data_9HTH
# 
_entry.id   9HTH 
# 
_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   9HTH         pdb_00009hth 10.2210/pdb9hth/pdb 
WWPDB D_1292143551 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-07 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HTH 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              daniel.kuemmel@uni-muenster.de 
_pdbx_contact_author.name_first         Daniel 
_pdbx_contact_author.name_last          Kuemmel 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3950-5914 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fitzian, K.' 1 ? 
'Yilmaz, Z.'  2 ? 
'Humberg, C.' 3 ? 
'Mootz, H.D.' 4 ? 
'Kuemmel, D.' 5 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2723 
_citation.page_last                 2723 
_citation.title                     
;A cysteine-less and ultra-fast split intein rationally engineered from being aggregation-prone to highly efficient in protein trans-splicing.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57596-x 
_citation.pdbx_database_id_PubMed   40108172 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Humberg, C.' 1 0000-0003-3394-9338 
primary 'Yilmaz, Z.'  2 ?                   
primary 'Fitzian, K.' 3 0000-0002-9668-9919 
primary 'Dorner, W.'  4 0000-0001-7921-5765 
primary 'Kummel, D.'  5 0000-0003-3950-5914 
primary 'Mootz, H.D.' 6 0000-0002-3385-0234 
# 
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 'DNA-directed DNA polymerase' 19793.750 2   2.7.7.7 ? ? IntN,IntC 
2 water   nat water                         18.015    196 ?       ? ? ?         
# 
_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       
;IDTDAVVGDTIIDVSGKKMTIAEFYDSTPDVFMRRNDEARDWVKRVGGKTSLSVNTYSGEVERKNINYIMKHTVKKRMFK
IKAGGKEVIVTADHSVMVKRDGKIIDVKPTEMKQTDRVVKWMLTGSHMIEFIEFEIEDLGVMEIDVYDIEVDGNHNFFGN
DILVHASVYLNKL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IDTDAVVGDTIIDVSGKKMTIAEFYDSTPDVFMRRNDEARDWVKRVGGKTSLSVNTYSGEVERKNINYIMKHTVKKRMFK
IKAGGKEVIVTADHSVMVKRDGKIIDVKPTEMKQTDRVVKWMLTGSHMIEFIEFEIEDLGVMEIDVYDIEVDGNHNFFGN
DILVHASVYLNKL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   ASP n 
1 3   THR n 
1 4   ASP n 
1 5   ALA n 
1 6   VAL n 
1 7   VAL n 
1 8   GLY n 
1 9   ASP n 
1 10  THR n 
1 11  ILE n 
1 12  ILE n 
1 13  ASP n 
1 14  VAL n 
1 15  SER n 
1 16  GLY n 
1 17  LYS n 
1 18  LYS n 
1 19  MET n 
1 20  THR n 
1 21  ILE n 
1 22  ALA n 
1 23  GLU n 
1 24  PHE n 
1 25  TYR n 
1 26  ASP n 
1 27  SER n 
1 28  THR n 
1 29  PRO n 
1 30  ASP n 
1 31  VAL n 
1 32  PHE n 
1 33  MET n 
1 34  ARG n 
1 35  ARG n 
1 36  ASN n 
1 37  ASP n 
1 38  GLU n 
1 39  ALA n 
1 40  ARG n 
1 41  ASP n 
1 42  TRP n 
1 43  VAL n 
1 44  LYS n 
1 45  ARG n 
1 46  VAL n 
1 47  GLY n 
1 48  GLY n 
1 49  LYS n 
1 50  THR n 
1 51  SER n 
1 52  LEU n 
1 53  SER n 
1 54  VAL n 
1 55  ASN n 
1 56  THR n 
1 57  TYR n 
1 58  SER n 
1 59  GLY n 
1 60  GLU n 
1 61  VAL n 
1 62  GLU n 
1 63  ARG n 
1 64  LYS n 
1 65  ASN n 
1 66  ILE n 
1 67  ASN n 
1 68  TYR n 
1 69  ILE n 
1 70  MET n 
1 71  LYS n 
1 72  HIS n 
1 73  THR n 
1 74  VAL n 
1 75  LYS n 
1 76  LYS n 
1 77  ARG n 
1 78  MET n 
1 79  PHE n 
1 80  LYS n 
1 81  ILE n 
1 82  LYS n 
1 83  ALA n 
1 84  GLY n 
1 85  GLY n 
1 86  LYS n 
1 87  GLU n 
1 88  VAL n 
1 89  ILE n 
1 90  VAL n 
1 91  THR n 
1 92  ALA n 
1 93  ASP n 
1 94  HIS n 
1 95  SER n 
1 96  VAL n 
1 97  MET n 
1 98  VAL n 
1 99  LYS n 
1 100 ARG n 
1 101 ASP n 
1 102 GLY n 
1 103 LYS n 
1 104 ILE n 
1 105 ILE n 
1 106 ASP n 
1 107 VAL n 
1 108 LYS n 
1 109 PRO n 
1 110 THR n 
1 111 GLU n 
1 112 MET n 
1 113 LYS n 
1 114 GLN n 
1 115 THR n 
1 116 ASP n 
1 117 ARG n 
1 118 VAL n 
1 119 VAL n 
1 120 LYS n 
1 121 TRP n 
1 122 MET n 
1 123 LEU n 
1 124 THR n 
1 125 GLY n 
1 126 SER n 
1 127 HIS n 
1 128 MET n 
1 129 ILE n 
1 130 GLU n 
1 131 PHE n 
1 132 ILE n 
1 133 GLU n 
1 134 PHE n 
1 135 GLU n 
1 136 ILE n 
1 137 GLU n 
1 138 ASP n 
1 139 LEU n 
1 140 GLY n 
1 141 VAL n 
1 142 MET n 
1 143 GLU n 
1 144 ILE n 
1 145 ASP n 
1 146 VAL n 
1 147 TYR n 
1 148 ASP n 
1 149 ILE n 
1 150 GLU n 
1 151 VAL n 
1 152 ASP n 
1 153 GLY n 
1 154 ASN n 
1 155 HIS n 
1 156 ASN n 
1 157 PHE n 
1 158 PHE n 
1 159 GLY n 
1 160 ASN n 
1 161 ASP n 
1 162 ILE n 
1 163 LEU n 
1 164 VAL n 
1 165 HIS n 
1 166 ALA n 
1 167 SER n 
1 168 VAL n 
1 169 TYR n 
1 170 LEU n 
1 171 ASN n 
1 172 LYS n 
1 173 LEU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   127 ? ? ? ? ? ? ? ? ? 'Aeromonas phage Aes123' 1198018 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 128 173 ? ? ? ? ? ? ? ? ? 'Aeromonas phage Aes123' 1198018 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ILE 1   -3  ?   ?   ?   A . n 
A 1 2   ASP 2   -2  ?   ?   ?   A . n 
A 1 3   THR 3   -1  ?   ?   ?   A . n 
A 1 4   ASP 4   0   0   ASP ASP A . n 
A 1 5   ALA 5   1   1   ALA ALA A . n 
A 1 6   VAL 6   2   2   VAL VAL A . n 
A 1 7   VAL 7   3   3   VAL VAL A . n 
A 1 8   GLY 8   4   4   GLY GLY A . n 
A 1 9   ASP 9   5   5   ASP ASP A . n 
A 1 10  THR 10  6   6   THR THR A . n 
A 1 11  ILE 11  7   7   ILE ILE A . n 
A 1 12  ILE 12  8   8   ILE ILE A . n 
A 1 13  ASP 13  9   9   ASP ASP A . n 
A 1 14  VAL 14  10  10  VAL VAL A . n 
A 1 15  SER 15  11  11  SER SER A . n 
A 1 16  GLY 16  12  12  GLY GLY A . n 
A 1 17  LYS 17  13  13  LYS LYS A . n 
A 1 18  LYS 18  14  14  LYS LYS A . n 
A 1 19  MET 19  15  15  MET MET A . n 
A 1 20  THR 20  16  16  THR THR A . n 
A 1 21  ILE 21  17  17  ILE ILE A . n 
A 1 22  ALA 22  18  18  ALA ALA A . n 
A 1 23  GLU 23  19  19  GLU GLU A . n 
A 1 24  PHE 24  20  20  PHE PHE A . n 
A 1 25  TYR 25  21  21  TYR TYR A . n 
A 1 26  ASP 26  22  22  ASP ASP A . n 
A 1 27  SER 27  23  23  SER SER A . n 
A 1 28  THR 28  24  24  THR THR A . n 
A 1 29  PRO 29  25  25  PRO PRO A . n 
A 1 30  ASP 30  26  26  ASP ASP A . n 
A 1 31  VAL 31  27  27  VAL VAL A . n 
A 1 32  PHE 32  28  28  PHE PHE A . n 
A 1 33  MET 33  29  29  MET MET A . n 
A 1 34  ARG 34  30  30  ARG ARG A . n 
A 1 35  ARG 35  31  31  ARG ARG A . n 
A 1 36  ASN 36  32  32  ASN ASN A . n 
A 1 37  ASP 37  33  33  ASP ASP A . n 
A 1 38  GLU 38  34  34  GLU GLU A . n 
A 1 39  ALA 39  35  35  ALA ALA A . n 
A 1 40  ARG 40  36  36  ARG ARG A . n 
A 1 41  ASP 41  37  37  ASP ASP A . n 
A 1 42  TRP 42  38  38  TRP TRP A . n 
A 1 43  VAL 43  39  39  VAL VAL A . n 
A 1 44  LYS 44  40  40  LYS LYS A . n 
A 1 45  ARG 45  41  41  ARG ARG A . n 
A 1 46  VAL 46  42  42  VAL VAL A . n 
A 1 47  GLY 47  43  43  GLY GLY A . n 
A 1 48  GLY 48  44  44  GLY GLY A . n 
A 1 49  LYS 49  45  45  LYS LYS A . n 
A 1 50  THR 50  46  46  THR THR A . n 
A 1 51  SER 51  47  47  SER SER A . n 
A 1 52  LEU 52  48  48  LEU LEU A . n 
A 1 53  SER 53  49  49  SER SER A . n 
A 1 54  VAL 54  50  50  VAL VAL A . n 
A 1 55  ASN 55  51  51  ASN ASN A . n 
A 1 56  THR 56  52  52  THR THR A . n 
A 1 57  TYR 57  53  53  TYR TYR A . n 
A 1 58  SER 58  54  54  SER SER A . n 
A 1 59  GLY 59  55  55  GLY GLY A . n 
A 1 60  GLU 60  56  56  GLU GLU A . n 
A 1 61  VAL 61  57  57  VAL VAL A . n 
A 1 62  GLU 62  58  58  GLU GLU A . n 
A 1 63  ARG 63  59  59  ARG ARG A . n 
A 1 64  LYS 64  60  60  LYS LYS A . n 
A 1 65  ASN 65  61  61  ASN ASN A . n 
A 1 66  ILE 66  62  62  ILE ILE A . n 
A 1 67  ASN 67  63  63  ASN ASN A . n 
A 1 68  TYR 68  64  64  TYR TYR A . n 
A 1 69  ILE 69  65  65  ILE ILE A . n 
A 1 70  MET 70  66  66  MET MET A . n 
A 1 71  LYS 71  67  67  LYS LYS A . n 
A 1 72  HIS 72  68  68  HIS HIS A . n 
A 1 73  THR 73  69  69  THR THR A . n 
A 1 74  VAL 74  70  70  VAL VAL A . n 
A 1 75  LYS 75  71  71  LYS LYS A . n 
A 1 76  LYS 76  72  72  LYS LYS A . n 
A 1 77  ARG 77  73  73  ARG ARG A . n 
A 1 78  MET 78  74  74  MET MET A . n 
A 1 79  PHE 79  75  75  PHE PHE A . n 
A 1 80  LYS 80  76  76  LYS LYS A . n 
A 1 81  ILE 81  77  77  ILE ILE A . n 
A 1 82  LYS 82  78  78  LYS LYS A . n 
A 1 83  ALA 83  79  79  ALA ALA A . n 
A 1 84  GLY 84  80  80  GLY GLY A . n 
A 1 85  GLY 85  81  81  GLY GLY A . n 
A 1 86  LYS 86  82  82  LYS LYS A . n 
A 1 87  GLU 87  83  83  GLU GLU A . n 
A 1 88  VAL 88  84  84  VAL VAL A . n 
A 1 89  ILE 89  85  85  ILE ILE A . n 
A 1 90  VAL 90  86  86  VAL VAL A . n 
A 1 91  THR 91  87  87  THR THR A . n 
A 1 92  ALA 92  88  88  ALA ALA A . n 
A 1 93  ASP 93  89  89  ASP ASP A . n 
A 1 94  HIS 94  90  90  HIS HIS A . n 
A 1 95  SER 95  91  91  SER SER A . n 
A 1 96  VAL 96  92  92  VAL VAL A . n 
A 1 97  MET 97  93  93  MET MET A . n 
A 1 98  VAL 98  94  94  VAL VAL A . n 
A 1 99  LYS 99  95  95  LYS LYS A . n 
A 1 100 ARG 100 96  96  ARG ARG A . n 
A 1 101 ASP 101 97  97  ASP ASP A . n 
A 1 102 GLY 102 98  98  GLY GLY A . n 
A 1 103 LYS 103 99  99  LYS LYS A . n 
A 1 104 ILE 104 100 100 ILE ILE A . n 
A 1 105 ILE 105 101 101 ILE ILE A . n 
A 1 106 ASP 106 102 102 ASP ASP A . n 
A 1 107 VAL 107 103 103 VAL VAL A . n 
A 1 108 LYS 108 104 104 LYS LYS A . n 
A 1 109 PRO 109 105 105 PRO PRO A . n 
A 1 110 THR 110 106 106 THR THR A . n 
A 1 111 GLU 111 107 107 GLU GLU A . n 
A 1 112 MET 112 108 108 MET MET A . n 
A 1 113 LYS 113 109 109 LYS LYS A . n 
A 1 114 GLN 114 110 110 GLN GLN A . n 
A 1 115 THR 115 111 111 THR THR A . n 
A 1 116 ASP 116 112 112 ASP ASP A . n 
A 1 117 ARG 117 113 113 ARG ARG A . n 
A 1 118 VAL 118 114 114 VAL VAL A . n 
A 1 119 VAL 119 115 115 VAL VAL A . n 
A 1 120 LYS 120 116 116 LYS LYS A . n 
A 1 121 TRP 121 117 117 TRP TRP A . n 
A 1 122 MET 122 118 118 MET MET A . n 
A 1 123 LEU 123 119 119 LEU LEU A . n 
A 1 124 THR 124 120 120 THR THR A . n 
A 1 125 GLY 125 120 120 GLY GLY A A n 
A 1 126 SER 126 120 120 SER SER A B n 
A 1 127 HIS 127 120 120 HIS HIS A C n 
A 1 128 MET 128 121 121 MET MET A . n 
A 1 129 ILE 129 122 122 ILE ILE A . n 
A 1 130 GLU 130 123 123 GLU GLU A . n 
A 1 131 PHE 131 124 124 PHE PHE A . n 
A 1 132 ILE 132 125 125 ILE ILE A . n 
A 1 133 GLU 133 126 126 GLU GLU A . n 
A 1 134 PHE 134 127 127 PHE PHE A . n 
A 1 135 GLU 135 128 128 GLU GLU A . n 
A 1 136 ILE 136 129 129 ILE ILE A . n 
A 1 137 GLU 137 130 130 GLU GLU A . n 
A 1 138 ASP 138 131 131 ASP ASP A . n 
A 1 139 LEU 139 132 132 LEU LEU A . n 
A 1 140 GLY 140 133 133 GLY GLY A . n 
A 1 141 VAL 141 134 134 VAL VAL A . n 
A 1 142 MET 142 135 135 MET MET A . n 
A 1 143 GLU 143 136 136 GLU GLU A . n 
A 1 144 ILE 144 137 137 ILE ILE A . n 
A 1 145 ASP 145 138 138 ASP ASP A . n 
A 1 146 VAL 146 139 139 VAL VAL A . n 
A 1 147 TYR 147 140 140 TYR TYR A . n 
A 1 148 ASP 148 141 141 ASP ASP A . n 
A 1 149 ILE 149 142 142 ILE ILE A . n 
A 1 150 GLU 150 143 143 GLU GLU A . n 
A 1 151 VAL 151 144 144 VAL VAL A . n 
A 1 152 ASP 152 145 145 ASP ASP A . n 
A 1 153 GLY 153 146 146 GLY GLY A . n 
A 1 154 ASN 154 147 147 ASN ASN A . n 
A 1 155 HIS 155 148 148 HIS HIS A . n 
A 1 156 ASN 156 149 149 ASN ASN A . n 
A 1 157 PHE 157 150 150 PHE PHE A . n 
A 1 158 PHE 158 151 151 PHE PHE A . n 
A 1 159 GLY 159 152 152 GLY GLY A . n 
A 1 160 ASN 160 153 153 ASN ASN A . n 
A 1 161 ASP 161 154 154 ASP ASP A . n 
A 1 162 ILE 162 155 155 ILE ILE A . n 
A 1 163 LEU 163 156 156 LEU LEU A . n 
A 1 164 VAL 164 157 157 VAL VAL A . n 
A 1 165 HIS 165 158 158 HIS HIS A . n 
A 1 166 ALA 166 159 159 ALA ALA A . n 
A 1 167 SER 167 160 160 SER SER A . n 
A 1 168 VAL 168 161 161 VAL VAL A . n 
A 1 169 TYR 169 162 162 TYR TYR A . n 
A 1 170 LEU 170 163 163 LEU LEU A . n 
A 1 171 ASN 171 164 164 ASN ASN A . n 
A 1 172 LYS 172 165 165 LYS LYS A . n 
A 1 173 LEU 173 166 166 LEU LEU A . n 
B 1 1   ILE 1   -3  -3  ILE ILE B . n 
B 1 2   ASP 2   -2  -2  ASP ASP B . n 
B 1 3   THR 3   -1  -1  THR THR B . n 
B 1 4   ASP 4   0   0   ASP ASP B . n 
B 1 5   ALA 5   1   1   ALA ALA B . n 
B 1 6   VAL 6   2   2   VAL VAL B . n 
B 1 7   VAL 7   3   3   VAL VAL B . n 
B 1 8   GLY 8   4   4   GLY GLY B . n 
B 1 9   ASP 9   5   5   ASP ASP B . n 
B 1 10  THR 10  6   6   THR THR B . n 
B 1 11  ILE 11  7   7   ILE ILE B . n 
B 1 12  ILE 12  8   8   ILE ILE B . n 
B 1 13  ASP 13  9   9   ASP ASP B . n 
B 1 14  VAL 14  10  10  VAL VAL B . n 
B 1 15  SER 15  11  11  SER SER B . n 
B 1 16  GLY 16  12  12  GLY GLY B . n 
B 1 17  LYS 17  13  13  LYS LYS B . n 
B 1 18  LYS 18  14  14  LYS LYS B . n 
B 1 19  MET 19  15  15  MET MET B . n 
B 1 20  THR 20  16  16  THR THR B . n 
B 1 21  ILE 21  17  17  ILE ILE B . n 
B 1 22  ALA 22  18  18  ALA ALA B . n 
B 1 23  GLU 23  19  19  GLU GLU B . n 
B 1 24  PHE 24  20  20  PHE PHE B . n 
B 1 25  TYR 25  21  21  TYR TYR B . n 
B 1 26  ASP 26  22  22  ASP ASP B . n 
B 1 27  SER 27  23  23  SER SER B . n 
B 1 28  THR 28  24  24  THR THR B . n 
B 1 29  PRO 29  25  25  PRO PRO B . n 
B 1 30  ASP 30  26  26  ASP ASP B . n 
B 1 31  VAL 31  27  27  VAL VAL B . n 
B 1 32  PHE 32  28  28  PHE PHE B . n 
B 1 33  MET 33  29  29  MET MET B . n 
B 1 34  ARG 34  30  30  ARG ARG B . n 
B 1 35  ARG 35  31  31  ARG ARG B . n 
B 1 36  ASN 36  32  32  ASN ASN B . n 
B 1 37  ASP 37  33  33  ASP ASP B . n 
B 1 38  GLU 38  34  34  GLU GLU B . n 
B 1 39  ALA 39  35  35  ALA ALA B . n 
B 1 40  ARG 40  36  36  ARG ARG B . n 
B 1 41  ASP 41  37  37  ASP ASP B . n 
B 1 42  TRP 42  38  38  TRP TRP B . n 
B 1 43  VAL 43  39  39  VAL VAL B . n 
B 1 44  LYS 44  40  40  LYS LYS B . n 
B 1 45  ARG 45  41  41  ARG ARG B . n 
B 1 46  VAL 46  42  42  VAL VAL B . n 
B 1 47  GLY 47  43  43  GLY GLY B . n 
B 1 48  GLY 48  44  44  GLY GLY B . n 
B 1 49  LYS 49  45  45  LYS LYS B . n 
B 1 50  THR 50  46  46  THR THR B . n 
B 1 51  SER 51  47  47  SER SER B . n 
B 1 52  LEU 52  48  48  LEU LEU B . n 
B 1 53  SER 53  49  49  SER SER B . n 
B 1 54  VAL 54  50  50  VAL VAL B . n 
B 1 55  ASN 55  51  51  ASN ASN B . n 
B 1 56  THR 56  52  52  THR THR B . n 
B 1 57  TYR 57  53  53  TYR TYR B . n 
B 1 58  SER 58  54  54  SER SER B . n 
B 1 59  GLY 59  55  55  GLY GLY B . n 
B 1 60  GLU 60  56  56  GLU GLU B . n 
B 1 61  VAL 61  57  57  VAL VAL B . n 
B 1 62  GLU 62  58  58  GLU GLU B . n 
B 1 63  ARG 63  59  59  ARG ARG B . n 
B 1 64  LYS 64  60  60  LYS LYS B . n 
B 1 65  ASN 65  61  61  ASN ASN B . n 
B 1 66  ILE 66  62  62  ILE ILE B . n 
B 1 67  ASN 67  63  63  ASN ASN B . n 
B 1 68  TYR 68  64  64  TYR TYR B . n 
B 1 69  ILE 69  65  65  ILE ILE B . n 
B 1 70  MET 70  66  66  MET MET B . n 
B 1 71  LYS 71  67  67  LYS LYS B . n 
B 1 72  HIS 72  68  68  HIS HIS B . n 
B 1 73  THR 73  69  69  THR THR B . n 
B 1 74  VAL 74  70  70  VAL VAL B . n 
B 1 75  LYS 75  71  71  LYS LYS B . n 
B 1 76  LYS 76  72  72  LYS LYS B . n 
B 1 77  ARG 77  73  73  ARG ARG B . n 
B 1 78  MET 78  74  74  MET MET B . n 
B 1 79  PHE 79  75  75  PHE PHE B . n 
B 1 80  LYS 80  76  76  LYS LYS B . n 
B 1 81  ILE 81  77  77  ILE ILE B . n 
B 1 82  LYS 82  78  78  LYS LYS B . n 
B 1 83  ALA 83  79  79  ALA ALA B . n 
B 1 84  GLY 84  80  80  GLY GLY B . n 
B 1 85  GLY 85  81  81  GLY GLY B . n 
B 1 86  LYS 86  82  82  LYS LYS B . n 
B 1 87  GLU 87  83  83  GLU GLU B . n 
B 1 88  VAL 88  84  84  VAL VAL B . n 
B 1 89  ILE 89  85  85  ILE ILE B . n 
B 1 90  VAL 90  86  86  VAL VAL B . n 
B 1 91  THR 91  87  87  THR THR B . n 
B 1 92  ALA 92  88  88  ALA ALA B . n 
B 1 93  ASP 93  89  89  ASP ASP B . n 
B 1 94  HIS 94  90  90  HIS HIS B . n 
B 1 95  SER 95  91  91  SER SER B . n 
B 1 96  VAL 96  92  92  VAL VAL B . n 
B 1 97  MET 97  93  93  MET MET B . n 
B 1 98  VAL 98  94  94  VAL VAL B . n 
B 1 99  LYS 99  95  95  LYS LYS B . n 
B 1 100 ARG 100 96  96  ARG ARG B . n 
B 1 101 ASP 101 97  97  ASP ASP B . n 
B 1 102 GLY 102 98  98  GLY GLY B . n 
B 1 103 LYS 103 99  99  LYS LYS B . n 
B 1 104 ILE 104 100 100 ILE ILE B . n 
B 1 105 ILE 105 101 101 ILE ILE B . n 
B 1 106 ASP 106 102 102 ASP ASP B . n 
B 1 107 VAL 107 103 103 VAL VAL B . n 
B 1 108 LYS 108 104 104 LYS LYS B . n 
B 1 109 PRO 109 105 105 PRO PRO B . n 
B 1 110 THR 110 106 106 THR THR B . n 
B 1 111 GLU 111 107 107 GLU GLU B . n 
B 1 112 MET 112 108 108 MET MET B . n 
B 1 113 LYS 113 109 109 LYS LYS B . n 
B 1 114 GLN 114 110 110 GLN GLN B . n 
B 1 115 THR 115 111 111 THR THR B . n 
B 1 116 ASP 116 112 112 ASP ASP B . n 
B 1 117 ARG 117 113 113 ARG ARG B . n 
B 1 118 VAL 118 114 114 VAL VAL B . n 
B 1 119 VAL 119 115 115 VAL VAL B . n 
B 1 120 LYS 120 116 116 LYS LYS B . n 
B 1 121 TRP 121 117 117 TRP TRP B . n 
B 1 122 MET 122 118 118 MET MET B . n 
B 1 123 LEU 123 119 119 LEU LEU B . n 
B 1 124 THR 124 120 120 THR THR B . n 
B 1 125 GLY 125 120 120 GLY GLY B A n 
B 1 126 SER 126 120 120 SER SER B B n 
B 1 127 HIS 127 120 120 HIS HIS B C n 
B 1 128 MET 128 121 121 MET MET B . n 
B 1 129 ILE 129 122 122 ILE ILE B . n 
B 1 130 GLU 130 123 123 GLU GLU B . n 
B 1 131 PHE 131 124 124 PHE PHE B . n 
B 1 132 ILE 132 125 125 ILE ILE B . n 
B 1 133 GLU 133 126 126 GLU GLU B . n 
B 1 134 PHE 134 127 127 PHE PHE B . n 
B 1 135 GLU 135 128 128 GLU GLU B . n 
B 1 136 ILE 136 129 129 ILE ILE B . n 
B 1 137 GLU 137 130 130 GLU GLU B . n 
B 1 138 ASP 138 131 131 ASP ASP B . n 
B 1 139 LEU 139 132 132 LEU LEU B . n 
B 1 140 GLY 140 133 133 GLY GLY B . n 
B 1 141 VAL 141 134 134 VAL VAL B . n 
B 1 142 MET 142 135 135 MET MET B . n 
B 1 143 GLU 143 136 136 GLU GLU B . n 
B 1 144 ILE 144 137 137 ILE ILE B . n 
B 1 145 ASP 145 138 138 ASP ASP B . n 
B 1 146 VAL 146 139 139 VAL VAL B . n 
B 1 147 TYR 147 140 140 TYR TYR B . n 
B 1 148 ASP 148 141 141 ASP ASP B . n 
B 1 149 ILE 149 142 142 ILE ILE B . n 
B 1 150 GLU 150 143 143 GLU GLU B . n 
B 1 151 VAL 151 144 144 VAL VAL B . n 
B 1 152 ASP 152 145 145 ASP ASP B . n 
B 1 153 GLY 153 146 146 GLY GLY B . n 
B 1 154 ASN 154 147 147 ASN ASN B . n 
B 1 155 HIS 155 148 148 HIS HIS B . n 
B 1 156 ASN 156 149 149 ASN ASN B . n 
B 1 157 PHE 157 150 150 PHE PHE B . n 
B 1 158 PHE 158 151 151 PHE PHE B . n 
B 1 159 GLY 159 152 152 GLY GLY B . n 
B 1 160 ASN 160 153 153 ASN ASN B . n 
B 1 161 ASP 161 154 154 ASP ASP B . n 
B 1 162 ILE 162 155 155 ILE ILE B . n 
B 1 163 LEU 163 156 156 LEU LEU B . n 
B 1 164 VAL 164 157 157 VAL VAL B . n 
B 1 165 HIS 165 158 158 HIS HIS B . n 
B 1 166 ALA 166 159 159 ALA ALA B . n 
B 1 167 SER 167 160 160 SER SER B . n 
B 1 168 VAL 168 161 161 VAL VAL B . n 
B 1 169 TYR 169 162 162 TYR TYR B . n 
B 1 170 LEU 170 163 163 LEU LEU B . n 
B 1 171 ASN 171 164 164 ASN ASN B . n 
B 1 172 LYS 172 165 165 LYS LYS B . n 
B 1 173 LEU 173 166 166 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1   201 165 HOH HOH A . 
C 2 HOH 2   202 146 HOH HOH A . 
C 2 HOH 3   203 89  HOH HOH A . 
C 2 HOH 4   204 96  HOH HOH A . 
C 2 HOH 5   205 46  HOH HOH A . 
C 2 HOH 6   206 190 HOH HOH A . 
C 2 HOH 7   207 141 HOH HOH A . 
C 2 HOH 8   208 203 HOH HOH A . 
C 2 HOH 9   209 136 HOH HOH A . 
C 2 HOH 10  210 196 HOH HOH A . 
C 2 HOH 11  211 188 HOH HOH A . 
C 2 HOH 12  212 133 HOH HOH A . 
C 2 HOH 13  213 17  HOH HOH A . 
C 2 HOH 14  214 112 HOH HOH A . 
C 2 HOH 15  215 25  HOH HOH A . 
C 2 HOH 16  216 150 HOH HOH A . 
C 2 HOH 17  217 159 HOH HOH A . 
C 2 HOH 18  218 14  HOH HOH A . 
C 2 HOH 19  219 168 HOH HOH A . 
C 2 HOH 20  220 52  HOH HOH A . 
C 2 HOH 21  221 37  HOH HOH A . 
C 2 HOH 22  222 127 HOH HOH A . 
C 2 HOH 23  223 131 HOH HOH A . 
C 2 HOH 24  224 30  HOH HOH A . 
C 2 HOH 25  225 117 HOH HOH A . 
C 2 HOH 26  226 164 HOH HOH A . 
C 2 HOH 27  227 32  HOH HOH A . 
C 2 HOH 28  228 50  HOH HOH A . 
C 2 HOH 29  229 23  HOH HOH A . 
C 2 HOH 30  230 85  HOH HOH A . 
C 2 HOH 31  231 38  HOH HOH A . 
C 2 HOH 32  232 40  HOH HOH A . 
C 2 HOH 33  233 28  HOH HOH A . 
C 2 HOH 34  234 80  HOH HOH A . 
C 2 HOH 35  235 101 HOH HOH A . 
C 2 HOH 36  236 156 HOH HOH A . 
C 2 HOH 37  237 120 HOH HOH A . 
C 2 HOH 38  238 18  HOH HOH A . 
C 2 HOH 39  239 49  HOH HOH A . 
C 2 HOH 40  240 29  HOH HOH A . 
C 2 HOH 41  241 84  HOH HOH A . 
C 2 HOH 42  242 9   HOH HOH A . 
C 2 HOH 43  243 82  HOH HOH A . 
C 2 HOH 44  244 76  HOH HOH A . 
C 2 HOH 45  245 78  HOH HOH A . 
C 2 HOH 46  246 66  HOH HOH A . 
C 2 HOH 47  247 16  HOH HOH A . 
C 2 HOH 48  248 8   HOH HOH A . 
C 2 HOH 49  249 35  HOH HOH A . 
C 2 HOH 50  250 126 HOH HOH A . 
C 2 HOH 51  251 43  HOH HOH A . 
C 2 HOH 52  252 109 HOH HOH A . 
C 2 HOH 53  253 103 HOH HOH A . 
C 2 HOH 54  254 148 HOH HOH A . 
C 2 HOH 55  255 153 HOH HOH A . 
C 2 HOH 56  256 132 HOH HOH A . 
C 2 HOH 57  257 97  HOH HOH A . 
C 2 HOH 58  258 157 HOH HOH A . 
C 2 HOH 59  259 94  HOH HOH A . 
C 2 HOH 60  260 60  HOH HOH A . 
C 2 HOH 61  261 58  HOH HOH A . 
C 2 HOH 62  262 91  HOH HOH A . 
C 2 HOH 63  263 174 HOH HOH A . 
C 2 HOH 64  264 138 HOH HOH A . 
C 2 HOH 65  265 158 HOH HOH A . 
C 2 HOH 66  266 116 HOH HOH A . 
C 2 HOH 67  267 108 HOH HOH A . 
C 2 HOH 68  268 128 HOH HOH A . 
C 2 HOH 69  269 160 HOH HOH A . 
C 2 HOH 70  270 41  HOH HOH A . 
C 2 HOH 71  271 15  HOH HOH A . 
C 2 HOH 72  272 104 HOH HOH A . 
C 2 HOH 73  273 74  HOH HOH A . 
C 2 HOH 74  274 20  HOH HOH A . 
C 2 HOH 75  275 154 HOH HOH A . 
C 2 HOH 76  276 169 HOH HOH A . 
C 2 HOH 77  277 181 HOH HOH A . 
C 2 HOH 78  278 119 HOH HOH A . 
C 2 HOH 79  279 86  HOH HOH A . 
C 2 HOH 80  280 87  HOH HOH A . 
C 2 HOH 81  281 173 HOH HOH A . 
D 2 HOH 1   201 176 HOH HOH B . 
D 2 HOH 2   202 22  HOH HOH B . 
D 2 HOH 3   203 142 HOH HOH B . 
D 2 HOH 4   204 191 HOH HOH B . 
D 2 HOH 5   205 135 HOH HOH B . 
D 2 HOH 6   206 198 HOH HOH B . 
D 2 HOH 7   207 139 HOH HOH B . 
D 2 HOH 8   208 134 HOH HOH B . 
D 2 HOH 9   209 64  HOH HOH B . 
D 2 HOH 10  210 3   HOH HOH B . 
D 2 HOH 11  211 39  HOH HOH B . 
D 2 HOH 12  212 202 HOH HOH B . 
D 2 HOH 13  213 44  HOH HOH B . 
D 2 HOH 14  214 189 HOH HOH B . 
D 2 HOH 15  215 63  HOH HOH B . 
D 2 HOH 16  216 19  HOH HOH B . 
D 2 HOH 17  217 27  HOH HOH B . 
D 2 HOH 18  218 100 HOH HOH B . 
D 2 HOH 19  219 11  HOH HOH B . 
D 2 HOH 20  220 118 HOH HOH B . 
D 2 HOH 21  221 56  HOH HOH B . 
D 2 HOH 22  222 92  HOH HOH B . 
D 2 HOH 23  223 178 HOH HOH B . 
D 2 HOH 24  224 162 HOH HOH B . 
D 2 HOH 25  225 33  HOH HOH B . 
D 2 HOH 26  226 171 HOH HOH B . 
D 2 HOH 27  227 102 HOH HOH B . 
D 2 HOH 28  228 10  HOH HOH B . 
D 2 HOH 29  229 145 HOH HOH B . 
D 2 HOH 30  230 90  HOH HOH B . 
D 2 HOH 31  231 54  HOH HOH B . 
D 2 HOH 32  232 125 HOH HOH B . 
D 2 HOH 33  233 194 HOH HOH B . 
D 2 HOH 34  234 12  HOH HOH B . 
D 2 HOH 35  235 31  HOH HOH B . 
D 2 HOH 36  236 115 HOH HOH B . 
D 2 HOH 37  237 129 HOH HOH B . 
D 2 HOH 38  238 59  HOH HOH B . 
D 2 HOH 39  239 42  HOH HOH B . 
D 2 HOH 40  240 193 HOH HOH B . 
D 2 HOH 41  241 140 HOH HOH B . 
D 2 HOH 42  242 53  HOH HOH B . 
D 2 HOH 43  243 197 HOH HOH B . 
D 2 HOH 44  244 72  HOH HOH B . 
D 2 HOH 45  245 106 HOH HOH B . 
D 2 HOH 46  246 69  HOH HOH B . 
D 2 HOH 47  247 199 HOH HOH B . 
D 2 HOH 48  248 180 HOH HOH B . 
D 2 HOH 49  249 98  HOH HOH B . 
D 2 HOH 50  250 192 HOH HOH B . 
D 2 HOH 51  251 81  HOH HOH B . 
D 2 HOH 52  252 6   HOH HOH B . 
D 2 HOH 53  253 68  HOH HOH B . 
D 2 HOH 54  254 172 HOH HOH B . 
D 2 HOH 55  255 34  HOH HOH B . 
D 2 HOH 56  256 62  HOH HOH B . 
D 2 HOH 57  257 13  HOH HOH B . 
D 2 HOH 58  258 182 HOH HOH B . 
D 2 HOH 59  259 51  HOH HOH B . 
D 2 HOH 60  260 149 HOH HOH B . 
D 2 HOH 61  261 65  HOH HOH B . 
D 2 HOH 62  262 179 HOH HOH B . 
D 2 HOH 63  263 107 HOH HOH B . 
D 2 HOH 64  264 7   HOH HOH B . 
D 2 HOH 65  265 166 HOH HOH B . 
D 2 HOH 66  266 36  HOH HOH B . 
D 2 HOH 67  267 77  HOH HOH B . 
D 2 HOH 68  268 70  HOH HOH B . 
D 2 HOH 69  269 161 HOH HOH B . 
D 2 HOH 70  270 163 HOH HOH B . 
D 2 HOH 71  271 147 HOH HOH B . 
D 2 HOH 72  272 83  HOH HOH B . 
D 2 HOH 73  273 95  HOH HOH B . 
D 2 HOH 74  274 24  HOH HOH B . 
D 2 HOH 75  275 88  HOH HOH B . 
D 2 HOH 76  276 130 HOH HOH B . 
D 2 HOH 77  277 45  HOH HOH B . 
D 2 HOH 78  278 122 HOH HOH B . 
D 2 HOH 79  279 121 HOH HOH B . 
D 2 HOH 80  280 110 HOH HOH B . 
D 2 HOH 81  281 151 HOH HOH B . 
D 2 HOH 82  282 26  HOH HOH B . 
D 2 HOH 83  283 124 HOH HOH B . 
D 2 HOH 84  284 201 HOH HOH B . 
D 2 HOH 85  285 5   HOH HOH B . 
D 2 HOH 86  286 200 HOH HOH B . 
D 2 HOH 87  287 93  HOH HOH B . 
D 2 HOH 88  288 75  HOH HOH B . 
D 2 HOH 89  289 113 HOH HOH B . 
D 2 HOH 90  290 79  HOH HOH B . 
D 2 HOH 91  291 21  HOH HOH B . 
D 2 HOH 92  292 61  HOH HOH B . 
D 2 HOH 93  293 71  HOH HOH B . 
D 2 HOH 94  294 47  HOH HOH B . 
D 2 HOH 95  295 177 HOH HOH B . 
D 2 HOH 96  296 137 HOH HOH B . 
D 2 HOH 97  297 57  HOH HOH B . 
D 2 HOH 98  298 167 HOH HOH B . 
D 2 HOH 99  299 195 HOH HOH B . 
D 2 HOH 100 300 152 HOH HOH B . 
D 2 HOH 101 301 170 HOH HOH B . 
D 2 HOH 102 302 105 HOH HOH B . 
D 2 HOH 103 303 155 HOH HOH B . 
D 2 HOH 104 304 143 HOH HOH B . 
D 2 HOH 105 305 204 HOH HOH B . 
D 2 HOH 106 306 73  HOH HOH B . 
D 2 HOH 107 307 144 HOH HOH B . 
D 2 HOH 108 308 99  HOH HOH B . 
D 2 HOH 109 309 67  HOH HOH B . 
D 2 HOH 110 310 175 HOH HOH B . 
D 2 HOH 111 311 111 HOH HOH B . 
D 2 HOH 112 312 187 HOH HOH B . 
D 2 HOH 113 313 184 HOH HOH B . 
D 2 HOH 114 314 55  HOH HOH B . 
D 2 HOH 115 315 186 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.13_2998: ???)' ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                  ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                  ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HTH 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     30.129 
_cell.length_a_esd                 ? 
_cell.length_b                     63.013 
_cell.length_b_esd                 ? 
_cell.length_c                     162.404 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9HTH 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9HTH 
_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             1.96 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.36 
_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              ? 
_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    
;Morpheus 50 % Precipitant mix 1, 0.1 M buffer system 3 pH 8.5, 0.1 M
monosaccharides
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     173 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-11-24 
_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   0.97956 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97956 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HTH 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.378 
_reflns.d_resolution_low                               40.601 
_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                                     64820 
_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                           96.27 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.43 
_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                                0.077 
_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                                   0.999 
_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                                    1.38 
_reflns_shell.d_res_low                                     1.43 
_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                             5518 
_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                                  0.782 
_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                                 9HTH 
_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                            1.378 
_refine.ls_d_res_low                             40.601 
_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                     62985 
_refine.ls_number_reflns_R_free                  1944 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.67 
_refine.ls_percent_reflns_R_free                 3.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1935 
_refine.ls_R_factor_R_free                       0.2263 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1925 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_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                 23.15 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.378 
_refine_hist.d_res_low                        40.601 
_refine_hist.number_atoms_solvent             196 
_refine_hist.number_atoms_total               2943 
_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        2747 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 2791 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 0.939 ? 3752 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 4.721 ? 1050 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.091 ? 425  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 474  ? f_plane_restr      ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.3781 1.4124 . . 124 3733 85.00  . . . . 0.2753 . . . . . . . . . . . . . . . 0.3044 
'X-RAY DIFFRACTION' 1.4124 1.4506 . . 128 4023 90.00  . . . . 0.2581 . . . . . . . . . . . . . . . 0.2731 
'X-RAY DIFFRACTION' 1.4506 1.4933 . . 130 4047 92.00  . . . . 0.2320 . . . . . . . . . . . . . . . 0.3043 
'X-RAY DIFFRACTION' 1.4933 1.5415 . . 134 4204 95.00  . . . . 0.2090 . . . . . . . . . . . . . . . 0.2018 
'X-RAY DIFFRACTION' 1.5415 1.5966 . . 136 4342 97.00  . . . . 0.2056 . . . . . . . . . . . . . . . 0.2233 
'X-RAY DIFFRACTION' 1.5966 1.6605 . . 136 4380 98.00  . . . . 0.2028 . . . . . . . . . . . . . . . 0.2240 
'X-RAY DIFFRACTION' 1.6605 1.7361 . . 140 4366 99.00  . . . . 0.2060 . . . . . . . . . . . . . . . 0.2350 
'X-RAY DIFFRACTION' 1.7361 1.8276 . . 142 4424 99.00  . . . . 0.2093 . . . . . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 1.8276 1.9421 . . 144 4518 100.00 . . . . 0.1993 . . . . . . . . . . . . . . . 0.2369 
'X-RAY DIFFRACTION' 1.9421 2.0921 . . 142 4481 100.00 . . . . 0.1941 . . . . . . . . . . . . . . . 0.2083 
'X-RAY DIFFRACTION' 2.0921 2.3026 . . 144 4539 100.00 . . . . 0.1949 . . . . . . . . . . . . . . . 0.2376 
'X-RAY DIFFRACTION' 2.3026 2.6357 . . 144 4541 100.00 . . . . 0.2022 . . . . . . . . . . . . . . . 0.2463 
'X-RAY DIFFRACTION' 2.6357 3.3205 . . 147 4621 100.00 . . . . 0.2028 . . . . . . . . . . . . . . . 0.2535 
'X-RAY DIFFRACTION' 3.3205 40.601 . . 153 4822 100.00 . . . . 0.1665 . . . . . . . . . . . . . . . 0.1968 
# 
_struct.entry_id                     9HTH 
_struct.title                        
'Crystal structure of the fused, cysteine-less Aes123 PolB1 split intein (with S1A, N159A mutations)' 
_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        9HTH 
_struct_keywords.text            'intein, protein splicing, cysteine-less, ligation, SPLICING' 
_struct_keywords.pdbx_keywords   SPLICING 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP I6YMS9_9CAUD I6YMS9 ? 1 
;IDTDSVVGDTIIDVSGKKMTIAEFYDSTPDVFMRRNDEARDWVKRVGGKTSLSVNTYSGEVERKNINYIMKHTVKKRMFK
IKAGGKEVIVTADHSVMVKRDGKIIDVKPTEMKQTDRVVKWMLT
;
169 
2 PDB 9HTH         9HTH   ? 1 ? 128 
# 
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 9HTH A 1   ? 124 ? I6YMS9 169 ? 292 ? -3  120 
2 2 9HTH A 128 ? 173 ? 9HTH   121 ? 166 ? 121 166 
3 1 9HTH B 1   ? 124 ? I6YMS9 169 ? 292 ? -3  120 
4 2 9HTH B 128 ? 173 ? 9HTH   121 ? 166 ? 121 166 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9HTH ALA A 5   ? UNP I6YMS9 SER 173 'engineered mutation' 1   1 
1 9HTH GLY A 125 A UNP I6YMS9 ?   ?   linker                120 2 
1 9HTH SER A 126 B UNP I6YMS9 ?   ?   linker                120 3 
1 9HTH HIS A 127 C UNP I6YMS9 ?   ?   linker                120 4 
3 9HTH ALA B 5   ? UNP I6YMS9 SER 173 'engineered mutation' 1   5 
3 9HTH GLY B 125 A UNP I6YMS9 ?   ?   linker                120 6 
3 9HTH SER B 126 B UNP I6YMS9 ?   ?   linker                120 7 
3 9HTH HIS B 127 C UNP I6YMS9 ?   ?   linker                120 8 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ILE A 21  ? THR A 28  ? ILE A 17  THR A 24  1 ? 8 
HELX_P HELX_P2 AA2 ILE B 21  ? THR B 28  ? ILE B 17  THR B 24  1 ? 8 
HELX_P HELX_P3 AA3 LYS B 108 ? MET B 112 ? LYS B 104 MET B 108 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
AA5 ? 7 ? 
AA6 ? 2 ? 
AA7 ? 4 ? 
AA8 ? 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 6 ? anti-parallel 
AA1 1 7 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 5 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 5 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 6 ? anti-parallel 
AA5 1 7 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 5 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 5 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 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 VAL A 6   ? VAL A 7   ? VAL A 2   VAL A 3   
AA1 2 PHE A 32  ? ASN A 36  ? PHE A 28  ASN A 32  
AA1 3 ASP A 41  ? ARG A 45  ? ASP A 37  ARG A 41  
AA1 4 THR A 50  ? VAL A 54  ? THR A 46  VAL A 50  
AA1 5 VAL A 61  ? ALA A 83  ? VAL A 57  ALA A 79  
AA1 6 LYS A 86  ? THR A 91  ? LYS A 82  THR A 87  
AA1 7 GLU A 135 ? VAL A 151 ? GLU A 128 VAL A 144 
AA2 1 ILE A 11  ? VAL A 14  ? ILE A 7   VAL A 10  
AA2 2 LYS A 17  ? THR A 20  ? LYS A 13  THR A 16  
AA3 1 LYS A 103 ? VAL A 107 ? LYS A 99  VAL A 103 
AA3 2 VAL A 96  ? ARG A 100 ? VAL A 92  ARG A 96  
AA3 3 ARG A 117 ? TRP A 121 ? ARG A 113 TRP A 117 
AA3 4 ILE A 129 ? ILE A 132 ? ILE A 122 ILE A 125 
AA4 1 ASN A 156 ? GLY A 159 ? ASN A 149 GLY A 152 
AA4 2 ILE A 162 ? HIS A 165 ? ILE A 155 HIS A 158 
AA5 1 VAL B 6   ? VAL B 7   ? VAL B 2   VAL B 3   
AA5 2 PHE B 32  ? ASN B 36  ? PHE B 28  ASN B 32  
AA5 3 ASP B 41  ? ARG B 45  ? ASP B 37  ARG B 41  
AA5 4 THR B 50  ? VAL B 54  ? THR B 46  VAL B 50  
AA5 5 VAL B 61  ? ALA B 83  ? VAL B 57  ALA B 79  
AA5 6 LYS B 86  ? THR B 91  ? LYS B 82  THR B 87  
AA5 7 GLU B 135 ? VAL B 151 ? GLU B 128 VAL B 144 
AA6 1 ILE B 11  ? VAL B 14  ? ILE B 7   VAL B 10  
AA6 2 LYS B 17  ? THR B 20  ? LYS B 13  THR B 16  
AA7 1 LYS B 103 ? VAL B 107 ? LYS B 99  VAL B 103 
AA7 2 VAL B 96  ? ARG B 100 ? VAL B 92  ARG B 96  
AA7 3 ARG B 117 ? TRP B 121 ? ARG B 113 TRP B 117 
AA7 4 ILE B 129 ? ILE B 132 ? ILE B 122 ILE B 125 
AA8 1 ASN B 156 ? GLY B 159 ? ASN B 149 GLY B 152 
AA8 2 ILE B 162 ? HIS B 165 ? ILE B 155 HIS B 158 
# 
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 6 N VAL A 7   ? N VAL A 3   O ILE A 89  ? O ILE A 85  
AA1 1 7 N VAL A 6   ? N VAL A 2   O TYR A 147 ? O TYR A 140 
AA1 2 3 N MET A 33  ? N MET A 29  O VAL A 43  ? O VAL A 39  
AA1 3 5 N LYS A 44  ? N LYS A 40  O ILE A 69  ? O ILE A 65  
AA1 4 5 N SER A 51  ? N SER A 47  O LYS A 64  ? O LYS A 60  
AA1 5 6 N ILE A 81  ? N ILE A 77  O VAL A 88  ? O VAL A 84  
AA1 5 7 N LYS A 80  ? N LYS A 76  O GLU A 137 ? O GLU A 130 
AA2 1 2 N VAL A 14  ? N VAL A 10  O LYS A 17  ? O LYS A 13  
AA3 1 2 O VAL A 107 ? O VAL A 103 N VAL A 96  ? N VAL A 92  
AA3 2 3 N LYS A 99  ? N LYS A 95  O ARG A 117 ? O ARG A 113 
AA3 3 4 N LYS A 120 ? N LYS A 116 O GLU A 130 ? O GLU A 123 
AA4 1 2 N PHE A 157 ? N PHE A 150 O VAL A 164 ? O VAL A 157 
AA5 1 6 N VAL B 7   ? N VAL B 3   O ILE B 89  ? O ILE B 85  
AA5 1 7 N VAL B 6   ? N VAL B 2   O TYR B 147 ? O TYR B 140 
AA5 2 3 N MET B 33  ? N MET B 29  O VAL B 43  ? O VAL B 39  
AA5 3 5 N LYS B 44  ? N LYS B 40  O ILE B 69  ? O ILE B 65  
AA5 4 5 N SER B 51  ? N SER B 47  O LYS B 64  ? O LYS B 60  
AA5 5 6 N PHE B 79  ? N PHE B 75  O VAL B 90  ? O VAL B 86  
AA5 5 7 N MET B 70  ? N MET B 66  O ASP B 148 ? O ASP B 141 
AA6 1 2 N VAL B 14  ? N VAL B 10  O LYS B 17  ? O LYS B 13  
AA7 1 2 O VAL B 107 ? O VAL B 103 N VAL B 96  ? N VAL B 92  
AA7 2 3 N LYS B 99  ? N LYS B 95  O ARG B 117 ? O ARG B 113 
AA7 3 4 N LYS B 120 ? N LYS B 116 O GLU B 130 ? O GLU B 123 
AA8 1 2 N PHE B 157 ? N PHE B 150 O VAL B 164 ? O VAL B 157 
# 
_pdbx_entry_details.entry_id                   9HTH 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    308 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    309 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
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 ALA A 1 ? ? -175.46 -167.55 
2 1 ALA B 1 ? ? -171.70 -170.62 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -5.6420  6.6081  -24.1502 0.2198 ? -0.0130 ? 0.0406  ? 0.1598 ? -0.0093 ? 0.1663 ? 0.8070 ? 
-0.6348 ? -0.3821 ? 0.7237 ? 0.7775  ? 1.0022 ? -0.0539 ? -0.0793 ? -0.0531 ? 0.2161  ? -0.0228 ? 0.0862  ? 0.0181  ? 0.0214  ? 
-0.0002 ? 
2  'X-RAY DIFFRACTION' ? refined -13.2762 9.1900  -41.3390 0.1608 ? 0.0173  ? 0.0181  ? 0.2710 ? -0.0444 ? 0.1987 ? 0.9235 ? 
0.1946  ? 0.5546  ? 0.6218 ? -0.7148 ? 1.5068 ? -0.0792 ? 0.2142  ? -0.0445 ? 0.0113  ? 0.1025  ? 0.1642  ? -0.3291 ? -0.3871 ? 
0.0457  ? 
3  'X-RAY DIFFRACTION' ? refined -4.9854  0.9085  -32.2295 0.2373 ? 0.0185  ? 0.0593  ? 0.1829 ? 0.0216  ? 0.1923 ? 0.5303 ? 
0.2602  ? 0.2400  ? 0.2414 ? 0.4352  ? 0.6554 ? -0.0400 ? -0.0187 ? -0.2132 ? 0.1805  ? -0.0551 ? 0.1035  ? 0.1638  ? -0.0833 ? 
-0.0027 ? 
4  'X-RAY DIFFRACTION' ? refined -2.1099  -3.2758 -40.2576 0.2053 ? -0.0196 ? 0.0293  ? 0.1896 ? -0.0493 ? 0.2524 ? 0.2885 ? 
-0.3215 ? -0.0375 ? 0.3885 ? 0.1408  ? 0.1597 ? 0.0134  ? 0.1613  ? -0.3533 ? 0.1455  ? -0.0918 ? 0.0952  ? 0.2442  ? 0.0637  ? 
-0.0096 ? 
5  'X-RAY DIFFRACTION' ? refined -6.0349  -8.0366 -47.0344 0.2875 ? 0.0075  ? -0.0142 ? 0.2557 ? -0.1245 ? 0.2974 ? 1.3060 ? 
0.8422  ? -1.0665 ? 0.5974 ? -0.7016 ? 2.0152 ? 0.0003  ? 0.0825  ? -0.6453 ? -0.0959 ? -0.3650 ? 0.3713  ? 0.3717  ? -0.0629 ? 
-0.5237 ? 
6  'X-RAY DIFFRACTION' ? refined -1.9653  9.7866  -49.8379 0.4076 ? 0.0664  ? 0.0192  ? 0.2547 ? -0.0332 ? 0.2759 ? 0.1410 ? 
0.1549  ? -0.0722 ? 0.3372 ? -0.3293 ? 0.4124 ? 0.2519  ? 0.1331  ? 0.2855  ? -0.7038 ? -0.3917 ? 0.1021  ? -0.6167 ? -0.0534 ? 
-0.0171 ? 
7  'X-RAY DIFFRACTION' ? refined 2.9909   -3.1209 -45.7485 0.2168 ? 0.0564  ? 0.0127  ? 0.2601 ? -0.0220 ? 0.2247 ? 0.1250 ? 
-0.0930 ? -0.1719 ? 0.0863 ? 0.0616  ? 0.2822 ? -0.1409 ? 0.0752  ? -0.1755 ? 0.0932  ? 0.0031  ? -0.1375 ? 0.1866  ? 0.1017  ? 
-0.0003 ? 
8  'X-RAY DIFFRACTION' ? refined -5.8183  1.2358  -31.8638 0.1868 ? 0.0163  ? 0.0443  ? 0.2133 ? -0.0331 ? 0.1950 ? 0.5307 ? 
0.0034  ? 0.0982  ? 0.6358 ? -0.0506 ? 0.6295 ? -0.1646 ? -0.1738 ? -0.1009 ? 0.2596  ? -0.0627 ? 0.1205  ? 0.0245  ? -0.1689 ? 
-0.1624 ? 
9  'X-RAY DIFFRACTION' ? refined -12.0428 1.3812  -32.4721 0.2553 ? -0.0588 ? 0.0832  ? 0.5221 ? -0.0405 ? 0.2110 ? 0.0811 ? 
-0.1873 ? 0.0568  ? 0.5093 ? -0.0159 ? 0.1463 ? 0.1910  ? -0.6337 ? -0.0565 ? 0.4893  ? -0.1970 ? 0.1774  ? -0.1728 ? -0.4050 ? 
-0.0035 ? 
10 'X-RAY DIFFRACTION' ? refined 8.9897   -2.6338 -78.9833 0.1728 ? 0.0021  ? -0.0014 ? 0.1815 ? 0.0060  ? 0.2287 ? 0.4422 ? 
0.3384  ? 0.0496  ? 0.3619 ? 0.2859  ? 0.5054 ? -0.0881 ? 0.0852  ? 0.1881  ? -0.2592 ? 0.2165  ? 0.1239  ? -0.0065 ? -0.1548 ? 
0.0002  ? 
11 'X-RAY DIFFRACTION' ? refined 5.5758   -5.8930 -88.5586 0.2076 ? -0.0305 ? -0.0148 ? 0.1300 ? -0.0011 ? 0.1634 ? 0.5522 ? 
0.0573  ? -0.1838 ? 0.4849 ? 0.4858  ? 0.5218 ? -0.0511 ? 0.1667  ? 0.0101  ? -0.2897 ? 0.0511  ? 0.0225  ? -0.0016 ? 0.1212  ? 
-0.0022 ? 
12 'X-RAY DIFFRACTION' ? refined 6.1601   1.4367  -72.0547 0.1248 ? 0.0111  ? -0.0158 ? 0.1250 ? -0.0253 ? 0.1469 ? 0.5275 ? 
0.1908  ? -0.0959 ? 1.1395 ? 0.2851  ? 1.5862 ? -0.0249 ? -0.0824 ? 0.0980  ? -0.0425 ? 0.0636  ? 0.0857  ? -0.1131 ? -0.0176 ? 
-0.0002 ? 
13 'X-RAY DIFFRACTION' ? refined 12.8367  2.0336  -61.7703 0.1968 ? -0.0066 ? -0.0030 ? 0.2665 ? -0.0711 ? 0.2358 ? 0.6391 ? 
0.2961  ? 0.2812  ? 0.1593 ? 0.2247  ? 0.5738 ? 0.0597  ? -0.4499 ? -0.0412 ? 0.0935  ? -0.0628 ? -0.3390 ? 0.0376  ? 0.2892  ? 
-0.0242 ? 
14 'X-RAY DIFFRACTION' ? refined 6.8508   0.0775  -78.2572 0.1825 ? -0.0284 ? -0.0176 ? 0.1473 ? -0.0322 ? 0.1707 ? 0.5971 ? 
-0.1250 ? 0.0739  ? 0.5389 ? 0.5687  ? 0.5558 ? -0.1094 ? -0.0190 ? 0.0662  ? -0.2142 ? 0.0878  ? 0.0981  ? -0.1518 ? -0.0289 ? 
0.0010  ? 
15 'X-RAY DIFFRACTION' ? refined 0.5747   0.0714  -77.5278 0.2219 ? 0.0430  ? -0.1036 ? 0.3005 ? -0.0843 ? 0.2408 ? 0.1683 ? 
0.2278  ? -0.0516 ? 0.4297 ? 0.0598  ? 0.1156 ? 0.1075  ? 0.3308  ? -0.3548 ? -0.4000 ? -0.0380 ? 0.2984  ? 0.0063  ? -0.0889 ? 
-0.0411 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 6 through 47 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 48 through 62 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 63 through 85 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 86 through 102 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 103 through 119 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 120 through 130 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 131 through 141 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 142 through 161 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 162 through 166 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 3 through 18 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 19 through 47 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 48 through 113 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 114 through 141 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 142 through 161 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 162 through 166 )
;
# 
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 ILE -3 ? A ILE 1 
2 1 Y 1 A ASP -2 ? A ASP 2 
3 1 Y 1 A THR -1 ? A THR 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  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
THR N    N N N 290 
THR CA   C N S 291 
THR C    C N N 292 
THR O    O N N 293 
THR CB   C N R 294 
THR OG1  O N N 295 
THR CG2  C N N 296 
THR OXT  O N N 297 
THR H    H N N 298 
THR H2   H N N 299 
THR HA   H N N 300 
THR HB   H N N 301 
THR HG1  H N N 302 
THR HG21 H N N 303 
THR HG22 H N N 304 
THR HG23 H N N 305 
THR HXT  H N N 306 
TRP N    N N N 307 
TRP CA   C N S 308 
TRP C    C N N 309 
TRP O    O N N 310 
TRP CB   C N N 311 
TRP CG   C Y N 312 
TRP CD1  C Y N 313 
TRP CD2  C Y N 314 
TRP NE1  N Y N 315 
TRP CE2  C Y N 316 
TRP CE3  C Y N 317 
TRP CZ2  C Y N 318 
TRP CZ3  C Y N 319 
TRP CH2  C Y N 320 
TRP OXT  O N N 321 
TRP H    H N N 322 
TRP H2   H N N 323 
TRP HA   H N N 324 
TRP HB2  H N N 325 
TRP HB3  H N N 326 
TRP HD1  H N N 327 
TRP HE1  H N N 328 
TRP HE3  H N N 329 
TRP HZ2  H N N 330 
TRP HZ3  H N N 331 
TRP HH2  H N N 332 
TRP HXT  H N N 333 
TYR N    N N N 334 
TYR CA   C N S 335 
TYR C    C N N 336 
TYR O    O N N 337 
TYR CB   C N N 338 
TYR CG   C Y N 339 
TYR CD1  C Y N 340 
TYR CD2  C Y N 341 
TYR CE1  C Y N 342 
TYR CE2  C Y N 343 
TYR CZ   C Y N 344 
TYR OH   O N N 345 
TYR OXT  O N N 346 
TYR H    H N N 347 
TYR H2   H N N 348 
TYR HA   H N N 349 
TYR HB2  H N N 350 
TYR HB3  H N N 351 
TYR HD1  H N N 352 
TYR HD2  H N N 353 
TYR HE1  H N N 354 
TYR HE2  H N N 355 
TYR HH   H N N 356 
TYR HXT  H N N 357 
VAL N    N N N 358 
VAL CA   C N S 359 
VAL C    C N N 360 
VAL O    O N N 361 
VAL CB   C N N 362 
VAL CG1  C N N 363 
VAL CG2  C N N 364 
VAL OXT  O N N 365 
VAL H    H N N 366 
VAL H2   H N N 367 
VAL HA   H N N 368 
VAL HB   H N N 369 
VAL HG11 H N N 370 
VAL HG12 H N N 371 
VAL HG13 H N N 372 
VAL HG21 H N N 373 
VAL HG22 H N N 374 
VAL HG23 H N N 375 
VAL HXT  H N N 376 
# 
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  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           'DFG MO1073/9-1' 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          Phyre2 
# 
_atom_sites.entry_id                    9HTH 
_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]   0.033191 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015870 
_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]   0.006157 
_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   . ASP A 1 4   ? -6.888  -5.946  -28.436  1.00 62.54 ? 0   ASP A N   1 
ATOM   2    C CA  . ASP A 1 4   ? -6.189  -5.664  -29.689  1.00 61.88 ? 0   ASP A CA  1 
ATOM   3    C C   . ASP A 1 4   ? -6.019  -4.153  -29.865  1.00 57.22 ? 0   ASP A C   1 
ATOM   4    O O   . ASP A 1 4   ? -6.932  -3.399  -29.521  1.00 58.77 ? 0   ASP A O   1 
ATOM   5    C CB  . ASP A 1 4   ? -6.949  -6.282  -30.869  1.00 63.99 ? 0   ASP A CB  1 
ATOM   6    C CG  . ASP A 1 4   ? -8.297  -5.622  -31.119  1.00 65.91 ? 0   ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 4   ? -8.330  -4.495  -31.656  1.00 66.04 ? 0   ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 4   ? -9.332  -6.241  -30.794  1.00 68.80 ? 0   ASP A OD2 1 
ATOM   9    N N   . ALA A 1 5   ? -4.866  -3.713  -30.381  1.00 46.18 ? 1   ALA A N   1 
ATOM   10   C CA  . ALA A 1 5   ? -4.573  -2.281  -30.480  1.00 39.38 ? 1   ALA A CA  1 
ATOM   11   C C   . ALA A 1 5   ? -3.236  -2.056  -31.211  1.00 31.66 ? 1   ALA A C   1 
ATOM   12   O O   . ALA A 1 5   ? -2.678  -2.972  -31.824  1.00 30.70 ? 1   ALA A O   1 
ATOM   13   C CB  . ALA A 1 5   ? -4.579  -1.680  -29.078  1.00 43.75 ? 1   ALA A CB  1 
ATOM   14   N N   . VAL A 1 6   ? -2.727  -0.810  -31.139  1.00 20.40 ? 2   VAL A N   1 
ATOM   15   C CA  . VAL A 1 6   ? -1.411  -0.404  -31.633  1.00 17.81 ? 2   VAL A CA  1 
ATOM   16   C C   . VAL A 1 6   ? -0.546  0.019   -30.446  1.00 17.97 ? 2   VAL A C   1 
ATOM   17   O O   . VAL A 1 6   ? -1.042  0.348   -29.362  1.00 17.16 ? 2   VAL A O   1 
ATOM   18   C CB  . VAL A 1 6   ? -1.441  0.771   -32.645  1.00 18.63 ? 2   VAL A CB  1 
ATOM   19   C CG1 . VAL A 1 6   ? -2.152  0.419   -33.918  1.00 23.57 ? 2   VAL A CG1 1 
ATOM   20   C CG2 . VAL A 1 6   ? -2.047  2.039   -32.030  1.00 18.34 ? 2   VAL A CG2 1 
ATOM   21   N N   . VAL A 1 7   ? 0.774   0.073   -30.681  1.00 15.10 ? 3   VAL A N   1 
ATOM   22   C CA  . VAL A 1 7   ? 1.686   0.448   -29.582  1.00 16.86 ? 3   VAL A CA  1 
ATOM   23   C C   . VAL A 1 7   ? 1.592   1.949   -29.292  1.00 16.81 ? 3   VAL A C   1 
ATOM   24   O O   . VAL A 1 7   ? 1.152   2.763   -30.121  1.00 16.35 ? 3   VAL A O   1 
ATOM   25   C CB  . VAL A 1 7   ? 3.138   0.022   -29.867  1.00 17.98 ? 3   VAL A CB  1 
ATOM   26   C CG1 . VAL A 1 7   ? 3.232   -1.489  -30.081  1.00 20.17 ? 3   VAL A CG1 1 
ATOM   27   C CG2 . VAL A 1 7   ? 3.697   0.772   -31.058  1.00 19.54 ? 3   VAL A CG2 1 
ATOM   28   N N   . GLY A 1 8   ? 2.040   2.329   -28.090  1.00 19.06 ? 4   GLY A N   1 
ATOM   29   C CA  . GLY A 1 8   ? 1.841   3.694   -27.630  1.00 16.81 ? 4   GLY A CA  1 
ATOM   30   C C   . GLY A 1 8   ? 2.609   4.752   -28.399  1.00 16.60 ? 4   GLY A C   1 
ATOM   31   O O   . GLY A 1 8   ? 2.178   5.909   -28.450  1.00 17.69 ? 4   GLY A O   1 
ATOM   32   N N   . ASP A 1 9   ? 3.727   4.383   -29.033  1.00 18.55 ? 5   ASP A N   1 
ATOM   33   C CA  . ASP A 1 9   ? 4.507   5.367   -29.772  1.00 18.43 ? 5   ASP A CA  1 
ATOM   34   C C   . ASP A 1 9   ? 3.942   5.655   -31.164  1.00 19.48 ? 5   ASP A C   1 
ATOM   35   O O   . ASP A 1 9   ? 4.499   6.494   -31.884  1.00 19.73 ? 5   ASP A O   1 
ATOM   36   C CB  . ASP A 1 9   ? 5.974   4.931   -29.878  1.00 26.25 ? 5   ASP A CB  1 
ATOM   37   C CG  . ASP A 1 9   ? 6.716   5.046   -28.553  1.00 42.75 ? 5   ASP A CG  1 
ATOM   38   O OD1 . ASP A 1 9   ? 6.262   5.809   -27.674  1.00 44.49 ? 5   ASP A OD1 1 
ATOM   39   O OD2 . ASP A 1 9   ? 7.760   4.378   -28.396  1.00 51.14 ? 5   ASP A OD2 1 
ATOM   40   N N   . THR A 1 10  ? 2.846   5.000   -31.552  1.00 16.88 ? 6   THR A N   1 
ATOM   41   C CA  . THR A 1 10  ? 2.258   5.216   -32.867  1.00 16.43 ? 6   THR A CA  1 
ATOM   42   C C   . THR A 1 10  ? 1.789   6.661   -32.991  1.00 17.06 ? 6   THR A C   1 
ATOM   43   O O   . THR A 1 10  ? 1.053   7.153   -32.138  1.00 15.85 ? 6   THR A O   1 
ATOM   44   C CB  . THR A 1 10  ? 1.058   4.291   -33.004  1.00 14.80 ? 6   THR A CB  1 
ATOM   45   O OG1 . THR A 1 10  ? 1.472   2.931   -32.829  1.00 16.74 ? 6   THR A OG1 1 
ATOM   46   C CG2 . THR A 1 10  ? 0.429   4.427   -34.359  1.00 17.05 ? 6   THR A CG2 1 
ATOM   47   N N   . ILE A 1 11  ? 2.176   7.330   -34.064  1.00 15.76 ? 7   ILE A N   1 
ATOM   48   C CA  . ILE A 1 11  ? 1.767   8.711   -34.274  1.00 15.61 ? 7   ILE A CA  1 
ATOM   49   C C   . ILE A 1 11  ? 0.382   8.739   -34.904  1.00 15.64 ? 7   ILE A C   1 
ATOM   50   O O   . ILE A 1 11  ? 0.123   8.036   -35.896  1.00 16.47 ? 7   ILE A O   1 
ATOM   51   C CB  . ILE A 1 11  ? 2.780   9.447   -35.166  1.00 17.03 ? 7   ILE A CB  1 
ATOM   52   C CG1 . ILE A 1 11  ? 4.118   9.564   -34.445  1.00 19.91 ? 7   ILE A CG1 1 
ATOM   53   C CG2 . ILE A 1 11  ? 2.255   10.812  -35.581  1.00 20.76 ? 7   ILE A CG2 1 
ATOM   54   C CD1 . ILE A 1 11  ? 4.148   10.638  -33.369  1.00 21.28 ? 7   ILE A CD1 1 
ATOM   55   N N   . ILE A 1 12  ? -0.495  9.574   -34.352  1.00 15.82 ? 8   ILE A N   1 
ATOM   56   C CA  . ILE A 1 12  ? -1.843  9.764   -34.869  1.00 15.20 ? 8   ILE A CA  1 
ATOM   57   C C   . ILE A 1 12  ? -2.129  11.249  -35.058  1.00 15.15 ? 8   ILE A C   1 
ATOM   58   O O   . ILE A 1 12  ? -1.481  12.117  -34.458  1.00 16.99 ? 8   ILE A O   1 
ATOM   59   C CB  . ILE A 1 12  ? -2.907  9.127   -33.956  1.00 14.57 ? 8   ILE A CB  1 
ATOM   60   C CG1 . ILE A 1 12  ? -2.894  9.761   -32.559  1.00 15.53 ? 8   ILE A CG1 1 
ATOM   61   C CG2 . ILE A 1 12  ? -2.701  7.611   -33.878  1.00 15.81 ? 8   ILE A CG2 1 
ATOM   62   C CD1 . ILE A 1 12  ? -4.158  9.444   -31.743  1.00 18.49 ? 8   ILE A CD1 1 
ATOM   63   N N   . ASP A 1 13  ? -3.133  11.523  -35.893  1.00 17.45 ? 9   ASP A N   1 
ATOM   64   C CA  . ASP A 1 13  ? -3.668  12.864  -36.085  1.00 16.85 ? 9   ASP A CA  1 
ATOM   65   C C   . ASP A 1 13  ? -4.719  13.119  -35.012  1.00 16.36 ? 9   ASP A C   1 
ATOM   66   O O   . ASP A 1 13  ? -5.653  12.325  -34.826  1.00 19.26 ? 9   ASP A O   1 
ATOM   67   C CB  . ASP A 1 13  ? -4.309  12.948  -37.479  1.00 19.52 ? 9   ASP A CB  1 
ATOM   68   C CG  . ASP A 1 13  ? -5.030  14.272  -37.743  1.00 20.94 ? 9   ASP A CG  1 
ATOM   69   O OD1 . ASP A 1 13  ? -6.016  14.606  -37.053  1.00 20.70 ? 9   ASP A OD1 1 
ATOM   70   O OD2 . ASP A 1 13  ? -4.641  14.953  -38.713  1.00 26.37 ? 9   ASP A OD2 1 
ATOM   71   N N   . VAL A 1 14  ? -4.572  14.225  -34.289  1.00 16.06 ? 10  VAL A N   1 
ATOM   72   C CA  . VAL A 1 14  ? -5.602  14.696  -33.370  1.00 18.25 ? 10  VAL A CA  1 
ATOM   73   C C   . VAL A 1 14  ? -5.904  16.125  -33.794  1.00 19.93 ? 10  VAL A C   1 
ATOM   74   O O   . VAL A 1 14  ? -5.092  17.032  -33.576  1.00 19.11 ? 10  VAL A O   1 
ATOM   75   C CB  . VAL A 1 14  ? -5.155  14.619  -31.910  1.00 15.20 ? 10  VAL A CB  1 
ATOM   76   C CG1 . VAL A 1 14  ? -6.233  15.159  -30.995  1.00 19.16 ? 10  VAL A CG1 1 
ATOM   77   C CG2 . VAL A 1 14  ? -4.817  13.174  -31.522  1.00 20.42 ? 10  VAL A CG2 1 
ATOM   78   N N   . SER A 1 15  ? -7.049  16.320  -34.448  1.00 20.16 ? 11  SER A N   1 
ATOM   79   C CA  . SER A 1 15  ? -7.460  17.636  -34.946  1.00 19.26 ? 11  SER A CA  1 
ATOM   80   C C   . SER A 1 15  ? -6.359  18.306  -35.777  1.00 20.94 ? 11  SER A C   1 
ATOM   81   O O   . SER A 1 15  ? -6.149  19.521  -35.712  1.00 26.45 ? 11  SER A O   1 
ATOM   82   C CB  . SER A 1 15  ? -7.969  18.539  -33.819  1.00 22.62 ? 11  SER A CB  1 
ATOM   83   O OG  . SER A 1 15  ? -9.034  17.917  -33.106  1.00 25.10 ? 11  SER A OG  1 
ATOM   84   N N   . GLY A 1 16  ? -5.643  17.511  -36.568  1.00 19.36 ? 12  GLY A N   1 
ATOM   85   C CA  . GLY A 1 16  ? -4.635  18.045  -37.468  1.00 19.65 ? 12  GLY A CA  1 
ATOM   86   C C   . GLY A 1 16  ? -3.240  18.139  -36.885  1.00 22.97 ? 12  GLY A C   1 
ATOM   87   O O   . GLY A 1 16  ? -2.277  18.320  -37.647  1.00 25.84 ? 12  GLY A O   1 
ATOM   88   N N   . LYS A 1 17  ? -3.098  17.995  -35.576  1.00 18.89 ? 13  LYS A N   1 
ATOM   89   C CA  . LYS A 1 17  ? -1.806  17.962  -34.908  1.00 23.45 ? 13  LYS A CA  1 
ATOM   90   C C   . LYS A 1 17  ? -1.359  16.517  -34.784  1.00 24.23 ? 13  LYS A C   1 
ATOM   91   O O   . LYS A 1 17  ? -2.173  15.589  -34.794  1.00 26.22 ? 13  LYS A O   1 
ATOM   92   C CB  . LYS A 1 17  ? -1.882  18.582  -33.511  1.00 24.11 ? 13  LYS A CB  1 
ATOM   93   C CG  . LYS A 1 17  ? -2.609  19.909  -33.443  1.00 30.24 ? 13  LYS A CG  1 
ATOM   94   C CD  . LYS A 1 17  ? -1.780  21.021  -34.007  1.00 32.19 ? 13  LYS A CD  1 
ATOM   95   C CE  . LYS A 1 17  ? -2.605  22.296  -34.068  1.00 37.68 ? 13  LYS A CE  1 
ATOM   96   N NZ  . LYS A 1 17  ? -3.328  22.557  -32.797  1.00 41.78 ? 13  LYS A NZ  1 
ATOM   97   N N   . LYS A 1 18  ? -0.056  16.328  -34.631  1.00 20.14 ? 14  LYS A N   1 
ATOM   98   C CA  . LYS A 1 18  ? 0.511   14.995  -34.522  1.00 20.35 ? 14  LYS A CA  1 
ATOM   99   C C   . LYS A 1 18  ? 0.996   14.740  -33.103  1.00 20.03 ? 14  LYS A C   1 
ATOM   100  O O   . LYS A 1 18  ? 1.671   15.586  -32.503  1.00 22.77 ? 14  LYS A O   1 
ATOM   101  C CB  . LYS A 1 18  ? 1.658   14.831  -35.516  1.00 19.75 ? 14  LYS A CB  1 
ATOM   102  C CG  . LYS A 1 18  ? 1.222   15.008  -36.969  1.00 23.90 ? 14  LYS A CG  1 
ATOM   103  C CD  . LYS A 1 18  ? 0.215   13.951  -37.371  1.00 30.17 ? 14  LYS A CD  1 
ATOM   104  C CE  . LYS A 1 18  ? -0.229  14.131  -38.813  1.00 41.49 ? 14  LYS A CE  1 
ATOM   105  N NZ  . LYS A 1 18  ? -0.906  15.440  -39.024  1.00 46.50 ? 14  LYS A NZ  1 
ATOM   106  N N   . MET A 1 19  ? 0.666   13.568  -32.569  1.00 18.41 ? 15  MET A N   1 
ATOM   107  C CA  . MET A 1 19  ? 1.170   13.154  -31.267  1.00 19.31 ? 15  MET A CA  1 
ATOM   108  C C   . MET A 1 19  ? 1.096   11.637  -31.214  1.00 16.97 ? 15  MET A C   1 
ATOM   109  O O   . MET A 1 19  ? 0.403   11.013  -32.016  1.00 17.08 ? 15  MET A O   1 
ATOM   110  C CB  . MET A 1 19  ? 0.372   13.800  -30.131  1.00 24.29 ? 15  MET A CB  1 
ATOM   111  C CG  . MET A 1 19  ? -1.101  13.438  -30.105  1.00 21.86 ? 15  MET A CG  1 
ATOM   112  S SD  . MET A 1 19  ? -2.132  14.496  -29.015  1.00 28.57 ? 15  MET A SD  1 
ATOM   113  C CE  . MET A 1 19  ? -1.102  14.644  -27.562  1.00 34.14 ? 15  MET A CE  1 
ATOM   114  N N   . THR A 1 20  ? 1.841   11.037  -30.294  1.00 17.02 ? 16  THR A N   1 
ATOM   115  C CA  . THR A 1 20  ? 1.685   9.595   -30.139  1.00 16.19 ? 16  THR A CA  1 
ATOM   116  C C   . THR A 1 20  ? 0.345   9.294   -29.483  1.00 15.10 ? 16  THR A C   1 
ATOM   117  O O   . THR A 1 20  ? -0.229  10.130  -28.775  1.00 15.92 ? 16  THR A O   1 
ATOM   118  C CB  . THR A 1 20  ? 2.808   8.970   -29.313  1.00 17.40 ? 16  THR A CB  1 
ATOM   119  O OG1 . THR A 1 20  ? 2.639   9.315   -27.929  1.00 19.50 ? 16  THR A OG1 1 
ATOM   120  C CG2 . THR A 1 20  ? 4.195   9.411   -29.818  1.00 19.80 ? 16  THR A CG2 1 
ATOM   121  N N   . ILE A 1 21  ? -0.167  8.092   -29.737  1.00 14.78 ? 17  ILE A N   1 
ATOM   122  C CA  . ILE A 1 21  ? -1.457  7.732   -29.160  1.00 15.10 ? 17  ILE A CA  1 
ATOM   123  C C   . ILE A 1 21  ? -1.371  7.673   -27.639  1.00 14.70 ? 17  ILE A C   1 
ATOM   124  O O   . ILE A 1 21  ? -2.331  8.031   -26.943  1.00 16.07 ? 17  ILE A O   1 
ATOM   125  C CB  . ILE A 1 21  ? -2.035  6.466   -29.837  1.00 13.57 ? 17  ILE A CB  1 
ATOM   126  C CG1 . ILE A 1 21  ? -3.482  6.224   -29.426  1.00 15.19 ? 17  ILE A CG1 1 
ATOM   127  C CG2 . ILE A 1 21  ? -1.159  5.242   -29.579  1.00 15.87 ? 17  ILE A CG2 1 
ATOM   128  C CD1 . ILE A 1 21  ? -4.168  5.157   -30.324  1.00 16.23 ? 17  ILE A CD1 1 
ATOM   129  N N   . ALA A 1 22  ? -0.222  7.257   -27.098  1.00 15.36 ? 18  ALA A N   1 
ATOM   130  C CA  . ALA A 1 22  ? -0.034  7.291   -25.644  1.00 15.87 ? 18  ALA A CA  1 
ATOM   131  C C   . ALA A 1 22  ? -0.069  8.718   -25.103  1.00 17.32 ? 18  ALA A C   1 
ATOM   132  O O   . ALA A 1 22  ? -0.666  8.972   -24.042  1.00 17.77 ? 18  ALA A O   1 
ATOM   133  C CB  . ALA A 1 22  ? 1.272   6.598   -25.255  1.00 17.75 ? 18  ALA A CB  1 
ATOM   134  N N   . GLU A 1 23  ? 0.607   9.651   -25.786  1.00 17.84 ? 19  GLU A N   1 
ATOM   135  C CA  . GLU A 1 23  ? 0.546   11.053  -25.377  1.00 19.30 ? 19  GLU A CA  1 
ATOM   136  C C   . GLU A 1 23  ? -0.881  11.564  -25.421  1.00 17.73 ? 19  GLU A C   1 
ATOM   137  O O   . GLU A 1 23  ? -1.309  12.299  -24.524  1.00 19.44 ? 19  GLU A O   1 
ATOM   138  C CB  . GLU A 1 23  ? 1.406   11.911  -26.305  1.00 21.55 ? 19  GLU A CB  1 
ATOM   139  C CG  . GLU A 1 23  ? 2.906   11.771  -26.076  1.00 27.68 ? 19  GLU A CG  1 
ATOM   140  C CD  . GLU A 1 23  ? 3.756   12.361  -27.202  1.00 35.18 ? 19  GLU A CD  1 
ATOM   141  O OE1 . GLU A 1 23  ? 3.210   12.737  -28.273  1.00 27.67 ? 19  GLU A OE1 1 
ATOM   142  O OE2 . GLU A 1 23  ? 4.991   12.432  -27.010  1.00 42.06 ? 19  GLU A OE2 1 
ATOM   143  N N   . PHE A 1 24  ? -1.641  11.175  -26.451  1.00 16.97 ? 20  PHE A N   1 
ATOM   144  C CA  . PHE A 1 24  ? -3.033  11.596  -26.549  1.00 16.58 ? 20  PHE A CA  1 
ATOM   145  C C   . PHE A 1 24  ? -3.848  11.029  -25.384  1.00 18.16 ? 20  PHE A C   1 
ATOM   146  O O   . PHE A 1 24  ? -4.597  11.756  -24.720  1.00 17.96 ? 20  PHE A O   1 
ATOM   147  C CB  . PHE A 1 24  ? -3.615  11.163  -27.903  1.00 17.66 ? 20  PHE A CB  1 
ATOM   148  C CG  . PHE A 1 24  ? -5.062  11.537  -28.077  1.00 15.71 ? 20  PHE A CG  1 
ATOM   149  C CD1 . PHE A 1 24  ? -5.497  12.819  -27.774  1.00 18.97 ? 20  PHE A CD1 1 
ATOM   150  C CD2 . PHE A 1 24  ? -5.998  10.610  -28.489  1.00 20.01 ? 20  PHE A CD2 1 
ATOM   151  C CE1 . PHE A 1 24  ? -6.825  13.170  -27.901  1.00 19.58 ? 20  PHE A CE1 1 
ATOM   152  C CE2 . PHE A 1 24  ? -7.340  10.957  -28.611  1.00 23.90 ? 20  PHE A CE2 1 
ATOM   153  C CZ  . PHE A 1 24  ? -7.745  12.242  -28.309  1.00 20.91 ? 20  PHE A CZ  1 
ATOM   154  N N   . TYR A 1 25  ? -3.683  9.735   -25.095  1.00 15.59 ? 21  TYR A N   1 
ATOM   155  C CA  . TYR A 1 25  ? -4.339  9.143   -23.935  1.00 16.60 ? 21  TYR A CA  1 
ATOM   156  C C   . TYR A 1 25  ? -3.997  9.909   -22.656  1.00 17.06 ? 21  TYR A C   1 
ATOM   157  O O   . TYR A 1 25  ? -4.887  10.239  -21.860  1.00 18.12 ? 21  TYR A O   1 
ATOM   158  C CB  . TYR A 1 25  ? -3.968  7.663   -23.805  1.00 18.80 ? 21  TYR A CB  1 
ATOM   159  C CG  . TYR A 1 25  ? -4.612  7.031   -22.584  1.00 17.99 ? 21  TYR A CG  1 
ATOM   160  C CD1 . TYR A 1 25  ? -3.973  7.049   -21.349  1.00 18.32 ? 21  TYR A CD1 1 
ATOM   161  C CD2 . TYR A 1 25  ? -5.878  6.450   -22.651  1.00 18.09 ? 21  TYR A CD2 1 
ATOM   162  C CE1 . TYR A 1 25  ? -4.573  6.505   -20.227  1.00 19.87 ? 21  TYR A CE1 1 
ATOM   163  C CE2 . TYR A 1 25  ? -6.488  5.901   -21.523  1.00 18.66 ? 21  TYR A CE2 1 
ATOM   164  C CZ  . TYR A 1 25  ? -5.827  5.933   -20.318  1.00 17.75 ? 21  TYR A CZ  1 
ATOM   165  O OH  . TYR A 1 25  ? -6.430  5.388   -19.187  1.00 20.82 ? 21  TYR A OH  1 
ATOM   166  N N   . ASP A 1 26  ? -2.714  10.194  -22.441  1.00 17.41 ? 22  ASP A N   1 
ATOM   167  C CA  . ASP A 1 26  ? -2.312  10.860  -21.198  1.00 20.24 ? 22  ASP A CA  1 
ATOM   168  C C   . ASP A 1 26  ? -2.875  12.272  -21.099  1.00 20.79 ? 22  ASP A C   1 
ATOM   169  O O   . ASP A 1 26  ? -3.096  12.773  -19.987  1.00 22.91 ? 22  ASP A O   1 
ATOM   170  C CB  . ASP A 1 26  ? -0.789  10.907  -21.092  1.00 21.03 ? 22  ASP A CB  1 
ATOM   171  C CG  . ASP A 1 26  ? -0.168  9.541   -20.890  1.00 26.80 ? 22  ASP A CG  1 
ATOM   172  O OD1 . ASP A 1 26  ? -0.893  8.597   -20.512  1.00 26.99 ? 22  ASP A OD1 1 
ATOM   173  O OD2 . ASP A 1 26  ? 1.063   9.421   -21.092  1.00 30.19 ? 22  ASP A OD2 1 
ATOM   174  N N   . SER A 1 27  ? -3.047  12.944  -22.231  1.00 21.13 ? 23  SER A N   1 
ATOM   175  C CA  . SER A 1 27  ? -3.571  14.299  -22.313  1.00 22.02 ? 23  SER A CA  1 
ATOM   176  C C   . SER A 1 27  ? -5.084  14.366  -22.159  1.00 21.01 ? 23  SER A C   1 
ATOM   177  O O   . SER A 1 27  ? -5.630  15.470  -22.006  1.00 23.52 ? 23  SER A O   1 
ATOM   178  C CB  . SER A 1 27  ? -3.195  14.906  -23.667  1.00 25.20 ? 23  SER A CB  1 
ATOM   179  O OG  . SER A 1 27  ? -4.112  14.514  -24.678  1.00 24.88 ? 23  SER A OG  1 
ATOM   180  N N   . THR A 1 28  ? -5.773  13.235  -22.254  1.00 19.21 ? 24  THR A N   1 
ATOM   181  C CA  . THR A 1 28  ? -7.227  13.200  -22.205  1.00 20.37 ? 24  THR A CA  1 
ATOM   182  C C   . THR A 1 28  ? -7.689  13.208  -20.751  1.00 20.06 ? 24  THR A C   1 
ATOM   183  O O   . THR A 1 28  ? -7.158  12.445  -19.932  1.00 20.78 ? 24  THR A O   1 
ATOM   184  C CB  . THR A 1 28  ? -7.732  11.945  -22.922  1.00 18.70 ? 24  THR A CB  1 
ATOM   185  O OG1 . THR A 1 28  ? -7.369  12.027  -24.300  1.00 19.06 ? 24  THR A OG1 1 
ATOM   186  C CG2 . THR A 1 28  ? -9.232  11.809  -22.842  1.00 20.01 ? 24  THR A CG2 1 
ATOM   187  N N   . PRO A 1 29  ? -8.640  14.071  -20.386  1.00 21.81 ? 25  PRO A N   1 
ATOM   188  C CA  . PRO A 1 29  ? -9.122  14.090  -18.999  1.00 21.07 ? 25  PRO A CA  1 
ATOM   189  C C   . PRO A 1 29  ? -9.671  12.733  -18.578  1.00 21.44 ? 25  PRO A C   1 
ATOM   190  O O   . PRO A 1 29  ? -10.134 11.943  -19.406  1.00 21.02 ? 25  PRO A O   1 
ATOM   191  C CB  . PRO A 1 29  ? -10.220 15.158  -19.030  1.00 24.87 ? 25  PRO A CB  1 
ATOM   192  C CG  . PRO A 1 29  ? -9.774  16.104  -20.105  1.00 25.23 ? 25  PRO A CG  1 
ATOM   193  C CD  . PRO A 1 29  ? -9.173  15.199  -21.171  1.00 20.64 ? 25  PRO A CD  1 
ATOM   194  N N   . ASP A 1 30  ? -9.598  12.476  -17.266  1.00 20.69 ? 26  ASP A N   1 
ATOM   195  C CA  . ASP A 1 30  ? -9.918  11.184  -16.643  1.00 21.27 ? 26  ASP A CA  1 
ATOM   196  C C   . ASP A 1 30  ? -11.433 10.973  -16.502  1.00 19.80 ? 26  ASP A C   1 
ATOM   197  O O   . ASP A 1 30  ? -11.973 10.748  -15.418  1.00 22.39 ? 26  ASP A O   1 
ATOM   198  C CB  . ASP A 1 30  ? -9.221  11.069  -15.290  1.00 23.36 ? 26  ASP A CB  1 
ATOM   199  C CG  . ASP A 1 30  ? -7.731  10.773  -15.412  1.00 24.55 ? 26  ASP A CG  1 
ATOM   200  O OD1 . ASP A 1 30  ? -7.259  10.508  -16.540  1.00 26.21 ? 26  ASP A OD1 1 
ATOM   201  O OD2 . ASP A 1 30  ? -7.018  10.807  -14.379  1.00 27.62 ? 26  ASP A OD2 1 
ATOM   202  N N   . VAL A 1 31  ? -12.111 11.009  -17.644  1.00 19.58 ? 27  VAL A N   1 
ATOM   203  C CA  . VAL A 1 31  ? -13.543 10.740  -17.729  1.00 20.82 ? 27  VAL A CA  1 
ATOM   204  C C   . VAL A 1 31  ? -13.649 9.281   -18.158  1.00 20.78 ? 27  VAL A C   1 
ATOM   205  O O   . VAL A 1 31  ? -13.648 8.964   -19.344  1.00 19.62 ? 27  VAL A O   1 
ATOM   206  C CB  . VAL A 1 31  ? -14.225 11.681  -18.720  1.00 22.02 ? 27  VAL A CB  1 
ATOM   207  C CG1 . VAL A 1 31  ? -15.696 11.326  -18.892  1.00 23.50 ? 27  VAL A CG1 1 
ATOM   208  C CG2 . VAL A 1 31  ? -14.063 13.116  -18.276  1.00 23.49 ? 27  VAL A CG2 1 
ATOM   209  N N   . PHE A 1 32  ? -13.674 8.368   -17.193  1.00 19.80 ? 28  PHE A N   1 
ATOM   210  C CA  . PHE A 1 32  ? -13.591 6.941   -17.500  1.00 20.74 ? 28  PHE A CA  1 
ATOM   211  C C   . PHE A 1 32  ? -14.962 6.355   -17.795  1.00 19.47 ? 28  PHE A C   1 
ATOM   212  O O   . PHE A 1 32  ? -15.906 6.531   -17.013  1.00 21.53 ? 28  PHE A O   1 
ATOM   213  C CB  . PHE A 1 32  ? -12.943 6.158   -16.355  1.00 21.13 ? 28  PHE A CB  1 
ATOM   214  C CG  . PHE A 1 32  ? -11.487 6.439   -16.188  1.00 21.55 ? 28  PHE A CG  1 
ATOM   215  C CD1 . PHE A 1 32  ? -10.573 6.018   -17.141  1.00 19.83 ? 28  PHE A CD1 1 
ATOM   216  C CD2 . PHE A 1 32  ? -11.032 7.145   -15.086  1.00 20.95 ? 28  PHE A CD2 1 
ATOM   217  C CE1 . PHE A 1 32  ? -9.226  6.284   -16.985  1.00 19.66 ? 28  PHE A CE1 1 
ATOM   218  C CE2 . PHE A 1 32  ? -9.692  7.421   -14.917  1.00 21.10 ? 28  PHE A CE2 1 
ATOM   219  C CZ  . PHE A 1 32  ? -8.782  6.997   -15.866  1.00 21.13 ? 28  PHE A CZ  1 
ATOM   220  N N   . MET A 1 33  ? -15.060 5.659   -18.926  1.00 20.75 ? 29  MET A N   1 
ATOM   221  C CA  . MET A 1 33  ? -16.180 4.779   -19.235  1.00 21.28 ? 29  MET A CA  1 
ATOM   222  C C   . MET A 1 33  ? -15.948 3.393   -18.687  1.00 21.30 ? 29  MET A C   1 
ATOM   223  O O   . MET A 1 33  ? -16.911 2.671   -18.405  1.00 23.88 ? 29  MET A O   1 
ATOM   224  C CB  . MET A 1 33  ? -16.321 4.631   -20.754  1.00 23.37 ? 29  MET A CB  1 
ATOM   225  C CG  . MET A 1 33  ? -16.471 5.938   -21.479  1.00 26.33 ? 29  MET A CG  1 
ATOM   226  S SD  . MET A 1 33  ? -17.929 6.801   -20.867  1.00 34.41 ? 29  MET A SD  1 
ATOM   227  C CE  . MET A 1 33  ? -19.203 5.616   -21.271  1.00 32.51 ? 29  MET A CE  1 
ATOM   228  N N   . ARG A 1 34  ? -14.687 3.004   -18.557  1.00 22.17 ? 30  ARG A N   1 
ATOM   229  C CA  . ARG A 1 34  ? -14.312 1.724   -17.994  1.00 22.29 ? 30  ARG A CA  1 
ATOM   230  C C   . ARG A 1 34  ? -12.966 1.911   -17.321  1.00 21.39 ? 30  ARG A C   1 
ATOM   231  O O   . ARG A 1 34  ? -12.056 2.529   -17.887  1.00 22.35 ? 30  ARG A O   1 
ATOM   232  C CB  . ARG A 1 34  ? -14.203 0.657   -19.089  1.00 24.16 ? 30  ARG A CB  1 
ATOM   233  C CG  . ARG A 1 34  ? -13.924 -0.732  -18.549  1.00 31.60 ? 30  ARG A CG  1 
ATOM   234  C CD  . ARG A 1 34  ? -13.289 -1.625  -19.595  1.00 41.80 ? 30  ARG A CD  1 
ATOM   235  N NE  . ARG A 1 34  ? -14.172 -1.861  -20.729  1.00 45.57 ? 30  ARG A NE  1 
ATOM   236  C CZ  . ARG A 1 34  ? -13.752 -2.182  -21.950  1.00 44.25 ? 30  ARG A CZ  1 
ATOM   237  N NH1 . ARG A 1 34  ? -12.452 -2.302  -22.207  1.00 44.59 ? 30  ARG A NH1 1 
ATOM   238  N NH2 . ARG A 1 34  ? -14.634 -2.377  -22.921  1.00 48.40 ? 30  ARG A NH2 1 
ATOM   239  N N   . ARG A 1 35  ? -12.836 1.368   -16.116  1.00 23.93 ? 31  ARG A N   1 
ATOM   240  C CA  . ARG A 1 35  ? -11.566 1.445   -15.416  1.00 22.85 ? 31  ARG A CA  1 
ATOM   241  C C   . ARG A 1 35  ? -11.449 0.216   -14.540  1.00 26.31 ? 31  ARG A C   1 
ATOM   242  O O   . ARG A 1 35  ? -12.293 -0.008  -13.666  1.00 26.49 ? 31  ARG A O   1 
ATOM   243  C CB  . ARG A 1 35  ? -11.461 2.716   -14.569  1.00 24.29 ? 31  ARG A CB  1 
ATOM   244  C CG  . ARG A 1 35  ? -10.202 2.721   -13.722  1.00 23.45 ? 31  ARG A CG  1 
ATOM   245  C CD  . ARG A 1 35  ? -9.922  4.058   -13.051  1.00 24.24 ? 31  ARG A CD  1 
ATOM   246  N NE  . ARG A 1 35  ? -8.680  3.974   -12.276  1.00 23.40 ? 31  ARG A NE  1 
ATOM   247  C CZ  . ARG A 1 35  ? -8.159  4.970   -11.578  1.00 25.32 ? 31  ARG A CZ  1 
ATOM   248  N NH1 . ARG A 1 35  ? -8.764  6.145   -11.536  1.00 29.36 ? 31  ARG A NH1 1 
ATOM   249  N NH2 . ARG A 1 35  ? -7.035  4.784   -10.905  1.00 32.22 ? 31  ARG A NH2 1 
ATOM   250  N N   . ASN A 1 36  ? -10.401 -0.568  -14.763  1.00 25.00 ? 32  ASN A N   1 
ATOM   251  C CA  . ASN A 1 36  ? -10.061 -1.680  -13.875  1.00 27.06 ? 32  ASN A CA  1 
ATOM   252  C C   . ASN A 1 36  ? -8.543  -1.682  -13.793  1.00 26.47 ? 32  ASN A C   1 
ATOM   253  O O   . ASN A 1 36  ? -7.865  -2.160  -14.710  1.00 26.48 ? 32  ASN A O   1 
ATOM   254  C CB  . ASN A 1 36  ? -10.605 -3.017  -14.361  1.00 30.34 ? 32  ASN A CB  1 
ATOM   255  C CG  . ASN A 1 36  ? -10.419 -4.123  -13.339  1.00 40.42 ? 32  ASN A CG  1 
ATOM   256  O OD1 . ASN A 1 36  ? -9.301  -4.400  -12.900  1.00 41.81 ? 32  ASN A OD1 1 
ATOM   257  N ND2 . ASN A 1 36  ? -11.520 -4.744  -12.934  1.00 41.87 ? 32  ASN A ND2 1 
ATOM   258  N N   . ASP A 1 37  ? -8.015  -1.085  -12.726  1.00 29.79 ? 33  ASP A N   1 
ATOM   259  C CA  . ASP A 1 37  ? -6.572  -1.009  -12.552  1.00 28.45 ? 33  ASP A CA  1 
ATOM   260  C C   . ASP A 1 37  ? -5.942  -2.391  -12.452  1.00 31.82 ? 33  ASP A C   1 
ATOM   261  O O   . ASP A 1 37  ? -4.810  -2.588  -12.907  1.00 31.29 ? 33  ASP A O   1 
ATOM   262  C CB  . ASP A 1 37  ? -6.244  -0.179  -11.309  1.00 33.70 ? 33  ASP A CB  1 
ATOM   263  C CG  . ASP A 1 37  ? -6.581  1.291   -11.482  1.00 29.41 ? 33  ASP A CG  1 
ATOM   264  O OD1 . ASP A 1 37  ? -6.745  1.747   -12.635  1.00 28.53 ? 33  ASP A OD1 1 
ATOM   265  O OD2 . ASP A 1 37  ? -6.675  1.991   -10.456  1.00 34.77 ? 33  ASP A OD2 1 
ATOM   266  N N   . GLU A 1 38  ? -6.653  -3.363  -11.874  1.00 35.15 ? 34  GLU A N   1 
ATOM   267  C CA  . GLU A 1 38  ? -6.050  -4.681  -11.710  1.00 34.09 ? 34  GLU A CA  1 
ATOM   268  C C   . GLU A 1 38  ? -5.927  -5.398  -13.045  1.00 34.73 ? 34  GLU A C   1 
ATOM   269  O O   . GLU A 1 38  ? -4.917  -6.054  -13.315  1.00 36.08 ? 34  GLU A O   1 
ATOM   270  C CB  . GLU A 1 38  ? -6.828  -5.512  -10.692  1.00 42.98 ? 34  GLU A CB  1 
ATOM   271  C CG  . GLU A 1 38  ? -7.054  -4.801  -9.367   1.00 53.05 ? 34  GLU A CG  1 
ATOM   272  C CD  . GLU A 1 38  ? -8.485  -4.332  -9.193   1.00 61.81 ? 34  GLU A CD  1 
ATOM   273  O OE1 . GLU A 1 38  ? -8.851  -3.286  -9.773   1.00 62.67 ? 34  GLU A OE1 1 
ATOM   274  O OE2 . GLU A 1 38  ? -9.247  -5.010  -8.469   1.00 66.47 ? 34  GLU A OE2 1 
ATOM   275  N N   . ALA A 1 39  ? -6.927  -5.258  -13.902  1.00 29.85 ? 35  ALA A N   1 
ATOM   276  C CA  . ALA A 1 39  ? -6.842  -5.798  -15.251  1.00 29.28 ? 35  ALA A CA  1 
ATOM   277  C C   . ALA A 1 39  ? -6.043  -4.905  -16.192  1.00 28.11 ? 35  ALA A C   1 
ATOM   278  O O   . ALA A 1 39  ? -5.813  -5.299  -17.342  1.00 31.72 ? 35  ALA A O   1 
ATOM   279  C CB  . ALA A 1 39  ? -8.251  -6.045  -15.810  1.00 33.22 ? 35  ALA A CB  1 
ATOM   280  N N   . ARG A 1 40  ? -5.592  -3.742  -15.718  1.00 26.74 ? 36  ARG A N   1 
ATOM   281  C CA  . ARG A 1 40  ? -4.888  -2.741  -16.522  1.00 27.70 ? 36  ARG A CA  1 
ATOM   282  C C   . ARG A 1 40  ? -5.644  -2.428  -17.811  1.00 23.42 ? 36  ARG A C   1 
ATOM   283  O O   . ARG A 1 40  ? -5.117  -2.541  -18.918  1.00 25.00 ? 36  ARG A O   1 
ATOM   284  C CB  . ARG A 1 40  ? -3.432  -3.138  -16.783  1.00 28.44 ? 36  ARG A CB  1 
ATOM   285  C CG  . ARG A 1 40  ? -2.660  -3.326  -15.490  1.00 31.29 ? 36  ARG A CG  1 
ATOM   286  C CD  . ARG A 1 40  ? -1.246  -3.778  -15.761  1.00 39.20 ? 36  ARG A CD  1 
ATOM   287  N NE  . ARG A 1 40  ? -0.477  -3.868  -14.524  1.00 47.50 ? 36  ARG A NE  1 
ATOM   288  C CZ  . ARG A 1 40  ? -0.390  -4.963  -13.775  1.00 53.51 ? 36  ARG A CZ  1 
ATOM   289  N NH1 . ARG A 1 40  ? -1.037  -6.067  -14.130  1.00 54.10 ? 36  ARG A NH1 1 
ATOM   290  N NH2 . ARG A 1 40  ? 0.342   -4.953  -12.670  1.00 52.80 ? 36  ARG A NH2 1 
ATOM   291  N N   . ASP A 1 41  ? -6.881  -1.966  -17.645  1.00 24.58 ? 37  ASP A N   1 
ATOM   292  C CA  . ASP A 1 41  ? -7.816  -1.792  -18.748  1.00 25.55 ? 37  ASP A CA  1 
ATOM   293  C C   . ASP A 1 41  ? -8.606  -0.507  -18.530  1.00 23.54 ? 37  ASP A C   1 
ATOM   294  O O   . ASP A 1 41  ? -9.310  -0.374  -17.526  1.00 23.29 ? 37  ASP A O   1 
ATOM   295  C CB  . ASP A 1 41  ? -8.739  -3.008  -18.779  1.00 29.74 ? 37  ASP A CB  1 
ATOM   296  C CG  . ASP A 1 41  ? -9.820  -2.905  -19.806  1.00 39.40 ? 37  ASP A CG  1 
ATOM   297  O OD1 . ASP A 1 41  ? -9.590  -2.327  -20.884  1.00 41.58 ? 37  ASP A OD1 1 
ATOM   298  O OD2 . ASP A 1 41  ? -10.912 -3.438  -19.528  1.00 45.74 ? 37  ASP A OD2 1 
ATOM   299  N N   . TRP A 1 42  ? -8.506  0.435   -19.468  1.00 21.93 ? 38  TRP A N   1 
ATOM   300  C CA  . TRP A 1 42  ? -9.109  1.751   -19.315  1.00 20.69 ? 38  TRP A CA  1 
ATOM   301  C C   . TRP A 1 42  ? -9.740  2.218   -20.613  1.00 20.28 ? 38  TRP A C   1 
ATOM   302  O O   . TRP A 1 42  ? -9.168  2.019   -21.691  1.00 21.62 ? 38  TRP A O   1 
ATOM   303  C CB  . TRP A 1 42  ? -8.072  2.803   -18.922  1.00 20.58 ? 38  TRP A CB  1 
ATOM   304  C CG  . TRP A 1 42  ? -7.336  2.469   -17.683  1.00 22.60 ? 38  TRP A CG  1 
ATOM   305  C CD1 . TRP A 1 42  ? -7.712  2.774   -16.409  1.00 23.75 ? 38  TRP A CD1 1 
ATOM   306  C CD2 . TRP A 1 42  ? -6.107  1.755   -17.584  1.00 23.30 ? 38  TRP A CD2 1 
ATOM   307  N NE1 . TRP A 1 42  ? -6.785  2.294   -15.515  1.00 23.95 ? 38  TRP A NE1 1 
ATOM   308  C CE2 . TRP A 1 42  ? -5.786  1.667   -16.213  1.00 23.75 ? 38  TRP A CE2 1 
ATOM   309  C CE3 . TRP A 1 42  ? -5.232  1.195   -18.522  1.00 23.02 ? 38  TRP A CE3 1 
ATOM   310  C CZ2 . TRP A 1 42  ? -4.632  1.033   -15.758  1.00 25.71 ? 38  TRP A CZ2 1 
ATOM   311  C CZ3 . TRP A 1 42  ? -4.091  0.560   -18.068  1.00 25.50 ? 38  TRP A CZ3 1 
ATOM   312  C CH2 . TRP A 1 42  ? -3.796  0.489   -16.698  1.00 27.51 ? 38  TRP A CH2 1 
ATOM   313  N N   . VAL A 1 43  ? -10.898 2.869   -20.502  1.00 20.22 ? 39  VAL A N   1 
ATOM   314  C CA  . VAL A 1 43  ? -11.542 3.557   -21.616  1.00 19.18 ? 39  VAL A CA  1 
ATOM   315  C C   . VAL A 1 43  ? -11.921 4.948   -21.129  1.00 19.10 ? 39  VAL A C   1 
ATOM   316  O O   . VAL A 1 43  ? -12.583 5.082   -20.090  1.00 19.27 ? 39  VAL A O   1 
ATOM   317  C CB  . VAL A 1 43  ? -12.790 2.816   -22.122  1.00 21.63 ? 39  VAL A CB  1 
ATOM   318  C CG1 . VAL A 1 43  ? -13.420 3.591   -23.273  1.00 20.16 ? 39  VAL A CG1 1 
ATOM   319  C CG2 . VAL A 1 43  ? -12.457 1.369   -22.527  1.00 22.11 ? 39  VAL A CG2 1 
ATOM   320  N N   . LYS A 1 44  ? -11.470 5.977   -21.839  1.00 18.96 ? 40  LYS A N   1 
ATOM   321  C CA  . LYS A 1 44  ? -11.833 7.359   -21.573  1.00 17.98 ? 40  LYS A CA  1 
ATOM   322  C C   . LYS A 1 44  ? -12.733 7.887   -22.676  1.00 18.55 ? 40  LYS A C   1 
ATOM   323  O O   . LYS A 1 44  ? -12.529 7.578   -23.852  1.00 19.11 ? 40  LYS A O   1 
ATOM   324  C CB  . LYS A 1 44  ? -10.605 8.268   -21.535  1.00 17.99 ? 40  LYS A CB  1 
ATOM   325  C CG  . LYS A 1 44  ? -9.664  8.031   -20.366  1.00 17.58 ? 40  LYS A CG  1 
ATOM   326  C CD  . LYS A 1 44  ? -8.515  9.011   -20.440  1.00 17.41 ? 40  LYS A CD  1 
ATOM   327  C CE  . LYS A 1 44  ? -7.518  8.783   -19.311  1.00 17.27 ? 40  LYS A CE  1 
ATOM   328  N NZ  . LYS A 1 44  ? -6.340  9.696   -19.451  1.00 19.77 ? 40  LYS A NZ  1 
ATOM   329  N N   . ARG A 1 45  ? -13.704 8.713   -22.299  1.00 19.29 ? 41  ARG A N   1 
ATOM   330  C CA  . ARG A 1 45  ? -14.435 9.512   -23.273  1.00 20.43 ? 41  ARG A CA  1 
ATOM   331  C C   . ARG A 1 45  ? -13.551 10.644  -23.777  1.00 21.81 ? 41  ARG A C   1 
ATOM   332  O O   . ARG A 1 45  ? -12.752 11.215  -23.021  1.00 23.24 ? 41  ARG A O   1 
ATOM   333  C CB  . ARG A 1 45  ? -15.681 10.114  -22.616  1.00 22.51 ? 41  ARG A CB  1 
ATOM   334  C CG  . ARG A 1 45  ? -16.681 10.683  -23.617  1.00 30.13 ? 41  ARG A CG  1 
ATOM   335  C CD  . ARG A 1 45  ? -17.973 11.121  -22.940  1.00 39.40 ? 41  ARG A CD  1 
ATOM   336  N NE  . ARG A 1 45  ? -18.809 9.984   -22.562  1.00 48.75 ? 41  ARG A NE  1 
ATOM   337  C CZ  . ARG A 1 45  ? -19.653 9.366   -23.383  1.00 52.85 ? 41  ARG A CZ  1 
ATOM   338  N NH1 . ARG A 1 45  ? -19.775 9.769   -24.642  1.00 54.43 ? 41  ARG A NH1 1 
ATOM   339  N NH2 . ARG A 1 45  ? -20.375 8.341   -22.948  1.00 54.68 ? 41  ARG A NH2 1 
ATOM   340  N N   . VAL A 1 46  ? -13.675 10.952  -25.075  1.00 21.51 ? 42  VAL A N   1 
ATOM   341  C CA  . VAL A 1 46  ? -12.989 12.071  -25.709  1.00 22.24 ? 42  VAL A CA  1 
ATOM   342  C C   . VAL A 1 46  ? -14.018 13.088  -26.184  1.00 23.02 ? 42  VAL A C   1 
ATOM   343  O O   . VAL A 1 46  ? -15.069 12.716  -26.715  1.00 26.61 ? 42  VAL A O   1 
ATOM   344  C CB  . VAL A 1 46  ? -12.137 11.584  -26.895  1.00 19.76 ? 42  VAL A CB  1 
ATOM   345  C CG1 . VAL A 1 46  ? -11.500 12.771  -27.594  1.00 22.07 ? 42  VAL A CG1 1 
ATOM   346  C CG2 . VAL A 1 46  ? -11.062 10.621  -26.405  1.00 19.75 ? 42  VAL A CG2 1 
ATOM   347  N N   . GLY A 1 47  ? -13.732 14.369  -25.965  1.00 27.21 ? 43  GLY A N   1 
ATOM   348  C CA  . GLY A 1 47  ? -14.592 15.436  -26.441  1.00 33.50 ? 43  GLY A CA  1 
ATOM   349  C C   . GLY A 1 47  ? -13.882 16.468  -27.295  1.00 29.27 ? 43  GLY A C   1 
ATOM   350  O O   . GLY A 1 47  ? -12.792 16.916  -26.931  1.00 31.44 ? 43  GLY A O   1 
ATOM   351  N N   . GLY A 1 48  ? -14.480 16.861  -28.417  1.00 29.52 ? 44  GLY A N   1 
ATOM   352  C CA  . GLY A 1 48  ? -13.952 17.964  -29.200  1.00 27.42 ? 44  GLY A CA  1 
ATOM   353  C C   . GLY A 1 48  ? -12.713 17.673  -30.018  1.00 26.96 ? 44  GLY A C   1 
ATOM   354  O O   . GLY A 1 48  ? -12.009 18.610  -30.408  1.00 31.31 ? 44  GLY A O   1 
ATOM   355  N N   . LYS A 1 49  ? -12.430 16.409  -30.312  1.00 24.51 ? 45  LYS A N   1 
ATOM   356  C CA  . LYS A 1 49  ? -11.252 16.014  -31.067  1.00 22.58 ? 45  LYS A CA  1 
ATOM   357  C C   . LYS A 1 49  ? -11.693 15.214  -32.289  1.00 22.96 ? 45  LYS A C   1 
ATOM   358  O O   . LYS A 1 49  ? -12.672 14.464  -32.236  1.00 22.41 ? 45  LYS A O   1 
ATOM   359  C CB  . LYS A 1 49  ? -10.317 15.151  -30.199  1.00 24.81 ? 45  LYS A CB  1 
ATOM   360  C CG  . LYS A 1 49  ? -9.887  15.764  -28.855  1.00 26.98 ? 45  LYS A CG  1 
ATOM   361  C CD  . LYS A 1 49  ? -9.076  17.030  -29.026  1.00 28.29 ? 45  LYS A CD  1 
ATOM   362  C CE  . LYS A 1 49  ? -8.519  17.508  -27.677  1.00 31.29 ? 45  LYS A CE  1 
ATOM   363  N NZ  . LYS A 1 49  ? -9.586  18.008  -26.764  1.00 40.58 ? 45  LYS A NZ  1 
ATOM   364  N N   . THR A 1 50  ? -10.953 15.352  -33.385  1.00 21.47 ? 46  THR A N   1 
ATOM   365  C CA  . THR A 1 50  ? -11.208 14.573  -34.594  1.00 20.27 ? 46  THR A CA  1 
ATOM   366  C C   . THR A 1 50  ? -9.941  13.857  -35.045  1.00 17.52 ? 46  THR A C   1 
ATOM   367  O O   . THR A 1 50  ? -8.823  14.180  -34.628  1.00 19.18 ? 46  THR A O   1 
ATOM   368  C CB  . THR A 1 50  ? -11.697 15.450  -35.752  1.00 23.25 ? 46  THR A CB  1 
ATOM   369  O OG1 . THR A 1 50  ? -10.681 16.400  -36.094  1.00 23.91 ? 46  THR A OG1 1 
ATOM   370  C CG2 . THR A 1 50  ? -12.984 16.170  -35.406  1.00 24.66 ? 46  THR A CG2 1 
ATOM   371  N N   . SER A 1 51  ? -10.124 12.900  -35.950  1.00 17.98 ? 47  SER A N   1 
ATOM   372  C CA  . SER A 1 51  ? -8.998  12.262  -36.619  1.00 17.02 ? 47  SER A CA  1 
ATOM   373  C C   . SER A 1 51  ? -9.383  11.921  -38.054  1.00 17.53 ? 47  SER A C   1 
ATOM   374  O O   . SER A 1 51  ? -10.529 12.073  -38.471  1.00 16.96 ? 47  SER A O   1 
ATOM   375  C CB  . SER A 1 51  ? -8.509  11.031  -35.848  1.00 19.83 ? 47  SER A CB  1 
ATOM   376  O OG  . SER A 1 51  ? -7.187  10.661  -36.236  1.00 20.71 ? 47  SER A OG  1 
ATOM   377  N N   . LEU A 1 52  ? -8.400  11.459  -38.811  1.00 18.13 ? 48  LEU A N   1 
ATOM   378  C CA  . LEU A 1 52  ? -8.603  11.068  -40.200  1.00 17.98 ? 48  LEU A CA  1 
ATOM   379  C C   . LEU A 1 52  ? -8.958  9.594   -40.299  1.00 19.11 ? 48  LEU A C   1 
ATOM   380  O O   . LEU A 1 52  ? -8.423  8.753   -39.570  1.00 25.10 ? 48  LEU A O   1 
ATOM   381  C CB  . LEU A 1 52  ? -7.326  11.301  -41.010  1.00 22.58 ? 48  LEU A CB  1 
ATOM   382  C CG  . LEU A 1 52  ? -6.917  12.753  -41.147  1.00 24.40 ? 48  LEU A CG  1 
ATOM   383  C CD1 . LEU A 1 52  ? -5.457  12.803  -41.515  1.00 26.47 ? 48  LEU A CD1 1 
ATOM   384  C CD2 . LEU A 1 52  ? -7.785  13.416  -42.192  1.00 27.55 ? 48  LEU A CD2 1 
ATOM   385  N N   . SER A 1 53  ? -9.838  9.283   -41.241  1.00 18.86 ? 49  SER A N   1 
ATOM   386  C CA  . SER A 1 53  ? -10.328 7.930   -41.440  1.00 18.05 ? 49  SER A CA  1 
ATOM   387  C C   . SER A 1 53  ? -10.661 7.799   -42.911  1.00 20.14 ? 49  SER A C   1 
ATOM   388  O O   . SER A 1 53  ? -10.598 8.773   -43.654  1.00 19.92 ? 49  SER A O   1 
ATOM   389  C CB  . SER A 1 53  ? -11.581 7.689   -40.594  1.00 19.41 ? 49  SER A CB  1 
ATOM   390  O OG  . SER A 1 53  ? -12.657 8.487   -41.062  1.00 20.25 ? 49  SER A OG  1 
ATOM   391  N N   . VAL A 1 54  ? -11.015 6.588   -43.319  1.00 17.66 ? 50  VAL A N   1 
ATOM   392  C CA  . VAL A 1 54  ? -11.454 6.326   -44.688  1.00 18.18 ? 50  VAL A CA  1 
ATOM   393  C C   . VAL A 1 54  ? -12.842 5.708   -44.657  1.00 18.33 ? 50  VAL A C   1 
ATOM   394  O O   . VAL A 1 54  ? -13.094 4.736   -43.933  1.00 19.82 ? 50  VAL A O   1 
ATOM   395  C CB  . VAL A 1 54  ? -10.452 5.446   -45.459  1.00 18.05 ? 50  VAL A CB  1 
ATOM   396  C CG1 . VAL A 1 54  ? -10.996 5.109   -46.847  1.00 21.39 ? 50  VAL A CG1 1 
ATOM   397  C CG2 . VAL A 1 54  ? -9.132  6.171   -45.609  1.00 19.42 ? 50  VAL A CG2 1 
ATOM   398  N N   . ASN A 1 55  ? -13.749 6.279   -45.446  1.00 19.37 ? 51  ASN A N   1 
ATOM   399  C CA  . ASN A 1 55  ? -15.070 5.695   -45.640  1.00 20.11 ? 51  ASN A CA  1 
ATOM   400  C C   . ASN A 1 55  ? -14.892 4.495   -46.567  1.00 20.27 ? 51  ASN A C   1 
ATOM   401  O O   . ASN A 1 55  ? -14.452 4.644   -47.713  1.00 21.70 ? 51  ASN A O   1 
ATOM   402  C CB  . ASN A 1 55  ? -15.979 6.759   -46.253  1.00 20.48 ? 51  ASN A CB  1 
ATOM   403  C CG  . ASN A 1 55  ? -17.408 6.304   -46.430  1.00 21.82 ? 51  ASN A CG  1 
ATOM   404  O OD1 . ASN A 1 55  ? -17.695 5.242   -46.982  1.00 21.75 ? 51  ASN A OD1 1 
ATOM   405  N ND2 . ASN A 1 55  ? -18.327 7.135   -45.958  1.00 25.63 ? 51  ASN A ND2 1 
ATOM   406  N N   . THR A 1 56  ? -15.174 3.295   -46.058  1.00 21.35 ? 52  THR A N   1 
ATOM   407  C CA  . THR A 1 56  ? -14.909 2.103   -46.858  1.00 23.82 ? 52  THR A CA  1 
ATOM   408  C C   . THR A 1 56  ? -15.929 1.895   -47.969  1.00 25.08 ? 52  THR A C   1 
ATOM   409  O O   . THR A 1 56  ? -15.712 1.044   -48.837  1.00 27.98 ? 52  THR A O   1 
ATOM   410  C CB  . THR A 1 56  ? -14.813 0.850   -45.986  1.00 25.71 ? 52  THR A CB  1 
ATOM   411  O OG1 . THR A 1 56  ? -16.048 0.631   -45.302  1.00 32.35 ? 52  THR A OG1 1 
ATOM   412  C CG2 . THR A 1 56  ? -13.680 0.986   -44.979  1.00 28.98 ? 52  THR A CG2 1 
ATOM   413  N N   . TYR A 1 57  ? -17.049 2.616   -47.957  1.00 20.39 ? 53  TYR A N   1 
ATOM   414  C CA  . TYR A 1 57  ? -18.001 2.524   -49.053  1.00 23.24 ? 53  TYR A CA  1 
ATOM   415  C C   . TYR A 1 57  ? -17.641 3.465   -50.202  1.00 26.30 ? 53  TYR A C   1 
ATOM   416  O O   . TYR A 1 57  ? -17.606 3.051   -51.364  1.00 26.17 ? 53  TYR A O   1 
ATOM   417  C CB  . TYR A 1 57  ? -19.422 2.786   -48.542  1.00 23.94 ? 53  TYR A CB  1 
ATOM   418  C CG  . TYR A 1 57  ? -20.444 2.551   -49.626  1.00 25.70 ? 53  TYR A CG  1 
ATOM   419  C CD1 . TYR A 1 57  ? -20.846 1.257   -49.972  1.00 26.19 ? 53  TYR A CD1 1 
ATOM   420  C CD2 . TYR A 1 57  ? -21.000 3.606   -50.322  1.00 26.26 ? 53  TYR A CD2 1 
ATOM   421  C CE1 . TYR A 1 57  ? -21.760 1.031   -50.973  1.00 27.88 ? 53  TYR A CE1 1 
ATOM   422  C CE2 . TYR A 1 57  ? -21.932 3.392   -51.315  1.00 25.21 ? 53  TYR A CE2 1 
ATOM   423  C CZ  . TYR A 1 57  ? -22.314 2.098   -51.637  1.00 27.55 ? 53  TYR A CZ  1 
ATOM   424  O OH  . TYR A 1 57  ? -23.226 1.856   -52.635  1.00 32.51 ? 53  TYR A OH  1 
ATOM   425  N N   . SER A 1 58  ? -17.359 4.730   -49.898  1.00 23.55 ? 54  SER A N   1 
ATOM   426  C CA  . SER A 1 58  ? -17.025 5.705   -50.928  1.00 25.24 ? 54  SER A CA  1 
ATOM   427  C C   . SER A 1 58  ? -15.545 5.690   -51.292  1.00 27.64 ? 54  SER A C   1 
ATOM   428  O O   . SER A 1 58  ? -15.189 6.122   -52.397  1.00 26.05 ? 54  SER A O   1 
ATOM   429  C CB  . SER A 1 58  ? -17.410 7.102   -50.453  1.00 26.13 ? 54  SER A CB  1 
ATOM   430  O OG  . SER A 1 58  ? -16.534 7.509   -49.417  1.00 24.65 ? 54  SER A OG  1 
ATOM   431  N N   . GLY A 1 59  ? -14.683 5.196   -50.404  1.00 23.45 ? 55  GLY A N   1 
ATOM   432  C CA  . GLY A 1 59  ? -13.250 5.247   -50.622  1.00 23.35 ? 55  GLY A CA  1 
ATOM   433  C C   . GLY A 1 59  ? -12.616 6.585   -50.336  1.00 28.64 ? 55  GLY A C   1 
ATOM   434  O O   . GLY A 1 59  ? -11.431 6.769   -50.639  1.00 29.88 ? 55  GLY A O   1 
ATOM   435  N N   . GLU A 1 60  ? -13.359 7.519   -49.760  1.00 26.38 ? 56  GLU A N   1 
ATOM   436  C CA  . GLU A 1 60  ? -12.906 8.884   -49.549  1.00 28.42 ? 56  GLU A CA  1 
ATOM   437  C C   . GLU A 1 60  ? -12.382 9.055   -48.128  1.00 23.74 ? 56  GLU A C   1 
ATOM   438  O O   . GLU A 1 60  ? -12.905 8.459   -47.177  1.00 22.27 ? 56  GLU A O   1 
ATOM   439  C CB  . GLU A 1 60  ? -14.067 9.856   -49.765  1.00 31.52 ? 56  GLU A CB  1 
ATOM   440  C CG  . GLU A 1 60  ? -14.737 9.754   -51.129  1.00 45.69 ? 56  GLU A CG  1 
ATOM   441  C CD  . GLU A 1 60  ? -14.038 10.582  -52.191  1.00 54.17 ? 56  GLU A CD  1 
ATOM   442  O OE1 . GLU A 1 60  ? -13.436 11.619  -51.837  1.00 59.05 ? 56  GLU A OE1 1 
ATOM   443  O OE2 . GLU A 1 60  ? -14.093 10.198  -53.380  1.00 59.73 ? 56  GLU A OE2 1 
ATOM   444  N N   . VAL A 1 61  ? -11.355 9.889   -47.984  1.00 21.17 ? 57  VAL A N   1 
ATOM   445  C CA  . VAL A 1 61  ? -10.872 10.256  -46.658  1.00 22.34 ? 57  VAL A CA  1 
ATOM   446  C C   . VAL A 1 61  ? -11.890 11.174  -46.000  1.00 22.52 ? 57  VAL A C   1 
ATOM   447  O O   . VAL A 1 61  ? -12.459 12.068  -46.643  1.00 24.61 ? 57  VAL A O   1 
ATOM   448  C CB  . VAL A 1 61  ? -9.493  10.930  -46.758  1.00 25.41 ? 57  VAL A CB  1 
ATOM   449  C CG1 . VAL A 1 61  ? -9.110  11.569  -45.430  1.00 25.72 ? 57  VAL A CG1 1 
ATOM   450  C CG2 . VAL A 1 61  ? -8.434  9.924   -47.190  1.00 27.60 ? 57  VAL A CG2 1 
ATOM   451  N N   . GLU A 1 62  ? -12.165 10.928  -44.718  1.00 19.90 ? 58  GLU A N   1 
ATOM   452  C CA  . GLU A 1 62  ? -13.104 11.748  -43.968  1.00 22.92 ? 58  GLU A CA  1 
ATOM   453  C C   . GLU A 1 62  ? -12.543 12.031  -42.585  1.00 19.91 ? 58  GLU A C   1 
ATOM   454  O O   . GLU A 1 62  ? -12.027 11.134  -41.913  1.00 21.85 ? 58  GLU A O   1 
ATOM   455  C CB  . GLU A 1 62  ? -14.478 11.056  -43.839  1.00 24.23 ? 58  GLU A CB  1 
ATOM   456  C CG  . GLU A 1 62  ? -15.173 10.838  -45.184  1.00 24.13 ? 58  GLU A CG  1 
ATOM   457  C CD  . GLU A 1 62  ? -16.549 10.201  -45.069  1.00 26.40 ? 58  GLU A CD  1 
ATOM   458  O OE1 . GLU A 1 62  ? -16.768 9.389   -44.148  1.00 28.10 ? 58  GLU A OE1 1 
ATOM   459  O OE2 . GLU A 1 62  ? -17.406 10.491  -45.934  1.00 32.48 ? 58  GLU A OE2 1 
ATOM   460  N N   . ARG A 1 63  ? -12.702 13.268  -42.141  1.00 21.35 ? 59  ARG A N   1 
ATOM   461  C CA  . ARG A 1 63  ? -12.333 13.646  -40.786  1.00 21.20 ? 59  ARG A CA  1 
ATOM   462  C C   . ARG A 1 63  ? -13.540 13.420  -39.885  1.00 22.90 ? 59  ARG A C   1 
ATOM   463  O O   . ARG A 1 63  ? -14.643 13.887  -40.189  1.00 26.07 ? 59  ARG A O   1 
ATOM   464  C CB  . ARG A 1 63  ? -11.896 15.111  -40.762  1.00 27.50 ? 59  ARG A CB  1 
ATOM   465  C CG  . ARG A 1 63  ? -11.485 15.620  -39.390  1.00 25.77 ? 59  ARG A CG  1 
ATOM   466  C CD  . ARG A 1 63  ? -10.648 16.891  -39.496  1.00 24.64 ? 59  ARG A CD  1 
ATOM   467  N NE  . ARG A 1 63  ? -9.320  16.624  -40.035  1.00 24.97 ? 59  ARG A NE  1 
ATOM   468  C CZ  . ARG A 1 63  ? -8.306  16.122  -39.333  1.00 24.04 ? 59  ARG A CZ  1 
ATOM   469  N NH1 . ARG A 1 63  ? -8.466  15.793  -38.058  1.00 23.49 ? 59  ARG A NH1 1 
ATOM   470  N NH2 . ARG A 1 63  ? -7.129  15.923  -39.918  1.00 22.24 ? 59  ARG A NH2 1 
ATOM   471  N N   . LYS A 1 64  ? -13.346 12.660  -38.811  1.00 18.65 ? 60  LYS A N   1 
ATOM   472  C CA  . LYS A 1 64  ? -14.450 12.189  -37.984  1.00 21.53 ? 60  LYS A CA  1 
ATOM   473  C C   . LYS A 1 64  ? -14.129 12.389  -36.507  1.00 19.65 ? 60  LYS A C   1 
ATOM   474  O O   . LYS A 1 64  ? -12.968 12.412  -36.101  1.00 21.97 ? 60  LYS A O   1 
ATOM   475  C CB  . LYS A 1 64  ? -14.706 10.694  -38.231  1.00 19.01 ? 60  LYS A CB  1 
ATOM   476  C CG  . LYS A 1 64  ? -15.273 10.368  -39.605  1.00 21.71 ? 60  LYS A CG  1 
ATOM   477  C CD  . LYS A 1 64  ? -16.700 10.836  -39.706  1.00 25.99 ? 60  LYS A CD  1 
ATOM   478  C CE  . LYS A 1 64  ? -17.414 10.210  -40.878  1.00 29.67 ? 60  LYS A CE  1 
ATOM   479  N NZ  . LYS A 1 64  ? -18.854 10.564  -40.794  1.00 33.08 ? 60  LYS A NZ  1 
ATOM   480  N N   . ASN A 1 65  ? -15.167 12.484  -35.687  1.00 19.29 ? 61  ASN A N   1 
ATOM   481  C CA  . ASN A 1 65  ? -14.946 12.673  -34.258  1.00 19.04 ? 61  ASN A CA  1 
ATOM   482  C C   . ASN A 1 65  ? -14.302 11.445  -33.626  1.00 19.52 ? 61  ASN A C   1 
ATOM   483  O O   . ASN A 1 65  ? -14.601 10.302  -33.985  1.00 21.02 ? 61  ASN A O   1 
ATOM   484  C CB  . ASN A 1 65  ? -16.278 12.938  -33.570  1.00 22.88 ? 61  ASN A CB  1 
ATOM   485  C CG  . ASN A 1 65  ? -16.861 14.277  -33.934  1.00 31.62 ? 61  ASN A CG  1 
ATOM   486  O OD1 . ASN A 1 65  ? -16.144 15.268  -34.052  1.00 39.52 ? 61  ASN A OD1 1 
ATOM   487  N ND2 . ASN A 1 65  ? -18.180 14.324  -34.083  1.00 43.33 ? 61  ASN A ND2 1 
ATOM   488  N N   . ILE A 1 66  ? -13.406 11.684  -32.671  1.00 19.88 ? 62  ILE A N   1 
ATOM   489  C CA  . ILE A 1 66  ? -12.893 10.622  -31.810  1.00 21.42 ? 62  ILE A CA  1 
ATOM   490  C C   . ILE A 1 66  ? -13.846 10.528  -30.629  1.00 18.90 ? 62  ILE A C   1 
ATOM   491  O O   . ILE A 1 66  ? -14.027 11.507  -29.899  1.00 21.12 ? 62  ILE A O   1 
ATOM   492  C CB  . ILE A 1 66  ? -11.476 10.937  -31.311  1.00 18.34 ? 62  ILE A CB  1 
ATOM   493  C CG1 . ILE A 1 66  ? -10.512 11.166  -32.486  1.00 21.45 ? 62  ILE A CG1 1 
ATOM   494  C CG2 . ILE A 1 66  ? -10.976 9.835   -30.398  1.00 18.95 ? 62  ILE A CG2 1 
ATOM   495  C CD1 . ILE A 1 66  ? -9.099  11.609  -32.058  1.00 22.22 ? 62  ILE A CD1 1 
ATOM   496  N N   . ASN A 1 67  ? -14.463 9.364   -30.442  1.00 19.43 ? 63  ASN A N   1 
ATOM   497  C CA  . ASN A 1 67  ? -15.439 9.223   -29.363  1.00 20.65 ? 63  ASN A CA  1 
ATOM   498  C C   . ASN A 1 67  ? -14.815 8.735   -28.060  1.00 19.14 ? 63  ASN A C   1 
ATOM   499  O O   . ASN A 1 67  ? -15.247 9.150   -26.975  1.00 20.57 ? 63  ASN A O   1 
ATOM   500  C CB  . ASN A 1 67  ? -16.537 8.235   -29.776  1.00 23.84 ? 63  ASN A CB  1 
ATOM   501  C CG  . ASN A 1 67  ? -17.352 8.718   -30.959  1.00 26.11 ? 63  ASN A CG  1 
ATOM   502  O OD1 . ASN A 1 67  ? -17.546 9.919   -31.141  1.00 27.77 ? 63  ASN A OD1 1 
ATOM   503  N ND2 . ASN A 1 67  ? -17.839 7.776   -31.770  1.00 25.44 ? 63  ASN A ND2 1 
ATOM   504  N N   . TYR A 1 68  ? -13.836 7.833   -28.151  1.00 18.93 ? 64  TYR A N   1 
ATOM   505  C CA  . TYR A 1 68  ? -13.219 7.205   -26.989  1.00 18.82 ? 64  TYR A CA  1 
ATOM   506  C C   . TYR A 1 68  ? -11.763 6.912   -27.299  1.00 19.12 ? 64  TYR A C   1 
ATOM   507  O O   . TYR A 1 68  ? -11.367 6.765   -28.456  1.00 18.19 ? 64  TYR A O   1 
ATOM   508  C CB  . TYR A 1 68  ? -13.900 5.883   -26.624  1.00 22.36 ? 64  TYR A CB  1 
ATOM   509  C CG  . TYR A 1 68  ? -15.360 6.017   -26.330  1.00 23.04 ? 64  TYR A CG  1 
ATOM   510  C CD1 . TYR A 1 68  ? -15.794 6.467   -25.087  1.00 22.14 ? 64  TYR A CD1 1 
ATOM   511  C CD2 . TYR A 1 68  ? -16.317 5.706   -27.297  1.00 25.21 ? 64  TYR A CD2 1 
ATOM   512  C CE1 . TYR A 1 68  ? -17.145 6.600   -24.812  1.00 29.27 ? 64  TYR A CE1 1 
ATOM   513  C CE2 . TYR A 1 68  ? -17.668 5.837   -27.032  1.00 25.53 ? 64  TYR A CE2 1 
ATOM   514  C CZ  . TYR A 1 68  ? -18.073 6.282   -25.787  1.00 26.74 ? 64  TYR A CZ  1 
ATOM   515  O OH  . TYR A 1 68  ? -19.418 6.421   -25.500  1.00 32.15 ? 64  TYR A OH  1 
ATOM   516  N N   . ILE A 1 69  ? -10.971 6.782   -26.244  1.00 19.76 ? 65  ILE A N   1 
ATOM   517  C CA  . ILE A 1 69  ? -9.606  6.293   -26.332  1.00 16.83 ? 65  ILE A CA  1 
ATOM   518  C C   . ILE A 1 69  ? -9.410  5.216   -25.278  1.00 19.57 ? 65  ILE A C   1 
ATOM   519  O O   . ILE A 1 69  ? -9.924  5.324   -24.157  1.00 19.52 ? 65  ILE A O   1 
ATOM   520  C CB  . ILE A 1 69  ? -8.566  7.425   -26.228  1.00 18.43 ? 65  ILE A CB  1 
ATOM   521  C CG1 . ILE A 1 69  ? -7.169  6.843   -26.425  1.00 19.90 ? 65  ILE A CG1 1 
ATOM   522  C CG2 . ILE A 1 69  ? -8.703  8.173   -24.889  1.00 20.10 ? 65  ILE A CG2 1 
ATOM   523  C CD1 . ILE A 1 69  ? -6.125  7.804   -26.849  1.00 27.64 ? 65  ILE A CD1 1 
ATOM   524  N N   . MET A 1 70  ? -8.716  4.146   -25.659  1.00 21.93 ? 66  MET A N   1 
ATOM   525  C CA  . MET A 1 70  ? -8.554  2.966   -24.822  1.00 21.80 ? 66  MET A CA  1 
ATOM   526  C C   . MET A 1 70  ? -7.079  2.672   -24.623  1.00 20.48 ? 66  MET A C   1 
ATOM   527  O O   . MET A 1 70  ? -6.258  2.894   -25.521  1.00 19.45 ? 66  MET A O   1 
ATOM   528  C CB  . MET A 1 70  ? -9.180  1.751   -25.504  1.00 31.03 ? 66  MET A CB  1 
ATOM   529  C CG  . MET A 1 70  ? -10.674 1.725   -25.433  1.00 44.49 ? 66  MET A CG  1 
ATOM   530  S SD  . MET A 1 70  ? -11.341 1.406   -27.053  1.00 55.16 ? 66  MET A SD  1 
ATOM   531  C CE  . MET A 1 70  ? -10.888 2.951   -27.819  1.00 44.04 ? 66  MET A CE  1 
ATOM   532  N N   . LYS A 1 71  ? -6.764  2.119   -23.463  1.00 22.03 ? 67  LYS A N   1 
ATOM   533  C CA  . LYS A 1 71  ? -5.429  1.665   -23.118  1.00 20.44 ? 67  LYS A CA  1 
ATOM   534  C C   . LYS A 1 71  ? -5.575  0.333   -22.407  1.00 22.12 ? 67  LYS A C   1 
ATOM   535  O O   . LYS A 1 71  ? -6.401  0.207   -21.499  1.00 22.48 ? 67  LYS A O   1 
ATOM   536  C CB  . LYS A 1 71  ? -4.748  2.675   -22.186  1.00 21.97 ? 67  LYS A CB  1 
ATOM   537  C CG  . LYS A 1 71  ? -3.393  2.241   -21.671  1.00 24.70 ? 67  LYS A CG  1 
ATOM   538  C CD  . LYS A 1 71  ? -2.821  3.244   -20.675  1.00 23.68 ? 67  LYS A CD  1 
ATOM   539  C CE  . LYS A 1 71  ? -1.492  2.780   -20.122  1.00 26.85 ? 67  LYS A CE  1 
ATOM   540  N NZ  . LYS A 1 71  ? -0.918  3.754   -19.151  1.00 30.15 ? 67  LYS A NZ  1 
ATOM   541  N N   . HIS A 1 72  ? -4.800  -0.663  -22.824  1.00 21.88 ? 68  HIS A N   1 
ATOM   542  C CA  . HIS A 1 72  ? -4.750  -1.937  -22.128  1.00 24.70 ? 68  HIS A CA  1 
ATOM   543  C C   . HIS A 1 72  ? -3.322  -2.449  -22.110  1.00 22.38 ? 68  HIS A C   1 
ATOM   544  O O   . HIS A 1 72  ? -2.648  -2.452  -23.141  1.00 25.14 ? 68  HIS A O   1 
ATOM   545  C CB  . HIS A 1 72  ? -5.659  -2.980  -22.804  1.00 32.15 ? 68  HIS A CB  1 
ATOM   546  C CG  . HIS A 1 72  ? -5.872  -4.226  -21.994  1.00 50.48 ? 68  HIS A CG  1 
ATOM   547  N ND1 . HIS A 1 72  ? -6.370  -5.389  -22.537  1.00 56.21 ? 68  HIS A ND1 1 
ATOM   548  C CD2 . HIS A 1 72  ? -5.657  -4.484  -20.683  1.00 55.15 ? 68  HIS A CD2 1 
ATOM   549  C CE1 . HIS A 1 72  ? -6.448  -6.314  -21.593  1.00 55.81 ? 68  HIS A CE1 1 
ATOM   550  N NE2 . HIS A 1 72  ? -6.019  -5.790  -20.462  1.00 55.82 ? 68  HIS A NE2 1 
ATOM   551  N N   . THR A 1 73  ? -2.888  -2.952  -20.964  1.00 26.02 ? 69  THR A N   1 
ATOM   552  C CA  . THR A 1 73  ? -1.595  -3.605  -20.878  1.00 27.83 ? 69  THR A CA  1 
ATOM   553  C C   . THR A 1 73  ? -1.824  -5.086  -21.129  1.00 30.34 ? 69  THR A C   1 
ATOM   554  O O   . THR A 1 73  ? -2.610  -5.728  -20.425  1.00 35.09 ? 69  THR A O   1 
ATOM   555  C CB  . THR A 1 73  ? -0.956  -3.370  -19.510  1.00 27.39 ? 69  THR A CB  1 
ATOM   556  O OG1 . THR A 1 73  ? -0.910  -1.968  -19.237  1.00 33.21 ? 69  THR A OG1 1 
ATOM   557  C CG2 . THR A 1 73  ? 0.460   -3.917  -19.504  1.00 32.91 ? 69  THR A CG2 1 
ATOM   558  N N   . VAL A 1 74  ? -1.154  -5.617  -22.148  1.00 32.75 ? 70  VAL A N   1 
ATOM   559  C CA  . VAL A 1 74  ? -1.403  -6.961  -22.647  1.00 35.53 ? 70  VAL A CA  1 
ATOM   560  C C   . VAL A 1 74  ? -0.073  -7.687  -22.772  1.00 30.54 ? 70  VAL A C   1 
ATOM   561  O O   . VAL A 1 74  ? 0.991   -7.075  -22.870  1.00 31.12 ? 70  VAL A O   1 
ATOM   562  C CB  . VAL A 1 74  ? -2.124  -6.948  -24.016  1.00 37.00 ? 70  VAL A CB  1 
ATOM   563  C CG1 . VAL A 1 74  ? -3.404  -6.140  -23.939  1.00 37.78 ? 70  VAL A CG1 1 
ATOM   564  C CG2 . VAL A 1 74  ? -1.205  -6.390  -25.105  1.00 39.94 ? 70  VAL A CG2 1 
ATOM   565  N N   . LYS A 1 75  ? -0.149  -9.012  -22.782  1.00 36.69 ? 71  LYS A N   1 
ATOM   566  C CA  . LYS A 1 75  ? 0.964   -9.859  -23.191  1.00 27.47 ? 71  LYS A CA  1 
ATOM   567  C C   . LYS A 1 75  ? 0.497   -10.583 -24.444  1.00 34.30 ? 71  LYS A C   1 
ATOM   568  O O   . LYS A 1 75  ? -0.309  -11.515 -24.366  1.00 38.77 ? 71  LYS A O   1 
ATOM   569  C CB  . LYS A 1 75  ? 1.371   -10.848 -22.097  1.00 28.25 ? 71  LYS A CB  1 
ATOM   570  C CG  . LYS A 1 75  ? 2.630   -11.620 -22.458  1.00 35.73 ? 71  LYS A CG  1 
ATOM   571  C CD  . LYS A 1 75  ? 3.159   -12.476 -21.321  1.00 44.07 ? 71  LYS A CD  1 
ATOM   572  C CE  . LYS A 1 75  ? 4.640   -12.769 -21.529  1.00 51.22 ? 71  LYS A CE  1 
ATOM   573  N NZ  . LYS A 1 75  ? 5.055   -14.084 -20.959  1.00 52.53 ? 71  LYS A NZ  1 
ATOM   574  N N   . LYS A 1 76  ? 0.983   -10.137 -25.600  1.00 30.09 ? 72  LYS A N   1 
ATOM   575  C CA  . LYS A 1 76  ? 0.407   -10.568 -26.860  1.00 33.30 ? 72  LYS A CA  1 
ATOM   576  C C   . LYS A 1 76  ? 1.489   -10.623 -27.920  1.00 32.92 ? 72  LYS A C   1 
ATOM   577  O O   . LYS A 1 76  ? 2.534   -9.975  -27.811  1.00 26.13 ? 72  LYS A O   1 
ATOM   578  C CB  . LYS A 1 76  ? -0.683  -9.603  -27.342  1.00 34.98 ? 72  LYS A CB  1 
ATOM   579  C CG  . LYS A 1 76  ? -1.986  -9.676  -26.575  1.00 42.21 ? 72  LYS A CG  1 
ATOM   580  C CD  . LYS A 1 76  ? -2.849  -10.829 -27.044  1.00 47.08 ? 72  LYS A CD  1 
ATOM   581  C CE  . LYS A 1 76  ? -4.298  -10.625 -26.627  1.00 49.75 ? 72  LYS A CE  1 
ATOM   582  N NZ  . LYS A 1 76  ? -4.866  -9.378  -27.215  1.00 49.92 ? 72  LYS A NZ  1 
ATOM   583  N N   . ARG A 1 77  ? 1.217   -11.437 -28.936  1.00 30.49 ? 73  ARG A N   1 
ATOM   584  C CA  . ARG A 1 77  ? 2.026   -11.484 -30.145  1.00 32.77 ? 73  ARG A CA  1 
ATOM   585  C C   . ARG A 1 77  ? 1.860   -10.189 -30.932  1.00 28.02 ? 73  ARG A C   1 
ATOM   586  O O   . ARG A 1 77  ? 0.735   -9.741  -31.174  1.00 27.36 ? 73  ARG A O   1 
ATOM   587  C CB  . ARG A 1 77  ? 1.533   -12.642 -31.006  1.00 38.83 ? 73  ARG A CB  1 
ATOM   588  C CG  . ARG A 1 77  ? 2.328   -12.852 -32.265  1.00 45.67 ? 73  ARG A CG  1 
ATOM   589  C CD  . ARG A 1 77  ? 3.596   -13.585 -31.933  1.00 57.04 ? 73  ARG A CD  1 
ATOM   590  N NE  . ARG A 1 77  ? 3.319   -14.986 -31.635  1.00 63.79 ? 73  ARG A NE  1 
ATOM   591  C CZ  . ARG A 1 77  ? 3.224   -15.939 -32.556  1.00 66.20 ? 73  ARG A CZ  1 
ATOM   592  N NH1 . ARG A 1 77  ? 3.384   -15.644 -33.839  1.00 66.97 ? 73  ARG A NH1 1 
ATOM   593  N NH2 . ARG A 1 77  ? 2.964   -17.187 -32.194  1.00 67.71 ? 73  ARG A NH2 1 
ATOM   594  N N   . MET A 1 78  ? 2.978   -9.581  -31.328  1.00 25.62 ? 74  MET A N   1 
ATOM   595  C CA  . MET A 1 78  ? 2.975   -8.301  -32.033  1.00 23.44 ? 74  MET A CA  1 
ATOM   596  C C   . MET A 1 78  ? 3.546   -8.447  -33.440  1.00 24.61 ? 74  MET A C   1 
ATOM   597  O O   . MET A 1 78  ? 4.504   -9.196  -33.656  1.00 24.50 ? 74  MET A O   1 
ATOM   598  C CB  . MET A 1 78  ? 3.791   -7.262  -31.268  1.00 23.75 ? 74  MET A CB  1 
ATOM   599  C CG  . MET A 1 78  ? 3.406   -7.130  -29.791  1.00 26.48 ? 74  MET A CG  1 
ATOM   600  S SD  . MET A 1 78  ? 1.729   -6.531  -29.532  1.00 26.23 ? 74  MET A SD  1 
ATOM   601  C CE  . MET A 1 78  ? 1.820   -4.886  -30.235  1.00 23.38 ? 74  MET A CE  1 
ATOM   602  N N   . PHE A 1 79  ? 2.975   -7.701  -34.391  1.00 19.64 ? 75  PHE A N   1 
ATOM   603  C CA  . PHE A 1 79  ? 3.427   -7.684  -35.777  1.00 20.37 ? 75  PHE A CA  1 
ATOM   604  C C   . PHE A 1 79  ? 3.684   -6.256  -36.225  1.00 19.31 ? 75  PHE A C   1 
ATOM   605  O O   . PHE A 1 79  ? 2.952   -5.333  -35.852  1.00 20.30 ? 75  PHE A O   1 
ATOM   606  C CB  . PHE A 1 79  ? 2.389   -8.309  -36.724  1.00 20.17 ? 75  PHE A CB  1 
ATOM   607  C CG  . PHE A 1 79  ? 2.292   -9.790  -36.600  1.00 19.49 ? 75  PHE A CG  1 
ATOM   608  C CD1 . PHE A 1 79  ? 1.429   -10.367 -35.677  1.00 25.22 ? 75  PHE A CD1 1 
ATOM   609  C CD2 . PHE A 1 79  ? 3.070   -10.616 -37.387  1.00 24.52 ? 75  PHE A CD2 1 
ATOM   610  C CE1 . PHE A 1 79  ? 1.348   -11.743 -35.542  1.00 28.46 ? 75  PHE A CE1 1 
ATOM   611  C CE2 . PHE A 1 79  ? 2.988   -11.991 -37.258  1.00 26.45 ? 75  PHE A CE2 1 
ATOM   612  C CZ  . PHE A 1 79  ? 2.125   -12.554 -36.332  1.00 30.00 ? 75  PHE A CZ  1 
ATOM   613  N N   . LYS A 1 80  ? 4.728   -6.071  -37.024  1.00 18.87 ? 76  LYS A N   1 
ATOM   614  C CA  . LYS A 1 80  ? 5.002   -4.784  -37.648  1.00 18.82 ? 76  LYS A CA  1 
ATOM   615  C C   . LYS A 1 80  ? 4.597   -4.833  -39.115  1.00 17.67 ? 76  LYS A C   1 
ATOM   616  O O   . LYS A 1 80  ? 5.010   -5.738  -39.853  1.00 18.98 ? 76  LYS A O   1 
ATOM   617  C CB  . LYS A 1 80  ? 6.480   -4.404  -37.521  1.00 21.81 ? 76  LYS A CB  1 
ATOM   618  C CG  . LYS A 1 80  ? 6.855   -3.085  -38.172  1.00 26.49 ? 76  LYS A CG  1 
ATOM   619  C CD  . LYS A 1 80  ? 8.363   -2.881  -38.185  1.00 35.71 ? 76  LYS A CD  1 
ATOM   620  C CE  . LYS A 1 80  ? 8.884   -2.580  -36.787  1.00 38.47 ? 76  LYS A CE  1 
ATOM   621  N NZ  . LYS A 1 80  ? 10.370  -2.532  -36.766  1.00 40.48 ? 76  LYS A NZ  1 
ATOM   622  N N   . ILE A 1 81  ? 3.817   -3.850  -39.544  1.00 17.01 ? 77  ILE A N   1 
ATOM   623  C CA  . ILE A 1 81  ? 3.465   -3.684  -40.954  1.00 18.63 ? 77  ILE A CA  1 
ATOM   624  C C   . ILE A 1 81  ? 4.363   -2.589  -41.502  1.00 18.01 ? 77  ILE A C   1 
ATOM   625  O O   . ILE A 1 81  ? 4.363   -1.472  -40.976  1.00 18.22 ? 77  ILE A O   1 
ATOM   626  C CB  . ILE A 1 81  ? 1.989   -3.282  -41.116  1.00 19.92 ? 77  ILE A CB  1 
ATOM   627  C CG1 . ILE A 1 81  ? 1.061   -4.223  -40.335  1.00 30.48 ? 77  ILE A CG1 1 
ATOM   628  C CG2 . ILE A 1 81  ? 1.626   -3.147  -42.607  1.00 22.89 ? 77  ILE A CG2 1 
ATOM   629  C CD1 . ILE A 1 81  ? 1.207   -5.680  -40.696  1.00 31.13 ? 77  ILE A CD1 1 
ATOM   630  N N   . LYS A 1 82  ? 5.119   -2.888  -42.553  1.00 16.94 ? 78  LYS A N   1 
ATOM   631  C CA  . LYS A 1 82  ? 6.046   -1.930  -43.143  1.00 16.26 ? 78  LYS A CA  1 
ATOM   632  C C   . LYS A 1 82  ? 5.575   -1.580  -44.549  1.00 17.57 ? 78  LYS A C   1 
ATOM   633  O O   . LYS A 1 82  ? 5.398   -2.471  -45.381  1.00 18.84 ? 78  LYS A O   1 
ATOM   634  C CB  . LYS A 1 82  ? 7.446   -2.541  -43.224  1.00 19.28 ? 78  LYS A CB  1 
ATOM   635  C CG  . LYS A 1 82  ? 7.961   -3.025  -41.895  1.00 21.29 ? 78  LYS A CG  1 
ATOM   636  C CD  . LYS A 1 82  ? 9.355   -3.633  -41.991  1.00 25.89 ? 78  LYS A CD  1 
ATOM   637  C CE  . LYS A 1 82  ? 10.411  -2.577  -42.272  1.00 36.01 ? 78  LYS A CE  1 
ATOM   638  N NZ  . LYS A 1 82  ? 11.792  -3.140  -42.165  1.00 46.54 ? 78  LYS A NZ  1 
ATOM   639  N N   . ALA A 1 83  ? 5.420   -0.291  -44.842  1.00 16.37 ? 79  ALA A N   1 
ATOM   640  C CA  . ALA A 1 83  ? 4.919   0.106   -46.154  1.00 17.92 ? 79  ALA A CA  1 
ATOM   641  C C   . ALA A 1 83  ? 5.398   1.514   -46.466  1.00 15.59 ? 79  ALA A C   1 
ATOM   642  O O   . ALA A 1 83  ? 5.218   2.414   -45.644  1.00 16.76 ? 79  ALA A O   1 
ATOM   643  C CB  . ALA A 1 83  ? 3.389   0.083   -46.150  1.00 18.63 ? 79  ALA A CB  1 
ATOM   644  N N   . GLY A 1 84  ? 6.015   1.701   -47.627  1.00 18.44 ? 80  GLY A N   1 
ATOM   645  C CA  . GLY A 1 84  ? 6.387   3.048   -48.049  1.00 20.82 ? 80  GLY A CA  1 
ATOM   646  C C   . GLY A 1 84  ? 7.343   3.777   -47.135  1.00 20.78 ? 80  GLY A C   1 
ATOM   647  O O   . GLY A 1 84  ? 7.309   5.009   -47.077  1.00 24.05 ? 80  GLY A O   1 
ATOM   648  N N   . GLY A 1 85  ? 8.187   3.052   -46.406  1.00 17.54 ? 81  GLY A N   1 
ATOM   649  C CA  . GLY A 1 85  ? 9.091   3.656   -45.445  1.00 17.96 ? 81  GLY A CA  1 
ATOM   650  C C   . GLY A 1 85  ? 8.483   4.004   -44.105  1.00 18.41 ? 81  GLY A C   1 
ATOM   651  O O   . GLY A 1 85  ? 9.194   4.532   -43.240  1.00 23.17 ? 81  GLY A O   1 
ATOM   652  N N   . LYS A 1 86  ? 7.206   3.693   -43.886  1.00 18.08 ? 82  LYS A N   1 
ATOM   653  C CA  . LYS A 1 86  ? 6.547   3.846   -42.600  1.00 18.58 ? 82  LYS A CA  1 
ATOM   654  C C   . LYS A 1 86  ? 6.290   2.467   -42.017  1.00 16.17 ? 82  LYS A C   1 
ATOM   655  O O   . LYS A 1 86  ? 6.309   1.463   -42.731  1.00 16.80 ? 82  LYS A O   1 
ATOM   656  C CB  . LYS A 1 86  ? 5.212   4.580   -42.761  1.00 21.02 ? 82  LYS A CB  1 
ATOM   657  C CG  . LYS A 1 86  ? 5.325   5.986   -43.341  1.00 25.46 ? 82  LYS A CG  1 
ATOM   658  C CD  . LYS A 1 86  ? 6.169   6.900   -42.482  1.00 33.07 ? 82  LYS A CD  1 
ATOM   659  C CE  . LYS A 1 86  ? 5.362   7.635   -41.434  1.00 40.96 ? 82  LYS A CE  1 
ATOM   660  N NZ  . LYS A 1 86  ? 6.153   8.777   -40.889  1.00 42.80 ? 82  LYS A NZ  1 
ATOM   661  N N   . GLU A 1 87  ? 5.993   2.426   -40.720  1.00 17.25 ? 83  GLU A N   1 
ATOM   662  C CA  . GLU A 1 87  ? 5.673   1.157   -40.090  1.00 16.55 ? 83  GLU A CA  1 
ATOM   663  C C   . GLU A 1 87  ? 4.689   1.399   -38.959  1.00 17.44 ? 83  GLU A C   1 
ATOM   664  O O   . GLU A 1 87  ? 4.686   2.469   -38.340  1.00 20.13 ? 83  GLU A O   1 
ATOM   665  C CB  . GLU A 1 87  ? 6.920   0.462   -39.543  1.00 21.60 ? 83  GLU A CB  1 
ATOM   666  C CG  . GLU A 1 87  ? 7.598   1.237   -38.445  1.00 28.04 ? 83  GLU A CG  1 
ATOM   667  C CD  . GLU A 1 87  ? 8.845   0.545   -37.933  1.00 36.18 ? 83  GLU A CD  1 
ATOM   668  O OE1 . GLU A 1 87  ? 9.637   0.043   -38.759  1.00 36.20 ? 83  GLU A OE1 1 
ATOM   669  O OE2 . GLU A 1 87  ? 9.028   0.493   -36.703  1.00 39.33 ? 83  GLU A OE2 1 
ATOM   670  N N   . VAL A 1 88  ? 3.863   0.394   -38.689  1.00 16.41 ? 84  VAL A N   1 
ATOM   671  C CA  . VAL A 1 88  ? 2.959   0.414   -37.540  1.00 15.28 ? 84  VAL A CA  1 
ATOM   672  C C   . VAL A 1 88  ? 3.019   -0.947  -36.851  1.00 15.81 ? 84  VAL A C   1 
ATOM   673  O O   . VAL A 1 88  ? 3.054   -1.990  -37.519  1.00 16.57 ? 84  VAL A O   1 
ATOM   674  C CB  . VAL A 1 88  ? 1.530   0.855   -37.947  1.00 15.38 ? 84  VAL A CB  1 
ATOM   675  C CG1 . VAL A 1 88  ? 0.892   -0.138  -38.878  1.00 16.22 ? 84  VAL A CG1 1 
ATOM   676  C CG2 . VAL A 1 88  ? 0.643   1.088   -36.706  1.00 16.22 ? 84  VAL A CG2 1 
ATOM   677  N N   . ILE A 1 89  ? 3.024   -0.934  -35.518  1.00 15.85 ? 85  ILE A N   1 
ATOM   678  C CA  . ILE A 1 89  ? 3.113   -2.154  -34.722  1.00 16.52 ? 85  ILE A CA  1 
ATOM   679  C C   . ILE A 1 89  ? 1.756   -2.408  -34.076  1.00 17.39 ? 85  ILE A C   1 
ATOM   680  O O   . ILE A 1 89  ? 1.245   -1.561  -33.326  1.00 17.06 ? 85  ILE A O   1 
ATOM   681  C CB  . ILE A 1 89  ? 4.244   -2.097  -33.686  1.00 17.54 ? 85  ILE A CB  1 
ATOM   682  C CG1 . ILE A 1 89  ? 5.577   -1.772  -34.372  1.00 20.46 ? 85  ILE A CG1 1 
ATOM   683  C CG2 . ILE A 1 89  ? 4.311   -3.420  -32.921  1.00 18.44 ? 85  ILE A CG2 1 
ATOM   684  C CD1 . ILE A 1 89  ? 6.693   -1.479  -33.379  1.00 22.61 ? 85  ILE A CD1 1 
ATOM   685  N N   . VAL A 1 90  ? 1.169   -3.568  -34.392  1.00 17.59 ? 86  VAL A N   1 
ATOM   686  C CA  . VAL A 1 90  ? -0.180  -3.949  -33.991  1.00 17.88 ? 86  VAL A CA  1 
ATOM   687  C C   . VAL A 1 90  ? -0.148  -5.306  -33.293  1.00 21.63 ? 86  VAL A C   1 
ATOM   688  O O   . VAL A 1 90  ? 0.792   -6.085  -33.440  1.00 19.52 ? 86  VAL A O   1 
ATOM   689  C CB  . VAL A 1 90  ? -1.134  -3.991  -35.210  1.00 20.94 ? 86  VAL A CB  1 
ATOM   690  C CG1 . VAL A 1 90  ? -1.098  -2.679  -35.968  1.00 21.62 ? 86  VAL A CG1 1 
ATOM   691  C CG2 . VAL A 1 90  ? -0.776  -5.149  -36.143  1.00 23.43 ? 86  VAL A CG2 1 
ATOM   692  N N   . THR A 1 91  ? -1.178  -5.579  -32.495  1.00 19.92 ? 87  THR A N   1 
ATOM   693  C CA  . THR A 1 91  ? -1.307  -6.928  -31.952  1.00 21.68 ? 87  THR A CA  1 
ATOM   694  C C   . THR A 1 91  ? -1.789  -7.912  -33.017  1.00 19.90 ? 87  THR A C   1 
ATOM   695  O O   . THR A 1 91  ? -2.343  -7.542  -34.062  1.00 24.15 ? 87  THR A O   1 
ATOM   696  C CB  . THR A 1 91  ? -2.263  -7.004  -30.763  1.00 28.41 ? 87  THR A CB  1 
ATOM   697  O OG1 . THR A 1 91  ? -3.589  -6.715  -31.207  1.00 30.44 ? 87  THR A OG1 1 
ATOM   698  C CG2 . THR A 1 91  ? -1.860  -6.041  -29.642  1.00 26.24 ? 87  THR A CG2 1 
ATOM   699  N N   . ALA A 1 92  ? -1.575  -9.198  -32.723  1.00 21.47 ? 88  ALA A N   1 
ATOM   700  C CA  . ALA A 1 92  ? -1.928  -10.254 -33.671  1.00 22.16 ? 88  ALA A CA  1 
ATOM   701  C C   . ALA A 1 92  ? -3.434  -10.339 -33.886  1.00 25.41 ? 88  ALA A C   1 
ATOM   702  O O   . ALA A 1 92  ? -3.893  -10.779 -34.948  1.00 28.09 ? 88  ALA A O   1 
ATOM   703  C CB  . ALA A 1 92  ? -1.397  -11.599 -33.175  1.00 27.77 ? 88  ALA A CB  1 
ATOM   704  N N   . ASP A 1 93  ? -4.217  -9.955  -32.882  1.00 28.34 ? 89  ASP A N   1 
ATOM   705  C CA  . ASP A 1 93  ? -5.669  -10.027 -32.944  1.00 39.46 ? 89  ASP A CA  1 
ATOM   706  C C   . ASP A 1 93  ? -6.290  -8.780  -33.553  1.00 34.95 ? 89  ASP A C   1 
ATOM   707  O O   . ASP A 1 93  ? -7.505  -8.749  -33.767  1.00 39.62 ? 89  ASP A O   1 
ATOM   708  C CB  . ASP A 1 93  ? -6.239  -10.265 -31.539  1.00 50.56 ? 89  ASP A CB  1 
ATOM   709  C CG  . ASP A 1 93  ? -5.475  -11.342 -30.774  1.00 59.65 ? 89  ASP A CG  1 
ATOM   710  O OD1 . ASP A 1 93  ? -5.345  -12.480 -31.291  1.00 62.25 ? 89  ASP A OD1 1 
ATOM   711  O OD2 . ASP A 1 93  ? -4.994  -11.062 -29.659  1.00 61.93 ? 89  ASP A OD2 1 
ATOM   712  N N   . HIS A 1 94  ? -5.487  -7.767  -33.864  1.00 28.11 ? 90  HIS A N   1 
ATOM   713  C CA  . HIS A 1 94  ? -6.005  -6.504  -34.356  1.00 27.68 ? 90  HIS A CA  1 
ATOM   714  C C   . HIS A 1 94  ? -5.930  -6.438  -35.874  1.00 28.12 ? 90  HIS A C   1 
ATOM   715  O O   . HIS A 1 94  ? -4.978  -6.929  -36.483  1.00 36.89 ? 90  HIS A O   1 
ATOM   716  C CB  . HIS A 1 94  ? -5.269  -5.314  -33.758  1.00 30.13 ? 90  HIS A CB  1 
ATOM   717  C CG  . HIS A 1 94  ? -5.960  -4.019  -34.030  1.00 34.39 ? 90  HIS A CG  1 
ATOM   718  N ND1 . HIS A 1 94  ? -7.070  -3.606  -33.325  1.00 40.65 ? 90  HIS A ND1 1 
ATOM   719  C CD2 . HIS A 1 94  ? -5.756  -3.087  -34.987  1.00 35.93 ? 90  HIS A CD2 1 
ATOM   720  C CE1 . HIS A 1 94  ? -7.484  -2.444  -33.799  1.00 36.24 ? 90  HIS A CE1 1 
ATOM   721  N NE2 . HIS A 1 94  ? -6.700  -2.104  -34.806  1.00 37.27 ? 90  HIS A NE2 1 
ATOM   722  N N   . SER A 1 95  ? -6.944  -5.829  -36.473  1.00 24.18 ? 91  SER A N   1 
ATOM   723  C CA  . SER A 1 95  ? -7.073  -5.752  -37.918  1.00 24.36 ? 91  SER A CA  1 
ATOM   724  C C   . SER A 1 95  ? -6.377  -4.527  -38.488  1.00 23.08 ? 91  SER A C   1 
ATOM   725  O O   . SER A 1 95  ? -6.453  -3.422  -37.931  1.00 24.17 ? 91  SER A O   1 
ATOM   726  C CB  . SER A 1 95  ? -8.549  -5.723  -38.307  1.00 30.22 ? 91  SER A CB  1 
ATOM   727  O OG  . SER A 1 95  ? -9.105  -7.023  -38.230  1.00 39.08 ? 91  SER A OG  1 
ATOM   728  N N   . VAL A 1 96  ? -5.714  -4.737  -39.606  1.00 23.98 ? 92  VAL A N   1 
ATOM   729  C CA  . VAL A 1 96  ? -5.163  -3.687  -40.440  1.00 21.22 ? 92  VAL A CA  1 
ATOM   730  C C   . VAL A 1 96  ? -6.078  -3.573  -41.642  1.00 20.99 ? 92  VAL A C   1 
ATOM   731  O O   . VAL A 1 96  ? -6.688  -4.555  -42.081  1.00 24.82 ? 92  VAL A O   1 
ATOM   732  C CB  . VAL A 1 96  ? -3.724  -4.073  -40.847  1.00 25.02 ? 92  VAL A CB  1 
ATOM   733  C CG1 . VAL A 1 96  ? -3.112  -3.053  -41.819  1.00 24.23 ? 92  VAL A CG1 1 
ATOM   734  C CG2 . VAL A 1 96  ? -2.843  -4.205  -39.603  1.00 26.73 ? 92  VAL A CG2 1 
ATOM   735  N N   . MET A 1 97  ? -6.207  -2.376  -42.175  1.00 18.68 ? 93  MET A N   1 
ATOM   736  C CA  . MET A 1 97  ? -7.021  -2.216  -43.364  1.00 17.33 ? 93  MET A CA  1 
ATOM   737  C C   . MET A 1 97  ? -6.210  -2.582  -44.599  1.00 18.61 ? 93  MET A C   1 
ATOM   738  O O   . MET A 1 97  ? -5.015  -2.289  -44.692  1.00 19.35 ? 93  MET A O   1 
ATOM   739  C CB  . MET A 1 97  ? -7.578  -0.796  -43.457  1.00 17.88 ? 93  MET A CB  1 
ATOM   740  C CG  . MET A 1 97  ? -8.297  -0.328  -42.189  1.00 19.39 ? 93  MET A CG  1 
ATOM   741  S SD  . MET A 1 97  ? -9.664  -1.407  -41.695  1.00 19.86 ? 93  MET A SD  1 
ATOM   742  C CE  . MET A 1 97  ? -10.806 -1.230  -43.071  1.00 20.15 ? 93  MET A CE  1 
ATOM   743  N N   . VAL A 1 98  ? -6.858  -3.263  -45.537  1.00 18.04 ? 94  VAL A N   1 
ATOM   744  C CA  . VAL A 1 98  ? -6.238  -3.578  -46.819  1.00 17.75 ? 94  VAL A CA  1 
ATOM   745  C C   . VAL A 1 98  ? -7.242  -3.331  -47.934  1.00 19.00 ? 94  VAL A C   1 
ATOM   746  O O   . VAL A 1 98  ? -8.456  -3.425  -47.735  1.00 21.37 ? 94  VAL A O   1 
ATOM   747  C CB  . VAL A 1 98  ? -5.684  -5.029  -46.920  1.00 21.55 ? 94  VAL A CB  1 
ATOM   748  C CG1 . VAL A 1 98  ? -4.619  -5.290  -45.877  1.00 24.25 ? 94  VAL A CG1 1 
ATOM   749  C CG2 . VAL A 1 98  ? -6.790  -6.064  -46.819  1.00 23.87 ? 94  VAL A CG2 1 
ATOM   750  N N   . LYS A 1 99  ? -6.724  -2.989  -49.107  1.00 21.62 ? 95  LYS A N   1 
ATOM   751  C CA  . LYS A 1 99  ? -7.509  -3.067  -50.334  1.00 22.96 ? 95  LYS A CA  1 
ATOM   752  C C   . LYS A 1 99  ? -7.332  -4.463  -50.905  1.00 22.78 ? 95  LYS A C   1 
ATOM   753  O O   . LYS A 1 99  ? -6.210  -4.867  -51.228  1.00 22.50 ? 95  LYS A O   1 
ATOM   754  C CB  . LYS A 1 99  ? -7.086  -2.007  -51.346  1.00 24.55 ? 95  LYS A CB  1 
ATOM   755  C CG  . LYS A 1 99  ? -8.054  -1.930  -52.533  1.00 31.13 ? 95  LYS A CG  1 
ATOM   756  C CD  . LYS A 1 99  ? -7.986  -0.582  -53.237  1.00 34.89 ? 95  LYS A CD  1 
ATOM   757  C CE  . LYS A 1 99  ? -9.022  -0.495  -54.351  1.00 39.71 ? 95  LYS A CE  1 
ATOM   758  N NZ  . LYS A 1 99  ? -8.861  0.761   -55.135  1.00 45.45 ? 95  LYS A NZ  1 
ATOM   759  N N   . ARG A 1 100 ? -8.434  -5.199  -50.998  1.00 22.60 ? 96  ARG A N   1 
ATOM   760  C CA  . ARG A 1 100 ? -8.441  -6.555  -51.521  1.00 23.54 ? 96  ARG A CA  1 
ATOM   761  C C   . ARG A 1 100 ? -9.575  -6.640  -52.527  1.00 27.09 ? 96  ARG A C   1 
ATOM   762  O O   . ARG A 1 100 ? -10.734 -6.394  -52.178  1.00 28.13 ? 96  ARG A O   1 
ATOM   763  C CB  . ARG A 1 100 ? -8.673  -7.552  -50.383  1.00 23.82 ? 96  ARG A CB  1 
ATOM   764  C CG  . ARG A 1 100 ? -8.930  -8.983  -50.836  1.00 25.67 ? 96  ARG A CG  1 
ATOM   765  C CD  . ARG A 1 100 ? -9.044  -9.950  -49.648  1.00 26.66 ? 96  ARG A CD  1 
ATOM   766  N NE  . ARG A 1 100 ? -7.845  -10.004 -48.803  1.00 28.08 ? 96  ARG A NE  1 
ATOM   767  C CZ  . ARG A 1 100 ? -7.756  -10.716 -47.684  1.00 24.06 ? 96  ARG A CZ  1 
ATOM   768  N NH1 . ARG A 1 100 ? -8.804  -11.414 -47.257  1.00 29.90 ? 96  ARG A NH1 1 
ATOM   769  N NH2 . ARG A 1 100 ? -6.624  -10.728 -46.986  1.00 28.29 ? 96  ARG A NH2 1 
ATOM   770  N N   . ASP A 1 101 ? -9.237  -6.976  -53.769  1.00 27.49 ? 97  ASP A N   1 
ATOM   771  C CA  . ASP A 1 101 ? -10.244 -7.181  -54.805  1.00 33.90 ? 97  ASP A CA  1 
ATOM   772  C C   . ASP A 1 101 ? -11.159 -5.964  -54.931  1.00 36.63 ? 97  ASP A C   1 
ATOM   773  O O   . ASP A 1 101 ? -12.382 -6.084  -55.018  1.00 35.52 ? 97  ASP A O   1 
ATOM   774  C CB  . ASP A 1 101 ? -11.033 -8.467  -54.554  1.00 41.22 ? 97  ASP A CB  1 
ATOM   775  C CG  . ASP A 1 101 ? -10.154 -9.707  -54.590  1.00 41.01 ? 97  ASP A CG  1 
ATOM   776  O OD1 . ASP A 1 101 ? -9.241  -9.763  -55.441  1.00 40.34 ? 97  ASP A OD1 1 
ATOM   777  O OD2 . ASP A 1 101 ? -10.365 -10.615 -53.753  1.00 42.60 ? 97  ASP A OD2 1 
ATOM   778  N N   . GLY A 1 102 ? -10.559 -4.775  -54.904  1.00 31.81 ? 98  GLY A N   1 
ATOM   779  C CA  . GLY A 1 102 ? -11.294 -3.541  -55.095  1.00 32.31 ? 98  GLY A CA  1 
ATOM   780  C C   . GLY A 1 102 ? -12.012 -2.986  -53.879  1.00 33.34 ? 98  GLY A C   1 
ATOM   781  O O   . GLY A 1 102 ? -12.645 -1.927  -53.990  1.00 35.18 ? 98  GLY A O   1 
ATOM   782  N N   . LYS A 1 103 ? -11.935 -3.642  -52.724  1.00 27.07 ? 99  LYS A N   1 
ATOM   783  C CA  . LYS A 1 103 ? -12.645 -3.185  -51.539  1.00 27.70 ? 99  LYS A CA  1 
ATOM   784  C C   . LYS A 1 103 ? -11.672 -2.987  -50.389  1.00 26.20 ? 99  LYS A C   1 
ATOM   785  O O   . LYS A 1 103 ? -10.714 -3.747  -50.228  1.00 28.83 ? 99  LYS A O   1 
ATOM   786  C CB  . LYS A 1 103 ? -13.693 -4.205  -51.082  1.00 34.95 ? 99  LYS A CB  1 
ATOM   787  C CG  . LYS A 1 103 ? -14.729 -4.578  -52.120  1.00 44.48 ? 99  LYS A CG  1 
ATOM   788  C CD  . LYS A 1 103 ? -15.931 -3.651  -52.081  1.00 46.23 ? 99  LYS A CD  1 
ATOM   789  C CE  . LYS A 1 103 ? -16.847 -3.910  -53.270  1.00 52.23 ? 99  LYS A CE  1 
ATOM   790  N NZ  . LYS A 1 103 ? -17.833 -2.812  -53.463  1.00 53.99 ? 99  LYS A NZ  1 
ATOM   791  N N   . ILE A 1 104 ? -11.961 -1.993  -49.557  1.00 24.82 ? 100 ILE A N   1 
ATOM   792  C CA  . ILE A 1 104 ? -11.163 -1.738  -48.366  1.00 25.50 ? 100 ILE A CA  1 
ATOM   793  C C   . ILE A 1 104 ? -11.809 -2.481  -47.205  1.00 26.70 ? 100 ILE A C   1 
ATOM   794  O O   . ILE A 1 104 ? -12.970 -2.225  -46.863  1.00 29.54 ? 100 ILE A O   1 
ATOM   795  C CB  . ILE A 1 104 ? -11.051 -0.235  -48.078  1.00 27.24 ? 100 ILE A CB  1 
ATOM   796  C CG1 . ILE A 1 104 ? -10.278 0.475   -49.190  1.00 25.11 ? 100 ILE A CG1 1 
ATOM   797  C CG2 . ILE A 1 104 ? -10.343 -0.010  -46.762  1.00 25.21 ? 100 ILE A CG2 1 
ATOM   798  C CD1 . ILE A 1 104 ? -10.237 1.986   -49.038  1.00 31.36 ? 100 ILE A CD1 1 
ATOM   799  N N   . ILE A 1 105 ? -11.069 -3.426  -46.618  1.00 27.38 ? 101 ILE A N   1 
ATOM   800  C CA  . ILE A 1 105 ? -11.573 -4.328  -45.591  1.00 26.69 ? 101 ILE A CA  1 
ATOM   801  C C   . ILE A 1 105 ? -10.548 -4.436  -44.472  1.00 25.52 ? 101 ILE A C   1 
ATOM   802  O O   . ILE A 1 105 ? -9.395  -4.030  -44.618  1.00 23.91 ? 101 ILE A O   1 
ATOM   803  C CB  . ILE A 1 105 ? -11.876 -5.726  -46.157  1.00 25.15 ? 101 ILE A CB  1 
ATOM   804  C CG1 . ILE A 1 105 ? -10.615 -6.327  -46.793  1.00 28.11 ? 101 ILE A CG1 1 
ATOM   805  C CG2 . ILE A 1 105 ? -12.983 -5.656  -47.201  1.00 28.60 ? 101 ILE A CG2 1 
ATOM   806  C CD1 . ILE A 1 105 ? -10.717 -7.812  -47.068  1.00 31.76 ? 101 ILE A CD1 1 
ATOM   807  N N   . ASP A 1 106 ? -10.974 -5.006  -43.346  1.00 24.46 ? 102 ASP A N   1 
ATOM   808  C CA  . ASP A 1 106 ? -10.100 -5.219  -42.195  1.00 24.77 ? 102 ASP A CA  1 
ATOM   809  C C   . ASP A 1 106 ? -9.669  -6.686  -42.127  1.00 27.87 ? 102 ASP A C   1 
ATOM   810  O O   . ASP A 1 106 ? -10.501 -7.591  -42.247  1.00 28.47 ? 102 ASP A O   1 
ATOM   811  C CB  . ASP A 1 106 ? -10.796 -4.782  -40.903  1.00 29.20 ? 102 ASP A CB  1 
ATOM   812  C CG  . ASP A 1 106 ? -12.047 -5.582  -40.609  1.00 41.33 ? 102 ASP A CG  1 
ATOM   813  O OD1 . ASP A 1 106 ? -13.058 -5.382  -41.320  1.00 37.61 ? 102 ASP A OD1 1 
ATOM   814  O OD2 . ASP A 1 106 ? -12.025 -6.398  -39.659  1.00 41.56 ? 102 ASP A OD2 1 
ATOM   815  N N   . VAL A 1 107 ? -8.365  -6.914  -41.940  1.00 25.72 ? 103 VAL A N   1 
ATOM   816  C CA  . VAL A 1 107 ? -7.796  -8.258  -41.885  1.00 26.99 ? 103 VAL A CA  1 
ATOM   817  C C   . VAL A 1 107 ? -6.732  -8.315  -40.795  1.00 25.88 ? 103 VAL A C   1 
ATOM   818  O O   . VAL A 1 107 ? -6.022  -7.337  -40.545  1.00 29.11 ? 103 VAL A O   1 
ATOM   819  C CB  . VAL A 1 107 ? -7.174  -8.680  -43.237  1.00 29.55 ? 103 VAL A CB  1 
ATOM   820  C CG1 . VAL A 1 107 ? -8.220  -8.702  -44.337  1.00 30.61 ? 103 VAL A CG1 1 
ATOM   821  C CG2 . VAL A 1 107 ? -6.037  -7.748  -43.611  1.00 34.84 ? 103 VAL A CG2 1 
ATOM   822  N N   . LYS A 1 108 ? -6.608  -9.484  -40.161  1.00 24.11 ? 104 LYS A N   1 
ATOM   823  C CA  . LYS A 1 108 ? -5.557  -9.698  -39.178  1.00 23.14 ? 104 LYS A CA  1 
ATOM   824  C C   . LYS A 1 108 ? -4.181  -9.821  -39.850  1.00 22.95 ? 104 LYS A C   1 
ATOM   825  O O   . LYS A 1 108 ? -4.074  -10.248 -41.005  1.00 23.29 ? 104 LYS A O   1 
ATOM   826  C CB  . LYS A 1 108 ? -5.839  -10.961 -38.366  1.00 28.91 ? 104 LYS A CB  1 
ATOM   827  C CG  . LYS A 1 108 ? -7.254  -11.060 -37.771  1.00 34.38 ? 104 LYS A CG  1 
ATOM   828  C CD  . LYS A 1 108 ? -7.599  -9.879  -36.875  1.00 41.94 ? 104 LYS A CD  1 
ATOM   829  C CE  . LYS A 1 108 ? -9.103  -9.811  -36.598  1.00 46.09 ? 104 LYS A CE  1 
ATOM   830  N NZ  . LYS A 1 108 ? -9.489  -8.489  -36.016  1.00 44.39 ? 104 LYS A NZ  1 
ATOM   831  N N   . PRO A 1 109 ? -3.110  -9.433  -39.144  1.00 22.47 ? 105 PRO A N   1 
ATOM   832  C CA  . PRO A 1 109 ? -1.760  -9.517  -39.730  1.00 22.36 ? 105 PRO A CA  1 
ATOM   833  C C   . PRO A 1 109 ? -1.321  -10.922 -40.091  1.00 23.74 ? 105 PRO A C   1 
ATOM   834  O O   . PRO A 1 109 ? -0.287  -11.070 -40.756  1.00 25.97 ? 105 PRO A O   1 
ATOM   835  C CB  . PRO A 1 109 ? -0.849  -8.853  -38.684  1.00 24.68 ? 105 PRO A CB  1 
ATOM   836  C CG  . PRO A 1 109 ? -1.641  -8.802  -37.444  1.00 23.93 ? 105 PRO A CG  1 
ATOM   837  C CD  . PRO A 1 109 ? -3.095  -8.806  -37.812  1.00 25.94 ? 105 PRO A CD  1 
ATOM   838  N N   . THR A 1 110 ? -1.974  -11.944 -39.556  1.00 24.94 ? 106 THR A N   1 
ATOM   839  C CA  . THR A 1 110 ? -1.681  -13.341 -39.853  1.00 26.52 ? 106 THR A CA  1 
ATOM   840  C C   . THR A 1 110 ? -2.471  -13.872 -41.044  1.00 27.35 ? 106 THR A C   1 
ATOM   841  O O   . THR A 1 110 ? -2.318  -15.047 -41.399  1.00 29.79 ? 106 THR A O   1 
ATOM   842  C CB  . THR A 1 110 ? -2.006  -14.196 -38.627  1.00 36.40 ? 106 THR A CB  1 
ATOM   843  O OG1 . THR A 1 110 ? -3.361  -13.948 -38.227  1.00 34.11 ? 106 THR A OG1 1 
ATOM   844  C CG2 . THR A 1 110 ? -1.073  -13.844 -37.478  1.00 39.99 ? 106 THR A CG2 1 
ATOM   845  N N   . GLU A 1 111 ? -3.372  -13.066 -41.610  1.00 26.26 ? 107 GLU A N   1 
ATOM   846  C CA  . GLU A 1 111 ? -4.244  -13.476 -42.707  1.00 30.83 ? 107 GLU A CA  1 
ATOM   847  C C   . GLU A 1 111 ? -4.085  -12.644 -43.981  1.00 28.25 ? 107 GLU A C   1 
ATOM   848  O O   . GLU A 1 111 ? -4.999  -12.611 -44.812  1.00 29.58 ? 107 GLU A O   1 
ATOM   849  C CB  . GLU A 1 111 ? -5.696  -13.618 -42.237  1.00 36.10 ? 107 GLU A CB  1 
ATOM   850  C CG  . GLU A 1 111 ? -5.853  -14.849 -41.328  1.00 48.39 ? 107 GLU A CG  1 
ATOM   851  C CD  . GLU A 1 111 ? -6.998  -14.754 -40.332  1.00 58.70 ? 107 GLU A CD  1 
ATOM   852  O OE1 . GLU A 1 111 ? -8.090  -14.277 -40.707  1.00 61.43 ? 107 GLU A OE1 1 
ATOM   853  O OE2 . GLU A 1 111 ? -6.799  -15.162 -39.166  1.00 59.95 ? 107 GLU A OE2 1 
ATOM   854  N N   . MET A 1 112 ? -2.990  -11.906 -44.118  1.00 24.95 ? 108 MET A N   1 
ATOM   855  C CA  . MET A 1 112 ? -2.784  -11.059 -45.288  1.00 24.44 ? 108 MET A CA  1 
ATOM   856  C C   . MET A 1 112 ? -2.295  -11.849 -46.502  1.00 24.99 ? 108 MET A C   1 
ATOM   857  O O   . MET A 1 112 ? -1.559  -12.835 -46.382  1.00 26.06 ? 108 MET A O   1 
ATOM   858  C CB  . MET A 1 112 ? -1.829  -9.916  -44.954  1.00 22.85 ? 108 MET A CB  1 
ATOM   859  C CG  . MET A 1 112 ? -2.343  -9.077  -43.785  1.00 24.78 ? 108 MET A CG  1 
ATOM   860  S SD  . MET A 1 112 ? -1.209  -7.847  -43.151  1.00 27.00 ? 108 MET A SD  1 
ATOM   861  C CE  . MET A 1 112 ? -1.875  -6.349  -43.887  1.00 38.33 ? 108 MET A CE  1 
ATOM   862  N N   . LYS A 1 113 ? -2.717  -11.402 -47.684  1.00 24.94 ? 109 LYS A N   1 
ATOM   863  C CA  . LYS A 1 113 ? -2.354  -12.028 -48.950  1.00 25.63 ? 109 LYS A CA  1 
ATOM   864  C C   . LYS A 1 113 ? -1.322  -11.185 -49.687  1.00 24.54 ? 109 LYS A C   1 
ATOM   865  O O   . LYS A 1 113 ? -1.215  -9.975  -49.486  1.00 23.36 ? 109 LYS A O   1 
ATOM   866  C CB  . LYS A 1 113 ? -3.574  -12.146 -49.869  1.00 26.40 ? 109 LYS A CB  1 
ATOM   867  C CG  . LYS A 1 113 ? -4.737  -12.966 -49.344  1.00 33.74 ? 109 LYS A CG  1 
ATOM   868  C CD  . LYS A 1 113 ? -5.914  -12.810 -50.301  1.00 38.96 ? 109 LYS A CD  1 
ATOM   869  C CE  . LYS A 1 113 ? -6.944  -13.900 -50.130  1.00 47.92 ? 109 LYS A CE  1 
ATOM   870  N NZ  . LYS A 1 113 ? -6.950  -14.398 -48.738  1.00 52.00 ? 109 LYS A NZ  1 
ATOM   871  N N   . GLN A 1 114 ? -0.562  -11.848 -50.569  1.00 29.99 ? 110 GLN A N   1 
ATOM   872  C CA  . GLN A 1 114 ? 0.454   -11.143 -51.344  1.00 33.39 ? 110 GLN A CA  1 
ATOM   873  C C   . GLN A 1 114 ? -0.153  -10.111 -52.288  1.00 30.05 ? 110 GLN A C   1 
ATOM   874  O O   . GLN A 1 114 ? 0.495   -9.105  -52.593  1.00 30.07 ? 110 GLN A O   1 
ATOM   875  C CB  . GLN A 1 114 ? 1.310   -12.144 -52.128  1.00 41.28 ? 110 GLN A CB  1 
ATOM   876  C CG  . GLN A 1 114 ? 2.677   -11.614 -52.546  1.00 48.33 ? 110 GLN A CG  1 
ATOM   877  C CD  . GLN A 1 114 ? 3.620   -11.421 -51.365  1.00 55.84 ? 110 GLN A CD  1 
ATOM   878  O OE1 . GLN A 1 114 ? 3.857   -10.293 -50.924  1.00 53.96 ? 110 GLN A OE1 1 
ATOM   879  N NE2 . GLN A 1 114 ? 4.171   -12.522 -50.856  1.00 60.24 ? 110 GLN A NE2 1 
ATOM   880  N N   . THR A 1 115 ? -1.395  -10.312 -52.722  1.00 25.43 ? 111 THR A N   1 
ATOM   881  C CA  . THR A 1 115 ? -2.083  -9.358  -53.584  1.00 23.61 ? 111 THR A CA  1 
ATOM   882  C C   . THR A 1 115 ? -2.795  -8.253  -52.811  1.00 22.41 ? 111 THR A C   1 
ATOM   883  O O   . THR A 1 115 ? -3.328  -7.327  -53.432  1.00 29.44 ? 111 THR A O   1 
ATOM   884  C CB  . THR A 1 115 ? -3.060  -10.104 -54.494  1.00 25.11 ? 111 THR A CB  1 
ATOM   885  O OG1 . THR A 1 115 ? -3.866  -10.974 -53.683  1.00 32.25 ? 111 THR A OG1 1 
ATOM   886  C CG2 . THR A 1 115 ? -2.290  -10.933 -55.546  1.00 27.45 ? 111 THR A CG2 1 
ATOM   887  N N   . ASP A 1 116 ? -2.831  -8.331  -51.483  1.00 22.15 ? 112 ASP A N   1 
ATOM   888  C CA  . ASP A 1 116 ? -3.381  -7.253  -50.688  1.00 21.54 ? 112 ASP A CA  1 
ATOM   889  C C   . ASP A 1 116 ? -2.491  -6.019  -50.788  1.00 23.10 ? 112 ASP A C   1 
ATOM   890  O O   . ASP A 1 116 ? -1.284  -6.109  -51.030  1.00 26.05 ? 112 ASP A O   1 
ATOM   891  C CB  . ASP A 1 116 ? -3.440  -7.674  -49.221  1.00 22.32 ? 112 ASP A CB  1 
ATOM   892  C CG  . ASP A 1 116 ? -4.579  -8.645  -48.923  1.00 23.57 ? 112 ASP A CG  1 
ATOM   893  O OD1 . ASP A 1 116 ? -5.493  -8.809  -49.753  1.00 24.46 ? 112 ASP A OD1 1 
ATOM   894  O OD2 . ASP A 1 116 ? -4.541  -9.262  -47.843  1.00 23.33 ? 112 ASP A OD2 1 
ATOM   895  N N   . ARG A 1 117 ? -3.097  -4.851  -50.581  1.00 20.54 ? 113 ARG A N   1 
ATOM   896  C CA  . ARG A 1 117 ? -2.334  -3.618  -50.445  1.00 20.32 ? 113 ARG A CA  1 
ATOM   897  C C   . ARG A 1 117 ? -2.801  -2.866  -49.216  1.00 22.79 ? 113 ARG A C   1 
ATOM   898  O O   . ARG A 1 117 ? -3.993  -2.852  -48.892  1.00 22.74 ? 113 ARG A O   1 
ATOM   899  C CB  . ARG A 1 117 ? -2.472  -2.731  -51.699  1.00 20.35 ? 113 ARG A CB  1 
ATOM   900  C CG  . ARG A 1 117 ? -1.745  -3.296  -52.935  1.00 23.96 ? 113 ARG A CG  1 
ATOM   901  C CD  . ARG A 1 117 ? -1.951  -2.442  -54.192  1.00 31.82 ? 113 ARG A CD  1 
ATOM   902  N NE  . ARG A 1 117 ? -3.348  -2.405  -54.622  1.00 33.50 ? 113 ARG A NE  1 
ATOM   903  C CZ  . ARG A 1 117 ? -3.822  -1.614  -55.585  1.00 31.76 ? 113 ARG A CZ  1 
ATOM   904  N NH1 . ARG A 1 117 ? -3.008  -0.780  -56.223  1.00 29.50 ? 113 ARG A NH1 1 
ATOM   905  N NH2 . ARG A 1 117 ? -5.111  -1.646  -55.903  1.00 40.74 ? 113 ARG A NH2 1 
ATOM   906  N N   . VAL A 1 118 ? -1.866  -2.256  -48.524  1.00 17.05 ? 114 VAL A N   1 
ATOM   907  C CA  . VAL A 1 118 ? -2.248  -1.420  -47.396  1.00 17.32 ? 114 VAL A CA  1 
ATOM   908  C C   . VAL A 1 118 ? -2.607  -0.024  -47.891  1.00 16.17 ? 114 VAL A C   1 
ATOM   909  O O   . VAL A 1 118 ? -2.293  0.374   -49.024  1.00 17.29 ? 114 VAL A O   1 
ATOM   910  C CB  . VAL A 1 118 ? -1.204  -1.387  -46.263  1.00 29.00 ? 114 VAL A CB  1 
ATOM   911  C CG1 . VAL A 1 118 ? -0.983  -2.773  -45.693  1.00 26.60 ? 114 VAL A CG1 1 
ATOM   912  C CG2 . VAL A 1 118 ? 0.057   -0.827  -46.744  1.00 25.28 ? 114 VAL A CG2 1 
ATOM   913  N N   . VAL A 1 119 ? -3.334  0.698   -47.053  1.00 17.36 ? 115 VAL A N   1 
ATOM   914  C CA  . VAL A 1 119 ? -3.809  2.036   -47.364  1.00 16.80 ? 115 VAL A CA  1 
ATOM   915  C C   . VAL A 1 119 ? -2.914  3.004   -46.604  1.00 16.84 ? 115 VAL A C   1 
ATOM   916  O O   . VAL A 1 119 ? -2.898  3.003   -45.366  1.00 17.54 ? 115 VAL A O   1 
ATOM   917  C CB  . VAL A 1 119 ? -5.274  2.197   -46.941  1.00 16.81 ? 115 VAL A CB  1 
ATOM   918  C CG1 . VAL A 1 119 ? -5.800  3.556   -47.362  1.00 20.07 ? 115 VAL A CG1 1 
ATOM   919  C CG2 . VAL A 1 119 ? -6.118  1.045   -47.485  1.00 19.11 ? 115 VAL A CG2 1 
ATOM   920  N N   . LYS A 1 120 ? -2.161  3.831   -47.320  1.00 17.95 ? 116 LYS A N   1 
ATOM   921  C CA  . LYS A 1 120 ? -1.192  4.734   -46.718  1.00 18.49 ? 116 LYS A CA  1 
ATOM   922  C C   . LYS A 1 120 ? -1.545  6.180   -47.041  1.00 19.53 ? 116 LYS A C   1 
ATOM   923  O O   . LYS A 1 120 ? -1.871  6.511   -48.189  1.00 20.73 ? 116 LYS A O   1 
ATOM   924  C CB  . LYS A 1 120 ? 0.224   4.402   -47.222  1.00 19.01 ? 116 LYS A CB  1 
ATOM   925  C CG  . LYS A 1 120 ? 1.309   5.262   -46.559  1.00 22.31 ? 116 LYS A CG  1 
ATOM   926  C CD  . LYS A 1 120 ? 2.670   5.017   -47.178  1.00 26.67 ? 116 LYS A CD  1 
ATOM   927  C CE  . LYS A 1 120 ? 3.452   6.330   -47.299  1.00 39.07 ? 116 LYS A CE  1 
ATOM   928  N NZ  . LYS A 1 120 ? 2.972   7.176   -48.439  1.00 42.37 ? 116 LYS A NZ  1 
ATOM   929  N N   . TRP A 1 121 ? -1.460  7.034   -46.031  1.00 19.45 ? 117 TRP A N   1 
ATOM   930  C CA  . TRP A 1 121 ? -1.628  8.467   -46.200  1.00 20.79 ? 117 TRP A CA  1 
ATOM   931  C C   . TRP A 1 121 ? -0.566  9.008   -47.151  1.00 26.51 ? 117 TRP A C   1 
ATOM   932  O O   . TRP A 1 121 ? 0.577   8.542   -47.177  1.00 29.75 ? 117 TRP A O   1 
ATOM   933  C CB  . TRP A 1 121 ? -1.479  9.144   -44.845  1.00 20.34 ? 117 TRP A CB  1 
ATOM   934  C CG  . TRP A 1 121 ? -1.809  10.567  -44.882  1.00 21.65 ? 117 TRP A CG  1 
ATOM   935  C CD1 . TRP A 1 121 ? -0.934  11.613  -44.860  1.00 30.27 ? 117 TRP A CD1 1 
ATOM   936  C CD2 . TRP A 1 121 ? -3.112  11.127  -44.974  1.00 24.79 ? 117 TRP A CD2 1 
ATOM   937  N NE1 . TRP A 1 121 ? -1.623  12.798  -44.911  1.00 40.86 ? 117 TRP A NE1 1 
ATOM   938  C CE2 . TRP A 1 121 ? -2.965  12.526  -44.981  1.00 33.02 ? 117 TRP A CE2 1 
ATOM   939  C CE3 . TRP A 1 121 ? -4.397  10.580  -45.035  1.00 30.56 ? 117 TRP A CE3 1 
ATOM   940  C CZ2 . TRP A 1 121 ? -4.050  13.386  -45.055  1.00 40.16 ? 117 TRP A CZ2 1 
ATOM   941  C CZ3 . TRP A 1 121 ? -5.476  11.437  -45.104  1.00 35.54 ? 117 TRP A CZ3 1 
ATOM   942  C CH2 . TRP A 1 121 ? -5.294  12.824  -45.112  1.00 39.52 ? 117 TRP A CH2 1 
ATOM   943  N N   . MET A 1 122 ? -0.960  9.993   -47.954  1.00 29.98 ? 118 MET A N   1 
ATOM   944  C CA  . MET A 1 122 ? -0.081  10.590  -48.949  1.00 43.54 ? 118 MET A CA  1 
ATOM   945  C C   . MET A 1 122 ? 0.115   12.062  -48.630  1.00 52.26 ? 118 MET A C   1 
ATOM   946  O O   . MET A 1 122 ? -0.809  12.741  -48.170  1.00 54.06 ? 118 MET A O   1 
ATOM   947  C CB  . MET A 1 122 ? -0.704  10.499  -50.341  1.00 49.06 ? 118 MET A CB  1 
ATOM   948  C CG  . MET A 1 122 ? -0.652  9.133   -50.989  1.00 52.99 ? 118 MET A CG  1 
ATOM   949  S SD  . MET A 1 122 ? 0.993   8.657   -51.554  1.00 57.31 ? 118 MET A SD  1 
ATOM   950  C CE  . MET A 1 122 ? 1.488   10.133  -52.426  1.00 42.92 ? 118 MET A CE  1 
ATOM   951  N N   . LEU A 1 123 ? 1.333   12.541  -48.855  1.00 57.34 ? 119 LEU A N   1 
ATOM   952  C CA  . LEU A 1 123 ? 1.649   13.949  -48.693  1.00 65.39 ? 119 LEU A CA  1 
ATOM   953  C C   . LEU A 1 123 ? 1.618   14.718  -50.011  1.00 62.76 ? 119 LEU A C   1 
ATOM   954  O O   . LEU A 1 123 ? 1.705   15.949  -49.987  1.00 66.97 ? 119 LEU A O   1 
ATOM   955  C CB  . LEU A 1 123 ? 3.026   14.102  -48.029  1.00 70.46 ? 119 LEU A CB  1 
ATOM   956  C CG  . LEU A 1 123 ? 3.320   13.172  -46.843  1.00 72.27 ? 119 LEU A CG  1 
ATOM   957  C CD1 . LEU A 1 123 ? 4.819   12.969  -46.662  1.00 71.99 ? 119 LEU A CD1 1 
ATOM   958  C CD2 . LEU A 1 123 ? 2.693   13.698  -45.559  1.00 73.51 ? 119 LEU A CD2 1 
ATOM   959  N N   . THR A 1 124 ? 1.480   14.032  -51.151  1.00 53.93 ? 120 THR A N   1 
ATOM   960  C CA  . THR A 1 124 ? 1.635   14.652  -52.463  1.00 50.49 ? 120 THR A CA  1 
ATOM   961  C C   . THR A 1 124 ? 0.616   14.088  -53.449  1.00 50.08 ? 120 THR A C   1 
ATOM   962  O O   . THR A 1 124 ? 0.164   12.945  -53.327  1.00 40.43 ? 120 THR A O   1 
ATOM   963  C CB  . THR A 1 124 ? 3.046   14.428  -53.031  1.00 48.64 ? 120 THR A CB  1 
ATOM   964  O OG1 . THR A 1 124 ? 3.294   13.019  -53.154  1.00 48.53 ? 120 THR A OG1 1 
ATOM   965  C CG2 . THR A 1 124 ? 4.109   15.059  -52.136  1.00 44.84 ? 120 THR A CG2 1 
ATOM   966  N N   . GLY A 1 125 A 0.272   14.903  -54.450  1.00 52.03 ? 120 GLY A N   1 
ATOM   967  C CA  . GLY A 1 125 A -0.622  14.483  -55.509  1.00 52.51 ? 120 GLY A CA  1 
ATOM   968  C C   . GLY A 1 125 A -2.085  14.699  -55.165  1.00 55.78 ? 120 GLY A C   1 
ATOM   969  O O   . GLY A 1 125 A -2.455  15.051  -54.044  1.00 59.35 ? 120 GLY A O   1 
ATOM   970  N N   . SER A 1 126 B -2.936  14.472  -56.169  1.00 56.83 ? 120 SER A N   1 
ATOM   971  C CA  . SER A 1 126 B -4.360  14.773  -56.050  1.00 61.54 ? 120 SER A CA  1 
ATOM   972  C C   . SER A 1 126 B -5.064  13.841  -55.080  1.00 63.64 ? 120 SER A C   1 
ATOM   973  O O   . SER A 1 126 B -6.098  14.195  -54.513  1.00 66.03 ? 120 SER A O   1 
ATOM   974  C CB  . SER A 1 126 B -5.023  14.665  -57.420  1.00 65.12 ? 120 SER A CB  1 
ATOM   975  O OG  . SER A 1 126 B -5.036  15.917  -58.075  1.00 68.86 ? 120 SER A OG  1 
ATOM   976  N N   . HIS A 1 127 C -4.511  12.670  -54.880  1.00 60.91 ? 120 HIS A N   1 
ATOM   977  C CA  . HIS A 1 127 C -4.974  11.659  -53.955  1.00 57.34 ? 120 HIS A CA  1 
ATOM   978  C C   . HIS A 1 127 C -4.369  11.831  -52.573  1.00 47.71 ? 120 HIS A C   1 
ATOM   979  O O   . HIS A 1 127 C -3.197  12.170  -52.411  1.00 45.97 ? 120 HIS A O   1 
ATOM   980  C CB  . HIS A 1 127 C -4.586  10.339  -54.604  1.00 62.39 ? 120 HIS A CB  1 
ATOM   981  C CG  . HIS A 1 127 C -5.534  9.953   -55.689  1.00 66.63 ? 120 HIS A CG  1 
ATOM   982  N ND1 . HIS A 1 127 C -6.400  10.864  -56.270  1.00 69.55 ? 120 HIS A ND1 1 
ATOM   983  C CD2 . HIS A 1 127 C -5.584  8.830   -56.463  1.00 68.16 ? 120 HIS A CD2 1 
ATOM   984  C CE1 . HIS A 1 127 C -7.076  10.264  -57.235  1.00 70.04 ? 120 HIS A CE1 1 
ATOM   985  N NE2 . HIS A 1 127 C -6.582  9.040   -57.388  1.00 69.04 ? 120 HIS A NE2 1 
ATOM   986  N N   . MET A 1 128 ? -5.199  11.590  -51.577  1.00 38.73 ? 121 MET A N   1 
ATOM   987  C CA  . MET A 1 128 ? -4.774  11.705  -50.202  1.00 34.25 ? 121 MET A CA  1 
ATOM   988  C C   . MET A 1 128 ? -4.287  10.387  -49.651  1.00 30.69 ? 121 MET A C   1 
ATOM   989  O O   . MET A 1 128 ? -3.656  10.376  -48.597  1.00 29.18 ? 121 MET A O   1 
ATOM   990  C CB  . MET A 1 128 ? -5.894  12.296  -49.346  1.00 41.42 ? 121 MET A CB  1 
ATOM   991  C CG  . MET A 1 128 ? -6.252  13.721  -49.723  1.00 52.33 ? 121 MET A CG  1 
ATOM   992  S SD  . MET A 1 128 ? -7.735  14.331  -48.908  1.00 61.33 ? 121 MET A SD  1 
ATOM   993  C CE  . MET A 1 128 ? -7.227  14.365  -47.200  1.00 60.60 ? 121 MET A CE  1 
ATOM   994  N N   . ILE A 1 129 ? -4.536  9.287   -50.360  1.00 25.27 ? 122 ILE A N   1 
ATOM   995  C CA  . ILE A 1 129 ? -4.097  7.961   -49.958  1.00 23.01 ? 122 ILE A CA  1 
ATOM   996  C C   . ILE A 1 129 ? -3.530  7.252   -51.176  1.00 21.09 ? 122 ILE A C   1 
ATOM   997  O O   . ILE A 1 129 ? -3.805  7.610   -52.323  1.00 25.34 ? 122 ILE A O   1 
ATOM   998  C CB  . ILE A 1 129 ? -5.242  7.114   -49.351  1.00 22.23 ? 122 ILE A CB  1 
ATOM   999  C CG1 . ILE A 1 129 ? -6.450  7.082   -50.295  1.00 23.81 ? 122 ILE A CG1 1 
ATOM   1000 C CG2 . ILE A 1 129 ? -5.645  7.658   -47.983  1.00 25.13 ? 122 ILE A CG2 1 
ATOM   1001 C CD1 . ILE A 1 129 ? -7.575  6.211   -49.773  1.00 25.03 ? 122 ILE A CD1 1 
ATOM   1002 N N   . GLU A 1 130 ? -2.712  6.253   -50.902  1.00 18.96 ? 123 GLU A N   1 
ATOM   1003 C CA  . GLU A 1 130 ? -2.231  5.330   -51.910  1.00 18.72 ? 123 GLU A CA  1 
ATOM   1004 C C   . GLU A 1 130 ? -2.478  3.919   -51.414  1.00 17.06 ? 123 GLU A C   1 
ATOM   1005 O O   . GLU A 1 130 ? -2.578  3.675   -50.207  1.00 18.81 ? 123 GLU A O   1 
ATOM   1006 C CB  . GLU A 1 130 ? -0.741  5.528   -52.221  1.00 21.20 ? 123 GLU A CB  1 
ATOM   1007 C CG  . GLU A 1 130 ? 0.188   5.198   -51.063  1.00 19.78 ? 123 GLU A CG  1 
ATOM   1008 C CD  . GLU A 1 130 ? 1.670   5.335   -51.410  1.00 24.32 ? 123 GLU A CD  1 
ATOM   1009 O OE1 . GLU A 1 130 ? 2.092   5.016   -52.537  1.00 27.30 ? 123 GLU A OE1 1 
ATOM   1010 O OE2 . GLU A 1 130 ? 2.434   5.769   -50.525  1.00 25.80 ? 123 GLU A OE2 1 
ATOM   1011 N N   . PHE A 1 131 ? -2.537  2.982   -52.353  1.00 17.98 ? 124 PHE A N   1 
ATOM   1012 C CA  . PHE A 1 131 ? -2.638  1.558   -52.049  1.00 17.71 ? 124 PHE A CA  1 
ATOM   1013 C C   . PHE A 1 131 ? -1.293  0.960   -52.415  1.00 17.11 ? 124 PHE A C   1 
ATOM   1014 O O   . PHE A 1 131 ? -0.895  1.002   -53.587  1.00 19.35 ? 124 PHE A O   1 
ATOM   1015 C CB  . PHE A 1 131 ? -3.773  0.941   -52.862  1.00 19.37 ? 124 PHE A CB  1 
ATOM   1016 C CG  . PHE A 1 131 ? -5.077  1.657   -52.660  1.00 19.85 ? 124 PHE A CG  1 
ATOM   1017 C CD1 . PHE A 1 131 ? -5.687  1.654   -51.428  1.00 21.75 ? 124 PHE A CD1 1 
ATOM   1018 C CD2 . PHE A 1 131 ? -5.669  2.371   -53.692  1.00 24.14 ? 124 PHE A CD2 1 
ATOM   1019 C CE1 . PHE A 1 131 ? -6.883  2.332   -51.212  1.00 23.91 ? 124 PHE A CE1 1 
ATOM   1020 C CE2 . PHE A 1 131 ? -6.870  3.049   -53.478  1.00 27.14 ? 124 PHE A CE2 1 
ATOM   1021 C CZ  . PHE A 1 131 ? -7.469  3.027   -52.239  1.00 26.78 ? 124 PHE A CZ  1 
ATOM   1022 N N   . ILE A 1 132 ? -0.590  0.414   -51.427  1.00 17.13 ? 125 ILE A N   1 
ATOM   1023 C CA  . ILE A 1 132 ? 0.837   0.156   -51.550  1.00 16.95 ? 125 ILE A CA  1 
ATOM   1024 C C   . ILE A 1 132 ? 1.163   -1.253  -51.082  1.00 17.46 ? 125 ILE A C   1 
ATOM   1025 O O   . ILE A 1 132 ? 0.520   -1.803  -50.186  1.00 17.56 ? 125 ILE A O   1 
ATOM   1026 C CB  . ILE A 1 132 ? 1.666   1.221   -50.781  1.00 18.14 ? 125 ILE A CB  1 
ATOM   1027 C CG1 . ILE A 1 132 ? 3.157   1.168   -51.155  1.00 17.35 ? 125 ILE A CG1 1 
ATOM   1028 C CG2 . ILE A 1 132 ? 1.414   1.134   -49.276  1.00 17.37 ? 125 ILE A CG2 1 
ATOM   1029 C CD1 . ILE A 1 132 ? 3.934   2.350   -50.588  1.00 20.18 ? 125 ILE A CD1 1 
ATOM   1030 N N   . GLU A 1 133 ? 2.141   -1.856  -51.746  1.00 17.85 ? 126 GLU A N   1 
ATOM   1031 C CA  . GLU A 1 133 ? 2.703   -3.120  -51.306  1.00 18.74 ? 126 GLU A CA  1 
ATOM   1032 C C   . GLU A 1 133 ? 3.315   -2.958  -49.916  1.00 20.29 ? 126 GLU A C   1 
ATOM   1033 O O   . GLU A 1 133 ? 3.627   -1.848  -49.464  1.00 20.47 ? 126 GLU A O   1 
ATOM   1034 C CB  . GLU A 1 133 ? 3.746   -3.605  -52.318  1.00 21.72 ? 126 GLU A CB  1 
ATOM   1035 C CG  . GLU A 1 133 ? 5.059   -2.804  -52.359  1.00 25.25 ? 126 GLU A CG  1 
ATOM   1036 C CD  . GLU A 1 133 ? 4.958   -1.429  -53.036  1.00 27.01 ? 126 GLU A CD  1 
ATOM   1037 O OE1 . GLU A 1 133 ? 3.960   -1.131  -53.748  1.00 24.28 ? 126 GLU A OE1 1 
ATOM   1038 O OE2 . GLU A 1 133 ? 5.909   -0.632  -52.834  1.00 32.02 ? 126 GLU A OE2 1 
ATOM   1039 N N   . PHE A 1 134 ? 3.489   -4.078  -49.225  1.00 18.85 ? 127 PHE A N   1 
ATOM   1040 C CA  . PHE A 1 134 ? 3.931   -4.002  -47.842  1.00 18.93 ? 127 PHE A CA  1 
ATOM   1041 C C   . PHE A 1 134 ? 4.637   -5.288  -47.445  1.00 19.53 ? 127 PHE A C   1 
ATOM   1042 O O   . PHE A 1 134 ? 4.568   -6.305  -48.143  1.00 21.13 ? 127 PHE A O   1 
ATOM   1043 C CB  . PHE A 1 134 ? 2.750   -3.716  -46.911  1.00 19.16 ? 127 PHE A CB  1 
ATOM   1044 C CG  . PHE A 1 134 ? 1.754   -4.820  -46.857  1.00 20.78 ? 127 PHE A CG  1 
ATOM   1045 C CD1 . PHE A 1 134 ? 0.792   -4.944  -47.844  1.00 24.75 ? 127 PHE A CD1 1 
ATOM   1046 C CD2 . PHE A 1 134 ? 1.790   -5.753  -45.839  1.00 26.65 ? 127 PHE A CD2 1 
ATOM   1047 C CE1 . PHE A 1 134 ? -0.123  -5.967  -47.812  1.00 30.22 ? 127 PHE A CE1 1 
ATOM   1048 C CE2 . PHE A 1 134 ? 0.872   -6.773  -45.799  1.00 38.77 ? 127 PHE A CE2 1 
ATOM   1049 C CZ  . PHE A 1 134 ? -0.085  -6.885  -46.793  1.00 39.47 ? 127 PHE A CZ  1 
ATOM   1050 N N   . GLU A 1 135 ? 5.331   -5.220  -46.311  1.00 19.69 ? 128 GLU A N   1 
ATOM   1051 C CA  . GLU A 1 135 ? 5.984   -6.354  -45.681  1.00 20.25 ? 128 GLU A CA  1 
ATOM   1052 C C   . GLU A 1 135 ? 5.491   -6.469  -44.245  1.00 20.22 ? 128 GLU A C   1 
ATOM   1053 O O   . GLU A 1 135 ? 5.007   -5.487  -43.660  1.00 19.78 ? 128 GLU A O   1 
ATOM   1054 C CB  . GLU A 1 135 ? 7.489   -6.103  -45.626  1.00 28.07 ? 128 GLU A CB  1 
ATOM   1055 C CG  . GLU A 1 135 ? 8.140   -5.940  -47.009  1.00 41.43 ? 128 GLU A CG  1 
ATOM   1056 C CD  . GLU A 1 135 ? 9.552   -5.399  -46.919  1.00 56.44 ? 128 GLU A CD  1 
ATOM   1057 O OE1 . GLU A 1 135 ? 10.488  -6.063  -47.410  1.00 60.56 ? 128 GLU A OE1 1 
ATOM   1058 O OE2 . GLU A 1 135 ? 9.733   -4.302  -46.344  1.00 59.34 ? 128 GLU A OE2 1 
ATOM   1059 N N   . ILE A 1 136 ? 5.586   -7.680  -43.691  1.00 23.32 ? 129 ILE A N   1 
ATOM   1060 C CA  . ILE A 1 136 ? 5.178   -7.994  -42.324  1.00 22.70 ? 129 ILE A CA  1 
ATOM   1061 C C   . ILE A 1 136 ? 6.378   -8.565  -41.581  1.00 21.28 ? 129 ILE A C   1 
ATOM   1062 O O   . ILE A 1 136 ? 7.126   -9.377  -42.138  1.00 24.33 ? 129 ILE A O   1 
ATOM   1063 C CB  . ILE A 1 136 ? 4.035   -9.027  -42.299  1.00 25.39 ? 129 ILE A CB  1 
ATOM   1064 C CG1 . ILE A 1 136 ? 2.889   -8.597  -43.195  1.00 26.10 ? 129 ILE A CG1 1 
ATOM   1065 C CG2 . ILE A 1 136 ? 3.515   -9.242  -40.864  1.00 24.84 ? 129 ILE A CG2 1 
ATOM   1066 C CD1 . ILE A 1 136 ? 1.908   -9.719  -43.495  1.00 29.85 ? 129 ILE A CD1 1 
ATOM   1067 N N   . GLU A 1 137 ? 6.570   -8.140  -40.334  1.00 21.51 ? 130 GLU A N   1 
ATOM   1068 C CA  . GLU A 1 137 ? 7.605   -8.693  -39.471  1.00 22.21 ? 130 GLU A CA  1 
ATOM   1069 C C   . GLU A 1 137 ? 6.950   -9.131  -38.171  1.00 21.81 ? 130 GLU A C   1 
ATOM   1070 O O   . GLU A 1 137 ? 6.209   -8.362  -37.554  1.00 23.71 ? 130 GLU A O   1 
ATOM   1071 C CB  . GLU A 1 137 ? 8.701   -7.664  -39.182  1.00 25.40 ? 130 GLU A CB  1 
ATOM   1072 C CG  . GLU A 1 137 ? 9.880   -8.213  -38.368  1.00 37.60 ? 130 GLU A CG  1 
ATOM   1073 C CD  . GLU A 1 137 ? 10.961  -7.170  -38.132  1.00 49.76 ? 130 GLU A CD  1 
ATOM   1074 O OE1 . GLU A 1 137 ? 10.879  -6.083  -38.752  1.00 50.74 ? 130 GLU A OE1 1 
ATOM   1075 O OE2 . GLU A 1 137 ? 11.866  -7.419  -37.302  1.00 50.12 ? 130 GLU A OE2 1 
ATOM   1076 N N   . ASP A 1 138 ? 7.241   -10.358 -37.758  1.00 25.90 ? 131 ASP A N   1 
ATOM   1077 C CA  . ASP A 1 138 ? 6.736   -10.937 -36.521  1.00 25.91 ? 131 ASP A CA  1 
ATOM   1078 C C   . ASP A 1 138 ? 7.682   -10.530 -35.397  1.00 24.51 ? 131 ASP A C   1 
ATOM   1079 O O   . ASP A 1 138 ? 8.866   -10.885 -35.417  1.00 26.23 ? 131 ASP A O   1 
ATOM   1080 C CB  . ASP A 1 138 ? 6.714   -12.458 -36.692  1.00 29.87 ? 131 ASP A CB  1 
ATOM   1081 C CG  . ASP A 1 138 ? 5.985   -13.186 -35.574  1.00 41.09 ? 131 ASP A CG  1 
ATOM   1082 O OD1 . ASP A 1 138 ? 5.839   -12.629 -34.470  1.00 35.96 ? 131 ASP A OD1 1 
ATOM   1083 O OD2 . ASP A 1 138 ? 5.559   -14.341 -35.808  1.00 43.07 ? 131 ASP A OD2 1 
ATOM   1084 N N   . LEU A 1 139 ? 7.172   -9.786  -34.425  1.00 27.73 ? 132 LEU A N   1 
ATOM   1085 C CA  . LEU A 1 139 ? 7.993   -9.320  -33.318  1.00 28.63 ? 132 LEU A CA  1 
ATOM   1086 C C   . LEU A 1 139 ? 7.930   -10.223 -32.098  1.00 31.22 ? 132 LEU A C   1 
ATOM   1087 O O   . LEU A 1 139 ? 8.572   -9.913  -31.091  1.00 31.79 ? 132 LEU A O   1 
ATOM   1088 C CB  . LEU A 1 139 ? 7.582   -7.895  -32.927  1.00 27.34 ? 132 LEU A CB  1 
ATOM   1089 C CG  . LEU A 1 139 ? 7.824   -6.860  -34.022  1.00 27.18 ? 132 LEU A CG  1 
ATOM   1090 C CD1 . LEU A 1 139 ? 7.416   -5.471  -33.570  1.00 27.35 ? 132 LEU A CD1 1 
ATOM   1091 C CD2 . LEU A 1 139 ? 9.298   -6.899  -34.375  1.00 32.04 ? 132 LEU A CD2 1 
ATOM   1092 N N   . GLY A 1 140 ? 7.178   -11.314 -32.152  1.00 29.73 ? 133 GLY A N   1 
ATOM   1093 C CA  . GLY A 1 140 ? 7.066   -12.175 -30.998  1.00 31.99 ? 133 GLY A CA  1 
ATOM   1094 C C   . GLY A 1 140 ? 6.134   -11.615 -29.941  1.00 35.58 ? 133 GLY A C   1 
ATOM   1095 O O   . GLY A 1 140 ? 5.438   -10.613 -30.127  1.00 36.41 ? 133 GLY A O   1 
ATOM   1096 N N   . VAL A 1 141 ? 6.107   -12.312 -28.813  1.00 30.46 ? 134 VAL A N   1 
ATOM   1097 C CA  . VAL A 1 141 ? 5.228   -11.958 -27.705  1.00 30.45 ? 134 VAL A CA  1 
ATOM   1098 C C   . VAL A 1 141 ? 5.880   -10.862 -26.871  1.00 30.92 ? 134 VAL A C   1 
ATOM   1099 O O   . VAL A 1 141 ? 7.081   -10.912 -26.586  1.00 34.00 ? 134 VAL A O   1 
ATOM   1100 C CB  . VAL A 1 141 ? 4.916   -13.201 -26.860  1.00 36.24 ? 134 VAL A CB  1 
ATOM   1101 C CG1 . VAL A 1 141 ? 3.781   -12.918 -25.885  1.00 32.98 ? 134 VAL A CG1 1 
ATOM   1102 C CG2 . VAL A 1 141 ? 4.592   -14.359 -27.782  1.00 38.42 ? 134 VAL A CG2 1 
ATOM   1103 N N   . MET A 1 142 ? 5.097   -9.842  -26.514  1.00 28.78 ? 135 MET A N   1 
ATOM   1104 C CA  . MET A 1 142 ? 5.558   -8.760  -25.652  1.00 29.49 ? 135 MET A CA  1 
ATOM   1105 C C   . MET A 1 142 ? 4.501   -8.449  -24.603  1.00 27.96 ? 135 MET A C   1 
ATOM   1106 O O   . MET A 1 142 ? 3.303   -8.531  -24.877  1.00 29.62 ? 135 MET A O   1 
ATOM   1107 C CB  . MET A 1 142 ? 5.788   -7.465  -26.430  1.00 34.27 ? 135 MET A CB  1 
ATOM   1108 C CG  . MET A 1 142 ? 6.589   -7.594  -27.688  1.00 36.97 ? 135 MET A CG  1 
ATOM   1109 S SD  . MET A 1 142 ? 6.851   -5.941  -28.351  1.00 36.95 ? 135 MET A SD  1 
ATOM   1110 C CE  . MET A 1 142 ? 8.075   -6.289  -29.605  1.00 40.23 ? 135 MET A CE  1 
ATOM   1111 N N   . GLU A 1 143 ? 4.947   -8.041  -23.411  1.00 26.67 ? 136 GLU A N   1 
ATOM   1112 C CA  . GLU A 1 143 ? 4.072   -7.397  -22.436  1.00 28.40 ? 136 GLU A CA  1 
ATOM   1113 C C   . GLU A 1 143 ? 4.198   -5.891  -22.626  1.00 27.70 ? 136 GLU A C   1 
ATOM   1114 O O   . GLU A 1 143 ? 5.286   -5.330  -22.468  1.00 32.41 ? 136 GLU A O   1 
ATOM   1115 C CB  . GLU A 1 143 ? 4.411   -7.807  -21.002  1.00 36.13 ? 136 GLU A CB  1 
ATOM   1116 C CG  . GLU A 1 143 ? 3.354   -7.375  -19.999  1.00 40.43 ? 136 GLU A CG  1 
ATOM   1117 C CD  . GLU A 1 143 ? 3.584   -7.947  -18.615  1.00 49.54 ? 136 GLU A CD  1 
ATOM   1118 O OE1 . GLU A 1 143 ? 4.577   -8.681  -18.429  1.00 52.22 ? 136 GLU A OE1 1 
ATOM   1119 O OE2 . GLU A 1 143 ? 2.768   -7.664  -17.714  1.00 53.09 ? 136 GLU A OE2 1 
ATOM   1120 N N   . ILE A 1 144 ? 3.098   -5.246  -23.008  1.00 27.04 ? 137 ILE A N   1 
ATOM   1121 C CA  . ILE A 1 144 ? 3.174   -3.923  -23.615  1.00 23.87 ? 137 ILE A CA  1 
ATOM   1122 C C   . ILE A 1 144 ? 1.842   -3.213  -23.441  1.00 24.82 ? 137 ILE A C   1 
ATOM   1123 O O   . ILE A 1 144 ? 0.779   -3.840  -23.452  1.00 25.89 ? 137 ILE A O   1 
ATOM   1124 C CB  . ILE A 1 144 ? 3.573   -4.068  -25.107  1.00 27.19 ? 137 ILE A CB  1 
ATOM   1125 C CG1 . ILE A 1 144 ? 3.809   -2.706  -25.741  1.00 26.33 ? 137 ILE A CG1 1 
ATOM   1126 C CG2 . ILE A 1 144 ? 2.529   -4.886  -25.865  1.00 24.17 ? 137 ILE A CG2 1 
ATOM   1127 C CD1 . ILE A 1 144 ? 4.642   -2.797  -26.992  1.00 24.46 ? 137 ILE A CD1 1 
ATOM   1128 N N   . ASP A 1 145 ? 1.896   -1.888  -23.309  1.00 24.22 ? 138 ASP A N   1 
ATOM   1129 C CA  . ASP A 1 145 ? 0.696   -1.066  -23.342  1.00 26.11 ? 138 ASP A CA  1 
ATOM   1130 C C   . ASP A 1 145 ? 0.264   -0.888  -24.790  1.00 22.50 ? 138 ASP A C   1 
ATOM   1131 O O   . ASP A 1 145 ? 1.063   -0.474  -25.638  1.00 22.92 ? 138 ASP A O   1 
ATOM   1132 C CB  . ASP A 1 145 ? 0.986   0.321   -22.769  1.00 25.69 ? 138 ASP A CB  1 
ATOM   1133 C CG  . ASP A 1 145 ? 1.250   0.312   -21.276  1.00 30.64 ? 138 ASP A CG  1 
ATOM   1134 O OD1 . ASP A 1 145 ? 0.784   -0.607  -20.569  1.00 30.35 ? 138 ASP A OD1 1 
ATOM   1135 O OD2 . ASP A 1 145 ? 1.933   1.250   -20.820  1.00 35.90 ? 138 ASP A OD2 1 
ATOM   1136 N N   . VAL A 1 146 ? -0.998  -1.186  -25.074  1.00 20.79 ? 139 VAL A N   1 
ATOM   1137 C CA  . VAL A 1 146 ? -1.533  -0.977  -26.411  1.00 21.33 ? 139 VAL A CA  1 
ATOM   1138 C C   . VAL A 1 146 ? -2.768  -0.088  -26.312  1.00 20.18 ? 139 VAL A C   1 
ATOM   1139 O O   . VAL A 1 146 ? -3.445  -0.040  -25.279  1.00 21.83 ? 139 VAL A O   1 
ATOM   1140 C CB  . VAL A 1 146 ? -1.802  -2.297  -27.172  1.00 24.38 ? 139 VAL A CB  1 
ATOM   1141 C CG1 . VAL A 1 146 ? -0.487  -2.998  -27.485  1.00 27.96 ? 139 VAL A CG1 1 
ATOM   1142 C CG2 . VAL A 1 146 ? -2.724  -3.204  -26.382  1.00 28.62 ? 139 VAL A CG2 1 
ATOM   1143 N N   . TYR A 1 147 ? -3.050  0.629   -27.394  1.00 19.83 ? 140 TYR A N   1 
ATOM   1144 C CA  . TYR A 1 147 ? -4.036  1.692   -27.379  1.00 19.63 ? 140 TYR A CA  1 
ATOM   1145 C C   . TYR A 1 147 ? -4.903  1.594   -28.614  1.00 19.88 ? 140 TYR A C   1 
ATOM   1146 O O   . TYR A 1 147 ? -4.474  1.110   -29.659  1.00 21.62 ? 140 TYR A O   1 
ATOM   1147 C CB  . TYR A 1 147 ? -3.382  3.073   -27.426  1.00 19.05 ? 140 TYR A CB  1 
ATOM   1148 C CG  . TYR A 1 147 ? -2.517  3.383   -26.229  1.00 17.71 ? 140 TYR A CG  1 
ATOM   1149 C CD1 . TYR A 1 147 ? -1.237  2.871   -26.135  1.00 19.09 ? 140 TYR A CD1 1 
ATOM   1150 C CD2 . TYR A 1 147 ? -2.991  4.177   -25.188  1.00 19.17 ? 140 TYR A CD2 1 
ATOM   1151 C CE1 . TYR A 1 147 ? -0.445  3.136   -25.029  1.00 18.27 ? 140 TYR A CE1 1 
ATOM   1152 C CE2 . TYR A 1 147 ? -2.204  4.462   -24.091  1.00 19.25 ? 140 TYR A CE2 1 
ATOM   1153 C CZ  . TYR A 1 147 ? -0.929  3.940   -24.020  1.00 18.76 ? 140 TYR A CZ  1 
ATOM   1154 O OH  . TYR A 1 147 ? -0.129  4.214   -22.927  1.00 23.22 ? 140 TYR A OH  1 
ATOM   1155 N N   . ASP A 1 148 ? -6.111  2.112   -28.499  1.00 20.25 ? 141 ASP A N   1 
ATOM   1156 C CA  . ASP A 1 148 ? -7.020  2.150   -29.620  1.00 21.62 ? 141 ASP A CA  1 
ATOM   1157 C C   . ASP A 1 148 ? -7.868  3.396   -29.461  1.00 21.68 ? 141 ASP A C   1 
ATOM   1158 O O   . ASP A 1 148 ? -7.958  3.975   -28.380  1.00 20.34 ? 141 ASP A O   1 
ATOM   1159 C CB  . ASP A 1 148 ? -7.912  0.903   -29.632  1.00 24.26 ? 141 ASP A CB  1 
ATOM   1160 C CG  . ASP A 1 148 ? -8.327  0.495   -31.029  1.00 33.41 ? 141 ASP A CG  1 
ATOM   1161 O OD1 . ASP A 1 148 ? -8.188  1.309   -31.968  1.00 34.37 ? 141 ASP A OD1 1 
ATOM   1162 O OD2 . ASP A 1 148 ? -8.772  -0.656  -31.187  1.00 37.45 ? 141 ASP A OD2 1 
ATOM   1163 N N   . ILE A 1 149 ? -8.436  3.847   -30.564  1.00 21.03 ? 142 ILE A N   1 
ATOM   1164 C CA  . ILE A 1 149 ? -9.408  4.923   -30.503  1.00 21.13 ? 142 ILE A CA  1 
ATOM   1165 C C   . ILE A 1 149 ? -10.661 4.421   -31.192  1.00 21.44 ? 142 ILE A C   1 
ATOM   1166 O O   . ILE A 1 149 ? -10.592 3.569   -32.085  1.00 24.08 ? 142 ILE A O   1 
ATOM   1167 C CB  . ILE A 1 149 ? -8.888  6.251   -31.106  1.00 21.62 ? 142 ILE A CB  1 
ATOM   1168 C CG1 . ILE A 1 149 ? -8.264  6.033   -32.487  1.00 26.04 ? 142 ILE A CG1 1 
ATOM   1169 C CG2 . ILE A 1 149 ? -7.897  6.935   -30.130  1.00 24.60 ? 142 ILE A CG2 1 
ATOM   1170 C CD1 . ILE A 1 149 ? -7.924  7.333   -33.180  1.00 25.78 ? 142 ILE A CD1 1 
ATOM   1171 N N   . GLU A 1 150 ? -11.808 4.910   -30.751  1.00 22.82 ? 143 GLU A N   1 
ATOM   1172 C CA  . GLU A 1 150 ? -13.049 4.712   -31.484  1.00 21.92 ? 143 GLU A CA  1 
ATOM   1173 C C   . GLU A 1 150 ? -13.277 5.943   -32.347  1.00 24.00 ? 143 GLU A C   1 
ATOM   1174 O O   . GLU A 1 150 ? -13.422 7.056   -31.830  1.00 25.30 ? 143 GLU A O   1 
ATOM   1175 C CB  . GLU A 1 150 ? -14.261 4.475   -30.588  1.00 29.97 ? 143 GLU A CB  1 
ATOM   1176 C CG  . GLU A 1 150 ? -15.497 4.253   -31.472  1.00 36.25 ? 143 GLU A CG  1 
ATOM   1177 C CD  . GLU A 1 150 ? -16.801 4.292   -30.740  1.00 40.61 ? 143 GLU A CD  1 
ATOM   1178 O OE1 . GLU A 1 150 ? -16.979 3.501   -29.790  1.00 47.48 ? 143 GLU A OE1 1 
ATOM   1179 O OE2 . GLU A 1 150 ? -17.658 5.107   -31.134  1.00 35.48 ? 143 GLU A OE2 1 
ATOM   1180 N N   . VAL A 1 151 ? -13.373 5.732   -33.651  1.00 25.03 ? 144 VAL A N   1 
ATOM   1181 C CA  . VAL A 1 151 ? -13.542 6.817   -34.609  1.00 25.81 ? 144 VAL A CA  1 
ATOM   1182 C C   . VAL A 1 151 ? -14.955 6.718   -35.157  1.00 26.38 ? 144 VAL A C   1 
ATOM   1183 O O   . VAL A 1 151 ? -15.336 5.682   -35.719  1.00 27.95 ? 144 VAL A O   1 
ATOM   1184 C CB  . VAL A 1 151 ? -12.498 6.743   -35.725  1.00 25.92 ? 144 VAL A CB  1 
ATOM   1185 C CG1 . VAL A 1 151 ? -12.753 7.835   -36.754  1.00 23.78 ? 144 VAL A CG1 1 
ATOM   1186 C CG2 . VAL A 1 151 ? -11.108 6.883   -35.124  1.00 23.32 ? 144 VAL A CG2 1 
ATOM   1187 N N   . ASP A 1 152 ? -15.720 7.797   -35.002  1.00 23.33 ? 145 ASP A N   1 
ATOM   1188 C CA  . ASP A 1 152 ? -17.131 7.787   -35.357  1.00 24.68 ? 145 ASP A CA  1 
ATOM   1189 C C   . ASP A 1 152 ? -17.332 7.406   -36.815  1.00 23.99 ? 145 ASP A C   1 
ATOM   1190 O O   . ASP A 1 152 ? -16.641 7.916   -37.706  1.00 25.10 ? 145 ASP A O   1 
ATOM   1191 C CB  . ASP A 1 152 ? -17.726 9.168   -35.132  1.00 23.97 ? 145 ASP A CB  1 
ATOM   1192 C CG  . ASP A 1 152 ? -19.236 9.157   -35.204  1.00 34.93 ? 145 ASP A CG  1 
ATOM   1193 O OD1 . ASP A 1 152 ? -19.854 8.461   -34.373  1.00 41.47 ? 145 ASP A OD1 1 
ATOM   1194 O OD2 . ASP A 1 152 ? -19.800 9.826   -36.094  1.00 40.45 ? 145 ASP A OD2 1 
ATOM   1195 N N   . GLY A 1 153 ? -18.263 6.486   -37.055  1.00 23.88 ? 146 GLY A N   1 
ATOM   1196 C CA  . GLY A 1 153 ? -18.692 6.218   -38.414  1.00 24.43 ? 146 GLY A CA  1 
ATOM   1197 C C   . GLY A 1 153 ? -17.819 5.254   -39.190  1.00 24.62 ? 146 GLY A C   1 
ATOM   1198 O O   . GLY A 1 153 ? -18.294 4.224   -39.676  1.00 27.15 ? 146 GLY A O   1 
ATOM   1199 N N   . ASN A 1 154 ? -16.533 5.567   -39.322  1.00 22.70 ? 147 ASN A N   1 
ATOM   1200 C CA  . ASN A 1 154 ? -15.681 4.805   -40.227  1.00 20.95 ? 147 ASN A CA  1 
ATOM   1201 C C   . ASN A 1 154 ? -14.869 3.697   -39.561  1.00 22.99 ? 147 ASN A C   1 
ATOM   1202 O O   . ASN A 1 154 ? -14.483 2.746   -40.243  1.00 25.87 ? 147 ASN A O   1 
ATOM   1203 C CB  . ASN A 1 154 ? -14.793 5.744   -41.059  1.00 21.63 ? 147 ASN A CB  1 
ATOM   1204 C CG  . ASN A 1 154 ? -15.593 6.540   -42.064  1.00 22.73 ? 147 ASN A CG  1 
ATOM   1205 O OD1 . ASN A 1 154 ? -16.640 6.083   -42.525  1.00 24.33 ? 147 ASN A OD1 1 
ATOM   1206 N ND2 . ASN A 1 154 ? -15.127 7.738   -42.396  1.00 24.21 ? 147 ASN A ND2 1 
ATOM   1207 N N   . HIS A 1 155 ? -14.608 3.787   -38.263  1.00 24.73 ? 148 HIS A N   1 
ATOM   1208 C CA  . HIS A 1 155 ? -13.968 2.703   -37.512  1.00 26.66 ? 148 HIS A CA  1 
ATOM   1209 C C   . HIS A 1 155 ? -12.594 2.330   -38.072  1.00 20.02 ? 148 HIS A C   1 
ATOM   1210 O O   . HIS A 1 155 ? -12.214 1.157   -38.151  1.00 22.42 ? 148 HIS A O   1 
ATOM   1211 C CB  . HIS A 1 155 ? -14.888 1.488   -37.371  1.00 24.31 ? 148 HIS A CB  1 
ATOM   1212 C CG  . HIS A 1 155 ? -16.301 1.841   -37.014  1.00 26.99 ? 148 HIS A CG  1 
ATOM   1213 N ND1 . HIS A 1 155 ? -16.615 2.816   -36.089  1.00 30.08 ? 148 HIS A ND1 1 
ATOM   1214 C CD2 . HIS A 1 155 ? -17.483 1.358   -37.465  1.00 32.04 ? 148 HIS A CD2 1 
ATOM   1215 C CE1 . HIS A 1 155 ? -17.928 2.915   -35.985  1.00 34.78 ? 148 HIS A CE1 1 
ATOM   1216 N NE2 . HIS A 1 155 ? -18.478 2.039   -36.805  1.00 33.03 ? 148 HIS A NE2 1 
ATOM   1217 N N   . ASN A 1 156 ? -11.825 3.342   -38.453  1.00 19.41 ? 149 ASN A N   1 
ATOM   1218 C CA  . ASN A 1 156 ? -10.424 3.144   -38.796  1.00 17.06 ? 149 ASN A CA  1 
ATOM   1219 C C   . ASN A 1 156 ? -9.705  4.465   -38.544  1.00 16.97 ? 149 ASN A C   1 
ATOM   1220 O O   . ASN A 1 156 ? -10.327 5.515   -38.365  1.00 16.76 ? 149 ASN A O   1 
ATOM   1221 C CB  . ASN A 1 156 ? -10.243 2.599   -40.230  1.00 16.13 ? 149 ASN A CB  1 
ATOM   1222 C CG  . ASN A 1 156 ? -10.906 3.470   -41.265  1.00 16.58 ? 149 ASN A CG  1 
ATOM   1223 O OD1 . ASN A 1 156 ? -10.631 4.673   -41.338  1.00 18.65 ? 149 ASN A OD1 1 
ATOM   1224 N ND2 . ASN A 1 156 ? -11.783 2.874   -42.085  1.00 17.45 ? 149 ASN A ND2 1 
ATOM   1225 N N   . PHE A 1 157 ? -8.380  4.404   -38.507  1.00 14.56 ? 150 PHE A N   1 
ATOM   1226 C CA  . PHE A 1 157 ? -7.559  5.586   -38.269  1.00 14.77 ? 150 PHE A CA  1 
ATOM   1227 C C   . PHE A 1 157 ? -6.167  5.287   -38.805  1.00 14.60 ? 150 PHE A C   1 
ATOM   1228 O O   . PHE A 1 157 ? -5.788  4.125   -38.978  1.00 14.60 ? 150 PHE A O   1 
ATOM   1229 C CB  . PHE A 1 157 ? -7.495  6.001   -36.784  1.00 16.61 ? 150 PHE A CB  1 
ATOM   1230 C CG  . PHE A 1 157 ? -6.777  5.032   -35.882  1.00 17.46 ? 150 PHE A CG  1 
ATOM   1231 C CD1 . PHE A 1 157 ? -7.443  3.946   -35.329  1.00 22.63 ? 150 PHE A CD1 1 
ATOM   1232 C CD2 . PHE A 1 157 ? -5.448  5.247   -35.533  1.00 16.38 ? 150 PHE A CD2 1 
ATOM   1233 C CE1 . PHE A 1 157 ? -6.786  3.069   -34.477  1.00 22.20 ? 150 PHE A CE1 1 
ATOM   1234 C CE2 . PHE A 1 157 ? -4.790  4.374   -34.709  1.00 18.03 ? 150 PHE A CE2 1 
ATOM   1235 C CZ  . PHE A 1 157 ? -5.461  3.296   -34.151  1.00 21.75 ? 150 PHE A CZ  1 
ATOM   1236 N N   . PHE A 1 158 ? -5.397  6.348   -39.072  1.00 15.98 ? 151 PHE A N   1 
ATOM   1237 C CA  . PHE A 1 158 ? -4.019  6.192   -39.529  1.00 16.39 ? 151 PHE A CA  1 
ATOM   1238 C C   . PHE A 1 158 ? -3.055  6.152   -38.344  1.00 14.81 ? 151 PHE A C   1 
ATOM   1239 O O   . PHE A 1 158 ? -3.084  7.039   -37.475  1.00 17.24 ? 151 PHE A O   1 
ATOM   1240 C CB  . PHE A 1 158 ? -3.615  7.310   -40.495  1.00 16.55 ? 151 PHE A CB  1 
ATOM   1241 C CG  . PHE A 1 158 ? -4.348  7.275   -41.799  1.00 15.73 ? 151 PHE A CG  1 
ATOM   1242 C CD1 . PHE A 1 158 ? -3.882  6.526   -42.884  1.00 17.88 ? 151 PHE A CD1 1 
ATOM   1243 C CD2 . PHE A 1 158 ? -5.507  8.000   -41.961  1.00 16.13 ? 151 PHE A CD2 1 
ATOM   1244 C CE1 . PHE A 1 158 ? -4.578  6.508   -44.074  1.00 15.84 ? 151 PHE A CE1 1 
ATOM   1245 C CE2 . PHE A 1 158 ? -6.224  7.982   -43.132  1.00 19.42 ? 151 PHE A CE2 1 
ATOM   1246 C CZ  . PHE A 1 158 ? -5.749  7.238   -44.212  1.00 18.14 ? 151 PHE A CZ  1 
ATOM   1247 N N   . GLY A 1 159 ? -2.231  5.111   -38.293  1.00 14.79 ? 152 GLY A N   1 
ATOM   1248 C CA  . GLY A 1 159 ? -1.143  5.040   -37.330  1.00 15.47 ? 152 GLY A CA  1 
ATOM   1249 C C   . GLY A 1 159 ? 0.175   5.043   -38.070  1.00 14.85 ? 152 GLY A C   1 
ATOM   1250 O O   . GLY A 1 159 ? 0.393   4.171   -38.932  1.00 14.60 ? 152 GLY A O   1 
ATOM   1251 N N   . ASN A 1 160 ? 1.020   6.049   -37.827  1.00 15.69 ? 153 ASN A N   1 
ATOM   1252 C CA  . ASN A 1 160 ? 2.232   6.237   -38.632  1.00 16.18 ? 153 ASN A CA  1 
ATOM   1253 C C   . ASN A 1 160 ? 1.919   6.202   -40.121  1.00 17.45 ? 153 ASN A C   1 
ATOM   1254 O O   . ASN A 1 160 ? 2.648   5.598   -40.916  1.00 17.09 ? 153 ASN A O   1 
ATOM   1255 C CB  . ASN A 1 160 ? 3.308   5.220   -38.273  1.00 16.87 ? 153 ASN A CB  1 
ATOM   1256 C CG  . ASN A 1 160 ? 3.805   5.394   -36.875  1.00 17.80 ? 153 ASN A CG  1 
ATOM   1257 O OD1 . ASN A 1 160 ? 3.780   6.502   -36.317  1.00 17.22 ? 153 ASN A OD1 1 
ATOM   1258 N ND2 . ASN A 1 160 ? 4.239   4.304   -36.272  1.00 21.70 ? 153 ASN A ND2 1 
ATOM   1259 N N   . ASP A 1 161 ? 0.808   6.836   -40.498  1.00 15.38 ? 154 ASP A N   1 
ATOM   1260 C CA  . ASP A 1 161 ? 0.332   7.006   -41.871  1.00 16.13 ? 154 ASP A CA  1 
ATOM   1261 C C   . ASP A 1 161 ? -0.239  5.745   -42.501  1.00 16.78 ? 154 ASP A C   1 
ATOM   1262 O O   . ASP A 1 161 ? -0.552  5.766   -43.695  1.00 16.71 ? 154 ASP A O   1 
ATOM   1263 C CB  . ASP A 1 161 ? 1.407   7.587   -42.806  1.00 18.32 ? 154 ASP A CB  1 
ATOM   1264 C CG  . ASP A 1 161 ? 1.736   9.034   -42.492  1.00 27.99 ? 154 ASP A CG  1 
ATOM   1265 O OD1 . ASP A 1 161 ? 0.963   9.688   -41.761  1.00 28.14 ? 154 ASP A OD1 1 
ATOM   1266 O OD2 . ASP A 1 161 ? 2.769   9.525   -42.996  1.00 32.64 ? 154 ASP A OD2 1 
ATOM   1267 N N   . ILE A 1 162 ? -0.402  4.661   -41.755  1.00 14.84 ? 155 ILE A N   1 
ATOM   1268 C CA  . ILE A 1 162 ? -0.921  3.396   -42.284  1.00 13.29 ? 155 ILE A CA  1 
ATOM   1269 C C   . ILE A 1 162 ? -2.304  3.160   -41.674  1.00 13.65 ? 155 ILE A C   1 
ATOM   1270 O O   . ILE A 1 162 ? -2.480  3.286   -40.453  1.00 14.78 ? 155 ILE A O   1 
ATOM   1271 C CB  . ILE A 1 162 ? 0.038   2.251   -41.926  1.00 13.26 ? 155 ILE A CB  1 
ATOM   1272 C CG1 . ILE A 1 162 ? 1.380   2.473   -42.660  1.00 15.42 ? 155 ILE A CG1 1 
ATOM   1273 C CG2 . ILE A 1 162 ? -0.573  0.899   -42.267  1.00 15.95 ? 155 ILE A CG2 1 
ATOM   1274 C CD1 . ILE A 1 162 ? 2.517   1.596   -42.167  1.00 18.04 ? 155 ILE A CD1 1 
ATOM   1275 N N   . LEU A 1 163 ? -3.284  2.816   -42.498  1.00 13.61 ? 156 LEU A N   1 
ATOM   1276 C CA  . LEU A 1 163 ? -4.660  2.726   -42.016  1.00 13.75 ? 156 LEU A CA  1 
ATOM   1277 C C   . LEU A 1 163 ? -4.871  1.435   -41.231  1.00 15.70 ? 156 LEU A C   1 
ATOM   1278 O O   . LEU A 1 163 ? -4.607  0.335   -41.750  1.00 16.49 ? 156 LEU A O   1 
ATOM   1279 C CB  . LEU A 1 163 ? -5.629  2.816   -43.187  1.00 14.77 ? 156 LEU A CB  1 
ATOM   1280 C CG  . LEU A 1 163 ? -7.068  3.089   -42.762  1.00 15.11 ? 156 LEU A CG  1 
ATOM   1281 C CD1 . LEU A 1 163 ? -7.245  4.506   -42.281  1.00 18.63 ? 156 LEU A CD1 1 
ATOM   1282 C CD2 . LEU A 1 163 ? -7.994  2.822   -43.946  1.00 17.27 ? 156 LEU A CD2 1 
ATOM   1283 N N   . VAL A 1 164 ? -5.352  1.554   -39.988  1.00 15.74 ? 157 VAL A N   1 
ATOM   1284 C CA  . VAL A 1 164 ? -5.633  0.398   -39.154  1.00 17.83 ? 157 VAL A CA  1 
ATOM   1285 C C   . VAL A 1 164 ? -7.090  0.448   -38.725  1.00 18.72 ? 157 VAL A C   1 
ATOM   1286 O O   . VAL A 1 164 ? -7.724  1.501   -38.705  1.00 18.91 ? 157 VAL A O   1 
ATOM   1287 C CB  . VAL A 1 164 ? -4.692  0.324   -37.946  1.00 18.94 ? 157 VAL A CB  1 
ATOM   1288 C CG1 . VAL A 1 164 ? -3.244  0.174   -38.424  1.00 18.72 ? 157 VAL A CG1 1 
ATOM   1289 C CG2 . VAL A 1 164 ? -4.853  1.546   -37.092  1.00 23.84 ? 157 VAL A CG2 1 
ATOM   1290 N N   . HIS A 1 165 ? -7.635  -0.722  -38.398  1.00 19.58 ? 158 HIS A N   1 
ATOM   1291 C CA  . HIS A 1 165 ? -8.996  -0.794  -37.901  1.00 23.53 ? 158 HIS A CA  1 
ATOM   1292 C C   . HIS A 1 165 ? -9.060  -0.170  -36.514  1.00 22.67 ? 158 HIS A C   1 
ATOM   1293 O O   . HIS A 1 165 ? -8.115  -0.261  -35.727  1.00 24.96 ? 158 HIS A O   1 
ATOM   1294 C CB  . HIS A 1 165 ? -9.420  -2.261  -37.850  1.00 26.76 ? 158 HIS A CB  1 
ATOM   1295 C CG  . HIS A 1 165 ? -10.894 -2.466  -37.726  1.00 28.66 ? 158 HIS A CG  1 
ATOM   1296 N ND1 . HIS A 1 165 ? -11.448 -3.295  -36.775  1.00 38.55 ? 158 HIS A ND1 1 
ATOM   1297 C CD2 . HIS A 1 165 ? -11.927 -1.968  -38.442  1.00 28.21 ? 158 HIS A CD2 1 
ATOM   1298 C CE1 . HIS A 1 165 ? -12.763 -3.288  -36.902  1.00 38.29 ? 158 HIS A CE1 1 
ATOM   1299 N NE2 . HIS A 1 165 ? -13.081 -2.489  -37.904  1.00 33.46 ? 158 HIS A NE2 1 
ATOM   1300 N N   . ALA A 1 166 ? -10.157 0.525   -36.239  1.00 23.45 ? 159 ALA A N   1 
ATOM   1301 C CA  . ALA A 1 166 ? -10.353 1.091   -34.921  1.00 28.42 ? 159 ALA A CA  1 
ATOM   1302 C C   . ALA A 1 166 ? -11.195 0.134   -34.082  1.00 29.93 ? 159 ALA A C   1 
ATOM   1303 O O   . ALA A 1 166 ? -11.868 -0.762  -34.596  1.00 38.87 ? 159 ALA A O   1 
ATOM   1304 C CB  . ALA A 1 166 ? -11.020 2.459   -35.055  1.00 28.32 ? 159 ALA A CB  1 
ATOM   1305 N N   . SER A 1 167 ? -11.188 0.346   -32.776  1.00 33.30 ? 160 SER A N   1 
ATOM   1306 C CA  . SER A 1 167 ? -12.153 -0.390  -31.983  1.00 39.58 ? 160 SER A CA  1 
ATOM   1307 C C   . SER A 1 167 ? -13.432 0.418   -31.937  1.00 37.23 ? 160 SER A C   1 
ATOM   1308 O O   . SER A 1 167 ? -13.443 1.629   -32.165  1.00 48.34 ? 160 SER A O   1 
ATOM   1309 C CB  . SER A 1 167 ? -11.654 -0.618  -30.555  1.00 44.05 ? 160 SER A CB  1 
ATOM   1310 O OG  . SER A 1 167 ? -12.549 -0.062  -29.603  1.00 44.78 ? 160 SER A OG  1 
ATOM   1311 N N   . VAL A 1 168 ? -14.522 -0.253  -31.622  1.00 47.62 ? 161 VAL A N   1 
ATOM   1312 C CA  . VAL A 1 168 ? -15.704 0.455   -31.176  1.00 48.21 ? 161 VAL A CA  1 
ATOM   1313 C C   . VAL A 1 168 ? -15.956 -0.002  -29.755  1.00 52.19 ? 161 VAL A C   1 
ATOM   1314 O O   . VAL A 1 168 ? -15.925 -1.204  -29.470  1.00 52.03 ? 161 VAL A O   1 
ATOM   1315 C CB  . VAL A 1 168 ? -16.918 0.200   -32.092  1.00 48.63 ? 161 VAL A CB  1 
ATOM   1316 C CG1 . VAL A 1 168 ? -18.216 0.342   -31.323  1.00 55.23 ? 161 VAL A CG1 1 
ATOM   1317 C CG2 . VAL A 1 168 ? -16.901 1.159   -33.271  1.00 47.50 ? 161 VAL A CG2 1 
ATOM   1318 N N   . TYR A 1 169 ? -16.143 0.957   -28.863  1.00 56.23 ? 162 TYR A N   1 
ATOM   1319 C CA  . TYR A 1 169 ? -16.605 0.676   -27.521  1.00 59.08 ? 162 TYR A CA  1 
ATOM   1320 C C   . TYR A 1 169 ? -18.093 0.927   -27.607  1.00 62.03 ? 162 TYR A C   1 
ATOM   1321 O O   . TYR A 1 169 ? -18.524 2.072   -27.785  1.00 65.73 ? 162 TYR A O   1 
ATOM   1322 C CB  . TYR A 1 169 ? -15.971 1.629   -26.505  1.00 54.44 ? 162 TYR A CB  1 
ATOM   1323 C CG  . TYR A 1 169 ? -16.574 1.594   -25.108  1.00 52.19 ? 162 TYR A CG  1 
ATOM   1324 C CD1 . TYR A 1 169 ? -16.244 0.588   -24.209  1.00 51.64 ? 162 TYR A CD1 1 
ATOM   1325 C CD2 . TYR A 1 169 ? -17.453 2.583   -24.682  1.00 49.72 ? 162 TYR A CD2 1 
ATOM   1326 C CE1 . TYR A 1 169 ? -16.778 0.557   -22.937  1.00 57.53 ? 162 TYR A CE1 1 
ATOM   1327 C CE2 . TYR A 1 169 ? -18.001 2.560   -23.401  1.00 49.97 ? 162 TYR A CE2 1 
ATOM   1328 C CZ  . TYR A 1 169 ? -17.660 1.543   -22.534  1.00 52.59 ? 162 TYR A CZ  1 
ATOM   1329 O OH  . TYR A 1 169 ? -18.201 1.510   -21.260  1.00 54.26 ? 162 TYR A OH  1 
ATOM   1330 N N   . LEU A 1 170 ? -18.874 -0.128  -27.469  1.00 54.36 ? 163 LEU A N   1 
ATOM   1331 C CA  . LEU A 1 170 ? -20.309 0.058   -27.447  1.00 57.29 ? 163 LEU A CA  1 
ATOM   1332 C C   . LEU A 1 170 ? -20.654 0.425   -26.017  1.00 60.30 ? 163 LEU A C   1 
ATOM   1333 O O   . LEU A 1 170 ? -20.412 -0.360  -25.094  1.00 63.29 ? 163 LEU A O   1 
ATOM   1334 C CB  . LEU A 1 170 ? -21.012 -1.220  -27.890  1.00 54.49 ? 163 LEU A CB  1 
ATOM   1335 C CG  . LEU A 1 170 ? -20.931 -1.535  -29.384  1.00 54.66 ? 163 LEU A CG  1 
ATOM   1336 C CD1 . LEU A 1 170 ? -20.182 -2.830  -29.688  1.00 55.16 ? 163 LEU A CD1 1 
ATOM   1337 C CD2 . LEU A 1 170 ? -22.331 -1.557  -29.965  1.00 52.55 ? 163 LEU A CD2 1 
ATOM   1338 N N   . ASN A 1 171 ? -21.156 1.645   -25.823  1.00 64.02 ? 164 ASN A N   1 
ATOM   1339 C CA  . ASN A 1 171 ? -21.585 2.072   -24.498  1.00 66.21 ? 164 ASN A CA  1 
ATOM   1340 C C   . ASN A 1 171 ? -22.872 1.293   -24.270  1.00 66.28 ? 164 ASN A C   1 
ATOM   1341 O O   . ASN A 1 171 ? -23.987 1.785   -24.455  1.00 70.38 ? 164 ASN A O   1 
ATOM   1342 C CB  . ASN A 1 171 ? -21.810 3.577   -24.466  1.00 70.74 ? 164 ASN A CB  1 
ATOM   1343 C CG  . ASN A 1 171 ? -22.171 4.081   -23.090  1.00 75.00 ? 164 ASN A CG  1 
ATOM   1344 O OD1 . ASN A 1 171 ? -21.927 3.412   -22.089  1.00 76.73 ? 164 ASN A OD1 1 
ATOM   1345 N ND2 . ASN A 1 171 ? -22.750 5.276   -23.031  1.00 77.05 ? 164 ASN A ND2 1 
ATOM   1346 N N   . LYS A 1 172 ? -22.697 0.033   -23.868  1.00 58.44 ? 165 LYS A N   1 
ATOM   1347 C CA  . LYS A 1 172 ? -23.818 -0.896  -23.797  1.00 56.10 ? 165 LYS A CA  1 
ATOM   1348 C C   . LYS A 1 172 ? -24.782 -0.499  -22.690  1.00 54.86 ? 165 LYS A C   1 
ATOM   1349 O O   . LYS A 1 172 ? -26.001 -0.471  -22.893  1.00 50.20 ? 165 LYS A O   1 
ATOM   1350 C CB  . LYS A 1 172 ? -23.299 -2.322  -23.590  1.00 53.34 ? 165 LYS A CB  1 
ATOM   1351 C CG  . LYS A 1 172 ? -22.466 -2.856  -24.749  1.00 54.24 ? 165 LYS A CG  1 
ATOM   1352 C CD  . LYS A 1 172 ? -22.003 -4.280  -24.483  1.00 57.46 ? 165 LYS A CD  1 
ATOM   1353 C CE  . LYS A 1 172 ? -20.539 -4.315  -24.072  1.00 59.15 ? 165 LYS A CE  1 
ATOM   1354 N NZ  . LYS A 1 172 ? -20.119 -5.656  -23.576  1.00 61.93 ? 165 LYS A NZ  1 
ATOM   1355 N N   . LEU A 1 173 ? -24.252 -0.193  -21.512  1.00 62.25 ? 166 LEU A N   1 
ATOM   1356 C CA  . LEU A 1 173 ? -25.077 0.042   -20.340  1.00 66.58 ? 166 LEU A CA  1 
ATOM   1357 C C   . LEU A 1 173 ? -24.759 1.401   -19.720  1.00 67.47 ? 166 LEU A C   1 
ATOM   1358 O O   . LEU A 1 173 ? -25.196 1.706   -18.612  1.00 67.12 ? 166 LEU A O   1 
ATOM   1359 C CB  . LEU A 1 173 ? -24.854 -1.079  -19.325  1.00 69.93 ? 166 LEU A CB  1 
ATOM   1360 C CG  . LEU A 1 173 ? -24.875 -2.480  -19.946  1.00 68.46 ? 166 LEU A CG  1 
ATOM   1361 C CD1 . LEU A 1 173 ? -23.996 -3.431  -19.166  1.00 70.13 ? 166 LEU A CD1 1 
ATOM   1362 C CD2 . LEU A 1 173 ? -26.286 -3.017  -20.029  1.00 65.78 ? 166 LEU A CD2 1 
ATOM   1363 N N   . ILE B 1 1   ? -1.068  9.369   -88.202  1.00 49.10 ? -3  ILE B N   1 
ATOM   1364 C CA  . ILE B 1 1   ? -0.655  8.178   -87.468  1.00 44.38 ? -3  ILE B CA  1 
ATOM   1365 C C   . ILE B 1 1   ? 0.454   8.506   -86.477  1.00 42.19 ? -3  ILE B C   1 
ATOM   1366 O O   . ILE B 1 1   ? 1.413   9.210   -86.801  1.00 35.04 ? -3  ILE B O   1 
ATOM   1367 C CB  . ILE B 1 1   ? -0.229  7.039   -88.417  1.00 48.80 ? -3  ILE B CB  1 
ATOM   1368 C CG1 . ILE B 1 1   ? 0.988   7.468   -89.243  1.00 51.71 ? -3  ILE B CG1 1 
ATOM   1369 C CG2 . ILE B 1 1   ? -1.390  6.621   -89.311  1.00 53.16 ? -3  ILE B CG2 1 
ATOM   1370 C CD1 . ILE B 1 1   ? 1.248   6.620   -90.462  1.00 54.93 ? -3  ILE B CD1 1 
ATOM   1371 N N   . ASP B 1 2   ? 0.313   7.996   -85.261  1.00 38.45 ? -2  ASP B N   1 
ATOM   1372 C CA  . ASP B 1 2   ? 1.356   8.147   -84.261  1.00 35.77 ? -2  ASP B CA  1 
ATOM   1373 C C   . ASP B 1 2   ? 2.490   7.178   -84.561  1.00 35.13 ? -2  ASP B C   1 
ATOM   1374 O O   . ASP B 1 2   ? 2.260   6.025   -84.935  1.00 36.95 ? -2  ASP B O   1 
ATOM   1375 C CB  . ASP B 1 2   ? 0.795   7.874   -82.866  1.00 41.04 ? -2  ASP B CB  1 
ATOM   1376 C CG  . ASP B 1 2   ? -0.073  9.011   -82.356  1.00 47.64 ? -2  ASP B CG  1 
ATOM   1377 O OD1 . ASP B 1 2   ? 0.064   10.143  -82.870  1.00 52.41 ? -2  ASP B OD1 1 
ATOM   1378 O OD2 . ASP B 1 2   ? -0.891  8.773   -81.442  1.00 52.84 ? -2  ASP B OD2 1 
ATOM   1379 N N   . THR B 1 3   ? 3.725   7.660   -84.415  1.00 26.92 ? -1  THR B N   1 
ATOM   1380 C CA  . THR B 1 3   ? 4.897   6.828   -84.655  1.00 24.20 ? -1  THR B CA  1 
ATOM   1381 C C   . THR B 1 3   ? 5.865   6.798   -83.477  1.00 28.49 ? -1  THR B C   1 
ATOM   1382 O O   . THR B 1 3   ? 7.018   6.395   -83.658  1.00 28.50 ? -1  THR B O   1 
ATOM   1383 C CB  . THR B 1 3   ? 5.636   7.274   -85.923  1.00 27.79 ? -1  THR B CB  1 
ATOM   1384 O OG1 . THR B 1 3   ? 5.909   8.679   -85.851  1.00 33.42 ? -1  THR B OG1 1 
ATOM   1385 C CG2 . THR B 1 3   ? 4.793   6.980   -87.169  1.00 28.96 ? -1  THR B CG2 1 
ATOM   1386 N N   . ASP B 1 4   ? 5.444   7.224   -82.288  1.00 24.90 ? 0   ASP B N   1 
ATOM   1387 C CA  . ASP B 1 4   ? 6.289   7.056   -81.111  1.00 22.17 ? 0   ASP B CA  1 
ATOM   1388 C C   . ASP B 1 4   ? 6.445   5.569   -80.814  1.00 18.80 ? 0   ASP B C   1 
ATOM   1389 O O   . ASP B 1 4   ? 5.495   4.793   -80.979  1.00 24.91 ? 0   ASP B O   1 
ATOM   1390 C CB  . ASP B 1 4   ? 5.638   7.767   -79.924  1.00 23.67 ? 0   ASP B CB  1 
ATOM   1391 C CG  . ASP B 1 4   ? 4.275   7.194   -79.580  1.00 27.87 ? 0   ASP B CG  1 
ATOM   1392 O OD1 . ASP B 1 4   ? 3.299   7.482   -80.304  1.00 34.88 ? 0   ASP B OD1 1 
ATOM   1393 O OD2 . ASP B 1 4   ? 4.172   6.441   -78.593  1.00 29.77 ? 0   ASP B OD2 1 
ATOM   1394 N N   . ALA B 1 5   ? 7.642   5.161   -80.383  1.00 18.38 ? 1   ALA B N   1 
ATOM   1395 C CA  . ALA B 1 5   ? 7.945   3.735   -80.199  1.00 18.89 ? 1   ALA B CA  1 
ATOM   1396 C C   . ALA B 1 5   ? 9.311   3.566   -79.503  1.00 20.00 ? 1   ALA B C   1 
ATOM   1397 O O   . ALA B 1 5   ? 9.919   4.544   -79.042  1.00 18.06 ? 1   ALA B O   1 
ATOM   1398 C CB  . ALA B 1 5   ? 7.877   3.004   -81.542  1.00 22.29 ? 1   ALA B CB  1 
ATOM   1399 N N   . VAL B 1 6   ? 9.812   2.311   -79.443  1.00 18.24 ? 2   VAL B N   1 
ATOM   1400 C CA  . VAL B 1 6   ? 11.096  1.953   -78.827  1.00 16.14 ? 2   VAL B CA  1 
ATOM   1401 C C   . VAL B 1 6   ? 12.042  1.362   -79.868  1.00 15.70 ? 2   VAL B C   1 
ATOM   1402 O O   . VAL B 1 6   ? 11.617  0.880   -80.925  1.00 16.06 ? 2   VAL B O   1 
ATOM   1403 C CB  . VAL B 1 6   ? 10.920  0.987   -77.634  1.00 15.14 ? 2   VAL B CB  1 
ATOM   1404 C CG1 . VAL B 1 6   ? 9.816   1.533   -76.718  1.00 18.12 ? 2   VAL B CG1 1 
ATOM   1405 C CG2 . VAL B 1 6   ? 10.563  -0.449  -78.072  1.00 15.07 ? 2   VAL B CG2 1 
ATOM   1406 N N   . VAL B 1 7   ? 13.342  1.340   -79.555  1.00 15.29 ? 3   VAL B N   1 
ATOM   1407 C CA  . VAL B 1 7   ? 14.304  0.834   -80.552  1.00 15.33 ? 3   VAL B CA  1 
ATOM   1408 C C   . VAL B 1 7   ? 14.184  -0.682  -80.713  1.00 15.11 ? 3   VAL B C   1 
ATOM   1409 O O   . VAL B 1 7   ? 13.720  -1.415  -79.829  1.00 14.77 ? 3   VAL B O   1 
ATOM   1410 C CB  . VAL B 1 7   ? 15.749  1.241   -80.223  1.00 15.34 ? 3   VAL B CB  1 
ATOM   1411 C CG1 . VAL B 1 7   ? 15.873  2.753   -80.135  1.00 19.52 ? 3   VAL B CG1 1 
ATOM   1412 C CG2 . VAL B 1 7   ? 16.233  0.545   -78.965  1.00 18.10 ? 3   VAL B CG2 1 
ATOM   1413 N N   . GLY B 1 8   ? 14.643  -1.168  -81.870  1.00 15.94 ? 4   GLY B N   1 
ATOM   1414 C CA  . GLY B 1 8   ? 14.433  -2.563  -82.222  1.00 15.31 ? 4   GLY B CA  1 
ATOM   1415 C C   . GLY B 1 8   ? 15.179  -3.568  -81.381  1.00 14.69 ? 4   GLY B C   1 
ATOM   1416 O O   . GLY B 1 8   ? 14.746  -4.723  -81.310  1.00 16.63 ? 4   GLY B O   1 
ATOM   1417 N N   . ASP B 1 9   ? 16.285  -3.173  -80.754  1.00 15.67 ? 5   ASP B N   1 
ATOM   1418 C CA  . ASP B 1 9   ? 17.050  -4.133  -79.968  1.00 18.14 ? 5   ASP B CA  1 
ATOM   1419 C C   . ASP B 1 9   ? 16.501  -4.330  -78.566  1.00 16.88 ? 5   ASP B C   1 
ATOM   1420 O O   . ASP B 1 9   ? 17.078  -5.114  -77.804  1.00 19.84 ? 5   ASP B O   1 
ATOM   1421 C CB  . ASP B 1 9   ? 18.537  -3.767  -79.926  1.00 27.07 ? 5   ASP B CB  1 
ATOM   1422 C CG  . ASP B 1 9   ? 19.209  -3.906  -81.276  1.00 39.77 ? 5   ASP B CG  1 
ATOM   1423 O OD1 . ASP B 1 9   ? 18.718  -4.691  -82.121  1.00 44.66 ? 5   ASP B OD1 1 
ATOM   1424 O OD2 . ASP B 1 9   ? 20.224  -3.219  -81.490  1.00 47.40 ? 5   ASP B OD2 1 
ATOM   1425 N N   . THR B 1 10  ? 15.412  -3.643  -78.223  1.00 15.28 ? 6   THR B N   1 
ATOM   1426 C CA  . THR B 1 10  ? 14.803  -3.768  -76.901  1.00 14.91 ? 6   THR B CA  1 
ATOM   1427 C C   . THR B 1 10  ? 14.319  -5.203  -76.707  1.00 16.71 ? 6   THR B C   1 
ATOM   1428 O O   . THR B 1 10  ? 13.562  -5.729  -77.535  1.00 15.58 ? 6   THR B O   1 
ATOM   1429 C CB  . THR B 1 10  ? 13.595  -2.831  -76.841  1.00 15.88 ? 6   THR B CB  1 
ATOM   1430 O OG1 . THR B 1 10  ? 14.009  -1.474  -77.084  1.00 16.02 ? 6   THR B OG1 1 
ATOM   1431 C CG2 . THR B 1 10  ? 12.914  -2.907  -75.502  1.00 15.63 ? 6   THR B CG2 1 
ATOM   1432 N N   . ILE B 1 11  ? 14.714  -5.836  -75.606  1.00 15.19 ? 7   ILE B N   1 
ATOM   1433 C CA  . ILE B 1 11  ? 14.352  -7.223  -75.323  1.00 16.31 ? 7   ILE B CA  1 
ATOM   1434 C C   . ILE B 1 11  ? 12.989  -7.266  -74.645  1.00 14.81 ? 7   ILE B C   1 
ATOM   1435 O O   . ILE B 1 11  ? 12.730  -6.523  -73.681  1.00 14.32 ? 7   ILE B O   1 
ATOM   1436 C CB  . ILE B 1 11  ? 15.414  -7.891  -74.440  1.00 17.66 ? 7   ILE B CB  1 
ATOM   1437 C CG1 . ILE B 1 11  ? 16.748  -7.948  -75.194  1.00 19.56 ? 7   ILE B CG1 1 
ATOM   1438 C CG2 . ILE B 1 11  ? 14.925  -9.248  -73.961  1.00 20.90 ? 7   ILE B CG2 1 
ATOM   1439 C CD1 . ILE B 1 11  ? 17.881  -8.590  -74.406  1.00 29.29 ? 7   ILE B CD1 1 
ATOM   1440 N N   . ILE B 1 12  ? 12.115  -8.136  -75.137  1.00 13.43 ? 8   ILE B N   1 
ATOM   1441 C CA  . ILE B 1 12  ? 10.777  -8.312  -74.582  1.00 14.69 ? 8   ILE B CA  1 
ATOM   1442 C C   . ILE B 1 12  ? 10.498  -9.795  -74.332  1.00 14.68 ? 8   ILE B C   1 
ATOM   1443 O O   . ILE B 1 12  ? 11.128  -10.677 -74.923  1.00 15.77 ? 8   ILE B O   1 
ATOM   1444 C CB  . ILE B 1 12  ? 9.698   -7.714  -75.518  1.00 14.69 ? 8   ILE B CB  1 
ATOM   1445 C CG1 . ILE B 1 12  ? 9.726   -8.412  -76.897  1.00 16.13 ? 8   ILE B CG1 1 
ATOM   1446 C CG2 . ILE B 1 12  ? 9.913   -6.212  -75.684  1.00 15.22 ? 8   ILE B CG2 1 
ATOM   1447 C CD1 . ILE B 1 12  ? 8.459   -8.147  -77.707  1.00 14.88 ? 8   ILE B CD1 1 
ATOM   1448 N N   . ASP B 1 13  ? 9.515   -10.059 -73.477  1.00 14.61 ? 9   ASP B N   1 
ATOM   1449 C CA  . ASP B 1 13  ? 8.989   -11.408 -73.277  1.00 14.73 ? 9   ASP B CA  1 
ATOM   1450 C C   . ASP B 1 13  ? 7.935   -11.673 -74.338  1.00 14.49 ? 9   ASP B C   1 
ATOM   1451 O O   . ASP B 1 13  ? 7.044   -10.843 -74.570  1.00 16.09 ? 9   ASP B O   1 
ATOM   1452 C CB  . ASP B 1 13  ? 8.341   -11.542 -71.887  1.00 16.79 ? 9   ASP B CB  1 
ATOM   1453 C CG  . ASP B 1 13  ? 7.640   -12.903 -71.663  1.00 19.44 ? 9   ASP B CG  1 
ATOM   1454 O OD1 . ASP B 1 13  ? 6.641   -13.221 -72.333  1.00 23.57 ? 9   ASP B OD1 1 
ATOM   1455 O OD2 . ASP B 1 13  ? 8.074   -13.639 -70.751  1.00 25.58 ? 9   ASP B OD2 1 
ATOM   1456 N N   . VAL B 1 14  ? 8.048   -12.803 -75.025  1.00 13.91 ? 10  VAL B N   1 
ATOM   1457 C CA  . VAL B 1 14  ? 6.994   -13.278 -75.906  1.00 14.91 ? 10  VAL B CA  1 
ATOM   1458 C C   . VAL B 1 14  ? 6.667   -14.696 -75.466  1.00 14.76 ? 10  VAL B C   1 
ATOM   1459 O O   . VAL B 1 14  ? 7.474   -15.613 -75.681  1.00 15.86 ? 10  VAL B O   1 
ATOM   1460 C CB  . VAL B 1 14  ? 7.394   -13.249 -77.391  1.00 15.02 ? 10  VAL B CB  1 
ATOM   1461 C CG1 . VAL B 1 14  ? 6.205   -13.695 -78.276  1.00 18.18 ? 10  VAL B CG1 1 
ATOM   1462 C CG2 . VAL B 1 14  ? 7.889   -11.862 -77.789  1.00 17.38 ? 10  VAL B CG2 1 
ATOM   1463 N N   . SER B 1 15  ? 5.522   -14.872 -74.808  1.00 14.68 ? 11  SER B N   1 
ATOM   1464 C CA  . SER B 1 15  ? 5.079   -16.181 -74.332  1.00 14.11 ? 11  SER B CA  1 
ATOM   1465 C C   . SER B 1 15  ? 6.163   -16.921 -73.552  1.00 14.93 ? 11  SER B C   1 
ATOM   1466 O O   . SER B 1 15  ? 6.321   -18.135 -73.692  1.00 18.42 ? 11  SER B O   1 
ATOM   1467 C CB  . SER B 1 15  ? 4.544   -17.044 -75.466  1.00 18.37 ? 11  SER B CB  1 
ATOM   1468 O OG  . SER B 1 15  ? 3.465   -16.396 -76.106  1.00 18.59 ? 11  SER B OG  1 
ATOM   1469 N N   . GLY B 1 16  ? 6.914   -16.200 -72.716  1.00 13.66 ? 12  GLY B N   1 
ATOM   1470 C CA  . GLY B 1 16  ? 7.900   -16.828 -71.853  1.00 14.47 ? 12  GLY B CA  1 
ATOM   1471 C C   . GLY B 1 16  ? 9.303   -16.908 -72.419  1.00 19.08 ? 12  GLY B C   1 
ATOM   1472 O O   . GLY B 1 16  ? 10.240  -17.232 -71.677  1.00 20.86 ? 12  GLY B O   1 
ATOM   1473 N N   . LYS B 1 17  ? 9.482   -16.642 -73.700  1.00 16.72 ? 13  LYS B N   1 
ATOM   1474 C CA  . LYS B 1 17  ? 10.776  -16.534 -74.356  1.00 19.42 ? 13  LYS B CA  1 
ATOM   1475 C C   . LYS B 1 17  ? 11.179  -15.071 -74.381  1.00 17.63 ? 13  LYS B C   1 
ATOM   1476 O O   . LYS B 1 17  ? 10.333  -14.180 -74.298  1.00 20.14 ? 13  LYS B O   1 
ATOM   1477 C CB  . LYS B 1 17  ? 10.673  -16.999 -75.816  1.00 22.29 ? 13  LYS B CB  1 
ATOM   1478 C CG  . LYS B 1 17  ? 10.082  -18.361 -76.015  1.00 27.52 ? 13  LYS B CG  1 
ATOM   1479 C CD  . LYS B 1 17  ? 10.618  -18.969 -77.286  1.00 26.67 ? 13  LYS B CD  1 
ATOM   1480 C CE  . LYS B 1 17  ? 9.866   -18.495 -78.489  1.00 21.93 ? 13  LYS B CE  1 
ATOM   1481 N NZ  . LYS B 1 17  ? 9.972   -19.545 -79.552  1.00 28.43 ? 13  LYS B NZ  1 
ATOM   1482 N N   . LYS B 1 18  ? 12.470  -14.822 -74.523  1.00 16.37 ? 14  LYS B N   1 
ATOM   1483 C CA  . LYS B 1 18  ? 13.005  -13.482 -74.690  1.00 16.88 ? 14  LYS B CA  1 
ATOM   1484 C C   . LYS B 1 18  ? 13.558  -13.328 -76.102  1.00 17.22 ? 14  LYS B C   1 
ATOM   1485 O O   . LYS B 1 18  ? 14.221  -14.230 -76.624  1.00 18.58 ? 14  LYS B O   1 
ATOM   1486 C CB  . LYS B 1 18  ? 14.124  -13.201 -73.681  1.00 21.11 ? 14  LYS B CB  1 
ATOM   1487 C CG  . LYS B 1 18  ? 13.647  -13.100 -72.233  1.00 29.86 ? 14  LYS B CG  1 
ATOM   1488 C CD  . LYS B 1 18  ? 12.839  -11.836 -72.012  1.00 33.00 ? 14  LYS B CD  1 
ATOM   1489 C CE  . LYS B 1 18  ? 12.378  -11.703 -70.565  1.00 38.43 ? 14  LYS B CE  1 
ATOM   1490 N NZ  . LYS B 1 18  ? 13.529  -11.667 -69.622  1.00 41.55 ? 14  LYS B NZ  1 
ATOM   1491 N N   . MET B 1 19  ? 13.275  -12.191 -76.716  1.00 15.64 ? 15  MET B N   1 
ATOM   1492 C CA  . MET B 1 19  ? 13.843  -11.840 -78.015  1.00 16.16 ? 15  MET B CA  1 
ATOM   1493 C C   . MET B 1 19  ? 13.739  -10.326 -78.152  1.00 14.67 ? 15  MET B C   1 
ATOM   1494 O O   . MET B 1 19  ? 13.032  -9.672  -77.379  1.00 14.47 ? 15  MET B O   1 
ATOM   1495 C CB  . MET B 1 19  ? 13.128  -12.566 -79.159  1.00 15.62 ? 15  MET B CB  1 
ATOM   1496 C CG  . MET B 1 19  ? 11.708  -12.113 -79.370  1.00 14.44 ? 15  MET B CG  1 
ATOM   1497 S SD  . MET B 1 19  ? 10.842  -13.082 -80.618  1.00 19.87 ? 15  MET B SD  1 
ATOM   1498 C CE  . MET B 1 19  ? 10.375  -14.513 -79.671  1.00 23.89 ? 15  MET B CE  1 
ATOM   1499 N N   . THR B 1 20  ? 14.460  -9.763  -79.117  1.00 15.29 ? 16  THR B N   1 
ATOM   1500 C CA  . THR B 1 20  ? 14.266  -8.332  -79.356  1.00 15.30 ? 16  THR B CA  1 
ATOM   1501 C C   . THR B 1 20  ? 12.921  -8.072  -80.032  1.00 14.23 ? 16  THR B C   1 
ATOM   1502 O O   . THR B 1 20  ? 12.351  -8.935  -80.710  1.00 14.06 ? 16  THR B O   1 
ATOM   1503 C CB  . THR B 1 20  ? 15.380  -7.714  -80.194  1.00 14.09 ? 16  THR B CB  1 
ATOM   1504 O OG1 . THR B 1 20  ? 15.219  -8.112  -81.562  1.00 16.23 ? 16  THR B OG1 1 
ATOM   1505 C CG2 . THR B 1 20  ? 16.767  -8.136  -79.685  1.00 16.72 ? 16  THR B CG2 1 
ATOM   1506 N N   . ILE B 1 21  ? 12.409  -6.855  -79.843  1.00 13.73 ? 17  ILE B N   1 
ATOM   1507 C CA  . ILE B 1 21  ? 11.141  -6.500  -80.473  1.00 13.08 ? 17  ILE B CA  1 
ATOM   1508 C C   . ILE B 1 21  ? 11.252  -6.541  -82.002  1.00 13.72 ? 17  ILE B C   1 
ATOM   1509 O O   . ILE B 1 21  ? 10.291  -6.908  -82.691  1.00 13.69 ? 17  ILE B O   1 
ATOM   1510 C CB  . ILE B 1 21  ? 10.596  -5.169  -79.901  1.00 12.76 ? 17  ILE B CB  1 
ATOM   1511 C CG1 . ILE B 1 21  ? 9.143   -4.964  -80.311  1.00 12.85 ? 17  ILE B CG1 1 
ATOM   1512 C CG2 . ILE B 1 21  ? 11.471  -3.988  -80.274  1.00 14.76 ? 17  ILE B CG2 1 
ATOM   1513 C CD1 . ILE B 1 21  ? 8.461   -3.841  -79.582  1.00 14.18 ? 17  ILE B CD1 1 
ATOM   1514 N N   . ALA B 1 22  ? 12.421  -6.191  -82.548  1.00 13.36 ? 18  ALA B N   1 
ATOM   1515 C CA  . ALA B 1 22  ? 12.639  -6.319  -83.989  1.00 14.82 ? 18  ALA B CA  1 
ATOM   1516 C C   . ALA B 1 22  ? 12.604  -7.778  -84.439  1.00 15.45 ? 18  ALA B C   1 
ATOM   1517 O O   . ALA B 1 22  ? 11.980  -8.105  -85.459  1.00 15.40 ? 18  ALA B O   1 
ATOM   1518 C CB  . ALA B 1 22  ? 13.949  -5.650  -84.395  1.00 16.54 ? 18  ALA B CB  1 
ATOM   1519 N N   . GLU B 1 23  ? 13.273  -8.669  -83.697  1.00 14.95 ? 19  GLU B N   1 
ATOM   1520 C CA  . GLU B 1 23  ? 13.210  -10.095 -84.010  1.00 14.34 ? 19  GLU B CA  1 
ATOM   1521 C C   . GLU B 1 23  ? 11.775  -10.606 -83.952  1.00 15.27 ? 19  GLU B C   1 
ATOM   1522 O O   . GLU B 1 23  ? 11.365  -11.429 -84.785  1.00 16.07 ? 19  GLU B O   1 
ATOM   1523 C CB  . GLU B 1 23  ? 14.060  -10.881 -83.013  1.00 16.71 ? 19  GLU B CB  1 
ATOM   1524 C CG  . GLU B 1 23  ? 15.552  -10.827 -83.287  1.00 15.14 ? 19  GLU B CG  1 
ATOM   1525 C CD  . GLU B 1 23  ? 16.372  -11.406 -82.144  1.00 15.41 ? 19  GLU B CD  1 
ATOM   1526 O OE1 . GLU B 1 23  ? 15.839  -11.536 -81.016  1.00 18.43 ? 19  GLU B OE1 1 
ATOM   1527 O OE2 . GLU B 1 23  ? 17.554  -11.753 -82.364  1.00 19.73 ? 19  GLU B OE2 1 
ATOM   1528 N N   . PHE B 1 24  ? 10.989  -10.133 -82.981  1.00 14.25 ? 20  PHE B N   1 
ATOM   1529 C CA  . PHE B 1 24  ? 9.592   -10.548 -82.887  1.00 13.87 ? 20  PHE B CA  1 
ATOM   1530 C C   . PHE B 1 24  ? 8.789   -10.053 -84.090  1.00 14.48 ? 20  PHE B C   1 
ATOM   1531 O O   . PHE B 1 24  ? 8.026   -10.817 -84.702  1.00 15.30 ? 20  PHE B O   1 
ATOM   1532 C CB  . PHE B 1 24  ? 8.989   -10.041 -81.571  1.00 15.12 ? 20  PHE B CB  1 
ATOM   1533 C CG  . PHE B 1 24  ? 7.538   -10.404 -81.384  1.00 13.19 ? 20  PHE B CG  1 
ATOM   1534 C CD1 . PHE B 1 24  ? 7.104   -11.705 -81.570  1.00 16.09 ? 20  PHE B CD1 1 
ATOM   1535 C CD2 . PHE B 1 24  ? 6.616   -9.446  -81.015  1.00 15.89 ? 20  PHE B CD2 1 
ATOM   1536 C CE1 . PHE B 1 24  ? 5.772   -12.041 -81.411  1.00 16.44 ? 20  PHE B CE1 1 
ATOM   1537 C CE2 . PHE B 1 24  ? 5.266   -9.781  -80.855  1.00 18.75 ? 20  PHE B CE2 1 
ATOM   1538 C CZ  . PHE B 1 24  ? 4.861   -11.089 -81.065  1.00 16.27 ? 20  PHE B CZ  1 
ATOM   1539 N N   . TYR B 1 25  ? 8.972   -8.788  -84.476  1.00 12.53 ? 21  TYR B N   1 
ATOM   1540 C CA  . TYR B 1 25  ? 8.331   -8.269  -85.683  1.00 13.62 ? 21  TYR B CA  1 
ATOM   1541 C C   . TYR B 1 25  ? 8.682   -9.116  -86.906  1.00 14.75 ? 21  TYR B C   1 
ATOM   1542 O O   . TYR B 1 25  ? 7.795   -9.518  -87.671  1.00 15.89 ? 21  TYR B O   1 
ATOM   1543 C CB  . TYR B 1 25  ? 8.730   -6.800  -85.922  1.00 14.86 ? 21  TYR B CB  1 
ATOM   1544 C CG  . TYR B 1 25  ? 8.099   -6.250  -87.183  1.00 14.57 ? 21  TYR B CG  1 
ATOM   1545 C CD1 . TYR B 1 25  ? 8.755   -6.351  -88.398  1.00 14.92 ? 21  TYR B CD1 1 
ATOM   1546 C CD2 . TYR B 1 25  ? 6.826   -5.684  -87.160  1.00 16.53 ? 21  TYR B CD2 1 
ATOM   1547 C CE1 . TYR B 1 25  ? 8.155   -5.892  -89.582  1.00 15.98 ? 21  TYR B CE1 1 
ATOM   1548 C CE2 . TYR B 1 25  ? 6.217   -5.223  -88.331  1.00 15.55 ? 21  TYR B CE2 1 
ATOM   1549 C CZ  . TYR B 1 25  ? 6.893   -5.326  -89.530  1.00 16.53 ? 21  TYR B CZ  1 
ATOM   1550 O OH  . TYR B 1 25  ? 6.315   -4.878  -90.713  1.00 18.47 ? 21  TYR B OH  1 
ATOM   1551 N N   . ASP B 1 26  ? 9.963   -9.421  -87.087  1.00 13.80 ? 22  ASP B N   1 
ATOM   1552 C CA  . ASP B 1 26  ? 10.387  -10.168 -88.274  1.00 15.40 ? 22  ASP B CA  1 
ATOM   1553 C C   . ASP B 1 26  ? 9.812   -11.579 -88.266  1.00 17.68 ? 22  ASP B C   1 
ATOM   1554 O O   . ASP B 1 26  ? 9.520   -12.127 -89.333  1.00 21.47 ? 22  ASP B O   1 
ATOM   1555 C CB  . ASP B 1 26  ? 11.917  -10.195 -88.354  1.00 18.73 ? 22  ASP B CB  1 
ATOM   1556 C CG  . ASP B 1 26  ? 12.528  -8.824  -88.653  1.00 23.88 ? 22  ASP B CG  1 
ATOM   1557 O OD1 . ASP B 1 26  ? 11.799  -7.905  -89.079  1.00 24.64 ? 22  ASP B OD1 1 
ATOM   1558 O OD2 . ASP B 1 26  ? 13.757  -8.671  -88.477  1.00 28.74 ? 22  ASP B OD2 1 
ATOM   1559 N N   . SER B 1 27  ? 9.641   -12.175 -87.085  1.00 16.91 ? 23  SER B N   1 
ATOM   1560 C CA  . SER B 1 27  ? 9.108   -13.524 -86.937  1.00 17.95 ? 23  SER B CA  1 
ATOM   1561 C C   . SER B 1 27  ? 7.595   -13.588 -87.103  1.00 20.91 ? 23  SER B C   1 
ATOM   1562 O O   . SER B 1 27  ? 7.042   -14.685 -87.244  1.00 23.43 ? 23  SER B O   1 
ATOM   1563 C CB  . SER B 1 27  ? 9.463   -14.051 -85.540  1.00 22.99 ? 23  SER B CB  1 
ATOM   1564 O OG  . SER B 1 27  ? 8.552   -13.565 -84.567  1.00 25.62 ? 23  SER B OG  1 
ATOM   1565 N N   . THR B 1 28  ? 6.913   -12.468 -87.059  1.00 16.97 ? 24  THR B N   1 
ATOM   1566 C CA  . THR B 1 28  ? 5.462   -12.478 -87.114  1.00 17.20 ? 24  THR B CA  1 
ATOM   1567 C C   . THR B 1 28  ? 5.030   -12.585 -88.577  1.00 15.84 ? 24  THR B C   1 
ATOM   1568 O O   . THR B 1 28  ? 5.507   -11.819 -89.416  1.00 17.42 ? 24  THR B O   1 
ATOM   1569 C CB  . THR B 1 28  ? 4.927   -11.197 -86.459  1.00 15.17 ? 24  THR B CB  1 
ATOM   1570 O OG1 . THR B 1 28  ? 5.253   -11.205 -85.056  1.00 15.53 ? 24  THR B OG1 1 
ATOM   1571 C CG2 . THR B 1 28  ? 3.420   -11.047 -86.611  1.00 16.24 ? 24  THR B CG2 1 
ATOM   1572 N N   . PRO B 1 29  ? 4.139   -13.519 -88.911  1.00 19.55 ? 25  PRO B N   1 
ATOM   1573 C CA  . PRO B 1 29  ? 3.707   -13.636 -90.309  1.00 20.82 ? 25  PRO B CA  1 
ATOM   1574 C C   . PRO B 1 29  ? 3.110   -12.334 -90.819  1.00 19.62 ? 25  PRO B C   1 
ATOM   1575 O O   . PRO B 1 29  ? 2.616   -11.505 -90.053  1.00 17.82 ? 25  PRO B O   1 
ATOM   1576 C CB  . PRO B 1 29  ? 2.660   -14.747 -90.249  1.00 25.28 ? 25  PRO B CB  1 
ATOM   1577 C CG  . PRO B 1 29  ? 3.146   -15.623 -89.148  1.00 24.40 ? 25  PRO B CG  1 
ATOM   1578 C CD  . PRO B 1 29  ? 3.715   -14.675 -88.109  1.00 21.50 ? 25  PRO B CD  1 
ATOM   1579 N N   . ASP B 1 30  ? 3.191   -12.153 -92.134  1.00 19.66 ? 26  ASP B N   1 
ATOM   1580 C CA  . ASP B 1 30  ? 2.820   -10.911 -92.815  1.00 18.83 ? 26  ASP B CA  1 
ATOM   1581 C C   . ASP B 1 30  ? 1.302   -10.768 -92.968  1.00 18.93 ? 26  ASP B C   1 
ATOM   1582 O O   . ASP B 1 30  ? 0.756   -10.693 -94.069  1.00 22.71 ? 26  ASP B O   1 
ATOM   1583 C CB  . ASP B 1 30  ? 3.493   -10.851 -94.179  1.00 22.14 ? 26  ASP B CB  1 
ATOM   1584 C CG  . ASP B 1 30  ? 4.954   -10.490 -94.102  1.00 25.32 ? 26  ASP B CG  1 
ATOM   1585 O OD1 . ASP B 1 30  ? 5.447   -10.213 -92.994  1.00 27.38 ? 26  ASP B OD1 1 
ATOM   1586 O OD2 . ASP B 1 30  ? 5.616   -10.473 -95.166  1.00 29.59 ? 26  ASP B OD2 1 
ATOM   1587 N N   . VAL B 1 31  ? 0.621   -10.740 -91.832  1.00 18.72 ? 27  VAL B N   1 
ATOM   1588 C CA  . VAL B 1 31  ? -0.819  -10.508 -91.767  1.00 17.10 ? 27  VAL B CA  1 
ATOM   1589 C C   . VAL B 1 31  ? -0.975  -9.034  -91.396  1.00 17.22 ? 27  VAL B C   1 
ATOM   1590 O O   . VAL B 1 31  ? -0.993  -8.655  -90.221  1.00 16.08 ? 27  VAL B O   1 
ATOM   1591 C CB  . VAL B 1 31  ? -1.480  -11.446 -90.759  1.00 17.15 ? 27  VAL B CB  1 
ATOM   1592 C CG1 . VAL B 1 31  ? -2.944  -11.130 -90.603  1.00 18.01 ? 27  VAL B CG1 1 
ATOM   1593 C CG2 . VAL B 1 31  ? -1.269  -12.903 -91.165  1.00 19.54 ? 27  VAL B CG2 1 
ATOM   1594 N N   . PHE B 1 32  ? -1.028  -8.168  -92.391  1.00 16.44 ? 28  PHE B N   1 
ATOM   1595 C CA  . PHE B 1 32  ? -0.981  -6.737  -92.125  1.00 15.76 ? 28  PHE B CA  1 
ATOM   1596 C C   . PHE B 1 32  ? -2.358  -6.174  -91.804  1.00 17.27 ? 28  PHE B C   1 
ATOM   1597 O O   . PHE B 1 32  ? -3.332  -6.431  -92.524  1.00 19.56 ? 28  PHE B O   1 
ATOM   1598 C CB  . PHE B 1 32  ? -0.378  -5.990  -93.312  1.00 18.19 ? 28  PHE B CB  1 
ATOM   1599 C CG  . PHE B 1 32  ? 1.090   -6.238  -93.490  1.00 17.17 ? 28  PHE B CG  1 
ATOM   1600 C CD1 . PHE B 1 32  ? 2.001   -5.706  -92.584  1.00 17.84 ? 28  PHE B CD1 1 
ATOM   1601 C CD2 . PHE B 1 32  ? 1.558   -7.035  -94.522  1.00 18.81 ? 28  PHE B CD2 1 
ATOM   1602 C CE1 . PHE B 1 32  ? 3.355   -5.931  -92.743  1.00 17.66 ? 28  PHE B CE1 1 
ATOM   1603 C CE2 . PHE B 1 32  ? 2.919   -7.268  -94.685  1.00 21.66 ? 28  PHE B CE2 1 
ATOM   1604 C CZ  . PHE B 1 32  ? 3.816   -6.721  -93.768  1.00 18.74 ? 28  PHE B CZ  1 
ATOM   1605 N N   . MET B 1 33  ? -2.430  -5.417  -90.709  1.00 17.61 ? 29  MET B N   1 
ATOM   1606 C CA  . MET B 1 33  ? -3.566  -4.561  -90.422  1.00 19.27 ? 29  MET B CA  1 
ATOM   1607 C C   . MET B 1 33  ? -3.415  -3.202  -91.084  1.00 19.58 ? 29  MET B C   1 
ATOM   1608 O O   . MET B 1 33  ? -4.416  -2.559  -91.428  1.00 21.60 ? 29  MET B O   1 
ATOM   1609 C CB  . MET B 1 33  ? -3.666  -4.354  -88.908  1.00 20.66 ? 29  MET B CB  1 
ATOM   1610 C CG  . MET B 1 33  ? -5.039  -3.949  -88.465  1.00 24.51 ? 29  MET B CG  1 
ATOM   1611 S SD  . MET B 1 33  ? -6.168  -5.333  -88.632  1.00 26.99 ? 29  MET B SD  1 
ATOM   1612 C CE  . MET B 1 33  ? -7.715  -4.544  -88.218  1.00 37.34 ? 29  MET B CE  1 
ATOM   1613 N N   . ARG B 1 34  ? -2.181  -2.755  -91.268  1.00 19.16 ? 30  ARG B N   1 
ATOM   1614 C CA  . ARG B 1 34  ? -1.871  -1.503  -91.931  1.00 17.85 ? 30  ARG B CA  1 
ATOM   1615 C C   . ARG B 1 34  ? -0.517  -1.666  -92.590  1.00 19.42 ? 30  ARG B C   1 
ATOM   1616 O O   . ARG B 1 34  ? 0.397   -2.247  -92.003  1.00 19.13 ? 30  ARG B O   1 
ATOM   1617 C CB  . ARG B 1 34  ? -1.810  -0.357  -90.916  1.00 20.39 ? 30  ARG B CB  1 
ATOM   1618 C CG  . ARG B 1 34  ? -1.697  0.995   -91.583  1.00 26.90 ? 30  ARG B CG  1 
ATOM   1619 C CD  . ARG B 1 34  ? -0.954  1.984   -90.727  1.00 40.15 ? 30  ARG B CD  1 
ATOM   1620 N NE  . ARG B 1 34  ? -1.689  2.398   -89.543  1.00 48.30 ? 30  ARG B NE  1 
ATOM   1621 C CZ  . ARG B 1 34  ? -1.118  2.823   -88.417  1.00 46.58 ? 30  ARG B CZ  1 
ATOM   1622 N NH1 . ARG B 1 34  ? 0.204   2.883   -88.314  1.00 45.22 ? 30  ARG B NH1 1 
ATOM   1623 N NH2 . ARG B 1 34  ? -1.871  3.186   -87.390  1.00 48.88 ? 30  ARG B NH2 1 
ATOM   1624 N N   . ARG B 1 35  ? -0.400  -1.192  -93.827  1.00 20.40 ? 31  ARG B N   1 
ATOM   1625 C CA  . ARG B 1 35  ? 0.882   -1.240  -94.518  1.00 19.11 ? 31  ARG B CA  1 
ATOM   1626 C C   . ARG B 1 35  ? 0.954   -0.089  -95.501  1.00 21.22 ? 31  ARG B C   1 
ATOM   1627 O O   . ARG B 1 35  ? 0.091   0.033   -96.380  1.00 22.45 ? 31  ARG B O   1 
ATOM   1628 C CB  . ARG B 1 35  ? 1.091   -2.568  -95.245  1.00 21.99 ? 31  ARG B CB  1 
ATOM   1629 C CG  . ARG B 1 35  ? 2.349   -2.585  -96.105  1.00 20.29 ? 31  ARG B CG  1 
ATOM   1630 C CD  . ARG B 1 35  ? 2.672   -3.950  -96.639  1.00 21.23 ? 31  ARG B CD  1 
ATOM   1631 N NE  . ARG B 1 35  ? 3.878   -3.906  -97.456  1.00 23.64 ? 31  ARG B NE  1 
ATOM   1632 C CZ  . ARG B 1 35  ? 4.374   -4.945  -98.116  1.00 24.61 ? 31  ARG B CZ  1 
ATOM   1633 N NH1 . ARG B 1 35  ? 3.757   -6.114  -98.061  1.00 27.62 ? 31  ARG B NH1 1 
ATOM   1634 N NH2 . ARG B 1 35  ? 5.477   -4.814  -98.844  1.00 28.00 ? 31  ARG B NH2 1 
ATOM   1635 N N   . ASN B 1 36  ? 1.977   0.744   -95.363  1.00 22.24 ? 32  ASN B N   1 
ATOM   1636 C CA  . ASN B 1 36  ? 2.285   1.774   -96.350  1.00 27.32 ? 32  ASN B CA  1 
ATOM   1637 C C   . ASN B 1 36  ? 3.803   1.822   -96.438  1.00 24.10 ? 32  ASN B C   1 
ATOM   1638 O O   . ASN B 1 36  ? 4.456   2.420   -95.572  1.00 22.45 ? 32  ASN B O   1 
ATOM   1639 C CB  . ASN B 1 36  ? 1.709   3.135   -95.979  1.00 29.89 ? 32  ASN B CB  1 
ATOM   1640 C CG  . ASN B 1 36  ? 1.828   4.135   -97.120  1.00 36.99 ? 32  ASN B CG  1 
ATOM   1641 O OD1 . ASN B 1 36  ? 2.901   4.310   -97.700  1.00 34.84 ? 32  ASN B OD1 1 
ATOM   1642 N ND2 . ASN B 1 36  ? 0.715   4.771   -97.469  1.00 47.17 ? 32  ASN B ND2 1 
ATOM   1643 N N   . ASP B 1 37  ? 4.358   1.142   -97.443  1.00 23.27 ? 33  ASP B N   1 
ATOM   1644 C CA  . ASP B 1 37  ? 5.807   1.128   -97.604  1.00 23.96 ? 33  ASP B CA  1 
ATOM   1645 C C   . ASP B 1 37  ? 6.347   2.530   -97.826  1.00 25.51 ? 33  ASP B C   1 
ATOM   1646 O O   . ASP B 1 37  ? 7.466   2.836   -97.400  1.00 29.98 ? 33  ASP B O   1 
ATOM   1647 C CB  . ASP B 1 37  ? 6.245   0.229   -98.768  1.00 25.18 ? 33  ASP B CB  1 
ATOM   1648 C CG  . ASP B 1 37  ? 6.003   -1.246  -98.507  1.00 26.54 ? 33  ASP B CG  1 
ATOM   1649 O OD1 . ASP B 1 37  ? 5.611   -1.612  -97.384  1.00 24.45 ? 33  ASP B OD1 1 
ATOM   1650 O OD2 . ASP B 1 37  ? 6.238   -2.059  -99.424  1.00 31.59 ? 33  ASP B OD2 1 
ATOM   1651 N N   . GLU B 1 38  ? 5.567   3.398   -98.477  1.00 26.38 ? 34  GLU B N   1 
ATOM   1652 C CA  . GLU B 1 38  ? 6.069   4.727   -98.806  1.00 33.34 ? 34  GLU B CA  1 
ATOM   1653 C C   . GLU B 1 38  ? 6.220   5.580   -97.557  1.00 28.75 ? 34  GLU B C   1 
ATOM   1654 O O   . GLU B 1 38  ? 7.181   6.351   -97.441  1.00 32.83 ? 34  GLU B O   1 
ATOM   1655 C CB  . GLU B 1 38  ? 5.144   5.413   -99.813  1.00 37.43 ? 34  GLU B CB  1 
ATOM   1656 C CG  . GLU B 1 38  ? 4.927   4.632   -101.100 1.00 48.99 ? 34  GLU B CG  1 
ATOM   1657 C CD  . GLU B 1 38  ? 3.665   3.790   -101.055 1.00 58.85 ? 34  GLU B CD  1 
ATOM   1658 O OE1 . GLU B 1 38  ? 3.772   2.566   -100.824 1.00 60.38 ? 34  GLU B OE1 1 
ATOM   1659 O OE2 . GLU B 1 38  ? 2.564   4.353   -101.241 1.00 63.08 ? 34  GLU B OE2 1 
ATOM   1660 N N   . ALA B 1 39  ? 5.276   5.463   -96.619  1.00 26.58 ? 35  ALA B N   1 
ATOM   1661 C CA  . ALA B 1 39  ? 5.361   6.127   -95.326  1.00 25.95 ? 35  ALA B CA  1 
ATOM   1662 C C   . ALA B 1 39  ? 6.223   5.372   -94.318  1.00 29.04 ? 35  ALA B C   1 
ATOM   1663 O O   . ALA B 1 39  ? 6.457   5.892   -93.223  1.00 30.25 ? 35  ALA B O   1 
ATOM   1664 C CB  . ALA B 1 39  ? 3.954   6.314   -94.750  1.00 30.69 ? 35  ALA B CB  1 
ATOM   1665 N N   . ARG B 1 40  ? 6.723   4.189   -94.672  1.00 23.67 ? 36  ARG B N   1 
ATOM   1666 C CA  . ARG B 1 40  ? 7.475   3.315   -93.757  1.00 23.88 ? 36  ARG B CA  1 
ATOM   1667 C C   . ARG B 1 40  ? 6.726   3.055   -92.446  1.00 19.90 ? 36  ARG B C   1 
ATOM   1668 O O   . ARG B 1 40  ? 7.195   3.357   -91.345  1.00 21.09 ? 36  ARG B O   1 
ATOM   1669 C CB  . ARG B 1 40  ? 8.897   3.834   -93.529  1.00 22.75 ? 36  ARG B CB  1 
ATOM   1670 C CG  . ARG B 1 40  ? 9.659   3.993   -94.840  1.00 29.83 ? 36  ARG B CG  1 
ATOM   1671 C CD  . ARG B 1 40  ? 11.146  4.207   -94.644  1.00 36.98 ? 36  ARG B CD  1 
ATOM   1672 N NE  . ARG B 1 40  ? 11.858  4.047   -95.908  1.00 41.56 ? 36  ARG B NE  1 
ATOM   1673 C CZ  . ARG B 1 40  ? 12.223  5.056   -96.691  1.00 49.43 ? 36  ARG B CZ  1 
ATOM   1674 N NH1 . ARG B 1 40  ? 11.935  6.303   -96.345  1.00 53.45 ? 36  ARG B NH1 1 
ATOM   1675 N NH2 . ARG B 1 40  ? 12.866  4.817   -97.825  1.00 46.49 ? 36  ARG B NH2 1 
ATOM   1676 N N   . ASP B 1 41  ? 5.545   2.468   -92.592  1.00 19.95 ? 37  ASP B N   1 
ATOM   1677 C CA  . ASP B 1 41  ? 4.609   2.282   -91.496  1.00 21.80 ? 37  ASP B CA  1 
ATOM   1678 C C   . ASP B 1 41  ? 3.922   0.942   -91.689  1.00 20.82 ? 37  ASP B C   1 
ATOM   1679 O O   . ASP B 1 41  ? 3.277   0.717   -92.720  1.00 20.97 ? 37  ASP B O   1 
ATOM   1680 C CB  . ASP B 1 41  ? 3.583   3.410   -91.512  1.00 27.51 ? 37  ASP B CB  1 
ATOM   1681 C CG  . ASP B 1 41  ? 2.549   3.259   -90.447  1.00 38.07 ? 37  ASP B CG  1 
ATOM   1682 O OD1 . ASP B 1 41  ? 2.887   2.775   -89.352  1.00 37.65 ? 37  ASP B OD1 1 
ATOM   1683 O OD2 . ASP B 1 41  ? 1.400   3.651   -90.701  1.00 45.33 ? 37  ASP B OD2 1 
ATOM   1684 N N   . TRP B 1 42  ? 4.058   0.058   -90.704  1.00 17.98 ? 38  TRP B N   1 
ATOM   1685 C CA  . TRP B 1 42  ? 3.532   -1.296  -90.786  1.00 17.93 ? 38  TRP B CA  1 
ATOM   1686 C C   . TRP B 1 42  ? 2.930   -1.699  -89.452  1.00 16.04 ? 38  TRP B C   1 
ATOM   1687 O O   . TRP B 1 42  ? 3.523   -1.454  -88.392  1.00 17.12 ? 38  TRP B O   1 
ATOM   1688 C CB  . TRP B 1 42  ? 4.653   -2.284  -91.110  1.00 16.84 ? 38  TRP B CB  1 
ATOM   1689 C CG  . TRP B 1 42  ? 5.376   -2.005  -92.382  1.00 17.74 ? 38  TRP B CG  1 
ATOM   1690 C CD1 . TRP B 1 42  ? 5.037   -2.460  -93.623  1.00 19.08 ? 38  TRP B CD1 1 
ATOM   1691 C CD2 . TRP B 1 42  ? 6.573   -1.226  -92.555  1.00 18.32 ? 38  TRP B CD2 1 
ATOM   1692 N NE1 . TRP B 1 42  ? 5.938   -2.010  -94.555  1.00 20.38 ? 38  TRP B NE1 1 
ATOM   1693 C CE2 . TRP B 1 42  ? 6.891   -1.251  -93.928  1.00 20.58 ? 38  TRP B CE2 1 
ATOM   1694 C CE3 . TRP B 1 42  ? 7.410   -0.519  -91.682  1.00 18.94 ? 38  TRP B CE3 1 
ATOM   1695 C CZ2 . TRP B 1 42  ? 8.003   -0.597  -94.447  1.00 20.91 ? 38  TRP B CZ2 1 
ATOM   1696 C CZ3 . TRP B 1 42  ? 8.512   0.140   -92.202  1.00 19.59 ? 38  TRP B CZ3 1 
ATOM   1697 C CH2 . TRP B 1 42  ? 8.798   0.094   -93.573  1.00 21.84 ? 38  TRP B CH2 1 
ATOM   1698 N N   . VAL B 1 43  ? 1.772   -2.352  -89.511  1.00 15.21 ? 39  VAL B N   1 
ATOM   1699 C CA  . VAL B 1 43  ? 1.133   -2.963  -88.346  1.00 15.30 ? 39  VAL B CA  1 
ATOM   1700 C C   . VAL B 1 43  ? 0.739   -4.384  -88.716  1.00 15.19 ? 39  VAL B C   1 
ATOM   1701 O O   . VAL B 1 43  ? -0.009  -4.589  -89.685  1.00 16.01 ? 39  VAL B O   1 
ATOM   1702 C CB  . VAL B 1 43  ? -0.110  -2.177  -87.888  1.00 15.89 ? 39  VAL B CB  1 
ATOM   1703 C CG1 . VAL B 1 43  ? -0.691  -2.807  -86.661  1.00 17.46 ? 39  VAL B CG1 1 
ATOM   1704 C CG2 . VAL B 1 43  ? 0.228   -0.701  -87.628  1.00 16.94 ? 39  VAL B CG2 1 
ATOM   1705 N N   . LYS B 1 44  ? 1.213   -5.354  -87.940  1.00 15.37 ? 40  LYS B N   1 
ATOM   1706 C CA  . LYS B 1 44  ? 0.864   -6.758  -88.121  1.00 15.49 ? 40  LYS B CA  1 
ATOM   1707 C C   . LYS B 1 44  ? -0.069  -7.216  -87.008  1.00 15.33 ? 40  LYS B C   1 
ATOM   1708 O O   . LYS B 1 44  ? 0.118   -6.841  -85.843  1.00 13.82 ? 40  LYS B O   1 
ATOM   1709 C CB  . LYS B 1 44  ? 2.103   -7.663  -88.107  1.00 14.21 ? 40  LYS B CB  1 
ATOM   1710 C CG  . LYS B 1 44  ? 3.030   -7.514  -89.299  1.00 15.66 ? 40  LYS B CG  1 
ATOM   1711 C CD  . LYS B 1 44  ? 4.236   -8.440  -89.137  1.00 15.18 ? 40  LYS B CD  1 
ATOM   1712 C CE  . LYS B 1 44  ? 5.186   -8.291  -90.301  1.00 16.20 ? 40  LYS B CE  1 
ATOM   1713 N NZ  . LYS B 1 44  ? 6.358   -9.184  -90.123  1.00 17.28 ? 40  LYS B NZ  1 
ATOM   1714 N N   . ARG B 1 45  ? -1.072  -8.014  -87.371  1.00 15.26 ? 41  ARG B N   1 
ATOM   1715 C CA  . ARG B 1 45  ? -1.841  -8.757  -86.382  1.00 15.08 ? 41  ARG B CA  1 
ATOM   1716 C C   . ARG B 1 45  ? -0.949  -9.840  -85.785  1.00 16.98 ? 41  ARG B C   1 
ATOM   1717 O O   . ARG B 1 45  ? -0.098  -10.416 -86.471  1.00 18.43 ? 41  ARG B O   1 
ATOM   1718 C CB  . ARG B 1 45  ? -3.065  -9.383  -87.049  1.00 15.30 ? 41  ARG B CB  1 
ATOM   1719 C CG  . ARG B 1 45  ? -3.984  -8.363  -87.698  1.00 16.98 ? 41  ARG B CG  1 
ATOM   1720 C CD  . ARG B 1 45  ? -5.160  -9.043  -88.400  1.00 18.77 ? 41  ARG B CD  1 
ATOM   1721 N NE  . ARG B 1 45  ? -6.089  -9.655  -87.448  1.00 20.40 ? 41  ARG B NE  1 
ATOM   1722 C CZ  . ARG B 1 45  ? -6.904  -10.660 -87.749  1.00 21.61 ? 41  ARG B CZ  1 
ATOM   1723 N NH1 . ARG B 1 45  ? -6.886  -11.189 -88.960  1.00 19.70 ? 41  ARG B NH1 1 
ATOM   1724 N NH2 . ARG B 1 45  ? -7.717  -11.158 -86.822  1.00 27.69 ? 41  ARG B NH2 1 
ATOM   1725 N N   . VAL B 1 46  ? -1.110  -10.105 -84.486  1.00 17.34 ? 42  VAL B N   1 
ATOM   1726 C CA  . VAL B 1 46  ? -0.307  -11.108 -83.799  1.00 18.26 ? 42  VAL B CA  1 
ATOM   1727 C C   . VAL B 1 46  ? -1.231  -12.198 -83.293  1.00 20.33 ? 42  VAL B C   1 
ATOM   1728 O O   . VAL B 1 46  ? -2.253  -11.900 -82.673  1.00 19.27 ? 42  VAL B O   1 
ATOM   1729 C CB  . VAL B 1 46  ? 0.485   -10.480 -82.641  1.00 15.01 ? 42  VAL B CB  1 
ATOM   1730 C CG1 . VAL B 1 46  ? 1.159   -11.562 -81.801  1.00 18.35 ? 42  VAL B CG1 1 
ATOM   1731 C CG2 . VAL B 1 46  ? 1.511   -9.554  -83.203  1.00 16.59 ? 42  VAL B CG2 1 
ATOM   1732 N N   . GLY B 1 47  ? -0.854  -13.454 -83.531  1.00 20.82 ? 43  GLY B N   1 
ATOM   1733 C CA  . GLY B 1 47  ? -1.660  -14.570 -83.070  1.00 21.40 ? 43  GLY B CA  1 
ATOM   1734 C C   . GLY B 1 47  ? -0.950  -15.490 -82.095  1.00 18.56 ? 43  GLY B C   1 
ATOM   1735 O O   . GLY B 1 47  ? 0.194   -15.899 -82.323  1.00 22.56 ? 43  GLY B O   1 
ATOM   1736 N N   . GLY B 1 48  ? -1.643  -15.811 -81.007  1.00 19.51 ? 44  GLY B N   1 
ATOM   1737 C CA  . GLY B 1 48  ? -1.195  -16.816 -80.057  1.00 18.72 ? 44  GLY B CA  1 
ATOM   1738 C C   . GLY B 1 48  ? -0.047  -16.418 -79.154  1.00 17.91 ? 44  GLY B C   1 
ATOM   1739 O O   . GLY B 1 48  ? 0.566   -17.304 -78.558  1.00 22.21 ? 44  GLY B O   1 
ATOM   1740 N N   . LYS B 1 49  ? 0.225   -15.116 -78.966  1.00 16.30 ? 45  LYS B N   1 
ATOM   1741 C CA  . LYS B 1 49  ? 1.366   -14.654 -78.183  1.00 14.64 ? 45  LYS B CA  1 
ATOM   1742 C C   . LYS B 1 49  ? 0.917   -13.770 -77.031  1.00 14.50 ? 45  LYS B C   1 
ATOM   1743 O O   . LYS B 1 49  ? -0.075  -13.042 -77.126  1.00 18.22 ? 45  LYS B O   1 
ATOM   1744 C CB  . LYS B 1 49  ? 2.348   -13.867 -79.053  1.00 14.93 ? 45  LYS B CB  1 
ATOM   1745 C CG  . LYS B 1 49  ? 2.755   -14.555 -80.366  1.00 17.72 ? 45  LYS B CG  1 
ATOM   1746 C CD  . LYS B 1 49  ? 3.418   -15.893 -80.113  1.00 18.54 ? 45  LYS B CD  1 
ATOM   1747 C CE  . LYS B 1 49  ? 3.922   -16.470 -81.440  1.00 21.08 ? 45  LYS B CE  1 
ATOM   1748 N NZ  . LYS B 1 49  ? 4.325   -17.912 -81.356  1.00 27.74 ? 45  LYS B NZ  1 
ATOM   1749 N N   . THR B 1 50  ? 1.673   -13.834 -75.942  1.00 13.48 ? 46  THR B N   1 
ATOM   1750 C CA  . THR B 1 50  ? 1.434   -13.023 -74.757  1.00 13.14 ? 46  THR B CA  1 
ATOM   1751 C C   . THR B 1 50  ? 2.718   -12.303 -74.350  1.00 15.65 ? 46  THR B C   1 
ATOM   1752 O O   . THR B 1 50  ? 3.819   -12.661 -74.774  1.00 15.06 ? 46  THR B O   1 
ATOM   1753 C CB  . THR B 1 50  ? 0.959   -13.880 -73.586  1.00 16.80 ? 46  THR B CB  1 
ATOM   1754 O OG1 . THR B 1 50  ? 2.010   -14.787 -73.208  1.00 16.93 ? 46  THR B OG1 1 
ATOM   1755 C CG2 . THR B 1 50  ? -0.326  -14.642 -73.927  1.00 18.62 ? 46  THR B CG2 1 
ATOM   1756 N N   . SER B 1 51  ? 2.580   -11.309 -73.474  1.00 14.62 ? 47  SER B N   1 
ATOM   1757 C CA  . SER B 1 51  ? 3.732   -10.673 -72.851  1.00 14.71 ? 47  SER B CA  1 
ATOM   1758 C C   . SER B 1 51  ? 3.388   -10.325 -71.405  1.00 16.56 ? 47  SER B C   1 
ATOM   1759 O O   . SER B 1 51  ? 2.262   -10.517 -70.938  1.00 17.30 ? 47  SER B O   1 
ATOM   1760 C CB  . SER B 1 51  ? 4.235   -9.446  -73.639  1.00 19.19 ? 47  SER B CB  1 
ATOM   1761 O OG  . SER B 1 51  ? 5.561   -9.054  -73.234  1.00 19.44 ? 47  SER B OG  1 
ATOM   1762 N N   . LEU B 1 52  ? 4.397   -9.857  -70.678  1.00 15.83 ? 48  LEU B N   1 
ATOM   1763 C CA  . LEU B 1 52  ? 4.238   -9.454  -69.285  1.00 14.97 ? 48  LEU B CA  1 
ATOM   1764 C C   . LEU B 1 52  ? 3.939   -7.965  -69.206  1.00 17.24 ? 48  LEU B C   1 
ATOM   1765 O O   . LEU B 1 52  ? 4.547   -7.155  -69.915  1.00 20.95 ? 48  LEU B O   1 
ATOM   1766 C CB  . LEU B 1 52  ? 5.528   -9.767  -68.524  1.00 17.01 ? 48  LEU B CB  1 
ATOM   1767 C CG  . LEU B 1 52  ? 5.768   -11.268 -68.382  1.00 19.65 ? 48  LEU B CG  1 
ATOM   1768 C CD1 . LEU B 1 52  ? 7.185   -11.528 -67.872  1.00 26.36 ? 48  LEU B CD1 1 
ATOM   1769 C CD2 . LEU B 1 52  ? 4.722   -11.877 -67.463  1.00 21.97 ? 48  LEU B CD2 1 
ATOM   1770 N N   . SER B 1 53  ? 3.049   -7.608  -68.281  1.00 15.59 ? 49  SER B N   1 
ATOM   1771 C CA  . SER B 1 53  ? 2.561   -6.239  -68.143  1.00 15.21 ? 49  SER B CA  1 
ATOM   1772 C C   . SER B 1 53  ? 2.221   -6.015  -66.678  1.00 15.49 ? 49  SER B C   1 
ATOM   1773 O O   . SER B 1 53  ? 2.281   -6.936  -65.860  1.00 16.68 ? 49  SER B O   1 
ATOM   1774 C CB  . SER B 1 53  ? 1.307   -6.008  -69.003  1.00 15.14 ? 49  SER B CB  1 
ATOM   1775 O OG  . SER B 1 53  ? 0.221   -6.797  -68.538  1.00 16.29 ? 49  SER B OG  1 
ATOM   1776 N N   . VAL B 1 54  ? 1.890   -4.773  -66.340  1.00 14.42 ? 50  VAL B N   1 
ATOM   1777 C CA  . VAL B 1 54  ? 1.440   -4.431  -64.989  1.00 14.13 ? 50  VAL B CA  1 
ATOM   1778 C C   . VAL B 1 54  ? 0.058   -3.798  -65.077  1.00 14.03 ? 50  VAL B C   1 
ATOM   1779 O O   . VAL B 1 54  ? -0.174  -2.875  -65.872  1.00 15.43 ? 50  VAL B O   1 
ATOM   1780 C CB  . VAL B 1 54  ? 2.427   -3.503  -64.260  1.00 15.68 ? 50  VAL B CB  1 
ATOM   1781 C CG1 . VAL B 1 54  ? 1.907   -3.142  -62.858  1.00 15.93 ? 50  VAL B CG1 1 
ATOM   1782 C CG2 . VAL B 1 54  ? 3.789   -4.172  -64.147  1.00 17.26 ? 50  VAL B CG2 1 
ATOM   1783 N N   . ASN B 1 55  ? -0.863  -4.308  -64.276  1.00 14.29 ? 51  ASN B N   1 
ATOM   1784 C CA  . ASN B 1 55  ? -2.178  -3.698  -64.165  1.00 13.64 ? 51  ASN B CA  1 
ATOM   1785 C C   . ASN B 1 55  ? -2.040  -2.434  -63.314  1.00 13.91 ? 51  ASN B C   1 
ATOM   1786 O O   . ASN B 1 55  ? -1.657  -2.509  -62.142  1.00 16.70 ? 51  ASN B O   1 
ATOM   1787 C CB  . ASN B 1 55  ? -3.098  -4.738  -63.521  1.00 15.71 ? 51  ASN B CB  1 
ATOM   1788 C CG  . ASN B 1 55  ? -4.539  -4.275  -63.384  1.00 16.67 ? 51  ASN B CG  1 
ATOM   1789 O OD1 . ASN B 1 55  ? -4.842  -3.174  -62.909  1.00 16.77 ? 51  ASN B OD1 1 
ATOM   1790 N ND2 . ASN B 1 55  ? -5.450  -5.132  -63.814  1.00 19.92 ? 51  ASN B ND2 1 
ATOM   1791 N N   . THR B 1 56  ? -2.302  -1.269  -63.905  1.00 15.99 ? 52  THR B N   1 
ATOM   1792 C CA  . THR B 1 56  ? -2.063  -0.027  -63.175  1.00 19.23 ? 52  THR B CA  1 
ATOM   1793 C C   . THR B 1 56  ? -3.086  0.230   -62.088  1.00 18.29 ? 52  THR B C   1 
ATOM   1794 O O   . THR B 1 56  ? -2.831  1.066   -61.212  1.00 21.42 ? 52  THR B O   1 
ATOM   1795 C CB  . THR B 1 56  ? -2.036  1.170   -64.119  1.00 20.89 ? 52  THR B CB  1 
ATOM   1796 O OG1 . THR B 1 56  ? -3.306  1.306   -64.752  1.00 23.16 ? 52  THR B OG1 1 
ATOM   1797 C CG2 . THR B 1 56  ? -0.939  1.011   -65.170  1.00 23.54 ? 52  THR B CG2 1 
ATOM   1798 N N   . TYR B 1 57  ? -4.208  -0.486  -62.081  1.00 15.03 ? 53  TYR B N   1 
ATOM   1799 C CA  . TYR B 1 57  ? -5.192  -0.352  -61.017  1.00 16.64 ? 53  TYR B CA  1 
ATOM   1800 C C   . TYR B 1 57  ? -4.840  -1.213  -59.809  1.00 18.45 ? 53  TYR B C   1 
ATOM   1801 O O   . TYR B 1 57  ? -4.952  -0.751  -58.663  1.00 19.35 ? 53  TYR B O   1 
ATOM   1802 C CB  . TYR B 1 57  ? -6.573  -0.726  -61.557  1.00 17.74 ? 53  TYR B CB  1 
ATOM   1803 C CG  . TYR B 1 57  ? -7.647  -0.727  -60.520  1.00 19.82 ? 53  TYR B CG  1 
ATOM   1804 C CD1 . TYR B 1 57  ? -8.182  0.458   -60.055  1.00 21.39 ? 53  TYR B CD1 1 
ATOM   1805 C CD2 . TYR B 1 57  ? -8.136  -1.924  -60.003  1.00 21.47 ? 53  TYR B CD2 1 
ATOM   1806 C CE1 . TYR B 1 57  ? -9.171  0.457   -59.081  1.00 22.50 ? 53  TYR B CE1 1 
ATOM   1807 C CE2 . TYR B 1 57  ? -9.114  -1.939  -59.046  1.00 27.25 ? 53  TYR B CE2 1 
ATOM   1808 C CZ  . TYR B 1 57  ? -9.634  -0.749  -58.596  1.00 21.74 ? 53  TYR B CZ  1 
ATOM   1809 O OH  . TYR B 1 57  ? -10.621 -0.762  -57.633  1.00 28.26 ? 53  TYR B OH  1 
ATOM   1810 N N   . SER B 1 58  ? -4.504  -2.488  -60.029  1.00 18.23 ? 54  SER B N   1 
ATOM   1811 C CA  . SER B 1 58  ? -4.192  -3.406  -58.933  1.00 18.58 ? 54  SER B CA  1 
ATOM   1812 C C   . SER B 1 58  ? -2.723  -3.412  -58.551  1.00 18.98 ? 54  SER B C   1 
ATOM   1813 O O   . SER B 1 58  ? -2.389  -3.832  -57.431  1.00 20.15 ? 54  SER B O   1 
ATOM   1814 C CB  . SER B 1 58  ? -4.598  -4.834  -59.286  1.00 19.35 ? 54  SER B CB  1 
ATOM   1815 O OG  . SER B 1 58  ? -3.768  -5.322  -60.318  1.00 19.17 ? 54  SER B OG  1 
ATOM   1816 N N   . GLY B 1 59  ? -1.845  -2.991  -59.449  1.00 17.37 ? 55  GLY B N   1 
ATOM   1817 C CA  . GLY B 1 59  ? -0.417  -3.084  -59.223  1.00 17.73 ? 55  GLY B CA  1 
ATOM   1818 C C   . GLY B 1 59  ? 0.190   -4.445  -59.473  1.00 18.82 ? 55  GLY B C   1 
ATOM   1819 O O   . GLY B 1 59  ? 1.382   -4.628  -59.214  1.00 20.99 ? 55  GLY B O   1 
ATOM   1820 N N   . GLU B 1 60  ? -0.568  -5.392  -60.019  1.00 17.28 ? 56  GLU B N   1 
ATOM   1821 C CA  . GLU B 1 60  ? -0.095  -6.759  -60.180  1.00 18.84 ? 56  GLU B CA  1 
ATOM   1822 C C   . GLU B 1 60  ? 0.461   -6.993  -61.580  1.00 18.34 ? 56  GLU B C   1 
ATOM   1823 O O   . GLU B 1 60  ? -0.036  -6.439  -62.567  1.00 17.66 ? 56  GLU B O   1 
ATOM   1824 C CB  . GLU B 1 60  ? -1.235  -7.753  -59.954  1.00 20.84 ? 56  GLU B CB  1 
ATOM   1825 C CG  . GLU B 1 60  ? -1.720  -7.841  -58.506  1.00 28.72 ? 56  GLU B CG  1 
ATOM   1826 C CD  . GLU B 1 60  ? -0.645  -8.346  -57.550  1.00 41.98 ? 56  GLU B CD  1 
ATOM   1827 O OE1 . GLU B 1 60  ? -0.039  -9.402  -57.829  1.00 45.55 ? 56  GLU B OE1 1 
ATOM   1828 O OE2 . GLU B 1 60  ? -0.405  -7.688  -56.513  1.00 47.36 ? 56  GLU B OE2 1 
ATOM   1829 N N   . VAL B 1 61  ? 1.501   -7.826  -61.664  1.00 17.69 ? 57  VAL B N   1 
ATOM   1830 C CA  . VAL B 1 61  ? 2.008   -8.281  -62.954  1.00 18.20 ? 57  VAL B CA  1 
ATOM   1831 C C   . VAL B 1 61  ? 1.017   -9.273  -63.540  1.00 20.10 ? 57  VAL B C   1 
ATOM   1832 O O   . VAL B 1 61  ? 0.519   -10.173 -62.843  1.00 22.27 ? 57  VAL B O   1 
ATOM   1833 C CB  . VAL B 1 61  ? 3.397   -8.914  -62.786  1.00 19.62 ? 57  VAL B CB  1 
ATOM   1834 C CG1 . VAL B 1 61  ? 3.859   -9.542  -64.096  1.00 20.54 ? 57  VAL B CG1 1 
ATOM   1835 C CG2 . VAL B 1 61  ? 4.381   -7.869  -62.270  1.00 19.78 ? 57  VAL B CG2 1 
ATOM   1836 N N   . GLU B 1 62  ? 0.707   -9.108  -64.826  1.00 16.63 ? 58  GLU B N   1 
ATOM   1837 C CA  . GLU B 1 62  ? -0.226  -9.986  -65.506  1.00 19.24 ? 58  GLU B CA  1 
ATOM   1838 C C   . GLU B 1 62  ? 0.311   -10.323 -66.886  1.00 17.52 ? 58  GLU B C   1 
ATOM   1839 O O   . GLU B 1 62  ? 0.882   -9.471  -67.567  1.00 17.71 ? 58  GLU B O   1 
ATOM   1840 C CB  . GLU B 1 62  ? -1.616  -9.339  -65.656  1.00 18.75 ? 58  GLU B CB  1 
ATOM   1841 C CG  . GLU B 1 62  ? -2.294  -9.067  -64.317  1.00 19.42 ? 58  GLU B CG  1 
ATOM   1842 C CD  . GLU B 1 62  ? -3.664  -8.413  -64.417  1.00 24.16 ? 58  GLU B CD  1 
ATOM   1843 O OE1 . GLU B 1 62  ? -3.878  -7.574  -65.309  1.00 22.93 ? 58  GLU B OE1 1 
ATOM   1844 O OE2 . GLU B 1 62  ? -4.530  -8.726  -63.570  1.00 29.48 ? 58  GLU B OE2 1 
ATOM   1845 N N   . ARG B 1 63  ? 0.116   -11.565 -67.291  1.00 16.52 ? 59  ARG B N   1 
ATOM   1846 C CA  . ARG B 1 63  ? 0.418   -11.984 -68.651  1.00 16.92 ? 59  ARG B CA  1 
ATOM   1847 C C   . ARG B 1 63  ? -0.811  -11.725 -69.522  1.00 18.33 ? 59  ARG B C   1 
ATOM   1848 O O   . ARG B 1 63  ? -1.910  -12.185 -69.200  1.00 20.22 ? 59  ARG B O   1 
ATOM   1849 C CB  . ARG B 1 63  ? 0.765   -13.473 -68.657  1.00 18.49 ? 59  ARG B CB  1 
ATOM   1850 C CG  . ARG B 1 63  ? 1.131   -14.024 -70.029  1.00 19.27 ? 59  ARG B CG  1 
ATOM   1851 C CD  . ARG B 1 63  ? 1.900   -15.354 -69.941  1.00 20.95 ? 59  ARG B CD  1 
ATOM   1852 N NE  . ARG B 1 63  ? 3.259   -15.224 -69.391  1.00 20.18 ? 59  ARG B NE  1 
ATOM   1853 C CZ  . ARG B 1 63  ? 4.306   -14.735 -70.061  1.00 20.34 ? 59  ARG B CZ  1 
ATOM   1854 N NH1 . ARG B 1 63  ? 4.159   -14.298 -71.306  1.00 17.40 ? 59  ARG B NH1 1 
ATOM   1855 N NH2 . ARG B 1 63  ? 5.496   -14.671 -69.476  1.00 20.23 ? 59  ARG B NH2 1 
ATOM   1856 N N   . LYS B 1 64  ? -0.623  -10.980 -70.619  1.00 15.79 ? 60  LYS B N   1 
ATOM   1857 C CA  . LYS B 1 64  ? -1.721  -10.492 -71.450  1.00 15.85 ? 60  LYS B CA  1 
ATOM   1858 C C   . LYS B 1 64  ? -1.416  -10.745 -72.921  1.00 15.23 ? 60  LYS B C   1 
ATOM   1859 O O   . LYS B 1 64  ? -0.248  -10.774 -73.326  1.00 15.39 ? 60  LYS B O   1 
ATOM   1860 C CB  . LYS B 1 64  ? -1.931  -8.977  -71.230  1.00 16.36 ? 60  LYS B CB  1 
ATOM   1861 C CG  . LYS B 1 64  ? -2.471  -8.616  -69.839  1.00 18.38 ? 60  LYS B CG  1 
ATOM   1862 C CD  . LYS B 1 64  ? -3.879  -9.150  -69.651  1.00 22.22 ? 60  LYS B CD  1 
ATOM   1863 C CE  . LYS B 1 64  ? -4.604  -8.428  -68.526  1.00 26.00 ? 60  LYS B CE  1 
ATOM   1864 N NZ  . LYS B 1 64  ? -6.045  -8.842  -68.523  1.00 29.87 ? 60  LYS B NZ  1 
ATOM   1865 N N   . ASN B 1 65  ? -2.466  -10.858 -73.732  1.00 15.95 ? 61  ASN B N   1 
ATOM   1866 C CA  . ASN B 1 65  ? -2.278  -11.106 -75.157  1.00 15.93 ? 61  ASN B CA  1 
ATOM   1867 C C   . ASN B 1 65  ? -1.622  -9.912  -75.834  1.00 17.02 ? 61  ASN B C   1 
ATOM   1868 O O   . ASN B 1 65  ? -1.899  -8.756  -75.499  1.00 16.92 ? 61  ASN B O   1 
ATOM   1869 C CB  . ASN B 1 65  ? -3.624  -11.296 -75.847  1.00 18.71 ? 61  ASN B CB  1 
ATOM   1870 C CG  . ASN B 1 65  ? -4.324  -12.559 -75.433  1.00 20.51 ? 61  ASN B CG  1 
ATOM   1871 O OD1 . ASN B 1 65  ? -3.697  -13.554 -75.073  1.00 23.63 ? 61  ASN B OD1 1 
ATOM   1872 N ND2 . ASN B 1 65  ? -5.649  -12.542 -75.513  1.00 24.34 ? 61  ASN B ND2 1 
ATOM   1873 N N   . ILE B 1 66  ? -0.751  -10.202 -76.800  1.00 15.75 ? 62  ILE B N   1 
ATOM   1874 C CA  . ILE B 1 66  ? -0.241  -9.203  -77.736  1.00 14.95 ? 62  ILE B CA  1 
ATOM   1875 C C   . ILE B 1 66  ? -1.193  -9.180  -78.925  1.00 15.80 ? 62  ILE B C   1 
ATOM   1876 O O   . ILE B 1 66  ? -1.430  -10.216 -79.562  1.00 18.03 ? 62  ILE B O   1 
ATOM   1877 C CB  . ILE B 1 66  ? 1.179   -9.549  -78.202  1.00 14.44 ? 62  ILE B CB  1 
ATOM   1878 C CG1 . ILE B 1 66  ? 2.158   -9.628  -77.022  1.00 16.64 ? 62  ILE B CG1 1 
ATOM   1879 C CG2 . ILE B 1 66  ? 1.646   -8.537  -79.226  1.00 14.07 ? 62  ILE B CG2 1 
ATOM   1880 C CD1 . ILE B 1 66  ? 3.505   -10.233 -77.411  1.00 18.15 ? 62  ILE B CD1 1 
ATOM   1881 N N   . ASN B 1 67  ? -1.774  -8.020  -79.221  1.00 15.15 ? 63  ASN B N   1 
ATOM   1882 C CA  . ASN B 1 67  ? -2.763  -7.940  -80.292  1.00 16.89 ? 63  ASN B CA  1 
ATOM   1883 C C   . ASN B 1 67  ? -2.145  -7.549  -81.631  1.00 15.06 ? 63  ASN B C   1 
ATOM   1884 O O   . ASN B 1 67  ? -2.600  -8.005  -82.689  1.00 17.44 ? 63  ASN B O   1 
ATOM   1885 C CB  . ASN B 1 67  ? -3.860  -6.927  -79.919  1.00 17.66 ? 63  ASN B CB  1 
ATOM   1886 C CG  . ASN B 1 67  ? -4.710  -7.377  -78.743  1.00 21.23 ? 63  ASN B CG  1 
ATOM   1887 O OD1 . ASN B 1 67  ? -4.894  -8.572  -78.513  1.00 23.04 ? 63  ASN B OD1 1 
ATOM   1888 N ND2 . ASN B 1 67  ? -5.222  -6.410  -77.985  1.00 20.15 ? 63  ASN B ND2 1 
ATOM   1889 N N   . TYR B 1 68  ? -1.154  -6.664  -81.596  1.00 15.14 ? 64  TYR B N   1 
ATOM   1890 C CA  . TYR B 1 68  ? -0.526  -6.141  -82.800  1.00 14.91 ? 64  TYR B CA  1 
ATOM   1891 C C   . TYR B 1 68  ? 0.936   -5.873  -82.508  1.00 14.69 ? 64  TYR B C   1 
ATOM   1892 O O   . TYR B 1 68  ? 1.334   -5.646  -81.360  1.00 14.22 ? 64  TYR B O   1 
ATOM   1893 C CB  . TYR B 1 68  ? -1.140  -4.795  -83.230  1.00 16.56 ? 64  TYR B CB  1 
ATOM   1894 C CG  . TYR B 1 68  ? -2.605  -4.853  -83.566  1.00 16.14 ? 64  TYR B CG  1 
ATOM   1895 C CD1 . TYR B 1 68  ? -3.045  -5.315  -84.804  1.00 16.51 ? 64  TYR B CD1 1 
ATOM   1896 C CD2 . TYR B 1 68  ? -3.567  -4.448  -82.640  1.00 18.80 ? 64  TYR B CD2 1 
ATOM   1897 C CE1 . TYR B 1 68  ? -4.389  -5.384  -85.104  1.00 22.13 ? 64  TYR B CE1 1 
ATOM   1898 C CE2 . TYR B 1 68  ? -4.922  -4.505  -82.938  1.00 19.60 ? 64  TYR B CE2 1 
ATOM   1899 C CZ  . TYR B 1 68  ? -5.327  -4.983  -84.173  1.00 20.04 ? 64  TYR B CZ  1 
ATOM   1900 O OH  . TYR B 1 68  ? -6.665  -5.058  -84.519  1.00 24.44 ? 64  TYR B OH  1 
ATOM   1901 N N   . ILE B 1 69  ? 1.732   -5.860  -83.572  1.00 15.17 ? 65  ILE B N   1 
ATOM   1902 C CA  . ILE B 1 69  ? 3.098   -5.367  -83.505  1.00 13.41 ? 65  ILE B CA  1 
ATOM   1903 C C   . ILE B 1 69  ? 3.310   -4.364  -84.624  1.00 15.13 ? 65  ILE B C   1 
ATOM   1904 O O   . ILE B 1 69  ? 2.828   -4.566  -85.743  1.00 16.42 ? 65  ILE B O   1 
ATOM   1905 C CB  . ILE B 1 69  ? 4.146   -6.496  -83.515  1.00 15.50 ? 65  ILE B CB  1 
ATOM   1906 C CG1 . ILE B 1 69  ? 5.531   -5.862  -83.366  1.00 21.17 ? 65  ILE B CG1 1 
ATOM   1907 C CG2 . ILE B 1 69  ? 4.038   -7.366  -84.771  1.00 16.98 ? 65  ILE B CG2 1 
ATOM   1908 C CD1 . ILE B 1 69  ? 6.595   -6.790  -82.939  1.00 27.06 ? 65  ILE B CD1 1 
ATOM   1909 N N   . MET B 1 70  ? 3.997   -3.263  -84.322  1.00 16.74 ? 66  MET B N   1 
ATOM   1910 C CA  . MET B 1 70  ? 4.148   -2.131  -85.229  1.00 16.74 ? 66  MET B CA  1 
ATOM   1911 C C   . MET B 1 70  ? 5.614   -1.822  -85.475  1.00 16.57 ? 66  MET B C   1 
ATOM   1912 O O   . MET B 1 70  ? 6.450   -1.977  -84.584  1.00 16.29 ? 66  MET B O   1 
ATOM   1913 C CB  . MET B 1 70  ? 3.538   -0.869  -84.637  1.00 27.78 ? 66  MET B CB  1 
ATOM   1914 C CG  . MET B 1 70  ? 2.068   -0.801  -84.776  1.00 43.25 ? 66  MET B CG  1 
ATOM   1915 S SD  . MET B 1 70  ? 1.334   -0.269  -83.252  1.00 47.84 ? 66  MET B SD  1 
ATOM   1916 C CE  . MET B 1 70  ? 1.554   -1.787  -82.344  1.00 27.55 ? 66  MET B CE  1 
ATOM   1917 N N   . LYS B 1 71  ? 5.895   -1.320  -86.674  1.00 16.63 ? 67  LYS B N   1 
ATOM   1918 C CA  . LYS B 1 71  ? 7.212   -0.855  -87.076  1.00 15.96 ? 67  LYS B CA  1 
ATOM   1919 C C   . LYS B 1 71  ? 7.028   0.442   -87.853  1.00 16.60 ? 67  LYS B C   1 
ATOM   1920 O O   . LYS B 1 71  ? 6.160   0.529   -88.727  1.00 18.00 ? 67  LYS B O   1 
ATOM   1921 C CB  . LYS B 1 71  ? 7.901   -1.914  -87.936  1.00 17.66 ? 67  LYS B CB  1 
ATOM   1922 C CG  . LYS B 1 71  ? 9.260   -1.475  -88.473  1.00 18.60 ? 67  LYS B CG  1 
ATOM   1923 C CD  . LYS B 1 71  ? 9.814   -2.510  -89.428  1.00 20.04 ? 67  LYS B CD  1 
ATOM   1924 C CE  . LYS B 1 71  ? 11.161  -2.096  -89.991  1.00 20.84 ? 67  LYS B CE  1 
ATOM   1925 N NZ  . LYS B 1 71  ? 11.630  -3.124  -90.969  1.00 24.98 ? 67  LYS B NZ  1 
ATOM   1926 N N   . HIS B 1 72  ? 7.821   1.456   -87.506  1.00 17.84 ? 68  HIS B N   1 
ATOM   1927 C CA  . HIS B 1 72  ? 7.843   2.717   -88.241  1.00 19.45 ? 68  HIS B CA  1 
ATOM   1928 C C   . HIS B 1 72  ? 9.269   3.217   -88.347  1.00 21.28 ? 68  HIS B C   1 
ATOM   1929 O O   . HIS B 1 72  ? 10.047  3.103   -87.405  1.00 23.82 ? 68  HIS B O   1 
ATOM   1930 C CB  . HIS B 1 72  ? 7.090   3.863   -87.549  1.00 28.04 ? 68  HIS B CB  1 
ATOM   1931 C CG  . HIS B 1 72  ? 5.981   3.429   -86.654  1.00 26.17 ? 68  HIS B CG  1 
ATOM   1932 N ND1 . HIS B 1 72  ? 4.721   3.128   -87.124  1.00 31.14 ? 68  HIS B ND1 1 
ATOM   1933 C CD2 . HIS B 1 72  ? 5.926   3.290   -85.308  1.00 29.70 ? 68  HIS B CD2 1 
ATOM   1934 C CE1 . HIS B 1 72  ? 3.945   2.798   -86.107  1.00 29.70 ? 68  HIS B CE1 1 
ATOM   1935 N NE2 . HIS B 1 72  ? 4.651   2.890   -84.994  1.00 29.99 ? 68  HIS B NE2 1 
ATOM   1936 N N   . THR B 1 73  ? 9.608   3.797   -89.481  1.00 21.94 ? 69  THR B N   1 
ATOM   1937 C CA  . THR B 1 73  ? 10.864  4.520   -89.604  1.00 23.22 ? 69  THR B CA  1 
ATOM   1938 C C   . THR B 1 73  ? 10.589  5.994   -89.347  1.00 26.34 ? 69  THR B C   1 
ATOM   1939 O O   . THR B 1 73  ? 9.740   6.595   -90.016  1.00 28.54 ? 69  THR B O   1 
ATOM   1940 C CB  . THR B 1 73  ? 11.478  4.311   -90.979  1.00 24.97 ? 69  THR B CB  1 
ATOM   1941 O OG1 . THR B 1 73  ? 11.612  2.907   -91.225  1.00 24.75 ? 69  THR B OG1 1 
ATOM   1942 C CG2 . THR B 1 73  ? 12.847  4.966   -91.009  1.00 24.17 ? 69  THR B CG2 1 
ATOM   1943 N N   . VAL B 1 74  ? 11.305  6.572   -88.382  1.00 26.45 ? 70  VAL B N   1 
ATOM   1944 C CA  . VAL B 1 74  ? 11.033  7.910   -87.875  1.00 26.67 ? 70  VAL B CA  1 
ATOM   1945 C C   . VAL B 1 74  ? 12.328  8.708   -87.868  1.00 24.42 ? 70  VAL B C   1 
ATOM   1946 O O   . VAL B 1 74  ? 13.424  8.152   -87.926  1.00 24.85 ? 70  VAL B O   1 
ATOM   1947 C CB  . VAL B 1 74  ? 10.418  7.873   -86.456  1.00 23.88 ? 70  VAL B CB  1 
ATOM   1948 C CG1 . VAL B 1 74  ? 9.198   6.950   -86.429  1.00 25.39 ? 70  VAL B CG1 1 
ATOM   1949 C CG2 . VAL B 1 74  ? 11.459  7.427   -85.411  1.00 23.63 ? 70  VAL B CG2 1 
ATOM   1950 N N   . LYS B 1 75  ? 12.187  10.033  -87.843  1.00 25.61 ? 71  LYS B N   1 
ATOM   1951 C CA  . LYS B 1 75  ? 13.296  10.942  -87.548  1.00 25.04 ? 71  LYS B CA  1 
ATOM   1952 C C   . LYS B 1 75  ? 12.914  11.735  -86.304  1.00 26.86 ? 71  LYS B C   1 
ATOM   1953 O O   . LYS B 1 75  ? 12.195  12.734  -86.398  1.00 28.99 ? 71  LYS B O   1 
ATOM   1954 C CB  . LYS B 1 75  ? 13.582  11.859  -88.743  1.00 27.74 ? 71  LYS B CB  1 
ATOM   1955 C CG  . LYS B 1 75  ? 13.713  11.132  -90.070  1.00 36.93 ? 71  LYS B CG  1 
ATOM   1956 C CD  . LYS B 1 75  ? 13.204  11.968  -91.240  1.00 45.68 ? 71  LYS B CD  1 
ATOM   1957 C CE  . LYS B 1 75  ? 13.720  11.425  -92.566  1.00 49.06 ? 71  LYS B CE  1 
ATOM   1958 N NZ  . LYS B 1 75  ? 14.769  12.297  -93.172  1.00 52.93 ? 71  LYS B NZ  1 
ATOM   1959 N N   . LYS B 1 76  ? 13.429  11.320  -85.149  1.00 21.16 ? 72  LYS B N   1 
ATOM   1960 C CA  . LYS B 1 76  ? 12.941  11.838  -83.878  1.00 23.71 ? 72  LYS B CA  1 
ATOM   1961 C C   . LYS B 1 76  ? 14.077  11.868  -82.871  1.00 22.41 ? 72  LYS B C   1 
ATOM   1962 O O   . LYS B 1 76  ? 15.052  11.118  -82.975  1.00 21.44 ? 72  LYS B O   1 
ATOM   1963 C CB  . LYS B 1 76  ? 11.810  10.954  -83.321  1.00 24.39 ? 72  LYS B CB  1 
ATOM   1964 C CG  . LYS B 1 76  ? 10.479  11.107  -84.046  1.00 28.11 ? 72  LYS B CG  1 
ATOM   1965 C CD  . LYS B 1 76  ? 9.357   10.400  -83.303  1.00 28.06 ? 72  LYS B CD  1 
ATOM   1966 C CE  . LYS B 1 76  ? 8.080   10.372  -84.131  1.00 32.16 ? 72  LYS B CE  1 
ATOM   1967 N NZ  . LYS B 1 76  ? 7.305   11.633  -83.988  1.00 44.39 ? 72  LYS B NZ  1 
ATOM   1968 N N   . ARG B 1 77  ? 13.929  12.753  -81.884  1.00 21.98 ? 73  ARG B N   1 
ATOM   1969 C CA  . ARG B 1 77  ? 14.830  12.777  -80.743  1.00 19.87 ? 73  ARG B CA  1 
ATOM   1970 C C   . ARG B 1 77  ? 14.633  11.512  -79.915  1.00 20.84 ? 73  ARG B C   1 
ATOM   1971 O O   . ARG B 1 77  ? 13.497  11.098  -79.642  1.00 22.70 ? 73  ARG B O   1 
ATOM   1972 C CB  . ARG B 1 77  ? 14.550  14.005  -79.871  1.00 22.44 ? 73  ARG B CB  1 
ATOM   1973 C CG  . ARG B 1 77  ? 15.563  14.229  -78.751  1.00 23.12 ? 73  ARG B CG  1 
ATOM   1974 C CD  . ARG B 1 77  ? 15.394  15.609  -78.109  1.00 26.61 ? 73  ARG B CD  1 
ATOM   1975 N NE  . ARG B 1 77  ? 15.610  16.664  -79.096  1.00 28.41 ? 73  ARG B NE  1 
ATOM   1976 C CZ  . ARG B 1 77  ? 16.806  17.076  -79.506  1.00 29.27 ? 73  ARG B CZ  1 
ATOM   1977 N NH1 . ARG B 1 77  ? 17.910  16.538  -79.003  1.00 29.57 ? 73  ARG B NH1 1 
ATOM   1978 N NH2 . ARG B 1 77  ? 16.895  18.031  -80.423  1.00 33.27 ? 73  ARG B NH2 1 
ATOM   1979 N N   . MET B 1 78  ? 15.735  10.884  -79.528  1.00 19.49 ? 74  MET B N   1 
ATOM   1980 C CA  . MET B 1 78  ? 15.685  9.635   -78.785  1.00 18.30 ? 74  MET B CA  1 
ATOM   1981 C C   . MET B 1 78  ? 16.213  9.868   -77.379  1.00 18.06 ? 74  MET B C   1 
ATOM   1982 O O   . MET B 1 78  ? 17.138  10.663  -77.182  1.00 19.85 ? 74  MET B O   1 
ATOM   1983 C CB  . MET B 1 78  ? 16.536  8.574   -79.480  1.00 19.31 ? 74  MET B CB  1 
ATOM   1984 C CG  . MET B 1 78  ? 16.153  8.341   -80.927  1.00 21.48 ? 74  MET B CG  1 
ATOM   1985 S SD  . MET B 1 78  ? 14.464  7.771   -81.150  1.00 20.94 ? 74  MET B SD  1 
ATOM   1986 C CE  . MET B 1 78  ? 14.515  6.172   -80.353  1.00 20.64 ? 74  MET B CE  1 
ATOM   1987 N N   . PHE B 1 79  ? 15.622  9.185   -76.394  1.00 16.88 ? 75  PHE B N   1 
ATOM   1988 C CA  . PHE B 1 79  ? 16.089  9.274   -75.016  1.00 18.12 ? 75  PHE B CA  1 
ATOM   1989 C C   . PHE B 1 79  ? 16.377  7.886   -74.471  1.00 18.54 ? 75  PHE B C   1 
ATOM   1990 O O   . PHE B 1 79  ? 15.617  6.938   -74.709  1.00 20.10 ? 75  PHE B O   1 
ATOM   1991 C CB  . PHE B 1 79  ? 15.063  9.951   -74.100  1.00 18.99 ? 75  PHE B CB  1 
ATOM   1992 C CG  . PHE B 1 79  ? 14.982  11.442  -74.266  1.00 20.94 ? 75  PHE B CG  1 
ATOM   1993 C CD1 . PHE B 1 79  ? 15.772  12.280  -73.499  1.00 23.92 ? 75  PHE B CD1 1 
ATOM   1994 C CD2 . PHE B 1 79  ? 14.106  12.009  -75.175  1.00 23.52 ? 75  PHE B CD2 1 
ATOM   1995 C CE1 . PHE B 1 79  ? 15.700  13.658  -73.646  1.00 26.78 ? 75  PHE B CE1 1 
ATOM   1996 C CE2 . PHE B 1 79  ? 14.033  13.389  -75.324  1.00 26.70 ? 75  PHE B CE2 1 
ATOM   1997 C CZ  . PHE B 1 79  ? 14.827  14.206  -74.560  1.00 27.09 ? 75  PHE B CZ  1 
ATOM   1998 N N   . LYS B 1 80  ? 17.455  7.778   -73.703  1.00 19.30 ? 76  LYS B N   1 
ATOM   1999 C CA  . LYS B 1 80  ? 17.780  6.559   -72.980  1.00 20.05 ? 76  LYS B CA  1 
ATOM   2000 C C   . LYS B 1 80  ? 17.369  6.726   -71.522  1.00 19.60 ? 76  LYS B C   1 
ATOM   2001 O O   . LYS B 1 80  ? 17.731  7.719   -70.878  1.00 21.20 ? 76  LYS B O   1 
ATOM   2002 C CB  . LYS B 1 80  ? 19.279  6.284   -73.065  1.00 22.55 ? 76  LYS B CB  1 
ATOM   2003 C CG  . LYS B 1 80  ? 19.736  5.039   -72.342  1.00 26.17 ? 76  LYS B CG  1 
ATOM   2004 C CD  . LYS B 1 80  ? 21.252  5.013   -72.211  1.00 33.83 ? 76  LYS B CD  1 
ATOM   2005 C CE  . LYS B 1 80  ? 21.915  4.820   -73.555  1.00 36.01 ? 76  LYS B CE  1 
ATOM   2006 N NZ  . LYS B 1 80  ? 23.382  4.603   -73.395  1.00 43.58 ? 76  LYS B NZ  1 
ATOM   2007 N N   . ILE B 1 81  ? 16.596  5.777   -71.002  1.00 17.41 ? 77  ILE B N   1 
ATOM   2008 C CA  . ILE B 1 81  ? 16.219  5.706   -69.593  1.00 17.69 ? 77  ILE B CA  1 
ATOM   2009 C C   . ILE B 1 81  ? 17.082  4.625   -68.970  1.00 16.45 ? 77  ILE B C   1 
ATOM   2010 O O   . ILE B 1 81  ? 17.022  3.466   -69.395  1.00 17.60 ? 77  ILE B O   1 
ATOM   2011 C CB  . ILE B 1 81  ? 14.734  5.322   -69.441  1.00 20.39 ? 77  ILE B CB  1 
ATOM   2012 C CG1 . ILE B 1 81  ? 13.824  6.007   -70.479  1.00 29.73 ? 77  ILE B CG1 1 
ATOM   2013 C CG2 . ILE B 1 81  ? 14.294  5.483   -67.991  1.00 22.45 ? 77  ILE B CG2 1 
ATOM   2014 C CD1 . ILE B 1 81  ? 13.959  7.485   -70.594  1.00 31.66 ? 77  ILE B CD1 1 
ATOM   2015 N N   . LYS B 1 82  ? 17.847  4.969   -67.942  1.00 17.78 ? 78  LYS B N   1 
ATOM   2016 C CA  . LYS B 1 82  ? 18.756  4.038   -67.286  1.00 19.34 ? 78  LYS B CA  1 
ATOM   2017 C C   . LYS B 1 82  ? 18.273  3.797   -65.859  1.00 17.03 ? 78  LYS B C   1 
ATOM   2018 O O   . LYS B 1 82  ? 18.006  4.754   -65.128  1.00 19.92 ? 78  LYS B O   1 
ATOM   2019 C CB  . LYS B 1 82  ? 20.164  4.629   -67.222  1.00 21.71 ? 78  LYS B CB  1 
ATOM   2020 C CG  . LYS B 1 82  ? 20.737  4.963   -68.580  1.00 23.46 ? 78  LYS B CG  1 
ATOM   2021 C CD  . LYS B 1 82  ? 22.081  5.667   -68.427  1.00 29.05 ? 78  LYS B CD  1 
ATOM   2022 C CE  . LYS B 1 82  ? 23.047  4.808   -67.628  1.00 38.40 ? 78  LYS B CE  1 
ATOM   2023 N NZ  . LYS B 1 82  ? 24.386  5.453   -67.481  1.00 39.98 ? 78  LYS B NZ  1 
ATOM   2024 N N   . ALA B 1 83  ? 18.146  2.531   -65.461  1.00 17.11 ? 79  ALA B N   1 
ATOM   2025 C CA  . ALA B 1 83  ? 17.696  2.221   -64.105  1.00 17.89 ? 79  ALA B CA  1 
ATOM   2026 C C   . ALA B 1 83  ? 18.138  0.813   -63.718  1.00 18.19 ? 79  ALA B C   1 
ATOM   2027 O O   . ALA B 1 83  ? 17.941  -0.133  -64.492  1.00 18.58 ? 79  ALA B O   1 
ATOM   2028 C CB  . ALA B 1 83  ? 16.178  2.347   -64.035  1.00 21.64 ? 79  ALA B CB  1 
ATOM   2029 N N   . GLY B 1 84  ? 18.740  0.672   -62.538  1.00 19.02 ? 80  GLY B N   1 
ATOM   2030 C CA  . GLY B 1 84  ? 19.073  -0.656  -62.046  1.00 19.85 ? 80  GLY B CA  1 
ATOM   2031 C C   . GLY B 1 84  ? 20.025  -1.442  -62.918  1.00 20.09 ? 80  GLY B C   1 
ATOM   2032 O O   . GLY B 1 84  ? 19.982  -2.678  -62.911  1.00 22.53 ? 80  GLY B O   1 
ATOM   2033 N N   . GLY B 1 85  ? 20.881  -0.760  -63.681  1.00 17.95 ? 81  GLY B N   1 
ATOM   2034 C CA  . GLY B 1 85  ? 21.791  -1.429  -64.593  1.00 18.54 ? 81  GLY B CA  1 
ATOM   2035 C C   . GLY B 1 85  ? 21.180  -1.858  -65.908  1.00 19.33 ? 81  GLY B C   1 
ATOM   2036 O O   . GLY B 1 85  ? 21.866  -2.506  -66.710  1.00 21.42 ? 81  GLY B O   1 
ATOM   2037 N N   . LYS B 1 86  ? 19.918  -1.530  -66.147  1.00 18.07 ? 82  LYS B N   1 
ATOM   2038 C CA  . LYS B 1 86  ? 19.236  -1.753  -67.408  1.00 19.29 ? 82  LYS B CA  1 
ATOM   2039 C C   . LYS B 1 86  ? 18.999  -0.414  -68.086  1.00 16.32 ? 82  LYS B C   1 
ATOM   2040 O O   . LYS B 1 86  ? 19.062  0.643   -67.456  1.00 16.92 ? 82  LYS B O   1 
ATOM   2041 C CB  . LYS B 1 86  ? 17.886  -2.435  -67.168  1.00 22.16 ? 82  LYS B CB  1 
ATOM   2042 C CG  . LYS B 1 86  ? 17.985  -3.773  -66.456  1.00 26.65 ? 82  LYS B CG  1 
ATOM   2043 C CD  . LYS B 1 86  ? 18.663  -4.813  -67.312  1.00 30.14 ? 82  LYS B CD  1 
ATOM   2044 C CE  . LYS B 1 86  ? 18.766  -6.149  -66.588  1.00 38.21 ? 82  LYS B CE  1 
ATOM   2045 N NZ  . LYS B 1 86  ? 19.184  -7.231  -67.521  1.00 46.07 ? 82  LYS B NZ  1 
ATOM   2046 N N   . GLU B 1 87  ? 18.672  -0.459  -69.373  1.00 17.64 ? 83  GLU B N   1 
ATOM   2047 C CA  . GLU B 1 87  ? 18.334  0.769   -70.071  1.00 19.48 ? 83  GLU B CA  1 
ATOM   2048 C C   . GLU B 1 87  ? 17.337  0.457   -71.169  1.00 17.81 ? 83  GLU B C   1 
ATOM   2049 O O   . GLU B 1 87  ? 17.303  -0.656  -71.691  1.00 19.58 ? 83  GLU B O   1 
ATOM   2050 C CB  . GLU B 1 87  ? 19.550  1.492   -70.654  1.00 20.92 ? 83  GLU B CB  1 
ATOM   2051 C CG  . GLU B 1 87  ? 20.297  0.691   -71.687  1.00 28.32 ? 83  GLU B CG  1 
ATOM   2052 C CD  . GLU B 1 87  ? 21.557  1.400   -72.174  1.00 32.69 ? 83  GLU B CD  1 
ATOM   2053 O OE1 . GLU B 1 87  ? 22.370  1.840   -71.331  1.00 31.71 ? 83  GLU B OE1 1 
ATOM   2054 O OE2 . GLU B 1 87  ? 21.714  1.540   -73.401  1.00 36.60 ? 83  GLU B OE2 1 
ATOM   2055 N N   . VAL B 1 88  ? 16.514  1.440   -71.502  1.00 15.92 ? 84  VAL B N   1 
ATOM   2056 C CA  . VAL B 1 88  ? 15.611  1.337   -72.642  1.00 15.67 ? 84  VAL B CA  1 
ATOM   2057 C C   . VAL B 1 88  ? 15.684  2.645   -73.428  1.00 15.41 ? 84  VAL B C   1 
ATOM   2058 O O   . VAL B 1 88  ? 15.793  3.725   -72.833  1.00 16.88 ? 84  VAL B O   1 
ATOM   2059 C CB  . VAL B 1 88  ? 14.170  0.950   -72.216  1.00 16.72 ? 84  VAL B CB  1 
ATOM   2060 C CG1 . VAL B 1 88  ? 13.520  2.045   -71.367  1.00 16.83 ? 84  VAL B CG1 1 
ATOM   2061 C CG2 . VAL B 1 88  ? 13.293  0.578   -73.439  1.00 16.42 ? 84  VAL B CG2 1 
ATOM   2062 N N   . ILE B 1 89  ? 15.677  2.548   -74.754  1.00 16.65 ? 85  ILE B N   1 
ATOM   2063 C CA  . ILE B 1 89  ? 15.770  3.718   -75.625  1.00 17.48 ? 85  ILE B CA  1 
ATOM   2064 C C   . ILE B 1 89  ? 14.428  3.918   -76.334  1.00 14.78 ? 85  ILE B C   1 
ATOM   2065 O O   . ILE B 1 89  ? 13.950  3.025   -77.047  1.00 14.84 ? 85  ILE B O   1 
ATOM   2066 C CB  . ILE B 1 89  ? 16.941  3.602   -76.615  1.00 16.97 ? 85  ILE B CB  1 
ATOM   2067 C CG1 . ILE B 1 89  ? 18.266  3.391   -75.857  1.00 18.67 ? 85  ILE B CG1 1 
ATOM   2068 C CG2 . ILE B 1 89  ? 17.022  4.844   -77.501  1.00 18.33 ? 85  ILE B CG2 1 
ATOM   2069 C CD1 . ILE B 1 89  ? 19.438  3.086   -76.752  1.00 21.27 ? 85  ILE B CD1 1 
ATOM   2070 N N   . VAL B 1 90  ? 13.815  5.088   -76.122  1.00 15.87 ? 86  VAL B N   1 
ATOM   2071 C CA  . VAL B 1 90  ? 12.479  5.407   -76.629  1.00 15.23 ? 86  VAL B CA  1 
ATOM   2072 C C   . VAL B 1 90  ? 12.507  6.731   -77.387  1.00 16.92 ? 86  VAL B C   1 
ATOM   2073 O O   . VAL B 1 90  ? 13.380  7.578   -77.182  1.00 16.57 ? 86  VAL B O   1 
ATOM   2074 C CB  . VAL B 1 90  ? 11.427  5.465   -75.498  1.00 18.30 ? 86  VAL B CB  1 
ATOM   2075 C CG1 . VAL B 1 90  ? 11.492  4.199   -74.644  1.00 22.84 ? 86  VAL B CG1 1 
ATOM   2076 C CG2 . VAL B 1 90  ? 11.631  6.705   -74.622  1.00 19.01 ? 86  VAL B CG2 1 
ATOM   2077 N N   . THR B 1 91  ? 11.514  6.936   -78.252  1.00 16.01 ? 87  THR B N   1 
ATOM   2078 C CA  . THR B 1 91  ? 11.383  8.247   -78.882  1.00 18.62 ? 87  THR B CA  1 
ATOM   2079 C C   . THR B 1 91  ? 10.909  9.269   -77.855  1.00 17.77 ? 87  THR B C   1 
ATOM   2080 O O   . THR B 1 91  ? 10.277  8.927   -76.859  1.00 17.29 ? 87  THR B O   1 
ATOM   2081 C CB  . THR B 1 91  ? 10.414  8.205   -80.067  1.00 19.45 ? 87  THR B CB  1 
ATOM   2082 O OG1 . THR B 1 91  ? 9.107   7.805   -79.611  1.00 18.99 ? 87  THR B OG1 1 
ATOM   2083 C CG2 . THR B 1 91  ? 10.897  7.210   -81.119  1.00 18.87 ? 87  THR B CG2 1 
ATOM   2084 N N   . ALA B 1 92  ? 11.188  10.547  -78.133  1.00 19.46 ? 88  ALA B N   1 
ATOM   2085 C CA  . ALA B 1 92  ? 10.861  11.599  -77.177  1.00 19.66 ? 88  ALA B CA  1 
ATOM   2086 C C   . ALA B 1 92  ? 9.367   11.674  -76.910  1.00 19.14 ? 88  ALA B C   1 
ATOM   2087 O O   . ALA B 1 92  ? 8.952   12.154  -75.845  1.00 22.42 ? 88  ALA B O   1 
ATOM   2088 C CB  . ALA B 1 92  ? 11.374  12.941  -77.702  1.00 23.00 ? 88  ALA B CB  1 
ATOM   2089 N N   . ASP B 1 93  ? 8.553   11.257  -77.876  1.00 21.48 ? 89  ASP B N   1 
ATOM   2090 C CA  . ASP B 1 93  ? 7.100   11.278  -77.776  1.00 25.79 ? 89  ASP B CA  1 
ATOM   2091 C C   . ASP B 1 93  ? 6.494   9.996   -77.209  1.00 24.26 ? 89  ASP B C   1 
ATOM   2092 O O   . ASP B 1 93  ? 5.269   9.872   -77.178  1.00 23.74 ? 89  ASP B O   1 
ATOM   2093 C CB  . ASP B 1 93  ? 6.426   11.716  -79.085  1.00 26.96 ? 89  ASP B CB  1 
ATOM   2094 C CG  . ASP B 1 93  ? 6.904   10.940  -80.305  1.00 30.79 ? 89  ASP B CG  1 
ATOM   2095 O OD1 . ASP B 1 93  ? 7.785   10.061  -80.188  1.00 25.17 ? 89  ASP B OD1 1 
ATOM   2096 O OD2 . ASP B 1 93  ? 6.371   11.216  -81.404  1.00 33.45 ? 89  ASP B OD2 1 
ATOM   2097 N N   . HIS B 1 94  ? 7.314   9.022   -76.825  1.00 18.94 ? 90  HIS B N   1 
ATOM   2098 C CA  . HIS B 1 94  ? 6.828   7.764   -76.278  1.00 19.83 ? 90  HIS B CA  1 
ATOM   2099 C C   . HIS B 1 94  ? 6.844   7.803   -74.747  1.00 19.97 ? 90  HIS B C   1 
ATOM   2100 O O   . HIS B 1 94  ? 7.770   8.338   -74.137  1.00 27.16 ? 90  HIS B O   1 
ATOM   2101 C CB  . HIS B 1 94  ? 7.682   6.589   -76.769  1.00 20.10 ? 90  HIS B CB  1 
ATOM   2102 C CG  . HIS B 1 94  ? 7.045   5.260   -76.529  1.00 19.71 ? 90  HIS B CG  1 
ATOM   2103 N ND1 . HIS B 1 94  ? 5.926   4.842   -77.219  1.00 24.79 ? 90  HIS B ND1 1 
ATOM   2104 C CD2 . HIS B 1 94  ? 7.328   4.282   -75.636  1.00 25.22 ? 90  HIS B CD2 1 
ATOM   2105 C CE1 . HIS B 1 94  ? 5.565   3.650   -76.778  1.00 30.32 ? 90  HIS B CE1 1 
ATOM   2106 N NE2 . HIS B 1 94  ? 6.392   3.291   -75.812  1.00 29.08 ? 90  HIS B NE2 1 
ATOM   2107 N N   . SER B 1 95  ? 5.818   7.227   -74.122  1.00 21.72 ? 91  SER B N   1 
ATOM   2108 C CA  . SER B 1 95  ? 5.698   7.266   -72.668  1.00 23.15 ? 91  SER B CA  1 
ATOM   2109 C C   . SER B 1 95  ? 6.398   6.088   -71.998  1.00 19.18 ? 91  SER B C   1 
ATOM   2110 O O   . SER B 1 95  ? 6.343   4.951   -72.483  1.00 20.35 ? 91  SER B O   1 
ATOM   2111 C CB  . SER B 1 95  ? 4.226   7.302   -72.258  1.00 25.42 ? 91  SER B CB  1 
ATOM   2112 O OG  . SER B 1 95  ? 3.619   8.510   -72.689  1.00 32.21 ? 91  SER B OG  1 
ATOM   2113 N N   . VAL B 1 96  ? 7.055   6.383   -70.874  1.00 20.65 ? 92  VAL B N   1 
ATOM   2114 C CA  . VAL B 1 96  ? 7.614   5.418   -69.935  1.00 18.88 ? 92  VAL B CA  1 
ATOM   2115 C C   . VAL B 1 96  ? 6.666   5.376   -68.743  1.00 17.52 ? 92  VAL B C   1 
ATOM   2116 O O   . VAL B 1 96  ? 6.019   6.376   -68.422  1.00 20.22 ? 92  VAL B O   1 
ATOM   2117 C CB  . VAL B 1 96  ? 9.017   5.908   -69.506  1.00 21.77 ? 92  VAL B CB  1 
ATOM   2118 C CG1 . VAL B 1 96  ? 9.629   5.013   -68.454  1.00 22.53 ? 92  VAL B CG1 1 
ATOM   2119 C CG2 . VAL B 1 96  ? 9.942   5.991   -70.714  1.00 25.21 ? 92  VAL B CG2 1 
ATOM   2120 N N   . MET B 1 97  ? 6.545   4.222   -68.091  1.00 14.58 ? 93  MET B N   1 
ATOM   2121 C CA  . MET B 1 97  ? 5.720   4.130   -66.889  1.00 14.50 ? 93  MET B CA  1 
ATOM   2122 C C   . MET B 1 97  ? 6.520   4.577   -65.676  1.00 15.98 ? 93  MET B C   1 
ATOM   2123 O O   . MET B 1 97  ? 7.702   4.246   -65.540  1.00 17.75 ? 93  MET B O   1 
ATOM   2124 C CB  . MET B 1 97  ? 5.206   2.702   -66.680  1.00 16.44 ? 93  MET B CB  1 
ATOM   2125 C CG  . MET B 1 97  ? 4.481   2.106   -67.902  1.00 15.53 ? 93  MET B CG  1 
ATOM   2126 S SD  . MET B 1 97  ? 3.096   3.106   -68.491  1.00 16.40 ? 93  MET B SD  1 
ATOM   2127 C CE  . MET B 1 97  ? 1.957   2.962   -67.113  1.00 16.27 ? 93  MET B CE  1 
ATOM   2128 N N   . VAL B 1 98  ? 5.873   5.324   -64.780  1.00 16.61 ? 94  VAL B N   1 
ATOM   2129 C CA  . VAL B 1 98  ? 6.495   5.692   -63.515  1.00 15.40 ? 94  VAL B CA  1 
ATOM   2130 C C   . VAL B 1 98  ? 5.457   5.542   -62.426  1.00 17.45 ? 94  VAL B C   1 
ATOM   2131 O O   . VAL B 1 98  ? 4.253   5.666   -62.670  1.00 17.81 ? 94  VAL B O   1 
ATOM   2132 C CB  . VAL B 1 98  ? 7.045   7.142   -63.475  1.00 17.71 ? 94  VAL B CB  1 
ATOM   2133 C CG1 . VAL B 1 98  ? 8.201   7.299   -64.443  1.00 18.99 ? 94  VAL B CG1 1 
ATOM   2134 C CG2 . VAL B 1 98  ? 5.955   8.176   -63.744  1.00 20.67 ? 94  VAL B CG2 1 
ATOM   2135 N N   . LYS B 1 99  ? 5.937   5.296   -61.209  1.00 16.53 ? 95  LYS B N   1 
ATOM   2136 C CA  . LYS B 1 99  ? 5.125   5.508   -60.022  1.00 17.68 ? 95  LYS B CA  1 
ATOM   2137 C C   . LYS B 1 99  ? 5.316   6.957   -59.601  1.00 19.21 ? 95  LYS B C   1 
ATOM   2138 O O   . LYS B 1 99  ? 6.455   7.393   -59.367  1.00 18.98 ? 95  LYS B O   1 
ATOM   2139 C CB  . LYS B 1 99  ? 5.498   4.553   -58.888  1.00 20.72 ? 95  LYS B CB  1 
ATOM   2140 C CG  . LYS B 1 99  ? 4.604   4.748   -57.656  1.00 24.48 ? 95  LYS B CG  1 
ATOM   2141 C CD  . LYS B 1 99  ? 4.765   3.634   -56.654  1.00 34.65 ? 95  LYS B CD  1 
ATOM   2142 C CE  . LYS B 1 99  ? 5.999   3.857   -55.791  1.00 39.23 ? 95  LYS B CE  1 
ATOM   2143 N NZ  . LYS B 1 99  ? 5.889   3.263   -54.415  1.00 38.97 ? 95  LYS B NZ  1 
ATOM   2144 N N   . ARG B 1 100 ? 4.215   7.708   -59.576  1.00 17.97 ? 96  ARG B N   1 
ATOM   2145 C CA  . ARG B 1 100 ? 4.204   9.103   -59.144  1.00 17.20 ? 96  ARG B CA  1 
ATOM   2146 C C   . ARG B 1 100 ? 3.023   9.313   -58.205  1.00 18.14 ? 96  ARG B C   1 
ATOM   2147 O O   . ARG B 1 100 ? 1.877   8.998   -58.554  1.00 18.33 ? 96  ARG B O   1 
ATOM   2148 C CB  . ARG B 1 100 ? 4.077   10.041  -60.346  1.00 20.28 ? 96  ARG B CB  1 
ATOM   2149 C CG  . ARG B 1 100 ? 3.854   11.492  -59.946  1.00 20.25 ? 96  ARG B CG  1 
ATOM   2150 C CD  . ARG B 1 100 ? 3.733   12.429  -61.136  1.00 22.01 ? 96  ARG B CD  1 
ATOM   2151 N NE  . ARG B 1 100 ? 4.919   12.432  -61.992  1.00 21.89 ? 96  ARG B NE  1 
ATOM   2152 C CZ  . ARG B 1 100 ? 4.998   13.079  -63.150  1.00 24.88 ? 96  ARG B CZ  1 
ATOM   2153 N NH1 . ARG B 1 100 ? 3.953   13.762  -63.599  1.00 26.25 ? 96  ARG B NH1 1 
ATOM   2154 N NH2 . ARG B 1 100 ? 6.118   13.035  -63.860  1.00 25.78 ? 96  ARG B NH2 1 
ATOM   2155 N N   . ASP B 1 101 ? 3.292   9.811   -56.995  1.00 18.28 ? 97  ASP B N   1 
ATOM   2156 C CA  . ASP B 1 101 ? 2.229   10.136  -56.035  1.00 19.21 ? 97  ASP B CA  1 
ATOM   2157 C C   . ASP B 1 101 ? 1.322   8.933   -55.779  1.00 18.79 ? 97  ASP B C   1 
ATOM   2158 O O   . ASP B 1 101 ? 0.105   9.069   -55.628  1.00 20.88 ? 97  ASP B O   1 
ATOM   2159 C CB  . ASP B 1 101 ? 1.409   11.344  -56.495  1.00 22.75 ? 97  ASP B CB  1 
ATOM   2160 C CG  . ASP B 1 101 ? 2.239   12.604  -56.625  1.00 32.61 ? 97  ASP B CG  1 
ATOM   2161 O OD1 . ASP B 1 101 ? 3.283   12.708  -55.950  1.00 32.18 ? 97  ASP B OD1 1 
ATOM   2162 O OD2 . ASP B 1 101 ? 1.829   13.497  -57.401  1.00 34.63 ? 97  ASP B OD2 1 
ATOM   2163 N N   . GLY B 1 102 ? 1.937   7.756   -55.677  1.00 21.28 ? 98  GLY B N   1 
ATOM   2164 C CA  . GLY B 1 102 ? 1.226   6.539   -55.351  1.00 25.38 ? 98  GLY B CA  1 
ATOM   2165 C C   . GLY B 1 102 ? 0.531   5.835   -56.501  1.00 22.18 ? 98  GLY B C   1 
ATOM   2166 O O   . GLY B 1 102 ? -0.146  4.825   -56.258  1.00 25.06 ? 98  GLY B O   1 
ATOM   2167 N N   . LYS B 1 103 ? 0.641   6.334   -57.734  1.00 19.54 ? 99  LYS B N   1 
ATOM   2168 C CA  . LYS B 1 103 ? -0.051  5.750   -58.879  1.00 19.52 ? 99  LYS B CA  1 
ATOM   2169 C C   . LYS B 1 103 ? 0.949   5.444   -59.985  1.00 18.33 ? 99  LYS B C   1 
ATOM   2170 O O   . LYS B 1 103 ? 1.922   6.172   -60.176  1.00 19.07 ? 99  LYS B O   1 
ATOM   2171 C CB  . LYS B 1 103 ? -1.126  6.702   -59.443  1.00 20.91 ? 99  LYS B CB  1 
ATOM   2172 C CG  . LYS B 1 103 ? -2.243  7.068   -58.446  1.00 26.09 ? 99  LYS B CG  1 
ATOM   2173 C CD  . LYS B 1 103 ? -3.108  5.841   -58.156  1.00 29.43 ? 99  LYS B CD  1 
ATOM   2174 C CE  . LYS B 1 103 ? -4.351  6.156   -57.337  1.00 39.33 ? 99  LYS B CE  1 
ATOM   2175 N NZ  . LYS B 1 103 ? -4.217  5.938   -55.862  1.00 39.51 ? 99  LYS B NZ  1 
ATOM   2176 N N   . ILE B 1 104 ? 0.681   4.384   -60.743  1.00 17.76 ? 100 ILE B N   1 
ATOM   2177 C CA  . ILE B 1 104 ? 1.499   4.038   -61.901  1.00 18.84 ? 100 ILE B CA  1 
ATOM   2178 C C   . ILE B 1 104 ? 0.862   4.690   -63.121  1.00 20.00 ? 100 ILE B C   1 
ATOM   2179 O O   . ILE B 1 104 ? -0.302  4.425   -63.438  1.00 20.04 ? 100 ILE B O   1 
ATOM   2180 C CB  . ILE B 1 104 ? 1.607   2.515   -62.067  1.00 20.83 ? 100 ILE B CB  1 
ATOM   2181 C CG1 . ILE B 1 104 ? 2.357   1.912   -60.875  1.00 26.18 ? 100 ILE B CG1 1 
ATOM   2182 C CG2 . ILE B 1 104 ? 2.336   2.180   -63.358  1.00 23.39 ? 100 ILE B CG2 1 
ATOM   2183 C CD1 . ILE B 1 104 ? 2.349   0.398   -60.851  1.00 29.68 ? 100 ILE B CD1 1 
ATOM   2184 N N   . ILE B 1 105 ? 1.609   5.587   -63.768  1.00 17.80 ? 101 ILE B N   1 
ATOM   2185 C CA  . ILE B 1 105 ? 1.122   6.426   -64.859  1.00 18.82 ? 101 ILE B CA  1 
ATOM   2186 C C   . ILE B 1 105 ? 2.144   6.424   -65.997  1.00 16.86 ? 101 ILE B C   1 
ATOM   2187 O O   . ILE B 1 105 ? 3.283   5.999   -65.841  1.00 17.44 ? 101 ILE B O   1 
ATOM   2188 C CB  . ILE B 1 105 ? 0.835   7.873   -64.388  1.00 18.72 ? 101 ILE B CB  1 
ATOM   2189 C CG1 . ILE B 1 105 ? 2.106   8.539   -63.832  1.00 19.51 ? 101 ILE B CG1 1 
ATOM   2190 C CG2 . ILE B 1 105 ? -0.287  7.884   -63.343  1.00 21.58 ? 101 ILE B CG2 1 
ATOM   2191 C CD1 . ILE B 1 105 ? 2.000   10.050  -63.709  1.00 20.80 ? 101 ILE B CD1 1 
ATOM   2192 N N   . ASP B 1 106 ? 1.720   6.908   -67.158  1.00 19.51 ? 102 ASP B N   1 
ATOM   2193 C CA  . ASP B 1 106 ? 2.600   7.041   -68.313  1.00 18.07 ? 102 ASP B CA  1 
ATOM   2194 C C   . ASP B 1 106 ? 2.996   8.502   -68.504  1.00 19.88 ? 102 ASP B C   1 
ATOM   2195 O O   . ASP B 1 106 ? 2.140   9.391   -68.458  1.00 24.04 ? 102 ASP B O   1 
ATOM   2196 C CB  . ASP B 1 106 ? 1.913   6.485   -69.567  1.00 21.75 ? 102 ASP B CB  1 
ATOM   2197 C CG  . ASP B 1 106 ? 0.596   7.170   -69.879  1.00 33.13 ? 102 ASP B CG  1 
ATOM   2198 O OD1 . ASP B 1 106 ? -0.436  6.803   -69.272  1.00 32.18 ? 102 ASP B OD1 1 
ATOM   2199 O OD2 . ASP B 1 106 ? 0.585   8.079   -70.734  1.00 35.91 ? 102 ASP B OD2 1 
ATOM   2200 N N   . VAL B 1 107 ? 4.295   8.747   -68.706  1.00 18.43 ? 103 VAL B N   1 
ATOM   2201 C CA  . VAL B 1 107 ? 4.835   10.092  -68.901  1.00 21.47 ? 103 VAL B CA  1 
ATOM   2202 C C   . VAL B 1 107 ? 5.918   10.070  -69.974  1.00 20.51 ? 103 VAL B C   1 
ATOM   2203 O O   . VAL B 1 107 ? 6.635   9.081   -70.139  1.00 21.25 ? 103 VAL B O   1 
ATOM   2204 C CB  . VAL B 1 107 ? 5.424   10.687  -67.597  1.00 22.53 ? 103 VAL B CB  1 
ATOM   2205 C CG1 . VAL B 1 107 ? 4.347   10.849  -66.504  1.00 25.23 ? 103 VAL B CG1 1 
ATOM   2206 C CG2 . VAL B 1 107 ? 6.571   9.834   -67.105  1.00 26.45 ? 103 VAL B CG2 1 
ATOM   2207 N N   . LYS B 1 108 ? 6.047   11.181  -70.699  1.00 19.45 ? 104 LYS B N   1 
ATOM   2208 C CA  . LYS B 1 108 ? 7.132   11.308  -71.671  1.00 20.67 ? 104 LYS B CA  1 
ATOM   2209 C C   . LYS B 1 108 ? 8.474   11.483  -70.950  1.00 20.58 ? 104 LYS B C   1 
ATOM   2210 O O   . LYS B 1 108 ? 8.516   11.997  -69.831  1.00 20.21 ? 104 LYS B O   1 
ATOM   2211 C CB  . LYS B 1 108 ? 6.887   12.507  -72.582  1.00 24.42 ? 104 LYS B CB  1 
ATOM   2212 C CG  . LYS B 1 108 ? 5.553   12.508  -73.309  1.00 28.47 ? 104 LYS B CG  1 
ATOM   2213 C CD  . LYS B 1 108 ? 5.354   11.262  -74.154  1.00 31.35 ? 104 LYS B CD  1 
ATOM   2214 C CE  . LYS B 1 108 ? 3.910   11.167  -74.629  1.00 31.30 ? 104 LYS B CE  1 
ATOM   2215 N NZ  . LYS B 1 108 ? 3.584   9.846   -75.257  1.00 34.12 ? 104 LYS B NZ  1 
ATOM   2216 N N   . PRO B 1 109 ? 9.596   11.114  -71.590  1.00 18.12 ? 105 PRO B N   1 
ATOM   2217 C CA  . PRO B 1 109 ? 10.895  11.229  -70.895  1.00 20.80 ? 105 PRO B CA  1 
ATOM   2218 C C   . PRO B 1 109 ? 11.229  12.625  -70.390  1.00 23.61 ? 105 PRO B C   1 
ATOM   2219 O O   . PRO B 1 109 ? 11.781  12.740  -69.290  1.00 25.04 ? 105 PRO B O   1 
ATOM   2220 C CB  . PRO B 1 109 ? 11.909  10.790  -71.966  1.00 20.78 ? 105 PRO B CB  1 
ATOM   2221 C CG  . PRO B 1 109 ? 11.142  9.927   -72.864  1.00 21.46 ? 105 PRO B CG  1 
ATOM   2222 C CD  . PRO B 1 109 ? 9.723   10.428  -72.890  1.00 19.86 ? 105 PRO B CD  1 
ATOM   2223 N N   . THR B 1 110 ? 10.804  13.685  -71.080  1.00 24.61 ? 106 THR B N   1 
ATOM   2224 C CA  . THR B 1 110 ? 11.108  15.033  -70.608  1.00 28.48 ? 106 THR B CA  1 
ATOM   2225 C C   . THR B 1 110 ? 10.140  15.492  -69.533  1.00 27.67 ? 106 THR B C   1 
ATOM   2226 O O   . THR B 1 110 ? 10.314  16.592  -68.994  1.00 31.43 ? 106 THR B O   1 
ATOM   2227 C CB  . THR B 1 110 ? 11.105  16.053  -71.750  1.00 29.64 ? 106 THR B CB  1 
ATOM   2228 O OG1 . THR B 1 110 ? 9.913   15.906  -72.533  1.00 32.70 ? 106 THR B OG1 1 
ATOM   2229 C CG2 . THR B 1 110 ? 12.341  15.880  -72.620  1.00 30.89 ? 106 THR B CG2 1 
ATOM   2230 N N   . GLU B 1 111 ? 9.148   14.670  -69.190  1.00 23.22 ? 107 GLU B N   1 
ATOM   2231 C CA  . GLU B 1 111 ? 8.208   14.995  -68.132  1.00 22.65 ? 107 GLU B CA  1 
ATOM   2232 C C   . GLU B 1 111 ? 8.495   14.185  -66.880  1.00 26.44 ? 107 GLU B C   1 
ATOM   2233 O O   . GLU B 1 111 ? 7.810   14.374  -65.869  1.00 26.81 ? 107 GLU B O   1 
ATOM   2234 C CB  . GLU B 1 111 ? 6.773   14.670  -68.579  1.00 27.29 ? 107 GLU B CB  1 
ATOM   2235 C CG  . GLU B 1 111 ? 6.207   15.480  -69.737  1.00 31.05 ? 107 GLU B CG  1 
ATOM   2236 C CD  . GLU B 1 111 ? 4.947   14.853  -70.340  1.00 38.27 ? 107 GLU B CD  1 
ATOM   2237 O OE1 . GLU B 1 111 ? 4.600   13.701  -69.989  1.00 36.90 ? 107 GLU B OE1 1 
ATOM   2238 O OE2 . GLU B 1 111 ? 4.279   15.532  -71.151  1.00 43.17 ? 107 GLU B OE2 1 
ATOM   2239 N N   . MET B 1 112 ? 9.553   13.377  -66.873  1.00 22.74 ? 108 MET B N   1 
ATOM   2240 C CA  . MET B 1 112 ? 9.862   12.578  -65.698  1.00 21.12 ? 108 MET B CA  1 
ATOM   2241 C C   . MET B 1 112 ? 10.553  13.462  -64.666  1.00 26.56 ? 108 MET B C   1 
ATOM   2242 O O   . MET B 1 112 ? 11.385  14.306  -65.009  1.00 29.16 ? 108 MET B O   1 
ATOM   2243 C CB  . MET B 1 112 ? 10.774  11.403  -66.088  1.00 23.12 ? 108 MET B CB  1 
ATOM   2244 C CG  . MET B 1 112 ? 10.168  10.381  -67.078  1.00 20.17 ? 108 MET B CG  1 
ATOM   2245 S SD  . MET B 1 112 ? 11.354  9.166   -67.686  1.00 24.26 ? 108 MET B SD  1 
ATOM   2246 C CE  . MET B 1 112 ? 11.289  7.958   -66.348  1.00 23.06 ? 108 MET B CE  1 
ATOM   2247 N N   . LYS B 1 113 ? 10.213  13.257  -63.398  1.00 26.02 ? 109 LYS B N   1 
ATOM   2248 C CA  . LYS B 1 113 ? 10.793  14.010  -62.298  1.00 27.28 ? 109 LYS B CA  1 
ATOM   2249 C C   . LYS B 1 113 ? 11.717  13.102  -61.501  1.00 28.10 ? 109 LYS B C   1 
ATOM   2250 O O   . LYS B 1 113 ? 11.527  11.886  -61.462  1.00 26.40 ? 109 LYS B O   1 
ATOM   2251 C CB  . LYS B 1 113 ? 9.693   14.547  -61.378  1.00 31.61 ? 109 LYS B CB  1 
ATOM   2252 C CG  . LYS B 1 113 ? 8.653   15.389  -62.101  1.00 34.55 ? 109 LYS B CG  1 
ATOM   2253 C CD  . LYS B 1 113 ? 7.719   16.076  -61.126  1.00 39.12 ? 109 LYS B CD  1 
ATOM   2254 C CE  . LYS B 1 113 ? 6.452   15.281  -60.887  1.00 37.49 ? 109 LYS B CE  1 
ATOM   2255 N NZ  . LYS B 1 113 ? 5.613   15.869  -59.800  1.00 46.89 ? 109 LYS B NZ  1 
ATOM   2256 N N   . GLN B 1 114 ? 12.686  13.704  -60.803  1.00 27.17 ? 110 GLN B N   1 
ATOM   2257 C CA  . GLN B 1 114 ? 13.632  12.885  -60.051  1.00 30.67 ? 110 GLN B CA  1 
ATOM   2258 C C   . GLN B 1 114 ? 12.937  12.081  -58.960  1.00 31.22 ? 110 GLN B C   1 
ATOM   2259 O O   . GLN B 1 114 ? 13.392  10.984  -58.613  1.00 33.44 ? 110 GLN B O   1 
ATOM   2260 C CB  . GLN B 1 114 ? 14.725  13.769  -59.440  1.00 42.51 ? 110 GLN B CB  1 
ATOM   2261 C CG  . GLN B 1 114 ? 15.812  13.020  -58.656  1.00 55.12 ? 110 GLN B CG  1 
ATOM   2262 C CD  . GLN B 1 114 ? 15.447  12.755  -57.195  1.00 67.40 ? 110 GLN B CD  1 
ATOM   2263 O OE1 . GLN B 1 114 ? 14.596  13.436  -56.620  1.00 71.67 ? 110 GLN B OE1 1 
ATOM   2264 N NE2 . GLN B 1 114 ? 16.097  11.761  -56.591  1.00 70.52 ? 110 GLN B NE2 1 
ATOM   2265 N N   . THR B 1 115 ? 11.805  12.569  -58.455  1.00 25.11 ? 111 THR B N   1 
ATOM   2266 C CA  . THR B 1 115 ? 11.090  11.816  -57.434  1.00 25.98 ? 111 THR B CA  1 
ATOM   2267 C C   . THR B 1 115 ? 10.209  10.723  -58.024  1.00 23.26 ? 111 THR B C   1 
ATOM   2268 O O   . THR B 1 115 ? 9.697   9.882   -57.278  1.00 25.68 ? 111 THR B O   1 
ATOM   2269 C CB  . THR B 1 115 ? 10.219  12.759  -56.598  1.00 27.45 ? 111 THR B CB  1 
ATOM   2270 O OG1 . THR B 1 115 ? 9.413   13.556  -57.471  1.00 27.53 ? 111 THR B OG1 1 
ATOM   2271 C CG2 . THR B 1 115 ? 11.092  13.677  -55.757  1.00 30.33 ? 111 THR B CG2 1 
ATOM   2272 N N   . ASP B 1 116 ? 10.030  10.695  -59.339  1.00 21.76 ? 112 ASP B N   1 
ATOM   2273 C CA  . ASP B 1 116 ? 9.346   9.575   -59.951  1.00 22.72 ? 112 ASP B CA  1 
ATOM   2274 C C   . ASP B 1 116 ? 10.201  8.323   -59.786  1.00 22.31 ? 112 ASP B C   1 
ATOM   2275 O O   . ASP B 1 116 ? 11.416  8.394   -59.559  1.00 23.79 ? 112 ASP B O   1 
ATOM   2276 C CB  . ASP B 1 116 ? 9.176   9.827   -61.447  1.00 22.68 ? 112 ASP B CB  1 
ATOM   2277 C CG  . ASP B 1 116 ? 8.132   10.892  -61.767  1.00 21.59 ? 112 ASP B CG  1 
ATOM   2278 O OD1 . ASP B 1 116 ? 7.276   11.198  -60.919  1.00 24.17 ? 112 ASP B OD1 1 
ATOM   2279 O OD2 . ASP B 1 116 ? 8.138   11.402  -62.910  1.00 23.28 ? 112 ASP B OD2 1 
ATOM   2280 N N   . ARG B 1 117 ? 9.561   7.162   -59.900  1.00 20.09 ? 113 ARG B N   1 
ATOM   2281 C CA  . ARG B 1 117 ? 10.295  5.901   -59.859  1.00 20.85 ? 113 ARG B CA  1 
ATOM   2282 C C   . ARG B 1 117 ? 9.903   5.058   -61.062  1.00 20.85 ? 113 ARG B C   1 
ATOM   2283 O O   . ARG B 1 117 ? 8.717   4.891   -61.352  1.00 19.87 ? 113 ARG B O   1 
ATOM   2284 C CB  . ARG B 1 117 ? 10.034  5.142   -58.539  1.00 20.28 ? 113 ARG B CB  1 
ATOM   2285 C CG  . ARG B 1 117 ? 10.543  5.846   -57.262  1.00 22.31 ? 113 ARG B CG  1 
ATOM   2286 C CD  . ARG B 1 117 ? 12.044  5.686   -57.149  1.00 22.82 ? 113 ARG B CD  1 
ATOM   2287 N NE  . ARG B 1 117 ? 12.605  6.296   -55.943  1.00 21.82 ? 113 ARG B NE  1 
ATOM   2288 C CZ  . ARG B 1 117 ? 13.040  7.546   -55.880  1.00 25.81 ? 113 ARG B CZ  1 
ATOM   2289 N NH1 . ARG B 1 117 ? 12.969  8.334   -56.942  1.00 27.35 ? 113 ARG B NH1 1 
ATOM   2290 N NH2 . ARG B 1 117 ? 13.555  8.010   -54.745  1.00 30.04 ? 113 ARG B NH2 1 
ATOM   2291 N N   . VAL B 1 118 ? 10.889  4.545   -61.780  1.00 18.06 ? 114 VAL B N   1 
ATOM   2292 C CA  . VAL B 1 118 ? 10.576  3.632   -62.865  1.00 16.51 ? 114 VAL B CA  1 
ATOM   2293 C C   . VAL B 1 118 ? 10.221  2.265   -62.291  1.00 16.65 ? 114 VAL B C   1 
ATOM   2294 O O   . VAL B 1 118 ? 10.564  1.919   -61.157  1.00 18.90 ? 114 VAL B O   1 
ATOM   2295 C CB  . VAL B 1 118 ? 11.705  3.528   -63.904  1.00 22.62 ? 114 VAL B CB  1 
ATOM   2296 C CG1 . VAL B 1 118 ? 12.005  4.872   -64.543  1.00 21.95 ? 114 VAL B CG1 1 
ATOM   2297 C CG2 . VAL B 1 118 ? 12.901  2.944   -63.291  1.00 25.46 ? 114 VAL B CG2 1 
ATOM   2298 N N   . VAL B 1 119 ? 9.502   1.489   -63.079  1.00 17.82 ? 115 VAL B N   1 
ATOM   2299 C CA  . VAL B 1 119 ? 9.017   0.175   -62.685  1.00 16.10 ? 115 VAL B CA  1 
ATOM   2300 C C   . VAL B 1 119 ? 9.904   -0.869  -63.346  1.00 16.51 ? 115 VAL B C   1 
ATOM   2301 O O   . VAL B 1 119 ? 9.938   -0.972  -64.583  1.00 16.72 ? 115 VAL B O   1 
ATOM   2302 C CB  . VAL B 1 119 ? 7.555   -0.015  -63.111  1.00 16.91 ? 115 VAL B CB  1 
ATOM   2303 C CG1 . VAL B 1 119 ? 7.026   -1.315  -62.554  1.00 19.47 ? 115 VAL B CG1 1 
ATOM   2304 C CG2 . VAL B 1 119 ? 6.689   1.183   -62.694  1.00 18.46 ? 115 VAL B CG2 1 
ATOM   2305 N N   . LYS B 1 120 ? 10.626  -1.649  -62.557  1.00 17.59 ? 116 LYS B N   1 
ATOM   2306 C CA  . LYS B 1 120 ? 11.562  -2.633  -63.077  1.00 17.55 ? 116 LYS B CA  1 
ATOM   2307 C C   . LYS B 1 120 ? 11.186  -4.033  -62.615  1.00 17.77 ? 116 LYS B C   1 
ATOM   2308 O O   . LYS B 1 120 ? 10.875  -4.252  -61.436  1.00 19.43 ? 116 LYS B O   1 
ATOM   2309 C CB  . LYS B 1 120 ? 12.997  -2.323  -62.639  1.00 19.14 ? 116 LYS B CB  1 
ATOM   2310 C CG  . LYS B 1 120 ? 14.059  -3.199  -63.294  1.00 25.88 ? 116 LYS B CG  1 
ATOM   2311 C CD  . LYS B 1 120 ? 15.454  -2.719  -62.929  1.00 27.23 ? 116 LYS B CD  1 
ATOM   2312 C CE  . LYS B 1 120 ? 16.502  -3.723  -63.352  1.00 36.15 ? 116 LYS B CE  1 
ATOM   2313 N NZ  . LYS B 1 120 ? 16.586  -4.834  -62.365  1.00 45.35 ? 116 LYS B NZ  1 
ATOM   2314 N N   . TRP B 1 121 ? 11.236  -4.979  -63.548  1.00 19.09 ? 117 TRP B N   1 
ATOM   2315 C CA  . TRP B 1 121 ? 11.042  -6.382  -63.226  1.00 19.68 ? 117 TRP B CA  1 
ATOM   2316 C C   . TRP B 1 121 ? 12.165  -6.859  -62.321  1.00 25.33 ? 117 TRP B C   1 
ATOM   2317 O O   . TRP B 1 121 ? 13.344  -6.581  -62.568  1.00 29.54 ? 117 TRP B O   1 
ATOM   2318 C CB  . TRP B 1 121 ? 11.108  -7.164  -64.545  1.00 25.74 ? 117 TRP B CB  1 
ATOM   2319 C CG  . TRP B 1 121 ? 10.966  -8.627  -64.398  1.00 24.93 ? 117 TRP B CG  1 
ATOM   2320 C CD1 . TRP B 1 121 ? 11.964  -9.557  -64.354  1.00 33.17 ? 117 TRP B CD1 1 
ATOM   2321 C CD2 . TRP B 1 121 ? 9.742   -9.341  -64.283  1.00 27.31 ? 117 TRP B CD2 1 
ATOM   2322 N NE1 . TRP B 1 121 ? 11.428  -10.813 -64.209  1.00 36.44 ? 117 TRP B NE1 1 
ATOM   2323 C CE2 . TRP B 1 121 ? 10.062  -10.705 -64.167  1.00 31.12 ? 117 TRP B CE2 1 
ATOM   2324 C CE3 . TRP B 1 121 ? 8.401   -8.957  -64.266  1.00 28.66 ? 117 TRP B CE3 1 
ATOM   2325 C CZ2 . TRP B 1 121 ? 9.089   -11.687 -64.032  1.00 39.92 ? 117 TRP B CZ2 1 
ATOM   2326 C CZ3 . TRP B 1 121 ? 7.438   -9.929  -64.135  1.00 39.69 ? 117 TRP B CZ3 1 
ATOM   2327 C CH2 . TRP B 1 121 ? 7.784   -11.278 -64.019  1.00 40.30 ? 117 TRP B CH2 1 
ATOM   2328 N N   . MET B 1 122 ? 11.808  -7.601  -61.275  1.00 24.20 ? 118 MET B N   1 
ATOM   2329 C CA  . MET B 1 122 ? 12.799  -8.136  -60.348  1.00 35.51 ? 118 MET B CA  1 
ATOM   2330 C C   . MET B 1 122 ? 12.619  -9.636  -60.181  1.00 44.35 ? 118 MET B C   1 
ATOM   2331 O O   . MET B 1 122 ? 11.527  -10.097 -59.837  1.00 46.52 ? 118 MET B O   1 
ATOM   2332 C CB  . MET B 1 122 ? 12.712  -7.458  -58.992  1.00 42.46 ? 118 MET B CB  1 
ATOM   2333 C CG  . MET B 1 122 ? 13.702  -6.341  -58.813  1.00 57.75 ? 118 MET B CG  1 
ATOM   2334 S SD  . MET B 1 122 ? 13.763  -5.924  -57.071  1.00 69.82 ? 118 MET B SD  1 
ATOM   2335 C CE  . MET B 1 122 ? 15.368  -6.591  -56.669  1.00 68.69 ? 118 MET B CE  1 
ATOM   2336 N N   . LEU B 1 123 ? 13.698  -10.390 -60.390  1.00 51.87 ? 119 LEU B N   1 
ATOM   2337 C CA  . LEU B 1 123 ? 13.645  -11.839 -60.234  1.00 63.67 ? 119 LEU B CA  1 
ATOM   2338 C C   . LEU B 1 123 ? 13.859  -12.294 -58.794  1.00 69.04 ? 119 LEU B C   1 
ATOM   2339 O O   . LEU B 1 123 ? 13.484  -13.422 -58.454  1.00 72.85 ? 119 LEU B O   1 
ATOM   2340 C CB  . LEU B 1 123 ? 14.678  -12.504 -61.149  1.00 65.75 ? 119 LEU B CB  1 
ATOM   2341 C CG  . LEU B 1 123 ? 14.408  -13.944 -61.591  1.00 65.51 ? 119 LEU B CG  1 
ATOM   2342 C CD1 . LEU B 1 123 ? 13.277  -14.007 -62.607  1.00 63.83 ? 119 LEU B CD1 1 
ATOM   2343 C CD2 . LEU B 1 123 ? 15.672  -14.579 -62.148  1.00 66.45 ? 119 LEU B CD2 1 
ATOM   2344 N N   . THR B 1 124 ? 14.441  -11.450 -57.940  1.00 69.47 ? 120 THR B N   1 
ATOM   2345 C CA  . THR B 1 124 ? 14.793  -11.825 -56.568  1.00 71.59 ? 120 THR B CA  1 
ATOM   2346 C C   . THR B 1 124 ? 14.334  -10.731 -55.611  1.00 67.60 ? 120 THR B C   1 
ATOM   2347 O O   . THR B 1 124 ? 15.075  -9.786  -55.332  1.00 69.89 ? 120 THR B O   1 
ATOM   2348 C CB  . THR B 1 124 ? 16.294  -12.072 -56.448  1.00 76.10 ? 120 THR B CB  1 
ATOM   2349 O OG1 . THR B 1 124 ? 16.754  -12.806 -57.590  1.00 77.75 ? 120 THR B OG1 1 
ATOM   2350 C CG2 . THR B 1 124 ? 16.609  -12.856 -55.181  1.00 77.61 ? 120 THR B CG2 1 
ATOM   2351 N N   . GLY B 1 125 A 13.123  -10.878 -55.093  1.00 61.42 ? 120 GLY B N   1 
ATOM   2352 C CA  . GLY B 1 125 A 12.618  -9.948  -54.102  1.00 56.59 ? 120 GLY B CA  1 
ATOM   2353 C C   . GLY B 1 125 A 11.309  -10.455 -53.546  1.00 53.97 ? 120 GLY B C   1 
ATOM   2354 O O   . GLY B 1 125 A 10.752  -11.451 -54.018  1.00 54.57 ? 120 GLY B O   1 
ATOM   2355 N N   . SER B 1 126 B 10.823  -9.757  -52.520  1.00 55.52 ? 120 SER B N   1 
ATOM   2356 C CA  . SER B 1 126 B 9.506   -10.073 -51.979  1.00 55.83 ? 120 SER B CA  1 
ATOM   2357 C C   . SER B 1 126 B 8.396   -9.748  -52.970  1.00 47.04 ? 120 SER B C   1 
ATOM   2358 O O   . SER B 1 126 B 7.309   -10.326 -52.882  1.00 49.88 ? 120 SER B O   1 
ATOM   2359 C CB  . SER B 1 126 B 9.277   -9.326  -50.658  1.00 63.89 ? 120 SER B CB  1 
ATOM   2360 O OG  . SER B 1 126 B 9.853   -8.030  -50.702  1.00 66.35 ? 120 SER B OG  1 
ATOM   2361 N N   . HIS B 1 127 C 8.654   -8.842  -53.906  1.00 37.91 ? 120 HIS B N   1 
ATOM   2362 C CA  . HIS B 1 127 C 7.694   -8.380  -54.894  1.00 33.12 ? 120 HIS B CA  1 
ATOM   2363 C C   . HIS B 1 127 C 8.272   -8.632  -56.281  1.00 27.93 ? 120 HIS B C   1 
ATOM   2364 O O   . HIS B 1 127 C 9.492   -8.726  -56.453  1.00 27.98 ? 120 HIS B O   1 
ATOM   2365 C CB  . HIS B 1 127 C 7.364   -6.892  -54.682  1.00 30.68 ? 120 HIS B CB  1 
ATOM   2366 C CG  . HIS B 1 127 C 7.045   -6.544  -53.259  1.00 35.55 ? 120 HIS B CG  1 
ATOM   2367 N ND1 . HIS B 1 127 C 5.942   -7.043  -52.600  1.00 37.41 ? 120 HIS B ND1 1 
ATOM   2368 C CD2 . HIS B 1 127 C 7.691   -5.759  -52.366  1.00 33.79 ? 120 HIS B CD2 1 
ATOM   2369 C CE1 . HIS B 1 127 C 5.918   -6.575  -51.364  1.00 32.52 ? 120 HIS B CE1 1 
ATOM   2370 N NE2 . HIS B 1 127 C 6.972   -5.797  -51.194  1.00 37.51 ? 120 HIS B NE2 1 
ATOM   2371 N N   . MET B 1 128 ? 7.392   -8.747  -57.281  1.00 25.71 ? 121 MET B N   1 
ATOM   2372 C CA  . MET B 1 128 ? 7.844   -9.062  -58.630  1.00 23.93 ? 121 MET B CA  1 
ATOM   2373 C C   . MET B 1 128 ? 8.361   -7.847  -59.385  1.00 26.57 ? 121 MET B C   1 
ATOM   2374 O O   . MET B 1 128 ? 9.023   -8.010  -60.417  1.00 28.68 ? 121 MET B O   1 
ATOM   2375 C CB  . MET B 1 128 ? 6.664   -9.607  -59.439  1.00 31.21 ? 121 MET B CB  1 
ATOM   2376 C CG  . MET B 1 128 ? 5.988   -10.824 -58.860  1.00 34.40 ? 121 MET B CG  1 
ATOM   2377 S SD  . MET B 1 128 ? 4.687   -11.423 -59.961  1.00 41.35 ? 121 MET B SD  1 
ATOM   2378 C CE  . MET B 1 128 ? 4.129   -12.867 -59.054  1.00 46.07 ? 121 MET B CE  1 
ATOM   2379 N N   . ILE B 1 129 ? 8.100   -6.644  -58.885  1.00 22.91 ? 122 ILE B N   1 
ATOM   2380 C CA  . ILE B 1 129 ? 8.596   -5.412  -59.474  1.00 21.64 ? 122 ILE B CA  1 
ATOM   2381 C C   . ILE B 1 129 ? 9.165   -4.553  -58.358  1.00 22.58 ? 122 ILE B C   1 
ATOM   2382 O O   . ILE B 1 129 ? 8.828   -4.715  -57.183  1.00 25.06 ? 122 ILE B O   1 
ATOM   2383 C CB  . ILE B 1 129 ? 7.512   -4.637  -60.253  1.00 18.84 ? 122 ILE B CB  1 
ATOM   2384 C CG1 . ILE B 1 129 ? 6.294   -4.372  -59.365  1.00 21.43 ? 122 ILE B CG1 1 
ATOM   2385 C CG2 . ILE B 1 129 ? 7.133   -5.388  -61.520  1.00 21.23 ? 122 ILE B CG2 1 
ATOM   2386 C CD1 . ILE B 1 129 ? 5.162   -3.626  -60.083  1.00 23.25 ? 122 ILE B CD1 1 
ATOM   2387 N N   . GLU B 1 130 ? 10.044  -3.637  -58.736  1.00 19.15 ? 123 GLU B N   1 
ATOM   2388 C CA  . GLU B 1 130 ? 10.568  -2.631  -57.827  1.00 22.23 ? 123 GLU B CA  1 
ATOM   2389 C C   . GLU B 1 130 ? 10.408  -1.253  -58.450  1.00 19.75 ? 123 GLU B C   1 
ATOM   2390 O O   . GLU B 1 130 ? 10.384  -1.103  -59.678  1.00 20.94 ? 123 GLU B O   1 
ATOM   2391 C CB  . GLU B 1 130 ? 12.052  -2.893  -57.488  1.00 23.41 ? 123 GLU B CB  1 
ATOM   2392 C CG  . GLU B 1 130 ? 12.989  -2.751  -58.698  1.00 29.42 ? 123 GLU B CG  1 
ATOM   2393 C CD  . GLU B 1 130 ? 14.472  -2.970  -58.376  1.00 42.37 ? 123 GLU B CD  1 
ATOM   2394 O OE1 . GLU B 1 130 ? 14.878  -2.799  -57.204  1.00 44.15 ? 123 GLU B OE1 1 
ATOM   2395 O OE2 . GLU B 1 130 ? 15.236  -3.300  -59.312  1.00 39.10 ? 123 GLU B OE2 1 
ATOM   2396 N N   . PHE B 1 131 ? 10.332  -0.241  -57.598  1.00 22.06 ? 124 PHE B N   1 
ATOM   2397 C CA  . PHE B 1 131 ? 10.233  1.147   -58.018  1.00 20.37 ? 124 PHE B CA  1 
ATOM   2398 C C   . PHE B 1 131 ? 11.558  1.805   -57.699  1.00 20.98 ? 124 PHE B C   1 
ATOM   2399 O O   . PHE B 1 131 ? 11.939  1.893   -56.527  1.00 22.96 ? 124 PHE B O   1 
ATOM   2400 C CB  . PHE B 1 131 ? 9.068   1.813   -57.287  1.00 22.68 ? 124 PHE B CB  1 
ATOM   2401 C CG  . PHE B 1 131 ? 7.780   1.102   -57.508  1.00 23.14 ? 124 PHE B CG  1 
ATOM   2402 C CD1 . PHE B 1 131 ? 7.146   1.181   -58.731  1.00 22.49 ? 124 PHE B CD1 1 
ATOM   2403 C CD2 . PHE B 1 131 ? 7.214   0.314   -56.508  1.00 27.86 ? 124 PHE B CD2 1 
ATOM   2404 C CE1 . PHE B 1 131 ? 5.970   0.508   -58.968  1.00 24.04 ? 124 PHE B CE1 1 
ATOM   2405 C CE2 . PHE B 1 131 ? 6.036   -0.367  -56.741  1.00 27.98 ? 124 PHE B CE2 1 
ATOM   2406 C CZ  . PHE B 1 131 ? 5.409   -0.264  -57.957  1.00 29.77 ? 124 PHE B CZ  1 
ATOM   2407 N N   . ILE B 1 132 ? 12.280  2.231   -58.736  1.00 19.64 ? 125 ILE B N   1 
ATOM   2408 C CA  . ILE B 1 132 ? 13.689  2.574   -58.607  1.00 22.04 ? 125 ILE B CA  1 
ATOM   2409 C C   . ILE B 1 132 ? 13.992  3.914   -59.260  1.00 20.22 ? 125 ILE B C   1 
ATOM   2410 O O   . ILE B 1 132 ? 13.296  4.350   -60.186  1.00 19.33 ? 125 ILE B O   1 
ATOM   2411 C CB  . ILE B 1 132 ? 14.650  1.492   -59.146  1.00 22.81 ? 125 ILE B CB  1 
ATOM   2412 C CG1 . ILE B 1 132 ? 14.369  1.137   -60.604  1.00 22.72 ? 125 ILE B CG1 1 
ATOM   2413 C CG2 . ILE B 1 132 ? 14.630  0.290   -58.253  1.00 35.56 ? 125 ILE B CG2 1 
ATOM   2414 C CD1 . ILE B 1 132 ? 15.457  0.247   -61.170  1.00 26.38 ? 125 ILE B CD1 1 
ATOM   2415 N N   . GLU B 1 133 ? 15.033  4.563   -58.746  1.00 21.06 ? 126 GLU B N   1 
ATOM   2416 C CA  . GLU B 1 133 ? 15.563  5.786   -59.323  1.00 22.23 ? 126 GLU B CA  1 
ATOM   2417 C C   . GLU B 1 133 ? 16.088  5.507   -60.731  1.00 22.75 ? 126 GLU B C   1 
ATOM   2418 O O   . GLU B 1 133 ? 16.367  4.365   -61.109  1.00 23.47 ? 126 GLU B O   1 
ATOM   2419 C CB  . GLU B 1 133 ? 16.702  6.322   -58.455  1.00 25.72 ? 126 GLU B CB  1 
ATOM   2420 C CG  . GLU B 1 133 ? 16.272  6.939   -57.144  1.00 33.97 ? 126 GLU B CG  1 
ATOM   2421 C CD  . GLU B 1 133 ? 17.438  7.570   -56.399  1.00 50.39 ? 126 GLU B CD  1 
ATOM   2422 O OE1 . GLU B 1 133 ? 18.380  6.834   -56.039  1.00 56.00 ? 126 GLU B OE1 1 
ATOM   2423 O OE2 . GLU B 1 133 ? 17.416  8.799   -56.178  1.00 55.43 ? 126 GLU B OE2 1 
ATOM   2424 N N   . PHE B 1 134 ? 16.246  6.580   -61.501  1.00 21.10 ? 127 PHE B N   1 
ATOM   2425 C CA  . PHE B 1 134 ? 16.591  6.461   -62.912  1.00 19.91 ? 127 PHE B CA  1 
ATOM   2426 C C   . PHE B 1 134 ? 17.382  7.695   -63.321  1.00 21.91 ? 127 PHE B C   1 
ATOM   2427 O O   . PHE B 1 134 ? 17.410  8.712   -62.620  1.00 24.94 ? 127 PHE B O   1 
ATOM   2428 C CB  . PHE B 1 134 ? 15.316  6.377   -63.784  1.00 23.95 ? 127 PHE B CB  1 
ATOM   2429 C CG  . PHE B 1 134 ? 14.509  7.644   -63.741  1.00 22.44 ? 127 PHE B CG  1 
ATOM   2430 C CD1 . PHE B 1 134 ? 13.664  7.902   -62.675  1.00 21.58 ? 127 PHE B CD1 1 
ATOM   2431 C CD2 . PHE B 1 134 ? 14.700  8.636   -64.683  1.00 23.55 ? 127 PHE B CD2 1 
ATOM   2432 C CE1 . PHE B 1 134 ? 12.973  9.109   -62.588  1.00 26.45 ? 127 PHE B CE1 1 
ATOM   2433 C CE2 . PHE B 1 134 ? 14.015  9.841   -64.603  1.00 24.47 ? 127 PHE B CE2 1 
ATOM   2434 C CZ  . PHE B 1 134 ? 13.151  10.078  -63.547  1.00 24.55 ? 127 PHE B CZ  1 
ATOM   2435 N N   . GLU B 1 135 ? 18.016  7.597   -64.479  1.00 22.53 ? 128 GLU B N   1 
ATOM   2436 C CA  . GLU B 1 135 ? 18.650  8.721   -65.146  1.00 24.06 ? 128 GLU B CA  1 
ATOM   2437 C C   . GLU B 1 135 ? 18.141  8.745   -66.581  1.00 23.22 ? 128 GLU B C   1 
ATOM   2438 O O   . GLU B 1 135 ? 17.755  7.703   -67.124  1.00 22.44 ? 128 GLU B O   1 
ATOM   2439 C CB  . GLU B 1 135 ? 20.179  8.560   -65.190  1.00 27.80 ? 128 GLU B CB  1 
ATOM   2440 C CG  . GLU B 1 135 ? 20.828  8.092   -63.904  1.00 38.39 ? 128 GLU B CG  1 
ATOM   2441 C CD  . GLU B 1 135 ? 22.282  7.708   -64.119  1.00 50.10 ? 128 GLU B CD  1 
ATOM   2442 O OE1 . GLU B 1 135 ? 22.602  6.499   -64.052  1.00 49.34 ? 128 GLU B OE1 1 
ATOM   2443 O OE2 . GLU B 1 135 ? 23.099  8.617   -64.378  1.00 52.97 ? 128 GLU B OE2 1 
ATOM   2444 N N   . ILE B 1 136 ? 18.169  9.928   -67.197  1.00 24.06 ? 129 ILE B N   1 
ATOM   2445 C CA  . ILE B 1 136 ? 17.737  10.147  -68.576  1.00 26.03 ? 129 ILE B CA  1 
ATOM   2446 C C   . ILE B 1 136 ? 18.901  10.732  -69.359  1.00 24.92 ? 129 ILE B C   1 
ATOM   2447 O O   . ILE B 1 136 ? 19.592  11.635  -68.876  1.00 27.16 ? 129 ILE B O   1 
ATOM   2448 C CB  . ILE B 1 136 ? 16.539  11.115  -68.658  1.00 35.50 ? 129 ILE B CB  1 
ATOM   2449 C CG1 . ILE B 1 136 ? 15.410  10.667  -67.741  1.00 42.16 ? 129 ILE B CG1 1 
ATOM   2450 C CG2 . ILE B 1 136 ? 16.015  11.181  -70.073  1.00 30.65 ? 129 ILE B CG2 1 
ATOM   2451 C CD1 . ILE B 1 136 ? 15.039  9.255   -67.934  1.00 43.05 ? 129 ILE B CD1 1 
ATOM   2452 N N   . GLU B 1 137 ? 19.106  10.239  -70.575  1.00 23.10 ? 130 GLU B N   1 
ATOM   2453 C CA  . GLU B 1 137 ? 20.115  10.780  -71.470  1.00 26.75 ? 130 GLU B CA  1 
ATOM   2454 C C   . GLU B 1 137 ? 19.469  11.124  -72.803  1.00 25.57 ? 130 GLU B C   1 
ATOM   2455 O O   . GLU B 1 137 ? 18.759  10.298  -73.383  1.00 24.40 ? 130 GLU B O   1 
ATOM   2456 C CB  . GLU B 1 137 ? 21.243  9.769   -71.680  1.00 26.16 ? 130 GLU B CB  1 
ATOM   2457 C CG  . GLU B 1 137 ? 22.351  10.249  -72.592  1.00 37.17 ? 130 GLU B CG  1 
ATOM   2458 C CD  . GLU B 1 137 ? 23.457  9.222   -72.744  1.00 44.69 ? 130 GLU B CD  1 
ATOM   2459 O OE1 . GLU B 1 137 ? 23.383  8.171   -72.069  1.00 43.33 ? 130 GLU B OE1 1 
ATOM   2460 O OE2 . GLU B 1 137 ? 24.401  9.472   -73.529  1.00 46.14 ? 130 GLU B OE2 1 
ATOM   2461 N N   . ASP B 1 138 ? 19.734  12.331  -73.289  1.00 26.88 ? 131 ASP B N   1 
ATOM   2462 C CA  . ASP B 1 138 ? 19.263  12.798  -74.585  1.00 26.71 ? 131 ASP B CA  1 
ATOM   2463 C C   . ASP B 1 138 ? 20.263  12.306  -75.624  1.00 27.09 ? 131 ASP B C   1 
ATOM   2464 O O   . ASP B 1 138 ? 21.436  12.689  -75.584  1.00 28.83 ? 131 ASP B O   1 
ATOM   2465 C CB  . ASP B 1 138 ? 19.239  14.328  -74.560  1.00 30.33 ? 131 ASP B CB  1 
ATOM   2466 C CG  . ASP B 1 138 ? 18.704  14.956  -75.845  1.00 36.79 ? 131 ASP B CG  1 
ATOM   2467 O OD1 . ASP B 1 138 ? 18.604  14.276  -76.881  1.00 33.09 ? 131 ASP B OD1 1 
ATOM   2468 O OD2 . ASP B 1 138 ? 18.397  16.169  -75.817  1.00 42.13 ? 131 ASP B OD2 1 
ATOM   2469 N N   . LEU B 1 139 ? 19.814  11.451  -76.539  1.00 24.44 ? 132 LEU B N   1 
ATOM   2470 C CA  . LEU B 1 139 ? 20.684  10.914  -77.575  1.00 25.45 ? 132 LEU B CA  1 
ATOM   2471 C C   . LEU B 1 139 ? 20.607  11.707  -78.871  1.00 26.86 ? 132 LEU B C   1 
ATOM   2472 O O   . LEU B 1 139 ? 21.293  11.356  -79.839  1.00 29.50 ? 132 LEU B O   1 
ATOM   2473 C CB  . LEU B 1 139 ? 20.373  9.428   -77.839  1.00 28.29 ? 132 LEU B CB  1 
ATOM   2474 C CG  . LEU B 1 139 ? 20.323  8.469   -76.638  1.00 28.06 ? 132 LEU B CG  1 
ATOM   2475 C CD1 . LEU B 1 139 ? 20.109  7.029   -77.115  1.00 27.87 ? 132 LEU B CD1 1 
ATOM   2476 C CD2 . LEU B 1 139 ? 21.572  8.561   -75.761  1.00 30.05 ? 132 LEU B CD2 1 
ATOM   2477 N N   . GLY B 1 140 ? 19.816  12.774  -78.903  1.00 26.77 ? 133 GLY B N   1 
ATOM   2478 C CA  . GLY B 1 140 ? 19.648  13.582  -80.095  1.00 24.23 ? 133 GLY B CA  1 
ATOM   2479 C C   . GLY B 1 140 ? 18.709  12.967  -81.115  1.00 25.57 ? 133 GLY B C   1 
ATOM   2480 O O   . GLY B 1 140 ? 18.116  11.904  -80.918  1.00 24.29 ? 133 GLY B O   1 
ATOM   2481 N N   . VAL B 1 141 ? 18.588  13.653  -82.250  1.00 26.38 ? 134 VAL B N   1 
ATOM   2482 C CA  . VAL B 1 141 ? 17.669  13.233  -83.303  1.00 26.37 ? 134 VAL B CA  1 
ATOM   2483 C C   . VAL B 1 141 ? 18.326  12.135  -84.129  1.00 27.98 ? 134 VAL B C   1 
ATOM   2484 O O   . VAL B 1 141 ? 19.503  12.235  -84.493  1.00 31.08 ? 134 VAL B O   1 
ATOM   2485 C CB  . VAL B 1 141 ? 17.271  14.430  -84.183  1.00 27.66 ? 134 VAL B CB  1 
ATOM   2486 C CG1 . VAL B 1 141 ? 16.470  13.954  -85.396  1.00 28.68 ? 134 VAL B CG1 1 
ATOM   2487 C CG2 . VAL B 1 141 ? 16.484  15.461  -83.366  1.00 29.64 ? 134 VAL B CG2 1 
ATOM   2488 N N   . MET B 1 142 ? 17.576  11.069  -84.411  1.00 25.07 ? 135 MET B N   1 
ATOM   2489 C CA  . MET B 1 142 ? 18.048  9.961   -85.235  1.00 28.03 ? 135 MET B CA  1 
ATOM   2490 C C   . MET B 1 142 ? 16.970  9.584   -86.248  1.00 27.74 ? 135 MET B C   1 
ATOM   2491 O O   . MET B 1 142 ? 15.773  9.702   -85.974  1.00 25.68 ? 135 MET B O   1 
ATOM   2492 C CB  . MET B 1 142 ? 18.327  8.720   -84.380  1.00 30.61 ? 135 MET B CB  1 
ATOM   2493 C CG  . MET B 1 142 ? 19.246  8.938   -83.189  1.00 38.34 ? 135 MET B CG  1 
ATOM   2494 S SD  . MET B 1 142 ? 19.560  7.392   -82.305  1.00 37.16 ? 135 MET B SD  1 
ATOM   2495 C CE  . MET B 1 142 ? 20.837  7.970   -81.182  1.00 41.22 ? 135 MET B CE  1 
ATOM   2496 N N   . GLU B 1 143 ? 17.394  9.122   -87.425  1.00 26.86 ? 136 GLU B N   1 
ATOM   2497 C CA  . GLU B 1 143 ? 16.504  8.403   -88.334  1.00 25.95 ? 136 GLU B CA  1 
ATOM   2498 C C   . GLU B 1 143 ? 16.678  6.916   -88.053  1.00 25.28 ? 136 GLU B C   1 
ATOM   2499 O O   . GLU B 1 143 ? 17.776  6.372   -88.195  1.00 27.13 ? 136 GLU B O   1 
ATOM   2500 C CB  . GLU B 1 143 ? 16.784  8.715   -89.808  1.00 27.50 ? 136 GLU B CB  1 
ATOM   2501 C CG  . GLU B 1 143 ? 15.748  8.088   -90.739  1.00 30.44 ? 136 GLU B CG  1 
ATOM   2502 C CD  . GLU B 1 143 ? 15.983  8.375   -92.210  1.00 42.56 ? 136 GLU B CD  1 
ATOM   2503 O OE1 . GLU B 1 143 ? 16.974  9.058   -92.544  1.00 46.94 ? 136 GLU B OE1 1 
ATOM   2504 O OE2 . GLU B 1 143 ? 15.166  7.909   -93.031  1.00 47.41 ? 136 GLU B OE2 1 
ATOM   2505 N N   . ILE B 1 144 ? 15.603  6.267   -87.614  1.00 24.13 ? 137 ILE B N   1 
ATOM   2506 C CA  . ILE B 1 144 ? 15.725  4.976   -86.952  1.00 23.01 ? 137 ILE B CA  1 
ATOM   2507 C C   . ILE B 1 144 ? 14.422  4.212   -87.122  1.00 24.58 ? 137 ILE B C   1 
ATOM   2508 O O   . ILE B 1 144 ? 13.341  4.802   -87.182  1.00 23.33 ? 137 ILE B O   1 
ATOM   2509 C CB  . ILE B 1 144 ? 16.081  5.219   -85.459  1.00 23.01 ? 137 ILE B CB  1 
ATOM   2510 C CG1 . ILE B 1 144 ? 16.258  3.917   -84.681  1.00 26.20 ? 137 ILE B CG1 1 
ATOM   2511 C CG2 . ILE B 1 144 ? 15.071  6.170   -84.789  1.00 23.92 ? 137 ILE B CG2 1 
ATOM   2512 C CD1 . ILE B 1 144 ? 16.967  4.152   -83.364  1.00 28.71 ? 137 ILE B CD1 1 
ATOM   2513 N N   . ASP B 1 145 ? 14.536  2.888   -87.218  1.00 21.64 ? 138 ASP B N   1 
ATOM   2514 C CA  . ASP B 1 145 ? 13.371  2.018   -87.139  1.00 22.75 ? 138 ASP B CA  1 
ATOM   2515 C C   . ASP B 1 145 ? 12.967  1.852   -85.680  1.00 21.95 ? 138 ASP B C   1 
ATOM   2516 O O   . ASP B 1 145 ? 13.802  1.546   -84.821  1.00 22.64 ? 138 ASP B O   1 
ATOM   2517 C CB  . ASP B 1 145 ? 13.701  0.640   -87.694  1.00 22.04 ? 138 ASP B CB  1 
ATOM   2518 C CG  . ASP B 1 145 ? 13.855  0.625   -89.202  1.00 25.85 ? 138 ASP B CG  1 
ATOM   2519 O OD1 . ASP B 1 145 ? 13.339  1.544   -89.882  1.00 28.95 ? 138 ASP B OD1 1 
ATOM   2520 O OD2 . ASP B 1 145 ? 14.502  -0.318  -89.702  1.00 32.66 ? 138 ASP B OD2 1 
ATOM   2521 N N   . VAL B 1 146 ? 11.697  2.092   -85.390  1.00 19.94 ? 139 VAL B N   1 
ATOM   2522 C CA  . VAL B 1 146 ? 11.180  1.933   -84.036  1.00 19.10 ? 139 VAL B CA  1 
ATOM   2523 C C   . VAL B 1 146 ? 9.971   1.007   -84.074  1.00 16.54 ? 139 VAL B C   1 
ATOM   2524 O O   . VAL B 1 146 ? 9.329   0.832   -85.116  1.00 17.68 ? 139 VAL B O   1 
ATOM   2525 C CB  . VAL B 1 146 ? 10.869  3.279   -83.346  1.00 19.34 ? 139 VAL B CB  1 
ATOM   2526 C CG1 . VAL B 1 146 ? 12.166  4.039   -83.059  1.00 21.07 ? 139 VAL B CG1 1 
ATOM   2527 C CG2 . VAL B 1 146 ? 9.984   4.116   -84.235  1.00 21.94 ? 139 VAL B CG2 1 
ATOM   2528 N N   . TYR B 1 147 ? 9.686   0.391   -82.925  1.00 15.29 ? 140 TYR B N   1 
ATOM   2529 C CA  . TYR B 1 147 ? 8.713   -0.685  -82.823  1.00 16.24 ? 140 TYR B CA  1 
ATOM   2530 C C   . TYR B 1 147 ? 7.838   -0.499  -81.593  1.00 15.61 ? 140 TYR B C   1 
ATOM   2531 O O   . TYR B 1 147 ? 8.259   0.075   -80.588  1.00 15.81 ? 140 TYR B O   1 
ATOM   2532 C CB  . TYR B 1 147 ? 9.401   -2.051  -82.707  1.00 18.16 ? 140 TYR B CB  1 
ATOM   2533 C CG  . TYR B 1 147 ? 10.262  -2.401  -83.890  1.00 15.80 ? 140 TYR B CG  1 
ATOM   2534 C CD1 . TYR B 1 147 ? 11.532  -1.862  -84.020  1.00 17.88 ? 140 TYR B CD1 1 
ATOM   2535 C CD2 . TYR B 1 147 ? 9.818   -3.291  -84.866  1.00 18.12 ? 140 TYR B CD2 1 
ATOM   2536 C CE1 . TYR B 1 147 ? 12.337  -2.181  -85.097  1.00 17.63 ? 140 TYR B CE1 1 
ATOM   2537 C CE2 . TYR B 1 147 ? 10.611  -3.612  -85.946  1.00 17.37 ? 140 TYR B CE2 1 
ATOM   2538 C CZ  . TYR B 1 147 ? 11.866  -3.061  -86.056  1.00 18.95 ? 140 TYR B CZ  1 
ATOM   2539 O OH  . TYR B 1 147 ? 12.653  -3.406  -87.143  1.00 21.80 ? 140 TYR B OH  1 
ATOM   2540 N N   . ASP B 1 148 ? 6.624   -1.030  -81.668  1.00 17.27 ? 141 ASP B N   1 
ATOM   2541 C CA  . ASP B 1 148 ? 5.700   -1.013  -80.543  1.00 18.38 ? 141 ASP B CA  1 
ATOM   2542 C C   . ASP B 1 148 ? 4.803   -2.242  -80.628  1.00 15.91 ? 141 ASP B C   1 
ATOM   2543 O O   . ASP B 1 148 ? 4.716   -2.904  -81.664  1.00 16.53 ? 141 ASP B O   1 
ATOM   2544 C CB  . ASP B 1 148 ? 4.884   0.288   -80.489  1.00 22.76 ? 141 ASP B CB  1 
ATOM   2545 C CG  . ASP B 1 148 ? 4.497   0.673   -79.059  1.00 34.18 ? 141 ASP B CG  1 
ATOM   2546 O OD1 . ASP B 1 148 ? 4.690   -0.153  -78.139  1.00 35.56 ? 141 ASP B OD1 1 
ATOM   2547 O OD2 . ASP B 1 148 ? 4.032   1.811   -78.844  1.00 38.62 ? 141 ASP B OD2 1 
ATOM   2548 N N   . ILE B 1 149 ? 4.205   -2.596  -79.493  1.00 18.10 ? 142 ILE B N   1 
ATOM   2549 C CA  . ILE B 1 149 ? 3.215   -3.664  -79.434  1.00 16.78 ? 142 ILE B CA  1 
ATOM   2550 C C   . ILE B 1 149 ? 1.963   -3.121  -78.762  1.00 15.08 ? 142 ILE B C   1 
ATOM   2551 O O   . ILE B 1 149 ? 2.035   -2.216  -77.925  1.00 18.24 ? 142 ILE B O   1 
ATOM   2552 C CB  . ILE B 1 149 ? 3.729   -4.966  -78.744  1.00 17.54 ? 142 ILE B CB  1 
ATOM   2553 C CG1 . ILE B 1 149 ? 4.361   -4.689  -77.369  1.00 22.40 ? 142 ILE B CG1 1 
ATOM   2554 C CG2 . ILE B 1 149 ? 4.726   -5.715  -79.637  1.00 20.79 ? 142 ILE B CG2 1 
ATOM   2555 C CD1 . ILE B 1 149 ? 4.617   -5.980  -76.558  1.00 21.28 ? 142 ILE B CD1 1 
ATOM   2556 N N   . GLU B 1 150 ? 0.810   -3.643  -79.154  1.00 15.35 ? 143 GLU B N   1 
ATOM   2557 C CA  . GLU B 1 150 ? -0.430  -3.420  -78.420  1.00 15.31 ? 143 GLU B CA  1 
ATOM   2558 C C   . GLU B 1 150 ? -0.617  -4.592  -77.470  1.00 18.16 ? 143 GLU B C   1 
ATOM   2559 O O   . GLU B 1 150 ? -0.683  -5.748  -77.909  1.00 17.85 ? 143 GLU B O   1 
ATOM   2560 C CB  . GLU B 1 150 ? -1.667  -3.280  -79.313  1.00 18.80 ? 143 GLU B CB  1 
ATOM   2561 C CG  . GLU B 1 150 ? -2.961  -3.157  -78.445  1.00 20.95 ? 143 GLU B CG  1 
ATOM   2562 C CD  . GLU B 1 150 ? -4.243  -3.012  -79.223  1.00 23.73 ? 143 GLU B CD  1 
ATOM   2563 O OE1 . GLU B 1 150 ? -4.319  -2.113  -80.083  1.00 25.96 ? 143 GLU B OE1 1 
ATOM   2564 O OE2 . GLU B 1 150 ? -5.195  -3.770  -78.943  1.00 28.88 ? 143 GLU B OE2 1 
ATOM   2565 N N   . VAL B 1 151 ? -0.729  -4.291  -76.181  1.00 18.37 ? 144 VAL B N   1 
ATOM   2566 C CA  . VAL B 1 151 ? -0.880  -5.300  -75.139  1.00 17.80 ? 144 VAL B CA  1 
ATOM   2567 C C   . VAL B 1 151 ? -2.286  -5.165  -74.570  1.00 19.19 ? 144 VAL B C   1 
ATOM   2568 O O   . VAL B 1 151 ? -2.650  -4.110  -74.027  1.00 19.65 ? 144 VAL B O   1 
ATOM   2569 C CB  . VAL B 1 151 ? 0.194   -5.149  -74.047  1.00 17.57 ? 144 VAL B CB  1 
ATOM   2570 C CG1 . VAL B 1 151 ? -0.071  -6.137  -72.912  1.00 19.52 ? 144 VAL B CG1 1 
ATOM   2571 C CG2 . VAL B 1 151 ? 1.591   -5.359  -74.618  1.00 18.48 ? 144 VAL B CG2 1 
ATOM   2572 N N   . ASP B 1 152 ? -3.060  -6.240  -74.676  1.00 17.20 ? 145 ASP B N   1 
ATOM   2573 C CA  . ASP B 1 152 ? -4.455  -6.238  -74.253  1.00 17.86 ? 145 ASP B CA  1 
ATOM   2574 C C   . ASP B 1 152 ? -4.603  -5.849  -72.779  1.00 17.22 ? 145 ASP B C   1 
ATOM   2575 O O   . ASP B 1 152 ? -3.867  -6.332  -71.909  1.00 18.92 ? 145 ASP B O   1 
ATOM   2576 C CB  . ASP B 1 152 ? -5.023  -7.635  -74.439  1.00 19.96 ? 145 ASP B CB  1 
ATOM   2577 C CG  . ASP B 1 152 ? -6.509  -7.632  -74.475  1.00 32.85 ? 145 ASP B CG  1 
ATOM   2578 O OD1 . ASP B 1 152 ? -7.066  -7.049  -75.431  1.00 34.72 ? 145 ASP B OD1 1 
ATOM   2579 O OD2 . ASP B 1 152 ? -7.106  -8.185  -73.533  1.00 34.09 ? 145 ASP B OD2 1 
ATOM   2580 N N   . GLY B 1 153 ? -5.550  -4.952  -72.498  1.00 18.97 ? 146 GLY B N   1 
ATOM   2581 C CA  . GLY B 1 153 ? -5.933  -4.660  -71.124  1.00 18.76 ? 146 GLY B CA  1 
ATOM   2582 C C   . GLY B 1 153 ? -5.041  -3.667  -70.409  1.00 19.67 ? 146 GLY B C   1 
ATOM   2583 O O   . GLY B 1 153 ? -5.497  -2.620  -69.954  1.00 21.62 ? 146 GLY B O   1 
ATOM   2584 N N   . ASN B 1 154 ? -3.754  -3.971  -70.313  1.00 17.46 ? 147 ASN B N   1 
ATOM   2585 C CA  . ASN B 1 154 ? -2.871  -3.177  -69.472  1.00 17.24 ? 147 ASN B CA  1 
ATOM   2586 C C   . ASN B 1 154 ? -2.079  -2.101  -70.212  1.00 17.05 ? 147 ASN B C   1 
ATOM   2587 O O   . ASN B 1 154 ? -1.637  -1.137  -69.576  1.00 22.25 ? 147 ASN B O   1 
ATOM   2588 C CB  . ASN B 1 154 ? -1.975  -4.084  -68.628  1.00 18.33 ? 147 ASN B CB  1 
ATOM   2589 C CG  . ASN B 1 154 ? -2.764  -4.834  -67.554  1.00 18.36 ? 147 ASN B CG  1 
ATOM   2590 O OD1 . ASN B 1 154 ? -3.807  -4.363  -67.089  1.00 19.56 ? 147 ASN B OD1 1 
ATOM   2591 N ND2 . ASN B 1 154 ? -2.279  -6.011  -67.172  1.00 20.11 ? 147 ASN B ND2 1 
ATOM   2592 N N   . HIS B 1 155 ? -1.877  -2.243  -71.513  1.00 18.14 ? 148 HIS B N   1 
ATOM   2593 C CA  . HIS B 1 155 ? -1.240  -1.207  -72.338  1.00 18.58 ? 148 HIS B CA  1 
ATOM   2594 C C   . HIS B 1 155 ? 0.152   -0.825  -71.844  1.00 14.93 ? 148 HIS B C   1 
ATOM   2595 O O   . HIS B 1 155 ? 0.536   0.343   -71.856  1.00 17.15 ? 148 HIS B O   1 
ATOM   2596 C CB  . HIS B 1 155 ? -2.110  0.042   -72.525  1.00 18.97 ? 148 HIS B CB  1 
ATOM   2597 C CG  . HIS B 1 155 ? -3.534  -0.244  -72.882  1.00 21.69 ? 148 HIS B CG  1 
ATOM   2598 N ND1 . HIS B 1 155 ? -3.914  -1.251  -73.747  1.00 26.03 ? 148 HIS B ND1 1 
ATOM   2599 C CD2 . HIS B 1 155 ? -4.676  0.362   -72.489  1.00 26.22 ? 148 HIS B CD2 1 
ATOM   2600 C CE1 . HIS B 1 155 ? -5.230  -1.259  -73.856  1.00 26.11 ? 148 HIS B CE1 1 
ATOM   2601 N NE2 . HIS B 1 155 ? -5.714  -0.286  -73.108  1.00 25.27 ? 148 HIS B NE2 1 
ATOM   2602 N N   . ASN B 1 156 ? 0.925   -1.812  -71.416  1.00 13.60 ? 149 ASN B N   1 
ATOM   2603 C CA  . ASN B 1 156 ? 2.326   -1.589  -71.103  1.00 13.45 ? 149 ASN B CA  1 
ATOM   2604 C C   . ASN B 1 156 ? 3.041   -2.926  -71.230  1.00 14.16 ? 149 ASN B C   1 
ATOM   2605 O O   . ASN B 1 156 ? 2.409   -3.980  -71.369  1.00 12.78 ? 149 ASN B O   1 
ATOM   2606 C CB  . ASN B 1 156 ? 2.525   -0.928  -69.728  1.00 13.94 ? 149 ASN B CB  1 
ATOM   2607 C CG  . ASN B 1 156 ? 1.896   -1.711  -68.628  1.00 13.25 ? 149 ASN B CG  1 
ATOM   2608 O OD1 . ASN B 1 156 ? 2.208   -2.895  -68.452  1.00 14.37 ? 149 ASN B OD1 1 
ATOM   2609 N ND2 . ASN B 1 156 ? 1.027   -1.055  -67.851  1.00 14.95 ? 149 ASN B ND2 1 
ATOM   2610 N N   . PHE B 1 157 ? 4.369   -2.864  -71.253  1.00 13.17 ? 150 PHE B N   1 
ATOM   2611 C CA  . PHE B 1 157 ? 5.194   -4.062  -71.383  1.00 12.58 ? 150 PHE B CA  1 
ATOM   2612 C C   . PHE B 1 157 ? 6.594   -3.749  -70.873  1.00 13.68 ? 150 PHE B C   1 
ATOM   2613 O O   . PHE B 1 157 ? 7.022   -2.587  -70.839  1.00 14.03 ? 150 PHE B O   1 
ATOM   2614 C CB  . PHE B 1 157 ? 5.243   -4.598  -72.837  1.00 14.80 ? 150 PHE B CB  1 
ATOM   2615 C CG  . PHE B 1 157 ? 5.950   -3.703  -73.813  1.00 15.12 ? 150 PHE B CG  1 
ATOM   2616 C CD1 . PHE B 1 157 ? 7.284   -3.904  -74.120  1.00 14.92 ? 150 PHE B CD1 1 
ATOM   2617 C CD2 . PHE B 1 157 ? 5.261   -2.703  -74.493  1.00 20.51 ? 150 PHE B CD2 1 
ATOM   2618 C CE1 . PHE B 1 157 ? 7.942   -3.086  -75.028  1.00 16.81 ? 150 PHE B CE1 1 
ATOM   2619 C CE2 . PHE B 1 157 ? 5.904   -1.888  -75.423  1.00 22.09 ? 150 PHE B CE2 1 
ATOM   2620 C CZ  . PHE B 1 157 ? 7.242   -2.083  -75.704  1.00 19.75 ? 150 PHE B CZ  1 
ATOM   2621 N N   . PHE B 1 158 ? 7.324   -4.796  -70.496  1.00 14.03 ? 151 PHE B N   1 
ATOM   2622 C CA  . PHE B 1 158 ? 8.712   -4.617  -70.068  1.00 15.35 ? 151 PHE B CA  1 
ATOM   2623 C C   . PHE B 1 158 ? 9.646   -4.638  -71.274  1.00 14.42 ? 151 PHE B C   1 
ATOM   2624 O O   . PHE B 1 158 ? 9.621   -5.582  -72.089  1.00 17.30 ? 151 PHE B O   1 
ATOM   2625 C CB  . PHE B 1 158 ? 9.115   -5.690  -69.060  1.00 15.87 ? 151 PHE B CB  1 
ATOM   2626 C CG  . PHE B 1 158 ? 8.397   -5.579  -67.749  1.00 13.62 ? 151 PHE B CG  1 
ATOM   2627 C CD1 . PHE B 1 158 ? 8.884   -4.758  -66.727  1.00 16.01 ? 151 PHE B CD1 1 
ATOM   2628 C CD2 . PHE B 1 158 ? 7.232   -6.296  -67.520  1.00 17.40 ? 151 PHE B CD2 1 
ATOM   2629 C CE1 . PHE B 1 158 ? 8.203   -4.655  -65.505  1.00 16.45 ? 151 PHE B CE1 1 
ATOM   2630 C CE2 . PHE B 1 158 ? 6.558   -6.204  -66.314  1.00 18.43 ? 151 PHE B CE2 1 
ATOM   2631 C CZ  . PHE B 1 158 ? 7.049   -5.391  -65.303  1.00 18.43 ? 151 PHE B CZ  1 
ATOM   2632 N N   . GLY B 1 159 ? 10.450  -3.588  -71.416  1.00 14.62 ? 152 GLY B N   1 
ATOM   2633 C CA  . GLY B 1 159 ? 11.511  -3.547  -72.407  1.00 15.22 ? 152 GLY B CA  1 
ATOM   2634 C C   . GLY B 1 159 ? 12.838  -3.472  -71.692  1.00 14.64 ? 152 GLY B C   1 
ATOM   2635 O O   . GLY B 1 159 ? 13.064  -2.542  -70.904  1.00 15.62 ? 152 GLY B O   1 
ATOM   2636 N N   . ASN B 1 160 ? 13.693  -4.475  -71.886  1.00 15.87 ? 153 ASN B N   1 
ATOM   2637 C CA  . ASN B 1 160 ? 14.916  -4.607  -71.084  1.00 15.90 ? 153 ASN B CA  1 
ATOM   2638 C C   . ASN B 1 160 ? 14.621  -4.491  -69.588  1.00 17.12 ? 153 ASN B C   1 
ATOM   2639 O O   . ASN B 1 160 ? 15.340  -3.817  -68.848  1.00 15.63 ? 153 ASN B O   1 
ATOM   2640 C CB  . ASN B 1 160 ? 15.993  -3.601  -71.488  1.00 15.97 ? 153 ASN B CB  1 
ATOM   2641 C CG  . ASN B 1 160 ? 16.437  -3.769  -72.925  1.00 16.01 ? 153 ASN B CG  1 
ATOM   2642 O OD1 . ASN B 1 160 ? 16.430  -4.874  -73.472  1.00 17.40 ? 153 ASN B OD1 1 
ATOM   2643 N ND2 . ASN B 1 160 ? 16.809  -2.669  -73.561  1.00 21.58 ? 153 ASN B ND2 1 
ATOM   2644 N N   . ASP B 1 161 ? 13.533  -5.120  -69.151  1.00 15.48 ? 154 ASP B N   1 
ATOM   2645 C CA  . ASP B 1 161 ? 13.088  -5.189  -67.762  1.00 13.97 ? 154 ASP B CA  1 
ATOM   2646 C C   . ASP B 1 161 ? 12.518  -3.886  -67.220  1.00 16.24 ? 154 ASP B C   1 
ATOM   2647 O O   . ASP B 1 161 ? 12.170  -3.827  -66.024  1.00 17.13 ? 154 ASP B O   1 
ATOM   2648 C CB  . ASP B 1 161 ? 14.156  -5.750  -66.808  1.00 16.44 ? 154 ASP B CB  1 
ATOM   2649 C CG  . ASP B 1 161 ? 14.470  -7.209  -67.053  1.00 26.32 ? 154 ASP B CG  1 
ATOM   2650 O OD1 . ASP B 1 161 ? 13.705  -7.900  -67.743  1.00 28.57 ? 154 ASP B OD1 1 
ATOM   2651 O OD2 . ASP B 1 161 ? 15.499  -7.670  -66.522  1.00 31.64 ? 154 ASP B OD2 1 
ATOM   2652 N N   . ILE B 1 162 ? 12.356  -2.858  -68.044  1.00 14.60 ? 155 ILE B N   1 
ATOM   2653 C CA  . ILE B 1 162 ? 11.827  -1.569  -67.597  1.00 13.67 ? 155 ILE B CA  1 
ATOM   2654 C C   . ILE B 1 162 ? 10.444  -1.379  -68.222  1.00 13.51 ? 155 ILE B C   1 
ATOM   2655 O O   . ILE B 1 162 ? 10.266  -1.561  -69.433  1.00 14.17 ? 155 ILE B O   1 
ATOM   2656 C CB  . ILE B 1 162 ? 12.766  -0.431  -68.019  1.00 13.11 ? 155 ILE B CB  1 
ATOM   2657 C CG1 . ILE B 1 162 ? 14.113  -0.555  -67.279  1.00 15.72 ? 155 ILE B CG1 1 
ATOM   2658 C CG2 . ILE B 1 162 ? 12.103  0.924   -67.793  1.00 15.18 ? 155 ILE B CG2 1 
ATOM   2659 C CD1 . ILE B 1 162 ? 15.190  0.377   -67.788  1.00 20.06 ? 155 ILE B CD1 1 
ATOM   2660 N N   . LEU B 1 163 ? 9.458   -0.992  -67.424  1.00 14.11 ? 156 LEU B N   1 
ATOM   2661 C CA  . LEU B 1 163 ? 8.097   -0.916  -67.924  1.00 12.78 ? 156 LEU B CA  1 
ATOM   2662 C C   . LEU B 1 163 ? 7.889   0.331   -68.778  1.00 13.24 ? 156 LEU B C   1 
ATOM   2663 O O   . LEU B 1 163 ? 8.103   1.461   -68.304  1.00 14.87 ? 156 LEU B O   1 
ATOM   2664 C CB  . LEU B 1 163 ? 7.110   -0.942  -66.758  1.00 13.81 ? 156 LEU B CB  1 
ATOM   2665 C CG  . LEU B 1 163 ? 5.682   -1.267  -67.152  1.00 13.79 ? 156 LEU B CG  1 
ATOM   2666 C CD1 . LEU B 1 163 ? 5.525   -2.727  -67.544  1.00 16.71 ? 156 LEU B CD1 1 
ATOM   2667 C CD2 . LEU B 1 163 ? 4.741   -0.924  -65.980  1.00 14.73 ? 156 LEU B CD2 1 
ATOM   2668 N N   . VAL B 1 164 ? 7.442   0.137   -70.026  1.00 13.55 ? 157 VAL B N   1 
ATOM   2669 C CA  . VAL B 1 164 ? 7.135   1.238   -70.931  1.00 15.25 ? 157 VAL B CA  1 
ATOM   2670 C C   . VAL B 1 164 ? 5.677   1.141   -71.348  1.00 14.07 ? 157 VAL B C   1 
ATOM   2671 O O   . VAL B 1 164 ? 5.059   0.070   -71.312  1.00 15.58 ? 157 VAL B O   1 
ATOM   2672 C CB  . VAL B 1 164 ? 8.051   1.275   -72.170  1.00 15.95 ? 157 VAL B CB  1 
ATOM   2673 C CG1 . VAL B 1 164 ? 9.496   1.465   -71.739  1.00 17.62 ? 157 VAL B CG1 1 
ATOM   2674 C CG2 . VAL B 1 164 ? 7.894   0.029   -73.005  1.00 19.21 ? 157 VAL B CG2 1 
ATOM   2675 N N   . HIS B 1 165 ? 5.112   2.276   -71.756  1.00 15.25 ? 158 HIS B N   1 
ATOM   2676 C CA  . HIS B 1 165 ? 3.740   2.281   -72.241  1.00 16.27 ? 158 HIS B CA  1 
ATOM   2677 C C   . HIS B 1 165 ? 3.671   1.613   -73.615  1.00 16.57 ? 158 HIS B C   1 
ATOM   2678 O O   . HIS B 1 165 ? 4.600   1.715   -74.426  1.00 20.87 ? 158 HIS B O   1 
ATOM   2679 C CB  . HIS B 1 165 ? 3.236   3.720   -72.331  1.00 22.95 ? 158 HIS B CB  1 
ATOM   2680 C CG  . HIS B 1 165 ? 1.750   3.836   -72.492  1.00 25.21 ? 158 HIS B CG  1 
ATOM   2681 N ND1 . HIS B 1 165 ? 0.856   3.449   -71.517  1.00 24.98 ? 158 HIS B ND1 1 
ATOM   2682 C CD2 . HIS B 1 165 ? 1.004   4.295   -73.525  1.00 33.63 ? 158 HIS B CD2 1 
ATOM   2683 C CE1 . HIS B 1 165 ? -0.378  3.676   -71.938  1.00 27.16 ? 158 HIS B CE1 1 
ATOM   2684 N NE2 . HIS B 1 165 ? -0.315  4.180   -73.157  1.00 32.85 ? 158 HIS B NE2 1 
ATOM   2685 N N   . ALA B 1 166 ? 2.586   0.886   -73.869  1.00 16.73 ? 159 ALA B N   1 
ATOM   2686 C CA  . ALA B 1 166 ? 2.371   0.248   -75.158  1.00 19.53 ? 159 ALA B CA  1 
ATOM   2687 C C   . ALA B 1 166 ? 1.531   1.162   -76.044  1.00 23.90 ? 159 ALA B C   1 
ATOM   2688 O O   . ALA B 1 166 ? 0.901   2.115   -75.580  1.00 31.48 ? 159 ALA B O   1 
ATOM   2689 C CB  . ALA B 1 166 ? 1.709   -1.116  -74.961  1.00 21.49 ? 159 ALA B CB  1 
ATOM   2690 N N   . SER B 1 167 ? 1.511   0.867   -77.329  1.00 27.51 ? 160 SER B N   1 
ATOM   2691 C CA  . SER B 1 167 ? 0.587   1.603   -78.168  1.00 31.23 ? 160 SER B CA  1 
ATOM   2692 C C   . SER B 1 167 ? -0.751  0.887   -78.154  1.00 28.37 ? 160 SER B C   1 
ATOM   2693 O O   . SER B 1 167 ? -0.842  -0.307  -77.871  1.00 37.09 ? 160 SER B O   1 
ATOM   2694 C CB  . SER B 1 167 ? 1.108   1.699   -79.603  1.00 43.88 ? 160 SER B CB  1 
ATOM   2695 O OG  . SER B 1 167 ? 0.514   0.719   -80.443  1.00 53.53 ? 160 SER B OG  1 
ATOM   2696 N N   . VAL B 1 168 ? -1.794  1.611   -78.508  1.00 37.92 ? 161 VAL B N   1 
ATOM   2697 C CA  . VAL B 1 168 ? -3.042  0.966   -78.865  1.00 39.92 ? 161 VAL B CA  1 
ATOM   2698 C C   . VAL B 1 168 ? -3.274  1.265   -80.330  1.00 37.95 ? 161 VAL B C   1 
ATOM   2699 O O   . VAL B 1 168 ? -3.070  2.398   -80.777  1.00 37.74 ? 161 VAL B O   1 
ATOM   2700 C CB  . VAL B 1 168 ? -4.222  1.432   -77.990  1.00 42.48 ? 161 VAL B CB  1 
ATOM   2701 C CG1 . VAL B 1 168 ? -5.511  0.750   -78.427  1.00 46.97 ? 161 VAL B CG1 1 
ATOM   2702 C CG2 . VAL B 1 168 ? -3.940  1.133   -76.520  1.00 42.51 ? 161 VAL B CG2 1 
ATOM   2703 N N   . TYR B 1 169 ? -3.620  0.234   -81.084  1.00 40.38 ? 162 TYR B N   1 
ATOM   2704 C CA  . TYR B 1 169 ? -4.067  0.397   -82.449  1.00 42.52 ? 162 TYR B CA  1 
ATOM   2705 C C   . TYR B 1 169 ? -5.574  0.412   -82.328  1.00 51.38 ? 162 TYR B C   1 
ATOM   2706 O O   . TYR B 1 169 ? -6.177  -0.585  -81.911  1.00 57.82 ? 162 TYR B O   1 
ATOM   2707 C CB  . TYR B 1 169 ? -3.637  -0.783  -83.325  1.00 33.22 ? 162 TYR B CB  1 
ATOM   2708 C CG  . TYR B 1 169 ? -4.152  -0.718  -84.750  1.00 40.31 ? 162 TYR B CG  1 
ATOM   2709 C CD1 . TYR B 1 169 ? -5.398  -1.230  -85.096  1.00 42.89 ? 162 TYR B CD1 1 
ATOM   2710 C CD2 . TYR B 1 169 ? -3.383  -0.143  -85.752  1.00 44.15 ? 162 TYR B CD2 1 
ATOM   2711 C CE1 . TYR B 1 169 ? -5.862  -1.163  -86.409  1.00 44.42 ? 162 TYR B CE1 1 
ATOM   2712 C CE2 . TYR B 1 169 ? -3.831  -0.074  -87.053  1.00 42.49 ? 162 TYR B CE2 1 
ATOM   2713 C CZ  . TYR B 1 169 ? -5.070  -0.585  -87.382  1.00 38.92 ? 162 TYR B CZ  1 
ATOM   2714 O OH  . TYR B 1 169 ? -5.513  -0.506  -88.687  1.00 45.30 ? 162 TYR B OH  1 
ATOM   2715 N N   . LEU B 1 170 ? -6.181  1.537   -82.648  1.00 42.91 ? 163 LEU B N   1 
ATOM   2716 C CA  . LEU B 1 170 ? -7.629  1.587   -82.672  1.00 47.05 ? 163 LEU B CA  1 
ATOM   2717 C C   . LEU B 1 170 ? -8.036  1.126   -84.063  1.00 54.66 ? 163 LEU B C   1 
ATOM   2718 O O   . LEU B 1 170 ? -7.729  1.789   -85.060  1.00 57.69 ? 163 LEU B O   1 
ATOM   2719 C CB  . LEU B 1 170 ? -8.132  2.989   -82.351  1.00 51.44 ? 163 LEU B CB  1 
ATOM   2720 C CG  . LEU B 1 170 ? -9.455  2.974   -81.582  1.00 55.74 ? 163 LEU B CG  1 
ATOM   2721 C CD1 . LEU B 1 170 ? -9.516  1.770   -80.645  1.00 56.81 ? 163 LEU B CD1 1 
ATOM   2722 C CD2 . LEU B 1 170 ? -9.632  4.272   -80.805  1.00 56.91 ? 163 LEU B CD2 1 
ATOM   2723 N N   . ASN B 1 171 ? -8.690  -0.034  -84.131  1.00 56.32 ? 164 ASN B N   1 
ATOM   2724 C CA  . ASN B 1 171 ? -9.174  -0.574  -85.398  1.00 59.59 ? 164 ASN B CA  1 
ATOM   2725 C C   . ASN B 1 171 ? -10.412 0.226   -85.774  1.00 56.54 ? 164 ASN B C   1 
ATOM   2726 O O   . ASN B 1 171 ? -11.555 -0.173  -85.534  1.00 61.34 ? 164 ASN B O   1 
ATOM   2727 C CB  . ASN B 1 171 ? -9.469  -2.062  -85.279  1.00 61.45 ? 164 ASN B CB  1 
ATOM   2728 C CG  . ASN B 1 171 ? -9.970  -2.655  -86.575  1.00 62.36 ? 164 ASN B CG  1 
ATOM   2729 O OD1 . ASN B 1 171 ? -9.799  -2.068  -87.644  1.00 58.33 ? 164 ASN B OD1 1 
ATOM   2730 N ND2 . ASN B 1 171 ? -10.581 -3.829  -86.493  1.00 63.99 ? 164 ASN B ND2 1 
ATOM   2731 N N   . LYS B 1 172 ? -10.166 1.396   -86.363  1.00 48.90 ? 165 LYS B N   1 
ATOM   2732 C CA  . LYS B 1 172 ? -11.253 2.326   -86.629  1.00 45.90 ? 165 LYS B CA  1 
ATOM   2733 C C   . LYS B 1 172 ? -12.156 1.812   -87.742  1.00 39.92 ? 165 LYS B C   1 
ATOM   2734 O O   . LYS B 1 172 ? -13.381 1.769   -87.590  1.00 38.66 ? 165 LYS B O   1 
ATOM   2735 C CB  . LYS B 1 172 ? -10.686 3.700   -86.990  1.00 42.02 ? 165 LYS B CB  1 
ATOM   2736 C CG  . LYS B 1 172 ? -9.852  4.353   -85.895  1.00 44.02 ? 165 LYS B CG  1 
ATOM   2737 C CD  . LYS B 1 172 ? -9.395  5.734   -86.334  1.00 46.30 ? 165 LYS B CD  1 
ATOM   2738 C CE  . LYS B 1 172 ? -8.476  6.373   -85.307  1.00 49.21 ? 165 LYS B CE  1 
ATOM   2739 N NZ  . LYS B 1 172 ? -7.926  7.668   -85.803  1.00 51.31 ? 165 LYS B NZ  1 
ATOM   2740 N N   . LEU B 1 173 ? -11.567 1.410   -88.866  1.00 48.21 ? 166 LEU B N   1 
ATOM   2741 C CA  . LEU B 1 173 ? -12.348 1.087   -90.056  1.00 48.51 ? 166 LEU B CA  1 
ATOM   2742 C C   . LEU B 1 173 ? -12.053 -0.289  -90.660  1.00 53.19 ? 166 LEU B C   1 
ATOM   2743 O O   . LEU B 1 173 ? -11.493 -1.170  -90.009  1.00 53.30 ? 166 LEU B O   1 
ATOM   2744 C CB  . LEU B 1 173 ? -12.189 2.192   -91.107  1.00 52.88 ? 166 LEU B CB  1 
ATOM   2745 C CG  . LEU B 1 173 ? -12.616 3.587   -90.631  1.00 52.18 ? 166 LEU B CG  1 
ATOM   2746 C CD1 . LEU B 1 173 ? -12.259 4.674   -91.630  1.00 56.78 ? 166 LEU B CD1 1 
ATOM   2747 C CD2 . LEU B 1 173 ? -14.100 3.606   -90.337  1.00 49.98 ? 166 LEU B CD2 1 
HETATM 2748 O O   . HOH C 2 .   ? -1.581  11.433  -53.837  1.00 77.44 ? 201 HOH A O   1 
HETATM 2749 O O   . HOH C 2 .   ? -9.635  -0.491  -22.272  1.00 65.98 ? 202 HOH A O   1 
HETATM 2750 O O   . HOH C 2 .   ? 6.349   -14.429 -32.915  1.00 72.09 ? 203 HOH A O   1 
HETATM 2751 O O   . HOH C 2 .   ? -6.617  21.964  -35.410  1.00 28.10 ? 204 HOH A O   1 
HETATM 2752 O O   . HOH C 2 .   ? -6.427  8.925   -38.050  1.00 25.37 ? 205 HOH A O   1 
HETATM 2753 O O   . HOH C 2 .   ? -14.230 2.869   -34.225  1.00 24.24 ? 206 HOH A O   1 
HETATM 2754 O O   . HOH C 2 .   ? 4.536   5.231   -53.201  1.00 35.20 ? 207 HOH A O   1 
HETATM 2755 O O   . HOH C 2 .   ? 2.280   3.407   -22.530  1.00 38.70 ? 208 HOH A O   1 
HETATM 2756 O O   . HOH C 2 .   ? -17.514 9.720   -48.400  1.00 39.26 ? 209 HOH A O   1 
HETATM 2757 O O   . HOH C 2 .   ? -3.993  9.462   -37.656  1.00 24.89 ? 210 HOH A O   1 
HETATM 2758 O O   . HOH C 2 .   ? -3.562  -0.161  -44.336  1.00 18.64 ? 211 HOH A O   1 
HETATM 2759 O O   . HOH C 2 .   ? 9.146   -5.511  -36.896  1.00 89.40 ? 212 HOH A O   1 
HETATM 2760 O O   . HOH C 2 .   ? 3.300   0.873   -25.977  1.00 24.47 ? 213 HOH A O   1 
HETATM 2761 O O   . HOH C 2 .   ? -8.409  -11.673 -41.051  1.00 34.47 ? 214 HOH A O   1 
HETATM 2762 O O   . HOH C 2 .   ? -5.755  -9.670  -52.363  1.00 26.72 ? 215 HOH A O   1 
HETATM 2763 O O   . HOH C 2 .   ? -4.396  -0.839  -35.221  1.00 82.49 ? 216 HOH A O   1 
HETATM 2764 O O   . HOH C 2 .   ? -0.192  -0.247  -55.838  1.00 33.18 ? 217 HOH A O   1 
HETATM 2765 O O   . HOH C 2 .   ? 6.000   -0.624  -49.494  1.00 22.69 ? 218 HOH A O   1 
HETATM 2766 O O   . HOH C 2 .   ? 8.023   -2.335  -46.935  1.00 40.04 ? 219 HOH A O   1 
HETATM 2767 O O   . HOH C 2 .   ? -19.421 11.249  -32.525  1.00 38.49 ? 220 HOH A O   1 
HETATM 2768 O O   . HOH C 2 .   ? -5.124  5.815   -16.874  1.00 28.62 ? 221 HOH A O   1 
HETATM 2769 O O   . HOH C 2 .   ? -7.671  11.767  -11.945  1.00 30.75 ? 222 HOH A O   1 
HETATM 2770 O O   . HOH C 2 .   ? -13.903 0.078   -50.607  1.00 29.98 ? 223 HOH A O   1 
HETATM 2771 O O   . HOH C 2 .   ? -11.648 11.355  -12.796  1.00 22.75 ? 224 HOH A O   1 
HETATM 2772 O O   . HOH C 2 .   ? -0.256  5.974   -20.768  1.00 30.72 ? 225 HOH A O   1 
HETATM 2773 O O   . HOH C 2 .   ? 3.718   1.284   -54.962  1.00 32.31 ? 226 HOH A O   1 
HETATM 2774 O O   . HOH C 2 .   ? -4.867  8.905   -17.298  1.00 32.27 ? 227 HOH A O   1 
HETATM 2775 O O   . HOH C 2 .   ? -14.147 14.225  -29.654  1.00 30.44 ? 228 HOH A O   1 
HETATM 2776 O O   . HOH C 2 .   ? -0.409  -12.546 -43.054  1.00 26.10 ? 229 HOH A O   1 
HETATM 2777 O O   . HOH C 2 .   ? 1.516   2.879   -54.158  1.00 25.51 ? 230 HOH A O   1 
HETATM 2778 O O   . HOH C 2 .   ? 6.790   8.004   -31.796  1.00 30.81 ? 231 HOH A O   1 
HETATM 2779 O O   . HOH C 2 .   ? -2.160  18.674  -40.388  1.00 26.62 ? 232 HOH A O   1 
HETATM 2780 O O   . HOH C 2 .   ? -17.670 0.024   -18.075  1.00 26.80 ? 233 HOH A O   1 
HETATM 2781 O O   . HOH C 2 .   ? 8.941   7.079   -46.158  1.00 34.75 ? 234 HOH A O   1 
HETATM 2782 O O   . HOH C 2 .   ? -13.762 2.352   -28.428  1.00 70.73 ? 235 HOH A O   1 
HETATM 2783 O O   . HOH C 2 .   ? -17.946 10.170  -26.727  1.00 36.98 ? 236 HOH A O   1 
HETATM 2784 O O   . HOH C 2 .   ? -19.356 6.754   -42.318  1.00 35.40 ? 237 HOH A O   1 
HETATM 2785 O O   . HOH C 2 .   ? -13.839 9.099   -14.106  1.00 17.76 ? 238 HOH A O   1 
HETATM 2786 O O   . HOH C 2 .   ? 8.880   0.615   -43.530  1.00 25.26 ? 239 HOH A O   1 
HETATM 2787 O O   . HOH C 2 .   ? 4.664   8.002   -26.457  1.00 27.89 ? 240 HOH A O   1 
HETATM 2788 O O   . HOH C 2 .   ? 0.644   13.896  -23.233  1.00 29.65 ? 241 HOH A O   1 
HETATM 2789 O O   . HOH C 2 .   ? 3.476   1.683   -34.399  1.00 18.48 ? 242 HOH A O   1 
HETATM 2790 O O   . HOH C 2 .   ? 1.550   16.922  -30.005  1.00 32.67 ? 243 HOH A O   1 
HETATM 2791 O O   . HOH C 2 .   ? 2.040   10.005  -39.154  1.00 29.20 ? 244 HOH A O   1 
HETATM 2792 O O   . HOH C 2 .   ? -9.872  -0.173  -10.761  1.00 30.14 ? 245 HOH A O   1 
HETATM 2793 O O   . HOH C 2 .   ? -10.278 11.059  -50.358  1.00 32.10 ? 246 HOH A O   1 
HETATM 2794 O O   . HOH C 2 .   ? -8.654  14.389  -25.287  1.00 23.42 ? 247 HOH A O   1 
HETATM 2795 O O   . HOH C 2 .   ? -0.328  8.852   -38.606  1.00 18.88 ? 248 HOH A O   1 
HETATM 2796 O O   . HOH C 2 .   ? -17.806 12.751  -36.791  1.00 26.56 ? 249 HOH A O   1 
HETATM 2797 O O   . HOH C 2 .   ? 5.065   13.411  -30.361  1.00 35.42 ? 250 HOH A O   1 
HETATM 2798 O O   . HOH C 2 .   ? 2.369   11.723  -22.250  1.00 39.96 ? 251 HOH A O   1 
HETATM 2799 O O   . HOH C 2 .   ? -5.326  -4.613  -53.969  1.00 31.02 ? 252 HOH A O   1 
HETATM 2800 O O   . HOH C 2 .   ? -6.578  -8.030  -54.230  1.00 32.33 ? 253 HOH A O   1 
HETATM 2801 O O   . HOH C 2 .   ? -26.571 3.095   -24.380  1.00 44.40 ? 254 HOH A O   1 
HETATM 2802 O O   . HOH C 2 .   ? -22.565 9.357   -34.889  1.00 38.96 ? 255 HOH A O   1 
HETATM 2803 O O   . HOH C 2 .   ? 9.076   -11.776 -39.518  1.00 30.08 ? 256 HOH A O   1 
HETATM 2804 O O   . HOH C 2 .   ? -18.337 -0.387  -46.791  1.00 32.87 ? 257 HOH A O   1 
HETATM 2805 O O   . HOH C 2 .   ? -9.499  17.174  -42.899  1.00 28.84 ? 258 HOH A O   1 
HETATM 2806 O O   . HOH C 2 .   ? -16.420 3.175   -43.403  1.00 33.35 ? 259 HOH A O   1 
HETATM 2807 O O   . HOH C 2 .   ? 8.898   0.200   -46.275  1.00 26.06 ? 260 HOH A O   1 
HETATM 2808 O O   . HOH C 2 .   ? 6.015   4.990   -33.910  1.00 24.96 ? 261 HOH A O   1 
HETATM 2809 O O   . HOH C 2 .   ? -13.905 15.283  -43.931  1.00 36.34 ? 262 HOH A O   1 
HETATM 2810 O O   . HOH C 2 .   ? -13.696 -2.512  -41.613  1.00 40.70 ? 263 HOH A O   1 
HETATM 2811 O O   . HOH C 2 .   ? -11.246 14.946  -24.459  1.00 29.14 ? 264 HOH A O   1 
HETATM 2812 O O   . HOH C 2 .   ? -7.999  14.424  -15.692  1.00 39.38 ? 265 HOH A O   1 
HETATM 2813 O O   . HOH C 2 .   ? -17.333 9.092   -16.424  1.00 29.39 ? 266 HOH A O   1 
HETATM 2814 O O   . HOH C 2 .   ? 2.528   -6.509  -50.699  1.00 33.63 ? 267 HOH A O   1 
HETATM 2815 O O   . HOH C 2 .   ? -3.193  3.936   -17.185  1.00 34.84 ? 268 HOH A O   1 
HETATM 2816 O O   . HOH C 2 .   ? -1.278  -13.124 -29.019  1.00 47.17 ? 269 HOH A O   1 
HETATM 2817 O O   . HOH C 2 .   ? -7.649  -11.644 -52.947  1.00 37.96 ? 270 HOH A O   1 
HETATM 2818 O O   . HOH C 2 .   ? -13.005 0.215   -40.953  1.00 24.75 ? 271 HOH A O   1 
HETATM 2819 O O   . HOH C 2 .   ? -2.846  2.141   -57.018  1.00 36.80 ? 272 HOH A O   1 
HETATM 2820 O O   . HOH C 2 .   ? 4.809   8.679   -38.161  1.00 39.26 ? 273 HOH A O   1 
HETATM 2821 O O   . HOH C 2 .   ? 7.131   4.802   -39.154  1.00 23.79 ? 274 HOH A O   1 
HETATM 2822 O O   . HOH C 2 .   ? -1.760  11.457  -17.522  1.00 43.05 ? 275 HOH A O   1 
HETATM 2823 O O   . HOH C 2 .   ? -2.203  12.386  -41.732  1.00 54.86 ? 276 HOH A O   1 
HETATM 2824 O O   . HOH C 2 .   ? -19.664 9.695   -28.381  1.00 40.08 ? 277 HOH A O   1 
HETATM 2825 O O   . HOH C 2 .   ? -5.998  5.563   -14.215  1.00 33.57 ? 278 HOH A O   1 
HETATM 2826 O O   . HOH C 2 .   ? -2.090  10.733  -39.290  1.00 30.59 ? 279 HOH A O   1 
HETATM 2827 O O   . HOH C 2 .   ? 6.071   2.284   -33.429  1.00 27.50 ? 280 HOH A O   1 
HETATM 2828 O O   . HOH C 2 .   ? 6.901   10.881  -31.374  1.00 43.28 ? 281 HOH A O   1 
HETATM 2829 O O   . HOH D 2 .   ? 2.891   0.910   -88.000  1.00 75.21 ? 201 HOH B O   1 
HETATM 2830 O O   . HOH D 2 .   ? 15.775  0.272   -84.079  1.00 24.85 ? 202 HOH B O   1 
HETATM 2831 O O   . HOH D 2 .   ? -7.889  -0.721  -89.423  1.00 37.15 ? 203 HOH B O   1 
HETATM 2832 O O   . HOH D 2 .   ? 7.481   -5.440  -92.887  1.00 27.42 ? 204 HOH B O   1 
HETATM 2833 O O   . HOH D 2 .   ? 17.029  5.300   -54.503  1.00 34.36 ? 205 HOH B O   1 
HETATM 2834 O O   . HOH D 2 .   ? 0.426   13.103  -59.528  1.00 37.44 ? 206 HOH B O   1 
HETATM 2835 O O   . HOH D 2 .   ? 7.522   -17.170 -87.809  1.00 40.45 ? 207 HOH B O   1 
HETATM 2836 O O   . HOH D 2 .   ? 20.488  -0.304  -74.770  1.00 33.43 ? 208 HOH B O   1 
HETATM 2837 O O   . HOH D 2 .   ? 17.102  -12.892 -79.183  1.00 35.07 ? 209 HOH B O   1 
HETATM 2838 O O   . HOH D 2 .   ? -1.548  -1.561  -75.678  1.00 20.46 ? 210 HOH B O   1 
HETATM 2839 O O   . HOH D 2 .   ? 9.871   -18.267 -69.286  1.00 26.39 ? 211 HOH B O   1 
HETATM 2840 O O   . HOH D 2 .   ? 10.842  -8.027  -91.530  1.00 33.60 ? 212 HOH B O   1 
HETATM 2841 O O   . HOH D 2 .   ? 18.314  -12.507 -84.773  1.00 27.17 ? 213 HOH B O   1 
HETATM 2842 O O   . HOH D 2 .   ? 9.234   2.125   -65.864  1.00 17.80 ? 214 HOH B O   1 
HETATM 2843 O O   . HOH D 2 .   ? 10.303  -13.806 -69.337  1.00 43.56 ? 215 HOH B O   1 
HETATM 2844 O O   . HOH D 2 .   ? 1.596   -17.389 -73.533  1.00 29.60 ? 216 HOH B O   1 
HETATM 2845 O O   . HOH D 2 .   ? -5.050  -7.495  -61.153  1.00 26.18 ? 217 HOH B O   1 
HETATM 2846 O O   . HOH D 2 .   ? -8.053  -2.001  -69.565  1.00 30.07 ? 218 HOH B O   1 
HETATM 2847 O O   . HOH D 2 .   ? -1.589  -12.868 -79.685  1.00 21.43 ? 219 HOH B O   1 
HETATM 2848 O O   . HOH D 2 .   ? 9.536   1.202   -97.024  1.00 31.10 ? 220 HOH B O   1 
HETATM 2849 O O   . HOH D 2 .   ? -1.199  2.557   -59.723  1.00 32.17 ? 221 HOH B O   1 
HETATM 2850 O O   . HOH D 2 .   ? -3.978  -15.323 -73.094  1.00 30.01 ? 222 HOH B O   1 
HETATM 2851 O O   . HOH D 2 .   ? 0.704   -12.370 -88.107  1.00 25.59 ? 223 HOH B O   1 
HETATM 2852 O O   . HOH D 2 .   ? 8.214   7.242   -99.742  1.00 36.80 ? 224 HOH B O   1 
HETATM 2853 O O   . HOH D 2 .   ? 7.135   12.267  -58.469  1.00 23.48 ? 225 HOH B O   1 
HETATM 2854 O O   . HOH D 2 .   ? 23.361  9.641   -80.076  1.00 43.60 ? 226 HOH B O   1 
HETATM 2855 O O   . HOH D 2 .   ? 2.590   -3.004  -57.431  1.00 31.36 ? 227 HOH B O   1 
HETATM 2856 O O   . HOH D 2 .   ? -2.487  4.018   -55.085  1.00 22.01 ? 228 HOH B O   1 
HETATM 2857 O O   . HOH D 2 .   ? 21.661  11.845  -82.470  1.00 34.16 ? 229 HOH B O   1 
HETATM 2858 O O   . HOH D 2 .   ? 12.949  14.254  -67.232  1.00 36.76 ? 230 HOH B O   1 
HETATM 2859 O O   . HOH D 2 .   ? -8.907  1.831   -89.310  1.00 37.55 ? 231 HOH B O   1 
HETATM 2860 O O   . HOH D 2 .   ? 10.323  13.616  -73.963  1.00 37.06 ? 232 HOH B O   1 
HETATM 2861 O O   . HOH D 2 .   ? 12.484  -5.249  -89.154  1.00 26.47 ? 233 HOH B O   1 
HETATM 2862 O O   . HOH D 2 .   ? 8.227   -7.919  -71.833  1.00 23.11 ? 234 HOH B O   1 
HETATM 2863 O O   . HOH D 2 .   ? 18.649  2.921   -60.633  1.00 25.72 ? 235 HOH B O   1 
HETATM 2864 O O   . HOH D 2 .   ? 7.058   -3.566  -55.425  1.00 26.27 ? 236 HOH B O   1 
HETATM 2865 O O   . HOH D 2 .   ? 17.843  -3.415  -58.438  1.00 33.22 ? 237 HOH B O   1 
HETATM 2866 O O   . HOH D 2 .   ? -3.605  -5.650  -55.755  1.00 27.41 ? 238 HOH B O   1 
HETATM 2867 O O   . HOH D 2 .   ? 7.345   7.975   -56.822  1.00 26.34 ? 239 HOH B O   1 
HETATM 2868 O O   . HOH D 2 .   ? 17.209  -7.068  -83.180  1.00 22.71 ? 240 HOH B O   1 
HETATM 2869 O O   . HOH D 2 .   ? 7.538   9.627   -87.881  1.00 42.85 ? 241 HOH B O   1 
HETATM 2870 O O   . HOH D 2 .   ? 4.616   7.306   -55.125  1.00 26.12 ? 242 HOH B O   1 
HETATM 2871 O O   . HOH D 2 .   ? 15.345  -10.269 -86.860  1.00 30.75 ? 243 HOH B O   1 
HETATM 2872 O O   . HOH D 2 .   ? -6.596  -10.166 -76.997  1.00 27.12 ? 244 HOH B O   1 
HETATM 2873 O O   . HOH D 2 .   ? 0.237   10.411  -60.301  1.00 28.71 ? 245 HOH B O   1 
HETATM 2874 O O   . HOH D 2 .   ? 20.604  4.633   -63.536  1.00 30.47 ? 246 HOH B O   1 
HETATM 2875 O O   . HOH D 2 .   ? 1.518   -14.138 -84.829  1.00 33.05 ? 247 HOH B O   1 
HETATM 2876 O O   . HOH D 2 .   ? 12.971  -13.307 -86.090  1.00 26.96 ? 248 HOH B O   1 
HETATM 2877 O O   . HOH D 2 .   ? 9.580   11.043  -87.775  1.00 33.50 ? 249 HOH B O   1 
HETATM 2878 O O   . HOH D 2 .   ? 4.099   -13.506 -83.959  1.00 22.00 ? 250 HOH B O   1 
HETATM 2879 O O   . HOH D 2 .   ? 23.515  -4.688  -67.353  1.00 26.34 ? 251 HOH B O   1 
HETATM 2880 O O   . HOH D 2 .   ? 16.060  -0.148  -75.694  1.00 18.55 ? 252 HOH B O   1 
HETATM 2881 O O   . HOH D 2 .   ? -2.808  5.113   -62.366  1.00 28.27 ? 253 HOH B O   1 
HETATM 2882 O O   . HOH D 2 .   ? -7.639  -10.655 -84.056  1.00 36.07 ? 254 HOH B O   1 
HETATM 2883 O O   . HOH D 2 .   ? 21.657  1.408   -66.673  1.00 24.97 ? 255 HOH B O   1 
HETATM 2884 O O   . HOH D 2 .   ? 21.696  -4.867  -63.413  1.00 27.64 ? 256 HOH B O   1 
HETATM 2885 O O   . HOH D 2 .   ? -2.154  7.584   -54.792  1.00 25.29 ? 257 HOH B O   1 
HETATM 2886 O O   . HOH D 2 .   ? 1.124   -11.455 -96.775  1.00 27.61 ? 258 HOH B O   1 
HETATM 2887 O O   . HOH D 2 .   ? 19.393  -6.749  -77.925  1.00 28.99 ? 259 HOH B O   1 
HETATM 2888 O O   . HOH D 2 .   ? 21.375  14.055  -71.744  1.00 31.70 ? 260 HOH B O   1 
HETATM 2889 O O   . HOH D 2 .   ? -4.493  -8.966  -93.055  1.00 22.04 ? 261 HOH B O   1 
HETATM 2890 O O   . HOH D 2 .   ? 21.690  1.953   -63.943  1.00 22.94 ? 262 HOH B O   1 
HETATM 2891 O O   . HOH D 2 .   ? 14.759  -16.401 -73.911  1.00 30.37 ? 263 HOH B O   1 
HETATM 2892 O O   . HOH D 2 .   ? 12.305  -7.174  -70.941  1.00 18.56 ? 264 HOH B O   1 
HETATM 2893 O O   . HOH D 2 .   ? 18.677  12.119  -65.440  1.00 35.90 ? 265 HOH B O   1 
HETATM 2894 O O   . HOH D 2 .   ? 2.455   -9.120  -59.206  1.00 27.03 ? 266 HOH B O   1 
HETATM 2895 O O   . HOH D 2 .   ? -5.641  2.369   -63.479  1.00 27.33 ? 267 HOH B O   1 
HETATM 2896 O O   . HOH D 2 .   ? 14.705  -8.427  -70.384  1.00 28.22 ? 268 HOH B O   1 
HETATM 2897 O O   . HOH D 2 .   ? 25.022  4.838   -64.745  1.00 35.09 ? 269 HOH B O   1 
HETATM 2898 O O   . HOH D 2 .   ? -4.121  -14.353 -80.921  1.00 36.94 ? 270 HOH B O   1 
HETATM 2899 O O   . HOH D 2 .   ? -4.044  -11.232 -62.234  1.00 41.52 ? 271 HOH B O   1 
HETATM 2900 O O   . HOH D 2 .   ? -0.707  -13.525 -65.338  1.00 32.60 ? 272 HOH B O   1 
HETATM 2901 O O   . HOH D 2 .   ? -1.032  4.147   -68.300  1.00 29.41 ? 273 HOH B O   1 
HETATM 2902 O O   . HOH D 2 .   ? -5.107  -10.877 -72.553  1.00 23.63 ? 274 HOH B O   1 
HETATM 2903 O O   . HOH D 2 .   ? -7.387  -3.572  -74.256  1.00 28.54 ? 275 HOH B O   1 
HETATM 2904 O O   . HOH D 2 .   ? -4.409  -11.109 -79.828  1.00 34.04 ? 276 HOH B O   1 
HETATM 2905 O O   . HOH D 2 .   ? 7.266   -16.815 -78.311  1.00 29.43 ? 277 HOH B O   1 
HETATM 2906 O O   . HOH D 2 .   ? 19.565  9.181   -60.727  1.00 40.37 ? 278 HOH B O   1 
HETATM 2907 O O   . HOH D 2 .   ? 7.067   1.521   -78.055  1.00 68.85 ? 279 HOH B O   1 
HETATM 2908 O O   . HOH D 2 .   ? 16.416  3.501   -56.418  1.00 29.56 ? 280 HOH B O   1 
HETATM 2909 O O   . HOH D 2 .   ? 11.498  14.348  -81.786  1.00 35.98 ? 281 HOH B O   1 
HETATM 2910 O O   . HOH D 2 .   ? -3.622  -1.458  -66.495  1.00 30.68 ? 282 HOH B O   1 
HETATM 2911 O O   . HOH D 2 .   ? 0.191   2.230   -57.544  1.00 33.55 ? 283 HOH B O   1 
HETATM 2912 O O   . HOH D 2 .   ? 20.274  15.994  -82.679  1.00 33.39 ? 284 HOH B O   1 
HETATM 2913 O O   . HOH D 2 .   ? -0.236  1.378   -69.098  1.00 20.16 ? 285 HOH B O   1 
HETATM 2914 O O   . HOH D 2 .   ? 4.738   -14.128 -93.635  1.00 34.87 ? 286 HOH B O   1 
HETATM 2915 O O   . HOH D 2 .   ? 11.963  -15.471 -70.084  1.00 35.66 ? 287 HOH B O   1 
HETATM 2916 O O   . HOH D 2 .   ? -1.874  4.663   -65.908  1.00 29.33 ? 288 HOH B O   1 
HETATM 2917 O O   . HOH D 2 .   ? 1.249   14.073  -62.457  1.00 39.41 ? 289 HOH B O   1 
HETATM 2918 O O   . HOH D 2 .   ? -2.517  -15.250 -77.185  1.00 33.43 ? 290 HOH B O   1 
HETATM 2919 O O   . HOH D 2 .   ? 19.819  -2.823  -70.743  1.00 24.25 ? 291 HOH B O   1 
HETATM 2920 O O   . HOH D 2 .   ? 6.074   10.731  -56.491  1.00 26.95 ? 292 HOH B O   1 
HETATM 2921 O O   . HOH D 2 .   ? 10.349  -0.897  -54.696  1.00 24.85 ? 293 HOH B O   1 
HETATM 2922 O O   . HOH D 2 .   ? 18.562  -3.381  -75.884  1.00 29.71 ? 294 HOH B O   1 
HETATM 2923 O O   . HOH D 2 .   ? 3.350   -15.912 -66.470  1.00 34.43 ? 295 HOH B O   1 
HETATM 2924 O O   . HOH D 2 .   ? 17.692  -6.842  -71.555  1.00 44.99 ? 296 HOH B O   1 
HETATM 2925 O O   . HOH D 2 .   ? 15.377  9.109   -59.913  1.00 31.15 ? 297 HOH B O   1 
HETATM 2926 O O   . HOH D 2 .   ? 13.159  3.740   -54.398  1.00 32.49 ? 298 HOH B O   1 
HETATM 2927 O O   . HOH D 2 .   ? 17.969  -1.013  -82.117  1.00 33.67 ? 299 HOH B O   1 
HETATM 2928 O O   . HOH D 2 .   ? 16.653  -10.473 -77.096  1.00 84.73 ? 300 HOH B O   1 
HETATM 2929 O O   . HOH D 2 .   ? 21.682  -6.198  -69.012  1.00 42.71 ? 301 HOH B O   1 
HETATM 2930 O O   . HOH D 2 .   ? 5.682   -18.013 -84.173  1.00 38.81 ? 302 HOH B O   1 
HETATM 2931 O O   . HOH D 2 .   ? 12.023  -7.081  -55.411  1.00 64.67 ? 303 HOH B O   1 
HETATM 2932 O O   . HOH D 2 .   ? 12.296  -13.819 -88.812  1.00 31.85 ? 304 HOH B O   1 
HETATM 2933 O O   . HOH D 2 .   ? 16.134  18.772  -76.094  1.00 49.24 ? 305 HOH B O   1 
HETATM 2934 O O   . HOH D 2 .   ? 10.251  -8.976  -70.138  1.00 24.91 ? 306 HOH B O   1 
HETATM 2935 O O   . HOH D 2 .   ? 7.558   -16.150 -80.983  1.00 34.06 ? 307 HOH B O   1 
HETATM 2936 O O   . HOH D 2 .   ? 19.006  -1.036  -78.654  1.00 52.28 ? 308 HOH B O   1 
HETATM 2937 O O   . HOH D 2 .   ? 18.583  -0.851  -76.531  1.00 37.73 ? 309 HOH B O   1 
HETATM 2938 O O   . HOH D 2 .   ? 16.950  -13.584 -70.639  1.00 34.87 ? 310 HOH B O   1 
HETATM 2939 O O   . HOH D 2 .   ? 15.116  -15.491 -70.918  1.00 63.06 ? 311 HOH B O   1 
HETATM 2940 O O   . HOH D 2 .   ? 17.908  -12.678 -74.846  1.00 33.04 ? 312 HOH B O   1 
HETATM 2941 O O   . HOH D 2 .   ? 2.823   -13.388 -97.412  1.00 34.50 ? 313 HOH B O   1 
HETATM 2942 O O   . HOH D 2 .   ? 19.249  -9.567  -78.113  1.00 32.06 ? 314 HOH B O   1 
HETATM 2943 O O   . HOH D 2 .   ? 17.653  -11.836 -72.442  1.00 35.80 ? 315 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   . ASP A 4   ? 0.8095 0.7407 0.8259 -0.0173 0.0780  -0.0145 0   ASP A N   
2    C CA  . ASP A 4   ? 0.7936 0.7397 0.8177 -0.0149 0.0676  -0.0165 0   ASP A CA  
3    C C   . ASP A 4   ? 0.7327 0.6881 0.7533 -0.0138 0.0600  -0.0164 0   ASP A C   
4    O O   . ASP A 4   ? 0.7518 0.7079 0.7734 -0.0156 0.0630  -0.0191 0   ASP A O   
5    C CB  . ASP A 4   ? 0.8099 0.7668 0.8548 -0.0167 0.0695  -0.0253 0   ASP A CB  
6    C CG  . ASP A 4   ? 0.8272 0.7931 0.8840 -0.0191 0.0726  -0.0334 0   ASP A CG  
7    O OD1 . ASP A 4   ? 0.8249 0.8019 0.8825 -0.0169 0.0656  -0.0351 0   ASP A OD1 
8    O OD2 . ASP A 4   ? 0.8622 0.8240 0.9278 -0.0230 0.0824  -0.0385 0   ASP A OD2 
9    N N   . ALA A 5   ? 0.5921 0.5539 0.6085 -0.0110 0.0510  -0.0135 1   ALA A N   
10   C CA  . ALA A 5   ? 0.5056 0.4733 0.5172 -0.0103 0.0449  -0.0127 1   ALA A CA  
11   C C   . ALA A 5   ? 0.4060 0.3811 0.4158 -0.0080 0.0364  -0.0103 1   ALA A C   
12   O O   . ALA A 5   ? 0.3912 0.3697 0.4057 -0.0065 0.0345  -0.0104 1   ALA A O   
13   C CB  . ALA A 5   ? 0.5693 0.5265 0.5666 -0.0109 0.0473  -0.0088 1   ALA A CB  
14   N N   . VAL A 6   ? 0.2646 0.2423 0.2682 -0.0079 0.0318  -0.0087 2   VAL A N   
15   C CA  . VAL A 6   ? 0.2307 0.2145 0.2316 -0.0068 0.0249  -0.0067 2   VAL A CA  
16   C C   . VAL A 6   ? 0.2392 0.2167 0.2269 -0.0069 0.0231  -0.0034 2   VAL A C   
17   O O   . VAL A 6   ? 0.2341 0.2035 0.2143 -0.0075 0.0264  -0.0025 2   VAL A O   
18   C CB  . VAL A 6   ? 0.2370 0.2290 0.2420 -0.0069 0.0217  -0.0084 2   VAL A CB  
19   C CG1 . VAL A 6   ? 0.2927 0.2931 0.3096 -0.0050 0.0220  -0.0123 2   VAL A CG1 
20   C CG2 . VAL A 6   ? 0.2368 0.2238 0.2361 -0.0083 0.0234  -0.0085 2   VAL A CG2 
21   N N   . VAL A 7   ? 0.2018 0.1847 0.1874 -0.0059 0.0175  -0.0024 3   VAL A N   
22   C CA  . VAL A 7   ? 0.2289 0.2086 0.2033 -0.0052 0.0149  -0.0010 3   VAL A CA  
23   C C   . VAL A 7   ? 0.2289 0.2087 0.2009 -0.0080 0.0143  -0.0022 3   VAL A C   
24   O O   . VAL A 7   ? 0.2200 0.2031 0.1980 -0.0101 0.0148  -0.0034 3   VAL A O   
25   C CB  . VAL A 7   ? 0.2407 0.2277 0.2147 -0.0032 0.0090  -0.0013 3   VAL A CB  
26   C CG1 . VAL A 7   ? 0.2686 0.2539 0.2437 0.0003  0.0096  -0.0001 3   VAL A CG1 
27   C CG2 . VAL A 7   ? 0.2541 0.2519 0.2365 -0.0057 0.0058  -0.0031 3   VAL A CG2 
28   N N   . GLY A 8   ? 0.2621 0.2377 0.2243 -0.0072 0.0132  -0.0021 4   GLY A N   
29   C CA  . GLY A 8   ? 0.2351 0.2090 0.1945 -0.0098 0.0134  -0.0036 4   GLY A CA  
30   C C   . GLY A 8   ? 0.2284 0.2094 0.1930 -0.0131 0.0103  -0.0058 4   GLY A C   
31   O O   . GLY A 8   ? 0.2429 0.2215 0.2079 -0.0157 0.0118  -0.0068 4   GLY A O   
32   N N   . ASP A 9   ? 0.2489 0.2382 0.2177 -0.0130 0.0066  -0.0066 5   ASP A N   
33   C CA  . ASP A 9   ? 0.2436 0.2390 0.2176 -0.0168 0.0051  -0.0087 5   ASP A CA  
34   C C   . ASP A 9   ? 0.2542 0.2508 0.2350 -0.0178 0.0075  -0.0071 5   ASP A C   
35   O O   . ASP A 9   ? 0.2553 0.2548 0.2393 -0.0207 0.0078  -0.0079 5   ASP A O   
36   C CB  . ASP A 9   ? 0.3386 0.3438 0.3148 -0.0164 0.0005  -0.0113 5   ASP A CB  
37   C CG  . ASP A 9   ? 0.5496 0.5558 0.5191 -0.0150 -0.0027 -0.0148 5   ASP A CG  
38   O OD1 . ASP A 9   ? 0.5753 0.5754 0.5396 -0.0158 -0.0013 -0.0158 5   ASP A OD1 
39   O OD2 . ASP A 9   ? 0.6533 0.6672 0.6225 -0.0122 -0.0070 -0.0172 5   ASP A OD2 
40   N N   . THR A 10  ? 0.2215 0.2157 0.2043 -0.0153 0.0097  -0.0054 6   THR A N   
41   C CA  . THR A 10  ? 0.2130 0.2098 0.2016 -0.0144 0.0113  -0.0049 6   THR A CA  
42   C C   . THR A 10  ? 0.2238 0.2150 0.2095 -0.0160 0.0138  -0.0049 6   THR A C   
43   O O   . THR A 10  ? 0.2124 0.1966 0.1935 -0.0164 0.0156  -0.0054 6   THR A O   
44   C CB  . THR A 10  ? 0.1915 0.1873 0.1835 -0.0114 0.0134  -0.0050 6   THR A CB  
45   O OG1 . THR A 10  ? 0.2146 0.2130 0.2084 -0.0099 0.0119  -0.0047 6   THR A OG1 
46   C CG2 . THR A 10  ? 0.2163 0.2168 0.2145 -0.0089 0.0141  -0.0058 6   THR A CG2 
47   N N   . ILE A 11  ? 0.2060 0.1992 0.1935 -0.0164 0.0144  -0.0043 7   ILE A N   
48   C CA  . ILE A 11  ? 0.2081 0.1938 0.1913 -0.0172 0.0175  -0.0038 7   ILE A CA  
49   C C   . ILE A 11  ? 0.2090 0.1929 0.1923 -0.0120 0.0191  -0.0036 7   ILE A C   
50   O O   . ILE A 11  ? 0.2157 0.2063 0.2038 -0.0080 0.0183  -0.0037 7   ILE A O   
51   C CB  . ILE A 11  ? 0.2257 0.2122 0.2093 -0.0196 0.0189  -0.0027 7   ILE A CB  
52   C CG1 . ILE A 11  ? 0.2606 0.2503 0.2457 -0.0252 0.0174  -0.0050 7   ILE A CG1 
53   C CG2 . ILE A 11  ? 0.2783 0.2546 0.2561 -0.0190 0.0231  -0.0013 7   ILE A CG2 
54   C CD1 . ILE A 11  ? 0.2820 0.2637 0.2628 -0.0291 0.0189  -0.0071 7   ILE A CD1 
55   N N   . ILE A 12  ? 0.2156 0.1915 0.1939 -0.0115 0.0211  -0.0043 8   ILE A N   
56   C CA  . ILE A 12  ? 0.2083 0.1831 0.1863 -0.0060 0.0225  -0.0056 8   ILE A CA  
57   C C   . ILE A 12  ? 0.2135 0.1785 0.1836 -0.0047 0.0250  -0.0047 8   ILE A C   
58   O O   . ILE A 12  ? 0.2408 0.1984 0.2063 -0.0094 0.0262  -0.0037 8   ILE A O   
59   C CB  . ILE A 12  ? 0.1993 0.1746 0.1795 -0.0054 0.0229  -0.0084 8   ILE A CB  
60   C CG1 . ILE A 12  ? 0.2162 0.1835 0.1903 -0.0092 0.0238  -0.0085 8   ILE A CG1 
61   C CG2 . ILE A 12  ? 0.2102 0.1929 0.1975 -0.0060 0.0216  -0.0090 8   ILE A CG2 
62   C CD1 . ILE A 12  ? 0.2539 0.2199 0.2285 -0.0080 0.0257  -0.0112 8   ILE A CD1 
63   N N   . ASP A 13  ? 0.2433 0.2082 0.2118 0.0022  0.0257  -0.0056 9   ASP A N   
64   C CA  . ASP A 13  ? 0.2421 0.1966 0.2016 0.0057  0.0281  -0.0050 9   ASP A CA  
65   C C   . ASP A 13  ? 0.2374 0.1885 0.1956 0.0058  0.0282  -0.0083 9   ASP A C   
66   O O   . ASP A 13  ? 0.2696 0.2283 0.2337 0.0082  0.0271  -0.0121 9   ASP A O   
67   C CB  . ASP A 13  ? 0.2756 0.2329 0.2330 0.0152  0.0280  -0.0053 9   ASP A CB  
68   C CG  . ASP A 13  ? 0.3012 0.2470 0.2474 0.0214  0.0303  -0.0048 9   ASP A CG  
69   O OD1 . ASP A 13  ? 0.2995 0.2429 0.2442 0.0231  0.0300  -0.0082 9   ASP A OD1 
70   O OD2 . ASP A 13  ? 0.3749 0.3140 0.3131 0.0254  0.0327  -0.0011 9   ASP A OD2 
71   N N   . VAL A 14  ? 0.2396 0.1797 0.1908 0.0028  0.0300  -0.0075 10  VAL A N   
72   C CA  . VAL A 14  ? 0.2697 0.2057 0.2180 0.0039  0.0303  -0.0106 10  VAL A CA  
73   C C   . VAL A 14  ? 0.2985 0.2222 0.2366 0.0081  0.0325  -0.0095 10  VAL A C   
74   O O   . VAL A 14  ? 0.2932 0.2067 0.2262 0.0038  0.0347  -0.0070 10  VAL A O   
75   C CB  . VAL A 14  ? 0.2315 0.1657 0.1803 -0.0033 0.0301  -0.0112 10  VAL A CB  
76   C CG1 . VAL A 14  ? 0.2843 0.2141 0.2295 -0.0017 0.0308  -0.0143 10  VAL A CG1 
77   C CG2 . VAL A 14  ? 0.2918 0.2358 0.2482 -0.0062 0.0284  -0.0115 10  VAL A CG2 
78   N N   . SER A 15  ? 0.3020 0.2268 0.2374 0.0171  0.0322  -0.0118 11  SER A N   
79   C CA  . SER A 15  ? 0.2987 0.2109 0.2223 0.0236  0.0342  -0.0107 11  SER A CA  
80   C C   . SER A 15  ? 0.3258 0.2275 0.2424 0.0226  0.0376  -0.0048 11  SER A C   
81   O O   . SER A 15  ? 0.4040 0.2902 0.3109 0.0223  0.0411  -0.0025 11  SER A O   
82   C CB  . SER A 15  ? 0.3459 0.2490 0.2645 0.0219  0.0350  -0.0128 11  SER A CB  
83   O OG  . SER A 15  ? 0.3719 0.2849 0.2968 0.0230  0.0328  -0.0183 11  SER A OG  
84   N N   . GLY A 16  ? 0.3014 0.2111 0.2231 0.0218  0.0371  -0.0026 12  GLY A N   
85   C CA  . GLY A 16  ? 0.3099 0.2111 0.2255 0.0211  0.0411  0.0028  12  GLY A CA  
86   C C   . GLY A 16  ? 0.3514 0.2499 0.2715 0.0093  0.0433  0.0046  12  GLY A C   
87   O O   . GLY A 16  ? 0.3895 0.2846 0.3079 0.0072  0.0468  0.0082  12  GLY A O   
88   N N   . LYS A 17  ? 0.2971 0.1980 0.2227 0.0020  0.0414  0.0015  13  LYS A N   
89   C CA  . LYS A 17  ? 0.3526 0.2546 0.2839 -0.0084 0.0421  0.0012  13  LYS A CA  
90   C C   . LYS A 17  ? 0.3536 0.2718 0.2951 -0.0108 0.0378  0.0000  13  LYS A C   
91   O O   . LYS A 17  ? 0.3747 0.3019 0.3198 -0.0063 0.0344  -0.0014 13  LYS A O   
92   C CB  . LYS A 17  ? 0.3629 0.2594 0.2937 -0.0135 0.0418  -0.0022 13  LYS A CB  
93   C CG  . LYS A 17  ? 0.4491 0.3300 0.3699 -0.0100 0.0451  -0.0020 13  LYS A CG  
94   C CD  . LYS A 17  ? 0.4804 0.3469 0.3958 -0.0132 0.0516  0.0006  13  LYS A CD  
95   C CE  . LYS A 17  ? 0.5597 0.4087 0.4632 -0.0078 0.0551  0.0015  13  LYS A CE  
96   N NZ  . LYS A 17  ? 0.6115 0.4605 0.5154 -0.0084 0.0519  -0.0031 13  LYS A NZ  
97   N N   . LYS A 18  ? 0.2989 0.2208 0.2456 -0.0179 0.0381  -0.0001 14  LYS A N   
98   C CA  . LYS A 18  ? 0.2939 0.2301 0.2491 -0.0198 0.0340  -0.0010 14  LYS A CA  
99   C C   . LYS A 18  ? 0.2875 0.2273 0.2462 -0.0254 0.0312  -0.0046 14  LYS A C   
100  O O   . LYS A 18  ? 0.3242 0.2589 0.2822 -0.0309 0.0329  -0.0068 14  LYS A O   
101  C CB  . LYS A 18  ? 0.2839 0.2242 0.2424 -0.0221 0.0357  0.0009  14  LYS A CB  
102  C CG  . LYS A 18  ? 0.3391 0.2763 0.2927 -0.0151 0.0384  0.0048  14  LYS A CG  
103  C CD  . LYS A 18  ? 0.4145 0.3611 0.3707 -0.0075 0.0342  0.0042  14  LYS A CD  
104  C CE  . LYS A 18  ? 0.5602 0.5054 0.5110 0.0011  0.0360  0.0069  14  LYS A CE  
105  N NZ  . LYS A 18  ? 0.6325 0.5627 0.5717 0.0057  0.0402  0.0087  14  LYS A NZ  
106  N N   . MET A 19  ? 0.2631 0.2114 0.2251 -0.0236 0.0274  -0.0056 15  MET A N   
107  C CA  . MET A 19  ? 0.2727 0.2249 0.2361 -0.0270 0.0245  -0.0084 15  MET A CA  
108  C C   . MET A 19  ? 0.2387 0.2002 0.2059 -0.0244 0.0214  -0.0078 15  MET A C   
109  O O   . MET A 19  ? 0.2385 0.2027 0.2079 -0.0204 0.0217  -0.0062 15  MET A O   
110  C CB  . MET A 19  ? 0.3400 0.2850 0.2981 -0.0268 0.0250  -0.0104 15  MET A CB  
111  C CG  . MET A 19  ? 0.3103 0.2538 0.2664 -0.0216 0.0255  -0.0096 15  MET A CG  
112  S SD  . MET A 19  ? 0.4008 0.3348 0.3501 -0.0209 0.0270  -0.0120 15  MET A SD  
113  C CE  . MET A 19  ? 0.4714 0.4064 0.4194 -0.0258 0.0249  -0.0151 15  MET A CE  
114  N N   . THR A 20  ? 0.2375 0.2037 0.2053 -0.0262 0.0186  -0.0096 16  THR A N   
115  C CA  . THR A 20  ? 0.2247 0.1965 0.1941 -0.0231 0.0165  -0.0086 16  THR A CA  
116  C C   . THR A 20  ? 0.2137 0.1805 0.1797 -0.0203 0.0183  -0.0082 16  THR A C   
117  O O   . THR A 20  ? 0.2276 0.1881 0.1891 -0.0208 0.0198  -0.0093 16  THR A O   
118  C CB  . THR A 20  ? 0.2384 0.2157 0.2071 -0.0239 0.0129  -0.0104 16  THR A CB  
119  O OG1 . THR A 20  ? 0.2687 0.2415 0.2308 -0.0238 0.0125  -0.0124 16  THR A OG1 
120  C CG2 . THR A 20  ? 0.2651 0.2487 0.2383 -0.0276 0.0114  -0.0128 16  THR A CG2 
121  N N   . ILE A 21  ? 0.2075 0.1774 0.1766 -0.0176 0.0187  -0.0071 17  ILE A N   
122  C CA  . ILE A 21  ? 0.2134 0.1792 0.1811 -0.0157 0.0217  -0.0074 17  ILE A CA  
123  C C   . ILE A 21  ? 0.2126 0.1734 0.1726 -0.0161 0.0220  -0.0076 17  ILE A C   
124  O O   . ILE A 21  ? 0.2329 0.1885 0.1893 -0.0157 0.0248  -0.0084 17  ILE A O   
125  C CB  . ILE A 21  ? 0.1903 0.1604 0.1649 -0.0134 0.0230  -0.0073 17  ILE A CB  
126  C CG1 . ILE A 21  ? 0.2115 0.1784 0.1873 -0.0123 0.0273  -0.0092 17  ILE A CG1 
127  C CG2 . ILE A 21  ? 0.2186 0.1911 0.1932 -0.0131 0.0213  -0.0058 17  ILE A CG2 
128  C CD1 . ILE A 21  ? 0.2194 0.1921 0.2052 -0.0105 0.0291  -0.0111 17  ILE A CD1 
129  N N   . ALA A 22  ? 0.2214 0.1843 0.1780 -0.0161 0.0190  -0.0073 18  ALA A N   
130  C CA  . ALA A 22  ? 0.2323 0.1911 0.1798 -0.0149 0.0187  -0.0079 18  ALA A CA  
131  C C   . ALA A 22  ? 0.2526 0.2086 0.1969 -0.0170 0.0182  -0.0106 18  ALA A C   
132  O O   . ALA A 22  ? 0.2623 0.2131 0.1999 -0.0157 0.0199  -0.0112 18  ALA A O   
133  C CB  . ALA A 22  ? 0.2556 0.2189 0.1999 -0.0130 0.0145  -0.0081 18  ALA A CB  
134  N N   . GLU A 23  ? 0.2567 0.2155 0.2055 -0.0202 0.0164  -0.0124 19  GLU A N   
135  C CA  . GLU A 23  ? 0.2774 0.2320 0.2241 -0.0226 0.0168  -0.0153 19  GLU A CA  
136  C C   . GLU A 23  ? 0.2603 0.2081 0.2054 -0.0216 0.0204  -0.0144 19  GLU A C   
137  O O   . GLU A 23  ? 0.2852 0.2282 0.2252 -0.0216 0.0211  -0.0164 19  GLU A O   
138  C CB  . GLU A 23  ? 0.3033 0.2599 0.2557 -0.0267 0.0164  -0.0167 19  GLU A CB  
139  C CG  . GLU A 23  ? 0.3774 0.3419 0.3324 -0.0288 0.0128  -0.0202 19  GLU A CG  
140  C CD  . GLU A 23  ? 0.4690 0.4363 0.4313 -0.0333 0.0138  -0.0211 19  GLU A CD  
141  O OE1 . GLU A 23  ? 0.3750 0.3376 0.3388 -0.0337 0.0172  -0.0178 19  GLU A OE1 
142  O OE2 . GLU A 23  ? 0.5525 0.5271 0.5186 -0.0360 0.0114  -0.0255 19  GLU A OE2 
143  N N   . PHE A 24  ? 0.2490 0.1974 0.1985 -0.0202 0.0225  -0.0123 20  PHE A N   
144  C CA  . PHE A 24  ? 0.2458 0.1898 0.1945 -0.0183 0.0255  -0.0128 20  PHE A CA  
145  C C   . PHE A 24  ? 0.2677 0.2097 0.2124 -0.0168 0.0276  -0.0133 20  PHE A C   
146  O O   . PHE A 24  ? 0.2680 0.2055 0.2087 -0.0163 0.0291  -0.0151 20  PHE A O   
147  C CB  . PHE A 24  ? 0.2561 0.2038 0.2113 -0.0160 0.0265  -0.0119 20  PHE A CB  
148  C CG  . PHE A 24  ? 0.2319 0.1776 0.1874 -0.0130 0.0290  -0.0139 20  PHE A CG  
149  C CD1 . PHE A 24  ? 0.2771 0.2162 0.2274 -0.0125 0.0296  -0.0154 20  PHE A CD1 
150  C CD2 . PHE A 24  ? 0.2826 0.2334 0.2442 -0.0105 0.0308  -0.0153 20  PHE A CD2 
151  C CE1 . PHE A 24  ? 0.2852 0.2234 0.2355 -0.0089 0.0314  -0.0181 20  PHE A CE1 
152  C CE2 . PHE A 24  ? 0.3313 0.2823 0.2944 -0.0074 0.0329  -0.0189 20  PHE A CE2 
153  C CZ  . PHE A 24  ? 0.2975 0.2424 0.2545 -0.0063 0.0329  -0.0202 20  PHE A CZ  
154  N N   . TYR A 25  ? 0.2344 0.1787 0.1794 -0.0159 0.0282  -0.0116 21  TYR A N   
155  C CA  . TYR A 25  ? 0.2503 0.1907 0.1896 -0.0144 0.0316  -0.0113 21  TYR A CA  
156  C C   . TYR A 25  ? 0.2605 0.1971 0.1906 -0.0141 0.0302  -0.0125 21  TYR A C   
157  O O   . TYR A 25  ? 0.2767 0.2093 0.2024 -0.0133 0.0331  -0.0137 21  TYR A O   
158  C CB  . TYR A 25  ? 0.2780 0.2191 0.2170 -0.0131 0.0328  -0.0086 21  TYR A CB  
159  C CG  . TYR A 25  ? 0.2725 0.2071 0.2038 -0.0113 0.0377  -0.0074 21  TYR A CG  
160  C CD1 . TYR A 25  ? 0.2820 0.2128 0.2015 -0.0089 0.0364  -0.0063 21  TYR A CD1 
161  C CD2 . TYR A 25  ? 0.2731 0.2055 0.2086 -0.0118 0.0442  -0.0080 21  TYR A CD2 
162  C CE1 . TYR A 25  ? 0.3071 0.2306 0.2175 -0.0064 0.0418  -0.0046 21  TYR A CE1 
163  C CE2 . TYR A 25  ? 0.2852 0.2104 0.2133 -0.0107 0.0504  -0.0067 21  TYR A CE2 
164  C CZ  . TYR A 25  ? 0.2799 0.1999 0.1944 -0.0078 0.0493  -0.0043 21  TYR A CZ  
165  O OH  . TYR A 25  ? 0.3248 0.2363 0.2298 -0.0058 0.0563  -0.0024 21  TYR A OH  
166  N N   . ASP A 26  ? 0.2649 0.2040 0.1927 -0.0147 0.0256  -0.0133 22  ASP A N   
167  C CA  . ASP A 26  ? 0.3039 0.2413 0.2238 -0.0137 0.0236  -0.0159 22  ASP A CA  
168  C C   . ASP A 26  ? 0.3120 0.2460 0.2322 -0.0156 0.0241  -0.0190 22  ASP A C   
169  O O   . ASP A 26  ? 0.3419 0.2732 0.2553 -0.0142 0.0240  -0.0212 22  ASP A O   
170  C CB  . ASP A 26  ? 0.3120 0.2552 0.2319 -0.0140 0.0184  -0.0181 22  ASP A CB  
171  C CG  . ASP A 26  ? 0.3854 0.3312 0.3017 -0.0103 0.0172  -0.0156 22  ASP A CG  
172  O OD1 . ASP A 26  ? 0.3911 0.3319 0.3023 -0.0073 0.0211  -0.0120 22  ASP A OD1 
173  O OD2 . ASP A 26  ? 0.4254 0.3779 0.3439 -0.0104 0.0127  -0.0176 22  ASP A OD2 
174  N N   . SER A 27  ? 0.3142 0.2477 0.2410 -0.0180 0.0244  -0.0192 23  SER A N   
175  C CA  . SER A 27  ? 0.3272 0.2557 0.2537 -0.0192 0.0251  -0.0217 23  SER A CA  
176  C C   . SER A 27  ? 0.3161 0.2413 0.2410 -0.0167 0.0286  -0.0218 23  SER A C   
177  O O   . SER A 27  ? 0.3501 0.2706 0.2729 -0.0165 0.0291  -0.0242 23  SER A O   
178  C CB  . SER A 27  ? 0.3658 0.2935 0.2981 -0.0214 0.0250  -0.0210 23  SER A CB  
179  O OG  . SER A 27  ? 0.3605 0.2886 0.2962 -0.0191 0.0271  -0.0188 23  SER A OG  
180  N N   . THR A 28  ? 0.2919 0.2195 0.2186 -0.0150 0.0314  -0.0198 24  THR A N   
181  C CA  . THR A 28  ? 0.3066 0.2332 0.2343 -0.0132 0.0353  -0.0213 24  THR A CA  
182  C C   . THR A 28  ? 0.3062 0.2299 0.2263 -0.0122 0.0375  -0.0224 24  THR A C   
183  O O   . THR A 28  ? 0.3171 0.2404 0.2320 -0.0116 0.0379  -0.0204 24  THR A O   
184  C CB  . THR A 28  ? 0.2816 0.2127 0.2163 -0.0127 0.0381  -0.0200 24  THR A CB  
185  O OG1 . THR A 28  ? 0.2829 0.2173 0.2240 -0.0126 0.0358  -0.0194 24  THR A OG1 
186  C CG2 . THR A 28  ? 0.2967 0.2289 0.2346 -0.0112 0.0427  -0.0231 24  THR A CG2 
187  N N   . PRO A 29  ? 0.3298 0.2510 0.2479 -0.0111 0.0388  -0.0256 25  PRO A N   
188  C CA  . PRO A 29  ? 0.3237 0.2425 0.2343 -0.0097 0.0413  -0.0267 25  PRO A CA  
189  C C   . PRO A 29  ? 0.3284 0.2478 0.2386 -0.0093 0.0471  -0.0246 25  PRO A C   
190  O O   . PRO A 29  ? 0.3193 0.2417 0.2375 -0.0102 0.0500  -0.0241 25  PRO A O   
191  C CB  . PRO A 29  ? 0.3721 0.2896 0.2834 -0.0085 0.0420  -0.0309 25  PRO A CB  
192  C CG  . PRO A 29  ? 0.3760 0.2920 0.2906 -0.0089 0.0381  -0.0315 25  PRO A CG  
193  C CD  . PRO A 29  ? 0.3145 0.2342 0.2355 -0.0102 0.0376  -0.0282 25  PRO A CD  
194  N N   . ASP A 30  ? 0.3232 0.2393 0.2236 -0.0076 0.0492  -0.0235 26  ASP A N   
195  C CA  . ASP A 30  ? 0.3329 0.2461 0.2291 -0.0067 0.0558  -0.0204 26  ASP A CA  
196  C C   . ASP A 30  ? 0.3129 0.2262 0.2132 -0.0076 0.0635  -0.0229 26  ASP A C   
197  O O   . ASP A 30  ? 0.3495 0.2589 0.2421 -0.0064 0.0692  -0.0225 26  ASP A O   
198  C CB  . ASP A 30  ? 0.3656 0.2745 0.2474 -0.0030 0.0551  -0.0182 26  ASP A CB  
199  C CG  . ASP A 30  ? 0.3812 0.2915 0.2599 -0.0016 0.0491  -0.0160 26  ASP A CG  
200  O OD1 . ASP A 30  ? 0.3981 0.3118 0.2858 -0.0041 0.0465  -0.0152 26  ASP A OD1 
201  O OD2 . ASP A 30  ? 0.4244 0.3332 0.2917 0.0026  0.0466  -0.0157 26  ASP A OD2 
202  N N   . VAL A 31  ? 0.3042 0.2228 0.2170 -0.0096 0.0640  -0.0261 27  VAL A N   
203  C CA  . VAL A 31  ? 0.3163 0.2380 0.2367 -0.0107 0.0710  -0.0304 27  VAL A CA  
204  C C   . VAL A 31  ? 0.3135 0.2353 0.2407 -0.0130 0.0770  -0.0287 27  VAL A C   
205  O O   . VAL A 31  ? 0.2933 0.2207 0.2315 -0.0140 0.0751  -0.0303 27  VAL A O   
206  C CB  . VAL A 31  ? 0.3262 0.2546 0.2557 -0.0099 0.0672  -0.0363 27  VAL A CB  
207  C CG1 . VAL A 31  ? 0.3397 0.2742 0.2792 -0.0107 0.0739  -0.0427 27  VAL A CG1 
208  C CG2 . VAL A 31  ? 0.3483 0.2742 0.2702 -0.0077 0.0618  -0.0377 27  VAL A CG2 
209  N N   . PHE A 32  ? 0.3061 0.2207 0.2258 -0.0134 0.0843  -0.0250 28  PHE A N   
210  C CA  . PHE A 32  ? 0.3175 0.2291 0.2415 -0.0154 0.0904  -0.0223 28  PHE A CA  
211  C C   . PHE A 32  ? 0.2957 0.2111 0.2329 -0.0191 0.0998  -0.0282 28  PHE A C   
212  O O   . PHE A 32  ? 0.3227 0.2370 0.2583 -0.0200 0.1067  -0.0311 28  PHE A O   
213  C CB  . PHE A 32  ? 0.3316 0.2315 0.2398 -0.0132 0.0949  -0.0152 28  PHE A CB  
214  C CG  . PHE A 32  ? 0.3411 0.2392 0.2387 -0.0094 0.0858  -0.0107 28  PHE A CG  
215  C CD1 . PHE A 32  ? 0.3165 0.2175 0.2194 -0.0096 0.0802  -0.0089 28  PHE A CD1 
216  C CD2 . PHE A 32  ? 0.3394 0.2342 0.2225 -0.0053 0.0825  -0.0093 28  PHE A CD2 
217  C CE1 . PHE A 32  ? 0.3172 0.2182 0.2116 -0.0064 0.0720  -0.0060 28  PHE A CE1 
218  C CE2 . PHE A 32  ? 0.3439 0.2390 0.2189 -0.0018 0.0740  -0.0070 28  PHE A CE2 
219  C CZ  . PHE A 32  ? 0.3411 0.2395 0.2221 -0.0025 0.0689  -0.0055 28  PHE A CZ  
220  N N   . MET A 33  ? 0.3054 0.2264 0.2565 -0.0213 0.1002  -0.0308 29  MET A N   
221  C CA  . MET A 33  ? 0.3062 0.2308 0.2717 -0.0254 0.1100  -0.0368 29  MET A CA  
222  C C   . MET A 33  ? 0.3118 0.2246 0.2728 -0.0277 0.1199  -0.0314 29  MET A C   
223  O O   . MET A 33  ? 0.3429 0.2536 0.3110 -0.0318 0.1317  -0.0352 29  MET A O   
224  C CB  . MET A 33  ? 0.3227 0.2596 0.3055 -0.0258 0.1053  -0.0427 29  MET A CB  
225  C CG  . MET A 33  ? 0.3559 0.3028 0.3418 -0.0222 0.0955  -0.0472 29  MET A CG  
226  S SD  . MET A 33  ? 0.4554 0.4079 0.4442 -0.0220 0.0997  -0.0557 29  MET A SD  
227  C CE  . MET A 33  ? 0.4216 0.3827 0.4309 -0.0268 0.1108  -0.0656 29  MET A CE  
228  N N   . ARG A 34  ? 0.3295 0.2342 0.2788 -0.0250 0.1156  -0.0232 30  ARG A N   
229  C CA  . ARG A 34  ? 0.3383 0.2293 0.2793 -0.0253 0.1241  -0.0169 30  ARG A CA  
230  C C   . ARG A 34  ? 0.3363 0.2192 0.2574 -0.0194 0.1172  -0.0083 30  ARG A C   
231  O O   . ARG A 34  ? 0.3462 0.2359 0.2671 -0.0170 0.1055  -0.0077 30  ARG A O   
232  C CB  . ARG A 34  ? 0.3564 0.2499 0.3115 -0.0281 0.1256  -0.0187 30  ARG A CB  
233  C CG  . ARG A 34  ? 0.4587 0.3361 0.4058 -0.0285 0.1359  -0.0125 30  ARG A CG  
234  C CD  . ARG A 34  ? 0.5843 0.4634 0.5404 -0.0290 0.1328  -0.0121 30  ARG A CD  
235  N NE  . ARG A 34  ? 0.6198 0.5118 0.5999 -0.0340 0.1347  -0.0221 30  ARG A NE  
236  C CZ  . ARG A 34  ? 0.5960 0.4971 0.5882 -0.0339 0.1281  -0.0248 30  ARG A CZ  
237  N NH1 . ARG A 34  ? 0.6042 0.5029 0.5873 -0.0297 0.1194  -0.0182 30  ARG A NH1 
238  N NH2 . ARG A 34  ? 0.6370 0.5510 0.6510 -0.0375 0.1300  -0.0350 30  ARG A NH2 
239  N N   . ARG A 35  ? 0.3789 0.2474 0.2830 -0.0168 0.1248  -0.0022 31  ARG A N   
240  C CA  . ARG A 35  ? 0.3740 0.2357 0.2585 -0.0098 0.1183  0.0049  31  ARG A CA  
241  C C   . ARG A 35  ? 0.4288 0.2726 0.2980 -0.0068 0.1293  0.0120  31  ARG A C   
242  O O   . ARG A 35  ? 0.4364 0.2710 0.2990 -0.0075 0.1409  0.0130  31  ARG A O   
243  C CB  . ARG A 35  ? 0.3947 0.2595 0.2686 -0.0062 0.1125  0.0042  31  ARG A CB  
244  C CG  . ARG A 35  ? 0.3929 0.2514 0.2466 0.0018  0.1066  0.0100  31  ARG A CG  
245  C CD  . ARG A 35  ? 0.4035 0.2679 0.2496 0.0052  0.0985  0.0077  31  ARG A CD  
246  N NE  . ARG A 35  ? 0.4003 0.2606 0.2283 0.0134  0.0926  0.0117  31  ARG A NE  
247  C CZ  . ARG A 35  ? 0.4258 0.2909 0.2453 0.0179  0.0850  0.0095  31  ARG A CZ  
248  N NH1 . ARG A 35  ? 0.4724 0.3445 0.2985 0.0147  0.0826  0.0042  31  ARG A NH1 
249  N NH2 . ARG A 35  ? 0.5191 0.3819 0.3232 0.0260  0.0797  0.0119  31  ARG A NH2 
250  N N   . ASN A 36  ? 0.4164 0.2546 0.2790 -0.0028 0.1260  0.0170  32  ASN A N   
251  C CA  . ASN A 36  ? 0.4552 0.2744 0.2984 0.0027  0.1348  0.0249  32  ASN A CA  
252  C C   . ASN A 36  ? 0.4520 0.2718 0.2820 0.0111  0.1229  0.0289  32  ASN A C   
253  O O   . ASN A 36  ? 0.4482 0.2721 0.2860 0.0107  0.1174  0.0287  32  ASN A O   
254  C CB  . ASN A 36  ? 0.4972 0.3063 0.3491 -0.0022 0.1470  0.0257  32  ASN A CB  
255  C CG  . ASN A 36  ? 0.6401 0.4259 0.4698 0.0036  0.1587  0.0345  32  ASN A CG  
256  O OD1 . ASN A 36  ? 0.6664 0.4450 0.4772 0.0129  0.1531  0.0406  32  ASN A OD1 
257  N ND2 . ASN A 36  ? 0.6621 0.4357 0.4933 -0.0014 0.1755  0.0347  32  ASN A ND2 
258  N N   . ASP A 37  ? 0.5010 0.3188 0.3122 0.0188  0.1185  0.0312  33  ASP A N   
259  C CA  . ASP A 37  ? 0.4871 0.3078 0.2862 0.0274  0.1068  0.0332  33  ASP A CA  
260  C C   . ASP A 37  ? 0.5388 0.3451 0.3252 0.0337  0.1110  0.0397  33  ASP A C   
261  O O   . ASP A 37  ? 0.5304 0.3423 0.3161 0.0378  0.1013  0.0397  33  ASP A O   
262  C CB  . ASP A 37  ? 0.5595 0.3805 0.3405 0.0353  0.1025  0.0333  33  ASP A CB  
263  C CG  . ASP A 37  ? 0.4959 0.3323 0.2893 0.0301  0.0954  0.0263  33  ASP A CG  
264  O OD1 . ASP A 37  ? 0.4740 0.3221 0.2880 0.0222  0.0908  0.0215  33  ASP A OD1 
265  O OD2 . ASP A 37  ? 0.5679 0.4041 0.3493 0.0347  0.0946  0.0255  33  ASP A OD2 
266  N N   . GLU A 38  ? 0.5908 0.3780 0.3669 0.0345  0.1260  0.0452  34  GLU A N   
267  C CA  . GLU A 38  ? 0.5879 0.3584 0.3491 0.0415  0.1308  0.0521  34  GLU A CA  
268  C C   . GLU A 38  ? 0.5882 0.3626 0.3688 0.0350  0.1298  0.0501  34  GLU A C   
269  O O   . GLU A 38  ? 0.6083 0.3801 0.3825 0.0412  0.1243  0.0527  34  GLU A O   
270  C CB  . GLU A 38  ? 0.7145 0.4608 0.4577 0.0443  0.1485  0.0591  34  GLU A CB  
271  C CG  . GLU A 38  ? 0.8496 0.5924 0.5736 0.0509  0.1504  0.0609  34  GLU A CG  
272  C CD  . GLU A 38  ? 0.9565 0.7002 0.6919 0.0411  0.1611  0.0577  34  GLU A CD  
273  O OE1 . GLU A 38  ? 0.9542 0.7172 0.7097 0.0334  0.1535  0.0499  34  GLU A OE1 
274  O OE2 . GLU A 38  ? 1.0217 0.7510 0.7528 0.0412  0.1732  0.0604  34  GLU A OE2 
275  N N   . ALA A 39  ? 0.5158 0.2979 0.3205 0.0233  0.1343  0.0447  35  ALA A N   
276  C CA  . ALA A 39  ? 0.4993 0.2887 0.3246 0.0172  0.1320  0.0412  35  ALA A CA  
277  C C   . ALA A 39  ? 0.4728 0.2842 0.3111 0.0163  0.1153  0.0359  35  ALA A C   
278  O O   . ALA A 39  ? 0.5108 0.3298 0.3647 0.0126  0.1116  0.0331  35  ALA A O   
279  C CB  . ALA A 39  ? 0.5419 0.3321 0.3882 0.0060  0.1435  0.0362  35  ALA A CB  
280  N N   . ARG A 40  ? 0.4544 0.2755 0.2862 0.0196  0.1058  0.0344  36  ARG A N   
281  C CA  . ARG A 40  ? 0.4560 0.2968 0.2997 0.0180  0.0916  0.0292  36  ARG A CA  
282  C C   . ARG A 40  ? 0.3893 0.2423 0.2582 0.0083  0.0913  0.0232  36  ARG A C   
283  O O   . ARG A 40  ? 0.4020 0.2648 0.2831 0.0064  0.0846  0.0209  36  ARG A O   
284  C CB  . ARG A 40  ? 0.4664 0.3104 0.3037 0.0246  0.0818  0.0307  36  ARG A CB  
285  C CG  . ARG A 40  ? 0.5143 0.3486 0.3260 0.0360  0.0804  0.0352  36  ARG A CG  
286  C CD  . ARG A 40  ? 0.6149 0.4536 0.4209 0.0433  0.0708  0.0355  36  ARG A CD  
287  N NE  . ARG A 40  ? 0.7304 0.5624 0.5118 0.0557  0.0680  0.0383  36  ARG A NE  
288  C CZ  . ARG A 40  ? 0.8198 0.6329 0.5804 0.0649  0.0752  0.0450  36  ARG A CZ  
289  N NH1 . ARG A 40  ? 0.8315 0.6296 0.5943 0.0616  0.0865  0.0496  36  ARG A NH1 
290  N NH2 . ARG A 40  ? 0.8200 0.6289 0.5573 0.0778  0.0714  0.0467  36  ARG A NH2 
291  N N   . ASP A 41  ? 0.4016 0.2549 0.2775 0.0029  0.0982  0.0202  37  ASP A N   
292  C CA  . ASP A 41  ? 0.4029 0.2665 0.3014 -0.0050 0.1000  0.0138  37  ASP A CA  
293  C C   . ASP A 41  ? 0.3733 0.2449 0.2762 -0.0078 0.0988  0.0092  37  ASP A C   
294  O O   . ASP A 41  ? 0.3755 0.2394 0.2700 -0.0076 0.1064  0.0101  37  ASP A O   
295  C CB  . ASP A 41  ? 0.4575 0.3105 0.3619 -0.0089 0.1138  0.0138  37  ASP A CB  
296  C CG  . ASP A 41  ? 0.5682 0.4327 0.4962 -0.0164 0.1165  0.0056  37  ASP A CG  
297  O OD1 . ASP A 41  ? 0.5865 0.4661 0.5273 -0.0175 0.1069  0.0012  37  ASP A OD1 
298  O OD2 . ASP A 41  ? 0.6488 0.5069 0.5824 -0.0208 0.1290  0.0032  37  ASP A OD2 
299  N N   . TRP A 42  ? 0.3440 0.2302 0.2592 -0.0100 0.0897  0.0043  38  TRP A N   
300  C CA  . TRP A 42  ? 0.3250 0.2182 0.2428 -0.0115 0.0870  0.0001  38  TRP A CA  
301  C C   . TRP A 42  ? 0.3092 0.2153 0.2461 -0.0154 0.0841  -0.0065 38  TRP A C   
302  O O   . TRP A 42  ? 0.3211 0.2340 0.2664 -0.0156 0.0784  -0.0071 38  TRP A O   
303  C CB  . TRP A 42  ? 0.3260 0.2225 0.2336 -0.0077 0.0768  0.0015  38  TRP A CB  
304  C CG  . TRP A 42  ? 0.3613 0.2480 0.2496 -0.0020 0.0774  0.0067  38  TRP A CG  
305  C CD1 . TRP A 42  ? 0.3827 0.2622 0.2575 0.0008  0.0817  0.0081  38  TRP A CD1 
306  C CD2 . TRP A 42  ? 0.3742 0.2576 0.2534 0.0029  0.0734  0.0108  38  TRP A CD2 
307  N NE1 . TRP A 42  ? 0.3937 0.2655 0.2507 0.0079  0.0805  0.0129  38  TRP A NE1 
308  C CE2 . TRP A 42  ? 0.3897 0.2638 0.2491 0.0094  0.0752  0.0145  38  TRP A CE2 
309  C CE3 . TRP A 42  ? 0.3671 0.2551 0.2525 0.0031  0.0681  0.0114  38  TRP A CE3 
310  C CZ2 . TRP A 42  ? 0.4206 0.2901 0.2661 0.0168  0.0716  0.0183  38  TRP A CZ2 
311  C CZ3 . TRP A 42  ? 0.4042 0.2878 0.2767 0.0096  0.0648  0.0152  38  TRP A CZ3 
312  C CH2 . TRP A 42  ? 0.4394 0.3139 0.2919 0.0167  0.0663  0.0184  38  TRP A CH2 
313  N N   . VAL A 43  ? 0.3052 0.2151 0.2480 -0.0177 0.0876  -0.0116 39  VAL A N   
314  C CA  . VAL A 43  ? 0.2828 0.2051 0.2406 -0.0192 0.0838  -0.0185 39  VAL A CA  
315  C C   . VAL A 43  ? 0.2829 0.2073 0.2357 -0.0180 0.0806  -0.0207 39  VAL A C   
316  O O   . VAL A 43  ? 0.2888 0.2081 0.2354 -0.0184 0.0866  -0.0211 39  VAL A O   
317  C CB  . VAL A 43  ? 0.3072 0.2340 0.2808 -0.0228 0.0920  -0.0251 39  VAL A CB  
318  C CG1 . VAL A 43  ? 0.2792 0.2201 0.2666 -0.0222 0.0868  -0.0329 39  VAL A CG1 
319  C CG2 . VAL A 43  ? 0.3127 0.2358 0.2917 -0.0243 0.0964  -0.0233 39  VAL A CG2 
320  N N   . LYS A 44  ? 0.2784 0.2091 0.2328 -0.0165 0.0717  -0.0219 40  LYS A N   
321  C CA  . LYS A 44  ? 0.2667 0.1991 0.2175 -0.0151 0.0682  -0.0246 40  LYS A CA  
322  C C   . LYS A 44  ? 0.2667 0.2085 0.2297 -0.0144 0.0666  -0.0313 40  LYS A C   
323  O O   . LYS A 44  ? 0.2689 0.2168 0.2406 -0.0138 0.0637  -0.0324 40  LYS A O   
324  C CB  . LYS A 44  ? 0.2702 0.2009 0.2125 -0.0135 0.0599  -0.0212 40  LYS A CB  
325  C CG  . LYS A 44  ? 0.2719 0.1953 0.2008 -0.0125 0.0594  -0.0163 40  LYS A CG  
326  C CD  . LYS A 44  ? 0.2710 0.1955 0.1952 -0.0116 0.0512  -0.0154 40  LYS A CD  
327  C CE  . LYS A 44  ? 0.2749 0.1948 0.1866 -0.0094 0.0495  -0.0122 40  LYS A CE  
328  N NZ  . LYS A 44  ? 0.3061 0.2290 0.2162 -0.0094 0.0418  -0.0132 40  LYS A NZ  
329  N N   . ARG A 45  ? 0.2756 0.2190 0.2384 -0.0135 0.0680  -0.0359 41  ARG A N   
330  C CA  . ARG A 45  ? 0.2847 0.2363 0.2552 -0.0106 0.0646  -0.0422 41  ARG A CA  
331  C C   . ARG A 45  ? 0.3053 0.2543 0.2690 -0.0079 0.0565  -0.0391 41  ARG A C   
332  O O   . ARG A 45  ? 0.3294 0.2712 0.2825 -0.0086 0.0541  -0.0348 41  ARG A O   
333  C CB  . ARG A 45  ? 0.3104 0.2638 0.2811 -0.0097 0.0682  -0.0482 41  ARG A CB  
334  C CG  . ARG A 45  ? 0.4004 0.3640 0.3806 -0.0056 0.0659  -0.0566 41  ARG A CG  
335  C CD  . ARG A 45  ? 0.5160 0.4832 0.4980 -0.0048 0.0701  -0.0638 41  ARG A CD  
336  N NE  . ARG A 45  ? 0.6294 0.6013 0.6217 -0.0091 0.0793  -0.0685 41  ARG A NE  
337  C CZ  . ARG A 45  ? 0.6720 0.6557 0.6802 -0.0089 0.0820  -0.0771 41  ARG A CZ  
338  N NH1 . ARG A 45  ? 0.6871 0.6797 0.7013 -0.0034 0.0753  -0.0817 41  ARG A NH1 
339  N NH2 . ARG A 45  ? 0.6910 0.6776 0.7091 -0.0140 0.0918  -0.0816 41  ARG A NH2 
340  N N   . VAL A 46  ? 0.2965 0.2765 0.2443 0.0740  0.0657  -0.0328 42  VAL A N   
341  C CA  . VAL A 46  ? 0.3241 0.2718 0.2492 0.0764  0.0603  -0.0343 42  VAL A CA  
342  C C   . VAL A 46  ? 0.3375 0.2861 0.2513 0.0961  0.0616  -0.0340 42  VAL A C   
343  O O   . VAL A 46  ? 0.3659 0.3465 0.2985 0.1024  0.0643  -0.0323 42  VAL A O   
344  C CB  . VAL A 46  ? 0.2872 0.2374 0.2260 0.0614  0.0543  -0.0347 42  VAL A CB  
345  C CG1 . VAL A 46  ? 0.3341 0.2542 0.2501 0.0637  0.0484  -0.0348 42  VAL A CG1 
346  C CG2 . VAL A 46  ? 0.2845 0.2321 0.2338 0.0433  0.0531  -0.0347 42  VAL A CG2 
347  N N   . GLY A 47  ? 0.4127 0.3257 0.2957 0.1057  0.0593  -0.0352 43  GLY A N   
348  C CA  . GLY A 47  ? 0.4982 0.4066 0.3682 0.1249  0.0594  -0.0349 43  GLY A CA  
349  C C   . GLY A 47  ? 0.4618 0.3384 0.3120 0.1239  0.0511  -0.0348 43  GLY A C   
350  O O   . GLY A 47  ? 0.5074 0.3499 0.3373 0.1157  0.0462  -0.0356 43  GLY A O   
351  N N   . GLY A 48  ? 0.4594 0.3471 0.3152 0.1315  0.0488  -0.0331 44  GLY A N   
352  C CA  . GLY A 48  ? 0.4495 0.3073 0.2849 0.1327  0.0406  -0.0320 44  GLY A CA  
353  C C   . GLY A 48  ? 0.4444 0.2954 0.2846 0.1123  0.0335  -0.0308 44  GLY A C   
354  O O   . GLY A 48  ? 0.5167 0.3370 0.3358 0.1101  0.0259  -0.0292 44  GLY A O   
355  N N   . LYS A 49  ? 0.3951 0.2739 0.2622 0.0976  0.0353  -0.0313 45  LYS A N   
356  C CA  . LYS A 49  ? 0.3693 0.2456 0.2429 0.0791  0.0299  -0.0306 45  LYS A CA  
357  C C   . LYS A 49  ? 0.3534 0.2652 0.2538 0.0744  0.0302  -0.0306 45  LYS A C   
358  O O   . LYS A 49  ? 0.3298 0.2718 0.2500 0.0789  0.0354  -0.0315 45  LYS A O   
359  C CB  . LYS A 49  ? 0.3967 0.2698 0.2763 0.0645  0.0315  -0.0318 45  LYS A CB  
360  C CG  . LYS A 49  ? 0.4434 0.2838 0.2979 0.0670  0.0315  -0.0318 45  LYS A CG  
361  C CD  . LYS A 49  ? 0.4832 0.2840 0.3077 0.0661  0.0233  -0.0294 45  LYS A CD  
362  C CE  . LYS A 49  ? 0.5408 0.3080 0.3401 0.0653  0.0223  -0.0296 45  LYS A CE  
363  N NZ  . LYS A 49  ? 0.6657 0.4259 0.4504 0.0844  0.0278  -0.0327 45  LYS A NZ  
364  N N   . THR A 50  ? 0.3355 0.2442 0.2359 0.0647  0.0243  -0.0293 46  THR A N   
365  C CA  . THR A 50  ? 0.3025 0.2421 0.2256 0.0585  0.0240  -0.0301 46  THR A CA  
366  C C   . THR A 50  ? 0.2644 0.2052 0.1959 0.0405  0.0217  -0.0313 46  THR A C   
367  O O   . THR A 50  ? 0.2979 0.2149 0.2161 0.0330  0.0189  -0.0298 46  THR A O   
368  C CB  . THR A 50  ? 0.3421 0.2829 0.2583 0.0658  0.0194  -0.0272 46  THR A CB  
369  O OG1 . THR A 50  ? 0.3672 0.2789 0.2623 0.0609  0.0124  -0.0242 46  THR A OG1 
370  C CG2 . THR A 50  ? 0.3620 0.3036 0.2713 0.0852  0.0217  -0.0255 46  THR A CG2 
371  N N   . SER A 51  ? 0.2537 0.2227 0.2068 0.0339  0.0224  -0.0337 47  SER A N   
372  C CA  . SER A 51  ? 0.2376 0.2105 0.1987 0.0191  0.0204  -0.0353 47  SER A CA  
373  C C   . SER A 51  ? 0.2321 0.2287 0.2051 0.0170  0.0187  -0.0368 47  SER A C   
374  O O   . SER A 51  ? 0.2185 0.2300 0.1958 0.0256  0.0189  -0.0363 47  SER A O   
375  C CB  . SER A 51  ? 0.2655 0.2453 0.2425 0.0099  0.0243  -0.0385 47  SER A CB  
376  O OG  . SER A 51  ? 0.2774 0.2529 0.2566 -0.0027 0.0224  -0.0389 47  SER A OG  
377  N N   . LEU A 52  ? 0.2367 0.2375 0.2146 0.0055  0.0169  -0.0384 48  LEU A N   
378  C CA  . LEU A 52  ? 0.2245 0.2468 0.2120 0.0018  0.0153  -0.0408 48  LEU A CA  
379  C C   . LEU A 52  ? 0.2233 0.2692 0.2337 -0.0033 0.0186  -0.0470 48  LEU A C   
380  O O   . LEU A 52  ? 0.2967 0.3408 0.3162 -0.0091 0.0214  -0.0498 48  LEU A O   
381  C CB  . LEU A 52  ? 0.2872 0.3034 0.2674 -0.0077 0.0120  -0.0395 48  LEU A CB  
382  C CG  . LEU A 52  ? 0.3253 0.3192 0.2827 -0.0051 0.0067  -0.0323 48  LEU A CG  
383  C CD1 . LEU A 52  ? 0.3554 0.3427 0.3076 -0.0165 0.0044  -0.0300 48  LEU A CD1 
384  C CD2 . LEU A 52  ? 0.3636 0.3666 0.3165 0.0013  0.0031  -0.0300 48  LEU A CD2 
385  N N   . SER A 53  ? 0.2101 0.2773 0.2292 -0.0017 0.0175  -0.0488 49  SER A N   
386  C CA  . SER A 53  ? 0.1859 0.2748 0.2251 -0.0067 0.0191  -0.0544 49  SER A CA  
387  C C   . SER A 53  ? 0.2058 0.3119 0.2474 -0.0093 0.0158  -0.0565 49  SER A C   
388  O O   . SER A 53  ? 0.2085 0.3109 0.2374 -0.0065 0.0128  -0.0529 49  SER A O   
389  C CB  . SER A 53  ? 0.1968 0.2958 0.2450 0.0004  0.0213  -0.0525 49  SER A CB  
390  O OG  . SER A 53  ? 0.2060 0.3137 0.2495 0.0100  0.0195  -0.0481 49  SER A OG  
391  N N   . VAL A 54  ? 0.1633 0.2872 0.2204 -0.0152 0.0158  -0.0622 50  VAL A N   
392  C CA  . VAL A 54  ? 0.1633 0.3048 0.2229 -0.0185 0.0125  -0.0649 50  VAL A CA  
393  C C   . VAL A 54  ? 0.1540 0.3154 0.2271 -0.0170 0.0112  -0.0645 50  VAL A C   
394  O O   . VAL A 54  ? 0.1670 0.3329 0.2532 -0.0200 0.0126  -0.0668 50  VAL A O   
395  C CB  . VAL A 54  ? 0.1599 0.3034 0.2224 -0.0283 0.0125  -0.0728 50  VAL A CB  
396  C CG1 . VAL A 54  ? 0.1958 0.3574 0.2596 -0.0318 0.0088  -0.0764 50  VAL A CG1 
397  C CG2 . VAL A 54  ? 0.1868 0.3151 0.2361 -0.0298 0.0133  -0.0711 50  VAL A CG2 
398  N N   . ASN A 55  ? 0.1639 0.3381 0.2340 -0.0127 0.0079  -0.0604 51  ASN A N   
399  C CA  . ASN A 55  ? 0.1614 0.3583 0.2445 -0.0128 0.0056  -0.0588 51  ASN A CA  
400  C C   . ASN A 55  ? 0.1577 0.3648 0.2479 -0.0245 0.0025  -0.0670 51  ASN A C   
401  O O   . ASN A 55  ? 0.1781 0.3863 0.2601 -0.0285 0.0002  -0.0702 51  ASN A O   
402  C CB  . ASN A 55  ? 0.1650 0.3715 0.2418 -0.0045 0.0027  -0.0512 51  ASN A CB  
403  C CG  . ASN A 55  ? 0.1689 0.4011 0.2592 -0.0037 0.0001  -0.0472 51  ASN A CG  
404  O OD1 . ASN A 55  ? 0.1600 0.4062 0.2600 -0.0135 -0.0031 -0.0514 51  ASN A OD1 
405  N ND2 . ASN A 55  ? 0.2151 0.4532 0.3053 0.0083  0.0011  -0.0385 51  ASN A ND2 
406  N N   . THR A 56  ? 0.1645 0.3778 0.2688 -0.0303 0.0024  -0.0705 52  THR A N   
407  C CA  . THR A 56  ? 0.1927 0.4106 0.3019 -0.0412 -0.0008 -0.0795 52  THR A CA  
408  C C   . THR A 56  ? 0.2014 0.4392 0.3124 -0.0449 -0.0069 -0.0787 52  THR A C   
409  O O   . THR A 56  ? 0.2373 0.4776 0.3481 -0.0536 -0.0103 -0.0867 52  THR A O   
410  C CB  . THR A 56  ? 0.2129 0.4281 0.3358 -0.0471 -0.0003 -0.0836 52  THR A CB  
411  O OG1 . THR A 56  ? 0.2881 0.5181 0.4230 -0.0457 -0.0019 -0.0766 52  THR A OG1 
412  C CG2 . THR A 56  ? 0.2617 0.4571 0.3825 -0.0449 0.0052  -0.0847 52  THR A CG2 
413  N N   . TYR A 57  ? 0.1366 0.3887 0.2493 -0.0385 -0.0085 -0.0693 53  TYR A N   
414  C CA  . TYR A 57  ? 0.1657 0.4377 0.2796 -0.0423 -0.0148 -0.0670 53  TYR A CA  
415  C C   . TYR A 57  ? 0.2099 0.4804 0.3088 -0.0404 -0.0161 -0.0667 53  TYR A C   
416  O O   . TYR A 57  ? 0.2075 0.4847 0.3021 -0.0483 -0.0205 -0.0718 53  TYR A O   
417  C CB  . TYR A 57  ? 0.1643 0.4560 0.2891 -0.0365 -0.0162 -0.0559 53  TYR A CB  
418  C CG  . TYR A 57  ? 0.1781 0.4923 0.3062 -0.0422 -0.0235 -0.0526 53  TYR A CG  
419  C CD1 . TYR A 57  ? 0.1788 0.5013 0.3149 -0.0546 -0.0292 -0.0566 53  TYR A CD1 
420  C CD2 . TYR A 57  ? 0.1837 0.5083 0.3057 -0.0358 -0.0255 -0.0450 53  TYR A CD2 
421  C CE1 . TYR A 57  ? 0.1963 0.5318 0.3310 -0.0600 -0.0359 -0.0525 53  TYR A CE1 
422  C CE2 . TYR A 57  ? 0.1622 0.5082 0.2875 -0.0418 -0.0326 -0.0411 53  TYR A CE2 
423  C CZ  . TYR A 57  ? 0.1871 0.5406 0.3193 -0.0547 -0.0381 -0.0452 53  TYR A CZ  
424  O OH  . TYR A 57  ? 0.2461 0.6120 0.3770 -0.0607 -0.0449 -0.0404 53  TYR A OH  
425  N N   . SER A 58  ? 0.1814 0.4422 0.2712 -0.0304 -0.0129 -0.0607 54  SER A N   
426  C CA  . SER A 58  ? 0.2081 0.4671 0.2837 -0.0288 -0.0149 -0.0586 54  SER A CA  
427  C C   . SER A 58  ? 0.2477 0.4902 0.3121 -0.0334 -0.0125 -0.0662 54  SER A C   
428  O O   . SER A 58  ? 0.2304 0.4754 0.2840 -0.0363 -0.0150 -0.0667 54  SER A O   
429  C CB  . SER A 58  ? 0.2229 0.4771 0.2927 -0.0159 -0.0138 -0.0481 54  SER A CB  
430  O OG  . SER A 58  ? 0.2135 0.4454 0.2778 -0.0108 -0.0086 -0.0488 54  SER A OG  
431  N N   . GLY A 59  ? 0.1988 0.4263 0.2659 -0.0345 -0.0079 -0.0713 55  GLY A N   
432  C CA  . GLY A 59  ? 0.2054 0.4185 0.2632 -0.0378 -0.0050 -0.0767 55  GLY A CA  
433  C C   . GLY A 59  ? 0.2816 0.4799 0.3267 -0.0314 -0.0035 -0.0697 55  GLY A C   
434  O O   . GLY A 59  ? 0.3032 0.4923 0.3397 -0.0347 -0.0019 -0.0720 55  GLY A O   
435  N N   . GLU A 60  ? 0.2545 0.4501 0.2979 -0.0223 -0.0041 -0.0609 56  GLU A N   
436  C CA  . GLU A 60  ? 0.2904 0.4698 0.3195 -0.0158 -0.0044 -0.0536 56  GLU A CA  
437  C C   . GLU A 60  ? 0.2382 0.3975 0.2664 -0.0115 -0.0001 -0.0526 56  GLU A C   
438  O O   . GLU A 60  ? 0.2152 0.3766 0.2545 -0.0090 0.0027  -0.0538 56  GLU A O   
439  C CB  . GLU A 60  ? 0.3284 0.5147 0.3546 -0.0068 -0.0081 -0.0447 56  GLU A CB  
440  C CG  . GLU A 60  ? 0.5003 0.7080 0.5277 -0.0109 -0.0131 -0.0439 56  GLU A CG  
441  C CD  . GLU A 60  ? 0.6139 0.8178 0.6265 -0.0142 -0.0167 -0.0412 56  GLU A CD  
442  O OE1 . GLU A 60  ? 0.6860 0.8711 0.6865 -0.0097 -0.0170 -0.0359 56  GLU A OE1 
443  O OE2 . GLU A 60  ? 0.6793 0.8989 0.6914 -0.0218 -0.0198 -0.0441 56  GLU A OE2 
444  N N   . VAL A 61  ? 0.2411 0.3072 0.2561 0.0122  -0.0024 -0.0354 57  VAL A N   
445  C CA  . VAL A 61  ? 0.2612 0.3184 0.2691 0.0150  -0.0009 -0.0306 57  VAL A CA  
446  C C   . VAL A 61  ? 0.2638 0.3197 0.2721 0.0187  -0.0034 -0.0322 57  VAL A C   
447  O O   . VAL A 61  ? 0.2894 0.3481 0.2976 0.0199  -0.0104 -0.0342 57  VAL A O   
448  C CB  . VAL A 61  ? 0.3057 0.3581 0.3019 0.0144  -0.0061 -0.0248 57  VAL A CB  
449  C CG1 . VAL A 61  ? 0.3150 0.3589 0.3035 0.0176  -0.0060 -0.0202 57  VAL A CG1 
450  C CG2 . VAL A 61  ? 0.3327 0.3869 0.3293 0.0112  -0.0027 -0.0240 57  VAL A CG2 
451  N N   . GLU A 62  ? 0.2317 0.2837 0.2408 0.0206  0.0023  -0.0317 58  GLU A N   
452  C CA  . GLU A 62  ? 0.2697 0.3213 0.2797 0.0242  0.0007  -0.0339 58  GLU A CA  
453  C C   . GLU A 62  ? 0.2366 0.2804 0.2393 0.0261  0.0031  -0.0292 58  GLU A C   
454  O O   . GLU A 62  ? 0.2627 0.3030 0.2644 0.0246  0.0098  -0.0266 58  GLU A O   
455  C CB  . GLU A 62  ? 0.2801 0.3388 0.3019 0.0238  0.0065  -0.0410 58  GLU A CB  
456  C CG  . GLU A 62  ? 0.2731 0.3407 0.3029 0.0223  0.0040  -0.0464 58  GLU A CG  
457  C CD  . GLU A 62  ? 0.2954 0.3709 0.3369 0.0217  0.0097  -0.0540 58  GLU A CD  
458  O OE1 . GLU A 62  ? 0.3165 0.3907 0.3606 0.0202  0.0180  -0.0546 58  GLU A OE1 
459  O OE2 . GLU A 62  ? 0.3677 0.4508 0.4154 0.0224  0.0056  -0.0595 58  GLU A OE2 
460  N N   . ARG A 63  ? 0.2574 0.2984 0.2554 0.0295  -0.0026 -0.0285 59  ARG A N   
461  C CA  . ARG A 63  ? 0.2597 0.2945 0.2515 0.0316  -0.0006 -0.0250 59  ARG A CA  
462  C C   . ARG A 63  ? 0.2773 0.3161 0.2765 0.0327  0.0049  -0.0302 59  ARG A C   
463  O O   . ARG A 63  ? 0.3133 0.3581 0.3192 0.0345  0.0019  -0.0363 59  ARG A O   
464  C CB  . ARG A 63  ? 0.3439 0.3739 0.3270 0.0345  -0.0096 -0.0221 59  ARG A CB  
465  C CG  . ARG A 63  ? 0.3262 0.3503 0.3027 0.0367  -0.0081 -0.0187 59  ARG A CG  
466  C CD  . ARG A 63  ? 0.3175 0.3352 0.2835 0.0384  -0.0166 -0.0143 59  ARG A CD  
467  N NE  . ARG A 63  ? 0.3252 0.3397 0.2837 0.0353  -0.0175 -0.0089 59  ARG A NE  
468  C CZ  . ARG A 63  ? 0.3166 0.3272 0.2697 0.0344  -0.0129 -0.0043 59  ARG A CZ  
469  N NH1 . ARG A 63  ? 0.3099 0.3189 0.2637 0.0358  -0.0068 -0.0038 59  ARG A NH1 
470  N NH2 . ARG A 63  ? 0.2962 0.3054 0.2434 0.0318  -0.0144 -0.0005 59  ARG A NH2 
471  N N   . LYS A 64  ? 0.2248 0.2607 0.2230 0.0313  0.0127  -0.0282 60  LYS A N   
472  C CA  . LYS A 64  ? 0.2576 0.2979 0.2626 0.0306  0.0195  -0.0331 60  LYS A CA  
473  C C   . LYS A 64  ? 0.2376 0.2728 0.2362 0.0313  0.0230  -0.0297 60  LYS A C   
474  O O   . LYS A 64  ? 0.2724 0.3001 0.2621 0.0315  0.0227  -0.0230 60  LYS A O   
475  C CB  . LYS A 64  ? 0.2228 0.2653 0.2340 0.0261  0.0274  -0.0347 60  LYS A CB  
476  C CG  . LYS A 64  ? 0.2519 0.3016 0.2715 0.0249  0.0255  -0.0397 60  LYS A CG  
477  C CD  . LYS A 64  ? 0.3001 0.3589 0.3284 0.0264  0.0243  -0.0479 60  LYS A CD  
478  C CE  . LYS A 64  ? 0.3408 0.4077 0.3788 0.0243  0.0249  -0.0536 60  LYS A CE  
479  N NZ  . LYS A 64  ? 0.3778 0.4543 0.4247 0.0258  0.0249  -0.0622 60  LYS A NZ  
480  N N   . ASN A 65  ? 0.2298 0.2699 0.2331 0.0315  0.0266  -0.0348 61  ASN A N   
481  C CA  . ASN A 65  ? 0.2298 0.2663 0.2272 0.0317  0.0302  -0.0321 61  ASN A CA  
482  C C   . ASN A 65  ? 0.2395 0.2698 0.2324 0.0277  0.0380  -0.0267 61  ASN A C   
483  O O   . ASN A 65  ? 0.2565 0.2879 0.2542 0.0240  0.0433  -0.0280 61  ASN A O   
484  C CB  . ASN A 65  ? 0.2733 0.3183 0.2777 0.0319  0.0331  -0.0399 61  ASN A CB  
485  C CG  . ASN A 65  ? 0.3812 0.4311 0.3892 0.0370  0.0247  -0.0452 61  ASN A CG  
486  O OD1 . ASN A 65  ? 0.4852 0.5297 0.4867 0.0405  0.0174  -0.0414 61  ASN A OD1 
487  N ND2 . ASN A 65  ? 0.5226 0.5827 0.5410 0.0373  0.0255  -0.0543 61  ASN A ND2 
488  N N   . ILE A 66  ? 0.2494 0.2728 0.2329 0.0285  0.0384  -0.0206 62  ILE A N   
489  C CA  . ILE A 66  ? 0.2728 0.2898 0.2513 0.0251  0.0455  -0.0155 62  ILE A CA  
490  C C   . ILE A 66  ? 0.2391 0.2599 0.2190 0.0228  0.0516  -0.0190 62  ILE A C   
491  O O   . ILE A 66  ? 0.2672 0.2905 0.2450 0.0252  0.0496  -0.0203 62  ILE A O   
492  C CB  . ILE A 66  ? 0.2405 0.2488 0.2078 0.0271  0.0429  -0.0075 62  ILE A CB  
493  C CG1 . ILE A 66  ? 0.2812 0.2871 0.2466 0.0290  0.0365  -0.0048 62  ILE A CG1 
494  C CG2 . ILE A 66  ? 0.2523 0.2535 0.2142 0.0241  0.0496  -0.0023 62  ILE A CG2 
495  C CD1 . ILE A 66  ? 0.2969 0.2957 0.2515 0.0311  0.0333  0.0022  62  ILE A CD1 
496  N N   . ASN A 67  ? 0.2442 0.2660 0.2279 0.0179  0.0590  -0.0209 63  ASN A N   
497  C CA  . ASN A 67  ? 0.2575 0.2843 0.2428 0.0145  0.0653  -0.0249 63  ASN A CA  
498  C C   . ASN A 67  ? 0.2446 0.2631 0.2196 0.0117  0.0702  -0.0181 63  ASN A C   
499  O O   . ASN A 67  ? 0.2622 0.2843 0.2350 0.0105  0.0729  -0.0198 63  ASN A O   
500  C CB  . ASN A 67  ? 0.2931 0.3256 0.2872 0.0095  0.0712  -0.0309 63  ASN A CB  
501  C CG  . ASN A 67  ? 0.3149 0.3573 0.3198 0.0120  0.0668  -0.0388 63  ASN A CG  
502  O OD1 . ASN A 67  ? 0.3336 0.3811 0.3406 0.0169  0.0604  -0.0420 63  ASN A OD1 
503  N ND2 . ASN A 67  ? 0.3033 0.3482 0.3151 0.0087  0.0699  -0.0419 63  ASN A ND2 
504  N N   . TYR A 68  ? 0.2472 0.2554 0.2165 0.0104  0.0715  -0.0109 64  TYR A N   
505  C CA  . TYR A 68  ? 0.2522 0.2512 0.2115 0.0076  0.0758  -0.0040 64  TYR A CA  
506  C C   . TYR A 68  ? 0.2617 0.2503 0.2143 0.0105  0.0721  0.0038  64  TYR A C   
507  O O   . TYR A 68  ? 0.2488 0.2370 0.2054 0.0126  0.0684  0.0034  64  TYR A O   
508  C CB  . TYR A 68  ? 0.2975 0.2942 0.2578 0.0006  0.0839  -0.0047 64  TYR A CB  
509  C CG  . TYR A 68  ? 0.3000 0.3079 0.2673 -0.0033 0.0885  -0.0131 64  TYR A CG  
510  C CD1 . TYR A 68  ? 0.2888 0.3007 0.2519 -0.0055 0.0917  -0.0143 64  TYR A CD1 
511  C CD2 . TYR A 68  ? 0.3213 0.3370 0.2995 -0.0049 0.0897  -0.0205 64  TYR A CD2 
512  C CE1 . TYR A 68  ? 0.3727 0.3965 0.3428 -0.0093 0.0960  -0.0231 64  TYR A CE1 
513  C CE2 . TYR A 68  ? 0.3191 0.3465 0.3043 -0.0084 0.0938  -0.0291 64  TYR A CE2 
514  C CZ  . TYR A 68  ? 0.3344 0.3660 0.3156 -0.0107 0.0970  -0.0306 64  TYR A CZ  
515  O OH  . TYR A 68  ? 0.3961 0.4407 0.3846 -0.0143 0.1012  -0.0400 64  TYR A OH  
516  N N   . ILE A 69  ? 0.2759 0.2567 0.2183 0.0104  0.0733  0.0105  65  ILE A N   
517  C CA  . ILE A 69  ? 0.2445 0.2149 0.1800 0.0125  0.0709  0.0178  65  ILE A CA  
518  C C   . ILE A 69  ? 0.2849 0.2456 0.2128 0.0084  0.0764  0.0232  65  ILE A C   
519  O O   . ILE A 69  ? 0.2855 0.2471 0.2090 0.0052  0.0804  0.0235  65  ILE A O   
520  C CB  . ILE A 69  ? 0.2668 0.2369 0.1964 0.0180  0.0645  0.0210  65  ILE A CB  
521  C CG1 . ILE A 69  ? 0.2905 0.2515 0.2143 0.0202  0.0620  0.0274  65  ILE A CG1 
522  C CG2 . ILE A 69  ? 0.2896 0.2612 0.2127 0.0179  0.0659  0.0223  65  ILE A CG2 
523  C CD1 . ILE A 69  ? 0.3893 0.3512 0.3098 0.0251  0.0552  0.0292  65  ILE A CD1 
524  N N   . MET A 70  ? 0.3185 0.2700 0.2450 0.0082  0.0764  0.0271  66  MET A N   
525  C CA  . MET A 70  ? 0.3229 0.2632 0.2425 0.0041  0.0809  0.0324  66  MET A CA  
526  C C   . MET A 70  ? 0.3122 0.2422 0.2238 0.0081  0.0770  0.0396  66  MET A C   
527  O O   . MET A 70  ? 0.2978 0.2288 0.2123 0.0128  0.0718  0.0394  66  MET A O   
528  C CB  . MET A 70  ? 0.4383 0.3759 0.3647 -0.0002 0.0846  0.0297  66  MET A CB  
529  C CG  . MET A 70  ? 0.6040 0.5499 0.5364 -0.0058 0.0902  0.0232  66  MET A CG  
530  S SD  . MET A 70  ? 0.7319 0.6854 0.6785 -0.0059 0.0896  0.0155  66  MET A SD  
531  C CE  . MET A 70  ? 0.5865 0.5501 0.5368 0.0016  0.0817  0.0129  66  MET A CE  
532  N N   . LYS A 71  ? 0.3383 0.2587 0.2401 0.0060  0.0794  0.0457  67  LYS A N   
533  C CA  . LYS A 71  ? 0.3245 0.2339 0.2182 0.0094  0.0761  0.0526  67  LYS A CA  
534  C C   . LYS A 71  ? 0.3522 0.2486 0.2398 0.0045  0.0802  0.0573  67  LYS A C   
535  O O   . LYS A 71  ? 0.3584 0.2541 0.2416 -0.0012 0.0854  0.0579  67  LYS A O   
536  C CB  . LYS A 71  ? 0.3463 0.2571 0.2312 0.0127  0.0736  0.0564  67  LYS A CB  
537  C CG  . LYS A 71  ? 0.3875 0.2877 0.2632 0.0163  0.0702  0.0635  67  LYS A CG  
538  C CD  . LYS A 71  ? 0.3767 0.2792 0.2437 0.0188  0.0684  0.0669  67  LYS A CD  
539  C CE  . LYS A 71  ? 0.4233 0.3155 0.2811 0.0224  0.0650  0.0738  67  LYS A CE  
540  N NZ  . LYS A 71  ? 0.4671 0.3620 0.3164 0.0248  0.0634  0.0769  67  LYS A NZ  
541  N N   . HIS A 72  ? 0.3526 0.2387 0.2399 0.0065  0.0778  0.0601  68  HIS A N   
542  C CA  . HIS A 72  ? 0.3958 0.2668 0.2759 0.0027  0.0803  0.0655  68  HIS A CA  
543  C C   . HIS A 72  ? 0.3716 0.2318 0.2467 0.0085  0.0747  0.0708  68  HIS A C   
544  O O   . HIS A 72  ? 0.4033 0.2664 0.2854 0.0136  0.0704  0.0680  68  HIS A O   
545  C CB  . HIS A 72  ? 0.4887 0.3568 0.3762 -0.0026 0.0844  0.0618  68  HIS A CB  
546  C CG  . HIS A 72  ? 0.7287 0.5812 0.6080 -0.0084 0.0878  0.0671  68  HIS A CG  
547  N ND1 . HIS A 72  ? 0.8021 0.6475 0.6861 -0.0125 0.0904  0.0653  68  HIS A ND1 
548  C CD2 . HIS A 72  ? 0.7958 0.6379 0.6618 -0.0111 0.0889  0.0742  68  HIS A CD2 
549  C CE1 . HIS A 72  ? 0.8056 0.6359 0.6792 -0.0177 0.0927  0.0714  68  HIS A CE1 
550  N NE2 . HIS A 72  ? 0.8102 0.6383 0.6725 -0.0170 0.0918  0.0770  68  HIS A NE2 
551  N N   . THR A 73  ? 0.4258 0.2736 0.2891 0.0075  0.0748  0.0780  69  THR A N   
552  C CA  . THR A 73  ? 0.4543 0.2905 0.3128 0.0129  0.0693  0.0829  69  THR A CA  
553  C C   . THR A 73  ? 0.4903 0.3126 0.3499 0.0098  0.0705  0.0840  69  THR A C   
554  O O   . THR A 73  ? 0.5553 0.3690 0.4090 0.0027  0.0752  0.0869  69  THR A O   
555  C CB  . THR A 73  ? 0.4555 0.2850 0.3001 0.0139  0.0679  0.0904  69  THR A CB  
556  O OG1 . THR A 73  ? 0.5251 0.3678 0.3689 0.0158  0.0677  0.0888  69  THR A OG1 
557  C CG2 . THR A 73  ? 0.5301 0.3495 0.3708 0.0209  0.0613  0.0944  69  THR A CG2 
558  N N   . VAL A 74  ? 0.5188 0.3393 0.3862 0.0146  0.0663  0.0812  70  VAL A N   
559  C CA  . VAL A 74  ? 0.5564 0.3657 0.4279 0.0122  0.0671  0.0804  70  VAL A CA  
560  C C   . VAL A 74  ? 0.4974 0.2957 0.3674 0.0192  0.0603  0.0830  70  VAL A C   
561  O O   . VAL A 74  ? 0.5029 0.3068 0.3727 0.0261  0.0551  0.0830  70  VAL A O   
562  C CB  . VAL A 74  ? 0.5664 0.3870 0.4526 0.0107  0.0693  0.0718  70  VAL A CB  
563  C CG1 . VAL A 74  ? 0.5712 0.4043 0.4599 0.0049  0.0752  0.0683  70  VAL A CG1 
564  C CG2 . VAL A 74  ? 0.5970 0.4286 0.4919 0.0181  0.0638  0.0670  70  VAL A CG2 
565  N N   . LYS A 75  ? 0.5807 0.3635 0.4500 0.0172  0.0601  0.0848  71  LYS A N   
566  C CA  . LYS A 75  ? 0.4663 0.2395 0.3380 0.0239  0.0536  0.0850  71  LYS A CA  
567  C C   . LYS A 75  ? 0.5478 0.3228 0.4328 0.0224  0.0549  0.0780  71  LYS A C   
568  O O   . LYS A 75  ? 0.6081 0.3724 0.4926 0.0162  0.0586  0.0787  71  LYS A O   
569  C CB  . LYS A 75  ? 0.4877 0.2389 0.3466 0.0236  0.0510  0.0933  71  LYS A CB  
570  C CG  . LYS A 75  ? 0.5848 0.3267 0.4462 0.0319  0.0431  0.0930  71  LYS A CG  
571  C CD  . LYS A 75  ? 0.7022 0.4222 0.5500 0.0329  0.0392  0.1018  71  LYS A CD  
572  C CE  . LYS A 75  ? 0.7934 0.5097 0.6431 0.0435  0.0302  0.1010  71  LYS A CE  
573  N NZ  . LYS A 75  ? 0.8205 0.5127 0.6627 0.0451  0.0252  0.1066  71  LYS A NZ  
574  N N   . LYS A 76  ? 0.4859 0.2749 0.3824 0.0274  0.0521  0.0710  72  LYS A N   
575  C CA  . LYS A 76  ? 0.5200 0.3154 0.4299 0.0253  0.0542  0.0633  72  LYS A CA  
576  C C   . LYS A 76  ? 0.5095 0.3122 0.4292 0.0327  0.0482  0.0576  72  LYS A C   
577  O O   . LYS A 76  ? 0.4224 0.2307 0.3396 0.0387  0.0434  0.0582  72  LYS A O   
578  C CB  . LYS A 76  ? 0.5336 0.3460 0.4493 0.0205  0.0596  0.0587  72  LYS A CB  
579  C CG  . LYS A 76  ? 0.6285 0.4368 0.5385 0.0119  0.0666  0.0615  72  LYS A CG  
580  C CD  . LYS A 76  ? 0.6906 0.4916 0.6064 0.0061  0.0705  0.0586  72  LYS A CD  
581  C CE  . LYS A 76  ? 0.7239 0.5285 0.6378 -0.0028 0.0782  0.0581  72  LYS A CE  
582  N NZ  . LYS A 76  ? 0.7167 0.5421 0.6380 -0.0028 0.0801  0.0522  72  LYS A NZ  
583  N N   . ARG A 77  ? 0.4749 0.2777 0.4056 0.0316  0.0487  0.0516  73  ARG A N   
584  C CA  . ARG A 77  ? 0.4966 0.3097 0.4388 0.0371  0.0443  0.0442  73  ARG A CA  
585  C C   . ARG A 77  ? 0.4272 0.2619 0.3753 0.0368  0.0453  0.0393  73  ARG A C   
586  O O   . ARG A 77  ? 0.4156 0.2578 0.3663 0.0312  0.0505  0.0375  73  ARG A O   
587  C CB  . ARG A 77  ? 0.5713 0.3800 0.5241 0.0345  0.0458  0.0389  73  ARG A CB  
588  C CG  . ARG A 77  ? 0.6503 0.4692 0.6157 0.0396  0.0414  0.0306  73  ARG A CG  
589  C CD  . ARG A 77  ? 0.7989 0.6063 0.7620 0.0468  0.0345  0.0320  73  ARG A CD  
590  N NE  . ARG A 77  ? 0.8913 0.6787 0.8538 0.0453  0.0345  0.0339  73  ARG A NE  
591  C CZ  . ARG A 77  ? 0.9185 0.7043 0.8924 0.0453  0.0340  0.0273  73  ARG A CZ  
592  N NH1 . ARG A 77  ? 0.9178 0.7221 0.9048 0.0465  0.0337  0.0182  73  ARG A NH1 
593  N NH2 . ARG A 77  ? 0.9449 0.7107 0.9169 0.0437  0.0338  0.0297  73  ARG A NH2 
594  N N   . MET A 78  ? 0.3931 0.2376 0.3428 0.0427  0.0401  0.0368  74  MET A N   
595  C CA  . MET A 78  ? 0.3578 0.2215 0.3112 0.0426  0.0401  0.0329  74  MET A CA  
596  C C   . MET A 78  ? 0.3646 0.2404 0.3301 0.0449  0.0369  0.0244  74  MET A C   
597  O O   . MET A 78  ? 0.3634 0.2353 0.3322 0.0496  0.0325  0.0221  74  MET A O   
598  C CB  . MET A 78  ? 0.3640 0.2307 0.3076 0.0463  0.0370  0.0373  74  MET A CB  
599  C CG  . MET A 78  ? 0.4067 0.2617 0.3377 0.0445  0.0394  0.0458  74  MET A CG  
600  S SD  . MET A 78  ? 0.4026 0.2615 0.3324 0.0366  0.0469  0.0467  74  MET A SD  
601  C CE  . MET A 78  ? 0.3587 0.2380 0.2916 0.0376  0.0455  0.0427  74  MET A CE  
602  N N   . PHE A 79  ? 0.2943 0.1854 0.2663 0.0418  0.0388  0.0195  75  PHE A N   
603  C CA  . PHE A 79  ? 0.2954 0.2003 0.2781 0.0428  0.0362  0.0113  75  PHE A CA  
604  C C   . PHE A 79  ? 0.2773 0.1981 0.2583 0.0426  0.0344  0.0099  75  PHE A C   
605  O O   . PHE A 79  ? 0.2906 0.2141 0.2666 0.0398  0.0369  0.0131  75  PHE A O   
606  C CB  . PHE A 79  ? 0.2882 0.1965 0.2818 0.0380  0.0401  0.0057  75  PHE A CB  
607  C CG  . PHE A 79  ? 0.2828 0.1772 0.2804 0.0382  0.0410  0.0051  75  PHE A CG  
608  C CD1 . PHE A 79  ? 0.3622 0.2416 0.3543 0.0348  0.0452  0.0105  75  PHE A CD1 
609  C CD2 . PHE A 79  ? 0.3431 0.2391 0.3495 0.0414  0.0375  -0.0010 75  PHE A CD2 
610  C CE1 . PHE A 79  ? 0.4073 0.2720 0.4020 0.0346  0.0457  0.0104  75  PHE A CE1 
611  C CE2 . PHE A 79  ? 0.3711 0.2528 0.3811 0.0419  0.0377  -0.0016 75  PHE A CE2 
612  C CZ  . PHE A 79  ? 0.4236 0.2889 0.4273 0.0383  0.0417  0.0044  75  PHE A CZ  
613  N N   . LYS A 80  ? 0.2668 0.1981 0.2520 0.0454  0.0300  0.0049  76  LYS A N   
614  C CA  . LYS A 80  ? 0.2615 0.2082 0.2455 0.0444  0.0279  0.0028  76  LYS A CA  
615  C C   . LYS A 80  ? 0.2389 0.1988 0.2338 0.0408  0.0284  -0.0048 76  LYS A C   
616  O O   . LYS A 80  ? 0.2517 0.2141 0.2554 0.0417  0.0272  -0.0107 76  LYS A O   
617  C CB  . LYS A 80  ? 0.2992 0.2504 0.2789 0.0490  0.0226  0.0025  76  LYS A CB  
618  C CG  . LYS A 80  ? 0.3543 0.3207 0.3317 0.0472  0.0202  0.0004  76  LYS A CG  
619  C CD  . LYS A 80  ? 0.4700 0.4422 0.4447 0.0512  0.0152  -0.0016 76  LYS A CD  
620  C CE  . LYS A 80  ? 0.5120 0.4743 0.4756 0.0551  0.0141  0.0055  76  LYS A CE  
621  N NZ  . LYS A 80  ? 0.5362 0.5039 0.4981 0.0595  0.0093  0.0029  76  LYS A NZ  
622  N N   . ILE A 81  ? 0.2279 0.1963 0.2221 0.0369  0.0298  -0.0051 77  ILE A N   
623  C CA  . ILE A 81  ? 0.2409 0.2230 0.2438 0.0332  0.0296  -0.0118 77  ILE A CA  
624  C C   . ILE A 81  ? 0.2302 0.2249 0.2293 0.0332  0.0250  -0.0133 77  ILE A C   
625  O O   . ILE A 81  ? 0.2358 0.2305 0.2258 0.0332  0.0239  -0.0087 77  ILE A O   
626  C CB  . ILE A 81  ? 0.2562 0.2398 0.2608 0.0288  0.0334  -0.0113 77  ILE A CB  
627  C CG1 . ILE A 81  ? 0.3939 0.3643 0.3998 0.0280  0.0385  -0.0088 77  ILE A CG1 
628  C CG2 . ILE A 81  ? 0.2861 0.2840 0.2997 0.0251  0.0328  -0.0184 77  ILE A CG2 
629  C CD1 . ILE A 81  ? 0.4010 0.3664 0.4154 0.0285  0.0397  -0.0128 77  ILE A CD1 
630  N N   . LYS A 82  ? 0.2109 0.2162 0.2165 0.0329  0.0223  -0.0200 78  LYS A N   
631  C CA  . LYS A 82  ? 0.1994 0.2173 0.2012 0.0320  0.0180  -0.0221 78  LYS A CA  
632  C C   . LYS A 82  ? 0.2093 0.2411 0.2171 0.0266  0.0176  -0.0277 78  LYS A C   
633  O O   . LYS A 82  ? 0.2203 0.2568 0.2386 0.0252  0.0188  -0.0339 78  LYS A O   
634  C CB  . LYS A 82  ? 0.2358 0.2568 0.2400 0.0356  0.0148  -0.0262 78  LYS A CB  
635  C CG  . LYS A 82  ? 0.2677 0.2747 0.2666 0.0413  0.0146  -0.0212 78  LYS A CG  
636  C CD  . LYS A 82  ? 0.3237 0.3343 0.3256 0.0457  0.0108  -0.0259 78  LYS A CD  
637  C CE  . LYS A 82  ? 0.4497 0.4729 0.4456 0.0449  0.0070  -0.0275 78  LYS A CE  
638  N NZ  . LYS A 82  ? 0.5812 0.6076 0.5794 0.0498  0.0032  -0.0321 78  LYS A NZ  
639  N N   . ALA A 83  ? 0.1942 0.2324 0.1953 0.0235  0.0156  -0.0258 79  ALA A N   
640  C CA  . ALA A 83  ? 0.2084 0.2589 0.2138 0.0181  0.0147  -0.0303 79  ALA A CA  
641  C C   . ALA A 83  ? 0.1795 0.2374 0.1753 0.0153  0.0104  -0.0285 79  ALA A C   
642  O O   . ALA A 83  ? 0.1998 0.2509 0.1863 0.0165  0.0097  -0.0223 79  ALA A O   
643  C CB  . ALA A 83  ? 0.2177 0.2638 0.2265 0.0164  0.0182  -0.0289 79  ALA A CB  
644  N N   . GLY A 84  ? 0.1785 0.2981 0.2242 0.0242  0.0035  -0.0508 80  GLY A N   
645  C CA  . GLY A 84  ? 0.2043 0.3388 0.2478 0.0249  0.0030  -0.0472 80  GLY A CA  
646  C C   . GLY A 84  ? 0.2053 0.3393 0.2449 0.0246  0.0017  -0.0378 80  GLY A C   
647  O O   . GLY A 84  ? 0.2449 0.3871 0.2819 0.0225  0.0019  -0.0335 80  GLY A O   
648  N N   . GLY A 85  ? 0.1677 0.2920 0.2068 0.0268  0.0003  -0.0345 81  GLY A N   
649  C CA  . GLY A 85  ? 0.1749 0.2973 0.2103 0.0267  -0.0013 -0.0259 81  GLY A CA  
650  C C   . GLY A 85  ? 0.1864 0.2966 0.2164 0.0208  -0.0008 -0.0203 81  GLY A C   
651  O O   . GLY A 85  ? 0.2485 0.3567 0.2752 0.0208  -0.0025 -0.0133 81  GLY A O   
652  N N   . LYS A 86  ? 0.1854 0.2872 0.2145 0.0160  0.0015  -0.0233 82  LYS A N   
653  C CA  . LYS A 86  ? 0.1978 0.2863 0.2218 0.0105  0.0026  -0.0185 82  LYS A CA  
654  C C   . LYS A 86  ? 0.1730 0.2444 0.1971 0.0105  0.0037  -0.0203 82  LYS A C   
655  O O   . LYS A 86  ? 0.1796 0.2502 0.2086 0.0135  0.0040  -0.0267 82  LYS A O   
656  C CB  . LYS A 86  ? 0.2279 0.3196 0.2511 0.0047  0.0049  -0.0203 82  LYS A CB  
657  C CG  . LYS A 86  ? 0.2789 0.3869 0.3014 0.0044  0.0042  -0.0186 82  LYS A CG  
658  C CD  . LYS A 86  ? 0.3763 0.4854 0.3946 0.0043  0.0022  -0.0099 82  LYS A CD  
659  C CE  . LYS A 86  ? 0.4805 0.5826 0.4931 -0.0018 0.0032  -0.0050 82  LYS A CE  
660  N NZ  . LYS A 86  ? 0.5030 0.6107 0.5125 -0.0016 0.0009  0.0024  82  LYS A NZ  
661  N N   . GLU A 87  ? 0.1932 0.2504 0.2118 0.0071  0.0046  -0.0148 83  GLU A N   
662  C CA  . GLU A 87  ? 0.1903 0.2300 0.2085 0.0067  0.0063  -0.0159 83  GLU A CA  
663  C C   . GLU A 87  ? 0.2076 0.2348 0.2205 0.0007  0.0089  -0.0117 83  GLU A C   
664  O O   . GLU A 87  ? 0.2425 0.2721 0.2503 -0.0016 0.0082  -0.0058 83  GLU A O   
665  C CB  . GLU A 87  ? 0.2574 0.2897 0.2736 0.0121  0.0039  -0.0123 83  GLU A CB  
666  C CG  . GLU A 87  ? 0.3422 0.3717 0.3514 0.0123  0.0018  -0.0036 83  GLU A CG  
667  C CD  . GLU A 87  ? 0.4482 0.4708 0.4556 0.0181  -0.0009 -0.0006 83  GLU A CD  
668  O OE1 . GLU A 87  ? 0.4445 0.4741 0.4569 0.0231  -0.0026 -0.0044 83  GLU A OE1 
669  O OE2 . GLU A 87  ? 0.4944 0.5046 0.4952 0.0179  -0.0014 0.0054  83  GLU A OE2 
670  N N   . VAL A 88  ? 0.1984 0.2122 0.2129 -0.0016 0.0120  -0.0148 84  VAL A N   
671  C CA  . VAL A 88  ? 0.1906 0.1900 0.2001 -0.0068 0.0151  -0.0107 84  VAL A CA  
672  C C   . VAL A 88  ? 0.2038 0.1846 0.2126 -0.0054 0.0170  -0.0102 84  VAL A C   
673  O O   . VAL A 88  ? 0.2118 0.1908 0.2268 -0.0031 0.0176  -0.0164 84  VAL A O   
674  C CB  . VAL A 88  ? 0.1894 0.1929 0.2022 -0.0129 0.0181  -0.0150 84  VAL A CB  
675  C CG1 . VAL A 88  ? 0.1971 0.2004 0.2187 -0.0130 0.0200  -0.0244 84  VAL A CG1 
676  C CG2 . VAL A 88  ? 0.2064 0.1966 0.2135 -0.0183 0.0213  -0.0098 84  VAL A CG2 
677  N N   . ILE A 89  ? 0.2114 0.1782 0.2124 -0.0065 0.0181  -0.0029 85  ILE A N   
678  C CA  . ILE A 89  ? 0.2271 0.1748 0.2257 -0.0049 0.0202  -0.0011 85  ILE A CA  
679  C C   . ILE A 89  ? 0.2427 0.1774 0.2406 -0.0109 0.0256  -0.0008 85  ILE A C   
680  O O   . ILE A 89  ? 0.2411 0.1738 0.2332 -0.0146 0.0267  0.0043  85  ILE A O   
681  C CB  . ILE A 89  ? 0.2454 0.1857 0.2353 -0.0003 0.0174  0.0068  85  ILE A CB  
682  C CG1 . ILE A 89  ? 0.2769 0.2316 0.2688 0.0054  0.0122  0.0062  85  ILE A CG1 
683  C CG2 . ILE A 89  ? 0.2644 0.1846 0.2517 0.0018  0.0199  0.0083  85  ILE A CG2 
684  C CD1 . ILE A 89  ? 0.3084 0.2586 0.2923 0.0096  0.0087  0.0138  85  ILE A CD1 
685  N N   . VAL A 90  ? 0.2460 0.1721 0.2504 -0.0118 0.0289  -0.0064 86  VAL A N   
686  C CA  . VAL A 90  ? 0.2528 0.1674 0.2593 -0.0176 0.0345  -0.0078 86  VAL A CA  
687  C C   . VAL A 90  ? 0.3073 0.2016 0.3130 -0.0161 0.0379  -0.0065 86  VAL A C   
688  O O   . VAL A 90  ? 0.2815 0.1727 0.2876 -0.0106 0.0357  -0.0071 86  VAL A O   
689  C CB  . VAL A 90  ? 0.2842 0.2096 0.3018 -0.0211 0.0358  -0.0175 86  VAL A CB  
690  C CG1 . VAL A 90  ? 0.2861 0.2316 0.3040 -0.0219 0.0325  -0.0189 86  VAL A CG1 
691  C CG2 . VAL A 90  ? 0.3127 0.2388 0.3387 -0.0173 0.0349  -0.0252 86  VAL A CG2 
692  N N   . THR A 91  ? 0.2907 0.1709 0.2952 -0.0208 0.0433  -0.0043 87  THR A N   
693  C CA  . THR A 91  ? 0.3191 0.1800 0.3245 -0.0198 0.0474  -0.0040 87  THR A CA  
694  C C   . THR A 91  ? 0.2918 0.1543 0.3101 -0.0207 0.0490  -0.0141 87  THR A C   
695  O O   . THR A 91  ? 0.3381 0.2148 0.3648 -0.0233 0.0481  -0.0214 87  THR A O   
696  C CB  . THR A 91  ? 0.4117 0.2557 0.4121 -0.0244 0.0535  0.0015  87  THR A CB  
697  O OG1 . THR A 91  ? 0.4330 0.2819 0.4415 -0.0311 0.0570  -0.0037 87  THR A OG1 
698  C CG2 . THR A 91  ? 0.3896 0.2309 0.3767 -0.0234 0.0521  0.0114  87  THR A CG2 
699  N N   . ALA A 92  ? 0.3163 0.1635 0.3361 -0.0182 0.0514  -0.0144 88  ALA A N   
700  C CA  . ALA A 92  ? 0.3209 0.1680 0.3531 -0.0183 0.0526  -0.0239 88  ALA A CA  
701  C C   . ALA A 92  ? 0.3597 0.2049 0.4010 -0.0254 0.0577  -0.0293 88  ALA A C   
702  O O   . ALA A 92  ? 0.3873 0.2397 0.4403 -0.0264 0.0574  -0.0389 88  ALA A O   
703  C CB  . ALA A 92  ? 0.3982 0.2275 0.4293 -0.0142 0.0544  -0.0222 88  ALA A CB  
704  N N   . ASP A 93  ? 0.4017 0.2372 0.4381 -0.0301 0.0623  -0.0234 89  ASP A N   
705  C CA  . ASP A 93  ? 0.5407 0.3731 0.5855 -0.0372 0.0676  -0.0277 89  ASP A CA  
706  C C   . ASP A 93  ? 0.4768 0.3273 0.5239 -0.0411 0.0656  -0.0309 89  ASP A C   
707  O O   . ASP A 93  ? 0.5331 0.3841 0.5883 -0.0468 0.0693  -0.0358 89  ASP A O   
708  C CB  . ASP A 93  ? 0.6902 0.5024 0.7286 -0.0402 0.0743  -0.0197 89  ASP A CB  
709  C CG  . ASP A 93  ? 0.8132 0.6071 0.8460 -0.0354 0.0760  -0.0145 89  ASP A CG  
710  O OD1 . ASP A 93  ? 0.8451 0.6339 0.8862 -0.0335 0.0767  -0.0203 89  ASP A OD1 
711  O OD2 . ASP A 93  ? 0.8497 0.6340 0.8695 -0.0331 0.0765  -0.0048 89  ASP A OD2 
712  N N   . HIS A 94  ? 0.3873 0.2527 0.4280 -0.0381 0.0599  -0.0286 90  HIS A N   
713  C CA  . HIS A 94  ? 0.3762 0.2581 0.4174 -0.0414 0.0579  -0.0305 90  HIS A CA  
714  C C   . HIS A 94  ? 0.3726 0.2726 0.4231 -0.0397 0.0539  -0.0405 90  HIS A C   
715  O O   . HIS A 94  ? 0.4818 0.3860 0.5338 -0.0341 0.0503  -0.0431 90  HIS A O   
716  C CB  . HIS A 94  ? 0.4095 0.2971 0.4382 -0.0396 0.0545  -0.0217 90  HIS A CB  
717  C CG  . HIS A 94  ? 0.4590 0.3603 0.4874 -0.0439 0.0537  -0.0224 90  HIS A CG  
718  N ND1 . HIS A 94  ? 0.5409 0.4359 0.5679 -0.0499 0.0582  -0.0198 90  HIS A ND1 
719  C CD2 . HIS A 94  ? 0.4714 0.3922 0.5014 -0.0431 0.0493  -0.0259 90  HIS A CD2 
720  C CE1 . HIS A 94  ? 0.4799 0.3899 0.5069 -0.0525 0.0562  -0.0214 90  HIS A CE1 
721  N NE2 . HIS A 94  ? 0.4872 0.4130 0.5159 -0.0484 0.0508  -0.0250 90  HIS A NE2 
722  N N   . SER A 95  ? 0.3172 0.2276 0.3738 -0.0442 0.0545  -0.0460 91  SER A N   
723  C CA  . SER A 95  ? 0.3110 0.2380 0.3765 -0.0428 0.0512  -0.0562 91  SER A CA  
724  C C   . SER A 95  ? 0.2906 0.2362 0.3503 -0.0399 0.0459  -0.0545 91  SER A C   
725  O O   . SER A 95  ? 0.3058 0.2547 0.3577 -0.0421 0.0456  -0.0481 91  SER A O   
726  C CB  . SER A 95  ? 0.3813 0.3104 0.4565 -0.0488 0.0544  -0.0636 91  SER A CB  
727  O OG  . SER A 95  ? 0.4949 0.4105 0.5795 -0.0504 0.0584  -0.0685 91  SER A OG  
728  N N   . VAL A 96  ? 0.2967 0.2539 0.3605 -0.0348 0.0418  -0.0604 92  VAL A N   
729  C CA  . VAL A 96  ? 0.2563 0.2327 0.3174 -0.0318 0.0372  -0.0612 92  VAL A CA  
730  C C   . VAL A 96  ? 0.2462 0.2348 0.3165 -0.0333 0.0368  -0.0718 92  VAL A C   
731  O O   . VAL A 96  ? 0.2931 0.2771 0.3730 -0.0340 0.0384  -0.0798 92  VAL A O   
732  C CB  . VAL A 96  ? 0.3038 0.2842 0.3628 -0.0245 0.0332  -0.0603 92  VAL A CB  
733  C CG1 . VAL A 96  ? 0.2876 0.2883 0.3448 -0.0209 0.0289  -0.0615 92  VAL A CG1 
734  C CG2 . VAL A 96  ? 0.3327 0.3004 0.3826 -0.0229 0.0335  -0.0500 92  VAL A CG2 
735  N N   . MET A 97  ? 0.2127 0.2168 0.2804 -0.0336 0.0346  -0.0721 93  MET A N   
736  C CA  . MET A 97  ? 0.1888 0.2054 0.2644 -0.0341 0.0337  -0.0823 93  MET A CA  
737  C C   . MET A 97  ? 0.2000 0.2279 0.2790 -0.0271 0.0298  -0.0885 93  MET A C   
738  O O   . MET A 97  ? 0.2096 0.2430 0.2828 -0.0223 0.0270  -0.0837 93  MET A O   
739  C CB  . MET A 97  ? 0.1933 0.2214 0.2646 -0.0373 0.0333  -0.0805 93  MET A CB  
740  C CG  . MET A 97  ? 0.2175 0.2350 0.2841 -0.0439 0.0369  -0.0734 93  MET A CG  
741  S SD  . MET A 97  ? 0.2258 0.2272 0.3018 -0.0498 0.0424  -0.0785 93  MET A SD  
742  C CE  . MET A 97  ? 0.2210 0.2368 0.3077 -0.0510 0.0414  -0.0917 93  MET A CE  
743  N N   . VAL A 98  ? 0.1885 0.2197 0.2774 -0.0263 0.0296  -0.0994 94  VAL A N   
744  C CA  . VAL A 98  ? 0.1795 0.2226 0.2721 -0.0195 0.0259  -0.1065 94  VAL A CA  
745  C C   . VAL A 98  ? 0.1891 0.2441 0.2886 -0.0199 0.0250  -0.1171 94  VAL A C   
746  O O   . VAL A 98  ? 0.2187 0.2692 0.3239 -0.0253 0.0275  -0.1212 94  VAL A O   
747  C CB  . VAL A 98  ? 0.2291 0.2625 0.3272 -0.0157 0.0257  -0.1099 94  VAL A CB  
748  C CG1 . VAL A 98  ? 0.2695 0.2917 0.3602 -0.0144 0.0261  -0.0998 94  VAL A CG1 
749  C CG2 . VAL A 98  ? 0.2588 0.2808 0.3673 -0.0197 0.0287  -0.1172 94  VAL A CG2 
750  N N   . LYS A 99  ? 0.2172 0.2878 0.3163 -0.0138 0.0214  -0.1215 95  LYS A N   
751  C CA  . LYS A 99  ? 0.2281 0.3095 0.3346 -0.0120 0.0198  -0.1333 95  LYS A CA  
752  C C   . LYS A 99  ? 0.2245 0.3013 0.3397 -0.0079 0.0187  -0.1416 95  LYS A C   
753  O O   . LYS A 99  ? 0.2211 0.2998 0.3342 -0.0020 0.0166  -0.1404 95  LYS A O   
754  C CB  . LYS A 99  ? 0.2438 0.3440 0.3449 -0.0070 0.0167  -0.1341 95  LYS A CB  
755  C CG  . LYS A 99  ? 0.3213 0.4327 0.4288 -0.0054 0.0152  -0.1460 95  LYS A CG  
756  C CD  . LYS A 99  ? 0.3657 0.4938 0.4663 -0.0029 0.0134  -0.1449 95  LYS A CD  
757  C CE  . LYS A 99  ? 0.4215 0.5593 0.5280 -0.0016 0.0113  -0.1536 95  LYS A CE  
758  N NZ  . LYS A 99  ? 0.4915 0.6442 0.5911 0.0013  0.0085  -0.1485 95  LYS A NZ  
759  N N   . ARG A 100 ? 0.2210 0.2915 0.3463 -0.0113 0.0202  -0.1501 96  ARG A N   
760  C CA  . ARG A 100 ? 0.2313 0.2966 0.3665 -0.0082 0.0194  -0.1590 96  ARG A CA  
761  C C   . ARG A 100 ? 0.2703 0.3439 0.4150 -0.0082 0.0180  -0.1719 96  ARG A C   
762  O O   . ARG A 100 ? 0.2831 0.3540 0.4317 -0.0143 0.0203  -0.1724 96  ARG A O   
763  C CB  . ARG A 100 ? 0.2402 0.2852 0.3797 -0.0132 0.0233  -0.1558 96  ARG A CB  
764  C CG  . ARG A 100 ? 0.2620 0.2999 0.4135 -0.0114 0.0231  -0.1657 96  ARG A CG  
765  C CD  . ARG A 100 ? 0.2805 0.2974 0.4351 -0.0160 0.0276  -0.1611 96  ARG A CD  
766  N NE  . ARG A 100 ? 0.3044 0.3133 0.4491 -0.0141 0.0281  -0.1497 96  ARG A NE  
767  C CZ  . ARG A 100 ? 0.2598 0.2505 0.4040 -0.0172 0.0318  -0.1437 96  ARG A CZ  
768  N NH1 . ARG A 100 ? 0.3347 0.3132 0.4883 -0.0227 0.0359  -0.1474 96  ARG A NH1 
769  N NH2 . ARG A 100 ? 0.3184 0.3031 0.4532 -0.0147 0.0316  -0.1339 96  ARG A NH2 
770  N N   . ASP A 101 ? 0.3352 0.3549 0.3543 0.0171  -0.0607 -0.1847 97  ASP A N   
771  C CA  . ASP A 101 ? 0.4094 0.4410 0.4376 0.0122  -0.0657 -0.1949 97  ASP A CA  
772  C C   . ASP A 101 ? 0.4326 0.4896 0.4697 0.0148  -0.0727 -0.1924 97  ASP A C   
773  O O   . ASP A 101 ? 0.4086 0.4792 0.4618 0.0081  -0.0749 -0.2016 97  ASP A O   
774  C CB  . ASP A 101 ? 0.5012 0.5224 0.5427 -0.0003 -0.0597 -0.2081 97  ASP A CB  
775  C CG  . ASP A 101 ? 0.5113 0.5034 0.5436 -0.0015 -0.0508 -0.2116 97  ASP A CG  
776  O OD1 . ASP A 101 ? 0.5105 0.4953 0.5269 0.0054  -0.0517 -0.2094 97  ASP A OD1 
777  O OD2 . ASP A 101 ? 0.5339 0.5093 0.5755 -0.0089 -0.0415 -0.2159 97  ASP A OD2 
778  N N   . GLY A 102 ? 0.3731 0.4358 0.3997 0.0245  -0.0753 -0.1799 98  GLY A N   
779  C CA  . GLY A 102 ? 0.3707 0.4534 0.4034 0.0293  -0.0803 -0.1770 98  GLY A CA  
780  C C   . GLY A 102 ? 0.3780 0.4670 0.4218 0.0272  -0.0775 -0.1770 98  GLY A C   
781  O O   . GLY A 102 ? 0.3942 0.4991 0.4432 0.0324  -0.0809 -0.1759 98  GLY A O   
782  N N   . LYS A 103 ? 0.3014 0.3783 0.3491 0.0198  -0.0708 -0.1787 99  LYS A N   
783  C CA  . LYS A 103 ? 0.3036 0.3859 0.3628 0.0156  -0.0668 -0.1797 99  LYS A CA  
784  C C   . LYS A 103 ? 0.2948 0.3612 0.3394 0.0146  -0.0599 -0.1697 99  LYS A C   
785  O O   . LYS A 103 ? 0.3370 0.3873 0.3713 0.0133  -0.0566 -0.1667 99  LYS A O   
786  C CB  . LYS A 103 ? 0.3874 0.4718 0.4689 0.0037  -0.0633 -0.1920 99  LYS A CB  
787  C CG  . LYS A 103 ? 0.4977 0.5989 0.5933 0.0009  -0.0694 -0.2030 99  LYS A CG  
788  C CD  . LYS A 103 ? 0.5056 0.6330 0.6180 0.0029  -0.0735 -0.2072 99  LYS A CD  
789  C CE  . LYS A 103 ? 0.5713 0.7190 0.6941 0.0008  -0.0811 -0.2163 99  LYS A CE  
790  N NZ  . LYS A 103 ? 0.5797 0.7559 0.7159 0.0070  -0.0869 -0.2181 99  LYS A NZ  
791  N N   . ILE A 104 ? 0.2759 0.3471 0.3199 0.0145  -0.0569 -0.1658 100 ILE A N   
792  C CA  . ILE A 104 ? 0.2938 0.3521 0.3229 0.0106  -0.0493 -0.1570 100 ILE A CA  
793  C C   . ILE A 104 ? 0.3043 0.3587 0.3513 -0.0022 -0.0412 -0.1642 100 ILE A C   
794  O O   . ILE A 104 ? 0.3304 0.3959 0.3962 -0.0065 -0.0393 -0.1715 100 ILE A O   
795  C CB  . ILE A 104 ? 0.3196 0.3814 0.3341 0.0151  -0.0479 -0.1485 100 ILE A CB  
796  C CG1 . ILE A 104 ? 0.2981 0.3606 0.2955 0.0259  -0.0540 -0.1386 100 ILE A CG1 
797  C CG2 . ILE A 104 ? 0.3033 0.3532 0.3013 0.0073  -0.0387 -0.1406 100 ILE A CG2 
798  C CD1 . ILE A 104 ? 0.3813 0.4448 0.3653 0.0302  -0.0519 -0.1307 100 ILE A CD1 
799  N N   . ILE A 105 ? 0.3192 0.3586 0.3625 -0.0084 -0.0357 -0.1626 101 ILE A N   
800  C CA  . ILE A 105 ? 0.3067 0.3391 0.3682 -0.0215 -0.0260 -0.1644 101 ILE A CA  
801  C C   . ILE A 105 ? 0.3009 0.3214 0.3475 -0.0264 -0.0159 -0.1450 101 ILE A C   
802  O O   . ILE A 105 ? 0.2892 0.3067 0.3127 -0.0200 -0.0176 -0.1335 101 ILE A O   
803  C CB  . ILE A 105 ? 0.2844 0.3094 0.3618 -0.0249 -0.0269 -0.1761 101 ILE A CB  
804  C CG1 . ILE A 105 ? 0.3322 0.3429 0.3929 -0.0170 -0.0282 -0.1711 101 ILE A CG1 
805  C CG2 . ILE A 105 ? 0.3183 0.3597 0.4086 -0.0220 -0.0347 -0.1852 101 ILE A CG2 
806  C CD1 . ILE A 105 ? 0.3797 0.3745 0.4525 -0.0218 -0.0235 -0.1791 101 ILE A CD1 
807  N N   . ASP A 106 ? 0.2844 0.3002 0.3446 -0.0388 -0.0055 -0.1406 102 ASP A N   
808  C CA  . ASP A 106 ? 0.2949 0.3025 0.3438 -0.0458 0.0046  -0.1209 102 ASP A CA  
809  C C   . ASP A 106 ? 0.3358 0.3295 0.3936 -0.0474 0.0095  -0.1164 102 ASP A C   
810  O O   . ASP A 106 ? 0.3382 0.3264 0.4172 -0.0523 0.0115  -0.1283 102 ASP A O   
811  C CB  . ASP A 106 ? 0.3474 0.3591 0.4028 -0.0593 0.0141  -0.1170 102 ASP A CB  
812  C CG  . ASP A 106 ? 0.4914 0.5031 0.5758 -0.0682 0.0180  -0.1288 102 ASP A CG  
813  O OD1 . ASP A 106 ? 0.4361 0.4573 0.5354 -0.0649 0.0117  -0.1455 102 ASP A OD1 
814  O OD2 . ASP A 106 ? 0.4941 0.4984 0.5866 -0.0790 0.0273  -0.1207 102 ASP A OD2 
815  N N   . VAL A 107 ? 0.3159 0.3041 0.3572 -0.0432 0.0124  -0.0985 103 VAL A N   
816  C CA  . VAL A 107 ? 0.3346 0.3084 0.3827 -0.0417 0.0189  -0.0906 103 VAL A CA  
817  C C   . VAL A 107 ? 0.3239 0.2994 0.3600 -0.0457 0.0272  -0.0639 103 VAL A C   
818  O O   . VAL A 107 ? 0.3679 0.3551 0.3830 -0.0453 0.0247  -0.0520 103 VAL A O   
819  C CB  . VAL A 107 ? 0.3717 0.3376 0.4133 -0.0272 0.0127  -0.0973 103 VAL A CB  
820  C CG1 . VAL A 107 ? 0.3811 0.3479 0.4342 -0.0255 0.0043  -0.1232 103 VAL A CG1 
821  C CG2 . VAL A 107 ? 0.4440 0.4196 0.4601 -0.0174 0.0064  -0.0860 103 VAL A CG2 
822  N N   . LYS A 108 ? 0.3008 0.2655 0.3498 -0.0502 0.0373  -0.0537 104 LYS A N   
823  C CA  . LYS A 108 ? 0.2901 0.2591 0.3301 -0.0532 0.0451  -0.0259 104 LYS A CA  
824  C C   . LYS A 108 ? 0.2925 0.2622 0.3171 -0.0381 0.0428  -0.0122 104 LYS A C   
825  O O   . LYS A 108 ? 0.2999 0.2585 0.3266 -0.0255 0.0392  -0.0242 104 LYS A O   
826  C CB  . LYS A 108 ? 0.3605 0.3173 0.4204 -0.0608 0.0570  -0.0179 104 LYS A CB  
827  C CG  . LYS A 108 ? 0.4245 0.3789 0.5029 -0.0756 0.0601  -0.0327 104 LYS A CG  
828  C CD  . LYS A 108 ? 0.5175 0.4893 0.5867 -0.0882 0.0593  -0.0297 104 LYS A CD  
829  C CE  . LYS A 108 ? 0.5641 0.5353 0.6519 -0.0993 0.0605  -0.0492 104 LYS A CE  
830  N NZ  . LYS A 108 ? 0.5412 0.5271 0.6184 -0.1080 0.0597  -0.0508 104 LYS A NZ  
831  N N   . PRO A 109 ? 0.2870 0.2715 0.2954 -0.0402 0.0452  0.0131  105 PRO A N   
832  C CA  . PRO A 109 ? 0.2887 0.2780 0.2828 -0.0259 0.0433  0.0283  105 PRO A CA  
833  C C   . PRO A 109 ? 0.3070 0.2794 0.3156 -0.0139 0.0516  0.0351  105 PRO A C   
834  O O   . PRO A 109 ? 0.3378 0.3117 0.3371 0.0005  0.0507  0.0446  105 PRO A O   
835  C CB  . PRO A 109 ? 0.3166 0.3289 0.2922 -0.0353 0.0453  0.0554  105 PRO A CB  
836  C CG  . PRO A 109 ? 0.3034 0.3184 0.2873 -0.0541 0.0515  0.0573  105 PRO A CG  
837  C CD  . PRO A 109 ? 0.3285 0.3285 0.3286 -0.0570 0.0493  0.0281  105 PRO A CD  
838  N N   . THR A 110 ? 0.3202 0.2773 0.3500 -0.0197 0.0612  0.0339  106 THR A N   
839  C CA  . THR A 110 ? 0.3427 0.2779 0.3869 -0.0092 0.0720  0.0389  106 THR A CA  
840  C C   . THR A 110 ? 0.3583 0.2692 0.4118 -0.0036 0.0704  0.0088  106 THR A C   
841  O O   . THR A 110 ? 0.3936 0.2809 0.4575 0.0042  0.0807  0.0087  106 THR A O   
842  C CB  . THR A 110 ? 0.4641 0.3935 0.5255 -0.0201 0.0844  0.0534  106 THR A CB  
843  O OG1 . THR A 110 ? 0.4326 0.3595 0.5037 -0.0361 0.0820  0.0336  106 THR A OG1 
844  C CG2 . THR A 110 ? 0.5041 0.4592 0.5562 -0.0255 0.0872  0.0868  106 THR A CG2 
845  N N   . GLU A 111 ? 0.3438 0.2596 0.3944 -0.0089 0.0589  -0.0163 107 GLU A N   
846  C CA  . GLU A 111 ? 0.4046 0.3032 0.4636 -0.0073 0.0557  -0.0456 107 GLU A CA  
847  C C   . GLU A 111 ? 0.3742 0.2810 0.4181 0.0020  0.0423  -0.0611 107 GLU A C   
848  O O   . GLU A 111 ? 0.3908 0.2931 0.4399 -0.0005 0.0358  -0.0865 107 GLU A O   
849  C CB  . GLU A 111 ? 0.4666 0.3622 0.5429 -0.0234 0.0563  -0.0625 107 GLU A CB  
850  C CG  . GLU A 111 ? 0.6226 0.5005 0.7156 -0.0304 0.0716  -0.0516 107 GLU A CG  
851  C CD  . GLU A 111 ? 0.7465 0.6304 0.8536 -0.0484 0.0733  -0.0566 107 GLU A CD  
852  O OE1 . GLU A 111 ? 0.7770 0.6675 0.8897 -0.0556 0.0652  -0.0793 107 GLU A OE1 
853  O OE2 . GLU A 111 ? 0.7603 0.6440 0.8735 -0.0552 0.0829  -0.0368 107 GLU A OE2 
854  N N   . MET A 112 ? 0.3339 0.2554 0.3588 0.0112  0.0373  -0.0459 108 MET A N   
855  C CA  . MET A 112 ? 0.3298 0.2599 0.3389 0.0199  0.0245  -0.0588 108 MET A CA  
856  C C   . MET A 112 ? 0.3433 0.2559 0.3504 0.0331  0.0267  -0.0674 108 MET A C   
857  O O   . MET A 112 ? 0.3605 0.2583 0.3713 0.0406  0.0388  -0.0538 108 MET A O   
858  C CB  . MET A 112 ? 0.3093 0.2619 0.2970 0.0226  0.0185  -0.0401 108 MET A CB  
859  C CG  . MET A 112 ? 0.3292 0.2965 0.3158 0.0078  0.0178  -0.0338 108 MET A CG  
860  S SD  . MET A 112 ? 0.3584 0.3497 0.3177 0.0056  0.0144  -0.0098 108 MET A SD  
861  C CE  . MET A 112 ? 0.5039 0.5035 0.4491 0.0049  0.0008  -0.0310 108 MET A CE  
862  N N   . LYS A 113 ? 0.3440 0.2585 0.3452 0.0360  0.0156  -0.0899 109 LYS A N   
863  C CA  . LYS A 113 ? 0.3594 0.2583 0.3559 0.0463  0.0165  -0.1021 109 LYS A CA  
864  C C   . LYS A 113 ? 0.3482 0.2613 0.3228 0.0588  0.0073  -0.0958 109 LYS A C   
865  O O   . LYS A 113 ? 0.3299 0.2648 0.2927 0.0574  -0.0031 -0.0904 109 LYS A O   
866  C CB  . LYS A 113 ? 0.3685 0.2622 0.3725 0.0389  0.0096  -0.1328 109 LYS A CB  
867  C CG  . LYS A 113 ? 0.4588 0.3395 0.4837 0.0247  0.0171  -0.1439 109 LYS A CG  
868  C CD  . LYS A 113 ? 0.5216 0.4074 0.5513 0.0165  0.0068  -0.1727 109 LYS A CD  
869  C CE  . LYS A 113 ? 0.6349 0.5031 0.6827 0.0027  0.0157  -0.1874 109 LYS A CE  
870  N NZ  . LYS A 113 ? 0.6853 0.5449 0.7454 -0.0027 0.0281  -0.1701 109 LYS A NZ  
871  N N   . GLN A 114 ? 0.4241 0.3229 0.3926 0.0707  0.0125  -0.0972 110 GLN A N   
872  C CA  . GLN A 114 ? 0.4697 0.3814 0.4176 0.0829  0.0045  -0.0918 110 GLN A CA  
873  C C   . GLN A 114 ? 0.4260 0.3517 0.3639 0.0803  -0.0128 -0.1127 110 GLN A C   
874  O O   . GLN A 114 ? 0.4264 0.3698 0.3462 0.0863  -0.0225 -0.1058 110 GLN A O   
875  C CB  . GLN A 114 ? 0.5773 0.4688 0.5222 0.0962  0.0153  -0.0908 110 GLN A CB  
876  C CG  . GLN A 114 ? 0.6682 0.5739 0.5940 0.1104  0.0120  -0.0746 110 GLN A CG  
877  C CD  . GLN A 114 ? 0.7585 0.6804 0.6827 0.1134  0.0175  -0.0412 110 GLN A CD  
878  O OE1 . GLN A 114 ? 0.7306 0.6774 0.6425 0.1092  0.0072  -0.0308 110 GLN A OE1 
879  N NE2 . GLN A 114 ? 0.8151 0.7230 0.7509 0.1203  0.0345  -0.0237 110 GLN A NE2 
880  N N   . THR A 115 ? 0.3656 0.2857 0.3148 0.0710  -0.0167 -0.1366 111 THR A N   
881  C CA  . THR A 115 ? 0.3391 0.2757 0.2822 0.0684  -0.0330 -0.1549 111 THR A CA  
882  C C   . THR A 115 ? 0.3163 0.2727 0.2626 0.0606  -0.0409 -0.1514 111 THR A C   
883  O O   . THR A 115 ? 0.3988 0.3741 0.3457 0.0559  -0.0501 -0.1500 111 THR A O   
884  C CB  . THR A 115 ? 0.3569 0.2853 0.3120 0.0577  -0.0315 -0.1716 111 THR A CB  
885  O OG1 . THR A 115 ? 0.4463 0.3594 0.4197 0.0487  -0.0223 -0.1798 111 THR A OG1 
886  C CG2 . THR A 115 ? 0.3955 0.3065 0.3411 0.0644  -0.0247 -0.1751 111 THR A CG2 
887  N N   . ASP A 116 ? 0.3104 0.2663 0.2649 0.0544  -0.0326 -0.1359 112 ASP A N   
888  C CA  . ASP A 116 ? 0.2971 0.2696 0.2517 0.0472  -0.0376 -0.1313 112 ASP A CA  
889  C C   . ASP A 116 ? 0.3198 0.3075 0.2504 0.0539  -0.0451 -0.1188 112 ASP A C   
890  O O   . ASP A 116 ? 0.3624 0.3493 0.2780 0.0627  -0.0437 -0.1062 112 ASP A O   
891  C CB  . ASP A 116 ? 0.3048 0.2727 0.2705 0.0383  -0.0257 -0.1156 112 ASP A CB  
892  C CG  . ASP A 116 ? 0.3165 0.2723 0.3066 0.0282  -0.0190 -0.1285 112 ASP A CG  
893  O OD1 . ASP A 116 ? 0.3250 0.2802 0.3240 0.0255  -0.0249 -0.1503 112 ASP A OD1 
894  O OD2 . ASP A 116 ? 0.3128 0.2608 0.3128 0.0219  -0.0078 -0.1160 112 ASP A OD2 
895  N N   . ARG A 117 ? 0.2841 0.2853 0.2111 0.0494  -0.0520 -0.1213 113 ARG A N   
896  C CA  . ARG A 117 ? 0.2832 0.2959 0.1930 0.0498  -0.0534 -0.1019 113 ARG A CA  
897  C C   . ARG A 117 ? 0.3135 0.3312 0.2210 0.0400  -0.0499 -0.0963 113 ARG A C   
898  O O   . ARG A 117 ? 0.3074 0.3254 0.2312 0.0336  -0.0492 -0.1075 113 ARG A O   
899  C CB  . ARG A 117 ? 0.2792 0.2992 0.1949 0.0512  -0.0572 -0.0978 113 ARG A CB  
900  C CG  . ARG A 117 ? 0.3265 0.3439 0.2400 0.0598  -0.0599 -0.0997 113 ARG A CG  
901  C CD  . ARG A 117 ? 0.4214 0.4462 0.3413 0.0604  -0.0629 -0.0971 113 ARG A CD  
902  N NE  . ARG A 117 ? 0.4360 0.4657 0.3710 0.0571  -0.0662 -0.1087 113 ARG A NE  
903  C CZ  . ARG A 117 ? 0.4095 0.4473 0.3501 0.0582  -0.0690 -0.1078 113 ARG A CZ  
904  N NH1 . ARG A 117 ? 0.3823 0.4220 0.3166 0.0624  -0.0684 -0.0977 113 ARG A NH1 
905  N NH2 . ARG A 117 ? 0.5164 0.5615 0.4701 0.0561  -0.0725 -0.1183 113 ARG A NH2 
906  N N   . VAL A 118 ? 0.1667 0.2839 0.1973 0.0398  0.0018  -0.0661 114 VAL A N   
907  C CA  . VAL A 118 ? 0.1594 0.2862 0.2124 0.0316  -0.0006 -0.0729 114 VAL A CA  
908  C C   . VAL A 118 ? 0.1659 0.2557 0.1927 0.0419  -0.0037 -0.0710 114 VAL A C   
909  O O   . VAL A 118 ? 0.2026 0.2595 0.1947 0.0518  -0.0005 -0.0619 114 VAL A O   
910  C CB  . VAL A 118 ? 0.2910 0.4402 0.3708 0.0087  0.0145  -0.0678 114 VAL A CB  
911  C CG1 . VAL A 118 ? 0.2575 0.4110 0.3420 -0.0015 0.0119  -0.0619 114 VAL A CG1 
912  C CG2 . VAL A 118 ? 0.2586 0.3847 0.3171 0.0024  0.0312  -0.0519 114 VAL A CG2 
913  N N   . VAL A 119 ? 0.1739 0.2689 0.2169 0.0404  -0.0107 -0.0800 115 VAL A N   
914  C CA  . VAL A 119 ? 0.1843 0.2471 0.2068 0.0501  -0.0147 -0.0800 115 VAL A CA  
915  C C   . VAL A 119 ? 0.1846 0.2419 0.2131 0.0335  -0.0003 -0.0731 115 VAL A C   
916  O O   . VAL A 119 ? 0.1746 0.2576 0.2342 0.0193  0.0018  -0.0788 115 VAL A O   
917  C CB  . VAL A 119 ? 0.1768 0.2487 0.2133 0.0603  -0.0324 -0.0949 115 VAL A CB  
918  C CG1 . VAL A 119 ? 0.2375 0.2744 0.2508 0.0721  -0.0370 -0.0944 115 VAL A CG1 
919  C CG2 . VAL A 119 ? 0.2009 0.2867 0.2385 0.0732  -0.0466 -0.1024 115 VAL A CG2 
920  N N   . LYS A 120 ? 0.2197 0.2436 0.2187 0.0346  0.0096  -0.0608 116 LYS A N   
921  C CA  . LYS A 120 ? 0.2285 0.2446 0.2295 0.0185  0.0243  -0.0523 116 LYS A CA  
922  C C   . LYS A 120 ? 0.2617 0.2413 0.2392 0.0270  0.0221  -0.0511 116 LYS A C   
923  O O   . LYS A 120 ? 0.2971 0.2470 0.2434 0.0439  0.0169  -0.0479 116 LYS A O   
924  C CB  . LYS A 120 ? 0.2411 0.2517 0.2294 0.0093  0.0408  -0.0368 116 LYS A CB  
925  C CG  . LYS A 120 ? 0.2835 0.2887 0.2756 -0.0093 0.0566  -0.0271 116 LYS A CG  
926  C CD  . LYS A 120 ? 0.3467 0.3433 0.3232 -0.0163 0.0724  -0.0107 116 LYS A CD  
927  C CE  . LYS A 120 ? 0.5208 0.4869 0.4770 -0.0228 0.0838  0.0008  116 LYS A CE  
928  N NZ  . LYS A 120 ? 0.5886 0.5137 0.5075 -0.0040 0.0778  0.0028  116 LYS A NZ  
929  N N   . TRP A 121 ? 0.2552 0.2368 0.2471 0.0152  0.0264  -0.0533 117 TRP A N   
930  C CA  . TRP A 121 ? 0.2904 0.2378 0.2617 0.0201  0.0270  -0.0510 117 TRP A CA  
931  C C   . TRP A 121 ? 0.3846 0.2997 0.3228 0.0199  0.0393  -0.0349 117 TRP A C   
932  O O   . TRP A 121 ? 0.4225 0.3457 0.3622 0.0075  0.0522  -0.0246 117 TRP A O   
933  C CB  . TRP A 121 ? 0.2731 0.2318 0.2678 0.0032  0.0325  -0.0548 117 TRP A CB  
934  C CG  . TRP A 121 ? 0.3064 0.2328 0.2834 0.0085  0.0316  -0.0547 117 TRP A CG  
935  C CD1 . TRP A 121 ? 0.4292 0.3308 0.3902 -0.0010 0.0441  -0.0443 117 TRP A CD1 
936  C CD2 . TRP A 121 ? 0.3516 0.2658 0.3243 0.0249  0.0175  -0.0653 117 TRP A CD2 
937  N NE1 . TRP A 121 ? 0.5771 0.4514 0.5241 0.0084  0.0387  -0.0481 117 TRP A NE1 
938  C CE2 . TRP A 121 ? 0.4730 0.3546 0.4271 0.0246  0.0225  -0.0609 117 TRP A CE2 
939  C CE3 . TRP A 121 ? 0.4165 0.3447 0.3999 0.0396  0.0010  -0.0779 117 TRP A CE3 
940  C CZ2 . TRP A 121 ? 0.5726 0.4350 0.5185 0.0390  0.0120  -0.0686 117 TRP A CZ2 
941  C CZ3 . TRP A 121 ? 0.4882 0.3981 0.4639 0.0537  -0.0095 -0.0853 117 TRP A CZ3 
942  C CH2 . TRP A 121 ? 0.5557 0.4330 0.5129 0.0535  -0.0038 -0.0806 117 TRP A CH2 
943  N N   . MET A 122 ? 0.4509 0.3291 0.3591 0.0342  0.0351  -0.0326 118 MET A N   
944  C CA  . MET A 122 ? 0.6454 0.4895 0.5194 0.0365  0.0452  -0.0179 118 MET A CA  
945  C C   . MET A 122 ? 0.7683 0.5860 0.6314 0.0316  0.0509  -0.0143 118 MET A C   
946  O O   . MET A 122 ? 0.7910 0.6035 0.6597 0.0371  0.0421  -0.0240 118 MET A O   
947  C CB  . MET A 122 ? 0.7337 0.5532 0.5770 0.0591  0.0352  -0.0172 118 MET A CB  
948  C CG  . MET A 122 ? 0.7783 0.6139 0.6211 0.0648  0.0323  -0.0167 118 MET A CG  
949  S SD  . MET A 122 ? 0.8389 0.6707 0.6679 0.0536  0.0513  0.0008  118 MET A SD  
950  C CE  . MET A 122 ? 0.6865 0.4690 0.4754 0.0591  0.0585  0.0134  118 MET A CE  
951  N N   . LEU A 123 ? 0.8433 0.6444 0.6911 0.0209  0.0659  -0.0002 119 LEU A N   
952  C CA  . LEU A 123 ? 0.9598 0.7320 0.7926 0.0161  0.0725  0.0053  119 LEU A CA  
953  C C   . LEU A 123 ? 0.9544 0.6838 0.7464 0.0322  0.0714  0.0133  119 LEU A C   
954  O O   . LEU A 123 ? 1.0222 0.7238 0.7987 0.0316  0.0747  0.0168  119 LEU A O   
955  C CB  . LEU A 123 ? 1.0183 0.7986 0.8604 -0.0075 0.0899  0.0163  119 LEU A CB  
956  C CG  . LEU A 123 ? 1.0136 0.8377 0.8947 -0.0254 0.0934  0.0115  119 LEU A CG  
957  C CD1 . LEU A 123 ? 1.0064 0.8384 0.8905 -0.0449 0.1108  0.0261  119 LEU A CD1 
958  C CD2 . LEU A 123 ? 1.0169 0.8535 0.9225 -0.0337 0.0890  -0.0002 119 LEU A CD2 
959  N N   . THR A 124 ? 0.8507 0.5738 0.6246 0.0467  0.0666  0.0161  120 THR A N   
960  C CA  . THR A 124 ? 0.8334 0.5171 0.5677 0.0604  0.0674  0.0256  120 THR A CA  
961  C C   . THR A 124 ? 0.8347 0.5128 0.5552 0.0825  0.0524  0.0194  120 THR A C   
962  O O   . THR A 124 ? 0.6973 0.4033 0.4357 0.0852  0.0451  0.0117  120 THR A O   
963  C CB  . THR A 124 ? 0.8177 0.4939 0.5365 0.0512  0.0832  0.0419  120 THR A CB  
964  O OG1 . THR A 124 ? 0.8024 0.5069 0.5345 0.0494  0.0840  0.0417  120 THR A OG1 
965  C CG2 . THR A 124 ? 0.7650 0.4441 0.4945 0.0292  0.0983  0.0497  120 THR A CG2 
966  N N   . GLY A 125 A 0.8827 0.5239 0.5704 0.0980  0.0479  0.0232  120 GLY A N   
967  C CA  . GLY A 125 A 0.8982 0.5291 0.5678 0.1191  0.0342  0.0193  120 GLY A CA  
968  C C   . GLY A 125 A 0.9340 0.5699 0.6154 0.1314  0.0171  0.0048  120 GLY A C   
969  O O   . GLY A 125 A 0.9659 0.6168 0.6723 0.1236  0.0156  -0.0034 120 GLY A O   
970  N N   . SER A 126 B 0.9579 0.5809 0.6204 0.1511  0.0041  0.0020  120 SER A N   
971  C CA  . SER A 126 B 1.0157 0.6383 0.6842 0.1655  -0.0128 -0.0100 120 SER A CA  
972  C C   . SER A 126 B 1.0162 0.6797 0.7221 0.1616  -0.0213 -0.0235 120 SER A C   
973  O O   . SER A 126 B 1.0393 0.7093 0.7602 0.1673  -0.0320 -0.0341 120 SER A O   
974  C CB  . SER A 126 B 1.0787 0.6786 0.7171 0.1867  -0.0244 -0.0085 120 SER A CB  
975  O OG  . SER A 126 B 1.1491 0.7095 0.7579 0.1955  -0.0235 -0.0017 120 SER A OG  
976  N N   . HIS A 127 C 0.9674 0.6584 0.6885 0.1519  -0.0165 -0.0229 120 HIS A N   
977  C CA  . HIS A 127 C 0.8964 0.6285 0.6536 0.1456  -0.0224 -0.0343 120 HIS A CA  
978  C C   . HIS A 127 C 0.7572 0.5114 0.5443 0.1247  -0.0116 -0.0359 120 HIS A C   
979  O O   . HIS A 127 C 0.7391 0.4863 0.5215 0.1107  0.0040  -0.0256 120 HIS A O   
980  C CB  . HIS A 127 C 0.9572 0.7028 0.7103 0.1466  -0.0217 -0.0310 120 HIS A CB  
981  C CG  . HIS A 127 C 1.0214 0.7556 0.7547 0.1671  -0.0369 -0.0344 120 HIS A CG  
982  N ND1 . HIS A 127 C 1.0743 0.7808 0.7874 0.1834  -0.0474 -0.0360 120 HIS A ND1 
983  C CD2 . HIS A 127 C 1.0414 0.7825 0.7660 0.1739  -0.0414 -0.0339 120 HIS A CD2 
984  C CE1 . HIS A 127 C 1.0876 0.7889 0.7848 0.1990  -0.0596 -0.0380 120 HIS A CE1 
985  N NE2 . HIS A 127 C 1.0665 0.7874 0.7692 0.1935  -0.0561 -0.0366 120 HIS A NE2 
986  N N   . MET A 128 ? 0.6242 0.4054 0.4421 0.1225  -0.0202 -0.0487 121 MET A N   
987  C CA  . MET A 128 ? 0.5495 0.3540 0.3978 0.1031  -0.0117 -0.0520 121 MET A CA  
988  C C   . MET A 128 ? 0.4828 0.3255 0.3576 0.0901  -0.0076 -0.0537 121 MET A C   
989  O O   . MET A 128 ? 0.4495 0.3118 0.3475 0.0715  0.0022  -0.0535 121 MET A O   
990  C CB  . MET A 128 ? 0.6320 0.4429 0.4990 0.1069  -0.0219 -0.0646 121 MET A CB  
991  C CG  . MET A 128 ? 0.7908 0.5637 0.6338 0.1171  -0.0234 -0.0622 121 MET A CG  
992  S SD  . MET A 128 ? 0.8963 0.6753 0.7587 0.1260  -0.0373 -0.0773 121 MET A SD  
993  C CE  . MET A 128 ? 0.8650 0.6733 0.7642 0.1015  -0.0269 -0.0824 121 MET A CE  
994  N N   . ILE A 129 ? 0.2882 0.4060 0.2658 0.0106  -0.0173 -0.0326 122 ILE A N   
995  C CA  . ILE A 129 ? 0.2612 0.3715 0.2418 0.0134  -0.0141 -0.0330 122 ILE A CA  
996  C C   . ILE A 129 ? 0.2326 0.3485 0.2201 0.0134  -0.0091 -0.0365 122 ILE A C   
997  O O   . ILE A 129 ? 0.2833 0.4075 0.2718 0.0108  -0.0072 -0.0397 122 ILE A O   
998  C CB  . ILE A 129 ? 0.2566 0.3571 0.2309 0.0125  -0.0109 -0.0353 122 ILE A CB  
999  C CG1 . ILE A 129 ? 0.2764 0.3810 0.2473 0.0083  -0.0068 -0.0409 122 ILE A CG1 
1000 C CG2 . ILE A 129 ? 0.2978 0.3913 0.2657 0.0133  -0.0158 -0.0312 122 ILE A CG2 
1001 C CD1 . ILE A 129 ? 0.2968 0.3922 0.2619 0.0070  -0.0032 -0.0437 122 ILE A CD1 
1002 N N   . GLU A 130 ? 0.2057 0.3169 0.1977 0.0167  -0.0070 -0.0357 123 GLU A N   
1003 C CA  . GLU A 130 ? 0.1997 0.3137 0.1977 0.0171  -0.0016 -0.0392 123 GLU A CA  
1004 C C   . GLU A 130 ? 0.1827 0.2861 0.1793 0.0188  0.0032  -0.0409 123 GLU A C   
1005 O O   . GLU A 130 ? 0.2091 0.3034 0.2021 0.0209  0.0013  -0.0380 123 GLU A O   
1006 C CB  . GLU A 130 ? 0.2264 0.3465 0.2325 0.0200  -0.0035 -0.0364 123 GLU A CB  
1007 C CG  . GLU A 130 ? 0.2100 0.3237 0.2181 0.0246  -0.0064 -0.0317 123 GLU A CG  
1008 C CD  . GLU A 130 ? 0.2624 0.3826 0.2789 0.0274  -0.0080 -0.0292 123 GLU A CD  
1009 O OE1 . GLU A 130 ? 0.2963 0.4227 0.3182 0.0269  -0.0044 -0.0320 123 GLU A OE1 
1010 O OE2 . GLU A 130 ? 0.2810 0.4004 0.2989 0.0302  -0.0130 -0.0245 123 GLU A OE2 
1011 N N   . PHE A 131 ? 0.1930 0.2974 0.1926 0.0179  0.0094  -0.0456 124 PHE A N   
1012 C CA  . PHE A 131 ? 0.1930 0.2876 0.1923 0.0196  0.0148  -0.0475 124 PHE A CA  
1013 C C   . PHE A 131 ? 0.1821 0.2786 0.1892 0.0232  0.0164  -0.0464 124 PHE A C   
1014 O O   . PHE A 131 ? 0.2061 0.3110 0.2183 0.0221  0.0185  -0.0489 124 PHE A O   
1015 C CB  . PHE A 131 ? 0.2150 0.3095 0.2115 0.0155  0.0209  -0.0541 124 PHE A CB  
1016 C CG  . PHE A 131 ? 0.2232 0.3183 0.2126 0.0118  0.0191  -0.0554 124 PHE A CG  
1017 C CD1 . PHE A 131 ? 0.2525 0.3384 0.2357 0.0122  0.0171  -0.0532 124 PHE A CD1 
1018 C CD2 . PHE A 131 ? 0.2745 0.3796 0.2633 0.0080  0.0193  -0.0587 124 PHE A CD2 
1019 C CE1 . PHE A 131 ? 0.2819 0.3684 0.2584 0.0089  0.0153  -0.0543 124 PHE A CE1 
1020 C CE2 . PHE A 131 ? 0.3145 0.4203 0.2964 0.0048  0.0175  -0.0598 124 PHE A CE2 
1021 C CZ  . PHE A 131 ? 0.3150 0.4115 0.2910 0.0052  0.0155  -0.0576 124 PHE A CZ  
1022 N N   . ILE A 132 ? 0.1847 0.2734 0.1927 0.0277  0.0154  -0.0426 125 ILE A N   
1023 C CA  . ILE A 132 ? 0.1791 0.2706 0.1944 0.0318  0.0148  -0.0399 125 ILE A CA  
1024 C C   . ILE A 132 ? 0.1887 0.2700 0.2045 0.0356  0.0195  -0.0400 125 ILE A C   
1025 O O   . ILE A 132 ? 0.1955 0.2661 0.2056 0.0363  0.0209  -0.0398 125 ILE A O   
1026 C CB  . ILE A 132 ? 0.1924 0.2875 0.2093 0.0343  0.0071  -0.0340 125 ILE A CB  
1027 C CG1 . ILE A 132 ? 0.1775 0.2788 0.2029 0.0377  0.0062  -0.0317 125 ILE A CG1 
1028 C CG2 . ILE A 132 ? 0.1879 0.2728 0.1993 0.0367  0.0041  -0.0303 125 ILE A CG2 
1029 C CD1 . ILE A 132 ? 0.2107 0.3177 0.2383 0.0392  -0.0013 -0.0266 125 ILE A CD1 
1030 N N   . GLU A 133 ? 0.1905 0.2748 0.2129 0.0380  0.0225  -0.0406 126 GLU A N   
1031 C CA  . GLU A 133 ? 0.2043 0.2797 0.2280 0.0424  0.0265  -0.0398 126 GLU A CA  
1032 C C   . GLU A 133 ? 0.2262 0.2962 0.2487 0.0472  0.0215  -0.0338 126 GLU A C   
1033 O O   . GLU A 133 ? 0.2265 0.3018 0.2495 0.0474  0.0147  -0.0301 126 GLU A O   
1034 C CB  . GLU A 133 ? 0.2374 0.3189 0.2690 0.0442  0.0297  -0.0410 126 GLU A CB  
1035 C CG  . GLU A 133 ? 0.2768 0.3676 0.3151 0.0470  0.0241  -0.0367 126 GLU A CG  
1036 C CD  . GLU A 133 ? 0.2944 0.3973 0.3344 0.0431  0.0197  -0.0369 126 GLU A CD  
1037 O OE1 . GLU A 133 ? 0.2599 0.3657 0.2969 0.0383  0.0216  -0.0410 126 GLU A OE1 
1038 O OE2 . GLU A 133 ? 0.3543 0.4637 0.3985 0.0451  0.0144  -0.0329 126 GLU A OE2 
1039 N N   . PHE A 134 ? 0.2120 0.2713 0.2330 0.0512  0.0249  -0.0328 127 PHE A N   
1040 C CA  . PHE A 134 ? 0.2159 0.2689 0.2346 0.0559  0.0205  -0.0274 127 PHE A CA  
1041 C C   . PHE A 134 ? 0.2258 0.2704 0.2459 0.0615  0.0248  -0.0261 127 PHE A C   
1042 O O   . PHE A 134 ? 0.2466 0.2881 0.2680 0.0613  0.0317  -0.0298 127 PHE A O   
1043 C CB  . PHE A 134 ? 0.2241 0.2695 0.2344 0.0538  0.0188  -0.0270 127 PHE A CB  
1044 C CG  . PHE A 134 ? 0.2501 0.2845 0.2550 0.0524  0.0258  -0.0308 127 PHE A CG  
1045 C CD1 . PHE A 134 ? 0.3000 0.3367 0.3037 0.0469  0.0302  -0.0366 127 PHE A CD1 
1046 C CD2 . PHE A 134 ? 0.3298 0.3517 0.3310 0.0567  0.0281  -0.0288 127 PHE A CD2 
1047 C CE1 . PHE A 134 ? 0.3741 0.4009 0.3731 0.0453  0.0368  -0.0405 127 PHE A CE1 
1048 C CE2 . PHE A 134 ? 0.4884 0.4998 0.4848 0.0552  0.0349  -0.0325 127 PHE A CE2 
1049 C CZ  . PHE A 134 ? 0.4968 0.5108 0.4922 0.0494  0.0393  -0.0384 127 PHE A CZ  
1050 N N   . GLU A 135 ? 0.2290 0.2702 0.2488 0.0667  0.0206  -0.0209 128 GLU A N   
1051 C CA  . GLU A 135 ? 0.2390 0.2713 0.2590 0.0729  0.0238  -0.0187 128 GLU A CA  
1052 C C   . GLU A 135 ? 0.2448 0.2660 0.2573 0.0754  0.0218  -0.0155 128 GLU A C   
1053 O O   . GLU A 135 ? 0.2398 0.2627 0.2489 0.0733  0.0162  -0.0138 128 GLU A O   
1054 C CB  . GLU A 135 ? 0.3330 0.3731 0.3603 0.0779  0.0198  -0.0147 128 GLU A CB  
1055 C CG  . GLU A 135 ? 0.4957 0.5473 0.5309 0.0760  0.0213  -0.0172 128 GLU A CG  
1056 C CD  . GLU A 135 ? 0.6803 0.7414 0.7227 0.0800  0.0160  -0.0131 128 GLU A CD  
1057 O OE1 . GLU A 135 ? 0.7298 0.7933 0.7779 0.0834  0.0190  -0.0131 128 GLU A OE1 
1058 O OE2 . GLU A 135 ? 0.7153 0.7817 0.7577 0.0796  0.0089  -0.0099 128 GLU A OE2 
1059 N N   . ILE A 136 ? 0.2888 0.2984 0.2987 0.0799  0.0267  -0.0149 129 ILE A N   
1060 C CA  . ILE A 136 ? 0.2873 0.2850 0.2900 0.0831  0.0260  -0.0119 129 ILE A CA  
1061 C C   . ILE A 136 ? 0.2697 0.2643 0.2747 0.0911  0.0252  -0.0072 129 ILE A C   
1062 O O   . ILE A 136 ? 0.3067 0.3016 0.3162 0.0942  0.0296  -0.0080 129 ILE A O   
1063 C CB  . ILE A 136 ? 0.3277 0.3128 0.3240 0.0810  0.0337  -0.0158 129 ILE A CB  
1064 C CG1 . ILE A 136 ? 0.3358 0.3250 0.3307 0.0731  0.0354  -0.0211 129 ILE A CG1 
1065 C CG2 . ILE A 136 ? 0.3275 0.3002 0.3159 0.0839  0.0326  -0.0127 129 ILE A CG2 
1066 C CD1 . ILE A 136 ? 0.3884 0.3671 0.3788 0.0706  0.0441  -0.0261 129 ILE A CD1 
1067 N N   . GLU A 137 ? 0.2746 0.2663 0.2764 0.0948  0.0196  -0.0024 130 GLU A N   
1068 C CA  . GLU A 137 ? 0.2844 0.2722 0.2871 0.1028  0.0186  0.0022  130 GLU A CA  
1069 C C   . GLU A 137 ? 0.2870 0.2609 0.2810 0.1057  0.0193  0.0044  130 GLU A C   
1070 O O   . GLU A 137 ? 0.3129 0.2857 0.3021 0.1029  0.0149  0.0053  130 GLU A O   
1071 C CB  . GLU A 137 ? 0.3190 0.3187 0.3273 0.1053  0.0102  0.0064  130 GLU A CB  
1072 C CG  . GLU A 137 ? 0.4737 0.4712 0.4838 0.1140  0.0090  0.0110  130 GLU A CG  
1073 C CD  . GLU A 137 ? 0.6214 0.6317 0.6375 0.1159  0.0007  0.0147  130 GLU A CD  
1074 O OE1 . GLU A 137 ? 0.6291 0.6501 0.6488 0.1105  -0.0033 0.0133  130 GLU A OE1 
1075 O OE2 . GLU A 137 ? 0.6259 0.6355 0.6430 0.1228  -0.0018 0.0188  130 GLU A OE2 
1076 N N   . ASP A 138 ? 0.3430 0.3063 0.3348 0.1113  0.0247  0.0054  131 ASP A N   
1077 C CA  . ASP A 138 ? 0.3506 0.2998 0.3342 0.1151  0.0263  0.0078  131 ASP A CA  
1078 C C   . ASP A 138 ? 0.3319 0.2833 0.3161 0.1219  0.0194  0.0139  131 ASP A C   
1079 O O   . ASP A 138 ? 0.3508 0.3059 0.3398 0.1276  0.0191  0.0163  131 ASP A O   
1080 C CB  . ASP A 138 ? 0.4053 0.3427 0.3869 0.1183  0.0358  0.0060  131 ASP A CB  
1081 C CG  . ASP A 138 ? 0.5560 0.4771 0.5283 0.1211  0.0392  0.0074  131 ASP A CG  
1082 O OD1 . ASP A 138 ? 0.4931 0.4119 0.4612 0.1231  0.0337  0.0112  131 ASP A OD1 
1083 O OD2 . ASP A 138 ? 0.5857 0.4959 0.5549 0.1213  0.0478  0.0046  131 ASP A OD2 
1084 N N   . LEU A 139 ? 0.3751 0.3245 0.3542 0.1212  0.0139  0.0164  132 LEU A N   
1085 C CA  . LEU A 139 ? 0.3856 0.3374 0.3647 0.1272  0.0069  0.0220  132 LEU A CA  
1086 C C   . LEU A 139 ? 0.4256 0.3632 0.3977 0.1341  0.0094  0.0252  132 LEU A C   
1087 O O   . LEU A 139 ? 0.4326 0.3713 0.4040 0.1396  0.0039  0.0299  132 LEU A O   
1088 C CB  . LEU A 139 ? 0.3673 0.3260 0.3453 0.1230  -0.0013 0.0232  132 LEU A CB  
1089 C CG  . LEU A 139 ? 0.3580 0.3318 0.3431 0.1171  -0.0050 0.0209  132 LEU A CG  
1090 C CD1 . LEU A 139 ? 0.3587 0.3383 0.3420 0.1132  -0.0128 0.0223  132 LEU A CD1 
1091 C CD2 . LEU A 139 ? 0.4133 0.3970 0.4070 0.1216  -0.0068 0.0228  132 LEU A CD2 
1092 N N   . GLY A 140 ? 0.3898 0.3320 0.4076 0.0158  0.0692  0.0674  133 GLY A N   
1093 C CA  . GLY A 140 ? 0.4243 0.3578 0.4336 0.0164  0.0746  0.0736  133 GLY A CA  
1094 C C   . GLY A 140 ? 0.4733 0.4075 0.4711 0.0153  0.0750  0.0714  133 GLY A C   
1095 O O   . GLY A 140 ? 0.4816 0.4231 0.4789 0.0139  0.0720  0.0642  133 GLY A O   
1096 N N   . VAL A 141 ? 0.4143 0.3406 0.4026 0.0160  0.0793  0.0778  134 VAL A N   
1097 C CA  . VAL A 141 ? 0.4182 0.3442 0.3945 0.0151  0.0813  0.0766  134 VAL A CA  
1098 C C   . VAL A 141 ? 0.4271 0.3551 0.3926 0.0189  0.0710  0.0793  134 VAL A C   
1099 O O   . VAL A 141 ? 0.4679 0.3927 0.4311 0.0224  0.0648  0.0867  134 VAL A O   
1100 C CB  . VAL A 141 ? 0.4970 0.4132 0.4669 0.0139  0.0906  0.0827  134 VAL A CB  
1101 C CG1 . VAL A 141 ? 0.4590 0.3761 0.4182 0.0119  0.0951  0.0801  134 VAL A CG1 
1102 C CG2 . VAL A 141 ? 0.5218 0.4344 0.5036 0.0106  0.0993  0.0812  134 VAL A CG2 
1103 N N   . MET A 142 ? 0.4003 0.3336 0.3596 0.0183  0.0687  0.0730  135 MET A N   
1104 C CA  . MET A 142 ? 0.4128 0.3472 0.3603 0.0215  0.0592  0.0745  135 MET A CA  
1105 C C   . MET A 142 ? 0.3978 0.3318 0.3326 0.0209  0.0632  0.0714  135 MET A C   
1106 O O   . MET A 142 ? 0.4163 0.3541 0.3550 0.0178  0.0706  0.0647  135 MET A O   
1107 C CB  . MET A 142 ? 0.4688 0.4112 0.4219 0.0222  0.0497  0.0684  135 MET A CB  
1108 C CG  . MET A 142 ? 0.4974 0.4427 0.4646 0.0221  0.0465  0.0690  135 MET A CG  
1109 S SD  . MET A 142 ? 0.4932 0.4470 0.4636 0.0228  0.0346  0.0629  135 MET A SD  
1110 C CE  . MET A 142 ? 0.5292 0.4852 0.5140 0.0231  0.0314  0.0667  135 MET A CE  
1111 N N   . GLU A 143 ? 0.3878 0.3180 0.3075 0.0239  0.0580  0.0760  136 GLU A N   
1112 C CA  . GLU A 143 ? 0.4139 0.3450 0.3203 0.0242  0.0593  0.0720  136 GLU A CA  
1113 C C   . GLU A 143 ? 0.4035 0.3404 0.3084 0.0262  0.0487  0.0656  136 GLU A C   
1114 O O   . GLU A 143 ? 0.4648 0.4003 0.3663 0.0288  0.0382  0.0694  136 GLU A O   
1115 C CB  . GLU A 143 ? 0.5203 0.4432 0.4093 0.0263  0.0600  0.0801  136 GLU A CB  
1116 C CG  . GLU A 143 ? 0.5791 0.5027 0.4543 0.0262  0.0644  0.0759  136 GLU A CG  
1117 C CD  . GLU A 143 ? 0.7032 0.6182 0.5609 0.0276  0.0669  0.0843  136 GLU A CD  
1118 O OE1 . GLU A 143 ? 0.7397 0.6480 0.5962 0.0288  0.0648  0.0935  136 GLU A OE1 
1119 O OE2 . GLU A 143 ? 0.7524 0.6674 0.5972 0.0277  0.0712  0.0816  136 GLU A OE2 
1120 N N   . ILE A 144 ? 0.3918 0.3353 0.3003 0.0248  0.0512  0.0562  137 ILE A N   
1121 C CA  . ILE A 144 ? 0.3484 0.2978 0.2609 0.0260  0.0417  0.0494  137 ILE A CA  
1122 C C   . ILE A 144 ? 0.3595 0.3142 0.2693 0.0258  0.0451  0.0400  137 ILE A C   
1123 O O   . ILE A 144 ? 0.3711 0.3283 0.2842 0.0233  0.0558  0.0371  137 ILE A O   
1124 C CB  . ILE A 144 ? 0.3831 0.3368 0.3133 0.0241  0.0398  0.0482  137 ILE A CB  
1125 C CG1 . ILE A 144 ? 0.3693 0.3281 0.3031 0.0253  0.0292  0.0426  137 ILE A CG1 
1126 C CG2 . ILE A 144 ? 0.3398 0.2970 0.2815 0.0204  0.0509  0.0438  137 ILE A CG2 
1127 C CD1 . ILE A 144 ? 0.3402 0.3016 0.2878 0.0242  0.0250  0.0443  137 ILE A CD1 
1128 N N   . ASP A 145 ? 0.3530 0.3097 0.2575 0.0283  0.0360  0.0351  138 ASP A N   
1129 C CA  . ASP A 145 ? 0.3750 0.3377 0.2794 0.0288  0.0378  0.0253  138 ASP A CA  
1130 C C   . ASP A 145 ? 0.3209 0.2910 0.2430 0.0265  0.0379  0.0192  138 ASP A C   
1131 O O   . ASP A 145 ? 0.3235 0.2944 0.2529 0.0265  0.0297  0.0200  138 ASP A O   
1132 C CB  . ASP A 145 ? 0.3741 0.3351 0.2669 0.0326  0.0270  0.0221  138 ASP A CB  
1133 C CG  . ASP A 145 ? 0.4457 0.3997 0.3190 0.0351  0.0265  0.0264  138 ASP A CG  
1134 O OD1 . ASP A 145 ? 0.4447 0.3966 0.3120 0.0342  0.0364  0.0296  138 ASP A OD1 
1135 O OD2 . ASP A 145 ? 0.5167 0.4669 0.3802 0.0378  0.0157  0.0265  138 ASP A OD2 
1136 N N   . VAL A 146 ? 0.2950 0.2711 0.2238 0.0245  0.0470  0.0133  139 VAL A N   
1137 C CA  . VAL A 146 ? 0.2940 0.2776 0.2387 0.0223  0.0470  0.0069  139 VAL A CA  
1138 C C   . VAL A 146 ? 0.2772 0.2676 0.2218 0.0238  0.0479  -0.0026 139 VAL A C   
1139 O O   . VAL A 146 ? 0.3014 0.2918 0.2363 0.0253  0.0531  -0.0042 139 VAL A O   
1140 C CB  . VAL A 146 ? 0.3280 0.3131 0.2853 0.0178  0.0563  0.0087  139 VAL A CB  
1141 C CG1 . VAL A 146 ? 0.3747 0.3536 0.3340 0.0173  0.0536  0.0172  139 VAL A CG1 
1142 C CG2 . VAL A 146 ? 0.3829 0.3678 0.3365 0.0159  0.0685  0.0094  139 VAL A CG2 
1143 N N   . TYR A 147 ? 0.2672 0.2636 0.2226 0.0236  0.0429  -0.0088 140 TYR A N   
1144 C CA  . TYR A 147 ? 0.2627 0.2650 0.2182 0.0261  0.0410  -0.0178 140 TYR A CA  
1145 C C   . TYR A 147 ? 0.2574 0.2686 0.2294 0.0234  0.0440  -0.0240 140 TYR A C   
1146 O O   . TYR A 147 ? 0.2758 0.2876 0.2581 0.0204  0.0431  -0.0219 140 TYR A O   
1147 C CB  . TYR A 147 ? 0.2583 0.2576 0.2081 0.0298  0.0278  -0.0196 140 TYR A CB  
1148 C CG  . TYR A 147 ? 0.2497 0.2404 0.1827 0.0327  0.0227  -0.0145 140 TYR A CG  
1149 C CD1 . TYR A 147 ? 0.2703 0.2546 0.2003 0.0316  0.0192  -0.0057 140 TYR A CD1 
1150 C CD2 . TYR A 147 ? 0.2731 0.2621 0.1931 0.0367  0.0214  -0.0187 140 TYR A CD2 
1151 C CE1 . TYR A 147 ? 0.2676 0.2443 0.1822 0.0341  0.0140  -0.0009 140 TYR A CE1 
1152 C CE2 . TYR A 147 ? 0.2823 0.2630 0.1860 0.0392  0.0163  -0.0144 140 TYR A CE2 
1153 C CZ  . TYR A 147 ? 0.2789 0.2537 0.1801 0.0377  0.0123  -0.0054 140 TYR A CZ  
1154 O OH  . TYR A 147 ? 0.3435 0.3103 0.2285 0.0401  0.0066  -0.0008 140 TYR A OH  
1155 N N   . ASP A 148 ? 0.2589 0.2772 0.2332 0.0249  0.0469  -0.0318 141 ASP A N   
1156 C CA  . ASP A 148 ? 0.2680 0.2957 0.2578 0.0227  0.0487  -0.0383 141 ASP A CA  
1157 C C   . ASP A 148 ? 0.2673 0.3003 0.2560 0.0271  0.0448  -0.0467 141 ASP A C   
1158 O O   . ASP A 148 ? 0.2554 0.2856 0.2318 0.0311  0.0439  -0.0477 141 ASP A O   
1159 C CB  . ASP A 148 ? 0.2971 0.3299 0.2947 0.0183  0.0617  -0.0385 141 ASP A CB  
1160 C CG  . ASP A 148 ? 0.4053 0.4446 0.4196 0.0142  0.0629  -0.0418 141 ASP A CG  
1161 O OD1 . ASP A 148 ? 0.4146 0.4565 0.4347 0.0153  0.0543  -0.0454 141 ASP A OD1 
1162 O OD2 . ASP A 148 ? 0.4535 0.4949 0.4746 0.0096  0.0722  -0.0406 141 ASP A OD2 
1163 N N   . ILE A 149 ? 0.2525 0.2928 0.2537 0.0266  0.0416  -0.0526 142 ILE A N   
1164 C CA  . ILE A 149 ? 0.2511 0.2978 0.2539 0.0308  0.0390  -0.0611 142 ILE A CA  
1165 C C   . ILE A 149 ? 0.2460 0.3044 0.2642 0.0279  0.0465  -0.0665 142 ILE A C   
1166 O O   . ILE A 149 ? 0.2754 0.3359 0.3038 0.0228  0.0493  -0.0646 142 ILE A O   
1167 C CB  . ILE A 149 ? 0.2587 0.3022 0.2605 0.0342  0.0255  -0.0634 142 ILE A CB  
1168 C CG1 . ILE A 149 ? 0.3114 0.3549 0.3233 0.0304  0.0205  -0.0609 142 ILE A CG1 
1169 C CG2 . ILE A 149 ? 0.3057 0.3385 0.2907 0.0379  0.0183  -0.0597 142 ILE A CG2 
1170 C CD1 . ILE A 149 ? 0.3084 0.3502 0.3209 0.0332  0.0079  -0.0636 142 ILE A CD1 
1171 N N   . GLU A 150 ? 0.2604 0.3265 0.2802 0.0310  0.0499  -0.0734 143 GLU A N   
1172 C CA  . GLU A 150 ? 0.2395 0.3183 0.2752 0.0290  0.0547  -0.0797 143 GLU A CA  
1173 C C   . GLU A 150 ? 0.2627 0.3449 0.3044 0.0327  0.0441  -0.0858 143 GLU A C   
1174 O O   . GLU A 150 ? 0.2820 0.3628 0.3167 0.0387  0.0388  -0.0896 143 GLU A O   
1175 C CB  . GLU A 150 ? 0.3383 0.4256 0.3749 0.0300  0.0653  -0.0838 143 GLU A CB  
1176 C CG  . GLU A 150 ? 0.4070 0.5083 0.4622 0.0274  0.0693  -0.0901 143 GLU A CG  
1177 C CD  . GLU A 150 ? 0.4572 0.5696 0.5161 0.0293  0.0782  -0.0957 143 GLU A CD  
1178 O OE1 . GLU A 150 ? 0.5461 0.6581 0.5996 0.0272  0.0885  -0.0924 143 GLU A OE1 
1179 O OE2 . GLU A 150 ? 0.3861 0.5079 0.4538 0.0329  0.0749  -0.1031 143 GLU A OE2 
1180 N N   . VAL A 151 ? 0.2700 0.3566 0.3244 0.0292  0.0413  -0.0869 144 VAL A N   
1181 C CA  . VAL A 151 ? 0.2769 0.3664 0.3374 0.0320  0.0310  -0.0918 144 VAL A CA  
1182 C C   . VAL A 151 ? 0.2744 0.3779 0.3501 0.0313  0.0353  -0.0990 144 VAL A C   
1183 O O   . VAL A 151 ? 0.2889 0.3982 0.3749 0.0255  0.0419  -0.0986 144 VAL A O   
1184 C CB  . VAL A 151 ? 0.2797 0.3632 0.3419 0.0288  0.0234  -0.0873 144 VAL A CB  
1185 C CG1 . VAL A 151 ? 0.2494 0.3361 0.3180 0.0313  0.0131  -0.0922 144 VAL A CG1 
1186 C CG2 . VAL A 151 ? 0.2557 0.3264 0.3037 0.0298  0.0189  -0.0802 144 VAL A CG2 
1187 N N   . ASP A 152 ? 0.2334 0.3422 0.3108 0.0371  0.0314  -0.1057 145 ASP A N   
1188 C CA  . ASP A 152 ? 0.2407 0.3642 0.3327 0.0374  0.0356  -0.1129 145 ASP A CA  
1189 C C   . ASP A 152 ? 0.2255 0.3548 0.3314 0.0325  0.0327  -0.1139 145 ASP A C   
1190 O O   . ASP A 152 ? 0.2417 0.3654 0.3467 0.0326  0.0229  -0.1124 145 ASP A O   
1191 C CB  . ASP A 152 ? 0.2310 0.3575 0.3223 0.0455  0.0291  -0.1196 145 ASP A CB  
1192 C CG  . ASP A 152 ? 0.3597 0.5021 0.4653 0.0467  0.0349  -0.1268 145 ASP A CG  
1193 O OD1 . ASP A 152 ? 0.4413 0.5879 0.5465 0.0445  0.0454  -0.1255 145 ASP A OD1 
1194 O OD2 . ASP A 152 ? 0.4250 0.5723 0.5395 0.0482  0.0275  -0.1303 145 ASP A OD2 
1195 N N   . GLY A 153 ? 0.2161 0.3565 0.3347 0.0279  0.0415  -0.1162 146 GLY A N   
1196 C CA  . GLY A 153 ? 0.2160 0.3638 0.3486 0.0238  0.0387  -0.1189 146 GLY A CA  
1197 C C   . GLY A 153 ? 0.2207 0.3617 0.3531 0.0169  0.0390  -0.1133 146 GLY A C   
1198 O O   . GLY A 153 ? 0.2473 0.3944 0.3897 0.0107  0.0454  -0.1139 146 GLY A O   
1199 N N   . ASN A 154 ? 0.2043 0.3328 0.3256 0.0178  0.0322  -0.1079 147 ASN A N   
1200 C CA  . ASN A 154 ? 0.1838 0.3065 0.3057 0.0122  0.0311  -0.1032 147 ASN A CA  
1201 C C   . ASN A 154 ? 0.2151 0.3291 0.3294 0.0085  0.0389  -0.0962 147 ASN A C   
1202 O O   . ASN A 154 ? 0.2511 0.3628 0.3690 0.0031  0.0417  -0.0934 147 ASN A O   
1203 C CB  . ASN A 154 ? 0.1963 0.3122 0.3135 0.0145  0.0188  -0.1016 147 ASN A CB  
1204 C CG  . ASN A 154 ? 0.2041 0.3286 0.3310 0.0163  0.0115  -0.1078 147 ASN A CG  
1205 O OD1 . ASN A 154 ? 0.2167 0.3520 0.3558 0.0136  0.0155  -0.1126 147 ASN A OD1 
1206 N ND2 . ASN A 154 ? 0.2262 0.3458 0.3479 0.0207  0.0005  -0.1078 147 ASN A ND2 
1207 N N   . HIS A 155 ? 0.2422 0.3512 0.3460 0.0116  0.0425  -0.0934 148 HIS A N   
1208 C CA  . HIS A 155 ? 0.2716 0.3731 0.3683 0.0084  0.0505  -0.0867 148 HIS A CA  
1209 C C   . HIS A 155 ? 0.1927 0.2836 0.2844 0.0061  0.0464  -0.0800 148 HIS A C   
1210 O O   . HIS A 155 ? 0.2241 0.3111 0.3166 0.0014  0.0528  -0.0757 148 HIS A O   
1211 C CB  . HIS A 155 ? 0.2365 0.3450 0.3422 0.0029  0.0624  -0.0880 148 HIS A CB  
1212 C CG  . HIS A 155 ? 0.2636 0.3848 0.3772 0.0047  0.0665  -0.0950 148 HIS A CG  
1213 N ND1 . HIS A 155 ? 0.3043 0.4272 0.4113 0.0111  0.0649  -0.0975 148 HIS A ND1 
1214 C CD2 . HIS A 155 ? 0.3187 0.4520 0.4468 0.0009  0.0719  -0.1001 148 HIS A CD2 
1215 C CE1 . HIS A 155 ? 0.3561 0.4920 0.4735 0.0116  0.0696  -0.1039 148 HIS A CE1 
1216 N NE2 . HIS A 155 ? 0.3283 0.4695 0.4575 0.0051  0.0729  -0.1044 148 HIS A NE2 
1217 N N   . ASN A 156 ? 0.1883 0.2745 0.2748 0.0095  0.0356  -0.0790 149 ASN A N   
1218 C CA  . ASN A 156 ? 0.1638 0.2401 0.2442 0.0083  0.0314  -0.0722 149 ASN A CA  
1219 C C   . ASN A 156 ? 0.1676 0.2383 0.2388 0.0136  0.0206  -0.0709 149 ASN A C   
1220 O O   . ASN A 156 ? 0.1639 0.2382 0.2347 0.0178  0.0158  -0.0761 149 ASN A O   
1221 C CB  . ASN A 156 ? 0.1484 0.2264 0.2379 0.0037  0.0303  -0.0723 149 ASN A CB  
1222 C CG  . ASN A 156 ? 0.1490 0.2345 0.2463 0.0047  0.0230  -0.0787 149 ASN A CG  
1223 O OD1 . ASN A 156 ? 0.1773 0.2610 0.2703 0.0089  0.0137  -0.0794 149 ASN A OD1 
1224 N ND2 . ASN A 156 ? 0.1536 0.2471 0.2623 0.0007  0.0269  -0.0832 149 ASN A ND2 
1225 N N   . PHE A 157 ? 0.1426 0.2043 0.2064 0.0133  0.0168  -0.0641 150 PHE A N   
1226 C CA  . PHE A 157 ? 0.1503 0.2058 0.2052 0.0174  0.0063  -0.0620 150 PHE A CA  
1227 C C   . PHE A 157 ? 0.1510 0.1998 0.2039 0.0151  0.0026  -0.0549 150 PHE A C   
1228 O O   . PHE A 157 ? 0.1506 0.1981 0.2060 0.0115  0.0092  -0.0509 150 PHE A O   
1229 C CB  . PHE A 157 ? 0.1791 0.2299 0.2222 0.0215  0.0068  -0.0611 150 PHE A CB  
1230 C CG  . PHE A 157 ? 0.1944 0.2389 0.2301 0.0201  0.0131  -0.0542 150 PHE A CG  
1231 C CD1 . PHE A 157 ? 0.2583 0.3057 0.2958 0.0179  0.0246  -0.0542 150 PHE A CD1 
1232 C CD2 . PHE A 157 ? 0.1866 0.2224 0.2132 0.0210  0.0072  -0.0474 150 PHE A CD2 
1233 C CE1 . PHE A 157 ? 0.2575 0.2984 0.2875 0.0168  0.0301  -0.0474 150 PHE A CE1 
1234 C CE2 . PHE A 157 ? 0.2117 0.2418 0.2316 0.0201  0.0124  -0.0409 150 PHE A CE2 
1235 C CZ  . PHE A 157 ? 0.2578 0.2900 0.2788 0.0182  0.0238  -0.0408 150 PHE A CZ  
1236 N N   . PHE A 158 ? 0.1714 0.2160 0.2199 0.0172  -0.0080 -0.0531 151 PHE A N   
1237 C CA  . PHE A 158 ? 0.1790 0.2181 0.2256 0.0153  -0.0121 -0.0461 151 PHE A CA  
1238 C C   . PHE A 158 ? 0.1652 0.1965 0.2010 0.0171  -0.0130 -0.0398 151 PHE A C   
1239 O O   . PHE A 158 ? 0.1999 0.2279 0.2273 0.0208  -0.0179 -0.0409 151 PHE A O   
1240 C CB  . PHE A 158 ? 0.1808 0.2195 0.2287 0.0159  -0.0230 -0.0466 151 PHE A CB  
1241 C CG  . PHE A 158 ? 0.1646 0.2103 0.2226 0.0137  -0.0230 -0.0515 151 PHE A CG  
1242 C CD1 . PHE A 158 ? 0.1895 0.2366 0.2534 0.0096  -0.0207 -0.0490 151 PHE A CD1 
1243 C CD2 . PHE A 158 ? 0.1669 0.2178 0.2283 0.0159  -0.0255 -0.0587 151 PHE A CD2 
1244 C CE1 . PHE A 158 ? 0.1588 0.2121 0.2309 0.0075  -0.0211 -0.0537 151 PHE A CE1 
1245 C CE2 . PHE A 158 ? 0.2032 0.2609 0.2737 0.0140  -0.0260 -0.0632 151 PHE A CE2 
1246 C CZ  . PHE A 158 ? 0.1850 0.2437 0.2605 0.0096  -0.0240 -0.0607 151 PHE A CZ  
1247 N N   . GLY A 159 ? 0.1659 0.1942 0.2018 0.0147  -0.0082 -0.0334 152 GLY A N   
1248 C CA  . GLY A 159 ? 0.1800 0.2011 0.2066 0.0161  -0.0102 -0.0264 152 GLY A CA  
1249 C C   . GLY A 159 ? 0.1722 0.1910 0.2011 0.0145  -0.0155 -0.0202 152 GLY A C   
1250 O O   . GLY A 159 ? 0.1657 0.1867 0.2022 0.0115  -0.0108 -0.0186 152 GLY A O   
1251 N N   . ASN A 160 ? 0.2020 0.2345 0.1597 -0.0301 -0.0183 -0.0446 153 ASN A N   
1252 C CA  . ASN A 160 ? 0.2122 0.2232 0.1793 -0.0268 -0.0275 -0.0417 153 ASN A CA  
1253 C C   . ASN A 160 ? 0.2223 0.2281 0.2124 -0.0148 -0.0262 -0.0427 153 ASN A C   
1254 O O   . ASN A 160 ? 0.2164 0.2117 0.2211 -0.0148 -0.0341 -0.0333 153 ASN A O   
1255 C CB  . ASN A 160 ? 0.2226 0.2287 0.1896 -0.0393 -0.0389 -0.0265 153 ASN A CB  
1256 C CG  . ASN A 160 ? 0.2420 0.2488 0.1857 -0.0501 -0.0416 -0.0263 153 ASN A CG  
1257 O OD1 . ASN A 160 ? 0.2410 0.2442 0.1689 -0.0471 -0.0376 -0.0382 153 ASN A OD1 
1258 N ND2 . ASN A 160 ? 0.2907 0.3023 0.2314 -0.0627 -0.0483 -0.0129 153 ASN A ND2 
1259 N N   . ASP A 161 ? 0.1926 0.2060 0.1857 -0.0044 -0.0162 -0.0542 154 ASP A N   
1260 C CA  . ASP A 161 ? 0.1971 0.2060 0.2096 0.0089  -0.0133 -0.0582 154 ASP A CA  
1261 C C   . ASP A 161 ? 0.1956 0.2154 0.2266 0.0076  -0.0143 -0.0474 154 ASP A C   
1262 O O   . ASP A 161 ? 0.1907 0.2055 0.2386 0.0183  -0.0133 -0.0492 154 ASP A O   
1263 C CB  . ASP A 161 ? 0.2303 0.2153 0.2505 0.0164  -0.0195 -0.0598 154 ASP A CB  
1264 C CG  . ASP A 161 ? 0.3614 0.3350 0.3672 0.0220  -0.0165 -0.0736 154 ASP A CG  
1265 O OD1 . ASP A 161 ? 0.3644 0.3485 0.3563 0.0230  -0.0084 -0.0839 154 ASP A OD1 
1266 O OD2 . ASP A 161 ? 0.4248 0.3827 0.4328 0.0234  -0.0204 -0.0678 154 ASP A OD2 
1267 N N   . ILE A 162 ? 0.1673 0.2013 0.1953 -0.0047 -0.0163 -0.0364 155 ILE A N   
1268 C CA  . ILE A 162 ? 0.1384 0.1831 0.1836 -0.0070 -0.0178 -0.0253 155 ILE A CA  
1269 C C   . ILE A 162 ? 0.1361 0.2043 0.1781 -0.0091 -0.0080 -0.0284 155 ILE A C   
1270 O O   . ILE A 162 ? 0.1531 0.2314 0.1771 -0.0172 -0.0045 -0.0300 155 ILE A O   
1271 C CB  . ILE A 162 ? 0.1388 0.1807 0.1843 -0.0200 -0.0283 -0.0090 155 ILE A CB  
1272 C CG1 . ILE A 162 ? 0.1720 0.1904 0.2235 -0.0168 -0.0377 -0.0058 155 ILE A CG1 
1273 C CG2 . ILE A 162 ? 0.1633 0.2187 0.2240 -0.0241 -0.0295 0.0027  155 ILE A CG2 
1274 C CD1 . ILE A 162 ? 0.2082 0.2210 0.2563 -0.0297 -0.0485 0.0084  155 ILE A CD1 
1275 N N   . LEU A 163 ? 0.1270 0.2042 0.1861 -0.0018 -0.0037 -0.0292 156 LEU A N   
1276 C CA  . LEU A 163 ? 0.1218 0.2210 0.1796 -0.0021 0.0065  -0.0338 156 LEU A CA  
1277 C C   . LEU A 163 ? 0.1415 0.2568 0.1981 -0.0161 0.0048  -0.0204 156 LEU A C   
1278 O O   . LEU A 163 ? 0.1470 0.2617 0.2177 -0.0200 -0.0023 -0.0079 156 LEU A O   
1279 C CB  . LEU A 163 ? 0.1271 0.2298 0.2043 0.0108  0.0113  -0.0395 156 LEU A CB  
1280 C CG  . LEU A 163 ? 0.1251 0.2485 0.2006 0.0136  0.0232  -0.0483 156 LEU A CG  
1281 C CD1 . LEU A 163 ? 0.1761 0.2968 0.2351 0.0198  0.0307  -0.0639 156 LEU A CD1 
1282 C CD2 . LEU A 163 ? 0.1433 0.2715 0.2413 0.0241  0.0258  -0.0501 156 LEU A CD2 
1283 N N   . VAL A 164 ? 0.1429 0.2726 0.1825 -0.0235 0.0112  -0.0229 157 VAL A N   
1284 C CA  . VAL A 164 ? 0.1650 0.3108 0.2017 -0.0367 0.0109  -0.0111 157 VAL A CA  
1285 C C   . VAL A 164 ? 0.1690 0.3368 0.2055 -0.0353 0.0230  -0.0171 157 VAL A C   
1286 O O   . VAL A 164 ? 0.1723 0.3426 0.2037 -0.0265 0.0316  -0.0310 157 VAL A O   
1287 C CB  . VAL A 164 ? 0.1877 0.3291 0.2026 -0.0490 0.0060  -0.0058 157 VAL A CB  
1288 C CG1 . VAL A 164 ? 0.1911 0.3112 0.2088 -0.0507 -0.0065 0.0012  157 VAL A CG1 
1289 C CG2 . VAL A 164 ? 0.2569 0.3984 0.2505 -0.0467 0.0132  -0.0192 157 VAL A CG2 
1290 N N   . HIS A 165 ? 0.1723 0.3565 0.2151 -0.0441 0.0237  -0.0063 158 HIS A N   
1291 C CA  . HIS A 165 ? 0.2149 0.4212 0.2578 -0.0443 0.0352  -0.0104 158 HIS A CA  
1292 C C   . HIS A 165 ? 0.2108 0.4229 0.2277 -0.0501 0.0417  -0.0162 158 HIS A C   
1293 O O   . HIS A 165 ? 0.2480 0.4524 0.2481 -0.0592 0.0359  -0.0110 158 HIS A O   
1294 C CB  . HIS A 165 ? 0.2468 0.4676 0.3024 -0.0536 0.0333  0.0040  158 HIS A CB  
1295 C CG  . HIS A 165 ? 0.2606 0.5037 0.3247 -0.0517 0.0442  0.0007  158 HIS A CG  
1296 N ND1 . HIS A 165 ? 0.3814 0.6428 0.4406 -0.0630 0.0486  0.0087  158 HIS A ND1 
1297 C CD2 . HIS A 165 ? 0.2481 0.4980 0.3259 -0.0400 0.0517  -0.0094 158 HIS A CD2 
1298 C CE1 . HIS A 165 ? 0.3686 0.6476 0.4386 -0.0583 0.0585  0.0036  158 HIS A CE1 
1299 N NE2 . HIS A 165 ? 0.3058 0.5784 0.3873 -0.0444 0.0604  -0.0075 158 HIS A NE2 
1300 N N   . ALA A 166 ? 0.2176 0.4424 0.2309 -0.0441 0.0536  -0.0277 159 ALA A N   
1301 C CA  . ALA A 166 ? 0.2864 0.5182 0.2753 -0.0490 0.0608  -0.0335 159 ALA A CA  
1302 C C   . ALA A 166 ? 0.2986 0.5525 0.2861 -0.0590 0.0670  -0.0252 159 ALA A C   
1303 O O   . ALA A 166 ? 0.4013 0.6670 0.4085 -0.0597 0.0679  -0.0183 159 ALA A O   
1304 C CB  . ALA A 166 ? 0.2866 0.5186 0.2707 -0.0365 0.0705  -0.0511 159 ALA A CB  
1305 N N   . SER A 167 ? 0.3473 0.6067 0.3112 -0.0666 0.0716  -0.0263 160 SER A N   
1306 C CA  . SER A 167 ? 0.4201 0.7014 0.3823 -0.0743 0.0799  -0.0208 160 SER A CA  
1307 C C   . SER A 167 ? 0.3855 0.6805 0.3488 -0.0651 0.0937  -0.0341 160 SER A C   
1308 O O   . SER A 167 ? 0.5312 0.8165 0.4889 -0.0546 0.0963  -0.0476 160 SER A O   
1309 C CB  . SER A 167 ? 0.4851 0.7675 0.4210 -0.0869 0.0794  -0.0151 160 SER A CB  
1310 O OG  . SER A 167 ? 0.4953 0.7906 0.4158 -0.0863 0.0918  -0.0232 160 SER A OG  
1311 N N   . VAL A 168 ? 0.5100 0.8176 0.4819 -0.0670 0.0986  -0.0295 161 VAL A N   
1312 C CA  . VAL A 168 ? 0.5174 0.8288 0.4857 -0.0596 0.1081  -0.0393 161 VAL A CA  
1313 C C   . VAL A 168 ? 0.5708 0.8906 0.5216 -0.0700 0.1122  -0.0333 161 VAL A C   
1314 O O   . VAL A 168 ? 0.5648 0.8923 0.5199 -0.0800 0.1093  -0.0205 161 VAL A O   
1315 C CB  . VAL A 168 ? 0.5124 0.8292 0.5062 -0.0509 0.1111  -0.0405 161 VAL A CB  
1316 C CG1 . VAL A 168 ? 0.5941 0.9200 0.5845 -0.0494 0.1207  -0.0436 161 VAL A CG1 
1317 C CG2 . VAL A 168 ? 0.4989 0.8026 0.5033 -0.0369 0.1093  -0.0513 161 VAL A CG2 
1318 N N   . TYR A 169 ? 0.6298 0.9459 0.5607 -0.0673 0.1179  -0.0422 162 TYR A N   
1319 C CA  . TYR A 169 ? 0.6686 0.9923 0.5839 -0.0745 0.1235  -0.0386 162 TYR A CA  
1320 C C   . TYR A 169 ? 0.6992 1.0312 0.6263 -0.0663 0.1329  -0.0441 162 TYR A C   
1321 O O   . TYR A 169 ? 0.7489 1.0742 0.6742 -0.0556 0.1371  -0.0557 162 TYR A O   
1322 C CB  . TYR A 169 ? 0.6228 0.9358 0.5099 -0.0754 0.1240  -0.0451 162 TYR A CB  
1323 C CG  . TYR A 169 ? 0.5980 0.9170 0.4680 -0.0798 0.1313  -0.0440 162 TYR A CG  
1324 C CD1 . TYR A 169 ? 0.5927 0.9167 0.4525 -0.0924 0.1290  -0.0324 162 TYR A CD1 
1325 C CD2 . TYR A 169 ? 0.5692 0.8872 0.4328 -0.0711 0.1400  -0.0542 162 TYR A CD2 
1326 C CE1 . TYR A 169 ? 0.6711 0.9997 0.5150 -0.0959 0.1358  -0.0314 162 TYR A CE1 
1327 C CE2 . TYR A 169 ? 0.5759 0.8991 0.4236 -0.0748 0.1471  -0.0531 162 TYR A CE2 
1328 C CZ  . TYR A 169 ? 0.6106 0.9393 0.4484 -0.0870 0.1452  -0.0419 162 TYR A CZ  
1329 O OH  . TYR A 169 ? 0.6356 0.9687 0.4573 -0.0903 0.1524  -0.0407 162 TYR A OH  
1330 N N   . LEU A 170 ? 0.5937 0.9388 0.5328 -0.0711 0.1357  -0.0354 163 LEU A N   
1331 C CA  . LEU A 170 ? 0.6249 0.9780 0.5740 -0.0644 0.1449  -0.0398 163 LEU A CA  
1332 C C   . LEU A 170 ? 0.6694 1.0254 0.5962 -0.0676 0.1526  -0.0418 163 LEU A C   
1333 O O   . LEU A 170 ? 0.7092 1.0705 0.6251 -0.0783 0.1525  -0.0329 163 LEU A O   
1334 C CB  . LEU A 170 ? 0.5782 0.9428 0.5494 -0.0680 0.1446  -0.0298 163 LEU A CB  
1335 C CG  . LEU A 170 ? 0.5734 0.9343 0.5692 -0.0625 0.1379  -0.0287 163 LEU A CG  
1336 C CD1 . LEU A 170 ? 0.5766 0.9385 0.5807 -0.0720 0.1286  -0.0152 163 LEU A CD1 
1337 C CD2 . LEU A 170 ? 0.5382 0.9046 0.5539 -0.0543 0.1435  -0.0319 163 LEU A CD2 
1338 N N   . ASN A 171 ? 0.7210 1.0714 0.6400 -0.0583 0.1587  -0.0533 164 ASN A N   
1339 C CA  . ASN A 171 ? 0.7550 1.1072 0.6536 -0.0598 0.1667  -0.0558 164 ASN A CA  
1340 C C   . ASN A 171 ? 0.7464 1.1139 0.6579 -0.0615 0.1745  -0.0505 164 ASN A C   
1341 O O   . ASN A 171 ? 0.7945 1.1651 0.7148 -0.0533 0.1818  -0.0564 164 ASN A O   
1342 C CB  . ASN A 171 ? 0.8192 1.1600 0.7084 -0.0486 0.1703  -0.0688 164 ASN A CB  
1343 C CG  . ASN A 171 ? 0.8807 1.2214 0.7474 -0.0497 0.1781  -0.0715 164 ASN A CG  
1344 O OD1 . ASN A 171 ? 0.9053 1.2515 0.7585 -0.0594 0.1791  -0.0642 164 ASN A OD1 
1345 N ND2 . ASN A 171 ? 0.9106 1.2441 0.7727 -0.0395 0.1833  -0.0815 164 ASN A ND2 
1346 N N   . LYS A 172 ? 0.6437 1.0200 0.5567 -0.0725 0.1726  -0.0386 165 LYS A N   
1347 C CA  . LYS A 172 ? 0.6043 0.9945 0.5329 -0.0749 0.1784  -0.0319 165 LYS A CA  
1348 C C   . LYS A 172 ? 0.5907 0.9866 0.5071 -0.0734 0.1901  -0.0352 165 LYS A C   
1349 O O   . LYS A 172 ? 0.5244 0.9280 0.4548 -0.0680 0.1976  -0.0375 165 LYS A O   
1350 C CB  . LYS A 172 ? 0.5665 0.9620 0.4980 -0.0871 0.1724  -0.0179 165 LYS A CB  
1351 C CG  . LYS A 172 ? 0.5746 0.9651 0.5213 -0.0884 0.1610  -0.0131 165 LYS A CG  
1352 C CD  . LYS A 172 ? 0.6133 1.0073 0.5624 -0.1003 0.1546  0.0014  165 LYS A CD  
1353 C CE  . LYS A 172 ? 0.6444 1.0285 0.5747 -0.1080 0.1457  0.0055  165 LYS A CE  
1354 N NZ  . LYS A 172 ? 0.6795 1.0653 0.6084 -0.1198 0.1398  0.0196  165 LYS A NZ  
1355 N N   . LEU A 173 ? 0.6945 1.0859 0.5848 -0.0781 0.1916  -0.0354 166 LEU A N   
1356 C CA  . LEU A 173 ? 0.7522 1.1488 0.6289 -0.0781 0.2025  -0.0367 166 LEU A CA  
1357 C C   . LEU A 173 ? 0.7752 1.1598 0.6285 -0.0722 0.2049  -0.0471 166 LEU A C   
1358 O O   . LEU A 173 ? 0.7761 1.1618 0.6125 -0.0725 0.2129  -0.0484 166 LEU A O   
1359 C CB  . LEU A 173 ? 0.7960 1.1987 0.6624 -0.0903 0.2027  -0.0250 166 LEU A CB  
1360 C CG  . LEU A 173 ? 0.7675 1.1785 0.6552 -0.0972 0.1974  -0.0135 166 LEU A CG  
1361 C CD1 . LEU A 173 ? 0.7938 1.2032 0.6678 -0.1095 0.1915  -0.0023 166 LEU A CD1 
1362 C CD2 . LEU A 173 ? 0.7229 1.1472 0.6292 -0.0953 0.2063  -0.0110 166 LEU A CD2 
1363 N N   . ILE B 1   ? 0.5971 0.5748 0.6938 0.0029  -0.0928 0.1285  -3  ILE B N   
1364 C CA  . ILE B 1   ? 0.5350 0.5214 0.6299 0.0017  -0.0851 0.1191  -3  ILE B CA  
1365 C C   . ILE B 1   ? 0.5064 0.4901 0.6065 0.0065  -0.0742 0.1086  -3  ILE B C   
1366 O O   . ILE B 1   ? 0.4230 0.3932 0.5152 0.0047  -0.0703 0.1071  -3  ILE B O   
1367 C CB  . ILE B 1   ? 0.6004 0.5817 0.6723 -0.0101 -0.0849 0.1193  -3  ILE B CB  
1368 C CG1 . ILE B 1   ? 0.6492 0.6126 0.7029 -0.0170 -0.0810 0.1185  -3  ILE B CG1 
1369 C CG2 . ILE B 1   ? 0.6554 0.6414 0.7230 -0.0149 -0.0956 0.1292  -3  ILE B CG2 
1370 C CD1 . ILE B 1   ? 0.6998 0.6565 0.7306 -0.0294 -0.0831 0.1212  -3  ILE B CD1 
1371 N N   . ASP B 2   ? 0.4503 0.4471 0.5634 0.0123  -0.0694 0.1013  -2  ASP B N   
1372 C CA  . ASP B 2   ? 0.4151 0.4111 0.5328 0.0165  -0.0590 0.0908  -2  ASP B CA  
1373 C C   . ASP B 2   ? 0.4156 0.4050 0.5142 0.0087  -0.0526 0.0845  -2  ASP B C   
1374 O O   . ASP B 2   ? 0.4408 0.4338 0.5295 0.0027  -0.0546 0.0852  -2  ASP B O   
1375 C CB  . ASP B 2   ? 0.4699 0.4825 0.6069 0.0247  -0.0564 0.0853  -2  ASP B CB  
1376 C CG  . ASP B 2   ? 0.5443 0.5630 0.7027 0.0338  -0.0602 0.0886  -2  ASP B CG  
1377 O OD1 . ASP B 2   ? 0.6080 0.6161 0.7671 0.0353  -0.0626 0.0931  -2  ASP B OD1 
1378 O OD2 . ASP B 2   ? 0.5997 0.6337 0.7743 0.0394  -0.0608 0.0866  -2  ASP B OD2 
1379 N N   . THR B 3   ? 0.3164 0.2962 0.4103 0.0086  -0.0450 0.0781  -1  THR B N   
1380 C CA  . THR B 3   ? 0.2894 0.2631 0.3668 0.0019  -0.0384 0.0709  -1  THR B CA  
1381 C C   . THR B 3   ? 0.3406 0.3172 0.4249 0.0071  -0.0285 0.0594  -1  THR B C   
1382 O O   . THR B 3   ? 0.3470 0.3168 0.4191 0.0026  -0.0223 0.0527  -1  THR B O   
1383 C CB  . THR B 3   ? 0.3464 0.3039 0.4057 -0.0065 -0.0387 0.0739  -1  THR B CB  
1384 O OG1 . THR B 3   ? 0.4181 0.3678 0.4839 -0.0023 -0.0376 0.0752  -1  THR B OG1 
1385 C CG2 . THR B 3   ? 0.3657 0.3205 0.4140 -0.0138 -0.0482 0.0844  -1  THR B CG2 
1386 N N   . ASP B 4   ? 0.2853 0.2719 0.3889 0.0164  -0.0269 0.0568  0   ASP B N   
1387 C CA  . ASP B 4   ? 0.2470 0.2381 0.3570 0.0211  -0.0179 0.0460  0   ASP B CA  
1388 C C   . ASP B 4   ? 0.2046 0.2020 0.3076 0.0179  -0.0160 0.0411  0   ASP B C   
1389 O O   . ASP B 4   ? 0.2798 0.2842 0.3824 0.0160  -0.0217 0.0459  0   ASP B O   
1390 C CB  . ASP B 4   ? 0.2550 0.2570 0.3873 0.0310  -0.0173 0.0448  0   ASP B CB  
1391 C CG  . ASP B 4   ? 0.3003 0.3160 0.4426 0.0333  -0.0236 0.0494  0   ASP B CG  
1392 O OD1 . ASP B 4   ? 0.3887 0.4045 0.5323 0.0322  -0.0317 0.0585  0   ASP B OD1 
1393 O OD2 . ASP B 4   ? 0.3188 0.3453 0.4671 0.0359  -0.0205 0.0438  0   ASP B OD2 
1394 N N   . ALA B 5   ? 0.2020 0.1967 0.2995 0.0173  -0.0082 0.0316  1   ALA B N   
1395 C CA  . ALA B 5   ? 0.2102 0.2082 0.2992 0.0139  -0.0065 0.0267  1   ALA B CA  
1396 C C   . ALA B 5   ? 0.2256 0.2215 0.3130 0.0157  0.0025  0.0154  1   ALA B C   
1397 O O   . ALA B 5   ? 0.1993 0.1931 0.2938 0.0201  0.0074  0.0113  1   ALA B O   
1398 C CB  . ALA B 5   ? 0.2618 0.2525 0.3326 0.0042  -0.0109 0.0315  1   ALA B CB  
1399 N N   . VAL B 6   ? 0.2063 0.2026 0.2842 0.0123  0.0045  0.0102  2   VAL B N   
1400 C CA  . VAL B 6   ? 0.1811 0.1758 0.2565 0.0137  0.0122  -0.0007 2   VAL B CA  
1401 C C   . VAL B 6   ? 0.1849 0.1692 0.2424 0.0056  0.0140  -0.0040 2   VAL B C   
1402 O O   . VAL B 6   ? 0.1947 0.1748 0.2409 -0.0013 0.0092  0.0017  2   VAL B O   
1403 C CB  . VAL B 6   ? 0.1628 0.1678 0.2448 0.0179  0.0134  -0.0053 2   VAL B CB  
1404 C CG1 . VAL B 6   ? 0.1910 0.2071 0.2903 0.0246  0.0109  -0.0013 2   VAL B CG1 
1405 C CG2 . VAL B 6   ? 0.1656 0.1707 0.2364 0.0123  0.0095  -0.0035 2   VAL B CG2 
1406 N N   . VAL B 7   ? 0.1818 0.1627 0.2366 0.0064  0.0211  -0.0138 3   VAL B N   
1407 C CA  . VAL B 7   ? 0.1909 0.1623 0.2294 -0.0013 0.0234  -0.0180 3   VAL B CA  
1408 C C   . VAL B 7   ? 0.1904 0.1634 0.2204 -0.0051 0.0211  -0.0194 3   VAL B C   
1409 O O   . VAL B 7   ? 0.1812 0.1621 0.2177 -0.0009 0.0198  -0.0201 3   VAL B O   
1410 C CB  . VAL B 7   ? 0.1922 0.1601 0.2305 0.0003  0.0317  -0.0287 3   VAL B CB  
1411 C CG1 . VAL B 7   ? 0.2436 0.2089 0.2892 0.0032  0.0340  -0.0272 3   VAL B CG1 
1412 C CG2 . VAL B 7   ? 0.2222 0.1977 0.2679 0.0065  0.0354  -0.0372 3   VAL B CG2 
1413 N N   . GLY B 8   ? 0.2087 0.1735 0.2234 -0.0135 0.0210  -0.0202 4   GLY B N   
1414 C CA  . GLY B 8   ? 0.2039 0.1687 0.2093 -0.0182 0.0182  -0.0204 4   GLY B CA  
1415 C C   . GLY B 8   ? 0.1947 0.1623 0.2013 -0.0148 0.0221  -0.0301 4   GLY B C   
1416 O O   . GLY B 8   ? 0.2197 0.1894 0.2227 -0.0163 0.0190  -0.0293 4   GLY B O   
1417 N N   . ASP B 9   ? 0.2056 0.1730 0.2170 -0.0104 0.0285  -0.0391 5   ASP B N   
1418 C CA  . ASP B 9   ? 0.2357 0.2053 0.2481 -0.0070 0.0318  -0.0484 5   ASP B CA  
1419 C C   . ASP B 9   ? 0.2125 0.1915 0.2375 0.0011  0.0307  -0.0478 5   ASP B C   
1420 O O   . ASP B 9   ? 0.2488 0.2298 0.2752 0.0045  0.0327  -0.0549 5   ASP B O   
1421 C CB  . ASP B 9   ? 0.3505 0.3164 0.3617 -0.0062 0.0390  -0.0593 5   ASP B CB  
1422 C CG  . ASP B 9   ? 0.5191 0.4760 0.5160 -0.0152 0.0406  -0.0620 5   ASP B CG  
1423 O OD1 . ASP B 9   ? 0.5854 0.5391 0.5723 -0.0217 0.0365  -0.0579 5   ASP B OD1 
1424 O OD2 . ASP B 9   ? 0.6173 0.5708 0.6130 -0.0161 0.0462  -0.0685 5   ASP B OD2 
1425 N N   . THR B 10  ? 0.1872 0.1719 0.2215 0.0041  0.0273  -0.0398 6   THR B N   
1426 C CA  . THR B 10  ? 0.1752 0.1696 0.2217 0.0111  0.0264  -0.0390 6   THR B CA  
1427 C C   . THR B 10  ? 0.1991 0.1955 0.2405 0.0092  0.0225  -0.0380 6   THR B C   
1428 O O   . THR B 10  ? 0.1881 0.1823 0.2216 0.0034  0.0176  -0.0317 6   THR B O   
1429 C CB  . THR B 10  ? 0.1825 0.1823 0.2385 0.0130  0.0227  -0.0299 6   THR B CB  
1430 O OG1 . THR B 10  ? 0.1839 0.1806 0.2442 0.0144  0.0258  -0.0302 6   THR B OG1 
1431 C CG2 . THR B 10  ? 0.1713 0.1820 0.2404 0.0196  0.0219  -0.0293 6   THR B CG2 
1432 N N   . ILE B 11  ? 0.1771 0.1773 0.2225 0.0140  0.0245  -0.0440 7   ILE B N   
1433 C CA  . ILE B 11  ? 0.1929 0.1938 0.2330 0.0125  0.0211  -0.0437 7   ILE B CA  
1434 C C   . ILE B 11  ? 0.1682 0.1782 0.2162 0.0144  0.0168  -0.0364 7   ILE B C   
1435 O O   . ILE B 11  ? 0.1552 0.1731 0.2158 0.0202  0.0184  -0.0364 7   ILE B O   
1436 C CB  . ILE B 11  ? 0.2101 0.2104 0.2505 0.0166  0.0247  -0.0533 7   ILE B CB  
1437 C CG1 . ILE B 11  ? 0.2397 0.2315 0.2721 0.0142  0.0288  -0.0612 7   ILE B CG1 
1438 C CG2 . ILE B 11  ? 0.2522 0.2534 0.2884 0.0158  0.0208  -0.0522 7   ILE B CG2 
1439 C CD1 . ILE B 11  ? 0.3629 0.3539 0.3959 0.0185  0.0320  -0.0713 7   ILE B CD1 
1440 N N   . ILE B 12  ? 0.1533 0.1628 0.1943 0.0092  0.0117  -0.0307 8   ILE B N   
1441 C CA  . ILE B 12  ? 0.1642 0.1826 0.2115 0.0099  0.0073  -0.0239 8   ILE B CA  
1442 C C   . ILE B 12  ? 0.1671 0.1844 0.2064 0.0069  0.0045  -0.0242 8   ILE B C   
1443 O O   . ILE B 12  ? 0.1876 0.1964 0.2153 0.0030  0.0045  -0.0276 8   ILE B O   
1444 C CB  . ILE B 12  ? 0.1634 0.1836 0.2112 0.0060  0.0029  -0.0147 8   ILE B CB  
1445 C CG1 . ILE B 12  ? 0.1895 0.2011 0.2222 -0.0023 0.0000  -0.0122 8   ILE B CG1 
1446 C CG2 . ILE B 12  ? 0.1671 0.1878 0.2234 0.0094  0.0053  -0.0140 8   ILE B CG2 
1447 C CD1 . ILE B 12  ? 0.1728 0.1876 0.2050 -0.0067 -0.0058 -0.0023 8   ILE B CD1 
1448 N N   . ASP B 13  ? 0.1611 0.1871 0.2068 0.0084  0.0019  -0.0206 9   ASP B N   
1449 C CA  . ASP B 13  ? 0.1654 0.1909 0.2035 0.0047  -0.0016 -0.0191 9   ASP B CA  
1450 C C   . ASP B 13  ? 0.1643 0.1899 0.1964 -0.0022 -0.0067 -0.0112 9   ASP B C   
1451 O O   . ASP B 13  ? 0.1797 0.2122 0.2193 -0.0021 -0.0089 -0.0051 9   ASP B O   
1452 C CB  . ASP B 13  ? 0.1851 0.2205 0.2322 0.0085  -0.0020 -0.0186 9   ASP B CB  
1453 C CG  . ASP B 13  ? 0.2214 0.2567 0.2606 0.0038  -0.0060 -0.0160 9   ASP B CG  
1454 O OD1 . ASP B 13  ? 0.2745 0.3115 0.3097 -0.0016 -0.0102 -0.0097 9   ASP B OD1 
1455 O OD2 . ASP B 13  ? 0.3004 0.3341 0.3374 0.0057  -0.0050 -0.0204 9   ASP B OD2 
1456 N N   . VAL B 14  ? 0.1640 0.1818 0.1827 -0.0082 -0.0088 -0.0114 10  VAL B N   
1457 C CA  . VAL B 14  ? 0.1786 0.1971 0.1906 -0.0153 -0.0139 -0.0042 10  VAL B CA  
1458 C C   . VAL B 14  ? 0.1798 0.1967 0.1843 -0.0184 -0.0161 -0.0047 10  VAL B C   
1459 O O   . VAL B 14  ? 0.2004 0.2076 0.1947 -0.0204 -0.0150 -0.0097 10  VAL B O   
1460 C CB  . VAL B 14  ? 0.1866 0.1961 0.1878 -0.0212 -0.0144 -0.0034 10  VAL B CB  
1461 C CG1 . VAL B 14  ? 0.2281 0.2397 0.2230 -0.0287 -0.0201 0.0046  10  VAL B CG1 
1462 C CG2 . VAL B 14  ? 0.2146 0.2238 0.2219 -0.0183 -0.0117 -0.0036 10  VAL B CG2 
1463 N N   . SER B 15  ? 0.1738 0.2001 0.1838 -0.0187 -0.0190 -0.0001 11  SER B N   
1464 C CA  . SER B 15  ? 0.1693 0.1946 0.1721 -0.0222 -0.0213 0.0002  11  SER B CA  
1465 C C   . SER B 15  ? 0.1838 0.2014 0.1823 -0.0190 -0.0184 -0.0073 11  SER B C   
1466 O O   . SER B 15  ? 0.2343 0.2440 0.2216 -0.0230 -0.0199 -0.0088 11  SER B O   
1467 C CB  . SER B 15  ? 0.2291 0.2494 0.2195 -0.0308 -0.0252 0.0042  11  SER B CB  
1468 O OG  . SER B 15  ? 0.2277 0.2562 0.2225 -0.0336 -0.0285 0.0115  11  SER B OG  
1469 N N   . GLY B 16  ? 0.1639 0.1837 0.1714 -0.0117 -0.0145 -0.0121 12  GLY B N   
1470 C CA  . GLY B 16  ? 0.1769 0.1909 0.1818 -0.0080 -0.0122 -0.0190 12  GLY B CA  
1471 C C   . GLY B 16  ? 0.2408 0.2441 0.2401 -0.0065 -0.0092 -0.0259 12  GLY B C   
1472 O O   . GLY B 16  ? 0.2646 0.2640 0.2640 -0.0021 -0.0071 -0.0323 12  GLY B O   
1473 N N   . LYS B 17  ? 0.2199 0.1709 0.2445 0.0390  0.0093  -0.0105 13  LYS B N   
1474 C CA  . LYS B 17  ? 0.2511 0.2110 0.2757 0.0419  0.0112  -0.0133 13  LYS B CA  
1475 C C   . LYS B 17  ? 0.2218 0.1954 0.2528 0.0378  0.0104  -0.0137 13  LYS B C   
1476 O O   . LYS B 17  ? 0.2525 0.2261 0.2865 0.0317  0.0082  -0.0120 13  LYS B O   
1477 C CB  . LYS B 17  ? 0.2921 0.2446 0.3105 0.0393  0.0124  -0.0159 13  LYS B CB  
1478 C CG  . LYS B 17  ? 0.3652 0.3030 0.3774 0.0414  0.0134  -0.0161 13  LYS B CG  
1479 C CD  . LYS B 17  ? 0.3571 0.2921 0.3642 0.0421  0.0157  -0.0199 13  LYS B CD  
1480 C CE  . LYS B 17  ? 0.2992 0.2307 0.3032 0.0343  0.0144  -0.0209 13  LYS B CE  
1481 N NZ  . LYS B 17  ? 0.3864 0.3099 0.3840 0.0352  0.0168  -0.0244 13  LYS B NZ  
1482 N N   . LYS B 18  ? 0.2013 0.1862 0.2346 0.0409  0.0125  -0.0165 14  LYS B N   
1483 C CA  . LYS B 18  ? 0.2016 0.1992 0.2405 0.0368  0.0129  -0.0177 14  LYS B CA  
1484 C C   . LYS B 18  ? 0.2070 0.2053 0.2419 0.0339  0.0151  -0.0208 14  LYS B C   
1485 O O   . LYS B 18  ? 0.2261 0.2226 0.2570 0.0380  0.0173  -0.0236 14  LYS B O   
1486 C CB  . LYS B 18  ? 0.2479 0.2604 0.2938 0.0422  0.0139  -0.0194 14  LYS B CB  
1487 C CG  . LYS B 18  ? 0.3566 0.3711 0.4069 0.0443  0.0117  -0.0164 14  LYS B CG  
1488 C CD  . LYS B 18  ? 0.3936 0.4108 0.4493 0.0368  0.0099  -0.0145 14  LYS B CD  
1489 C CE  . LYS B 18  ? 0.4599 0.4800 0.5203 0.0383  0.0080  -0.0121 14  LYS B CE  
1490 N NZ  . LYS B 18  ? 0.4931 0.5274 0.5583 0.0447  0.0090  -0.0141 14  LYS B NZ  
1491 N N   . MET B 19  ? 0.1862 0.1864 0.2218 0.0267  0.0147  -0.0202 15  MET B N   
1492 C CA  . MET B 19  ? 0.1936 0.1953 0.2249 0.0229  0.0172  -0.0229 15  MET B CA  
1493 C C   . MET B 19  ? 0.1717 0.1791 0.2066 0.0162  0.0170  -0.0217 15  MET B C   
1494 O O   . MET B 19  ? 0.1672 0.1753 0.2074 0.0142  0.0143  -0.0188 15  MET B O   
1495 C CB  . MET B 19  ? 0.1945 0.1827 0.2164 0.0207  0.0165  -0.0227 15  MET B CB  
1496 C CG  . MET B 19  ? 0.1832 0.1623 0.2031 0.0150  0.0126  -0.0191 15  MET B CG  
1497 S SD  . MET B 19  ? 0.2604 0.2248 0.2699 0.0130  0.0115  -0.0197 15  MET B SD  
1498 C CE  . MET B 19  ? 0.3135 0.2704 0.3240 0.0193  0.0111  -0.0194 15  MET B CE  
1499 N N   . THR B 20  ? 0.1793 0.1905 0.2114 0.0127  0.0200  -0.0240 16  THR B N   
1500 C CA  . THR B 20  ? 0.1779 0.1917 0.2119 0.0058  0.0200  -0.0223 16  THR B CA  
1501 C C   . THR B 20  ? 0.1706 0.1715 0.1985 0.0007  0.0160  -0.0183 16  THR B C   
1502 O O   . THR B 20  ? 0.1744 0.1652 0.1947 0.0012  0.0145  -0.0180 16  THR B O   
1503 C CB  . THR B 20  ? 0.1609 0.1816 0.1930 0.0026  0.0249  -0.0258 16  THR B CB  
1504 O OG1 . THR B 20  ? 0.1949 0.2061 0.2158 -0.0002 0.0256  -0.0261 16  THR B OG1 
1505 C CG2 . THR B 20  ? 0.1878 0.2217 0.2257 0.0082  0.0289  -0.0312 16  THR B CG2 
1506 N N   . ILE B 21  ? 0.1628 0.1646 0.1945 -0.0041 0.0142  -0.0156 17  ILE B N   
1507 C CA  . ILE B 21  ? 0.1601 0.1505 0.1866 -0.0086 0.0099  -0.0120 17  ILE B CA  
1508 C C   . ILE B 21  ? 0.1744 0.1577 0.1890 -0.0120 0.0110  -0.0124 17  ILE B C   
1509 O O   . ILE B 21  ? 0.1798 0.1527 0.1875 -0.0134 0.0075  -0.0108 17  ILE B O   
1510 C CB  . ILE B 21  ? 0.1527 0.1456 0.1866 -0.0125 0.0076  -0.0092 17  ILE B CB  
1511 C CG1 . ILE B 21  ? 0.1586 0.1402 0.1892 -0.0156 0.0020  -0.0058 17  ILE B CG1 
1512 C CG2 . ILE B 21  ? 0.1755 0.1748 0.2103 -0.0166 0.0115  -0.0098 17  ILE B CG2 
1513 C CD1 . ILE B 21  ? 0.1719 0.1555 0.2114 -0.0185 -0.0009 -0.0035 17  ILE B CD1 
1514 N N   . ALA B 22  ? 0.1687 0.1581 0.1809 -0.0135 0.0161  -0.0149 18  ALA B N   
1515 C CA  . ALA B 22  ? 0.1932 0.1764 0.1933 -0.0166 0.0179  -0.0157 18  ALA B CA  
1516 C C   . ALA B 22  ? 0.2048 0.1832 0.1991 -0.0128 0.0179  -0.0183 18  ALA B C   
1517 O O   . ALA B 22  ? 0.2105 0.1795 0.1951 -0.0151 0.0159  -0.0175 18  ALA B O   
1518 C CB  . ALA B 22  ? 0.2126 0.2040 0.2120 -0.0193 0.0242  -0.0186 18  ALA B CB  
1519 N N   . GLU B 23  ? 0.1944 0.1792 0.1945 -0.0069 0.0201  -0.0215 19  GLU B N   
1520 C CA  . GLU B 23  ? 0.1900 0.1695 0.1856 -0.0028 0.0202  -0.0239 19  GLU B CA  
1521 C C   . GLU B 23  ? 0.2061 0.1745 0.1995 -0.0028 0.0149  -0.0210 19  GLU B C   
1522 O O   . GLU B 23  ? 0.2215 0.1818 0.2073 -0.0030 0.0143  -0.0223 19  GLU B O   
1523 C CB  . GLU B 23  ? 0.2147 0.2023 0.2180 0.0044  0.0225  -0.0269 19  GLU B CB  
1524 C CG  . GLU B 23  ? 0.1908 0.1890 0.1954 0.0056  0.0280  -0.0319 19  GLU B CG  
1525 C CD  . GLU B 23  ? 0.1882 0.1958 0.2017 0.0133  0.0293  -0.0346 19  GLU B CD  
1526 O OE1 . GLU B 23  ? 0.2245 0.2319 0.2437 0.0167  0.0262  -0.0318 19  GLU B OE1 
1527 O OE2 . GLU B 23  ? 0.2397 0.2553 0.2545 0.0161  0.0334  -0.0398 19  GLU B OE2 
1528 N N   . PHE B 24  ? 0.1909 0.1592 0.1912 -0.0028 0.0113  -0.0177 20  PHE B N   
1529 C CA  . PHE B 24  ? 0.1898 0.1483 0.1891 -0.0034 0.0066  -0.0157 20  PHE B CA  
1530 C C   . PHE B 24  ? 0.2029 0.1536 0.1938 -0.0089 0.0035  -0.0142 20  PHE B C   
1531 O O   . PHE B 24  ? 0.2180 0.1604 0.2031 -0.0091 0.0014  -0.0151 20  PHE B O   
1532 C CB  . PHE B 24  ? 0.2014 0.1627 0.2105 -0.0028 0.0038  -0.0130 20  PHE B CB  
1533 C CG  . PHE B 24  ? 0.1799 0.1320 0.1892 -0.0038 -0.0008 -0.0116 20  PHE B CG  
1534 C CD1 . PHE B 24  ? 0.2206 0.1649 0.2258 -0.0014 -0.0008 -0.0134 20  PHE B CD1 
1535 C CD2 . PHE B 24  ? 0.2126 0.1642 0.2269 -0.0073 -0.0048 -0.0090 20  PHE B CD2 
1536 C CE1 . PHE B 24  ? 0.2274 0.1638 0.2333 -0.0028 -0.0045 -0.0129 20  PHE B CE1 
1537 C CE2 . PHE B 24  ? 0.2511 0.1951 0.2663 -0.0084 -0.0090 -0.0085 20  PHE B CE2 
1538 C CZ  . PHE B 24  ? 0.2236 0.1602 0.2345 -0.0063 -0.0086 -0.0107 20  PHE B CZ  
1539 N N   . TYR B 25  ? 0.1776 0.1309 0.1673 -0.0132 0.0034  -0.0121 21  TYR B N   
1540 C CA  . TYR B 25  ? 0.1972 0.1430 0.1773 -0.0180 0.0005  -0.0104 21  TYR B CA  
1541 C C   . TYR B 25  ? 0.2166 0.1583 0.1855 -0.0182 0.0027  -0.0134 21  TYR B C   
1542 O O   . TYR B 25  ? 0.2360 0.1697 0.1979 -0.0196 -0.0008 -0.0134 21  TYR B O   
1543 C CB  . TYR B 25  ? 0.2120 0.1609 0.1915 -0.0223 0.0014  -0.0077 21  TYR B CB  
1544 C CG  . TYR B 25  ? 0.2151 0.1553 0.1832 -0.0267 -0.0018 -0.0053 21  TYR B CG  
1545 C CD1 . TYR B 25  ? 0.2242 0.1623 0.1805 -0.0290 0.0015  -0.0066 21  TYR B CD1 
1546 C CD2 . TYR B 25  ? 0.2416 0.1758 0.2106 -0.0283 -0.0083 -0.0021 21  TYR B CD2 
1547 C CE1 . TYR B 25  ? 0.2444 0.1740 0.1886 -0.0328 -0.0017 -0.0042 21  TYR B CE1 
1548 C CE2 . TYR B 25  ? 0.2357 0.1617 0.1935 -0.0316 -0.0120 0.0002  21  TYR B CE2 
1549 C CZ  . TYR B 25  ? 0.2532 0.1768 0.1982 -0.0338 -0.0087 -0.0006 21  TYR B CZ  
1550 O OH  . TYR B 25  ? 0.2846 0.2000 0.2171 -0.0368 -0.0124 0.0018  21  TYR B OH  
1551 N N   . ASP B 26  ? 0.2029 0.1506 0.1707 -0.0169 0.0085  -0.0165 22  ASP B N   
1552 C CA  . ASP B 26  ? 0.2276 0.1724 0.1851 -0.0175 0.0113  -0.0199 22  ASP B CA  
1553 C C   . ASP B 26  ? 0.2585 0.1977 0.2155 -0.0140 0.0099  -0.0224 22  ASP B C   
1554 O O   . ASP B 26  ? 0.3116 0.2450 0.2594 -0.0156 0.0095  -0.0244 22  ASP B O   
1555 C CB  . ASP B 26  ? 0.2665 0.2201 0.2249 -0.0166 0.0180  -0.0235 22  ASP B CB  
1556 C CG  . ASP B 26  ? 0.3311 0.2889 0.2875 -0.0215 0.0205  -0.0218 22  ASP B CG  
1557 O OD1 . ASP B 26  ? 0.3443 0.2963 0.2957 -0.0259 0.0172  -0.0176 22  ASP B OD1 
1558 O OD2 . ASP B 26  ? 0.3883 0.3552 0.3483 -0.0210 0.0261  -0.0250 22  ASP B OD2 
1559 N N   . SER B 27  ? 0.2452 0.1857 0.2114 -0.0093 0.0094  -0.0226 23  SER B N   
1560 C CA  . SER B 27  ? 0.2604 0.1948 0.2267 -0.0058 0.0088  -0.0248 23  SER B CA  
1561 C C   . SER B 27  ? 0.3013 0.2272 0.2660 -0.0082 0.0033  -0.0233 23  SER B C   
1562 O O   . SER B 27  ? 0.3359 0.2554 0.2989 -0.0066 0.0030  -0.0258 23  SER B O   
1563 C CB  . SER B 27  ? 0.3197 0.2579 0.2958 0.0000  0.0102  -0.0249 23  SER B CB  
1564 O OG  . SER B 27  ? 0.3512 0.2884 0.3339 -0.0004 0.0063  -0.0214 23  SER B OG  
1565 N N   . THR B 28  ? 0.2512 0.1767 0.2168 -0.0117 -0.0009 -0.0197 24  THR B N   
1566 C CA  . THR B 28  ? 0.2564 0.1751 0.2221 -0.0136 -0.0065 -0.0188 24  THR B CA  
1567 C C   . THR B 28  ? 0.2447 0.1580 0.1991 -0.0169 -0.0085 -0.0203 24  THR B C   
1568 O O   . THR B 28  ? 0.2667 0.1814 0.2138 -0.0198 -0.0080 -0.0190 24  THR B O   
1569 C CB  . THR B 28  ? 0.2277 0.1489 0.1999 -0.0157 -0.0104 -0.0147 24  THR B CB  
1570 O OG1 . THR B 28  ? 0.2270 0.1534 0.2097 -0.0126 -0.0086 -0.0138 24  THR B OG1 
1571 C CG2 . THR B 28  ? 0.2431 0.1581 0.2157 -0.0179 -0.0167 -0.0142 24  THR B CG2 
1572 N N   . PRO B 29  ? 0.2945 0.2016 0.2468 -0.0168 -0.0105 -0.0233 25  PRO B N   
1573 C CA  . PRO B 29  ? 0.3156 0.2184 0.2569 -0.0198 -0.0127 -0.0252 25  PRO B CA  
1574 C C   . PRO B 29  ? 0.3021 0.2040 0.2392 -0.0234 -0.0183 -0.0213 25  PRO B C   
1575 O O   . PRO B 29  ? 0.2765 0.1796 0.2209 -0.0237 -0.0216 -0.0180 25  PRO B O   
1576 C CB  . PRO B 29  ? 0.3733 0.2705 0.3167 -0.0190 -0.0145 -0.0291 25  PRO B CB  
1577 C CG  . PRO B 29  ? 0.3592 0.2571 0.3106 -0.0148 -0.0099 -0.0302 25  PRO B CG  
1578 C CD  . PRO B 29  ? 0.3181 0.2220 0.2767 -0.0136 -0.0093 -0.0258 25  PRO B CD  
1579 N N   . ASP B 30  ? 0.3075 0.2072 0.2325 -0.0261 -0.0191 -0.0218 26  ASP B N   
1580 C CA  . ASP B 30  ? 0.2999 0.1978 0.2178 -0.0294 -0.0238 -0.0177 26  ASP B CA  
1581 C C   . ASP B 30  ? 0.3023 0.1959 0.2210 -0.0300 -0.0317 -0.0178 26  ASP B C   
1582 O O   . ASP B 30  ? 0.3548 0.2448 0.2633 -0.0318 -0.0357 -0.0185 26  ASP B O   
1583 C CB  . ASP B 30  ? 0.3472 0.2438 0.2504 -0.0320 -0.0214 -0.0183 26  ASP B CB  
1584 C CG  . ASP B 30  ? 0.3862 0.2876 0.2882 -0.0325 -0.0144 -0.0173 26  ASP B CG  
1585 O OD1 . ASP B 30  ? 0.4072 0.3133 0.3198 -0.0307 -0.0119 -0.0160 26  ASP B OD1 
1586 O OD2 . ASP B 30  ? 0.4444 0.3453 0.3347 -0.0351 -0.0113 -0.0183 26  ASP B OD2 
1587 N N   . VAL B 31  ? 0.2952 0.1897 0.2264 -0.0284 -0.0340 -0.0175 27  VAL B N   
1588 C CA  . VAL B 31  ? 0.2743 0.1660 0.2093 -0.0289 -0.0414 -0.0181 27  VAL B CA  
1589 C C   . VAL B 31  ? 0.2744 0.1671 0.2128 -0.0299 -0.0452 -0.0125 27  VAL B C   
1590 O O   . VAL B 31  ? 0.2551 0.1509 0.2051 -0.0290 -0.0446 -0.0109 27  VAL B O   
1591 C CB  . VAL B 31  ? 0.2710 0.1628 0.2176 -0.0272 -0.0409 -0.0219 27  VAL B CB  
1592 C CG1 . VAL B 31  ? 0.2807 0.1709 0.2329 -0.0280 -0.0482 -0.0231 27  VAL B CG1 
1593 C CG2 . VAL B 31  ? 0.3032 0.1930 0.2460 -0.0262 -0.0366 -0.0273 27  VAL B CG2 
1594 N N   . PHE B 32  ? 0.2690 0.1589 0.1969 -0.0317 -0.0487 -0.0094 28  PHE B N   
1595 C CA  . PHE B 32  ? 0.2598 0.1496 0.1895 -0.0327 -0.0511 -0.0038 28  PHE B CA  
1596 C C   . PHE B 32  ? 0.2770 0.1652 0.2140 -0.0322 -0.0593 -0.0034 28  PHE B C   
1597 O O   . PHE B 32  ? 0.3086 0.1937 0.2410 -0.0321 -0.0653 -0.0057 28  PHE B O   
1598 C CB  . PHE B 32  ? 0.2969 0.1830 0.2112 -0.0349 -0.0507 -0.0001 28  PHE B CB  
1599 C CG  . PHE B 32  ? 0.2848 0.1737 0.1939 -0.0359 -0.0421 -0.0002 28  PHE B CG  
1600 C CD1 . PHE B 32  ? 0.2891 0.1827 0.2062 -0.0360 -0.0368 0.0019  28  PHE B CD1 
1601 C CD2 . PHE B 32  ? 0.3100 0.1975 0.2072 -0.0368 -0.0391 -0.0031 28  PHE B CD2 
1602 C CE1 . PHE B 32  ? 0.2869 0.1841 0.2002 -0.0368 -0.0289 0.0010  28  PHE B CE1 
1603 C CE2 . PHE B 32  ? 0.3463 0.2371 0.2397 -0.0377 -0.0310 -0.0040 28  PHE B CE2 
1604 C CZ  . PHE B 32  ? 0.3048 0.2006 0.2067 -0.0376 -0.0260 -0.0021 28  PHE B CZ  
1605 N N   . MET B 33  ? 0.2763 0.1674 0.2253 -0.0320 -0.0596 -0.0010 29  MET B N   
1606 C CA  . MET B 33  ? 0.2954 0.1853 0.2514 -0.0318 -0.0672 0.0003  29  MET B CA  
1607 C C   . MET B 33  ? 0.3034 0.1891 0.2514 -0.0330 -0.0703 0.0062  29  MET B C   
1608 O O   . MET B 33  ? 0.3304 0.2126 0.2779 -0.0325 -0.0781 0.0072  29  MET B O   
1609 C CB  . MET B 33  ? 0.3057 0.2007 0.2785 -0.0313 -0.0655 0.0000  29  MET B CB  
1610 C CG  . MET B 33  ? 0.3511 0.2461 0.3342 -0.0310 -0.0728 -0.0015 29  MET B CG  
1611 S SD  . MET B 33  ? 0.3821 0.2763 0.3671 -0.0303 -0.0757 -0.0090 29  MET B SD  
1612 C CE  . MET B 33  ? 0.5090 0.4039 0.5059 -0.0302 -0.0849 -0.0107 29  MET B CE  
1613 N N   . ARG B 34  ? 0.3003 0.1860 0.2419 -0.0344 -0.0641 0.0097  30  ARG B N   
1614 C CA  . ARG B 34  ? 0.2885 0.1690 0.2207 -0.0360 -0.0654 0.0155  30  ARG B CA  
1615 C C   . ARG B 34  ? 0.3125 0.1926 0.2327 -0.0381 -0.0577 0.0166  30  ARG B C   
1616 O O   . ARG B 34  ? 0.3052 0.1912 0.2305 -0.0381 -0.0505 0.0143  30  ARG B O   
1617 C CB  . ARG B 34  ? 0.3159 0.1985 0.2603 -0.0365 -0.0651 0.0188  30  ARG B CB  
1618 C CG  . ARG B 34  ? 0.4037 0.2793 0.3391 -0.0380 -0.0672 0.0249  30  ARG B CG  
1619 C CD  . ARG B 34  ? 0.5676 0.4461 0.5118 -0.0397 -0.0622 0.0277  30  ARG B CD  
1620 N NE  . ARG B 34  ? 0.6635 0.5462 0.6254 -0.0385 -0.0656 0.0268  30  ARG B NE  
1621 C CZ  . ARG B 34  ? 0.6352 0.5246 0.6100 -0.0394 -0.0606 0.0266  30  ARG B CZ  
1622 N NH1 . ARG B 34  ? 0.6176 0.5106 0.5899 -0.0413 -0.0521 0.0272  30  ARG B NH1 
1623 N NH2 . ARG B 34  ? 0.6579 0.5511 0.6482 -0.0386 -0.0640 0.0254  30  ARG B NH2 
1624 N N   . ARG B 35  ? 0.3328 0.2059 0.2364 -0.0396 -0.0592 0.0199  31  ARG B N   
1625 C CA  . ARG B 35  ? 0.3209 0.1932 0.2122 -0.0423 -0.0516 0.0208  31  ARG B CA  
1626 C C   . ARG B 35  ? 0.3556 0.2189 0.2318 -0.0446 -0.0536 0.0269  31  ARG B C   
1627 O O   . ARG B 35  ? 0.3768 0.2335 0.2426 -0.0438 -0.0608 0.0284  31  ARG B O   
1628 C CB  . ARG B 35  ? 0.3597 0.2333 0.2427 -0.0421 -0.0494 0.0159  31  ARG B CB  
1629 C CG  . ARG B 35  ? 0.3431 0.2156 0.2123 -0.0452 -0.0420 0.0165  31  ARG B CG  
1630 C CD  . ARG B 35  ? 0.3558 0.2311 0.2199 -0.0448 -0.0387 0.0107  31  ARG B CD  
1631 N NE  . ARG B 35  ? 0.3907 0.2654 0.2420 -0.0481 -0.0314 0.0108  31  ARG B NE  
1632 C CZ  . ARG B 35  ? 0.4047 0.2814 0.2491 -0.0487 -0.0274 0.0060  31  ARG B CZ  
1633 N NH1 . ARG B 35  ? 0.4407 0.3194 0.2895 -0.0461 -0.0299 0.0010  31  ARG B NH1 
1634 N NH2 . ARG B 35  ? 0.4514 0.3279 0.2846 -0.0522 -0.0205 0.0059  31  ARG B NH2 
1635 N N   . ASN B 36  ? 0.3692 0.2321 0.2439 -0.0474 -0.0470 0.0301  32  ASN B N   
1636 C CA  . ASN B 36  ? 0.4421 0.2955 0.3003 -0.0504 -0.0466 0.0359  32  ASN B CA  
1637 C C   . ASN B 36  ? 0.4017 0.2582 0.2558 -0.0543 -0.0355 0.0351  32  ASN B C   
1638 O O   . ASN B 36  ? 0.3758 0.2367 0.2406 -0.0555 -0.0303 0.0356  32  ASN B O   
1639 C CB  . ASN B 36  ? 0.4752 0.3228 0.3379 -0.0501 -0.0513 0.0415  32  ASN B CB  
1640 C CG  . ASN B 36  ? 0.5758 0.4109 0.4190 -0.0526 -0.0522 0.0480  32  ASN B CG  
1641 O OD1 . ASN B 36  ? 0.5532 0.3858 0.3846 -0.0566 -0.0444 0.0492  32  ASN B OD1 
1642 N ND2 . ASN B 36  ? 0.7087 0.5356 0.5478 -0.0502 -0.0617 0.0520  32  ASN B ND2 
1643 N N   . ASP B 37  ? 0.3964 0.2517 0.2362 -0.0561 -0.0319 0.0330  33  ASP B N   
1644 C CA  . ASP B 37  ? 0.4053 0.2642 0.2410 -0.0599 -0.0212 0.0313  33  ASP B CA  
1645 C C   . ASP B 37  ? 0.4295 0.2815 0.2582 -0.0641 -0.0174 0.0370  33  ASP B C   
1646 O O   . ASP B 37  ? 0.4828 0.3400 0.3165 -0.0669 -0.0086 0.0355  33  ASP B O   
1647 C CB  . ASP B 37  ? 0.4261 0.2841 0.2463 -0.0617 -0.0182 0.0281  33  ASP B CB  
1648 C CG  . ASP B 37  ? 0.4383 0.3039 0.2663 -0.0582 -0.0193 0.0214  33  ASP B CG  
1649 O OD1 . ASP B 37  ? 0.4040 0.2758 0.2492 -0.0546 -0.0214 0.0193  33  ASP B OD1 
1650 O OD2 . ASP B 37  ? 0.5061 0.3714 0.3229 -0.0592 -0.0176 0.0181  33  ASP B OD2 
1651 N N   . GLU B 38  ? 0.4483 0.2885 0.2655 -0.0644 -0.0238 0.0432  34  GLU B N   
1652 C CA  . GLU B 38  ? 0.5425 0.3738 0.3505 -0.0686 -0.0198 0.0491  34  GLU B CA  
1653 C C   . GLU B 38  ? 0.4770 0.3124 0.3032 -0.0685 -0.0178 0.0501  34  GLU B C   
1654 O O   . GLU B 38  ? 0.5290 0.3637 0.3546 -0.0728 -0.0096 0.0513  34  GLU B O   
1655 C CB  . GLU B 38  ? 0.6049 0.4216 0.3956 -0.0681 -0.0280 0.0559  34  GLU B CB  
1656 C CG  . GLU B 38  ? 0.7591 0.5717 0.5307 -0.0682 -0.0307 0.0550  34  GLU B CG  
1657 C CD  . GLU B 38  ? 0.8811 0.6968 0.6580 -0.0627 -0.0411 0.0523  34  GLU B CD  
1658 O OE1 . GLU B 38  ? 0.8948 0.7203 0.6792 -0.0613 -0.0396 0.0455  34  GLU B OE1 
1659 O OE2 . GLU B 38  ? 0.9381 0.7466 0.7122 -0.0597 -0.0507 0.0566  34  GLU B OE2 
1660 N N   . ALA B 39  ? 0.4425 0.2823 0.2850 -0.0640 -0.0248 0.0493  35  ALA B N   
1661 C CA  . ALA B 39  ? 0.4261 0.2719 0.2878 -0.0636 -0.0232 0.0491  35  ALA B CA  
1662 C C   . ALA B 39  ? 0.4552 0.3158 0.3324 -0.0633 -0.0162 0.0425  35  ALA B C   
1663 O O   . ALA B 39  ? 0.4631 0.3302 0.3560 -0.0633 -0.0137 0.0418  35  ALA B O   
1664 C CB  . ALA B 39  ? 0.4831 0.3276 0.3556 -0.0591 -0.0337 0.0506  35  ALA B CB  
1665 N N   . ARG B 40  ? 0.3867 0.2529 0.2597 -0.0628 -0.0130 0.0377  36  ARG B N   
1666 C CA  . ARG B 40  ? 0.3801 0.2600 0.2671 -0.0613 -0.0075 0.0313  36  ARG B CA  
1667 C C   . ARG B 40  ? 0.3210 0.2080 0.2272 -0.0570 -0.0124 0.0296  36  ARG B C   
1668 O O   . ARG B 40  ? 0.3282 0.2238 0.2492 -0.0568 -0.0087 0.0279  36  ARG B O   
1669 C CB  . ARG B 40  ? 0.3632 0.2488 0.2524 -0.0653 0.0031  0.0296  36  ARG B CB  
1670 C CG  . ARG B 40  ? 0.4617 0.3404 0.3314 -0.0702 0.0087  0.0305  36  ARG B CG  
1671 C CD  . ARG B 40  ? 0.5485 0.4352 0.4212 -0.0740 0.0200  0.0265  36  ARG B CD  
1672 N NE  . ARG B 40  ? 0.6143 0.4960 0.4687 -0.0784 0.0256  0.0257  36  ARG B NE  
1673 C CZ  . ARG B 40  ? 0.7220 0.5938 0.5625 -0.0841 0.0298  0.0297  36  ARG B CZ  
1674 N NH1 . ARG B 40  ? 0.7740 0.6395 0.6173 -0.0858 0.0289  0.0349  36  ARG B NH1 
1675 N NH2 . ARG B 40  ? 0.6917 0.5595 0.5153 -0.0882 0.0351  0.0285  36  ARG B NH2 
1676 N N   . ASP B 41  ? 0.3229 0.2066 0.2287 -0.0537 -0.0207 0.0297  37  ASP B N   
1677 C CA  . ASP B 41  ? 0.3394 0.2275 0.2613 -0.0501 -0.0264 0.0285  37  ASP B CA  
1678 C C   . ASP B 41  ? 0.3271 0.2161 0.2480 -0.0469 -0.0307 0.0248  37  ASP B C   
1679 O O   . ASP B 41  ? 0.3356 0.2172 0.2441 -0.0468 -0.0356 0.0258  37  ASP B O   
1680 C CB  . ASP B 41  ? 0.4140 0.2943 0.3368 -0.0502 -0.0335 0.0335  37  ASP B CB  
1681 C CG  . ASP B 41  ? 0.5409 0.4256 0.4801 -0.0470 -0.0395 0.0318  37  ASP B CG  
1682 O OD1 . ASP B 41  ? 0.5277 0.4222 0.4805 -0.0458 -0.0361 0.0281  37  ASP B OD1 
1683 O OD2 . ASP B 41  ? 0.6353 0.5135 0.5735 -0.0457 -0.0477 0.0341  37  ASP B OD2 
1684 N N   . TRP B 42  ? 0.2840 0.1817 0.2175 -0.0443 -0.0286 0.0204  38  TRP B N   
1685 C CA  . TRP B 42  ? 0.2830 0.1818 0.2166 -0.0415 -0.0311 0.0162  38  TRP B CA  
1686 C C   . TRP B 42  ? 0.2515 0.1560 0.2019 -0.0386 -0.0333 0.0139  38  TRP B C   
1687 O O   . TRP B 42  ? 0.2590 0.1708 0.2207 -0.0382 -0.0292 0.0134  38  TRP B O   
1688 C CB  . TRP B 42  ? 0.2695 0.1725 0.1979 -0.0414 -0.0239 0.0124  38  TRP B CB  
1689 C CG  . TRP B 42  ? 0.2879 0.1863 0.1999 -0.0447 -0.0204 0.0137  38  TRP B CG  
1690 C CD1 . TRP B 42  ? 0.3120 0.2039 0.2092 -0.0456 -0.0229 0.0133  38  TRP B CD1 
1691 C CD2 . TRP B 42  ? 0.2959 0.1961 0.2041 -0.0481 -0.0133 0.0150  38  TRP B CD2 
1692 N NE1 . TRP B 42  ? 0.3338 0.2230 0.2177 -0.0493 -0.0178 0.0148  38  TRP B NE1 
1693 C CE2 . TRP B 42  ? 0.3326 0.2264 0.2230 -0.0511 -0.0116 0.0157  38  TRP B CE2 
1694 C CE3 . TRP B 42  ? 0.2982 0.2051 0.2165 -0.0491 -0.0079 0.0152  38  TRP B CE3 
1695 C CZ2 . TRP B 42  ? 0.3396 0.2330 0.2218 -0.0553 -0.0045 0.0166  38  TRP B CZ2 
1696 C CZ3 . TRP B 42  ? 0.3088 0.2157 0.2197 -0.0532 -0.0009 0.0158  38  TRP B CZ3 
1697 C CH2 . TRP B 42  ? 0.3457 0.2455 0.2385 -0.0564 0.0009  0.0165  38  TRP B CH2 
1698 N N   . VAL B 43  ? 0.2415 0.1432 0.1932 -0.0367 -0.0394 0.0120  39  VAL B N   
1699 C CA  . VAL B 43  ? 0.2364 0.1426 0.2023 -0.0343 -0.0410 0.0091  39  VAL B CA  
1700 C C   . VAL B 43  ? 0.2368 0.1413 0.1989 -0.0325 -0.0417 0.0047  39  VAL B C   
1701 O O   . VAL B 43  ? 0.2521 0.1508 0.2055 -0.0330 -0.0465 0.0041  39  VAL B O   
1702 C CB  . VAL B 43  ? 0.2417 0.1459 0.2161 -0.0344 -0.0483 0.0106  39  VAL B CB  
1703 C CG1 . VAL B 43  ? 0.2552 0.1642 0.2438 -0.0325 -0.0489 0.0072  39  VAL B CG1 
1704 C CG2 . VAL B 43  ? 0.2538 0.1583 0.2314 -0.0363 -0.0478 0.0151  39  VAL B CG2 
1705 N N   . LYS B 44  ? 0.2354 0.1447 0.2040 -0.0305 -0.0370 0.0015  40  LYS B N   
1706 C CA  . LYS B 44  ? 0.2382 0.1456 0.2049 -0.0287 -0.0367 -0.0029 40  LYS B CA  
1707 C C   . LYS B 44  ? 0.2317 0.1401 0.2106 -0.0272 -0.0390 -0.0051 40  LYS B C   
1708 O O   . LYS B 44  ? 0.2074 0.1207 0.1970 -0.0265 -0.0375 -0.0040 40  LYS B O   
1709 C CB  . LYS B 44  ? 0.2217 0.1324 0.1856 -0.0270 -0.0293 -0.0052 40  LYS B CB  
1710 C CG  . LYS B 44  ? 0.2449 0.1545 0.1958 -0.0288 -0.0260 -0.0047 40  LYS B CG  
1711 C CD  . LYS B 44  ? 0.2374 0.1515 0.1881 -0.0266 -0.0187 -0.0079 40  LYS B CD  
1712 C CE  . LYS B 44  ? 0.2544 0.1682 0.1929 -0.0289 -0.0148 -0.0081 40  LYS B CE  
1713 N NZ  . LYS B 44  ? 0.2660 0.1849 0.2057 -0.0264 -0.0080 -0.0119 40  LYS B NZ  
1714 N N   . ARG B 45  ? 0.2328 0.1369 0.2103 -0.0270 -0.0425 -0.0086 41  ARG B N   
1715 C CA  . ARG B 45  ? 0.2270 0.1313 0.2146 -0.0258 -0.0430 -0.0117 41  ARG B CA  
1716 C C   . ARG B 45  ? 0.2501 0.1562 0.2390 -0.0233 -0.0360 -0.0134 41  ARG B C   
1717 O O   . ARG B 45  ? 0.2714 0.1768 0.2520 -0.0224 -0.0321 -0.0144 41  ARG B O   
1718 C CB  . ARG B 45  ? 0.2324 0.1318 0.2173 -0.0266 -0.0478 -0.0159 41  ARG B CB  
1719 C CG  . ARG B 45  ? 0.2547 0.1524 0.2379 -0.0283 -0.0555 -0.0145 41  ARG B CG  
1720 C CD  . ARG B 45  ? 0.2795 0.1737 0.2601 -0.0288 -0.0604 -0.0196 41  ARG B CD  
1721 N NE  . ARG B 45  ? 0.2960 0.1907 0.2883 -0.0289 -0.0608 -0.0239 41  ARG B NE  
1722 C CZ  . ARG B 45  ? 0.3123 0.2044 0.3045 -0.0294 -0.0618 -0.0299 41  ARG B CZ  
1723 N NH1 . ARG B 45  ? 0.2925 0.1821 0.2739 -0.0295 -0.0626 -0.0323 41  ARG B NH1 
1724 N NH2 . ARG B 45  ? 0.3848 0.2794 0.3877 -0.0294 -0.0601 -0.0331 41  ARG B NH2 
1725 N N   . VAL B 46  ? 0.2439 0.2025 0.2123 -0.0431 -0.0544 0.0007  42  VAL B N   
1726 C CA  . VAL B 46  ? 0.2600 0.2110 0.2227 -0.0430 -0.0474 -0.0009 42  VAL B CA  
1727 C C   . VAL B 46  ? 0.2845 0.2386 0.2493 -0.0491 -0.0471 -0.0008 42  VAL B C   
1728 O O   . VAL B 46  ? 0.2617 0.2305 0.2399 -0.0499 -0.0490 0.0001  42  VAL B O   
1729 C CB  . VAL B 46  ? 0.2146 0.1707 0.1848 -0.0353 -0.0422 -0.0015 42  VAL B CB  
1730 C CG1 . VAL B 46  ? 0.2607 0.2105 0.2258 -0.0344 -0.0362 -0.0026 42  VAL B CG1 
1731 C CG2 . VAL B 46  ? 0.2378 0.1889 0.2038 -0.0313 -0.0415 -0.0022 42  VAL B CG2 
1732 N N   . GLY B 47  ? 0.3000 0.2397 0.2513 -0.0534 -0.0442 -0.0019 43  GLY B N   
1733 C CA  . GLY B 47  ? 0.3080 0.2469 0.2581 -0.0606 -0.0432 -0.0018 43  GLY B CA  
1734 C C   . GLY B 47  ? 0.2778 0.2064 0.2209 -0.0583 -0.0363 -0.0022 43  GLY B C   
1735 O O   . GLY B 47  ? 0.3370 0.2514 0.2686 -0.0543 -0.0329 -0.0033 43  GLY B O   
1736 N N   . GLY B 48  ? 0.2852 0.2210 0.2350 -0.0607 -0.0340 -0.0012 44  GLY B N   
1737 C CA  . GLY B 48  ? 0.2822 0.2062 0.2229 -0.0600 -0.0282 -0.0009 44  GLY B CA  
1738 C C   . GLY B 48  ? 0.2718 0.1951 0.2135 -0.0494 -0.0243 -0.0008 44  GLY B C   
1739 O O   . GLY B 48  ? 0.3343 0.2444 0.2653 -0.0471 -0.0204 -0.0005 44  GLY B O   
1740 N N   . LYS B 49  ? 0.2427 0.1798 0.1968 -0.0429 -0.0256 -0.0010 45  LYS B N   
1741 C CA  . LYS B 49  ? 0.2210 0.1589 0.1764 -0.0336 -0.0226 -0.0015 45  LYS B CA  
1742 C C   . LYS B 49  ? 0.2096 0.1630 0.1782 -0.0308 -0.0218 -0.0009 45  LYS B C   
1743 O O   . LYS B 49  ? 0.2485 0.2150 0.2286 -0.0333 -0.0243 -0.0007 45  LYS B O   
1744 C CB  . LYS B 49  ? 0.2248 0.1621 0.1803 -0.0287 -0.0239 -0.0031 45  LYS B CB  
1745 C CG  . LYS B 49  ? 0.2691 0.1922 0.2118 -0.0316 -0.0245 -0.0043 45  LYS B CG  
1746 C CD  . LYS B 49  ? 0.2892 0.1964 0.2187 -0.0301 -0.0207 -0.0049 45  LYS B CD  
1747 C CE  . LYS B 49  ? 0.3306 0.2234 0.2471 -0.0320 -0.0205 -0.0069 45  LYS B CE  
1748 N NZ  . LYS B 49  ? 0.4261 0.3001 0.3276 -0.0315 -0.0172 -0.0076 45  LYS B NZ  
1749 N N   . THR B 50  ? 0.1979 0.1498 0.1646 -0.0249 -0.0185 -0.0010 46  THR B N   
1750 C CA  . THR B 50  ? 0.1861 0.1505 0.1626 -0.0216 -0.0170 -0.0009 46  THR B CA  
1751 C C   . THR B 50  ? 0.2169 0.1830 0.1945 -0.0132 -0.0164 -0.0025 46  THR B C   
1752 O O   . THR B 50  ? 0.2147 0.1724 0.1852 -0.0097 -0.0163 -0.0034 46  THR B O   
1753 C CB  . THR B 50  ? 0.2354 0.1964 0.2066 -0.0243 -0.0133 0.0006  46  THR B CB  
1754 O OG1 . THR B 50  ? 0.2466 0.1928 0.2040 -0.0202 -0.0116 0.0012  46  THR B OG1 
1755 C CG2 . THR B 50  ? 0.2590 0.2192 0.2293 -0.0343 -0.0132 0.0018  46  THR B CG2 
1756 N N   . SER B 51  ? 0.1972 0.1745 0.1838 -0.0102 -0.0157 -0.0032 47  SER B N   
1757 C CA  . SER B 51  ? 0.1972 0.1769 0.1846 -0.0034 -0.0150 -0.0050 47  SER B CA  
1758 C C   . SER B 51  ? 0.2175 0.2040 0.2078 -0.0017 -0.0127 -0.0051 47  SER B C   
1759 O O   . SER B 51  ? 0.2248 0.2150 0.2176 -0.0057 -0.0110 -0.0039 47  SER B O   
1760 C CB  . SER B 51  ? 0.2501 0.2348 0.2441 -0.0014 -0.0170 -0.0070 47  SER B CB  
1761 O OG  . SER B 51  ? 0.2532 0.2390 0.2464 0.0039  -0.0163 -0.0093 47  SER B OG  
1762 N N   . LEU B 52  ? 0.2077 0.1963 0.1974 0.0038  -0.0124 -0.0068 48  LEU B N   
1763 C CA  . LEU B 52  ? 0.1948 0.1888 0.1852 0.0057  -0.0103 -0.0073 48  LEU B CA  
1764 C C   . LEU B 52  ? 0.2165 0.2208 0.2178 0.0067  -0.0104 -0.0098 48  LEU B C   
1765 O O   . LEU B 52  ? 0.2616 0.2674 0.2669 0.0083  -0.0124 -0.0116 48  LEU B O   
1766 C CB  . LEU B 52  ? 0.2243 0.2148 0.2071 0.0112  -0.0109 -0.0081 48  LEU B CB  
1767 C CG  . LEU B 52  ? 0.2662 0.2443 0.2363 0.0117  -0.0107 -0.0054 48  LEU B CG  
1768 C CD1 . LEU B 52  ? 0.3538 0.3297 0.3181 0.0189  -0.0128 -0.0064 48  LEU B CD1 
1769 C CD2 . LEU B 52  ? 0.2990 0.2731 0.2626 0.0077  -0.0076 -0.0027 48  LEU B CD2 
1770 N N   . SER B 53  ? 0.1925 0.2027 0.1971 0.0059  -0.0077 -0.0101 49  SER B N   
1771 C CA  . SER B 53  ? 0.1815 0.2002 0.1960 0.0073  -0.0072 -0.0125 49  SER B CA  
1772 C C   . SER B 53  ? 0.1844 0.2070 0.1973 0.0084  -0.0033 -0.0138 49  SER B C   
1773 O O   . SER B 53  ? 0.2038 0.2223 0.2076 0.0073  -0.0013 -0.0123 49  SER B O   
1774 C CB  . SER B 53  ? 0.1758 0.1997 0.1997 0.0045  -0.0081 -0.0115 49  SER B CB  
1775 O OG  . SER B 53  ? 0.1889 0.2164 0.2137 0.0005  -0.0052 -0.0099 49  SER B OG  
1776 N N   . VAL B 54  ? 0.1664 0.1952 0.1863 0.0107  -0.0021 -0.0166 50  VAL B N   
1777 C CA  . VAL B 54  ? 0.1618 0.1945 0.1804 0.0116  0.0024  -0.0185 50  VAL B CA  
1778 C C   . VAL B 54  ? 0.1536 0.1955 0.1842 0.0115  0.0051  -0.0196 50  VAL B C   
1779 O O   . VAL B 54  ? 0.1675 0.2120 0.2069 0.0138  0.0026  -0.0207 50  VAL B O   
1780 C CB  . VAL B 54  ? 0.1833 0.2146 0.1978 0.0152  0.0021  -0.0221 50  VAL B CB  
1781 C CG1 . VAL B 54  ? 0.1865 0.2207 0.1979 0.0158  0.0071  -0.0245 50  VAL B CG1 
1782 C CG2 . VAL B 54  ? 0.2086 0.2339 0.2133 0.0159  -0.0011 -0.0214 50  VAL B CG2 
1783 N N   . ASN B 55  ? 0.1551 0.2019 0.1858 0.0088  0.0100  -0.0193 51  ASN B N   
1784 C CA  . ASN B 55  ? 0.1388 0.1972 0.1822 0.0094  0.0135  -0.0211 51  ASN B CA  
1785 C C   . ASN B 55  ? 0.1416 0.2012 0.1856 0.0146  0.0163  -0.0256 51  ASN B C   
1786 O O   . ASN B 55  ? 0.1814 0.2376 0.2154 0.0145  0.0200  -0.0271 51  ASN B O   
1787 C CB  . ASN B 55  ? 0.1639 0.2271 0.2060 0.0035  0.0190  -0.0197 51  ASN B CB  
1788 C CG  . ASN B 55  ? 0.1658 0.2444 0.2231 0.0034  0.0234  -0.0220 51  ASN B CG  
1789 O OD1 . ASN B 55  ? 0.1629 0.2474 0.2268 0.0087  0.0261  -0.0258 51  ASN B OD1 
1790 N ND2 . ASN B 55  ? 0.2025 0.2884 0.2661 -0.0028 0.0242  -0.0200 51  ASN B ND2 
1791 N N   . THR B 56  ? 0.1637 0.2261 0.2175 0.0193  0.0143  -0.0276 52  THR B N   
1792 C CA  . THR B 56  ? 0.2061 0.2663 0.2585 0.0243  0.0167  -0.0321 52  THR B CA  
1793 C C   . THR B 56  ? 0.1899 0.2586 0.2464 0.0256  0.0242  -0.0353 52  THR B C   
1794 O O   . THR B 56  ? 0.2324 0.2976 0.2838 0.0287  0.0275  -0.0394 52  THR B O   
1795 C CB  . THR B 56  ? 0.2256 0.2831 0.2849 0.0292  0.0125  -0.0332 52  THR B CB  
1796 O OG1 . THR B 56  ? 0.2463 0.3139 0.3199 0.0314  0.0121  -0.0324 52  THR B OG1 
1797 C CG2 . THR B 56  ? 0.2640 0.3124 0.3179 0.0273  0.0062  -0.0306 52  THR B CG2 
1798 N N   . TYR B 57  ? 0.1421 0.2220 0.2069 0.0226  0.0276  -0.0339 53  TYR B N   
1799 C CA  . TYR B 57  ? 0.1578 0.2475 0.2268 0.0229  0.0360  -0.0373 53  TYR B CA  
1800 C C   . TYR B 57  ? 0.1878 0.2723 0.2410 0.0174  0.0413  -0.0368 53  TYR B C   
1801 O O   . TYR B 57  ? 0.2012 0.2854 0.2487 0.0189  0.0476  -0.0406 53  TYR B O   
1802 C CB  . TYR B 57  ? 0.1605 0.2667 0.2468 0.0212  0.0375  -0.0364 53  TYR B CB  
1803 C CG  . TYR B 57  ? 0.1806 0.2995 0.2729 0.0203  0.0472  -0.0400 53  TYR B CG  
1804 C CD1 . TYR B 57  ? 0.1955 0.3208 0.2963 0.0279  0.0515  -0.0452 53  TYR B CD1 
1805 C CD2 . TYR B 57  ? 0.2010 0.3249 0.2897 0.0115  0.0527  -0.0382 53  TYR B CD2 
1806 C CE1 . TYR B 57  ? 0.2034 0.3414 0.3100 0.0272  0.0616  -0.0491 53  TYR B CE1 
1807 C CE2 . TYR B 57  ? 0.2684 0.4045 0.3622 0.0096  0.0627  -0.0417 53  TYR B CE2 
1808 C CZ  . TYR B 57  ? 0.1928 0.3370 0.2963 0.0176  0.0673  -0.0473 53  TYR B CZ  
1809 O OH  . TYR B 57  ? 0.2691 0.4265 0.3781 0.0159  0.0783  -0.0514 53  TYR B OH  
1810 N N   . SER B 58  ? 0.1893 0.2689 0.2345 0.0112  0.0392  -0.0322 54  SER B N   
1811 C CA  . SER B 58  ? 0.2019 0.2742 0.2300 0.0062  0.0434  -0.0308 54  SER B CA  
1812 C C   . SER B 58  ? 0.2172 0.2753 0.2285 0.0081  0.0389  -0.0301 54  SER B C   
1813 O O   . SER B 58  ? 0.2395 0.2909 0.2352 0.0062  0.0421  -0.0300 54  SER B O   
1814 C CB  . SER B 58  ? 0.2126 0.2845 0.2383 -0.0015 0.0438  -0.0261 54  SER B CB  
1815 O OG  . SER B 58  ? 0.2140 0.2774 0.2368 -0.0014 0.0357  -0.0225 54  SER B OG  
1816 N N   . GLY B 59  ? 0.1974 0.2513 0.2114 0.0116  0.0315  -0.0297 55  GLY B N   
1817 C CA  . GLY B 59  ? 0.2098 0.2532 0.2107 0.0130  0.0265  -0.0292 55  GLY B CA  
1818 C C   . GLY B 59  ? 0.2294 0.2651 0.2204 0.0100  0.0230  -0.0243 55  GLY B C   
1819 O O   . GLY B 59  ? 0.2628 0.2914 0.2434 0.0119  0.0187  -0.0239 55  GLY B O   
1820 N N   . GLU B 60  ? 0.2083 0.2455 0.2028 0.0057  0.0242  -0.0208 56  GLU B N   
1821 C CA  . GLU B 60  ? 0.2353 0.2624 0.2181 0.0027  0.0219  -0.0162 56  GLU B CA  
1822 C C   . GLU B 60  ? 0.2278 0.2526 0.2163 0.0038  0.0154  -0.0144 56  GLU B C   
1823 O O   . GLU B 60  ? 0.2122 0.2441 0.2145 0.0039  0.0140  -0.0153 56  GLU B O   
1824 C CB  . GLU B 60  ? 0.2611 0.2887 0.2418 -0.0043 0.0275  -0.0137 56  GLU B CB  
1825 C CG  . GLU B 60  ? 0.3646 0.3915 0.3350 -0.0068 0.0350  -0.0146 56  GLU B CG  
1826 C CD  . GLU B 60  ? 0.5445 0.5573 0.4934 -0.0049 0.0331  -0.0128 56  GLU B CD  
1827 O OE1 . GLU B 60  ? 0.5971 0.5982 0.5352 -0.0054 0.0292  -0.0086 56  GLU B OE1 
1828 O OE2 . GLU B 60  ? 0.6148 0.6278 0.5571 -0.0024 0.0352  -0.0157 56  GLU B OE2 
1829 N N   . VAL B 61  ? 0.2269 0.2412 0.2039 0.0050  0.0115  -0.0119 57  VAL B N   
1830 C CA  . VAL B 61  ? 0.2337 0.2442 0.2136 0.0054  0.0066  -0.0101 57  VAL B CA  
1831 C C   . VAL B 61  ? 0.2583 0.2665 0.2388 -0.0008 0.0086  -0.0071 57  VAL B C   
1832 O O   . VAL B 61  ? 0.2909 0.2935 0.2616 -0.0050 0.0124  -0.0048 57  VAL B O   
1833 C CB  . VAL B 61  ? 0.2589 0.2599 0.2268 0.0095  0.0024  -0.0089 57  VAL B CB  
1834 C CG1 . VAL B 61  ? 0.2717 0.2677 0.2412 0.0097  -0.0013 -0.0072 57  VAL B CG1 
1835 C CG2 . VAL B 61  ? 0.2590 0.2647 0.2280 0.0145  0.0000  -0.0126 57  VAL B CG2 
1836 N N   . GLU B 62  ? 0.2095 0.2216 0.2006 -0.0022 0.0059  -0.0071 58  GLU B N   
1837 C CA  . GLU B 62  ? 0.2425 0.2535 0.2352 -0.0088 0.0068  -0.0048 58  GLU B CA  
1838 C C   . GLU B 62  ? 0.2225 0.2277 0.2154 -0.0086 0.0017  -0.0038 58  GLU B C   
1839 O O   . GLU B 62  ? 0.2216 0.2301 0.2211 -0.0045 -0.0018 -0.0055 58  GLU B O   
1840 C CB  . GLU B 62  ? 0.2261 0.2522 0.2342 -0.0121 0.0093  -0.0064 58  GLU B CB  
1841 C CG  . GLU B 62  ? 0.2322 0.2650 0.2406 -0.0131 0.0159  -0.0079 58  GLU B CG  
1842 C CD  . GLU B 62  ? 0.2808 0.3307 0.3065 -0.0152 0.0188  -0.0102 58  GLU B CD  
1843 O OE1 . GLU B 62  ? 0.2582 0.3161 0.2970 -0.0118 0.0148  -0.0115 58  GLU B OE1 
1844 O OE2 . GLU B 62  ? 0.3463 0.4019 0.3721 -0.0198 0.0254  -0.0106 58  GLU B OE2 
1845 N N   . ARG B 63  ? 0.2159 0.2113 0.2004 -0.0135 0.0018  -0.0012 59  ARG B N   
1846 C CA  . ARG B 63  ? 0.2232 0.2125 0.2071 -0.0147 -0.0021 -0.0005 59  ARG B CA  
1847 C C   . ARG B 63  ? 0.2337 0.2330 0.2297 -0.0205 -0.0032 -0.0008 59  ARG B C   
1848 O O   . ARG B 63  ? 0.2555 0.2591 0.2536 -0.0272 -0.0001 -0.0002 59  ARG B O   
1849 C CB  . ARG B 63  ? 0.2544 0.2263 0.2218 -0.0172 -0.0014 0.0022  59  ARG B CB  
1850 C CG  . ARG B 63  ? 0.2683 0.2315 0.2324 -0.0183 -0.0048 0.0024  59  ARG B CG  
1851 C CD  . ARG B 63  ? 0.3022 0.2456 0.2484 -0.0169 -0.0043 0.0043  59  ARG B CD  
1852 N NE  . ARG B 63  ? 0.2952 0.2351 0.2363 -0.0073 -0.0056 0.0038  59  ARG B NE  
1853 C CZ  . ARG B 63  ? 0.2949 0.2375 0.2404 -0.0012 -0.0084 0.0016  59  ARG B CZ  
1854 N NH1 . ARG B 63  ? 0.2538 0.2007 0.2069 -0.0036 -0.0102 0.0002  59  ARG B NH1 
1855 N NH2 . ARG B 63  ? 0.2950 0.2367 0.2371 0.0070  -0.0096 0.0009  59  ARG B NH2 
1856 N N   . LYS B 64  ? 0.1976 0.2010 0.2013 -0.0182 -0.0075 -0.0020 60  LYS B N   
1857 C CA  . LYS B 64  ? 0.1905 0.2050 0.2067 -0.0217 -0.0101 -0.0024 60  LYS B CA  
1858 C C   . LYS B 64  ? 0.1862 0.1935 0.1990 -0.0234 -0.0150 -0.0018 60  LYS B C   
1859 O O   . LYS B 64  ? 0.1941 0.1916 0.1991 -0.0196 -0.0162 -0.0020 60  LYS B O   
1860 C CB  . LYS B 64  ? 0.1884 0.2155 0.2176 -0.0159 -0.0108 -0.0045 60  LYS B CB  
1861 C CG  . LYS B 64  ? 0.2094 0.2456 0.2435 -0.0147 -0.0055 -0.0058 60  LYS B CG  
1862 C CD  . LYS B 64  ? 0.2522 0.2985 0.2936 -0.0216 -0.0028 -0.0054 60  LYS B CD  
1863 C CE  . LYS B 64  ? 0.2925 0.3520 0.3433 -0.0195 0.0023  -0.0077 60  LYS B CE  
1864 N NZ  . LYS B 64  ? 0.3332 0.4067 0.3949 -0.0265 0.0048  -0.0081 60  LYS B NZ  
1865 N N   . ASN B 65  ? 0.1911 0.2047 0.2103 -0.0289 -0.0179 -0.0014 61  ASN B N   
1866 C CA  . ASN B 65  ? 0.1949 0.2012 0.2093 -0.0314 -0.0228 -0.0009 61  ASN B CA  
1867 C C   . ASN B 65  ? 0.2075 0.2144 0.2249 -0.0250 -0.0263 -0.0017 61  ASN B C   
1868 O O   . ASN B 65  ? 0.1993 0.2164 0.2272 -0.0204 -0.0268 -0.0024 61  ASN B O   
1869 C CB  . ASN B 65  ? 0.2243 0.2400 0.2465 -0.0385 -0.0263 -0.0006 61  ASN B CB  
1870 C CG  . ASN B 65  ? 0.2491 0.2630 0.2671 -0.0475 -0.0231 -0.0001 61  ASN B CG  
1871 O OD1 . ASN B 65  ? 0.2985 0.2971 0.3023 -0.0493 -0.0196 0.0007  61  ASN B OD1 
1872 N ND2 . ASN B 65  ? 0.2885 0.3176 0.3186 -0.0535 -0.0244 -0.0005 61  ASN B ND2 
1873 N N   . ILE B 66  ? 0.1988 0.1935 0.2060 -0.0251 -0.0281 -0.0016 62  ILE B N   
1874 C CA  . ILE B 66  ? 0.1891 0.1822 0.1966 -0.0217 -0.0315 -0.0020 62  ILE B CA  
1875 C C   . ILE B 66  ? 0.1986 0.1938 0.2077 -0.0264 -0.0373 -0.0009 62  ILE B C   
1876 O O   . ILE B 66  ? 0.2318 0.2202 0.2332 -0.0327 -0.0385 -0.0005 62  ILE B O   
1877 C CB  . ILE B 66  ? 0.1910 0.1710 0.1866 -0.0198 -0.0298 -0.0029 62  ILE B CB  
1878 C CG1 . ILE B 66  ? 0.2194 0.1988 0.2139 -0.0147 -0.0252 -0.0041 62  ILE B CG1 
1879 C CG2 . ILE B 66  ? 0.1875 0.1652 0.1821 -0.0181 -0.0326 -0.0033 62  ILE B CG2 
1880 C CD1 . ILE B 66  ? 0.2456 0.2141 0.2297 -0.0127 -0.0232 -0.0054 62  ILE B CD1 
1881 N N   . ASN B 67  ? 0.1844 0.1883 0.2028 -0.0234 -0.0414 -0.0005 63  ASN B N   
1882 C CA  . ASN B 67  ? 0.2044 0.2122 0.2253 -0.0271 -0.0482 0.0007  63  ASN B CA  
1883 C C   . ASN B 67  ? 0.1889 0.1847 0.1987 -0.0270 -0.0522 0.0014  63  ASN B C   
1884 O O   . ASN B 67  ? 0.2222 0.2145 0.2261 -0.0323 -0.0572 0.0023  63  ASN B O   
1885 C CB  . ASN B 67  ? 0.2031 0.2274 0.2404 -0.0230 -0.0512 0.0009  63  ASN B CB  
1886 C CG  . ASN B 67  ? 0.2398 0.2781 0.2887 -0.0247 -0.0472 -0.0001 63  ASN B CG  
1887 O OD1 . ASN B 67  ? 0.2647 0.3013 0.3095 -0.0317 -0.0446 -0.0002 63  ASN B OD1 
1888 N ND2 . ASN B 67  ? 0.2176 0.2682 0.2796 -0.0186 -0.0462 -0.0010 63  ASN B ND2 
1889 N N   . TYR B 68  ? 0.1930 0.1828 0.1994 -0.0218 -0.0501 0.0010  64  TYR B N   
1890 C CA  . TYR B 68  ? 0.1977 0.1758 0.1930 -0.0219 -0.0528 0.0016  64  TYR B CA  
1891 C C   . TYR B 68  ? 0.1996 0.1698 0.1888 -0.0192 -0.0467 -0.0002 64  TYR B C   
1892 O O   . TYR B 68  ? 0.1896 0.1651 0.1854 -0.0155 -0.0423 -0.0016 64  TYR B O   
1893 C CB  . TYR B 68  ? 0.2160 0.1971 0.2160 -0.0178 -0.0586 0.0034  64  TYR B CB  
1894 C CG  . TYR B 68  ? 0.2042 0.1962 0.2128 -0.0190 -0.0659 0.0050  64  TYR B CG  
1895 C CD1 . TYR B 68  ? 0.2132 0.2005 0.2134 -0.0242 -0.0723 0.0064  64  TYR B CD1 
1896 C CD2 . TYR B 68  ? 0.2269 0.2351 0.2524 -0.0149 -0.0664 0.0047  64  TYR B CD2 
1897 C CE1 . TYR B 68  ? 0.2772 0.2769 0.2866 -0.0256 -0.0798 0.0076  64  TYR B CE1 
1898 C CE2 . TYR B 68  ? 0.2292 0.2507 0.2651 -0.0157 -0.0731 0.0057  64  TYR B CE2 
1899 C CZ  . TYR B 68  ? 0.2384 0.2563 0.2667 -0.0212 -0.0802 0.0071  64  TYR B CZ  
1900 O OH  . TYR B 68  ? 0.2855 0.3184 0.3248 -0.0225 -0.0879 0.0078  64  TYR B OH  
1901 N N   . ILE B 69  ? 0.2139 0.1720 0.1904 -0.0215 -0.0465 -0.0004 65  ILE B N   
1902 C CA  . ILE B 69  ? 0.1951 0.1475 0.1669 -0.0195 -0.0413 -0.0024 65  ILE B CA  
1903 C C   . ILE B 69  ? 0.2230 0.1660 0.1858 -0.0206 -0.0439 -0.0012 65  ILE B C   
1904 O O   . ILE B 69  ? 0.2445 0.1807 0.1985 -0.0243 -0.0485 0.0006  65  ILE B O   
1905 C CB  . ILE B 69  ? 0.2257 0.1727 0.1905 -0.0210 -0.0359 -0.0048 65  ILE B CB  
1906 C CG1 . ILE B 69  ? 0.2985 0.2439 0.2618 -0.0188 -0.0307 -0.0074 65  ILE B CG1 
1907 C CG2 . ILE B 69  ? 0.2522 0.1887 0.2041 -0.0264 -0.0375 -0.0045 65  ILE B CG2 
1908 C CD1 . ILE B 69  ? 0.3736 0.3191 0.3356 -0.0172 -0.0252 -0.0102 65  ILE B CD1 
1909 N N   . MET B 70  ? 0.2435 0.1852 0.2074 -0.0180 -0.0412 -0.0021 66  MET B N   
1910 C CA  . MET B 70  ? 0.2500 0.1813 0.2049 -0.0190 -0.0433 -0.0006 66  MET B CA  
1911 C C   . MET B 70  ? 0.2528 0.1771 0.1998 -0.0215 -0.0366 -0.0034 66  MET B C   
1912 O O   . MET B 70  ? 0.2447 0.1759 0.1984 -0.0200 -0.0312 -0.0065 66  MET B O   
1913 C CB  . MET B 70  ? 0.3863 0.3205 0.3488 -0.0139 -0.0462 0.0007  66  MET B CB  
1914 C CG  . MET B 70  ? 0.5784 0.5180 0.5470 -0.0113 -0.0539 0.0037  66  MET B CG  
1915 S SD  . MET B 70  ? 0.6256 0.5796 0.6124 -0.0043 -0.0534 0.0027  66  MET B SD  
1916 C CE  . MET B 70  ? 0.3628 0.3277 0.3563 -0.0068 -0.0483 0.0003  66  MET B CE  
1917 N N   . LYS B 71  ? 0.2625 0.1738 0.1955 -0.0254 -0.0373 -0.0021 67  LYS B N   
1918 C CA  . LYS B 71  ? 0.2592 0.1633 0.1837 -0.0292 -0.0306 -0.0047 67  LYS B CA  
1919 C C   . LYS B 71  ? 0.2761 0.1660 0.1887 -0.0310 -0.0334 -0.0018 67  LYS B C   
1920 O O   . LYS B 71  ? 0.2995 0.1810 0.2032 -0.0315 -0.0401 0.0021  67  LYS B O   
1921 C CB  . LYS B 71  ? 0.2855 0.1853 0.2004 -0.0336 -0.0266 -0.0067 67  LYS B CB  
1922 C CG  . LYS B 71  ? 0.3022 0.1960 0.2086 -0.0384 -0.0189 -0.0098 67  LYS B CG  
1923 C CD  . LYS B 71  ? 0.3256 0.2142 0.2215 -0.0422 -0.0148 -0.0119 67  LYS B CD  
1924 C CE  . LYS B 71  ? 0.3395 0.2242 0.2279 -0.0473 -0.0061 -0.0155 67  LYS B CE  
1925 N NZ  . LYS B 71  ? 0.3976 0.2766 0.2751 -0.0505 -0.0018 -0.0179 67  LYS B NZ  
1926 N N   . HIS B 72  ? 0.2929 0.1799 0.2050 -0.0321 -0.0288 -0.0036 68  HIS B N   
1927 C CA  . HIS B 72  ? 0.3236 0.1937 0.2216 -0.0348 -0.0300 -0.0010 68  HIS B CA  
1928 C C   . HIS B 72  ? 0.3502 0.2161 0.2424 -0.0413 -0.0210 -0.0048 68  HIS B C   
1929 O O   . HIS B 72  ? 0.3742 0.2526 0.2783 -0.0410 -0.0156 -0.0092 68  HIS B O   
1930 C CB  . HIS B 72  ? 0.4314 0.2993 0.3347 -0.0291 -0.0345 0.0011  68  HIS B CB  
1931 C CG  . HIS B 72  ? 0.3974 0.2797 0.3171 -0.0216 -0.0398 0.0019  68  HIS B CG  
1932 N ND1 . HIS B 72  ? 0.4601 0.3429 0.3801 -0.0182 -0.0481 0.0058  68  HIS B ND1 
1933 C CD2 . HIS B 72  ? 0.4320 0.3287 0.3678 -0.0173 -0.0378 -0.0008 68  HIS B CD2 
1934 C CE1 . HIS B 72  ? 0.4312 0.3293 0.3679 -0.0125 -0.0503 0.0053  68  HIS B CE1 
1935 N NE2 . HIS B 72  ? 0.4294 0.3351 0.3749 -0.0118 -0.0439 0.0015  68  HIS B NE2 
1936 N N   . THR B 73  ? 0.3706 0.2191 0.2440 -0.0475 -0.0194 -0.0032 69  THR B N   
1937 C CA  . THR B 73  ? 0.3908 0.2339 0.2578 -0.0548 -0.0108 -0.0066 69  THR B CA  
1938 C C   . THR B 73  ? 0.4367 0.2663 0.2977 -0.0544 -0.0129 -0.0043 69  THR B C   
1939 O O   . THR B 73  ? 0.4747 0.2874 0.3223 -0.0526 -0.0195 0.0011  69  THR B O   
1940 C CB  . THR B 73  ? 0.4233 0.2539 0.2715 -0.0631 -0.0061 -0.0066 69  THR B CB  
1941 O OG1 . THR B 73  ? 0.4154 0.2567 0.2682 -0.0623 -0.0047 -0.0087 69  THR B OG1 
1942 C CG2 . THR B 73  ? 0.4149 0.2440 0.2594 -0.0716 0.0042  -0.0111 69  THR B CG2 
1943 N N   . VAL B 74  ? 0.4327 0.2692 0.3030 -0.0558 -0.0078 -0.0084 70  VAL B N   
1944 C CA  . VAL B 74  ? 0.4404 0.2654 0.3074 -0.0544 -0.0095 -0.0073 70  VAL B CA  
1945 C C   . VAL B 74  ? 0.4161 0.2353 0.2765 -0.0645 -0.0005 -0.0115 70  VAL B C   
1946 O O   . VAL B 74  ? 0.4158 0.2473 0.2812 -0.0708 0.0068  -0.0164 70  VAL B O   
1947 C CB  . VAL B 74  ? 0.3938 0.2335 0.2800 -0.0454 -0.0132 -0.0086 70  VAL B CB  
1948 C CG1 . VAL B 74  ? 0.4070 0.2559 0.3017 -0.0369 -0.0208 -0.0052 70  VAL B CG1 
1949 C CG2 . VAL B 74  ? 0.3786 0.2386 0.2805 -0.0476 -0.0067 -0.0152 70  VAL B CG2 
1950 N N   . LYS B 75  ? 0.4415 0.2414 0.2902 -0.0663 -0.0011 -0.0098 71  LYS B N   
1951 C CA  . LYS B 75  ? 0.4374 0.2323 0.2819 -0.0760 0.0069  -0.0144 71  LYS B CA  
1952 C C   . LYS B 75  ? 0.4576 0.2526 0.3104 -0.0705 0.0044  -0.0158 71  LYS B C   
1953 O O   . LYS B 75  ? 0.4957 0.2694 0.3364 -0.0671 0.0002  -0.0119 71  LYS B O   
1954 C CB  . LYS B 75  ? 0.4900 0.2564 0.3078 -0.0853 0.0100  -0.0113 71  LYS B CB  
1955 C CG  . LYS B 75  ? 0.6118 0.3739 0.4174 -0.0896 0.0114  -0.0089 71  LYS B CG  
1956 C CD  . LYS B 75  ? 0.7430 0.4724 0.5200 -0.0922 0.0081  -0.0021 71  LYS B CD  
1957 C CE  . LYS B 75  ? 0.7933 0.5163 0.5543 -0.1008 0.0129  -0.0013 71  LYS B CE  
1958 N NZ  . LYS B 75  ? 0.8504 0.5645 0.5963 -0.1118 0.0224  -0.0032 71  LYS B NZ  
1959 N N   . LYS B 76  ? 0.3714 0.1893 0.2435 -0.0696 0.0070  -0.0215 72  LYS B N   
1960 C CA  . LYS B 76  ? 0.3994 0.2206 0.2811 -0.0629 0.0040  -0.0231 72  LYS B CA  
1961 C C   . LYS B 76  ? 0.3732 0.2114 0.2669 -0.0688 0.0099  -0.0306 72  LYS B C   
1962 O O   . LYS B 76  ? 0.3525 0.2080 0.2541 -0.0742 0.0146  -0.0345 72  LYS B O   
1963 C CB  . LYS B 76  ? 0.3983 0.2339 0.2946 -0.0502 -0.0030 -0.0206 72  LYS B CB  
1964 C CG  . LYS B 76  ? 0.4532 0.2741 0.3408 -0.0426 -0.0106 -0.0136 72  LYS B CG  
1965 C CD  . LYS B 76  ? 0.4419 0.2786 0.3458 -0.0312 -0.0166 -0.0123 72  LYS B CD  
1966 C CE  . LYS B 76  ? 0.4991 0.3260 0.3969 -0.0242 -0.0247 -0.0058 72  LYS B CE  
1967 N NZ  . LYS B 76  ? 0.6623 0.4714 0.5528 -0.0180 -0.0286 -0.0033 72  LYS B NZ  
1968 N N   . ARG B 77  ? 0.3689 0.2023 0.2638 -0.0674 0.0094  -0.0330 73  ARG B N   
1969 C CA  . ARG B 77  ? 0.3323 0.1831 0.2395 -0.0715 0.0131  -0.0402 73  ARG B CA  
1970 C C   . ARG B 77  ? 0.3292 0.2066 0.2560 -0.0629 0.0100  -0.0413 73  ARG B C   
1971 O O   . ARG B 77  ? 0.3508 0.2295 0.2822 -0.0524 0.0046  -0.0375 73  ARG B O   
1972 C CB  . ARG B 77  ? 0.3714 0.2082 0.2731 -0.0710 0.0126  -0.0422 73  ARG B CB  
1973 C CG  . ARG B 77  ? 0.3721 0.2236 0.2829 -0.0775 0.0163  -0.0501 73  ARG B CG  
1974 C CD  . ARG B 77  ? 0.4266 0.2579 0.3266 -0.0798 0.0170  -0.0525 73  ARG B CD  
1975 N NE  . ARG B 77  ? 0.4659 0.2688 0.3448 -0.0888 0.0205  -0.0506 73  ARG B NE  
1976 C CZ  . ARG B 77  ? 0.4775 0.2823 0.3522 -0.1017 0.0267  -0.0535 73  ARG B CZ  
1977 N NH1 . ARG B 77  ? 0.4678 0.2988 0.3570 -0.1086 0.0301  -0.0599 73  ARG B NH1 
1978 N NH2 . ARG B 77  ? 0.5415 0.3245 0.3982 -0.1064 0.0293  -0.0493 73  ARG B NH2 
1979 N N   . MET B 78  ? 0.3012 0.1999 0.2394 -0.0675 0.0136  -0.0466 74  MET B N   
1980 C CA  . MET B 78  ? 0.2728 0.1950 0.2275 -0.0599 0.0110  -0.0476 74  MET B CA  
1981 C C   . MET B 78  ? 0.2620 0.1978 0.2263 -0.0603 0.0111  -0.0534 74  MET B C   
1982 O O   . MET B 78  ? 0.2856 0.2209 0.2476 -0.0696 0.0150  -0.0585 74  MET B O   
1983 C CB  . MET B 78  ? 0.2789 0.2156 0.2391 -0.0628 0.0141  -0.0489 74  MET B CB  
1984 C CG  . MET B 78  ? 0.3149 0.2377 0.2636 -0.0640 0.0146  -0.0439 74  MET B CG  
1985 S SD  . MET B 78  ? 0.3116 0.2261 0.2581 -0.0525 0.0069  -0.0363 74  MET B SD  
1986 C CE  . MET B 78  ? 0.2936 0.2330 0.2575 -0.0447 0.0050  -0.0378 74  MET B CE  
1987 N N   . PHE B 79  ? 0.2400 0.1874 0.2141 -0.0510 0.0070  -0.0528 75  PHE B N   
1988 C CA  . PHE B 79  ? 0.2485 0.2093 0.2306 -0.0506 0.0064  -0.0580 75  PHE B CA  
1989 C C   . PHE B 79  ? 0.2421 0.2251 0.2371 -0.0446 0.0043  -0.0586 75  PHE B C   
1990 O O   . PHE B 79  ? 0.2607 0.2450 0.2579 -0.0372 0.0018  -0.0540 75  PHE B O   
1991 C CB  . PHE B 79  ? 0.2641 0.2147 0.2428 -0.0449 0.0038  -0.0573 75  PHE B CB  
1992 C CG  . PHE B 79  ? 0.3002 0.2291 0.2662 -0.0506 0.0059  -0.0586 75  PHE B CG  
1993 C CD1 . PHE B 79  ? 0.3386 0.2677 0.3026 -0.0580 0.0082  -0.0649 75  PHE B CD1 
1994 C CD2 . PHE B 79  ? 0.3437 0.2512 0.2988 -0.0485 0.0052  -0.0534 75  PHE B CD2 
1995 C CE1 . PHE B 79  ? 0.3870 0.2932 0.3373 -0.0636 0.0105  -0.0663 75  PHE B CE1 
1996 C CE2 . PHE B 79  ? 0.3962 0.2807 0.3376 -0.0530 0.0070  -0.0543 75  PHE B CE2 
1997 C CZ  . PHE B 79  ? 0.4026 0.2856 0.3411 -0.0607 0.0100  -0.0607 75  PHE B CZ  
1998 N N   . LYS B 80  ? 0.2436 0.2434 0.2463 -0.0478 0.0049  -0.0643 76  LYS B N   
1999 C CA  . LYS B 80  ? 0.2428 0.2626 0.2564 -0.0413 0.0020  -0.0652 76  LYS B CA  
2000 C C   . LYS B 80  ? 0.2358 0.2585 0.2505 -0.0368 -0.0014 -0.0666 76  LYS B C   
2001 O O   . LYS B 80  ? 0.2576 0.2784 0.2696 -0.0422 -0.0008 -0.0712 76  LYS B O   
2002 C CB  . LYS B 80  ? 0.2653 0.3039 0.2877 -0.0466 0.0041  -0.0708 76  LYS B CB  
2003 C CG  . LYS B 80  ? 0.3009 0.3596 0.3340 -0.0390 0.0006  -0.0717 76  LYS B CG  
2004 C CD  . LYS B 80  ? 0.3874 0.4671 0.4307 -0.0441 0.0019  -0.0785 76  LYS B CD  
2005 C CE  . LYS B 80  ? 0.4135 0.4958 0.4590 -0.0490 0.0073  -0.0794 76  LYS B CE  
2006 N NZ  . LYS B 80  ? 0.4965 0.6038 0.5554 -0.0523 0.0085  -0.0863 76  LYS B NZ  
2007 N N   . ILE B 81  ? 0.2061 0.2321 0.2232 -0.0276 -0.0045 -0.0628 77  ILE B N   
2008 C CA  . ILE B 81  ? 0.2082 0.2383 0.2255 -0.0229 -0.0074 -0.0639 77  ILE B CA  
2009 C C   . ILE B 81  ? 0.1837 0.2327 0.2085 -0.0194 -0.0101 -0.0657 77  ILE B C   
2010 O O   . ILE B 81  ? 0.1958 0.2492 0.2238 -0.0143 -0.0110 -0.0622 77  ILE B O   
2011 C CB  . ILE B 81  ? 0.2464 0.2674 0.2608 -0.0154 -0.0085 -0.0584 77  ILE B CB  
2012 C CG1 . ILE B 81  ? 0.3721 0.3762 0.3812 -0.0164 -0.0068 -0.0548 77  ILE B CG1 
2013 C CG2 . ILE B 81  ? 0.2726 0.2953 0.2852 -0.0119 -0.0099 -0.0600 77  ILE B CG2 
2014 C CD1 . ILE B 81  ? 0.4030 0.3944 0.4054 -0.0223 -0.0047 -0.0578 77  ILE B CD1 
2015 N N   . LYS B 82  ? 0.1966 0.2557 0.2232 -0.0217 -0.0120 -0.0709 78  LYS B N   
2016 C CA  . LYS B 82  ? 0.2078 0.2856 0.2413 -0.0179 -0.0158 -0.0729 78  LYS B CA  
2017 C C   . LYS B 82  ? 0.1799 0.2583 0.2087 -0.0124 -0.0195 -0.0725 78  LYS B C   
2018 O O   . LYS B 82  ? 0.2205 0.2928 0.2436 -0.0159 -0.0193 -0.0753 78  LYS B O   
2019 C CB  . LYS B 82  ? 0.2310 0.3231 0.2708 -0.0256 -0.0158 -0.0800 78  LYS B CB  
2020 C CG  . LYS B 82  ? 0.2520 0.3440 0.2955 -0.0327 -0.0110 -0.0813 78  LYS B CG  
2021 C CD  . LYS B 82  ? 0.3156 0.4226 0.3657 -0.0421 -0.0103 -0.0891 78  LYS B CD  
2022 C CE  . LYS B 82  ? 0.4222 0.5537 0.4831 -0.0369 -0.0157 -0.0923 78  LYS B CE  
2023 N NZ  . LYS B 82  ? 0.4332 0.5831 0.5029 -0.0464 -0.0155 -0.1005 78  LYS B NZ  
2024 N N   . ALA B 83  ? 0.1789 0.2627 0.2084 -0.0042 -0.0226 -0.0690 79  ALA B N   
2025 C CA  . ALA B 83  ? 0.1911 0.2745 0.2142 0.0006  -0.0258 -0.0681 79  ALA B CA  
2026 C C   . ALA B 83  ? 0.1913 0.2841 0.2158 0.0086  -0.0302 -0.0656 79  ALA B C   
2027 O O   . ALA B 83  ? 0.1963 0.2868 0.2228 0.0128  -0.0293 -0.0614 79  ALA B O   
2028 C CB  . ALA B 83  ? 0.2462 0.3137 0.2622 0.0026  -0.0228 -0.0637 79  ALA B CB  
2029 N N   . GLY B 84  ? 0.1995 0.3015 0.2216 0.0108  -0.0352 -0.0683 80  GLY B N   
2030 C CA  . GLY B 84  ? 0.2086 0.3164 0.2292 0.0195  -0.0401 -0.0653 80  GLY B CA  
2031 C C   . GLY B 84  ? 0.2044 0.3235 0.2353 0.0232  -0.0413 -0.0655 80  GLY B C   
2032 O O   . GLY B 84  ? 0.2368 0.3540 0.2652 0.0314  -0.0434 -0.0612 80  GLY B O   
2033 N N   . GLY B 85  ? 0.1703 0.2999 0.2118 0.0171  -0.0394 -0.0705 81  GLY B N   
2034 C CA  . GLY B 85  ? 0.1702 0.3115 0.2225 0.0201  -0.0391 -0.0715 81  GLY B CA  
2035 C C   . GLY B 85  ? 0.1843 0.3137 0.2363 0.0203  -0.0335 -0.0674 81  GLY B C   
2036 O O   . GLY B 85  ? 0.2058 0.3428 0.2652 0.0233  -0.0324 -0.0682 81  GLY B O   
2037 N N   . LYS B 86  ? 0.1770 0.2887 0.2207 0.0174  -0.0300 -0.0634 82  LYS B N   
2038 C CA  . LYS B 86  ? 0.1970 0.2967 0.2394 0.0161  -0.0252 -0.0597 82  LYS B CA  
2039 C C   . LYS B 86  ? 0.1613 0.2550 0.2040 0.0066  -0.0209 -0.0618 82  LYS B C   
2040 O O   . LYS B 86  ? 0.1690 0.2634 0.2105 0.0015  -0.0212 -0.0652 82  LYS B O   
2041 C CB  . LYS B 86  ? 0.2415 0.3259 0.2744 0.0204  -0.0252 -0.0533 82  LYS B CB  
2042 C CG  . LYS B 86  ? 0.2995 0.3848 0.3282 0.0294  -0.0292 -0.0503 82  LYS B CG  
2043 C CD  . LYS B 86  ? 0.3412 0.4299 0.3741 0.0343  -0.0289 -0.0498 82  LYS B CD  
2044 C CE  . LYS B 86  ? 0.4462 0.5326 0.4728 0.0440  -0.0331 -0.0466 82  LYS B CE  
2045 N NZ  . LYS B 86  ? 0.5458 0.6305 0.5741 0.0494  -0.0318 -0.0455 82  LYS B NZ  
2046 N N   . GLU B 87  ? 0.1809 0.2663 0.2231 0.0041  -0.0169 -0.0596 83  GLU B N   
2047 C CA  . GLU B 87  ? 0.2083 0.2841 0.2479 -0.0042 -0.0131 -0.0605 83  GLU B CA  
2048 C C   . GLU B 87  ? 0.1936 0.2549 0.2280 -0.0037 -0.0108 -0.0552 83  GLU B C   
2049 O O   . GLU B 87  ? 0.2160 0.2772 0.2506 0.0007  -0.0109 -0.0525 83  GLU B O   
2050 C CB  . GLU B 87  ? 0.2214 0.3066 0.2669 -0.0120 -0.0102 -0.0662 83  GLU B CB  
2051 C CG  . GLU B 87  ? 0.3107 0.4033 0.3618 -0.0109 -0.0077 -0.0668 83  GLU B CG  
2052 C CD  . GLU B 87  ? 0.3596 0.4644 0.4179 -0.0193 -0.0040 -0.0732 83  GLU B CD  
2053 O OE1 . GLU B 87  ? 0.3402 0.4596 0.4050 -0.0218 -0.0061 -0.0784 83  GLU B OE1 
2054 O OE2 . GLU B 87  ? 0.4115 0.5111 0.4681 -0.0243 0.0011  -0.0732 83  GLU B OE2 
2055 N N   . VAL B 88  ? 0.1758 0.2241 0.2049 -0.0080 -0.0093 -0.0537 84  VAL B N   
2056 C CA  . VAL B 88  ? 0.1788 0.2138 0.2028 -0.0085 -0.0079 -0.0491 84  VAL B CA  
2057 C C   . VAL B 88  ? 0.1802 0.2055 0.1998 -0.0162 -0.0050 -0.0504 84  VAL B C   
2058 O O   . VAL B 88  ? 0.1999 0.2232 0.2182 -0.0197 -0.0047 -0.0533 84  VAL B O   
2059 C CB  . VAL B 88  ? 0.1957 0.2230 0.2165 -0.0033 -0.0101 -0.0442 84  VAL B CB  
2060 C CG1 . VAL B 88  ? 0.1993 0.2218 0.2181 -0.0039 -0.0105 -0.0451 84  VAL B CG1 
2061 C CG2 . VAL B 88  ? 0.1968 0.2135 0.2137 -0.0034 -0.0098 -0.0394 84  VAL B CG2 
2062 N N   . ILE B 89  ? 0.1997 0.2177 0.2155 -0.0192 -0.0028 -0.0485 85  ILE B N   
2063 C CA  . ILE B 89  ? 0.2164 0.2224 0.2252 -0.0267 0.0000  -0.0490 85  ILE B CA  
2064 C C   . ILE B 89  ? 0.1905 0.1799 0.1913 -0.0248 -0.0019 -0.0432 85  ILE B C   
2065 O O   . ILE B 89  ? 0.1924 0.1796 0.1917 -0.0220 -0.0029 -0.0396 85  ILE B O   
2066 C CB  . ILE B 89  ? 0.2084 0.2190 0.2175 -0.0330 0.0045  -0.0519 85  ILE B CB  
2067 C CG1 . ILE B 89  ? 0.2196 0.2503 0.2393 -0.0341 0.0057  -0.0581 85  ILE B CG1 
2068 C CG2 . ILE B 89  ? 0.2340 0.2295 0.2331 -0.0419 0.0079  -0.0521 85  ILE B CG2 
2069 C CD1 . ILE B 89  ? 0.2483 0.2881 0.2716 -0.0389 0.0106  -0.0617 85  ILE B CD1 
2070 N N   . VAL B 90  ? 0.2098 0.1875 0.2055 -0.0259 -0.0026 -0.0426 86  VAL B N   
2071 C CA  . VAL B 90  ? 0.2084 0.1720 0.1981 -0.0225 -0.0054 -0.0374 86  VAL B CA  
2072 C C   . VAL B 90  ? 0.2394 0.1853 0.2180 -0.0280 -0.0040 -0.0370 86  VAL B C   
2073 O O   . VAL B 90  ? 0.2367 0.1803 0.2125 -0.0344 -0.0007 -0.0412 86  VAL B O   
2074 C CB  . VAL B 90  ? 0.2450 0.2109 0.2394 -0.0154 -0.0083 -0.0365 86  VAL B CB  
2075 C CG1 . VAL B 90  ? 0.2944 0.2759 0.2974 -0.0110 -0.0092 -0.0369 86  VAL B CG1 
2076 C CG2 . VAL B 90  ? 0.2561 0.2176 0.2487 -0.0171 -0.0069 -0.0403 86  VAL B CG2 
2077 N N   . THR B 91  ? 0.2349 0.1673 0.2063 -0.0257 -0.0068 -0.0320 87  THR B N   
2078 C CA  . THR B 91  ? 0.2788 0.1911 0.2376 -0.0293 -0.0064 -0.0308 87  THR B CA  
2079 C C   . THR B 91  ? 0.2697 0.1763 0.2290 -0.0258 -0.0071 -0.0325 87  THR B C   
2080 O O   . THR B 91  ? 0.2573 0.1738 0.2259 -0.0190 -0.0091 -0.0330 87  THR B O   
2081 C CB  . THR B 91  ? 0.2965 0.1956 0.2468 -0.0266 -0.0105 -0.0246 87  THR B CB  
2082 O OG1 . THR B 91  ? 0.2862 0.1908 0.2444 -0.0173 -0.0157 -0.0217 87  THR B OG1 
2083 C CG2 . THR B 91  ? 0.2888 0.1916 0.2364 -0.0306 -0.0093 -0.0234 87  THR B CG2 
2084 N N   . ALA B 92  ? 0.3011 0.1896 0.2486 -0.0307 -0.0052 -0.0334 88  ALA B N   
2085 C CA  . ALA B 92  ? 0.3070 0.1873 0.2527 -0.0281 -0.0050 -0.0359 88  ALA B CA  
2086 C C   . ALA B 92  ? 0.3004 0.1775 0.2494 -0.0167 -0.0098 -0.0322 88  ALA B C   
2087 O O   . ALA B 92  ? 0.3406 0.2181 0.2931 -0.0120 -0.0096 -0.0349 88  ALA B O   
2088 C CB  . ALA B 92  ? 0.3624 0.2196 0.2919 -0.0358 -0.0021 -0.0369 88  ALA B CB  
2089 N N   . ASP B 93  ? 0.3316 0.2053 0.2792 -0.0124 -0.0140 -0.0266 89  ASP B N   
2090 C CA  . ASP B 93  ? 0.3847 0.2580 0.3371 -0.0017 -0.0191 -0.0230 89  ASP B CA  
2091 C C   . ASP B 93  ? 0.3526 0.2483 0.3207 0.0034  -0.0208 -0.0225 89  ASP B C   
2092 O O   . ASP B 93  ? 0.3429 0.2419 0.3171 0.0113  -0.0248 -0.0197 89  ASP B O   
2093 C CB  . ASP B 93  ? 0.4091 0.2650 0.3504 0.0007  -0.0239 -0.0171 89  ASP B CB  
2094 C CG  . ASP B 93  ? 0.4594 0.3156 0.3949 -0.0058 -0.0245 -0.0142 89  ASP B CG  
2095 O OD1 . ASP B 93  ? 0.3819 0.2517 0.3227 -0.0117 -0.0208 -0.0168 89  ASP B OD1 
2096 O OD2 . ASP B 93  ? 0.5012 0.3434 0.4263 -0.0043 -0.0289 -0.0092 89  ASP B OD2 
2097 N N   . HIS B 94  ? 0.2782 0.1889 0.2524 -0.0011 -0.0180 -0.0250 90  HIS B N   
2098 C CA  . HIS B 94  ? 0.2794 0.2085 0.2657 0.0027  -0.0192 -0.0244 90  HIS B CA  
2099 C C   . HIS B 94  ? 0.2754 0.2145 0.2691 0.0054  -0.0166 -0.0286 90  HIS B C   
2100 O O   . HIS B 94  ? 0.3679 0.3055 0.3586 0.0014  -0.0134 -0.0330 90  HIS B O   
2101 C CB  . HIS B 94  ? 0.2796 0.2174 0.2668 -0.0026 -0.0180 -0.0243 90  HIS B CB  
2102 C CG  . HIS B 94  ? 0.2671 0.2185 0.2631 0.0010  -0.0198 -0.0224 90  HIS B CG  
2103 N ND1 . HIS B 94  ? 0.3313 0.2821 0.3286 0.0041  -0.0241 -0.0180 90  HIS B ND1 
2104 C CD2 . HIS B 94  ? 0.3300 0.2950 0.3331 0.0018  -0.0182 -0.0242 90  HIS B CD2 
2105 C CE1 . HIS B 94  ? 0.3947 0.3579 0.3995 0.0056  -0.0243 -0.0175 90  HIS B CE1 
2106 N NE2 . HIS B 94  ? 0.3755 0.3463 0.3830 0.0045  -0.0208 -0.0209 90  HIS B NE2 
2107 N N   . SER B 95  ? 0.2909 0.2405 0.2938 0.0115  -0.0179 -0.0275 91  SER B N   
2108 C CA  . SER B 95  ? 0.3045 0.2623 0.3126 0.0143  -0.0152 -0.0312 91  SER B CA  
2109 C C   . SER B 95  ? 0.2485 0.2200 0.2604 0.0116  -0.0137 -0.0326 91  SER B C   
2110 O O   . SER B 95  ? 0.2602 0.2383 0.2748 0.0109  -0.0151 -0.0297 91  SER B O   
2111 C CB  . SER B 95  ? 0.3292 0.2916 0.3450 0.0220  -0.0163 -0.0297 91  SER B CB  
2112 O OG  . SER B 95  ? 0.4208 0.3700 0.4331 0.0263  -0.0179 -0.0291 91  SER B OG  
2113 N N   . VAL B 96  ? 0.2663 0.2410 0.2773 0.0104  -0.0111 -0.0371 92  VAL B N   
2114 C CA  . VAL B 96  ? 0.2389 0.2259 0.2526 0.0097  -0.0102 -0.0388 92  VAL B CA  
2115 C C   . VAL B 96  ? 0.2191 0.2108 0.2358 0.0146  -0.0087 -0.0396 92  VAL B C   
2116 O O   . VAL B 96  ? 0.2556 0.2411 0.2716 0.0175  -0.0074 -0.0413 92  VAL B O   
2117 C CB  . VAL B 96  ? 0.2767 0.2641 0.2863 0.0046  -0.0090 -0.0437 92  VAL B CB  
2118 C CG1 . VAL B 96  ? 0.2815 0.2814 0.2931 0.0049  -0.0091 -0.0456 92  VAL B CG1 
2119 C CG2 . VAL B 96  ? 0.3224 0.3061 0.3295 -0.0010 -0.0092 -0.0433 92  VAL B CG2 
2120 N N   . MET B 97  ? 0.1777 0.1793 0.1969 0.0157  -0.0085 -0.0385 93  MET B N   
2121 C CA  . MET B 97  ? 0.1747 0.1810 0.1954 0.0192  -0.0061 -0.0396 93  MET B CA  
2122 C C   . MET B 97  ? 0.1952 0.2019 0.2101 0.0179  -0.0045 -0.0445 93  MET B C   
2123 O O   . MET B 97  ? 0.2176 0.2274 0.2295 0.0148  -0.0061 -0.0459 93  MET B O   
2124 C CB  . MET B 97  ? 0.1957 0.2101 0.2190 0.0200  -0.0061 -0.0361 93  MET B CB  
2125 C CG  . MET B 97  ? 0.1823 0.1971 0.2107 0.0199  -0.0082 -0.0314 93  MET B CG  
2126 S SD  . MET B 97  ? 0.1919 0.2041 0.2271 0.0238  -0.0086 -0.0306 93  MET B SD  
2127 C CE  . MET B 97  ? 0.1855 0.2068 0.2257 0.0272  -0.0040 -0.0322 93  MET B CE  
2128 N N   . VAL B 98  ? 0.2044 0.2088 0.2179 0.0206  -0.0015 -0.0475 94  VAL B N   
2129 C CA  . VAL B 98  ? 0.1913 0.1959 0.1978 0.0192  0.0000  -0.0524 94  VAL B CA  
2130 C C   . VAL B 98  ? 0.2165 0.2242 0.2225 0.0229  0.0039  -0.0531 94  VAL B C   
2131 O O   . VAL B 98  ? 0.2187 0.2269 0.2310 0.0268  0.0062  -0.0515 94  VAL B O   
2132 C CB  . VAL B 98  ? 0.2258 0.2202 0.2271 0.0169  0.0006  -0.0574 94  VAL B CB  
2133 C CG1 . VAL B 98  ? 0.2429 0.2352 0.2437 0.0116  -0.0023 -0.0574 94  VAL B CG1 
2134 C CG2 . VAL B 98  ? 0.2659 0.2507 0.2687 0.0213  0.0031  -0.0579 94  VAL B CG2 
2135 N N   . LYS B 99  ? 0.2063 0.2167 0.2049 0.0217  0.0048  -0.0559 95  LYS B N   
2136 C CA  . LYS B 99  ? 0.2222 0.2327 0.2168 0.0241  0.0097  -0.0585 95  LYS B CA  
2137 C C   . LYS B 99  ? 0.2465 0.2477 0.2357 0.0241  0.0116  -0.0646 95  LYS B C   
2138 O O   . LYS B 99  ? 0.2468 0.2449 0.2294 0.0199  0.0091  -0.0681 95  LYS B O   
2139 C CB  . LYS B 99  ? 0.2619 0.2774 0.2480 0.0227  0.0096  -0.0582 95  LYS B CB  
2140 C CG  . LYS B 99  ? 0.3115 0.3265 0.2920 0.0246  0.0158  -0.0609 95  LYS B CG  
2141 C CD  . LYS B 99  ? 0.4423 0.4609 0.4133 0.0232  0.0160  -0.0591 95  LYS B CD  
2142 C CE  . LYS B 99  ? 0.5052 0.5214 0.4638 0.0208  0.0123  -0.0628 95  LYS B CE  
2143 N NZ  . LYS B 99  ? 0.5067 0.5225 0.4514 0.0203  0.0144  -0.0631 95  LYS B NZ  
2144 N N   . ARG B 100 ? 0.2311 0.2281 0.2238 0.0286  0.0160  -0.0662 96  ARG B N   
2145 C CA  . ARG B 100 ? 0.2271 0.2127 0.2136 0.0298  0.0188  -0.0722 96  ARG B CA  
2146 C C   . ARG B 100 ? 0.2386 0.2255 0.2251 0.0350  0.0255  -0.0749 96  ARG B C   
2147 O O   . ARG B 100 ? 0.2353 0.2287 0.2323 0.0398  0.0279  -0.0720 96  ARG B O   
2148 C CB  . ARG B 100 ? 0.2681 0.2435 0.2588 0.0316  0.0171  -0.0714 96  ARG B CB  
2149 C CG  . ARG B 100 ? 0.2750 0.2356 0.2588 0.0342  0.0207  -0.0773 96  ARG B CG  
2150 C CD  . ARG B 100 ? 0.3012 0.2486 0.2865 0.0363  0.0187  -0.0760 96  ARG B CD  
2151 N NE  . ARG B 100 ? 0.3021 0.2454 0.2842 0.0289  0.0141  -0.0744 96  ARG B NE  
2152 C CZ  . ARG B 100 ? 0.3441 0.2756 0.3255 0.0288  0.0118  -0.0722 96  ARG B CZ  
2153 N NH1 . ARG B 100 ? 0.3637 0.2861 0.3475 0.0367  0.0128  -0.0710 96  ARG B NH1 
2154 N NH2 . ARG B 100 ? 0.3574 0.2866 0.3355 0.0210  0.0087  -0.0712 96  ARG B NH2 
2155 N N   . ASP B 101 ? 0.2460 0.2278 0.2208 0.0336  0.0289  -0.0808 97  ASP B N   
2156 C CA  . ASP B 101 ? 0.2584 0.2402 0.2315 0.0384  0.0365  -0.0846 97  ASP B CA  
2157 C C   . ASP B 101 ? 0.2460 0.2419 0.2262 0.0399  0.0396  -0.0804 97  ASP B C   
2158 O O   . ASP B 101 ? 0.2682 0.2689 0.2562 0.0452  0.0456  -0.0813 97  ASP B O   
2159 C CB  . ASP B 101 ? 0.3044 0.2770 0.2829 0.0453  0.0397  -0.0873 97  ASP B CB  
2160 C CG  . ASP B 101 ? 0.4386 0.3936 0.4069 0.0432  0.0379  -0.0920 97  ASP B CG  
2161 O OD1 . ASP B 101 ? 0.4387 0.3895 0.3945 0.0364  0.0364  -0.0956 97  ASP B OD1 
2162 O OD2 . ASP B 101 ? 0.4662 0.4111 0.4385 0.0481  0.0378  -0.0922 97  ASP B OD2 
2163 N N   . GLY B 102 ? 0.2763 0.2789 0.2533 0.0350  0.0359  -0.0763 98  GLY B N   
2164 C CA  . GLY B 102 ? 0.3238 0.3369 0.3037 0.0345  0.0389  -0.0723 98  GLY B CA  
2165 C C   . GLY B 102 ? 0.2752 0.2970 0.2705 0.0359  0.0371  -0.0663 98  GLY B C   
2166 O O   . GLY B 102 ? 0.3081 0.3383 0.3059 0.0346  0.0401  -0.0632 98  GLY B O   
2167 N N   . LYS B 103 ? 0.2397 0.2588 0.2439 0.0379  0.0325  -0.0647 99  LYS B N   
2168 C CA  . LYS B 103 ? 0.2322 0.2591 0.2503 0.0392  0.0302  -0.0594 99  LYS B CA  
2169 C C   . LYS B 103 ? 0.2184 0.2416 0.2364 0.0360  0.0226  -0.0556 99  LYS B C   
2170 O O   . LYS B 103 ? 0.2328 0.2471 0.2448 0.0348  0.0196  -0.0578 99  LYS B O   
2171 C CB  . LYS B 103 ? 0.2456 0.2733 0.2757 0.0460  0.0321  -0.0609 99  LYS B CB  
2172 C CG  . LYS B 103 ? 0.3082 0.3416 0.3414 0.0504  0.0406  -0.0654 99  LYS B CG  
2173 C CD  . LYS B 103 ? 0.3433 0.3916 0.3833 0.0478  0.0444  -0.0625 99  LYS B CD  
2174 C CE  . LYS B 103 ? 0.4635 0.5209 0.5101 0.0520  0.0536  -0.0668 99  LYS B CE  
2175 N NZ  . LYS B 103 ? 0.4710 0.5266 0.5037 0.0486  0.0609  -0.0704 99  LYS B NZ  
2176 N N   . ILE B 104 ? 0.2067 0.2366 0.2313 0.0343  0.0200  -0.0502 100 ILE B N   
2177 C CA  . ILE B 104 ? 0.2212 0.2481 0.2465 0.0318  0.0136  -0.0466 100 ILE B CA  
2178 C C   . ILE B 104 ? 0.2331 0.2586 0.2683 0.0351  0.0113  -0.0452 100 ILE B C   
2179 O O   . ILE B 104 ? 0.2277 0.2609 0.2729 0.0376  0.0124  -0.0432 100 ILE B O   
2180 C CB  . ILE B 104 ? 0.2448 0.2772 0.2694 0.0282  0.0120  -0.0418 100 ILE B CB  
2181 C CG1 . ILE B 104 ? 0.3169 0.3483 0.3294 0.0258  0.0131  -0.0429 100 ILE B CG1 
2182 C CG2 . ILE B 104 ? 0.2777 0.3072 0.3039 0.0262  0.0062  -0.0386 100 ILE B CG2 
2183 C CD1 . ILE B 104 ? 0.3614 0.3955 0.3707 0.0231  0.0124  -0.0382 100 ILE B CD1 
2184 N N   . ILE B 105 ? 0.2097 0.2251 0.2414 0.0351  0.0081  -0.0463 101 ILE B N   
2185 C CA  . ILE B 105 ? 0.2227 0.2324 0.2599 0.0387  0.0056  -0.0451 101 ILE B CA  
2186 C C   . ILE B 105 ? 0.2019 0.2040 0.2347 0.0345  0.0006  -0.0428 101 ILE B C   
2187 O O   . ILE B 105 ? 0.2114 0.2131 0.2381 0.0295  -0.0002 -0.0433 101 ILE B O   
2188 C CB  . ILE B 105 ? 0.2254 0.2258 0.2600 0.0436  0.0085  -0.0499 101 ILE B CB  
2189 C CG1 . ILE B 105 ? 0.2432 0.2329 0.2653 0.0394  0.0091  -0.0543 101 ILE B CG1 
2190 C CG2 . ILE B 105 ? 0.2569 0.2659 0.2971 0.0485  0.0143  -0.0527 101 ILE B CG2 
2191 C CD1 . ILE B 105 ? 0.2661 0.2412 0.2830 0.0430  0.0109  -0.0586 101 ILE B CD1 
2192 N N   . ASP B 106 ? 0.2362 0.2328 0.2722 0.0368  -0.0026 -0.0402 102 ASP B N   
2193 C CA  . ASP B 106 ? 0.2227 0.2105 0.2534 0.0327  -0.0065 -0.0381 102 ASP B CA  
2194 C C   . ASP B 106 ? 0.2536 0.2254 0.2766 0.0334  -0.0063 -0.0408 102 ASP B C   
2195 O O   . ASP B 106 ? 0.3076 0.2735 0.3322 0.0397  -0.0058 -0.0416 102 ASP B O   
2196 C CB  . ASP B 106 ? 0.2665 0.2570 0.3029 0.0336  -0.0108 -0.0328 102 ASP B CB  
2197 C CG  . ASP B 106 ? 0.4084 0.3985 0.4517 0.0410  -0.0122 -0.0318 102 ASP B CG  
2198 O OD1 . ASP B 106 ? 0.3891 0.3915 0.4420 0.0447  -0.0103 -0.0322 102 ASP B OD1 
2199 O OD2 . ASP B 106 ? 0.4492 0.4269 0.4882 0.0431  -0.0153 -0.0306 102 ASP B OD2 
2200 N N   . VAL B 107 ? 0.2403 0.2051 0.2550 0.0269  -0.0065 -0.0424 103 VAL B N   
2201 C CA  . VAL B 107 ? 0.2876 0.2355 0.2928 0.0251  -0.0058 -0.0452 103 VAL B CA  
2202 C C   . VAL B 107 ? 0.2795 0.2211 0.2786 0.0177  -0.0076 -0.0437 103 VAL B C   
2203 O O   . VAL B 107 ? 0.2846 0.2365 0.2862 0.0132  -0.0082 -0.0429 103 VAL B O   
2204 C CB  . VAL B 107 ? 0.3035 0.2493 0.3032 0.0230  -0.0020 -0.0516 103 VAL B CB  
2205 C CG1 . VAL B 107 ? 0.3350 0.2849 0.3387 0.0302  0.0010  -0.0539 103 VAL B CG1 
2206 C CG2 . VAL B 107 ? 0.3495 0.3067 0.3489 0.0164  -0.0020 -0.0533 103 VAL B CG2 
2207 N N   . LYS B 108 ? 0.2749 0.1987 0.2654 0.0165  -0.0080 -0.0435 104 LYS B N   
2208 C CA  . LYS B 108 ? 0.2954 0.2118 0.2783 0.0081  -0.0084 -0.0428 104 LYS B CA  
2209 C C   . LYS B 108 ? 0.2943 0.2139 0.2739 0.0000  -0.0053 -0.0486 104 LYS B C   
2210 O O   . LYS B 108 ? 0.2903 0.2093 0.2685 0.0006  -0.0032 -0.0532 104 LYS B O   
2211 C CB  . LYS B 108 ? 0.3541 0.2478 0.3260 0.0085  -0.0093 -0.0410 104 LYS B CB  
2212 C CG  . LYS B 108 ? 0.4058 0.2955 0.3804 0.0174  -0.0136 -0.0356 104 LYS B CG  
2213 C CD  . LYS B 108 ? 0.4360 0.3381 0.4171 0.0168  -0.0168 -0.0308 104 LYS B CD  
2214 C CE  . LYS B 108 ? 0.4330 0.3363 0.4199 0.0260  -0.0216 -0.0263 104 LYS B CE  
2215 N NZ  . LYS B 108 ? 0.4615 0.3790 0.4558 0.0252  -0.0247 -0.0225 104 LYS B NZ  
2216 N N   . PRO B 109 ? 0.2624 0.1856 0.2405 -0.0080 -0.0049 -0.0488 105 PRO B N   
2217 C CA  . PRO B 109 ? 0.2943 0.2245 0.2717 -0.0157 -0.0026 -0.0546 105 PRO B CA  
2218 C C   . PRO B 109 ? 0.3380 0.2534 0.3057 -0.0202 -0.0001 -0.0597 105 PRO B C   
2219 O O   . PRO B 109 ? 0.3535 0.2761 0.3220 -0.0229 0.0009  -0.0650 105 PRO B O   
2220 C CB  . PRO B 109 ? 0.2928 0.2268 0.2700 -0.0232 -0.0021 -0.0537 105 PRO B CB  
2221 C CG  . PRO B 109 ? 0.2997 0.2354 0.2802 -0.0180 -0.0045 -0.0475 105 PRO B CG  
2222 C CD  . PRO B 109 ? 0.2839 0.2083 0.2624 -0.0100 -0.0065 -0.0442 105 PRO B CD  
2223 N N   . THR B 110 ? 0.3615 0.2548 0.3189 -0.0203 0.0005  -0.0581 106 THR B N   
2224 C CA  . THR B 110 ? 0.4202 0.2959 0.3661 -0.0248 0.0032  -0.0630 106 THR B CA  
2225 C C   . THR B 110 ? 0.4115 0.2825 0.3572 -0.0161 0.0035  -0.0651 106 THR B C   
2226 O O   . THR B 110 ? 0.4677 0.3233 0.4033 -0.0189 0.0059  -0.0698 106 THR B O   
2227 C CB  . THR B 110 ? 0.4480 0.2982 0.3799 -0.0286 0.0041  -0.0605 106 THR B CB  
2228 O OG1 . THR B 110 ? 0.4891 0.3321 0.4214 -0.0188 0.0008  -0.0538 106 THR B OG1 
2229 C CG2 . THR B 110 ? 0.4639 0.3168 0.3931 -0.0407 0.0060  -0.0610 106 THR B CG2 
2230 N N   . GLU B 111 ? 0.3474 0.2313 0.3036 -0.0062 0.0016  -0.0621 107 GLU B N   
2231 C CA  . GLU B 111 ? 0.3402 0.2227 0.2976 0.0022  0.0029  -0.0644 107 GLU B CA  
2232 C C   . GLU B 111 ? 0.3793 0.2816 0.3436 0.0016  0.0037  -0.0679 107 GLU B C   
2233 O O   . GLU B 111 ? 0.3838 0.2867 0.3484 0.0074  0.0056  -0.0706 107 GLU B O   
2234 C CB  . GLU B 111 ? 0.3960 0.2801 0.3609 0.0136  0.0008  -0.0589 107 GLU B CB  
2235 C CG  . GLU B 111 ? 0.4525 0.3167 0.4105 0.0174  -0.0013 -0.0548 107 GLU B CG  
2236 C CD  . GLU B 111 ? 0.5377 0.4102 0.5062 0.0272  -0.0050 -0.0488 107 GLU B CD  
2237 O OE1 . GLU B 111 ? 0.5092 0.4029 0.4900 0.0292  -0.0056 -0.0476 107 GLU B OE1 
2238 O OE2 . GLU B 111 ? 0.6064 0.4637 0.5701 0.0328  -0.0076 -0.0454 107 GLU B OE2 
2239 N N   . MET B 112 ? 0.2918 0.2677 0.3046 -0.0368 0.0170  -0.1061 108 MET B N   
2240 C CA  . MET B 112 ? 0.2657 0.2556 0.2813 -0.0382 0.0154  -0.1125 108 MET B CA  
2241 C C   . MET B 112 ? 0.3282 0.3320 0.3489 -0.0435 0.0112  -0.1202 108 MET B C   
2242 O O   . MET B 112 ? 0.3585 0.3636 0.3859 -0.0472 0.0114  -0.1228 108 MET B O   
2243 C CB  . MET B 112 ? 0.2862 0.2812 0.3112 -0.0381 0.0192  -0.1150 108 MET B CB  
2244 C CG  . MET B 112 ? 0.2547 0.2364 0.2752 -0.0324 0.0238  -0.1070 108 MET B CG  
2245 S SD  . MET B 112 ? 0.3008 0.2862 0.3349 -0.0315 0.0292  -0.1100 108 MET B SD  
2246 C CE  . MET B 112 ? 0.2819 0.2796 0.3145 -0.0295 0.0258  -0.1163 108 MET B CE  
2247 N N   . LYS B 113 ? 0.3190 0.3339 0.3359 -0.0439 0.0071  -0.1235 109 LYS B N   
2248 C CA  . LYS B 113 ? 0.3285 0.3586 0.3493 -0.0486 0.0024  -0.1299 109 LYS B CA  
2249 C C   . LYS B 113 ? 0.3295 0.3808 0.3574 -0.0513 -0.0006 -0.1356 109 LYS B C   
2250 O O   . LYS B 113 ? 0.3077 0.3618 0.3336 -0.0489 -0.0003 -0.1347 109 LYS B O   
2251 C CB  . LYS B 113 ? 0.3869 0.4161 0.3979 -0.0472 -0.0009 -0.1286 109 LYS B CB  
2252 C CG  . LYS B 113 ? 0.4331 0.4429 0.4366 -0.0438 0.0003  -0.1225 109 LYS B CG  
2253 C CD  . LYS B 113 ? 0.4930 0.5037 0.4896 -0.0432 -0.0033 -0.1229 109 LYS B CD  
2254 C CE  . LYS B 113 ? 0.4769 0.4833 0.4643 -0.0389 -0.0030 -0.1182 109 LYS B CE  
2255 N NZ  . LYS B 113 ? 0.5946 0.6080 0.5791 -0.0395 -0.0054 -0.1214 109 LYS B NZ  
2256 N N   . GLN B 114 ? 0.3099 0.3772 0.3453 -0.0563 -0.0045 -0.1410 110 GLN B N   
2257 C CA  . GLN B 114 ? 0.3437 0.4346 0.3870 -0.0590 -0.0093 -0.1448 110 GLN B CA  
2258 C C   . GLN B 114 ? 0.3501 0.4515 0.3846 -0.0572 -0.0137 -0.1432 110 GLN B C   
2259 O O   . GLN B 114 ? 0.3717 0.4891 0.4099 -0.0573 -0.0178 -0.1433 110 GLN B O   
2260 C CB  . GLN B 114 ? 0.4854 0.5921 0.5375 -0.0645 -0.0132 -0.1490 110 GLN B CB  
2261 C CG  . GLN B 114 ? 0.6324 0.7670 0.6949 -0.0673 -0.0195 -0.1507 110 GLN B CG  
2262 C CD  . GLN B 114 ? 0.7849 0.9356 0.8402 -0.0672 -0.0257 -0.1493 110 GLN B CD  
2263 O OE1 . GLN B 114 ? 0.8450 0.9883 0.8899 -0.0666 -0.0253 -0.1492 110 GLN B OE1 
2264 N NE2 . GLN B 114 ? 0.8149 0.9880 0.8766 -0.0671 -0.0316 -0.1463 110 GLN B NE2 
2265 N N   . THR B 115 ? 0.2792 0.3724 0.3025 -0.0554 -0.0135 -0.1409 111 THR B N   
2266 C CA  . THR B 115 ? 0.2902 0.3927 0.3044 -0.0540 -0.0171 -0.1387 111 THR B CA  
2267 C C   . THR B 115 ? 0.2625 0.3528 0.2687 -0.0494 -0.0140 -0.1342 111 THR B C   
2268 O O   . THR B 115 ? 0.2930 0.3914 0.2914 -0.0485 -0.0171 -0.1316 111 THR B O   
2269 C CB  . THR B 115 ? 0.3120 0.4119 0.3190 -0.0542 -0.0180 -0.1383 111 THR B CB  
2270 O OG1 . THR B 115 ? 0.3216 0.3992 0.3252 -0.0514 -0.0134 -0.1361 111 THR B OG1 
2271 C CG2 . THR B 115 ? 0.3413 0.4562 0.3548 -0.0587 -0.0218 -0.1429 111 THR B CG2 
2272 N N   . ASP B 116 ? 0.2495 0.3204 0.2569 -0.0465 -0.0080 -0.1323 112 ASP B N   
2273 C CA  . ASP B 116 ? 0.2677 0.3271 0.2684 -0.0419 -0.0046 -0.1279 112 ASP B CA  
2274 C C   . ASP B 116 ? 0.2560 0.3296 0.2622 -0.0410 -0.0074 -0.1269 112 ASP B C   
2275 O O   . ASP B 116 ? 0.2659 0.3536 0.2843 -0.0422 -0.0101 -0.1251 112 ASP B O   
2276 C CB  . ASP B 116 ? 0.2739 0.3110 0.2768 -0.0389 0.0024  -0.1241 112 ASP B CB  
2277 C CG  . ASP B 116 ? 0.2675 0.2889 0.2638 -0.0371 0.0038  -0.1189 112 ASP B CG  
2278 O OD1 . ASP B 116 ? 0.3020 0.3256 0.2907 -0.0369 0.0008  -0.1179 112 ASP B OD1 
2279 O OD2 . ASP B 116 ? 0.2930 0.3002 0.2913 -0.0357 0.0073  -0.1152 112 ASP B OD2 
2280 N N   . ARG B 117 ? 0.2326 0.2994 0.2313 -0.0356 -0.0059 -0.1184 113 ARG B N   
2281 C CA  . ARG B 117 ? 0.2376 0.3114 0.2430 -0.0302 -0.0074 -0.1062 113 ARG B CA  
2282 C C   . ARG B 117 ? 0.2449 0.2985 0.2490 -0.0237 -0.0005 -0.0997 113 ARG B C   
2283 O O   . ARG B 117 ? 0.2413 0.2805 0.2331 -0.0226 0.0028  -0.1006 113 ARG B O   
2284 C CB  . ARG B 117 ? 0.2276 0.3175 0.2255 -0.0302 -0.0145 -0.1005 113 ARG B CB  
2285 C CG  . ARG B 117 ? 0.2448 0.3580 0.2450 -0.0365 -0.0219 -0.1058 113 ARG B CG  
2286 C CD  . ARG B 117 ? 0.2410 0.3688 0.2571 -0.0356 -0.0251 -0.1013 113 ARG B CD  
2287 N NE  . ARG B 117 ? 0.2197 0.3706 0.2387 -0.0416 -0.0322 -0.1057 113 ARG B NE  
2288 C CZ  . ARG B 117 ? 0.2666 0.4229 0.2913 -0.0473 -0.0324 -0.1161 113 ARG B CZ  
2289 N NH1 . ARG B 117 ? 0.2905 0.4304 0.3182 -0.0482 -0.0262 -0.1228 113 ARG B NH1 
2290 N NH2 . ARG B 117 ? 0.3120 0.4902 0.3391 -0.0525 -0.0391 -0.1196 113 ARG B NH2 
2291 N N   . VAL B 118 ? 0.2054 0.2583 0.2223 -0.0197 0.0019  -0.0938 114 VAL B N   
2292 C CA  . VAL B 118 ? 0.1918 0.2272 0.2081 -0.0133 0.0080  -0.0872 114 VAL B CA  
2293 C C   . VAL B 118 ? 0.1948 0.2329 0.2049 -0.0082 0.0045  -0.0767 114 VAL B C   
2294 O O   . VAL B 118 ? 0.2175 0.2730 0.2278 -0.0090 -0.0029 -0.0728 114 VAL B O   
2295 C CB  . VAL B 118 ? 0.2647 0.2981 0.2968 -0.0105 0.0123  -0.0851 114 VAL B CB  
2296 C CG1 . VAL B 118 ? 0.2560 0.2850 0.2931 -0.0163 0.0159  -0.0949 114 VAL B CG1 
2297 C CG2 . VAL B 118 ? 0.2901 0.3428 0.3344 -0.0082 0.0066  -0.0790 114 VAL B CG2 
2298 N N   . VAL B 119 ? 0.2174 0.2380 0.2215 -0.0033 0.0096  -0.0720 115 VAL B N   
2299 C CA  . VAL B 119 ? 0.1987 0.2177 0.1954 0.0013  0.0070  -0.0620 115 VAL B CA  
2300 C C   . VAL B 119 ? 0.2004 0.2173 0.2097 0.0085  0.0083  -0.0532 115 VAL B C   
2301 O O   . VAL B 119 ? 0.2062 0.2086 0.2203 0.0117  0.0156  -0.0536 115 VAL B O   
2302 C CB  . VAL B 119 ? 0.2203 0.2210 0.2013 0.0018  0.0118  -0.0629 115 VAL B CB  
2303 C CG1 . VAL B 119 ? 0.2557 0.2563 0.2277 0.0053  0.0082  -0.0528 115 VAL B CG1 
2304 C CG2 . VAL B 119 ? 0.2434 0.2442 0.2137 -0.0049 0.0118  -0.0740 115 VAL B CG2 
2305 N N   . LYS B 120 ? 0.2072 0.2387 0.2226 0.0111  0.0012  -0.0454 116 LYS B N   
2306 C CA  . LYS B 120 ? 0.2020 0.2338 0.2310 0.0184  0.0012  -0.0375 116 LYS B CA  
2307 C C   . LYS B 120 ? 0.2077 0.2370 0.2305 0.0235  -0.0034 -0.0262 116 LYS B C   
2308 O O   . LYS B 120 ? 0.2283 0.2677 0.2422 0.0207  -0.0107 -0.0226 116 LYS B O   
2309 C CB  . LYS B 120 ? 0.2099 0.2621 0.2552 0.0177  -0.0037 -0.0382 116 LYS B CB  
2310 C CG  . LYS B 120 ? 0.2893 0.3428 0.3512 0.0253  -0.0031 -0.0321 116 LYS B CG  
2311 C CD  . LYS B 120 ? 0.2941 0.3683 0.3722 0.0239  -0.0072 -0.0345 116 LYS B CD  
2312 C CE  . LYS B 120 ? 0.4001 0.4787 0.4946 0.0321  -0.0085 -0.0279 116 LYS B CE  
2313 N NZ  . LYS B 120 ? 0.5145 0.6009 0.6076 0.0365  -0.0177 -0.0175 116 LYS B NZ  
2314 N N   . TRP B 121 ? 0.2274 0.2432 0.2548 0.0306  0.0008  -0.0206 117 TRP B N   
2315 C CA  . TRP B 121 ? 0.2372 0.2494 0.2612 0.0362  -0.0038 -0.0092 117 TRP B CA  
2316 C C   . TRP B 121 ? 0.2987 0.3300 0.3338 0.0384  -0.0133 -0.0029 117 TRP B C   
2317 O O   . TRP B 121 ? 0.3428 0.3847 0.3948 0.0402  -0.0136 -0.0052 117 TRP B O   
2318 C CB  . TRP B 121 ? 0.3172 0.3125 0.3481 0.0437  0.0031  -0.0063 117 TRP B CB  
2319 C CG  . TRP B 121 ? 0.3097 0.2987 0.3389 0.0502  -0.0010 0.0050  117 TRP B CG  
2320 C CD1 . TRP B 121 ? 0.4074 0.4023 0.4507 0.0572  -0.0059 0.0122  117 TRP B CD1 
2321 C CD2 . TRP B 121 ? 0.3501 0.3250 0.3624 0.0504  -0.0008 0.0103  117 TRP B CD2 
2322 N NE1 . TRP B 121 ? 0.4547 0.4391 0.4907 0.0618  -0.0092 0.0220  117 TRP B NE1 
2323 C CE2 . TRP B 121 ? 0.3979 0.3700 0.4146 0.0574  -0.0059 0.0212  117 TRP B CE2 
2324 C CE3 . TRP B 121 ? 0.3768 0.3414 0.3709 0.0453  0.0031  0.0068  117 TRP B CE3 
2325 C CZ2 . TRP B 121 ? 0.5183 0.4772 0.5213 0.0588  -0.0072 0.0289  117 TRP B CZ2 
2326 C CZ3 . TRP B 121 ? 0.5249 0.4776 0.5054 0.0468  0.0021  0.0141  117 TRP B CZ3 
2327 C CH2 . TRP B 121 ? 0.5322 0.4819 0.5170 0.0532  -0.0030 0.0252  117 TRP B CH2 
2328 N N   . MET B 122 ? 0.2857 0.3220 0.3116 0.0381  -0.0214 0.0054  118 MET B N   
2329 C CA  . MET B 122 ? 0.4200 0.4740 0.4551 0.0402  -0.0315 0.0126  118 MET B CA  
2330 C C   . MET B 122 ? 0.5356 0.5817 0.5679 0.0465  -0.0367 0.0252  118 MET B C   
2331 O O   . MET B 122 ? 0.5717 0.6087 0.5872 0.0443  -0.0378 0.0296  118 MET B O   
2332 C CB  . MET B 122 ? 0.5046 0.5770 0.5319 0.0321  -0.0386 0.0105  118 MET B CB  
2333 C CG  . MET B 122 ? 0.6883 0.7779 0.7279 0.0285  -0.0390 0.0021  118 MET B CG  
2334 S SD  . MET B 122 ? 0.8357 0.9493 0.8678 0.0205  -0.0497 0.0028  118 MET B SD  
2335 C CE  . MET B 122 ? 0.8089 0.9401 0.8608 0.0263  -0.0583 0.0106  118 MET B CE  
2336 N N   . LEU B 123 ? 0.6239 0.6741 0.6728 0.0540  -0.0404 0.0309  119 LEU B N   
2337 C CA  . LEU B 123 ? 0.7762 0.8187 0.8244 0.0607  -0.0463 0.0431  119 LEU B CA  
2338 C C   . LEU B 123 ? 0.8406 0.8981 0.8843 0.0583  -0.0590 0.0520  119 LEU B C   
2339 O O   . LEU B 123 ? 0.8938 0.9436 0.9306 0.0613  -0.0648 0.0627  119 LEU B O   
2340 C CB  . LEU B 123 ? 0.7968 0.8361 0.8654 0.0706  -0.0448 0.0449  119 LEU B CB  
2341 C CG  . LEU B 123 ? 0.7995 0.8218 0.8679 0.0789  -0.0462 0.0546  119 LEU B CG  
2342 C CD1 . LEU B 123 ? 0.7895 0.7893 0.8467 0.0787  -0.0359 0.0515  119 LEU B CD1 
2343 C CD2 . LEU B 123 ? 0.8025 0.8286 0.8937 0.0886  -0.0480 0.0564  119 LEU B CD2 
2344 N N   . THR B 124 ? 0.8379 0.9165 0.8850 0.0528  -0.0636 0.0479  120 THR B N   
2345 C CA  . THR B 124 ? 0.8599 0.9554 0.9046 0.0503  -0.0759 0.0561  120 THR B CA  
2346 C C   . THR B 124 ? 0.8088 0.9186 0.8412 0.0395  -0.0773 0.0496  120 THR B C   
2347 O O   . THR B 124 ? 0.8292 0.9557 0.8705 0.0361  -0.0777 0.0424  120 THR B O   
2348 C CB  . THR B 124 ? 0.9050 1.0153 0.9710 0.0563  -0.0821 0.0587  120 THR B CB  
2349 O OG1 . THR B 124 ? 0.9256 1.0229 1.0055 0.0663  -0.0780 0.0605  120 THR B OG1 
2350 C CG2 . THR B 124 ? 0.9208 1.0434 0.9845 0.0562  -0.0957 0.0704  120 THR B CG2 
2351 N N   . GLY B 125 A 0.7391 0.8431 0.7514 0.0339  -0.0781 0.0520  120 GLY B N   
2352 C CA  . GLY B 125 A 0.6773 0.7958 0.6772 0.0236  -0.0801 0.0462  120 GLY B CA  
2353 C C   . GLY B 125 A 0.6537 0.7651 0.6318 0.0188  -0.0822 0.0515  120 GLY B C   
2354 O O   . GLY B 125 A 0.6691 0.7628 0.6414 0.0231  -0.0811 0.0590  120 GLY B O   
2355 N N   . SER B 126 B 0.6724 0.7987 0.6385 0.0093  -0.0853 0.0471  120 SER B N   
2356 C CA  . SER B 126 B 0.6850 0.8067 0.6295 0.0033  -0.0863 0.0500  120 SER B CA  
2357 C C   . SER B 126 B 0.5832 0.6852 0.5188 0.0035  -0.0752 0.0424  120 SER B C   
2358 O O   . SER B 126 B 0.6279 0.7198 0.5474 0.0013  -0.0747 0.0467  120 SER B O   
2359 C CB  . SER B 126 B 0.7828 0.9272 0.7175 -0.0071 -0.0919 0.0456  120 SER B CB  
2360 O OG  . SER B 126 B 0.8067 0.9630 0.7514 -0.0095 -0.0886 0.0331  120 SER B OG  
2361 N N   . HIS B 127 C 0.4662 0.5627 0.4117 0.0056  -0.0666 0.0315  120 HIS B N   
2362 C CA  . HIS B 127 C 0.4137 0.4923 0.3525 0.0057  -0.0559 0.0232  120 HIS B CA  
2363 C C   . HIS B 127 C 0.3484 0.4109 0.3019 0.0146  -0.0490 0.0232  120 HIS B C   
2364 O O   . HIS B 127 C 0.3411 0.4102 0.3117 0.0192  -0.0514 0.0252  120 HIS B O   
2365 C CB  . HIS B 127 C 0.3809 0.4685 0.3163 -0.0014 -0.0521 0.0087  120 HIS B CB  
2366 C CG  . HIS B 127 C 0.4394 0.5474 0.3638 -0.0101 -0.0595 0.0074  120 HIS B CG  
2367 N ND1 . HIS B 127 C 0.4691 0.5771 0.3750 -0.0149 -0.0622 0.0114  120 HIS B ND1 
2368 C CD2 . HIS B 127 C 0.4083 0.5381 0.3376 -0.0153 -0.0646 0.0024  120 HIS B CD2 
2369 C CE1 . HIS B 127 C 0.4021 0.5315 0.3019 -0.0227 -0.0686 0.0088  120 HIS B CE1 
2370 N NE2 . HIS B 127 C 0.4562 0.5990 0.3701 -0.0230 -0.0703 0.0033  120 HIS B NE2 
2371 N N   . MET B 128 ? 0.3294 0.3713 0.2762 0.0168  -0.0404 0.0207  121 MET B N   
2372 C CA  . MET B 128 ? 0.3079 0.3340 0.2675 0.0248  -0.0335 0.0209  121 MET B CA  
2373 C C   . MET B 128 ? 0.3371 0.3643 0.3081 0.0243  -0.0265 0.0091  121 MET B C   
2374 O O   . MET B 128 ? 0.3620 0.3811 0.3466 0.0303  -0.0217 0.0088  121 MET B O   
2375 C CB  . MET B 128 ? 0.4116 0.4153 0.3590 0.0268  -0.0266 0.0224  121 MET B CB  
2376 C CG  . MET B 128 ? 0.4580 0.4568 0.3922 0.0269  -0.0323 0.0339  121 MET B CG  
2377 S SD  . MET B 128 ? 0.5590 0.5310 0.4809 0.0296  -0.0232 0.0347  121 MET B SD  
2378 C CE  . MET B 128 ? 0.6241 0.5942 0.5319 0.0287  -0.0322 0.0495  121 MET B CE  
2379 N N   . ILE B 129 ? 0.2890 0.3263 0.2550 0.0169  -0.0261 -0.0007 122 ILE B N   
2380 C CA  . ILE B 129 ? 0.2690 0.3083 0.2450 0.0152  -0.0207 -0.0120 122 ILE B CA  
2381 C C   . ILE B 129 ? 0.2724 0.3344 0.2512 0.0089  -0.0272 -0.0168 122 ILE B C   
2382 O O   . ILE B 129 ? 0.3030 0.3773 0.2720 0.0045  -0.0342 -0.0138 122 ILE B O   
2383 C CB  . ILE B 129 ? 0.2420 0.2656 0.2082 0.0125  -0.0118 -0.0214 122 ILE B CB  
2384 C CG1 . ILE B 129 ? 0.2799 0.3068 0.2274 0.0061  -0.0141 -0.0244 122 ILE B CG1 
2385 C CG2 . ILE B 129 ? 0.2795 0.2811 0.2459 0.0189  -0.0044 -0.0176 122 ILE B CG2 
2386 C CD1 . ILE B 129 ? 0.3113 0.3232 0.2490 0.0038  -0.0060 -0.0339 122 ILE B CD1 
2387 N N   . GLU B 130 ? 0.2225 0.2906 0.2147 0.0081  -0.0248 -0.0242 123 GLU B N   
2388 C CA  . GLU B 130 ? 0.2536 0.3418 0.2490 0.0016  -0.0296 -0.0309 123 GLU B CA  
2389 C C   . GLU B 130 ? 0.2235 0.3064 0.2204 -0.0026 -0.0229 -0.0440 123 GLU B C   
2390 O O   . GLU B 130 ? 0.2424 0.3092 0.2439 0.0005  -0.0151 -0.0467 123 GLU B O   
2391 C CB  . GLU B 130 ? 0.2574 0.3623 0.2699 0.0042  -0.0355 -0.0262 123 GLU B CB  
2392 C CG  . GLU B 130 ? 0.3300 0.4285 0.3595 0.0091  -0.0295 -0.0283 123 GLU B CG  
2393 C CD  . GLU B 130 ? 0.4820 0.5985 0.5292 0.0118  -0.0352 -0.0246 123 GLU B CD  
2394 O OE1 . GLU B 130 ? 0.4981 0.6340 0.5454 0.0080  -0.0432 -0.0235 123 GLU B OE1 
2395 O OE2 . GLU B 130 ? 0.4376 0.5492 0.4987 0.0176  -0.0315 -0.0231 123 GLU B OE2 
2396 N N   . PHE B 131 ? 0.2495 0.3461 0.2428 -0.0098 -0.0262 -0.0522 124 PHE B N   
2397 C CA  . PHE B 131 ? 0.2286 0.3219 0.2234 -0.0145 -0.0215 -0.0650 124 PHE B CA  
2398 C C   . PHE B 131 ? 0.2256 0.3363 0.2354 -0.0169 -0.0250 -0.0682 124 PHE B C   
2399 O O   . PHE B 131 ? 0.2440 0.3746 0.2539 -0.0206 -0.0325 -0.0676 124 PHE B O   
2400 C CB  . PHE B 131 ? 0.2624 0.3578 0.2417 -0.0207 -0.0228 -0.0727 124 PHE B CB  
2401 C CG  . PHE B 131 ? 0.2780 0.3587 0.2424 -0.0186 -0.0199 -0.0691 124 PHE B CG  
2402 C CD1 . PHE B 131 ? 0.2781 0.3366 0.2399 -0.0156 -0.0116 -0.0716 124 PHE B CD1 
2403 C CD2 . PHE B 131 ? 0.3388 0.4279 0.2916 -0.0198 -0.0256 -0.0625 124 PHE B CD2 
2404 C CE1 . PHE B 131 ? 0.3067 0.3517 0.2549 -0.0136 -0.0088 -0.0683 124 PHE B CE1 
2405 C CE2 . PHE B 131 ? 0.3496 0.4251 0.2886 -0.0182 -0.0228 -0.0590 124 PHE B CE2 
2406 C CZ  . PHE B 131 ? 0.3803 0.4340 0.3171 -0.0150 -0.0144 -0.0620 124 PHE B CZ  
2407 N N   . ILE B 132 ? 0.2068 0.3107 0.2289 -0.0153 -0.0197 -0.0714 125 ILE B N   
2408 C CA  . ILE B 132 ? 0.2264 0.3462 0.2649 -0.0162 -0.0225 -0.0722 125 ILE B CA  
2409 C C   . ILE B 132 ? 0.2028 0.3185 0.2471 -0.0210 -0.0177 -0.0833 125 ILE B C   
2410 O O   . ILE B 132 ? 0.1994 0.2964 0.2387 -0.0214 -0.0109 -0.0882 125 ILE B O   
2411 C CB  . ILE B 132 ? 0.2314 0.3519 0.2832 -0.0085 -0.0225 -0.0625 125 ILE B CB  
2412 C CG1 . ILE B 132 ? 0.2370 0.3355 0.2906 -0.0034 -0.0136 -0.0614 125 ILE B CG1 
2413 C CG2 . ILE B 132 ? 0.3912 0.5204 0.4395 -0.0048 -0.0298 -0.0516 125 ILE B CG2 
2414 C CD1 . ILE B 132 ? 0.2771 0.3787 0.3465 0.0037  -0.0133 -0.0542 125 ILE B CD1 
2415 N N   . GLU B 133 ? 0.2038 0.3377 0.2586 -0.0251 -0.0218 -0.0870 126 GLU B N   
2416 C CA  . GLU B 133 ? 0.2165 0.3490 0.2791 -0.0300 -0.0182 -0.0965 126 GLU B CA  
2417 C C   . GLU B 133 ? 0.2240 0.3438 0.2968 -0.0257 -0.0111 -0.0941 126 GLU B C   
2418 O O   . GLU B 133 ? 0.2321 0.3499 0.3099 -0.0186 -0.0102 -0.0851 126 GLU B O   
2419 C CB  . GLU B 133 ? 0.2493 0.4057 0.3222 -0.0346 -0.0245 -0.0992 126 GLU B CB  
2420 C CG  . GLU B 133 ? 0.3523 0.5221 0.4163 -0.0408 -0.0308 -0.1047 126 GLU B CG  
2421 C CD  . GLU B 133 ? 0.5490 0.7417 0.6239 -0.0458 -0.0362 -0.1083 126 GLU B CD  
2422 O OE1 . GLU B 133 ? 0.6117 0.8195 0.6964 -0.0425 -0.0404 -0.1006 126 GLU B OE1 
2423 O OE2 . GLU B 133 ? 0.6122 0.8077 0.6863 -0.0529 -0.0365 -0.1188 126 GLU B OE2 
2424 N N   . PHE B 134 ? 0.2045 0.3164 0.2808 -0.0304 -0.0063 -0.1023 127 PHE B N   
2425 C CA  . PHE B 134 ? 0.1914 0.2899 0.2753 -0.0278 0.0012  -0.1013 127 PHE B CA  
2426 C C   . PHE B 134 ? 0.2125 0.3146 0.3053 -0.0348 0.0029  -0.1096 127 PHE B C   
2427 O O   . PHE B 134 ? 0.2490 0.3589 0.3396 -0.0416 -0.0009 -0.1170 127 PHE B O   
2428 C CB  . PHE B 134 ? 0.2550 0.3284 0.3267 -0.0259 0.0077  -0.1021 127 PHE B CB  
2429 C CG  . PHE B 134 ? 0.2422 0.3063 0.3041 -0.0328 0.0086  -0.1122 127 PHE B CG  
2430 C CD1 . PHE B 134 ? 0.2339 0.3021 0.2840 -0.0352 0.0037  -0.1156 127 PHE B CD1 
2431 C CD2 . PHE B 134 ? 0.2586 0.3121 0.3241 -0.0374 0.0134  -0.1189 127 PHE B CD2 
2432 C CE1 . PHE B 134 ? 0.3006 0.3614 0.3430 -0.0412 0.0039  -0.1259 127 PHE B CE1 
2433 C CE2 . PHE B 134 ? 0.2758 0.3208 0.3333 -0.0436 0.0131  -0.1284 127 PHE B CE2 
2434 C CZ  . PHE B 134 ? 0.2793 0.3280 0.3256 -0.0452 0.0083  -0.1323 127 PHE B CZ  
2435 N N   . GLU B 135 ? 0.2190 0.3153 0.3217 -0.0334 0.0087  -0.1085 128 GLU B N   
2436 C CA  . GLU B 135 ? 0.2363 0.3316 0.3462 -0.0404 0.0118  -0.1157 128 GLU B CA  
2437 C C   . GLU B 135 ? 0.2343 0.3069 0.3412 -0.0395 0.0204  -0.1161 128 GLU B C   
2438 O O   . GLU B 135 ? 0.2280 0.2913 0.3332 -0.0324 0.0240  -0.1096 128 GLU B O   
2439 C CB  . GLU B 135 ? 0.2714 0.3862 0.3988 -0.0405 0.0105  -0.1139 128 GLU B CB  
2440 C CG  . GLU B 135 ? 0.3958 0.5342 0.5287 -0.0385 0.0024  -0.1103 128 GLU B CG  
2441 C CD  . GLU B 135 ? 0.5322 0.6882 0.6831 -0.0365 0.0019  -0.1074 128 GLU B CD  
2442 O OE1 . GLU B 135 ? 0.5186 0.6807 0.6755 -0.0283 0.0004  -0.0994 128 GLU B OE1 
2443 O OE2 . GLU B 135 ? 0.5633 0.7269 0.7225 -0.0432 0.0029  -0.1134 128 GLU B OE2 
2444 N N   . ILE B 136 ? 0.2479 0.3118 0.3545 -0.0470 0.0233  -0.1235 129 ILE B N   
2445 C CA  . ILE B 136 ? 0.2809 0.3237 0.3846 -0.0479 0.0310  -0.1246 129 ILE B CA  
2446 C C   . ILE B 136 ? 0.2607 0.3091 0.3771 -0.0535 0.0340  -0.1272 129 ILE B C   
2447 O O   . ILE B 136 ? 0.2834 0.3436 0.4049 -0.0604 0.0302  -0.1325 129 ILE B O   
2448 C CB  . ILE B 136 ? 0.4118 0.4359 0.5013 -0.0525 0.0315  -0.1313 129 ILE B CB  
2449 C CG1 . ILE B 136 ? 0.5011 0.5227 0.5779 -0.0483 0.0279  -0.1302 129 ILE B CG1 
2450 C CG2 . ILE B 136 ? 0.3587 0.3632 0.4426 -0.0500 0.0385  -0.1248 129 ILE B CG2 
2451 C CD1 . ILE B 136 ? 0.5142 0.5325 0.5889 -0.0394 0.0303  -0.1213 129 ILE B CD1 
2452 N N   . GLU B 137 ? 0.2388 0.2790 0.3600 -0.0510 0.0409  -0.1239 130 GLU B N   
2453 C CA  . GLU B 137 ? 0.2801 0.3242 0.4122 -0.0569 0.0447  -0.1264 130 GLU B CA  
2454 C C   . GLU B 137 ? 0.2750 0.2961 0.4006 -0.0597 0.0520  -0.1277 130 GLU B C   
2455 O O   . GLU B 137 ? 0.2661 0.2745 0.3866 -0.0532 0.0564  -0.1233 130 GLU B O   
2456 C CB  . GLU B 137 ? 0.2617 0.3232 0.4092 -0.0514 0.0460  -0.1212 130 GLU B CB  
2457 C CG  . GLU B 137 ? 0.3947 0.4632 0.5544 -0.0576 0.0502  -0.1240 130 GLU B CG  
2458 C CD  . GLU B 137 ? 0.4783 0.5656 0.6540 -0.0514 0.0510  -0.1196 130 GLU B CD  
2459 O OE1 . GLU B 137 ? 0.4582 0.5526 0.6355 -0.0424 0.0476  -0.1142 130 GLU B OE1 
2460 O OE2 . GLU B 137 ? 0.4904 0.5856 0.6771 -0.0557 0.0549  -0.1217 130 GLU B OE2 
2461 N N   . ASP B 138 ? 0.2935 0.3112 0.4167 -0.0667 0.0526  -0.1295 131 ASP B N   
2462 C CA  . ASP B 138 ? 0.2997 0.3024 0.4127 -0.0651 0.0572  -0.1219 131 ASP B CA  
2463 C C   . ASP B 138 ? 0.2981 0.3061 0.4249 -0.0673 0.0638  -0.1232 131 ASP B C   
2464 O O   . ASP B 138 ? 0.3115 0.3333 0.4506 -0.0741 0.0634  -0.1283 131 ASP B O   
2465 C CB  . ASP B 138 ? 0.3498 0.3490 0.4536 -0.0697 0.0532  -0.1209 131 ASP B CB  
2466 C CG  . ASP B 138 ? 0.4400 0.4250 0.5327 -0.0685 0.0556  -0.1131 131 ASP B CG  
2467 O OD1 . ASP B 138 ? 0.3942 0.3750 0.4879 -0.0657 0.0612  -0.1091 131 ASP B OD1 
2468 O OD2 . ASP B 138 ? 0.5129 0.4916 0.5961 -0.0705 0.0511  -0.1112 131 ASP B OD2 
2469 N N   . LEU B 139 ? 0.2681 0.2673 0.3933 -0.0617 0.0695  -0.1179 132 LEU B N   
2470 C CA  . LEU B 139 ? 0.2750 0.2789 0.4133 -0.0631 0.0764  -0.1192 132 LEU B CA  
2471 C C   . LEU B 139 ? 0.2985 0.2947 0.4274 -0.0652 0.0798  -0.1139 132 LEU B C   
2472 O O   . LEU B 139 ? 0.3279 0.3277 0.4655 -0.0665 0.0858  -0.1148 132 LEU B O   
2473 C CB  . LEU B 139 ? 0.3104 0.3104 0.4539 -0.0550 0.0808  -0.1170 132 LEU B CB  
2474 C CG  . LEU B 139 ? 0.3034 0.3130 0.4497 -0.0466 0.0756  -0.1149 132 LEU B CG  
2475 C CD1 . LEU B 139 ? 0.3010 0.3077 0.4502 -0.0360 0.0797  -0.1087 132 LEU B CD1 
2476 C CD2 . LEU B 139 ? 0.3156 0.3509 0.4751 -0.0477 0.0699  -0.1160 132 LEU B CD2 
2477 N N   . GLY B 140 ? 0.3997 0.2777 0.3400 -0.0880 0.0273  -0.0742 133 GLY B N   
2478 C CA  . GLY B 140 ? 0.3808 0.2356 0.3043 -0.0955 0.0269  -0.0684 133 GLY B CA  
2479 C C   . GLY B 140 ? 0.4051 0.2510 0.3155 -0.0954 0.0221  -0.0598 133 GLY B C   
2480 O O   . GLY B 140 ? 0.3834 0.2409 0.2984 -0.0896 0.0190  -0.0582 133 GLY B O   
2481 N N   . VAL B 141 ? 0.4282 0.2526 0.3215 -0.1021 0.0216  -0.0543 134 VAL B N   
2482 C CA  . VAL B 141 ? 0.4364 0.2500 0.3156 -0.1018 0.0164  -0.0461 134 VAL B CA  
2483 C C   . VAL B 141 ? 0.4573 0.2757 0.3301 -0.1083 0.0221  -0.0469 134 VAL B C   
2484 O O   . VAL B 141 ? 0.4965 0.3170 0.3675 -0.1150 0.0301  -0.0500 134 VAL B O   
2485 C CB  . VAL B 141 ? 0.4672 0.2547 0.3291 -0.1057 0.0130  -0.0398 134 VAL B CB  
2486 C CG1 . VAL B 141 ? 0.4893 0.2655 0.3348 -0.1062 0.0082  -0.0321 134 VAL B CG1 
2487 C CG2 . VAL B 141 ? 0.4914 0.2745 0.3604 -0.0981 0.0059  -0.0391 134 VAL B CG2 
2488 N N   . MET B 142 ? 0.4185 0.2434 0.2908 -0.1039 0.0179  -0.0436 135 MET B N   
2489 C CA  . MET B 142 ? 0.4563 0.2858 0.3228 -0.1090 0.0221  -0.0441 135 MET B CA  
2490 C C   . MET B 142 ? 0.4601 0.2798 0.3140 -0.1074 0.0156  -0.0365 135 MET B C   
2491 O O   . MET B 142 ? 0.4337 0.2520 0.2902 -0.0996 0.0075  -0.0325 135 MET B O   
2492 C CB  . MET B 142 ? 0.4758 0.3286 0.3587 -0.1042 0.0241  -0.0495 135 MET B CB  
2493 C CG  . MET B 142 ? 0.5643 0.4303 0.4621 -0.1029 0.0290  -0.0576 135 MET B CG  
2494 S SD  . MET B 142 ? 0.5357 0.4266 0.4496 -0.0970 0.0307  -0.0632 135 MET B SD  
2495 C CE  . MET B 142 ? 0.5783 0.4819 0.5061 -0.0958 0.0366  -0.0719 135 MET B CE  
2496 N N   . GLU B 143 ? 0.4554 0.2691 0.2959 -0.1148 0.0191  -0.0351 136 GLU B N   
2497 C CA  . GLU B 143 ? 0.4481 0.2583 0.2796 -0.1129 0.0137  -0.0298 136 GLU B CA  
2498 C C   . GLU B 143 ? 0.4289 0.2591 0.2724 -0.1106 0.0157  -0.0339 136 GLU B C   
2499 O O   . GLU B 143 ? 0.4492 0.2873 0.2944 -0.1164 0.0231  -0.0390 136 GLU B O   
2500 C CB  . GLU B 143 ? 0.4812 0.2733 0.2904 -0.1216 0.0158  -0.0258 136 GLU B CB  
2501 C CG  . GLU B 143 ? 0.5232 0.3107 0.3227 -0.1185 0.0089  -0.0204 136 GLU B CG  
2502 C CD  . GLU B 143 ? 0.6904 0.4601 0.4665 -0.1265 0.0106  -0.0162 136 GLU B CD  
2503 O OE1 . GLU B 143 ? 0.7522 0.5123 0.5189 -0.1354 0.0178  -0.0172 136 GLU B OE1 
2504 O OE2 . GLU B 143 ? 0.7563 0.5217 0.5234 -0.1239 0.0048  -0.0121 136 GLU B OE2 
2505 N N   . ILE B 144 ? 0.4086 0.2473 0.2611 -0.1020 0.0091  -0.0320 137 ILE B N   
2506 C CA  . ILE B 144 ? 0.3828 0.2413 0.2504 -0.0981 0.0108  -0.0360 137 ILE B CA  
2507 C C   . ILE B 144 ? 0.4008 0.2625 0.2708 -0.0916 0.0035  -0.0321 137 ILE B C   
2508 O O   . ILE B 144 ? 0.3886 0.2420 0.2556 -0.0870 -0.0035 -0.0277 137 ILE B O   
2509 C CB  . ILE B 144 ? 0.3732 0.2439 0.2572 -0.0934 0.0128  -0.0407 137 ILE B CB  
2510 C CG1 . ILE B 144 ? 0.4022 0.2924 0.3009 -0.0890 0.0146  -0.0446 137 ILE B CG1 
2511 C CG2 . ILE B 144 ? 0.3853 0.2509 0.2729 -0.0866 0.0062  -0.0375 137 ILE B CG2 
2512 C CD1 . ILE B 144 ? 0.4258 0.3274 0.3377 -0.0861 0.0182  -0.0504 137 ILE B CD1 
2513 N N   . ASP B 145 ? 0.3575 0.2312 0.2335 -0.0912 0.0052  -0.0342 138 ASP B N   
2514 C CA  . ASP B 145 ? 0.3671 0.2474 0.2498 -0.0848 -0.0006 -0.0318 138 ASP B CA  
2515 C C   . ASP B 145 ? 0.3470 0.2401 0.2468 -0.0771 -0.0018 -0.0334 138 ASP B C   
2516 O O   . ASP B 145 ? 0.3490 0.2529 0.2582 -0.0768 0.0034  -0.0378 138 ASP B O   
2517 C CB  . ASP B 145 ? 0.3549 0.2436 0.2390 -0.0873 0.0020  -0.0340 138 ASP B CB  
2518 C CG  . ASP B 145 ? 0.4124 0.2899 0.2797 -0.0938 0.0021  -0.0322 138 ASP B CG  
2519 O OD1 . ASP B 145 ? 0.4610 0.3236 0.3153 -0.0947 -0.0020 -0.0279 138 ASP B OD1 
2520 O OD2 . ASP B 145 ? 0.4966 0.3804 0.3637 -0.0978 0.0060  -0.0354 138 ASP B OD2 
2521 N N   . VAL B 146 ? 0.3207 0.2127 0.2242 -0.0708 -0.0085 -0.0301 139 VAL B N   
2522 C CA  . VAL B 146 ? 0.3007 0.2049 0.2199 -0.0634 -0.0097 -0.0313 139 VAL B CA  
2523 C C   . VAL B 146 ? 0.2641 0.1746 0.1898 -0.0586 -0.0144 -0.0293 139 VAL B C   
2524 O O   . VAL B 146 ? 0.2835 0.1868 0.2013 -0.0597 -0.0185 -0.0268 139 VAL B O   
2525 C CB  . VAL B 146 ? 0.3050 0.2041 0.2257 -0.0600 -0.0127 -0.0308 139 VAL B CB  
2526 C CG1 . VAL B 146 ? 0.3286 0.2251 0.2469 -0.0645 -0.0068 -0.0341 139 VAL B CG1 
2527 C CG2 . VAL B 146 ? 0.3470 0.2306 0.2562 -0.0598 -0.0195 -0.0266 139 VAL B CG2 
2528 N N   . TYR B 147 ? 0.2389 0.1631 0.1789 -0.0534 -0.0133 -0.0308 140 TYR B N   
2529 C CA  . TYR B 147 ? 0.2455 0.1778 0.1937 -0.0498 -0.0157 -0.0298 140 TYR B CA  
2530 C C   . TYR B 147 ? 0.2306 0.1714 0.1911 -0.0428 -0.0180 -0.0297 140 TYR B C   
2531 O O   . TYR B 147 ? 0.2300 0.1751 0.1954 -0.0405 -0.0158 -0.0313 140 TYR B O   
2532 C CB  . TYR B 147 ? 0.2650 0.2068 0.2183 -0.0516 -0.0104 -0.0318 140 TYR B CB  
2533 C CG  . TYR B 147 ? 0.2405 0.1764 0.1833 -0.0584 -0.0078 -0.0328 140 TYR B CG  
2534 C CD1 . TYR B 147 ? 0.2702 0.2025 0.2065 -0.0632 -0.0032 -0.0353 140 TYR B CD1 
2535 C CD2 . TYR B 147 ? 0.2713 0.2061 0.2113 -0.0602 -0.0098 -0.0319 140 TYR B CD2 
2536 C CE1 . TYR B 147 ? 0.2719 0.1996 0.1986 -0.0698 -0.0003 -0.0368 140 TYR B CE1 
2537 C CE2 . TYR B 147 ? 0.2665 0.1968 0.1969 -0.0664 -0.0073 -0.0332 140 TYR B CE2 
2538 C CZ  . TYR B 147 ? 0.2899 0.2167 0.2135 -0.0713 -0.0025 -0.0356 140 TYR B CZ  
2539 O OH  . TYR B 147 ? 0.3303 0.2535 0.2445 -0.0779 0.0003  -0.0374 140 TYR B OH  
2540 N N   . ASP B 148 ? 0.2486 0.1930 0.2148 -0.0394 -0.0220 -0.0283 141 ASP B N   
2541 C CA  . ASP B 148 ? 0.2553 0.2093 0.2339 -0.0332 -0.0237 -0.0286 141 ASP B CA  
2542 C C   . ASP B 148 ? 0.2188 0.1803 0.2053 -0.0319 -0.0243 -0.0281 141 ASP B C   
2543 O O   . ASP B 148 ? 0.2295 0.1872 0.2114 -0.0351 -0.0253 -0.0276 141 ASP B O   
2544 C CB  . ASP B 148 ? 0.3132 0.2611 0.2904 -0.0297 -0.0300 -0.0282 141 ASP B CB  
2545 C CG  . ASP B 148 ? 0.4505 0.4087 0.4395 -0.0240 -0.0297 -0.0297 141 ASP B CG  
2546 O OD1 . ASP B 148 ? 0.4610 0.4310 0.4590 -0.0225 -0.0248 -0.0305 141 ASP B OD1 
2547 O OD2 . ASP B 148 ? 0.5082 0.4623 0.4970 -0.0209 -0.0343 -0.0302 141 ASP B OD2 
2548 N N   . ILE B 149 ? 0.2389 0.2115 0.2375 -0.0275 -0.0231 -0.0286 142 ILE B N   
2549 C CA  . ILE B 149 ? 0.2166 0.1966 0.2243 -0.0261 -0.0235 -0.0283 142 ILE B CA  
2550 C C   . ILE B 149 ? 0.1904 0.1758 0.2069 -0.0209 -0.0274 -0.0291 142 ILE B C   
2551 O O   . ILE B 149 ? 0.2291 0.2165 0.2475 -0.0178 -0.0277 -0.0298 142 ILE B O   
2552 C CB  . ILE B 149 ? 0.2211 0.2100 0.2353 -0.0266 -0.0168 -0.0282 142 ILE B CB  
2553 C CG1 . ILE B 149 ? 0.2790 0.2747 0.2972 -0.0236 -0.0124 -0.0287 142 ILE B CG1 
2554 C CG2 . ILE B 149 ? 0.2662 0.2504 0.2732 -0.0317 -0.0141 -0.0283 142 ILE B CG2 
2555 C CD1 . ILE B 149 ? 0.2598 0.2641 0.2847 -0.0227 -0.0067 -0.0281 142 ILE B CD1 
2556 N N   . GLU B 150 ? 0.1910 0.1791 0.2132 -0.0201 -0.0307 -0.0296 143 GLU B N   
2557 C CA  . GLU B 150 ? 0.1839 0.1804 0.2173 -0.0155 -0.0332 -0.0312 143 GLU B CA  
2558 C C   . GLU B 150 ? 0.2125 0.2208 0.2568 -0.0152 -0.0269 -0.0309 143 GLU B C   
2559 O O   . GLU B 150 ? 0.2074 0.2169 0.2538 -0.0181 -0.0245 -0.0303 143 GLU B O   
2560 C CB  . GLU B 150 ? 0.2286 0.2224 0.2633 -0.0143 -0.0405 -0.0329 143 GLU B CB  
2561 C CG  . GLU B 150 ? 0.2475 0.2525 0.2961 -0.0097 -0.0423 -0.0357 143 GLU B CG  
2562 C CD  . GLU B 150 ? 0.2818 0.2861 0.3338 -0.0077 -0.0498 -0.0387 143 GLU B CD  
2563 O OE1 . GLU B 150 ? 0.3167 0.3104 0.3592 -0.0066 -0.0569 -0.0390 143 GLU B OE1 
2564 O OE2 . GLU B 150 ? 0.3395 0.3540 0.4037 -0.0071 -0.0488 -0.0411 143 GLU B OE2 
2565 N N   . VAL B 151 ? 0.2100 0.2267 0.2611 -0.0117 -0.0242 -0.0313 144 VAL B N   
2566 C CA  . VAL B 151 ? 0.1964 0.2236 0.2564 -0.0111 -0.0178 -0.0305 144 VAL B CA  
2567 C C   . VAL B 151 ? 0.2071 0.2435 0.2786 -0.0080 -0.0195 -0.0327 144 VAL B C   
2568 O O   . VAL B 151 ? 0.2112 0.2505 0.2850 -0.0042 -0.0226 -0.0347 144 VAL B O   
2569 C CB  . VAL B 151 ? 0.1931 0.2234 0.2509 -0.0094 -0.0125 -0.0294 144 VAL B CB  
2570 C CG1 . VAL B 151 ? 0.2118 0.2523 0.2777 -0.0081 -0.0062 -0.0282 144 VAL B CG1 
2571 C CG2 . VAL B 151 ? 0.2107 0.2332 0.2584 -0.0127 -0.0104 -0.0283 144 VAL B CG2 
2572 N N   . ASP B 152 ? 0.1776 0.2190 0.2569 -0.0097 -0.0175 -0.0329 145 ASP B N   
2573 C CA  . ASP B 152 ? 0.1789 0.2297 0.2702 -0.0077 -0.0187 -0.0359 145 ASP B CA  
2574 C C   . ASP B 152 ? 0.1654 0.2262 0.2625 -0.0041 -0.0150 -0.0362 145 ASP B C   
2575 O O   . ASP B 152 ? 0.1867 0.2502 0.2821 -0.0042 -0.0085 -0.0334 145 ASP B O   
2576 C CB  . ASP B 152 ? 0.2016 0.2563 0.3003 -0.0111 -0.0148 -0.0356 145 ASP B CB  
2577 C CG  . ASP B 152 ? 0.3583 0.4208 0.4689 -0.0101 -0.0176 -0.0399 145 ASP B CG  
2578 O OD1 . ASP B 152 ? 0.3834 0.4422 0.4934 -0.0091 -0.0253 -0.0432 145 ASP B OD1 
2579 O OD2 . ASP B 152 ? 0.3675 0.4399 0.4879 -0.0103 -0.0121 -0.0403 145 ASP B OD2 
2580 N N   . GLY B 153 ? 0.1836 0.2500 0.2871 -0.0006 -0.0196 -0.0401 146 GLY B N   
2581 C CA  . GLY B 153 ? 0.1746 0.2527 0.2857 0.0028  -0.0161 -0.0414 146 GLY B CA  
2582 C C   . GLY B 153 ? 0.1883 0.2655 0.2935 0.0062  -0.0163 -0.0409 146 GLY B C   
2583 O O   . GLY B 153 ? 0.2102 0.2920 0.3193 0.0103  -0.0201 -0.0443 146 GLY B O   
2584 N N   . ASN B 154 ? 0.1650 0.2368 0.2615 0.0048  -0.0123 -0.0372 147 ASN B N   
2585 C CA  . ASN B 154 ? 0.1632 0.2361 0.2556 0.0081  -0.0111 -0.0372 147 ASN B CA  
2586 C C   . ASN B 154 ? 0.1675 0.2294 0.2509 0.0082  -0.0165 -0.0379 147 ASN B C   
2587 O O   . ASN B 154 ? 0.2331 0.2966 0.3155 0.0115  -0.0175 -0.0395 147 ASN B O   
2588 C CB  . ASN B 154 ? 0.1770 0.2530 0.2665 0.0077  -0.0032 -0.0339 147 ASN B CB  
2589 C CG  . ASN B 154 ? 0.1707 0.2584 0.2686 0.0088  0.0025  -0.0333 147 ASN B CG  
2590 O OD1 . ASN B 154 ? 0.1802 0.2765 0.2865 0.0111  0.0010  -0.0364 147 ASN B OD1 
2591 N ND2 . ASN B 154 ? 0.1937 0.2815 0.2891 0.0071  0.0091  -0.0295 147 ASN B ND2 
2592 N N   . HIS B 155 ? 0.1873 0.2381 0.2639 0.0045  -0.0198 -0.0368 148 HIS B N   
2593 C CA  . HIS B 155 ? 0.2000 0.2389 0.2671 0.0039  -0.0249 -0.0371 148 HIS B CA  
2594 C C   . HIS B 155 ? 0.1566 0.1933 0.2174 0.0040  -0.0213 -0.0365 148 HIS B C   
2595 O O   . HIS B 155 ? 0.1876 0.2194 0.2448 0.0054  -0.0246 -0.0381 148 HIS B O   
2596 C CB  . HIS B 155 ? 0.2046 0.2418 0.2742 0.0074  -0.0327 -0.0404 148 HIS B CB  
2597 C CG  . HIS B 155 ? 0.2351 0.2765 0.3126 0.0083  -0.0367 -0.0425 148 HIS B CG  
2598 N ND1 . HIS B 155 ? 0.2907 0.3300 0.3682 0.0048  -0.0365 -0.0413 148 HIS B ND1 
2599 C CD2 . HIS B 155 ? 0.2870 0.3356 0.3736 0.0125  -0.0412 -0.0465 148 HIS B CD2 
2600 C CE1 . HIS B 155 ? 0.2868 0.3319 0.3732 0.0068  -0.0405 -0.0447 148 HIS B CE1 
2601 N NE2 . HIS B 155 ? 0.2725 0.3233 0.3645 0.0114  -0.0435 -0.0479 148 HIS B NE2 
2602 N N   . ASN B 156 ? 0.1390 0.1791 0.1988 0.0025  -0.0147 -0.0346 149 ASN B N   
2603 C CA  . ASN B 156 ? 0.1400 0.1777 0.1935 0.0022  -0.0115 -0.0346 149 ASN B CA  
2604 C C   . ASN B 156 ? 0.1499 0.1874 0.2006 -0.0008 -0.0060 -0.0323 149 ASN B C   
2605 O O   . ASN B 156 ? 0.1304 0.1704 0.1848 -0.0021 -0.0043 -0.0304 149 ASN B O   
2606 C CB  . ASN B 156 ? 0.1415 0.1885 0.1998 0.0074  -0.0098 -0.0369 149 ASN B CB  
2607 C CG  . ASN B 156 ? 0.1260 0.1852 0.1921 0.0104  -0.0056 -0.0361 149 ASN B CG  
2608 O OD1 . ASN B 156 ? 0.1400 0.2009 0.2051 0.0090  -0.0006 -0.0336 149 ASN B OD1 
2609 N ND2 . ASN B 156 ? 0.1423 0.2099 0.2159 0.0145  -0.0075 -0.0384 149 ASN B ND2 
2610 N N   . PHE B 157 ? 0.1406 0.1747 0.1850 -0.0020 -0.0035 -0.0329 150 PHE B N   
2611 C CA  . PHE B 157 ? 0.1344 0.1679 0.1756 -0.0044 0.0012  -0.0316 150 PHE B CA  
2612 C C   . PHE B 157 ? 0.1494 0.1837 0.1866 -0.0033 0.0040  -0.0339 150 PHE B C   
2613 O O   . PHE B 157 ? 0.1552 0.1873 0.1905 -0.0027 0.0021  -0.0365 150 PHE B O   
2614 C CB  . PHE B 157 ? 0.1674 0.1916 0.2033 -0.0100 -0.0005 -0.0304 150 PHE B CB  
2615 C CG  . PHE B 157 ? 0.1776 0.1920 0.2049 -0.0135 -0.0032 -0.0319 150 PHE B CG  
2616 C CD1 . PHE B 157 ? 0.1782 0.1893 0.1993 -0.0164 -0.0001 -0.0333 150 PHE B CD1 
2617 C CD2 . PHE B 157 ? 0.2488 0.2567 0.2738 -0.0141 -0.0088 -0.0320 150 PHE B CD2 
2618 C CE1 . PHE B 157 ? 0.2080 0.2098 0.2208 -0.0204 -0.0018 -0.0347 150 PHE B CE1 
2619 C CE2 . PHE B 157 ? 0.2756 0.2727 0.2912 -0.0177 -0.0109 -0.0327 150 PHE B CE2 
2620 C CZ  . PHE B 157 ? 0.2490 0.2431 0.2585 -0.0213 -0.0071 -0.0340 150 PHE B CZ  
2621 N N   . PHE B 158 ? 0.1532 0.1904 0.1896 -0.0029 0.0085  -0.0334 151 PHE B N   
2622 C CA  . PHE B 158 ? 0.1706 0.2091 0.2035 -0.0017 0.0110  -0.0366 151 PHE B CA  
2623 C C   . PHE B 158 ? 0.1639 0.1939 0.1900 -0.0074 0.0108  -0.0383 151 PHE B C   
2624 O O   . PHE B 158 ? 0.2025 0.2284 0.2264 -0.0111 0.0113  -0.0366 151 PHE B O   
2625 C CB  . PHE B 158 ? 0.1743 0.2198 0.2088 0.0022  0.0154  -0.0358 151 PHE B CB  
2626 C CG  . PHE B 158 ? 0.1410 0.1955 0.1808 0.0080  0.0164  -0.0347 151 PHE B CG  
2627 C CD1 . PHE B 158 ? 0.1688 0.2298 0.2098 0.0130  0.0168  -0.0379 151 PHE B CD1 
2628 C CD2 . PHE B 158 ? 0.1868 0.2437 0.2307 0.0083  0.0173  -0.0307 151 PHE B CD2 
2629 C CE1 . PHE B 158 ? 0.1698 0.2399 0.2153 0.0185  0.0179  -0.0371 151 PHE B CE1 
2630 C CE2 . PHE B 158 ? 0.1953 0.2610 0.2438 0.0132  0.0189  -0.0298 151 PHE B CE2 
2631 C CZ  . PHE B 158 ? 0.1930 0.2653 0.2419 0.0184  0.0192  -0.0328 151 PHE B CZ  
2632 N N   . GLY B 159 ? 0.1684 0.1957 0.1913 -0.0085 0.0102  -0.0420 152 GLY B N   
2633 C CA  . GLY B 159 ? 0.1805 0.2009 0.1967 -0.0140 0.0112  -0.0445 152 GLY B CA  
2634 C C   . GLY B 159 ? 0.1712 0.1972 0.1879 -0.0119 0.0146  -0.0495 152 GLY B C   
2635 O O   . GLY B 159 ? 0.1814 0.2114 0.2008 -0.0085 0.0144  -0.0523 152 GLY B O   
2636 N N   . ASN B 160 ? 0.1686 0.2233 0.2109 0.0247  -0.0089 -0.0785 153 ASN B N   
2637 C CA  . ASN B 160 ? 0.1681 0.2217 0.2145 0.0226  0.0005  -0.0740 153 ASN B CA  
2638 C C   . ASN B 160 ? 0.1765 0.2331 0.2409 0.0178  0.0037  -0.0621 153 ASN B C   
2639 O O   . ASN B 160 ? 0.1593 0.2161 0.2185 0.0162  0.0127  -0.0535 153 ASN B O   
2640 C CB  . ASN B 160 ? 0.1782 0.2298 0.1990 0.0252  0.0096  -0.0723 153 ASN B CB  
2641 C CG  . ASN B 160 ? 0.1859 0.2338 0.1887 0.0294  0.0076  -0.0843 153 ASN B CG  
2642 O OD1 . ASN B 160 ? 0.2010 0.2471 0.2128 0.0299  0.0021  -0.0942 153 ASN B OD1 
2643 N ND2 . ASN B 160 ? 0.2655 0.3121 0.2424 0.0323  0.0120  -0.0835 153 ASN B ND2 
2644 N N   . ASP B 161 ? 0.1482 0.2069 0.2332 0.0153  -0.0036 -0.0617 154 ASP B N   
2645 C CA  . ASP B 161 ? 0.1216 0.1827 0.2262 0.0101  -0.0020 -0.0517 154 ASP B CA  
2646 C C   . ASP B 161 ? 0.1521 0.2161 0.2487 0.0092  0.0016  -0.0410 154 ASP B C   
2647 O O   . ASP B 161 ? 0.1580 0.2237 0.2692 0.0045  0.0040  -0.0321 154 ASP B O   
2648 C CB  . ASP B 161 ? 0.1497 0.2092 0.2659 0.0067  0.0047  -0.0477 154 ASP B CB  
2649 C CG  . ASP B 161 ? 0.2702 0.3274 0.4022 0.0064  0.0001  -0.0570 154 ASP B CG  
2650 O OD1 . ASP B 161 ? 0.2967 0.3538 0.4351 0.0078  -0.0088 -0.0655 154 ASP B OD1 
2651 O OD2 . ASP B 161 ? 0.3361 0.3914 0.4745 0.0047  0.0054  -0.0554 154 ASP B OD2 
2652 N N   . ILE B 162 ? 0.1387 0.2029 0.2132 0.0131  0.0019  -0.0417 155 ILE B N   
2653 C CA  . ILE B 162 ? 0.1289 0.1956 0.1948 0.0126  0.0055  -0.0318 155 ILE B CA  
2654 C C   . ILE B 162 ? 0.1259 0.1949 0.1925 0.0146  -0.0039 -0.0349 155 ILE B C   
2655 O O   . ILE B 162 ? 0.1381 0.2058 0.1944 0.0186  -0.0103 -0.0442 155 ILE B O   
2656 C CB  . ILE B 162 ? 0.1313 0.1965 0.1704 0.0155  0.0138  -0.0293 155 ILE B CB  
2657 C CG1 . ILE B 162 ? 0.1647 0.2281 0.2044 0.0131  0.0236  -0.0251 155 ILE B CG1 
2658 C CG2 . ILE B 162 ? 0.1604 0.2279 0.1887 0.0159  0.0163  -0.0206 155 ILE B CG2 
2659 C CD1 . ILE B 162 ? 0.2290 0.2904 0.2429 0.0161  0.0317  -0.0244 155 ILE B CD1 
2660 N N   . LEU B 163 ? 0.1286 0.2008 0.2068 0.0117  -0.0049 -0.0272 156 LEU B N   
2661 C CA  . LEU B 163 ? 0.1095 0.1842 0.1921 0.0132  -0.0144 -0.0300 156 LEU B CA  
2662 C C   . LEU B 163 ? 0.1232 0.1982 0.1817 0.0177  -0.0144 -0.0293 156 LEU B C   
2663 O O   . LEU B 163 ? 0.1472 0.2228 0.1949 0.0173  -0.0067 -0.0203 156 LEU B O   
2664 C CB  . LEU B 163 ? 0.1140 0.1922 0.2184 0.0084  -0.0151 -0.0222 156 LEU B CB  
2665 C CG  . LEU B 163 ? 0.1088 0.1898 0.2254 0.0091  -0.0261 -0.0265 156 LEU B CG  
2666 C CD1 . LEU B 163 ? 0.1410 0.2209 0.2729 0.0088  -0.0343 -0.0367 156 LEU B CD1 
2667 C CD2 . LEU B 163 ? 0.1139 0.1983 0.2477 0.0045  -0.0246 -0.0171 156 LEU B CD2 
2668 N N   . VAL B 164 ? 0.1302 0.2045 0.1803 0.0218  -0.0231 -0.0385 157 VAL B N   
2669 C CA  . VAL B 164 ? 0.1593 0.2334 0.1869 0.0261  -0.0248 -0.0386 157 VAL B CA  
2670 C C   . VAL B 164 ? 0.1402 0.2172 0.1771 0.0271  -0.0361 -0.0413 157 VAL B C   
2671 O O   . VAL B 164 ? 0.1524 0.2306 0.2089 0.0255  -0.0436 -0.0467 157 VAL B O   
2672 C CB  . VAL B 164 ? 0.1776 0.2473 0.1813 0.0304  -0.0244 -0.0469 157 VAL B CB  
2673 C CG1 . VAL B 164 ? 0.2026 0.2698 0.1971 0.0295  -0.0128 -0.0437 157 VAL B CG1 
2674 C CG2 . VAL B 164 ? 0.2171 0.2852 0.2278 0.0314  -0.0335 -0.0592 157 VAL B CG2 
2675 N N   . HIS B 165 ? 0.1595 0.2376 0.1823 0.0299  -0.0374 -0.0376 158 HIS B N   
2676 C CA  . HIS B 165 ? 0.1691 0.2500 0.1991 0.0313  -0.0483 -0.0402 158 HIS B CA  
2677 C C   . HIS B 165 ? 0.1766 0.2550 0.1979 0.0347  -0.0579 -0.0525 158 HIS B C   
2678 O O   . HIS B 165 ? 0.2395 0.3137 0.2399 0.0374  -0.0554 -0.0576 158 HIS B O   
2679 C CB  . HIS B 165 ? 0.2577 0.3401 0.2740 0.0335  -0.0468 -0.0328 158 HIS B CB  
2680 C CG  . HIS B 165 ? 0.2811 0.3674 0.3094 0.0341  -0.0567 -0.0326 158 HIS B CG  
2681 N ND1 . HIS B 165 ? 0.2679 0.3584 0.3227 0.0302  -0.0585 -0.0286 158 HIS B ND1 
2682 C CD2 . HIS B 165 ? 0.3913 0.4779 0.4087 0.0380  -0.0655 -0.0361 158 HIS B CD2 
2683 C CE1 . HIS B 165 ? 0.2927 0.3862 0.3531 0.0318  -0.0678 -0.0297 158 HIS B CE1 
2684 N NE2 . HIS B 165 ? 0.3729 0.4641 0.4111 0.0366  -0.0724 -0.0341 158 HIS B NE2 
2685 N N   . ALA B 166 ? 0.1723 0.2531 0.2101 0.0343  -0.0687 -0.0577 159 ALA B N   
2686 C CA  . ALA B 166 ? 0.2109 0.2895 0.2416 0.0371  -0.0787 -0.0693 159 ALA B CA  
2687 C C   . ALA B 166 ? 0.2709 0.3502 0.2870 0.0408  -0.0859 -0.0693 159 ALA B C   
2688 O O   . ALA B 166 ? 0.3654 0.4479 0.3829 0.0409  -0.0846 -0.0607 159 ALA B O   
2689 C CB  . ALA B 166 ? 0.2264 0.3069 0.2832 0.0345  -0.0866 -0.0755 159 ALA B CB  
2690 N N   . SER B 167 ? 0.3222 0.3986 0.3244 0.0438  -0.0936 -0.0790 160 SER B N   
2691 C CA  . SER B 167 ? 0.3728 0.4500 0.3639 0.0470  -0.1022 -0.0793 160 SER B CA  
2692 C C   . SER B 167 ? 0.3274 0.4087 0.3417 0.0457  -0.1138 -0.0826 160 SER B C   
2693 O O   . SER B 167 ? 0.4311 0.5133 0.4647 0.0431  -0.1165 -0.0878 160 SER B O   
2694 C CB  . SER B 167 ? 0.5440 0.6156 0.5078 0.0506  -0.1057 -0.0879 160 SER B CB  
2695 O OG  . SER B 167 ? 0.6644 0.7355 0.6341 0.0508  -0.1174 -0.0984 160 SER B OG  
2696 N N   . VAL B 168 ? 0.4481 0.5321 0.4604 0.0477  -0.1209 -0.0799 161 VAL B N   
2697 C CA  . VAL B 168 ? 0.4669 0.5541 0.4958 0.0475  -0.1338 -0.0852 161 VAL B CA  
2698 C C   . VAL B 168 ? 0.4507 0.5337 0.4575 0.0509  -0.1413 -0.0909 161 VAL B C   
2699 O O   . VAL B 168 ? 0.4562 0.5368 0.4410 0.0536  -0.1385 -0.0865 161 VAL B O   
2700 C CB  . VAL B 168 ? 0.4903 0.5838 0.5400 0.0460  -0.1357 -0.0768 161 VAL B CB  
2701 C CG1 . VAL B 168 ? 0.5421 0.6357 0.6069 0.0448  -0.1451 -0.0806 161 VAL B CG1 
2702 C CG2 . VAL B 168 ? 0.4830 0.5788 0.5533 0.0416  -0.1260 -0.0701 161 VAL B CG2 
2703 N N   . TYR B 169 ? 0.4809 0.5611 0.4924 0.0501  -0.1480 -0.0994 162 TYR B N   
2704 C CA  . TYR B 169 ? 0.5150 0.5906 0.5100 0.0520  -0.1543 -0.1033 162 TYR B CA  
2705 C C   . TYR B 169 ? 0.6198 0.6993 0.6330 0.0511  -0.1619 -0.1001 162 TYR B C   
2706 O O   . TYR B 169 ? 0.6928 0.7748 0.7291 0.0485  -0.1653 -0.1027 162 TYR B O   
2707 C CB  . TYR B 169 ? 0.4002 0.4708 0.3913 0.0514  -0.1572 -0.1142 162 TYR B CB  
2708 C CG  . TYR B 169 ? 0.4965 0.5627 0.4725 0.0526  -0.1641 -0.1183 162 TYR B CG  
2709 C CD1 . TYR B 169 ? 0.5239 0.5918 0.5138 0.0518  -0.1735 -0.1204 162 TYR B CD1 
2710 C CD2 . TYR B 169 ? 0.5565 0.6164 0.5044 0.0543  -0.1606 -0.1195 162 TYR B CD2 
2711 C CE1 . TYR B 169 ? 0.5493 0.6134 0.5251 0.0527  -0.1800 -0.1240 162 TYR B CE1 
2712 C CE2 . TYR B 169 ? 0.5414 0.5972 0.4757 0.0548  -0.1665 -0.1227 162 TYR B CE2 
2713 C CZ  . TYR B 169 ? 0.4908 0.5489 0.4389 0.0541  -0.1767 -0.1251 162 TYR B CZ  
2714 O OH  . TYR B 169 ? 0.5777 0.6318 0.5118 0.0544  -0.1829 -0.1283 162 TYR B OH  
2715 N N   . LEU B 170 ? 0.5157 0.5957 0.5192 0.0530  -0.1636 -0.0940 163 LEU B N   
2716 C CA  . LEU B 170 ? 0.5618 0.6451 0.5809 0.0523  -0.1708 -0.0914 163 LEU B CA  
2717 C C   . LEU B 170 ? 0.6630 0.7421 0.6718 0.0531  -0.1793 -0.0989 163 LEU B C   
2718 O O   . LEU B 170 ? 0.7109 0.7855 0.6958 0.0552  -0.1799 -0.0994 163 LEU B O   
2719 C CB  . LEU B 170 ? 0.6178 0.7038 0.6330 0.0537  -0.1689 -0.0814 163 LEU B CB  
2720 C CG  . LEU B 170 ? 0.6617 0.7534 0.7029 0.0517  -0.1716 -0.0762 163 LEU B CG  
2721 C CD1 . LEU B 170 ? 0.6660 0.7602 0.7324 0.0480  -0.1698 -0.0787 163 LEU B CD1 
2722 C CD2 . LEU B 170 ? 0.6751 0.7704 0.7167 0.0523  -0.1659 -0.0654 163 LEU B CD2 
2723 N N   . ASN B 171 ? 0.6778 0.7578 0.7045 0.0511  -0.1850 -0.1045 164 ASN B N   
2724 C CA  . ASN B 171 ? 0.7227 0.7993 0.7423 0.0514  -0.1935 -0.1116 164 ASN B CA  
2725 C C   . ASN B 171 ? 0.6830 0.7618 0.7034 0.0524  -0.1998 -0.1067 164 ASN B C   
2726 O O   . ASN B 171 ? 0.7361 0.8184 0.7762 0.0511  -0.2050 -0.1062 164 ASN B O   
2727 C CB  . ASN B 171 ? 0.7396 0.8166 0.7786 0.0490  -0.1969 -0.1188 164 ASN B CB  
2728 C CG  . ASN B 171 ? 0.7546 0.8283 0.7865 0.0492  -0.2055 -0.1261 164 ASN B CG  
2729 O OD1 . ASN B 171 ? 0.7122 0.7821 0.7218 0.0509  -0.2079 -0.1272 164 ASN B OD1 
2730 N ND2 . ASN B 171 ? 0.7687 0.8434 0.8193 0.0471  -0.2098 -0.1310 164 ASN B ND2 
2731 N N   . LYS B 172 ? 0.5944 0.6708 0.5928 0.0548  -0.1987 -0.1027 165 LYS B N   
2732 C CA  . LYS B 172 ? 0.5555 0.6342 0.5541 0.0559  -0.2036 -0.0968 165 LYS B CA  
2733 C C   . LYS B 172 ? 0.4805 0.5577 0.4788 0.0557  -0.2140 -0.1023 165 LYS B C   
2734 O O   . LYS B 172 ? 0.4576 0.5389 0.4726 0.0551  -0.2198 -0.1003 165 LYS B O   
2735 C CB  . LYS B 172 ? 0.5155 0.5912 0.4899 0.0582  -0.1990 -0.0910 165 LYS B CB  
2736 C CG  . LYS B 172 ? 0.5406 0.6179 0.5141 0.0586  -0.1886 -0.0845 165 LYS B CG  
2737 C CD  . LYS B 172 ? 0.5787 0.6525 0.5280 0.0607  -0.1840 -0.0785 165 LYS B CD  
2738 C CE  . LYS B 172 ? 0.6163 0.6911 0.5624 0.0610  -0.1730 -0.0722 165 LYS B CE  
2739 N NZ  . LYS B 172 ? 0.6527 0.7230 0.5739 0.0626  -0.1672 -0.0668 165 LYS B NZ  
2740 N N   . LEU B 173 ? 0.5936 0.6650 0.5733 0.0559  -0.2161 -0.1093 166 LEU B N   
2741 C CA  . LEU B 173 ? 0.5996 0.6691 0.5746 0.0557  -0.2258 -0.1139 166 LEU B CA  
2742 C C   . LEU B 173 ? 0.6597 0.7260 0.6353 0.0540  -0.2290 -0.1241 166 LEU B C   
2743 O O   . LEU B 173 ? 0.6573 0.7240 0.6438 0.0528  -0.2247 -0.1278 166 LEU B O   
2744 C CB  . LEU B 173 ? 0.6650 0.7302 0.6138 0.0573  -0.2268 -0.1111 166 LEU B CB  
2745 C CG  . LEU B 173 ? 0.6553 0.7236 0.6036 0.0590  -0.2246 -0.1010 166 LEU B CG  
2746 C CD1 . LEU B 173 ? 0.7243 0.7876 0.6456 0.0602  -0.2238 -0.0981 166 LEU B CD1 
2747 C CD2 . LEU B 173 ? 0.6184 0.6926 0.5882 0.0588  -0.2321 -0.0980 166 LEU B CD2 
# 
