data_8YV4
# 
_entry.id   8YV4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YV4         pdb_00008yv4 10.2210/pdb8yv4/pdb 
WWPDB D_1300046403 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YV4 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ganjhh@fudan.edu.cn 
_pdbx_contact_author.name_first         Jianhua 
_pdbx_contact_author.name_last          Gan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8438-8852 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cao, C.L.' 1 0009-0007-8207-5063 
'Gan, J.H.' 2 0000-0002-8438-8852 
# 
_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                     'The crystal structure of G.acetivorans RNA kinase Ark1' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cao, C.L.' 1 ? 
primary 'Gan, J.H.' 2 ? 
# 
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 'Putative serine/threonine protein kinase' 20954.289 2  ? ? ? ? 
2 non-polymer syn GLYCEROL                                   92.094    1  ? ? ? ? 
3 water       nat water                                      18.015    77 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Archaeal RNA kinase' 
# 
_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       
;MRGRHSVVRVEGDRAIKQFFPAYRYNFWKEAGFLSLLQEFDFVPRLYSINPEKLEIEMEFIEGRPIKDVINELNSETIGR
ILDICRKLDVLGIQKEEMNHPDRHIIISDRIVFIDFERGVIKCRPSNLTQFAVYLNSRLRLMKNEELKKLLREYKKGFDD
ESYRELRTQILQYM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRGRHSVVRVEGDRAIKQFFPAYRYNFWKEAGFLSLLQEFDFVPRLYSINPEKLEIEMEFIEGRPIKDVINELNSETIGR
ILDICRKLDVLGIQKEEMNHPDRHIIISDRIVFIDFERGVIKCRPSNLTQFAVYLNSRLRLMKNEELKKLLREYKKGFDD
ESYRELRTQILQYM
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL GOL 
3 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ARG n 
1 3   GLY n 
1 4   ARG n 
1 5   HIS n 
1 6   SER n 
1 7   VAL n 
1 8   VAL n 
1 9   ARG n 
1 10  VAL n 
1 11  GLU n 
1 12  GLY n 
1 13  ASP n 
1 14  ARG n 
1 15  ALA n 
1 16  ILE n 
1 17  LYS n 
1 18  GLN n 
1 19  PHE n 
1 20  PHE n 
1 21  PRO n 
1 22  ALA n 
1 23  TYR n 
1 24  ARG n 
1 25  TYR n 
1 26  ASN n 
1 27  PHE n 
1 28  TRP n 
1 29  LYS n 
1 30  GLU n 
1 31  ALA n 
1 32  GLY n 
1 33  PHE n 
1 34  LEU n 
1 35  SER n 
1 36  LEU n 
1 37  LEU n 
1 38  GLN n 
1 39  GLU n 
1 40  PHE n 
1 41  ASP n 
1 42  PHE n 
1 43  VAL n 
1 44  PRO n 
1 45  ARG n 
1 46  LEU n 
1 47  TYR n 
1 48  SER n 
1 49  ILE n 
1 50  ASN n 
1 51  PRO n 
1 52  GLU n 
1 53  LYS n 
1 54  LEU n 
1 55  GLU n 
1 56  ILE n 
1 57  GLU n 
1 58  MET n 
1 59  GLU n 
1 60  PHE n 
1 61  ILE n 
1 62  GLU n 
1 63  GLY n 
1 64  ARG n 
1 65  PRO n 
1 66  ILE n 
1 67  LYS n 
1 68  ASP n 
1 69  VAL n 
1 70  ILE n 
1 71  ASN n 
1 72  GLU n 
1 73  LEU n 
1 74  ASN n 
1 75  SER n 
1 76  GLU n 
1 77  THR n 
1 78  ILE n 
1 79  GLY n 
1 80  ARG n 
1 81  ILE n 
1 82  LEU n 
1 83  ASP n 
1 84  ILE n 
1 85  CYS n 
1 86  ARG n 
1 87  LYS n 
1 88  LEU n 
1 89  ASP n 
1 90  VAL n 
1 91  LEU n 
1 92  GLY n 
1 93  ILE n 
1 94  GLN n 
1 95  LYS n 
1 96  GLU n 
1 97  GLU n 
1 98  MET n 
1 99  ASN n 
1 100 HIS n 
1 101 PRO n 
1 102 ASP n 
1 103 ARG n 
1 104 HIS n 
1 105 ILE n 
1 106 ILE n 
1 107 ILE n 
1 108 SER n 
1 109 ASP n 
1 110 ARG n 
1 111 ILE n 
1 112 VAL n 
1 113 PHE n 
1 114 ILE n 
1 115 ASP n 
1 116 PHE n 
1 117 GLU n 
1 118 ARG n 
1 119 GLY n 
1 120 VAL n 
1 121 ILE n 
1 122 LYS n 
1 123 CYS n 
1 124 ARG n 
1 125 PRO n 
1 126 SER n 
1 127 ASN n 
1 128 LEU n 
1 129 THR n 
1 130 GLN n 
1 131 PHE n 
1 132 ALA n 
1 133 VAL n 
1 134 TYR n 
1 135 LEU n 
1 136 ASN n 
1 137 SER n 
1 138 ARG n 
1 139 LEU n 
1 140 ARG n 
1 141 LEU n 
1 142 MET n 
1 143 LYS n 
1 144 ASN n 
1 145 GLU n 
1 146 GLU n 
1 147 LEU n 
1 148 LYS n 
1 149 LYS n 
1 150 LEU n 
1 151 LEU n 
1 152 ARG n 
1 153 GLU n 
1 154 TYR n 
1 155 LYS n 
1 156 LYS n 
1 157 GLY n 
1 158 PHE n 
1 159 ASP n 
1 160 ASP n 
1 161 GLU n 
1 162 SER n 
1 163 TYR n 
1 164 ARG n 
1 165 GLU n 
1 166 LEU n 
1 167 ARG n 
1 168 THR n 
1 169 GLN n 
1 170 ILE n 
1 171 LEU n 
1 172 GLN n 
1 173 TYR n 
1 174 MET 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                   174 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GACE_0057 
_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      'Geoglobus acetivorans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     565033 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ARG 2   2   ?   ?   ?   A . n 
A 1 3   GLY 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   HIS 5   5   5   HIS HIS A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   VAL 8   8   8   VAL VAL A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  GLN 18  18  18  GLN GLN A . n 
A 1 19  PHE 19  19  19  PHE PHE A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  TRP 28  28  28  TRP TRP A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  PRO 51  51  51  PRO PRO A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  MET 58  58  58  MET MET A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  ILE 81  81  81  ILE ILE A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ASP 89  89  89  ASP ASP A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  MET 98  98  98  MET MET A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 PHE 113 113 113 PHE PHE A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 CYS 123 123 123 CYS CYS A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 TYR 134 134 134 TYR TYR A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 ASN 136 136 136 ASN ASN A . n 
A 1 137 SER 137 137 137 SER SER A . n 
A 1 138 ARG 138 138 138 ARG ARG A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 MET 142 142 142 MET MET A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 GLU 153 153 153 GLU GLU A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 GLN 172 172 172 GLN GLN A . n 
A 1 173 TYR 173 173 173 TYR TYR A . n 
A 1 174 MET 174 174 174 MET MET A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ARG 2   2   ?   ?   ?   B . n 
B 1 3   GLY 3   3   ?   ?   ?   B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   HIS 5   5   5   HIS HIS B . n 
B 1 6   SER 6   6   6   SER SER B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   VAL 8   8   8   VAL VAL B . n 
B 1 9   ARG 9   9   9   ARG ARG B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  GLU 11  11  11  GLU GLU B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  ASP 13  13  13  ASP ASP B . n 
B 1 14  ARG 14  14  14  ARG ARG B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  GLN 18  18  18  GLN GLN B . n 
B 1 19  PHE 19  19  19  PHE PHE B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  TYR 23  23  23  TYR TYR B . n 
B 1 24  ARG 24  24  24  ARG ARG B . n 
B 1 25  TYR 25  25  25  TYR TYR B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  TRP 28  28  28  TRP TRP B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  GLU 30  30  30  GLU GLU B . n 
B 1 31  ALA 31  31  31  ALA ALA B . n 
B 1 32  GLY 32  32  32  GLY GLY B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  SER 35  35  35  SER SER B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  PHE 42  42  42  PHE PHE B . n 
B 1 43  VAL 43  43  43  VAL VAL B . n 
B 1 44  PRO 44  44  44  PRO PRO B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  TYR 47  47  47  TYR TYR B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  ILE 49  49  49  ILE ILE B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  PRO 51  51  51  PRO PRO B . n 
B 1 52  GLU 52  52  52  GLU GLU B . n 
B 1 53  LYS 53  53  53  LYS LYS B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ILE 56  56  56  ILE ILE B . n 
B 1 57  GLU 57  57  57  GLU GLU B . n 
B 1 58  MET 58  58  58  MET MET B . n 
B 1 59  GLU 59  59  59  GLU GLU B . n 
B 1 60  PHE 60  60  60  PHE PHE B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  ARG 64  64  64  ARG ARG B . n 
B 1 65  PRO 65  65  65  PRO PRO B . n 
B 1 66  ILE 66  66  66  ILE ILE B . n 
B 1 67  LYS 67  67  67  LYS LYS B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  VAL 69  69  69  VAL VAL B . n 
B 1 70  ILE 70  70  70  ILE ILE B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  GLU 72  72  72  GLU GLU B . n 
B 1 73  LEU 73  73  73  LEU LEU B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  SER 75  75  75  SER SER B . n 
B 1 76  GLU 76  76  76  GLU GLU B . n 
B 1 77  THR 77  77  77  THR THR B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  ILE 81  81  81  ILE ILE B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  ARG 86  86  86  ARG ARG B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ASP 89  89  89  ASP ASP B . n 
B 1 90  VAL 90  90  90  VAL VAL B . n 
B 1 91  LEU 91  91  91  LEU LEU B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  ILE 93  93  93  ILE ILE B . n 
B 1 94  GLN 94  94  94  GLN GLN B . n 
B 1 95  LYS 95  95  95  LYS LYS B . n 
B 1 96  GLU 96  96  96  GLU GLU B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  MET 98  98  98  MET MET B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 HIS 100 100 100 HIS HIS B . n 
B 1 101 PRO 101 101 101 PRO PRO B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 ARG 103 103 103 ARG ARG B . n 
B 1 104 HIS 104 104 104 HIS HIS B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 ARG 110 110 110 ARG ARG B . n 
B 1 111 ILE 111 111 111 ILE ILE B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 PHE 113 113 113 PHE PHE B . n 
B 1 114 ILE 114 114 114 ILE ILE B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 ARG 118 118 118 ARG ARG B . n 
B 1 119 GLY 119 119 119 GLY GLY B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 ILE 121 121 121 ILE ILE B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 CYS 123 123 123 CYS CYS B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 ASN 127 127 127 ASN ASN B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 THR 129 129 129 THR THR B . n 
B 1 130 GLN 130 130 130 GLN GLN B . n 
B 1 131 PHE 131 131 131 PHE PHE B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 VAL 133 133 133 VAL VAL B . n 
B 1 134 TYR 134 134 134 TYR TYR B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 ASN 136 136 136 ASN ASN B . n 
B 1 137 SER 137 137 137 SER SER B . n 
B 1 138 ARG 138 138 138 ARG ARG B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ARG 140 140 140 ARG ARG B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 MET 142 142 142 MET MET B . n 
B 1 143 LYS 143 143 143 LYS LYS B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 GLU 145 145 145 GLU GLU B . n 
B 1 146 GLU 146 146 146 GLU GLU B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 LYS 149 149 149 LYS LYS B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ARG 152 152 152 ARG ARG B . n 
B 1 153 GLU 153 153 153 GLU GLU B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 LYS 155 155 155 LYS LYS B . n 
B 1 156 LYS 156 156 156 LYS LYS B . n 
B 1 157 GLY 157 157 157 GLY GLY B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 ASP 159 159 159 ASP ASP B . n 
B 1 160 ASP 160 160 160 ASP ASP B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 SER 162 162 162 SER SER B . n 
B 1 163 TYR 163 163 163 TYR TYR B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 GLU 165 165 165 GLU GLU B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 GLN 169 169 169 GLN GLN B . n 
B 1 170 ILE 170 170 170 ILE ILE B . n 
B 1 171 LEU 171 171 171 LEU LEU B . n 
B 1 172 GLN 172 172 172 GLN GLN B . n 
B 1 173 TYR 173 173 173 TYR TYR B . n 
B 1 174 MET 174 174 174 MET MET B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        GOL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   GOL 
_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 GOL 1  201 201 GOL GOL B . 
D 3 HOH 1  201 83  HOH HOH A . 
D 3 HOH 2  202 67  HOH HOH A . 
D 3 HOH 3  203 24  HOH HOH A . 
D 3 HOH 4  204 88  HOH HOH A . 
D 3 HOH 5  205 87  HOH HOH A . 
D 3 HOH 6  206 72  HOH HOH A . 
D 3 HOH 7  207 15  HOH HOH A . 
D 3 HOH 8  208 4   HOH HOH A . 
D 3 HOH 9  209 74  HOH HOH A . 
D 3 HOH 10 210 86  HOH HOH A . 
D 3 HOH 11 211 89  HOH HOH A . 
D 3 HOH 12 212 36  HOH HOH A . 
D 3 HOH 13 213 17  HOH HOH A . 
D 3 HOH 14 214 62  HOH HOH A . 
D 3 HOH 15 215 51  HOH HOH A . 
D 3 HOH 16 216 33  HOH HOH A . 
D 3 HOH 17 217 3   HOH HOH A . 
D 3 HOH 18 218 52  HOH HOH A . 
D 3 HOH 19 219 55  HOH HOH A . 
D 3 HOH 20 220 70  HOH HOH A . 
D 3 HOH 21 221 1   HOH HOH A . 
D 3 HOH 22 222 31  HOH HOH A . 
D 3 HOH 23 223 49  HOH HOH A . 
D 3 HOH 24 224 7   HOH HOH A . 
D 3 HOH 25 225 69  HOH HOH A . 
D 3 HOH 26 226 21  HOH HOH A . 
D 3 HOH 27 227 57  HOH HOH A . 
D 3 HOH 28 228 65  HOH HOH A . 
D 3 HOH 29 229 71  HOH HOH A . 
D 3 HOH 30 230 45  HOH HOH A . 
D 3 HOH 31 231 10  HOH HOH A . 
D 3 HOH 32 232 53  HOH HOH A . 
D 3 HOH 33 233 34  HOH HOH A . 
D 3 HOH 34 234 14  HOH HOH A . 
D 3 HOH 35 235 63  HOH HOH A . 
D 3 HOH 36 236 90  HOH HOH A . 
D 3 HOH 37 237 75  HOH HOH A . 
E 3 HOH 1  301 82  HOH HOH B . 
E 3 HOH 2  302 40  HOH HOH B . 
E 3 HOH 3  303 35  HOH HOH B . 
E 3 HOH 4  304 28  HOH HOH B . 
E 3 HOH 5  305 68  HOH HOH B . 
E 3 HOH 6  306 41  HOH HOH B . 
E 3 HOH 7  307 44  HOH HOH B . 
E 3 HOH 8  308 84  HOH HOH B . 
E 3 HOH 9  309 12  HOH HOH B . 
E 3 HOH 10 310 54  HOH HOH B . 
E 3 HOH 11 311 5   HOH HOH B . 
E 3 HOH 12 312 78  HOH HOH B . 
E 3 HOH 13 313 2   HOH HOH B . 
E 3 HOH 14 314 76  HOH HOH B . 
E 3 HOH 15 315 47  HOH HOH B . 
E 3 HOH 16 316 38  HOH HOH B . 
E 3 HOH 17 317 19  HOH HOH B . 
E 3 HOH 18 318 6   HOH HOH B . 
E 3 HOH 19 319 20  HOH HOH B . 
E 3 HOH 20 320 22  HOH HOH B . 
E 3 HOH 21 321 18  HOH HOH B . 
E 3 HOH 22 322 16  HOH HOH B . 
E 3 HOH 23 323 66  HOH HOH B . 
E 3 HOH 24 324 43  HOH HOH B . 
E 3 HOH 25 325 8   HOH HOH B . 
E 3 HOH 26 326 59  HOH HOH B . 
E 3 HOH 27 327 58  HOH HOH B . 
E 3 HOH 28 328 85  HOH HOH B . 
E 3 HOH 29 329 37  HOH HOH B . 
E 3 HOH 30 330 26  HOH HOH B . 
E 3 HOH 31 331 80  HOH HOH B . 
E 3 HOH 32 332 42  HOH HOH B . 
E 3 HOH 33 333 61  HOH HOH B . 
E 3 HOH 34 334 48  HOH HOH B . 
E 3 HOH 35 335 29  HOH HOH B . 
E 3 HOH 36 336 81  HOH HOH B . 
E 3 HOH 37 337 79  HOH HOH B . 
E 3 HOH 38 338 39  HOH HOH B . 
E 3 HOH 39 339 77  HOH HOH B . 
E 3 HOH 40 340 73  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ARG 4   ? CG  ? A ARG 4   CG  
2  1 Y 1 A ARG 4   ? CD  ? A ARG 4   CD  
3  1 Y 1 A ARG 4   ? NE  ? A ARG 4   NE  
4  1 Y 1 A ARG 4   ? CZ  ? A ARG 4   CZ  
5  1 Y 1 A ARG 4   ? NH1 ? A ARG 4   NH1 
6  1 Y 1 A ARG 4   ? NH2 ? A ARG 4   NH2 
7  1 Y 1 A ARG 24  ? CD  ? A ARG 24  CD  
8  1 Y 1 A ARG 24  ? NE  ? A ARG 24  NE  
9  1 Y 1 A ARG 24  ? CZ  ? A ARG 24  CZ  
10 1 Y 1 A ARG 24  ? NH1 ? A ARG 24  NH1 
11 1 Y 1 A ARG 24  ? NH2 ? A ARG 24  NH2 
12 1 Y 1 A ASP 109 ? CG  ? A ASP 109 CG  
13 1 Y 1 A ASP 109 ? OD1 ? A ASP 109 OD1 
14 1 Y 1 A ASP 109 ? OD2 ? A ASP 109 OD2 
15 1 Y 1 A LYS 143 ? CG  ? A LYS 143 CG  
16 1 Y 1 A LYS 143 ? CD  ? A LYS 143 CD  
17 1 Y 1 A LYS 143 ? CE  ? A LYS 143 CE  
18 1 Y 1 A LYS 143 ? NZ  ? A LYS 143 NZ  
19 1 Y 1 A GLU 145 ? CG  ? A GLU 145 CG  
20 1 Y 1 A GLU 145 ? CD  ? A GLU 145 CD  
21 1 Y 1 A GLU 145 ? OE1 ? A GLU 145 OE1 
22 1 Y 1 A GLU 145 ? OE2 ? A GLU 145 OE2 
23 1 Y 1 A GLU 146 ? CD  ? A GLU 146 CD  
24 1 Y 1 A GLU 146 ? OE1 ? A GLU 146 OE1 
25 1 Y 1 A GLU 146 ? OE2 ? A GLU 146 OE2 
26 1 Y 1 A LYS 149 ? CG  ? A LYS 149 CG  
27 1 Y 1 A LYS 149 ? CD  ? A LYS 149 CD  
28 1 Y 1 A LYS 149 ? CE  ? A LYS 149 CE  
29 1 Y 1 A LYS 149 ? NZ  ? A LYS 149 NZ  
30 1 Y 1 A GLU 153 ? CG  ? A GLU 153 CG  
31 1 Y 1 A GLU 153 ? CD  ? A GLU 153 CD  
32 1 Y 1 A GLU 153 ? OE1 ? A GLU 153 OE1 
33 1 Y 1 A GLU 153 ? OE2 ? A GLU 153 OE2 
34 1 Y 1 A LYS 155 ? CD  ? A LYS 155 CD  
35 1 Y 1 A LYS 155 ? CE  ? A LYS 155 CE  
36 1 Y 1 A LYS 155 ? NZ  ? A LYS 155 NZ  
37 1 Y 1 A LYS 156 ? CG  ? A LYS 156 CG  
38 1 Y 1 A LYS 156 ? CD  ? A LYS 156 CD  
39 1 Y 1 A LYS 156 ? CE  ? A LYS 156 CE  
40 1 Y 1 A LYS 156 ? NZ  ? A LYS 156 NZ  
41 1 Y 1 A GLU 161 ? CG  ? A GLU 161 CG  
42 1 Y 1 A GLU 161 ? CD  ? A GLU 161 CD  
43 1 Y 1 A GLU 161 ? OE1 ? A GLU 161 OE1 
44 1 Y 1 A GLU 161 ? OE2 ? A GLU 161 OE2 
45 1 Y 1 A ARG 164 ? CG  ? A ARG 164 CG  
46 1 Y 1 A ARG 164 ? CD  ? A ARG 164 CD  
47 1 Y 1 A ARG 164 ? NE  ? A ARG 164 NE  
48 1 Y 1 A ARG 164 ? CZ  ? A ARG 164 CZ  
49 1 Y 1 A ARG 164 ? NH1 ? A ARG 164 NH1 
50 1 Y 1 A ARG 164 ? NH2 ? A ARG 164 NH2 
51 1 Y 1 A GLU 165 ? CG  ? A GLU 165 CG  
52 1 Y 1 A GLU 165 ? CD  ? A GLU 165 CD  
53 1 Y 1 A GLU 165 ? OE1 ? A GLU 165 OE1 
54 1 Y 1 A GLU 165 ? OE2 ? A GLU 165 OE2 
55 1 Y 1 A GLN 172 ? CG  ? A GLN 172 CG  
56 1 Y 1 A GLN 172 ? CD  ? A GLN 172 CD  
57 1 Y 1 A GLN 172 ? OE1 ? A GLN 172 OE1 
58 1 Y 1 A GLN 172 ? NE2 ? A GLN 172 NE2 
59 1 Y 1 B ARG 4   ? CG  ? B ARG 4   CG  
60 1 Y 1 B ARG 4   ? CD  ? B ARG 4   CD  
61 1 Y 1 B ARG 4   ? NE  ? B ARG 4   NE  
62 1 Y 1 B ARG 4   ? CZ  ? B ARG 4   CZ  
63 1 Y 1 B ARG 4   ? NH1 ? B ARG 4   NH1 
64 1 Y 1 B ARG 4   ? NH2 ? B ARG 4   NH2 
65 1 Y 1 B GLU 52  ? CG  ? B GLU 52  CG  
66 1 Y 1 B GLU 52  ? CD  ? B GLU 52  CD  
67 1 Y 1 B GLU 52  ? OE1 ? B GLU 52  OE1 
68 1 Y 1 B GLU 52  ? OE2 ? B GLU 52  OE2 
69 1 Y 1 B ARG 138 ? CZ  ? B ARG 138 CZ  
70 1 Y 1 B ARG 138 ? NH1 ? B ARG 138 NH1 
71 1 Y 1 B ARG 138 ? NH2 ? B ARG 138 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.19.1_4122: ???)' 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0123             2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? 7.21                 3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? 7.21                 4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? 2.7.0                5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.46 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YV4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.870 
_cell.length_a_esd                 ? 
_cell.length_b                     63.297 
_cell.length_b_esd                 ? 
_cell.length_c                     70.220 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8YV4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   8YV4 
_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             2.68 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.05 
_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    
;0.1M tri-Sodium citrate pH5.5
20%(w/v) PEG 3000
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-24 
_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   0.987 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YV4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.87 
_reflns.d_resolution_low                               50.79 
_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                                     35482 
_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                           96.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.87 
_reflns_shell.d_res_low                                     1.97 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             35482 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.539 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YV4 
_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                            1.87 
_refine.ls_d_res_low                             26.86 
_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                     35482 
_refine.ls_number_reflns_R_free                  1752 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.38 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1929 
_refine.ls_R_factor_R_free                       0.2204 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1914 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.18 
_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                            0.22 
_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                       1.87 
_refine_hist.d_res_low                        26.86 
_refine_hist.number_atoms_solvent             77 
_refine_hist.number_atoms_total               2912 
_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        2835 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.009  ? 2904 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.020  ? 3908 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.348 ? 1117 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.066  ? 423  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.019  ? 504  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.87 1.92  . . 65  1726 63.00  . . . . 0.3299 . . . . . . . . . . . 0.4123 
'X-RAY DIFFRACTION' 1.92 1.97  . . 99  2259 83.00  . . . . 0.2659 . . . . . . . . . . . 0.3638 
'X-RAY DIFFRACTION' 1.97 2.04  . . 133 2585 96.00  . . . . 0.2232 . . . . . . . . . . . 0.2917 
'X-RAY DIFFRACTION' 2.04 2.11  . . 151 2676 100.00 . . . . 0.2140 . . . . . . . . . . . 0.2288 
'X-RAY DIFFRACTION' 2.11 2.19  . . 122 2732 100.00 . . . . 0.1952 . . . . . . . . . . . 0.1976 
'X-RAY DIFFRACTION' 2.19 2.29  . . 134 2692 100.00 . . . . 0.2001 . . . . . . . . . . . 0.2304 
'X-RAY DIFFRACTION' 2.29 2.41  . . 155 2695 100.00 . . . . 0.2129 . . . . . . . . . . . 0.2709 
'X-RAY DIFFRACTION' 2.41 2.56  . . 148 2696 100.00 . . . . 0.2135 . . . . . . . . . . . 0.2459 
'X-RAY DIFFRACTION' 2.56 2.76  . . 144 2735 100.00 . . . . 0.2128 . . . . . . . . . . . 0.2693 
'X-RAY DIFFRACTION' 2.76 3.04  . . 142 2710 100.00 . . . . 0.2211 . . . . . . . . . . . 0.2308 
'X-RAY DIFFRACTION' 3.04 3.48  . . 171 2703 100.00 . . . . 0.1991 . . . . . . . . . . . 0.2373 
'X-RAY DIFFRACTION' 3.48 4.38  . . 135 2749 100.00 . . . . 0.1625 . . . . . . . . . . . 0.1750 
'X-RAY DIFFRACTION' 4.38 26.86 . . 153 2772 99.00  . . . . 0.1625 . . . . . . . . . . . 0.1890 
# 
_struct.entry_id                     8YV4 
_struct.title                        'The crystal structure of G.acetivorans RNA kinase Ark1' 
_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        8YV4 
_struct_keywords.text            'Kinase, 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 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0A7GDU7_GEOAI 
_struct_ref.pdbx_db_accession          A0A0A7GDU7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRGRHSVVRVEGDRAIKQFFPAYRYNFWKEAGFLSLLQEFDFVPRLYSINPEKLEIEMEFIEGRPIKDVINELNSETIGR
ILDICRKLDVLGIQKEEMNHPDRHIIISDRIVFIDFERGVIKCRPSNLTQFAVYLNSRLRLMKNEELKKLLREYKKGFDD
ESYRELRTQILQYM
;
_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 8YV4 A 1 ? 174 ? A0A0A7GDU7 1 ? 174 ? 1 174 
2 1 8YV4 B 1 ? 174 ? A0A0A7GDU7 1 ? 174 ? 1 174 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1970  ? 
1 MORE         -18   ? 
1 'SSA (A^2)'  16150 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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 TYR A 23  ? LEU A 37  ? TYR A 23  LEU A 37  1 ? 15 
HELX_P HELX_P2  AA2 LYS A 67  ? LEU A 73  ? LYS A 67  LEU A 73  5 ? 7  
HELX_P HELX_P3  AA3 ASN A 74  ? GLY A 92  ? ASN A 74  GLY A 92  1 ? 19 
HELX_P HELX_P4  AA4 SER A 126 ? ARG A 140 ? SER A 126 ARG A 140 1 ? 15 
HELX_P HELX_P5  AA5 LYS A 143 ? PHE A 158 ? LYS A 143 PHE A 158 1 ? 16 
HELX_P HELX_P6  AA6 ASP A 159 ? GLN A 172 ? ASP A 159 GLN A 172 1 ? 14 
HELX_P HELX_P7  AA7 TYR B 23  ? GLN B 38  ? TYR B 23  GLN B 38  1 ? 16 
HELX_P HELX_P8  AA8 LYS B 67  ? LEU B 73  ? LYS B 67  LEU B 73  5 ? 7  
HELX_P HELX_P9  AA9 ASN B 74  ? GLY B 92  ? ASN B 74  GLY B 92  1 ? 19 
HELX_P HELX_P10 AB1 SER B 126 ? ARG B 140 ? SER B 126 ARG B 140 1 ? 15 
HELX_P HELX_P11 AB2 LYS B 143 ? PHE B 158 ? LYS B 143 PHE B 158 1 ? 16 
HELX_P HELX_P12 AB3 ASP B 159 ? GLN B 172 ? ASP B 159 GLN B 172 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? 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 SER A 6   ? GLU A 11  ? SER A 6   GLU A 11  
AA1 2 ARG A 14  ? PHE A 19  ? ARG A 14  PHE A 19  
AA1 3 GLU A 55  ? GLU A 59  ? GLU A 55  GLU A 59  
AA1 4 LEU A 46  ? ASN A 50  ? LEU A 46  ASN A 50  
AA2 1 ARG A 64  ? PRO A 65  ? ARG A 64  PRO A 65  
AA2 2 ILE A 105 ? ILE A 107 ? ILE A 105 ILE A 107 
AA2 3 ILE A 111 ? PHE A 113 ? ILE A 111 PHE A 113 
AA3 1 ILE A 93  ? GLN A 94  ? ILE A 93  GLN A 94  
AA3 2 VAL A 120 ? ILE A 121 ? VAL A 120 ILE A 121 
AA4 1 SER B 6   ? GLU B 11  ? SER B 6   GLU B 11  
AA4 2 ARG B 14  ? PHE B 19  ? ARG B 14  PHE B 19  
AA4 3 GLU B 55  ? GLU B 59  ? GLU B 55  GLU B 59  
AA4 4 LEU B 46  ? ASN B 50  ? LEU B 46  ASN B 50  
AA5 1 ARG B 64  ? PRO B 65  ? ARG B 64  PRO B 65  
AA5 2 ILE B 105 ? ILE B 107 ? ILE B 105 ILE B 107 
AA5 3 ILE B 111 ? PHE B 113 ? ILE B 111 PHE B 113 
AA6 1 ILE B 93  ? GLN B 94  ? ILE B 93  GLN B 94  
AA6 2 VAL B 120 ? ILE B 121 ? VAL B 120 ILE B 121 
# 
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 ARG A 9   ? N ARG A 9   O ILE A 16  ? O ILE A 16  
AA1 2 3 N ALA A 15  ? N ALA A 15  O MET A 58  ? O MET A 58  
AA1 3 4 O GLU A 57  ? O GLU A 57  N TYR A 47  ? N TYR A 47  
AA2 1 2 N ARG A 64  ? N ARG A 64  O ILE A 107 ? O ILE A 107 
AA2 2 3 N ILE A 106 ? N ILE A 106 O VAL A 112 ? O VAL A 112 
AA3 1 2 N GLN A 94  ? N GLN A 94  O VAL A 120 ? O VAL A 120 
AA4 1 2 N ARG B 9   ? N ARG B 9   O ILE B 16  ? O ILE B 16  
AA4 2 3 N LYS B 17  ? N LYS B 17  O ILE B 56  ? O ILE B 56  
AA4 3 4 O GLU B 57  ? O GLU B 57  N TYR B 47  ? N TYR B 47  
AA5 1 2 N ARG B 64  ? N ARG B 64  O ILE B 107 ? O ILE B 107 
AA5 2 3 N ILE B 106 ? N ILE B 106 O VAL B 112 ? O VAL B 112 
AA6 1 2 N GLN B 94  ? N GLN B 94  O VAL B 120 ? O VAL B 120 
# 
_pdbx_entry_details.entry_id                   8YV4 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 96  ? ? 76.09   156.31  
2 1 SER A 108 ? ? -128.72 -133.87 
3 1 ASP A 115 ? ? 75.89   86.16   
4 1 ARG A 140 ? ? 39.91   56.24   
5 1 GLU B 96  ? ? 77.42   157.97  
6 1 SER B 108 ? ? -129.58 -133.49 
7 1 ASP B 115 ? ? 74.87   86.26   
8 1 ARG B 140 ? ? 38.01   55.47   
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     118 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.243 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         0.4417 
_pdbx_refine_tls.origin_y         6.8477 
_pdbx_refine_tls.origin_z         25.3529 
_pdbx_refine_tls.T[1][1]          0.2352 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0634 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0212 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2398 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0231 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2514 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.5108 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.3479 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0448 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.3815 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0004 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.5698 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0361 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.2331 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0352 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0903 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0482 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0957 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.2069 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.5224 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0143 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A ARG 2 ? A ARG 2 
3 1 Y 1 A GLY 3 ? A GLY 3 
4 1 Y 1 B MET 1 ? B MET 1 
5 1 Y 1 B ARG 2 ? B ARG 2 
6 1 Y 1 B GLY 3 ? B GLY 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PRO N    N N N 287 
PRO CA   C N S 288 
PRO C    C N N 289 
PRO O    O N N 290 
PRO CB   C N N 291 
PRO CG   C N N 292 
PRO CD   C N N 293 
PRO OXT  O N N 294 
PRO H    H N N 295 
PRO HA   H N N 296 
PRO HB2  H N N 297 
PRO HB3  H N N 298 
PRO HG2  H N N 299 
PRO HG3  H N N 300 
PRO HD2  H N N 301 
PRO HD3  H N N 302 
PRO HXT  H N N 303 
SER N    N N N 304 
SER CA   C N S 305 
SER C    C N N 306 
SER O    O N N 307 
SER CB   C N N 308 
SER OG   O N N 309 
SER OXT  O N N 310 
SER H    H N N 311 
SER H2   H N N 312 
SER HA   H N N 313 
SER HB2  H N N 314 
SER HB3  H N N 315 
SER HG   H N N 316 
SER HXT  H N N 317 
THR N    N N N 318 
THR CA   C N S 319 
THR C    C N N 320 
THR O    O N N 321 
THR CB   C N R 322 
THR OG1  O N N 323 
THR CG2  C N N 324 
THR OXT  O N N 325 
THR H    H N N 326 
THR H2   H N N 327 
THR HA   H N N 328 
THR HB   H N N 329 
THR HG1  H N N 330 
THR HG21 H N N 331 
THR HG22 H N N 332 
THR HG23 H N N 333 
THR HXT  H N N 334 
TRP N    N N N 335 
TRP CA   C N S 336 
TRP C    C N N 337 
TRP O    O N N 338 
TRP CB   C N N 339 
TRP CG   C Y N 340 
TRP CD1  C Y N 341 
TRP CD2  C Y N 342 
TRP NE1  N Y N 343 
TRP CE2  C Y N 344 
TRP CE3  C Y N 345 
TRP CZ2  C Y N 346 
TRP CZ3  C Y N 347 
TRP CH2  C Y N 348 
TRP OXT  O N N 349 
TRP H    H N N 350 
TRP H2   H N N 351 
TRP HA   H N N 352 
TRP HB2  H N N 353 
TRP HB3  H N N 354 
TRP HD1  H N N 355 
TRP HE1  H N N 356 
TRP HE3  H N N 357 
TRP HZ2  H N N 358 
TRP HZ3  H N N 359 
TRP HH2  H N N 360 
TRP HXT  H N N 361 
TYR N    N N N 362 
TYR CA   C N S 363 
TYR C    C N N 364 
TYR O    O N N 365 
TYR CB   C N N 366 
TYR CG   C Y N 367 
TYR CD1  C Y N 368 
TYR CD2  C Y N 369 
TYR CE1  C Y N 370 
TYR CE2  C Y N 371 
TYR CZ   C Y N 372 
TYR OH   O N N 373 
TYR OXT  O N N 374 
TYR H    H N N 375 
TYR H2   H N N 376 
TYR HA   H N N 377 
TYR HB2  H N N 378 
TYR HB3  H N N 379 
TYR HD1  H N N 380 
TYR HD2  H N N 381 
TYR HE1  H N N 382 
TYR HE2  H N N 383 
TYR HH   H N N 384 
TYR HXT  H N N 385 
VAL N    N N N 386 
VAL CA   C N S 387 
VAL C    C N N 388 
VAL O    O N N 389 
VAL CB   C N N 390 
VAL CG1  C N N 391 
VAL CG2  C N N 392 
VAL OXT  O N N 393 
VAL H    H N N 394 
VAL H2   H N N 395 
VAL HA   H N N 396 
VAL HB   H N N 397 
VAL HG11 H N N 398 
VAL HG12 H N N 399 
VAL HG13 H N N 400 
VAL HG21 H N N 401 
VAL HG22 H N N 402 
VAL HG23 H N N 403 
VAL HXT  H N N 404 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YV4 
_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]   0.018563 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006560 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015799 
_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]   0.015104 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ARG A 1 4   ? 14.020  21.377  12.900  1.00 60.64  ? 4   ARG A N   1 
ATOM   2    C CA  . ARG A 1 4   ? 13.810  22.624  13.623  1.00 62.27  ? 4   ARG A CA  1 
ATOM   3    C C   . ARG A 1 4   ? 13.656  22.387  15.134  1.00 55.93  ? 4   ARG A C   1 
ATOM   4    O O   . ARG A 1 4   ? 14.059  23.224  15.944  1.00 61.47  ? 4   ARG A O   1 
ATOM   5    C CB  . ARG A 1 4   ? 12.579  23.356  13.074  1.00 62.09  ? 4   ARG A CB  1 
ATOM   6    N N   . HIS A 1 5   ? 13.062  21.255  15.514  1.00 50.60  ? 5   HIS A N   1 
ATOM   7    C CA  . HIS A 1 5   ? 12.859  20.941  16.924  1.00 46.30  ? 5   HIS A CA  1 
ATOM   8    C C   . HIS A 1 5   ? 14.039  20.225  17.560  1.00 46.46  ? 5   HIS A C   1 
ATOM   9    O O   . HIS A 1 5   ? 14.141  20.205  18.797  1.00 36.03  ? 5   HIS A O   1 
ATOM   10   C CB  . HIS A 1 5   ? 11.610  20.083  17.110  1.00 47.86  ? 5   HIS A CB  1 
ATOM   11   C CG  . HIS A 1 5   ? 10.334  20.836  16.946  1.00 49.91  ? 5   HIS A CG  1 
ATOM   12   N ND1 . HIS A 1 5   ? 10.264  22.041  16.278  1.00 59.78  ? 5   HIS A ND1 1 
ATOM   13   C CD2 . HIS A 1 5   ? 9.072   20.552  17.344  1.00 56.34  ? 5   HIS A CD2 1 
ATOM   14   C CE1 . HIS A 1 5   ? 9.016   22.474  16.286  1.00 59.00  ? 5   HIS A CE1 1 
ATOM   15   N NE2 . HIS A 1 5   ? 8.273   21.590  16.928  1.00 65.41  ? 5   HIS A NE2 1 
ATOM   16   N N   . SER A 1 6   ? 14.895  19.589  16.764  1.00 38.69  ? 6   SER A N   1 
ATOM   17   C CA  . SER A 1 6   ? 15.885  18.685  17.331  1.00 37.21  ? 6   SER A CA  1 
ATOM   18   C C   . SER A 1 6   ? 17.024  18.490  16.345  1.00 46.76  ? 6   SER A C   1 
ATOM   19   O O   . SER A 1 6   ? 16.951  18.906  15.185  1.00 44.25  ? 6   SER A O   1 
ATOM   20   C CB  . SER A 1 6   ? 15.237  17.340  17.680  1.00 39.55  ? 6   SER A CB  1 
ATOM   21   O OG  . SER A 1 6   ? 14.779  16.745  16.470  1.00 43.48  ? 6   SER A OG  1 
ATOM   22   N N   . VAL A 1 7   ? 18.095  17.866  16.838  1.00 39.34  ? 7   VAL A N   1 
ATOM   23   C CA  . VAL A 1 7   ? 19.241  17.478  16.025  1.00 44.61  ? 7   VAL A CA  1 
ATOM   24   C C   . VAL A 1 7   ? 19.610  16.046  16.381  1.00 44.43  ? 7   VAL A C   1 
ATOM   25   O O   . VAL A 1 7   ? 19.698  15.707  17.562  1.00 39.69  ? 7   VAL A O   1 
ATOM   26   C CB  . VAL A 1 7   ? 20.441  18.418  16.239  1.00 50.52  ? 7   VAL A CB  1 
ATOM   27   C CG1 . VAL A 1 7   ? 21.703  17.843  15.604  1.00 51.70  ? 7   VAL A CG1 1 
ATOM   28   C CG2 . VAL A 1 7   ? 20.150  19.783  15.642  1.00 54.04  ? 7   VAL A CG2 1 
ATOM   29   N N   . VAL A 1 8   ? 19.824  15.204  15.372  1.00 47.52  ? 8   VAL A N   1 
ATOM   30   C CA  . VAL A 1 8   ? 20.230  13.818  15.591  1.00 44.05  ? 8   VAL A CA  1 
ATOM   31   C C   . VAL A 1 8   ? 21.703  13.698  15.239  1.00 47.85  ? 8   VAL A C   1 
ATOM   32   O O   . VAL A 1 8   ? 22.125  14.133  14.163  1.00 46.53  ? 8   VAL A O   1 
ATOM   33   C CB  . VAL A 1 8   ? 19.394  12.826  14.762  1.00 43.87  ? 8   VAL A CB  1 
ATOM   34   C CG1 . VAL A 1 8   ? 19.933  11.416  14.961  1.00 43.76  ? 8   VAL A CG1 1 
ATOM   35   C CG2 . VAL A 1 8   ? 17.919  12.874  15.171  1.00 40.23  ? 8   VAL A CG2 1 
ATOM   36   N N   . ARG A 1 9   ? 22.486  13.121  16.143  1.00 39.14  ? 9   ARG A N   1 
ATOM   37   C CA  . ARG A 1 9   ? 23.881  12.807  15.872  1.00 40.78  ? 9   ARG A CA  1 
ATOM   38   C C   . ARG A 1 9   ? 24.095  11.316  16.097  1.00 49.93  ? 9   ARG A C   1 
ATOM   39   O O   . ARG A 1 9   ? 23.532  10.735  17.026  1.00 43.42  ? 9   ARG A O   1 
ATOM   40   C CB  . ARG A 1 9   ? 24.813  13.656  16.754  1.00 48.97  ? 9   ARG A CB  1 
ATOM   41   C CG  . ARG A 1 9   ? 24.779  13.354  18.234  1.00 42.84  ? 9   ARG A CG  1 
ATOM   42   C CD  . ARG A 1 9   ? 25.705  14.310  19.003  1.00 54.39  ? 9   ARG A CD  1 
ATOM   43   N NE  . ARG A 1 9   ? 25.790  14.012  20.433  1.00 50.51  ? 9   ARG A NE  1 
ATOM   44   C CZ  . ARG A 1 9   ? 24.957  14.477  21.359  1.00 54.46  ? 9   ARG A CZ  1 
ATOM   45   N NH1 . ARG A 1 9   ? 23.919  15.238  21.040  1.00 46.58  ? 9   ARG A NH1 1 
ATOM   46   N NH2 . ARG A 1 9   ? 25.169  14.174  22.638  1.00 50.71  ? 9   ARG A NH2 1 
ATOM   47   N N   . VAL A 1 10  ? 24.902  10.691  15.245  1.00 44.99  ? 10  VAL A N   1 
ATOM   48   C CA  . VAL A 1 10  ? 25.081  9.242   15.264  1.00 46.96  ? 10  VAL A CA  1 
ATOM   49   C C   . VAL A 1 10  ? 26.454  8.944   15.846  1.00 58.27  ? 10  VAL A C   1 
ATOM   50   O O   . VAL A 1 10  ? 27.476  9.393   15.314  1.00 56.09  ? 10  VAL A O   1 
ATOM   51   C CB  . VAL A 1 10  ? 24.924  8.627   13.866  1.00 56.06  ? 10  VAL A CB  1 
ATOM   52   C CG1 . VAL A 1 10  ? 25.106  7.110   13.931  1.00 52.95  ? 10  VAL A CG1 1 
ATOM   53   C CG2 . VAL A 1 10  ? 23.563  8.976   13.288  1.00 48.53  ? 10  VAL A CG2 1 
ATOM   54   N N   . GLU A 1 11  ? 26.471  8.194   16.945  1.00 56.63  ? 11  GLU A N   1 
ATOM   55   C CA  . GLU A 1 11  ? 27.690  7.833   17.671  1.00 57.35  ? 11  GLU A CA  1 
ATOM   56   C C   . GLU A 1 11  ? 27.704  6.311   17.807  1.00 60.13  ? 11  GLU A C   1 
ATOM   57   O O   . GLU A 1 11  ? 27.123  5.754   18.744  1.00 64.96  ? 11  GLU A O   1 
ATOM   58   C CB  . GLU A 1 11  ? 27.716  8.544   19.019  1.00 60.70  ? 11  GLU A CB  1 
ATOM   59   C CG  . GLU A 1 11  ? 27.438  10.038  18.886  1.00 65.39  ? 11  GLU A CG  1 
ATOM   60   C CD  . GLU A 1 11  ? 27.961  10.864  20.051  1.00 84.01  ? 11  GLU A CD  1 
ATOM   61   O OE1 . GLU A 1 11  ? 27.942  10.363  21.202  1.00 77.02  ? 11  GLU A OE1 1 
ATOM   62   O OE2 . GLU A 1 11  ? 28.389  12.018  19.807  1.00 75.04  ? 11  GLU A OE2 1 
ATOM   63   N N   . GLY A 1 12  ? 28.390  5.646   16.882  1.00 61.90  ? 12  GLY A N   1 
ATOM   64   C CA  . GLY A 1 12  ? 28.395  4.187   16.865  1.00 58.31  ? 12  GLY A CA  1 
ATOM   65   C C   . GLY A 1 12  ? 27.080  3.650   16.345  1.00 56.81  ? 12  GLY A C   1 
ATOM   66   O O   . GLY A 1 12  ? 26.564  4.121   15.327  1.00 57.80  ? 12  GLY A O   1 
ATOM   67   N N   . ASP A 1 13  ? 26.522  2.655   17.034  1.00 52.50  ? 13  ASP A N   1 
ATOM   68   C CA  . ASP A 1 13  ? 25.226  2.116   16.645  1.00 54.23  ? 13  ASP A CA  1 
ATOM   69   C C   . ASP A 1 13  ? 24.095  2.805   17.380  1.00 50.28  ? 13  ASP A C   1 
ATOM   70   O O   . ASP A 1 13  ? 22.999  2.240   17.496  1.00 41.28  ? 13  ASP A O   1 
ATOM   71   C CB  . ASP A 1 13  ? 25.150  0.608   16.885  1.00 52.20  ? 13  ASP A CB  1 
ATOM   72   C CG  . ASP A 1 13  ? 25.497  0.218   18.313  1.00 57.98  ? 13  ASP A CG  1 
ATOM   73   O OD1 . ASP A 1 13  ? 25.514  1.097   19.205  1.00 59.17  ? 13  ASP A OD1 1 
ATOM   74   O OD2 . ASP A 1 13  ? 25.740  -0.987  18.544  1.00 66.85  ? 13  ASP A OD2 1 
ATOM   75   N N   . ARG A 1 14  ? 24.352  3.998   17.907  1.00 42.59  ? 14  ARG A N   1 
ATOM   76   C CA  . ARG A 1 14  ? 23.359  4.773   18.623  1.00 43.82  ? 14  ARG A CA  1 
ATOM   77   C C   . ARG A 1 14  ? 23.132  6.108   17.936  1.00 46.10  ? 14  ARG A C   1 
ATOM   78   O O   . ARG A 1 14  ? 24.075  6.748   17.453  1.00 46.61  ? 14  ARG A O   1 
ATOM   79   C CB  . ARG A 1 14  ? 23.783  4.968   20.078  1.00 45.86  ? 14  ARG A CB  1 
ATOM   80   C CG  . ARG A 1 14  ? 23.356  3.767   20.888  1.00 56.58  ? 14  ARG A CG  1 
ATOM   81   C CD  . ARG A 1 14  ? 24.253  3.436   22.035  1.00 55.18  ? 14  ARG A CD  1 
ATOM   82   N NE  . ARG A 1 14  ? 24.048  2.048   22.439  1.00 60.97  ? 14  ARG A NE  1 
ATOM   83   C CZ  . ARG A 1 14  ? 23.705  1.683   23.667  1.00 61.20  ? 14  ARG A CZ  1 
ATOM   84   N NH1 . ARG A 1 14  ? 23.522  2.582   24.626  1.00 44.45  ? 14  ARG A NH1 1 
ATOM   85   N NH2 . ARG A 1 14  ? 23.543  0.386   23.938  1.00 52.85  ? 14  ARG A NH2 1 
ATOM   86   N N   . ALA A 1 15  ? 21.867  6.502   17.877  1.00 38.90  ? 15  ALA A N   1 
ATOM   87   C CA  . ALA A 1 15  ? 21.465  7.831   17.457  1.00 41.48  ? 15  ALA A CA  1 
ATOM   88   C C   . ALA A 1 15  ? 21.039  8.605   18.698  1.00 41.60  ? 15  ALA A C   1 
ATOM   89   O O   . ALA A 1 15  ? 20.261  8.096   19.514  1.00 36.37  ? 15  ALA A O   1 
ATOM   90   C CB  . ALA A 1 15  ? 20.324  7.763   16.436  1.00 40.00  ? 15  ALA A CB  1 
ATOM   91   N N   . ILE A 1 16  ? 21.575  9.811   18.857  1.00 34.68  ? 16  ILE A N   1 
ATOM   92   C CA  . ILE A 1 16  ? 21.232  10.675  19.982  1.00 32.47  ? 16  ILE A CA  1 
ATOM   93   C C   . ILE A 1 16  ? 20.450  11.849  19.424  1.00 33.46  ? 16  ILE A C   1 
ATOM   94   O O   . ILE A 1 16  ? 20.983  12.648  18.644  1.00 36.98  ? 16  ILE A O   1 
ATOM   95   C CB  . ILE A 1 16  ? 22.477  11.157  20.739  1.00 45.16  ? 16  ILE A CB  1 
ATOM   96   C CG1 . ILE A 1 16  ? 23.315  9.964   21.192  1.00 45.12  ? 16  ILE A CG1 1 
ATOM   97   C CG2 . ILE A 1 16  ? 22.074  12.057  21.941  1.00 37.94  ? 16  ILE A CG2 1 
ATOM   98   C CD1 . ILE A 1 16  ? 24.220  10.272  22.383  1.00 49.75  ? 16  ILE A CD1 1 
ATOM   99   N N   . LYS A 1 17  ? 19.197  11.960  19.821  1.00 31.59  ? 17  LYS A N   1 
ATOM   100  C CA  . LYS A 1 17  ? 18.338  13.042  19.352  1.00 34.15  ? 17  LYS A CA  1 
ATOM   101  C C   . LYS A 1 17  ? 18.250  14.076  20.471  1.00 30.16  ? 17  LYS A C   1 
ATOM   102  O O   . LYS A 1 17  ? 17.765  13.771  21.562  1.00 29.88  ? 17  LYS A O   1 
ATOM   103  C CB  . LYS A 1 17  ? 16.952  12.499  19.006  1.00 33.23  ? 17  LYS A CB  1 
ATOM   104  C CG  . LYS A 1 17  ? 15.999  13.528  18.441  1.00 33.18  ? 17  LYS A CG  1 
ATOM   105  C CD  . LYS A 1 17  ? 14.740  12.838  17.934  1.00 38.85  ? 17  LYS A CD  1 
ATOM   106  C CE  . LYS A 1 17  ? 14.079  13.661  16.847  1.00 47.84  ? 17  LYS A CE  1 
ATOM   107  N NZ  . LYS A 1 17  ? 12.761  13.077  16.487  1.00 43.98  ? 17  LYS A NZ  1 
ATOM   108  N N   . GLN A 1 18  ? 18.727  15.289  20.215  1.00 29.87  ? 18  GLN A N   1 
ATOM   109  C CA  . GLN A 1 18  ? 18.664  16.334  21.229  1.00 27.97  ? 18  GLN A CA  1 
ATOM   110  C C   . GLN A 1 18  ? 17.680  17.391  20.767  1.00 26.56  ? 18  GLN A C   1 
ATOM   111  O O   . GLN A 1 18  ? 17.812  17.927  19.666  1.00 31.39  ? 18  GLN A O   1 
ATOM   112  C CB  . GLN A 1 18  ? 20.033  16.964  21.481  1.00 30.46  ? 18  GLN A CB  1 
ATOM   113  C CG  . GLN A 1 18  ? 20.005  17.946  22.701  1.00 39.47  ? 18  GLN A CG  1 
ATOM   114  C CD  . GLN A 1 18  ? 21.362  18.525  23.036  1.00 42.20  ? 18  GLN A CD  1 
ATOM   115  O OE1 . GLN A 1 18  ? 22.241  18.599  22.181  1.00 45.95  ? 18  GLN A OE1 1 
ATOM   116  N NE2 . GLN A 1 18  ? 21.564  18.890  24.313  1.00 37.79  ? 18  GLN A NE2 1 
ATOM   117  N N   . PHE A 1 19  ? 16.697  17.684  21.598  1.00 26.58  ? 19  PHE A N   1 
ATOM   118  C CA  . PHE A 1 19  ? 15.738  18.719  21.262  1.00 32.07  ? 19  PHE A CA  1 
ATOM   119  C C   . PHE A 1 19  ? 16.289  20.049  21.732  1.00 38.81  ? 19  PHE A C   1 
ATOM   120  O O   . PHE A 1 19  ? 17.033  20.113  22.706  1.00 32.98  ? 19  PHE A O   1 
ATOM   121  C CB  . PHE A 1 19  ? 14.392  18.438  21.913  1.00 29.80  ? 19  PHE A CB  1 
ATOM   122  C CG  . PHE A 1 19  ? 13.713  17.237  21.350  1.00 30.93  ? 19  PHE A CG  1 
ATOM   123  C CD1 . PHE A 1 19  ? 14.152  15.955  21.669  1.00 27.45  ? 19  PHE A CD1 1 
ATOM   124  C CD2 . PHE A 1 19  ? 12.661  17.389  20.456  1.00 33.76  ? 19  PHE A CD2 1 
ATOM   125  C CE1 . PHE A 1 19  ? 13.521  14.823  21.117  1.00 29.56  ? 19  PHE A CE1 1 
ATOM   126  C CE2 . PHE A 1 19  ? 12.031  16.284  19.904  1.00 33.86  ? 19  PHE A CE2 1 
ATOM   127  C CZ  . PHE A 1 19  ? 12.456  15.005  20.233  1.00 32.75  ? 19  PHE A CZ  1 
ATOM   128  N N   . PHE A 1 20  ? 15.930  21.115  21.027  1.00 35.53  ? 20  PHE A N   1 
ATOM   129  C CA  . PHE A 1 20  ? 16.296  22.444  21.494  1.00 35.74  ? 20  PHE A CA  1 
ATOM   130  C C   . PHE A 1 20  ? 15.494  22.787  22.738  1.00 33.12  ? 20  PHE A C   1 
ATOM   131  O O   . PHE A 1 20  ? 14.448  22.184  22.991  1.00 30.96  ? 20  PHE A O   1 
ATOM   132  C CB  . PHE A 1 20  ? 16.109  23.453  20.371  1.00 38.21  ? 20  PHE A CB  1 
ATOM   133  C CG  . PHE A 1 20  ? 16.970  23.155  19.193  1.00 49.17  ? 20  PHE A CG  1 
ATOM   134  C CD1 . PHE A 1 20  ? 18.347  23.263  19.295  1.00 53.37  ? 20  PHE A CD1 1 
ATOM   135  C CD2 . PHE A 1 20  ? 16.418  22.718  18.002  1.00 48.95  ? 20  PHE A CD2 1 
ATOM   136  C CE1 . PHE A 1 20  ? 19.157  22.978  18.221  1.00 61.06  ? 20  PHE A CE1 1 
ATOM   137  C CE2 . PHE A 1 20  ? 17.222  22.430  16.920  1.00 52.74  ? 20  PHE A CE2 1 
ATOM   138  C CZ  . PHE A 1 20  ? 18.595  22.559  17.028  1.00 56.22  ? 20  PHE A CZ  1 
ATOM   139  N N   . PRO A 1 21  ? 16.013  23.699  23.580  1.00 32.41  ? 21  PRO A N   1 
ATOM   140  C CA  . PRO A 1 21  ? 15.376  23.947  24.885  1.00 32.54  ? 21  PRO A CA  1 
ATOM   141  C C   . PRO A 1 21  ? 13.916  24.355  24.810  1.00 34.97  ? 21  PRO A C   1 
ATOM   142  O O   . PRO A 1 21  ? 13.156  24.065  25.744  1.00 33.27  ? 21  PRO A O   1 
ATOM   143  C CB  . PRO A 1 21  ? 16.200  25.110  25.477  1.00 34.04  ? 21  PRO A CB  1 
ATOM   144  C CG  . PRO A 1 21  ? 17.533  25.059  24.802  1.00 38.88  ? 21  PRO A CG  1 
ATOM   145  C CD  . PRO A 1 21  ? 17.235  24.504  23.386  1.00 38.58  ? 21  PRO A CD  1 
ATOM   146  N N   . ALA A 1 22  ? 13.508  25.060  23.752  1.00 33.88  ? 22  ALA A N   1 
ATOM   147  C CA  . ALA A 1 22  ? 12.108  25.450  23.621  1.00 36.64  ? 22  ALA A CA  1 
ATOM   148  C C   . ALA A 1 22  ? 11.166  24.260  23.412  1.00 37.88  ? 22  ALA A C   1 
ATOM   149  O O   . ALA A 1 22  ? 9.947   24.428  23.526  1.00 34.45  ? 22  ALA A O   1 
ATOM   150  C CB  . ALA A 1 22  ? 11.957  26.476  22.496  1.00 38.60  ? 22  ALA A CB  1 
ATOM   151  N N   . TYR A 1 23  ? 11.686  23.070  23.109  1.00 30.85  ? 23  TYR A N   1 
ATOM   152  C CA  . TYR A 1 23  ? 10.854  21.948  22.677  1.00 32.86  ? 23  TYR A CA  1 
ATOM   153  C C   . TYR A 1 23  ? 10.820  20.805  23.681  1.00 34.06  ? 23  TYR A C   1 
ATOM   154  O O   . TYR A 1 23  ? 10.747  19.630  23.298  1.00 30.58  ? 23  TYR A O   1 
ATOM   155  C CB  . TYR A 1 23  ? 11.330  21.468  21.312  1.00 31.48  ? 23  TYR A CB  1 
ATOM   156  C CG  . TYR A 1 23  ? 11.235  22.611  20.349  1.00 34.06  ? 23  TYR A CG  1 
ATOM   157  C CD1 . TYR A 1 23  ? 10.006  23.166  20.028  1.00 40.66  ? 23  TYR A CD1 1 
ATOM   158  C CD2 . TYR A 1 23  ? 12.382  23.197  19.822  1.00 39.73  ? 23  TYR A CD2 1 
ATOM   159  C CE1 . TYR A 1 23  ? 9.917   24.251  19.176  1.00 46.83  ? 23  TYR A CE1 1 
ATOM   160  C CE2 . TYR A 1 23  ? 12.309  24.278  18.966  1.00 42.89  ? 23  TYR A CE2 1 
ATOM   161  C CZ  . TYR A 1 23  ? 11.071  24.799  18.648  1.00 48.43  ? 23  TYR A CZ  1 
ATOM   162  O OH  . TYR A 1 23  ? 10.983  25.864  17.801  1.00 53.01  ? 23  TYR A OH  1 
ATOM   163  N N   . ARG A 1 24  ? 10.880  21.125  24.977  1.00 29.62  ? 24  ARG A N   1 
ATOM   164  C CA  . ARG A 1 24  ? 10.732  20.072  25.983  1.00 31.57  ? 24  ARG A CA  1 
ATOM   165  C C   . ARG A 1 24  ? 9.446   19.274  25.754  1.00 30.09  ? 24  ARG A C   1 
ATOM   166  O O   . ARG A 1 24  ? 9.405   18.069  26.000  1.00 30.90  ? 24  ARG A O   1 
ATOM   167  C CB  . ARG A 1 24  ? 10.756  20.689  27.387  1.00 32.12  ? 24  ARG A CB  1 
ATOM   168  C CG  . ARG A 1 24  ? 9.999   19.885  28.439  1.00 40.67  ? 24  ARG A CG  1 
ATOM   169  N N   . TYR A 1 25  ? 8.382   19.933  25.271  1.00 32.83  ? 25  TYR A N   1 
ATOM   170  C CA  . TYR A 1 25  ? 7.117   19.227  25.063  1.00 33.38  ? 25  TYR A CA  1 
ATOM   171  C C   . TYR A 1 25  ? 7.297   18.069  24.075  1.00 35.00  ? 25  TYR A C   1 
ATOM   172  O O   . TYR A 1 25  ? 6.839   16.944  24.323  1.00 31.59  ? 25  TYR A O   1 
ATOM   173  C CB  . TYR A 1 25  ? 6.053   20.241  24.595  1.00 40.75  ? 25  TYR A CB  1 
ATOM   174  C CG  . TYR A 1 25  ? 4.698   19.650  24.251  1.00 46.73  ? 25  TYR A CG  1 
ATOM   175  C CD1 . TYR A 1 25  ? 3.727   19.447  25.234  1.00 51.25  ? 25  TYR A CD1 1 
ATOM   176  C CD2 . TYR A 1 25  ? 4.387   19.303  22.941  1.00 47.68  ? 25  TYR A CD2 1 
ATOM   177  C CE1 . TYR A 1 25  ? 2.484   18.895  24.916  1.00 49.62  ? 25  TYR A CE1 1 
ATOM   178  C CE2 . TYR A 1 25  ? 3.148   18.761  22.615  1.00 54.68  ? 25  TYR A CE2 1 
ATOM   179  C CZ  . TYR A 1 25  ? 2.205   18.557  23.605  1.00 55.22  ? 25  TYR A CZ  1 
ATOM   180  O OH  . TYR A 1 25  ? 0.984   18.007  23.271  1.00 57.38  ? 25  TYR A OH  1 
ATOM   181  N N   . ASN A 1 26  ? 8.005   18.315  22.968  1.00 28.31  ? 26  ASN A N   1 
ATOM   182  C CA  . ASN A 1 26  ? 8.190   17.289  21.950  1.00 30.31  ? 26  ASN A CA  1 
ATOM   183  C C   . ASN A 1 26  ? 9.165   16.221  22.413  1.00 32.18  ? 26  ASN A C   1 
ATOM   184  O O   . ASN A 1 26  ? 9.019   15.047  22.052  1.00 28.31  ? 26  ASN A O   1 
ATOM   185  C CB  . ASN A 1 26  ? 8.668   17.940  20.653  1.00 29.40  ? 26  ASN A CB  1 
ATOM   186  C CG  . ASN A 1 26  ? 7.656   18.925  20.101  1.00 41.33  ? 26  ASN A CG  1 
ATOM   187  O OD1 . ASN A 1 26  ? 7.746   20.131  20.348  1.00 41.86  ? 26  ASN A OD1 1 
ATOM   188  N ND2 . ASN A 1 26  ? 6.654   18.412  19.393  1.00 38.16  ? 26  ASN A ND2 1 
ATOM   189  N N   . PHE A 1 27  ? 10.153  16.609  23.223  1.00 26.44  ? 27  PHE A N   1 
ATOM   190  C CA  . PHE A 1 27  ? 11.057  15.634  23.826  1.00 25.44  ? 27  PHE A CA  1 
ATOM   191  C C   . PHE A 1 27  ? 10.282  14.535  24.561  1.00 24.90  ? 27  PHE A C   1 
ATOM   192  O O   . PHE A 1 27  ? 10.557  13.337  24.391  1.00 26.23  ? 27  PHE A O   1 
ATOM   193  C CB  . PHE A 1 27  ? 12.017  16.365  24.776  1.00 28.38  ? 27  PHE A CB  1 
ATOM   194  C CG  . PHE A 1 27  ? 12.732  15.440  25.746  1.00 27.93  ? 27  PHE A CG  1 
ATOM   195  C CD1 . PHE A 1 27  ? 13.895  14.768  25.363  1.00 25.48  ? 27  PHE A CD1 1 
ATOM   196  C CD2 . PHE A 1 27  ? 12.237  15.246  27.038  1.00 25.46  ? 27  PHE A CD2 1 
ATOM   197  C CE1 . PHE A 1 27  ? 14.574  13.909  26.266  1.00 24.00  ? 27  PHE A CE1 1 
ATOM   198  C CE2 . PHE A 1 27  ? 12.888  14.389  27.948  1.00 28.40  ? 27  PHE A CE2 1 
ATOM   199  C CZ  . PHE A 1 27  ? 14.062  13.720  27.558  1.00 24.93  ? 27  PHE A CZ  1 
ATOM   200  N N   . TRP A 1 28  ? 9.281   14.922  25.363  1.00 24.43  ? 28  TRP A N   1 
ATOM   201  C CA  . TRP A 1 28  ? 8.555   13.925  26.157  1.00 24.08  ? 28  TRP A CA  1 
ATOM   202  C C   . TRP A 1 28  ? 7.622   13.079  25.306  1.00 27.37  ? 28  TRP A C   1 
ATOM   203  O O   . TRP A 1 28  ? 7.383   11.902  25.616  1.00 26.77  ? 28  TRP A O   1 
ATOM   204  C CB  . TRP A 1 28  ? 7.759   14.627  27.262  1.00 22.19  ? 28  TRP A CB  1 
ATOM   205  C CG  . TRP A 1 28  ? 8.628   15.072  28.406  1.00 24.68  ? 28  TRP A CG  1 
ATOM   206  C CD1 . TRP A 1 28  ? 8.834   16.344  28.846  1.00 29.01  ? 28  TRP A CD1 1 
ATOM   207  C CD2 . TRP A 1 28  ? 9.389   14.217  29.256  1.00 23.99  ? 28  TRP A CD2 1 
ATOM   208  N NE1 . TRP A 1 28  ? 9.704   16.331  29.933  1.00 25.66  ? 28  TRP A NE1 1 
ATOM   209  C CE2 . TRP A 1 28  ? 10.052  15.032  30.192  1.00 24.28  ? 28  TRP A CE2 1 
ATOM   210  C CE3 . TRP A 1 28  ? 9.579   12.830  29.309  1.00 22.57  ? 28  TRP A CE3 1 
ATOM   211  C CZ2 . TRP A 1 28  ? 10.879  14.507  31.182  1.00 29.19  ? 28  TRP A CZ2 1 
ATOM   212  C CZ3 . TRP A 1 28  ? 10.410  12.302  30.280  1.00 25.21  ? 28  TRP A CZ3 1 
ATOM   213  C CH2 . TRP A 1 28  ? 11.049  13.151  31.210  1.00 27.72  ? 28  TRP A CH2 1 
ATOM   214  N N   . LYS A 1 29  ? 7.056   13.654  24.252  1.00 26.11  ? 29  LYS A N   1 
ATOM   215  C CA  . LYS A 1 29  ? 6.218   12.860  23.356  1.00 27.80  ? 29  LYS A CA  1 
ATOM   216  C C   . LYS A 1 29  ? 7.050   11.828  22.618  1.00 26.62  ? 29  LYS A C   1 
ATOM   217  O O   . LYS A 1 29  ? 6.624   10.681  22.464  1.00 29.27  ? 29  LYS A O   1 
ATOM   218  C CB  . LYS A 1 29  ? 5.475   13.774  22.368  1.00 30.05  ? 29  LYS A CB  1 
ATOM   219  C CG  . LYS A 1 29  ? 4.424   14.739  23.011  1.00 36.69  ? 29  LYS A CG  1 
ATOM   220  C CD  . LYS A 1 29  ? 3.732   14.245  24.325  1.00 36.15  ? 29  LYS A CD  1 
ATOM   221  C CE  . LYS A 1 29  ? 2.695   15.261  24.824  1.00 44.59  ? 29  LYS A CE  1 
ATOM   222  N NZ  . LYS A 1 29  ? 2.072   14.888  26.146  1.00 41.60  ? 29  LYS A NZ  1 
ATOM   223  N N   . GLU A 1 30  ? 8.241   12.211  22.146  1.00 26.30  ? 30  GLU A N   1 
ATOM   224  C CA  . GLU A 1 30  ? 9.123   11.231  21.519  1.00 29.20  ? 30  GLU A CA  1 
ATOM   225  C C   . GLU A 1 30  ? 9.476   10.117  22.489  1.00 30.16  ? 30  GLU A C   1 
ATOM   226  O O   . GLU A 1 30  ? 9.383   8.928   22.153  1.00 27.48  ? 30  GLU A O   1 
ATOM   227  C CB  . GLU A 1 30  ? 10.398  11.888  20.993  1.00 27.25  ? 30  GLU A CB  1 
ATOM   228  C CG  . GLU A 1 30  ? 11.321  10.844  20.355  1.00 33.61  ? 30  GLU A CG  1 
ATOM   229  C CD  . GLU A 1 30  ? 11.241  10.856  18.825  1.00 42.84  ? 30  GLU A CD  1 
ATOM   230  O OE1 . GLU A 1 30  ? 11.054  11.936  18.233  1.00 46.72  ? 30  GLU A OE1 1 
ATOM   231  O OE2 . GLU A 1 30  ? 11.358  9.772   18.220  1.00 47.96  ? 30  GLU A OE2 1 
ATOM   232  N N   . ALA A 1 31  ? 9.878   10.483  23.700  1.00 24.93  ? 31  ALA A N   1 
ATOM   233  C CA  . ALA A 1 31  ? 10.231  9.464   24.686  1.00 25.76  ? 31  ALA A CA  1 
ATOM   234  C C   . ALA A 1 31  ? 9.027   8.590   25.027  1.00 23.85  ? 31  ALA A C   1 
ATOM   235  O O   . ALA A 1 31  ? 9.159   7.362   25.156  1.00 26.47  ? 31  ALA A O   1 
ATOM   236  C CB  . ALA A 1 31  ? 10.774  10.147  25.953  1.00 23.40  ? 31  ALA A CB  1 
ATOM   237  N N   . GLY A 1 32  ? 7.851   9.217   25.212  1.00 23.66  ? 32  GLY A N   1 
ATOM   238  C CA  . GLY A 1 32  ? 6.675   8.467   25.624  1.00 24.90  ? 32  GLY A CA  1 
ATOM   239  C C   . GLY A 1 32  ? 6.229   7.464   24.575  1.00 28.53  ? 32  GLY A C   1 
ATOM   240  O O   . GLY A 1 32  ? 5.989   6.286   24.874  1.00 22.51  ? 32  GLY A O   1 
ATOM   241  N N   . PHE A 1 33  ? 6.104   7.918   23.331  1.00 23.51  ? 33  PHE A N   1 
ATOM   242  C CA  . PHE A 1 33  ? 5.597   7.013   22.304  1.00 24.64  ? 33  PHE A CA  1 
ATOM   243  C C   . PHE A 1 33  ? 6.618   5.953   21.940  1.00 22.93  ? 33  PHE A C   1 
ATOM   244  O O   . PHE A 1 33  ? 6.243   4.804   21.698  1.00 23.43  ? 33  PHE A O   1 
ATOM   245  C CB  . PHE A 1 33  ? 5.142   7.800   21.071  1.00 22.74  ? 33  PHE A CB  1 
ATOM   246  C CG  . PHE A 1 33  ? 3.868   8.570   21.316  1.00 28.07  ? 33  PHE A CG  1 
ATOM   247  C CD1 . PHE A 1 33  ? 2.706   7.900   21.694  1.00 26.49  ? 33  PHE A CD1 1 
ATOM   248  C CD2 . PHE A 1 33  ? 3.848   9.955   21.246  1.00 28.09  ? 33  PHE A CD2 1 
ATOM   249  C CE1 . PHE A 1 33  ? 1.537   8.603   21.986  1.00 31.99  ? 33  PHE A CE1 1 
ATOM   250  C CE2 . PHE A 1 33  ? 2.680   10.663  21.518  1.00 35.82  ? 33  PHE A CE2 1 
ATOM   251  C CZ  . PHE A 1 33  ? 1.517   9.986   21.872  1.00 31.05  ? 33  PHE A CZ  1 
ATOM   252  N N   . LEU A 1 34  ? 7.912   6.292   21.907  1.00 20.21  ? 34  LEU A N   1 
ATOM   253  C CA  . LEU A 1 34  ? 8.896   5.235   21.683  1.00 24.77  ? 34  LEU A CA  1 
ATOM   254  C C   . LEU A 1 34  ? 8.816   4.173   22.781  1.00 25.10  ? 34  LEU A C   1 
ATOM   255  O O   . LEU A 1 34  ? 8.871   2.970   22.482  1.00 23.36  ? 34  LEU A O   1 
ATOM   256  C CB  . LEU A 1 34  ? 10.308  5.817   21.610  1.00 23.24  ? 34  LEU A CB  1 
ATOM   257  C CG  . LEU A 1 34  ? 10.715  6.464   20.283  1.00 28.77  ? 34  LEU A CG  1 
ATOM   258  C CD1 . LEU A 1 34  ? 12.096  7.093   20.487  1.00 29.70  ? 34  LEU A CD1 1 
ATOM   259  C CD2 . LEU A 1 34  ? 10.720  5.435   19.127  1.00 25.77  ? 34  LEU A CD2 1 
ATOM   260  N N   . SER A 1 35  ? 8.663   4.605   24.053  1.00 21.25  ? 35  SER A N   1 
ATOM   261  C CA  . SER A 1 35  ? 8.546   3.661   25.175  1.00 22.42  ? 35  SER A CA  1 
ATOM   262  C C   . SER A 1 35  ? 7.347   2.748   24.985  1.00 27.31  ? 35  SER A C   1 
ATOM   263  O O   . SER A 1 35  ? 7.439   1.534   25.182  1.00 22.83  ? 35  SER A O   1 
ATOM   264  C CB  . SER A 1 35  ? 8.391   4.395   26.518  1.00 19.06  ? 35  SER A CB  1 
ATOM   265  O OG  . SER A 1 35  ? 9.556   5.114   26.872  1.00 23.21  ? 35  SER A OG  1 
ATOM   266  N N   . LEU A 1 36  ? 6.190   3.335   24.646  1.00 21.93  ? 36  LEU A N   1 
ATOM   267  C CA  . LEU A 1 36  ? 4.975   2.550   24.481  1.00 22.89  ? 36  LEU A CA  1 
ATOM   268  C C   . LEU A 1 36  ? 5.036   1.627   23.265  1.00 29.45  ? 36  LEU A C   1 
ATOM   269  O O   . LEU A 1 36  ? 4.233   0.694   23.177  1.00 26.02  ? 36  LEU A O   1 
ATOM   270  C CB  . LEU A 1 36  ? 3.783   3.490   24.325  1.00 26.82  ? 36  LEU A CB  1 
ATOM   271  C CG  . LEU A 1 36  ? 3.413   4.313   25.572  1.00 28.71  ? 36  LEU A CG  1 
ATOM   272  C CD1 . LEU A 1 36  ? 2.141   5.084   25.251  1.00 26.99  ? 36  LEU A CD1 1 
ATOM   273  C CD2 . LEU A 1 36  ? 3.241   3.437   26.815  1.00 25.26  ? 36  LEU A CD2 1 
ATOM   274  N N   . LEU A 1 37  ? 5.957   1.859   22.320  1.00 26.05  ? 37  LEU A N   1 
ATOM   275  C CA  . LEU A 1 37  ? 6.069   0.987   21.140  1.00 25.84  ? 37  LEU A CA  1 
ATOM   276  C C   . LEU A 1 37  ? 7.240   0.004   21.209  1.00 26.83  ? 37  LEU A C   1 
ATOM   277  O O   . LEU A 1 37  ? 7.501   -0.711  20.230  1.00 27.88  ? 37  LEU A O   1 
ATOM   278  C CB  . LEU A 1 37  ? 6.185   1.848   19.878  1.00 21.13  ? 37  LEU A CB  1 
ATOM   279  C CG  . LEU A 1 37  ? 4.901   2.672   19.638  1.00 25.23  ? 37  LEU A CG  1 
ATOM   280  C CD1 . LEU A 1 37  ? 5.110   3.728   18.533  1.00 28.61  ? 37  LEU A CD1 1 
ATOM   281  C CD2 . LEU A 1 37  ? 3.725   1.729   19.219  1.00 31.61  ? 37  LEU A CD2 1 
ATOM   282  N N   . GLN A 1 38  ? 7.966   -0.049  22.327  1.00 24.89  ? 38  GLN A N   1 
ATOM   283  C CA  . GLN A 1 38  ? 9.105   -0.956  22.410  1.00 23.98  ? 38  GLN A CA  1 
ATOM   284  C C   . GLN A 1 38  ? 8.709   -2.426  22.285  1.00 31.61  ? 38  GLN A C   1 
ATOM   285  O O   . GLN A 1 38  ? 9.555   -3.251  21.934  1.00 30.19  ? 38  GLN A O   1 
ATOM   286  C CB  . GLN A 1 38  ? 9.863   -0.745  23.725  1.00 23.81  ? 38  GLN A CB  1 
ATOM   287  C CG  . GLN A 1 38  ? 10.588  0.604   23.816  1.00 25.81  ? 38  GLN A CG  1 
ATOM   288  C CD  . GLN A 1 38  ? 11.640  0.742   22.725  1.00 26.93  ? 38  GLN A CD  1 
ATOM   289  O OE1 . GLN A 1 38  ? 12.698  0.089   22.781  1.00 27.39  ? 38  GLN A OE1 1 
ATOM   290  N NE2 . GLN A 1 38  ? 11.374  1.616   21.740  1.00 22.94  ? 38  GLN A NE2 1 
ATOM   291  N N   . GLU A 1 39  ? 7.465   -2.800  22.587  1.00 32.05  ? 39  GLU A N   1 
ATOM   292  C CA  . GLU A 1 39  ? 7.154   -4.218  22.372  1.00 38.09  ? 39  GLU A CA  1 
ATOM   293  C C   . GLU A 1 39  ? 7.102   -4.587  20.898  1.00 40.41  ? 39  GLU A C   1 
ATOM   294  O O   . GLU A 1 39  ? 6.998   -5.773  20.583  1.00 42.74  ? 39  GLU A O   1 
ATOM   295  C CB  . GLU A 1 39  ? 5.826   -4.602  23.025  1.00 46.27  ? 39  GLU A CB  1 
ATOM   296  C CG  . GLU A 1 39  ? 4.606   -4.079  22.281  1.00 48.00  ? 39  GLU A CG  1 
ATOM   297  C CD  . GLU A 1 39  ? 3.293   -4.428  22.957  1.00 51.31  ? 39  GLU A CD  1 
ATOM   298  O OE1 . GLU A 1 39  ? 2.933   -5.628  22.986  1.00 55.72  ? 39  GLU A OE1 1 
ATOM   299  O OE2 . GLU A 1 39  ? 2.633   -3.494  23.468  1.00 47.65  ? 39  GLU A OE2 1 
ATOM   300  N N   . PHE A 1 40  ? 7.194   -3.628  19.982  1.00 36.05  ? 40  PHE A N   1 
ATOM   301  C CA  . PHE A 1 40  ? 7.139   -3.935  18.557  1.00 34.50  ? 40  PHE A CA  1 
ATOM   302  C C   . PHE A 1 40  ? 8.481   -3.694  17.884  1.00 35.16  ? 40  PHE A C   1 
ATOM   303  O O   . PHE A 1 40  ? 9.297   -2.891  18.336  1.00 37.79  ? 40  PHE A O   1 
ATOM   304  C CB  . PHE A 1 40  ? 6.066   -3.082  17.885  1.00 34.72  ? 40  PHE A CB  1 
ATOM   305  C CG  . PHE A 1 40  ? 4.729   -3.184  18.544  1.00 38.88  ? 40  PHE A CG  1 
ATOM   306  C CD1 . PHE A 1 40  ? 3.989   -4.360  18.459  1.00 44.96  ? 40  PHE A CD1 1 
ATOM   307  C CD2 . PHE A 1 40  ? 4.217   -2.129  19.286  1.00 35.55  ? 40  PHE A CD2 1 
ATOM   308  C CE1 . PHE A 1 40  ? 2.755   -4.472  19.078  1.00 43.98  ? 40  PHE A CE1 1 
ATOM   309  C CE2 . PHE A 1 40  ? 2.981   -2.241  19.902  1.00 40.17  ? 40  PHE A CE2 1 
ATOM   310  C CZ  . PHE A 1 40  ? 2.248   -3.413  19.787  1.00 37.64  ? 40  PHE A CZ  1 
ATOM   311  N N   . ASP A 1 41  ? 8.692   -4.347  16.746  1.00 34.75  ? 41  ASP A N   1 
ATOM   312  C CA  . ASP A 1 41  ? 9.982   -4.236  16.089  1.00 37.66  ? 41  ASP A CA  1 
ATOM   313  C C   . ASP A 1 41  ? 10.046  -3.100  15.068  1.00 39.64  ? 41  ASP A C   1 
ATOM   314  O O   . ASP A 1 41  ? 11.054  -2.980  14.368  1.00 44.58  ? 41  ASP A O   1 
ATOM   315  C CB  . ASP A 1 41  ? 10.363  -5.553  15.393  1.00 42.91  ? 41  ASP A CB  1 
ATOM   316  C CG  . ASP A 1 41  ? 9.271   -6.084  14.488  1.00 63.51  ? 41  ASP A CG  1 
ATOM   317  O OD1 . ASP A 1 41  ? 8.387   -5.299  14.064  1.00 60.85  ? 41  ASP A OD1 1 
ATOM   318  O OD2 . ASP A 1 41  ? 9.311   -7.297  14.176  1.00 76.29  ? 41  ASP A OD2 1 
ATOM   319  N N   . PHE A 1 42  ? 9.002   -2.274  14.936  1.00 36.31  ? 42  PHE A N   1 
ATOM   320  C CA  . PHE A 1 42  ? 9.027   -1.259  13.888  1.00 33.33  ? 42  PHE A CA  1 
ATOM   321  C C   . PHE A 1 42  ? 9.408   0.131   14.406  1.00 30.53  ? 42  PHE A C   1 
ATOM   322  O O   . PHE A 1 42  ? 9.223   1.116   13.686  1.00 31.27  ? 42  PHE A O   1 
ATOM   323  C CB  . PHE A 1 42  ? 7.696   -1.227  13.125  1.00 33.53  ? 42  PHE A CB  1 
ATOM   324  C CG  . PHE A 1 42  ? 6.487   -1.052  13.992  1.00 35.88  ? 42  PHE A CG  1 
ATOM   325  C CD1 . PHE A 1 42  ? 6.141   0.202   14.490  1.00 31.39  ? 42  PHE A CD1 1 
ATOM   326  C CD2 . PHE A 1 42  ? 5.658   -2.133  14.265  1.00 39.77  ? 42  PHE A CD2 1 
ATOM   327  C CE1 . PHE A 1 42  ? 5.004   0.364   15.295  1.00 36.34  ? 42  PHE A CE1 1 
ATOM   328  C CE2 . PHE A 1 42  ? 4.526   -1.980  15.051  1.00 36.59  ? 42  PHE A CE2 1 
ATOM   329  C CZ  . PHE A 1 42  ? 4.202   -0.733  15.578  1.00 35.89  ? 42  PHE A CZ  1 
ATOM   330  N N   . VAL A 1 43  ? 10.002  0.224   15.591  1.00 29.61  ? 43  VAL A N   1 
ATOM   331  C CA  . VAL A 1 43  ? 10.559  1.488   16.087  1.00 25.30  ? 43  VAL A CA  1 
ATOM   332  C C   . VAL A 1 43  ? 11.970  1.219   16.581  1.00 26.79  ? 43  VAL A C   1 
ATOM   333  O O   . VAL A 1 43  ? 12.306  0.068   16.912  1.00 29.60  ? 43  VAL A O   1 
ATOM   334  C CB  . VAL A 1 43  ? 9.702   2.106   17.226  1.00 29.87  ? 43  VAL A CB  1 
ATOM   335  C CG1 . VAL A 1 43  ? 8.311   2.410   16.758  1.00 26.52  ? 43  VAL A CG1 1 
ATOM   336  C CG2 . VAL A 1 43  ? 9.692   1.242   18.497  1.00 28.48  ? 43  VAL A CG2 1 
ATOM   337  N N   . PRO A 1 44  ? 12.811  2.259   16.698  1.00 26.66  ? 44  PRO A N   1 
ATOM   338  C CA  . PRO A 1 44  ? 14.148  2.037   17.268  1.00 32.92  ? 44  PRO A CA  1 
ATOM   339  C C   . PRO A 1 44  ? 14.065  1.604   18.730  1.00 27.36  ? 44  PRO A C   1 
ATOM   340  O O   . PRO A 1 44  ? 13.143  1.983   19.463  1.00 29.35  ? 44  PRO A O   1 
ATOM   341  C CB  . PRO A 1 44  ? 14.841  3.406   17.139  1.00 30.07  ? 44  PRO A CB  1 
ATOM   342  C CG  . PRO A 1 44  ? 14.030  4.202   16.145  1.00 32.82  ? 44  PRO A CG  1 
ATOM   343  C CD  . PRO A 1 44  ? 12.612  3.642   16.224  1.00 29.78  ? 44  PRO A CD  1 
ATOM   344  N N   . ARG A 1 45  ? 15.047  0.799   19.152  1.00 26.55  ? 45  ARG A N   1 
ATOM   345  C CA  . ARG A 1 45  ? 15.206  0.526   20.574  1.00 29.41  ? 45  ARG A CA  1 
ATOM   346  C C   . ARG A 1 45  ? 15.516  1.834   21.280  1.00 30.61  ? 45  ARG A C   1 
ATOM   347  O O   . ARG A 1 45  ? 16.251  2.681   20.758  1.00 28.38  ? 45  ARG A O   1 
ATOM   348  C CB  . ARG A 1 45  ? 16.330  -0.497  20.847  1.00 27.75  ? 45  ARG A CB  1 
ATOM   349  C CG  . ARG A 1 45  ? 16.215  -1.842  20.117  1.00 32.77  ? 45  ARG A CG  1 
ATOM   350  C CD  . ARG A 1 45  ? 14.974  -2.668  20.495  1.00 32.23  ? 45  ARG A CD  1 
ATOM   351  N NE  . ARG A 1 45  ? 13.809  -2.206  19.739  1.00 35.74  ? 45  ARG A NE  1 
ATOM   352  C CZ  . ARG A 1 45  ? 12.537  -2.416  20.066  1.00 37.94  ? 45  ARG A CZ  1 
ATOM   353  N NH1 . ARG A 1 45  ? 12.200  -3.175  21.099  1.00 32.06  ? 45  ARG A NH1 1 
ATOM   354  N NH2 . ARG A 1 45  ? 11.574  -1.824  19.353  1.00 37.02  ? 45  ARG A NH2 1 
ATOM   355  N N   . LEU A 1 46  ? 14.906  2.020   22.443  1.00 24.17  ? 46  LEU A N   1 
ATOM   356  C CA  . LEU A 1 46  ? 15.169  3.169   23.292  1.00 25.77  ? 46  LEU A CA  1 
ATOM   357  C C   . LEU A 1 46  ? 16.126  2.767   24.407  1.00 27.12  ? 46  LEU A C   1 
ATOM   358  O O   . LEU A 1 46  ? 15.864  1.802   25.128  1.00 27.85  ? 46  LEU A O   1 
ATOM   359  C CB  . LEU A 1 46  ? 13.849  3.680   23.862  1.00 21.81  ? 46  LEU A CB  1 
ATOM   360  C CG  . LEU A 1 46  ? 13.904  4.866   24.799  1.00 28.10  ? 46  LEU A CG  1 
ATOM   361  C CD1 . LEU A 1 46  ? 14.623  6.015   24.132  1.00 29.34  ? 46  LEU A CD1 1 
ATOM   362  C CD2 . LEU A 1 46  ? 12.481  5.273   25.152  1.00 28.22  ? 46  LEU A CD2 1 
ATOM   363  N N   . TYR A 1 47  ? 17.231  3.504   24.557  1.00 22.83  ? 47  TYR A N   1 
ATOM   364  C CA  . TYR A 1 47  ? 18.269  3.133   25.510  1.00 23.95  ? 47  TYR A CA  1 
ATOM   365  C C   . TYR A 1 47  ? 18.276  4.013   26.735  1.00 25.37  ? 47  TYR A C   1 
ATOM   366  O O   . TYR A 1 47  ? 18.499  3.509   27.831  1.00 26.88  ? 47  TYR A O   1 
ATOM   367  C CB  . TYR A 1 47  ? 19.667  3.170   24.866  1.00 26.92  ? 47  TYR A CB  1 
ATOM   368  C CG  . TYR A 1 47  ? 19.806  2.194   23.716  1.00 30.64  ? 47  TYR A CG  1 
ATOM   369  C CD1 . TYR A 1 47  ? 19.483  0.857   23.886  1.00 33.81  ? 47  TYR A CD1 1 
ATOM   370  C CD2 . TYR A 1 47  ? 20.268  2.612   22.464  1.00 33.82  ? 47  TYR A CD2 1 
ATOM   371  C CE1 . TYR A 1 47  ? 19.607  -0.055  22.829  1.00 41.60  ? 47  TYR A CE1 1 
ATOM   372  C CE2 . TYR A 1 47  ? 20.396  1.702   21.392  1.00 32.16  ? 47  TYR A CE2 1 
ATOM   373  C CZ  . TYR A 1 47  ? 20.056  0.380   21.589  1.00 41.73  ? 47  TYR A CZ  1 
ATOM   374  O OH  . TYR A 1 47  ? 20.181  -0.524  20.545  1.00 37.77  ? 47  TYR A OH  1 
ATOM   375  N N   . SER A 1 48  ? 18.021  5.305   26.582  1.00 24.57  ? 48  SER A N   1 
ATOM   376  C CA  . SER A 1 48  ? 18.085  6.171   27.750  1.00 29.28  ? 48  SER A CA  1 
ATOM   377  C C   . SER A 1 48  ? 17.429  7.502   27.403  1.00 30.64  ? 48  SER A C   1 
ATOM   378  O O   . SER A 1 48  ? 17.279  7.858   26.231  1.00 27.77  ? 48  SER A O   1 
ATOM   379  C CB  . SER A 1 48  ? 19.534  6.357   28.220  1.00 32.27  ? 48  SER A CB  1 
ATOM   380  O OG  . SER A 1 48  ? 20.213  7.204   27.326  1.00 34.37  ? 48  SER A OG  1 
ATOM   381  N N   . ILE A 1 49  ? 17.013  8.222   28.437  1.00 26.04  ? 49  ILE A N   1 
ATOM   382  C CA  . ILE A 1 49  ? 16.509  9.580   28.266  1.00 29.33  ? 49  ILE A CA  1 
ATOM   383  C C   . ILE A 1 49  ? 17.234  10.473  29.253  1.00 32.06  ? 49  ILE A C   1 
ATOM   384  O O   . ILE A 1 49  ? 17.618  10.052  30.351  1.00 32.12  ? 49  ILE A O   1 
ATOM   385  C CB  . ILE A 1 49  ? 14.982  9.669   28.475  1.00 30.08  ? 49  ILE A CB  1 
ATOM   386  C CG1 . ILE A 1 49  ? 14.618  9.355   29.926  1.00 32.33  ? 49  ILE A CG1 1 
ATOM   387  C CG2 . ILE A 1 49  ? 14.236  8.703   27.528  1.00 30.72  ? 49  ILE A CG2 1 
ATOM   388  C CD1 . ILE A 1 49  ? 13.269  9.965   30.352  1.00 34.10  ? 49  ILE A CD1 1 
ATOM   389  N N   . ASN A 1 50  ? 17.470  11.716  28.847  1.00 26.93  ? 50  ASN A N   1 
ATOM   390  C CA  . ASN A 1 50  ? 18.098  12.678  29.742  1.00 25.53  ? 50  ASN A CA  1 
ATOM   391  C C   . ASN A 1 50  ? 17.318  13.972  29.598  1.00 27.04  ? 50  ASN A C   1 
ATOM   392  O O   . ASN A 1 50  ? 17.561  14.757  28.677  1.00 27.59  ? 50  ASN A O   1 
ATOM   393  C CB  . ASN A 1 50  ? 19.583  12.859  29.418  1.00 26.17  ? 50  ASN A CB  1 
ATOM   394  C CG  . ASN A 1 50  ? 20.282  13.784  30.389  1.00 32.22  ? 50  ASN A CG  1 
ATOM   395  O OD1 . ASN A 1 50  ? 19.646  14.476  31.201  1.00 31.74  ? 50  ASN A OD1 1 
ATOM   396  N ND2 . ASN A 1 50  ? 21.607  13.810  30.314  1.00 35.88  ? 50  ASN A ND2 1 
ATOM   397  N N   . PRO A 1 51  ? 16.346  14.208  30.483  1.00 26.06  ? 51  PRO A N   1 
ATOM   398  C CA  . PRO A 1 51  ? 15.562  15.445  30.431  1.00 29.76  ? 51  PRO A CA  1 
ATOM   399  C C   . PRO A 1 51  ? 16.370  16.694  30.727  1.00 31.81  ? 51  PRO A C   1 
ATOM   400  O O   . PRO A 1 51  ? 15.902  17.794  30.412  1.00 30.31  ? 51  PRO A O   1 
ATOM   401  C CB  . PRO A 1 51  ? 14.483  15.238  31.500  1.00 30.34  ? 51  PRO A CB  1 
ATOM   402  C CG  . PRO A 1 51  ? 14.571  13.762  31.896  1.00 33.35  ? 51  PRO A CG  1 
ATOM   403  C CD  . PRO A 1 51  ? 15.971  13.323  31.600  1.00 26.70  ? 51  PRO A CD  1 
ATOM   404  N N   . GLU A 1 52  ? 17.519  16.576  31.400  1.00 27.16  ? 52  GLU A N   1 
ATOM   405  C CA  . GLU A 1 52  ? 18.345  17.751  31.657  1.00 29.36  ? 52  GLU A CA  1 
ATOM   406  C C   . GLU A 1 52  ? 18.948  18.308  30.373  1.00 30.73  ? 52  GLU A C   1 
ATOM   407  O O   . GLU A 1 52  ? 19.138  19.519  30.252  1.00 31.63  ? 52  GLU A O   1 
ATOM   408  C CB  . GLU A 1 52  ? 19.441  17.418  32.667  1.00 35.51  ? 52  GLU A CB  1 
ATOM   409  C CG  . GLU A 1 52  ? 18.918  17.006  34.025  1.00 36.76  ? 52  GLU A CG  1 
ATOM   410  C CD  . GLU A 1 52  ? 17.887  18.002  34.552  1.00 44.51  ? 52  GLU A CD  1 
ATOM   411  O OE1 . GLU A 1 52  ? 18.297  19.023  35.141  1.00 58.89  ? 52  GLU A OE1 1 
ATOM   412  O OE2 . GLU A 1 52  ? 16.669  17.785  34.361  1.00 63.05  ? 52  GLU A OE2 1 
ATOM   413  N N   . LYS A 1 53  ? 19.323  17.436  29.443  1.00 29.31  ? 53  LYS A N   1 
ATOM   414  C CA  . LYS A 1 53  ? 19.834  17.833  28.140  1.00 30.66  ? 53  LYS A CA  1 
ATOM   415  C C   . LYS A 1 53  ? 18.810  17.678  27.018  1.00 31.03  ? 53  LYS A C   1 
ATOM   416  O O   . LYS A 1 53  ? 19.145  17.943  25.856  1.00 29.30  ? 53  LYS A O   1 
ATOM   417  C CB  . LYS A 1 53  ? 21.113  17.053  27.830  1.00 35.14  ? 53  LYS A CB  1 
ATOM   418  C CG  . LYS A 1 53  ? 22.152  17.306  28.926  1.00 41.31  ? 53  LYS A CG  1 
ATOM   419  C CD  . LYS A 1 53  ? 23.509  16.823  28.542  1.00 43.64  ? 53  LYS A CD  1 
ATOM   420  C CE  . LYS A 1 53  ? 24.464  17.020  29.702  1.00 45.97  ? 53  LYS A CE  1 
ATOM   421  N NZ  . LYS A 1 53  ? 25.763  16.373  29.410  1.00 49.76  ? 53  LYS A NZ  1 
ATOM   422  N N   . LEU A 1 54  ? 17.596  17.225  27.331  1.00 27.44  ? 54  LEU A N   1 
ATOM   423  C CA  . LEU A 1 54  ? 16.582  16.900  26.324  1.00 29.88  ? 54  LEU A CA  1 
ATOM   424  C C   . LEU A 1 54  ? 17.158  15.982  25.264  1.00 30.46  ? 54  LEU A C   1 
ATOM   425  O O   . LEU A 1 54  ? 16.982  16.198  24.062  1.00 28.13  ? 54  LEU A O   1 
ATOM   426  C CB  . LEU A 1 54  ? 16.013  18.173  25.666  1.00 24.89  ? 54  LEU A CB  1 
ATOM   427  C CG  . LEU A 1 54  ? 15.348  19.187  26.602  1.00 26.49  ? 54  LEU A CG  1 
ATOM   428  C CD1 . LEU A 1 54  ? 14.848  20.412  25.837  1.00 30.49  ? 54  LEU A CD1 1 
ATOM   429  C CD2 . LEU A 1 54  ? 14.208  18.545  27.427  1.00 25.33  ? 54  LEU A CD2 1 
ATOM   430  N N   . GLU A 1 55  ? 17.852  14.941  25.722  1.00 25.51  ? 55  GLU A N   1 
ATOM   431  C CA  . GLU A 1 55  ? 18.493  13.981  24.831  1.00 29.22  ? 55  GLU A CA  1 
ATOM   432  C C   . GLU A 1 55  ? 17.840  12.614  24.956  1.00 27.54  ? 55  GLU A C   1 
ATOM   433  O O   . GLU A 1 55  ? 17.600  12.116  26.068  1.00 27.47  ? 55  GLU A O   1 
ATOM   434  C CB  . GLU A 1 55  ? 19.985  13.832  25.138  1.00 30.55  ? 55  GLU A CB  1 
ATOM   435  C CG  . GLU A 1 55  ? 20.819  14.961  24.597  1.00 38.65  ? 55  GLU A CG  1 
ATOM   436  C CD  . GLU A 1 55  ? 22.299  14.681  24.718  1.00 47.20  ? 55  GLU A CD  1 
ATOM   437  O OE1 . GLU A 1 55  ? 22.668  13.855  25.576  1.00 43.54  ? 55  GLU A OE1 1 
ATOM   438  O OE2 . GLU A 1 55  ? 23.095  15.307  23.979  1.00 48.20  ? 55  GLU A OE2 1 
ATOM   439  N N   . ILE A 1 56  ? 17.613  11.986  23.812  1.00 30.24  ? 56  ILE A N   1 
ATOM   440  C CA  . ILE A 1 56  ? 17.145  10.611  23.753  1.00 28.66  ? 56  ILE A CA  1 
ATOM   441  C C   . ILE A 1 56  ? 18.201  9.790   23.029  1.00 26.92  ? 56  ILE A C   1 
ATOM   442  O O   . ILE A 1 56  ? 18.613  10.145  21.924  1.00 31.58  ? 56  ILE A O   1 
ATOM   443  C CB  . ILE A 1 56  ? 15.778  10.503  23.058  1.00 30.18  ? 56  ILE A CB  1 
ATOM   444  C CG1 . ILE A 1 56  ? 14.734  11.319  23.807  1.00 29.75  ? 56  ILE A CG1 1 
ATOM   445  C CG2 . ILE A 1 56  ? 15.303  9.059   23.004  1.00 28.16  ? 56  ILE A CG2 1 
ATOM   446  C CD1 . ILE A 1 56  ? 13.495  11.469  22.998  1.00 33.78  ? 56  ILE A CD1 1 
ATOM   447  N N   . GLU A 1 57  ? 18.632  8.702   23.656  1.00 24.86  ? 57  GLU A N   1 
ATOM   448  C CA  . GLU A 1 57  ? 19.612  7.776   23.093  1.00 28.23  ? 57  GLU A CA  1 
ATOM   449  C C   . GLU A 1 57  ? 18.856  6.567   22.568  1.00 31.02  ? 57  GLU A C   1 
ATOM   450  O O   . GLU A 1 57  ? 18.148  5.896   23.334  1.00 24.71  ? 57  GLU A O   1 
ATOM   451  C CB  . GLU A 1 57  ? 20.613  7.347   24.169  1.00 32.09  ? 57  GLU A CB  1 
ATOM   452  C CG  . GLU A 1 57  ? 21.889  6.642   23.701  1.00 43.24  ? 57  GLU A CG  1 
ATOM   453  C CD  . GLU A 1 57  ? 22.535  5.787   24.827  1.00 58.23  ? 57  GLU A CD  1 
ATOM   454  O OE1 . GLU A 1 57  ? 22.203  5.988   26.026  1.00 60.73  ? 57  GLU A OE1 1 
ATOM   455  O OE2 . GLU A 1 57  ? 23.363  4.901   24.522  1.00 50.23  ? 57  GLU A OE2 1 
ATOM   456  N N   . MET A 1 58  ? 19.005  6.276   21.277  1.00 31.51  ? 58  MET A N   1 
ATOM   457  C CA  . MET A 1 58  ? 18.238  5.181   20.704  1.00 31.20  ? 58  MET A CA  1 
ATOM   458  C C   . MET A 1 58  ? 19.077  4.439   19.670  1.00 28.24  ? 58  MET A C   1 
ATOM   459  O O   . MET A 1 58  ? 20.194  4.839   19.322  1.00 31.78  ? 58  MET A O   1 
ATOM   460  C CB  . MET A 1 58  ? 16.936  5.713   20.092  1.00 31.66  ? 58  MET A CB  1 
ATOM   461  C CG  . MET A 1 58  ? 17.123  6.453   18.784  1.00 34.83  ? 58  MET A CG  1 
ATOM   462  S SD  . MET A 1 58  ? 15.604  7.339   18.279  1.00 50.30  ? 58  MET A SD  1 
ATOM   463  C CE  . MET A 1 58  ? 15.414  8.458   19.618  1.00 43.57  ? 58  MET A CE  1 
ATOM   464  N N   . GLU A 1 59  ? 18.506  3.361   19.158  1.00 31.42  ? 59  GLU A N   1 
ATOM   465  C CA  . GLU A 1 59  ? 19.140  2.553   18.115  1.00 31.98  ? 59  GLU A CA  1 
ATOM   466  C C   . GLU A 1 59  ? 19.329  3.364   16.836  1.00 33.03  ? 59  GLU A C   1 
ATOM   467  O O   . GLU A 1 59  ? 18.373  3.960   16.336  1.00 34.38  ? 59  GLU A O   1 
ATOM   468  C CB  . GLU A 1 59  ? 18.237  1.352   17.834  1.00 30.27  ? 59  GLU A CB  1 
ATOM   469  C CG  . GLU A 1 59  ? 18.782  0.280   16.930  1.00 31.71  ? 59  GLU A CG  1 
ATOM   470  C CD  . GLU A 1 59  ? 17.691  -0.696  16.520  1.00 36.66  ? 59  GLU A CD  1 
ATOM   471  O OE1 . GLU A 1 59  ? 16.536  -0.521  16.968  1.00 32.49  ? 59  GLU A OE1 1 
ATOM   472  O OE2 . GLU A 1 59  ? 17.986  -1.643  15.765  1.00 37.27  ? 59  GLU A OE2 1 
ATOM   473  N N   . PHE A 1 60  ? 20.549  3.353   16.274  1.00 38.07  ? 60  PHE A N   1 
ATOM   474  C CA  . PHE A 1 60  ? 20.734  3.847   14.909  1.00 38.05  ? 60  PHE A CA  1 
ATOM   475  C C   . PHE A 1 60  ? 20.115  2.881   13.911  1.00 39.62  ? 60  PHE A C   1 
ATOM   476  O O   . PHE A 1 60  ? 20.386  1.679   13.964  1.00 37.35  ? 60  PHE A O   1 
ATOM   477  C CB  . PHE A 1 60  ? 22.209  4.009   14.567  1.00 43.37  ? 60  PHE A CB  1 
ATOM   478  C CG  . PHE A 1 60  ? 22.436  4.443   13.137  1.00 51.35  ? 60  PHE A CG  1 
ATOM   479  C CD1 . PHE A 1 60  ? 22.053  5.708   12.715  1.00 51.03  ? 60  PHE A CD1 1 
ATOM   480  C CD2 . PHE A 1 60  ? 22.967  3.561   12.203  1.00 53.83  ? 60  PHE A CD2 1 
ATOM   481  C CE1 . PHE A 1 60  ? 22.245  6.105   11.399  1.00 54.13  ? 60  PHE A CE1 1 
ATOM   482  C CE2 . PHE A 1 60  ? 23.158  3.948   10.879  1.00 55.08  ? 60  PHE A CE2 1 
ATOM   483  C CZ  . PHE A 1 60  ? 22.798  5.223   10.478  1.00 52.39  ? 60  PHE A CZ  1 
ATOM   484  N N   . ILE A 1 61  ? 19.317  3.399   12.973  1.00 40.96  ? 61  ILE A N   1 
ATOM   485  C CA  . ILE A 1 61  ? 18.569  2.552   12.045  1.00 36.73  ? 61  ILE A CA  1 
ATOM   486  C C   . ILE A 1 61  ? 19.244  2.594   10.681  1.00 48.07  ? 61  ILE A C   1 
ATOM   487  O O   . ILE A 1 61  ? 19.198  3.600   9.961   1.00 43.98  ? 61  ILE A O   1 
ATOM   488  C CB  . ILE A 1 61  ? 17.098  2.973   11.940  1.00 39.98  ? 61  ILE A CB  1 
ATOM   489  C CG1 . ILE A 1 61  ? 16.442  3.010   13.333  1.00 38.53  ? 61  ILE A CG1 1 
ATOM   490  C CG2 . ILE A 1 61  ? 16.374  1.998   11.005  1.00 39.73  ? 61  ILE A CG2 1 
ATOM   491  C CD1 . ILE A 1 61  ? 16.588  1.718   14.134  1.00 36.24  ? 61  ILE A CD1 1 
ATOM   492  N N   . GLU A 1 62  ? 19.849  1.493   10.303  1.00 44.11  ? 62  GLU A N   1 
ATOM   493  C CA  . GLU A 1 62  ? 20.465  1.406   9.002   1.00 51.61  ? 62  GLU A CA  1 
ATOM   494  C C   . GLU A 1 62  ? 19.423  0.982   7.970   1.00 50.54  ? 62  GLU A C   1 
ATOM   495  O O   . GLU A 1 62  ? 18.422  0.335   8.294   1.00 51.56  ? 62  GLU A O   1 
ATOM   496  C CB  . GLU A 1 62  ? 21.689  0.498   9.105   1.00 55.25  ? 62  GLU A CB  1 
ATOM   497  C CG  . GLU A 1 62  ? 21.444  -0.941  9.469   1.00 61.68  ? 62  GLU A CG  1 
ATOM   498  C CD  . GLU A 1 62  ? 22.750  -1.716  9.447   1.00 90.34  ? 62  GLU A CD  1 
ATOM   499  O OE1 . GLU A 1 62  ? 23.769  -1.128  9.878   1.00 85.89  ? 62  GLU A OE1 1 
ATOM   500  O OE2 . GLU A 1 62  ? 22.768  -2.893  9.022   1.00 95.05  ? 62  GLU A OE2 1 
ATOM   501  N N   . GLY A 1 63  ? 19.595  1.484   6.754   1.00 51.43  ? 63  GLY A N   1 
ATOM   502  C CA  . GLY A 1 63  ? 18.647  1.282   5.678   1.00 53.38  ? 63  GLY A CA  1 
ATOM   503  C C   . GLY A 1 63  ? 18.450  2.577   4.914   1.00 54.54  ? 63  GLY A C   1 
ATOM   504  O O   . GLY A 1 63  ? 19.090  3.589   5.217   1.00 49.57  ? 63  GLY A O   1 
ATOM   505  N N   . ARG A 1 64  ? 17.557  2.570   3.937   1.00 54.07  ? 64  ARG A N   1 
ATOM   506  C CA  . ARG A 1 64  ? 17.359  3.781   3.161   1.00 46.02  ? 64  ARG A CA  1 
ATOM   507  C C   . ARG A 1 64  ? 16.000  4.398   3.484   1.00 52.84  ? 64  ARG A C   1 
ATOM   508  O O   . ARG A 1 64  ? 15.024  3.669   3.724   1.00 44.68  ? 64  ARG A O   1 
ATOM   509  C CB  . ARG A 1 64  ? 17.451  3.483   1.658   1.00 53.35  ? 64  ARG A CB  1 
ATOM   510  C CG  . ARG A 1 64  ? 18.675  2.641   1.295   1.00 53.98  ? 64  ARG A CG  1 
ATOM   511  C CD  . ARG A 1 64  ? 18.743  2.278   -0.182  1.00 55.41  ? 64  ARG A CD  1 
ATOM   512  N NE  . ARG A 1 64  ? 18.900  3.438   -1.053  1.00 60.47  ? 64  ARG A NE  1 
ATOM   513  C CZ  . ARG A 1 64  ? 18.861  3.390   -2.381  1.00 63.91  ? 64  ARG A CZ  1 
ATOM   514  N NH1 . ARG A 1 64  ? 18.641  2.255   -3.029  1.00 54.09  ? 64  ARG A NH1 1 
ATOM   515  N NH2 . ARG A 1 64  ? 19.072  4.502   -3.080  1.00 59.58  ? 64  ARG A NH2 1 
ATOM   516  N N   . PRO A 1 65  ? 15.903  5.725   3.516   1.00 47.10  ? 65  PRO A N   1 
ATOM   517  C CA  . PRO A 1 65  ? 14.593  6.352   3.726   1.00 45.93  ? 65  PRO A CA  1 
ATOM   518  C C   . PRO A 1 65  ? 13.684  6.059   2.537   1.00 53.11  ? 65  PRO A C   1 
ATOM   519  O O   . PRO A 1 65  ? 14.144  5.879   1.404   1.00 51.93  ? 65  PRO A O   1 
ATOM   520  C CB  . PRO A 1 65  ? 14.918  7.846   3.831   1.00 46.08  ? 65  PRO A CB  1 
ATOM   521  C CG  . PRO A 1 65  ? 16.223  8.007   3.088   1.00 53.57  ? 65  PRO A CG  1 
ATOM   522  C CD  . PRO A 1 65  ? 16.965  6.703   3.217   1.00 52.89  ? 65  PRO A CD  1 
ATOM   523  N N   . ILE A 1 66  ? 12.377  6.003   2.814   1.00 47.58  ? 66  ILE A N   1 
ATOM   524  C CA  . ILE A 1 66  ? 11.407  5.573   1.810   1.00 45.56  ? 66  ILE A CA  1 
ATOM   525  C C   . ILE A 1 66  ? 11.464  6.454   0.563   1.00 53.48  ? 66  ILE A C   1 
ATOM   526  O O   . ILE A 1 66  ? 11.266  5.966   -0.559  1.00 55.73  ? 66  ILE A O   1 
ATOM   527  C CB  . ILE A 1 66  ? 9.987   5.516   2.423   1.00 48.64  ? 66  ILE A CB  1 
ATOM   528  C CG1 . ILE A 1 66  ? 9.024   4.767   1.495   1.00 49.64  ? 66  ILE A CG1 1 
ATOM   529  C CG2 . ILE A 1 66  ? 9.460   6.913   2.805   1.00 41.97  ? 66  ILE A CG2 1 
ATOM   530  C CD1 . ILE A 1 66  ? 7.724   4.372   2.162   1.00 48.02  ? 66  ILE A CD1 1 
ATOM   531  N N   . LYS A 1 67  ? 11.773  7.745   0.723   1.00 48.43  ? 67  LYS A N   1 
ATOM   532  C CA  . LYS A 1 67  ? 11.824  8.647   -0.427  1.00 57.02  ? 67  LYS A CA  1 
ATOM   533  C C   . LYS A 1 67  ? 12.873  8.225   -1.449  1.00 58.30  ? 67  LYS A C   1 
ATOM   534  O O   . LYS A 1 67  ? 12.766  8.615   -2.614  1.00 58.85  ? 67  LYS A O   1 
ATOM   535  C CB  . LYS A 1 67  ? 12.067  10.083  0.049   1.00 48.96  ? 67  LYS A CB  1 
ATOM   536  C CG  . LYS A 1 67  ? 13.375  10.333  0.796   1.00 59.60  ? 67  LYS A CG  1 
ATOM   537  C CD  . LYS A 1 67  ? 13.960  11.701  0.468   1.00 61.55  ? 67  LYS A CD  1 
ATOM   538  C CE  . LYS A 1 67  ? 15.483  11.778  0.591   1.00 73.03  ? 67  LYS A CE  1 
ATOM   539  N NZ  . LYS A 1 67  ? 16.184  10.887  -0.369  1.00 73.32  ? 67  LYS A NZ  1 
ATOM   540  N N   . ASP A 1 68  ? 13.890  7.462   -1.037  1.00 56.33  ? 68  ASP A N   1 
ATOM   541  C CA  . ASP A 1 68  ? 14.925  6.969   -1.944  1.00 61.33  ? 68  ASP A CA  1 
ATOM   542  C C   . ASP A 1 68  ? 14.545  5.690   -2.675  1.00 58.16  ? 68  ASP A C   1 
ATOM   543  O O   . ASP A 1 68  ? 15.236  5.317   -3.628  1.00 55.31  ? 68  ASP A O   1 
ATOM   544  C CB  . ASP A 1 68  ? 16.225  6.710   -1.169  1.00 64.51  ? 68  ASP A CB  1 
ATOM   545  C CG  . ASP A 1 68  ? 16.968  7.987   -0.813  1.00 71.60  ? 68  ASP A CG  1 
ATOM   546  O OD1 . ASP A 1 68  ? 16.552  9.068   -1.289  1.00 63.96  ? 68  ASP A OD1 1 
ATOM   547  O OD2 . ASP A 1 68  ? 17.948  7.909   -0.036  1.00 63.74  ? 68  ASP A OD2 1 
ATOM   548  N N   . VAL A 1 69  ? 13.489  4.990   -2.263  1.00 57.19  ? 69  VAL A N   1 
ATOM   549  C CA  . VAL A 1 69  ? 13.242  3.662   -2.829  1.00 61.97  ? 69  VAL A CA  1 
ATOM   550  C C   . VAL A 1 69  ? 11.771  3.424   -3.161  1.00 59.06  ? 69  VAL A C   1 
ATOM   551  O O   . VAL A 1 69  ? 11.404  2.321   -3.579  1.00 55.19  ? 69  VAL A O   1 
ATOM   552  C CB  . VAL A 1 69  ? 13.734  2.563   -1.857  1.00 55.96  ? 69  VAL A CB  1 
ATOM   553  C CG1 . VAL A 1 69  ? 15.215  2.724   -1.530  1.00 58.10  ? 69  VAL A CG1 1 
ATOM   554  C CG2 . VAL A 1 69  ? 12.917  2.596   -0.571  1.00 53.08  ? 69  VAL A CG2 1 
ATOM   555  N N   . ILE A 1 70  ? 10.918  4.443   -2.972  1.00 57.21  ? 70  ILE A N   1 
ATOM   556  C CA  . ILE A 1 70  ? 9.468   4.223   -2.992  1.00 54.71  ? 70  ILE A CA  1 
ATOM   557  C C   . ILE A 1 70  ? 9.018   3.634   -4.330  1.00 61.70  ? 70  ILE A C   1 
ATOM   558  O O   . ILE A 1 70  ? 8.130   2.776   -4.381  1.00 56.31  ? 70  ILE A O   1 
ATOM   559  C CB  . ILE A 1 70  ? 8.722   5.532   -2.665  1.00 57.39  ? 70  ILE A CB  1 
ATOM   560  C CG1 . ILE A 1 70  ? 7.209   5.302   -2.631  1.00 58.39  ? 70  ILE A CG1 1 
ATOM   561  C CG2 . ILE A 1 70  ? 9.081   6.628   -3.647  1.00 58.21  ? 70  ILE A CG2 1 
ATOM   562  C CD1 . ILE A 1 70  ? 6.782   4.211   -1.671  1.00 56.64  ? 70  ILE A CD1 1 
ATOM   563  N N   . ASN A 1 71  ? 9.633   4.060   -5.425  1.00 60.54  ? 71  ASN A N   1 
ATOM   564  C CA  . ASN A 1 71  ? 9.232   3.562   -6.733  1.00 69.50  ? 71  ASN A CA  1 
ATOM   565  C C   . ASN A 1 71  ? 9.796   2.184   -7.052  1.00 68.02  ? 71  ASN A C   1 
ATOM   566  O O   . ASN A 1 71  ? 9.364   1.571   -8.032  1.00 64.66  ? 71  ASN A O   1 
ATOM   567  C CB  . ASN A 1 71  ? 9.630   4.582   -7.796  1.00 70.47  ? 71  ASN A CB  1 
ATOM   568  C CG  . ASN A 1 71  ? 8.837   5.867   -7.675  1.00 64.84  ? 71  ASN A CG  1 
ATOM   569  O OD1 . ASN A 1 71  ? 9.378   6.917   -7.330  1.00 67.52  ? 71  ASN A OD1 1 
ATOM   570  N ND2 . ASN A 1 71  ? 7.546   5.790   -7.972  1.00 65.25  ? 71  ASN A ND2 1 
ATOM   571  N N   . GLU A 1 72  ? 10.744  1.678   -6.260  1.00 62.71  ? 72  GLU A N   1 
ATOM   572  C CA  . GLU A 1 72  ? 11.276  0.338   -6.482  1.00 66.58  ? 72  GLU A CA  1 
ATOM   573  C C   . GLU A 1 72  ? 10.627  -0.712  -5.585  1.00 66.46  ? 72  GLU A C   1 
ATOM   574  O O   . GLU A 1 72  ? 10.894  -1.904  -5.765  1.00 63.05  ? 72  GLU A O   1 
ATOM   575  C CB  . GLU A 1 72  ? 12.803  0.321   -6.284  1.00 61.04  ? 72  GLU A CB  1 
ATOM   576  C CG  . GLU A 1 72  ? 13.520  1.679   -6.454  1.00 65.35  ? 72  GLU A CG  1 
ATOM   577  C CD  . GLU A 1 72  ? 13.433  2.269   -7.868  1.00 80.95  ? 72  GLU A CD  1 
ATOM   578  O OE1 . GLU A 1 72  ? 13.323  1.493   -8.846  1.00 83.90  ? 72  GLU A OE1 1 
ATOM   579  O OE2 . GLU A 1 72  ? 13.493  3.515   -8.007  1.00 77.19  ? 72  GLU A OE2 1 
ATOM   580  N N   . LEU A 1 73  ? 9.782   -0.297  -4.635  1.00 63.28  ? 73  LEU A N   1 
ATOM   581  C CA  . LEU A 1 73  ? 9.262   -1.186  -3.601  1.00 59.99  ? 73  LEU A CA  1 
ATOM   582  C C   . LEU A 1 73  ? 8.202   -2.108  -4.186  1.00 62.75  ? 73  LEU A C   1 
ATOM   583  O O   . LEU A 1 73  ? 7.323   -1.657  -4.926  1.00 64.06  ? 73  LEU A O   1 
ATOM   584  C CB  . LEU A 1 73  ? 8.657   -0.362  -2.463  1.00 54.04  ? 73  LEU A CB  1 
ATOM   585  C CG  . LEU A 1 73  ? 9.600   0.297   -1.454  1.00 56.88  ? 73  LEU A CG  1 
ATOM   586  C CD1 . LEU A 1 73  ? 8.841   0.664   -0.179  1.00 56.11  ? 73  LEU A CD1 1 
ATOM   587  C CD2 . LEU A 1 73  ? 10.808  -0.573  -1.153  1.00 56.95  ? 73  LEU A CD2 1 
ATOM   588  N N   . ASN A 1 74  ? 8.277   -3.398  -3.852  1.00 66.06  ? 74  ASN A N   1 
ATOM   589  C CA  . ASN A 1 74  ? 7.316   -4.359  -4.379  1.00 66.12  ? 74  ASN A CA  1 
ATOM   590  C C   . ASN A 1 74  ? 6.046   -4.350  -3.529  1.00 66.88  ? 74  ASN A C   1 
ATOM   591  O O   . ASN A 1 74  ? 5.964   -3.677  -2.495  1.00 58.04  ? 74  ASN A O   1 
ATOM   592  C CB  . ASN A 1 74  ? 7.942   -5.757  -4.465  1.00 63.98  ? 74  ASN A CB  1 
ATOM   593  C CG  . ASN A 1 74  ? 8.361   -6.318  -3.103  1.00 70.10  ? 74  ASN A CG  1 
ATOM   594  O OD1 . ASN A 1 74  ? 7.928   -5.849  -2.057  1.00 63.19  ? 74  ASN A OD1 1 
ATOM   595  N ND2 . ASN A 1 74  ? 9.218   -7.332  -3.125  1.00 71.86  ? 74  ASN A ND2 1 
ATOM   596  N N   . SER A 1 75  ? 5.047   -5.126  -3.960  1.00 66.09  ? 75  SER A N   1 
ATOM   597  C CA  . SER A 1 75  ? 3.764   -5.137  -3.259  1.00 60.04  ? 75  SER A CA  1 
ATOM   598  C C   . SER A 1 75  ? 3.879   -5.774  -1.876  1.00 64.28  ? 75  SER A C   1 
ATOM   599  O O   . SER A 1 75  ? 3.201   -5.334  -0.936  1.00 60.79  ? 75  SER A O   1 
ATOM   600  C CB  . SER A 1 75  ? 2.709   -5.851  -4.108  1.00 73.56  ? 75  SER A CB  1 
ATOM   601  O OG  . SER A 1 75  ? 2.529   -7.191  -3.687  1.00 86.14  ? 75  SER A OG  1 
ATOM   602  N N   . GLU A 1 76  ? 4.749   -6.778  -1.716  1.00 59.37  ? 76  GLU A N   1 
ATOM   603  C CA  . GLU A 1 76  ? 4.971   -7.356  -0.390  1.00 63.87  ? 76  GLU A CA  1 
ATOM   604  C C   . GLU A 1 76  ? 5.432   -6.294  0.602   1.00 62.93  ? 76  GLU A C   1 
ATOM   605  O O   . GLU A 1 76  ? 4.943   -6.229  1.740   1.00 52.29  ? 76  GLU A O   1 
ATOM   606  C CB  . GLU A 1 76  ? 6.019   -8.474  -0.476  1.00 68.44  ? 76  GLU A CB  1 
ATOM   607  C CG  . GLU A 1 76  ? 5.860   -9.623  0.536   1.00 72.36  ? 76  GLU A CG  1 
ATOM   608  C CD  . GLU A 1 76  ? 6.316   -9.252  1.945   1.00 82.28  ? 76  GLU A CD  1 
ATOM   609  O OE1 . GLU A 1 76  ? 7.494   -8.862  2.120   1.00 74.18  ? 76  GLU A OE1 1 
ATOM   610  O OE2 . GLU A 1 76  ? 5.498   -9.371  2.890   1.00 83.62  ? 76  GLU A OE2 1 
ATOM   611  N N   . THR A 1 77  ? 6.352   -5.431  0.173   1.00 63.29  ? 77  THR A N   1 
ATOM   612  C CA  . THR A 1 77  ? 6.935   -4.450  1.079   1.00 53.96  ? 77  THR A CA  1 
ATOM   613  C C   . THR A 1 77  ? 5.944   -3.340  1.410   1.00 58.65  ? 77  THR A C   1 
ATOM   614  O O   . THR A 1 77  ? 5.819   -2.944  2.578   1.00 54.02  ? 77  THR A O   1 
ATOM   615  C CB  . THR A 1 77  ? 8.201   -3.879  0.459   1.00 62.40  ? 77  THR A CB  1 
ATOM   616  O OG1 . THR A 1 77  ? 9.184   -4.918  0.375   1.00 64.10  ? 77  THR A OG1 1 
ATOM   617  C CG2 . THR A 1 77  ? 8.743   -2.744  1.314   1.00 52.00  ? 77  THR A CG2 1 
ATOM   618  N N   . ILE A 1 78  ? 5.219   -2.838  0.403   1.00 53.70  ? 78  ILE A N   1 
ATOM   619  C CA  . ILE A 1 78  ? 4.178   -1.844  0.658   1.00 53.81  ? 78  ILE A CA  1 
ATOM   620  C C   . ILE A 1 78  ? 3.135   -2.400  1.616   1.00 54.64  ? 78  ILE A C   1 
ATOM   621  O O   . ILE A 1 78  ? 2.672   -1.700  2.523   1.00 51.45  ? 78  ILE A O   1 
ATOM   622  C CB  . ILE A 1 78  ? 3.529   -1.382  -0.657  1.00 61.62  ? 78  ILE A CB  1 
ATOM   623  C CG1 . ILE A 1 78  ? 4.560   -0.670  -1.528  1.00 59.15  ? 78  ILE A CG1 1 
ATOM   624  C CG2 . ILE A 1 78  ? 2.337   -0.469  -0.357  1.00 53.54  ? 78  ILE A CG2 1 
ATOM   625  C CD1 . ILE A 1 78  ? 5.127   0.570   -0.862  1.00 62.12  ? 78  ILE A CD1 1 
ATOM   626  N N   . GLY A 1 79  ? 2.755   -3.669  1.437   1.00 49.74  ? 79  GLY A N   1 
ATOM   627  C CA  . GLY A 1 79  ? 1.794   -4.269  2.344   1.00 48.54  ? 79  GLY A CA  1 
ATOM   628  C C   . GLY A 1 79  ? 2.288   -4.277  3.777   1.00 53.89  ? 79  GLY A C   1 
ATOM   629  O O   . GLY A 1 79  ? 1.514   -4.040  4.712   1.00 49.28  ? 79  GLY A O   1 
ATOM   630  N N   . ARG A 1 80  ? 3.596   -4.499  3.965   1.00 52.64  ? 80  ARG A N   1 
ATOM   631  C CA  . ARG A 1 80  ? 4.156   -4.482  5.313   1.00 50.62  ? 80  ARG A CA  1 
ATOM   632  C C   . ARG A 1 80  ? 4.082   -3.091  5.923   1.00 46.20  ? 80  ARG A C   1 
ATOM   633  O O   . ARG A 1 80  ? 3.827   -2.956  7.123   1.00 42.66  ? 80  ARG A O   1 
ATOM   634  C CB  . ARG A 1 80  ? 5.597   -5.001  5.297   1.00 49.59  ? 80  ARG A CB  1 
ATOM   635  C CG  . ARG A 1 80  ? 5.672   -6.530  5.305   1.00 60.70  ? 80  ARG A CG  1 
ATOM   636  C CD  . ARG A 1 80  ? 6.930   -7.097  4.654   1.00 65.10  ? 80  ARG A CD  1 
ATOM   637  N NE  . ARG A 1 80  ? 8.164   -6.733  5.339   1.00 66.09  ? 80  ARG A NE  1 
ATOM   638  C CZ  . ARG A 1 80  ? 9.248   -6.272  4.727   1.00 70.87  ? 80  ARG A CZ  1 
ATOM   639  N NH1 . ARG A 1 80  ? 9.303   -6.161  3.409   1.00 65.66  ? 80  ARG A NH1 1 
ATOM   640  N NH2 . ARG A 1 80  ? 10.315  -5.942  5.453   1.00 65.81  ? 80  ARG A NH2 1 
ATOM   641  N N   . ILE A 1 81  ? 4.274   -2.045  5.115   1.00 46.17  ? 81  ILE A N   1 
ATOM   642  C CA  . ILE A 1 81  ? 4.174   -0.684  5.642   1.00 45.74  ? 81  ILE A CA  1 
ATOM   643  C C   . ILE A 1 81  ? 2.729   -0.358  6.008   1.00 45.38  ? 81  ILE A C   1 
ATOM   644  O O   . ILE A 1 81  ? 2.457   0.249   7.055   1.00 39.98  ? 81  ILE A O   1 
ATOM   645  C CB  . ILE A 1 81  ? 4.737   0.327   4.628   1.00 48.92  ? 81  ILE A CB  1 
ATOM   646  C CG1 . ILE A 1 81  ? 6.186   -0.012  4.269   1.00 44.03  ? 81  ILE A CG1 1 
ATOM   647  C CG2 . ILE A 1 81  ? 4.659   1.732   5.212   1.00 42.95  ? 81  ILE A CG2 1 
ATOM   648  C CD1 . ILE A 1 81  ? 6.709   0.777   3.068   1.00 48.23  ? 81  ILE A CD1 1 
ATOM   649  N N   . LEU A 1 82  ? 1.780   -0.755  5.156   1.00 42.84  ? 82  LEU A N   1 
ATOM   650  C CA  . LEU A 1 82  ? 0.366   -0.586  5.476   1.00 42.68  ? 82  LEU A CA  1 
ATOM   651  C C   . LEU A 1 82  ? 0.012   -1.275  6.788   1.00 42.97  ? 82  LEU A C   1 
ATOM   652  O O   . LEU A 1 82  ? -0.803  -0.762  7.561   1.00 45.60  ? 82  LEU A O   1 
ATOM   653  C CB  . LEU A 1 82  ? -0.499  -1.138  4.345   1.00 44.12  ? 82  LEU A CB  1 
ATOM   654  C CG  . LEU A 1 82  ? -0.372  -0.453  2.981   1.00 50.78  ? 82  LEU A CG  1 
ATOM   655  C CD1 . LEU A 1 82  ? -1.225  -1.170  1.925   1.00 50.75  ? 82  LEU A CD1 1 
ATOM   656  C CD2 . LEU A 1 82  ? -0.774  1.015   3.074   1.00 46.82  ? 82  LEU A CD2 1 
ATOM   657  N N   . ASP A 1 83  ? 0.586   -2.456  7.040   1.00 44.08  ? 83  ASP A N   1 
ATOM   658  C CA  . ASP A 1 83  ? 0.335   -3.157  8.303   1.00 42.55  ? 83  ASP A CA  1 
ATOM   659  C C   . ASP A 1 83  ? 0.797   -2.337  9.504   1.00 37.52  ? 83  ASP A C   1 
ATOM   660  O O   . ASP A 1 83  ? 0.131   -2.319  10.548  1.00 37.73  ? 83  ASP A O   1 
ATOM   661  C CB  . ASP A 1 83  ? 1.049   -4.511  8.305   1.00 37.07  ? 83  ASP A CB  1 
ATOM   662  C CG  . ASP A 1 83  ? 0.446   -5.496  7.310   1.00 52.77  ? 83  ASP A CG  1 
ATOM   663  O OD1 . ASP A 1 83  ? -0.711  -5.302  6.858   1.00 46.08  ? 83  ASP A OD1 1 
ATOM   664  O OD2 . ASP A 1 83  ? 1.167   -6.450  6.950   1.00 52.89  ? 83  ASP A OD2 1 
ATOM   665  N N   . ILE A 1 84  ? 1.952   -1.682  9.397   1.00 36.00  ? 84  ILE A N   1 
ATOM   666  C CA  . ILE A 1 84  ? 2.435   -0.899  10.539  1.00 33.79  ? 84  ILE A CA  1 
ATOM   667  C C   . ILE A 1 84  ? 1.542   0.317   10.770  1.00 34.88  ? 84  ILE A C   1 
ATOM   668  O O   . ILE A 1 84  ? 1.242   0.666   11.911  1.00 35.43  ? 84  ILE A O   1 
ATOM   669  C CB  . ILE A 1 84  ? 3.904   -0.496  10.327  1.00 35.41  ? 84  ILE A CB  1 
ATOM   670  C CG1 . ILE A 1 84  ? 4.788   -1.749  10.329  1.00 40.83  ? 84  ILE A CG1 1 
ATOM   671  C CG2 . ILE A 1 84  ? 4.380   0.490   11.446  1.00 37.25  ? 84  ILE A CG2 1 
ATOM   672  C CD1 . ILE A 1 84  ? 6.127   -1.549  9.640   1.00 38.18  ? 84  ILE A CD1 1 
ATOM   673  N N   . CYS A 1 85  ? 1.125   0.998   9.694   1.00 36.98  ? 85  CYS A N   1 
ATOM   674  C CA  . CYS A 1 85  ? 0.198   2.115   9.860   1.00 39.73  ? 85  CYS A CA  1 
ATOM   675  C C   . CYS A 1 85  ? -1.085  1.654   10.524  1.00 40.46  ? 85  CYS A C   1 
ATOM   676  O O   . CYS A 1 85  ? -1.630  2.342   11.391  1.00 35.98  ? 85  CYS A O   1 
ATOM   677  C CB  . CYS A 1 85  ? -0.127  2.748   8.509   1.00 36.54  ? 85  CYS A CB  1 
ATOM   678  S SG  . CYS A 1 85  ? 1.307   3.479   7.674   1.00 45.08  ? 85  CYS A SG  1 
ATOM   679  N N   . ARG A 1 86  ? -1.610  0.510   10.084  1.00 38.77  ? 86  ARG A N   1 
ATOM   680  C CA  . ARG A 1 86  ? -2.818  -0.042  10.679  1.00 38.36  ? 86  ARG A CA  1 
ATOM   681  C C   . ARG A 1 86  ? -2.595  -0.367  12.150  1.00 39.08  ? 86  ARG A C   1 
ATOM   682  O O   . ARG A 1 86  ? -3.440  -0.058  12.997  1.00 37.59  ? 86  ARG A O   1 
ATOM   683  C CB  . ARG A 1 86  ? -3.247  -1.284  9.885   1.00 44.91  ? 86  ARG A CB  1 
ATOM   684  C CG  . ARG A 1 86  ? -4.345  -2.119  10.522  1.00 45.93  ? 86  ARG A CG  1 
ATOM   685  C CD  . ARG A 1 86  ? -5.616  -1.319  10.744  1.00 47.89  ? 86  ARG A CD  1 
ATOM   686  N NE  . ARG A 1 86  ? -6.639  -2.155  11.361  1.00 50.61  ? 86  ARG A NE  1 
ATOM   687  C CZ  . ARG A 1 86  ? -7.722  -1.693  11.971  1.00 54.56  ? 86  ARG A CZ  1 
ATOM   688  N NH1 . ARG A 1 86  ? -7.992  -0.397  12.014  1.00 54.41  ? 86  ARG A NH1 1 
ATOM   689  N NH2 . ARG A 1 86  ? -8.543  -2.553  12.571  1.00 55.44  ? 86  ARG A NH2 1 
ATOM   690  N N   . LYS A 1 87  ? -1.442  -0.960  12.478  1.00 38.63  ? 87  LYS A N   1 
ATOM   691  C CA  . LYS A 1 87  ? -1.130  -1.263  13.868  1.00 35.36  ? 87  LYS A CA  1 
ATOM   692  C C   . LYS A 1 87  ? -1.191  -0.004  14.729  1.00 37.56  ? 87  LYS A C   1 
ATOM   693  O O   . LYS A 1 87  ? -1.771  -0.009  15.820  1.00 38.24  ? 87  LYS A O   1 
ATOM   694  C CB  . LYS A 1 87  ? 0.251   -1.909  13.963  1.00 37.85  ? 87  LYS A CB  1 
ATOM   695  C CG  . LYS A 1 87  ? 0.610   -2.503  15.334  1.00 41.93  ? 87  LYS A CG  1 
ATOM   696  C CD  . LYS A 1 87  ? -0.576  -3.191  16.000  1.00 46.22  ? 87  LYS A CD  1 
ATOM   697  C CE  . LYS A 1 87  ? -0.097  -4.270  16.964  1.00 53.84  ? 87  LYS A CE  1 
ATOM   698  N NZ  . LYS A 1 87  ? -0.906  -5.534  16.857  1.00 69.53  ? 87  LYS A NZ  1 
ATOM   699  N N   . LEU A 1 88  ? -0.588  1.092   14.249  1.00 39.57  ? 88  LEU A N   1 
ATOM   700  C CA  . LEU A 1 88  ? -0.625  2.352   14.998  1.00 38.04  ? 88  LEU A CA  1 
ATOM   701  C C   . LEU A 1 88  ? -2.054  2.871   15.108  1.00 38.96  ? 88  LEU A C   1 
ATOM   702  O O   . LEU A 1 88  ? -2.441  3.426   16.141  1.00 37.87  ? 88  LEU A O   1 
ATOM   703  C CB  . LEU A 1 88  ? 0.291   3.390   14.332  1.00 36.07  ? 88  LEU A CB  1 
ATOM   704  C CG  . LEU A 1 88  ? 1.815   3.206   14.445  1.00 33.93  ? 88  LEU A CG  1 
ATOM   705  C CD1 . LEU A 1 88  ? 2.524   4.228   13.578  1.00 39.33  ? 88  LEU A CD1 1 
ATOM   706  C CD2 . LEU A 1 88  ? 2.296   3.411   15.877  1.00 32.57  ? 88  LEU A CD2 1 
ATOM   707  N N   . ASP A 1 89  ? -2.844  2.729   14.040  1.00 36.95  ? 89  ASP A N   1 
ATOM   708  C CA  . ASP A 1 89  ? -4.264  3.050   14.132  1.00 41.94  ? 89  ASP A CA  1 
ATOM   709  C C   . ASP A 1 89  ? -4.924  2.271   15.262  1.00 41.70  ? 89  ASP A C   1 
ATOM   710  O O   . ASP A 1 89  ? -5.737  2.821   16.010  1.00 39.67  ? 89  ASP A O   1 
ATOM   711  C CB  . ASP A 1 89  ? -4.987  2.748   12.814  1.00 40.12  ? 89  ASP A CB  1 
ATOM   712  C CG  . ASP A 1 89  ? -4.715  3.779   11.714  1.00 44.76  ? 89  ASP A CG  1 
ATOM   713  O OD1 . ASP A 1 89  ? -3.855  4.670   11.889  1.00 42.74  ? 89  ASP A OD1 1 
ATOM   714  O OD2 . ASP A 1 89  ? -5.364  3.667   10.643  1.00 45.28  ? 89  ASP A OD2 1 
ATOM   715  N N   . VAL A 1 90  ? -4.626  0.973   15.364  1.00 41.23  ? 90  VAL A N   1 
ATOM   716  C CA  . VAL A 1 90  ? -5.312  0.130   16.338  1.00 44.91  ? 90  VAL A CA  1 
ATOM   717  C C   . VAL A 1 90  ? -4.858  0.487   17.754  1.00 41.88  ? 90  VAL A C   1 
ATOM   718  O O   . VAL A 1 90  ? -5.660  0.541   18.694  1.00 42.09  ? 90  VAL A O   1 
ATOM   719  C CB  . VAL A 1 90  ? -5.078  -1.355  15.998  1.00 39.57  ? 90  VAL A CB  1 
ATOM   720  C CG1 . VAL A 1 90  ? -5.248  -2.235  17.216  1.00 46.56  ? 90  VAL A CG1 1 
ATOM   721  C CG2 . VAL A 1 90  ? -6.016  -1.794  14.882  1.00 46.42  ? 90  VAL A CG2 1 
ATOM   722  N N   . LEU A 1 91  ? -3.570  0.777   17.919  1.00 36.00  ? 91  LEU A N   1 
ATOM   723  C CA  . LEU A 1 91  ? -3.022  1.188   19.200  1.00 36.34  ? 91  LEU A CA  1 
ATOM   724  C C   . LEU A 1 91  ? -3.529  2.554   19.650  1.00 38.36  ? 91  LEU A C   1 
ATOM   725  O O   . LEU A 1 91  ? -3.305  2.929   20.812  1.00 36.94  ? 91  LEU A O   1 
ATOM   726  C CB  . LEU A 1 91  ? -1.498  1.193   19.098  1.00 30.82  ? 91  LEU A CB  1 
ATOM   727  C CG  . LEU A 1 91  ? -0.917  -0.198  18.874  1.00 35.85  ? 91  LEU A CG  1 
ATOM   728  C CD1 . LEU A 1 91  ? 0.571   -0.101  18.552  1.00 41.01  ? 91  LEU A CD1 1 
ATOM   729  C CD2 . LEU A 1 91  ? -1.135  -1.050  20.119  1.00 41.46  ? 91  LEU A CD2 1 
ATOM   730  N N   . GLY A 1 92  ? -4.189  3.309   18.773  1.00 36.19  ? 92  GLY A N   1 
ATOM   731  C CA  . GLY A 1 92  ? -4.650  4.633   19.138  1.00 37.43  ? 92  GLY A CA  1 
ATOM   732  C C   . GLY A 1 92  ? -3.591  5.714   19.099  1.00 41.67  ? 92  GLY A C   1 
ATOM   733  O O   . GLY A 1 92  ? -3.757  6.754   19.757  1.00 36.69  ? 92  GLY A O   1 
ATOM   734  N N   . ILE A 1 93  ? -2.496  5.508   18.358  1.00 34.56  ? 93  ILE A N   1 
ATOM   735  C CA  . ILE A 1 93  ? -1.406  6.482   18.286  1.00 34.13  ? 93  ILE A CA  1 
ATOM   736  C C   . ILE A 1 93  ? -1.403  7.095   16.892  1.00 36.22  ? 93  ILE A C   1 
ATOM   737  O O   . ILE A 1 93  ? -1.098  6.412   15.905  1.00 34.14  ? 93  ILE A O   1 
ATOM   738  C CB  . ILE A 1 93  ? -0.050  5.848   18.615  1.00 32.61  ? 93  ILE A CB  1 
ATOM   739  C CG1 . ILE A 1 93  ? -0.008  5.392   20.076  1.00 26.99  ? 93  ILE A CG1 1 
ATOM   740  C CG2 . ILE A 1 93  ? 1.093   6.813   18.335  1.00 32.15  ? 93  ILE A CG2 1 
ATOM   741  C CD1 . ILE A 1 93  ? 1.126   4.411   20.319  1.00 28.72  ? 93  ILE A CD1 1 
ATOM   742  N N   . GLN A 1 94  ? -1.715  8.391   16.822  1.00 29.52  ? 94  GLN A N   1 
ATOM   743  C CA  . GLN A 1 94  ? -1.608  9.168   15.589  1.00 35.29  ? 94  GLN A CA  1 
ATOM   744  C C   . GLN A 1 94  ? -0.205  9.772   15.518  1.00 37.23  ? 94  GLN A C   1 
ATOM   745  O O   . GLN A 1 94  ? 0.101   10.741  16.224  1.00 34.79  ? 94  GLN A O   1 
ATOM   746  C CB  . GLN A 1 94  ? -2.676  10.257  15.548  1.00 35.29  ? 94  GLN A CB  1 
ATOM   747  C CG  . GLN A 1 94  ? -2.599  11.149  14.288  1.00 38.09  ? 94  GLN A CG  1 
ATOM   748  C CD  . GLN A 1 94  ? -3.946  11.692  13.892  1.00 49.07  ? 94  GLN A CD  1 
ATOM   749  O OE1 . GLN A 1 94  ? -4.824  10.942  13.476  1.00 46.21  ? 94  GLN A OE1 1 
ATOM   750  N NE2 . GLN A 1 94  ? -4.129  13.005  14.030  1.00 52.40  ? 94  GLN A NE2 1 
ATOM   751  N N   . LYS A 1 95  ? 0.648   9.207   14.656  1.00 37.94  ? 95  LYS A N   1 
ATOM   752  C CA  . LYS A 1 95  ? 2.036   9.661   14.594  1.00 36.14  ? 95  LYS A CA  1 
ATOM   753  C C   . LYS A 1 95  ? 2.162   11.068  14.008  1.00 42.49  ? 95  LYS A C   1 
ATOM   754  O O   . LYS A 1 95  ? 3.088   11.800  14.381  1.00 40.26  ? 95  LYS A O   1 
ATOM   755  C CB  . LYS A 1 95  ? 2.865   8.660   13.791  1.00 36.33  ? 95  LYS A CB  1 
ATOM   756  C CG  . LYS A 1 95  ? 4.362   8.913   13.799  1.00 33.10  ? 95  LYS A CG  1 
ATOM   757  C CD  . LYS A 1 95  ? 5.098   7.747   13.080  1.00 41.72  ? 95  LYS A CD  1 
ATOM   758  C CE  . LYS A 1 95  ? 6.609   7.945   13.008  1.00 33.19  ? 95  LYS A CE  1 
ATOM   759  N NZ  . LYS A 1 95  ? 6.956   9.125   12.110  1.00 33.29  ? 95  LYS A NZ  1 
ATOM   760  N N   . GLU A 1 96  ? 1.252   11.447  13.102  1.00 35.04  ? 96  GLU A N   1 
ATOM   761  C CA  . GLU A 1 96  ? 1.204   12.710  12.356  1.00 43.69  ? 96  GLU A CA  1 
ATOM   762  C C   . GLU A 1 96  ? 2.230   12.752  11.219  1.00 49.85  ? 96  GLU A C   1 
ATOM   763  O O   . GLU A 1 96  ? 3.237   12.039  11.245  1.00 46.68  ? 96  GLU A O   1 
ATOM   764  C CB  . GLU A 1 96  ? 1.393   13.906  13.286  1.00 45.28  ? 96  GLU A CB  1 
ATOM   765  C CG  . GLU A 1 96  ? 0.286   14.112  14.343  1.00 44.86  ? 96  GLU A CG  1 
ATOM   766  C CD  . GLU A 1 96  ? -1.080  14.513  13.794  1.00 60.81  ? 96  GLU A CD  1 
ATOM   767  O OE1 . GLU A 1 96  ? -1.308  14.415  12.563  1.00 54.11  ? 96  GLU A OE1 1 
ATOM   768  O OE2 . GLU A 1 96  ? -1.930  14.941  14.615  1.00 54.27  ? 96  GLU A OE2 1 
ATOM   769  N N   . GLU A 1 97  ? 1.971   13.583  10.206  1.00 52.24  ? 97  GLU A N   1 
ATOM   770  C CA  . GLU A 1 97  ? 2.855   13.744  9.045   1.00 54.86  ? 97  GLU A CA  1 
ATOM   771  C C   . GLU A 1 97  ? 3.063   12.435  8.283   1.00 51.64  ? 97  GLU A C   1 
ATOM   772  O O   . GLU A 1 97  ? 4.074   12.262  7.592   1.00 53.85  ? 97  GLU A O   1 
ATOM   773  C CB  . GLU A 1 97  ? 4.215   14.329  9.437   1.00 60.41  ? 97  GLU A CB  1 
ATOM   774  C CG  . GLU A 1 97  ? 4.181   15.760  9.911   1.00 71.29  ? 97  GLU A CG  1 
ATOM   775  C CD  . GLU A 1 97  ? 5.572   16.365  9.951   1.00 92.34  ? 97  GLU A CD  1 
ATOM   776  O OE1 . GLU A 1 97  ? 6.541   15.629  9.655   1.00 92.21  ? 97  GLU A OE1 1 
ATOM   777  O OE2 . GLU A 1 97  ? 5.698   17.563  10.287  1.00 100.32 ? 97  GLU A OE2 1 
ATOM   778  N N   . MET A 1 98  ? 2.117   11.503  8.387   1.00 51.09  ? 98  MET A N   1 
ATOM   779  C CA  . MET A 1 98  ? 2.250   10.224  7.705   1.00 46.49  ? 98  MET A CA  1 
ATOM   780  C C   . MET A 1 98  ? 2.002   10.363  6.201   1.00 55.15  ? 98  MET A C   1 
ATOM   781  O O   . MET A 1 98  ? 2.316   9.443   5.425   1.00 47.42  ? 98  MET A O   1 
ATOM   782  C CB  . MET A 1 98  ? 1.270   9.230   8.333   1.00 46.32  ? 98  MET A CB  1 
ATOM   783  C CG  . MET A 1 98  ? 1.830   8.289   9.414   1.00 50.05  ? 98  MET A CG  1 
ATOM   784  S SD  . MET A 1 98  ? 3.584   7.890   9.294   1.00 49.65  ? 98  MET A SD  1 
ATOM   785  C CE  . MET A 1 98  ? 3.423   6.423   8.270   1.00 54.41  ? 98  MET A CE  1 
ATOM   786  N N   . ASN A 1 99  ? 1.451   11.502  5.771   1.00 46.02  ? 99  ASN A N   1 
ATOM   787  C CA  . ASN A 1 99  ? 1.358   11.838  4.359   1.00 54.45  ? 99  ASN A CA  1 
ATOM   788  C C   . ASN A 1 99  ? 2.643   12.445  3.832   1.00 51.35  ? 99  ASN A C   1 
ATOM   789  O O   . ASN A 1 99  ? 2.747   12.681  2.629   1.00 55.67  ? 99  ASN A O   1 
ATOM   790  C CB  . ASN A 1 99  ? 0.203   12.814  4.134   1.00 56.39  ? 99  ASN A CB  1 
ATOM   791  C CG  . ASN A 1 99  ? 0.365   14.078  4.959   1.00 57.31  ? 99  ASN A CG  1 
ATOM   792  O OD1 . ASN A 1 99  ? 0.569   14.012  6.174   1.00 60.31  ? 99  ASN A OD1 1 
ATOM   793  N ND2 . ASN A 1 99  ? 0.267   15.231  4.310   1.00 66.20  ? 99  ASN A ND2 1 
ATOM   794  N N   . HIS A 1 100 ? 3.607   12.720  4.708   1.00 52.96  ? 100 HIS A N   1 
ATOM   795  C CA  . HIS A 1 100 ? 4.962   13.096  4.308   1.00 56.95  ? 100 HIS A CA  1 
ATOM   796  C C   . HIS A 1 100 ? 5.967   12.229  5.060   1.00 52.50  ? 100 HIS A C   1 
ATOM   797  O O   . HIS A 1 100 ? 6.748   12.722  5.884   1.00 48.87  ? 100 HIS A O   1 
ATOM   798  C CB  . HIS A 1 100 ? 5.183   14.584  4.575   1.00 56.57  ? 100 HIS A CB  1 
ATOM   799  C CG  . HIS A 1 100 ? 4.287   15.468  3.768   1.00 62.04  ? 100 HIS A CG  1 
ATOM   800  N ND1 . HIS A 1 100 ? 3.750   16.638  4.263   1.00 66.73  ? 100 HIS A ND1 1 
ATOM   801  C CD2 . HIS A 1 100 ? 3.870   15.379  2.481   1.00 63.09  ? 100 HIS A CD2 1 
ATOM   802  C CE1 . HIS A 1 100 ? 3.011   17.211  3.329   1.00 62.83  ? 100 HIS A CE1 1 
ATOM   803  N NE2 . HIS A 1 100 ? 3.072   16.471  2.237   1.00 66.17  ? 100 HIS A NE2 1 
ATOM   804  N N   . PRO A 1 101 ? 5.942   10.913  4.834   1.00 54.02  ? 101 PRO A N   1 
ATOM   805  C CA  . PRO A 1 101 ? 6.827   10.009  5.579   1.00 42.73  ? 101 PRO A CA  1 
ATOM   806  C C   . PRO A 1 101 ? 8.209   9.871   4.966   1.00 44.92  ? 101 PRO A C   1 
ATOM   807  O O   . PRO A 1 101 ? 8.930   8.942   5.339   1.00 39.85  ? 101 PRO A O   1 
ATOM   808  C CB  . PRO A 1 101 ? 6.075   8.674   5.492   1.00 44.35  ? 101 PRO A CB  1 
ATOM   809  C CG  . PRO A 1 101 ? 5.519   8.715   4.059   1.00 48.70  ? 101 PRO A CG  1 
ATOM   810  C CD  . PRO A 1 101 ? 5.100   10.170  3.865   1.00 52.65  ? 101 PRO A CD  1 
ATOM   811  N N   . ASP A 1 102 ? 8.549   10.780  4.040   1.00 48.61  ? 102 ASP A N   1 
ATOM   812  C CA  . ASP A 1 102 ? 9.687   10.627  3.132   1.00 47.53  ? 102 ASP A CA  1 
ATOM   813  C C   . ASP A 1 102 ? 10.972  10.249  3.856   1.00 45.92  ? 102 ASP A C   1 
ATOM   814  O O   . ASP A 1 102 ? 11.722  9.378   3.396   1.00 50.72  ? 102 ASP A O   1 
ATOM   815  C CB  . ASP A 1 102 ? 9.890   11.928  2.358   1.00 57.81  ? 102 ASP A CB  1 
ATOM   816  C CG  . ASP A 1 102 ? 8.651   12.343  1.589   1.00 62.31  ? 102 ASP A CG  1 
ATOM   817  O OD1 . ASP A 1 102 ? 7.635   12.685  2.245   1.00 62.32  ? 102 ASP A OD1 1 
ATOM   818  O OD2 . ASP A 1 102 ? 8.697   12.324  0.346   1.00 63.90  ? 102 ASP A OD2 1 
ATOM   819  N N   . ARG A 1 103 ? 11.256  10.911  4.973   1.00 45.44  ? 103 ARG A N   1 
ATOM   820  C CA  . ARG A 1 103 ? 12.465  10.679  5.742   1.00 48.11  ? 103 ARG A CA  1 
ATOM   821  C C   . ARG A 1 103 ? 12.230  9.880   7.018   1.00 43.17  ? 103 ARG A C   1 
ATOM   822  O O   . ARG A 1 103 ? 13.174  9.708   7.791   1.00 42.44  ? 103 ARG A O   1 
ATOM   823  C CB  . ARG A 1 103 ? 13.122  12.016  6.096   1.00 53.46  ? 103 ARG A CB  1 
ATOM   824  C CG  . ARG A 1 103 ? 13.108  13.016  4.948   1.00 61.99  ? 103 ARG A CG  1 
ATOM   825  C CD  . ARG A 1 103 ? 13.870  14.286  5.278   1.00 66.39  ? 103 ARG A CD  1 
ATOM   826  N NE  . ARG A 1 103 ? 13.030  15.469  5.111   1.00 87.29  ? 103 ARG A NE  1 
ATOM   827  C CZ  . ARG A 1 103 ? 12.598  15.939  3.944   1.00 90.71  ? 103 ARG A CZ  1 
ATOM   828  N NH1 . ARG A 1 103 ? 12.877  15.330  2.801   1.00 83.01  ? 103 ARG A NH1 1 
ATOM   829  N NH2 . ARG A 1 103 ? 11.853  17.042  3.925   1.00 86.29  ? 103 ARG A NH2 1 
ATOM   830  N N   . HIS A 1 104 ? 11.010  9.373   7.251   1.00 42.59  ? 104 HIS A N   1 
ATOM   831  C CA  . HIS A 1 104 ? 10.639  8.797   8.542   1.00 38.75  ? 104 HIS A CA  1 
ATOM   832  C C   . HIS A 1 104 ? 10.280  7.315   8.489   1.00 41.83  ? 104 HIS A C   1 
ATOM   833  O O   . HIS A 1 104 ? 9.902   6.753   9.519   1.00 39.31  ? 104 HIS A O   1 
ATOM   834  C CB  . HIS A 1 104 ? 9.457   9.570   9.140   1.00 42.00  ? 104 HIS A CB  1 
ATOM   835  C CG  . HIS A 1 104 ? 9.756   11.013  9.397   1.00 43.31  ? 104 HIS A CG  1 
ATOM   836  N ND1 . HIS A 1 104 ? 11.036  11.480  9.621   1.00 53.28  ? 104 HIS A ND1 1 
ATOM   837  C CD2 . HIS A 1 104 ? 8.945   12.096  9.449   1.00 48.84  ? 104 HIS A CD2 1 
ATOM   838  C CE1 . HIS A 1 104 ? 11.000  12.787  9.809   1.00 48.80  ? 104 HIS A CE1 1 
ATOM   839  N NE2 . HIS A 1 104 ? 9.744   13.186  9.704   1.00 57.41  ? 104 HIS A NE2 1 
ATOM   840  N N   . ILE A 1 105 ? 10.345  6.681   7.325   1.00 43.01  ? 105 ILE A N   1 
ATOM   841  C CA  . ILE A 1 105 ? 10.249  5.231   7.189   1.00 42.24  ? 105 ILE A CA  1 
ATOM   842  C C   . ILE A 1 105 ? 11.567  4.760   6.594   1.00 39.31  ? 105 ILE A C   1 
ATOM   843  O O   . ILE A 1 105 ? 11.921  5.153   5.482   1.00 41.25  ? 105 ILE A O   1 
ATOM   844  C CB  . ILE A 1 105 ? 9.069   4.809   6.300   1.00 41.48  ? 105 ILE A CB  1 
ATOM   845  C CG1 . ILE A 1 105 ? 7.740   5.368   6.836   1.00 43.10  ? 105 ILE A CG1 1 
ATOM   846  C CG2 . ILE A 1 105 ? 9.028   3.298   6.184   1.00 39.91  ? 105 ILE A CG2 1 
ATOM   847  C CD1 . ILE A 1 105 ? 6.523   5.017   5.943   1.00 42.07  ? 105 ILE A CD1 1 
ATOM   848  N N   . ILE A 1 106 ? 12.314  3.966   7.351   1.00 40.17  ? 106 ILE A N   1 
ATOM   849  C CA  . ILE A 1 106 ? 13.640  3.503   6.948   1.00 43.00  ? 106 ILE A CA  1 
ATOM   850  C C   . ILE A 1 106 ? 13.531  2.038   6.572   1.00 44.65  ? 106 ILE A C   1 
ATOM   851  O O   . ILE A 1 106 ? 13.038  1.222   7.364   1.00 42.22  ? 106 ILE A O   1 
ATOM   852  C CB  . ILE A 1 106 ? 14.671  3.701   8.071   1.00 43.51  ? 106 ILE A CB  1 
ATOM   853  C CG1 . ILE A 1 106 ? 14.535  5.103   8.675   1.00 40.88  ? 106 ILE A CG1 1 
ATOM   854  C CG2 . ILE A 1 106 ? 16.069  3.488   7.526   1.00 44.38  ? 106 ILE A CG2 1 
ATOM   855  C CD1 . ILE A 1 106 ? 14.769  6.212   7.668   1.00 40.33  ? 106 ILE A CD1 1 
ATOM   856  N N   . ILE A 1 107 ? 14.002  1.699   5.377   1.00 48.79  ? 107 ILE A N   1 
ATOM   857  C CA  . ILE A 1 107 ? 13.762  0.385   4.792   1.00 52.33  ? 107 ILE A CA  1 
ATOM   858  C C   . ILE A 1 107 ? 15.096  -0.318  4.582   1.00 56.02  ? 107 ILE A C   1 
ATOM   859  O O   . ILE A 1 107 ? 15.978  0.193   3.880   1.00 51.36  ? 107 ILE A O   1 
ATOM   860  C CB  . ILE A 1 107 ? 12.953  0.501   3.491   1.00 48.81  ? 107 ILE A CB  1 
ATOM   861  C CG1 . ILE A 1 107 ? 11.597  1.138   3.834   1.00 50.43  ? 107 ILE A CG1 1 
ATOM   862  C CG2 . ILE A 1 107 ? 12.785  -0.859  2.835   1.00 51.63  ? 107 ILE A CG2 1 
ATOM   863  C CD1 . ILE A 1 107 ? 10.827  1.673   2.667   1.00 52.79  ? 107 ILE A CD1 1 
ATOM   864  N N   . SER A 1 108 ? 15.249  -1.474  5.227   1.00 57.78  ? 108 SER A N   1 
ATOM   865  C CA  . SER A 1 108 ? 16.372  -2.380  5.016   1.00 56.97  ? 108 SER A CA  1 
ATOM   866  C C   . SER A 1 108 ? 15.773  -3.756  4.756   1.00 56.66  ? 108 SER A C   1 
ATOM   867  O O   . SER A 1 108 ? 14.811  -3.857  3.993   1.00 58.45  ? 108 SER A O   1 
ATOM   868  C CB  . SER A 1 108 ? 17.311  -2.360  6.224   1.00 56.32  ? 108 SER A CB  1 
ATOM   869  O OG  . SER A 1 108 ? 16.624  -2.742  7.400   1.00 53.54  ? 108 SER A OG  1 
ATOM   870  N N   . ASP A 1 109 ? 16.283  -4.816  5.389   1.00 59.49  ? 109 ASP A N   1 
ATOM   871  C CA  . ASP A 1 109 ? 15.514  -6.059  5.413   1.00 57.66  ? 109 ASP A CA  1 
ATOM   872  C C   . ASP A 1 109 ? 14.233  -5.901  6.227   1.00 63.23  ? 109 ASP A C   1 
ATOM   873  O O   . ASP A 1 109 ? 13.286  -6.674  6.043   1.00 62.20  ? 109 ASP A O   1 
ATOM   874  C CB  . ASP A 1 109 ? 16.353  -7.210  5.967   1.00 61.50  ? 109 ASP A CB  1 
ATOM   875  N N   . ARG A 1 110 ? 14.193  -4.915  7.121   1.00 48.44  ? 110 ARG A N   1 
ATOM   876  C CA  . ARG A 1 110 ? 13.036  -4.608  7.945   1.00 48.68  ? 110 ARG A CA  1 
ATOM   877  C C   . ARG A 1 110 ? 12.568  -3.180  7.677   1.00 52.60  ? 110 ARG A C   1 
ATOM   878  O O   . ARG A 1 110 ? 13.186  -2.423  6.916   1.00 51.52  ? 110 ARG A O   1 
ATOM   879  C CB  . ARG A 1 110 ? 13.364  -4.800  9.430   1.00 50.52  ? 110 ARG A CB  1 
ATOM   880  C CG  . ARG A 1 110 ? 14.622  -4.063  9.854   1.00 46.74  ? 110 ARG A CG  1 
ATOM   881  C CD  . ARG A 1 110 ? 14.691  -3.912  11.371  1.00 45.78  ? 110 ARG A CD  1 
ATOM   882  N NE  . ARG A 1 110 ? 15.876  -3.161  11.769  1.00 51.03  ? 110 ARG A NE  1 
ATOM   883  C CZ  . ARG A 1 110 ? 16.095  -2.700  12.993  1.00 51.59  ? 110 ARG A CZ  1 
ATOM   884  N NH1 . ARG A 1 110 ? 15.204  -2.859  13.956  1.00 50.49  ? 110 ARG A NH1 1 
ATOM   885  N NH2 . ARG A 1 110 ? 17.242  -2.081  13.258  1.00 47.89  ? 110 ARG A NH2 1 
ATOM   886  N N   . ILE A 1 111 ? 11.439  -2.829  8.287   1.00 43.95  ? 111 ILE A N   1 
ATOM   887  C CA  . ILE A 1 111 ? 10.803  -1.529  8.111   1.00 41.41  ? 111 ILE A CA  1 
ATOM   888  C C   . ILE A 1 111 ? 10.764  -0.885  9.485   1.00 37.93  ? 111 ILE A C   1 
ATOM   889  O O   . ILE A 1 111 ? 10.194  -1.464  10.416  1.00 37.83  ? 111 ILE A O   1 
ATOM   890  C CB  . ILE A 1 111 ? 9.375   -1.660  7.553   1.00 42.73  ? 111 ILE A CB  1 
ATOM   891  C CG1 . ILE A 1 111 ? 9.349   -2.406  6.219   1.00 48.80  ? 111 ILE A CG1 1 
ATOM   892  C CG2 . ILE A 1 111 ? 8.724   -0.271  7.404   1.00 41.44  ? 111 ILE A CG2 1 
ATOM   893  C CD1 . ILE A 1 111 ? 10.268  -1.867  5.174   1.00 59.98  ? 111 ILE A CD1 1 
ATOM   894  N N   . VAL A 1 112 ? 11.377  0.291   9.635   1.00 36.25  ? 112 VAL A N   1 
ATOM   895  C CA  . VAL A 1 112 ? 11.364  1.004   10.912  1.00 34.55  ? 112 VAL A CA  1 
ATOM   896  C C   . VAL A 1 112 ? 10.754  2.391   10.715  1.00 34.31  ? 112 VAL A C   1 
ATOM   897  O O   . VAL A 1 112 ? 11.137  3.123   9.791   1.00 38.14  ? 112 VAL A O   1 
ATOM   898  C CB  . VAL A 1 112 ? 12.780  1.103   11.520  1.00 33.02  ? 112 VAL A CB  1 
ATOM   899  C CG1 . VAL A 1 112 ? 12.715  1.751   12.902  1.00 32.98  ? 112 VAL A CG1 1 
ATOM   900  C CG2 . VAL A 1 112 ? 13.410  -0.291  11.609  1.00 36.38  ? 112 VAL A CG2 1 
ATOM   901  N N   . PHE A 1 113 ? 9.806   2.742   11.575  1.00 30.86  ? 113 PHE A N   1 
ATOM   902  C CA  . PHE A 1 113 ? 9.281   4.098   11.650  1.00 32.38  ? 113 PHE A CA  1 
ATOM   903  C C   . PHE A 1 113 ? 10.079  4.909   12.683  1.00 32.54  ? 113 PHE A C   1 
ATOM   904  O O   . PHE A 1 113 ? 10.380  4.431   13.785  1.00 30.72  ? 113 PHE A O   1 
ATOM   905  C CB  . PHE A 1 113 ? 7.803   4.064   12.045  1.00 31.19  ? 113 PHE A CB  1 
ATOM   906  C CG  . PHE A 1 113 ? 6.859   3.697   10.925  1.00 39.48  ? 113 PHE A CG  1 
ATOM   907  C CD1 . PHE A 1 113 ? 7.253   2.862   9.888   1.00 34.92  ? 113 PHE A CD1 1 
ATOM   908  C CD2 . PHE A 1 113 ? 5.547   4.149   10.951  1.00 40.04  ? 113 PHE A CD2 1 
ATOM   909  C CE1 . PHE A 1 113 ? 6.370   2.523   8.879   1.00 39.43  ? 113 PHE A CE1 1 
ATOM   910  C CE2 . PHE A 1 113 ? 4.667   3.820   9.938   1.00 41.55  ? 113 PHE A CE2 1 
ATOM   911  C CZ  . PHE A 1 113 ? 5.078   3.004   8.900   1.00 37.67  ? 113 PHE A CZ  1 
ATOM   912  N N   . ILE A 1 114 ? 10.421  6.149   12.334  1.00 32.16  ? 114 ILE A N   1 
ATOM   913  C CA  . ILE A 1 114 ? 11.127  7.013   13.278  1.00 33.53  ? 114 ILE A CA  1 
ATOM   914  C C   . ILE A 1 114 ? 10.415  8.358   13.374  1.00 35.92  ? 114 ILE A C   1 
ATOM   915  O O   . ILE A 1 114 ? 9.594   8.711   12.523  1.00 31.66  ? 114 ILE A O   1 
ATOM   916  C CB  . ILE A 1 114 ? 12.610  7.210   12.889  1.00 35.08  ? 114 ILE A CB  1 
ATOM   917  C CG1 . ILE A 1 114 ? 12.711  7.896   11.526  1.00 36.91  ? 114 ILE A CG1 1 
ATOM   918  C CG2 . ILE A 1 114 ? 13.353  5.879   12.871  1.00 37.06  ? 114 ILE A CG2 1 
ATOM   919  C CD1 . ILE A 1 114 ? 14.116  8.329   11.170  1.00 36.54  ? 114 ILE A CD1 1 
ATOM   920  N N   . ASP A 1 115 ? 10.748  9.103   14.447  1.00 31.52  ? 115 ASP A N   1 
ATOM   921  C CA  . ASP A 1 115 ? 10.283  10.463  14.726  1.00 34.16  ? 115 ASP A CA  1 
ATOM   922  C C   . ASP A 1 115 ? 8.840   10.499  15.232  1.00 37.86  ? 115 ASP A C   1 
ATOM   923  O O   . ASP A 1 115 ? 7.897   10.704  14.447  1.00 33.72  ? 115 ASP A O   1 
ATOM   924  C CB  . ASP A 1 115 ? 10.444  11.349  13.480  1.00 38.02  ? 115 ASP A CB  1 
ATOM   925  C CG  . ASP A 1 115 ? 10.044  12.799  13.734  1.00 52.88  ? 115 ASP A CG  1 
ATOM   926  O OD1 . ASP A 1 115 ? 9.994   13.188  14.913  1.00 50.08  ? 115 ASP A OD1 1 
ATOM   927  O OD2 . ASP A 1 115 ? 9.803   13.556  12.768  1.00 58.75  ? 115 ASP A OD2 1 
ATOM   928  N N   . PHE A 1 116 ? 8.655   10.337  16.550  1.00 27.52  ? 116 PHE A N   1 
ATOM   929  C CA  . PHE A 1 116 ? 7.324   10.340  17.156  1.00 29.89  ? 116 PHE A CA  1 
ATOM   930  C C   . PHE A 1 116 ? 6.996   11.618  17.949  1.00 33.65  ? 116 PHE A C   1 
ATOM   931  O O   . PHE A 1 116 ? 6.011   11.626  18.692  1.00 31.76  ? 116 PHE A O   1 
ATOM   932  C CB  . PHE A 1 116 ? 7.185   9.087   18.036  1.00 32.39  ? 116 PHE A CB  1 
ATOM   933  C CG  . PHE A 1 116 ? 7.005   7.810   17.233  1.00 31.26  ? 116 PHE A CG  1 
ATOM   934  C CD1 . PHE A 1 116 ? 8.118   7.138   16.723  1.00 32.63  ? 116 PHE A CD1 1 
ATOM   935  C CD2 . PHE A 1 116 ? 5.734   7.325   16.942  1.00 34.75  ? 116 PHE A CD2 1 
ATOM   936  C CE1 . PHE A 1 116 ? 7.960   5.959   15.954  1.00 33.96  ? 116 PHE A CE1 1 
ATOM   937  C CE2 . PHE A 1 116 ? 5.559   6.162   16.164  1.00 30.18  ? 116 PHE A CE2 1 
ATOM   938  C CZ  . PHE A 1 116 ? 6.679   5.480   15.679  1.00 31.04  ? 116 PHE A CZ  1 
ATOM   939  N N   . GLU A 1 117 ? 7.764   12.706  17.780  1.00 34.52  ? 117 GLU A N   1 
ATOM   940  C CA  . GLU A 1 117 ? 7.680   13.893  18.660  1.00 36.25  ? 117 GLU A CA  1 
ATOM   941  C C   . GLU A 1 117 ? 6.425   14.760  18.454  1.00 38.53  ? 117 GLU A C   1 
ATOM   942  O O   . GLU A 1 117 ? 6.033   15.475  19.394  1.00 36.58  ? 117 GLU A O   1 
ATOM   943  C CB  . GLU A 1 117 ? 8.934   14.758  18.455  1.00 34.97  ? 117 GLU A CB  1 
ATOM   944  C CG  . GLU A 1 117 ? 9.253   15.022  17.043  1.00 43.09  ? 117 GLU A CG  1 
ATOM   945  C CD  . GLU A 1 117 ? 9.852   16.365  16.796  1.00 59.36  ? 117 GLU A CD  1 
ATOM   946  O OE1 . GLU A 1 117 ? 9.251   17.373  17.236  1.00 56.02  ? 117 GLU A OE1 1 
ATOM   947  O OE2 . GLU A 1 117 ? 10.923  16.409  16.158  1.00 61.57  ? 117 GLU A OE2 1 
ATOM   948  N N   . ARG A 1 118 ? 5.680   14.367  17.420  1.00 35.40  ? 118 ARG A N   1 
ATOM   949  C CA  . ARG A 1 118 ? 4.366   14.994  17.169  1.00 33.52  ? 118 ARG A CA  1 
ATOM   950  C C   . ARG A 1 118 ? 3.250   13.955  17.380  1.00 37.79  ? 118 ARG A C   1 
ATOM   951  O O   . ARG A 1 118 ? 2.113   14.300  17.047  1.00 36.28  ? 118 ARG A O   1 
ATOM   952  C CB  . ARG A 1 118 ? 4.344   15.569  15.752  1.00 47.05  ? 118 ARG A CB  1 
ATOM   953  C CG  . ARG A 1 118 ? 5.481   16.532  15.448  1.00 53.24  ? 118 ARG A CG  1 
ATOM   954  C CD  . ARG A 1 118 ? 5.415   17.013  14.013  1.00 67.53  ? 118 ARG A CD  1 
ATOM   955  N NE  . ARG A 1 118 ? 6.679   17.576  13.567  1.00 83.78  ? 118 ARG A NE  1 
ATOM   956  C CZ  . ARG A 1 118 ? 7.334   18.543  14.197  1.00 89.91  ? 118 ARG A CZ  1 
ATOM   957  N NH1 . ARG A 1 118 ? 6.740   19.699  14.433  1.00 81.93  ? 118 ARG A NH1 1 
ATOM   958  N NH2 . ARG A 1 118 ? 8.584   18.352  14.585  1.00 82.24  ? 118 ARG A NH2 1 
ATOM   959  N N   . GLY A 1 119 ? 3.533   12.751  17.927  1.00 34.07  ? 119 GLY A N   1 
ATOM   960  C CA  . GLY A 1 119 ? 2.479   11.815  18.125  1.00 36.25  ? 119 GLY A CA  1 
ATOM   961  C C   . GLY A 1 119 ? 1.445   12.391  19.065  1.00 39.49  ? 119 GLY A C   1 
ATOM   962  O O   . GLY A 1 119 ? 1.753   13.228  19.914  1.00 33.84  ? 119 GLY A O   1 
ATOM   963  N N   . VAL A 1 120 ? 0.194   11.953  18.881  1.00 34.25  ? 120 VAL A N   1 
ATOM   964  C CA  . VAL A 1 120 ? -0.892  12.207  19.826  1.00 40.64  ? 120 VAL A CA  1 
ATOM   965  C C   . VAL A 1 120 ? -1.765  10.963  19.919  1.00 41.19  ? 120 VAL A C   1 
ATOM   966  O O   . VAL A 1 120 ? -1.849  10.171  18.977  1.00 36.23  ? 120 VAL A O   1 
ATOM   967  C CB  . VAL A 1 120 ? -1.774  13.421  19.451  1.00 42.93  ? 120 VAL A CB  1 
ATOM   968  C CG1 . VAL A 1 120 ? -1.043  14.737  19.529  1.00 43.99  ? 120 VAL A CG1 1 
ATOM   969  C CG2 . VAL A 1 120 ? -2.400  13.235  18.060  1.00 41.77  ? 120 VAL A CG2 1 
ATOM   970  N N   . ILE A 1 121 ? -2.477  10.836  21.045  1.00 33.15  ? 121 ILE A N   1 
ATOM   971  C CA  . ILE A 1 121 ? -3.431  9.739   21.233  1.00 36.07  ? 121 ILE A CA  1 
ATOM   972  C C   . ILE A 1 121 ? -4.750  10.113  20.565  1.00 39.72  ? 121 ILE A C   1 
ATOM   973  O O   . ILE A 1 121 ? -5.223  11.245  20.710  1.00 41.72  ? 121 ILE A O   1 
ATOM   974  C CB  . ILE A 1 121 ? -3.625  9.431   22.733  1.00 35.61  ? 121 ILE A CB  1 
ATOM   975  C CG1 . ILE A 1 121 ? -2.324  8.888   23.344  1.00 38.20  ? 121 ILE A CG1 1 
ATOM   976  C CG2 . ILE A 1 121 ? -4.792  8.454   22.938  1.00 34.20  ? 121 ILE A CG2 1 
ATOM   977  C CD1 . ILE A 1 121 ? -2.401  8.515   24.847  1.00 36.79  ? 121 ILE A CD1 1 
ATOM   978  N N   . LYS A 1 122 ? -5.348  9.183   19.803  1.00 41.26  ? 122 LYS A N   1 
ATOM   979  C CA  . LYS A 1 122 ? -6.670  9.438   19.220  1.00 36.90  ? 122 LYS A CA  1 
ATOM   980  C C   . LYS A 1 122 ? -7.466  8.148   19.097  1.00 40.58  ? 122 LYS A C   1 
ATOM   981  O O   . LYS A 1 122 ? -6.900  7.077   18.858  1.00 36.38  ? 122 LYS A O   1 
ATOM   982  C CB  . LYS A 1 122 ? -6.591  10.034  17.803  1.00 47.32  ? 122 LYS A CB  1 
ATOM   983  C CG  . LYS A 1 122 ? -5.837  11.337  17.638  1.00 51.79  ? 122 LYS A CG  1 
ATOM   984  C CD  . LYS A 1 122 ? -6.815  12.498  17.422  1.00 60.96  ? 122 LYS A CD  1 
ATOM   985  C CE  . LYS A 1 122 ? -6.150  13.857  17.657  1.00 56.88  ? 122 LYS A CE  1 
ATOM   986  N NZ  . LYS A 1 122 ? -7.130  14.976  17.753  1.00 63.49  ? 122 LYS A NZ  1 
ATOM   987  N N   . CYS A 1 123 ? -8.794  8.281   19.185  1.00 40.99  ? 123 CYS A N   1 
ATOM   988  C CA  . CYS A 1 123 ? -9.685  7.130   19.052  1.00 49.46  ? 123 CYS A CA  1 
ATOM   989  C C   . CYS A 1 123 ? -9.528  6.468   17.690  1.00 50.34  ? 123 CYS A C   1 
ATOM   990  O O   . CYS A 1 123 ? -9.395  5.242   17.596  1.00 49.96  ? 123 CYS A O   1 
ATOM   991  C CB  . CYS A 1 123 ? -11.148 7.544   19.261  1.00 50.56  ? 123 CYS A CB  1 
ATOM   992  S SG  . CYS A 1 123 ? -11.496 8.394   20.826  1.00 91.41  ? 123 CYS A SG  1 
ATOM   993  N N   . ARG A 1 124 ? -9.555  7.268   16.622  1.00 41.29  ? 124 ARG A N   1 
ATOM   994  C CA  . ARG A 1 124 ? -9.432  6.782   15.244  1.00 47.35  ? 124 ARG A CA  1 
ATOM   995  C C   . ARG A 1 124 ? -8.322  7.553   14.538  1.00 45.98  ? 124 ARG A C   1 
ATOM   996  O O   . ARG A 1 124 ? -8.578  8.550   13.839  1.00 42.58  ? 124 ARG A O   1 
ATOM   997  C CB  . ARG A 1 124 ? -10.762 6.908   14.497  1.00 48.18  ? 124 ARG A CB  1 
ATOM   998  C CG  . ARG A 1 124 ? -11.638 5.673   14.611  1.00 57.08  ? 124 ARG A CG  1 
ATOM   999  C CD  . ARG A 1 124 ? -13.112 6.017   14.461  1.00 65.71  ? 124 ARG A CD  1 
ATOM   1000 N NE  . ARG A 1 124 ? -13.968 4.966   14.997  1.00 71.33  ? 124 ARG A NE  1 
ATOM   1001 C CZ  . ARG A 1 124 ? -14.865 4.292   14.289  1.00 74.20  ? 124 ARG A CZ  1 
ATOM   1002 N NH1 . ARG A 1 124 ? -15.071 4.551   13.007  1.00 76.65  ? 124 ARG A NH1 1 
ATOM   1003 N NH2 . ARG A 1 124 ? -15.574 3.334   14.881  1.00 73.72  ? 124 ARG A NH2 1 
ATOM   1004 N N   . PRO A 1 125 ? -7.071  7.124   14.715  1.00 42.36  ? 125 PRO A N   1 
ATOM   1005 C CA  . PRO A 1 125 ? -5.940  7.809   14.081  1.00 41.86  ? 125 PRO A CA  1 
ATOM   1006 C C   . PRO A 1 125 ? -5.987  7.777   12.560  1.00 48.50  ? 125 PRO A C   1 
ATOM   1007 O O   . PRO A 1 125 ? -6.708  6.989   11.936  1.00 40.89  ? 125 PRO A O   1 
ATOM   1008 C CB  . PRO A 1 125 ? -4.724  7.037   14.606  1.00 36.80  ? 125 PRO A CB  1 
ATOM   1009 C CG  . PRO A 1 125 ? -5.200  6.490   15.929  1.00 39.19  ? 125 PRO A CG  1 
ATOM   1010 C CD  . PRO A 1 125 ? -6.614  6.086   15.660  1.00 41.93  ? 125 PRO A CD  1 
ATOM   1011 N N   . SER A 1 126 ? -5.166  8.641   11.963  1.00 39.63  ? 126 SER A N   1 
ATOM   1012 C CA  . SER A 1 126 ? -5.117  8.804   10.513  1.00 45.26  ? 126 SER A CA  1 
ATOM   1013 C C   . SER A 1 126 ? -3.818  8.295   9.893   1.00 44.17  ? 126 SER A C   1 
ATOM   1014 O O   . SER A 1 126 ? -3.417  8.779   8.838   1.00 46.74  ? 126 SER A O   1 
ATOM   1015 C CB  . SER A 1 126 ? -5.321  10.272  10.147  1.00 47.52  ? 126 SER A CB  1 
ATOM   1016 O OG  . SER A 1 126 ? -6.586  10.733  10.584  1.00 53.65  ? 126 SER A OG  1 
ATOM   1017 N N   . ASN A 1 127 ? -3.138  7.337   10.522  1.00 39.43  ? 127 ASN A N   1 
ATOM   1018 C CA  . ASN A 1 127 ? -1.846  6.891   9.994   1.00 38.51  ? 127 ASN A CA  1 
ATOM   1019 C C   . ASN A 1 127 ? -1.993  6.271   8.616   1.00 46.34  ? 127 ASN A C   1 
ATOM   1020 O O   . ASN A 1 127 ? -1.275  6.637   7.674   1.00 42.27  ? 127 ASN A O   1 
ATOM   1021 C CB  . ASN A 1 127 ? -1.206  5.880   10.934  1.00 32.69  ? 127 ASN A CB  1 
ATOM   1022 C CG  . ASN A 1 127 ? -0.997  6.436   12.315  1.00 36.16  ? 127 ASN A CG  1 
ATOM   1023 O OD1 . ASN A 1 127 ? -0.213  7.364   12.514  1.00 35.12  ? 127 ASN A OD1 1 
ATOM   1024 N ND2 . ASN A 1 127 ? -1.722  5.891   13.275  1.00 35.13  ? 127 ASN A ND2 1 
ATOM   1025 N N   . LEU A 1 128 ? -2.939  5.341   8.477   1.00 46.63  ? 128 LEU A N   1 
ATOM   1026 C CA  . LEU A 1 128 ? -3.075  4.587   7.231   1.00 48.95  ? 128 LEU A CA  1 
ATOM   1027 C C   . LEU A 1 128 ? -3.554  5.469   6.092   1.00 51.37  ? 128 LEU A C   1 
ATOM   1028 O O   . LEU A 1 128 ? -3.128  5.304   4.947   1.00 46.16  ? 128 LEU A O   1 
ATOM   1029 C CB  . LEU A 1 128 ? -4.038  3.416   7.440   1.00 41.77  ? 128 LEU A CB  1 
ATOM   1030 C CG  . LEU A 1 128 ? -4.183  2.440   6.277   1.00 52.28  ? 128 LEU A CG  1 
ATOM   1031 C CD1 . LEU A 1 128 ? -2.833  1.900   5.859   1.00 48.34  ? 128 LEU A CD1 1 
ATOM   1032 C CD2 . LEU A 1 128 ? -5.081  1.302   6.717   1.00 53.53  ? 128 LEU A CD2 1 
ATOM   1033 N N   . THR A 1 129 ? -4.479  6.372   6.372   1.00 49.05  ? 129 THR A N   1 
ATOM   1034 C CA  . THR A 1 129 ? -5.002  7.218   5.310   1.00 54.94  ? 129 THR A CA  1 
ATOM   1035 C C   . THR A 1 129 ? -4.082  8.390   4.969   1.00 52.86  ? 129 THR A C   1 
ATOM   1036 O O   . THR A 1 129 ? -4.075  8.849   3.822   1.00 62.33  ? 129 THR A O   1 
ATOM   1037 C CB  . THR A 1 129 ? -6.406  7.620   5.705   1.00 55.27  ? 129 THR A CB  1 
ATOM   1038 O OG1 . THR A 1 129 ? -6.358  8.430   6.883   1.00 55.70  ? 129 THR A OG1 1 
ATOM   1039 C CG2 . THR A 1 129 ? -7.134  6.310   6.022   1.00 58.16  ? 129 THR A CG2 1 
ATOM   1040 N N   . GLN A 1 130 ? -3.315  8.894   5.928   1.00 48.79  ? 130 GLN A N   1 
ATOM   1041 C CA  . GLN A 1 130 ? -2.260  9.842   5.592   1.00 52.24  ? 130 GLN A CA  1 
ATOM   1042 C C   . GLN A 1 130 ? -1.230  9.169   4.683   1.00 52.39  ? 130 GLN A C   1 
ATOM   1043 O O   . GLN A 1 130 ? -0.853  9.712   3.635   1.00 51.52  ? 130 GLN A O   1 
ATOM   1044 C CB  . GLN A 1 130 ? -1.633  10.348  6.886   1.00 52.27  ? 130 GLN A CB  1 
ATOM   1045 C CG  . GLN A 1 130 ? -2.287  11.592  7.473   1.00 55.11  ? 130 GLN A CG  1 
ATOM   1046 C CD  . GLN A 1 130 ? -1.722  11.928  8.852   1.00 57.31  ? 130 GLN A CD  1 
ATOM   1047 O OE1 . GLN A 1 130 ? -0.583  11.588  9.167   1.00 51.65  ? 130 GLN A OE1 1 
ATOM   1048 N NE2 . GLN A 1 130 ? -2.531  12.578  9.686   1.00 59.77  ? 130 GLN A NE2 1 
ATOM   1049 N N   . PHE A 1 131 ? -0.818  7.944   5.038   1.00 47.10  ? 131 PHE A N   1 
ATOM   1050 C CA  . PHE A 1 131 ? 0.152   7.220   4.220   1.00 47.48  ? 131 PHE A CA  1 
ATOM   1051 C C   . PHE A 1 131 ? -0.421  6.878   2.848   1.00 56.50  ? 131 PHE A C   1 
ATOM   1052 O O   . PHE A 1 131 ? 0.296   6.908   1.836   1.00 48.41  ? 131 PHE A O   1 
ATOM   1053 C CB  . PHE A 1 131 ? 0.615   5.939   4.923   1.00 44.28  ? 131 PHE A CB  1 
ATOM   1054 C CG  . PHE A 1 131 ? 1.694   5.219   4.166   1.00 45.37  ? 131 PHE A CG  1 
ATOM   1055 C CD1 . PHE A 1 131 ? 2.958   5.781   4.040   1.00 47.17  ? 131 PHE A CD1 1 
ATOM   1056 C CD2 . PHE A 1 131 ? 1.415   4.057   3.474   1.00 52.54  ? 131 PHE A CD2 1 
ATOM   1057 C CE1 . PHE A 1 131 ? 3.957   5.151   3.292   1.00 52.89  ? 131 PHE A CE1 1 
ATOM   1058 C CE2 . PHE A 1 131 ? 2.402   3.420   2.715   1.00 49.53  ? 131 PHE A CE2 1 
ATOM   1059 C CZ  . PHE A 1 131 ? 3.674   3.970   2.622   1.00 51.79  ? 131 PHE A CZ  1 
ATOM   1060 N N   . ALA A 1 132 ? -1.713  6.535   2.793   1.00 51.61  ? 132 ALA A N   1 
ATOM   1061 C CA  . ALA A 1 132 ? -2.329  6.185   1.519   1.00 54.35  ? 132 ALA A CA  1 
ATOM   1062 C C   . ALA A 1 132 ? -2.293  7.361   0.551   1.00 54.07  ? 132 ALA A C   1 
ATOM   1063 O O   . ALA A 1 132 ? -2.093  7.176   -0.655  1.00 58.77  ? 132 ALA A O   1 
ATOM   1064 C CB  . ALA A 1 132 ? -3.762  5.709   1.747   1.00 52.01  ? 132 ALA A CB  1 
ATOM   1065 N N   . VAL A 1 133 ? -2.458  8.582   1.062   1.00 51.67  ? 133 VAL A N   1 
ATOM   1066 C CA  . VAL A 1 133 ? -2.351  9.763   0.207   1.00 61.23  ? 133 VAL A CA  1 
ATOM   1067 C C   . VAL A 1 133 ? -0.937  9.865   -0.357  1.00 57.84  ? 133 VAL A C   1 
ATOM   1068 O O   . VAL A 1 133 ? -0.735  10.078  -1.561  1.00 54.66  ? 133 VAL A O   1 
ATOM   1069 C CB  . VAL A 1 133 ? -2.735  11.031  0.995   1.00 64.62  ? 133 VAL A CB  1 
ATOM   1070 C CG1 . VAL A 1 133 ? -2.143  12.271  0.327   1.00 68.12  ? 133 VAL A CG1 1 
ATOM   1071 C CG2 . VAL A 1 133 ? -4.250  11.146  1.156   1.00 59.86  ? 133 VAL A CG2 1 
ATOM   1072 N N   . TYR A 1 134 ? 0.063   9.674   0.506   1.00 47.88  ? 134 TYR A N   1 
ATOM   1073 C CA  . TYR A 1 134 ? 1.446   9.692   0.048   1.00 54.78  ? 134 TYR A CA  1 
ATOM   1074 C C   . TYR A 1 134 ? 1.690   8.588   -0.978  1.00 57.17  ? 134 TYR A C   1 
ATOM   1075 O O   . TYR A 1 134 ? 2.263   8.832   -2.048  1.00 57.63  ? 134 TYR A O   1 
ATOM   1076 C CB  . TYR A 1 134 ? 2.396   9.560   1.246   1.00 52.55  ? 134 TYR A CB  1 
ATOM   1077 C CG  . TYR A 1 134 ? 3.810   9.207   0.852   1.00 45.72  ? 134 TYR A CG  1 
ATOM   1078 C CD1 . TYR A 1 134 ? 4.714   10.197  0.489   1.00 54.25  ? 134 TYR A CD1 1 
ATOM   1079 C CD2 . TYR A 1 134 ? 4.245   7.884   0.847   1.00 54.36  ? 134 TYR A CD2 1 
ATOM   1080 C CE1 . TYR A 1 134 ? 6.013   9.884   0.111   1.00 52.22  ? 134 TYR A CE1 1 
ATOM   1081 C CE2 . TYR A 1 134 ? 5.545   7.561   0.479   1.00 52.28  ? 134 TYR A CE2 1 
ATOM   1082 C CZ  . TYR A 1 134 ? 6.419   8.568   0.108   1.00 53.64  ? 134 TYR A CZ  1 
ATOM   1083 O OH  . TYR A 1 134 ? 7.702   8.257   -0.265  1.00 59.77  ? 134 TYR A OH  1 
ATOM   1084 N N   . LEU A 1 135 ? 1.248   7.368   -0.666  1.00 55.68  ? 135 LEU A N   1 
ATOM   1085 C CA  . LEU A 1 135 ? 1.468   6.225   -1.547  1.00 55.99  ? 135 LEU A CA  1 
ATOM   1086 C C   . LEU A 1 135 ? 0.875   6.468   -2.929  1.00 57.07  ? 135 LEU A C   1 
ATOM   1087 O O   . LEU A 1 135 ? 1.538   6.253   -3.947  1.00 63.14  ? 135 LEU A O   1 
ATOM   1088 C CB  . LEU A 1 135 ? 0.869   4.969   -0.919  1.00 61.75  ? 135 LEU A CB  1 
ATOM   1089 C CG  . LEU A 1 135 ? 1.221   3.649   -1.605  1.00 69.24  ? 135 LEU A CG  1 
ATOM   1090 C CD1 . LEU A 1 135 ? 2.698   3.348   -1.380  1.00 63.58  ? 135 LEU A CD1 1 
ATOM   1091 C CD2 . LEU A 1 135 ? 0.344   2.511   -1.092  1.00 69.07  ? 135 LEU A CD2 1 
ATOM   1092 N N   . ASN A 1 136 ? -0.382  6.918   -2.980  1.00 53.31  ? 136 ASN A N   1 
ATOM   1093 C CA  . ASN A 1 136 ? -1.008  7.240   -4.259  1.00 64.13  ? 136 ASN A CA  1 
ATOM   1094 C C   . ASN A 1 136 ? -0.340  8.435   -4.920  1.00 61.93  ? 136 ASN A C   1 
ATOM   1095 O O   . ASN A 1 136 ? -0.300  8.519   -6.154  1.00 66.46  ? 136 ASN A O   1 
ATOM   1096 C CB  . ASN A 1 136 ? -2.503  7.503   -4.063  1.00 64.99  ? 136 ASN A CB  1 
ATOM   1097 C CG  . ASN A 1 136 ? -3.293  7.407   -5.352  1.00 67.78  ? 136 ASN A CG  1 
ATOM   1098 O OD1 . ASN A 1 136 ? -3.144  6.459   -6.125  1.00 65.81  ? 136 ASN A OD1 1 
ATOM   1099 N ND2 . ASN A 1 136 ? -4.168  8.380   -5.573  1.00 67.21  ? 136 ASN A ND2 1 
ATOM   1100 N N   . SER A 1 137 ? 0.187   9.367   -4.128  1.00 66.78  ? 137 SER A N   1 
ATOM   1101 C CA  . SER A 1 137 ? 0.870   10.510  -4.715  1.00 66.13  ? 137 SER A CA  1 
ATOM   1102 C C   . SER A 1 137 ? 2.149   10.084  -5.426  1.00 67.58  ? 137 SER A C   1 
ATOM   1103 O O   . SER A 1 137 ? 2.514   10.675  -6.449  1.00 64.63  ? 137 SER A O   1 
ATOM   1104 C CB  . SER A 1 137 ? 1.178   11.550  -3.636  1.00 71.75  ? 137 SER A CB  1 
ATOM   1105 O OG  . SER A 1 137 ? 1.917   12.628  -4.185  1.00 80.82  ? 137 SER A OG  1 
ATOM   1106 N N   . ARG A 1 138 ? 2.819   9.042   -4.926  1.00 63.61  ? 138 ARG A N   1 
ATOM   1107 C CA  . ARG A 1 138 ? 4.086   8.608   -5.503  1.00 65.89  ? 138 ARG A CA  1 
ATOM   1108 C C   . ARG A 1 138 ? 3.926   7.517   -6.555  1.00 62.81  ? 138 ARG A C   1 
ATOM   1109 O O   . ARG A 1 138 ? 4.699   7.483   -7.520  1.00 66.93  ? 138 ARG A O   1 
ATOM   1110 C CB  . ARG A 1 138 ? 5.022   8.101   -4.405  1.00 66.21  ? 138 ARG A CB  1 
ATOM   1111 C CG  . ARG A 1 138 ? 6.045   9.114   -3.890  1.00 67.94  ? 138 ARG A CG  1 
ATOM   1112 C CD  . ARG A 1 138 ? 5.527   10.544  -3.897  1.00 71.70  ? 138 ARG A CD  1 
ATOM   1113 N NE  . ARG A 1 138 ? 6.464   11.447  -3.238  1.00 80.32  ? 138 ARG A NE  1 
ATOM   1114 C CZ  . ARG A 1 138 ? 6.116   12.543  -2.574  1.00 86.07  ? 138 ARG A CZ  1 
ATOM   1115 N NH1 . ARG A 1 138 ? 4.849   12.918  -2.470  1.00 81.38  ? 138 ARG A NH1 1 
ATOM   1116 N NH2 . ARG A 1 138 ? 7.058   13.267  -1.975  1.00 85.01  ? 138 ARG A NH2 1 
ATOM   1117 N N   . LEU A 1 139 ? 2.956   6.619   -6.396  1.00 64.59  ? 139 LEU A N   1 
ATOM   1118 C CA  . LEU A 1 139 ? 2.794   5.482   -7.298  1.00 65.08  ? 139 LEU A CA  1 
ATOM   1119 C C   . LEU A 1 139 ? 1.675   5.676   -8.322  1.00 71.25  ? 139 LEU A C   1 
ATOM   1120 O O   . LEU A 1 139 ? 1.540   4.845   -9.232  1.00 67.93  ? 139 LEU A O   1 
ATOM   1121 C CB  . LEU A 1 139 ? 2.531   4.206   -6.478  1.00 60.34  ? 139 LEU A CB  1 
ATOM   1122 C CG  . LEU A 1 139 ? 3.543   3.835   -5.380  1.00 70.51  ? 139 LEU A CG  1 
ATOM   1123 C CD1 . LEU A 1 139 ? 3.411   2.375   -4.962  1.00 68.02  ? 139 LEU A CD1 1 
ATOM   1124 C CD2 . LEU A 1 139 ? 4.971   4.117   -5.835  1.00 70.53  ? 139 LEU A CD2 1 
ATOM   1125 N N   . ARG A 1 140 ? 0.921   6.775   -8.234  1.00 67.90  ? 140 ARG A N   1 
ATOM   1126 C CA  . ARG A 1 140 ? -0.271  7.018   -9.055  1.00 68.27  ? 140 ARG A CA  1 
ATOM   1127 C C   . ARG A 1 140 ? -1.114  5.768   -9.250  1.00 73.52  ? 140 ARG A C   1 
ATOM   1128 O O   . ARG A 1 140 ? -1.404  5.339   -10.368 1.00 70.49  ? 140 ARG A O   1 
ATOM   1129 C CB  . ARG A 1 140 ? 0.072   7.644   -10.394 1.00 70.04  ? 140 ARG A CB  1 
ATOM   1130 C CG  . ARG A 1 140 ? 0.978   8.820   -10.297 1.00 76.16  ? 140 ARG A CG  1 
ATOM   1131 C CD  . ARG A 1 140 ? 1.263   9.272   -11.685 1.00 81.42  ? 140 ARG A CD  1 
ATOM   1132 N NE  . ARG A 1 140 ? 0.005   9.299   -12.420 1.00 84.96  ? 140 ARG A NE  1 
ATOM   1133 C CZ  . ARG A 1 140 ? -0.627  10.388  -12.829 1.00 95.32  ? 140 ARG A CZ  1 
ATOM   1134 N NH1 . ARG A 1 140 ? -0.230  11.596  -12.463 1.00 97.34  ? 140 ARG A NH1 1 
ATOM   1135 N NH2 . ARG A 1 140 ? -1.692  10.261  -13.619 1.00 100.32 ? 140 ARG A NH2 1 
ATOM   1136 N N   . LEU A 1 141 ? -1.512  5.182   -8.126  1.00 73.03  ? 141 LEU A N   1 
ATOM   1137 C CA  . LEU A 1 141 ? -2.275  3.947   -8.174  1.00 75.67  ? 141 LEU A CA  1 
ATOM   1138 C C   . LEU A 1 141 ? -3.674  4.192   -8.741  1.00 77.10  ? 141 LEU A C   1 
ATOM   1139 O O   . LEU A 1 141 ? -4.211  3.331   -9.442  1.00 82.32  ? 141 LEU A O   1 
ATOM   1140 C CB  . LEU A 1 141 ? -2.323  3.362   -6.762  1.00 69.51  ? 141 LEU A CB  1 
ATOM   1141 C CG  . LEU A 1 141 ? -1.026  2.662   -6.305  1.00 70.89  ? 141 LEU A CG  1 
ATOM   1142 C CD1 . LEU A 1 141 ? -1.212  1.843   -5.009  1.00 63.52  ? 141 LEU A CD1 1 
ATOM   1143 C CD2 . LEU A 1 141 ? -0.442  1.793   -7.401  1.00 66.65  ? 141 LEU A CD2 1 
ATOM   1144 N N   . MET A 1 142 ? -4.240  5.382   -8.517  1.00 71.30  ? 142 MET A N   1 
ATOM   1145 C CA  . MET A 1 142 ? -5.650  5.661   -8.783  1.00 71.47  ? 142 MET A CA  1 
ATOM   1146 C C   . MET A 1 142 ? -5.892  7.160   -8.631  1.00 75.65  ? 142 MET A C   1 
ATOM   1147 O O   . MET A 1 142 ? -5.021  7.900   -8.167  1.00 73.64  ? 142 MET A O   1 
ATOM   1148 C CB  . MET A 1 142 ? -6.557  4.878   -7.833  1.00 80.53  ? 142 MET A CB  1 
ATOM   1149 C CG  . MET A 1 142 ? -6.305  5.205   -6.371  1.00 74.92  ? 142 MET A CG  1 
ATOM   1150 S SD  . MET A 1 142 ? -7.234  4.169   -5.236  1.00 79.87  ? 142 MET A SD  1 
ATOM   1151 C CE  . MET A 1 142 ? -6.142  2.760   -5.042  1.00 79.46  ? 142 MET A CE  1 
ATOM   1152 N N   . LYS A 1 143 ? -7.075  7.609   -9.060  1.00 73.49  ? 143 LYS A N   1 
ATOM   1153 C CA  . LYS A 1 143 ? -7.470  9.005   -8.872  1.00 81.17  ? 143 LYS A CA  1 
ATOM   1154 C C   . LYS A 1 143 ? -8.023  9.213   -7.462  1.00 81.98  ? 143 LYS A C   1 
ATOM   1155 O O   . LYS A 1 143 ? -8.480  8.261   -6.821  1.00 89.03  ? 143 LYS A O   1 
ATOM   1156 C CB  . LYS A 1 143 ? -8.513  9.417   -9.912  1.00 80.88  ? 143 LYS A CB  1 
ATOM   1157 N N   . ASN A 1 144 ? -7.935  10.459  -6.959  1.00 79.09  ? 144 ASN A N   1 
ATOM   1158 C CA  . ASN A 1 144 ? -8.473  10.761  -5.625  1.00 84.75  ? 144 ASN A CA  1 
ATOM   1159 C C   . ASN A 1 144 ? -9.863  10.192  -5.394  1.00 85.13  ? 144 ASN A C   1 
ATOM   1160 O O   . ASN A 1 144 ? -10.090 9.489   -4.401  1.00 89.73  ? 144 ASN A O   1 
ATOM   1161 C CB  . ASN A 1 144 ? -8.499  12.261  -5.319  1.00 99.36  ? 144 ASN A CB  1 
ATOM   1162 C CG  . ASN A 1 144 ? -7.185  12.777  -4.777  1.00 108.88 ? 144 ASN A CG  1 
ATOM   1163 O OD1 . ASN A 1 144 ? -6.136  12.172  -4.974  1.00 113.33 ? 144 ASN A OD1 1 
ATOM   1164 N ND2 . ASN A 1 144 ? -7.261  13.838  -3.977  1.00 113.00 ? 144 ASN A ND2 1 
ATOM   1165 N N   . GLU A 1 145 ? -10.813 10.507  -6.278  1.00 71.98  ? 145 GLU A N   1 
ATOM   1166 C CA  . GLU A 1 145 ? -12.196 10.124  -6.015  1.00 82.04  ? 145 GLU A CA  1 
ATOM   1167 C C   . GLU A 1 145 ? -12.287 8.652   -5.634  1.00 86.84  ? 145 GLU A C   1 
ATOM   1168 O O   . GLU A 1 145 ? -12.979 8.293   -4.672  1.00 88.65  ? 145 GLU A O   1 
ATOM   1169 C CB  . GLU A 1 145 ? -13.069 10.430  -7.234  1.00 77.30  ? 145 GLU A CB  1 
ATOM   1170 N N   . GLU A 1 146 ? -11.521 7.797   -6.316  1.00 79.62  ? 146 GLU A N   1 
ATOM   1171 C CA  . GLU A 1 146 ? -11.475 6.389   -5.936  1.00 75.84  ? 146 GLU A CA  1 
ATOM   1172 C C   . GLU A 1 146 ? -10.727 6.197   -4.620  1.00 81.35  ? 146 GLU A C   1 
ATOM   1173 O O   . GLU A 1 146 ? -11.209 5.498   -3.720  1.00 85.60  ? 146 GLU A O   1 
ATOM   1174 C CB  . GLU A 1 146 ? -10.834 5.558   -7.046  1.00 78.97  ? 146 GLU A CB  1 
ATOM   1175 C CG  . GLU A 1 146 ? -10.891 4.058   -6.793  1.00 80.31  ? 146 GLU A CG  1 
ATOM   1176 N N   . LEU A 1 147 ? -9.540  6.802   -4.485  1.00 78.63  ? 147 LEU A N   1 
ATOM   1177 C CA  . LEU A 1 147 ? -8.814  6.677   -3.219  1.00 70.59  ? 147 LEU A CA  1 
ATOM   1178 C C   . LEU A 1 147 ? -9.614  7.266   -2.065  1.00 76.39  ? 147 LEU A C   1 
ATOM   1179 O O   . LEU A 1 147 ? -9.693  6.666   -0.987  1.00 76.36  ? 147 LEU A O   1 
ATOM   1180 C CB  . LEU A 1 147 ? -7.441  7.348   -3.295  1.00 69.64  ? 147 LEU A CB  1 
ATOM   1181 C CG  . LEU A 1 147 ? -6.699  7.320   -1.937  1.00 71.57  ? 147 LEU A CG  1 
ATOM   1182 C CD1 . LEU A 1 147 ? -6.300  5.896   -1.547  1.00 59.11  ? 147 LEU A CD1 1 
ATOM   1183 C CD2 . LEU A 1 147 ? -5.478  8.240   -1.904  1.00 64.67  ? 147 LEU A CD2 1 
ATOM   1184 N N   . LYS A 1 148 ? -10.214 8.443   -2.273  1.00 79.08  ? 148 LYS A N   1 
ATOM   1185 C CA  . LYS A 1 148 ? -10.972 9.089   -1.204  1.00 88.37  ? 148 LYS A CA  1 
ATOM   1186 C C   . LYS A 1 148 ? -12.177 8.250   -0.788  1.00 81.77  ? 148 LYS A C   1 
ATOM   1187 O O   . LYS A 1 148 ? -12.536 8.209   0.397   1.00 84.37  ? 148 LYS A O   1 
ATOM   1188 C CB  . LYS A 1 148 ? -11.396 10.498  -1.630  1.00 86.31  ? 148 LYS A CB  1 
ATOM   1189 C CG  . LYS A 1 148 ? -10.256 11.520  -1.536  1.00 96.70  ? 148 LYS A CG  1 
ATOM   1190 C CD  . LYS A 1 148 ? -10.645 12.775  -0.755  1.00 97.01  ? 148 LYS A CD  1 
ATOM   1191 C CE  . LYS A 1 148 ? -11.901 13.427  -1.314  1.00 95.01  ? 148 LYS A CE  1 
ATOM   1192 N NZ  . LYS A 1 148 ? -11.604 14.196  -2.555  1.00 95.30  ? 148 LYS A NZ  1 
ATOM   1193 N N   . LYS A 1 149 ? -12.810 7.570   -1.743  1.00 80.46  ? 149 LYS A N   1 
ATOM   1194 C CA  . LYS A 1 149 ? -13.890 6.653   -1.394  1.00 83.36  ? 149 LYS A CA  1 
ATOM   1195 C C   . LYS A 1 149 ? -13.364 5.488   -0.565  1.00 79.54  ? 149 LYS A C   1 
ATOM   1196 O O   . LYS A 1 149 ? -13.966 5.112   0.449   1.00 78.29  ? 149 LYS A O   1 
ATOM   1197 C CB  . LYS A 1 149 ? -14.584 6.146   -2.659  1.00 73.21  ? 149 LYS A CB  1 
ATOM   1198 N N   . LEU A 1 150 ? -12.220 4.928   -0.960  1.00 80.24  ? 150 LEU A N   1 
ATOM   1199 C CA  . LEU A 1 150 ? -11.654 3.795   -0.238  1.00 78.30  ? 150 LEU A CA  1 
ATOM   1200 C C   . LEU A 1 150 ? -11.341 4.163   1.202   1.00 76.26  ? 150 LEU A C   1 
ATOM   1201 O O   . LEU A 1 150 ? -11.570 3.368   2.121   1.00 68.41  ? 150 LEU A O   1 
ATOM   1202 C CB  . LEU A 1 150 ? -10.380 3.322   -0.928  1.00 78.48  ? 150 LEU A CB  1 
ATOM   1203 C CG  . LEU A 1 150 ? -10.545 2.618   -2.267  1.00 77.93  ? 150 LEU A CG  1 
ATOM   1204 C CD1 . LEU A 1 150 ? -9.256  2.726   -3.021  1.00 77.08  ? 150 LEU A CD1 1 
ATOM   1205 C CD2 . LEU A 1 150 ? -10.914 1.202   -2.070  1.00 79.04  ? 150 LEU A CD2 1 
ATOM   1206 N N   . LEU A 1 151 ? -10.800 5.363   1.414   1.00 74.45  ? 151 LEU A N   1 
ATOM   1207 C CA  . LEU A 1 151 ? -10.444 5.787   2.760   1.00 76.69  ? 151 LEU A CA  1 
ATOM   1208 C C   . LEU A 1 151 ? -11.686 6.036   3.602   1.00 76.78  ? 151 LEU A C   1 
ATOM   1209 O O   . LEU A 1 151 ? -11.674 5.777   4.813   1.00 74.08  ? 151 LEU A O   1 
ATOM   1210 C CB  . LEU A 1 151 ? -9.560  7.035   2.695   1.00 66.73  ? 151 LEU A CB  1 
ATOM   1211 C CG  . LEU A 1 151 ? -8.264  6.847   1.890   1.00 69.21  ? 151 LEU A CG  1 
ATOM   1212 C CD1 . LEU A 1 151 ? -7.324  8.047   2.007   1.00 64.85  ? 151 LEU A CD1 1 
ATOM   1213 C CD2 . LEU A 1 151 ? -7.544  5.562   2.298   1.00 62.51  ? 151 LEU A CD2 1 
ATOM   1214 N N   . ARG A 1 152 ? -12.766 6.528   2.980   1.00 78.51  ? 152 ARG A N   1 
ATOM   1215 C CA  . ARG A 1 152 ? -14.014 6.732   3.712   1.00 80.31  ? 152 ARG A CA  1 
ATOM   1216 C C   . ARG A 1 152 ? -14.560 5.417   4.270   1.00 75.77  ? 152 ARG A C   1 
ATOM   1217 O O   . ARG A 1 152 ? -15.052 5.377   5.406   1.00 72.63  ? 152 ARG A O   1 
ATOM   1218 C CB  . ARG A 1 152 ? -15.046 7.419   2.812   1.00 81.17  ? 152 ARG A CB  1 
ATOM   1219 C CG  . ARG A 1 152 ? -14.889 8.935   2.748   1.00 88.59  ? 152 ARG A CG  1 
ATOM   1220 C CD  . ARG A 1 152 ? -15.993 9.593   1.928   1.00 86.66  ? 152 ARG A CD  1 
ATOM   1221 N NE  . ARG A 1 152 ? -15.493 10.746  1.187   1.00 94.32  ? 152 ARG A NE  1 
ATOM   1222 C CZ  . ARG A 1 152 ? -15.481 10.835  -0.136  1.00 95.80  ? 152 ARG A CZ  1 
ATOM   1223 N NH1 . ARG A 1 152 ? -15.987 9.878   -0.897  1.00 92.40  ? 152 ARG A NH1 1 
ATOM   1224 N NH2 . ARG A 1 152 ? -14.954 11.914  -0.710  1.00 100.33 ? 152 ARG A NH2 1 
ATOM   1225 N N   . GLU A 1 153 ? -14.477 4.328   3.491   1.00 74.14  ? 153 GLU A N   1 
ATOM   1226 C CA  . GLU A 1 153 ? -15.055 3.058   3.928   1.00 72.39  ? 153 GLU A CA  1 
ATOM   1227 C C   . GLU A 1 153 ? -14.264 2.445   5.075   1.00 75.48  ? 153 GLU A C   1 
ATOM   1228 O O   . GLU A 1 153 ? -14.840 1.954   6.045   1.00 75.73  ? 153 GLU A O   1 
ATOM   1229 C CB  . GLU A 1 153 ? -15.110 2.087   2.753   1.00 66.85  ? 153 GLU A CB  1 
ATOM   1230 N N   . TYR A 1 154 ? -12.940 2.444   4.965   1.00 70.28  ? 154 TYR A N   1 
ATOM   1231 C CA  . TYR A 1 154 ? -12.101 2.007   6.074   1.00 65.20  ? 154 TYR A CA  1 
ATOM   1232 C C   . TYR A 1 154 ? -12.403 2.807   7.324   1.00 69.37  ? 154 TYR A C   1 
ATOM   1233 O O   . TYR A 1 154 ? -12.505 2.240   8.434   1.00 64.52  ? 154 TYR A O   1 
ATOM   1234 C CB  . TYR A 1 154 ? -10.630 2.170   5.707   1.00 57.18  ? 154 TYR A CB  1 
ATOM   1235 C CG  . TYR A 1 154 ? -9.692  2.014   6.890   1.00 56.95  ? 154 TYR A CG  1 
ATOM   1236 C CD1 . TYR A 1 154 ? -9.488  0.806   7.501   1.00 57.37  ? 154 TYR A CD1 1 
ATOM   1237 C CD2 . TYR A 1 154 ? -8.969  3.128   7.364   1.00 56.80  ? 154 TYR A CD2 1 
ATOM   1238 C CE1 . TYR A 1 154 ? -8.650  0.669   8.574   1.00 51.84  ? 154 TYR A CE1 1 
ATOM   1239 C CE2 . TYR A 1 154 ? -8.117  2.995   8.433   1.00 48.89  ? 154 TYR A CE2 1 
ATOM   1240 C CZ  . TYR A 1 154 ? -7.959  1.767   9.029   1.00 53.52  ? 154 TYR A CZ  1 
ATOM   1241 O OH  . TYR A 1 154 ? -7.102  1.655   10.102  1.00 49.20  ? 154 TYR A OH  1 
ATOM   1242 N N   . LYS A 1 155 ? -12.489 4.126   7.193   1.00 68.60  ? 155 LYS A N   1 
ATOM   1243 C CA  . LYS A 1 155 ? -12.675 4.977   8.396   1.00 69.64  ? 155 LYS A CA  1 
ATOM   1244 C C   . LYS A 1 155 ? -14.008 4.650   9.071   1.00 73.66  ? 155 LYS A C   1 
ATOM   1245 O O   . LYS A 1 155 ? -14.042 4.654   10.311  1.00 75.13  ? 155 LYS A O   1 
ATOM   1246 C CB  . LYS A 1 155 ? -12.600 6.457   8.024   1.00 70.11  ? 155 LYS A CB  1 
ATOM   1247 C CG  . LYS A 1 155 ? -11.215 7.077   8.130   1.00 67.73  ? 155 LYS A CG  1 
ATOM   1248 N N   . LYS A 1 156 ? -15.055 4.380   8.293   1.00 70.32  ? 156 LYS A N   1 
ATOM   1249 C CA  . LYS A 1 156 ? -16.346 4.058   8.828   1.00 71.45  ? 156 LYS A CA  1 
ATOM   1250 C C   . LYS A 1 156 ? -16.304 2.789   9.648   1.00 71.86  ? 156 LYS A C   1 
ATOM   1251 O O   . LYS A 1 156 ? -16.659 2.807   10.835  1.00 77.00  ? 156 LYS A O   1 
ATOM   1252 C CB  . LYS A 1 156 ? -17.385 3.926   7.704   1.00 73.91  ? 156 LYS A CB  1 
ATOM   1253 N N   . GLY A 1 157 ? -15.823 1.694   9.057   1.00 71.87  ? 157 GLY A N   1 
ATOM   1254 C CA  . GLY A 1 157 ? -15.756 0.431   9.763   1.00 76.37  ? 157 GLY A CA  1 
ATOM   1255 C C   . GLY A 1 157 ? -14.637 0.357   10.786  1.00 69.37  ? 157 GLY A C   1 
ATOM   1256 O O   . GLY A 1 157 ? -14.881 0.091   11.965  1.00 72.01  ? 157 GLY A O   1 
ATOM   1257 N N   . PHE A 1 158 ? -13.401 0.605   10.343  1.00 73.90  ? 158 PHE A N   1 
ATOM   1258 C CA  . PHE A 1 158 ? -12.223 0.702   11.218  1.00 65.76  ? 158 PHE A CA  1 
ATOM   1259 C C   . PHE A 1 158 ? -11.973 -0.574  12.012  1.00 63.42  ? 158 PHE A C   1 
ATOM   1260 O O   . PHE A 1 158 ? -11.401 -0.535  13.102  1.00 68.71  ? 158 PHE A O   1 
ATOM   1261 C CB  . PHE A 1 158 ? -12.323 1.904   12.166  1.00 62.18  ? 158 PHE A CB  1 
ATOM   1262 C CG  . PHE A 1 158 ? -10.988 2.491   12.547  1.00 59.26  ? 158 PHE A CG  1 
ATOM   1263 C CD1 . PHE A 1 158 ? -10.288 3.294   11.656  1.00 56.79  ? 158 PHE A CD1 1 
ATOM   1264 C CD2 . PHE A 1 158 ? -10.453 2.276   13.813  1.00 65.22  ? 158 PHE A CD2 1 
ATOM   1265 C CE1 . PHE A 1 158 ? -9.064  3.846   12.004  1.00 54.22  ? 158 PHE A CE1 1 
ATOM   1266 C CE2 . PHE A 1 158 ? -9.232  2.829   14.177  1.00 58.55  ? 158 PHE A CE2 1 
ATOM   1267 C CZ  . PHE A 1 158 ? -8.536  3.618   13.272  1.00 55.00  ? 158 PHE A CZ  1 
ATOM   1268 N N   . ASP A 1 159 ? -12.373 -1.717  11.472  1.00 69.18  ? 159 ASP A N   1 
ATOM   1269 C CA  . ASP A 1 159 ? -12.031 -3.012  12.046  1.00 67.89  ? 159 ASP A CA  1 
ATOM   1270 C C   . ASP A 1 159 ? -11.166 -3.796  11.067  1.00 62.85  ? 159 ASP A C   1 
ATOM   1271 O O   . ASP A 1 159 ? -10.864 -3.335  9.961   1.00 64.90  ? 159 ASP A O   1 
ATOM   1272 C CB  . ASP A 1 159 ? -13.292 -3.794  12.421  1.00 66.64  ? 159 ASP A CB  1 
ATOM   1273 C CG  . ASP A 1 159 ? -14.238 -3.968  11.254  1.00 75.37  ? 159 ASP A CG  1 
ATOM   1274 O OD1 . ASP A 1 159 ? -13.921 -3.491  10.135  1.00 70.94  ? 159 ASP A OD1 1 
ATOM   1275 O OD2 . ASP A 1 159 ? -15.306 -4.583  11.464  1.00 82.46  ? 159 ASP A OD2 1 
ATOM   1276 N N   . ASP A 1 160 ? -10.776 -4.999  11.501  1.00 60.59  ? 160 ASP A N   1 
ATOM   1277 C CA  . ASP A 1 160 ? -9.929  -5.868  10.689  1.00 64.97  ? 160 ASP A CA  1 
ATOM   1278 C C   . ASP A 1 160 ? -10.485 -6.050  9.282   1.00 68.31  ? 160 ASP A C   1 
ATOM   1279 O O   . ASP A 1 160 ? -9.733  -6.002  8.300   1.00 69.90  ? 160 ASP A O   1 
ATOM   1280 C CB  . ASP A 1 160 ? -9.779  -7.227  11.376  1.00 68.95  ? 160 ASP A CB  1 
ATOM   1281 C CG  . ASP A 1 160 ? -8.940  -7.155  12.633  1.00 78.83  ? 160 ASP A CG  1 
ATOM   1282 O OD1 . ASP A 1 160 ? -8.503  -6.039  12.992  1.00 81.18  ? 160 ASP A OD1 1 
ATOM   1283 O OD2 . ASP A 1 160 ? -8.732  -8.211  13.271  1.00 81.52  ? 160 ASP A OD2 1 
ATOM   1284 N N   . GLU A 1 161 ? -11.799 -6.278  9.169   1.00 73.59  ? 161 GLU A N   1 
ATOM   1285 C CA  . GLU A 1 161 ? -12.436 -6.457  7.865   1.00 63.92  ? 161 GLU A CA  1 
ATOM   1286 C C   . GLU A 1 161 ? -12.269 -5.223  6.985   1.00 65.49  ? 161 GLU A C   1 
ATOM   1287 O O   . GLU A 1 161 ? -11.853 -5.323  5.824   1.00 72.51  ? 161 GLU A O   1 
ATOM   1288 C CB  . GLU A 1 161 ? -13.917 -6.794  8.049   1.00 71.76  ? 161 GLU A CB  1 
ATOM   1289 N N   . SER A 1 162 ? -12.624 -4.047  7.511   1.00 69.82  ? 162 SER A N   1 
ATOM   1290 C CA  . SER A 1 162 ? -12.430 -2.807  6.765   1.00 66.67  ? 162 SER A CA  1 
ATOM   1291 C C   . SER A 1 162 ? -10.986 -2.649  6.309   1.00 66.76  ? 162 SER A C   1 
ATOM   1292 O O   . SER A 1 162 ? -10.725 -2.195  5.187   1.00 64.10  ? 162 SER A O   1 
ATOM   1293 C CB  . SER A 1 162 ? -12.840 -1.611  7.629   1.00 70.99  ? 162 SER A CB  1 
ATOM   1294 O OG  . SER A 1 162 ? -14.182 -1.238  7.370   1.00 77.67  ? 162 SER A OG  1 
ATOM   1295 N N   . TYR A 1 163 ? -10.031 -3.013  7.167   1.00 68.05  ? 163 TYR A N   1 
ATOM   1296 C CA  . TYR A 1 163 ? -8.627  -2.867  6.798   1.00 66.43  ? 163 TYR A CA  1 
ATOM   1297 C C   . TYR A 1 163 ? -8.262  -3.810  5.659   1.00 64.06  ? 163 TYR A C   1 
ATOM   1298 O O   . TYR A 1 163 ? -7.621  -3.396  4.683   1.00 59.89  ? 163 TYR A O   1 
ATOM   1299 C CB  . TYR A 1 163 ? -7.707  -3.102  8.001   1.00 53.64  ? 163 TYR A CB  1 
ATOM   1300 C CG  . TYR A 1 163 ? -6.258  -3.160  7.574   1.00 51.38  ? 163 TYR A CG  1 
ATOM   1301 C CD1 . TYR A 1 163 ? -5.655  -2.071  6.949   1.00 49.95  ? 163 TYR A CD1 1 
ATOM   1302 C CD2 . TYR A 1 163 ? -5.503  -4.317  7.748   1.00 55.78  ? 163 TYR A CD2 1 
ATOM   1303 C CE1 . TYR A 1 163 ? -4.327  -2.126  6.523   1.00 53.86  ? 163 TYR A CE1 1 
ATOM   1304 C CE2 . TYR A 1 163 ? -4.174  -4.383  7.329   1.00 52.50  ? 163 TYR A CE2 1 
ATOM   1305 C CZ  . TYR A 1 163 ? -3.590  -3.286  6.720   1.00 54.77  ? 163 TYR A CZ  1 
ATOM   1306 O OH  . TYR A 1 163 ? -2.279  -3.355  6.295   1.00 47.85  ? 163 TYR A OH  1 
ATOM   1307 N N   . ARG A 1 164 ? -8.655  -5.084  5.771   1.00 65.97  ? 164 ARG A N   1 
ATOM   1308 C CA  . ARG A 1 164 ? -8.319  -6.053  4.731   1.00 67.30  ? 164 ARG A CA  1 
ATOM   1309 C C   . ARG A 1 164 ? -8.840  -5.604  3.376   1.00 65.67  ? 164 ARG A C   1 
ATOM   1310 O O   . ARG A 1 164 ? -8.134  -5.717  2.366   1.00 68.03  ? 164 ARG A O   1 
ATOM   1311 C CB  . ARG A 1 164 ? -8.873  -7.433  5.089   1.00 69.09  ? 164 ARG A CB  1 
ATOM   1312 N N   . GLU A 1 165 ? -10.067 -5.076  3.332   1.00 69.47  ? 165 GLU A N   1 
ATOM   1313 C CA  . GLU A 1 165 ? -10.604 -4.567  2.070   1.00 67.01  ? 165 GLU A CA  1 
ATOM   1314 C C   . GLU A 1 165 ? -9.739  -3.437  1.523   1.00 70.15  ? 165 GLU A C   1 
ATOM   1315 O O   . GLU A 1 165 ? -9.361  -3.449  0.347   1.00 72.31  ? 165 GLU A O   1 
ATOM   1316 C CB  . GLU A 1 165 ? -12.050 -4.104  2.253   1.00 67.09  ? 165 GLU A CB  1 
ATOM   1317 N N   . LEU A 1 166 ? -9.400  -2.455  2.367   1.00 66.76  ? 166 LEU A N   1 
ATOM   1318 C CA  . LEU A 1 166 ? -8.517  -1.378  1.924   1.00 63.06  ? 166 LEU A CA  1 
ATOM   1319 C C   . LEU A 1 166 ? -7.183  -1.935  1.435   1.00 62.19  ? 166 LEU A C   1 
ATOM   1320 O O   . LEU A 1 166 ? -6.698  -1.560  0.360   1.00 68.14  ? 166 LEU A O   1 
ATOM   1321 C CB  . LEU A 1 166 ? -8.296  -0.368  3.055   1.00 64.69  ? 166 LEU A CB  1 
ATOM   1322 C CG  . LEU A 1 166 ? -7.527  0.892   2.631   1.00 56.63  ? 166 LEU A CG  1 
ATOM   1323 C CD1 . LEU A 1 166 ? -8.359  1.744   1.684   1.00 68.10  ? 166 LEU A CD1 1 
ATOM   1324 C CD2 . LEU A 1 166 ? -7.088  1.711   3.825   1.00 57.79  ? 166 LEU A CD2 1 
ATOM   1325 N N   . ARG A 1 167 ? -6.594  -2.856  2.206   1.00 59.87  ? 167 ARG A N   1 
ATOM   1326 C CA  . ARG A 1 167 ? -5.272  -3.390  1.888   1.00 58.40  ? 167 ARG A CA  1 
ATOM   1327 C C   . ARG A 1 167 ? -5.248  -4.049  0.510   1.00 67.05  ? 167 ARG A C   1 
ATOM   1328 O O   . ARG A 1 167 ? -4.421  -3.697  -0.342  1.00 63.36  ? 167 ARG A O   1 
ATOM   1329 C CB  . ARG A 1 167 ? -4.850  -4.381  2.970   1.00 57.57  ? 167 ARG A CB  1 
ATOM   1330 C CG  . ARG A 1 167 ? -3.394  -4.809  2.919   1.00 57.84  ? 167 ARG A CG  1 
ATOM   1331 C CD  . ARG A 1 167 ? -3.152  -5.880  3.973   1.00 58.71  ? 167 ARG A CD  1 
ATOM   1332 N NE  . ARG A 1 167 ? -1.742  -6.093  4.282   1.00 54.18  ? 167 ARG A NE  1 
ATOM   1333 C CZ  . ARG A 1 167 ? -0.876  -6.711  3.488   1.00 54.11  ? 167 ARG A CZ  1 
ATOM   1334 N NH1 . ARG A 1 167 ? -1.239  -7.196  2.311   1.00 50.27  ? 167 ARG A NH1 1 
ATOM   1335 N NH2 . ARG A 1 167 ? 0.381   -6.863  3.895   1.00 53.64  ? 167 ARG A NH2 1 
ATOM   1336 N N   . THR A 1 168 ? -6.145  -5.014  0.274   1.00 63.04  ? 168 THR A N   1 
ATOM   1337 C CA  . THR A 1 168 ? -6.205  -5.650  -1.046  1.00 66.65  ? 168 THR A CA  1 
ATOM   1338 C C   . THR A 1 168 ? -6.563  -4.648  -2.139  1.00 68.43  ? 168 THR A C   1 
ATOM   1339 O O   . THR A 1 168 ? -6.028  -4.713  -3.255  1.00 70.48  ? 168 THR A O   1 
ATOM   1340 C CB  . THR A 1 168 ? -7.209  -6.808  -1.054  1.00 70.45  ? 168 THR A CB  1 
ATOM   1341 O OG1 . THR A 1 168 ? -8.526  -6.300  -1.307  1.00 85.36  ? 168 THR A OG1 1 
ATOM   1342 C CG2 . THR A 1 168 ? -7.186  -7.596  0.232   1.00 57.26  ? 168 THR A CG2 1 
ATOM   1343 N N   . GLN A 1 169 ? -7.500  -3.744  -1.855  1.00 67.62  ? 169 GLN A N   1 
ATOM   1344 C CA  . GLN A 1 169 ? -7.908  -2.778  -2.867  1.00 71.73  ? 169 GLN A CA  1 
ATOM   1345 C C   . GLN A 1 169 ? -6.823  -1.747  -3.162  1.00 73.96  ? 169 GLN A C   1 
ATOM   1346 O O   . GLN A 1 169 ? -6.870  -1.111  -4.216  1.00 78.89  ? 169 GLN A O   1 
ATOM   1347 C CB  . GLN A 1 169 ? -9.235  -2.143  -2.443  1.00 75.14  ? 169 GLN A CB  1 
ATOM   1348 C CG  . GLN A 1 169 ? -10.391 -3.110  -2.735  1.00 89.44  ? 169 GLN A CG  1 
ATOM   1349 C CD  . GLN A 1 169 ? -11.766 -2.597  -2.357  1.00 98.82  ? 169 GLN A CD  1 
ATOM   1350 O OE1 . GLN A 1 169 ? -11.924 -1.473  -1.908  1.00 98.06  ? 169 GLN A OE1 1 
ATOM   1351 N NE2 . GLN A 1 169 ? -12.780 -3.426  -2.573  1.00 106.83 ? 169 GLN A NE2 1 
ATOM   1352 N N   . ILE A 1 170 ? -5.846  -1.562  -2.267  1.00 70.79  ? 170 ILE A N   1 
ATOM   1353 C CA  . ILE A 1 170 ? -4.679  -0.756  -2.619  1.00 56.13  ? 170 ILE A CA  1 
ATOM   1354 C C   . ILE A 1 170 ? -3.684  -1.579  -3.429  1.00 62.17  ? 170 ILE A C   1 
ATOM   1355 O O   . ILE A 1 170 ? -3.210  -1.141  -4.485  1.00 68.51  ? 170 ILE A O   1 
ATOM   1356 C CB  . ILE A 1 170 ? -4.017  -0.167  -1.358  1.00 60.40  ? 170 ILE A CB  1 
ATOM   1357 C CG1 . ILE A 1 170 ? -4.829  1.011   -0.822  1.00 55.82  ? 170 ILE A CG1 1 
ATOM   1358 C CG2 . ILE A 1 170 ? -2.589  0.277   -1.682  1.00 57.87  ? 170 ILE A CG2 1 
ATOM   1359 C CD1 . ILE A 1 170 ? -4.375  1.494   0.546   1.00 52.95  ? 170 ILE A CD1 1 
ATOM   1360 N N   . LEU A 1 171 ? -3.366  -2.790  -2.958  1.00 56.67  ? 171 LEU A N   1 
ATOM   1361 C CA  . LEU A 1 171 ? -2.243  -3.555  -3.504  1.00 59.93  ? 171 LEU A CA  1 
ATOM   1362 C C   . LEU A 1 171 ? -2.538  -4.178  -4.870  1.00 73.57  ? 171 LEU A C   1 
ATOM   1363 O O   . LEU A 1 171 ? -1.594  -4.476  -5.621  1.00 69.49  ? 171 LEU A O   1 
ATOM   1364 C CB  . LEU A 1 171 ? -1.843  -4.652  -2.518  1.00 63.92  ? 171 LEU A CB  1 
ATOM   1365 C CG  . LEU A 1 171 ? -1.219  -4.186  -1.194  1.00 63.62  ? 171 LEU A CG  1 
ATOM   1366 C CD1 . LEU A 1 171 ? -0.621  -5.358  -0.427  1.00 58.08  ? 171 LEU A CD1 1 
ATOM   1367 C CD2 . LEU A 1 171 ? -0.167  -3.105  -1.427  1.00 58.24  ? 171 LEU A CD2 1 
ATOM   1368 N N   . GLN A 1 172 ? -3.812  -4.381  -5.216  1.00 67.79  ? 172 GLN A N   1 
ATOM   1369 C CA  . GLN A 1 172 ? -4.138  -4.875  -6.553  1.00 66.43  ? 172 GLN A CA  1 
ATOM   1370 C C   . GLN A 1 172 ? -3.562  -3.953  -7.616  1.00 75.96  ? 172 GLN A C   1 
ATOM   1371 O O   . GLN A 1 172 ? -3.105  -4.402  -8.675  1.00 76.89  ? 172 GLN A O   1 
ATOM   1372 C CB  . GLN A 1 172 ? -5.652  -4.993  -6.711  1.00 68.18  ? 172 GLN A CB  1 
ATOM   1373 N N   . TYR A 1 173 ? -3.558  -2.657  -7.328  1.00 72.37  ? 173 TYR A N   1 
ATOM   1374 C CA  . TYR A 1 173 ? -3.194  -1.556  -8.202  1.00 78.15  ? 173 TYR A CA  1 
ATOM   1375 C C   . TYR A 1 173 ? -1.713  -1.501  -8.555  1.00 80.75  ? 173 TYR A C   1 
ATOM   1376 O O   . TYR A 1 173 ? -1.334  -0.674  -9.393  1.00 82.43  ? 173 TYR A O   1 
ATOM   1377 C CB  . TYR A 1 173 ? -3.614  -0.264  -7.513  1.00 76.02  ? 173 TYR A CB  1 
ATOM   1378 C CG  . TYR A 1 173 ? -5.081  0.009   -7.673  1.00 86.93  ? 173 TYR A CG  1 
ATOM   1379 C CD1 . TYR A 1 173 ? -6.023  -0.729  -6.969  1.00 82.04  ? 173 TYR A CD1 1 
ATOM   1380 C CD2 . TYR A 1 173 ? -5.530  0.980   -8.547  1.00 95.26  ? 173 TYR A CD2 1 
ATOM   1381 C CE1 . TYR A 1 173 ? -7.376  -0.491  -7.123  1.00 86.92  ? 173 TYR A CE1 1 
ATOM   1382 C CE2 . TYR A 1 173 ? -6.874  1.230   -8.709  1.00 93.67  ? 173 TYR A CE2 1 
ATOM   1383 C CZ  . TYR A 1 173 ? -7.794  0.495   -7.997  1.00 96.73  ? 173 TYR A CZ  1 
ATOM   1384 O OH  . TYR A 1 173 ? -9.131  0.756   -8.170  1.00 85.72  ? 173 TYR A OH  1 
ATOM   1385 N N   . MET A 1 174 ? -0.869  -2.363  -7.998  1.00 80.07  ? 174 MET A N   1 
ATOM   1386 C CA  . MET A 1 174 ? 0.563   -2.189  -8.203  1.00 83.79  ? 174 MET A CA  1 
ATOM   1387 C C   . MET A 1 174 ? 1.132   -3.167  -9.216  1.00 77.00  ? 174 MET A C   1 
ATOM   1388 O O   . MET A 1 174 ? 0.693   -4.308  -9.285  1.00 89.55  ? 174 MET A O   1 
ATOM   1389 C CB  . MET A 1 174 ? 1.303   -2.357  -6.878  1.00 77.49  ? 174 MET A CB  1 
ATOM   1390 C CG  . MET A 1 174 ? 1.179   -1.183  -5.932  1.00 73.63  ? 174 MET A CG  1 
ATOM   1391 S SD  . MET A 1 174 ? 2.187   -1.508  -4.495  1.00 75.57  ? 174 MET A SD  1 
ATOM   1392 C CE  . MET A 1 174 ? 3.800   -1.574  -5.280  1.00 70.11  ? 174 MET A CE  1 
ATOM   1393 N N   . ARG B 1 4   ? 4.394   -7.178  43.416  1.00 68.72  ? 4   ARG B N   1 
ATOM   1394 C CA  . ARG B 1 4   ? 4.783   -8.419  42.750  1.00 62.67  ? 4   ARG B CA  1 
ATOM   1395 C C   . ARG B 1 4   ? 5.514   -8.114  41.439  1.00 41.21  ? 4   ARG B C   1 
ATOM   1396 O O   . ARG B 1 4   ? 6.351   -8.905  40.999  1.00 43.09  ? 4   ARG B O   1 
ATOM   1397 C CB  . ARG B 1 4   ? 3.564   -9.325  42.505  1.00 56.92  ? 4   ARG B CB  1 
ATOM   1398 N N   . HIS B 1 5   ? 5.179   -6.993  40.792  1.00 39.30  ? 5   HIS B N   1 
ATOM   1399 C CA  . HIS B 1 5   ? 5.846   -6.666  39.536  1.00 34.24  ? 5   HIS B CA  1 
ATOM   1400 C C   . HIS B 1 5   ? 7.165   -5.937  39.751  1.00 36.16  ? 5   HIS B C   1 
ATOM   1401 O O   . HIS B 1 5   ? 8.050   -5.991  38.891  1.00 27.12  ? 5   HIS B O   1 
ATOM   1402 C CB  . HIS B 1 5   ? 4.939   -5.801  38.652  1.00 38.25  ? 5   HIS B CB  1 
ATOM   1403 C CG  . HIS B 1 5   ? 3.802   -6.553  38.036  1.00 44.77  ? 5   HIS B CG  1 
ATOM   1404 N ND1 . HIS B 1 5   ? 3.077   -6.063  36.971  1.00 49.70  ? 5   HIS B ND1 1 
ATOM   1405 C CD2 . HIS B 1 5   ? 3.278   -7.770  38.325  1.00 43.62  ? 5   HIS B CD2 1 
ATOM   1406 C CE1 . HIS B 1 5   ? 2.152   -6.944  36.632  1.00 48.36  ? 5   HIS B CE1 1 
ATOM   1407 N NE2 . HIS B 1 5   ? 2.251   -7.988  37.438  1.00 50.97  ? 5   HIS B NE2 1 
ATOM   1408 N N   . SER B 1 6   ? 7.327   -5.254  40.873  1.00 35.90  ? 6   SER B N   1 
ATOM   1409 C CA  . SER B 1 6   ? 8.465   -4.361  41.002  1.00 34.87  ? 6   SER B CA  1 
ATOM   1410 C C   . SER B 1 6   ? 8.713   -4.097  42.477  1.00 42.36  ? 6   SER B C   1 
ATOM   1411 O O   . SER B 1 6   ? 7.907   -4.451  43.342  1.00 37.72  ? 6   SER B O   1 
ATOM   1412 C CB  . SER B 1 6   ? 8.222   -3.068  40.227  1.00 35.34  ? 6   SER B CB  1 
ATOM   1413 O OG  . SER B 1 6   ? 7.185   -2.327  40.848  1.00 40.02  ? 6   SER B OG  1 
ATOM   1414 N N   . VAL B 1 7   ? 9.852   -3.481  42.750  1.00 27.71  ? 7   VAL B N   1 
ATOM   1415 C CA  . VAL B 1 7   ? 10.217  -3.061  44.097  1.00 34.53  ? 7   VAL B CA  1 
ATOM   1416 C C   . VAL B 1 7   ? 10.603  -1.590  43.992  1.00 34.92  ? 7   VAL B C   1 
ATOM   1417 O O   . VAL B 1 7   ? 11.315  -1.203  43.061  1.00 32.55  ? 7   VAL B O   1 
ATOM   1418 C CB  . VAL B 1 7   ? 11.376  -3.895  44.670  1.00 35.39  ? 7   VAL B CB  1 
ATOM   1419 C CG1 . VAL B 1 7   ? 11.925  -3.267  45.965  1.00 43.78  ? 7   VAL B CG1 1 
ATOM   1420 C CG2 . VAL B 1 7   ? 10.914  -5.332  44.927  1.00 35.29  ? 7   VAL B CG2 1 
ATOM   1421 N N   . VAL B 1 8   ? 10.073  -0.766  44.892  1.00 35.17  ? 8   VAL B N   1 
ATOM   1422 C CA  . VAL B 1 8   ? 10.372  0.659   44.922  1.00 30.89  ? 8   VAL B CA  1 
ATOM   1423 C C   . VAL B 1 8   ? 11.255  0.931   46.131  1.00 36.21  ? 8   VAL B C   1 
ATOM   1424 O O   . VAL B 1 8   ? 10.962  0.473   47.240  1.00 33.55  ? 8   VAL B O   1 
ATOM   1425 C CB  . VAL B 1 8   ? 9.092   1.516   44.975  1.00 34.76  ? 8   VAL B CB  1 
ATOM   1426 C CG1 . VAL B 1 8   ? 9.484   2.985   45.146  1.00 34.18  ? 8   VAL B CG1 1 
ATOM   1427 C CG2 . VAL B 1 8   ? 8.257   1.355   43.702  1.00 37.26  ? 8   VAL B CG2 1 
ATOM   1428 N N   . ARG B 1 9   ? 12.344  1.654   45.920  1.00 34.66  ? 9   ARG B N   1 
ATOM   1429 C CA  . ARG B 1 9   ? 13.188  2.120   47.013  1.00 37.03  ? 9   ARG B CA  1 
ATOM   1430 C C   . ARG B 1 9   ? 13.296  3.638   46.937  1.00 37.95  ? 9   ARG B C   1 
ATOM   1431 O O   . ARG B 1 9   ? 13.239  4.221   45.852  1.00 33.93  ? 9   ARG B O   1 
ATOM   1432 C CB  . ARG B 1 9   ? 14.556  1.449   46.956  1.00 37.16  ? 9   ARG B CB  1 
ATOM   1433 C CG  . ARG B 1 9   ? 15.411  1.902   45.812  1.00 35.20  ? 9   ARG B CG  1 
ATOM   1434 C CD  . ARG B 1 9   ? 16.764  1.230   45.867  1.00 47.76  ? 9   ARG B CD  1 
ATOM   1435 N NE  . ARG B 1 9   ? 17.659  1.654   44.795  1.00 40.70  ? 9   ARG B NE  1 
ATOM   1436 C CZ  . ARG B 1 9   ? 17.602  1.203   43.545  1.00 48.87  ? 9   ARG B CZ  1 
ATOM   1437 N NH1 . ARG B 1 9   ? 16.654  0.362   43.151  1.00 37.54  ? 9   ARG B NH1 1 
ATOM   1438 N NH2 . ARG B 1 9   ? 18.527  1.597   42.668  1.00 44.62  ? 9   ARG B NH2 1 
ATOM   1439 N N   . VAL B 1 10  ? 13.348  4.280   48.096  1.00 33.56  ? 10  VAL B N   1 
ATOM   1440 C CA  . VAL B 1 10  ? 13.366  5.733   48.190  1.00 36.53  ? 10  VAL B CA  1 
ATOM   1441 C C   . VAL B 1 10  ? 14.761  6.144   48.620  1.00 47.10  ? 10  VAL B C   1 
ATOM   1442 O O   . VAL B 1 10  ? 15.231  5.733   49.685  1.00 42.81  ? 10  VAL B O   1 
ATOM   1443 C CB  . VAL B 1 10  ? 12.305  6.258   49.167  1.00 41.66  ? 10  VAL B CB  1 
ATOM   1444 C CG1 . VAL B 1 10  ? 12.448  7.789   49.330  1.00 43.91  ? 10  VAL B CG1 1 
ATOM   1445 C CG2 . VAL B 1 10  ? 10.920  5.902   48.662  1.00 38.47  ? 10  VAL B CG2 1 
ATOM   1446 N N   . GLU B 1 11  ? 15.423  6.948   47.796  1.00 40.24  ? 11  GLU B N   1 
ATOM   1447 C CA  . GLU B 1 11  ? 16.779  7.424   48.062  1.00 44.37  ? 11  GLU B CA  1 
ATOM   1448 C C   . GLU B 1 11  ? 16.752  8.950   47.971  1.00 47.42  ? 11  GLU B C   1 
ATOM   1449 O O   . GLU B 1 11  ? 16.766  9.513   46.873  1.00 43.08  ? 11  GLU B O   1 
ATOM   1450 C CB  . GLU B 1 11  ? 17.755  6.796   47.073  1.00 45.47  ? 11  GLU B CB  1 
ATOM   1451 C CG  . GLU B 1 11  ? 17.846  5.282   47.252  1.00 50.48  ? 11  GLU B CG  1 
ATOM   1452 C CD  . GLU B 1 11  ? 18.833  4.622   46.308  1.00 65.57  ? 11  GLU B CD  1 
ATOM   1453 O OE1 . GLU B 1 11  ? 19.399  5.330   45.447  1.00 62.26  ? 11  GLU B OE1 1 
ATOM   1454 O OE2 . GLU B 1 11  ? 19.034  3.388   46.425  1.00 62.78  ? 11  GLU B OE2 1 
ATOM   1455 N N   . GLY B 1 12  ? 16.630  9.625   49.107  1.00 46.15  ? 12  GLY B N   1 
ATOM   1456 C CA  . GLY B 1 12  ? 16.563  11.079  49.038  1.00 41.68  ? 12  GLY B CA  1 
ATOM   1457 C C   . GLY B 1 12  ? 15.230  11.519  48.463  1.00 40.81  ? 12  GLY B C   1 
ATOM   1458 O O   . GLY B 1 12  ? 14.157  11.052  48.866  1.00 44.44  ? 12  GLY B O   1 
ATOM   1459 N N   . ASP B 1 13  ? 15.280  12.421  47.490  1.00 35.79  ? 13  ASP B N   1 
ATOM   1460 C CA  . ASP B 1 13  ? 14.059  12.898  46.868  1.00 37.60  ? 13  ASP B CA  1 
ATOM   1461 C C   . ASP B 1 13  ? 13.719  12.102  45.620  1.00 33.18  ? 13  ASP B C   1 
ATOM   1462 O O   . ASP B 1 13  ? 12.950  12.580  44.781  1.00 33.52  ? 13  ASP B O   1 
ATOM   1463 C CB  . ASP B 1 13  ? 14.179  14.391  46.547  1.00 37.84  ? 13  ASP B CB  1 
ATOM   1464 C CG  . ASP B 1 13  ? 15.342  14.696  45.631  1.00 49.35  ? 13  ASP B CG  1 
ATOM   1465 O OD1 . ASP B 1 13  ? 15.893  13.745  45.027  1.00 46.54  ? 13  ASP B OD1 1 
ATOM   1466 O OD2 . ASP B 1 13  ? 15.737  15.877  45.539  1.00 62.57  ? 13  ASP B OD2 1 
ATOM   1467 N N   . ARG B 1 14  ? 14.292  10.909  45.467  1.00 31.78  ? 14  ARG B N   1 
ATOM   1468 C CA  . ARG B 1 14  ? 13.988  10.057  44.322  1.00 34.72  ? 14  ARG B CA  1 
ATOM   1469 C C   . ARG B 1 14  ? 13.421  8.719   44.765  1.00 33.84  ? 14  ARG B C   1 
ATOM   1470 O O   . ARG B 1 14  ? 13.866  8.133   45.758  1.00 32.72  ? 14  ARG B O   1 
ATOM   1471 C CB  . ARG B 1 14  ? 15.222  9.842   43.459  1.00 34.69  ? 14  ARG B CB  1 
ATOM   1472 C CG  . ARG B 1 14  ? 15.440  11.049  42.571  1.00 44.09  ? 14  ARG B CG  1 
ATOM   1473 C CD  . ARG B 1 14  ? 16.869  11.246  42.216  1.00 48.47  ? 14  ARG B CD  1 
ATOM   1474 N NE  . ARG B 1 14  ? 17.220  10.445  41.062  1.00 55.60  ? 14  ARG B NE  1 
ATOM   1475 C CZ  . ARG B 1 14  ? 17.681  10.946  39.926  1.00 50.50  ? 14  ARG B CZ  1 
ATOM   1476 N NH1 . ARG B 1 14  ? 17.849  12.249  39.764  1.00 45.82  ? 14  ARG B NH1 1 
ATOM   1477 N NH2 . ARG B 1 14  ? 17.971  10.117  38.928  1.00 47.21  ? 14  ARG B NH2 1 
ATOM   1478 N N   . ALA B 1 15  ? 12.426  8.257   44.020  1.00 29.86  ? 15  ALA B N   1 
ATOM   1479 C CA  . ALA B 1 15  ? 11.898  6.905   44.136  1.00 31.33  ? 15  ALA B CA  1 
ATOM   1480 C C   . ALA B 1 15  ? 12.407  6.116   42.940  1.00 31.75  ? 15  ALA B C   1 
ATOM   1481 O O   . ALA B 1 15  ? 12.291  6.570   41.794  1.00 28.36  ? 15  ALA B O   1 
ATOM   1482 C CB  . ALA B 1 15  ? 10.368  6.896   44.175  1.00 31.03  ? 15  ALA B CB  1 
ATOM   1483 N N   . ILE B 1 16  ? 12.994  4.953   43.205  1.00 28.24  ? 16  ILE B N   1 
ATOM   1484 C CA  . ILE B 1 16  ? 13.581  4.129   42.159  1.00 26.64  ? 16  ILE B CA  1 
ATOM   1485 C C   . ILE B 1 16  ? 12.803  2.819   42.096  1.00 31.66  ? 16  ILE B C   1 
ATOM   1486 O O   . ILE B 1 16  ? 12.762  2.066   43.074  1.00 30.66  ? 16  ILE B O   1 
ATOM   1487 C CB  . ILE B 1 16  ? 15.072  3.903   42.420  1.00 32.54  ? 16  ILE B CB  1 
ATOM   1488 C CG1 . ILE B 1 16  ? 15.729  5.269   42.675  1.00 38.18  ? 16  ILE B CG1 1 
ATOM   1489 C CG2 . ILE B 1 16  ? 15.688  3.202   41.232  1.00 34.53  ? 16  ILE B CG2 1 
ATOM   1490 C CD1 . ILE B 1 16  ? 17.220  5.222   42.866  1.00 44.64  ? 16  ILE B CD1 1 
ATOM   1491 N N   . LYS B 1 17  ? 12.173  2.563   40.960  1.00 26.43  ? 17  LYS B N   1 
ATOM   1492 C CA  . LYS B 1 17  ? 11.298  1.413   40.779  1.00 30.22  ? 17  LYS B CA  1 
ATOM   1493 C C   . LYS B 1 17  ? 12.004  0.410   39.879  1.00 29.78  ? 17  LYS B C   1 
ATOM   1494 O O   . LYS B 1 17  ? 12.382  0.760   38.762  1.00 27.18  ? 17  LYS B O   1 
ATOM   1495 C CB  . LYS B 1 17  ? 9.980   1.866   40.153  1.00 30.00  ? 17  LYS B CB  1 
ATOM   1496 C CG  . LYS B 1 17  ? 8.933   0.789   39.972  1.00 29.10  ? 17  LYS B CG  1 
ATOM   1497 C CD  . LYS B 1 17  ? 7.630   1.452   39.514  1.00 31.22  ? 17  LYS B CD  1 
ATOM   1498 C CE  . LYS B 1 17  ? 6.402   0.759   40.047  1.00 44.68  ? 17  LYS B CE  1 
ATOM   1499 N NZ  . LYS B 1 17  ? 5.159   1.495   39.623  1.00 40.91  ? 17  LYS B NZ  1 
ATOM   1500 N N   . GLN B 1 18  ? 12.234  -0.802  40.374  1.00 24.80  ? 18  GLN B N   1 
ATOM   1501 C CA  . GLN B 1 18  ? 12.880  -1.838  39.573  1.00 27.83  ? 18  GLN B CA  1 
ATOM   1502 C C   . GLN B 1 18  ? 11.922  -3.008  39.363  1.00 26.25  ? 18  GLN B C   1 
ATOM   1503 O O   . GLN B 1 18  ? 11.420  -3.583  40.334  1.00 28.16  ? 18  GLN B O   1 
ATOM   1504 C CB  . GLN B 1 18  ? 14.186  -2.310  40.219  1.00 24.81  ? 18  GLN B CB  1 
ATOM   1505 C CG  . GLN B 1 18  ? 14.984  -3.206  39.248  1.00 29.73  ? 18  GLN B CG  1 
ATOM   1506 C CD  . GLN B 1 18  ? 16.313  -3.677  39.765  1.00 30.73  ? 18  GLN B CD  1 
ATOM   1507 O OE1 . GLN B 1 18  ? 16.548  -3.745  40.975  1.00 34.85  ? 18  GLN B OE1 1 
ATOM   1508 N NE2 . GLN B 1 18  ? 17.193  -4.070  38.839  1.00 30.70  ? 18  GLN B NE2 1 
ATOM   1509 N N   . PHE B 1 19  ? 11.703  -3.374  38.099  1.00 23.58  ? 19  PHE B N   1 
ATOM   1510 C CA  . PHE B 1 19  ? 10.814  -4.462  37.686  1.00 25.77  ? 19  PHE B CA  1 
ATOM   1511 C C   . PHE B 1 19  ? 11.546  -5.787  37.514  1.00 25.77  ? 19  PHE B C   1 
ATOM   1512 O O   . PHE B 1 19  ? 12.727  -5.819  37.166  1.00 26.64  ? 19  PHE B O   1 
ATOM   1513 C CB  . PHE B 1 19  ? 10.166  -4.135  36.339  1.00 24.21  ? 19  PHE B CB  1 
ATOM   1514 C CG  . PHE B 1 19  ? 9.242   -2.967  36.378  1.00 26.76  ? 19  PHE B CG  1 
ATOM   1515 C CD1 . PHE B 1 19  ? 9.734   -1.667  36.420  1.00 24.64  ? 19  PHE B CD1 1 
ATOM   1516 C CD2 . PHE B 1 19  ? 7.882   -3.167  36.380  1.00 25.48  ? 19  PHE B CD2 1 
ATOM   1517 C CE1 . PHE B 1 19  ? 8.854   -0.577  36.454  1.00 28.20  ? 19  PHE B CE1 1 
ATOM   1518 C CE2 . PHE B 1 19  ? 6.998   -2.094  36.409  1.00 28.32  ? 19  PHE B CE2 1 
ATOM   1519 C CZ  . PHE B 1 19  ? 7.483   -0.807  36.460  1.00 27.48  ? 19  PHE B CZ  1 
ATOM   1520 N N   . PHE B 1 20  ? 10.826  -6.893  37.719  1.00 26.23  ? 20  PHE B N   1 
ATOM   1521 C CA  . PHE B 1 20  ? 11.367  -8.170  37.300  1.00 27.80  ? 20  PHE B CA  1 
ATOM   1522 C C   . PHE B 1 20  ? 11.358  -8.236  35.775  1.00 24.95  ? 20  PHE B C   1 
ATOM   1523 O O   . PHE B 1 20  ? 10.532  -7.586  35.119  1.00 25.87  ? 20  PHE B O   1 
ATOM   1524 C CB  . PHE B 1 20  ? 10.549  -9.345  37.852  1.00 25.86  ? 20  PHE B CB  1 
ATOM   1525 C CG  . PHE B 1 20  ? 10.636  -9.523  39.358  1.00 31.35  ? 20  PHE B CG  1 
ATOM   1526 C CD1 . PHE B 1 20  ? 11.720  -10.156 39.934  1.00 32.26  ? 20  PHE B CD1 1 
ATOM   1527 C CD2 . PHE B 1 20  ? 9.613   -9.066  40.188  1.00 38.41  ? 20  PHE B CD2 1 
ATOM   1528 C CE1 . PHE B 1 20  ? 11.804  -10.343 41.322  1.00 36.19  ? 20  PHE B CE1 1 
ATOM   1529 C CE2 . PHE B 1 20  ? 9.682   -9.240  41.566  1.00 37.88  ? 20  PHE B CE2 1 
ATOM   1530 C CZ  . PHE B 1 20  ? 10.779  -9.883  42.138  1.00 42.24  ? 20  PHE B CZ  1 
ATOM   1531 N N   . PRO B 1 21  ? 12.277  -9.014  35.187  1.00 29.31  ? 21  PRO B N   1 
ATOM   1532 C CA  . PRO B 1 21  ? 12.304  -9.140  33.715  1.00 29.56  ? 21  PRO B CA  1 
ATOM   1533 C C   . PRO B 1 21  ? 10.996  -9.639  33.123  1.00 29.81  ? 21  PRO B C   1 
ATOM   1534 O O   . PRO B 1 21  ? 10.666  -9.264  31.988  1.00 32.26  ? 21  PRO B O   1 
ATOM   1535 C CB  . PRO B 1 21  ? 13.442  -10.147 33.465  1.00 33.07  ? 21  PRO B CB  1 
ATOM   1536 C CG  . PRO B 1 21  ? 14.351  -9.981  34.678  1.00 35.02  ? 21  PRO B CG  1 
ATOM   1537 C CD  . PRO B 1 21  ? 13.401  -9.710  35.837  1.00 29.27  ? 21  PRO B CD  1 
ATOM   1538 N N   . ALA B 1 22  ? 10.232  -10.457 33.857  1.00 27.06  ? 22  ALA B N   1 
ATOM   1539 C CA  . ALA B 1 22  ? 8.946   -10.899 33.336  1.00 29.62  ? 22  ALA B CA  1 
ATOM   1540 C C   . ALA B 1 22  ? 8.006   -9.732  33.077  1.00 30.18  ? 22  ALA B C   1 
ATOM   1541 O O   . ALA B 1 22  ? 7.061   -9.881  32.305  1.00 28.33  ? 22  ALA B O   1 
ATOM   1542 C CB  . ALA B 1 22  ? 8.274   -11.846 34.322  1.00 28.79  ? 22  ALA B CB  1 
ATOM   1543 N N   . TYR B 1 23  ? 8.241   -8.574  33.689  1.00 24.86  ? 23  TYR B N   1 
ATOM   1544 C CA  . TYR B 1 23  ? 7.339   -7.426  33.581  1.00 30.50  ? 23  TYR B CA  1 
ATOM   1545 C C   . TYR B 1 23  ? 7.996   -6.275  32.831  1.00 26.67  ? 23  TYR B C   1 
ATOM   1546 O O   . TYR B 1 23  ? 7.709   -5.099  33.081  1.00 26.58  ? 23  TYR B O   1 
ATOM   1547 C CB  . TYR B 1 23  ? 6.866   -6.997  34.966  1.00 26.18  ? 23  TYR B CB  1 
ATOM   1548 C CG  . TYR B 1 23  ? 6.352   -8.209  35.722  1.00 31.68  ? 23  TYR B CG  1 
ATOM   1549 C CD1 . TYR B 1 23  ? 5.243   -8.917  35.266  1.00 34.08  ? 23  TYR B CD1 1 
ATOM   1550 C CD2 . TYR B 1 23  ? 7.018   -8.685  36.847  1.00 30.36  ? 23  TYR B CD2 1 
ATOM   1551 C CE1 . TYR B 1 23  ? 4.785   -10.034 35.934  1.00 37.34  ? 23  TYR B CE1 1 
ATOM   1552 C CE2 . TYR B 1 23  ? 6.575   -9.808  37.512  1.00 39.34  ? 23  TYR B CE2 1 
ATOM   1553 C CZ  . TYR B 1 23  ? 5.460   -10.472 37.056  1.00 43.76  ? 23  TYR B CZ  1 
ATOM   1554 O OH  . TYR B 1 23  ? 5.027   -11.579 37.739  1.00 43.80  ? 23  TYR B OH  1 
ATOM   1555 N N   . ARG B 1 24  ? 8.899   -6.621  31.910  1.00 23.20  ? 24  ARG B N   1 
ATOM   1556 C CA  . ARG B 1 24  ? 9.500   -5.649  30.997  1.00 24.50  ? 24  ARG B CA  1 
ATOM   1557 C C   . ARG B 1 24  ? 8.433   -4.801  30.302  1.00 31.06  ? 24  ARG B C   1 
ATOM   1558 O O   . ARG B 1 24  ? 8.617   -3.595  30.082  1.00 26.84  ? 24  ARG B O   1 
ATOM   1559 C CB  . ARG B 1 24  ? 10.342  -6.406  29.952  1.00 30.57  ? 24  ARG B CB  1 
ATOM   1560 C CG  . ARG B 1 24  ? 11.044  -5.526  28.890  1.00 36.11  ? 24  ARG B CG  1 
ATOM   1561 C CD  . ARG B 1 24  ? 12.138  -6.322  28.087  1.00 37.75  ? 24  ARG B CD  1 
ATOM   1562 N NE  . ARG B 1 24  ? 13.397  -6.487  28.818  1.00 39.45  ? 24  ARG B NE  1 
ATOM   1563 C CZ  . ARG B 1 24  ? 14.382  -5.587  28.868  1.00 51.08  ? 24  ARG B CZ  1 
ATOM   1564 N NH1 . ARG B 1 24  ? 14.325  -4.444  28.187  1.00 40.23  ? 24  ARG B NH1 1 
ATOM   1565 N NH2 . ARG B 1 24  ? 15.445  -5.830  29.635  1.00 45.43  ? 24  ARG B NH2 1 
ATOM   1566 N N   A TYR B 1 25  ? 7.324   -5.451  29.926  0.49 30.94  ? 25  TYR B N   1 
ATOM   1567 N N   B TYR B 1 25  ? 7.294   -5.377  29.955  0.51 30.99  ? 25  TYR B N   1 
ATOM   1568 C CA  A TYR B 1 25  ? 6.188   -4.783  29.296  0.49 30.93  ? 25  TYR B CA  1 
ATOM   1569 C CA  B TYR B 1 25  ? 6.368   -4.491  29.254  0.51 30.49  ? 25  TYR B CA  1 
ATOM   1570 C C   A TYR B 1 25  ? 5.635   -3.673  30.186  0.49 31.73  ? 25  TYR B C   1 
ATOM   1571 C C   B TYR B 1 25  ? 5.577   -3.606  30.203  0.51 31.77  ? 25  TYR B C   1 
ATOM   1572 O O   A TYR B 1 25  ? 5.336   -2.568  29.707  0.49 26.89  ? 25  TYR B O   1 
ATOM   1573 O O   B TYR B 1 25  ? 5.070   -2.556  29.776  0.51 27.31  ? 25  TYR B O   1 
ATOM   1574 C CB  A TYR B 1 25  ? 5.127   -5.850  28.966  0.49 32.27  ? 25  TYR B CB  1 
ATOM   1575 C CB  B TYR B 1 25  ? 5.494   -5.309  28.310  0.51 32.30  ? 25  TYR B CB  1 
ATOM   1576 C CG  A TYR B 1 25  ? 3.861   -5.365  28.313  0.49 33.61  ? 25  TYR B CG  1 
ATOM   1577 C CG  B TYR B 1 25  ? 6.376   -5.824  27.207  0.51 33.98  ? 25  TYR B CG  1 
ATOM   1578 C CD1 A TYR B 1 25  ? 3.824   -5.054  26.955  0.49 36.41  ? 25  TYR B CD1 1 
ATOM   1579 C CD1 B TYR B 1 25  ? 7.200   -4.948  26.499  0.51 32.99  ? 25  TYR B CD1 1 
ATOM   1580 C CD2 A TYR B 1 25  ? 2.686   -5.270  29.041  0.49 38.90  ? 25  TYR B CD2 1 
ATOM   1581 C CD2 B TYR B 1 25  ? 6.487   -7.179  26.953  0.51 36.33  ? 25  TYR B CD2 1 
ATOM   1582 C CE1 A TYR B 1 25  ? 2.662   -4.604  26.356  0.49 38.05  ? 25  TYR B CE1 1 
ATOM   1583 C CE1 B TYR B 1 25  ? 8.053   -5.403  25.529  0.51 33.05  ? 25  TYR B CE1 1 
ATOM   1584 C CE2 A TYR B 1 25  ? 1.518   -4.847  28.443  0.49 42.74  ? 25  TYR B CE2 1 
ATOM   1585 C CE2 B TYR B 1 25  ? 7.332   -7.654  25.971  0.51 35.50  ? 25  TYR B CE2 1 
ATOM   1586 C CZ  A TYR B 1 25  ? 1.510   -4.510  27.106  0.49 41.71  ? 25  TYR B CZ  1 
ATOM   1587 C CZ  B TYR B 1 25  ? 8.115   -6.763  25.263  0.51 39.71  ? 25  TYR B CZ  1 
ATOM   1588 O OH  A TYR B 1 25  ? 0.339   -4.078  26.520  0.49 49.13  ? 25  TYR B OH  1 
ATOM   1589 O OH  B TYR B 1 25  ? 8.965   -7.235  24.285  0.51 47.66  ? 25  TYR B OH  1 
ATOM   1590 N N   . ASN B 1 26  ? 5.551   -3.930  31.495  1.00 24.63  ? 26  ASN B N   1 
ATOM   1591 C CA  . ASN B 1 26  ? 4.997   -2.961  32.431  1.00 23.67  ? 26  ASN B CA  1 
ATOM   1592 C C   . ASN B 1 26  ? 5.981   -1.820  32.711  1.00 27.57  ? 26  ASN B C   1 
ATOM   1593 O O   . ASN B 1 26  ? 5.553   -0.681  32.960  1.00 26.02  ? 26  ASN B O   1 
ATOM   1594 C CB  . ASN B 1 26  ? 4.616   -3.642  33.750  1.00 27.30  ? 26  ASN B CB  1 
ATOM   1595 C CG  . ASN B 1 26  ? 3.543   -4.702  33.579  1.00 42.21  ? 26  ASN B CG  1 
ATOM   1596 O OD1 . ASN B 1 26  ? 3.846   -5.895  33.465  1.00 38.51  ? 26  ASN B OD1 1 
ATOM   1597 N ND2 . ASN B 1 26  ? 2.285   -4.264  33.478  1.00 34.65  ? 26  ASN B ND2 1 
ATOM   1598 N N   . PHE B 1 27  ? 7.285   -2.124  32.709  1.00 23.90  ? 27  PHE B N   1 
ATOM   1599 C CA  . PHE B 1 27  ? 8.337   -1.102  32.762  1.00 22.33  ? 27  PHE B CA  1 
ATOM   1600 C C   . PHE B 1 27  ? 8.152   -0.060  31.650  1.00 24.89  ? 27  PHE B C   1 
ATOM   1601 O O   . PHE B 1 27  ? 8.213   1.155   31.897  1.00 23.66  ? 27  PHE B O   1 
ATOM   1602 C CB  . PHE B 1 27  ? 9.700   -1.797  32.636  1.00 24.49  ? 27  PHE B CB  1 
ATOM   1603 C CG  . PHE B 1 27  ? 10.839  -0.866  32.225  1.00 21.82  ? 27  PHE B CG  1 
ATOM   1604 C CD1 . PHE B 1 27  ? 11.544  -0.149  33.183  1.00 22.75  ? 27  PHE B CD1 1 
ATOM   1605 C CD2 . PHE B 1 27  ? 11.223  -0.755  30.887  1.00 23.44  ? 27  PHE B CD2 1 
ATOM   1606 C CE1 . PHE B 1 27  ? 12.609  0.679   32.820  1.00 23.43  ? 27  PHE B CE1 1 
ATOM   1607 C CE2 . PHE B 1 27  ? 12.290  0.093   30.496  1.00 22.71  ? 27  PHE B CE2 1 
ATOM   1608 C CZ  . PHE B 1 27  ? 12.983  0.797   31.469  1.00 23.35  ? 27  PHE B CZ  1 
ATOM   1609 N N   . TRP B 1 28  ? 7.892   -0.522  30.420  1.00 22.56  ? 28  TRP B N   1 
ATOM   1610 C CA  . TRP B 1 28  ? 7.771   0.431   29.313  1.00 20.48  ? 28  TRP B CA  1 
ATOM   1611 C C   . TRP B 1 28  ? 6.471   1.216   29.397  1.00 22.88  ? 28  TRP B C   1 
ATOM   1612 O O   . TRP B 1 28  ? 6.426   2.396   28.989  1.00 26.83  ? 28  TRP B O   1 
ATOM   1613 C CB  . TRP B 1 28  ? 7.879   -0.301  27.967  1.00 21.52  ? 28  TRP B CB  1 
ATOM   1614 C CG  . TRP B 1 28  ? 9.299   -0.746  27.623  1.00 24.20  ? 28  TRP B CG  1 
ATOM   1615 C CD1 . TRP B 1 28  ? 9.749   -2.028  27.452  1.00 24.38  ? 28  TRP B CD1 1 
ATOM   1616 C CD2 . TRP B 1 28  ? 10.418  0.110   27.386  1.00 23.80  ? 28  TRP B CD2 1 
ATOM   1617 N NE1 . TRP B 1 28  ? 11.095  -2.009  27.128  1.00 25.75  ? 28  TRP B NE1 1 
ATOM   1618 C CE2 . TRP B 1 28  ? 11.523  -0.711  27.099  1.00 26.36  ? 28  TRP B CE2 1 
ATOM   1619 C CE3 . TRP B 1 28  ? 10.596  1.503   27.425  1.00 24.34  ? 28  TRP B CE3 1 
ATOM   1620 C CZ2 . TRP B 1 28  ? 12.787  -0.192  26.821  1.00 26.89  ? 28  TRP B CZ2 1 
ATOM   1621 C CZ3 . TRP B 1 28  ? 11.854  2.021   27.135  1.00 25.58  ? 28  TRP B CZ3 1 
ATOM   1622 C CH2 . TRP B 1 28  ? 12.931  1.161   26.854  1.00 23.94  ? 28  TRP B CH2 1 
ATOM   1623 N N   . LYS B 1 29  ? 5.400   0.607   29.923  1.00 23.69  ? 29  LYS B N   1 
ATOM   1624 C CA  . LYS B 1 29  ? 4.167   1.373   30.097  1.00 26.36  ? 29  LYS B CA  1 
ATOM   1625 C C   . LYS B 1 29  ? 4.335   2.456   31.154  1.00 30.57  ? 29  LYS B C   1 
ATOM   1626 O O   . LYS B 1 29  ? 3.896   3.595   30.959  1.00 31.03  ? 29  LYS B O   1 
ATOM   1627 C CB  . LYS B 1 29  ? 2.999   0.469   30.481  1.00 27.40  ? 29  LYS B CB  1 
ATOM   1628 C CG  . LYS B 1 29  ? 2.500   -0.543  29.445  1.00 26.29  ? 29  LYS B CG  1 
ATOM   1629 C CD  . LYS B 1 29  ? 1.272   -1.287  30.059  1.00 40.29  ? 29  LYS B CD  1 
ATOM   1630 C CE  . LYS B 1 29  ? 0.344   -1.941  28.979  1.00 40.00  ? 29  LYS B CE  1 
ATOM   1631 N NZ  . LYS B 1 29  ? -0.414  -0.996  28.100  1.00 50.27  ? 29  LYS B NZ  1 
ATOM   1632 N N   . GLU B 1 30  ? 4.957   2.123   32.284  1.00 24.77  ? 30  GLU B N   1 
ATOM   1633 C CA  . GLU B 1 30  ? 5.252   3.134   33.293  1.00 30.27  ? 30  GLU B CA  1 
ATOM   1634 C C   . GLU B 1 30  ? 6.105   4.245   32.699  1.00 31.53  ? 30  GLU B C   1 
ATOM   1635 O O   . GLU B 1 30  ? 5.806   5.434   32.872  1.00 26.43  ? 30  GLU B O   1 
ATOM   1636 C CB  . GLU B 1 30  ? 5.994   2.530   34.491  1.00 28.11  ? 30  GLU B CB  1 
ATOM   1637 C CG  . GLU B 1 30  ? 6.231   3.552   35.628  1.00 32.23  ? 30  GLU B CG  1 
ATOM   1638 C CD  . GLU B 1 30  ? 5.234   3.409   36.794  1.00 42.90  ? 30  GLU B CD  1 
ATOM   1639 O OE1 . GLU B 1 30  ? 4.878   2.258   37.150  1.00 47.51  ? 30  GLU B OE1 1 
ATOM   1640 O OE2 . GLU B 1 30  ? 4.758   4.437   37.308  1.00 48.52  ? 30  GLU B OE2 1 
ATOM   1641 N N   . ALA B 1 31  ? 7.185   3.876   31.994  1.00 26.41  ? 31  ALA B N   1 
ATOM   1642 C CA  . ALA B 1 31  ? 8.033   4.911   31.399  1.00 25.48  ? 31  ALA B CA  1 
ATOM   1643 C C   . ALA B 1 31  ? 7.251   5.740   30.375  1.00 22.87  ? 31  ALA B C   1 
ATOM   1644 O O   . ALA B 1 31  ? 7.383   6.977   30.314  1.00 21.95  ? 31  ALA B O   1 
ATOM   1645 C CB  . ALA B 1 31  ? 9.244   4.260   30.713  1.00 21.20  ? 31  ALA B CB  1 
ATOM   1646 N N   . GLY B 1 32  ? 6.472   5.055   29.543  1.00 20.75  ? 32  GLY B N   1 
ATOM   1647 C CA  . GLY B 1 32  ? 5.766   5.717   28.457  1.00 22.39  ? 32  GLY B CA  1 
ATOM   1648 C C   . GLY B 1 32  ? 4.704   6.670   28.969  1.00 26.88  ? 32  GLY B C   1 
ATOM   1649 O O   . GLY B 1 32  ? 4.637   7.823   28.553  1.00 23.28  ? 32  GLY B O   1 
ATOM   1650 N N   . PHE B 1 33  ? 3.851   6.192   29.875  1.00 21.17  ? 33  PHE B N   1 
ATOM   1651 C CA  . PHE B 1 33  ? 2.762   7.050   30.330  1.00 25.24  ? 33  PHE B CA  1 
ATOM   1652 C C   . PHE B 1 33  ? 3.264   8.167   31.230  1.00 23.92  ? 33  PHE B C   1 
ATOM   1653 O O   . PHE B 1 33  ? 2.758   9.289   31.139  1.00 25.58  ? 33  PHE B O   1 
ATOM   1654 C CB  . PHE B 1 33  ? 1.676   6.207   31.000  1.00 25.17  ? 33  PHE B CB  1 
ATOM   1655 C CG  . PHE B 1 33  ? 0.909   5.380   30.004  1.00 23.63  ? 33  PHE B CG  1 
ATOM   1656 C CD1 . PHE B 1 33  ? 0.202   6.015   28.964  1.00 26.33  ? 33  PHE B CD1 1 
ATOM   1657 C CD2 . PHE B 1 33  ? 0.945   4.004   30.035  1.00 27.59  ? 33  PHE B CD2 1 
ATOM   1658 C CE1 . PHE B 1 33  ? -0.482  5.256   27.989  1.00 27.77  ? 33  PHE B CE1 1 
ATOM   1659 C CE2 . PHE B 1 33  ? 0.267   3.254   29.083  1.00 29.59  ? 33  PHE B CE2 1 
ATOM   1660 C CZ  . PHE B 1 33  ? -0.443  3.887   28.054  1.00 33.93  ? 33  PHE B CZ  1 
ATOM   1661 N N   . LEU B 1 34  ? 4.269   7.910   32.083  1.00 21.52  ? 34  LEU B N   1 
ATOM   1662 C CA  . LEU B 1 34  ? 4.849   9.025   32.848  1.00 22.13  ? 34  LEU B CA  1 
ATOM   1663 C C   . LEU B 1 34  ? 5.415   10.084  31.905  1.00 24.46  ? 34  LEU B C   1 
ATOM   1664 O O   . LEU B 1 34  ? 5.200   11.291  32.104  1.00 25.79  ? 34  LEU B O   1 
ATOM   1665 C CB  . LEU B 1 34  ? 5.944   8.520   33.805  1.00 24.43  ? 34  LEU B CB  1 
ATOM   1666 C CG  . LEU B 1 34  ? 5.473   7.820   35.084  1.00 22.98  ? 34  LEU B CG  1 
ATOM   1667 C CD1 . LEU B 1 34  ? 6.676   7.267   35.888  1.00 24.39  ? 34  LEU B CD1 1 
ATOM   1668 C CD2 . LEU B 1 34  ? 4.629   8.776   35.940  1.00 22.94  ? 34  LEU B CD2 1 
ATOM   1669 N N   . SER B 1 35  ? 6.102   9.640   30.839  1.00 22.25  ? 35  SER B N   1 
ATOM   1670 C CA  . SER B 1 35  ? 6.646   10.561  29.833  1.00 24.86  ? 35  SER B CA  1 
ATOM   1671 C C   . SER B 1 35  ? 5.555   11.417  29.213  1.00 24.03  ? 35  SER B C   1 
ATOM   1672 O O   . SER B 1 35  ? 5.681   12.646  29.134  1.00 24.39  ? 35  SER B O   1 
ATOM   1673 C CB  . SER B 1 35  ? 7.355   9.778   28.720  1.00 23.44  ? 35  SER B CB  1 
ATOM   1674 O OG  . SER B 1 35  ? 8.588   9.247   29.174  1.00 24.11  ? 35  SER B OG  1 
ATOM   1675 N N   . LEU B 1 36  ? 4.472   10.770  28.760  1.00 24.32  ? 36  LEU B N   1 
ATOM   1676 C CA  . LEU B 1 36  ? 3.355   11.457  28.127  1.00 23.45  ? 36  LEU B CA  1 
ATOM   1677 C C   . LEU B 1 36  ? 2.590   12.347  29.084  1.00 31.30  ? 36  LEU B C   1 
ATOM   1678 O O   . LEU B 1 36  ? 1.800   13.164  28.629  1.00 27.99  ? 36  LEU B O   1 
ATOM   1679 C CB  . LEU B 1 36  ? 2.372   10.453  27.516  1.00 23.68  ? 36  LEU B CB  1 
ATOM   1680 C CG  . LEU B 1 36  ? 2.871   9.647   26.332  1.00 24.77  ? 36  LEU B CG  1 
ATOM   1681 C CD1 . LEU B 1 36  ? 1.708   8.821   25.726  1.00 27.03  ? 36  LEU B CD1 1 
ATOM   1682 C CD2 . LEU B 1 36  ? 3.540   10.526  25.299  1.00 28.04  ? 36  LEU B CD2 1 
ATOM   1683 N N   . LEU B 1 37  ? 2.764   12.184  30.393  1.00 24.45  ? 37  LEU B N   1 
ATOM   1684 C CA  . LEU B 1 37  ? 2.077   13.031  31.357  1.00 24.17  ? 37  LEU B CA  1 
ATOM   1685 C C   . LEU B 1 37  ? 2.983   14.078  32.003  1.00 29.38  ? 37  LEU B C   1 
ATOM   1686 O O   . LEU B 1 37  ? 2.505   14.833  32.854  1.00 30.40  ? 37  LEU B O   1 
ATOM   1687 C CB  . LEU B 1 37  ? 1.422   12.147  32.427  1.00 26.14  ? 37  LEU B CB  1 
ATOM   1688 C CG  . LEU B 1 37  ? 0.341   11.259  31.810  1.00 28.47  ? 37  LEU B CG  1 
ATOM   1689 C CD1 . LEU B 1 37  ? -0.124  10.203  32.805  1.00 29.31  ? 37  LEU B CD1 1 
ATOM   1690 C CD2 . LEU B 1 37  ? -0.864  12.097  31.322  1.00 29.11  ? 37  LEU B CD2 1 
ATOM   1691 N N   . GLN B 1 38  ? 4.258   14.186  31.597  1.00 26.22  ? 38  GLN B N   1 
ATOM   1692 C CA  . GLN B 1 38  ? 5.124   15.184  32.230  1.00 24.37  ? 38  GLN B CA  1 
ATOM   1693 C C   . GLN B 1 38  ? 4.624   16.613  32.009  1.00 31.10  ? 38  GLN B C   1 
ATOM   1694 O O   . GLN B 1 38  ? 4.910   17.498  32.821  1.00 29.67  ? 38  GLN B O   1 
ATOM   1695 C CB  . GLN B 1 38  ? 6.560   15.074  31.703  1.00 26.73  ? 38  GLN B CB  1 
ATOM   1696 C CG  . GLN B 1 38  ? 7.302   13.784  32.139  1.00 24.61  ? 38  GLN B CG  1 
ATOM   1697 C CD  . GLN B 1 38  ? 7.435   13.667  33.642  1.00 25.09  ? 38  GLN B CD  1 
ATOM   1698 O OE1 . GLN B 1 38  ? 8.246   14.355  34.263  1.00 26.64  ? 38  GLN B OE1 1 
ATOM   1699 N NE2 . GLN B 1 38  ? 6.653   12.751  34.241  1.00 26.39  ? 38  GLN B NE2 1 
ATOM   1700 N N   . GLU B 1 39  ? 3.858   16.861  30.947  1.00 33.30  ? 39  GLU B N   1 
ATOM   1701 C CA  . GLU B 1 39  ? 3.324   18.205  30.774  1.00 40.73  ? 39  GLU B CA  1 
ATOM   1702 C C   . GLU B 1 39  ? 2.287   18.571  31.826  1.00 42.84  ? 39  GLU B C   1 
ATOM   1703 O O   . GLU B 1 39  ? 1.890   19.741  31.891  1.00 37.84  ? 39  GLU B O   1 
ATOM   1704 C CB  . GLU B 1 39  ? 2.743   18.352  29.372  1.00 47.43  ? 39  GLU B CB  1 
ATOM   1705 C CG  . GLU B 1 39  ? 1.434   17.621  29.162  1.00 44.81  ? 39  GLU B CG  1 
ATOM   1706 C CD  . GLU B 1 39  ? 0.726   18.048  27.879  1.00 51.65  ? 39  GLU B CD  1 
ATOM   1707 O OE1 . GLU B 1 39  ? 0.479   19.267  27.699  1.00 52.61  ? 39  GLU B OE1 1 
ATOM   1708 O OE2 . GLU B 1 39  ? 0.377   17.152  27.079  1.00 47.03  ? 39  GLU B OE2 1 
ATOM   1709 N N   . PHE B 1 40  ? 1.861   17.627  32.665  1.00 32.12  ? 40  PHE B N   1 
ATOM   1710 C CA  . PHE B 1 40  ? 0.902   17.905  33.726  1.00 34.51  ? 40  PHE B CA  1 
ATOM   1711 C C   . PHE B 1 40  ? 1.546   17.749  35.096  1.00 36.00  ? 40  PHE B C   1 
ATOM   1712 O O   . PHE B 1 40  ? 2.572   17.086  35.256  1.00 39.30  ? 40  PHE B O   1 
ATOM   1713 C CB  . PHE B 1 40  ? -0.325  16.995  33.598  1.00 32.20  ? 40  PHE B CB  1 
ATOM   1714 C CG  . PHE B 1 40  ? -0.951  17.050  32.244  1.00 41.76  ? 40  PHE B CG  1 
ATOM   1715 C CD1 . PHE B 1 40  ? -1.569  18.214  31.811  1.00 44.64  ? 40  PHE B CD1 1 
ATOM   1716 C CD2 . PHE B 1 40  ? -0.871  15.969  31.375  1.00 35.44  ? 40  PHE B CD2 1 
ATOM   1717 C CE1 . PHE B 1 40  ? -2.117  18.283  30.546  1.00 48.08  ? 40  PHE B CE1 1 
ATOM   1718 C CE2 . PHE B 1 40  ? -1.427  16.031  30.111  1.00 45.07  ? 40  PHE B CE2 1 
ATOM   1719 C CZ  . PHE B 1 40  ? -2.048  17.187  29.699  1.00 44.07  ? 40  PHE B CZ  1 
ATOM   1720 N N   . ASP B 1 41  ? 0.929   18.367  36.096  1.00 38.43  ? 41  ASP B N   1 
ATOM   1721 C CA  . ASP B 1 41  ? 1.512   18.364  37.429  1.00 41.99  ? 41  ASP B CA  1 
ATOM   1722 C C   . ASP B 1 41  ? 1.014   17.238  38.337  1.00 38.30  ? 41  ASP B C   1 
ATOM   1723 O O   . ASP B 1 41  ? 1.465   17.149  39.480  1.00 44.09  ? 41  ASP B O   1 
ATOM   1724 C CB  . ASP B 1 41  ? 1.318   19.754  38.070  1.00 51.27  ? 41  ASP B CB  1 
ATOM   1725 C CG  . ASP B 1 41  ? -0.128  20.050  38.460  1.00 58.05  ? 41  ASP B CG  1 
ATOM   1726 O OD1 . ASP B 1 41  ? -1.004  19.174  38.326  1.00 57.51  ? 41  ASP B OD1 1 
ATOM   1727 O OD2 . ASP B 1 41  ? -0.404  21.194  38.875  1.00 68.17  ? 41  ASP B OD2 1 
ATOM   1728 N N   . PHE B 1 42  ? 0.170   16.328  37.857  1.00 41.30  ? 42  PHE B N   1 
ATOM   1729 C CA  . PHE B 1 42  ? -0.406  15.321  38.741  1.00 34.68  ? 42  PHE B CA  1 
ATOM   1730 C C   . PHE B 1 42  ? 0.279   13.954  38.648  1.00 33.41  ? 42  PHE B C   1 
ATOM   1731 O O   . PHE B 1 42  ? -0.294  12.955  39.107  1.00 31.10  ? 42  PHE B O   1 
ATOM   1732 C CB  . PHE B 1 42  ? -1.911  15.206  38.494  1.00 37.07  ? 42  PHE B CB  1 
ATOM   1733 C CG  . PHE B 1 42  ? -2.283  14.945  37.062  1.00 36.63  ? 42  PHE B CG  1 
ATOM   1734 C CD1 . PHE B 1 42  ? -2.077  13.693  36.486  1.00 32.16  ? 42  PHE B CD1 1 
ATOM   1735 C CD2 . PHE B 1 42  ? -2.887  15.934  36.309  1.00 44.10  ? 42  PHE B CD2 1 
ATOM   1736 C CE1 . PHE B 1 42  ? -2.430  13.449  35.167  1.00 36.38  ? 42  PHE B CE1 1 
ATOM   1737 C CE2 . PHE B 1 42  ? -3.253  15.701  34.999  1.00 39.40  ? 42  PHE B CE2 1 
ATOM   1738 C CZ  . PHE B 1 42  ? -3.026  14.458  34.423  1.00 34.90  ? 42  PHE B CZ  1 
ATOM   1739 N N   . VAL B 1 43  ? 1.487   13.893  38.089  1.00 32.55  ? 43  VAL B N   1 
ATOM   1740 C CA  . VAL B 1 43  ? 2.322   12.689  38.115  1.00 28.21  ? 43  VAL B CA  1 
ATOM   1741 C C   . VAL B 1 43  ? 3.714   13.081  38.588  1.00 26.67  ? 43  VAL B C   1 
ATOM   1742 O O   . VAL B 1 43  ? 4.100   14.263  38.535  1.00 29.42  ? 43  VAL B O   1 
ATOM   1743 C CB  . VAL B 1 43  ? 2.414   12.012  36.721  1.00 29.49  ? 43  VAL B CB  1 
ATOM   1744 C CG1 . VAL B 1 43  ? 1.042   11.611  36.208  1.00 30.13  ? 43  VAL B CG1 1 
ATOM   1745 C CG2 . VAL B 1 43  ? 3.100   12.958  35.759  1.00 27.38  ? 43  VAL B CG2 1 
ATOM   1746 N N   . PRO B 1 44  ? 4.507   12.107  39.045  1.00 29.20  ? 44  PRO B N   1 
ATOM   1747 C CA  . PRO B 1 44  ? 5.896   12.403  39.409  1.00 26.20  ? 44  PRO B CA  1 
ATOM   1748 C C   . PRO B 1 44  ? 6.728   12.794  38.195  1.00 30.58  ? 44  PRO B C   1 
ATOM   1749 O O   . PRO B 1 44  ? 6.507   12.319  37.069  1.00 26.67  ? 44  PRO B O   1 
ATOM   1750 C CB  . PRO B 1 44  ? 6.419   11.078  40.011  1.00 29.38  ? 44  PRO B CB  1 
ATOM   1751 C CG  . PRO B 1 44  ? 5.244   10.185  40.182  1.00 32.49  ? 44  PRO B CG  1 
ATOM   1752 C CD  . PRO B 1 44  ? 4.145   10.692  39.267  1.00 31.13  ? 44  PRO B CD  1 
ATOM   1753 N N   . ARG B 1 45  ? 7.712   13.650  38.451  1.00 26.93  ? 45  ARG B N   1 
ATOM   1754 C CA  . ARG B 1 45  ? 8.751   13.932  37.474  1.00 30.80  ? 45  ARG B CA  1 
ATOM   1755 C C   . ARG B 1 45  ? 9.518   12.653  37.184  1.00 28.59  ? 45  ARG B C   1 
ATOM   1756 O O   . ARG B 1 45  ? 9.850   11.896  38.098  1.00 27.37  ? 45  ARG B O   1 
ATOM   1757 C CB  . ARG B 1 45  ? 9.718   14.991  38.016  1.00 25.15  ? 45  ARG B CB  1 
ATOM   1758 C CG  . ARG B 1 45  ? 9.126   16.352  38.422  1.00 30.48  ? 45  ARG B CG  1 
ATOM   1759 C CD  . ARG B 1 45  ? 8.342   17.016  37.290  1.00 30.87  ? 45  ARG B CD  1 
ATOM   1760 N NE  . ARG B 1 45  ? 6.965   16.529  37.240  1.00 31.88  ? 45  ARG B NE  1 
ATOM   1761 C CZ  . ARG B 1 45  ? 6.146   16.683  36.202  1.00 35.40  ? 45  ARG B CZ  1 
ATOM   1762 N NH1 . ARG B 1 45  ? 6.512   17.359  35.127  1.00 36.32  ? 45  ARG B NH1 1 
ATOM   1763 N NH2 . ARG B 1 45  ? 4.924   16.152  36.251  1.00 37.45  ? 45  ARG B NH2 1 
ATOM   1764 N N   . LEU B 1 46  ? 9.812   12.418  35.911  1.00 24.50  ? 46  LEU B N   1 
ATOM   1765 C CA  . LEU B 1 46  ? 10.600  11.271  35.472  1.00 25.03  ? 46  LEU B CA  1 
ATOM   1766 C C   . LEU B 1 46  ? 12.040  11.708  35.200  1.00 31.36  ? 46  LEU B C   1 
ATOM   1767 O O   . LEU B 1 46  ? 12.272  12.688  34.480  1.00 23.37  ? 46  LEU B O   1 
ATOM   1768 C CB  . LEU B 1 46  ? 9.953   10.665  34.227  1.00 21.08  ? 46  LEU B CB  1 
ATOM   1769 C CG  . LEU B 1 46  ? 10.631  9.515   33.523  1.00 25.66  ? 46  LEU B CG  1 
ATOM   1770 C CD1 . LEU B 1 46  ? 10.830  8.392   34.534  1.00 24.53  ? 46  LEU B CD1 1 
ATOM   1771 C CD2 . LEU B 1 46  ? 9.744   9.039   32.348  1.00 28.80  ? 46  LEU B CD2 1 
ATOM   1772 N N   . TYR B 1 47  ? 13.007  11.013  35.798  1.00 23.47  ? 47  TYR B N   1 
ATOM   1773 C CA  . TYR B 1 47  ? 14.398  11.453  35.686  1.00 23.61  ? 47  TYR B CA  1 
ATOM   1774 C C   . TYR B 1 47  ? 15.229  10.579  34.778  1.00 24.74  ? 47  TYR B C   1 
ATOM   1775 O O   . TYR B 1 47  ? 16.051  11.098  34.013  1.00 24.56  ? 47  TYR B O   1 
ATOM   1776 C CB  . TYR B 1 47  ? 15.065  11.491  37.062  1.00 23.60  ? 47  TYR B CB  1 
ATOM   1777 C CG  . TYR B 1 47  ? 14.392  12.421  38.017  1.00 30.33  ? 47  TYR B CG  1 
ATOM   1778 C CD1 . TYR B 1 47  ? 14.050  13.716  37.637  1.00 33.38  ? 47  TYR B CD1 1 
ATOM   1779 C CD2 . TYR B 1 47  ? 14.150  12.032  39.332  1.00 27.71  ? 47  TYR B CD2 1 
ATOM   1780 C CE1 . TYR B 1 47  ? 13.445  14.586  38.534  1.00 37.24  ? 47  TYR B CE1 1 
ATOM   1781 C CE2 . TYR B 1 47  ? 13.547  12.901  40.235  1.00 28.12  ? 47  TYR B CE2 1 
ATOM   1782 C CZ  . TYR B 1 47  ? 13.205  14.167  39.832  1.00 33.29  ? 47  TYR B CZ  1 
ATOM   1783 O OH  . TYR B 1 47  ? 12.604  15.000  40.747  1.00 33.43  ? 47  TYR B OH  1 
ATOM   1784 N N   . SER B 1 48  ? 15.005  9.262   34.788  1.00 24.96  ? 48  SER B N   1 
ATOM   1785 C CA  . SER B 1 48  ? 15.844  8.402   33.970  1.00 28.42  ? 48  SER B CA  1 
ATOM   1786 C C   . SER B 1 48  ? 15.166  7.054   33.810  1.00 28.26  ? 48  SER B C   1 
ATOM   1787 O O   . SER B 1 48  ? 14.267  6.685   34.573  1.00 27.33  ? 48  SER B O   1 
ATOM   1788 C CB  . SER B 1 48  ? 17.236  8.225   34.596  1.00 32.32  ? 48  SER B CB  1 
ATOM   1789 O OG  . SER B 1 48  ? 17.141  7.410   35.765  1.00 32.39  ? 48  SER B OG  1 
ATOM   1790 N N   . ILE B 1 49  ? 15.570  6.348   32.760  1.00 25.85  ? 49  ILE B N   1 
ATOM   1791 C CA  . ILE B 1 49  ? 15.176  4.956   32.577  1.00 27.98  ? 49  ILE B CA  1 
ATOM   1792 C C   . ILE B 1 49  ? 16.426  4.146   32.277  1.00 35.26  ? 49  ILE B C   1 
ATOM   1793 O O   . ILE B 1 49  ? 17.419  4.649   31.736  1.00 34.98  ? 49  ILE B O   1 
ATOM   1794 C CB  . ILE B 1 49  ? 14.133  4.781   31.473  1.00 24.14  ? 49  ILE B CB  1 
ATOM   1795 C CG1 . ILE B 1 49  ? 14.792  5.022   30.119  1.00 32.17  ? 49  ILE B CG1 1 
ATOM   1796 C CG2 . ILE B 1 49  ? 12.897  5.685   31.716  1.00 27.98  ? 49  ILE B CG2 1 
ATOM   1797 C CD1 . ILE B 1 49  ? 13.912  4.574   28.946  1.00 33.70  ? 49  ILE B CD1 1 
ATOM   1798 N N   . ASN B 1 50  ? 16.397  2.898   32.709  1.00 25.78  ? 50  ASN B N   1 
ATOM   1799 C CA  . ASN B 1 50  ? 17.503  1.986   32.484  1.00 27.13  ? 50  ASN B CA  1 
ATOM   1800 C C   . ASN B 1 50  ? 16.844  0.677   32.062  1.00 28.57  ? 50  ASN B C   1 
ATOM   1801 O O   . ASN B 1 50  ? 16.439  -0.135  32.905  1.00 25.41  ? 50  ASN B O   1 
ATOM   1802 C CB  . ASN B 1 50  ? 18.369  1.836   33.737  1.00 28.23  ? 50  ASN B CB  1 
ATOM   1803 C CG  . ASN B 1 50  ? 19.576  0.979   33.487  1.00 29.09  ? 50  ASN B CG  1 
ATOM   1804 O OD1 . ASN B 1 50  ? 19.554  0.130   32.599  1.00 31.62  ? 50  ASN B OD1 1 
ATOM   1805 N ND2 . ASN B 1 50  ? 20.629  1.173   34.263  1.00 30.82  ? 50  ASN B ND2 1 
ATOM   1806 N N   . PRO B 1 51  ? 16.719  0.446   30.748  1.00 28.36  ? 51  PRO B N   1 
ATOM   1807 C CA  . PRO B 1 51  ? 16.111  -0.803  30.267  1.00 26.96  ? 51  PRO B CA  1 
ATOM   1808 C C   . PRO B 1 51  ? 16.922  -2.040  30.580  1.00 28.13  ? 51  PRO B C   1 
ATOM   1809 O O   . PRO B 1 51  ? 16.348  -3.130  30.643  1.00 27.57  ? 51  PRO B O   1 
ATOM   1810 C CB  . PRO B 1 51  ? 16.030  -0.598  28.741  1.00 30.21  ? 51  PRO B CB  1 
ATOM   1811 C CG  . PRO B 1 51  ? 16.139  0.874   28.544  1.00 34.27  ? 51  PRO B CG  1 
ATOM   1812 C CD  . PRO B 1 51  ? 17.068  1.359   29.650  1.00 27.02  ? 51  PRO B CD  1 
ATOM   1813 N N   . GLU B 1 52  ? 18.235  -1.923  30.768  1.00 28.46  ? 52  GLU B N   1 
ATOM   1814 C CA  . GLU B 1 52  ? 19.001  -3.122  31.087  1.00 29.82  ? 52  GLU B CA  1 
ATOM   1815 C C   . GLU B 1 52  ? 18.666  -3.633  32.489  1.00 36.00  ? 52  GLU B C   1 
ATOM   1816 O O   . GLU B 1 52  ? 18.518  -4.846  32.698  1.00 30.95  ? 52  GLU B O   1 
ATOM   1817 C CB  . GLU B 1 52  ? 20.500  -2.849  30.930  1.00 30.33  ? 52  GLU B CB  1 
ATOM   1818 N N   . LYS B 1 53  ? 18.449  -2.726  33.441  1.00 29.58  ? 53  LYS B N   1 
ATOM   1819 C CA  . LYS B 1 53  ? 18.065  -3.106  34.796  1.00 29.83  ? 53  LYS B CA  1 
ATOM   1820 C C   . LYS B 1 53  ? 16.560  -3.047  35.015  1.00 27.24  ? 53  LYS B C   1 
ATOM   1821 O O   . LYS B 1 53  ? 16.099  -3.464  36.081  1.00 29.15  ? 53  LYS B O   1 
ATOM   1822 C CB  . LYS B 1 53  ? 18.744  -2.170  35.817  1.00 33.40  ? 53  LYS B CB  1 
ATOM   1823 C CG  . LYS B 1 53  ? 20.277  -2.068  35.617  1.00 41.15  ? 53  LYS B CG  1 
ATOM   1824 C CD  . LYS B 1 53  ? 21.057  -1.799  36.900  1.00 45.47  ? 53  LYS B CD  1 
ATOM   1825 C CE  . LYS B 1 53  ? 20.371  -0.784  37.798  1.00 54.27  ? 53  LYS B CE  1 
ATOM   1826 N NZ  . LYS B 1 53  ? 21.067  -0.662  39.123  1.00 66.09  ? 53  LYS B NZ  1 
ATOM   1827 N N   . LEU B 1 54  ? 15.795  -2.592  34.016  1.00 22.89  ? 54  LEU B N   1 
ATOM   1828 C CA  . LEU B 1 54  ? 14.365  -2.283  34.153  1.00 21.72  ? 54  LEU B CA  1 
ATOM   1829 C C   . LEU B 1 54  ? 14.110  -1.391  35.365  1.00 24.22  ? 54  LEU B C   1 
ATOM   1830 O O   . LEU B 1 54  ? 13.266  -1.689  36.214  1.00 24.45  ? 54  LEU B O   1 
ATOM   1831 C CB  . LEU B 1 54  ? 13.520  -3.571  34.229  1.00 23.62  ? 54  LEU B CB  1 
ATOM   1832 C CG  . LEU B 1 54  ? 13.651  -4.482  32.998  1.00 26.91  ? 54  LEU B CG  1 
ATOM   1833 C CD1 . LEU B 1 54  ? 12.941  -5.781  33.255  1.00 28.96  ? 54  LEU B CD1 1 
ATOM   1834 C CD2 . LEU B 1 54  ? 13.019  -3.817  31.770  1.00 28.11  ? 54  LEU B CD2 1 
ATOM   1835 N N   . GLU B 1 55  ? 14.886  -0.314  35.466  1.00 24.63  ? 55  GLU B N   1 
ATOM   1836 C CA  . GLU B 1 55  ? 14.782  0.631   36.575  1.00 24.20  ? 55  GLU B CA  1 
ATOM   1837 C C   . GLU B 1 55  ? 14.325  1.988   36.054  1.00 26.30  ? 55  GLU B C   1 
ATOM   1838 O O   . GLU B 1 55  ? 14.806  2.454   35.015  1.00 23.22  ? 55  GLU B O   1 
ATOM   1839 C CB  . GLU B 1 55  ? 16.133  0.786   37.283  1.00 34.10  ? 55  GLU B CB  1 
ATOM   1840 C CG  . GLU B 1 55  ? 16.005  0.786   38.778  1.00 41.60  ? 55  GLU B CG  1 
ATOM   1841 C CD  . GLU B 1 55  ? 17.350  0.683   39.482  1.00 48.60  ? 55  GLU B CD  1 
ATOM   1842 O OE1 . GLU B 1 55  ? 18.330  1.302   39.001  1.00 38.27  ? 55  GLU B OE1 1 
ATOM   1843 O OE2 . GLU B 1 55  ? 17.430  -0.100  40.456  1.00 40.50  ? 55  GLU B OE2 1 
ATOM   1844 N N   . ILE B 1 56  ? 13.382  2.606   36.773  1.00 23.51  ? 56  ILE B N   1 
ATOM   1845 C CA  . ILE B 1 56  ? 12.901  3.960   36.497  1.00 23.30  ? 56  ILE B CA  1 
ATOM   1846 C C   . ILE B 1 56  ? 13.180  4.820   37.726  1.00 28.41  ? 56  ILE B C   1 
ATOM   1847 O O   . ILE B 1 56  ? 12.869  4.410   38.844  1.00 26.27  ? 56  ILE B O   1 
ATOM   1848 C CB  . ILE B 1 56  ? 11.399  3.958   36.182  1.00 20.88  ? 56  ILE B CB  1 
ATOM   1849 C CG1 . ILE B 1 56  ? 11.080  3.038   35.001  1.00 24.90  ? 56  ILE B CG1 1 
ATOM   1850 C CG2 . ILE B 1 56  ? 10.919  5.354   35.800  1.00 24.53  ? 56  ILE B CG2 1 
ATOM   1851 C CD1 . ILE B 1 56  ? 9.629   3.152   34.599  1.00 30.28  ? 56  ILE B CD1 1 
ATOM   1852 N N   . GLU B 1 57  ? 13.827  5.967   37.530  1.00 23.14  ? 57  GLU B N   1 
ATOM   1853 C CA  . GLU B 1 57  ? 14.066  6.915   38.610  1.00 25.21  ? 57  GLU B CA  1 
ATOM   1854 C C   . GLU B 1 57  ? 13.138  8.098   38.430  1.00 27.71  ? 57  GLU B C   1 
ATOM   1855 O O   . GLU B 1 57  ? 13.095  8.700   37.340  1.00 25.94  ? 57  GLU B O   1 
ATOM   1856 C CB  . GLU B 1 57  ? 15.526  7.372   38.685  1.00 24.86  ? 57  GLU B CB  1 
ATOM   1857 C CG  . GLU B 1 57  ? 16.454  6.164   38.884  1.00 30.13  ? 57  GLU B CG  1 
ATOM   1858 C CD  . GLU B 1 57  ? 17.854  6.534   39.373  1.00 47.42  ? 57  GLU B CD  1 
ATOM   1859 O OE1 . GLU B 1 57  ? 18.050  7.691   39.818  1.00 39.92  ? 57  GLU B OE1 1 
ATOM   1860 O OE2 . GLU B 1 57  ? 18.750  5.654   39.298  1.00 41.95  ? 57  GLU B OE2 1 
ATOM   1861 N N   . MET B 1 58  ? 12.375  8.411   39.479  1.00 28.28  ? 58  MET B N   1 
ATOM   1862 C CA  . MET B 1 58  ? 11.387  9.483   39.398  1.00 27.21  ? 58  MET B CA  1 
ATOM   1863 C C   . MET B 1 58  ? 11.373  10.237  40.713  1.00 28.58  ? 58  MET B C   1 
ATOM   1864 O O   . MET B 1 58  ? 12.080  9.890   41.669  1.00 26.13  ? 58  MET B O   1 
ATOM   1865 C CB  . MET B 1 58  ? 9.986   8.941   39.101  1.00 28.16  ? 58  MET B CB  1 
ATOM   1866 C CG  . MET B 1 58  ? 9.473   7.959   40.125  1.00 35.29  ? 58  MET B CG  1 
ATOM   1867 S SD  . MET B 1 58  ? 7.958   7.147   39.490  1.00 45.17  ? 58  MET B SD  1 
ATOM   1868 C CE  . MET B 1 58  ? 8.675   5.887   38.536  1.00 34.10  ? 58  MET B CE  1 
ATOM   1869 N N   . GLU B 1 59  ? 10.548  11.279  40.749  1.00 28.50  ? 59  GLU B N   1 
ATOM   1870 C CA  . GLU B 1 59  ? 10.364  12.078  41.959  1.00 26.31  ? 59  GLU B CA  1 
ATOM   1871 C C   . GLU B 1 59  ? 9.725   11.240  43.066  1.00 27.93  ? 59  GLU B C   1 
ATOM   1872 O O   . GLU B 1 59  ? 8.704   10.584  42.838  1.00 27.47  ? 59  GLU B O   1 
ATOM   1873 C CB  . GLU B 1 59  ? 9.444   13.247  41.616  1.00 25.04  ? 59  GLU B CB  1 
ATOM   1874 C CG  . GLU B 1 59  ? 9.321   14.320  42.628  1.00 27.11  ? 59  GLU B CG  1 
ATOM   1875 C CD  . GLU B 1 59  ? 8.178   15.270  42.252  1.00 34.80  ? 59  GLU B CD  1 
ATOM   1876 O OE1 . GLU B 1 59  ? 7.563   15.079  41.174  1.00 32.94  ? 59  GLU B OE1 1 
ATOM   1877 O OE2 . GLU B 1 59  ? 7.871   16.160  43.057  1.00 34.61  ? 59  GLU B OE2 1 
ATOM   1878 N N   . PHE B 1 60  ? 10.305  11.277  44.274  1.00 31.71  ? 60  PHE B N   1 
ATOM   1879 C CA  . PHE B 1 60  ? 9.588   10.811  45.460  1.00 31.59  ? 60  PHE B CA  1 
ATOM   1880 C C   . PHE B 1 60  ? 8.475   11.794  45.804  1.00 35.66  ? 60  PHE B C   1 
ATOM   1881 O O   . PHE B 1 60  ? 8.715   13.004  45.884  1.00 31.33  ? 60  PHE B O   1 
ATOM   1882 C CB  . PHE B 1 60  ? 10.534  10.696  46.666  1.00 36.41  ? 60  PHE B CB  1 
ATOM   1883 C CG  . PHE B 1 60  ? 9.822   10.327  47.957  1.00 36.91  ? 60  PHE B CG  1 
ATOM   1884 C CD1 . PHE B 1 60  ? 9.199   9.099   48.100  1.00 44.15  ? 60  PHE B CD1 1 
ATOM   1885 C CD2 . PHE B 1 60  ? 9.716   11.246  48.989  1.00 46.46  ? 60  PHE B CD2 1 
ATOM   1886 C CE1 . PHE B 1 60  ? 8.531   8.774   49.279  1.00 42.87  ? 60  PHE B CE1 1 
ATOM   1887 C CE2 . PHE B 1 60  ? 9.046   10.927  50.162  1.00 52.82  ? 60  PHE B CE2 1 
ATOM   1888 C CZ  . PHE B 1 60  ? 8.451   9.689   50.296  1.00 46.68  ? 60  PHE B CZ  1 
ATOM   1889 N N   . ILE B 1 61  ? 7.267   11.294  46.044  1.00 34.19  ? 61  ILE B N   1 
ATOM   1890 C CA  . ILE B 1 61  ? 6.113   12.161  46.280  1.00 35.23  ? 61  ILE B CA  1 
ATOM   1891 C C   . ILE B 1 61  ? 5.827   12.175  47.774  1.00 42.54  ? 61  ILE B C   1 
ATOM   1892 O O   . ILE B 1 61  ? 5.437   11.161  48.360  1.00 32.65  ? 61  ILE B O   1 
ATOM   1893 C CB  . ILE B 1 61  ? 4.874   11.723  45.491  1.00 40.14  ? 61  ILE B CB  1 
ATOM   1894 C CG1 . ILE B 1 61  ? 5.175   11.658  43.977  1.00 39.44  ? 61  ILE B CG1 1 
ATOM   1895 C CG2 . ILE B 1 61  ? 3.709   12.695  45.804  1.00 38.81  ? 61  ILE B CG2 1 
ATOM   1896 C CD1 . ILE B 1 61  ? 5.676   12.976  43.345  1.00 34.46  ? 61  ILE B CD1 1 
ATOM   1897 N N   . GLU B 1 62  ? 5.995   13.328  48.388  1.00 41.17  ? 62  GLU B N   1 
ATOM   1898 C CA  . GLU B 1 62  ? 5.696   13.460  49.802  1.00 48.57  ? 62  GLU B CA  1 
ATOM   1899 C C   . GLU B 1 62  ? 4.198   13.658  49.975  1.00 45.74  ? 62  GLU B C   1 
ATOM   1900 O O   . GLU B 1 62  ? 3.517   14.195  49.096  1.00 51.95  ? 62  GLU B O   1 
ATOM   1901 C CB  . GLU B 1 62  ? 6.472   14.633  50.389  1.00 45.35  ? 62  GLU B CB  1 
ATOM   1902 C CG  . GLU B 1 62  ? 7.633   14.200  51.258  1.00 68.79  ? 62  GLU B CG  1 
ATOM   1903 C CD  . GLU B 1 62  ? 8.419   15.377  51.807  1.00 86.32  ? 62  GLU B CD  1 
ATOM   1904 O OE1 . GLU B 1 62  ? 7.994   15.952  52.835  1.00 93.07  ? 62  GLU B OE1 1 
ATOM   1905 O OE2 . GLU B 1 62  ? 9.457   15.730  51.207  1.00 88.31  ? 62  GLU B OE2 1 
ATOM   1906 N N   . GLY B 1 63  ? 3.668   13.125  51.070  1.00 46.16  ? 63  GLY B N   1 
ATOM   1907 C CA  . GLY B 1 63  ? 2.237   13.190  51.324  1.00 50.02  ? 63  GLY B CA  1 
ATOM   1908 C C   . GLY B 1 63  ? 1.670   11.883  51.840  1.00 45.75  ? 63  GLY B C   1 
ATOM   1909 O O   . GLY B 1 63  ? 2.417   10.923  52.060  1.00 46.08  ? 63  GLY B O   1 
ATOM   1910 N N   . ARG B 1 64  ? 0.347   11.821  52.023  1.00 45.87  ? 64  ARG B N   1 
ATOM   1911 C CA  . ARG B 1 64  ? -0.260  10.597  52.530  1.00 46.28  ? 64  ARG B CA  1 
ATOM   1912 C C   . ARG B 1 64  ? -1.072  9.910   51.436  1.00 45.93  ? 64  ARG B C   1 
ATOM   1913 O O   . ARG B 1 64  ? -1.692  10.587  50.603  1.00 45.38  ? 64  ARG B O   1 
ATOM   1914 C CB  . ARG B 1 64  ? -1.164  10.885  53.742  1.00 48.30  ? 64  ARG B CB  1 
ATOM   1915 C CG  . ARG B 1 64  ? -0.518  11.827  54.756  1.00 52.21  ? 64  ARG B CG  1 
ATOM   1916 C CD  . ARG B 1 64  ? -1.366  12.108  55.999  1.00 53.18  ? 64  ARG B CD  1 
ATOM   1917 N NE  . ARG B 1 64  ? -1.623  10.920  56.813  1.00 64.08  ? 64  ARG B NE  1 
ATOM   1918 C CZ  . ARG B 1 64  ? -2.541  10.844  57.774  1.00 64.53  ? 64  ARG B CZ  1 
ATOM   1919 N NH1 . ARG B 1 64  ? -3.324  11.869  58.072  1.00 52.03  ? 64  ARG B NH1 1 
ATOM   1920 N NH2 . ARG B 1 64  ? -2.667  9.711   58.465  1.00 54.60  ? 64  ARG B NH2 1 
ATOM   1921 N N   . PRO B 1 65  ? -1.067  8.579   51.385  1.00 50.36  ? 65  PRO B N   1 
ATOM   1922 C CA  . PRO B 1 65  ? -1.910  7.888   50.401  1.00 48.03  ? 65  PRO B CA  1 
ATOM   1923 C C   . PRO B 1 65  ? -3.376  8.117   50.727  1.00 51.95  ? 65  PRO B C   1 
ATOM   1924 O O   . PRO B 1 65  ? -3.747  8.343   51.883  1.00 49.78  ? 65  PRO B O   1 
ATOM   1925 C CB  . PRO B 1 65  ? -1.521  6.412   50.551  1.00 42.59  ? 65  PRO B CB  1 
ATOM   1926 C CG  . PRO B 1 65  ? -0.927  6.315   51.952  1.00 45.30  ? 65  PRO B CG  1 
ATOM   1927 C CD  . PRO B 1 65  ? -0.315  7.649   52.249  1.00 47.10  ? 65  PRO B CD  1 
ATOM   1928 N N   . ILE B 1 66  ? -4.208  8.090   49.682  1.00 40.05  ? 66  ILE B N   1 
ATOM   1929 C CA  . ILE B 1 66  ? -5.616  8.437   49.841  1.00 44.17  ? 66  ILE B CA  1 
ATOM   1930 C C   . ILE B 1 66  ? -6.303  7.546   50.872  1.00 51.38  ? 66  ILE B C   1 
ATOM   1931 O O   . ILE B 1 66  ? -7.199  8.008   51.585  1.00 46.40  ? 66  ILE B O   1 
ATOM   1932 C CB  . ILE B 1 66  ? -6.349  8.405   48.476  1.00 45.02  ? 66  ILE B CB  1 
ATOM   1933 C CG1 . ILE B 1 66  ? -7.740  9.049   48.595  1.00 43.72  ? 66  ILE B CG1 1 
ATOM   1934 C CG2 . ILE B 1 66  ? -6.426  6.981   47.899  1.00 40.07  ? 66  ILE B CG2 1 
ATOM   1935 C CD1 . ILE B 1 66  ? -8.398  9.330   47.235  1.00 41.76  ? 66  ILE B CD1 1 
ATOM   1936 N N   . LYS B 1 67  ? -5.896  6.274   50.991  1.00 46.71  ? 67  LYS B N   1 
ATOM   1937 C CA  . LYS B 1 67  ? -6.564  5.391   51.944  1.00 51.05  ? 67  LYS B CA  1 
ATOM   1938 C C   . LYS B 1 67  ? -6.433  5.884   53.381  1.00 53.42  ? 67  LYS B C   1 
ATOM   1939 O O   . LYS B 1 67  ? -7.314  5.602   54.200  1.00 52.27  ? 67  LYS B O   1 
ATOM   1940 C CB  . LYS B 1 67  ? -6.000  3.974   51.835  1.00 51.18  ? 67  LYS B CB  1 
ATOM   1941 C CG  . LYS B 1 67  ? -4.526  3.895   52.185  1.00 55.09  ? 67  LYS B CG  1 
ATOM   1942 C CD  . LYS B 1 67  ? -4.131  2.491   52.573  1.00 62.96  ? 67  LYS B CD  1 
ATOM   1943 C CE  . LYS B 1 67  ? -2.624  2.334   52.556  1.00 60.14  ? 67  LYS B CE  1 
ATOM   1944 N NZ  . LYS B 1 67  ? -2.082  2.837   53.858  1.00 68.12  ? 67  LYS B NZ  1 
ATOM   1945 N N   . ASP B 1 68  ? -5.392  6.665   53.692  1.00 48.22  ? 68  ASP B N   1 
ATOM   1946 C CA  . ASP B 1 68  ? -5.205  7.185   55.041  1.00 58.27  ? 68  ASP B CA  1 
ATOM   1947 C C   . ASP B 1 68  ? -6.028  8.431   55.327  1.00 55.20  ? 68  ASP B C   1 
ATOM   1948 O O   . ASP B 1 68  ? -6.112  8.836   56.488  1.00 54.76  ? 68  ASP B O   1 
ATOM   1949 C CB  . ASP B 1 68  ? -3.730  7.526   55.299  1.00 60.28  ? 68  ASP B CB  1 
ATOM   1950 C CG  . ASP B 1 68  ? -2.833  6.299   55.384  1.00 63.64  ? 68  ASP B CG  1 
ATOM   1951 O OD1 . ASP B 1 68  ? -3.347  5.154   55.388  1.00 60.19  ? 68  ASP B OD1 1 
ATOM   1952 O OD2 . ASP B 1 68  ? -1.596  6.495   55.435  1.00 63.24  ? 68  ASP B OD2 1 
ATOM   1953 N N   . VAL B 1 69  ? -6.621  9.073   54.320  1.00 50.16  ? 69  VAL B N   1 
ATOM   1954 C CA  . VAL B 1 69  ? -7.261  10.365  54.577  1.00 53.68  ? 69  VAL B CA  1 
ATOM   1955 C C   . VAL B 1 69  ? -8.622  10.487  53.899  1.00 58.64  ? 69  VAL B C   1 
ATOM   1956 O O   . VAL B 1 69  ? -9.264  11.539  53.991  1.00 54.33  ? 69  VAL B O   1 
ATOM   1957 C CB  . VAL B 1 69  ? -6.355  11.527  54.122  1.00 56.06  ? 69  VAL B CB  1 
ATOM   1958 C CG1 . VAL B 1 69  ? -5.125  11.652  55.004  1.00 55.33  ? 69  VAL B CG1 1 
ATOM   1959 C CG2 . VAL B 1 69  ? -5.967  11.357  52.627  1.00 53.20  ? 69  VAL B CG2 1 
ATOM   1960 N N   . ILE B 1 70  ? -9.080  9.417   53.233  1.00 56.36  ? 70  ILE B N   1 
ATOM   1961 C CA  . ILE B 1 70  ? -10.233 9.528   52.338  1.00 54.11  ? 70  ILE B CA  1 
ATOM   1962 C C   . ILE B 1 70  ? -11.466 10.033  53.088  1.00 58.92  ? 70  ILE B C   1 
ATOM   1963 O O   . ILE B 1 70  ? -12.254 10.821  52.555  1.00 57.26  ? 70  ILE B O   1 
ATOM   1964 C CB  . ILE B 1 70  ? -10.495 8.182   51.624  1.00 48.89  ? 70  ILE B CB  1 
ATOM   1965 C CG1 . ILE B 1 70  ? -11.659 8.302   50.636  1.00 49.74  ? 70  ILE B CG1 1 
ATOM   1966 C CG2 . ILE B 1 70  ? -10.727 7.041   52.609  1.00 49.34  ? 70  ILE B CG2 1 
ATOM   1967 C CD1 . ILE B 1 70  ? -11.529 9.483   49.686  1.00 51.71  ? 70  ILE B CD1 1 
ATOM   1968 N N   . ASN B 1 71  ? -11.640 9.621   54.342  1.00 57.00  ? 71  ASN B N   1 
ATOM   1969 C CA  . ASN B 1 71  ? -12.804 10.061  55.102  1.00 61.87  ? 71  ASN B CA  1 
ATOM   1970 C C   . ASN B 1 71  ? -12.655 11.467  55.681  1.00 63.46  ? 71  ASN B C   1 
ATOM   1971 O O   . ASN B 1 71  ? -13.637 12.011  56.187  1.00 67.38  ? 71  ASN B O   1 
ATOM   1972 C CB  . ASN B 1 71  ? -13.082 9.047   56.203  1.00 63.80  ? 71  ASN B CB  1 
ATOM   1973 C CG  . ASN B 1 71  ? -13.609 7.752   55.648  1.00 56.87  ? 71  ASN B CG  1 
ATOM   1974 O OD1 . ASN B 1 71  ? -12.904 6.745   55.612  1.00 62.20  ? 71  ASN B OD1 1 
ATOM   1975 N ND2 . ASN B 1 71  ? -14.873 7.759   55.243  1.00 62.49  ? 71  ASN B ND2 1 
ATOM   1976 N N   . GLU B 1 72  ? -11.457 12.057  55.644  1.00 66.19  ? 72  GLU B N   1 
ATOM   1977 C CA  . GLU B 1 72  ? -11.255 13.421  56.106  1.00 63.27  ? 72  GLU B CA  1 
ATOM   1978 C C   . GLU B 1 72  ? -11.279 14.430  54.966  1.00 65.67  ? 72  GLU B C   1 
ATOM   1979 O O   . GLU B 1 72  ? -11.305 15.634  55.236  1.00 68.76  ? 72  GLU B O   1 
ATOM   1980 C CB  . GLU B 1 72  ? -9.897  13.535  56.836  1.00 65.40  ? 72  GLU B CB  1 
ATOM   1981 C CG  . GLU B 1 72  ? -9.417  12.301  57.681  1.00 69.28  ? 72  GLU B CG  1 
ATOM   1982 C CD  . GLU B 1 72  ? -10.480 11.620  58.533  1.00 77.67  ? 72  GLU B CD  1 
ATOM   1983 O OE1 . GLU B 1 72  ? -11.490 12.268  58.910  1.00 81.91  ? 72  GLU B OE1 1 
ATOM   1984 O OE2 . GLU B 1 72  ? -10.293 10.423  58.871  1.00 75.34  ? 72  GLU B OE2 1 
ATOM   1985 N N   . LEU B 1 73  ? -11.273 13.967  53.720  1.00 65.75  ? 73  LEU B N   1 
ATOM   1986 C CA  . LEU B 1 73  ? -11.083 14.839  52.569  1.00 56.18  ? 73  LEU B CA  1 
ATOM   1987 C C   . LEU B 1 73  ? -12.332 15.674  52.331  1.00 57.91  ? 73  LEU B C   1 
ATOM   1988 O O   . LEU B 1 73  ? -13.455 15.171  52.415  1.00 57.82  ? 73  LEU B O   1 
ATOM   1989 C CB  . LEU B 1 73  ? -10.783 13.997  51.326  1.00 53.95  ? 73  LEU B CB  1 
ATOM   1990 C CG  . LEU B 1 73  ? -9.383  13.400  51.159  1.00 55.29  ? 73  LEU B CG  1 
ATOM   1991 C CD1 . LEU B 1 73  ? -9.169  12.984  49.696  1.00 48.36  ? 73  LEU B CD1 1 
ATOM   1992 C CD2 . LEU B 1 73  ? -8.290  14.343  51.617  1.00 50.00  ? 73  LEU B CD2 1 
ATOM   1993 N N   . ASN B 1 74  ? -12.142 16.964  52.062  1.00 60.09  ? 74  ASN B N   1 
ATOM   1994 C CA  . ASN B 1 74  ? -13.284 17.832  51.833  1.00 65.46  ? 74  ASN B CA  1 
ATOM   1995 C C   . ASN B 1 74  ? -13.762 17.735  50.382  1.00 67.63  ? 74  ASN B C   1 
ATOM   1996 O O   . ASN B 1 74  ? -13.168 17.053  49.537  1.00 64.62  ? 74  ASN B O   1 
ATOM   1997 C CB  . ASN B 1 74  ? -12.966 19.273  52.259  1.00 68.14  ? 74  ASN B CB  1 
ATOM   1998 C CG  . ASN B 1 74  ? -11.925 19.957  51.375  1.00 78.85  ? 74  ASN B CG  1 
ATOM   1999 O OD1 . ASN B 1 74  ? -11.841 19.730  50.167  1.00 70.62  ? 74  ASN B OD1 1 
ATOM   2000 N ND2 . ASN B 1 74  ? -11.151 20.847  51.984  1.00 78.55  ? 74  ASN B ND2 1 
ATOM   2001 N N   . SER B 1 75  ? -14.858 18.443  50.099  1.00 67.00  ? 75  SER B N   1 
ATOM   2002 C CA  . SER B 1 75  ? -15.488 18.377  48.786  1.00 67.88  ? 75  SER B CA  1 
ATOM   2003 C C   . SER B 1 75  ? -14.636 19.021  47.708  1.00 69.61  ? 75  SER B C   1 
ATOM   2004 O O   . SER B 1 75  ? -14.618 18.548  46.563  1.00 65.01  ? 75  SER B O   1 
ATOM   2005 C CB  . SER B 1 75  ? -16.858 19.053  48.834  1.00 76.66  ? 75  SER B CB  1 
ATOM   2006 O OG  . SER B 1 75  ? -16.786 20.361  48.299  1.00 89.49  ? 75  SER B OG  1 
ATOM   2007 N N   . GLU B 1 76  ? -13.935 20.098  48.047  1.00 65.81  ? 76  GLU B N   1 
ATOM   2008 C CA  . GLU B 1 76  ? -13.025 20.713  47.094  1.00 69.74  ? 76  GLU B CA  1 
ATOM   2009 C C   . GLU B 1 76  ? -11.939 19.734  46.657  1.00 68.40  ? 76  GLU B C   1 
ATOM   2010 O O   . GLU B 1 76  ? -11.608 19.651  45.466  1.00 66.27  ? 76  GLU B O   1 
ATOM   2011 C CB  . GLU B 1 76  ? -12.441 21.985  47.706  1.00 72.16  ? 76  GLU B CB  1 
ATOM   2012 C CG  . GLU B 1 76  ? -11.341 22.625  46.898  1.00 80.53  ? 76  GLU B CG  1 
ATOM   2013 C CD  . GLU B 1 76  ? -10.010 22.535  47.611  1.00 83.58  ? 76  GLU B CD  1 
ATOM   2014 O OE1 . GLU B 1 76  ? -9.953  22.947  48.797  1.00 82.22  ? 76  GLU B OE1 1 
ATOM   2015 O OE2 . GLU B 1 76  ? -9.037  22.036  47.002  1.00 76.11  ? 76  GLU B OE2 1 
ATOM   2016 N N   . THR B 1 77  ? -11.397 18.956  47.600  1.00 65.27  ? 77  THR B N   1 
ATOM   2017 C CA  . THR B 1 77  ? -10.303 18.045  47.265  1.00 65.36  ? 77  THR B CA  1 
ATOM   2018 C C   . THR B 1 77  ? -10.794 16.870  46.431  1.00 59.11  ? 77  THR B C   1 
ATOM   2019 O O   . THR B 1 77  ? -10.132 16.473  45.461  1.00 56.53  ? 77  THR B O   1 
ATOM   2020 C CB  . THR B 1 77  ? -9.619  17.554  48.540  1.00 62.04  ? 77  THR B CB  1 
ATOM   2021 O OG1 . THR B 1 77  ? -9.034  18.671  49.223  1.00 68.26  ? 77  THR B OG1 1 
ATOM   2022 C CG2 . THR B 1 77  ? -8.533  16.539  48.219  1.00 50.59  ? 77  THR B CG2 1 
ATOM   2023 N N   . ILE B 1 78  ? -11.952 16.305  46.787  1.00 55.64  ? 78  ILE B N   1 
ATOM   2024 C CA  . ILE B 1 78  ? -12.539 15.240  45.976  1.00 55.20  ? 78  ILE B CA  1 
ATOM   2025 C C   . ILE B 1 78  ? -12.769 15.731  44.553  1.00 56.69  ? 78  ILE B C   1 
ATOM   2026 O O   . ILE B 1 78  ? -12.478 15.024  43.581  1.00 53.52  ? 78  ILE B O   1 
ATOM   2027 C CB  . ILE B 1 78  ? -13.841 14.730  46.626  1.00 59.30  ? 78  ILE B CB  1 
ATOM   2028 C CG1 . ILE B 1 78  ? -13.540 14.099  47.988  1.00 57.57  ? 78  ILE B CG1 1 
ATOM   2029 C CG2 . ILE B 1 78  ? -14.535 13.717  45.721  1.00 56.84  ? 78  ILE B CG2 1 
ATOM   2030 C CD1 . ILE B 1 78  ? -12.610 12.892  47.892  1.00 57.78  ? 78  ILE B CD1 1 
ATOM   2031 N N   . GLY B 1 79  ? -13.257 16.967  44.409  1.00 56.60  ? 79  GLY B N   1 
ATOM   2032 C CA  . GLY B 1 79  ? -13.440 17.536  43.083  1.00 58.03  ? 79  GLY B CA  1 
ATOM   2033 C C   . GLY B 1 79  ? -12.143 17.635  42.300  1.00 55.55  ? 79  GLY B C   1 
ATOM   2034 O O   . GLY B 1 79  ? -12.131 17.466  41.076  1.00 55.67  ? 79  GLY B O   1 
ATOM   2035 N N   . ARG B 1 80  ? -11.034 17.931  42.988  1.00 54.61  ? 80  ARG B N   1 
ATOM   2036 C CA  . ARG B 1 80  ? -9.745  17.983  42.309  1.00 53.01  ? 80  ARG B CA  1 
ATOM   2037 C C   . ARG B 1 80  ? -9.325  16.601  41.816  1.00 51.61  ? 80  ARG B C   1 
ATOM   2038 O O   . ARG B 1 80  ? -8.751  16.475  40.729  1.00 45.59  ? 80  ARG B O   1 
ATOM   2039 C CB  . ARG B 1 80  ? -8.683  18.584  43.234  1.00 55.88  ? 80  ARG B CB  1 
ATOM   2040 C CG  . ARG B 1 80  ? -8.559  20.103  43.117  1.00 66.21  ? 80  ARG B CG  1 
ATOM   2041 C CD  . ARG B 1 80  ? -7.530  20.740  44.071  1.00 67.06  ? 80  ARG B CD  1 
ATOM   2042 N NE  . ARG B 1 80  ? -7.427  20.111  45.385  1.00 73.67  ? 80  ARG B NE  1 
ATOM   2043 C CZ  . ARG B 1 80  ? -6.323  20.079  46.125  1.00 72.92  ? 80  ARG B CZ  1 
ATOM   2044 N NH1 . ARG B 1 80  ? -5.174  20.559  45.676  1.00 69.63  ? 80  ARG B NH1 1 
ATOM   2045 N NH2 . ARG B 1 80  ? -6.377  19.573  47.354  1.00 77.28  ? 80  ARG B NH2 1 
ATOM   2046 N N   . ILE B 1 81  ? -9.612  15.557  42.597  1.00 46.81  ? 81  ILE B N   1 
ATOM   2047 C CA  . ILE B 1 81  ? -9.280  14.196  42.181  1.00 49.20  ? 81  ILE B CA  1 
ATOM   2048 C C   . ILE B 1 81  ? -10.176 13.766  41.030  1.00 49.82  ? 81  ILE B C   1 
ATOM   2049 O O   . ILE B 1 81  ? -9.721  13.122  40.076  1.00 43.79  ? 81  ILE B O   1 
ATOM   2050 C CB  . ILE B 1 81  ? -9.397  13.226  43.369  1.00 48.07  ? 81  ILE B CB  1 
ATOM   2051 C CG1 . ILE B 1 81  ? -8.486  13.665  44.518  1.00 46.75  ? 81  ILE B CG1 1 
ATOM   2052 C CG2 . ILE B 1 81  ? -9.020  11.806  42.940  1.00 40.16  ? 81  ILE B CG2 1 
ATOM   2053 C CD1 . ILE B 1 81  ? -8.721  12.861  45.803  1.00 43.80  ? 81  ILE B CD1 1 
ATOM   2054 N N   . LEU B 1 82  ? -11.468 14.097  41.109  1.00 43.09  ? 82  LEU B N   1 
ATOM   2055 C CA  . LEU B 1 82  ? -12.371 13.819  39.997  1.00 47.11  ? 82  LEU B CA  1 
ATOM   2056 C C   . LEU B 1 82  ? -11.879 14.476  38.715  1.00 52.17  ? 82  LEU B C   1 
ATOM   2057 O O   . LEU B 1 82  ? -11.959 13.882  37.633  1.00 45.75  ? 82  LEU B O   1 
ATOM   2058 C CB  . LEU B 1 82  ? -13.775 14.312  40.325  1.00 49.38  ? 82  LEU B CB  1 
ATOM   2059 C CG  . LEU B 1 82  ? -14.463 13.628  41.514  1.00 53.48  ? 82  LEU B CG  1 
ATOM   2060 C CD1 . LEU B 1 82  ? -15.835 14.258  41.789  1.00 51.70  ? 82  LEU B CD1 1 
ATOM   2061 C CD2 . LEU B 1 82  ? -14.582 12.138  41.294  1.00 43.19  ? 82  LEU B CD2 1 
ATOM   2062 N N   . ASP B 1 83  ? -11.366 15.706  38.820  1.00 49.37  ? 83  ASP B N   1 
ATOM   2063 C CA  . ASP B 1 83  ? -10.840 16.404  37.650  1.00 46.56  ? 83  ASP B CA  1 
ATOM   2064 C C   . ASP B 1 83  ? -9.672  15.650  37.027  1.00 43.68  ? 83  ASP B C   1 
ATOM   2065 O O   . ASP B 1 83  ? -9.554  15.576  35.799  1.00 42.54  ? 83  ASP B O   1 
ATOM   2066 C CB  . ASP B 1 83  ? -10.394 17.812  38.040  1.00 40.42  ? 83  ASP B CB  1 
ATOM   2067 C CG  . ASP B 1 83  ? -11.564 18.775  38.257  1.00 55.53  ? 83  ASP B CG  1 
ATOM   2068 O OD1 . ASP B 1 83  ? -12.740 18.403  38.031  1.00 46.66  ? 83  ASP B OD1 1 
ATOM   2069 O OD2 . ASP B 1 83  ? -11.284 19.907  38.699  1.00 49.02  ? 83  ASP B OD2 1 
ATOM   2070 N N   . ILE B 1 84  ? -8.778  15.103  37.859  1.00 43.35  ? 84  ILE B N   1 
ATOM   2071 C CA  . ILE B 1 84  ? -7.618  14.402  37.309  1.00 38.82  ? 84  ILE B CA  1 
ATOM   2072 C C   . ILE B 1 84  ? -8.058  13.132  36.594  1.00 38.98  ? 84  ILE B C   1 
ATOM   2073 O O   . ILE B 1 84  ? -7.547  12.811  35.519  1.00 37.46  ? 84  ILE B O   1 
ATOM   2074 C CB  . ILE B 1 84  ? -6.590  14.104  38.414  1.00 36.72  ? 84  ILE B CB  1 
ATOM   2075 C CG1 . ILE B 1 84  ? -5.937  15.401  38.900  1.00 40.15  ? 84  ILE B CG1 1 
ATOM   2076 C CG2 . ILE B 1 84  ? -5.498  13.155  37.886  1.00 34.83  ? 84  ILE B CG2 1 
ATOM   2077 C CD1 . ILE B 1 84  ? -5.332  15.283  40.305  1.00 40.75  ? 84  ILE B CD1 1 
ATOM   2078 N N   . CYS B 1 85  ? -9.026  12.400  37.163  1.00 36.45  ? 85  CYS B N   1 
ATOM   2079 C CA  . CYS B 1 85  ? -9.562  11.229  36.472  1.00 35.93  ? 85  CYS B CA  1 
ATOM   2080 C C   . CYS B 1 85  ? -10.143 11.621  35.118  1.00 40.37  ? 85  CYS B C   1 
ATOM   2081 O O   . CYS B 1 85  ? -9.912  10.950  34.107  1.00 35.65  ? 85  CYS B O   1 
ATOM   2082 C CB  . CYS B 1 85  ? -10.642 10.574  37.317  1.00 39.37  ? 85  CYS B CB  1 
ATOM   2083 S SG  . CYS B 1 85  ? -10.008 9.884   38.880  1.00 44.02  ? 85  CYS B SG  1 
ATOM   2084 N N   . ARG B 1 86  ? -10.923 12.706  35.090  1.00 40.83  ? 86  ARG B N   1 
ATOM   2085 C CA  . ARG B 1 86  ? -11.510 13.180  33.841  1.00 41.04  ? 86  ARG B CA  1 
ATOM   2086 C C   . ARG B 1 86  ? -10.434 13.551  32.841  1.00 38.41  ? 86  ARG B C   1 
ATOM   2087 O O   . ARG B 1 86  ? -10.554 13.249  31.648  1.00 39.60  ? 86  ARG B O   1 
ATOM   2088 C CB  . ARG B 1 86  ? -12.406 14.386  34.114  1.00 45.48  ? 86  ARG B CB  1 
ATOM   2089 C CG  . ARG B 1 86  ? -12.896 15.113  32.859  1.00 44.99  ? 86  ARG B CG  1 
ATOM   2090 C CD  . ARG B 1 86  ? -13.723 14.216  31.954  1.00 48.56  ? 86  ARG B CD  1 
ATOM   2091 N NE  . ARG B 1 86  ? -14.225 14.931  30.786  1.00 50.75  ? 86  ARG B NE  1 
ATOM   2092 C CZ  . ARG B 1 86  ? -14.713 14.345  29.700  1.00 55.43  ? 86  ARG B CZ  1 
ATOM   2093 N NH1 . ARG B 1 86  ? -14.819 13.027  29.611  1.00 47.33  ? 86  ARG B NH1 1 
ATOM   2094 N NH2 . ARG B 1 86  ? -15.128 15.099  28.683  1.00 53.90  ? 86  ARG B NH2 1 
ATOM   2095 N N   . LYS B 1 87  ? -9.388  14.237  33.308  1.00 37.66  ? 87  LYS B N   1 
ATOM   2096 C CA  . LYS B 1 87  ? -8.285  14.593  32.429  1.00 41.51  ? 87  LYS B CA  1 
ATOM   2097 C C   . LYS B 1 87  ? -7.700  13.344  31.781  1.00 39.03  ? 87  LYS B C   1 
ATOM   2098 O O   . LYS B 1 87  ? -7.478  13.299  30.569  1.00 33.97  ? 87  LYS B O   1 
ATOM   2099 C CB  . LYS B 1 87  ? -7.220  15.329  33.237  1.00 36.82  ? 87  LYS B CB  1 
ATOM   2100 C CG  . LYS B 1 87  ? -6.136  15.994  32.427  1.00 45.38  ? 87  LYS B CG  1 
ATOM   2101 C CD  . LYS B 1 87  ? -6.710  16.672  31.179  1.00 50.36  ? 87  LYS B CD  1 
ATOM   2102 C CE  . LYS B 1 87  ? -5.703  17.666  30.617  1.00 50.56  ? 87  LYS B CE  1 
ATOM   2103 N NZ  . LYS B 1 87  ? -6.088  19.083  30.859  1.00 64.71  ? 87  LYS B NZ  1 
ATOM   2104 N N   . LEU B 1 88  ? -7.462  12.298  32.581  1.00 37.23  ? 88  LEU B N   1 
ATOM   2105 C CA  . LEU B 1 88  ? -6.927  11.060  32.025  1.00 30.91  ? 88  LEU B CA  1 
ATOM   2106 C C   . LEU B 1 88  ? -7.906  10.452  31.034  1.00 33.96  ? 88  LEU B C   1 
ATOM   2107 O O   . LEU B 1 88  ? -7.505  9.959   29.969  1.00 34.68  ? 88  LEU B O   1 
ATOM   2108 C CB  . LEU B 1 88  ? -6.627  10.086  33.177  1.00 34.67  ? 88  LEU B CB  1 
ATOM   2109 C CG  . LEU B 1 88  ? -5.391  10.443  34.003  1.00 35.48  ? 88  LEU B CG  1 
ATOM   2110 C CD1 . LEU B 1 88  ? -5.271  9.502   35.222  1.00 32.55  ? 88  LEU B CD1 1 
ATOM   2111 C CD2 . LEU B 1 88  ? -4.111  10.336  33.164  1.00 32.51  ? 88  LEU B CD2 1 
ATOM   2112 N N   . ASP B 1 89  ? -9.201  10.492  31.366  1.00 33.48  ? 89  ASP B N   1 
ATOM   2113 C CA  . ASP B 1 89  ? -10.241 10.044  30.449  1.00 39.67  ? 89  ASP B CA  1 
ATOM   2114 C C   . ASP B 1 89  ? -10.123 10.776  29.113  1.00 45.17  ? 89  ASP B C   1 
ATOM   2115 O O   . ASP B 1 89  ? -10.166 10.160  28.039  1.00 35.53  ? 89  ASP B O   1 
ATOM   2116 C CB  . ASP B 1 89  ? -11.630 10.318  31.051  1.00 39.64  ? 89  ASP B CB  1 
ATOM   2117 C CG  . ASP B 1 89  ? -12.078 9.256   32.067  1.00 44.96  ? 89  ASP B CG  1 
ATOM   2118 O OD1 . ASP B 1 89  ? -11.277 8.351   32.378  1.00 38.26  ? 89  ASP B OD1 1 
ATOM   2119 O OD2 . ASP B 1 89  ? -13.241 9.347   32.556  1.00 43.15  ? 89  ASP B OD2 1 
ATOM   2120 N N   . VAL B 1 90  ? -9.946  12.101  29.174  1.00 37.92  ? 90  VAL B N   1 
ATOM   2121 C CA  . VAL B 1 90  ? -9.952  12.910  27.955  1.00 39.91  ? 90  VAL B CA  1 
ATOM   2122 C C   . VAL B 1 90  ? -8.723  12.600  27.116  1.00 41.92  ? 90  VAL B C   1 
ATOM   2123 O O   . VAL B 1 90  ? -8.798  12.498  25.887  1.00 44.74  ? 90  VAL B O   1 
ATOM   2124 C CB  . VAL B 1 90  ? -10.032 14.408  28.312  1.00 43.24  ? 90  VAL B CB  1 
ATOM   2125 C CG1 . VAL B 1 90  ? -9.567  15.273  27.151  1.00 46.67  ? 90  VAL B CG1 1 
ATOM   2126 C CG2 . VAL B 1 90  ? -11.457 14.785  28.699  1.00 41.82  ? 90  VAL B CG2 1 
ATOM   2127 N N   . LEU B 1 91  ? -7.588  12.399  27.777  1.00 38.55  ? 91  LEU B N   1 
ATOM   2128 C CA  . LEU B 1 91  ? -6.322  12.067  27.142  1.00 35.00  ? 91  LEU B CA  1 
ATOM   2129 C C   . LEU B 1 91  ? -6.313  10.681  26.508  1.00 34.55  ? 91  LEU B C   1 
ATOM   2130 O O   . LEU B 1 91  ? -5.374  10.361  25.761  1.00 37.33  ? 91  LEU B O   1 
ATOM   2131 C CB  . LEU B 1 91  ? -5.220  12.182  28.193  1.00 33.39  ? 91  LEU B CB  1 
ATOM   2132 C CG  . LEU B 1 91  ? -4.900  13.612  28.657  1.00 40.79  ? 91  LEU B CG  1 
ATOM   2133 C CD1 . LEU B 1 91  ? -3.932  13.585  29.838  1.00 33.01  ? 91  LEU B CD1 1 
ATOM   2134 C CD2 . LEU B 1 91  ? -4.351  14.452  27.516  1.00 37.51  ? 91  LEU B CD2 1 
ATOM   2135 N N   . GLY B 1 92  ? -7.307  9.846   26.791  1.00 31.00  ? 92  GLY B N   1 
ATOM   2136 C CA  . GLY B 1 92  ? -7.301  8.500   26.254  1.00 31.83  ? 92  GLY B CA  1 
ATOM   2137 C C   . GLY B 1 92  ? -6.424  7.512   26.995  1.00 34.28  ? 92  GLY B C   1 
ATOM   2138 O O   . GLY B 1 92  ? -6.080  6.474   26.425  1.00 31.98  ? 92  GLY B O   1 
ATOM   2139 N N   . ILE B 1 93  ? -6.065  7.788   28.252  1.00 31.09  ? 93  ILE B N   1 
ATOM   2140 C CA  . ILE B 1 93  ? -5.204  6.901   29.043  1.00 32.39  ? 93  ILE B CA  1 
ATOM   2141 C C   . ILE B 1 93  ? -6.035  6.281   30.160  1.00 34.28  ? 93  ILE B C   1 
ATOM   2142 O O   . ILE B 1 93  ? -6.487  6.982   31.074  1.00 34.44  ? 93  ILE B O   1 
ATOM   2143 C CB  . ILE B 1 93  ? -3.980  7.633   29.618  1.00 33.22  ? 93  ILE B CB  1 
ATOM   2144 C CG1 . ILE B 1 93  ? -3.120  8.229   28.497  1.00 30.37  ? 93  ILE B CG1 1 
ATOM   2145 C CG2 . ILE B 1 93  ? -3.158  6.701   30.594  1.00 25.32  ? 93  ILE B CG2 1 
ATOM   2146 C CD1 . ILE B 1 93  ? -2.137  9.265   29.006  1.00 28.40  ? 93  ILE B CD1 1 
ATOM   2147 N N   . GLN B 1 94  ? -6.226  4.962   30.087  1.00 29.02  ? 94  GLN B N   1 
ATOM   2148 C CA  . GLN B 1 94  ? -6.861  4.184   31.147  1.00 31.69  ? 94  GLN B CA  1 
ATOM   2149 C C   . GLN B 1 94  ? -5.765  3.695   32.093  1.00 33.41  ? 94  GLN B C   1 
ATOM   2150 O O   . GLN B 1 94  ? -4.952  2.841   31.728  1.00 31.91  ? 94  GLN B O   1 
ATOM   2151 C CB  . GLN B 1 94  ? -7.662  3.020   30.556  1.00 36.84  ? 94  GLN B CB  1 
ATOM   2152 C CG  . GLN B 1 94  ? -8.322  2.100   31.591  1.00 34.50  ? 94  GLN B CG  1 
ATOM   2153 C CD  . GLN B 1 94  ? -9.566  1.423   31.067  1.00 47.42  ? 94  GLN B CD  1 
ATOM   2154 O OE1 . GLN B 1 94  ? -10.573 2.075   30.780  1.00 42.97  ? 94  GLN B OE1 1 
ATOM   2155 N NE2 . GLN B 1 94  ? -9.490  0.107   30.885  1.00 46.55  ? 94  GLN B NE2 1 
ATOM   2156 N N   . LYS B 1 95  ? -5.709  4.270   33.288  1.00 30.51  ? 95  LYS B N   1 
ATOM   2157 C CA  . LYS B 1 95  ? -4.643  3.909   34.222  1.00 28.81  ? 95  LYS B CA  1 
ATOM   2158 C C   . LYS B 1 95  ? -4.808  2.490   34.764  1.00 32.75  ? 95  LYS B C   1 
ATOM   2159 O O   . LYS B 1 95  ? -3.804  1.810   35.018  1.00 34.58  ? 95  LYS B O   1 
ATOM   2160 C CB  . LYS B 1 95  ? -4.609  4.932   35.343  1.00 30.55  ? 95  LYS B CB  1 
ATOM   2161 C CG  . LYS B 1 95  ? -3.476  4.783   36.334  1.00 30.11  ? 95  LYS B CG  1 
ATOM   2162 C CD  . LYS B 1 95  ? -3.431  6.019   37.232  1.00 33.30  ? 95  LYS B CD  1 
ATOM   2163 C CE  . LYS B 1 95  ? -2.220  5.961   38.150  1.00 33.35  ? 95  LYS B CE  1 
ATOM   2164 N NZ  . LYS B 1 95  ? -2.407  4.815   39.127  1.00 32.29  ? 95  LYS B NZ  1 
ATOM   2165 N N   . GLU B 1 96  ? -6.061  2.031   34.902  1.00 28.12  ? 96  GLU B N   1 
ATOM   2166 C CA  . GLU B 1 96  ? -6.479  0.755   35.481  1.00 41.89  ? 96  GLU B CA  1 
ATOM   2167 C C   . GLU B 1 96  ? -6.414  0.813   37.005  1.00 42.90  ? 96  GLU B C   1 
ATOM   2168 O O   . GLU B 1 96  ? -5.761  1.694   37.580  1.00 37.64  ? 96  GLU B O   1 
ATOM   2169 C CB  . GLU B 1 96  ? -5.646  -0.423  34.953  1.00 38.03  ? 96  GLU B CB  1 
ATOM   2170 C CG  . GLU B 1 96  ? -5.742  -0.661  33.434  1.00 39.84  ? 96  GLU B CG  1 
ATOM   2171 C CD  . GLU B 1 96  ? -7.122  -1.142  32.937  1.00 56.02  ? 96  GLU B CD  1 
ATOM   2172 O OE1 . GLU B 1 96  ? -8.139  -1.019  33.665  1.00 56.04  ? 96  GLU B OE1 1 
ATOM   2173 O OE2 . GLU B 1 96  ? -7.190  -1.628  31.787  1.00 50.74  ? 96  GLU B OE2 1 
ATOM   2174 N N   . GLU B 1 97  ? -7.168  -0.067  37.658  1.00 37.13  ? 97  GLU B N   1 
ATOM   2175 C CA  . GLU B 1 97  ? -7.183  -0.223  39.115  1.00 47.98  ? 97  GLU B CA  1 
ATOM   2176 C C   . GLU B 1 97  ? -7.575  1.059   39.851  1.00 47.10  ? 97  GLU B C   1 
ATOM   2177 O O   . GLU B 1 97  ? -7.228  1.236   41.023  1.00 44.74  ? 97  GLU B O   1 
ATOM   2178 C CB  . GLU B 1 97  ? -5.828  -0.733  39.617  1.00 45.18  ? 97  GLU B CB  1 
ATOM   2179 C CG  . GLU B 1 97  ? -5.530  -2.163  39.169  1.00 53.13  ? 97  GLU B CG  1 
ATOM   2180 C CD  . GLU B 1 97  ? -6.310  -3.196  39.976  1.00 74.77  ? 97  GLU B CD  1 
ATOM   2181 O OE1 . GLU B 1 97  ? -6.047  -3.333  41.194  1.00 86.22  ? 97  GLU B OE1 1 
ATOM   2182 O OE2 . GLU B 1 97  ? -7.199  -3.863  39.398  1.00 75.77  ? 97  GLU B OE2 1 
ATOM   2183 N N   . MET B 1 98  ? -8.301  1.962   39.189  1.00 38.84  ? 98  MET B N   1 
ATOM   2184 C CA  . MET B 1 98  ? -8.728  3.210   39.814  1.00 41.59  ? 98  MET B CA  1 
ATOM   2185 C C   . MET B 1 98  ? -9.855  2.992   40.814  1.00 40.65  ? 98  MET B C   1 
ATOM   2186 O O   . MET B 1 98  ? -10.213 3.924   41.549  1.00 41.47  ? 98  MET B O   1 
ATOM   2187 C CB  . MET B 1 98  ? -9.177  4.196   38.728  1.00 44.51  ? 98  MET B CB  1 
ATOM   2188 C CG  . MET B 1 98  ? -8.125  5.147   38.141  1.00 42.90  ? 98  MET B CG  1 
ATOM   2189 S SD  . MET B 1 98  ? -6.804  5.617   39.262  1.00 45.54  ? 98  MET B SD  1 
ATOM   2190 C CE  . MET B 1 98  ? -7.633  6.965   40.107  1.00 41.59  ? 98  MET B CE  1 
ATOM   2191 N N   . ASN B 1 99  ? -10.457 1.800   40.825  1.00 39.20  ? 99  ASN B N   1 
ATOM   2192 C CA  . ASN B 1 99  ? -11.400 1.441   41.872  1.00 44.47  ? 99  ASN B CA  1 
ATOM   2193 C C   . ASN B 1 99  ? -10.692 0.923   43.116  1.00 42.92  ? 99  ASN B C   1 
ATOM   2194 O O   . ASN B 1 99  ? -11.351 0.712   44.133  1.00 43.95  ? 99  ASN B O   1 
ATOM   2195 C CB  . ASN B 1 99  ? -12.403 0.403   41.353  1.00 47.43  ? 99  ASN B CB  1 
ATOM   2196 C CG  . ASN B 1 99  ? -11.729 -0.868  40.861  1.00 46.40  ? 99  ASN B CG  1 
ATOM   2197 O OD1 . ASN B 1 99  ? -10.660 -0.821  40.258  1.00 47.03  ? 99  ASN B OD1 1 
ATOM   2198 N ND2 . ASN B 1 99  ? -12.354 -2.008  41.119  1.00 50.08  ? 99  ASN B ND2 1 
ATOM   2199 N N   . HIS B 1 100 ? -9.375  0.726   43.054  1.00 42.16  ? 100 HIS B N   1 
ATOM   2200 C CA  . HIS B 1 100 ? -8.535  0.462   44.226  1.00 47.02  ? 100 HIS B CA  1 
ATOM   2201 C C   . HIS B 1 100 ? -7.349  1.422   44.240  1.00 42.04  ? 100 HIS B C   1 
ATOM   2202 O O   . HIS B 1 100 ? -6.191  0.996   44.168  1.00 38.10  ? 100 HIS B O   1 
ATOM   2203 C CB  . HIS B 1 100 ? -8.057  -0.990  44.235  1.00 50.44  ? 100 HIS B CB  1 
ATOM   2204 C CG  . HIS B 1 100 ? -9.169  -1.990  44.303  1.00 56.80  ? 100 HIS B CG  1 
ATOM   2205 N ND1 . HIS B 1 100 ? -10.119 -1.975  45.307  1.00 54.29  ? 100 HIS B ND1 1 
ATOM   2206 C CD2 . HIS B 1 100 ? -9.517  -2.999  43.471  1.00 59.08  ? 100 HIS B CD2 1 
ATOM   2207 C CE1 . HIS B 1 100 ? -10.987 -2.950  45.100  1.00 60.78  ? 100 HIS B CE1 1 
ATOM   2208 N NE2 . HIS B 1 100 ? -10.645 -3.586  43.992  1.00 60.79  ? 100 HIS B NE2 1 
ATOM   2209 N N   . PRO B 1 101 ? -7.596  2.728   44.336  1.00 42.32  ? 101 PRO B N   1 
ATOM   2210 C CA  . PRO B 1 101 ? -6.507  3.711   44.278  1.00 40.88  ? 101 PRO B CA  1 
ATOM   2211 C C   . PRO B 1 101 ? -5.816  3.934   45.612  1.00 45.54  ? 101 PRO B C   1 
ATOM   2212 O O   . PRO B 1 101 ? -5.053  4.898   45.740  1.00 41.20  ? 101 PRO B O   1 
ATOM   2213 C CB  . PRO B 1 101 ? -7.246  4.991   43.853  1.00 39.93  ? 101 PRO B CB  1 
ATOM   2214 C CG  . PRO B 1 101 ? -8.557  4.853   44.561  1.00 42.64  ? 101 PRO B CG  1 
ATOM   2215 C CD  . PRO B 1 101 ? -8.906  3.392   44.497  1.00 44.75  ? 101 PRO B CD  1 
ATOM   2216 N N   . ASP B 1 102 ? -6.069  3.039   46.571  1.00 43.69  ? 102 ASP B N   1 
ATOM   2217 C CA  . ASP B 1 102 ? -5.764  3.274   47.980  1.00 45.07  ? 102 ASP B CA  1 
ATOM   2218 C C   . ASP B 1 102 ? -4.347  3.791   48.191  1.00 40.15  ? 102 ASP B C   1 
ATOM   2219 O O   . ASP B 1 102 ? -4.120  4.718   48.976  1.00 49.52  ? 102 ASP B O   1 
ATOM   2220 C CB  . ASP B 1 102 ? -5.983  1.973   48.745  1.00 45.32  ? 102 ASP B CB  1 
ATOM   2221 C CG  . ASP B 1 102 ? -7.407  1.456   48.597  1.00 53.74  ? 102 ASP B CG  1 
ATOM   2222 O OD1 . ASP B 1 102 ? -7.788  1.111   47.448  1.00 47.72  ? 102 ASP B OD1 1 
ATOM   2223 O OD2 . ASP B 1 102 ? -8.139  1.391   49.610  1.00 54.14  ? 102 ASP B OD2 1 
ATOM   2224 N N   . ARG B 1 103 ? -3.371  3.190   47.519  1.00 41.69  ? 103 ARG B N   1 
ATOM   2225 C CA  . ARG B 1 103 ? -1.979  3.579   47.702  1.00 41.69  ? 103 ARG B CA  1 
ATOM   2226 C C   . ARG B 1 103 ? -1.424  4.369   46.525  1.00 45.52  ? 103 ARG B C   1 
ATOM   2227 O O   . ARG B 1 103 ? -0.219  4.635   46.497  1.00 35.43  ? 103 ARG B O   1 
ATOM   2228 C CB  . ARG B 1 103 ? -1.106  2.345   47.932  1.00 51.42  ? 103 ARG B CB  1 
ATOM   2229 C CG  . ARG B 1 103 ? -1.456  1.535   49.190  1.00 61.19  ? 103 ARG B CG  1 
ATOM   2230 C CD  . ARG B 1 103 ? -0.561  0.308   49.242  1.00 69.65  ? 103 ARG B CD  1 
ATOM   2231 N NE  . ARG B 1 103 ? -1.077  -0.703  48.327  1.00 78.64  ? 103 ARG B NE  1 
ATOM   2232 C CZ  . ARG B 1 103 ? -0.475  -1.067  47.200  1.00 77.41  ? 103 ARG B CZ  1 
ATOM   2233 N NH1 . ARG B 1 103 ? 0.704   -0.568  46.856  1.00 72.79  ? 103 ARG B NH1 1 
ATOM   2234 N NH2 . ARG B 1 103 ? -1.084  -1.921  46.381  1.00 75.60  ? 103 ARG B NH2 1 
ATOM   2235 N N   . HIS B 1 104 ? -2.260  4.742   45.552  1.00 39.90  ? 104 HIS B N   1 
ATOM   2236 C CA  . HIS B 1 104 ? -1.770  5.290   44.290  1.00 37.14  ? 104 HIS B CA  1 
ATOM   2237 C C   . HIS B 1 104 ? -2.197  6.725   44.036  1.00 38.65  ? 104 HIS B C   1 
ATOM   2238 O O   . HIS B 1 104 ? -1.881  7.273   42.972  1.00 39.07  ? 104 HIS B O   1 
ATOM   2239 C CB  . HIS B 1 104 ? -2.202  4.390   43.132  1.00 38.00  ? 104 HIS B CB  1 
ATOM   2240 C CG  . HIS B 1 104 ? -1.600  3.020   43.201  1.00 42.32  ? 104 HIS B CG  1 
ATOM   2241 N ND1 . HIS B 1 104 ? -2.232  1.896   42.713  1.00 47.90  ? 104 HIS B ND1 1 
ATOM   2242 C CD2 . HIS B 1 104 ? -0.423  2.594   43.718  1.00 43.47  ? 104 HIS B CD2 1 
ATOM   2243 C CE1 . HIS B 1 104 ? -1.465  0.840   42.912  1.00 49.57  ? 104 HIS B CE1 1 
ATOM   2244 N NE2 . HIS B 1 104 ? -0.362  1.236   43.525  1.00 53.26  ? 104 HIS B NE2 1 
ATOM   2245 N N   . ILE B 1 105 ? -2.908  7.338   44.970  1.00 38.61  ? 105 ILE B N   1 
ATOM   2246 C CA  . ILE B 1 105 ? -3.167  8.772   44.983  1.00 39.64  ? 105 ILE B CA  1 
ATOM   2247 C C   . ILE B 1 105 ? -2.529  9.322   46.249  1.00 40.94  ? 105 ILE B C   1 
ATOM   2248 O O   . ILE B 1 105 ? -2.958  8.980   47.358  1.00 41.86  ? 105 ILE B O   1 
ATOM   2249 C CB  . ILE B 1 105 ? -4.668  9.080   44.928  1.00 36.80  ? 105 ILE B CB  1 
ATOM   2250 C CG1 . ILE B 1 105 ? -5.304  8.406   43.693  1.00 37.36  ? 105 ILE B CG1 1 
ATOM   2251 C CG2 . ILE B 1 105 ? -4.904  10.582  44.978  1.00 41.27  ? 105 ILE B CG2 1 
ATOM   2252 C CD1 . ILE B 1 105 ? -6.800  8.715   43.534  1.00 37.96  ? 105 ILE B CD1 1 
ATOM   2253 N N   . ILE B 1 106 ? -1.511  10.174  46.096  1.00 37.94  ? 106 ILE B N   1 
ATOM   2254 C CA  . ILE B 1 106 ? -0.787  10.736  47.235  1.00 35.78  ? 106 ILE B CA  1 
ATOM   2255 C C   . ILE B 1 106 ? -1.228  12.180  47.421  1.00 42.53  ? 106 ILE B C   1 
ATOM   2256 O O   . ILE B 1 106 ? -1.172  12.982  46.482  1.00 41.36  ? 106 ILE B O   1 
ATOM   2257 C CB  . ILE B 1 106 ? 0.738   10.633  47.043  1.00 41.39  ? 106 ILE B CB  1 
ATOM   2258 C CG1 . ILE B 1 106 ? 1.135   9.223   46.583  1.00 38.35  ? 106 ILE B CG1 1 
ATOM   2259 C CG2 . ILE B 1 106 ? 1.459   10.993  48.325  1.00 40.56  ? 106 ILE B CG2 1 
ATOM   2260 C CD1 . ILE B 1 106 ? 0.721   8.133   47.566  1.00 41.25  ? 106 ILE B CD1 1 
ATOM   2261 N N   . ILE B 1 107 ? -1.657  12.515  48.637  1.00 43.27  ? 107 ILE B N   1 
ATOM   2262 C CA  . ILE B 1 107 ? -2.307  13.783  48.926  1.00 47.15  ? 107 ILE B CA  1 
ATOM   2263 C C   . ILE B 1 107 ? -1.448  14.544  49.919  1.00 50.19  ? 107 ILE B C   1 
ATOM   2264 O O   . ILE B 1 107 ? -1.156  14.043  51.010  1.00 43.93  ? 107 ILE B O   1 
ATOM   2265 C CB  . ILE B 1 107 ? -3.736  13.584  49.463  1.00 45.89  ? 107 ILE B CB  1 
ATOM   2266 C CG1 . ILE B 1 107 ? -4.583  12.891  48.391  1.00 50.83  ? 107 ILE B CG1 1 
ATOM   2267 C CG2 . ILE B 1 107 ? -4.334  14.917  49.899  1.00 49.85  ? 107 ILE B CG2 1 
ATOM   2268 C CD1 . ILE B 1 107 ? -5.861  12.298  48.897  1.00 52.59  ? 107 ILE B CD1 1 
ATOM   2269 N N   . SER B 1 108 ? -1.011  15.732  49.514  1.00 52.51  ? 108 SER B N   1 
ATOM   2270 C CA  . SER B 1 108 ? -0.336  16.699  50.368  1.00 58.58  ? 108 SER B CA  1 
ATOM   2271 C C   . SER B 1 108 ? -1.056  18.027  50.168  1.00 58.04  ? 108 SER B C   1 
ATOM   2272 O O   . SER B 1 108 ? -2.289  18.061  50.163  1.00 59.83  ? 108 SER B O   1 
ATOM   2273 C CB  . SER B 1 108 ? 1.156   16.763  50.015  1.00 58.47  ? 108 SER B CB  1 
ATOM   2274 O OG  . SER B 1 108 ? 1.358   17.176  48.669  1.00 52.79  ? 108 SER B OG  1 
ATOM   2275 N N   . ASP B 1 109 ? -0.323  19.122  49.973  1.00 57.06  ? 109 ASP B N   1 
ATOM   2276 C CA  . ASP B 1 109 ? -0.956  20.315  49.420  1.00 55.21  ? 109 ASP B CA  1 
ATOM   2277 C C   . ASP B 1 109 ? -1.436  20.082  47.990  1.00 60.86  ? 109 ASP B C   1 
ATOM   2278 O O   . ASP B 1 109 ? -2.350  20.773  47.522  1.00 54.45  ? 109 ASP B O   1 
ATOM   2279 C CB  . ASP B 1 109 ? 0.038   21.468  49.420  1.00 64.74  ? 109 ASP B CB  1 
ATOM   2280 C CG  . ASP B 1 109 ? 1.431   21.014  49.002  1.00 78.07  ? 109 ASP B CG  1 
ATOM   2281 O OD1 . ASP B 1 109 ? 2.016   20.177  49.726  1.00 76.39  ? 109 ASP B OD1 1 
ATOM   2282 O OD2 . ASP B 1 109 ? 1.913   21.437  47.926  1.00 79.85  ? 109 ASP B OD2 1 
ATOM   2283 N N   . ARG B 1 110 ? -0.835  19.126  47.291  1.00 58.49  ? 110 ARG B N   1 
ATOM   2284 C CA  . ARG B 1 110 ? -1.171  18.768  45.922  1.00 51.49  ? 110 ARG B CA  1 
ATOM   2285 C C   . ARG B 1 110 ? -1.584  17.304  45.861  1.00 52.63  ? 110 ARG B C   1 
ATOM   2286 O O   . ARG B 1 110 ? -1.463  16.557  46.837  1.00 50.78  ? 110 ARG B O   1 
ATOM   2287 C CB  . ARG B 1 110 ? 0.015   19.040  44.992  1.00 48.57  ? 110 ARG B CB  1 
ATOM   2288 C CG  . ARG B 1 110 ? 1.276   18.331  45.426  1.00 49.77  ? 110 ARG B CG  1 
ATOM   2289 C CD  . ARG B 1 110 ? 2.292   18.269  44.298  1.00 49.75  ? 110 ARG B CD  1 
ATOM   2290 N NE  . ARG B 1 110 ? 3.496   17.556  44.702  1.00 45.98  ? 110 ARG B NE  1 
ATOM   2291 C CZ  . ARG B 1 110 ? 4.457   17.182  43.868  1.00 52.47  ? 110 ARG B CZ  1 
ATOM   2292 N NH1 . ARG B 1 110 ? 4.364   17.399  42.565  1.00 52.83  ? 110 ARG B NH1 1 
ATOM   2293 N NH2 . ARG B 1 110 ? 5.542   16.584  44.355  1.00 47.75  ? 110 ARG B NH2 1 
ATOM   2294 N N   . ILE B 1 111 ? -2.072  16.900  44.691  1.00 43.88  ? 111 ILE B N   1 
ATOM   2295 C CA  . ILE B 1 111 ? -2.587  15.559  44.451  1.00 41.43  ? 111 ILE B CA  1 
ATOM   2296 C C   . ILE B 1 111 ? -1.735  14.942  43.346  1.00 42.66  ? 111 ILE B C   1 
ATOM   2297 O O   . ILE B 1 111 ? -1.694  15.470  42.226  1.00 42.80  ? 111 ILE B O   1 
ATOM   2298 C CB  . ILE B 1 111 ? -4.063  15.592  44.024  1.00 41.31  ? 111 ILE B CB  1 
ATOM   2299 C CG1 . ILE B 1 111 ? -4.932  16.344  45.047  1.00 49.72  ? 111 ILE B CG1 1 
ATOM   2300 C CG2 . ILE B 1 111 ? -4.589  14.179  43.779  1.00 42.32  ? 111 ILE B CG2 1 
ATOM   2301 C CD1 . ILE B 1 111 ? -4.740  15.939  46.468  1.00 52.72  ? 111 ILE B CD1 1 
ATOM   2302 N N   . VAL B 1 112 ? -1.065  13.829  43.635  1.00 34.92  ? 112 VAL B N   1 
ATOM   2303 C CA  . VAL B 1 112 ? -0.246  13.153  42.628  1.00 37.47  ? 112 VAL B CA  1 
ATOM   2304 C C   . VAL B 1 112 ? -0.740  11.726  42.471  1.00 39.25  ? 112 VAL B C   1 
ATOM   2305 O O   . VAL B 1 112 ? -0.964  11.030  43.467  1.00 35.39  ? 112 VAL B O   1 
ATOM   2306 C CB  . VAL B 1 112 ? 1.252   13.178  42.979  1.00 32.68  ? 112 VAL B CB  1 
ATOM   2307 C CG1 . VAL B 1 112 ? 2.078   12.519  41.824  1.00 28.92  ? 112 VAL B CG1 1 
ATOM   2308 C CG2 . VAL B 1 112 ? 1.692   14.622  43.263  1.00 41.86  ? 112 VAL B CG2 1 
ATOM   2309 N N   . PHE B 1 113 ? -0.930  11.308  41.223  1.00 30.84  ? 113 PHE B N   1 
ATOM   2310 C CA  . PHE B 1 113 ? -1.215  9.922   40.887  1.00 30.54  ? 113 PHE B CA  1 
ATOM   2311 C C   . PHE B 1 113 ? 0.097   9.204   40.608  1.00 36.36  ? 113 PHE B C   1 
ATOM   2312 O O   . PHE B 1 113 ? 0.975   9.739   39.930  1.00 32.88  ? 113 PHE B O   1 
ATOM   2313 C CB  . PHE B 1 113 ? -2.114  9.839   39.649  1.00 30.36  ? 113 PHE B CB  1 
ATOM   2314 C CG  . PHE B 1 113 ? -3.572  10.142  39.905  1.00 33.03  ? 113 PHE B CG  1 
ATOM   2315 C CD1 . PHE B 1 113 ? -3.960  10.970  40.937  1.00 33.20  ? 113 PHE B CD1 1 
ATOM   2316 C CD2 . PHE B 1 113 ? -4.549  9.652   39.033  1.00 38.71  ? 113 PHE B CD2 1 
ATOM   2317 C CE1 . PHE B 1 113 ? -5.298  11.269  41.142  1.00 37.85  ? 113 PHE B CE1 1 
ATOM   2318 C CE2 . PHE B 1 113 ? -5.895  9.943   39.221  1.00 36.30  ? 113 PHE B CE2 1 
ATOM   2319 C CZ  . PHE B 1 113 ? -6.276  10.759  40.283  1.00 34.00  ? 113 PHE B CZ  1 
ATOM   2320 N N   . ILE B 1 114 ? 0.240   7.985   41.123  1.00 28.37  ? 114 ILE B N   1 
ATOM   2321 C CA  . ILE B 1 114 ? 1.452   7.230   40.861  1.00 29.51  ? 114 ILE B CA  1 
ATOM   2322 C C   . ILE B 1 114 ? 1.057   5.845   40.386  1.00 30.66  ? 114 ILE B C   1 
ATOM   2323 O O   . ILE B 1 114 ? -0.093  5.417   40.531  1.00 33.03  ? 114 ILE B O   1 
ATOM   2324 C CB  . ILE B 1 114 ? 2.392   7.156   42.099  1.00 32.18  ? 114 ILE B CB  1 
ATOM   2325 C CG1 . ILE B 1 114 ? 1.711   6.414   43.255  1.00 33.84  ? 114 ILE B CG1 1 
ATOM   2326 C CG2 . ILE B 1 114 ? 2.845   8.553   42.529  1.00 30.34  ? 114 ILE B CG2 1 
ATOM   2327 C CD1 . ILE B 1 114 ? 2.673   6.054   44.421  1.00 35.66  ? 114 ILE B CD1 1 
ATOM   2328 N N   . ASP B 1 115 ? 2.035   5.168   39.784  1.00 30.27  ? 115 ASP B N   1 
ATOM   2329 C CA  . ASP B 1 115 ? 1.954   3.788   39.292  1.00 32.20  ? 115 ASP B CA  1 
ATOM   2330 C C   . ASP B 1 115 ? 1.145   3.676   38.004  1.00 29.56  ? 115 ASP B C   1 
ATOM   2331 O O   . ASP B 1 115 ? -0.052  3.341   38.025  1.00 27.01  ? 115 ASP B O   1 
ATOM   2332 C CB  . ASP B 1 115 ? 1.395   2.846   40.374  1.00 36.14  ? 115 ASP B CB  1 
ATOM   2333 C CG  . ASP B 1 115 ? 1.278   1.400   39.878  1.00 50.07  ? 115 ASP B CG  1 
ATOM   2334 O OD1 . ASP B 1 115 ? 1.960   1.078   38.879  1.00 46.78  ? 115 ASP B OD1 1 
ATOM   2335 O OD2 . ASP B 1 115 ? 0.573   0.574   40.502  1.00 54.50  ? 115 ASP B OD2 1 
ATOM   2336 N N   . PHE B 1 116 ? 1.822   3.881   36.869  1.00 28.60  ? 116 PHE B N   1 
ATOM   2337 C CA  . PHE B 1 116 ? 1.212   3.811   35.543  1.00 30.27  ? 116 PHE B CA  1 
ATOM   2338 C C   . PHE B 1 116 ? 1.570   2.532   34.793  1.00 30.47  ? 116 PHE B C   1 
ATOM   2339 O O   . PHE B 1 116 ? 1.299   2.419   33.594  1.00 31.00  ? 116 PHE B O   1 
ATOM   2340 C CB  . PHE B 1 116 ? 1.608   5.062   34.749  1.00 28.20  ? 116 PHE B CB  1 
ATOM   2341 C CG  . PHE B 1 116 ? 0.824   6.282   35.168  1.00 30.19  ? 116 PHE B CG  1 
ATOM   2342 C CD1 . PHE B 1 116 ? 1.229   7.051   36.255  1.00 32.39  ? 116 PHE B CD1 1 
ATOM   2343 C CD2 . PHE B 1 116 ? -0.344  6.615   34.513  1.00 32.76  ? 116 PHE B CD2 1 
ATOM   2344 C CE1 . PHE B 1 116 ? 0.486   8.177   36.656  1.00 30.13  ? 116 PHE B CE1 1 
ATOM   2345 C CE2 . PHE B 1 116 ? -1.099  7.715   34.909  1.00 32.57  ? 116 PHE B CE2 1 
ATOM   2346 C CZ  . PHE B 1 116 ? -0.680  8.497   35.978  1.00 29.52  ? 116 PHE B CZ  1 
ATOM   2347 N N   . GLU B 1 117 ? 2.113   1.532   35.492  1.00 29.06  ? 117 GLU B N   1 
ATOM   2348 C CA  . GLU B 1 117 ? 2.647   0.337   34.844  1.00 29.79  ? 117 GLU B CA  1 
ATOM   2349 C C   . GLU B 1 117 ? 1.567   -0.547  34.226  1.00 32.74  ? 117 GLU B C   1 
ATOM   2350 O O   . GLU B 1 117 ? 1.888   -1.423  33.418  1.00 30.62  ? 117 GLU B O   1 
ATOM   2351 C CB  . GLU B 1 117 ? 3.496   -0.423  35.879  1.00 30.02  ? 117 GLU B CB  1 
ATOM   2352 C CG  . GLU B 1 117 ? 2.687   -0.991  36.984  1.00 37.11  ? 117 GLU B CG  1 
ATOM   2353 C CD  . GLU B 1 117 ? 3.350   -2.184  37.640  1.00 49.83  ? 117 GLU B CD  1 
ATOM   2354 O OE1 . GLU B 1 117 ? 4.180   -1.929  38.543  1.00 49.68  ? 117 GLU B OE1 1 
ATOM   2355 O OE2 . GLU B 1 117 ? 3.064   -3.342  37.259  1.00 52.82  ? 117 GLU B OE2 1 
ATOM   2356 N N   . ARG B 1 118 ? 0.299   -0.379  34.608  1.00 29.89  ? 118 ARG B N   1 
ATOM   2357 C CA  . ARG B 1 118 ? -0.799  -1.106  33.982  1.00 32.18  ? 118 ARG B CA  1 
ATOM   2358 C C   . ARG B 1 118 ? -1.579  -0.280  32.956  1.00 35.04  ? 118 ARG B C   1 
ATOM   2359 O O   . ARG B 1 118 ? -2.569  -0.772  32.399  1.00 30.56  ? 118 ARG B O   1 
ATOM   2360 C CB  . ARG B 1 118 ? -1.737  -1.633  35.072  1.00 32.79  ? 118 ARG B CB  1 
ATOM   2361 C CG  . ARG B 1 118 ? -1.134  -2.853  35.794  1.00 42.60  ? 118 ARG B CG  1 
ATOM   2362 C CD  . ARG B 1 118 ? -2.188  -3.698  36.492  1.00 56.93  ? 118 ARG B CD  1 
ATOM   2363 N NE  . ARG B 1 118 ? -3.119  -4.288  35.532  1.00 62.78  ? 118 ARG B NE  1 
ATOM   2364 C CZ  . ARG B 1 118 ? -4.393  -4.573  35.789  1.00 64.72  ? 118 ARG B CZ  1 
ATOM   2365 N NH1 . ARG B 1 118 ? -4.881  -4.519  37.019  1.00 58.06  ? 118 ARG B NH1 1 
ATOM   2366 N NH2 . ARG B 1 118 ? -5.182  -4.974  34.794  1.00 62.29  ? 118 ARG B NH2 1 
ATOM   2367 N N   . GLY B 1 119 ? -1.149  0.943   32.668  1.00 27.83  ? 119 GLY B N   1 
ATOM   2368 C CA  . GLY B 1 119 ? -1.942  1.805   31.798  1.00 28.83  ? 119 GLY B CA  1 
ATOM   2369 C C   . GLY B 1 119 ? -2.123  1.230   30.406  1.00 36.15  ? 119 GLY B C   1 
ATOM   2370 O O   . GLY B 1 119 ? -1.289  0.476   29.901  1.00 32.36  ? 119 GLY B O   1 
ATOM   2371 N N   . VAL B 1 120 ? -3.236  1.602   29.769  1.00 32.89  ? 120 VAL B N   1 
ATOM   2372 C CA  . VAL B 1 120 ? -3.502  1.287   28.366  1.00 33.88  ? 120 VAL B CA  1 
ATOM   2373 C C   . VAL B 1 120 ? -4.201  2.473   27.717  1.00 35.06  ? 120 VAL B C   1 
ATOM   2374 O O   . VAL B 1 120 ? -4.875  3.261   28.384  1.00 32.07  ? 120 VAL B O   1 
ATOM   2375 C CB  . VAL B 1 120 ? -4.362  0.011   28.186  1.00 33.85  ? 120 VAL B CB  1 
ATOM   2376 C CG1 . VAL B 1 120 ? -3.807  -1.140  28.980  1.00 45.47  ? 120 VAL B CG1 1 
ATOM   2377 C CG2 . VAL B 1 120 ? -5.774  0.284   28.692  1.00 41.70  ? 120 VAL B CG2 1 
ATOM   2378 N N   . ILE B 1 121 ? -4.055  2.586   26.403  1.00 33.62  ? 121 ILE B N   1 
ATOM   2379 C CA  . ILE B 1 121 ? -4.753  3.608   25.623  1.00 32.40  ? 121 ILE B CA  1 
ATOM   2380 C C   . ILE B 1 121 ? -6.144  3.089   25.276  1.00 34.19  ? 121 ILE B C   1 
ATOM   2381 O O   . ILE B 1 121 ? -6.295  1.924   24.888  1.00 38.87  ? 121 ILE B O   1 
ATOM   2382 C CB  . ILE B 1 121 ? -3.945  3.955   24.358  1.00 34.24  ? 121 ILE B CB  1 
ATOM   2383 C CG1 . ILE B 1 121 ? -2.613  4.622   24.753  1.00 34.79  ? 121 ILE B CG1 1 
ATOM   2384 C CG2 . ILE B 1 121 ? -4.778  4.815   23.359  1.00 35.26  ? 121 ILE B CG2 1 
ATOM   2385 C CD1 . ILE B 1 121 ? -1.706  5.048   23.562  1.00 36.72  ? 121 ILE B CD1 1 
ATOM   2386 N N   . LYS B 1 122 ? -7.181  3.906   25.489  1.00 34.76  ? 122 LYS B N   1 
ATOM   2387 C CA  . LYS B 1 122 ? -8.486  3.557   24.931  1.00 45.54  ? 122 LYS B CA  1 
ATOM   2388 C C   . LYS B 1 122 ? -9.341  4.789   24.703  1.00 41.94  ? 122 LYS B C   1 
ATOM   2389 O O   . LYS B 1 122 ? -9.133  5.842   25.306  1.00 39.65  ? 122 LYS B O   1 
ATOM   2390 C CB  . LYS B 1 122 ? -9.286  2.530   25.728  1.00 51.63  ? 122 LYS B CB  1 
ATOM   2391 C CG  . LYS B 1 122 ? -9.051  2.396   27.155  1.00 46.92  ? 122 LYS B CG  1 
ATOM   2392 C CD  . LYS B 1 122 ? -9.629  1.027   27.498  1.00 61.53  ? 122 LYS B CD  1 
ATOM   2393 C CE  . LYS B 1 122 ? -8.977  -0.037  26.590  1.00 54.49  ? 122 LYS B CE  1 
ATOM   2394 N NZ  . LYS B 1 122 ? -9.326  -1.444  26.927  1.00 68.23  ? 122 LYS B NZ  1 
ATOM   2395 N N   . CYS B 1 123 ? -10.322 4.602   23.813  1.00 39.28  ? 123 CYS B N   1 
ATOM   2396 C CA  . CYS B 1 123 ? -11.178 5.684   23.333  1.00 46.34  ? 123 CYS B CA  1 
ATOM   2397 C C   . CYS B 1 123 ? -11.903 6.372   24.479  1.00 44.24  ? 123 CYS B C   1 
ATOM   2398 O O   . CYS B 1 123 ? -11.899 7.606   24.578  1.00 44.81  ? 123 CYS B O   1 
ATOM   2399 C CB  . CYS B 1 123 ? -12.194 5.117   22.339  1.00 51.79  ? 123 CYS B CB  1 
ATOM   2400 S SG  . CYS B 1 123 ? -11.456 4.535   20.797  1.00 80.24  ? 123 CYS B SG  1 
ATOM   2401 N N   . ARG B 1 124 ? -12.545 5.589   25.349  1.00 47.73  ? 124 ARG B N   1 
ATOM   2402 C CA  . ARG B 1 124 ? -13.281 6.126   26.493  1.00 48.64  ? 124 ARG B CA  1 
ATOM   2403 C C   . ARG B 1 124 ? -12.819 5.414   27.758  1.00 41.55  ? 124 ARG B C   1 
ATOM   2404 O O   . ARG B 1 124 ? -13.436 4.431   28.195  1.00 45.35  ? 124 ARG B O   1 
ATOM   2405 C CB  . ARG B 1 124 ? -14.795 6.004   26.309  1.00 51.57  ? 124 ARG B CB  1 
ATOM   2406 C CG  . ARG B 1 124 ? -15.314 6.486   24.965  1.00 49.52  ? 124 ARG B CG  1 
ATOM   2407 C CD  . ARG B 1 124 ? -16.808 6.828   25.055  1.00 67.01  ? 124 ARG B CD  1 
ATOM   2408 N NE  . ARG B 1 124 ? -17.161 7.948   24.189  1.00 69.55  ? 124 ARG B NE  1 
ATOM   2409 C CZ  . ARG B 1 124 ? -18.402 8.346   23.936  1.00 73.11  ? 124 ARG B CZ  1 
ATOM   2410 N NH1 . ARG B 1 124 ? -19.445 7.741   24.481  1.00 61.58  ? 124 ARG B NH1 1 
ATOM   2411 N NH2 . ARG B 1 124 ? -18.602 9.363   23.097  1.00 71.30  ? 124 ARG B NH2 1 
ATOM   2412 N N   . PRO B 1 125 ? -11.744 5.901   28.382  1.00 39.58  ? 125 PRO B N   1 
ATOM   2413 C CA  . PRO B 1 125 ? -11.220 5.256   29.600  1.00 39.26  ? 125 PRO B CA  1 
ATOM   2414 C C   . PRO B 1 125 ? -12.236 5.204   30.734  1.00 43.76  ? 125 PRO B C   1 
ATOM   2415 O O   . PRO B 1 125 ? -13.243 5.918   30.750  1.00 41.87  ? 125 PRO B O   1 
ATOM   2416 C CB  . PRO B 1 125 ? -10.028 6.147   29.981  1.00 34.51  ? 125 PRO B CB  1 
ATOM   2417 C CG  . PRO B 1 125 ? -9.594  6.762   28.655  1.00 39.94  ? 125 PRO B CG  1 
ATOM   2418 C CD  . PRO B 1 125 ? -10.895 7.016   27.929  1.00 38.95  ? 125 PRO B CD  1 
ATOM   2419 N N   . SER B 1 126 ? -11.940 4.346   31.713  1.00 37.75  ? 126 SER B N   1 
ATOM   2420 C CA  . SER B 1 126 ? -12.801 4.130   32.868  1.00 43.56  ? 126 SER B CA  1 
ATOM   2421 C C   . SER B 1 126 ? -12.209 4.698   34.157  1.00 40.36  ? 126 SER B C   1 
ATOM   2422 O O   . SER B 1 126 ? -12.526 4.210   35.243  1.00 44.73  ? 126 SER B O   1 
ATOM   2423 C CB  . SER B 1 126 ? -13.094 2.642   33.052  1.00 42.43  ? 126 SER B CB  1 
ATOM   2424 O OG  . SER B 1 126 ? -13.774 2.129   31.923  1.00 57.18  ? 126 SER B OG  1 
ATOM   2425 N N   . ASN B 1 127 ? -11.342 5.711   34.064  1.00 32.83  ? 127 ASN B N   1 
ATOM   2426 C CA  . ASN B 1 127 ? -10.714 6.233   35.275  1.00 32.60  ? 127 ASN B CA  1 
ATOM   2427 C C   . ASN B 1 127 ? -11.756 6.800   36.216  1.00 40.10  ? 127 ASN B C   1 
ATOM   2428 O O   . ASN B 1 127 ? -11.748 6.517   37.422  1.00 35.39  ? 127 ASN B O   1 
ATOM   2429 C CB  . ASN B 1 127 ? -9.688  7.316   34.942  1.00 28.21  ? 127 ASN B CB  1 
ATOM   2430 C CG  . ASN B 1 127 ? -8.637  6.827   33.997  1.00 35.20  ? 127 ASN B CG  1 
ATOM   2431 O OD1 . ASN B 1 127 ? -7.897  5.899   34.316  1.00 35.41  ? 127 ASN B OD1 1 
ATOM   2432 N ND2 . ASN B 1 127 ? -8.597  7.408   32.798  1.00 33.85  ? 127 ASN B ND2 1 
ATOM   2433 N N   . LEU B 1 128 ? -12.648 7.637   35.679  1.00 38.89  ? 128 LEU B N   1 
ATOM   2434 C CA  . LEU B 1 128 ? -13.619 8.314   36.526  1.00 37.58  ? 128 LEU B CA  1 
ATOM   2435 C C   . LEU B 1 128 ? -14.661 7.339   37.059  1.00 44.25  ? 128 LEU B C   1 
ATOM   2436 O O   . LEU B 1 128 ? -15.064 7.435   38.224  1.00 43.53  ? 128 LEU B O   1 
ATOM   2437 C CB  . LEU B 1 128 ? -14.283 9.450   35.742  1.00 37.79  ? 128 LEU B CB  1 
ATOM   2438 C CG  . LEU B 1 128 ? -15.209 10.376  36.523  1.00 46.39  ? 128 LEU B CG  1 
ATOM   2439 C CD1 . LEU B 1 128 ? -14.501 10.978  37.743  1.00 42.88  ? 128 LEU B CD1 1 
ATOM   2440 C CD2 . LEU B 1 128 ? -15.712 11.468  35.575  1.00 49.41  ? 128 LEU B CD2 1 
ATOM   2441 N N   . THR B 1 129 ? -15.115 6.390   36.226  1.00 38.20  ? 129 THR B N   1 
ATOM   2442 C CA  . THR B 1 129 ? -16.151 5.470   36.697  1.00 40.19  ? 129 THR B CA  1 
ATOM   2443 C C   . THR B 1 129 ? -15.584 4.460   37.686  1.00 43.27  ? 129 THR B C   1 
ATOM   2444 O O   . THR B 1 129 ? -16.280 4.047   38.621  1.00 50.36  ? 129 THR B O   1 
ATOM   2445 C CB  . THR B 1 129 ? -16.797 4.741   35.517  1.00 44.36  ? 129 THR B CB  1 
ATOM   2446 O OG1 . THR B 1 129 ? -15.803 3.929   34.869  1.00 42.10  ? 129 THR B OG1 1 
ATOM   2447 C CG2 . THR B 1 129 ? -17.399 5.729   34.507  1.00 43.79  ? 129 THR B CG2 1 
ATOM   2448 N N   . GLN B 1 130 ? -14.321 4.076   37.514  1.00 37.05  ? 130 GLN B N   1 
ATOM   2449 C CA  . GLN B 1 130 ? -13.651 3.242   38.508  1.00 41.49  ? 130 GLN B CA  1 
ATOM   2450 C C   . GLN B 1 130 ? -13.482 3.997   39.826  1.00 46.79  ? 130 GLN B C   1 
ATOM   2451 O O   . GLN B 1 130 ? -13.838 3.484   40.898  1.00 43.02  ? 130 GLN B O   1 
ATOM   2452 C CB  . GLN B 1 130 ? -12.296 2.797   37.959  1.00 40.46  ? 130 GLN B CB  1 
ATOM   2453 C CG  . GLN B 1 130 ? -12.362 1.577   37.056  1.00 46.58  ? 130 GLN B CG  1 
ATOM   2454 C CD  . GLN B 1 130 ? -11.028 1.276   36.365  1.00 45.98  ? 130 GLN B CD  1 
ATOM   2455 O OE1 . GLN B 1 130 ? -9.971  1.751   36.780  1.00 39.50  ? 130 GLN B OE1 1 
ATOM   2456 N NE2 . GLN B 1 130 ? -11.088 0.515   35.270  1.00 50.22  ? 130 GLN B NE2 1 
ATOM   2457 N N   . PHE B 1 131 ? -12.993 5.246   39.758  1.00 41.32  ? 131 PHE B N   1 
ATOM   2458 C CA  . PHE B 1 131 ? -12.785 6.016   40.987  1.00 42.43  ? 131 PHE B CA  1 
ATOM   2459 C C   . PHE B 1 131 ? -14.105 6.284   41.709  1.00 44.97  ? 131 PHE B C   1 
ATOM   2460 O O   . PHE B 1 131 ? -14.153 6.277   42.944  1.00 50.78  ? 131 PHE B O   1 
ATOM   2461 C CB  . PHE B 1 131 ? -12.078 7.344   40.701  1.00 38.24  ? 131 PHE B CB  1 
ATOM   2462 C CG  . PHE B 1 131 ? -11.720 8.102   41.955  1.00 47.47  ? 131 PHE B CG  1 
ATOM   2463 C CD1 . PHE B 1 131 ? -10.814 7.576   42.870  1.00 45.49  ? 131 PHE B CD1 1 
ATOM   2464 C CD2 . PHE B 1 131 ? -12.372 9.275   42.276  1.00 44.40  ? 131 PHE B CD2 1 
ATOM   2465 C CE1 . PHE B 1 131 ? -10.512 8.249   44.056  1.00 47.79  ? 131 PHE B CE1 1 
ATOM   2466 C CE2 . PHE B 1 131 ? -12.083 9.955   43.463  1.00 49.90  ? 131 PHE B CE2 1 
ATOM   2467 C CZ  . PHE B 1 131 ? -11.149 9.433   44.354  1.00 46.41  ? 131 PHE B CZ  1 
ATOM   2468 N N   . ALA B 1 132 ? -15.185 6.538   40.961  1.00 43.00  ? 132 ALA B N   1 
ATOM   2469 C CA  . ALA B 1 132 ? -16.471 6.803   41.611  1.00 43.60  ? 132 ALA B CA  1 
ATOM   2470 C C   . ALA B 1 132 ? -16.945 5.596   42.404  1.00 47.40  ? 132 ALA B C   1 
ATOM   2471 O O   . ALA B 1 132 ? -17.572 5.742   43.463  1.00 48.89  ? 132 ALA B O   1 
ATOM   2472 C CB  . ALA B 1 132 ? -17.517 7.207   40.574  1.00 44.86  ? 132 ALA B CB  1 
ATOM   2473 N N   . VAL B 1 133 ? -16.673 4.392   41.905  1.00 45.51  ? 133 VAL B N   1 
ATOM   2474 C CA  . VAL B 1 133 ? -17.046 3.197   42.654  1.00 49.26  ? 133 VAL B CA  1 
ATOM   2475 C C   . VAL B 1 133 ? -16.276 3.145   43.970  1.00 47.79  ? 133 VAL B C   1 
ATOM   2476 O O   . VAL B 1 133 ? -16.847 2.864   45.029  1.00 54.62  ? 133 VAL B O   1 
ATOM   2477 C CB  . VAL B 1 133 ? -16.828 1.935   41.800  1.00 51.06  ? 133 VAL B CB  1 
ATOM   2478 C CG1 . VAL B 1 133 ? -16.829 0.702   42.683  1.00 49.50  ? 133 VAL B CG1 1 
ATOM   2479 C CG2 . VAL B 1 133 ? -17.903 1.843   40.716  1.00 48.46  ? 133 VAL B CG2 1 
ATOM   2480 N N   . TYR B 1 134 ? -14.969 3.431   43.929  1.00 45.74  ? 134 TYR B N   1 
ATOM   2481 C CA  . TYR B 1 134 ? -14.193 3.488   45.166  1.00 43.67  ? 134 TYR B CA  1 
ATOM   2482 C C   . TYR B 1 134 ? -14.731 4.581   46.076  1.00 52.09  ? 134 TYR B C   1 
ATOM   2483 O O   . TYR B 1 134 ? -15.005 4.349   47.266  1.00 51.62  ? 134 TYR B O   1 
ATOM   2484 C CB  . TYR B 1 134 ? -12.713 3.735   44.853  1.00 46.25  ? 134 TYR B CB  1 
ATOM   2485 C CG  . TYR B 1 134 ? -11.903 4.217   46.052  1.00 42.15  ? 134 TYR B CG  1 
ATOM   2486 C CD1 . TYR B 1 134 ? -11.319 3.312   46.928  1.00 47.18  ? 134 TYR B CD1 1 
ATOM   2487 C CD2 . TYR B 1 134 ? -11.699 5.578   46.286  1.00 48.49  ? 134 TYR B CD2 1 
ATOM   2488 C CE1 . TYR B 1 134 ? -10.567 3.750   48.033  1.00 45.95  ? 134 TYR B CE1 1 
ATOM   2489 C CE2 . TYR B 1 134 ? -10.951 6.028   47.395  1.00 46.78  ? 134 TYR B CE2 1 
ATOM   2490 C CZ  . TYR B 1 134 ? -10.384 5.109   48.253  1.00 49.75  ? 134 TYR B CZ  1 
ATOM   2491 O OH  . TYR B 1 134 ? -9.645  5.548   49.343  1.00 50.45  ? 134 TYR B OH  1 
ATOM   2492 N N   . LEU B 1 135 ? -14.931 5.776   45.512  1.00 45.14  ? 135 LEU B N   1 
ATOM   2493 C CA  . LEU B 1 135 ? -15.420 6.910   46.291  1.00 52.51  ? 135 LEU B CA  1 
ATOM   2494 C C   . LEU B 1 135 ? -16.724 6.573   47.000  1.00 57.86  ? 135 LEU B C   1 
ATOM   2495 O O   . LEU B 1 135 ? -16.876 6.810   48.206  1.00 58.74  ? 135 LEU B O   1 
ATOM   2496 C CB  . LEU B 1 135 ? -15.613 8.117   45.372  1.00 51.38  ? 135 LEU B CB  1 
ATOM   2497 C CG  . LEU B 1 135 ? -15.878 9.459   46.046  1.00 63.44  ? 135 LEU B CG  1 
ATOM   2498 C CD1 . LEU B 1 135 ? -14.612 9.955   46.754  1.00 59.98  ? 135 LEU B CD1 1 
ATOM   2499 C CD2 . LEU B 1 135 ? -16.351 10.456  45.015  1.00 62.76  ? 135 LEU B CD2 1 
ATOM   2500 N N   . ASN B 1 136 ? -17.679 5.998   46.266  1.00 55.03  ? 136 ASN B N   1 
ATOM   2501 C CA  . ASN B 1 136 ? -18.937 5.608   46.892  1.00 55.80  ? 136 ASN B CA  1 
ATOM   2502 C C   . ASN B 1 136 ? -18.738 4.483   47.904  1.00 58.52  ? 136 ASN B C   1 
ATOM   2503 O O   . ASN B 1 136 ? -19.460 4.413   48.908  1.00 60.89  ? 136 ASN B O   1 
ATOM   2504 C CB  . ASN B 1 136 ? -19.941 5.192   45.819  1.00 52.69  ? 136 ASN B CB  1 
ATOM   2505 C CG  . ASN B 1 136 ? -21.367 5.236   46.308  1.00 58.69  ? 136 ASN B CG  1 
ATOM   2506 O OD1 . ASN B 1 136 ? -21.791 6.222   46.912  1.00 57.05  ? 136 ASN B OD1 1 
ATOM   2507 N ND2 . ASN B 1 136 ? -22.133 4.182   46.021  1.00 60.43  ? 136 ASN B ND2 1 
ATOM   2508 N N   . SER B 1 137 ? -17.767 3.604   47.663  1.00 57.74  ? 137 SER B N   1 
ATOM   2509 C CA  . SER B 1 137 ? -17.518 2.499   48.577  1.00 61.54  ? 137 SER B CA  1 
ATOM   2510 C C   . SER B 1 137 ? -16.995 2.987   49.920  1.00 60.92  ? 137 SER B C   1 
ATOM   2511 O O   . SER B 1 137 ? -17.302 2.387   50.956  1.00 65.03  ? 137 SER B O   1 
ATOM   2512 C CB  . SER B 1 137 ? -16.527 1.520   47.941  1.00 64.46  ? 137 SER B CB  1 
ATOM   2513 O OG  . SER B 1 137 ? -16.270 0.440   48.818  1.00 72.61  ? 137 SER B OG  1 
ATOM   2514 N N   . ARG B 1 138 ? -16.233 4.080   49.933  1.00 61.81  ? 138 ARG B N   1 
ATOM   2515 C CA  . ARG B 1 138 ? -15.649 4.571   51.176  1.00 64.70  ? 138 ARG B CA  1 
ATOM   2516 C C   . ARG B 1 138 ? -16.521 5.615   51.859  1.00 65.19  ? 138 ARG B C   1 
ATOM   2517 O O   . ARG B 1 138 ? -16.593 5.646   53.094  1.00 62.56  ? 138 ARG B O   1 
ATOM   2518 C CB  . ARG B 1 138 ? -14.266 5.170   50.905  1.00 58.10  ? 138 ARG B CB  1 
ATOM   2519 C CG  . ARG B 1 138 ? -13.216 4.164   50.454  1.00 54.84  ? 138 ARG B CG  1 
ATOM   2520 C CD  . ARG B 1 138 ? -12.957 3.068   51.478  1.00 62.71  ? 138 ARG B CD  1 
ATOM   2521 N NE  . ARG B 1 138 ? -12.287 1.935   50.846  1.00 60.92  ? 138 ARG B NE  1 
ATOM   2522 N N   . LEU B 1 139 ? -17.212 6.448   51.081  1.00 60.30  ? 139 LEU B N   1 
ATOM   2523 C CA  . LEU B 1 139 ? -17.999 7.546   51.620  1.00 60.55  ? 139 LEU B CA  1 
ATOM   2524 C C   . LEU B 1 139 ? -19.487 7.214   51.669  1.00 65.87  ? 139 LEU B C   1 
ATOM   2525 O O   . LEU B 1 139 ? -20.268 7.988   52.241  1.00 70.89  ? 139 LEU B O   1 
ATOM   2526 C CB  . LEU B 1 139 ? -17.753 8.788   50.760  1.00 56.60  ? 139 LEU B CB  1 
ATOM   2527 C CG  . LEU B 1 139 ? -16.309 9.300   50.834  1.00 56.55  ? 139 LEU B CG  1 
ATOM   2528 C CD1 . LEU B 1 139 ? -16.199 10.736  50.371  1.00 67.35  ? 139 LEU B CD1 1 
ATOM   2529 C CD2 . LEU B 1 139 ? -15.776 9.165   52.263  1.00 62.18  ? 139 LEU B CD2 1 
ATOM   2530 N N   . ARG B 1 140 ? -19.866 6.058   51.122  1.00 66.32  ? 140 ARG B N   1 
ATOM   2531 C CA  . ARG B 1 140 ? -21.245 5.576   51.006  1.00 68.04  ? 140 ARG B CA  1 
ATOM   2532 C C   . ARG B 1 140 ? -22.202 6.721   50.685  1.00 67.97  ? 140 ARG B C   1 
ATOM   2533 O O   . ARG B 1 140 ? -23.174 6.988   51.395  1.00 67.87  ? 140 ARG B O   1 
ATOM   2534 C CB  . ARG B 1 140 ? -21.660 4.812   52.259  1.00 69.17  ? 140 ARG B CB  1 
ATOM   2535 C CG  . ARG B 1 140 ? -21.015 3.425   52.268  1.00 80.18  ? 140 ARG B CG  1 
ATOM   2536 C CD  . ARG B 1 140 ? -21.492 2.582   53.412  1.00 78.39  ? 140 ARG B CD  1 
ATOM   2537 N NE  . ARG B 1 140 ? -22.845 2.975   53.772  1.00 74.87  ? 140 ARG B NE  1 
ATOM   2538 C CZ  . ARG B 1 140 ? -23.678 2.215   54.465  1.00 81.19  ? 140 ARG B CZ  1 
ATOM   2539 N NH1 . ARG B 1 140 ? -23.355 0.983   54.822  1.00 91.00  ? 140 ARG B NH1 1 
ATOM   2540 N NH2 . ARG B 1 140 ? -24.897 2.673   54.738  1.00 86.57  ? 140 ARG B NH2 1 
ATOM   2541 N N   . LEU B 1 141 ? -21.883 7.416   49.596  1.00 65.43  ? 141 LEU B N   1 
ATOM   2542 C CA  . LEU B 1 141 ? -22.577 8.640   49.230  1.00 68.34  ? 141 LEU B CA  1 
ATOM   2543 C C   . LEU B 1 141 ? -24.007 8.371   48.773  1.00 75.13  ? 141 LEU B C   1 
ATOM   2544 O O   . LEU B 1 141 ? -24.886 9.220   48.954  1.00 70.48  ? 141 LEU B O   1 
ATOM   2545 C CB  . LEU B 1 141 ? -21.810 9.343   48.111  1.00 72.32  ? 141 LEU B CB  1 
ATOM   2546 C CG  . LEU B 1 141 ? -20.612 10.211  48.509  1.00 67.41  ? 141 LEU B CG  1 
ATOM   2547 C CD1 . LEU B 1 141 ? -19.861 10.711  47.258  1.00 63.25  ? 141 LEU B CD1 1 
ATOM   2548 C CD2 . LEU B 1 141 ? -20.934 11.301  49.515  1.00 75.05  ? 141 LEU B CD2 1 
ATOM   2549 N N   . MET B 1 142 ? -24.258 7.197   48.198  1.00 69.27  ? 142 MET B N   1 
ATOM   2550 C CA  . MET B 1 142 ? -25.479 6.912   47.455  1.00 63.41  ? 142 MET B CA  1 
ATOM   2551 C C   . MET B 1 142 ? -25.539 5.410   47.222  1.00 66.44  ? 142 MET B C   1 
ATOM   2552 O O   . MET B 1 142 ? -24.530 4.714   47.354  1.00 72.65  ? 142 MET B O   1 
ATOM   2553 C CB  . MET B 1 142 ? -25.479 7.712   46.147  1.00 68.05  ? 142 MET B CB  1 
ATOM   2554 C CG  . MET B 1 142 ? -24.773 7.016   44.981  1.00 66.48  ? 142 MET B CG  1 
ATOM   2555 S SD  . MET B 1 142 ? -24.729 8.025   43.475  1.00 71.48  ? 142 MET B SD  1 
ATOM   2556 C CE  . MET B 1 142 ? -23.654 9.371   43.977  1.00 64.58  ? 142 MET B CE  1 
ATOM   2557 N N   . LYS B 1 143 ? -26.721 4.908   46.873  1.00 68.71  ? 143 LYS B N   1 
ATOM   2558 C CA  . LYS B 1 143 ? -26.805 3.472   46.646  1.00 74.94  ? 143 LYS B CA  1 
ATOM   2559 C C   . LYS B 1 143 ? -26.300 3.143   45.250  1.00 69.25  ? 143 LYS B C   1 
ATOM   2560 O O   . LYS B 1 143 ? -26.350 3.975   44.342  1.00 71.53  ? 143 LYS B O   1 
ATOM   2561 C CB  . LYS B 1 143 ? -28.230 2.947   46.851  1.00 77.70  ? 143 LYS B CB  1 
ATOM   2562 C CG  . LYS B 1 143 ? -28.272 1.442   47.212  1.00 86.11  ? 143 LYS B CG  1 
ATOM   2563 C CD  . LYS B 1 143 ? -26.929 0.961   47.814  1.00 83.14  ? 143 LYS B CD  1 
ATOM   2564 C CE  . LYS B 1 143 ? -26.987 -0.460  48.358  1.00 86.83  ? 143 LYS B CE  1 
ATOM   2565 N NZ  . LYS B 1 143 ? -27.873 -0.580  49.557  1.00 78.46  ? 143 LYS B NZ  1 
ATOM   2566 N N   . ASN B 1 144 ? -25.789 1.914   45.101  1.00 72.64  ? 144 ASN B N   1 
ATOM   2567 C CA  . ASN B 1 144 ? -25.221 1.428   43.848  1.00 71.52  ? 144 ASN B CA  1 
ATOM   2568 C C   . ASN B 1 144 ? -26.066 1.808   42.641  1.00 69.95  ? 144 ASN B C   1 
ATOM   2569 O O   . ASN B 1 144 ? -25.564 2.406   41.686  1.00 71.21  ? 144 ASN B O   1 
ATOM   2570 C CB  . ASN B 1 144 ? -25.046 -0.093  43.921  1.00 74.88  ? 144 ASN B CB  1 
ATOM   2571 C CG  . ASN B 1 144 ? -23.678 -0.544  43.465  1.00 85.26  ? 144 ASN B CG  1 
ATOM   2572 O OD1 . ASN B 1 144 ? -22.831 0.272   43.095  1.00 89.69  ? 144 ASN B OD1 1 
ATOM   2573 N ND2 . ASN B 1 144 ? -23.453 -1.854  43.481  1.00 87.84  ? 144 ASN B ND2 1 
ATOM   2574 N N   . GLU B 1 145 ? -27.354 1.448   42.670  1.00 68.15  ? 145 GLU B N   1 
ATOM   2575 C CA  . GLU B 1 145 ? -28.225 1.686   41.522  1.00 75.48  ? 145 GLU B CA  1 
ATOM   2576 C C   . GLU B 1 145 ? -28.220 3.147   41.089  1.00 71.21  ? 145 GLU B C   1 
ATOM   2577 O O   . GLU B 1 145 ? -28.239 3.442   39.887  1.00 70.75  ? 145 GLU B O   1 
ATOM   2578 C CB  . GLU B 1 145 ? -29.654 1.208   41.816  1.00 74.43  ? 145 GLU B CB  1 
ATOM   2579 C CG  . GLU B 1 145 ? -29.903 -0.307  41.600  1.00 82.96  ? 145 GLU B CG  1 
ATOM   2580 C CD  . GLU B 1 145 ? -29.061 -0.956  40.478  1.00 96.33  ? 145 GLU B CD  1 
ATOM   2581 O OE1 . GLU B 1 145 ? -28.799 -0.319  39.428  1.00 92.05  ? 145 GLU B OE1 1 
ATOM   2582 O OE2 . GLU B 1 145 ? -28.733 -2.155  40.611  1.00 96.06  ? 145 GLU B OE2 1 
ATOM   2583 N N   . GLU B 1 146 ? -28.184 4.079   42.046  1.00 69.64  ? 146 GLU B N   1 
ATOM   2584 C CA  . GLU B 1 146 ? -28.115 5.487   41.668  1.00 70.76  ? 146 GLU B CA  1 
ATOM   2585 C C   . GLU B 1 146 ? -26.765 5.804   41.040  1.00 67.27  ? 146 GLU B C   1 
ATOM   2586 O O   . GLU B 1 146 ? -26.693 6.440   39.981  1.00 65.65  ? 146 GLU B O   1 
ATOM   2587 C CB  . GLU B 1 146 ? -28.372 6.390   42.876  1.00 69.81  ? 146 GLU B CB  1 
ATOM   2588 C CG  . GLU B 1 146 ? -28.271 7.884   42.551  1.00 72.30  ? 146 GLU B CG  1 
ATOM   2589 C CD  . GLU B 1 146 ? -29.291 8.366   41.510  1.00 86.88  ? 146 GLU B CD  1 
ATOM   2590 O OE1 . GLU B 1 146 ? -30.315 7.675   41.274  1.00 85.49  ? 146 GLU B OE1 1 
ATOM   2591 O OE2 . GLU B 1 146 ? -29.049 9.431   40.901  1.00 85.49  ? 146 GLU B OE2 1 
ATOM   2592 N N   . LEU B 1 147 ? -25.680 5.347   41.671  1.00 68.02  ? 147 LEU B N   1 
ATOM   2593 C CA  . LEU B 1 147 ? -24.353 5.559   41.104  1.00 63.58  ? 147 LEU B CA  1 
ATOM   2594 C C   . LEU B 1 147 ? -24.236 4.927   39.720  1.00 65.32  ? 147 LEU B C   1 
ATOM   2595 O O   . LEU B 1 147 ? -23.686 5.537   38.794  1.00 61.78  ? 147 LEU B O   1 
ATOM   2596 C CB  . LEU B 1 147 ? -23.293 5.002   42.052  1.00 61.29  ? 147 LEU B CB  1 
ATOM   2597 C CG  . LEU B 1 147 ? -21.863 5.078   41.523  1.00 57.81  ? 147 LEU B CG  1 
ATOM   2598 C CD1 . LEU B 1 147 ? -21.436 6.533   41.394  1.00 56.28  ? 147 LEU B CD1 1 
ATOM   2599 C CD2 . LEU B 1 147 ? -20.910 4.303   42.431  1.00 55.31  ? 147 LEU B CD2 1 
ATOM   2600 N N   . LYS B 1 148 ? -24.754 3.702   39.563  1.00 67.90  ? 148 LYS B N   1 
ATOM   2601 C CA  . LYS B 1 148 ? -24.682 3.020   38.274  1.00 69.21  ? 148 LYS B CA  1 
ATOM   2602 C C   . LYS B 1 148 ? -25.456 3.791   37.211  1.00 65.33  ? 148 LYS B C   1 
ATOM   2603 O O   . LYS B 1 148 ? -25.040 3.855   36.049  1.00 59.81  ? 148 LYS B O   1 
ATOM   2604 C CB  . LYS B 1 148 ? -25.223 1.598   38.413  1.00 70.41  ? 148 LYS B CB  1 
ATOM   2605 C CG  . LYS B 1 148 ? -24.196 0.575   38.879  1.00 70.79  ? 148 LYS B CG  1 
ATOM   2606 C CD  . LYS B 1 148 ? -24.872 -0.540  39.666  1.00 82.62  ? 148 LYS B CD  1 
ATOM   2607 C CE  . LYS B 1 148 ? -25.837 -1.336  38.801  1.00 82.92  ? 148 LYS B CE  1 
ATOM   2608 N NZ  . LYS B 1 148 ? -25.193 -1.835  37.552  1.00 91.90  ? 148 LYS B NZ  1 
ATOM   2609 N N   . LYS B 1 149 ? -26.577 4.398   37.605  1.00 67.74  ? 149 LYS B N   1 
ATOM   2610 C CA  . LYS B 1 149 ? -27.309 5.269   36.693  1.00 65.94  ? 149 LYS B CA  1 
ATOM   2611 C C   . LYS B 1 149 ? -26.478 6.499   36.324  1.00 63.53  ? 149 LYS B C   1 
ATOM   2612 O O   . LYS B 1 149 ? -26.396 6.870   35.146  1.00 63.66  ? 149 LYS B O   1 
ATOM   2613 C CB  . LYS B 1 149 ? -28.653 5.647   37.327  1.00 62.72  ? 149 LYS B CB  1 
ATOM   2614 C CG  . LYS B 1 149 ? -29.468 6.653   36.545  1.00 64.71  ? 149 LYS B CG  1 
ATOM   2615 C CD  . LYS B 1 149 ? -30.488 7.381   37.415  1.00 67.89  ? 149 LYS B CD  1 
ATOM   2616 C CE  . LYS B 1 149 ? -31.391 6.413   38.167  1.00 70.15  ? 149 LYS B CE  1 
ATOM   2617 N NZ  . LYS B 1 149 ? -32.565 7.101   38.803  1.00 73.81  ? 149 LYS B NZ  1 
ATOM   2618 N N   . LEU B 1 150 ? -25.829 7.123   37.314  1.00 57.88  ? 150 LEU B N   1 
ATOM   2619 C CA  . LEU B 1 150 ? -24.996 8.293   37.042  1.00 58.44  ? 150 LEU B CA  1 
ATOM   2620 C C   . LEU B 1 150 ? -23.823 7.942   36.137  1.00 62.36  ? 150 LEU B C   1 
ATOM   2621 O O   . LEU B 1 150 ? -23.462 8.716   35.241  1.00 59.90  ? 150 LEU B O   1 
ATOM   2622 C CB  . LEU B 1 150 ? -24.483 8.888   38.355  1.00 63.39  ? 150 LEU B CB  1 
ATOM   2623 C CG  . LEU B 1 150 ? -25.501 9.559   39.289  1.00 65.60  ? 150 LEU B CG  1 
ATOM   2624 C CD1 . LEU B 1 150 ? -24.807 10.553  40.209  1.00 66.77  ? 150 LEU B CD1 1 
ATOM   2625 C CD2 . LEU B 1 150 ? -26.587 10.256  38.489  1.00 60.93  ? 150 LEU B CD2 1 
ATOM   2626 N N   . LEU B 1 151 ? -23.193 6.788   36.378  1.00 60.05  ? 151 LEU B N   1 
ATOM   2627 C CA  . LEU B 1 151 ? -22.043 6.387   35.574  1.00 55.55  ? 151 LEU B CA  1 
ATOM   2628 C C   . LEU B 1 151 ? -22.460 5.993   34.164  1.00 58.87  ? 151 LEU B C   1 
ATOM   2629 O O   . LEU B 1 151 ? -21.714 6.225   33.205  1.00 56.03  ? 151 LEU B O   1 
ATOM   2630 C CB  . LEU B 1 151 ? -21.314 5.238   36.260  1.00 57.84  ? 151 LEU B CB  1 
ATOM   2631 C CG  . LEU B 1 151 ? -20.722 5.667   37.604  1.00 52.21  ? 151 LEU B CG  1 
ATOM   2632 C CD1 . LEU B 1 151 ? -19.878 4.551   38.176  1.00 52.39  ? 151 LEU B CD1 1 
ATOM   2633 C CD2 . LEU B 1 151 ? -19.904 6.946   37.416  1.00 51.43  ? 151 LEU B CD2 1 
ATOM   2634 N N   . ARG B 1 152 ? -23.631 5.376   34.019  1.00 57.15  ? 152 ARG B N   1 
ATOM   2635 C CA  . ARG B 1 152 ? -24.115 5.044   32.684  1.00 66.19  ? 152 ARG B CA  1 
ATOM   2636 C C   . ARG B 1 152 ? -24.284 6.300   31.844  1.00 60.92  ? 152 ARG B C   1 
ATOM   2637 O O   . ARG B 1 152 ? -23.929 6.312   30.660  1.00 60.84  ? 152 ARG B O   1 
ATOM   2638 C CB  . ARG B 1 152 ? -25.448 4.293   32.754  1.00 68.48  ? 152 ARG B CB  1 
ATOM   2639 C CG  . ARG B 1 152 ? -25.350 2.781   32.668  1.00 66.22  ? 152 ARG B CG  1 
ATOM   2640 C CD  . ARG B 1 152 ? -26.692 2.145   33.015  1.00 77.90  ? 152 ARG B CD  1 
ATOM   2641 N NE  . ARG B 1 152 ? -26.591 1.179   34.102  1.00 83.72  ? 152 ARG B NE  1 
ATOM   2642 C CZ  . ARG B 1 152 ? -27.491 1.044   35.067  1.00 80.44  ? 152 ARG B CZ  1 
ATOM   2643 N NH1 . ARG B 1 152 ? -28.601 1.766   35.083  1.00 69.56  ? 152 ARG B NH1 1 
ATOM   2644 N NH2 . ARG B 1 152 ? -27.275 0.159   36.038  1.00 85.02  ? 152 ARG B NH2 1 
ATOM   2645 N N   . GLU B 1 153 ? -24.807 7.373   32.445  1.00 61.32  ? 153 GLU B N   1 
ATOM   2646 C CA  . GLU B 1 153 ? -25.042 8.599   31.691  1.00 57.32  ? 153 GLU B CA  1 
ATOM   2647 C C   . GLU B 1 153 ? -23.734 9.273   31.303  1.00 61.58  ? 153 GLU B C   1 
ATOM   2648 O O   . GLU B 1 153 ? -23.577 9.726   30.163  1.00 60.81  ? 153 GLU B O   1 
ATOM   2649 C CB  . GLU B 1 153 ? -25.914 9.553   32.507  1.00 66.81  ? 153 GLU B CB  1 
ATOM   2650 C CG  . GLU B 1 153 ? -26.895 10.333  31.669  1.00 74.29  ? 153 GLU B CG  1 
ATOM   2651 C CD  . GLU B 1 153 ? -27.955 9.445   31.061  1.00 82.93  ? 153 GLU B CD  1 
ATOM   2652 O OE1 . GLU B 1 153 ? -28.719 8.823   31.830  1.00 91.60  ? 153 GLU B OE1 1 
ATOM   2653 O OE2 . GLU B 1 153 ? -27.991 9.339   29.815  1.00 82.58  ? 153 GLU B OE2 1 
ATOM   2654 N N   . TYR B 1 154 ? -22.775 9.330   32.228  1.00 58.58  ? 154 TYR B N   1 
ATOM   2655 C CA  . TYR B 1 154 ? -21.476 9.911   31.902  1.00 53.25  ? 154 TYR B CA  1 
ATOM   2656 C C   . TYR B 1 154 ? -20.806 9.184   30.739  1.00 57.06  ? 154 TYR B C   1 
ATOM   2657 O O   . TYR B 1 154 ? -20.251 9.822   29.837  1.00 55.57  ? 154 TYR B O   1 
ATOM   2658 C CB  . TYR B 1 154 ? -20.568 9.894   33.126  1.00 53.35  ? 154 TYR B CB  1 
ATOM   2659 C CG  . TYR B 1 154 ? -19.131 10.213  32.787  1.00 50.99  ? 154 TYR B CG  1 
ATOM   2660 C CD1 . TYR B 1 154 ? -18.759 11.494  32.401  1.00 49.61  ? 154 TYR B CD1 1 
ATOM   2661 C CD2 . TYR B 1 154 ? -18.153 9.221   32.810  1.00 48.93  ? 154 TYR B CD2 1 
ATOM   2662 C CE1 . TYR B 1 154 ? -17.452 11.787  32.069  1.00 47.14  ? 154 TYR B CE1 1 
ATOM   2663 C CE2 . TYR B 1 154 ? -16.849 9.503   32.478  1.00 44.58  ? 154 TYR B CE2 1 
ATOM   2664 C CZ  . TYR B 1 154 ? -16.498 10.783  32.106  1.00 47.06  ? 154 TYR B CZ  1 
ATOM   2665 O OH  . TYR B 1 154 ? -15.189 11.059  31.787  1.00 44.33  ? 154 TYR B OH  1 
ATOM   2666 N N   . LYS B 1 155 ? -20.814 7.847   30.760  1.00 54.38  ? 155 LYS B N   1 
ATOM   2667 C CA  . LYS B 1 155 ? -20.155 7.087   29.702  1.00 50.93  ? 155 LYS B CA  1 
ATOM   2668 C C   . LYS B 1 155 ? -20.834 7.307   28.352  1.00 64.24  ? 155 LYS B C   1 
ATOM   2669 O O   . LYS B 1 155 ? -20.160 7.278   27.310  1.00 56.91  ? 155 LYS B O   1 
ATOM   2670 C CB  . LYS B 1 155 ? -20.123 5.601   30.060  1.00 52.80  ? 155 LYS B CB  1 
ATOM   2671 C CG  . LYS B 1 155 ? -18.938 5.197   30.926  1.00 54.13  ? 155 LYS B CG  1 
ATOM   2672 C CD  . LYS B 1 155 ? -17.619 5.716   30.354  1.00 64.15  ? 155 LYS B CD  1 
ATOM   2673 C CE  . LYS B 1 155 ? -16.615 4.592   30.144  1.00 56.33  ? 155 LYS B CE  1 
ATOM   2674 N NZ  . LYS B 1 155 ? -16.367 3.867   31.441  1.00 57.77  ? 155 LYS B NZ  1 
ATOM   2675 N N   . LYS B 1 156 ? -22.161 7.507   28.347  1.00 54.21  ? 156 LYS B N   1 
ATOM   2676 C CA  . LYS B 1 156 ? -22.869 7.786   27.096  1.00 61.75  ? 156 LYS B CA  1 
ATOM   2677 C C   . LYS B 1 156 ? -22.437 9.119   26.494  1.00 63.95  ? 156 LYS B C   1 
ATOM   2678 O O   . LYS B 1 156 ? -22.025 9.178   25.328  1.00 65.94  ? 156 LYS B O   1 
ATOM   2679 C CB  . LYS B 1 156 ? -24.385 7.767   27.303  1.00 61.87  ? 156 LYS B CB  1 
ATOM   2680 C CG  . LYS B 1 156 ? -25.055 6.544   26.693  1.00 68.83  ? 156 LYS B CG  1 
ATOM   2681 C CD  . LYS B 1 156 ? -26.555 6.747   26.489  1.00 74.21  ? 156 LYS B CD  1 
ATOM   2682 C CE  . LYS B 1 156 ? -27.320 6.760   27.806  1.00 76.20  ? 156 LYS B CE  1 
ATOM   2683 N NZ  . LYS B 1 156 ? -28.583 5.971   27.708  1.00 71.85  ? 156 LYS B NZ  1 
ATOM   2684 N N   . GLY B 1 157 ? -22.547 10.203  27.262  1.00 63.20  ? 157 GLY B N   1 
ATOM   2685 C CA  . GLY B 1 157 ? -22.197 11.517  26.758  1.00 61.83  ? 157 GLY B CA  1 
ATOM   2686 C C   . GLY B 1 157 ? -20.703 11.728  26.631  1.00 62.17  ? 157 GLY B C   1 
ATOM   2687 O O   . GLY B 1 157 ? -20.207 12.091  25.559  1.00 60.22  ? 157 GLY B O   1 
ATOM   2688 N N   . PHE B 1 158 ? -19.985 11.535  27.739  1.00 53.91  ? 158 PHE B N   1 
ATOM   2689 C CA  . PHE B 1 158 ? -18.523 11.554  27.773  1.00 56.02  ? 158 PHE B CA  1 
ATOM   2690 C C   . PHE B 1 158 ? -17.935 12.858  27.247  1.00 58.02  ? 158 PHE B C   1 
ATOM   2691 O O   . PHE B 1 158 ? -16.803 12.888  26.768  1.00 66.44  ? 158 PHE B O   1 
ATOM   2692 C CB  . PHE B 1 158 ? -17.927 10.355  27.027  1.00 51.44  ? 158 PHE B CB  1 
ATOM   2693 C CG  . PHE B 1 158 ? -16.556 9.959   27.525  1.00 53.56  ? 158 PHE B CG  1 
ATOM   2694 C CD1 . PHE B 1 158 ? -16.413 9.270   28.722  1.00 53.18  ? 158 PHE B CD1 1 
ATOM   2695 C CD2 . PHE B 1 158 ? -15.414 10.254  26.783  1.00 55.82  ? 158 PHE B CD2 1 
ATOM   2696 C CE1 . PHE B 1 158 ? -15.159 8.899   29.185  1.00 48.82  ? 158 PHE B CE1 1 
ATOM   2697 C CE2 . PHE B 1 158 ? -14.154 9.887   27.234  1.00 54.11  ? 158 PHE B CE2 1 
ATOM   2698 C CZ  . PHE B 1 158 ? -14.026 9.204   28.436  1.00 50.50  ? 158 PHE B CZ  1 
ATOM   2699 N N   . ASP B 1 159 ? -18.667 13.959  27.360  1.00 59.62  ? 159 ASP B N   1 
ATOM   2700 C CA  . ASP B 1 159 ? -18.106 15.273  27.083  1.00 56.56  ? 159 ASP B CA  1 
ATOM   2701 C C   . ASP B 1 159 ? -18.084 16.085  28.375  1.00 62.50  ? 159 ASP B C   1 
ATOM   2702 O O   . ASP B 1 159 ? -18.517 15.615  29.440  1.00 60.22  ? 159 ASP B O   1 
ATOM   2703 C CB  . ASP B 1 159 ? -18.893 15.979  25.972  1.00 61.23  ? 159 ASP B CB  1 
ATOM   2704 C CG  . ASP B 1 159 ? -20.381 16.041  26.252  1.00 64.85  ? 159 ASP B CG  1 
ATOM   2705 O OD1 . ASP B 1 159 ? -20.799 15.803  27.409  1.00 59.69  ? 159 ASP B OD1 1 
ATOM   2706 O OD2 . ASP B 1 159 ? -21.143 16.339  25.299  1.00 74.45  ? 159 ASP B OD2 1 
ATOM   2707 N N   . ASP B 1 160 ? -17.552 17.309  28.281  1.00 58.34  ? 160 ASP B N   1 
ATOM   2708 C CA  . ASP B 1 160 ? -17.475 18.186  29.449  1.00 65.91  ? 160 ASP B CA  1 
ATOM   2709 C C   . ASP B 1 160 ? -18.830 18.319  30.141  1.00 66.87  ? 160 ASP B C   1 
ATOM   2710 O O   . ASP B 1 160 ? -18.916 18.271  31.376  1.00 62.85  ? 160 ASP B O   1 
ATOM   2711 C CB  . ASP B 1 160 ? -16.944 19.559  29.040  1.00 66.33  ? 160 ASP B CB  1 
ATOM   2712 C CG  . ASP B 1 160 ? -15.760 19.465  28.099  1.00 82.45  ? 160 ASP B CG  1 
ATOM   2713 O OD1 . ASP B 1 160 ? -15.849 18.712  27.104  1.00 83.59  ? 160 ASP B OD1 1 
ATOM   2714 O OD2 . ASP B 1 160 ? -14.741 20.141  28.351  1.00 99.41  ? 160 ASP B OD2 1 
ATOM   2715 N N   . GLU B 1 161 ? -19.899 18.494  29.360  1.00 66.05  ? 161 GLU B N   1 
ATOM   2716 C CA  . GLU B 1 161 ? -21.230 18.601  29.949  1.00 62.19  ? 161 GLU B CA  1 
ATOM   2717 C C   . GLU B 1 161 ? -21.589 17.360  30.746  1.00 59.77  ? 161 GLU B C   1 
ATOM   2718 O O   . GLU B 1 161 ? -22.021 17.456  31.901  1.00 65.52  ? 161 GLU B O   1 
ATOM   2719 C CB  . GLU B 1 161 ? -22.291 18.822  28.875  1.00 68.07  ? 161 GLU B CB  1 
ATOM   2720 C CG  . GLU B 1 161 ? -23.677 18.819  29.498  1.00 65.71  ? 161 GLU B CG  1 
ATOM   2721 C CD  . GLU B 1 161 ? -24.547 19.937  29.028  1.00 73.43  ? 161 GLU B CD  1 
ATOM   2722 O OE1 . GLU B 1 161 ? -24.142 21.109  29.186  1.00 81.64  ? 161 GLU B OE1 1 
ATOM   2723 O OE2 . GLU B 1 161 ? -25.658 19.639  28.540  1.00 75.40  ? 161 GLU B OE2 1 
ATOM   2724 N N   . SER B 1 162 ? -21.467 16.185  30.125  1.00 53.73  ? 162 SER B N   1 
ATOM   2725 C CA  . SER B 1 162 ? -21.719 14.955  30.861  1.00 62.05  ? 162 SER B CA  1 
ATOM   2726 C C   . SER B 1 162 ? -20.878 14.913  32.128  1.00 58.81  ? 162 SER B C   1 
ATOM   2727 O O   . SER B 1 162 ? -21.370 14.525  33.196  1.00 57.02  ? 162 SER B O   1 
ATOM   2728 C CB  . SER B 1 162 ? -21.425 13.740  29.979  1.00 64.38  ? 162 SER B CB  1 
ATOM   2729 O OG  . SER B 1 162 ? -22.599 13.278  29.342  1.00 64.63  ? 162 SER B OG  1 
ATOM   2730 N N   . TYR B 1 163 ? -19.623 15.370  32.036  1.00 60.61  ? 163 TYR B N   1 
ATOM   2731 C CA  . TYR B 1 163 ? -18.729 15.341  33.190  1.00 57.73  ? 163 TYR B CA  1 
ATOM   2732 C C   . TYR B 1 163 ? -19.214 16.282  34.288  1.00 59.74  ? 163 TYR B C   1 
ATOM   2733 O O   . TYR B 1 163 ? -19.260 15.900  35.462  1.00 60.29  ? 163 TYR B O   1 
ATOM   2734 C CB  . TYR B 1 163 ? -17.298 15.710  32.791  1.00 50.35  ? 163 TYR B CB  1 
ATOM   2735 C CG  . TYR B 1 163 ? -16.418 15.867  34.015  1.00 54.42  ? 163 TYR B CG  1 
ATOM   2736 C CD1 . TYR B 1 163 ? -16.249 14.803  34.896  1.00 46.28  ? 163 TYR B CD1 1 
ATOM   2737 C CD2 . TYR B 1 163 ? -15.816 17.086  34.333  1.00 57.56  ? 163 TYR B CD2 1 
ATOM   2738 C CE1 . TYR B 1 163 ? -15.482 14.929  36.044  1.00 48.61  ? 163 TYR B CE1 1 
ATOM   2739 C CE2 . TYR B 1 163 ? -15.050 17.227  35.484  1.00 55.83  ? 163 TYR B CE2 1 
ATOM   2740 C CZ  . TYR B 1 163 ? -14.886 16.142  36.339  1.00 53.69  ? 163 TYR B CZ  1 
ATOM   2741 O OH  . TYR B 1 163 ? -14.128 16.253  37.490  1.00 47.34  ? 163 TYR B OH  1 
ATOM   2742 N N   . ARG B 1 164 ? -19.548 17.529  33.931  1.00 65.91  ? 164 ARG B N   1 
ATOM   2743 C CA  . ARG B 1 164 ? -20.006 18.484  34.947  1.00 70.53  ? 164 ARG B CA  1 
ATOM   2744 C C   . ARG B 1 164 ? -21.241 17.966  35.675  1.00 61.02  ? 164 ARG B C   1 
ATOM   2745 O O   . ARG B 1 164 ? -21.337 18.082  36.905  1.00 63.14  ? 164 ARG B O   1 
ATOM   2746 C CB  . ARG B 1 164 ? -20.289 19.854  34.322  1.00 66.10  ? 164 ARG B CB  1 
ATOM   2747 C CG  . ARG B 1 164 ? -19.060 20.500  33.698  1.00 81.31  ? 164 ARG B CG  1 
ATOM   2748 C CD  . ARG B 1 164 ? -17.915 20.596  34.707  1.00 87.78  ? 164 ARG B CD  1 
ATOM   2749 N NE  . ARG B 1 164 ? -16.672 21.042  34.083  1.00 107.26 ? 164 ARG B NE  1 
ATOM   2750 C CZ  . ARG B 1 164 ? -15.638 21.558  34.736  1.00 109.17 ? 164 ARG B CZ  1 
ATOM   2751 N NH1 . ARG B 1 164 ? -15.663 21.730  36.049  1.00 102.00 ? 164 ARG B NH1 1 
ATOM   2752 N NH2 . ARG B 1 164 ? -14.545 21.900  34.055  1.00 106.79 ? 164 ARG B NH2 1 
ATOM   2753 N N   . GLU B 1 165 ? -22.187 17.377  34.937  1.00 62.91  ? 165 GLU B N   1 
ATOM   2754 C CA  . GLU B 1 165 ? -23.358 16.782  35.574  1.00 64.96  ? 165 GLU B CA  1 
ATOM   2755 C C   . GLU B 1 165 ? -22.948 15.701  36.565  1.00 70.85  ? 165 GLU B C   1 
ATOM   2756 O O   . GLU B 1 165 ? -23.432 15.672  37.704  1.00 68.44  ? 165 GLU B O   1 
ATOM   2757 C CB  . GLU B 1 165 ? -24.302 16.213  34.517  1.00 68.58  ? 165 GLU B CB  1 
ATOM   2758 C CG  . GLU B 1 165 ? -25.688 15.894  35.042  1.00 83.43  ? 165 GLU B CG  1 
ATOM   2759 C CD  . GLU B 1 165 ? -26.381 17.093  35.670  1.00 96.15  ? 165 GLU B CD  1 
ATOM   2760 O OE1 . GLU B 1 165 ? -26.834 17.985  34.919  1.00 110.08 ? 165 GLU B OE1 1 
ATOM   2761 O OE2 . GLU B 1 165 ? -26.472 17.145  36.917  1.00 83.44  ? 165 GLU B OE2 1 
ATOM   2762 N N   . LEU B 1 166 ? -22.054 14.800  36.144  1.00 63.71  ? 166 LEU B N   1 
ATOM   2763 C CA  . LEU B 1 166 ? -21.534 13.790  37.058  1.00 58.64  ? 166 LEU B CA  1 
ATOM   2764 C C   . LEU B 1 166 ? -20.864 14.438  38.265  1.00 58.90  ? 166 LEU B C   1 
ATOM   2765 O O   . LEU B 1 166 ? -21.114 14.052  39.412  1.00 62.45  ? 166 LEU B O   1 
ATOM   2766 C CB  . LEU B 1 166 ? -20.537 12.891  36.325  1.00 56.04  ? 166 LEU B CB  1 
ATOM   2767 C CG  . LEU B 1 166 ? -20.078 11.647  37.090  1.00 53.21  ? 166 LEU B CG  1 
ATOM   2768 C CD1 . LEU B 1 166 ? -21.247 10.968  37.782  1.00 54.61  ? 166 LEU B CD1 1 
ATOM   2769 C CD2 . LEU B 1 166 ? -19.319 10.683  36.203  1.00 51.46  ? 166 LEU B CD2 1 
ATOM   2770 N N   . ARG B 1 167 ? -20.010 15.435  38.014  1.00 58.74  ? 167 ARG B N   1 
ATOM   2771 C CA  . ARG B 1 167 ? -19.210 16.059  39.064  1.00 52.70  ? 167 ARG B CA  1 
ATOM   2772 C C   . ARG B 1 167 ? -20.088 16.677  40.143  1.00 65.12  ? 167 ARG B C   1 
ATOM   2773 O O   . ARG B 1 167 ? -19.966 16.350  41.331  1.00 62.45  ? 167 ARG B O   1 
ATOM   2774 C CB  . ARG B 1 167 ? -18.299 17.113  38.433  1.00 54.46  ? 167 ARG B CB  1 
ATOM   2775 C CG  . ARG B 1 167 ? -17.234 17.685  39.351  1.00 56.33  ? 167 ARG B CG  1 
ATOM   2776 C CD  . ARG B 1 167 ? -16.490 18.810  38.639  1.00 59.76  ? 167 ARG B CD  1 
ATOM   2777 N NE  . ARG B 1 167 ? -15.197 19.119  39.242  1.00 58.10  ? 167 ARG B NE  1 
ATOM   2778 C CZ  . ARG B 1 167 ? -15.026 19.738  40.402  1.00 60.92  ? 167 ARG B CZ  1 
ATOM   2779 N NH1 . ARG B 1 167 ? -16.055 20.149  41.131  1.00 56.09  ? 167 ARG B NH1 1 
ATOM   2780 N NH2 . ARG B 1 167 ? -13.792 19.961  40.840  1.00 54.41  ? 167 ARG B NH2 1 
ATOM   2781 N N   . THR B 1 168 ? -20.998 17.566  39.744  1.00 65.57  ? 168 THR B N   1 
ATOM   2782 C CA  . THR B 1 168 ? -21.891 18.178  40.723  1.00 63.00  ? 168 THR B CA  1 
ATOM   2783 C C   . THR B 1 168 ? -22.766 17.128  41.401  1.00 65.54  ? 168 THR B C   1 
ATOM   2784 O O   . THR B 1 168 ? -22.963 17.166  42.621  1.00 68.97  ? 168 THR B O   1 
ATOM   2785 C CB  . THR B 1 168 ? -22.753 19.251  40.051  1.00 74.54  ? 168 THR B CB  1 
ATOM   2786 O OG1 . THR B 1 168 ? -23.643 18.629  39.118  1.00 77.35  ? 168 THR B OG1 1 
ATOM   2787 C CG2 . THR B 1 168 ? -21.883 20.259  39.299  1.00 63.48  ? 168 THR B CG2 1 
ATOM   2788 N N   . GLN B 1 169 ? -23.286 16.168  40.635  1.00 61.05  ? 169 GLN B N   1 
ATOM   2789 C CA  . GLN B 1 169 ? -24.165 15.179  41.246  1.00 69.94  ? 169 GLN B CA  1 
ATOM   2790 C C   . GLN B 1 169 ? -23.431 14.229  42.184  1.00 71.68  ? 169 GLN B C   1 
ATOM   2791 O O   . GLN B 1 169 ? -24.063 13.667  43.086  1.00 74.50  ? 169 GLN B O   1 
ATOM   2792 C CB  . GLN B 1 169 ? -24.921 14.406  40.168  1.00 67.94  ? 169 GLN B CB  1 
ATOM   2793 C CG  . GLN B 1 169 ? -26.199 15.111  39.733  1.00 75.09  ? 169 GLN B CG  1 
ATOM   2794 C CD  . GLN B 1 169 ? -26.864 14.452  38.540  1.00 88.05  ? 169 GLN B CD  1 
ATOM   2795 O OE1 . GLN B 1 169 ? -26.284 13.579  37.887  1.00 83.59  ? 169 GLN B OE1 1 
ATOM   2796 N NE2 . GLN B 1 169 ? -28.100 14.858  38.255  1.00 97.85  ? 169 GLN B NE2 1 
ATOM   2797 N N   . ILE B 1 170 ? -22.114 14.077  42.046  1.00 61.97  ? 170 ILE B N   1 
ATOM   2798 C CA  . ILE B 1 170 ? -21.381 13.332  43.060  1.00 60.87  ? 170 ILE B CA  1 
ATOM   2799 C C   . ILE B 1 170 ? -21.149 14.200  44.290  1.00 66.32  ? 170 ILE B C   1 
ATOM   2800 O O   . ILE B 1 170 ? -21.410 13.781  45.423  1.00 72.40  ? 170 ILE B O   1 
ATOM   2801 C CB  . ILE B 1 170 ? -20.042 12.811  42.509  1.00 59.29  ? 170 ILE B CB  1 
ATOM   2802 C CG1 . ILE B 1 170 ? -20.254 11.668  41.509  1.00 50.12  ? 170 ILE B CG1 1 
ATOM   2803 C CG2 . ILE B 1 170 ? -19.162 12.377  43.667  1.00 51.08  ? 170 ILE B CG2 1 
ATOM   2804 C CD1 . ILE B 1 170 ? -19.041 11.438  40.592  1.00 47.09  ? 170 ILE B CD1 1 
ATOM   2805 N N   . LEU B 1 171 ? -20.681 15.435  44.080  1.00 64.82  ? 171 LEU B N   1 
ATOM   2806 C CA  . LEU B 1 171 ? -20.191 16.251  45.184  1.00 62.18  ? 171 LEU B CA  1 
ATOM   2807 C C   . LEU B 1 171 ? -21.326 16.765  46.061  1.00 70.45  ? 171 LEU B C   1 
ATOM   2808 O O   . LEU B 1 171 ? -21.087 17.140  47.216  1.00 78.01  ? 171 LEU B O   1 
ATOM   2809 C CB  . LEU B 1 171 ? -19.381 17.426  44.640  1.00 60.10  ? 171 LEU B CB  1 
ATOM   2810 C CG  . LEU B 1 171 ? -18.025 17.074  44.023  1.00 64.01  ? 171 LEU B CG  1 
ATOM   2811 C CD1 . LEU B 1 171 ? -17.219 18.326  43.700  1.00 63.00  ? 171 LEU B CD1 1 
ATOM   2812 C CD2 . LEU B 1 171 ? -17.237 16.146  44.927  1.00 59.27  ? 171 LEU B CD2 1 
ATOM   2813 N N   . GLN B 1 172 ? -22.551 16.791  45.541  1.00 67.06  ? 172 GLN B N   1 
ATOM   2814 C CA  . GLN B 1 172 ? -23.683 17.196  46.364  1.00 73.75  ? 172 GLN B CA  1 
ATOM   2815 C C   . GLN B 1 172 ? -23.814 16.326  47.607  1.00 80.38  ? 172 GLN B C   1 
ATOM   2816 O O   . GLN B 1 172 ? -24.206 16.817  48.671  1.00 86.64  ? 172 GLN B O   1 
ATOM   2817 C CB  . GLN B 1 172 ? -24.973 17.164  45.545  1.00 75.16  ? 172 GLN B CB  1 
ATOM   2818 C CG  . GLN B 1 172 ? -25.486 15.766  45.249  1.00 81.37  ? 172 GLN B CG  1 
ATOM   2819 C CD  . GLN B 1 172 ? -26.763 15.760  44.433  1.00 93.08  ? 172 GLN B CD  1 
ATOM   2820 O OE1 . GLN B 1 172 ? -27.440 16.784  44.302  1.00 97.42  ? 172 GLN B OE1 1 
ATOM   2821 N NE2 . GLN B 1 172 ? -27.073 14.614  43.835  1.00 88.71  ? 172 GLN B NE2 1 
ATOM   2822 N N   . TYR B 1 173 ? -23.497 15.031  47.499  1.00 78.16  ? 173 TYR B N   1 
ATOM   2823 C CA  . TYR B 1 173 ? -23.784 14.135  48.617  1.00 82.35  ? 173 TYR B CA  1 
ATOM   2824 C C   . TYR B 1 173 ? -22.911 14.359  49.853  1.00 79.71  ? 173 TYR B C   1 
ATOM   2825 O O   . TYR B 1 173 ? -23.136 13.684  50.864  1.00 83.43  ? 173 TYR B O   1 
ATOM   2826 C CB  . TYR B 1 173 ? -23.695 12.671  48.179  1.00 74.55  ? 173 TYR B CB  1 
ATOM   2827 C CG  . TYR B 1 173 ? -24.836 12.244  47.291  1.00 77.44  ? 173 TYR B CG  1 
ATOM   2828 C CD1 . TYR B 1 173 ? -24.800 12.456  45.919  1.00 79.59  ? 173 TYR B CD1 1 
ATOM   2829 C CD2 . TYR B 1 173 ? -26.002 11.738  47.847  1.00 80.31  ? 173 TYR B CD2 1 
ATOM   2830 C CE1 . TYR B 1 173 ? -25.866 12.080  45.114  1.00 82.23  ? 173 TYR B CE1 1 
ATOM   2831 C CE2 . TYR B 1 173 ? -27.074 11.374  47.063  1.00 81.90  ? 173 TYR B CE2 1 
ATOM   2832 C CZ  . TYR B 1 173 ? -27.008 11.549  45.699  1.00 90.85  ? 173 TYR B CZ  1 
ATOM   2833 O OH  . TYR B 1 173 ? -28.089 11.178  44.926  1.00 82.42  ? 173 TYR B OH  1 
ATOM   2834 N N   . MET B 1 174 ? -21.905 15.226  49.808  1.00 74.52  ? 174 MET B N   1 
ATOM   2835 C CA  . MET B 1 174 ? -21.115 15.473  51.022  1.00 86.00  ? 174 MET B CA  1 
ATOM   2836 C C   . MET B 1 174 ? -21.295 16.876  51.613  1.00 77.78  ? 174 MET B C   1 
ATOM   2837 O O   . MET B 1 174 ? -21.077 17.884  50.947  1.00 88.29  ? 174 MET B O   1 
ATOM   2838 C CB  . MET B 1 174 ? -19.638 15.163  50.767  1.00 85.25  ? 174 MET B CB  1 
ATOM   2839 C CG  . MET B 1 174 ? -19.403 14.358  49.507  1.00 74.12  ? 174 MET B CG  1 
ATOM   2840 S SD  . MET B 1 174 ? -17.679 14.151  49.064  1.00 72.92  ? 174 MET B SD  1 
ATOM   2841 C CE  . MET B 1 174 ? -17.413 15.754  48.397  1.00 69.33  ? 174 MET B CE  1 
HETATM 2842 C C1  . GOL C 2 .   ? -0.956  1.181   23.156  1.00 49.23  ? 201 GOL B C1  1 
HETATM 2843 O O1  . GOL C 2 .   ? -2.280  1.031   22.669  1.00 51.41  ? 201 GOL B O1  1 
HETATM 2844 C C2  . GOL C 2 .   ? -1.085  1.434   24.687  1.00 50.17  ? 201 GOL B C2  1 
HETATM 2845 O O2  . GOL C 2 .   ? -2.240  0.847   25.187  1.00 45.23  ? 201 GOL B O2  1 
HETATM 2846 C C3  . GOL C 2 .   ? 0.238   0.877   25.335  1.00 50.63  ? 201 GOL B C3  1 
HETATM 2847 O O3  . GOL C 2 .   ? 0.396   -0.464  24.942  1.00 67.29  ? 201 GOL B O3  1 
HETATM 2848 O O   . HOH D 3 .   ? 14.638  18.866  33.651  1.00 49.21  ? 201 HOH A O   1 
HETATM 2849 O O   . HOH D 3 .   ? 19.750  -2.875  20.965  1.00 46.02  ? 202 HOH A O   1 
HETATM 2850 O O   . HOH D 3 .   ? 12.355  8.163   16.638  1.00 33.38  ? 203 HOH A O   1 
HETATM 2851 O O   . HOH D 3 .   ? 5.666   11.621  11.847  1.00 46.18  ? 204 HOH A O   1 
HETATM 2852 O O   . HOH D 3 .   ? 17.207  -3.844  16.781  1.00 49.14  ? 205 HOH A O   1 
HETATM 2853 O O   . HOH D 3 .   ? 10.986  10.224  -3.512  1.00 65.90  ? 206 HOH A O   1 
HETATM 2854 O O   . HOH D 3 .   ? 13.867  -1.902  23.908  1.00 32.42  ? 207 HOH A O   1 
HETATM 2855 O O   . HOH D 3 .   ? -5.909  5.837   9.298   1.00 47.40  ? 208 HOH A O   1 
HETATM 2856 O O   . HOH D 3 .   ? 14.238  -1.741  16.628  1.00 38.10  ? 209 HOH A O   1 
HETATM 2857 O O   . HOH D 3 .   ? 4.660   -4.897  8.700   1.00 44.86  ? 210 HOH A O   1 
HETATM 2858 O O   . HOH D 3 .   ? 10.662  23.940  26.640  1.00 45.69  ? 211 HOH A O   1 
HETATM 2859 O O   . HOH D 3 .   ? -7.816  3.103   17.838  1.00 45.50  ? 212 HOH A O   1 
HETATM 2860 O O   . HOH D 3 .   ? 16.040  -0.849  24.861  1.00 33.31  ? 213 HOH A O   1 
HETATM 2861 O O   . HOH D 3 .   ? 8.325   22.894  25.024  1.00 44.59  ? 214 HOH A O   1 
HETATM 2862 O O   . HOH D 3 .   ? 6.482   -6.059  15.816  1.00 46.31  ? 215 HOH A O   1 
HETATM 2863 O O   . HOH D 3 .   ? 6.208   -0.880  25.102  1.00 29.57  ? 216 HOH A O   1 
HETATM 2864 O O   . HOH D 3 .   ? -0.692  10.224  11.628  1.00 44.18  ? 217 HOH A O   1 
HETATM 2865 O O   . HOH D 3 .   ? 9.684   12.847  6.101   1.00 51.35  ? 218 HOH A O   1 
HETATM 2866 O O   . HOH D 3 .   ? 20.079  4.857   7.694   1.00 49.21  ? 219 HOH A O   1 
HETATM 2867 O O   . HOH D 3 .   ? 13.600  19.089  31.203  1.00 33.55  ? 220 HOH A O   1 
HETATM 2868 O O   . HOH D 3 .   ? 17.594  7.395   31.091  1.00 24.97  ? 221 HOH A O   1 
HETATM 2869 O O   . HOH D 3 .   ? 14.278  23.357  28.183  1.00 33.25  ? 222 HOH A O   1 
HETATM 2870 O O   . HOH D 3 .   ? 14.512  16.276  35.285  1.00 46.86  ? 223 HOH A O   1 
HETATM 2871 O O   . HOH D 3 .   ? 5.690   12.383  15.236  1.00 35.50  ? 224 HOH A O   1 
HETATM 2872 O O   . HOH D 3 .   ? 10.734  18.319  31.638  1.00 34.71  ? 225 HOH A O   1 
HETATM 2873 O O   . HOH D 3 .   ? 18.430  6.109   12.950  1.00 42.24  ? 226 HOH A O   1 
HETATM 2874 O O   . HOH D 3 .   ? 16.947  6.078   15.052  1.00 44.17  ? 227 HOH A O   1 
HETATM 2875 O O   . HOH D 3 .   ? 19.290  16.035  12.667  1.00 50.78  ? 228 HOH A O   1 
HETATM 2876 O O   . HOH D 3 .   ? 15.322  -0.329  8.342   1.00 48.36  ? 229 HOH A O   1 
HETATM 2877 O O   . HOH D 3 .   ? 3.206   15.701  20.400  1.00 51.92  ? 230 HOH A O   1 
HETATM 2878 O O   . HOH D 3 .   ? 0.058   13.087  25.011  1.00 40.56  ? 231 HOH A O   1 
HETATM 2879 O O   . HOH D 3 .   ? 15.227  26.343  21.627  1.00 40.23  ? 232 HOH A O   1 
HETATM 2880 O O   . HOH D 3 .   ? 5.193   16.952  26.857  1.00 42.28  ? 233 HOH A O   1 
HETATM 2881 O O   . HOH D 3 .   ? 19.917  10.286  26.942  1.00 37.27  ? 234 HOH A O   1 
HETATM 2882 O O   . HOH D 3 .   ? 6.825   2.975   -9.315  1.00 72.24  ? 235 HOH A O   1 
HETATM 2883 O O   . HOH D 3 .   ? 10.405  26.338  27.254  1.00 50.85  ? 236 HOH A O   1 
HETATM 2884 O O   . HOH D 3 .   ? -7.589  3.273   20.876  1.00 45.35  ? 237 HOH A O   1 
HETATM 2885 O O   . HOH E 3 .   ? 9.215   16.996  44.892  1.00 46.89  ? 301 HOH B O   1 
HETATM 2886 O O   . HOH E 3 .   ? 4.505   6.298   38.990  1.00 33.31  ? 302 HOH B O   1 
HETATM 2887 O O   . HOH E 3 .   ? 2.807   -7.779  32.115  1.00 44.02  ? 303 HOH B O   1 
HETATM 2888 O O   . HOH E 3 .   ? 12.520  -1.015  48.590  1.00 53.18  ? 304 HOH B O   1 
HETATM 2889 O O   . HOH E 3 .   ? -9.287  3.965   53.743  1.00 54.74  ? 305 HOH B O   1 
HETATM 2890 O O   . HOH E 3 .   ? 12.907  14.835  43.352  1.00 33.25  ? 306 HOH B O   1 
HETATM 2891 O O   . HOH E 3 .   ? 18.498  3.694   37.551  1.00 36.51  ? 307 HOH B O   1 
HETATM 2892 O O   . HOH E 3 .   ? -9.410  3.270   50.964  1.00 52.87  ? 308 HOH B O   1 
HETATM 2893 O O   . HOH E 3 .   ? 12.292  15.342  34.665  1.00 35.01  ? 309 HOH B O   1 
HETATM 2894 O O   . HOH E 3 .   ? -3.882  1.277   45.741  1.00 46.59  ? 310 HOH B O   1 
HETATM 2895 O O   . HOH E 3 .   ? -8.499  3.338   34.796  1.00 40.14  ? 311 HOH B O   1 
HETATM 2896 O O   . HOH E 3 .   ? -10.681 9.919   25.191  1.00 42.29  ? 312 HOH B O   1 
HETATM 2897 O O   . HOH E 3 .   ? -14.403 6.984   33.100  1.00 41.11  ? 313 HOH B O   1 
HETATM 2898 O O   . HOH E 3 .   ? 5.448   16.290  40.001  1.00 37.93  ? 314 HOH B O   1 
HETATM 2899 O O   . HOH E 3 .   ? 15.531  -2.872  43.334  1.00 35.59  ? 315 HOH B O   1 
HETATM 2900 O O   . HOH E 3 .   ? 15.308  -6.288  36.445  1.00 34.80  ? 316 HOH B O   1 
HETATM 2901 O O   . HOH E 3 .   ? 6.923   8.530   43.057  1.00 39.38  ? 317 HOH B O   1 
HETATM 2902 O O   . HOH E 3 .   ? 17.089  4.659   35.638  1.00 31.54  ? 318 HOH B O   1 
HETATM 2903 O O   . HOH E 3 .   ? 6.694   8.606   45.689  1.00 38.70  ? 319 HOH B O   1 
HETATM 2904 O O   . HOH E 3 .   ? -4.545  2.593   41.346  1.00 45.98  ? 320 HOH B O   1 
HETATM 2905 O O   . HOH E 3 .   ? 6.857   -8.190  29.955  1.00 38.02  ? 321 HOH B O   1 
HETATM 2906 O O   . HOH E 3 .   ? 9.769   16.636  33.788  1.00 33.60  ? 322 HOH B O   1 
HETATM 2907 O O   . HOH E 3 .   ? -9.768  2.346   22.275  1.00 48.81  ? 323 HOH B O   1 
HETATM 2908 O O   . HOH E 3 .   ? 8.165   -1.542  46.799  1.00 47.05  ? 324 HOH B O   1 
HETATM 2909 O O   . HOH E 3 .   ? -1.197  1.616   36.062  1.00 31.94  ? 325 HOH B O   1 
HETATM 2910 O O   . HOH E 3 .   ? 12.836  -3.782  25.633  1.00 35.51  ? 326 HOH B O   1 
HETATM 2911 O O   . HOH E 3 .   ? 16.626  -6.692  33.975  1.00 41.47  ? 327 HOH B O   1 
HETATM 2912 O O   . HOH E 3 .   ? -9.896  8.396   56.364  1.00 55.57  ? 328 HOH B O   1 
HETATM 2913 O O   . HOH E 3 .   ? 14.109  -0.723  44.145  1.00 38.94  ? 329 HOH B O   1 
HETATM 2914 O O   . HOH E 3 .   ? 4.253   15.084  28.295  1.00 33.55  ? 330 HOH B O   1 
HETATM 2915 O O   . HOH E 3 .   ? -8.075  7.545   23.137  1.00 43.22  ? 331 HOH B O   1 
HETATM 2916 O O   . HOH E 3 .   ? -1.426  20.094  35.443  1.00 47.53  ? 332 HOH B O   1 
HETATM 2917 O O   . HOH E 3 .   ? 16.958  14.900  41.018  1.00 51.34  ? 333 HOH B O   1 
HETATM 2918 O O   . HOH E 3 .   ? 17.871  2.645   49.192  1.00 50.62  ? 334 HOH B O   1 
HETATM 2919 O O   . HOH E 3 .   ? 17.979  -2.027  44.974  1.00 49.65  ? 335 HOH B O   1 
HETATM 2920 O O   . HOH E 3 .   ? 5.266   18.829  39.430  1.00 49.56  ? 336 HOH B O   1 
HETATM 2921 O O   . HOH E 3 .   ? -8.661  10.083  23.244  1.00 45.16  ? 337 HOH B O   1 
HETATM 2922 O O   . HOH E 3 .   ? 5.987   18.996  28.653  1.00 44.87  ? 338 HOH B O   1 
HETATM 2923 O O   . HOH E 3 .   ? 11.653  16.821  44.973  1.00 49.30  ? 339 HOH B O   1 
HETATM 2924 O O   . HOH E 3 .   ? 17.426  -10.106 36.383  1.00 43.80  ? 340 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   . ARG A 4   ? 0.9168 0.6589 0.7282 -0.0398 0.0281  0.1471  4   ARG A N   
2    C CA  . ARG A 4   ? 0.9547 0.6483 0.7630 -0.0354 0.0234  0.1563  4   ARG A CA  
3    C C   . ARG A 4   ? 0.8713 0.5537 0.6999 -0.0273 0.0193  0.1368  4   ARG A C   
4    O O   . ARG A 4   ? 0.9522 0.5994 0.7840 -0.0321 0.0189  0.1362  4   ARG A O   
5    C CB  . ARG A 4   ? 0.9649 0.6400 0.7542 -0.0180 0.0154  0.1753  4   ARG A CB  
6    N N   . HIS A 5   ? 0.7900 0.5017 0.6308 -0.0159 0.0162  0.1211  5   HIS A N   
7    C CA  . HIS A 5   ? 0.7320 0.4373 0.5901 -0.0082 0.0125  0.1037  5   HIS A CA  
8    C C   . HIS A 5   ? 0.7224 0.4440 0.5990 -0.0226 0.0175  0.0878  5   HIS A C   
9    O O   . HIS A 5   ? 0.5898 0.3005 0.4785 -0.0205 0.0147  0.0758  5   HIS A O   
10   C CB  . HIS A 5   ? 0.7424 0.4704 0.6056 0.0102  0.0066  0.0957  5   HIS A CB  
11   C CG  . HIS A 5   ? 0.7781 0.4887 0.6296 0.0287  -0.0004 0.1078  5   HIS A CG  
12   N ND1 . HIS A 5   ? 0.9185 0.6004 0.7526 0.0295  -0.0012 0.1279  5   HIS A ND1 
13   C CD2 . HIS A 5   ? 0.8550 0.5748 0.7111 0.0475  -0.0067 0.1035  5   HIS A CD2 
14   C CE1 . HIS A 5   ? 0.9132 0.5864 0.7422 0.0499  -0.0084 0.1353  5   HIS A CE1 
15   N NE2 . HIS A 5   ? 0.9815 0.6794 0.8243 0.0610  -0.0116 0.1202  5   HIS A NE2 
16   N N   . SER A 6   ? 0.6134 0.3638 0.4930 -0.0357 0.0247  0.0868  6   SER A N   
17   C CA  . SER A 6   ? 0.5800 0.3533 0.4805 -0.0448 0.0287  0.0708  6   SER A CA  
18   C C   . SER A 6   ? 0.6932 0.4893 0.5942 -0.0618 0.0385  0.0741  6   SER A C   
19   O O   . SER A 6   ? 0.6668 0.4646 0.5500 -0.0663 0.0424  0.0881  6   SER A O   
20   C CB  . SER A 6   ? 0.5969 0.3966 0.5092 -0.0323 0.0256  0.0562  6   SER A CB  
21   O OG  . SER A 6   ? 0.6418 0.4658 0.5444 -0.0294 0.0280  0.0594  6   SER A OG  
22   N N   . VAL A 7   ? 0.5858 0.4012 0.5075 -0.0710 0.0427  0.0616  7   VAL A N   
23   C CA  . VAL A 7   ? 0.6406 0.4856 0.5687 -0.0855 0.0532  0.0607  7   VAL A CA  
24   C C   . VAL A 7   ? 0.6199 0.4977 0.5706 -0.0805 0.0549  0.0422  7   VAL A C   
25   O O   . VAL A 7   ? 0.5556 0.4296 0.5229 -0.0758 0.0493  0.0321  7   VAL A O   
26   C CB  . VAL A 7   ? 0.7174 0.5512 0.6508 -0.1052 0.0575  0.0667  7   VAL A CB  
27   C CG1 . VAL A 7   ? 0.7150 0.5874 0.6621 -0.1190 0.0689  0.0621  7   VAL A CG1 
28   C CG2 . VAL A 7   ? 0.7812 0.5818 0.6903 -0.1119 0.0577  0.0871  7   VAL A CG2 
29   N N   . VAL A 8   ? 0.6486 0.5577 0.5993 -0.0812 0.0627  0.0377  8   VAL A N   
30   C CA  . VAL A 8   ? 0.5878 0.5260 0.5601 -0.0760 0.0655  0.0202  8   VAL A CA  
31   C C   . VAL A 8   ? 0.6219 0.5863 0.6098 -0.0896 0.0763  0.0169  8   VAL A C   
32   O O   . VAL A 8   ? 0.6056 0.5810 0.5813 -0.1007 0.0854  0.0251  8   VAL A O   
33   C CB  . VAL A 8   ? 0.5830 0.5380 0.5461 -0.0658 0.0667  0.0134  8   VAL A CB  
34   C CG1 . VAL A 8   ? 0.5652 0.5460 0.5515 -0.0611 0.0707  -0.0050 8   VAL A CG1 
35   C CG2 . VAL A 8   ? 0.5474 0.4821 0.4990 -0.0523 0.0557  0.0159  8   VAL A CG2 
36   N N   . ARG A 9   ? 0.4986 0.4752 0.5135 -0.0890 0.0753  0.0057  9   ARG A N   
37   C CA  . ARG A 9   ? 0.5018 0.5104 0.5374 -0.0989 0.0854  0.0001  9   ARG A CA  
38   C C   . ARG A 9   ? 0.6020 0.6351 0.6600 -0.0861 0.0867  -0.0171 9   ARG A C   
39   O O   . ARG A 9   ? 0.5210 0.5422 0.5866 -0.0739 0.0773  -0.0232 9   ARG A O   
40   C CB  . ARG A 9   ? 0.6028 0.6051 0.6526 -0.1120 0.0826  0.0046  9   ARG A CB  
41   C CG  . ARG A 9   ? 0.5227 0.5153 0.5899 -0.1043 0.0711  -0.0029 9   ARG A CG  
42   C CD  . ARG A 9   ? 0.6672 0.6545 0.7450 -0.1203 0.0681  0.0013  9   ARG A CD  
43   N NE  . ARG A 9   ? 0.6140 0.5970 0.7080 -0.1142 0.0569  -0.0063 9   ARG A NE  
44   C CZ  . ARG A 9   ? 0.6792 0.6293 0.7608 -0.1091 0.0463  -0.0050 9   ARG A CZ  
45   N NH1 . ARG A 9   ? 0.5991 0.5165 0.6542 -0.1069 0.0448  0.0033  9   ARG A NH1 
46   N NH2 . ARG A 9   ? 0.6263 0.5781 0.7224 -0.1054 0.0370  -0.0119 9   ARG A NH2 
47   N N   . VAL A 10  ? 0.5248 0.5913 0.5931 -0.0886 0.0989  -0.0247 10  VAL A N   
48   C CA  . VAL A 10  ? 0.5363 0.6237 0.6242 -0.0752 0.1019  -0.0417 10  VAL A CA  
49   C C   . VAL A 10  ? 0.6596 0.7728 0.7816 -0.0773 0.1050  -0.0477 10  VAL A C   
50   O O   . VAL A 10  ? 0.6213 0.7590 0.7509 -0.0899 0.1151  -0.0451 10  VAL A O   
51   C CB  . VAL A 10  ? 0.6493 0.7563 0.7243 -0.0734 0.1137  -0.0493 10  VAL A CB  
52   C CG1 . VAL A 10  ? 0.5975 0.7208 0.6936 -0.0589 0.1167  -0.0686 10  VAL A CG1 
53   C CG2 . VAL A 10  ? 0.5725 0.6577 0.6140 -0.0720 0.1089  -0.0419 10  VAL A CG2 
54   N N   . GLU A 11  ? 0.6332 0.7427 0.7759 -0.0654 0.0961  -0.0548 11  GLU A N   
55   C CA  . GLU A 11  ? 0.6227 0.7567 0.7997 -0.0644 0.0958  -0.0597 11  GLU A CA  
56   C C   . GLU A 11  ? 0.6478 0.7924 0.8444 -0.0456 0.0964  -0.0739 11  GLU A C   
57   O O   . GLU A 11  ? 0.7141 0.8396 0.9144 -0.0345 0.0852  -0.0753 11  GLU A O   
58   C CB  . GLU A 11  ? 0.6697 0.7856 0.8511 -0.0692 0.0821  -0.0516 11  GLU A CB  
59   C CG  . GLU A 11  ? 0.7445 0.8383 0.9018 -0.0860 0.0806  -0.0384 11  GLU A CG  
60   C CD  . GLU A 11  ? 0.9796 1.0658 1.1464 -0.0963 0.0710  -0.0331 11  GLU A CD  
61   O OE1 . GLU A 11  ? 0.8873 0.9710 1.0679 -0.0872 0.0604  -0.0373 11  GLU A OE1 
62   O OE2 . GLU A 11  ? 0.8699 0.9521 1.0291 -0.1145 0.0739  -0.0244 11  GLU A OE2 
63   N N   . GLY A 12  ? 0.6562 0.8306 0.8652 -0.0423 0.1099  -0.0845 12  GLY A N   
64   C CA  . GLY A 12  ? 0.6028 0.7837 0.8291 -0.0239 0.1121  -0.0994 12  GLY A CA  
65   C C   . GLY A 12  ? 0.6007 0.7565 0.8012 -0.0174 0.1113  -0.1048 12  GLY A C   
66   O O   . GLY A 12  ? 0.6229 0.7766 0.7965 -0.0257 0.1176  -0.1031 12  GLY A O   
67   N N   . ASP A 13  ? 0.5498 0.6872 0.7578 -0.0034 0.1030  -0.1106 13  ASP A N   
68   C CA  . ASP A 13  ? 0.5871 0.7009 0.7726 0.0012  0.1008  -0.1158 13  ASP A CA  
69   C C   . ASP A 13  ? 0.5537 0.6379 0.7188 -0.0029 0.0875  -0.1028 13  ASP A C   
70   O O   . ASP A 13  ? 0.4503 0.5142 0.6039 0.0028  0.0819  -0.1057 13  ASP A O   
71   C CB  . ASP A 13  ? 0.5575 0.6653 0.7607 0.0173  0.1004  -0.1297 13  ASP A CB  
72   C CG  . ASP A 13  ? 0.6250 0.7250 0.8529 0.0263  0.0891  -0.1242 13  ASP A CG  
73   O OD1 . ASP A 13  ? 0.6424 0.7371 0.8687 0.0198  0.0795  -0.1104 13  ASP A OD1 
74   O OD2 . ASP A 13  ? 0.7313 0.8293 0.9793 0.0402  0.0896  -0.1337 13  ASP A OD2 
75   N N   . ARG A 14  ? 0.4582 0.5400 0.6198 -0.0126 0.0825  -0.0894 14  ARG A N   
76   C CA  . ARG A 14  ? 0.4891 0.5436 0.6321 -0.0159 0.0710  -0.0778 14  ARG A CA  
77   C C   . ARG A 14  ? 0.5276 0.5777 0.6462 -0.0289 0.0739  -0.0672 14  ARG A C   
78   O O   . ARG A 14  ? 0.5271 0.5945 0.6495 -0.0392 0.0815  -0.0638 14  ARG A O   
79   C CB  . ARG A 14  ? 0.5113 0.5601 0.6711 -0.0145 0.0605  -0.0720 14  ARG A CB  
80   C CG  . ARG A 14  ? 0.6464 0.6854 0.8180 -0.0010 0.0534  -0.0773 14  ARG A CG  
81   C CD  . ARG A 14  ? 0.6169 0.6649 0.8147 0.0037  0.0468  -0.0758 14  ARG A CD  
82   N NE  . ARG A 14  ? 0.6874 0.7301 0.8990 0.0178  0.0439  -0.0820 14  ARG A NE  
83   C CZ  . ARG A 14  ? 0.6936 0.7224 0.9093 0.0235  0.0326  -0.0767 14  ARG A CZ  
84   N NH1 . ARG A 14  ? 0.4871 0.5078 0.6941 0.0171  0.0234  -0.0670 14  ARG A NH1 
85   N NH2 . ARG A 14  ? 0.5860 0.6080 0.8141 0.0355  0.0309  -0.0812 14  ARG A NH2 
86   N N   . ALA A 15  ? 0.4519 0.4798 0.5464 -0.0282 0.0679  -0.0613 15  ALA A N   
87   C CA  . ALA A 15  ? 0.4965 0.5122 0.5672 -0.0378 0.0674  -0.0483 15  ALA A CA  
88   C C   . ALA A 15  ? 0.5072 0.4979 0.5753 -0.0376 0.0559  -0.0396 15  ALA A C   
89   O O   . ALA A 15  ? 0.4446 0.4228 0.5145 -0.0282 0.0477  -0.0423 15  ALA A O   
90   C CB  . ALA A 15  ? 0.4877 0.4990 0.5330 -0.0357 0.0686  -0.0476 15  ALA A CB  
91   N N   . ILE A 16  ? 0.4233 0.4071 0.4875 -0.0486 0.0558  -0.0299 16  ILE A N   
92   C CA  . ILE A 16  ? 0.4053 0.3637 0.4649 -0.0497 0.0460  -0.0233 16  ILE A CA  
93   C C   . ILE A 16  ? 0.4342 0.3702 0.4671 -0.0536 0.0454  -0.0114 16  ILE A C   
94   O O   . ILE A 16  ? 0.4810 0.4184 0.5056 -0.0652 0.0518  -0.0034 16  ILE A O   
95   C CB  . ILE A 16  ? 0.5580 0.5228 0.6352 -0.0599 0.0449  -0.0227 16  ILE A CB  
96   C CG1 . ILE A 16  ? 0.5392 0.5303 0.6449 -0.0543 0.0454  -0.0330 16  ILE A CG1 
97   C CG2 . ILE A 16  ? 0.4783 0.4150 0.5481 -0.0614 0.0345  -0.0183 16  ILE A CG2 
98   C CD1 . ILE A 16  ? 0.5903 0.5859 0.7140 -0.0601 0.0386  -0.0331 16  ILE A CD1 
99   N N   . LYS A 17  ? 0.4214 0.3373 0.4414 -0.0437 0.0380  -0.0093 17  LYS A N   
100  C CA  . LYS A 17  ? 0.4693 0.3629 0.4652 -0.0436 0.0361  0.0025  17  LYS A CA  
101  C C   . LYS A 17  ? 0.4291 0.2944 0.4224 -0.0450 0.0292  0.0066  17  LYS A C   
102  O O   . LYS A 17  ? 0.4260 0.2842 0.4249 -0.0366 0.0223  0.0007  17  LYS A O   
103  C CB  . LYS A 17  ? 0.4613 0.3551 0.4460 -0.0308 0.0325  0.0015  17  LYS A CB  
104  C CG  . LYS A 17  ? 0.4747 0.3499 0.4362 -0.0278 0.0299  0.0145  17  LYS A CG  
105  C CD  . LYS A 17  ? 0.5458 0.4314 0.4991 -0.0168 0.0268  0.0124  17  LYS A CD  
106  C CE  . LYS A 17  ? 0.6691 0.5492 0.5995 -0.0158 0.0265  0.0263  17  LYS A CE  
107  N NZ  . LYS A 17  ? 0.6185 0.5102 0.5422 -0.0049 0.0214  0.0243  17  LYS A NZ  
108  N N   . GLN A 18  ? 0.4342 0.2826 0.4182 -0.0562 0.0314  0.0163  18  GLN A N   
109  C CA  . GLN A 18  ? 0.4217 0.2394 0.4016 -0.0585 0.0253  0.0185  18  GLN A CA  
110  C C   . GLN A 18  ? 0.4216 0.2093 0.3784 -0.0533 0.0235  0.0306  18  GLN A C   
111  O O   . GLN A 18  ? 0.4878 0.2726 0.4321 -0.0599 0.0285  0.0423  18  GLN A O   
112  C CB  . GLN A 18  ? 0.4502 0.2673 0.4396 -0.0770 0.0281  0.0191  18  GLN A CB  
113  C CG  . GLN A 18  ? 0.5761 0.3613 0.5621 -0.0802 0.0209  0.0172  18  GLN A CG  
114  C CD  . GLN A 18  ? 0.6065 0.3933 0.6034 -0.1005 0.0223  0.0161  18  GLN A CD  
115  O OE1 . GLN A 18  ? 0.6467 0.4504 0.6488 -0.1139 0.0299  0.0215  18  GLN A OE1 
116  N NE2 . GLN A 18  ? 0.5539 0.3271 0.5550 -0.1036 0.0151  0.0081  18  GLN A NE2 
117  N N   . PHE A 19  ? 0.4307 0.1975 0.3817 -0.0408 0.0165  0.0285  19  PHE A N   
118  C CA  . PHE A 19  ? 0.5165 0.2539 0.4481 -0.0328 0.0142  0.0397  19  PHE A CA  
119  C C   . PHE A 19  ? 0.6159 0.3174 0.5414 -0.0433 0.0136  0.0438  19  PHE A C   
120  O O   . PHE A 19  ? 0.5395 0.2380 0.4757 -0.0520 0.0121  0.0343  19  PHE A O   
121  C CB  . PHE A 19  ? 0.4896 0.2233 0.4193 -0.0136 0.0079  0.0347  19  PHE A CB  
122  C CG  . PHE A 19  ? 0.4923 0.2573 0.4256 -0.0047 0.0080  0.0320  19  PHE A CG  
123  C CD1 . PHE A 19  ? 0.4335 0.2263 0.3833 -0.0072 0.0092  0.0204  19  PHE A CD1 
124  C CD2 . PHE A 19  ? 0.5319 0.2986 0.4522 0.0055  0.0066  0.0413  19  PHE A CD2 
125  C CE1 . PHE A 19  ? 0.4507 0.2692 0.4034 -0.0004 0.0096  0.0167  19  PHE A CE1 
126  C CE2 . PHE A 19  ? 0.5223 0.3186 0.4455 0.0115  0.0063  0.0376  19  PHE A CE2 
127  C CZ  . PHE A 19  ? 0.4950 0.3154 0.4338 0.0080  0.0081  0.0247  19  PHE A CZ  
128  N N   . PHE A 20  ? 0.5894 0.2632 0.4974 -0.0429 0.0144  0.0584  20  PHE A N   
129  C CA  . PHE A 20  ? 0.6085 0.2405 0.5090 -0.0516 0.0134  0.0622  20  PHE A CA  
130  C C   . PHE A 20  ? 0.5838 0.1917 0.4831 -0.0374 0.0070  0.0520  20  PHE A C   
131  O O   . PHE A 20  ? 0.5517 0.1725 0.4523 -0.0190 0.0037  0.0473  20  PHE A O   
132  C CB  . PHE A 20  ? 0.6545 0.2612 0.5361 -0.0542 0.0160  0.0825  20  PHE A CB  
133  C CG  . PHE A 20  ? 0.7850 0.4172 0.6661 -0.0703 0.0235  0.0920  20  PHE A CG  
134  C CD1 . PHE A 20  ? 0.8322 0.4718 0.7236 -0.0931 0.0287  0.0891  20  PHE A CD1 
135  C CD2 . PHE A 20  ? 0.7784 0.4319 0.6495 -0.0630 0.0255  0.1025  20  PHE A CD2 
136  C CE1 . PHE A 20  ? 0.9204 0.5873 0.8124 -0.1077 0.0371  0.0970  20  PHE A CE1 
137  C CE2 . PHE A 20  ? 0.8185 0.4977 0.6876 -0.0779 0.0335  0.1098  20  PHE A CE2 
138  C CZ  . PHE A 20  ? 0.8567 0.5429 0.7366 -0.0999 0.0399  0.1070  20  PHE A CZ  
139  N N   . PRO A 21  ? 0.5860 0.1618 0.4837 -0.0471 0.0056  0.0465  21  PRO A N   
140  C CA  . PRO A 21  ? 0.5879 0.1573 0.4911 -0.0341 0.0005  0.0323  21  PRO A CA  
141  C C   . PRO A 21  ? 0.6237 0.1841 0.5209 -0.0104 -0.0018 0.0363  21  PRO A C   
142  O O   . PRO A 21  ? 0.5973 0.1672 0.4998 0.0034  -0.0045 0.0247  21  PRO A O   
143  C CB  . PRO A 21  ? 0.6119 0.1616 0.5199 -0.0487 0.0004  0.0278  21  PRO A CB  
144  C CG  . PRO A 21  ? 0.6706 0.2257 0.5809 -0.0730 0.0045  0.0347  21  PRO A CG  
145  C CD  . PRO A 21  ? 0.6683 0.2304 0.5672 -0.0705 0.0089  0.0510  21  PRO A CD  
146  N N   . ALA A 22  ? 0.6189 0.1628 0.5056 -0.0059 -0.0006 0.0531  22  ALA A N   
147  C CA  . ALA A 22  ? 0.6567 0.1955 0.5398 0.0172  -0.0034 0.0580  22  ALA A CA  
148  C C   . ALA A 22  ? 0.6636 0.2298 0.5457 0.0330  -0.0054 0.0570  22  ALA A C   
149  O O   . ALA A 22  ? 0.6185 0.1887 0.5018 0.0526  -0.0081 0.0576  22  ALA A O   
150  C CB  . ALA A 22  ? 0.6926 0.2088 0.5653 0.0179  -0.0028 0.0781  22  ALA A CB  
151  N N   . TYR A 23  ? 0.5675 0.1552 0.4496 0.0246  -0.0037 0.0551  23  TYR A N   
152  C CA  . TYR A 23  ? 0.5779 0.2051 0.4657 0.0363  -0.0051 0.0548  23  TYR A CA  
153  C C   . TYR A 23  ? 0.5787 0.2340 0.4814 0.0374  -0.0061 0.0378  23  TYR A C   
154  O O   . TYR A 23  ? 0.5201 0.2109 0.4309 0.0365  -0.0054 0.0354  23  TYR A O   
155  C CB  . TYR A 23  ? 0.5535 0.2041 0.4386 0.0259  -0.0018 0.0657  23  TYR A CB  
156  C CG  . TYR A 23  ? 0.6011 0.2239 0.4691 0.0261  -0.0015 0.0850  23  TYR A CG  
157  C CD1 . TYR A 23  ? 0.6919 0.3024 0.5504 0.0458  -0.0061 0.0954  23  TYR A CD1 
158  C CD2 . TYR A 23  ? 0.6801 0.2876 0.5420 0.0064  0.0033  0.0937  23  TYR A CD2 
159  C CE1 . TYR A 23  ? 0.7851 0.3668 0.6273 0.0471  -0.0066 0.1153  23  TYR A CE1 
160  C CE2 . TYR A 23  ? 0.7353 0.3140 0.5802 0.0054  0.0037  0.1135  23  TYR A CE2 
161  C CZ  . TYR A 23  ? 0.8138 0.3782 0.6483 0.0264  -0.0016 0.1247  23  TYR A CZ  
162  O OH  . TYR A 23  ? 0.8859 0.4232 0.7050 0.0264  -0.0021 0.1458  23  TYR A OH  
163  N N   . ARG A 24  ? 0.5272 0.1660 0.4324 0.0387  -0.0076 0.0259  24  ARG A N   
164  C CA  . ARG A 24  ? 0.5392 0.2039 0.4563 0.0411  -0.0090 0.0119  24  ARG A CA  
165  C C   . ARG A 24  ? 0.5104 0.2019 0.4309 0.0571  -0.0105 0.0128  24  ARG A C   
166  O O   . ARG A 24  ? 0.5072 0.2287 0.4383 0.0554  -0.0107 0.0064  24  ARG A O   
167  C CB  . ARG A 24  ? 0.5512 0.1999 0.4692 0.0419  -0.0102 -0.0001 24  ARG A CB  
168  C CG  . ARG A 24  ? 0.6497 0.3210 0.5744 0.0520  -0.0117 -0.0111 24  ARG A CG  
169  N N   . TYR A 25  ? 0.5512 0.2323 0.4637 0.0726  -0.0119 0.0212  25  TYR A N   
170  C CA  . TYR A 25  ? 0.5471 0.2569 0.4644 0.0871  -0.0139 0.0218  25  TYR A CA  
171  C C   . TYR A 25  ? 0.5545 0.2981 0.4772 0.0789  -0.0134 0.0251  25  TYR A C   
172  O O   . TYR A 25  ? 0.4984 0.2710 0.4308 0.0803  -0.0140 0.0182  25  TYR A O   
173  C CB  . TYR A 25  ? 0.6486 0.3423 0.5574 0.1054  -0.0161 0.0322  25  TYR A CB  
174  C CG  . TYR A 25  ? 0.7116 0.4378 0.6260 0.1206  -0.0190 0.0347  25  TYR A CG  
175  C CD1 . TYR A 25  ? 0.7621 0.5006 0.6844 0.1339  -0.0194 0.0253  25  TYR A CD1 
176  C CD2 . TYR A 25  ? 0.7176 0.4648 0.6293 0.1205  -0.0213 0.0462  25  TYR A CD2 
177  C CE1 . TYR A 25  ? 0.7278 0.5001 0.6575 0.1460  -0.0220 0.0276  25  TYR A CE1 
178  C CE2 . TYR A 25  ? 0.7933 0.5732 0.7110 0.1326  -0.0249 0.0479  25  TYR A CE2 
179  C CZ  . TYR A 25  ? 0.7925 0.5853 0.7204 0.1450  -0.0253 0.0388  25  TYR A CZ  
180  O OH  . TYR A 25  ? 0.8052 0.6339 0.7410 0.1553  -0.0288 0.0405  25  TYR A OH  
181  N N   . ASN A 26  ? 0.4736 0.2127 0.3893 0.0690  -0.0116 0.0349  26  ASN A N   
182  C CA  . ASN A 26  ? 0.4878 0.2576 0.4062 0.0616  -0.0103 0.0366  26  ASN A CA  
183  C C   . ASN A 26  ? 0.5019 0.2875 0.4331 0.0485  -0.0073 0.0249  26  ASN A C   
184  O O   . ASN A 26  ? 0.4412 0.2547 0.3796 0.0465  -0.0067 0.0200  26  ASN A O   
185  C CB  . ASN A 26  ? 0.4836 0.2447 0.3887 0.0549  -0.0084 0.0508  26  ASN A CB  
186  C CG  . ASN A 26  ? 0.6436 0.3907 0.5361 0.0695  -0.0125 0.0650  26  ASN A CG  
187  O OD1 . ASN A 26  ? 0.6647 0.3764 0.5494 0.0731  -0.0129 0.0720  26  ASN A OD1 
188  N ND2 . ASN A 26  ? 0.5949 0.3692 0.4860 0.0786  -0.0161 0.0689  26  ASN A ND2 
189  N N   . PHE A 27  ? 0.4340 0.2019 0.3686 0.0398  -0.0058 0.0201  27  PHE A N   
190  C CA  . PHE A 27  ? 0.4115 0.1949 0.3601 0.0299  -0.0043 0.0097  27  PHE A CA  
191  C C   . PHE A 27  ? 0.3948 0.1981 0.3531 0.0376  -0.0068 0.0011  27  PHE A C   
192  O O   . PHE A 27  ? 0.4009 0.2262 0.3695 0.0333  -0.0056 -0.0039 27  PHE A O   
193  C CB  . PHE A 27  ? 0.4556 0.2172 0.4056 0.0213  -0.0045 0.0058  27  PHE A CB  
194  C CG  . PHE A 27  ? 0.4398 0.2169 0.4045 0.0152  -0.0055 -0.0048 27  PHE A CG  
195  C CD1 . PHE A 27  ? 0.3990 0.1937 0.3754 0.0037  -0.0025 -0.0065 27  PHE A CD1 
196  C CD2 . PHE A 27  ? 0.4083 0.1840 0.3752 0.0218  -0.0093 -0.0124 27  PHE A CD2 
197  C CE1 . PHE A 27  ? 0.3704 0.1798 0.3617 -0.0002 -0.0045 -0.0147 27  PHE A CE1 
198  C CE2 . PHE A 27  ? 0.4366 0.2268 0.4157 0.0166  -0.0112 -0.0199 27  PHE A CE2 
199  C CZ  . PHE A 27  ? 0.3830 0.1894 0.3749 0.0061  -0.0094 -0.0205 27  PHE A CZ  
200  N N   . TRP A 28  ? 0.3927 0.1879 0.3477 0.0493  -0.0098 -0.0006 28  TRP A N   
201  C CA  . TRP A 28  ? 0.3790 0.1933 0.3427 0.0547  -0.0115 -0.0078 28  TRP A CA  
202  C C   . TRP A 28  ? 0.4116 0.2505 0.3779 0.0592  -0.0120 -0.0057 28  TRP A C   
203  O O   . TRP A 28  ? 0.3944 0.2524 0.3704 0.0573  -0.0122 -0.0113 28  TRP A O   
204  C CB  . TRP A 28  ? 0.3607 0.1624 0.3198 0.0656  -0.0133 -0.0110 28  TRP A CB  
205  C CG  . TRP A 28  ? 0.3986 0.1827 0.3566 0.0593  -0.0136 -0.0176 28  TRP A CG  
206  C CD1 . TRP A 28  ? 0.4662 0.2214 0.4146 0.0607  -0.0138 -0.0188 28  TRP A CD1 
207  C CD2 . TRP A 28  ? 0.3832 0.1784 0.3500 0.0504  -0.0146 -0.0241 28  TRP A CD2 
208  N NE1 . TRP A 28  ? 0.4251 0.1746 0.3751 0.0516  -0.0150 -0.0270 28  TRP A NE1 
209  C CE2 . TRP A 28  ? 0.3952 0.1705 0.3567 0.0459  -0.0159 -0.0293 28  TRP A CE2 
210  C CE3 . TRP A 28  ? 0.3534 0.1722 0.3321 0.0460  -0.0150 -0.0258 28  TRP A CE3 
211  C CZ2 . TRP A 28  ? 0.4530 0.2356 0.4204 0.0374  -0.0183 -0.0353 28  TRP A CZ2 
212  C CZ3 . TRP A 28  ? 0.3831 0.2062 0.3685 0.0389  -0.0170 -0.0305 28  TRP A CZ3 
213  C CH2 . TRP A 28  ? 0.4222 0.2292 0.4018 0.0347  -0.0191 -0.0348 28  TRP A CH2 
214  N N   . LYS A 29  ? 0.3987 0.2373 0.3562 0.0647  -0.0126 0.0026  29  LYS A N   
215  C CA  . LYS A 29  ? 0.4108 0.2756 0.3699 0.0670  -0.0139 0.0040  29  LYS A CA  
216  C C   . LYS A 29  ? 0.3898 0.2684 0.3533 0.0546  -0.0110 -0.0001 29  LYS A C   
217  O O   . LYS A 29  ? 0.4139 0.3134 0.3848 0.0525  -0.0114 -0.0060 29  LYS A O   
218  C CB  . LYS A 29  ? 0.4440 0.3066 0.3912 0.0761  -0.0164 0.0153  29  LYS A CB  
219  C CG  . LYS A 29  ? 0.5323 0.3844 0.4772 0.0926  -0.0194 0.0189  29  LYS A CG  
220  C CD  . LYS A 29  ? 0.5185 0.3808 0.4742 0.0984  -0.0195 0.0093  29  LYS A CD  
221  C CE  . LYS A 29  ? 0.6290 0.4830 0.5823 0.1164  -0.0211 0.0121  29  LYS A CE  
222  N NZ  . LYS A 29  ? 0.5846 0.4493 0.5467 0.1216  -0.0197 0.0025  29  LYS A NZ  
223  N N   . GLU A 30  ? 0.3906 0.2582 0.3504 0.0458  -0.0074 0.0024  30  GLU A N   
224  C CA  . GLU A 30  ? 0.4205 0.3024 0.3865 0.0353  -0.0033 -0.0033 30  GLU A CA  
225  C C   . GLU A 30  ? 0.4253 0.3135 0.4072 0.0325  -0.0031 -0.0135 30  GLU A C   
226  O O   . GLU A 30  ? 0.3834 0.2879 0.3726 0.0298  -0.0019 -0.0203 30  GLU A O   
227  C CB  . GLU A 30  ? 0.4007 0.2722 0.3624 0.0260  0.0014  0.0011  30  GLU A CB  
228  C CG  . GLU A 30  ? 0.4725 0.3621 0.4425 0.0168  0.0069  -0.0063 30  GLU A CG  
229  C CD  . GLU A 30  ? 0.5892 0.4920 0.5465 0.0133  0.0103  -0.0022 30  GLU A CD  
230  O OE1 . GLU A 30  ? 0.6466 0.5398 0.5887 0.0139  0.0098  0.0098  30  GLU A OE1 
231  O OE2 . GLU A 30  ? 0.6462 0.5682 0.6078 0.0101  0.0135  -0.0110 30  GLU A OE2 
232  N N   . ALA A 31  ? 0.3620 0.2365 0.3486 0.0330  -0.0045 -0.0148 31  ALA A N   
233  C CA  . ALA A 31  ? 0.3660 0.2462 0.3664 0.0309  -0.0053 -0.0221 31  ALA A CA  
234  C C   . ALA A 31  ? 0.3366 0.2291 0.3405 0.0361  -0.0078 -0.0249 31  ALA A C   
235  O O   . ALA A 31  ? 0.3631 0.2653 0.3775 0.0328  -0.0073 -0.0302 31  ALA A O   
236  C CB  . ALA A 31  ? 0.3411 0.2059 0.3423 0.0303  -0.0076 -0.0222 31  ALA A CB  
237  N N   . GLY A 32  ? 0.3371 0.2287 0.3332 0.0443  -0.0103 -0.0213 32  GLY A N   
238  C CA  . GLY A 32  ? 0.3463 0.2526 0.3470 0.0482  -0.0122 -0.0236 32  GLY A CA  
239  C C   . GLY A 32  ? 0.3852 0.3098 0.3891 0.0442  -0.0118 -0.0264 32  GLY A C   
240  O O   . GLY A 32  ? 0.3028 0.2366 0.3159 0.0400  -0.0119 -0.0314 32  GLY A O   
241  N N   . PHE A 33  ? 0.3230 0.2521 0.3181 0.0446  -0.0115 -0.0231 33  PHE A N   
242  C CA  . PHE A 33  ? 0.3308 0.2790 0.3263 0.0402  -0.0117 -0.0273 33  PHE A CA  
243  C C   . PHE A 33  ? 0.3069 0.2550 0.3094 0.0310  -0.0076 -0.0357 33  PHE A C   
244  O O   . PHE A 33  ? 0.3076 0.2665 0.3162 0.0262  -0.0075 -0.0431 33  PHE A O   
245  C CB  . PHE A 33  ? 0.3087 0.2645 0.2907 0.0434  -0.0133 -0.0206 33  PHE A CB  
246  C CG  . PHE A 33  ? 0.3753 0.3373 0.3539 0.0546  -0.0182 -0.0135 33  PHE A CG  
247  C CD1 . PHE A 33  ? 0.3461 0.3276 0.3329 0.0562  -0.0211 -0.0169 33  PHE A CD1 
248  C CD2 . PHE A 33  ? 0.3837 0.3312 0.3524 0.0635  -0.0193 -0.0034 33  PHE A CD2 
249  C CE1 . PHE A 33  ? 0.4126 0.4037 0.3993 0.0679  -0.0249 -0.0110 33  PHE A CE1 
250  C CE2 . PHE A 33  ? 0.4802 0.4329 0.4479 0.0764  -0.0234 0.0026  33  PHE A CE2 
251  C CZ  . PHE A 33  ? 0.4084 0.3854 0.3859 0.0793  -0.0261 -0.0014 33  PHE A CZ  
252  N N   . LEU A 34  ? 0.2760 0.2125 0.2792 0.0283  -0.0039 -0.0353 34  LEU A N   
253  C CA  . LEU A 34  ? 0.3299 0.2680 0.3433 0.0220  0.0004  -0.0439 34  LEU A CA  
254  C C   . LEU A 34  ? 0.3303 0.2654 0.3579 0.0218  -0.0013 -0.0485 34  LEU A C   
255  O O   . LEU A 34  ? 0.3043 0.2436 0.3397 0.0180  0.0005  -0.0566 34  LEU A O   
256  C CB  . LEU A 34  ? 0.3128 0.2428 0.3277 0.0193  0.0045  -0.0421 34  LEU A CB  
257  C CG  . LEU A 34  ? 0.3851 0.3204 0.3878 0.0157  0.0088  -0.0393 34  LEU A CG  
258  C CD1 . LEU A 34  ? 0.3979 0.3254 0.4051 0.0117  0.0127  -0.0365 34  LEU A CD1 
259  C CD2 . LEU A 34  ? 0.3419 0.2931 0.3439 0.0114  0.0131  -0.0492 34  LEU A CD2 
260  N N   . SER A 35  ? 0.2837 0.2104 0.3134 0.0256  -0.0046 -0.0432 35  SER A N   
261  C CA  . SER A 35  ? 0.2957 0.2199 0.3364 0.0251  -0.0066 -0.0447 35  SER A CA  
262  C C   . SER A 35  ? 0.3536 0.2879 0.3959 0.0227  -0.0078 -0.0479 35  SER A C   
263  O O   . SER A 35  ? 0.2943 0.2268 0.3465 0.0186  -0.0072 -0.0523 35  SER A O   
264  C CB  . SER A 35  ? 0.2563 0.1734 0.2944 0.0292  -0.0098 -0.0387 35  SER A CB  
265  O OG  . SER A 35  ? 0.3121 0.2193 0.3504 0.0291  -0.0096 -0.0370 35  SER A OG  
266  N N   . LEU A 36  ? 0.2849 0.2298 0.3185 0.0253  -0.0097 -0.0451 36  LEU A N   
267  C CA  . LEU A 36  ? 0.2914 0.2506 0.3277 0.0217  -0.0114 -0.0479 36  LEU A CA  
268  C C   . LEU A 36  ? 0.3721 0.3375 0.4094 0.0143  -0.0097 -0.0569 36  LEU A C   
269  O O   . LEU A 36  ? 0.3243 0.2981 0.3662 0.0080  -0.0109 -0.0616 36  LEU A O   
270  C CB  . LEU A 36  ? 0.3391 0.3123 0.3675 0.0279  -0.0143 -0.0425 36  LEU A CB  
271  C CG  . LEU A 36  ? 0.3646 0.3342 0.3920 0.0358  -0.0153 -0.0361 36  LEU A CG  
272  C CD1 . LEU A 36  ? 0.3387 0.3254 0.3613 0.0434  -0.0178 -0.0321 36  LEU A CD1 
273  C CD2 . LEU A 36  ? 0.3183 0.2871 0.3544 0.0317  -0.0150 -0.0365 36  LEU A CD2 
274  N N   . LEU A 37  ? 0.3317 0.2939 0.3642 0.0139  -0.0065 -0.0603 37  LEU A N   
275  C CA  . LEU A 37  ? 0.3272 0.2960 0.3588 0.0071  -0.0038 -0.0712 37  LEU A CA  
276  C C   . LEU A 37  ? 0.3404 0.2958 0.3832 0.0046  0.0010  -0.0796 37  LEU A C   
277  O O   . LEU A 37  ? 0.3529 0.3113 0.3950 -0.0001 0.0046  -0.0909 37  LEU A O   
278  C CB  . LEU A 37  ? 0.2690 0.2480 0.2857 0.0080  -0.0027 -0.0700 37  LEU A CB  
279  C CG  . LEU A 37  ? 0.3192 0.3136 0.3258 0.0116  -0.0085 -0.0620 37  LEU A CG  
280  C CD1 . LEU A 37  ? 0.3653 0.3659 0.3557 0.0143  -0.0081 -0.0560 37  LEU A CD1 
281  C CD2 . LEU A 37  ? 0.3933 0.4059 0.4018 0.0046  -0.0120 -0.0696 37  LEU A CD2 
282  N N   . GLN A 38  ? 0.3169 0.2589 0.3700 0.0083  0.0009  -0.0749 38  GLN A N   
283  C CA  . GLN A 38  ? 0.3046 0.2357 0.3707 0.0084  0.0048  -0.0815 38  GLN A CA  
284  C C   . GLN A 38  ? 0.4007 0.3256 0.4748 0.0031  0.0055  -0.0911 38  GLN A C   
285  O O   . GLN A 38  ? 0.3823 0.2991 0.4656 0.0038  0.0099  -0.1001 38  GLN A O   
286  C CB  . GLN A 38  ? 0.3029 0.2235 0.3784 0.0133  0.0027  -0.0730 38  GLN A CB  
287  C CG  . GLN A 38  ? 0.3292 0.2521 0.3993 0.0168  0.0030  -0.0664 38  GLN A CG  
288  C CD  . GLN A 38  ? 0.3414 0.2695 0.4122 0.0160  0.0092  -0.0726 38  GLN A CD  
289  O OE1 . GLN A 38  ? 0.3433 0.2693 0.4282 0.0177  0.0124  -0.0774 38  GLN A OE1 
290  N NE2 . GLN A 38  ? 0.2930 0.2296 0.3491 0.0141  0.0112  -0.0715 38  GLN A NE2 
291  N N   . GLU A 39  ? 0.4059 0.3338 0.4780 -0.0021 0.0016  -0.0896 39  GLU A N   
292  C CA  . GLU A 39  ? 0.4830 0.4019 0.5625 -0.0093 0.0026  -0.0997 39  GLU A CA  
293  C C   . GLU A 39  ? 0.5121 0.4385 0.5847 -0.0146 0.0063  -0.1150 39  GLU A C   
294  O O   . GLU A 39  ? 0.5433 0.4592 0.6215 -0.0208 0.0082  -0.1267 39  GLU A O   
295  C CB  . GLU A 39  ? 0.5852 0.5075 0.6654 -0.0165 -0.0019 -0.0948 39  GLU A CB  
296  C CG  . GLU A 39  ? 0.6029 0.5489 0.6719 -0.0216 -0.0046 -0.0965 39  GLU A CG  
297  C CD  . GLU A 39  ? 0.6409 0.5955 0.7132 -0.0290 -0.0085 -0.0915 39  GLU A CD  
298  O OE1 . GLU A 39  ? 0.6973 0.6432 0.7766 -0.0395 -0.0083 -0.0978 39  GLU A OE1 
299  O OE2 . GLU A 39  ? 0.5908 0.5607 0.6592 -0.0245 -0.0113 -0.0814 39  GLU A OE2 
300  N N   . PHE A 40  ? 0.4558 0.3985 0.5155 -0.0128 0.0076  -0.1155 40  PHE A N   
301  C CA  . PHE A 40  ? 0.4361 0.3891 0.4859 -0.0184 0.0110  -0.1297 40  PHE A CA  
302  C C   . PHE A 40  ? 0.4448 0.3974 0.4936 -0.0133 0.0186  -0.1353 40  PHE A C   
303  O O   . PHE A 40  ? 0.4778 0.4286 0.5296 -0.0063 0.0198  -0.1254 40  PHE A O   
304  C CB  . PHE A 40  ? 0.4364 0.4130 0.4697 -0.0216 0.0062  -0.1253 40  PHE A CB  
305  C CG  . PHE A 40  ? 0.4858 0.4694 0.5220 -0.0257 -0.0007 -0.1190 40  PHE A CG  
306  C CD1 . PHE A 40  ? 0.5615 0.5439 0.6028 -0.0367 -0.0022 -0.1294 40  PHE A CD1 
307  C CD2 . PHE A 40  ? 0.4418 0.4327 0.4764 -0.0191 -0.0051 -0.1035 40  PHE A CD2 
308  C CE1 . PHE A 40  ? 0.5444 0.5369 0.5899 -0.0420 -0.0079 -0.1233 40  PHE A CE1 
309  C CE2 . PHE A 40  ? 0.4954 0.4968 0.5341 -0.0224 -0.0103 -0.0985 40  PHE A CE2 
310  C CZ  . PHE A 40  ? 0.4605 0.4646 0.5051 -0.0344 -0.0116 -0.1078 40  PHE A CZ  
311  N N   . ASP A 41  ? 0.4401 0.3967 0.4835 -0.0180 0.0239  -0.1520 41  ASP A N   
312  C CA  . ASP A 41  ? 0.4760 0.4350 0.5200 -0.0134 0.0328  -0.1590 41  ASP A CA  
313  C C   . ASP A 41  ? 0.5004 0.4814 0.5245 -0.0149 0.0347  -0.1548 41  ASP A C   
314  O O   . ASP A 41  ? 0.5614 0.5491 0.5835 -0.0133 0.0431  -0.1610 41  ASP A O   
315  C CB  . ASP A 41  ? 0.5435 0.4945 0.5925 -0.0160 0.0398  -0.1811 41  ASP A CB  
316  C CG  . ASP A 41  ? 0.8065 0.7657 0.8408 -0.0274 0.0376  -0.1944 41  ASP A CG  
317  O OD1 . ASP A 41  ? 0.7718 0.7509 0.7895 -0.0324 0.0319  -0.1870 41  ASP A OD1 
318  O OD2 . ASP A 41  ? 0.9710 0.9170 1.0107 -0.0312 0.0413  -0.2128 41  ASP A OD2 
319  N N   . PHE A 42  ? 0.4588 0.4522 0.4685 -0.0176 0.0275  -0.1439 42  PHE A N   
320  C CA  . PHE A 42  ? 0.4215 0.4341 0.4109 -0.0191 0.0288  -0.1387 42  PHE A CA  
321  C C   . PHE A 42  ? 0.3875 0.3978 0.3749 -0.0128 0.0272  -0.1190 42  PHE A C   
322  O O   . PHE A 42  ? 0.3986 0.4213 0.3683 -0.0136 0.0262  -0.1098 42  PHE A O   
323  C CB  . PHE A 42  ? 0.4236 0.4544 0.3960 -0.0257 0.0219  -0.1402 42  PHE A CB  
324  C CG  . PHE A 42  ? 0.4518 0.4821 0.4294 -0.0247 0.0119  -0.1299 42  PHE A CG  
325  C CD1 . PHE A 42  ? 0.3953 0.4279 0.3694 -0.0176 0.0067  -0.1107 42  PHE A CD1 
326  C CD2 . PHE A 42  ? 0.4989 0.5274 0.4848 -0.0313 0.0083  -0.1400 42  PHE A CD2 
327  C CE1 . PHE A 42  ? 0.4552 0.4905 0.4351 -0.0154 -0.0013 -0.1025 42  PHE A CE1 
328  C CE2 . PHE A 42  ? 0.4553 0.4880 0.4470 -0.0312 0.0001  -0.1305 42  PHE A CE2 
329  C CZ  . PHE A 42  ? 0.4457 0.4832 0.4348 -0.0225 -0.0043 -0.1121 42  PHE A CZ  
330  N N   . VAL A 43  ? 0.3755 0.3698 0.3798 -0.0072 0.0271  -0.1126 43  VAL A N   
331  C CA  . VAL A 43  ? 0.3227 0.3124 0.3260 -0.0029 0.0266  -0.0970 43  VAL A CA  
332  C C   . VAL A 43  ? 0.3386 0.3203 0.3591 -0.0004 0.0329  -0.1003 43  VAL A C   
333  O O   . VAL A 43  ? 0.3711 0.3464 0.4073 0.0010  0.0351  -0.1113 43  VAL A O   
334  C CB  . VAL A 43  ? 0.3830 0.3637 0.3883 0.0017  0.0179  -0.0840 43  VAL A CB  
335  C CG1 . VAL A 43  ? 0.3411 0.3338 0.3327 0.0009  0.0115  -0.0800 43  VAL A CG1 
336  C CG2 . VAL A 43  ? 0.3636 0.3310 0.3876 0.0039  0.0155  -0.0868 43  VAL A CG2 
337  N N   . PRO A 44  ? 0.3372 0.3187 0.3569 0.0002  0.0353  -0.0904 44  PRO A N   
338  C CA  . PRO A 44  ? 0.4112 0.3894 0.4502 0.0024  0.0400  -0.0927 44  PRO A CA  
339  C C   . PRO A 44  ? 0.3401 0.3036 0.3957 0.0075  0.0334  -0.0898 44  PRO A C   
340  O O   . PRO A 44  ? 0.3699 0.3250 0.4203 0.0089  0.0259  -0.0816 44  PRO A O   
341  C CB  . PRO A 44  ? 0.3765 0.3574 0.4086 -0.0008 0.0421  -0.0807 44  PRO A CB  
342  C CG  . PRO A 44  ? 0.4177 0.4044 0.4250 -0.0045 0.0413  -0.0739 44  PRO A CG  
343  C CD  . PRO A 44  ? 0.3817 0.3666 0.3831 -0.0019 0.0341  -0.0770 44  PRO A CD  
344  N N   . ARG A 45  ? 0.3236 0.2856 0.3995 0.0110  0.0366  -0.0963 45  ARG A N   
345  C CA  . ARG A 45  ? 0.3588 0.3090 0.4498 0.0157  0.0302  -0.0907 45  ARG A CA  
346  C C   . ARG A 45  ? 0.3757 0.3242 0.4630 0.0144  0.0262  -0.0779 45  ARG A C   
347  O O   . ARG A 45  ? 0.3459 0.3026 0.4298 0.0107  0.0306  -0.0753 45  ARG A O   
348  C CB  . ARG A 45  ? 0.3297 0.2805 0.4442 0.0212  0.0338  -0.0982 45  ARG A CB  
349  C CG  . ARG A 45  ? 0.3922 0.3409 0.5122 0.0233  0.0392  -0.1135 45  ARG A CG  
350  C CD  . ARG A 45  ? 0.3918 0.3250 0.5079 0.0222  0.0334  -0.1151 45  ARG A CD  
351  N NE  . ARG A 45  ? 0.4416 0.3804 0.5359 0.0151  0.0324  -0.1157 45  ARG A NE  
352  C CZ  . ARG A 45  ? 0.4741 0.4067 0.5609 0.0116  0.0262  -0.1130 45  ARG A CZ  
353  N NH1 . ARG A 45  ? 0.4008 0.3191 0.4982 0.0131  0.0214  -0.1099 45  ARG A NH1 
354  N NH2 . ARG A 45  ? 0.4651 0.4080 0.5334 0.0064  0.0246  -0.1120 45  ARG A NH2 
355  N N   . LEU A 46  ? 0.2981 0.2356 0.3847 0.0165  0.0183  -0.0704 46  LEU A N   
356  C CA  . LEU A 46  ? 0.3210 0.2538 0.4044 0.0155  0.0139  -0.0606 46  LEU A CA  
357  C C   . LEU A 46  ? 0.3321 0.2643 0.4339 0.0182  0.0105  -0.0593 46  LEU A C   
358  O O   . LEU A 46  ? 0.3402 0.2673 0.4506 0.0223  0.0068  -0.0599 46  LEU A O   
359  C CB  . LEU A 46  ? 0.2786 0.2021 0.3479 0.0169  0.0078  -0.0543 46  LEU A CB  
360  C CG  . LEU A 46  ? 0.3631 0.2781 0.4263 0.0168  0.0032  -0.0462 46  LEU A CG  
361  C CD1 . LEU A 46  ? 0.3810 0.2961 0.4376 0.0119  0.0068  -0.0431 46  LEU A CD1 
362  C CD2 . LEU A 46  ? 0.3711 0.2801 0.4210 0.0201  -0.0008 -0.0423 46  LEU A CD2 
363  N N   . TYR A 47  ? 0.2738 0.2122 0.3816 0.0150  0.0114  -0.0565 47  TYR A N   
364  C CA  . TYR A 47  ? 0.2797 0.2234 0.4067 0.0173  0.0077  -0.0554 47  TYR A CA  
365  C C   . TYR A 47  ? 0.3018 0.2388 0.4234 0.0146  -0.0003 -0.0479 47  TYR A C   
366  O O   . TYR A 47  ? 0.3177 0.2547 0.4487 0.0181  -0.0068 -0.0453 47  TYR A O   
367  C CB  . TYR A 47  ? 0.3062 0.2678 0.4489 0.0151  0.0141  -0.0593 47  TYR A CB  
368  C CG  . TYR A 47  ? 0.3482 0.3182 0.4980 0.0188  0.0230  -0.0693 47  TYR A CG  
369  C CD1 . TYR A 47  ? 0.3873 0.3510 0.5465 0.0269  0.0221  -0.0747 47  TYR A CD1 
370  C CD2 . TYR A 47  ? 0.3853 0.3684 0.5311 0.0137  0.0326  -0.0737 47  TYR A CD2 
371  C CE1 . TYR A 47  ? 0.4824 0.4511 0.6472 0.0302  0.0305  -0.0864 47  TYR A CE1 
372  C CE2 . TYR A 47  ? 0.3600 0.3519 0.5102 0.0171  0.0416  -0.0851 47  TYR A CE2 
373  C CZ  . TYR A 47  ? 0.4806 0.4644 0.6404 0.0256  0.0404  -0.0924 47  TYR A CZ  
374  O OH  . TYR A 47  ? 0.4273 0.4171 0.5908 0.0289  0.0494  -0.1060 47  TYR A OH  
375  N N   . SER A 48  ? 0.2992 0.2295 0.4050 0.0088  -0.0001 -0.0445 48  SER A N   
376  C CA  . SER A 48  ? 0.3633 0.2856 0.4634 0.0058  -0.0071 -0.0400 48  SER A CA  
377  C C   . SER A 48  ? 0.3924 0.3003 0.4717 0.0019  -0.0058 -0.0370 48  SER A C   
378  O O   . SER A 48  ? 0.3584 0.2662 0.4306 -0.0003 0.0002  -0.0366 48  SER A O   
379  C CB  . SER A 48  ? 0.3915 0.3267 0.5079 0.0007  -0.0093 -0.0399 48  SER A CB  
380  O OG  . SER A 48  ? 0.4168 0.3568 0.5325 -0.0078 -0.0033 -0.0401 48  SER A OG  
381  N N   . ILE A 49  ? 0.3416 0.2369 0.4107 0.0018  -0.0116 -0.0350 49  ILE A N   
382  C CA  . ILE A 49  ? 0.3952 0.2730 0.4462 -0.0008 -0.0109 -0.0324 49  ILE A CA  
383  C C   . ILE A 49  ? 0.4327 0.3030 0.4825 -0.0079 -0.0157 -0.0331 49  ILE A C   
384  O O   . ILE A 49  ? 0.4287 0.3059 0.4860 -0.0080 -0.0215 -0.0351 49  ILE A O   
385  C CB  . ILE A 49  ? 0.4129 0.2803 0.4496 0.0080  -0.0123 -0.0313 49  ILE A CB  
386  C CG1 . ILE A 49  ? 0.4418 0.3084 0.4783 0.0116  -0.0183 -0.0330 49  ILE A CG1 
387  C CG2 . ILE A 49  ? 0.4171 0.2947 0.4556 0.0131  -0.0088 -0.0316 49  ILE A CG2 
388  C CD1 . ILE A 49  ? 0.4734 0.3282 0.4939 0.0187  -0.0192 -0.0326 49  ILE A CD1 
389  N N   . ASN A 50  ? 0.3757 0.2316 0.4159 -0.0150 -0.0135 -0.0312 50  ASN A N   
390  C CA  . ASN A 50  ? 0.3627 0.2076 0.3996 -0.0237 -0.0180 -0.0334 50  ASN A CA  
391  C C   . ASN A 50  ? 0.3985 0.2142 0.4149 -0.0228 -0.0168 -0.0316 50  ASN A C   
392  O O   . ASN A 50  ? 0.4109 0.2155 0.4220 -0.0289 -0.0123 -0.0269 50  ASN A O   
393  C CB  . ASN A 50  ? 0.3616 0.2198 0.4129 -0.0371 -0.0165 -0.0333 50  ASN A CB  
394  C CG  . ASN A 50  ? 0.4418 0.2914 0.4911 -0.0485 -0.0222 -0.0368 50  ASN A CG  
395  O OD1 . ASN A 50  ? 0.4480 0.2762 0.4816 -0.0467 -0.0262 -0.0400 50  ASN A OD1 
396  N ND2 . ASN A 50  ? 0.4767 0.3444 0.5422 -0.0607 -0.0224 -0.0373 50  ASN A ND2 
397  N N   . PRO A 51  ? 0.3942 0.1970 0.3990 -0.0143 -0.0203 -0.0349 51  PRO A N   
398  C CA  . PRO A 51  ? 0.4568 0.2304 0.4435 -0.0104 -0.0192 -0.0342 51  PRO A CA  
399  C C   . PRO A 51  ? 0.4923 0.2436 0.4729 -0.0230 -0.0204 -0.0366 51  PRO A C   
400  O O   . PRO A 51  ? 0.4874 0.2101 0.4542 -0.0211 -0.0184 -0.0343 51  PRO A O   
401  C CB  . PRO A 51  ? 0.4672 0.2392 0.4465 0.0013  -0.0223 -0.0394 51  PRO A CB  
402  C CG  . PRO A 51  ? 0.4913 0.2918 0.4840 0.0034  -0.0244 -0.0400 51  PRO A CG  
403  C CD  . PRO A 51  ? 0.3969 0.2125 0.4052 -0.0078 -0.0250 -0.0389 51  PRO A CD  
404  N N   . GLU A 52  ? 0.4264 0.1888 0.4168 -0.0354 -0.0243 -0.0415 52  GLU A N   
405  C CA  . GLU A 52  ? 0.4624 0.2050 0.4480 -0.0505 -0.0257 -0.0447 52  GLU A CA  
406  C C   . GLU A 52  ? 0.4813 0.2172 0.4691 -0.0610 -0.0197 -0.0360 52  GLU A C   
407  O O   . GLU A 52  ? 0.5060 0.2125 0.4833 -0.0702 -0.0187 -0.0352 52  GLU A O   
408  C CB  . GLU A 52  ? 0.5297 0.2924 0.5270 -0.0620 -0.0323 -0.0517 52  GLU A CB  
409  C CG  . GLU A 52  ? 0.5458 0.3137 0.5372 -0.0540 -0.0386 -0.0595 52  GLU A CG  
410  C CD  . GLU A 52  ? 0.6625 0.3970 0.6317 -0.0470 -0.0380 -0.0658 52  GLU A CD  
411  O OE1 . GLU A 52  ? 0.8548 0.5684 0.8144 -0.0576 -0.0408 -0.0739 52  GLU A OE1 
412  O OE2 . GLU A 52  ? 0.9015 0.6308 0.8633 -0.0311 -0.0347 -0.0635 52  GLU A OE2 
413  N N   . LYS A 53  ? 0.4499 0.2126 0.4512 -0.0611 -0.0155 -0.0300 53  LYS A N   
414  C CA  . LYS A 53  ? 0.4670 0.2288 0.4691 -0.0703 -0.0085 -0.0211 53  LYS A CA  
415  C C   . LYS A 53  ? 0.4766 0.2339 0.4685 -0.0580 -0.0034 -0.0126 53  LYS A C   
416  O O   . LYS A 53  ? 0.4549 0.2137 0.4447 -0.0648 0.0027  -0.0040 53  LYS A O   
417  C CB  . LYS A 53  ? 0.5041 0.3023 0.5287 -0.0807 -0.0063 -0.0216 53  LYS A CB  
418  C CG  . LYS A 53  ? 0.5763 0.3816 0.6115 -0.0940 -0.0127 -0.0290 53  LYS A CG  
419  C CD  . LYS A 53  ? 0.5864 0.4266 0.6450 -0.1059 -0.0100 -0.0284 53  LYS A CD  
420  C CE  . LYS A 53  ? 0.6084 0.4600 0.6784 -0.1181 -0.0183 -0.0357 53  LYS A CE  
421  N NZ  . LYS A 53  ? 0.6333 0.5266 0.7309 -0.1263 -0.0165 -0.0354 53  LYS A NZ  
422  N N   . LEU A 54  ? 0.4339 0.1893 0.4194 -0.0410 -0.0059 -0.0147 54  LEU A N   
423  C CA  . LEU A 54  ? 0.4662 0.2247 0.4444 -0.0290 -0.0026 -0.0078 54  LEU A CA  
424  C C   . LEU A 54  ? 0.4601 0.2479 0.4493 -0.0333 0.0028  -0.0051 54  LEU A C   
425  O O   . LEU A 54  ? 0.4334 0.2211 0.4144 -0.0340 0.0076  0.0032  54  LEU A O   
426  C CB  . LEU A 54  ? 0.4197 0.1466 0.3794 -0.0272 -0.0009 0.0018  54  LEU A CB  
427  C CG  . LEU A 54  ? 0.4551 0.1485 0.4028 -0.0204 -0.0050 -0.0017 54  LEU A CG  
428  C CD1 . LEU A 54  ? 0.5224 0.1827 0.4533 -0.0173 -0.0032 0.0097  54  LEU A CD1 
429  C CD2 . LEU A 54  ? 0.4373 0.1396 0.3854 -0.0034 -0.0086 -0.0090 54  LEU A CD2 
430  N N   . GLU A 55  ? 0.3830 0.1961 0.3902 -0.0355 0.0019  -0.0122 55  GLU A N   
431  C CA  . GLU A 55  ? 0.4161 0.2578 0.4365 -0.0383 0.0076  -0.0126 55  GLU A CA  
432  C C   . GLU A 55  ? 0.3866 0.2452 0.4145 -0.0259 0.0062  -0.0180 55  GLU A C   
433  O O   . GLU A 55  ? 0.3836 0.2430 0.4173 -0.0203 0.0004  -0.0229 55  GLU A O   
434  C CB  . GLU A 55  ? 0.4205 0.2802 0.4599 -0.0506 0.0085  -0.0162 55  GLU A CB  
435  C CG  . GLU A 55  ? 0.5272 0.3787 0.5627 -0.0667 0.0129  -0.0102 55  GLU A CG  
436  C CD  . GLU A 55  ? 0.6191 0.4975 0.6769 -0.0790 0.0150  -0.0138 55  GLU A CD  
437  O OE1 . GLU A 55  ? 0.5612 0.4573 0.6359 -0.0746 0.0100  -0.0209 55  GLU A OE1 
438  O OE2 . GLU A 55  ? 0.6298 0.5127 0.6887 -0.0933 0.0214  -0.0086 55  GLU A OE2 
439  N N   . ILE A 56  ? 0.4165 0.2888 0.4437 -0.0232 0.0118  -0.0172 56  ILE A N   
440  C CA  . ILE A 56  ? 0.3883 0.2767 0.4240 -0.0143 0.0116  -0.0234 56  ILE A CA  
441  C C   . ILE A 56  ? 0.3532 0.2652 0.4044 -0.0187 0.0184  -0.0282 56  ILE A C   
442  O O   . ILE A 56  ? 0.4116 0.3305 0.4577 -0.0251 0.0255  -0.0254 56  ILE A O   
443  C CB  . ILE A 56  ? 0.4139 0.2985 0.4345 -0.0063 0.0117  -0.0210 56  ILE A CB  
444  C CG1 . ILE A 56  ? 0.4194 0.2834 0.4274 0.0001  0.0057  -0.0169 56  ILE A CG1 
445  C CG2 . ILE A 56  ? 0.3803 0.2798 0.4099 0.0002  0.0116  -0.0285 56  ILE A CG2 
446  C CD1 . ILE A 56  ? 0.4756 0.3383 0.4694 0.0073  0.0055  -0.0123 56  ILE A CD1 
447  N N   . GLU A 57  ? 0.3167 0.2412 0.3866 -0.0145 0.0165  -0.0349 57  GLU A N   
448  C CA  . GLU A 57  ? 0.3457 0.2930 0.4340 -0.0151 0.0228  -0.0413 57  GLU A CA  
449  C C   . GLU A 57  ? 0.3797 0.3311 0.4679 -0.0065 0.0249  -0.0478 57  GLU A C   
450  O O   . GLU A 57  ? 0.3015 0.2454 0.3918 0.0006  0.0190  -0.0494 57  GLU A O   
451  C CB  . GLU A 57  ? 0.3837 0.3410 0.4944 -0.0146 0.0184  -0.0437 57  GLU A CB  
452  C CG  . GLU A 57  ? 0.5085 0.4919 0.6426 -0.0152 0.0249  -0.0494 57  GLU A CG  
453  C CD  . GLU A 57  ? 0.6874 0.6804 0.8448 -0.0085 0.0181  -0.0516 57  GLU A CD  
454  O OE1 . GLU A 57  ? 0.7240 0.7054 0.8779 -0.0074 0.0083  -0.0476 57  GLU A OE1 
455  O OE2 . GLU A 57  ? 0.5722 0.5851 0.7512 -0.0035 0.0226  -0.0572 57  GLU A OE2 
456  N N   . MET A 58  ? 0.3827 0.3465 0.4679 -0.0083 0.0336  -0.0521 58  MET A N   
457  C CA  . MET A 58  ? 0.3788 0.3451 0.4614 -0.0020 0.0354  -0.0600 58  MET A CA  
458  C C   . MET A 58  ? 0.3315 0.3176 0.4241 -0.0026 0.0458  -0.0701 58  MET A C   
459  O O   . MET A 58  ? 0.3688 0.3693 0.4693 -0.0080 0.0522  -0.0697 58  MET A O   
460  C CB  . MET A 58  ? 0.3957 0.3531 0.4539 -0.0026 0.0336  -0.0553 58  MET A CB  
461  C CG  . MET A 58  ? 0.4384 0.4041 0.4810 -0.0095 0.0407  -0.0517 58  MET A CG  
462  S SD  . MET A 58  ? 0.6475 0.6015 0.6620 -0.0083 0.0354  -0.0415 58  MET A SD  
463  C CE  . MET A 58  ? 0.5702 0.5012 0.5841 -0.0066 0.0273  -0.0311 58  MET A CE  
464  N N   . GLU A 59  ? 0.3716 0.3590 0.4632 0.0023  0.0479  -0.0800 59  GLU A N   
465  C CA  . GLU A 59  ? 0.3707 0.3751 0.4693 0.0030  0.0585  -0.0928 59  GLU A CA  
466  C C   . GLU A 59  ? 0.3855 0.4036 0.4660 -0.0056 0.0668  -0.0907 59  GLU A C   
467  O O   . GLU A 59  ? 0.4123 0.4245 0.4695 -0.0093 0.0641  -0.0845 59  GLU A O   
468  C CB  . GLU A 59  ? 0.3524 0.3497 0.4481 0.0080  0.0577  -0.1040 59  GLU A CB  
469  C CG  . GLU A 59  ? 0.3637 0.3730 0.4680 0.0110  0.0679  -0.1210 59  GLU A CG  
470  C CD  . GLU A 59  ? 0.4328 0.4325 0.5278 0.0121  0.0664  -0.1318 59  GLU A CD  
471  O OE1 . GLU A 59  ? 0.3878 0.3748 0.4717 0.0104  0.0573  -0.1248 59  GLU A OE1 
472  O OE2 . GLU A 59  ? 0.4371 0.4424 0.5365 0.0143  0.0744  -0.1482 59  GLU A OE2 
473  N N   . PHE A 60  ? 0.4387 0.4775 0.5303 -0.0085 0.0771  -0.0955 60  PHE A N   
474  C CA  . PHE A 60  ? 0.4389 0.4942 0.5126 -0.0169 0.0872  -0.0958 60  PHE A CA  
475  C C   . PHE A 60  ? 0.4606 0.5218 0.5230 -0.0140 0.0921  -0.1104 60  PHE A C   
476  O O   . PHE A 60  ? 0.4254 0.4894 0.5044 -0.0063 0.0956  -0.1258 60  PHE A O   
477  C CB  . PHE A 60  ? 0.4926 0.5728 0.5825 -0.0213 0.0984  -0.0983 60  PHE A CB  
478  C CG  . PHE A 60  ? 0.5934 0.6934 0.6640 -0.0307 0.1103  -0.0987 60  PHE A CG  
479  C CD1 . PHE A 60  ? 0.5998 0.6937 0.6454 -0.0414 0.1087  -0.0823 60  PHE A CD1 
480  C CD2 . PHE A 60  ? 0.6155 0.7388 0.6911 -0.0281 0.1231  -0.1155 60  PHE A CD2 
481  C CE1 . PHE A 60  ? 0.6397 0.7520 0.6651 -0.0507 0.1193  -0.0804 60  PHE A CE1 
482  C CE2 . PHE A 60  ? 0.6313 0.7752 0.6863 -0.0375 0.1346  -0.1159 60  PHE A CE2 
483  C CZ  . PHE A 60  ? 0.6074 0.7464 0.6367 -0.0493 0.1324  -0.0973 60  PHE A CZ  
484  N N   . ILE A 61  ? 0.4864 0.5494 0.5203 -0.0202 0.0923  -0.1059 61  ILE A N   
485  C CA  . ILE A 61  ? 0.4358 0.5044 0.4553 -0.0193 0.0948  -0.1197 61  ILE A CA  
486  C C   . ILE A 61  ? 0.5747 0.6694 0.5822 -0.0259 0.1087  -0.1270 61  ILE A C   
487  O O   . ILE A 61  ? 0.5273 0.6309 0.5130 -0.0346 0.1109  -0.1146 61  ILE A O   
488  C CB  . ILE A 61  ? 0.4887 0.5457 0.4847 -0.0210 0.0840  -0.1107 61  ILE A CB  
489  C CG1 . ILE A 61  ? 0.4741 0.5079 0.4817 -0.0149 0.0716  -0.1030 61  ILE A CG1 
490  C CG2 . ILE A 61  ? 0.4869 0.5525 0.4700 -0.0217 0.0859  -0.1272 61  ILE A CG2 
491  C CD1 . ILE A 61  ? 0.4401 0.4651 0.4717 -0.0074 0.0704  -0.1161 61  ILE A CD1 
492  N N   . GLU A 62  ? 0.5162 0.6230 0.5370 -0.0213 0.1184  -0.1472 62  GLU A N   
493  C CA  . GLU A 62  ? 0.6059 0.7399 0.6152 -0.0268 0.1330  -0.1575 62  GLU A CA  
494  C C   . GLU A 62  ? 0.6007 0.7382 0.5814 -0.0304 0.1323  -0.1677 62  GLU A C   
495  O O   . GLU A 62  ? 0.6198 0.7403 0.5990 -0.0266 0.1228  -0.1739 62  GLU A O   
496  C CB  . GLU A 62  ? 0.6377 0.7850 0.6767 -0.0188 0.1446  -0.1749 62  GLU A CB  
497  C CG  . GLU A 62  ? 0.7184 0.8510 0.7742 -0.0071 0.1430  -0.1948 62  GLU A CG  
498  C CD  . GLU A 62  ? 1.0663 1.2148 1.1514 0.0023  0.1558  -0.2108 62  GLU A CD  
499  O OE1 . GLU A 62  ? 0.9989 1.1616 1.1028 0.0023  0.1589  -0.2006 62  GLU A OE1 
500  O OE2 . GLU A 62  ? 1.1247 1.2717 1.2153 0.0098  0.1624  -0.2335 62  GLU A OE2 
501  N N   . GLY A 63  ? 0.6125 0.7732 0.5684 -0.0396 0.1411  -0.1663 63  GLY A N   
502  C CA  . GLY A 63  ? 0.6448 0.8143 0.5691 -0.0452 0.1397  -0.1731 63  GLY A CA  
503  C C   . GLY A 63  ? 0.6654 0.8476 0.5594 -0.0558 0.1392  -0.1516 63  GLY A C   
504  O O   . GLY A 63  ? 0.6011 0.7828 0.4996 -0.0595 0.1411  -0.1327 63  GLY A O   
505  N N   . ARG A 64  ? 0.6663 0.8592 0.5290 -0.0614 0.1360  -0.1532 64  ARG A N   
506  C CA  . ARG A 64  ? 0.5705 0.7753 0.4027 -0.0707 0.1350  -0.1309 64  ARG A CA  
507  C C   . ARG A 64  ? 0.6671 0.8547 0.4858 -0.0688 0.1168  -0.1125 64  ARG A C   
508  O O   . ARG A 64  ? 0.5655 0.7459 0.3863 -0.0642 0.1071  -0.1235 64  ARG A O   
509  C CB  . ARG A 64  ? 0.6627 0.8994 0.4651 -0.0793 0.1457  -0.1430 64  ARG A CB  
510  C CG  . ARG A 64  ? 0.6593 0.9153 0.4763 -0.0788 0.1647  -0.1674 64  ARG A CG  
511  C CD  . ARG A 64  ? 0.6772 0.9615 0.4666 -0.0858 0.1735  -0.1801 64  ARG A CD  
512  N NE  . ARG A 64  ? 0.7451 1.0476 0.5050 -0.0971 0.1764  -0.1567 64  ARG A NE  
513  C CZ  . ARG A 64  ? 0.7904 1.1129 0.5250 -0.1032 0.1788  -0.1580 64  ARG A CZ  
514  N NH1 . ARG A 64  ? 0.6646 0.9926 0.3980 -0.1002 0.1789  -0.1825 64  ARG A NH1 
515  N NH2 . ARG A 64  ? 0.7392 1.0752 0.4492 -0.1131 0.1815  -0.1338 64  ARG A NH2 
516  N N   . PRO A 65  ? 0.6010 0.7816 0.4071 -0.0720 0.1119  -0.0848 65  PRO A N   
517  C CA  . PRO A 65  ? 0.5951 0.7622 0.3879 -0.0682 0.0951  -0.0673 65  PRO A CA  
518  C C   . PRO A 65  ? 0.6887 0.8789 0.4505 -0.0724 0.0910  -0.0719 65  PRO A C   
519  O O   . PRO A 65  ? 0.6721 0.8878 0.4134 -0.0808 0.1014  -0.0791 65  PRO A O   
520  C CB  . PRO A 65  ? 0.6038 0.7587 0.3882 -0.0715 0.0941  -0.0378 65  PRO A CB  
521  C CG  . PRO A 65  ? 0.6940 0.8684 0.4728 -0.0822 0.1111  -0.0391 65  PRO A CG  
522  C CD  . PRO A 65  ? 0.6737 0.8608 0.4752 -0.0802 0.1222  -0.0686 65  PRO A CD  
523  N N   . ILE A 66  ? 0.6218 0.8056 0.3806 -0.0667 0.0756  -0.0682 66  ILE A N   
524  C CA  . ILE A 66  ? 0.5967 0.8044 0.3300 -0.0706 0.0691  -0.0755 66  ILE A CA  
525  C C   . ILE A 66  ? 0.7019 0.9309 0.3991 -0.0783 0.0710  -0.0575 66  ILE A C   
526  O O   . ILE A 66  ? 0.7293 0.9865 0.4018 -0.0858 0.0734  -0.0692 66  ILE A O   
527  C CB  . ILE A 66  ? 0.6363 0.8356 0.3761 -0.0631 0.0515  -0.0709 66  ILE A CB  
528  C CG1 . ILE A 66  ? 0.6465 0.8731 0.3666 -0.0686 0.0448  -0.0854 66  ILE A CG1 
529  C CG2 . ILE A 66  ? 0.5582 0.7434 0.2931 -0.0560 0.0407  -0.0389 66  ILE A CG2 
530  C CD1 . ILE A 66  ? 0.6229 0.8453 0.3563 -0.0632 0.0298  -0.0882 66  ILE A CD1 
531  N N   . LYS A 67  ? 0.6443 0.8596 0.3363 -0.0775 0.0703  -0.0291 67  LYS A N   
532  C CA  . LYS A 67  ? 0.7592 0.9914 0.4159 -0.0850 0.0715  -0.0078 67  LYS A CA  
533  C C   . LYS A 67  ? 0.7716 1.0308 0.4128 -0.0973 0.0894  -0.0214 67  LYS A C   
534  O O   . LYS A 67  ? 0.7823 1.0649 0.3888 -0.1053 0.0906  -0.0107 67  LYS A O   
535  C CB  . LYS A 67  ? 0.6658 0.8711 0.3234 -0.0824 0.0687  0.0243  67  LYS A CB  
536  C CG  . LYS A 67  ? 0.7988 0.9851 0.4805 -0.0856 0.0814  0.0237  67  LYS A CG  
537  C CD  . LYS A 67  ? 0.8324 1.0080 0.4980 -0.0931 0.0856  0.0535  67  LYS A CD  
538  C CE  . LYS A 67  ? 0.9727 1.1498 0.6523 -0.1037 0.1032  0.0492  67  LYS A CE  
539  N NZ  . LYS A 67  ? 0.9669 1.1813 0.6374 -0.1129 0.1186  0.0283  67  LYS A NZ  
540  N N   . ASP A 68  ? 0.7389 0.9966 0.4047 -0.0984 0.1033  -0.0439 68  ASP A N   
541  C CA  . ASP A 68  ? 0.7964 1.0819 0.4519 -0.1082 0.1220  -0.0605 68  ASP A CA  
542  C C   . ASP A 68  ? 0.7518 1.0575 0.4006 -0.1088 0.1229  -0.0908 68  ASP A C   
543  O O   . ASP A 68  ? 0.7116 1.0348 0.3552 -0.1135 0.1337  -0.1018 68  ASP A O   
544  C CB  . ASP A 68  ? 0.8284 1.1040 0.5186 -0.1067 0.1360  -0.0711 68  ASP A CB  
545  C CG  . ASP A 68  ? 0.9213 1.1833 0.6159 -0.1112 0.1395  -0.0431 68  ASP A CG  
546  O OD1 . ASP A 68  ? 0.8342 1.0936 0.5023 -0.1161 0.1332  -0.0154 68  ASP A OD1 
547  O OD2 . ASP A 68  ? 0.8146 1.0676 0.5398 -0.1099 0.1477  -0.0483 68  ASP A OD2 
548  N N   . VAL A 69  ? 0.7398 1.0387 0.3947 -0.1031 0.1104  -0.1038 69  VAL A N   
549  C CA  . VAL A 69  ? 0.7958 1.1034 0.4556 -0.1031 0.1106  -0.1337 69  VAL A CA  
550  C C   . VAL A 69  ? 0.7616 1.0749 0.4074 -0.1033 0.0926  -0.1337 69  VAL A C   
551  O O   . VAL A 69  ? 0.7097 1.0281 0.3593 -0.1049 0.0909  -0.1576 69  VAL A O   
552  C CB  . VAL A 69  ? 0.7137 1.0037 0.4090 -0.0966 0.1176  -0.1601 69  VAL A CB  
553  C CG1 . VAL A 69  ? 0.7351 1.0233 0.4490 -0.0955 0.1350  -0.1614 69  VAL A CG1 
554  C CG2 . VAL A 69  ? 0.6792 0.9463 0.3912 -0.0897 0.1050  -0.1555 69  VAL A CG2 
555  N N   . ILE A 70  ? 0.7433 1.0558 0.3746 -0.1013 0.0789  -0.1066 70  ILE A N   
556  C CA  . ILE A 70  ? 0.7115 1.0293 0.3379 -0.0992 0.0604  -0.1060 70  ILE A CA  
557  C C   . ILE A 70  ? 0.7980 1.1393 0.4071 -0.1062 0.0572  -0.1179 70  ILE A C   
558  O O   . ILE A 70  ? 0.7262 1.0721 0.3413 -0.1075 0.0481  -0.1345 70  ILE A O   
559  C CB  . ILE A 70  ? 0.7505 1.0652 0.3647 -0.0936 0.0465  -0.0716 70  ILE A CB  
560  C CG1 . ILE A 70  ? 0.7601 1.0840 0.3744 -0.0899 0.0272  -0.0710 70  ILE A CG1 
561  C CG2 . ILE A 70  ? 0.7668 1.0909 0.3542 -0.0972 0.0487  -0.0453 70  ILE A CG2 
562  C CD1 . ILE A 70  ? 0.7326 1.0461 0.3735 -0.0880 0.0244  -0.0958 70  ILE A CD1 
563  N N   . ASN A 71  ? 0.7853 1.1420 0.3729 -0.1119 0.0651  -0.1102 71  ASN A N   
564  C CA  . ASN A 71  ? 0.8973 1.2779 0.4655 -0.1191 0.0624  -0.1209 71  ASN A CA  
565  C C   . ASN A 71  ? 0.8742 1.2564 0.4540 -0.1232 0.0742  -0.1566 71  ASN A C   
566  O O   . ASN A 71  ? 0.8302 1.2302 0.3965 -0.1296 0.0714  -0.1704 71  ASN A O   
567  C CB  . ASN A 71  ? 0.9140 1.3105 0.4531 -0.1236 0.0657  -0.0974 71  ASN A CB  
568  C CG  . ASN A 71  ? 0.8480 1.2422 0.3734 -0.1186 0.0507  -0.0616 71  ASN A CG  
569  O OD1 . ASN A 71  ? 0.8874 1.2684 0.4098 -0.1162 0.0546  -0.0370 71  ASN A OD1 
570  N ND2 . ASN A 71  ? 0.8513 1.2580 0.3698 -0.1170 0.0334  -0.0582 71  ASN A ND2 
571  N N   . GLU A 72  ? 0.8047 1.1684 0.4095 -0.1193 0.0872  -0.1715 72  GLU A N   
572  C CA  . GLU A 72  ? 0.8499 1.2106 0.4691 -0.1205 0.0978  -0.2046 72  GLU A CA  
573  C C   . GLU A 72  ? 0.8469 1.1870 0.4914 -0.1170 0.0909  -0.2240 72  GLU A C   
574  O O   . GLU A 72  ? 0.8019 1.1355 0.4581 -0.1177 0.0974  -0.2509 72  GLU A O   
575  C CB  . GLU A 72  ? 0.7768 1.1319 0.4104 -0.1173 0.1171  -0.2102 72  GLU A CB  
576  C CG  . GLU A 72  ? 0.8329 1.1970 0.4529 -0.1190 0.1235  -0.1821 72  GLU A CG  
577  C CD  . GLU A 72  ? 1.0333 1.4240 0.6184 -0.1275 0.1233  -0.1693 72  GLU A CD  
578  O OE1 . GLU A 72  ? 1.0692 1.4756 0.6430 -0.1322 0.1254  -0.1886 72  GLU A OE1 
579  O OE2 . GLU A 72  ? 0.9898 1.3845 0.5584 -0.1297 0.1212  -0.1394 72  GLU A OE2 
580  N N   . LEU A 73  ? 0.8075 1.1365 0.4602 -0.1131 0.0780  -0.2103 73  LEU A N   
581  C CA  . LEU A 73  ? 0.7644 1.0713 0.4436 -0.1097 0.0724  -0.2254 73  LEU A CA  
582  C C   . LEU A 73  ? 0.7982 1.1135 0.4725 -0.1171 0.0626  -0.2415 73  LEU A C   
583  O O   . LEU A 73  ? 0.8144 1.1526 0.4670 -0.1224 0.0514  -0.2304 73  LEU A O   
584  C CB  . LEU A 73  ? 0.6899 0.9864 0.3768 -0.1039 0.0616  -0.2044 73  LEU A CB  
585  C CG  . LEU A 73  ? 0.7270 1.0062 0.4279 -0.0963 0.0704  -0.1933 73  LEU A CG  
586  C CD1 . LEU A 73  ? 0.7179 0.9823 0.4318 -0.0905 0.0589  -0.1822 73  LEU A CD1 
587  C CD2 . LEU A 73  ? 0.7253 0.9888 0.4498 -0.0931 0.0864  -0.2146 73  LEU A CD2 
588  N N   . ASN A 74  ? 0.8395 1.1359 0.5345 -0.1174 0.0665  -0.2667 74  ASN A N   
589  C CA  . ASN A 74  ? 0.8397 1.1415 0.5313 -0.1261 0.0585  -0.2836 74  ASN A CA  
590  C C   . ASN A 74  ? 0.8471 1.1439 0.5503 -0.1271 0.0425  -0.2759 74  ASN A C   
591  O O   . ASN A 74  ? 0.7347 1.0214 0.4493 -0.1200 0.0385  -0.2596 74  ASN A O   
592  C CB  . ASN A 74  ? 0.8140 1.0960 0.5209 -0.1265 0.0697  -0.3129 74  ASN A CB  
593  C CG  . ASN A 74  ? 0.8922 1.1388 0.6325 -0.1177 0.0737  -0.3183 74  ASN A CG  
594  O OD1 . ASN A 74  ? 0.8038 1.0405 0.5566 -0.1139 0.0660  -0.3039 74  ASN A OD1 
595  N ND2 . ASN A 74  ? 0.9160 1.1437 0.6706 -0.1139 0.0857  -0.3386 74  ASN A ND2 
596  N N   . SER A 75  ? 0.8353 1.1399 0.5360 -0.1364 0.0337  -0.2884 75  SER A N   
597  C CA  . SER A 75  ? 0.7546 1.0602 0.4663 -0.1389 0.0184  -0.2811 75  SER A CA  
598  C C   . SER A 75  ? 0.8095 1.0808 0.5522 -0.1343 0.0207  -0.2878 75  SER A C   
599  O O   . SER A 75  ? 0.7620 1.0311 0.5165 -0.1313 0.0111  -0.2738 75  SER A O   
600  C CB  . SER A 75  ? 0.9229 1.2473 0.6249 -0.1516 0.0094  -0.2937 75  SER A CB  
601  O OG  . SER A 75  ? 1.0838 1.3839 0.8051 -0.1571 0.0117  -0.3161 75  SER A OG  
602  N N   . GLU A 76  ? 0.7515 0.9960 0.5082 -0.1327 0.0331  -0.3075 76  GLU A N   
603  C CA  . GLU A 76  ? 0.8102 1.0200 0.5965 -0.1269 0.0356  -0.3111 76  GLU A CA  
604  C C   . GLU A 76  ? 0.7974 1.0012 0.5924 -0.1159 0.0363  -0.2912 76  GLU A C   
605  O O   . GLU A 76  ? 0.6614 0.8515 0.4739 -0.1133 0.0297  -0.2834 76  GLU A O   
606  C CB  . GLU A 76  ? 0.8728 1.0562 0.6713 -0.1235 0.0495  -0.3322 76  GLU A CB  
607  C CG  . GLU A 76  ? 0.9255 1.0727 0.7512 -0.1227 0.0491  -0.3420 76  GLU A CG  
608  C CD  . GLU A 76  ? 1.0507 1.1756 0.8998 -0.1115 0.0503  -0.3284 76  GLU A CD  
609  O OE1 . GLU A 76  ? 0.9483 1.0676 0.8028 -0.1009 0.0605  -0.3249 76  GLU A OE1 
610  O OE2 . GLU A 76  ? 1.0668 1.1808 0.9295 -0.1139 0.0412  -0.3212 76  GLU A OE2 
611  N N   . THR A 77  ? 0.8028 1.0175 0.5845 -0.1102 0.0444  -0.2824 77  THR A N   
612  C CA  . THR A 77  ? 0.6847 0.8916 0.4738 -0.1004 0.0471  -0.2651 77  THR A CA  
613  C C   . THR A 77  ? 0.7420 0.9657 0.5207 -0.1001 0.0331  -0.2427 77  THR A C   
614  O O   . THR A 77  ? 0.6831 0.8932 0.4764 -0.0939 0.0294  -0.2329 77  THR A O   
615  C CB  . THR A 77  ? 0.7926 1.0080 0.5702 -0.0964 0.0606  -0.2620 77  THR A CB  
616  O OG1 . THR A 77  ? 0.8145 1.0128 0.6080 -0.0935 0.0735  -0.2821 77  THR A OG1 
617  C CG2 . THR A 77  ? 0.6612 0.8715 0.4430 -0.0882 0.0629  -0.2425 77  THR A CG2 
618  N N   . ILE A 78  ? 0.6776 0.9311 0.4318 -0.1058 0.0246  -0.2339 78  ILE A N   
619  C CA  . ILE A 78  ? 0.6758 0.9469 0.4217 -0.1036 0.0096  -0.2113 78  ILE A CA  
620  C C   . ILE A 78  ? 0.6818 0.9450 0.4494 -0.1052 -0.0010 -0.2153 78  ILE A C   
621  O O   . ILE A 78  ? 0.6390 0.9019 0.4140 -0.0986 -0.0090 -0.1995 78  ILE A O   
622  C CB  . ILE A 78  ? 0.7726 1.0771 0.4916 -0.1090 0.0015  -0.2018 78  ILE A CB  
623  C CG1 . ILE A 78  ? 0.7461 1.0586 0.4428 -0.1075 0.0119  -0.1932 78  ILE A CG1 
624  C CG2 . ILE A 78  ? 0.6652 0.9879 0.3810 -0.1045 -0.0156 -0.1782 78  ILE A CG2 
625  C CD1 . ILE A 78  ? 0.7873 1.0916 0.4813 -0.0980 0.0143  -0.1695 78  ILE A CD1 
626  N N   . GLY A 79  ? 0.6184 0.8750 0.3966 -0.1142 -0.0008 -0.2360 79  GLY A N   
627  C CA  . GLY A 79  ? 0.5987 0.8470 0.3985 -0.1177 -0.0095 -0.2394 79  GLY A CA  
628  C C   . GLY A 79  ? 0.6688 0.8870 0.4918 -0.1098 -0.0052 -0.2372 79  GLY A C   
629  O O   . GLY A 79  ? 0.6057 0.8247 0.4419 -0.1082 -0.0144 -0.2278 79  GLY A O   
630  N N   . ARG A 80  ? 0.6590 0.8528 0.4882 -0.1039 0.0087  -0.2448 80  ARG A N   
631  C CA  . ARG A 80  ? 0.6354 0.8004 0.4874 -0.0955 0.0131  -0.2418 80  ARG A CA  
632  C C   . ARG A 80  ? 0.5775 0.7453 0.4325 -0.0832 0.0078  -0.2101 80  ARG A C   
633  O O   . ARG A 80  ? 0.5312 0.6821 0.4077 -0.0767 0.0040  -0.1981 80  ARG A O   
634  C CB  . ARG A 80  ? 0.6272 0.7685 0.4885 -0.0897 0.0288  -0.2531 80  ARG A CB  
635  C CG  . ARG A 80  ? 0.7702 0.8883 0.6479 -0.0939 0.0329  -0.2719 80  ARG A CG  
636  C CD  . ARG A 80  ? 0.8289 0.9376 0.7070 -0.0897 0.0470  -0.2853 80  ARG A CD  
637  N NE  . ARG A 80  ? 0.8416 0.9352 0.7344 -0.0775 0.0565  -0.2796 80  ARG A NE  
638  C CZ  . ARG A 80  ? 0.9012 1.0056 0.7860 -0.0727 0.0673  -0.2801 80  ARG A CZ  
639  N NH1 . ARG A 80  ? 0.8351 0.9632 0.6964 -0.0787 0.0707  -0.2861 80  ARG A NH1 
640  N NH2 . ARG A 80  ? 0.8355 0.9278 0.7371 -0.0622 0.0750  -0.2741 80  ARG A NH2 
641  N N   . ILE A 81  ? 0.5779 0.7661 0.4104 -0.0804 0.0076  -0.1963 81  ILE A N   
642  C CA  . ILE A 81  ? 0.5722 0.7595 0.4063 -0.0689 0.0024  -0.1666 81  ILE A CA  
643  C C   . ILE A 81  ? 0.5612 0.7636 0.3993 -0.0677 -0.0128 -0.1541 81  ILE A C   
644  O O   . ILE A 81  ? 0.4916 0.6816 0.3459 -0.0577 -0.0169 -0.1369 81  ILE A O   
645  C CB  . ILE A 81  ? 0.6159 0.8191 0.4238 -0.0675 0.0061  -0.1539 81  ILE A CB  
646  C CG1 . ILE A 81  ? 0.5580 0.7511 0.3640 -0.0691 0.0225  -0.1670 81  ILE A CG1 
647  C CG2 . ILE A 81  ? 0.5420 0.7377 0.3522 -0.0556 0.0010  -0.1235 81  ILE A CG2 
648  C CD1 . ILE A 81  ? 0.6140 0.8282 0.3904 -0.0720 0.0276  -0.1585 81  ILE A CD1 
649  N N   . LEU A 82  ? 0.5241 0.7557 0.3480 -0.0778 -0.0212 -0.1632 82  LEU A N   
650  C CA  . LEU A 82  ? 0.5130 0.7645 0.3441 -0.0777 -0.0356 -0.1540 82  LEU A CA  
651  C C   . LEU A 82  ? 0.5136 0.7445 0.3745 -0.0777 -0.0359 -0.1589 82  LEU A C   
652  O O   . LEU A 82  ? 0.5407 0.7770 0.4150 -0.0705 -0.0439 -0.1432 82  LEU A O   
653  C CB  . LEU A 82  ? 0.5254 0.8127 0.3383 -0.0918 -0.0441 -0.1680 82  LEU A CB  
654  C CG  . LEU A 82  ? 0.6115 0.9267 0.3912 -0.0931 -0.0464 -0.1613 82  LEU A CG  
655  C CD1 . LEU A 82  ? 0.6052 0.9452 0.3777 -0.1055 -0.0526 -0.1726 82  LEU A CD1 
656  C CD2 . LEU A 82  ? 0.5594 0.8854 0.3341 -0.0781 -0.0550 -0.1285 82  LEU A CD2 
657  N N   . ASP A 83  ? 0.5319 0.7399 0.4033 -0.0857 -0.0273 -0.1805 83  ASP A N   
658  C CA  . ASP A 83  ? 0.5109 0.6964 0.4094 -0.0865 -0.0270 -0.1835 83  ASP A CA  
659  C C   . ASP A 83  ? 0.4493 0.6131 0.3630 -0.0710 -0.0243 -0.1630 83  ASP A C   
660  O O   . ASP A 83  ? 0.4474 0.6075 0.3787 -0.0681 -0.0290 -0.1544 83  ASP A O   
661  C CB  . ASP A 83  ? 0.4478 0.6074 0.3534 -0.0955 -0.0173 -0.2086 83  ASP A CB  
662  C CG  . ASP A 83  ? 0.6451 0.8214 0.5387 -0.1132 -0.0204 -0.2326 83  ASP A CG  
663  O OD1 . ASP A 83  ? 0.5520 0.7606 0.4382 -0.1202 -0.0317 -0.2289 83  ASP A OD1 
664  O OD2 . ASP A 83  ? 0.6534 0.8079 0.5484 -0.1167 -0.0107 -0.2496 83  ASP A OD2 
665  N N   . ILE A 84  ? 0.4369 0.5868 0.3441 -0.0620 -0.0163 -0.1561 84  ILE A N   
666  C CA  . ILE A 84  ? 0.4113 0.5402 0.3322 -0.0489 -0.0141 -0.1383 84  ILE A CA  
667  C C   . ILE A 84  ? 0.4210 0.5657 0.3386 -0.0398 -0.0236 -0.1163 84  ILE A C   
668  O O   . ILE A 84  ? 0.4264 0.5605 0.3592 -0.0320 -0.0259 -0.1055 84  ILE A O   
669  C CB  . ILE A 84  ? 0.4390 0.5518 0.3548 -0.0437 -0.0034 -0.1370 84  ILE A CB  
670  C CG1 . ILE A 84  ? 0.5102 0.6053 0.4357 -0.0492 0.0064  -0.1586 84  ILE A CG1 
671  C CG2 . ILE A 84  ? 0.4649 0.5585 0.3920 -0.0313 -0.0026 -0.1177 84  ILE A CG2 
672  C CD1 . ILE A 84  ? 0.4805 0.5730 0.3971 -0.0474 0.0176  -0.1633 84  ILE A CD1 
673  N N   . CYS A 85  ? 0.4460 0.6161 0.3430 -0.0395 -0.0291 -0.1092 85  CYS A N   
674  C CA  . CYS A 85  ? 0.4763 0.6620 0.3713 -0.0290 -0.0390 -0.0883 85  CYS A CA  
675  C C   . CYS A 85  ? 0.4748 0.6757 0.3868 -0.0308 -0.0472 -0.0902 85  CYS A C   
676  O O   . CYS A 85  ? 0.4146 0.6144 0.3382 -0.0196 -0.0511 -0.0759 85  CYS A O   
677  C CB  . CYS A 85  ? 0.4350 0.6486 0.3046 -0.0295 -0.0450 -0.0807 85  CYS A CB  
678  S SG  . CYS A 85  ? 0.5552 0.7553 0.4023 -0.0281 -0.0350 -0.0740 85  CYS A SG  
679  N N   . ARG A 86  ? 0.4477 0.6645 0.3608 -0.0456 -0.0497 -0.1083 86  ARG A N   
680  C CA  . ARG A 86  ? 0.4311 0.6646 0.3616 -0.0510 -0.0567 -0.1113 86  ARG A CA  
681  C C   . ARG A 86  ? 0.4422 0.6476 0.3952 -0.0477 -0.0511 -0.1101 86  ARG A C   
682  O O   . ARG A 86  ? 0.4152 0.6304 0.3824 -0.0420 -0.0555 -0.1001 86  ARG A O   
683  C CB  . ARG A 86  ? 0.5099 0.7603 0.4359 -0.0707 -0.0592 -0.1334 86  ARG A CB  
684  C CG  . ARG A 86  ? 0.5121 0.7753 0.4579 -0.0816 -0.0644 -0.1402 86  ARG A CG  
685  C CD  . ARG A 86  ? 0.5224 0.8216 0.4757 -0.0737 -0.0754 -0.1236 86  ARG A CD  
686  N NE  . ARG A 86  ? 0.5450 0.8594 0.5185 -0.0861 -0.0792 -0.1304 86  ARG A NE  
687  C CZ  . ARG A 86  ? 0.5808 0.9223 0.5699 -0.0798 -0.0857 -0.1179 86  ARG A CZ  
688  N NH1 . ARG A 86  ? 0.5748 0.9309 0.5618 -0.0598 -0.0901 -0.0984 86  ARG A NH1 
689  N NH2 . ARG A 86  ? 0.5817 0.9351 0.5897 -0.0938 -0.0872 -0.1250 86  ARG A NH2 
690  N N   . LYS A 87  ? 0.4465 0.6187 0.4027 -0.0504 -0.0411 -0.1195 87  LYS A N   
691  C CA  . LYS A 87  ? 0.4075 0.5529 0.3831 -0.0470 -0.0363 -0.1169 87  LYS A CA  
692  C C   . LYS A 87  ? 0.4353 0.5768 0.4150 -0.0305 -0.0376 -0.0967 87  LYS A C   
693  O O   . LYS A 87  ? 0.4393 0.5801 0.4337 -0.0275 -0.0390 -0.0908 87  LYS A O   
694  C CB  . LYS A 87  ? 0.4494 0.5622 0.4265 -0.0489 -0.0261 -0.1276 87  LYS A CB  
695  C CG  . LYS A 87  ? 0.5038 0.5889 0.5005 -0.0479 -0.0219 -0.1270 87  LYS A CG  
696  C CD  . LYS A 87  ? 0.5505 0.6451 0.5605 -0.0567 -0.0269 -0.1281 87  LYS A CD  
697  C CE  . LYS A 87  ? 0.6520 0.7163 0.6772 -0.0618 -0.0217 -0.1336 87  LYS A CE  
698  N NZ  . LYS A 87  ? 0.8474 0.9149 0.8796 -0.0792 -0.0239 -0.1463 87  LYS A NZ  
699  N N   . LEU A 88  ? 0.4665 0.6045 0.4324 -0.0203 -0.0365 -0.0864 88  LEU A N   
700  C CA  . LEU A 88  ? 0.4490 0.5794 0.4171 -0.0047 -0.0377 -0.0684 88  LEU A CA  
701  C C   . LEU A 88  ? 0.4497 0.6089 0.4219 0.0017  -0.0468 -0.0590 88  LEU A C   
702  O O   . LEU A 88  ? 0.4337 0.5888 0.4166 0.0119  -0.0474 -0.0498 88  LEU A O   
703  C CB  . LEU A 88  ? 0.4331 0.5529 0.3845 0.0024  -0.0349 -0.0593 88  LEU A CB  
704  C CG  . LEU A 88  ? 0.4156 0.5074 0.3662 0.0000  -0.0250 -0.0646 88  LEU A CG  
705  C CD1 . LEU A 88  ? 0.4909 0.5802 0.4233 0.0038  -0.0228 -0.0549 88  LEU A CD1 
706  C CD2 . LEU A 88  ? 0.4017 0.4684 0.3673 0.0065  -0.0217 -0.0599 88  LEU A CD2 
707  N N   . ASP A 89  ? 0.4164 0.6073 0.3802 -0.0037 -0.0540 -0.0614 89  ASP A N   
708  C CA  . ASP A 89  ? 0.4657 0.6903 0.4374 0.0013  -0.0633 -0.0540 89  ASP A CA  
709  C C   . ASP A 89  ? 0.4542 0.6826 0.4477 -0.0044 -0.0622 -0.0598 89  ASP A C   
710  O O   . ASP A 89  ? 0.4200 0.6618 0.4254 0.0060  -0.0649 -0.0503 89  ASP A O   
711  C CB  . ASP A 89  ? 0.4340 0.6956 0.3947 -0.0076 -0.0719 -0.0588 89  ASP A CB  
712  C CG  . ASP A 89  ? 0.4981 0.7663 0.4364 0.0013  -0.0759 -0.0466 89  ASP A CG  
713  O OD1 . ASP A 89  ? 0.4843 0.7248 0.4150 0.0123  -0.0707 -0.0356 89  ASP A OD1 
714  O OD2 . ASP A 89  ? 0.4970 0.7991 0.4244 -0.0043 -0.0844 -0.0479 89  ASP A OD2 
715  N N   . VAL A 90  ? 0.4499 0.6679 0.4487 -0.0212 -0.0580 -0.0755 90  VAL A N   
716  C CA  . VAL A 90  ? 0.4884 0.7114 0.5065 -0.0300 -0.0573 -0.0802 90  VAL A CA  
717  C C   . VAL A 90  ? 0.4557 0.6521 0.4835 -0.0198 -0.0508 -0.0719 90  VAL A C   
718  O O   . VAL A 90  ? 0.4495 0.6585 0.4911 -0.0173 -0.0514 -0.0666 90  VAL A O   
719  C CB  . VAL A 90  ? 0.4234 0.6372 0.4430 -0.0510 -0.0548 -0.0988 90  VAL A CB  
720  C CG1 . VAL A 90  ? 0.5108 0.7101 0.5482 -0.0593 -0.0505 -0.1014 90  VAL A CG1 
721  C CG2 . VAL A 90  ? 0.4994 0.7501 0.5142 -0.0640 -0.0631 -0.1079 90  VAL A CG2 
722  N N   . LEU A 91  ? 0.3951 0.5573 0.4154 -0.0139 -0.0447 -0.0707 91  LEU A N   
723  C CA  . LEU A 91  ? 0.4056 0.5428 0.4323 -0.0046 -0.0394 -0.0634 91  LEU A CA  
724  C C   . LEU A 91  ? 0.4283 0.5745 0.4546 0.0131  -0.0419 -0.0495 91  LEU A C   
725  O O   . LEU A 91  ? 0.4137 0.5441 0.4455 0.0206  -0.0381 -0.0444 91  LEU A O   
726  C CB  . LEU A 91  ? 0.3494 0.4532 0.3686 -0.0036 -0.0333 -0.0662 91  LEU A CB  
727  C CG  . LEU A 91  ? 0.4164 0.5063 0.4392 -0.0180 -0.0294 -0.0805 91  LEU A CG  
728  C CD1 . LEU A 91  ? 0.4926 0.5570 0.5085 -0.0153 -0.0234 -0.0836 91  LEU A CD1 
729  C CD2 . LEU A 91  ? 0.4859 0.5652 0.5241 -0.0238 -0.0274 -0.0813 91  LEU A CD2 
730  N N   . GLY A 92  ? 0.3952 0.5654 0.4145 0.0205  -0.0482 -0.0434 92  GLY A N   
731  C CA  . GLY A 92  ? 0.4094 0.5844 0.4285 0.0394  -0.0505 -0.0303 92  GLY A CA  
732  C C   . GLY A 92  ? 0.4780 0.6213 0.4842 0.0506  -0.0474 -0.0225 92  GLY A C   
733  O O   . GLY A 92  ? 0.4172 0.5522 0.4246 0.0659  -0.0470 -0.0136 92  GLY A O   
734  N N   . ILE A 93  ? 0.3978 0.5232 0.3920 0.0431  -0.0446 -0.0262 93  ILE A N   
735  C CA  . ILE A 93  ? 0.4060 0.5023 0.3886 0.0505  -0.0410 -0.0189 93  ILE A CA  
736  C C   . ILE A 93  ? 0.4348 0.5411 0.4005 0.0527  -0.0451 -0.0117 93  ILE A C   
737  O O   . ILE A 93  ? 0.4080 0.5237 0.3655 0.0411  -0.0449 -0.0191 93  ILE A O   
738  C CB  . ILE A 93  ? 0.3953 0.4649 0.3789 0.0409  -0.0335 -0.0274 93  ILE A CB  
739  C CG1 . ILE A 93  ? 0.3232 0.3810 0.3212 0.0404  -0.0303 -0.0310 93  ILE A CG1 
740  C CG2 . ILE A 93  ? 0.4016 0.4468 0.3733 0.0452  -0.0299 -0.0203 93  ILE A CG2 
741  C CD1 . ILE A 93  ? 0.3499 0.3891 0.3524 0.0298  -0.0247 -0.0404 93  ILE A CD1 
742  N N   . GLN A 94  ? 0.3532 0.4559 0.3126 0.0678  -0.0486 0.0027  94  GLN A N   
743  C CA  . GLN A 94  ? 0.4312 0.5375 0.3722 0.0715  -0.0525 0.0140  94  GLN A CA  
744  C C   . GLN A 94  ? 0.4712 0.5426 0.4008 0.0696  -0.0455 0.0182  94  GLN A C   
745  O O   . GLN A 94  ? 0.4488 0.4940 0.3791 0.0794  -0.0435 0.0262  94  GLN A O   
746  C CB  . GLN A 94  ? 0.4272 0.5454 0.3683 0.0899  -0.0602 0.0290  94  GLN A CB  
747  C CG  . GLN A 94  ? 0.4689 0.5889 0.3895 0.0952  -0.0652 0.0445  94  GLN A CG  
748  C CD  . GLN A 94  ? 0.5973 0.7473 0.5200 0.1100  -0.0760 0.0563  94  GLN A CD  
749  O OE1 . GLN A 94  ? 0.5461 0.7352 0.4746 0.1049  -0.0823 0.0505  94  GLN A OE1 
750  N NE2 . GLN A 94  ? 0.6466 0.7788 0.5657 0.1288  -0.0786 0.0729  94  GLN A NE2 
751  N N   . LYS A 95  ? 0.4833 0.5554 0.4027 0.0563  -0.0414 0.0119  95  LYS A N   
752  C CA  . LYS A 95  ? 0.4726 0.5166 0.3840 0.0521  -0.0337 0.0145  95  LYS A CA  
753  C C   . LYS A 95  ? 0.5627 0.5942 0.4574 0.0603  -0.0358 0.0336  95  LYS A C   
754  O O   . LYS A 95  ? 0.5451 0.5473 0.4374 0.0606  -0.0307 0.0393  95  LYS A O   
755  C CB  . LYS A 95  ? 0.4741 0.5263 0.3802 0.0369  -0.0278 0.0018  95  LYS A CB  
756  C CG  . LYS A 95  ? 0.4418 0.4711 0.3447 0.0309  -0.0186 0.0016  95  LYS A CG  
757  C CD  . LYS A 95  ? 0.5475 0.5885 0.4490 0.0177  -0.0119 -0.0145 95  LYS A CD  
758  C CE  . LYS A 95  ? 0.4452 0.4702 0.3458 0.0117  -0.0019 -0.0154 95  LYS A CE  
759  N NZ  . LYS A 95  ? 0.4541 0.4767 0.3341 0.0114  -0.0008 0.0011  95  LYS A NZ  
760  N N   . GLU A 96  ? 0.4649 0.5180 0.3483 0.0663  -0.0438 0.0442  96  GLU A N   
761  C CA  . GLU A 96  ? 0.5834 0.6280 0.4487 0.0746  -0.0476 0.0651  96  GLU A CA  
762  C C   . GLU A 96  ? 0.6687 0.7118 0.5135 0.0617  -0.0422 0.0687  96  GLU A C   
763  O O   . GLU A 96  ? 0.6292 0.6681 0.4765 0.0484  -0.0333 0.0553  96  GLU A O   
764  C CB  . GLU A 96  ? 0.6143 0.6223 0.4839 0.0871  -0.0463 0.0758  96  GLU A CB  
765  C CG  . GLU A 96  ? 0.6024 0.6127 0.4892 0.1031  -0.0514 0.0747  96  GLU A CG  
766  C CD  . GLU A 96  ? 0.7961 0.8330 0.6812 0.1180  -0.0621 0.0865  96  GLU A CD  
767  O OE1 . GLU A 96  ? 0.7084 0.7685 0.5791 0.1143  -0.0674 0.0939  96  GLU A OE1 
768  O OE2 . GLU A 96  ? 0.7090 0.7455 0.6076 0.1340  -0.0653 0.0883  96  GLU A OE2 
769  N N   . GLU A 97  ? 0.7040 0.7523 0.5286 0.0660  -0.0474 0.0874  97  GLU A N   
770  C CA  . GLU A 97  ? 0.7442 0.7941 0.5459 0.0539  -0.0422 0.0940  97  GLU A CA  
771  C C   . GLU A 97  ? 0.6946 0.7761 0.4914 0.0387  -0.0388 0.0753  97  GLU A C   
772  O O   . GLU A 97  ? 0.7267 0.8087 0.5106 0.0260  -0.0301 0.0724  97  GLU A O   
773  C CB  . GLU A 97  ? 0.8267 0.8407 0.6278 0.0473  -0.0316 0.0974  97  GLU A CB  
774  C CG  . GLU A 97  ? 0.9772 0.9555 0.7760 0.0590  -0.0341 0.1174  97  GLU A CG  
775  C CD  . GLU A 97  ? 1.2557 1.2041 1.0486 0.0477  -0.0239 0.1227  97  GLU A CD  
776  O OE1 . GLU A 97  ? 1.2504 1.2096 1.0435 0.0322  -0.0148 0.1104  97  GLU A OE1 
777  O OE2 . GLU A 97  ? 1.3694 1.2837 1.1586 0.0540  -0.0248 0.1385  97  GLU A OE2 
778  N N   . MET A 98  ? 0.6751 0.7836 0.4824 0.0393  -0.0450 0.0618  98  MET A N   
779  C CA  . MET A 98  ? 0.6094 0.7446 0.4126 0.0247  -0.0420 0.0416  98  MET A CA  
780  C C   . MET A 98  ? 0.7189 0.8828 0.4938 0.0194  -0.0466 0.0495  98  MET A C   
781  O O   . MET A 98  ? 0.6175 0.8017 0.3824 0.0058  -0.0423 0.0332  98  MET A O   
782  C CB  . MET A 98  ? 0.5947 0.7472 0.4181 0.0254  -0.0476 0.0256  98  MET A CB  
783  C CG  . MET A 98  ? 0.6402 0.7752 0.4864 0.0199  -0.0393 0.0063  98  MET A CG  
784  S SD  . MET A 98  ? 0.6428 0.7569 0.4866 0.0083  -0.0240 -0.0049 98  MET A SD  
785  C CE  . MET A 98  ? 0.6955 0.8398 0.5318 -0.0064 -0.0226 -0.0284 98  MET A CE  
786  N N   . ASN A 99  ? 0.6074 0.7728 0.3684 0.0303  -0.0553 0.0743  99  ASN A N   
787  C CA  . ASN A 99  ? 0.7164 0.9053 0.4471 0.0259  -0.0596 0.0871  99  ASN A CA  
788  C C   . ASN A 99  ? 0.6902 0.8590 0.4018 0.0178  -0.0484 0.0975  99  ASN A C   
789  O O   . ASN A 99  ? 0.7480 0.9355 0.4316 0.0114  -0.0495 0.1078  99  ASN A O   
790  C CB  . ASN A 99  ? 0.7396 0.9385 0.4643 0.0426  -0.0746 0.1118  99  ASN A CB  
791  C CG  . ASN A 99  ? 0.7622 0.9199 0.4953 0.0580  -0.0740 0.1318  99  ASN A CG  
792  O OD1 . ASN A 99  ? 0.8008 0.9333 0.5574 0.0622  -0.0689 0.1225  99  ASN A OD1 
793  N ND2 . ASN A 99  ? 0.8842 1.0339 0.5973 0.0661  -0.0794 0.1594  99  ASN A ND2 
794  N N   . HIS A 100 ? 0.7178 0.8510 0.4436 0.0171  -0.0380 0.0957  100 HIS A N   
795  C CA  . HIS A 100 ? 0.7779 0.8951 0.4909 0.0059  -0.0252 0.1006  100 HIS A CA  
796  C C   . HIS A 100 ? 0.7181 0.8241 0.4524 -0.0027 -0.0126 0.0766  100 HIS A C   
797  O O   . HIS A 100 ? 0.6780 0.7534 0.4254 -0.0020 -0.0062 0.0801  100 HIS A O   
798  C CB  . HIS A 100 ? 0.7864 0.8690 0.4940 0.0140  -0.0265 0.1281  100 HIS A CB  
799  C CG  . HIS A 100 ? 0.8602 0.9515 0.5458 0.0236  -0.0386 0.1542  100 HIS A CG  
800  N ND1 . HIS A 100 ? 0.9277 0.9911 0.6167 0.0400  -0.0465 0.1762  100 HIS A ND1 
801  C CD2 . HIS A 100 ? 0.8712 0.9958 0.5302 0.0195  -0.0443 0.1625  100 HIS A CD2 
802  C CE1 . HIS A 100 ? 0.8803 0.9595 0.5476 0.0471  -0.0572 0.1981  100 HIS A CE1 
803  N NE2 . HIS A 100 ? 0.9162 1.0338 0.5643 0.0342  -0.0564 0.1908  100 HIS A NE2 
804  N N   . PRO A 101 ? 0.7278 0.8576 0.4672 -0.0105 -0.0096 0.0518  101 PRO A N   
805  C CA  . PRO A 101 ? 0.5808 0.6999 0.3427 -0.0163 0.0011  0.0293  101 PRO A CA  
806  C C   . PRO A 101 ? 0.6107 0.7322 0.3640 -0.0286 0.0159  0.0236  101 PRO A C   
807  O O   . PRO A 101 ? 0.5410 0.6617 0.3113 -0.0334 0.0250  0.0026  101 PRO A O   
808  C CB  . PRO A 101 ? 0.5912 0.7338 0.3603 -0.0188 -0.0030 0.0063  101 PRO A CB  
809  C CG  . PRO A 101 ? 0.6453 0.8206 0.3844 -0.0241 -0.0082 0.0110  101 PRO A CG  
810  C CD  . PRO A 101 ? 0.7029 0.8702 0.4274 -0.0148 -0.0164 0.0425  101 PRO A CD  
811  N N   . ASP A 102 ? 0.6645 0.7901 0.3925 -0.0333 0.0184  0.0428  102 ASP A N   
812  C CA  . ASP A 102 ? 0.6511 0.7906 0.3644 -0.0467 0.0324  0.0382  102 ASP A CA  
813  C C   . ASP A 102 ? 0.6271 0.7529 0.3645 -0.0512 0.0457  0.0243  102 ASP A C   
814  O O   . ASP A 102 ? 0.6816 0.8254 0.4203 -0.0592 0.0573  0.0047  102 ASP A O   
815  C CB  . ASP A 102 ? 0.7915 0.9275 0.4777 -0.0502 0.0325  0.0674  102 ASP A CB  
816  C CG  . ASP A 102 ? 0.8513 1.0031 0.5130 -0.0444 0.0184  0.0838  102 ASP A CG  
817  O OD1 . ASP A 102 ? 0.8522 0.9917 0.5242 -0.0309 0.0052  0.0922  102 ASP A OD1 
818  O OD2 . ASP A 102 ? 0.8723 1.0509 0.5048 -0.0530 0.0205  0.0881  102 ASP A OD2 
819  N N   . ARG A 103 ? 0.6249 0.7202 0.3814 -0.0458 0.0443  0.0339  103 ARG A N   
820  C CA  . ARG A 103 ? 0.6548 0.7378 0.4352 -0.0497 0.0548  0.0237  103 ARG A CA  
821  C C   . ARG A 103 ? 0.5865 0.6570 0.3967 -0.0413 0.0507  0.0072  103 ARG A C   
822  O O   . ARG A 103 ? 0.5736 0.6335 0.4055 -0.0428 0.0572  0.0002  103 ARG A O   
823  C CB  . ARG A 103 ? 0.7313 0.7893 0.5108 -0.0528 0.0570  0.0458  103 ARG A CB  
824  C CG  . ARG A 103 ? 0.8483 0.9112 0.5961 -0.0596 0.0580  0.0690  103 ARG A CG  
825  C CD  . ARG A 103 ? 0.9131 0.9485 0.6609 -0.0656 0.0617  0.0896  103 ARG A CD  
826  N NE  . ARG A 103 ? 1.1914 1.2051 0.9201 -0.0592 0.0509  0.1161  103 ARG A NE  
827  C CZ  . ARG A 103 ? 1.2409 1.2665 0.9391 -0.0615 0.0484  0.1340  103 ARG A CZ  
828  N NH1 . ARG A 103 ? 1.1376 1.1987 0.8179 -0.0712 0.0559  0.1273  103 ARG A NH1 
829  N NH2 . ARG A 103 ? 1.1974 1.1991 0.8821 -0.0531 0.0379  0.1591  103 ARG A NH2 
830  N N   . HIS A 104 ? 0.5775 0.6513 0.3896 -0.0333 0.0399  0.0015  104 HIS A N   
831  C CA  . HIS A 104 ? 0.5249 0.5843 0.3630 -0.0254 0.0347  -0.0090 104 HIS A CA  
832  C C   . HIS A 104 ? 0.5557 0.6305 0.4033 -0.0263 0.0349  -0.0328 104 HIS A C   
833  O O   . HIS A 104 ? 0.5206 0.5846 0.3883 -0.0208 0.0305  -0.0407 104 HIS A O   
834  C CB  . HIS A 104 ? 0.5710 0.6167 0.4081 -0.0146 0.0217  0.0064  104 HIS A CB  
835  C CG  . HIS A 104 ? 0.5975 0.6197 0.4283 -0.0121 0.0208  0.0284  104 HIS A CG  
836  N ND1 . HIS A 104 ? 0.7268 0.7349 0.5626 -0.0194 0.0300  0.0317  104 HIS A ND1 
837  C CD2 . HIS A 104 ? 0.6753 0.6847 0.4957 -0.0034 0.0119  0.0480  104 HIS A CD2 
838  C CE1 . HIS A 104 ? 0.6804 0.6655 0.5082 -0.0168 0.0267  0.0519  104 HIS A CE1 
839  N NE2 . HIS A 104 ? 0.7931 0.7769 0.6112 -0.0061 0.0159  0.0621  104 HIS A NE2 
840  N N   . ILE A 105 ? 0.5677 0.6665 0.3999 -0.0336 0.0398  -0.0443 105 ILE A N   
841  C CA  . ILE A 105 ? 0.5514 0.6613 0.3923 -0.0364 0.0427  -0.0700 105 ILE A CA  
842  C C   . ILE A 105 ? 0.5110 0.6302 0.3524 -0.0430 0.0579  -0.0835 105 ILE A C   
843  O O   . ILE A 105 ? 0.5371 0.6743 0.3560 -0.0498 0.0640  -0.0795 105 ILE A O   
844  C CB  . ILE A 105 ? 0.5406 0.6730 0.3624 -0.0396 0.0348  -0.0757 105 ILE A CB  
845  C CG1 . ILE A 105 ? 0.5620 0.6908 0.3848 -0.0319 0.0198  -0.0606 105 ILE A CG1 
846  C CG2 . ILE A 105 ? 0.5155 0.6545 0.3465 -0.0441 0.0385  -0.1039 105 ILE A CG2 
847  C CD1 . ILE A 105 ? 0.5456 0.7021 0.3507 -0.0355 0.0102  -0.0646 105 ILE A CD1 
848  N N   . ILE A 106 ? 0.5169 0.6251 0.3842 -0.0405 0.0642  -0.0981 106 ILE A N   
849  C CA  . ILE A 106 ? 0.5474 0.6648 0.4215 -0.0440 0.0792  -0.1115 106 ILE A CA  
850  C C   . ILE A 106 ? 0.5642 0.6892 0.4430 -0.0446 0.0834  -0.1392 106 ILE A C   
851  O O   . ILE A 106 ? 0.5328 0.6425 0.4290 -0.0400 0.0775  -0.1486 106 ILE A O   
852  C CB  . ILE A 106 ? 0.5502 0.6510 0.4522 -0.0394 0.0831  -0.1073 106 ILE A CB  
853  C CG1 . ILE A 106 ? 0.5229 0.6086 0.4217 -0.0385 0.0759  -0.0816 106 ILE A CG1 
854  C CG2 . ILE A 106 ? 0.5538 0.6707 0.4618 -0.0432 0.0988  -0.1169 106 ILE A CG2 
855  C CD1 . ILE A 106 ? 0.5207 0.6179 0.3939 -0.0463 0.0799  -0.0652 106 ILE A CD1 
856  N N   . ILE A 107 ? 0.6146 0.7618 0.4773 -0.0509 0.0942  -0.1525 107 ILE A N   
857  C CA  . ILE A 107 ? 0.6578 0.8128 0.5177 -0.0530 0.0981  -0.1803 107 ILE A CA  
858  C C   . ILE A 107 ? 0.6976 0.8583 0.5726 -0.0509 0.1148  -0.1996 107 ILE A C   
859  O O   . ILE A 107 ? 0.6353 0.8155 0.5006 -0.0548 0.1264  -0.1966 107 ILE A O   
860  C CB  . ILE A 107 ? 0.6170 0.7962 0.4414 -0.0621 0.0950  -0.1827 107 ILE A CB  
861  C CG1 . ILE A 107 ? 0.6420 0.8163 0.4578 -0.0614 0.0773  -0.1634 107 ILE A CG1 
862  C CG2 . ILE A 107 ? 0.6516 0.8386 0.4717 -0.0662 0.1001  -0.2145 107 ILE A CG2 
863  C CD1 . ILE A 107 ? 0.6750 0.8748 0.4558 -0.0687 0.0714  -0.1552 107 ILE A CD1 
864  N N   . SER A 108 ? 0.7173 0.8610 0.6173 -0.0442 0.1161  -0.2182 108 SER A N   
865  C CA  . SER A 108 ? 0.7001 0.8477 0.6167 -0.0394 0.1312  -0.2408 108 SER A CA  
866  C C   . SER A 108 ? 0.6996 0.8342 0.6190 -0.0389 0.1272  -0.2611 108 SER A C   
867  O O   . SER A 108 ? 0.7276 0.8702 0.6230 -0.0473 0.1208  -0.2644 108 SER A O   
868  C CB  . SER A 108 ? 0.6852 0.8175 0.6372 -0.0291 0.1329  -0.2333 108 SER A CB  
869  O OG  . SER A 108 ? 0.6538 0.7580 0.6227 -0.0238 0.1201  -0.2284 108 SER A OG  
870  N N   . ASP A 109 ? 0.7327 0.8462 0.6815 -0.0294 0.1286  -0.2710 109 ASP A N   
871  C CA  . ASP A 109 ? 0.7150 0.8081 0.6678 -0.0300 0.1213  -0.2836 109 ASP A CA  
872  C C   . ASP A 109 ? 0.7912 0.8691 0.7422 -0.0339 0.1071  -0.2747 109 ASP A C   
873  O O   . ASP A 109 ? 0.7830 0.8516 0.7287 -0.0396 0.0998  -0.2826 109 ASP A O   
874  C CB  . ASP A 109 ? 0.7608 0.8324 0.7437 -0.0184 0.1255  -0.2925 109 ASP A CB  
875  N N   . ARG A 110 ? 0.6029 0.6790 0.5587 -0.0315 0.1036  -0.2588 110 ARG A N   
876  C CA  . ARG A 110 ? 0.6100 0.6741 0.5654 -0.0340 0.0896  -0.2461 110 ARG A CA  
877  C C   . ARG A 110 ? 0.6607 0.7427 0.5952 -0.0381 0.0830  -0.2224 110 ARG A C   
878  O O   . ARG A 110 ? 0.6453 0.7468 0.5653 -0.0401 0.0902  -0.2169 110 ARG A O   
879  C CB  . ARG A 110 ? 0.6318 0.6703 0.6175 -0.0244 0.0856  -0.2359 110 ARG A CB  
880  C CG  . ARG A 110 ? 0.5778 0.6208 0.5774 -0.0167 0.0919  -0.2234 110 ARG A CG  
881  C CD  . ARG A 110 ? 0.5648 0.5871 0.5875 -0.0094 0.0838  -0.2073 110 ARG A CD  
882  N NE  . ARG A 110 ? 0.6248 0.6538 0.6602 -0.0040 0.0887  -0.1958 110 ARG A NE  
883  C CZ  . ARG A 110 ? 0.6305 0.6480 0.6816 0.0009  0.0820  -0.1795 110 ARG A CZ  
884  N NH1 . ARG A 110 ? 0.6214 0.6206 0.6763 0.0018  0.0709  -0.1716 110 ARG A NH1 
885  N NH2 . ARG A 110 ? 0.5767 0.6031 0.6398 0.0040  0.0869  -0.1717 110 ARG A NH2 
886  N N   . ILE A 111 ? 0.5539 0.6294 0.4868 -0.0394 0.0695  -0.2083 111 ILE A N   
887  C CA  . ILE A 111 ? 0.5233 0.6120 0.4381 -0.0412 0.0613  -0.1857 111 ILE A CA  
888  C C   . ILE A 111 ? 0.4794 0.5494 0.4122 -0.0336 0.0546  -0.1658 111 ILE A C   
889  O O   . ILE A 111 ? 0.4781 0.5325 0.4266 -0.0314 0.0481  -0.1673 111 ILE A O   
890  C CB  . ILE A 111 ? 0.5416 0.6439 0.4380 -0.0487 0.0507  -0.1878 111 ILE A CB  
891  C CG1 . ILE A 111 ? 0.6189 0.7396 0.4958 -0.0579 0.0564  -0.2107 111 ILE A CG1 
892  C CG2 . ILE A 111 ? 0.5266 0.6419 0.4062 -0.0475 0.0417  -0.1624 111 ILE A CG2 
893  C CD1 . ILE A 111 ? 0.7604 0.9001 0.6185 -0.0597 0.0674  -0.2109 111 ILE A CD1 
894  N N   . VAL A 112 ? 0.4586 0.5298 0.3889 -0.0304 0.0564  -0.1477 112 VAL A N   
895  C CA  . VAL A 112 ? 0.4382 0.4919 0.3828 -0.0238 0.0501  -0.1299 112 VAL A CA  
896  C C   . VAL A 112 ? 0.4394 0.4985 0.3658 -0.0236 0.0432  -0.1084 112 VAL A C   
897  O O   . VAL A 112 ? 0.4898 0.5613 0.3981 -0.0273 0.0476  -0.1014 112 VAL A O   
898  C CB  . VAL A 112 ? 0.4154 0.4600 0.3792 -0.0197 0.0583  -0.1289 112 VAL A CB  
899  C CG1 . VAL A 112 ? 0.4163 0.4428 0.3939 -0.0140 0.0509  -0.1130 112 VAL A CG1 
900  C CG2 . VAL A 112 ? 0.4533 0.4934 0.4357 -0.0176 0.0654  -0.1500 112 VAL A CG2 
901  N N   . PHE A 113 ? 0.3973 0.4467 0.3283 -0.0189 0.0328  -0.0976 113 PHE A N   
902  C CA  . PHE A 113 ? 0.4210 0.4692 0.3400 -0.0151 0.0261  -0.0765 113 PHE A CA  
903  C C   . PHE A 113 ? 0.4258 0.4536 0.3570 -0.0104 0.0277  -0.0648 113 PHE A C   
904  O O   . PHE A 113 ? 0.4006 0.4147 0.3519 -0.0073 0.0276  -0.0695 113 PHE A O   
905  C CB  . PHE A 113 ? 0.4049 0.4563 0.3238 -0.0113 0.0146  -0.0724 113 PHE A CB  
906  C CG  . PHE A 113 ? 0.5074 0.5832 0.4095 -0.0165 0.0101  -0.0781 113 PHE A CG  
907  C CD1 . PHE A 113 ? 0.4481 0.5377 0.3411 -0.0252 0.0165  -0.0949 113 PHE A CD1 
908  C CD2 . PHE A 113 ? 0.5127 0.5995 0.4092 -0.0125 -0.0009 -0.0680 113 PHE A CD2 
909  C CE1 . PHE A 113 ? 0.5029 0.6164 0.3791 -0.0313 0.0114  -0.1013 113 PHE A CE1 
910  C CE2 . PHE A 113 ? 0.5279 0.6410 0.4097 -0.0179 -0.0065 -0.0728 113 PHE A CE2 
911  C CZ  . PHE A 113 ? 0.4781 0.6043 0.3487 -0.0282 -0.0007 -0.0897 113 PHE A CZ  
912  N N   . ILE A 114 ? 0.4262 0.4512 0.3444 -0.0107 0.0287  -0.0491 114 ILE A N   
913  C CA  . ILE A 114 ? 0.4471 0.4518 0.3749 -0.0082 0.0295  -0.0384 114 ILE A CA  
914  C C   . ILE A 114 ? 0.4856 0.4794 0.4000 -0.0032 0.0223  -0.0191 114 ILE A C   
915  O O   . ILE A 114 ? 0.4340 0.4386 0.3305 -0.0020 0.0179  -0.0117 114 ILE A O   
916  C CB  . ILE A 114 ? 0.4651 0.4725 0.3953 -0.0154 0.0403  -0.0394 114 ILE A CB  
917  C CG1 . ILE A 114 ? 0.4921 0.5125 0.3977 -0.0218 0.0445  -0.0303 114 ILE A CG1 
918  C CG2 . ILE A 114 ? 0.4813 0.4987 0.4282 -0.0173 0.0478  -0.0591 114 ILE A CG2 
919  C CD1 . ILE A 114 ? 0.4860 0.5098 0.3927 -0.0302 0.0554  -0.0275 114 ILE A CD1 
920  N N   . ASP A 115 ? 0.4341 0.4059 0.3577 0.0003  0.0206  -0.0115 115 ASP A N   
921  C CA  . ASP A 115 ? 0.4768 0.4305 0.3906 0.0059  0.0151  0.0056  115 ASP A CA  
922  C C   . ASP A 115 ? 0.5236 0.4769 0.4379 0.0172  0.0056  0.0080  115 ASP A C   
923  O O   . ASP A 115 ? 0.4715 0.4373 0.3724 0.0211  0.0007  0.0146  115 ASP A O   
924  C CB  . ASP A 115 ? 0.5322 0.4888 0.4235 0.0014  0.0174  0.0196  115 ASP A CB  
925  C CG  . ASP A 115 ? 0.7319 0.6643 0.6131 0.0078  0.0121  0.0384  115 ASP A CG  
926  O OD1 . ASP A 115 ? 0.6996 0.6111 0.5921 0.0133  0.0092  0.0383  115 ASP A OD1 
927  O OD2 . ASP A 115 ? 0.8127 0.7456 0.6740 0.0075  0.0109  0.0533  115 ASP A OD2 
928  N N   . PHE A 116 ? 0.3914 0.3330 0.3211 0.0224  0.0029  0.0033  116 PHE A N   
929  C CA  . PHE A 116 ? 0.4197 0.3636 0.3526 0.0328  -0.0047 0.0045  116 PHE A CA  
930  C C   . PHE A 116 ? 0.4757 0.3966 0.4061 0.0426  -0.0083 0.0154  116 PHE A C   
931  O O   . PHE A 116 ? 0.4493 0.3717 0.3857 0.0520  -0.0130 0.0146  116 PHE A O   
932  C CB  . PHE A 116 ? 0.4432 0.3939 0.3938 0.0315  -0.0047 -0.0095 116 PHE A CB  
933  C CG  . PHE A 116 ? 0.4210 0.3937 0.3730 0.0247  -0.0032 -0.0209 116 PHE A CG  
934  C CD1 . PHE A 116 ? 0.4366 0.4120 0.3913 0.0161  0.0040  -0.0299 116 PHE A CD1 
935  C CD2 . PHE A 116 ? 0.4594 0.4509 0.4101 0.0269  -0.0088 -0.0233 116 PHE A CD2 
936  C CE1 . PHE A 116 ? 0.4475 0.4404 0.4024 0.0101  0.0059  -0.0427 116 PHE A CE1 
937  C CE2 . PHE A 116 ? 0.3954 0.4054 0.3460 0.0189  -0.0077 -0.0354 116 PHE A CE2 
938  C CZ  . PHE A 116 ? 0.4063 0.4149 0.3583 0.0108  -0.0001 -0.0457 116 PHE A CZ  
939  N N   . GLU A 117 ? 0.4966 0.3966 0.4182 0.0402  -0.0057 0.0251  117 GLU A N   
940  C CA  . GLU A 117 ? 0.5285 0.3999 0.4488 0.0477  -0.0079 0.0323  117 GLU A CA  
941  C C   . GLU A 117 ? 0.5620 0.4291 0.4730 0.0625  -0.0142 0.0437  117 GLU A C   
942  O O   . GLU A 117 ? 0.5428 0.3905 0.4566 0.0723  -0.0164 0.0449  117 GLU A O   
943  C CB  . GLU A 117 ? 0.5219 0.3712 0.4356 0.0379  -0.0030 0.0390  117 GLU A CB  
944  C CG  . GLU A 117 ? 0.6273 0.4839 0.5261 0.0311  -0.0001 0.0492  117 GLU A CG  
945  C CD  . GLU A 117 ? 0.8468 0.6752 0.7335 0.0269  0.0018  0.0635  117 GLU A CD  
946  O OE1 . GLU A 117 ? 0.8145 0.6178 0.6961 0.0372  -0.0028 0.0719  117 GLU A OE1 
947  O OE2 . GLU A 117 ? 0.8751 0.7064 0.7579 0.0130  0.0084  0.0661  117 GLU A OE2 
948  N N   . ARG A 118 ? 0.5162 0.4082 0.4205 0.0647  -0.0174 0.0477  118 ARG A N   
949  C CA  . ARG A 118 ? 0.4924 0.3898 0.3913 0.0803  -0.0248 0.0581  118 ARG A CA  
950  C C   . ARG A 118 ? 0.5318 0.4615 0.4424 0.0847  -0.0290 0.0484  118 ARG A C   
951  O O   . ARG A 118 ? 0.5087 0.4527 0.4170 0.0968  -0.0355 0.0562  118 ARG A O   
952  C CB  . ARG A 118 ? 0.6687 0.5704 0.5484 0.0796  -0.0269 0.0738  118 ARG A CB  
953  C CG  . ARG A 118 ? 0.7617 0.6322 0.6289 0.0727  -0.0222 0.0852  118 ARG A CG  
954  C CD  . ARG A 118 ? 0.9471 0.8253 0.7936 0.0710  -0.0243 0.1022  118 ARG A CD  
955  N NE  . ARG A 118 ? 1.1656 1.0176 1.0001 0.0601  -0.0182 0.1129  118 ARG A NE  
956  C CZ  . ARG A 118 ? 1.2423 1.0929 1.0808 0.0434  -0.0094 0.1041  118 ARG A CZ  
957  N NH1 . ARG A 118 ? 1.1300 1.0117 0.9713 0.0334  -0.0053 0.0919  118 ARG A NH1 
958  N NH2 . ARG A 118 ? 1.1551 0.9738 0.9958 0.0370  -0.0050 0.1067  118 ARG A NH2 
959  N N   . GLY A 119 ? 0.4766 0.4178 0.4001 0.0756  -0.0257 0.0330  119 GLY A N   
960  C CA  . GLY A 119 ? 0.4913 0.4605 0.4255 0.0777  -0.0294 0.0251  119 GLY A CA  
961  C C   . GLY A 119 ? 0.5302 0.4980 0.4722 0.0930  -0.0331 0.0281  119 GLY A C   
962  O O   . GLY A 119 ? 0.4675 0.4087 0.4098 0.0996  -0.0310 0.0305  119 GLY A O   
963  N N   . VAL A 120 ? 0.4515 0.4502 0.3998 0.0983  -0.0384 0.0273  120 VAL A N   
964  C CA  . VAL A 120 ? 0.5256 0.5330 0.4857 0.1117  -0.0406 0.0270  120 VAL A CA  
965  C C   . VAL A 120 ? 0.5162 0.5595 0.4893 0.1052  -0.0427 0.0178  120 VAL A C   
966  O O   . VAL A 120 ? 0.4474 0.5114 0.4178 0.0945  -0.0451 0.0146  120 VAL A O   
967  C CB  . VAL A 120 ? 0.5555 0.5648 0.5109 0.1309  -0.0463 0.0408  120 VAL A CB  
968  C CG1 . VAL A 120 ? 0.5864 0.5550 0.5300 0.1383  -0.0443 0.0503  120 VAL A CG1 
969  C CG2 . VAL A 120 ? 0.5329 0.5728 0.4815 0.1304  -0.0536 0.0484  120 VAL A CG2 
970  N N   . ILE A 121 ? 0.4072 0.4587 0.3937 0.1114  -0.0416 0.0134  121 ILE A N   
971  C CA  . ILE A 121 ? 0.4280 0.5143 0.4282 0.1048  -0.0433 0.0062  121 ILE A CA  
972  C C   . ILE A 121 ? 0.4614 0.5823 0.4654 0.1159  -0.0507 0.0134  121 ILE A C   
973  O O   . ILE A 121 ? 0.4881 0.6055 0.4917 0.1346  -0.0527 0.0223  121 ILE A O   
974  C CB  . ILE A 121 ? 0.4191 0.5027 0.4314 0.1054  -0.0382 -0.0003 121 ILE A CB  
975  C CG1 . ILE A 121 ? 0.4624 0.5170 0.4720 0.0931  -0.0325 -0.0069 121 ILE A CG1 
976  C CG2 . ILE A 121 ? 0.3833 0.5056 0.4106 0.0994  -0.0399 -0.0052 121 ILE A CG2 
977  C CD1 . ILE A 121 ? 0.4427 0.4939 0.4611 0.0918  -0.0279 -0.0122 121 ILE A CD1 
978  N N   . LYS A 122 ? 0.4684 0.6228 0.4764 0.1049  -0.0554 0.0094  122 LYS A N   
979  C CA  . LYS A 122 ? 0.3977 0.5924 0.4121 0.1143  -0.0637 0.0157  122 LYS A CA  
980  C C   . LYS A 122 ? 0.4272 0.6603 0.4544 0.0986  -0.0663 0.0059  122 LYS A C   
981  O O   . LYS A 122 ? 0.3769 0.6041 0.4012 0.0793  -0.0639 -0.0043 122 LYS A O   
982  C CB  . LYS A 122 ? 0.5334 0.7328 0.5317 0.1186  -0.0710 0.0262  122 LYS A CB  
983  C CG  . LYS A 122 ? 0.6075 0.7696 0.5907 0.1319  -0.0696 0.0385  122 LYS A CG  
984  C CD  . LYS A 122 ? 0.7185 0.8936 0.7039 0.1555  -0.0768 0.0533  122 LYS A CD  
985  C CE  . LYS A 122 ? 0.6856 0.8155 0.6599 0.1704  -0.0738 0.0643  122 LYS A CE  
986  N NZ  . LYS A 122 ? 0.7651 0.9016 0.7457 0.1966  -0.0791 0.0768  122 LYS A NZ  
987  N N   . CYS A 123 ? 0.4141 0.6874 0.4559 0.1072  -0.0715 0.0092  123 CYS A N   
988  C CA  . CYS A 123 ? 0.5031 0.8174 0.5587 0.0913  -0.0748 0.0007  123 CYS A CA  
989  C C   . CYS A 123 ? 0.5137 0.8411 0.5577 0.0754  -0.0814 -0.0037 123 CYS A C   
990  O O   . CYS A 123 ? 0.5071 0.8378 0.5534 0.0540  -0.0797 -0.0162 123 CYS A O   
991  C CB  . CYS A 123 ? 0.4954 0.8561 0.5696 0.1051  -0.0801 0.0065  123 CYS A CB  
992  S SG  . CYS A 123 ? 1.0111 1.3631 1.0990 0.1263  -0.0717 0.0098  123 CYS A SG  
993  N N   . ARG A 124 ? 0.4014 0.7356 0.4319 0.0857  -0.0888 0.0066  124 ARG A N   
994  C CA  . ARG A 124 ? 0.4779 0.8276 0.4936 0.0722  -0.0956 0.0033  124 ARG A CA  
995  C C   . ARG A 124 ? 0.4799 0.7957 0.4715 0.0781  -0.0941 0.0116  124 ARG A C   
996  O O   . ARG A 124 ? 0.4374 0.7615 0.4189 0.0928  -0.1011 0.0266  124 ARG A O   
997  C CB  . ARG A 124 ? 0.4678 0.8725 0.4903 0.0765  -0.1083 0.0090  124 ARG A CB  
998  C CG  . ARG A 124 ? 0.5620 1.0053 0.6016 0.0570  -0.1109 -0.0047 124 ARG A CG  
999  C CD  . ARG A 124 ? 0.6464 1.1466 0.7036 0.0672  -0.1216 0.0030  124 ARG A CD  
1000 N NE  . ARG A 124 ? 0.6991 1.2325 0.7786 0.0502  -0.1211 -0.0087 124 ARG A NE  
1001 C CZ  . ARG A 124 ? 0.7222 1.2908 0.8061 0.0343  -0.1269 -0.0146 124 ARG A CZ  
1002 N NH1 . ARG A 124 ? 0.7541 1.3357 0.8225 0.0344  -0.1350 -0.0101 124 ARG A NH1 
1003 N NH2 . ARG A 124 ? 0.7033 1.2914 0.8062 0.0171  -0.1236 -0.0246 124 ARG A NH2 
1004 N N   . PRO A 125 ? 0.4496 0.7275 0.4324 0.0671  -0.0849 0.0032  125 PRO A N   
1005 C CA  . PRO A 125 ? 0.4607 0.7078 0.4220 0.0701  -0.0819 0.0104  125 PRO A CA  
1006 C C   . PRO A 125 ? 0.5439 0.8131 0.4856 0.0638  -0.0889 0.0132  125 PRO A C   
1007 O O   . PRO A 125 ? 0.4351 0.7405 0.3781 0.0525  -0.0955 0.0048  125 PRO A O   
1008 C CB  . PRO A 125 ? 0.4079 0.6211 0.3693 0.0565  -0.0709 -0.0029 125 PRO A CB  
1009 C CG  . PRO A 125 ? 0.4307 0.6446 0.4138 0.0556  -0.0677 -0.0098 125 PRO A CG  
1010 C CD  . PRO A 125 ? 0.4464 0.7062 0.4405 0.0534  -0.0762 -0.0113 125 PRO A CD  
1011 N N   . SER A 126 ? 0.4458 0.6923 0.3677 0.0695  -0.0873 0.0247  126 SER A N   
1012 C CA  . SER A 126 ? 0.5186 0.7837 0.4175 0.0651  -0.0933 0.0309  126 SER A CA  
1013 C C   . SER A 126 ? 0.5171 0.7626 0.3986 0.0490  -0.0844 0.0209  126 SER A C   
1014 O O   . SER A 126 ? 0.5565 0.8042 0.4151 0.0480  -0.0858 0.0302  126 SER A O   
1015 C CB  . SER A 126 ? 0.5527 0.8123 0.4405 0.0847  -0.0993 0.0556  126 SER A CB  
1016 O OG  . SER A 126 ? 0.6170 0.9000 0.5214 0.1015  -0.1081 0.0644  126 SER A OG  
1017 N N   . ASN A 127 ? 0.4597 0.6870 0.3515 0.0371  -0.0749 0.0029  127 ASN A N   
1018 C CA  . ASN A 127 ? 0.4587 0.6675 0.3369 0.0246  -0.0653 -0.0069 127 ASN A CA  
1019 C C   . ASN A 127 ? 0.5543 0.7928 0.4137 0.0114  -0.0689 -0.0157 127 ASN A C   
1020 O O   . ASN A 127 ? 0.5109 0.7471 0.3480 0.0082  -0.0657 -0.0110 127 ASN A O   
1021 C CB  . ASN A 127 ? 0.3865 0.5736 0.2819 0.0159  -0.0560 -0.0247 127 ASN A CB  
1022 C CG  . ASN A 127 ? 0.4342 0.5936 0.3459 0.0271  -0.0524 -0.0174 127 ASN A CG  
1023 O OD1 . ASN A 127 ? 0.4316 0.5655 0.3373 0.0345  -0.0481 -0.0065 127 ASN A OD1 
1024 N ND2 . ASN A 127 ? 0.4128 0.5778 0.3441 0.0275  -0.0541 -0.0234 127 ASN A ND2 
1025 N N   . LEU A 128 ? 0.5455 0.8135 0.4127 0.0025  -0.0754 -0.0288 128 LEU A N   
1026 C CA  . LEU A 128 ? 0.5715 0.8673 0.4211 -0.0128 -0.0785 -0.0422 128 LEU A CA  
1027 C C   . LEU A 128 ? 0.6003 0.9245 0.4269 -0.0071 -0.0886 -0.0249 128 LEU A C   
1028 O O   . LEU A 128 ? 0.5387 0.8746 0.3407 -0.0167 -0.0875 -0.0296 128 LEU A O   
1029 C CB  . LEU A 128 ? 0.4675 0.7869 0.3328 -0.0249 -0.0838 -0.0601 128 LEU A CB  
1030 C CG  . LEU A 128 ? 0.5974 0.9424 0.4466 -0.0438 -0.0864 -0.0797 128 LEU A CG  
1031 C CD1 . LEU A 128 ? 0.5606 0.8795 0.3967 -0.0528 -0.0731 -0.0951 128 LEU A CD1 
1032 C CD2 . LEU A 128 ? 0.6016 0.9619 0.4704 -0.0568 -0.0906 -0.0970 128 LEU A CD2 
1033 N N   . THR A 129 ? 0.5640 0.9017 0.3978 0.0088  -0.0988 -0.0053 129 THR A N   
1034 C CA  . THR A 129 ? 0.6363 1.0017 0.4493 0.0161  -0.1101 0.0137  129 THR A CA  
1035 C C   . THR A 129 ? 0.6260 0.9632 0.4191 0.0257  -0.1051 0.0343  129 THR A C   
1036 O O   . THR A 129 ? 0.7488 1.1037 0.5157 0.0248  -0.1106 0.0464  129 THR A O   
1037 C CB  . THR A 129 ? 0.6249 1.0194 0.4559 0.0297  -0.1233 0.0252  129 THR A CB  
1038 O OG1 . THR A 129 ? 0.6343 0.9985 0.4837 0.0479  -0.1193 0.0376  129 THR A OG1 
1039 C CG2 . THR A 129 ? 0.6466 1.0669 0.4965 0.0145  -0.1257 0.0020  129 THR A CG2 
1040 N N   . GLN A 130 ? 0.5850 0.8798 0.3891 0.0336  -0.0953 0.0393  130 GLN A N   
1041 C CA  . GLN A 130 ? 0.6447 0.9100 0.4301 0.0371  -0.0883 0.0550  130 GLN A CA  
1042 C C   . GLN A 130 ? 0.6527 0.9200 0.4177 0.0186  -0.0789 0.0412  130 GLN A C   
1043 O O   . GLN A 130 ? 0.6486 0.9224 0.3865 0.0160  -0.0790 0.0538  130 GLN A O   
1044 C CB  . GLN A 130 ? 0.6536 0.8750 0.4573 0.0461  -0.0796 0.0582  130 GLN A CB  
1045 C CG  . GLN A 130 ? 0.6912 0.9001 0.5028 0.0676  -0.0866 0.0802  130 GLN A CG  
1046 C CD  . GLN A 130 ? 0.7265 0.8943 0.5568 0.0742  -0.0779 0.0780  130 GLN A CD  
1047 O OE1 . GLN A 130 ? 0.6626 0.8062 0.4937 0.0636  -0.0666 0.0677  130 GLN A OE1 
1048 N NE2 . GLN A 130 ? 0.7542 0.9167 0.6002 0.0919  -0.0831 0.0868  130 GLN A NE2 
1049 N N   . PHE A 131 ? 0.5828 0.8468 0.3600 0.0057  -0.0707 0.0149  131 PHE A N   
1050 C CA  . PHE A 131 ? 0.5924 0.8588 0.3530 -0.0104 -0.0605 -0.0017 131 PHE A CA  
1051 C C   . PHE A 131 ? 0.7012 1.0089 0.4365 -0.0200 -0.0684 -0.0057 131 PHE A C   
1052 O O   . PHE A 131 ? 0.6051 0.9195 0.3147 -0.0287 -0.0623 -0.0068 131 PHE A O   
1053 C CB  . PHE A 131 ? 0.5496 0.8023 0.3307 -0.0199 -0.0512 -0.0290 131 PHE A CB  
1054 C CG  . PHE A 131 ? 0.5682 0.8202 0.3354 -0.0336 -0.0391 -0.0472 131 PHE A CG  
1055 C CD1 . PHE A 131 ? 0.6005 0.8320 0.3596 -0.0331 -0.0274 -0.0401 131 PHE A CD1 
1056 C CD2 . PHE A 131 ? 0.6537 0.9285 0.4139 -0.0472 -0.0395 -0.0710 131 PHE A CD2 
1057 C CE1 . PHE A 131 ? 0.6758 0.9113 0.4226 -0.0446 -0.0151 -0.0570 131 PHE A CE1 
1058 C CE2 . PHE A 131 ? 0.6201 0.8955 0.3662 -0.0583 -0.0274 -0.0892 131 PHE A CE2 
1059 C CZ  . PHE A 131 ? 0.6569 0.9141 0.3968 -0.0563 -0.0149 -0.0820 131 PHE A CZ  
1060 N N   . ALA A 132 ? 0.6269 0.9655 0.3687 -0.0194 -0.0819 -0.0085 132 ALA A N   
1061 C CA  . ALA A 132 ? 0.6550 1.0367 0.3732 -0.0296 -0.0912 -0.0134 132 ALA A CA  
1062 C C   . ALA A 132 ? 0.6577 1.0462 0.3505 -0.0222 -0.0958 0.0138  132 ALA A C   
1063 O O   . ALA A 132 ? 0.7197 1.1214 0.3919 -0.0324 -0.0936 0.0100  132 ALA A O   
1064 C CB  . ALA A 132 ? 0.6094 1.0195 0.3472 -0.0294 -0.1044 -0.0188 132 ALA A CB  
1065 N N   . VAL A 133 ? 0.6309 1.0056 0.3267 -0.0041 -0.1010 0.0416  133 VAL A N   
1066 C CA  . VAL A 133 ? 0.7606 1.1310 0.4349 0.0034  -0.1039 0.0692  133 VAL A CA  
1067 C C   . VAL A 133 ? 0.7314 1.0848 0.3813 -0.0075 -0.0894 0.0685  133 VAL A C   
1068 O O   . VAL A 133 ? 0.6954 1.0591 0.3221 -0.0144 -0.0884 0.0746  133 VAL A O   
1069 C CB  . VAL A 133 ? 0.8067 1.1562 0.4924 0.0258  -0.1105 0.0973  133 VAL A CB  
1070 C CG1 . VAL A 133 ? 0.8660 1.1940 0.5282 0.0311  -0.1083 0.1249  133 VAL A CG1 
1071 C CG2 . VAL A 133 ? 0.7317 1.1048 0.4380 0.0378  -0.1253 0.1024  133 VAL A CG2 
1072 N N   . TYR A 134 ? 0.6117 0.9332 0.2743 -0.0096 -0.0758 0.0587  134 TYR A N   
1073 C CA  . TYR A 134 ? 0.7096 1.0156 0.3560 -0.0206 -0.0599 0.0552  134 TYR A CA  
1074 C C   . TYR A 134 ? 0.7360 1.0731 0.3631 -0.0385 -0.0549 0.0303  134 TYR A C   
1075 O O   . TYR A 134 ? 0.7477 1.0907 0.3515 -0.0461 -0.0487 0.0354  134 TYR A O   
1076 C CB  . TYR A 134 ? 0.6859 0.9514 0.3592 -0.0192 -0.0465 0.0456  134 TYR A CB  
1077 C CG  . TYR A 134 ? 0.6054 0.8625 0.2694 -0.0323 -0.0291 0.0333  134 TYR A CG  
1078 C CD1 . TYR A 134 ? 0.7238 0.9656 0.3717 -0.0336 -0.0214 0.0535  134 TYR A CD1 
1079 C CD2 . TYR A 134 ? 0.7095 0.9740 0.3821 -0.0433 -0.0200 0.0016  134 TYR A CD2 
1080 C CE1 . TYR A 134 ? 0.7012 0.9406 0.3423 -0.0459 -0.0047 0.0423  134 TYR A CE1 
1081 C CE2 . TYR A 134 ? 0.6868 0.9466 0.3532 -0.0533 -0.0034 -0.0103 134 TYR A CE2 
1082 C CZ  . TYR A 134 ? 0.7124 0.9623 0.3635 -0.0546 0.0043  0.0102  134 TYR A CZ  
1083 O OH  . TYR A 134 ? 0.7914 1.0416 0.4381 -0.0647 0.0213  -0.0015 134 TYR A OH  
1084 N N   . LEU A 135 ? 0.7077 1.0562 0.3515 -0.0449 -0.0562 0.0022  135 LEU A N   
1085 C CA  . LEU A 135 ? 0.7087 1.0732 0.3454 -0.0605 -0.0496 -0.0254 135 LEU A CA  
1086 C C   . LEU A 135 ? 0.7205 1.1115 0.3365 -0.0640 -0.0576 -0.0163 135 LEU A C   
1087 O O   . LEU A 135 ? 0.8015 1.1995 0.3983 -0.0738 -0.0487 -0.0235 135 LEU A O   
1088 C CB  . LEU A 135 ? 0.7724 1.1407 0.4331 -0.0657 -0.0524 -0.0529 135 LEU A CB  
1089 C CG  . LEU A 135 ? 0.8659 1.2398 0.5252 -0.0810 -0.0433 -0.0847 135 LEU A CG  
1090 C CD1 . LEU A 135 ? 0.8019 1.1524 0.4615 -0.0843 -0.0245 -0.0981 135 LEU A CD1 
1091 C CD2 . LEU A 135 ? 0.8548 1.2326 0.5371 -0.0866 -0.0495 -0.1064 135 LEU A CD2 
1092 N N   . ASN A 136 ? 0.6659 1.0734 0.2864 -0.0556 -0.0743 -0.0005 136 ASN A N   
1093 C CA  . ASN A 136 ? 0.8006 1.2343 0.4017 -0.0575 -0.0833 0.0105  136 ASN A CA  
1094 C C   . ASN A 136 ? 0.7845 1.2082 0.3604 -0.0532 -0.0798 0.0377  136 ASN A C   
1095 O O   . ASN A 136 ? 0.8436 1.2850 0.3965 -0.0601 -0.0802 0.0409  136 ASN A O   
1096 C CB  . ASN A 136 ? 0.8001 1.2536 0.4158 -0.0476 -0.1015 0.0221  136 ASN A CB  
1097 C CG  . ASN A 136 ? 0.8292 1.3165 0.4295 -0.0533 -0.1113 0.0237  136 ASN A CG  
1098 O OD1 . ASN A 136 ? 0.8022 1.3053 0.3931 -0.0688 -0.1068 0.0009  136 ASN A OD1 
1099 N ND2 . ASN A 136 ? 0.8187 1.3173 0.4178 -0.0402 -0.1251 0.0502  136 ASN A ND2 
1100 N N   . SER A 137 ? 0.8543 1.2492 0.4338 -0.0426 -0.0763 0.0578  137 SER A N   
1101 C CA  . SER A 137 ? 0.8585 1.2390 0.4150 -0.0402 -0.0719 0.0844  137 SER A CA  
1102 C C   . SER A 137 ? 0.8829 1.2634 0.4215 -0.0557 -0.0544 0.0705  137 SER A C   
1103 O O   . SER A 137 ? 0.8523 1.2372 0.3664 -0.0597 -0.0518 0.0854  137 SER A O   
1104 C CB  . SER A 137 ? 0.9379 1.2836 0.5045 -0.0266 -0.0711 0.1074  137 SER A CB  
1105 O OG  . SER A 137 ? 1.0662 1.3935 0.6113 -0.0268 -0.0654 0.1325  137 SER A OG  
1106 N N   . ARG A 138 ? 0.8297 1.2061 0.3812 -0.0642 -0.0422 0.0414  138 ARG A N   
1107 C CA  . ARG A 138 ? 0.8626 1.2386 0.4024 -0.0769 -0.0240 0.0263  138 ARG A CA  
1108 C C   . ARG A 138 ? 0.8174 1.2206 0.3485 -0.0888 -0.0222 0.0000  138 ARG A C   
1109 O O   . ARG A 138 ? 0.8731 1.2849 0.3852 -0.0975 -0.0114 -0.0033 138 ARG A O   
1110 C CB  . ARG A 138 ? 0.8672 1.2215 0.4271 -0.0784 -0.0102 0.0089  138 ARG A CB  
1111 C CG  . ARG A 138 ? 0.8983 1.2272 0.4560 -0.0758 -0.0001 0.0302  138 ARG A CG  
1112 C CD  . ARG A 138 ? 0.9534 1.2705 0.5005 -0.0653 -0.0118 0.0686  138 ARG A CD  
1113 N NE  . ARG A 138 ? 1.0717 1.3595 0.6207 -0.0639 -0.0025 0.0875  138 ARG A NE  
1114 C CZ  . ARG A 138 ? 1.1514 1.4145 0.7045 -0.0520 -0.0110 0.1156  138 ARG A CZ  
1115 N NH1 . ARG A 138 ? 1.0899 1.3558 0.6464 -0.0384 -0.0289 0.1288  138 ARG A NH1 
1116 N NH2 . ARG A 138 ? 1.1460 1.3739 0.7100 -0.0521 -0.0011 0.1272  138 ARG A NH2 
1117 N N   . LEU A 139 ? 0.8308 1.2476 0.3757 -0.0899 -0.0318 -0.0189 139 LEU A N   
1118 C CA  . LEU A 139 ? 0.8315 1.2704 0.3707 -0.1020 -0.0297 -0.0464 139 LEU A CA  
1119 C C   . LEU A 139 ? 0.9050 1.3741 0.4280 -0.1035 -0.0451 -0.0366 139 LEU A C   
1120 O O   . LEU A 139 ? 0.8594 1.3491 0.3727 -0.1146 -0.0438 -0.0569 139 LEU A O   
1121 C CB  . LEU A 139 ? 0.7649 1.1967 0.3310 -0.1052 -0.0285 -0.0769 139 LEU A CB  
1122 C CG  . LEU A 139 ? 0.8970 1.2993 0.4829 -0.1033 -0.0144 -0.0901 139 LEU A CG  
1123 C CD1 . LEU A 139 ? 0.8603 1.2563 0.4678 -0.1096 -0.0110 -0.1241 139 LEU A CD1 
1124 C CD2 . LEU A 139 ? 0.9039 1.2988 0.4769 -0.1066 0.0033  -0.0894 139 LEU A CD2 
1125 N N   . ARG A 140 ? 0.8629 1.3346 0.3825 -0.0923 -0.0590 -0.0058 140 ARG A N   
1126 C CA  . ARG A 140 ? 0.8613 1.3621 0.3704 -0.0911 -0.0757 0.0055  140 ARG A CA  
1127 C C   . ARG A 140 ? 0.9163 1.4406 0.4366 -0.1006 -0.0818 -0.0227 140 ARG A C   
1128 O O   . ARG A 140 ? 0.8749 1.4254 0.3781 -0.1106 -0.0845 -0.0321 140 ARG A O   
1129 C CB  . ARG A 140 ? 0.8902 1.4049 0.3661 -0.0953 -0.0743 0.0211  140 ARG A CB  
1130 C CG  . ARG A 140 ? 0.9801 1.4702 0.4436 -0.0890 -0.0666 0.0481  140 ARG A CG  
1131 C CD  . ARG A 140 ? 1.0520 1.5588 0.4826 -0.0956 -0.0650 0.0604  140 ARG A CD  
1132 N NE  . ARG A 140 ? 1.0895 1.6266 0.5121 -0.0940 -0.0828 0.0667  140 ARG A NE  
1133 C CZ  . ARG A 140 ? 1.2235 1.7646 0.6335 -0.0842 -0.0959 0.0986  140 ARG A CZ  
1134 N NH1 . ARG A 140 ? 1.2601 1.7722 0.6663 -0.0735 -0.0947 0.1285  140 ARG A NH1 
1135 N NH2 . ARG A 140 ? 1.2787 1.8525 0.6804 -0.0850 -0.1108 0.1004  140 ARG A NH2 
1136 N N   . LEU A 141 ? 0.9040 1.4180 0.4530 -0.0982 -0.0838 -0.0359 141 LEU A N   
1137 C CA  . LEU A 141 ? 0.9273 1.4582 0.4898 -0.1086 -0.0883 -0.0631 141 LEU A CA  
1138 C C   . LEU A 141 ? 0.9348 1.4996 0.4952 -0.1071 -0.1067 -0.0514 141 LEU A C   
1139 O O   . LEU A 141 ? 0.9942 1.5826 0.5509 -0.1195 -0.1104 -0.0704 141 LEU A O   
1140 C CB  . LEU A 141 ? 0.8462 1.3551 0.4400 -0.1061 -0.0855 -0.0767 141 LEU A CB  
1141 C CG  . LEU A 141 ? 0.8716 1.3513 0.4706 -0.1114 -0.0669 -0.0987 141 LEU A CG  
1142 C CD1 . LEU A 141 ? 0.7743 1.2347 0.4043 -0.1116 -0.0654 -0.1162 141 LEU A CD1 
1143 C CD2 . LEU A 141 ? 0.8208 1.3085 0.4032 -0.1253 -0.0567 -0.1226 141 LEU A CD2 
1144 N N   . MET A 142 ? 0.8599 1.4275 0.4218 -0.0917 -0.1181 -0.0200 142 MET A N   
1145 C CA  . MET A 142 ? 0.8497 1.4480 0.4179 -0.0865 -0.1362 -0.0075 142 MET A CA  
1146 C C   . MET A 142 ? 0.9061 1.4974 0.4709 -0.0670 -0.1448 0.0300  142 MET A C   
1147 O O   . MET A 142 ? 0.8923 1.4527 0.4530 -0.0585 -0.1368 0.0445  142 MET A O   
1148 C CB  . MET A 142 ? 0.9515 1.5561 0.5523 -0.0879 -0.1419 -0.0232 142 MET A CB  
1149 C CG  . MET A 142 ? 0.8824 1.4570 0.5072 -0.0757 -0.1380 -0.0168 142 MET A CG  
1150 S SD  . MET A 142 ? 0.9307 1.5111 0.5930 -0.0801 -0.1419 -0.0375 142 MET A SD  
1151 C CE  . MET A 142 ? 0.9338 1.4890 0.5963 -0.0984 -0.1244 -0.0740 142 MET A CE  
1152 N N   . LYS A 143 ? 0.8687 1.4884 0.4352 -0.0599 -0.1611 0.0456  143 LYS A N   
1153 C CA  . LYS A 143 ? 0.9683 1.5802 0.5357 -0.0392 -0.1707 0.0807  143 LYS A CA  
1154 C C   . LYS A 143 ? 0.9714 1.5701 0.5733 -0.0247 -0.1743 0.0850  143 LYS A C   
1155 O O   . LYS A 143 ? 1.0496 1.6582 0.6748 -0.0314 -0.1741 0.0630  143 LYS A O   
1156 C CB  . LYS A 143 ? 0.9563 1.6044 0.5124 -0.0360 -0.1867 0.0959  143 LYS A CB  
1157 N N   . ASN A 144 ? 0.9422 1.5159 0.5470 -0.0051 -0.1767 0.1131  144 ASN A N   
1158 C CA  . ASN A 144 ? 1.0073 1.5683 0.6445 0.0108  -0.1800 0.1185  144 ASN A CA  
1159 C C   . ASN A 144 ? 0.9912 1.5889 0.6545 0.0114  -0.1913 0.1087  144 ASN A C   
1160 O O   . ASN A 144 ? 1.0412 1.6381 0.7302 0.0087  -0.1881 0.0915  144 ASN A O   
1161 C CB  . ASN A 144 ? 1.2013 1.7357 0.8382 0.0336  -0.1845 0.1517  144 ASN A CB  
1162 C CG  . ASN A 144 ? 1.3404 1.8287 0.9680 0.0358  -0.1712 0.1588  144 ASN A CG  
1163 O OD1 . ASN A 144 ? 1.4046 1.8839 1.0177 0.0200  -0.1587 0.1434  144 ASN A OD1 
1164 N ND2 . ASN A 144 ? 1.3984 1.8570 1.0382 0.0557  -0.1731 0.1799  144 ASN A ND2 
1165 N N   . GLU A 145 ? 0.8157 1.4461 0.4732 0.0149  -0.2047 0.1204  145 GLU A N   
1166 C CA  . GLU A 145 ? 0.9220 1.5887 0.6065 0.0176  -0.2159 0.1148  145 GLU A CA  
1167 C C   . GLU A 145 ? 0.9735 1.6535 0.6726 -0.0027 -0.2100 0.0814  145 GLU A C   
1168 O O   . GLU A 145 ? 0.9836 1.6713 0.7134 0.0004  -0.2115 0.0737  145 GLU A O   
1169 C CB  . GLU A 145 ? 0.8536 1.5586 0.5247 0.0184  -0.2303 0.1271  145 GLU A CB  
1170 N N   . GLU A 146 ? 0.8896 1.5682 0.5674 -0.0233 -0.2018 0.0611  146 GLU A N   
1171 C CA  . GLU A 146 ? 0.8362 1.5185 0.5267 -0.0426 -0.1948 0.0287  146 GLU A CA  
1172 C C   . GLU A 146 ? 0.9131 1.5579 0.6201 -0.0396 -0.1830 0.0207  146 GLU A C   
1173 O O   . GLU A 146 ? 0.9570 1.6049 0.6906 -0.0436 -0.1822 0.0062  146 GLU A O   
1174 C CB  . GLU A 146 ? 0.8831 1.5711 0.5464 -0.0637 -0.1885 0.0084  146 GLU A CB  
1175 C CG  . GLU A 146 ? 0.8950 1.5860 0.5705 -0.0843 -0.1823 -0.0259 146 GLU A CG  
1176 N N   . LEU A 147 ? 0.8955 1.5054 0.5869 -0.0334 -0.1735 0.0301  147 LEU A N   
1177 C CA  . LEU A 147 ? 0.8000 1.3756 0.5065 -0.0298 -0.1630 0.0237  147 LEU A CA  
1178 C C   . LEU A 147 ? 0.8640 1.4385 0.6000 -0.0114 -0.1695 0.0378  147 LEU A C   
1179 O O   . LEU A 147 ? 0.8586 1.4250 0.6178 -0.0136 -0.1653 0.0240  147 LEU A O   
1180 C CB  . LEU A 147 ? 0.8069 1.3476 0.4915 -0.0256 -0.1523 0.0343  147 LEU A CB  
1181 C CG  . LEU A 147 ? 0.8376 1.3437 0.5379 -0.0204 -0.1424 0.0298  147 LEU A CG  
1182 C CD1 . LEU A 147 ? 0.6782 1.1797 0.3880 -0.0383 -0.1330 -0.0033 147 LEU A CD1 
1183 C CD2 . LEU A 147 ? 0.7676 1.2402 0.4492 -0.0130 -0.1335 0.0466  147 LEU A CD2 
1184 N N   . LYS A 148 ? 0.8958 1.4771 0.6316 0.0073  -0.1792 0.0650  148 LYS A N   
1185 C CA  . LYS A 148 ? 1.0048 1.5838 0.7690 0.0272  -0.1843 0.0785  148 LYS A CA  
1186 C C   . LYS A 148 ? 0.9004 1.5136 0.6928 0.0211  -0.1900 0.0635  148 LYS A C   
1187 O O   . LYS A 148 ? 0.9260 1.5340 0.7455 0.0291  -0.1881 0.0613  148 LYS A O   
1188 C CB  . LYS A 148 ? 0.9814 1.5592 0.7389 0.0484  -0.1936 0.1096  148 LYS A CB  
1189 C CG  . LYS A 148 ? 1.1341 1.6673 0.8728 0.0588  -0.1866 0.1282  148 LYS A CG  
1190 C CD  . LYS A 148 ? 1.1399 1.6513 0.8949 0.0852  -0.1904 0.1517  148 LYS A CD  
1191 C CE  . LYS A 148 ? 1.1029 1.6423 0.8645 0.0990  -0.2047 0.1686  148 LYS A CE  
1192 N NZ  . LYS A 148 ? 1.1187 1.6532 0.8490 0.1003  -0.2098 0.1887  148 LYS A NZ  
1193 N N   . LYS A 149 ? 0.8741 1.5228 0.6603 0.0063  -0.1964 0.0528  149 LYS A N   
1194 C CA  . LYS A 149 ? 0.8918 1.5723 0.7033 -0.0037 -0.2006 0.0366  149 LYS A CA  
1195 C C   . LYS A 149 ? 0.8458 1.5080 0.6684 -0.0201 -0.1895 0.0107  149 LYS A C   
1196 O O   . LYS A 149 ? 0.8187 1.4866 0.6695 -0.0196 -0.1888 0.0043  149 LYS A O   
1197 C CB  . LYS A 149 ? 0.7540 1.4742 0.5534 -0.0181 -0.2095 0.0298  149 LYS A CB  
1198 N N   . LEU A 150 ? 0.8696 1.5087 0.6706 -0.0343 -0.1801 -0.0040 150 LEU A N   
1199 C CA  . LEU A 150 ? 0.8488 1.4670 0.6592 -0.0498 -0.1694 -0.0292 150 LEU A CA  
1200 C C   . LEU A 150 ? 0.8252 1.4169 0.6555 -0.0366 -0.1640 -0.0232 150 LEU A C   
1201 O O   . LEU A 150 ? 0.7197 1.3078 0.5719 -0.0444 -0.1603 -0.0379 150 LEU A O   
1202 C CB  . LEU A 150 ? 0.8679 1.4630 0.6510 -0.0629 -0.1592 -0.0436 150 LEU A CB  
1203 C CG  . LEU A 150 ? 0.8600 1.4771 0.6238 -0.0806 -0.1613 -0.0580 150 LEU A CG  
1204 C CD1 . LEU A 150 ? 0.8663 1.4622 0.6002 -0.0844 -0.1518 -0.0611 150 LEU A CD1 
1205 C CD2 . LEU A 150 ? 0.8679 1.4895 0.6457 -0.1007 -0.1585 -0.0859 150 LEU A CD2 
1206 N N   . LEU A 151 ? 0.8117 1.3832 0.6340 -0.0170 -0.1633 -0.0013 151 LEU A N   
1207 C CA  . LEU A 151 ? 0.8432 1.3883 0.6823 -0.0034 -0.1582 0.0050  151 LEU A CA  
1208 C C   . LEU A 151 ? 0.8270 1.3929 0.6972 0.0087  -0.1646 0.0126  151 LEU A C   
1209 O O   . LEU A 151 ? 0.7898 1.3440 0.6810 0.0110  -0.1598 0.0066  151 LEU A O   
1210 C CB  . LEU A 151 ? 0.7327 1.2489 0.5537 0.0138  -0.1556 0.0270  151 LEU A CB  
1211 C CG  . LEU A 151 ? 0.7810 1.2775 0.5710 0.0018  -0.1472 0.0204  151 LEU A CG  
1212 C CD1 . LEU A 151 ? 0.7419 1.2060 0.5162 0.0169  -0.1428 0.0423  151 LEU A CD1 
1213 C CD2 . LEU A 151 ? 0.6998 1.1827 0.4928 -0.0172 -0.1367 -0.0085 151 LEU A CD2 
1214 N N   . ARG A 152 ? 0.8372 1.4349 0.7109 0.0165  -0.1751 0.0255  152 ARG A N   
1215 C CA  . ARG A 152 ? 0.8418 1.4637 0.7459 0.0276  -0.1804 0.0314  152 ARG A CA  
1216 C C   . ARG A 152 ? 0.7715 1.4109 0.6965 0.0080  -0.1777 0.0086  152 ARG A C   
1217 O O   . ARG A 152 ? 0.7223 1.3640 0.6734 0.0142  -0.1751 0.0082  152 ARG A O   
1218 C CB  . ARG A 152 ? 0.8421 1.4975 0.7446 0.0378  -0.1924 0.0477  152 ARG A CB  
1219 C CG  . ARG A 152 ? 0.9447 1.5812 0.8400 0.0644  -0.1956 0.0749  152 ARG A CG  
1220 C CD  . ARG A 152 ? 0.9085 1.5788 0.8052 0.0755  -0.2083 0.0911  152 ARG A CD  
1221 N NE  . ARG A 152 ? 1.0205 1.6700 0.8933 0.0896  -0.2120 0.1136  152 ARG A NE  
1222 C CZ  . ARG A 152 ? 1.0423 1.7072 0.8906 0.0829  -0.2192 0.1197  152 ARG A CZ  
1223 N NH1 . ARG A 152 ? 0.9879 1.6903 0.8325 0.0633  -0.2240 0.1047  152 ARG A NH1 
1224 N NH2 . ARG A 152 ? 1.1149 1.7559 0.9411 0.0955  -0.2214 0.1414  152 ARG A NH2 
1225 N N   . GLU A 153 ? 0.7513 1.4010 0.6646 -0.0162 -0.1775 -0.0105 153 GLU A N   
1226 C CA  . GLU A 153 ? 0.7182 1.3819 0.6503 -0.0366 -0.1753 -0.0315 153 GLU A CA  
1227 C C   . GLU A 153 ? 0.7656 1.3949 0.7072 -0.0431 -0.1643 -0.0445 153 GLU A C   
1228 O O   . GLU A 153 ? 0.7585 1.3941 0.7250 -0.0474 -0.1620 -0.0503 153 GLU A O   
1229 C CB  . GLU A 153 ? 0.6489 1.3268 0.5641 -0.0601 -0.1774 -0.0490 153 GLU A CB  
1230 N N   . TYR A 154 ? 0.7182 1.3121 0.6400 -0.0447 -0.1571 -0.0492 154 TYR A N   
1231 C CA  . TYR A 154 ? 0.6624 1.2223 0.5926 -0.0480 -0.1473 -0.0593 154 TYR A CA  
1232 C C   . TYR A 154 ? 0.7089 1.2662 0.6608 -0.0278 -0.1472 -0.0439 154 TYR A C   
1233 O O   . TYR A 154 ? 0.6429 1.1929 0.6156 -0.0330 -0.1422 -0.0524 154 TYR A O   
1234 C CB  . TYR A 154 ? 0.5809 1.1063 0.4853 -0.0479 -0.1403 -0.0624 154 TYR A CB  
1235 C CG  . TYR A 154 ? 0.5871 1.0774 0.4994 -0.0459 -0.1312 -0.0683 154 TYR A CG  
1236 C CD1 . TYR A 154 ? 0.5934 1.0683 0.5181 -0.0634 -0.1245 -0.0895 154 TYR A CD1 
1237 C CD2 . TYR A 154 ? 0.5947 1.0619 0.5014 -0.0256 -0.1285 -0.0510 154 TYR A CD2 
1238 C CE1 . TYR A 154 ? 0.5336 0.9681 0.4680 -0.0600 -0.1136 -0.0923 154 TYR A CE1 
1239 C CE2 . TYR A 154 ? 0.5063 0.9273 0.4240 -0.0228 -0.1152 -0.0544 154 TYR A CE2 
1240 C CZ  . TYR A 154 ? 0.5652 0.9715 0.4966 -0.0394 -0.1081 -0.0744 154 TYR A CZ  
1241 O OH  . TYR A 154 ? 0.5217 0.8840 0.4635 -0.0355 -0.0960 -0.0759 154 TYR A OH  
1242 N N   . LYS A 155 ? 0.7001 1.2594 0.6471 -0.0043 -0.1516 -0.0214 155 LYS A N   
1243 C CA  . LYS A 155 ? 0.7098 1.2603 0.6759 0.0178  -0.1499 -0.0072 155 LYS A CA  
1244 C C   . LYS A 155 ? 0.7401 1.3221 0.7363 0.0170  -0.1518 -0.0092 155 LYS A C   
1245 O O   . LYS A 155 ? 0.7554 1.3282 0.7709 0.0231  -0.1462 -0.0097 155 LYS A O   
1246 C CB  . LYS A 155 ? 0.7220 1.2648 0.6769 0.0430  -0.1540 0.0172  155 LYS A CB  
1247 C CG  . LYS A 155 ? 0.7126 1.2136 0.6472 0.0515  -0.1483 0.0242  155 LYS A CG  
1248 N N   . LYS A 156 ? 0.6845 1.3033 0.6840 0.0095  -0.1591 -0.0102 156 LYS A N   
1249 C CA  . LYS A 156 ? 0.6786 1.3309 0.7051 0.0073  -0.1609 -0.0119 156 LYS A CA  
1250 C C   . LYS A 156 ? 0.6811 1.3275 0.7218 -0.0146 -0.1537 -0.0308 156 LYS A C   
1251 O O   . LYS A 156 ? 0.7385 1.3859 0.8012 -0.0091 -0.1486 -0.0292 156 LYS A O   
1252 C CB  . LYS A 156 ? 0.6968 1.3903 0.7212 0.0007  -0.1708 -0.0107 156 LYS A CB  
1253 N N   . GLY A 157 ? 0.6889 1.3254 0.7164 -0.0392 -0.1522 -0.0488 157 GLY A N   
1254 C CA  . GLY A 157 ? 0.7457 1.3706 0.7854 -0.0614 -0.1453 -0.0668 157 GLY A CA  
1255 C C   . GLY A 157 ? 0.6701 1.2546 0.7111 -0.0589 -0.1362 -0.0703 157 GLY A C   
1256 O O   . GLY A 157 ? 0.6975 1.2793 0.7593 -0.0601 -0.1309 -0.0710 157 GLY A O   
1257 N N   . PHE A 158 ? 0.7451 1.2994 0.7635 -0.0556 -0.1342 -0.0721 158 PHE A N   
1258 C CA  . PHE A 158 ? 0.6551 1.1715 0.6720 -0.0506 -0.1266 -0.0741 158 PHE A CA  
1259 C C   . PHE A 158 ? 0.6285 1.1229 0.6581 -0.0714 -0.1184 -0.0915 158 PHE A C   
1260 O O   . PHE A 158 ? 0.7051 1.1627 0.7429 -0.0648 -0.1080 -0.0882 158 PHE A O   
1261 C CB  . PHE A 158 ? 0.6075 1.1191 0.6360 -0.0237 -0.1249 -0.0546 158 PHE A CB  
1262 C CG  . PHE A 158 ? 0.5934 1.0495 0.6086 -0.0110 -0.1142 -0.0488 158 PHE A CG  
1263 C CD1 . PHE A 158 ? 0.5745 1.0175 0.5659 -0.0008 -0.1160 -0.0401 158 PHE A CD1 
1264 C CD2 . PHE A 158 ? 0.6772 1.0969 0.7039 -0.0097 -0.1028 -0.0509 158 PHE A CD2 
1265 C CE1 . PHE A 158 ? 0.5616 0.9562 0.5424 0.0089  -0.1062 -0.0347 158 PHE A CE1 
1266 C CE2 . PHE A 158 ? 0.6122 0.9845 0.6280 0.0010  -0.0939 -0.0459 158 PHE A CE2 
1267 C CZ  . PHE A 158 ? 0.5786 0.9386 0.5723 0.0099  -0.0955 -0.0381 158 PHE A CZ  
1268 N N   . ASP A 159 ? 0.6996 1.2000 0.7288 -0.0945 -0.1187 -0.1070 159 ASP A N   
1269 C CA  . ASP A 159 ? 0.6901 1.1619 0.7274 -0.1155 -0.1108 -0.1240 159 ASP A CA  
1270 C C   . ASP A 159 ? 0.6427 1.0867 0.6585 -0.1295 -0.1071 -0.1419 159 ASP A C   
1271 O O   . ASP A 159 ? 0.6735 1.1245 0.6681 -0.1241 -0.1105 -0.1411 159 ASP A O   
1272 C CB  . ASP A 159 ? 0.6597 1.1547 0.7175 -0.1307 -0.1117 -0.1264 159 ASP A CB  
1273 C CG  . ASP A 159 ? 0.7610 1.2900 0.8125 -0.1385 -0.1196 -0.1290 159 ASP A CG  
1274 O OD1 . ASP A 159 ? 0.7100 1.2446 0.7407 -0.1322 -0.1242 -0.1283 159 ASP A OD1 
1275 O OD2 . ASP A 159 ? 0.8382 1.3893 0.9054 -0.1514 -0.1211 -0.1312 159 ASP A OD2 
1276 N N   . ASP A 160 ? 0.6231 1.0341 0.6450 -0.1466 -0.0993 -0.1571 160 ASP A N   
1277 C CA  . ASP A 160 ? 0.6949 1.0740 0.6996 -0.1583 -0.0936 -0.1757 160 ASP A CA  
1278 C C   . ASP A 160 ? 0.7338 1.1386 0.7230 -0.1660 -0.0996 -0.1819 160 ASP A C   
1279 O O   . ASP A 160 ? 0.7647 1.1593 0.7320 -0.1647 -0.0975 -0.1896 160 ASP A O   
1280 C CB  . ASP A 160 ? 0.7530 1.0962 0.7705 -0.1754 -0.0858 -0.1885 160 ASP A CB  
1281 C CG  . ASP A 160 ? 0.8858 1.1952 0.9143 -0.1686 -0.0784 -0.1846 160 ASP A CG  
1282 O OD1 . ASP A 160 ? 0.9158 1.2264 0.9422 -0.1486 -0.0779 -0.1702 160 ASP A OD1 
1283 O OD2 . ASP A 160 ? 0.9277 1.2035 0.9664 -0.1801 -0.0717 -0.1918 160 ASP A OD2 
1284 N N   . GLU A 161 ? 0.7853 1.2248 0.7858 -0.1745 -0.1066 -0.1791 161 GLU A N   
1285 C CA  . GLU A 161 ? 0.6578 1.1257 0.6452 -0.1828 -0.1134 -0.1849 161 GLU A CA  
1286 C C   . GLU A 161 ? 0.6759 1.1678 0.6448 -0.1656 -0.1196 -0.1723 161 GLU A C   
1287 O O   . GLU A 161 ? 0.7724 1.2636 0.7190 -0.1692 -0.1198 -0.1805 161 GLU A O   
1288 C CB  . GLU A 161 ? 0.7387 1.2431 0.7447 -0.1933 -0.1201 -0.1818 161 GLU A CB  
1289 N N   . SER A 162 ? 0.7207 1.2340 0.6983 -0.1463 -0.1245 -0.1514 162 SER A N   
1290 C CA  . SER A 162 ? 0.6809 1.2111 0.6412 -0.1279 -0.1303 -0.1360 162 SER A CA  
1291 C C   . SER A 162 ? 0.7011 1.1978 0.6375 -0.1243 -0.1234 -0.1415 162 SER A C   
1292 O O   . SER A 162 ? 0.6718 1.1780 0.5856 -0.1207 -0.1262 -0.1383 162 SER A O   
1293 C CB  . SER A 162 ? 0.7255 1.2710 0.7008 -0.1053 -0.1342 -0.1133 162 SER A CB  
1294 O OG  . SER A 162 ? 0.7917 1.3809 0.7783 -0.1009 -0.1434 -0.1024 162 SER A OG  
1295 N N   . TYR A 163 ? 0.7287 1.1868 0.6700 -0.1254 -0.1139 -0.1494 163 TYR A N   
1296 C CA  . TYR A 163 ? 0.7255 1.1523 0.6461 -0.1216 -0.1060 -0.1551 163 TYR A CA  
1297 C C   . TYR A 163 ? 0.7042 1.1220 0.6076 -0.1374 -0.1014 -0.1751 163 TYR A C   
1298 O O   . TYR A 163 ? 0.6591 1.0776 0.5389 -0.1334 -0.0997 -0.1746 163 TYR A O   
1299 C CB  . TYR A 163 ? 0.5727 0.9607 0.5047 -0.1193 -0.0968 -0.1601 163 TYR A CB  
1300 C CG  . TYR A 163 ? 0.5613 0.9167 0.4741 -0.1179 -0.0868 -0.1697 163 TYR A CG  
1301 C CD1 . TYR A 163 ? 0.5491 0.9074 0.4413 -0.1037 -0.0865 -0.1561 163 TYR A CD1 
1302 C CD2 . TYR A 163 ? 0.6281 0.9465 0.5447 -0.1291 -0.0759 -0.1899 163 TYR A CD2 
1303 C CE1 . TYR A 163 ? 0.6135 0.9429 0.4899 -0.1023 -0.0752 -0.1634 163 TYR A CE1 
1304 C CE2 . TYR A 163 ? 0.6008 0.8916 0.5024 -0.1262 -0.0654 -0.1989 163 TYR A CE2 
1305 C CZ  . TYR A 163 ? 0.6337 0.9317 0.5157 -0.1132 -0.0646 -0.1857 163 TYR A CZ  
1306 O OH  . TYR A 163 ? 0.5585 0.8321 0.4275 -0.1107 -0.0528 -0.1937 163 TYR A OH  
1307 N N   . ARG A 164 ? 0.7278 1.1364 0.6425 -0.1552 -0.0988 -0.1924 164 ARG A N   
1308 C CA  . ARG A 164 ? 0.7533 1.1508 0.6529 -0.1694 -0.0940 -0.2129 164 ARG A CA  
1309 C C   . ARG A 164 ? 0.7267 1.1618 0.6065 -0.1702 -0.1022 -0.2090 164 ARG A C   
1310 O O   . ARG A 164 ? 0.7660 1.1951 0.6238 -0.1723 -0.0976 -0.2182 164 ARG A O   
1311 C CB  . ARG A 164 ? 0.7752 1.1592 0.6908 -0.1880 -0.0921 -0.2290 164 ARG A CB  
1312 N N   . GLU A 165 ? 0.7588 1.2342 0.6467 -0.1677 -0.1140 -0.1948 165 GLU A N   
1313 C CA  . GLU A 165 ? 0.7212 1.2338 0.5911 -0.1668 -0.1229 -0.1883 165 GLU A CA  
1314 C C   . GLU A 165 ? 0.7691 1.2798 0.6166 -0.1508 -0.1217 -0.1742 165 GLU A C   
1315 O O   . GLU A 165 ? 0.8023 1.3191 0.6261 -0.1547 -0.1208 -0.1796 165 GLU A O   
1316 C CB  . GLU A 165 ? 0.7024 1.2578 0.5887 -0.1634 -0.1354 -0.1730 165 GLU A CB  
1317 N N   . LEU A 166 ? 0.7269 1.2287 0.5810 -0.1330 -0.1214 -0.1559 166 LEU A N   
1318 C CA  . LEU A 166 ? 0.6895 1.1846 0.5220 -0.1184 -0.1195 -0.1414 166 LEU A CA  
1319 C C   . LEU A 166 ? 0.6948 1.1591 0.5089 -0.1259 -0.1066 -0.1590 166 LEU A C   
1320 O O   . LEU A 166 ? 0.7763 1.2471 0.5656 -0.1249 -0.1052 -0.1564 166 LEU A O   
1321 C CB  . LEU A 166 ? 0.7100 1.1937 0.5541 -0.0993 -0.1200 -0.1218 166 LEU A CB  
1322 C CG  . LEU A 166 ? 0.6173 1.0949 0.4393 -0.0832 -0.1194 -0.1020 166 LEU A CG  
1323 C CD1 . LEU A 166 ? 0.7549 1.2666 0.5661 -0.0751 -0.1310 -0.0825 166 LEU A CD1 
1324 C CD2 . LEU A 166 ? 0.6353 1.0927 0.4677 -0.0663 -0.1174 -0.0873 166 LEU A CD2 
1325 N N   . ARG A 167 ? 0.6721 1.1033 0.4993 -0.1331 -0.0966 -0.1769 167 ARG A N   
1326 C CA  . ARG A 167 ? 0.6684 1.0676 0.4831 -0.1372 -0.0829 -0.1936 167 ARG A CA  
1327 C C   . ARG A 167 ? 0.7806 1.1908 0.5762 -0.1498 -0.0810 -0.2094 167 ARG A C   
1328 O O   . ARG A 167 ? 0.7416 1.1510 0.5149 -0.1470 -0.0752 -0.2094 167 ARG A O   
1329 C CB  . ARG A 167 ? 0.6630 1.0254 0.4991 -0.1426 -0.0740 -0.2095 167 ARG A CB  
1330 C CG  . ARG A 167 ? 0.6806 1.0065 0.5104 -0.1415 -0.0589 -0.2236 167 ARG A CG  
1331 C CD  . ARG A 167 ? 0.6958 0.9855 0.5493 -0.1466 -0.0520 -0.2376 167 ARG A CD  
1332 N NE  . ARG A 167 ? 0.6503 0.9036 0.5049 -0.1402 -0.0382 -0.2456 167 ARG A NE  
1333 C CZ  . ARG A 167 ? 0.6576 0.8965 0.5018 -0.1429 -0.0277 -0.2615 167 ARG A CZ  
1334 N NH1 . ARG A 167 ? 0.6082 0.8643 0.4376 -0.1529 -0.0294 -0.2727 167 ARG A NH1 
1335 N NH2 . ARG A 167 ? 0.6600 0.8680 0.5101 -0.1349 -0.0154 -0.2666 167 ARG A NH2 
1336 N N   . THR A 168 ? 0.7234 1.1447 0.5271 -0.1643 -0.0856 -0.2233 168 THR A N   
1337 C CA  . THR A 168 ? 0.7712 1.2051 0.5561 -0.1768 -0.0850 -0.2394 168 THR A CA  
1338 C C   . THR A 168 ? 0.7885 1.2606 0.5510 -0.1718 -0.0939 -0.2229 168 THR A C   
1339 O O   . THR A 168 ? 0.8206 1.2978 0.5596 -0.1757 -0.0896 -0.2304 168 THR A O   
1340 C CB  . THR A 168 ? 0.8129 1.2531 0.6107 -0.1940 -0.0898 -0.2556 168 THR A CB  
1341 O OG1 . THR A 168 ? 0.9864 1.4698 0.7870 -0.1951 -0.1044 -0.2415 168 THR A OG1 
1342 C CG2 . THR A 168 ? 0.6481 1.0554 0.4721 -0.1975 -0.0847 -0.2634 168 THR A CG2 
1343 N N   . GLN A 169 ? 0.7665 1.2663 0.5363 -0.1630 -0.1064 -0.2002 169 GLN A N   
1344 C CA  . GLN A 169 ? 0.8136 1.3482 0.5637 -0.1568 -0.1159 -0.1820 169 GLN A CA  
1345 C C   . GLN A 169 ? 0.8525 1.3754 0.5821 -0.1435 -0.1100 -0.1667 169 GLN A C   
1346 O O   . GLN A 169 ? 0.9151 1.4600 0.6223 -0.1411 -0.1147 -0.1552 169 GLN A O   
1347 C CB  . GLN A 169 ? 0.8407 1.4065 0.6078 -0.1492 -0.1304 -0.1621 169 GLN A CB  
1348 C CG  . GLN A 169 ? 1.0101 1.6007 0.7877 -0.1660 -0.1376 -0.1770 169 GLN A CG  
1349 C CD  . GLN A 169 ? 1.1106 1.7365 0.9076 -0.1597 -0.1511 -0.1596 169 GLN A CD  
1350 O OE1 . GLN A 169 ? 1.0968 1.7294 0.8996 -0.1410 -0.1560 -0.1356 169 GLN A OE1 
1351 N NE2 . GLN A 169 ? 1.2010 1.8500 1.0081 -0.1752 -0.1571 -0.1721 169 GLN A NE2 
1352 N N   . ILE A 170 ? 0.8214 1.3107 0.5577 -0.1355 -0.1000 -0.1655 170 ILE A N   
1353 C CA  . ILE A 170 ? 0.6471 1.1230 0.3627 -0.1266 -0.0918 -0.1549 170 ILE A CA  
1354 C C   . ILE A 170 ? 0.7333 1.1958 0.4331 -0.1377 -0.0785 -0.1781 170 ILE A C   
1355 O O   . ILE A 170 ? 0.8183 1.2918 0.4929 -0.1379 -0.0758 -0.1730 170 ILE A O   
1356 C CB  . ILE A 170 ? 0.7063 1.1538 0.4347 -0.1135 -0.0865 -0.1439 170 ILE A CB  
1357 C CG1 . ILE A 170 ? 0.6406 1.1033 0.3769 -0.0980 -0.0991 -0.1150 170 ILE A CG1 
1358 C CG2 . ILE A 170 ? 0.6874 1.1148 0.3966 -0.1096 -0.0735 -0.1416 170 ILE A CG2 
1359 C CD1 . ILE A 170 ? 0.6077 1.0446 0.3596 -0.0859 -0.0955 -0.1060 170 ILE A CD1 
1360 N N   . LEU A 171 ? 0.6667 1.1050 0.3816 -0.1467 -0.0698 -0.2035 171 LEU A N   
1361 C CA  . LEU A 171 ? 0.7179 1.1363 0.4228 -0.1531 -0.0547 -0.2255 171 LEU A CA  
1362 C C   . LEU A 171 ? 0.8897 1.3298 0.5757 -0.1660 -0.0560 -0.2408 171 LEU A C   
1363 O O   . LEU A 171 ? 0.8456 1.2787 0.5159 -0.1689 -0.0444 -0.2536 171 LEU A O   
1364 C CB  . LEU A 171 ? 0.7725 1.1546 0.5016 -0.1563 -0.0457 -0.2458 171 LEU A CB  
1365 C CG  . LEU A 171 ? 0.7720 1.1271 0.5182 -0.1443 -0.0407 -0.2356 171 LEU A CG  
1366 C CD1 . LEU A 171 ? 0.7076 1.0246 0.4747 -0.1474 -0.0299 -0.2568 171 LEU A CD1 
1367 C CD2 . LEU A 171 ? 0.7100 1.0633 0.4396 -0.1334 -0.0336 -0.2205 171 LEU A CD2 
1368 N N   . GLN A 172 ? 0.8069 1.2747 0.4942 -0.1739 -0.0693 -0.2403 172 GLN A N   
1369 C CA  . GLN A 172 ? 0.7884 1.2803 0.4553 -0.1865 -0.0718 -0.2537 172 GLN A CA  
1370 C C   . GLN A 172 ? 0.9129 1.4229 0.5502 -0.1814 -0.0700 -0.2400 172 GLN A C   
1371 O O   . GLN A 172 ? 0.9293 1.4455 0.5465 -0.1896 -0.0635 -0.2554 172 GLN A O   
1372 C CB  . GLN A 172 ? 0.7976 1.3218 0.4711 -0.1940 -0.0882 -0.2498 172 GLN A CB  
1373 N N   . TYR A 173 ? 0.8662 1.3830 0.5004 -0.1678 -0.0753 -0.2107 173 TYR A N   
1374 C CA  . TYR A 173 ? 0.9427 1.4765 0.5502 -0.1613 -0.0763 -0.1896 173 TYR A CA  
1375 C C   . TYR A 173 ? 0.9872 1.5016 0.5794 -0.1602 -0.0591 -0.1958 173 TYR A C   
1376 O O   . TYR A 173 ? 1.0119 1.5402 0.5796 -0.1574 -0.0583 -0.1798 173 TYR A O   
1377 C CB  . TYR A 173 ? 0.9124 1.4493 0.5268 -0.1456 -0.0862 -0.1567 173 TYR A CB  
1378 C CG  . TYR A 173 ? 1.0377 1.6072 0.6579 -0.1448 -0.1044 -0.1441 173 TYR A CG  
1379 C CD1 . TYR A 173 ? 0.9660 1.5394 0.6119 -0.1500 -0.1110 -0.1556 173 TYR A CD1 
1380 C CD2 . TYR A 173 ? 1.1407 1.7377 0.7412 -0.1392 -0.1148 -0.1206 173 TYR A CD2 
1381 C CE1 . TYR A 173 ? 1.0142 1.6210 0.6674 -0.1493 -0.1270 -0.1444 173 TYR A CE1 
1382 C CE2 . TYR A 173 ? 1.1076 1.7363 0.7151 -0.1372 -0.1315 -0.1091 173 TYR A CE2 
1383 C CZ  . TYR A 173 ? 1.1353 1.7703 0.7698 -0.1423 -0.1374 -0.1214 173 TYR A CZ  
1384 O OH  . TYR A 173 ? 0.9814 1.6511 0.6244 -0.1402 -0.1533 -0.1098 173 TYR A OH  
1385 N N   . MET A 174 ? 0.9840 1.4681 0.5901 -0.1625 -0.0452 -0.2179 174 MET A N   
1386 C CA  . MET A 174 ? 1.0401 1.5074 0.6361 -0.1590 -0.0285 -0.2209 174 MET A CA  
1387 C C   . MET A 174 ? 0.9576 1.4276 0.5404 -0.1696 -0.0175 -0.2483 174 MET A C   
1388 O O   . MET A 174 ? 1.1148 1.5813 0.7062 -0.1788 -0.0184 -0.2723 174 MET A O   
1389 C CB  . MET A 174 ? 0.9640 1.3953 0.5849 -0.1511 -0.0189 -0.2248 174 MET A CB  
1390 C CG  . MET A 174 ? 0.9146 1.3398 0.5432 -0.1386 -0.0251 -0.1963 174 MET A CG  
1391 S SD  . MET A 174 ? 0.9439 1.3281 0.5993 -0.1313 -0.0120 -0.2051 174 MET A SD  
1392 C CE  . MET A 174 ? 0.8820 1.2596 0.5223 -0.1323 0.0080  -0.2149 174 MET A CE  
1393 N N   . ARG B 4   ? 0.8911 0.8074 0.9127 -0.0399 -0.0331 0.1067  4   ARG B N   
1394 C CA  . ARG B 4   ? 0.8183 0.7058 0.8569 -0.0424 -0.0356 0.1116  4   ARG B CA  
1395 C C   . ARG B 4   ? 0.5453 0.4215 0.5991 -0.0324 -0.0368 0.0946  4   ARG B C   
1396 O O   . ARG B 4   ? 0.5725 0.4250 0.6398 -0.0282 -0.0408 0.0966  4   ARG B O   
1397 C CB  . ARG B 4   ? 0.7449 0.6296 0.7881 -0.0579 -0.0292 0.1158  4   ARG B CB  
1398 N N   . HIS B 5   ? 0.5162 0.4091 0.5679 -0.0282 -0.0330 0.0782  5   HIS B N   
1399 C CA  . HIS B 5   ? 0.4510 0.3352 0.5148 -0.0200 -0.0334 0.0632  5   HIS B CA  
1400 C C   . HIS B 5   ? 0.4757 0.3597 0.5386 -0.0084 -0.0392 0.0612  5   HIS B C   
1401 O O   . HIS B 5   ? 0.3606 0.2339 0.4361 -0.0018 -0.0407 0.0535  5   HIS B O   
1402 C CB  . HIS B 5   ? 0.4968 0.3975 0.5590 -0.0205 -0.0274 0.0483  5   HIS B CB  
1403 C CG  . HIS B 5   ? 0.5769 0.4786 0.6457 -0.0317 -0.0226 0.0462  5   HIS B CG  
1404 N ND1 . HIS B 5   ? 0.6341 0.5483 0.7060 -0.0323 -0.0187 0.0329  5   HIS B ND1 
1405 C CD2 . HIS B 5   ? 0.5642 0.4560 0.6371 -0.0438 -0.0216 0.0560  5   HIS B CD2 
1406 C CE1 . HIS B 5   ? 0.6150 0.5295 0.6931 -0.0448 -0.0159 0.0334  5   HIS B CE1 
1407 N NE2 . HIS B 5   ? 0.6527 0.5523 0.7316 -0.0526 -0.0171 0.0470  5   HIS B NE2 
1408 N N   . SER B 6   ? 0.4728 0.3702 0.5212 -0.0067 -0.0422 0.0670  6   SER B N   
1409 C CA  . SER B 6   ? 0.4590 0.3600 0.5059 0.0021  -0.0474 0.0619  6   SER B CA  
1410 C C   . SER B 6   ? 0.5555 0.4676 0.5862 0.0013  -0.0528 0.0727  6   SER B C   
1411 O O   . SER B 6   ? 0.4985 0.4177 0.5171 -0.0056 -0.0510 0.0829  6   SER B O   
1412 C CB  . SER B 6   ? 0.4631 0.3731 0.5067 0.0058  -0.0429 0.0454  6   SER B CB  
1413 O OG  . SER B 6   ? 0.5224 0.4483 0.5497 0.0031  -0.0387 0.0436  6   SER B OG  
1414 N N   . VAL B 7   ? 0.3691 0.2845 0.3993 0.0073  -0.0595 0.0704  7   VAL B N   
1415 C CA  . VAL B 7   ? 0.4568 0.3851 0.4700 0.0065  -0.0658 0.0776  7   VAL B CA  
1416 C C   . VAL B 7   ? 0.4612 0.3984 0.4671 0.0097  -0.0659 0.0620  7   VAL B C   
1417 O O   . VAL B 7   ? 0.4287 0.3600 0.4480 0.0140  -0.0664 0.0525  7   VAL B O   
1418 C CB  . VAL B 7   ? 0.4665 0.3905 0.4877 0.0096  -0.0765 0.0925  7   VAL B CB  
1419 C CG1 . VAL B 7   ? 0.5731 0.5144 0.5761 0.0088  -0.0847 0.0971  7   VAL B CG1 
1420 C CG2 . VAL B 7   ? 0.4681 0.3793 0.4934 0.0058  -0.0764 0.1101  7   VAL B CG2 
1421 N N   . VAL B 8   ? 0.4672 0.4175 0.4514 0.0069  -0.0644 0.0585  8   VAL B N   
1422 C CA  . VAL B 8   ? 0.4146 0.3696 0.3892 0.0091  -0.0644 0.0433  8   VAL B CA  
1423 C C   . VAL B 8   ? 0.4829 0.4483 0.4445 0.0070  -0.0741 0.0474  8   VAL B C   
1424 O O   . VAL B 8   ? 0.4507 0.4264 0.3976 0.0031  -0.0765 0.0585  8   VAL B O   
1425 C CB  . VAL B 8   ? 0.4666 0.4276 0.4265 0.0092  -0.0547 0.0327  8   VAL B CB  
1426 C CG1 . VAL B 8   ? 0.4631 0.4241 0.4114 0.0115  -0.0555 0.0174  8   VAL B CG1 
1427 C CG2 . VAL B 8   ? 0.4960 0.4503 0.4695 0.0114  -0.0466 0.0279  8   VAL B CG2 
1428 N N   . ARG B 9   ? 0.4618 0.4264 0.4285 0.0084  -0.0799 0.0391  9   ARG B N   
1429 C CA  . ARG B 9   ? 0.4921 0.4691 0.4457 0.0050  -0.0897 0.0394  9   ARG B CA  
1430 C C   . ARG B 9   ? 0.5081 0.4831 0.4508 0.0034  -0.0875 0.0200  9   ARG B C   
1431 O O   . ARG B 9   ? 0.4578 0.4204 0.4108 0.0059  -0.0817 0.0096  9   ARG B O   
1432 C CB  . ARG B 9   ? 0.4862 0.4668 0.4588 0.0068  -0.1009 0.0494  9   ARG B CB  
1433 C CG  . ARG B 9   ? 0.4565 0.4306 0.4504 0.0093  -0.1007 0.0393  9   ARG B CG  
1434 C CD  . ARG B 9   ? 0.6059 0.5890 0.6199 0.0122  -0.1116 0.0492  9   ARG B CD  
1435 N NE  . ARG B 9   ? 0.5099 0.4914 0.5453 0.0138  -0.1106 0.0397  9   ARG B NE  
1436 C CZ  . ARG B 9   ? 0.6107 0.5805 0.6655 0.0189  -0.1032 0.0377  9   ARG B CZ  
1437 N NH1 . ARG B 9   ? 0.4712 0.4280 0.5272 0.0222  -0.0963 0.0429  9   ARG B NH1 
1438 N NH2 . ARG B 9   ? 0.5499 0.5226 0.6230 0.0195  -0.1026 0.0299  9   ARG B NH2 
1439 N N   . VAL B 10  ? 0.4566 0.4422 0.3762 -0.0012 -0.0914 0.0151  10  VAL B N   
1440 C CA  . VAL B 10  ? 0.5007 0.4811 0.4063 -0.0035 -0.0891 -0.0043 10  VAL B CA  
1441 C C   . VAL B 10  ? 0.6316 0.6197 0.5382 -0.0098 -0.1014 -0.0073 10  VAL B C   
1442 O O   . VAL B 10  ? 0.5748 0.5803 0.4714 -0.0138 -0.1111 0.0010  10  VAL B O   
1443 C CB  . VAL B 10  ? 0.5730 0.5596 0.4503 -0.0042 -0.0829 -0.0118 10  VAL B CB  
1444 C CG1 . VAL B 10  ? 0.6095 0.5867 0.4720 -0.0062 -0.0814 -0.0335 10  VAL B CG1 
1445 C CG2 . VAL B 10  ? 0.5328 0.5159 0.4129 0.0017  -0.0705 -0.0094 10  VAL B CG2 
1446 N N   . GLU B 11  ? 0.5445 0.5215 0.4630 -0.0114 -0.1014 -0.0183 11  GLU B N   
1447 C CA  . GLU B 11  ? 0.5924 0.5780 0.5155 -0.0191 -0.1125 -0.0227 11  GLU B CA  
1448 C C   . GLU B 11  ? 0.6407 0.6108 0.5505 -0.0248 -0.1088 -0.0433 11  GLU B C   
1449 O O   . GLU B 11  ? 0.5876 0.5400 0.5091 -0.0235 -0.1024 -0.0498 11  GLU B O   
1450 C CB  . GLU B 11  ? 0.5948 0.5831 0.5498 -0.0169 -0.1160 -0.0141 11  GLU B CB  
1451 C CG  . GLU B 11  ? 0.6500 0.6501 0.6180 -0.0105 -0.1206 0.0058  11  GLU B CG  
1452 C CD  . GLU B 11  ? 0.8291 0.8325 0.8295 -0.0063 -0.1234 0.0127  11  GLU B CD  
1453 O OE1 . GLU B 11  ? 0.7847 0.7833 0.7975 -0.0092 -0.1207 0.0026  11  GLU B OE1 
1454 O OE2 . GLU B 11  ? 0.7873 0.7975 0.8006 0.0000  -0.1277 0.0285  11  GLU B OE2 
1455 N N   . GLY B 12  ? 0.6317 0.6064 0.5153 -0.0307 -0.1119 -0.0537 12  GLY B N   
1456 C CA  . GLY B 12  ? 0.5862 0.5411 0.4564 -0.0356 -0.1079 -0.0745 12  GLY B CA  
1457 C C   . GLY B 12  ? 0.5845 0.5177 0.4484 -0.0256 -0.0934 -0.0811 12  GLY B C   
1458 O O   . GLY B 12  ? 0.6319 0.5713 0.4852 -0.0183 -0.0871 -0.0771 12  GLY B O   
1459 N N   . ASP B 13  ? 0.5264 0.4354 0.3978 -0.0252 -0.0880 -0.0903 13  ASP B N   
1460 C CA  . ASP B 13  ? 0.5574 0.4465 0.4248 -0.0143 -0.0754 -0.0956 13  ASP B CA  
1461 C C   . ASP B 13  ? 0.4939 0.3825 0.3843 -0.0064 -0.0703 -0.0820 13  ASP B C   
1462 O O   . ASP B 13  ? 0.5032 0.3747 0.3958 0.0014  -0.0615 -0.0853 13  ASP B O   
1463 C CB  . ASP B 13  ? 0.5729 0.4326 0.4323 -0.0172 -0.0722 -0.1127 13  ASP B CB  
1464 C CG  . ASP B 13  ? 0.7156 0.5661 0.5935 -0.0263 -0.0766 -0.1106 13  ASP B CG  
1465 O OD1 . ASP B 13  ? 0.6676 0.5337 0.5671 -0.0269 -0.0798 -0.0964 13  ASP B OD1 
1466 O OD2 . ASP B 13  ? 0.8929 0.7207 0.7638 -0.0336 -0.0767 -0.1234 13  ASP B OD2 
1467 N N   . ARG B 14  ? 0.4645 0.3710 0.3718 -0.0080 -0.0759 -0.0672 14  ARG B N   
1468 C CA  . ARG B 14  ? 0.4950 0.4013 0.4229 -0.0013 -0.0711 -0.0559 14  ARG B CA  
1469 C C   . ARG B 14  ? 0.4775 0.4008 0.4075 0.0027  -0.0713 -0.0425 14  ARG B C   
1470 O O   . ARG B 14  ? 0.4597 0.3990 0.3846 -0.0013 -0.0790 -0.0358 14  ARG B O   
1471 C CB  . ARG B 14  ? 0.4867 0.3941 0.4372 -0.0062 -0.0757 -0.0513 14  ARG B CB  
1472 C CG  . ARG B 14  ? 0.6125 0.4988 0.5640 -0.0088 -0.0714 -0.0612 14  ARG B CG  
1473 C CD  . ARG B 14  ? 0.6615 0.5523 0.6279 -0.0187 -0.0775 -0.0612 14  ARG B CD  
1474 N NE  . ARG B 14  ? 0.7421 0.6388 0.7318 -0.0154 -0.0748 -0.0519 14  ARG B NE  
1475 C CZ  . ARG B 14  ? 0.6769 0.5644 0.6774 -0.0187 -0.0706 -0.0535 14  ARG B CZ  
1476 N NH1 . ARG B 14  ? 0.6271 0.4961 0.6179 -0.0257 -0.0689 -0.0625 14  ARG B NH1 
1477 N NH2 . ARG B 14  ? 0.6259 0.5217 0.6463 -0.0151 -0.0676 -0.0461 14  ARG B NH2 
1478 N N   . ALA B 15  ? 0.4260 0.3458 0.3629 0.0099  -0.0631 -0.0381 15  ALA B N   
1479 C CA  . ALA B 15  ? 0.4384 0.3701 0.3819 0.0123  -0.0623 -0.0245 15  ALA B CA  
1480 C C   . ALA B 15  ? 0.4368 0.3647 0.4049 0.0137  -0.0626 -0.0172 15  ALA B C   
1481 O O   . ALA B 15  ? 0.3948 0.3116 0.3710 0.0163  -0.0574 -0.0226 15  ALA B O   
1482 C CB  . ALA B 15  ? 0.4370 0.3706 0.3714 0.0178  -0.0527 -0.0258 15  ALA B CB  
1483 N N   . ILE B 16  ? 0.3856 0.3224 0.3648 0.0124  -0.0687 -0.0050 16  ILE B N   
1484 C CA  . ILE B 16  ? 0.3586 0.2921 0.3615 0.0146  -0.0690 0.0005  16  ILE B CA  
1485 C C   . ILE B 16  ? 0.4202 0.3541 0.4287 0.0169  -0.0661 0.0114  16  ILE B C   
1486 O O   . ILE B 16  ? 0.4068 0.3479 0.4102 0.0154  -0.0707 0.0224  16  ILE B O   
1487 C CB  . ILE B 16  ? 0.4264 0.3683 0.4418 0.0124  -0.0787 0.0046  16  ILE B CB  
1488 C CG1 . ILE B 16  ? 0.5006 0.4430 0.5070 0.0068  -0.0818 -0.0069 16  ILE B CG1 
1489 C CG2 . ILE B 16  ? 0.4442 0.3830 0.4847 0.0161  -0.0770 0.0070  16  ILE B CG2 
1490 C CD1 . ILE B 16  ? 0.5736 0.5286 0.5939 0.0030  -0.0915 -0.0048 16  ILE B CD1 
1491 N N   . LYS B 17  ? 0.3534 0.2795 0.3711 0.0194  -0.0587 0.0088  17  LYS B N   
1492 C CA  . LYS B 17  ? 0.4003 0.3250 0.4230 0.0195  -0.0550 0.0166  17  LYS B CA  
1493 C C   . LYS B 17  ? 0.3899 0.3072 0.4344 0.0215  -0.0560 0.0200  17  LYS B C   
1494 O O   . LYS B 17  ? 0.3552 0.2681 0.4094 0.0235  -0.0530 0.0117  17  LYS B O   
1495 C CB  . LYS B 17  ? 0.3998 0.3237 0.4165 0.0203  -0.0463 0.0095  17  LYS B CB  
1496 C CG  . LYS B 17  ? 0.3865 0.3118 0.4074 0.0179  -0.0420 0.0159  17  LYS B CG  
1497 C CD  . LYS B 17  ? 0.4135 0.3449 0.4278 0.0193  -0.0345 0.0084  17  LYS B CD  
1498 C CE  . LYS B 17  ? 0.5818 0.5239 0.5921 0.0148  -0.0306 0.0150  17  LYS B CE  
1499 N NZ  . LYS B 17  ? 0.5318 0.4848 0.5379 0.0178  -0.0237 0.0073  17  LYS B NZ  
1500 N N   . GLN B 18  ? 0.3249 0.2405 0.3767 0.0215  -0.0602 0.0320  18  GLN B N   
1501 C CA  . GLN B 18  ? 0.3593 0.2655 0.4325 0.0251  -0.0607 0.0344  18  GLN B CA  
1502 C C   . GLN B 18  ? 0.3417 0.2375 0.4180 0.0224  -0.0566 0.0403  18  GLN B C   
1503 O O   . GLN B 18  ? 0.3686 0.2646 0.4366 0.0187  -0.0588 0.0522  18  GLN B O   
1504 C CB  . GLN B 18  ? 0.3163 0.2262 0.4001 0.0291  -0.0701 0.0436  18  GLN B CB  
1505 C CG  . GLN B 18  ? 0.3732 0.2744 0.4819 0.0356  -0.0693 0.0424  18  GLN B CG  
1506 C CD  . GLN B 18  ? 0.3788 0.2864 0.5026 0.0422  -0.0785 0.0511  18  GLN B CD  
1507 O OE1 . GLN B 18  ? 0.4309 0.3465 0.5467 0.0416  -0.0872 0.0629  18  GLN B OE1 
1508 N NE2 . GLN B 18  ? 0.3714 0.2773 0.5178 0.0491  -0.0767 0.0457  18  GLN B NE2 
1509 N N   . PHE B 19  ? 0.3071 0.1940 0.3948 0.0230  -0.0507 0.0321  19  PHE B N   
1510 C CA  . PHE B 19  ? 0.3372 0.2128 0.4293 0.0186  -0.0464 0.0342  19  PHE B CA  
1511 C C   . PHE B 19  ? 0.3368 0.1958 0.4466 0.0223  -0.0490 0.0401  19  PHE B C   
1512 O O   . PHE B 19  ? 0.3437 0.2015 0.4671 0.0300  -0.0515 0.0371  19  PHE B O   
1513 C CB  . PHE B 19  ? 0.3168 0.1927 0.4105 0.0168  -0.0390 0.0203  19  PHE B CB  
1514 C CG  . PHE B 19  ? 0.3495 0.2393 0.4280 0.0146  -0.0358 0.0152  19  PHE B CG  
1515 C CD1 . PHE B 19  ? 0.3224 0.2197 0.3939 0.0188  -0.0368 0.0097  19  PHE B CD1 
1516 C CD2 . PHE B 19  ? 0.3335 0.2287 0.4059 0.0084  -0.0317 0.0157  19  PHE B CD2 
1517 C CE1 . PHE B 19  ? 0.3689 0.2757 0.4268 0.0186  -0.0336 0.0048  19  PHE B CE1 
1518 C CE2 . PHE B 19  ? 0.3687 0.2783 0.4291 0.0088  -0.0285 0.0109  19  PHE B CE2 
1519 C CZ  . PHE B 19  ? 0.3591 0.2728 0.4121 0.0148  -0.0295 0.0056  19  PHE B CZ  
1520 N N   . PHE B 20  ? 0.3467 0.1924 0.4576 0.0167  -0.0479 0.0480  20  PHE B N   
1521 C CA  . PHE B 20  ? 0.3680 0.1920 0.4964 0.0204  -0.0486 0.0503  20  PHE B CA  
1522 C C   . PHE B 20  ? 0.3305 0.1487 0.4688 0.0213  -0.0417 0.0322  20  PHE B C   
1523 O O   . PHE B 20  ? 0.3416 0.1699 0.4713 0.0156  -0.0365 0.0218  20  PHE B O   
1524 C CB  . PHE B 20  ? 0.3498 0.1567 0.4760 0.0120  -0.0486 0.0631  20  PHE B CB  
1525 C CG  . PHE B 20  ? 0.4216 0.2318 0.5379 0.0109  -0.0556 0.0837  20  PHE B CG  
1526 C CD1 . PHE B 20  ? 0.4332 0.2332 0.5593 0.0201  -0.0635 0.0966  20  PHE B CD1 
1527 C CD2 . PHE B 20  ? 0.5124 0.3378 0.6094 0.0012  -0.0541 0.0904  20  PHE B CD2 
1528 C CE1 . PHE B 20  ? 0.4853 0.2897 0.6001 0.0188  -0.0708 0.1171  20  PHE B CE1 
1529 C CE2 . PHE B 20  ? 0.5079 0.3383 0.5931 -0.0007 -0.0600 0.1092  20  PHE B CE2 
1530 C CZ  . PHE B 20  ? 0.5641 0.3837 0.6572 0.0076  -0.0688 0.1232  20  PHE B CZ  
1531 N N   . PRO B 21  ? 0.3846 0.1886 0.5406 0.0293  -0.0414 0.0280  21  PRO B N   
1532 C CA  . PRO B 21  ? 0.3866 0.1908 0.5458 0.0292  -0.0332 0.0093  21  PRO B CA  
1533 C C   . PRO B 21  ? 0.3948 0.1889 0.5488 0.0177  -0.0283 0.0029  21  PRO B C   
1534 O O   . PRO B 21  ? 0.4243 0.2250 0.5762 0.0149  -0.0230 -0.0120 21  PRO B O   
1535 C CB  . PRO B 21  ? 0.4298 0.2260 0.6005 0.0386  -0.0323 0.0082  21  PRO B CB  
1536 C CG  . PRO B 21  ? 0.4508 0.2532 0.6267 0.0466  -0.0408 0.0234  21  PRO B CG  
1537 C CD  . PRO B 21  ? 0.3824 0.1826 0.5469 0.0386  -0.0465 0.0383  21  PRO B CD  
1538 N N   . ALA B 22  ? 0.3656 0.1452 0.5175 0.0097  -0.0303 0.0144  22  ALA B N   
1539 C CA  . ALA B 22  ? 0.4014 0.1736 0.5503 -0.0040 -0.0262 0.0084  22  ALA B CA  
1540 C C   . ALA B 22  ? 0.4038 0.2035 0.5392 -0.0101 -0.0238 0.0026  22  ALA B C   
1541 O O   . ALA B 22  ? 0.3801 0.1833 0.5130 -0.0196 -0.0200 -0.0071 22  ALA B O   
1542 C CB  . ALA B 22  ? 0.3969 0.1531 0.5440 -0.0137 -0.0286 0.0248  22  ALA B CB  
1543 N N   . TYR B 23  ? 0.3329 0.1523 0.4594 -0.0045 -0.0262 0.0077  23  TYR B N   
1544 C CA  . TYR B 23  ? 0.4006 0.2442 0.5141 -0.0080 -0.0241 0.0037  23  TYR B CA  
1545 C C   . TYR B 23  ? 0.3489 0.2040 0.4606 0.0005  -0.0231 -0.0066 23  TYR B C   
1546 O O   . TYR B 23  ? 0.3458 0.2174 0.4467 0.0025  -0.0233 -0.0063 23  TYR B O   
1547 C CB  . TYR B 23  ? 0.3458 0.2011 0.4478 -0.0102 -0.0267 0.0175  23  TYR B CB  
1548 C CG  . TYR B 23  ? 0.4192 0.2617 0.5229 -0.0195 -0.0275 0.0302  23  TYR B CG  
1549 C CD1 . TYR B 23  ? 0.4496 0.2898 0.5555 -0.0321 -0.0237 0.0272  23  TYR B CD1 
1550 C CD2 . TYR B 23  ? 0.4059 0.2381 0.5095 -0.0166 -0.0326 0.0457  23  TYR B CD2 
1551 C CE1 . TYR B 23  ? 0.4951 0.3212 0.6027 -0.0426 -0.0240 0.0396  23  TYR B CE1 
1552 C CE2 . TYR B 23  ? 0.5243 0.3420 0.6285 -0.0256 -0.0333 0.0594  23  TYR B CE2 
1553 C CZ  . TYR B 23  ? 0.5810 0.3945 0.6872 -0.0391 -0.0286 0.0564  23  TYR B CZ  
1554 O OH  . TYR B 23  ? 0.5867 0.3841 0.6933 -0.0499 -0.0290 0.0712  23  TYR B OH  
1555 N N   . ARG B 24  ? 0.3046 0.1499 0.4269 0.0056  -0.0215 -0.0158 24  ARG B N   
1556 C CA  . ARG B 24  ? 0.3180 0.1739 0.4390 0.0113  -0.0191 -0.0260 24  ARG B CA  
1557 C C   . ARG B 24  ? 0.3999 0.2715 0.5087 0.0067  -0.0163 -0.0324 24  ARG B C   
1558 O O   . ARG B 24  ? 0.3452 0.2283 0.4465 0.0108  -0.0160 -0.0341 24  ARG B O   
1559 C CB  . ARG B 24  ? 0.3943 0.2389 0.5285 0.0149  -0.0156 -0.0370 24  ARG B CB  
1560 C CG  . ARG B 24  ? 0.4607 0.3172 0.5940 0.0195  -0.0117 -0.0475 24  ARG B CG  
1561 C CD  . ARG B 24  ? 0.4793 0.3296 0.6253 0.0250  -0.0074 -0.0566 24  ARG B CD  
1562 N NE  . ARG B 24  ? 0.4972 0.3480 0.6538 0.0335  -0.0103 -0.0487 24  ARG B NE  
1563 C CZ  . ARG B 24  ? 0.6387 0.5022 0.8000 0.0387  -0.0110 -0.0481 24  ARG B CZ  
1564 N NH1 . ARG B 24  ? 0.4999 0.3741 0.6547 0.0367  -0.0080 -0.0544 24  ARG B NH1 
1565 N NH2 . ARG B 24  ? 0.5625 0.4276 0.7361 0.0459  -0.0151 -0.0406 24  ARG B NH2 
1566 N N   A TYR B 25  ? 0.3987 0.2706 0.5064 -0.0020 -0.0147 -0.0357 25  TYR B N   
1567 N N   B TYR B 25  ? 0.3992 0.2722 0.5063 -0.0019 -0.0148 -0.0354 25  TYR B N   
1568 C CA  A TYR B 25  ? 0.3955 0.2857 0.4939 -0.0063 -0.0132 -0.0405 25  TYR B CA  
1569 C CA  B TYR B 25  ? 0.3899 0.2816 0.4870 -0.0040 -0.0132 -0.0407 25  TYR B CA  
1570 C C   A TYR B 25  ? 0.4040 0.3090 0.4924 -0.0031 -0.0150 -0.0321 25  TYR B C   
1571 C C   B TYR B 25  ? 0.4044 0.3106 0.4921 -0.0031 -0.0150 -0.0319 25  TYR B C   
1572 O O   A TYR B 25  ? 0.3411 0.2592 0.4214 0.0009  -0.0144 -0.0350 25  TYR B O   
1573 O O   B TYR B 25  ? 0.3457 0.2666 0.4253 0.0001  -0.0144 -0.0344 25  TYR B O   
1574 C CB  A TYR B 25  ? 0.4119 0.3007 0.5135 -0.0181 -0.0122 -0.0442 25  TYR B CB  
1575 C CB  B TYR B 25  ? 0.4116 0.3049 0.5106 -0.0137 -0.0113 -0.0498 25  TYR B CB  
1576 C CG  A TYR B 25  ? 0.4235 0.3350 0.5183 -0.0237 -0.0118 -0.0489 25  TYR B CG  
1577 C CG  B TYR B 25  ? 0.4347 0.3168 0.5394 -0.0120 -0.0084 -0.0619 25  TYR B CG  
1578 C CD1 A TYR B 25  ? 0.4575 0.3775 0.5486 -0.0234 -0.0106 -0.0604 25  TYR B CD1 
1579 C CD1 B TYR B 25  ? 0.4214 0.3097 0.5224 -0.0044 -0.0065 -0.0667 25  TYR B CD1 
1580 C CD2 A TYR B 25  ? 0.4862 0.4130 0.5788 -0.0293 -0.0126 -0.0416 25  TYR B CD2 
1581 C CD2 B TYR B 25  ? 0.4677 0.3312 0.5817 -0.0175 -0.0069 -0.0682 25  TYR B CD2 
1582 C CE1 A TYR B 25  ? 0.4724 0.4158 0.5577 -0.0276 -0.0116 -0.0633 25  TYR B CE1 
1583 C CE1 B TYR B 25  ? 0.4228 0.3041 0.5290 -0.0025 -0.0025 -0.0780 25  TYR B CE1 
1584 C CE2 A TYR B 25  ? 0.5278 0.4791 0.6170 -0.0332 -0.0128 -0.0456 25  TYR B CE2 
1585 C CE2 B TYR B 25  ? 0.4587 0.3121 0.5780 -0.0145 -0.0031 -0.0811 25  TYR B CE2 
1586 C CZ  A TYR B 25  ? 0.5132 0.4727 0.5990 -0.0320 -0.0130 -0.0559 25  TYR B CZ  
1587 C CZ  B TYR B 25  ? 0.5095 0.3740 0.6251 -0.0068 -0.0006 -0.0861 25  TYR B CZ  
1588 O OH  A TYR B 25  ? 0.5991 0.5857 0.6819 -0.0349 -0.0145 -0.0585 25  TYR B OH  
1589 O OH  B TYR B 25  ? 0.6106 0.4686 0.7315 -0.0037 0.0045  -0.0995 25  TYR B OH  
1590 N N   . ASN B 26  ? 0.3153 0.2174 0.4032 -0.0042 -0.0170 -0.0214 26  ASN B N   
1591 C CA  . ASN B 26  ? 0.3019 0.2180 0.3794 -0.0014 -0.0177 -0.0150 26  ASN B CA  
1592 C C   . ASN B 26  ? 0.3538 0.2683 0.4256 0.0079  -0.0194 -0.0150 26  ASN B C   
1593 O O   . ASN B 26  ? 0.3339 0.2589 0.3960 0.0123  -0.0189 -0.0153 26  ASN B O   
1594 C CB  . ASN B 26  ? 0.3485 0.2637 0.4252 -0.0069 -0.0188 -0.0037 26  ASN B CB  
1595 C CG  . ASN B 26  ? 0.5348 0.4523 0.6166 -0.0188 -0.0167 -0.0026 26  ASN B CG  
1596 O OD1 . ASN B 26  ? 0.4911 0.3906 0.5814 -0.0247 -0.0173 -0.0009 26  ASN B OD1 
1597 N ND2 . ASN B 26  ? 0.4328 0.3727 0.5109 -0.0223 -0.0143 -0.0043 26  ASN B ND2 
1598 N N   . PHE B 27  ? 0.3092 0.2108 0.3881 0.0110  -0.0214 -0.0147 27  PHE B N   
1599 C CA  . PHE B 27  ? 0.2904 0.1914 0.3667 0.0175  -0.0230 -0.0162 27  PHE B CA  
1600 C C   . PHE B 27  ? 0.3228 0.2295 0.3934 0.0200  -0.0200 -0.0240 27  PHE B C   
1601 O O   . PHE B 27  ? 0.3094 0.2188 0.3706 0.0237  -0.0205 -0.0240 27  PHE B O   
1602 C CB  . PHE B 27  ? 0.3168 0.2075 0.4064 0.0198  -0.0248 -0.0161 27  PHE B CB  
1603 C CG  . PHE B 27  ? 0.2818 0.1746 0.3728 0.0242  -0.0250 -0.0204 27  PHE B CG  
1604 C CD1 . PHE B 27  ? 0.2939 0.1892 0.3813 0.0261  -0.0294 -0.0159 27  PHE B CD1 
1605 C CD2 . PHE B 27  ? 0.3005 0.1938 0.3962 0.0248  -0.0206 -0.0292 27  PHE B CD2 
1606 C CE1 . PHE B 27  ? 0.3007 0.1986 0.3910 0.0277  -0.0296 -0.0197 27  PHE B CE1 
1607 C CE2 . PHE B 27  ? 0.2896 0.1862 0.3871 0.0269  -0.0198 -0.0321 27  PHE B CE2 
1608 C CZ  . PHE B 27  ? 0.2976 0.1962 0.3934 0.0279  -0.0244 -0.0272 27  PHE B CZ  
1609 N N   . TRP B 28  ? 0.2917 0.1992 0.3664 0.0176  -0.0170 -0.0307 28  TRP B N   
1610 C CA  . TRP B 28  ? 0.2656 0.1792 0.3335 0.0198  -0.0147 -0.0362 28  TRP B CA  
1611 C C   . TRP B 28  ? 0.2955 0.2206 0.3531 0.0214  -0.0148 -0.0344 28  TRP B C   
1612 O O   . TRP B 28  ? 0.3476 0.2748 0.3968 0.0263  -0.0144 -0.0347 28  TRP B O   
1613 C CB  . TRP B 28  ? 0.2769 0.1907 0.3502 0.0164  -0.0116 -0.0445 28  TRP B CB  
1614 C CG  . TRP B 28  ? 0.3103 0.2155 0.3937 0.0179  -0.0098 -0.0485 28  TRP B CG  
1615 C CD1 . TRP B 28  ? 0.3113 0.2080 0.4070 0.0164  -0.0084 -0.0528 28  TRP B CD1 
1616 C CD2 . TRP B 28  ? 0.3051 0.2107 0.3884 0.0213  -0.0086 -0.0487 28  TRP B CD2 
1617 N NE1 . TRP B 28  ? 0.3264 0.2210 0.4308 0.0206  -0.0063 -0.0561 28  TRP B NE1 
1618 C CE2 . TRP B 28  ? 0.3344 0.2358 0.4316 0.0225  -0.0064 -0.0533 28  TRP B CE2 
1619 C CE3 . TRP B 28  ? 0.3144 0.2225 0.3879 0.0233  -0.0091 -0.0454 28  TRP B CE3 
1620 C CZ2 . TRP B 28  ? 0.3381 0.2429 0.4407 0.0248  -0.0044 -0.0546 28  TRP B CZ2 
1621 C CZ3 . TRP B 28  ? 0.3288 0.2367 0.4063 0.0237  -0.0074 -0.0463 28  TRP B CZ3 
1622 C CH2 . TRP B 28  ? 0.3028 0.2113 0.3953 0.0242  -0.0050 -0.0508 28  TRP B CH2 
1623 N N   . LYS B 29  ? 0.3028 0.2358 0.3617 0.0177  -0.0152 -0.0319 29  LYS B N   
1624 C CA  . LYS B 29  ? 0.3338 0.2821 0.3856 0.0210  -0.0149 -0.0302 29  LYS B CA  
1625 C C   . LYS B 29  ? 0.3909 0.3363 0.4342 0.0280  -0.0155 -0.0265 29  LYS B C   
1626 O O   . LYS B 29  ? 0.3978 0.3474 0.4337 0.0353  -0.0150 -0.0273 29  LYS B O   
1627 C CB  . LYS B 29  ? 0.3411 0.3023 0.3976 0.0140  -0.0144 -0.0283 29  LYS B CB  
1628 C CG  . LYS B 29  ? 0.3229 0.2896 0.3865 0.0052  -0.0140 -0.0336 29  LYS B CG  
1629 C CD  . LYS B 29  ? 0.4938 0.4751 0.5621 -0.0033 -0.0134 -0.0302 29  LYS B CD  
1630 C CE  . LYS B 29  ? 0.4834 0.4793 0.5570 -0.0126 -0.0138 -0.0367 29  LYS B CE  
1631 N NZ  . LYS B 29  ? 0.6075 0.6257 0.6769 -0.0067 -0.0151 -0.0397 29  LYS B NZ  
1632 N N   . GLU B 30  ? 0.3199 0.2576 0.3637 0.0263  -0.0169 -0.0227 30  GLU B N   
1633 C CA  . GLU B 30  ? 0.3939 0.3281 0.4281 0.0316  -0.0178 -0.0213 30  GLU B CA  
1634 C C   . GLU B 30  ? 0.4150 0.3381 0.4449 0.0361  -0.0184 -0.0249 30  GLU B C   
1635 O O   . GLU B 30  ? 0.3542 0.2753 0.3746 0.0423  -0.0177 -0.0266 30  GLU B O   
1636 C CB  . GLU B 30  ? 0.3681 0.2968 0.4031 0.0279  -0.0207 -0.0163 30  GLU B CB  
1637 C CG  . GLU B 30  ? 0.4248 0.3522 0.4474 0.0318  -0.0220 -0.0165 30  GLU B CG  
1638 C CD  . GLU B 30  ? 0.5584 0.4987 0.5732 0.0312  -0.0202 -0.0130 30  GLU B CD  
1639 O OE1 . GLU B 30  ? 0.6130 0.5593 0.6328 0.0248  -0.0201 -0.0065 30  GLU B OE1 
1640 O OE2 . GLU B 30  ? 0.6318 0.5762 0.6356 0.0368  -0.0181 -0.0172 30  GLU B OE2 
1641 N N   . ALA B 31  ? 0.3504 0.2655 0.3876 0.0330  -0.0191 -0.0263 31  ALA B N   
1642 C CA  . ALA B 31  ? 0.3429 0.2490 0.3764 0.0350  -0.0188 -0.0287 31  ALA B CA  
1643 C C   . ALA B 31  ? 0.3113 0.2197 0.3378 0.0394  -0.0166 -0.0299 31  ALA B C   
1644 O O   . ALA B 31  ? 0.3056 0.2051 0.3233 0.0435  -0.0165 -0.0298 31  ALA B O   
1645 C CB  . ALA B 31  ? 0.2861 0.1888 0.3307 0.0309  -0.0185 -0.0303 31  ALA B CB  
1646 N N   . GLY B 32  ? 0.2795 0.1990 0.3098 0.0382  -0.0153 -0.0308 32  GLY B N   
1647 C CA  . GLY B 32  ? 0.3004 0.2256 0.3246 0.0422  -0.0145 -0.0307 32  GLY B CA  
1648 C C   . GLY B 32  ? 0.3584 0.2877 0.3752 0.0509  -0.0149 -0.0284 32  GLY B C   
1649 O O   . GLY B 32  ? 0.3179 0.2400 0.3266 0.0575  -0.0150 -0.0266 32  GLY B O   
1650 N N   . PHE B 33  ? 0.2813 0.2221 0.3011 0.0514  -0.0148 -0.0282 33  PHE B N   
1651 C CA  . PHE B 33  ? 0.3318 0.2808 0.3465 0.0612  -0.0141 -0.0274 33  PHE B CA  
1652 C C   . PHE B 33  ? 0.3240 0.2555 0.3294 0.0672  -0.0136 -0.0286 33  PHE B C   
1653 O O   . PHE B 33  ? 0.3485 0.2758 0.3475 0.0777  -0.0130 -0.0286 33  PHE B O   
1654 C CB  . PHE B 33  ? 0.3215 0.2922 0.3427 0.0587  -0.0129 -0.0270 33  PHE B CB  
1655 C CG  . PHE B 33  ? 0.2930 0.2825 0.3223 0.0535  -0.0137 -0.0270 33  PHE B CG  
1656 C CD1 . PHE B 33  ? 0.3238 0.3248 0.3517 0.0605  -0.0152 -0.0263 33  PHE B CD1 
1657 C CD2 . PHE B 33  ? 0.3389 0.3331 0.3764 0.0415  -0.0137 -0.0276 33  PHE B CD2 
1658 C CE1 . PHE B 33  ? 0.3333 0.3541 0.3676 0.0543  -0.0170 -0.0273 33  PHE B CE1 
1659 C CE2 . PHE B 33  ? 0.3568 0.3667 0.4007 0.0350  -0.0147 -0.0297 33  PHE B CE2 
1660 C CZ  . PHE B 33  ? 0.4075 0.4324 0.4495 0.0409  -0.0166 -0.0301 33  PHE B CZ  
1661 N N   . LEU B 34  ? 0.2975 0.2180 0.3021 0.0611  -0.0145 -0.0298 34  LEU B N   
1662 C CA  . LEU B 34  ? 0.3144 0.2173 0.3090 0.0647  -0.0148 -0.0326 34  LEU B CA  
1663 C C   . LEU B 34  ? 0.3516 0.2364 0.3413 0.0672  -0.0151 -0.0322 34  LEU B C   
1664 O O   . LEU B 34  ? 0.3761 0.2471 0.3567 0.0749  -0.0144 -0.0340 34  LEU B O   
1665 C CB  . LEU B 34  ? 0.3452 0.2426 0.3404 0.0563  -0.0172 -0.0333 34  LEU B CB  
1666 C CG  . LEU B 34  ? 0.3229 0.2333 0.3170 0.0544  -0.0170 -0.0325 34  LEU B CG  
1667 C CD1 . LEU B 34  ? 0.3419 0.2475 0.3371 0.0464  -0.0211 -0.0309 34  LEU B CD1 
1668 C CD2 . LEU B 34  ? 0.3256 0.2378 0.3082 0.0630  -0.0142 -0.0372 34  LEU B CD2 
1669 N N   . SER B 35  ? 0.3221 0.2062 0.3173 0.0607  -0.0157 -0.0297 35  SER B N   
1670 C CA  . SER B 35  ? 0.3618 0.2311 0.3518 0.0611  -0.0153 -0.0274 35  SER B CA  
1671 C C   . SER B 35  ? 0.3535 0.2225 0.3369 0.0722  -0.0148 -0.0240 35  SER B C   
1672 O O   . SER B 35  ? 0.3677 0.2168 0.3422 0.0773  -0.0146 -0.0224 35  SER B O   
1673 C CB  . SER B 35  ? 0.3392 0.2150 0.3363 0.0529  -0.0146 -0.0259 35  SER B CB  
1674 O OG  . SER B 35  ? 0.3463 0.2193 0.3506 0.0445  -0.0151 -0.0282 35  SER B OG  
1675 N N   . LEU B 36  ? 0.3483 0.2392 0.3366 0.0759  -0.0150 -0.0225 36  LEU B N   
1676 C CA  . LEU B 36  ? 0.3363 0.2336 0.3211 0.0875  -0.0157 -0.0182 36  LEU B CA  
1677 C C   . LEU B 36  ? 0.4387 0.3308 0.4196 0.1003  -0.0147 -0.0203 36  LEU B C   
1678 O O   . LEU B 36  ? 0.3979 0.2898 0.3758 0.1128  -0.0154 -0.0163 36  LEU B O   
1679 C CB  . LEU B 36  ? 0.3266 0.2537 0.3195 0.0865  -0.0168 -0.0174 36  LEU B CB  
1680 C CG  . LEU B 36  ? 0.3374 0.2715 0.3324 0.0762  -0.0175 -0.0168 36  LEU B CG  
1681 C CD1 . LEU B 36  ? 0.3539 0.3176 0.3553 0.0754  -0.0195 -0.0172 36  LEU B CD1 
1682 C CD2 . LEU B 36  ? 0.3872 0.3060 0.3723 0.0768  -0.0177 -0.0114 36  LEU B CD2 
1683 N N   . LEU B 37  ? 0.3528 0.2424 0.3337 0.0983  -0.0131 -0.0265 37  LEU B N   
1684 C CA  . LEU B 37  ? 0.3525 0.2375 0.3283 0.1105  -0.0109 -0.0309 37  LEU B CA  
1685 C C   . LEU B 37  ? 0.4330 0.2857 0.3977 0.1102  -0.0105 -0.0357 37  LEU B C   
1686 O O   . LEU B 37  ? 0.4505 0.2956 0.4091 0.1201  -0.0081 -0.0418 37  LEU B O   
1687 C CB  . LEU B 37  ? 0.3675 0.2770 0.3488 0.1087  -0.0087 -0.0350 37  LEU B CB  
1688 C CG  . LEU B 37  ? 0.3825 0.3240 0.3752 0.1090  -0.0089 -0.0309 37  LEU B CG  
1689 C CD1 . LEU B 37  ? 0.3837 0.3477 0.3822 0.1023  -0.0065 -0.0330 37  LEU B CD1 
1690 C CD2 . LEU B 37  ? 0.3863 0.3389 0.3809 0.1259  -0.0085 -0.0288 37  LEU B CD2 
1691 N N   . GLN B 38  ? 0.4000 0.2342 0.3620 0.0991  -0.0123 -0.0340 38  GLN B N   
1692 C CA  . GLN B 38  ? 0.3898 0.1944 0.3419 0.0963  -0.0124 -0.0393 38  GLN B CA  
1693 C C   . GLN B 38  ? 0.4863 0.2660 0.4294 0.1096  -0.0111 -0.0392 38  GLN B C   
1694 O O   . GLN B 38  ? 0.4760 0.2385 0.4130 0.1080  -0.0095 -0.0458 38  GLN B O   
1695 C CB  . GLN B 38  ? 0.4230 0.2163 0.3765 0.0813  -0.0143 -0.0365 38  GLN B CB  
1696 C CG  . GLN B 38  ? 0.3869 0.1988 0.3495 0.0691  -0.0159 -0.0380 38  GLN B CG  
1697 C CD  . GLN B 38  ? 0.3935 0.2072 0.3524 0.0672  -0.0170 -0.0456 38  GLN B CD  
1698 O OE1 . GLN B 38  ? 0.4212 0.2177 0.3733 0.0616  -0.0186 -0.0508 38  GLN B OE1 
1699 N NE2 . GLN B 38  ? 0.4014 0.2374 0.3641 0.0701  -0.0163 -0.0459 38  GLN B NE2 
1700 N N   . GLU B 39  ? 0.5120 0.2962 0.4572 0.1197  -0.0114 -0.0307 39  GLU B N   
1701 C CA  . GLU B 39  ? 0.6122 0.3811 0.5544 0.1295  -0.0098 -0.0280 39  GLU B CA  
1702 C C   . GLU B 39  ? 0.6355 0.4131 0.5792 0.1419  -0.0064 -0.0363 39  GLU B C   
1703 O O   . GLU B 39  ? 0.5778 0.3400 0.5199 0.1503  -0.0046 -0.0366 39  GLU B O   
1704 C CB  . GLU B 39  ? 0.6951 0.4686 0.6385 0.1382  -0.0122 -0.0154 39  GLU B CB  
1705 C CG  . GLU B 39  ? 0.6481 0.4551 0.5995 0.1515  -0.0133 -0.0136 39  GLU B CG  
1706 C CD  . GLU B 39  ? 0.7328 0.5451 0.6844 0.1628  -0.0166 -0.0010 39  GLU B CD  
1707 O OE1 . GLU B 39  ? 0.7520 0.5460 0.7010 0.1701  -0.0164 0.0037  39  GLU B OE1 
1708 O OE2 . GLU B 39  ? 0.6630 0.5037 0.6201 0.1601  -0.0194 0.0042  39  GLU B OE2 
1709 N N   . PHE B 40  ? 0.4911 0.2918 0.4375 0.1435  -0.0052 -0.0432 40  PHE B N   
1710 C CA  . PHE B 40  ? 0.5176 0.3295 0.4641 0.1550  -0.0007 -0.0520 40  PHE B CA  
1711 C C   . PHE B 40  ? 0.5418 0.3468 0.4793 0.1468  0.0010  -0.0640 40  PHE B C   
1712 O O   . PHE B 40  ? 0.5862 0.3866 0.5204 0.1334  -0.0022 -0.0648 40  PHE B O   
1713 C CB  . PHE B 40  ? 0.4722 0.3221 0.4290 0.1656  0.0002  -0.0498 40  PHE B CB  
1714 C CG  . PHE B 40  ? 0.5870 0.4479 0.5518 0.1732  -0.0031 -0.0382 40  PHE B CG  
1715 C CD1 . PHE B 40  ? 0.6260 0.4779 0.5922 0.1851  -0.0028 -0.0339 40  PHE B CD1 
1716 C CD2 . PHE B 40  ? 0.4980 0.3792 0.4695 0.1650  -0.0068 -0.0310 40  PHE B CD2 
1717 C CE1 . PHE B 40  ? 0.6642 0.5267 0.6359 0.1925  -0.0070 -0.0222 40  PHE B CE1 
1718 C CE2 . PHE B 40  ? 0.6143 0.5073 0.5909 0.1713  -0.0106 -0.0209 40  PHE B CE2 
1719 C CZ  . PHE B 40  ? 0.6054 0.4884 0.5808 0.1875  -0.0112 -0.0160 40  PHE B CZ  
1720 N N   . ASP B 41  ? 0.5739 0.3793 0.5070 0.1557  0.0059  -0.0739 41  ASP B N   
1721 C CA  . ASP B 41  ? 0.6255 0.4234 0.5464 0.1487  0.0073  -0.0866 41  ASP B CA  
1722 C C   . ASP B 41  ? 0.5693 0.3977 0.4883 0.1508  0.0096  -0.0919 41  ASP B C   
1723 O O   . ASP B 41  ? 0.6465 0.4744 0.5544 0.1430  0.0104  -0.1009 41  ASP B O   
1724 C CB  . ASP B 41  ? 0.7522 0.5292 0.6665 0.1546  0.0117  -0.0966 41  ASP B CB  
1725 C CG  . ASP B 41  ? 0.8300 0.6266 0.7492 0.1728  0.0184  -0.1011 41  ASP B CG  
1726 O OD1 . ASP B 41  ? 0.8092 0.6391 0.7368 0.1801  0.0198  -0.0969 41  ASP B OD1 
1727 O OD2 . ASP B 41  ? 0.9647 0.7443 0.8810 0.1799  0.0225  -0.1091 41  ASP B OD2 
1728 N N   . PHE B 42  ? 0.5914 0.4535 0.5243 0.1531  0.0105  -0.0829 42  PHE B N   
1729 C CA  . PHE B 42  ? 0.4947 0.3926 0.4303 0.1485  0.0140  -0.0839 42  PHE B CA  
1730 C C   . PHE B 42  ? 0.4724 0.3836 0.4135 0.1293  0.0094  -0.0747 42  PHE B C   
1731 O O   . PHE B 42  ? 0.4314 0.3727 0.3777 0.1243  0.0117  -0.0712 42  PHE B O   
1732 C CB  . PHE B 42  ? 0.5103 0.4401 0.4582 0.1631  0.0191  -0.0817 42  PHE B CB  
1733 C CG  . PHE B 42  ? 0.4970 0.4352 0.4596 0.1658  0.0150  -0.0701 42  PHE B CG  
1734 C CD1 . PHE B 42  ? 0.4314 0.3872 0.4035 0.1506  0.0110  -0.0605 42  PHE B CD1 
1735 C CD2 . PHE B 42  ? 0.5932 0.5226 0.5597 0.1840  0.0150  -0.0690 42  PHE B CD2 
1736 C CE1 . PHE B 42  ? 0.4779 0.4430 0.4613 0.1522  0.0072  -0.0516 42  PHE B CE1 
1737 C CE2 . PHE B 42  ? 0.5262 0.4665 0.5042 0.1863  0.0105  -0.0578 42  PHE B CE2 
1738 C CZ  . PHE B 42  ? 0.4604 0.4196 0.4462 0.1697  0.0066  -0.0499 42  PHE B CZ  
1739 N N   . VAL B 43  ? 0.4690 0.3584 0.4094 0.1184  0.0033  -0.0707 43  VAL B N   
1740 C CA  . VAL B 43  ? 0.4098 0.3071 0.3550 0.1018  -0.0011 -0.0638 43  VAL B CA  
1741 C C   . VAL B 43  ? 0.4015 0.2749 0.3369 0.0922  -0.0055 -0.0681 43  VAL B C   
1742 O O   . VAL B 43  ? 0.4479 0.2951 0.3748 0.0962  -0.0057 -0.0749 43  VAL B O   
1743 C CB  . VAL B 43  ? 0.4198 0.3217 0.3789 0.0976  -0.0041 -0.0538 43  VAL B CB  
1744 C CG1 . VAL B 43  ? 0.4156 0.3440 0.3851 0.1052  -0.0011 -0.0499 43  VAL B CG1 
1745 C CG2 . VAL B 43  ? 0.4030 0.2774 0.3598 0.0998  -0.0066 -0.0534 43  VAL B CG2 
1746 N N   . PRO B 44  ? 0.4302 0.3117 0.3675 0.0792  -0.0096 -0.0639 44  PRO B N   
1747 C CA  . PRO B 44  ? 0.3999 0.2641 0.3313 0.0693  -0.0151 -0.0669 44  PRO B CA  
1748 C C   . PRO B 44  ? 0.4593 0.3045 0.3980 0.0661  -0.0178 -0.0638 44  PRO B C   
1749 O O   . PRO B 44  ? 0.4042 0.2548 0.3545 0.0672  -0.0171 -0.0564 44  PRO B O   
1750 C CB  . PRO B 44  ? 0.4327 0.3150 0.3688 0.0586  -0.0192 -0.0597 44  PRO B CB  
1751 C CG  . PRO B 44  ? 0.4626 0.3686 0.4031 0.0618  -0.0149 -0.0542 44  PRO B CG  
1752 C CD  . PRO B 44  ? 0.4433 0.3504 0.3890 0.0732  -0.0096 -0.0556 44  PRO B CD  
1753 N N   . ARG B 45  ? 0.4225 0.2469 0.3537 0.0603  -0.0208 -0.0699 45  ARG B N   
1754 C CA  . ARG B 45  ? 0.4742 0.2838 0.4123 0.0530  -0.0235 -0.0663 45  ARG B CA  
1755 C C   . ARG B 45  ? 0.4355 0.2629 0.3879 0.0440  -0.0271 -0.0582 45  ARG B C   
1756 O O   . ARG B 45  ? 0.4151 0.2566 0.3682 0.0389  -0.0305 -0.0574 45  ARG B O   
1757 C CB  . ARG B 45  ? 0.4134 0.2008 0.3413 0.0453  -0.0265 -0.0750 45  ARG B CB  
1758 C CG  . ARG B 45  ? 0.4944 0.2571 0.4066 0.0535  -0.0231 -0.0857 45  ARG B CG  
1759 C CD  . ARG B 45  ? 0.5039 0.2510 0.4178 0.0655  -0.0185 -0.0813 45  ARG B CD  
1760 N NE  . ARG B 45  ? 0.5090 0.2761 0.4262 0.0796  -0.0143 -0.0786 45  ARG B NE  
1761 C CZ  . ARG B 45  ? 0.5515 0.3189 0.4745 0.0906  -0.0117 -0.0716 45  ARG B CZ  
1762 N NH1 . ARG B 45  ? 0.5684 0.3181 0.4937 0.0889  -0.0119 -0.0651 45  ARG B NH1 
1763 N NH2 . ARG B 45  ? 0.5679 0.3594 0.4958 0.1015  -0.0085 -0.0696 45  ARG B NH2 
1764 N N   . LEU B 46  ? 0.3804 0.2068 0.3436 0.0424  -0.0261 -0.0520 46  LEU B N   
1765 C CA  . LEU B 46  ? 0.3774 0.2180 0.3556 0.0353  -0.0284 -0.0460 46  LEU B CA  
1766 C C   . LEU B 46  ? 0.4588 0.2911 0.4417 0.0253  -0.0312 -0.0468 46  LEU B C   
1767 O O   . LEU B 46  ? 0.3643 0.1800 0.3434 0.0237  -0.0291 -0.0477 46  LEU B O   
1768 C CB  . LEU B 46  ? 0.3221 0.1703 0.3086 0.0397  -0.0248 -0.0405 46  LEU B CB  
1769 C CG  . LEU B 46  ? 0.3711 0.2309 0.3728 0.0343  -0.0253 -0.0362 46  LEU B CG  
1770 C CD1 . LEU B 46  ? 0.3506 0.2231 0.3584 0.0318  -0.0288 -0.0343 46  LEU B CD1 
1771 C CD2 . LEU B 46  ? 0.4073 0.2742 0.4128 0.0388  -0.0215 -0.0334 46  LEU B CD2 
1772 N N   . TYR B 47  ? 0.3520 0.1964 0.3433 0.0183  -0.0361 -0.0459 47  TYR B N   
1773 C CA  . TYR B 47  ? 0.3525 0.1945 0.3502 0.0079  -0.0393 -0.0474 47  TYR B CA  
1774 C C   . TYR B 47  ? 0.3558 0.2115 0.3727 0.0048  -0.0385 -0.0421 47  TYR B C   
1775 O O   . TYR B 47  ? 0.3528 0.2051 0.3754 -0.0018 -0.0367 -0.0423 47  TYR B O   
1776 C CB  . TYR B 47  ? 0.3515 0.1999 0.3455 0.0017  -0.0466 -0.0511 47  TYR B CB  
1777 C CG  . TYR B 47  ? 0.4480 0.2829 0.4216 0.0037  -0.0469 -0.0592 47  TYR B CG  
1778 C CD1 . TYR B 47  ? 0.4986 0.3088 0.4608 0.0047  -0.0429 -0.0651 47  TYR B CD1 
1779 C CD2 . TYR B 47  ? 0.4140 0.2601 0.3788 0.0044  -0.0511 -0.0611 47  TYR B CD2 
1780 C CE1 . TYR B 47  ? 0.5585 0.3544 0.5021 0.0078  -0.0425 -0.0746 47  TYR B CE1 
1781 C CE2 . TYR B 47  ? 0.4295 0.2646 0.3742 0.0064  -0.0503 -0.0707 47  TYR B CE2 
1782 C CZ  . TYR B 47  ? 0.5068 0.3164 0.4418 0.0086  -0.0458 -0.0784 47  TYR B CZ  
1783 O OH  . TYR B 47  ? 0.5190 0.3167 0.4346 0.0120  -0.0444 -0.0897 47  TYR B OH  
1784 N N   . SER B 48  ? 0.3503 0.2207 0.3774 0.0095  -0.0389 -0.0377 48  SER B N   
1785 C CA  . SER B 48  ? 0.3838 0.2664 0.4299 0.0079  -0.0376 -0.0348 48  SER B CA  
1786 C C   . SER B 48  ? 0.3768 0.2670 0.4298 0.0146  -0.0362 -0.0311 48  SER B C   
1787 O O   . SER B 48  ? 0.3677 0.2578 0.4130 0.0184  -0.0378 -0.0293 48  SER B O   
1788 C CB  . SER B 48  ? 0.4246 0.3199 0.4835 0.0016  -0.0439 -0.0344 48  SER B CB  
1789 O OG  . SER B 48  ? 0.4222 0.3265 0.4819 0.0046  -0.0503 -0.0309 48  SER B OG  
1790 N N   . ILE B 49  ? 0.3396 0.2360 0.4065 0.0153  -0.0323 -0.0308 49  ILE B N   
1791 C CA  . ILE B 49  ? 0.3616 0.2633 0.4381 0.0201  -0.0313 -0.0286 49  ILE B CA  
1792 C C   . ILE B 49  ? 0.4434 0.3554 0.5407 0.0202  -0.0318 -0.0285 49  ILE B C   
1793 O O   . ILE B 49  ? 0.4355 0.3534 0.5403 0.0166  -0.0299 -0.0311 49  ILE B O   
1794 C CB  . ILE B 49  ? 0.3160 0.2140 0.3873 0.0225  -0.0251 -0.0307 49  ILE B CB  
1795 C CG1 . ILE B 49  ? 0.4150 0.3156 0.4919 0.0202  -0.0195 -0.0343 49  ILE B CG1 
1796 C CG2 . ILE B 49  ? 0.3732 0.2639 0.4262 0.0244  -0.0246 -0.0306 49  ILE B CG2 
1797 C CD1 . ILE B 49  ? 0.4352 0.3365 0.5088 0.0221  -0.0142 -0.0369 49  ILE B CD1 
1798 N N   . ASN B 50  ? 0.3193 0.2337 0.4266 0.0246  -0.0344 -0.0249 50  ASN B N   
1799 C CA  . ASN B 50  ? 0.3262 0.2495 0.4553 0.0280  -0.0349 -0.0246 50  ASN B CA  
1800 C C   . ASN B 50  ? 0.3450 0.2610 0.4797 0.0328  -0.0317 -0.0248 50  ASN B C   
1801 O O   . ASN B 50  ? 0.3065 0.2174 0.4415 0.0352  -0.0362 -0.0183 50  ASN B O   
1802 C CB  . ASN B 50  ? 0.3344 0.2667 0.4715 0.0288  -0.0442 -0.0182 50  ASN B CB  
1803 C CG  . ASN B 50  ? 0.3329 0.2771 0.4955 0.0343  -0.0451 -0.0175 50  ASN B CG  
1804 O OD1 . ASN B 50  ? 0.3622 0.3032 0.5358 0.0394  -0.0390 -0.0213 50  ASN B OD1 
1805 N ND2 . ASN B 50  ? 0.3463 0.3055 0.5191 0.0338  -0.0527 -0.0135 50  ASN B ND2 
1806 N N   . PRO B 51  ? 0.3415 0.2564 0.4794 0.0332  -0.0239 -0.0324 51  PRO B N   
1807 C CA  . PRO B 51  ? 0.3250 0.2315 0.4678 0.0361  -0.0207 -0.0352 51  PRO B CA  
1808 C C   . PRO B 51  ? 0.3335 0.2383 0.4970 0.0430  -0.0229 -0.0331 51  PRO B C   
1809 O O   . PRO B 51  ? 0.3297 0.2220 0.4959 0.0448  -0.0227 -0.0322 51  PRO B O   
1810 C CB  . PRO B 51  ? 0.3659 0.2754 0.5065 0.0342  -0.0120 -0.0454 51  PRO B CB  
1811 C CG  . PRO B 51  ? 0.4194 0.3349 0.5478 0.0296  -0.0112 -0.0447 51  PRO B CG  
1812 C CD  . PRO B 51  ? 0.3237 0.2445 0.4583 0.0295  -0.0177 -0.0387 51  PRO B CD  
1813 N N   . GLU B 52  ? 0.3284 0.2453 0.5075 0.0469  -0.0250 -0.0321 52  GLU B N   
1814 C CA  . GLU B 52  ? 0.3388 0.2545 0.5395 0.0561  -0.0277 -0.0291 52  GLU B CA  
1815 C C   . GLU B 52  ? 0.4209 0.3285 0.6185 0.0577  -0.0373 -0.0157 52  GLU B C   
1816 O O   . GLU B 52  ? 0.3586 0.2524 0.5649 0.0633  -0.0386 -0.0115 52  GLU B O   
1817 C CB  . GLU B 52  ? 0.3318 0.2681 0.5526 0.0605  -0.0277 -0.0312 52  GLU B CB  
1818 N N   . LYS B 53  ? 0.3425 0.2562 0.5253 0.0521  -0.0435 -0.0089 53  LYS B N   
1819 C CA  . LYS B 53  ? 0.3496 0.2585 0.5251 0.0521  -0.0521 0.0040  53  LYS B CA  
1820 C C   . LYS B 53  ? 0.3278 0.2250 0.4822 0.0455  -0.0498 0.0056  53  LYS B C   
1821 O O   . LYS B 53  ? 0.3560 0.2490 0.5027 0.0443  -0.0552 0.0165  53  LYS B O   
1822 C CB  . LYS B 53  ? 0.3911 0.3164 0.5617 0.0494  -0.0606 0.0093  53  LYS B CB  
1823 C CG  . LYS B 53  ? 0.4756 0.4194 0.6687 0.0541  -0.0633 0.0075  53  LYS B CG  
1824 C CD  . LYS B 53  ? 0.5242 0.4843 0.7190 0.0539  -0.0755 0.0170  53  LYS B CD  
1825 C CE  . LYS B 53  ? 0.6449 0.6046 0.8127 0.0441  -0.0794 0.0183  53  LYS B CE  
1826 N NZ  . LYS B 53  ? 0.7894 0.7654 0.9563 0.0433  -0.0923 0.0275  53  LYS B NZ  
1827 N N   . LEU B 54  ? 0.2767 0.1706 0.4223 0.0413  -0.0420 -0.0043 54  LEU B N   
1828 C CA  . LEU B 54  ? 0.2697 0.1590 0.3964 0.0353  -0.0397 -0.0041 54  LEU B CA  
1829 C C   . LEU B 54  ? 0.3045 0.2008 0.4151 0.0323  -0.0449 0.0020  54  LEU B C   
1830 O O   . LEU B 54  ? 0.3114 0.2058 0.4117 0.0297  -0.0467 0.0092  54  LEU B O   
1831 C CB  . LEU B 54  ? 0.2974 0.1738 0.4262 0.0338  -0.0386 0.0002  54  LEU B CB  
1832 C CG  . LEU B 54  ? 0.3379 0.2044 0.4803 0.0358  -0.0328 -0.0088 54  LEU B CG  
1833 C CD1 . LEU B 54  ? 0.3683 0.2184 0.5135 0.0331  -0.0330 -0.0035 54  LEU B CD1 
1834 C CD2 . LEU B 54  ? 0.3541 0.2256 0.4882 0.0318  -0.0258 -0.0209 54  LEU B CD2 
1835 N N   . GLU B 55  ? 0.3074 0.2123 0.4160 0.0320  -0.0470 -0.0013 55  GLU B N   
1836 C CA  . GLU B 55  ? 0.3054 0.2160 0.3982 0.0289  -0.0518 0.0013  55  GLU B CA  
1837 C C   . GLU B 55  ? 0.3368 0.2459 0.4164 0.0261  -0.0471 -0.0076 55  GLU B C   
1838 O O   . GLU B 55  ? 0.2960 0.2046 0.3817 0.0258  -0.0432 -0.0140 55  GLU B O   
1839 C CB  . GLU B 55  ? 0.4246 0.3455 0.5256 0.0294  -0.0600 0.0049  55  GLU B CB  
1840 C CG  . GLU B 55  ? 0.5220 0.4483 0.6104 0.0276  -0.0678 0.0133  55  GLU B CG  
1841 C CD  . GLU B 55  ? 0.6027 0.5424 0.7017 0.0286  -0.0776 0.0187  55  GLU B CD  
1842 O OE1 . GLU B 55  ? 0.4656 0.4133 0.5752 0.0273  -0.0782 0.0123  55  GLU B OE1 
1843 O OE2 . GLU B 55  ? 0.4991 0.4424 0.5975 0.0306  -0.0847 0.0306  55  GLU B OE2 
1844 N N   . ILE B 56  ? 0.3079 0.2162 0.3693 0.0246  -0.0470 -0.0075 56  ILE B N   
1845 C CA  . ILE B 56  ? 0.3111 0.2154 0.3588 0.0239  -0.0435 -0.0150 56  ILE B CA  
1846 C C   . ILE B 56  ? 0.3798 0.2859 0.4139 0.0215  -0.0486 -0.0161 56  ILE B C   
1847 O O   . ILE B 56  ? 0.3533 0.2651 0.3799 0.0210  -0.0520 -0.0110 56  ILE B O   
1848 C CB  . ILE B 56  ? 0.2839 0.1866 0.3227 0.0262  -0.0378 -0.0161 56  ILE B CB  
1849 C CG1 . ILE B 56  ? 0.3311 0.2332 0.3819 0.0268  -0.0336 -0.0162 56  ILE B CG1 
1850 C CG2 . ILE B 56  ? 0.3361 0.2331 0.3628 0.0282  -0.0343 -0.0229 56  ILE B CG2 
1851 C CD1 . ILE B 56  ? 0.4008 0.3056 0.4442 0.0281  -0.0289 -0.0179 56  ILE B CD1 
1852 N N   . GLU B 57  ? 0.3157 0.2170 0.3464 0.0186  -0.0491 -0.0226 57  GLU B N   
1853 C CA  . GLU B 57  ? 0.3472 0.2475 0.3633 0.0150  -0.0536 -0.0268 57  GLU B CA  
1854 C C   . GLU B 57  ? 0.3885 0.2757 0.3886 0.0174  -0.0480 -0.0345 57  GLU B C   
1855 O O   . GLU B 57  ? 0.3686 0.2456 0.3712 0.0184  -0.0435 -0.0375 57  GLU B O   
1856 C CB  . GLU B 57  ? 0.3389 0.2428 0.3629 0.0082  -0.0593 -0.0291 57  GLU B CB  
1857 C CG  . GLU B 57  ? 0.3942 0.3136 0.4369 0.0086  -0.0653 -0.0208 57  GLU B CG  
1858 C CD  . GLU B 57  ? 0.6068 0.5379 0.6570 0.0018  -0.0734 -0.0220 57  GLU B CD  
1859 O OE1 . GLU B 57  ? 0.5177 0.4441 0.5549 -0.0052 -0.0756 -0.0296 57  GLU B OE1 
1860 O OE2 . GLU B 57  ? 0.5262 0.4713 0.5963 0.0037  -0.0778 -0.0157 57  GLU B OE2 
1861 N N   . MET B 58  ? 0.4010 0.2891 0.3845 0.0193  -0.0481 -0.0372 58  MET B N   
1862 C CA  . MET B 58  ? 0.3960 0.2725 0.3654 0.0246  -0.0423 -0.0449 58  MET B CA  
1863 C C   . MET B 58  ? 0.4201 0.2947 0.3709 0.0227  -0.0448 -0.0528 58  MET B C   
1864 O O   . MET B 58  ? 0.3867 0.2714 0.3346 0.0165  -0.0514 -0.0513 58  MET B O   
1865 C CB  . MET B 58  ? 0.4056 0.2890 0.3752 0.0322  -0.0362 -0.0414 58  MET B CB  
1866 C CG  . MET B 58  ? 0.4915 0.3914 0.4578 0.0315  -0.0372 -0.0357 58  MET B CG  
1867 S SD  . MET B 58  ? 0.6108 0.5215 0.5839 0.0368  -0.0302 -0.0305 58  MET B SD  
1868 C CE  . MET B 58  ? 0.4639 0.3747 0.4570 0.0323  -0.0328 -0.0225 58  MET B CE  
1869 N N   . GLU B 59  ? 0.4277 0.2897 0.3656 0.0289  -0.0394 -0.0615 59  GLU B N   
1870 C CA  . GLU B 59  ? 0.4079 0.2660 0.3259 0.0287  -0.0398 -0.0721 59  GLU B CA  
1871 C C   . GLU B 59  ? 0.4236 0.3037 0.3336 0.0298  -0.0396 -0.0685 59  GLU B C   
1872 O O   . GLU B 59  ? 0.4126 0.3040 0.3272 0.0359  -0.0343 -0.0624 59  GLU B O   
1873 C CB  . GLU B 59  ? 0.4010 0.2406 0.3100 0.0386  -0.0326 -0.0814 59  GLU B CB  
1874 C CG  . GLU B 59  ? 0.4379 0.2654 0.3267 0.0396  -0.0316 -0.0960 59  GLU B CG  
1875 C CD  . GLU B 59  ? 0.5425 0.3541 0.4256 0.0539  -0.0233 -0.1033 59  GLU B CD  
1876 O OE1 . GLU B 59  ? 0.5146 0.3269 0.4100 0.0618  -0.0197 -0.0953 59  GLU B OE1 
1877 O OE2 . GLU B 59  ? 0.5494 0.3498 0.4159 0.0579  -0.0206 -0.1170 59  GLU B OE2 
1878 N N   . PHE B 60  ? 0.4734 0.3609 0.3705 0.0227  -0.0453 -0.0720 60  PHE B N   
1879 C CA  . PHE B 60  ? 0.4705 0.3768 0.3530 0.0238  -0.0436 -0.0709 60  PHE B CA  
1880 C C   . PHE B 60  ? 0.5294 0.4296 0.3959 0.0328  -0.0346 -0.0845 60  PHE B C   
1881 O O   . PHE B 60  ? 0.4844 0.3650 0.3408 0.0336  -0.0341 -0.0987 60  PHE B O   
1882 C CB  . PHE B 60  ? 0.5323 0.4491 0.4021 0.0137  -0.0530 -0.0716 60  PHE B CB  
1883 C CG  . PHE B 60  ? 0.5385 0.4753 0.3887 0.0137  -0.0509 -0.0708 60  PHE B CG  
1884 C CD1 . PHE B 60  ? 0.6225 0.5773 0.4779 0.0148  -0.0487 -0.0555 60  PHE B CD1 
1885 C CD2 . PHE B 60  ? 0.6678 0.6040 0.4933 0.0122  -0.0500 -0.0863 60  PHE B CD2 
1886 C CE1 . PHE B 60  ? 0.6060 0.5805 0.4424 0.0135  -0.0458 -0.0534 60  PHE B CE1 
1887 C CE2 . PHE B 60  ? 0.7481 0.7051 0.5537 0.0119  -0.0468 -0.0861 60  PHE B CE2 
1888 C CZ  . PHE B 60  ? 0.6618 0.6389 0.4730 0.0124  -0.0446 -0.0686 60  PHE B CZ  
1889 N N   . ILE B 61  ? 0.5058 0.4229 0.3705 0.0394  -0.0272 -0.0807 61  ILE B N   
1890 C CA  . ILE B 61  ? 0.5231 0.4386 0.3768 0.0507  -0.0174 -0.0932 61  ILE B CA  
1891 C C   . ILE B 61  ? 0.6175 0.5504 0.4485 0.0482  -0.0153 -0.0998 61  ILE B C   
1892 O O   . ILE B 61  ? 0.4845 0.4424 0.3136 0.0442  -0.0143 -0.0890 61  ILE B O   
1893 C CB  . ILE B 61  ? 0.5766 0.5035 0.4449 0.0603  -0.0095 -0.0862 61  ILE B CB  
1894 C CG1 . ILE B 61  ? 0.5661 0.4780 0.4546 0.0618  -0.0120 -0.0795 61  ILE B CG1 
1895 C CG2 . ILE B 61  ? 0.5627 0.4908 0.4212 0.0741  0.0006  -0.1000 61  ILE B CG2 
1896 C CD1 . ILE B 61  ? 0.5138 0.3950 0.4004 0.0659  -0.0129 -0.0895 61  ILE B CD1 
1897 N N   . GLU B 62  ? 0.6108 0.5298 0.4235 0.0499  -0.0142 -0.1178 62  GLU B N   
1898 C CA  . GLU B 62  ? 0.7073 0.6430 0.4953 0.0479  -0.0112 -0.1273 62  GLU B CA  
1899 C C   . GLU B 62  ? 0.6677 0.6177 0.4527 0.0616  0.0024  -0.1333 62  GLU B C   
1900 O O   . GLU B 62  ? 0.7461 0.6842 0.5438 0.0744  0.0087  -0.1370 62  GLU B O   
1901 C CB  . GLU B 62  ? 0.6800 0.5944 0.4488 0.0436  -0.0152 -0.1469 62  GLU B CB  
1902 C CG  . GLU B 62  ? 0.9771 0.9025 0.7341 0.0275  -0.0272 -0.1433 62  GLU B CG  
1903 C CD  . GLU B 62  ? 1.2121 1.1172 0.9505 0.0208  -0.0320 -0.1642 62  GLU B CD  
1904 O OE1 . GLU B 62  ? 1.3045 1.2139 1.0177 0.0223  -0.0270 -0.1812 62  GLU B OE1 
1905 O OE2 . GLU B 62  ? 1.2404 1.1258 0.9893 0.0132  -0.0403 -0.1644 62  GLU B OE2 
1906 N N   . GLY B 63  ? 0.6681 0.6475 0.4381 0.0587  0.0069  -0.1317 63  GLY B N   
1907 C CA  . GLY B 63  ? 0.7104 0.7114 0.4789 0.0703  0.0207  -0.1364 63  GLY B CA  
1908 C C   . GLY B 63  ? 0.6440 0.6814 0.4131 0.0629  0.0236  -0.1188 63  GLY B C   
1909 O O   . GLY B 63  ? 0.6464 0.6893 0.4152 0.0494  0.0143  -0.1028 63  GLY B O   
1910 N N   . ARG B 64  ? 0.6364 0.6991 0.4075 0.0715  0.0365  -0.1209 64  ARG B N   
1911 C CA  . ARG B 64  ? 0.6297 0.7275 0.4011 0.0625  0.0405  -0.1037 64  ARG B CA  
1912 C C   . ARG B 64  ? 0.6123 0.7198 0.4129 0.0656  0.0439  -0.0903 64  ARG B C   
1913 O O   . ARG B 64  ? 0.6026 0.7037 0.4181 0.0798  0.0489  -0.0990 64  ARG B O   
1914 C CB  . ARG B 64  ? 0.6522 0.7807 0.4021 0.0659  0.0535  -0.1148 64  ARG B CB  
1915 C CG  . ARG B 64  ? 0.7156 0.8331 0.4350 0.0657  0.0520  -0.1348 64  ARG B CG  
1916 C CD  . ARG B 64  ? 0.7254 0.8747 0.4204 0.0687  0.0657  -0.1477 64  ARG B CD  
1917 N NE  . ARG B 64  ? 0.8551 1.0401 0.5397 0.0543  0.0675  -0.1285 64  ARG B NE  
1918 C CZ  . ARG B 64  ? 0.8539 1.0759 0.5220 0.0545  0.0812  -0.1328 64  ARG B CZ  
1919 N NH1 . ARG B 64  ? 0.6952 0.9254 0.3561 0.0701  0.0950  -0.1573 64  ARG B NH1 
1920 N NH2 . ARG B 64  ? 0.7217 0.9728 0.3799 0.0390  0.0814  -0.1118 64  ARG B NH2 
1921 N N   . PRO B 65  ? 0.6610 0.7823 0.4702 0.0526  0.0405  -0.0691 65  PRO B N   
1922 C CA  . PRO B 65  ? 0.6188 0.7516 0.4544 0.0533  0.0440  -0.0579 65  PRO B CA  
1923 C C   . PRO B 65  ? 0.6562 0.8238 0.4938 0.0613  0.0588  -0.0644 65  PRO B C   
1924 O O   . PRO B 65  ? 0.6283 0.8174 0.4457 0.0610  0.0669  -0.0710 65  PRO B O   
1925 C CB  . PRO B 65  ? 0.5471 0.6850 0.3862 0.0358  0.0376  -0.0352 65  PRO B CB  
1926 C CG  . PRO B 65  ? 0.5886 0.7331 0.3994 0.0273  0.0351  -0.0332 65  PRO B CG  
1927 C CD  . PRO B 65  ? 0.6227 0.7495 0.4174 0.0366  0.0330  -0.0542 65  PRO B CD  
1928 N N   . ILE B 66  ? 0.4947 0.6702 0.3570 0.0687  0.0624  -0.0631 66  ILE B N   
1929 C CA  . ILE B 66  ? 0.5329 0.7434 0.4021 0.0793  0.0760  -0.0707 66  ILE B CA  
1930 C C   . ILE B 66  ? 0.6137 0.8636 0.4748 0.0661  0.0848  -0.0607 66  ILE B C   
1931 O O   . ILE B 66  ? 0.5426 0.8234 0.3970 0.0738  0.0976  -0.0709 66  ILE B O   
1932 C CB  . ILE B 66  ? 0.5319 0.7477 0.4310 0.0873  0.0760  -0.0679 66  ILE B CB  
1933 C CG1 . ILE B 66  ? 0.5005 0.7518 0.4087 0.1034  0.0893  -0.0789 66  ILE B CG1 
1934 C CG2 . ILE B 66  ? 0.4609 0.6849 0.3765 0.0694  0.0710  -0.0479 66  ILE B CG2 
1935 C CD1 . ILE B 66  ? 0.4655 0.7201 0.4013 0.1159  0.0876  -0.0789 66  ILE B CD1 
1936 N N   . LYS B 67  ? 0.5547 0.8041 0.4159 0.0465  0.0787  -0.0406 67  LYS B N   
1937 C CA  . LYS B 67  ? 0.6004 0.8857 0.4535 0.0322  0.0871  -0.0283 67  LYS B CA  
1938 C C   . LYS B 67  ? 0.6367 0.9351 0.4579 0.0327  0.0934  -0.0369 67  LYS B C   
1939 O O   . LYS B 67  ? 0.6117 0.9490 0.4253 0.0273  0.1056  -0.0341 67  LYS B O   
1940 C CB  . LYS B 67  ? 0.6048 0.8783 0.4616 0.0117  0.0779  -0.0044 67  LYS B CB  
1941 C CG  . LYS B 67  ? 0.6716 0.9109 0.5108 0.0072  0.0648  -0.0001 67  LYS B CG  
1942 C CD  . LYS B 67  ? 0.7731 1.0099 0.6090 -0.0122 0.0589  0.0245  67  LYS B CD  
1943 C CE  . LYS B 67  ? 0.7518 0.9531 0.5804 -0.0142 0.0436  0.0299  67  LYS B CE  
1944 N NZ  . LYS B 67  ? 0.8613 1.0688 0.6582 -0.0145 0.0425  0.0254  67  LYS B NZ  
1945 N N   . ASP B 68  ? 0.5868 0.8562 0.3891 0.0387  0.0860  -0.0487 68  ASP B N   
1946 C CA  . ASP B 68  ? 0.7212 1.0019 0.4908 0.0385  0.0909  -0.0594 68  ASP B CA  
1947 C C   . ASP B 68  ? 0.6788 0.9751 0.4433 0.0575  0.1046  -0.0850 68  ASP B C   
1948 O O   . ASP B 68  ? 0.6768 0.9898 0.4140 0.0577  0.1121  -0.0960 68  ASP B O   
1949 C CB  . ASP B 68  ? 0.7648 1.0097 0.5159 0.0357  0.0767  -0.0631 68  ASP B CB  
1950 C CG  . ASP B 68  ? 0.8114 1.0457 0.5611 0.0177  0.0636  -0.0382 68  ASP B CG  
1951 O OD1 . ASP B 68  ? 0.7586 1.0111 0.5173 0.0059  0.0662  -0.0177 68  ASP B OD1 
1952 O OD2 . ASP B 68  ? 0.8183 1.0255 0.5591 0.0155  0.0506  -0.0393 68  ASP B OD2 
1953 N N   . VAL B 69  ? 0.6085 0.8997 0.3975 0.0744  0.1081  -0.0952 69  VAL B N   
1954 C CA  . VAL B 69  ? 0.6524 0.9508 0.4364 0.0956  0.1197  -0.1208 69  VAL B CA  
1955 C C   . VAL B 69  ? 0.6955 1.0240 0.5085 0.1094  0.1307  -0.1227 69  VAL B C   
1956 O O   . VAL B 69  ? 0.6391 0.9679 0.4572 0.1276  0.1382  -0.1401 69  VAL B O   
1957 C CB  . VAL B 69  ? 0.7004 0.9501 0.4794 0.1083  0.1110  -0.1379 69  VAL B CB  
1958 C CG1 . VAL B 69  ? 0.7089 0.9366 0.4567 0.0968  0.1024  -0.1420 69  VAL B CG1 
1959 C CG2 . VAL B 69  ? 0.6649 0.8852 0.4714 0.1099  0.0992  -0.1270 69  VAL B CG2 
1960 N N   . ILE B 70  ? 0.6527 0.9993 0.4893 0.0981  0.1286  -0.1024 70  ILE B N   
1961 C CA  . ILE B 70  ? 0.6054 0.9770 0.4737 0.1104  0.1349  -0.1030 70  ILE B CA  
1962 C C   . ILE B 70  ? 0.6529 1.0615 0.5243 0.1202  0.1497  -0.1138 70  ILE B C   
1963 O O   . ILE B 70  ? 0.6240 1.0353 0.5165 0.1386  0.1524  -0.1231 70  ILE B O   
1964 C CB  . ILE B 70  ? 0.5273 0.9125 0.4178 0.0916  0.1295  -0.0794 70  ILE B CB  
1965 C CG1 . ILE B 70  ? 0.5176 0.9309 0.4416 0.1031  0.1340  -0.0803 70  ILE B CG1 
1966 C CG2 . ILE B 70  ? 0.5267 0.9426 0.4054 0.0685  0.1353  -0.0636 70  ILE B CG2 
1967 C CD1 . ILE B 70  ? 0.5483 0.9333 0.4831 0.1276  0.1289  -0.0942 70  ILE B CD1 
1968 N N   . ASN B 71  ? 0.6277 1.0582 0.4797 0.1067  0.1567  -0.1106 71  ASN B N   
1969 C CA  . ASN B 71  ? 0.6779 1.1388 0.5342 0.1136  0.1692  -0.1193 71  ASN B CA  
1970 C C   . ASN B 71  ? 0.7115 1.1473 0.5524 0.1318  0.1726  -0.1430 71  ASN B C   
1971 O O   . ASN B 71  ? 0.7520 1.2094 0.5988 0.1419  0.1834  -0.1531 71  ASN B O   
1972 C CB  . ASN B 71  ? 0.6961 1.1903 0.5378 0.0914  0.1758  -0.1055 71  ASN B CB  
1973 C CG  . ASN B 71  ? 0.5915 1.1147 0.4547 0.0739  0.1754  -0.0830 71  ASN B CG  
1974 O OD1 . ASN B 71  ? 0.6644 1.1804 0.5183 0.0545  0.1690  -0.0652 71  ASN B OD1 
1975 N ND2 . ASN B 71  ? 0.6419 1.1982 0.5341 0.0797  0.1821  -0.0831 71  ASN B ND2 
1976 N N   . GLU B 72  ? 0.7676 1.1585 0.5889 0.1352  0.1638  -0.1524 72  GLU B N   
1977 C CA  . GLU B 72  ? 0.7452 1.1062 0.5526 0.1505  0.1662  -0.1751 72  GLU B CA  
1978 C C   . GLU B 72  ? 0.7797 1.1078 0.6076 0.1713  0.1615  -0.1844 72  GLU B C   
1979 O O   . GLU B 72  ? 0.8293 1.1322 0.6510 0.1855  0.1649  -0.2025 72  GLU B O   
1980 C CB  . GLU B 72  ? 0.7944 1.1242 0.5664 0.1393  0.1586  -0.1806 72  GLU B CB  
1981 C CG  . GLU B 72  ? 0.8435 1.1955 0.5933 0.1146  0.1563  -0.1639 72  GLU B CG  
1982 C CD  . GLU B 72  ? 0.9334 1.3341 0.6837 0.1055  0.1685  -0.1548 72  GLU B CD  
1983 O OE1 . GLU B 72  ? 0.9787 1.3970 0.7364 0.1178  0.1805  -0.1673 72  GLU B OE1 
1984 O OE2 . GLU B 72  ? 0.8998 1.3206 0.6422 0.0852  0.1662  -0.1343 72  GLU B OE2 
1985 N N   . LEU B 73  ? 0.7734 1.1003 0.6246 0.1726  0.1539  -0.1716 73  LEU B N   
1986 C CA  . LEU B 73  ? 0.6589 0.9495 0.5262 0.1895  0.1466  -0.1767 73  LEU B CA  
1987 C C   . LEU B 73  ? 0.6690 0.9727 0.5587 0.2095  0.1544  -0.1840 73  LEU B C   
1988 O O   . LEU B 73  ? 0.6467 0.9963 0.5538 0.2093  0.1619  -0.1775 73  LEU B O   
1989 C CB  . LEU B 73  ? 0.6246 0.9155 0.5097 0.1840  0.1367  -0.1598 73  LEU B CB  
1990 C CG  . LEU B 73  ? 0.6561 0.9211 0.5236 0.1699  0.1261  -0.1536 73  LEU B CG  
1991 C CD1 . LEU B 73  ? 0.5645 0.8190 0.4541 0.1712  0.1165  -0.1412 73  LEU B CD1 
1992 C CD2 . LEU B 73  ? 0.6131 0.8311 0.4554 0.1719  0.1208  -0.1686 73  LEU B CD2 
1993 N N   . ASN B 74  ? 0.7101 0.9736 0.5995 0.2258  0.1528  -0.1972 74  ASN B N   
1994 C CA  . ASN B 74  ? 0.7681 1.0409 0.6782 0.2462  0.1599  -0.2039 74  ASN B CA  
1995 C C   . ASN B 74  ? 0.7836 1.0612 0.7246 0.2554  0.1520  -0.1907 74  ASN B C   
1996 O O   . ASN B 74  ? 0.7466 1.0167 0.6921 0.2463  0.1416  -0.1777 74  ASN B O   
1997 C CB  . ASN B 74  ? 0.8213 1.0503 0.7176 0.2591  0.1632  -0.2236 74  ASN B CB  
1998 C CG  . ASN B 74  ? 0.9766 1.1488 0.8706 0.2619  0.1511  -0.2238 74  ASN B CG  
1999 O OD1 . ASN B 74  ? 0.8685 1.0341 0.7806 0.2641  0.1415  -0.2103 74  ASN B OD1 
2000 N ND2 . ASN B 74  ? 0.9940 1.1250 0.8655 0.2611  0.1520  -0.2395 74  ASN B ND2 
2001 N N   . SER B 75  ? 0.7643 1.0551 0.7263 0.2741  0.1572  -0.1943 75  SER B N   
2002 C CA  . SER B 75  ? 0.7618 1.0643 0.7532 0.2835  0.1501  -0.1816 75  SER B CA  
2003 C C   . SER B 75  ? 0.8009 1.0515 0.7924 0.2892  0.1377  -0.1782 75  SER B C   
2004 O O   . SER B 75  ? 0.7363 0.9907 0.7429 0.2872  0.1279  -0.1638 75  SER B O   
2005 C CB  . SER B 75  ? 0.8568 1.1866 0.8694 0.3031  0.1587  -0.1870 75  SER B CB  
2006 O OG  . SER B 75  ? 1.0314 1.3200 1.0488 0.3225  0.1557  -0.1936 75  SER B OG  
2007 N N   . GLU B 76  ? 0.7745 0.9767 0.7491 0.2952  0.1381  -0.1912 76  GLU B N   
2008 C CA  . GLU B 76  ? 0.8421 0.9928 0.8147 0.2973  0.1267  -0.1874 76  GLU B CA  
2009 C C   . GLU B 76  ? 0.8317 0.9727 0.7946 0.2784  0.1164  -0.1764 76  GLU B C   
2010 O O   . GLU B 76  ? 0.8066 0.9317 0.7795 0.2783  0.1059  -0.1643 76  GLU B O   
2011 C CB  . GLU B 76  ? 0.8948 0.9974 0.8497 0.3030  0.1305  -0.2045 76  GLU B CB  
2012 C CG  . GLU B 76  ? 1.0211 1.0683 0.9702 0.3004  0.1196  -0.2014 76  GLU B CG  
2013 C CD  . GLU B 76  ? 1.0793 1.0963 1.0002 0.2828  0.1173  -0.2099 76  GLU B CD  
2014 O OE1 . GLU B 76  ? 1.0693 1.0821 0.9726 0.2816  0.1262  -0.2268 76  GLU B OE1 
2015 O OE2 . GLU B 76  ? 0.9920 0.9916 0.9081 0.2700  0.1065  -0.2000 76  GLU B OE2 
2016 N N   . THR B 77  ? 0.7947 0.9471 0.7382 0.2624  0.1194  -0.1799 77  THR B N   
2017 C CA  . THR B 77  ? 0.8027 0.9443 0.7363 0.2454  0.1101  -0.1706 77  THR B CA  
2018 C C   . THR B 77  ? 0.7042 0.8836 0.6582 0.2401  0.1065  -0.1537 77  THR B C   
2019 O O   . THR B 77  ? 0.6757 0.8384 0.6337 0.2348  0.0965  -0.1436 77  THR B O   
2020 C CB  . THR B 77  ? 0.7684 0.9137 0.6749 0.2301  0.1140  -0.1783 77  THR B CB  
2021 O OG1 . THR B 77  ? 0.8668 0.9731 0.7536 0.2329  0.1158  -0.1948 77  THR B OG1 
2022 C CG2 . THR B 77  ? 0.6289 0.7670 0.5264 0.2135  0.1047  -0.1682 77  THR B CG2 
2023 N N   . ILE B 78  ? 0.6386 0.8695 0.6060 0.2404  0.1148  -0.1507 78  ILE B N   
2024 C CA  . ILE B 78  ? 0.6129 0.8822 0.6023 0.2341  0.1118  -0.1353 78  ILE B CA  
2025 C C   . ILE B 78  ? 0.6301 0.8847 0.6390 0.2462  0.1025  -0.1280 78  ILE B C   
2026 O O   . ILE B 78  ? 0.5862 0.8431 0.6043 0.2388  0.0942  -0.1162 78  ILE B O   
2027 C CB  . ILE B 78  ? 0.6416 0.9681 0.6435 0.2320  0.1226  -0.1342 78  ILE B CB  
2028 C CG1 . ILE B 78  ? 0.6218 0.9639 0.6018 0.2162  0.1311  -0.1379 78  ILE B CG1 
2029 C CG2 . ILE B 78  ? 0.5887 0.9550 0.6160 0.2243  0.1190  -0.1189 78  ILE B CG2 
2030 C CD1 . ILE B 78  ? 0.6279 0.9694 0.5980 0.1954  0.1259  -0.1267 78  ILE B CD1 
2031 N N   . GLY B 79  ? 0.6327 0.8707 0.6472 0.2646  0.1038  -0.1347 79  GLY B N   
2032 C CA  . GLY B 79  ? 0.6511 0.8726 0.6812 0.2762  0.0946  -0.1265 79  GLY B CA  
2033 C C   . GLY B 79  ? 0.6393 0.8133 0.6581 0.2697  0.0837  -0.1214 79  GLY B C   
2034 O O   . GLY B 79  ? 0.6376 0.8093 0.6682 0.2702  0.0746  -0.1095 79  GLY B O   
2035 N N   . ARG B 80  ? 0.6476 0.7841 0.6432 0.2628  0.0842  -0.1303 80  ARG B N   
2036 C CA  . ARG B 80  ? 0.6454 0.7384 0.6305 0.2546  0.0742  -0.1256 80  ARG B CA  
2037 C C   . ARG B 80  ? 0.6202 0.7320 0.6085 0.2399  0.0688  -0.1146 80  ARG B C   
2038 O O   . ARG B 80  ? 0.5494 0.6415 0.5412 0.2366  0.0595  -0.1053 80  ARG B O   
2039 C CB  . ARG B 80  ? 0.7033 0.7564 0.6636 0.2487  0.0758  -0.1386 80  ARG B CB  
2040 C CG  . ARG B 80  ? 0.8490 0.8601 0.8065 0.2600  0.0758  -0.1458 80  ARG B CG  
2041 C CD  . ARG B 80  ? 0.8804 0.8536 0.8140 0.2522  0.0776  -0.1604 80  ARG B CD  
2042 N NE  . ARG B 80  ? 0.9622 0.9573 0.8796 0.2433  0.0843  -0.1704 80  ARG B NE  
2043 C CZ  . ARG B 80  ? 0.9677 0.9406 0.8622 0.2299  0.0823  -0.1788 80  ARG B CZ  
2044 N NH1 . ARG B 80  ? 0.9431 0.8724 0.8300 0.2221  0.0739  -0.1783 80  ARG B NH1 
2045 N NH2 . ARG B 80  ? 1.0202 1.0171 0.8989 0.2230  0.0889  -0.1875 80  ARG B NH2 
2046 N N   . ILE B 81  ? 0.5470 0.6974 0.5342 0.2305  0.0752  -0.1153 81  ILE B N   
2047 C CA  . ILE B 81  ? 0.5691 0.7387 0.5616 0.2145  0.0712  -0.1043 81  ILE B CA  
2048 C C   . ILE B 81  ? 0.5579 0.7588 0.5763 0.2179  0.0675  -0.0930 81  ILE B C   
2049 O O   . ILE B 81  ? 0.4827 0.6744 0.5067 0.2047  0.0580  -0.0816 81  ILE B O   
2050 C CB  . ILE B 81  ? 0.5477 0.7466 0.5320 0.1968  0.0780  -0.1037 81  ILE B CB  
2051 C CG1 . ILE B 81  ? 0.5497 0.7201 0.5063 0.1930  0.0803  -0.1150 81  ILE B CG1 
2052 C CG2 . ILE B 81  ? 0.4430 0.6494 0.4336 0.1714  0.0708  -0.0875 81  ILE B CG2 
2053 C CD1 . ILE B 81  ? 0.5053 0.7078 0.4510 0.1786  0.0883  -0.1147 81  ILE B CD1 
2054 N N   . LEU B 82  ? 0.4564 0.6906 0.4900 0.2287  0.0728  -0.0940 82  LEU B N   
2055 C CA  . LEU B 82  ? 0.4894 0.7533 0.5471 0.2317  0.0677  -0.0837 82  LEU B CA  
2056 C C   . LEU B 82  ? 0.5656 0.7928 0.6238 0.2392  0.0565  -0.0778 82  LEU B C   
2057 O O   . LEU B 82  ? 0.4759 0.7163 0.5462 0.2340  0.0490  -0.0678 82  LEU B O   
2058 C CB  . LEU B 82  ? 0.5020 0.8004 0.5740 0.2439  0.0743  -0.0868 82  LEU B CB  
2059 C CG  . LEU B 82  ? 0.5385 0.8809 0.6125 0.2350  0.0859  -0.0907 82  LEU B CG  
2060 C CD1 . LEU B 82  ? 0.5007 0.8741 0.5895 0.2495  0.0923  -0.0947 82  LEU B CD1 
2061 C CD2 . LEU B 82  ? 0.3921 0.7720 0.4768 0.2140  0.0853  -0.0807 82  LEU B CD2 
2062 N N   . ASP B 83  ? 0.5498 0.7314 0.5947 0.2498  0.0556  -0.0836 83  ASP B N   
2063 C CA  . ASP B 83  ? 0.5271 0.6714 0.5704 0.2548  0.0459  -0.0767 83  ASP B CA  
2064 C C   . ASP B 83  ? 0.4998 0.6244 0.5354 0.2402  0.0385  -0.0705 83  ASP B C   
2065 O O   . ASP B 83  ? 0.4850 0.6048 0.5267 0.2396  0.0302  -0.0605 83  ASP B O   
2066 C CB  . ASP B 83  ? 0.4695 0.5672 0.4991 0.2646  0.0477  -0.0847 83  ASP B CB  
2067 C CG  . ASP B 83  ? 0.6530 0.7633 0.6938 0.2833  0.0529  -0.0888 83  ASP B CG  
2068 O OD1 . ASP B 83  ? 0.5192 0.6749 0.5786 0.2893  0.0543  -0.0846 83  ASP B OD1 
2069 O OD2 . ASP B 83  ? 0.5854 0.6602 0.6168 0.2913  0.0560  -0.0972 83  ASP B OD2 
2070 N N   . ILE B 84  ? 0.5042 0.6172 0.5258 0.2287  0.0415  -0.0766 84  ILE B N   
2071 C CA  . ILE B 84  ? 0.4567 0.5469 0.4714 0.2103  0.0338  -0.0697 84  ILE B CA  
2072 C C   . ILE B 84  ? 0.4420 0.5667 0.4723 0.1954  0.0298  -0.0589 84  ILE B C   
2073 O O   . ILE B 84  ? 0.4264 0.5384 0.4584 0.1871  0.0218  -0.0510 84  ILE B O   
2074 C CB  . ILE B 84  ? 0.4433 0.5123 0.4396 0.1948  0.0359  -0.0758 84  ILE B CB  
2075 C CG1 . ILE B 84  ? 0.5064 0.5334 0.4855 0.2061  0.0374  -0.0870 84  ILE B CG1 
2076 C CG2 . ILE B 84  ? 0.4254 0.4788 0.4191 0.1724  0.0280  -0.0668 84  ILE B CG2 
2077 C CD1 . ILE B 84  ? 0.5226 0.5419 0.4836 0.1959  0.0418  -0.0969 84  ILE B CD1 
2078 N N   . CYS B 85  ? 0.3914 0.5606 0.4328 0.1911  0.0357  -0.0591 85  CYS B N   
2079 C CA  . CYS B 85  ? 0.3683 0.5710 0.4257 0.1764  0.0320  -0.0501 85  CYS B CA  
2080 C C   . CYS B 85  ? 0.4162 0.6305 0.4873 0.1884  0.0252  -0.0445 85  CYS B C   
2081 O O   . CYS B 85  ? 0.3548 0.5695 0.4301 0.1757  0.0175  -0.0374 85  CYS B O   
2082 C CB  . CYS B 85  ? 0.3921 0.6432 0.4607 0.1716  0.0405  -0.0512 85  CYS B CB  
2083 S SG  . CYS B 85  ? 0.4595 0.7026 0.5105 0.1536  0.0476  -0.0540 85  CYS B SG  
2084 N N   . ARG B 86  ? 0.4163 0.6411 0.4940 0.2135  0.0278  -0.0478 86  ARG B N   
2085 C CA  . ARG B 86  ? 0.4114 0.6469 0.5008 0.2263  0.0203  -0.0406 86  ARG B CA  
2086 C C   . ARG B 86  ? 0.3970 0.5887 0.4738 0.2253  0.0115  -0.0350 86  ARG B C   
2087 O O   . ARG B 86  ? 0.4066 0.6084 0.4895 0.2211  0.0032  -0.0266 86  ARG B O   
2088 C CB  . ARG B 86  ? 0.4666 0.7024 0.5589 0.2447  0.0237  -0.0430 86  ARG B CB  
2089 C CG  . ARG B 86  ? 0.4588 0.6927 0.5577 0.2564  0.0151  -0.0338 86  ARG B CG  
2090 C CD  . ARG B 86  ? 0.4818 0.7646 0.5988 0.2494  0.0088  -0.0261 86  ARG B CD  
2091 N NE  . ARG B 86  ? 0.5076 0.7912 0.6294 0.2612  0.0003  -0.0169 86  ARG B NE  
2092 C CZ  . ARG B 86  ? 0.5526 0.8684 0.6850 0.2552  -0.0083 -0.0089 86  ARG B CZ  
2093 N NH1 . ARG B 86  ? 0.4356 0.7858 0.5770 0.2366  -0.0094 -0.0097 86  ARG B NH1 
2094 N NH2 . ARG B 86  ? 0.5331 0.8474 0.6674 0.2673  -0.0160 -0.0001 86  ARG B NH2 
2095 N N   . LYS B 87  ? 0.4098 0.5530 0.4680 0.2271  0.0133  -0.0398 87  LYS B N   
2096 C CA  . LYS B 87  ? 0.4770 0.5777 0.5225 0.2228  0.0062  -0.0343 87  LYS B CA  
2097 C C   . LYS B 87  ? 0.4438 0.5496 0.4895 0.1980  0.0010  -0.0288 87  LYS B C   
2098 O O   . LYS B 87  ? 0.3814 0.4826 0.4269 0.1952  -0.0062 -0.0212 87  LYS B O   
2099 C CB  . LYS B 87  ? 0.4398 0.4926 0.4665 0.2219  0.0097  -0.0418 87  LYS B CB  
2100 C CG  . LYS B 87  ? 0.5676 0.5750 0.5816 0.2182  0.0039  -0.0363 87  LYS B CG  
2101 C CD  . LYS B 87  ? 0.6280 0.6377 0.6478 0.2283  -0.0018 -0.0254 87  LYS B CD  
2102 C CE  . LYS B 87  ? 0.6513 0.6126 0.6571 0.2261  -0.0049 -0.0206 87  LYS B CE  
2103 N NZ  . LYS B 87  ? 0.8380 0.7780 0.8426 0.2390  -0.0025 -0.0217 87  LYS B NZ  
2104 N N   . LEU B 88  ? 0.4178 0.5332 0.4635 0.1799  0.0047  -0.0327 88  LEU B N   
2105 C CA  . LEU B 88  ? 0.3366 0.4545 0.3836 0.1575  0.0005  -0.0286 88  LEU B CA  
2106 C C   . LEU B 88  ? 0.3571 0.5137 0.4194 0.1547  -0.0041 -0.0234 88  LEU B C   
2107 O O   . LEU B 88  ? 0.3681 0.5203 0.4295 0.1442  -0.0102 -0.0195 88  LEU B O   
2108 C CB  . LEU B 88  ? 0.3835 0.5051 0.4286 0.1411  0.0055  -0.0323 88  LEU B CB  
2109 C CG  . LEU B 88  ? 0.4122 0.4950 0.4407 0.1381  0.0072  -0.0365 88  LEU B CG  
2110 C CD1 . LEU B 88  ? 0.3727 0.4651 0.3991 0.1240  0.0117  -0.0382 88  LEU B CD1 
2111 C CD2 . LEU B 88  ? 0.3879 0.4382 0.4093 0.1288  0.0012  -0.0333 88  LEU B CD2 
2112 N N   . ASP B 89  ? 0.3327 0.5301 0.4094 0.1637  -0.0010 -0.0243 89  ASP B N   
2113 C CA  . ASP B 89  ? 0.3915 0.6313 0.4845 0.1624  -0.0061 -0.0198 89  ASP B CA  
2114 C C   . ASP B 89  ? 0.4659 0.6951 0.5553 0.1737  -0.0147 -0.0133 89  ASP B C   
2115 O O   . ASP B 89  ? 0.3387 0.5807 0.4306 0.1625  -0.0217 -0.0095 89  ASP B O   
2116 C CB  . ASP B 89  ? 0.3703 0.6556 0.4804 0.1761  -0.0010 -0.0216 89  ASP B CB  
2117 C CG  . ASP B 89  ? 0.4256 0.7390 0.5436 0.1591  0.0064  -0.0251 89  ASP B CG  
2118 O OD1 . ASP B 89  ? 0.3505 0.6434 0.4597 0.1382  0.0072  -0.0256 89  ASP B OD1 
2119 O OD2 . ASP B 89  ? 0.3829 0.7399 0.5167 0.1672  0.0117  -0.0267 89  ASP B OD2 
2120 N N   . VAL B 90  ? 0.3851 0.5889 0.4669 0.1953  -0.0142 -0.0120 90  VAL B N   
2121 C CA  . VAL B 90  ? 0.4145 0.6093 0.4927 0.2084  -0.0222 -0.0032 90  VAL B CA  
2122 C C   . VAL B 90  ? 0.4561 0.6180 0.5187 0.1924  -0.0268 0.0001  90  VAL B C   
2123 O O   . VAL B 90  ? 0.4891 0.6605 0.5503 0.1899  -0.0344 0.0071  90  VAL B O   
2124 C CB  . VAL B 90  ? 0.4676 0.6353 0.5402 0.2327  -0.0195 -0.0025 90  VAL B CB  
2125 C CG1 . VAL B 90  ? 0.5250 0.6624 0.5857 0.2386  -0.0267 0.0080  90  VAL B CG1 
2126 C CG2 . VAL B 90  ? 0.4329 0.6352 0.5208 0.2445  -0.0165 -0.0035 90  VAL B CG2 
2127 N N   . LEU B 91  ? 0.4290 0.5557 0.4800 0.1807  -0.0221 -0.0053 91  LEU B N   
2128 C CA  . LEU B 91  ? 0.3983 0.4949 0.4364 0.1652  -0.0246 -0.0038 91  LEU B CA  
2129 C C   . LEU B 91  ? 0.3835 0.5023 0.4269 0.1445  -0.0276 -0.0050 91  LEU B C   
2130 O O   . LEU B 91  ? 0.4280 0.5281 0.4622 0.1330  -0.0298 -0.0040 91  LEU B O   
2131 C CB  . LEU B 91  ? 0.3933 0.4537 0.4215 0.1593  -0.0189 -0.0101 91  LEU B CB  
2132 C CG  . LEU B 91  ? 0.5016 0.5282 0.5199 0.1761  -0.0165 -0.0105 91  LEU B CG  
2133 C CD1 . LEU B 91  ? 0.4151 0.4143 0.4248 0.1678  -0.0114 -0.0187 91  LEU B CD1 
2134 C CD2 . LEU B 91  ? 0.4724 0.4727 0.4803 0.1810  -0.0214 -0.0017 91  LEU B CD2 
2135 N N   . GLY B 92  ? 0.3209 0.4783 0.3787 0.1388  -0.0270 -0.0078 92  GLY B N   
2136 C CA  . GLY B 92  ? 0.3242 0.4985 0.3868 0.1177  -0.0295 -0.0105 92  GLY B CA  
2137 C C   . GLY B 92  ? 0.3628 0.5168 0.4229 0.1000  -0.0247 -0.0162 92  GLY B C   
2138 O O   . GLY B 92  ? 0.3334 0.4877 0.3940 0.0831  -0.0266 -0.0189 92  GLY B O   
2139 N N   . ILE B 93  ? 0.3292 0.4660 0.3862 0.1036  -0.0188 -0.0182 93  ILE B N   
2140 C CA  . ILE B 93  ? 0.3528 0.4707 0.4070 0.0885  -0.0152 -0.0216 93  ILE B CA  
2141 C C   . ILE B 93  ? 0.3654 0.5080 0.4290 0.0834  -0.0103 -0.0228 93  ILE B C   
2142 O O   . ILE B 93  ? 0.3654 0.5146 0.4287 0.0953  -0.0059 -0.0236 93  ILE B O   
2143 C CB  . ILE B 93  ? 0.3808 0.4597 0.4218 0.0936  -0.0131 -0.0224 93  ILE B CB  
2144 C CG1 . ILE B 93  ? 0.3554 0.4109 0.3874 0.0962  -0.0170 -0.0201 93  ILE B CG1 
2145 C CG2 . ILE B 93  ? 0.2861 0.3504 0.3256 0.0795  -0.0102 -0.0246 93  ILE B CG2 
2146 C CD1 . ILE B 93  ? 0.3459 0.3669 0.3662 0.1035  -0.0152 -0.0205 93  ILE B CD1 
2147 N N   . GLN B 94  ? 0.2921 0.4472 0.3634 0.0652  -0.0106 -0.0234 94  GLN B N   
2148 C CA  . GLN B 94  ? 0.3168 0.4916 0.3958 0.0555  -0.0057 -0.0228 94  GLN B CA  
2149 C C   . GLN B 94  ? 0.3519 0.4958 0.4218 0.0472  -0.0029 -0.0220 94  GLN B C   
2150 O O   . GLN B 94  ? 0.3402 0.4636 0.4088 0.0349  -0.0054 -0.0221 94  GLN B O   
2151 C CB  . GLN B 94  ? 0.3684 0.5707 0.4605 0.0386  -0.0079 -0.0230 94  GLN B CB  
2152 C CG  . GLN B 94  ? 0.3294 0.5514 0.4298 0.0247  -0.0024 -0.0208 94  GLN B CG  
2153 C CD  . GLN B 94  ? 0.4740 0.7369 0.5906 0.0130  -0.0040 -0.0213 94  GLN B CD  
2154 O OE1 . GLN B 94  ? 0.4027 0.7013 0.5286 0.0238  -0.0048 -0.0215 94  GLN B OE1 
2155 N NE2 . GLN B 94  ? 0.4634 0.7209 0.5843 -0.0092 -0.0050 -0.0217 94  GLN B NE2 
2156 N N   . LYS B 95  ? 0.3184 0.4590 0.3816 0.0550  0.0019  -0.0218 95  LYS B N   
2157 C CA  . LYS B 95  ? 0.3093 0.4230 0.3626 0.0484  0.0032  -0.0202 95  LYS B CA  
2158 C C   . LYS B 95  ? 0.3549 0.4757 0.4137 0.0298  0.0048  -0.0153 95  LYS B C   
2159 O O   . LYS B 95  ? 0.3880 0.4835 0.4424 0.0211  0.0028  -0.0125 95  LYS B O   
2160 C CB  . LYS B 95  ? 0.3357 0.4465 0.3784 0.0610  0.0076  -0.0226 95  LYS B CB  
2161 C CG  . LYS B 95  ? 0.3429 0.4281 0.3731 0.0561  0.0076  -0.0215 95  LYS B CG  
2162 C CD  . LYS B 95  ? 0.3889 0.4695 0.4068 0.0700  0.0112  -0.0271 95  LYS B CD  
2163 C CE  . LYS B 95  ? 0.4022 0.4583 0.4065 0.0647  0.0095  -0.0268 95  LYS B CE  
2164 N NZ  . LYS B 95  ? 0.3844 0.4543 0.3880 0.0512  0.0118  -0.0197 95  LYS B NZ  
2165 N N   . GLU B 96  ? 0.2813 0.4363 0.3506 0.0235  0.0081  -0.0136 96  GLU B N   
2166 C CA  . GLU B 96  ? 0.4501 0.6162 0.5253 0.0047  0.0108  -0.0077 96  GLU B CA  
2167 C C   . GLU B 96  ? 0.4656 0.6336 0.5309 0.0045  0.0166  -0.0029 96  GLU B C   
2168 O O   . GLU B 96  ? 0.4084 0.5610 0.4608 0.0168  0.0172  -0.0054 96  GLU B O   
2169 C CB  . GLU B 96  ? 0.4100 0.5481 0.4870 -0.0102 0.0062  -0.0056 96  GLU B CB  
2170 C CG  . GLU B 96  ? 0.4301 0.5683 0.5153 -0.0132 0.0011  -0.0117 96  GLU B CG  
2171 C CD  . GLU B 96  ? 0.6180 0.7935 0.7172 -0.0235 0.0015  -0.0129 96  GLU B CD  
2172 O OE1 . GLU B 96  ? 0.6057 0.8132 0.7105 -0.0244 0.0064  -0.0097 96  GLU B OE1 
2173 O OE2 . GLU B 96  ? 0.5492 0.7244 0.6542 -0.0311 -0.0031 -0.0179 96  GLU B OE2 
2174 N N   . GLU B 97  ? 0.3835 0.5730 0.4541 -0.0101 0.0213  0.0036  97  GLU B N   
2175 C CA  . GLU B 97  ? 0.5228 0.7176 0.5827 -0.0142 0.0272  0.0102  97  GLU B CA  
2176 C C   . GLU B 97  ? 0.5081 0.7217 0.5597 0.0035  0.0333  0.0041  97  GLU B C   
2177 O O   . GLU B 97  ? 0.4846 0.6941 0.5213 0.0045  0.0369  0.0064  97  GLU B O   
2178 C CB  . GLU B 97  ? 0.5044 0.6603 0.5518 -0.0193 0.0229  0.0164  97  GLU B CB  
2179 C CG  . GLU B 97  ? 0.6086 0.7461 0.6642 -0.0375 0.0189  0.0238  97  GLU B CG  
2180 C CD  . GLU B 97  ? 0.8759 1.0309 0.9341 -0.0560 0.0241  0.0351  97  GLU B CD  
2181 O OE1 . GLU B 97  ? 1.0259 1.1788 1.0711 -0.0587 0.0269  0.0441  97  GLU B OE1 
2182 O OE2 . GLU B 97  ? 0.8781 1.0503 0.9506 -0.0689 0.0255  0.0353  97  GLU B OE2 
2183 N N   . MET B 98  ? 0.3937 0.6278 0.4542 0.0180  0.0342  -0.0040 98  MET B N   
2184 C CA  . MET B 98  ? 0.4253 0.6751 0.4797 0.0371  0.0404  -0.0114 98  MET B CA  
2185 C C   . MET B 98  ? 0.3981 0.6905 0.4559 0.0326  0.0509  -0.0093 98  MET B C   
2186 O O   . MET B 98  ? 0.4059 0.7129 0.4570 0.0476  0.0580  -0.0163 98  MET B O   
2187 C CB  . MET B 98  ? 0.4564 0.7139 0.5210 0.0552  0.0376  -0.0189 98  MET B CB  
2188 C CG  . MET B 98  ? 0.4526 0.6705 0.5069 0.0692  0.0312  -0.0241 98  MET B CG  
2189 S SD  . MET B 98  ? 0.5066 0.6866 0.5370 0.0716  0.0317  -0.0268 98  MET B SD  
2190 C CE  . MET B 98  ? 0.4517 0.6518 0.4767 0.0930  0.0410  -0.0372 98  MET B CE  
2191 N N   . ASN B 99  ? 0.3690 0.6825 0.4378 0.0122  0.0526  -0.0006 99  ASN B N   
2192 C CA  . ASN B 99  ? 0.4222 0.7749 0.4926 0.0034  0.0632  0.0039  99  ASN B CA  
2193 C C   . ASN B 99  ? 0.4155 0.7501 0.4652 -0.0079 0.0659  0.0122  99  ASN B C   
2194 O O   . ASN B 99  ? 0.4197 0.7847 0.4654 -0.0147 0.0756  0.0165  99  ASN B O   
2195 C CB  . ASN B 99  ? 0.4419 0.8267 0.5336 -0.0159 0.0641  0.0103  99  ASN B CB  
2196 C CG  . ASN B 99  ? 0.4396 0.7916 0.5318 -0.0375 0.0563  0.0190  99  ASN B CG  
2197 O OD1 . ASN B 99  ? 0.4637 0.7742 0.5493 -0.0331 0.0477  0.0169  99  ASN B OD1 
2198 N ND2 . ASN B 99  ? 0.4773 0.8475 0.5780 -0.0610 0.0598  0.0285  99  ASN B ND2 
2199 N N   . HIS B 100 ? 0.4254 0.7142 0.4623 -0.0096 0.0576  0.0151  100 HIS B N   
2200 C CA  . HIS B 100 ? 0.5007 0.7701 0.5158 -0.0156 0.0579  0.0222  100 HIS B CA  
2201 C C   . HIS B 100 ? 0.4540 0.6889 0.4543 0.0004  0.0518  0.0136  100 HIS B C   
2202 O O   . HIS B 100 ? 0.4180 0.6181 0.4115 -0.0047 0.0435  0.0190  100 HIS B O   
2203 C CB  . HIS B 100 ? 0.5504 0.7992 0.5667 -0.0374 0.0529  0.0376  100 HIS B CB  
2204 C CG  . HIS B 100 ? 0.6165 0.8955 0.6460 -0.0568 0.0589  0.0470  100 HIS B CG  
2205 N ND1 . HIS B 100 ? 0.5727 0.8918 0.5983 -0.0622 0.0702  0.0509  100 HIS B ND1 
2206 C CD2 . HIS B 100 ? 0.6404 0.9171 0.6871 -0.0728 0.0558  0.0522  100 HIS B CD2 
2207 C CE1 . HIS B 100 ? 0.6426 0.9831 0.6835 -0.0819 0.0736  0.0595  100 HIS B CE1 
2208 N NE2 . HIS B 100 ? 0.6474 0.9615 0.7010 -0.0889 0.0646  0.0599  100 HIS B NE2 
2209 N N   . PRO B 101 ? 0.4562 0.6997 0.4521 0.0198  0.0557  0.0001  101 PRO B N   
2210 C CA  . PRO B 101 ? 0.4537 0.6631 0.4364 0.0336  0.0499  -0.0090 101 PRO B CA  
2211 C C   . PRO B 101 ? 0.5238 0.7243 0.4820 0.0323  0.0512  -0.0094 101 PRO B C   
2212 O O   . PRO B 101 ? 0.4805 0.6583 0.4265 0.0436  0.0480  -0.0194 101 PRO B O   
2213 C CB  . PRO B 101 ? 0.4349 0.6583 0.4240 0.0545  0.0546  -0.0229 101 PRO B CB  
2214 C CG  . PRO B 101 ? 0.4522 0.7220 0.4459 0.0534  0.0662  -0.0228 101 PRO B CG  
2215 C CD  . PRO B 101 ? 0.4705 0.7553 0.4745 0.0306  0.0659  -0.0079 101 PRO B CD  
2216 N N   . ASP B 102 ? 0.4971 0.7152 0.4477 0.0174  0.0553  0.0020  102 ASP B N   
2217 C CA  . ASP B 102 ? 0.5212 0.7445 0.4468 0.0161  0.0590  0.0016  102 ASP B CA  
2218 C C   . ASP B 102 ? 0.4762 0.6635 0.3857 0.0207  0.0494  -0.0029 102 ASP B C   
2219 O O   . ASP B 102 ? 0.6012 0.7884 0.4917 0.0292  0.0520  -0.0146 102 ASP B O   
2220 C CB  . ASP B 102 ? 0.5210 0.7593 0.4418 -0.0043 0.0612  0.0203  102 ASP B CB  
2221 C CG  . ASP B 102 ? 0.6092 0.8864 0.5463 -0.0118 0.0714  0.0249  102 ASP B CG  
2222 O OD1 . ASP B 102 ? 0.5255 0.8017 0.4857 -0.0136 0.0687  0.0257  102 ASP B OD1 
2223 O OD2 . ASP B 102 ? 0.6064 0.9171 0.5334 -0.0168 0.0820  0.0273  102 ASP B OD2 
2224 N N   . ARG B 103 ? 0.5031 0.6608 0.4201 0.0146  0.0385  0.0053  103 ARG B N   
2225 C CA  . ARG B 103 ? 0.5173 0.6448 0.4221 0.0171  0.0288  0.0024  103 ARG B CA  
2226 C C   . ARG B 103 ? 0.5705 0.6726 0.4863 0.0283  0.0234  -0.0084 103 ARG B C   
2227 O O   . ARG B 103 ? 0.4529 0.5301 0.3630 0.0289  0.0150  -0.0101 103 ARG B O   
2228 C CB  . ARG B 103 ? 0.6454 0.7587 0.5497 0.0031  0.0201  0.0203  103 ARG B CB  
2229 C CG  . ARG B 103 ? 0.7673 0.9010 0.6566 -0.0095 0.0238  0.0345  103 ARG B CG  
2230 C CD  . ARG B 103 ? 0.8801 0.9941 0.7723 -0.0209 0.0140  0.0535  103 ARG B CD  
2231 N NE  . ARG B 103 ? 0.9878 1.0980 0.9023 -0.0287 0.0150  0.0625  103 ARG B NE  
2232 C CZ  . ARG B 103 ? 0.9746 1.0595 0.9071 -0.0272 0.0081  0.0623  103 ARG B CZ  
2233 N NH1 . ARG B 103 ? 0.9235 0.9860 0.8560 -0.0188 -0.0003 0.0558  103 ARG B NH1 
2234 N NH2 . ARG B 103 ? 0.9459 1.0298 0.8968 -0.0349 0.0102  0.0673  103 ARG B NH2 
2235 N N   . HIS B 104 ? 0.4916 0.6011 0.4232 0.0366  0.0277  -0.0146 104 HIS B N   
2236 C CA  . HIS B 104 ? 0.4607 0.5467 0.4038 0.0448  0.0221  -0.0207 104 HIS B CA  
2237 C C   . HIS B 104 ? 0.4811 0.5658 0.4218 0.0621  0.0264  -0.0358 104 HIS B C   
2238 O O   . HIS B 104 ? 0.4899 0.5558 0.4387 0.0694  0.0224  -0.0398 104 HIS B O   
2239 C CB  . HIS B 104 ? 0.4631 0.5533 0.4274 0.0387  0.0206  -0.0129 104 HIS B CB  
2240 C CG  . HIS B 104 ? 0.5197 0.6006 0.4878 0.0232  0.0153  0.0008  104 HIS B CG  
2241 N ND1 . HIS B 104 ? 0.5820 0.6734 0.5645 0.0124  0.0164  0.0095  104 HIS B ND1 
2242 C CD2 . HIS B 104 ? 0.5434 0.6050 0.5032 0.0172  0.0085  0.0072  104 HIS B CD2 
2243 C CE1 . HIS B 104 ? 0.6085 0.6836 0.5912 0.0012  0.0110  0.0206  104 HIS B CE1 
2244 N NE2 . HIS B 104 ? 0.6653 0.7236 0.6349 0.0048  0.0060  0.0201  104 HIS B NE2 
2245 N N   . ILE B 105 ? 0.4780 0.5815 0.4074 0.0692  0.0347  -0.0440 105 ILE B N   
2246 C CA  . ILE B 105 ? 0.4954 0.5920 0.4188 0.0870  0.0389  -0.0599 105 ILE B CA  
2247 C C   . ILE B 105 ? 0.5232 0.6106 0.4218 0.0862  0.0396  -0.0688 105 ILE B C   
2248 O O   . ILE B 105 ? 0.5307 0.6423 0.4175 0.0812  0.0458  -0.0681 105 ILE B O   
2249 C CB  . ILE B 105 ? 0.4450 0.5747 0.3787 0.0988  0.0493  -0.0646 105 ILE B CB  
2250 C CG1 . ILE B 105 ? 0.4393 0.5828 0.3974 0.0964  0.0471  -0.0549 105 ILE B CG1 
2251 C CG2 . ILE B 105 ? 0.5074 0.6258 0.4349 0.1195  0.0537  -0.0813 105 ILE B CG2 
2252 C CD1 . ILE B 105 ? 0.4297 0.6107 0.4020 0.1085  0.0560  -0.0588 105 ILE B CD1 
2253 N N   . ILE B 106 ? 0.4991 0.5532 0.3891 0.0899  0.0335  -0.0772 106 ILE B N   
2254 C CA  . ILE B 106 ? 0.4834 0.5266 0.3493 0.0873  0.0323  -0.0873 106 ILE B CA  
2255 C C   . ILE B 106 ? 0.5753 0.6083 0.4323 0.1043  0.0391  -0.1070 106 ILE B C   
2256 O O   . ILE B 106 ? 0.5653 0.5749 0.4314 0.1149  0.0375  -0.1121 106 ILE B O   
2257 C CB  . ILE B 106 ? 0.5652 0.5799 0.4277 0.0769  0.0201  -0.0835 106 ILE B CB  
2258 C CG1 . ILE B 106 ? 0.5200 0.5404 0.3967 0.0641  0.0136  -0.0643 106 ILE B CG1 
2259 C CG2 . ILE B 106 ? 0.5642 0.5753 0.4017 0.0708  0.0175  -0.0919 106 ILE B CG2 
2260 C CD1 . ILE B 106 ? 0.5497 0.5979 0.4196 0.0539  0.0162  -0.0530 106 ILE B CD1 
2261 N N   . ILE B 107 ? 0.5854 0.6348 0.4237 0.1070  0.0470  -0.1181 107 ILE B N   
2262 C CA  . ILE B 107 ? 0.6386 0.6834 0.4693 0.1251  0.0561  -0.1381 107 ILE B CA  
2263 C C   . ILE B 107 ? 0.6933 0.7170 0.4966 0.1214  0.0540  -0.1542 107 ILE B C   
2264 O O   . ILE B 107 ? 0.6146 0.6552 0.3994 0.1093  0.0536  -0.1533 107 ILE B O   
2265 C CB  . ILE B 107 ? 0.6076 0.6949 0.4413 0.1336  0.0698  -0.1406 107 ILE B CB  
2266 C CG1 . ILE B 107 ? 0.6535 0.7618 0.5159 0.1362  0.0708  -0.1257 107 ILE B CG1 
2267 C CG2 . ILE B 107 ? 0.6626 0.7446 0.4868 0.1540  0.0801  -0.1637 107 ILE B CG2 
2268 C CD1 . ILE B 107 ? 0.6572 0.8145 0.5262 0.1369  0.0823  -0.1222 107 ILE B CD1 
2269 N N   . SER B 108 ? 0.7361 0.7224 0.5367 0.1305  0.0517  -0.1680 108 SER B N   
2270 C CA  . SER B 108 ? 0.8295 0.7916 0.6048 0.1292  0.0508  -0.1880 108 SER B CA  
2271 C C   . SER B 108 ? 0.8286 0.7709 0.6057 0.1500  0.0598  -0.2058 108 SER B C   
2272 O O   . SER B 108 ? 0.8390 0.8058 0.6284 0.1624  0.0702  -0.2049 108 SER B O   
2273 C CB  . SER B 108 ? 0.8394 0.7696 0.6125 0.1142  0.0368  -0.1839 108 SER B CB  
2274 O OG  . SER B 108 ? 0.7706 0.6724 0.5629 0.1203  0.0328  -0.1784 108 SER B OG  
2275 N N   . ASP B 109 ? 0.8314 0.7310 0.6055 0.1475  0.0554  -0.2144 109 ASP B N   
2276 C CA  . ASP B 109 ? 0.8105 0.6874 0.5998 0.1613  0.0616  -0.2187 109 ASP B CA  
2277 C C   . ASP B 109 ? 0.8729 0.7506 0.6890 0.1714  0.0593  -0.2021 109 ASP B C   
2278 O O   . ASP B 109 ? 0.7871 0.6627 0.6190 0.1862  0.0654  -0.2016 109 ASP B O   
2279 C CB  . ASP B 109 ? 0.9492 0.7801 0.7306 0.1533  0.0571  -0.2290 109 ASP B CB  
2280 C CG  . ASP B 109 ? 1.1249 0.9390 0.9023 0.1364  0.0434  -0.2216 109 ASP B CG  
2281 O OD1 . ASP B 109 ? 1.1033 0.9351 0.8640 0.1245  0.0378  -0.2225 109 ASP B OD1 
2282 O OD2 . ASP B 109 ? 1.1519 0.9385 0.9435 0.1351  0.0380  -0.2135 109 ASP B OD2 
2283 N N   . ARG B 110 ? 0.8400 0.7211 0.6611 0.1637  0.0503  -0.1885 110 ARG B N   
2284 C CA  . ARG B 110 ? 0.7430 0.6264 0.5870 0.1703  0.0471  -0.1724 110 ARG B CA  
2285 C C   . ARG B 110 ? 0.7408 0.6658 0.5930 0.1653  0.0471  -0.1592 110 ARG B C   
2286 O O   . ARG B 110 ? 0.7129 0.6618 0.5546 0.1531  0.0482  -0.1584 110 ARG B O   
2287 C CB  . ARG B 110 ? 0.7174 0.5636 0.5645 0.1605  0.0366  -0.1654 110 ARG B CB  
2288 C CG  . ARG B 110 ? 0.7381 0.5808 0.5723 0.1413  0.0280  -0.1643 110 ARG B CG  
2289 C CD  . ARG B 110 ? 0.7422 0.5611 0.5871 0.1312  0.0185  -0.1523 110 ARG B CD  
2290 N NE  . ARG B 110 ? 0.6946 0.5176 0.5347 0.1104  0.0100  -0.1473 110 ARG B NE  
2291 C CZ  . ARG B 110 ? 0.7764 0.5898 0.6274 0.0990  0.0021  -0.1357 110 ARG B CZ  
2292 N NH1 . ARG B 110 ? 0.7808 0.5806 0.6460 0.1045  0.0016  -0.1272 110 ARG B NH1 
2293 N NH2 . ARG B 110 ? 0.7157 0.5353 0.5632 0.0821  -0.0054 -0.1325 110 ARG B NH2 
2294 N N   . ILE B 111 ? 0.6195 0.5541 0.4937 0.1701  0.0453  -0.1449 111 ILE B N   
2295 C CA  . ILE B 111 ? 0.5706 0.5440 0.4595 0.1616  0.0452  -0.1292 111 ILE B CA  
2296 C C   . ILE B 111 ? 0.5873 0.5462 0.4873 0.1491  0.0348  -0.1143 111 ILE B C   
2297 O O   . ILE B 111 ? 0.5924 0.5319 0.5019 0.1568  0.0316  -0.1110 111 ILE B O   
2298 C CB  . ILE B 111 ? 0.5530 0.5572 0.4595 0.1786  0.0529  -0.1275 111 ILE B CB  
2299 C CG1 . ILE B 111 ? 0.6578 0.6762 0.5552 0.1947  0.0648  -0.1445 111 ILE B CG1 
2300 C CG2 . ILE B 111 ? 0.5475 0.5911 0.4693 0.1666  0.0526  -0.1120 111 ILE B CG2 
2301 C CD1 . ILE B 111 ? 0.6969 0.7318 0.5746 0.1831  0.0696  -0.1514 111 ILE B CD1 
2302 N N   . VAL B 112 ? 0.4866 0.4549 0.3853 0.1305  0.0298  -0.1048 112 VAL B N   
2303 C CA  . VAL B 112 ? 0.5188 0.4759 0.4288 0.1191  0.0210  -0.0919 112 VAL B CA  
2304 C C   . VAL B 112 ? 0.5267 0.5150 0.4497 0.1097  0.0211  -0.0785 112 VAL B C   
2305 O O   . VAL B 112 ? 0.4728 0.4826 0.3894 0.1021  0.0240  -0.0763 112 VAL B O   
2306 C CB  . VAL B 112 ? 0.4700 0.4027 0.3689 0.1057  0.0132  -0.0929 112 VAL B CB  
2307 C CG1 . VAL B 112 ? 0.4210 0.3437 0.3341 0.0962  0.0055  -0.0806 112 VAL B CG1 
2308 C CG2 . VAL B 112 ? 0.6016 0.5029 0.4860 0.1126  0.0135  -0.1081 112 VAL B CG2 
2309 N N   . PHE B 113 ? 0.4139 0.4041 0.3537 0.1095  0.0182  -0.0696 113 PHE B N   
2310 C CA  . PHE B 113 ? 0.3984 0.4107 0.3512 0.0981  0.0168  -0.0576 113 PHE B CA  
2311 C C   . PHE B 113 ? 0.4782 0.4717 0.4317 0.0841  0.0088  -0.0506 113 PHE B C   
2312 O O   . PHE B 113 ? 0.4425 0.4109 0.3959 0.0850  0.0041  -0.0523 113 PHE B O   
2313 C CB  . PHE B 113 ? 0.3859 0.4117 0.3560 0.1047  0.0174  -0.0535 113 PHE B CB  
2314 C CG  . PHE B 113 ? 0.4073 0.4642 0.3834 0.1166  0.0252  -0.0571 113 PHE B CG  
2315 C CD1 . PHE B 113 ? 0.4118 0.4728 0.3767 0.1274  0.0320  -0.0675 113 PHE B CD1 
2316 C CD2 . PHE B 113 ? 0.4646 0.5477 0.4584 0.1178  0.0255  -0.0513 113 PHE B CD2 
2317 C CE1 . PHE B 113 ? 0.4577 0.5501 0.4303 0.1402  0.0400  -0.0715 113 PHE B CE1 
2318 C CE2 . PHE B 113 ? 0.4201 0.5364 0.4226 0.1293  0.0323  -0.0543 113 PHE B CE2 
2319 C CZ  . PHE B 113 ? 0.3924 0.5141 0.3852 0.1415  0.0401  -0.0643 113 PHE B CZ  
2320 N N   . ILE B 114 ? 0.3722 0.3782 0.3274 0.0713  0.0076  -0.0420 114 ILE B N   
2321 C CA  . ILE B 114 ? 0.3908 0.3808 0.3495 0.0602  0.0001  -0.0350 114 ILE B CA  
2322 C C   . ILE B 114 ? 0.3963 0.3995 0.3691 0.0509  -0.0002 -0.0246 114 ILE B C   
2323 O O   . ILE B 114 ? 0.4169 0.4436 0.3943 0.0499  0.0050  -0.0220 114 ILE B O   
2324 C CB  . ILE B 114 ? 0.4316 0.4153 0.3758 0.0536  -0.0035 -0.0347 114 ILE B CB  
2325 C CG1 . ILE B 114 ? 0.4471 0.4545 0.3841 0.0478  0.0005  -0.0289 114 ILE B CG1 
2326 C CG2 . ILE B 114 ? 0.4185 0.3863 0.3480 0.0607  -0.0037 -0.0473 114 ILE B CG2 
2327 C CD1 . ILE B 114 ? 0.4759 0.4802 0.3990 0.0392  -0.0050 -0.0243 114 ILE B CD1 
2328 N N   . ASP B 115 ? 0.3939 0.3817 0.3744 0.0440  -0.0061 -0.0195 115 ASP B N   
2329 C CA  . ASP B 115 ? 0.4128 0.4043 0.4063 0.0342  -0.0075 -0.0108 115 ASP B CA  
2330 C C   . ASP B 115 ? 0.3726 0.3721 0.3786 0.0359  -0.0055 -0.0129 115 ASP B C   
2331 O O   . ASP B 115 ? 0.3314 0.3528 0.3422 0.0341  -0.0013 -0.0114 115 ASP B O   
2332 C CB  . ASP B 115 ? 0.4585 0.4660 0.4489 0.0255  -0.0051 -0.0021 115 ASP B CB  
2333 C CG  . ASP B 115 ? 0.6307 0.6373 0.6346 0.0144  -0.0064 0.0068  115 ASP B CG  
2334 O OD1 . ASP B 115 ? 0.5911 0.5816 0.6048 0.0138  -0.0103 0.0055  115 ASP B OD1 
2335 O OD2 . ASP B 115 ? 0.6821 0.7024 0.6862 0.0057  -0.0034 0.0148  115 ASP B OD2 
2336 N N   . PHE B 116 ? 0.3637 0.3479 0.3752 0.0380  -0.0088 -0.0158 116 PHE B N   
2337 C CA  . PHE B 116 ? 0.3794 0.3704 0.4003 0.0392  -0.0082 -0.0180 116 PHE B CA  
2338 C C   . PHE B 116 ? 0.3801 0.3656 0.4119 0.0288  -0.0104 -0.0153 116 PHE B C   
2339 O O   . PHE B 116 ? 0.3837 0.3724 0.4219 0.0284  -0.0108 -0.0184 116 PHE B O   
2340 C CB  . PHE B 116 ? 0.3587 0.3374 0.3752 0.0493  -0.0093 -0.0234 116 PHE B CB  
2341 C CG  . PHE B 116 ? 0.3841 0.3700 0.3930 0.0614  -0.0061 -0.0272 116 PHE B CG  
2342 C CD1 . PHE B 116 ? 0.4193 0.3953 0.4163 0.0657  -0.0052 -0.0306 116 PHE B CD1 
2343 C CD2 . PHE B 116 ? 0.4088 0.4129 0.4229 0.0686  -0.0043 -0.0280 116 PHE B CD2 
2344 C CE1 . PHE B 116 ? 0.3914 0.3719 0.3814 0.0782  -0.0014 -0.0361 116 PHE B CE1 
2345 C CE2 . PHE B 116 ? 0.4058 0.4169 0.4150 0.0822  -0.0010 -0.0317 116 PHE B CE2 
2346 C CZ  . PHE B 116 ? 0.3757 0.3733 0.3727 0.0874  0.0010  -0.0364 116 PHE B CZ  
2347 N N   . GLU B 117 ? 0.3642 0.3421 0.3980 0.0206  -0.0119 -0.0096 117 GLU B N   
2348 C CA  . GLU B 117 ? 0.3738 0.3402 0.4181 0.0126  -0.0139 -0.0081 117 GLU B CA  
2349 C C   . GLU B 117 ? 0.4040 0.3829 0.4570 0.0041  -0.0119 -0.0085 117 GLU B C   
2350 O O   . GLU B 117 ? 0.3778 0.3464 0.4391 -0.0020 -0.0130 -0.0108 117 GLU B O   
2351 C CB  . GLU B 117 ? 0.3809 0.3348 0.4248 0.0083  -0.0167 -0.0001 117 GLU B CB  
2352 C CG  . GLU B 117 ? 0.4681 0.4335 0.5083 0.0017  -0.0148 0.0082  117 GLU B CG  
2353 C CD  . GLU B 117 ? 0.6328 0.5841 0.6763 -0.0053 -0.0180 0.0186  117 GLU B CD  
2354 O OE1 . GLU B 117 ? 0.6352 0.5812 0.6714 -0.0019 -0.0216 0.0234  117 GLU B OE1 
2355 O OE2 . GLU B 117 ? 0.6696 0.6144 0.7228 -0.0139 -0.0175 0.0218  117 GLU B OE2 
2356 N N   . ARG B 118 ? 0.3606 0.3625 0.4126 0.0027  -0.0088 -0.0071 118 ARG B N   
2357 C CA  . ARG B 118 ? 0.3809 0.3996 0.4423 -0.0066 -0.0073 -0.0083 118 ARG B CA  
2358 C C   . ARG B 118 ? 0.4101 0.4481 0.4732 0.0003  -0.0073 -0.0150 118 ARG B C   
2359 O O   . ARG B 118 ? 0.3441 0.4017 0.4154 -0.0073 -0.0070 -0.0168 118 ARG B O   
2360 C CB  . ARG B 118 ? 0.3824 0.4189 0.4445 -0.0151 -0.0037 -0.0008 118 ARG B CB  
2361 C CG  . ARG B 118 ? 0.5130 0.5297 0.5758 -0.0261 -0.0047 0.0082  118 ARG B CG  
2362 C CD  . ARG B 118 ? 0.6878 0.7212 0.7540 -0.0401 -0.0009 0.0163  118 ARG B CD  
2363 N NE  . ARG B 118 ? 0.7535 0.8003 0.8316 -0.0507 -0.0002 0.0114  118 ARG B NE  
2364 C CZ  . ARG B 118 ? 0.7666 0.8422 0.8504 -0.0610 0.0038  0.0141  118 ARG B CZ  
2365 N NH1 . ARG B 118 ? 0.6786 0.7704 0.7571 -0.0638 0.0085  0.0231  118 ARG B NH1 
2366 N NH2 . ARG B 118 ? 0.7273 0.8174 0.8222 -0.0701 0.0031  0.0077  118 ARG B NH2 
2367 N N   . GLY B 119 ? 0.3229 0.3555 0.3789 0.0137  -0.0082 -0.0183 119 GLY B N   
2368 C CA  . GLY B 119 ? 0.3293 0.3801 0.3859 0.0222  -0.0087 -0.0220 119 GLY B CA  
2369 C C   . GLY B 119 ? 0.4184 0.4740 0.4812 0.0153  -0.0116 -0.0262 119 GLY B C   
2370 O O   . GLY B 119 ? 0.3762 0.4132 0.4403 0.0078  -0.0129 -0.0288 119 GLY B O   
2371 N N   . VAL B 120 ? 0.3666 0.4495 0.4335 0.0185  -0.0127 -0.0276 120 VAL B N   
2372 C CA  . VAL B 120 ? 0.3750 0.4675 0.4448 0.0135  -0.0164 -0.0322 120 VAL B CA  
2373 C C   . VAL B 120 ? 0.3840 0.4966 0.4515 0.0274  -0.0190 -0.0310 120 VAL B C   
2374 O O   . VAL B 120 ? 0.3409 0.4680 0.4097 0.0386  -0.0172 -0.0276 120 VAL B O   
2375 C CB  . VAL B 120 ? 0.3647 0.4761 0.4455 -0.0037 -0.0169 -0.0347 120 VAL B CB  
2376 C CG1 . VAL B 120 ? 0.5181 0.6081 0.6015 -0.0163 -0.0142 -0.0333 120 VAL B CG1 
2377 C CG2 . VAL B 120 ? 0.4490 0.5975 0.5380 -0.0019 -0.0157 -0.0313 120 VAL B CG2 
2378 N N   . ILE B 121 ? 0.3665 0.4805 0.4303 0.0273  -0.0230 -0.0337 121 ILE B N   
2379 C CA  . ILE B 121 ? 0.3451 0.4794 0.4066 0.0399  -0.0269 -0.0307 121 ILE B CA  
2380 C C   . ILE B 121 ? 0.3502 0.5254 0.4235 0.0334  -0.0301 -0.0320 121 ILE B C   
2381 O O   . ILE B 121 ? 0.4055 0.5876 0.4839 0.0162  -0.0313 -0.0377 121 ILE B O   
2382 C CB  . ILE B 121 ? 0.3772 0.4966 0.4272 0.0413  -0.0300 -0.0316 121 ILE B CB  
2383 C CG1 . ILE B 121 ? 0.3996 0.4826 0.4398 0.0479  -0.0267 -0.0295 121 ILE B CG1 
2384 C CG2 . ILE B 121 ? 0.3828 0.5270 0.4299 0.0520  -0.0358 -0.0268 121 ILE B CG2 
2385 C CD1 . ILE B 121 ? 0.4329 0.5009 0.4612 0.0487  -0.0281 -0.0292 121 ILE B CD1 
2386 N N   . LYS B 122 ? 0.3462 0.5491 0.4255 0.0468  -0.0312 -0.0273 122 LYS B N   
2387 C CA  . LYS B 122 ? 0.4638 0.7111 0.5553 0.0420  -0.0359 -0.0279 122 LYS B CA  
2388 C C   . LYS B 122 ? 0.4085 0.6815 0.5035 0.0632  -0.0393 -0.0214 122 LYS B C   
2389 O O   . LYS B 122 ? 0.3861 0.6438 0.4767 0.0812  -0.0361 -0.0172 122 LYS B O   
2390 C CB  . LYS B 122 ? 0.5282 0.7990 0.6346 0.0269  -0.0325 -0.0304 122 LYS B CB  
2391 C CG  . LYS B 122 ? 0.4729 0.7294 0.5804 0.0264  -0.0247 -0.0286 122 LYS B CG  
2392 C CD  . LYS B 122 ? 0.6484 0.9218 0.7676 0.0037  -0.0228 -0.0311 122 LYS B CD  
2393 C CE  . LYS B 122 ? 0.5676 0.8201 0.6826 -0.0143 -0.0265 -0.0376 122 LYS B CE  
2394 N NZ  . LYS B 122 ? 0.7373 0.9934 0.8616 -0.0381 -0.0245 -0.0403 122 LYS B NZ  
2395 N N   . CYS B 123 ? 0.3587 0.6715 0.4621 0.0603  -0.0463 -0.0212 123 CYS B N   
2396 C CA  . CYS B 123 ? 0.4371 0.7788 0.5450 0.0807  -0.0520 -0.0139 123 CYS B CA  
2397 C C   . CYS B 123 ? 0.4012 0.7584 0.5214 0.0977  -0.0464 -0.0108 123 CYS B C   
2398 O O   . CYS B 123 ? 0.4129 0.7602 0.5292 0.1210  -0.0463 -0.0050 123 CYS B O   
2399 C CB  . CYS B 123 ? 0.4868 0.8762 0.6048 0.0707  -0.0609 -0.0153 123 CYS B CB  
2400 S SG  . CYS B 123 ? 0.8574 1.2336 0.9578 0.0547  -0.0682 -0.0199 123 CYS B SG  
2401 N N   . ARG B 124 ? 0.4325 0.8138 0.5672 0.0860  -0.0412 -0.0148 124 ARG B N   
2402 C CA  . ARG B 124 ? 0.4334 0.8348 0.5800 0.1002  -0.0341 -0.0135 124 ARG B CA  
2403 C C   . ARG B 124 ? 0.3508 0.7328 0.4951 0.0863  -0.0244 -0.0175 124 ARG B C   
2404 O O   . ARG B 124 ? 0.3860 0.7948 0.5424 0.0687  -0.0214 -0.0195 124 ARG B O   
2405 C CB  . ARG B 124 ? 0.4416 0.9065 0.6114 0.1020  -0.0372 -0.0122 124 ARG B CB  
2406 C CG  . ARG B 124 ? 0.4058 0.8967 0.5788 0.1120  -0.0491 -0.0073 124 ARG B CG  
2407 C CD  . ARG B 124 ? 0.6018 1.1480 0.7963 0.1231  -0.0502 -0.0043 124 ARG B CD  
2408 N NE  . ARG B 124 ? 0.6367 1.1805 0.8253 0.1444  -0.0572 0.0037  124 ARG B NE  
2409 C CZ  . ARG B 124 ? 0.6669 1.2442 0.8668 0.1531  -0.0596 0.0076  124 ARG B CZ  
2410 N NH1 . ARG B 124 ? 0.5016 1.1188 0.7193 0.1426  -0.0552 0.0039  124 ARG B NH1 
2411 N NH2 . ARG B 124 ? 0.6481 1.2193 0.8417 0.1721  -0.0666 0.0161  124 ARG B NH2 
2412 N N   . PRO B 125 ? 0.3464 0.6827 0.4748 0.0933  -0.0197 -0.0179 125 PRO B N   
2413 C CA  . PRO B 125 ? 0.3503 0.6672 0.4741 0.0809  -0.0117 -0.0203 125 PRO B CA  
2414 C C   . PRO B 125 ? 0.3912 0.7439 0.5276 0.0829  -0.0037 -0.0205 125 PRO B C   
2415 O O   . PRO B 125 ? 0.3515 0.7394 0.4999 0.0993  -0.0028 -0.0200 125 PRO B O   
2416 C CB  . PRO B 125 ? 0.3123 0.5813 0.4178 0.0937  -0.0096 -0.0206 125 PRO B CB  
2417 C CG  . PRO B 125 ? 0.3886 0.6421 0.4869 0.1019  -0.0176 -0.0183 125 PRO B CG  
2418 C CD  . PRO B 125 ? 0.3559 0.6553 0.4688 0.1105  -0.0225 -0.0155 125 PRO B CD  
2419 N N   . SER B 126 ? 0.3190 0.6626 0.4525 0.0664  0.0025  -0.0208 126 SER B N   
2420 C CA  . SER B 126 ? 0.3786 0.7551 0.5213 0.0637  0.0114  -0.0203 126 SER B CA  
2421 C C   . SER B 126 ? 0.3511 0.7033 0.4791 0.0732  0.0194  -0.0217 126 SER B C   
2422 O O   . SER B 126 ? 0.4012 0.7684 0.5300 0.0640  0.0273  -0.0204 126 SER B O   
2423 C CB  . SER B 126 ? 0.3570 0.7476 0.5077 0.0349  0.0127  -0.0178 126 SER B CB  
2424 O OG  . SER B 126 ? 0.5297 0.9480 0.6947 0.0247  0.0057  -0.0185 126 SER B OG  
2425 N N   . ASN B 127 ? 0.2728 0.5881 0.3863 0.0901  0.0174  -0.0242 127 ASN B N   
2426 C CA  . ASN B 127 ? 0.2832 0.5742 0.3811 0.0970  0.0240  -0.0271 127 ASN B CA  
2427 C C   . ASN B 127 ? 0.3642 0.6909 0.4686 0.1101  0.0334  -0.0308 127 ASN B C   
2428 O O   . ASN B 127 ? 0.3052 0.6367 0.4026 0.1037  0.0414  -0.0316 127 ASN B O   
2429 C CB  . ASN B 127 ? 0.2472 0.4945 0.3302 0.1123  0.0200  -0.0301 127 ASN B CB  
2430 C CG  . ASN B 127 ? 0.3483 0.5636 0.4254 0.1007  0.0119  -0.0271 127 ASN B CG  
2431 O OD1 . ASN B 127 ? 0.3584 0.5566 0.4302 0.0835  0.0116  -0.0252 127 ASN B OD1 
2432 N ND2 . ASN B 127 ? 0.3328 0.5420 0.4115 0.1102  0.0055  -0.0262 127 ASN B ND2 
2433 N N   . LEU B 128 ? 0.3359 0.6886 0.4531 0.1298  0.0328  -0.0329 128 LEU B N   
2434 C CA  . LEU B 128 ? 0.3056 0.6921 0.4303 0.1467  0.0426  -0.0381 128 LEU B CA  
2435 C C   . LEU B 128 ? 0.3674 0.8061 0.5079 0.1309  0.0493  -0.0354 128 LEU B C   
2436 O O   . LEU B 128 ? 0.3523 0.8107 0.4908 0.1332  0.0604  -0.0391 128 LEU B O   
2437 C CB  . LEU B 128 ? 0.2998 0.6997 0.4362 0.1738  0.0392  -0.0398 128 LEU B CB  
2438 C CG  . LEU B 128 ? 0.3992 0.8221 0.5412 0.1952  0.0483  -0.0464 128 LEU B CG  
2439 C CD1 . LEU B 128 ? 0.3728 0.7630 0.4936 0.2023  0.0570  -0.0554 128 LEU B CD1 
2440 C CD2 . LEU B 128 ? 0.4391 0.8525 0.5858 0.2150  0.0407  -0.0440 128 LEU B CD2 
2441 N N   . THR B 129 ? 0.2776 0.7403 0.4334 0.1134  0.0433  -0.0295 129 THR B N   
2442 C CA  . THR B 129 ? 0.2803 0.7941 0.4528 0.0962  0.0497  -0.0265 129 THR B CA  
2443 C C   . THR B 129 ? 0.3297 0.8258 0.4885 0.0720  0.0553  -0.0225 129 THR B C   
2444 O O   . THR B 129 ? 0.4061 0.9370 0.5704 0.0630  0.0653  -0.0208 129 THR B O   
2445 C CB  . THR B 129 ? 0.3166 0.8600 0.5089 0.0823  0.0410  -0.0225 129 THR B CB  
2446 O OG1 . THR B 129 ? 0.3059 0.8072 0.4866 0.0632  0.0325  -0.0195 129 THR B OG1 
2447 C CG2 . THR B 129 ? 0.2977 0.8626 0.5035 0.1068  0.0341  -0.0243 129 THR B CG2 
2448 N N   . GLN B 130 ? 0.2743 0.7181 0.4155 0.0621  0.0491  -0.0201 130 GLN B N   
2449 C CA  . GLN B 130 ? 0.3428 0.7646 0.4689 0.0433  0.0532  -0.0151 130 GLN B CA  
2450 C C   . GLN B 130 ? 0.4162 0.8352 0.5266 0.0563  0.0627  -0.0193 130 GLN B C   
2451 O O   . GLN B 130 ? 0.3627 0.8024 0.4696 0.0447  0.0717  -0.0155 130 GLN B O   
2452 C CB  . GLN B 130 ? 0.3522 0.7199 0.4652 0.0345  0.0438  -0.0126 130 GLN B CB  
2453 C CG  . GLN B 130 ? 0.4261 0.7936 0.5502 0.0123  0.0373  -0.0079 130 GLN B CG  
2454 C CD  . GLN B 130 ? 0.4394 0.7554 0.5523 0.0082  0.0285  -0.0078 130 GLN B CD  
2455 O OE1 . GLN B 130 ? 0.3746 0.6551 0.4711 0.0168  0.0279  -0.0087 130 GLN B OE1 
2456 N NE2 . GLN B 130 ? 0.4904 0.8049 0.6127 -0.0048 0.0218  -0.0079 130 GLN B NE2 
2457 N N   . PHE B 131 ? 0.3583 0.7531 0.4585 0.0800  0.0614  -0.0275 131 PHE B N   
2458 C CA  . PHE B 131 ? 0.3800 0.7688 0.4632 0.0923  0.0700  -0.0343 131 PHE B CA  
2459 C C   . PHE B 131 ? 0.3902 0.8336 0.4847 0.1003  0.0826  -0.0384 131 PHE B C   
2460 O O   . PHE B 131 ? 0.4649 0.9180 0.5464 0.0977  0.0924  -0.0405 131 PHE B O   
2461 C CB  . PHE B 131 ? 0.3434 0.6945 0.4150 0.1156  0.0661  -0.0435 131 PHE B CB  
2462 C CG  . PHE B 131 ? 0.4714 0.8098 0.5225 0.1257  0.0740  -0.0525 131 PHE B CG  
2463 C CD1 . PHE B 131 ? 0.4605 0.7768 0.4911 0.1102  0.0743  -0.0496 131 PHE B CD1 
2464 C CD2 . PHE B 131 ? 0.4271 0.7800 0.4800 0.1502  0.0815  -0.0641 131 PHE B CD2 
2465 C CE1 . PHE B 131 ? 0.4992 0.8074 0.5091 0.1179  0.0812  -0.0589 131 PHE B CE1 
2466 C CE2 . PHE B 131 ? 0.5071 0.8492 0.5397 0.1586  0.0895  -0.0750 131 PHE B CE2 
2467 C CZ  . PHE B 131 ? 0.4774 0.7982 0.4876 0.1414  0.0891  -0.0726 131 PHE B CZ  
2468 N N   . ALA B 132 ? 0.3443 0.8265 0.4630 0.1105  0.0825  -0.0397 132 ALA B N   
2469 C CA  . ALA B 132 ? 0.3279 0.8675 0.4611 0.1195  0.0949  -0.0441 132 ALA B CA  
2470 C C   . ALA B 132 ? 0.3640 0.9371 0.4998 0.0924  0.1029  -0.0358 132 ALA B C   
2471 O O   . ALA B 132 ? 0.3753 0.9748 0.5073 0.0937  0.1142  -0.0387 132 ALA B O   
2472 C CB  . ALA B 132 ? 0.3267 0.8935 0.4842 0.1317  0.0890  -0.0442 132 ALA B CB  
2473 N N   . VAL B 133 ? 0.3423 0.9054 0.4816 0.0658  0.0955  -0.0248 133 VAL B N   
2474 C CA  . VAL B 133 ? 0.3814 0.9687 0.5214 0.0380  0.1025  -0.0148 133 VAL B CA  
2475 C C   . VAL B 133 ? 0.3808 0.9430 0.4922 0.0332  0.1089  -0.0131 133 VAL B C   
2476 O O   . VAL B 133 ? 0.4571 1.0532 0.5650 0.0247  0.1211  -0.0102 133 VAL B O   
2477 C CB  . VAL B 133 ? 0.4062 0.9791 0.5547 0.0112  0.0924  -0.0045 133 VAL B CB  
2478 C CG1 . VAL B 133 ? 0.3876 0.9643 0.5290 -0.0182 0.0983  0.0077  133 VAL B CG1 
2479 C CG2 . VAL B 133 ? 0.3489 0.9650 0.5273 0.0108  0.0884  -0.0059 133 VAL B CG2 
2480 N N   . TYR B 134 ? 0.3808 0.8862 0.4709 0.0384  0.1009  -0.0147 134 TYR B N   
2481 C CA  . TYR B 134 ? 0.3715 0.8544 0.4335 0.0356  0.1053  -0.0140 134 TYR B CA  
2482 C C   . TYR B 134 ? 0.4716 0.9813 0.5262 0.0563  0.1178  -0.0270 134 TYR B C   
2483 O O   . TYR B 134 ? 0.4622 0.9951 0.5041 0.0484  0.1288  -0.0250 134 TYR B O   
2484 C CB  . TYR B 134 ? 0.4305 0.8520 0.4748 0.0397  0.0936  -0.0152 134 TYR B CB  
2485 C CG  . TYR B 134 ? 0.3954 0.7952 0.4107 0.0444  0.0968  -0.0194 134 TYR B CG  
2486 C CD1 . TYR B 134 ? 0.4686 0.8574 0.4667 0.0246  0.0966  -0.0075 134 TYR B CD1 
2487 C CD2 . TYR B 134 ? 0.4830 0.8718 0.4878 0.0684  0.0993  -0.0352 134 TYR B CD2 
2488 C CE1 . TYR B 134 ? 0.4679 0.8401 0.4381 0.0281  0.0984  -0.0113 134 TYR B CE1 
2489 C CE2 . TYR B 134 ? 0.4769 0.8467 0.4537 0.0710  0.1018  -0.0409 134 TYR B CE2 
2490 C CZ  . TYR B 134 ? 0.5224 0.8858 0.4820 0.0506  0.1008  -0.0289 134 TYR B CZ  
2491 O OH  . TYR B 134 ? 0.5459 0.8940 0.4771 0.0525  0.1020  -0.0345 134 TYR B OH  
2492 N N   . LEU B 135 ? 0.3817 0.8893 0.4441 0.0832  0.1168  -0.0402 135 LEU B N   
2493 C CA  . LEU B 135 ? 0.4704 0.9981 0.5268 0.1064  0.1286  -0.0552 135 LEU B CA  
2494 C C   . LEU B 135 ? 0.5177 1.0959 0.5847 0.0989  0.1392  -0.0528 135 LEU B C   
2495 O O   . LEU B 135 ? 0.5323 1.1176 0.5822 0.0991  0.1483  -0.0577 135 LEU B O   
2496 C CB  . LEU B 135 ? 0.4566 0.9703 0.5253 0.1345  0.1231  -0.0660 135 LEU B CB  
2497 C CG  . LEU B 135 ? 0.6171 1.1181 0.6752 0.1574  0.1282  -0.0811 135 LEU B CG  
2498 C CD1 . LEU B 135 ? 0.5984 1.0554 0.6252 0.1607  0.1285  -0.0898 135 LEU B CD1 
2499 C CD2 . LEU B 135 ? 0.6062 1.0969 0.6815 0.1801  0.1214  -0.0856 135 LEU B CD2 
2500 N N   . ASN B 136 ? 0.4619 1.0728 0.5561 0.0903  0.1367  -0.0453 136 ASN B N   
2501 C CA  . ASN B 136 ? 0.4529 1.1094 0.5579 0.0807  0.1452  -0.0421 136 ASN B CA  
2502 C C   . ASN B 136 ? 0.4894 1.1551 0.5791 0.0524  0.1520  -0.0301 136 ASN B C   
2503 O O   . ASN B 136 ? 0.5117 1.2049 0.5970 0.0477  0.1618  -0.0303 136 ASN B O   
2504 C CB  . ASN B 136 ? 0.3928 1.0802 0.5289 0.0756  0.1393  -0.0366 136 ASN B CB  
2505 C CG  . ASN B 136 ? 0.4482 1.1830 0.5988 0.0759  0.1473  -0.0381 136 ASN B CG  
2506 O OD1 . ASN B 136 ? 0.4265 1.1679 0.5732 0.0966  0.1542  -0.0492 136 ASN B OD1 
2507 N ND2 . ASN B 136 ? 0.4535 1.2209 0.6216 0.0529  0.1465  -0.0275 136 ASN B ND2 
2508 N N   . SER B 137 ? 0.4902 1.1323 0.5714 0.0335  0.1468  -0.0188 137 SER B N   
2509 C CA  . SER B 137 ? 0.5428 1.1872 0.6082 0.0058  0.1515  -0.0041 137 SER B CA  
2510 C C   . SER B 137 ? 0.5496 1.1822 0.5829 0.0117  0.1587  -0.0091 137 SER B C   
2511 O O   . SER B 137 ? 0.6002 1.2490 0.6215 -0.0051 0.1657  -0.0002 137 SER B O   
2512 C CB  . SER B 137 ? 0.5927 1.2009 0.6555 -0.0138 0.1409  0.0094  137 SER B CB  
2513 O OG  . SER B 137 ? 0.7027 1.3066 0.7495 -0.0402 0.1440  0.0260  137 SER B OG  
2514 N N   . ARG B 138 ? 0.5756 1.1791 0.5940 0.0347  0.1565  -0.0235 138 ARG B N   
2515 C CA  . ARG B 138 ? 0.6280 1.2166 0.6139 0.0393  0.1615  -0.0301 138 ARG B CA  
2516 C C   . ARG B 138 ? 0.6277 1.2358 0.6134 0.0585  0.1704  -0.0466 138 ARG B C   
2517 O O   . ARG B 138 ? 0.5983 1.2155 0.5631 0.0536  0.1782  -0.0482 138 ARG B O   
2518 C CB  . ARG B 138 ? 0.5672 1.1063 0.5342 0.0510  0.1526  -0.0375 138 ARG B CB  
2519 C CG  . ARG B 138 ? 0.5418 1.0375 0.5043 0.0307  0.1375  -0.0204 138 ARG B CG  
2520 C CD  . ARG B 138 ? 0.6462 1.1469 0.5896 0.0052  0.1399  -0.0027 138 ARG B CD  
2521 N NE  . ARG B 138 ? 0.6324 1.1003 0.5820 -0.0140 0.1270  0.0152  138 ARG B NE  
2522 N N   . LEU B 139 ? 0.5556 1.1710 0.5646 0.0799  0.1693  -0.0578 139 LEU B N   
2523 C CA  . LEU B 139 ? 0.5538 1.1827 0.5643 0.1009  0.1773  -0.0740 139 LEU B CA  
2524 C C   . LEU B 139 ? 0.5956 1.2761 0.6308 0.0968  0.1845  -0.0701 139 LEU B C   
2525 O O   . LEU B 139 ? 0.6522 1.3517 0.6898 0.1119  0.1932  -0.0820 139 LEU B O   
2526 C CB  . LEU B 139 ? 0.5115 1.1093 0.5296 0.1288  0.1707  -0.0881 139 LEU B CB  
2527 C CG  . LEU B 139 ? 0.5371 1.0825 0.5289 0.1346  0.1645  -0.0951 139 LEU B CG  
2528 C CD1 . LEU B 139 ? 0.6839 1.1970 0.6782 0.1625  0.1611  -0.1114 139 LEU B CD1 
2529 C CD2 . LEU B 139 ? 0.6209 1.1619 0.5798 0.1236  0.1711  -0.0977 139 LEU B CD2 
2530 N N   . ARG B 140 ? 0.5882 1.2908 0.6409 0.0754  0.1811  -0.0539 140 ARG B N   
2531 C CA  . ARG B 140 ? 0.5851 1.3367 0.6634 0.0671  0.1857  -0.0483 140 ARG B CA  
2532 C C   . ARG B 140 ? 0.5716 1.3416 0.6692 0.0949  0.1882  -0.0627 140 ARG B C   
2533 O O   . ARG B 140 ? 0.5571 1.3619 0.6599 0.0996  0.1987  -0.0681 140 ARG B O   
2534 C CB  . ARG B 140 ? 0.5943 1.3736 0.6601 0.0457  0.1965  -0.0399 140 ARG B CB  
2535 C CG  . ARG B 140 ? 0.7409 1.5078 0.7976 0.0143  0.1920  -0.0200 140 ARG B CG  
2536 C CD  . ARG B 140 ? 0.7133 1.5062 0.7591 -0.0088 0.2014  -0.0084 140 ARG B CD  
2537 N NE  . ARG B 140 ? 0.6479 1.4871 0.7099 -0.0007 0.2113  -0.0162 140 ARG B NE  
2538 C CZ  . ARG B 140 ? 0.7150 1.5900 0.7798 -0.0205 0.2196  -0.0063 140 ARG B CZ  
2539 N NH1 . ARG B 140 ? 0.8455 1.7132 0.8991 -0.0502 0.2185  0.0129  140 ARG B NH1 
2540 N NH2 . ARG B 140 ? 0.7632 1.6819 0.8441 -0.0105 0.2289  -0.0150 140 ARG B NH2 
2541 N N   . LEU B 141 ? 0.5445 1.2891 0.6522 0.1137  0.1783  -0.0684 141 LEU B N   
2542 C CA  . LEU B 141 ? 0.5747 1.3245 0.6973 0.1429  0.1788  -0.0812 141 LEU B CA  
2543 C C   . LEU B 141 ? 0.6332 1.4344 0.7869 0.1417  0.1800  -0.0769 141 LEU B C   
2544 O O   . LEU B 141 ? 0.5635 1.3855 0.7288 0.1619  0.1859  -0.0866 141 LEU B O   
2545 C CB  . LEU B 141 ? 0.6392 1.3454 0.7632 0.1602  0.1664  -0.0848 141 LEU B CB  
2546 C CG  . LEU B 141 ? 0.6037 1.2571 0.7004 0.1735  0.1657  -0.0957 141 LEU B CG  
2547 C CD1 . LEU B 141 ? 0.5637 1.1756 0.6640 0.1860  0.1523  -0.0956 141 LEU B CD1 
2548 C CD2 . LEU B 141 ? 0.7051 1.3560 0.7906 0.1922  0.1765  -0.1118 141 LEU B CD2 
2549 N N   . MET B 142 ? 0.5475 1.3694 0.7150 0.1176  0.1746  -0.0628 142 MET B N   
2550 C CA  . MET B 142 ? 0.4487 1.3138 0.6468 0.1152  0.1716  -0.0583 142 MET B CA  
2551 C C   . MET B 142 ? 0.4799 1.3607 0.6838 0.0805  0.1683  -0.0429 142 MET B C   
2552 O O   . MET B 142 ? 0.5741 1.4253 0.7609 0.0628  0.1658  -0.0355 142 MET B O   
2553 C CB  . MET B 142 ? 0.5079 1.3568 0.7208 0.1377  0.1595  -0.0621 142 MET B CB  
2554 C CG  . MET B 142 ? 0.4946 1.3209 0.7105 0.1237  0.1456  -0.0525 142 MET B CG  
2555 S SD  . MET B 142 ? 0.5604 1.3658 0.7896 0.1506  0.1313  -0.0560 142 MET B SD  
2556 C CE  . MET B 142 ? 0.5002 1.2496 0.7042 0.1775  0.1340  -0.0682 142 MET B CE  
2557 N N   . LYS B 143 ? 0.4854 1.4117 0.7136 0.0703  0.1683  -0.0380 143 LYS B N   
2558 C CA  . LYS B 143 ? 0.5589 1.4962 0.7925 0.0357  0.1651  -0.0240 143 LYS B CA  
2559 C C   . LYS B 143 ? 0.4916 1.4056 0.7340 0.0309  0.1499  -0.0198 143 LYS B C   
2560 O O   . LYS B 143 ? 0.5194 1.4268 0.7717 0.0536  0.1417  -0.0263 143 LYS B O   
2561 C CB  . LYS B 143 ? 0.5679 1.5618 0.8227 0.0223  0.1709  -0.0202 143 LYS B CB  
2562 C CG  . LYS B 143 ? 0.6731 1.6742 0.9246 -0.0168 0.1731  -0.0057 143 LYS B CG  
2563 C CD  . LYS B 143 ? 0.6608 1.6151 0.8830 -0.0300 0.1741  0.0011  143 LYS B CD  
2564 C CE  . LYS B 143 ? 0.7084 1.6662 0.9246 -0.0671 0.1777  0.0168  143 LYS B CE  
2565 N NZ  . LYS B 143 ? 0.5900 1.5871 0.8039 -0.0739 0.1917  0.0186  143 LYS B NZ  
2566 N N   . ASN B 144 ? 0.5411 1.4403 0.7786 0.0007  0.1462  -0.0085 144 ASN B N   
2567 C CA  . ASN B 144 ? 0.5330 1.4079 0.7767 -0.0085 0.1326  -0.0045 144 ASN B CA  
2568 C C   . ASN B 144 ? 0.4968 1.3963 0.7647 0.0030  0.1231  -0.0087 144 ASN B C   
2569 O O   . ASN B 144 ? 0.5200 1.3967 0.7890 0.0198  0.1131  -0.0129 144 ASN B O   
2570 C CB  . ASN B 144 ? 0.5781 1.4470 0.8199 -0.0465 0.1317  0.0085  144 ASN B CB  
2571 C CG  . ASN B 144 ? 0.7305 1.5500 0.9592 -0.0557 0.1242  0.0129  144 ASN B CG  
2572 O OD1 . ASN B 144 ? 0.7985 1.5901 1.0192 -0.0343 0.1198  0.0063  144 ASN B OD1 
2573 N ND2 . ASN B 144 ? 0.7680 1.5746 0.9947 -0.0879 0.1227  0.0243  144 ASN B ND2 
2574 N N   . GLU B 145 ? 0.4519 1.3989 0.7387 -0.0067 0.1259  -0.0069 145 GLU B N   
2575 C CA  . GLU B 145 ? 0.5277 1.5026 0.8376 0.0010  0.1163  -0.0094 145 GLU B CA  
2576 C C   . GLU B 145 ? 0.4748 1.4436 0.7871 0.0392  0.1127  -0.0185 145 GLU B C   
2577 O O   . GLU B 145 ? 0.4676 1.4318 0.7889 0.0484  0.1004  -0.0193 145 GLU B O   
2578 C CB  . GLU B 145 ? 0.4892 1.5203 0.8187 -0.0125 0.1220  -0.0070 145 GLU B CB  
2579 C CG  . GLU B 145 ? 0.5926 1.6318 0.9279 -0.0522 0.1193  0.0023  145 GLU B CG  
2580 C CD  . GLU B 145 ? 0.7759 1.7769 1.1074 -0.0669 0.1058  0.0051  145 GLU B CD  
2581 O OE1 . GLU B 145 ? 0.7242 1.7138 1.0594 -0.0487 0.0950  0.0001  145 GLU B OE1 
2582 O OE2 . GLU B 145 ? 0.7802 1.7639 1.1059 -0.0980 0.1059  0.0126  145 GLU B OE2 
2583 N N   . GLU B 146 ? 0.4591 1.4250 0.7621 0.0613  0.1230  -0.0252 146 GLU B N   
2584 C CA  . GLU B 146 ? 0.4777 1.4294 0.7814 0.0973  0.1197  -0.0337 146 GLU B CA  
2585 C C   . GLU B 146 ? 0.4577 1.3536 0.7448 0.1051  0.1106  -0.0342 146 GLU B C   
2586 O O   . GLU B 146 ? 0.4392 1.3228 0.7322 0.1222  0.0999  -0.0353 146 GLU B O   
2587 C CB  . GLU B 146 ? 0.4661 1.4239 0.7626 0.1178  0.1334  -0.0425 146 GLU B CB  
2588 C CG  . GLU B 146 ? 0.5049 1.4410 0.8010 0.1549  0.1307  -0.0516 146 GLU B CG  
2589 C CD  . GLU B 146 ? 0.6710 1.6375 0.9927 0.1703  0.1224  -0.0508 146 GLU B CD  
2590 O OE1 . GLU B 146 ? 0.6304 1.6455 0.9722 0.1553  0.1217  -0.0459 146 GLU B OE1 
2591 O OE2 . GLU B 146 ? 0.6622 1.6027 0.9834 0.1968  0.1159  -0.0543 146 GLU B OE2 
2592 N N   . LEU B 147 ? 0.4853 1.3479 0.7513 0.0922  0.1145  -0.0325 147 LEU B N   
2593 C CA  . LEU B 147 ? 0.4510 1.2627 0.7020 0.0975  0.1064  -0.0328 147 LEU B CA  
2594 C C   . LEU B 147 ? 0.4702 1.2793 0.7323 0.0846  0.0925  -0.0267 147 LEU B C   
2595 O O   . LEU B 147 ? 0.4352 1.2171 0.6949 0.1002  0.0826  -0.0284 147 LEU B O   
2596 C CB  . LEU B 147 ? 0.4389 1.2226 0.6674 0.0821  0.1133  -0.0306 147 LEU B CB  
2597 C CG  . LEU B 147 ? 0.4164 1.1501 0.6301 0.0845  0.1056  -0.0303 147 LEU B CG  
2598 C CD1 . LEU B 147 ? 0.4103 1.1134 0.6147 0.1177  0.1038  -0.0401 147 LEU B CD1 
2599 C CD2 . LEU B 147 ? 0.3982 1.1112 0.5921 0.0645  0.1120  -0.0255 147 LEU B CD2 
2600 N N   . LYS B 148 ? 0.4904 1.3260 0.7636 0.0552  0.0914  -0.0199 148 LYS B N   
2601 C CA  . LYS B 148 ? 0.5045 1.3379 0.7872 0.0400  0.0784  -0.0158 148 LYS B CA  
2602 C C   . LYS B 148 ? 0.4436 1.2974 0.7414 0.0600  0.0691  -0.0185 148 LYS B C   
2603 O O   . LYS B 148 ? 0.3793 1.2158 0.6773 0.0624  0.0569  -0.0178 148 LYS B O   
2604 C CB  . LYS B 148 ? 0.5089 1.3661 0.8003 0.0042  0.0801  -0.0092 148 LYS B CB  
2605 C CG  . LYS B 148 ? 0.5297 1.3537 0.8063 -0.0214 0.0828  -0.0033 148 LYS B CG  
2606 C CD  . LYS B 148 ? 0.6704 1.5180 0.9509 -0.0509 0.0909  0.0038  148 LYS B CD  
2607 C CE  . LYS B 148 ? 0.6582 1.5343 0.9579 -0.0711 0.0836  0.0056  148 LYS B CE  
2608 N NZ  . LYS B 148 ? 0.7812 1.6292 1.0814 -0.0818 0.0704  0.0049  148 LYS B NZ  
2609 N N   . LYS B 149 ? 0.4576 1.3486 0.7677 0.0748  0.0747  -0.0212 149 LYS B N   
2610 C CA  . LYS B 149 ? 0.4239 1.3334 0.7479 0.0975  0.0665  -0.0228 149 LYS B CA  
2611 C C   . LYS B 149 ? 0.4122 1.2784 0.7234 0.1273  0.0620  -0.0261 149 LYS B C   
2612 O O   . LYS B 149 ? 0.4158 1.2732 0.7298 0.1369  0.0499  -0.0239 149 LYS B O   
2613 C CB  . LYS B 149 ? 0.3612 1.3198 0.7020 0.1073  0.0751  -0.0252 149 LYS B CB  
2614 C CG  . LYS B 149 ? 0.3742 1.3539 0.7306 0.1340  0.0683  -0.0264 149 LYS B CG  
2615 C CD  . LYS B 149 ? 0.3987 1.4135 0.7675 0.1530  0.0795  -0.0313 149 LYS B CD  
2616 C CE  . LYS B 149 ? 0.4071 1.4702 0.7880 0.1287  0.0888  -0.0299 149 LYS B CE  
2617 N NZ  . LYS B 149 ? 0.4330 1.5402 0.8311 0.1475  0.0984  -0.0346 149 LYS B NZ  
2618 N N   . LEU B 150 ? 0.3555 1.1928 0.6508 0.1409  0.0714  -0.0311 150 LEU B N   
2619 C CA  . LEU B 150 ? 0.3826 1.1738 0.6641 0.1674  0.0677  -0.0347 150 LEU B CA  
2620 C C   . LEU B 150 ? 0.4491 1.2013 0.7190 0.1585  0.0570  -0.0309 150 LEU B C   
2621 O O   . LEU B 150 ? 0.4276 1.1545 0.6938 0.1759  0.0478  -0.0299 150 LEU B O   
2622 C CB  . LEU B 150 ? 0.4589 1.2258 0.7237 0.1787  0.0802  -0.0422 150 LEU B CB  
2623 C CG  . LEU B 150 ? 0.4743 1.2709 0.7473 0.1945  0.0917  -0.0488 150 LEU B CG  
2624 C CD1 . LEU B 150 ? 0.5088 1.2661 0.7619 0.2137  0.1000  -0.0583 150 LEU B CD1 
2625 C CD2 . LEU B 150 ? 0.3989 1.2234 0.6930 0.2138  0.0857  -0.0478 150 LEU B CD2 
2626 N N   . LEU B 151 ? 0.4241 1.1698 0.6878 0.1315  0.0584  -0.0283 151 LEU B N   
2627 C CA  . LEU B 151 ? 0.3822 1.0923 0.6362 0.1222  0.0493  -0.0256 151 LEU B CA  
2628 C C   . LEU B 151 ? 0.4145 1.1414 0.6808 0.1139  0.0360  -0.0213 151 LEU B C   
2629 O O   . LEU B 151 ? 0.3904 1.0890 0.6495 0.1191  0.0261  -0.0200 151 LEU B O   
2630 C CB  . LEU B 151 ? 0.4171 1.1173 0.6631 0.0952  0.0550  -0.0236 151 LEU B CB  
2631 C CG  . LEU B 151 ? 0.3584 1.0378 0.5875 0.1038  0.0671  -0.0277 151 LEU B CG  
2632 C CD1 . LEU B 151 ? 0.3682 1.0343 0.5879 0.0776  0.0714  -0.0236 151 LEU B CD1 
2633 C CD2 . LEU B 151 ? 0.3677 1.0041 0.5824 0.1321  0.0642  -0.0331 151 LEU B CD2 
2634 N N   . ARG B 152 ? 0.3717 1.1445 0.6553 0.0999  0.0356  -0.0193 152 ARG B N   
2635 C CA  . ARG B 152 ? 0.4765 1.2680 0.7706 0.0922  0.0228  -0.0164 152 ARG B CA  
2636 C C   . ARG B 152 ? 0.4118 1.1969 0.7061 0.1220  0.0147  -0.0155 152 ARG B C   
2637 O O   . ARG B 152 ? 0.4160 1.1888 0.7066 0.1216  0.0029  -0.0129 152 ARG B O   
2638 C CB  . ARG B 152 ? 0.4815 1.3257 0.7948 0.0742  0.0244  -0.0152 152 ARG B CB  
2639 C CG  . ARG B 152 ? 0.4507 1.2994 0.7659 0.0368  0.0233  -0.0137 152 ARG B CG  
2640 C CD  . ARG B 152 ? 0.5760 1.4750 0.9088 0.0203  0.0277  -0.0126 152 ARG B CD  
2641 N NE  . ARG B 152 ? 0.6510 1.5490 0.9811 -0.0044 0.0385  -0.0107 152 ARG B NE  
2642 C CZ  . ARG B 152 ? 0.5951 1.5273 0.9340 -0.0088 0.0491  -0.0096 152 ARG B CZ  
2643 N NH1 . ARG B 152 ? 0.4388 1.4117 0.7924 0.0093  0.0505  -0.0112 152 ARG B NH1 
2644 N NH2 . ARG B 152 ? 0.6573 1.5828 0.9902 -0.0319 0.0585  -0.0062 152 ARG B NH2 
2645 N N   . GLU B 153 ? 0.4137 1.2051 0.7111 0.1476  0.0211  -0.0174 153 GLU B N   
2646 C CA  . GLU B 153 ? 0.3652 1.1490 0.6638 0.1761  0.0139  -0.0152 153 GLU B CA  
2647 C C   . GLU B 153 ? 0.4450 1.1714 0.7232 0.1889  0.0094  -0.0145 153 GLU B C   
2648 O O   . GLU B 153 ? 0.4402 1.1548 0.7155 0.1980  -0.0018 -0.0095 153 GLU B O   
2649 C CB  . GLU B 153 ? 0.4760 1.2783 0.7840 0.1995  0.0229  -0.0185 153 GLU B CB  
2650 C CG  . GLU B 153 ? 0.5573 1.3852 0.8803 0.2194  0.0151  -0.0144 153 GLU B CG  
2651 C CD  . GLU B 153 ? 0.6419 1.5248 0.9842 0.2009  0.0092  -0.0110 153 GLU B CD  
2652 O OE1 . GLU B 153 ? 0.7348 1.6560 1.0896 0.1877  0.0177  -0.0139 153 GLU B OE1 
2653 O OE2 . GLU B 153 ? 0.6357 1.5227 0.9792 0.1979  -0.0038 -0.0056 153 GLU B OE2 
2654 N N   . TYR B 154 ? 0.4238 1.1149 0.6870 0.1888  0.0178  -0.0190 154 TYR B N   
2655 C CA  . TYR B 154 ? 0.3813 1.0171 0.6248 0.1987  0.0138  -0.0186 154 TYR B CA  
2656 C C   . TYR B 154 ? 0.4344 1.0602 0.6735 0.1821  0.0023  -0.0141 154 TYR B C   
2657 O O   . TYR B 154 ? 0.4283 1.0253 0.6577 0.1938  -0.0062 -0.0102 154 TYR B O   
2658 C CB  . TYR B 154 ? 0.3979 1.0027 0.6265 0.1969  0.0246  -0.0248 154 TYR B CB  
2659 C CG  . TYR B 154 ? 0.3927 0.9429 0.6017 0.2006  0.0203  -0.0246 154 TYR B CG  
2660 C CD1 . TYR B 154 ? 0.3915 0.9037 0.5899 0.2238  0.0166  -0.0238 154 TYR B CD1 
2661 C CD2 . TYR B 154 ? 0.3737 0.9100 0.5756 0.1800  0.0195  -0.0246 154 TYR B CD2 
2662 C CE1 . TYR B 154 ? 0.3830 0.8450 0.5631 0.2256  0.0126  -0.0231 154 TYR B CE1 
2663 C CE2 . TYR B 154 ? 0.3399 0.8288 0.5251 0.1837  0.0154  -0.0245 154 TYR B CE2 
2664 C CZ  . TYR B 154 ? 0.3876 0.8392 0.5612 0.2061  0.0120  -0.0237 154 TYR B CZ  
2665 O OH  . TYR B 154 ? 0.3749 0.7782 0.5311 0.2079  0.0082  -0.0233 154 TYR B OH  
2666 N N   . LYS B 155 ? 0.3914 1.0384 0.6365 0.1539  0.0024  -0.0146 155 LYS B N   
2667 C CA  . LYS B 155 ? 0.3524 0.9894 0.5933 0.1363  -0.0079 -0.0125 155 LYS B CA  
2668 C C   . LYS B 155 ? 0.5118 1.1699 0.7589 0.1402  -0.0202 -0.0079 155 LYS B C   
2669 O O   . LYS B 155 ? 0.4289 1.0673 0.6663 0.1379  -0.0299 -0.0055 155 LYS B O   
2670 C CB  . LYS B 155 ? 0.3683 1.0222 0.6156 0.1036  -0.0047 -0.0147 155 LYS B CB  
2671 C CG  . LYS B 155 ? 0.3998 1.0209 0.6361 0.0952  0.0026  -0.0172 155 LYS B CG  
2672 C CD  . LYS B 155 ? 0.5473 1.1226 0.7676 0.1067  -0.0034 -0.0172 155 LYS B CD  
2673 C CE  . LYS B 155 ? 0.4655 1.0030 0.6718 0.0791  -0.0058 -0.0182 155 LYS B CE  
2674 N NZ  . LYS B 155 ? 0.4889 1.0154 0.6908 0.0630  0.0050  -0.0189 155 LYS B NZ  
2675 N N   . LYS B 156 ? 0.3656 1.0655 0.6285 0.1458  -0.0199 -0.0064 156 LYS B N   
2676 C CA  . LYS B 156 ? 0.4513 1.1745 0.7204 0.1513  -0.0317 -0.0013 156 LYS B CA  
2677 C C   . LYS B 156 ? 0.4938 1.1846 0.7513 0.1793  -0.0373 0.0043  156 LYS B C   
2678 O O   . LYS B 156 ? 0.5259 1.2051 0.7743 0.1781  -0.0481 0.0089  156 LYS B O   
2679 C CB  . LYS B 156 ? 0.4281 1.2046 0.7183 0.1529  -0.0297 -0.0009 156 LYS B CB  
2680 C CG  . LYS B 156 ? 0.4995 1.3153 0.8006 0.1244  -0.0357 -0.0019 156 LYS B CG  
2681 C CD  . LYS B 156 ? 0.5429 1.4122 0.8645 0.1305  -0.0380 0.0004  156 LYS B CD  
2682 C CE  . LYS B 156 ? 0.5548 1.4500 0.8903 0.1331  -0.0248 -0.0027 156 LYS B CE  
2683 N NZ  . LYS B 156 ? 0.4744 1.4256 0.8298 0.1147  -0.0258 -0.0033 156 LYS B NZ  
2684 N N   . GLY B 157 ? 0.4897 1.1650 0.7467 0.2036  -0.0299 0.0039  157 GLY B N   
2685 C CA  . GLY B 157 ? 0.4871 1.1282 0.7338 0.2295  -0.0344 0.0097  157 GLY B CA  
2686 C C   . GLY B 157 ? 0.5177 1.1025 0.7421 0.2294  -0.0353 0.0100  157 GLY B C   
2687 O O   . GLY B 157 ? 0.5035 1.0678 0.7169 0.2335  -0.0448 0.0169  157 GLY B O   
2688 N N   . PHE B 158 ? 0.4238 0.9840 0.6407 0.2250  -0.0251 0.0028  158 PHE B N   
2689 C CA  . PHE B 158 ? 0.4738 0.9838 0.6709 0.2217  -0.0248 0.0017  158 PHE B CA  
2690 C C   . PHE B 158 ? 0.5193 0.9838 0.7015 0.2426  -0.0290 0.0074  158 PHE B C   
2691 O O   . PHE B 158 ? 0.6437 1.0712 0.8097 0.2388  -0.0329 0.0097  158 PHE B O   
2692 C CB  . PHE B 158 ? 0.4147 0.9307 0.6091 0.1972  -0.0318 0.0021  158 PHE B CB  
2693 C CG  . PHE B 158 ? 0.4589 0.9367 0.6396 0.1882  -0.0277 -0.0023 158 PHE B CG  
2694 C CD1 . PHE B 158 ? 0.4508 0.9342 0.6356 0.1767  -0.0177 -0.0091 158 PHE B CD1 
2695 C CD2 . PHE B 158 ? 0.5062 0.9444 0.6701 0.1908  -0.0340 0.0010  158 PHE B CD2 
2696 C CE1 . PHE B 158 ? 0.4127 0.8585 0.5838 0.1675  -0.0142 -0.0126 158 PHE B CE1 
2697 C CE2 . PHE B 158 ? 0.5021 0.9015 0.6522 0.1809  -0.0301 -0.0032 158 PHE B CE2 
2698 C CZ  . PHE B 158 ? 0.4566 0.8542 0.6080 0.1673  -0.0202 -0.0100 158 PHE B CZ  
2699 N N   . ASP B 159 ? 0.5375 1.0025 0.7252 0.2643  -0.0277 0.0098  159 ASP B N   
2700 C CA  . ASP B 159 ? 0.5195 0.9360 0.6936 0.2834  -0.0296 0.0145  159 ASP B CA  
2701 C C   . ASP B 159 ? 0.6034 0.9957 0.7754 0.2972  -0.0180 0.0059  159 ASP B C   
2702 O O   . ASP B 159 ? 0.5639 0.9799 0.7441 0.2926  -0.0088 -0.0029 159 ASP B O   
2703 C CB  . ASP B 159 ? 0.5711 1.0028 0.7524 0.2978  -0.0394 0.0256  159 ASP B CB  
2704 C CG  . ASP B 159 ? 0.5925 1.0746 0.7969 0.3069  -0.0376 0.0244  159 ASP B CG  
2705 O OD1 . ASP B 159 ? 0.5187 1.0173 0.7321 0.3061  -0.0271 0.0148  159 ASP B OD1 
2706 O OD2 . ASP B 159 ? 0.7029 1.2095 0.9164 0.3151  -0.0468 0.0335  159 ASP B OD2 
2707 N N   . ASP B 160 ? 0.5708 0.9151 0.7308 0.3128  -0.0184 0.0084  160 ASP B N   
2708 C CA  . ASP B 160 ? 0.6771 0.9938 0.8335 0.3255  -0.0081 -0.0010 160 ASP B CA  
2709 C C   . ASP B 160 ? 0.6682 1.0279 0.8449 0.3370  -0.0016 -0.0064 160 ASP B C   
2710 O O   . ASP B 160 ? 0.6163 0.9785 0.7932 0.3370  0.0095  -0.0178 160 ASP B O   
2711 C CB  . ASP B 160 ? 0.7036 0.9680 0.8488 0.3408  -0.0111 0.0041  160 ASP B CB  
2712 C CG  . ASP B 160 ? 0.9254 1.1544 1.0527 0.3300  -0.0190 0.0126  160 ASP B CG  
2713 O OD1 . ASP B 160 ? 0.9305 1.1852 1.0602 0.3203  -0.0275 0.0209  160 ASP B OD1 
2714 O OD2 . ASP B 160 ? 1.1631 1.3400 1.2742 0.3301  -0.0166 0.0105  160 ASP B OD2 
2715 N N   . GLU B 161 ? 0.6402 1.0356 0.8339 0.3469  -0.0083 0.0017  161 GLU B N   
2716 C CA  . GLU B 161 ? 0.5691 1.0096 0.7843 0.3581  -0.0024 -0.0029 161 GLU B CA  
2717 C C   . GLU B 161 ? 0.5217 1.0048 0.7444 0.3394  0.0049  -0.0106 161 GLU B C   
2718 O O   . GLU B 161 ? 0.5886 1.0842 0.8167 0.3439  0.0162  -0.0205 161 GLU B O   
2719 C CB  . GLU B 161 ? 0.6255 1.1026 0.8584 0.3688  -0.0125 0.0081  161 GLU B CB  
2720 C CG  . GLU B 161 ? 0.5702 1.0992 0.8272 0.3786  -0.0062 0.0030  161 GLU B CG  
2721 C CD  . GLU B 161 ? 0.6607 1.1966 0.9329 0.4051  -0.0106 0.0092  161 GLU B CD  
2722 O OE1 . GLU B 161 ? 0.7827 1.2718 1.0475 0.4232  -0.0086 0.0087  161 GLU B OE1 
2723 O OE2 . GLU B 161 ? 0.6611 1.2501 0.9536 0.4075  -0.0157 0.0144  161 GLU B OE2 
2724 N N   . SER B 162 ? 0.4367 0.9443 0.6605 0.3180  -0.0015 -0.0060 162 SER B N   
2725 C CA  . SER B 162 ? 0.5278 1.0717 0.7582 0.2973  0.0052  -0.0122 162 SER B CA  
2726 C C   . SER B 162 ? 0.5020 1.0149 0.7176 0.2929  0.0166  -0.0222 162 SER B C   
2727 O O   . SER B 162 ? 0.4683 1.0076 0.6904 0.2880  0.0270  -0.0295 162 SER B O   
2728 C CB  . SER B 162 ? 0.5517 1.1127 0.7819 0.2732  -0.0036 -0.0068 162 SER B CB  
2729 O OG  . SER B 162 ? 0.5303 1.1451 0.7801 0.2684  -0.0094 -0.0022 162 SER B OG  
2730 N N   . TYR B 163 ? 0.5502 1.0074 0.7452 0.2948  0.0149  -0.0225 163 TYR B N   
2731 C CA  . TYR B 163 ? 0.5296 0.9554 0.7085 0.2897  0.0244  -0.0320 163 TYR B CA  
2732 C C   . TYR B 163 ? 0.5564 0.9773 0.7362 0.3071  0.0351  -0.0416 163 TYR B C   
2733 O O   . TYR B 163 ? 0.5603 0.9930 0.7375 0.3006  0.0457  -0.0504 163 TYR B O   
2734 C CB  . TYR B 163 ? 0.4629 0.8299 0.6203 0.2882  0.0195  -0.0302 163 TYR B CB  
2735 C CG  . TYR B 163 ? 0.5314 0.8645 0.6717 0.2854  0.0289  -0.0408 163 TYR B CG  
2736 C CD1 . TYR B 163 ? 0.4218 0.7755 0.5610 0.2687  0.0358  -0.0461 163 TYR B CD1 
2737 C CD2 . TYR B 163 ? 0.5927 0.8757 0.7186 0.2985  0.0311  -0.0456 163 TYR B CD2 
2738 C CE1 . TYR B 163 ? 0.4660 0.7924 0.5885 0.2660  0.0440  -0.0557 163 TYR B CE1 
2739 C CE2 . TYR B 163 ? 0.5856 0.8405 0.6953 0.2947  0.0392  -0.0565 163 TYR B CE2 
2740 C CZ  . TYR B 163 ? 0.5517 0.8293 0.6590 0.2789  0.0454  -0.0615 163 TYR B CZ  
2741 O OH  . TYR B 163 ? 0.4855 0.7380 0.5751 0.2747  0.0529  -0.0719 163 TYR B OH  
2742 N N   . ARG B 164 ? 0.6398 1.0421 0.8226 0.3292  0.0328  -0.0401 164 ARG B N   
2743 C CA  . ARG B 164 ? 0.6999 1.0955 0.8846 0.3469  0.0433  -0.0506 164 ARG B CA  
2744 C C   . ARG B 164 ? 0.5535 1.0082 0.7567 0.3463  0.0518  -0.0555 164 ARG B C   
2745 O O   . ARG B 164 ? 0.5809 1.0382 0.7800 0.3479  0.0638  -0.0669 164 ARG B O   
2746 C CB  . ARG B 164 ? 0.6505 1.0209 0.8399 0.3709  0.0387  -0.0466 164 ARG B CB  
2747 C CG  . ARG B 164 ? 0.8701 1.1789 1.0404 0.3710  0.0317  -0.0419 164 ARG B CG  
2748 C CD  . ARG B 164 ? 0.9737 1.2397 1.1220 0.3621  0.0392  -0.0533 164 ARG B CD  
2749 N NE  . ARG B 164 ? 1.2448 1.4557 1.3750 0.3575  0.0323  -0.0482 164 ARG B NE  
2750 C CZ  . ARG B 164 ? 1.2913 1.4540 1.4028 0.3540  0.0366  -0.0567 164 ARG B CZ  
2751 N NH1 . ARG B 164 ? 1.2029 1.3633 1.3093 0.3554  0.0477  -0.0714 164 ARG B NH1 
2752 N NH2 . ARG B 164 ? 1.2810 1.3983 1.3781 0.3478  0.0296  -0.0503 164 ARG B NH2 
2753 N N   . GLU B 165 ? 0.5545 1.0584 0.7775 0.3427  0.0458  -0.0471 165 GLU B N   
2754 C CA  . GLU B 165 ? 0.5545 1.1177 0.7961 0.3385  0.0535  -0.0506 165 GLU B CA  
2755 C C   . GLU B 165 ? 0.6284 1.2026 0.8608 0.3155  0.0621  -0.0562 165 GLU B C   
2756 O O   . GLU B 165 ? 0.5900 1.1854 0.8249 0.3163  0.0743  -0.0648 165 GLU B O   
2757 C CB  . GLU B 165 ? 0.5771 1.1890 0.8396 0.3336  0.0439  -0.0402 165 GLU B CB  
2758 C CG  . GLU B 165 ? 0.7368 1.4107 1.0224 0.3344  0.0510  -0.0430 165 GLU B CG  
2759 C CD  . GLU B 165 ? 0.8946 1.5694 1.1894 0.3620  0.0594  -0.0505 165 GLU B CD  
2760 O OE1 . GLU B 165 ? 1.0686 1.7400 1.3741 0.3832  0.0526  -0.0454 165 GLU B OE1 
2761 O OE2 . GLU B 165 ? 0.7333 1.4123 1.0245 0.3626  0.0729  -0.0614 165 GLU B OE2 
2762 N N   . LEU B 166 ? 0.5461 1.1067 0.7678 0.2948  0.0561  -0.0511 166 LEU B N   
2763 C CA  . LEU B 166 ? 0.4836 1.0491 0.6955 0.2730  0.0637  -0.0551 166 LEU B CA  
2764 C C   . LEU B 166 ? 0.5053 1.0350 0.6978 0.2807  0.0740  -0.0662 166 LEU B C   
2765 O O   . LEU B 166 ? 0.5440 1.0947 0.7342 0.2732  0.0853  -0.0726 166 LEU B O   
2766 C CB  . LEU B 166 ? 0.4594 1.0072 0.6628 0.2533  0.0549  -0.0482 166 LEU B CB  
2767 C CG  . LEU B 166 ? 0.4216 0.9807 0.6192 0.2280  0.0611  -0.0493 166 LEU B CG  
2768 C CD1 . LEU B 166 ? 0.4157 1.0304 0.6290 0.2170  0.0695  -0.0497 166 LEU B CD1 
2769 C CD2 . LEU B 166 ? 0.4029 0.9535 0.5989 0.2087  0.0517  -0.0421 166 LEU B CD2 
2770 N N   . ARG B 167 ? 0.5263 1.0017 0.7038 0.2944  0.0702  -0.0687 167 ARG B N   
2771 C CA  . ARG B 167 ? 0.4704 0.9054 0.6268 0.2992  0.0783  -0.0800 167 ARG B CA  
2772 C C   . ARG B 167 ? 0.6194 1.0742 0.7808 0.3125  0.0908  -0.0909 167 ARG B C   
2773 O O   . ARG B 167 ? 0.5863 1.0493 0.7373 0.3043  0.1013  -0.0992 167 ARG B O   
2774 C CB  . ARG B 167 ? 0.5169 0.8921 0.6601 0.3112  0.0709  -0.0795 167 ARG B CB  
2775 C CG  . ARG B 167 ? 0.5649 0.8915 0.6838 0.3114  0.0766  -0.0906 167 ARG B CG  
2776 C CD  . ARG B 167 ? 0.6303 0.9006 0.7398 0.3226  0.0692  -0.0889 167 ARG B CD  
2777 N NE  . ARG B 167 ? 0.6338 0.8546 0.7190 0.3157  0.0709  -0.0969 167 ARG B NE  
2778 C CZ  . ARG B 167 ? 0.6795 0.8828 0.7523 0.3201  0.0804  -0.1111 167 ARG B CZ  
2779 N NH1 . ARG B 167 ? 0.6064 0.8359 0.6887 0.3327  0.0901  -0.1197 167 ARG B NH1 
2780 N NH2 . ARG B 167 ? 0.6191 0.7784 0.6697 0.3114  0.0800  -0.1175 167 ARG B NH2 
2781 N N   . THR B 168 ? 0.6163 1.0810 0.7939 0.3335  0.0900  -0.0909 168 THR B N   
2782 C CA  . THR B 168 ? 0.5743 1.0601 0.7594 0.3481  0.1024  -0.1020 168 THR B CA  
2783 C C   . THR B 168 ? 0.5821 1.1292 0.7788 0.3340  0.1107  -0.1021 168 THR B C   
2784 O O   . THR B 168 ? 0.6240 1.1825 0.8140 0.3334  0.1236  -0.1127 168 THR B O   
2785 C CB  . THR B 168 ? 0.7131 1.2019 0.9172 0.3737  0.0991  -0.1002 168 THR B CB  
2786 O OG1 . THR B 168 ? 0.7254 1.2614 0.9520 0.3704  0.0913  -0.0881 168 THR B OG1 
2787 C CG2 . THR B 168 ? 0.5973 1.0246 0.7901 0.3852  0.0903  -0.0975 168 THR B CG2 
2788 N N   . GLN B 169 ? 0.5066 1.0933 0.7195 0.3207  0.1037  -0.0904 169 GLN B N   
2789 C CA  . GLN B 169 ? 0.5957 1.2406 0.8210 0.3053  0.1115  -0.0896 169 GLN B CA  
2790 C C   . GLN B 169 ? 0.6251 1.2668 0.8316 0.2814  0.1182  -0.0914 169 GLN B C   
2791 O O   . GLN B 169 ? 0.6464 1.3275 0.8569 0.2710  0.1287  -0.0937 169 GLN B O   
2792 C CB  . GLN B 169 ? 0.5489 1.2359 0.7965 0.2952  0.1018  -0.0773 169 GLN B CB  
2793 C CG  . GLN B 169 ? 0.6201 1.3406 0.8924 0.3162  0.1008  -0.0768 169 GLN B CG  
2794 C CD  . GLN B 169 ? 0.7652 1.5228 1.0575 0.3071  0.0891  -0.0649 169 GLN B CD  
2795 O OE1 . GLN B 169 ? 0.7128 1.4637 0.9994 0.2868  0.0805  -0.0573 169 GLN B OE1 
2796 N NE2 . GLN B 169 ? 0.8678 1.6663 1.1840 0.3218  0.0888  -0.0638 169 GLN B NE2 
2797 N N   . ILE B 170 ? 0.5243 1.1203 0.7102 0.2731  0.1130  -0.0903 170 ILE B N   
2798 C CA  . ILE B 170 ? 0.5188 1.1088 0.6851 0.2538  0.1203  -0.0929 170 ILE B CA  
2799 C C   . ILE B 170 ? 0.6010 1.1698 0.7491 0.2658  0.1315  -0.1072 170 ILE B C   
2800 O O   . ILE B 170 ? 0.6721 1.2653 0.8133 0.2559  0.1429  -0.1115 170 ILE B O   
2801 C CB  . ILE B 170 ? 0.5166 1.0682 0.6681 0.2404  0.1110  -0.0869 170 ILE B CB  
2802 C CG1 . ILE B 170 ? 0.3860 0.9644 0.5538 0.2220  0.1023  -0.0738 170 ILE B CG1 
2803 C CG2 . ILE B 170 ? 0.4257 0.9618 0.5532 0.2266  0.1188  -0.0915 170 ILE B CG2 
2804 C CD1 . ILE B 170 ? 0.3641 0.9024 0.5227 0.2162  0.0910  -0.0684 170 ILE B CD1 
2805 N N   . LEU B 171 ? 0.6001 1.1230 0.7398 0.2862  0.1287  -0.1148 171 LEU B N   
2806 C CA  . LEU B 171 ? 0.5842 1.0761 0.7024 0.2946  0.1379  -0.1296 171 LEU B CA  
2807 C C   . LEU B 171 ? 0.6748 1.2000 0.8020 0.3074  0.1511  -0.1399 171 LEU B C   
2808 O O   . LEU B 171 ? 0.7802 1.2945 0.8892 0.3088  0.1617  -0.1527 171 LEU B O   
2809 C CB  . LEU B 171 ? 0.5813 1.0128 0.6895 0.3105  0.1308  -0.1342 171 LEU B CB  
2810 C CG  . LEU B 171 ? 0.6498 1.0396 0.7426 0.2980  0.1198  -0.1276 171 LEU B CG  
2811 C CD1 . LEU B 171 ? 0.6615 0.9902 0.7420 0.3118  0.1148  -0.1336 171 LEU B CD1 
2812 C CD2 . LEU B 171 ? 0.5961 0.9872 0.6685 0.2767  0.1240  -0.1292 171 LEU B CD2 
2813 N N   . GLN B 172 ? 0.6089 1.1754 0.7636 0.3168  0.1509  -0.1351 172 GLN B N   
2814 C CA  . GLN B 172 ? 0.6775 1.2813 0.8434 0.3287  0.1642  -0.1445 172 GLN B CA  
2815 C C   . GLN B 172 ? 0.7542 1.3909 0.9088 0.3092  0.1762  -0.1473 172 GLN B C   
2816 O O   . GLN B 172 ? 0.8323 1.4790 0.9807 0.3173  0.1895  -0.1601 172 GLN B O   
2817 C CB  . GLN B 172 ? 0.6691 1.3187 0.8680 0.3384  0.1607  -0.1367 172 GLN B CB  
2818 C CG  . GLN B 172 ? 0.7263 1.4267 0.9388 0.3145  0.1577  -0.1235 172 GLN B CG  
2819 C CD  . GLN B 172 ? 0.8484 1.5953 1.0930 0.3233  0.1535  -0.1165 172 GLN B CD  
2820 O OE1 . GLN B 172 ? 0.8975 1.6479 1.1560 0.3487  0.1557  -0.1223 172 GLN B OE1 
2821 N NE2 . GLN B 172 ? 0.7776 1.5588 1.0343 0.3022  0.1467  -0.1040 172 GLN B NE2 
2822 N N   . TYR B 173 ? 0.7215 1.3752 0.8729 0.2829  0.1721  -0.1352 173 TYR B N   
2823 C CA  . TYR B 173 ? 0.7649 1.4555 0.9086 0.2629  0.1833  -0.1345 173 TYR B CA  
2824 C C   . TYR B 173 ? 0.7520 1.4138 0.8629 0.2586  0.1917  -0.1453 173 TYR B C   
2825 O O   . TYR B 173 ? 0.7924 1.4835 0.8938 0.2424  0.2015  -0.1446 173 TYR B O   
2826 C CB  . TYR B 173 ? 0.6561 1.3706 0.8058 0.2346  0.1770  -0.1177 173 TYR B CB  
2827 C CG  . TYR B 173 ? 0.6670 1.4267 0.8487 0.2330  0.1724  -0.1083 173 TYR B CG  
2828 C CD1 . TYR B 173 ? 0.6935 1.4403 0.8902 0.2415  0.1587  -0.1022 173 TYR B CD1 
2829 C CD2 . TYR B 173 ? 0.6795 1.4958 0.8761 0.2245  0.1819  -0.1064 173 TYR B CD2 
2830 C CE1 . TYR B 173 ? 0.7032 1.4933 0.9279 0.2395  0.1538  -0.0941 173 TYR B CE1 
2831 C CE2 . TYR B 173 ? 0.6755 1.5349 0.9013 0.2225  0.1775  -0.0987 173 TYR B CE2 
2832 C CZ  . TYR B 173 ? 0.7886 1.6352 1.0283 0.2301  0.1631  -0.0929 173 TYR B CZ  
2833 O OH  . TYR B 173 ? 0.6574 1.5490 0.9251 0.2271  0.1581  -0.0856 173 TYR B OH  
2834 N N   . MET B 174 ? 0.7112 1.3171 0.8033 0.2700  0.1876  -0.1544 174 MET B N   
2835 C CA  . MET B 174 ? 0.8757 1.4563 0.9357 0.2652  0.1953  -0.1660 174 MET B CA  
2836 C C   . MET B 174 ? 0.7813 1.3397 0.8342 0.2887  0.2040  -0.1857 174 MET B C   
2837 O O   . MET B 174 ? 0.9253 1.4460 0.9833 0.3075  0.1983  -0.1912 174 MET B O   
2838 C CB  . MET B 174 ? 0.8888 1.4234 0.9268 0.2526  0.1849  -0.1617 174 MET B CB  
2839 C CG  . MET B 174 ? 0.7422 1.2780 0.7958 0.2427  0.1719  -0.1449 174 MET B CG  
2840 S SD  . MET B 174 ? 0.7533 1.2330 0.7844 0.2326  0.1597  -0.1411 174 MET B SD  
2841 C CE  . MET B 174 ? 0.7243 1.1530 0.7571 0.2597  0.1540  -0.1524 174 MET B CE  
2842 C C1  . GOL C .   ? 0.5887 0.6488 0.6332 0.0067  -0.0242 -0.0527 201 GOL B C1  
2843 O O1  . GOL C .   ? 0.6046 0.6963 0.6525 0.0029  -0.0285 -0.0537 201 GOL B O1  
2844 C C2  . GOL C .   ? 0.6007 0.6546 0.6509 0.0120  -0.0221 -0.0459 201 GOL B C2  
2845 O O2  . GOL C .   ? 0.5279 0.6030 0.5875 0.0055  -0.0228 -0.0456 201 GOL B O2  
2846 C C3  . GOL C .   ? 0.6161 0.6397 0.6679 0.0087  -0.0186 -0.0473 201 GOL B C3  
2847 O O3  . GOL C .   ? 0.8268 0.8454 0.8847 -0.0040 -0.0179 -0.0549 201 GOL B O3  
2848 O O   . HOH D .   ? 0.7469 0.4361 0.6869 -0.0083 -0.0271 -0.0603 201 HOH A O   
2849 O O   . HOH D .   ? 0.5328 0.4996 0.7160 0.0430  0.0475  -0.1193 202 HOH A O   
2850 O O   . HOH D .   ? 0.4495 0.4039 0.4151 -0.0006 0.0250  -0.0274 203 HOH A O   
2851 O O   . HOH D .   ? 0.6305 0.6371 0.4872 0.0302  -0.0144 0.0406  204 HOH A O   
2852 O O   . HOH D .   ? 0.5919 0.5627 0.7126 0.0241  0.0672  -0.1618 205 HOH A O   
2853 O O   . HOH D .   ? 0.8857 1.1725 0.4458 -0.1006 0.0634  0.0389  206 HOH A O   
2854 O O   . HOH D .   ? 0.4008 0.3124 0.5186 0.0246  0.0118  -0.0820 207 HOH A O   
2855 O O   . HOH D .   ? 0.5237 0.8537 0.4237 0.0209  -0.0988 -0.0124 208 HOH A O   
2856 O O   . HOH D .   ? 0.4696 0.4423 0.5356 0.0062  0.0492  -0.1356 209 HOH A O   
2857 O O   . HOH D .   ? 0.5636 0.6585 0.4824 -0.0767 0.0148  -0.2215 210 HOH A O   
2858 O O   . HOH D .   ? 0.7488 0.3329 0.6544 0.0428  -0.0079 0.0161  211 HOH A O   
2859 O O   . HOH D .   ? 0.4683 0.7516 0.5090 0.0175  -0.0681 -0.0404 212 HOH A O   
2860 O O   . HOH D .   ? 0.4026 0.3248 0.5380 0.0301  0.0102  -0.0726 213 HOH A O   
2861 O O   . HOH D .   ? 0.7262 0.3427 0.6252 0.0773  -0.0113 0.0348  214 HOH A O   
2862 O O   . HOH D .   ? 0.5875 0.5506 0.6215 -0.0404 0.0174  -0.1753 215 HOH A O   
2863 O O   . HOH D .   ? 0.3742 0.3100 0.4391 0.0066  -0.0077 -0.0615 216 HOH A O   
2864 O O   . HOH D .   ? 0.5578 0.6845 0.4363 0.0618  -0.0586 0.0374  217 HOH A O   
2865 O O   . HOH D .   ? 0.7148 0.7650 0.4712 -0.0247 0.0218  0.0721  218 HOH A O   
2866 O O   . HOH D .   ? 0.5927 0.7382 0.5390 -0.0545 0.1308  -0.1041 219 HOH A O   
2867 O O   . HOH D .   ? 0.5518 0.2318 0.4912 0.0054  -0.0185 -0.0395 220 HOH A O   
2868 O O   . HOH D .   ? 0.3212 0.2246 0.4029 0.0040  -0.0259 -0.0345 221 HOH A O   
2869 O O   . HOH D .   ? 0.5844 0.1752 0.5038 -0.0113 -0.0080 -0.0066 222 HOH A O   
2870 O O   . HOH D .   ? 0.6903 0.4439 0.6464 -0.0024 -0.0341 -0.0643 223 HOH A O   
2871 O O   . HOH D .   ? 0.5009 0.4517 0.3964 0.0472  -0.0153 0.0369  224 HOH A O   
2872 O O   . HOH D .   ? 0.5599 0.2631 0.4957 0.0417  -0.0164 -0.0405 225 HOH A O   
2873 O O   . HOH D .   ? 0.5219 0.5654 0.5177 -0.0325 0.0816  -0.0679 226 HOH A O   
2874 O O   . HOH D .   ? 0.5556 0.5609 0.5616 -0.0197 0.0603  -0.0612 227 HOH A O   
2875 O O   . HOH D .   ? 0.7029 0.6216 0.6048 -0.0905 0.0728  0.0637  228 HOH A O   
2876 O O   . HOH D .   ? 0.5976 0.6931 0.5467 -0.0295 0.0970  -0.1762 229 HOH A O   
2877 O O   . HOH D .   ? 0.7268 0.5945 0.6515 0.1057  -0.0267 0.0448  230 HOH A O   
2878 O O   . HOH D .   ? 0.5414 0.4793 0.5203 0.1231  -0.0248 0.0045  231 HOH A O   
2879 O O   . HOH D .   ? 0.7140 0.2298 0.5846 -0.0416 0.0080  0.0858  232 HOH A O   
2880 O O   . HOH D .   ? 0.6297 0.4059 0.5708 0.1026  -0.0155 0.0005  233 HOH A O   
2881 O O   . HOH D .   ? 0.4768 0.3829 0.5565 -0.0260 -0.0016 -0.0324 234 HOH A O   
2882 O O   . HOH D .   ? 0.9280 1.3683 0.4486 -0.1328 0.0339  -0.1266 235 HOH A O   
2883 O O   . HOH D .   ? 0.8309 0.3658 0.7353 0.0470  -0.0070 0.0142  236 HOH A O   
2884 O O   . HOH D .   ? 0.4709 0.7185 0.5337 0.0284  -0.0531 -0.0353 237 HOH A O   
2885 O O   . HOH E .   ? 0.7178 0.5074 0.5565 0.0401  -0.0288 -0.1378 301 HOH B O   
2886 O O   . HOH E .   ? 0.4476 0.3923 0.4257 0.0459  -0.0159 -0.0264 302 HOH B O   
2887 O O   . HOH E .   ? 0.5607 0.4472 0.6646 -0.0449 -0.0143 -0.0115 303 HOH B O   
2888 O O   . HOH E .   ? 0.6955 0.6802 0.6451 0.0019  -0.0967 0.0887  304 HOH B O   
2889 O O   . HOH E .   ? 0.6104 1.0090 0.4604 0.0078  0.1197  -0.0091 305 HOH B O   
2890 O O   . HOH E .   ? 0.5180 0.3372 0.4082 0.0035  -0.0532 -0.1023 306 HOH B O   
2891 O O   . HOH E .   ? 0.4485 0.3905 0.5483 0.0167  -0.0677 -0.0088 307 HOH B O   
2892 O O   . HOH E .   ? 0.5777 0.9449 0.4862 0.0082  0.1042  -0.0002 308 HOH B O   
2893 O O   . HOH E .   ? 0.5360 0.3031 0.4911 0.0227  -0.0277 -0.0569 309 HOH B O   
2894 O O   . HOH E .   ? 0.5539 0.7069 0.5095 -0.0031 0.0338  0.0234  310 HOH B O   
2895 O O   . HOH E .   ? 0.4039 0.6311 0.4900 0.0441  0.0141  -0.0178 311 HOH B O   
2896 O O   . HOH E .   ? 0.4125 0.6881 0.5061 0.1581  -0.0410 0.0022  312 HOH B O   
2897 O O   . HOH E .   ? 0.3263 0.7520 0.4837 0.1249  0.0168  -0.0247 313 HOH B O   
2898 O O   . HOH E .   ? 0.5819 0.3797 0.4797 0.0913  -0.0078 -0.0976 314 HOH B O   
2899 O O   . HOH E .   ? 0.4497 0.3827 0.5197 0.0297  -0.0947 0.0749  315 HOH B O   
2900 O O   . HOH E .   ? 0.4348 0.2928 0.5947 0.0481  -0.0562 0.0326  316 HOH B O   
2901 O O   . HOH E .   ? 0.5483 0.4760 0.4720 0.0392  -0.0272 -0.0447 317 HOH B O   
2902 O O   . HOH E .   ? 0.3975 0.3174 0.4835 0.0161  -0.0513 -0.0199 318 HOH B O   
2903 O O   . HOH E .   ? 0.5437 0.4941 0.4326 0.0339  -0.0278 -0.0490 319 HOH B O   
2904 O O   . HOH E .   ? 0.5342 0.6719 0.5410 0.0234  0.0260  -0.0017 320 HOH B O   
2905 O O   . HOH E .   ? 0.4945 0.3311 0.6188 -0.0158 -0.0138 -0.0365 321 HOH B O   
2906 O O   . HOH E .   ? 0.5321 0.2737 0.4707 0.0513  -0.0196 -0.0543 322 HOH B O   
2907 O O   . HOH E .   ? 0.4829 0.7914 0.5803 0.0175  -0.0520 -0.0367 323 HOH B O   
2908 O O   . HOH E .   ? 0.6211 0.5930 0.5735 -0.0050 -0.0575 0.0775  324 HOH B O   
2909 O O   . HOH E .   ? 0.3792 0.4178 0.4167 0.0193  -0.0019 -0.0084 325 HOH B O   
2910 O O   . HOH E .   ? 0.4444 0.3303 0.5744 0.0253  0.0030  -0.0751 326 HOH B O   
2911 O O   . HOH E .   ? 0.5095 0.3674 0.6987 0.0584  -0.0434 0.0065  327 HOH B O   
2912 O O   . HOH E .   ? 0.6342 1.0550 0.4221 0.0688  0.1501  -0.0932 328 HOH B O   
2913 O O   . HOH E .   ? 0.5023 0.4487 0.5285 0.0182  -0.0875 0.0576  329 HOH B O   
2914 O O   . HOH E .   ? 0.4981 0.3206 0.4561 0.1033  -0.0150 -0.0132 330 HOH B O   
2915 O O   . HOH E .   ? 0.4514 0.6759 0.5147 0.1014  -0.0467 -0.0067 331 HOH B O   
2916 O O   . HOH E .   ? 0.6814 0.4956 0.6290 0.1898  0.0119  -0.0698 332 HOH B O   
2917 O O   . HOH E .   ? 0.7283 0.5498 0.6727 -0.0316 -0.0671 -0.0882 333 HOH B O   
2918 O O   . HOH E .   ? 0.6439 0.6731 0.6062 -0.0043 -0.1374 0.0485  334 HOH B O   
2919 O O   . HOH E .   ? 0.6142 0.5863 0.6860 0.0314  -0.1193 0.0821  335 HOH B O   
2920 O O   . HOH E .   ? 0.7508 0.4933 0.6391 0.1044  -0.0032 -0.1082 336 HOH B O   
2921 O O   . HOH E .   ? 0.4799 0.6964 0.5396 0.1454  -0.0491 0.0086  337 HOH B O   
2922 O O   . HOH E .   ? 0.6844 0.4050 0.6153 0.1015  -0.0128 -0.0108 338 HOH B O   
2923 O O   . HOH E .   ? 0.7459 0.5352 0.5921 0.0117  -0.0455 -0.1342 339 HOH B O   
2924 O O   . HOH E .   ? 0.5453 0.3700 0.7487 0.0729  -0.0583 0.0462  340 HOH B O   
# 
