110 ? 0.71463 0.50497 0.67815 -0.20244 0.10816  0.08464  108 ARG B CG  
2103 C CD  . ARG B 110 ? 0.85836 0.65246 0.79986 -0.24014 0.08864  0.06135  108 ARG B CD  
2104 N NE  . ARG B 110 ? 0.85696 0.64065 0.81922 -0.25266 0.09564  0.07288  108 ARG B NE  
2105 C CZ  . ARG B 110 ? 0.97970 0.79230 0.94204 -0.27760 0.07714  0.06362  108 ARG B CZ  
2106 N NH1 . ARG B 110 ? 0.79625 0.65631 0.73642 -0.28884 0.04773  0.04869  108 ARG B NH1 
2107 N NH2 . ARG B 110 ? 0.96126 0.75635 0.94922 -0.29027 0.09045  0.07291  108 ARG B NH2 
2108 N N   . SER B 111 ? 0.47159 0.44770 0.48838 -0.11834 0.06363  0.10081  109 SER B N   
2109 C CA  . SER B 111 ? 0.38624 0.42627 0.42700 -0.09208 0.05359  0.12763  109 SER B CA  
2110 C C   . SER B 111 ? 0.41622 0.51915 0.45417 -0.09568 0.02812  0.11820  109 SER B C   
2111 O O   . SER B 111 ? 0.36277 0.50557 0.40265 -0.09019 0.01838  0.13725  109 SER B O   
2112 C CB  . SER B 111 ? 0.38147 0.44921 0.45216 -0.05644 0.06289  0.13907  109 SER B CB  
2113 O OG  . SER B 111 ? 0.42162 0.52197 0.50359 -0.05379 0.05451  0.11239  109 SER B OG  
2114 N N   . ALA B 112 ? 0.40550 0.51164 0.43817 -0.10452 0.02254  0.09009  110 ALA B N   
2115 C CA  . ALA B 112 ? 0.30510 0.45571 0.33555 -0.10868 0.00659  0.07927  110 ALA B CA  
2116 C C   . ALA B 112 ? 0.41307 0.55964 0.42623 -0.12671 -0.00170 0.09072  110 ALA B C   
2117 O O   . ALA B 112 ? 0.32665 0.51873 0.34437 -0.12125 -0.01146 0.09957  110 ALA B O   
2118 C CB  . ALA B 112 ? 0.30604 0.44275 0.33439 -0.11576 0.01143  0.05154  110 ALA B CB  
2119 N N   . ILE B 113 ? 0.36154 0.45859 0.35542 -0.14948 0.00271  0.08858  111 ILE B N   
2120 C CA  . ILE B 113 ? 0.30738 0.41146 0.29066 -0.17097 -0.00776 0.09698  111 ILE B CA  
2121 C C   . ILE B 113 ? 0.35894 0.48052 0.35710 -0.16962 -0.00692 0.12287  111 ILE B C   
2122 O O   . ILE B 113 ? 0.41766 0.57974 0.42272 -0.17264 -0.01650 0.13569  111 ILE B O   
2123 C CB  . ILE B 113 ? 0.43786 0.49327 0.39475 -0.19953 -0.00518 0.08308  111 ILE B CB  
2124 C CG1 . ILE B 113 ? 0.33962 0.39022 0.27674 -0.19870 -0.00694 0.06513  111 ILE B CG1 
2125 C CG2 . ILE B 113 ? 0.47292 0.54081 0.42777 -0.21937 -0.01656 0.08992  111 ILE B CG2 
2126 C CD1 . ILE B 113 ? 0.43098 0.42519 0.33391 -0.21885 0.00261  0.04629  111 ILE B CD1 
2127 N N   . GLU B 114 ? 0.45193 0.54012 0.45690 -0.16377 0.00922  0.13438  112 GLU B N   
2128 C CA  . GLU B 114 ? 0.39798 0.49528 0.41726 -0.16101 0.01680  0.16442  112 GLU B CA  
2129 C C   . GLU B 114 ? 0.42142 0.58604 0.45071 -0.13077 0.00873  0.18247  112 GLU B C   
2130 O O   . GLU B 114 ? 0.39620 0.59144 0.43164 -0.13136 0.00769  0.20370  112 GLU B O   
2131 C CB  . GLU B 114 ? 0.55763 0.59806 0.58358 -0.15494 0.04309  0.17741  112 GLU B CB  
2132 C CG  . GLU B 114 ? 0.62528 0.59125 0.63716 -0.18809 0.05709  0.15492  112 GLU B CG  
2133 C CD  . GLU B 114 ? 0.71137 0.68406 0.71471 -0.22154 0.04218  0.13638  112 GLU B CD  
2134 O OE1 . GLU B 114 ? 0.60237 0.58620 0.62281 -0.22708 0.04548  0.14992  112 GLU B OE1 
2135 O OE2 . GLU B 114 ? 0.83862 0.81135 0.81979 -0.23507 0.02744  0.10834  112 GLU B OE2 
2136 N N   . PHE B 115 ? 0.42284 0.61443 0.45402 -0.10599 0.00422  0.17209  113 PHE B N   
2137 C CA  . PHE B 115 ? 0.40565 0.66761 0.43966 -0.08220 -0.00621 0.17742  113 PHE B CA  
2138 C C   . PHE B 115 ? 0.42905 0.72155 0.45711 -0.09339 -0.01682 0.16701  113 PHE B C   
2139 O O   . PHE B 115 ? 0.36446 0.69996 0.39130 -0.08308 -0.01805 0.18342  113 PHE B O   
2140 C CB  . PHE B 115 ? 0.30048 0.58986 0.34170 -0.06399 -0.01141 0.15652  113 PHE B CB  
2141 C CG  . PHE B 115 ? 0.39461 0.75736 0.43433 -0.04961 -0.02416 0.14595  113 PHE B CG  
2142 C CD1 . PHE B 115 ? 0.33796 0.75534 0.37370 -0.02517 -0.02694 0.17135  113 PHE B CD1 
2143 C CD2 . PHE B 115 ? 0.28083 0.65573 0.32007 -0.06044 -0.02971 0.11095  113 PHE B CD2 
2144 C CE1 . PHE B 115 ? 0.41709 0.90450 0.44375 -0.01473 -0.03834 0.15593  113 PHE B CE1 
2145 C CE2 . PHE B 115 ? 0.32124 0.75656 0.35747 -0.05149 -0.03674 0.09419  113 PHE B CE2 
2146 C CZ  . PHE B 115 ? 0.26184 0.75588 0.28918 -0.03014 -0.04271 0.11396  113 PHE B CZ  
2147 N N   . TYR B 116 ? 0.34110 0.61342 0.36488 -0.11037 -0.02127 0.14252  114 TYR B N   
2148 C CA  . TYR B 116 ? 0.30260 0.60479 0.32534 -0.11345 -0.02660 0.13620  114 TYR B CA  
2149 C C   . TYR B 116 ? 0.30522 0.61479 0.33244 -0.12695 -0.02777 0.15990  114 TYR B C   
2150 O O   . TYR B 116 ? 0.31119 0.65616 0.34338 -0.11633 -0.02916 0.16542  114 TYR B O   
2151 C CB  . TYR B 116 ? 0.34125 0.61954 0.35942 -0.12271 -0.02672 0.11197  114 TYR B CB  
2152 C CG  . TYR B 116 ? 0.30868 0.61515 0.33066 -0.11385 -0.02352 0.09999  114 TYR B CG  
2153 C CD1 . TYR B 116 ? 0.39050 0.72424 0.41741 -0.09961 -0.01893 0.07938  114 TYR B CD1 
2154 C CD2 . TYR B 116 ? 0.27709 0.58445 0.29932 -0.11978 -0.02299 0.10848  114 TYR B CD2 
2155 C CE1 . TYR B 116 ? 0.27221 0.61932 0.30303 -0.09410 -0.00869 0.06325  114 TYR B CE1 
2156 C CE2 . TYR B 116 ? 0.21260 0.53590 0.24129 -0.10761 -0.01220 0.10046  114 TYR B CE2 
2157 C CZ  . TYR B 116 ? 0.33865 0.67497 0.37099 -0.09612 -0.00261 0.07594  114 TYR B CZ  
2158 O OH  . TYR B 116 ? 0.26022 0.60153 0.29931 -0.08665 0.01471  0.06301  114 TYR B OH  
2159 N N   . LYS B 117 ? 0.27427 0.54191 0.30109 -0.14529 -0.02846 0.16336  115 LYS B N   
2160 C CA  . LYS B 117 ? 0.28824 0.56219 0.32498 -0.15430 -0.03206 0.17548  115 LYS B CA  
2161 C C   . LYS B 117 ? 0.39451 0.69045 0.44386 -0.13901 -0.02251 0.19959  115 LYS B C   
2162 O O   . LYS B 117 ? 0.35332 0.67918 0.41447 -0.13527 -0.02373 0.21060  115 LYS B O   
2163 C CB  . LYS B 117 ? 0.41339 0.64148 0.44560 -0.18204 -0.03180 0.16719  115 LYS B CB  
2164 C CG  . LYS B 117 ? 0.33684 0.55494 0.35033 -0.19529 -0.04326 0.14664  115 LYS B CG  
2165 C CD  . LYS B 117 ? 0.55464 0.73462 0.55666 -0.22536 -0.04358 0.13312  115 LYS B CD  
2166 C CE  . LYS B 117 ? 0.54928 0.67564 0.55569 -0.23245 -0.02318 0.13189  115 LYS B CE  
2167 N NZ  . LYS B 117 ? 0.71271 0.78869 0.70025 -0.26086 -0.01827 0.10732  115 LYS B NZ  
2168 N N   . LYS B 118 ? 0.29882 0.58255 0.34535 -0.12654 -0.01118 0.21133  116 LYS B N   
2169 C CA  . LYS B 118 ? 0.43557 0.74218 0.48827 -0.10476 -0.00057 0.23760  116 LYS B CA  
2170 C C   . LYS B 118 ? 0.51694 0.88471 0.56633 -0.08389 -0.00693 0.23512  116 LYS B C   
2171 O O   . LYS B 118 ? 0.42419 0.81532 0.48100 -0.07365 -0.00071 0.25095  116 LYS B O   
2172 C CB  . LYS B 118 ? 0.50086 0.79102 0.54853 -0.08668 0.01132  0.25345  116 LYS B CB  
2173 C CG  . LYS B 118 ? 0.60451 0.90633 0.65678 -0.06072 0.02619  0.28550  116 LYS B CG  
2174 C CD  . LYS B 118 ? 0.64359 0.96726 0.68840 -0.02942 0.02762  0.29730  116 LYS B CD  
2175 C CE  . LYS B 118 ? 0.67664 1.06849 0.70784 -0.01771 0.00667  0.27226  116 LYS B CE  
2176 N NZ  . LYS B 118 ? 0.65405 1.10268 0.68030 0.00048  0.00452  0.27203  116 LYS B NZ  
2177 N N   . ALA B 119 ? 0.41469 0.84657 0.24662 -0.04567 0.02262  0.12057  117 ALA B N   
2178 C CA  . ALA B 119 ? 0.42627 0.88899 0.24782 -0.04204 0.02956  0.09849  117 ALA B CA  
2179 C C   . ALA B 119 ? 0.42469 0.91963 0.26366 -0.03943 0.04647  0.08125  117 ALA B C   
2180 O O   . ALA B 119 ? 0.46110 0.97895 0.29051 -0.03516 0.05625  0.06104  117 ALA B O   
2181 C CB  . ALA B 119 ? 0.41284 0.87077 0.23428 -0.02946 0.01957  0.08326  117 ALA B CB  
2182 N N   . GLY B 120 ? 0.39198 0.89014 0.25661 -0.04106 0.05039  0.08739  118 GLY B N   
2183 C CA  . GLY B 120 ? 0.38372 0.91803 0.27090 -0.03590 0.06455  0.07309  118 GLY B CA  
2184 C C   . GLY B 120 ? 0.34601 0.88403 0.26430 -0.01856 0.06408  0.06417  118 GLY B C   
2185 O O   . GLY B 120 ? 0.37119 0.93839 0.31417 -0.01250 0.07299  0.05708  118 GLY B O   
2186 N N   . GLY B 121 ? 0.34566 0.85671 0.26402 -0.00966 0.05348  0.06501  119 GLY B N   
2187 C CA  . GLY B 121 ? 0.32602 0.83834 0.27239 0.00606  0.05355  0.05884  119 GLY B CA  
2188 C C   . GLY B 121 ? 0.36286 0.88281 0.33518 -0.00280 0.05186  0.07238  119 GLY B C   
2189 O O   . GLY B 121 ? 0.31310 0.81819 0.27728 -0.02296 0.04680  0.08918  119 GLY B O   
2190 N N   . VAL B 122 ? 0.27617 0.81479 0.27908 0.01283  0.05515  0.06411  120 VAL B N   
2191 C CA  . VAL B 122 ? 0.24325 0.79353 0.27029 0.00513  0.05072  0.07371  120 VAL B CA  
2192 C C   . VAL B 122 ? 0.27275 0.80714 0.32122 0.01927  0.04248  0.07363  120 VAL B C   
2193 O O   . VAL B 122 ? 0.24892 0.77513 0.30608 0.04275  0.04360  0.06119  120 VAL B O   
2194 C CB  . VAL B 122 ? 0.40665 0.99937 0.44972 0.00964  0.05923  0.06682  120 VAL B CB  
2195 C CG1 . VAL B 122 ? 0.46925 1.07358 0.52584 0.04171  0.06789  0.04828  120 VAL B CG1 
2196 C CG2 . VAL B 122 ? 0.33227 0.93932 0.39432 -0.00108 0.05237  0.07641  120 VAL B CG2 
2197 N N   . GLU B 123 ? 0.23790 0.75951 0.29161 0.00361  0.03344  0.08619  121 GLU B N   
2198 C CA  . GLU B 123 ? 0.18361 0.68655 0.25434 0.01387  0.02383  0.08676  121 GLU B CA  
2199 C C   . GLU B 123 ? 0.18843 0.71150 0.27919 0.03169  0.02408  0.08145  121 GLU B C   
2200 O O   . GLU B 123 ? 0.21500 0.76980 0.31120 0.02418  0.02681  0.08401  121 GLU B O   
2201 C CB  . GLU B 123 ? 0.25315 0.73572 0.31907 -0.00916 0.01604  0.09904  121 GLU B CB  
2202 C CG  . GLU B 123 ? 0.23280 0.69166 0.31020 -0.00133 0.00550  0.09889  121 GLU B CG  
2203 C CD  . GLU B 123 ? 0.39870 0.84113 0.46999 -0.02515 0.00028  0.10746  121 GLU B CD  
2204 O OE1 . GLU B 123 ? 0.39762 0.81592 0.45022 -0.04235 0.00275  0.11281  121 GLU B OE1 
2205 O OE2 . GLU B 123 ? 0.33186 0.77207 0.40893 -0.02534 -0.00557 0.10754  121 GLU B OE2 
2206 N N   . ILE B 124 ? 0.18875 0.69469 0.29029 0.05628  0.02185  0.07444  122 ILE B N   
2207 C CA  . ILE B 124 ? 0.19746 0.71585 0.31764 0.07723  0.02217  0.07280  122 ILE B CA  
2208 C C   . ILE B 124 ? 0.19015 0.68403 0.31617 0.07749  0.01023  0.08158  122 ILE B C   
2209 O O   . ILE B 124 ? 0.20155 0.71114 0.34164 0.08905  0.00824  0.08591  122 ILE B O   
2210 C CB  . ILE B 124 ? 0.21558 0.73183 0.34251 0.10887  0.03197  0.05815  122 ILE B CB  
2211 C CG1 . ILE B 124 ? 0.22921 0.70389 0.34728 0.11752  0.02915  0.05085  122 ILE B CG1 
2212 C CG2 . ILE B 124 ? 0.23136 0.77833 0.35003 0.10773  0.04664  0.04731  122 ILE B CG2 
2213 C CD1 . ILE B 124 ? 0.24554 0.69669 0.36088 0.14637  0.03926  0.03326  122 ILE B CD1 
2214 N N   . GLY B 125 ? 0.17552 0.63453 0.29088 0.06514  0.00250  0.08481  123 GLY B N   
2215 C CA  . GLY B 125 ? 0.17323 0.61199 0.29090 0.06250  -0.00707 0.09245  123 GLY B CA  
2216 C C   . GLY B 125 ? 0.15989 0.56131 0.26455 0.04773  -0.01350 0.09379  123 GLY B C   
2217 O O   . GLY B 125 ? 0.19827 0.58940 0.29366 0.04093  -0.01217 0.09027  123 GLY B O   
2218 N N   . VAL B 126 ? 0.17175 0.55631 0.27585 0.04346  -0.02060 0.09957  124 VAL B N   
2219 C CA  . VAL B 126 ? 0.15112 0.50311 0.24418 0.03017  -0.02575 0.10032  124 VAL B CA  
2220 C C   . VAL B 126 ? 0.15887 0.48978 0.25451 0.04191  -0.03189 0.10367  124 VAL B C   
2221 O O   . VAL B 126 ? 0.17502 0.51838 0.27772 0.05026  -0.03449 0.11038  124 VAL B O   
2222 C CB  . VAL B 126 ? 0.19832 0.55709 0.28364 0.00514  -0.02708 0.10528  124 VAL B CB  
2223 C CG1 . VAL B 126 ? 0.14505 0.47372 0.22120 -0.00491 -0.03117 0.10503  124 VAL B CG1 
2224 C CG2 . VAL B 126 ? 0.26700 0.64460 0.34814 -0.00898 -0.02191 0.10552  124 VAL B CG2 
2225 N N   . ARG B 127 ? 0.15572 0.45790 0.24535 0.04219  -0.03483 0.10097  125 ARG B N   
2226 C CA  . ARG B 127 ? 0.18570 0.46594 0.27275 0.04543  -0.04133 0.10767  125 ARG B CA  
2227 C C   . ARG B 127 ? 0.18344 0.45383 0.26016 0.02304  -0.04331 0.10870  125 ARG B C   
2228 O O   . ARG B 127 ? 0.20085 0.45534 0.27150 0.01434  -0.04004 0.10057  125 ARG B O   
2229 C CB  . ARG B 127 ? 0.26038 0.50116 0.33997 0.05467  -0.03799 0.09799  125 ARG B CB  
2230 C CG  . ARG B 127 ? 0.22364 0.46666 0.30833 0.07571  -0.03219 0.09093  125 ARG B CG  
2231 C CD  . ARG B 127 ? 0.36939 0.56742 0.44134 0.08010  -0.02832 0.07870  125 ARG B CD  
2232 N NE  . ARG B 127 ? 0.48216 0.68044 0.55444 0.09819  -0.01992 0.06667  125 ARG B NE  
2233 C CZ  . ARG B 127 ? 0.55561 0.74325 0.63293 0.12319  -0.01537 0.06780  125 ARG B CZ  
2234 N NH1 . ARG B 127 ? 0.60894 0.78351 0.69077 0.13408  -0.02051 0.08367  125 ARG B NH1 
2235 N NH2 . ARG B 127 ? 0.63315 0.82335 0.70968 0.13926  -0.00483 0.05320  125 ARG B NH2 
2236 N N   . LYS B 128 ? 0.16422 0.44088 0.23679 0.01418  -0.04656 0.11638  126 LYS B N   
2237 C CA  . LYS B 128 ? 0.18664 0.45906 0.24822 -0.00671 -0.04731 0.11629  126 LYS B CA  
2238 C C   . LYS B 128 ? 0.23720 0.47861 0.29108 -0.00872 -0.04654 0.11387  126 LYS B C   
2239 O O   . LYS B 128 ? 0.22890 0.45328 0.28114 0.00066  -0.04899 0.11907  126 LYS B O   
2240 C CB  . LYS B 128 ? 0.19301 0.48237 0.24870 -0.01732 -0.05088 0.12396  126 LYS B CB  
2241 C CG  . LYS B 128 ? 0.27069 0.59122 0.33232 -0.02143 -0.04894 0.12383  126 LYS B CG  
2242 C CD  . LYS B 128 ? 0.19369 0.51892 0.24941 -0.04020 -0.04435 0.11659  126 LYS B CD  
2243 C CE  . LYS B 128 ? 0.36651 0.68446 0.40600 -0.06289 -0.04617 0.11441  126 LYS B CE  
2244 N NZ  . LYS B 128 ? 0.47706 0.78800 0.50765 -0.08152 -0.03965 0.10584  126 LYS B NZ  
2245 N N   . ASN B 129 ? 0.21625 0.44665 0.26472 -0.02106 -0.04091 0.10495  127 ASN B N   
2246 C CA  . ASN B 129 ? 0.21264 0.42293 0.25444 -0.02851 -0.03782 0.10169  127 ASN B CA  
2247 C C   . ASN B 129 ? 0.26000 0.45143 0.30511 -0.01944 -0.03840 0.09966  127 ASN B C   
2248 O O   . ASN B 129 ? 0.25505 0.42887 0.29251 -0.02388 -0.03887 0.10397  127 ASN B O   
2249 C CB  . ASN B 129 ? 0.20503 0.41732 0.23360 -0.04034 -0.04019 0.11025  127 ASN B CB  
2250 C CG  . ASN B 129 ? 0.29079 0.51931 0.31114 -0.05471 -0.03845 0.10784  127 ASN B CG  
2251 O OD1 . ASN B 129 ? 0.32311 0.54532 0.34196 -0.06128 -0.03032 0.09663  127 ASN B OD1 
2252 N ND2 . ASN B 129 ? 0.26394 0.51367 0.27898 -0.05884 -0.04616 0.11819  127 ASN B ND2 
2253 N N   . TYR B 130 ? 0.23185 0.42505 0.28474 -0.00993 -0.03759 0.09243  128 TYR B N   
2254 C CA  . TYR B 130 ? 0.25205 0.42826 0.30515 -0.00236 -0.03771 0.08680  128 TYR B CA  
2255 C C   . TYR B 130 ? 0.24565 0.41720 0.29975 -0.01228 -0.03531 0.07659  128 TYR B C   
2256 O O   . TYR B 130 ? 0.36599 0.51788 0.41491 -0.01760 -0.03486 0.07244  128 TYR B O   
2257 C CB  . TYR B 130 ? 0.30477 0.49242 0.36302 0.01179  -0.03764 0.08323  128 TYR B CB  
2258 C CG  . TYR B 130 ? 0.27804 0.44556 0.33210 0.01950  -0.03609 0.07408  128 TYR B CG  
2259 C CD1 . TYR B 130 ? 0.31273 0.45387 0.36136 0.02839  -0.03567 0.07746  128 TYR B CD1 
2260 C CD2 . TYR B 130 ? 0.29833 0.47034 0.35086 0.01720  -0.03496 0.06221  128 TYR B CD2 
2261 C CE1 . TYR B 130 ? 0.36717 0.48103 0.40764 0.03362  -0.03202 0.06611  128 TYR B CE1 
2262 C CE2 . TYR B 130 ? 0.47609 0.62888 0.52028 0.01999  -0.03290 0.05060  128 TYR B CE2 
2263 C CZ  . TYR B 130 ? 0.38791 0.50841 0.42539 0.02766  -0.03035 0.05106  128 TYR B CZ  
2264 O OH  . TYR B 130 ? 0.61590 0.70762 0.64060 0.02905  -0.02602 0.03627  128 TYR B OH  
2265 N N   . TYR B 131 ? 0.17056 0.36120 0.23169 -0.01491 -0.03353 0.07263  129 TYR B N   
2266 C CA  . TYR B 131 ? 0.23804 0.43654 0.30549 -0.02046 -0.03280 0.06446  129 TYR B CA  
2267 C C   . TYR B 131 ? 0.20323 0.40924 0.27515 -0.03028 -0.02772 0.06439  129 TYR B C   
2268 O O   . TYR B 131 ? 0.20398 0.40920 0.27222 -0.03150 -0.02413 0.06862  129 TYR B O   
2269 C CB  . TYR B 131 ? 0.18528 0.40148 0.25856 -0.01167 -0.03458 0.06225  129 TYR B CB  
2270 C CG  . TYR B 131 ? 0.18862 0.40504 0.25623 -0.00357 -0.03777 0.06003  129 TYR B CG  
2271 C CD1 . TYR B 131 ? 0.23603 0.45285 0.30021 -0.00634 -0.04066 0.05051  129 TYR B CD1 
2272 C CD2 . TYR B 131 ? 0.20393 0.42319 0.26817 0.00405  -0.03675 0.06577  129 TYR B CD2 
2273 C CE1 . TYR B 131 ? 0.28486 0.50275 0.34060 0.00020  -0.04162 0.04574  129 TYR B CE1 
2274 C CE2 . TYR B 131 ? 0.23906 0.46349 0.29783 0.01100  -0.03740 0.06244  129 TYR B CE2 
2275 C CZ  . TYR B 131 ? 0.34417 0.56655 0.39779 0.01007  -0.03935 0.05200  129 TYR B CZ  
2276 O OH  . TYR B 131 ? 0.33290 0.56014 0.37758 0.01638  -0.03796 0.04621  129 TYR B OH  
2277 N N   . PRO B 132 ? 0.27318 0.49067 0.35293 -0.03891 -0.02620 0.05809  130 PRO B N   
2278 C CA  . PRO B 132 ? 0.22430 0.45735 0.31189 -0.04539 -0.01866 0.05633  130 PRO B CA  
2279 C C   . PRO B 132 ? 0.29096 0.54015 0.38982 -0.03107 -0.01599 0.05536  130 PRO B C   
2280 O O   . PRO B 132 ? 0.22134 0.48047 0.32663 -0.01965 -0.02157 0.05578  130 PRO B O   
2281 C CB  . PRO B 132 ? 0.24716 0.49580 0.34307 -0.05969 -0.01810 0.04974  130 PRO B CB  
2282 C CG  . PRO B 132 ? 0.34756 0.59411 0.44230 -0.05761 -0.02652 0.04563  130 PRO B CG  
2283 C CD  . PRO B 132 ? 0.26352 0.48323 0.34460 -0.04561 -0.03020 0.05065  130 PRO B CD  
2284 N N   . ALA B 133 ? 0.21150 0.45893 0.30885 -0.03147 -0.00684 0.05453  131 ALA B N   
2285 C CA  . ALA B 133 ? 0.22984 0.48173 0.33508 -0.01646 -0.00144 0.05319  131 ALA B CA  
2286 C C   . ALA B 133 ? 0.27386 0.54083 0.38880 -0.01772 0.01118  0.04575  131 ALA B C   
2287 O O   . ALA B 133 ? 0.26434 0.53873 0.37647 -0.03391 0.01585  0.04241  131 ALA B O   
2288 C CB  . ALA B 133 ? 0.19465 0.41991 0.28325 -0.01397 0.00031  0.05685  131 ALA B CB  
2289 N N   . GLU B 134 ? 0.23421 0.50510 0.36000 0.00070  0.01788  0.04377  132 GLU B N   
2290 C CA  . GLU B 134 ? 0.25103 0.54173 0.39078 0.00515  0.03222  0.03487  132 GLU B CA  
2291 C C   . GLU B 134 ? 0.23953 0.51302 0.35858 -0.01271 0.04409  0.02758  132 GLU B C   
2292 O O   . GLU B 134 ? 0.25599 0.55231 0.38036 -0.02385 0.05317  0.02099  132 GLU B O   
2293 C CB  . GLU B 134 ? 0.25398 0.53948 0.40463 0.03271  0.03938  0.03485  132 GLU B CB  
2294 C CG  . GLU B 134 ? 0.30066 0.60782 0.46774 0.04172  0.05743  0.02349  132 GLU B CG  
2295 C CD  . GLU B 134 ? 0.51140 0.82162 0.69785 0.07668  0.06324  0.02589  132 GLU B CD  
2296 O OE1 . GLU B 134 ? 0.56645 0.84459 0.74291 0.09078  0.05653  0.03613  132 GLU B OE1 
2297 O OE2 . GLU B 134 ? 0.58454 0.93036 0.79645 0.09110  0.07557  0.01845  132 GLU B OE2 
2298 N N   . LYS B 135 ? 0.24381 0.48167 0.33770 -0.01865 0.04372  0.02906  133 LYS B N   
2299 C CA  . LYS B 135 ? 0.40802 0.63315 0.47692 -0.03990 0.05013  0.02461  133 LYS B CA  
2300 C C   . LYS B 135 ? 0.20507 0.41881 0.25819 -0.05256 0.03507  0.03601  133 LYS B C   
2301 O O   . LYS B 135 ? 0.23493 0.43278 0.28260 -0.04736 0.02802  0.04109  133 LYS B O   
2302 C CB  . LYS B 135 ? 0.32447 0.52223 0.37608 -0.03796 0.06424  0.01389  133 LYS B CB  
2303 C CG  . LYS B 135 ? 0.49945 0.68757 0.52071 -0.06265 0.07004  0.00787  133 LYS B CG  
2304 C CD  . LYS B 135 ? 0.43369 0.64502 0.45679 -0.07040 0.08391  -0.00154 133 LYS B CD  
2305 C CE  . LYS B 135 ? 0.46876 0.66820 0.45767 -0.09186 0.09569  -0.01278 133 LYS B CE  
2306 N NZ  . LYS B 135 ? 0.59951 0.79211 0.56346 -0.11248 0.07965  -0.00061 133 LYS B NZ  
2307 N N   . GLY B 136 ? 0.22190 0.44434 0.26831 -0.06808 0.03069  0.04129  134 GLY B N   
2308 C CA  . GLY B 136 ? 0.19974 0.41136 0.23269 -0.07480 0.01719  0.05352  134 GLY B CA  
2309 C C   . GLY B 136 ? 0.19221 0.40288 0.23882 -0.06231 0.00512  0.06025  134 GLY B C   
2310 O O   . GLY B 136 ? 0.23112 0.45254 0.29427 -0.05623 0.00432  0.05752  134 GLY B O   
2311 N N   . ARG B 137 ? 0.18697 0.38929 0.22590 -0.05993 -0.00416 0.06840  135 ARG B N   
2312 C CA  . ARG B 137 ? 0.20938 0.41088 0.25809 -0.04801 -0.01319 0.07263  135 ARG B CA  
2313 C C   . ARG B 137 ? 0.28922 0.49026 0.33833 -0.03976 -0.01523 0.07377  135 ARG B C   
2314 O O   . ARG B 137 ? 0.20773 0.40532 0.24710 -0.04619 -0.01136 0.07279  135 ARG B O   
2315 C CB  . ARG B 137 ? 0.28058 0.47411 0.32215 -0.05006 -0.02081 0.08200  135 ARG B CB  
2316 C CG  . ARG B 137 ? 0.30263 0.48983 0.33919 -0.06231 -0.01766 0.08264  135 ARG B CG  
2317 C CD  . ARG B 137 ? 0.37942 0.54817 0.40363 -0.06347 -0.02411 0.09505  135 ARG B CD  
2318 N NE  . ARG B 137 ? 0.32952 0.48501 0.34707 -0.07741 -0.02035 0.09584  135 ARG B NE  
2319 C CZ  . ARG B 137 ? 0.38236 0.51859 0.38141 -0.08610 -0.02195 0.10904  135 ARG B CZ  
2320 N NH1 . ARG B 137 ? 0.35471 0.48899 0.34185 -0.08041 -0.02867 0.12335  135 ARG B NH1 
2321 N NH2 . ARG B 137 ? 0.33893 0.45970 0.33041 -0.10225 -0.01716 0.10941  135 ARG B NH2 
2322 N N   . GLU B 138 ? 0.20742 0.41132 0.26479 -0.02857 -0.02048 0.07500  136 GLU B N   
2323 C CA  . GLU B 138 ? 0.18986 0.39489 0.24653 -0.02229 -0.02127 0.07716  136 GLU B CA  
2324 C C   . GLU B 138 ? 0.16901 0.38138 0.22589 -0.01731 -0.02759 0.08225  136 GLU B C   
2325 O O   . GLU B 138 ? 0.21324 0.42443 0.27354 -0.01163 -0.03117 0.08125  136 GLU B O   
2326 C CB  . GLU B 138 ? 0.18727 0.39429 0.25187 -0.01176 -0.02028 0.07470  136 GLU B CB  
2327 C CG  . GLU B 138 ? 0.22960 0.43462 0.28887 -0.00655 -0.02109 0.08000  136 GLU B CG  
2328 C CD  . GLU B 138 ? 0.25107 0.45449 0.31339 0.00474  -0.02034 0.08230  136 GLU B CD  
2329 O OE1 . GLU B 138 ? 0.24363 0.45914 0.31756 0.01175  -0.02245 0.07934  136 GLU B OE1 
2330 O OE2 . GLU B 138 ? 0.25850 0.45026 0.31105 0.00615  -0.01801 0.08879  136 GLU B OE2 
2331 N N   . ASP B 139 ? 0.19260 0.41251 0.24568 -0.01981 -0.02745 0.08640  137 ASP B N   
2332 C CA  . ASP B 139 ? 0.21072 0.44660 0.26784 -0.01323 -0.03147 0.09080  137 ASP B CA  
2333 C C   . ASP B 139 ? 0.17030 0.40791 0.23057 -0.00190 -0.03142 0.08727  137 ASP B C   
2334 O O   . ASP B 139 ? 0.17814 0.41039 0.23592 -0.00131 -0.02973 0.08536  137 ASP B O   
2335 C CB  . ASP B 139 ? 0.22333 0.47662 0.27772 -0.02239 -0.03052 0.09550  137 ASP B CB  
2336 C CG  . ASP B 139 ? 0.22293 0.48039 0.27038 -0.03758 -0.03165 0.09775  137 ASP B CG  
2337 O OD1 . ASP B 139 ? 0.20635 0.45734 0.25190 -0.03746 -0.03423 0.09863  137 ASP B OD1 
2338 O OD2 . ASP B 139 ? 0.32421 0.59251 0.36556 -0.05235 -0.02983 0.09868  137 ASP B OD2 
2339 N N   . ALA B 140 ? 0.15123 0.39617 0.21553 0.00829  -0.03312 0.08657  138 ALA B N   
2340 C CA  . ALA B 140 ? 0.21802 0.46835 0.28121 0.01740  -0.03157 0.08106  138 ALA B CA  
2341 C C   . ALA B 140 ? 0.19508 0.47143 0.26094 0.01969  -0.02836 0.08513  138 ALA B C   
2342 O O   . ALA B 140 ? 0.17304 0.46576 0.24684 0.02144  -0.02906 0.09038  138 ALA B O   
2343 C CB  . ALA B 140 ? 0.25364 0.48966 0.31662 0.02698  -0.03223 0.07363  138 ALA B CB  
2344 N N   . LEU B 141 ? 0.14888 0.43371 0.20803 0.01821  -0.02515 0.08434  139 LEU B N   
2345 C CA  . LEU B 141 ? 0.16877 0.48247 0.22989 0.02023  -0.01990 0.08597  139 LEU B CA  
2346 C C   . LEU B 141 ? 0.21308 0.53060 0.27234 0.03493  -0.01643 0.07534  139 LEU B C   
2347 O O   . LEU B 141 ? 0.18502 0.48484 0.23408 0.03631  -0.01832 0.06778  139 LEU B O   
2348 C CB  . LEU B 141 ? 0.23233 0.55071 0.28177 0.00716  -0.01648 0.09260  139 LEU B CB  
2349 C CG  . LEU B 141 ? 0.34201 0.64402 0.38628 -0.00850 -0.01712 0.10011  139 LEU B CG  
2350 C CD1 . LEU B 141 ? 0.37211 0.66962 0.40038 -0.01832 -0.01243 0.10754  139 LEU B CD1 
2351 C CD2 . LEU B 141 ? 0.35742 0.67999 0.41107 -0.01832 -0.01700 0.10299  139 LEU B CD2 
2352 N N   . VAL B 142 ? 0.20965 0.55304 0.27903 0.04568  -0.01087 0.07367  140 VAL B N   
2353 C CA  . VAL B 142 ? 0.18565 0.53073 0.25298 0.06258  -0.00402 0.06067  140 VAL B CA  
2354 C C   . VAL B 142 ? 0.22274 0.60598 0.28762 0.06108  0.00557  0.05962  140 VAL B C   
2355 O O   . VAL B 142 ? 0.19877 0.61855 0.27745 0.05779  0.00873  0.06809  140 VAL B O   
2356 C CB  . VAL B 142 ? 0.20325 0.54399 0.28570 0.08279  -0.00316 0.05933  140 VAL B CB  
2357 C CG1 . VAL B 142 ? 0.27674 0.60701 0.35331 0.10195  0.00669  0.04256  140 VAL B CG1 
2358 C CG2 . VAL B 142 ? 0.21433 0.51854 0.29627 0.07915  -0.01267 0.06476  140 VAL B CG2 
2359 N N   . PHE B 143 ? 0.20074 0.57970 0.24667 0.06066  0.01022  0.04916  141 PHE B N   
2360 C CA  . PHE B 143 ? 0.28124 0.69450 0.31774 0.05644  0.02050  0.04767  141 PHE B CA  
2361 C C   . PHE B 143 ? 0.23842 0.65689 0.26918 0.07376  0.03194  0.02783  141 PHE B C   
2362 O O   . PHE B 143 ? 0.28983 0.67372 0.31277 0.08281  0.03036  0.01388  141 PHE B O   
2363 C CB  . PHE B 143 ? 0.22934 0.63475 0.24076 0.03867  0.01639  0.05448  141 PHE B CB  
2364 C CG  . PHE B 143 ? 0.23790 0.63407 0.25074 0.02301  0.00932  0.07275  141 PHE B CG  
2365 C CD1 . PHE B 143 ? 0.23610 0.59935 0.25217 0.02183  -0.00138 0.07634  141 PHE B CD1 
2366 C CD2 . PHE B 143 ? 0.25606 0.67553 0.26653 0.00805  0.01534  0.08503  141 PHE B CD2 
2367 C CE1 . PHE B 143 ? 0.24251 0.59242 0.25795 0.00936  -0.00520 0.09010  141 PHE B CE1 
2368 C CE2 . PHE B 143 ? 0.25067 0.65173 0.25845 -0.00789 0.01072  0.09956  141 PHE B CE2 
2369 C CZ  . PHE B 143 ? 0.27965 0.64425 0.29007 -0.00534 0.00085  0.10108  141 PHE B CZ  
2370 N N   . ASN B 144 ? 0.25406 0.71484 0.28560 0.07566  0.04515  0.02514  142 ASN B N   
2371 C CA  . ASN B 144 ? 0.28030 0.74921 0.30266 0.09148  0.05978  0.00384  142 ASN B CA  
2372 C C   . ASN B 144 ? 0.30119 0.80098 0.29909 0.07519  0.06832  0.00348  142 ASN B C   
2373 O O   . ASN B 144 ? 0.31047 0.84203 0.31164 0.05895  0.06928  0.02049  142 ASN B O   
2374 C CB  . ASN B 144 ? 0.30368 0.80283 0.35667 0.11780  0.07168  -0.00095 142 ASN B CB  
2375 C CG  . ASN B 144 ? 0.44472 0.95586 0.48829 0.13595  0.09121  -0.02455 142 ASN B CG  
2376 O OD1 . ASN B 144 ? 0.49787 0.96741 0.53336 0.15434  0.09563  -0.04320 142 ASN B OD1 
2377 N ND2 . ASN B 144 ? 0.46765 1.02424 0.50829 0.12731  0.10205  -0.02448 142 ASN B ND2 
2378 N N   . LEU B 145 ? 0.32733 0.81605 0.29715 0.07669  0.07477  -0.01578 143 LEU B N   
2379 C CA  . LEU B 145 ? 0.34844 0.86709 0.28879 0.06140  0.08348  -0.01709 143 LEU B CA  
2380 C C   . LEU B 145 ? 0.44503 0.97980 0.37761 0.07775  0.10419  -0.04456 143 LEU B C   
2381 O O   . LEU B 145 ? 0.54052 1.04103 0.46352 0.09124  0.10718  -0.06760 143 LEU B O   
2382 C CB  . LEU B 145 ? 0.35752 0.85035 0.26378 0.04300  0.06888  -0.01275 143 LEU B CB  
2383 C CG  . LEU B 145 ? 0.39154 0.90546 0.26090 0.02706  0.07386  -0.01428 143 LEU B CG  
2384 C CD1 . LEU B 145 ? 0.46844 1.00315 0.34502 0.01194  0.07500  0.00832  143 LEU B CD1 
2385 C CD2 . LEU B 145 ? 0.47942 0.97131 0.31860 0.01371  0.05616  -0.01039 143 LEU B CD2 
2386 N N   . ASN B 146 ? 0.40122 0.96849 0.34051 0.07334  0.11373  -0.04168 144 ASN B N   
2387 C CA  . ASN B 146 ? 0.46686 1.04405 0.39938 0.08684  0.13284  -0.06649 144 ASN B CA  
2388 C C   . ASN B 146 ? 0.51564 1.08876 0.40325 0.06648  0.13455  -0.07514 144 ASN B C   
2389 O O   . ASN B 146 ? 0.52600 1.10767 0.39792 0.04167  0.12389  -0.05441 144 ASN B O   
2390 C CB  . ASN B 146 ? 0.53842 1.15876 0.50063 0.09148  0.14273  -0.05955 144 ASN B CB  
2391 C CG  . ASN B 146 ? 0.44213 1.06983 0.44796 0.10971  0.13727  -0.04867 144 ASN B CG  
2392 O OD1 . ASN B 146 ? 0.49405 1.09118 0.50976 0.12863  0.13280  -0.05348 144 ASN B OD1 
2393 N ND2 . ASN B 146 ? 0.60841 1.27650 0.63831 0.10256  0.13691  -0.03401 144 ASN B ND2 
2394 N N   . PHE B 147 ? 0.59746 1.15210 0.46282 0.07680  0.14725  -0.10530 145 PHE B N   
2395 C CA  . PHE B 147 ? 0.56944 1.12351 0.39072 0.05688  0.14978  -0.11581 145 PHE B CA  
2396 C C   . PHE B 147 ? 0.78138 1.33008 0.58859 0.07151  0.17397  -0.14984 145 PHE B C   
2397 O O   . PHE B 147 ? 0.76557 1.28832 0.58603 0.09789  0.18584  -0.17156 145 PHE B O   
2398 C CB  . PHE B 147 ? 0.64688 1.17013 0.43716 0.04096  0.13099  -0.11631 145 PHE B CB  
2399 C CG  . PHE B 147 ? 0.66669 1.14926 0.45389 0.05608  0.13241  -0.14222 145 PHE B CG  
2400 C CD1 . PHE B 147 ? 0.60613 1.07416 0.42243 0.07067  0.12505  -0.13405 145 PHE B CD1 
2401 C CD2 . PHE B 147 ? 0.69294 1.14786 0.44572 0.05376  0.14155  -0.17530 145 PHE B CD2 
2402 C CE1 . PHE B 147 ? 0.57396 0.99151 0.38944 0.08179  0.12404  -0.15481 145 PHE B CE1 
2403 C CE2 . PHE B 147 ? 0.77174 1.18019 0.51865 0.06420  0.14340  -0.20076 145 PHE B CE2 
2404 C CZ  . PHE B 147 ? 0.76317 1.15228 0.54185 0.07861  0.13456  -0.19005 145 PHE B CZ  
# 
