data_8Y26
# 
_entry.id   8Y26 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8Y26         pdb_00008y26 10.2210/pdb8y26/pdb 
WWPDB D_1300040392 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_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                        8Y26 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8XG4 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ssugiyama@kochi-u.ac.jp 
_pdbx_contact_author.name_first         Shigeru 
_pdbx_contact_author.name_last          Sugiyama 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0563-6799 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Higashiura, A.' 1 ? 
'Yamamoto, A.'   2 ? 
'Sugiyama, S.'   3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Binding competition between substrates and cryoprotectants in protein crystals directly observed by a hybrid method of in-gel crystallization and high-pressure cryo-cooling in X-ray crystallography
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Higashiura, A.' 1 ? 
primary 'Sugiyama, S.'   2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat Streptavidin                                                                          12764.833 4   ? ? ? ? 
2 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                  78.133    4   ? ? ? ? 
3 non-polymer syn 'dimethyl 5-(4-oxidanylidene-5~{H}-furo[3,2-c]pyridin-2-yl)benzene-1,3-dicarboxylate' 327.288   2   ? ? ? ? 
4 water       nat water                                                                                 18.015    747 ? ? ? ? 
# 
_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       
;AGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSG
QYVGGAEARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSG
QYVGGAEARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKP
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIMETHYL SULFOXIDE'                                                                  DMS   
3 'dimethyl 5-(4-oxidanylidene-5~{H}-furo[3,2-c]pyridin-2-yl)benzene-1,3-dicarboxylate' A1LXQ 
4 water                                                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   GLY n 
1 3   ILE n 
1 4   THR n 
1 5   GLY n 
1 6   THR n 
1 7   TRP n 
1 8   TYR n 
1 9   ASN n 
1 10  GLN n 
1 11  LEU n 
1 12  GLY n 
1 13  SER n 
1 14  THR n 
1 15  PHE n 
1 16  ILE n 
1 17  VAL n 
1 18  THR n 
1 19  ALA n 
1 20  GLY n 
1 21  ALA n 
1 22  ASP n 
1 23  GLY n 
1 24  ALA n 
1 25  LEU n 
1 26  THR n 
1 27  GLY n 
1 28  THR n 
1 29  TYR n 
1 30  GLU n 
1 31  SER n 
1 32  ALA n 
1 33  VAL n 
1 34  GLY n 
1 35  ASN n 
1 36  ALA n 
1 37  GLU n 
1 38  SER n 
1 39  ARG n 
1 40  TYR n 
1 41  VAL n 
1 42  LEU n 
1 43  THR n 
1 44  GLY n 
1 45  ARG n 
1 46  TYR n 
1 47  ASP n 
1 48  SER n 
1 49  ALA n 
1 50  PRO n 
1 51  ALA n 
1 52  THR n 
1 53  ASP n 
1 54  GLY n 
1 55  SER n 
1 56  GLY n 
1 57  THR n 
1 58  ALA n 
1 59  LEU n 
1 60  GLY n 
1 61  TRP n 
1 62  THR n 
1 63  VAL n 
1 64  ALA n 
1 65  TRP n 
1 66  LYS n 
1 67  ASN n 
1 68  ASN n 
1 69  TYR n 
1 70  ARG n 
1 71  ASN n 
1 72  ALA n 
1 73  HIS n 
1 74  SER n 
1 75  ALA n 
1 76  THR n 
1 77  THR n 
1 78  TRP n 
1 79  SER n 
1 80  GLY n 
1 81  GLN n 
1 82  TYR n 
1 83  VAL n 
1 84  GLY n 
1 85  GLY n 
1 86  ALA n 
1 87  GLU n 
1 88  ALA n 
1 89  ARG n 
1 90  ILE n 
1 91  ASN n 
1 92  THR n 
1 93  GLN n 
1 94  TRP n 
1 95  LEU n 
1 96  LEU n 
1 97  THR n 
1 98  SER n 
1 99  GLY n 
1 100 THR n 
1 101 THR n 
1 102 GLU n 
1 103 ALA n 
1 104 ASN n 
1 105 ALA n 
1 106 TRP n 
1 107 LYS n 
1 108 SER n 
1 109 THR n 
1 110 LEU n 
1 111 VAL n 
1 112 GLY n 
1 113 HIS n 
1 114 ASP n 
1 115 THR n 
1 116 PHE n 
1 117 THR n 
1 118 LYS n 
1 119 VAL n 
1 120 LYS n 
1 121 PRO n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           121 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Streptomyces avidinii' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      1895 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
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 
A1LXQ non-polymer         . 'dimethyl 5-(4-oxidanylidene-5~{H}-furo[3,2-c]pyridin-2-yl)benzene-1,3-dicarboxylate' ? 'C17 H13 N O6' 
327.288 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                  ? 'C2 H6 O S' 
78.133  
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 
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   ALA 1   15  15  ALA ALA A . n 
A 1 2   GLY 2   16  16  GLY GLY A . n 
A 1 3   ILE 3   17  17  ILE ILE A . n 
A 1 4   THR 4   18  18  THR THR A . n 
A 1 5   GLY 5   19  19  GLY GLY A . n 
A 1 6   THR 6   20  20  THR THR A . n 
A 1 7   TRP 7   21  21  TRP TRP A . n 
A 1 8   TYR 8   22  22  TYR TYR A . n 
A 1 9   ASN 9   23  23  ASN ASN A . n 
A 1 10  GLN 10  24  24  GLN GLN A . n 
A 1 11  LEU 11  25  25  LEU LEU A . n 
A 1 12  GLY 12  26  26  GLY GLY A . n 
A 1 13  SER 13  27  27  SER SER A . n 
A 1 14  THR 14  28  28  THR THR A . n 
A 1 15  PHE 15  29  29  PHE PHE A . n 
A 1 16  ILE 16  30  30  ILE ILE A . n 
A 1 17  VAL 17  31  31  VAL VAL A . n 
A 1 18  THR 18  32  32  THR THR A . n 
A 1 19  ALA 19  33  33  ALA ALA A . n 
A 1 20  GLY 20  34  34  GLY GLY A . n 
A 1 21  ALA 21  35  35  ALA ALA A . n 
A 1 22  ASP 22  36  36  ASP ASP A . n 
A 1 23  GLY 23  37  37  GLY GLY A . n 
A 1 24  ALA 24  38  38  ALA ALA A . n 
A 1 25  LEU 25  39  39  LEU LEU A . n 
A 1 26  THR 26  40  40  THR THR A . n 
A 1 27  GLY 27  41  41  GLY GLY A . n 
A 1 28  THR 28  42  42  THR THR A . n 
A 1 29  TYR 29  43  43  TYR TYR A . n 
A 1 30  GLU 30  44  44  GLU GLU A . n 
A 1 31  SER 31  45  45  SER SER A . n 
A 1 32  ALA 32  46  46  ALA ALA A . n 
A 1 33  VAL 33  47  47  VAL VAL A . n 
A 1 34  GLY 34  48  48  GLY GLY A . n 
A 1 35  ASN 35  49  49  ASN ASN A . n 
A 1 36  ALA 36  50  50  ALA ALA A . n 
A 1 37  GLU 37  51  51  GLU GLU A . n 
A 1 38  SER 38  52  52  SER SER A . n 
A 1 39  ARG 39  53  53  ARG ARG A . n 
A 1 40  TYR 40  54  54  TYR TYR A . n 
A 1 41  VAL 41  55  55  VAL VAL A . n 
A 1 42  LEU 42  56  56  LEU LEU A . n 
A 1 43  THR 43  57  57  THR THR A . n 
A 1 44  GLY 44  58  58  GLY GLY A . n 
A 1 45  ARG 45  59  59  ARG ARG A . n 
A 1 46  TYR 46  60  60  TYR TYR A . n 
A 1 47  ASP 47  61  61  ASP ASP A . n 
A 1 48  SER 48  62  62  SER SER A . n 
A 1 49  ALA 49  63  63  ALA ALA A . n 
A 1 50  PRO 50  64  64  PRO PRO A . n 
A 1 51  ALA 51  65  65  ALA ALA A . n 
A 1 52  THR 52  66  66  THR THR A . n 
A 1 53  ASP 53  67  67  ASP ASP A . n 
A 1 54  GLY 54  68  68  GLY GLY A . n 
A 1 55  SER 55  69  69  SER SER A . n 
A 1 56  GLY 56  70  70  GLY GLY A . n 
A 1 57  THR 57  71  71  THR THR A . n 
A 1 58  ALA 58  72  72  ALA ALA A . n 
A 1 59  LEU 59  73  73  LEU LEU A . n 
A 1 60  GLY 60  74  74  GLY GLY A . n 
A 1 61  TRP 61  75  75  TRP TRP A . n 
A 1 62  THR 62  76  76  THR THR A . n 
A 1 63  VAL 63  77  77  VAL VAL A . n 
A 1 64  ALA 64  78  78  ALA ALA A . n 
A 1 65  TRP 65  79  79  TRP TRP A . n 
A 1 66  LYS 66  80  80  LYS LYS A . n 
A 1 67  ASN 67  81  81  ASN ASN A . n 
A 1 68  ASN 68  82  82  ASN ASN A . n 
A 1 69  TYR 69  83  83  TYR TYR A . n 
A 1 70  ARG 70  84  84  ARG ARG A . n 
A 1 71  ASN 71  85  85  ASN ASN A . n 
A 1 72  ALA 72  86  86  ALA ALA A . n 
A 1 73  HIS 73  87  87  HIS HIS A . n 
A 1 74  SER 74  88  88  SER SER A . n 
A 1 75  ALA 75  89  89  ALA ALA A . n 
A 1 76  THR 76  90  90  THR THR A . n 
A 1 77  THR 77  91  91  THR THR A . n 
A 1 78  TRP 78  92  92  TRP TRP A . n 
A 1 79  SER 79  93  93  SER SER A . n 
A 1 80  GLY 80  94  94  GLY GLY A . n 
A 1 81  GLN 81  95  95  GLN GLN A . n 
A 1 82  TYR 82  96  96  TYR TYR A . n 
A 1 83  VAL 83  97  97  VAL VAL A . n 
A 1 84  GLY 84  98  98  GLY GLY A . n 
A 1 85  GLY 85  99  99  GLY GLY A . n 
A 1 86  ALA 86  100 100 ALA ALA A . n 
A 1 87  GLU 87  101 101 GLU GLU A . n 
A 1 88  ALA 88  102 102 ALA ALA A . n 
A 1 89  ARG 89  103 103 ARG ARG A . n 
A 1 90  ILE 90  104 104 ILE ILE A . n 
A 1 91  ASN 91  105 105 ASN ASN A . n 
A 1 92  THR 92  106 106 THR THR A . n 
A 1 93  GLN 93  107 107 GLN GLN A . n 
A 1 94  TRP 94  108 108 TRP TRP A . n 
A 1 95  LEU 95  109 109 LEU LEU A . n 
A 1 96  LEU 96  110 110 LEU LEU A . n 
A 1 97  THR 97  111 111 THR THR A . n 
A 1 98  SER 98  112 112 SER SER A . n 
A 1 99  GLY 99  113 113 GLY GLY A . n 
A 1 100 THR 100 114 114 THR THR A . n 
A 1 101 THR 101 115 115 THR THR A . n 
A 1 102 GLU 102 116 116 GLU GLU A . n 
A 1 103 ALA 103 117 117 ALA ALA A . n 
A 1 104 ASN 104 118 118 ASN ASN A . n 
A 1 105 ALA 105 119 119 ALA ALA A . n 
A 1 106 TRP 106 120 120 TRP TRP A . n 
A 1 107 LYS 107 121 121 LYS LYS A . n 
A 1 108 SER 108 122 122 SER SER A . n 
A 1 109 THR 109 123 123 THR THR A . n 
A 1 110 LEU 110 124 124 LEU LEU A . n 
A 1 111 VAL 111 125 125 VAL VAL A . n 
A 1 112 GLY 112 126 126 GLY GLY A . n 
A 1 113 HIS 113 127 127 HIS HIS A . n 
A 1 114 ASP 114 128 128 ASP ASP A . n 
A 1 115 THR 115 129 129 THR THR A . n 
A 1 116 PHE 116 130 130 PHE PHE A . n 
A 1 117 THR 117 131 131 THR THR A . n 
A 1 118 LYS 118 132 132 LYS LYS A . n 
A 1 119 VAL 119 133 133 VAL VAL A . n 
A 1 120 LYS 120 134 134 LYS LYS A . n 
A 1 121 PRO 121 135 135 PRO PRO A . n 
B 1 1   ALA 1   15  15  ALA ALA B . n 
B 1 2   GLY 2   16  16  GLY GLY B . n 
B 1 3   ILE 3   17  17  ILE ILE B . n 
B 1 4   THR 4   18  18  THR THR B . n 
B 1 5   GLY 5   19  19  GLY GLY B . n 
B 1 6   THR 6   20  20  THR THR B . n 
B 1 7   TRP 7   21  21  TRP TRP B . n 
B 1 8   TYR 8   22  22  TYR TYR B . n 
B 1 9   ASN 9   23  23  ASN ASN B . n 
B 1 10  GLN 10  24  24  GLN GLN B . n 
B 1 11  LEU 11  25  25  LEU LEU B . n 
B 1 12  GLY 12  26  26  GLY GLY B . n 
B 1 13  SER 13  27  27  SER SER B . n 
B 1 14  THR 14  28  28  THR THR B . n 
B 1 15  PHE 15  29  29  PHE PHE B . n 
B 1 16  ILE 16  30  30  ILE ILE B . n 
B 1 17  VAL 17  31  31  VAL VAL B . n 
B 1 18  THR 18  32  32  THR THR B . n 
B 1 19  ALA 19  33  33  ALA ALA B . n 
B 1 20  GLY 20  34  34  GLY GLY B . n 
B 1 21  ALA 21  35  35  ALA ALA B . n 
B 1 22  ASP 22  36  36  ASP ASP B . n 
B 1 23  GLY 23  37  37  GLY GLY B . n 
B 1 24  ALA 24  38  38  ALA ALA B . n 
B 1 25  LEU 25  39  39  LEU LEU B . n 
B 1 26  THR 26  40  40  THR THR B . n 
B 1 27  GLY 27  41  41  GLY GLY B . n 
B 1 28  THR 28  42  42  THR THR B . n 
B 1 29  TYR 29  43  43  TYR TYR B . n 
B 1 30  GLU 30  44  44  GLU GLU B . n 
B 1 31  SER 31  45  45  SER SER B . n 
B 1 32  ALA 32  46  ?   ?   ?   B . n 
B 1 33  VAL 33  47  ?   ?   ?   B . n 
B 1 34  GLY 34  48  ?   ?   ?   B . n 
B 1 35  ASN 35  49  49  ASN ASN B . n 
B 1 36  ALA 36  50  50  ALA ALA B . n 
B 1 37  GLU 37  51  51  GLU GLU B . n 
B 1 38  SER 38  52  52  SER SER B . n 
B 1 39  ARG 39  53  53  ARG ARG B . n 
B 1 40  TYR 40  54  54  TYR TYR B . n 
B 1 41  VAL 41  55  55  VAL VAL B . n 
B 1 42  LEU 42  56  56  LEU LEU B . n 
B 1 43  THR 43  57  57  THR THR B . n 
B 1 44  GLY 44  58  58  GLY GLY B . n 
B 1 45  ARG 45  59  59  ARG ARG B . n 
B 1 46  TYR 46  60  60  TYR TYR B . n 
B 1 47  ASP 47  61  61  ASP ASP B . n 
B 1 48  SER 48  62  62  SER SER B . n 
B 1 49  ALA 49  63  63  ALA ALA B . n 
B 1 50  PRO 50  64  64  PRO PRO B . n 
B 1 51  ALA 51  65  65  ALA ALA B . n 
B 1 52  THR 52  66  66  THR THR B . n 
B 1 53  ASP 53  67  67  ASP ASP B . n 
B 1 54  GLY 54  68  68  GLY GLY B . n 
B 1 55  SER 55  69  69  SER SER B . n 
B 1 56  GLY 56  70  70  GLY GLY B . n 
B 1 57  THR 57  71  71  THR THR B . n 
B 1 58  ALA 58  72  72  ALA ALA B . n 
B 1 59  LEU 59  73  73  LEU LEU B . n 
B 1 60  GLY 60  74  74  GLY GLY B . n 
B 1 61  TRP 61  75  75  TRP TRP B . n 
B 1 62  THR 62  76  76  THR THR B . n 
B 1 63  VAL 63  77  77  VAL VAL B . n 
B 1 64  ALA 64  78  78  ALA ALA B . n 
B 1 65  TRP 65  79  79  TRP TRP B . n 
B 1 66  LYS 66  80  80  LYS LYS B . n 
B 1 67  ASN 67  81  81  ASN ASN B . n 
B 1 68  ASN 68  82  82  ASN ASN B . n 
B 1 69  TYR 69  83  83  TYR TYR B . n 
B 1 70  ARG 70  84  84  ARG ARG B . n 
B 1 71  ASN 71  85  85  ASN ASN B . n 
B 1 72  ALA 72  86  86  ALA ALA B . n 
B 1 73  HIS 73  87  87  HIS HIS B . n 
B 1 74  SER 74  88  88  SER SER B . n 
B 1 75  ALA 75  89  89  ALA ALA B . n 
B 1 76  THR 76  90  90  THR THR B . n 
B 1 77  THR 77  91  91  THR THR B . n 
B 1 78  TRP 78  92  92  TRP TRP B . n 
B 1 79  SER 79  93  93  SER SER B . n 
B 1 80  GLY 80  94  94  GLY GLY B . n 
B 1 81  GLN 81  95  95  GLN GLN B . n 
B 1 82  TYR 82  96  96  TYR TYR B . n 
B 1 83  VAL 83  97  97  VAL VAL B . n 
B 1 84  GLY 84  98  98  GLY GLY B . n 
B 1 85  GLY 85  99  99  GLY GLY B . n 
B 1 86  ALA 86  100 100 ALA ALA B . n 
B 1 87  GLU 87  101 101 GLU GLU B . n 
B 1 88  ALA 88  102 102 ALA ALA B . n 
B 1 89  ARG 89  103 103 ARG ARG B . n 
B 1 90  ILE 90  104 104 ILE ILE B . n 
B 1 91  ASN 91  105 105 ASN ASN B . n 
B 1 92  THR 92  106 106 THR THR B . n 
B 1 93  GLN 93  107 107 GLN GLN B . n 
B 1 94  TRP 94  108 108 TRP TRP B . n 
B 1 95  LEU 95  109 109 LEU LEU B . n 
B 1 96  LEU 96  110 110 LEU LEU B . n 
B 1 97  THR 97  111 111 THR THR B . n 
B 1 98  SER 98  112 112 SER SER B . n 
B 1 99  GLY 99  113 113 GLY GLY B . n 
B 1 100 THR 100 114 114 THR THR B . n 
B 1 101 THR 101 115 115 THR THR B . n 
B 1 102 GLU 102 116 116 GLU GLU B . n 
B 1 103 ALA 103 117 117 ALA ALA B . n 
B 1 104 ASN 104 118 118 ASN ASN B . n 
B 1 105 ALA 105 119 119 ALA ALA B . n 
B 1 106 TRP 106 120 120 TRP TRP B . n 
B 1 107 LYS 107 121 121 LYS LYS B . n 
B 1 108 SER 108 122 122 SER SER B . n 
B 1 109 THR 109 123 123 THR THR B . n 
B 1 110 LEU 110 124 124 LEU LEU B . n 
B 1 111 VAL 111 125 125 VAL VAL B . n 
B 1 112 GLY 112 126 126 GLY GLY B . n 
B 1 113 HIS 113 127 127 HIS HIS B . n 
B 1 114 ASP 114 128 128 ASP ASP B . n 
B 1 115 THR 115 129 129 THR THR B . n 
B 1 116 PHE 116 130 130 PHE PHE B . n 
B 1 117 THR 117 131 131 THR THR B . n 
B 1 118 LYS 118 132 132 LYS LYS B . n 
B 1 119 VAL 119 133 133 VAL VAL B . n 
B 1 120 LYS 120 134 134 LYS LYS B . n 
B 1 121 PRO 121 135 ?   ?   ?   B . n 
C 1 1   ALA 1   15  ?   ?   ?   C . n 
C 1 2   GLY 2   16  16  GLY GLY C . n 
C 1 3   ILE 3   17  17  ILE ILE C . n 
C 1 4   THR 4   18  18  THR THR C . n 
C 1 5   GLY 5   19  19  GLY GLY C . n 
C 1 6   THR 6   20  20  THR THR C . n 
C 1 7   TRP 7   21  21  TRP TRP C . n 
C 1 8   TYR 8   22  22  TYR TYR C . n 
C 1 9   ASN 9   23  23  ASN ASN C . n 
C 1 10  GLN 10  24  24  GLN GLN C . n 
C 1 11  LEU 11  25  25  LEU LEU C . n 
C 1 12  GLY 12  26  26  GLY GLY C . n 
C 1 13  SER 13  27  27  SER SER C . n 
C 1 14  THR 14  28  28  THR THR C . n 
C 1 15  PHE 15  29  29  PHE PHE C . n 
C 1 16  ILE 16  30  30  ILE ILE C . n 
C 1 17  VAL 17  31  31  VAL VAL C . n 
C 1 18  THR 18  32  32  THR THR C . n 
C 1 19  ALA 19  33  33  ALA ALA C . n 
C 1 20  GLY 20  34  34  GLY GLY C . n 
C 1 21  ALA 21  35  35  ALA ALA C . n 
C 1 22  ASP 22  36  36  ASP ASP C . n 
C 1 23  GLY 23  37  37  GLY GLY C . n 
C 1 24  ALA 24  38  38  ALA ALA C . n 
C 1 25  LEU 25  39  39  LEU LEU C . n 
C 1 26  THR 26  40  40  THR THR C . n 
C 1 27  GLY 27  41  41  GLY GLY C . n 
C 1 28  THR 28  42  42  THR THR C . n 
C 1 29  TYR 29  43  43  TYR TYR C . n 
C 1 30  GLU 30  44  44  GLU GLU C . n 
C 1 31  SER 31  45  45  SER SER C . n 
C 1 32  ALA 32  46  46  ALA ALA C . n 
C 1 33  VAL 33  47  47  VAL VAL C . n 
C 1 34  GLY 34  48  48  GLY GLY C . n 
C 1 35  ASN 35  49  49  ASN ASN C . n 
C 1 36  ALA 36  50  50  ALA ALA C . n 
C 1 37  GLU 37  51  51  GLU GLU C . n 
C 1 38  SER 38  52  52  SER SER C . n 
C 1 39  ARG 39  53  53  ARG ARG C . n 
C 1 40  TYR 40  54  54  TYR TYR C . n 
C 1 41  VAL 41  55  55  VAL VAL C . n 
C 1 42  LEU 42  56  56  LEU LEU C . n 
C 1 43  THR 43  57  57  THR THR C . n 
C 1 44  GLY 44  58  58  GLY GLY C . n 
C 1 45  ARG 45  59  59  ARG ARG C . n 
C 1 46  TYR 46  60  60  TYR TYR C . n 
C 1 47  ASP 47  61  61  ASP ASP C . n 
C 1 48  SER 48  62  62  SER SER C . n 
C 1 49  ALA 49  63  63  ALA ALA C . n 
C 1 50  PRO 50  64  64  PRO PRO C . n 
C 1 51  ALA 51  65  65  ALA ALA C . n 
C 1 52  THR 52  66  66  THR THR C . n 
C 1 53  ASP 53  67  67  ASP ASP C . n 
C 1 54  GLY 54  68  68  GLY GLY C . n 
C 1 55  SER 55  69  69  SER SER C . n 
C 1 56  GLY 56  70  70  GLY GLY C . n 
C 1 57  THR 57  71  71  THR THR C . n 
C 1 58  ALA 58  72  72  ALA ALA C . n 
C 1 59  LEU 59  73  73  LEU LEU C . n 
C 1 60  GLY 60  74  74  GLY GLY C . n 
C 1 61  TRP 61  75  75  TRP TRP C . n 
C 1 62  THR 62  76  76  THR THR C . n 
C 1 63  VAL 63  77  77  VAL VAL C . n 
C 1 64  ALA 64  78  78  ALA ALA C . n 
C 1 65  TRP 65  79  79  TRP TRP C . n 
C 1 66  LYS 66  80  80  LYS LYS C . n 
C 1 67  ASN 67  81  81  ASN ASN C . n 
C 1 68  ASN 68  82  82  ASN ASN C . n 
C 1 69  TYR 69  83  83  TYR TYR C . n 
C 1 70  ARG 70  84  84  ARG ARG C . n 
C 1 71  ASN 71  85  85  ASN ASN C . n 
C 1 72  ALA 72  86  86  ALA ALA C . n 
C 1 73  HIS 73  87  87  HIS HIS C . n 
C 1 74  SER 74  88  88  SER SER C . n 
C 1 75  ALA 75  89  89  ALA ALA C . n 
C 1 76  THR 76  90  90  THR THR C . n 
C 1 77  THR 77  91  91  THR THR C . n 
C 1 78  TRP 78  92  92  TRP TRP C . n 
C 1 79  SER 79  93  93  SER SER C . n 
C 1 80  GLY 80  94  94  GLY GLY C . n 
C 1 81  GLN 81  95  95  GLN GLN C . n 
C 1 82  TYR 82  96  96  TYR TYR C . n 
C 1 83  VAL 83  97  97  VAL VAL C . n 
C 1 84  GLY 84  98  98  GLY GLY C . n 
C 1 85  GLY 85  99  99  GLY GLY C . n 
C 1 86  ALA 86  100 100 ALA ALA C . n 
C 1 87  GLU 87  101 101 GLU GLU C . n 
C 1 88  ALA 88  102 102 ALA ALA C . n 
C 1 89  ARG 89  103 103 ARG ARG C . n 
C 1 90  ILE 90  104 104 ILE ILE C . n 
C 1 91  ASN 91  105 105 ASN ASN C . n 
C 1 92  THR 92  106 106 THR THR C . n 
C 1 93  GLN 93  107 107 GLN GLN C . n 
C 1 94  TRP 94  108 108 TRP TRP C . n 
C 1 95  LEU 95  109 109 LEU LEU C . n 
C 1 96  LEU 96  110 110 LEU LEU C . n 
C 1 97  THR 97  111 111 THR THR C . n 
C 1 98  SER 98  112 112 SER SER C . n 
C 1 99  GLY 99  113 113 GLY GLY C . n 
C 1 100 THR 100 114 114 THR THR C . n 
C 1 101 THR 101 115 115 THR THR C . n 
C 1 102 GLU 102 116 116 GLU GLU C . n 
C 1 103 ALA 103 117 117 ALA ALA C . n 
C 1 104 ASN 104 118 118 ASN ASN C . n 
C 1 105 ALA 105 119 119 ALA ALA C . n 
C 1 106 TRP 106 120 120 TRP TRP C . n 
C 1 107 LYS 107 121 121 LYS LYS C . n 
C 1 108 SER 108 122 122 SER SER C . n 
C 1 109 THR 109 123 123 THR THR C . n 
C 1 110 LEU 110 124 124 LEU LEU C . n 
C 1 111 VAL 111 125 125 VAL VAL C . n 
C 1 112 GLY 112 126 126 GLY GLY C . n 
C 1 113 HIS 113 127 127 HIS HIS C . n 
C 1 114 ASP 114 128 128 ASP ASP C . n 
C 1 115 THR 115 129 129 THR THR C . n 
C 1 116 PHE 116 130 130 PHE PHE C . n 
C 1 117 THR 117 131 131 THR THR C . n 
C 1 118 LYS 118 132 132 LYS LYS C . n 
C 1 119 VAL 119 133 133 VAL VAL C . n 
C 1 120 LYS 120 134 134 LYS LYS C . n 
C 1 121 PRO 121 135 135 PRO PRO C . n 
D 1 1   ALA 1   15  15  ALA ALA D . n 
D 1 2   GLY 2   16  16  GLY GLY D . n 
D 1 3   ILE 3   17  17  ILE ILE D . n 
D 1 4   THR 4   18  18  THR THR D . n 
D 1 5   GLY 5   19  19  GLY GLY D . n 
D 1 6   THR 6   20  20  THR THR D . n 
D 1 7   TRP 7   21  21  TRP TRP D . n 
D 1 8   TYR 8   22  22  TYR TYR D . n 
D 1 9   ASN 9   23  23  ASN ASN D . n 
D 1 10  GLN 10  24  24  GLN GLN D . n 
D 1 11  LEU 11  25  25  LEU LEU D . n 
D 1 12  GLY 12  26  26  GLY GLY D . n 
D 1 13  SER 13  27  27  SER SER D . n 
D 1 14  THR 14  28  28  THR THR D . n 
D 1 15  PHE 15  29  29  PHE PHE D . n 
D 1 16  ILE 16  30  30  ILE ILE D . n 
D 1 17  VAL 17  31  31  VAL VAL D . n 
D 1 18  THR 18  32  32  THR THR D . n 
D 1 19  ALA 19  33  33  ALA ALA D . n 
D 1 20  GLY 20  34  34  GLY GLY D . n 
D 1 21  ALA 21  35  35  ALA ALA D . n 
D 1 22  ASP 22  36  36  ASP ASP D . n 
D 1 23  GLY 23  37  37  GLY GLY D . n 
D 1 24  ALA 24  38  38  ALA ALA D . n 
D 1 25  LEU 25  39  39  LEU LEU D . n 
D 1 26  THR 26  40  40  THR THR D . n 
D 1 27  GLY 27  41  41  GLY GLY D . n 
D 1 28  THR 28  42  42  THR THR D . n 
D 1 29  TYR 29  43  43  TYR TYR D . n 
D 1 30  GLU 30  44  44  GLU GLU D . n 
D 1 31  SER 31  45  45  SER SER D . n 
D 1 32  ALA 32  46  46  ALA ALA D . n 
D 1 33  VAL 33  47  47  VAL VAL D . n 
D 1 34  GLY 34  48  48  GLY GLY D . n 
D 1 35  ASN 35  49  49  ASN ASN D . n 
D 1 36  ALA 36  50  50  ALA ALA D . n 
D 1 37  GLU 37  51  51  GLU GLU D . n 
D 1 38  SER 38  52  52  SER SER D . n 
D 1 39  ARG 39  53  53  ARG ARG D . n 
D 1 40  TYR 40  54  54  TYR TYR D . n 
D 1 41  VAL 41  55  55  VAL VAL D . n 
D 1 42  LEU 42  56  56  LEU LEU D . n 
D 1 43  THR 43  57  57  THR THR D . n 
D 1 44  GLY 44  58  58  GLY GLY D . n 
D 1 45  ARG 45  59  59  ARG ARG D . n 
D 1 46  TYR 46  60  60  TYR TYR D . n 
D 1 47  ASP 47  61  61  ASP ASP D . n 
D 1 48  SER 48  62  62  SER SER D . n 
D 1 49  ALA 49  63  63  ALA ALA D . n 
D 1 50  PRO 50  64  64  PRO PRO D . n 
D 1 51  ALA 51  65  65  ALA ALA D . n 
D 1 52  THR 52  66  66  THR THR D . n 
D 1 53  ASP 53  67  67  ASP ASP D . n 
D 1 54  GLY 54  68  68  GLY GLY D . n 
D 1 55  SER 55  69  69  SER SER D . n 
D 1 56  GLY 56  70  70  GLY GLY D . n 
D 1 57  THR 57  71  71  THR THR D . n 
D 1 58  ALA 58  72  72  ALA ALA D . n 
D 1 59  LEU 59  73  73  LEU LEU D . n 
D 1 60  GLY 60  74  74  GLY GLY D . n 
D 1 61  TRP 61  75  75  TRP TRP D . n 
D 1 62  THR 62  76  76  THR THR D . n 
D 1 63  VAL 63  77  77  VAL VAL D . n 
D 1 64  ALA 64  78  78  ALA ALA D . n 
D 1 65  TRP 65  79  79  TRP TRP D . n 
D 1 66  LYS 66  80  80  LYS LYS D . n 
D 1 67  ASN 67  81  81  ASN ASN D . n 
D 1 68  ASN 68  82  82  ASN ASN D . n 
D 1 69  TYR 69  83  83  TYR TYR D . n 
D 1 70  ARG 70  84  84  ARG ARG D . n 
D 1 71  ASN 71  85  85  ASN ASN D . n 
D 1 72  ALA 72  86  86  ALA ALA D . n 
D 1 73  HIS 73  87  87  HIS HIS D . n 
D 1 74  SER 74  88  88  SER SER D . n 
D 1 75  ALA 75  89  89  ALA ALA D . n 
D 1 76  THR 76  90  90  THR THR D . n 
D 1 77  THR 77  91  91  THR THR D . n 
D 1 78  TRP 78  92  92  TRP TRP D . n 
D 1 79  SER 79  93  93  SER SER D . n 
D 1 80  GLY 80  94  94  GLY GLY D . n 
D 1 81  GLN 81  95  95  GLN GLN D . n 
D 1 82  TYR 82  96  96  TYR TYR D . n 
D 1 83  VAL 83  97  97  VAL VAL D . n 
D 1 84  GLY 84  98  98  GLY GLY D . n 
D 1 85  GLY 85  99  99  GLY GLY D . n 
D 1 86  ALA 86  100 100 ALA ALA D . n 
D 1 87  GLU 87  101 101 GLU GLU D . n 
D 1 88  ALA 88  102 102 ALA ALA D . n 
D 1 89  ARG 89  103 103 ARG ARG D . n 
D 1 90  ILE 90  104 104 ILE ILE D . n 
D 1 91  ASN 91  105 105 ASN ASN D . n 
D 1 92  THR 92  106 106 THR THR D . n 
D 1 93  GLN 93  107 107 GLN GLN D . n 
D 1 94  TRP 94  108 108 TRP TRP D . n 
D 1 95  LEU 95  109 109 LEU LEU D . n 
D 1 96  LEU 96  110 110 LEU LEU D . n 
D 1 97  THR 97  111 111 THR THR D . n 
D 1 98  SER 98  112 112 SER SER D . n 
D 1 99  GLY 99  113 113 GLY GLY D . n 
D 1 100 THR 100 114 114 THR THR D . n 
D 1 101 THR 101 115 115 THR THR D . n 
D 1 102 GLU 102 116 116 GLU GLU D . n 
D 1 103 ALA 103 117 117 ALA ALA D . n 
D 1 104 ASN 104 118 118 ASN ASN D . n 
D 1 105 ALA 105 119 119 ALA ALA D . n 
D 1 106 TRP 106 120 120 TRP TRP D . n 
D 1 107 LYS 107 121 121 LYS LYS D . n 
D 1 108 SER 108 122 122 SER SER D . n 
D 1 109 THR 109 123 123 THR THR D . n 
D 1 110 LEU 110 124 124 LEU LEU D . n 
D 1 111 VAL 111 125 125 VAL VAL D . n 
D 1 112 GLY 112 126 126 GLY GLY D . n 
D 1 113 HIS 113 127 127 HIS HIS D . n 
D 1 114 ASP 114 128 128 ASP ASP D . n 
D 1 115 THR 115 129 129 THR THR D . n 
D 1 116 PHE 116 130 130 PHE PHE D . n 
D 1 117 THR 117 131 131 THR THR D . n 
D 1 118 LYS 118 132 132 LYS LYS D . n 
D 1 119 VAL 119 133 133 VAL VAL D . n 
D 1 120 LYS 120 134 134 LYS LYS D . n 
D 1 121 PRO 121 135 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1LXQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1LXQ 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 DMS   1   301 301 DMS   DMS A . 
F 2 DMS   1   302 302 DMS   DMS A . 
G 3 A1LXQ 1   201 201 A1LXQ AS5 B . 
H 2 DMS   1   301 301 DMS   DMS C . 
I 2 DMS   1   302 302 DMS   DMS C . 
J 3 A1LXQ 1   201 201 A1LXQ AS5 D . 
K 4 HOH   1   401 510 HOH   HOH A . 
K 4 HOH   2   402 333 HOH   HOH A . 
K 4 HOH   3   403 316 HOH   HOH A . 
K 4 HOH   4   404 131 HOH   HOH A . 
K 4 HOH   5   405 456 HOH   HOH A . 
K 4 HOH   6   406 477 HOH   HOH A . 
K 4 HOH   7   407 156 HOH   HOH A . 
K 4 HOH   8   408 383 HOH   HOH A . 
K 4 HOH   9   409 695 HOH   HOH A . 
K 4 HOH   10  410 693 HOH   HOH A . 
K 4 HOH   11  411 207 HOH   HOH A . 
K 4 HOH   12  412 337 HOH   HOH A . 
K 4 HOH   13  413 75  HOH   HOH A . 
K 4 HOH   14  414 380 HOH   HOH A . 
K 4 HOH   15  415 690 HOH   HOH A . 
K 4 HOH   16  416 590 HOH   HOH A . 
K 4 HOH   17  417 25  HOH   HOH A . 
K 4 HOH   18  418 551 HOH   HOH A . 
K 4 HOH   19  419 404 HOH   HOH A . 
K 4 HOH   20  420 298 HOH   HOH A . 
K 4 HOH   21  421 2   HOH   HOH A . 
K 4 HOH   22  422 253 HOH   HOH A . 
K 4 HOH   23  423 59  HOH   HOH A . 
K 4 HOH   24  424 649 HOH   HOH A . 
K 4 HOH   25  425 183 HOH   HOH A . 
K 4 HOH   26  426 280 HOH   HOH A . 
K 4 HOH   27  427 51  HOH   HOH A . 
K 4 HOH   28  428 99  HOH   HOH A . 
K 4 HOH   29  429 71  HOH   HOH A . 
K 4 HOH   30  430 394 HOH   HOH A . 
K 4 HOH   31  431 1   HOH   HOH A . 
K 4 HOH   32  432 153 HOH   HOH A . 
K 4 HOH   33  433 136 HOH   HOH A . 
K 4 HOH   34  434 411 HOH   HOH A . 
K 4 HOH   35  435 168 HOH   HOH A . 
K 4 HOH   36  436 34  HOH   HOH A . 
K 4 HOH   37  437 351 HOH   HOH A . 
K 4 HOH   38  438 194 HOH   HOH A . 
K 4 HOH   39  439 457 HOH   HOH A . 
K 4 HOH   40  440 318 HOH   HOH A . 
K 4 HOH   41  441 211 HOH   HOH A . 
K 4 HOH   42  442 126 HOH   HOH A . 
K 4 HOH   43  443 282 HOH   HOH A . 
K 4 HOH   44  444 224 HOH   HOH A . 
K 4 HOH   45  445 81  HOH   HOH A . 
K 4 HOH   46  446 7   HOH   HOH A . 
K 4 HOH   47  447 328 HOH   HOH A . 
K 4 HOH   48  448 76  HOH   HOH A . 
K 4 HOH   49  449 9   HOH   HOH A . 
K 4 HOH   50  450 86  HOH   HOH A . 
K 4 HOH   51  451 460 HOH   HOH A . 
K 4 HOH   52  452 539 HOH   HOH A . 
K 4 HOH   53  453 110 HOH   HOH A . 
K 4 HOH   54  454 84  HOH   HOH A . 
K 4 HOH   55  455 163 HOH   HOH A . 
K 4 HOH   56  456 313 HOH   HOH A . 
K 4 HOH   57  457 261 HOH   HOH A . 
K 4 HOH   58  458 61  HOH   HOH A . 
K 4 HOH   59  459 251 HOH   HOH A . 
K 4 HOH   60  460 113 HOH   HOH A . 
K 4 HOH   61  461 5   HOH   HOH A . 
K 4 HOH   62  462 260 HOH   HOH A . 
K 4 HOH   63  463 42  HOH   HOH A . 
K 4 HOH   64  464 193 HOH   HOH A . 
K 4 HOH   65  465 574 HOH   HOH A . 
K 4 HOH   66  466 454 HOH   HOH A . 
K 4 HOH   67  467 448 HOH   HOH A . 
K 4 HOH   68  468 174 HOH   HOH A . 
K 4 HOH   69  469 104 HOH   HOH A . 
K 4 HOH   70  470 305 HOH   HOH A . 
K 4 HOH   71  471 67  HOH   HOH A . 
K 4 HOH   72  472 184 HOH   HOH A . 
K 4 HOH   73  473 18  HOH   HOH A . 
K 4 HOH   74  474 666 HOH   HOH A . 
K 4 HOH   75  475 132 HOH   HOH A . 
K 4 HOH   76  476 169 HOH   HOH A . 
K 4 HOH   77  477 41  HOH   HOH A . 
K 4 HOH   78  478 473 HOH   HOH A . 
K 4 HOH   79  479 56  HOH   HOH A . 
K 4 HOH   80  480 292 HOH   HOH A . 
K 4 HOH   81  481 532 HOH   HOH A . 
K 4 HOH   82  482 319 HOH   HOH A . 
K 4 HOH   83  483 66  HOH   HOH A . 
K 4 HOH   84  484 414 HOH   HOH A . 
K 4 HOH   85  485 83  HOH   HOH A . 
K 4 HOH   86  486 150 HOH   HOH A . 
K 4 HOH   87  487 97  HOH   HOH A . 
K 4 HOH   88  488 706 HOH   HOH A . 
K 4 HOH   89  489 54  HOH   HOH A . 
K 4 HOH   90  490 464 HOH   HOH A . 
K 4 HOH   91  491 122 HOH   HOH A . 
K 4 HOH   92  492 413 HOH   HOH A . 
K 4 HOH   93  493 593 HOH   HOH A . 
K 4 HOH   94  494 219 HOH   HOH A . 
K 4 HOH   95  495 85  HOH   HOH A . 
K 4 HOH   96  496 82  HOH   HOH A . 
K 4 HOH   97  497 284 HOH   HOH A . 
K 4 HOH   98  498 357 HOH   HOH A . 
K 4 HOH   99  499 589 HOH   HOH A . 
K 4 HOH   100 500 399 HOH   HOH A . 
K 4 HOH   101 501 252 HOH   HOH A . 
K 4 HOH   102 502 40  HOH   HOH A . 
K 4 HOH   103 503 250 HOH   HOH A . 
K 4 HOH   104 504 511 HOH   HOH A . 
K 4 HOH   105 505 519 HOH   HOH A . 
K 4 HOH   106 506 617 HOH   HOH A . 
K 4 HOH   107 507 142 HOH   HOH A . 
K 4 HOH   108 508 299 HOH   HOH A . 
K 4 HOH   109 509 95  HOH   HOH A . 
K 4 HOH   110 510 218 HOH   HOH A . 
K 4 HOH   111 511 459 HOH   HOH A . 
K 4 HOH   112 512 103 HOH   HOH A . 
K 4 HOH   113 513 111 HOH   HOH A . 
K 4 HOH   114 514 236 HOH   HOH A . 
K 4 HOH   115 515 181 HOH   HOH A . 
K 4 HOH   116 516 732 HOH   HOH A . 
K 4 HOH   117 517 441 HOH   HOH A . 
K 4 HOH   118 518 484 HOH   HOH A . 
K 4 HOH   119 519 628 HOH   HOH A . 
K 4 HOH   120 520 26  HOH   HOH A . 
K 4 HOH   121 521 595 HOH   HOH A . 
K 4 HOH   122 522 466 HOH   HOH A . 
K 4 HOH   123 523 155 HOH   HOH A . 
K 4 HOH   124 524 296 HOH   HOH A . 
K 4 HOH   125 525 311 HOH   HOH A . 
K 4 HOH   126 526 332 HOH   HOH A . 
K 4 HOH   127 527 190 HOH   HOH A . 
K 4 HOH   128 528 297 HOH   HOH A . 
K 4 HOH   129 529 525 HOH   HOH A . 
K 4 HOH   130 530 447 HOH   HOH A . 
K 4 HOH   131 531 230 HOH   HOH A . 
K 4 HOH   132 532 643 HOH   HOH A . 
K 4 HOH   133 533 735 HOH   HOH A . 
K 4 HOH   134 534 450 HOH   HOH A . 
K 4 HOH   135 535 588 HOH   HOH A . 
K 4 HOH   136 536 130 HOH   HOH A . 
K 4 HOH   137 537 598 HOH   HOH A . 
K 4 HOH   138 538 232 HOH   HOH A . 
K 4 HOH   139 539 669 HOH   HOH A . 
K 4 HOH   140 540 469 HOH   HOH A . 
K 4 HOH   141 541 667 HOH   HOH A . 
K 4 HOH   142 542 696 HOH   HOH A . 
K 4 HOH   143 543 556 HOH   HOH A . 
K 4 HOH   144 544 488 HOH   HOH A . 
K 4 HOH   145 545 641 HOH   HOH A . 
K 4 HOH   146 546 418 HOH   HOH A . 
K 4 HOH   147 547 73  HOH   HOH A . 
K 4 HOH   148 548 204 HOH   HOH A . 
K 4 HOH   149 549 549 HOH   HOH A . 
K 4 HOH   150 550 144 HOH   HOH A . 
K 4 HOH   151 551 453 HOH   HOH A . 
K 4 HOH   152 552 546 HOH   HOH A . 
K 4 HOH   153 553 304 HOH   HOH A . 
K 4 HOH   154 554 692 HOH   HOH A . 
K 4 HOH   155 555 501 HOH   HOH A . 
K 4 HOH   156 556 636 HOH   HOH A . 
K 4 HOH   157 557 594 HOH   HOH A . 
K 4 HOH   158 558 500 HOH   HOH A . 
K 4 HOH   159 559 687 HOH   HOH A . 
K 4 HOH   160 560 568 HOH   HOH A . 
K 4 HOH   161 561 653 HOH   HOH A . 
K 4 HOH   162 562 338 HOH   HOH A . 
K 4 HOH   163 563 386 HOH   HOH A . 
K 4 HOH   164 564 302 HOH   HOH A . 
K 4 HOH   165 565 601 HOH   HOH A . 
K 4 HOH   166 566 604 HOH   HOH A . 
K 4 HOH   167 567 295 HOH   HOH A . 
K 4 HOH   168 568 528 HOH   HOH A . 
K 4 HOH   169 569 712 HOH   HOH A . 
K 4 HOH   170 570 612 HOH   HOH A . 
K 4 HOH   171 571 513 HOH   HOH A . 
K 4 HOH   172 572 737 HOH   HOH A . 
K 4 HOH   173 573 362 HOH   HOH A . 
K 4 HOH   174 574 197 HOH   HOH A . 
K 4 HOH   175 575 392 HOH   HOH A . 
K 4 HOH   176 576 419 HOH   HOH A . 
K 4 HOH   177 577 372 HOH   HOH A . 
K 4 HOH   178 578 655 HOH   HOH A . 
K 4 HOH   179 579 716 HOH   HOH A . 
K 4 HOH   180 580 523 HOH   HOH A . 
K 4 HOH   181 581 185 HOH   HOH A . 
K 4 HOH   182 582 495 HOH   HOH A . 
K 4 HOH   183 583 322 HOH   HOH A . 
K 4 HOH   184 584 742 HOH   HOH A . 
K 4 HOH   185 585 444 HOH   HOH A . 
K 4 HOH   186 586 509 HOH   HOH A . 
K 4 HOH   187 587 562 HOH   HOH A . 
K 4 HOH   188 588 241 HOH   HOH A . 
K 4 HOH   189 589 672 HOH   HOH A . 
K 4 HOH   190 590 272 HOH   HOH A . 
K 4 HOH   191 591 668 HOH   HOH A . 
K 4 HOH   192 592 210 HOH   HOH A . 
K 4 HOH   193 593 356 HOH   HOH A . 
K 4 HOH   194 594 656 HOH   HOH A . 
K 4 HOH   195 595 654 HOH   HOH A . 
K 4 HOH   196 596 492 HOH   HOH A . 
K 4 HOH   197 597 209 HOH   HOH A . 
K 4 HOH   198 598 596 HOH   HOH A . 
K 4 HOH   199 599 611 HOH   HOH A . 
K 4 HOH   200 600 308 HOH   HOH A . 
K 4 HOH   201 601 366 HOH   HOH A . 
K 4 HOH   202 602 508 HOH   HOH A . 
K 4 HOH   203 603 274 HOH   HOH A . 
K 4 HOH   204 604 661 HOH   HOH A . 
K 4 HOH   205 605 339 HOH   HOH A . 
K 4 HOH   206 606 652 HOH   HOH A . 
K 4 HOH   207 607 425 HOH   HOH A . 
K 4 HOH   208 608 365 HOH   HOH A . 
K 4 HOH   209 609 682 HOH   HOH A . 
K 4 HOH   210 610 613 HOH   HOH A . 
K 4 HOH   211 611 540 HOH   HOH A . 
K 4 HOH   212 612 167 HOH   HOH A . 
K 4 HOH   213 613 602 HOH   HOH A . 
K 4 HOH   214 614 647 HOH   HOH A . 
K 4 HOH   215 615 738 HOH   HOH A . 
K 4 HOH   216 616 714 HOH   HOH A . 
K 4 HOH   217 617 566 HOH   HOH A . 
K 4 HOH   218 618 630 HOH   HOH A . 
L 4 HOH   1   301 382 HOH   HOH B . 
L 4 HOH   2   302 614 HOH   HOH B . 
L 4 HOH   3   303 526 HOH   HOH B . 
L 4 HOH   4   304 673 HOH   HOH B . 
L 4 HOH   5   305 451 HOH   HOH B . 
L 4 HOH   6   306 228 HOH   HOH B . 
L 4 HOH   7   307 417 HOH   HOH B . 
L 4 HOH   8   308 583 HOH   HOH B . 
L 4 HOH   9   309 234 HOH   HOH B . 
L 4 HOH   10  310 603 HOH   HOH B . 
L 4 HOH   11  311 220 HOH   HOH B . 
L 4 HOH   12  312 176 HOH   HOH B . 
L 4 HOH   13  313 578 HOH   HOH B . 
L 4 HOH   14  314 287 HOH   HOH B . 
L 4 HOH   15  315 31  HOH   HOH B . 
L 4 HOH   16  316 483 HOH   HOH B . 
L 4 HOH   17  317 335 HOH   HOH B . 
L 4 HOH   18  318 268 HOH   HOH B . 
L 4 HOH   19  319 674 HOH   HOH B . 
L 4 HOH   20  320 8   HOH   HOH B . 
L 4 HOH   21  321 573 HOH   HOH B . 
L 4 HOH   22  322 522 HOH   HOH B . 
L 4 HOH   23  323 270 HOH   HOH B . 
L 4 HOH   24  324 242 HOH   HOH B . 
L 4 HOH   25  325 323 HOH   HOH B . 
L 4 HOH   26  326 93  HOH   HOH B . 
L 4 HOH   27  327 342 HOH   HOH B . 
L 4 HOH   28  328 43  HOH   HOH B . 
L 4 HOH   29  329 257 HOH   HOH B . 
L 4 HOH   30  330 200 HOH   HOH B . 
L 4 HOH   31  331 507 HOH   HOH B . 
L 4 HOH   32  332 6   HOH   HOH B . 
L 4 HOH   33  333 33  HOH   HOH B . 
L 4 HOH   34  334 10  HOH   HOH B . 
L 4 HOH   35  335 363 HOH   HOH B . 
L 4 HOH   36  336 291 HOH   HOH B . 
L 4 HOH   37  337 162 HOH   HOH B . 
L 4 HOH   38  338 58  HOH   HOH B . 
L 4 HOH   39  339 72  HOH   HOH B . 
L 4 HOH   40  340 106 HOH   HOH B . 
L 4 HOH   41  341 344 HOH   HOH B . 
L 4 HOH   42  342 273 HOH   HOH B . 
L 4 HOH   43  343 134 HOH   HOH B . 
L 4 HOH   44  344 517 HOH   HOH B . 
L 4 HOH   45  345 543 HOH   HOH B . 
L 4 HOH   46  346 347 HOH   HOH B . 
L 4 HOH   47  347 725 HOH   HOH B . 
L 4 HOH   48  348 221 HOH   HOH B . 
L 4 HOH   49  349 406 HOH   HOH B . 
L 4 HOH   50  350 262 HOH   HOH B . 
L 4 HOH   51  351 69  HOH   HOH B . 
L 4 HOH   52  352 187 HOH   HOH B . 
L 4 HOH   53  353 361 HOH   HOH B . 
L 4 HOH   54  354 20  HOH   HOH B . 
L 4 HOH   55  355 263 HOH   HOH B . 
L 4 HOH   56  356 39  HOH   HOH B . 
L 4 HOH   57  357 702 HOH   HOH B . 
L 4 HOH   58  358 336 HOH   HOH B . 
L 4 HOH   59  359 15  HOH   HOH B . 
L 4 HOH   60  360 377 HOH   HOH B . 
L 4 HOH   61  361 572 HOH   HOH B . 
L 4 HOH   62  362 63  HOH   HOH B . 
L 4 HOH   63  363 478 HOH   HOH B . 
L 4 HOH   64  364 233 HOH   HOH B . 
L 4 HOH   65  365 78  HOH   HOH B . 
L 4 HOH   66  366 160 HOH   HOH B . 
L 4 HOH   67  367 102 HOH   HOH B . 
L 4 HOH   68  368 719 HOH   HOH B . 
L 4 HOH   69  369 402 HOH   HOH B . 
L 4 HOH   70  370 38  HOH   HOH B . 
L 4 HOH   71  371 53  HOH   HOH B . 
L 4 HOH   72  372 151 HOH   HOH B . 
L 4 HOH   73  373 410 HOH   HOH B . 
L 4 HOH   74  374 531 HOH   HOH B . 
L 4 HOH   75  375 470 HOH   HOH B . 
L 4 HOH   76  376 199 HOH   HOH B . 
L 4 HOH   77  377 101 HOH   HOH B . 
L 4 HOH   78  378 321 HOH   HOH B . 
L 4 HOH   79  379 279 HOH   HOH B . 
L 4 HOH   80  380 463 HOH   HOH B . 
L 4 HOH   81  381 186 HOH   HOH B . 
L 4 HOH   82  382 191 HOH   HOH B . 
L 4 HOH   83  383 683 HOH   HOH B . 
L 4 HOH   84  384 358 HOH   HOH B . 
L 4 HOH   85  385 141 HOH   HOH B . 
L 4 HOH   86  386 480 HOH   HOH B . 
L 4 HOH   87  387 55  HOH   HOH B . 
L 4 HOH   88  388 412 HOH   HOH B . 
L 4 HOH   89  389 173 HOH   HOH B . 
L 4 HOH   90  390 192 HOH   HOH B . 
L 4 HOH   91  391 62  HOH   HOH B . 
L 4 HOH   92  392 29  HOH   HOH B . 
L 4 HOH   93  393 158 HOH   HOH B . 
L 4 HOH   94  394 524 HOH   HOH B . 
L 4 HOH   95  395 398 HOH   HOH B . 
L 4 HOH   96  396 300 HOH   HOH B . 
L 4 HOH   97  397 700 HOH   HOH B . 
L 4 HOH   98  398 740 HOH   HOH B . 
L 4 HOH   99  399 490 HOH   HOH B . 
L 4 HOH   100 400 226 HOH   HOH B . 
L 4 HOH   101 401 680 HOH   HOH B . 
L 4 HOH   102 402 597 HOH   HOH B . 
L 4 HOH   103 403 303 HOH   HOH B . 
L 4 HOH   104 404 245 HOH   HOH B . 
L 4 HOH   105 405 216 HOH   HOH B . 
L 4 HOH   106 406 256 HOH   HOH B . 
L 4 HOH   107 407 264 HOH   HOH B . 
L 4 HOH   108 408 378 HOH   HOH B . 
L 4 HOH   109 409 348 HOH   HOH B . 
L 4 HOH   110 410 475 HOH   HOH B . 
L 4 HOH   111 411 476 HOH   HOH B . 
L 4 HOH   112 412 642 HOH   HOH B . 
L 4 HOH   113 413 327 HOH   HOH B . 
L 4 HOH   114 414 608 HOH   HOH B . 
L 4 HOH   115 415 676 HOH   HOH B . 
L 4 HOH   116 416 195 HOH   HOH B . 
L 4 HOH   117 417 350 HOH   HOH B . 
L 4 HOH   118 418 571 HOH   HOH B . 
L 4 HOH   119 419 565 HOH   HOH B . 
L 4 HOH   120 420 651 HOH   HOH B . 
L 4 HOH   121 421 440 HOH   HOH B . 
L 4 HOH   122 422 486 HOH   HOH B . 
L 4 HOH   123 423 278 HOH   HOH B . 
L 4 HOH   124 424 405 HOH   HOH B . 
L 4 HOH   125 425 494 HOH   HOH B . 
L 4 HOH   126 426 407 HOH   HOH B . 
L 4 HOH   127 427 397 HOH   HOH B . 
L 4 HOH   128 428 393 HOH   HOH B . 
L 4 HOH   129 429 426 HOH   HOH B . 
L 4 HOH   130 430 600 HOH   HOH B . 
L 4 HOH   131 431 422 HOH   HOH B . 
L 4 HOH   132 432 591 HOH   HOH B . 
L 4 HOH   133 433 493 HOH   HOH B . 
L 4 HOH   134 434 727 HOH   HOH B . 
L 4 HOH   135 435 346 HOH   HOH B . 
L 4 HOH   136 436 587 HOH   HOH B . 
L 4 HOH   137 437 717 HOH   HOH B . 
L 4 HOH   138 438 381 HOH   HOH B . 
L 4 HOH   139 439 633 HOH   HOH B . 
L 4 HOH   140 440 586 HOH   HOH B . 
L 4 HOH   141 441 723 HOH   HOH B . 
L 4 HOH   142 442 709 HOH   HOH B . 
L 4 HOH   143 443 518 HOH   HOH B . 
L 4 HOH   144 444 512 HOH   HOH B . 
L 4 HOH   145 445 691 HOH   HOH B . 
L 4 HOH   146 446 248 HOH   HOH B . 
L 4 HOH   147 447 722 HOH   HOH B . 
L 4 HOH   148 448 345 HOH   HOH B . 
L 4 HOH   149 449 538 HOH   HOH B . 
L 4 HOH   150 450 431 HOH   HOH B . 
L 4 HOH   151 451 734 HOH   HOH B . 
L 4 HOH   152 452 559 HOH   HOH B . 
L 4 HOH   153 453 658 HOH   HOH B . 
L 4 HOH   154 454 489 HOH   HOH B . 
L 4 HOH   155 455 733 HOH   HOH B . 
M 4 HOH   1   401 681 HOH   HOH C . 
M 4 HOH   2   402 379 HOH   HOH C . 
M 4 HOH   3   403 472 HOH   HOH C . 
M 4 HOH   4   404 627 HOH   HOH C . 
M 4 HOH   5   405 432 HOH   HOH C . 
M 4 HOH   6   406 640 HOH   HOH C . 
M 4 HOH   7   407 96  HOH   HOH C . 
M 4 HOH   8   408 579 HOH   HOH C . 
M 4 HOH   9   409 502 HOH   HOH C . 
M 4 HOH   10  410 208 HOH   HOH C . 
M 4 HOH   11  411 395 HOH   HOH C . 
M 4 HOH   12  412 240 HOH   HOH C . 
M 4 HOH   13  413 341 HOH   HOH C . 
M 4 HOH   14  414 196 HOH   HOH C . 
M 4 HOH   15  415 657 HOH   HOH C . 
M 4 HOH   16  416 4   HOH   HOH C . 
M 4 HOH   17  417 127 HOH   HOH C . 
M 4 HOH   18  418 744 HOH   HOH C . 
M 4 HOH   19  419 355 HOH   HOH C . 
M 4 HOH   20  420 117 HOH   HOH C . 
M 4 HOH   21  421 90  HOH   HOH C . 
M 4 HOH   22  422 198 HOH   HOH C . 
M 4 HOH   23  423 745 HOH   HOH C . 
M 4 HOH   24  424 503 HOH   HOH C . 
M 4 HOH   25  425 371 HOH   HOH C . 
M 4 HOH   26  426 718 HOH   HOH C . 
M 4 HOH   27  427 385 HOH   HOH C . 
M 4 HOH   28  428 665 HOH   HOH C . 
M 4 HOH   29  429 214 HOH   HOH C . 
M 4 HOH   30  430 584 HOH   HOH C . 
M 4 HOH   31  431 324 HOH   HOH C . 
M 4 HOH   32  432 247 HOH   HOH C . 
M 4 HOH   33  433 391 HOH   HOH C . 
M 4 HOH   34  434 269 HOH   HOH C . 
M 4 HOH   35  435 235 HOH   HOH C . 
M 4 HOH   36  436 149 HOH   HOH C . 
M 4 HOH   37  437 35  HOH   HOH C . 
M 4 HOH   38  438 416 HOH   HOH C . 
M 4 HOH   39  439 3   HOH   HOH C . 
M 4 HOH   40  440 118 HOH   HOH C . 
M 4 HOH   41  441 631 HOH   HOH C . 
M 4 HOH   42  442 625 HOH   HOH C . 
M 4 HOH   43  443 37  HOH   HOH C . 
M 4 HOH   44  444 52  HOH   HOH C . 
M 4 HOH   45  445 105 HOH   HOH C . 
M 4 HOH   46  446 46  HOH   HOH C . 
M 4 HOH   47  447 125 HOH   HOH C . 
M 4 HOH   48  448 374 HOH   HOH C . 
M 4 HOH   49  449 65  HOH   HOH C . 
M 4 HOH   50  450 728 HOH   HOH C . 
M 4 HOH   51  451 13  HOH   HOH C . 
M 4 HOH   52  452 161 HOH   HOH C . 
M 4 HOH   53  453 384 HOH   HOH C . 
M 4 HOH   54  454 487 HOH   HOH C . 
M 4 HOH   55  455 315 HOH   HOH C . 
M 4 HOH   56  456 48  HOH   HOH C . 
M 4 HOH   57  457 435 HOH   HOH C . 
M 4 HOH   58  458 550 HOH   HOH C . 
M 4 HOH   59  459 698 HOH   HOH C . 
M 4 HOH   60  460 375 HOH   HOH C . 
M 4 HOH   61  461 57  HOH   HOH C . 
M 4 HOH   62  462 645 HOH   HOH C . 
M 4 HOH   63  463 534 HOH   HOH C . 
M 4 HOH   64  464 170 HOH   HOH C . 
M 4 HOH   65  465 746 HOH   HOH C . 
M 4 HOH   66  466 554 HOH   HOH C . 
M 4 HOH   67  467 154 HOH   HOH C . 
M 4 HOH   68  468 244 HOH   HOH C . 
M 4 HOH   69  469 11  HOH   HOH C . 
M 4 HOH   70  470 100 HOH   HOH C . 
M 4 HOH   71  471 255 HOH   HOH C . 
M 4 HOH   72  472 47  HOH   HOH C . 
M 4 HOH   73  473 14  HOH   HOH C . 
M 4 HOH   74  474 368 HOH   HOH C . 
M 4 HOH   75  475 364 HOH   HOH C . 
M 4 HOH   76  476 249 HOH   HOH C . 
M 4 HOH   77  477 629 HOH   HOH C . 
M 4 HOH   78  478 206 HOH   HOH C . 
M 4 HOH   79  479 231 HOH   HOH C . 
M 4 HOH   80  480 22  HOH   HOH C . 
M 4 HOH   81  481 485 HOH   HOH C . 
M 4 HOH   82  482 74  HOH   HOH C . 
M 4 HOH   83  483 428 HOH   HOH C . 
M 4 HOH   84  484 23  HOH   HOH C . 
M 4 HOH   85  485 116 HOH   HOH C . 
M 4 HOH   86  486 360 HOH   HOH C . 
M 4 HOH   87  487 607 HOH   HOH C . 
M 4 HOH   88  488 529 HOH   HOH C . 
M 4 HOH   89  489 50  HOH   HOH C . 
M 4 HOH   90  490 373 HOH   HOH C . 
M 4 HOH   91  491 114 HOH   HOH C . 
M 4 HOH   92  492 548 HOH   HOH C . 
M 4 HOH   93  493 171 HOH   HOH C . 
M 4 HOH   94  494 286 HOH   HOH C . 
M 4 HOH   95  495 148 HOH   HOH C . 
M 4 HOH   96  496 92  HOH   HOH C . 
M 4 HOH   97  497 580 HOH   HOH C . 
M 4 HOH   98  498 202 HOH   HOH C . 
M 4 HOH   99  499 215 HOH   HOH C . 
M 4 HOH   100 500 276 HOH   HOH C . 
M 4 HOH   101 501 599 HOH   HOH C . 
M 4 HOH   102 502 159 HOH   HOH C . 
M 4 HOH   103 503 98  HOH   HOH C . 
M 4 HOH   104 504 124 HOH   HOH C . 
M 4 HOH   105 505 238 HOH   HOH C . 
M 4 HOH   106 506 458 HOH   HOH C . 
M 4 HOH   107 507 552 HOH   HOH C . 
M 4 HOH   108 508 349 HOH   HOH C . 
M 4 HOH   109 509 205 HOH   HOH C . 
M 4 HOH   110 510 504 HOH   HOH C . 
M 4 HOH   111 511 135 HOH   HOH C . 
M 4 HOH   112 512 294 HOH   HOH C . 
M 4 HOH   113 513 626 HOH   HOH C . 
M 4 HOH   114 514 265 HOH   HOH C . 
M 4 HOH   115 515 340 HOH   HOH C . 
M 4 HOH   116 516 115 HOH   HOH C . 
M 4 HOH   117 517 288 HOH   HOH C . 
M 4 HOH   118 518 285 HOH   HOH C . 
M 4 HOH   119 519 145 HOH   HOH C . 
M 4 HOH   120 520 677 HOH   HOH C . 
M 4 HOH   121 521 177 HOH   HOH C . 
M 4 HOH   122 522 436 HOH   HOH C . 
M 4 HOH   123 523 172 HOH   HOH C . 
M 4 HOH   124 524 387 HOH   HOH C . 
M 4 HOH   125 525 330 HOH   HOH C . 
M 4 HOH   126 526 139 HOH   HOH C . 
M 4 HOH   127 527 560 HOH   HOH C . 
M 4 HOH   128 528 306 HOH   HOH C . 
M 4 HOH   129 529 563 HOH   HOH C . 
M 4 HOH   130 530 660 HOH   HOH C . 
M 4 HOH   131 531 442 HOH   HOH C . 
M 4 HOH   132 532 326 HOH   HOH C . 
M 4 HOH   133 533 140 HOH   HOH C . 
M 4 HOH   134 534 713 HOH   HOH C . 
M 4 HOH   135 535 547 HOH   HOH C . 
M 4 HOH   136 536 259 HOH   HOH C . 
M 4 HOH   137 537 289 HOH   HOH C . 
M 4 HOH   138 538 703 HOH   HOH C . 
M 4 HOH   139 539 605 HOH   HOH C . 
M 4 HOH   140 540 541 HOH   HOH C . 
M 4 HOH   141 541 499 HOH   HOH C . 
M 4 HOH   142 542 535 HOH   HOH C . 
M 4 HOH   143 543 290 HOH   HOH C . 
M 4 HOH   144 544 481 HOH   HOH C . 
M 4 HOH   145 545 701 HOH   HOH C . 
M 4 HOH   146 546 467 HOH   HOH C . 
M 4 HOH   147 547 452 HOH   HOH C . 
M 4 HOH   148 548 443 HOH   HOH C . 
M 4 HOH   149 549 446 HOH   HOH C . 
M 4 HOH   150 550 314 HOH   HOH C . 
M 4 HOH   151 551 465 HOH   HOH C . 
M 4 HOH   152 552 496 HOH   HOH C . 
M 4 HOH   153 553 567 HOH   HOH C . 
M 4 HOH   154 554 293 HOH   HOH C . 
M 4 HOH   155 555 354 HOH   HOH C . 
M 4 HOH   156 556 331 HOH   HOH C . 
M 4 HOH   157 557 237 HOH   HOH C . 
M 4 HOH   158 558 30  HOH   HOH C . 
M 4 HOH   159 559 301 HOH   HOH C . 
M 4 HOH   160 560 710 HOH   HOH C . 
M 4 HOH   161 561 606 HOH   HOH C . 
M 4 HOH   162 562 537 HOH   HOH C . 
M 4 HOH   163 563 659 HOH   HOH C . 
M 4 HOH   164 564 396 HOH   HOH C . 
M 4 HOH   165 565 616 HOH   HOH C . 
M 4 HOH   166 566 275 HOH   HOH C . 
M 4 HOH   167 567 542 HOH   HOH C . 
M 4 HOH   168 568 307 HOH   HOH C . 
M 4 HOH   169 569 720 HOH   HOH C . 
M 4 HOH   170 570 582 HOH   HOH C . 
M 4 HOH   171 571 721 HOH   HOH C . 
M 4 HOH   172 572 468 HOH   HOH C . 
M 4 HOH   173 573 705 HOH   HOH C . 
M 4 HOH   174 574 479 HOH   HOH C . 
M 4 HOH   175 575 438 HOH   HOH C . 
M 4 HOH   176 576 107 HOH   HOH C . 
M 4 HOH   177 577 180 HOH   HOH C . 
M 4 HOH   178 578 424 HOH   HOH C . 
M 4 HOH   179 579 634 HOH   HOH C . 
M 4 HOH   180 580 445 HOH   HOH C . 
M 4 HOH   181 581 429 HOH   HOH C . 
M 4 HOH   182 582 388 HOH   HOH C . 
M 4 HOH   183 583 670 HOH   HOH C . 
M 4 HOH   184 584 369 HOH   HOH C . 
M 4 HOH   185 585 310 HOH   HOH C . 
M 4 HOH   186 586 491 HOH   HOH C . 
M 4 HOH   187 587 430 HOH   HOH C . 
M 4 HOH   188 588 400 HOH   HOH C . 
M 4 HOH   189 589 474 HOH   HOH C . 
M 4 HOH   190 590 585 HOH   HOH C . 
M 4 HOH   191 591 212 HOH   HOH C . 
M 4 HOH   192 592 433 HOH   HOH C . 
M 4 HOH   193 593 570 HOH   HOH C . 
M 4 HOH   194 594 533 HOH   HOH C . 
M 4 HOH   195 595 569 HOH   HOH C . 
M 4 HOH   196 596 152 HOH   HOH C . 
M 4 HOH   197 597 632 HOH   HOH C . 
M 4 HOH   198 598 137 HOH   HOH C . 
M 4 HOH   199 599 592 HOH   HOH C . 
M 4 HOH   200 600 646 HOH   HOH C . 
M 4 HOH   201 601 409 HOH   HOH C . 
M 4 HOH   202 602 624 HOH   HOH C . 
N 4 HOH   1   301 544 HOH   HOH D . 
N 4 HOH   2   302 736 HOH   HOH D . 
N 4 HOH   3   303 343 HOH   HOH D . 
N 4 HOH   4   304 505 HOH   HOH D . 
N 4 HOH   5   305 557 HOH   HOH D . 
N 4 HOH   6   306 420 HOH   HOH D . 
N 4 HOH   7   307 178 HOH   HOH D . 
N 4 HOH   8   308 19  HOH   HOH D . 
N 4 HOH   9   309 729 HOH   HOH D . 
N 4 HOH   10  310 157 HOH   HOH D . 
N 4 HOH   11  311 520 HOH   HOH D . 
N 4 HOH   12  312 119 HOH   HOH D . 
N 4 HOH   13  313 558 HOH   HOH D . 
N 4 HOH   14  314 390 HOH   HOH D . 
N 4 HOH   15  315 21  HOH   HOH D . 
N 4 HOH   16  316 138 HOH   HOH D . 
N 4 HOH   17  317 182 HOH   HOH D . 
N 4 HOH   18  318 89  HOH   HOH D . 
N 4 HOH   19  319 650 HOH   HOH D . 
N 4 HOH   20  320 415 HOH   HOH D . 
N 4 HOH   21  321 87  HOH   HOH D . 
N 4 HOH   22  322 514 HOH   HOH D . 
N 4 HOH   23  323 715 HOH   HOH D . 
N 4 HOH   24  324 128 HOH   HOH D . 
N 4 HOH   25  325 108 HOH   HOH D . 
N 4 HOH   26  326 44  HOH   HOH D . 
N 4 HOH   27  327 70  HOH   HOH D . 
N 4 HOH   28  328 12  HOH   HOH D . 
N 4 HOH   29  329 68  HOH   HOH D . 
N 4 HOH   30  330 267 HOH   HOH D . 
N 4 HOH   31  331 527 HOH   HOH D . 
N 4 HOH   32  332 421 HOH   HOH D . 
N 4 HOH   33  333 266 HOH   HOH D . 
N 4 HOH   34  334 16  HOH   HOH D . 
N 4 HOH   35  335 329 HOH   HOH D . 
N 4 HOH   36  336 334 HOH   HOH D . 
N 4 HOH   37  337 283 HOH   HOH D . 
N 4 HOH   38  338 724 HOH   HOH D . 
N 4 HOH   39  339 79  HOH   HOH D . 
N 4 HOH   40  340 60  HOH   HOH D . 
N 4 HOH   41  341 743 HOH   HOH D . 
N 4 HOH   42  342 675 HOH   HOH D . 
N 4 HOH   43  343 166 HOH   HOH D . 
N 4 HOH   44  344 367 HOH   HOH D . 
N 4 HOH   45  345 112 HOH   HOH D . 
N 4 HOH   46  346 561 HOH   HOH D . 
N 4 HOH   47  347 64  HOH   HOH D . 
N 4 HOH   48  348 271 HOH   HOH D . 
N 4 HOH   49  349 225 HOH   HOH D . 
N 4 HOH   50  350 312 HOH   HOH D . 
N 4 HOH   51  351 27  HOH   HOH D . 
N 4 HOH   52  352 353 HOH   HOH D . 
N 4 HOH   53  353 686 HOH   HOH D . 
N 4 HOH   54  354 179 HOH   HOH D . 
N 4 HOH   55  355 726 HOH   HOH D . 
N 4 HOH   56  356 129 HOH   HOH D . 
N 4 HOH   57  357 620 HOH   HOH D . 
N 4 HOH   58  358 36  HOH   HOH D . 
N 4 HOH   59  359 17  HOH   HOH D . 
N 4 HOH   60  360 91  HOH   HOH D . 
N 4 HOH   61  361 376 HOH   HOH D . 
N 4 HOH   62  362 545 HOH   HOH D . 
N 4 HOH   63  363 49  HOH   HOH D . 
N 4 HOH   64  364 217 HOH   HOH D . 
N 4 HOH   65  365 32  HOH   HOH D . 
N 4 HOH   66  366 45  HOH   HOH D . 
N 4 HOH   67  367 747 HOH   HOH D . 
N 4 HOH   68  368 223 HOH   HOH D . 
N 4 HOH   69  369 455 HOH   HOH D . 
N 4 HOH   70  370 24  HOH   HOH D . 
N 4 HOH   71  371 239 HOH   HOH D . 
N 4 HOH   72  372 439 HOH   HOH D . 
N 4 HOH   73  373 427 HOH   HOH D . 
N 4 HOH   74  374 254 HOH   HOH D . 
N 4 HOH   75  375 449 HOH   HOH D . 
N 4 HOH   76  376 615 HOH   HOH D . 
N 4 HOH   77  377 317 HOH   HOH D . 
N 4 HOH   78  378 462 HOH   HOH D . 
N 4 HOH   79  379 697 HOH   HOH D . 
N 4 HOH   80  380 143 HOH   HOH D . 
N 4 HOH   81  381 80  HOH   HOH D . 
N 4 HOH   82  382 637 HOH   HOH D . 
N 4 HOH   83  383 165 HOH   HOH D . 
N 4 HOH   84  384 133 HOH   HOH D . 
N 4 HOH   85  385 164 HOH   HOH D . 
N 4 HOH   86  386 671 HOH   HOH D . 
N 4 HOH   87  387 506 HOH   HOH D . 
N 4 HOH   88  388 28  HOH   HOH D . 
N 4 HOH   89  389 246 HOH   HOH D . 
N 4 HOH   90  390 109 HOH   HOH D . 
N 4 HOH   91  391 201 HOH   HOH D . 
N 4 HOH   92  392 123 HOH   HOH D . 
N 4 HOH   93  393 94  HOH   HOH D . 
N 4 HOH   94  394 146 HOH   HOH D . 
N 4 HOH   95  395 619 HOH   HOH D . 
N 4 HOH   96  396 564 HOH   HOH D . 
N 4 HOH   97  397 277 HOH   HOH D . 
N 4 HOH   98  398 227 HOH   HOH D . 
N 4 HOH   99  399 188 HOH   HOH D . 
N 4 HOH   100 400 575 HOH   HOH D . 
N 4 HOH   101 401 401 HOH   HOH D . 
N 4 HOH   102 402 515 HOH   HOH D . 
N 4 HOH   103 403 685 HOH   HOH D . 
N 4 HOH   104 404 229 HOH   HOH D . 
N 4 HOH   105 405 88  HOH   HOH D . 
N 4 HOH   106 406 408 HOH   HOH D . 
N 4 HOH   107 407 679 HOH   HOH D . 
N 4 HOH   108 408 694 HOH   HOH D . 
N 4 HOH   109 409 147 HOH   HOH D . 
N 4 HOH   110 410 639 HOH   HOH D . 
N 4 HOH   111 411 77  HOH   HOH D . 
N 4 HOH   112 412 497 HOH   HOH D . 
N 4 HOH   113 413 175 HOH   HOH D . 
N 4 HOH   114 414 707 HOH   HOH D . 
N 4 HOH   115 415 320 HOH   HOH D . 
N 4 HOH   116 416 434 HOH   HOH D . 
N 4 HOH   117 417 120 HOH   HOH D . 
N 4 HOH   118 418 530 HOH   HOH D . 
N 4 HOH   119 419 553 HOH   HOH D . 
N 4 HOH   120 420 471 HOH   HOH D . 
N 4 HOH   121 421 121 HOH   HOH D . 
N 4 HOH   122 422 689 HOH   HOH D . 
N 4 HOH   123 423 482 HOH   HOH D . 
N 4 HOH   124 424 189 HOH   HOH D . 
N 4 HOH   125 425 389 HOH   HOH D . 
N 4 HOH   126 426 309 HOH   HOH D . 
N 4 HOH   127 427 684 HOH   HOH D . 
N 4 HOH   128 428 581 HOH   HOH D . 
N 4 HOH   129 429 662 HOH   HOH D . 
N 4 HOH   130 430 699 HOH   HOH D . 
N 4 HOH   131 431 521 HOH   HOH D . 
N 4 HOH   132 432 516 HOH   HOH D . 
N 4 HOH   133 433 281 HOH   HOH D . 
N 4 HOH   134 434 708 HOH   HOH D . 
N 4 HOH   135 435 638 HOH   HOH D . 
N 4 HOH   136 436 243 HOH   HOH D . 
N 4 HOH   137 437 370 HOH   HOH D . 
N 4 HOH   138 438 704 HOH   HOH D . 
N 4 HOH   139 439 610 HOH   HOH D . 
N 4 HOH   140 440 461 HOH   HOH D . 
N 4 HOH   141 441 536 HOH   HOH D . 
N 4 HOH   142 442 555 HOH   HOH D . 
N 4 HOH   143 443 203 HOH   HOH D . 
N 4 HOH   144 444 623 HOH   HOH D . 
N 4 HOH   145 445 213 HOH   HOH D . 
N 4 HOH   146 446 576 HOH   HOH D . 
N 4 HOH   147 447 618 HOH   HOH D . 
N 4 HOH   148 448 498 HOH   HOH D . 
N 4 HOH   149 449 663 HOH   HOH D . 
N 4 HOH   150 450 403 HOH   HOH D . 
N 4 HOH   151 451 423 HOH   HOH D . 
N 4 HOH   152 452 609 HOH   HOH D . 
N 4 HOH   153 453 222 HOH   HOH D . 
N 4 HOH   154 454 258 HOH   HOH D . 
N 4 HOH   155 455 730 HOH   HOH D . 
N 4 HOH   156 456 359 HOH   HOH D . 
N 4 HOH   157 457 437 HOH   HOH D . 
N 4 HOH   158 458 644 HOH   HOH D . 
N 4 HOH   159 459 688 HOH   HOH D . 
N 4 HOH   160 460 678 HOH   HOH D . 
N 4 HOH   161 461 622 HOH   HOH D . 
N 4 HOH   162 462 621 HOH   HOH D . 
N 4 HOH   163 463 635 HOH   HOH D . 
N 4 HOH   164 464 352 HOH   HOH D . 
N 4 HOH   165 465 664 HOH   HOH D . 
N 4 HOH   166 466 325 HOH   HOH D . 
N 4 HOH   167 467 739 HOH   HOH D . 
N 4 HOH   168 468 648 HOH   HOH D . 
N 4 HOH   169 469 731 HOH   HOH D . 
N 4 HOH   170 470 577 HOH   HOH D . 
N 4 HOH   171 471 741 HOH   HOH D . 
N 4 HOH   172 472 711 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 B PHE 29 ? N   B B PHE 15 N   
2  1 Y 0 B PHE 29 ? CA  B B PHE 15 CA  
3  1 Y 0 B PHE 29 ? C   B B PHE 15 C   
4  1 Y 0 B PHE 29 ? O   B B PHE 15 O   
5  1 Y 0 B PHE 29 ? CB  B B PHE 15 CB  
6  1 Y 0 B PHE 29 ? CG  B B PHE 15 CG  
7  1 Y 0 B PHE 29 ? CD1 B B PHE 15 CD1 
8  1 Y 0 B PHE 29 ? CD2 B B PHE 15 CD2 
9  1 Y 0 B PHE 29 ? CE1 B B PHE 15 CE1 
10 1 Y 0 B PHE 29 ? CE2 B B PHE 15 CE2 
11 1 Y 0 B PHE 29 ? CZ  B B PHE 15 CZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.19 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y26 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.000 
_cell.length_a_esd                 ? 
_cell.length_b                     85.768 
_cell.length_b_esd                 ? 
_cell.length_c                     58.421 
_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                         8Y26 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Y26 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.49 
_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    '0.1 M MES pH 6.0, 20% PEG 1000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX300HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-02-14 
_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   0.9 
_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                        'SPRING-8 BEAMLINE BL44XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL44XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Y26 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.23 
_reflns.d_resolution_low                               47.86 
_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                                     553345 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_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                                    1.23 
_reflns_shell.d_res_low                                     1.25 
_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                             6591 
_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                                  0.685 
_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                                 8Y26 
_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                            1.23 
_refine.ls_d_res_low                             46.40 
_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                     132140 
_refine.ls_number_reflns_R_free                  6588 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1468 
_refine.ls_R_factor_R_free                       0.1777 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1452 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 17.05 
_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                            0.12 
_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                       1.23 
_refine_hist.d_res_low                        46.40 
_refine_hist.number_atoms_solvent             747 
_refine_hist.number_atoms_total               4390 
_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        3579 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 3918 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.904  ? 5412 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.426 ? 1343 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.085  ? 605  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 683  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.23 1.24  . . 218 4192 100.00 . . . . 0.2356 . . . . . . . . . . . 0.2401 
'X-RAY DIFFRACTION' 1.24 1.26  . . 201 4191 100.00 . . . . 0.2293 . . . . . . . . . . . 0.2590 
'X-RAY DIFFRACTION' 1.26 1.27  . . 227 4177 100.00 . . . . 0.2301 . . . . . . . . . . . 0.2688 
'X-RAY DIFFRACTION' 1.27 1.29  . . 245 4103 100.00 . . . . 0.2216 . . . . . . . . . . . 0.2451 
'X-RAY DIFFRACTION' 1.29 1.31  . . 227 4219 100.00 . . . . 0.2213 . . . . . . . . . . . 0.2546 
'X-RAY DIFFRACTION' 1.31 1.32  . . 231 4158 100.00 . . . . 0.2083 . . . . . . . . . . . 0.2369 
'X-RAY DIFFRACTION' 1.32 1.34  . . 222 4185 100.00 . . . . 0.1969 . . . . . . . . . . . 0.2483 
'X-RAY DIFFRACTION' 1.34 1.36  . . 220 4146 100.00 . . . . 0.1803 . . . . . . . . . . . 0.2317 
'X-RAY DIFFRACTION' 1.36 1.39  . . 225 4196 100.00 . . . . 0.1736 . . . . . . . . . . . 0.2044 
'X-RAY DIFFRACTION' 1.39 1.41  . . 231 4129 100.00 . . . . 0.1578 . . . . . . . . . . . 0.1904 
'X-RAY DIFFRACTION' 1.41 1.43  . . 233 4171 100.00 . . . . 0.1555 . . . . . . . . . . . 0.2047 
'X-RAY DIFFRACTION' 1.43 1.46  . . 216 4205 100.00 . . . . 0.1451 . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 1.46 1.49  . . 218 4146 100.00 . . . . 0.1422 . . . . . . . . . . . 0.1647 
'X-RAY DIFFRACTION' 1.49 1.52  . . 202 4210 100.00 . . . . 0.1342 . . . . . . . . . . . 0.2013 
'X-RAY DIFFRACTION' 1.52 1.55  . . 198 4217 100.00 . . . . 0.1358 . . . . . . . . . . . 0.1615 
'X-RAY DIFFRACTION' 1.55 1.59  . . 200 4179 100.00 . . . . 0.1333 . . . . . . . . . . . 0.1697 
'X-RAY DIFFRACTION' 1.59 1.63  . . 227 4210 100.00 . . . . 0.1262 . . . . . . . . . . . 0.1688 
'X-RAY DIFFRACTION' 1.63 1.67  . . 216 4182 100.00 . . . . 0.1212 . . . . . . . . . . . 0.1492 
'X-RAY DIFFRACTION' 1.67 1.72  . . 219 4192 100.00 . . . . 0.1187 . . . . . . . . . . . 0.1545 
'X-RAY DIFFRACTION' 1.72 1.77  . . 217 4168 100.00 . . . . 0.1260 . . . . . . . . . . . 0.1710 
'X-RAY DIFFRACTION' 1.77 1.84  . . 205 4182 100.00 . . . . 0.1250 . . . . . . . . . . . 0.1573 
'X-RAY DIFFRACTION' 1.84 1.91  . . 226 4193 100.00 . . . . 0.1273 . . . . . . . . . . . 0.1842 
'X-RAY DIFFRACTION' 1.91 2.00  . . 231 4188 100.00 . . . . 0.1301 . . . . . . . . . . . 0.1621 
'X-RAY DIFFRACTION' 2.00 2.10  . . 217 4181 100.00 . . . . 0.1372 . . . . . . . . . . . 0.1778 
'X-RAY DIFFRACTION' 2.10 2.23  . . 244 4203 100.00 . . . . 0.1347 . . . . . . . . . . . 0.1579 
'X-RAY DIFFRACTION' 2.24 2.41  . . 197 4193 100.00 . . . . 0.1438 . . . . . . . . . . . 0.1731 
'X-RAY DIFFRACTION' 2.41 2.65  . . 224 4223 100.00 . . . . 0.1497 . . . . . . . . . . . 0.1672 
'X-RAY DIFFRACTION' 2.65 3.03  . . 232 4198 100.00 . . . . 0.1496 . . . . . . . . . . . 0.1909 
'X-RAY DIFFRACTION' 3.03 3.82  . . 210 4219 100.00 . . . . 0.1384 . . . . . . . . . . . 0.1558 
'X-RAY DIFFRACTION' 3.82 46.40 . . 209 4196 98.00  . . . . 0.1458 . . . . . . . . . . . 0.1763 
# 
_struct.entry_id                     8Y26 
_struct.title                        
'X-ray crystal structure of ALiS5-Streptavidine complex without cryo-protectant using a high-pressure cryocooling method' 
_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        8Y26 
_struct_keywords.text            'streptavidin, CYTOSOLIC PROTEIN' 
_struct_keywords.pdbx_keywords   'CYTOSOLIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 2 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SAV_STRAV 
_struct_ref.pdbx_db_accession          P22629 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLTGRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSG
QYVGGAEARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKP
;
_struct_ref.pdbx_align_begin           39 
# 
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 8Y26 A 1 ? 121 ? P22629 39 ? 159 ? 15 135 
2 1 8Y26 B 1 ? 121 ? P22629 39 ? 159 ? 15 135 
3 1 8Y26 C 1 ? 121 ? P22629 39 ? 159 ? 15 135 
4 1 8Y26 D 1 ? 121 ? P22629 39 ? 159 ? 15 135 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 10150 ? 
1 MORE         -40   ? 
1 'SSA (A^2)'  19180 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 THR A 101 ? LYS A 107 ? THR A 115 LYS A 121 5 ? 7 
HELX_P HELX_P2 AA2 ASN B 35  ? GLU B 37  ? ASN B 49  GLU B 51  5 ? 3 
HELX_P HELX_P3 AA3 THR B 101 ? LYS B 107 ? THR B 115 LYS B 121 5 ? 7 
HELX_P HELX_P4 AA4 THR C 101 ? LYS C 107 ? THR C 115 LYS C 121 5 ? 7 
HELX_P HELX_P5 AA5 ASN D 35  ? ARG D 39  ? ASN D 49  ARG D 53  5 ? 5 
HELX_P HELX_P6 AA6 THR D 101 ? LYS D 107 ? THR D 115 LYS D 121 5 ? 7 
# 
_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 ? 9 ? 
AA2 ? 9 ? 
AA3 ? 9 ? 
AA4 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA2 8 9 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA3 8 9 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA4 7 8 ? anti-parallel 
AA4 8 9 ? 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 GLY A 5   ? ASN A 9   ? GLY A 19  ASN A 23  
AA1 2 THR A 14  ? ALA A 19  ? THR A 28  ALA A 33  
AA1 3 ALA A 24  ? GLU A 30  ? ALA A 38  GLU A 44  
AA1 4 TYR A 40  ? TYR A 46  ? TYR A 54  TYR A 60  
AA1 5 THR A 57  ? LYS A 66  ? THR A 71  LYS A 80  
AA1 6 ASN A 71  ? VAL A 83  ? ASN A 85  VAL A 97  
AA1 7 ARG A 89  ? SER A 98  ? ARG A 103 SER A 112 
AA1 8 THR A 109 ? THR A 117 ? THR A 123 THR A 131 
AA1 9 GLY A 5   ? ASN A 9   ? GLY A 19  ASN A 23  
AA2 1 GLY B 5   ? TYR B 8   ? GLY B 19  TYR B 22  
AA2 2 THR B 14  ? ALA B 19  ? THR B 28  ALA B 33  
AA2 3 ALA B 24  ? GLU B 30  ? ALA B 38  GLU B 44  
AA2 4 ARG B 39  ? TYR B 46  ? ARG B 53  TYR B 60  
AA2 5 THR B 57  ? LYS B 66  ? THR B 71  LYS B 80  
AA2 6 ASN B 71  ? VAL B 83  ? ASN B 85  VAL B 97  
AA2 7 ARG B 89  ? SER B 98  ? ARG B 103 SER B 112 
AA2 8 THR B 109 ? THR B 117 ? THR B 123 THR B 131 
AA2 9 GLY B 5   ? TYR B 8   ? GLY B 19  TYR B 22  
AA3 1 GLY C 5   ? ASN C 9   ? GLY C 19  ASN C 23  
AA3 2 THR C 14  ? ALA C 19  ? THR C 28  ALA C 33  
AA3 3 ALA C 24  ? GLU C 30  ? ALA C 38  GLU C 44  
AA3 4 TYR C 40  ? TYR C 46  ? TYR C 54  TYR C 60  
AA3 5 THR C 57  ? LYS C 66  ? THR C 71  LYS C 80  
AA3 6 ASN C 71  ? VAL C 83  ? ASN C 85  VAL C 97  
AA3 7 ARG C 89  ? SER C 98  ? ARG C 103 SER C 112 
AA3 8 THR C 109 ? THR C 117 ? THR C 123 THR C 131 
AA3 9 GLY C 5   ? ASN C 9   ? GLY C 19  ASN C 23  
AA4 1 GLY D 5   ? ASN D 9   ? GLY D 19  ASN D 23  
AA4 2 THR D 14  ? ALA D 19  ? THR D 28  ALA D 33  
AA4 3 ALA D 24  ? GLU D 30  ? ALA D 38  GLU D 44  
AA4 4 TYR D 40  ? TYR D 46  ? TYR D 54  TYR D 60  
AA4 5 THR D 57  ? LYS D 66  ? THR D 71  LYS D 80  
AA4 6 ASN D 71  ? VAL D 83  ? ASN D 85  VAL D 97  
AA4 7 ARG D 89  ? SER D 98  ? ARG D 103 SER D 112 
AA4 8 THR D 109 ? THR D 117 ? THR D 123 THR D 131 
AA4 9 GLY D 5   ? ASN D 9   ? GLY D 19  ASN D 23  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 7   ? N TRP A 21  O PHE A 15  ? O PHE A 29  
AA1 2 3 N ILE A 16  ? N ILE A 30  O THR A 28  ? O THR A 42  
AA1 3 4 N LEU A 25  ? N LEU A 39  O GLY A 44  ? O GLY A 58  
AA1 4 5 N THR A 43  ? N THR A 57  O THR A 62  ? O THR A 76  
AA1 5 6 N TRP A 65  ? N TRP A 79  O SER A 74  ? O SER A 88  
AA1 6 7 N VAL A 83  ? N VAL A 97  O ARG A 89  ? O ARG A 103 
AA1 7 8 N ILE A 90  ? N ILE A 104 O PHE A 116 ? O PHE A 130 
AA1 8 9 O THR A 117 ? O THR A 131 N TYR A 8   ? N TYR A 22  
AA2 1 2 N TRP B 7   ? N TRP B 21  O PHE B 15  ? O PHE B 29  
AA2 2 3 N ILE B 16  ? N ILE B 30  O THR B 28  ? O THR B 42  
AA2 3 4 N TYR B 29  ? N TYR B 43  O TYR B 40  ? O TYR B 54  
AA2 4 5 N THR B 43  ? N THR B 57  O THR B 62  ? O THR B 76  
AA2 5 6 N TRP B 61  ? N TRP B 75  O TRP B 78  ? O TRP B 92  
AA2 6 7 N VAL B 83  ? N VAL B 97  O ARG B 89  ? O ARG B 103 
AA2 7 8 N TRP B 94  ? N TRP B 108 O GLY B 112 ? O GLY B 126 
AA2 8 9 O THR B 117 ? O THR B 131 N TYR B 8   ? N TYR B 22  
AA3 1 2 N TRP C 7   ? N TRP C 21  O PHE C 15  ? O PHE C 29  
AA3 2 3 N ILE C 16  ? N ILE C 30  O THR C 28  ? O THR C 42  
AA3 3 4 N LEU C 25  ? N LEU C 39  O GLY C 44  ? O GLY C 58  
AA3 4 5 N THR C 43  ? N THR C 57  O THR C 62  ? O THR C 76  
AA3 5 6 N THR C 57  ? N THR C 71  O TYR C 82  ? O TYR C 96  
AA3 6 7 N VAL C 83  ? N VAL C 97  O ARG C 89  ? O ARG C 103 
AA3 7 8 N ILE C 90  ? N ILE C 104 O PHE C 116 ? O PHE C 130 
AA3 8 9 O THR C 117 ? O THR C 131 N TYR C 8   ? N TYR C 22  
AA4 1 2 N TRP D 7   ? N TRP D 21  O PHE D 15  ? O PHE D 29  
AA4 2 3 N ILE D 16  ? N ILE D 30  O THR D 28  ? O THR D 42  
AA4 3 4 N TYR D 29  ? N TYR D 43  O TYR D 40  ? O TYR D 54  
AA4 4 5 N THR D 43  ? N THR D 57  O THR D 62  ? O THR D 76  
AA4 5 6 N TRP D 65  ? N TRP D 79  O SER D 74  ? O SER D 88  
AA4 6 7 N VAL D 83  ? N VAL D 97  O ARG D 89  ? O ARG D 103 
AA4 7 8 N ILE D 90  ? N ILE D 104 O PHE D 116 ? O PHE D 130 
AA4 8 9 O THR D 117 ? O THR D 131 N TYR D 8   ? N TYR D 22  
# 
_pdbx_entry_details.entry_id                   8Y26 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 52  ? ? 63.50   -159.54 
2 1 THR B 66  ? ? -113.73 53.30   
3 1 THR B 66  ? ? -114.28 54.00   
4 1 SER C 52  ? ? 63.69   -168.78 
5 1 GLU D 101 ? ? -114.84 56.73   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 613 ? 5.81 .    
2  1 O ? A HOH 614 ? 6.40 .    
3  1 O ? A HOH 615 ? 6.67 .    
4  1 O ? A HOH 616 ? 6.82 .    
5  1 O ? A HOH 617 ? 6.83 .    
6  1 O ? A HOH 618 ? 7.52 .    
7  1 O ? B HOH 454 ? 5.83 .    
8  1 O ? B HOH 455 ? 6.37 .    
9  1 O ? C HOH 600 ? 5.92 .    
10 1 O ? C HOH 601 ? 6.74 .    
11 1 O ? C HOH 602 ? 7.23 .    
12 1 O ? D HOH 468 ? 5.88 .    
13 1 O ? D HOH 469 ? 6.20 .    
14 1 O ? D HOH 470 ? 6.31 .    
15 1 O ? D HOH 471 ? .    6.89 
16 1 O ? D HOH 472 ? 7.57 .    
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 B ALA 46  ? B ALA 32  
2 1 Y 1 B VAL 47  ? B VAL 33  
3 1 Y 1 B GLY 48  ? B GLY 34  
4 1 Y 1 B PRO 135 ? B PRO 121 
5 1 Y 1 C ALA 15  ? C ALA 1   
6 1 Y 1 D PRO 135 ? D PRO 121 
# 
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 
A1LXQ C1   C Y N 1   
A1LXQ C10  C Y N 2   
A1LXQ C11  C N N 3   
A1LXQ C12  C N N 4   
A1LXQ C13  C N N 5   
A1LXQ C14  C N N 6   
A1LXQ C15  C N N 7   
A1LXQ C16  C N N 8   
A1LXQ C17  C N N 9   
A1LXQ C2   C Y N 10  
A1LXQ C3   C Y N 11  
A1LXQ C4   C Y N 12  
A1LXQ C5   C Y N 13  
A1LXQ C6   C Y N 14  
A1LXQ C7   C Y N 15  
A1LXQ C8   C Y N 16  
A1LXQ C9   C Y N 17  
A1LXQ N1   N N N 18  
A1LXQ O1   O Y N 19  
A1LXQ O2   O N N 20  
A1LXQ O3   O N N 21  
A1LXQ O4   O N N 22  
A1LXQ O5   O N N 23  
A1LXQ O6   O N N 24  
A1LXQ H1   H N N 25  
A1LXQ H2   H N N 26  
A1LXQ H3   H N N 27  
A1LXQ H5   H N N 28  
A1LXQ H6   H N N 29  
A1LXQ H7   H N N 30  
A1LXQ H8   H N N 31  
A1LXQ H9   H N N 32  
A1LXQ H10  H N N 33  
A1LXQ H11  H N N 34  
A1LXQ H12  H N N 35  
A1LXQ H13  H N N 36  
A1LXQ H4   H N N 37  
ALA   N    N N N 38  
ALA   CA   C N S 39  
ALA   C    C N N 40  
ALA   O    O N N 41  
ALA   CB   C N N 42  
ALA   OXT  O N N 43  
ALA   H    H N N 44  
ALA   H2   H N N 45  
ALA   HA   H N N 46  
ALA   HB1  H N N 47  
ALA   HB2  H N N 48  
ALA   HB3  H N N 49  
ALA   HXT  H N N 50  
ARG   N    N N N 51  
ARG   CA   C N S 52  
ARG   C    C N N 53  
ARG   O    O N N 54  
ARG   CB   C N N 55  
ARG   CG   C N N 56  
ARG   CD   C N N 57  
ARG   NE   N N N 58  
ARG   CZ   C N N 59  
ARG   NH1  N N N 60  
ARG   NH2  N N N 61  
ARG   OXT  O N N 62  
ARG   H    H N N 63  
ARG   H2   H N N 64  
ARG   HA   H N N 65  
ARG   HB2  H N N 66  
ARG   HB3  H N N 67  
ARG   HG2  H N N 68  
ARG   HG3  H N N 69  
ARG   HD2  H N N 70  
ARG   HD3  H N N 71  
ARG   HE   H N N 72  
ARG   HH11 H N N 73  
ARG   HH12 H N N 74  
ARG   HH21 H N N 75  
ARG   HH22 H N N 76  
ARG   HXT  H N N 77  
ASN   N    N N N 78  
ASN   CA   C N S 79  
ASN   C    C N N 80  
ASN   O    O N N 81  
ASN   CB   C N N 82  
ASN   CG   C N N 83  
ASN   OD1  O N N 84  
ASN   ND2  N N N 85  
ASN   OXT  O N N 86  
ASN   H    H N N 87  
ASN   H2   H N N 88  
ASN   HA   H N N 89  
ASN   HB2  H N N 90  
ASN   HB3  H N N 91  
ASN   HD21 H N N 92  
ASN   HD22 H N N 93  
ASN   HXT  H N N 94  
ASP   N    N N N 95  
ASP   CA   C N S 96  
ASP   C    C N N 97  
ASP   O    O N N 98  
ASP   CB   C N N 99  
ASP   CG   C N N 100 
ASP   OD1  O N N 101 
ASP   OD2  O N N 102 
ASP   OXT  O N N 103 
ASP   H    H N N 104 
ASP   H2   H N N 105 
ASP   HA   H N N 106 
ASP   HB2  H N N 107 
ASP   HB3  H N N 108 
ASP   HD2  H N N 109 
ASP   HXT  H N N 110 
DMS   S    S N N 111 
DMS   O    O N N 112 
DMS   C1   C N N 113 
DMS   C2   C N N 114 
DMS   H11  H N N 115 
DMS   H12  H N N 116 
DMS   H13  H N N 117 
DMS   H21  H N N 118 
DMS   H22  H N N 119 
DMS   H23  H N N 120 
GLN   N    N N N 121 
GLN   CA   C N S 122 
GLN   C    C N N 123 
GLN   O    O N N 124 
GLN   CB   C N N 125 
GLN   CG   C N N 126 
GLN   CD   C N N 127 
GLN   OE1  O N N 128 
GLN   NE2  N N N 129 
GLN   OXT  O N N 130 
GLN   H    H N N 131 
GLN   H2   H N N 132 
GLN   HA   H N N 133 
GLN   HB2  H N N 134 
GLN   HB3  H N N 135 
GLN   HG2  H N N 136 
GLN   HG3  H N N 137 
GLN   HE21 H N N 138 
GLN   HE22 H N N 139 
GLN   HXT  H N N 140 
GLU   N    N N N 141 
GLU   CA   C N S 142 
GLU   C    C N N 143 
GLU   O    O N N 144 
GLU   CB   C N N 145 
GLU   CG   C N N 146 
GLU   CD   C N N 147 
GLU   OE1  O N N 148 
GLU   OE2  O N N 149 
GLU   OXT  O N N 150 
GLU   H    H N N 151 
GLU   H2   H N N 152 
GLU   HA   H N N 153 
GLU   HB2  H N N 154 
GLU   HB3  H N N 155 
GLU   HG2  H N N 156 
GLU   HG3  H N N 157 
GLU   HE2  H N N 158 
GLU   HXT  H N N 159 
GLY   N    N N N 160 
GLY   CA   C N N 161 
GLY   C    C N N 162 
GLY   O    O N N 163 
GLY   OXT  O N N 164 
GLY   H    H N N 165 
GLY   H2   H N N 166 
GLY   HA2  H N N 167 
GLY   HA3  H N N 168 
GLY   HXT  H N N 169 
HIS   N    N N N 170 
HIS   CA   C N S 171 
HIS   C    C N N 172 
HIS   O    O N N 173 
HIS   CB   C N N 174 
HIS   CG   C Y N 175 
HIS   ND1  N Y N 176 
HIS   CD2  C Y N 177 
HIS   CE1  C Y N 178 
HIS   NE2  N Y N 179 
HIS   OXT  O N N 180 
HIS   H    H N N 181 
HIS   H2   H N N 182 
HIS   HA   H N N 183 
HIS   HB2  H N N 184 
HIS   HB3  H N N 185 
HIS   HD1  H N N 186 
HIS   HD2  H N N 187 
HIS   HE1  H N N 188 
HIS   HE2  H N N 189 
HIS   HXT  H N N 190 
HOH   O    O N N 191 
HOH   H1   H N N 192 
HOH   H2   H N N 193 
ILE   N    N N N 194 
ILE   CA   C N S 195 
ILE   C    C N N 196 
ILE   O    O N N 197 
ILE   CB   C N S 198 
ILE   CG1  C N N 199 
ILE   CG2  C N N 200 
ILE   CD1  C N N 201 
ILE   OXT  O N N 202 
ILE   H    H N N 203 
ILE   H2   H N N 204 
ILE   HA   H N N 205 
ILE   HB   H N N 206 
ILE   HG12 H N N 207 
ILE   HG13 H N N 208 
ILE   HG21 H N N 209 
ILE   HG22 H N N 210 
ILE   HG23 H N N 211 
ILE   HD11 H N N 212 
ILE   HD12 H N N 213 
ILE   HD13 H N N 214 
ILE   HXT  H N N 215 
LEU   N    N N N 216 
LEU   CA   C N S 217 
LEU   C    C N N 218 
LEU   O    O N N 219 
LEU   CB   C N N 220 
LEU   CG   C N N 221 
LEU   CD1  C N N 222 
LEU   CD2  C N N 223 
LEU   OXT  O N N 224 
LEU   H    H N N 225 
LEU   H2   H N N 226 
LEU   HA   H N N 227 
LEU   HB2  H N N 228 
LEU   HB3  H N N 229 
LEU   HG   H N N 230 
LEU   HD11 H N N 231 
LEU   HD12 H N N 232 
LEU   HD13 H N N 233 
LEU   HD21 H N N 234 
LEU   HD22 H N N 235 
LEU   HD23 H N N 236 
LEU   HXT  H N N 237 
LYS   N    N N N 238 
LYS   CA   C N S 239 
LYS   C    C N N 240 
LYS   O    O N N 241 
LYS   CB   C N N 242 
LYS   CG   C N N 243 
LYS   CD   C N N 244 
LYS   CE   C N N 245 
LYS   NZ   N N N 246 
LYS   OXT  O N N 247 
LYS   H    H N N 248 
LYS   H2   H N N 249 
LYS   HA   H N N 250 
LYS   HB2  H N N 251 
LYS   HB3  H N N 252 
LYS   HG2  H N N 253 
LYS   HG3  H N N 254 
LYS   HD2  H N N 255 
LYS   HD3  H N N 256 
LYS   HE2  H N N 257 
LYS   HE3  H N N 258 
LYS   HZ1  H N N 259 
LYS   HZ2  H N N 260 
LYS   HZ3  H N N 261 
LYS   HXT  H N N 262 
PHE   N    N N N 263 
PHE   CA   C N S 264 
PHE   C    C N N 265 
PHE   O    O N N 266 
PHE   CB   C N N 267 
PHE   CG   C Y N 268 
PHE   CD1  C Y N 269 
PHE   CD2  C Y N 270 
PHE   CE1  C Y N 271 
PHE   CE2  C Y N 272 
PHE   CZ   C Y N 273 
PHE   OXT  O N N 274 
PHE   H    H N N 275 
PHE   H2   H N N 276 
PHE   HA   H N N 277 
PHE   HB2  H N N 278 
PHE   HB3  H N N 279 
PHE   HD1  H N N 280 
PHE   HD2  H N N 281 
PHE   HE1  H N N 282 
PHE   HE2  H N N 283 
PHE   HZ   H N N 284 
PHE   HXT  H N N 285 
PRO   N    N N N 286 
PRO   CA   C N S 287 
PRO   C    C N N 288 
PRO   O    O N N 289 
PRO   CB   C N N 290 
PRO   CG   C N N 291 
PRO   CD   C N N 292 
PRO   OXT  O N N 293 
PRO   H    H N N 294 
PRO   HA   H N N 295 
PRO   HB2  H N N 296 
PRO   HB3  H N N 297 
PRO   HG2  H N N 298 
PRO   HG3  H N N 299 
PRO   HD2  H N N 300 
PRO   HD3  H N N 301 
PRO   HXT  H N N 302 
SER   N    N N N 303 
SER   CA   C N S 304 
SER   C    C N N 305 
SER   O    O N N 306 
SER   CB   C N N 307 
SER   OG   O N N 308 
SER   OXT  O N N 309 
SER   H    H N N 310 
SER   H2   H N N 311 
SER   HA   H N N 312 
SER   HB2  H N N 313 
SER   HB3  H N N 314 
SER   HG   H N N 315 
SER   HXT  H N N 316 
THR   N    N N N 317 
THR   CA   C N S 318 
THR   C    C N N 319 
THR   O    O N N 320 
THR   CB   C N R 321 
THR   OG1  O N N 322 
THR   CG2  C N N 323 
THR   OXT  O N N 324 
THR   H    H N N 325 
THR   H2   H N N 326 
THR   HA   H N N 327 
THR   HB   H N N 328 
THR   HG1  H N N 329 
THR   HG21 H N N 330 
THR   HG22 H N N 331 
THR   HG23 H N N 332 
THR   HXT  H N N 333 
TRP   N    N N N 334 
TRP   CA   C N S 335 
TRP   C    C N N 336 
TRP   O    O N N 337 
TRP   CB   C N N 338 
TRP   CG   C Y N 339 
TRP   CD1  C Y N 340 
TRP   CD2  C Y N 341 
TRP   NE1  N Y N 342 
TRP   CE2  C Y N 343 
TRP   CE3  C Y N 344 
TRP   CZ2  C Y N 345 
TRP   CZ3  C Y N 346 
TRP   CH2  C Y N 347 
TRP   OXT  O N N 348 
TRP   H    H N N 349 
TRP   H2   H N N 350 
TRP   HA   H N N 351 
TRP   HB2  H N N 352 
TRP   HB3  H N N 353 
TRP   HD1  H N N 354 
TRP   HE1  H N N 355 
TRP   HE3  H N N 356 
TRP   HZ2  H N N 357 
TRP   HZ3  H N N 358 
TRP   HH2  H N N 359 
TRP   HXT  H N N 360 
TYR   N    N N N 361 
TYR   CA   C N S 362 
TYR   C    C N N 363 
TYR   O    O N N 364 
TYR   CB   C N N 365 
TYR   CG   C Y N 366 
TYR   CD1  C Y N 367 
TYR   CD2  C Y N 368 
TYR   CE1  C Y N 369 
TYR   CE2  C Y N 370 
TYR   CZ   C Y N 371 
TYR   OH   O N N 372 
TYR   OXT  O N N 373 
TYR   H    H N N 374 
TYR   H2   H N N 375 
TYR   HA   H N N 376 
TYR   HB2  H N N 377 
TYR   HB3  H N N 378 
TYR   HD1  H N N 379 
TYR   HD2  H N N 380 
TYR   HE1  H N N 381 
TYR   HE2  H N N 382 
TYR   HH   H N N 383 
TYR   HXT  H N N 384 
VAL   N    N N N 385 
VAL   CA   C N S 386 
VAL   C    C N N 387 
VAL   O    O N N 388 
VAL   CB   C N N 389 
VAL   CG1  C N N 390 
VAL   CG2  C N N 391 
VAL   OXT  O N N 392 
VAL   H    H N N 393 
VAL   H2   H N N 394 
VAL   HA   H N N 395 
VAL   HB   H N N 396 
VAL   HG11 H N N 397 
VAL   HG12 H N N 398 
VAL   HG13 H N N 399 
VAL   HG21 H N N 400 
VAL   HG22 H N N 401 
VAL   HG23 H N N 402 
VAL   HXT  H N N 403 
# 
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 
A1LXQ C15 O4   sing N N 1   
A1LXQ O4  C14  sing N N 2   
A1LXQ C14 O3   doub N N 3   
A1LXQ C14 C6   sing N N 4   
A1LXQ C13 C12  doub N N 5   
A1LXQ C13 C10  sing N N 6   
A1LXQ C12 N1   sing N N 7   
A1LXQ O1  C10  sing Y N 8   
A1LXQ O1  C7   sing Y N 9   
A1LXQ C5  C6   doub Y N 10  
A1LXQ C5  C4   sing Y N 11  
A1LXQ C6  C1   sing Y N 12  
A1LXQ C10 C9   doub Y N 13  
A1LXQ C7  C4   sing N N 14  
A1LXQ C7  C8   doub Y N 15  
A1LXQ C4  C3   doub Y N 16  
A1LXQ N1  C11  sing N N 17  
A1LXQ C1  C2   doub Y N 18  
A1LXQ C9  C11  sing N N 19  
A1LXQ C9  C8   sing Y N 20  
A1LXQ C11 O2   doub N N 21  
A1LXQ C3  C2   sing Y N 22  
A1LXQ C2  C16  sing N N 23  
A1LXQ O6  C16  sing N N 24  
A1LXQ O6  C17  sing N N 25  
A1LXQ C16 O5   doub N N 26  
A1LXQ C1  H1   sing N N 27  
A1LXQ C12 H2   sing N N 28  
A1LXQ C13 H3   sing N N 29  
A1LXQ C15 H5   sing N N 30  
A1LXQ C15 H6   sing N N 31  
A1LXQ C15 H7   sing N N 32  
A1LXQ C17 H8   sing N N 33  
A1LXQ C17 H9   sing N N 34  
A1LXQ C17 H10  sing N N 35  
A1LXQ C3  H11  sing N N 36  
A1LXQ C5  H12  sing N N 37  
A1LXQ C8  H13  sing N N 38  
A1LXQ N1  H4   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
DMS   S   O    doub N N 109 
DMS   S   C1   sing N N 110 
DMS   S   C2   sing N N 111 
DMS   C1  H11  sing N N 112 
DMS   C1  H12  sing N N 113 
DMS   C1  H13  sing N N 114 
DMS   C2  H21  sing N N 115 
DMS   C2  H22  sing N N 116 
DMS   C2  H23  sing N N 117 
GLN   N   CA   sing N N 118 
GLN   N   H    sing N N 119 
GLN   N   H2   sing N N 120 
GLN   CA  C    sing N N 121 
GLN   CA  CB   sing N N 122 
GLN   CA  HA   sing N N 123 
GLN   C   O    doub N N 124 
GLN   C   OXT  sing N N 125 
GLN   CB  CG   sing N N 126 
GLN   CB  HB2  sing N N 127 
GLN   CB  HB3  sing N N 128 
GLN   CG  CD   sing N N 129 
GLN   CG  HG2  sing N N 130 
GLN   CG  HG3  sing N N 131 
GLN   CD  OE1  doub N N 132 
GLN   CD  NE2  sing N N 133 
GLN   NE2 HE21 sing N N 134 
GLN   NE2 HE22 sing N N 135 
GLN   OXT HXT  sing N N 136 
GLU   N   CA   sing N N 137 
GLU   N   H    sing N N 138 
GLU   N   H2   sing N N 139 
GLU   CA  C    sing N N 140 
GLU   CA  CB   sing N N 141 
GLU   CA  HA   sing N N 142 
GLU   C   O    doub N N 143 
GLU   C   OXT  sing N N 144 
GLU   CB  CG   sing N N 145 
GLU   CB  HB2  sing N N 146 
GLU   CB  HB3  sing N N 147 
GLU   CG  CD   sing N N 148 
GLU   CG  HG2  sing N N 149 
GLU   CG  HG3  sing N N 150 
GLU   CD  OE1  doub N N 151 
GLU   CD  OE2  sing N N 152 
GLU   OE2 HE2  sing N N 153 
GLU   OXT HXT  sing N N 154 
GLY   N   CA   sing N N 155 
GLY   N   H    sing N N 156 
GLY   N   H2   sing N N 157 
GLY   CA  C    sing N N 158 
GLY   CA  HA2  sing N N 159 
GLY   CA  HA3  sing N N 160 
GLY   C   O    doub N N 161 
GLY   C   OXT  sing N N 162 
GLY   OXT HXT  sing N N 163 
HIS   N   CA   sing N N 164 
HIS   N   H    sing N N 165 
HIS   N   H2   sing N N 166 
HIS   CA  C    sing N N 167 
HIS   CA  CB   sing N N 168 
HIS   CA  HA   sing N N 169 
HIS   C   O    doub N N 170 
HIS   C   OXT  sing N N 171 
HIS   CB  CG   sing N N 172 
HIS   CB  HB2  sing N N 173 
HIS   CB  HB3  sing N N 174 
HIS   CG  ND1  sing Y N 175 
HIS   CG  CD2  doub Y N 176 
HIS   ND1 CE1  doub Y N 177 
HIS   ND1 HD1  sing N N 178 
HIS   CD2 NE2  sing Y N 179 
HIS   CD2 HD2  sing N N 180 
HIS   CE1 NE2  sing Y N 181 
HIS   CE1 HE1  sing N N 182 
HIS   NE2 HE2  sing N N 183 
HIS   OXT HXT  sing N N 184 
HOH   O   H1   sing N N 185 
HOH   O   H2   sing N N 186 
ILE   N   CA   sing N N 187 
ILE   N   H    sing N N 188 
ILE   N   H2   sing N N 189 
ILE   CA  C    sing N N 190 
ILE   CA  CB   sing N N 191 
ILE   CA  HA   sing N N 192 
ILE   C   O    doub N N 193 
ILE   C   OXT  sing N N 194 
ILE   CB  CG1  sing N N 195 
ILE   CB  CG2  sing N N 196 
ILE   CB  HB   sing N N 197 
ILE   CG1 CD1  sing N N 198 
ILE   CG1 HG12 sing N N 199 
ILE   CG1 HG13 sing N N 200 
ILE   CG2 HG21 sing N N 201 
ILE   CG2 HG22 sing N N 202 
ILE   CG2 HG23 sing N N 203 
ILE   CD1 HD11 sing N N 204 
ILE   CD1 HD12 sing N N 205 
ILE   CD1 HD13 sing N N 206 
ILE   OXT HXT  sing N N 207 
LEU   N   CA   sing N N 208 
LEU   N   H    sing N N 209 
LEU   N   H2   sing N N 210 
LEU   CA  C    sing N N 211 
LEU   CA  CB   sing N N 212 
LEU   CA  HA   sing N N 213 
LEU   C   O    doub N N 214 
LEU   C   OXT  sing N N 215 
LEU   CB  CG   sing N N 216 
LEU   CB  HB2  sing N N 217 
LEU   CB  HB3  sing N N 218 
LEU   CG  CD1  sing N N 219 
LEU   CG  CD2  sing N N 220 
LEU   CG  HG   sing N N 221 
LEU   CD1 HD11 sing N N 222 
LEU   CD1 HD12 sing N N 223 
LEU   CD1 HD13 sing N N 224 
LEU   CD2 HD21 sing N N 225 
LEU   CD2 HD22 sing N N 226 
LEU   CD2 HD23 sing N N 227 
LEU   OXT HXT  sing N N 228 
LYS   N   CA   sing N N 229 
LYS   N   H    sing N N 230 
LYS   N   H2   sing N N 231 
LYS   CA  C    sing N N 232 
LYS   CA  CB   sing N N 233 
LYS   CA  HA   sing N N 234 
LYS   C   O    doub N N 235 
LYS   C   OXT  sing N N 236 
LYS   CB  CG   sing N N 237 
LYS   CB  HB2  sing N N 238 
LYS   CB  HB3  sing N N 239 
LYS   CG  CD   sing N N 240 
LYS   CG  HG2  sing N N 241 
LYS   CG  HG3  sing N N 242 
LYS   CD  CE   sing N N 243 
LYS   CD  HD2  sing N N 244 
LYS   CD  HD3  sing N N 245 
LYS   CE  NZ   sing N N 246 
LYS   CE  HE2  sing N N 247 
LYS   CE  HE3  sing N N 248 
LYS   NZ  HZ1  sing N N 249 
LYS   NZ  HZ2  sing N N 250 
LYS   NZ  HZ3  sing N N 251 
LYS   OXT HXT  sing N N 252 
PHE   N   CA   sing N N 253 
PHE   N   H    sing N N 254 
PHE   N   H2   sing N N 255 
PHE   CA  C    sing N N 256 
PHE   CA  CB   sing N N 257 
PHE   CA  HA   sing N N 258 
PHE   C   O    doub N N 259 
PHE   C   OXT  sing N N 260 
PHE   CB  CG   sing N N 261 
PHE   CB  HB2  sing N N 262 
PHE   CB  HB3  sing N N 263 
PHE   CG  CD1  doub Y N 264 
PHE   CG  CD2  sing Y N 265 
PHE   CD1 CE1  sing Y N 266 
PHE   CD1 HD1  sing N N 267 
PHE   CD2 CE2  doub Y N 268 
PHE   CD2 HD2  sing N N 269 
PHE   CE1 CZ   doub Y N 270 
PHE   CE1 HE1  sing N N 271 
PHE   CE2 CZ   sing Y N 272 
PHE   CE2 HE2  sing N N 273 
PHE   CZ  HZ   sing N N 274 
PHE   OXT HXT  sing N N 275 
PRO   N   CA   sing N N 276 
PRO   N   CD   sing N N 277 
PRO   N   H    sing N N 278 
PRO   CA  C    sing N N 279 
PRO   CA  CB   sing N N 280 
PRO   CA  HA   sing N N 281 
PRO   C   O    doub N N 282 
PRO   C   OXT  sing N N 283 
PRO   CB  CG   sing N N 284 
PRO   CB  HB2  sing N N 285 
PRO   CB  HB3  sing N N 286 
PRO   CG  CD   sing N N 287 
PRO   CG  HG2  sing N N 288 
PRO   CG  HG3  sing N N 289 
PRO   CD  HD2  sing N N 290 
PRO   CD  HD3  sing N N 291 
PRO   OXT HXT  sing N N 292 
SER   N   CA   sing N N 293 
SER   N   H    sing N N 294 
SER   N   H2   sing N N 295 
SER   CA  C    sing N N 296 
SER   CA  CB   sing N N 297 
SER   CA  HA   sing N N 298 
SER   C   O    doub N N 299 
SER   C   OXT  sing N N 300 
SER   CB  OG   sing N N 301 
SER   CB  HB2  sing N N 302 
SER   CB  HB3  sing N N 303 
SER   OG  HG   sing N N 304 
SER   OXT HXT  sing N N 305 
THR   N   CA   sing N N 306 
THR   N   H    sing N N 307 
THR   N   H2   sing N N 308 
THR   CA  C    sing N N 309 
THR   CA  CB   sing N N 310 
THR   CA  HA   sing N N 311 
THR   C   O    doub N N 312 
THR   C   OXT  sing N N 313 
THR   CB  OG1  sing N N 314 
THR   CB  CG2  sing N N 315 
THR   CB  HB   sing N N 316 
THR   OG1 HG1  sing N N 317 
THR   CG2 HG21 sing N N 318 
THR   CG2 HG22 sing N N 319 
THR   CG2 HG23 sing N N 320 
THR   OXT HXT  sing N N 321 
TRP   N   CA   sing N N 322 
TRP   N   H    sing N N 323 
TRP   N   H2   sing N N 324 
TRP   CA  C    sing N N 325 
TRP   CA  CB   sing N N 326 
TRP   CA  HA   sing N N 327 
TRP   C   O    doub N N 328 
TRP   C   OXT  sing N N 329 
TRP   CB  CG   sing N N 330 
TRP   CB  HB2  sing N N 331 
TRP   CB  HB3  sing N N 332 
TRP   CG  CD1  doub Y N 333 
TRP   CG  CD2  sing Y N 334 
TRP   CD1 NE1  sing Y N 335 
TRP   CD1 HD1  sing N N 336 
TRP   CD2 CE2  doub Y N 337 
TRP   CD2 CE3  sing Y N 338 
TRP   NE1 CE2  sing Y N 339 
TRP   NE1 HE1  sing N N 340 
TRP   CE2 CZ2  sing Y N 341 
TRP   CE3 CZ3  doub Y N 342 
TRP   CE3 HE3  sing N N 343 
TRP   CZ2 CH2  doub Y N 344 
TRP   CZ2 HZ2  sing N N 345 
TRP   CZ3 CH2  sing Y N 346 
TRP   CZ3 HZ3  sing N N 347 
TRP   CH2 HH2  sing N N 348 
TRP   OXT HXT  sing N N 349 
TYR   N   CA   sing N N 350 
TYR   N   H    sing N N 351 
TYR   N   H2   sing N N 352 
TYR   CA  C    sing N N 353 
TYR   CA  CB   sing N N 354 
TYR   CA  HA   sing N N 355 
TYR   C   O    doub N N 356 
TYR   C   OXT  sing N N 357 
TYR   CB  CG   sing N N 358 
TYR   CB  HB2  sing N N 359 
TYR   CB  HB3  sing N N 360 
TYR   CG  CD1  doub Y N 361 
TYR   CG  CD2  sing Y N 362 
TYR   CD1 CE1  sing Y N 363 
TYR   CD1 HD1  sing N N 364 
TYR   CD2 CE2  doub Y N 365 
TYR   CD2 HD2  sing N N 366 
TYR   CE1 CZ   doub Y N 367 
TYR   CE1 HE1  sing N N 368 
TYR   CE2 CZ   sing Y N 369 
TYR   CE2 HE2  sing N N 370 
TYR   CZ  OH   sing N N 371 
TYR   OH  HH   sing N N 372 
TYR   OXT HXT  sing N N 373 
VAL   N   CA   sing N N 374 
VAL   N   H    sing N N 375 
VAL   N   H2   sing N N 376 
VAL   CA  C    sing N N 377 
VAL   CA  CB   sing N N 378 
VAL   CA  HA   sing N N 379 
VAL   C   O    doub N N 380 
VAL   C   OXT  sing N N 381 
VAL   CB  CG1  sing N N 382 
VAL   CB  CG2  sing N N 383 
VAL   CB  HB   sing N N 384 
VAL   CG1 HG11 sing N N 385 
VAL   CG1 HG12 sing N N 386 
VAL   CG1 HG13 sing N N 387 
VAL   CG2 HG21 sing N N 388 
VAL   CG2 HG22 sing N N 389 
VAL   CG2 HG23 sing N N 390 
VAL   OXT HXT  sing N N 391 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5b5g 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Y26 
_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]   0.021277 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003442 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011659 
_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]   0.017340 
_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   . ALA   A 1 1   ? 7.264   -16.997 13.733  1.00 36.53 ? 15  ALA   A N   1 
ATOM   2    C CA  . ALA   A 1 1   ? 7.800   -15.832 14.427  1.00 35.94 ? 15  ALA   A CA  1 
ATOM   3    C C   . ALA   A 1 1   ? 8.504   -14.899 13.446  1.00 33.63 ? 15  ALA   A C   1 
ATOM   4    O O   . ALA   A 1 1   ? 9.300   -15.341 12.618  1.00 34.62 ? 15  ALA   A O   1 
ATOM   5    C CB  . ALA   A 1 1   ? 8.752   -16.261 15.530  1.00 37.07 ? 15  ALA   A CB  1 
ATOM   6    N N   . GLY   A 1 2   ? 8.201   -13.615 13.542  1.00 30.03 ? 16  GLY   A N   1 
ATOM   7    C CA  . GLY   A 1 2   ? 8.765   -12.625 12.651  1.00 24.07 ? 16  GLY   A CA  1 
ATOM   8    C C   . GLY   A 1 2   ? 7.756   -11.521 12.403  1.00 19.85 ? 16  GLY   A C   1 
ATOM   9    O O   . GLY   A 1 2   ? 6.725   -11.442 13.056  1.00 19.73 ? 16  GLY   A O   1 
ATOM   10   N N   . ILE   A 1 3   ? 8.073   -10.682 11.418  1.00 18.58 ? 17  ILE   A N   1 
ATOM   11   C CA  . ILE   A 1 3   ? 7.242   -9.521  11.119  1.00 17.77 ? 17  ILE   A CA  1 
ATOM   12   C C   . ILE   A 1 3   ? 5.937   -9.932  10.440  1.00 17.21 ? 17  ILE   A C   1 
ATOM   13   O O   . ILE   A 1 3   ? 4.872   -9.368  10.722  1.00 18.16 ? 17  ILE   A O   1 
ATOM   14   C CB  . ILE   A 1 3   ? 8.049   -8.513  10.281  1.00 17.48 ? 17  ILE   A CB  1 
ATOM   15   C CG1 . ILE   A 1 3   ? 9.192   -7.929  11.126  1.00 18.67 ? 17  ILE   A CG1 1 
ATOM   16   C CG2 . ILE   A 1 3   ? 7.138   -7.436  9.685   1.00 17.84 ? 17  ILE   A CG2 1 
ATOM   17   C CD1 . ILE   A 1 3   ? 10.182  -7.111  10.327  1.00 19.47 ? 17  ILE   A CD1 1 
ATOM   18   N N   . THR   A 1 4   ? 5.991   -10.904 9.529   1.00 17.87 ? 18  THR   A N   1 
ATOM   19   C CA  . THR   A 1 4   ? 4.789   -11.339 8.826   1.00 17.85 ? 18  THR   A CA  1 
ATOM   20   C C   . THR   A 1 4   ? 3.711   -11.787 9.808   1.00 17.68 ? 18  THR   A C   1 
ATOM   21   O O   . THR   A 1 4   ? 3.967   -12.613 10.689  1.00 18.98 ? 18  THR   A O   1 
ATOM   22   C CB  . THR   A 1 4   ? 5.147   -12.498 7.898   1.00 17.74 ? 18  THR   A CB  1 
ATOM   23   O OG1 . THR   A 1 4   ? 6.045   -12.035 6.881   1.00 17.97 ? 18  THR   A OG1 1 
ATOM   24   C CG2 . THR   A 1 4   ? 3.894   -13.076 7.263   1.00 17.62 ? 18  THR   A CG2 1 
ATOM   25   N N   . GLY   A 1 5   ? 2.501   -11.262 9.641   1.00 16.47 ? 19  GLY   A N   1 
ATOM   26   C CA  . GLY   A 1 5   ? 1.385   -11.633 10.492  1.00 16.02 ? 19  GLY   A CA  1 
ATOM   27   C C   . GLY   A 1 5   ? 0.345   -10.529 10.573  1.00 15.55 ? 19  GLY   A C   1 
ATOM   28   O O   . GLY   A 1 5   ? 0.389   -9.550  9.842   1.00 16.56 ? 19  GLY   A O   1 
ATOM   29   N N   . THR   A 1 6   ? -0.596  -10.716 11.498  1.00 16.37 ? 20  THR   A N   1 
ATOM   30   C CA  . THR   A 1 6   ? -1.640  -9.742  11.796  1.00 16.81 ? 20  THR   A CA  1 
ATOM   31   C C   . THR   A 1 6   ? -1.335  -9.096  13.140  1.00 16.54 ? 20  THR   A C   1 
ATOM   32   O O   . THR   A 1 6   ? -1.115  -9.796  14.137  1.00 18.61 ? 20  THR   A O   1 
ATOM   33   C CB  . THR   A 1 6   ? -3.021  -10.407 11.825  1.00 17.91 ? 20  THR   A CB  1 
ATOM   34   O OG1 . THR   A 1 6   ? -3.360  -10.859 10.507  1.00 18.61 ? 20  THR   A OG1 1 
ATOM   35   C CG2 . THR   A 1 6   ? -4.089  -9.435  12.308  1.00 19.31 ? 20  THR   A CG2 1 
ATOM   36   N N   . TRP   A 1 7   ? -1.312  -7.766  13.154  1.00 15.27 ? 21  TRP   A N   1 
ATOM   37   C CA  . TRP   A 1 7   ? -0.935  -6.981  14.316  1.00 15.14 ? 21  TRP   A CA  1 
ATOM   38   C C   . TRP   A 1 7   ? -2.058  -6.005  14.640  1.00 15.20 ? 21  TRP   A C   1 
ATOM   39   O O   . TRP   A 1 7   ? -2.838  -5.620  13.765  1.00 15.25 ? 21  TRP   A O   1 
ATOM   40   C CB  . TRP   A 1 7   ? 0.337   -6.170  14.021  1.00 14.98 ? 21  TRP   A CB  1 
ATOM   41   C CG  . TRP   A 1 7   ? 1.560   -6.987  13.713  1.00 15.34 ? 21  TRP   A CG  1 
ATOM   42   C CD1 . TRP   A 1 7   ? 1.893   -7.551  12.512  1.00 14.97 ? 21  TRP   A CD1 1 
ATOM   43   C CD2 . TRP   A 1 7   ? 2.634   -7.305  14.616  1.00 16.62 ? 21  TRP   A CD2 1 
ATOM   44   N NE1 . TRP   A 1 7   ? 3.100   -8.206  12.615  1.00 16.42 ? 21  TRP   A NE1 1 
ATOM   45   C CE2 . TRP   A 1 7   ? 3.574   -8.072  13.896  1.00 16.90 ? 21  TRP   A CE2 1 
ATOM   46   C CE3 . TRP   A 1 7   ? 2.889   -7.016  15.964  1.00 17.57 ? 21  TRP   A CE3 1 
ATOM   47   C CZ2 . TRP   A 1 7   ? 4.752   -8.546  14.478  1.00 18.72 ? 21  TRP   A CZ2 1 
ATOM   48   C CZ3 . TRP   A 1 7   ? 4.057   -7.502  16.542  1.00 18.60 ? 21  TRP   A CZ3 1 
ATOM   49   C CH2 . TRP   A 1 7   ? 4.969   -8.259  15.801  1.00 19.52 ? 21  TRP   A CH2 1 
ATOM   50   N N   . TYR   A 1 8   ? -2.118  -5.578  15.904  1.00 15.31 ? 22  TYR   A N   1 
ATOM   51   C CA  . TYR   A 1 8   ? -3.088  -4.586  16.345  1.00 15.89 ? 22  TYR   A CA  1 
ATOM   52   C C   . TYR   A 1 8   ? -2.366  -3.500  17.125  1.00 15.99 ? 22  TYR   A C   1 
ATOM   53   O O   . TYR   A 1 8   ? -1.463  -3.796  17.911  1.00 16.08 ? 22  TYR   A O   1 
ATOM   54   C CB  . TYR   A 1 8   ? -4.151  -5.218  17.265  1.00 19.03 ? 22  TYR   A CB  1 
ATOM   55   C CG  . TYR   A 1 8   ? -4.831  -6.413  16.645  1.00 20.65 ? 22  TYR   A CG  1 
ATOM   56   C CD1 . TYR   A 1 8   ? -5.950  -6.255  15.841  1.00 21.38 ? 22  TYR   A CD1 1 
ATOM   57   C CD2 . TYR   A 1 8   ? -4.342  -7.700  16.846  1.00 21.73 ? 22  TYR   A CD2 1 
ATOM   58   C CE1 . TYR   A 1 8   ? -6.569  -7.338  15.259  1.00 22.92 ? 22  TYR   A CE1 1 
ATOM   59   C CE2 . TYR   A 1 8   ? -4.954  -8.791  16.261  1.00 23.04 ? 22  TYR   A CE2 1 
ATOM   60   C CZ  . TYR   A 1 8   ? -6.066  -8.602  15.472  1.00 23.80 ? 22  TYR   A CZ  1 
ATOM   61   O OH  . TYR   A 1 8   ? -6.674  -9.687  14.889  1.00 26.27 ? 22  TYR   A OH  1 
ATOM   62   N N   . ASN   A 1 9   ? -2.760  -2.244  16.917  1.00 14.95 ? 23  ASN   A N   1 
ATOM   63   C CA  . ASN   A 1 9   ? -2.177  -1.182  17.724  1.00 15.16 ? 23  ASN   A CA  1 
ATOM   64   C C   . ASN   A 1 9   ? -2.989  -0.956  19.001  1.00 16.07 ? 23  ASN   A C   1 
ATOM   65   O O   . ASN   A 1 9   ? -3.982  -1.637  19.279  1.00 17.20 ? 23  ASN   A O   1 
ATOM   66   C CB  . ASN   A 1 9   ? -1.865  0.083   16.906  1.00 15.27 ? 23  ASN   A CB  1 
ATOM   67   C CG  . ASN   A 1 9   ? -3.078  0.983   16.669  1.00 13.63 ? 23  ASN   A CG  1 
ATOM   68   O OD1 . ASN   A 1 9   ? -4.194  0.693   17.095  1.00 14.18 ? 23  ASN   A OD1 1 
ATOM   69   N ND2 . ASN   A 1 9   ? -2.851  2.099   15.975  1.00 14.33 ? 23  ASN   A ND2 1 
ATOM   70   N N   . GLN   A 1 10  ? -2.543  0.016   19.798  1.00 15.78 ? 24  GLN   A N   1 
ATOM   71   C CA  . GLN   A 1 10  ? -3.139  0.267   21.104  1.00 17.00 ? 24  GLN   A CA  1 
ATOM   72   C C   . GLN   A 1 10  ? -4.570  0.782   21.008  1.00 17.03 ? 24  GLN   A C   1 
ATOM   73   O O   . GLN   A 1 10  ? -5.305  0.714   22.001  1.00 19.49 ? 24  GLN   A O   1 
ATOM   74   C CB  . GLN   A 1 10  ? -2.244  1.224   21.908  1.00 17.11 ? 24  GLN   A CB  1 
ATOM   75   C CG  . GLN   A 1 10  ? -2.227  2.696   21.439  1.00 16.50 ? 24  GLN   A CG  1 
ATOM   76   C CD  . GLN   A 1 10  ? -1.481  2.954   20.129  1.00 14.97 ? 24  GLN   A CD  1 
ATOM   77   O OE1 . GLN   A 1 10  ? -0.749  2.103   19.610  1.00 15.51 ? 24  GLN   A OE1 1 
ATOM   78   N NE2 . GLN   A 1 10  ? -1.666  4.151   19.595  1.00 14.81 ? 24  GLN   A NE2 1 
ATOM   79   N N   . LEU   A 1 11  ? -4.987  1.276   19.840  1.00 17.35 ? 25  LEU   A N   1 
ATOM   80   C CA  . LEU   A 1 11  ? -6.346  1.755   19.626  1.00 19.33 ? 25  LEU   A CA  1 
ATOM   81   C C   . LEU   A 1 11  ? -7.223  0.753   18.888  1.00 20.92 ? 25  LEU   A C   1 
ATOM   82   O O   . LEU   A 1 11  ? -8.395  1.044   18.636  1.00 23.03 ? 25  LEU   A O   1 
ATOM   83   C CB  . LEU   A 1 11  ? -6.330  3.088   18.873  1.00 20.86 ? 25  LEU   A CB  1 
ATOM   84   C CG  . LEU   A 1 11  ? -5.606  4.224   19.603  1.00 21.70 ? 25  LEU   A CG  1 
ATOM   85   C CD1 . LEU   A 1 11  ? -5.646  5.517   18.800  1.00 22.93 ? 25  LEU   A CD1 1 
ATOM   86   C CD2 . LEU   A 1 11  ? -6.186  4.434   21.002  1.00 22.07 ? 25  LEU   A CD2 1 
ATOM   87   N N   . GLY   A 1 12  ? -6.692  -0.412  18.540  1.00 20.73 ? 26  GLY   A N   1 
ATOM   88   C CA  . GLY   A 1 12  ? -7.471  -1.418  17.845  1.00 20.42 ? 26  GLY   A CA  1 
ATOM   89   C C   . GLY   A 1 12  ? -7.419  -1.371  16.333  1.00 19.39 ? 26  GLY   A C   1 
ATOM   90   O O   . GLY   A 1 12  ? -8.193  -2.087  15.687  1.00 21.07 ? 26  GLY   A O   1 
ATOM   91   N N   . SER   A 1 13  ? -6.539  -0.565  15.743  1.00 16.49 ? 27  SER   A N   1 
ATOM   92   C CA  . SER   A 1 13  ? -6.300  -0.648  14.306  1.00 15.33 ? 27  SER   A CA  1 
ATOM   93   C C   . SER   A 1 13  ? -5.655  -1.993  13.972  1.00 14.61 ? 27  SER   A C   1 
ATOM   94   O O   . SER   A 1 13  ? -4.956  -2.581  14.800  1.00 16.42 ? 27  SER   A O   1 
ATOM   95   C CB  . SER   A 1 13  ? -5.379  0.488   13.862  1.00 15.06 ? 27  SER   A CB  1 
ATOM   96   O OG  . SER   A 1 13  ? -5.999  1.746   14.066  1.00 16.00 ? 27  SER   A OG  1 
ATOM   97   N N   . THR   A 1 14  ? -5.892  -2.480  12.746  1.00 14.91 ? 28  THR   A N   1 
ATOM   98   C CA  . THR   A 1 14  ? -5.441  -3.803  12.308  1.00 15.06 ? 28  THR   A CA  1 
ATOM   99   C C   . THR   A 1 14  ? -4.441  -3.667  11.166  1.00 13.91 ? 28  THR   A C   1 
ATOM   100  O O   . THR   A 1 14  ? -4.765  -3.097  10.116  1.00 14.74 ? 28  THR   A O   1 
ATOM   101  C CB  . THR   A 1 14  ? -6.624  -4.667  11.855  1.00 16.95 ? 28  THR   A CB  1 
ATOM   102  O OG1 . THR   A 1 14  ? -7.600  -4.724  12.903  1.00 19.07 ? 28  THR   A OG1 1 
ATOM   103  C CG2 . THR   A 1 14  ? -6.167  -6.087  11.527  1.00 17.43 ? 28  THR   A CG2 1 
ATOM   104  N N   . PHE   A 1 15  ? -3.250  -4.237  11.354  1.00 13.30 ? 29  PHE   A N   1 
ATOM   105  C CA  . PHE   A 1 15  ? -2.111  -4.132  10.439  1.00 13.74 ? 29  PHE   A CA  1 
ATOM   106  C C   . PHE   A 1 15  ? -1.783  -5.550  9.977   1.00 13.44 ? 29  PHE   A C   1 
ATOM   107  O O   . PHE   A 1 15  ? -1.248  -6.350  10.752  1.00 14.31 ? 29  PHE   A O   1 
ATOM   108  C CB  . PHE   A 1 15  ? -0.960  -3.468  11.213  1.00 13.44 ? 29  PHE   A CB  1 
ATOM   109  C CG  . PHE   A 1 15  ? 0.394   -3.455  10.525  1.00 13.24 ? 29  PHE   A CG  1 
ATOM   110  C CD1 . PHE   A 1 15  ? 0.548   -3.147  9.174   1.00 13.94 ? 29  PHE   A CD1 1 
ATOM   111  C CD2 . PHE   A 1 15  ? 1.540   -3.674  11.293  1.00 14.67 ? 29  PHE   A CD2 1 
ATOM   112  C CE1 . PHE   A 1 15  ? 1.829   -3.096  8.609   1.00 13.92 ? 29  PHE   A CE1 1 
ATOM   113  C CE2 . PHE   A 1 15  ? 2.807   -3.626  10.736  1.00 14.64 ? 29  PHE   A CE2 1 
ATOM   114  C CZ  . PHE   A 1 15  ? 2.957   -3.337  9.391   1.00 13.52 ? 29  PHE   A CZ  1 
ATOM   115  N N   . ILE   A 1 16  ? -2.132  -5.877  8.730   1.00 14.08 ? 30  ILE   A N   1 
ATOM   116  C CA  . ILE   A 1 16  ? -1.917  -7.210  8.167   1.00 14.65 ? 30  ILE   A CA  1 
ATOM   117  C C   . ILE   A 1 16  ? -0.771  -7.097  7.171   1.00 14.46 ? 30  ILE   A C   1 
ATOM   118  O O   . ILE   A 1 16  ? -0.913  -6.465  6.119   1.00 17.14 ? 30  ILE   A O   1 
ATOM   119  C CB  . ILE   A 1 16  ? -3.188  -7.761  7.502   1.00 15.98 ? 30  ILE   A CB  1 
ATOM   120  C CG1 . ILE   A 1 16  ? -4.353  -7.786  8.503   1.00 16.45 ? 30  ILE   A CG1 1 
ATOM   121  C CG2 . ILE   A 1 16  ? -2.934  -9.160  6.934   1.00 18.25 ? 30  ILE   A CG2 1 
ATOM   122  C CD1 . ILE   A 1 16  ? -5.695  -8.154  7.872   1.00 17.78 ? 30  ILE   A CD1 1 
ATOM   123  N N   . VAL   A 1 17  ? 0.367   -7.705  7.488   1.00 13.59 ? 31  VAL   A N   1 
ATOM   124  C CA  . VAL   A 1 17  ? 1.596   -7.433  6.757   1.00 13.64 ? 31  VAL   A CA  1 
ATOM   125  C C   . VAL   A 1 17  ? 2.292   -8.733  6.376   1.00 14.21 ? 31  VAL   A C   1 
ATOM   126  O O   . VAL   A 1 17  ? 2.217   -9.742  7.083   1.00 14.56 ? 31  VAL   A O   1 
ATOM   127  C CB  . VAL   A 1 17  ? 2.531   -6.507  7.576   1.00 14.39 ? 31  VAL   A CB  1 
ATOM   128  C CG1 . VAL   A 1 17  ? 3.104   -7.242  8.798   1.00 15.52 ? 31  VAL   A CG1 1 
ATOM   129  C CG2 . VAL   A 1 17  ? 3.628   -5.928  6.705   1.00 14.50 ? 31  VAL   A CG2 1 
ATOM   130  N N   . THR   A 1 18  ? 2.982   -8.693  5.239   1.00 13.47 ? 32  THR   A N   1 
ATOM   131  C CA  . THR   A 1 18  ? 3.875   -9.754  4.797   1.00 14.38 ? 32  THR   A CA  1 
ATOM   132  C C   . THR   A 1 18  ? 5.251   -9.144  4.570   1.00 14.30 ? 32  THR   A C   1 
ATOM   133  O O   . THR   A 1 18  ? 5.369   -8.107  3.904   1.00 14.35 ? 32  THR   A O   1 
ATOM   134  C CB  . THR   A 1 18  ? 3.360   -10.396 3.509   1.00 16.37 ? 32  THR   A CB  1 
ATOM   135  O OG1 . THR   A 1 18  ? 2.079   -10.985 3.765   1.00 17.84 ? 32  THR   A OG1 1 
ATOM   136  C CG2 . THR   A 1 18  ? 4.330   -11.465 3.030   1.00 17.61 ? 32  THR   A CG2 1 
ATOM   137  N N   . ALA   A 1 19  ? 6.276   -9.761  5.159   1.00 15.78 ? 33  ALA   A N   1 
ATOM   138  C CA  . ALA   A 1 19  ? 7.660   -9.317  5.032   1.00 17.11 ? 33  ALA   A CA  1 
ATOM   139  C C   . ALA   A 1 19  ? 8.362   -10.253 4.051   1.00 18.58 ? 33  ALA   A C   1 
ATOM   140  O O   . ALA   A 1 19  ? 8.639   -11.411 4.379   1.00 20.98 ? 33  ALA   A O   1 
ATOM   141  C CB  . ALA   A 1 19  ? 8.351   -9.337  6.394   1.00 18.11 ? 33  ALA   A CB  1 
ATOM   142  N N   . GLY   A 1 20  ? 8.641   -9.756  2.847   1.00 17.90 ? 34  GLY   A N   1 
ATOM   143  C CA  . GLY   A 1 20  ? 9.207   -10.600 1.814   1.00 19.76 ? 34  GLY   A CA  1 
ATOM   144  C C   . GLY   A 1 20  ? 10.715  -10.729 1.927   1.00 21.23 ? 34  GLY   A C   1 
ATOM   145  O O   . GLY   A 1 20  ? 11.393  -9.924  2.565   1.00 22.34 ? 34  GLY   A O   1 
ATOM   146  N N   . ALA   A 1 21  ? 11.252  -11.766 1.278   1.00 22.87 ? 35  ALA   A N   1 
ATOM   147  C CA  . ALA   A 1 21  ? 12.682  -12.039 1.379   1.00 24.54 ? 35  ALA   A CA  1 
ATOM   148  C C   . ALA   A 1 21  ? 13.536  -10.903 0.827   1.00 25.53 ? 35  ALA   A C   1 
ATOM   149  O O   . ALA   A 1 21  ? 14.700  -10.767 1.225   1.00 26.73 ? 35  ALA   A O   1 
ATOM   150  C CB  . ALA   A 1 21  ? 13.025  -13.358 0.684   1.00 25.42 ? 35  ALA   A CB  1 
ATOM   151  N N   . ASP   A 1 22  ? 12.983  -10.078 -0.061  1.00 24.67 ? 36  ASP   A N   1 
ATOM   152  C CA  . ASP   A 1 22  ? 13.700  -8.974  -0.688  1.00 23.57 ? 36  ASP   A CA  1 
ATOM   153  C C   . ASP   A 1 22  ? 13.643  -7.672  0.113   1.00 20.54 ? 36  ASP   A C   1 
ATOM   154  O O   . ASP   A 1 22  ? 14.099  -6.641  -0.390  1.00 21.27 ? 36  ASP   A O   1 
ATOM   155  C CB  . ASP   A 1 22  ? 13.152  -8.724  -2.097  1.00 23.96 ? 36  ASP   A CB  1 
ATOM   156  C CG  . ASP   A 1 22  ? 11.694  -8.299  -2.088  1.00 24.42 ? 36  ASP   A CG  1 
ATOM   157  O OD1 . ASP   A 1 22  ? 11.018  -8.516  -1.059  1.00 22.34 ? 36  ASP   A OD1 1 
ATOM   158  O OD2 . ASP   A 1 22  ? 11.223  -7.749  -3.108  1.00 26.66 ? 36  ASP   A OD2 1 
ATOM   159  N N   . GLY   A 1 23  ? 13.089  -7.686  1.329   1.00 17.73 ? 37  GLY   A N   1 
ATOM   160  C CA  . GLY   A 1 23  ? 12.960  -6.476  2.121   1.00 15.61 ? 37  GLY   A CA  1 
ATOM   161  C C   . GLY   A 1 23  ? 11.641  -5.743  1.970   1.00 14.70 ? 37  GLY   A C   1 
ATOM   162  O O   . GLY   A 1 23  ? 11.473  -4.668  2.564   1.00 14.19 ? 37  GLY   A O   1 
ATOM   163  N N   . ALA   A 1 24  ? 10.696  -6.291  1.215   1.00 14.80 ? 38  ALA   A N   1 
ATOM   164  C CA  . ALA   A 1 24  ? 9.432   -5.613  0.961   1.00 13.94 ? 38  ALA   A CA  1 
ATOM   165  C C   . ALA   A 1 24  ? 8.433   -5.864  2.087   1.00 13.75 ? 38  ALA   A C   1 
ATOM   166  O O   . ALA   A 1 24  ? 8.312   -6.986  2.585   1.00 15.51 ? 38  ALA   A O   1 
ATOM   167  C CB  . ALA   A 1 24  ? 8.841   -6.119  -0.357  1.00 16.83 ? 38  ALA   A CB  1 
ATOM   168  N N   . LEU   A 1 25  ? 7.696   -4.818  2.464   1.00 12.93 ? 39  LEU   A N   1 
ATOM   169  C CA  . LEU   A 1 25  ? 6.480   -4.954  3.261   1.00 12.31 ? 39  LEU   A CA  1 
ATOM   170  C C   . LEU   A 1 25  ? 5.274   -4.672  2.372   1.00 11.82 ? 39  LEU   A C   1 
ATOM   171  O O   . LEU   A 1 25  ? 5.260   -3.676  1.640   1.00 12.00 ? 39  LEU   A O   1 
ATOM   172  C CB  . LEU   A 1 25  ? 6.455   -3.966  4.427   1.00 12.51 ? 39  LEU   A CB  1 
ATOM   173  C CG  . LEU   A 1 25  ? 7.548   -4.075  5.484   1.00 12.46 ? 39  LEU   A CG  1 
ATOM   174  C CD1 . LEU   A 1 25  ? 7.361   -2.991  6.553   1.00 12.65 ? 39  LEU   A CD1 1 
ATOM   175  C CD2 . LEU   A 1 25  ? 7.544   -5.469  6.115   1.00 14.05 ? 39  LEU   A CD2 1 
ATOM   176  N N   . THR   A 1 26  ? 4.268   -5.547  2.441   1.00 11.97 ? 40  THR   A N   1 
ATOM   177  C CA  . THR   A 1 26  ? 3.019   -5.381  1.707   1.00 12.05 ? 40  THR   A CA  1 
ATOM   178  C C   . THR   A 1 26  ? 1.873   -5.798  2.622   1.00 12.72 ? 40  THR   A C   1 
ATOM   179  O O   . THR   A 1 26  ? 2.062   -6.577  3.560   1.00 14.95 ? 40  THR   A O   1 
ATOM   180  C CB  . THR   A 1 26  ? 2.991   -6.254  0.431   1.00 14.11 ? 40  THR   A CB  1 
ATOM   181  O OG1 . THR   A 1 26  ? 3.108   -7.633  0.793   1.00 15.55 ? 40  THR   A OG1 1 
ATOM   182  C CG2 . THR   A 1 26  ? 4.133   -5.902  -0.520  1.00 15.38 ? 40  THR   A CG2 1 
ATOM   183  N N   . GLY   A 1 27  ? 0.681   -5.291  2.347   1.00 12.77 ? 41  GLY   A N   1 
ATOM   184  C CA  . GLY   A 1 27  ? -0.478  -5.740  3.103   1.00 13.59 ? 41  GLY   A CA  1 
ATOM   185  C C   . GLY   A 1 27  ? -1.558  -4.670  3.164   1.00 11.96 ? 41  GLY   A C   1 
ATOM   186  O O   . GLY   A 1 27  ? -1.697  -3.862  2.248   1.00 11.90 ? 41  GLY   A O   1 
ATOM   187  N N   . THR   A 1 28  ? -2.350  -4.724  4.244   1.00 12.42 ? 42  THR   A N   1 
ATOM   188  C CA  . THR   A 1 28  ? -3.487  -3.829  4.421   1.00 13.57 ? 42  THR   A CA  1 
ATOM   189  C C   . THR   A 1 28  ? -3.510  -3.246  5.829   1.00 12.70 ? 42  THR   A C   1 
ATOM   190  O O   . THR   A 1 28  ? -3.021  -3.852  6.789   1.00 13.93 ? 42  THR   A O   1 
ATOM   191  C CB  . THR   A 1 28  ? -4.838  -4.533  4.152   1.00 14.77 ? 42  THR   A CB  1 
ATOM   192  O OG1 . THR   A 1 28  ? -5.026  -5.616  5.076   1.00 15.75 ? 42  THR   A OG1 1 
ATOM   193  C CG2 . THR   A 1 28  ? -4.907  -5.053  2.714   1.00 15.87 ? 42  THR   A CG2 1 
ATOM   194  N N   . TYR   A 1 29  ? -4.110  -2.064  5.942   1.00 12.58 ? 43  TYR   A N   1 
ATOM   195  C CA  . TYR   A 1 29  ? -4.272  -1.383  7.216   1.00 12.47 ? 43  TYR   A CA  1 
ATOM   196  C C   . TYR   A 1 29  ? -5.722  -0.943  7.364   1.00 12.37 ? 43  TYR   A C   1 
ATOM   197  O O   . TYR   A 1 29  ? -6.322  -0.414  6.419   1.00 13.40 ? 43  TYR   A O   1 
ATOM   198  C CB  . TYR   A 1 29  ? -3.366  -0.152  7.293   1.00 11.87 ? 43  TYR   A CB  1 
ATOM   199  C CG  . TYR   A 1 29  ? -3.092  0.320   8.708   1.00 11.14 ? 43  TYR   A CG  1 
ATOM   200  C CD1 . TYR   A 1 29  ? -3.965  1.185   9.366   1.00 11.71 ? 43  TYR   A CD1 1 
ATOM   201  C CD2 . TYR   A 1 29  ? -1.959  -0.106  9.393   1.00 11.77 ? 43  TYR   A CD2 1 
ATOM   202  C CE1 . TYR   A 1 29  ? -3.709  1.607   10.674  1.00 11.92 ? 43  TYR   A CE1 1 
ATOM   203  C CE2 . TYR   A 1 29  ? -1.695  0.311   10.698  1.00 12.10 ? 43  TYR   A CE2 1 
ATOM   204  C CZ  . TYR   A 1 29  ? -2.572  1.166   11.328  1.00 11.64 ? 43  TYR   A CZ  1 
ATOM   205  O OH  . TYR   A 1 29  ? -2.305  1.570   12.621  1.00 13.01 ? 43  TYR   A OH  1 
ATOM   206  N N   . GLU   A 1 30  ? -6.282  -1.164  8.552   1.00 12.53 ? 44  GLU   A N   1 
ATOM   207  C CA  . GLU   A 1 30  ? -7.631  -0.717  8.882   1.00 13.84 ? 44  GLU   A CA  1 
ATOM   208  C C   . GLU   A 1 30  ? -7.521  0.158   10.121  1.00 14.24 ? 44  GLU   A C   1 
ATOM   209  O O   . GLU   A 1 30  ? -7.032  -0.300  11.159  1.00 15.07 ? 44  GLU   A O   1 
ATOM   210  C CB  . GLU   A 1 30  ? -8.554  -1.914  9.129   1.00 16.25 ? 44  GLU   A CB  1 
ATOM   211  C CG  . GLU   A 1 30  ? -9.996  -1.530  9.401   1.00 20.19 ? 44  GLU   A CG  1 
ATOM   212  C CD  . GLU   A 1 30  ? -10.950 -2.723  9.383   1.00 23.47 ? 44  GLU   A CD  1 
ATOM   213  O OE1 . GLU   A 1 30  ? -10.500 -3.872  9.159   1.00 25.22 ? 44  GLU   A OE1 1 
ATOM   214  O OE2 . GLU   A 1 30  ? -12.164 -2.503  9.587   1.00 25.09 ? 44  GLU   A OE2 1 
ATOM   215  N N   . SER   A 1 31  ? -7.933  1.423   10.001  1.00 14.91 ? 45  SER   A N   1 
ATOM   216  C CA  . SER   A 1 31  ? -7.734  2.416   11.054  1.00 16.14 ? 45  SER   A CA  1 
ATOM   217  C C   . SER   A 1 31  ? -8.949  2.492   11.967  1.00 18.14 ? 45  SER   A C   1 
ATOM   218  O O   . SER   A 1 31  ? -10.084 2.599   11.495  1.00 20.79 ? 45  SER   A O   1 
ATOM   219  C CB  . SER   A 1 31  ? -7.479  3.799   10.448  1.00 16.10 ? 45  SER   A CB  1 
ATOM   220  O OG  . SER   A 1 31  ? -7.302  4.778   11.461  1.00 16.65 ? 45  SER   A OG  1 
ATOM   221  N N   . ALA   A 1 32  ? -8.700  2.485   13.274  1.00 19.03 ? 46  ALA   A N   1 
ATOM   222  C CA  . ALA   A 1 32  ? -9.762  2.695   14.246  1.00 21.71 ? 46  ALA   A CA  1 
ATOM   223  C C   . ALA   A 1 32  ? -10.117 4.167   14.435  1.00 21.22 ? 46  ALA   A C   1 
ATOM   224  O O   . ALA   A 1 32  ? -11.107 4.464   15.116  1.00 23.77 ? 46  ALA   A O   1 
ATOM   225  C CB  . ALA   A 1 32  ? -9.370  2.076   15.588  1.00 23.95 ? 46  ALA   A CB  1 
ATOM   226  N N   . VAL   A 1 33  ? -9.351  5.093   13.846  1.00 19.39 ? 47  VAL   A N   1 
ATOM   227  C CA  . VAL   A 1 33  ? -9.556  6.526   14.035  1.00 19.59 ? 47  VAL   A CA  1 
ATOM   228  C C   . VAL   A 1 33  ? -9.607  7.249   12.693  1.00 18.28 ? 47  VAL   A C   1 
ATOM   229  O O   . VAL   A 1 33  ? -9.081  6.782   11.681  1.00 17.90 ? 47  VAL   A O   1 
ATOM   230  C CB  . VAL   A 1 33  ? -8.475  7.171   14.935  1.00 21.23 ? 47  VAL   A CB  1 
ATOM   231  C CG1 . VAL   A 1 33  ? -8.495  6.559   16.324  1.00 22.24 ? 47  VAL   A CG1 1 
ATOM   232  C CG2 . VAL   A 1 33  ? -7.095  7.049   14.293  1.00 22.56 ? 47  VAL   A CG2 1 
ATOM   233  N N   . GLY   A 1 34  ? -10.252 8.424   12.704  1.00 17.54 ? 48  GLY   A N   1 
ATOM   234  C CA  . GLY   A 1 34  ? -10.216 9.322   11.565  1.00 18.14 ? 48  GLY   A CA  1 
ATOM   235  C C   . GLY   A 1 34  ? -11.229 9.007   10.477  1.00 17.78 ? 48  GLY   A C   1 
ATOM   236  O O   . GLY   A 1 34  ? -12.107 8.151   10.604  1.00 18.87 ? 48  GLY   A O   1 
ATOM   237  N N   . ASN   A 1 35  ? -11.069 9.727   9.364   1.00 19.19 ? 49  ASN   A N   1 
ATOM   238  C CA  . ASN   A 1 35  ? -11.940 9.603   8.195   1.00 20.02 ? 49  ASN   A CA  1 
ATOM   239  C C   . ASN   A 1 35  ? -11.473 8.396   7.387   1.00 19.93 ? 49  ASN   A C   1 
ATOM   240  O O   . ASN   A 1 35  ? -10.757 8.506   6.385   1.00 20.46 ? 49  ASN   A O   1 
ATOM   241  C CB  . ASN   A 1 35  ? -11.899 10.890  7.378   1.00 23.03 ? 49  ASN   A CB  1 
ATOM   242  C CG  . ASN   A 1 35  ? -12.785 10.838  6.150   1.00 25.44 ? 49  ASN   A CG  1 
ATOM   243  O OD1 . ASN   A 1 35  ? -13.689 10.008  6.053   1.00 27.38 ? 49  ASN   A OD1 1 
ATOM   244  N ND2 . ASN   A 1 35  ? -12.526 11.730  5.199   1.00 26.67 ? 49  ASN   A ND2 1 
ATOM   245  N N   . ALA   A 1 36  ? -11.896 7.216   7.841   1.00 20.25 ? 50  ALA   A N   1 
ATOM   246  C CA  . ALA   A 1 36  ? -11.393 5.958   7.314   1.00 18.59 ? 50  ALA   A CA  1 
ATOM   247  C C   . ALA   A 1 36  ? -12.441 4.874   7.504   1.00 17.53 ? 50  ALA   A C   1 
ATOM   248  O O   . ALA   A 1 36  ? -13.187 4.868   8.487   1.00 18.80 ? 50  ALA   A O   1 
ATOM   249  C CB  . ALA   A 1 36  ? -10.089 5.542   8.008   1.00 19.10 ? 50  ALA   A CB  1 
ATOM   250  N N   . GLU   A 1 37  ? -12.487 3.953   6.546   1.00 16.58 ? 51  GLU   A N   1 
ATOM   251  C CA  . GLU   A 1 37  ? -13.408 2.831   6.579   1.00 16.80 ? 51  GLU   A CA  1 
ATOM   252  C C   . GLU   A 1 37  ? -12.775 1.676   5.816   1.00 16.52 ? 51  GLU   A C   1 
ATOM   253  O O   . GLU   A 1 37  ? -12.179 1.882   4.757   1.00 16.06 ? 51  GLU   A O   1 
ATOM   254  C CB  . GLU   A 1 37  ? -14.746 3.246   5.955   1.00 19.27 ? 51  GLU   A CB  1 
ATOM   255  C CG  . GLU   A 1 37  ? -15.597 2.122   5.443   1.00 22.03 ? 51  GLU   A CG  1 
ATOM   256  C CD  . GLU   A 1 37  ? -16.926 2.602   4.873   1.00 22.30 ? 51  GLU   A CD  1 
ATOM   257  O OE1 . GLU   A 1 37  ? -17.120 3.830   4.693   1.00 21.89 ? 51  GLU   A OE1 1 
ATOM   258  O OE2 . GLU   A 1 37  ? -17.780 1.739   4.610   1.00 23.20 ? 51  GLU   A OE2 1 
ATOM   259  N N   . SER   A 1 38  ? -12.878 0.470   6.375   1.00 17.07 ? 52  SER   A N   1 
ATOM   260  C CA  . SER   A 1 38  ? -12.377 -0.742  5.729   1.00 18.41 ? 52  SER   A CA  1 
ATOM   261  C C   . SER   A 1 38  ? -10.859 -0.720  5.540   1.00 16.53 ? 52  SER   A C   1 
ATOM   262  O O   . SER   A 1 38  ? -10.155 0.021   6.236   1.00 16.85 ? 52  SER   A O   1 
ATOM   263  C CB  . SER   A 1 38  ? -13.119 -0.979  4.408   1.00 21.93 ? 52  SER   A CB  1 
ATOM   264  O OG  . SER   A 1 38  ? -12.904 -2.283  3.906   1.00 24.73 ? 52  SER   A OG  1 
ATOM   265  N N   . ARG   A 1 39  ? -10.348 -1.537  4.619   1.00 16.43 ? 53  ARG   A N   1 
ATOM   266  C CA  . ARG   A 1 39  ? -8.911  -1.727  4.451   1.00 15.30 ? 53  ARG   A CA  1 
ATOM   267  C C   . ARG   A 1 39  ? -8.322  -0.769  3.420   1.00 13.10 ? 53  ARG   A C   1 
ATOM   268  O O   . ARG   A 1 39  ? -8.963  -0.430  2.422   1.00 14.17 ? 53  ARG   A O   1 
ATOM   269  C CB  . ARG   A 1 39  ? -8.613  -3.168  4.021   1.00 16.63 ? 53  ARG   A CB  1 
ATOM   270  C CG  . ARG   A 1 39  ? -8.769  -4.182  5.150   1.00 18.84 ? 53  ARG   A CG  1 
ATOM   271  C CD  . ARG   A 1 39  ? -8.633  -5.616  4.665   1.00 21.32 ? 53  ARG   A CD  1 
ATOM   272  N NE  . ARG   A 1 39  ? -8.813  -6.574  5.751   1.00 24.72 ? 53  ARG   A NE  1 
ATOM   273  C CZ  . ARG   A 1 39  ? -8.930  -7.884  5.581   1.00 26.70 ? 53  ARG   A CZ  1 
ATOM   274  N NH1 . ARG   A 1 39  ? -8.886  -8.431  4.378   1.00 28.61 ? 53  ARG   A NH1 1 
ATOM   275  N NH2 . ARG   A 1 39  ? -9.102  -8.666  6.645   1.00 27.70 ? 53  ARG   A NH2 1 
ATOM   276  N N   . TYR   A 1 40  ? -7.081  -0.351  3.676   1.00 12.48 ? 54  TYR   A N   1 
ATOM   277  C CA  . TYR   A 1 40  ? -6.286  0.465   2.769   1.00 11.82 ? 54  TYR   A CA  1 
ATOM   278  C C   . TYR   A 1 40  ? -4.985  -0.263  2.455   1.00 11.24 ? 54  TYR   A C   1 
ATOM   279  O O   . TYR   A 1 40  ? -4.443  -0.985  3.295   1.00 12.68 ? 54  TYR   A O   1 
ATOM   280  C CB  . TYR   A 1 40  ? -5.942  1.828   3.414   1.00 12.15 ? 54  TYR   A CB  1 
ATOM   281  C CG  . TYR   A 1 40  ? -7.163  2.669   3.689   1.00 11.54 ? 54  TYR   A CG  1 
ATOM   282  C CD1 . TYR   A 1 40  ? -7.962  2.428   4.806   1.00 11.91 ? 54  TYR   A CD1 1 
ATOM   283  C CD2 . TYR   A 1 40  ? -7.521  3.707   2.840   1.00 12.03 ? 54  TYR   A CD2 1 
ATOM   284  C CE1 . TYR   A 1 40  ? -9.091  3.179   5.045   1.00 12.38 ? 54  TYR   A CE1 1 
ATOM   285  C CE2 . TYR   A 1 40  ? -8.650  4.476   3.082   1.00 12.04 ? 54  TYR   A CE2 1 
ATOM   286  C CZ  . TYR   A 1 40  ? -9.436  4.204   4.185   1.00 13.14 ? 54  TYR   A CZ  1 
ATOM   287  O OH  . TYR   A 1 40  ? -10.574 4.936   4.444   1.00 14.40 ? 54  TYR   A OH  1 
ATOM   288  N N   . VAL   A 1 41  ? -4.477  -0.054  1.236   1.00 11.07 ? 55  VAL   A N   1 
ATOM   289  C CA  . VAL   A 1 41  ? -3.202  -0.635  0.825   1.00 11.34 ? 55  VAL   A CA  1 
ATOM   290  C C   . VAL   A 1 41  ? -2.055  -0.005  1.606   1.00 10.99 ? 55  VAL   A C   1 
ATOM   291  O O   . VAL   A 1 41  ? -2.014  1.217   1.814   1.00 11.07 ? 55  VAL   A O   1 
ATOM   292  C CB  . VAL   A 1 41  ? -2.995  -0.411  -0.684  1.00 12.65 ? 55  VAL   A CB  1 
ATOM   293  C CG1 . VAL   A 1 41  ? -1.590  -0.850  -1.115  1.00 13.06 ? 55  VAL   A CG1 1 
ATOM   294  C CG2 . VAL   A 1 41  ? -4.066  -1.135  -1.514  1.00 13.81 ? 55  VAL   A CG2 1 
ATOM   295  N N   . LEU   A 1 42  ? -1.082  -0.827  2.004   1.00 10.95 ? 56  LEU   A N   1 
ATOM   296  C CA  . LEU   A 1 42  ? 0.182   -0.313  2.518   1.00 11.43 ? 56  LEU   A CA  1 
ATOM   297  C C   . LEU   A 1 42  ? 1.353   -0.940  1.768   1.00 10.93 ? 56  LEU   A C   1 
ATOM   298  O O   . LEU   A 1 42  ? 1.274   -2.083  1.306   1.00 11.60 ? 56  LEU   A O   1 
ATOM   299  C CB  . LEU   A 1 42  ? 0.351   -0.598  4.018   1.00 12.23 ? 56  LEU   A CB  1 
ATOM   300  C CG  . LEU   A 1 42  ? 0.607   -2.042  4.461   1.00 12.25 ? 56  LEU   A CG  1 
ATOM   301  C CD1 . LEU   A 1 42  ? 2.101   -2.373  4.589   1.00 12.31 ? 56  LEU   A CD1 1 
ATOM   302  C CD2 . LEU   A 1 42  ? -0.135  -2.320  5.765   1.00 14.52 ? 56  LEU   A CD2 1 
ATOM   303  N N   . THR   A 1 43  ? 2.445   -0.185  1.666   1.00 11.08 ? 57  THR   A N   1 
ATOM   304  C CA  A THR   A 1 43  ? 3.719   -0.739  1.237   0.21 10.64 ? 57  THR   A CA  1 
ATOM   305  C CA  B THR   A 1 43  ? 3.727   -0.715  1.207   0.79 10.81 ? 57  THR   A CA  1 
ATOM   306  C C   . THR   A 1 43  ? 4.844   -0.089  2.035   1.00 10.15 ? 57  THR   A C   1 
ATOM   307  O O   . THR   A 1 43  ? 4.718   1.041   2.516   1.00 10.18 ? 57  THR   A O   1 
ATOM   308  C CB  A THR   A 1 43  ? 3.935   -0.567  -0.274  0.21 10.91 ? 57  THR   A CB  1 
ATOM   309  C CB  B THR   A 1 43  ? 4.014   -0.491  -0.304  0.79 11.96 ? 57  THR   A CB  1 
ATOM   310  O OG1 A THR   A 1 43  ? 5.188   -1.148  -0.649  0.21 11.73 ? 57  THR   A OG1 1 
ATOM   311  O OG1 B THR   A 1 43  ? 3.984   0.909   -0.615  0.79 13.21 ? 57  THR   A OG1 1 
ATOM   312  C CG2 A THR   A 1 43  ? 3.935   0.892   -0.634  0.21 11.19 ? 57  THR   A CG2 1 
ATOM   313  C CG2 B THR   A 1 43  ? 3.037   -1.272  -1.180  0.79 14.14 ? 57  THR   A CG2 1 
ATOM   314  N N   . GLY   A 1 44  ? 5.938   -0.822  2.185   1.00 11.01 ? 58  GLY   A N   1 
ATOM   315  C CA  . GLY   A 1 44  ? 7.083   -0.309  2.908   1.00 10.85 ? 58  GLY   A CA  1 
ATOM   316  C C   . GLY   A 1 44  ? 8.281   -1.211  2.742   1.00 10.73 ? 58  GLY   A C   1 
ATOM   317  O O   . GLY   A 1 44  ? 8.322   -2.043  1.835   1.00 11.62 ? 58  GLY   A O   1 
ATOM   318  N N   . ARG   A 1 45  ? 9.245   -1.044  3.651   1.00 10.53 ? 59  ARG   A N   1 
ATOM   319  C CA  . ARG   A 1 45  ? 10.530  -1.728  3.589   1.00 11.47 ? 59  ARG   A CA  1 
ATOM   320  C C   . ARG   A 1 45  ? 10.971  -2.102  5.000   1.00 11.06 ? 59  ARG   A C   1 
ATOM   321  O O   . ARG   A 1 45  ? 10.629  -1.423  5.976   1.00 12.01 ? 59  ARG   A O   1 
ATOM   322  C CB  . ARG   A 1 45  ? 11.616  -0.819  2.987   1.00 12.47 ? 59  ARG   A CB  1 
ATOM   323  C CG  . ARG   A 1 45  ? 11.347  -0.316  1.560   1.00 13.95 ? 59  ARG   A CG  1 
ATOM   324  C CD  . ARG   A 1 45  ? 11.432  -1.439  0.524   1.00 15.20 ? 59  ARG   A CD  1 
ATOM   325  N NE  . ARG   A 1 45  ? 12.780  -1.993  0.438   1.00 14.26 ? 59  ARG   A NE  1 
ATOM   326  C CZ  . ARG   A 1 45  ? 13.086  -3.142  -0.152  1.00 15.34 ? 59  ARG   A CZ  1 
ATOM   327  N NH1 . ARG   A 1 45  ? 12.166  -3.877  -0.761  1.00 15.48 ? 59  ARG   A NH1 1 
ATOM   328  N NH2 . ARG   A 1 45  ? 14.345  -3.574  -0.119  1.00 16.10 ? 59  ARG   A NH2 1 
ATOM   329  N N   . TYR   A 1 46  ? 11.772  -3.165  5.103   1.00 12.47 ? 60  TYR   A N   1 
ATOM   330  C CA  . TYR   A 1 46  ? 12.347  -3.553  6.390   1.00 12.56 ? 60  TYR   A CA  1 
ATOM   331  C C   . TYR   A 1 46  ? 13.743  -4.121  6.163   1.00 12.59 ? 60  TYR   A C   1 
ATOM   332  O O   . TYR   A 1 46  ? 14.088  -4.546  5.054   1.00 13.87 ? 60  TYR   A O   1 
ATOM   333  C CB  . TYR   A 1 46  ? 11.461  -4.570  7.132   1.00 14.01 ? 60  TYR   A CB  1 
ATOM   334  C CG  . TYR   A 1 46  ? 11.579  -5.986  6.595   1.00 13.78 ? 60  TYR   A CG  1 
ATOM   335  C CD1 . TYR   A 1 46  ? 10.994  -6.346  5.383   1.00 14.24 ? 60  TYR   A CD1 1 
ATOM   336  C CD2 . TYR   A 1 46  ? 12.287  -6.966  7.297   1.00 15.77 ? 60  TYR   A CD2 1 
ATOM   337  C CE1 . TYR   A 1 46  ? 11.118  -7.649  4.879   1.00 16.40 ? 60  TYR   A CE1 1 
ATOM   338  C CE2 . TYR   A 1 46  ? 12.407  -8.257  6.813   1.00 16.88 ? 60  TYR   A CE2 1 
ATOM   339  C CZ  . TYR   A 1 46  ? 11.826  -8.594  5.605   1.00 16.82 ? 60  TYR   A CZ  1 
ATOM   340  O OH  . TYR   A 1 46  ? 11.957  -9.885  5.127   1.00 19.31 ? 60  TYR   A OH  1 
ATOM   341  N N   . ASP   A 1 47  ? 14.545  -4.133  7.230   1.00 13.73 ? 61  ASP   A N   1 
ATOM   342  C CA  . ASP   A 1 47  ? 15.898  -4.684  7.186   1.00 14.38 ? 61  ASP   A CA  1 
ATOM   343  C C   . ASP   A 1 47  ? 15.814  -6.211  7.200   1.00 15.55 ? 61  ASP   A C   1 
ATOM   344  O O   . ASP   A 1 47  ? 15.473  -6.819  8.222   1.00 16.04 ? 61  ASP   A O   1 
ATOM   345  C CB  . ASP   A 1 47  ? 16.692  -4.149  8.377   1.00 14.60 ? 61  ASP   A CB  1 
ATOM   346  C CG  . ASP   A 1 47  ? 18.112  -4.700  8.460   1.00 15.29 ? 61  ASP   A CG  1 
ATOM   347  O OD1 . ASP   A 1 47  ? 18.536  -5.456  7.556   1.00 15.89 ? 61  ASP   A OD1 1 
ATOM   348  O OD2 . ASP   A 1 47  ? 18.811  -4.374  9.453   1.00 16.45 ? 61  ASP   A OD2 1 
ATOM   349  N N   . SER   A 1 48  ? 16.138  -6.839  6.071   1.00 16.86 ? 62  SER   A N   1 
ATOM   350  C CA  . SER   A 1 48  ? 16.027  -8.291  5.949   1.00 18.29 ? 62  SER   A CA  1 
ATOM   351  C C   . SER   A 1 48  ? 17.208  -9.042  6.544   1.00 19.25 ? 62  SER   A C   1 
ATOM   352  O O   . SER   A 1 48  ? 17.185  -10.276 6.549   1.00 20.07 ? 62  SER   A O   1 
ATOM   353  C CB  . SER   A 1 48  ? 15.837  -8.698  4.487   1.00 20.13 ? 62  SER   A CB  1 
ATOM   354  O OG  . SER   A 1 48  ? 16.894  -8.190  3.697   1.00 22.49 ? 62  SER   A OG  1 
ATOM   355  N N   . ALA   A 1 49  ? 18.225  -8.344  7.048   1.00 18.57 ? 63  ALA   A N   1 
ATOM   356  C CA  . ALA   A 1 49  ? 19.386  -8.978  7.674   1.00 19.25 ? 63  ALA   A CA  1 
ATOM   357  C C   . ALA   A 1 49  ? 19.793  -8.171  8.901   1.00 19.55 ? 63  ALA   A C   1 
ATOM   358  O O   . ALA   A 1 49  ? 20.852  -7.538  8.929   1.00 19.74 ? 63  ALA   A O   1 
ATOM   359  C CB  . ALA   A 1 49  ? 20.539  -9.101  6.676   1.00 20.70 ? 63  ALA   A CB  1 
ATOM   360  N N   . PRO   A 1 50  ? 18.964  -8.181  9.945   1.00 19.31 ? 64  PRO   A N   1 
ATOM   361  C CA  . PRO   A 1 50  ? 19.244  -7.336  11.113  1.00 19.70 ? 64  PRO   A CA  1 
ATOM   362  C C   . PRO   A 1 50  ? 20.520  -7.743  11.838  1.00 20.51 ? 64  PRO   A C   1 
ATOM   363  O O   . PRO   A 1 50  ? 21.087  -8.820  11.627  1.00 21.18 ? 64  PRO   A O   1 
ATOM   364  C CB  . PRO   A 1 50  ? 18.012  -7.540  12.004  1.00 21.44 ? 64  PRO   A CB  1 
ATOM   365  C CG  . PRO   A 1 50  ? 17.426  -8.839  11.559  1.00 21.46 ? 64  PRO   A CG  1 
ATOM   366  C CD  . PRO   A 1 50  ? 17.705  -8.931  10.092  1.00 20.73 ? 64  PRO   A CD  1 
ATOM   367  N N   . ALA   A 1 51  ? 20.977  -6.840  12.701  1.00 20.67 ? 65  ALA   A N   1 
ATOM   368  C CA  . ALA   A 1 51  ? 22.151  -7.108  13.513  1.00 21.95 ? 65  ALA   A CA  1 
ATOM   369  C C   . ALA   A 1 51  ? 21.892  -8.293  14.436  1.00 23.27 ? 65  ALA   A C   1 
ATOM   370  O O   . ALA   A 1 51  ? 20.748  -8.643  14.741  1.00 24.38 ? 65  ALA   A O   1 
ATOM   371  C CB  . ALA   A 1 51  ? 22.505  -5.876  14.346  1.00 22.18 ? 65  ALA   A CB  1 
ATOM   372  N N   . THR   A 1 52  ? 22.981  -8.919  14.878  1.00 24.22 ? 66  THR   A N   1 
ATOM   373  C CA  . THR   A 1 52  ? 22.918  -10.090 15.743  1.00 26.75 ? 66  THR   A CA  1 
ATOM   374  C C   . THR   A 1 52  ? 23.342  -9.772  17.177  1.00 27.97 ? 66  THR   A C   1 
ATOM   375  O O   . THR   A 1 52  ? 23.799  -10.655 17.907  1.00 29.80 ? 66  THR   A O   1 
ATOM   376  C CB  . THR   A 1 52  ? 23.763  -11.224 15.165  1.00 28.51 ? 66  THR   A CB  1 
ATOM   377  O OG1 . THR   A 1 52  ? 25.119  -10.782 15.028  1.00 28.90 ? 66  THR   A OG1 1 
ATOM   378  C CG2 . THR   A 1 52  ? 23.234  -11.636 13.802  1.00 29.01 ? 66  THR   A CG2 1 
ATOM   379  N N   . ASP   A 1 53  ? 23.192  -8.514  17.593  1.00 27.76 ? 67  ASP   A N   1 
ATOM   380  C CA  . ASP   A 1 53  ? 23.654  -8.047  18.894  1.00 27.67 ? 67  ASP   A CA  1 
ATOM   381  C C   . ASP   A 1 53  ? 22.509  -7.746  19.855  1.00 27.71 ? 67  ASP   A C   1 
ATOM   382  O O   . ASP   A 1 53  ? 22.710  -7.033  20.842  1.00 28.76 ? 67  ASP   A O   1 
ATOM   383  C CB  . ASP   A 1 53  ? 24.547  -6.815  18.731  1.00 28.30 ? 67  ASP   A CB  1 
ATOM   384  C CG  . ASP   A 1 53  ? 23.828  -5.656  18.056  1.00 29.62 ? 67  ASP   A CG  1 
ATOM   385  O OD1 . ASP   A 1 53  ? 22.613  -5.777  17.790  1.00 27.70 ? 67  ASP   A OD1 1 
ATOM   386  O OD2 . ASP   A 1 53  ? 24.478  -4.621  17.786  1.00 31.48 ? 67  ASP   A OD2 1 
ATOM   387  N N   . GLY   A 1 54  ? 21.311  -8.254  19.581  1.00 26.55 ? 68  GLY   A N   1 
ATOM   388  C CA  . GLY   A 1 54  ? 20.165  -7.970  20.419  1.00 24.71 ? 68  GLY   A CA  1 
ATOM   389  C C   . GLY   A 1 54  ? 19.325  -6.783  19.991  1.00 24.01 ? 68  GLY   A C   1 
ATOM   390  O O   . GLY   A 1 54  ? 18.325  -6.485  20.656  1.00 25.76 ? 68  GLY   A O   1 
ATOM   391  N N   . SER   A 1 55  ? 19.686  -6.105  18.902  1.00 21.88 ? 69  SER   A N   1 
ATOM   392  C CA  . SER   A 1 55  ? 18.941  -4.952  18.421  1.00 20.50 ? 69  SER   A CA  1 
ATOM   393  C C   . SER   A 1 55  ? 17.667  -5.391  17.703  1.00 19.32 ? 69  SER   A C   1 
ATOM   394  O O   . SER   A 1 55  ? 17.572  -6.500  17.170  1.00 20.12 ? 69  SER   A O   1 
ATOM   395  C CB  . SER   A 1 55  ? 19.798  -4.142  17.446  1.00 22.80 ? 69  SER   A CB  1 
ATOM   396  O OG  . SER   A 1 55  ? 20.973  -3.644  18.068  1.00 24.73 ? 69  SER   A OG  1 
ATOM   397  N N   . GLY   A 1 56  ? 16.686  -4.492  17.678  1.00 19.01 ? 70  GLY   A N   1 
ATOM   398  C CA  . GLY   A 1 56  ? 15.475  -4.721  16.910  1.00 18.36 ? 70  GLY   A CA  1 
ATOM   399  C C   . GLY   A 1 56  ? 15.717  -4.591  15.412  1.00 17.27 ? 70  GLY   A C   1 
ATOM   400  O O   . GLY   A 1 56  ? 16.816  -4.278  14.950  1.00 16.65 ? 70  GLY   A O   1 
ATOM   401  N N   . THR   A 1 57  ? 14.654  -4.842  14.641  1.00 16.28 ? 71  THR   A N   1 
ATOM   402  C CA  . THR   A 1 57  ? 14.689  -4.824  13.175  1.00 15.48 ? 71  THR   A CA  1 
ATOM   403  C C   . THR   A 1 57  ? 14.003  -3.560  12.663  1.00 15.14 ? 71  THR   A C   1 
ATOM   404  O O   . THR   A 1 57  ? 12.793  -3.379  12.861  1.00 14.60 ? 71  THR   A O   1 
ATOM   405  C CB  . THR   A 1 57  ? 13.987  -6.051  12.583  1.00 15.71 ? 71  THR   A CB  1 
ATOM   406  O OG1 . THR   A 1 57  ? 14.592  -7.251  13.084  1.00 16.78 ? 71  THR   A OG1 1 
ATOM   407  C CG2 . THR   A 1 57  ? 14.083  -6.047  11.054  1.00 16.47 ? 71  THR   A CG2 1 
ATOM   408  N N   . ALA   A 1 58  ? 14.761  -2.704  11.985  1.00 14.28 ? 72  ALA   A N   1 
ATOM   409  C CA  . ALA   A 1 58  ? 14.207  -1.437  11.516  1.00 13.72 ? 72  ALA   A CA  1 
ATOM   410  C C   . ALA   A 1 58  ? 13.234  -1.652  10.356  1.00 14.01 ? 72  ALA   A C   1 
ATOM   411  O O   . ALA   A 1 58  ? 13.415  -2.549  9.524   1.00 14.80 ? 72  ALA   A O   1 
ATOM   412  C CB  . ALA   A 1 58  ? 15.334  -0.495  11.100  1.00 14.34 ? 72  ALA   A CB  1 
ATOM   413  N N   . LEU   A 1 59  ? 12.199  -0.808  10.295  1.00 13.02 ? 73  LEU   A N   1 
ATOM   414  C CA  A LEU   A 1 59  ? 11.185  -0.934  9.256   0.52 12.99 ? 73  LEU   A CA  1 
ATOM   415  C CA  B LEU   A 1 59  ? 11.177  -0.938  9.261   0.48 12.96 ? 73  LEU   A CA  1 
ATOM   416  C C   . LEU   A 1 59  ? 10.388  0.364   9.135   1.00 12.15 ? 73  LEU   A C   1 
ATOM   417  O O   . LEU   A 1 59  ? 10.439  1.232   10.010  1.00 13.83 ? 73  LEU   A O   1 
ATOM   418  C CB  A LEU   A 1 59  ? 10.257  -2.120  9.534   0.52 13.99 ? 73  LEU   A CB  1 
ATOM   419  C CB  B LEU   A 1 59  ? 10.244  -2.137  9.514   0.48 13.95 ? 73  LEU   A CB  1 
ATOM   420  C CG  A LEU   A 1 59  ? 9.668   -2.191  10.946  0.52 15.41 ? 73  LEU   A CG  1 
ATOM   421  C CG  B LEU   A 1 59  ? 8.985   -2.011  10.393  0.48 15.35 ? 73  LEU   A CG  1 
ATOM   422  C CD1 A LEU   A 1 59  ? 8.476   -1.254  11.128  0.52 16.64 ? 73  LEU   A CD1 1 
ATOM   423  C CD1 B LEU   A 1 59  ? 8.145   -3.289  10.311  0.48 16.36 ? 73  LEU   A CD1 1 
ATOM   424  C CD2 A LEU   A 1 59  ? 9.261   -3.614  11.236  0.52 15.86 ? 73  LEU   A CD2 1 
ATOM   425  C CD2 B LEU   A 1 59  ? 9.330   -1.707  11.844  0.48 15.91 ? 73  LEU   A CD2 1 
ATOM   426  N N   . GLY   A 1 60  ? 9.634   0.470   8.040   1.00 11.05 ? 74  GLY   A N   1 
ATOM   427  C CA  . GLY   A 1 60  ? 8.705   1.573   7.856   1.00 10.69 ? 74  GLY   A CA  1 
ATOM   428  C C   . GLY   A 1 60  ? 7.692   1.255   6.779   1.00 10.14 ? 74  GLY   A C   1 
ATOM   429  O O   . GLY   A 1 60  ? 7.941   0.417   5.909   1.00 11.12 ? 74  GLY   A O   1 
ATOM   430  N N   . TRP   A 1 61  ? 6.529   1.912   6.850   1.00 10.32 ? 75  TRP   A N   1 
ATOM   431  C CA  . TRP   A 1 61  ? 5.524   1.717   5.804   1.00 9.26  ? 75  TRP   A CA  1 
ATOM   432  C C   . TRP   A 1 61  ? 4.641   2.952   5.687   1.00 9.49  ? 75  TRP   A C   1 
ATOM   433  O O   . TRP   A 1 61  ? 4.612   3.804   6.581   1.00 10.58 ? 75  TRP   A O   1 
ATOM   434  C CB  . TRP   A 1 61  ? 4.689   0.439   6.021   1.00 10.33 ? 75  TRP   A CB  1 
ATOM   435  C CG  . TRP   A 1 61  ? 3.727   0.484   7.189   1.00 10.51 ? 75  TRP   A CG  1 
ATOM   436  C CD1 . TRP   A 1 61  ? 2.407   0.812   7.142   1.00 10.51 ? 75  TRP   A CD1 1 
ATOM   437  C CD2 . TRP   A 1 61  ? 4.011   0.155   8.560   1.00 10.75 ? 75  TRP   A CD2 1 
ATOM   438  N NE1 . TRP   A 1 61  ? 1.846   0.703   8.392   1.00 11.52 ? 75  TRP   A NE1 1 
ATOM   439  C CE2 . TRP   A 1 61  ? 2.811   0.316   9.282   1.00 11.30 ? 75  TRP   A CE2 1 
ATOM   440  C CE3 . TRP   A 1 61  ? 5.159   -0.267  9.244   1.00 11.55 ? 75  TRP   A CE3 1 
ATOM   441  C CZ2 . TRP   A 1 61  ? 2.725   0.089   10.663  1.00 12.83 ? 75  TRP   A CZ2 1 
ATOM   442  C CZ3 . TRP   A 1 61  ? 5.071   -0.490  10.617  1.00 12.70 ? 75  TRP   A CZ3 1 
ATOM   443  C CH2 . TRP   A 1 61  ? 3.862   -0.315  11.303  1.00 12.63 ? 75  TRP   A CH2 1 
ATOM   444  N N   . THR   A 1 62  ? 3.912   3.027   4.561   1.00 9.26  ? 76  THR   A N   1 
ATOM   445  C CA  . THR   A 1 62  ? 3.029   4.144   4.231   1.00 9.04  ? 76  THR   A CA  1 
ATOM   446  C C   . THR   A 1 62  ? 1.633   3.639   3.878   1.00 9.12  ? 76  THR   A C   1 
ATOM   447  O O   . THR   A 1 62  ? 1.482   2.620   3.189   1.00 10.51 ? 76  THR   A O   1 
ATOM   448  C CB  . THR   A 1 62  ? 3.561   4.936   3.008   1.00 9.67  ? 76  THR   A CB  1 
ATOM   449  O OG1 . THR   A 1 62  ? 4.892   5.382   3.253   1.00 9.76  ? 76  THR   A OG1 1 
ATOM   450  C CG2 . THR   A 1 62  ? 2.678   6.156   2.703   1.00 10.29 ? 76  THR   A CG2 1 
ATOM   451  N N   . VAL   A 1 63  ? 0.612   4.370   4.338   1.00 9.38  ? 77  VAL   A N   1 
ATOM   452  C CA  . VAL   A 1 63  ? -0.766  4.241   3.867   1.00 10.02 ? 77  VAL   A CA  1 
ATOM   453  C C   . VAL   A 1 63  ? -1.203  5.604   3.346   1.00 9.38  ? 77  VAL   A C   1 
ATOM   454  O O   . VAL   A 1 63  ? -1.120  6.601   4.076   1.00 10.73 ? 77  VAL   A O   1 
ATOM   455  C CB  . VAL   A 1 63  ? -1.716  3.807   4.993   1.00 10.56 ? 77  VAL   A CB  1 
ATOM   456  C CG1 . VAL   A 1 63  ? -3.179  3.908   4.543   1.00 11.63 ? 77  VAL   A CG1 1 
ATOM   457  C CG2 . VAL   A 1 63  ? -1.379  2.411   5.469   1.00 11.49 ? 77  VAL   A CG2 1 
ATOM   458  N N   . ALA   A 1 64  ? -1.662  5.657   2.090   1.00 9.54  ? 78  ALA   A N   1 
ATOM   459  C CA  . ALA   A 1 64  ? -2.419  6.804   1.601   1.00 9.61  ? 78  ALA   A CA  1 
ATOM   460  C C   . ALA   A 1 64  ? -3.898  6.516   1.831   1.00 10.65 ? 78  ALA   A C   1 
ATOM   461  O O   . ALA   A 1 64  ? -4.384  5.443   1.451   1.00 11.22 ? 78  ALA   A O   1 
ATOM   462  C CB  . ALA   A 1 64  ? -2.150  7.032   0.112   1.00 11.35 ? 78  ALA   A CB  1 
ATOM   463  N N   . TRP   A 1 65  ? -4.612  7.468   2.444   1.00 10.89 ? 79  TRP   A N   1 
ATOM   464  C CA  . TRP   A 1 65  ? -5.961  7.213   2.948   1.00 10.72 ? 79  TRP   A CA  1 
ATOM   465  C C   . TRP   A 1 65  ? -7.043  7.350   1.875   1.00 10.81 ? 79  TRP   A C   1 
ATOM   466  O O   . TRP   A 1 65  ? -8.049  8.056   2.062   1.00 11.37 ? 79  TRP   A O   1 
ATOM   467  C CB  . TRP   A 1 65  ? -6.242  8.073   4.191   1.00 11.21 ? 79  TRP   A CB  1 
ATOM   468  C CG  . TRP   A 1 65  ? -5.309  7.747   5.332   1.00 10.54 ? 79  TRP   A CG  1 
ATOM   469  C CD1 . TRP   A 1 65  ? -4.266  8.508   5.778   1.00 10.33 ? 79  TRP   A CD1 1 
ATOM   470  C CD2 . TRP   A 1 65  ? -5.313  6.556   6.136   1.00 10.55 ? 79  TRP   A CD2 1 
ATOM   471  N NE1 . TRP   A 1 65  ? -3.617  7.865   6.812   1.00 10.14 ? 79  TRP   A NE1 1 
ATOM   472  C CE2 . TRP   A 1 65  ? -4.245  6.668   7.057   1.00 10.24 ? 79  TRP   A CE2 1 
ATOM   473  C CE3 . TRP   A 1 65  ? -6.119  5.410   6.170   1.00 11.74 ? 79  TRP   A CE3 1 
ATOM   474  C CZ2 . TRP   A 1 65  ? -3.967  5.678   8.009   1.00 10.94 ? 79  TRP   A CZ2 1 
ATOM   475  C CZ3 . TRP   A 1 65  ? -5.840  4.428   7.116   1.00 12.49 ? 79  TRP   A CZ3 1 
ATOM   476  C CH2 . TRP   A 1 65  ? -4.774  4.572   8.023   1.00 12.08 ? 79  TRP   A CH2 1 
ATOM   477  N N   . LYS   A 1 66  ? -6.836  6.653   0.751   1.00 11.31 ? 80  LYS   A N   1 
ATOM   478  C CA  . LYS   A 1 66  ? -7.797  6.530   -0.340  1.00 10.84 ? 80  LYS   A CA  1 
ATOM   479  C C   . LYS   A 1 66  ? -8.060  5.049   -0.573  1.00 10.99 ? 80  LYS   A C   1 
ATOM   480  O O   . LYS   A 1 66  ? -7.114  4.263   -0.710  1.00 11.69 ? 80  LYS   A O   1 
ATOM   481  C CB  . LYS   A 1 66  ? -7.251  7.169   -1.629  1.00 11.98 ? 80  LYS   A CB  1 
ATOM   482  C CG  . LYS   A 1 66  ? -8.080  6.888   -2.891  1.00 13.03 ? 80  LYS   A CG  1 
ATOM   483  C CD  . LYS   A 1 66  ? -7.386  7.497   -4.126  1.00 15.14 ? 80  LYS   A CD  1 
ATOM   484  C CE  . LYS   A 1 66  ? -8.113  7.160   -5.418  1.00 17.30 ? 80  LYS   A CE  1 
ATOM   485  N NZ  . LYS   A 1 66  ? -8.078  5.706   -5.720  1.00 19.47 ? 80  LYS   A NZ  1 
ATOM   486  N N   . ASN   A 1 67  ? -9.331  4.670   -0.598  1.00 11.44 ? 81  ASN   A N   1 
ATOM   487  C CA  . ASN   A 1 67  ? -9.736  3.330   -1.030  1.00 12.13 ? 81  ASN   A CA  1 
ATOM   488  C C   . ASN   A 1 67  ? -11.021 3.483   -1.837  1.00 12.44 ? 81  ASN   A C   1 
ATOM   489  O O   . ASN   A 1 67  ? -11.382 4.588   -2.256  1.00 13.43 ? 81  ASN   A O   1 
ATOM   490  C CB  . ASN   A 1 67  ? -9.780  2.320   0.136   1.00 13.17 ? 81  ASN   A CB  1 
ATOM   491  C CG  . ASN   A 1 67  ? -10.864 2.631   1.156   1.00 12.94 ? 81  ASN   A CG  1 
ATOM   492  O OD1 . ASN   A 1 67  ? -11.720 3.490   0.936   1.00 13.15 ? 81  ASN   A OD1 1 
ATOM   493  N ND2 . ASN   A 1 67  ? -10.837 1.921   2.283   1.00 14.51 ? 81  ASN   A ND2 1 
ATOM   494  N N   . ASN   A 1 68  ? -11.739 2.377   -2.057  1.00 13.98 ? 82  ASN   A N   1 
ATOM   495  C CA  . ASN   A 1 68  ? -12.957 2.459   -2.863  1.00 15.14 ? 82  ASN   A CA  1 
ATOM   496  C C   . ASN   A 1 68  ? -14.078 3.200   -2.153  1.00 15.70 ? 82  ASN   A C   1 
ATOM   497  O O   . ASN   A 1 68  ? -15.053 3.597   -2.801  1.00 18.24 ? 82  ASN   A O   1 
ATOM   498  C CB  . ASN   A 1 68  ? -13.469 1.065   -3.224  1.00 17.93 ? 82  ASN   A CB  1 
ATOM   499  C CG  . ASN   A 1 68  ? -12.601 0.355   -4.250  1.00 20.43 ? 82  ASN   A CG  1 
ATOM   500  O OD1 . ASN   A 1 68  ? -11.574 0.867   -4.696  1.00 21.00 ? 82  ASN   A OD1 1 
ATOM   501  N ND2 . ASN   A 1 68  ? -13.015 -0.845  -4.623  1.00 24.02 ? 82  ASN   A ND2 1 
ATOM   502  N N   . TYR   A 1 69  ? -13.972 3.375   -0.841  1.00 14.51 ? 83  TYR   A N   1 
ATOM   503  C CA  . TYR   A 1 69  ? -15.048 3.934   -0.035  1.00 14.22 ? 83  TYR   A CA  1 
ATOM   504  C C   . TYR   A 1 69  ? -14.856 5.409   0.278   1.00 14.67 ? 83  TYR   A C   1 
ATOM   505  O O   . TYR   A 1 69  ? -15.827 6.171   0.233   1.00 15.64 ? 83  TYR   A O   1 
ATOM   506  C CB  . TYR   A 1 69  ? -15.174 3.154   1.281   1.00 15.92 ? 83  TYR   A CB  1 
ATOM   507  C CG  . TYR   A 1 69  ? -15.417 1.680   1.070   1.00 16.55 ? 83  TYR   A CG  1 
ATOM   508  C CD1 . TYR   A 1 69  ? -16.703 1.185   0.941   1.00 17.43 ? 83  TYR   A CD1 1 
ATOM   509  C CD2 . TYR   A 1 69  ? -14.361 0.788   0.958   1.00 18.35 ? 83  TYR   A CD2 1 
ATOM   510  C CE1 . TYR   A 1 69  ? -16.931 -0.158  0.728   1.00 18.50 ? 83  TYR   A CE1 1 
ATOM   511  C CE2 . TYR   A 1 69  ? -14.583 -0.557  0.739   1.00 19.58 ? 83  TYR   A CE2 1 
ATOM   512  C CZ  . TYR   A 1 69  ? -15.869 -1.021  0.628   1.00 19.89 ? 83  TYR   A CZ  1 
ATOM   513  O OH  . TYR   A 1 69  ? -16.096 -2.357  0.409   1.00 22.20 ? 83  TYR   A OH  1 
ATOM   514  N N   . ARG   A 1 70  ? -13.629 5.826   0.592   1.00 14.15 ? 84  ARG   A N   1 
ATOM   515  C CA  . ARG   A 1 70  ? -13.371 7.169   1.099   1.00 14.59 ? 84  ARG   A CA  1 
ATOM   516  C C   . ARG   A 1 70  ? -12.011 7.643   0.606   1.00 13.34 ? 84  ARG   A C   1 
ATOM   517  O O   . ARG   A 1 70  ? -11.155 6.845   0.227   1.00 13.72 ? 84  ARG   A O   1 
ATOM   518  C CB  . ARG   A 1 70  ? -13.377 7.197   2.637   1.00 16.46 ? 84  ARG   A CB  1 
ATOM   519  C CG  . ARG   A 1 70  ? -14.698 6.808   3.274   1.00 18.35 ? 84  ARG   A CG  1 
ATOM   520  C CD  . ARG   A 1 70  ? -14.645 7.022   4.764   1.00 20.11 ? 84  ARG   A CD  1 
ATOM   521  N NE  . ARG   A 1 70  ? -15.826 6.498   5.430   1.00 22.86 ? 84  ARG   A NE  1 
ATOM   522  C CZ  . ARG   A 1 70  ? -16.203 6.853   6.649   1.00 25.22 ? 84  ARG   A CZ  1 
ATOM   523  N NH1 . ARG   A 1 70  ? -15.555 7.789   7.325   1.00 25.88 ? 84  ARG   A NH1 1 
ATOM   524  N NH2 . ARG   A 1 70  ? -17.254 6.256   7.204   1.00 26.41 ? 84  ARG   A NH2 1 
ATOM   525  N N   . ASN   A 1 71  ? -11.820 8.960   0.629   1.00 13.27 ? 85  ASN   A N   1 
ATOM   526  C CA  . ASN   A 1 71  ? -10.515 9.562   0.353   1.00 12.74 ? 85  ASN   A CA  1 
ATOM   527  C C   . ASN   A 1 71  ? -10.340 10.763  1.272   1.00 12.53 ? 85  ASN   A C   1 
ATOM   528  O O   . ASN   A 1 71  ? -11.008 11.788  1.092   1.00 14.24 ? 85  ASN   A O   1 
ATOM   529  C CB  . ASN   A 1 71  ? -10.379 9.977   -1.112  1.00 12.88 ? 85  ASN   A CB  1 
ATOM   530  C CG  . ASN   A 1 71  ? -8.952  10.354  -1.471  1.00 12.66 ? 85  ASN   A CG  1 
ATOM   531  O OD1 . ASN   A 1 71  ? -8.095  10.465  -0.593  1.00 12.88 ? 85  ASN   A OD1 1 
ATOM   532  N ND2 . ASN   A 1 71  ? -8.684  10.544  -2.755  1.00 13.58 ? 85  ASN   A ND2 1 
ATOM   533  N N   . ALA   A 1 72  ? -9.450  10.638  2.254   1.00 11.91 ? 86  ALA   A N   1 
ATOM   534  C CA  . ALA   A 1 72  ? -9.162  11.704  3.208   1.00 11.92 ? 86  ALA   A CA  1 
ATOM   535  C C   . ALA   A 1 72  ? -8.115  12.693  2.707   1.00 11.83 ? 86  ALA   A C   1 
ATOM   536  O O   . ALA   A 1 72  ? -7.830  13.673  3.403   1.00 13.09 ? 86  ALA   A O   1 
ATOM   537  C CB  . ALA   A 1 72  ? -8.719  11.110  4.548   1.00 13.28 ? 86  ALA   A CB  1 
ATOM   538  N N   . HIS   A 1 73  ? -7.536  12.461  1.530   1.00 11.96 ? 87  HIS   A N   1 
ATOM   539  C CA  . HIS   A 1 73  ? -6.484  13.319  0.971   1.00 10.95 ? 87  HIS   A CA  1 
ATOM   540  C C   . HIS   A 1 73  ? -5.332  13.509  1.966   1.00 10.94 ? 87  HIS   A C   1 
ATOM   541  O O   . HIS   A 1 73  ? -4.967  14.627  2.338   1.00 11.57 ? 87  HIS   A O   1 
ATOM   542  C CB  . HIS   A 1 73  ? -7.037  14.664  0.482   1.00 12.01 ? 87  HIS   A CB  1 
ATOM   543  C CG  . HIS   A 1 73  ? -8.137  14.535  -0.527  1.00 13.58 ? 87  HIS   A CG  1 
ATOM   544  N ND1 . HIS   A 1 73  ? -8.021  13.782  -1.678  1.00 13.64 ? 87  HIS   A ND1 1 
ATOM   545  C CD2 . HIS   A 1 73  ? -9.378  15.073  -0.555  1.00 14.77 ? 87  HIS   A CD2 1 
ATOM   546  C CE1 . HIS   A 1 73  ? -9.143  13.865  -2.371  1.00 15.40 ? 87  HIS   A CE1 1 
ATOM   547  N NE2 . HIS   A 1 73  ? -9.983  14.639  -1.710  1.00 15.88 ? 87  HIS   A NE2 1 
ATOM   548  N N   . SER   A 1 74  ? -4.749  12.389  2.386   1.00 10.28 ? 88  SER   A N   1 
ATOM   549  C CA  . SER   A 1 74  ? -3.733  12.382  3.434   1.00 9.91  ? 88  SER   A CA  1 
ATOM   550  C C   . SER   A 1 74  ? -2.995  11.048  3.381   1.00 9.44  ? 88  SER   A C   1 
ATOM   551  O O   . SER   A 1 74  ? -3.455  10.091  2.753   1.00 10.25 ? 88  SER   A O   1 
ATOM   552  C CB  . SER   A 1 74  ? -4.350  12.613  4.815   1.00 11.32 ? 88  SER   A CB  1 
ATOM   553  O OG  . SER   A 1 74  ? -5.193  11.530  5.165   1.00 11.73 ? 88  SER   A OG  1 
ATOM   554  N N   . ALA   A 1 75  ? -1.851  10.986  4.075   1.00 9.62  ? 89  ALA   A N   1 
ATOM   555  C CA  . ALA   A 1 75  ? -1.048  9.771   4.109   1.00 9.91  ? 89  ALA   A CA  1 
ATOM   556  C C   . ALA   A 1 75  ? -0.302  9.711   5.437   1.00 9.37  ? 89  ALA   A C   1 
ATOM   557  O O   . ALA   A 1 75  ? 0.204   10.733  5.909   1.00 10.10 ? 89  ALA   A O   1 
ATOM   558  C CB  . ALA   A 1 75  ? -0.048  9.741   2.943   1.00 11.54 ? 89  ALA   A CB  1 
ATOM   559  N N   . THR   A 1 76  ? -0.214  8.509   6.021   1.00 9.25  ? 90  THR   A N   1 
ATOM   560  C CA  . THR   A 1 76  ? 0.563   8.276   7.236   1.00 9.12  ? 90  THR   A CA  1 
ATOM   561  C C   . THR   A 1 76  ? 1.781   7.417   6.911   1.00 9.33  ? 90  THR   A C   1 
ATOM   562  O O   . THR   A 1 76  ? 1.677   6.441   6.158   1.00 9.45  ? 90  THR   A O   1 
ATOM   563  C CB  . THR   A 1 76  ? -0.273  7.533   8.287   1.00 9.76  ? 90  THR   A CB  1 
ATOM   564  O OG1 . THR   A 1 76  ? -1.427  8.319   8.607   1.00 9.94  ? 90  THR   A OG1 1 
ATOM   565  C CG2 . THR   A 1 76  ? 0.531   7.266   9.568   1.00 9.75  ? 90  THR   A CG2 1 
ATOM   566  N N   . THR   A 1 77  ? 2.934   7.773   7.478   1.00 8.93  ? 91  THR   A N   1 
ATOM   567  C CA  . THR   A 1 77  ? 4.104   6.899   7.491   1.00 9.28  ? 91  THR   A CA  1 
ATOM   568  C C   . THR   A 1 77  ? 4.413   6.501   8.929   1.00 9.27  ? 91  THR   A C   1 
ATOM   569  O O   . THR   A 1 77  ? 4.451   7.359   9.822   1.00 11.05 ? 91  THR   A O   1 
ATOM   570  C CB  . THR   A 1 77  ? 5.346   7.573   6.883   1.00 10.40 ? 91  THR   A CB  1 
ATOM   571  O OG1 . THR   A 1 77  ? 5.697   8.745   7.641   1.00 10.85 ? 91  THR   A OG1 1 
ATOM   572  C CG2 . THR   A 1 77  ? 5.115   7.948   5.426   1.00 11.27 ? 91  THR   A CG2 1 
ATOM   573  N N   . TRP   A 1 78  ? 4.650   5.209   9.147   1.00 9.34  ? 92  TRP   A N   1 
ATOM   574  C CA  . TRP   A 1 78  ? 5.117   4.686   10.427  1.00 9.18  ? 92  TRP   A CA  1 
ATOM   575  C C   . TRP   A 1 78  ? 6.579   4.286   10.277  1.00 9.91  ? 92  TRP   A C   1 
ATOM   576  O O   . TRP   A 1 78  ? 6.934   3.586   9.319   1.00 10.41 ? 92  TRP   A O   1 
ATOM   577  C CB  . TRP   A 1 78  ? 4.325   3.448   10.855  1.00 10.16 ? 92  TRP   A CB  1 
ATOM   578  C CG  . TRP   A 1 78  ? 2.873   3.612   11.220  1.00 10.21 ? 92  TRP   A CG  1 
ATOM   579  C CD1 . TRP   A 1 78  ? 2.351   3.623   12.485  1.00 10.34 ? 92  TRP   A CD1 1 
ATOM   580  C CD2 . TRP   A 1 78  ? 1.749   3.702   10.324  1.00 10.19 ? 92  TRP   A CD2 1 
ATOM   581  N NE1 . TRP   A 1 78  ? 0.983   3.713   12.436  1.00 10.86 ? 92  TRP   A NE1 1 
ATOM   582  C CE2 . TRP   A 1 78  ? 0.585   3.765   11.123  1.00 10.14 ? 92  TRP   A CE2 1 
ATOM   583  C CE3 . TRP   A 1 78  ? 1.612   3.731   8.927   1.00 10.35 ? 92  TRP   A CE3 1 
ATOM   584  C CZ2 . TRP   A 1 78  ? -0.694  3.864   10.574  1.00 11.13 ? 92  TRP   A CZ2 1 
ATOM   585  C CZ3 . TRP   A 1 78  ? 0.333   3.820   8.389   1.00 10.89 ? 92  TRP   A CZ3 1 
ATOM   586  C CH2 . TRP   A 1 78  ? -0.797  3.892   9.210   1.00 11.08 ? 92  TRP   A CH2 1 
ATOM   587  N N   . SER   A 1 79  ? 7.414   4.717   11.218  1.00 9.69  ? 93  SER   A N   1 
ATOM   588  C CA  . SER   A 1 79  ? 8.836   4.407   11.250  1.00 10.66 ? 93  SER   A CA  1 
ATOM   589  C C   . SER   A 1 79  ? 9.139   3.766   12.600  1.00 10.67 ? 93  SER   A C   1 
ATOM   590  O O   . SER   A 1 79  ? 8.778   4.324   13.643  1.00 11.36 ? 93  SER   A O   1 
ATOM   591  C CB  . SER   A 1 79  ? 9.630   5.705   11.115  1.00 11.57 ? 93  SER   A CB  1 
ATOM   592  O OG  . SER   A 1 79  ? 11.030  5.472   11.129  1.00 12.96 ? 93  SER   A OG  1 
ATOM   593  N N   . GLY   A 1 80  ? 9.783   2.605   12.604  1.00 10.63 ? 94  GLY   A N   1 
ATOM   594  C CA  . GLY   A 1 80  ? 10.012  1.952   13.877  1.00 12.00 ? 94  GLY   A CA  1 
ATOM   595  C C   . GLY   A 1 80  ? 10.871  0.713   13.802  1.00 11.82 ? 94  GLY   A C   1 
ATOM   596  O O   . GLY   A 1 80  ? 11.696  0.557   12.899  1.00 11.99 ? 94  GLY   A O   1 
ATOM   597  N N   . GLN   A 1 81  ? 10.689  -0.159  14.797  1.00 13.07 ? 95  GLN   A N   1 
ATOM   598  C CA  . GLN   A 1 81  ? 11.454  -1.396  14.870  1.00 13.83 ? 95  GLN   A CA  1 
ATOM   599  C C   . GLN   A 1 81  ? 10.630  -2.526  15.473  1.00 14.22 ? 95  GLN   A C   1 
ATOM   600  O O   . GLN   A 1 81  ? 9.811   -2.315  16.376  1.00 14.49 ? 95  GLN   A O   1 
ATOM   601  C CB  . GLN   A 1 81  ? 12.797  -1.226  15.595  1.00 15.15 ? 95  GLN   A CB  1 
ATOM   602  C CG  . GLN   A 1 81  ? 12.715  -0.773  17.043  1.00 16.01 ? 95  GLN   A CG  1 
ATOM   603  C CD  . GLN   A 1 81  ? 14.093  -0.627  17.675  1.00 16.06 ? 95  GLN   A CD  1 
ATOM   604  O OE1 . GLN   A 1 81  ? 14.975  -1.477  17.497  1.00 16.83 ? 95  GLN   A OE1 1 
ATOM   605  N NE2 . GLN   A 1 81  ? 14.284  0.455   18.427  1.00 16.97 ? 95  GLN   A NE2 1 
ATOM   606  N N   . TYR   A 1 82  ? 10.856  -3.721  14.937  1.00 15.32 ? 96  TYR   A N   1 
ATOM   607  C CA  . TYR   A 1 82  ? 10.305  -4.966  15.453  1.00 16.28 ? 96  TYR   A CA  1 
ATOM   608  C C   . TYR   A 1 82  ? 11.219  -5.509  16.546  1.00 17.08 ? 96  TYR   A C   1 
ATOM   609  O O   . TYR   A 1 82  ? 12.438  -5.574  16.364  1.00 17.10 ? 96  TYR   A O   1 
ATOM   610  C CB  . TYR   A 1 82  ? 10.215  -5.968  14.301  1.00 16.47 ? 96  TYR   A CB  1 
ATOM   611  C CG  . TYR   A 1 82  ? 10.022  -7.415  14.706  1.00 16.63 ? 96  TYR   A CG  1 
ATOM   612  C CD1 . TYR   A 1 82  ? 8.754   -7.938  14.934  1.00 17.55 ? 96  TYR   A CD1 1 
ATOM   613  C CD2 . TYR   A 1 82  ? 11.110  -8.271  14.817  1.00 19.04 ? 96  TYR   A CD2 1 
ATOM   614  C CE1 . TYR   A 1 82  ? 8.576   -9.268  15.287  1.00 19.22 ? 96  TYR   A CE1 1 
ATOM   615  C CE2 . TYR   A 1 82  ? 10.942  -9.596  15.176  1.00 20.24 ? 96  TYR   A CE2 1 
ATOM   616  C CZ  . TYR   A 1 82  ? 9.673   -10.090 15.406  1.00 19.89 ? 96  TYR   A CZ  1 
ATOM   617  O OH  . TYR   A 1 82  ? 9.507   -11.412 15.758  1.00 22.36 ? 96  TYR   A OH  1 
ATOM   618  N N   . VAL   A 1 83  ? 10.621  -5.908  17.670  1.00 19.10 ? 97  VAL   A N   1 
ATOM   619  C CA  . VAL   A 1 83  ? 11.332  -6.429  18.836  1.00 23.65 ? 97  VAL   A CA  1 
ATOM   620  C C   . VAL   A 1 83  ? 10.771  -7.819  19.113  1.00 26.16 ? 97  VAL   A C   1 
ATOM   621  O O   . VAL   A 1 83  ? 9.607   -7.954  19.516  1.00 27.64 ? 97  VAL   A O   1 
ATOM   622  C CB  . VAL   A 1 83  ? 11.152  -5.514  20.058  1.00 24.25 ? 97  VAL   A CB  1 
ATOM   623  C CG1 . VAL   A 1 83  ? 11.848  -6.086  21.297  1.00 24.82 ? 97  VAL   A CG1 1 
ATOM   624  C CG2 . VAL   A 1 83  ? 11.650  -4.102  19.750  1.00 25.28 ? 97  VAL   A CG2 1 
ATOM   625  N N   . GLY   A 1 84  ? 11.582  -8.854  18.891  1.00 27.15 ? 98  GLY   A N   1 
ATOM   626  C CA  . GLY   A 1 84  ? 11.129  -10.208 19.142  1.00 29.44 ? 98  GLY   A CA  1 
ATOM   627  C C   . GLY   A 1 84  ? 11.032  -10.523 20.623  1.00 31.24 ? 98  GLY   A C   1 
ATOM   628  O O   . GLY   A 1 84  ? 11.552  -9.806  21.477  1.00 32.10 ? 98  GLY   A O   1 
ATOM   629  N N   . GLY   A 1 85  ? 10.345  -11.616 20.929  1.00 32.77 ? 99  GLY   A N   1 
ATOM   630  C CA  . GLY   A 1 85  ? 10.190  -12.042 22.304  1.00 33.95 ? 99  GLY   A CA  1 
ATOM   631  C C   . GLY   A 1 85  ? 8.939   -12.882 22.477  1.00 34.91 ? 99  GLY   A C   1 
ATOM   632  O O   . GLY   A 1 85  ? 8.248   -13.213 21.513  1.00 35.87 ? 99  GLY   A O   1 
ATOM   633  N N   . ALA   A 1 86  ? 8.668   -13.222 23.741  1.00 34.78 ? 100 ALA   A N   1 
ATOM   634  C CA  . ALA   A 1 86  ? 7.440   -13.943 24.061  1.00 34.78 ? 100 ALA   A CA  1 
ATOM   635  C C   . ALA   A 1 86  ? 6.208   -13.094 23.793  1.00 35.28 ? 100 ALA   A C   1 
ATOM   636  O O   . ALA   A 1 86  ? 5.131   -13.633 23.510  1.00 37.35 ? 100 ALA   A O   1 
ATOM   637  C CB  . ALA   A 1 86  ? 7.462   -14.414 25.515  1.00 34.34 ? 100 ALA   A CB  1 
ATOM   638  N N   . GLU   A 1 87  ? 6.339   -11.774 23.890  1.00 33.08 ? 101 GLU   A N   1 
ATOM   639  C CA  . GLU   A 1 87  ? 5.302   -10.835 23.474  1.00 30.97 ? 101 GLU   A CA  1 
ATOM   640  C C   . GLU   A 1 87  ? 5.935   -9.945  22.410  1.00 28.01 ? 101 GLU   A C   1 
ATOM   641  O O   . GLU   A 1 87  ? 6.408   -8.845  22.706  1.00 27.35 ? 101 GLU   A O   1 
ATOM   642  C CB  . GLU   A 1 87  ? 4.776   -10.021 24.651  1.00 31.43 ? 101 GLU   A CB  1 
ATOM   643  C CG  . GLU   A 1 87  ? 3.576   -9.148  24.297  0.61 32.14 ? 101 GLU   A CG  1 
ATOM   644  C CD  . GLU   A 1 87  ? 3.357   -8.008  25.276  0.69 32.66 ? 101 GLU   A CD  1 
ATOM   645  O OE1 . GLU   A 1 87  ? 4.353   -7.491  25.826  0.22 32.89 ? 101 GLU   A OE1 1 
ATOM   646  O OE2 . GLU   A 1 87  ? 2.188   -7.630  25.495  0.52 33.16 ? 101 GLU   A OE2 1 
ATOM   647  N N   . ALA   A 1 88  ? 5.962   -10.439 21.173  1.00 26.34 ? 102 ALA   A N   1 
ATOM   648  C CA  . ALA   A 1 88  ? 6.528   -9.679  20.066  1.00 25.08 ? 102 ALA   A CA  1 
ATOM   649  C C   . ALA   A 1 88  ? 5.814   -8.341  19.908  1.00 22.32 ? 102 ALA   A C   1 
ATOM   650  O O   . ALA   A 1 88  ? 4.611   -8.222  20.150  1.00 23.00 ? 102 ALA   A O   1 
ATOM   651  C CB  . ALA   A 1 88  ? 6.412   -10.478 18.771  1.00 26.44 ? 102 ALA   A CB  1 
ATOM   652  N N   . ARG   A 1 89  ? 6.568   -7.333  19.474  1.00 21.17 ? 103 ARG   A N   1 
ATOM   653  C CA  . ARG   A 1 89  ? 6.069   -5.965  19.443  1.00 20.09 ? 103 ARG   A CA  1 
ATOM   654  C C   . ARG   A 1 89  ? 6.741   -5.189  18.315  1.00 18.50 ? 103 ARG   A C   1 
ATOM   655  O O   . ARG   A 1 89  ? 7.907   -5.426  17.986  1.00 19.21 ? 103 ARG   A O   1 
ATOM   656  C CB  . ARG   A 1 89  ? 6.347   -5.304  20.802  1.00 22.32 ? 103 ARG   A CB  1 
ATOM   657  C CG  . ARG   A 1 89  ? 5.678   -3.968  21.029  1.00 22.73 ? 103 ARG   A CG  1 
ATOM   658  C CD  . ARG   A 1 89  ? 5.859   -3.521  22.485  1.00 23.09 ? 103 ARG   A CD  1 
ATOM   659  N NE  . ARG   A 1 89  ? 5.051   -4.288  23.430  1.00 24.16 ? 103 ARG   A NE  1 
ATOM   660  C CZ  . ARG   A 1 89  ? 3.795   -3.995  23.740  1.00 24.15 ? 103 ARG   A CZ  1 
ATOM   661  N NH1 . ARG   A 1 89  ? 3.160   -2.987  23.162  1.00 23.20 ? 103 ARG   A NH1 1 
ATOM   662  N NH2 . ARG   A 1 89  ? 3.161   -4.732  24.649  1.00 25.75 ? 103 ARG   A NH2 1 
ATOM   663  N N   . ILE   A 1 90  ? 5.992   -4.271  17.710  1.00 16.15 ? 104 ILE   A N   1 
ATOM   664  C CA  . ILE   A 1 90  ? 6.554   -3.295  16.779  1.00 14.78 ? 104 ILE   A CA  1 
ATOM   665  C C   . ILE   A 1 90  ? 6.280   -1.913  17.365  1.00 14.18 ? 104 ILE   A C   1 
ATOM   666  O O   . ILE   A 1 90  ? 5.117   -1.534  17.561  1.00 15.14 ? 104 ILE   A O   1 
ATOM   667  C CB  . ILE   A 1 90  ? 5.972   -3.423  15.358  1.00 15.10 ? 104 ILE   A CB  1 
ATOM   668  C CG1 . ILE   A 1 90  ? 6.275   -4.803  14.756  1.00 17.15 ? 104 ILE   A CG1 1 
ATOM   669  C CG2 . ILE   A 1 90  ? 6.516   -2.312  14.459  1.00 15.24 ? 104 ILE   A CG2 1 
ATOM   670  C CD1 . ILE   A 1 90  ? 5.558   -5.060  13.422  1.00 18.04 ? 104 ILE   A CD1 1 
ATOM   671  N N   . ASN   A 1 91  ? 7.344   -1.181  17.688  1.00 14.21 ? 105 ASN   A N   1 
ATOM   672  C CA  . ASN   A 1 91  ? 7.231   0.159   18.255  1.00 13.43 ? 105 ASN   A CA  1 
ATOM   673  C C   . ASN   A 1 91  ? 7.511   1.188   17.171  1.00 12.06 ? 105 ASN   A C   1 
ATOM   674  O O   . ASN   A 1 91  ? 8.566   1.134   16.526  1.00 13.56 ? 105 ASN   A O   1 
ATOM   675  C CB  . ASN   A 1 91  ? 8.228   0.343   19.401  1.00 15.93 ? 105 ASN   A CB  1 
ATOM   676  C CG  . ASN   A 1 91  ? 7.916   -0.534  20.585  1.00 19.44 ? 105 ASN   A CG  1 
ATOM   677  O OD1 . ASN   A 1 91  ? 6.750   -0.754  20.920  1.00 19.91 ? 105 ASN   A OD1 1 
ATOM   678  N ND2 . ASN   A 1 91  ? 8.959   -1.049  21.228  1.00 22.63 ? 105 ASN   A ND2 1 
ATOM   679  N N   . THR   A 1 92  ? 6.590   2.139   17.000  1.00 11.42 ? 106 THR   A N   1 
ATOM   680  C CA  . THR   A 1 92  ? 6.694   3.103   15.916  1.00 11.20 ? 106 THR   A CA  1 
ATOM   681  C C   . THR   A 1 92  ? 6.413   4.524   16.380  1.00 10.65 ? 106 THR   A C   1 
ATOM   682  O O   . THR   A 1 92  ? 5.765   4.775   17.407  1.00 11.35 ? 106 THR   A O   1 
ATOM   683  C CB  . THR   A 1 92  ? 5.698   2.823   14.765  1.00 11.03 ? 106 THR   A CB  1 
ATOM   684  O OG1 . THR   A 1 92  ? 4.359   3.151   15.178  1.00 12.47 ? 106 THR   A OG1 1 
ATOM   685  C CG2 . THR   A 1 92  ? 5.764   1.372   14.295  1.00 12.40 ? 106 THR   A CG2 1 
ATOM   686  N N   . GLN   A 1 93  ? 6.908   5.454   15.567  1.00 10.93 ? 107 GLN   A N   1 
ATOM   687  C CA  A GLN   A 1 93  ? 6.420   6.817   15.557  0.65 11.34 ? 107 GLN   A CA  1 
ATOM   688  C CA  B GLN   A 1 93  ? 6.499   6.853   15.534  0.35 10.72 ? 107 GLN   A CA  1 
ATOM   689  C C   . GLN   A 1 93  ? 5.905   7.105   14.155  1.00 9.98  ? 107 GLN   A C   1 
ATOM   690  O O   . GLN   A 1 93  ? 6.326   6.477   13.180  1.00 10.71 ? 107 GLN   A O   1 
ATOM   691  C CB  A GLN   A 1 93  ? 7.500   7.783   16.031  0.65 13.41 ? 107 GLN   A CB  1 
ATOM   692  C CB  B GLN   A 1 93  ? 7.714   7.781   15.676  0.35 12.07 ? 107 GLN   A CB  1 
ATOM   693  C CG  A GLN   A 1 93  ? 7.881   7.495   17.484  0.65 14.37 ? 107 GLN   A CG  1 
ATOM   694  C CG  B GLN   A 1 93  ? 8.559   7.555   16.909  0.35 13.40 ? 107 GLN   A CG  1 
ATOM   695  C CD  A GLN   A 1 93  ? 8.923   8.446   18.025  0.65 14.97 ? 107 GLN   A CD  1 
ATOM   696  C CD  B GLN   A 1 93  ? 8.104   8.379   18.097  0.35 13.37 ? 107 GLN   A CD  1 
ATOM   697  O OE1 A GLN   A 1 93  ? 8.591   9.528   18.499  0.65 16.88 ? 107 GLN   A OE1 1 
ATOM   698  O OE1 B GLN   A 1 93  ? 8.631   8.235   19.199  0.35 14.28 ? 107 GLN   A OE1 1 
ATOM   699  N NE2 A GLN   A 1 93  ? 10.190  8.043   17.969  0.65 15.28 ? 107 GLN   A NE2 1 
ATOM   700  N NE2 B GLN   A 1 93  ? 7.122   9.249   17.881  0.35 12.92 ? 107 GLN   A NE2 1 
ATOM   701  N N   . TRP   A 1 94  ? 4.926   8.008   14.058  1.00 8.83  ? 108 TRP   A N   1 
ATOM   702  C CA  . TRP   A 1 94  ? 4.268   8.224   12.773  1.00 9.20  ? 108 TRP   A CA  1 
ATOM   703  C C   . TRP   A 1 94  ? 4.079   9.704   12.478  1.00 9.18  ? 108 TRP   A C   1 
ATOM   704  O O   . TRP   A 1 94  ? 4.035   10.542  13.383  1.00 9.86  ? 108 TRP   A O   1 
ATOM   705  C CB  . TRP   A 1 94  ? 2.937   7.456   12.664  1.00 9.91  ? 108 TRP   A CB  1 
ATOM   706  C CG  . TRP   A 1 94  ? 1.922   7.682   13.770  1.00 9.46  ? 108 TRP   A CG  1 
ATOM   707  C CD1 . TRP   A 1 94  ? 1.655   6.834   14.813  1.00 10.23 ? 108 TRP   A CD1 1 
ATOM   708  C CD2 . TRP   A 1 94  ? 1.028   8.800   13.922  1.00 9.54  ? 108 TRP   A CD2 1 
ATOM   709  N NE1 . TRP   A 1 94  ? 0.663   7.360   15.606  1.00 10.42 ? 108 TRP   A NE1 1 
ATOM   710  C CE2 . TRP   A 1 94  ? 0.253   8.563   15.083  1.00 9.87  ? 108 TRP   A CE2 1 
ATOM   711  C CE3 . TRP   A 1 94  ? 0.801   9.980   13.186  1.00 9.75  ? 108 TRP   A CE3 1 
ATOM   712  C CZ2 . TRP   A 1 94  ? -0.730  9.461   15.530  1.00 10.78 ? 108 TRP   A CZ2 1 
ATOM   713  C CZ3 . TRP   A 1 94  ? -0.180  10.871  13.625  1.00 9.89  ? 108 TRP   A CZ3 1 
ATOM   714  C CH2 . TRP   A 1 94  ? -0.922  10.610  14.799  1.00 9.99  ? 108 TRP   A CH2 1 
ATOM   715  N N   . LEU   A 1 95  ? 3.973   10.002  11.175  1.00 9.21  ? 109 LEU   A N   1 
ATOM   716  C CA  . LEU   A 1 95  ? 3.671   11.327  10.635  1.00 8.86  ? 109 LEU   A CA  1 
ATOM   717  C C   . LEU   A 1 95  ? 2.492   11.185  9.684   1.00 9.37  ? 109 LEU   A C   1 
ATOM   718  O O   . LEU   A 1 95  ? 2.532   10.368  8.756   1.00 11.31 ? 109 LEU   A O   1 
ATOM   719  C CB  . LEU   A 1 95  ? 4.860   11.889  9.842   1.00 9.91  ? 109 LEU   A CB  1 
ATOM   720  C CG  . LEU   A 1 95  ? 6.142   12.144  10.627  1.00 10.20 ? 109 LEU   A CG  1 
ATOM   721  C CD1 . LEU   A 1 95  ? 7.275   12.510  9.671   1.00 11.89 ? 109 LEU   A CD1 1 
ATOM   722  C CD2 . LEU   A 1 95  ? 5.927   13.251  11.653  1.00 12.64 ? 109 LEU   A CD2 1 
ATOM   723  N N   . LEU   A 1 96  ? 1.462   12.004  9.885   1.00 8.86  ? 110 LEU   A N   1 
ATOM   724  C CA  . LEU   A 1 96  ? 0.243   11.987  9.074   1.00 9.83  ? 110 LEU   A CA  1 
ATOM   725  C C   . LEU   A 1 96  ? 0.132   13.355  8.391   1.00 8.78  ? 110 LEU   A C   1 
ATOM   726  O O   . LEU   A 1 96  ? -0.201  14.353  9.039   1.00 9.42  ? 110 LEU   A O   1 
ATOM   727  C CB  . LEU   A 1 96  ? -0.968  11.666  9.965   1.00 10.01 ? 110 LEU   A CB  1 
ATOM   728  C CG  . LEU   A 1 96  ? -2.394  11.911  9.442   1.00 10.53 ? 110 LEU   A CG  1 
ATOM   729  C CD1 . LEU   A 1 96  ? -2.628  11.383  8.024   1.00 10.90 ? 110 LEU   A CD1 1 
ATOM   730  C CD2 . LEU   A 1 96  ? -3.405  11.303  10.418  1.00 11.78 ? 110 LEU   A CD2 1 
ATOM   731  N N   . THR   A 1 97  ? 0.429   13.414  7.084   1.00 8.97  ? 111 THR   A N   1 
ATOM   732  C CA  . THR   A 1 97  ? 0.402   14.665  6.334   1.00 9.10  ? 111 THR   A CA  1 
ATOM   733  C C   . THR   A 1 97  ? -0.843  14.720  5.462   1.00 9.77  ? 111 THR   A C   1 
ATOM   734  O O   . THR   A 1 97  ? -1.121  13.779  4.716   1.00 10.57 ? 111 THR   A O   1 
ATOM   735  C CB  . THR   A 1 97  ? 1.644   14.835  5.443   1.00 10.51 ? 111 THR   A CB  1 
ATOM   736  O OG1 . THR   A 1 97  ? 2.835   14.687  6.228   1.00 11.62 ? 111 THR   A OG1 1 
ATOM   737  C CG2 . THR   A 1 97  ? 1.640   16.211  4.773   1.00 11.95 ? 111 THR   A CG2 1 
ATOM   738  N N   . SER   A 1 98  ? -1.579  15.825  5.549   1.00 9.82  ? 112 SER   A N   1 
ATOM   739  C CA  . SER   A 1 98  ? -2.712  16.099  4.675   1.00 10.73 ? 112 SER   A CA  1 
ATOM   740  C C   . SER   A 1 98  ? -2.283  16.985  3.508   1.00 11.47 ? 112 SER   A C   1 
ATOM   741  O O   . SER   A 1 98  ? -1.405  17.838  3.639   1.00 13.40 ? 112 SER   A O   1 
ATOM   742  C CB  . SER   A 1 98  ? -3.805  16.834  5.452   1.00 11.91 ? 112 SER   A CB  1 
ATOM   743  O OG  . SER   A 1 98  ? -4.366  16.033  6.474   1.00 13.39 ? 112 SER   A OG  1 
ATOM   744  N N   . GLY   A 1 99  ? -2.923  16.787  2.353   1.00 11.94 ? 113 GLY   A N   1 
ATOM   745  C CA  . GLY   A 1 99  ? -2.780  17.749  1.270   1.00 13.15 ? 113 GLY   A CA  1 
ATOM   746  C C   . GLY   A 1 99  ? -3.491  19.043  1.634   1.00 13.11 ? 113 GLY   A C   1 
ATOM   747  O O   . GLY   A 1 99  ? -4.668  19.030  2.017   1.00 15.63 ? 113 GLY   A O   1 
ATOM   748  N N   . THR   A 1 100 ? -2.772  20.165  1.545   1.00 13.00 ? 114 THR   A N   1 
ATOM   749  C CA  . THR   A 1 100 ? -3.281  21.465  1.968   1.00 13.28 ? 114 THR   A CA  1 
ATOM   750  C C   . THR   A 1 100 ? -2.886  22.529  0.949   1.00 12.91 ? 114 THR   A C   1 
ATOM   751  O O   . THR   A 1 100 ? -2.034  22.314  0.081   1.00 13.77 ? 114 THR   A O   1 
ATOM   752  C CB  . THR   A 1 100 ? -2.712  21.889  3.340   1.00 14.10 ? 114 THR   A CB  1 
ATOM   753  O OG1 . THR   A 1 100 ? -1.315  22.182  3.216   1.00 14.33 ? 114 THR   A OG1 1 
ATOM   754  C CG2 . THR   A 1 100 ? -2.911  20.820  4.410   1.00 15.04 ? 114 THR   A CG2 1 
ATOM   755  N N   . THR   A 1 101 ? -3.501  23.703  1.081   1.00 13.75 ? 115 THR   A N   1 
ATOM   756  C CA  . THR   A 1 101 ? -2.968  24.890  0.429   1.00 14.68 ? 115 THR   A CA  1 
ATOM   757  C C   . THR   A 1 101 ? -1.669  25.320  1.110   1.00 14.46 ? 115 THR   A C   1 
ATOM   758  O O   . THR   A 1 101 ? -1.342  24.891  2.223   1.00 13.30 ? 115 THR   A O   1 
ATOM   759  C CB  . THR   A 1 101 ? -3.960  26.048  0.528   1.00 16.41 ? 115 THR   A CB  1 
ATOM   760  O OG1 . THR   A 1 101 ? -4.177  26.357  1.913   1.00 16.64 ? 115 THR   A OG1 1 
ATOM   761  C CG2 . THR   A 1 101 ? -5.280  25.689  -0.149  1.00 18.03 ? 115 THR   A CG2 1 
ATOM   762  N N   . GLU   A 1 102 ? -0.921  26.198  0.439   1.00 15.06 ? 116 GLU   A N   1 
ATOM   763  C CA  . GLU   A 1 102 ? 0.310   26.705  1.042   1.00 16.47 ? 116 GLU   A CA  1 
ATOM   764  C C   . GLU   A 1 102 ? 0.026   27.465  2.333   1.00 15.51 ? 116 GLU   A C   1 
ATOM   765  O O   . GLU   A 1 102 ? 0.758   27.317  3.319   1.00 15.73 ? 116 GLU   A O   1 
ATOM   766  C CB  . GLU   A 1 102 ? 1.096   27.563  0.048   1.00 18.32 ? 116 GLU   A CB  1 
ATOM   767  C CG  . GLU   A 1 102 ? 2.452   28.036  0.581   1.00 21.25 ? 116 GLU   A CG  1 
ATOM   768  C CD  . GLU   A 1 102 ? 3.369   26.888  1.002   0.52 22.35 ? 116 GLU   A CD  1 
ATOM   769  O OE1 . GLU   A 1 102 ? 3.394   25.845  0.312   0.53 23.32 ? 116 GLU   A OE1 1 
ATOM   770  O OE2 . GLU   A 1 102 ? 4.074   27.033  2.027   0.50 23.28 ? 116 GLU   A OE2 1 
ATOM   771  N N   . ALA   A 1 103 ? -1.050  28.257  2.358   1.00 16.12 ? 117 ALA   A N   1 
ATOM   772  C CA  . ALA   A 1 103 ? -1.386  29.015  3.562   1.00 17.16 ? 117 ALA   A CA  1 
ATOM   773  C C   . ALA   A 1 103 ? -1.661  28.116  4.762   1.00 15.45 ? 117 ALA   A C   1 
ATOM   774  O O   . ALA   A 1 103 ? -1.458  28.535  5.911   1.00 17.41 ? 117 ALA   A O   1 
ATOM   775  C CB  . ALA   A 1 103 ? -2.587  29.924  3.298   1.00 18.80 ? 117 ALA   A CB  1 
ATOM   776  N N   . ASN   A 1 104 ? -2.142  26.895  4.524   1.00 14.42 ? 118 ASN   A N   1 
ATOM   777  C CA  . ASN   A 1 104 ? -2.476  25.960  5.591   1.00 14.50 ? 118 ASN   A CA  1 
ATOM   778  C C   . ASN   A 1 104 ? -1.407  24.900  5.812   1.00 13.90 ? 118 ASN   A C   1 
ATOM   779  O O   . ASN   A 1 104 ? -1.594  24.009  6.651   1.00 14.21 ? 118 ASN   A O   1 
ATOM   780  C CB  . ASN   A 1 104 ? -3.822  25.291  5.301   1.00 16.41 ? 118 ASN   A CB  1 
ATOM   781  C CG  . ASN   A 1 104 ? -4.983  26.248  5.439   1.00 18.40 ? 118 ASN   A CG  1 
ATOM   782  O OD1 . ASN   A 1 104 ? -4.933  27.186  6.237   1.00 19.94 ? 118 ASN   A OD1 1 
ATOM   783  N ND2 . ASN   A 1 104 ? -6.041  26.018  4.663   1.00 19.29 ? 118 ASN   A ND2 1 
ATOM   784  N N   . ALA   A 1 105 ? -0.279  24.988  5.103   1.00 13.44 ? 119 ALA   A N   1 
ATOM   785  C CA  . ALA   A 1 105 ? 0.710   23.915  5.168   1.00 13.31 ? 119 ALA   A CA  1 
ATOM   786  C C   . ALA   A 1 105 ? 1.359   23.820  6.542   1.00 12.00 ? 119 ALA   A C   1 
ATOM   787  O O   . ALA   A 1 105 ? 1.807   22.737  6.937   1.00 12.55 ? 119 ALA   A O   1 
ATOM   788  C CB  . ALA   A 1 105 ? 1.768   24.106  4.087   1.00 13.30 ? 119 ALA   A CB  1 
ATOM   789  N N   . TRP   A 1 106 ? 1.416   24.927  7.284   1.00 13.26 ? 120 TRP   A N   1 
ATOM   790  C CA  . TRP   A 1 106 ? 2.056   24.889  8.595   1.00 14.36 ? 120 TRP   A CA  1 
ATOM   791  C C   . TRP   A 1 106 ? 1.390   23.880  9.521   1.00 14.12 ? 120 TRP   A C   1 
ATOM   792  O O   . TRP   A 1 106 ? 2.050   23.327  10.411  1.00 15.29 ? 120 TRP   A O   1 
ATOM   793  C CB  . TRP   A 1 106 ? 2.065   26.280  9.234   1.00 16.58 ? 120 TRP   A CB  1 
ATOM   794  C CG  . TRP   A 1 106 ? 0.706   26.777  9.635   1.00 17.60 ? 120 TRP   A CG  1 
ATOM   795  C CD1 . TRP   A 1 106 ? -0.176  27.456  8.848   1.00 18.80 ? 120 TRP   A CD1 1 
ATOM   796  C CD2 . TRP   A 1 106 ? 0.074   26.640  10.918  1.00 19.19 ? 120 TRP   A CD2 1 
ATOM   797  N NE1 . TRP   A 1 106 ? -1.316  27.744  9.556   1.00 20.82 ? 120 TRP   A NE1 1 
ATOM   798  C CE2 . TRP   A 1 106 ? -1.190  27.255  10.827  1.00 21.08 ? 120 TRP   A CE2 1 
ATOM   799  C CE3 . TRP   A 1 106 ? 0.443   26.039  12.125  1.00 20.89 ? 120 TRP   A CE3 1 
ATOM   800  C CZ2 . TRP   A 1 106 ? -2.078  27.308  11.905  1.00 23.80 ? 120 TRP   A CZ2 1 
ATOM   801  C CZ3 . TRP   A 1 106 ? -0.441  26.099  13.199  1.00 23.39 ? 120 TRP   A CZ3 1 
ATOM   802  C CH2 . TRP   A 1 106 ? -1.685  26.725  13.077  1.00 24.46 ? 120 TRP   A CH2 1 
ATOM   803  N N   . LYS   A 1 107 ? 0.092   23.628  9.338   1.00 13.79 ? 121 LYS   A N   1 
ATOM   804  C CA  . LYS   A 1 107 ? -0.661  22.695  10.169  1.00 14.32 ? 121 LYS   A CA  1 
ATOM   805  C C   . LYS   A 1 107 ? -1.037  21.417  9.417   1.00 12.47 ? 121 LYS   A C   1 
ATOM   806  O O   . LYS   A 1 107 ? -2.037  20.775  9.738   1.00 13.01 ? 121 LYS   A O   1 
ATOM   807  C CB  . LYS   A 1 107 ? -1.890  23.373  10.781  1.00 16.28 ? 121 LYS   A CB  1 
ATOM   808  C CG  . LYS   A 1 107 ? -2.803  24.037  9.762   1.00 17.46 ? 121 LYS   A CG  1 
ATOM   809  C CD  . LYS   A 1 107 ? -4.030  24.626  10.444  1.00 20.41 ? 121 LYS   A CD  1 
ATOM   810  C CE  . LYS   A 1 107 ? -4.929  25.311  9.434   1.00 22.37 ? 121 LYS   A CE  1 
ATOM   811  N NZ  . LYS   A 1 107 ? -6.096  25.958  10.093  1.00 24.92 ? 121 LYS   A NZ  1 
ATOM   812  N N   . SER   A 1 108 ? -0.230  21.030  8.425   1.00 11.10 ? 122 SER   A N   1 
ATOM   813  C CA  . SER   A 1 108 ? -0.515  19.870  7.593   1.00 10.79 ? 122 SER   A CA  1 
ATOM   814  C C   . SER   A 1 108 ? -0.150  18.527  8.220   1.00 9.86  ? 122 SER   A C   1 
ATOM   815  O O   . SER   A 1 108 ? -0.587  17.500  7.692   1.00 10.86 ? 122 SER   A O   1 
ATOM   816  C CB  . SER   A 1 108 ? 0.273   19.980  6.287   1.00 12.34 ? 122 SER   A CB  1 
ATOM   817  O OG  . SER   A 1 108 ? 1.663   19.898  6.573   1.00 13.63 ? 122 SER   A OG  1 
ATOM   818  N N   . THR   A 1 109 ? 0.649   18.479  9.289   1.00 9.91  ? 123 THR   A N   1 
ATOM   819  C CA  . THR   A 1 109 ? 1.271   17.222  9.712   1.00 9.02  ? 123 THR   A CA  1 
ATOM   820  C C   . THR   A 1 109 ? 1.035   16.945  11.197  1.00 9.36  ? 123 THR   A C   1 
ATOM   821  O O   . THR   A 1 109 ? 1.512   17.692  12.062  1.00 10.56 ? 123 THR   A O   1 
ATOM   822  C CB  . THR   A 1 109 ? 2.777   17.229  9.418   1.00 9.85  ? 123 THR   A CB  1 
ATOM   823  O OG1 . THR   A 1 109 ? 2.996   17.612  8.053   1.00 11.20 ? 123 THR   A OG1 1 
ATOM   824  C CG2 . THR   A 1 109 ? 3.369   15.839  9.624   1.00 10.63 ? 123 THR   A CG2 1 
ATOM   825  N N   . LEU   A 1 110 ? 0.340   15.847  11.488  1.00 9.25  ? 124 LEU   A N   1 
ATOM   826  C CA  . LEU   A 1 110 ? 0.193   15.327  12.842  1.00 9.69  ? 124 LEU   A CA  1 
ATOM   827  C C   . LEU   A 1 110 ? 1.307   14.320  13.131  1.00 9.23  ? 124 LEU   A C   1 
ATOM   828  O O   . LEU   A 1 110 ? 1.822   13.660  12.219  1.00 10.40 ? 124 LEU   A O   1 
ATOM   829  C CB  . LEU   A 1 110 ? -1.170  14.646  12.982  1.00 10.70 ? 124 LEU   A CB  1 
ATOM   830  C CG  . LEU   A 1 110 ? -2.401  15.555  12.931  1.00 11.40 ? 124 LEU   A CG  1 
ATOM   831  C CD1 . LEU   A 1 110 ? -3.654  14.718  12.713  1.00 12.51 ? 124 LEU   A CD1 1 
ATOM   832  C CD2 . LEU   A 1 110 ? -2.525  16.389  14.210  1.00 12.75 ? 124 LEU   A CD2 1 
ATOM   833  N N   . VAL   A 1 111 ? 1.663   14.186  14.414  1.00 9.99  ? 125 VAL   A N   1 
ATOM   834  C CA  . VAL   A 1 111 ? 2.694   13.246  14.862  1.00 10.26 ? 125 VAL   A CA  1 
ATOM   835  C C   . VAL   A 1 111 ? 2.186   12.438  16.060  1.00 9.63  ? 125 VAL   A C   1 
ATOM   836  O O   . VAL   A 1 111 ? 1.470   12.958  16.927  1.00 10.02 ? 125 VAL   A O   1 
ATOM   837  C CB  . VAL   A 1 111 ? 4.026   13.976  15.193  1.00 10.63 ? 125 VAL   A CB  1 
ATOM   838  C CG1 . VAL   A 1 111 ? 3.863   14.978  16.334  1.00 11.29 ? 125 VAL   A CG1 1 
ATOM   839  C CG2 . VAL   A 1 111 ? 5.153   12.991  15.494  1.00 11.29 ? 125 VAL   A CG2 1 
ATOM   840  N N   . GLY   A 1 112 ? 2.578   11.168  16.128  1.00 9.97  ? 126 GLY   A N   1 
ATOM   841  C CA  . GLY   A 1 112 ? 2.234   10.352  17.276  1.00 10.61 ? 126 GLY   A CA  1 
ATOM   842  C C   . GLY   A 1 112 ? 3.084   9.103   17.318  1.00 10.04 ? 126 GLY   A C   1 
ATOM   843  O O   . GLY   A 1 112 ? 4.093   8.984   16.614  1.00 10.57 ? 126 GLY   A O   1 
ATOM   844  N N   . HIS   A 1 113 ? 2.671   8.167   18.173  1.00 10.83 ? 127 HIS   A N   1 
ATOM   845  C CA  . HIS   A 1 113 ? 3.401   6.915   18.356  1.00 11.40 ? 127 HIS   A CA  1 
ATOM   846  C C   . HIS   A 1 113 ? 2.411   5.778   18.543  1.00 11.27 ? 127 HIS   A C   1 
ATOM   847  O O   . HIS   A 1 113 ? 1.454   5.904   19.319  1.00 12.90 ? 127 HIS   A O   1 
ATOM   848  C CB  . HIS   A 1 113 ? 4.380   6.985   19.538  1.00 11.92 ? 127 HIS   A CB  1 
ATOM   849  C CG  . HIS   A 1 113 ? 3.783   7.552   20.785  1.00 13.73 ? 127 HIS   A CG  1 
ATOM   850  N ND1 . HIS   A 1 113 ? 3.361   6.765   21.834  1.00 16.10 ? 127 HIS   A ND1 1 
ATOM   851  C CD2 . HIS   A 1 113 ? 3.549   8.832   21.155  1.00 14.55 ? 127 HIS   A CD2 1 
ATOM   852  C CE1 . HIS   A 1 113 ? 2.884   7.538   22.796  1.00 17.05 ? 127 HIS   A CE1 1 
ATOM   853  N NE2 . HIS   A 1 113 ? 2.977   8.794   22.404  1.00 17.29 ? 127 HIS   A NE2 1 
ATOM   854  N N   . ASP   A 1 114 ? 2.643   4.673   17.831  1.00 11.18 ? 128 ASP   A N   1 
ATOM   855  C CA  . ASP   A 1 114 ? 1.798   3.482   17.885  1.00 11.45 ? 128 ASP   A CA  1 
ATOM   856  C C   . ASP   A 1 114 ? 2.647   2.272   18.242  1.00 11.88 ? 128 ASP   A C   1 
ATOM   857  O O   . ASP   A 1 114 ? 3.742   2.096   17.702  1.00 12.52 ? 128 ASP   A O   1 
ATOM   858  C CB  . ASP   A 1 114 ? 1.168   3.154   16.514  1.00 11.32 ? 128 ASP   A CB  1 
ATOM   859  C CG  . ASP   A 1 114 ? -0.011  4.040   16.155  1.00 12.29 ? 128 ASP   A CG  1 
ATOM   860  O OD1 . ASP   A 1 114 ? -0.422  4.902   16.964  1.00 12.66 ? 128 ASP   A OD1 1 
ATOM   861  O OD2 . ASP   A 1 114 ? -0.531  3.861   15.031  1.00 12.01 ? 128 ASP   A OD2 1 
ATOM   862  N N   . THR   A 1 115 ? 2.133   1.420   19.128  1.00 13.29 ? 129 THR   A N   1 
ATOM   863  C CA  A THR   A 1 115 ? 2.778   0.151   19.434  0.92 13.74 ? 129 THR   A CA  1 
ATOM   864  C CA  B THR   A 1 115 ? 2.764   0.147   19.464  0.08 14.03 ? 129 THR   A CA  1 
ATOM   865  C C   . THR   A 1 115 ? 1.857   -0.991  19.018  1.00 14.57 ? 129 THR   A C   1 
ATOM   866  O O   . THR   A 1 115 ? 0.653   -0.964  19.291  1.00 15.39 ? 129 THR   A O   1 
ATOM   867  C CB  A THR   A 1 115 ? 3.247   0.060   20.901  0.92 16.04 ? 129 THR   A CB  1 
ATOM   868  C CB  B THR   A 1 115 ? 3.000   0.044   20.971  0.08 14.11 ? 129 THR   A CB  1 
ATOM   869  O OG1 A THR   A 1 115 ? 3.997   -1.145  21.085  0.92 16.70 ? 129 THR   A OG1 1 
ATOM   870  O OG1 B THR   A 1 115 ? 1.804   0.410   21.672  0.08 14.55 ? 129 THR   A OG1 1 
ATOM   871  C CG2 A THR   A 1 115 ? 2.077   0.092   21.876  0.92 17.80 ? 129 THR   A CG2 1 
ATOM   872  C CG2 B THR   A 1 115 ? 4.123   0.958   21.386  0.08 13.74 ? 129 THR   A CG2 1 
ATOM   873  N N   . PHE   A 1 116 ? 2.429   -1.980  18.332  1.00 14.83 ? 130 PHE   A N   1 
ATOM   874  C CA  . PHE   A 1 116 ? 1.669   -3.083  17.760  1.00 15.52 ? 130 PHE   A CA  1 
ATOM   875  C C   . PHE   A 1 116 ? 2.041   -4.393  18.439  1.00 17.14 ? 130 PHE   A C   1 
ATOM   876  O O   . PHE   A 1 116 ? 3.217   -4.652  18.713  1.00 17.76 ? 130 PHE   A O   1 
ATOM   877  C CB  . PHE   A 1 116 ? 1.970   -3.209  16.261  1.00 15.29 ? 130 PHE   A CB  1 
ATOM   878  C CG  . PHE   A 1 116 ? 1.513   -2.025  15.441  1.00 14.29 ? 130 PHE   A CG  1 
ATOM   879  C CD1 . PHE   A 1 116 ? 2.316   -0.897  15.310  1.00 13.89 ? 130 PHE   A CD1 1 
ATOM   880  C CD2 . PHE   A 1 116 ? 0.282   -2.049  14.795  1.00 13.96 ? 130 PHE   A CD2 1 
ATOM   881  C CE1 . PHE   A 1 116 ? 1.890   0.199   14.554  1.00 13.40 ? 130 PHE   A CE1 1 
ATOM   882  C CE2 . PHE   A 1 116 ? -0.147  -0.963  14.039  1.00 13.22 ? 130 PHE   A CE2 1 
ATOM   883  C CZ  . PHE   A 1 116 ? 0.654   0.160   13.912  1.00 13.12 ? 130 PHE   A CZ  1 
ATOM   884  N N   . THR   A 1 117 ? 1.039   -5.230  18.687  1.00 17.03 ? 131 THR   A N   1 
ATOM   885  C CA  . THR   A 1 117 ? 1.270   -6.575  19.194  1.00 18.66 ? 131 THR   A CA  1 
ATOM   886  C C   . THR   A 1 117 ? 0.455   -7.550  18.366  1.00 19.39 ? 131 THR   A C   1 
ATOM   887  O O   . THR   A 1 117 ? -0.559  -7.179  17.761  1.00 17.44 ? 131 THR   A O   1 
ATOM   888  C CB  . THR   A 1 117 ? 0.902   -6.719  20.684  1.00 21.35 ? 131 THR   A CB  1 
ATOM   889  O OG1 . THR   A 1 117 ? -0.487  -6.420  20.872  1.00 24.84 ? 131 THR   A OG1 1 
ATOM   890  C CG2 . THR   A 1 117 ? 1.736   -5.773  21.523  1.00 22.07 ? 131 THR   A CG2 1 
ATOM   891  N N   . LYS   A 1 118 ? 0.929   -8.800  18.323  1.00 22.75 ? 132 LYS   A N   1 
ATOM   892  C CA  . LYS   A 1 118 ? 0.176   -9.847  17.642  1.00 23.04 ? 132 LYS   A CA  1 
ATOM   893  C C   . LYS   A 1 118 ? -1.010  -10.308 18.469  1.00 23.92 ? 132 LYS   A C   1 
ATOM   894  O O   . LYS   A 1 118 ? -1.899  -10.980 17.940  1.00 25.81 ? 132 LYS   A O   1 
ATOM   895  C CB  . LYS   A 1 118 ? 1.076   -11.034 17.268  1.00 22.60 ? 132 LYS   A CB  1 
ATOM   896  C CG  . LYS   A 1 118 ? 2.032   -10.744 16.107  1.00 23.33 ? 132 LYS   A CG  1 
ATOM   897  C CD  . LYS   A 1 118 ? 2.695   -12.019 15.591  1.00 24.58 ? 132 LYS   A CD  1 
ATOM   898  C CE  . LYS   A 1 118 ? 3.644   -11.727 14.437  1.00 26.41 ? 132 LYS   A CE  1 
ATOM   899  N NZ  . LYS   A 1 118 ? 4.375   -12.939 13.980  1.00 27.27 ? 132 LYS   A NZ  1 
ATOM   900  N N   . VAL   A 1 119 ? -1.036  -9.973  19.755  1.00 24.27 ? 133 VAL   A N   1 
ATOM   901  C CA  . VAL   A 1 119 ? -2.202  -10.166 20.602  1.00 23.82 ? 133 VAL   A CA  1 
ATOM   902  C C   . VAL   A 1 119 ? -2.918  -8.830  20.698  1.00 22.29 ? 133 VAL   A C   1 
ATOM   903  O O   . VAL   A 1 119 ? -2.293  -7.804  20.992  1.00 24.17 ? 133 VAL   A O   1 
ATOM   904  C CB  . VAL   A 1 119 ? -1.797  -10.677 21.995  1.00 24.82 ? 133 VAL   A CB  1 
ATOM   905  C CG1 . VAL   A 1 119 ? -3.012  -10.759 22.907  1.00 24.37 ? 133 VAL   A CG1 1 
ATOM   906  C CG2 . VAL   A 1 119 ? -1.111  -12.034 21.884  1.00 26.36 ? 133 VAL   A CG2 1 
ATOM   907  N N   . LYS   A 1 120 ? -4.213  -8.831  20.451  1.00 20.18 ? 134 LYS   A N   1 
ATOM   908  C CA  . LYS   A 1 120 ? -4.971  -7.588  20.485  1.00 22.45 ? 134 LYS   A CA  1 
ATOM   909  C C   . LYS   A 1 120 ? -5.115  -7.114  21.928  1.00 25.60 ? 134 LYS   A C   1 
ATOM   910  O O   . LYS   A 1 120 ? -5.574  -7.886  22.781  1.00 26.41 ? 134 LYS   A O   1 
ATOM   911  C CB  . LYS   A 1 120 ? -6.342  -7.842  19.894  1.00 20.58 ? 134 LYS   A CB  1 
ATOM   912  C CG  . LYS   A 1 120 ? -7.170  -6.595  19.682  1.00 21.96 ? 134 LYS   A CG  1 
ATOM   913  C CD  . LYS   A 1 120 ? -8.321  -6.897  18.744  1.00 24.12 ? 134 LYS   A CD  1 
ATOM   914  C CE  . LYS   A 1 120 ? -9.036  -5.632  18.308  1.00 26.66 ? 134 LYS   A CE  1 
ATOM   915  N NZ  . LYS   A 1 120 ? -9.959  -5.906  17.170  1.00 28.60 ? 134 LYS   A NZ  1 
ATOM   916  N N   . PRO   A 1 121 ? -4.744  -5.862  22.254  1.00 28.66 ? 135 PRO   A N   1 
ATOM   917  C CA  . PRO   A 1 121 ? -4.877  -5.389  23.638  1.00 30.25 ? 135 PRO   A CA  1 
ATOM   918  C C   . PRO   A 1 121 ? -6.325  -5.090  24.017  1.00 31.81 ? 135 PRO   A C   1 
ATOM   919  O O   . PRO   A 1 121 ? -7.188  -4.919  23.153  1.00 31.90 ? 135 PRO   A O   1 
ATOM   920  C CB  . PRO   A 1 121 ? -4.046  -4.102  23.648  1.00 30.29 ? 135 PRO   A CB  1 
ATOM   921  C CG  . PRO   A 1 121 ? -4.084  -3.621  22.242  1.00 30.36 ? 135 PRO   A CG  1 
ATOM   922  C CD  . PRO   A 1 121 ? -4.123  -4.852  21.375  1.00 29.15 ? 135 PRO   A CD  1 
ATOM   923  O OXT . PRO   A 1 121 ? -6.665  -5.020  25.205  1.00 33.49 ? 135 PRO   A OXT 1 
ATOM   924  N N   . ALA   B 1 1   ? -5.244  22.815  39.612  1.00 28.25 ? 15  ALA   B N   1 
ATOM   925  C CA  . ALA   B 1 1   ? -4.512  22.517  38.384  1.00 26.51 ? 15  ALA   B CA  1 
ATOM   926  C C   . ALA   B 1 1   ? -3.961  21.088  38.363  1.00 23.24 ? 15  ALA   B C   1 
ATOM   927  O O   . ALA   B 1 1   ? -3.915  20.461  37.304  1.00 23.97 ? 15  ALA   B O   1 
ATOM   928  C CB  . ALA   B 1 1   ? -3.390  23.532  38.171  1.00 27.84 ? 15  ALA   B CB  1 
ATOM   929  N N   . GLY   B 1 2   ? -3.538  20.583  39.528  1.00 20.28 ? 16  GLY   B N   1 
ATOM   930  C CA  . GLY   B 1 2   ? -3.068  19.215  39.671  1.00 17.34 ? 16  GLY   B CA  1 
ATOM   931  C C   . GLY   B 1 2   ? -1.674  18.940  39.150  1.00 15.84 ? 16  GLY   B C   1 
ATOM   932  O O   . GLY   B 1 2   ? -1.216  17.792  39.226  1.00 16.43 ? 16  GLY   B O   1 
ATOM   933  N N   . ILE   B 1 3   ? -0.978  19.949  38.640  1.00 14.95 ? 17  ILE   B N   1 
ATOM   934  C CA  . ILE   B 1 3   ? 0.323   19.742  38.005  1.00 12.90 ? 17  ILE   B CA  1 
ATOM   935  C C   . ILE   B 1 3   ? 1.470   19.830  39.008  1.00 13.45 ? 17  ILE   B C   1 
ATOM   936  O O   . ILE   B 1 3   ? 2.424   19.053  38.935  1.00 13.03 ? 17  ILE   B O   1 
ATOM   937  C CB  . ILE   B 1 3   ? 0.487   20.755  36.854  1.00 13.24 ? 17  ILE   B CB  1 
ATOM   938  C CG1 . ILE   B 1 3   ? -0.479  20.429  35.704  1.00 14.60 ? 17  ILE   B CG1 1 
ATOM   939  C CG2 . ILE   B 1 3   ? 1.913   20.753  36.325  1.00 13.40 ? 17  ILE   B CG2 1 
ATOM   940  C CD1 . ILE   B 1 3   ? -0.611  21.542  34.677  1.00 15.93 ? 17  ILE   B CD1 1 
ATOM   941  N N   . THR   B 1 4   ? 1.412   20.760  39.959  1.00 13.12 ? 18  THR   B N   1 
ATOM   942  C CA  . THR   B 1 4   ? 2.514   20.928  40.901  1.00 13.06 ? 18  THR   B CA  1 
ATOM   943  C C   . THR   B 1 4   ? 2.797   19.620  41.634  1.00 12.75 ? 18  THR   B C   1 
ATOM   944  O O   . THR   B 1 4   ? 1.875   18.966  42.132  1.00 14.11 ? 18  THR   B O   1 
ATOM   945  C CB  . THR   B 1 4   ? 2.158   22.023  41.912  1.00 13.65 ? 18  THR   B CB  1 
ATOM   946  O OG1 . THR   B 1 4   ? 2.127   23.291  41.248  1.00 13.80 ? 18  THR   B OG1 1 
ATOM   947  C CG2 . THR   B 1 4   ? 3.183   22.070  43.046  1.00 15.17 ? 18  THR   B CG2 1 
ATOM   948  N N   . GLY   B 1 5   ? 4.075   19.240  41.701  1.00 12.53 ? 19  GLY   B N   1 
ATOM   949  C CA  . GLY   B 1 5   ? 4.484   18.081  42.460  1.00 13.35 ? 19  GLY   B CA  1 
ATOM   950  C C   . GLY   B 1 5   ? 5.565   17.301  41.741  1.00 13.05 ? 19  GLY   B C   1 
ATOM   951  O O   . GLY   B 1 5   ? 6.190   17.774  40.788  1.00 13.20 ? 19  GLY   B O   1 
ATOM   952  N N   . THR   B 1 6   ? 5.762   16.070  42.201  1.00 13.66 ? 20  THR   B N   1 
ATOM   953  C CA  . THR   B 1 6   ? 6.809   15.187  41.702  1.00 14.00 ? 20  THR   B CA  1 
ATOM   954  C C   . THR   B 1 6   ? 6.205   14.159  40.753  1.00 13.63 ? 20  THR   B C   1 
ATOM   955  O O   . THR   B 1 6   ? 5.196   13.522  41.071  1.00 15.59 ? 20  THR   B O   1 
ATOM   956  C CB  . THR   B 1 6   ? 7.496   14.496  42.884  1.00 15.36 ? 20  THR   B CB  1 
ATOM   957  O OG1 . THR   B 1 6   ? 8.064   15.492  43.743  1.00 18.44 ? 20  THR   B OG1 1 
ATOM   958  C CG2 . THR   B 1 6   ? 8.592   13.543  42.415  1.00 15.59 ? 20  THR   B CG2 1 
ATOM   959  N N   . TRP   B 1 7   ? 6.833   13.994  39.590  1.00 12.40 ? 21  TRP   B N   1 
ATOM   960  C CA  . TRP   B 1 7   ? 6.356   13.106  38.545  1.00 13.01 ? 21  TRP   B CA  1 
ATOM   961  C C   . TRP   B 1 7   ? 7.491   12.183  38.133  1.00 13.72 ? 21  TRP   B C   1 
ATOM   962  O O   . TRP   B 1 7   ? 8.672   12.538  38.230  1.00 14.07 ? 21  TRP   B O   1 
ATOM   963  C CB  . TRP   B 1 7   ? 5.872   13.907  37.333  1.00 12.69 ? 21  TRP   B CB  1 
ATOM   964  C CG  . TRP   B 1 7   ? 4.632   14.727  37.585  1.00 12.70 ? 21  TRP   B CG  1 
ATOM   965  C CD1 . TRP   B 1 7   ? 4.571   15.998  38.084  1.00 12.72 ? 21  TRP   B CD1 1 
ATOM   966  C CD2 . TRP   B 1 7   ? 3.277   14.332  37.327  1.00 12.04 ? 21  TRP   B CD2 1 
ATOM   967  N NE1 . TRP   B 1 7   ? 3.259   16.416  38.163  1.00 12.75 ? 21  TRP   B NE1 1 
ATOM   968  C CE2 . TRP   B 1 7   ? 2.447   15.413  37.698  1.00 12.52 ? 21  TRP   B CE2 1 
ATOM   969  C CE3 . TRP   B 1 7   ? 2.687   13.170  36.810  1.00 13.00 ? 21  TRP   B CE3 1 
ATOM   970  C CZ2 . TRP   B 1 7   ? 1.058   15.367  37.564  1.00 13.03 ? 21  TRP   B CZ2 1 
ATOM   971  C CZ3 . TRP   B 1 7   ? 1.303   13.123  36.683  1.00 13.80 ? 21  TRP   B CZ3 1 
ATOM   972  C CH2 . TRP   B 1 7   ? 0.507   14.216  37.056  1.00 13.70 ? 21  TRP   B CH2 1 
ATOM   973  N N   . TYR   B 1 8   ? 7.116   11.010  37.626  1.00 14.57 ? 22  TYR   B N   1 
ATOM   974  C CA  A TYR   B 1 8   ? 8.048   9.950   37.281  0.60 15.62 ? 22  TYR   B CA  1 
ATOM   975  C CA  B TYR   B 1 8   ? 8.077   9.984   37.246  0.40 16.16 ? 22  TYR   B CA  1 
ATOM   976  C C   . TYR   B 1 8   ? 7.735   9.476   35.862  1.00 16.69 ? 22  TYR   B C   1 
ATOM   977  O O   . TYR   B 1 8   ? 6.582   9.149   35.572  1.00 16.75 ? 22  TYR   B O   1 
ATOM   978  C CB  A TYR   B 1 8   ? 7.856   8.807   38.301  0.60 16.04 ? 22  TYR   B CB  1 
ATOM   979  C CB  B TYR   B 1 8   ? 8.086   8.805   38.219  0.40 17.41 ? 22  TYR   B CB  1 
ATOM   980  C CG  A TYR   B 1 8   ? 7.904   9.252   39.767  0.60 14.36 ? 22  TYR   B CG  1 
ATOM   981  C CG  B TYR   B 1 8   ? 8.563   9.178   39.588  0.40 17.06 ? 22  TYR   B CG  1 
ATOM   982  C CD1 A TYR   B 1 8   ? 9.111   9.312   40.444  0.60 15.02 ? 22  TYR   B CD1 1 
ATOM   983  C CD1 B TYR   B 1 8   ? 9.918   9.347   39.855  0.40 16.92 ? 22  TYR   B CD1 1 
ATOM   984  C CD2 A TYR   B 1 8   ? 6.745   9.608   40.464  0.60 13.58 ? 22  TYR   B CD2 1 
ATOM   985  C CD2 B TYR   B 1 8   ? 7.658   9.374   40.612  0.40 17.28 ? 22  TYR   B CD2 1 
ATOM   986  C CE1 A TYR   B 1 8   ? 9.183   9.709   41.763  0.60 14.57 ? 22  TYR   B CE1 1 
ATOM   987  C CE1 B TYR   B 1 8   ? 10.349  9.692   41.116  0.40 17.50 ? 22  TYR   B CE1 1 
ATOM   988  C CE2 A TYR   B 1 8   ? 6.807   10.012  41.801  0.60 13.94 ? 22  TYR   B CE2 1 
ATOM   989  C CE2 B TYR   B 1 8   ? 8.074   9.718   41.865  0.40 17.30 ? 22  TYR   B CE2 1 
ATOM   990  C CZ  A TYR   B 1 8   ? 8.035   10.060  42.442  0.60 14.78 ? 22  TYR   B CZ  1 
ATOM   991  C CZ  B TYR   B 1 8   ? 9.418   9.878   42.114  0.40 17.27 ? 22  TYR   B CZ  1 
ATOM   992  O OH  A TYR   B 1 8   ? 8.142   10.453  43.762  0.60 14.94 ? 22  TYR   B OH  1 
ATOM   993  O OH  B TYR   B 1 8   ? 9.821   10.225  43.374  0.40 16.66 ? 22  TYR   B OH  1 
ATOM   994  N N   . ASN   B 1 9   ? 8.743   9.433   34.989  1.00 17.07 ? 23  ASN   B N   1 
ATOM   995  C CA  . ASN   B 1 9   ? 8.520   8.900   33.651  1.00 18.84 ? 23  ASN   B CA  1 
ATOM   996  C C   . ASN   B 1 9   ? 8.711   7.386   33.642  1.00 18.85 ? 23  ASN   B C   1 
ATOM   997  O O   . ASN   B 1 9   ? 8.947   6.751   34.675  1.00 20.40 ? 23  ASN   B O   1 
ATOM   998  C CB  . ASN   B 1 9   ? 9.355   9.628   32.590  1.00 19.98 ? 23  ASN   B CB  1 
ATOM   999  C CG  . ASN   B 1 9   ? 10.768  9.067   32.436  1.00 21.08 ? 23  ASN   B CG  1 
ATOM   1000 O OD1 . ASN   B 1 9   ? 11.276  8.347   33.294  1.00 20.99 ? 23  ASN   B OD1 1 
ATOM   1001 N ND2 . ASN   B 1 9   ? 11.418  9.431   31.337  1.00 22.03 ? 23  ASN   B ND2 1 
ATOM   1002 N N   . GLN   B 1 10  ? 8.640   6.806   32.445  1.00 18.71 ? 24  GLN   B N   1 
ATOM   1003 C CA  . GLN   B 1 10  ? 8.684   5.366   32.270  1.00 20.60 ? 24  GLN   B CA  1 
ATOM   1004 C C   . GLN   B 1 10  ? 10.094  4.788   32.370  1.00 21.71 ? 24  GLN   B C   1 
ATOM   1005 O O   . GLN   B 1 10  ? 10.238  3.564   32.437  1.00 23.85 ? 24  GLN   B O   1 
ATOM   1006 C CB  . GLN   B 1 10  ? 8.028   4.998   30.932  1.00 21.28 ? 24  GLN   B CB  1 
ATOM   1007 C CG  . GLN   B 1 10  ? 8.857   5.290   29.659  1.00 21.03 ? 24  GLN   B CG  1 
ATOM   1008 C CD  . GLN   B 1 10  ? 8.953   6.770   29.258  1.00 20.06 ? 24  GLN   B CD  1 
ATOM   1009 O OE1 . GLN   B 1 10  ? 8.245   7.641   29.780  1.00 16.76 ? 24  GLN   B OE1 1 
ATOM   1010 N NE2 . GLN   B 1 10  ? 9.834   7.049   28.295  1.00 22.20 ? 24  GLN   B NE2 1 
ATOM   1011 N N   . LEU   B 1 11  ? 11.131  5.630   32.408  1.00 22.18 ? 25  LEU   B N   1 
ATOM   1012 C CA  . LEU   B 1 11  ? 12.517  5.170   32.381  1.00 22.43 ? 25  LEU   B CA  1 
ATOM   1013 C C   . LEU   B 1 11  ? 13.311  5.590   33.613  1.00 23.73 ? 25  LEU   B C   1 
ATOM   1014 O O   . LEU   B 1 11  ? 14.544  5.532   33.599  1.00 27.08 ? 25  LEU   B O   1 
ATOM   1015 C CB  . LEU   B 1 11  ? 13.222  5.649   31.112  1.00 23.70 ? 25  LEU   B CB  1 
ATOM   1016 C CG  . LEU   B 1 11  ? 12.631  5.171   29.787  1.00 26.19 ? 25  LEU   B CG  1 
ATOM   1017 C CD1 . LEU   B 1 11  ? 13.431  5.725   28.614  1.00 27.75 ? 25  LEU   B CD1 1 
ATOM   1018 C CD2 . LEU   B 1 11  ? 12.571  3.651   29.726  1.00 26.68 ? 25  LEU   B CD2 1 
ATOM   1019 N N   . GLY   B 1 12  ? 12.643  6.026   34.673  1.00 21.75 ? 26  GLY   B N   1 
ATOM   1020 C CA  . GLY   B 1 12  ? 13.339  6.313   35.907  1.00 21.74 ? 26  GLY   B CA  1 
ATOM   1021 C C   . GLY   B 1 12  ? 13.734  7.757   36.124  1.00 21.26 ? 26  GLY   B C   1 
ATOM   1022 O O   . GLY   B 1 12  ? 14.408  8.048   37.118  1.00 22.77 ? 26  GLY   B O   1 
ATOM   1023 N N   . SER   B 1 13  ? 13.370  8.665   35.229  1.00 18.57 ? 27  SER   B N   1 
ATOM   1024 C CA  A SER   B 1 13  ? 13.642  10.074  35.460  0.74 17.81 ? 27  SER   B CA  1 
ATOM   1025 C CA  B SER   B 1 13  ? 13.638  10.077  35.455  0.26 17.98 ? 27  SER   B CA  1 
ATOM   1026 C C   . SER   B 1 13  ? 12.594  10.671  36.397  1.00 16.91 ? 27  SER   B C   1 
ATOM   1027 O O   . SER   B 1 13  ? 11.469  10.176  36.510  1.00 17.31 ? 27  SER   B O   1 
ATOM   1028 C CB  A SER   B 1 13  ? 13.668  10.838  34.138  0.74 18.51 ? 27  SER   B CB  1 
ATOM   1029 C CB  B SER   B 1 13  ? 13.628  10.850  34.135  0.26 18.51 ? 27  SER   B CB  1 
ATOM   1030 O OG  A SER   B 1 13  ? 14.788  10.445  33.362  0.74 20.24 ? 27  SER   B OG  1 
ATOM   1031 O OG  B SER   B 1 13  ? 12.317  11.270  33.800  0.26 19.35 ? 27  SER   B OG  1 
ATOM   1032 N N   . THR   B 1 14  ? 12.983  11.752  37.076  1.00 16.65 ? 28  THR   B N   1 
ATOM   1033 C CA  . THR   B 1 14  ? 12.131  12.433  38.047  1.00 17.59 ? 28  THR   B CA  1 
ATOM   1034 C C   . THR   B 1 14  ? 11.973  13.889  37.638  1.00 16.42 ? 28  THR   B C   1 
ATOM   1035 O O   . THR   B 1 14  ? 12.969  14.585  37.406  1.00 17.05 ? 28  THR   B O   1 
ATOM   1036 C CB  . THR   B 1 14  ? 12.715  12.347  39.463  1.00 21.68 ? 28  THR   B CB  1 
ATOM   1037 O OG1 . THR   B 1 14  ? 12.949  10.975  39.787  1.00 25.01 ? 28  THR   B OG1 1 
ATOM   1038 C CG2 . THR   B 1 14  ? 11.748  12.928  40.484  1.00 22.98 ? 28  THR   B CG2 1 
ATOM   1039 N N   A PHE   B 1 15  ? 10.723  14.343  37.574  1.00 15.71 ? 29  PHE   B N   1 
ATOM   1040 N N   B PHE   B 1 15  ? 10.724  14.343  37.576  0.00 16.32 ? 29  PHE   B N   1 
ATOM   1041 C CA  A PHE   B 1 15  ? 10.324  15.644  37.037  1.00 16.89 ? 29  PHE   B CA  1 
ATOM   1042 C CA  B PHE   B 1 15  ? 10.355  15.652  37.041  0.00 16.26 ? 29  PHE   B CA  1 
ATOM   1043 C C   A PHE   B 1 15  ? 9.661   16.355  38.215  1.00 16.55 ? 29  PHE   B C   1 
ATOM   1044 C C   B PHE   B 1 15  ? 9.630   16.417  38.146  0.00 16.38 ? 29  PHE   B C   1 
ATOM   1045 O O   A PHE   B 1 15  ? 8.596   15.932  38.682  1.00 18.12 ? 29  PHE   B O   1 
ATOM   1046 O O   B PHE   B 1 15  ? 8.461   16.147  38.438  0.00 16.37 ? 29  PHE   B O   1 
ATOM   1047 C CB  A PHE   B 1 15  ? 9.369   15.387  35.855  1.00 17.27 ? 29  PHE   B CB  1 
ATOM   1048 C CB  B PHE   B 1 15  ? 9.501   15.453  35.787  0.00 16.09 ? 29  PHE   B CB  1 
ATOM   1049 C CG  A PHE   B 1 15  ? 8.629   16.591  35.330  1.00 16.64 ? 29  PHE   B CG  1 
ATOM   1050 C CG  B PHE   B 1 15  ? 8.605   16.608  35.453  0.00 15.96 ? 29  PHE   B CG  1 
ATOM   1051 C CD1 A PHE   B 1 15  ? 9.253   17.814  35.135  1.00 16.52 ? 29  PHE   B CD1 1 
ATOM   1052 C CD1 B PHE   B 1 15  ? 9.129   17.843  35.115  0.00 15.91 ? 29  PHE   B CD1 1 
ATOM   1053 C CD2 A PHE   B 1 15  ? 7.294   16.461  34.942  1.00 16.87 ? 29  PHE   B CD2 1 
ATOM   1054 C CD2 B PHE   B 1 15  ? 7.231   16.441  35.434  0.00 15.91 ? 29  PHE   B CD2 1 
ATOM   1055 C CE1 A PHE   B 1 15  ? 8.542   18.901  34.616  1.00 16.98 ? 29  PHE   B CE1 1 
ATOM   1056 C CE1 B PHE   B 1 15  ? 8.295   18.897  34.794  0.00 15.90 ? 29  PHE   B CE1 1 
ATOM   1057 C CE2 A PHE   B 1 15  ? 6.588   17.536  34.423  1.00 16.83 ? 29  PHE   B CE2 1 
ATOM   1058 C CE2 B PHE   B 1 15  ? 6.393   17.487  35.113  0.00 15.90 ? 29  PHE   B CE2 1 
ATOM   1059 C CZ  A PHE   B 1 15  ? 7.212   18.758  34.259  1.00 16.39 ? 29  PHE   B CZ  1 
ATOM   1060 C CZ  B PHE   B 1 15  ? 6.925   18.716  34.789  0.00 15.90 ? 29  PHE   B CZ  1 
ATOM   1061 N N   . ILE   B 1 16  ? 10.333  17.367  38.763  1.00 16.69 ? 30  ILE   B N   1 
ATOM   1062 C CA  . ILE   B 1 16  ? 9.856   18.091  39.943  1.00 15.73 ? 30  ILE   B CA  1 
ATOM   1063 C C   . ILE   B 1 16  ? 9.430   19.494  39.511  1.00 15.50 ? 30  ILE   B C   1 
ATOM   1064 O O   . ILE   B 1 16  ? 10.270  20.287  39.075  1.00 18.44 ? 30  ILE   B O   1 
ATOM   1065 C CB  . ILE   B 1 16  ? 10.947  18.161  41.024  1.00 17.75 ? 30  ILE   B CB  1 
ATOM   1066 C CG1 . ILE   B 1 16  ? 11.320  16.756  41.510  1.00 19.55 ? 30  ILE   B CG1 1 
ATOM   1067 C CG2 . ILE   B 1 16  ? 10.495  19.034  42.176  1.00 17.66 ? 30  ILE   B CG2 1 
ATOM   1068 C CD1 . ILE   B 1 16  ? 12.398  16.739  42.592  1.00 21.95 ? 30  ILE   B CD1 1 
ATOM   1069 N N   . VAL   B 1 17  ? 8.137   19.824  39.626  1.00 13.22 ? 31  VAL   B N   1 
ATOM   1070 C CA  . VAL   B 1 17  ? 7.606   21.018  38.971  1.00 12.85 ? 31  VAL   B CA  1 
ATOM   1071 C C   . VAL   B 1 17  ? 6.657   21.787  39.880  1.00 12.85 ? 31  VAL   B C   1 
ATOM   1072 O O   . VAL   B 1 17  ? 5.916   21.204  40.676  1.00 13.19 ? 31  VAL   B O   1 
ATOM   1073 C CB  . VAL   B 1 17  ? 6.912   20.673  37.625  1.00 13.73 ? 31  VAL   B CB  1 
ATOM   1074 C CG1 . VAL   B 1 17  ? 5.611   19.905  37.862  1.00 14.27 ? 31  VAL   B CG1 1 
ATOM   1075 C CG2 . VAL   B 1 17  ? 6.670   21.932  36.780  1.00 13.85 ? 31  VAL   B CG2 1 
ATOM   1076 N N   . THR   B 1 18  ? 6.673   23.113  39.739  1.00 12.91 ? 32  THR   B N   1 
ATOM   1077 C CA  . THR   B 1 18  ? 5.654   23.987  40.309  1.00 13.22 ? 32  THR   B CA  1 
ATOM   1078 C C   . THR   B 1 18  ? 4.942   24.712  39.175  1.00 12.29 ? 32  THR   B C   1 
ATOM   1079 O O   . THR   B 1 18  ? 5.592   25.304  38.303  1.00 12.44 ? 32  THR   B O   1 
ATOM   1080 C CB  . THR   B 1 18  ? 6.255   25.007  41.286  1.00 16.21 ? 32  THR   B CB  1 
ATOM   1081 O OG1 . THR   B 1 18  ? 6.871   24.315  42.377  1.00 18.65 ? 32  THR   B OG1 1 
ATOM   1082 C CG2 . THR   B 1 18  ? 5.162   25.916  41.833  1.00 16.52 ? 32  THR   B CG2 1 
ATOM   1083 N N   . ALA   B 1 19  ? 3.611   24.642  39.182  1.00 12.04 ? 33  ALA   B N   1 
ATOM   1084 C CA  . ALA   B 1 19  ? 2.766   25.344  38.221  1.00 12.56 ? 33  ALA   B CA  1 
ATOM   1085 C C   . ALA   B 1 19  ? 2.292   26.636  38.883  1.00 13.53 ? 33  ALA   B C   1 
ATOM   1086 O O   . ALA   B 1 19  ? 1.439   26.611  39.777  1.00 15.64 ? 33  ALA   B O   1 
ATOM   1087 C CB  . ALA   B 1 19  ? 1.588   24.466  37.802  1.00 13.93 ? 33  ALA   B CB  1 
ATOM   1088 N N   . GLY   B 1 20  ? 2.875   27.756  38.476  1.00 13.40 ? 34  GLY   B N   1 
ATOM   1089 C CA  . GLY   B 1 20  ? 2.559   29.027  39.090  1.00 14.61 ? 34  GLY   B CA  1 
ATOM   1090 C C   . GLY   B 1 20  ? 1.271   29.639  38.573  1.00 13.21 ? 34  GLY   B C   1 
ATOM   1091 O O   . GLY   B 1 20  ? 0.768   29.298  37.496  1.00 13.79 ? 34  GLY   B O   1 
ATOM   1092 N N   . ALA   B 1 21  ? 0.752   30.589  39.353  1.00 14.50 ? 35  ALA   B N   1 
ATOM   1093 C CA  . ALA   B 1 21  ? -0.534  31.191  39.034  1.00 15.60 ? 35  ALA   B CA  1 
ATOM   1094 C C   . ALA   B 1 21  ? -0.520  31.937  37.704  1.00 15.82 ? 35  ALA   B C   1 
ATOM   1095 O O   . ALA   B 1 21  ? -1.583  32.117  37.102  1.00 17.52 ? 35  ALA   B O   1 
ATOM   1096 C CB  . ALA   B 1 21  ? -0.967  32.122  40.171  1.00 17.46 ? 35  ALA   B CB  1 
ATOM   1097 N N   . ASP   B 1 22  ? 0.649   32.371  37.235  1.00 14.76 ? 36  ASP   B N   1 
ATOM   1098 C CA  . ASP   B 1 22  ? 0.774   33.128  35.994  1.00 15.03 ? 36  ASP   B CA  1 
ATOM   1099 C C   . ASP   B 1 22  ? 1.010   32.257  34.762  1.00 14.23 ? 36  ASP   B C   1 
ATOM   1100 O O   . ASP   B 1 22  ? 1.313   32.801  33.696  1.00 15.17 ? 36  ASP   B O   1 
ATOM   1101 C CB  . ASP   B 1 22  ? 1.899   34.160  36.108  1.00 17.52 ? 36  ASP   B CB  1 
ATOM   1102 C CG  . ASP   B 1 22  ? 3.266   33.522  36.307  1.00 19.98 ? 36  ASP   B CG  1 
ATOM   1103 O OD1 . ASP   B 1 22  ? 3.336   32.307  36.606  1.00 19.04 ? 36  ASP   B OD1 1 
ATOM   1104 O OD2 . ASP   B 1 22  ? 4.278   34.244  36.149  1.00 23.02 ? 36  ASP   B OD2 1 
ATOM   1105 N N   . GLY   B 1 23  ? 0.891   30.935  34.880  1.00 12.86 ? 37  GLY   B N   1 
ATOM   1106 C CA  . GLY   B 1 23  ? 1.150   30.053  33.758  1.00 12.45 ? 37  GLY   B CA  1 
ATOM   1107 C C   . GLY   B 1 23  ? 2.561   29.504  33.685  1.00 11.36 ? 37  GLY   B C   1 
ATOM   1108 O O   . GLY   B 1 23  ? 2.877   28.763  32.732  1.00 11.10 ? 37  GLY   B O   1 
ATOM   1109 N N   . ALA   B 1 24  ? 3.416   29.822  34.659  1.00 11.25 ? 38  ALA   B N   1 
ATOM   1110 C CA  . ALA   B 1 24  ? 4.802   29.365  34.629  1.00 12.12 ? 38  ALA   B CA  1 
ATOM   1111 C C   . ALA   B 1 24  ? 4.947   27.923  35.109  1.00 11.96 ? 38  ALA   B C   1 
ATOM   1112 O O   . ALA   B 1 24  ? 4.292   27.502  36.066  1.00 13.23 ? 38  ALA   B O   1 
ATOM   1113 C CB  . ALA   B 1 24  ? 5.667   30.255  35.520  1.00 14.16 ? 38  ALA   B CB  1 
ATOM   1114 N N   . LEU   B 1 25  ? 5.824   27.170  34.447  1.00 11.11 ? 39  LEU   B N   1 
ATOM   1115 C CA  . LEU   B 1 25  ? 6.363   25.924  34.990  1.00 11.06 ? 39  LEU   B CA  1 
ATOM   1116 C C   . LEU   B 1 25  ? 7.823   26.154  35.357  1.00 10.95 ? 39  LEU   B C   1 
ATOM   1117 O O   . LEU   B 1 25  ? 8.594   26.678  34.545  1.00 11.00 ? 39  LEU   B O   1 
ATOM   1118 C CB  . LEU   B 1 25  ? 6.280   24.765  33.986  1.00 11.23 ? 39  LEU   B CB  1 
ATOM   1119 C CG  . LEU   B 1 25  ? 4.889   24.355  33.505  1.00 11.11 ? 39  LEU   B CG  1 
ATOM   1120 C CD1 . LEU   B 1 25  ? 4.989   23.242  32.476  1.00 11.94 ? 39  LEU   B CD1 1 
ATOM   1121 C CD2 . LEU   B 1 25  ? 3.974   23.936  34.659  1.00 11.42 ? 39  LEU   B CD2 1 
ATOM   1122 N N   . THR   B 1 26  ? 8.194   25.754  36.574  1.00 11.22 ? 40  THR   B N   1 
ATOM   1123 C CA  A THR   B 1 26  ? 9.564   25.858  37.047  0.81 11.83 ? 40  THR   B CA  1 
ATOM   1124 C CA  B THR   B 1 26  ? 9.540   25.896  37.107  0.19 11.91 ? 40  THR   B CA  1 
ATOM   1125 C C   . THR   B 1 26  ? 9.893   24.613  37.854  1.00 12.10 ? 40  THR   B C   1 
ATOM   1126 O O   . THR   B 1 26  ? 9.014   23.979  38.439  1.00 15.57 ? 40  THR   B O   1 
ATOM   1127 C CB  A THR   B 1 26  ? 9.801   27.097  37.944  0.81 12.20 ? 40  THR   B CB  1 
ATOM   1128 C CB  B THR   B 1 26  ? 9.540   27.083  38.090  0.19 12.49 ? 40  THR   B CB  1 
ATOM   1129 O OG1 A THR   B 1 26  ? 8.923   27.041  39.078  0.81 13.01 ? 40  THR   B OG1 1 
ATOM   1130 O OG1 B THR   B 1 26  ? 8.998   28.243  37.445  0.19 12.89 ? 40  THR   B OG1 1 
ATOM   1131 C CG2 A THR   B 1 26  ? 9.587   28.405  37.177  0.81 14.10 ? 40  THR   B CG2 1 
ATOM   1132 C CG2 B THR   B 1 26  ? 10.924  27.400  38.590  0.19 13.03 ? 40  THR   B CG2 1 
ATOM   1133 N N   . GLY   B 1 27  ? 11.168  24.242  37.862  1.00 12.00 ? 41  GLY   B N   1 
ATOM   1134 C CA  . GLY   B 1 27  ? 11.529  23.081  38.670  1.00 12.65 ? 41  GLY   B CA  1 
ATOM   1135 C C   . GLY   B 1 27  ? 12.854  22.465  38.243  1.00 12.27 ? 41  GLY   B C   1 
ATOM   1136 O O   . GLY   B 1 27  ? 13.726  23.147  37.705  1.00 12.96 ? 41  GLY   B O   1 
ATOM   1137 N N   . THR   B 1 28  ? 12.972  21.159  38.495  1.00 13.13 ? 42  THR   B N   1 
ATOM   1138 C CA  . THR   B 1 28  ? 14.200  20.425  38.225  1.00 14.88 ? 42  THR   B CA  1 
ATOM   1139 C C   . THR   B 1 28  ? 13.874  19.080  37.585  1.00 14.48 ? 42  THR   B C   1 
ATOM   1140 O O   . THR   B 1 28  ? 12.819  18.488  37.838  1.00 16.26 ? 42  THR   B O   1 
ATOM   1141 C CB  . THR   B 1 28  ? 15.015  20.183  39.503  1.00 18.38 ? 42  THR   B CB  1 
ATOM   1142 O OG1 . THR   B 1 28  ? 14.272  19.331  40.377  1.00 21.41 ? 42  THR   B OG1 1 
ATOM   1143 C CG2 . THR   B 1 28  ? 15.314  21.492  40.205  1.00 18.56 ? 42  THR   B CG2 1 
ATOM   1144 N N   . TYR   B 1 29  ? 14.798  18.602  36.754  1.00 14.29 ? 43  TYR   B N   1 
ATOM   1145 C CA  . TYR   B 1 29  ? 14.671  17.321  36.075  1.00 14.23 ? 43  TYR   B CA  1 
ATOM   1146 C C   . TYR   B 1 29  ? 15.905  16.494  36.407  1.00 15.49 ? 43  TYR   B C   1 
ATOM   1147 O O   . TYR   B 1 29  ? 17.031  17.000  36.331  1.00 15.97 ? 43  TYR   B O   1 
ATOM   1148 C CB  . TYR   B 1 29  ? 14.543  17.533  34.553  1.00 14.27 ? 43  TYR   B CB  1 
ATOM   1149 C CG  . TYR   B 1 29  ? 13.903  16.365  33.826  1.00 13.52 ? 43  TYR   B CG  1 
ATOM   1150 C CD1 . TYR   B 1 29  ? 14.663  15.282  33.391  1.00 15.10 ? 43  TYR   B CD1 1 
ATOM   1151 C CD2 . TYR   B 1 29  ? 12.539  16.343  33.576  1.00 13.53 ? 43  TYR   B CD2 1 
ATOM   1152 C CE1 . TYR   B 1 29  ? 14.079  14.209  32.733  1.00 15.24 ? 43  TYR   B CE1 1 
ATOM   1153 C CE2 . TYR   B 1 29  ? 11.952  15.281  32.928  1.00 13.84 ? 43  TYR   B CE2 1 
ATOM   1154 C CZ  . TYR   B 1 29  ? 12.722  14.217  32.507  1.00 15.15 ? 43  TYR   B CZ  1 
ATOM   1155 O OH  . TYR   B 1 29  ? 12.131  13.155  31.864  1.00 16.54 ? 43  TYR   B OH  1 
ATOM   1156 N N   . GLU   B 1 30  ? 15.694  15.236  36.799  1.00 18.46 ? 44  GLU   B N   1 
ATOM   1157 C CA  . GLU   B 1 30  ? 16.768  14.368  37.266  1.00 22.89 ? 44  GLU   B CA  1 
ATOM   1158 C C   . GLU   B 1 30  ? 16.785  13.068  36.486  1.00 24.88 ? 44  GLU   B C   1 
ATOM   1159 O O   . GLU   B 1 30  ? 15.733  12.480  36.221  1.00 23.34 ? 44  GLU   B O   1 
ATOM   1160 C CB  . GLU   B 1 30  ? 16.568  13.981  38.726  1.00 27.51 ? 44  GLU   B CB  1 
ATOM   1161 C CG  . GLU   B 1 30  ? 16.938  15.032  39.724  1.00 32.18 ? 44  GLU   B CG  1 
ATOM   1162 C CD  . GLU   B 1 30  ? 16.508  14.649  41.119  1.00 34.56 ? 44  GLU   B CD  1 
ATOM   1163 O OE1 . GLU   B 1 30  ? 16.936  13.573  41.596  1.00 36.15 ? 44  GLU   B OE1 1 
ATOM   1164 O OE2 . GLU   B 1 30  ? 15.730  15.415  41.727  1.00 35.04 ? 44  GLU   B OE2 1 
ATOM   1165 N N   . SER   B 1 31  ? 17.994  12.607  36.166  1.00 30.20 ? 45  SER   B N   1 
ATOM   1166 C CA  . SER   B 1 31  ? 18.236  11.281  35.592  1.00 35.63 ? 45  SER   B CA  1 
ATOM   1167 C C   . SER   B 1 31  ? 17.529  11.047  34.264  1.00 38.34 ? 45  SER   B C   1 
ATOM   1168 O O   . SER   B 1 31  ? 17.461  9.912   33.787  1.00 39.46 ? 45  SER   B O   1 
ATOM   1169 C CB  . SER   B 1 31  ? 17.854  10.183  36.586  1.00 37.25 ? 45  SER   B CB  1 
ATOM   1170 O OG  . SER   B 1 31  ? 18.549  10.342  37.809  1.00 38.88 ? 45  SER   B OG  1 
ATOM   1171 N N   . ASN   B 1 35  ? 24.299  12.412  42.292  1.00 44.33 ? 49  ASN   B N   1 
ATOM   1172 C CA  . ASN   B 1 35  ? 22.886  12.662  42.033  1.00 44.03 ? 49  ASN   B CA  1 
ATOM   1173 C C   . ASN   B 1 35  ? 22.652  14.122  41.663  1.00 42.16 ? 49  ASN   B C   1 
ATOM   1174 O O   . ASN   B 1 35  ? 21.924  14.416  40.716  1.00 41.96 ? 49  ASN   B O   1 
ATOM   1175 C CB  . ASN   B 1 35  ? 22.035  12.272  43.242  1.00 45.72 ? 49  ASN   B CB  1 
ATOM   1176 C CG  . ASN   B 1 35  ? 20.555  12.211  42.917  1.00 47.26 ? 49  ASN   B CG  1 
ATOM   1177 O OD1 . ASN   B 1 35  ? 19.779  13.073  43.331  1.00 48.01 ? 49  ASN   B OD1 1 
ATOM   1178 N ND2 . ASN   B 1 35  ? 20.157  11.191  42.164  1.00 47.85 ? 49  ASN   B ND2 1 
ATOM   1179 N N   . ALA   B 1 36  ? 23.266  15.039  42.417  1.00 39.97 ? 50  ALA   B N   1 
ATOM   1180 C CA  . ALA   B 1 36  ? 23.239  16.443  42.021  1.00 38.05 ? 50  ALA   B CA  1 
ATOM   1181 C C   . ALA   B 1 36  ? 23.866  16.634  40.647  1.00 34.67 ? 50  ALA   B C   1 
ATOM   1182 O O   . ALA   B 1 36  ? 23.439  17.506  39.880  1.00 33.03 ? 50  ALA   B O   1 
ATOM   1183 C CB  . ALA   B 1 36  ? 23.957  17.302  43.062  1.00 38.42 ? 50  ALA   B CB  1 
ATOM   1184 N N   . GLU   B 1 37  ? 24.861  15.810  40.312  1.00 32.09 ? 51  GLU   B N   1 
ATOM   1185 C CA  . GLU   B 1 37  ? 25.476  15.856  38.992  1.00 30.74 ? 51  GLU   B CA  1 
ATOM   1186 C C   . GLU   B 1 37  ? 24.484  15.534  37.882  1.00 28.18 ? 51  GLU   B C   1 
ATOM   1187 O O   . GLU   B 1 37  ? 24.757  15.839  36.717  1.00 28.37 ? 51  GLU   B O   1 
ATOM   1188 C CB  . GLU   B 1 37  ? 26.645  14.870  38.929  1.00 32.57 ? 51  GLU   B CB  1 
ATOM   1189 C CG  . GLU   B 1 37  ? 27.254  14.501  40.279  1.00 34.56 ? 51  GLU   B CG  1 
ATOM   1190 C CD  . GLU   B 1 37  ? 28.045  15.633  40.908  0.36 35.78 ? 51  GLU   B CD  1 
ATOM   1191 O OE1 . GLU   B 1 37  ? 27.425  16.611  41.375  0.34 36.16 ? 51  GLU   B OE1 1 
ATOM   1192 O OE2 . GLU   B 1 37  ? 29.291  15.542  40.937  0.34 36.24 ? 51  GLU   B OE2 1 
ATOM   1193 N N   . SER   B 1 38  ? 23.342  14.925  38.209  1.00 25.76 ? 52  SER   B N   1 
ATOM   1194 C CA  . SER   B 1 38  ? 22.353  14.546  37.207  1.00 25.31 ? 52  SER   B CA  1 
ATOM   1195 C C   . SER   B 1 38  ? 21.067  15.367  37.296  1.00 20.98 ? 52  SER   B C   1 
ATOM   1196 O O   . SER   B 1 38  ? 20.049  14.974  36.720  1.00 20.57 ? 52  SER   B O   1 
ATOM   1197 C CB  . SER   B 1 38  ? 22.044  13.050  37.293  1.00 29.20 ? 52  SER   B CB  1 
ATOM   1198 O OG  . SER   B 1 38  ? 21.402  12.735  38.513  1.00 32.42 ? 52  SER   B OG  1 
ATOM   1199 N N   . ARG   B 1 39  ? 21.091  16.503  37.990  1.00 19.91 ? 53  ARG   B N   1 
ATOM   1200 C CA  . ARG   B 1 39  ? 19.916  17.353  38.142  1.00 19.27 ? 53  ARG   B CA  1 
ATOM   1201 C C   . ARG   B 1 39  ? 20.077  18.634  37.329  1.00 15.67 ? 53  ARG   B C   1 
ATOM   1202 O O   . ARG   B 1 39  ? 21.155  19.243  37.319  1.00 16.00 ? 53  ARG   B O   1 
ATOM   1203 C CB  . ARG   B 1 39  ? 19.680  17.689  39.617  1.00 22.71 ? 53  ARG   B CB  1 
ATOM   1204 C CG  . ARG   B 1 39  ? 18.333  18.321  39.896  1.00 27.04 ? 53  ARG   B CG  1 
ATOM   1205 C CD  . ARG   B 1 39  ? 17.881  18.079  41.334  1.00 31.24 ? 53  ARG   B CD  1 
ATOM   1206 N NE  . ARG   B 1 39  ? 18.944  18.300  42.308  1.00 34.78 ? 53  ARG   B NE  1 
ATOM   1207 C CZ  . ARG   B 1 39  ? 19.523  17.341  43.020  1.00 36.83 ? 53  ARG   B CZ  1 
ATOM   1208 N NH1 . ARG   B 1 39  ? 19.161  16.074  42.897  1.00 37.07 ? 53  ARG   B NH1 1 
ATOM   1209 N NH2 . ARG   B 1 39  ? 20.484  17.663  43.880  1.00 38.28 ? 53  ARG   B NH2 1 
ATOM   1210 N N   . TYR   B 1 40  ? 19.001  19.035  36.644  1.00 13.78 ? 54  TYR   B N   1 
ATOM   1211 C CA  . TYR   B 1 40  ? 19.038  20.139  35.692  1.00 13.21 ? 54  TYR   B CA  1 
ATOM   1212 C C   . TYR   B 1 40  ? 17.818  21.034  35.877  1.00 13.20 ? 54  TYR   B C   1 
ATOM   1213 O O   . TYR   B 1 40  ? 16.735  20.563  36.226  1.00 13.78 ? 54  TYR   B O   1 
ATOM   1214 C CB  . TYR   B 1 40  ? 19.047  19.603  34.246  1.00 13.33 ? 54  TYR   B CB  1 
ATOM   1215 C CG  . TYR   B 1 40  ? 20.249  18.737  33.950  1.00 13.73 ? 54  TYR   B CG  1 
ATOM   1216 C CD1 . TYR   B 1 40  ? 20.262  17.381  34.278  1.00 14.77 ? 54  TYR   B CD1 1 
ATOM   1217 C CD2 . TYR   B 1 40  ? 21.392  19.288  33.381  1.00 13.71 ? 54  TYR   B CD2 1 
ATOM   1218 C CE1 . TYR   B 1 40  ? 21.381  16.597  34.043  1.00 16.27 ? 54  TYR   B CE1 1 
ATOM   1219 C CE2 . TYR   B 1 40  ? 22.516  18.512  33.135  1.00 14.78 ? 54  TYR   B CE2 1 
ATOM   1220 C CZ  . TYR   B 1 40  ? 22.503  17.166  33.457  1.00 16.18 ? 54  TYR   B CZ  1 
ATOM   1221 O OH  . TYR   B 1 40  ? 23.620  16.393  33.222  1.00 17.90 ? 54  TYR   B OH  1 
ATOM   1222 N N   . VAL   B 1 41  ? 17.999  22.332  35.612  1.00 12.62 ? 55  VAL   B N   1 
ATOM   1223 C CA  . VAL   B 1 41  ? 16.889  23.285  35.650  1.00 13.19 ? 55  VAL   B CA  1 
ATOM   1224 C C   . VAL   B 1 41  ? 15.921  23.037  34.498  1.00 12.85 ? 55  VAL   B C   1 
ATOM   1225 O O   . VAL   B 1 41  ? 16.328  22.744  33.366  1.00 13.50 ? 55  VAL   B O   1 
ATOM   1226 C CB  . VAL   B 1 41  ? 17.445  24.719  35.567  1.00 14.16 ? 55  VAL   B CB  1 
ATOM   1227 C CG1 . VAL   B 1 41  ? 16.325  25.761  35.415  1.00 14.82 ? 55  VAL   B CG1 1 
ATOM   1228 C CG2 . VAL   B 1 41  ? 18.293  25.031  36.773  1.00 15.39 ? 55  VAL   B CG2 1 
ATOM   1229 N N   . LEU   B 1 42  ? 14.627  23.201  34.762  1.00 12.62 ? 56  LEU   B N   1 
ATOM   1230 C CA  . LEU   B 1 42  ? 13.641  23.252  33.689  1.00 13.74 ? 56  LEU   B CA  1 
ATOM   1231 C C   . LEU   B 1 42  ? 12.761  24.481  33.832  1.00 13.54 ? 56  LEU   B C   1 
ATOM   1232 O O   . LEU   B 1 42  ? 12.508  24.956  34.944  1.00 13.99 ? 56  LEU   B O   1 
ATOM   1233 C CB  . LEU   B 1 42  ? 12.743  22.019  33.696  1.00 15.20 ? 56  LEU   B CB  1 
ATOM   1234 C CG  . LEU   B 1 42  ? 11.713  21.908  34.826  1.00 14.74 ? 56  LEU   B CG  1 
ATOM   1235 C CD1 . LEU   B 1 42  ? 10.336  22.510  34.451  1.00 14.64 ? 56  LEU   B CD1 1 
ATOM   1236 C CD2 . LEU   B 1 42  ? 11.558  20.464  35.221  1.00 17.54 ? 56  LEU   B CD2 1 
ATOM   1237 N N   . THR   B 1 43  ? 12.275  24.974  32.692  1.00 12.60 ? 57  THR   B N   1 
ATOM   1238 C CA  A THR   B 1 43  ? 11.270  26.027  32.678  0.38 12.07 ? 57  THR   B CA  1 
ATOM   1239 C CA  B THR   B 1 43  ? 11.282  26.043  32.663  0.62 12.25 ? 57  THR   B CA  1 
ATOM   1240 C C   . THR   B 1 43  ? 10.320  25.805  31.507  1.00 10.89 ? 57  THR   B C   1 
ATOM   1241 O O   . THR   B 1 43  ? 10.701  25.263  30.462  1.00 10.11 ? 57  THR   B O   1 
ATOM   1242 C CB  A THR   B 1 43  ? 11.904  27.424  32.631  0.38 14.04 ? 57  THR   B CB  1 
ATOM   1243 C CB  B THR   B 1 43  ? 11.885  27.466  32.557  0.62 14.85 ? 57  THR   B CB  1 
ATOM   1244 O OG1 A THR   B 1 43  ? 10.878  28.419  32.612  0.38 14.76 ? 57  THR   B OG1 1 
ATOM   1245 O OG1 B THR   B 1 43  ? 12.524  27.648  31.288  0.62 16.87 ? 57  THR   B OG1 1 
ATOM   1246 C CG2 A THR   B 1 43  ? 12.747  27.582  31.407  0.38 14.94 ? 57  THR   B CG2 1 
ATOM   1247 C CG2 B THR   B 1 43  ? 12.890  27.722  33.676  0.62 15.68 ? 57  THR   B CG2 1 
ATOM   1248 N N   . GLY   B 1 44  ? 9.072   26.223  31.683  1.00 10.94 ? 58  GLY   B N   1 
ATOM   1249 C CA  . GLY   B 1 44  ? 8.079   26.078  30.636  1.00 10.29 ? 58  GLY   B CA  1 
ATOM   1250 C C   . GLY   B 1 44  ? 6.819   26.859  30.956  1.00 9.69  ? 58  GLY   B C   1 
ATOM   1251 O O   . GLY   B 1 44  ? 6.826   27.768  31.793  1.00 10.41 ? 58  GLY   B O   1 
ATOM   1252 N N   . ARG   B 1 45  ? 5.730   26.479  30.288  1.00 9.40  ? 59  ARG   B N   1 
ATOM   1253 C CA  . ARG   B 1 45  ? 4.454   27.183  30.380  1.00 9.83  ? 59  ARG   B CA  1 
ATOM   1254 C C   . ARG   B 1 45  ? 3.322   26.166  30.306  1.00 9.91  ? 59  ARG   B C   1 
ATOM   1255 O O   . ARG   B 1 45  ? 3.471   25.098  29.698  1.00 10.77 ? 59  ARG   B O   1 
ATOM   1256 C CB  . ARG   B 1 45  ? 4.278   28.166  29.203  1.00 11.32 ? 59  ARG   B CB  1 
ATOM   1257 C CG  . ARG   B 1 45  ? 5.354   29.253  29.089  1.00 11.57 ? 59  ARG   B CG  1 
ATOM   1258 C CD  . ARG   B 1 45  ? 5.223   30.306  30.188  1.00 12.20 ? 59  ARG   B CD  1 
ATOM   1259 N NE  . ARG   B 1 45  ? 3.962   31.028  30.070  1.00 10.93 ? 59  ARG   B NE  1 
ATOM   1260 C CZ  . ARG   B 1 45  ? 3.460   31.814  31.014  1.00 12.49 ? 59  ARG   B CZ  1 
ATOM   1261 N NH1 . ARG   B 1 45  ? 4.098   32.011  32.160  1.00 13.72 ? 59  ARG   B NH1 1 
ATOM   1262 N NH2 . ARG   B 1 45  ? 2.293   32.420  30.800  1.00 13.38 ? 59  ARG   B NH2 1 
ATOM   1263 N N   . TYR   B 1 46  ? 2.175   26.510  30.902  1.00 10.00 ? 60  TYR   B N   1 
ATOM   1264 C CA  . TYR   B 1 46  ? 0.977   25.685  30.812  1.00 10.28 ? 60  TYR   B CA  1 
ATOM   1265 C C   . TYR   B 1 46  ? -0.247  26.584  30.700  1.00 10.61 ? 60  TYR   B C   1 
ATOM   1266 O O   . TYR   B 1 46  ? -0.201  27.765  31.057  1.00 11.61 ? 60  TYR   B O   1 
ATOM   1267 C CB  . TYR   B 1 46  ? 0.844   24.732  32.018  1.00 11.00 ? 60  TYR   B CB  1 
ATOM   1268 C CG  . TYR   B 1 46  ? 0.412   25.408  33.303  1.00 10.94 ? 60  TYR   B CG  1 
ATOM   1269 C CD1 . TYR   B 1 46  ? 1.287   26.217  34.025  1.00 10.99 ? 60  TYR   B CD1 1 
ATOM   1270 C CD2 . TYR   B 1 46  ? -0.875  25.239  33.795  1.00 11.87 ? 60  TYR   B CD2 1 
ATOM   1271 C CE1 . TYR   B 1 46  ? 0.881   26.849  35.205  1.00 11.60 ? 60  TYR   B CE1 1 
ATOM   1272 C CE2 . TYR   B 1 46  ? -1.287  25.868  34.970  1.00 12.25 ? 60  TYR   B CE2 1 
ATOM   1273 C CZ  . TYR   B 1 46  ? -0.407  26.665  35.662  1.00 11.96 ? 60  TYR   B CZ  1 
ATOM   1274 O OH  . TYR   B 1 46  ? -0.847  27.274  36.819  1.00 13.07 ? 60  TYR   B OH  1 
ATOM   1275 N N   . ASP   B 1 47  ? -1.348  26.006  30.213  1.00 10.84 ? 61  ASP   B N   1 
ATOM   1276 C CA  . ASP   B 1 47  ? -2.640  26.698  30.144  1.00 11.64 ? 61  ASP   B CA  1 
ATOM   1277 C C   . ASP   B 1 47  ? -3.232  26.810  31.549  1.00 11.85 ? 61  ASP   B C   1 
ATOM   1278 O O   . ASP   B 1 47  ? -3.667  25.811  32.130  1.00 11.74 ? 61  ASP   B O   1 
ATOM   1279 C CB  . ASP   B 1 47  ? -3.570  25.921  29.209  1.00 11.89 ? 61  ASP   B CB  1 
ATOM   1280 C CG  . ASP   B 1 47  ? -4.951  26.556  29.057  1.00 12.64 ? 61  ASP   B CG  1 
ATOM   1281 O OD1 . ASP   B 1 47  ? -5.198  27.654  29.612  1.00 13.34 ? 61  ASP   B OD1 1 
ATOM   1282 O OD2 . ASP   B 1 47  ? -5.786  25.942  28.340  1.00 12.58 ? 61  ASP   B OD2 1 
ATOM   1283 N N   . SER   B 1 48  ? -3.259  28.026  32.104  1.00 11.78 ? 62  SER   B N   1 
ATOM   1284 C CA  . SER   B 1 48  ? -3.762  28.233  33.459  1.00 11.59 ? 62  SER   B CA  1 
ATOM   1285 C C   . SER   B 1 48  ? -5.285  28.308  33.527  1.00 13.21 ? 62  SER   B C   1 
ATOM   1286 O O   . SER   B 1 48  ? -5.831  28.409  34.634  1.00 14.68 ? 62  SER   B O   1 
ATOM   1287 C CB  . SER   B 1 48  ? -3.149  29.502  34.058  1.00 13.71 ? 62  SER   B CB  1 
ATOM   1288 O OG  . SER   B 1 48  ? -3.429  30.605  33.219  1.00 15.28 ? 62  SER   B OG  1 
ATOM   1289 N N   . ALA   B 1 49  ? -5.983  28.276  32.391  1.00 13.09 ? 63  ALA   B N   1 
ATOM   1290 C CA  . ALA   B 1 49  ? -7.448  28.284  32.362  1.00 13.56 ? 63  ALA   B CA  1 
ATOM   1291 C C   . ALA   B 1 49  ? -7.956  27.221  31.391  1.00 13.47 ? 63  ALA   B C   1 
ATOM   1292 O O   . ALA   B 1 49  ? -8.599  27.534  30.384  1.00 14.88 ? 63  ALA   B O   1 
ATOM   1293 C CB  . ALA   B 1 49  ? -7.970  29.672  31.988  1.00 15.98 ? 63  ALA   B CB  1 
ATOM   1294 N N   . PRO   B 1 50  ? -7.686  25.944  31.664  1.00 13.62 ? 64  PRO   B N   1 
ATOM   1295 C CA  . PRO   B 1 50  ? -8.114  24.891  30.733  1.00 13.98 ? 64  PRO   B CA  1 
ATOM   1296 C C   . PRO   B 1 50  ? -9.628  24.747  30.708  1.00 14.82 ? 64  PRO   B C   1 
ATOM   1297 O O   . PRO   B 1 50  ? -10.347 25.221  31.590  1.00 15.78 ? 64  PRO   B O   1 
ATOM   1298 C CB  . PRO   B 1 50  ? -7.462  23.630  31.314  1.00 14.58 ? 64  PRO   B CB  1 
ATOM   1299 C CG  . PRO   B 1 50  ? -7.410  23.918  32.793  1.00 14.58 ? 64  PRO   B CG  1 
ATOM   1300 C CD  . PRO   B 1 50  ? -7.041  25.379  32.865  1.00 14.47 ? 64  PRO   B CD  1 
ATOM   1301 N N   . ALA   B 1 51  ? -10.110 24.071  29.671  1.00 15.44 ? 65  ALA   B N   1 
ATOM   1302 C CA  . ALA   B 1 51  ? -11.526 23.751  29.582  1.00 16.33 ? 65  ALA   B CA  1 
ATOM   1303 C C   . ALA   B 1 51  ? -11.928 22.793  30.703  1.00 16.81 ? 65  ALA   B C   1 
ATOM   1304 O O   . ALA   B 1 51  ? -11.101 22.065  31.256  1.00 18.23 ? 65  ALA   B O   1 
ATOM   1305 C CB  . ALA   B 1 51  ? -11.832 23.128  28.221  1.00 17.73 ? 65  ALA   B CB  1 
ATOM   1306 N N   . THR   B 1 52  ? -13.215 22.824  31.059  1.00 18.51 ? 66  THR   B N   1 
ATOM   1307 C CA  A THR   B 1 52  ? -13.775 21.892  32.031  0.42 19.65 ? 66  THR   B CA  1 
ATOM   1308 C CA  B THR   B 1 52  ? -13.765 21.887  32.033  0.58 19.50 ? 66  THR   B CA  1 
ATOM   1309 C C   . THR   B 1 52  ? -14.776 20.979  31.336  1.00 18.77 ? 66  THR   B C   1 
ATOM   1310 O O   . THR   B 1 52  ? -15.935 20.864  31.759  1.00 19.14 ? 66  THR   B O   1 
ATOM   1311 C CB  A THR   B 1 52  ? -14.439 22.651  33.178  0.42 21.31 ? 66  THR   B CB  1 
ATOM   1312 C CB  B THR   B 1 52  ? -14.375 22.634  33.226  0.58 20.97 ? 66  THR   B CB  1 
ATOM   1313 O OG1 A THR   B 1 52  ? -15.239 23.713  32.644  0.42 22.89 ? 66  THR   B OG1 1 
ATOM   1314 O OG1 B THR   B 1 52  ? -13.476 23.667  33.656  0.58 22.43 ? 66  THR   B OG1 1 
ATOM   1315 C CG2 A THR   B 1 52  ? -13.385 23.222  34.116  0.42 20.87 ? 66  THR   B CG2 1 
ATOM   1316 C CG2 B THR   B 1 52  ? -14.618 21.678  34.397  0.58 20.55 ? 66  THR   B CG2 1 
ATOM   1317 N N   . ASP   B 1 53  ? -14.330 20.335  30.251  1.00 17.97 ? 67  ASP   B N   1 
ATOM   1318 C CA  . ASP   B 1 53  ? -15.180 19.482  29.433  1.00 17.67 ? 67  ASP   B CA  1 
ATOM   1319 C C   . ASP   B 1 53  ? -14.606 18.085  29.233  1.00 18.67 ? 67  ASP   B C   1 
ATOM   1320 O O   . ASP   B 1 53  ? -15.071 17.362  28.346  1.00 21.43 ? 67  ASP   B O   1 
ATOM   1321 C CB  . ASP   B 1 53  ? -15.480 20.138  28.075  1.00 17.40 ? 67  ASP   B CB  1 
ATOM   1322 C CG  . ASP   B 1 53  ? -14.243 20.311  27.215  1.00 17.40 ? 67  ASP   B CG  1 
ATOM   1323 O OD1 . ASP   B 1 53  ? -13.131 19.970  27.673  1.00 17.07 ? 67  ASP   B OD1 1 
ATOM   1324 O OD2 . ASP   B 1 53  ? -14.391 20.809  26.079  1.00 18.08 ? 67  ASP   B OD2 1 
ATOM   1325 N N   . GLY   B 1 54  ? -13.614 17.690  30.025  1.00 17.67 ? 68  GLY   B N   1 
ATOM   1326 C CA  . GLY   B 1 54  ? -12.927 16.428  29.850  1.00 18.64 ? 68  GLY   B CA  1 
ATOM   1327 C C   . GLY   B 1 54  ? -11.618 16.518  29.089  1.00 18.08 ? 68  GLY   B C   1 
ATOM   1328 O O   . GLY   B 1 54  ? -10.896 15.513  29.004  1.00 20.96 ? 68  GLY   B O   1 
ATOM   1329 N N   . SER   B 1 55  ? -11.290 17.683  28.538  1.00 16.54 ? 69  SER   B N   1 
ATOM   1330 C CA  . SER   B 1 55  ? -10.040 17.863  27.813  1.00 15.95 ? 69  SER   B CA  1 
ATOM   1331 C C   . SER   B 1 55  ? -8.864  18.009  28.773  1.00 14.21 ? 69  SER   B C   1 
ATOM   1332 O O   . SER   B 1 55  ? -9.004  18.501  29.892  1.00 14.58 ? 69  SER   B O   1 
ATOM   1333 C CB  . SER   B 1 55  ? -10.115 19.141  26.979  1.00 17.26 ? 69  SER   B CB  1 
ATOM   1334 O OG  . SER   B 1 55  ? -11.175 19.075  26.052  1.00 19.23 ? 69  SER   B OG  1 
ATOM   1335 N N   . GLY   B 1 56  ? -7.684  17.608  28.308  1.00 12.82 ? 70  GLY   B N   1 
ATOM   1336 C CA  . GLY   B 1 56  ? -6.474  17.799  29.079  1.00 12.24 ? 70  GLY   B CA  1 
ATOM   1337 C C   . GLY   B 1 56  ? -6.009  19.250  29.097  1.00 10.87 ? 70  GLY   B C   1 
ATOM   1338 O O   . GLY   B 1 56  ? -6.558  20.128  28.424  1.00 11.99 ? 70  GLY   B O   1 
ATOM   1339 N N   . THR   B 1 57  ? -4.958  19.491  29.890  1.00 11.14 ? 71  THR   B N   1 
ATOM   1340 C CA  . THR   B 1 57  ? -4.359  20.817  30.057  1.00 11.37 ? 71  THR   B CA  1 
ATOM   1341 C C   . THR   B 1 57  ? -3.056  20.866  29.267  1.00 9.98  ? 71  THR   B C   1 
ATOM   1342 O O   . THR   B 1 57  ? -2.107  20.136  29.576  1.00 10.55 ? 71  THR   B O   1 
ATOM   1343 C CB  . THR   B 1 57  ? -4.078  21.091  31.534  1.00 11.84 ? 71  THR   B CB  1 
ATOM   1344 O OG1 . THR   B 1 57  ? -5.301  21.040  32.269  1.00 12.39 ? 71  THR   B OG1 1 
ATOM   1345 C CG2 . THR   B 1 57  ? -3.459  22.463  31.712  1.00 12.29 ? 71  THR   B CG2 1 
ATOM   1346 N N   . ALA   B 1 58  ? -3.009  21.713  28.236  1.00 9.92  ? 72  ALA   B N   1 
ATOM   1347 C CA  . ALA   B 1 58  ? -1.818  21.779  27.394  1.00 9.74  ? 72  ALA   B CA  1 
ATOM   1348 C C   . ALA   B 1 58  ? -0.643  22.413  28.142  1.00 9.74  ? 72  ALA   B C   1 
ATOM   1349 O O   . ALA   B 1 58  ? -0.817  23.340  28.943  1.00 10.60 ? 72  ALA   B O   1 
ATOM   1350 C CB  . ALA   B 1 58  ? -2.116  22.603  26.148  1.00 10.97 ? 72  ALA   B CB  1 
ATOM   1351 N N   . LEU   B 1 59  ? 0.572   21.922  27.861  1.00 9.35  ? 73  LEU   B N   1 
ATOM   1352 C CA  A LEU   B 1 59  ? 1.765   22.416  28.543  0.68 9.18  ? 73  LEU   B CA  1 
ATOM   1353 C CA  B LEU   B 1 59  ? 1.764   22.436  28.531  0.32 9.10  ? 73  LEU   B CA  1 
ATOM   1354 C C   . LEU   B 1 59  ? 3.013   22.045  27.748  1.00 9.30  ? 73  LEU   B C   1 
ATOM   1355 O O   . LEU   B 1 59  ? 2.970   21.216  26.837  1.00 10.84 ? 73  LEU   B O   1 
ATOM   1356 C CB  A LEU   B 1 59  ? 1.852   21.853  29.968  0.68 10.93 ? 73  LEU   B CB  1 
ATOM   1357 C CB  B LEU   B 1 59  ? 1.844   21.951  29.989  0.32 9.70  ? 73  LEU   B CB  1 
ATOM   1358 C CG  A LEU   B 1 59  ? 1.707   20.333  30.140  0.68 12.09 ? 73  LEU   B CG  1 
ATOM   1359 C CG  B LEU   B 1 59  ? 2.441   20.580  30.339  0.32 9.62  ? 73  LEU   B CG  1 
ATOM   1360 C CD1 A LEU   B 1 59  ? 2.943   19.548  29.684  0.68 13.65 ? 73  LEU   B CD1 1 
ATOM   1361 C CD1 B LEU   B 1 59  ? 2.506   20.387  31.853  0.32 9.90  ? 73  LEU   B CD1 1 
ATOM   1362 C CD2 A LEU   B 1 59  ? 1.362   19.987  31.575  0.68 12.56 ? 73  LEU   B CD2 1 
ATOM   1363 C CD2 B LEU   B 1 59  ? 1.667   19.437  29.702  0.32 9.87  ? 73  LEU   B CD2 1 
ATOM   1364 N N   . GLY   B 1 60  ? 4.144   22.643  28.136  1.00 9.35  ? 74  GLY   B N   1 
ATOM   1365 C CA  . GLY   B 1 60  ? 5.438   22.267  27.589  1.00 9.23  ? 74  GLY   B CA  1 
ATOM   1366 C C   . GLY   B 1 60  ? 6.558   22.796  28.457  1.00 9.25  ? 74  GLY   B C   1 
ATOM   1367 O O   . GLY   B 1 60  ? 6.370   23.746  29.228  1.00 9.72  ? 74  GLY   B O   1 
ATOM   1368 N N   . TRP   B 1 61  ? 7.726   22.146  28.371  1.00 8.98  ? 75  TRP   B N   1 
ATOM   1369 C CA  . TRP   B 1 61  ? 8.891   22.648  29.094  1.00 8.56  ? 75  TRP   B CA  1 
ATOM   1370 C C   . TRP   B 1 61  ? 10.184  22.243  28.388  1.00 9.03  ? 75  TRP   B C   1 
ATOM   1371 O O   . TRP   B 1 61  ? 10.198  21.360  27.522  1.00 9.77  ? 75  TRP   B O   1 
ATOM   1372 C CB  . TRP   B 1 61  ? 8.883   22.207  30.573  1.00 9.73  ? 75  TRP   B CB  1 
ATOM   1373 C CG  . TRP   B 1 61  ? 9.145   20.740  30.802  1.00 9.67  ? 75  TRP   B CG  1 
ATOM   1374 C CD1 . TRP   B 1 61  ? 10.354  20.153  31.050  1.00 10.36 ? 75  TRP   B CD1 1 
ATOM   1375 C CD2 . TRP   B 1 61  ? 8.173   19.685  30.840  1.00 9.87  ? 75  TRP   B CD2 1 
ATOM   1376 N NE1 . TRP   B 1 61  ? 10.199  18.800  31.229  1.00 11.59 ? 75  TRP   B NE1 1 
ATOM   1377 C CE2 . TRP   B 1 61  ? 8.872   18.484  31.095  1.00 10.63 ? 75  TRP   B CE2 1 
ATOM   1378 C CE3 . TRP   B 1 61  ? 6.782   19.633  30.673  1.00 10.90 ? 75  TRP   B CE3 1 
ATOM   1379 C CZ2 . TRP   B 1 61  ? 8.231   17.249  31.185  1.00 11.55 ? 75  TRP   B CZ2 1 
ATOM   1380 C CZ3 . TRP   B 1 61  ? 6.148   18.398  30.762  1.00 11.41 ? 75  TRP   B CZ3 1 
ATOM   1381 C CH2 . TRP   B 1 61  ? 6.875   17.226  31.009  1.00 11.46 ? 75  TRP   B CH2 1 
ATOM   1382 N N   . THR   B 1 62  ? 11.286  22.894  28.790  1.00 9.91  ? 76  THR   B N   1 
ATOM   1383 C CA  . THR   B 1 62  ? 12.615  22.691  28.223  1.00 9.77  ? 76  THR   B CA  1 
ATOM   1384 C C   . THR   B 1 62  ? 13.623  22.413  29.334  1.00 9.83  ? 76  THR   B C   1 
ATOM   1385 O O   . THR   B 1 62  ? 13.564  23.031  30.407  1.00 10.93 ? 76  THR   B O   1 
ATOM   1386 C CB  . THR   B 1 62  ? 13.095  23.955  27.472  1.00 9.84  ? 76  THR   B CB  1 
ATOM   1387 O OG1 . THR   B 1 62  ? 12.147  24.312  26.459  1.00 10.09 ? 76  THR   B OG1 1 
ATOM   1388 C CG2 . THR   B 1 62  ? 14.440  23.719  26.798  1.00 10.78 ? 76  THR   B CG2 1 
ATOM   1389 N N   . VAL   B 1 63  ? 14.549  21.490  29.060  1.00 10.00 ? 77  VAL   B N   1 
ATOM   1390 C CA  . VAL   B 1 63  ? 15.778  21.310  29.833  1.00 11.47 ? 77  VAL   B CA  1 
ATOM   1391 C C   . VAL   B 1 63  ? 16.953  21.466  28.878  1.00 11.31 ? 77  VAL   B C   1 
ATOM   1392 O O   . VAL   B 1 63  ? 17.032  20.751  27.873  1.00 12.28 ? 77  VAL   B O   1 
ATOM   1393 C CB  . VAL   B 1 63  ? 15.837  19.923  30.502  1.00 12.43 ? 77  VAL   B CB  1 
ATOM   1394 C CG1 . VAL   B 1 63  ? 17.229  19.663  31.109  1.00 13.39 ? 77  VAL   B CG1 1 
ATOM   1395 C CG2 . VAL   B 1 63  ? 14.739  19.779  31.560  1.00 12.93 ? 77  VAL   B CG2 1 
ATOM   1396 N N   . ALA   B 1 64  ? 17.871  22.386  29.192  1.00 11.44 ? 78  ALA   B N   1 
ATOM   1397 C CA  . ALA   B 1 64  ? 19.183  22.397  28.552  1.00 12.19 ? 78  ALA   B CA  1 
ATOM   1398 C C   . ALA   B 1 64  ? 20.125  21.569  29.413  1.00 11.97 ? 78  ALA   B C   1 
ATOM   1399 O O   . ALA   B 1 64  ? 20.189  21.773  30.630  1.00 12.72 ? 78  ALA   B O   1 
ATOM   1400 C CB  . ALA   B 1 64  ? 19.722  23.821  28.403  1.00 12.88 ? 78  ALA   B CB  1 
ATOM   1401 N N   . TRP   B 1 65  ? 20.850  20.637  28.792  1.00 11.98 ? 79  TRP   B N   1 
ATOM   1402 C CA  . TRP   B 1 65  ? 21.573  19.609  29.537  1.00 12.73 ? 79  TRP   B CA  1 
ATOM   1403 C C   . TRP   B 1 65  ? 22.941  20.090  30.013  1.00 13.05 ? 79  TRP   B C   1 
ATOM   1404 O O   . TRP   B 1 65  ? 23.965  19.420  29.812  1.00 13.42 ? 79  TRP   B O   1 
ATOM   1405 C CB  . TRP   B 1 65  ? 21.649  18.305  28.728  1.00 13.07 ? 79  TRP   B CB  1 
ATOM   1406 C CG  . TRP   B 1 65  ? 20.283  17.735  28.469  1.00 12.31 ? 79  TRP   B CG  1 
ATOM   1407 C CD1 . TRP   B 1 65  ? 19.595  17.761  27.286  1.00 12.01 ? 79  TRP   B CD1 1 
ATOM   1408 C CD2 . TRP   B 1 65  ? 19.410  17.107  29.425  1.00 11.97 ? 79  TRP   B CD2 1 
ATOM   1409 N NE1 . TRP   B 1 65  ? 18.360  17.176  27.448  1.00 11.39 ? 79  TRP   B NE1 1 
ATOM   1410 C CE2 . TRP   B 1 65  ? 18.224  16.762  28.745  1.00 11.88 ? 79  TRP   B CE2 1 
ATOM   1411 C CE3 . TRP   B 1 65  ? 19.527  16.788  30.785  1.00 12.42 ? 79  TRP   B CE3 1 
ATOM   1412 C CZ2 . TRP   B 1 65  ? 17.156  16.121  29.375  1.00 12.65 ? 79  TRP   B CZ2 1 
ATOM   1413 C CZ3 . TRP   B 1 65  ? 18.467  16.148  31.416  1.00 13.11 ? 79  TRP   B CZ3 1 
ATOM   1414 C CH2 . TRP   B 1 65  ? 17.294  15.821  30.706  1.00 12.78 ? 79  TRP   B CH2 1 
ATOM   1415 N N   . LYS   B 1 66  ? 22.948  21.248  30.672  1.00 13.78 ? 80  LYS   B N   1 
ATOM   1416 C CA  . LYS   B 1 66  ? 24.122  21.809  31.327  1.00 14.15 ? 80  LYS   B CA  1 
ATOM   1417 C C   . LYS   B 1 66  ? 23.774  22.062  32.787  1.00 13.73 ? 80  LYS   B C   1 
ATOM   1418 O O   . LYS   B 1 66  ? 22.715  22.622  33.090  1.00 14.00 ? 80  LYS   B O   1 
ATOM   1419 C CB  . LYS   B 1 66  ? 24.537  23.140  30.688  1.00 15.71 ? 80  LYS   B CB  1 
ATOM   1420 C CG  . LYS   B 1 66  ? 25.671  23.844  31.435  1.00 17.20 ? 80  LYS   B CG  1 
ATOM   1421 C CD  . LYS   B 1 66  ? 25.953  25.244  30.894  1.00 19.93 ? 80  LYS   B CD  1 
ATOM   1422 C CE  . LYS   B 1 66  ? 26.931  26.023  31.780  1.00 23.71 ? 80  LYS   B CE  1 
ATOM   1423 N NZ  . LYS   B 1 66  ? 26.399  26.279  33.155  1.00 25.65 ? 80  LYS   B NZ  1 
ATOM   1424 N N   . ASN   B 1 67  ? 24.663  21.650  33.685  1.00 14.51 ? 81  ASN   B N   1 
ATOM   1425 C CA  . ASN   B 1 67  ? 24.587  22.046  35.087  1.00 15.24 ? 81  ASN   B CA  1 
ATOM   1426 C C   . ASN   B 1 67  ? 26.001  22.441  35.511  1.00 17.19 ? 81  ASN   B C   1 
ATOM   1427 O O   . ASN   B 1 67  ? 26.895  22.654  34.683  1.00 17.97 ? 81  ASN   B O   1 
ATOM   1428 C CB  . ASN   B 1 67  ? 23.897  20.989  35.956  1.00 15.23 ? 81  ASN   B CB  1 
ATOM   1429 C CG  . ASN   B 1 67  ? 24.626  19.667  35.958  1.00 15.19 ? 81  ASN   B CG  1 
ATOM   1430 O OD1 . ASN   B 1 67  ? 25.818  19.597  35.657  1.00 15.93 ? 81  ASN   B OD1 1 
ATOM   1431 N ND2 . ASN   B 1 67  ? 23.910  18.602  36.314  1.00 16.32 ? 81  ASN   B ND2 1 
ATOM   1432 N N   . ASN   B 1 68  ? 26.237  22.535  36.821  1.00 18.98 ? 82  ASN   B N   1 
ATOM   1433 C CA  . ASN   B 1 68  ? 27.552  22.968  37.289  1.00 21.65 ? 82  ASN   B CA  1 
ATOM   1434 C C   . ASN   B 1 68  ? 28.621  21.896  37.141  1.00 22.18 ? 82  ASN   B C   1 
ATOM   1435 O O   . ASN   B 1 68  ? 29.797  22.179  37.399  1.00 24.91 ? 82  ASN   B O   1 
ATOM   1436 C CB  . ASN   B 1 68  ? 27.487  23.411  38.755  1.00 24.62 ? 82  ASN   B CB  1 
ATOM   1437 C CG  . ASN   B 1 68  ? 26.696  24.691  38.950  1.00 28.31 ? 82  ASN   B CG  1 
ATOM   1438 O OD1 . ASN   B 1 68  ? 26.425  25.422  37.995  1.00 30.48 ? 82  ASN   B OD1 1 
ATOM   1439 N ND2 . ASN   B 1 68  ? 26.336  24.978  40.195  1.00 29.98 ? 82  ASN   B ND2 1 
ATOM   1440 N N   . TYR   B 1 69  ? 28.247  20.687  36.738  1.00 21.58 ? 83  TYR   B N   1 
ATOM   1441 C CA  . TYR   B 1 69  ? 29.149  19.545  36.704  1.00 22.20 ? 83  TYR   B CA  1 
ATOM   1442 C C   . TYR   B 1 69  ? 29.385  18.978  35.312  1.00 21.68 ? 83  TYR   B C   1 
ATOM   1443 O O   . TYR   B 1 69  ? 30.472  18.448  35.056  1.00 22.65 ? 83  TYR   B O   1 
ATOM   1444 C CB  . TYR   B 1 69  ? 28.591  18.420  37.588  1.00 23.25 ? 83  TYR   B CB  1 
ATOM   1445 C CG  . TYR   B 1 69  ? 28.185  18.879  38.976  1.00 25.08 ? 83  TYR   B CG  1 
ATOM   1446 C CD1 . TYR   B 1 69  ? 29.128  19.008  39.990  1.00 26.78 ? 83  TYR   B CD1 1 
ATOM   1447 C CD2 . TYR   B 1 69  ? 26.861  19.185  39.272  1.00 26.63 ? 83  TYR   B CD2 1 
ATOM   1448 C CE1 . TYR   B 1 69  ? 28.764  19.429  41.259  1.00 27.93 ? 83  TYR   B CE1 1 
ATOM   1449 C CE2 . TYR   B 1 69  ? 26.486  19.606  40.539  1.00 27.80 ? 83  TYR   B CE2 1 
ATOM   1450 C CZ  . TYR   B 1 69  ? 27.445  19.727  41.528  1.00 28.67 ? 83  TYR   B CZ  1 
ATOM   1451 O OH  . TYR   B 1 69  ? 27.095  20.143  42.796  1.00 30.45 ? 83  TYR   B OH  1 
ATOM   1452 N N   . ARG   B 1 70  ? 28.401  19.068  34.416  1.00 19.73 ? 84  ARG   B N   1 
ATOM   1453 C CA  . ARG   B 1 70  ? 28.441  18.411  33.116  1.00 19.46 ? 84  ARG   B CA  1 
ATOM   1454 C C   . ARG   B 1 70  ? 27.739  19.289  32.085  1.00 16.18 ? 84  ARG   B C   1 
ATOM   1455 O O   . ARG   B 1 70  ? 26.969  20.192  32.429  1.00 16.14 ? 84  ARG   B O   1 
ATOM   1456 C CB  . ARG   B 1 70  ? 27.719  17.054  33.143  1.00 24.41 ? 84  ARG   B CB  1 
ATOM   1457 C CG  . ARG   B 1 70  ? 28.118  16.110  34.261  1.00 29.56 ? 84  ARG   B CG  1 
ATOM   1458 C CD  . ARG   B 1 70  ? 27.522  14.730  34.034  1.00 33.60 ? 84  ARG   B CD  1 
ATOM   1459 N NE  . ARG   B 1 70  ? 27.981  13.771  35.031  1.00 36.82 ? 84  ARG   B NE  1 
ATOM   1460 C CZ  . ARG   B 1 70  ? 27.206  13.208  35.948  1.00 39.03 ? 84  ARG   B CZ  1 
ATOM   1461 N NH1 . ARG   B 1 70  ? 25.906  13.452  35.999  1.00 39.81 ? 84  ARG   B NH1 1 
ATOM   1462 N NH2 . ARG   B 1 70  ? 27.747  12.377  36.833  1.00 40.01 ? 84  ARG   B NH2 1 
ATOM   1463 N N   . ASN   B 1 71  ? 27.992  18.999  30.806  1.00 14.77 ? 85  ASN   B N   1 
ATOM   1464 C CA  . ASN   B 1 71  ? 27.326  19.729  29.725  1.00 14.37 ? 85  ASN   B CA  1 
ATOM   1465 C C   . ASN   B 1 71  ? 27.326  18.862  28.471  1.00 14.55 ? 85  ASN   B C   1 
ATOM   1466 O O   . ASN   B 1 71  ? 28.386  18.617  27.887  1.00 15.68 ? 85  ASN   B O   1 
ATOM   1467 C CB  . ASN   B 1 71  ? 28.020  21.067  29.477  1.00 14.14 ? 85  ASN   B CB  1 
ATOM   1468 C CG  . ASN   B 1 71  ? 27.236  21.963  28.539  1.00 13.41 ? 85  ASN   B CG  1 
ATOM   1469 O OD1 . ASN   B 1 71  ? 26.255  21.534  27.930  1.00 14.83 ? 85  ASN   B OD1 1 
ATOM   1470 N ND2 . ASN   B 1 71  ? 27.666  23.211  28.411  1.00 14.58 ? 85  ASN   B ND2 1 
ATOM   1471 N N   . ALA   B 1 72  ? 26.141  18.407  28.063  1.00 14.42 ? 86  ALA   B N   1 
ATOM   1472 C CA  . ALA   B 1 72  ? 25.958  17.591  26.866  1.00 13.85 ? 86  ALA   B CA  1 
ATOM   1473 C C   . ALA   B 1 72  ? 25.789  18.412  25.588  1.00 13.42 ? 86  ALA   B C   1 
ATOM   1474 O O   . ALA   B 1 72  ? 25.673  17.825  24.504  1.00 15.25 ? 86  ALA   B O   1 
ATOM   1475 C CB  . ALA   B 1 72  ? 24.756  16.653  27.045  1.00 15.36 ? 86  ALA   B CB  1 
ATOM   1476 N N   . HIS   B 1 73  ? 25.778  19.742  25.680  1.00 14.00 ? 87  HIS   B N   1 
ATOM   1477 C CA  . HIS   B 1 73  ? 25.575  20.620  24.528  1.00 12.82 ? 87  HIS   B CA  1 
ATOM   1478 C C   . HIS   B 1 73  ? 24.329  20.205  23.741  1.00 12.55 ? 87  HIS   B C   1 
ATOM   1479 O O   . HIS   B 1 73  ? 24.382  19.911  22.543  1.00 13.41 ? 87  HIS   B O   1 
ATOM   1480 C CB  . HIS   B 1 73  ? 26.825  20.665  23.636  1.00 13.98 ? 87  HIS   B CB  1 
ATOM   1481 C CG  . HIS   B 1 73  ? 28.069  21.104  24.355  1.00 14.09 ? 87  HIS   B CG  1 
ATOM   1482 N ND1 . HIS   B 1 73  ? 28.127  22.241  25.135  1.00 14.20 ? 87  HIS   B ND1 1 
ATOM   1483 C CD2 . HIS   B 1 73  ? 29.302  20.547  24.416  1.00 14.79 ? 87  HIS   B CD2 1 
ATOM   1484 C CE1 . HIS   B 1 73  ? 29.341  22.367  25.643  1.00 15.18 ? 87  HIS   B CE1 1 
ATOM   1485 N NE2 . HIS   B 1 73  ? 30.077  21.354  25.217  1.00 14.86 ? 87  HIS   B NE2 1 
ATOM   1486 N N   . SER   B 1 74  ? 23.200  20.160  24.450  1.00 12.39 ? 88  SER   B N   1 
ATOM   1487 C CA  . SER   B 1 74  ? 21.939  19.702  23.872  1.00 12.63 ? 88  SER   B CA  1 
ATOM   1488 C C   . SER   B 1 74  ? 20.796  20.173  24.763  1.00 11.77 ? 88  SER   B C   1 
ATOM   1489 O O   . SER   B 1 74  ? 21.010  20.614  25.895  1.00 12.48 ? 88  SER   B O   1 
ATOM   1490 C CB  . SER   B 1 74  ? 21.912  18.181  23.740  1.00 14.23 ? 88  SER   B CB  1 
ATOM   1491 O OG  . SER   B 1 74  ? 21.995  17.599  25.026  1.00 14.82 ? 88  SER   B OG  1 
ATOM   1492 N N   . ALA   B 1 75  ? 19.571  20.065  24.248  1.00 10.77 ? 89  ALA   B N   1 
ATOM   1493 C CA  . ALA   B 1 75  ? 18.397  20.502  24.996  1.00 10.81 ? 89  ALA   B CA  1 
ATOM   1494 C C   . ALA   B 1 75  ? 17.184  19.700  24.541  1.00 10.51 ? 89  ALA   B C   1 
ATOM   1495 O O   . ALA   B 1 75  ? 17.026  19.430  23.344  1.00 11.32 ? 89  ALA   B O   1 
ATOM   1496 C CB  . ALA   B 1 75  ? 18.138  22.002  24.799  1.00 12.55 ? 89  ALA   B CB  1 
ATOM   1497 N N   . THR   B 1 76  ? 16.325  19.331  25.491  1.00 10.09 ? 90  THR   B N   1 
ATOM   1498 C CA  . THR   B 1 76  ? 15.084  18.623  25.202  1.00 9.70  ? 90  THR   B CA  1 
ATOM   1499 C C   . THR   B 1 76  ? 13.887  19.529  25.478  1.00 10.35 ? 90  THR   B C   1 
ATOM   1500 O O   . THR   B 1 76  ? 13.854  20.234  26.496  1.00 10.35 ? 90  THR   B O   1 
ATOM   1501 C CB  . THR   B 1 76  ? 14.954  17.367  26.079  1.00 10.41 ? 90  THR   B CB  1 
ATOM   1502 O OG1 . THR   B 1 76  ? 16.065  16.493  25.838  1.00 10.82 ? 90  THR   B OG1 1 
ATOM   1503 C CG2 . THR   B 1 76  ? 13.644  16.620  25.810  1.00 11.01 ? 90  THR   B CG2 1 
ATOM   1504 N N   . THR   B 1 77  ? 12.887  19.493  24.591  1.00 9.49  ? 91  THR   B N   1 
ATOM   1505 C CA  . THR   B 1 77  ? 11.580  20.086  24.860  1.00 9.75  ? 91  THR   B CA  1 
ATOM   1506 C C   . THR   B 1 77  ? 10.535  18.984  24.903  1.00 9.58  ? 91  THR   B C   1 
ATOM   1507 O O   . THR   B 1 77  ? 10.509  18.117  24.020  1.00 11.84 ? 91  THR   B O   1 
ATOM   1508 C CB  . THR   B 1 77  ? 11.159  21.129  23.808  1.00 10.13 ? 91  THR   B CB  1 
ATOM   1509 O OG1 . THR   B 1 77  ? 11.040  20.508  22.518  1.00 11.17 ? 91  THR   B OG1 1 
ATOM   1510 C CG2 . THR   B 1 77  ? 12.163  22.268  23.719  1.00 11.81 ? 91  THR   B CG2 1 
ATOM   1511 N N   . TRP   B 1 78  ? 9.666   19.032  25.910  1.00 9.00  ? 92  TRP   B N   1 
ATOM   1512 C CA  . TRP   B 1 78  ? 8.514   18.143  26.022  1.00 9.35  ? 92  TRP   B CA  1 
ATOM   1513 C C   . TRP   B 1 78  ? 7.254   18.958  25.757  1.00 8.96  ? 92  TRP   B C   1 
ATOM   1514 O O   . TRP   B 1 78  ? 7.077   20.033  26.351  1.00 9.32  ? 92  TRP   B O   1 
ATOM   1515 C CB  . TRP   B 1 78  ? 8.409   17.559  27.432  1.00 9.94  ? 92  TRP   B CB  1 
ATOM   1516 C CG  . TRP   B 1 78  ? 9.452   16.563  27.866  1.00 9.53  ? 92  TRP   B CG  1 
ATOM   1517 C CD1 . TRP   B 1 78  ? 9.295   15.209  27.940  1.00 10.36 ? 92  TRP   B CD1 1 
ATOM   1518 C CD2 . TRP   B 1 78  ? 10.769  16.843  28.369  1.00 9.96  ? 92  TRP   B CD2 1 
ATOM   1519 N NE1 . TRP   B 1 78  ? 10.431  14.627  28.452  1.00 10.18 ? 92  TRP   B NE1 1 
ATOM   1520 C CE2 . TRP   B 1 78  ? 11.352  15.605  28.724  1.00 10.28 ? 92  TRP   B CE2 1 
ATOM   1521 C CE3 . TRP   B 1 78  ? 11.514  18.017  28.544  1.00 10.46 ? 92  TRP   B CE3 1 
ATOM   1522 C CZ2 . TRP   B 1 78  ? 12.641  15.506  29.273  1.00 10.36 ? 92  TRP   B CZ2 1 
ATOM   1523 C CZ3 . TRP   B 1 78  ? 12.795  17.919  29.092  1.00 10.88 ? 92  TRP   B CZ3 1 
ATOM   1524 C CH2 . TRP   B 1 78  ? 13.343  16.673  29.445  1.00 10.77 ? 92  TRP   B CH2 1 
ATOM   1525 N N   . SER   B 1 79  ? 6.384   18.447  24.880  1.00 8.59  ? 93  SER   B N   1 
ATOM   1526 C CA  . SER   B 1 79  ? 5.110   19.075  24.539  1.00 8.90  ? 93  SER   B CA  1 
ATOM   1527 C C   . SER   B 1 79  ? 3.995   18.070  24.825  1.00 9.21  ? 93  SER   B C   1 
ATOM   1528 O O   . SER   B 1 79  ? 4.079   16.916  24.395  1.00 9.62  ? 93  SER   B O   1 
ATOM   1529 C CB  . SER   B 1 79  ? 5.120   19.449  23.048  1.00 10.51 ? 93  SER   B CB  1 
ATOM   1530 O OG  . SER   B 1 79  ? 3.899   20.062  22.659  1.00 11.69 ? 93  SER   B OG  1 
ATOM   1531 N N   . GLY   B 1 80  ? 2.964   18.464  25.565  1.00 8.93  ? 94  GLY   B N   1 
ATOM   1532 C CA  . GLY   B 1 80  ? 1.963   17.474  25.902  1.00 9.75  ? 94  GLY   B CA  1 
ATOM   1533 C C   . GLY   B 1 80  ? 0.778   18.034  26.646  1.00 9.12  ? 94  GLY   B C   1 
ATOM   1534 O O   . GLY   B 1 80  ? 0.465   19.221  26.554  1.00 10.04 ? 94  GLY   B O   1 
ATOM   1535 N N   . GLN   B 1 81  ? 0.104   17.143  27.372  1.00 10.17 ? 95  GLN   B N   1 
ATOM   1536 C CA  . GLN   B 1 81  ? -1.053  17.540  28.154  1.00 10.94 ? 95  GLN   B CA  1 
ATOM   1537 C C   . GLN   B 1 81  ? -1.138  16.769  29.463  1.00 10.72 ? 95  GLN   B C   1 
ATOM   1538 O O   . GLN   B 1 81  ? -0.789  15.583  29.529  1.00 11.21 ? 95  GLN   B O   1 
ATOM   1539 C CB  . GLN   B 1 81  ? -2.368  17.445  27.360  1.00 13.99 ? 95  GLN   B CB  1 
ATOM   1540 C CG  . GLN   B 1 81  ? -2.711  16.099  26.754  1.00 14.76 ? 95  GLN   B CG  1 
ATOM   1541 C CD  . GLN   B 1 81  ? -4.006  16.162  25.925  1.00 13.28 ? 95  GLN   B CD  1 
ATOM   1542 O OE1 . GLN   B 1 81  ? -4.992  16.783  26.345  1.00 13.02 ? 95  GLN   B OE1 1 
ATOM   1543 N NE2 . GLN   B 1 81  ? -4.000  15.536  24.746  1.00 13.98 ? 95  GLN   B NE2 1 
ATOM   1544 N N   . TYR   B 1 82  ? -1.593  17.474  30.502  1.00 11.09 ? 96  TYR   B N   1 
ATOM   1545 C CA  . TYR   B 1 82  ? -1.900  16.885  31.799  1.00 11.31 ? 96  TYR   B CA  1 
ATOM   1546 C C   . TYR   B 1 82  ? -3.329  16.362  31.781  1.00 12.05 ? 96  TYR   B C   1 
ATOM   1547 O O   . TYR   B 1 82  ? -4.249  17.060  31.337  1.00 13.17 ? 96  TYR   B O   1 
ATOM   1548 C CB  . TYR   B 1 82  ? -1.731  17.935  32.903  1.00 12.34 ? 96  TYR   B CB  1 
ATOM   1549 C CG  . TYR   B 1 82  ? -2.459  17.610  34.193  1.00 12.69 ? 96  TYR   B CG  1 
ATOM   1550 C CD1 . TYR   B 1 82  ? -1.895  16.759  35.145  1.00 13.30 ? 96  TYR   B CD1 1 
ATOM   1551 C CD2 . TYR   B 1 82  ? -3.707  18.159  34.462  1.00 15.01 ? 96  TYR   B CD2 1 
ATOM   1552 C CE1 . TYR   B 1 82  ? -2.556  16.464  36.326  1.00 15.97 ? 96  TYR   B CE1 1 
ATOM   1553 C CE2 . TYR   B 1 82  ? -4.374  17.863  35.635  1.00 16.28 ? 96  TYR   B CE2 1 
ATOM   1554 C CZ  . TYR   B 1 82  ? -3.794  17.012  36.557  1.00 16.22 ? 96  TYR   B CZ  1 
ATOM   1555 O OH  . TYR   B 1 82  ? -4.442  16.719  37.736  1.00 19.58 ? 96  TYR   B OH  1 
ATOM   1556 N N   . VAL   B 1 83  ? -3.508  15.134  32.265  1.00 13.31 ? 97  VAL   B N   1 
ATOM   1557 C CA  . VAL   B 1 83  ? -4.805  14.475  32.332  1.00 16.31 ? 97  VAL   B CA  1 
ATOM   1558 C C   . VAL   B 1 83  ? -5.028  14.099  33.789  1.00 18.51 ? 97  VAL   B C   1 
ATOM   1559 O O   . VAL   B 1 83  ? -4.322  13.236  34.324  1.00 19.91 ? 97  VAL   B O   1 
ATOM   1560 C CB  . VAL   B 1 83  ? -4.863  13.236  31.427  1.00 18.65 ? 97  VAL   B CB  1 
ATOM   1561 C CG1 . VAL   B 1 83  ? -6.208  12.543  31.546  1.00 20.86 ? 97  VAL   B CG1 1 
ATOM   1562 C CG2 . VAL   B 1 83  ? -4.596  13.631  29.983  1.00 19.41 ? 97  VAL   B CG2 1 
ATOM   1563 N N   . GLY   B 1 84  ? -5.995  14.748  34.438  1.00 20.36 ? 98  GLY   B N   1 
ATOM   1564 C CA  . GLY   B 1 84  ? -6.260  14.501  35.837  1.00 23.73 ? 98  GLY   B CA  1 
ATOM   1565 C C   . GLY   B 1 84  ? -7.088  13.250  36.069  1.00 27.21 ? 98  GLY   B C   1 
ATOM   1566 O O   . GLY   B 1 84  ? -7.497  12.546  35.146  1.00 29.35 ? 98  GLY   B O   1 
ATOM   1567 N N   . GLY   B 1 85  ? -7.332  12.971  37.346  1.00 29.76 ? 99  GLY   B N   1 
ATOM   1568 C CA  . GLY   B 1 85  ? -8.164  11.863  37.760  1.00 30.60 ? 99  GLY   B CA  1 
ATOM   1569 C C   . GLY   B 1 85  ? -7.427  10.949  38.710  1.00 30.35 ? 99  GLY   B C   1 
ATOM   1570 O O   . GLY   B 1 85  ? -6.340  11.267  39.204  1.00 30.98 ? 99  GLY   B O   1 
ATOM   1571 N N   . ALA   B 1 86  ? -8.033  9.784   38.964  1.00 31.26 ? 100 ALA   B N   1 
ATOM   1572 C CA  . ALA   B 1 86  ? -7.485  8.846   39.941  1.00 32.05 ? 100 ALA   B CA  1 
ATOM   1573 C C   . ALA   B 1 86  ? -6.115  8.327   39.528  1.00 31.80 ? 100 ALA   B C   1 
ATOM   1574 O O   . ALA   B 1 86  ? -5.278  8.032   40.389  1.00 33.05 ? 100 ALA   B O   1 
ATOM   1575 C CB  . ALA   B 1 86  ? -8.452  7.680   40.146  1.00 32.39 ? 100 ALA   B CB  1 
ATOM   1576 N N   . GLU   B 1 87  ? -5.872  8.206   38.228  1.00 30.16 ? 101 GLU   B N   1 
ATOM   1577 C CA  . GLU   B 1 87  ? -4.585  7.791   37.681  1.00 28.51 ? 101 GLU   B CA  1 
ATOM   1578 C C   . GLU   B 1 87  ? -4.092  8.905   36.758  1.00 24.68 ? 101 GLU   B C   1 
ATOM   1579 O O   . GLU   B 1 87  ? -4.070  8.772   35.528  1.00 24.93 ? 101 GLU   B O   1 
ATOM   1580 C CB  . GLU   B 1 87  ? -4.699  6.436   36.969  1.00 30.19 ? 101 GLU   B CB  1 
ATOM   1581 C CG  . GLU   B 1 87  ? -5.040  5.283   37.909  0.55 31.27 ? 101 GLU   B CG  1 
ATOM   1582 C CD  . GLU   B 1 87  ? -5.042  3.939   37.209  0.68 31.79 ? 101 GLU   B CD  1 
ATOM   1583 O OE1 . GLU   B 1 87  ? -4.907  3.913   35.968  0.31 32.12 ? 101 GLU   B OE1 1 
ATOM   1584 O OE2 . GLU   B 1 87  ? -5.176  2.907   37.900  0.20 31.91 ? 101 GLU   B OE2 1 
ATOM   1585 N N   . ALA   B 1 88  ? -3.707  10.018  37.372  1.00 20.67 ? 102 ALA   B N   1 
ATOM   1586 C CA  . ALA   B 1 88  ? -3.321  11.212  36.635  1.00 16.95 ? 102 ALA   B CA  1 
ATOM   1587 C C   . ALA   B 1 88  ? -2.050  10.965  35.827  1.00 16.11 ? 102 ALA   B C   1 
ATOM   1588 O O   . ALA   B 1 88  ? -1.195  10.158  36.203  1.00 17.09 ? 102 ALA   B O   1 
ATOM   1589 C CB  . ALA   B 1 88  ? -3.082  12.364  37.610  1.00 17.82 ? 102 ALA   B CB  1 
ATOM   1590 N N   . ARG   B 1 89  ? -1.933  11.665  34.699  1.00 14.00 ? 103 ARG   B N   1 
ATOM   1591 C CA  . ARG   B 1 89  ? -0.803  11.474  33.802  1.00 13.97 ? 103 ARG   B CA  1 
ATOM   1592 C C   . ARG   B 1 89  ? -0.414  12.806  33.184  1.00 11.87 ? 103 ARG   B C   1 
ATOM   1593 O O   . ARG   B 1 89  ? -1.253  13.689  33.003  1.00 13.43 ? 103 ARG   B O   1 
ATOM   1594 C CB  . ARG   B 1 89  ? -1.184  10.557  32.623  1.00 17.84 ? 103 ARG   B CB  1 
ATOM   1595 C CG  . ARG   B 1 89  ? -1.585  9.154   32.997  1.00 20.87 ? 103 ARG   B CG  1 
ATOM   1596 C CD  . ARG   B 1 89  ? -0.368  8.309   33.268  1.00 24.16 ? 103 ARG   B CD  1 
ATOM   1597 N NE  . ARG   B 1 89  ? -0.717  6.906   33.463  1.00 26.17 ? 103 ARG   B NE  1 
ATOM   1598 C CZ  . ARG   B 1 89  ? -1.172  6.401   34.603  1.00 27.82 ? 103 ARG   B CZ  1 
ATOM   1599 N NH1 . ARG   B 1 89  ? -1.368  7.163   35.667  1.00 27.65 ? 103 ARG   B NH1 1 
ATOM   1600 N NH2 . ARG   B 1 89  ? -1.437  5.099   34.678  1.00 29.50 ? 103 ARG   B NH2 1 
ATOM   1601 N N   . ILE   B 1 90  ? 0.860   12.929  32.813  1.00 11.34 ? 104 ILE   B N   1 
ATOM   1602 C CA  . ILE   B 1 90  ? 1.287   13.941  31.841  1.00 10.57 ? 104 ILE   B CA  1 
ATOM   1603 C C   . ILE   B 1 90  ? 1.816   13.180  30.629  1.00 10.48 ? 104 ILE   B C   1 
ATOM   1604 O O   . ILE   B 1 90  ? 2.819   12.462  30.730  1.00 11.62 ? 104 ILE   B O   1 
ATOM   1605 C CB  . ILE   B 1 90  ? 2.330   14.927  32.399  1.00 11.33 ? 104 ILE   B CB  1 
ATOM   1606 C CG1 . ILE   B 1 90  ? 1.774   15.632  33.644  1.00 12.08 ? 104 ILE   B CG1 1 
ATOM   1607 C CG2 . ILE   B 1 90  ? 2.718   15.958  31.319  1.00 13.35 ? 104 ILE   B CG2 1 
ATOM   1608 C CD1 . ILE   B 1 90  ? 2.767   16.570  34.346  1.00 13.62 ? 104 ILE   B CD1 1 
ATOM   1609 N N   . ASN   B 1 91  ? 1.125   13.305  29.491  1.00 10.68 ? 105 ASN   B N   1 
ATOM   1610 C CA  . ASN   B 1 91  ? 1.445   12.560  28.275  1.00 11.00 ? 105 ASN   B CA  1 
ATOM   1611 C C   . ASN   B 1 91  ? 2.157   13.501  27.317  1.00 10.01 ? 105 ASN   B C   1 
ATOM   1612 O O   . ASN   B 1 91  ? 1.602   14.548  26.960  1.00 10.40 ? 105 ASN   B O   1 
ATOM   1613 C CB  . ASN   B 1 91  ? 0.153   12.042  27.645  1.00 13.33 ? 105 ASN   B CB  1 
ATOM   1614 C CG  . ASN   B 1 91  ? -0.571  11.073  28.558  1.00 16.29 ? 105 ASN   B CG  1 
ATOM   1615 O OD1 . ASN   B 1 91  ? 0.063   10.235  29.205  1.00 17.04 ? 105 ASN   B OD1 1 
ATOM   1616 N ND2 . ASN   B 1 91  ? -1.891  11.198  28.647  1.00 17.26 ? 105 ASN   B ND2 1 
ATOM   1617 N N   . THR   B 1 92  ? 3.382   13.142  26.914  1.00 9.89  ? 106 THR   B N   1 
ATOM   1618 C CA  . THR   B 1 92  ? 4.226   14.050  26.143  1.00 9.69  ? 106 THR   B CA  1 
ATOM   1619 C C   . THR   B 1 92  ? 4.854   13.378  24.927  1.00 9.28  ? 106 THR   B C   1 
ATOM   1620 O O   . THR   B 1 92  ? 5.038   12.154  24.868  1.00 10.16 ? 106 THR   B O   1 
ATOM   1621 C CB  . THR   B 1 92  ? 5.377   14.657  26.984  1.00 9.98  ? 106 THR   B CB  1 
ATOM   1622 O OG1 . THR   B 1 92  ? 6.373   13.657  27.242  1.00 10.47 ? 106 THR   B OG1 1 
ATOM   1623 C CG2 . THR   B 1 92  ? 4.870   15.264  28.302  1.00 11.21 ? 106 THR   B CG2 1 
ATOM   1624 N N   . GLN   B 1 93  ? 5.205   14.225  23.962  1.00 9.04  ? 107 GLN   B N   1 
ATOM   1625 C CA  . GLN   B 1 93  ? 6.184   13.910  22.932  1.00 9.76  ? 107 GLN   B CA  1 
ATOM   1626 C C   . GLN   B 1 93  ? 7.321   14.915  23.078  1.00 9.29  ? 107 GLN   B C   1 
ATOM   1627 O O   . GLN   B 1 93  ? 7.115   16.031  23.577  1.00 10.73 ? 107 GLN   B O   1 
ATOM   1628 C CB  . GLN   B 1 93  ? 5.541   13.943  21.536  1.00 10.48 ? 107 GLN   B CB  1 
ATOM   1629 C CG  . GLN   B 1 93  ? 4.376   12.953  21.477  1.00 12.12 ? 107 GLN   B CG  1 
ATOM   1630 C CD  . GLN   B 1 93  ? 3.793   12.799  20.093  1.00 12.92 ? 107 GLN   B CD  1 
ATOM   1631 O OE1 . GLN   B 1 93  ? 4.337   12.080  19.255  1.00 14.80 ? 107 GLN   B OE1 1 
ATOM   1632 N NE2 . GLN   B 1 93  ? 2.672   13.465  19.841  1.00 12.92 ? 107 GLN   B NE2 1 
ATOM   1633 N N   . TRP   B 1 94  ? 8.536   14.511  22.702  1.00 9.31  ? 108 TRP   B N   1 
ATOM   1634 C CA  . TRP   B 1 94  ? 9.709   15.340  22.942  1.00 9.35  ? 108 TRP   B CA  1 
ATOM   1635 C C   . TRP   B 1 94  ? 10.622  15.418  21.721  1.00 8.92  ? 108 TRP   B C   1 
ATOM   1636 O O   . TRP   B 1 94  ? 10.638  14.528  20.863  1.00 10.01 ? 108 TRP   B O   1 
ATOM   1637 C CB  . TRP   B 1 94  ? 10.483  14.905  24.205  1.00 9.90  ? 108 TRP   B CB  1 
ATOM   1638 C CG  . TRP   B 1 94  ? 10.903  13.472  24.279  1.00 10.05 ? 108 TRP   B CG  1 
ATOM   1639 C CD1 . TRP   B 1 94  ? 10.321  12.489  25.033  1.00 11.10 ? 108 TRP   B CD1 1 
ATOM   1640 C CD2 . TRP   B 1 94  ? 12.030  12.855  23.622  1.00 9.91  ? 108 TRP   B CD2 1 
ATOM   1641 N NE1 . TRP   B 1 94  ? 11.003  11.301  24.878  1.00 10.87 ? 108 TRP   B NE1 1 
ATOM   1642 C CE2 . TRP   B 1 94  ? 12.054  11.500  24.020  1.00 10.76 ? 108 TRP   B CE2 1 
ATOM   1643 C CE3 . TRP   B 1 94  ? 13.023  13.319  22.746  1.00 10.13 ? 108 TRP   B CE3 1 
ATOM   1644 C CZ2 . TRP   B 1 94  ? 13.016  10.607  23.562  1.00 10.92 ? 108 TRP   B CZ2 1 
ATOM   1645 C CZ3 . TRP   B 1 94  ? 13.983  12.424  22.291  1.00 10.86 ? 108 TRP   B CZ3 1 
ATOM   1646 C CH2 . TRP   B 1 94  ? 13.970  11.085  22.698  1.00 11.13 ? 108 TRP   B CH2 1 
ATOM   1647 N N   . LEU   B 1 95  ? 11.408  16.502  21.693  1.00 9.43  ? 109 LEU   B N   1 
ATOM   1648 C CA  . LEU   B 1 95  ? 12.453  16.733  20.702  1.00 9.80  ? 109 LEU   B CA  1 
ATOM   1649 C C   . LEU   B 1 95  ? 13.744  17.060  21.440  1.00 10.47 ? 109 LEU   B C   1 
ATOM   1650 O O   . LEU   B 1 95  ? 13.750  17.920  22.329  1.00 13.05 ? 109 LEU   B O   1 
ATOM   1651 C CB  . LEU   B 1 95  ? 12.093  17.923  19.815  1.00 10.61 ? 109 LEU   B CB  1 
ATOM   1652 C CG  . LEU   B 1 95  ? 10.876  17.783  18.903  1.00 11.22 ? 109 LEU   B CG  1 
ATOM   1653 C CD1 . LEU   B 1 95  ? 10.513  19.132  18.287  1.00 12.04 ? 109 LEU   B CD1 1 
ATOM   1654 C CD2 . LEU   B 1 95  ? 11.130  16.741  17.813  1.00 13.29 ? 109 LEU   B CD2 1 
ATOM   1655 N N   . LEU   B 1 96  ? 14.834  16.386  21.076  1.00 10.30 ? 110 LEU   B N   1 
ATOM   1656 C CA  . LEU   B 1 96  ? 16.142  16.577  21.704  1.00 10.80 ? 110 LEU   B CA  1 
ATOM   1657 C C   . LEU   B 1 96  ? 17.130  17.014  20.622  1.00 9.83  ? 110 LEU   B C   1 
ATOM   1658 O O   . LEU   B 1 96  ? 17.533  16.206  19.771  1.00 10.59 ? 110 LEU   B O   1 
ATOM   1659 C CB  . LEU   B 1 96  ? 16.574  15.281  22.395  1.00 11.57 ? 110 LEU   B CB  1 
ATOM   1660 C CG  . LEU   B 1 96  ? 18.028  15.085  22.820  1.00 12.61 ? 110 LEU   B CG  1 
ATOM   1661 C CD1 . LEU   B 1 96  ? 18.554  16.259  23.606  1.00 13.72 ? 110 LEU   B CD1 1 
ATOM   1662 C CD2 . LEU   B 1 96  ? 18.153  13.821  23.657  1.00 13.63 ? 110 LEU   B CD2 1 
ATOM   1663 N N   . THR   B 1 97  ? 17.515  18.292  20.641  1.00 10.86 ? 111 THR   B N   1 
ATOM   1664 C CA  . THR   B 1 97  ? 18.430  18.844  19.642  1.00 11.34 ? 111 THR   B CA  1 
ATOM   1665 C C   . THR   B 1 97  ? 19.813  19.020  20.251  1.00 11.73 ? 111 THR   B C   1 
ATOM   1666 O O   . THR   B 1 97  ? 19.949  19.573  21.352  1.00 12.59 ? 111 THR   B O   1 
ATOM   1667 C CB  . THR   B 1 97  ? 17.937  20.187  19.080  1.00 11.98 ? 111 THR   B CB  1 
ATOM   1668 O OG1 . THR   B 1 97  ? 16.600  20.058  18.580  1.00 12.85 ? 111 THR   B OG1 1 
ATOM   1669 C CG2 . THR   B 1 97  ? 18.831  20.639  17.919  1.00 13.83 ? 111 THR   B CG2 1 
ATOM   1670 N N   . SER   B 1 98  ? 20.830  18.538  19.543  1.00 12.20 ? 112 SER   B N   1 
ATOM   1671 C CA  . SER   B 1 98  ? 22.219  18.755  19.908  1.00 13.54 ? 112 SER   B CA  1 
ATOM   1672 C C   . SER   B 1 98  ? 22.802  19.909  19.104  1.00 14.23 ? 112 SER   B C   1 
ATOM   1673 O O   . SER   B 1 98  ? 22.431  20.127  17.949  1.00 14.79 ? 112 SER   B O   1 
ATOM   1674 C CB  . SER   B 1 98  ? 23.035  17.496  19.608  1.00 14.88 ? 112 SER   B CB  1 
ATOM   1675 O OG  . SER   B 1 98  ? 22.656  16.435  20.462  1.00 15.94 ? 112 SER   B OG  1 
ATOM   1676 N N   . GLY   B 1 99  ? 23.732  20.640  19.717  1.00 14.61 ? 113 GLY   B N   1 
ATOM   1677 C CA  . GLY   B 1 99  ? 24.532  21.588  18.954  1.00 15.74 ? 113 GLY   B CA  1 
ATOM   1678 C C   . GLY   B 1 99  ? 25.492  20.840  18.042  1.00 16.89 ? 113 GLY   B C   1 
ATOM   1679 O O   . GLY   B 1 99  ? 26.249  19.973  18.494  1.00 17.68 ? 113 GLY   B O   1 
ATOM   1680 N N   . THR   B 1 100 ? 25.454  21.157  16.746  1.00 16.65 ? 114 THR   B N   1 
ATOM   1681 C CA  . THR   B 1 100 ? 26.257  20.448  15.754  1.00 16.76 ? 114 THR   B CA  1 
ATOM   1682 C C   . THR   B 1 100 ? 26.887  21.449  14.795  1.00 17.42 ? 114 THR   B C   1 
ATOM   1683 O O   . THR   B 1 100 ? 26.531  22.626  14.767  1.00 17.62 ? 114 THR   B O   1 
ATOM   1684 C CB  . THR   B 1 100 ? 25.417  19.456  14.927  1.00 17.01 ? 114 THR   B CB  1 
ATOM   1685 O OG1 . THR   B 1 100 ? 24.520  20.178  14.073  1.00 17.43 ? 114 THR   B OG1 1 
ATOM   1686 C CG2 . THR   B 1 100 ? 24.622  18.498  15.809  1.00 18.63 ? 114 THR   B CG2 1 
ATOM   1687 N N   . THR   B 1 101 ? 27.812  20.955  13.971  1.00 18.36 ? 115 THR   B N   1 
ATOM   1688 C CA  . THR   B 1 101 ? 28.218  21.705  12.792  1.00 19.51 ? 115 THR   B CA  1 
ATOM   1689 C C   . THR   B 1 101 ? 27.104  21.657  11.750  1.00 19.50 ? 115 THR   B C   1 
ATOM   1690 O O   . THR   B 1 101 ? 26.186  20.840  11.821  1.00 18.61 ? 115 THR   B O   1 
ATOM   1691 C CB  . THR   B 1 101 ? 29.461  21.082  12.162  1.00 21.42 ? 115 THR   B CB  1 
ATOM   1692 O OG1 . THR   B 1 101 ? 29.133  19.764  11.714  1.00 21.69 ? 115 THR   B OG1 1 
ATOM   1693 C CG2 . THR   B 1 101 ? 30.607  21.020  13.166  1.00 22.01 ? 115 THR   B CG2 1 
ATOM   1694 N N   . GLU   B 1 102 ? 27.203  22.533  10.749  1.00 21.60 ? 116 GLU   B N   1 
ATOM   1695 C CA  A GLU   B 1 102 ? 26.209  22.531  9.681   0.26 22.26 ? 116 GLU   B CA  1 
ATOM   1696 C CA  B GLU   B 1 102 ? 26.209  22.531  9.681   0.74 23.02 ? 116 GLU   B CA  1 
ATOM   1697 C C   . GLU   B 1 102 ? 26.201  21.202  8.936   1.00 21.75 ? 116 GLU   B C   1 
ATOM   1698 O O   . GLU   B 1 102 ? 25.137  20.699  8.563   1.00 21.04 ? 116 GLU   B O   1 
ATOM   1699 C CB  A GLU   B 1 102 ? 26.452  23.698  8.724   0.26 23.38 ? 116 GLU   B CB  1 
ATOM   1700 C CB  B GLU   B 1 102 ? 26.451  23.695  8.717   0.74 25.76 ? 116 GLU   B CB  1 
ATOM   1701 C CG  A GLU   B 1 102 ? 26.095  25.057  9.305   0.26 24.68 ? 116 GLU   B CG  1 
ATOM   1702 C CG  B GLU   B 1 102 ? 25.431  23.775  7.585   0.74 28.73 ? 116 GLU   B CG  1 
ATOM   1703 C CD  A GLU   B 1 102 ? 24.609  25.206  9.576   0.26 25.81 ? 116 GLU   B CD  1 
ATOM   1704 C CD  B GLU   B 1 102 ? 24.003  23.897  8.091   0.74 31.68 ? 116 GLU   B CD  1 
ATOM   1705 O OE1 A GLU   B 1 102 ? 23.803  24.615  8.828   0.26 26.71 ? 116 GLU   B OE1 1 
ATOM   1706 O OE1 B GLU   B 1 102 ? 23.773  24.664  9.052   0.74 33.18 ? 116 GLU   B OE1 1 
ATOM   1707 O OE2 A GLU   B 1 102 ? 24.247  25.911  10.541  0.26 26.03 ? 116 GLU   B OE2 1 
ATOM   1708 O OE2 B GLU   B 1 102 ? 23.112  23.220  7.533   0.74 33.02 ? 116 GLU   B OE2 1 
ATOM   1709 N N   . ALA   B 1 103 ? 27.379  20.610  8.722   1.00 21.24 ? 117 ALA   B N   1 
ATOM   1710 C CA  . ALA   B 1 103 ? 27.448  19.349  7.990   1.00 21.39 ? 117 ALA   B CA  1 
ATOM   1711 C C   . ALA   B 1 103 ? 26.722  18.221  8.715   1.00 20.11 ? 117 ALA   B C   1 
ATOM   1712 O O   . ALA   B 1 103 ? 26.236  17.283  8.073   1.00 21.43 ? 117 ALA   B O   1 
ATOM   1713 C CB  . ALA   B 1 103 ? 28.907  18.969  7.734   1.00 22.07 ? 117 ALA   B CB  1 
ATOM   1714 N N   . ASN   B 1 104 ? 26.631  18.294  10.041  1.00 18.89 ? 118 ASN   B N   1 
ATOM   1715 C CA  . ASN   B 1 104 ? 25.977  17.269  10.843  1.00 18.56 ? 118 ASN   B CA  1 
ATOM   1716 C C   . ASN   B 1 104 ? 24.586  17.674  11.317  1.00 17.50 ? 118 ASN   B C   1 
ATOM   1717 O O   . ASN   B 1 104 ? 23.964  16.937  12.094  1.00 17.25 ? 118 ASN   B O   1 
ATOM   1718 C CB  . ASN   B 1 104 ? 26.854  16.895  12.036  1.00 20.08 ? 118 ASN   B CB  1 
ATOM   1719 C CG  . ASN   B 1 104 ? 28.139  16.221  11.610  1.00 22.77 ? 118 ASN   B CG  1 
ATOM   1720 O OD1 . ASN   B 1 104 ? 28.161  15.479  10.629  1.00 24.41 ? 118 ASN   B OD1 1 
ATOM   1721 N ND2 . ASN   B 1 104 ? 29.219  16.485  12.335  1.00 24.14 ? 118 ASN   B ND2 1 
ATOM   1722 N N   . ALA   B 1 105 ? 24.071  18.816  10.860  1.00 15.90 ? 119 ALA   B N   1 
ATOM   1723 C CA  . ALA   B 1 105 ? 22.807  19.314  11.393  1.00 15.77 ? 119 ALA   B CA  1 
ATOM   1724 C C   . ALA   B 1 105 ? 21.625  18.435  10.994  1.00 16.23 ? 119 ALA   B C   1 
ATOM   1725 O O   . ALA   B 1 105 ? 20.629  18.375  11.721  1.00 16.34 ? 119 ALA   B O   1 
ATOM   1726 C CB  . ALA   B 1 105 ? 22.582  20.756  10.941  1.00 18.21 ? 119 ALA   B CB  1 
ATOM   1727 N N   . TRP   B 1 106 ? 21.714  17.750  9.851   1.00 17.24 ? 120 TRP   B N   1 
ATOM   1728 C CA  . TRP   B 1 106 ? 20.597  16.931  9.391   1.00 18.23 ? 120 TRP   B CA  1 
ATOM   1729 C C   . TRP   B 1 106 ? 20.240  15.851  10.405  1.00 19.19 ? 120 TRP   B C   1 
ATOM   1730 O O   . TRP   B 1 106 ? 19.089  15.401  10.455  1.00 19.48 ? 120 TRP   B O   1 
ATOM   1731 C CB  . TRP   B 1 106 ? 20.919  16.322  8.022   1.00 20.20 ? 120 TRP   B CB  1 
ATOM   1732 C CG  . TRP   B 1 106 ? 21.920  15.222  8.073   1.00 20.74 ? 120 TRP   B CG  1 
ATOM   1733 C CD1 . TRP   B 1 106 ? 23.285  15.344  8.038   1.00 21.41 ? 120 TRP   B CD1 1 
ATOM   1734 C CD2 . TRP   B 1 106 ? 21.644  13.823  8.154   1.00 22.73 ? 120 TRP   B CD2 1 
ATOM   1735 N NE1 . TRP   B 1 106 ? 23.869  14.103  8.103   1.00 23.38 ? 120 TRP   B NE1 1 
ATOM   1736 C CE2 . TRP   B 1 106 ? 22.884  13.152  8.172   1.00 24.17 ? 120 TRP   B CE2 1 
ATOM   1737 C CE3 . TRP   B 1 106 ? 20.464  13.069  8.216   1.00 23.64 ? 120 TRP   B CE3 1 
ATOM   1738 C CZ2 . TRP   B 1 106 ? 22.978  11.762  8.242   1.00 25.19 ? 120 TRP   B CZ2 1 
ATOM   1739 C CZ3 . TRP   B 1 106 ? 20.561  11.691  8.288   1.00 25.38 ? 120 TRP   B CZ3 1 
ATOM   1740 C CH2 . TRP   B 1 106 ? 21.808  11.052  8.298   1.00 25.90 ? 120 TRP   B CH2 1 
ATOM   1741 N N   . LYS   B 1 107 ? 21.205  15.429  11.223  1.00 18.86 ? 121 LYS   B N   1 
ATOM   1742 C CA  . LYS   B 1 107 ? 20.989  14.402  12.237  1.00 18.88 ? 121 LYS   B CA  1 
ATOM   1743 C C   . LYS   B 1 107 ? 21.083  14.957  13.661  1.00 16.40 ? 121 LYS   B C   1 
ATOM   1744 O O   . LYS   B 1 107 ? 21.442  14.237  14.595  1.00 17.66 ? 121 LYS   B O   1 
ATOM   1745 C CB  . LYS   B 1 107 ? 21.930  13.213  12.028  1.00 21.92 ? 121 LYS   B CB  1 
ATOM   1746 C CG  . LYS   B 1 107 ? 23.399  13.579  11.898  1.00 23.67 ? 121 LYS   B CG  1 
ATOM   1747 C CD  . LYS   B 1 107 ? 24.256  12.328  11.750  1.00 25.54 ? 121 LYS   B CD  1 
ATOM   1748 C CE  . LYS   B 1 107 ? 25.744  12.652  11.806  1.00 29.16 ? 121 LYS   B CE  1 
ATOM   1749 N NZ  . LYS   B 1 107 ? 26.581  11.425  11.666  1.00 32.08 ? 121 LYS   B NZ  1 
ATOM   1750 N N   . SER   B 1 108 ? 20.729  16.230  13.842  1.00 14.24 ? 122 SER   B N   1 
ATOM   1751 C CA  . SER   B 1 108 ? 20.840  16.913  15.131  1.00 13.02 ? 122 SER   B CA  1 
ATOM   1752 C C   . SER   B 1 108 ? 19.699  16.629  16.109  1.00 12.55 ? 122 SER   B C   1 
ATOM   1753 O O   . SER   B 1 108 ? 19.844  16.958  17.292  1.00 12.80 ? 122 SER   B O   1 
ATOM   1754 C CB  . SER   B 1 108 ? 20.873  18.425  14.895  1.00 14.66 ? 122 SER   B CB  1 
ATOM   1755 O OG  . SER   B 1 108 ? 19.629  18.864  14.356  1.00 16.80 ? 122 SER   B OG  1 
ATOM   1756 N N   . THR   B 1 109 ? 18.574  16.062  15.668  1.00 11.98 ? 123 THR   B N   1 
ATOM   1757 C CA  . THR   B 1 109 ? 17.355  16.063  16.477  1.00 10.75 ? 123 THR   B CA  1 
ATOM   1758 C C   . THR   B 1 109 ? 16.768  14.662  16.618  1.00 10.89 ? 123 THR   B C   1 
ATOM   1759 O O   . THR   B 1 109 ? 16.374  14.041  15.623  1.00 11.93 ? 123 THR   B O   1 
ATOM   1760 C CB  . THR   B 1 109 ? 16.306  17.002  15.866  1.00 11.43 ? 123 THR   B CB  1 
ATOM   1761 O OG1 . THR   B 1 109 ? 16.894  18.276  15.588  1.00 14.29 ? 123 THR   B OG1 1 
ATOM   1762 C CG2 . THR   B 1 109 ? 15.154  17.216  16.842  1.00 11.65 ? 123 THR   B CG2 1 
ATOM   1763 N N   . LEU   B 1 110 ? 16.672  14.186  17.861  1.00 10.62 ? 124 LEU   B N   1 
ATOM   1764 C CA  . LEU   B 1 110 ? 15.951  12.964  18.198  1.00 10.96 ? 124 LEU   B CA  1 
ATOM   1765 C C   . LEU   B 1 110 ? 14.509  13.298  18.581  1.00 10.76 ? 124 LEU   B C   1 
ATOM   1766 O O   . LEU   B 1 110 ? 14.221  14.384  19.102  1.00 10.75 ? 124 LEU   B O   1 
ATOM   1767 C CB  . LEU   B 1 110 ? 16.634  12.266  19.384  1.00 12.39 ? 124 LEU   B CB  1 
ATOM   1768 C CG  . LEU   B 1 110 ? 18.034  11.709  19.091  1.00 13.56 ? 124 LEU   B CG  1 
ATOM   1769 C CD1 . LEU   B 1 110 ? 18.800  11.474  20.381  1.00 14.54 ? 124 LEU   B CD1 1 
ATOM   1770 C CD2 . LEU   B 1 110 ? 17.970  10.419  18.262  1.00 15.22 ? 124 LEU   B CD2 1 
ATOM   1771 N N   . VAL   B 1 111 ? 13.606  12.340  18.353  1.00 10.82 ? 125 VAL   B N   1 
ATOM   1772 C CA  . VAL   B 1 111 ? 12.201  12.488  18.721  1.00 10.68 ? 125 VAL   B CA  1 
ATOM   1773 C C   . VAL   B 1 111 ? 11.756  11.262  19.509  1.00 10.06 ? 125 VAL   B C   1 
ATOM   1774 O O   . VAL   B 1 111 ? 12.191  10.140  19.232  1.00 11.03 ? 125 VAL   B O   1 
ATOM   1775 C CB  . VAL   B 1 111 ? 11.301  12.723  17.472  1.00 11.57 ? 125 VAL   B CB  1 
ATOM   1776 C CG1 . VAL   B 1 111 ? 11.368  11.538  16.480  1.00 12.47 ? 125 VAL   B CG1 1 
ATOM   1777 C CG2 . VAL   B 1 111 ? 9.862   12.991  17.880  1.00 12.31 ? 125 VAL   B CG2 1 
ATOM   1778 N N   . GLY   B 1 112 ? 10.877  11.470  20.484  1.00 10.20 ? 126 GLY   B N   1 
ATOM   1779 C CA  . GLY   B 1 112 ? 10.319  10.354  21.223  1.00 10.56 ? 126 GLY   B CA  1 
ATOM   1780 C C   . GLY   B 1 112 ? 9.119   10.770  22.046  1.00 9.56  ? 126 GLY   B C   1 
ATOM   1781 O O   . GLY   B 1 112 ? 8.515   11.817  21.809  1.00 10.28 ? 126 GLY   B O   1 
ATOM   1782 N N   . HIS   B 1 113 ? 8.780   9.933   23.027  1.00 10.31 ? 127 HIS   B N   1 
ATOM   1783 C CA  . HIS   B 1 113 ? 7.607   10.171  23.857  1.00 11.24 ? 127 HIS   B CA  1 
ATOM   1784 C C   . HIS   B 1 113 ? 7.881   9.721   25.288  1.00 11.77 ? 127 HIS   B C   1 
ATOM   1785 O O   . HIS   B 1 113 ? 8.567   8.722   25.511  1.00 15.89 ? 127 HIS   B O   1 
ATOM   1786 C CB  . HIS   B 1 113 ? 6.359   9.470   23.287  1.00 13.96 ? 127 HIS   B CB  1 
ATOM   1787 C CG  . HIS   B 1 113 ? 6.605   8.058   22.845  1.00 17.14 ? 127 HIS   B CG  1 
ATOM   1788 N ND1 . HIS   B 1 113 ? 6.258   6.969   23.614  1.00 21.46 ? 127 HIS   B ND1 1 
ATOM   1789 C CD2 . HIS   B 1 113 ? 7.156   7.557   21.712  1.00 18.71 ? 127 HIS   B CD2 1 
ATOM   1790 C CE1 . HIS   B 1 113 ? 6.589   5.858   22.979  1.00 22.47 ? 127 HIS   B CE1 1 
ATOM   1791 N NE2 . HIS   B 1 113 ? 7.138   6.187   21.824  1.00 22.19 ? 127 HIS   B NE2 1 
ATOM   1792 N N   . ASP   B 1 114 ? 7.349   10.481  26.253  1.00 11.46 ? 128 ASP   B N   1 
ATOM   1793 C CA  A ASP   B 1 114 ? 7.454   10.164  27.673  0.60 11.81 ? 128 ASP   B CA  1 
ATOM   1794 C CA  B ASP   B 1 114 ? 7.459   10.186  27.678  0.40 11.89 ? 128 ASP   B CA  1 
ATOM   1795 C C   . ASP   B 1 114 ? 6.073   10.268  28.302  1.00 11.23 ? 128 ASP   B C   1 
ATOM   1796 O O   . ASP   B 1 114 ? 5.322   11.209  28.022  1.00 11.43 ? 128 ASP   B O   1 
ATOM   1797 C CB  A ASP   B 1 114 ? 8.370   11.149  28.437  0.60 13.04 ? 128 ASP   B CB  1 
ATOM   1798 C CB  B ASP   B 1 114 ? 8.328   11.240  28.391  0.40 13.08 ? 128 ASP   B CB  1 
ATOM   1799 C CG  A ASP   B 1 114 ? 9.857   10.883  28.233  0.60 13.48 ? 128 ASP   B CG  1 
ATOM   1800 C CG  B ASP   B 1 114 ? 9.770   10.800  28.590  0.40 13.16 ? 128 ASP   B CG  1 
ATOM   1801 O OD1 A ASP   B 1 114 ? 10.227  9.909   27.532  0.60 14.17 ? 128 ASP   B OD1 1 
ATOM   1802 O OD1 B ASP   B 1 114 ? 10.010  9.620   28.926  0.40 13.40 ? 128 ASP   B OD1 1 
ATOM   1803 O OD2 A ASP   B 1 114 ? 10.664  11.676  28.778  0.60 13.22 ? 128 ASP   B OD2 1 
ATOM   1804 O OD2 B ASP   B 1 114 ? 10.669  11.657  28.437  0.40 14.47 ? 128 ASP   B OD2 1 
ATOM   1805 N N   . THR   B 1 115 ? 5.748   9.308   29.173  1.00 12.53 ? 129 THR   B N   1 
ATOM   1806 C CA  A THR   B 1 115 ? 4.532   9.353   29.981  0.99 13.03 ? 129 THR   B CA  1 
ATOM   1807 C CA  B THR   B 1 115 ? 4.533   9.341   29.981  0.01 12.18 ? 129 THR   B CA  1 
ATOM   1808 C C   . THR   B 1 115 ? 4.930   9.476   31.444  1.00 12.16 ? 129 THR   B C   1 
ATOM   1809 O O   . THR   B 1 115 ? 5.748   8.690   31.937  1.00 13.19 ? 129 THR   B O   1 
ATOM   1810 C CB  A THR   B 1 115 ? 3.678   8.095   29.784  0.99 16.65 ? 129 THR   B CB  1 
ATOM   1811 C CB  B THR   B 1 115 ? 3.731   8.048   29.815  0.01 12.14 ? 129 THR   B CB  1 
ATOM   1812 O OG1 A THR   B 1 115 ? 3.436   7.891   28.389  0.99 20.94 ? 129 THR   B OG1 1 
ATOM   1813 O OG1 B THR   B 1 115 ? 4.074   7.138   30.868  0.01 12.21 ? 129 THR   B OG1 1 
ATOM   1814 C CG2 A THR   B 1 115 ? 2.337   8.244   30.499  0.99 17.72 ? 129 THR   B CG2 1 
ATOM   1815 C CG2 B THR   B 1 115 ? 4.043   7.391   28.490  0.01 12.20 ? 129 THR   B CG2 1 
ATOM   1816 N N   . PHE   B 1 116 ? 4.350   10.457  32.137  1.00 12.30 ? 130 PHE   B N   1 
ATOM   1817 C CA  . PHE   B 1 116 ? 4.666   10.719  33.539  1.00 12.60 ? 130 PHE   B CA  1 
ATOM   1818 C C   . PHE   B 1 116 ? 3.492   10.350  34.446  1.00 13.59 ? 130 PHE   B C   1 
ATOM   1819 O O   . PHE   B 1 116 ? 2.330   10.614  34.119  1.00 13.64 ? 130 PHE   B O   1 
ATOM   1820 C CB  . PHE   B 1 116 ? 5.036   12.197  33.748  1.00 12.55 ? 130 PHE   B CB  1 
ATOM   1821 C CG  . PHE   B 1 116 ? 6.267   12.636  32.997  1.00 11.77 ? 130 PHE   B CG  1 
ATOM   1822 C CD1 . PHE   B 1 116 ? 6.177   13.097  31.692  1.00 11.62 ? 130 PHE   B CD1 1 
ATOM   1823 C CD2 . PHE   B 1 116 ? 7.514   12.592  33.597  1.00 12.67 ? 130 PHE   B CD2 1 
ATOM   1824 C CE1 . PHE   B 1 116 ? 7.318   13.496  31.004  1.00 11.77 ? 130 PHE   B CE1 1 
ATOM   1825 C CE2 . PHE   B 1 116 ? 8.653   12.992  32.919  1.00 12.99 ? 130 PHE   B CE2 1 
ATOM   1826 C CZ  . PHE   B 1 116 ? 8.557   13.440  31.617  1.00 12.95 ? 130 PHE   B CZ  1 
ATOM   1827 N N   . THR   B 1 117 ? 3.809   9.759   35.604  1.00 14.95 ? 131 THR   B N   1 
ATOM   1828 C CA  A THR   B 1 117 ? 2.815   9.357   36.591  0.89 16.79 ? 131 THR   B CA  1 
ATOM   1829 C CA  B THR   B 1 117 ? 2.830   9.336   36.597  0.11 16.50 ? 131 THR   B CA  1 
ATOM   1830 C C   . THR   B 1 117 ? 3.192   9.943   37.950  1.00 17.85 ? 131 THR   B C   1 
ATOM   1831 O O   . THR   B 1 117 ? 4.352   10.283  38.202  1.00 17.02 ? 131 THR   B O   1 
ATOM   1832 C CB  A THR   B 1 117 ? 2.693   7.819   36.674  0.89 18.99 ? 131 THR   B CB  1 
ATOM   1833 C CB  B THR   B 1 117 ? 2.821   7.795   36.691  0.11 16.65 ? 131 THR   B CB  1 
ATOM   1834 O OG1 A THR   B 1 117 ? 3.981   7.239   36.921  0.89 20.36 ? 131 THR   B OG1 1 
ATOM   1835 O OG1 B THR   B 1 117 ? 2.732   7.234   35.375  0.11 17.26 ? 131 THR   B OG1 1 
ATOM   1836 C CG2 A THR   B 1 117 ? 2.138   7.239   35.385  0.89 21.39 ? 131 THR   B CG2 1 
ATOM   1837 C CG2 B THR   B 1 117 ? 1.651   7.290   37.523  0.11 16.46 ? 131 THR   B CG2 1 
ATOM   1838 N N   . LYS   B 1 118 ? 2.182   10.095  38.831  1.00 19.35 ? 132 LYS   B N   1 
ATOM   1839 C CA  . LYS   B 1 118 ? 2.396   10.614  40.183  1.00 22.08 ? 132 LYS   B CA  1 
ATOM   1840 C C   . LYS   B 1 118 ? 2.912   9.548   41.134  1.00 23.69 ? 132 LYS   B C   1 
ATOM   1841 O O   . LYS   B 1 118 ? 3.317   9.881   42.255  1.00 22.59 ? 132 LYS   B O   1 
ATOM   1842 C CB  . LYS   B 1 118 ? 1.109   11.225  40.759  1.00 22.71 ? 132 LYS   B CB  1 
ATOM   1843 C CG  . LYS   B 1 118 ? 0.694   12.553  40.137  1.00 24.36 ? 132 LYS   B CG  1 
ATOM   1844 C CD  . LYS   B 1 118 ? -0.582  13.114  40.775  1.00 25.35 ? 132 LYS   B CD  1 
ATOM   1845 C CE  . LYS   B 1 118 ? -1.032  14.394  40.069  1.00 28.20 ? 132 LYS   B CE  1 
ATOM   1846 N NZ  . LYS   B 1 118 ? -2.320  14.990  40.546  1.00 29.06 ? 132 LYS   B NZ  1 
ATOM   1847 N N   . VAL   B 1 119 ? 2.898   8.286   40.710  1.00 26.63 ? 133 VAL   B N   1 
ATOM   1848 C CA  . VAL   B 1 119 ? 3.483   7.167   41.434  1.00 31.33 ? 133 VAL   B CA  1 
ATOM   1849 C C   . VAL   B 1 119 ? 4.581   6.591   40.552  1.00 34.27 ? 133 VAL   B C   1 
ATOM   1850 O O   . VAL   B 1 119 ? 4.403   6.469   39.336  1.00 35.74 ? 133 VAL   B O   1 
ATOM   1851 C CB  . VAL   B 1 119 ? 2.413   6.090   41.711  1.00 33.53 ? 133 VAL   B CB  1 
ATOM   1852 C CG1 . VAL   B 1 119 ? 2.937   5.047   42.685  1.00 33.93 ? 133 VAL   B CG1 1 
ATOM   1853 C CG2 . VAL   B 1 119 ? 1.123   6.728   42.221  1.00 35.15 ? 133 VAL   B CG2 1 
ATOM   1854 N N   . LYS   B 1 120 ? 5.712   6.242   41.153  1.00 36.98 ? 134 LYS   B N   1 
ATOM   1855 C CA  . LYS   B 1 120 ? 6.823   5.694   40.377  1.00 39.05 ? 134 LYS   B CA  1 
ATOM   1856 C C   . LYS   B 1 120 ? 6.584   4.226   40.035  1.00 39.55 ? 134 LYS   B C   1 
ATOM   1857 O O   . LYS   B 1 120 ? 5.630   3.612   40.515  1.00 39.72 ? 134 LYS   B O   1 
ATOM   1858 C CB  . LYS   B 1 120 ? 8.145   5.847   41.130  1.00 40.75 ? 134 LYS   B CB  1 
ATOM   1859 C CG  . LYS   B 1 120 ? 8.290   4.912   42.316  1.00 42.15 ? 134 LYS   B CG  1 
ATOM   1860 C CD  . LYS   B 1 120 ? 9.588   5.164   43.068  1.00 42.76 ? 134 LYS   B CD  1 
ATOM   1861 C CE  . LYS   B 1 120 ? 9.606   6.547   43.702  1.00 42.81 ? 134 LYS   B CE  1 
ATOM   1862 N NZ  . LYS   B 1 120 ? 10.871  6.796   44.452  1.00 42.71 ? 134 LYS   B NZ  1 
ATOM   1863 N N   . GLY   C 1 2   ? 24.585  37.531  20.086  1.00 29.07 ? 16  GLY   C N   1 
ATOM   1864 C CA  . GLY   C 1 2   ? 24.215  36.151  20.334  1.00 26.02 ? 16  GLY   C CA  1 
ATOM   1865 C C   . GLY   C 1 2   ? 22.732  35.869  20.159  1.00 22.38 ? 16  GLY   C C   1 
ATOM   1866 O O   . GLY   C 1 2   ? 22.128  36.257  19.162  1.00 22.50 ? 16  GLY   C O   1 
ATOM   1867 N N   . ILE   C 1 3   ? 22.146  35.190  21.144  1.00 20.18 ? 17  ILE   C N   1 
ATOM   1868 C CA  . ILE   C 1 3   ? 20.742  34.795  21.065  1.00 18.89 ? 17  ILE   C CA  1 
ATOM   1869 C C   . ILE   C 1 3   ? 19.815  35.965  21.380  1.00 17.23 ? 17  ILE   C C   1 
ATOM   1870 O O   . ILE   C 1 3   ? 18.758  36.114  20.759  1.00 16.77 ? 17  ILE   C O   1 
ATOM   1871 C CB  . ILE   C 1 3   ? 20.485  33.576  21.975  1.00 18.66 ? 17  ILE   C CB  1 
ATOM   1872 C CG1 . ILE   C 1 3   ? 21.221  32.345  21.434  1.00 19.89 ? 17  ILE   C CG1 1 
ATOM   1873 C CG2 . ILE   C 1 3   ? 18.987  33.306  22.125  1.00 17.94 ? 17  ILE   C CG2 1 
ATOM   1874 C CD1 . ILE   C 1 3   ? 21.295  31.201  22.423  1.00 20.62 ? 17  ILE   C CD1 1 
ATOM   1875 N N   . THR   C 1 4   ? 20.185  36.806  22.344  1.00 17.33 ? 18  THR   C N   1 
ATOM   1876 C CA  . THR   C 1 4   ? 19.339  37.931  22.729  1.00 17.46 ? 18  THR   C CA  1 
ATOM   1877 C C   . THR   C 1 4   ? 19.067  38.834  21.530  1.00 17.20 ? 18  THR   C C   1 
ATOM   1878 O O   . THR   C 1 4   ? 19.992  39.235  20.819  1.00 19.11 ? 18  THR   C O   1 
ATOM   1879 C CB  . THR   C 1 4   ? 20.049  38.726  23.824  1.00 18.63 ? 18  THR   C CB  1 
ATOM   1880 O OG1 . THR   C 1 4   ? 20.177  37.909  24.993  1.00 18.61 ? 18  THR   C OG1 1 
ATOM   1881 C CG2 . THR   C 1 4   ? 19.280  39.996  24.167  1.00 19.95 ? 18  THR   C CG2 1 
ATOM   1882 N N   . GLY   C 1 5   ? 17.800  39.151  21.303  1.00 16.70 ? 19  GLY   C N   1 
ATOM   1883 C CA  . GLY   C 1 5   ? 17.429  40.047  20.229  1.00 17.10 ? 19  GLY   C CA  1 
ATOM   1884 C C   . GLY   C 1 5   ? 16.025  39.752  19.734  1.00 16.47 ? 19  GLY   C C   1 
ATOM   1885 O O   . GLY   C 1 5   ? 15.263  39.012  20.353  1.00 16.40 ? 19  GLY   C O   1 
ATOM   1886 N N   . THR   C 1 6   ? 15.700  40.358  18.593  1.00 16.83 ? 20  THR   C N   1 
ATOM   1887 C CA  . THR   C 1 6   ? 14.415  40.171  17.934  1.00 16.71 ? 20  THR   C CA  1 
ATOM   1888 C C   . THR   C 1 6   ? 14.621  39.354  16.666  1.00 16.64 ? 20  THR   C C   1 
ATOM   1889 O O   . THR   C 1 6   ? 15.440  39.718  15.811  1.00 17.83 ? 20  THR   C O   1 
ATOM   1890 C CB  . THR   C 1 6   ? 13.771  41.521  17.609  1.00 18.80 ? 20  THR   C CB  1 
ATOM   1891 O OG1 . THR   C 1 6   ? 13.416  42.184  18.832  1.00 19.91 ? 20  THR   C OG1 1 
ATOM   1892 C CG2 . THR   C 1 6   ? 12.525  41.337  16.744  1.00 19.61 ? 20  THR   C CG2 1 
ATOM   1893 N N   . TRP   C 1 7   ? 13.875  38.255  16.552  1.00 16.68 ? 21  TRP   C N   1 
ATOM   1894 C CA  . TRP   C 1 7   ? 13.978  37.307  15.454  1.00 15.11 ? 21  TRP   C CA  1 
ATOM   1895 C C   . TRP   C 1 7   ? 12.620  37.165  14.776  1.00 15.06 ? 21  TRP   C C   1 
ATOM   1896 O O   . TRP   C 1 7   ? 11.571  37.433  15.370  1.00 16.07 ? 21  TRP   C O   1 
ATOM   1897 C CB  . TRP   C 1 7   ? 14.403  35.926  15.980  1.00 15.88 ? 21  TRP   C CB  1 
ATOM   1898 C CG  . TRP   C 1 7   ? 15.720  35.884  16.706  1.00 15.89 ? 21  TRP   C CG  1 
ATOM   1899 C CD1 . TRP   C 1 7   ? 15.947  36.205  18.016  1.00 15.84 ? 21  TRP   C CD1 1 
ATOM   1900 C CD2 . TRP   C 1 7   ? 16.984  35.465  16.172  1.00 16.11 ? 21  TRP   C CD2 1 
ATOM   1901 N NE1 . TRP   C 1 7   ? 17.275  36.025  18.326  1.00 15.33 ? 21  TRP   C NE1 1 
ATOM   1902 C CE2 . TRP   C 1 7   ? 17.934  35.572  17.213  1.00 15.51 ? 21  TRP   C CE2 1 
ATOM   1903 C CE3 . TRP   C 1 7   ? 17.406  35.017  14.917  1.00 17.46 ? 21  TRP   C CE3 1 
ATOM   1904 C CZ2 . TRP   C 1 7   ? 19.276  35.241  17.037  1.00 16.76 ? 21  TRP   C CZ2 1 
ATOM   1905 C CZ3 . TRP   C 1 7   ? 18.740  34.694  14.742  1.00 18.05 ? 21  TRP   C CZ3 1 
ATOM   1906 C CH2 . TRP   C 1 7   ? 19.660  34.809  15.797  1.00 17.69 ? 21  TRP   C CH2 1 
ATOM   1907 N N   . TYR   C 1 8   ? 12.651  36.725  13.520  1.00 14.63 ? 22  TYR   C N   1 
ATOM   1908 C CA  . TYR   C 1 8   ? 11.448  36.510  12.727  1.00 14.66 ? 22  TYR   C CA  1 
ATOM   1909 C C   . TYR   C 1 8   ? 11.527  35.140  12.076  1.00 15.20 ? 22  TYR   C C   1 
ATOM   1910 O O   . TYR   C 1 8   ? 12.573  34.771  11.529  1.00 14.64 ? 22  TYR   C O   1 
ATOM   1911 C CB  . TYR   C 1 8   ? 11.329  37.575  11.632  1.00 15.62 ? 22  TYR   C CB  1 
ATOM   1912 C CG  . TYR   C 1 8   ? 11.397  38.986  12.167  1.00 16.75 ? 22  TYR   C CG  1 
ATOM   1913 C CD1 . TYR   C 1 8   ? 10.272  39.589  12.721  1.00 17.97 ? 22  TYR   C CD1 1 
ATOM   1914 C CD2 . TYR   C 1 8   ? 12.588  39.704  12.155  1.00 17.33 ? 22  TYR   C CD2 1 
ATOM   1915 C CE1 . TYR   C 1 8   ? 10.325  40.875  13.226  1.00 19.80 ? 22  TYR   C CE1 1 
ATOM   1916 C CE2 . TYR   C 1 8   ? 12.649  40.992  12.658  1.00 18.84 ? 22  TYR   C CE2 1 
ATOM   1917 C CZ  . TYR   C 1 8   ? 11.514  41.568  13.193  1.00 20.46 ? 22  TYR   C CZ  1 
ATOM   1918 O OH  . TYR   C 1 8   ? 11.568  42.850  13.693  1.00 22.45 ? 22  TYR   C OH  1 
ATOM   1919 N N   . ASN   C 1 9   ? 10.423  34.388  12.119  1.00 15.17 ? 23  ASN   C N   1 
ATOM   1920 C CA  . ASN   C 1 9   ? 10.408  33.113  11.409  1.00 15.15 ? 23  ASN   C CA  1 
ATOM   1921 C C   . ASN   C 1 9   ? 10.039  33.311  9.939   1.00 15.37 ? 23  ASN   C C   1 
ATOM   1922 O O   . ASN   C 1 9   ? 9.798   34.431  9.471   1.00 16.50 ? 23  ASN   C O   1 
ATOM   1923 C CB  . ASN   C 1 9   ? 9.614   32.024  12.148  1.00 15.51 ? 23  ASN   C CB  1 
ATOM   1924 C CG  . ASN   C 1 9   ? 8.106   32.096  11.922  1.00 15.81 ? 23  ASN   C CG  1 
ATOM   1925 O OD1 . ASN   C 1 9   ? 7.587   32.989  11.255  1.00 15.83 ? 23  ASN   C OD1 1 
ATOM   1926 N ND2 . ASN   C 1 9   ? 7.393   31.124  12.484  1.00 16.80 ? 23  ASN   C ND2 1 
ATOM   1927 N N   . GLN   C 1 10  ? 10.020  32.199  9.200   1.00 15.88 ? 24  GLN   C N   1 
ATOM   1928 C CA  . GLN   C 1 10  ? 9.807   32.241  7.760   1.00 16.84 ? 24  GLN   C CA  1 
ATOM   1929 C C   . GLN   C 1 10  ? 8.404   32.708  7.390   1.00 17.21 ? 24  GLN   C C   1 
ATOM   1930 O O   . GLN   C 1 10  ? 8.178   33.111  6.242   1.00 19.06 ? 24  GLN   C O   1 
ATOM   1931 C CB  . GLN   C 1 10  ? 10.141  30.873  7.148   1.00 16.54 ? 24  GLN   C CB  1 
ATOM   1932 C CG  . GLN   C 1 10  ? 9.136   29.740  7.430   1.00 16.23 ? 24  GLN   C CG  1 
ATOM   1933 C CD  . GLN   C 1 10  ? 9.156   29.192  8.857   1.00 15.95 ? 24  GLN   C CD  1 
ATOM   1934 O OE1 . GLN   C 1 10  ? 10.056  29.475  9.658   1.00 16.51 ? 24  GLN   C OE1 1 
ATOM   1935 N NE2 . GLN   C 1 10  ? 8.153   28.389  9.173   1.00 16.34 ? 24  GLN   C NE2 1 
ATOM   1936 N N   . LEU   C 1 11  ? 7.468   32.675  8.337   1.00 16.50 ? 25  LEU   C N   1 
ATOM   1937 C CA  . LEU   C 1 11  ? 6.103   33.135  8.131   1.00 17.48 ? 25  LEU   C CA  1 
ATOM   1938 C C   . LEU   C 1 11  ? 5.850   34.514  8.716   1.00 18.74 ? 25  LEU   C C   1 
ATOM   1939 O O   . LEU   C 1 11  ? 4.722   35.010  8.631   1.00 21.28 ? 25  LEU   C O   1 
ATOM   1940 C CB  . LEU   C 1 11  ? 5.109   32.125  8.716   1.00 18.26 ? 25  LEU   C CB  1 
ATOM   1941 C CG  . LEU   C 1 11  ? 5.138   30.746  8.048   1.00 20.35 ? 25  LEU   C CG  1 
ATOM   1942 C CD1 . LEU   C 1 11  ? 4.146   29.797  8.706   1.00 20.61 ? 25  LEU   C CD1 1 
ATOM   1943 C CD2 . LEU   C 1 11  ? 4.869   30.859  6.547   1.00 21.98 ? 25  LEU   C CD2 1 
ATOM   1944 N N   . GLY   C 1 12  ? 6.862   35.148  9.300   1.00 18.10 ? 26  GLY   C N   1 
ATOM   1945 C CA  . GLY   C 1 12  ? 6.713   36.487  9.831   1.00 19.74 ? 26  GLY   C CA  1 
ATOM   1946 C C   . GLY   C 1 12  ? 6.352   36.589  11.300  1.00 19.66 ? 26  GLY   C C   1 
ATOM   1947 O O   . GLY   C 1 12  ? 6.102   37.705  11.777  1.00 21.93 ? 26  GLY   C O   1 
ATOM   1948 N N   . SER   C 1 13  ? 6.305   35.477  12.035  1.00 17.99 ? 27  SER   C N   1 
ATOM   1949 C CA  . SER   C 1 13  ? 6.129   35.559  13.482  1.00 17.28 ? 27  SER   C CA  1 
ATOM   1950 C C   . SER   C 1 13  ? 7.322   36.282  14.105  1.00 16.53 ? 27  SER   C C   1 
ATOM   1951 O O   . SER   C 1 13  ? 8.437   36.236  13.581  1.00 18.41 ? 27  SER   C O   1 
ATOM   1952 C CB  . SER   C 1 13  ? 6.029   34.154  14.077  1.00 17.64 ? 27  SER   C CB  1 
ATOM   1953 O OG  . SER   C 1 13  ? 4.919   33.443  13.550  1.00 20.34 ? 27  SER   C OG  1 
ATOM   1954 N N   . THR   C 1 14  ? 7.087   36.961  15.233  1.00 16.34 ? 28  THR   C N   1 
ATOM   1955 C CA  . THR   C 1 14  ? 8.117   37.759  15.900  1.00 15.97 ? 28  THR   C CA  1 
ATOM   1956 C C   . THR   C 1 14  ? 8.466   37.154  17.259  1.00 15.20 ? 28  THR   C C   1 
ATOM   1957 O O   . THR   C 1 14  ? 7.590   37.002  18.118  1.00 16.23 ? 28  THR   C O   1 
ATOM   1958 C CB  . THR   C 1 14  ? 7.667   39.209  16.077  1.00 17.97 ? 28  THR   C CB  1 
ATOM   1959 O OG1 . THR   C 1 14  ? 7.314   39.757  14.806  1.00 18.80 ? 28  THR   C OG1 1 
ATOM   1960 C CG2 . THR   C 1 14  ? 8.795   40.047  16.679  1.00 18.73 ? 28  THR   C CG2 1 
ATOM   1961 N N   . PHE   C 1 15  ? 9.754   36.874  17.461  1.00 14.41 ? 29  PHE   C N   1 
ATOM   1962 C CA  . PHE   C 1 15  ? 10.305  36.173  18.627  1.00 14.90 ? 29  PHE   C CA  1 
ATOM   1963 C C   . PHE   C 1 15  ? 11.275  37.150  19.292  1.00 15.19 ? 29  PHE   C C   1 
ATOM   1964 O O   . PHE   C 1 15  ? 12.362  37.407  18.765  1.00 15.70 ? 29  PHE   C O   1 
ATOM   1965 C CB  . PHE   C 1 15  ? 10.995  34.900  18.106  1.00 15.11 ? 29  PHE   C CB  1 
ATOM   1966 C CG  . PHE   C 1 15  ? 11.813  34.121  19.123  1.00 14.26 ? 29  PHE   C CG  1 
ATOM   1967 C CD1 . PHE   C 1 15  ? 11.365  33.900  20.412  1.00 14.42 ? 29  PHE   C CD1 1 
ATOM   1968 C CD2 . PHE   C 1 15  ? 13.011  33.531  18.736  1.00 14.35 ? 29  PHE   C CD2 1 
ATOM   1969 C CE1 . PHE   C 1 15  ? 12.124  33.141  21.311  1.00 14.14 ? 29  PHE   C CE1 1 
ATOM   1970 C CE2 . PHE   C 1 15  ? 13.764  32.771  19.617  1.00 14.75 ? 29  PHE   C CE2 1 
ATOM   1971 C CZ  . PHE   C 1 15  ? 13.323  32.580  20.913  1.00 13.94 ? 29  PHE   C CZ  1 
ATOM   1972 N N   . ILE   C 1 16  ? 10.866  37.742  20.416  1.00 14.27 ? 30  ILE   C N   1 
ATOM   1973 C CA  . ILE   C 1 16  ? 11.674  38.728  21.133  1.00 14.54 ? 30  ILE   C CA  1 
ATOM   1974 C C   . ILE   C 1 16  ? 12.196  38.041  22.387  1.00 15.50 ? 30  ILE   C C   1 
ATOM   1975 O O   . ILE   C 1 16  ? 11.417  37.710  23.289  1.00 17.83 ? 30  ILE   C O   1 
ATOM   1976 C CB  . ILE   C 1 16  ? 10.870  39.987  21.489  1.00 16.36 ? 30  ILE   C CB  1 
ATOM   1977 C CG1 . ILE   C 1 16  ? 10.215  40.584  20.243  1.00 18.23 ? 30  ILE   C CG1 1 
ATOM   1978 C CG2 . ILE   C 1 16  ? 11.764  41.013  22.180  1.00 17.50 ? 30  ILE   C CG2 1 
ATOM   1979 C CD1 . ILE   C 1 16  ? 9.312   41.774  20.536  1.00 19.29 ? 30  ILE   C CD1 1 
ATOM   1980 N N   . VAL   C 1 17  ? 13.504  37.808  22.454  1.00 15.21 ? 31  VAL   C N   1 
ATOM   1981 C CA  . VAL   C 1 17  ? 14.052  36.907  23.457  1.00 14.79 ? 31  VAL   C CA  1 
ATOM   1982 C C   . VAL   C 1 17  ? 15.265  37.536  24.125  1.00 15.03 ? 31  VAL   C C   1 
ATOM   1983 O O   . VAL   C 1 17  ? 16.014  38.305  23.513  1.00 15.76 ? 31  VAL   C O   1 
ATOM   1984 C CB  . VAL   C 1 17  ? 14.398  35.532  22.830  1.00 14.40 ? 31  VAL   C CB  1 
ATOM   1985 C CG1 . VAL   C 1 17  ? 15.591  35.647  21.885  1.00 15.03 ? 31  VAL   C CG1 1 
ATOM   1986 C CG2 . VAL   C 1 17  ? 14.655  34.484  23.905  1.00 15.42 ? 31  VAL   C CG2 1 
ATOM   1987 N N   . THR   C 1 18  ? 15.446  37.212  25.403  1.00 15.75 ? 32  THR   C N   1 
ATOM   1988 C CA  . THR   C 1 18  ? 16.648  37.548  26.147  1.00 17.44 ? 32  THR   C CA  1 
ATOM   1989 C C   . THR   C 1 18  ? 17.248  36.259  26.694  1.00 16.08 ? 32  THR   C C   1 
ATOM   1990 O O   . THR   C 1 18  ? 16.535  35.430  27.271  1.00 16.09 ? 32  THR   C O   1 
ATOM   1991 C CB  . THR   C 1 18  ? 16.329  38.534  27.278  1.00 19.61 ? 32  THR   C CB  1 
ATOM   1992 O OG1 . THR   C 1 18  ? 15.761  39.728  26.717  1.00 21.53 ? 32  THR   C OG1 1 
ATOM   1993 C CG2 . THR   C 1 18  ? 17.586  38.899  28.050  1.00 20.65 ? 32  THR   C CG2 1 
ATOM   1994 N N   . ALA   C 1 19  ? 18.549  36.086  26.483  1.00 17.05 ? 33  ALA   C N   1 
ATOM   1995 C CA  . ALA   C 1 19  ? 19.297  34.937  26.977  1.00 17.13 ? 33  ALA   C CA  1 
ATOM   1996 C C   . ALA   C 1 19  ? 20.087  35.388  28.198  1.00 18.79 ? 33  ALA   C C   1 
ATOM   1997 O O   . ALA   C 1 19  ? 21.046  36.156  28.076  1.00 20.58 ? 33  ALA   C O   1 
ATOM   1998 C CB  . ALA   C 1 19  ? 20.239  34.419  25.892  1.00 16.71 ? 33  ALA   C CB  1 
ATOM   1999 N N   . GLY   C 1 20  ? 19.687  34.910  29.367  1.00 18.62 ? 34  GLY   C N   1 
ATOM   2000 C CA  . GLY   C 1 20  ? 20.289  35.360  30.602  1.00 19.91 ? 34  GLY   C CA  1 
ATOM   2001 C C   . GLY   C 1 20  ? 21.510  34.556  30.984  1.00 20.50 ? 34  GLY   C C   1 
ATOM   2002 O O   . GLY   C 1 20  ? 21.770  33.481  30.448  1.00 21.42 ? 34  GLY   C O   1 
ATOM   2003 N N   . ALA   C 1 21  ? 22.259  35.095  31.951  1.00 22.57 ? 35  ALA   C N   1 
ATOM   2004 C CA  . ALA   C 1 21  ? 23.514  34.474  32.356  1.00 24.82 ? 35  ALA   C CA  1 
ATOM   2005 C C   . ALA   C 1 21  ? 23.323  33.061  32.896  1.00 26.12 ? 35  ALA   C C   1 
ATOM   2006 O O   . ALA   C 1 21  ? 24.251  32.250  32.812  1.00 27.91 ? 35  ALA   C O   1 
ATOM   2007 C CB  . ALA   C 1 21  ? 24.216  35.350  33.398  1.00 25.88 ? 35  ALA   C CB  1 
ATOM   2008 N N   . ASP   C 1 22  ? 22.141  32.740  33.420  1.00 24.19 ? 36  ASP   C N   1 
ATOM   2009 C CA  . ASP   C 1 22  ? 21.884  31.460  34.064  1.00 24.28 ? 36  ASP   C CA  1 
ATOM   2010 C C   . ASP   C 1 22  ? 21.335  30.391  33.119  1.00 22.08 ? 36  ASP   C C   1 
ATOM   2011 O O   . ASP   C 1 22  ? 20.895  29.340  33.599  1.00 24.12 ? 36  ASP   C O   1 
ATOM   2012 C CB  . ASP   C 1 22  ? 20.921  31.650  35.239  1.00 26.50 ? 36  ASP   C CB  1 
ATOM   2013 C CG  . ASP   C 1 22  ? 19.569  32.192  34.807  1.00 28.10 ? 36  ASP   C CG  1 
ATOM   2014 O OD1 . ASP   C 1 22  ? 19.484  32.786  33.707  1.00 27.88 ? 36  ASP   C OD1 1 
ATOM   2015 O OD2 . ASP   C 1 22  ? 18.593  32.026  35.574  1.00 29.81 ? 36  ASP   C OD2 1 
ATOM   2016 N N   . GLY   C 1 23  ? 21.351  30.615  31.804  1.00 19.27 ? 37  GLY   C N   1 
ATOM   2017 C CA  . GLY   C 1 23  ? 20.751  29.679  30.867  1.00 16.33 ? 37  GLY   C CA  1 
ATOM   2018 C C   . GLY   C 1 23  ? 19.286  29.913  30.575  1.00 14.53 ? 37  GLY   C C   1 
ATOM   2019 O O   . GLY   C 1 23  ? 18.679  29.106  29.857  1.00 14.86 ? 37  GLY   C O   1 
ATOM   2020 N N   . ALA   C 1 24  ? 18.704  30.997  31.088  1.00 14.95 ? 38  ALA   C N   1 
ATOM   2021 C CA  . ALA   C 1 24  ? 17.281  31.269  30.919  1.00 14.47 ? 38  ALA   C CA  1 
ATOM   2022 C C   . ALA   C 1 24  ? 16.998  31.953  29.583  1.00 14.12 ? 38  ALA   C C   1 
ATOM   2023 O O   . ALA   C 1 24  ? 17.738  32.842  29.155  1.00 15.45 ? 38  ALA   C O   1 
ATOM   2024 C CB  . ALA   C 1 24  ? 16.783  32.164  32.058  1.00 16.58 ? 38  ALA   C CB  1 
ATOM   2025 N N   . LEU   C 1 25  ? 15.912  31.539  28.930  1.00 13.40 ? 39  LEU   C N   1 
ATOM   2026 C CA  . LEU   C 1 25  ? 15.303  32.305  27.848  1.00 13.42 ? 39  LEU   C CA  1 
ATOM   2027 C C   . LEU   C 1 25  ? 13.983  32.876  28.346  1.00 12.60 ? 39  LEU   C C   1 
ATOM   2028 O O   . LEU   C 1 25  ? 13.177  32.152  28.946  1.00 13.67 ? 39  LEU   C O   1 
ATOM   2029 C CB  . LEU   C 1 25  ? 15.049  31.448  26.602  1.00 13.24 ? 39  LEU   C CB  1 
ATOM   2030 C CG  . LEU   C 1 25  ? 16.252  30.788  25.932  1.00 13.01 ? 39  LEU   C CG  1 
ATOM   2031 C CD1 . LEU   C 1 25  ? 15.761  29.954  24.758  1.00 13.33 ? 39  LEU   C CD1 1 
ATOM   2032 C CD2 . LEU   C 1 25  ? 17.244  31.840  25.475  1.00 14.22 ? 39  LEU   C CD2 1 
ATOM   2033 N N   . THR   C 1 26  ? 13.769  34.169  28.100  1.00 13.28 ? 40  THR   C N   1 
ATOM   2034 C CA  . THR   C 1 26  ? 12.534  34.851  28.469  1.00 14.09 ? 40  THR   C CA  1 
ATOM   2035 C C   . THR   C 1 26  ? 12.159  35.797  27.338  1.00 13.69 ? 40  THR   C C   1 
ATOM   2036 O O   . THR   C 1 26  ? 13.015  36.225  26.563  1.00 16.26 ? 40  THR   C O   1 
ATOM   2037 C CB  . THR   C 1 26  ? 12.681  35.644  29.783  1.00 15.76 ? 40  THR   C CB  1 
ATOM   2038 O OG1 . THR   C 1 26  ? 13.703  36.639  29.638  1.00 17.21 ? 40  THR   C OG1 1 
ATOM   2039 C CG2 . THR   C 1 26  ? 13.053  34.731  30.943  1.00 15.95 ? 40  THR   C CG2 1 
ATOM   2040 N N   . GLY   C 1 27  ? 10.881  36.124  27.240  1.00 14.20 ? 41  GLY   C N   1 
ATOM   2041 C CA  . GLY   C 1 27  ? 10.485  37.099  26.231  1.00 15.31 ? 41  GLY   C CA  1 
ATOM   2042 C C   . GLY   C 1 27  ? 9.041   36.899  25.791  1.00 14.50 ? 41  GLY   C C   1 
ATOM   2043 O O   . GLY   C 1 27  ? 8.209   36.412  26.557  1.00 14.53 ? 41  GLY   C O   1 
ATOM   2044 N N   . THR   C 1 28  ? 8.766   37.317  24.551  1.00 14.38 ? 42  THR   C N   1 
ATOM   2045 C CA  . THR   C 1 28  ? 7.423   37.287  23.988  1.00 15.29 ? 42  THR   C CA  1 
ATOM   2046 C C   . THR   C 1 28  ? 7.457   36.715  22.579  1.00 14.74 ? 42  THR   C C   1 
ATOM   2047 O O   . THR   C 1 28  ? 8.456   36.830  21.862  1.00 15.51 ? 42  THR   C O   1 
ATOM   2048 C CB  . THR   C 1 28  ? 6.775   38.689  23.949  1.00 16.65 ? 42  THR   C CB  1 
ATOM   2049 O OG1 . THR   C 1 28  ? 7.527   39.555  23.085  1.00 18.30 ? 42  THR   C OG1 1 
ATOM   2050 C CG2 . THR   C 1 28  ? 6.691   39.295  25.349  1.00 17.45 ? 42  THR   C CG2 1 
ATOM   2051 N N   . TYR   C 1 29  ? 6.337   36.115  22.183  1.00 14.68 ? 43  TYR   C N   1 
ATOM   2052 C CA  . TYR   C 1 29  ? 6.163   35.557  20.851  1.00 14.28 ? 43  TYR   C CA  1 
ATOM   2053 C C   . TYR   C 1 29  ? 4.854   36.080  20.281  1.00 15.15 ? 43  TYR   C C   1 
ATOM   2054 O O   . TYR   C 1 29  ? 3.836   36.118  20.985  1.00 16.28 ? 43  TYR   C O   1 
ATOM   2055 C CB  . TYR   C 1 29  ? 6.113   34.017  20.906  1.00 14.37 ? 43  TYR   C CB  1 
ATOM   2056 C CG  . TYR   C 1 29  ? 6.423   33.345  19.578  1.00 13.56 ? 43  TYR   C CG  1 
ATOM   2057 C CD1 . TYR   C 1 29  ? 5.424   33.111  18.630  1.00 14.25 ? 43  TYR   C CD1 1 
ATOM   2058 C CD2 . TYR   C 1 29  ? 7.717   32.958  19.270  1.00 14.55 ? 43  TYR   C CD2 1 
ATOM   2059 C CE1 . TYR   C 1 29  ? 5.709   32.505  17.416  1.00 15.00 ? 43  TYR   C CE1 1 
ATOM   2060 C CE2 . TYR   C 1 29  ? 8.014   32.357  18.053  1.00 14.22 ? 43  TYR   C CE2 1 
ATOM   2061 C CZ  . TYR   C 1 29  ? 7.006   32.131  17.131  1.00 14.55 ? 43  TYR   C CZ  1 
ATOM   2062 O OH  . TYR   C 1 29  ? 7.295   31.535  15.919  1.00 14.95 ? 43  TYR   C OH  1 
ATOM   2063 N N   . GLU   C 1 30  ? 4.884   36.498  19.021  1.00 16.22 ? 44  GLU   C N   1 
ATOM   2064 C CA  A GLU   C 1 30  ? 3.691   36.912  18.284  0.52 18.32 ? 44  GLU   C CA  1 
ATOM   2065 C CA  B GLU   C 1 30  ? 3.684   36.890  18.298  0.48 18.63 ? 44  GLU   C CA  1 
ATOM   2066 C C   . GLU   C 1 30  ? 3.594   36.009  17.063  1.00 19.60 ? 44  GLU   C C   1 
ATOM   2067 O O   . GLU   C 1 30  ? 4.469   36.058  16.193  1.00 19.30 ? 44  GLU   C O   1 
ATOM   2068 C CB  A GLU   C 1 30  ? 3.805   38.370  17.845  0.52 19.72 ? 44  GLU   C CB  1 
ATOM   2069 C CB  B GLU   C 1 30  ? 3.716   38.375  17.934  0.48 20.19 ? 44  GLU   C CB  1 
ATOM   2070 C CG  A GLU   C 1 30  ? 4.135   39.336  18.953  0.52 19.93 ? 44  GLU   C CG  1 
ATOM   2071 C CG  B GLU   C 1 30  ? 2.445   38.859  17.261  0.48 20.86 ? 44  GLU   C CG  1 
ATOM   2072 C CD  A GLU   C 1 30  ? 4.663   40.667  18.443  0.52 19.63 ? 44  GLU   C CD  1 
ATOM   2073 C CD  B GLU   C 1 30  ? 2.332   40.371  17.219  0.48 22.20 ? 44  GLU   C CD  1 
ATOM   2074 O OE1 A GLU   C 1 30  ? 4.023   41.273  17.554  0.52 21.55 ? 44  GLU   C OE1 1 
ATOM   2075 O OE1 B GLU   C 1 30  ? 3.157   41.057  17.856  0.48 23.32 ? 44  GLU   C OE1 1 
ATOM   2076 O OE2 A GLU   C 1 30  ? 5.730   41.099  18.927  0.52 17.58 ? 44  GLU   C OE2 1 
ATOM   2077 O OE2 B GLU   C 1 30  ? 1.407   40.872  16.548  0.48 22.99 ? 44  GLU   C OE2 1 
ATOM   2078 N N   . SER   C 1 31  ? 2.546   35.187  17.003  1.00 21.46 ? 45  SER   C N   1 
ATOM   2079 C CA  . SER   C 1 31  ? 2.404   34.195  15.945  1.00 23.62 ? 45  SER   C CA  1 
ATOM   2080 C C   . SER   C 1 31  ? 1.739   34.791  14.713  1.00 26.61 ? 45  SER   C C   1 
ATOM   2081 O O   . SER   C 1 31  ? 0.766   35.546  14.811  1.00 27.97 ? 45  SER   C O   1 
ATOM   2082 C CB  . SER   C 1 31  ? 1.572   33.019  16.455  1.00 23.01 ? 45  SER   C CB  1 
ATOM   2083 O OG  . SER   C 1 31  ? 1.417   32.021  15.463  1.00 23.11 ? 45  SER   C OG  1 
ATOM   2084 N N   . ALA   C 1 32  ? 2.266   34.433  13.545  1.00 29.11 ? 46  ALA   C N   1 
ATOM   2085 C CA  . ALA   C 1 32  ? 1.671   34.823  12.276  1.00 30.87 ? 46  ALA   C CA  1 
ATOM   2086 C C   . ALA   C 1 32  ? 0.569   33.877  11.821  1.00 32.33 ? 46  ALA   C C   1 
ATOM   2087 O O   . ALA   C 1 32  ? -0.074  34.148  10.800  1.00 34.91 ? 46  ALA   C O   1 
ATOM   2088 C CB  . ALA   C 1 32  ? 2.750   34.904  11.194  1.00 31.89 ? 46  ALA   C CB  1 
ATOM   2089 N N   . VAL   C 1 33  ? 0.336   32.775  12.540  1.00 31.68 ? 47  VAL   C N   1 
ATOM   2090 C CA  . VAL   C 1 33  ? -0.646  31.773  12.146  1.00 30.85 ? 47  VAL   C CA  1 
ATOM   2091 C C   . VAL   C 1 33  ? -1.424  31.302  13.369  1.00 28.75 ? 47  VAL   C C   1 
ATOM   2092 O O   . VAL   C 1 33  ? -1.003  31.478  14.515  1.00 27.71 ? 47  VAL   C O   1 
ATOM   2093 C CB  . VAL   C 1 33  ? -0.007  30.557  11.435  1.00 31.64 ? 47  VAL   C CB  1 
ATOM   2094 C CG1 . VAL   C 1 33  ? 0.631   30.968  10.107  1.00 32.22 ? 47  VAL   C CG1 1 
ATOM   2095 C CG2 . VAL   C 1 33  ? 1.013   29.884  12.346  1.00 31.50 ? 47  VAL   C CG2 1 
ATOM   2096 N N   . GLY   C 1 34  ? -2.582  30.696  13.102  1.00 27.61 ? 48  GLY   C N   1 
ATOM   2097 C CA  . GLY   C 1 34  ? -3.343  30.012  14.128  1.00 28.52 ? 48  GLY   C CA  1 
ATOM   2098 C C   . GLY   C 1 34  ? -4.261  30.915  14.927  1.00 30.01 ? 48  GLY   C C   1 
ATOM   2099 O O   . GLY   C 1 34  ? -4.418  32.113  14.672  1.00 29.90 ? 48  GLY   C O   1 
ATOM   2100 N N   . ASN   C 1 35  ? -4.886  30.297  15.933  1.00 30.94 ? 49  ASN   C N   1 
ATOM   2101 C CA  . ASN   C 1 35  ? -5.811  30.970  16.846  1.00 31.60 ? 49  ASN   C CA  1 
ATOM   2102 C C   . ASN   C 1 35  ? -5.001  31.774  17.865  1.00 31.57 ? 49  ASN   C C   1 
ATOM   2103 O O   . ASN   C 1 35  ? -4.927  31.459  19.056  1.00 32.31 ? 49  ASN   C O   1 
ATOM   2104 C CB  . ASN   C 1 35  ? -6.711  29.937  17.515  1.00 32.61 ? 49  ASN   C CB  1 
ATOM   2105 C CG  . ASN   C 1 35  ? -7.745  30.558  18.435  1.00 33.70 ? 49  ASN   C CG  1 
ATOM   2106 O OD1 . ASN   C 1 35  ? -7.982  31.767  18.402  1.00 34.84 ? 49  ASN   C OD1 1 
ATOM   2107 N ND2 . ASN   C 1 35  ? -8.374  29.726  19.263  1.00 33.30 ? 49  ASN   C ND2 1 
ATOM   2108 N N   . ALA   C 1 36  ? -4.379  32.841  17.365  1.00 30.59 ? 50  ALA   C N   1 
ATOM   2109 C CA  . ALA   C 1 36  ? -3.453  33.641  18.152  1.00 29.07 ? 50  ALA   C CA  1 
ATOM   2110 C C   . ALA   C 1 36  ? -3.563  35.104  17.749  1.00 29.47 ? 50  ALA   C C   1 
ATOM   2111 O O   . ALA   C 1 36  ? -3.806  35.429  16.583  1.00 29.75 ? 50  ALA   C O   1 
ATOM   2112 C CB  . ALA   C 1 36  ? -2.006  33.159  17.962  1.00 26.71 ? 50  ALA   C CB  1 
ATOM   2113 N N   . GLU   C 1 37  ? -3.377  35.983  18.729  1.00 29.77 ? 51  GLU   C N   1 
ATOM   2114 C CA  . GLU   C 1 37  ? -3.394  37.419  18.492  1.00 29.74 ? 51  GLU   C CA  1 
ATOM   2115 C C   . GLU   C 1 37  ? -2.586  38.088  19.593  1.00 28.65 ? 51  GLU   C C   1 
ATOM   2116 O O   . GLU   C 1 37  ? -2.631  37.657  20.749  1.00 28.60 ? 51  GLU   C O   1 
ATOM   2117 C CB  . GLU   C 1 37  ? -4.831  37.956  18.482  1.00 31.26 ? 51  GLU   C CB  1 
ATOM   2118 C CG  . GLU   C 1 37  ? -4.968  39.465  18.413  0.47 31.83 ? 51  GLU   C CG  1 
ATOM   2119 C CD  . GLU   C 1 37  ? -6.387  39.917  18.701  0.44 32.11 ? 51  GLU   C CD  1 
ATOM   2120 O OE1 . GLU   C 1 37  ? -7.229  39.053  19.029  0.76 32.35 ? 51  GLU   C OE1 1 
ATOM   2121 O OE2 . GLU   C 1 37  ? -6.662  41.132  18.602  0.52 32.00 ? 51  GLU   C OE2 1 
ATOM   2122 N N   . SER   C 1 38  ? -1.845  39.131  19.220  1.00 28.52 ? 52  SER   C N   1 
ATOM   2123 C CA  . SER   C 1 38  ? -0.985  39.861  20.145  1.00 29.33 ? 52  SER   C CA  1 
ATOM   2124 C C   . SER   C 1 38  ? 0.130   38.971  20.687  1.00 27.73 ? 52  SER   C C   1 
ATOM   2125 O O   . SER   C 1 38  ? 0.360   37.867  20.180  1.00 28.33 ? 52  SER   C O   1 
ATOM   2126 C CB  . SER   C 1 38  ? -1.798  40.490  21.283  1.00 31.38 ? 52  SER   C CB  1 
ATOM   2127 O OG  . SER   C 1 38  ? -1.000  41.371  22.054  1.00 32.64 ? 52  SER   C OG  1 
ATOM   2128 N N   . ARG   C 1 39  ? 0.831   39.457  21.706  1.00 25.98 ? 53  ARG   C N   1 
ATOM   2129 C CA  . ARG   C 1 39  ? 1.991   38.768  22.238  1.00 24.36 ? 53  ARG   C CA  1 
ATOM   2130 C C   . ARG   C 1 39  ? 1.577   37.727  23.270  1.00 19.99 ? 53  ARG   C C   1 
ATOM   2131 O O   . ARG   C 1 39  ? 0.557   37.862  23.958  1.00 19.99 ? 53  ARG   C O   1 
ATOM   2132 C CB  . ARG   C 1 39  ? 2.956   39.772  22.877  1.00 25.95 ? 53  ARG   C CB  1 
ATOM   2133 C CG  . ARG   C 1 39  ? 3.457   40.858  21.930  1.00 29.05 ? 53  ARG   C CG  1 
ATOM   2134 C CD  . ARG   C 1 39  ? 4.490   41.768  22.578  1.00 30.98 ? 53  ARG   C CD  1 
ATOM   2135 N NE  . ARG   C 1 39  ? 5.212   42.561  21.587  1.00 32.41 ? 53  ARG   C NE  1 
ATOM   2136 C CZ  . ARG   C 1 39  ? 6.084   43.518  21.878  1.00 32.32 ? 53  ARG   C CZ  1 
ATOM   2137 N NH1 . ARG   C 1 39  ? 6.371   43.837  23.130  1.00 32.92 ? 53  ARG   C NH1 1 
ATOM   2138 N NH2 . ARG   C 1 39  ? 6.685   44.173  20.888  1.00 31.78 ? 53  ARG   C NH2 1 
ATOM   2139 N N   . TYR   C 1 40  ? 2.384   36.674  23.358  1.00 17.01 ? 54  TYR   C N   1 
ATOM   2140 C CA  . TYR   C 1 40  ? 2.265   35.644  24.377  1.00 14.50 ? 54  TYR   C CA  1 
ATOM   2141 C C   . TYR   C 1 40  ? 3.603   35.506  25.091  1.00 14.10 ? 54  TYR   C C   1 
ATOM   2142 O O   . TYR   C 1 40  ? 4.660   35.727  24.495  1.00 15.25 ? 54  TYR   C O   1 
ATOM   2143 C CB  . TYR   C 1 40  ? 1.881   34.289  23.752  1.00 13.89 ? 54  TYR   C CB  1 
ATOM   2144 C CG  . TYR   C 1 40  ? 0.529   34.297  23.081  1.00 14.10 ? 54  TYR   C CG  1 
ATOM   2145 C CD1 . TYR   C 1 40  ? 0.364   34.817  21.800  1.00 15.19 ? 54  TYR   C CD1 1 
ATOM   2146 C CD2 . TYR   C 1 40  ? -0.583  33.786  23.730  1.00 13.81 ? 54  TYR   C CD2 1 
ATOM   2147 C CE1 . TYR   C 1 40  ? -0.881  34.838  21.196  1.00 15.98 ? 54  TYR   C CE1 1 
ATOM   2148 C CE2 . TYR   C 1 40  ? -1.830  33.802  23.140  1.00 14.68 ? 54  TYR   C CE2 1 
ATOM   2149 C CZ  . TYR   C 1 40  ? -1.978  34.322  21.869  1.00 16.15 ? 54  TYR   C CZ  1 
ATOM   2150 O OH  . TYR   C 1 40  ? -3.227  34.337  21.285  1.00 18.77 ? 54  TYR   C OH  1 
ATOM   2151 N N   . VAL   C 1 41  ? 3.550   35.146  26.377  1.00 13.80 ? 55  VAL   C N   1 
ATOM   2152 C CA  . VAL   C 1 41  ? 4.760   34.889  27.152  1.00 13.51 ? 55  VAL   C CA  1 
ATOM   2153 C C   . VAL   C 1 41  ? 5.448   33.622  26.651  1.00 12.29 ? 55  VAL   C C   1 
ATOM   2154 O O   . VAL   C 1 41  ? 4.794   32.617  26.331  1.00 12.48 ? 55  VAL   C O   1 
ATOM   2155 C CB  . VAL   C 1 41  ? 4.394   34.741  28.642  1.00 14.63 ? 55  VAL   C CB  1 
ATOM   2156 C CG1 . VAL   C 1 41  ? 5.596   34.262  29.455  1.00 13.50 ? 55  VAL   C CG1 1 
ATOM   2157 C CG2 . VAL   C 1 41  ? 3.859   36.055  29.222  1.00 16.24 ? 55  VAL   C CG2 1 
ATOM   2158 N N   . LEU   C 1 42  ? 6.781   33.648  26.607  1.00 12.77 ? 56  LEU   C N   1 
ATOM   2159 C CA  . LEU   C 1 42  ? 7.569   32.441  26.393  1.00 12.57 ? 56  LEU   C CA  1 
ATOM   2160 C C   . LEU   C 1 42  ? 8.632   32.310  27.476  1.00 13.04 ? 56  LEU   C C   1 
ATOM   2161 O O   . LEU   C 1 42  ? 9.120   33.308  28.011  1.00 13.20 ? 56  LEU   C O   1 
ATOM   2162 C CB  . LEU   C 1 42  ? 8.256   32.445  25.024  1.00 13.19 ? 56  LEU   C CB  1 
ATOM   2163 C CG  . LEU   C 1 42  ? 9.440   33.407  24.841  1.00 13.88 ? 56  LEU   C CG  1 
ATOM   2164 C CD1 . LEU   C 1 42  ? 10.791  32.754  25.156  1.00 13.18 ? 56  LEU   C CD1 1 
ATOM   2165 C CD2 . LEU   C 1 42  ? 9.438   33.986  23.425  1.00 16.11 ? 56  LEU   C CD2 1 
ATOM   2166 N N   . THR   C 1 43  ? 8.988   31.063  27.792  1.00 12.82 ? 57  THR   C N   1 
ATOM   2167 C CA  A THR   C 1 43  ? 10.153  30.783  28.615  0.21 12.39 ? 57  THR   C CA  1 
ATOM   2168 C CA  B THR   C 1 43  ? 10.138  30.763  28.640  0.79 11.94 ? 57  THR   C CA  1 
ATOM   2169 C C   . THR   C 1 43  ? 10.828  29.517  28.106  1.00 11.68 ? 57  THR   C C   1 
ATOM   2170 O O   . THR   C 1 43  ? 10.185  28.635  27.523  1.00 10.97 ? 57  THR   C O   1 
ATOM   2171 C CB  A THR   C 1 43  ? 9.792   30.663  30.102  0.21 13.24 ? 57  THR   C CB  1 
ATOM   2172 C CB  B THR   C 1 43  ? 9.800   30.554  30.141  0.79 14.57 ? 57  THR   C CB  1 
ATOM   2173 O OG1 A THR   C 1 43  ? 10.973  30.392  30.865  0.21 13.66 ? 57  THR   C OG1 1 
ATOM   2174 O OG1 B THR   C 1 43  ? 8.931   29.427  30.294  0.79 15.84 ? 57  THR   C OG1 1 
ATOM   2175 C CG2 A THR   C 1 43  ? 8.808   29.554  30.304  0.21 13.54 ? 57  THR   C CG2 1 
ATOM   2176 C CG2 B THR   C 1 43  ? 9.176   31.807  30.757  0.79 16.25 ? 57  THR   C CG2 1 
ATOM   2177 N N   . GLY   C 1 44  ? 12.134  29.448  28.320  1.00 11.83 ? 58  GLY   C N   1 
ATOM   2178 C CA  . GLY   C 1 44  ? 12.902  28.301  27.881  1.00 11.74 ? 58  GLY   C CA  1 
ATOM   2179 C C   . GLY   C 1 44  ? 14.302  28.308  28.456  1.00 11.08 ? 58  GLY   C C   1 
ATOM   2180 O O   . GLY   C 1 44  ? 14.586  29.014  29.428  1.00 11.26 ? 58  GLY   C O   1 
ATOM   2181 N N   . ARG   C 1 45  ? 15.181  27.519  27.826  1.00 11.59 ? 59  ARG   C N   1 
ATOM   2182 C CA  . ARG   C 1 45  ? 16.544  27.307  28.301  1.00 12.16 ? 59  ARG   C CA  1 
ATOM   2183 C C   . ARG   C 1 45  ? 17.479  27.197  27.104  1.00 12.19 ? 59  ARG   C C   1 
ATOM   2184 O O   . ARG   C 1 45  ? 17.062  26.806  26.011  1.00 12.49 ? 59  ARG   C O   1 
ATOM   2185 C CB  . ARG   C 1 45  ? 16.683  26.005  29.110  1.00 12.64 ? 59  ARG   C CB  1 
ATOM   2186 C CG  . ARG   C 1 45  ? 15.776  25.887  30.335  1.00 13.12 ? 59  ARG   C CG  1 
ATOM   2187 C CD  . ARG   C 1 45  ? 16.210  26.813  31.475  1.00 13.39 ? 59  ARG   C CD  1 
ATOM   2188 N NE  . ARG   C 1 45  ? 17.529  26.445  31.972  1.00 12.69 ? 59  ARG   C NE  1 
ATOM   2189 C CZ  . ARG   C 1 45  ? 18.279  27.209  32.750  1.00 13.31 ? 59  ARG   C CZ  1 
ATOM   2190 N NH1 . ARG   C 1 45  ? 17.860  28.395  33.169  1.00 14.22 ? 59  ARG   C NH1 1 
ATOM   2191 N NH2 . ARG   C 1 45  ? 19.476  26.770  33.122  1.00 14.29 ? 59  ARG   C NH2 1 
ATOM   2192 N N   . TYR   C 1 46  ? 18.749  27.547  27.313  1.00 12.83 ? 60  TYR   C N   1 
ATOM   2193 C CA  . TYR   C 1 46  ? 19.771  27.404  26.281  1.00 12.84 ? 60  TYR   C CA  1 
ATOM   2194 C C   . TYR   C 1 46  ? 21.080  27.001  26.951  1.00 12.41 ? 60  TYR   C C   1 
ATOM   2195 O O   . TYR   C 1 46  ? 21.267  27.209  28.155  1.00 13.55 ? 60  TYR   C O   1 
ATOM   2196 C CB  . TYR   C 1 46  ? 19.951  28.703  25.460  1.00 13.85 ? 60  TYR   C CB  1 
ATOM   2197 C CG  . TYR   C 1 46  ? 20.710  29.794  26.188  1.00 13.97 ? 60  TYR   C CG  1 
ATOM   2198 C CD1 . TYR   C 1 46  ? 20.124  30.505  27.236  1.00 15.18 ? 60  TYR   C CD1 1 
ATOM   2199 C CD2 . TYR   C 1 46  ? 22.025  30.101  25.849  1.00 15.43 ? 60  TYR   C CD2 1 
ATOM   2200 C CE1 . TYR   C 1 46  ? 20.828  31.499  27.924  1.00 16.17 ? 60  TYR   C CE1 1 
ATOM   2201 C CE2 . TYR   C 1 46  ? 22.731  31.084  26.528  1.00 16.92 ? 60  TYR   C CE2 1 
ATOM   2202 C CZ  . TYR   C 1 46  ? 22.129  31.782  27.560  1.00 16.70 ? 60  TYR   C CZ  1 
ATOM   2203 O OH  . TYR   C 1 46  ? 22.836  32.764  28.229  1.00 19.78 ? 60  TYR   C OH  1 
ATOM   2204 N N   . ASP   C 1 47  ? 21.987  26.417  26.162  1.00 13.03 ? 61  ASP   C N   1 
ATOM   2205 C CA  . ASP   C 1 47  ? 23.329  26.061  26.634  1.00 13.54 ? 61  ASP   C CA  1 
ATOM   2206 C C   . ASP   C 1 47  ? 24.165  27.331  26.764  1.00 13.68 ? 61  ASP   C C   1 
ATOM   2207 O O   . ASP   C 1 47  ? 24.555  27.935  25.759  1.00 14.91 ? 61  ASP   C O   1 
ATOM   2208 C CB  . ASP   C 1 47  ? 23.957  25.076  25.647  1.00 12.91 ? 61  ASP   C CB  1 
ATOM   2209 C CG  . ASP   C 1 47  ? 25.381  24.664  26.023  1.00 13.45 ? 61  ASP   C CG  1 
ATOM   2210 O OD1 . ASP   C 1 47  ? 25.900  25.079  27.087  1.00 14.70 ? 61  ASP   C OD1 1 
ATOM   2211 O OD2 . ASP   C 1 47  ? 25.992  23.908  25.222  1.00 13.63 ? 61  ASP   C OD2 1 
ATOM   2212 N N   . SER   C 1 48  ? 24.451  27.736  28.005  1.00 14.40 ? 62  SER   C N   1 
ATOM   2213 C CA  . SER   C 1 48  ? 25.186  28.972  28.258  1.00 15.59 ? 62  SER   C CA  1 
ATOM   2214 C C   . SER   C 1 48  ? 26.692  28.818  28.095  1.00 16.31 ? 62  SER   C C   1 
ATOM   2215 O O   . SER   C 1 48  ? 27.413  29.809  28.249  1.00 17.51 ? 62  SER   C O   1 
ATOM   2216 C CB  . SER   C 1 48  ? 24.866  29.506  29.654  1.00 17.93 ? 62  SER   C CB  1 
ATOM   2217 O OG  . SER   C 1 48  ? 25.259  28.570  30.634  1.00 19.97 ? 62  SER   C OG  1 
ATOM   2218 N N   . ALA   C 1 49  ? 27.194  27.618  27.811  1.00 15.84 ? 63  ALA   C N   1 
ATOM   2219 C CA  . ALA   C 1 49  ? 28.626  27.402  27.574  1.00 16.80 ? 63  ALA   C CA  1 
ATOM   2220 C C   . ALA   C 1 49  ? 28.807  26.413  26.431  1.00 16.19 ? 63  ALA   C C   1 
ATOM   2221 O O   . ALA   C 1 49  ? 29.216  25.266  26.636  1.00 16.36 ? 63  ALA   C O   1 
ATOM   2222 C CB  . ALA   C 1 49  ? 29.324  26.917  28.845  1.00 18.37 ? 63  ALA   C CB  1 
ATOM   2223 N N   . PRO   C 1 50  ? 28.512  26.835  25.202  1.00 16.37 ? 64  PRO   C N   1 
ATOM   2224 C CA  . PRO   C 1 50  ? 28.568  25.907  24.069  1.00 15.90 ? 64  PRO   C CA  1 
ATOM   2225 C C   . PRO   C 1 50  ? 29.992  25.465  23.776  1.00 16.95 ? 64  PRO   C C   1 
ATOM   2226 O O   . PRO   C 1 50  ? 30.978  26.017  24.273  1.00 17.50 ? 64  PRO   C O   1 
ATOM   2227 C CB  . PRO   C 1 50  ? 28.001  26.731  22.909  1.00 16.34 ? 64  PRO   C CB  1 
ATOM   2228 C CG  . PRO   C 1 50  ? 28.241  28.164  23.310  1.00 17.97 ? 64  PRO   C CG  1 
ATOM   2229 C CD  . PRO   C 1 50  ? 28.047  28.174  24.798  1.00 17.52 ? 64  PRO   C CD  1 
ATOM   2230 N N   . ALA   C 1 51  ? 30.083  24.439  22.937  1.00 16.76 ? 65  ALA   C N   1 
ATOM   2231 C CA  . ALA   C 1 51  ? 31.372  23.980  22.459  1.00 17.43 ? 65  ALA   C CA  1 
ATOM   2232 C C   . ALA   C 1 51  ? 32.078  25.087  21.681  1.00 18.98 ? 65  ALA   C C   1 
ATOM   2233 O O   . ALA   C 1 51  ? 31.462  26.044  21.205  1.00 19.37 ? 65  ALA   C O   1 
ATOM   2234 C CB  . ALA   C 1 51  ? 31.191  22.750  21.575  1.00 17.85 ? 65  ALA   C CB  1 
ATOM   2235 N N   . THR   C 1 52  ? 33.394  24.953  21.574  1.00 19.84 ? 66  THR   C N   1 
ATOM   2236 C CA  . THR   C 1 52  ? 34.245  25.907  20.869  1.00 20.28 ? 66  THR   C CA  1 
ATOM   2237 C C   . THR   C 1 52  ? 34.882  25.277  19.632  1.00 20.97 ? 66  THR   C C   1 
ATOM   2238 O O   . THR   C 1 52  ? 36.034  25.549  19.298  1.00 23.07 ? 66  THR   C O   1 
ATOM   2239 C CB  . THR   C 1 52  ? 35.300  26.494  21.805  1.00 21.75 ? 66  THR   C CB  1 
ATOM   2240 O OG1 . THR   C 1 52  ? 36.011  25.432  22.452  1.00 21.79 ? 66  THR   C OG1 1 
ATOM   2241 C CG2 . THR   C 1 52  ? 34.647  27.369  22.870  1.00 22.75 ? 66  THR   C CG2 1 
ATOM   2242 N N   . ASP   C 1 53  ? 34.121  24.425  18.942  1.00 21.17 ? 67  ASP   C N   1 
ATOM   2243 C CA  . ASP   C 1 53  ? 34.594  23.704  17.765  1.00 23.10 ? 67  ASP   C CA  1 
ATOM   2244 C C   . ASP   C 1 53  ? 33.785  24.038  16.514  1.00 23.14 ? 67  ASP   C C   1 
ATOM   2245 O O   . ASP   C 1 53  ? 33.867  23.312  15.516  1.00 26.01 ? 67  ASP   C O   1 
ATOM   2246 C CB  . ASP   C 1 53  ? 34.569  22.194  18.018  1.00 24.50 ? 67  ASP   C CB  1 
ATOM   2247 C CG  . ASP   C 1 53  ? 33.155  21.651  18.195  1.00 26.84 ? 67  ASP   C CG  1 
ATOM   2248 O OD1 . ASP   C 1 53  ? 32.200  22.454  18.298  1.00 23.73 ? 67  ASP   C OD1 1 
ATOM   2249 O OD2 . ASP   C 1 53  ? 32.996  20.411  18.222  1.00 30.60 ? 67  ASP   C OD2 1 
ATOM   2250 N N   . GLY   C 1 54  ? 32.997  25.111  16.548  1.00 21.91 ? 68  GLY   C N   1 
ATOM   2251 C CA  . GLY   C 1 54  ? 32.139  25.474  15.439  1.00 21.02 ? 68  GLY   C CA  1 
ATOM   2252 C C   . GLY   C 1 54  ? 30.713  24.970  15.528  1.00 20.79 ? 68  GLY   C C   1 
ATOM   2253 O O   . GLY   C 1 54  ? 29.904  25.289  14.645  1.00 22.40 ? 68  GLY   C O   1 
ATOM   2254 N N   . SER   C 1 55  ? 30.377  24.197  16.558  1.00 19.52 ? 69  SER   C N   1 
ATOM   2255 C CA  . SER   C 1 55  ? 29.022  23.690  16.732  1.00 19.00 ? 69  SER   C CA  1 
ATOM   2256 C C   . SER   C 1 55  ? 28.067  24.810  17.150  1.00 17.51 ? 69  SER   C C   1 
ATOM   2257 O O   . SER   C 1 55  ? 28.466  25.819  17.739  1.00 17.48 ? 69  SER   C O   1 
ATOM   2258 C CB  . SER   C 1 55  ? 29.009  22.597  17.802  1.00 22.25 ? 69  SER   C CB  1 
ATOM   2259 O OG  . SER   C 1 55  ? 29.791  21.481  17.413  1.00 25.90 ? 69  SER   C OG  1 
ATOM   2260 N N   . GLY   C 1 56  ? 26.781  24.613  16.850  1.00 16.38 ? 70  GLY   C N   1 
ATOM   2261 C CA  . GLY   C 1 56  ? 25.751  25.541  17.268  1.00 15.15 ? 70  GLY   C CA  1 
ATOM   2262 C C   . GLY   C 1 56  ? 25.449  25.435  18.756  1.00 14.30 ? 70  GLY   C C   1 
ATOM   2263 O O   . GLY   C 1 56  ? 25.977  24.585  19.473  1.00 15.24 ? 70  GLY   C O   1 
ATOM   2264 N N   . THR   C 1 57  ? 24.575  26.325  19.220  1.00 14.30 ? 71  THR   C N   1 
ATOM   2265 C CA  . THR   C 1 57  ? 24.173  26.404  20.624  1.00 13.14 ? 71  THR   C CA  1 
ATOM   2266 C C   . THR   C 1 57  ? 22.759  25.846  20.771  1.00 12.56 ? 71  THR   C C   1 
ATOM   2267 O O   . THR   C 1 57  ? 21.812  26.423  20.234  1.00 13.16 ? 71  THR   C O   1 
ATOM   2268 C CB  . THR   C 1 57  ? 24.197  27.858  21.105  1.00 14.28 ? 71  THR   C CB  1 
ATOM   2269 O OG1 . THR   C 1 57  ? 25.513  28.399  20.955  1.00 15.36 ? 71  THR   C OG1 1 
ATOM   2270 C CG2 . THR   C 1 57  ? 23.768  27.952  22.563  1.00 15.07 ? 71  THR   C CG2 1 
ATOM   2271 N N   . ALA   C 1 58  ? 22.613  24.755  21.524  1.00 12.93 ? 72  ALA   C N   1 
ATOM   2272 C CA  . ALA   C 1 58  ? 21.304  24.127  21.691  1.00 12.38 ? 72  ALA   C CA  1 
ATOM   2273 C C   . ALA   C 1 58  ? 20.385  24.971  22.575  1.00 12.35 ? 72  ALA   C C   1 
ATOM   2274 O O   . ALA   C 1 58  ? 20.828  25.593  23.548  1.00 12.53 ? 72  ALA   C O   1 
ATOM   2275 C CB  . ALA   C 1 58  ? 21.471  22.737  22.302  1.00 12.39 ? 72  ALA   C CB  1 
ATOM   2276 N N   . LEU   C 1 59  ? 19.092  24.963  22.258  1.00 11.45 ? 73  LEU   C N   1 
ATOM   2277 C CA  A LEU   C 1 59  ? 18.117  25.751  23.003  0.45 11.48 ? 73  LEU   C CA  1 
ATOM   2278 C CA  B LEU   C 1 59  ? 18.118  25.748  23.008  0.55 11.52 ? 73  LEU   C CA  1 
ATOM   2279 C C   . LEU   C 1 59  ? 16.718  25.193  22.775  1.00 10.95 ? 73  LEU   C C   1 
ATOM   2280 O O   . LEU   C 1 59  ? 16.482  24.393  21.865  1.00 11.80 ? 73  LEU   C O   1 
ATOM   2281 C CB  A LEU   C 1 59  ? 18.182  27.233  22.613  0.45 12.31 ? 73  LEU   C CB  1 
ATOM   2282 C CB  B LEU   C 1 59  ? 18.187  27.244  22.650  0.55 12.59 ? 73  LEU   C CB  1 
ATOM   2283 C CG  A LEU   C 1 59  ? 18.191  27.584  21.119  0.45 13.54 ? 73  LEU   C CG  1 
ATOM   2284 C CG  B LEU   C 1 59  ? 17.472  27.794  21.404  0.55 14.13 ? 73  LEU   C CG  1 
ATOM   2285 C CD1 A LEU   C 1 59  ? 16.832  27.386  20.454  0.45 14.10 ? 73  LEU   C CD1 1 
ATOM   2286 C CD1 B LEU   C 1 59  ? 17.621  29.312  21.312  0.55 14.81 ? 73  LEU   C CD1 1 
ATOM   2287 C CD2 A LEU   C 1 59  ? 18.651  29.014  20.930  0.45 13.91 ? 73  LEU   C CD2 1 
ATOM   2288 C CD2 B LEU   C 1 59  ? 17.983  27.151  20.128  0.55 14.64 ? 73  LEU   C CD2 1 
ATOM   2289 N N   . GLY   C 1 60  ? 15.777  25.651  23.605  1.00 10.50 ? 74  GLY   C N   1 
ATOM   2290 C CA  . GLY   C 1 60  ? 14.368  25.345  23.430  1.00 10.38 ? 74  GLY   C CA  1 
ATOM   2291 C C   . GLY   C 1 60  ? 13.503  26.317  24.198  1.00 10.20 ? 74  GLY   C C   1 
ATOM   2292 O O   . GLY   C 1 60  ? 13.956  26.922  25.172  1.00 10.38 ? 74  GLY   C O   1 
ATOM   2293 N N   . TRP   C 1 61  ? 12.246  26.467  23.766  1.00 10.50 ? 75  TRP   C N   1 
ATOM   2294 C CA  . TRP   C 1 61  ? 11.317  27.310  24.523  1.00 9.72  ? 75  TRP   C CA  1 
ATOM   2295 C C   . TRP   C 1 61  ? 9.877   26.874  24.277  1.00 9.17  ? 75  TRP   C C   1 
ATOM   2296 O O   . TRP   C 1 61  ? 9.584   26.141  23.327  1.00 9.65  ? 75  TRP   C O   1 
ATOM   2297 C CB  . TRP   C 1 61  ? 11.506  28.813  24.236  1.00 9.96  ? 75  TRP   C CB  1 
ATOM   2298 C CG  . TRP   C 1 61  ? 11.080  29.248  22.833  1.00 10.93 ? 75  TRP   C CG  1 
ATOM   2299 C CD1 . TRP   C 1 61  ? 9.871   29.779  22.478  1.00 11.12 ? 75  TRP   C CD1 1 
ATOM   2300 C CD2 . TRP   C 1 61  ? 11.877  29.233  21.632  1.00 11.56 ? 75  TRP   C CD2 1 
ATOM   2301 N NE1 . TRP   C 1 61  ? 9.856   30.078  21.132  1.00 12.51 ? 75  TRP   C NE1 1 
ATOM   2302 C CE2 . TRP   C 1 61  ? 11.071  29.747  20.590  1.00 12.09 ? 75  TRP   C CE2 1 
ATOM   2303 C CE3 . TRP   C 1 61  ? 13.183  28.819  21.330  1.00 12.58 ? 75  TRP   C CE3 1 
ATOM   2304 C CZ2 . TRP   C 1 61  ? 11.528  29.862  19.271  1.00 13.07 ? 75  TRP   C CZ2 1 
ATOM   2305 C CZ3 . TRP   C 1 61  ? 13.636  28.935  20.010  1.00 13.40 ? 75  TRP   C CZ3 1 
ATOM   2306 C CH2 . TRP   C 1 61  ? 12.807  29.451  19.003  1.00 13.19 ? 75  TRP   C CH2 1 
ATOM   2307 N N   . THR   C 1 62  ? 8.971   27.350  25.149  1.00 9.32  ? 76  THR   C N   1 
ATOM   2308 C CA  . THR   C 1 62  ? 7.548   27.022  25.115  1.00 9.05  ? 76  THR   C CA  1 
ATOM   2309 C C   . THR   C 1 62  ? 6.706   28.293  25.119  1.00 9.92  ? 76  THR   C C   1 
ATOM   2310 O O   . THR   C 1 62  ? 7.034   29.260  25.813  1.00 10.47 ? 76  THR   C O   1 
ATOM   2311 C CB  . THR   C 1 62  ? 7.155   26.189  26.362  1.00 10.19 ? 76  THR   C CB  1 
ATOM   2312 O OG1 . THR   C 1 62  ? 7.968   25.012  26.440  1.00 10.33 ? 76  THR   C OG1 1 
ATOM   2313 C CG2 . THR   C 1 62  ? 5.698   25.757  26.318  1.00 10.29 ? 76  THR   C CG2 1 
ATOM   2314 N N   . VAL   C 1 63  ? 5.608   28.275  24.353  1.00 10.03 ? 77  VAL   C N   1 
ATOM   2315 C CA  . VAL   C 1 63  ? 4.512   29.235  24.466  1.00 10.58 ? 77  VAL   C CA  1 
ATOM   2316 C C   . VAL   C 1 63  ? 3.226   28.460  24.720  1.00 10.86 ? 77  VAL   C C   1 
ATOM   2317 O O   . VAL   C 1 63  ? 2.886   27.557  23.944  1.00 11.09 ? 77  VAL   C O   1 
ATOM   2318 C CB  . VAL   C 1 63  ? 4.359   30.062  23.176  1.00 12.07 ? 77  VAL   C CB  1 
ATOM   2319 C CG1 . VAL   C 1 63  ? 3.056   30.889  23.209  1.00 12.94 ? 77  VAL   C CG1 1 
ATOM   2320 C CG2 . VAL   C 1 63  ? 5.574   30.942  22.960  1.00 12.72 ? 77  VAL   C CG2 1 
ATOM   2321 N N   . ALA   C 1 64  ? 2.516   28.801  25.805  1.00 10.44 ? 78  ALA   C N   1 
ATOM   2322 C CA  . ALA   C 1 64  ? 1.129   28.386  25.978  1.00 10.72 ? 78  ALA   C CA  1 
ATOM   2323 C C   . ALA   C 1 64  ? 0.243   29.475  25.385  1.00 10.54 ? 78  ALA   C C   1 
ATOM   2324 O O   . ALA   C 1 64  ? 0.417   30.659  25.698  1.00 11.66 ? 78  ALA   C O   1 
ATOM   2325 C CB  . ALA   C 1 64  ? 0.802   28.169  27.460  1.00 11.75 ? 78  ALA   C CB  1 
ATOM   2326 N N   . TRP   C 1 65  ? -0.699  29.078  24.524  1.00 11.78 ? 79  TRP   C N   1 
ATOM   2327 C CA  . TRP   C 1 65  ? -1.450  30.030  23.706  1.00 11.69 ? 79  TRP   C CA  1 
ATOM   2328 C C   . TRP   C 1 65  ? -2.624  30.652  24.457  1.00 12.26 ? 79  TRP   C C   1 
ATOM   2329 O O   . TRP   C 1 65  ? -3.766  30.648  23.976  1.00 13.48 ? 79  TRP   C O   1 
ATOM   2330 C CB  . TRP   C 1 65  ? -1.860  29.391  22.373  1.00 12.12 ? 79  TRP   C CB  1 
ATOM   2331 C CG  . TRP   C 1 65  ? -0.651  28.997  21.566  1.00 10.89 ? 79  TRP   C CG  1 
ATOM   2332 C CD1 . TRP   C 1 65  ? -0.182  27.727  21.357  1.00 10.87 ? 79  TRP   C CD1 1 
ATOM   2333 C CD2 . TRP   C 1 65  ? 0.273   29.879  20.903  1.00 12.23 ? 79  TRP   C CD2 1 
ATOM   2334 N NE1 . TRP   C 1 65  ? 0.970   27.762  20.601  1.00 11.45 ? 79  TRP   C NE1 1 
ATOM   2335 C CE2 . TRP   C 1 65  ? 1.265   29.070  20.302  1.00 11.71 ? 79  TRP   C CE2 1 
ATOM   2336 C CE3 . TRP   C 1 65  ? 0.349   31.272  20.744  1.00 12.62 ? 79  TRP   C CE3 1 
ATOM   2337 C CZ2 . TRP   C 1 65  ? 2.318   29.607  19.556  1.00 12.26 ? 79  TRP   C CZ2 1 
ATOM   2338 C CZ3 . TRP   C 1 65  ? 1.398   31.801  20.001  1.00 13.72 ? 79  TRP   C CZ3 1 
ATOM   2339 C CH2 . TRP   C 1 65  ? 2.367   30.970  19.415  1.00 13.98 ? 79  TRP   C CH2 1 
ATOM   2340 N N   . LYS   C 1 66  ? -2.337  31.191  25.644  1.00 13.27 ? 80  LYS   C N   1 
ATOM   2341 C CA  . LYS   C 1 66  ? -3.279  31.960  26.444  1.00 13.72 ? 80  LYS   C CA  1 
ATOM   2342 C C   . LYS   C 1 66  ? -2.670  33.325  26.732  1.00 13.76 ? 80  LYS   C C   1 
ATOM   2343 O O   . LYS   C 1 66  ? -1.512  33.414  27.162  1.00 13.89 ? 80  LYS   C O   1 
ATOM   2344 C CB  . LYS   C 1 66  ? -3.577  31.258  27.776  1.00 14.72 ? 80  LYS   C CB  1 
ATOM   2345 C CG  . LYS   C 1 66  ? -4.418  32.092  28.735  1.00 15.77 ? 80  LYS   C CG  1 
ATOM   2346 C CD  . LYS   C 1 66  ? -4.592  31.395  30.075  1.00 18.05 ? 80  LYS   C CD  1 
ATOM   2347 C CE  . LYS   C 1 66  ? -5.301  32.291  31.084  1.00 20.66 ? 80  LYS   C CE  1 
ATOM   2348 N NZ  . LYS   C 1 66  ? -4.393  33.382  31.576  1.00 23.47 ? 80  LYS   C NZ  1 
ATOM   2349 N N   . ASN   C 1 67  ? -3.439  34.379  26.484  1.00 14.60 ? 81  ASN   C N   1 
ATOM   2350 C CA  . ASN   C 1 67  ? -3.080  35.726  26.922  1.00 16.49 ? 81  ASN   C CA  1 
ATOM   2351 C C   . ASN   C 1 67  ? -4.366  36.415  27.358  1.00 20.09 ? 81  ASN   C C   1 
ATOM   2352 O O   . ASN   C 1 67  ? -5.408  35.772  27.515  1.00 21.44 ? 81  ASN   C O   1 
ATOM   2353 C CB  . ASN   C 1 67  ? -2.246  36.474  25.865  1.00 17.18 ? 81  ASN   C CB  1 
ATOM   2354 C CG  . ASN   C 1 67  ? -3.021  36.775  24.589  1.00 18.07 ? 81  ASN   C CG  1 
ATOM   2355 O OD1 . ASN   C 1 67  ? -4.243  36.627  24.524  1.00 19.46 ? 81  ASN   C OD1 1 
ATOM   2356 N ND2 . ASN   C 1 67  ? -2.300  37.200  23.559  1.00 19.06 ? 81  ASN   C ND2 1 
ATOM   2357 N N   . ASN   C 1 68  ? -4.314  37.737  27.529  1.00 22.86 ? 82  ASN   C N   1 
ATOM   2358 C CA  . ASN   C 1 68  ? -5.495  38.455  27.999  1.00 26.38 ? 82  ASN   C CA  1 
ATOM   2359 C C   . ASN   C 1 68  ? -6.591  38.575  26.950  1.00 28.03 ? 82  ASN   C C   1 
ATOM   2360 O O   . ASN   C 1 68  ? -7.673  39.075  27.272  1.00 29.88 ? 82  ASN   C O   1 
ATOM   2361 C CB  . ASN   C 1 68  ? -5.117  39.850  28.498  1.00 28.29 ? 82  ASN   C CB  1 
ATOM   2362 C CG  . ASN   C 1 68  ? -4.435  39.810  29.838  1.00 29.97 ? 82  ASN   C CG  1 
ATOM   2363 O OD1 . ASN   C 1 68  ? -4.511  38.808  30.548  1.00 32.05 ? 82  ASN   C OD1 1 
ATOM   2364 N ND2 . ASN   C 1 68  ? -3.772  40.903  30.203  1.00 30.20 ? 82  ASN   C ND2 1 
ATOM   2365 N N   . TYR   C 1 69  ? -6.345  38.151  25.719  1.00 28.67 ? 83  TYR   C N   1 
ATOM   2366 C CA  . TYR   C 1 69  ? -7.303  38.319  24.637  1.00 29.90 ? 83  TYR   C CA  1 
ATOM   2367 C C   . TYR   C 1 69  ? -7.868  37.011  24.103  1.00 27.65 ? 83  TYR   C C   1 
ATOM   2368 O O   . TYR   C 1 69  ? -9.002  37.002  23.621  1.00 28.24 ? 83  TYR   C O   1 
ATOM   2369 C CB  . TYR   C 1 69  ? -6.654  39.105  23.490  1.00 33.82 ? 83  TYR   C CB  1 
ATOM   2370 C CG  . TYR   C 1 69  ? -5.879  40.307  23.988  1.00 38.26 ? 83  TYR   C CG  1 
ATOM   2371 C CD1 . TYR   C 1 69  ? -6.467  41.222  24.854  1.00 40.94 ? 83  TYR   C CD1 1 
ATOM   2372 C CD2 . TYR   C 1 69  ? -4.553  40.508  23.623  1.00 40.01 ? 83  TYR   C CD2 1 
ATOM   2373 C CE1 . TYR   C 1 69  ? -5.765  42.315  25.327  1.00 42.63 ? 83  TYR   C CE1 1 
ATOM   2374 C CE2 . TYR   C 1 69  ? -3.841  41.600  24.092  1.00 41.72 ? 83  TYR   C CE2 1 
ATOM   2375 C CZ  . TYR   C 1 69  ? -4.453  42.500  24.945  1.00 43.48 ? 83  TYR   C CZ  1 
ATOM   2376 O OH  . TYR   C 1 69  ? -3.758  43.591  25.419  1.00 45.01 ? 83  TYR   C OH  1 
ATOM   2377 N N   . ARG   C 1 70  ? -7.120  35.910  24.185  1.00 24.92 ? 84  ARG   C N   1 
ATOM   2378 C CA  . ARG   C 1 70  ? -7.547  34.640  23.615  1.00 24.05 ? 84  ARG   C CA  1 
ATOM   2379 C C   . ARG   C 1 70  ? -6.972  33.492  24.432  1.00 19.80 ? 84  ARG   C C   1 
ATOM   2380 O O   . ARG   C 1 70  ? -5.985  33.646  25.156  1.00 19.91 ? 84  ARG   C O   1 
ATOM   2381 C CB  . ARG   C 1 70  ? -7.066  34.481  22.167  1.00 27.12 ? 84  ARG   C CB  1 
ATOM   2382 C CG  . ARG   C 1 70  ? -7.689  35.445  21.175  1.00 31.20 ? 84  ARG   C CG  1 
ATOM   2383 C CD  . ARG   C 1 70  ? -6.808  35.567  19.954  1.00 35.48 ? 84  ARG   C CD  1 
ATOM   2384 N NE  . ARG   C 1 70  ? -7.186  34.663  18.876  1.00 38.79 ? 84  ARG   C NE  1 
ATOM   2385 C CZ  . ARG   C 1 70  ? -7.715  35.058  17.725  1.00 40.58 ? 84  ARG   C CZ  1 
ATOM   2386 N NH1 . ARG   C 1 70  ? -7.951  36.336  17.476  1.00 41.38 ? 84  ARG   C NH1 1 
ATOM   2387 N NH2 . ARG   C 1 70  ? -8.006  34.149  16.798  1.00 40.89 ? 84  ARG   C NH2 1 
ATOM   2388 N N   . ASN   C 1 71  ? -7.597  32.324  24.291  1.00 17.94 ? 85  ASN   C N   1 
ATOM   2389 C CA  . ASN   C 1 71  ? -7.044  31.081  24.826  1.00 16.57 ? 85  ASN   C CA  1 
ATOM   2390 C C   . ASN   C 1 71  ? -7.391  29.955  23.863  1.00 16.78 ? 85  ASN   C C   1 
ATOM   2391 O O   . ASN   C 1 71  ? -8.563  29.592  23.721  1.00 18.16 ? 85  ASN   C O   1 
ATOM   2392 C CB  . ASN   C 1 71  ? -7.576  30.770  26.224  1.00 16.33 ? 85  ASN   C CB  1 
ATOM   2393 C CG  . ASN   C 1 71  ? -6.803  29.647  26.905  1.00 15.20 ? 85  ASN   C CG  1 
ATOM   2394 O OD1 . ASN   C 1 71  ? -5.972  28.977  26.279  1.00 15.09 ? 85  ASN   C OD1 1 
ATOM   2395 N ND2 . ASN   C 1 71  ? -7.064  29.439  28.193  1.00 16.40 ? 85  ASN   C ND2 1 
ATOM   2396 N N   . ALA   C 1 72  ? -6.375  29.394  23.217  1.00 15.45 ? 86  ALA   C N   1 
ATOM   2397 C CA  . ALA   C 1 72  ? -6.562  28.295  22.280  1.00 15.06 ? 86  ALA   C CA  1 
ATOM   2398 C C   . ALA   C 1 72  ? -6.458  26.928  22.944  1.00 14.14 ? 86  ALA   C C   1 
ATOM   2399 O O   . ALA   C 1 72  ? -6.660  25.912  22.269  1.00 14.89 ? 86  ALA   C O   1 
ATOM   2400 C CB  . ALA   C 1 72  ? -5.551  28.397  21.132  1.00 15.51 ? 86  ALA   C CB  1 
ATOM   2401 N N   . HIS   C 1 73  ? -6.152  26.877  24.242  1.00 13.55 ? 87  HIS   C N   1 
ATOM   2402 C CA  . HIS   C 1 73  ? -5.995  25.622  24.981  1.00 13.13 ? 87  HIS   C CA  1 
ATOM   2403 C C   . HIS   C 1 73  ? -4.992  24.695  24.284  1.00 12.20 ? 87  HIS   C C   1 
ATOM   2404 O O   . HIS   C 1 73  ? -5.302  23.554  23.913  1.00 12.22 ? 87  HIS   C O   1 
ATOM   2405 C CB  . HIS   C 1 73  ? -7.338  24.914  25.202  1.00 13.99 ? 87  HIS   C CB  1 
ATOM   2406 C CG  . HIS   C 1 73  ? -8.385  25.756  25.874  1.00 14.41 ? 87  HIS   C CG  1 
ATOM   2407 N ND1 . HIS   C 1 73  ? -8.206  26.324  27.118  1.00 15.10 ? 87  HIS   C ND1 1 
ATOM   2408 C CD2 . HIS   C 1 73  ? -9.638  26.092  25.484  1.00 17.05 ? 87  HIS   C CD2 1 
ATOM   2409 C CE1 . HIS   C 1 73  ? -9.296  26.990  27.457  1.00 16.40 ? 87  HIS   C CE1 1 
ATOM   2410 N NE2 . HIS   C 1 73  ? -10.181 26.859  26.486  1.00 17.23 ? 87  HIS   C NE2 1 
ATOM   2411 N N   . SER   C 1 74  ? -3.771  25.209  24.128  1.00 11.87 ? 88  SER   C N   1 
ATOM   2412 C CA  . SER   C 1 74  ? -2.716  24.537  23.371  1.00 10.93 ? 88  SER   C CA  1 
ATOM   2413 C C   . SER   C 1 74  ? -1.375  25.162  23.739  1.00 10.93 ? 88  SER   C C   1 
ATOM   2414 O O   . SER   C 1 74  ? -1.313  26.245  24.328  1.00 11.41 ? 88  SER   C O   1 
ATOM   2415 C CB  . SER   C 1 74  ? -2.967  24.626  21.866  1.00 12.76 ? 88  SER   C CB  1 
ATOM   2416 O OG  . SER   C 1 74  ? -2.921  25.973  21.449  1.00 14.77 ? 88  SER   C OG  1 
ATOM   2417 N N   . ALA   C 1 75  ? -0.292  24.474  23.369  1.00 11.22 ? 89  ALA   C N   1 
ATOM   2418 C CA  . ALA   C 1 75  ? 1.053   24.962  23.651  1.00 10.53 ? 89  ALA   C CA  1 
ATOM   2419 C C   . ALA   C 1 75  ? 2.018   24.450  22.584  1.00 10.46 ? 89  ALA   C C   1 
ATOM   2420 O O   . ALA   C 1 75  ? 1.911   23.297  22.154  1.00 10.69 ? 89  ALA   C O   1 
ATOM   2421 C CB  . ALA   C 1 75  ? 1.529   24.528  25.046  1.00 11.48 ? 89  ALA   C CB  1 
ATOM   2422 N N   . THR   C 1 76  ? 2.970   25.295  22.180  1.00 9.77  ? 90  THR   C N   1 
ATOM   2423 C CA  . THR   C 1 76  ? 4.023   24.922  21.236  1.00 9.79  ? 90  THR   C CA  1 
ATOM   2424 C C   . THR   C 1 76  ? 5.371   24.910  21.946  1.00 9.82  ? 90  THR   C C   1 
ATOM   2425 O O   . THR   C 1 76  ? 5.679   25.827  22.712  1.00 10.14 ? 90  THR   C O   1 
ATOM   2426 C CB  . THR   C 1 76  ? 4.100   25.919  20.064  1.00 10.03 ? 90  THR   C CB  1 
ATOM   2427 O OG1 . THR   C 1 76  ? 2.844   25.943  19.384  1.00 10.77 ? 90  THR   C OG1 1 
ATOM   2428 C CG2 . THR   C 1 76  ? 5.196   25.531  19.068  1.00 10.63 ? 90  THR   C CG2 1 
ATOM   2429 N N   . THR   C 1 77  ? 6.188   23.891  21.671  1.00 9.88  ? 91  THR   C N   1 
ATOM   2430 C CA  . THR   C 1 77  ? 7.600   23.900  22.035  1.00 9.22  ? 91  THR   C CA  1 
ATOM   2431 C C   . THR   C 1 77  ? 8.456   23.916  20.777  1.00 9.33  ? 91  THR   C C   1 
ATOM   2432 O O   . THR   C 1 77  ? 8.197   23.154  19.841  1.00 11.54 ? 91  THR   C O   1 
ATOM   2433 C CB  . THR   C 1 77  ? 8.000   22.673  22.879  1.00 10.00 ? 91  THR   C CB  1 
ATOM   2434 O OG1 . THR   C 1 77  ? 7.792   21.454  22.147  1.00 11.35 ? 91  THR   C OG1 1 
ATOM   2435 C CG2 . THR   C 1 77  ? 7.218   22.617  24.180  1.00 10.97 ? 91  THR   C CG2 1 
ATOM   2436 N N   . TRP   C 1 78  ? 9.482   24.765  20.766  1.00 9.33  ? 92  TRP   C N   1 
ATOM   2437 C CA  . TRP   C 1 78  ? 10.487  24.787  19.706  1.00 9.79  ? 92  TRP   C CA  1 
ATOM   2438 C C   . TRP   C 1 78  ? 11.793  24.252  20.277  1.00 9.63  ? 92  TRP   C C   1 
ATOM   2439 O O   . TRP   C 1 78  ? 12.219  24.685  21.357  1.00 10.52 ? 92  TRP   C O   1 
ATOM   2440 C CB  . TRP   C 1 78  ? 10.749  26.211  19.216  1.00 10.62 ? 92  TRP   C CB  1 
ATOM   2441 C CG  . TRP   C 1 78  ? 9.654   26.915  18.466  1.00 10.51 ? 92  TRP   C CG  1 
ATOM   2442 C CD1 . TRP   C 1 78  ? 9.596   27.113  17.112  1.00 10.01 ? 92  TRP   C CD1 1 
ATOM   2443 C CD2 . TRP   C 1 78  ? 8.502   27.582  19.015  1.00 10.09 ? 92  TRP   C CD2 1 
ATOM   2444 N NE1 . TRP   C 1 78  ? 8.483   27.847  16.786  1.00 11.04 ? 92  TRP   C NE1 1 
ATOM   2445 C CE2 . TRP   C 1 78  ? 7.791   28.147  17.932  1.00 10.56 ? 92  TRP   C CE2 1 
ATOM   2446 C CE3 . TRP   C 1 78  ? 8.001   27.754  20.314  1.00 10.52 ? 92  TRP   C CE3 1 
ATOM   2447 C CZ2 . TRP   C 1 78  ? 6.614   28.893  18.113  1.00 11.62 ? 92  TRP   C CZ2 1 
ATOM   2448 C CZ3 . TRP   C 1 78  ? 6.826   28.489  20.490  1.00 11.75 ? 92  TRP   C CZ3 1 
ATOM   2449 C CH2 . TRP   C 1 78  ? 6.147   29.043  19.393  1.00 12.05 ? 92  TRP   C CH2 1 
ATOM   2450 N N   . SER   C 1 79  ? 12.434  23.333  19.552  1.00 10.25 ? 93  SER   C N   1 
ATOM   2451 C CA  . SER   C 1 79  ? 13.709  22.739  19.938  1.00 11.10 ? 93  SER   C CA  1 
ATOM   2452 C C   . SER   C 1 79  ? 14.677  22.952  18.784  1.00 10.41 ? 93  SER   C C   1 
ATOM   2453 O O   . SER   C 1 79  ? 14.333  22.662  17.637  1.00 11.38 ? 93  SER   C O   1 
ATOM   2454 C CB  . SER   C 1 79  ? 13.511  21.236  20.157  1.00 11.56 ? 93  SER   C CB  1 
ATOM   2455 O OG  . SER   C 1 79  ? 14.717  20.588  20.519  1.00 12.54 ? 93  SER   C OG  1 
ATOM   2456 N N   . GLY   C 1 80  ? 15.867  23.472  19.051  1.00 11.12 ? 94  GLY   C N   1 
ATOM   2457 C CA  . GLY   C 1 80  ? 16.735  23.782  17.934  1.00 11.63 ? 94  GLY   C CA  1 
ATOM   2458 C C   . GLY   C 1 80  ? 18.120  24.209  18.353  1.00 10.96 ? 94  GLY   C C   1 
ATOM   2459 O O   . GLY   C 1 80  ? 18.579  23.912  19.456  1.00 12.08 ? 94  GLY   C O   1 
ATOM   2460 N N   . GLN   C 1 81  ? 18.803  24.899  17.442  1.00 12.19 ? 95  GLN   C N   1 
ATOM   2461 C CA  . GLN   C 1 81  ? 20.124  25.424  17.740  1.00 12.99 ? 95  GLN   C CA  1 
ATOM   2462 C C   . GLN   C 1 81  ? 20.332  26.774  17.076  1.00 12.28 ? 95  GLN   C C   1 
ATOM   2463 O O   . GLN   C 1 81  ? 19.830  27.028  15.973  1.00 13.11 ? 95  GLN   C O   1 
ATOM   2464 C CB  . GLN   C 1 81  ? 21.249  24.448  17.370  1.00 14.33 ? 95  GLN   C CB  1 
ATOM   2465 C CG  . GLN   C 1 81  ? 21.313  24.050  15.916  1.00 16.18 ? 95  GLN   C CG  1 
ATOM   2466 C CD  . GLN   C 1 81  ? 22.454  23.071  15.640  1.00 15.71 ? 95  GLN   C CD  1 
ATOM   2467 O OE1 . GLN   C 1 81  ? 23.569  23.233  16.146  1.00 15.96 ? 95  GLN   C OE1 1 
ATOM   2468 N NE2 . GLN   C 1 81  ? 22.175  22.043  14.844  1.00 17.03 ? 95  GLN   C NE2 1 
ATOM   2469 N N   . TYR   C 1 82  ? 21.065  27.634  17.777  1.00 13.26 ? 96  TYR   C N   1 
ATOM   2470 C CA  . TYR   C 1 82  ? 21.500  28.924  17.267  1.00 14.20 ? 96  TYR   C CA  1 
ATOM   2471 C C   . TYR   C 1 82  ? 22.825  28.742  16.546  1.00 15.55 ? 96  TYR   C C   1 
ATOM   2472 O O   . TYR   C 1 82  ? 23.733  28.085  17.063  1.00 16.21 ? 96  TYR   C O   1 
ATOM   2473 C CB  . TYR   C 1 82  ? 21.673  29.888  18.445  1.00 13.88 ? 96  TYR   C CB  1 
ATOM   2474 C CG  . TYR   C 1 82  ? 22.571  31.071  18.190  1.00 14.92 ? 96  TYR   C CG  1 
ATOM   2475 C CD1 . TYR   C 1 82  ? 22.074  32.240  17.626  1.00 16.29 ? 96  TYR   C CD1 1 
ATOM   2476 C CD2 . TYR   C 1 82  ? 23.917  31.033  18.539  1.00 16.91 ? 96  TYR   C CD2 1 
ATOM   2477 C CE1 . TYR   C 1 82  ? 22.902  33.328  17.394  1.00 17.82 ? 96  TYR   C CE1 1 
ATOM   2478 C CE2 . TYR   C 1 82  ? 24.745  32.115  18.314  1.00 18.96 ? 96  TYR   C CE2 1 
ATOM   2479 C CZ  . TYR   C 1 82  ? 24.233  33.260  17.744  1.00 19.19 ? 96  TYR   C CZ  1 
ATOM   2480 O OH  . TYR   C 1 82  ? 25.061  34.340  17.518  1.00 22.87 ? 96  TYR   C OH  1 
ATOM   2481 N N   . VAL   C 1 83  ? 22.919  29.308  15.347  1.00 17.28 ? 97  VAL   C N   1 
ATOM   2482 C CA  . VAL   C 1 83  ? 24.109  29.222  14.513  1.00 20.36 ? 97  VAL   C CA  1 
ATOM   2483 C C   . VAL   C 1 83  ? 24.565  30.653  14.274  1.00 21.00 ? 97  VAL   C C   1 
ATOM   2484 O O   . VAL   C 1 83  ? 23.901  31.412  13.558  1.00 22.01 ? 97  VAL   C O   1 
ATOM   2485 C CB  . VAL   C 1 83  ? 23.825  28.502  13.187  1.00 23.52 ? 97  VAL   C CB  1 
ATOM   2486 C CG1 . VAL   C 1 83  ? 25.088  28.435  12.332  1.00 24.77 ? 97  VAL   C CG1 1 
ATOM   2487 C CG2 . VAL   C 1 83  ? 23.275  27.104  13.443  1.00 25.71 ? 97  VAL   C CG2 1 
ATOM   2488 N N   . GLY   C 1 84  ? 25.681  31.034  14.888  1.00 22.72 ? 98  GLY   C N   1 
ATOM   2489 C CA  . GLY   C 1 84  ? 26.181  32.383  14.756  1.00 25.16 ? 98  GLY   C CA  1 
ATOM   2490 C C   . GLY   C 1 84  ? 26.881  32.606  13.430  1.00 28.71 ? 98  GLY   C C   1 
ATOM   2491 O O   . GLY   C 1 84  ? 27.008  31.716  12.589  1.00 29.60 ? 98  GLY   C O   1 
ATOM   2492 N N   . GLY   C 1 85  ? 27.347  33.833  13.243  1.00 32.29 ? 99  GLY   C N   1 
ATOM   2493 C CA  . GLY   C 1 85  ? 28.117  34.156  12.066  1.00 33.62 ? 99  GLY   C CA  1 
ATOM   2494 C C   . GLY   C 1 85  ? 27.549  35.366  11.369  1.00 35.29 ? 99  GLY   C C   1 
ATOM   2495 O O   . GLY   C 1 85  ? 26.830  36.172  11.973  1.00 35.96 ? 99  GLY   C O   1 
ATOM   2496 N N   . ALA   C 1 86  ? 27.887  35.483  10.081  1.00 35.96 ? 100 ALA   C N   1 
ATOM   2497 C CA  . ALA   C 1 86  ? 27.493  36.611  9.243   1.00 37.05 ? 100 ALA   C CA  1 
ATOM   2498 C C   . ALA   C 1 86  ? 26.003  36.906  9.351   1.00 37.36 ? 100 ALA   C C   1 
ATOM   2499 O O   . ALA   C 1 86  ? 25.613  37.976  9.831   1.00 38.58 ? 100 ALA   C O   1 
ATOM   2500 C CB  . ALA   C 1 86  ? 27.886  36.358  7.784   1.00 37.87 ? 100 ALA   C CB  1 
ATOM   2501 N N   . GLU   C 1 87  ? 25.165  35.977  8.904   1.00 35.44 ? 101 GLU   C N   1 
ATOM   2502 C CA  . GLU   C 1 87  ? 23.722  36.069  9.101   1.00 33.08 ? 101 GLU   C CA  1 
ATOM   2503 C C   . GLU   C 1 87  ? 23.348  35.009  10.128  1.00 29.90 ? 101 GLU   C C   1 
ATOM   2504 O O   . GLU   C 1 87  ? 23.260  33.819  9.809   1.00 29.59 ? 101 GLU   C O   1 
ATOM   2505 C CB  . GLU   C 1 87  ? 22.938  35.890  7.803   1.00 34.73 ? 101 GLU   C CB  1 
ATOM   2506 C CG  . GLU   C 1 87  ? 21.427  35.902  8.038   0.48 35.84 ? 101 GLU   C CG  1 
ATOM   2507 C CD  . GLU   C 1 87  ? 20.607  35.722  6.777   0.61 36.62 ? 101 GLU   C CD  1 
ATOM   2508 O OE1 . GLU   C 1 87  ? 21.158  35.256  5.758   0.42 36.90 ? 101 GLU   C OE1 1 
ATOM   2509 O OE2 . GLU   C 1 87  ? 19.401  36.051  6.812   0.79 36.99 ? 101 GLU   C OE2 1 
ATOM   2510 N N   . ALA   C 1 88  ? 23.145  35.449  11.365  1.00 27.15 ? 102 ALA   C N   1 
ATOM   2511 C CA  . ALA   C 1 88  ? 22.793  34.531  12.433  1.00 23.18 ? 102 ALA   C CA  1 
ATOM   2512 C C   . ALA   C 1 88  ? 21.423  33.916  12.161  1.00 20.86 ? 102 ALA   C C   1 
ATOM   2513 O O   . ALA   C 1 88  ? 20.563  34.521  11.517  1.00 21.93 ? 102 ALA   C O   1 
ATOM   2514 C CB  . ALA   C 1 88  ? 22.785  35.274  13.770  1.00 24.20 ? 102 ALA   C CB  1 
ATOM   2515 N N   . ARG   C 1 89  ? 21.225  32.698  12.667  1.00 18.62 ? 103 ARG   C N   1 
ATOM   2516 C CA  . ARG   C 1 89  ? 20.022  31.929  12.389  1.00 17.67 ? 103 ARG   C CA  1 
ATOM   2517 C C   . ARG   C 1 89  ? 19.741  31.034  13.587  1.00 15.60 ? 103 ARG   C C   1 
ATOM   2518 O O   . ARG   C 1 89  ? 20.667  30.569  14.257  1.00 16.48 ? 103 ARG   C O   1 
ATOM   2519 C CB  . ARG   C 1 89  ? 20.248  31.077  11.131  1.00 20.69 ? 103 ARG   C CB  1 
ATOM   2520 C CG  . ARG   C 1 89  ? 19.021  30.409  10.558  1.00 21.79 ? 103 ARG   C CG  1 
ATOM   2521 C CD  . ARG   C 1 89  ? 19.309  29.848  9.156   1.00 23.01 ? 103 ARG   C CD  1 
ATOM   2522 N NE  . ARG   C 1 89  ? 19.414  30.875  8.124   1.00 23.95 ? 103 ARG   C NE  1 
ATOM   2523 C CZ  . ARG   C 1 89  ? 18.387  31.351  7.434   1.00 24.80 ? 103 ARG   C CZ  1 
ATOM   2524 N NH1 . ARG   C 1 89  ? 17.150  30.941  7.664   1.00 24.50 ? 103 ARG   C NH1 1 
ATOM   2525 N NH2 . ARG   C 1 89  ? 18.605  32.264  6.490   1.00 26.68 ? 103 ARG   C NH2 1 
ATOM   2526 N N   . ILE   C 1 90  ? 18.458  30.814  13.868  1.00 14.13 ? 104 ILE   C N   1 
ATOM   2527 C CA  . ILE   C 1 90  ? 18.036  29.776  14.804  1.00 13.48 ? 104 ILE   C CA  1 
ATOM   2528 C C   . ILE   C 1 90  ? 17.170  28.791  14.029  1.00 13.19 ? 104 ILE   C C   1 
ATOM   2529 O O   . ILE   C 1 90  ? 16.116  29.166  13.504  1.00 14.68 ? 104 ILE   C O   1 
ATOM   2530 C CB  . ILE   C 1 90  ? 17.287  30.340  16.024  1.00 13.73 ? 104 ILE   C CB  1 
ATOM   2531 C CG1 . ILE   C 1 90  ? 18.154  31.350  16.786  1.00 15.26 ? 104 ILE   C CG1 1 
ATOM   2532 C CG2 . ILE   C 1 90  ? 16.888  29.205  16.939  1.00 15.34 ? 104 ILE   C CG2 1 
ATOM   2533 C CD1 . ILE   C 1 90  ? 17.425  32.070  17.921  1.00 16.72 ? 104 ILE   C CD1 1 
ATOM   2534 N N   . ASN   C 1 91  ? 17.625  27.545  13.937  1.00 13.07 ? 105 ASN   C N   1 
ATOM   2535 C CA  . ASN   C 1 91  ? 16.913  26.499  13.210  1.00 12.31 ? 105 ASN   C CA  1 
ATOM   2536 C C   . ASN   C 1 91  ? 16.217  25.589  14.206  1.00 11.90 ? 105 ASN   C C   1 
ATOM   2537 O O   . ASN   C 1 91  ? 16.863  25.061  15.118  1.00 12.85 ? 105 ASN   C O   1 
ATOM   2538 C CB  . ASN   C 1 91  ? 17.893  25.672  12.384  1.00 15.19 ? 105 ASN   C CB  1 
ATOM   2539 C CG  . ASN   C 1 91  ? 18.536  26.484  11.300  1.00 18.20 ? 105 ASN   C CG  1 
ATOM   2540 O OD1 . ASN   C 1 91  ? 17.863  27.253  10.608  1.00 18.66 ? 105 ASN   C OD1 1 
ATOM   2541 N ND2 . ASN   C 1 91  ? 19.850  26.353  11.159  1.00 21.31 ? 105 ASN   C ND2 1 
ATOM   2542 N N   . THR   C 1 92  ? 14.911  25.390  14.025  1.00 11.45 ? 106 THR   C N   1 
ATOM   2543 C CA  . THR   C 1 92  ? 14.120  24.651  15.006  1.00 11.79 ? 106 THR   C CA  1 
ATOM   2544 C C   . THR   C 1 92  ? 13.176  23.653  14.348  1.00 11.21 ? 106 THR   C C   1 
ATOM   2545 O O   . THR   C 1 92  ? 12.810  23.762  13.169  1.00 11.31 ? 106 THR   C O   1 
ATOM   2546 C CB  . THR   C 1 92  ? 13.236  25.572  15.876  1.00 11.24 ? 106 THR   C CB  1 
ATOM   2547 O OG1 . THR   C 1 92  ? 12.139  26.074  15.088  1.00 12.11 ? 106 THR   C OG1 1 
ATOM   2548 C CG2 . THR   C 1 92  ? 14.032  26.740  16.466  1.00 12.23 ? 106 THR   C CG2 1 
ATOM   2549 N N   . GLN   C 1 93  ? 12.790  22.674  15.160  1.00 11.02 ? 107 GLN   C N   1 
ATOM   2550 C CA  A GLN   C 1 93  ? 11.602  21.879  14.921  0.76 10.74 ? 107 GLN   C CA  1 
ATOM   2551 C CA  B GLN   C 1 93  ? 11.634  21.807  14.963  0.24 10.00 ? 107 GLN   C CA  1 
ATOM   2552 C C   . GLN   C 1 93  ? 10.661  22.093  16.102  1.00 9.56  ? 107 GLN   C C   1 
ATOM   2553 O O   . GLN   C 1 93  ? 11.091  22.440  17.209  1.00 10.80 ? 107 GLN   C O   1 
ATOM   2554 C CB  A GLN   C 1 93  ? 11.968  20.415  14.664  0.76 13.96 ? 107 GLN   C CB  1 
ATOM   2555 C CB  B GLN   C 1 93  ? 12.047  20.331  15.079  0.24 9.98  ? 107 GLN   C CB  1 
ATOM   2556 C CG  A GLN   C 1 93  ? 12.808  20.297  13.381  0.76 14.90 ? 107 GLN   C CG  1 
ATOM   2557 C CG  B GLN   C 1 93  ? 13.147  19.888  14.130  0.24 10.14 ? 107 GLN   C CG  1 
ATOM   2558 C CD  A GLN   C 1 93  ? 13.187  18.880  13.012  0.76 15.01 ? 107 GLN   C CD  1 
ATOM   2559 C CD  B GLN   C 1 93  ? 12.610  19.397  12.806  0.24 9.78  ? 107 GLN   C CD  1 
ATOM   2560 O OE1 A GLN   C 1 93  ? 12.452  18.191  12.313  0.76 16.37 ? 107 GLN   C OE1 1 
ATOM   2561 O OE1 B GLN   C 1 93  ? 11.399  19.253  12.629  0.24 10.03 ? 107 GLN   C OE1 1 
ATOM   2562 N NE2 A GLN   C 1 93  ? 14.358  18.445  13.458  0.76 14.44 ? 107 GLN   C NE2 1 
ATOM   2563 N NE2 B GLN   C 1 93  ? 13.508  19.134  11.865  0.24 10.37 ? 107 GLN   C NE2 1 
ATOM   2564 N N   . TRP   C 1 94  ? 9.360   21.950  15.853  1.00 9.06  ? 108 TRP   C N   1 
ATOM   2565 C CA  . TRP   C 1 94  ? 8.384   22.280  16.887  1.00 9.76  ? 108 TRP   C CA  1 
ATOM   2566 C C   . TRP   C 1 94  ? 7.283   21.233  16.982  1.00 9.15  ? 108 TRP   C C   1 
ATOM   2567 O O   . TRP   C 1 94  ? 6.985   20.511  16.019  1.00 9.57  ? 108 TRP   C O   1 
ATOM   2568 C CB  . TRP   C 1 94  ? 7.799   23.695  16.701  1.00 9.98  ? 108 TRP   C CB  1 
ATOM   2569 C CG  . TRP   C 1 94  ? 7.192   23.994  15.349  1.00 10.18 ? 108 TRP   C CG  1 
ATOM   2570 C CD1 . TRP   C 1 94  ? 7.767   24.732  14.347  1.00 11.53 ? 108 TRP   C CD1 1 
ATOM   2571 C CD2 . TRP   C 1 94  ? 5.883   23.618  14.870  1.00 10.38 ? 108 TRP   C CD2 1 
ATOM   2572 N NE1 . TRP   C 1 94  ? 6.913   24.810  13.270  1.00 11.81 ? 108 TRP   C NE1 1 
ATOM   2573 C CE2 . TRP   C 1 94  ? 5.753   24.140  13.560  1.00 11.16 ? 108 TRP   C CE2 1 
ATOM   2574 C CE3 . TRP   C 1 94  ? 4.827   22.866  15.404  1.00 9.58  ? 108 TRP   C CE3 1 
ATOM   2575 C CZ2 . TRP   C 1 94  ? 4.592   23.954  12.787  1.00 11.76 ? 108 TRP   C CZ2 1 
ATOM   2576 C CZ3 . TRP   C 1 94  ? 3.679   22.688  14.645  1.00 9.72  ? 108 TRP   C CZ3 1 
ATOM   2577 C CH2 . TRP   C 1 94  ? 3.569   23.225  13.343  1.00 10.67 ? 108 TRP   C CH2 1 
ATOM   2578 N N   . LEU   C 1 95  ? 6.682   21.180  18.178  1.00 9.38  ? 109 LEU   C N   1 
ATOM   2579 C CA  . LEU   C 1 95  ? 5.523   20.351  18.493  1.00 9.63  ? 109 LEU   C CA  1 
ATOM   2580 C C   . LEU   C 1 95  ? 4.440   21.227  19.105  1.00 10.55 ? 109 LEU   C C   1 
ATOM   2581 O O   . LEU   C 1 95  ? 4.702   21.964  20.060  1.00 12.18 ? 109 LEU   C O   1 
ATOM   2582 C CB  . LEU   C 1 95  ? 5.885   19.269  19.518  1.00 10.04 ? 109 LEU   C CB  1 
ATOM   2583 C CG  . LEU   C 1 95  ? 6.893   18.208  19.081  1.00 11.04 ? 109 LEU   C CG  1 
ATOM   2584 C CD1 . LEU   C 1 95  ? 7.287   17.378  20.289  1.00 12.27 ? 109 LEU   C CD1 1 
ATOM   2585 C CD2 . LEU   C 1 95  ? 6.300   17.351  17.971  1.00 13.37 ? 109 LEU   C CD2 1 
ATOM   2586 N N   . LEU   C 1 96  ? 3.220   21.120  18.592  1.00 9.61  ? 110 LEU   C N   1 
ATOM   2587 C CA  . LEU   C 1 96  ? 2.096   21.940  19.036  1.00 9.93  ? 110 LEU   C CA  1 
ATOM   2588 C C   . LEU   C 1 96  ? 0.995   21.003  19.530  1.00 9.63  ? 110 LEU   C C   1 
ATOM   2589 O O   . LEU   C 1 96  ? 0.326   20.349  18.721  1.00 10.15 ? 110 LEU   C O   1 
ATOM   2590 C CB  . LEU   C 1 96  ? 1.611   22.838  17.887  1.00 10.97 ? 110 LEU   C CB  1 
ATOM   2591 C CG  . LEU   C 1 96  ? 0.235   23.514  17.932  1.00 11.49 ? 110 LEU   C CG  1 
ATOM   2592 C CD1 . LEU   C 1 96  ? -0.044  24.212  19.278  1.00 12.36 ? 110 LEU   C CD1 1 
ATOM   2593 C CD2 . LEU   C 1 96  ? 0.078   24.489  16.759  1.00 13.73 ? 110 LEU   C CD2 1 
ATOM   2594 N N   . THR   C 1 97  ? 0.817   20.917  20.851  1.00 9.74  ? 111 THR   C N   1 
ATOM   2595 C CA  . THR   C 1 97  ? -0.159  20.008  21.449  1.00 9.74  ? 111 THR   C CA  1 
ATOM   2596 C C   . THR   C 1 97  ? -1.377  20.792  21.929  1.00 10.04 ? 111 THR   C C   1 
ATOM   2597 O O   . THR   C 1 97  ? -1.237  21.781  22.660  1.00 11.17 ? 111 THR   C O   1 
ATOM   2598 C CB  . THR   C 1 97  ? 0.447   19.255  22.641  1.00 11.08 ? 111 THR   C CB  1 
ATOM   2599 O OG1 . THR   C 1 97  ? 1.618   18.541  22.232  1.00 11.24 ? 111 THR   C OG1 1 
ATOM   2600 C CG2 . THR   C 1 97  ? -0.551  18.244  23.197  1.00 12.10 ? 111 THR   C CG2 1 
ATOM   2601 N N   . SER   C 1 98  ? -2.565  20.334  21.550  1.00 11.02 ? 112 SER   C N   1 
ATOM   2602 C CA  . SER   C 1 98  ? -3.820  20.874  22.064  1.00 11.97 ? 112 SER   C CA  1 
ATOM   2603 C C   . SER   C 1 98  ? -4.360  19.982  23.181  1.00 12.27 ? 112 SER   C C   1 
ATOM   2604 O O   . SER   C 1 98  ? -4.191  18.760  23.158  1.00 12.95 ? 112 SER   C O   1 
ATOM   2605 C CB  . SER   C 1 98  ? -4.867  20.908  20.951  1.00 12.63 ? 112 SER   C CB  1 
ATOM   2606 O OG  . SER   C 1 98  ? -4.483  21.790  19.923  1.00 14.44 ? 112 SER   C OG  1 
ATOM   2607 N N   . GLY   C 1 99  ? -5.019  20.600  24.167  1.00 11.95 ? 113 GLY   C N   1 
ATOM   2608 C CA  . GLY   C 1 99  ? -5.775  19.817  25.132  1.00 13.02 ? 113 GLY   C CA  1 
ATOM   2609 C C   . GLY   C 1 99  ? -6.921  19.091  24.445  1.00 13.61 ? 113 GLY   C C   1 
ATOM   2610 O O   . GLY   C 1 99  ? -7.681  19.719  23.695  1.00 15.90 ? 113 GLY   C O   1 
ATOM   2611 N N   . THR   C 1 100 ? -7.057  17.778  24.670  1.00 13.08 ? 114 THR   C N   1 
ATOM   2612 C CA  . THR   C 1 100 ? -8.105  16.983  24.031  1.00 13.48 ? 114 THR   C CA  1 
ATOM   2613 C C   . THR   C 1 100 ? -8.675  15.994  25.041  1.00 13.29 ? 114 THR   C C   1 
ATOM   2614 O O   . THR   C 1 100 ? -8.088  15.753  26.100  1.00 13.42 ? 114 THR   C O   1 
ATOM   2615 C CB  . THR   C 1 100 ? -7.570  16.174  22.830  1.00 13.62 ? 114 THR   C CB  1 
ATOM   2616 O OG1 . THR   C 1 100 ? -6.688  15.144  23.295  1.00 13.66 ? 114 THR   C OG1 1 
ATOM   2617 C CG2 . THR   C 1 100 ? -6.835  17.059  21.808  1.00 15.06 ? 114 THR   C CG2 1 
ATOM   2618 N N   . THR   C 1 101 ? -9.828  15.409  24.708  1.00 15.30 ? 115 THR   C N   1 
ATOM   2619 C CA  . THR   C 1 101 ? -10.251 14.207  25.410  1.00 16.27 ? 115 THR   C CA  1 
ATOM   2620 C C   . THR   C 1 101 ? -9.343  13.043  25.015  1.00 16.19 ? 115 THR   C C   1 
ATOM   2621 O O   . THR   C 1 101 ? -8.585  13.109  24.038  1.00 15.92 ? 115 THR   C O   1 
ATOM   2622 C CB  . THR   C 1 101 ? -11.681 13.832  25.032  1.00 19.06 ? 115 THR   C CB  1 
ATOM   2623 O OG1 . THR   C 1 101 ? -11.717 13.541  23.630  1.00 20.60 ? 115 THR   C OG1 1 
ATOM   2624 C CG2 . THR   C 1 101 ? -12.647 14.964  25.370  1.00 20.90 ? 115 THR   C CG2 1 
ATOM   2625 N N   . GLU   C 1 102 ? -9.422  11.960  25.792  1.00 17.90 ? 116 GLU   C N   1 
ATOM   2626 C CA  . GLU   C 1 102 ? -8.619  10.783  25.481  1.00 19.31 ? 116 GLU   C CA  1 
ATOM   2627 C C   . GLU   C 1 102 ? -8.950  10.241  24.097  1.00 18.74 ? 116 GLU   C C   1 
ATOM   2628 O O   . GLU   C 1 102 ? -8.048  9.883   23.333  1.00 19.21 ? 116 GLU   C O   1 
ATOM   2629 C CB  . GLU   C 1 102 ? -8.805  9.700   26.544  1.00 21.78 ? 116 GLU   C CB  1 
ATOM   2630 C CG  . GLU   C 1 102 ? -7.904  8.493   26.327  1.00 24.28 ? 116 GLU   C CG  1 
ATOM   2631 C CD  . GLU   C 1 102 ? -6.434  8.875   26.259  0.49 25.16 ? 116 GLU   C CD  1 
ATOM   2632 O OE1 . GLU   C 1 102 ? -5.988  9.675   27.107  0.42 25.91 ? 116 GLU   C OE1 1 
ATOM   2633 O OE2 . GLU   C 1 102 ? -5.727  8.387   25.352  0.44 25.44 ? 116 GLU   C OE2 1 
ATOM   2634 N N   . ALA   C 1 103 ? -10.236 10.197  23.743  1.00 19.10 ? 117 ALA   C N   1 
ATOM   2635 C CA  . ALA   C 1 103 ? -10.618 9.643   22.448  1.00 20.02 ? 117 ALA   C CA  1 
ATOM   2636 C C   . ALA   C 1 103 ? -10.064 10.448  21.278  1.00 18.68 ? 117 ALA   C C   1 
ATOM   2637 O O   . ALA   C 1 103 ? -9.904  9.894   20.184  1.00 19.64 ? 117 ALA   C O   1 
ATOM   2638 C CB  . ALA   C 1 103 ? -12.139 9.520   22.349  1.00 21.45 ? 117 ALA   C CB  1 
ATOM   2639 N N   . ASN   C 1 104 ? -9.754  11.731  21.484  1.00 17.24 ? 118 ASN   C N   1 
ATOM   2640 C CA  . ASN   C 1 104 ? -9.200  12.588  20.440  1.00 17.00 ? 118 ASN   C CA  1 
ATOM   2641 C C   . ASN   C 1 104 ? -7.699  12.820  20.578  1.00 15.15 ? 118 ASN   C C   1 
ATOM   2642 O O   . ASN   C 1 104 ? -7.129  13.592  19.796  1.00 15.50 ? 118 ASN   C O   1 
ATOM   2643 C CB  . ASN   C 1 104 ? -9.921  13.936  20.421  1.00 19.05 ? 118 ASN   C CB  1 
ATOM   2644 C CG  . ASN   C 1 104 ? -11.338 13.824  19.924  1.00 21.86 ? 118 ASN   C CG  1 
ATOM   2645 O OD1 . ASN   C 1 104 ? -11.648 12.985  19.075  1.00 23.47 ? 118 ASN   C OD1 1 
ATOM   2646 N ND2 . ASN   C 1 104 ? -12.210 14.675  20.442  1.00 24.46 ? 118 ASN   C ND2 1 
ATOM   2647 N N   . ALA   C 1 105 ? -7.046  12.171  21.542  1.00 13.95 ? 119 ALA   C N   1 
ATOM   2648 C CA  . ALA   C 1 105 ? -5.642  12.462  21.808  1.00 13.46 ? 119 ALA   C CA  1 
ATOM   2649 C C   . ALA   C 1 105 ? -4.742  12.057  20.648  1.00 13.47 ? 119 ALA   C C   1 
ATOM   2650 O O   . ALA   C 1 105 ? -3.658  12.630  20.480  1.00 13.38 ? 119 ALA   C O   1 
ATOM   2651 C CB  . ALA   C 1 105 ? -5.206  11.786  23.106  1.00 14.69 ? 119 ALA   C CB  1 
ATOM   2652 N N   . TRP   C 1 106 ? -5.168  11.082  19.836  1.00 14.10 ? 120 TRP   C N   1 
ATOM   2653 C CA  . TRP   C 1 106 ? -4.334  10.647  18.718  1.00 15.12 ? 120 TRP   C CA  1 
ATOM   2654 C C   . TRP   C 1 106 ? -4.035  11.792  17.758  1.00 13.90 ? 120 TRP   C C   1 
ATOM   2655 O O   . TRP   C 1 106 ? -2.989  11.785  17.100  1.00 15.55 ? 120 TRP   C O   1 
ATOM   2656 C CB  . TRP   C 1 106 ? -4.997  9.480   17.978  1.00 17.46 ? 120 TRP   C CB  1 
ATOM   2657 C CG  . TRP   C 1 106 ? -6.255  9.859   17.252  1.00 18.39 ? 120 TRP   C CG  1 
ATOM   2658 C CD1 . TRP   C 1 106 ? -7.520  9.877   17.760  1.00 18.99 ? 120 TRP   C CD1 1 
ATOM   2659 C CD2 . TRP   C 1 106 ? -6.371  10.263  15.879  1.00 18.98 ? 120 TRP   C CD2 1 
ATOM   2660 N NE1 . TRP   C 1 106 ? -8.415  10.269  16.795  1.00 19.38 ? 120 TRP   C NE1 1 
ATOM   2661 C CE2 . TRP   C 1 106 ? -7.733  10.521  15.633  1.00 19.27 ? 120 TRP   C CE2 1 
ATOM   2662 C CE3 . TRP   C 1 106 ? -5.451  10.455  14.844  1.00 19.93 ? 120 TRP   C CE3 1 
ATOM   2663 C CZ2 . TRP   C 1 106 ? -8.202  10.938  14.386  1.00 21.41 ? 120 TRP   C CZ2 1 
ATOM   2664 C CZ3 . TRP   C 1 106 ? -5.917  10.873  13.607  1.00 20.72 ? 120 TRP   C CZ3 1 
ATOM   2665 C CH2 . TRP   C 1 106 ? -7.282  11.106  13.391  1.00 20.78 ? 120 TRP   C CH2 1 
ATOM   2666 N N   . LYS   C 1 107 ? -4.936  12.772  17.654  1.00 13.82 ? 121 LYS   C N   1 
ATOM   2667 C CA  . LYS   C 1 107 ? -4.764  13.910  16.757  1.00 13.41 ? 121 LYS   C CA  1 
ATOM   2668 C C   . LYS   C 1 107 ? -4.445  15.201  17.513  1.00 12.42 ? 121 LYS   C C   1 
ATOM   2669 O O   . LYS   C 1 107 ? -4.720  16.302  17.025  1.00 13.57 ? 121 LYS   C O   1 
ATOM   2670 C CB  . LYS   C 1 107 ? -5.972  14.068  15.827  1.00 15.92 ? 121 LYS   C CB  1 
ATOM   2671 C CG  . LYS   C 1 107 ? -7.325  14.130  16.541  1.00 17.36 ? 121 LYS   C CG  1 
ATOM   2672 C CD  . LYS   C 1 107 ? -8.466  14.375  15.558  1.00 19.63 ? 121 LYS   C CD  1 
ATOM   2673 C CE  . LYS   C 1 107 ? -9.799  14.432  16.283  1.00 21.95 ? 121 LYS   C CE  1 
ATOM   2674 N NZ  . LYS   C 1 107 ? -10.937 14.755  15.378  1.00 24.68 ? 121 LYS   C NZ  1 
ATOM   2675 N N   . SER   C 1 108 ? -3.840  15.085  18.700  1.00 11.58 ? 122 SER   C N   1 
ATOM   2676 C CA  . SER   C 1 108 ? -3.573  16.252  19.535  1.00 11.54 ? 122 SER   C CA  1 
ATOM   2677 C C   . SER   C 1 108 ? -2.337  17.052  19.144  1.00 10.45 ? 122 SER   C C   1 
ATOM   2678 O O   . SER   C 1 108 ? -2.213  18.187  19.616  1.00 10.49 ? 122 SER   C O   1 
ATOM   2679 C CB  . SER   C 1 108 ? -3.381  15.827  20.992  1.00 12.68 ? 122 SER   C CB  1 
ATOM   2680 O OG  . SER   C 1 108 ? -2.217  15.021  21.126  1.00 13.96 ? 122 SER   C OG  1 
ATOM   2681 N N   . THR   C 1 109 ? -1.409  16.508  18.348  1.00 9.87  ? 123 THR   C N   1 
ATOM   2682 C CA  . THR   C 1 109 ? -0.080  17.112  18.228  1.00 9.69  ? 123 THR   C CA  1 
ATOM   2683 C C   . THR   C 1 109 ? 0.317   17.332  16.771  1.00 9.49  ? 123 THR   C C   1 
ATOM   2684 O O   . THR   C 1 109 ? 0.439   16.369  16.000  1.00 10.45 ? 123 THR   C O   1 
ATOM   2685 C CB  . THR   C 1 109 ? 0.983   16.252  18.915  1.00 10.25 ? 123 THR   C CB  1 
ATOM   2686 O OG1 . THR   C 1 109 ? 0.550   15.895  20.237  1.00 11.58 ? 123 THR   C OG1 1 
ATOM   2687 C CG2 . THR   C 1 109 ? 2.295   17.014  19.013  1.00 10.63 ? 123 THR   C CG2 1 
ATOM   2688 N N   . LEU   C 1 110 ? 0.577   18.589  16.408  1.00 9.66  ? 124 LEU   C N   1 
ATOM   2689 C CA  . LEU   C 1 110 ? 1.123   18.961  15.107  1.00 9.55  ? 124 LEU   C CA  1 
ATOM   2690 C C   . LEU   C 1 110 ? 2.641   19.097  15.208  1.00 9.22  ? 124 LEU   C C   1 
ATOM   2691 O O   . LEU   C 1 110 ? 3.177   19.418  16.274  1.00 10.11 ? 124 LEU   C O   1 
ATOM   2692 C CB  . LEU   C 1 110 ? 0.521   20.294  14.651  1.00 11.06 ? 124 LEU   C CB  1 
ATOM   2693 C CG  . LEU   C 1 110 ? -0.974  20.309  14.309  1.00 11.42 ? 124 LEU   C CG  1 
ATOM   2694 C CD1 . LEU   C 1 110 ? -1.501  21.729  14.275  1.00 14.00 ? 124 LEU   C CD1 1 
ATOM   2695 C CD2 . LEU   C 1 110 ? -1.206  19.600  12.973  1.00 11.83 ? 124 LEU   C CD2 1 
ATOM   2696 N N   . VAL   C 1 111 ? 3.337   18.859  14.087  1.00 9.87  ? 125 VAL   C N   1 
ATOM   2697 C CA  . VAL   C 1 111 ? 4.793   18.977  14.024  1.00 10.11 ? 125 VAL   C CA  1 
ATOM   2698 C C   . VAL   C 1 111 ? 5.191   19.810  12.809  1.00 9.30  ? 125 VAL   C C   1 
ATOM   2699 O O   . VAL   C 1 111 ? 4.556   19.743  11.745  1.00 10.34 ? 125 VAL   C O   1 
ATOM   2700 C CB  . VAL   C 1 111 ? 5.485   17.583  14.005  1.00 10.73 ? 125 VAL   C CB  1 
ATOM   2701 C CG1 . VAL   C 1 111 ? 5.045   16.762  12.786  1.00 11.65 ? 125 VAL   C CG1 1 
ATOM   2702 C CG2 . VAL   C 1 111 ? 7.004   17.706  14.097  1.00 10.87 ? 125 VAL   C CG2 1 
ATOM   2703 N N   . GLY   C 1 112 ? 6.271   20.579  12.945  1.00 9.40  ? 126 GLY   C N   1 
ATOM   2704 C CA  . GLY   C 1 112 ? 6.796   21.343  11.833  1.00 9.65  ? 126 GLY   C CA  1 
ATOM   2705 C C   . GLY   C 1 112 ? 8.190   21.847  12.128  1.00 9.74  ? 126 GLY   C C   1 
ATOM   2706 O O   . GLY   C 1 112 ? 8.835   21.420  13.089  1.00 10.42 ? 126 GLY   C O   1 
ATOM   2707 N N   . HIS   C 1 113 ? 8.661   22.768  11.286  1.00 11.11 ? 127 HIS   C N   1 
ATOM   2708 C CA  . HIS   C 1 113 ? 9.996   23.334  11.441  1.00 11.73 ? 127 HIS   C CA  1 
ATOM   2709 C C   . HIS   C 1 113 ? 9.967   24.820  11.121  1.00 11.77 ? 127 HIS   C C   1 
ATOM   2710 O O   . HIS   C 1 113 ? 9.376   25.222  10.115  1.00 14.12 ? 127 HIS   C O   1 
ATOM   2711 C CB  . HIS   C 1 113 ? 11.028  22.601  10.563  1.00 12.79 ? 127 HIS   C CB  1 
ATOM   2712 C CG  . HIS   C 1 113 ? 10.573  22.380  9.153   1.00 14.77 ? 127 HIS   C CG  1 
ATOM   2713 N ND1 . HIS   C 1 113 ? 10.972  23.181  8.106   1.00 17.77 ? 127 HIS   C ND1 1 
ATOM   2714 C CD2 . HIS   C 1 113 ? 9.735   21.457  8.622   1.00 14.56 ? 127 HIS   C CD2 1 
ATOM   2715 C CE1 . HIS   C 1 113 ? 10.411  22.755  6.989   1.00 18.61 ? 127 HIS   C CE1 1 
ATOM   2716 N NE2 . HIS   C 1 113 ? 9.650   21.714  7.275   1.00 17.79 ? 127 HIS   C NE2 1 
ATOM   2717 N N   . ASP   C 1 114 ? 10.606  25.629  11.972  1.00 11.71 ? 128 ASP   C N   1 
ATOM   2718 C CA  . ASP   C 1 114 ? 10.703  27.073  11.783  1.00 11.94 ? 128 ASP   C CA  1 
ATOM   2719 C C   . ASP   C 1 114 ? 12.167  27.484  11.767  1.00 12.67 ? 128 ASP   C C   1 
ATOM   2720 O O   . ASP   C 1 114 ? 12.957  27.012  12.591  1.00 12.48 ? 128 ASP   C O   1 
ATOM   2721 C CB  . ASP   C 1 114 ? 10.069  27.839  12.959  1.00 12.34 ? 128 ASP   C CB  1 
ATOM   2722 C CG  . ASP   C 1 114 ? 8.552   27.875  12.913  1.00 12.71 ? 128 ASP   C CG  1 
ATOM   2723 O OD1 . ASP   C 1 114 ? 7.946   27.342  11.956  1.00 14.29 ? 128 ASP   C OD1 1 
ATOM   2724 O OD2 . ASP   C 1 114 ? 7.966   28.442  13.868  1.00 12.81 ? 128 ASP   C OD2 1 
ATOM   2725 N N   . THR   C 1 115 ? 12.530  28.385  10.854  1.00 12.59 ? 129 THR   C N   1 
ATOM   2726 C CA  A THR   C 1 115 ? 13.851  28.991  10.858  0.87 13.77 ? 129 THR   C CA  1 
ATOM   2727 C CA  B THR   C 1 115 ? 13.853  28.999  10.818  0.13 13.59 ? 129 THR   C CA  1 
ATOM   2728 C C   . THR   C 1 115 ? 13.716  30.486  11.115  1.00 13.74 ? 129 THR   C C   1 
ATOM   2729 O O   . THR   C 1 115 ? 12.855  31.156  10.532  1.00 14.54 ? 129 THR   C O   1 
ATOM   2730 C CB  A THR   C 1 115 ? 14.638  28.680  9.576   0.87 16.48 ? 129 THR   C CB  1 
ATOM   2731 C CB  B THR   C 1 115 ? 14.496  28.809  9.444   0.13 14.17 ? 129 THR   C CB  1 
ATOM   2732 O OG1 A THR   C 1 115 ? 15.975  29.188  9.694   0.87 16.81 ? 129 THR   C OG1 1 
ATOM   2733 O OG1 B THR   C 1 115 ? 13.557  29.164  8.421   0.13 14.80 ? 129 THR   C OG1 1 
ATOM   2734 C CG2 A THR   C 1 115 ? 13.968  29.269  8.338   0.87 18.33 ? 129 THR   C CG2 1 
ATOM   2735 C CG2 B THR   C 1 115 ? 14.918  27.370  9.257   0.13 14.09 ? 129 THR   C CG2 1 
ATOM   2736 N N   . PHE   C 1 116 ? 14.555  30.991  12.014  1.00 13.35 ? 130 PHE   C N   1 
ATOM   2737 C CA  . PHE   C 1 116 ? 14.488  32.368  12.484  1.00 13.33 ? 130 PHE   C CA  1 
ATOM   2738 C C   . PHE   C 1 116 ? 15.728  33.137  12.049  1.00 14.28 ? 130 PHE   C C   1 
ATOM   2739 O O   . PHE   C 1 116 ? 16.851  32.627  12.136  1.00 13.97 ? 130 PHE   C O   1 
ATOM   2740 C CB  . PHE   C 1 116 ? 14.415  32.411  14.020  1.00 13.54 ? 130 PHE   C CB  1 
ATOM   2741 C CG  . PHE   C 1 116 ? 13.141  31.849  14.590  1.00 12.85 ? 130 PHE   C CG  1 
ATOM   2742 C CD1 . PHE   C 1 116 ? 13.009  30.484  14.818  1.00 12.86 ? 130 PHE   C CD1 1 
ATOM   2743 C CD2 . PHE   C 1 116 ? 12.073  32.678  14.882  1.00 12.66 ? 130 PHE   C CD2 1 
ATOM   2744 C CE1 . PHE   C 1 116 ? 11.837  29.954  15.332  1.00 12.55 ? 130 PHE   C CE1 1 
ATOM   2745 C CE2 . PHE   C 1 116 ? 10.897  32.161  15.407  1.00 13.79 ? 130 PHE   C CE2 1 
ATOM   2746 C CZ  . PHE   C 1 116 ? 10.778  30.797  15.629  1.00 12.75 ? 130 PHE   C CZ  1 
ATOM   2747 N N   . THR   C 1 117 ? 15.525  34.371  11.587  1.00 15.15 ? 131 THR   C N   1 
ATOM   2748 C CA  . THR   C 1 117 ? 16.627  35.273  11.273  1.00 15.86 ? 131 THR   C CA  1 
ATOM   2749 C C   . THR   C 1 117 ? 16.340  36.651  11.862  1.00 16.34 ? 131 THR   C C   1 
ATOM   2750 O O   . THR   C 1 117 ? 15.253  36.926  12.373  1.00 15.55 ? 131 THR   C O   1 
ATOM   2751 C CB  . THR   C 1 117 ? 16.873  35.411  9.760   1.00 18.51 ? 131 THR   C CB  1 
ATOM   2752 O OG1 . THR   C 1 117 ? 15.813  36.178  9.186   1.00 21.15 ? 131 THR   C OG1 1 
ATOM   2753 C CG2 . THR   C 1 117 ? 16.949  34.057  9.075   1.00 19.28 ? 131 THR   C CG2 1 
ATOM   2754 N N   . LYS   C 1 118 ? 17.329  37.537  11.763  1.00 17.52 ? 132 LYS   C N   1 
ATOM   2755 C CA  . LYS   C 1 118 ? 17.196  38.895  12.275  1.00 19.30 ? 132 LYS   C CA  1 
ATOM   2756 C C   . LYS   C 1 118 ? 16.444  39.821  11.327  1.00 18.65 ? 132 LYS   C C   1 
ATOM   2757 O O   . LYS   C 1 118 ? 16.226  40.985  11.677  1.00 20.46 ? 132 LYS   C O   1 
ATOM   2758 C CB  . LYS   C 1 118 ? 18.580  39.486  12.564  1.00 22.09 ? 132 LYS   C CB  1 
ATOM   2759 C CG  . LYS   C 1 118 ? 19.432  38.680  13.541  1.00 25.26 ? 132 LYS   C CG  1 
ATOM   2760 C CD  . LYS   C 1 118 ? 19.038  38.917  14.996  1.00 29.52 ? 132 LYS   C CD  1 
ATOM   2761 C CE  . LYS   C 1 118 ? 20.143  38.422  15.929  1.00 33.00 ? 132 LYS   C CE  1 
ATOM   2762 N NZ  . LYS   C 1 118 ? 19.930  38.768  17.362  1.00 35.54 ? 132 LYS   C NZ  1 
ATOM   2763 N N   . VAL   C 1 119 ? 16.048  39.343  10.149  1.00 18.98 ? 133 VAL   C N   1 
ATOM   2764 C CA  . VAL   C 1 119 ? 15.390  40.156  9.131   1.00 21.31 ? 133 VAL   C CA  1 
ATOM   2765 C C   . VAL   C 1 119 ? 14.006  39.583  8.850   1.00 22.69 ? 133 VAL   C C   1 
ATOM   2766 O O   . VAL   C 1 119 ? 13.820  38.362  8.843   1.00 24.03 ? 133 VAL   C O   1 
ATOM   2767 C CB  . VAL   C 1 119 ? 16.247  40.195  7.847   1.00 24.89 ? 133 VAL   C CB  1 
ATOM   2768 C CG1 . VAL   C 1 119 ? 15.475  40.793  6.695   1.00 27.29 ? 133 VAL   C CG1 1 
ATOM   2769 C CG2 . VAL   C 1 119 ? 17.523  40.990  8.092   1.00 25.78 ? 133 VAL   C CG2 1 
ATOM   2770 N N   . LYS   C 1 120 ? 13.034  40.466  8.621   1.00 24.29 ? 134 LYS   C N   1 
ATOM   2771 C CA  . LYS   C 1 120 ? 11.688  40.025  8.273   1.00 26.40 ? 134 LYS   C CA  1 
ATOM   2772 C C   . LYS   C 1 120 ? 11.689  39.358  6.898   1.00 28.54 ? 134 LYS   C C   1 
ATOM   2773 O O   . LYS   C 1 120 ? 12.395  39.805  5.988   1.00 29.11 ? 134 LYS   C O   1 
ATOM   2774 C CB  . LYS   C 1 120 ? 10.730  41.218  8.260   1.00 27.18 ? 134 LYS   C CB  1 
ATOM   2775 C CG  . LYS   C 1 120 ? 10.412  41.782  9.639   1.00 28.84 ? 134 LYS   C CG  1 
ATOM   2776 C CD  . LYS   C 1 120 ? 9.456   42.967  9.544   1.00 31.02 ? 134 LYS   C CD  1 
ATOM   2777 C CE  . LYS   C 1 120 ? 9.134   43.536  10.919  1.00 32.81 ? 134 LYS   C CE  1 
ATOM   2778 N NZ  . LYS   C 1 120 ? 8.253   44.737  10.832  1.00 34.02 ? 134 LYS   C NZ  1 
ATOM   2779 N N   . PRO   C 1 121 ? 10.899  38.290  6.707   1.00 30.18 ? 135 PRO   C N   1 
ATOM   2780 C CA  . PRO   C 1 121 ? 10.864  37.545  5.442   1.00 32.02 ? 135 PRO   C CA  1 
ATOM   2781 C C   . PRO   C 1 121 ? 10.192  38.305  4.300   1.00 34.02 ? 135 PRO   C C   1 
ATOM   2782 O O   . PRO   C 1 121 ? 9.345   39.176  4.515   1.00 33.89 ? 135 PRO   C O   1 
ATOM   2783 C CB  . PRO   C 1 121 ? 10.042  36.303  5.797   1.00 31.31 ? 135 PRO   C CB  1 
ATOM   2784 C CG  . PRO   C 1 121 ? 9.178   36.739  6.934   1.00 30.81 ? 135 PRO   C CG  1 
ATOM   2785 C CD  . PRO   C 1 121 ? 10.025  37.686  7.729   1.00 30.19 ? 135 PRO   C CD  1 
ATOM   2786 O OXT . PRO   C 1 121 ? 10.482  38.053  3.126   1.00 35.82 ? 135 PRO   C OXT 1 
ATOM   2787 N N   . ALA   D 1 1   ? -0.351  13.319  -12.602 1.00 28.82 ? 15  ALA   D N   1 
ATOM   2788 C CA  . ALA   D 1 1   ? 0.042   13.402  -11.198 1.00 27.38 ? 15  ALA   D CA  1 
ATOM   2789 C C   . ALA   D 1 1   ? 1.255   14.312  -10.979 1.00 25.38 ? 15  ALA   D C   1 
ATOM   2790 O O   . ALA   D 1 1   ? 1.361   14.960  -9.938  1.00 25.87 ? 15  ALA   D O   1 
ATOM   2791 C CB  . ALA   D 1 1   ? 0.305   12.010  -10.631 1.00 27.71 ? 15  ALA   D CB  1 
ATOM   2792 N N   . GLY   D 1 2   ? 2.165   14.356  -11.959 1.00 24.22 ? 16  GLY   D N   1 
ATOM   2793 C CA  . GLY   D 1 2   ? 3.350   15.193  -11.885 1.00 22.04 ? 16  GLY   D CA  1 
ATOM   2794 C C   . GLY   D 1 2   ? 4.480   14.652  -11.031 1.00 19.15 ? 16  GLY   D C   1 
ATOM   2795 O O   . GLY   D 1 2   ? 5.520   15.316  -10.915 1.00 20.29 ? 16  GLY   D O   1 
ATOM   2796 N N   . ILE   D 1 3   ? 4.323   13.466  -10.455 1.00 17.57 ? 17  ILE   D N   1 
ATOM   2797 C CA  . ILE   D 1 3   ? 5.287   12.942  -9.488  1.00 15.50 ? 17  ILE   D CA  1 
ATOM   2798 C C   . ILE   D 1 3   ? 6.369   12.093  -10.154 1.00 14.20 ? 17  ILE   D C   1 
ATOM   2799 O O   . ILE   D 1 3   ? 7.534   12.142  -9.751  1.00 14.34 ? 17  ILE   D O   1 
ATOM   2800 C CB  . ILE   D 1 3   ? 4.528   12.171  -8.390  1.00 15.65 ? 17  ILE   D CB  1 
ATOM   2801 C CG1 . ILE   D 1 3   ? 3.675   13.131  -7.558  1.00 16.30 ? 17  ILE   D CG1 1 
ATOM   2802 C CG2 . ILE   D 1 3   ? 5.488   11.398  -7.499  1.00 15.79 ? 17  ILE   D CG2 1 
ATOM   2803 C CD1 . ILE   D 1 3   ? 2.683   12.427  -6.639  1.00 17.04 ? 17  ILE   D CD1 1 
ATOM   2804 N N   . THR   D 1 4   ? 6.020   11.301  -11.171 1.00 14.40 ? 18  THR   D N   1 
ATOM   2805 C CA  . THR   D 1 4   ? 7.005   10.432  -11.809 1.00 14.78 ? 18  THR   D CA  1 
ATOM   2806 C C   . THR   D 1 4   ? 8.178   11.246  -12.346 1.00 15.41 ? 18  THR   D C   1 
ATOM   2807 O O   . THR   D 1 4   ? 7.990   12.272  -13.004 1.00 16.42 ? 18  THR   D O   1 
ATOM   2808 C CB  . THR   D 1 4   ? 6.339   9.680   -12.965 1.00 15.96 ? 18  THR   D CB  1 
ATOM   2809 O OG1 . THR   D 1 4   ? 5.377   8.764   -12.428 1.00 16.44 ? 18  THR   D OG1 1 
ATOM   2810 C CG2 . THR   D 1 4   ? 7.375   8.912   -13.797 1.00 17.45 ? 18  THR   D CG2 1 
ATOM   2811 N N   . GLY   D 1 5   ? 9.385   10.790  -12.059 1.00 14.71 ? 19  GLY   D N   1 
ATOM   2812 C CA  . GLY   D 1 5   ? 10.594  11.425  -12.530 1.00 13.98 ? 19  GLY   D CA  1 
ATOM   2813 C C   . GLY   D 1 5   ? 11.655  11.440  -11.448 1.00 13.82 ? 19  GLY   D C   1 
ATOM   2814 O O   . GLY   D 1 5   ? 11.554  10.752  -10.429 1.00 14.55 ? 19  GLY   D O   1 
ATOM   2815 N N   . THR   D 1 6   ? 12.681  12.255  -11.671 1.00 13.95 ? 20  THR   D N   1 
ATOM   2816 C CA  . THR   D 1 6   ? 13.820  12.371  -10.772 1.00 14.38 ? 20  THR   D CA  1 
ATOM   2817 C C   . THR   D 1 6   ? 13.702  13.648  -9.953  1.00 13.30 ? 20  THR   D C   1 
ATOM   2818 O O   . THR   D 1 6   ? 13.413  14.721  -10.490 1.00 15.24 ? 20  THR   D O   1 
ATOM   2819 C CB  . THR   D 1 6   ? 15.116  12.388  -11.587 1.00 15.77 ? 20  THR   D CB  1 
ATOM   2820 O OG1 . THR   D 1 6   ? 15.204  11.174  -12.338 1.00 17.95 ? 20  THR   D OG1 1 
ATOM   2821 C CG2 . THR   D 1 6   ? 16.325  12.485  -10.678 1.00 16.84 ? 20  THR   D CG2 1 
ATOM   2822 N N   . TRP   D 1 7   ? 13.933  13.525  -8.650  1.00 12.65 ? 21  TRP   D N   1 
ATOM   2823 C CA  . TRP   D 1 7   ? 13.858  14.639  -7.717  1.00 12.50 ? 21  TRP   D CA  1 
ATOM   2824 C C   . TRP   D 1 7   ? 15.166  14.745  -6.940  1.00 12.54 ? 21  TRP   D C   1 
ATOM   2825 O O   . TRP   D 1 7   ? 15.873  13.752  -6.754  1.00 13.44 ? 21  TRP   D O   1 
ATOM   2826 C CB  . TRP   D 1 7   ? 12.692  14.431  -6.742  1.00 13.43 ? 21  TRP   D CB  1 
ATOM   2827 C CG  . TRP   D 1 7   ? 11.323  14.464  -7.381  1.00 13.40 ? 21  TRP   D CG  1 
ATOM   2828 C CD1 . TRP   D 1 7   ? 10.663  13.420  -7.969  1.00 13.85 ? 21  TRP   D CD1 1 
ATOM   2829 C CD2 . TRP   D 1 7   ? 10.449  15.595  -7.473  1.00 13.33 ? 21  TRP   D CD2 1 
ATOM   2830 N NE1 . TRP   D 1 7   ? 9.430   13.837  -8.424  1.00 14.64 ? 21  TRP   D NE1 1 
ATOM   2831 C CE2 . TRP   D 1 7   ? 9.276   15.169  -8.130  1.00 14.14 ? 21  TRP   D CE2 1 
ATOM   2832 C CE3 . TRP   D 1 7   ? 10.541  16.929  -7.057  1.00 13.34 ? 21  TRP   D CE3 1 
ATOM   2833 C CZ2 . TRP   D 1 7   ? 8.205   16.035  -8.382  1.00 14.24 ? 21  TRP   D CZ2 1 
ATOM   2834 C CZ3 . TRP   D 1 7   ? 9.482   17.783  -7.301  1.00 14.09 ? 21  TRP   D CZ3 1 
ATOM   2835 C CH2 . TRP   D 1 7   ? 8.327   17.332  -7.961  1.00 14.96 ? 21  TRP   D CH2 1 
ATOM   2836 N N   . TYR   D 1 8   ? 15.473  15.958  -6.475  1.00 12.67 ? 22  TYR   D N   1 
ATOM   2837 C CA  . TYR   D 1 8   ? 16.724  16.262  -5.783  1.00 13.33 ? 22  TYR   D CA  1 
ATOM   2838 C C   . TYR   D 1 8   ? 16.411  17.052  -4.523  1.00 13.07 ? 22  TYR   D C   1 
ATOM   2839 O O   . TYR   D 1 8   ? 15.653  18.022  -4.578  1.00 13.47 ? 22  TYR   D O   1 
ATOM   2840 C CB  . TYR   D 1 8   ? 17.637  17.111  -6.688  1.00 14.21 ? 22  TYR   D CB  1 
ATOM   2841 C CG  . TYR   D 1 8   ? 17.914  16.487  -8.044  1.00 13.93 ? 22  TYR   D CG  1 
ATOM   2842 C CD1 . TYR   D 1 8   ? 18.971  15.603  -8.216  1.00 15.67 ? 22  TYR   D CD1 1 
ATOM   2843 C CD2 . TYR   D 1 8   ? 17.122  16.780  -9.156  1.00 13.97 ? 22  TYR   D CD2 1 
ATOM   2844 C CE1 . TYR   D 1 8   ? 19.233  15.023  -9.441  1.00 16.02 ? 22  TYR   D CE1 1 
ATOM   2845 C CE2 . TYR   D 1 8   ? 17.385  16.200  -10.400 1.00 14.45 ? 22  TYR   D CE2 1 
ATOM   2846 C CZ  . TYR   D 1 8   ? 18.447  15.326  -10.529 1.00 14.79 ? 22  TYR   D CZ  1 
ATOM   2847 O OH  . TYR   D 1 8   ? 18.709  14.749  -11.750 1.00 16.17 ? 22  TYR   D OH  1 
ATOM   2848 N N   . ASN   D 1 9   ? 17.001  16.663  -3.393  1.00 14.22 ? 23  ASN   D N   1 
ATOM   2849 C CA  . ASN   D 1 9   ? 16.753  17.420  -2.172  1.00 16.24 ? 23  ASN   D CA  1 
ATOM   2850 C C   . ASN   D 1 9   ? 17.867  18.428  -1.925  1.00 17.69 ? 23  ASN   D C   1 
ATOM   2851 O O   . ASN   D 1 9   ? 18.797  18.574  -2.721  1.00 19.50 ? 23  ASN   D O   1 
ATOM   2852 C CB  . ASN   D 1 9   ? 16.415  16.547  -0.949  1.00 17.64 ? 23  ASN   D CB  1 
ATOM   2853 C CG  . ASN   D 1 9   ? 17.626  15.866  -0.329  1.00 19.42 ? 23  ASN   D CG  1 
ATOM   2854 O OD1 . ASN   D 1 9   ? 18.770  16.101  -0.708  1.00 18.64 ? 23  ASN   D OD1 1 
ATOM   2855 N ND2 . ASN   D 1 9   ? 17.363  15.022  0.665   1.00 22.72 ? 23  ASN   D ND2 1 
ATOM   2856 N N   . GLN   D 1 10  ? 17.767  19.121  -0.789  1.00 18.85 ? 24  GLN   D N   1 
ATOM   2857 C CA  . GLN   D 1 10  ? 18.651  20.230  -0.469  1.00 21.89 ? 24  GLN   D CA  1 
ATOM   2858 C C   . GLN   D 1 10  ? 20.058  19.777  -0.109  1.00 25.67 ? 24  GLN   D C   1 
ATOM   2859 O O   . GLN   D 1 10  ? 20.967  20.616  -0.056  1.00 27.98 ? 24  GLN   D O   1 
ATOM   2860 C CB  . GLN   D 1 10  ? 18.032  21.061  0.662   1.00 20.84 ? 24  GLN   D CB  1 
ATOM   2861 C CG  . GLN   D 1 10  ? 18.077  20.418  2.071   1.00 20.03 ? 24  GLN   D CG  1 
ATOM   2862 C CD  . GLN   D 1 10  ? 17.060  19.293  2.290   1.00 18.94 ? 24  GLN   D CD  1 
ATOM   2863 O OE1 . GLN   D 1 10  ? 16.159  19.069  1.474   1.00 18.17 ? 24  GLN   D OE1 1 
ATOM   2864 N NE2 . GLN   D 1 10  ? 17.199  18.589  3.414   1.00 20.77 ? 24  GLN   D NE2 1 
ATOM   2865 N N   . LEU   D 1 11  ? 20.259  18.485  0.142   1.00 26.94 ? 25  LEU   D N   1 
ATOM   2866 C CA  . LEU   D 1 11  ? 21.576  17.931  0.428   1.00 28.77 ? 25  LEU   D CA  1 
ATOM   2867 C C   . LEU   D 1 11  ? 22.102  17.062  -0.708  1.00 29.59 ? 25  LEU   D C   1 
ATOM   2868 O O   . LEU   D 1 11  ? 23.067  16.315  -0.510  1.00 30.54 ? 25  LEU   D O   1 
ATOM   2869 C CB  . LEU   D 1 11  ? 21.549  17.146  1.739   1.00 30.08 ? 25  LEU   D CB  1 
ATOM   2870 C CG  . LEU   D 1 11  ? 21.243  17.948  3.007   1.00 32.09 ? 25  LEU   D CG  1 
ATOM   2871 C CD1 . LEU   D 1 11  ? 21.207  17.035  4.220   1.00 32.93 ? 25  LEU   D CD1 1 
ATOM   2872 C CD2 . LEU   D 1 11  ? 22.260  19.065  3.203   1.00 32.71 ? 25  LEU   D CD2 1 
ATOM   2873 N N   . GLY   D 1 12  ? 21.487  17.132  -1.888  1.00 28.75 ? 26  GLY   D N   1 
ATOM   2874 C CA  . GLY   D 1 12  ? 21.972  16.422  -3.050  1.00 27.63 ? 26  GLY   D CA  1 
ATOM   2875 C C   . GLY   D 1 12  ? 21.383  15.045  -3.276  1.00 24.24 ? 26  GLY   D C   1 
ATOM   2876 O O   . GLY   D 1 12  ? 21.579  14.483  -4.364  1.00 25.39 ? 26  GLY   D O   1 
ATOM   2877 N N   . SER   D 1 13  ? 20.684  14.475  -2.293  1.00 19.66 ? 27  SER   D N   1 
ATOM   2878 C CA  . SER   D 1 13  ? 20.095  13.155  -2.482  1.00 17.75 ? 27  SER   D CA  1 
ATOM   2879 C C   . SER   D 1 13  ? 19.184  13.160  -3.700  1.00 16.61 ? 27  SER   D C   1 
ATOM   2880 O O   . SER   D 1 13  ? 18.516  14.151  -3.999  1.00 18.66 ? 27  SER   D O   1 
ATOM   2881 C CB  . SER   D 1 13  ? 19.280  12.750  -1.255  1.00 18.26 ? 27  SER   D CB  1 
ATOM   2882 O OG  . SER   D 1 13  ? 20.114  12.631  -0.124  1.00 20.26 ? 27  SER   D OG  1 
ATOM   2883 N N   . THR   D 1 14  ? 19.151  12.027  -4.396  1.00 15.48 ? 28  THR   D N   1 
ATOM   2884 C CA  . THR   D 1 14  ? 18.397  11.876  -5.634  1.00 16.01 ? 28  THR   D CA  1 
ATOM   2885 C C   . THR   D 1 14  ? 17.356  10.780  -5.455  1.00 16.06 ? 28  THR   D C   1 
ATOM   2886 O O   . THR   D 1 14  ? 17.699  9.647   -5.097  1.00 18.66 ? 28  THR   D O   1 
ATOM   2887 C CB  . THR   D 1 14  ? 19.348  11.532  -6.783  1.00 18.34 ? 28  THR   D CB  1 
ATOM   2888 O OG1 . THR   D 1 14  ? 20.334  12.559  -6.886  1.00 20.17 ? 28  THR   D OG1 1 
ATOM   2889 C CG2 . THR   D 1 14  ? 18.598  11.429  -8.101  1.00 19.75 ? 28  THR   D CG2 1 
ATOM   2890 N N   A PHE   D 1 15  ? 16.104  11.116  -5.788  0.80 14.89 ? 29  PHE   D N   1 
ATOM   2891 N N   B PHE   D 1 15  ? 16.086  11.120  -5.638  0.20 16.84 ? 29  PHE   D N   1 
ATOM   2892 C CA  A PHE   D 1 15  ? 14.891  10.321  -5.564  0.80 16.88 ? 29  PHE   D CA  1 
ATOM   2893 C CA  B PHE   D 1 15  ? 15.035  10.120  -5.520  0.20 17.80 ? 29  PHE   D CA  1 
ATOM   2894 C C   A PHE   D 1 15  ? 14.341  10.005  -6.957  0.80 16.64 ? 29  PHE   D C   1 
ATOM   2895 C C   B PHE   D 1 15  ? 14.314  9.949   -6.847  0.20 17.64 ? 29  PHE   D C   1 
ATOM   2896 O O   A PHE   D 1 15  ? 13.923  10.914  -7.688  0.80 17.43 ? 29  PHE   D O   1 
ATOM   2897 O O   B PHE   D 1 15  ? 13.728  10.896  -7.384  0.20 18.58 ? 29  PHE   D O   1 
ATOM   2898 C CB  A PHE   D 1 15  ? 13.941  11.202  -4.725  0.80 17.39 ? 29  PHE   D CB  1 
ATOM   2899 C CB  B PHE   D 1 15  ? 14.150  10.291  -4.274  0.20 18.76 ? 29  PHE   D CB  1 
ATOM   2900 C CG  A PHE   D 1 15  ? 12.542  10.657  -4.475  0.80 16.80 ? 29  PHE   D CG  1 
ATOM   2901 C CG  B PHE   D 1 15  ? 12.817  10.926  -4.500  0.20 18.63 ? 29  PHE   D CG  1 
ATOM   2902 C CD1 A PHE   D 1 15  ? 12.299  9.329   -4.162  0.80 16.04 ? 29  PHE   D CD1 1 
ATOM   2903 C CD1 B PHE   D 1 15  ? 11.777  10.232  -5.088  0.20 18.51 ? 29  PHE   D CD1 1 
ATOM   2904 C CD2 A PHE   D 1 15  ? 11.460  11.545  -4.461  0.80 15.70 ? 29  PHE   D CD2 1 
ATOM   2905 C CD2 B PHE   D 1 15  ? 12.567  12.189  -4.007  0.20 18.52 ? 29  PHE   D CD2 1 
ATOM   2906 C CE1 A PHE   D 1 15  ? 10.996  8.890   -3.898  0.80 16.83 ? 29  PHE   D CE1 1 
ATOM   2907 C CE1 B PHE   D 1 15  ? 10.548  10.824  -5.246  0.20 18.67 ? 29  PHE   D CE1 1 
ATOM   2908 C CE2 A PHE   D 1 15  ? 10.172  11.112  -4.193  0.80 16.78 ? 29  PHE   D CE2 1 
ATOM   2909 C CE2 B PHE   D 1 15  ? 11.338  12.778  -4.158  0.20 19.05 ? 29  PHE   D CE2 1 
ATOM   2910 C CZ  A PHE   D 1 15  ? 9.938   9.787   -3.916  0.80 16.84 ? 29  PHE   D CZ  1 
ATOM   2911 C CZ  B PHE   D 1 15  ? 10.329  12.097  -4.782  0.20 19.00 ? 29  PHE   D CZ  1 
ATOM   2912 N N   . ILE   D 1 16  ? 14.401  8.738   -7.370  1.00 16.90 ? 30  ILE   D N   1 
ATOM   2913 C CA  . ILE   D 1 16  ? 13.979  8.356   -8.711  1.00 17.29 ? 30  ILE   D CA  1 
ATOM   2914 C C   . ILE   D 1 16  ? 12.701  7.549   -8.548  1.00 16.14 ? 30  ILE   D C   1 
ATOM   2915 O O   . ILE   D 1 16  ? 12.744  6.435   -8.020  1.00 18.54 ? 30  ILE   D O   1 
ATOM   2916 C CB  . ILE   D 1 16  ? 15.070  7.505   -9.370  1.00 20.48 ? 30  ILE   D CB  1 
ATOM   2917 C CG1 . ILE   D 1 16  ? 16.395  8.275   -9.392  1.00 21.84 ? 30  ILE   D CG1 1 
ATOM   2918 C CG2 . ILE   D 1 16  ? 14.645  7.091   -10.752 1.00 21.00 ? 30  ILE   D CG2 1 
ATOM   2919 C CD1 . ILE   D 1 16  ? 17.604  7.401   -9.649  1.00 23.82 ? 30  ILE   D CD1 1 
ATOM   2920 N N   . VAL   D 1 17  ? 11.556  8.077   -8.996  1.00 14.02 ? 31  VAL   D N   1 
ATOM   2921 C CA  . VAL   D 1 17  ? 10.273  7.497   -8.600  1.00 13.95 ? 31  VAL   D CA  1 
ATOM   2922 C C   . VAL   D 1 17  ? 9.329   7.349   -9.789  1.00 14.41 ? 31  VAL   D C   1 
ATOM   2923 O O   . VAL   D 1 17  ? 9.318   8.172   -10.708 1.00 14.96 ? 31  VAL   D O   1 
ATOM   2924 C CB  . VAL   D 1 17  ? 9.601   8.321   -7.469  1.00 14.36 ? 31  VAL   D CB  1 
ATOM   2925 C CG1 . VAL   D 1 17  ? 9.097   9.668   -7.995  1.00 14.34 ? 31  VAL   D CG1 1 
ATOM   2926 C CG2 . VAL   D 1 17  ? 8.472   7.534   -6.788  1.00 14.32 ? 31  VAL   D CG2 1 
ATOM   2927 N N   . THR   D 1 18  ? 8.512   6.293   -9.750  1.00 15.24 ? 32  THR   D N   1 
ATOM   2928 C CA  . THR   D 1 18  ? 7.372   6.133   -10.645 1.00 15.75 ? 32  THR   D CA  1 
ATOM   2929 C C   . THR   D 1 18  ? 6.102   6.141   -9.808  1.00 14.02 ? 32  THR   D C   1 
ATOM   2930 O O   . THR   D 1 18  ? 5.994   5.392   -8.827  1.00 14.62 ? 32  THR   D O   1 
ATOM   2931 C CB  . THR   D 1 18  ? 7.456   4.819   -11.431 1.00 18.80 ? 32  THR   D CB  1 
ATOM   2932 O OG1 . THR   D 1 18  ? 8.632   4.836   -12.250 1.00 21.62 ? 32  THR   D OG1 1 
ATOM   2933 C CG2 . THR   D 1 18  ? 6.220   4.641   -12.320 1.00 20.68 ? 32  THR   D CG2 1 
ATOM   2934 N N   . ALA   D 1 19  ? 5.149   6.989   -10.190 1.00 14.53 ? 33  ALA   D N   1 
ATOM   2935 C CA  . ALA   D 1 19  ? 3.844   7.059   -9.538  1.00 15.18 ? 33  ALA   D CA  1 
ATOM   2936 C C   . ALA   D 1 19  ? 2.846   6.269   -10.377 1.00 15.15 ? 33  ALA   D C   1 
ATOM   2937 O O   . ALA   D 1 19  ? 2.445   6.709   -11.462 1.00 17.60 ? 33  ALA   D O   1 
ATOM   2938 C CB  . ALA   D 1 19  ? 3.400   8.511   -9.368  1.00 15.54 ? 33  ALA   D CB  1 
ATOM   2939 N N   . GLY   D 1 20  ? 2.469   5.085   -9.893  1.00 15.41 ? 34  GLY   D N   1 
ATOM   2940 C CA  . GLY   D 1 20  ? 1.569   4.224   -10.634 1.00 16.84 ? 34  GLY   D CA  1 
ATOM   2941 C C   . GLY   D 1 20  ? 0.121   4.671   -10.558 1.00 17.81 ? 34  GLY   D C   1 
ATOM   2942 O O   . GLY   D 1 20  ? -0.284  5.415   -9.663  1.00 17.80 ? 34  GLY   D O   1 
ATOM   2943 N N   . ALA   D 1 21  ? -0.678  4.164   -11.502 1.00 19.43 ? 35  ALA   D N   1 
ATOM   2944 C CA  . ALA   D 1 21  ? -2.042  4.660   -11.672 1.00 21.04 ? 35  ALA   D CA  1 
ATOM   2945 C C   . ALA   D 1 21  ? -2.906  4.431   -10.438 1.00 23.46 ? 35  ALA   D C   1 
ATOM   2946 O O   . ALA   D 1 21  ? -3.868  5.176   -10.212 1.00 25.64 ? 35  ALA   D O   1 
ATOM   2947 C CB  . ALA   D 1 21  ? -2.697  4.022   -12.898 1.00 22.03 ? 35  ALA   D CB  1 
ATOM   2948 N N   . ASP   D 1 22  ? -2.598  3.413   -9.634  1.00 22.27 ? 36  ASP   D N   1 
ATOM   2949 C CA  . ASP   D 1 22  ? -3.444  3.066   -8.499  1.00 23.49 ? 36  ASP   D CA  1 
ATOM   2950 C C   . ASP   D 1 22  ? -2.863  3.502   -7.154  1.00 20.66 ? 36  ASP   D C   1 
ATOM   2951 O O   . ASP   D 1 22  ? -3.349  3.063   -6.106  1.00 22.15 ? 36  ASP   D O   1 
ATOM   2952 C CB  . ASP   D 1 22  ? -3.798  1.576   -8.508  1.00 28.60 ? 36  ASP   D CB  1 
ATOM   2953 C CG  . ASP   D 1 22  ? -4.813  1.219   -9.593  1.00 32.47 ? 36  ASP   D CG  1 
ATOM   2954 O OD1 . ASP   D 1 22  ? -5.623  2.092   -9.976  1.00 32.81 ? 36  ASP   D OD1 1 
ATOM   2955 O OD2 . ASP   D 1 22  ? -4.805  0.060   -10.059 1.00 34.72 ? 36  ASP   D OD2 1 
ATOM   2956 N N   . GLY   D 1 23  ? -1.854  4.368   -7.158  1.00 16.78 ? 37  GLY   D N   1 
ATOM   2957 C CA  . GLY   D 1 23  ? -1.344  4.945   -5.932  1.00 14.50 ? 37  GLY   D CA  1 
ATOM   2958 C C   . GLY   D 1 23  ? 0.011   4.444   -5.496  1.00 12.74 ? 37  GLY   D C   1 
ATOM   2959 O O   . GLY   D 1 23  ? 0.476   4.854   -4.432  1.00 12.92 ? 37  GLY   D O   1 
ATOM   2960 N N   . ALA   D 1 24  ? 0.667   3.593   -6.273  1.00 12.67 ? 38  ALA   D N   1 
ATOM   2961 C CA  . ALA   D 1 24  ? 1.967   3.063   -5.887  1.00 13.10 ? 38  ALA   D CA  1 
ATOM   2962 C C   . ALA   D 1 24  ? 3.084   4.062   -6.162  1.00 12.26 ? 38  ALA   D C   1 
ATOM   2963 O O   . ALA   D 1 24  ? 3.099   4.730   -7.204  1.00 14.00 ? 38  ALA   D O   1 
ATOM   2964 C CB  . ALA   D 1 24  ? 2.249   1.778   -6.666  1.00 15.09 ? 38  ALA   D CB  1 
ATOM   2965 N N   . LEU   D 1 25  ? 4.038   4.139   -5.234  1.00 11.75 ? 39  LEU   D N   1 
ATOM   2966 C CA  . LEU   D 1 25  ? 5.338   4.757   -5.482  1.00 11.90 ? 39  LEU   D CA  1 
ATOM   2967 C C   . LEU   D 1 25  ? 6.403   3.664   -5.455  1.00 12.11 ? 39  LEU   D C   1 
ATOM   2968 O O   . LEU   D 1 25  ? 6.469   2.881   -4.499  1.00 12.81 ? 39  LEU   D O   1 
ATOM   2969 C CB  . LEU   D 1 25  ? 5.671   5.822   -4.426  1.00 12.32 ? 39  LEU   D CB  1 
ATOM   2970 C CG  . LEU   D 1 25  ? 4.766   7.055   -4.321  1.00 11.99 ? 39  LEU   D CG  1 
ATOM   2971 C CD1 . LEU   D 1 25  ? 5.251   7.962   -3.183  1.00 12.62 ? 39  LEU   D CD1 1 
ATOM   2972 C CD2 . LEU   D 1 25  ? 4.683   7.816   -5.647  1.00 12.85 ? 39  LEU   D CD2 1 
ATOM   2973 N N   . THR   D 1 26  ? 7.231   3.609   -6.500  1.00 12.21 ? 40  THR   D N   1 
ATOM   2974 C CA  . THR   D 1 26  ? 8.349   2.673   -6.572  1.00 12.66 ? 40  THR   D CA  1 
ATOM   2975 C C   . THR   D 1 26  ? 9.552   3.396   -7.158  1.00 13.23 ? 40  THR   D C   1 
ATOM   2976 O O   . THR   D 1 26  ? 9.398   4.338   -7.934  1.00 16.80 ? 40  THR   D O   1 
ATOM   2977 C CB  . THR   D 1 26  ? 8.011   1.460   -7.464  1.00 13.93 ? 40  THR   D CB  1 
ATOM   2978 O OG1 . THR   D 1 26  ? 7.694   1.908   -8.786  1.00 16.54 ? 40  THR   D OG1 1 
ATOM   2979 C CG2 . THR   D 1 26  ? 6.821   0.679   -6.918  1.00 15.03 ? 40  THR   D CG2 1 
ATOM   2980 N N   . GLY   D 1 27  ? 10.747  2.942   -6.810  1.00 13.47 ? 41  GLY   D N   1 
ATOM   2981 C CA  . GLY   D 1 27  ? 11.929  3.563   -7.401  1.00 13.32 ? 41  GLY   D CA  1 
ATOM   2982 C C   . GLY   D 1 27  ? 13.179  3.310   -6.573  1.00 12.99 ? 41  GLY   D C   1 
ATOM   2983 O O   . GLY   D 1 27  ? 13.289  2.296   -5.883  1.00 12.73 ? 41  GLY   D O   1 
ATOM   2984 N N   . THR   D 1 28  ? 14.122  4.249   -6.683  1.00 13.30 ? 42  THR   D N   1 
ATOM   2985 C CA  A THR   D 1 28  ? 15.411  4.120   -6.022  0.33 13.76 ? 42  THR   D CA  1 
ATOM   2986 C CA  B THR   D 1 28  ? 15.444  4.133   -6.081  0.67 13.67 ? 42  THR   D CA  1 
ATOM   2987 C C   . THR   D 1 28  ? 15.807  5.456   -5.416  1.00 13.70 ? 42  THR   D C   1 
ATOM   2988 O O   . THR   D 1 28  ? 15.468  6.523   -5.935  1.00 16.03 ? 42  THR   D O   1 
ATOM   2989 C CB  A THR   D 1 28  ? 16.523  3.700   -6.987  0.33 14.98 ? 42  THR   D CB  1 
ATOM   2990 C CB  B THR   D 1 28  ? 16.486  3.817   -7.173  0.67 15.34 ? 42  THR   D CB  1 
ATOM   2991 O OG1 A THR   D 1 28  ? 16.540  4.599   -8.098  0.33 15.55 ? 42  THR   D OG1 1 
ATOM   2992 O OG1 B THR   D 1 28  ? 16.072  2.659   -7.908  0.67 16.33 ? 42  THR   D OG1 1 
ATOM   2993 C CG2 A THR   D 1 28  ? 16.320  2.270   -7.472  0.33 15.60 ? 42  THR   D CG2 1 
ATOM   2994 C CG2 B THR   D 1 28  ? 17.867  3.555   -6.571  0.67 16.18 ? 42  THR   D CG2 1 
ATOM   2995 N N   . TYR   D 1 29  ? 16.508  5.383   -4.288  1.00 12.36 ? 43  TYR   D N   1 
ATOM   2996 C CA  . TYR   D 1 29  ? 17.015  6.559   -3.594  1.00 12.91 ? 43  TYR   D CA  1 
ATOM   2997 C C   . TYR   D 1 29  ? 18.531  6.443   -3.589  1.00 12.62 ? 43  TYR   D C   1 
ATOM   2998 O O   . TYR   D 1 29  ? 19.063  5.374   -3.284  1.00 13.96 ? 43  TYR   D O   1 
ATOM   2999 C CB  . TYR   D 1 29  ? 16.496  6.581   -2.145  1.00 14.18 ? 43  TYR   D CB  1 
ATOM   3000 C CG  . TYR   D 1 29  ? 16.445  7.958   -1.522  1.00 12.98 ? 43  TYR   D CG  1 
ATOM   3001 C CD1 . TYR   D 1 29  ? 15.311  8.743   -1.645  1.00 13.37 ? 43  TYR   D CD1 1 
ATOM   3002 C CD2 . TYR   D 1 29  ? 17.518  8.475   -0.810  1.00 14.92 ? 43  TYR   D CD2 1 
ATOM   3003 C CE1 . TYR   D 1 29  ? 15.242  10.008  -1.090  1.00 13.72 ? 43  TYR   D CE1 1 
ATOM   3004 C CE2 . TYR   D 1 29  ? 17.453  9.748   -0.234  1.00 14.51 ? 43  TYR   D CE2 1 
ATOM   3005 C CZ  . TYR   D 1 29  ? 16.310  10.510  -0.394  1.00 13.78 ? 43  TYR   D CZ  1 
ATOM   3006 O OH  . TYR   D 1 29  ? 16.196  11.772  0.145   1.00 15.15 ? 43  TYR   D OH  1 
ATOM   3007 N N   . GLU   D 1 30  ? 19.228  7.528   -3.927  1.00 13.61 ? 44  GLU   D N   1 
ATOM   3008 C CA  . GLU   D 1 30  ? 20.679  7.450   -4.040  1.00 14.69 ? 44  GLU   D CA  1 
ATOM   3009 C C   . GLU   D 1 30  ? 21.311  8.786   -3.665  1.00 16.00 ? 44  GLU   D C   1 
ATOM   3010 O O   . GLU   D 1 30  ? 20.631  9.781   -3.418  1.00 16.15 ? 44  GLU   D O   1 
ATOM   3011 C CB  . GLU   D 1 30  ? 21.112  6.985   -5.438  1.00 18.34 ? 44  GLU   D CB  1 
ATOM   3012 C CG  . GLU   D 1 30  ? 20.822  7.988   -6.529  1.00 20.78 ? 44  GLU   D CG  1 
ATOM   3013 C CD  . GLU   D 1 30  ? 20.980  7.405   -7.916  1.00 23.88 ? 44  GLU   D CD  1 
ATOM   3014 O OE1 . GLU   D 1 30  ? 20.669  6.210   -8.102  1.00 25.42 ? 44  GLU   D OE1 1 
ATOM   3015 O OE2 . GLU   D 1 30  ? 21.416  8.141   -8.821  1.00 26.90 ? 44  GLU   D OE2 1 
ATOM   3016 N N   . SER   D 1 31  ? 22.635  8.796   -3.616  1.00 16.66 ? 45  SER   D N   1 
ATOM   3017 C CA  . SER   D 1 31  ? 23.347  10.032  -3.337  1.00 18.55 ? 45  SER   D CA  1 
ATOM   3018 C C   . SER   D 1 31  ? 23.553  10.825  -4.623  1.00 20.74 ? 45  SER   D C   1 
ATOM   3019 O O   . SER   D 1 31  ? 23.297  10.345  -5.731  1.00 21.08 ? 45  SER   D O   1 
ATOM   3020 C CB  . SER   D 1 31  ? 24.701  9.730   -2.710  1.00 19.12 ? 45  SER   D CB  1 
ATOM   3021 O OG  . SER   D 1 31  ? 25.579  9.183   -3.676  1.00 19.67 ? 45  SER   D OG  1 
ATOM   3022 N N   . ALA   D 1 32  ? 24.037  12.061  -4.461  1.00 22.31 ? 46  ALA   D N   1 
ATOM   3023 C CA  . ALA   D 1 32  ? 24.356  12.888  -5.620  1.00 24.59 ? 46  ALA   D CA  1 
ATOM   3024 C C   . ALA   D 1 32  ? 25.338  12.183  -6.544  1.00 27.34 ? 46  ALA   D C   1 
ATOM   3025 O O   . ALA   D 1 32  ? 25.233  12.291  -7.770  1.00 28.60 ? 46  ALA   D O   1 
ATOM   3026 C CB  . ALA   D 1 32  ? 24.914  14.236  -5.165  1.00 24.69 ? 46  ALA   D CB  1 
ATOM   3027 N N   . VAL   D 1 33  ? 26.283  11.435  -5.969  1.00 28.49 ? 47  VAL   D N   1 
ATOM   3028 C CA  . VAL   D 1 33  ? 27.271  10.709  -6.766  1.00 29.45 ? 47  VAL   D CA  1 
ATOM   3029 C C   . VAL   D 1 33  ? 26.602  9.608   -7.581  1.00 28.87 ? 47  VAL   D C   1 
ATOM   3030 O O   . VAL   D 1 33  ? 26.868  9.447   -8.778  1.00 30.15 ? 47  VAL   D O   1 
ATOM   3031 C CB  . VAL   D 1 33  ? 28.382  10.153  -5.857  1.00 30.11 ? 47  VAL   D CB  1 
ATOM   3032 C CG1 . VAL   D 1 33  ? 29.293  9.225   -6.641  1.00 30.59 ? 47  VAL   D CG1 1 
ATOM   3033 C CG2 . VAL   D 1 33  ? 29.175  11.289  -5.231  1.00 31.29 ? 47  VAL   D CG2 1 
ATOM   3034 N N   . GLY   D 1 34  ? 25.740  8.822   -6.942  1.00 27.45 ? 48  GLY   D N   1 
ATOM   3035 C CA  . GLY   D 1 34  ? 25.008  7.785   -7.636  1.00 26.66 ? 48  GLY   D CA  1 
ATOM   3036 C C   . GLY   D 1 34  ? 25.710  6.451   -7.762  1.00 24.05 ? 48  GLY   D C   1 
ATOM   3037 O O   . GLY   D 1 34  ? 25.215  5.584   -8.494  1.00 24.21 ? 48  GLY   D O   1 
ATOM   3038 N N   . ASN   D 1 35  ? 26.835  6.250   -7.075  1.00 20.52 ? 49  ASN   D N   1 
ATOM   3039 C CA  . ASN   D 1 35  ? 27.507  4.958   -7.099  1.00 19.08 ? 49  ASN   D CA  1 
ATOM   3040 C C   . ASN   D 1 35  ? 26.592  3.880   -6.515  1.00 17.86 ? 49  ASN   D C   1 
ATOM   3041 O O   . ASN   D 1 35  ? 25.676  4.157   -5.739  1.00 17.41 ? 49  ASN   D O   1 
ATOM   3042 C CB  . ASN   D 1 35  ? 28.824  5.023   -6.321  1.00 19.13 ? 49  ASN   D CB  1 
ATOM   3043 C CG  . ASN   D 1 35  ? 28.631  5.502   -4.897  1.00 18.90 ? 49  ASN   D CG  1 
ATOM   3044 O OD1 . ASN   D 1 35  ? 28.077  6.576   -4.663  1.00 20.25 ? 49  ASN   D OD1 1 
ATOM   3045 N ND2 . ASN   D 1 35  ? 29.062  4.698   -3.936  1.00 19.17 ? 49  ASN   D ND2 1 
ATOM   3046 N N   . ALA   D 1 36  ? 26.864  2.630   -6.898  1.00 19.08 ? 50  ALA   D N   1 
ATOM   3047 C CA  . ALA   D 1 36  ? 25.969  1.530   -6.552  1.00 18.70 ? 50  ALA   D CA  1 
ATOM   3048 C C   . ALA   D 1 36  ? 25.838  1.354   -5.043  1.00 17.22 ? 50  ALA   D C   1 
ATOM   3049 O O   . ALA   D 1 36  ? 24.757  1.017   -4.545  1.00 17.31 ? 50  ALA   D O   1 
ATOM   3050 C CB  . ALA   D 1 36  ? 26.449  0.238   -7.216  1.00 20.80 ? 50  ALA   D CB  1 
ATOM   3051 N N   . GLU   D 1 37  ? 26.925  1.581   -4.295  1.00 16.38 ? 51  GLU   D N   1 
ATOM   3052 C CA  . GLU   D 1 37  ? 26.890  1.422   -2.847  1.00 17.27 ? 51  GLU   D CA  1 
ATOM   3053 C C   . GLU   D 1 37  ? 25.970  2.428   -2.176  1.00 16.29 ? 51  GLU   D C   1 
ATOM   3054 O O   . GLU   D 1 37  ? 25.645  2.256   -0.993  1.00 18.07 ? 51  GLU   D O   1 
ATOM   3055 C CB  . GLU   D 1 37  ? 28.309  1.540   -2.271  1.00 17.84 ? 51  GLU   D CB  1 
ATOM   3056 C CG  . GLU   D 1 37  ? 29.273  0.458   -2.762  1.00 18.55 ? 51  GLU   D CG  1 
ATOM   3057 C CD  . GLU   D 1 37  ? 29.943  0.778   -4.103  1.00 19.66 ? 51  GLU   D CD  1 
ATOM   3058 O OE1 . GLU   D 1 37  ? 29.630  1.827   -4.717  1.00 19.91 ? 51  GLU   D OE1 1 
ATOM   3059 O OE2 . GLU   D 1 37  ? 30.792  -0.025  -4.534  1.00 20.75 ? 51  GLU   D OE2 1 
ATOM   3060 N N   . SER   D 1 38  ? 25.528  3.454   -2.907  1.00 16.58 ? 52  SER   D N   1 
ATOM   3061 C CA  . SER   D 1 38  ? 24.682  4.517   -2.392  1.00 16.93 ? 52  SER   D CA  1 
ATOM   3062 C C   . SER   D 1 38  ? 23.223  4.377   -2.809  1.00 15.41 ? 52  SER   D C   1 
ATOM   3063 O O   . SER   D 1 38  ? 22.412  5.234   -2.450  1.00 16.17 ? 52  SER   D O   1 
ATOM   3064 C CB  . SER   D 1 38  ? 25.208  5.867   -2.897  1.00 20.49 ? 52  SER   D CB  1 
ATOM   3065 O OG  . SER   D 1 38  ? 24.636  6.212   -4.151  1.00 23.11 ? 52  SER   D OG  1 
ATOM   3066 N N   . ARG   D 1 39  ? 22.874  3.345   -3.576  1.00 14.28 ? 53  ARG   D N   1 
ATOM   3067 C CA  . ARG   D 1 39  ? 21.530  3.193   -4.126  1.00 14.13 ? 53  ARG   D CA  1 
ATOM   3068 C C   . ARG   D 1 39  ? 20.726  2.189   -3.310  1.00 13.69 ? 53  ARG   D C   1 
ATOM   3069 O O   . ARG   D 1 39  ? 21.225  1.109   -2.976  1.00 14.22 ? 53  ARG   D O   1 
ATOM   3070 C CB  . ARG   D 1 39  ? 21.591  2.694   -5.572  1.00 16.35 ? 53  ARG   D CB  1 
ATOM   3071 C CG  . ARG   D 1 39  ? 22.384  3.558   -6.547  1.00 20.06 ? 53  ARG   D CG  1 
ATOM   3072 C CD  . ARG   D 1 39  ? 22.139  3.131   -7.998  1.00 24.78 ? 53  ARG   D CD  1 
ATOM   3073 N NE  . ARG   D 1 39  ? 23.253  3.479   -8.870  1.00 29.67 ? 53  ARG   D NE  1 
ATOM   3074 C CZ  . ARG   D 1 39  ? 24.020  2.594   -9.494  1.00 33.63 ? 53  ARG   D CZ  1 
ATOM   3075 N NH1 . ARG   D 1 39  ? 23.792  1.293   -9.401  1.00 34.43 ? 53  ARG   D NH1 1 
ATOM   3076 N NH2 . ARG   D 1 39  ? 25.035  3.026   -10.239 1.00 35.88 ? 53  ARG   D NH2 1 
ATOM   3077 N N   . TYR   D 1 40  ? 19.465  2.535   -3.029  1.00 12.65 ? 54  TYR   D N   1 
ATOM   3078 C CA  . TYR   D 1 40  ? 18.585  1.712   -2.206  1.00 12.59 ? 54  TYR   D CA  1 
ATOM   3079 C C   . TYR   D 1 40  ? 17.179  1.695   -2.802  1.00 12.57 ? 54  TYR   D C   1 
ATOM   3080 O O   . TYR   D 1 40  ? 16.737  2.668   -3.423  1.00 13.34 ? 54  TYR   D O   1 
ATOM   3081 C CB  . TYR   D 1 40  ? 18.497  2.260   -0.772  1.00 13.17 ? 54  TYR   D CB  1 
ATOM   3082 C CG  . TYR   D 1 40  ? 19.823  2.420   -0.072  1.00 12.59 ? 54  TYR   D CG  1 
ATOM   3083 C CD1 . TYR   D 1 40  ? 20.590  3.566   -0.255  1.00 13.78 ? 54  TYR   D CD1 1 
ATOM   3084 C CD2 . TYR   D 1 40  ? 20.287  1.449   0.810   1.00 13.17 ? 54  TYR   D CD2 1 
ATOM   3085 C CE1 . TYR   D 1 40  ? 21.799  3.737   0.404   1.00 14.28 ? 54  TYR   D CE1 1 
ATOM   3086 C CE2 . TYR   D 1 40  ? 21.493  1.611   1.479   1.00 14.36 ? 54  TYR   D CE2 1 
ATOM   3087 C CZ  . TYR   D 1 40  ? 22.245  2.757   1.270   1.00 14.82 ? 54  TYR   D CZ  1 
ATOM   3088 O OH  . TYR   D 1 40  ? 23.436  2.930   1.942   1.00 16.74 ? 54  TYR   D OH  1 
ATOM   3089 N N   . VAL   D 1 41  ? 16.465  0.585   -2.575  1.00 13.09 ? 55  VAL   D N   1 
ATOM   3090 C CA  . VAL   D 1 41  ? 15.071  0.471   -3.003  1.00 13.20 ? 55  VAL   D CA  1 
ATOM   3091 C C   . VAL   D 1 41  ? 14.186  1.389   -2.166  1.00 13.41 ? 55  VAL   D C   1 
ATOM   3092 O O   . VAL   D 1 41  ? 14.372  1.529   -0.947  1.00 13.88 ? 55  VAL   D O   1 
ATOM   3093 C CB  . VAL   D 1 41  ? 14.602  -0.991  -2.869  1.00 14.23 ? 55  VAL   D CB  1 
ATOM   3094 C CG1 . VAL   D 1 41  ? 13.091  -1.128  -3.137  1.00 15.07 ? 55  VAL   D CG1 1 
ATOM   3095 C CG2 . VAL   D 1 41  ? 15.395  -1.906  -3.794  1.00 15.12 ? 55  VAL   D CG2 1 
ATOM   3096 N N   . LEU   D 1 42  ? 13.183  1.996   -2.801  1.00 14.09 ? 56  LEU   D N   1 
ATOM   3097 C CA  . LEU   D 1 42  ? 12.138  2.676   -2.051  1.00 15.86 ? 56  LEU   D CA  1 
ATOM   3098 C C   . LEU   D 1 42  ? 10.769  2.229   -2.530  1.00 14.93 ? 56  LEU   D C   1 
ATOM   3099 O O   . LEU   D 1 42  ? 10.576  1.907   -3.708  1.00 16.35 ? 56  LEU   D O   1 
ATOM   3100 C CB  . LEU   D 1 42  ? 12.212  4.181   -2.207  1.00 17.07 ? 56  LEU   D CB  1 
ATOM   3101 C CG  . LEU   D 1 42  ? 11.789  4.763   -3.557  1.00 17.14 ? 56  LEU   D CG  1 
ATOM   3102 C CD1 . LEU   D 1 42  ? 10.293  5.201   -3.632  1.00 16.09 ? 56  LEU   D CD1 1 
ATOM   3103 C CD2 . LEU   D 1 42  ? 12.696  5.914   -3.895  1.00 18.47 ? 56  LEU   D CD2 1 
ATOM   3104 N N   . THR   D 1 43  ? 9.811   2.251   -1.605  1.00 14.11 ? 57  THR   D N   1 
ATOM   3105 C CA  A THR   D 1 43  ? 8.420   2.019   -1.952  0.30 12.83 ? 57  THR   D CA  1 
ATOM   3106 C CA  B THR   D 1 43  ? 8.413   1.983   -1.921  0.70 13.03 ? 57  THR   D CA  1 
ATOM   3107 C C   . THR   D 1 43  ? 7.533   2.876   -1.060  1.00 11.26 ? 57  THR   D C   1 
ATOM   3108 O O   . THR   D 1 43  ? 7.876   3.181   0.087   1.00 11.07 ? 57  THR   D O   1 
ATOM   3109 C CB  A THR   D 1 43  ? 8.046   0.531   -1.872  0.30 15.04 ? 57  THR   D CB  1 
ATOM   3110 C CB  B THR   D 1 43  ? 7.995   0.497   -1.726  0.70 16.77 ? 57  THR   D CB  1 
ATOM   3111 O OG1 A THR   D 1 43  ? 6.687   0.353   -2.279  0.30 15.46 ? 57  THR   D OG1 1 
ATOM   3112 O OG1 B THR   D 1 43  ? 8.071   0.133   -0.341  0.70 18.85 ? 57  THR   D OG1 1 
ATOM   3113 C CG2 A THR   D 1 43  ? 8.214   0.016   -0.468  0.30 15.68 ? 57  THR   D CG2 1 
ATOM   3114 C CG2 B THR   D 1 43  ? 8.872   -0.441  -2.553  0.70 18.20 ? 57  THR   D CG2 1 
ATOM   3115 N N   . GLY   D 1 44  ? 6.397   3.286   -1.607  1.00 11.56 ? 58  GLY   D N   1 
ATOM   3116 C CA  . GLY   D 1 44  ? 5.448   4.081   -0.854  1.00 11.37 ? 58  GLY   D CA  1 
ATOM   3117 C C   . GLY   D 1 44  ? 4.110   4.186   -1.561  1.00 10.67 ? 58  GLY   D C   1 
ATOM   3118 O O   . GLY   D 1 44  ? 3.788   3.391   -2.452  1.00 11.15 ? 58  GLY   D O   1 
ATOM   3119 N N   . ARG   D 1 45  ? 3.327   5.189   -1.155  1.00 10.72 ? 59  ARG   D N   1 
ATOM   3120 C CA  . ARG   D 1 45  ? 1.958   5.375   -1.623  1.00 10.94 ? 59  ARG   D CA  1 
ATOM   3121 C C   . ARG   D 1 45  ? 1.699   6.868   -1.781  1.00 10.00 ? 59  ARG   D C   1 
ATOM   3122 O O   . ARG   D 1 45  ? 2.291   7.684   -1.070  1.00 10.98 ? 59  ARG   D O   1 
ATOM   3123 C CB  . ARG   D 1 45  ? 0.934   4.806   -0.612  1.00 10.79 ? 59  ARG   D CB  1 
ATOM   3124 C CG  . ARG   D 1 45  ? 1.044   3.298   -0.354  1.00 11.15 ? 59  ARG   D CG  1 
ATOM   3125 C CD  . ARG   D 1 45  ? 0.618   2.470   -1.561  1.00 11.46 ? 59  ARG   D CD  1 
ATOM   3126 N NE  . ARG   D 1 45  ? -0.805  2.626   -1.818  1.00 11.38 ? 59  ARG   D NE  1 
ATOM   3127 C CZ  . ARG   D 1 45  ? -1.410  2.229   -2.929  1.00 12.26 ? 59  ARG   D CZ  1 
ATOM   3128 N NH1 . ARG   D 1 45  ? -0.748  1.593   -3.886  1.00 13.17 ? 59  ARG   D NH1 1 
ATOM   3129 N NH2 . ARG   D 1 45  ? -2.703  2.497   -3.092  1.00 13.34 ? 59  ARG   D NH2 1 
ATOM   3130 N N   . TYR   D 1 46  ? 0.800   7.222   -2.702  1.00 10.90 ? 60  TYR   D N   1 
ATOM   3131 C CA  . TYR   D 1 46  ? 0.360   8.604   -2.850  1.00 11.34 ? 60  TYR   D CA  1 
ATOM   3132 C C   . TYR   D 1 46  ? -1.134  8.619   -3.147  1.00 11.12 ? 60  TYR   D C   1 
ATOM   3133 O O   . TYR   D 1 46  ? -1.701  7.621   -3.598  1.00 11.82 ? 60  TYR   D O   1 
ATOM   3134 C CB  . TYR   D 1 46  ? 1.140   9.352   -3.956  1.00 12.27 ? 60  TYR   D CB  1 
ATOM   3135 C CG  . TYR   D 1 46  ? 0.728   8.984   -5.374  1.00 12.74 ? 60  TYR   D CG  1 
ATOM   3136 C CD1 . TYR   D 1 46  ? 1.090   7.763   -5.931  1.00 13.27 ? 60  TYR   D CD1 1 
ATOM   3137 C CD2 . TYR   D 1 46  ? -0.022  9.864   -6.153  1.00 13.89 ? 60  TYR   D CD2 1 
ATOM   3138 C CE1 . TYR   D 1 46  ? 0.706   7.420   -7.224  1.00 14.05 ? 60  TYR   D CE1 1 
ATOM   3139 C CE2 . TYR   D 1 46  ? -0.407  9.535   -7.440  1.00 14.45 ? 60  TYR   D CE2 1 
ATOM   3140 C CZ  . TYR   D 1 46  ? -0.045  8.318   -7.973  1.00 14.43 ? 60  TYR   D CZ  1 
ATOM   3141 O OH  . TYR   D 1 46  ? -0.441  8.008   -9.262  1.00 16.19 ? 60  TYR   D OH  1 
ATOM   3142 N N   . ASP   D 1 47  ? -1.763  9.775   -2.911  1.00 11.51 ? 61  ASP   D N   1 
ATOM   3143 C CA  . ASP   D 1 47  ? -3.180  9.983   -3.219  1.00 11.52 ? 61  ASP   D CA  1 
ATOM   3144 C C   . ASP   D 1 47  ? -3.338  10.150  -4.730  1.00 12.39 ? 61  ASP   D C   1 
ATOM   3145 O O   . ASP   D 1 47  ? -2.978  11.193  -5.288  1.00 12.44 ? 61  ASP   D O   1 
ATOM   3146 C CB  . ASP   D 1 47  ? -3.672  11.232  -2.489  1.00 11.64 ? 61  ASP   D CB  1 
ATOM   3147 C CG  . ASP   D 1 47  ? -5.136  11.558  -2.769  1.00 12.42 ? 61  ASP   D CG  1 
ATOM   3148 O OD1 . ASP   D 1 47  ? -5.819  10.801  -3.502  1.00 12.78 ? 61  ASP   D OD1 1 
ATOM   3149 O OD2 . ASP   D 1 47  ? -5.609  12.589  -2.239  1.00 12.01 ? 61  ASP   D OD2 1 
ATOM   3150 N N   . SER   D 1 48  ? -3.904  9.141   -5.395  1.00 12.62 ? 62  SER   D N   1 
ATOM   3151 C CA  . SER   D 1 48  ? -4.030  9.171   -6.848  1.00 14.34 ? 62  SER   D CA  1 
ATOM   3152 C C   . SER   D 1 48  ? -5.260  9.926   -7.331  1.00 15.07 ? 62  SER   D C   1 
ATOM   3153 O O   . SER   D 1 48  ? -5.481  9.985   -8.541  1.00 17.17 ? 62  SER   D O   1 
ATOM   3154 C CB  . SER   D 1 48  ? -4.010  7.752   -7.430  1.00 15.86 ? 62  SER   D CB  1 
ATOM   3155 O OG  . SER   D 1 48  ? -4.945  6.926   -6.767  1.00 18.47 ? 62  SER   D OG  1 
ATOM   3156 N N   . ALA   D 1 49  ? -6.073  10.489  -6.437  1.00 14.65 ? 63  ALA   D N   1 
ATOM   3157 C CA  . ALA   D 1 49  ? -7.203  11.340  -6.826  1.00 15.34 ? 63  ALA   D CA  1 
ATOM   3158 C C   . ALA   D 1 49  ? -7.259  12.536  -5.888  1.00 15.84 ? 63  ALA   D C   1 
ATOM   3159 O O   . ALA   D 1 49  ? -8.180  12.671  -5.069  1.00 16.20 ? 63  ALA   D O   1 
ATOM   3160 C CB  . ALA   D 1 49  ? -8.512  10.547  -6.822  1.00 16.29 ? 63  ALA   D CB  1 
ATOM   3161 N N   . PRO   D 1 50  ? -6.276  13.430  -5.965  1.00 15.86 ? 64  PRO   D N   1 
ATOM   3162 C CA  . PRO   D 1 50  ? -6.216  14.557  -5.029  1.00 16.30 ? 64  PRO   D CA  1 
ATOM   3163 C C   . PRO   D 1 50  ? -7.364  15.534  -5.247  1.00 17.13 ? 64  PRO   D C   1 
ATOM   3164 O O   . PRO   D 1 50  ? -8.075  15.513  -6.257  1.00 18.43 ? 64  PRO   D O   1 
ATOM   3165 C CB  . PRO   D 1 50  ? -4.869  15.210  -5.356  1.00 16.73 ? 64  PRO   D CB  1 
ATOM   3166 C CG  . PRO   D 1 50  ? -4.633  14.855  -6.803  1.00 17.26 ? 64  PRO   D CG  1 
ATOM   3167 C CD  . PRO   D 1 50  ? -5.161  13.459  -6.938  1.00 16.76 ? 64  PRO   D CD  1 
ATOM   3168 N N   . ALA   D 1 51  ? -7.532  16.412  -4.260  1.00 17.73 ? 65  ALA   D N   1 
ATOM   3169 C CA  . ALA   D 1 51  ? -8.524  17.471  -4.348  1.00 19.54 ? 65  ALA   D CA  1 
ATOM   3170 C C   . ALA   D 1 51  ? -8.188  18.419  -5.497  1.00 21.85 ? 65  ALA   D C   1 
ATOM   3171 O O   . ALA   D 1 51  ? -7.051  18.491  -5.969  1.00 22.32 ? 65  ALA   D O   1 
ATOM   3172 C CB  . ALA   D 1 51  ? -8.577  18.249  -3.033  1.00 20.06 ? 65  ALA   D CB  1 
ATOM   3173 N N   . THR   D 1 52  ? -9.201  19.152  -5.951  1.00 24.33 ? 66  THR   D N   1 
ATOM   3174 C CA  . THR   D 1 52  ? -9.065  20.068  -7.078  1.00 27.52 ? 66  THR   D CA  1 
ATOM   3175 C C   . THR   D 1 52  ? -9.217  21.526  -6.654  1.00 28.95 ? 66  THR   D C   1 
ATOM   3176 O O   . THR   D 1 52  ? -9.603  22.377  -7.457  1.00 31.01 ? 66  THR   D O   1 
ATOM   3177 C CB  . THR   D 1 52  ? -10.045 19.708  -8.196  1.00 29.86 ? 66  THR   D CB  1 
ATOM   3178 O OG1 . THR   D 1 52  ? -11.378 19.681  -7.672  1.00 31.33 ? 66  THR   D OG1 1 
ATOM   3179 C CG2 . THR   D 1 52  ? -9.709  18.339  -8.772  1.00 30.99 ? 66  THR   D CG2 1 
ATOM   3180 N N   . ASP   D 1 53  ? -8.902  21.827  -5.395  1.00 27.99 ? 67  ASP   D N   1 
ATOM   3181 C CA  . ASP   D 1 53  ? -9.101  23.151  -4.820  1.00 27.13 ? 67  ASP   D CA  1 
ATOM   3182 C C   . ASP   D 1 53  ? -7.799  23.918  -4.620  1.00 26.58 ? 67  ASP   D C   1 
ATOM   3183 O O   . ASP   D 1 53  ? -7.800  24.957  -3.950  1.00 29.09 ? 67  ASP   D O   1 
ATOM   3184 C CB  . ASP   D 1 53  ? -9.851  23.037  -3.491  1.00 26.58 ? 67  ASP   D CB  1 
ATOM   3185 C CG  . ASP   D 1 53  ? -9.116  22.169  -2.473  1.00 26.43 ? 67  ASP   D CG  1 
ATOM   3186 O OD1 . ASP   D 1 53  ? -7.978  21.730  -2.748  1.00 24.36 ? 67  ASP   D OD1 1 
ATOM   3187 O OD2 . ASP   D 1 53  ? -9.679  21.921  -1.387  1.00 28.62 ? 67  ASP   D OD2 1 
ATOM   3188 N N   . GLY   D 1 54  ? -6.690  23.433  -5.171  1.00 24.46 ? 68  GLY   D N   1 
ATOM   3189 C CA  . GLY   D 1 54  ? -5.398  24.050  -4.955  1.00 23.17 ? 68  GLY   D CA  1 
ATOM   3190 C C   . GLY   D 1 54  ? -4.548  23.385  -3.894  1.00 21.27 ? 68  GLY   D C   1 
ATOM   3191 O O   . GLY   D 1 54  ? -3.402  23.806  -3.694  1.00 23.10 ? 68  GLY   D O   1 
ATOM   3192 N N   . SER   D 1 55  ? -5.066  22.360  -3.221  1.00 18.64 ? 69  SER   D N   1 
ATOM   3193 C CA  . SER   D 1 55  ? -4.311  21.636  -2.208  1.00 16.86 ? 69  SER   D CA  1 
ATOM   3194 C C   . SER   D 1 55  ? -3.258  20.742  -2.858  1.00 15.72 ? 69  SER   D C   1 
ATOM   3195 O O   . SER   D 1 55  ? -3.398  20.305  -4.006  1.00 15.63 ? 69  SER   D O   1 
ATOM   3196 C CB  . SER   D 1 55  ? -5.241  20.744  -1.382  1.00 18.66 ? 69  SER   D CB  1 
ATOM   3197 O OG  . SER   D 1 55  ? -6.201  21.496  -0.666  1.00 21.75 ? 69  SER   D OG  1 
ATOM   3198 N N   . GLY   D 1 56  ? -2.210  20.444  -2.093  1.00 14.68 ? 70  GLY   D N   1 
ATOM   3199 C CA  . GLY   D 1 56  ? -1.189  19.515  -2.529  1.00 14.10 ? 70  GLY   D CA  1 
ATOM   3200 C C   . GLY   D 1 56  ? -1.684  18.075  -2.524  1.00 13.09 ? 70  GLY   D C   1 
ATOM   3201 O O   . GLY   D 1 56  ? -2.795  17.759  -2.099  1.00 12.61 ? 70  GLY   D O   1 
ATOM   3202 N N   . THR   D 1 57  ? -0.810  17.182  -2.996  1.00 12.80 ? 71  THR   D N   1 
ATOM   3203 C CA  . THR   D 1 57  ? -1.082  15.748  -3.091  1.00 12.28 ? 71  THR   D CA  1 
ATOM   3204 C C   . THR   D 1 57  ? -0.304  15.011  -2.005  1.00 11.03 ? 71  THR   D C   1 
ATOM   3205 O O   . THR   D 1 57  ? 0.932   15.014  -2.017  1.00 11.41 ? 71  THR   D O   1 
ATOM   3206 C CB  . THR   D 1 57  ? -0.659  15.229  -4.470  1.00 12.61 ? 71  THR   D CB  1 
ATOM   3207 O OG1 . THR   D 1 57  ? -1.398  15.902  -5.487  1.00 13.39 ? 71  THR   D OG1 1 
ATOM   3208 C CG2 . THR   D 1 57  ? -0.909  13.735  -4.586  1.00 13.09 ? 71  THR   D CG2 1 
ATOM   3209 N N   . ALA   D 1 58  ? -1.023  14.379  -1.075  1.00 10.58 ? 72  ALA   D N   1 
ATOM   3210 C CA  . ALA   D 1 58  ? -0.359  13.683  0.027   1.00 10.95 ? 72  ALA   D CA  1 
ATOM   3211 C C   . ALA   D 1 58  ? 0.361   12.421  -0.455  1.00 10.70 ? 72  ALA   D C   1 
ATOM   3212 O O   . ALA   D 1 58  ? -0.117  11.712  -1.341  1.00 11.42 ? 72  ALA   D O   1 
ATOM   3213 C CB  . ALA   D 1 58  ? -1.373  13.335  1.116   1.00 11.54 ? 72  ALA   D CB  1 
ATOM   3214 N N   . LEU   D 1 59  ? 1.502   12.116  0.173   1.00 10.59 ? 73  LEU   D N   1 
ATOM   3215 C CA  A LEU   D 1 59  ? 2.308   10.966  -0.225  0.42 10.50 ? 73  LEU   D CA  1 
ATOM   3216 C CA  B LEU   D 1 59  ? 2.289   10.950  -0.216  0.58 10.81 ? 73  LEU   D CA  1 
ATOM   3217 C C   . LEU   D 1 59  ? 3.252   10.597  0.916   1.00 10.35 ? 73  LEU   D C   1 
ATOM   3218 O O   . LEU   D 1 59  ? 3.489   11.384  1.834   1.00 11.54 ? 73  LEU   D O   1 
ATOM   3219 C CB  A LEU   D 1 59  ? 3.107   11.270  -1.498  0.42 10.92 ? 73  LEU   D CB  1 
ATOM   3220 C CB  B LEU   D 1 59  ? 3.040   11.177  -1.543  0.58 11.90 ? 73  LEU   D CB  1 
ATOM   3221 C CG  A LEU   D 1 59  ? 3.885   12.592  -1.535  0.42 11.69 ? 73  LEU   D CG  1 
ATOM   3222 C CG  B LEU   D 1 59  ? 4.404   11.884  -1.582  0.58 12.58 ? 73  LEU   D CG  1 
ATOM   3223 C CD1 A LEU   D 1 59  ? 5.139   12.596  -0.650  0.42 12.37 ? 73  LEU   D CD1 1 
ATOM   3224 C CD1 B LEU   D 1 59  ? 4.964   11.874  -3.005  0.58 12.97 ? 73  LEU   D CD1 1 
ATOM   3225 C CD2 A LEU   D 1 59  ? 4.252   12.902  -2.971  0.42 11.35 ? 73  LEU   D CD2 1 
ATOM   3226 C CD2 B LEU   D 1 59  ? 4.296   13.311  -1.085  0.58 14.11 ? 73  LEU   D CD2 1 
ATOM   3227 N N   . GLY   D 1 60  ? 3.820   9.398   0.823   1.00 9.96  ? 74  GLY   D N   1 
ATOM   3228 C CA  . GLY   D 1 60  ? 4.892   8.985   1.712   1.00 9.99  ? 74  GLY   D CA  1 
ATOM   3229 C C   . GLY   D 1 60  ? 5.651   7.823   1.120   1.00 9.30  ? 74  GLY   D C   1 
ATOM   3230 O O   . GLY   D 1 60  ? 5.136   7.104   0.260   1.00 9.95  ? 74  GLY   D O   1 
ATOM   3231 N N   . TRP   D 1 61  ? 6.883   7.627   1.596   1.00 9.69  ? 75  TRP   D N   1 
ATOM   3232 C CA  . TRP   D 1 61  ? 7.667   6.477   1.149   1.00 9.52  ? 75  TRP   D CA  1 
ATOM   3233 C C   . TRP   D 1 61  ? 8.702   6.098   2.208   1.00 9.84  ? 75  TRP   D C   1 
ATOM   3234 O O   . TRP   D 1 61  ? 8.988   6.871   3.130   1.00 9.91  ? 75  TRP   D O   1 
ATOM   3235 C CB  . TRP   D 1 61  ? 8.320   6.707   -0.237  1.00 10.55 ? 75  TRP   D CB  1 
ATOM   3236 C CG  . TRP   D 1 61  ? 9.439   7.719   -0.256  1.00 10.56 ? 75  TRP   D CG  1 
ATOM   3237 C CD1 . TRP   D 1 61  ? 10.779  7.464   -0.095  1.00 11.87 ? 75  TRP   D CD1 1 
ATOM   3238 C CD2 . TRP   D 1 61  ? 9.326   9.134   -0.466  1.00 10.94 ? 75  TRP   D CD2 1 
ATOM   3239 N NE1 . TRP   D 1 61  ? 11.500  8.635   -0.184  1.00 11.83 ? 75  TRP   D NE1 1 
ATOM   3240 C CE2 . TRP   D 1 61  ? 10.632  9.675   -0.405  1.00 11.71 ? 75  TRP   D CE2 1 
ATOM   3241 C CE3 . TRP   D 1 61  ? 8.249   9.998   -0.696  1.00 12.43 ? 75  TRP   D CE3 1 
ATOM   3242 C CZ2 . TRP   D 1 61  ? 10.885  11.041  -0.555  1.00 12.99 ? 75  TRP   D CZ2 1 
ATOM   3243 C CZ3 . TRP   D 1 61  ? 8.507   11.350  -0.848  1.00 13.03 ? 75  TRP   D CZ3 1 
ATOM   3244 C CH2 . TRP   D 1 61  ? 9.813   11.859  -0.780  1.00 13.27 ? 75  TRP   D CH2 1 
ATOM   3245 N N   . THR   D 1 62  ? 9.251   4.884   2.065   1.00 10.18 ? 76  THR   D N   1 
ATOM   3246 C CA  . THR   D 1 62  ? 10.237  4.317   2.982   1.00 10.32 ? 76  THR   D CA  1 
ATOM   3247 C C   . THR   D 1 62  ? 11.462  3.833   2.209   1.00 10.23 ? 76  THR   D C   1 
ATOM   3248 O O   . THR   D 1 62  ? 11.332  3.276   1.105   1.00 11.30 ? 76  THR   D O   1 
ATOM   3249 C CB  . THR   D 1 62  ? 9.644   3.104   3.733   1.00 10.77 ? 76  THR   D CB  1 
ATOM   3250 O OG1 . THR   D 1 62  ? 8.452   3.489   4.419   1.00 10.26 ? 76  THR   D OG1 1 
ATOM   3251 C CG2 . THR   D 1 62  ? 10.626  2.529   4.745   1.00 11.04 ? 76  THR   D CG2 1 
ATOM   3252 N N   . VAL   D 1 63  ? 12.643  4.039   2.802   1.00 11.01 ? 77  VAL   D N   1 
ATOM   3253 C CA  . VAL   D 1 63  ? 13.896  3.412   2.383   1.00 11.66 ? 77  VAL   D CA  1 
ATOM   3254 C C   . VAL   D 1 63  ? 14.473  2.704   3.606   1.00 11.62 ? 77  VAL   D C   1 
ATOM   3255 O O   . VAL   D 1 63  ? 14.683  3.341   4.646   1.00 13.17 ? 77  VAL   D O   1 
ATOM   3256 C CB  . VAL   D 1 63  ? 14.914  4.450   1.876   1.00 13.00 ? 77  VAL   D CB  1 
ATOM   3257 C CG1 . VAL   D 1 63  ? 16.290  3.807   1.672   1.00 15.35 ? 77  VAL   D CG1 1 
ATOM   3258 C CG2 . VAL   D 1 63  ? 14.433  5.099   0.588   1.00 13.21 ? 77  VAL   D CG2 1 
ATOM   3259 N N   . ALA   D 1 64  ? 14.724  1.400   3.495   1.00 11.97 ? 78  ALA   D N   1 
ATOM   3260 C CA  . ALA   D 1 64  ? 15.560  0.709   4.472   1.00 12.33 ? 78  ALA   D CA  1 
ATOM   3261 C C   . ALA   D 1 64  ? 16.999  0.773   3.980   1.00 12.64 ? 78  ALA   D C   1 
ATOM   3262 O O   . ALA   D 1 64  ? 17.266  0.489   2.808   1.00 13.59 ? 78  ALA   D O   1 
ATOM   3263 C CB  . ALA   D 1 64  ? 15.118  -0.744  4.648   1.00 14.00 ? 78  ALA   D CB  1 
ATOM   3264 N N   . TRP   D 1 65  ? 17.921  1.142   4.872   1.00 12.32 ? 79  TRP   D N   1 
ATOM   3265 C CA  . TRP   D 1 65  ? 19.300  1.426   4.481   1.00 12.48 ? 79  TRP   D CA  1 
ATOM   3266 C C   . TRP   D 1 65  ? 20.142  0.156   4.380   1.00 13.04 ? 79  TRP   D C   1 
ATOM   3267 O O   . TRP   D 1 65  ? 21.226  0.055   4.965   1.00 15.24 ? 79  TRP   D O   1 
ATOM   3268 C CB  . TRP   D 1 65  ? 19.921  2.506   5.385   1.00 12.97 ? 79  TRP   D CB  1 
ATOM   3269 C CG  . TRP   D 1 65  ? 19.128  3.789   5.355   1.00 12.56 ? 79  TRP   D CG  1 
ATOM   3270 C CD1 . TRP   D 1 65  ? 18.309  4.278   6.340   1.00 13.20 ? 79  TRP   D CD1 1 
ATOM   3271 C CD2 . TRP   D 1 65  ? 19.029  4.718   4.260   1.00 13.21 ? 79  TRP   D CD2 1 
ATOM   3272 N NE1 . TRP   D 1 65  ? 17.733  5.456   5.933   1.00 13.48 ? 79  TRP   D NE1 1 
ATOM   3273 C CE2 . TRP   D 1 65  ? 18.151  5.746   4.662   1.00 13.27 ? 79  TRP   D CE2 1 
ATOM   3274 C CE3 . TRP   D 1 65  ? 19.599  4.782   2.984   1.00 12.98 ? 79  TRP   D CE3 1 
ATOM   3275 C CZ2 . TRP   D 1 65  ? 17.832  6.828   3.837   1.00 13.62 ? 79  TRP   D CZ2 1 
ATOM   3276 C CZ3 . TRP   D 1 65  ? 19.290  5.855   2.170   1.00 13.05 ? 79  TRP   D CZ3 1 
ATOM   3277 C CH2 . TRP   D 1 65  ? 18.411  6.863   2.594   1.00 13.34 ? 79  TRP   D CH2 1 
ATOM   3278 N N   . LYS   D 1 66  ? 19.633  -0.811  3.615   1.00 13.36 ? 80  LYS   D N   1 
ATOM   3279 C CA  . LYS   D 1 66  ? 20.333  -2.039  3.266   1.00 13.97 ? 80  LYS   D CA  1 
ATOM   3280 C C   . LYS   D 1 66  ? 20.323  -2.171  1.750   1.00 13.59 ? 80  LYS   D C   1 
ATOM   3281 O O   . LYS   D 1 66  ? 19.276  -2.011  1.115   1.00 13.47 ? 80  LYS   D O   1 
ATOM   3282 C CB  . LYS   D 1 66  ? 19.632  -3.264  3.872   1.00 14.85 ? 80  LYS   D CB  1 
ATOM   3283 C CG  . LYS   D 1 66  ? 20.230  -4.608  3.426   1.00 17.39 ? 80  LYS   D CG  1 
ATOM   3284 C CD  . LYS   D 1 66  ? 19.486  -5.802  4.029   1.00 19.43 ? 80  LYS   D CD  1 
ATOM   3285 C CE  . LYS   D 1 66  ? 19.954  -7.134  3.431   1.00 21.70 ? 80  LYS   D CE  1 
ATOM   3286 N NZ  . LYS   D 1 66  ? 19.488  -7.353  2.028   1.00 23.17 ? 80  LYS   D NZ  1 
ATOM   3287 N N   . ASN   D 1 67  ? 21.486  -2.460  1.171   1.00 14.01 ? 81  ASN   D N   1 
ATOM   3288 C CA  . ASN   D 1 67  ? 21.590  -2.839  -0.235  1.00 14.09 ? 81  ASN   D CA  1 
ATOM   3289 C C   . ASN   D 1 67  ? 22.569  -4.005  -0.324  1.00 14.77 ? 81  ASN   D C   1 
ATOM   3290 O O   . ASN   D 1 67  ? 22.956  -4.588  0.693   1.00 15.67 ? 81  ASN   D O   1 
ATOM   3291 C CB  . ASN   D 1 67  ? 21.911  -1.631  -1.130  1.00 14.75 ? 81  ASN   D CB  1 
ATOM   3292 C CG  . ASN   D 1 67  ? 23.240  -0.973  -0.789  1.00 14.32 ? 81  ASN   D CG  1 
ATOM   3293 O OD1 . ASN   D 1 67  ? 24.135  -1.602  -0.225  1.00 14.33 ? 81  ASN   D OD1 1 
ATOM   3294 N ND2 . ASN   D 1 67  ? 23.370  0.303   -1.138  1.00 14.82 ? 81  ASN   D ND2 1 
ATOM   3295 N N   . ASN   D 1 68  ? 22.984  -4.350  -1.542  1.00 15.25 ? 82  ASN   D N   1 
ATOM   3296 C CA  . ASN   D 1 68  ? 23.895  -5.477  -1.712  1.00 17.28 ? 82  ASN   D CA  1 
ATOM   3297 C C   . ASN   D 1 68  ? 25.304  -5.191  -1.215  1.00 17.64 ? 82  ASN   D C   1 
ATOM   3298 O O   . ASN   D 1 68  ? 26.134  -6.107  -1.217  1.00 19.88 ? 82  ASN   D O   1 
ATOM   3299 C CB  . ASN   D 1 68  ? 23.943  -5.891  -3.184  1.00 21.62 ? 82  ASN   D CB  1 
ATOM   3300 C CG  . ASN   D 1 68  ? 22.662  -6.569  -3.639  1.00 27.66 ? 82  ASN   D CG  1 
ATOM   3301 O OD1 . ASN   D 1 68  ? 21.707  -6.696  -2.871  1.00 29.77 ? 82  ASN   D OD1 1 
ATOM   3302 N ND2 . ASN   D 1 68  ? 22.636  -7.005  -4.894  1.00 31.07 ? 82  ASN   D ND2 1 
ATOM   3303 N N   . TYR   D 1 69  ? 25.592  -3.964  -0.777  1.00 16.21 ? 83  TYR   D N   1 
ATOM   3304 C CA  . TYR   D 1 69  ? 26.941  -3.551  -0.427  1.00 16.02 ? 83  TYR   D CA  1 
ATOM   3305 C C   . TYR   D 1 69  ? 27.120  -3.144  1.028   1.00 15.22 ? 83  TYR   D C   1 
ATOM   3306 O O   . TYR   D 1 69  ? 28.255  -3.168  1.512   1.00 16.77 ? 83  TYR   D O   1 
ATOM   3307 C CB  . TYR   D 1 69  ? 27.386  -2.392  -1.335  1.00 16.37 ? 83  TYR   D CB  1 
ATOM   3308 C CG  . TYR   D 1 69  ? 27.129  -2.697  -2.794  1.00 16.84 ? 83  TYR   D CG  1 
ATOM   3309 C CD1 . TYR   D 1 69  ? 28.022  -3.468  -3.531  1.00 18.81 ? 83  TYR   D CD1 1 
ATOM   3310 C CD2 . TYR   D 1 69  ? 25.971  -2.254  -3.425  1.00 17.55 ? 83  TYR   D CD2 1 
ATOM   3311 C CE1 . TYR   D 1 69  ? 27.777  -3.767  -4.860  1.00 19.58 ? 83  TYR   D CE1 1 
ATOM   3312 C CE2 . TYR   D 1 69  ? 25.716  -2.551  -4.752  1.00 18.56 ? 83  TYR   D CE2 1 
ATOM   3313 C CZ  . TYR   D 1 69  ? 26.624  -3.307  -5.464  1.00 19.72 ? 83  TYR   D CZ  1 
ATOM   3314 O OH  . TYR   D 1 69  ? 26.381  -3.612  -6.786  1.00 21.27 ? 83  TYR   D OH  1 
ATOM   3315 N N   . ARG   D 1 70  ? 26.049  -2.778  1.735   1.00 15.01 ? 84  ARG   D N   1 
ATOM   3316 C CA  A ARG   D 1 70  ? 26.152  -2.311  3.114   0.61 15.58 ? 84  ARG   D CA  1 
ATOM   3317 C CA  B ARG   D 1 70  ? 26.163  -2.375  3.131   0.39 16.57 ? 84  ARG   D CA  1 
ATOM   3318 C C   . ARG   D 1 70  ? 24.790  -2.444  3.782   1.00 15.73 ? 84  ARG   D C   1 
ATOM   3319 O O   . ARG   D 1 70  ? 23.768  -2.633  3.120   1.00 15.35 ? 84  ARG   D O   1 
ATOM   3320 C CB  A ARG   D 1 70  ? 26.637  -0.858  3.180   0.61 15.93 ? 84  ARG   D CB  1 
ATOM   3321 C CB  B ARG   D 1 70  ? 26.792  -0.985  3.281   0.39 18.81 ? 84  ARG   D CB  1 
ATOM   3322 C CG  A ARG   D 1 70  ? 25.630  0.149   2.653   0.61 14.31 ? 84  ARG   D CG  1 
ATOM   3323 C CG  B ARG   D 1 70  ? 26.245  0.071   2.339   0.39 20.03 ? 84  ARG   D CG  1 
ATOM   3324 C CD  A ARG   D 1 70  ? 26.210  1.560   2.605   0.61 14.66 ? 84  ARG   D CD  1 
ATOM   3325 C CD  B ARG   D 1 70  ? 26.994  1.375   2.541   0.39 20.66 ? 84  ARG   D CD  1 
ATOM   3326 N NE  A ARG   D 1 70  ? 26.662  2.021   3.915   0.61 15.32 ? 84  ARG   D NE  1 
ATOM   3327 N NE  B ARG   D 1 70  ? 26.672  2.379   1.538   0.39 20.83 ? 84  ARG   D NE  1 
ATOM   3328 C CZ  A ARG   D 1 70  ? 25.878  2.552   4.846   0.61 15.19 ? 84  ARG   D CZ  1 
ATOM   3329 C CZ  B ARG   D 1 70  ? 27.168  3.609   1.523   0.39 18.84 ? 84  ARG   D CZ  1 
ATOM   3330 N NH1 A ARG   D 1 70  ? 24.571  2.684   4.664   0.61 14.87 ? 84  ARG   D NH1 1 
ATOM   3331 N NH1 B ARG   D 1 70  ? 28.020  4.024   2.446   0.39 20.77 ? 84  ARG   D NH1 1 
ATOM   3332 N NH2 A ARG   D 1 70  ? 26.418  2.963   5.988   0.61 15.79 ? 84  ARG   D NH2 1 
ATOM   3333 N NH2 B ARG   D 1 70  ? 26.788  4.448   0.566   0.39 14.71 ? 84  ARG   D NH2 1 
ATOM   3334 N N   . ASN   D 1 71  ? 24.786  -2.308  5.106   1.00 16.16 ? 85  ASN   D N   1 
ATOM   3335 C CA  . ASN   D 1 71  ? 23.547  -2.387  5.877   1.00 16.53 ? 85  ASN   D CA  1 
ATOM   3336 C C   . ASN   D 1 71  ? 23.736  -1.588  7.158   1.00 16.64 ? 85  ASN   D C   1 
ATOM   3337 O O   . ASN   D 1 71  ? 24.475  -2.015  8.054   1.00 18.20 ? 85  ASN   D O   1 
ATOM   3338 C CB  . ASN   D 1 71  ? 23.183  -3.834  6.198   1.00 15.71 ? 85  ASN   D CB  1 
ATOM   3339 C CG  . ASN   D 1 71  ? 21.790  -3.960  6.789   1.00 15.43 ? 85  ASN   D CG  1 
ATOM   3340 O OD1 . ASN   D 1 71  ? 21.151  -2.958  7.101   1.00 15.82 ? 85  ASN   D OD1 1 
ATOM   3341 N ND2 . ASN   D 1 71  ? 21.310  -5.188  6.931   1.00 16.28 ? 85  ASN   D ND2 1 
ATOM   3342 N N   . ALA   D 1 72  ? 23.060  -0.445  7.251   1.00 15.68 ? 86  ALA   D N   1 
ATOM   3343 C CA  . ALA   D 1 72  ? 23.128  0.409   8.430   1.00 16.79 ? 86  ALA   D CA  1 
ATOM   3344 C C   . ALA   D 1 72  ? 22.077  0.069   9.479   1.00 15.84 ? 86  ALA   D C   1 
ATOM   3345 O O   . ALA   D 1 72  ? 21.993  0.765   10.498  1.00 17.37 ? 86  ALA   D O   1 
ATOM   3346 C CB  . ALA   D 1 72  ? 22.991  1.877   8.022   1.00 18.39 ? 86  ALA   D CB  1 
ATOM   3347 N N   . HIS   D 1 73  ? 21.276  -0.972  9.258   1.00 16.06 ? 87  HIS   D N   1 
ATOM   3348 C CA  . HIS   D 1 73  ? 20.270  -1.434  10.217  1.00 16.18 ? 87  HIS   D CA  1 
ATOM   3349 C C   . HIS   D 1 73  ? 19.356  -0.291  10.657  1.00 15.50 ? 87  HIS   D C   1 
ATOM   3350 O O   . HIS   D 1 73  ? 19.201  0.002   11.847  1.00 16.47 ? 87  HIS   D O   1 
ATOM   3351 C CB  . HIS   D 1 73  ? 20.921  -2.136  11.418  1.00 16.14 ? 87  HIS   D CB  1 
ATOM   3352 C CG  . HIS   D 1 73  ? 21.831  -3.264  11.043  1.00 16.40 ? 87  HIS   D CG  1 
ATOM   3353 N ND1 . HIS   D 1 73  ? 21.428  -4.324  10.258  1.00 17.13 ? 87  HIS   D ND1 1 
ATOM   3354 C CD2 . HIS   D 1 73  ? 23.126  -3.499  11.359  1.00 17.61 ? 87  HIS   D CD2 1 
ATOM   3355 C CE1 . HIS   D 1 73  ? 22.440  -5.161  10.105  1.00 17.29 ? 87  HIS   D CE1 1 
ATOM   3356 N NE2 . HIS   D 1 73  ? 23.479  -4.686  10.768  1.00 17.79 ? 87  HIS   D NE2 1 
ATOM   3357 N N   . SER   D 1 74  ? 18.754  0.366   9.667   1.00 15.17 ? 88  SER   D N   1 
ATOM   3358 C CA  . SER   D 1 74  ? 17.918  1.534   9.922   1.00 14.65 ? 88  SER   D CA  1 
ATOM   3359 C C   . SER   D 1 74  ? 17.022  1.764   8.712   1.00 13.54 ? 88  SER   D C   1 
ATOM   3360 O O   . SER   D 1 74  ? 17.238  1.191   7.644   1.00 13.45 ? 88  SER   D O   1 
ATOM   3361 C CB  . SER   D 1 74  ? 18.756  2.782   10.205  1.00 18.14 ? 88  SER   D CB  1 
ATOM   3362 O OG  . SER   D 1 74  ? 19.594  3.069   9.107   1.00 21.21 ? 88  SER   D OG  1 
ATOM   3363 N N   . ALA   D 1 75  ? 16.015  2.624   8.884   1.00 13.10 ? 89  ALA   D N   1 
ATOM   3364 C CA  . ALA   D 1 75  ? 15.079  2.944   7.816   1.00 12.56 ? 89  ALA   D CA  1 
ATOM   3365 C C   . ALA   D 1 75  ? 14.549  4.355   8.014   1.00 10.76 ? 89  ALA   D C   1 
ATOM   3366 O O   . ALA   D 1 75  ? 14.306  4.782   9.151   1.00 11.78 ? 89  ALA   D O   1 
ATOM   3367 C CB  . ALA   D 1 75  ? 13.904  1.968   7.822   1.00 13.25 ? 89  ALA   D CB  1 
ATOM   3368 N N   . THR   D 1 76  ? 14.323  5.059   6.907   1.00 11.00 ? 90  THR   D N   1 
ATOM   3369 C CA  . THR   D 1 76  ? 13.714  6.384   6.914   1.00 10.40 ? 90  THR   D CA  1 
ATOM   3370 C C   . THR   D 1 76  ? 12.354  6.351   6.226   1.00 10.57 ? 90  THR   D C   1 
ATOM   3371 O O   . THR   D 1 76  ? 12.197  5.725   5.170   1.00 10.69 ? 90  THR   D O   1 
ATOM   3372 C CB  . THR   D 1 76  ? 14.620  7.374   6.183   1.00 11.12 ? 90  THR   D CB  1 
ATOM   3373 O OG1 . THR   D 1 76  ? 15.891  7.432   6.844   1.00 12.06 ? 90  THR   D OG1 1 
ATOM   3374 C CG2 . THR   D 1 76  ? 14.004  8.772   6.132   1.00 11.38 ? 90  THR   D CG2 1 
ATOM   3375 N N   . THR   D 1 77  ? 11.374  7.040   6.810   1.00 10.27 ? 91  THR   D N   1 
ATOM   3376 C CA  . THR   D 1 77  ? 10.105  7.334   6.146   1.00 10.08 ? 91  THR   D CA  1 
ATOM   3377 C C   . THR   D 1 77  ? 9.979   8.835   5.926   1.00 10.40 ? 91  THR   D C   1 
ATOM   3378 O O   . THR   D 1 77  ? 10.248  9.627   6.836   1.00 12.77 ? 91  THR   D O   1 
ATOM   3379 C CB  . THR   D 1 77  ? 8.884   6.862   6.947   1.00 10.48 ? 91  THR   D CB  1 
ATOM   3380 O OG1 . THR   D 1 77  ? 8.831   7.528   8.219   1.00 11.57 ? 91  THR   D OG1 1 
ATOM   3381 C CG2 . THR   D 1 77  ? 8.915   5.371   7.180   1.00 11.78 ? 91  THR   D CG2 1 
ATOM   3382 N N   . TRP   D 1 78  ? 9.554   9.223   4.725   1.00 9.86  ? 92  TRP   D N   1 
ATOM   3383 C CA  . TRP   D 1 78  ? 9.239   10.610  4.393   1.00 9.34  ? 92  TRP   D CA  1 
ATOM   3384 C C   . TRP   D 1 78  ? 7.728   10.728  4.240   1.00 9.55  ? 92  TRP   D C   1 
ATOM   3385 O O   . TRP   D 1 78  ? 7.115   9.918   3.539   1.00 10.36 ? 92  TRP   D O   1 
ATOM   3386 C CB  . TRP   D 1 78  ? 9.873   11.027  3.063   1.00 10.25 ? 92  TRP   D CB  1 
ATOM   3387 C CG  . TRP   D 1 78  ? 11.372  11.161  3.010   1.00 9.71  ? 92  TRP   D CG  1 
ATOM   3388 C CD1 . TRP   D 1 78  ? 12.084  12.328  3.003   1.00 10.35 ? 92  TRP   D CD1 1 
ATOM   3389 C CD2 . TRP   D 1 78  ? 12.340  10.101  2.875   1.00 10.36 ? 92  TRP   D CD2 1 
ATOM   3390 N NE1 . TRP   D 1 78  ? 13.428  12.062  2.876   1.00 11.11 ? 92  TRP   D NE1 1 
ATOM   3391 C CE2 . TRP   D 1 78  ? 13.613  10.705  2.798   1.00 10.64 ? 92  TRP   D CE2 1 
ATOM   3392 C CE3 . TRP   D 1 78  ? 12.251  8.703   2.804   1.00 10.67 ? 92  TRP   D CE3 1 
ATOM   3393 C CZ2 . TRP   D 1 78  ? 14.787  9.957   2.641   1.00 11.53 ? 92  TRP   D CZ2 1 
ATOM   3394 C CZ3 . TRP   D 1 78  ? 13.412  7.969   2.648   1.00 12.13 ? 92  TRP   D CZ3 1 
ATOM   3395 C CH2 . TRP   D 1 78  ? 14.662  8.597   2.579   1.00 11.41 ? 92  TRP   D CH2 1 
ATOM   3396 N N   . SER   D 1 79  ? 7.138   11.739  4.884   1.00 9.33  ? 93  SER   D N   1 
ATOM   3397 C CA  . SER   D 1 79  ? 5.713   12.036  4.832   1.00 10.68 ? 93  SER   D CA  1 
ATOM   3398 C C   . SER   D 1 79  ? 5.550   13.474  4.357   1.00 9.75  ? 93  SER   D C   1 
ATOM   3399 O O   . SER   D 1 79  ? 6.187   14.377  4.904   1.00 10.47 ? 93  SER   D O   1 
ATOM   3400 C CB  . SER   D 1 79  ? 5.123   11.894  6.240   1.00 11.61 ? 93  SER   D CB  1 
ATOM   3401 O OG  . SER   D 1 79  ? 3.723   12.109  6.233   1.00 12.36 ? 93  SER   D OG  1 
ATOM   3402 N N   . GLY   D 1 80  ? 4.739   13.702  3.327   1.00 9.87  ? 94  GLY   D N   1 
ATOM   3403 C CA  . GLY   D 1 80  ? 4.649   15.058  2.823   1.00 10.83 ? 94  GLY   D CA  1 
ATOM   3404 C C   . GLY   D 1 80  ? 3.590   15.253  1.769   1.00 9.99  ? 94  GLY   D C   1 
ATOM   3405 O O   . GLY   D 1 80  ? 2.615   14.507  1.690   1.00 10.68 ? 94  GLY   D O   1 
ATOM   3406 N N   . GLN   D 1 81  ? 3.786   16.299  0.967   1.00 10.67 ? 95  GLN   D N   1 
ATOM   3407 C CA  . GLN   D 1 81  ? 2.875   16.595  -0.129  1.00 11.54 ? 95  GLN   D CA  1 
ATOM   3408 C C   . GLN   D 1 81  ? 3.625   17.138  -1.337  1.00 12.00 ? 95  GLN   D C   1 
ATOM   3409 O O   . GLN   D 1 81  ? 4.623   17.856  -1.203  1.00 11.82 ? 95  GLN   D O   1 
ATOM   3410 C CB  . GLN   D 1 81  ? 1.716   17.514  0.285   1.00 13.90 ? 95  GLN   D CB  1 
ATOM   3411 C CG  . GLN   D 1 81  ? 2.105   18.854  0.863   1.00 15.26 ? 95  GLN   D CG  1 
ATOM   3412 C CD  . GLN   D 1 81  ? 0.886   19.640  1.326   1.00 14.40 ? 95  GLN   D CD  1 
ATOM   3413 O OE1 . GLN   D 1 81  ? -0.110  19.737  0.607   1.00 13.31 ? 95  GLN   D OE1 1 
ATOM   3414 N NE2 . GLN   D 1 81  ? 0.957   20.206  2.532   1.00 15.17 ? 95  GLN   D NE2 1 
ATOM   3415 N N   . TYR   D 1 82  ? 3.138   16.751  -2.516  1.00 11.98 ? 96  TYR   D N   1 
ATOM   3416 C CA  . TYR   D 1 82  ? 3.595   17.263  -3.798  1.00 11.96 ? 96  TYR   D CA  1 
ATOM   3417 C C   . TYR   D 1 82  ? 2.793   18.502  -4.159  1.00 13.34 ? 96  TYR   D C   1 
ATOM   3418 O O   . TYR   D 1 82  ? 1.564   18.531  -4.012  1.00 14.10 ? 96  TYR   D O   1 
ATOM   3419 C CB  . TYR   D 1 82  ? 3.415   16.181  -4.867  1.00 12.85 ? 96  TYR   D CB  1 
ATOM   3420 C CG  . TYR   D 1 82  ? 3.368   16.699  -6.292  1.00 14.34 ? 96  TYR   D CG  1 
ATOM   3421 C CD1 . TYR   D 1 82  ? 4.539   16.911  -7.023  1.00 14.90 ? 96  TYR   D CD1 1 
ATOM   3422 C CD2 . TYR   D 1 82  ? 2.152   16.983  -6.914  1.00 16.57 ? 96  TYR   D CD2 1 
ATOM   3423 C CE1 . TYR   D 1 82  ? 4.494   17.391  -8.336  1.00 16.91 ? 96  TYR   D CE1 1 
ATOM   3424 C CE2 . TYR   D 1 82  ? 2.102   17.466  -8.217  1.00 18.24 ? 96  TYR   D CE2 1 
ATOM   3425 C CZ  . TYR   D 1 82  ? 3.275   17.665  -8.918  1.00 18.34 ? 96  TYR   D CZ  1 
ATOM   3426 O OH  . TYR   D 1 82  ? 3.231   18.141  -10.216 1.00 21.19 ? 96  TYR   D OH  1 
ATOM   3427 N N   . VAL   D 1 83  ? 3.498   19.526  -4.631  1.00 15.17 ? 97  VAL   D N   1 
ATOM   3428 C CA  . VAL   D 1 83  ? 2.895   20.778  -5.073  1.00 18.97 ? 97  VAL   D CA  1 
ATOM   3429 C C   . VAL   D 1 83  ? 3.353   21.024  -6.504  1.00 20.72 ? 97  VAL   D C   1 
ATOM   3430 O O   . VAL   D 1 83  ? 4.556   21.149  -6.759  1.00 21.01 ? 97  VAL   D O   1 
ATOM   3431 C CB  . VAL   D 1 83  ? 3.299   21.951  -4.161  1.00 21.20 ? 97  VAL   D CB  1 
ATOM   3432 C CG1 . VAL   D 1 83  ? 2.634   23.246  -4.630  1.00 22.54 ? 97  VAL   D CG1 1 
ATOM   3433 C CG2 . VAL   D 1 83  ? 2.955   21.643  -2.700  1.00 22.64 ? 97  VAL   D CG2 1 
ATOM   3434 N N   . GLY   D 1 84  ? 2.405   21.078  -7.436  1.00 23.07 ? 98  GLY   D N   1 
ATOM   3435 C CA  . GLY   D 1 84  ? 2.737   21.176  -8.844  1.00 24.98 ? 98  GLY   D CA  1 
ATOM   3436 C C   . GLY   D 1 84  ? 3.093   22.584  -9.298  1.00 27.79 ? 98  GLY   D C   1 
ATOM   3437 O O   . GLY   D 1 84  ? 3.177   23.533  -8.518  1.00 31.09 ? 98  GLY   D O   1 
ATOM   3438 N N   . GLY   D 1 85  ? 3.314   22.707  -10.601 1.00 28.23 ? 99  GLY   D N   1 
ATOM   3439 C CA  . GLY   D 1 85  ? 3.611   23.974  -11.242 1.00 27.60 ? 99  GLY   D CA  1 
ATOM   3440 C C   . GLY   D 1 85  ? 4.980   23.977  -11.894 1.00 26.18 ? 99  GLY   D C   1 
ATOM   3441 O O   . GLY   D 1 85  ? 5.702   22.979  -11.907 1.00 26.54 ? 99  GLY   D O   1 
ATOM   3442 N N   . ALA   D 1 86  ? 5.326   25.141  -12.452 1.00 24.94 ? 100 ALA   D N   1 
ATOM   3443 C CA  . ALA   D 1 86  ? 6.640   25.316  -13.060 1.00 23.80 ? 100 ALA   D CA  1 
ATOM   3444 C C   . ALA   D 1 86  ? 7.758   25.180  -12.041 1.00 24.46 ? 100 ALA   D C   1 
ATOM   3445 O O   . ALA   D 1 86  ? 8.887   24.842  -12.415 1.00 26.29 ? 100 ALA   D O   1 
ATOM   3446 C CB  . ALA   D 1 86  ? 6.729   26.681  -13.738 1.00 23.99 ? 100 ALA   D CB  1 
ATOM   3447 N N   . GLU   D 1 87  ? 7.467   25.435  -10.764 1.00 24.54 ? 101 GLU   D N   1 
ATOM   3448 C CA  . GLU   D 1 87  ? 8.434   25.286  -9.687  1.00 25.33 ? 101 GLU   D CA  1 
ATOM   3449 C C   . GLU   D 1 87  ? 7.964   24.170  -8.764  1.00 22.26 ? 101 GLU   D C   1 
ATOM   3450 O O   . GLU   D 1 87  ? 7.784   24.383  -7.560  1.00 22.97 ? 101 GLU   D O   1 
ATOM   3451 C CB  . GLU   D 1 87  ? 8.551   26.599  -8.907  1.00 29.17 ? 101 GLU   D CB  1 
ATOM   3452 C CG  . GLU   D 1 87  ? 8.654   27.833  -9.783  1.00 32.84 ? 101 GLU   D CG  1 
ATOM   3453 C CD  . GLU   D 1 87  ? 9.910   27.834  -10.624 1.00 36.13 ? 101 GLU   D CD  1 
ATOM   3454 O OE1 . GLU   D 1 87  ? 10.947  27.343  -10.131 1.00 37.55 ? 101 GLU   D OE1 1 
ATOM   3455 O OE2 . GLU   D 1 87  ? 9.861   28.315  -11.776 1.00 38.06 ? 101 GLU   D OE2 1 
ATOM   3456 N N   . ALA   D 1 88  ? 7.758   22.978  -9.322  1.00 19.44 ? 102 ALA   D N   1 
ATOM   3457 C CA  . ALA   D 1 88  ? 7.171   21.880  -8.566  1.00 18.71 ? 102 ALA   D CA  1 
ATOM   3458 C C   . ALA   D 1 88  ? 8.059   21.488  -7.387  1.00 16.80 ? 102 ALA   D C   1 
ATOM   3459 O O   . ALA   D 1 88  ? 9.284   21.591  -7.443  1.00 16.37 ? 102 ALA   D O   1 
ATOM   3460 C CB  . ALA   D 1 88  ? 6.962   20.670  -9.475  1.00 19.74 ? 102 ALA   D CB  1 
ATOM   3461 N N   . ARG   D 1 89  ? 7.422   21.026  -6.307  1.00 14.91 ? 103 ARG   D N   1 
ATOM   3462 C CA  . ARG   D 1 89  ? 8.120   20.709  -5.070  1.00 14.44 ? 103 ARG   D CA  1 
ATOM   3463 C C   . ARG   D 1 89  ? 7.476   19.493  -4.425  1.00 13.94 ? 103 ARG   D C   1 
ATOM   3464 O O   . ARG   D 1 89  ? 6.271   19.269  -4.553  1.00 16.11 ? 103 ARG   D O   1 
ATOM   3465 C CB  . ARG   D 1 89  ? 7.990   21.842  -4.032  1.00 17.55 ? 103 ARG   D CB  1 
ATOM   3466 C CG  . ARG   D 1 89  ? 8.653   23.149  -4.383  1.00 19.26 ? 103 ARG   D CG  1 
ATOM   3467 C CD  . ARG   D 1 89  ? 10.156  23.036  -4.338  1.00 21.60 ? 103 ARG   D CD  1 
ATOM   3468 N NE  . ARG   D 1 89  ? 10.814  24.323  -4.547  1.00 25.12 ? 103 ARG   D NE  1 
ATOM   3469 C CZ  . ARG   D 1 89  ? 11.047  24.865  -5.736  1.00 27.94 ? 103 ARG   D CZ  1 
ATOM   3470 N NH1 . ARG   D 1 89  ? 10.672  24.265  -6.854  1.00 28.55 ? 103 ARG   D NH1 1 
ATOM   3471 N NH2 . ARG   D 1 89  ? 11.668  26.042  -5.805  1.00 29.70 ? 103 ARG   D NH2 1 
ATOM   3472 N N   . ILE   D 1 90  ? 8.283   18.713  -3.715  1.00 12.61 ? 104 ILE   D N   1 
ATOM   3473 C CA  . ILE   D 1 90  ? 7.763   17.760  -2.740  1.00 12.78 ? 104 ILE   D CA  1 
ATOM   3474 C C   . ILE   D 1 90  ? 8.310   18.174  -1.382  1.00 12.23 ? 104 ILE   D C   1 
ATOM   3475 O O   . ILE   D 1 90  ? 9.530   18.173  -1.170  1.00 13.24 ? 104 ILE   D O   1 
ATOM   3476 C CB  . ILE   D 1 90  ? 8.104   16.298  -3.075  1.00 12.61 ? 104 ILE   D CB  1 
ATOM   3477 C CG1 . ILE   D 1 90  ? 7.560   15.941  -4.468  1.00 13.77 ? 104 ILE   D CG1 1 
ATOM   3478 C CG2 . ILE   D 1 90  ? 7.551   15.370  -1.970  1.00 14.31 ? 104 ILE   D CG2 1 
ATOM   3479 C CD1 . ILE   D 1 90  ? 7.897   14.541  -4.938  1.00 15.37 ? 104 ILE   D CD1 1 
ATOM   3480 N N   . ASN   D 1 91  ? 7.411   18.565  -0.478  1.00 11.64 ? 105 ASN   D N   1 
ATOM   3481 C CA  . ASN   D 1 91  ? 7.782   19.072  0.840   1.00 11.79 ? 105 ASN   D CA  1 
ATOM   3482 C C   . ASN   D 1 91  ? 7.513   17.991  1.877   1.00 10.90 ? 105 ASN   D C   1 
ATOM   3483 O O   . ASN   D 1 91  ? 6.370   17.539  2.005   1.00 11.74 ? 105 ASN   D O   1 
ATOM   3484 C CB  . ASN   D 1 91  ? 6.948   20.315  1.147   1.00 14.09 ? 105 ASN   D CB  1 
ATOM   3485 C CG  . ASN   D 1 91  ? 7.167   21.411  0.123   1.00 16.67 ? 105 ASN   D CG  1 
ATOM   3486 O OD1 . ASN   D 1 91  ? 8.301   21.671  -0.285  1.00 17.84 ? 105 ASN   D OD1 1 
ATOM   3487 N ND2 . ASN   D 1 91  ? 6.083   22.040  -0.316  1.00 18.55 ? 105 ASN   D ND2 1 
ATOM   3488 N N   . THR   D 1 92  ? 8.553   17.587  2.621   1.00 10.92 ? 106 THR   D N   1 
ATOM   3489 C CA  . THR   D 1 92  ? 8.458   16.422  3.498   1.00 10.62 ? 106 THR   D CA  1 
ATOM   3490 C C   . THR   D 1 92  ? 9.026   16.679  4.887   1.00 10.49 ? 106 THR   D C   1 
ATOM   3491 O O   . THR   D 1 92  ? 9.883   17.539  5.099   1.00 10.95 ? 106 THR   D O   1 
ATOM   3492 C CB  . THR   D 1 92  ? 9.214   15.195  2.943   1.00 11.07 ? 106 THR   D CB  1 
ATOM   3493 O OG1 . THR   D 1 92  ? 10.634  15.397  3.064   1.00 11.13 ? 106 THR   D OG1 1 
ATOM   3494 C CG2 . THR   D 1 92  ? 8.832   14.929  1.488   1.00 12.00 ? 106 THR   D CG2 1 
ATOM   3495 N N   . GLN   D 1 93  ? 8.547   15.868  5.823   1.00 9.92  ? 107 GLN   D N   1 
ATOM   3496 C CA  . GLN   D 1 93  ? 9.182   15.644  7.111   1.00 9.74  ? 107 GLN   D CA  1 
ATOM   3497 C C   . GLN   D 1 93  ? 9.498   14.154  7.185   1.00 9.64  ? 107 GLN   D C   1 
ATOM   3498 O O   . GLN   D 1 93  ? 8.793   13.330  6.587   1.00 11.08 ? 107 GLN   D O   1 
ATOM   3499 C CB  . GLN   D 1 93  ? 8.277   16.122  8.254   1.00 11.22 ? 107 GLN   D CB  1 
ATOM   3500 C CG  . GLN   D 1 93  ? 8.004   17.620  8.130   1.00 12.47 ? 107 GLN   D CG  1 
ATOM   3501 C CD  . GLN   D 1 93  ? 7.199   18.197  9.285   1.00 12.53 ? 107 GLN   D CD  1 
ATOM   3502 O OE1 . GLN   D 1 93  ? 5.979   18.344  9.199   1.00 14.95 ? 107 GLN   D OE1 1 
ATOM   3503 N NE2 . GLN   D 1 93  ? 7.874   18.546  10.359  1.00 12.80 ? 107 GLN   D NE2 1 
ATOM   3504 N N   . TRP   D 1 94  ? 10.597  13.798  7.850   1.00 10.12 ? 108 TRP   D N   1 
ATOM   3505 C CA  . TRP   D 1 94  ? 11.041  12.412  7.860   1.00 9.95  ? 108 TRP   D CA  1 
ATOM   3506 C C   . TRP   D 1 94  ? 11.396  11.933  9.266   1.00 9.87  ? 108 TRP   D C   1 
ATOM   3507 O O   . TRP   D 1 94  ? 11.691  12.728  10.171  1.00 10.11 ? 108 TRP   D O   1 
ATOM   3508 C CB  . TRP   D 1 94  ? 12.208  12.162  6.882   1.00 10.71 ? 108 TRP   D CB  1 
ATOM   3509 C CG  . TRP   D 1 94  ? 13.405  13.052  7.030   1.00 10.97 ? 108 TRP   D CG  1 
ATOM   3510 C CD1 . TRP   D 1 94  ? 13.734  14.118  6.232   1.00 12.16 ? 108 TRP   D CD1 1 
ATOM   3511 C CD2 . TRP   D 1 94  ? 14.457  12.943  8.001   1.00 11.46 ? 108 TRP   D CD2 1 
ATOM   3512 N NE1 . TRP   D 1 94  ? 14.914  14.681  6.652   1.00 12.65 ? 108 TRP   D NE1 1 
ATOM   3513 C CE2 . TRP   D 1 94  ? 15.380  13.979  7.734   1.00 12.03 ? 108 TRP   D CE2 1 
ATOM   3514 C CE3 . TRP   D 1 94  ? 14.709  12.071  9.064   1.00 11.40 ? 108 TRP   D CE3 1 
ATOM   3515 C CZ2 . TRP   D 1 94  ? 16.532  14.169  8.494   1.00 13.09 ? 108 TRP   D CZ2 1 
ATOM   3516 C CZ3 . TRP   D 1 94  ? 15.853  12.262  9.821   1.00 12.42 ? 108 TRP   D CZ3 1 
ATOM   3517 C CH2 . TRP   D 1 94  ? 16.748  13.308  9.537   1.00 13.06 ? 108 TRP   D CH2 1 
ATOM   3518 N N   . LEU   D 1 95  ? 11.357  10.602  9.416   1.00 9.80  ? 109 LEU   D N   1 
ATOM   3519 C CA  . LEU   D 1 95  ? 11.746  9.896   10.633  1.00 10.83 ? 109 LEU   D CA  1 
ATOM   3520 C C   . LEU   D 1 95  ? 12.725  8.794   10.253  1.00 11.08 ? 109 LEU   D C   1 
ATOM   3521 O O   . LEU   D 1 95  ? 12.446  8.003   9.347   1.00 13.78 ? 109 LEU   D O   1 
ATOM   3522 C CB  . LEU   D 1 95  ? 10.528  9.247   11.304  1.00 11.06 ? 109 LEU   D CB  1 
ATOM   3523 C CG  . LEU   D 1 95  ? 9.413   10.148  11.824  1.00 11.55 ? 109 LEU   D CG  1 
ATOM   3524 C CD1 . LEU   D 1 95  ? 8.191   9.318   12.206  1.00 13.39 ? 109 LEU   D CD1 1 
ATOM   3525 C CD2 . LEU   D 1 95  ? 9.898   10.963  13.018  1.00 13.60 ? 109 LEU   D CD2 1 
ATOM   3526 N N   . LEU   D 1 96  ? 13.867  8.740   10.932  1.00 11.07 ? 110 LEU   D N   1 
ATOM   3527 C CA  A LEU   D 1 96  ? 14.891  7.725   10.681  0.51 11.46 ? 110 LEU   D CA  1 
ATOM   3528 C CA  B LEU   D 1 96  ? 14.895  7.736   10.683  0.49 11.41 ? 110 LEU   D CA  1 
ATOM   3529 C C   . LEU   D 1 96  ? 15.055  6.913   11.957  1.00 11.43 ? 110 LEU   D C   1 
ATOM   3530 O O   . LEU   D 1 96  ? 15.589  7.411   12.952  1.00 12.06 ? 110 LEU   D O   1 
ATOM   3531 C CB  A LEU   D 1 96  ? 16.221  8.361   10.256  0.51 12.57 ? 110 LEU   D CB  1 
ATOM   3532 C CB  B LEU   D 1 96  ? 16.195  8.444   10.293  0.49 12.18 ? 110 LEU   D CB  1 
ATOM   3533 C CG  A LEU   D 1 96  ? 17.345  7.442   9.739   0.51 13.06 ? 110 LEU   D CG  1 
ATOM   3534 C CG  B LEU   D 1 96  ? 17.536  7.719   10.317  0.49 12.42 ? 110 LEU   D CG  1 
ATOM   3535 C CD1 A LEU   D 1 96  ? 18.375  8.245   8.961   0.51 12.97 ? 110 LEU   D CD1 1 
ATOM   3536 C CD1 B LEU   D 1 96  ? 17.450  6.405   9.582   0.49 12.43 ? 110 LEU   D CD1 1 
ATOM   3537 C CD2 A LEU   D 1 96  ? 18.047  6.668   10.851  0.51 14.55 ? 110 LEU   D CD2 1 
ATOM   3538 C CD2 B LEU   D 1 96  ? 18.618  8.608   9.700   0.49 12.37 ? 110 LEU   D CD2 1 
ATOM   3539 N N   . THR   D 1 97  ? 14.599  5.659   11.931  1.00 12.08 ? 111 THR   D N   1 
ATOM   3540 C CA  . THR   D 1 97  ? 14.687  4.770   13.089  1.00 12.03 ? 111 THR   D CA  1 
ATOM   3541 C C   . THR   D 1 97  ? 15.775  3.730   12.855  1.00 13.24 ? 111 THR   D C   1 
ATOM   3542 O O   . THR   D 1 97  ? 15.792  3.062   11.816  1.00 14.38 ? 111 THR   D O   1 
ATOM   3543 C CB  . THR   D 1 97  ? 13.354  4.057   13.359  1.00 13.03 ? 111 THR   D CB  1 
ATOM   3544 O OG1 . THR   D 1 97  ? 12.302  5.013   13.506  1.00 13.33 ? 111 THR   D OG1 1 
ATOM   3545 C CG2 . THR   D 1 97  ? 13.431  3.225   14.637  1.00 14.60 ? 111 THR   D CG2 1 
ATOM   3546 N N   . SER   D 1 98  ? 16.675  3.594   13.822  1.00 13.68 ? 112 SER   D N   1 
ATOM   3547 C CA  . SER   D 1 98  ? 17.689  2.551   13.818  1.00 15.28 ? 112 SER   D CA  1 
ATOM   3548 C C   . SER   D 1 98  ? 17.242  1.403   14.712  1.00 15.81 ? 112 SER   D C   1 
ATOM   3549 O O   . SER   D 1 98  ? 16.588  1.613   15.734  1.00 16.69 ? 112 SER   D O   1 
ATOM   3550 C CB  . SER   D 1 98  ? 19.016  3.098   14.350  1.00 17.40 ? 112 SER   D CB  1 
ATOM   3551 O OG  . SER   D 1 98  ? 19.502  4.154   13.544  1.00 19.95 ? 112 SER   D OG  1 
ATOM   3552 N N   . GLY   D 1 99  ? 17.612  0.182   14.336  1.00 16.33 ? 113 GLY   D N   1 
ATOM   3553 C CA  . GLY   D 1 99  ? 17.437  -0.934  15.252  1.00 18.03 ? 113 GLY   D CA  1 
ATOM   3554 C C   . GLY   D 1 99  ? 18.346  -0.768  16.456  1.00 19.18 ? 113 GLY   D C   1 
ATOM   3555 O O   . GLY   D 1 99  ? 19.542  -0.487  16.310  1.00 21.09 ? 113 GLY   D O   1 
ATOM   3556 N N   . THR   D 1 100 ? 17.782  -0.922  17.657  1.00 18.21 ? 114 THR   D N   1 
ATOM   3557 C CA  . THR   D 1 100 ? 18.520  -0.739  18.903  1.00 19.21 ? 114 THR   D CA  1 
ATOM   3558 C C   . THR   D 1 100 ? 18.111  -1.823  19.895  1.00 20.18 ? 114 THR   D C   1 
ATOM   3559 O O   . THR   D 1 100 ? 17.113  -2.523  19.713  1.00 21.45 ? 114 THR   D O   1 
ATOM   3560 C CB  . THR   D 1 100 ? 18.235  0.629   19.557  1.00 19.36 ? 114 THR   D CB  1 
ATOM   3561 O OG1 . THR   D 1 100 ? 16.894  0.650   20.056  1.00 19.58 ? 114 THR   D OG1 1 
ATOM   3562 C CG2 . THR   D 1 100 ? 18.432  1.789   18.586  1.00 19.66 ? 114 THR   D CG2 1 
ATOM   3563 N N   . THR   D 1 101 ? 18.890  -1.948  20.968  1.00 21.57 ? 115 THR   D N   1 
ATOM   3564 C CA  . THR   D 1 101 ? 18.417  -2.678  22.136  1.00 22.49 ? 115 THR   D CA  1 
ATOM   3565 C C   . THR   D 1 101 ? 17.347  -1.852  22.843  1.00 23.08 ? 115 THR   D C   1 
ATOM   3566 O O   . THR   D 1 101 ? 17.186  -0.649  22.603  1.00 21.21 ? 115 THR   D O   1 
ATOM   3567 C CB  . THR   D 1 101 ? 19.552  -2.928  23.125  1.00 24.81 ? 115 THR   D CB  1 
ATOM   3568 O OG1 . THR   D 1 101 ? 20.057  -1.667  23.576  1.00 27.05 ? 115 THR   D OG1 1 
ATOM   3569 C CG2 . THR   D 1 101 ? 20.668  -3.736  22.482  1.00 25.42 ? 115 THR   D CG2 1 
ATOM   3570 N N   . GLU   D 1 102 ? 16.614  -2.507  23.745  1.00 25.29 ? 116 GLU   D N   1 
ATOM   3571 C CA  . GLU   D 1 102 ? 15.572  -1.794  24.473  1.00 25.24 ? 116 GLU   D CA  1 
ATOM   3572 C C   . GLU   D 1 102 ? 16.158  -0.670  25.319  1.00 23.94 ? 116 GLU   D C   1 
ATOM   3573 O O   . GLU   D 1 102 ? 15.563  0.408   25.419  1.00 23.73 ? 116 GLU   D O   1 
ATOM   3574 C CB  . GLU   D 1 102 ? 14.741  -2.765  25.315  1.00 27.14 ? 116 GLU   D CB  1 
ATOM   3575 C CG  . GLU   D 1 102 ? 13.788  -3.613  24.483  1.00 28.43 ? 116 GLU   D CG  1 
ATOM   3576 C CD  . GLU   D 1 102 ? 12.838  -2.768  23.653  0.47 28.31 ? 116 GLU   D CD  1 
ATOM   3577 O OE1 . GLU   D 1 102 ? 11.885  -2.197  24.224  0.46 28.41 ? 116 GLU   D OE1 1 
ATOM   3578 O OE2 . GLU   D 1 102 ? 13.053  -2.659  22.428  0.47 28.04 ? 116 GLU   D OE2 1 
ATOM   3579 N N   . ALA   D 1 103 ? 17.341  -0.888  25.908  1.00 24.32 ? 117 ALA   D N   1 
ATOM   3580 C CA  . ALA   D 1 103 ? 17.966  0.146   26.729  1.00 23.99 ? 117 ALA   D CA  1 
ATOM   3581 C C   . ALA   D 1 103 ? 18.346  1.382   25.920  1.00 23.41 ? 117 ALA   D C   1 
ATOM   3582 O O   . ALA   D 1 103 ? 18.440  2.483   26.479  1.00 24.96 ? 117 ALA   D O   1 
ATOM   3583 C CB  . ALA   D 1 103 ? 19.184  -0.419  27.463  1.00 25.39 ? 117 ALA   D CB  1 
ATOM   3584 N N   . ASN   D 1 104 ? 18.557  1.232   24.613  1.00 22.19 ? 118 ASN   D N   1 
ATOM   3585 C CA  . ASN   D 1 104 ? 18.933  2.352   23.761  1.00 21.62 ? 118 ASN   D CA  1 
ATOM   3586 C C   . ASN   D 1 104 ? 17.780  2.846   22.895  1.00 18.60 ? 118 ASN   D C   1 
ATOM   3587 O O   . ASN   D 1 104 ? 17.982  3.713   22.034  1.00 18.66 ? 118 ASN   D O   1 
ATOM   3588 C CB  . ASN   D 1 104 ? 20.124  1.971   22.887  1.00 24.12 ? 118 ASN   D CB  1 
ATOM   3589 C CG  . ASN   D 1 104 ? 21.377  1.772   23.698  1.00 26.21 ? 118 ASN   D CG  1 
ATOM   3590 O OD1 . ASN   D 1 104 ? 21.694  2.582   24.566  1.00 28.21 ? 118 ASN   D OD1 1 
ATOM   3591 N ND2 . ASN   D 1 104 ? 22.081  0.676   23.448  1.00 27.52 ? 118 ASN   D ND2 1 
ATOM   3592 N N   . ALA   D 1 105 ? 16.570  2.327   23.108  1.00 17.92 ? 119 ALA   D N   1 
ATOM   3593 C CA  . ALA   D 1 105 ? 15.471  2.645   22.202  1.00 17.13 ? 119 ALA   D CA  1 
ATOM   3594 C C   . ALA   D 1 105 ? 15.039  4.100   22.314  1.00 17.26 ? 119 ALA   D C   1 
ATOM   3595 O O   . ALA   D 1 105 ? 14.500  4.654   21.348  1.00 16.64 ? 119 ALA   D O   1 
ATOM   3596 C CB  . ALA   D 1 105 ? 14.289  1.701   22.426  1.00 18.27 ? 119 ALA   D CB  1 
ATOM   3597 N N   . TRP   D 1 106 ? 15.273  4.733   23.468  1.00 19.12 ? 120 TRP   D N   1 
ATOM   3598 C CA  . TRP   D 1 106 ? 14.877  6.126   23.643  1.00 20.64 ? 120 TRP   D CA  1 
ATOM   3599 C C   . TRP   D 1 106 ? 15.532  7.035   22.610  1.00 20.87 ? 120 TRP   D C   1 
ATOM   3600 O O   . TRP   D 1 106 ? 14.960  8.070   22.254  1.00 22.18 ? 120 TRP   D O   1 
ATOM   3601 C CB  . TRP   D 1 106 ? 15.197  6.595   25.068  1.00 22.09 ? 120 TRP   D CB  1 
ATOM   3602 C CG  . TRP   D 1 106 ? 16.662  6.723   25.344  1.00 23.96 ? 120 TRP   D CG  1 
ATOM   3603 C CD1 . TRP   D 1 106 ? 17.498  5.744   25.792  1.00 24.40 ? 120 TRP   D CD1 1 
ATOM   3604 C CD2 . TRP   D 1 106 ? 17.471  7.897   25.181  1.00 26.16 ? 120 TRP   D CD2 1 
ATOM   3605 N NE1 . TRP   D 1 106 ? 18.777  6.231   25.919  1.00 25.49 ? 120 TRP   D NE1 1 
ATOM   3606 C CE2 . TRP   D 1 106 ? 18.787  7.551   25.553  1.00 27.59 ? 120 TRP   D CE2 1 
ATOM   3607 C CE3 . TRP   D 1 106 ? 17.211  9.206   24.759  1.00 29.24 ? 120 TRP   D CE3 1 
ATOM   3608 C CZ2 . TRP   D 1 106 ? 19.839  8.465   25.517  1.00 29.01 ? 120 TRP   D CZ2 1 
ATOM   3609 C CZ3 . TRP   D 1 106 ? 18.260  10.114  24.723  1.00 30.46 ? 120 TRP   D CZ3 1 
ATOM   3610 C CH2 . TRP   D 1 106 ? 19.557  9.738   25.104  1.00 30.55 ? 120 TRP   D CH2 1 
ATOM   3611 N N   . LYS   D 1 107 ? 16.725  6.680   22.124  1.00 20.35 ? 121 LYS   D N   1 
ATOM   3612 C CA  A LYS   D 1 107 ? 17.455  7.469   21.137  0.91 21.10 ? 121 LYS   D CA  1 
ATOM   3613 C CA  B LYS   D 1 107 ? 17.415  7.490   21.124  0.09 19.47 ? 121 LYS   D CA  1 
ATOM   3614 C C   . LYS   D 1 107 ? 17.508  6.787   19.767  1.00 18.32 ? 121 LYS   D C   1 
ATOM   3615 O O   . LYS   D 1 107 ? 18.453  6.995   19.001  1.00 19.42 ? 121 LYS   D O   1 
ATOM   3616 C CB  A LYS   D 1 107 ? 18.856  7.805   21.649  0.91 24.12 ? 121 LYS   D CB  1 
ATOM   3617 C CB  B LYS   D 1 107 ? 18.765  8.007   21.631  0.09 19.70 ? 121 LYS   D CB  1 
ATOM   3618 C CG  A LYS   D 1 107 ? 19.692  6.593   22.048  0.91 25.98 ? 121 LYS   D CG  1 
ATOM   3619 C CG  B LYS   D 1 107 ? 19.938  7.039   21.561  0.09 19.64 ? 121 LYS   D CG  1 
ATOM   3620 C CD  A LYS   D 1 107 ? 21.060  7.043   22.546  0.91 27.75 ? 121 LYS   D CD  1 
ATOM   3621 C CD  B LYS   D 1 107 ? 21.114  7.725   20.878  0.09 19.44 ? 121 LYS   D CD  1 
ATOM   3622 C CE  A LYS   D 1 107 ? 21.929  5.863   22.948  0.91 28.98 ? 121 LYS   D CE  1 
ATOM   3623 C CE  B LYS   D 1 107 ? 22.216  6.750   20.510  0.09 19.08 ? 121 LYS   D CE  1 
ATOM   3624 N NZ  A LYS   D 1 107 ? 23.217  6.316   23.547  0.91 31.48 ? 121 LYS   D NZ  1 
ATOM   3625 N NZ  B LYS   D 1 107 ? 23.265  7.412   19.686  0.09 18.82 ? 121 LYS   D NZ  1 
ATOM   3626 N N   . SER   D 1 108 ? 16.496  5.980   19.440  1.00 15.62 ? 122 SER   D N   1 
ATOM   3627 C CA  . SER   D 1 108 ? 16.451  5.256   18.177  1.00 13.60 ? 122 SER   D CA  1 
ATOM   3628 C C   . SER   D 1 108 ? 16.020  6.099   16.977  1.00 12.11 ? 122 SER   D C   1 
ATOM   3629 O O   . SER   D 1 108 ? 16.247  5.655   15.846  1.00 13.17 ? 122 SER   D O   1 
ATOM   3630 C CB  . SER   D 1 108 ? 15.469  4.089   18.296  1.00 13.90 ? 122 SER   D CB  1 
ATOM   3631 O OG  . SER   D 1 108 ? 14.150  4.583   18.482  1.00 15.97 ? 122 SER   D OG  1 
ATOM   3632 N N   . THR   D 1 109 ? 15.382  7.262   17.168  1.00 11.40 ? 123 THR   D N   1 
ATOM   3633 C CA  . THR   D 1 109 ? 14.657  7.918   16.074  1.00 11.42 ? 123 THR   D CA  1 
ATOM   3634 C C   . THR   D 1 109 ? 15.064  9.377   15.903  1.00 10.46 ? 123 THR   D C   1 
ATOM   3635 O O   . THR   D 1 109 ? 14.859  10.196  16.808  1.00 11.67 ? 123 THR   D O   1 
ATOM   3636 C CB  . THR   D 1 109 ? 13.145  7.834   16.293  1.00 11.73 ? 123 THR   D CB  1 
ATOM   3637 O OG1 . THR   D 1 109 ? 12.776  6.489   16.607  1.00 13.61 ? 123 THR   D OG1 1 
ATOM   3638 C CG2 . THR   D 1 109 ? 12.391  8.294   15.033  1.00 11.69 ? 123 THR   D CG2 1 
ATOM   3639 N N   . LEU   D 1 110 ? 15.585  9.708   14.718  1.00 10.54 ? 124 LEU   D N   1 
ATOM   3640 C CA  . LEU   D 1 110 ? 15.858  11.081  14.315  1.00 10.79 ? 124 LEU   D CA  1 
ATOM   3641 C C   . LEU   D 1 110 ? 14.684  11.639  13.512  1.00 10.64 ? 124 LEU   D C   1 
ATOM   3642 O O   . LEU   D 1 110 ? 13.975  10.894  12.829  1.00 11.44 ? 124 LEU   D O   1 
ATOM   3643 C CB  . LEU   D 1 110 ? 17.106  11.113  13.426  1.00 11.81 ? 124 LEU   D CB  1 
ATOM   3644 C CG  . LEU   D 1 110 ? 18.433  10.707  14.079  1.00 13.21 ? 124 LEU   D CG  1 
ATOM   3645 C CD1 . LEU   D 1 110 ? 19.507  10.411  13.038  1.00 14.09 ? 124 LEU   D CD1 1 
ATOM   3646 C CD2 . LEU   D 1 110 ? 18.908  11.810  14.996  1.00 14.19 ? 124 LEU   D CD2 1 
ATOM   3647 N N   . VAL   D 1 111 ? 14.497  12.959  13.582  1.00 11.14 ? 125 VAL   D N   1 
ATOM   3648 C CA  . VAL   D 1 111 ? 13.465  13.659  12.817  1.00 10.51 ? 125 VAL   D CA  1 
ATOM   3649 C C   . VAL   D 1 111 ? 14.097  14.819  12.053  1.00 10.88 ? 125 VAL   D C   1 
ATOM   3650 O O   . VAL   D 1 111 ? 15.029  15.468  12.540  1.00 11.55 ? 125 VAL   D O   1 
ATOM   3651 C CB  . VAL   D 1 111 ? 12.314  14.146  13.734  1.00 11.70 ? 125 VAL   D CB  1 
ATOM   3652 C CG1 . VAL   D 1 111 ? 12.824  15.127  14.788  1.00 12.57 ? 125 VAL   D CG1 1 
ATOM   3653 C CG2 . VAL   D 1 111 ? 11.174  14.760  12.921  1.00 11.94 ? 125 VAL   D CG2 1 
ATOM   3654 N N   . GLY   D 1 112 ? 13.591  15.076  10.847  1.00 10.42 ? 126 GLY   D N   1 
ATOM   3655 C CA  . GLY   D 1 112 ? 14.057  16.196  10.060  1.00 11.25 ? 126 GLY   D CA  1 
ATOM   3656 C C   . GLY   D 1 112 ? 13.084  16.523  8.945   1.00 10.63 ? 126 GLY   D C   1 
ATOM   3657 O O   . GLY   D 1 112 ? 11.939  16.067  8.939   1.00 11.17 ? 126 GLY   D O   1 
ATOM   3658 N N   . HIS   D 1 113 ? 13.554  17.333  7.997   1.00 11.25 ? 127 HIS   D N   1 
ATOM   3659 C CA  . HIS   D 1 113 ? 12.710  17.779  6.895   1.00 11.55 ? 127 HIS   D CA  1 
ATOM   3660 C C   . HIS   D 1 113 ? 13.550  17.939  5.635   1.00 12.36 ? 127 HIS   D C   1 
ATOM   3661 O O   . HIS   D 1 113 ? 14.679  18.428  5.695   1.00 14.39 ? 127 HIS   D O   1 
ATOM   3662 C CB  . HIS   D 1 113 ? 12.004  19.095  7.248   1.00 14.00 ? 127 HIS   D CB  1 
ATOM   3663 C CG  . HIS   D 1 113 ? 12.922  20.135  7.818   1.00 16.28 ? 127 HIS   D CG  1 
ATOM   3664 N ND1 . HIS   D 1 113 ? 13.222  20.214  9.163   1.00 18.28 ? 127 HIS   D ND1 1 
ATOM   3665 C CD2 . HIS   D 1 113 ? 13.613  21.133  7.221   1.00 18.89 ? 127 HIS   D CD2 1 
ATOM   3666 C CE1 . HIS   D 1 113 ? 14.057  21.219  9.367   1.00 20.04 ? 127 HIS   D CE1 1 
ATOM   3667 N NE2 . HIS   D 1 113 ? 14.310  21.792  8.206   1.00 21.03 ? 127 HIS   D NE2 1 
ATOM   3668 N N   . ASP   D 1 114 ? 12.977  17.545  4.492   1.00 11.84 ? 128 ASP   D N   1 
ATOM   3669 C CA  . ASP   D 1 114 ? 13.616  17.648  3.182   1.00 11.40 ? 128 ASP   D CA  1 
ATOM   3670 C C   . ASP   D 1 114 ? 12.649  18.277  2.193   1.00 11.94 ? 128 ASP   D C   1 
ATOM   3671 O O   . ASP   D 1 114 ? 11.459  17.954  2.190   1.00 11.89 ? 128 ASP   D O   1 
ATOM   3672 C CB  . ASP   D 1 114 ? 13.931  16.258  2.588   1.00 12.55 ? 128 ASP   D CB  1 
ATOM   3673 C CG  . ASP   D 1 114 ? 15.083  15.554  3.257   1.00 14.72 ? 128 ASP   D CG  1 
ATOM   3674 O OD1 . ASP   D 1 114 ? 15.802  16.151  4.085   1.00 15.63 ? 128 ASP   D OD1 1 
ATOM   3675 O OD2 . ASP   D 1 114 ? 15.249  14.366  2.953   1.00 14.77 ? 128 ASP   D OD2 1 
ATOM   3676 N N   . THR   D 1 115 ? 13.169  19.142  1.325   1.00 13.05 ? 129 THR   D N   1 
ATOM   3677 C CA  A THR   D 1 115 ? 12.418  19.686  0.198   0.78 13.89 ? 129 THR   D CA  1 
ATOM   3678 C CA  B THR   D 1 115 ? 12.405  19.663  0.197   0.22 13.57 ? 129 THR   D CA  1 
ATOM   3679 C C   . THR   D 1 115 ? 13.056  19.203  -1.096  1.00 13.34 ? 129 THR   D C   1 
ATOM   3680 O O   . THR   D 1 115 ? 14.274  19.319  -1.264  1.00 13.31 ? 129 THR   D O   1 
ATOM   3681 C CB  A THR   D 1 115 ? 12.441  21.215  0.217   0.78 18.15 ? 129 THR   D CB  1 
ATOM   3682 C CB  B THR   D 1 115 ? 12.286  21.192  0.219   0.22 15.03 ? 129 THR   D CB  1 
ATOM   3683 O OG1 A THR   D 1 115 ? 12.068  21.691  1.515   0.78 21.82 ? 129 THR   D OG1 1 
ATOM   3684 O OG1 B THR   D 1 115 ? 13.578  21.781  0.407   0.22 15.45 ? 129 THR   D OG1 1 
ATOM   3685 C CG2 A THR   D 1 115 ? 11.479  21.762  -0.826  0.78 18.03 ? 129 THR   D CG2 1 
ATOM   3686 C CG2 B THR   D 1 115 ? 11.341  21.644  1.322   0.22 15.87 ? 129 THR   D CG2 1 
ATOM   3687 N N   . PHE   D 1 116 ? 12.240  18.678  -2.006  1.00 12.23 ? 130 PHE   D N   1 
ATOM   3688 C CA  . PHE   D 1 116 ? 12.711  18.140  -3.276  1.00 12.37 ? 130 PHE   D CA  1 
ATOM   3689 C C   . PHE   D 1 116 ? 12.242  19.001  -4.441  1.00 12.58 ? 130 PHE   D C   1 
ATOM   3690 O O   . PHE   D 1 116 ? 11.111  19.504  -4.442  1.00 13.10 ? 130 PHE   D O   1 
ATOM   3691 C CB  . PHE   D 1 116 ? 12.177  16.719  -3.488  1.00 12.87 ? 130 PHE   D CB  1 
ATOM   3692 C CG  . PHE   D 1 116 ? 12.670  15.715  -2.475  1.00 12.64 ? 130 PHE   D CG  1 
ATOM   3693 C CD1 . PHE   D 1 116 ? 12.002  15.538  -1.264  1.00 13.04 ? 130 PHE   D CD1 1 
ATOM   3694 C CD2 . PHE   D 1 116 ? 13.772  14.926  -2.740  1.00 14.05 ? 130 PHE   D CD2 1 
ATOM   3695 C CE1 . PHE   D 1 116 ? 12.446  14.603  -0.324  1.00 12.86 ? 130 PHE   D CE1 1 
ATOM   3696 C CE2 . PHE   D 1 116 ? 14.215  13.991  -1.821  1.00 14.25 ? 130 PHE   D CE2 1 
ATOM   3697 C CZ  . PHE   D 1 116 ? 13.557  13.833  -0.598  1.00 13.32 ? 130 PHE   D CZ  1 
ATOM   3698 N N   . THR   D 1 117 ? 13.126  19.155  -5.431  1.00 12.27 ? 131 THR   D N   1 
ATOM   3699 C CA  A THR   D 1 117 ? 12.828  19.876  -6.661  0.94 14.14 ? 131 THR   D CA  1 
ATOM   3700 C CA  B THR   D 1 117 ? 12.851  19.885  -6.659  0.06 12.79 ? 131 THR   D CA  1 
ATOM   3701 C C   . THR   D 1 117 ? 13.245  19.017  -7.849  1.00 12.82 ? 131 THR   D C   1 
ATOM   3702 O O   . THR   D 1 117 ? 13.987  18.042  -7.707  1.00 12.34 ? 131 THR   D O   1 
ATOM   3703 C CB  A THR   D 1 117 ? 13.543  21.242  -6.698  0.94 19.69 ? 131 THR   D CB  1 
ATOM   3704 C CB  B THR   D 1 117 ? 13.667  21.181  -6.687  0.06 12.95 ? 131 THR   D CB  1 
ATOM   3705 O OG1 A THR   D 1 117 ? 14.963  21.051  -6.718  0.94 23.76 ? 131 THR   D OG1 1 
ATOM   3706 O OG1 B THR   D 1 117 ? 13.793  21.697  -5.355  0.06 12.98 ? 131 THR   D OG1 1 
ATOM   3707 C CG2 A THR   D 1 117 ? 13.188  22.082  -5.487  0.94 22.43 ? 131 THR   D CG2 1 
ATOM   3708 C CG2 B THR   D 1 117 ? 12.986  22.208  -7.544  0.06 13.26 ? 131 THR   D CG2 1 
ATOM   3709 N N   . LYS   D 1 118 ? 12.752  19.382  -9.044  1.00 14.37 ? 132 LYS   D N   1 
ATOM   3710 C CA  . LYS   D 1 118 ? 13.110  18.650  -10.260 1.00 14.79 ? 132 LYS   D CA  1 
ATOM   3711 C C   . LYS   D 1 118 ? 14.453  19.072  -10.849 1.00 15.33 ? 132 LYS   D C   1 
ATOM   3712 O O   . LYS   D 1 118 ? 14.896  18.457  -11.825 1.00 14.57 ? 132 LYS   D O   1 
ATOM   3713 C CB  . LYS   D 1 118 ? 11.999  18.760  -11.312 1.00 17.30 ? 132 LYS   D CB  1 
ATOM   3714 C CG  . LYS   D 1 118 ? 10.732  18.014  -10.931 1.00 18.05 ? 132 LYS   D CG  1 
ATOM   3715 C CD  . LYS   D 1 118 ? 9.735   17.999  -12.071 1.00 22.06 ? 132 LYS   D CD  1 
ATOM   3716 C CE  . LYS   D 1 118 ? 8.417   17.426  -11.607 1.00 24.47 ? 132 LYS   D CE  1 
ATOM   3717 N NZ  . LYS   D 1 118 ? 7.534   17.038  -12.741 1.00 27.06 ? 132 LYS   D NZ  1 
ATOM   3718 N N   . VAL   D 1 119 ? 15.098  20.091  -10.286 1.00 18.21 ? 133 VAL   D N   1 
ATOM   3719 C CA  . VAL   D 1 119 ? 16.358  20.644  -10.773 1.00 23.15 ? 133 VAL   D CA  1 
ATOM   3720 C C   . VAL   D 1 119 ? 17.425  20.406  -9.712  1.00 27.21 ? 133 VAL   D C   1 
ATOM   3721 O O   . VAL   D 1 119 ? 17.161  20.572  -8.518  1.00 28.39 ? 133 VAL   D O   1 
ATOM   3722 C CB  . VAL   D 1 119 ? 16.196  22.160  -11.014 1.00 24.90 ? 133 VAL   D CB  1 
ATOM   3723 C CG1 . VAL   D 1 119 ? 17.448  22.747  -11.638 1.00 26.06 ? 133 VAL   D CG1 1 
ATOM   3724 C CG2 . VAL   D 1 119 ? 14.964  22.450  -11.863 1.00 26.38 ? 133 VAL   D CG2 1 
ATOM   3725 N N   . LYS   D 1 120 ? 18.632  20.037  -10.140 1.00 33.23 ? 134 LYS   D N   1 
ATOM   3726 C CA  . LYS   D 1 120 ? 19.732  19.808  -9.194  1.00 36.28 ? 134 LYS   D CA  1 
ATOM   3727 C C   . LYS   D 1 120 ? 20.015  20.997  -8.270  1.00 35.60 ? 134 LYS   D C   1 
ATOM   3728 O O   . LYS   D 1 120 ? 19.858  22.159  -8.653  1.00 35.64 ? 134 LYS   D O   1 
ATOM   3729 C CB  . LYS   D 1 120 ? 21.015  19.406  -9.923  1.00 37.89 ? 134 LYS   D CB  1 
ATOM   3730 C CG  . LYS   D 1 120 ? 21.043  17.956  -10.378 1.00 39.27 ? 134 LYS   D CG  1 
ATOM   3731 C CD  . LYS   D 1 120 ? 22.425  17.558  -10.855 1.00 40.52 ? 134 LYS   D CD  1 
ATOM   3732 C CE  . LYS   D 1 120 ? 22.520  16.062  -11.096 1.00 41.36 ? 134 LYS   D CE  1 
ATOM   3733 N NZ  . LYS   D 1 120 ? 23.898  15.661  -11.494 1.00 41.78 ? 134 LYS   D NZ  1 
HETATM 3734 S S   . DMS   E 2 .   ? -6.428  9.377   8.724   0.85 18.96 ? 301 DMS   A S   1 
HETATM 3735 O O   . DMS   E 2 .   ? -7.024  10.485  9.522   0.85 21.45 ? 301 DMS   A O   1 
HETATM 3736 C C1  . DMS   E 2 .   ? -7.773  8.682   7.733   0.85 19.64 ? 301 DMS   A C1  1 
HETATM 3737 C C2  . DMS   E 2 .   ? -6.086  8.013   9.858   0.85 18.27 ? 301 DMS   A C2  1 
HETATM 3738 S S   . DMS   F 2 .   ? -2.112  7.834   12.144  0.87 13.23 ? 302 DMS   A S   1 
HETATM 3739 O O   . DMS   F 2 .   ? -2.731  7.342   10.868  0.87 12.09 ? 302 DMS   A O   1 
HETATM 3740 C C1  . DMS   F 2 .   ? -1.353  6.423   12.969  0.87 11.63 ? 302 DMS   A C1  1 
HETATM 3741 C C2  . DMS   F 2 .   ? -3.463  8.167   13.301  0.87 15.01 ? 302 DMS   A C2  1 
HETATM 3742 C C1  . A1LXQ G 3 .   ? 21.823  13.660  28.320  0.74 29.43 ? 201 A1LXQ B C1  1 
HETATM 3743 C C10 . A1LXQ G 3 .   ? 15.814  13.032  27.080  0.74 17.06 ? 201 A1LXQ B C10 1 
HETATM 3744 C C11 . A1LXQ G 3 .   ? 14.514  12.261  28.916  0.74 21.47 ? 201 A1LXQ B C11 1 
HETATM 3745 C C12 . A1LXQ G 3 .   ? 13.400  12.867  26.782  0.74 11.45 ? 201 A1LXQ B C12 1 
HETATM 3746 C C13 . A1LXQ G 3 .   ? 14.784  13.081  26.086  0.74 5.21  ? 201 A1LXQ B C13 1 
HETATM 3747 C C14 . A1LXQ G 3 .   ? 22.072  13.662  25.973  0.74 31.15 ? 201 A1LXQ B C14 1 
HETATM 3748 C C15 . A1LXQ G 3 .   ? 22.718  14.781  24.173  0.74 28.68 ? 201 A1LXQ B C15 1 
HETATM 3749 C C16 . A1LXQ G 3 .   ? 21.745  13.665  30.692  0.74 31.84 ? 201 A1LXQ B C16 1 
HETATM 3750 C C17 . A1LXQ G 3 .   ? 23.802  12.659  30.925  0.74 33.90 ? 201 A1LXQ B C17 1 
HETATM 3751 C C2  . A1LXQ G 3 .   ? 21.069  13.571  29.476  0.74 29.34 ? 201 A1LXQ B C2  1 
HETATM 3752 C C3  . A1LXQ G 3 .   ? 19.689  13.389  29.386  0.74 27.13 ? 201 A1LXQ B C3  1 
HETATM 3753 C C4  . A1LXQ G 3 .   ? 19.078  13.309  28.134  0.74 25.95 ? 201 A1LXQ B C4  1 
HETATM 3754 C C5  . A1LXQ G 3 .   ? 19.855  13.398  26.978  0.74 27.12 ? 201 A1LXQ B C5  1 
HETATM 3755 C C6  . A1LXQ G 3 .   ? 21.232  13.575  27.076  0.74 29.46 ? 201 A1LXQ B C6  1 
HETATM 3756 C C7  . A1LXQ G 3 .   ? 17.760  13.123  28.009  0.74 23.66 ? 201 A1LXQ B C7  1 
HETATM 3757 C C8  . A1LXQ G 3 .   ? 16.905  12.699  28.941  0.74 22.89 ? 201 A1LXQ B C8  1 
HETATM 3758 C C9  . A1LXQ G 3 .   ? 15.687  12.636  28.377  0.74 20.92 ? 201 A1LXQ B C9  1 
HETATM 3759 N N1  . A1LXQ G 3 .   ? 13.366  12.310  28.147  0.74 17.70 ? 201 A1LXQ B N1  1 
HETATM 3760 O O1  . A1LXQ G 3 .   ? 17.123  13.299  26.894  0.74 21.25 ? 201 A1LXQ B O1  1 
HETATM 3761 O O2  . A1LXQ G 3 .   ? 14.416  11.817  30.067  0.74 24.28 ? 201 A1LXQ B O2  1 
HETATM 3762 O O3  . A1LXQ G 3 .   ? 23.204  13.176  26.020  0.74 32.43 ? 201 A1LXQ B O3  1 
HETATM 3763 O O4  . A1LXQ G 3 .   ? 21.579  14.304  24.887  0.74 30.54 ? 201 A1LXQ B O4  1 
HETATM 3764 O O5  . A1LXQ G 3 .   ? 21.163  13.557  31.770  0.74 32.79 ? 201 A1LXQ B O5  1 
HETATM 3765 O O6  . A1LXQ G 3 .   ? 23.089  13.852  30.571  0.74 33.40 ? 201 A1LXQ B O6  1 
HETATM 3766 S S   . DMS   H 2 .   ? -1.396  27.968  17.733  0.83 26.50 ? 301 DMS   C S   1 
HETATM 3767 O O   . DMS   H 2 .   ? -2.174  27.335  16.621  0.83 28.49 ? 301 DMS   C O   1 
HETATM 3768 C C1  . DMS   H 2 .   ? -2.416  29.272  18.471  0.83 26.45 ? 301 DMS   C C1  1 
HETATM 3769 C C2  . DMS   H 2 .   ? -0.093  28.988  16.992  0.83 24.00 ? 301 DMS   C C2  1 
HETATM 3770 S S   . DMS   I 2 .   ? 3.636   26.452  15.859  0.90 16.25 ? 302 DMS   C S   1 
HETATM 3771 O O   . DMS   I 2 .   ? 3.116   27.313  16.976  0.90 16.43 ? 302 DMS   C O   1 
HETATM 3772 C C1  . DMS   I 2 .   ? 5.255   27.082  15.357  0.90 14.97 ? 302 DMS   C C1  1 
HETATM 3773 C C2  . DMS   I 2 .   ? 2.774   26.922  14.346  0.90 17.35 ? 302 DMS   C C2  1 
HETATM 3774 C C1  . A1LXQ J 3 .   ? 23.037  6.134   4.181   0.80 18.31 ? 201 A1LXQ D C1  1 
HETATM 3775 C C10 . A1LXQ J 3 .   ? 18.869  10.883  3.544   0.80 14.81 ? 201 A1LXQ D C10 1 
HETATM 3776 C C11 . A1LXQ J 3 .   ? 17.605  11.020  5.532   0.80 16.99 ? 201 A1LXQ D C11 1 
HETATM 3777 C C12 . A1LXQ J 3 .   ? 17.312  12.742  3.830   0.80 15.06 ? 201 A1LXQ D C12 1 
HETATM 3778 C C13 . A1LXQ J 3 .   ? 18.151  11.893  2.894   0.80 16.43 ? 201 A1LXQ D C13 1 
HETATM 3779 C C14 . A1LXQ J 3 .   ? 22.249  5.557   6.390   0.80 17.85 ? 201 A1LXQ D C14 1 
HETATM 3780 C C15 . A1LXQ J 3 .   ? 21.747  5.228   8.625   0.80 19.35 ? 201 A1LXQ D C15 1 
HETATM 3781 C C16 . A1LXQ J 3 .   ? 23.850  6.693   1.983   0.80 19.89 ? 201 A1LXQ D C16 1 
HETATM 3782 C C17 . A1LXQ J 3 .   ? 24.428  7.324   -0.098  0.80 25.30 ? 201 A1LXQ D C17 1 
HETATM 3783 C C2  . A1LXQ J 3 .   ? 22.976  6.942   3.048   0.80 17.75 ? 201 A1LXQ D C2  1 
HETATM 3784 C C3  . A1LXQ J 3 .   ? 22.053  8.005   3.001   0.80 17.09 ? 201 A1LXQ D C3  1 
HETATM 3785 C C4  . A1LXQ J 3 .   ? 21.197  8.263   4.084   0.80 15.09 ? 201 A1LXQ D C4  1 
HETATM 3786 C C5  . A1LXQ J 3 .   ? 21.274  7.424   5.202   0.80 15.23 ? 201 A1LXQ D C5  1 
HETATM 3787 C C6  . A1LXQ J 3 .   ? 22.189  6.371   5.257   0.80 16.51 ? 201 A1LXQ D C6  1 
HETATM 3788 C C7  . A1LXQ J 3 .   ? 20.264  9.240   4.088   0.80 15.26 ? 201 A1LXQ D C7  1 
HETATM 3789 C C8  . A1LXQ J 3 .   ? 19.436  9.479   5.107   0.80 12.90 ? 201 A1LXQ D C8  1 
HETATM 3790 C C9  . A1LXQ J 3 .   ? 18.595  10.476  4.803   0.80 15.56 ? 201 A1LXQ D C9  1 
HETATM 3791 N N1  . A1LXQ J 3 .   ? 16.891  12.106  5.084   0.80 16.96 ? 201 A1LXQ D N1  1 
HETATM 3792 O O1  . A1LXQ J 3 .   ? 19.942  10.092  3.061   0.80 18.42 ? 201 A1LXQ D O1  1 
HETATM 3793 O O2  . A1LXQ J 3 .   ? 17.235  10.547  6.601   0.80 19.16 ? 201 A1LXQ D O2  1 
HETATM 3794 O O3  . A1LXQ J 3 .   ? 22.918  4.526   6.406   0.80 18.54 ? 201 A1LXQ D O3  1 
HETATM 3795 O O4  . A1LXQ J 3 .   ? 21.497  5.983   7.441   0.80 18.46 ? 201 A1LXQ D O4  1 
HETATM 3796 O O5  . A1LXQ J 3 .   ? 24.419  5.608   1.823   0.80 18.18 ? 201 A1LXQ D O5  1 
HETATM 3797 O O6  . A1LXQ J 3 .   ? 24.059  7.764   1.186   0.80 22.72 ? 201 A1LXQ D O6  1 
HETATM 3798 O O   . HOH   K 4 .   ? 3.364   25.318  -1.932  1.00 35.05 ? 401 HOH   A O   1 
HETATM 3799 O O   . HOH   K 4 .   ? -8.435  -9.482  13.359  1.00 36.05 ? 402 HOH   A O   1 
HETATM 3800 O O   . HOH   K 4 .   ? 6.296   -6.735  24.633  1.00 34.50 ? 403 HOH   A O   1 
HETATM 3801 O O   . HOH   K 4 .   ? -5.766  -11.904 14.659  1.00 41.01 ? 404 HOH   A O   1 
HETATM 3802 O O   . HOH   K 4 .   ? -14.584 -3.888  3.264   1.00 35.81 ? 405 HOH   A O   1 
HETATM 3803 O O   . HOH   K 4 .   ? 11.559  3.971   9.269   1.00 24.50 ? 406 HOH   A O   1 
HETATM 3804 O O   . HOH   K 4 .   ? 6.222   10.314  19.912  1.00 26.79 ? 407 HOH   A O   1 
HETATM 3805 O O   . HOH   K 4 .   ? -13.611 12.486  3.090   1.00 42.13 ? 408 HOH   A O   1 
HETATM 3806 O O   . HOH   K 4 .   ? -12.586 -2.786  -3.076  1.00 54.73 ? 409 HOH   A O   1 
HETATM 3807 O O   . HOH   K 4 .   ? 9.072   -6.673  -3.909  1.00 36.54 ? 410 HOH   A O   1 
HETATM 3808 O O   . HOH   K 4 .   ? 16.544  -8.935  1.075   1.00 33.74 ? 411 HOH   A O   1 
HETATM 3809 O O   . HOH   K 4 .   ? 6.845   -3.150  -0.867  1.00 19.56 ? 412 HOH   A O   1 
HETATM 3810 O O   . HOH   K 4 .   ? -8.407  -5.325  8.509   1.00 19.28 ? 413 HOH   A O   1 
HETATM 3811 O O   . HOH   K 4 .   ? -17.193 -0.757  5.195   1.00 28.80 ? 414 HOH   A O   1 
HETATM 3812 O O   . HOH   K 4 .   ? -9.966  2.882   19.696  1.00 38.26 ? 415 HOH   A O   1 
HETATM 3813 O O   . HOH   K 4 .   ? 8.902   -13.217 6.288   1.00 49.92 ? 416 HOH   A O   1 
HETATM 3814 O O   . HOH   K 4 .   ? -10.231 7.497   3.872   1.00 14.93 ? 417 HOH   A O   1 
HETATM 3815 O O   . HOH   K 4 .   ? 25.683  -12.512 18.261  1.00 33.61 ? 418 HOH   A O   1 
HETATM 3816 O O   . HOH   K 4 .   ? -12.114 1.995   9.868   1.00 37.89 ? 419 HOH   A O   1 
HETATM 3817 O O   . HOH   K 4 .   ? -6.446  19.823  3.852   1.00 38.23 ? 420 HOH   A O   1 
HETATM 3818 O O   . HOH   K 4 .   ? -2.457  3.446   0.382   1.00 10.99 ? 421 HOH   A O   1 
HETATM 3819 O O   . HOH   K 4 .   ? 23.773  -3.041  15.723  1.00 36.51 ? 422 HOH   A O   1 
HETATM 3820 O O   . HOH   K 4 .   ? 16.290  -4.700  3.496   1.00 17.65 ? 423 HOH   A O   1 
HETATM 3821 O O   . HOH   K 4 .   ? -2.648  6.395   16.594  1.00 37.34 ? 424 HOH   A O   1 
HETATM 3822 O O   . HOH   K 4 .   ? -2.527  -11.817 15.444  1.00 31.16 ? 425 HOH   A O   1 
HETATM 3823 O O   . HOH   K 4 .   ? 13.977  -8.640  17.642  1.00 44.28 ? 426 HOH   A O   1 
HETATM 3824 O O   . HOH   K 4 .   ? 17.569  -3.345  11.633  1.00 17.90 ? 427 HOH   A O   1 
HETATM 3825 O O   . HOH   K 4 .   ? -9.213  -2.565  13.211  1.00 23.68 ? 428 HOH   A O   1 
HETATM 3826 O O   . HOH   K 4 .   ? -10.034 1.951   8.141   1.00 16.94 ? 429 HOH   A O   1 
HETATM 3827 O O   . HOH   K 4 .   ? -9.335  11.875  9.209   1.00 29.18 ? 430 HOH   A O   1 
HETATM 3828 O O   . HOH   K 4 .   ? 6.436   3.145   2.449   1.00 10.65 ? 431 HOH   A O   1 
HETATM 3829 O O   . HOH   K 4 .   ? -5.957  -11.300 9.774   1.00 26.30 ? 432 HOH   A O   1 
HETATM 3830 O O   . HOH   K 4 .   ? -5.243  -8.138  4.011   1.00 34.14 ? 433 HOH   A O   1 
HETATM 3831 O O   . HOH   K 4 .   ? 6.859   -14.224 5.431   1.00 34.35 ? 434 HOH   A O   1 
HETATM 3832 O O   . HOH   K 4 .   ? -1.915  -12.447 8.788   1.00 23.13 ? 435 HOH   A O   1 
HETATM 3833 O O   . HOH   K 4 .   ? 15.889  -7.875  15.430  1.00 23.05 ? 436 HOH   A O   1 
HETATM 3834 O O   . HOH   K 4 .   ? 6.044   -14.389 11.028  1.00 30.36 ? 437 HOH   A O   1 
HETATM 3835 O O   . HOH   K 4 .   ? -3.749  28.896  8.054   1.00 36.80 ? 438 HOH   A O   1 
HETATM 3836 O O   . HOH   K 4 .   ? -4.026  3.579   13.450  1.00 16.37 ? 439 HOH   A O   1 
HETATM 3837 O O   . HOH   K 4 .   ? 0.634   -4.052  -0.526  1.00 21.35 ? 440 HOH   A O   1 
HETATM 3838 O O   . HOH   K 4 .   ? 19.405  -8.574  17.182  1.00 29.63 ? 441 HOH   A O   1 
HETATM 3839 O O   . HOH   K 4 .   ? -11.194 -1.592  1.249   1.00 21.44 ? 442 HOH   A O   1 
HETATM 3840 O O   . HOH   K 4 .   ? 11.912  -12.788 15.994  1.00 47.25 ? 443 HOH   A O   1 
HETATM 3841 O O   . HOH   K 4 .   ? -4.940  -0.627  24.411  1.00 31.45 ? 444 HOH   A O   1 
HETATM 3842 O O   . HOH   K 4 .   ? -6.097  28.356  2.180   1.00 27.26 ? 445 HOH   A O   1 
HETATM 3843 O O   . HOH   K 4 .   ? 5.068   16.583  6.488   1.00 13.53 ? 446 HOH   A O   1 
HETATM 3844 O O   . HOH   K 4 .   ? 0.663   -8.863  1.386   1.00 25.22 ? 447 HOH   A O   1 
HETATM 3845 O O   . HOH   K 4 .   ? 1.875   20.579  10.922  1.00 17.79 ? 448 HOH   A O   1 
HETATM 3846 O O   . HOH   K 4 .   ? -2.850  15.668  8.801   1.00 11.90 ? 449 HOH   A O   1 
HETATM 3847 O O   . HOH   K 4 .   ? -5.940  -4.574  7.512   1.00 16.86 ? 450 HOH   A O   1 
HETATM 3848 O O   . HOH   K 4 .   ? -6.375  12.572  7.493   1.00 18.19 ? 451 HOH   A O   1 
HETATM 3849 O O   . HOH   K 4 .   ? 13.694  -12.068 5.483   1.00 38.97 ? 452 HOH   A O   1 
HETATM 3850 O O   . HOH   K 4 .   ? 3.798   3.989   21.723  1.00 19.47 ? 453 HOH   A O   1 
HETATM 3851 O O   . HOH   K 4 .   ? -3.131  18.194  9.966   1.00 16.26 ? 454 HOH   A O   1 
HETATM 3852 O O   . HOH   K 4 .   ? -4.523  5.221   11.351  1.00 18.89 ? 455 HOH   A O   1 
HETATM 3853 O O   . HOH   K 4 .   ? -10.847 5.502   -4.867  1.00 30.91 ? 456 HOH   A O   1 
HETATM 3854 O O   . HOH   K 4 .   ? 8.961   -7.731  22.250  1.00 34.44 ? 457 HOH   A O   1 
HETATM 3855 O O   . HOH   K 4 .   ? 13.319  -9.457  11.877  1.00 20.97 ? 458 HOH   A O   1 
HETATM 3856 O O   . HOH   K 4 .   ? 0.053   6.194   21.750  1.00 35.42 ? 459 HOH   A O   1 
HETATM 3857 O O   . HOH   K 4 .   ? -6.496  16.884  3.094   1.00 28.68 ? 460 HOH   A O   1 
HETATM 3858 O O   . HOH   K 4 .   ? -5.446  10.208  0.369   1.00 12.35 ? 461 HOH   A O   1 
HETATM 3859 O O   . HOH   K 4 .   ? 19.319  -11.041 14.273  1.00 41.98 ? 462 HOH   A O   1 
HETATM 3860 O O   . HOH   K 4 .   ? 5.828   -8.382  1.030   1.00 17.90 ? 463 HOH   A O   1 
HETATM 3861 O O   . HOH   K 4 .   ? -13.858 -0.115  8.969   1.00 40.81 ? 464 HOH   A O   1 
HETATM 3862 O O   . HOH   K 4 .   ? -13.064 6.443   12.656  1.00 40.48 ? 465 HOH   A O   1 
HETATM 3863 O O   . HOH   K 4 .   ? 12.394  -8.979  -5.384  1.00 45.83 ? 466 HOH   A O   1 
HETATM 3864 O O   . HOH   K 4 .   ? -2.388  -13.690 18.647  1.00 38.04 ? 467 HOH   A O   1 
HETATM 3865 O O   . HOH   K 4 .   ? 20.528  -11.286 10.327  1.00 33.24 ? 468 HOH   A O   1 
HETATM 3866 O O   . HOH   K 4 .   ? -2.554  -4.776  -0.306  1.00 29.64 ? 469 HOH   A O   1 
HETATM 3867 O O   . HOH   K 4 .   ? 11.651  -0.355  20.616  1.00 29.68 ? 470 HOH   A O   1 
HETATM 3868 O O   . HOH   K 4 .   ? 1.806   27.621  5.952   1.00 18.52 ? 471 HOH   A O   1 
HETATM 3869 O O   . HOH   K 4 .   ? 12.943  -5.479  -3.254  1.00 31.04 ? 472 HOH   A O   1 
HETATM 3870 O O   . HOH   K 4 .   ? -6.183  1.566   -0.557  1.00 13.69 ? 473 HOH   A O   1 
HETATM 3871 O O   . HOH   K 4 .   ? -10.665 13.819  5.791   1.00 45.36 ? 474 HOH   A O   1 
HETATM 3872 O O   . HOH   K 4 .   ? 2.344   -9.910  20.587  1.00 31.14 ? 475 HOH   A O   1 
HETATM 3873 O O   . HOH   K 4 .   ? -1.454  26.668  -2.335  1.00 41.88 ? 476 HOH   A O   1 
HETATM 3874 O O   . HOH   K 4 .   ? -4.404  4.429   -1.628  1.00 16.97 ? 477 HOH   A O   1 
HETATM 3875 O O   . HOH   K 4 .   ? -11.446 14.346  2.309   1.00 29.66 ? 478 HOH   A O   1 
HETATM 3876 O O   . HOH   K 4 .   ? 3.336   20.140  4.258   1.00 18.97 ? 479 HOH   A O   1 
HETATM 3877 O O   . HOH   K 4 .   ? 9.539   -13.543 -0.182  1.00 35.06 ? 480 HOH   A O   1 
HETATM 3878 O O   . HOH   K 4 .   ? -12.811 12.929  -0.825  1.00 35.24 ? 481 HOH   A O   1 
HETATM 3879 O O   . HOH   K 4 .   ? -0.776  -2.660  21.121  1.00 27.35 ? 482 HOH   A O   1 
HETATM 3880 O O   . HOH   K 4 .   ? 5.838   3.385   19.924  1.00 19.48 ? 483 HOH   A O   1 
HETATM 3881 O O   . HOH   K 4 .   ? -4.560  21.122  11.075  1.00 30.60 ? 484 HOH   A O   1 
HETATM 3882 O O   . HOH   K 4 .   ? 19.356  -4.488  13.616  1.00 21.23 ? 485 HOH   A O   1 
HETATM 3883 O O   . HOH   K 4 .   ? -14.741 3.939   -5.643  1.00 25.46 ? 486 HOH   A O   1 
HETATM 3884 O O   . HOH   K 4 .   ? 0.065   -11.653 6.959   1.00 23.69 ? 487 HOH   A O   1 
HETATM 3885 O O   . HOH   K 4 .   ? -12.297 15.775  -2.996  1.00 49.24 ? 488 HOH   A O   1 
HETATM 3886 O O   . HOH   K 4 .   ? 9.929   3.428   17.623  1.00 21.39 ? 489 HOH   A O   1 
HETATM 3887 O O   . HOH   K 4 .   ? -18.224 5.388   -1.170  1.00 20.62 ? 490 HOH   A O   1 
HETATM 3888 O O   . HOH   K 4 .   ? -11.230 -0.351  -1.259  1.00 22.44 ? 491 HOH   A O   1 
HETATM 3889 O O   . HOH   K 4 .   ? -8.036  -7.490  1.783   1.00 34.15 ? 492 HOH   A O   1 
HETATM 3890 O O   . HOH   K 4 .   ? -12.406 4.352   11.220  1.00 43.67 ? 493 HOH   A O   1 
HETATM 3891 O O   . HOH   K 4 .   ? 2.244   -14.394 12.680  1.00 36.04 ? 494 HOH   A O   1 
HETATM 3892 O O   . HOH   K 4 .   ? 14.404  -9.275  9.307   1.00 19.23 ? 495 HOH   A O   1 
HETATM 3893 O O   . HOH   K 4 .   ? 9.476   -3.264  -1.626  1.00 26.59 ? 496 HOH   A O   1 
HETATM 3894 O O   . HOH   K 4 .   ? -7.216  15.043  5.885   1.00 34.80 ? 497 HOH   A O   1 
HETATM 3895 O O   . HOH   K 4 .   ? -9.918  -6.506  12.833  1.00 38.06 ? 498 HOH   A O   1 
HETATM 3896 O O   . HOH   K 4 .   ? 19.117  -12.408 6.014   1.00 43.90 ? 499 HOH   A O   1 
HETATM 3897 O O   . HOH   K 4 .   ? -11.827 8.966   15.119  1.00 31.62 ? 500 HOH   A O   1 
HETATM 3898 O O   . HOH   K 4 .   ? -2.843  5.985   21.560  1.00 26.49 ? 501 HOH   A O   1 
HETATM 3899 O O   . HOH   K 4 .   ? -5.774  23.625  2.977   1.00 19.03 ? 502 HOH   A O   1 
HETATM 3900 O O   . HOH   K 4 .   ? 0.917   30.144  6.568   1.00 23.70 ? 503 HOH   A O   1 
HETATM 3901 O O   . HOH   K 4 .   ? -1.173  -6.885  23.696  1.00 34.55 ? 504 HOH   A O   1 
HETATM 3902 O O   . HOH   K 4 .   ? 6.118   0.174   23.642  1.00 32.07 ? 505 HOH   A O   1 
HETATM 3903 O O   . HOH   K 4 .   ? 25.500  -8.094  13.593  1.00 48.75 ? 506 HOH   A O   1 
HETATM 3904 O O   . HOH   K 4 .   ? 8.342   -12.513 8.763   1.00 25.19 ? 507 HOH   A O   1 
HETATM 3905 O O   . HOH   K 4 .   ? 23.484  -8.788  9.887   1.00 37.09 ? 508 HOH   A O   1 
HETATM 3906 O O   . HOH   K 4 .   ? -2.408  29.357  -0.035  1.00 20.08 ? 509 HOH   A O   1 
HETATM 3907 O O   . HOH   K 4 .   ? 6.709   -12.722 15.961  1.00 34.38 ? 510 HOH   A O   1 
HETATM 3908 O O   . HOH   K 4 .   ? 0.194   9.062   19.576  1.00 19.99 ? 511 HOH   A O   1 
HETATM 3909 O O   . HOH   K 4 .   ? -0.242  -13.327 12.908  1.00 25.05 ? 512 HOH   A O   1 
HETATM 3910 O O   . HOH   K 4 .   ? -14.276 10.507  1.366   1.00 27.39 ? 513 HOH   A O   1 
HETATM 3911 O O   . HOH   K 4 .   ? -9.167  -7.744  9.505   1.00 28.90 ? 514 HOH   A O   1 
HETATM 3912 O O   . HOH   K 4 .   ? -0.239  -9.089  4.039   1.00 24.10 ? 515 HOH   A O   1 
HETATM 3913 O O   . HOH   K 4 .   ? 10.649  -18.006 12.257  1.00 47.97 ? 516 HOH   A O   1 
HETATM 3914 O O   . HOH   K 4 .   ? -8.758  27.180  5.322   1.00 44.00 ? 517 HOH   A O   1 
HETATM 3915 O O   . HOH   K 4 .   ? 0.143   -4.863  24.961  1.00 29.93 ? 518 HOH   A O   1 
HETATM 3916 O O   . HOH   K 4 .   ? 8.230   -15.002 9.756   1.00 34.73 ? 519 HOH   A O   1 
HETATM 3917 O O   . HOH   K 4 .   ? -6.696  18.054  -0.079  1.00 15.90 ? 520 HOH   A O   1 
HETATM 3918 O O   . HOH   K 4 .   ? -11.780 -5.609  6.951   1.00 42.47 ? 521 HOH   A O   1 
HETATM 3919 O O   . HOH   K 4 .   ? -4.058  22.221  7.169   1.00 23.34 ? 522 HOH   A O   1 
HETATM 3920 O O   . HOH   K 4 .   ? 16.746  -6.085  1.158   1.00 20.37 ? 523 HOH   A O   1 
HETATM 3921 O O   . HOH   K 4 .   ? -7.796  -0.744  -0.462  1.00 34.51 ? 524 HOH   A O   1 
HETATM 3922 O O   . HOH   K 4 .   ? -6.206  29.551  4.633   1.00 37.67 ? 525 HOH   A O   1 
HETATM 3923 O O   . HOH   K 4 .   ? -11.406 -6.329  10.887  1.00 42.97 ? 526 HOH   A O   1 
HETATM 3924 O O   . HOH   K 4 .   ? 1.474   11.524  22.809  1.00 37.23 ? 527 HOH   A O   1 
HETATM 3925 O O   . HOH   K 4 .   ? 23.234  -9.103  23.194  1.00 26.37 ? 528 HOH   A O   1 
HETATM 3926 O O   . HOH   K 4 .   ? 0.071   -2.362  23.673  1.00 40.12 ? 529 HOH   A O   1 
HETATM 3927 O O   . HOH   K 4 .   ? -2.589  31.323  7.027   1.00 46.21 ? 530 HOH   A O   1 
HETATM 3928 O O   . HOH   K 4 .   ? 1.111   22.898  0.383   1.00 28.74 ? 531 HOH   A O   1 
HETATM 3929 O O   . HOH   K 4 .   ? 15.687  -5.743  -3.052  1.00 29.44 ? 532 HOH   A O   1 
HETATM 3930 O O   . HOH   K 4 .   ? 7.034   26.015  1.192   1.00 56.95 ? 533 HOH   A O   1 
HETATM 3931 O O   . HOH   K 4 .   ? -11.080 2.256   -7.582  1.00 52.69 ? 534 HOH   A O   1 
HETATM 3932 O O   . HOH   K 4 .   ? -11.442 -4.484  2.027   1.00 41.12 ? 535 HOH   A O   1 
HETATM 3933 O O   . HOH   K 4 .   ? 17.304  -4.491  -1.100  1.00 17.87 ? 536 HOH   A O   1 
HETATM 3934 O O   . HOH   K 4 .   ? 10.448  -11.968 -1.871  1.00 52.78 ? 537 HOH   A O   1 
HETATM 3935 O O   . HOH   K 4 .   ? 1.025   3.833   21.828  1.00 28.93 ? 538 HOH   A O   1 
HETATM 3936 O O   . HOH   K 4 .   ? -9.032  2.901   -4.222  1.00 33.10 ? 539 HOH   A O   1 
HETATM 3937 O O   . HOH   K 4 .   ? -4.212  19.569  7.580   1.00 21.99 ? 540 HOH   A O   1 
HETATM 3938 O O   . HOH   K 4 .   ? -14.209 -3.933  6.492   1.00 43.61 ? 541 HOH   A O   1 
HETATM 3939 O O   . HOH   K 4 .   ? -8.068  2.674   -7.108  1.00 47.09 ? 542 HOH   A O   1 
HETATM 3940 O O   . HOH   K 4 .   ? -0.339  8.427   22.238  1.00 42.79 ? 543 HOH   A O   1 
HETATM 3941 O O   . HOH   K 4 .   ? -9.595  16.473  2.785   1.00 31.49 ? 544 HOH   A O   1 
HETATM 3942 O O   . HOH   K 4 .   ? 4.527   21.653  8.835   1.00 44.12 ? 545 HOH   A O   1 
HETATM 3943 O O   . HOH   K 4 .   ? 4.821   23.835  5.845   1.00 31.26 ? 546 HOH   A O   1 
HETATM 3944 O O   . HOH   K 4 .   ? -5.314  14.398  9.289   1.00 18.32 ? 547 HOH   A O   1 
HETATM 3945 O O   . HOH   K 4 .   ? 4.371   26.390  6.453   1.00 25.16 ? 548 HOH   A O   1 
HETATM 3946 O O   . HOH   K 4 .   ? -11.006 -0.435  12.771  1.00 39.59 ? 549 HOH   A O   1 
HETATM 3947 O O   . HOH   K 4 .   ? -1.930  7.508   18.590  1.00 32.68 ? 550 HOH   A O   1 
HETATM 3948 O O   . HOH   K 4 .   ? 0.350   24.202  -2.093  1.00 40.99 ? 551 HOH   A O   1 
HETATM 3949 O O   . HOH   K 4 .   ? 15.671  -8.523  19.694  1.00 34.08 ? 552 HOH   A O   1 
HETATM 3950 O O   . HOH   K 4 .   ? -7.027  -2.757  0.675   1.00 29.50 ? 553 HOH   A O   1 
HETATM 3951 O O   . HOH   K 4 .   ? -6.857  16.938  8.772   1.00 52.07 ? 554 HOH   A O   1 
HETATM 3952 O O   . HOH   K 4 .   ? -9.371  25.049  4.002   1.00 48.84 ? 555 HOH   A O   1 
HETATM 3953 O O   . HOH   K 4 .   ? 0.691   2.140   24.543  1.00 46.30 ? 556 HOH   A O   1 
HETATM 3954 O O   . HOH   K 4 .   ? -15.771 -1.309  7.585   1.00 42.63 ? 557 HOH   A O   1 
HETATM 3955 O O   . HOH   K 4 .   ? -8.173  23.864  6.620   1.00 46.27 ? 558 HOH   A O   1 
HETATM 3956 O O   . HOH   K 4 .   ? -0.710  -9.827  25.569  1.00 41.60 ? 559 HOH   A O   1 
HETATM 3957 O O   . HOH   K 4 .   ? 0.014   -0.283  24.767  1.00 45.90 ? 560 HOH   A O   1 
HETATM 3958 O O   . HOH   K 4 .   ? 2.210   -9.144  -2.403  1.00 41.81 ? 561 HOH   A O   1 
HETATM 3959 O O   . HOH   K 4 .   ? 5.185   -3.884  -3.094  1.00 22.36 ? 562 HOH   A O   1 
HETATM 3960 O O   . HOH   K 4 .   ? 25.609  -4.622  14.282  1.00 42.25 ? 563 HOH   A O   1 
HETATM 3961 O O   . HOH   K 4 .   ? -12.033 4.075   -6.463  1.00 38.31 ? 564 HOH   A O   1 
HETATM 3962 O O   . HOH   K 4 .   ? 20.856  -12.533 16.645  1.00 47.78 ? 565 HOH   A O   1 
HETATM 3963 O O   . HOH   K 4 .   ? -5.968  -10.660 4.931   1.00 34.35 ? 566 HOH   A O   1 
HETATM 3964 O O   . HOH   K 4 .   ? -6.088  22.397  5.574   1.00 29.15 ? 567 HOH   A O   1 
HETATM 3965 O O   . HOH   K 4 .   ? 2.983   27.381  -3.131  1.00 33.72 ? 568 HOH   A O   1 
HETATM 3966 O O   . HOH   K 4 .   ? 0.324   9.438   25.039  1.00 41.63 ? 569 HOH   A O   1 
HETATM 3967 O O   . HOH   K 4 .   ? -6.588  22.193  9.806   1.00 49.48 ? 570 HOH   A O   1 
HETATM 3968 O O   . HOH   K 4 .   ? -6.568  19.155  6.460   1.00 41.47 ? 571 HOH   A O   1 
HETATM 3969 O O   . HOH   K 4 .   ? 23.960  -0.826  17.021  1.00 55.76 ? 572 HOH   A O   1 
HETATM 3970 O O   . HOH   K 4 .   ? 0.779   -11.463 0.103   1.00 39.51 ? 573 HOH   A O   1 
HETATM 3971 O O   . HOH   K 4 .   ? 6.966   -13.721 1.693   1.00 32.76 ? 574 HOH   A O   1 
HETATM 3972 O O   . HOH   K 4 .   ? -11.596 18.084  -0.758  1.00 47.77 ? 575 HOH   A O   1 
HETATM 3973 O O   . HOH   K 4 .   ? -1.598  -7.619  0.130   1.00 44.44 ? 576 HOH   A O   1 
HETATM 3974 O O   . HOH   K 4 .   ? -1.559  -14.460 10.517  1.00 34.42 ? 577 HOH   A O   1 
HETATM 3975 O O   . HOH   K 4 .   ? 1.925   31.057  4.163   1.00 40.25 ? 578 HOH   A O   1 
HETATM 3976 O O   . HOH   K 4 .   ? -11.787 -3.764  13.433  1.00 47.23 ? 579 HOH   A O   1 
HETATM 3977 O O   . HOH   K 4 .   ? 5.814   -10.420 -0.657  1.00 37.83 ? 580 HOH   A O   1 
HETATM 3978 O O   . HOH   K 4 .   ? 14.770  -11.454 13.152  1.00 32.02 ? 581 HOH   A O   1 
HETATM 3979 O O   . HOH   K 4 .   ? -9.466  13.226  11.589  1.00 41.99 ? 582 HOH   A O   1 
HETATM 3980 O O   . HOH   K 4 .   ? -8.022  -9.807  10.559  1.00 36.35 ? 583 HOH   A O   1 
HETATM 3981 O O   . HOH   K 4 .   ? 6.337   -16.112 8.008   1.00 41.35 ? 584 HOH   A O   1 
HETATM 3982 O O   . HOH   K 4 .   ? -2.946  -8.700  2.893   1.00 48.74 ? 585 HOH   A O   1 
HETATM 3983 O O   . HOH   K 4 .   ? 14.178  -11.628 16.941  1.00 40.22 ? 586 HOH   A O   1 
HETATM 3984 O O   . HOH   K 4 .   ? -11.558 8.157   -6.095  1.00 49.68 ? 587 HOH   A O   1 
HETATM 3985 O O   . HOH   K 4 .   ? 16.617  -10.499 15.001  1.00 30.49 ? 588 HOH   A O   1 
HETATM 3986 O O   . HOH   K 4 .   ? 9.365   -3.995  -4.111  1.00 35.74 ? 589 HOH   A O   1 
HETATM 3987 O O   . HOH   K 4 .   ? 7.268   28.913  4.301   1.00 29.71 ? 590 HOH   A O   1 
HETATM 3988 O O   . HOH   K 4 .   ? -0.187  -14.311 15.728  1.00 44.83 ? 591 HOH   A O   1 
HETATM 3989 O O   . HOH   K 4 .   ? -5.063  18.439  11.825  1.00 23.12 ? 592 HOH   A O   1 
HETATM 3990 O O   . HOH   K 4 .   ? -6.249  -11.942 7.202   1.00 44.54 ? 593 HOH   A O   1 
HETATM 3991 O O   . HOH   K 4 .   ? 4.489   -9.551  -2.899  1.00 32.22 ? 594 HOH   A O   1 
HETATM 3992 O O   . HOH   K 4 .   ? -7.018  14.318  11.662  1.00 39.52 ? 595 HOH   A O   1 
HETATM 3993 O O   . HOH   K 4 .   ? 6.560   -8.317  -1.850  1.00 46.32 ? 596 HOH   A O   1 
HETATM 3994 O O   . HOH   K 4 .   ? 4.689   2.813   24.043  1.00 34.88 ? 597 HOH   A O   1 
HETATM 3995 O O   . HOH   K 4 .   ? 11.603  -14.115 6.778   1.00 45.76 ? 598 HOH   A O   1 
HETATM 3996 O O   . HOH   K 4 .   ? -12.792 -0.041  14.103  1.00 45.16 ? 599 HOH   A O   1 
HETATM 3997 O O   . HOH   K 4 .   ? -1.475  -4.245  -2.392  1.00 35.40 ? 600 HOH   A O   1 
HETATM 3998 O O   . HOH   K 4 .   ? -1.646  29.275  -2.994  1.00 38.08 ? 601 HOH   A O   1 
HETATM 3999 O O   . HOH   K 4 .   ? -8.657  -4.801  0.699   1.00 41.10 ? 602 HOH   A O   1 
HETATM 4000 O O   . HOH   K 4 .   ? -5.307  -4.433  -0.812  1.00 32.27 ? 603 HOH   A O   1 
HETATM 4001 O O   . HOH   K 4 .   ? 5.610   -15.038 3.105   1.00 45.17 ? 604 HOH   A O   1 
HETATM 4002 O O   . HOH   K 4 .   ? 2.332   -4.234  -3.071  1.00 28.59 ? 605 HOH   A O   1 
HETATM 4003 O O   . HOH   K 4 .   ? 6.556   -6.296  -3.584  1.00 31.51 ? 606 HOH   A O   1 
HETATM 4004 O O   . HOH   K 4 .   ? 0.885   29.276  -2.975  1.00 40.77 ? 607 HOH   A O   1 
HETATM 4005 O O   . HOH   K 4 .   ? -5.286  22.255  13.327  1.00 35.41 ? 608 HOH   A O   1 
HETATM 4006 O O   . HOH   K 4 .   ? -4.823  32.265  5.204   1.00 38.69 ? 609 HOH   A O   1 
HETATM 4007 O O   . HOH   K 4 .   ? 21.478  -14.710 15.477  1.00 49.69 ? 610 HOH   A O   1 
HETATM 4008 O O   . HOH   K 4 .   ? -3.773  -15.617 16.203  1.00 45.39 ? 611 HOH   A O   1 
HETATM 4009 O O   . HOH   K 4 .   ? 5.145   -12.973 -0.138  1.00 30.53 ? 612 HOH   A O   1 
HETATM 4010 O O   . HOH   K 4 .   ? -5.585  -7.283  -0.458  1.00 37.83 ? 613 HOH   A O   1 
HETATM 4011 O O   . HOH   K 4 .   ? -0.931  -11.692 -2.063  1.00 38.67 ? 614 HOH   A O   1 
HETATM 4012 O O   . HOH   K 4 .   ? -6.145  -16.067 17.208  1.00 46.20 ? 615 HOH   A O   1 
HETATM 4013 O O   . HOH   K 4 .   ? -14.356 8.973   -6.938  1.00 51.26 ? 616 HOH   A O   1 
HETATM 4014 O O   . HOH   K 4 .   ? -2.813  -16.631 14.208  1.00 48.81 ? 617 HOH   A O   1 
HETATM 4015 O O   . HOH   K 4 .   ? 2.031   31.213  -4.777  1.00 47.78 ? 618 HOH   A O   1 
HETATM 4016 O O   . HOH   L 4 .   ? 4.924   7.458   25.536  1.00 36.81 ? 301 HOH   B O   1 
HETATM 4017 O O   . HOH   L 4 .   ? 8.940   18.983  22.429  1.00 42.44 ? 302 HOH   B O   1 
HETATM 4018 O O   . HOH   L 4 .   ? 14.374  9.046   31.424  1.00 33.72 ? 303 HOH   B O   1 
HETATM 4019 O O   . HOH   L 4 .   ? 19.442  13.391  33.502  1.00 43.31 ? 304 HOH   B O   1 
HETATM 4020 O O   . HOH   L 4 .   ? 1.778   9.300   27.264  1.00 49.75 ? 305 HOH   B O   1 
HETATM 4021 O O   . HOH   L 4 .   ? 3.608   22.111  24.024  1.00 28.17 ? 306 HOH   B O   1 
HETATM 4022 O O   . HOH   L 4 .   ? 25.633  15.673  23.260  1.00 53.44 ? 307 HOH   B O   1 
HETATM 4023 O O   . HOH   L 4 .   ? 0.472   5.539   31.674  1.00 55.51 ? 308 HOH   B O   1 
HETATM 4024 O O   . HOH   L 4 .   ? -3.981  31.479  37.918  1.00 23.67 ? 309 HOH   B O   1 
HETATM 4025 O O   . HOH   L 4 .   ? -6.671  17.942  38.346  1.00 43.64 ? 310 HOH   B O   1 
HETATM 4026 O O   . HOH   L 4 .   ? 4.230   8.851   44.487  1.00 25.64 ? 311 HOH   B O   1 
HETATM 4027 O O   . HOH   L 4 .   ? 12.692  9.106   27.114  1.00 27.53 ? 312 HOH   B O   1 
HETATM 4028 O O   . HOH   L 4 .   ? 8.170   25.873  44.049  1.00 42.27 ? 313 HOH   B O   1 
HETATM 4029 O O   . HOH   L 4 .   ? 22.826  20.037  39.496  1.00 29.22 ? 314 HOH   B O   1 
HETATM 4030 O O   . HOH   L 4 .   ? 4.000   12.290  43.084  1.00 25.39 ? 315 HOH   B O   1 
HETATM 4031 O O   . HOH   L 4 .   ? 23.622  13.836  33.897  1.00 35.07 ? 316 HOH   B O   1 
HETATM 4032 O O   . HOH   L 4 .   ? -0.587  9.171   38.583  1.00 25.10 ? 317 HOH   B O   1 
HETATM 4033 O O   . HOH   L 4 .   ? 13.161  26.687  36.844  1.00 28.71 ? 318 HOH   B O   1 
HETATM 4034 O O   . HOH   L 4 .   ? 15.236  9.958   38.795  1.00 40.29 ? 319 HOH   B O   1 
HETATM 4035 O O   . HOH   L 4 .   ? 18.255  23.674  31.741  1.00 13.75 ? 320 HOH   B O   1 
HETATM 4036 O O   . HOH   L 4 .   ? -12.377 13.283  29.298  1.00 43.71 ? 321 HOH   B O   1 
HETATM 4037 O O   . HOH   L 4 .   ? -4.891  10.279  33.445  1.00 33.78 ? 322 HOH   B O   1 
HETATM 4038 O O   . HOH   L 4 .   ? 27.287  17.489  18.236  1.00 39.26 ? 323 HOH   B O   1 
HETATM 4039 O O   . HOH   L 4 .   ? 0.804   25.106  42.756  1.00 33.17 ? 324 HOH   B O   1 
HETATM 4040 O O   . HOH   L 4 .   ? 25.966  24.736  13.158  1.00 41.61 ? 325 HOH   B O   1 
HETATM 4041 O O   . HOH   L 4 .   ? 24.762  16.788  30.791  1.00 21.31 ? 326 HOH   B O   1 
HETATM 4042 O O   . HOH   L 4 .   ? 8.615   29.615  33.525  1.00 17.90 ? 327 HOH   B O   1 
HETATM 4043 O O   . HOH   L 4 .   ? -7.513  19.461  32.127  1.00 18.28 ? 328 HOH   B O   1 
HETATM 4044 O O   . HOH   L 4 .   ? 10.072  25.812  41.221  1.00 31.10 ? 329 HOH   B O   1 
HETATM 4045 O O   . HOH   L 4 .   ? -3.369  27.475  37.878  1.00 30.68 ? 330 HOH   B O   1 
HETATM 4046 O O   . HOH   L 4 .   ? 14.374  16.720  39.543  1.00 30.15 ? 331 HOH   B O   1 
HETATM 4047 O O   . HOH   L 4 .   ? -5.376  23.300  27.720  1.00 12.41 ? 332 HOH   B O   1 
HETATM 4048 O O   . HOH   L 4 .   ? 15.578  20.680  15.806  1.00 16.04 ? 333 HOH   B O   1 
HETATM 4049 O O   . HOH   L 4 .   ? -1.344  30.214  30.545  1.00 14.53 ? 334 HOH   B O   1 
HETATM 4050 O O   . HOH   L 4 .   ? 2.729   14.736  41.220  1.00 27.49 ? 335 HOH   B O   1 
HETATM 4051 O O   . HOH   L 4 .   ? 31.421  18.685  10.621  1.00 36.69 ? 336 HOH   B O   1 
HETATM 4052 O O   . HOH   L 4 .   ? 3.330   10.072  25.477  1.00 31.31 ? 337 HOH   B O   1 
HETATM 4053 O O   . HOH   L 4 .   ? -4.904  21.676  34.932  1.00 18.09 ? 338 HOH   B O   1 
HETATM 4054 O O   . HOH   L 4 .   ? 6.392   28.096  38.704  1.00 18.32 ? 339 HOH   B O   1 
HETATM 4055 O O   . HOH   L 4 .   ? -11.294 19.247  31.262  1.00 20.52 ? 340 HOH   B O   1 
HETATM 4056 O O   . HOH   L 4 .   ? 0.854   16.700  40.896  1.00 21.37 ? 341 HOH   B O   1 
HETATM 4057 O O   . HOH   L 4 .   ? 32.234  17.500  33.131  1.00 39.80 ? 342 HOH   B O   1 
HETATM 4058 O O   . HOH   L 4 .   ? -2.238  32.807  34.488  1.00 22.16 ? 343 HOH   B O   1 
HETATM 4059 O O   . HOH   L 4 .   ? 5.108   32.179  38.753  1.00 30.46 ? 344 HOH   B O   1 
HETATM 4060 O O   . HOH   L 4 .   ? 27.941  26.816  35.418  1.00 44.00 ? 345 HOH   B O   1 
HETATM 4061 O O   . HOH   L 4 .   ? -0.780  19.504  42.811  1.00 31.72 ? 346 HOH   B O   1 
HETATM 4062 O O   . HOH   L 4 .   ? 29.073  12.858  10.945  1.00 44.72 ? 347 HOH   B O   1 
HETATM 4063 O O   . HOH   L 4 .   ? 29.452  17.306  25.662  1.00 32.00 ? 348 HOH   B O   1 
HETATM 4064 O O   . HOH   L 4 .   ? -0.899  7.611   29.113  1.00 32.43 ? 349 HOH   B O   1 
HETATM 4065 O O   . HOH   L 4 .   ? -10.121 26.695  33.963  1.00 30.68 ? 350 HOH   B O   1 
HETATM 4066 O O   . HOH   L 4 .   ? 29.125  22.622  32.973  1.00 21.34 ? 351 HOH   B O   1 
HETATM 4067 O O   . HOH   L 4 .   ? 6.807   31.697  32.846  1.00 22.50 ? 352 HOH   B O   1 
HETATM 4068 O O   . HOH   L 4 .   ? -5.097  29.261  37.214  1.00 28.07 ? 353 HOH   B O   1 
HETATM 4069 O O   . HOH   L 4 .   ? 23.638  21.880  26.934  1.00 14.05 ? 354 HOH   B O   1 
HETATM 4070 O O   . HOH   L 4 .   ? -0.905  25.253  40.566  1.00 29.79 ? 355 HOH   B O   1 
HETATM 4071 O O   . HOH   L 4 .   ? 20.282  15.089  19.733  1.00 14.52 ? 356 HOH   B O   1 
HETATM 4072 O O   . HOH   L 4 .   ? -3.913  16.147  42.575  1.00 52.42 ? 357 HOH   B O   1 
HETATM 4073 O O   . HOH   L 4 .   ? -11.325 28.300  30.342  1.00 33.76 ? 358 HOH   B O   1 
HETATM 4074 O O   . HOH   L 4 .   ? 20.820  23.127  35.134  1.00 16.57 ? 359 HOH   B O   1 
HETATM 4075 O O   . HOH   L 4 .   ? 23.031  11.928  15.078  1.00 30.31 ? 360 HOH   B O   1 
HETATM 4076 O O   . HOH   L 4 .   ? -2.866  21.978  41.921  1.00 42.97 ? 361 HOH   B O   1 
HETATM 4077 O O   . HOH   L 4 .   ? 23.362  18.732  7.510   1.00 22.56 ? 362 HOH   B O   1 
HETATM 4078 O O   . HOH   L 4 .   ? -14.957 25.001  30.115  1.00 32.33 ? 363 HOH   B O   1 
HETATM 4079 O O   . HOH   L 4 .   ? 24.959  17.527  5.532   1.00 32.40 ? 364 HOH   B O   1 
HETATM 4080 O O   . HOH   L 4 .   ? 19.513  21.618  13.610  1.00 21.65 ? 365 HOH   B O   1 
HETATM 4081 O O   . HOH   L 4 .   ? 21.171  13.788  17.422  1.00 21.03 ? 366 HOH   B O   1 
HETATM 4082 O O   . HOH   L 4 .   ? -12.358 22.511  24.961  1.00 22.62 ? 367 HOH   B O   1 
HETATM 4083 O O   . HOH   L 4 .   ? 29.179  24.625  10.735  1.00 39.69 ? 368 HOH   B O   1 
HETATM 4084 O O   . HOH   L 4 .   ? 9.369   23.021  41.763  1.00 43.48 ? 369 HOH   B O   1 
HETATM 4085 O O   . HOH   L 4 .   ? -8.170  22.471  27.961  1.00 14.67 ? 370 HOH   B O   1 
HETATM 4086 O O   . HOH   L 4 .   ? 1.051   14.115  24.164  1.00 18.38 ? 371 HOH   B O   1 
HETATM 4087 O O   . HOH   L 4 .   ? 5.141   6.574   33.809  1.00 35.55 ? 372 HOH   B O   1 
HETATM 4088 O O   . HOH   L 4 .   ? 24.636  25.323  35.716  1.00 33.45 ? 373 HOH   B O   1 
HETATM 4089 O O   . HOH   L 4 .   ? 10.569  4.784   26.612  1.00 38.25 ? 374 HOH   B O   1 
HETATM 4090 O O   . HOH   L 4 .   ? 24.886  15.449  14.435  1.00 25.12 ? 375 HOH   B O   1 
HETATM 4091 O O   . HOH   L 4 .   ? -3.508  12.444  26.546  1.00 31.87 ? 376 HOH   B O   1 
HETATM 4092 O O   . HOH   L 4 .   ? -0.935  22.480  40.302  1.00 25.57 ? 377 HOH   B O   1 
HETATM 4093 O O   . HOH   L 4 .   ? 26.795  13.958  8.056   1.00 45.95 ? 378 HOH   B O   1 
HETATM 4094 O O   . HOH   L 4 .   ? 13.406  10.559  42.653  1.00 41.17 ? 379 HOH   B O   1 
HETATM 4095 O O   . HOH   L 4 .   ? 29.565  16.629  30.087  1.00 22.84 ? 380 HOH   B O   1 
HETATM 4096 O O   . HOH   L 4 .   ? 26.159  17.915  21.327  1.00 27.70 ? 381 HOH   B O   1 
HETATM 4097 O O   . HOH   L 4 .   ? 7.536   20.819  43.102  1.00 26.79 ? 382 HOH   B O   1 
HETATM 4098 O O   . HOH   L 4 .   ? 32.491  18.454  37.198  1.00 38.20 ? 383 HOH   B O   1 
HETATM 4099 O O   . HOH   L 4 .   ? 2.056   31.060  41.953  1.00 27.27 ? 384 HOH   B O   1 
HETATM 4100 O O   . HOH   L 4 .   ? 28.683  18.238  14.732  1.00 23.39 ? 385 HOH   B O   1 
HETATM 4101 O O   . HOH   L 4 .   ? 29.899  22.177  8.666   1.00 30.91 ? 386 HOH   B O   1 
HETATM 4102 O O   . HOH   L 4 .   ? 28.196  20.908  20.531  1.00 18.76 ? 387 HOH   B O   1 
HETATM 4103 O O   . HOH   L 4 .   ? 3.891   34.905  33.268  1.00 26.22 ? 388 HOH   B O   1 
HETATM 4104 O O   . HOH   L 4 .   ? -7.394  16.993  33.052  1.00 33.19 ? 389 HOH   B O   1 
HETATM 4105 O O   . HOH   L 4 .   ? 24.167  22.332  38.969  1.00 24.42 ? 390 HOH   B O   1 
HETATM 4106 O O   . HOH   L 4 .   ? -4.292  24.397  34.690  1.00 16.46 ? 391 HOH   B O   1 
HETATM 4107 O O   . HOH   L 4 .   ? 10.532  7.509   23.067  1.00 18.87 ? 392 HOH   B O   1 
HETATM 4108 O O   . HOH   L 4 .   ? -2.966  9.946   40.426  1.00 32.93 ? 393 HOH   B O   1 
HETATM 4109 O O   . HOH   L 4 .   ? -8.457  15.070  30.733  1.00 34.42 ? 394 HOH   B O   1 
HETATM 4110 O O   . HOH   L 4 .   ? 20.762  23.521  9.412   1.00 38.61 ? 395 HOH   B O   1 
HETATM 4111 O O   . HOH   L 4 .   ? -5.688  25.884  36.325  1.00 33.81 ? 396 HOH   B O   1 
HETATM 4112 O O   . HOH   L 4 .   ? 30.718  16.115  9.089   1.00 46.98 ? 397 HOH   B O   1 
HETATM 4113 O O   . HOH   L 4 .   ? -8.062  15.285  39.214  1.00 48.43 ? 398 HOH   B O   1 
HETATM 4114 O O   . HOH   L 4 .   ? 29.420  24.137  30.756  1.00 25.62 ? 399 HOH   B O   1 
HETATM 4115 O O   . HOH   L 4 .   ? 17.588  18.614  11.297  1.00 34.68 ? 400 HOH   B O   1 
HETATM 4116 O O   . HOH   L 4 .   ? -4.213  11.495  41.426  1.00 42.69 ? 401 HOH   B O   1 
HETATM 4117 O O   . HOH   L 4 .   ? 14.979  8.916   28.998  1.00 49.07 ? 402 HOH   B O   1 
HETATM 4118 O O   . HOH   L 4 .   ? -3.991  9.578   30.338  1.00 29.50 ? 403 HOH   B O   1 
HETATM 4119 O O   . HOH   L 4 .   ? 7.975   3.149   21.559  1.00 30.70 ? 404 HOH   B O   1 
HETATM 4120 O O   . HOH   L 4 .   ? -1.336  32.657  31.970  1.00 21.18 ? 405 HOH   B O   1 
HETATM 4121 O O   . HOH   L 4 .   ? 9.211   5.011   19.668  1.00 30.58 ? 406 HOH   B O   1 
HETATM 4122 O O   . HOH   L 4 .   ? 21.485  13.532  21.736  1.00 29.80 ? 407 HOH   B O   1 
HETATM 4123 O O   . HOH   L 4 .   ? 28.448  17.278  22.799  1.00 29.27 ? 408 HOH   B O   1 
HETATM 4124 O O   . HOH   L 4 .   ? 1.657   35.853  32.478  1.00 22.61 ? 409 HOH   B O   1 
HETATM 4125 O O   . HOH   L 4 .   ? 0.080   34.845  30.401  1.00 23.56 ? 410 HOH   B O   1 
HETATM 4126 O O   . HOH   L 4 .   ? 7.308   30.808  38.683  1.00 25.41 ? 411 HOH   B O   1 
HETATM 4127 O O   . HOH   L 4 .   ? 23.589  15.240  16.933  1.00 23.38 ? 412 HOH   B O   1 
HETATM 4128 O O   . HOH   L 4 .   ? -9.310  20.885  33.863  1.00 32.03 ? 413 HOH   B O   1 
HETATM 4129 O O   . HOH   L 4 .   ? 2.604   33.631  39.754  1.00 38.18 ? 414 HOH   B O   1 
HETATM 4130 O O   . HOH   L 4 .   ? -14.945 13.873  28.299  1.00 46.50 ? 415 HOH   B O   1 
HETATM 4131 O O   . HOH   L 4 .   ? 11.922  7.222   25.448  1.00 33.91 ? 416 HOH   B O   1 
HETATM 4132 O O   . HOH   L 4 .   ? 10.498  30.950  35.074  1.00 22.60 ? 417 HOH   B O   1 
HETATM 4133 O O   . HOH   L 4 .   ? 25.637  11.990  15.088  1.00 50.97 ? 418 HOH   B O   1 
HETATM 4134 O O   . HOH   L 4 .   ? 19.097  22.034  39.049  1.00 31.67 ? 419 HOH   B O   1 
HETATM 4135 O O   . HOH   L 4 .   ? 25.655  15.074  18.949  1.00 45.78 ? 420 HOH   B O   1 
HETATM 4136 O O   . HOH   L 4 .   ? 2.196   5.822   25.630  1.00 33.62 ? 421 HOH   B O   1 
HETATM 4137 O O   . HOH   L 4 .   ? 26.974  15.270  29.778  1.00 26.89 ? 422 HOH   B O   1 
HETATM 4138 O O   . HOH   L 4 .   ? 12.642  25.804  40.951  1.00 36.85 ? 423 HOH   B O   1 
HETATM 4139 O O   . HOH   L 4 .   ? 20.987  20.105  6.978   1.00 41.71 ? 424 HOH   B O   1 
HETATM 4140 O O   . HOH   L 4 .   ? 27.251  16.057  15.569  1.00 29.69 ? 425 HOH   B O   1 
HETATM 4141 O O   . HOH   L 4 .   ? 19.171  20.569  8.943   1.00 47.78 ? 426 HOH   B O   1 
HETATM 4142 O O   . HOH   L 4 .   ? -7.392  21.575  36.103  1.00 30.03 ? 427 HOH   B O   1 
HETATM 4143 O O   . HOH   L 4 .   ? -2.021  11.704  24.775  1.00 39.46 ? 428 HOH   B O   1 
HETATM 4144 O O   . HOH   L 4 .   ? 8.685   32.109  36.795  1.00 20.79 ? 429 HOH   B O   1 
HETATM 4145 O O   . HOH   L 4 .   ? 29.955  25.126  34.629  1.00 39.93 ? 430 HOH   B O   1 
HETATM 4146 O O   . HOH   L 4 .   ? 32.266  20.662  9.483   1.00 39.66 ? 431 HOH   B O   1 
HETATM 4147 O O   . HOH   L 4 .   ? 9.179   30.702  40.582  1.00 34.94 ? 432 HOH   B O   1 
HETATM 4148 O O   . HOH   L 4 .   ? 21.497  23.171  37.786  1.00 33.38 ? 433 HOH   B O   1 
HETATM 4149 O O   . HOH   L 4 .   ? 29.525  22.223  5.783   1.00 47.56 ? 434 HOH   B O   1 
HETATM 4150 O O   . HOH   L 4 .   ? 12.504  29.907  36.559  1.00 28.41 ? 435 HOH   B O   1 
HETATM 4151 O O   . HOH   L 4 .   ? 26.894  13.850  27.360  1.00 43.32 ? 436 HOH   B O   1 
HETATM 4152 O O   . HOH   L 4 .   ? 31.730  18.074  15.021  1.00 60.00 ? 437 HOH   B O   1 
HETATM 4153 O O   . HOH   L 4 .   ? 23.374  29.645  9.009   1.00 38.22 ? 438 HOH   B O   1 
HETATM 4154 O O   . HOH   L 4 .   ? 31.822  17.592  25.234  1.00 38.79 ? 439 HOH   B O   1 
HETATM 4155 O O   . HOH   L 4 .   ? 8.110   28.369  42.960  1.00 44.32 ? 440 HOH   B O   1 
HETATM 4156 O O   . HOH   L 4 .   ? 0.184   5.322   29.024  1.00 67.15 ? 441 HOH   B O   1 
HETATM 4157 O O   . HOH   L 4 .   ? 21.321  8.640   32.743  1.00 46.03 ? 442 HOH   B O   1 
HETATM 4158 O O   . HOH   L 4 .   ? 3.468   28.828  42.807  1.00 37.56 ? 443 HOH   B O   1 
HETATM 4159 O O   . HOH   L 4 .   ? 5.786   29.137  41.343  1.00 33.98 ? 444 HOH   B O   1 
HETATM 4160 O O   . HOH   L 4 .   ? 13.104  23.500  42.131  1.00 49.80 ? 445 HOH   B O   1 
HETATM 4161 O O   . HOH   L 4 .   ? 26.629  18.787  4.024   1.00 43.82 ? 446 HOH   B O   1 
HETATM 4162 O O   . HOH   L 4 .   ? 6.156   26.308  46.230  1.00 50.09 ? 447 HOH   B O   1 
HETATM 4163 O O   . HOH   L 4 .   ? -13.781 27.265  29.741  1.00 33.90 ? 448 HOH   B O   1 
HETATM 4164 O O   . HOH   L 4 .   ? 31.211  15.494  31.771  1.00 33.02 ? 449 HOH   B O   1 
HETATM 4165 O O   . HOH   L 4 .   ? 6.043   36.600  32.747  1.00 29.14 ? 450 HOH   B O   1 
HETATM 4166 O O   . HOH   L 4 .   ? 26.064  29.557  8.529   1.00 46.70 ? 451 HOH   B O   1 
HETATM 4167 O O   . HOH   L 4 .   ? 1.023   31.877  44.009  1.00 40.44 ? 452 HOH   B O   1 
HETATM 4168 O O   . HOH   L 4 .   ? 2.085   38.247  31.934  1.00 41.41 ? 453 HOH   B O   1 
HETATM 4169 O O   . HOH   L 4 .   ? 10.484  33.870  37.861  1.00 33.40 ? 454 HOH   B O   1 
HETATM 4170 O O   . HOH   L 4 .   ? 10.700  33.505  40.602  1.00 40.63 ? 455 HOH   B O   1 
HETATM 4171 O O   . HOH   M 4 .   ? 1.351   42.137  14.736  1.00 46.43 ? 401 HOH   C O   1 
HETATM 4172 O O   . HOH   M 4 .   ? 23.974  31.635  10.345  1.00 40.78 ? 402 HOH   C O   1 
HETATM 4173 O O   . HOH   M 4 .   ? 15.500  21.630  22.578  1.00 24.40 ? 403 HOH   C O   1 
HETATM 4174 O O   . HOH   M 4 .   ? -0.775  38.941  17.034  1.00 53.23 ? 404 HOH   C O   1 
HETATM 4175 O O   . HOH   M 4 .   ? 26.338  32.711  31.627  1.00 33.71 ? 405 HOH   C O   1 
HETATM 4176 O O   . HOH   M 4 .   ? -3.954  35.475  30.388  1.00 39.81 ? 406 HOH   C O   1 
HETATM 4177 O O   . HOH   M 4 .   ? 10.509  18.777  10.357  1.00 27.46 ? 407 HOH   C O   1 
HETATM 4178 O O   . HOH   M 4 .   ? -2.229  41.158  32.143  1.00 41.71 ? 408 HOH   C O   1 
HETATM 4179 O O   . HOH   M 4 .   ? 16.944  36.481  6.420   1.00 35.51 ? 409 HOH   C O   1 
HETATM 4180 O O   . HOH   M 4 .   ? 13.403  35.488  8.806   1.00 34.96 ? 410 HOH   C O   1 
HETATM 4181 O O   . HOH   M 4 .   ? -3.561  9.707   25.293  1.00 49.78 ? 411 HOH   C O   1 
HETATM 4182 O O   . HOH   M 4 .   ? 16.016  31.726  35.400  1.00 36.48 ? 412 HOH   C O   1 
HETATM 4183 O O   . HOH   M 4 .   ? 13.400  30.969  31.711  1.00 19.36 ? 413 HOH   C O   1 
HETATM 4184 O O   . HOH   M 4 .   ? -4.587  32.091  21.604  1.00 21.47 ? 414 HOH   C O   1 
HETATM 4185 O O   . HOH   M 4 .   ? 30.312  18.941  16.881  1.00 36.31 ? 415 HOH   C O   1 
HETATM 4186 O O   . HOH   M 4 .   ? 2.846   31.192  27.432  1.00 12.10 ? 416 HOH   C O   1 
HETATM 4187 O O   . HOH   M 4 .   ? 19.935  36.948  10.638  1.00 23.86 ? 417 HOH   C O   1 
HETATM 4188 O O   . HOH   M 4 .   ? 2.943   29.933  16.131  1.00 26.49 ? 418 HOH   C O   1 
HETATM 4189 O O   . HOH   M 4 .   ? 11.694  44.234  18.857  1.00 28.00 ? 419 HOH   C O   1 
HETATM 4190 O O   . HOH   M 4 .   ? 31.820  28.164  25.636  1.00 30.04 ? 420 HOH   C O   1 
HETATM 4191 O O   . HOH   M 4 .   ? -7.786  22.338  23.137  1.00 20.66 ? 421 HOH   C O   1 
HETATM 4192 O O   . HOH   M 4 .   ? 22.637  39.406  21.246  1.00 31.04 ? 422 HOH   C O   1 
HETATM 4193 O O   . HOH   M 4 .   ? 5.088   30.758  14.590  1.00 18.79 ? 423 HOH   C O   1 
HETATM 4194 O O   . HOH   M 4 .   ? 6.792   43.478  18.240  1.00 37.47 ? 424 HOH   C O   1 
HETATM 4195 O O   . HOH   M 4 .   ? 9.426   44.004  14.879  1.00 29.67 ? 425 HOH   C O   1 
HETATM 4196 O O   . HOH   M 4 .   ? 23.659  38.067  11.841  1.00 43.20 ? 426 HOH   C O   1 
HETATM 4197 O O   . HOH   M 4 .   ? -11.253 11.049  17.211  1.00 34.15 ? 427 HOH   C O   1 
HETATM 4198 O O   . HOH   M 4 .   ? -10.103 30.158  21.321  1.00 44.37 ? 428 HOH   C O   1 
HETATM 4199 O O   . HOH   M 4 .   ? 9.275   35.324  29.834  1.00 25.51 ? 429 HOH   C O   1 
HETATM 4200 O O   . HOH   M 4 .   ? -7.673  34.294  27.838  1.00 34.05 ? 430 HOH   C O   1 
HETATM 4201 O O   . HOH   M 4 .   ? 13.089  39.054  28.532  1.00 26.26 ? 431 HOH   C O   1 
HETATM 4202 O O   . HOH   M 4 .   ? 5.244   27.376  11.577  1.00 23.40 ? 432 HOH   C O   1 
HETATM 4203 O O   . HOH   M 4 .   ? 21.970  39.350  26.473  1.00 38.71 ? 433 HOH   C O   1 
HETATM 4204 O O   . HOH   M 4 .   ? 15.039  42.751  20.960  1.00 26.02 ? 434 HOH   C O   1 
HETATM 4205 O O   . HOH   M 4 .   ? 7.231   42.449  14.316  1.00 25.14 ? 435 HOH   C O   1 
HETATM 4206 O O   . HOH   M 4 .   ? 16.089  41.918  14.311  1.00 23.57 ? 436 HOH   C O   1 
HETATM 4207 O O   . HOH   M 4 .   ? -1.264  13.915  17.050  1.00 22.16 ? 437 HOH   C O   1 
HETATM 4208 O O   . HOH   M 4 .   ? -11.309 12.734  13.563  1.00 46.46 ? 438 HOH   C O   1 
HETATM 4209 O O   . HOH   M 4 .   ? 10.256  25.909  27.820  1.00 10.73 ? 439 HOH   C O   1 
HETATM 4210 O O   . HOH   M 4 .   ? 37.414  23.367  21.314  1.00 28.17 ? 440 HOH   C O   1 
HETATM 4211 O O   . HOH   M 4 .   ? -11.217 35.426  23.220  1.00 42.80 ? 441 HOH   C O   1 
HETATM 4212 O O   . HOH   M 4 .   ? 27.728  34.027  18.112  1.00 38.81 ? 442 HOH   C O   1 
HETATM 4213 O O   . HOH   M 4 .   ? 25.642  30.958  21.967  1.00 17.72 ? 443 HOH   C O   1 
HETATM 4214 O O   . HOH   M 4 .   ? 22.758  26.373  30.318  1.00 17.01 ? 444 HOH   C O   1 
HETATM 4215 O O   . HOH   M 4 .   ? 12.844  25.152  8.581   1.00 23.88 ? 445 HOH   C O   1 
HETATM 4216 O O   . HOH   M 4 .   ? 27.466  28.124  19.018  1.00 17.92 ? 446 HOH   C O   1 
HETATM 4217 O O   . HOH   M 4 .   ? 7.475   37.964  28.728  1.00 29.34 ? 447 HOH   C O   1 
HETATM 4218 O O   . HOH   M 4 .   ? -4.023  18.971  16.780  1.00 19.26 ? 448 HOH   C O   1 
HETATM 4219 O O   . HOH   M 4 .   ? 31.057  26.517  18.506  1.00 22.39 ? 449 HOH   C O   1 
HETATM 4220 O O   . HOH   M 4 .   ? 9.230   41.911  4.940   1.00 38.58 ? 450 HOH   C O   1 
HETATM 4221 O O   . HOH   M 4 .   ? 25.008  23.607  22.648  1.00 14.57 ? 451 HOH   C O   1 
HETATM 4222 O O   . HOH   M 4 .   ? 6.914   39.058  20.382  1.00 19.32 ? 452 HOH   C O   1 
HETATM 4223 O O   . HOH   M 4 .   ? 22.880  27.574  32.807  1.00 35.31 ? 453 HOH   C O   1 
HETATM 4224 O O   . HOH   M 4 .   ? -6.068  24.063  20.017  1.00 26.09 ? 454 HOH   C O   1 
HETATM 4225 O O   . HOH   M 4 .   ? 31.673  24.231  27.416  1.00 30.57 ? 455 HOH   C O   1 
HETATM 4226 O O   . HOH   M 4 .   ? -2.546  20.904  18.129  1.00 12.90 ? 456 HOH   C O   1 
HETATM 4227 O O   . HOH   M 4 .   ? 2.572   34.530  6.920   1.00 35.72 ? 457 HOH   C O   1 
HETATM 4228 O O   . HOH   M 4 .   ? 4.746   39.078  13.951  1.00 36.12 ? 458 HOH   C O   1 
HETATM 4229 O O   . HOH   M 4 .   ? 21.540  32.647  7.727   1.00 58.14 ? 459 HOH   C O   1 
HETATM 4230 O O   . HOH   M 4 .   ? -0.686  40.258  24.696  1.00 27.26 ? 460 HOH   C O   1 
HETATM 4231 O O   . HOH   M 4 .   ? 16.916  22.371  14.340  1.00 19.87 ? 461 HOH   C O   1 
HETATM 4232 O O   . HOH   M 4 .   ? 18.793  35.498  33.877  1.00 29.87 ? 462 HOH   C O   1 
HETATM 4233 O O   . HOH   M 4 .   ? 17.681  26.852  7.837   1.00 37.20 ? 463 HOH   C O   1 
HETATM 4234 O O   . HOH   M 4 .   ? 31.594  28.836  21.455  1.00 29.02 ? 464 HOH   C O   1 
HETATM 4235 O O   . HOH   M 4 .   ? -3.896  25.676  18.833  1.00 24.13 ? 465 HOH   C O   1 
HETATM 4236 O O   . HOH   M 4 .   ? 30.995  25.262  12.058  1.00 36.57 ? 466 HOH   C O   1 
HETATM 4237 O O   . HOH   M 4 .   ? -12.897 27.473  26.877  1.00 37.32 ? 467 HOH   C O   1 
HETATM 4238 O O   . HOH   M 4 .   ? -14.327 12.829  22.841  1.00 38.36 ? 468 HOH   C O   1 
HETATM 4239 O O   . HOH   M 4 .   ? 2.347   15.628  22.396  1.00 13.12 ? 469 HOH   C O   1 
HETATM 4240 O O   . HOH   M 4 .   ? -6.824  8.738   21.053  1.00 18.66 ? 470 HOH   C O   1 
HETATM 4241 O O   . HOH   M 4 .   ? -6.662  17.492  15.340  1.00 30.78 ? 471 HOH   C O   1 
HETATM 4242 O O   . HOH   M 4 .   ? 27.694  23.472  21.433  1.00 15.85 ? 472 HOH   C O   1 
HETATM 4243 O O   . HOH   M 4 .   ? -3.518  27.573  26.083  1.00 13.25 ? 473 HOH   C O   1 
HETATM 4244 O O   . HOH   M 4 .   ? -11.101 30.159  24.869  1.00 38.20 ? 474 HOH   C O   1 
HETATM 4245 O O   . HOH   M 4 .   ? 8.600   25.543  7.398   1.00 30.24 ? 475 HOH   C O   1 
HETATM 4246 O O   . HOH   M 4 .   ? 2.299   37.853  14.164  1.00 39.22 ? 476 HOH   C O   1 
HETATM 4247 O O   . HOH   M 4 .   ? 10.128  33.285  4.164   1.00 42.31 ? 477 HOH   C O   1 
HETATM 4248 O O   . HOH   M 4 .   ? 27.301  29.255  16.429  1.00 28.94 ? 478 HOH   C O   1 
HETATM 4249 O O   . HOH   M 4 .   ? 13.255  32.969  8.357   1.00 31.38 ? 479 HOH   C O   1 
HETATM 4250 O O   . HOH   M 4 .   ? 0.827   35.011  27.572  1.00 16.02 ? 480 HOH   C O   1 
HETATM 4251 O O   . HOH   M 4 .   ? 38.613  26.587  19.979  1.00 25.76 ? 481 HOH   C O   1 
HETATM 4252 O O   . HOH   M 4 .   ? 14.339  24.613  10.902  1.00 20.29 ? 482 HOH   C O   1 
HETATM 4253 O O   . HOH   M 4 .   ? -10.888 11.886  28.255  1.00 44.46 ? 483 HOH   C O   1 
HETATM 4254 O O   . HOH   M 4 .   ? -1.610  13.994  23.738  1.00 20.18 ? 484 HOH   C O   1 
HETATM 4255 O O   . HOH   M 4 .   ? 21.064  24.707  31.907  1.00 19.37 ? 485 HOH   C O   1 
HETATM 4256 O O   . HOH   M 4 .   ? 7.234   40.040  10.542  1.00 29.84 ? 486 HOH   C O   1 
HETATM 4257 O O   . HOH   M 4 .   ? -2.040  35.497  14.183  1.00 50.56 ? 487 HOH   C O   1 
HETATM 4258 O O   . HOH   M 4 .   ? 8.924   41.738  24.340  1.00 28.65 ? 488 HOH   C O   1 
HETATM 4259 O O   . HOH   M 4 .   ? 25.470  30.452  24.688  1.00 19.36 ? 489 HOH   C O   1 
HETATM 4260 O O   . HOH   M 4 .   ? 24.684  29.479  33.494  1.00 38.54 ? 490 HOH   C O   1 
HETATM 4261 O O   . HOH   M 4 .   ? 16.385  35.671  30.171  1.00 21.35 ? 491 HOH   C O   1 
HETATM 4262 O O   . HOH   M 4 .   ? -9.548  19.618  21.475  1.00 39.51 ? 492 HOH   C O   1 
HETATM 4263 O O   . HOH   M 4 .   ? 33.331  25.045  25.667  1.00 26.18 ? 493 HOH   C O   1 
HETATM 4264 O O   . HOH   M 4 .   ? 14.151  43.924  14.491  1.00 32.93 ? 494 HOH   C O   1 
HETATM 4265 O O   . HOH   M 4 .   ? 15.560  41.175  23.338  1.00 24.41 ? 495 HOH   C O   1 
HETATM 4266 O O   . HOH   M 4 .   ? 0.242   31.714  28.747  1.00 15.94 ? 496 HOH   C O   1 
HETATM 4267 O O   . HOH   M 4 .   ? 24.601  38.481  22.842  1.00 45.66 ? 497 HOH   C O   1 
HETATM 4268 O O   . HOH   M 4 .   ? 22.654  36.625  23.887  1.00 25.89 ? 498 HOH   C O   1 
HETATM 4269 O O   . HOH   M 4 .   ? 27.523  26.944  14.303  1.00 38.38 ? 499 HOH   C O   1 
HETATM 4270 O O   . HOH   M 4 .   ? 17.848  42.124  17.685  1.00 28.13 ? 500 HOH   C O   1 
HETATM 4271 O O   . HOH   M 4 .   ? -3.279  31.012  10.269  1.00 41.78 ? 501 HOH   C O   1 
HETATM 4272 O O   . HOH   M 4 .   ? 21.752  27.273  9.116   1.00 40.62 ? 502 HOH   C O   1 
HETATM 4273 O O   . HOH   M 4 .   ? -11.153 16.633  22.367  1.00 24.61 ? 503 HOH   C O   1 
HETATM 4274 O O   . HOH   M 4 .   ? 15.180  29.618  33.312  1.00 23.39 ? 504 HOH   C O   1 
HETATM 4275 O O   . HOH   M 4 .   ? 6.717   27.628  6.699   1.00 24.92 ? 505 HOH   C O   1 
HETATM 4276 O O   . HOH   M 4 .   ? 6.654   23.336  9.182   1.00 17.93 ? 506 HOH   C O   1 
HETATM 4277 O O   . HOH   M 4 .   ? -10.059 32.680  22.671  1.00 35.80 ? 507 HOH   C O   1 
HETATM 4278 O O   . HOH   M 4 .   ? -9.137  31.295  29.233  1.00 36.69 ? 508 HOH   C O   1 
HETATM 4279 O O   . HOH   M 4 .   ? 27.290  31.935  26.173  1.00 34.97 ? 509 HOH   C O   1 
HETATM 4280 O O   . HOH   M 4 .   ? 6.903   40.506  3.456   1.00 41.64 ? 510 HOH   C O   1 
HETATM 4281 O O   . HOH   M 4 .   ? -12.466 10.369  25.708  1.00 28.42 ? 511 HOH   C O   1 
HETATM 4282 O O   . HOH   M 4 .   ? 14.740  31.911  6.200   1.00 36.91 ? 512 HOH   C O   1 
HETATM 4283 O O   . HOH   M 4 .   ? 7.731   31.434  3.817   1.00 40.47 ? 513 HOH   C O   1 
HETATM 4284 O O   . HOH   M 4 .   ? -6.107  13.612  26.722  1.00 30.66 ? 514 HOH   C O   1 
HETATM 4285 O O   . HOH   M 4 .   ? 21.107  37.402  33.455  1.00 33.56 ? 515 HOH   C O   1 
HETATM 4286 O O   . HOH   M 4 .   ? 34.778  22.367  22.140  1.00 27.56 ? 516 HOH   C O   1 
HETATM 4287 O O   . HOH   M 4 .   ? 12.924  39.553  25.796  1.00 24.48 ? 517 HOH   C O   1 
HETATM 4288 O O   . HOH   M 4 .   ? 16.071  42.620  27.425  1.00 35.73 ? 518 HOH   C O   1 
HETATM 4289 O O   . HOH   M 4 .   ? -8.915  7.065   20.262  1.00 24.28 ? 519 HOH   C O   1 
HETATM 4290 O O   . HOH   M 4 .   ? 9.296   45.846  13.420  1.00 44.95 ? 520 HOH   C O   1 
HETATM 4291 O O   . HOH   M 4 .   ? 13.546  43.430  8.570   1.00 28.72 ? 521 HOH   C O   1 
HETATM 4292 O O   . HOH   M 4 .   ? 23.654  36.898  16.647  1.00 35.36 ? 522 HOH   C O   1 
HETATM 4293 O O   . HOH   M 4 .   ? 21.179  23.860  12.214  1.00 31.87 ? 523 HOH   C O   1 
HETATM 4294 O O   . HOH   M 4 .   ? 18.997  29.064  36.010  1.00 35.91 ? 524 HOH   C O   1 
HETATM 4295 O O   . HOH   M 4 .   ? 18.126  43.243  10.969  1.00 41.86 ? 525 HOH   C O   1 
HETATM 4296 O O   . HOH   M 4 .   ? -1.911  39.604  27.277  1.00 23.58 ? 526 HOH   C O   1 
HETATM 4297 O O   . HOH   M 4 .   ? -7.952  14.029  28.642  1.00 40.64 ? 527 HOH   C O   1 
HETATM 4298 O O   . HOH   M 4 .   ? -14.749 16.018  19.326  1.00 41.11 ? 528 HOH   C O   1 
HETATM 4299 O O   . HOH   M 4 .   ? 1.394   39.877  13.616  1.00 61.97 ? 529 HOH   C O   1 
HETATM 4300 O O   . HOH   M 4 .   ? 6.294   35.330  5.059   1.00 43.35 ? 530 HOH   C O   1 
HETATM 4301 O O   . HOH   M 4 .   ? 16.286  33.924  5.110   1.00 34.44 ? 531 HOH   C O   1 
HETATM 4302 O O   . HOH   M 4 .   ? 22.007  26.131  34.981  1.00 28.48 ? 532 HOH   C O   1 
HETATM 4303 O O   . HOH   M 4 .   ? 20.894  28.027  36.566  1.00 28.07 ? 533 HOH   C O   1 
HETATM 4304 O O   . HOH   M 4 .   ? 30.410  30.498  27.174  1.00 51.08 ? 534 HOH   C O   1 
HETATM 4305 O O   . HOH   M 4 .   ? 13.954  42.051  25.311  1.00 36.63 ? 535 HOH   C O   1 
HETATM 4306 O O   . HOH   M 4 .   ? 15.967  21.286  11.792  1.00 26.82 ? 536 HOH   C O   1 
HETATM 4307 O O   . HOH   M 4 .   ? 7.290   23.891  6.519   1.00 45.72 ? 537 HOH   C O   1 
HETATM 4308 O O   . HOH   M 4 .   ? 28.596  28.814  12.743  1.00 48.94 ? 538 HOH   C O   1 
HETATM 4309 O O   . HOH   M 4 .   ? -8.188  16.584  18.795  1.00 34.45 ? 539 HOH   C O   1 
HETATM 4310 O O   . HOH   M 4 .   ? -0.512  11.743  19.384  1.00 42.19 ? 540 HOH   C O   1 
HETATM 4311 O O   . HOH   M 4 .   ? -4.082  8.288   21.379  1.00 29.52 ? 541 HOH   C O   1 
HETATM 4312 O O   . HOH   M 4 .   ? 38.492  23.257  18.977  1.00 33.99 ? 542 HOH   C O   1 
HETATM 4313 O O   . HOH   M 4 .   ? 11.049  26.889  7.695   1.00 27.83 ? 543 HOH   C O   1 
HETATM 4314 O O   . HOH   M 4 .   ? -6.396  18.752  18.670  1.00 25.13 ? 544 HOH   C O   1 
HETATM 4315 O O   . HOH   M 4 .   ? -3.197  34.415  12.473  1.00 50.57 ? 545 HOH   C O   1 
HETATM 4316 O O   . HOH   M 4 .   ? -3.468  23.433  17.088  1.00 22.90 ? 546 HOH   C O   1 
HETATM 4317 O O   . HOH   M 4 .   ? 14.260  37.728  32.855  1.00 36.80 ? 547 HOH   C O   1 
HETATM 4318 O O   . HOH   M 4 .   ? 25.045  33.320  21.291  1.00 39.39 ? 548 HOH   C O   1 
HETATM 4319 O O   . HOH   M 4 .   ? 13.375  44.312  11.127  1.00 50.66 ? 549 HOH   C O   1 
HETATM 4320 O O   . HOH   M 4 .   ? 6.727   20.273  6.104   1.00 40.04 ? 550 HOH   C O   1 
HETATM 4321 O O   . HOH   M 4 .   ? -10.132 17.398  19.835  1.00 32.44 ? 551 HOH   C O   1 
HETATM 4322 O O   . HOH   M 4 .   ? -1.809  36.678  30.009  1.00 33.14 ? 552 HOH   C O   1 
HETATM 4323 O O   . HOH   M 4 .   ? 9.946   34.775  1.934   1.00 45.00 ? 553 HOH   C O   1 
HETATM 4324 O O   . HOH   M 4 .   ? 0.768   37.861  27.483  1.00 26.35 ? 554 HOH   C O   1 
HETATM 4325 O O   . HOH   M 4 .   ? 11.906  32.683  33.449  1.00 24.37 ? 555 HOH   C O   1 
HETATM 4326 O O   . HOH   M 4 .   ? 3.101   38.820  26.293  1.00 28.63 ? 556 HOH   C O   1 
HETATM 4327 O O   . HOH   M 4 .   ? 32.076  28.453  17.462  1.00 44.80 ? 557 HOH   C O   1 
HETATM 4328 O O   . HOH   M 4 .   ? -9.504  22.218  25.516  1.00 16.43 ? 558 HOH   C O   1 
HETATM 4329 O O   . HOH   M 4 .   ? 5.629   25.826  9.384   1.00 33.36 ? 559 HOH   C O   1 
HETATM 4330 O O   . HOH   M 4 .   ? 10.841  38.982  30.057  1.00 45.19 ? 560 HOH   C O   1 
HETATM 4331 O O   . HOH   M 4 .   ? 10.112  44.302  23.468  1.00 46.85 ? 561 HOH   C O   1 
HETATM 4332 O O   . HOH   M 4 .   ? 7.994   22.342  3.928   1.00 36.11 ? 562 HOH   C O   1 
HETATM 4333 O O   . HOH   M 4 .   ? -0.796  39.413  32.022  1.00 47.94 ? 563 HOH   C O   1 
HETATM 4334 O O   . HOH   M 4 .   ? -14.733 11.485  24.961  1.00 46.88 ? 564 HOH   C O   1 
HETATM 4335 O O   . HOH   M 4 .   ? 5.751   37.647  5.968   1.00 44.67 ? 565 HOH   C O   1 
HETATM 4336 O O   . HOH   M 4 .   ? 31.972  29.847  23.592  1.00 37.05 ? 566 HOH   C O   1 
HETATM 4337 O O   . HOH   M 4 .   ? -3.905  24.362  14.547  1.00 38.70 ? 567 HOH   C O   1 
HETATM 4338 O O   . HOH   M 4 .   ? 17.384  43.857  19.697  1.00 39.61 ? 568 HOH   C O   1 
HETATM 4339 O O   . HOH   M 4 .   ? -6.497  26.555  17.611  1.00 47.55 ? 569 HOH   C O   1 
HETATM 4340 O O   . HOH   M 4 .   ? -9.220  6.054   22.737  1.00 40.64 ? 570 HOH   C O   1 
HETATM 4341 O O   . HOH   M 4 .   ? 24.469  33.866  24.247  1.00 49.00 ? 571 HOH   C O   1 
HETATM 4342 O O   . HOH   M 4 .   ? 16.002  35.692  32.935  1.00 25.16 ? 572 HOH   C O   1 
HETATM 4343 O O   . HOH   M 4 .   ? 21.648  39.323  10.542  1.00 37.36 ? 573 HOH   C O   1 
HETATM 4344 O O   . HOH   M 4 .   ? -5.149  19.645  14.388  1.00 28.55 ? 574 HOH   C O   1 
HETATM 4345 O O   . HOH   M 4 .   ? 9.253   44.236  17.464  1.00 35.80 ? 575 HOH   C O   1 
HETATM 4346 O O   . HOH   M 4 .   ? 29.488  29.790  19.933  1.00 23.65 ? 576 HOH   C O   1 
HETATM 4347 O O   . HOH   M 4 .   ? 28.219  31.764  21.431  1.00 30.07 ? 577 HOH   C O   1 
HETATM 4348 O O   . HOH   M 4 .   ? 10.727  41.024  26.022  1.00 40.40 ? 578 HOH   C O   1 
HETATM 4349 O O   . HOH   M 4 .   ? 10.871  45.212  21.502  1.00 39.88 ? 579 HOH   C O   1 
HETATM 4350 O O   . HOH   M 4 .   ? 33.930  29.398  19.853  1.00 46.25 ? 580 HOH   C O   1 
HETATM 4351 O O   . HOH   M 4 .   ? 6.466   39.759  7.920   1.00 45.73 ? 581 HOH   C O   1 
HETATM 4352 O O   . HOH   M 4 .   ? 18.757  42.939  26.787  1.00 36.33 ? 582 HOH   C O   1 
HETATM 4353 O O   . HOH   M 4 .   ? 30.210  18.983  21.310  1.00 35.13 ? 583 HOH   C O   1 
HETATM 4354 O O   . HOH   M 4 .   ? 17.183  28.610  38.003  1.00 35.38 ? 584 HOH   C O   1 
HETATM 4355 O O   . HOH   M 4 .   ? -3.490  4.751   24.152  1.00 40.16 ? 585 HOH   C O   1 
HETATM 4356 O O   . HOH   M 4 .   ? 7.755   37.092  31.056  1.00 40.09 ? 586 HOH   C O   1 
HETATM 4357 O O   . HOH   M 4 .   ? 10.394  38.362  32.313  1.00 43.17 ? 587 HOH   C O   1 
HETATM 4358 O O   . HOH   M 4 .   ? 18.389  43.196  15.167  1.00 38.12 ? 588 HOH   C O   1 
HETATM 4359 O O   . HOH   M 4 .   ? 17.534  42.989  23.893  1.00 29.99 ? 589 HOH   C O   1 
HETATM 4360 O O   . HOH   M 4 .   ? 20.663  42.233  11.077  1.00 42.70 ? 590 HOH   C O   1 
HETATM 4361 O O   . HOH   M 4 .   ? 10.061  34.561  32.844  1.00 33.41 ? 591 HOH   C O   1 
HETATM 4362 O O   . HOH   M 4 .   ? 4.971   39.517  28.420  1.00 30.87 ? 592 HOH   C O   1 
HETATM 4363 O O   . HOH   M 4 .   ? 2.990   41.494  26.096  1.00 36.69 ? 593 HOH   C O   1 
HETATM 4364 O O   . HOH   M 4 .   ? 20.846  42.377  14.226  1.00 38.30 ? 594 HOH   C O   1 
HETATM 4365 O O   . HOH   M 4 .   ? -7.284  16.735  12.778  1.00 35.22 ? 595 HOH   C O   1 
HETATM 4366 O O   . HOH   M 4 .   ? 15.626  44.533  7.004   1.00 21.90 ? 596 HOH   C O   1 
HETATM 4367 O O   . HOH   M 4 .   ? 2.298   39.346  29.408  1.00 46.34 ? 597 HOH   C O   1 
HETATM 4368 O O   . HOH   M 4 .   ? 17.841  45.161  8.662   1.00 27.07 ? 598 HOH   C O   1 
HETATM 4369 O O   . HOH   M 4 .   ? 38.618  20.637  19.058  1.00 34.66 ? 599 HOH   C O   1 
HETATM 4370 O O   . HOH   M 4 .   ? 32.456  32.489  26.679  1.00 43.81 ? 600 HOH   C O   1 
HETATM 4371 O O   . HOH   M 4 .   ? 16.766  47.366  9.581   1.00 49.09 ? 601 HOH   C O   1 
HETATM 4372 O O   . HOH   M 4 .   ? 19.613  47.328  10.954  1.00 51.04 ? 602 HOH   C O   1 
HETATM 4373 O O   . HOH   N 4 .   ? 7.846   14.432  -12.059 1.00 37.59 ? 301 HOH   D O   1 
HETATM 4374 O O   . HOH   N 4 .   ? 17.841  23.296  -8.014  1.00 39.84 ? 302 HOH   D O   1 
HETATM 4375 O O   . HOH   N 4 .   ? 24.148  -3.220  -7.744  1.00 39.43 ? 303 HOH   D O   1 
HETATM 4376 O O   . HOH   N 4 .   ? 2.756   10.491  4.629   1.00 24.98 ? 304 HOH   D O   1 
HETATM 4377 O O   . HOH   N 4 .   ? 21.145  7.908   -11.352 1.00 41.33 ? 305 HOH   D O   1 
HETATM 4378 O O   . HOH   N 4 .   ? 22.726  10.356  -8.384  1.00 33.22 ? 306 HOH   D O   1 
HETATM 4379 O O   . HOH   N 4 .   ? -8.104  14.522  -8.710  1.00 31.48 ? 307 HOH   D O   1 
HETATM 4380 O O   . HOH   N 4 .   ? 14.874  -0.152  1.036   1.00 14.50 ? 308 HOH   D O   1 
HETATM 4381 O O   . HOH   N 4 .   ? 11.309  25.199  -2.091  1.00 56.32 ? 309 HOH   D O   1 
HETATM 4382 O O   . HOH   N 4 .   ? 4.513   0.597   -3.783  1.00 17.41 ? 310 HOH   D O   1 
HETATM 4383 O O   . HOH   N 4 .   ? 9.832   1.951   -10.375 1.00 38.01 ? 311 HOH   D O   1 
HETATM 4384 O O   . HOH   N 4 .   ? 20.792  13.087  -11.862 1.00 32.96 ? 312 HOH   D O   1 
HETATM 4385 O O   . HOH   N 4 .   ? 24.647  2.147   -12.733 1.00 53.71 ? 313 HOH   D O   1 
HETATM 4386 O O   . HOH   N 4 .   ? 0.811   18.435  -11.315 1.00 35.09 ? 314 HOH   D O   1 
HETATM 4387 O O   . HOH   N 4 .   ? 14.129  15.985  -12.742 1.00 15.11 ? 315 HOH   D O   1 
HETATM 4388 O O   . HOH   N 4 .   ? 3.666   8.197   -14.440 1.00 30.93 ? 316 HOH   D O   1 
HETATM 4389 O O   . HOH   N 4 .   ? 9.317   -2.795  23.584  1.00 38.60 ? 317 HOH   D O   1 
HETATM 4390 O O   . HOH   N 4 .   ? 27.809  8.320   -2.393  1.00 21.24 ? 318 HOH   D O   1 
HETATM 4391 O O   . HOH   N 4 .   ? 8.773   15.402  -14.517 1.00 45.82 ? 319 HOH   D O   1 
HETATM 4392 O O   . HOH   N 4 .   ? -6.115  18.051  -8.479  1.00 37.87 ? 320 HOH   D O   1 
HETATM 4393 O O   . HOH   N 4 .   ? 14.261  8.388   19.649  1.00 25.21 ? 321 HOH   D O   1 
HETATM 4394 O O   . HOH   N 4 .   ? 14.184  2.489   -9.858  1.00 35.12 ? 322 HOH   D O   1 
HETATM 4395 O O   . HOH   N 4 .   ? 24.126  10.485  1.244   1.00 43.91 ? 323 HOH   D O   1 
HETATM 4396 O O   . HOH   N 4 .   ? 22.600  -0.644  -4.667  1.00 20.14 ? 324 HOH   D O   1 
HETATM 4397 O O   . HOH   N 4 .   ? 17.095  18.250  -13.425 1.00 19.53 ? 325 HOH   D O   1 
HETATM 4398 O O   . HOH   N 4 .   ? -2.132  18.506  -5.841  1.00 21.07 ? 326 HOH   D O   1 
HETATM 4399 O O   . HOH   N 4 .   ? 17.735  15.425  12.895  1.00 26.63 ? 327 HOH   D O   1 
HETATM 4400 O O   . HOH   N 4 .   ? -3.898  14.485  -1.263  1.00 12.90 ? 328 HOH   D O   1 
HETATM 4401 O O   . HOH   N 4 .   ? -4.132  6.354   -3.688  1.00 16.78 ? 329 HOH   D O   1 
HETATM 4402 O O   . HOH   N 4 .   ? 29.886  -2.870  3.699   1.00 25.63 ? 330 HOH   D O   1 
HETATM 4403 O O   . HOH   N 4 .   ? 5.259   26.013  -9.236  1.00 45.74 ? 331 HOH   D O   1 
HETATM 4404 O O   . HOH   N 4 .   ? 9.059   24.314  -0.384  1.00 34.66 ? 332 HOH   D O   1 
HETATM 4405 O O   . HOH   N 4 .   ? 15.561  21.416  -2.498  1.00 33.86 ? 333 HOH   D O   1 
HETATM 4406 O O   . HOH   N 4 .   ? 10.407  5.321   15.832  1.00 15.19 ? 334 HOH   D O   1 
HETATM 4407 O O   . HOH   N 4 .   ? 25.592  -6.387  11.243  1.00 46.97 ? 335 HOH   D O   1 
HETATM 4408 O O   . HOH   N 4 .   ? 10.927  21.590  -9.655  1.00 21.22 ? 336 HOH   D O   1 
HETATM 4409 O O   . HOH   N 4 .   ? 10.404  -0.147  -5.537  1.00 30.13 ? 337 HOH   D O   1 
HETATM 4410 O O   . HOH   N 4 .   ? 16.759  20.239  5.706   1.00 89.15 ? 338 HOH   D O   1 
HETATM 4411 O O   . HOH   N 4 .   ? -5.419  20.714  -5.913  1.00 28.70 ? 339 HOH   D O   1 
HETATM 4412 O O   . HOH   N 4 .   ? 18.383  6.656   13.940  1.00 17.89 ? 340 HOH   D O   1 
HETATM 4413 O O   . HOH   N 4 .   ? 3.911   27.452  -11.881 1.00 42.83 ? 341 HOH   D O   1 
HETATM 4414 O O   . HOH   N 4 .   ? 5.414   18.599  -11.880 1.00 44.34 ? 342 HOH   D O   1 
HETATM 4415 O O   . HOH   N 4 .   ? 1.795   9.053   -12.788 1.00 34.67 ? 343 HOH   D O   1 
HETATM 4416 O O   . HOH   N 4 .   ? 31.613  -2.257  -3.112  1.00 26.93 ? 344 HOH   D O   1 
HETATM 4417 O O   . HOH   N 4 .   ? -5.554  4.262   -4.915  1.00 24.74 ? 345 HOH   D O   1 
HETATM 4418 O O   . HOH   N 4 .   ? 21.765  0.852   17.302  1.00 39.01 ? 346 HOH   D O   1 
HETATM 4419 O O   . HOH   N 4 .   ? -0.799  14.864  -8.004  1.00 19.49 ? 347 HOH   D O   1 
HETATM 4420 O O   . HOH   N 4 .   ? 19.331  7.451   16.388  1.00 26.62 ? 348 HOH   D O   1 
HETATM 4421 O O   . HOH   N 4 .   ? -2.281  9.155   -11.035 1.00 33.92 ? 349 HOH   D O   1 
HETATM 4422 O O   . HOH   N 4 .   ? 5.721   13.436  -14.180 1.00 32.79 ? 350 HOH   D O   1 
HETATM 4423 O O   . HOH   N 4 .   ? 18.005  -1.669  -1.368  1.00 14.92 ? 351 HOH   D O   1 
HETATM 4424 O O   . HOH   N 4 .   ? 19.941  -5.599  -0.978  1.00 31.42 ? 352 HOH   D O   1 
HETATM 4425 O O   . HOH   N 4 .   ? 2.761   13.045  -14.378 1.00 39.62 ? 353 HOH   D O   1 
HETATM 4426 O O   . HOH   N 4 .   ? 10.105  20.214  4.216   1.00 26.30 ? 354 HOH   D O   1 
HETATM 4427 O O   . HOH   N 4 .   ? 11.007  0.431   23.654  1.00 43.40 ? 355 HOH   D O   1 
HETATM 4428 O O   . HOH   N 4 .   ? 15.060  3.112   26.091  1.00 25.52 ? 356 HOH   D O   1 
HETATM 4429 O O   . HOH   N 4 .   ? 25.681  4.417   8.312   1.00 43.50 ? 357 HOH   D O   1 
HETATM 4430 O O   . HOH   N 4 .   ? 4.972   2.666   -9.065  1.00 19.72 ? 358 HOH   D O   1 
HETATM 4431 O O   . HOH   N 4 .   ? 18.694  -1.544  7.293   1.00 15.11 ? 359 HOH   D O   1 
HETATM 4432 O O   . HOH   N 4 .   ? 1.716   0.181   -3.782  1.00 19.24 ? 360 HOH   D O   1 
HETATM 4433 O O   . HOH   N 4 .   ? 21.216  4.694   26.408  1.00 36.21 ? 361 HOH   D O   1 
HETATM 4434 O O   . HOH   N 4 .   ? 21.684  10.255  -0.156  1.00 38.46 ? 362 HOH   D O   1 
HETATM 4435 O O   . HOH   N 4 .   ? 12.206  2.536   18.863  1.00 25.30 ? 363 HOH   D O   1 
HETATM 4436 O O   . HOH   N 4 .   ? 0.315   2.501   -13.592 1.00 29.27 ? 364 HOH   D O   1 
HETATM 4437 O O   . HOH   N 4 .   ? -5.468  16.768  -2.140  1.00 15.77 ? 365 HOH   D O   1 
HETATM 4438 O O   . HOH   N 4 .   ? 5.515   18.427  4.577   1.00 19.22 ? 366 HOH   D O   1 
HETATM 4439 O O   . HOH   N 4 .   ? 21.442  7.212   -0.629  1.00 27.93 ? 367 HOH   D O   1 
HETATM 4440 O O   . HOH   N 4 .   ? 21.197  0.244   13.880  1.00 34.37 ? 368 HOH   D O   1 
HETATM 4441 O O   . HOH   N 4 .   ? 5.678   24.392  -5.624  1.00 43.62 ? 369 HOH   D O   1 
HETATM 4442 O O   . HOH   N 4 .   ? 16.506  -2.530  1.643   1.00 16.26 ? 370 HOH   D O   1 
HETATM 4443 O O   . HOH   N 4 .   ? -0.841  22.714  -4.391  1.00 29.99 ? 371 HOH   D O   1 
HETATM 4444 O O   . HOH   N 4 .   ? 9.828   22.175  -11.867 1.00 39.04 ? 372 HOH   D O   1 
HETATM 4445 O O   . HOH   N 4 .   ? 25.911  -1.116  10.390  1.00 46.23 ? 373 HOH   D O   1 
HETATM 4446 O O   . HOH   N 4 .   ? 24.194  -5.781  3.016   1.00 25.37 ? 374 HOH   D O   1 
HETATM 4447 O O   . HOH   N 4 .   ? -7.628  22.977  1.367   1.00 41.14 ? 375 HOH   D O   1 
HETATM 4448 O O   . HOH   N 4 .   ? 20.873  23.169  -11.173 1.00 40.12 ? 376 HOH   D O   1 
HETATM 4449 O O   . HOH   N 4 .   ? 3.611   22.099  1.234   1.00 30.53 ? 377 HOH   D O   1 
HETATM 4450 O O   . HOH   N 4 .   ? 12.585  21.324  4.372   1.00 30.73 ? 378 HOH   D O   1 
HETATM 4451 O O   . HOH   N 4 .   ? 24.122  13.200  -1.765  1.00 42.82 ? 379 HOH   D O   1 
HETATM 4452 O O   . HOH   N 4 .   ? 12.955  -0.447  -6.873  1.00 33.07 ? 380 HOH   D O   1 
HETATM 4453 O O   . HOH   N 4 .   ? -2.025  12.421  -7.785  1.00 17.84 ? 381 HOH   D O   1 
HETATM 4454 O O   . HOH   N 4 .   ? 19.948  4.786   -10.585 1.00 48.38 ? 382 HOH   D O   1 
HETATM 4455 O O   . HOH   N 4 .   ? 21.397  -0.404  20.725  1.00 26.79 ? 383 HOH   D O   1 
HETATM 4456 O O   . HOH   N 4 .   ? 17.630  16.900  6.293   1.00 31.22 ? 384 HOH   D O   1 
HETATM 4457 O O   . HOH   N 4 .   ? 27.403  -1.892  6.433   1.00 31.78 ? 385 HOH   D O   1 
HETATM 4458 O O   . HOH   N 4 .   ? 30.016  -5.394  0.643   1.00 35.75 ? 386 HOH   D O   1 
HETATM 4459 O O   . HOH   N 4 .   ? 22.189  15.822  -6.947  1.00 36.90 ? 387 HOH   D O   1 
HETATM 4460 O O   . HOH   N 4 .   ? 16.339  18.186  8.620   1.00 20.16 ? 388 HOH   D O   1 
HETATM 4461 O O   . HOH   N 4 .   ? 16.424  3.267   28.531  1.00 31.38 ? 389 HOH   D O   1 
HETATM 4462 O O   . HOH   N 4 .   ? -3.499  11.671  -10.003 1.00 31.71 ? 390 HOH   D O   1 
HETATM 4463 O O   . HOH   N 4 .   ? 17.991  -3.756  26.422  1.00 32.88 ? 391 HOH   D O   1 
HETATM 4464 O O   . HOH   N 4 .   ? 3.196   11.289  -12.160 1.00 25.37 ? 392 HOH   D O   1 
HETATM 4465 O O   . HOH   N 4 .   ? 21.958  -3.184  -4.093  1.00 20.75 ? 393 HOH   D O   1 
HETATM 4466 O O   . HOH   N 4 .   ? 21.708  -2.775  25.826  1.00 33.40 ? 394 HOH   D O   1 
HETATM 4467 O O   . HOH   N 4 .   ? 25.967  -4.545  8.710   1.00 43.10 ? 395 HOH   D O   1 
HETATM 4468 O O   . HOH   N 4 .   ? 25.929  13.503  -10.443 1.00 58.64 ? 396 HOH   D O   1 
HETATM 4469 O O   . HOH   N 4 .   ? -10.875 13.933  -5.590  1.00 37.28 ? 397 HOH   D O   1 
HETATM 4470 O O   . HOH   N 4 .   ? 11.627  7.124   -12.384 1.00 41.42 ? 398 HOH   D O   1 
HETATM 4471 O O   . HOH   N 4 .   ? 23.124  -7.113  5.395   1.00 29.89 ? 399 HOH   D O   1 
HETATM 4472 O O   . HOH   N 4 .   ? 11.907  25.317  -12.273 1.00 41.49 ? 400 HOH   D O   1 
HETATM 4473 O O   . HOH   N 4 .   ? 16.445  23.268  9.845   1.00 26.26 ? 401 HOH   D O   1 
HETATM 4474 O O   . HOH   N 4 .   ? 11.991  24.494  -9.620  1.00 51.28 ? 402 HOH   D O   1 
HETATM 4475 O O   . HOH   N 4 .   ? 20.368  4.048   20.120  1.00 38.02 ? 403 HOH   D O   1 
HETATM 4476 O O   . HOH   N 4 .   ? -0.481  20.682  -6.429  1.00 29.33 ? 404 HOH   D O   1 
HETATM 4477 O O   . HOH   N 4 .   ? 11.953  6.349   20.866  1.00 31.77 ? 405 HOH   D O   1 
HETATM 4478 O O   . HOH   N 4 .   ? 11.366  4.852   -10.777 1.00 33.50 ? 406 HOH   D O   1 
HETATM 4479 O O   . HOH   N 4 .   ? 28.806  3.445   7.987   1.00 45.50 ? 407 HOH   D O   1 
HETATM 4480 O O   . HOH   N 4 .   ? -11.804 18.754  -4.202  1.00 45.90 ? 408 HOH   D O   1 
HETATM 4481 O O   . HOH   N 4 .   ? -9.237  19.284  0.309   1.00 35.64 ? 409 HOH   D O   1 
HETATM 4482 O O   . HOH   N 4 .   ? -2.719  -0.375  -5.396  1.00 47.39 ? 410 HOH   D O   1 
HETATM 4483 O O   . HOH   N 4 .   ? 21.135  -2.759  14.737  1.00 23.52 ? 411 HOH   D O   1 
HETATM 4484 O O   . HOH   N 4 .   ? 20.151  4.759   17.462  1.00 34.56 ? 412 HOH   D O   1 
HETATM 4485 O O   . HOH   N 4 .   ? -3.392  27.026  -3.784  1.00 31.98 ? 413 HOH   D O   1 
HETATM 4486 O O   . HOH   N 4 .   ? 22.161  3.776   11.720  1.00 43.77 ? 414 HOH   D O   1 
HETATM 4487 O O   . HOH   N 4 .   ? 22.241  13.133  -9.473  1.00 40.44 ? 415 HOH   D O   1 
HETATM 4488 O O   . HOH   N 4 .   ? 12.680  4.238   25.446  1.00 34.06 ? 416 HOH   D O   1 
HETATM 4489 O O   . HOH   N 4 .   ? -5.992  1.858   -3.490  1.00 20.24 ? 417 HOH   D O   1 
HETATM 4490 O O   . HOH   N 4 .   ? 24.011  -0.522  12.882  1.00 42.78 ? 418 HOH   D O   1 
HETATM 4491 O O   . HOH   N 4 .   ? 20.926  6.940   12.256  1.00 40.56 ? 419 HOH   D O   1 
HETATM 4492 O O   . HOH   N 4 .   ? 15.105  24.335  -7.667  1.00 37.67 ? 420 HOH   D O   1 
HETATM 4493 O O   . HOH   N 4 .   ? 27.227  8.503   0.077   1.00 39.47 ? 421 HOH   D O   1 
HETATM 4494 O O   . HOH   N 4 .   ? 14.858  21.369  3.685   1.00 41.30 ? 422 HOH   D O   1 
HETATM 4495 O O   . HOH   N 4 .   ? 18.679  0.020   -5.345  1.00 24.25 ? 423 HOH   D O   1 
HETATM 4496 O O   . HOH   N 4 .   ? 5.512   -1.763  -4.840  1.00 22.64 ? 424 HOH   D O   1 
HETATM 4497 O O   . HOH   N 4 .   ? 11.545  3.982   23.162  1.00 35.66 ? 425 HOH   D O   1 
HETATM 4498 O O   . HOH   N 4 .   ? 28.821  7.427   1.851   1.00 30.42 ? 426 HOH   D O   1 
HETATM 4499 O O   . HOH   N 4 .   ? 17.943  6.493   29.392  1.00 42.34 ? 427 HOH   D O   1 
HETATM 4500 O O   . HOH   N 4 .   ? 15.164  25.008  -5.221  1.00 42.37 ? 428 HOH   D O   1 
HETATM 4501 O O   . HOH   N 4 .   ? 26.840  -5.657  3.798   1.00 42.47 ? 429 HOH   D O   1 
HETATM 4502 O O   . HOH   N 4 .   ? 18.800  1.488   -10.019 1.00 46.01 ? 430 HOH   D O   1 
HETATM 4503 O O   . HOH   N 4 .   ? 11.341  0.433   -9.445  1.00 38.80 ? 431 HOH   D O   1 
HETATM 4504 O O   . HOH   N 4 .   ? 11.429  24.073  4.291   1.00 37.62 ? 432 HOH   D O   1 
HETATM 4505 O O   . HOH   N 4 .   ? -4.979  -0.116  -5.046  1.00 32.93 ? 433 HOH   D O   1 
HETATM 4506 O O   . HOH   N 4 .   ? -12.423 16.557  -5.789  1.00 46.56 ? 434 HOH   D O   1 
HETATM 4507 O O   . HOH   N 4 .   ? 22.233  3.481   16.096  1.00 49.97 ? 435 HOH   D O   1 
HETATM 4508 O O   . HOH   N 4 .   ? 14.769  25.289  6.666   1.00 39.43 ? 436 HOH   D O   1 
HETATM 4509 O O   . HOH   N 4 .   ? -2.493  26.629  -6.232  1.00 29.83 ? 437 HOH   D O   1 
HETATM 4510 O O   . HOH   N 4 .   ? 27.390  0.585   8.949   1.00 51.76 ? 438 HOH   D O   1 
HETATM 4511 O O   . HOH   N 4 .   ? 3.835   1.660   -11.275 1.00 39.48 ? 439 HOH   D O   1 
HETATM 4512 O O   . HOH   N 4 .   ? 19.286  -2.234  -3.741  1.00 19.59 ? 440 HOH   D O   1 
HETATM 4513 O O   . HOH   N 4 .   ? 4.647   22.166  3.351   1.00 38.31 ? 441 HOH   D O   1 
HETATM 4514 O O   . HOH   N 4 .   ? 21.933  2.121   19.776  1.00 37.10 ? 442 HOH   D O   1 
HETATM 4515 O O   . HOH   N 4 .   ? -2.291  16.446  -9.686  1.00 36.95 ? 443 HOH   D O   1 
HETATM 4516 O O   . HOH   N 4 .   ? 15.112  0.544   29.468  1.00 43.26 ? 444 HOH   D O   1 
HETATM 4517 O O   . HOH   N 4 .   ? -3.636  18.346  -8.212  1.00 28.99 ? 445 HOH   D O   1 
HETATM 4518 O O   . HOH   N 4 .   ? 1.222   -1.930  -4.825  1.00 54.54 ? 446 HOH   D O   1 
HETATM 4519 O O   . HOH   N 4 .   ? 21.472  8.902   16.238  1.00 49.26 ? 447 HOH   D O   1 
HETATM 4520 O O   . HOH   N 4 .   ? 20.318  -0.197  -7.624  1.00 32.41 ? 448 HOH   D O   1 
HETATM 4521 O O   . HOH   N 4 .   ? 30.247  -6.116  -2.091  1.00 37.12 ? 449 HOH   D O   1 
HETATM 4522 O O   . HOH   N 4 .   ? 1.277   0.609   -10.335 1.00 29.68 ? 450 HOH   D O   1 
HETATM 4523 O O   . HOH   N 4 .   ? 20.049  -4.841  26.392  1.00 40.72 ? 451 HOH   D O   1 
HETATM 4524 O O   . HOH   N 4 .   ? 4.027   -0.249  -9.112  1.00 37.48 ? 452 HOH   D O   1 
HETATM 4525 O O   . HOH   N 4 .   ? -8.809  20.547  2.597   1.00 37.67 ? 453 HOH   D O   1 
HETATM 4526 O O   . HOH   N 4 .   ? 7.913   -2.173  -5.550  1.00 28.92 ? 454 HOH   D O   1 
HETATM 4527 O O   . HOH   N 4 .   ? -4.304  14.373  -10.932 1.00 43.65 ? 455 HOH   D O   1 
HETATM 4528 O O   . HOH   N 4 .   ? 21.936  11.207  17.845  1.00 28.83 ? 456 HOH   D O   1 
HETATM 4529 O O   . HOH   N 4 .   ? 3.226   2.943   -13.787 1.00 43.11 ? 457 HOH   D O   1 
HETATM 4530 O O   . HOH   N 4 .   ? 15.866  4.390   -12.613 1.00 36.93 ? 458 HOH   D O   1 
HETATM 4531 O O   . HOH   N 4 .   ? 8.409   -2.680  -8.309  1.00 37.31 ? 459 HOH   D O   1 
HETATM 4532 O O   . HOH   N 4 .   ? -4.006  26.085  -8.029  1.00 40.06 ? 460 HOH   D O   1 
HETATM 4533 O O   . HOH   N 4 .   ? 19.894  24.893  -12.553 1.00 36.99 ? 461 HOH   D O   1 
HETATM 4534 O O   . HOH   N 4 .   ? 23.081  -9.636  4.274   1.00 44.37 ? 462 HOH   D O   1 
HETATM 4535 O O   . HOH   N 4 .   ? 13.441  3.482   -11.854 1.00 43.43 ? 463 HOH   D O   1 
HETATM 4536 O O   . HOH   N 4 .   ? -2.157  -3.015  -4.453  1.00 35.67 ? 464 HOH   D O   1 
HETATM 4537 O O   . HOH   N 4 .   ? 31.459  -4.957  -3.853  1.00 35.42 ? 465 HOH   D O   1 
HETATM 4538 O O   . HOH   N 4 .   ? 17.931  -3.782  -5.494  1.00 36.68 ? 466 HOH   D O   1 
HETATM 4539 O O   . HOH   N 4 .   ? -13.184 18.919  2.106   1.00 50.27 ? 467 HOH   D O   1 
HETATM 4540 O O   . HOH   N 4 .   ? 3.703   -2.052  -7.068  1.00 33.58 ? 468 HOH   D O   1 
HETATM 4541 O O   . HOH   N 4 .   ? 30.015  9.861   3.107   1.00 64.20 ? 469 HOH   D O   1 
HETATM 4542 O O   . HOH   N 4 .   ? -0.667  28.469  -6.940  1.00 43.17 ? 470 HOH   D O   1 
HETATM 4543 O O   . HOH   N 4 .   ? 29.384  12.121  1.559   1.00 48.22 ? 471 HOH   D O   1 
HETATM 4544 O O   . HOH   N 4 .   ? 21.547  27.799  -13.408 1.00 50.53 ? 472 HOH   D 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   . ALA   A 1   ? 0.5726 0.3074 0.5078 0.0623  0.0419  0.0349  15  ALA   A N   
2    C CA  . ALA   A 1   ? 0.5671 0.3130 0.4856 0.0759  0.0422  0.0317  15  ALA   A CA  
3    C C   . ALA   A 1   ? 0.5261 0.3039 0.4478 0.0892  0.0394  0.0297  15  ALA   A C   
4    O O   . ALA   A 1   ? 0.5397 0.3162 0.4594 0.0933  0.0519  0.0144  15  ALA   A O   
5    C CB  . ALA   A 1   ? 0.5894 0.3274 0.4917 0.0729  0.0503  0.0262  15  ALA   A CB  
6    N N   . GLY   A 2   ? 0.4711 0.2806 0.3895 0.0843  0.0193  0.0291  16  GLY   A N   
7    C CA  . GLY   A 2   ? 0.3812 0.2368 0.2966 0.0763  -0.0090 0.0343  16  GLY   A CA  
8    C C   . GLY   A 2   ? 0.3146 0.2043 0.2352 0.0518  -0.0168 0.0161  16  GLY   A C   
9    O O   . GLY   A 2   ? 0.3265 0.1886 0.2346 0.0288  -0.0118 -0.0020 16  GLY   A O   
10   N N   . ILE   A 3   ? 0.2800 0.1995 0.2264 0.0595  -0.0144 0.0341  17  ILE   A N   
11   C CA  . ILE   A 3   ? 0.2734 0.1872 0.2145 0.0360  0.0079  0.0208  17  ILE   A CA  
12   C C   . ILE   A 3   ? 0.2909 0.1612 0.2018 0.0412  0.0099  -0.0014 17  ILE   A C   
13   O O   . ILE   A 3   ? 0.3189 0.1602 0.2107 0.0561  0.0166  0.0013  17  ILE   A O   
14   C CB  . ILE   A 3   ? 0.2704 0.1927 0.2013 0.0174  0.0090  0.0271  17  ILE   A CB  
15   C CG1 . ILE   A 3   ? 0.2874 0.2191 0.2028 0.0157  0.0018  0.0161  17  ILE   A CG1 
16   C CG2 . ILE   A 3   ? 0.2828 0.1846 0.2107 0.0072  0.0137  0.0444  17  ILE   A CG2 
17   C CD1 . ILE   A 3   ? 0.2917 0.2320 0.2160 0.0037  0.0013  0.0127  17  ILE   A CD1 
18   N N   . THR   A 4   ? 0.3174 0.1471 0.2144 0.0434  0.0029  0.0006  18  THR   A N   
19   C CA  . THR   A 4   ? 0.3250 0.1401 0.2133 0.0346  0.0209  -0.0095 18  THR   A CA  
20   C C   . THR   A 4   ? 0.3363 0.1323 0.2032 0.0239  0.0357  0.0027  18  THR   A C   
21   O O   . THR   A 4   ? 0.3611 0.1367 0.2235 0.0364  0.0468  0.0271  18  THR   A O   
22   C CB  . THR   A 4   ? 0.3175 0.1407 0.2158 0.0313  0.0289  -0.0179 18  THR   A CB  
23   O OG1 . THR   A 4   ? 0.3180 0.1392 0.2256 0.0339  0.0264  -0.0125 18  THR   A OG1 
24   C CG2 . THR   A 4   ? 0.3146 0.1391 0.2157 0.0405  0.0353  -0.0158 18  THR   A CG2 
25   N N   . GLY   A 5   ? 0.3095 0.1360 0.1805 0.0148  0.0217  -0.0006 19  GLY   A N   
26   C CA  . GLY   A 5   ? 0.2937 0.1352 0.1798 0.0281  0.0259  0.0063  19  GLY   A CA  
27   C C   . GLY   A 5   ? 0.3089 0.1193 0.1627 0.0012  0.0408  0.0062  19  GLY   A C   
28   O O   . GLY   A 5   ? 0.3303 0.1147 0.1842 0.0006  0.0513  0.0164  19  GLY   A O   
29   N N   . THR   A 6   ? 0.3142 0.1173 0.1903 -0.0018 0.0591  0.0032  20  THR   A N   
30   C CA  . THR   A 6   ? 0.3251 0.1329 0.1808 -0.0141 0.0529  -0.0043 20  THR   A CA  
31   C C   . THR   A 6   ? 0.3384 0.1252 0.1647 -0.0159 0.0414  0.0216  20  THR   A C   
32   O O   . THR   A 6   ? 0.3770 0.1319 0.1981 0.0018  0.0083  0.0251  20  THR   A O   
33   C CB  . THR   A 6   ? 0.3335 0.1596 0.1876 -0.0209 0.0458  -0.0121 20  THR   A CB  
34   O OG1 . THR   A 6   ? 0.3555 0.1656 0.1859 -0.0357 0.0509  -0.0127 20  THR   A OG1 
35   C CG2 . THR   A 6   ? 0.3345 0.1809 0.2184 -0.0098 0.0413  -0.0059 20  THR   A CG2 
36   N N   . TRP   A 7   ? 0.3018 0.1275 0.1510 0.0056  0.0442  0.0068  21  TRP   A N   
37   C CA  . TRP   A 7   ? 0.2869 0.1325 0.1559 0.0132  0.0317  0.0003  21  TRP   A CA  
38   C C   . TRP   A 7   ? 0.2884 0.1328 0.1562 0.0024  0.0512  0.0164  21  TRP   A C   
39   O O   . TRP   A 7   ? 0.2676 0.1473 0.1647 0.0093  0.0417  0.0249  21  TRP   A O   
40   C CB  . TRP   A 7   ? 0.2759 0.1384 0.1550 0.0294  0.0190  0.0140  21  TRP   A CB  
41   C CG  . TRP   A 7   ? 0.2806 0.1458 0.1565 0.0435  0.0155  0.0032  21  TRP   A CG  
42   C CD1 . TRP   A 7   ? 0.2539 0.1499 0.1650 0.0332  0.0214  -0.0041 21  TRP   A CD1 
43   C CD2 . TRP   A 7   ? 0.3011 0.1615 0.1690 0.0621  0.0129  -0.0074 21  TRP   A CD2 
44   N NE1 . TRP   A 7   ? 0.2833 0.1590 0.1817 0.0483  0.0334  -0.0019 21  TRP   A NE1 
45   C CE2 . TRP   A 7   ? 0.3069 0.1625 0.1728 0.0715  0.0148  -0.0007 21  TRP   A CE2 
46   C CE3 . TRP   A 7   ? 0.3177 0.1717 0.1783 0.0741  -0.0168 0.0020  21  TRP   A CE3 
47   C CZ2 . TRP   A 7   ? 0.3395 0.1837 0.1880 0.0794  0.0291  -0.0141 21  TRP   A CZ2 
48   C CZ3 . TRP   A 7   ? 0.3419 0.1879 0.1769 0.0742  -0.0075 -0.0173 21  TRP   A CZ3 
49   C CH2 . TRP   A 7   ? 0.3530 0.1881 0.2005 0.0814  0.0154  -0.0188 21  TRP   A CH2 
50   N N   . TYR   A 8   ? 0.2891 0.1251 0.1674 -0.0036 0.0521  0.0178  22  TYR   A N   
51   C CA  . TYR   A 8   ? 0.3057 0.1297 0.1682 -0.0348 0.0828  0.0093  22  TYR   A CA  
52   C C   . TYR   A 8   ? 0.2991 0.1267 0.1819 -0.0234 0.0547  0.0093  22  TYR   A C   
53   O O   . TYR   A 8   ? 0.3031 0.1335 0.1745 -0.0106 0.0419  0.0048  22  TYR   A O   
54   C CB  . TYR   A 8   ? 0.3556 0.1508 0.2167 -0.0618 0.1142  -0.0031 22  TYR   A CB  
55   C CG  . TYR   A 8   ? 0.3970 0.1601 0.2276 -0.0795 0.1325  -0.0152 22  TYR   A CG  
56   C CD1 . TYR   A 8   ? 0.3908 0.1781 0.2434 -0.0983 0.1288  -0.0168 22  TYR   A CD1 
57   C CD2 . TYR   A 8   ? 0.4101 0.1821 0.2335 -0.0901 0.1361  -0.0119 22  TYR   A CD2 
58   C CE1 . TYR   A 8   ? 0.4186 0.1967 0.2556 -0.1180 0.1383  -0.0339 22  TYR   A CE1 
59   C CE2 . TYR   A 8   ? 0.4253 0.2031 0.2471 -0.1058 0.1497  -0.0256 22  TYR   A CE2 
60   C CZ  . TYR   A 8   ? 0.4381 0.2127 0.2535 -0.1291 0.1468  -0.0434 22  TYR   A CZ  
61   O OH  . TYR   A 8   ? 0.4873 0.2382 0.2726 -0.1534 0.1611  -0.0651 22  TYR   A OH  
62   N N   . ASN   A 9   ? 0.2705 0.1156 0.1818 -0.0361 0.0576  0.0064  23  ASN   A N   
63   C CA  . ASN   A 9   ? 0.2750 0.1204 0.1805 -0.0258 0.0524  0.0073  23  ASN   A CA  
64   C C   . ASN   A 9   ? 0.2951 0.1253 0.1903 -0.0316 0.0552  0.0108  23  ASN   A C   
65   O O   . ASN   A 9   ? 0.3077 0.1377 0.2081 -0.0555 0.0743  -0.0053 23  ASN   A O   
66   C CB  . ASN   A 9   ? 0.2432 0.1429 0.1941 -0.0169 0.0673  0.0132  23  ASN   A CB  
67   C CG  . ASN   A 9   ? 0.2316 0.1383 0.1482 -0.0286 0.0305  0.0083  23  ASN   A CG  
68   O OD1 . ASN   A 9   ? 0.2287 0.1371 0.1729 -0.0188 0.0436  -0.0022 23  ASN   A OD1 
69   N ND2 . ASN   A 9   ? 0.2395 0.1502 0.1547 -0.0376 -0.0110 0.0194  23  ASN   A ND2 
70   N N   . GLN   A 10  ? 0.3180 0.1247 0.1570 -0.0251 0.0360  0.0093  24  GLN   A N   
71   C CA  . GLN   A 10  ? 0.3423 0.1460 0.1576 -0.0267 0.0522  0.0076  24  GLN   A CA  
72   C C   . GLN   A 10  ? 0.3209 0.1762 0.1500 -0.0526 0.0874  -0.0022 24  GLN   A C   
73   O O   . GLN   A 10  ? 0.3509 0.2032 0.1866 -0.0434 0.1051  -0.0040 24  GLN   A O   
74   C CB  . GLN   A 10  ? 0.3465 0.1371 0.1665 -0.0163 0.0412  0.0058  24  GLN   A CB  
75   C CG  . GLN   A 10  ? 0.3164 0.1399 0.1706 -0.0100 0.0499  0.0243  24  GLN   A CG  
76   C CD  . GLN   A 10  ? 0.2619 0.1331 0.1736 -0.0073 0.0420  0.0181  24  GLN   A CD  
77   O OE1 . GLN   A 10  ? 0.2641 0.1322 0.1931 -0.0074 0.0500  0.0220  24  GLN   A OE1 
78   N NE2 . GLN   A 10  ? 0.2340 0.1438 0.1849 -0.0193 0.0449  0.0229  24  GLN   A NE2 
79   N N   . LEU   A 11  ? 0.2870 0.1931 0.1793 -0.0558 0.0548  -0.0152 25  LEU   A N   
80   C CA  . LEU   A 11  ? 0.3032 0.2167 0.2144 -0.0625 0.0562  -0.0312 25  LEU   A CA  
81   C C   . LEU   A 11  ? 0.3255 0.2459 0.2235 -0.0762 0.0779  -0.0405 25  LEU   A C   
82   O O   . LEU   A 11  ? 0.3457 0.2766 0.2527 -0.0745 0.0681  -0.0502 25  LEU   A O   
83   C CB  . LEU   A 11  ? 0.3209 0.2204 0.2514 -0.0446 0.0169  -0.0174 25  LEU   A CB  
84   C CG  . LEU   A 11  ? 0.3381 0.2197 0.2668 -0.0239 -0.0209 -0.0107 25  LEU   A CG  
85   C CD1 . LEU   A 11  ? 0.3607 0.2217 0.2889 -0.0150 -0.0127 -0.0036 25  LEU   A CD1 
86   C CD2 . LEU   A 11  ? 0.3478 0.2176 0.2733 -0.0213 -0.0140 -0.0055 25  LEU   A CD2 
87   N N   . GLY   A 12  ? 0.3377 0.2336 0.2164 -0.1085 0.0959  -0.0394 26  GLY   A N   
88   C CA  . GLY   A 12  ? 0.3443 0.2259 0.2056 -0.1188 0.0944  -0.0423 26  GLY   A CA  
89   C C   . GLY   A 12  ? 0.3180 0.2078 0.2108 -0.0997 0.0984  -0.0315 26  GLY   A C   
90   O O   . GLY   A 12  ? 0.3317 0.2335 0.2353 -0.1118 0.0718  -0.0242 26  GLY   A O   
91   N N   . SER   A 13  ? 0.2577 0.1702 0.1986 -0.0715 0.0924  -0.0157 27  SER   A N   
92   C CA  . SER   A 13  ? 0.2535 0.1383 0.1908 -0.0398 0.0781  -0.0107 27  SER   A CA  
93   C C   . SER   A 13  ? 0.2419 0.1343 0.1788 -0.0155 0.0634  0.0030  27  SER   A C   
94   O O   . SER   A 13  ? 0.2702 0.1503 0.2033 -0.0193 0.0329  -0.0010 27  SER   A O   
95   C CB  . SER   A 13  ? 0.2416 0.1278 0.2029 -0.0186 0.0800  -0.0157 27  SER   A CB  
96   O OG  . SER   A 13  ? 0.2487 0.1409 0.2183 -0.0119 0.0622  -0.0135 27  SER   A OG  
97   N N   . THR   A 14  ? 0.2493 0.1332 0.1840 -0.0202 0.0663  -0.0091 28  THR   A N   
98   C CA  . THR   A 14  ? 0.2494 0.1329 0.1897 -0.0315 0.0747  -0.0104 28  THR   A CA  
99   C C   . THR   A 14  ? 0.2397 0.1323 0.1567 -0.0192 0.0636  0.0032  28  THR   A C   
100  O O   . THR   A 14  ? 0.2364 0.1513 0.1723 -0.0138 0.0303  0.0075  28  THR   A O   
101  C CB  . THR   A 14  ? 0.2722 0.1559 0.2161 -0.0422 0.0929  -0.0256 28  THR   A CB  
102  O OG1 . THR   A 14  ? 0.3150 0.1800 0.2296 -0.0624 0.1113  -0.0182 28  THR   A OG1 
103  C CG2 . THR   A 14  ? 0.2802 0.1575 0.2245 -0.0409 0.0607  -0.0199 28  THR   A CG2 
104  N N   . PHE   A 15  ? 0.2249 0.1266 0.1537 -0.0064 0.0572  -0.0085 29  PHE   A N   
105  C CA  . PHE   A 15  ? 0.2308 0.1340 0.1574 0.0000  0.0283  -0.0080 29  PHE   A CA  
106  C C   . PHE   A 15  ? 0.2327 0.1287 0.1492 -0.0048 0.0246  0.0001  29  PHE   A C   
107  O O   . PHE   A 15  ? 0.2660 0.1168 0.1610 0.0083  0.0225  0.0078  29  PHE   A O   
108  C CB  . PHE   A 15  ? 0.2116 0.1349 0.1640 0.0018  0.0198  0.0049  29  PHE   A CB  
109  C CG  . PHE   A 15  ? 0.2193 0.1208 0.1630 0.0238  0.0071  0.0059  29  PHE   A CG  
110  C CD1 . PHE   A 15  ? 0.2138 0.1311 0.1847 0.0168  0.0319  0.0005  29  PHE   A CD1 
111  C CD2 . PHE   A 15  ? 0.2426 0.1290 0.1858 0.0176  0.0072  0.0012  29  PHE   A CD2 
112  C CE1 . PHE   A 15  ? 0.2217 0.1217 0.1857 0.0407  0.0141  0.0159  29  PHE   A CE1 
113  C CE2 . PHE   A 15  ? 0.2398 0.1307 0.1857 0.0211  0.0125  0.0018  29  PHE   A CE2 
114  C CZ  . PHE   A 15  ? 0.2275 0.1093 0.1769 0.0339  0.0297  0.0143  29  PHE   A CZ  
115  N N   . ILE   A 16  ? 0.2306 0.1296 0.1746 -0.0020 0.0319  0.0020  30  ILE   A N   
116  C CA  . ILE   A 16  ? 0.2465 0.1432 0.1670 0.0000  0.0349  -0.0038 30  ILE   A CA  
117  C C   . ILE   A 16  ? 0.2366 0.1572 0.1556 0.0069  0.0231  0.0193  30  ILE   A C   
118  O O   . ILE   A 16  ? 0.2742 0.1987 0.1785 0.0307  0.0433  0.0504  30  ILE   A O   
119  C CB  . ILE   A 16  ? 0.2646 0.1521 0.1905 0.0108  0.0402  -0.0040 30  ILE   A CB  
120  C CG1 . ILE   A 16  ? 0.2582 0.1618 0.2051 -0.0092 0.0440  -0.0133 30  ILE   A CG1 
121  C CG2 . ILE   A 16  ? 0.3006 0.1636 0.2292 0.0304  0.0298  -0.0010 30  ILE   A CG2 
122  C CD1 . ILE   A 16  ? 0.2750 0.1687 0.2319 -0.0047 0.0326  -0.0064 30  ILE   A CD1 
123  N N   . VAL   A 17  ? 0.2298 0.1339 0.1527 0.0040  0.0219  -0.0029 31  VAL   A N   
124  C CA  . VAL   A 17  ? 0.2418 0.1255 0.1510 0.0049  0.0190  -0.0055 31  VAL   A CA  
125  C C   . VAL   A 17  ? 0.2441 0.1318 0.1638 0.0086  0.0283  -0.0019 31  VAL   A C   
126  O O   . VAL   A 17  ? 0.2428 0.1313 0.1792 0.0021  0.0070  0.0022  31  VAL   A O   
127  C CB  . VAL   A 17  ? 0.2363 0.1492 0.1611 -0.0013 -0.0180 -0.0081 31  VAL   A CB  
128  C CG1 . VAL   A 17  ? 0.2604 0.1669 0.1625 0.0113  -0.0376 -0.0100 31  VAL   A CG1 
129  C CG2 . VAL   A 17  ? 0.2270 0.1447 0.1792 0.0002  0.0098  0.0038  31  VAL   A CG2 
130  N N   . THR   A 18  ? 0.2171 0.1397 0.1549 0.0157  0.0108  -0.0259 32  THR   A N   
131  C CA  . THR   A 18  ? 0.2298 0.1512 0.1655 0.0012  -0.0050 -0.0519 32  THR   A CA  
132  C C   . THR   A 18  ? 0.2338 0.1369 0.1726 0.0067  -0.0154 -0.0271 32  THR   A C   
133  O O   . THR   A 18  ? 0.2290 0.1389 0.1773 0.0079  -0.0070 -0.0151 32  THR   A O   
134  C CB  . THR   A 18  ? 0.2487 0.1655 0.2079 -0.0090 -0.0145 -0.0601 32  THR   A CB  
135  O OG1 . THR   A 18  ? 0.2705 0.1820 0.2254 -0.0265 -0.0039 -0.0340 32  THR   A OG1 
136  C CG2 . THR   A 18  ? 0.2791 0.1776 0.2121 0.0163  -0.0186 -0.0718 32  THR   A CG2 
137  N N   . ALA   A 19  ? 0.2594 0.1386 0.2014 0.0189  -0.0199 -0.0202 33  ALA   A N   
138  C CA  . ALA   A 19  ? 0.2677 0.1570 0.2253 0.0319  -0.0137 -0.0171 33  ALA   A CA  
139  C C   . ALA   A 19  ? 0.2767 0.1642 0.2652 0.0272  0.0146  -0.0303 33  ALA   A C   
140  O O   . ALA   A 19  ? 0.3078 0.1715 0.3178 0.0330  0.0399  0.0048  33  ALA   A O   
141  C CB  . ALA   A 19  ? 0.2776 0.1753 0.2352 0.0215  -0.0024 0.0112  33  ALA   A CB  
142  N N   . GLY   A 20  ? 0.2681 0.1755 0.2367 0.0215  0.0030  -0.0691 34  GLY   A N   
143  C CA  . GLY   A 20  ? 0.2983 0.1816 0.2709 0.0391  0.0195  -0.0940 34  GLY   A CA  
144  C C   . GLY   A 20  ? 0.3121 0.1910 0.3036 0.0667  0.0277  -0.0905 34  GLY   A C   
145  O O   . GLY   A 20  ? 0.3409 0.1949 0.3132 0.0567  0.0191  -0.0795 34  GLY   A O   
146  N N   . ALA   A 21  ? 0.3230 0.2016 0.3443 0.0708  0.0236  -0.0906 35  ALA   A N   
147  C CA  . ALA   A 21  ? 0.3329 0.2182 0.3814 0.0878  0.0210  -0.1033 35  ALA   A CA  
148  C C   . ALA   A 21  ? 0.3387 0.2451 0.3865 0.0832  0.0184  -0.1088 35  ALA   A C   
149  O O   . ALA   A 21  ? 0.3568 0.2596 0.3994 0.0952  -0.0133 -0.0936 35  ALA   A O   
150  C CB  . ALA   A 21  ? 0.3422 0.2158 0.4078 0.0835  0.0246  -0.1048 35  ALA   A CB  
151  N N   . ASP   A 22  ? 0.3311 0.2450 0.3614 0.0763  0.0290  -0.1139 36  ASP   A N   
152  C CA  . ASP   A 22  ? 0.3162 0.2546 0.3248 0.0661  0.0205  -0.0999 36  ASP   A CA  
153  C C   . ASP   A 22  ? 0.2730 0.2320 0.2755 0.0647  0.0267  -0.0964 36  ASP   A C   
154  O O   . ASP   A 22  ? 0.2883 0.2441 0.2757 0.0203  0.0515  -0.1072 36  ASP   A O   
155  C CB  . ASP   A 22  ? 0.3222 0.2745 0.3139 0.0490  0.0081  -0.1065 36  ASP   A CB  
156  C CG  . ASP   A 22  ? 0.3363 0.2910 0.3004 0.0362  -0.0085 -0.1077 36  ASP   A CG  
157  O OD1 . ASP   A 22  ? 0.2906 0.2872 0.2709 0.0528  -0.0207 -0.1275 36  ASP   A OD1 
158  O OD2 . ASP   A 22  ? 0.3829 0.3123 0.3178 0.0115  0.0107  -0.0924 36  ASP   A OD2 
159  N N   . GLY   A 23  ? 0.2337 0.2053 0.2348 0.0718  0.0064  -0.0765 37  GLY   A N   
160  C CA  . GLY   A 23  ? 0.2105 0.1809 0.2019 0.0730  -0.0129 -0.0558 37  GLY   A CA  
161  C C   . GLY   A 23  ? 0.2063 0.1810 0.1712 0.0642  -0.0044 -0.0476 37  GLY   A C   
162  O O   . GLY   A 23  ? 0.2073 0.1788 0.1532 0.0706  -0.0126 -0.0347 37  GLY   A O   
163  N N   . ALA   A 24  ? 0.1917 0.1839 0.1867 0.0495  -0.0083 -0.0410 38  ALA   A N   
164  C CA  . ALA   A 24  ? 0.1844 0.1760 0.1693 0.0362  -0.0134 -0.0469 38  ALA   A CA  
165  C C   . ALA   A 24  ? 0.1926 0.1555 0.1742 0.0454  0.0063  -0.0193 38  ALA   A C   
166  O O   . ALA   A 24  ? 0.2063 0.1481 0.2350 0.0368  0.0111  -0.0221 38  ALA   A O   
167  C CB  . ALA   A 24  ? 0.2444 0.2064 0.1886 0.0142  -0.0307 -0.0370 38  ALA   A CB  
168  N N   . LEU   A 25  ? 0.1924 0.1429 0.1561 0.0309  0.0054  -0.0161 39  LEU   A N   
169  C CA  . LEU   A 25  ? 0.1852 0.1423 0.1403 0.0141  0.0121  -0.0220 39  LEU   A CA  
170  C C   . LEU   A 25  ? 0.1740 0.1356 0.1396 0.0047  -0.0110 -0.0197 39  LEU   A C   
171  O O   . LEU   A 25  ? 0.1704 0.1408 0.1447 0.0078  -0.0052 -0.0247 39  LEU   A O   
172  C CB  . LEU   A 25  ? 0.1944 0.1387 0.1421 0.0076  -0.0084 -0.0078 39  LEU   A CB  
173  C CG  . LEU   A 25  ? 0.1998 0.1285 0.1453 0.0157  -0.0243 -0.0154 39  LEU   A CG  
174  C CD1 . LEU   A 25  ? 0.1908 0.1382 0.1517 0.0162  -0.0037 -0.0280 39  LEU   A CD1 
175  C CD2 . LEU   A 25  ? 0.2412 0.1246 0.1683 0.0158  -0.0154 -0.0035 39  LEU   A CD2 
176  N N   . THR   A 26  ? 0.1713 0.1447 0.1387 -0.0035 -0.0051 -0.0248 40  THR   A N   
177  C CA  . THR   A 26  ? 0.1747 0.1406 0.1424 -0.0044 -0.0143 -0.0245 40  THR   A CA  
178  C C   . THR   A 26  ? 0.1790 0.1456 0.1588 -0.0086 0.0110  0.0000  40  THR   A C   
179  O O   . THR   A 26  ? 0.2043 0.1617 0.2020 0.0002  0.0041  0.0326  40  THR   A O   
180  C CB  . THR   A 26  ? 0.2185 0.1527 0.1651 -0.0086 -0.0039 -0.0296 40  THR   A CB  
181  O OG1 . THR   A 26  ? 0.2402 0.1608 0.1899 0.0080  0.0020  -0.0420 40  THR   A OG1 
182  C CG2 . THR   A 26  ? 0.2317 0.1740 0.1789 -0.0166 0.0351  -0.0381 40  THR   A CG2 
183  N N   . GLY   A 27  ? 0.1874 0.1436 0.1542 -0.0005 0.0250  -0.0018 41  GLY   A N   
184  C CA  . GLY   A 27  ? 0.1973 0.1303 0.1886 -0.0043 0.0326  0.0093  41  GLY   A CA  
185  C C   . GLY   A 27  ? 0.1876 0.1142 0.1528 -0.0133 0.0162  0.0072  41  GLY   A C   
186  O O   . GLY   A 27  ? 0.1798 0.1169 0.1556 -0.0162 0.0134  -0.0002 41  GLY   A O   
187  N N   . THR   A 28  ? 0.1881 0.1276 0.1560 -0.0144 0.0267  0.0005  42  THR   A N   
188  C CA  . THR   A 28  ? 0.2020 0.1397 0.1738 -0.0081 0.0353  -0.0098 42  THR   A CA  
189  C C   . THR   A 28  ? 0.1892 0.1371 0.1563 -0.0128 0.0209  0.0010  42  THR   A C   
190  O O   . THR   A 28  ? 0.2073 0.1570 0.1651 -0.0042 0.0218  -0.0001 42  THR   A O   
191  C CB  . THR   A 28  ? 0.2287 0.1557 0.1767 -0.0191 0.0355  -0.0049 42  THR   A CB  
192  O OG1 . THR   A 28  ? 0.2347 0.1566 0.2071 -0.0295 0.0386  -0.0016 42  THR   A OG1 
193  C CG2 . THR   A 28  ? 0.2358 0.1829 0.1844 0.0036  0.0380  -0.0102 42  THR   A CG2 
194  N N   . TYR   A 29  ? 0.1774 0.1398 0.1610 -0.0124 0.0259  -0.0106 43  TYR   A N   
195  C CA  . TYR   A 29  ? 0.1769 0.1383 0.1588 -0.0201 0.0147  -0.0269 43  TYR   A CA  
196  C C   . TYR   A 29  ? 0.1671 0.1493 0.1535 -0.0161 0.0220  -0.0043 43  TYR   A C   
197  O O   . TYR   A 29  ? 0.1711 0.1633 0.1749 -0.0203 0.0264  -0.0002 43  TYR   A O   
198  C CB  . TYR   A 29  ? 0.1627 0.1211 0.1670 -0.0270 0.0109  -0.0135 43  TYR   A CB  
199  C CG  . TYR   A 29  ? 0.1775 0.1002 0.1456 -0.0230 0.0062  0.0031  43  TYR   A CG  
200  C CD1 . TYR   A 29  ? 0.1672 0.1072 0.1706 -0.0281 0.0201  0.0005  43  TYR   A CD1 
201  C CD2 . TYR   A 29  ? 0.1804 0.1141 0.1527 -0.0226 0.0032  0.0079  43  TYR   A CD2 
202  C CE1 . TYR   A 29  ? 0.1759 0.1081 0.1690 -0.0201 -0.0083 0.0079  43  TYR   A CE1 
203  C CE2 . TYR   A 29  ? 0.1877 0.1136 0.1584 -0.0172 0.0173  0.0122  43  TYR   A CE2 
204  C CZ  . TYR   A 29  ? 0.1810 0.1149 0.1462 -0.0137 0.0178  0.0203  43  TYR   A CZ  
205  O OH  . TYR   A 29  ? 0.2138 0.1271 0.1533 -0.0052 0.0189  0.0147  43  TYR   A OH  
206  N N   . GLU   A 30  ? 0.1580 0.1517 0.1662 -0.0177 0.0270  -0.0158 44  GLU   A N   
207  C CA  . GLU   A 30  ? 0.1676 0.1637 0.1946 -0.0304 0.0323  -0.0210 44  GLU   A CA  
208  C C   . GLU   A 30  ? 0.1828 0.1642 0.1942 -0.0009 0.0395  -0.0106 44  GLU   A C   
209  O O   . GLU   A 30  ? 0.2214 0.1654 0.1857 -0.0056 0.0480  -0.0051 44  GLU   A O   
210  C CB  . GLU   A 30  ? 0.1709 0.1960 0.2506 -0.0328 0.0308  -0.0120 44  GLU   A CB  
211  C CG  . GLU   A 30  ? 0.2143 0.2373 0.3155 -0.0370 0.0685  -0.0224 44  GLU   A CG  
212  C CD  . GLU   A 30  ? 0.2431 0.2579 0.3909 -0.0392 0.0867  -0.0301 44  GLU   A CD  
213  O OE1 . GLU   A 30  ? 0.2677 0.2670 0.4237 -0.0460 0.0706  -0.0138 44  GLU   A OE1 
214  O OE2 . GLU   A 30  ? 0.2432 0.2766 0.4336 -0.0426 0.0866  -0.0437 44  GLU   A OE2 
215  N N   . SER   A 31  ? 0.1958 0.1577 0.2129 -0.0083 0.0352  -0.0197 45  SER   A N   
216  C CA  . SER   A 31  ? 0.2045 0.1595 0.2493 -0.0081 0.0461  -0.0240 45  SER   A CA  
217  C C   . SER   A 31  ? 0.2218 0.2001 0.2675 -0.0074 0.0573  -0.0312 45  SER   A C   
218  O O   . SER   A 31  ? 0.2331 0.2442 0.3125 -0.0137 0.0481  -0.0357 45  SER   A O   
219  C CB  . SER   A 31  ? 0.2069 0.1428 0.2620 -0.0271 0.0205  -0.0293 45  SER   A CB  
220  O OG  . SER   A 31  ? 0.1831 0.1582 0.2913 -0.0293 0.0330  -0.0366 45  SER   A OG  
221  N N   . ALA   A 32  ? 0.2372 0.2129 0.2732 0.0246  0.0952  -0.0312 46  ALA   A N   
222  C CA  . ALA   A 32  ? 0.3035 0.2421 0.2794 0.0382  0.1210  -0.0192 46  ALA   A CA  
223  C C   . ALA   A 32  ? 0.3053 0.2408 0.2600 0.0401  0.1103  -0.0322 46  ALA   A C   
224  O O   . ALA   A 32  ? 0.3330 0.2663 0.3037 0.0347  0.1129  -0.0194 46  ALA   A O   
225  C CB  . ALA   A 32  ? 0.3503 0.2575 0.3022 0.0578  0.1273  -0.0064 46  ALA   A CB  
226  N N   . VAL   A 33  ? 0.2663 0.2175 0.2529 0.0284  0.0561  -0.0486 47  VAL   A N   
227  C CA  . VAL   A 33  ? 0.2773 0.2154 0.2516 0.0035  0.0402  -0.0544 47  VAL   A CA  
228  C C   . VAL   A 33  ? 0.2297 0.2165 0.2485 0.0084  0.0350  -0.0368 47  VAL   A C   
229  O O   . VAL   A 33  ? 0.2083 0.2127 0.2592 0.0062  0.0180  -0.0369 47  VAL   A O   
230  C CB  . VAL   A 33  ? 0.3136 0.2354 0.2575 -0.0004 0.0240  -0.0453 47  VAL   A CB  
231  C CG1 . VAL   A 33  ? 0.3441 0.2391 0.2617 0.0102  0.0307  -0.0487 47  VAL   A CG1 
232  C CG2 . VAL   A 33  ? 0.3341 0.2446 0.2783 0.0020  -0.0063 -0.0383 47  VAL   A CG2 
233  N N   . GLY   A 34  ? 0.2193 0.2171 0.2299 -0.0132 0.0139  -0.0292 48  GLY   A N   
234  C CA  . GLY   A 34  ? 0.2308 0.2351 0.2235 -0.0202 0.0083  -0.0214 48  GLY   A CA  
235  C C   . GLY   A 34  ? 0.2083 0.2445 0.2227 -0.0080 0.0089  -0.0166 48  GLY   A C   
236  O O   . GLY   A 34  ? 0.2007 0.2716 0.2448 0.0097  0.0262  -0.0182 48  GLY   A O   
237  N N   . ASN   A 35  ? 0.2470 0.2496 0.2324 0.0284  0.0079  -0.0201 49  ASN   A N   
238  C CA  . ASN   A 35  ? 0.2716 0.2398 0.2492 0.0370  -0.0028 -0.0163 49  ASN   A CA  
239  C C   . ASN   A 35  ? 0.2776 0.2308 0.2488 0.0241  0.0233  -0.0212 49  ASN   A C   
240  O O   . ASN   A 35  ? 0.3037 0.2327 0.2410 0.0168  0.0350  -0.0235 49  ASN   A O   
241  C CB  . ASN   A 35  ? 0.3383 0.2515 0.2852 0.0486  0.0107  0.0127  49  ASN   A CB  
242  C CG  . ASN   A 35  ? 0.3804 0.2651 0.3211 0.0530  0.0275  0.0246  49  ASN   A CG  
243  O OD1 . ASN   A 35  ? 0.4265 0.2776 0.3364 0.0505  0.0006  0.0219  49  ASN   A OD1 
244  N ND2 . ASN   A 35  ? 0.3891 0.2780 0.3461 0.0575  0.0488  0.0387  49  ASN   A ND2 
245  N N   . ALA   A 36  ? 0.2503 0.2267 0.2926 0.0109  0.0065  -0.0199 50  ALA   A N   
246  C CA  . ALA   A 36  ? 0.2207 0.2091 0.2765 0.0140  -0.0068 -0.0440 50  ALA   A CA  
247  C C   . ALA   A 36  ? 0.1993 0.2168 0.2499 0.0026  -0.0092 -0.0482 50  ALA   A C   
248  O O   . ALA   A 36  ? 0.2375 0.2308 0.2458 0.0079  0.0318  -0.0447 50  ALA   A O   
249  C CB  . ALA   A 36  ? 0.2356 0.1913 0.2990 0.0312  -0.0063 -0.0528 50  ALA   A CB  
250  N N   . GLU   A 37  ? 0.1702 0.2065 0.2533 -0.0248 -0.0343 -0.0525 51  GLU   A N   
251  C CA  . GLU   A 37  ? 0.1617 0.2228 0.2538 -0.0149 -0.0126 -0.0417 51  GLU   A CA  
252  C C   . GLU   A 37  ? 0.1724 0.2091 0.2460 -0.0241 0.0083  -0.0374 51  GLU   A C   
253  O O   . GLU   A 37  ? 0.1721 0.2071 0.2308 -0.0248 0.0273  -0.0289 51  GLU   A O   
254  C CB  . GLU   A 37  ? 0.1725 0.2598 0.2999 0.0013  -0.0322 -0.0388 51  GLU   A CB  
255  C CG  . GLU   A 37  ? 0.2137 0.2958 0.3274 0.0081  -0.0494 -0.0314 51  GLU   A CG  
256  C CD  . GLU   A 37  ? 0.2293 0.3142 0.3040 0.0095  -0.0349 -0.0228 51  GLU   A CD  
257  O OE1 . GLU   A 37  ? 0.2238 0.3262 0.2817 -0.0005 -0.0314 -0.0145 51  GLU   A OE1 
258  O OE2 . GLU   A 37  ? 0.2440 0.3260 0.3114 0.0081  -0.0706 -0.0250 51  GLU   A OE2 
259  N N   . SER   A 38  ? 0.1721 0.2042 0.2725 -0.0088 0.0558  -0.0110 52  SER   A N   
260  C CA  . SER   A 38  ? 0.1750 0.2057 0.3188 -0.0181 0.0563  -0.0349 52  SER   A CA  
261  C C   . SER   A 38  ? 0.1622 0.1899 0.2760 -0.0187 0.0404  -0.0103 52  SER   A C   
262  O O   . SER   A 38  ? 0.1830 0.1885 0.2688 -0.0120 0.0470  -0.0034 52  SER   A O   
263  C CB  . SER   A 38  ? 0.2113 0.2126 0.4095 -0.0152 0.0305  -0.0895 52  SER   A CB  
264  O OG  . SER   A 38  ? 0.2279 0.2252 0.4865 -0.0179 0.0048  -0.1179 52  SER   A OG  
265  N N   . ARG   A 39  ? 0.1912 0.1928 0.2403 -0.0291 0.0470  -0.0068 53  ARG   A N   
266  C CA  . ARG   A 39  ? 0.1927 0.1635 0.2251 -0.0196 0.0489  -0.0025 53  ARG   A CA  
267  C C   . ARG   A 39  ? 0.1554 0.1580 0.1843 -0.0384 0.0120  0.0042  53  ARG   A C   
268  O O   . ARG   A 39  ? 0.1609 0.1757 0.2018 -0.0350 0.0022  0.0081  53  ARG   A O   
269  C CB  . ARG   A 39  ? 0.2213 0.1578 0.2526 -0.0198 0.0526  -0.0019 53  ARG   A CB  
270  C CG  . ARG   A 39  ? 0.2664 0.1768 0.2726 -0.0383 0.0625  0.0071  53  ARG   A CG  
271  C CD  . ARG   A 39  ? 0.3219 0.1916 0.2963 -0.0565 0.0611  0.0130  53  ARG   A CD  
272  N NE  . ARG   A 39  ? 0.3916 0.2181 0.3296 -0.0687 0.0643  0.0094  53  ARG   A NE  
273  C CZ  . ARG   A 39  ? 0.4389 0.2352 0.3402 -0.0754 0.0638  0.0111  53  ARG   A CZ  
274  N NH1 . ARG   A 39  ? 0.4735 0.2574 0.3563 -0.0663 0.0511  0.0080  53  ARG   A NH1 
275  N NH2 . ARG   A 39  ? 0.4533 0.2432 0.3558 -0.0859 0.0745  0.0242  53  ARG   A NH2 
276  N N   . TYR   A 40  ? 0.1388 0.1481 0.1874 -0.0262 0.0080  0.0046  54  TYR   A N   
277  C CA  . TYR   A 40  ? 0.1461 0.1308 0.1723 -0.0254 0.0143  0.0003  54  TYR   A CA  
278  C C   . TYR   A 40  ? 0.1377 0.1293 0.1602 -0.0100 0.0060  0.0128  54  TYR   A C   
279  O O   . TYR   A 40  ? 0.1613 0.1431 0.1776 -0.0052 0.0155  0.0072  54  TYR   A O   
280  C CB  . TYR   A 40  ? 0.1568 0.1294 0.1754 -0.0270 0.0045  0.0009  54  TYR   A CB  
281  C CG  . TYR   A 40  ? 0.1367 0.1261 0.1756 -0.0145 0.0047  -0.0069 54  TYR   A CG  
282  C CD1 . TYR   A 40  ? 0.1492 0.1259 0.1776 -0.0160 0.0014  -0.0058 54  TYR   A CD1 
283  C CD2 . TYR   A 40  ? 0.1524 0.1289 0.1759 -0.0125 -0.0104 -0.0081 54  TYR   A CD2 
284  C CE1 . TYR   A 40  ? 0.1570 0.1286 0.1846 -0.0085 -0.0010 -0.0084 54  TYR   A CE1 
285  C CE2 . TYR   A 40  ? 0.1387 0.1232 0.1958 -0.0105 -0.0148 -0.0108 54  TYR   A CE2 
286  C CZ  . TYR   A 40  ? 0.1571 0.1330 0.2092 -0.0047 0.0082  -0.0181 54  TYR   A CZ  
287  O OH  . TYR   A 40  ? 0.1582 0.1594 0.2298 -0.0089 0.0265  -0.0088 54  TYR   A OH  
288  N N   . VAL   A 41  ? 0.1245 0.1319 0.1642 -0.0186 0.0148  -0.0027 55  VAL   A N   
289  C CA  . VAL   A 41  ? 0.1277 0.1398 0.1633 -0.0125 0.0028  -0.0135 55  VAL   A CA  
290  C C   . VAL   A 41  ? 0.1373 0.1310 0.1494 -0.0037 0.0028  -0.0082 55  VAL   A C   
291  O O   . VAL   A 41  ? 0.1330 0.1205 0.1673 -0.0116 0.0131  -0.0029 55  VAL   A O   
292  C CB  . VAL   A 41  ? 0.1561 0.1603 0.1642 -0.0177 0.0013  -0.0165 55  VAL   A CB  
293  C CG1 . VAL   A 41  ? 0.1577 0.1766 0.1621 -0.0290 0.0091  -0.0178 55  VAL   A CG1 
294  C CG2 . VAL   A 41  ? 0.1855 0.1728 0.1664 -0.0412 -0.0143 -0.0441 55  VAL   A CG2 
295  N N   . LEU   A 42  ? 0.1295 0.1403 0.1463 0.0059  -0.0093 -0.0032 56  LEU   A N   
296  C CA  . LEU   A 42  ? 0.1575 0.1381 0.1385 0.0066  -0.0024 -0.0236 56  LEU   A CA  
297  C C   . LEU   A 42  ? 0.1414 0.1337 0.1403 0.0044  -0.0021 -0.0220 56  LEU   A C   
298  O O   . LEU   A 42  ? 0.1622 0.1322 0.1465 0.0034  0.0092  -0.0262 56  LEU   A O   
299  C CB  . LEU   A 42  ? 0.1744 0.1395 0.1509 0.0153  0.0090  -0.0051 56  LEU   A CB  
300  C CG  . LEU   A 42  ? 0.1783 0.1338 0.1532 -0.0193 0.0056  0.0076  56  LEU   A CG  
301  C CD1 . LEU   A 42  ? 0.1691 0.1346 0.1641 0.0139  -0.0147 -0.0234 56  LEU   A CD1 
302  C CD2 . LEU   A 42  ? 0.2148 0.1599 0.1770 -0.0064 0.0213  0.0146  56  LEU   A CD2 
303  N N   . THR   A 43  ? 0.1302 0.1405 0.1502 -0.0076 -0.0071 -0.0133 57  THR   A N   
304  C CA  A THR   A 43  ? 0.1279 0.1385 0.1379 -0.0054 -0.0042 -0.0090 57  THR   A CA  
305  C CA  B THR   A 43  ? 0.1341 0.1386 0.1380 0.0082  0.0004  0.0005  57  THR   A CA  
306  C C   . THR   A 43  ? 0.1287 0.1326 0.1244 0.0048  0.0061  -0.0050 57  THR   A C   
307  O O   . THR   A 43  ? 0.1337 0.1261 0.1271 0.0138  0.0050  -0.0115 57  THR   A O   
308  C CB  A THR   A 43  ? 0.1341 0.1458 0.1348 -0.0245 -0.0086 -0.0141 57  THR   A CB  
309  C CB  B THR   A 43  ? 0.1621 0.1505 0.1420 -0.0169 -0.0155 0.0065  57  THR   A CB  
310  O OG1 A THR   A 43  ? 0.1490 0.1552 0.1415 -0.0311 0.0021  -0.0153 57  THR   A OG1 
311  O OG1 B THR   A 43  ? 0.1701 0.1696 0.1623 -0.0005 0.0109  0.0054  57  THR   A OG1 
312  C CG2 A THR   A 43  ? 0.1387 0.1521 0.1343 -0.0274 -0.0039 -0.0176 57  THR   A CG2 
313  C CG2 B THR   A 43  ? 0.2138 0.1636 0.1597 -0.0234 -0.0082 0.0006  57  THR   A CG2 
314  N N   . GLY   A 44  ? 0.1356 0.1338 0.1491 0.0119  -0.0095 -0.0179 58  GLY   A N   
315  C CA  . GLY   A 44  ? 0.1291 0.1451 0.1380 0.0130  -0.0229 -0.0088 58  GLY   A CA  
316  C C   . GLY   A 44  ? 0.1514 0.1404 0.1157 0.0258  -0.0051 -0.0160 58  GLY   A C   
317  O O   . GLY   A 44  ? 0.1613 0.1409 0.1392 0.0185  0.0085  -0.0222 58  GLY   A O   
318  N N   . ARG   A 45  ? 0.1313 0.1368 0.1320 0.0338  -0.0109 -0.0110 59  ARG   A N   
319  C CA  . ARG   A 45  ? 0.1461 0.1527 0.1371 0.0384  -0.0095 -0.0162 59  ARG   A CA  
320  C C   . ARG   A 45  ? 0.1487 0.1431 0.1283 0.0353  -0.0205 -0.0135 59  ARG   A C   
321  O O   . ARG   A 45  ? 0.1740 0.1468 0.1357 0.0270  -0.0058 -0.0180 59  ARG   A O   
322  C CB  . ARG   A 45  ? 0.1570 0.1785 0.1386 0.0347  0.0027  -0.0165 59  ARG   A CB  
323  C CG  . ARG   A 45  ? 0.1937 0.2016 0.1347 0.0313  0.0191  -0.0120 59  ARG   A CG  
324  C CD  . ARG   A 45  ? 0.1890 0.2265 0.1619 0.0512  0.0090  -0.0194 59  ARG   A CD  
325  N NE  . ARG   A 45  ? 0.1535 0.2380 0.1502 0.0549  -0.0016 -0.0287 59  ARG   A NE  
326  C CZ  . ARG   A 45  ? 0.1722 0.2495 0.1612 0.0382  0.0143  -0.0472 59  ARG   A CZ  
327  N NH1 . ARG   A 45  ? 0.1766 0.2603 0.1513 0.0133  0.0201  -0.0480 59  ARG   A NH1 
328  N NH2 . ARG   A 45  ? 0.1872 0.2419 0.1826 0.0620  0.0362  -0.0439 59  ARG   A NH2 
329  N N   . TYR   A 46  ? 0.1816 0.1528 0.1394 0.0491  -0.0176 -0.0106 60  TYR   A N   
330  C CA  . TYR   A 46  ? 0.1794 0.1434 0.1543 0.0449  -0.0298 -0.0125 60  TYR   A CA  
331  C C   . TYR   A 46  ? 0.1920 0.1496 0.1366 0.0659  -0.0383 -0.0177 60  TYR   A C   
332  O O   . TYR   A 46  ? 0.2166 0.1588 0.1515 0.0678  -0.0099 -0.0324 60  TYR   A O   
333  C CB  . TYR   A 46  ? 0.2015 0.1441 0.1866 0.0293  -0.0133 -0.0227 60  TYR   A CB  
334  C CG  . TYR   A 46  ? 0.1865 0.1423 0.1948 0.0276  -0.0214 -0.0108 60  TYR   A CG  
335  C CD1 . TYR   A 46  ? 0.2074 0.1396 0.1942 0.0132  -0.0091 -0.0228 60  TYR   A CD1 
336  C CD2 . TYR   A 46  ? 0.2148 0.1556 0.2288 0.0222  -0.0349 -0.0076 60  TYR   A CD2 
337  C CE1 . TYR   A 46  ? 0.2377 0.1528 0.2327 0.0299  -0.0097 -0.0313 60  TYR   A CE1 
338  C CE2 . TYR   A 46  ? 0.2236 0.1676 0.2500 0.0205  -0.0465 -0.0276 60  TYR   A CE2 
339  C CZ  . TYR   A 46  ? 0.2415 0.1509 0.2468 0.0407  -0.0325 -0.0422 60  TYR   A CZ  
340  O OH  . TYR   A 46  ? 0.2649 0.1538 0.3150 0.0629  -0.0325 -0.0446 60  TYR   A OH  
341  N N   . ASP   A 47  ? 0.1950 0.1595 0.1672 0.0743  -0.0322 -0.0178 61  ASP   A N   
342  C CA  . ASP   A 47  ? 0.2039 0.1660 0.1765 0.0789  -0.0529 -0.0190 61  ASP   A CA  
343  C C   . ASP   A 47  ? 0.2364 0.1754 0.1789 0.0838  -0.0320 -0.0377 61  ASP   A C   
344  O O   . ASP   A 47  ? 0.2364 0.1845 0.1887 0.0591  -0.0281 -0.0271 61  ASP   A O   
345  C CB  . ASP   A 47  ? 0.1920 0.1824 0.1803 0.0670  -0.0413 -0.0257 61  ASP   A CB  
346  C CG  . ASP   A 47  ? 0.2156 0.1869 0.1786 0.0823  -0.0389 -0.0478 61  ASP   A CG  
347  O OD1 . ASP   A 47  ? 0.2265 0.1882 0.1892 0.0817  -0.0115 -0.0283 61  ASP   A OD1 
348  O OD2 . ASP   A 47  ? 0.2099 0.2017 0.2135 0.0889  -0.0352 -0.0522 61  ASP   A OD2 
349  N N   . SER   A 48  ? 0.2694 0.1791 0.1921 0.0742  -0.0388 -0.0707 62  SER   A N   
350  C CA  . SER   A 48  ? 0.2843 0.1979 0.2125 0.0817  -0.0374 -0.0616 62  SER   A CA  
351  C C   . SER   A 48  ? 0.2818 0.2024 0.2474 0.0921  -0.0266 -0.0498 62  SER   A C   
352  O O   . SER   A 48  ? 0.2830 0.2002 0.2795 0.0874  -0.0089 -0.0588 62  SER   A O   
353  C CB  . SER   A 48  ? 0.3403 0.2266 0.1979 0.0537  -0.0175 -0.0535 62  SER   A CB  
354  O OG  . SER   A 48  ? 0.4055 0.2464 0.2028 0.0256  0.0076  -0.0421 62  SER   A OG  
355  N N   . ALA   A 49  ? 0.2713 0.2013 0.2329 0.1117  -0.0225 -0.0280 63  ALA   A N   
356  C CA  . ALA   A 49  ? 0.2831 0.2222 0.2263 0.1205  -0.0154 -0.0158 63  ALA   A CA  
357  C C   . ALA   A 49  ? 0.2805 0.2277 0.2346 0.1178  -0.0183 -0.0084 63  ALA   A C   
358  O O   . ALA   A 49  ? 0.2733 0.2336 0.2430 0.1259  -0.0327 -0.0065 63  ALA   A O   
359  C CB  . ALA   A 49  ? 0.2959 0.2374 0.2532 0.1143  -0.0007 -0.0098 63  ALA   A CB  
360  N N   . PRO   A 50  ? 0.2728 0.2245 0.2364 0.1167  -0.0041 -0.0120 64  PRO   A N   
361  C CA  . PRO   A 50  ? 0.2828 0.2396 0.2261 0.1179  -0.0080 -0.0123 64  PRO   A CA  
362  C C   . PRO   A 50  ? 0.2859 0.2580 0.2353 0.1369  -0.0106 -0.0090 64  PRO   A C   
363  O O   . PRO   A 50  ? 0.3040 0.2572 0.2435 0.1456  -0.0094 -0.0127 64  PRO   A O   
364  C CB  . PRO   A 50  ? 0.3093 0.2412 0.2640 0.1098  0.0040  -0.0064 64  PRO   A CB  
365  C CG  . PRO   A 50  ? 0.3144 0.2364 0.2646 0.0960  0.0141  -0.0044 64  PRO   A CG  
366  C CD  . PRO   A 50  ? 0.2977 0.2294 0.2607 0.1048  0.0068  0.0009  64  PRO   A CD  
367  N N   . ALA   A 51  ? 0.2790 0.2861 0.2204 0.1337  -0.0207 0.0073  65  ALA   A N   
368  C CA  . ALA   A 51  ? 0.2925 0.3002 0.2412 0.1277  -0.0243 0.0111  65  ALA   A CA  
369  C C   . ALA   A 51  ? 0.3080 0.3047 0.2715 0.1477  -0.0202 0.0375  65  ALA   A C   
370  O O   . ALA   A 51  ? 0.3483 0.3057 0.2724 0.1393  -0.0015 0.0404  65  ALA   A O   
371  C CB  . ALA   A 51  ? 0.3032 0.3045 0.2352 0.1026  -0.0567 -0.0110 65  ALA   A CB  
372  N N   . THR   A 52  ? 0.2993 0.3270 0.2939 0.1571  -0.0319 0.0505  66  THR   A N   
373  C CA  . THR   A 52  ? 0.3446 0.3497 0.3219 0.1588  -0.0364 0.0681  66  THR   A CA  
374  C C   . THR   A 52  ? 0.3562 0.3661 0.3405 0.1528  -0.0507 0.0736  66  THR   A C   
375  O O   . THR   A 52  ? 0.3907 0.3679 0.3738 0.1504  -0.0373 0.0781  66  THR   A O   
376  C CB  . THR   A 52  ? 0.3697 0.3669 0.3468 0.1483  -0.0269 0.0634  66  THR   A CB  
377  O OG1 . THR   A 52  ? 0.3669 0.3759 0.3551 0.1588  -0.0418 0.0746  66  THR   A OG1 
378  C CG2 . THR   A 52  ? 0.3806 0.3693 0.3521 0.1398  -0.0205 0.0549  66  THR   A CG2 
379  N N   . ASP   A 53  ? 0.3623 0.3763 0.3161 0.1484  -0.0515 0.0744  67  ASP   A N   
380  C CA  . ASP   A 53  ? 0.3582 0.3928 0.3002 0.1307  -0.0696 0.0655  67  ASP   A CA  
381  C C   . ASP   A 53  ? 0.3530 0.3987 0.3012 0.1203  -0.0562 0.0500  67  ASP   A C   
382  O O   . ASP   A 53  ? 0.3540 0.4209 0.3177 0.1016  -0.0568 0.0286  67  ASP   A O   
383  C CB  . ASP   A 53  ? 0.3688 0.4045 0.3019 0.1079  -0.0868 0.0663  67  ASP   A CB  
384  C CG  . ASP   A 53  ? 0.3891 0.4189 0.3172 0.0733  -0.0732 0.0531  67  ASP   A CG  
385  O OD1 . ASP   A 53  ? 0.3536 0.4244 0.2746 0.0649  -0.0749 0.0479  67  ASP   A OD1 
386  O OD2 . ASP   A 53  ? 0.4121 0.4278 0.3562 0.0589  -0.0734 0.0454  67  ASP   A OD2 
387  N N   . GLY   A 54  ? 0.3547 0.3736 0.2805 0.1263  -0.0372 0.0576  68  GLY   A N   
388  C CA  . GLY   A 54  ? 0.3481 0.3492 0.2414 0.1329  -0.0288 0.0711  68  GLY   A CA  
389  C C   . GLY   A 54  ? 0.3503 0.3302 0.2318 0.1420  -0.0045 0.0581  68  GLY   A C   
390  O O   . GLY   A 54  ? 0.3745 0.3356 0.2688 0.1353  0.0308  0.0516  68  GLY   A O   
391  N N   . SER   A 55  ? 0.3447 0.3132 0.1734 0.1221  -0.0500 0.0451  69  SER   A N   
392  C CA  . SER   A 55  ? 0.3106 0.2912 0.1773 0.1079  -0.0666 0.0246  69  SER   A CA  
393  C C   . SER   A 55  ? 0.3072 0.2524 0.1744 0.1181  -0.0539 0.0178  69  SER   A C   
394  O O   . SER   A 55  ? 0.3060 0.2438 0.2145 0.1187  -0.0396 0.0049  69  SER   A O   
395  C CB  . SER   A 55  ? 0.3299 0.3158 0.2208 0.0675  -0.0798 0.0219  69  SER   A CB  
396  O OG  . SER   A 55  ? 0.3461 0.3362 0.2573 0.0402  -0.0659 0.0009  69  SER   A OG  
397  N N   . GLY   A 56  ? 0.3185 0.2332 0.1705 0.1230  -0.0443 0.0125  70  GLY   A N   
398  C CA  . GLY   A 56  ? 0.3213 0.2164 0.1599 0.1106  -0.0458 0.0080  70  GLY   A CA  
399  C C   . GLY   A 56  ? 0.2964 0.1997 0.1602 0.1038  -0.0367 0.0094  70  GLY   A C   
400  O O   . GLY   A 56  ? 0.2563 0.2105 0.1657 0.0868  -0.0457 -0.0077 70  GLY   A O   
401  N N   . THR   A 57  ? 0.2850 0.1869 0.1466 0.1097  -0.0459 -0.0075 71  THR   A N   
402  C CA  . THR   A 57  ? 0.2780 0.1735 0.1368 0.0983  -0.0352 -0.0144 71  THR   A CA  
403  C C   . THR   A 57  ? 0.2643 0.1652 0.1457 0.0882  -0.0275 -0.0194 71  THR   A C   
404  O O   . THR   A 57  ? 0.2501 0.1660 0.1387 0.0798  -0.0172 -0.0169 71  THR   A O   
405  C CB  . THR   A 57  ? 0.2884 0.1720 0.1365 0.0976  -0.0259 -0.0067 71  THR   A CB  
406  O OG1 . THR   A 57  ? 0.3042 0.1676 0.1658 0.0998  -0.0279 -0.0006 71  THR   A OG1 
407  C CG2 . THR   A 57  ? 0.3106 0.1839 0.1314 0.0886  -0.0433 -0.0065 71  THR   A CG2 
408  N N   . ALA   A 58  ? 0.2438 0.1681 0.1306 0.0821  -0.0379 -0.0238 72  ALA   A N   
409  C CA  . ALA   A 58  ? 0.2214 0.1610 0.1388 0.0781  -0.0317 0.0032  72  ALA   A CA  
410  C C   . ALA   A 58  ? 0.2350 0.1547 0.1427 0.0782  -0.0268 -0.0168 72  ALA   A C   
411  O O   . ALA   A 58  ? 0.2531 0.1600 0.1491 0.0783  -0.0237 -0.0222 72  ALA   A O   
412  C CB  . ALA   A 58  ? 0.2112 0.1667 0.1669 0.0873  -0.0360 -0.0032 72  ALA   A CB  
413  N N   . LEU   A 59  ? 0.1980 0.1534 0.1433 0.0788  -0.0381 -0.0142 73  LEU   A N   
414  C CA  A LEU   A 59  ? 0.2087 0.1471 0.1377 0.0575  -0.0315 0.0014  73  LEU   A CA  
415  C CA  B LEU   A 59  ? 0.2137 0.1465 0.1324 0.0498  -0.0327 -0.0039 73  LEU   A CA  
416  C C   . LEU   A 59  ? 0.1991 0.1421 0.1204 0.0497  -0.0339 -0.0057 73  LEU   A C   
417  O O   . LEU   A 59  ? 0.2290 0.1599 0.1366 0.0613  -0.0413 -0.0314 73  LEU   A O   
418  C CB  A LEU   A 59  ? 0.2339 0.1460 0.1516 0.0624  -0.0016 0.0186  73  LEU   A CB  
419  C CB  B LEU   A 59  ? 0.2515 0.1435 0.1352 0.0419  0.0022  0.0049  73  LEU   A CB  
420  C CG  A LEU   A 59  ? 0.2584 0.1500 0.1771 0.0563  0.0021  0.0289  73  LEU   A CG  
421  C CG  B LEU   A 59  ? 0.2854 0.1444 0.1533 0.0291  0.0205  0.0122  73  LEU   A CG  
422  C CD1 A LEU   A 59  ? 0.2504 0.1570 0.2249 0.0448  0.0094  0.0265  73  LEU   A CD1 
423  C CD1 B LEU   A 59  ? 0.3028 0.1476 0.1712 0.0215  0.0084  0.0112  73  LEU   A CD1 
424  C CD2 A LEU   A 59  ? 0.2662 0.1483 0.1879 0.0411  0.0123  0.0480  73  LEU   A CD2 
425  C CD2 B LEU   A 59  ? 0.2959 0.1514 0.1572 0.0350  0.0197  0.0090  73  LEU   A CD2 
426  N N   . GLY   A 60  ? 0.1530 0.1333 0.1334 0.0398  -0.0123 -0.0055 74  GLY   A N   
427  C CA  . GLY   A 60  ? 0.1529 0.1228 0.1305 0.0282  -0.0143 -0.0103 74  GLY   A CA  
428  C C   . GLY   A 60  ? 0.1487 0.1131 0.1235 0.0337  0.0040  -0.0051 74  GLY   A C   
429  O O   . GLY   A 60  ? 0.1661 0.1214 0.1351 0.0389  0.0119  -0.0144 74  GLY   A O   
430  N N   . TRP   A 61  ? 0.1496 0.1144 0.1279 0.0164  0.0026  0.0023  75  TRP   A N   
431  C CA  . TRP   A 61  ? 0.1379 0.1009 0.1130 0.0152  -0.0219 -0.0066 75  TRP   A CA  
432  C C   . TRP   A 61  ? 0.1468 0.1129 0.1009 0.0037  0.0120  -0.0013 75  TRP   A C   
433  O O   . TRP   A 61  ? 0.1646 0.1307 0.1065 0.0185  -0.0036 -0.0014 75  TRP   A O   
434  C CB  . TRP   A 61  ? 0.1503 0.1091 0.1330 0.0120  -0.0099 -0.0222 75  TRP   A CB  
435  C CG  . TRP   A 61  ? 0.1542 0.1172 0.1279 0.0017  0.0102  -0.0111 75  TRP   A CG  
436  C CD1 . TRP   A 61  ? 0.1696 0.1146 0.1152 -0.0050 0.0138  -0.0220 75  TRP   A CD1 
437  C CD2 . TRP   A 61  ? 0.1695 0.1112 0.1276 0.0089  0.0088  -0.0060 75  TRP   A CD2 
438  N NE1 . TRP   A 61  ? 0.1975 0.1084 0.1317 0.0069  0.0295  -0.0115 75  TRP   A NE1 
439  C CE2 . TRP   A 61  ? 0.1814 0.1079 0.1402 -0.0022 0.0214  -0.0071 75  TRP   A CE2 
440  C CE3 . TRP   A 61  ? 0.2073 0.1133 0.1182 0.0132  -0.0017 -0.0061 75  TRP   A CE3 
441  C CZ2 . TRP   A 61  ? 0.2286 0.1054 0.1537 -0.0137 0.0130  0.0099  75  TRP   A CZ2 
442  C CZ3 . TRP   A 61  ? 0.2273 0.1221 0.1333 -0.0058 0.0013  0.0021  75  TRP   A CZ3 
443  C CH2 . TRP   A 61  ? 0.2409 0.1078 0.1310 -0.0186 0.0117  0.0123  75  TRP   A CH2 
444  N N   . THR   A 62  ? 0.1314 0.1174 0.1030 0.0096  0.0026  0.0068  76  THR   A N   
445  C CA  . THR   A 62  ? 0.1194 0.1096 0.1144 0.0135  0.0091  0.0051  76  THR   A CA  
446  C C   . THR   A 62  ? 0.1211 0.1123 0.1132 0.0059  -0.0056 -0.0172 76  THR   A C   
447  O O   . THR   A 62  ? 0.1518 0.1221 0.1252 0.0009  -0.0026 -0.0127 76  THR   A O   
448  C CB  . THR   A 62  ? 0.1285 0.1235 0.1155 0.0022  0.0136  0.0041  76  THR   A CB  
449  O OG1 . THR   A 62  ? 0.1094 0.1344 0.1270 -0.0035 -0.0072 0.0063  76  THR   A OG1 
450  C CG2 . THR   A 62  ? 0.1259 0.1344 0.1308 0.0022  0.0068  -0.0002 76  THR   A CG2 
451  N N   . VAL   A 63  ? 0.1145 0.1107 0.1313 0.0051  0.0065  -0.0006 77  VAL   A N   
452  C CA  . VAL   A 63  ? 0.1253 0.1250 0.1303 0.0030  -0.0024 0.0100  77  VAL   A CA  
453  C C   . VAL   A 63  ? 0.1124 0.1213 0.1227 -0.0070 -0.0078 -0.0021 77  VAL   A C   
454  O O   . VAL   A 63  ? 0.1357 0.1325 0.1395 -0.0011 -0.0133 -0.0166 77  VAL   A O   
455  C CB  . VAL   A 63  ? 0.1223 0.1325 0.1465 -0.0093 0.0075  -0.0059 77  VAL   A CB  
456  C CG1 . VAL   A 63  ? 0.1244 0.1504 0.1669 -0.0215 0.0065  -0.0161 77  VAL   A CG1 
457  C CG2 . VAL   A 63  ? 0.1507 0.1262 0.1599 -0.0109 0.0171  0.0070  77  VAL   A CG2 
458  N N   . ALA   A 64  ? 0.1120 0.1209 0.1296 0.0057  -0.0092 0.0007  78  ALA   A N   
459  C CA  . ALA   A 64  ? 0.1083 0.1282 0.1286 -0.0025 -0.0060 0.0040  78  ALA   A CA  
460  C C   . ALA   A 64  ? 0.1232 0.1376 0.1439 0.0164  -0.0105 -0.0098 78  ALA   A C   
461  O O   . ALA   A 64  ? 0.1469 0.1228 0.1568 -0.0106 -0.0148 -0.0246 78  ALA   A O   
462  C CB  . ALA   A 64  ? 0.1421 0.1459 0.1431 0.0016  -0.0187 0.0020  78  ALA   A CB  
463  N N   . TRP   A 65  ? 0.1198 0.1419 0.1523 0.0025  0.0020  0.0017  79  TRP   A N   
464  C CA  . TRP   A 65  ? 0.1290 0.1311 0.1471 -0.0014 0.0012  -0.0068 79  TRP   A CA  
465  C C   . TRP   A 65  ? 0.1289 0.1302 0.1517 -0.0067 0.0056  -0.0093 79  TRP   A C   
466  O O   . TRP   A 65  ? 0.1273 0.1453 0.1595 -0.0063 -0.0017 -0.0020 79  TRP   A O   
467  C CB  . TRP   A 65  ? 0.1577 0.1210 0.1472 0.0045  -0.0148 0.0044  79  TRP   A CB  
468  C CG  . TRP   A 65  ? 0.1480 0.1178 0.1348 -0.0015 0.0014  0.0058  79  TRP   A CG  
469  C CD1 . TRP   A 65  ? 0.1435 0.1240 0.1248 0.0029  -0.0006 0.0070  79  TRP   A CD1 
470  C CD2 . TRP   A 65  ? 0.1382 0.1173 0.1453 0.0035  0.0076  0.0073  79  TRP   A CD2 
471  N NE1 . TRP   A 65  ? 0.1327 0.1153 0.1371 0.0009  0.0042  0.0168  79  TRP   A NE1 
472  C CE2 . TRP   A 65  ? 0.1361 0.1155 0.1375 -0.0016 0.0016  0.0196  79  TRP   A CE2 
473  C CE3 . TRP   A 65  ? 0.1629 0.1297 0.1535 -0.0017 0.0128  0.0195  79  TRP   A CE3 
474  C CZ2 . TRP   A 65  ? 0.1415 0.1215 0.1528 -0.0191 -0.0014 0.0071  79  TRP   A CZ2 
475  C CZ3 . TRP   A 65  ? 0.1765 0.1344 0.1635 -0.0105 -0.0021 0.0233  79  TRP   A CZ3 
476  C CH2 . TRP   A 65  ? 0.1619 0.1313 0.1659 -0.0167 0.0017  0.0073  79  TRP   A CH2 
477  N N   . LYS   A 66  ? 0.1393 0.1423 0.1480 -0.0213 0.0064  -0.0143 80  LYS   A N   
478  C CA  . LYS   A 66  ? 0.1292 0.1461 0.1366 -0.0252 -0.0049 -0.0032 80  LYS   A CA  
479  C C   . LYS   A 66  ? 0.1224 0.1459 0.1493 -0.0221 0.0017  -0.0005 80  LYS   A C   
480  O O   . LYS   A 66  ? 0.1188 0.1517 0.1736 -0.0218 0.0038  0.0001  80  LYS   A O   
481  C CB  . LYS   A 66  ? 0.1403 0.1741 0.1410 -0.0206 -0.0072 0.0074  80  LYS   A CB  
482  C CG  . LYS   A 66  ? 0.1465 0.2049 0.1436 -0.0254 -0.0161 0.0191  80  LYS   A CG  
483  C CD  . LYS   A 66  ? 0.1856 0.2327 0.1571 -0.0213 -0.0211 -0.0006 80  LYS   A CD  
484  C CE  . LYS   A 66  ? 0.2295 0.2480 0.1798 -0.0357 -0.0111 -0.0295 80  LYS   A CE  
485  N NZ  . LYS   A 66  ? 0.2689 0.2642 0.2066 -0.0297 0.0049  -0.0519 80  LYS   A NZ  
486  N N   . ASN   A 67  ? 0.1386 0.1444 0.1515 -0.0172 0.0043  -0.0001 81  ASN   A N   
487  C CA  . ASN   A 67  ? 0.1350 0.1609 0.1650 -0.0152 -0.0025 -0.0079 81  ASN   A CA  
488  C C   . ASN   A 67  ? 0.1223 0.1778 0.1726 -0.0108 0.0003  -0.0302 81  ASN   A C   
489  O O   . ASN   A 67  ? 0.1380 0.1804 0.1919 -0.0052 -0.0189 -0.0118 81  ASN   A O   
490  C CB  . ASN   A 67  ? 0.1566 0.1677 0.1763 -0.0059 0.0177  0.0072  81  ASN   A CB  
491  C CG  . ASN   A 67  ? 0.1491 0.1650 0.1774 -0.0222 -0.0261 -0.0066 81  ASN   A CG  
492  O OD1 . ASN   A 67  ? 0.1552 0.1663 0.1780 -0.0141 -0.0128 -0.0095 81  ASN   A OD1 
493  N ND2 . ASN   A 67  ? 0.1675 0.1768 0.2070 -0.0471 -0.0101 -0.0117 81  ASN   A ND2 
494  N N   . ASN   A 68  ? 0.1217 0.2044 0.2049 -0.0357 0.0139  -0.0638 82  ASN   A N   
495  C CA  . ASN   A 68  ? 0.1192 0.2292 0.2267 -0.0167 -0.0097 -0.0845 82  ASN   A CA  
496  C C   . ASN   A 68  ? 0.1277 0.2363 0.2324 -0.0055 -0.0086 -0.0600 82  ASN   A C   
497  O O   . ASN   A 68  ? 0.1671 0.2781 0.2480 -0.0010 -0.0072 -0.0499 82  ASN   A O   
498  C CB  . ASN   A 68  ? 0.1681 0.2551 0.2580 -0.0197 -0.0054 -0.1010 82  ASN   A CB  
499  C CG  . ASN   A 68  ? 0.2145 0.2918 0.2698 -0.0279 -0.0037 -0.1032 82  ASN   A CG  
500  O OD1 . ASN   A 68  ? 0.2448 0.3067 0.2464 -0.0083 0.0176  -0.0882 82  ASN   A OD1 
501  N ND2 . ASN   A 68  ? 0.2667 0.3113 0.3346 -0.0322 0.0324  -0.1006 82  ASN   A ND2 
502  N N   . TYR   A 69  ? 0.1344 0.2002 0.2167 -0.0204 0.0299  -0.0660 83  TYR   A N   
503  C CA  . TYR   A 69  ? 0.1467 0.1900 0.2037 -0.0138 0.0343  -0.0448 83  TYR   A CA  
504  C C   . TYR   A 69  ? 0.1424 0.1834 0.2317 -0.0128 0.0140  -0.0310 83  TYR   A C   
505  O O   . TYR   A 69  ? 0.1411 0.2024 0.2509 0.0012  -0.0068 -0.0299 83  TYR   A O   
506  C CB  . TYR   A 69  ? 0.1835 0.1947 0.2265 -0.0142 0.0464  -0.0287 83  TYR   A CB  
507  C CG  . TYR   A 69  ? 0.1727 0.1905 0.2658 -0.0143 0.0248  -0.0251 83  TYR   A CG  
508  C CD1 . TYR   A 69  ? 0.1767 0.1971 0.2885 -0.0284 0.0292  -0.0174 83  TYR   A CD1 
509  C CD2 . TYR   A 69  ? 0.1728 0.1949 0.3293 -0.0226 -0.0090 -0.0229 83  TYR   A CD2 
510  C CE1 . TYR   A 69  ? 0.1864 0.1932 0.3232 -0.0226 0.0024  -0.0122 83  TYR   A CE1 
511  C CE2 . TYR   A 69  ? 0.1812 0.1956 0.3671 -0.0179 -0.0132 -0.0140 83  TYR   A CE2 
512  C CZ  . TYR   A 69  ? 0.1877 0.1943 0.3737 -0.0257 -0.0058 -0.0101 83  TYR   A CZ  
513  O OH  . TYR   A 69  ? 0.2113 0.2066 0.4258 -0.0251 -0.0190 -0.0165 83  TYR   A OH  
514  N N   . ARG   A 70  ? 0.1478 0.1801 0.2098 -0.0299 0.0144  -0.0307 84  ARG   A N   
515  C CA  . ARG   A 70  ? 0.1549 0.1936 0.2058 -0.0175 0.0083  -0.0262 84  ARG   A CA  
516  C C   . ARG   A 70  ? 0.1244 0.1791 0.2034 -0.0074 -0.0126 -0.0210 84  ARG   A C   
517  O O   . ARG   A 70  ? 0.1412 0.1707 0.2093 -0.0023 -0.0029 -0.0100 84  ARG   A O   
518  C CB  . ARG   A 70  ? 0.1972 0.2259 0.2021 -0.0247 0.0336  -0.0258 84  ARG   A CB  
519  C CG  . ARG   A 70  ? 0.2431 0.2517 0.2025 -0.0202 0.0256  -0.0075 84  ARG   A CG  
520  C CD  . ARG   A 70  ? 0.2650 0.2750 0.2240 -0.0131 0.0319  -0.0032 84  ARG   A CD  
521  N NE  . ARG   A 70  ? 0.3102 0.2960 0.2625 -0.0106 0.0209  0.0176  84  ARG   A NE  
522  C CZ  . ARG   A 70  ? 0.3312 0.3142 0.3127 -0.0221 0.0124  0.0165  84  ARG   A CZ  
523  N NH1 . ARG   A 70  ? 0.3312 0.3214 0.3306 -0.0253 -0.0175 0.0150  84  ARG   A NH1 
524  N NH2 . ARG   A 70  ? 0.3449 0.3242 0.3345 -0.0394 0.0309  0.0297  84  ARG   A NH2 
525  N N   . ASN   A 71  ? 0.1303 0.1631 0.2107 -0.0125 -0.0104 -0.0120 85  ASN   A N   
526  C CA  . ASN   A 71  ? 0.1325 0.1639 0.1876 -0.0164 -0.0180 -0.0078 85  ASN   A CA  
527  C C   . ASN   A 71  ? 0.1323 0.1505 0.1932 0.0007  -0.0027 -0.0041 85  ASN   A C   
528  O O   . ASN   A 71  ? 0.1570 0.1554 0.2285 -0.0030 -0.0264 -0.0048 85  ASN   A O   
529  C CB  . ASN   A 71  ? 0.1287 0.1778 0.1829 -0.0018 -0.0288 -0.0091 85  ASN   A CB  
530  C CG  . ASN   A 71  ? 0.1362 0.1742 0.1706 -0.0171 -0.0345 -0.0211 85  ASN   A CG  
531  O OD1 . ASN   A 71  ? 0.1352 0.1630 0.1911 -0.0054 -0.0138 -0.0177 85  ASN   A OD1 
532  N ND2 . ASN   A 71  ? 0.1628 0.1901 0.1630 -0.0233 -0.0253 -0.0195 85  ASN   A ND2 
533  N N   . ALA   A 72  ? 0.1343 0.1429 0.1752 -0.0105 0.0005  -0.0042 86  ALA   A N   
534  C CA  . ALA   A 72  ? 0.1442 0.1408 0.1679 0.0000  -0.0004 0.0099  86  ALA   A CA  
535  C C   . ALA   A 72  ? 0.1435 0.1400 0.1659 -0.0010 -0.0093 0.0048  86  ALA   A C   
536  O O   . ALA   A 72  ? 0.1697 0.1532 0.1746 -0.0006 -0.0078 -0.0007 86  ALA   A O   
537  C CB  . ALA   A 72  ? 0.1731 0.1552 0.1761 0.0004  -0.0072 -0.0004 86  ALA   A CB  
538  N N   . HIS   A 73  ? 0.1443 0.1481 0.1620 -0.0019 -0.0099 0.0164  87  HIS   A N   
539  C CA  . HIS   A 73  ? 0.1210 0.1365 0.1584 0.0027  -0.0379 0.0204  87  HIS   A CA  
540  C C   . HIS   A 73  ? 0.1354 0.1326 0.1478 -0.0016 -0.0211 0.0104  87  HIS   A C   
541  O O   . HIS   A 73  ? 0.1586 0.1227 0.1583 -0.0035 -0.0193 -0.0032 87  HIS   A O   
542  C CB  . HIS   A 73  ? 0.1453 0.1480 0.1629 0.0081  -0.0303 0.0084  87  HIS   A CB  
543  C CG  . HIS   A 73  ? 0.1739 0.1724 0.1696 0.0168  -0.0264 0.0157  87  HIS   A CG  
544  N ND1 . HIS   A 73  ? 0.1771 0.1839 0.1573 0.0227  -0.0480 0.0118  87  HIS   A ND1 
545  C CD2 . HIS   A 73  ? 0.1709 0.1957 0.1946 0.0232  -0.0453 0.0110  87  HIS   A CD2 
546  C CE1 . HIS   A 73  ? 0.1979 0.1899 0.1975 0.0259  -0.0456 0.0010  87  HIS   A CE1 
547  N NE2 . HIS   A 73  ? 0.1931 0.2051 0.2052 0.0350  -0.0640 0.0049  87  HIS   A NE2 
548  N N   . SER   A 74  ? 0.1192 0.1372 0.1343 0.0080  -0.0235 0.0126  88  SER   A N   
549  C CA  . SER   A 74  ? 0.1459 0.1229 0.1077 0.0033  -0.0140 0.0168  88  SER   A CA  
550  C C   . SER   A 74  ? 0.1393 0.1066 0.1129 -0.0005 -0.0087 0.0061  88  SER   A C   
551  O O   . SER   A 74  ? 0.1451 0.1174 0.1268 0.0007  -0.0028 0.0058  88  SER   A O   
552  C CB  . SER   A 74  ? 0.1734 0.1272 0.1296 -0.0078 0.0194  0.0294  88  SER   A CB  
553  O OG  . SER   A 74  ? 0.1598 0.1329 0.1530 -0.0036 0.0005  0.0144  88  SER   A OG  
554  N N   . ALA   A 75  ? 0.1403 0.1155 0.1098 0.0114  -0.0011 0.0196  89  ALA   A N   
555  C CA  . ALA   A 75  ? 0.1612 0.1251 0.0902 0.0058  -0.0156 0.0125  89  ALA   A CA  
556  C C   . ALA   A 75  ? 0.1435 0.1106 0.1020 -0.0010 0.0046  0.0048  89  ALA   A C   
557  O O   . ALA   A 75  ? 0.1603 0.1131 0.1103 -0.0234 0.0061  -0.0083 89  ALA   A O   
558  C CB  . ALA   A 75  ? 0.1721 0.1555 0.1109 0.0201  -0.0030 0.0119  89  ALA   A CB  
559  N N   . THR   A 76  ? 0.1356 0.1168 0.0992 0.0019  0.0017  0.0106  90  THR   A N   
560  C CA  . THR   A 76  ? 0.1219 0.1237 0.1010 0.0145  0.0026  0.0078  90  THR   A CA  
561  C C   . THR   A 76  ? 0.1352 0.1074 0.1117 0.0005  -0.0028 -0.0064 90  THR   A C   
562  O O   . THR   A 76  ? 0.1323 0.1179 0.1091 0.0031  -0.0007 -0.0050 90  THR   A O   
563  C CB  . THR   A 76  ? 0.1304 0.1269 0.1134 -0.0017 0.0075  0.0036  90  THR   A CB  
564  O OG1 . THR   A 76  ? 0.1224 0.1275 0.1280 -0.0047 0.0046  0.0007  90  THR   A OG1 
565  C CG2 . THR   A 76  ? 0.1425 0.1290 0.0991 -0.0125 0.0034  0.0103  90  THR   A CG2 
566  N N   . THR   A 77  ? 0.1247 0.1155 0.0991 -0.0050 0.0013  0.0094  91  THR   A N   
567  C CA  . THR   A 77  ? 0.1416 0.1118 0.0992 0.0140  0.0034  0.0165  91  THR   A CA  
568  C C   . THR   A 77  ? 0.1526 0.1100 0.0896 0.0080  0.0042  -0.0056 91  THR   A C   
569  O O   . THR   A 77  ? 0.2020 0.1136 0.1044 0.0193  -0.0055 -0.0026 91  THR   A O   
570  C CB  . THR   A 77  ? 0.1635 0.1258 0.1059 -0.0110 0.0048  -0.0053 91  THR   A CB  
571  O OG1 . THR   A 77  ? 0.1569 0.1288 0.1266 -0.0234 -0.0153 0.0008  91  THR   A OG1 
572  C CG2 . THR   A 77  ? 0.1733 0.1404 0.1144 0.0037  -0.0072 -0.0051 91  THR   A CG2 
573  N N   . TRP   A 78  ? 0.1449 0.0998 0.1101 0.0170  0.0054  0.0167  92  TRP   A N   
574  C CA  . TRP   A 78  ? 0.1394 0.0974 0.1121 0.0089  -0.0101 0.0089  92  TRP   A CA  
575  C C   . TRP   A 78  ? 0.1439 0.1134 0.1193 0.0152  -0.0190 0.0015  92  TRP   A C   
576  O O   . TRP   A 78  ? 0.1674 0.1133 0.1148 0.0320  0.0014  0.0042  92  TRP   A O   
577  C CB  . TRP   A 78  ? 0.1615 0.0908 0.1338 0.0241  0.0102  -0.0017 92  TRP   A CB  
578  C CG  . TRP   A 78  ? 0.1725 0.1041 0.1113 0.0091  0.0047  0.0003  92  TRP   A CG  
579  C CD1 . TRP   A 78  ? 0.1658 0.1091 0.1181 0.0058  0.0018  0.0047  92  TRP   A CD1 
580  C CD2 . TRP   A 78  ? 0.1584 0.1070 0.1216 0.0027  -0.0035 0.0014  92  TRP   A CD2 
581  N NE1 . TRP   A 78  ? 0.1607 0.1121 0.1398 0.0013  -0.0077 0.0029  92  TRP   A NE1 
582  C CE2 . TRP   A 78  ? 0.1617 0.1009 0.1227 0.0061  -0.0122 0.0019  92  TRP   A CE2 
583  C CE3 . TRP   A 78  ? 0.1641 0.1075 0.1214 0.0225  -0.0162 0.0058  92  TRP   A CE3 
584  C CZ2 . TRP   A 78  ? 0.1739 0.1057 0.1433 0.0045  -0.0028 0.0007  92  TRP   A CZ2 
585  C CZ3 . TRP   A 78  ? 0.1775 0.1066 0.1297 0.0264  0.0053  -0.0027 92  TRP   A CZ3 
586  C CH2 . TRP   A 78  ? 0.1860 0.1067 0.1284 0.0096  0.0091  0.0036  92  TRP   A CH2 
587  N N   . SER   A 79  ? 0.1273 0.1151 0.1258 0.0264  -0.0122 0.0136  93  SER   A N   
588  C CA  . SER   A 79  ? 0.1376 0.1279 0.1396 0.0183  -0.0098 -0.0087 93  SER   A CA  
589  C C   . SER   A 79  ? 0.1534 0.1299 0.1223 0.0468  -0.0202 0.0010  93  SER   A C   
590  O O   . SER   A 79  ? 0.1717 0.1390 0.1210 0.0399  -0.0043 -0.0038 93  SER   A O   
591  C CB  . SER   A 79  ? 0.1296 0.1493 0.1608 0.0047  0.0024  -0.0194 93  SER   A CB  
592  O OG  . SER   A 79  ? 0.1484 0.1676 0.1762 0.0117  -0.0093 0.0071  93  SER   A OG  
593  N N   . GLY   A 80  ? 0.1692 0.1125 0.1220 0.0441  -0.0048 0.0078  94  GLY   A N   
594  C CA  . GLY   A 80  ? 0.1903 0.1212 0.1445 0.0517  -0.0136 0.0170  94  GLY   A CA  
595  C C   . GLY   A 80  ? 0.1833 0.1321 0.1337 0.0498  -0.0125 0.0040  94  GLY   A C   
596  O O   . GLY   A 80  ? 0.1878 0.1480 0.1196 0.0445  -0.0128 -0.0070 94  GLY   A O   
597  N N   . GLN   A 81  ? 0.2175 0.1271 0.1520 0.0617  -0.0049 0.0069  95  GLN   A N   
598  C CA  . GLN   A 81  ? 0.2478 0.1341 0.1436 0.0648  -0.0286 0.0125  95  GLN   A CA  
599  C C   . GLN   A 81  ? 0.2660 0.1269 0.1474 0.0606  -0.0118 0.0089  95  GLN   A C   
600  O O   . GLN   A 81  ? 0.2704 0.1170 0.1631 0.0480  -0.0265 0.0099  95  GLN   A O   
601  C CB  . GLN   A 81  ? 0.2674 0.1552 0.1532 0.0656  -0.0414 -0.0017 95  GLN   A CB  
602  C CG  . GLN   A 81  ? 0.2756 0.1680 0.1647 0.0770  -0.0360 -0.0073 95  GLN   A CG  
603  C CD  . GLN   A 81  ? 0.2757 0.1721 0.1625 0.0905  -0.0385 -0.0098 95  GLN   A CD  
604  O OE1 . GLN   A 81  ? 0.2891 0.1773 0.1732 0.0984  -0.0521 -0.0099 95  GLN   A OE1 
605  N NE2 . GLN   A 81  ? 0.2647 0.1853 0.1948 0.0719  -0.0327 -0.0207 95  GLN   A NE2 
606  N N   . TYR   A 82  ? 0.2813 0.1231 0.1777 0.0690  -0.0180 0.0081  96  TYR   A N   
607  C CA  . TYR   A 82  ? 0.3153 0.1379 0.1653 0.0559  -0.0397 0.0049  96  TYR   A CA  
608  C C   . TYR   A 82  ? 0.3188 0.1523 0.1779 0.0614  -0.0557 0.0104  96  TYR   A C   
609  O O   . TYR   A 82  ? 0.3088 0.1583 0.1828 0.0573  -0.0637 -0.0022 96  TYR   A O   
610  C CB  . TYR   A 82  ? 0.3184 0.1424 0.1651 0.0709  -0.0401 -0.0210 96  TYR   A CB  
611  C CG  . TYR   A 82  ? 0.3215 0.1388 0.1714 0.0772  -0.0375 -0.0169 96  TYR   A CG  
612  C CD1 . TYR   A 82  ? 0.3317 0.1338 0.2012 0.0624  -0.0354 -0.0177 96  TYR   A CD1 
613  C CD2 . TYR   A 82  ? 0.3591 0.1418 0.2227 0.0670  -0.0303 -0.0099 96  TYR   A CD2 
614  C CE1 . TYR   A 82  ? 0.3544 0.1441 0.2317 0.0647  -0.0191 -0.0204 96  TYR   A CE1 
615  C CE2 . TYR   A 82  ? 0.3852 0.1429 0.2408 0.0558  -0.0280 -0.0167 96  TYR   A CE2 
616  C CZ  . TYR   A 82  ? 0.3828 0.1409 0.2320 0.0572  -0.0259 -0.0130 96  TYR   A CZ  
617  O OH  . TYR   A 82  ? 0.4277 0.1414 0.2806 0.0330  -0.0420 -0.0052 96  TYR   A OH  
618  N N   . VAL   A 83  ? 0.3559 0.1904 0.1794 0.0807  -0.0501 0.0365  97  VAL   A N   
619  C CA  . VAL   A 83  ? 0.4298 0.2325 0.2363 0.0696  -0.0460 0.0357  97  VAL   A CA  
620  C C   . VAL   A 83  ? 0.4712 0.2408 0.2821 0.0997  -0.0295 0.0672  97  VAL   A C   
621  O O   . VAL   A 83  ? 0.4914 0.2234 0.3356 0.1147  0.0112  0.0887  97  VAL   A O   
622  C CB  . VAL   A 83  ? 0.4405 0.2479 0.2332 0.0575  -0.0940 0.0278  97  VAL   A CB  
623  C CG1 . VAL   A 83  ? 0.4335 0.2573 0.2524 0.0549  -0.1045 0.0372  97  VAL   A CG1 
624  C CG2 . VAL   A 83  ? 0.4627 0.2524 0.2454 0.0337  -0.0909 0.0100  97  VAL   A CG2 
625  N N   . GLY   A 84  ? 0.4880 0.2726 0.2709 0.1023  -0.0407 0.0857  98  GLY   A N   
626  C CA  . GLY   A 84  ? 0.5170 0.2988 0.3027 0.1059  -0.0164 0.0932  98  GLY   A CA  
627  C C   . GLY   A 84  ? 0.5261 0.3221 0.3387 0.1077  -0.0102 0.1073  98  GLY   A C   
628  O O   . GLY   A 84  ? 0.5308 0.3399 0.3490 0.1018  -0.0182 0.1001  98  GLY   A O   
629  N N   . GLY   A 85  ? 0.5352 0.3377 0.3721 0.0986  0.0163  0.1143  99  GLY   A N   
630  C CA  . GLY   A 85  ? 0.5375 0.3538 0.3987 0.0892  0.0317  0.1146  99  GLY   A CA  
631  C C   . GLY   A 85  ? 0.5615 0.3539 0.4109 0.0882  0.0435  0.1210  99  GLY   A C   
632  O O   . GLY   A 85  ? 0.5816 0.3548 0.4263 0.0856  0.0553  0.1070  99  GLY   A O   
633  N N   . ALA   A 86  ? 0.5560 0.3507 0.4148 0.0896  0.0646  0.1367  100 ALA   A N   
634  C CA  . ALA   A 86  ? 0.5492 0.3549 0.4172 0.0932  0.0505  0.1288  100 ALA   A CA  
635  C C   . ALA   A 86  ? 0.5558 0.3520 0.4329 0.0800  0.0443  0.1090  100 ALA   A C   
636  O O   . ALA   A 86  ? 0.5753 0.3680 0.4757 0.0795  0.0448  0.1003  100 ALA   A O   
637  C CB  . ALA   A 86  ? 0.5435 0.3584 0.4028 0.1014  0.0402  0.1450  100 ALA   A CB  
638  N N   . GLU   A 87  ? 0.5380 0.3273 0.3916 0.0962  0.0353  0.1064  101 GLU   A N   
639  C CA  . GLU   A 87  ? 0.5155 0.3060 0.3552 0.0957  0.0176  0.0966  101 GLU   A CA  
640  C C   . GLU   A 87  ? 0.4955 0.2755 0.2934 0.1031  -0.0250 0.0999  101 GLU   A C   
641  O O   . GLU   A 87  ? 0.4870 0.2780 0.2743 0.0822  -0.0502 0.0977  101 GLU   A O   
642  C CB  . GLU   A 87  ? 0.5031 0.3210 0.3702 0.0879  0.0507  0.0796  101 GLU   A CB  
643  C CG  . GLU   A 87  ? 0.4897 0.3358 0.3957 0.0869  0.0544  0.0557  101 GLU   A CG  
644  C CD  . GLU   A 87  ? 0.4770 0.3512 0.4126 0.0920  0.0473  0.0358  101 GLU   A CD  
645  O OE1 . GLU   A 87  ? 0.4766 0.3547 0.4183 0.0894  0.0470  0.0329  101 GLU   A OE1 
646  O OE2 . GLU   A 87  ? 0.4820 0.3582 0.4197 0.0973  0.0502  0.0250  101 GLU   A OE2 
647  N N   . ALA   A 88  ? 0.4874 0.2458 0.2674 0.1156  -0.0244 0.0895  102 ALA   A N   
648  C CA  . ALA   A 88  ? 0.4870 0.2169 0.2491 0.1127  0.0031  0.0604  102 ALA   A CA  
649  C C   . ALA   A 88  ? 0.4469 0.1934 0.2076 0.1117  -0.0207 0.0434  102 ALA   A C   
650  O O   . ALA   A 88  ? 0.4696 0.1805 0.2239 0.0925  -0.0245 0.0389  102 ALA   A O   
651  C CB  . ALA   A 88  ? 0.5135 0.2189 0.2721 0.0984  0.0044  0.0593  102 ALA   A CB  
652  N N   . ARG   A 89  ? 0.4303 0.1798 0.1944 0.1105  -0.0037 0.0382  103 ARG   A N   
653  C CA  . ARG   A 89  ? 0.4182 0.1736 0.1715 0.0974  0.0178  0.0362  103 ARG   A CA  
654  C C   . ARG   A 89  ? 0.3680 0.1599 0.1751 0.0990  0.0123  0.0247  103 ARG   A C   
655  O O   . ARG   A 89  ? 0.3501 0.1721 0.2078 0.1050  0.0097  0.0322  103 ARG   A O   
656  C CB  . ARG   A 89  ? 0.4464 0.1967 0.2048 0.0864  0.0237  0.0253  103 ARG   A CB  
657  C CG  . ARG   A 89  ? 0.4507 0.2128 0.2003 0.0729  0.0140  0.0438  103 ARG   A CG  
658  C CD  . ARG   A 89  ? 0.4444 0.2317 0.2010 0.0700  0.0096  0.0506  103 ARG   A CD  
659  N NE  . ARG   A 89  ? 0.4571 0.2432 0.2176 0.0561  -0.0036 0.0338  103 ARG   A NE  
660  C CZ  . ARG   A 89  ? 0.4790 0.2305 0.2082 0.0290  0.0017  0.0368  103 ARG   A CZ  
661  N NH1 . ARG   A 89  ? 0.4716 0.2120 0.1977 0.0357  -0.0099 0.0224  103 ARG   A NH1 
662  N NH2 . ARG   A 89  ? 0.5108 0.2361 0.2316 0.0070  0.0092  0.0306  103 ARG   A NH2 
663  N N   . ILE   A 90  ? 0.3341 0.1338 0.1456 0.0697  -0.0168 0.0125  104 ILE   A N   
664  C CA  . ILE   A 90  ? 0.3111 0.1313 0.1193 0.0551  -0.0150 0.0144  104 ILE   A CA  
665  C C   . ILE   A 90  ? 0.2706 0.1280 0.1402 0.0476  -0.0058 0.0156  104 ILE   A C   
666  O O   . ILE   A 90  ? 0.2575 0.1375 0.1804 0.0393  -0.0135 0.0155  104 ILE   A O   
667  C CB  . ILE   A 90  ? 0.3058 0.1372 0.1308 0.0605  -0.0108 0.0109  104 ILE   A CB  
668  C CG1 . ILE   A 90  ? 0.3552 0.1465 0.1498 0.0707  -0.0202 -0.0063 104 ILE   A CG1 
669  C CG2 . ILE   A 90  ? 0.2885 0.1451 0.1453 0.0474  -0.0002 0.0121  104 ILE   A CG2 
670  C CD1 . ILE   A 90  ? 0.3800 0.1518 0.1536 0.0534  0.0012  0.0136  104 ILE   A CD1 
671  N N   . ASN   A 91  ? 0.2606 0.1275 0.1517 0.0413  -0.0083 0.0184  105 ASN   A N   
672  C CA  . ASN   A 91  ? 0.2448 0.1329 0.1328 0.0416  -0.0058 0.0272  105 ASN   A CA  
673  C C   . ASN   A 91  ? 0.2077 0.1302 0.1202 0.0397  -0.0047 0.0150  105 ASN   A C   
674  O O   . ASN   A 91  ? 0.2239 0.1432 0.1481 0.0536  0.0135  0.0187  105 ASN   A O   
675  C CB  . ASN   A 91  ? 0.2671 0.1866 0.1514 0.0464  -0.0242 0.0512  105 ASN   A CB  
676  C CG  . ASN   A 91  ? 0.3004 0.2518 0.1863 0.0345  -0.0512 0.0619  105 ASN   A CG  
677  O OD1 . ASN   A 91  ? 0.3011 0.2750 0.1802 0.0226  -0.0255 0.0710  105 ASN   A OD1 
678  N ND2 . ASN   A 91  ? 0.3532 0.2781 0.2284 0.0412  -0.0759 0.0840  105 ASN   A ND2 
679  N N   . THR   A 92  ? 0.1992 0.1273 0.1074 0.0408  -0.0129 0.0134  106 THR   A N   
680  C CA  . THR   A 92  ? 0.1915 0.1250 0.1089 0.0357  0.0011  0.0035  106 THR   A CA  
681  C C   . THR   A 92  ? 0.1913 0.1249 0.0886 0.0287  0.0072  0.0012  106 THR   A C   
682  O O   . THR   A 92  ? 0.2084 0.1243 0.0985 0.0213  0.0065  0.0065  106 THR   A O   
683  C CB  . THR   A 92  ? 0.1841 0.1227 0.1124 0.0348  -0.0016 -0.0007 106 THR   A CB  
684  O OG1 . THR   A 92  ? 0.1989 0.1403 0.1345 0.0231  -0.0033 0.0111  106 THR   A OG1 
685  C CG2 . THR   A 92  ? 0.2123 0.1284 0.1303 0.0177  -0.0091 -0.0135 106 THR   A CG2 
686  N N   . GLN   A 93  ? 0.1734 0.1221 0.1199 0.0319  -0.0084 0.0065  107 GLN   A N   
687  C CA  A GLN   A 93  ? 0.1849 0.1237 0.1223 0.0351  -0.0180 0.0124  107 GLN   A CA  
688  C CA  B GLN   A 93  ? 0.1707 0.1252 0.1116 0.0330  -0.0255 0.0110  107 GLN   A CA  
689  C C   . GLN   A 93  ? 0.1552 0.1179 0.1063 0.0297  -0.0174 0.0065  107 GLN   A C   
690  O O   . GLN   A 93  ? 0.1557 0.1330 0.1184 0.0394  0.0006  -0.0037 107 GLN   A O   
691  C CB  A GLN   A 93  ? 0.2321 0.1446 0.1330 0.0336  -0.0351 -0.0013 107 GLN   A CB  
692  C CB  B GLN   A 93  ? 0.2018 0.1448 0.1122 0.0346  -0.0542 0.0020  107 GLN   A CB  
693  C CG  A GLN   A 93  ? 0.2276 0.1631 0.1553 0.0264  -0.0249 -0.0187 107 GLN   A CG  
694  C CG  B GLN   A 93  ? 0.2208 0.1715 0.1167 0.0304  -0.0375 -0.0014 107 GLN   A CG  
695  C CD  A GLN   A 93  ? 0.2176 0.1702 0.1808 0.0216  -0.0175 -0.0307 107 GLN   A CD  
696  C CD  B GLN   A 93  ? 0.2242 0.1862 0.0975 0.0231  -0.0170 0.0039  107 GLN   A CD  
697  O OE1 A GLN   A 93  ? 0.2298 0.1819 0.2298 0.0325  -0.0143 -0.0419 107 GLN   A OE1 
698  O OE1 B GLN   A 93  ? 0.2344 0.2045 0.1038 0.0038  0.0017  0.0103  107 GLN   A OE1 
699  N NE2 A GLN   A 93  ? 0.2221 0.1689 0.1895 0.0184  0.0116  -0.0203 107 GLN   A NE2 
700  N NE2 B GLN   A 93  ? 0.2132 0.1816 0.0964 0.0321  -0.0412 -0.0012 107 GLN   A NE2 
701  N N   . TRP   A 94  ? 0.1285 0.1002 0.1068 0.0041  -0.0087 0.0105  108 TRP   A N   
702  C CA  . TRP   A 94  ? 0.1338 0.1093 0.1066 0.0055  -0.0103 0.0144  108 TRP   A CA  
703  C C   . TRP   A 94  ? 0.1393 0.1149 0.0945 0.0168  0.0048  0.0029  108 TRP   A C   
704  O O   . TRP   A 94  ? 0.1523 0.1052 0.1173 0.0123  0.0034  0.0113  108 TRP   A O   
705  C CB  . TRP   A 94  ? 0.1380 0.1196 0.1189 -0.0086 0.0032  -0.0050 108 TRP   A CB  
706  C CG  . TRP   A 94  ? 0.1472 0.1118 0.1005 0.0014  -0.0117 0.0024  108 TRP   A CG  
707  C CD1 . TRP   A 94  ? 0.1679 0.1134 0.1073 0.0086  0.0028  0.0100  108 TRP   A CD1 
708  C CD2 . TRP   A 94  ? 0.1416 0.1119 0.1089 -0.0088 -0.0040 0.0077  108 TRP   A CD2 
709  N NE1 . TRP   A 94  ? 0.1569 0.1199 0.1190 0.0067  0.0058  0.0091  108 TRP   A NE1 
710  C CE2 . TRP   A 94  ? 0.1460 0.1110 0.1180 0.0016  0.0151  0.0065  108 TRP   A CE2 
711  C CE3 . TRP   A 94  ? 0.1558 0.1058 0.1087 0.0113  0.0026  0.0088  108 TRP   A CE3 
712  C CZ2 . TRP   A 94  ? 0.1664 0.1191 0.1240 -0.0029 -0.0002 0.0064  108 TRP   A CZ2 
713  C CZ3 . TRP   A 94  ? 0.1474 0.1177 0.1107 -0.0003 -0.0020 -0.0108 108 TRP   A CZ3 
714  C CH2 . TRP   A 94  ? 0.1418 0.1194 0.1184 0.0004  0.0019  -0.0143 108 TRP   A CH2 
715  N N   . LEU   A 95  ? 0.1459 0.1118 0.0922 0.0222  -0.0061 0.0140  109 LEU   A N   
716  C CA  . LEU   A 95  ? 0.1390 0.1003 0.0972 0.0118  -0.0097 0.0200  109 LEU   A CA  
717  C C   . LEU   A 95  ? 0.1496 0.1039 0.1025 0.0115  0.0023  -0.0045 109 LEU   A C   
718  O O   . LEU   A 95  ? 0.1618 0.1163 0.1516 0.0161  -0.0264 -0.0286 109 LEU   A O   
719  C CB  . LEU   A 95  ? 0.1376 0.1214 0.1174 0.0053  -0.0113 -0.0023 109 LEU   A CB  
720  C CG  . LEU   A 95  ? 0.1298 0.1348 0.1231 0.0035  -0.0159 0.0004  109 LEU   A CG  
721  C CD1 . LEU   A 95  ? 0.1490 0.1545 0.1481 -0.0012 0.0091  0.0111  109 LEU   A CD1 
722  C CD2 . LEU   A 95  ? 0.1717 0.1407 0.1678 -0.0051 -0.0302 -0.0262 109 LEU   A CD2 
723  N N   . LEU   A 96  ? 0.1269 0.1095 0.1003 0.0250  -0.0130 0.0019  110 LEU   A N   
724  C CA  . LEU   A 96  ? 0.1613 0.1103 0.1020 0.0039  0.0038  0.0199  110 LEU   A CA  
725  C C   . LEU   A 96  ? 0.1476 0.1018 0.0844 0.0117  -0.0196 -0.0061 110 LEU   A C   
726  O O   . LEU   A 96  ? 0.1527 0.1023 0.1030 0.0137  -0.0056 -0.0139 110 LEU   A O   
727  C CB  . LEU   A 96  ? 0.1502 0.1175 0.1128 0.0077  -0.0047 0.0104  110 LEU   A CB  
728  C CG  . LEU   A 96  ? 0.1328 0.1414 0.1258 0.0046  -0.0110 0.0161  110 LEU   A CG  
729  C CD1 . LEU   A 96  ? 0.1411 0.1501 0.1229 0.0061  -0.0146 0.0044  110 LEU   A CD1 
730  C CD2 . LEU   A 96  ? 0.1397 0.1538 0.1543 0.0012  0.0089  0.0193  110 LEU   A CD2 
731  N N   . THR   A 97  ? 0.1387 0.1097 0.0924 0.0082  -0.0197 0.0150  111 THR   A N   
732  C CA  . THR   A 97  ? 0.1445 0.1096 0.0915 0.0096  -0.0072 0.0151  111 THR   A CA  
733  C C   . THR   A 97  ? 0.1408 0.1119 0.1187 0.0024  -0.0221 0.0069  111 THR   A C   
734  O O   . THR   A 97  ? 0.1655 0.1160 0.1200 -0.0134 -0.0192 0.0012  111 THR   A O   
735  C CB  . THR   A 97  ? 0.1500 0.1323 0.1169 0.0042  -0.0142 0.0202  111 THR   A CB  
736  O OG1 . THR   A 97  ? 0.1409 0.1501 0.1504 -0.0065 -0.0147 0.0179  111 THR   A OG1 
737  C CG2 . THR   A 97  ? 0.1722 0.1395 0.1423 0.0070  0.0018  0.0278  111 THR   A CG2 
738  N N   . SER   A 98  ? 0.1251 0.1252 0.1229 0.0159  -0.0110 0.0257  112 SER   A N   
739  C CA  . SER   A 98  ? 0.1386 0.1346 0.1346 0.0177  -0.0165 0.0268  112 SER   A CA  
740  C C   . SER   A 98  ? 0.1597 0.1369 0.1393 0.0052  -0.0376 0.0256  112 SER   A C   
741  O O   . SER   A 98  ? 0.1973 0.1438 0.1680 -0.0049 -0.0448 0.0406  112 SER   A O   
742  C CB  . SER   A 98  ? 0.1414 0.1561 0.1550 0.0227  -0.0167 0.0260  112 SER   A CB  
743  O OG  . SER   A 98  ? 0.1766 0.1722 0.1601 0.0178  0.0003  0.0099  112 SER   A OG  
744  N N   . GLY   A 99  ? 0.1790 0.1542 0.1205 0.0050  -0.0245 0.0316  113 GLY   A N   
745  C CA  . GLY   A 99  ? 0.1938 0.1580 0.1478 0.0040  -0.0141 0.0365  113 GLY   A CA  
746  C C   . GLY   A 99  ? 0.1763 0.1537 0.1680 0.0026  -0.0110 0.0330  113 GLY   A C   
747  O O   . GLY   A 99  ? 0.1835 0.1785 0.2320 0.0148  0.0162  0.0353  113 GLY   A O   
748  N N   . THR   A 100 ? 0.1941 0.1390 0.1608 0.0141  -0.0170 0.0283  114 THR   A N   
749  C CA  . THR   A 100 ? 0.2140 0.1448 0.1459 0.0300  -0.0180 0.0400  114 THR   A CA  
750  C C   . THR   A 100 ? 0.1956 0.1442 0.1506 0.0125  -0.0239 0.0208  114 THR   A C   
751  O O   . THR   A 100 ? 0.2099 0.1557 0.1578 0.0173  -0.0157 0.0250  114 THR   A O   
752  C CB  . THR   A 100 ? 0.2203 0.1549 0.1604 0.0252  -0.0386 0.0423  114 THR   A CB  
753  O OG1 . THR   A 100 ? 0.2251 0.1666 0.1529 0.0279  -0.0412 0.0175  114 THR   A OG1 
754  C CG2 . THR   A 100 ? 0.2403 0.1582 0.1729 0.0301  -0.0326 0.0480  114 THR   A CG2 
755  N N   . THR   A 101 ? 0.1899 0.1482 0.1845 -0.0009 -0.0566 0.0474  115 THR   A N   
756  C CA  . THR   A 101 ? 0.2206 0.1408 0.1963 -0.0001 -0.0379 0.0438  115 THR   A CA  
757  C C   . THR   A 101 ? 0.2335 0.1423 0.1735 0.0084  -0.0336 0.0288  115 THR   A C   
758  O O   . THR   A 101 ? 0.2199 0.1395 0.1461 0.0135  -0.0371 0.0321  115 THR   A O   
759  C CB  . THR   A 101 ? 0.2500 0.1636 0.2100 0.0167  -0.0560 0.0410  115 THR   A CB  
760  O OG1 . THR   A 101 ? 0.2616 0.1756 0.1948 0.0371  -0.0288 0.0462  115 THR   A OG1 
761  C CG2 . THR   A 101 ? 0.2694 0.1697 0.2460 0.0151  -0.0751 0.0450  115 THR   A CG2 
762  N N   . GLU   A 102 ? 0.2435 0.1566 0.1720 -0.0211 -0.0214 0.0290  116 GLU   A N   
763  C CA  . GLU   A 102 ? 0.2615 0.1667 0.1975 -0.0290 -0.0030 0.0321  116 GLU   A CA  
764  C C   . GLU   A 102 ? 0.2633 0.1504 0.1758 -0.0082 -0.0293 0.0373  116 GLU   A C   
765  O O   . GLU   A 102 ? 0.2711 0.1500 0.1766 -0.0084 -0.0432 0.0343  116 GLU   A O   
766  C CB  . GLU   A 102 ? 0.2735 0.1876 0.2350 -0.0464 -0.0014 0.0290  116 GLU   A CB  
767  C CG  . GLU   A 102 ? 0.3030 0.2101 0.2944 -0.0501 -0.0001 0.0282  116 GLU   A CG  
768  C CD  . GLU   A 102 ? 0.3175 0.2250 0.3066 -0.0370 -0.0247 0.0215  116 GLU   A CD  
769  O OE1 . GLU   A 102 ? 0.3198 0.2285 0.3380 -0.0419 -0.0120 0.0206  116 GLU   A OE1 
770  O OE2 . GLU   A 102 ? 0.3406 0.2404 0.3037 -0.0140 -0.0335 0.0397  116 GLU   A OE2 
771  N N   . ALA   A 103 ? 0.2756 0.1417 0.1953 0.0022  -0.0117 0.0462  117 ALA   A N   
772  C CA  . ALA   A 103 ? 0.2997 0.1556 0.1967 0.0258  -0.0326 0.0393  117 ALA   A CA  
773  C C   . ALA   A 103 ? 0.2769 0.1442 0.1658 0.0411  -0.0390 0.0284  117 ALA   A C   
774  O O   . ALA   A 103 ? 0.3179 0.1470 0.1965 0.0434  -0.0447 0.0288  117 ALA   A O   
775  C CB  . ALA   A 103 ? 0.3274 0.1678 0.2191 0.0526  -0.0347 0.0512  117 ALA   A CB  
776  N N   . ASN   A 104 ? 0.2487 0.1373 0.1619 0.0476  -0.0076 0.0359  118 ASN   A N   
777  C CA  . ASN   A 104 ? 0.2301 0.1447 0.1763 0.0335  -0.0215 0.0343  118 ASN   A CA  
778  C C   . ASN   A 104 ? 0.2277 0.1447 0.1557 0.0313  -0.0098 0.0382  118 ASN   A C   
779  O O   . ASN   A 104 ? 0.2363 0.1502 0.1532 0.0214  0.0055  0.0358  118 ASN   A O   
780  C CB  . ASN   A 104 ? 0.2241 0.1711 0.2285 0.0610  -0.0142 0.0388  118 ASN   A CB  
781  C CG  . ASN   A 104 ? 0.2364 0.2109 0.2518 0.0717  0.0018  0.0308  118 ASN   A CG  
782  O OD1 . ASN   A 104 ? 0.2781 0.2155 0.2639 0.0900  0.0197  0.0255  118 ASN   A OD1 
783  N ND2 . ASN   A 104 ? 0.2250 0.2341 0.2741 0.0684  0.0011  0.0404  118 ASN   A ND2 
784  N N   . ALA   A 105 ? 0.2024 0.1384 0.1700 0.0281  -0.0035 0.0315  119 ALA   A N   
785  C CA  . ALA   A 105 ? 0.2077 0.1348 0.1631 0.0256  -0.0180 0.0217  119 ALA   A CA  
786  C C   . ALA   A 105 ? 0.1758 0.1196 0.1604 -0.0071 -0.0371 0.0285  119 ALA   A C   
787  O O   . ALA   A 105 ? 0.1934 0.1136 0.1698 0.0030  -0.0340 0.0299  119 ALA   A O   
788  C CB  . ALA   A 105 ? 0.2048 0.1423 0.1581 0.0136  0.0029  0.0299  119 ALA   A CB  
789  N N   . TRP   A 106 ? 0.2145 0.1169 0.1725 -0.0037 -0.0395 0.0203  120 TRP   A N   
790  C CA  . TRP   A 106 ? 0.2578 0.1155 0.1722 -0.0117 -0.0622 0.0176  120 TRP   A CA  
791  C C   . TRP   A 106 ? 0.2575 0.1146 0.1642 0.0129  -0.0644 0.0296  120 TRP   A C   
792  O O   . TRP   A 106 ? 0.2796 0.1191 0.1821 -0.0047 -0.0839 0.0322  120 TRP   A O   
793  C CB  . TRP   A 106 ? 0.3039 0.1314 0.1946 -0.0036 -0.0720 0.0011  120 TRP   A CB  
794  C CG  . TRP   A 106 ? 0.3425 0.1356 0.1906 0.0131  -0.0486 -0.0133 120 TRP   A CG  
795  C CD1 . TRP   A 106 ? 0.3579 0.1402 0.2163 0.0194  -0.0539 -0.0089 120 TRP   A CD1 
796  C CD2 . TRP   A 106 ? 0.3912 0.1528 0.1849 0.0051  -0.0167 -0.0031 120 TRP   A CD2 
797  N NE1 . TRP   A 106 ? 0.3948 0.1595 0.2369 0.0136  -0.0276 -0.0085 120 TRP   A NE1 
798  C CE2 . TRP   A 106 ? 0.4202 0.1595 0.2213 0.0018  0.0234  -0.0152 120 TRP   A CE2 
799  C CE3 . TRP   A 106 ? 0.4248 0.1619 0.2072 0.0032  0.0125  0.0074  120 TRP   A CE3 
800  C CZ2 . TRP   A 106 ? 0.4669 0.1812 0.2561 -0.0076 0.0604  -0.0121 120 TRP   A CZ2 
801  C CZ3 . TRP   A 106 ? 0.4564 0.1794 0.2530 0.0046  0.0394  0.0022  120 TRP   A CZ3 
802  C CH2 . TRP   A 106 ? 0.4744 0.1860 0.2689 -0.0106 0.0654  -0.0183 120 TRP   A CH2 
803  N N   . LYS   A 107 ? 0.2528 0.1119 0.1594 0.0250  -0.0228 0.0119  121 LYS   A N   
804  C CA  . LYS   A 107 ? 0.2475 0.1308 0.1658 0.0332  0.0060  0.0069  121 LYS   A CA  
805  C C   . LYS   A 107 ? 0.1986 0.1224 0.1527 0.0296  -0.0167 0.0107  121 LYS   A C   
806  O O   . LYS   A 107 ? 0.1925 0.1267 0.1751 0.0170  0.0084  0.0102  121 LYS   A O   
807  C CB  . LYS   A 107 ? 0.2828 0.1576 0.1779 0.0606  0.0109  0.0331  121 LYS   A CB  
808  C CG  . LYS   A 107 ? 0.2741 0.1863 0.2031 0.0888  0.0415  0.0370  121 LYS   A CG  
809  C CD  . LYS   A 107 ? 0.2820 0.2290 0.2646 0.1020  0.0465  0.0498  121 LYS   A CD  
810  C CE  . LYS   A 107 ? 0.2907 0.2588 0.3003 0.1230  0.0366  0.0438  121 LYS   A CE  
811  N NZ  . LYS   A 107 ? 0.3245 0.2770 0.3454 0.1298  0.0316  0.0452  121 LYS   A NZ  
812  N N   . SER   A 108 ? 0.1963 0.1085 0.1169 0.0241  -0.0405 0.0019  122 SER   A N   
813  C CA  . SER   A 108 ? 0.1738 0.1094 0.1268 0.0224  -0.0197 0.0009  122 SER   A CA  
814  C C   . SER   A 108 ? 0.1474 0.1131 0.1139 0.0099  0.0060  0.0155  122 SER   A C   
815  O O   . SER   A 108 ? 0.1585 0.1279 0.1263 -0.0051 -0.0299 0.0063  122 SER   A O   
816  C CB  . SER   A 108 ? 0.2145 0.1263 0.1280 0.0051  -0.0281 0.0071  122 SER   A CB  
817  O OG  . SER   A 108 ? 0.2165 0.1530 0.1482 -0.0127 0.0072  0.0007  122 SER   A OG  
818  N N   . THR   A 109 ? 0.1644 0.0996 0.1124 0.0128  -0.0014 0.0170  123 THR   A N   
819  C CA  . THR   A 109 ? 0.1391 0.0943 0.1095 -0.0004 -0.0158 0.0126  123 THR   A CA  
820  C C   . THR   A 109 ? 0.1346 0.1133 0.1075 0.0114  -0.0203 -0.0004 123 THR   A C   
821  O O   . THR   A 109 ? 0.1523 0.1375 0.1114 -0.0003 -0.0046 -0.0001 123 THR   A O   
822  C CB  . THR   A 109 ? 0.1516 0.1187 0.1039 0.0158  0.0012  0.0070  123 THR   A CB  
823  O OG1 . THR   A 109 ? 0.1751 0.1445 0.1061 0.0120  0.0007  0.0195  123 THR   A OG1 
824  C CG2 . THR   A 109 ? 0.1575 0.1181 0.1284 0.0143  -0.0104 -0.0090 123 THR   A CG2 
825  N N   . LEU   A 110 ? 0.1357 0.1063 0.1093 0.0133  -0.0055 0.0120  124 LEU   A N   
826  C CA  . LEU   A 110 ? 0.1470 0.1149 0.1062 0.0114  0.0050  0.0133  124 LEU   A CA  
827  C C   . LEU   A 110 ? 0.1442 0.1078 0.0985 0.0184  -0.0062 -0.0014 124 LEU   A C   
828  O O   . LEU   A 110 ? 0.1713 0.1132 0.1107 0.0248  -0.0086 -0.0135 124 LEU   A O   
829  C CB  . LEU   A 110 ? 0.1460 0.1258 0.1347 0.0183  0.0001  -0.0006 124 LEU   A CB  
830  C CG  . LEU   A 110 ? 0.1736 0.1248 0.1346 0.0096  -0.0010 -0.0087 124 LEU   A CG  
831  C CD1 . LEU   A 110 ? 0.1650 0.1509 0.1595 -0.0079 0.0055  -0.0246 124 LEU   A CD1 
832  C CD2 . LEU   A 110 ? 0.2069 0.1277 0.1498 0.0246  0.0173  -0.0003 124 LEU   A CD2 
833  N N   . VAL   A 111 ? 0.1602 0.1069 0.1124 0.0184  -0.0056 0.0058  125 VAL   A N   
834  C CA  . VAL   A 111 ? 0.1590 0.1118 0.1189 0.0080  -0.0092 0.0069  125 VAL   A CA  
835  C C   . VAL   A 111 ? 0.1484 0.1001 0.1172 0.0120  0.0026  -0.0021 125 VAL   A C   
836  O O   . VAL   A 111 ? 0.1530 0.1094 0.1183 0.0093  0.0007  0.0002  125 VAL   A O   
837  C CB  . VAL   A 111 ? 0.1663 0.1163 0.1212 0.0103  0.0063  -0.0142 125 VAL   A CB  
838  C CG1 . VAL   A 111 ? 0.1824 0.1151 0.1316 0.0065  0.0138  -0.0135 125 VAL   A CG1 
839  C CG2 . VAL   A 111 ? 0.1686 0.1326 0.1276 0.0223  -0.0076 -0.0050 125 VAL   A CG2 
840  N N   . GLY   A 112 ? 0.1618 0.0996 0.1174 0.0051  0.0044  0.0150  126 GLY   A N   
841  C CA  . GLY   A 112 ? 0.1758 0.1091 0.1181 0.0001  0.0091  0.0130  126 GLY   A CA  
842  C C   . GLY   A 112 ? 0.1600 0.1162 0.1054 0.0216  -0.0056 0.0125  126 GLY   A C   
843  O O   . GLY   A 112 ? 0.1799 0.1172 0.1044 0.0204  0.0034  0.0062  126 GLY   A O   
844  N N   . HIS   A 113 ? 0.1798 0.1220 0.1098 0.0300  0.0011  0.0087  127 HIS   A N   
845  C CA  . HIS   A 113 ? 0.1931 0.1224 0.1174 0.0241  -0.0057 0.0039  127 HIS   A CA  
846  C C   . HIS   A 113 ? 0.1887 0.1210 0.1187 0.0153  0.0064  0.0166  127 HIS   A C   
847  O O   . HIS   A 113 ? 0.2167 0.1283 0.1452 0.0131  0.0264  -0.0006 127 HIS   A O   
848  C CB  . HIS   A 113 ? 0.1913 0.1407 0.1209 0.0164  -0.0015 -0.0028 127 HIS   A CB  
849  C CG  . HIS   A 113 ? 0.2047 0.1823 0.1346 -0.0280 -0.0140 -0.0103 127 HIS   A CG  
850  N ND1 . HIS   A 113 ? 0.2592 0.2070 0.1456 -0.0464 0.0203  -0.0271 127 HIS   A ND1 
851  C CD2 . HIS   A 113 ? 0.1988 0.2076 0.1465 -0.0292 -0.0053 -0.0511 127 HIS   A CD2 
852  C CE1 . HIS   A 113 ? 0.2611 0.2262 0.1605 -0.0534 0.0269  -0.0460 127 HIS   A CE1 
853  N NE2 . HIS   A 113 ? 0.2485 0.2360 0.1725 -0.0342 0.0122  -0.0483 127 HIS   A NE2 
854  N N   . ASP   A 114 ? 0.1926 0.1136 0.1185 0.0061  0.0069  0.0054  128 ASP   A N   
855  C CA  . ASP   A 114 ? 0.1926 0.1045 0.1377 -0.0031 -0.0092 0.0163  128 ASP   A CA  
856  C C   . ASP   A 114 ? 0.1982 0.1186 0.1345 0.0060  -0.0021 0.0156  128 ASP   A C   
857  O O   . ASP   A 114 ? 0.1997 0.1251 0.1509 0.0100  -0.0070 0.0154  128 ASP   A O   
858  C CB  . ASP   A 114 ? 0.1910 0.1135 0.1255 0.0035  -0.0062 0.0125  128 ASP   A CB  
859  C CG  . ASP   A 114 ? 0.2068 0.1353 0.1249 -0.0005 0.0138  0.0084  128 ASP   A CG  
860  O OD1 . ASP   A 114 ? 0.2126 0.1345 0.1340 0.0027  0.0101  0.0181  128 ASP   A OD1 
861  O OD2 . ASP   A 114 ? 0.1944 0.1381 0.1238 -0.0025 0.0202  0.0225  128 ASP   A OD2 
862  N N   . THR   A 115 ? 0.2410 0.1200 0.1439 0.0081  0.0067  0.0144  129 THR   A N   
863  C CA  A THR   A 115 ? 0.2587 0.1297 0.1335 0.0220  -0.0152 0.0450  129 THR   A CA  
864  C CA  B THR   A 115 ? 0.2615 0.1197 0.1520 0.0131  0.0147  0.0271  129 THR   A CA  
865  C C   . THR   A 115 ? 0.2756 0.1188 0.1591 0.0194  0.0152  0.0273  129 THR   A C   
866  O O   . THR   A 115 ? 0.2920 0.1179 0.1749 0.0090  0.0315  0.0249  129 THR   A O   
867  C CB  A THR   A 115 ? 0.2928 0.1550 0.1615 0.0582  -0.0070 0.0374  129 THR   A CB  
868  C CB  B THR   A 115 ? 0.2551 0.1219 0.1589 0.0118  0.0172  0.0343  129 THR   A CB  
869  O OG1 A THR   A 115 ? 0.3002 0.1595 0.1747 0.0561  -0.0036 0.0364  129 THR   A OG1 
870  O OG1 B THR   A 115 ? 0.2550 0.1260 0.1720 0.0095  0.0219  0.0357  129 THR   A OG1 
871  C CG2 A THR   A 115 ? 0.3200 0.1739 0.1822 0.0754  0.0040  0.0348  129 THR   A CG2 
872  C CG2 B THR   A 115 ? 0.2428 0.1187 0.1606 0.0146  0.0117  0.0392  129 THR   A CG2 
873  N N   . PHE   A 116 ? 0.2925 0.1201 0.1508 0.0273  -0.0059 0.0190  130 PHE   A N   
874  C CA  . PHE   A 116 ? 0.3136 0.1243 0.1517 0.0258  -0.0092 0.0054  130 PHE   A CA  
875  C C   . PHE   A 116 ? 0.3483 0.1311 0.1717 0.0147  -0.0088 0.0087  130 PHE   A C   
876  O O   . PHE   A 116 ? 0.3591 0.1291 0.1865 0.0258  -0.0234 0.0225  130 PHE   A O   
877  C CB  . PHE   A 116 ? 0.3080 0.1220 0.1508 0.0291  0.0169  0.0091  130 PHE   A CB  
878  C CG  . PHE   A 116 ? 0.2736 0.1321 0.1373 0.0258  0.0078  0.0084  130 PHE   A CG  
879  C CD1 . PHE   A 116 ? 0.2617 0.1376 0.1286 0.0192  0.0121  -0.0106 130 PHE   A CD1 
880  C CD2 . PHE   A 116 ? 0.2665 0.1430 0.1210 0.0179  -0.0005 -0.0028 130 PHE   A CD2 
881  C CE1 . PHE   A 116 ? 0.2349 0.1418 0.1325 0.0076  0.0249  -0.0088 130 PHE   A CE1 
882  C CE2 . PHE   A 116 ? 0.2344 0.1373 0.1307 0.0061  0.0186  -0.0040 130 PHE   A CE2 
883  C CZ  . PHE   A 116 ? 0.2290 0.1367 0.1328 -0.0011 0.0233  -0.0118 130 PHE   A CZ  
884  N N   . THR   A 117 ? 0.3610 0.1339 0.1521 0.0087  -0.0114 0.0187  131 THR   A N   
885  C CA  . THR   A 117 ? 0.3856 0.1645 0.1588 0.0129  -0.0203 0.0301  131 THR   A CA  
886  C C   . THR   A 117 ? 0.4003 0.1524 0.1839 0.0092  -0.0188 0.0355  131 THR   A C   
887  O O   . THR   A 117 ? 0.3633 0.1205 0.1789 -0.0170 0.0020  0.0144  131 THR   A O   
888  C CB  . THR   A 117 ? 0.4047 0.2307 0.1757 0.0292  -0.0198 -0.0084 131 THR   A CB  
889  O OG1 . THR   A 117 ? 0.4484 0.2850 0.2105 0.0462  -0.0069 -0.0421 131 THR   A OG1 
890  C CG2 . THR   A 117 ? 0.4200 0.2382 0.1804 -0.0025 -0.0237 -0.0052 131 THR   A CG2 
891  N N   . LYS   A 118 ? 0.4357 0.1822 0.2463 -0.0029 -0.0005 0.0296  132 LYS   A N   
892  C CA  . LYS   A 118 ? 0.4222 0.2025 0.2508 -0.0286 0.0269  0.0321  132 LYS   A CA  
893  C C   . LYS   A 118 ? 0.4306 0.2444 0.2339 -0.0791 0.0383  0.0323  132 LYS   A C   
894  O O   . LYS   A 118 ? 0.4791 0.2626 0.2391 -0.1006 0.0010  0.0475  132 LYS   A O   
895  C CB  . LYS   A 118 ? 0.3808 0.2117 0.2661 -0.0144 0.0526  0.0177  132 LYS   A CB  
896  C CG  . LYS   A 118 ? 0.3609 0.2286 0.2970 -0.0140 0.0568  0.0115  132 LYS   A CG  
897  C CD  . LYS   A 118 ? 0.3653 0.2500 0.3187 -0.0115 0.0966  -0.0137 132 LYS   A CD  
898  C CE  . LYS   A 118 ? 0.3773 0.2648 0.3613 -0.0069 0.1140  -0.0245 132 LYS   A CE  
899  N NZ  . LYS   A 118 ? 0.3842 0.2676 0.3844 0.0023  0.1202  -0.0310 132 LYS   A NZ  
900  N N   . VAL   A 119 ? 0.4057 0.2611 0.2555 -0.0940 0.0624  0.0427  133 VAL   A N   
901  C CA  . VAL   A 119 ? 0.3636 0.2724 0.2691 -0.0867 0.0680  0.0337  133 VAL   A CA  
902  C C   . VAL   A 119 ? 0.3153 0.2567 0.2748 -0.1240 0.0394  0.0117  133 VAL   A C   
903  O O   . VAL   A 119 ? 0.3166 0.2676 0.3342 -0.1348 0.0296  -0.0239 133 VAL   A O   
904  C CB  . VAL   A 119 ? 0.3655 0.2925 0.2852 -0.0620 0.0936  0.0548  133 VAL   A CB  
905  C CG1 . VAL   A 119 ? 0.3295 0.2945 0.3019 -0.0713 0.1267  0.0782  133 VAL   A CG1 
906  C CG2 . VAL   A 119 ? 0.3898 0.3084 0.3036 -0.0398 0.0961  0.0538  133 VAL   A CG2 
907  N N   . LYS   A 120 ? 0.3016 0.2530 0.2119 -0.1207 0.0653  -0.0059 134 LYS   A N   
908  C CA  . LYS   A 120 ? 0.3864 0.2623 0.2042 -0.0970 0.0745  0.0128  134 LYS   A CA  
909  C C   . LYS   A 120 ? 0.4626 0.2855 0.2248 -0.1373 0.1085  0.0089  134 LYS   A C   
910  O O   . LYS   A 120 ? 0.4820 0.3089 0.2124 -0.1286 0.1058  -0.0061 134 LYS   A O   
911  C CB  . LYS   A 120 ? 0.3471 0.2448 0.1900 -0.1010 0.0655  0.0167  134 LYS   A CB  
912  C CG  . LYS   A 120 ? 0.3404 0.2531 0.2410 -0.0945 0.0435  0.0145  134 LYS   A CG  
913  C CD  . LYS   A 120 ? 0.3507 0.2772 0.2885 -0.0953 0.0199  0.0141  134 LYS   A CD  
914  C CE  . LYS   A 120 ? 0.3767 0.3037 0.3325 -0.0892 0.0100  0.0152  134 LYS   A CE  
915  N NZ  . LYS   A 120 ? 0.3752 0.3205 0.3909 -0.0988 0.0058  0.0146  134 LYS   A NZ  
916  N N   . PRO   A 121 ? 0.5263 0.2879 0.2747 -0.1517 0.1372  0.0040  135 PRO   A N   
917  C CA  . PRO   A 121 ? 0.5611 0.2933 0.2948 -0.1582 0.1451  0.0045  135 PRO   A CA  
918  C C   . PRO   A 121 ? 0.5823 0.3033 0.3232 -0.1585 0.1758  -0.0086 135 PRO   A C   
919  O O   . PRO   A 121 ? 0.5870 0.3021 0.3228 -0.1520 0.2012  -0.0516 135 PRO   A O   
920  C CB  . PRO   A 121 ? 0.5595 0.2926 0.2989 -0.1628 0.1379  0.0075  135 PRO   A CB  
921  C CG  . PRO   A 121 ? 0.5626 0.2875 0.3032 -0.1637 0.1340  0.0089  135 PRO   A CG  
922  C CD  . PRO   A 121 ? 0.5389 0.2846 0.2842 -0.1587 0.1386  -0.0007 135 PRO   A CD  
923  O OXT . PRO   A 121 ? 0.6320 0.3158 0.3248 -0.1468 0.1508  -0.0033 135 PRO   A OXT 
924  N N   . ALA   B 1   ? 0.4353 0.3027 0.3355 0.0667  0.0447  -0.0144 15  ALA   B N   
925  C CA  . ALA   B 1   ? 0.3903 0.2961 0.3207 0.0479  0.0264  -0.0034 15  ALA   B CA  
926  C C   . ALA   B 1   ? 0.3141 0.2893 0.2797 0.0292  0.0256  -0.0003 15  ALA   B C   
927  O O   . ALA   B 1   ? 0.3544 0.2989 0.2574 0.0378  0.0381  0.0068  15  ALA   B O   
928  C CB  . ALA   B 1   ? 0.4292 0.2985 0.3300 0.0481  0.0148  0.0052  15  ALA   B CB  
929  N N   . GLY   B 2   ? 0.2264 0.2747 0.2695 0.0050  0.0209  0.0078  16  GLY   B N   
930  C CA  . GLY   B 2   ? 0.1823 0.2475 0.2291 -0.0138 0.0190  0.0069  16  GLY   B CA  
931  C C   . GLY   B 2   ? 0.1795 0.2263 0.1960 -0.0114 0.0104  0.0069  16  GLY   B C   
932  O O   . GLY   B 2   ? 0.2069 0.2203 0.1972 -0.0265 0.0148  0.0076  16  GLY   B O   
933  N N   . ILE   B 3   ? 0.1629 0.2143 0.1908 -0.0112 0.0086  0.0039  17  ILE   B N   
934  C CA  . ILE   B 3   ? 0.1634 0.1927 0.1340 0.0052  -0.0029 0.0055  17  ILE   B CA  
935  C C   . ILE   B 3   ? 0.1801 0.1867 0.1442 -0.0115 0.0127  -0.0149 17  ILE   B C   
936  O O   . ILE   B 3   ? 0.1705 0.1698 0.1549 -0.0103 0.0255  -0.0120 17  ILE   B O   
937  C CB  . ILE   B 3   ? 0.1712 0.1916 0.1404 -0.0049 -0.0155 0.0065  17  ILE   B CB  
938  C CG1 . ILE   B 3   ? 0.2024 0.2006 0.1518 0.0137  -0.0316 0.0009  17  ILE   B CG1 
939  C CG2 . ILE   B 3   ? 0.1525 0.1968 0.1599 0.0029  -0.0003 0.0047  17  ILE   B CG2 
940  C CD1 . ILE   B 3   ? 0.2230 0.2173 0.1648 0.0242  -0.0229 0.0018  17  ILE   B CD1 
941  N N   . THR   B 4   ? 0.1887 0.1835 0.1264 0.0072  0.0055  -0.0070 18  THR   B N   
942  C CA  . THR   B 4   ? 0.1861 0.1802 0.1297 0.0000  -0.0024 -0.0116 18  THR   B CA  
943  C C   . THR   B 4   ? 0.1695 0.1812 0.1339 -0.0001 0.0213  0.0122  18  THR   B C   
944  O O   . THR   B 4   ? 0.1903 0.1947 0.1511 -0.0095 0.0273  0.0079  18  THR   B O   
945  C CB  . THR   B 4   ? 0.1984 0.1795 0.1406 -0.0075 0.0079  -0.0168 18  THR   B CB  
946  O OG1 . THR   B 4   ? 0.2134 0.1708 0.1403 -0.0046 0.0372  0.0012  18  THR   B OG1 
947  C CG2 . THR   B 4   ? 0.2271 0.1908 0.1585 -0.0234 0.0042  -0.0299 18  THR   B CG2 
948  N N   . GLY   B 5   ? 0.1780 0.1817 0.1164 0.0103  0.0198  0.0169  19  GLY   B N   
949  C CA  . GLY   B 5   ? 0.1967 0.1850 0.1255 0.0126  0.0326  0.0154  19  GLY   B CA  
950  C C   . GLY   B 5   ? 0.1942 0.1812 0.1204 -0.0138 0.0304  0.0055  19  GLY   B C   
951  O O   . GLY   B 5   ? 0.1842 0.1825 0.1350 -0.0117 0.0234  0.0110  19  GLY   B O   
952  N N   . THR   B 6   ? 0.2213 0.1789 0.1188 -0.0060 0.0211  0.0157  20  THR   B N   
953  C CA  . THR   B 6   ? 0.2340 0.1862 0.1118 0.0020  0.0112  0.0074  20  THR   B CA  
954  C C   . THR   B 6   ? 0.2068 0.1867 0.1243 -0.0191 0.0305  0.0162  20  THR   B C   
955  O O   . THR   B 6   ? 0.2398 0.2077 0.1449 -0.0404 0.0498  0.0221  20  THR   B O   
956  C CB  . THR   B 6   ? 0.2668 0.2066 0.1101 0.0339  -0.0146 -0.0156 20  THR   B CB  
957  O OG1 . THR   B 6   ? 0.3336 0.2265 0.1404 0.0600  -0.0349 -0.0167 20  THR   B OG1 
958  C CG2 . THR   B 6   ? 0.2402 0.2160 0.1362 0.0314  -0.0216 -0.0158 20  THR   B CG2 
959  N N   . TRP   B 7   ? 0.1904 0.1728 0.1080 -0.0129 0.0086  0.0093  21  TRP   B N   
960  C CA  . TRP   B 7   ? 0.2009 0.1696 0.1240 -0.0050 0.0037  0.0084  21  TRP   B CA  
961  C C   . TRP   B 7   ? 0.2143 0.1598 0.1471 -0.0067 -0.0071 0.0142  21  TRP   B C   
962  O O   . TRP   B 7   ? 0.2114 0.1611 0.1621 -0.0121 0.0228  0.0179  21  TRP   B O   
963  C CB  . TRP   B 7   ? 0.1960 0.1664 0.1198 0.0010  -0.0176 -0.0018 21  TRP   B CB  
964  C CG  . TRP   B 7   ? 0.1922 0.1726 0.1176 -0.0051 0.0032  -0.0136 21  TRP   B CG  
965  C CD1 . TRP   B 7   ? 0.1905 0.1729 0.1201 -0.0048 0.0073  -0.0127 21  TRP   B CD1 
966  C CD2 . TRP   B 7   ? 0.1667 0.1768 0.1138 -0.0187 0.0048  -0.0124 21  TRP   B CD2 
967  N NE1 . TRP   B 7   ? 0.1818 0.1777 0.1248 -0.0102 0.0168  -0.0137 21  TRP   B NE1 
968  C CE2 . TRP   B 7   ? 0.1639 0.1889 0.1228 -0.0222 0.0229  -0.0212 21  TRP   B CE2 
969  C CE3 . TRP   B 7   ? 0.1766 0.1940 0.1235 -0.0295 0.0013  -0.0057 21  TRP   B CE3 
970  C CZ2 . TRP   B 7   ? 0.1680 0.1970 0.1303 -0.0207 0.0176  -0.0002 21  TRP   B CZ2 
971  C CZ3 . TRP   B 7   ? 0.1696 0.2051 0.1496 -0.0229 0.0049  0.0060  21  TRP   B CZ3 
972  C CH2 . TRP   B 7   ? 0.1565 0.2042 0.1597 -0.0247 0.0140  -0.0112 21  TRP   B CH2 
973  N N   . TYR   B 8   ? 0.2566 0.1616 0.1354 0.0170  -0.0238 0.0175  22  TYR   B N   
974  C CA  A TYR   B 8   ? 0.2716 0.1707 0.1510 0.0352  -0.0223 0.0184  22  TYR   B CA  
975  C CA  B TYR   B 8   ? 0.2822 0.1726 0.1591 0.0294  -0.0436 0.0238  22  TYR   B CA  
976  C C   . TYR   B 8   ? 0.2701 0.1798 0.1841 0.0499  -0.0343 0.0013  22  TYR   B C   
977  O O   . TYR   B 8   ? 0.2595 0.1860 0.1911 0.0453  -0.0556 0.0093  22  TYR   B O   
978  C CB  A TYR   B 8   ? 0.2675 0.1847 0.1574 0.0160  -0.0028 0.0139  22  TYR   B CB  
979  C CB  B TYR   B 8   ? 0.3070 0.1850 0.1696 0.0069  -0.0697 0.0399  22  TYR   B CB  
980  C CG  A TYR   B 8   ? 0.2082 0.1890 0.1487 0.0196  -0.0081 0.0055  22  TYR   B CG  
981  C CG  B TYR   B 8   ? 0.2895 0.1901 0.1685 -0.0034 -0.0955 0.0484  22  TYR   B CG  
982  C CD1 A TYR   B 8   ? 0.2047 0.2070 0.1589 0.0344  0.0098  0.0060  22  TYR   B CD1 
983  C CD1 B TYR   B 8   ? 0.2917 0.1966 0.1546 -0.0084 -0.0809 0.0560  22  TYR   B CD1 
984  C CD2 A TYR   B 8   ? 0.1905 0.1955 0.1298 0.0007  -0.0508 0.0261  22  TYR   B CD2 
985  C CD2 B TYR   B 8   ? 0.2826 0.1941 0.1800 -0.0126 -0.0858 0.0559  22  TYR   B CD2 
986  C CE1 A TYR   B 8   ? 0.1835 0.2129 0.1573 0.0200  0.0370  0.0234  22  TYR   B CE1 
987  C CE1 B TYR   B 8   ? 0.2915 0.2036 0.1698 -0.0108 -0.0819 0.0463  22  TYR   B CE1 
988  C CE2 A TYR   B 8   ? 0.1749 0.2077 0.1471 -0.0058 -0.0342 0.0323  22  TYR   B CE2 
989  C CE2 B TYR   B 8   ? 0.2783 0.1982 0.1808 -0.0212 -0.0867 0.0506  22  TYR   B CE2 
990  C CZ  A TYR   B 8   ? 0.1864 0.2145 0.1608 0.0098  0.0059  0.0396  22  TYR   B CZ  
991  C CZ  B TYR   B 8   ? 0.2727 0.2031 0.1803 -0.0266 -0.0844 0.0343  22  TYR   B CZ  
992  O OH  A TYR   B 8   ? 0.1825 0.2257 0.1594 0.0173  0.0103  0.0567  22  TYR   B OH  
993  O OH  B TYR   B 8   ? 0.2616 0.2053 0.1661 -0.0326 -0.1035 0.0083  22  TYR   B OH  
994  N N   . ASN   B 9   ? 0.2622 0.1996 0.1869 0.0637  -0.0645 -0.0102 23  ASN   B N   
995  C CA  . ASN   B 9   ? 0.2778 0.2197 0.2185 0.0530  -0.0448 -0.0264 23  ASN   B CA  
996  C C   . ASN   B 9   ? 0.2859 0.2143 0.2159 0.0468  -0.0559 -0.0203 23  ASN   B C   
997  O O   . ASN   B 9   ? 0.3458 0.1993 0.2299 0.0602  -0.0605 -0.0040 23  ASN   B O   
998  C CB  . ASN   B 9   ? 0.2795 0.2445 0.2350 0.0684  -0.0493 -0.0198 23  ASN   B CB  
999  C CG  . ASN   B 9   ? 0.2711 0.2670 0.2628 0.0431  -0.0701 -0.0362 23  ASN   B CG  
1000 O OD1 . ASN   B 9   ? 0.2494 0.2454 0.3026 0.0530  -0.0675 -0.0346 23  ASN   B OD1 
1001 N ND2 . ASN   B 9   ? 0.2712 0.2907 0.2752 0.0408  -0.0663 -0.0379 23  ASN   B ND2 
1002 N N   . GLN   B 10  ? 0.2719 0.2160 0.2231 0.0395  -0.0384 -0.0349 24  GLN   B N   
1003 C CA  . GLN   B 10  ? 0.3145 0.2359 0.2324 0.0368  0.0020  -0.0341 24  GLN   B CA  
1004 C C   . GLN   B 10  ? 0.3310 0.2408 0.2533 0.0518  -0.0027 -0.0403 24  GLN   B C   
1005 O O   . GLN   B 10  ? 0.3629 0.2539 0.2892 0.0413  -0.0064 -0.0212 24  GLN   B O   
1006 C CB  . GLN   B 10  ? 0.3389 0.2458 0.2240 0.0347  0.0092  -0.0333 24  GLN   B CB  
1007 C CG  . GLN   B 10  ? 0.3143 0.2458 0.2388 0.0428  0.0194  -0.0080 24  GLN   B CG  
1008 C CD  . GLN   B 10  ? 0.2644 0.2483 0.2496 0.0444  0.0213  -0.0005 24  GLN   B CD  
1009 O OE1 . GLN   B 10  ? 0.2059 0.2294 0.2016 0.0580  -0.0050 0.0046  24  GLN   B OE1 
1010 N NE2 . GLN   B 10  ? 0.2921 0.2670 0.2844 0.0381  0.0150  -0.0083 24  GLN   B NE2 
1011 N N   . LEU   B 11  ? 0.3161 0.2532 0.2734 0.0641  -0.0163 -0.0549 25  LEU   B N   
1012 C CA  . LEU   B 11  ? 0.3364 0.2603 0.2554 0.0685  -0.0157 -0.0342 25  LEU   B CA  
1013 C C   . LEU   B 11  ? 0.3381 0.2793 0.2843 0.0566  -0.0109 -0.0254 25  LEU   B C   
1014 O O   . LEU   B 11  ? 0.3714 0.3154 0.3423 0.0543  -0.0189 -0.0183 25  LEU   B O   
1015 C CB  . LEU   B 11  ? 0.3851 0.2683 0.2470 0.0574  0.0003  -0.0169 25  LEU   B CB  
1016 C CG  . LEU   B 11  ? 0.4455 0.2765 0.2729 0.0413  0.0026  -0.0202 25  LEU   B CG  
1017 C CD1 . LEU   B 11  ? 0.4697 0.2859 0.2988 0.0261  0.0122  -0.0079 25  LEU   B CD1 
1018 C CD2 . LEU   B 11  ? 0.4605 0.2700 0.2832 0.0316  0.0116  -0.0309 25  LEU   B CD2 
1019 N N   . GLY   B 12  ? 0.3386 0.2633 0.2245 0.0279  -0.0071 -0.0125 26  GLY   B N   
1020 C CA  . GLY   B 12  ? 0.3568 0.2598 0.2096 0.0014  -0.0406 -0.0058 26  GLY   B CA  
1021 C C   . GLY   B 12  ? 0.3414 0.2478 0.2186 0.0183  -0.0319 0.0016  26  GLY   B C   
1022 O O   . GLY   B 12  ? 0.3800 0.2609 0.2242 0.0105  -0.0517 0.0356  26  GLY   B O   
1023 N N   . SER   B 13  ? 0.2592 0.2256 0.2206 0.0422  -0.0269 -0.0146 27  SER   B N   
1024 C CA  A SER   B 13  ? 0.2254 0.2227 0.2285 0.0432  -0.0251 -0.0022 27  SER   B CA  
1025 C CA  B SER   B 13  ? 0.2398 0.2171 0.2261 0.0424  -0.0274 -0.0039 27  SER   B CA  
1026 C C   . SER   B 13  ? 0.2119 0.2193 0.2114 0.0447  -0.0299 -0.0012 27  SER   B C   
1027 O O   . SER   B 13  ? 0.2201 0.2228 0.2150 0.0357  -0.0224 -0.0077 27  SER   B O   
1028 C CB  A SER   B 13  ? 0.2144 0.2295 0.2594 0.0559  0.0185  0.0202  27  SER   B CB  
1029 C CB  B SER   B 13  ? 0.2480 0.2101 0.2452 0.0453  -0.0160 0.0080  27  SER   B CB  
1030 O OG  A SER   B 13  ? 0.2358 0.2462 0.2870 0.0583  0.0510  0.0279  27  SER   B OG  
1031 O OG  B SER   B 13  ? 0.2630 0.2094 0.2627 0.0417  -0.0132 0.0125  27  SER   B OG  
1032 N N   . THR   B 14  ? 0.2277 0.2082 0.1965 0.0600  -0.0038 -0.0067 28  THR   B N   
1033 C CA  . THR   B 14  ? 0.2636 0.2182 0.1866 0.0651  0.0071  0.0123  28  THR   B CA  
1034 C C   . THR   B 14  ? 0.2128 0.1987 0.2124 0.0144  -0.0023 0.0031  28  THR   B C   
1035 O O   . THR   B 14  ? 0.1852 0.2196 0.2433 -0.0040 0.0126  -0.0167 28  THR   B O   
1036 C CB  . THR   B 14  ? 0.3756 0.2492 0.1991 0.0939  0.0051  0.0168  28  THR   B CB  
1037 O OG1 . THR   B 14  ? 0.4624 0.2648 0.2231 0.0988  -0.0077 0.0283  28  THR   B OG1 
1038 C CG2 . THR   B 14  ? 0.3977 0.2658 0.2094 0.1001  0.0161  0.0154  28  THR   B CG2 
1039 N N   A PHE   B 15  ? 0.1980 0.1726 0.2264 0.0126  0.0023  -0.0005 29  PHE   B N   
1040 N N   B PHE   B 15  ? 0.2046 0.1959 0.2194 0.0141  -0.0001 0.0056  29  PHE   B N   
1041 C CA  A PHE   B 15  ? 0.2128 0.1996 0.2292 0.0053  0.0095  0.0005  29  PHE   B CA  
1042 C CA  B PHE   B 15  ? 0.1991 0.1928 0.2257 0.0101  0.0052  0.0056  29  PHE   B CA  
1043 C C   A PHE   B 15  ? 0.2183 0.1865 0.2240 -0.0180 0.0660  0.0015  29  PHE   B C   
1044 C C   B PHE   B 15  ? 0.1974 0.1906 0.2342 0.0082  0.0086  0.0084  29  PHE   B C   
1045 O O   A PHE   B 15  ? 0.2348 0.1860 0.2676 -0.0364 0.1046  -0.0202 29  PHE   B O   
1046 O O   B PHE   B 15  ? 0.1969 0.1884 0.2367 0.0071  0.0075  0.0085  29  PHE   B O   
1047 C CB  A PHE   B 15  ? 0.2128 0.2213 0.2222 -0.0206 0.0382  0.0126  29  PHE   B CB  
1048 C CB  B PHE   B 15  ? 0.1962 0.1929 0.2222 0.0097  0.0027  0.0039  29  PHE   B CB  
1049 C CG  A PHE   B 15  ? 0.2027 0.2227 0.2067 -0.0398 0.0502  0.0215  29  PHE   B CG  
1050 C CG  B PHE   B 15  ? 0.1941 0.1953 0.2171 0.0090  -0.0001 0.0031  29  PHE   B CG  
1051 C CD1 A PHE   B 15  ? 0.2190 0.2205 0.1880 -0.0243 0.0463  0.0305  29  PHE   B CD1 
1052 C CD1 B PHE   B 15  ? 0.1931 0.1966 0.2148 0.0087  -0.0015 0.0033  29  PHE   B CD1 
1053 C CD2 A PHE   B 15  ? 0.2178 0.2291 0.1941 -0.0541 -0.0104 0.0526  29  PHE   B CD2 
1054 C CD2 B PHE   B 15  ? 0.1931 0.1966 0.2148 0.0087  -0.0015 0.0033  29  PHE   B CD2 
1055 C CE1 A PHE   B 15  ? 0.2346 0.2310 0.1796 -0.0445 0.0146  0.0137  29  PHE   B CE1 
1056 C CE1 B PHE   B 15  ? 0.1922 0.1971 0.2146 0.0091  -0.0024 0.0045  29  PHE   B CE1 
1057 C CE2 A PHE   B 15  ? 0.2229 0.2343 0.1823 -0.0455 -0.0081 0.0130  29  PHE   B CE2 
1058 C CE2 B PHE   B 15  ? 0.1922 0.1971 0.2146 0.0091  -0.0024 0.0045  29  PHE   B CE2 
1059 C CZ  A PHE   B 15  ? 0.2347 0.2312 0.1568 -0.0419 -0.0119 0.0113  29  PHE   B CZ  
1060 C CZ  B PHE   B 15  ? 0.1919 0.1971 0.2150 0.0094  -0.0025 0.0051  29  PHE   B CZ  
1061 N N   . ILE   B 16  ? 0.1988 0.1910 0.2444 0.0109  0.0180  0.0115  30  ILE   B N   
1062 C CA  . ILE   B 16  ? 0.1828 0.2123 0.2024 -0.0122 -0.0137 0.0254  30  ILE   B CA  
1063 C C   . ILE   B 16  ? 0.1709 0.1847 0.2335 0.0068  0.0027  0.0402  30  ILE   B C   
1064 O O   . ILE   B 16  ? 0.1794 0.1821 0.3392 0.0043  0.0088  0.0558  30  ILE   B O   
1065 C CB  . ILE   B 16  ? 0.2095 0.2497 0.2151 0.0097  -0.0086 0.0092  30  ILE   B CB  
1066 C CG1 . ILE   B 16  ? 0.2277 0.2645 0.2504 0.0352  -0.0598 0.0053  30  ILE   B CG1 
1067 C CG2 . ILE   B 16  ? 0.2150 0.2777 0.1781 0.0157  0.0442  -0.0071 30  ILE   B CG2 
1068 C CD1 . ILE   B 16  ? 0.2724 0.2857 0.2759 0.0285  -0.0461 -0.0033 30  ILE   B CD1 
1069 N N   . VAL   B 17  ? 0.1709 0.1576 0.1738 -0.0090 -0.0027 0.0107  31  VAL   B N   
1070 C CA  . VAL   B 17  ? 0.1648 0.1587 0.1649 -0.0063 -0.0011 0.0128  31  VAL   B CA  
1071 C C   . VAL   B 17  ? 0.1886 0.1564 0.1432 -0.0208 -0.0075 0.0208  31  VAL   B C   
1072 O O   . VAL   B 17  ? 0.1827 0.1653 0.1531 -0.0285 0.0049  0.0265  31  VAL   B O   
1073 C CB  . VAL   B 17  ? 0.1900 0.1636 0.1680 -0.0367 -0.0089 0.0169  31  VAL   B CB  
1074 C CG1 . VAL   B 17  ? 0.2123 0.1711 0.1589 -0.0459 -0.0139 0.0074  31  VAL   B CG1 
1075 C CG2 . VAL   B 17  ? 0.2037 0.1559 0.1665 -0.0120 0.0009  0.0232  31  VAL   B CG2 
1076 N N   . THR   B 18  ? 0.1760 0.1549 0.1598 -0.0006 -0.0056 0.0003  32  THR   B N   
1077 C CA  . THR   B 18  ? 0.1947 0.1750 0.1328 -0.0123 -0.0092 -0.0022 32  THR   B CA  
1078 C C   . THR   B 18  ? 0.1773 0.1645 0.1252 -0.0164 0.0072  -0.0033 32  THR   B C   
1079 O O   . THR   B 18  ? 0.1546 0.1664 0.1516 -0.0060 0.0109  0.0040  32  THR   B O   
1080 C CB  . THR   B 18  ? 0.2484 0.2042 0.1631 -0.0111 -0.0088 -0.0170 32  THR   B CB  
1081 O OG1 . THR   B 18  ? 0.2901 0.2256 0.1928 -0.0366 -0.0439 -0.0122 32  THR   B OG1 
1082 C CG2 . THR   B 18  ? 0.2583 0.2087 0.1606 -0.0097 0.0153  -0.0369 32  THR   B CG2 
1083 N N   . ALA   B 19  ? 0.1614 0.1605 0.1357 0.0018  0.0080  -0.0080 33  ALA   B N   
1084 C CA  . ALA   B 19  ? 0.1617 0.1665 0.1491 0.0143  0.0201  -0.0156 33  ALA   B CA  
1085 C C   . ALA   B 19  ? 0.2062 0.1694 0.1385 0.0302  0.0473  -0.0150 33  ALA   B C   
1086 O O   . ALA   B 19  ? 0.2382 0.1890 0.1670 0.0273  0.0690  -0.0272 33  ALA   B O   
1087 C CB  . ALA   B 19  ? 0.1753 0.1727 0.1811 -0.0171 0.0049  -0.0117 33  ALA   B CB  
1088 N N   . GLY   B 20  ? 0.2111 0.1567 0.1413 0.0430  0.0312  -0.0166 34  GLY   B N   
1089 C CA  . GLY   B 20  ? 0.2405 0.1573 0.1570 0.0371  0.0321  -0.0355 34  GLY   B CA  
1090 C C   . GLY   B 20  ? 0.2293 0.1403 0.1324 0.0358  0.0472  -0.0336 34  GLY   B C   
1091 O O   . GLY   B 20  ? 0.2258 0.1416 0.1567 0.0214  0.0204  -0.0255 34  GLY   B O   
1092 N N   . ALA   B 21  ? 0.2341 0.1502 0.1664 0.0401  0.0579  -0.0119 35  ALA   B N   
1093 C CA  . ALA   B 21  ? 0.2393 0.1665 0.1867 0.0542  0.0448  -0.0218 35  ALA   B CA  
1094 C C   . ALA   B 21  ? 0.2408 0.1577 0.2027 0.0397  0.0516  -0.0213 35  ALA   B C   
1095 O O   . ALA   B 21  ? 0.2715 0.1527 0.2415 0.0034  0.0366  -0.0221 35  ALA   B O   
1096 C CB  . ALA   B 21  ? 0.2826 0.1830 0.1976 0.0575  0.0701  -0.0257 35  ALA   B CB  
1097 N N   . ASP   B 22  ? 0.2502 0.1552 0.1555 0.0139  0.0691  -0.0214 36  ASP   B N   
1098 C CA  . ASP   B 22  ? 0.2576 0.1591 0.1544 -0.0046 0.0626  -0.0300 36  ASP   B CA  
1099 C C   . ASP   B 22  ? 0.2301 0.1420 0.1686 0.0184  0.0570  -0.0233 36  ASP   B C   
1100 O O   . ASP   B 22  ? 0.2500 0.1453 0.1813 0.0173  0.0406  -0.0218 36  ASP   B O   
1101 C CB  . ASP   B 22  ? 0.2968 0.1816 0.1873 -0.0429 0.0519  -0.0526 36  ASP   B CB  
1102 C CG  . ASP   B 22  ? 0.3190 0.2164 0.2237 -0.0775 0.0383  -0.0605 36  ASP   B CG  
1103 O OD1 . ASP   B 22  ? 0.2891 0.2265 0.2078 -0.0490 0.0029  -0.0734 36  ASP   B OD1 
1104 O OD2 . ASP   B 22  ? 0.3565 0.2473 0.2708 -0.0891 0.0770  -0.0574 36  ASP   B OD2 
1105 N N   . GLY   B 23  ? 0.1942 0.1268 0.1676 0.0231  0.0332  -0.0319 37  GLY   B N   
1106 C CA  . GLY   B 23  ? 0.1699 0.1377 0.1654 0.0171  0.0292  -0.0298 37  GLY   B CA  
1107 C C   . GLY   B 23  ? 0.1536 0.1293 0.1486 0.0089  0.0210  -0.0257 37  GLY   B C   
1108 O O   . GLY   B 23  ? 0.1417 0.1270 0.1529 -0.0012 0.0074  -0.0254 37  GLY   B O   
1109 N N   . ALA   B 24  ? 0.1467 0.1251 0.1556 -0.0035 0.0205  -0.0203 38  ALA   B N   
1110 C CA  . ALA   B 24  ? 0.1614 0.1344 0.1647 0.0037  0.0022  -0.0101 38  ALA   B CA  
1111 C C   . ALA   B 24  ? 0.1676 0.1440 0.1428 -0.0043 0.0142  -0.0185 38  ALA   B C   
1112 O O   . ALA   B 24  ? 0.1891 0.1664 0.1472 0.0110  0.0365  -0.0076 38  ALA   B O   
1113 C CB  . ALA   B 24  ? 0.1991 0.1423 0.1966 -0.0229 -0.0129 -0.0438 38  ALA   B CB  
1114 N N   . LEU   B 25  ? 0.1399 0.1447 0.1373 -0.0027 -0.0076 -0.0221 39  LEU   B N   
1115 C CA  . LEU   B 25  ? 0.1428 0.1426 0.1348 0.0090  -0.0002 -0.0142 39  LEU   B CA  
1116 C C   . LEU   B 25  ? 0.1500 0.1487 0.1175 -0.0120 0.0040  -0.0102 39  LEU   B C   
1117 O O   . LEU   B 25  ? 0.1402 0.1596 0.1180 -0.0012 0.0180  -0.0151 39  LEU   B O   
1118 C CB  . LEU   B 25  ? 0.1503 0.1483 0.1279 0.0007  0.0110  -0.0209 39  LEU   B CB  
1119 C CG  . LEU   B 25  ? 0.1384 0.1511 0.1324 -0.0080 -0.0046 -0.0157 39  LEU   B CG  
1120 C CD1 . LEU   B 25  ? 0.1606 0.1601 0.1329 -0.0001 -0.0024 -0.0285 39  LEU   B CD1 
1121 C CD2 . LEU   B 25  ? 0.1425 0.1595 0.1318 -0.0139 0.0176  -0.0012 39  LEU   B CD2 
1122 N N   . THR   B 26  ? 0.1516 0.1385 0.1362 -0.0075 0.0036  -0.0175 40  THR   B N   
1123 C CA  A THR   B 26  ? 0.1662 0.1530 0.1301 -0.0072 -0.0007 -0.0164 40  THR   B CA  
1124 C CA  B THR   B 26  ? 0.1588 0.1501 0.1435 -0.0047 -0.0063 -0.0202 40  THR   B CA  
1125 C C   . THR   B 26  ? 0.1532 0.1597 0.1468 -0.0067 -0.0168 0.0043  40  THR   B C   
1126 O O   . THR   B 26  ? 0.1738 0.1841 0.2339 -0.0275 0.0150  0.0501  40  THR   B O   
1127 C CB  A THR   B 26  ? 0.1794 0.1515 0.1328 -0.0076 0.0153  -0.0217 40  THR   B CB  
1128 C CB  B THR   B 26  ? 0.1728 0.1491 0.1527 0.0039  0.0028  -0.0454 40  THR   B CB  
1129 O OG1 A THR   B 26  ? 0.1942 0.1653 0.1349 -0.0148 0.0208  -0.0247 40  THR   B OG1 
1130 O OG1 B THR   B 26  ? 0.1852 0.1476 0.1569 0.0069  0.0242  -0.0648 40  THR   B OG1 
1131 C CG2 A THR   B 26  ? 0.2115 0.1589 0.1653 -0.0192 0.0077  -0.0202 40  THR   B CG2 
1132 C CG2 B THR   B 26  ? 0.1807 0.1503 0.1639 0.0028  -0.0035 -0.0489 40  THR   B CG2 
1133 N N   . GLY   B 27  ? 0.1588 0.1471 0.1499 -0.0026 -0.0141 -0.0040 41  GLY   B N   
1134 C CA  . GLY   B 27  ? 0.1560 0.1642 0.1602 0.0105  -0.0002 0.0100  41  GLY   B CA  
1135 C C   . GLY   B 27  ? 0.1376 0.1776 0.1510 -0.0157 -0.0228 -0.0027 41  GLY   B C   
1136 O O   . GLY   B 27  ? 0.1517 0.1960 0.1448 -0.0213 -0.0199 -0.0074 41  GLY   B O   
1137 N N   . THR   B 28  ? 0.1455 0.1909 0.1625 0.0086  -0.0154 -0.0153 42  THR   B N   
1138 C CA  . THR   B 28  ? 0.1587 0.2109 0.1958 0.0209  -0.0428 -0.0222 42  THR   B CA  
1139 C C   . THR   B 28  ? 0.1408 0.2011 0.2084 0.0077  -0.0154 -0.0075 42  THR   B C   
1140 O O   . THR   B 28  ? 0.1413 0.2064 0.2701 0.0138  0.0130  -0.0040 42  THR   B O   
1141 C CB  . THR   B 28  ? 0.2308 0.2380 0.2295 -0.0035 -0.0565 -0.0244 42  THR   B CB  
1142 O OG1 . THR   B 28  ? 0.2789 0.2746 0.2598 0.0044  -0.0392 -0.0118 42  THR   B OG1 
1143 C CG2 . THR   B 28  ? 0.2539 0.2333 0.2182 -0.0008 -0.0978 -0.0238 42  THR   B CG2 
1144 N N   . TYR   B 29  ? 0.1681 0.1963 0.1787 0.0101  -0.0197 -0.0093 43  TYR   B N   
1145 C CA  . TYR   B 29  ? 0.1712 0.2028 0.1667 0.0157  -0.0409 -0.0070 43  TYR   B CA  
1146 C C   . TYR   B 29  ? 0.1676 0.2112 0.2097 0.0203  -0.0562 -0.0087 43  TYR   B C   
1147 O O   . TYR   B 29  ? 0.1725 0.2099 0.2245 0.0110  -0.0582 -0.0108 43  TYR   B O   
1148 C CB  . TYR   B 29  ? 0.1849 0.2041 0.1531 0.0026  -0.0123 0.0155  43  TYR   B CB  
1149 C CG  . TYR   B 29  ? 0.1749 0.2079 0.1310 0.0061  -0.0107 0.0008  43  TYR   B CG  
1150 C CD1 . TYR   B 29  ? 0.2183 0.2068 0.1485 0.0073  -0.0123 -0.0012 43  TYR   B CD1 
1151 C CD2 . TYR   B 29  ? 0.1934 0.2123 0.1085 0.0040  -0.0110 0.0128  43  TYR   B CD2 
1152 C CE1 . TYR   B 29  ? 0.2181 0.2057 0.1552 0.0200  -0.0147 0.0021  43  TYR   B CE1 
1153 C CE2 . TYR   B 29  ? 0.2061 0.2091 0.1105 -0.0010 0.0020  0.0104  43  TYR   B CE2 
1154 C CZ  . TYR   B 29  ? 0.2276 0.2074 0.1408 -0.0145 -0.0201 0.0009  43  TYR   B CZ  
1155 O OH  . TYR   B 29  ? 0.2551 0.2180 0.1554 -0.0205 -0.0305 0.0215  43  TYR   B OH  
1156 N N   . GLU   B 30  ? 0.2002 0.2386 0.2627 0.0545  -0.0636 -0.0121 44  GLU   B N   
1157 C CA  . GLU   B 30  ? 0.2413 0.2803 0.3479 0.0718  -0.0708 -0.0222 44  GLU   B CA  
1158 C C   . GLU   B 30  ? 0.2497 0.2894 0.4064 0.0749  -0.0518 -0.0420 44  GLU   B C   
1159 O O   . GLU   B 30  ? 0.2085 0.2671 0.4110 0.0676  -0.0455 -0.0397 44  GLU   B O   
1160 C CB  . GLU   B 30  ? 0.3467 0.3153 0.3833 0.1018  -0.0806 -0.0057 44  GLU   B CB  
1161 C CG  . GLU   B 30  ? 0.4459 0.3496 0.4274 0.1064  -0.0481 0.0111  44  GLU   B CG  
1162 C CD  . GLU   B 30  ? 0.4990 0.3720 0.4420 0.1169  -0.0574 0.0332  44  GLU   B CD  
1163 O OE1 . GLU   B 30  ? 0.5286 0.3822 0.4627 0.1226  -0.0489 0.0315  44  GLU   B OE1 
1164 O OE2 . GLU   B 30  ? 0.5056 0.3848 0.4410 0.1143  -0.0783 0.0397  44  GLU   B OE2 
1165 N N   . SER   B 31  ? 0.3494 0.3276 0.4705 0.0659  0.0056  -0.0725 45  SER   B N   
1166 C CA  . SER   B 31  ? 0.4587 0.3663 0.5287 0.0502  0.0302  -0.0868 45  SER   B CA  
1167 C C   . SER   B 31  ? 0.5082 0.3885 0.5600 0.0416  0.0472  -0.0885 45  SER   B C   
1168 O O   . SER   B 31  ? 0.5277 0.3993 0.5723 0.0478  0.0610  -0.0865 45  SER   B O   
1169 C CB  . SER   B 31  ? 0.4957 0.3745 0.5451 0.0450  0.0115  -0.0850 45  SER   B CB  
1170 O OG  . SER   B 31  ? 0.5384 0.3825 0.5564 0.0302  0.0052  -0.0935 45  SER   B OG  
1171 N N   . ASN   B 35  ? 0.5785 0.5615 0.5442 0.0242  -0.0521 0.0703  49  ASN   B N   
1172 C CA  . ASN   B 35  ? 0.5660 0.5631 0.5437 0.0268  -0.0528 0.0691  49  ASN   B CA  
1173 C C   . ASN   B 35  ? 0.5362 0.5518 0.5139 0.0302  -0.0452 0.0681  49  ASN   B C   
1174 O O   . ASN   B 35  ? 0.5276 0.5557 0.5108 0.0379  -0.0456 0.0773  49  ASN   B O   
1175 C CB  . ASN   B 35  ? 0.5851 0.5775 0.5747 0.0235  -0.0544 0.0637  49  ASN   B CB  
1176 C CG  . ASN   B 35  ? 0.6058 0.5898 0.6002 0.0189  -0.0516 0.0579  49  ASN   B CG  
1177 O OD1 . ASN   B 35  ? 0.6055 0.5977 0.6210 0.0127  -0.0376 0.0486  49  ASN   B OD1 
1178 N ND2 . ASN   B 35  ? 0.6230 0.5940 0.6012 0.0218  -0.0532 0.0615  49  ASN   B ND2 
1179 N N   . ALA   B 36  ? 0.5100 0.5350 0.4738 0.0340  -0.0522 0.0611  50  ALA   B N   
1180 C CA  . ALA   B 36  ? 0.4784 0.5170 0.4504 0.0310  -0.0520 0.0434  50  ALA   B CA  
1181 C C   . ALA   B 36  ? 0.4051 0.4895 0.4227 0.0592  -0.0758 0.0414  50  ALA   B C   
1182 O O   . ALA   B 36  ? 0.3482 0.4834 0.4234 0.0797  -0.0904 0.0334  50  ALA   B O   
1183 C CB  . ALA   B 36  ? 0.4948 0.5222 0.4427 0.0163  -0.0504 0.0390  50  ALA   B CB  
1184 N N   . GLU   B 37  ? 0.3569 0.4671 0.3952 0.0696  -0.1027 0.0480  51  GLU   B N   
1185 C CA  . GLU   B 37  ? 0.3376 0.4430 0.3874 0.0799  -0.0972 0.0578  51  GLU   B CA  
1186 C C   . GLU   B 37  ? 0.3147 0.4055 0.3506 0.0731  -0.0774 0.0702  51  GLU   B C   
1187 O O   . GLU   B 37  ? 0.3263 0.4027 0.3490 0.0589  -0.0358 0.0760  51  GLU   B O   
1188 C CB  . GLU   B 37  ? 0.3608 0.4512 0.4256 0.0913  -0.0845 0.0520  51  GLU   B CB  
1189 C CG  . GLU   B 37  ? 0.3971 0.4589 0.4571 0.0879  -0.0699 0.0337  51  GLU   B CG  
1190 C CD  . GLU   B 37  ? 0.4222 0.4617 0.4757 0.0846  -0.0428 0.0184  51  GLU   B CD  
1191 O OE1 . GLU   B 37  ? 0.4317 0.4627 0.4794 0.0849  -0.0366 0.0119  51  GLU   B OE1 
1192 O OE2 . GLU   B 37  ? 0.4298 0.4623 0.4849 0.0823  -0.0267 0.0138  51  GLU   B OE2 
1193 N N   . SER   B 38  ? 0.2844 0.3693 0.3251 0.0736  -0.0764 0.0697  52  SER   B N   
1194 C CA  . SER   B 38  ? 0.2920 0.3449 0.3247 0.0521  -0.0505 0.0455  52  SER   B CA  
1195 C C   . SER   B 38  ? 0.2198 0.3179 0.2594 0.0393  -0.0483 0.0394  52  SER   B C   
1196 O O   . SER   B 38  ? 0.2191 0.3125 0.2500 0.0142  -0.0300 0.0404  52  SER   B O   
1197 C CB  . SER   B 38  ? 0.3750 0.3570 0.3774 0.0402  -0.0177 0.0382  52  SER   B CB  
1198 O OG  . SER   B 38  ? 0.4445 0.3654 0.4219 0.0299  -0.0258 0.0311  52  SER   B OG  
1199 N N   . ARG   B 39  ? 0.2186 0.3032 0.2347 0.0282  -0.0332 0.0274  53  ARG   B N   
1200 C CA  . ARG   B 39  ? 0.2184 0.2959 0.2178 0.0222  -0.0281 0.0156  53  ARG   B CA  
1201 C C   . ARG   B 39  ? 0.1541 0.2619 0.1794 0.0134  -0.0319 -0.0027 53  ARG   B C   
1202 O O   . ARG   B 39  ? 0.1468 0.2656 0.1957 0.0017  -0.0415 -0.0043 53  ARG   B O   
1203 C CB  . ARG   B 39  ? 0.2820 0.3326 0.2484 0.0242  -0.0290 0.0131  53  ARG   B CB  
1204 C CG  . ARG   B 39  ? 0.3544 0.3683 0.3048 0.0233  -0.0303 -0.0052 53  ARG   B CG  
1205 C CD  . ARG   B 39  ? 0.4218 0.3991 0.3662 0.0224  -0.0332 -0.0055 53  ARG   B CD  
1206 N NE  . ARG   B 39  ? 0.4847 0.4189 0.4178 0.0287  -0.0219 -0.0090 53  ARG   B NE  
1207 C CZ  . ARG   B 39  ? 0.5141 0.4297 0.4556 0.0293  -0.0253 -0.0110 53  ARG   B CZ  
1208 N NH1 . ARG   B 39  ? 0.5083 0.4335 0.4666 0.0320  -0.0320 -0.0151 53  ARG   B NH1 
1209 N NH2 . ARG   B 39  ? 0.5349 0.4358 0.4837 0.0257  -0.0265 -0.0134 53  ARG   B NH2 
1210 N N   . TYR   B 40  ? 0.1412 0.2358 0.1467 0.0230  -0.0237 -0.0075 54  TYR   B N   
1211 C CA  . TYR   B 40  ? 0.1460 0.2247 0.1311 0.0101  -0.0184 -0.0135 54  TYR   B CA  
1212 C C   . TYR   B 40  ? 0.1455 0.2180 0.1380 0.0069  -0.0068 -0.0132 54  TYR   B C   
1213 O O   . TYR   B 40  ? 0.1524 0.2150 0.1561 0.0103  -0.0004 -0.0041 54  TYR   B O   
1214 C CB  . TYR   B 40  ? 0.1558 0.2219 0.1289 0.0176  -0.0246 -0.0187 54  TYR   B CB  
1215 C CG  . TYR   B 40  ? 0.1612 0.2203 0.1401 0.0104  -0.0236 -0.0209 54  TYR   B CG  
1216 C CD1 . TYR   B 40  ? 0.2031 0.2278 0.1303 0.0224  -0.0407 -0.0204 54  TYR   B CD1 
1217 C CD2 . TYR   B 40  ? 0.1440 0.2324 0.1444 0.0104  -0.0195 -0.0301 54  TYR   B CD2 
1218 C CE1 . TYR   B 40  ? 0.2168 0.2416 0.1599 0.0170  -0.0211 -0.0085 54  TYR   B CE1 
1219 C CE2 . TYR   B 40  ? 0.1589 0.2431 0.1595 0.0292  -0.0390 -0.0291 54  TYR   B CE2 
1220 C CZ  . TYR   B 40  ? 0.1892 0.2486 0.1768 0.0424  -0.0167 -0.0122 54  TYR   B CZ  
1221 O OH  . TYR   B 40  ? 0.2209 0.2568 0.2025 0.0659  0.0089  0.0053  54  TYR   B OH  
1222 N N   . VAL   B 41  ? 0.1368 0.2166 0.1260 0.0066  -0.0150 -0.0228 55  VAL   B N   
1223 C CA  . VAL   B 41  ? 0.1478 0.2177 0.1354 0.0205  -0.0110 -0.0284 55  VAL   B CA  
1224 C C   . VAL   B 41  ? 0.1392 0.2062 0.1428 0.0266  -0.0049 -0.0135 55  VAL   B C   
1225 O O   . VAL   B 41  ? 0.1672 0.2072 0.1386 0.0307  -0.0119 -0.0179 55  VAL   B O   
1226 C CB  . VAL   B 41  ? 0.1719 0.2276 0.1387 0.0134  0.0169  -0.0270 55  VAL   B CB  
1227 C CG1 . VAL   B 41  ? 0.1752 0.2258 0.1621 0.0277  -0.0049 -0.0302 55  VAL   B CG1 
1228 C CG2 . VAL   B 41  ? 0.2032 0.2502 0.1315 -0.0113 -0.0034 -0.0370 55  VAL   B CG2 
1229 N N   . LEU   B 42  ? 0.1361 0.2133 0.1302 0.0074  -0.0185 -0.0355 56  LEU   B N   
1230 C CA  . LEU   B 42  ? 0.1502 0.2190 0.1529 0.0151  -0.0309 -0.0382 56  LEU   B CA  
1231 C C   . LEU   B 42  ? 0.1552 0.2157 0.1437 0.0221  -0.0147 -0.0438 56  LEU   B C   
1232 O O   . LEU   B 42  ? 0.1765 0.2126 0.1425 0.0366  -0.0214 -0.0525 56  LEU   B O   
1233 C CB  . LEU   B 42  ? 0.1753 0.2199 0.1825 -0.0088 -0.0085 -0.0326 56  LEU   B CB  
1234 C CG  . LEU   B 42  ? 0.1853 0.2191 0.1558 -0.0131 -0.0035 -0.0076 56  LEU   B CG  
1235 C CD1 . LEU   B 42  ? 0.1613 0.2264 0.1686 0.0220  -0.0100 -0.0073 56  LEU   B CD1 
1236 C CD2 . LEU   B 42  ? 0.2467 0.2287 0.1911 -0.0177 -0.0361 -0.0079 56  LEU   B CD2 
1237 N N   . THR   B 43  ? 0.1345 0.1937 0.1507 0.0063  -0.0200 -0.0324 57  THR   B N   
1238 C CA  A THR   B 43  ? 0.1387 0.1769 0.1428 -0.0076 -0.0175 -0.0330 57  THR   B CA  
1239 C CA  B THR   B 43  ? 0.1333 0.1888 0.1432 -0.0092 -0.0044 -0.0268 57  THR   B CA  
1240 C C   . THR   B 43  ? 0.1235 0.1634 0.1269 -0.0094 -0.0086 -0.0282 57  THR   B C   
1241 O O   . THR   B 43  ? 0.1347 0.1379 0.1114 -0.0019 -0.0080 -0.0263 57  THR   B O   
1242 C CB  A THR   B 43  ? 0.1801 0.1882 0.1652 -0.0410 -0.0222 -0.0344 57  THR   B CB  
1243 C CB  B THR   B 43  ? 0.1667 0.2348 0.1627 -0.0600 -0.0052 -0.0180 57  THR   B CB  
1244 O OG1 A THR   B 43  ? 0.2134 0.1790 0.1685 -0.0386 -0.0376 -0.0235 57  THR   B OG1 
1245 O OG1 B THR   B 43  ? 0.1874 0.2448 0.2087 -0.0382 0.0004  -0.0040 57  THR   B OG1 
1246 C CG2 A THR   B 43  ? 0.1840 0.1947 0.1889 -0.0455 -0.0209 -0.0430 57  THR   B CG2 
1247 C CG2 B THR   B 43  ? 0.1848 0.2552 0.1558 -0.0849 -0.0434 -0.0110 57  THR   B CG2 
1248 N N   . GLY   B 44  ? 0.1164 0.1629 0.1364 -0.0022 0.0107  -0.0370 58  GLY   B N   
1249 C CA  . GLY   B 44  ? 0.1104 0.1428 0.1379 -0.0003 -0.0163 -0.0145 58  GLY   B CA  
1250 C C   . GLY   B 44  ? 0.1229 0.1244 0.1209 0.0067  0.0128  -0.0124 58  GLY   B C   
1251 O O   . GLY   B 44  ? 0.1474 0.1299 0.1183 0.0052  0.0112  -0.0211 58  GLY   B O   
1252 N N   . ARG   B 45  ? 0.0992 0.1258 0.1320 0.0067  0.0013  0.0024  59  ARG   B N   
1253 C CA  . ARG   B 45  ? 0.1152 0.1225 0.1358 0.0160  0.0128  0.0049  59  ARG   B CA  
1254 C C   . ARG   B 45  ? 0.1107 0.1237 0.1424 0.0105  0.0015  -0.0251 59  ARG   B C   
1255 O O   . ARG   B 45  ? 0.1365 0.1240 0.1487 0.0078  0.0025  -0.0259 59  ARG   B O   
1256 C CB  . ARG   B 45  ? 0.1542 0.1186 0.1574 0.0066  0.0056  -0.0022 59  ARG   B CB  
1257 C CG  . ARG   B 45  ? 0.1496 0.1124 0.1776 0.0112  0.0036  -0.0143 59  ARG   B CG  
1258 C CD  . ARG   B 45  ? 0.1669 0.1123 0.1842 0.0083  0.0163  -0.0182 59  ARG   B CD  
1259 N NE  . ARG   B 45  ? 0.1478 0.1158 0.1517 0.0167  0.0068  -0.0194 59  ARG   B NE  
1260 C CZ  . ARG   B 45  ? 0.1732 0.1385 0.1631 0.0245  0.0268  -0.0144 59  ARG   B CZ  
1261 N NH1 . ARG   B 45  ? 0.2028 0.1480 0.1703 0.0051  0.0128  -0.0210 59  ARG   B NH1 
1262 N NH2 . ARG   B 45  ? 0.1959 0.1505 0.1618 0.0371  0.0443  -0.0072 59  ARG   B NH2 
1263 N N   . TYR   B 46  ? 0.1060 0.1342 0.1397 0.0028  -0.0063 -0.0268 60  TYR   B N   
1264 C CA  . TYR   B 46  ? 0.1104 0.1361 0.1440 0.0122  0.0004  -0.0180 60  TYR   B CA  
1265 C C   . TYR   B 46  ? 0.1115 0.1425 0.1491 0.0195  0.0044  -0.0086 60  TYR   B C   
1266 O O   . TYR   B 46  ? 0.1443 0.1401 0.1569 0.0087  0.0160  -0.0204 60  TYR   B O   
1267 C CB  . TYR   B 46  ? 0.1436 0.1306 0.1436 0.0184  0.0164  -0.0040 60  TYR   B CB  
1268 C CG  . TYR   B 46  ? 0.1448 0.1345 0.1366 0.0064  0.0220  -0.0075 60  TYR   B CG  
1269 C CD1 . TYR   B 46  ? 0.1512 0.1382 0.1280 0.0072  0.0074  -0.0048 60  TYR   B CD1 
1270 C CD2 . TYR   B 46  ? 0.1463 0.1452 0.1597 0.0295  0.0176  -0.0103 60  TYR   B CD2 
1271 C CE1 . TYR   B 46  ? 0.1554 0.1443 0.1410 0.0215  0.0097  -0.0146 60  TYR   B CE1 
1272 C CE2 . TYR   B 46  ? 0.1633 0.1489 0.1534 0.0189  0.0173  -0.0205 60  TYR   B CE2 
1273 C CZ  . TYR   B 46  ? 0.1479 0.1528 0.1537 0.0246  0.0248  -0.0216 60  TYR   B CZ  
1274 O OH  . TYR   B 46  ? 0.1592 0.1685 0.1689 0.0129  0.0322  -0.0283 60  TYR   B OH  
1275 N N   . ASP   B 47  ? 0.1138 0.1554 0.1426 0.0321  0.0038  -0.0174 61  ASP   B N   
1276 C CA  . ASP   B 47  ? 0.1243 0.1673 0.1506 0.0330  0.0034  -0.0337 61  ASP   B CA  
1277 C C   . ASP   B 47  ? 0.1372 0.1644 0.1487 0.0335  0.0055  -0.0343 61  ASP   B C   
1278 O O   . ASP   B 47  ? 0.1254 0.1707 0.1500 0.0067  0.0084  -0.0250 61  ASP   B O   
1279 C CB  . ASP   B 47  ? 0.1222 0.1727 0.1567 0.0368  -0.0086 -0.0428 61  ASP   B CB  
1280 C CG  . ASP   B 47  ? 0.1390 0.1754 0.1658 0.0272  -0.0074 -0.0538 61  ASP   B CG  
1281 O OD1 . ASP   B 47  ? 0.1485 0.1833 0.1751 0.0403  -0.0174 -0.0414 61  ASP   B OD1 
1282 O OD2 . ASP   B 47  ? 0.1274 0.1756 0.1749 0.0219  -0.0064 -0.0448 61  ASP   B OD2 
1283 N N   . SER   B 48  ? 0.1357 0.1659 0.1460 0.0238  0.0009  -0.0489 62  SER   B N   
1284 C CA  . SER   B 48  ? 0.1222 0.1641 0.1542 0.0246  -0.0068 -0.0554 62  SER   B CA  
1285 C C   . SER   B 48  ? 0.1368 0.1862 0.1789 0.0212  0.0025  -0.0417 62  SER   B C   
1286 O O   . SER   B 48  ? 0.1492 0.2127 0.1958 0.0236  0.0241  -0.0417 62  SER   B O   
1287 C CB  . SER   B 48  ? 0.1780 0.1715 0.1713 0.0030  0.0246  -0.0430 62  SER   B CB  
1288 O OG  . SER   B 48  ? 0.2258 0.1821 0.1726 0.0009  0.0333  -0.0463 62  SER   B OG  
1289 N N   . ALA   B 49  ? 0.1295 0.1900 0.1776 0.0193  -0.0302 -0.0439 63  ALA   B N   
1290 C CA  . ALA   B 49  ? 0.1257 0.1926 0.1968 0.0295  -0.0225 -0.0449 63  ALA   B CA  
1291 C C   . ALA   B 49  ? 0.1213 0.2071 0.1833 0.0164  -0.0151 -0.0285 63  ALA   B C   
1292 O O   . ALA   B 49  ? 0.1301 0.2224 0.2128 0.0206  -0.0150 -0.0186 63  ALA   B O   
1293 C CB  . ALA   B 49  ? 0.1606 0.1956 0.2510 0.0461  -0.0136 -0.0528 63  ALA   B CB  
1294 N N   . PRO   B 50  ? 0.1281 0.2096 0.1800 0.0099  -0.0023 -0.0211 64  PRO   B N   
1295 C CA  . PRO   B 50  ? 0.1229 0.2109 0.1972 0.0035  -0.0058 -0.0173 64  PRO   B CA  
1296 C C   . PRO   B 50  ? 0.1361 0.2251 0.2020 0.0012  -0.0058 -0.0257 64  PRO   B C   
1297 O O   . PRO   B 50  ? 0.1332 0.2393 0.2271 0.0135  -0.0138 -0.0338 64  PRO   B O   
1298 C CB  . PRO   B 50  ? 0.1498 0.2135 0.1907 0.0086  -0.0224 -0.0168 64  PRO   B CB  
1299 C CG  . PRO   B 50  ? 0.1524 0.2038 0.1978 -0.0046 -0.0081 -0.0253 64  PRO   B CG  
1300 C CD  . PRO   B 50  ? 0.1462 0.2029 0.2009 0.0020  0.0084  -0.0051 64  PRO   B CD  
1301 N N   . ALA   B 51  ? 0.1382 0.2393 0.2091 -0.0147 -0.0029 -0.0093 65  ALA   B N   
1302 C CA  . ALA   B 51  ? 0.1293 0.2616 0.2294 -0.0349 -0.0161 -0.0038 65  ALA   B CA  
1303 C C   . ALA   B 51  ? 0.1158 0.2839 0.2391 -0.0256 -0.0121 -0.0157 65  ALA   B C   
1304 O O   . ALA   B 51  ? 0.1472 0.2909 0.2547 -0.0153 0.0290  -0.0101 65  ALA   B O   
1305 C CB  . ALA   B 51  ? 0.1571 0.2714 0.2451 -0.0404 -0.0413 0.0071  65  ALA   B CB  
1306 N N   . THR   B 52  ? 0.1304 0.3135 0.2593 -0.0432 0.0087  -0.0088 66  THR   B N   
1307 C CA  A THR   B 52  ? 0.1572 0.3230 0.2666 -0.0423 0.0279  -0.0241 66  THR   B CA  
1308 C CA  B THR   B 52  ? 0.1420 0.3309 0.2681 -0.0408 0.0144  -0.0213 66  THR   B CA  
1309 C C   . THR   B 52  ? 0.1327 0.3221 0.2584 -0.0428 0.0330  -0.0210 66  THR   B C   
1310 O O   . THR   B 52  ? 0.1532 0.3215 0.2527 -0.0304 0.0271  -0.0333 66  THR   B O   
1311 C CB  A THR   B 52  ? 0.2014 0.3302 0.2780 -0.0414 0.0410  -0.0302 66  THR   B CB  
1312 C CB  B THR   B 52  ? 0.1581 0.3525 0.2863 -0.0392 0.0064  -0.0222 66  THR   B CB  
1313 O OG1 A THR   B 52  ? 0.2280 0.3334 0.3083 -0.0393 0.0445  -0.0414 66  THR   B OG1 
1314 O OG1 B THR   B 52  ? 0.1854 0.3680 0.2988 -0.0218 0.0254  -0.0347 66  THR   B OG1 
1315 C CG2 A THR   B 52  ? 0.2088 0.3326 0.2517 -0.0363 0.0410  -0.0228 66  THR   B CG2 
1316 C CG2 B THR   B 52  ? 0.1383 0.3564 0.2860 -0.0390 -0.0284 -0.0063 66  THR   B CG2 
1317 N N   . ASP   B 53  ? 0.1377 0.3155 0.2295 -0.0225 0.0415  -0.0308 67  ASP   B N   
1318 C CA  . ASP   B 53  ? 0.1194 0.3110 0.2408 -0.0346 0.0309  -0.0230 67  ASP   B CA  
1319 C C   . ASP   B 53  ? 0.1297 0.3110 0.2686 -0.0268 0.0543  -0.0074 67  ASP   B C   
1320 O O   . ASP   B 53  ? 0.1651 0.3159 0.3331 -0.0316 0.0186  -0.0062 67  ASP   B O   
1321 C CB  . ASP   B 53  ? 0.1195 0.3118 0.2298 -0.0279 0.0374  -0.0211 67  ASP   B CB  
1322 C CG  . ASP   B 53  ? 0.1261 0.3129 0.2219 -0.0075 0.0077  -0.0217 67  ASP   B CG  
1323 O OD1 . ASP   B 53  ? 0.1103 0.3032 0.2350 -0.0231 0.0165  -0.0260 67  ASP   B OD1 
1324 O OD2 . ASP   B 53  ? 0.1342 0.3249 0.2277 0.0142  0.0058  -0.0201 67  ASP   B OD2 
1325 N N   . GLY   B 54  ? 0.1296 0.3049 0.2368 -0.0208 0.0374  0.0233  68  GLY   B N   
1326 C CA  . GLY   B 54  ? 0.1554 0.3021 0.2508 -0.0094 0.0561  0.0303  68  GLY   B CA  
1327 C C   . GLY   B 54  ? 0.1491 0.2941 0.2437 -0.0154 0.0436  0.0186  68  GLY   B C   
1328 O O   . GLY   B 54  ? 0.1997 0.3015 0.2954 -0.0208 0.0358  0.0260  68  GLY   B O   
1329 N N   . SER   B 55  ? 0.1397 0.2916 0.1971 -0.0269 0.0273  0.0074  69  SER   B N   
1330 C CA  . SER   B 55  ? 0.1292 0.2824 0.1944 -0.0314 0.0185  0.0064  69  SER   B CA  
1331 C C   . SER   B 55  ? 0.1285 0.2375 0.1741 -0.0268 0.0195  -0.0034 69  SER   B C   
1332 O O   . SER   B 55  ? 0.1311 0.2460 0.1769 -0.0214 0.0319  -0.0049 69  SER   B O   
1333 C CB  . SER   B 55  ? 0.1411 0.3152 0.1993 -0.0182 0.0069  0.0190  69  SER   B CB  
1334 O OG  . SER   B 55  ? 0.1755 0.3403 0.2148 -0.0180 -0.0018 -0.0050 69  SER   B OG  
1335 N N   . GLY   B 56  ? 0.1140 0.2001 0.1731 -0.0229 0.0110  -0.0138 70  GLY   B N   
1336 C CA  . GLY   B 56  ? 0.1195 0.1775 0.1681 -0.0216 0.0115  -0.0158 70  GLY   B CA  
1337 C C   . GLY   B 56  ? 0.1165 0.1611 0.1354 0.0008  0.0197  -0.0011 70  GLY   B C   
1338 O O   . GLY   B 56  ? 0.1362 0.1754 0.1440 0.0070  0.0224  0.0045  70  GLY   B O   
1339 N N   . THR   B 57  ? 0.1169 0.1696 0.1367 -0.0097 0.0128  -0.0206 71  THR   B N   
1340 C CA  . THR   B 57  ? 0.1334 0.1631 0.1354 -0.0041 0.0021  -0.0178 71  THR   B CA  
1341 C C   . THR   B 57  ? 0.1089 0.1444 0.1259 -0.0026 0.0182  0.0069  71  THR   B C   
1342 O O   . THR   B 57  ? 0.1231 0.1418 0.1359 0.0054  0.0132  0.0004  71  THR   B O   
1343 C CB  . THR   B 57  ? 0.1400 0.1712 0.1385 -0.0182 0.0180  -0.0163 71  THR   B CB  
1344 O OG1 . THR   B 57  ? 0.1359 0.1879 0.1468 -0.0008 0.0175  -0.0112 71  THR   B OG1 
1345 C CG2 . THR   B 57  ? 0.1519 0.1636 0.1515 -0.0251 0.0114  -0.0181 71  THR   B CG2 
1346 N N   . ALA   B 58  ? 0.1151 0.1354 0.1263 -0.0143 0.0206  -0.0113 72  ALA   B N   
1347 C CA  . ALA   B 58  ? 0.1050 0.1386 0.1264 0.0024  0.0003  0.0074  72  ALA   B CA  
1348 C C   . ALA   B 58  ? 0.1055 0.1252 0.1394 0.0086  0.0044  -0.0078 72  ALA   B C   
1349 O O   . ALA   B 58  ? 0.1307 0.1231 0.1491 0.0144  0.0016  -0.0199 72  ALA   B O   
1350 C CB  . ALA   B 58  ? 0.1431 0.1433 0.1305 0.0008  0.0040  0.0208  72  ALA   B CB  
1351 N N   . LEU   B 59  ? 0.0878 0.1304 0.1370 -0.0007 0.0076  -0.0104 73  LEU   B N   
1352 C CA  A LEU   B 59  ? 0.0897 0.1303 0.1288 0.0009  -0.0085 -0.0012 73  LEU   B CA  
1353 C CA  B LEU   B 59  ? 0.0951 0.1274 0.1231 0.0043  0.0060  -0.0128 73  LEU   B CA  
1354 C C   . LEU   B 59  ? 0.1029 0.1204 0.1301 0.0130  0.0084  -0.0155 73  LEU   B C   
1355 O O   . LEU   B 59  ? 0.1378 0.1369 0.1373 -0.0079 0.0078  -0.0417 73  LEU   B O   
1356 C CB  A LEU   B 59  ? 0.1495 0.1287 0.1372 -0.0064 0.0077  0.0099  73  LEU   B CB  
1357 C CB  B LEU   B 59  ? 0.1311 0.1269 0.1105 -0.0006 0.0292  -0.0215 73  LEU   B CB  
1358 C CG  A LEU   B 59  ? 0.1722 0.1426 0.1444 -0.0023 0.0242  0.0044  73  LEU   B CG  
1359 C CG  B LEU   B 59  ? 0.1387 0.1298 0.0971 -0.0064 0.0339  -0.0363 73  LEU   B CG  
1360 C CD1 A LEU   B 59  ? 0.1923 0.1539 0.1722 0.0142  0.0368  0.0180  73  LEU   B CD1 
1361 C CD1 B LEU   B 59  ? 0.1400 0.1365 0.0997 -0.0137 0.0218  -0.0386 73  LEU   B CD1 
1362 C CD2 A LEU   B 59  ? 0.1775 0.1532 0.1466 -0.0212 0.0364  0.0060  73  LEU   B CD2 
1363 C CD2 B LEU   B 59  ? 0.1393 0.1328 0.1031 -0.0020 0.0184  -0.0467 73  LEU   B CD2 
1364 N N   . GLY   B 60  ? 0.1135 0.1251 0.1165 -0.0035 0.0132  -0.0099 74  GLY   B N   
1365 C CA  . GLY   B 60  ? 0.1103 0.1278 0.1124 -0.0082 0.0117  -0.0046 74  GLY   B CA  
1366 C C   . GLY   B 60  ? 0.1099 0.1208 0.1206 -0.0001 0.0095  -0.0101 74  GLY   B C   
1367 O O   . GLY   B 60  ? 0.1373 0.1134 0.1185 0.0154  -0.0003 -0.0235 74  GLY   B O   
1368 N N   . TRP   B 61  ? 0.1065 0.1165 0.1181 0.0115  -0.0011 -0.0183 75  TRP   B N   
1369 C CA  . TRP   B 61  ? 0.1002 0.1212 0.1038 0.0091  -0.0030 -0.0247 75  TRP   B CA  
1370 C C   . TRP   B 61  ? 0.1070 0.1194 0.1167 0.0097  -0.0052 -0.0193 75  TRP   B C   
1371 O O   . TRP   B 61  ? 0.1351 0.1134 0.1225 -0.0028 0.0125  -0.0156 75  TRP   B O   
1372 C CB  . TRP   B 61  ? 0.1375 0.1240 0.1082 0.0002  -0.0021 -0.0110 75  TRP   B CB  
1373 C CG  . TRP   B 61  ? 0.1254 0.1383 0.1039 -0.0043 -0.0091 -0.0181 75  TRP   B CG  
1374 C CD1 . TRP   B 61  ? 0.1505 0.1410 0.1021 0.0002  -0.0039 -0.0105 75  TRP   B CD1 
1375 C CD2 . TRP   B 61  ? 0.1379 0.1355 0.1017 -0.0064 -0.0012 -0.0094 75  TRP   B CD2 
1376 N NE1 . TRP   B 61  ? 0.1679 0.1447 0.1276 0.0050  0.0206  0.0118  75  TRP   B NE1 
1377 C CE2 . TRP   B 61  ? 0.1623 0.1340 0.1077 -0.0079 0.0070  0.0046  75  TRP   B CE2 
1378 C CE3 . TRP   B 61  ? 0.1517 0.1424 0.1201 -0.0238 -0.0113 -0.0029 75  TRP   B CE3 
1379 C CZ2 . TRP   B 61  ? 0.1804 0.1365 0.1219 -0.0187 0.0027  -0.0029 75  TRP   B CZ2 
1380 C CZ3 . TRP   B 61  ? 0.1609 0.1467 0.1258 -0.0285 -0.0160 0.0046  75  TRP   B CZ3 
1381 C CH2 . TRP   B 61  ? 0.1677 0.1449 0.1229 -0.0282 -0.0071 0.0007  75  TRP   B CH2 
1382 N N   . THR   B 62  ? 0.1174 0.1403 0.1190 -0.0095 -0.0061 -0.0158 76  THR   B N   
1383 C CA  . THR   B 62  ? 0.1147 0.1448 0.1117 -0.0028 0.0053  -0.0052 76  THR   B CA  
1384 C C   . THR   B 62  ? 0.1221 0.1388 0.1126 -0.0004 -0.0063 -0.0308 76  THR   B C   
1385 O O   . THR   B 62  ? 0.1355 0.1567 0.1232 0.0072  -0.0137 -0.0249 76  THR   B O   
1386 C CB  . THR   B 62  ? 0.1162 0.1372 0.1206 -0.0047 0.0011  -0.0104 76  THR   B CB  
1387 O OG1 . THR   B 62  ? 0.1326 0.1276 0.1231 0.0083  -0.0116 0.0006  76  THR   B OG1 
1388 C CG2 . THR   B 62  ? 0.1201 0.1549 0.1348 0.0042  0.0087  -0.0066 76  THR   B CG2 
1389 N N   . VAL   B 63  ? 0.1159 0.1417 0.1226 0.0017  -0.0024 -0.0189 77  VAL   B N   
1390 C CA  . VAL   B 63  ? 0.1279 0.1564 0.1516 0.0103  0.0045  -0.0083 77  VAL   B CA  
1391 C C   . VAL   B 63  ? 0.1184 0.1700 0.1412 0.0094  -0.0115 -0.0422 77  VAL   B C   
1392 O O   . VAL   B 63  ? 0.1425 0.1758 0.1484 0.0078  -0.0088 -0.0403 77  VAL   B O   
1393 C CB  . VAL   B 63  ? 0.1724 0.1572 0.1425 0.0059  -0.0321 -0.0094 77  VAL   B CB  
1394 C CG1 . VAL   B 63  ? 0.1780 0.1751 0.1554 0.0119  -0.0660 -0.0104 77  VAL   B CG1 
1395 C CG2 . VAL   B 63  ? 0.2032 0.1512 0.1370 0.0058  0.0131  -0.0139 77  VAL   B CG2 
1396 N N   . ALA   B 64  ? 0.1231 0.1772 0.1343 0.0005  0.0022  -0.0314 78  ALA   B N   
1397 C CA  . ALA   B 64  ? 0.1132 0.1961 0.1539 0.0038  0.0013  -0.0347 78  ALA   B CA  
1398 C C   . ALA   B 64  ? 0.0928 0.2030 0.1593 0.0022  -0.0060 -0.0360 78  ALA   B C   
1399 O O   . ALA   B 64  ? 0.1262 0.2060 0.1510 0.0187  -0.0108 -0.0393 78  ALA   B O   
1400 C CB  . ALA   B 64  ? 0.1108 0.2013 0.1773 -0.0144 0.0033  -0.0381 78  ALA   B CB  
1401 N N   . TRP   B 65  ? 0.1019 0.1998 0.1536 0.0061  0.0023  -0.0274 79  TRP   B N   
1402 C CA  . TRP   B 65  ? 0.1097 0.2129 0.1611 -0.0020 -0.0087 -0.0434 79  TRP   B CA  
1403 C C   . TRP   B 65  ? 0.1134 0.2327 0.1499 0.0099  0.0157  -0.0363 79  TRP   B C   
1404 O O   . TRP   B 65  ? 0.1254 0.2347 0.1496 0.0067  -0.0127 -0.0446 79  TRP   B O   
1405 C CB  . TRP   B 65  ? 0.1331 0.2014 0.1619 -0.0093 -0.0063 -0.0446 79  TRP   B CB  
1406 C CG  . TRP   B 65  ? 0.1322 0.1808 0.1548 -0.0017 -0.0044 -0.0218 79  TRP   B CG  
1407 C CD1 . TRP   B 65  ? 0.1314 0.1822 0.1428 0.0030  -0.0047 -0.0076 79  TRP   B CD1 
1408 C CD2 . TRP   B 65  ? 0.1286 0.1734 0.1526 0.0155  -0.0141 -0.0203 79  TRP   B CD2 
1409 N NE1 . TRP   B 65  ? 0.1226 0.1738 0.1362 -0.0064 -0.0002 -0.0088 79  TRP   B NE1 
1410 C CE2 . TRP   B 65  ? 0.1220 0.1744 0.1549 0.0122  -0.0063 -0.0176 79  TRP   B CE2 
1411 C CE3 . TRP   B 65  ? 0.1486 0.1761 0.1472 0.0127  -0.0026 -0.0101 79  TRP   B CE3 
1412 C CZ2 . TRP   B 65  ? 0.1461 0.1693 0.1653 0.0033  -0.0069 -0.0375 79  TRP   B CZ2 
1413 C CZ3 . TRP   B 65  ? 0.1686 0.1851 0.1442 -0.0063 -0.0285 -0.0124 79  TRP   B CZ3 
1414 C CH2 . TRP   B 65  ? 0.1553 0.1772 0.1530 -0.0144 -0.0153 -0.0255 79  TRP   B CH2 
1415 N N   . LYS   B 66  ? 0.1282 0.2490 0.1464 -0.0066 -0.0178 -0.0387 80  LYS   B N   
1416 C CA  . LYS   B 66  ? 0.1366 0.2490 0.1521 -0.0121 -0.0202 -0.0454 80  LYS   B CA  
1417 C C   . LYS   B 66  ? 0.1219 0.2408 0.1589 -0.0149 -0.0089 -0.0335 80  LYS   B C   
1418 O O   . LYS   B 66  ? 0.1335 0.2339 0.1644 -0.0262 -0.0088 -0.0318 80  LYS   B O   
1419 C CB  . LYS   B 66  ? 0.1517 0.2670 0.1780 -0.0152 -0.0008 -0.0375 80  LYS   B CB  
1420 C CG  . LYS   B 66  ? 0.1660 0.2855 0.2019 -0.0450 -0.0238 -0.0128 80  LYS   B CG  
1421 C CD  . LYS   B 66  ? 0.2156 0.3073 0.2343 -0.0712 -0.0259 -0.0070 80  LYS   B CD  
1422 C CE  . LYS   B 66  ? 0.2796 0.3318 0.2894 -0.0954 -0.0073 -0.0046 80  LYS   B CE  
1423 N NZ  . LYS   B 66  ? 0.3125 0.3481 0.3141 -0.1188 0.0073  -0.0040 80  LYS   B NZ  
1424 N N   . ASN   B 67  ? 0.1380 0.2604 0.1530 0.0028  -0.0115 -0.0196 81  ASN   B N   
1425 C CA  . ASN   B 67  ? 0.1411 0.2824 0.1557 -0.0087 -0.0111 -0.0209 81  ASN   B CA  
1426 C C   . ASN   B 67  ? 0.1611 0.3127 0.1795 -0.0192 -0.0208 -0.0408 81  ASN   B C   
1427 O O   . ASN   B 67  ? 0.1649 0.3195 0.1984 -0.0336 -0.0161 -0.0537 81  ASN   B O   
1428 C CB  . ASN   B 67  ? 0.1491 0.2758 0.1538 0.0014  -0.0165 -0.0044 81  ASN   B CB  
1429 C CG  . ASN   B 67  ? 0.1527 0.2660 0.1583 0.0056  -0.0312 -0.0080 81  ASN   B CG  
1430 O OD1 . ASN   B 67  ? 0.1480 0.2741 0.1831 0.0178  -0.0201 -0.0171 81  ASN   B OD1 
1431 N ND2 . ASN   B 67  ? 0.1807 0.2600 0.1795 -0.0018 -0.0471 -0.0063 81  ASN   B ND2 
1432 N N   . ASN   B 68  ? 0.1829 0.3445 0.1939 -0.0434 -0.0359 -0.0501 82  ASN   B N   
1433 C CA  . ASN   B 68  ? 0.2321 0.3790 0.2113 -0.0344 -0.0640 -0.0618 82  ASN   B CA  
1434 C C   . ASN   B 68  ? 0.1974 0.4057 0.2396 -0.0181 -0.0750 -0.0398 82  ASN   B C   
1435 O O   . ASN   B 68  ? 0.2200 0.4217 0.3046 -0.0292 -0.0807 -0.0363 82  ASN   B O   
1436 C CB  . ASN   B 68  ? 0.3100 0.3935 0.2320 -0.0324 -0.0668 -0.0874 82  ASN   B CB  
1437 C CG  . ASN   B 68  ? 0.4020 0.4065 0.2671 -0.0336 -0.0187 -0.0922 82  ASN   B CG  
1438 O OD1 . ASN   B 68  ? 0.4373 0.4120 0.3089 -0.0386 -0.0056 -0.0884 82  ASN   B OD1 
1439 N ND2 . ASN   B 68  ? 0.4411 0.4105 0.2875 -0.0269 0.0335  -0.0977 82  ASN   B ND2 
1440 N N   . TYR   B 69  ? 0.1916 0.4088 0.2194 0.0225  -0.0618 -0.0228 83  TYR   B N   
1441 C CA  . TYR   B 69  ? 0.2208 0.4202 0.2027 0.0391  -0.0531 0.0012  83  TYR   B CA  
1442 C C   . TYR   B 69  ? 0.2004 0.3992 0.2241 0.0412  -0.0217 -0.0025 83  TYR   B C   
1443 O O   . TYR   B 69  ? 0.2074 0.4062 0.2472 0.0401  -0.0331 -0.0064 83  TYR   B O   
1444 C CB  . TYR   B 69  ? 0.2520 0.4505 0.1808 0.0388  -0.0396 0.0060  83  TYR   B CB  
1445 C CG  . TYR   B 69  ? 0.2818 0.4804 0.1907 0.0340  -0.0486 0.0016  83  TYR   B CG  
1446 C CD1 . TYR   B 69  ? 0.3136 0.4986 0.2052 0.0296  -0.0591 -0.0114 83  TYR   B CD1 
1447 C CD2 . TYR   B 69  ? 0.3023 0.4955 0.2142 0.0297  -0.0026 -0.0102 83  TYR   B CD2 
1448 C CE1 . TYR   B 69  ? 0.3340 0.5135 0.2139 0.0311  -0.0332 -0.0106 83  TYR   B CE1 
1449 C CE2 . TYR   B 69  ? 0.3258 0.5113 0.2190 0.0257  -0.0124 -0.0190 83  TYR   B CE2 
1450 C CZ  . TYR   B 69  ? 0.3528 0.5214 0.2149 0.0249  -0.0159 -0.0196 83  TYR   B CZ  
1451 O OH  . TYR   B 69  ? 0.3843 0.5358 0.2370 0.0238  0.0000  -0.0224 83  TYR   B OH  
1452 N N   . ARG   B 70  ? 0.1858 0.3715 0.1922 0.0433  -0.0344 -0.0068 84  ARG   B N   
1453 C CA  . ARG   B 70  ? 0.2018 0.3508 0.1868 0.0207  -0.0461 -0.0069 84  ARG   B CA  
1454 C C   . ARG   B 70  ? 0.1371 0.3083 0.1695 0.0139  -0.0261 -0.0200 84  ARG   B C   
1455 O O   . ARG   B 70  ? 0.1478 0.2997 0.1656 0.0153  -0.0046 -0.0196 84  ARG   B O   
1456 C CB  . ARG   B 70  ? 0.3063 0.3707 0.2504 0.0193  -0.0584 0.0277  84  ARG   B CB  
1457 C CG  . ARG   B 70  ? 0.3933 0.3998 0.3301 0.0079  -0.0535 0.0374  84  ARG   B CG  
1458 C CD  . ARG   B 70  ? 0.4498 0.4211 0.4058 0.0061  -0.0298 0.0578  84  ARG   B CD  
1459 N NE  . ARG   B 70  ? 0.4907 0.4464 0.4620 0.0160  -0.0125 0.0717  84  ARG   B NE  
1460 C CZ  . ARG   B 70  ? 0.5150 0.4636 0.5044 0.0316  0.0034  0.0810  84  ARG   B CZ  
1461 N NH1 . ARG   B 70  ? 0.5220 0.4727 0.5178 0.0382  0.0175  0.0908  84  ARG   B NH1 
1462 N NH2 . ARG   B 70  ? 0.5248 0.4684 0.5268 0.0384  -0.0066 0.0781  84  ARG   B NH2 
1463 N N   . ASN   B 71  ? 0.1230 0.2798 0.1583 0.0051  -0.0259 -0.0084 85  ASN   B N   
1464 C CA  . ASN   B 71  ? 0.1299 0.2562 0.1598 0.0109  -0.0090 -0.0152 85  ASN   B CA  
1465 C C   . ASN   B 71  ? 0.1252 0.2463 0.1812 0.0143  0.0031  -0.0083 85  ASN   B C   
1466 O O   . ASN   B 71  ? 0.1333 0.2561 0.2065 0.0128  0.0088  -0.0146 85  ASN   B O   
1467 C CB  . ASN   B 71  ? 0.1223 0.2500 0.1651 -0.0027 -0.0131 -0.0203 85  ASN   B CB  
1468 C CG  . ASN   B 71  ? 0.1103 0.2455 0.1538 -0.0015 -0.0107 -0.0186 85  ASN   B CG  
1469 O OD1 . ASN   B 71  ? 0.1263 0.2628 0.1746 0.0073  -0.0319 -0.0255 85  ASN   B OD1 
1470 N ND2 . ASN   B 71  ? 0.1456 0.2429 0.1655 -0.0178 0.0084  -0.0242 85  ASN   B ND2 
1471 N N   . ALA   B 72  ? 0.1481 0.2321 0.1679 -0.0177 0.0038  -0.0334 86  ALA   B N   
1472 C CA  . ALA   B 72  ? 0.1444 0.2251 0.1568 -0.0328 0.0091  -0.0171 86  ALA   B CA  
1473 C C   . ALA   B 72  ? 0.1238 0.2304 0.1556 -0.0135 0.0076  -0.0368 86  ALA   B C   
1474 O O   . ALA   B 72  ? 0.1692 0.2371 0.1730 -0.0010 -0.0203 -0.0553 86  ALA   B O   
1475 C CB  . ALA   B 72  ? 0.1618 0.2203 0.2015 -0.0448 0.0189  -0.0146 86  ALA   B CB  
1476 N N   . HIS   B 73  ? 0.1273 0.2259 0.1785 -0.0162 0.0187  -0.0275 87  HIS   B N   
1477 C CA  . HIS   B 73  ? 0.1021 0.2249 0.1600 -0.0105 0.0050  -0.0224 87  HIS   B CA  
1478 C C   . HIS   B 73  ? 0.1171 0.2102 0.1495 -0.0052 0.0091  -0.0378 87  HIS   B C   
1479 O O   . HIS   B 73  ? 0.1312 0.2260 0.1522 -0.0033 -0.0015 -0.0423 87  HIS   B O   
1480 C CB  . HIS   B 73  ? 0.1278 0.2413 0.1622 -0.0139 0.0145  -0.0230 87  HIS   B CB  
1481 C CG  . HIS   B 73  ? 0.1240 0.2515 0.1599 -0.0171 0.0032  -0.0292 87  HIS   B CG  
1482 N ND1 . HIS   B 73  ? 0.1083 0.2542 0.1769 -0.0247 -0.0084 -0.0233 87  HIS   B ND1 
1483 C CD2 . HIS   B 73  ? 0.1107 0.2595 0.1916 -0.0148 -0.0159 -0.0278 87  HIS   B CD2 
1484 C CE1 . HIS   B 73  ? 0.1313 0.2570 0.1884 -0.0214 0.0020  -0.0334 87  HIS   B CE1 
1485 N NE2 . HIS   B 73  ? 0.1160 0.2587 0.1900 -0.0149 -0.0068 -0.0287 87  HIS   B NE2 
1486 N N   . SER   B 74  ? 0.1152 0.1995 0.1560 -0.0093 0.0028  -0.0248 88  SER   B N   
1487 C CA  . SER   B 74  ? 0.1232 0.1901 0.1667 -0.0073 0.0086  -0.0367 88  SER   B CA  
1488 C C   . SER   B 74  ? 0.1187 0.1908 0.1376 -0.0004 0.0015  -0.0240 88  SER   B C   
1489 O O   . SER   B 74  ? 0.1432 0.1894 0.1415 -0.0127 -0.0018 -0.0372 88  SER   B O   
1490 C CB  . SER   B 74  ? 0.1727 0.2098 0.1581 0.0026  0.0032  -0.0276 88  SER   B CB  
1491 O OG  . SER   B 74  ? 0.1621 0.2305 0.1704 0.0101  0.0062  -0.0073 88  SER   B OG  
1492 N N   . ALA   B 75  ? 0.1013 0.1708 0.1370 0.0080  0.0090  -0.0379 89  ALA   B N   
1493 C CA  . ALA   B 75  ? 0.1128 0.1502 0.1477 0.0011  0.0256  -0.0349 89  ALA   B CA  
1494 C C   . ALA   B 75  ? 0.1259 0.1461 0.1275 0.0035  0.0027  -0.0217 89  ALA   B C   
1495 O O   . ALA   B 75  ? 0.1462 0.1493 0.1348 -0.0087 0.0020  -0.0127 89  ALA   B O   
1496 C CB  . ALA   B 75  ? 0.1494 0.1524 0.1752 0.0124  0.0318  -0.0424 89  ALA   B CB  
1497 N N   . THR   B 76  ? 0.1037 0.1461 0.1337 0.0042  -0.0025 -0.0148 90  THR   B N   
1498 C CA  . THR   B 76  ? 0.0916 0.1412 0.1358 0.0095  -0.0004 -0.0164 90  THR   B CA  
1499 C C   . THR   B 76  ? 0.1163 0.1412 0.1356 0.0056  0.0061  -0.0271 90  THR   B C   
1500 O O   . THR   B 76  ? 0.1285 0.1399 0.1249 -0.0044 0.0021  -0.0312 90  THR   B O   
1501 C CB  . THR   B 76  ? 0.1193 0.1432 0.1329 -0.0010 -0.0053 -0.0217 90  THR   B CB  
1502 O OG1 . THR   B 76  ? 0.1204 0.1559 0.1350 0.0126  -0.0088 -0.0184 90  THR   B OG1 
1503 C CG2 . THR   B 76  ? 0.1193 0.1378 0.1614 -0.0060 0.0005  -0.0091 90  THR   B CG2 
1504 N N   . THR   B 77  ? 0.1067 0.1377 0.1163 0.0055  0.0023  -0.0076 91  THR   B N   
1505 C CA  . THR   B 77  ? 0.1169 0.1384 0.1152 0.0126  -0.0022 -0.0108 91  THR   B CA  
1506 C C   . THR   B 77  ? 0.1337 0.1313 0.0989 -0.0059 0.0058  -0.0345 91  THR   B C   
1507 O O   . THR   B 77  ? 0.1599 0.1572 0.1327 -0.0134 0.0262  -0.0369 91  THR   B O   
1508 C CB  . THR   B 77  ? 0.1421 0.1390 0.1039 -0.0047 -0.0165 0.0074  91  THR   B CB  
1509 O OG1 . THR   B 77  ? 0.1605 0.1594 0.1045 -0.0113 0.0012  0.0064  91  THR   B OG1 
1510 C CG2 . THR   B 77  ? 0.1707 0.1334 0.1445 -0.0193 -0.0063 0.0000  91  THR   B CG2 
1511 N N   . TRP   B 78  ? 0.1176 0.1135 0.1110 -0.0045 0.0017  -0.0071 92  TRP   B N   
1512 C CA  . TRP   B 78  ? 0.1280 0.1252 0.1020 0.0032  -0.0089 -0.0099 92  TRP   B CA  
1513 C C   . TRP   B 78  ? 0.1148 0.1158 0.1099 0.0082  -0.0016 -0.0149 92  TRP   B C   
1514 O O   . TRP   B 78  ? 0.1206 0.1206 0.1130 0.0050  -0.0052 -0.0087 92  TRP   B O   
1515 C CB  . TRP   B 78  ? 0.1381 0.1387 0.1009 0.0197  -0.0022 -0.0059 92  TRP   B CB  
1516 C CG  . TRP   B 78  ? 0.1278 0.1359 0.0985 0.0227  -0.0023 -0.0054 92  TRP   B CG  
1517 C CD1 . TRP   B 78  ? 0.1467 0.1403 0.1065 0.0208  0.0089  -0.0093 92  TRP   B CD1 
1518 C CD2 . TRP   B 78  ? 0.1188 0.1429 0.1169 0.0102  -0.0003 -0.0023 92  TRP   B CD2 
1519 N NE1 . TRP   B 78  ? 0.1247 0.1466 0.1155 0.0157  -0.0004 -0.0029 92  TRP   B NE1 
1520 C CE2 . TRP   B 78  ? 0.1167 0.1522 0.1218 0.0100  -0.0037 -0.0038 92  TRP   B CE2 
1521 C CE3 . TRP   B 78  ? 0.1329 0.1620 0.1026 -0.0039 -0.0017 0.0011  92  TRP   B CE3 
1522 C CZ2 . TRP   B 78  ? 0.1263 0.1523 0.1152 0.0007  0.0059  0.0068  92  TRP   B CZ2 
1523 C CZ3 . TRP   B 78  ? 0.1304 0.1678 0.1150 0.0206  0.0037  -0.0106 92  TRP   B CZ3 
1524 C CH2 . TRP   B 78  ? 0.1337 0.1590 0.1166 0.0051  -0.0103 -0.0175 92  TRP   B CH2 
1525 N N   . SER   B 79  ? 0.1076 0.1186 0.1002 0.0057  -0.0037 0.0014  93  SER   B N   
1526 C CA  . SER   B 79  ? 0.1055 0.1250 0.1077 -0.0035 -0.0115 0.0118  93  SER   B CA  
1527 C C   . SER   B 79  ? 0.1071 0.1182 0.1246 0.0172  0.0062  0.0002  93  SER   B C   
1528 O O   . SER   B 79  ? 0.1237 0.1067 0.1352 0.0143  0.0114  -0.0118 93  SER   B O   
1529 C CB  . SER   B 79  ? 0.1348 0.1525 0.1119 0.0164  -0.0088 0.0167  93  SER   B CB  
1530 O OG  . SER   B 79  ? 0.1387 0.1792 0.1264 0.0019  -0.0076 0.0287  93  SER   B OG  
1531 N N   . GLY   B 80  ? 0.1080 0.1207 0.1105 -0.0054 -0.0016 0.0096  94  GLY   B N   
1532 C CA  . GLY   B 80  ? 0.1268 0.1191 0.1247 0.0034  0.0116  -0.0025 94  GLY   B CA  
1533 C C   . GLY   B 80  ? 0.1223 0.1145 0.1095 -0.0001 0.0044  0.0005  94  GLY   B C   
1534 O O   . GLY   B 80  ? 0.1403 0.1192 0.1219 0.0022  0.0071  -0.0067 94  GLY   B O   
1535 N N   . GLN   B 81  ? 0.1244 0.1394 0.1226 -0.0056 0.0332  -0.0010 95  GLN   B N   
1536 C CA  . GLN   B 81  ? 0.1164 0.1705 0.1286 0.0068  0.0123  0.0069  95  GLN   B CA  
1537 C C   . GLN   B 81  ? 0.1191 0.1543 0.1338 0.0148  0.0262  0.0087  95  GLN   B C   
1538 O O   . GLN   B 81  ? 0.1385 0.1536 0.1338 0.0103  0.0161  0.0011  95  GLN   B O   
1539 C CB  . GLN   B 81  ? 0.1710 0.1970 0.1636 0.0064  0.0219  -0.0052 95  GLN   B CB  
1540 C CG  . GLN   B 81  ? 0.1691 0.1973 0.1945 -0.0057 0.0129  -0.0002 95  GLN   B CG  
1541 C CD  . GLN   B 81  ? 0.1371 0.1931 0.1744 0.0028  -0.0035 -0.0201 95  GLN   B CD  
1542 O OE1 . GLN   B 81  ? 0.1299 0.1922 0.1725 0.0087  0.0122  -0.0130 95  GLN   B OE1 
1543 N NE2 . GLN   B 81  ? 0.1591 0.1997 0.1725 -0.0104 -0.0074 -0.0096 95  GLN   B NE2 
1544 N N   . TYR   B 82  ? 0.1304 0.1708 0.1202 -0.0103 0.0196  0.0063  96  TYR   B N   
1545 C CA  . TYR   B 82  ? 0.1337 0.1821 0.1138 -0.0210 0.0307  0.0022  96  TYR   B CA  
1546 C C   . TYR   B 82  ? 0.1326 0.1862 0.1389 -0.0023 0.0095  0.0276  96  TYR   B C   
1547 O O   . TYR   B 82  ? 0.1414 0.1938 0.1651 -0.0019 -0.0034 0.0298  96  TYR   B O   
1548 C CB  . TYR   B 82  ? 0.1582 0.1886 0.1223 -0.0054 0.0241  -0.0101 96  TYR   B CB  
1549 C CG  . TYR   B 82  ? 0.1469 0.2069 0.1285 -0.0024 0.0181  -0.0082 96  TYR   B CG  
1550 C CD1 . TYR   B 82  ? 0.1711 0.2274 0.1067 -0.0159 0.0094  -0.0043 96  TYR   B CD1 
1551 C CD2 . TYR   B 82  ? 0.1775 0.2379 0.1549 0.0011  0.0330  -0.0030 96  TYR   B CD2 
1552 C CE1 . TYR   B 82  ? 0.2223 0.2455 0.1390 -0.0150 0.0343  -0.0029 96  TYR   B CE1 
1553 C CE2 . TYR   B 82  ? 0.2160 0.2510 0.1516 -0.0038 0.0566  0.0045  96  TYR   B CE2 
1554 C CZ  . TYR   B 82  ? 0.2226 0.2623 0.1316 -0.0208 0.0628  0.0010  96  TYR   B CZ  
1555 O OH  . TYR   B 82  ? 0.2679 0.3031 0.1732 -0.0405 0.0855  -0.0022 96  TYR   B OH  
1556 N N   . VAL   B 83  ? 0.1505 0.1974 0.1576 -0.0327 0.0221  0.0306  97  VAL   B N   
1557 C CA  . VAL   B 83  ? 0.1751 0.2378 0.2067 -0.0326 0.0193  0.0449  97  VAL   B CA  
1558 C C   . VAL   B 83  ? 0.1763 0.2755 0.2513 -0.0187 0.0717  0.0840  97  VAL   B C   
1559 O O   . VAL   B 83  ? 0.2001 0.2837 0.2727 0.0144  0.0831  0.1082  97  VAL   B O   
1560 C CB  . VAL   B 83  ? 0.2171 0.2394 0.2522 -0.0592 -0.0180 0.0285  97  VAL   B CB  
1561 C CG1 . VAL   B 83  ? 0.2365 0.2573 0.2986 -0.0690 -0.0453 0.0266  97  VAL   B CG1 
1562 C CG2 . VAL   B 83  ? 0.2458 0.2442 0.2477 -0.0559 -0.0367 0.0136  97  VAL   B CG2 
1563 N N   . GLY   B 84  ? 0.2031 0.2993 0.2713 -0.0240 0.0767  0.0853  98  GLY   B N   
1564 C CA  . GLY   B 84  ? 0.2430 0.3404 0.3182 -0.0356 0.0911  0.0858  98  GLY   B CA  
1565 C C   . GLY   B 84  ? 0.2896 0.3789 0.3652 -0.0543 0.1177  0.0937  98  GLY   B C   
1566 O O   . GLY   B 84  ? 0.3062 0.3938 0.4152 -0.0706 0.1505  0.0785  98  GLY   B O   
1567 N N   . GLY   B 85  ? 0.3544 0.3996 0.3767 -0.0503 0.1017  0.1344  99  GLY   B N   
1568 C CA  . GLY   B 85  ? 0.3772 0.4105 0.3751 -0.0485 0.0957  0.1603  99  GLY   B CA  
1569 C C   . GLY   B 85  ? 0.3931 0.4142 0.3459 -0.0518 0.1129  0.1755  99  GLY   B C   
1570 O O   . GLY   B 85  ? 0.4195 0.4288 0.3287 -0.0343 0.1092  0.1826  99  GLY   B O   
1571 N N   . ALA   B 86  ? 0.4012 0.4193 0.3672 -0.0620 0.1159  0.1796  100 ALA   B N   
1572 C CA  . ALA   B 86  ? 0.4150 0.4170 0.3856 -0.0664 0.1137  0.1590  100 ALA   B CA  
1573 C C   . ALA   B 86  ? 0.4147 0.4069 0.3867 -0.0682 0.1071  0.1416  100 ALA   B C   
1574 O O   . ALA   B 86  ? 0.4452 0.4215 0.3888 -0.0664 0.1317  0.1373  100 ALA   B O   
1575 C CB  . ALA   B 86  ? 0.4161 0.4211 0.3935 -0.0753 0.1229  0.1599  100 ALA   B CB  
1576 N N   . GLU   B 87  ? 0.3817 0.3780 0.3861 -0.0851 0.0977  0.1110  101 GLU   B N   
1577 C CA  . GLU   B 87  ? 0.3692 0.3499 0.3642 -0.0833 0.0937  0.0860  101 GLU   B CA  
1578 C C   . GLU   B 87  ? 0.3016 0.3128 0.3233 -0.0792 0.0647  0.0797  101 GLU   B C   
1579 O O   . GLU   B 87  ? 0.3036 0.2995 0.3440 -0.0987 0.0410  0.0575  101 GLU   B O   
1580 C CB  . GLU   B 87  ? 0.4015 0.3623 0.3832 -0.0798 0.0978  0.0826  101 GLU   B CB  
1581 C CG  . GLU   B 87  ? 0.4164 0.3706 0.4011 -0.0719 0.0937  0.0806  101 GLU   B CG  
1582 C CD  . GLU   B 87  ? 0.4238 0.3778 0.4063 -0.0654 0.0725  0.0837  101 GLU   B CD  
1583 O OE1 . GLU   B 87  ? 0.4306 0.3834 0.4063 -0.0606 0.0703  0.0810  101 GLU   B OE1 
1584 O OE2 . GLU   B 87  ? 0.4238 0.3784 0.4102 -0.0595 0.0596  0.0856  101 GLU   B OE2 
1585 N N   . ALA   B 88  ? 0.2365 0.2859 0.2630 -0.0667 0.0634  0.0911  102 ALA   B N   
1586 C CA  . ALA   B 88  ? 0.1819 0.2591 0.2029 -0.0689 0.0486  0.0787  102 ALA   B CA  
1587 C C   . ALA   B 88  ? 0.1921 0.2396 0.1806 -0.0444 0.0191  0.0744  102 ALA   B C   
1588 O O   . ALA   B 88  ? 0.2107 0.2430 0.1956 -0.0421 -0.0073 0.0868  102 ALA   B O   
1589 C CB  . ALA   B 88  ? 0.1961 0.2796 0.2013 -0.0479 0.0295  0.0524  102 ALA   B CB  
1590 N N   . ARG   B 89  ? 0.1838 0.2064 0.1418 -0.0403 0.0168  0.0491  103 ARG   B N   
1591 C CA  . ARG   B 89  ? 0.2038 0.1796 0.1473 -0.0456 0.0363  0.0237  103 ARG   B CA  
1592 C C   . ARG   B 89  ? 0.1660 0.1650 0.1199 -0.0187 0.0188  0.0282  103 ARG   B C   
1593 O O   . ARG   B 89  ? 0.1586 0.1739 0.1777 -0.0023 0.0258  0.0353  103 ARG   B O   
1594 C CB  . ARG   B 89  ? 0.2730 0.1877 0.2170 -0.0341 0.0267  0.0198  103 ARG   B CB  
1595 C CG  . ARG   B 89  ? 0.3202 0.1986 0.2743 -0.0294 0.0012  0.0251  103 ARG   B CG  
1596 C CD  . ARG   B 89  ? 0.3598 0.2100 0.3481 -0.0435 -0.0099 0.0223  103 ARG   B CD  
1597 N NE  . ARG   B 89  ? 0.3870 0.2188 0.3883 -0.0570 -0.0229 0.0199  103 ARG   B NE  
1598 C CZ  . ARG   B 89  ? 0.4146 0.2297 0.4129 -0.0511 -0.0320 0.0199  103 ARG   B CZ  
1599 N NH1 . ARG   B 89  ? 0.4095 0.2384 0.4027 -0.0475 -0.0267 0.0123  103 ARG   B NH1 
1600 N NH2 . ARG   B 89  ? 0.4404 0.2347 0.4458 -0.0553 -0.0365 0.0163  103 ARG   B NH2 
1601 N N   . ILE   B 90  ? 0.1601 0.1576 0.1132 -0.0245 0.0232  0.0171  104 ILE   B N   
1602 C CA  . ILE   B 90  ? 0.1513 0.1413 0.1092 -0.0204 0.0136  0.0126  104 ILE   B CA  
1603 C C   . ILE   B 90  ? 0.1540 0.1413 0.1029 0.0006  0.0008  0.0102  104 ILE   B C   
1604 O O   . ILE   B 90  ? 0.1715 0.1411 0.1289 0.0167  -0.0006 0.0091  104 ILE   B O   
1605 C CB  . ILE   B 90  ? 0.1729 0.1465 0.1110 -0.0113 0.0180  -0.0004 104 ILE   B CB  
1606 C CG1 . ILE   B 90  ? 0.1797 0.1595 0.1196 -0.0286 0.0251  -0.0094 104 ILE   B CG1 
1607 C CG2 . ILE   B 90  ? 0.2212 0.1588 0.1273 -0.0161 0.0416  0.0019  104 ILE   B CG2 
1608 C CD1 . ILE   B 90  ? 0.2003 0.1694 0.1481 -0.0265 0.0238  -0.0089 104 ILE   B CD1 
1609 N N   . ASN   B 91  ? 0.1645 0.1351 0.1062 -0.0207 0.0107  0.0111  105 ASN   B N   
1610 C CA  . ASN   B 91  ? 0.1587 0.1365 0.1226 -0.0277 0.0072  -0.0009 105 ASN   B CA  
1611 C C   . ASN   B 91  ? 0.1419 0.1267 0.1119 -0.0136 0.0124  0.0117  105 ASN   B C   
1612 O O   . ASN   B 91  ? 0.1420 0.1198 0.1333 0.0056  0.0210  0.0226  105 ASN   B O   
1613 C CB  . ASN   B 91  ? 0.1760 0.1673 0.1633 -0.0572 0.0038  0.0325  105 ASN   B CB  
1614 C CG  . ASN   B 91  ? 0.2052 0.1948 0.2191 -0.0506 -0.0073 0.0511  105 ASN   B CG  
1615 O OD1 . ASN   B 91  ? 0.2144 0.1978 0.2352 -0.0495 -0.0133 0.0565  105 ASN   B OD1 
1616 N ND2 . ASN   B 91  ? 0.2044 0.2087 0.2427 -0.0625 -0.0315 0.0583  105 ASN   B ND2 
1617 N N   . THR   B 92  ? 0.1504 0.1313 0.0942 -0.0028 0.0096  0.0083  106 THR   B N   
1618 C CA  . THR   B 92  ? 0.1467 0.1231 0.0982 0.0102  0.0080  -0.0053 106 THR   B CA  
1619 C C   . THR   B 92  ? 0.1453 0.1081 0.0995 0.0259  0.0091  0.0086  106 THR   B C   
1620 O O   . THR   B 92  ? 0.1476 0.1204 0.1181 0.0155  0.0036  0.0016  106 THR   B O   
1621 C CB  . THR   B 92  ? 0.1437 0.1234 0.1122 0.0213  -0.0204 -0.0053 106 THR   B CB  
1622 O OG1 . THR   B 92  ? 0.1520 0.1209 0.1247 0.0062  -0.0182 0.0161  106 THR   B OG1 
1623 C CG2 . THR   B 92  ? 0.1656 0.1470 0.1134 0.0084  -0.0075 -0.0128 106 THR   B CG2 
1624 N N   . GLN   B 93  ? 0.1311 0.1244 0.0879 0.0052  0.0146  -0.0057 107 GLN   B N   
1625 C CA  . GLN   B 93  ? 0.1379 0.1311 0.1019 -0.0042 0.0022  -0.0026 107 GLN   B CA  
1626 C C   . GLN   B 93  ? 0.1409 0.1039 0.1082 0.0089  -0.0027 -0.0056 107 GLN   B C   
1627 O O   . GLN   B 93  ? 0.1309 0.1233 0.1535 0.0137  -0.0019 -0.0298 107 GLN   B O   
1628 C CB  . GLN   B 93  ? 0.1456 0.1438 0.1089 -0.0219 0.0010  -0.0150 107 GLN   B CB  
1629 C CG  . GLN   B 93  ? 0.1748 0.1592 0.1265 -0.0357 -0.0149 -0.0277 107 GLN   B CG  
1630 C CD  . GLN   B 93  ? 0.1773 0.1685 0.1449 0.0005  -0.0027 -0.0333 107 GLN   B CD  
1631 O OE1 . GLN   B 93  ? 0.1807 0.2104 0.1712 0.0220  -0.0185 -0.0370 107 GLN   B OE1 
1632 N NE2 . GLN   B 93  ? 0.1845 0.1595 0.1468 0.0128  -0.0024 0.0015  107 GLN   B NE2 
1633 N N   . TRP   B 94  ? 0.1369 0.1124 0.1045 0.0028  -0.0101 -0.0072 108 TRP   B N   
1634 C CA  . TRP   B 94  ? 0.1448 0.1190 0.0915 0.0054  0.0108  -0.0120 108 TRP   B CA  
1635 C C   . TRP   B 94  ? 0.1343 0.1109 0.0938 0.0083  0.0026  -0.0107 108 TRP   B C   
1636 O O   . TRP   B 94  ? 0.1585 0.1237 0.0980 0.0056  0.0029  -0.0040 108 TRP   B O   
1637 C CB  . TRP   B 94  ? 0.1457 0.1265 0.1040 0.0044  -0.0022 -0.0004 108 TRP   B CB  
1638 C CG  . TRP   B 94  ? 0.1384 0.1290 0.1144 0.0156  0.0001  0.0026  108 TRP   B CG  
1639 C CD1 . TRP   B 94  ? 0.1472 0.1368 0.1376 0.0135  -0.0078 0.0084  108 TRP   B CD1 
1640 C CD2 . TRP   B 94  ? 0.1255 0.1362 0.1149 0.0029  -0.0018 -0.0057 108 TRP   B CD2 
1641 N NE1 . TRP   B 94  ? 0.1443 0.1339 0.1348 0.0280  -0.0010 0.0186  108 TRP   B NE1 
1642 C CE2 . TRP   B 94  ? 0.1410 0.1368 0.1312 0.0096  0.0017  0.0052  108 TRP   B CE2 
1643 C CE3 . TRP   B 94  ? 0.1392 0.1423 0.1036 0.0171  -0.0081 -0.0184 108 TRP   B CE3 
1644 C CZ2 . TRP   B 94  ? 0.1560 0.1372 0.1216 0.0147  0.0038  -0.0039 108 TRP   B CZ2 
1645 C CZ3 . TRP   B 94  ? 0.1390 0.1429 0.1307 0.0074  -0.0017 -0.0124 108 TRP   B CZ3 
1646 C CH2 . TRP   B 94  ? 0.1533 0.1388 0.1307 0.0186  -0.0005 -0.0086 108 TRP   B CH2 
1647 N N   . LEU   B 95  ? 0.1232 0.1270 0.1083 0.0142  0.0106  -0.0001 109 LEU   B N   
1648 C CA  . LEU   B 95  ? 0.1204 0.1443 0.1077 0.0034  -0.0014 -0.0030 109 LEU   B CA  
1649 C C   . LEU   B 95  ? 0.1240 0.1625 0.1112 0.0042  -0.0036 -0.0380 109 LEU   B C   
1650 O O   . LEU   B 95  ? 0.1603 0.1987 0.1368 0.0226  -0.0082 -0.0716 109 LEU   B O   
1651 C CB  . LEU   B 95  ? 0.1339 0.1377 0.1315 0.0080  -0.0009 0.0036  109 LEU   B CB  
1652 C CG  . LEU   B 95  ? 0.1349 0.1395 0.1517 0.0053  -0.0022 0.0016  109 LEU   B CG  
1653 C CD1 . LEU   B 95  ? 0.1510 0.1428 0.1635 0.0104  -0.0207 0.0096  109 LEU   B CD1 
1654 C CD2 . LEU   B 95  ? 0.1843 0.1656 0.1550 -0.0081 -0.0141 -0.0150 109 LEU   B CD2 
1655 N N   . LEU   B 96  ? 0.1168 0.1578 0.1169 -0.0001 0.0052  -0.0213 110 LEU   B N   
1656 C CA  . LEU   B 96  ? 0.1299 0.1491 0.1313 -0.0066 0.0082  -0.0208 110 LEU   B CA  
1657 C C   . LEU   B 96  ? 0.1125 0.1524 0.1085 -0.0058 0.0100  -0.0301 110 LEU   B C   
1658 O O   . LEU   B 96  ? 0.1231 0.1607 0.1187 -0.0120 0.0174  -0.0328 110 LEU   B O   
1659 C CB  . LEU   B 96  ? 0.1265 0.1549 0.1583 -0.0050 -0.0125 -0.0156 110 LEU   B CB  
1660 C CG  . LEU   B 96  ? 0.1524 0.1712 0.1555 0.0155  -0.0078 -0.0004 110 LEU   B CG  
1661 C CD1 . LEU   B 96  ? 0.1586 0.1897 0.1732 0.0238  -0.0116 -0.0211 110 LEU   B CD1 
1662 C CD2 . LEU   B 96  ? 0.1741 0.1704 0.1735 0.0320  0.0033  0.0183  110 LEU   B CD2 
1663 N N   . THR   B 97  ? 0.1157 0.1584 0.1386 -0.0174 0.0053  -0.0142 111 THR   B N   
1664 C CA  . THR   B 97  ? 0.1233 0.1643 0.1433 -0.0171 0.0016  -0.0109 111 THR   B CA  
1665 C C   . THR   B 97  ? 0.1281 0.1832 0.1346 -0.0279 0.0041  -0.0323 111 THR   B C   
1666 O O   . THR   B 97  ? 0.1431 0.1938 0.1416 -0.0209 0.0158  -0.0250 111 THR   B O   
1667 C CB  . THR   B 97  ? 0.1299 0.1656 0.1598 -0.0125 0.0083  -0.0028 111 THR   B CB  
1668 O OG1 . THR   B 97  ? 0.1431 0.1723 0.1729 -0.0213 -0.0061 0.0036  111 THR   B OG1 
1669 C CG2 . THR   B 97  ? 0.1774 0.1679 0.1803 -0.0248 0.0486  0.0069  111 THR   B CG2 
1670 N N   . SER   B 98  ? 0.1170 0.1976 0.1491 -0.0195 0.0137  -0.0247 112 SER   B N   
1671 C CA  . SER   B 98  ? 0.1266 0.2263 0.1616 -0.0008 0.0082  -0.0338 112 SER   B CA  
1672 C C   . SER   B 98  ? 0.1373 0.2460 0.1572 -0.0216 0.0199  -0.0416 112 SER   B C   
1673 O O   . SER   B 98  ? 0.1602 0.2517 0.1501 -0.0301 0.0187  -0.0358 112 SER   B O   
1674 C CB  . SER   B 98  ? 0.1365 0.2298 0.1990 0.0186  0.0212  -0.0352 112 SER   B CB  
1675 O OG  . SER   B 98  ? 0.1521 0.2339 0.2195 0.0340  -0.0098 -0.0216 112 SER   B OG  
1676 N N   . GLY   B 99  ? 0.1448 0.2440 0.1662 -0.0332 0.0254  -0.0431 113 GLY   B N   
1677 C CA  . GLY   B 99  ? 0.1542 0.2595 0.1844 -0.0336 0.0264  -0.0469 113 GLY   B CA  
1678 C C   . GLY   B 99  ? 0.1678 0.2778 0.1961 -0.0240 0.0374  -0.0380 113 GLY   B C   
1679 O O   . GLY   B 99  ? 0.1902 0.2897 0.1920 -0.0176 0.0460  -0.0215 113 GLY   B O   
1680 N N   . THR   B 100 ? 0.1589 0.2833 0.1906 -0.0329 0.0514  -0.0481 114 THR   B N   
1681 C CA  . THR   B 100 ? 0.1563 0.2896 0.1910 -0.0294 0.0533  -0.0583 114 THR   B CA  
1682 C C   . THR   B 100 ? 0.1819 0.3037 0.1761 -0.0356 0.0471  -0.0611 114 THR   B C   
1683 O O   . THR   B 100 ? 0.1943 0.2902 0.1848 -0.0448 0.0602  -0.0660 114 THR   B O   
1684 C CB  . THR   B 100 ? 0.1573 0.2861 0.2029 -0.0212 0.0462  -0.0605 114 THR   B CB  
1685 O OG1 . THR   B 100 ? 0.1613 0.2827 0.2182 -0.0256 0.0284  -0.0564 114 THR   B OG1 
1686 C CG2 . THR   B 100 ? 0.1875 0.2925 0.2277 -0.0267 0.0399  -0.0602 114 THR   B CG2 
1687 N N   . THR   B 101 ? 0.1765 0.3234 0.1976 -0.0434 0.0443  -0.0503 115 THR   B N   
1688 C CA  . THR   B 101 ? 0.1771 0.3469 0.2172 -0.0253 0.0593  -0.0455 115 THR   B CA  
1689 C C   . THR   B 101 ? 0.1872 0.3560 0.1976 -0.0345 0.0602  -0.0494 115 THR   B C   
1690 O O   . THR   B 101 ? 0.1834 0.3410 0.1829 -0.0429 0.0451  -0.0411 115 THR   B O   
1691 C CB  . THR   B 101 ? 0.1943 0.3626 0.2570 -0.0227 0.0467  -0.0350 115 THR   B CB  
1692 O OG1 . THR   B 101 ? 0.2223 0.3605 0.2413 0.0094  0.0492  -0.0324 115 THR   B OG1 
1693 C CG2 . THR   B 101 ? 0.1989 0.3737 0.2635 -0.0353 0.0293  -0.0423 115 THR   B CG2 
1694 N N   . GLU   B 102 ? 0.2258 0.3730 0.2220 -0.0568 0.0617  -0.0297 116 GLU   B N   
1695 C CA  A GLU   B 102 ? 0.2497 0.3761 0.2199 -0.0549 0.0558  -0.0340 116 GLU   B CA  
1696 C CA  B GLU   B 102 ? 0.2673 0.3801 0.2274 -0.0542 0.0648  -0.0269 116 GLU   B CA  
1697 C C   . GLU   B 102 ? 0.2451 0.3787 0.2027 -0.0513 0.0744  -0.0416 116 GLU   B C   
1698 O O   . GLU   B 102 ? 0.2324 0.3845 0.1827 -0.0469 0.0496  -0.0446 116 GLU   B O   
1699 C CB  A GLU   B 102 ? 0.2664 0.3783 0.2435 -0.0564 0.0372  -0.0336 116 GLU   B CB  
1700 C CB  B GLU   B 102 ? 0.3091 0.3936 0.2761 -0.0501 0.0570  -0.0131 116 GLU   B CB  
1701 C CG  A GLU   B 102 ? 0.2889 0.3809 0.2680 -0.0546 0.0194  -0.0328 116 GLU   B CG  
1702 C CG  B GLU   B 102 ? 0.3578 0.4071 0.3266 -0.0381 0.0418  -0.0009 116 GLU   B CG  
1703 C CD  A GLU   B 102 ? 0.3098 0.3839 0.2868 -0.0529 0.0068  -0.0305 116 GLU   B CD  
1704 C CD  B GLU   B 102 ? 0.4152 0.4188 0.3695 -0.0240 0.0152  0.0043  116 GLU   B CD  
1705 O OE1 A GLU   B 102 ? 0.3231 0.3890 0.3028 -0.0514 0.0037  -0.0219 116 GLU   B OE1 
1706 O OE1 B GLU   B 102 ? 0.4343 0.4307 0.3958 -0.0247 0.0114  0.0095  116 GLU   B OE1 
1707 O OE2 A GLU   B 102 ? 0.3152 0.3833 0.2905 -0.0511 0.0002  -0.0310 116 GLU   B OE2 
1708 O OE2 B GLU   B 102 ? 0.4425 0.4230 0.3892 -0.0163 0.0048  0.0156  116 GLU   B OE2 
1709 N N   . ALA   B 103 ? 0.2245 0.3732 0.2093 -0.0402 0.0889  -0.0614 117 ALA   B N   
1710 C CA  . ALA   B 103 ? 0.2199 0.3688 0.2238 -0.0323 0.0845  -0.0647 117 ALA   B CA  
1711 C C   . ALA   B 103 ? 0.2005 0.3475 0.2163 -0.0311 0.0600  -0.0719 117 ALA   B C   
1712 O O   . ALA   B 103 ? 0.2341 0.3512 0.2289 -0.0237 0.0759  -0.0886 117 ALA   B O   
1713 C CB  . ALA   B 103 ? 0.2212 0.3791 0.2384 -0.0216 0.0921  -0.0575 117 ALA   B CB  
1714 N N   . ASN   B 104 ? 0.1713 0.3278 0.2185 -0.0147 0.0683  -0.0542 118 ASN   B N   
1715 C CA  . ASN   B 104 ? 0.1597 0.3150 0.2303 -0.0096 0.0465  -0.0476 118 ASN   B CA  
1716 C C   . ASN   B 104 ? 0.1655 0.2884 0.2111 -0.0103 0.0506  -0.0428 118 ASN   B C   
1717 O O   . ASN   B 104 ? 0.1847 0.2713 0.1994 -0.0135 0.0451  -0.0300 118 ASN   B O   
1718 C CB  . ASN   B 104 ? 0.1719 0.3248 0.2663 0.0242  0.0415  -0.0650 118 ASN   B CB  
1719 C CG  . ASN   B 104 ? 0.2007 0.3495 0.3147 0.0394  0.0347  -0.0745 118 ASN   B CG  
1720 O OD1 . ASN   B 104 ? 0.2413 0.3558 0.3302 0.0581  0.0435  -0.0779 118 ASN   B OD1 
1721 N ND2 . ASN   B 104 ? 0.2015 0.3616 0.3542 0.0464  0.0196  -0.0656 118 ASN   B ND2 
1722 N N   . ALA   B 105 ? 0.1399 0.2703 0.1939 -0.0148 0.0280  -0.0413 119 ALA   B N   
1723 C CA  . ALA   B 105 ? 0.1492 0.2684 0.1817 -0.0213 0.0210  -0.0357 119 ALA   B CA  
1724 C C   . ALA   B 105 ? 0.1558 0.2804 0.1806 -0.0282 0.0311  -0.0450 119 ALA   B C   
1725 O O   . ALA   B 105 ? 0.1563 0.2766 0.1878 -0.0157 0.0412  -0.0532 119 ALA   B O   
1726 C CB  . ALA   B 105 ? 0.2032 0.2640 0.2246 -0.0175 0.0424  -0.0289 119 ALA   B CB  
1727 N N   . TRP   B 106 ? 0.1843 0.3004 0.1706 -0.0478 0.0280  -0.0505 120 TRP   B N   
1728 C CA  . TRP   B 106 ? 0.2110 0.3109 0.1708 -0.0519 0.0512  -0.0701 120 TRP   B CA  
1729 C C   . TRP   B 106 ? 0.2157 0.3054 0.2081 -0.0602 0.0594  -0.0760 120 TRP   B C   
1730 O O   . TRP   B 106 ? 0.2168 0.3096 0.2137 -0.0812 0.0728  -0.0837 120 TRP   B O   
1731 C CB  . TRP   B 106 ? 0.2497 0.3256 0.1923 -0.0604 0.0618  -0.0782 120 TRP   B CB  
1732 C CG  . TRP   B 106 ? 0.2327 0.3292 0.2261 -0.0765 0.0751  -0.0922 120 TRP   B CG  
1733 C CD1 . TRP   B 106 ? 0.2309 0.3343 0.2481 -0.0690 0.0757  -0.0979 120 TRP   B CD1 
1734 C CD2 . TRP   B 106 ? 0.2566 0.3343 0.2726 -0.0678 0.0897  -0.0914 120 TRP   B CD2 
1735 N NE1 . TRP   B 106 ? 0.2646 0.3448 0.2792 -0.0549 0.0865  -0.0961 120 TRP   B NE1 
1736 C CE2 . TRP   B 106 ? 0.2742 0.3404 0.3036 -0.0599 0.0775  -0.0875 120 TRP   B CE2 
1737 C CE3 . TRP   B 106 ? 0.2719 0.3344 0.2920 -0.0691 0.0887  -0.0783 120 TRP   B CE3 
1738 C CZ2 . TRP   B 106 ? 0.2829 0.3400 0.3343 -0.0465 0.0776  -0.0879 120 TRP   B CZ2 
1739 C CZ3 . TRP   B 106 ? 0.3050 0.3421 0.3171 -0.0497 0.0919  -0.0759 120 TRP   B CZ3 
1740 C CH2 . TRP   B 106 ? 0.3012 0.3414 0.3414 -0.0354 0.0801  -0.0787 120 TRP   B CH2 
1741 N N   . LYS   B 107 ? 0.2230 0.2908 0.2028 -0.0379 0.0616  -0.0763 121 LYS   B N   
1742 C CA  . LYS   B 107 ? 0.2131 0.2747 0.2296 -0.0138 0.0605  -0.0607 121 LYS   B CA  
1743 C C   . LYS   B 107 ? 0.1666 0.2628 0.1939 0.0058  0.0531  -0.0347 121 LYS   B C   
1744 O O   . LYS   B 107 ? 0.1706 0.2672 0.2332 0.0324  0.0576  -0.0141 121 LYS   B O   
1745 C CB  . LYS   B 107 ? 0.2498 0.2776 0.3056 -0.0004 0.0776  -0.0667 121 LYS   B CB  
1746 C CG  . LYS   B 107 ? 0.2527 0.2757 0.3707 0.0254  0.1200  -0.0727 121 LYS   B CG  
1747 C CD  . LYS   B 107 ? 0.2464 0.2863 0.4379 0.0358  0.1361  -0.0596 121 LYS   B CD  
1748 C CE  . LYS   B 107 ? 0.2915 0.3032 0.5132 0.0522  0.1345  -0.0559 121 LYS   B CE  
1749 N NZ  . LYS   B 107 ? 0.3284 0.3161 0.5744 0.0542  0.1228  -0.0479 121 LYS   B NZ  
1750 N N   . SER   B 108 ? 0.1566 0.2364 0.1482 0.0060  0.0358  -0.0287 122 SER   B N   
1751 C CA  . SER   B 108 ? 0.1480 0.2075 0.1392 0.0001  0.0284  -0.0363 122 SER   B CA  
1752 C C   . SER   B 108 ? 0.1449 0.1893 0.1427 0.0075  0.0100  -0.0196 122 SER   B C   
1753 O O   . SER   B 108 ? 0.1492 0.1910 0.1463 -0.0018 0.0220  -0.0234 122 SER   B O   
1754 C CB  . SER   B 108 ? 0.1651 0.2184 0.1734 -0.0164 0.0334  -0.0334 122 SER   B CB  
1755 O OG  . SER   B 108 ? 0.2428 0.2237 0.1719 0.0135  0.0159  -0.0217 122 SER   B OG  
1756 N N   . THR   B 109 ? 0.1343 0.1713 0.1498 0.0119  0.0105  -0.0094 123 THR   B N   
1757 C CA  . THR   B 109 ? 0.1324 0.1452 0.1308 0.0079  0.0221  -0.0117 123 THR   B CA  
1758 C C   . THR   B 109 ? 0.1494 0.1415 0.1228 0.0009  0.0020  -0.0295 123 THR   B C   
1759 O O   . THR   B 109 ? 0.1823 0.1431 0.1280 0.0028  -0.0186 -0.0138 123 THR   B O   
1760 C CB  . THR   B 109 ? 0.1433 0.1461 0.1449 0.0168  0.0005  0.0000  123 THR   B CB  
1761 O OG1 . THR   B 109 ? 0.1780 0.1582 0.2066 -0.0024 0.0001  0.0091  123 THR   B OG1 
1762 C CG2 . THR   B 109 ? 0.1367 0.1600 0.1461 0.0205  0.0078  0.0027  123 THR   B CG2 
1763 N N   . LEU   B 110 ? 0.1277 0.1554 0.1204 0.0093  0.0068  -0.0173 124 LEU   B N   
1764 C CA  . LEU   B 110 ? 0.1297 0.1597 0.1270 0.0040  0.0026  -0.0203 124 LEU   B CA  
1765 C C   . LEU   B 110 ? 0.1451 0.1478 0.1159 -0.0001 -0.0012 -0.0368 124 LEU   B C   
1766 O O   . LEU   B 110 ? 0.1450 0.1382 0.1254 0.0141  -0.0080 -0.0278 124 LEU   B O   
1767 C CB  . LEU   B 110 ? 0.1443 0.1884 0.1381 0.0194  0.0003  -0.0192 124 LEU   B CB  
1768 C CG  . LEU   B 110 ? 0.1585 0.2074 0.1494 0.0263  -0.0039 -0.0280 124 LEU   B CG  
1769 C CD1 . LEU   B 110 ? 0.1708 0.2255 0.1561 0.0241  -0.0325 -0.0251 124 LEU   B CD1 
1770 C CD2 . LEU   B 110 ? 0.1891 0.2079 0.1814 0.0372  -0.0044 -0.0413 124 LEU   B CD2 
1771 N N   . VAL   B 111 ? 0.1335 0.1503 0.1272 0.0039  0.0055  -0.0296 125 VAL   B N   
1772 C CA  . VAL   B 111 ? 0.1520 0.1417 0.1122 0.0122  -0.0008 -0.0225 125 VAL   B CA  
1773 C C   . VAL   B 111 ? 0.1538 0.1365 0.0919 0.0105  -0.0013 -0.0159 125 VAL   B C   
1774 O O   . VAL   B 111 ? 0.1336 0.1477 0.1378 0.0114  0.0015  -0.0274 125 VAL   B O   
1775 C CB  . VAL   B 111 ? 0.1710 0.1508 0.1179 0.0260  -0.0074 -0.0222 125 VAL   B CB  
1776 C CG1 . VAL   B 111 ? 0.1959 0.1468 0.1311 0.0106  -0.0100 -0.0434 125 VAL   B CG1 
1777 C CG2 . VAL   B 111 ? 0.1561 0.1568 0.1547 0.0424  -0.0305 -0.0085 125 VAL   B CG2 
1778 N N   . GLY   B 112 ? 0.1591 0.1350 0.0935 0.0062  -0.0016 -0.0114 126 GLY   B N   
1779 C CA  . GLY   B 112 ? 0.1564 0.1195 0.1255 0.0184  0.0085  -0.0152 126 GLY   B CA  
1780 C C   . GLY   B 112 ? 0.1381 0.1115 0.1138 0.0121  -0.0095 -0.0044 126 GLY   B C   
1781 O O   . GLY   B 112 ? 0.1586 0.1114 0.1204 0.0196  0.0044  -0.0035 126 GLY   B O   
1782 N N   . HIS   B 113 ? 0.1501 0.1171 0.1244 0.0196  0.0028  -0.0040 127 HIS   B N   
1783 C CA  . HIS   B 113 ? 0.1579 0.1371 0.1323 0.0251  0.0008  -0.0039 127 HIS   B CA  
1784 C C   . HIS   B 113 ? 0.1628 0.1553 0.1291 0.0476  0.0050  0.0155  127 HIS   B C   
1785 O O   . HIS   B 113 ? 0.2452 0.2039 0.1546 0.1045  0.0397  0.0321  127 HIS   B O   
1786 C CB  . HIS   B 113 ? 0.1849 0.1515 0.1940 0.0003  -0.0191 -0.0207 127 HIS   B CB  
1787 C CG  . HIS   B 113 ? 0.2371 0.1739 0.2402 -0.0199 -0.0407 -0.0252 127 HIS   B CG  
1788 N ND1 . HIS   B 113 ? 0.3100 0.1871 0.3184 -0.0403 -0.0238 -0.0286 127 HIS   B ND1 
1789 C CD2 . HIS   B 113 ? 0.2533 0.1775 0.2802 -0.0345 -0.0615 -0.0525 127 HIS   B CD2 
1790 C CE1 . HIS   B 113 ? 0.3275 0.1860 0.3402 -0.0429 -0.0291 -0.0389 127 HIS   B CE1 
1791 N NE2 . HIS   B 113 ? 0.3090 0.1922 0.3421 -0.0299 -0.0423 -0.0586 127 HIS   B NE2 
1792 N N   . ASP   B 114 ? 0.1811 0.1400 0.1145 0.0255  0.0265  0.0070  128 ASP   B N   
1793 C CA  A ASP   B 114 ? 0.1836 0.1580 0.1072 0.0175  0.0022  0.0064  128 ASP   B CA  
1794 C CA  B ASP   B 114 ? 0.1810 0.1545 0.1164 0.0139  0.0008  0.0101  128 ASP   B CA  
1795 C C   . ASP   B 114 ? 0.1662 0.1550 0.1057 0.0170  -0.0064 0.0126  128 ASP   B C   
1796 O O   . ASP   B 114 ? 0.1675 0.1505 0.1165 0.0231  0.0005  0.0049  128 ASP   B O   
1797 C CB  A ASP   B 114 ? 0.1894 0.1693 0.1365 0.0193  -0.0071 -0.0130 128 ASP   B CB  
1798 C CB  B ASP   B 114 ? 0.1889 0.1620 0.1460 0.0054  -0.0077 0.0049  128 ASP   B CB  
1799 C CG  A ASP   B 114 ? 0.1929 0.1639 0.1554 0.0258  -0.0021 -0.0097 128 ASP   B CG  
1800 C CG  B ASP   B 114 ? 0.1958 0.1507 0.1535 0.0072  -0.0137 0.0295  128 ASP   B CG  
1801 O OD1 A ASP   B 114 ? 0.2041 0.1613 0.1730 0.0321  0.0064  -0.0040 128 ASP   B OD1 
1802 O OD1 B ASP   B 114 ? 0.1976 0.1414 0.1700 0.0173  -0.0271 0.0383  128 ASP   B OD1 
1803 O OD2 A ASP   B 114 ? 0.1724 0.1730 0.1570 0.0263  0.0213  0.0025  128 ASP   B OD2 
1804 O OD2 B ASP   B 114 ? 0.2024 0.1631 0.1843 0.0061  -0.0104 0.0303  128 ASP   B OD2 
1805 N N   . THR   B 115 ? 0.1950 0.1685 0.1125 0.0088  0.0107  0.0101  129 THR   B N   
1806 C CA  A THR   B 115 ? 0.2016 0.1767 0.1166 -0.0136 0.0202  -0.0069 129 THR   B CA  
1807 C CA  B THR   B 115 ? 0.1833 0.1616 0.1180 0.0072  0.0023  0.0060  129 THR   B CA  
1808 C C   . THR   B 115 ? 0.1891 0.1553 0.1177 0.0069  -0.0006 0.0050  129 THR   B C   
1809 O O   . THR   B 115 ? 0.2098 0.1482 0.1430 0.0244  -0.0092 0.0189  129 THR   B O   
1810 C CB  A THR   B 115 ? 0.2423 0.2364 0.1540 -0.0620 0.0329  -0.0340 129 THR   B CB  
1811 C CB  B THR   B 115 ? 0.1760 0.1624 0.1229 0.0078  -0.0026 0.0048  129 THR   B CB  
1812 O OG1 A THR   B 115 ? 0.3217 0.2656 0.2085 -0.0661 -0.0053 -0.0278 129 THR   B OG1 
1813 O OG1 B THR   B 115 ? 0.1746 0.1622 0.1273 0.0082  -0.0027 0.0051  129 THR   B OG1 
1814 C CG2 A THR   B 115 ? 0.2303 0.2515 0.1916 -0.0639 0.0329  -0.0531 129 THR   B CG2 
1815 C CG2 B THR   B 115 ? 0.1748 0.1621 0.1266 0.0094  -0.0042 0.0046  129 THR   B CG2 
1816 N N   . PHE   B 116 ? 0.1991 0.1506 0.1175 0.0077  -0.0032 -0.0086 130 PHE   B N   
1817 C CA  . PHE   B 116 ? 0.2087 0.1561 0.1141 -0.0039 0.0010  -0.0033 130 PHE   B CA  
1818 C C   . PHE   B 116 ? 0.2251 0.1660 0.1251 -0.0210 0.0005  0.0083  130 PHE   B C   
1819 O O   . PHE   B 116 ? 0.2132 0.1707 0.1343 -0.0233 0.0110  0.0104  130 PHE   B O   
1820 C CB  . PHE   B 116 ? 0.1950 0.1490 0.1328 -0.0141 0.0105  -0.0024 130 PHE   B CB  
1821 C CG  . PHE   B 116 ? 0.1807 0.1508 0.1155 0.0013  -0.0155 -0.0002 130 PHE   B CG  
1822 C CD1 . PHE   B 116 ? 0.1876 0.1437 0.1103 0.0122  0.0048  -0.0086 130 PHE   B CD1 
1823 C CD2 . PHE   B 116 ? 0.1816 0.1640 0.1359 -0.0061 0.0038  0.0104  130 PHE   B CD2 
1824 C CE1 . PHE   B 116 ? 0.1739 0.1417 0.1315 0.0220  -0.0090 -0.0083 130 PHE   B CE1 
1825 C CE2 . PHE   B 116 ? 0.1866 0.1648 0.1422 -0.0019 0.0054  0.0116  130 PHE   B CE2 
1826 C CZ  . PHE   B 116 ? 0.2051 0.1523 0.1345 0.0095  0.0055  0.0066  130 PHE   B CZ  
1827 N N   . THR   B 117 ? 0.2523 0.1796 0.1361 -0.0494 -0.0113 0.0240  131 THR   B N   
1828 C CA  A THR   B 117 ? 0.2860 0.1999 0.1523 -0.0634 -0.0101 0.0292  131 THR   B CA  
1829 C CA  B THR   B 117 ? 0.2666 0.2052 0.1551 -0.0632 -0.0073 0.0254  131 THR   B CA  
1830 C C   . THR   B 117 ? 0.2884 0.2270 0.1629 -0.0764 -0.0052 0.0236  131 THR   B C   
1831 O O   . THR   B 117 ? 0.2796 0.2216 0.1455 -0.0752 -0.0333 0.0390  131 THR   B O   
1832 C CB  A THR   B 117 ? 0.3002 0.2075 0.2140 -0.0379 -0.0567 0.0248  131 THR   B CB  
1833 C CB  B THR   B 117 ? 0.2503 0.2092 0.1733 -0.0589 -0.0221 0.0264  131 THR   B CB  
1834 O OG1 A THR   B 117 ? 0.3166 0.2030 0.2539 0.0007  -0.0402 0.0304  131 THR   B OG1 
1835 O OG1 B THR   B 117 ? 0.2466 0.2129 0.1964 -0.0557 -0.0298 0.0265  131 THR   B OG1 
1836 C CG2 A THR   B 117 ? 0.3285 0.2170 0.2672 -0.0454 -0.0646 0.0152  131 THR   B CG2 
1837 C CG2 B THR   B 117 ? 0.2417 0.2084 0.1754 -0.0554 -0.0240 0.0284  131 THR   B CG2 
1838 N N   . LYS   B 118 ? 0.3141 0.2750 0.1463 -0.1032 -0.0371 0.0269  132 LYS   B N   
1839 C CA  . LYS   B 118 ? 0.3522 0.3091 0.1776 -0.0819 -0.0472 0.0236  132 LYS   B CA  
1840 C C   . LYS   B 118 ? 0.3892 0.3095 0.2013 -0.0876 -0.0440 0.0569  132 LYS   B C   
1841 O O   . LYS   B 118 ? 0.3786 0.3023 0.1773 -0.0645 -0.0697 0.0653  132 LYS   B O   
1842 C CB  . LYS   B 118 ? 0.3683 0.3272 0.1674 -0.0521 -0.0538 0.0234  132 LYS   B CB  
1843 C CG  . LYS   B 118 ? 0.3870 0.3432 0.1953 -0.0353 -0.0041 0.0349  132 LYS   B CG  
1844 C CD  . LYS   B 118 ? 0.3963 0.3420 0.2250 -0.0188 0.0128  0.0378  132 LYS   B CD  
1845 C CE  . LYS   B 118 ? 0.4190 0.3542 0.2984 -0.0195 0.0750  0.0129  132 LYS   B CE  
1846 N NZ  . LYS   B 118 ? 0.4129 0.3664 0.3251 -0.0264 0.1112  -0.0219 132 LYS   B NZ  
1847 N N   . VAL   B 119 ? 0.4654 0.3051 0.2412 -0.0925 -0.0329 0.1061  133 VAL   B N   
1848 C CA  . VAL   B 119 ? 0.5145 0.3274 0.3486 -0.0966 -0.0160 0.1010  133 VAL   B CA  
1849 C C   . VAL   B 119 ? 0.5326 0.3512 0.4182 -0.1021 -0.0257 0.0734  133 VAL   B C   
1850 O O   . VAL   B 119 ? 0.5622 0.3591 0.4365 -0.0971 -0.0136 0.0666  133 VAL   B O   
1851 C CB  . VAL   B 119 ? 0.5328 0.3363 0.4051 -0.0845 0.0172  0.1054  133 VAL   B CB  
1852 C CG1 . VAL   B 119 ? 0.5420 0.3377 0.4096 -0.0724 0.0171  0.1113  133 VAL   B CG1 
1853 C CG2 . VAL   B 119 ? 0.5475 0.3393 0.4489 -0.0886 0.0377  0.1094  133 VAL   B CG2 
1854 N N   . LYS   B 120 ? 0.5536 0.3718 0.4795 -0.0998 -0.0283 0.0596  134 LYS   B N   
1855 C CA  . LYS   B 120 ? 0.5723 0.3947 0.5167 -0.0844 -0.0321 0.0466  134 LYS   B CA  
1856 C C   . LYS   B 120 ? 0.5812 0.3981 0.5235 -0.0811 -0.0261 0.0516  134 LYS   B C   
1857 O O   . LYS   B 120 ? 0.5872 0.4016 0.5203 -0.0759 -0.0273 0.0533  134 LYS   B O   
1858 C CB  . LYS   B 120 ? 0.5866 0.4129 0.5487 -0.0657 -0.0389 0.0421  134 LYS   B CB  
1859 C CG  . LYS   B 120 ? 0.6041 0.4282 0.5694 -0.0537 -0.0429 0.0326  134 LYS   B CG  
1860 C CD  . LYS   B 120 ? 0.6154 0.4359 0.5735 -0.0482 -0.0521 0.0182  134 LYS   B CD  
1861 C CE  . LYS   B 120 ? 0.6176 0.4368 0.5723 -0.0398 -0.0602 0.0079  134 LYS   B CE  
1862 N NZ  . LYS   B 120 ? 0.6183 0.4387 0.5658 -0.0332 -0.0703 -0.0029 134 LYS   B NZ  
1863 N N   . GLY   C 2   ? 0.3517 0.3380 0.4149 -0.0334 0.0469  -0.0228 16  GLY   C N   
1864 C CA  . GLY   C 2   ? 0.2944 0.3178 0.3763 -0.0530 0.0413  -0.0168 16  GLY   C CA  
1865 C C   . GLY   C 2   ? 0.2354 0.2925 0.3223 -0.0666 0.0178  -0.0130 16  GLY   C C   
1866 O O   . GLY   C 2   ? 0.2495 0.2830 0.3224 -0.0965 0.0266  -0.0131 16  GLY   C O   
1867 N N   . ILE   C 3   ? 0.2108 0.2824 0.2734 -0.0441 0.0034  -0.0077 17  ILE   C N   
1868 C CA  . ILE   C 3   ? 0.2085 0.2577 0.2514 -0.0412 0.0173  -0.0026 17  ILE   C CA  
1869 C C   . ILE   C 3   ? 0.1968 0.2370 0.2207 -0.0676 0.0197  -0.0124 17  ILE   C C   
1870 O O   . ILE   C 3   ? 0.1950 0.2357 0.2066 -0.0421 0.0112  -0.0164 17  ILE   C O   
1871 C CB  . ILE   C 3   ? 0.2226 0.2601 0.2264 0.0052  0.0265  0.0079  17  ILE   C CB  
1872 C CG1 . ILE   C 3   ? 0.2492 0.2771 0.2294 0.0404  0.0101  0.0040  17  ILE   C CG1 
1873 C CG2 . ILE   C 3   ? 0.2202 0.2399 0.2214 -0.0030 0.0156  0.0208  17  ILE   C CG2 
1874 C CD1 . ILE   C 3   ? 0.2796 0.2852 0.2187 0.0588  -0.0139 0.0107  17  ILE   C CD1 
1875 N N   . THR   C 4   ? 0.2011 0.2359 0.2215 -0.0702 0.0146  -0.0185 18  THR   C N   
1876 C CA  . THR   C 4   ? 0.2210 0.2380 0.2044 -0.0680 -0.0019 -0.0209 18  THR   C CA  
1877 C C   . THR   C 4   ? 0.2158 0.2237 0.2140 -0.0677 -0.0023 0.0046  18  THR   C C   
1878 O O   . THR   C 4   ? 0.2416 0.2385 0.2462 -0.0732 0.0196  0.0030  18  THR   C O   
1879 C CB  . THR   C 4   ? 0.2530 0.2498 0.2048 -0.0831 0.0035  -0.0318 18  THR   C CB  
1880 O OG1 . THR   C 4   ? 0.2461 0.2637 0.1973 -0.1006 0.0128  -0.0187 18  THR   C OG1 
1881 C CG2 . THR   C 4   ? 0.2793 0.2498 0.2289 -0.0971 0.0023  -0.0512 18  THR   C CG2 
1882 N N   . GLY   C 5   ? 0.2196 0.2027 0.2122 -0.0719 0.0129  0.0016  19  GLY   C N   
1883 C CA  . GLY   C 5   ? 0.2443 0.1993 0.2060 -0.0711 0.0092  0.0003  19  GLY   C CA  
1884 C C   . GLY   C 5   ? 0.2490 0.1859 0.1910 -0.0695 0.0142  0.0052  19  GLY   C C   
1885 O O   . GLY   C 5   ? 0.2630 0.1844 0.1756 -0.0675 0.0329  -0.0009 19  GLY   C O   
1886 N N   . THR   C 6   ? 0.2641 0.1845 0.1909 -0.0580 0.0082  0.0008  20  THR   C N   
1887 C CA  . THR   C 6   ? 0.2698 0.1788 0.1861 -0.0474 0.0079  0.0096  20  THR   C CA  
1888 C C   . THR   C 6   ? 0.2667 0.1701 0.1954 -0.0595 0.0179  0.0038  20  THR   C C   
1889 O O   . THR   C 6   ? 0.2616 0.1875 0.2284 -0.0694 0.0285  0.0054  20  THR   C O   
1890 C CB  . THR   C 6   ? 0.2946 0.1892 0.2305 -0.0387 -0.0086 -0.0043 20  THR   C CB  
1891 O OG1 . THR   C 6   ? 0.3172 0.1861 0.2532 -0.0303 0.0122  -0.0120 20  THR   C OG1 
1892 C CG2 . THR   C 6   ? 0.2972 0.1955 0.2525 -0.0364 -0.0006 0.0128  20  THR   C CG2 
1893 N N   . TRP   C 7   ? 0.2679 0.1648 0.2011 -0.0536 0.0001  -0.0103 21  TRP   C N   
1894 C CA  . TRP   C 7   ? 0.2359 0.1558 0.1824 -0.0442 -0.0012 -0.0046 21  TRP   C CA  
1895 C C   . TRP   C 7   ? 0.2451 0.1551 0.1719 -0.0315 0.0265  0.0015  21  TRP   C C   
1896 O O   . TRP   C 7   ? 0.2544 0.1790 0.1770 -0.0383 0.0074  -0.0102 21  TRP   C O   
1897 C CB  . TRP   C 7   ? 0.2412 0.1672 0.1949 -0.0370 -0.0119 -0.0055 21  TRP   C CB  
1898 C CG  . TRP   C 7   ? 0.2369 0.1689 0.1982 -0.0521 -0.0144 -0.0052 21  TRP   C CG  
1899 C CD1 . TRP   C 7   ? 0.2300 0.1815 0.1903 -0.0487 -0.0217 -0.0039 21  TRP   C CD1 
1900 C CD2 . TRP   C 7   ? 0.2450 0.1660 0.2010 -0.0547 -0.0092 0.0026  21  TRP   C CD2 
1901 N NE1 . TRP   C 7   ? 0.2124 0.1850 0.1851 -0.0556 -0.0020 -0.0045 21  TRP   C NE1 
1902 C CE2 . TRP   C 7   ? 0.2245 0.1691 0.1959 -0.0502 -0.0100 0.0048  21  TRP   C CE2 
1903 C CE3 . TRP   C 7   ? 0.2731 0.1773 0.2130 -0.0510 -0.0134 0.0108  21  TRP   C CE3 
1904 C CZ2 . TRP   C 7   ? 0.2577 0.1733 0.2059 -0.0504 0.0008  0.0150  21  TRP   C CZ2 
1905 C CZ3 . TRP   C 7   ? 0.2858 0.1877 0.2123 -0.0383 -0.0055 0.0065  21  TRP   C CZ3 
1906 C CH2 . TRP   C 7   ? 0.2676 0.1822 0.2224 -0.0355 0.0009  0.0023  21  TRP   C CH2 
1907 N N   . TYR   C 8   ? 0.2400 0.1443 0.1717 -0.0475 0.0068  0.0039  22  TYR   C N   
1908 C CA  . TYR   C 8   ? 0.2444 0.1419 0.1706 -0.0328 0.0122  0.0145  22  TYR   C CA  
1909 C C   . TYR   C 8   ? 0.2465 0.1559 0.1751 -0.0374 -0.0067 0.0025  22  TYR   C C   
1910 O O   . TYR   C 8   ? 0.2246 0.1660 0.1657 -0.0218 -0.0006 0.0104  22  TYR   C O   
1911 C CB  . TYR   C 8   ? 0.2446 0.1422 0.2068 -0.0162 0.0057  0.0215  22  TYR   C CB  
1912 C CG  . TYR   C 8   ? 0.2593 0.1460 0.2312 -0.0214 -0.0012 0.0172  22  TYR   C CG  
1913 C CD1 . TYR   C 8   ? 0.2877 0.1535 0.2418 0.0119  -0.0120 0.0246  22  TYR   C CD1 
1914 C CD2 . TYR   C 8   ? 0.2577 0.1486 0.2523 -0.0279 -0.0048 0.0086  22  TYR   C CD2 
1915 C CE1 . TYR   C 8   ? 0.3154 0.1596 0.2772 0.0052  -0.0123 0.0187  22  TYR   C CE1 
1916 C CE2 . TYR   C 8   ? 0.2873 0.1502 0.2785 -0.0232 -0.0219 0.0084  22  TYR   C CE2 
1917 C CZ  . TYR   C 8   ? 0.3280 0.1555 0.2938 -0.0076 -0.0192 0.0113  22  TYR   C CZ  
1918 O OH  . TYR   C 8   ? 0.3761 0.1661 0.3106 -0.0149 -0.0104 0.0011  22  TYR   C OH  
1919 N N   . ASN   C 9   ? 0.2366 0.1582 0.1817 -0.0573 -0.0183 0.0193  23  ASN   C N   
1920 C CA  . ASN   C 9   ? 0.2388 0.1614 0.1753 -0.0584 -0.0034 0.0174  23  ASN   C CA  
1921 C C   . ASN   C 9   ? 0.2438 0.1637 0.1764 -0.0419 0.0115  0.0191  23  ASN   C C   
1922 O O   . ASN   C 9   ? 0.2704 0.1564 0.2001 -0.0211 0.0054  0.0378  23  ASN   C O   
1923 C CB  . ASN   C 9   ? 0.2549 0.1691 0.1652 -0.0449 -0.0067 0.0252  23  ASN   C CB  
1924 C CG  . ASN   C 9   ? 0.2715 0.1720 0.1572 -0.0513 0.0009  0.0163  23  ASN   C CG  
1925 O OD1 . ASN   C 9   ? 0.2563 0.1868 0.1586 -0.0305 -0.0098 0.0281  23  ASN   C OD1 
1926 N ND2 . ASN   C 9   ? 0.2855 0.1628 0.1900 -0.0448 0.0318  0.0184  23  ASN   C ND2 
1927 N N   . GLN   C 10  ? 0.2612 0.1811 0.1611 -0.0552 0.0094  0.0079  24  GLN   C N   
1928 C CA  . GLN   C 10  ? 0.2843 0.1896 0.1661 -0.0227 0.0025  0.0113  24  GLN   C CA  
1929 C C   . GLN   C 10  ? 0.2990 0.1944 0.1604 -0.0109 -0.0023 0.0334  24  GLN   C C   
1930 O O   . GLN   C 10  ? 0.3422 0.2089 0.1729 -0.0175 0.0093  0.0370  24  GLN   C O   
1931 C CB  . GLN   C 10  ? 0.2744 0.1818 0.1723 -0.0471 -0.0003 0.0078  24  GLN   C CB  
1932 C CG  . GLN   C 10  ? 0.2514 0.1858 0.1793 -0.0452 -0.0028 0.0141  24  GLN   C CG  
1933 C CD  . GLN   C 10  ? 0.2328 0.1914 0.1819 -0.0347 -0.0191 0.0170  24  GLN   C CD  
1934 O OE1 . GLN   C 10  ? 0.2515 0.1871 0.1888 -0.0382 -0.0224 0.0143  24  GLN   C OE1 
1935 N NE2 . GLN   C 10  ? 0.2363 0.1962 0.1883 -0.0280 -0.0045 0.0284  24  GLN   C NE2 
1936 N N   . LEU   C 11  ? 0.2644 0.1867 0.1758 -0.0050 -0.0026 0.0337  25  LEU   C N   
1937 C CA  . LEU   C 11  ? 0.2820 0.1858 0.1962 0.0147  -0.0126 0.0257  25  LEU   C CA  
1938 C C   . LEU   C 11  ? 0.3142 0.1997 0.1981 0.0377  -0.0315 0.0236  25  LEU   C C   
1939 O O   . LEU   C 11  ? 0.3352 0.2260 0.2474 0.0515  -0.0333 0.0150  25  LEU   C O   
1940 C CB  . LEU   C 11  ? 0.2904 0.1859 0.2173 -0.0014 -0.0136 0.0095  25  LEU   C CB  
1941 C CG  . LEU   C 11  ? 0.3261 0.1967 0.2505 -0.0210 0.0015  0.0069  25  LEU   C CG  
1942 C CD1 . LEU   C 11  ? 0.3242 0.1977 0.2612 -0.0304 0.0152  0.0148  25  LEU   C CD1 
1943 C CD2 . LEU   C 11  ? 0.3678 0.2067 0.2608 -0.0263 0.0071  0.0067  25  LEU   C CD2 
1944 N N   . GLY   C 12  ? 0.3205 0.1789 0.1882 0.0251  -0.0227 0.0215  26  GLY   C N   
1945 C CA  . GLY   C 12  ? 0.3761 0.1727 0.2012 0.0040  0.0080  0.0299  26  GLY   C CA  
1946 C C   . GLY   C 12  ? 0.3734 0.1749 0.1986 -0.0127 0.0076  0.0324  26  GLY   C C   
1947 O O   . GLY   C 12  ? 0.4445 0.1801 0.2085 -0.0188 0.0206  0.0141  26  GLY   C O   
1948 N N   . SER   C 13  ? 0.2978 0.1888 0.1970 -0.0241 0.0057  0.0323  27  SER   C N   
1949 C CA  . SER   C 13  ? 0.2738 0.1962 0.1867 -0.0353 0.0004  0.0199  27  SER   C CA  
1950 C C   . SER   C 13  ? 0.2354 0.1995 0.1931 -0.0289 -0.0049 -0.0036 27  SER   C C   
1951 O O   . SER   C 13  ? 0.2478 0.2300 0.2215 -0.0393 0.0217  -0.0218 27  SER   C O   
1952 C CB  . SER   C 13  ? 0.2738 0.2021 0.1943 -0.0594 -0.0045 0.0306  27  SER   C CB  
1953 O OG  . SER   C 13  ? 0.3089 0.2300 0.2339 -0.0642 -0.0279 0.0213  27  SER   C OG  
1954 N N   . THR   C 14  ? 0.2406 0.1807 0.1998 -0.0186 0.0153  0.0040  28  THR   C N   
1955 C CA  . THR   C 14  ? 0.2373 0.1659 0.2037 -0.0198 0.0054  0.0248  28  THR   C CA  
1956 C C   . THR   C 14  ? 0.2370 0.1642 0.1765 -0.0253 0.0128  0.0114  28  THR   C C   
1957 O O   . THR   C 14  ? 0.2472 0.1774 0.1921 -0.0266 0.0319  -0.0055 28  THR   C O   
1958 C CB  . THR   C 14  ? 0.2685 0.1755 0.2387 -0.0151 0.0002  0.0269  28  THR   C CB  
1959 O OG1 . THR   C 14  ? 0.2870 0.1912 0.2361 -0.0139 -0.0090 0.0426  28  THR   C OG1 
1960 C CG2 . THR   C 14  ? 0.2883 0.1692 0.2541 -0.0388 0.0007  0.0158  28  THR   C CG2 
1961 N N   . PHE   C 15  ? 0.2227 0.1511 0.1736 -0.0239 0.0007  0.0046  29  PHE   C N   
1962 C CA  . PHE   C 15  ? 0.2310 0.1505 0.1845 -0.0232 0.0154  -0.0055 29  PHE   C CA  
1963 C C   . PHE   C 15  ? 0.2405 0.1461 0.1905 -0.0154 0.0415  0.0031  29  PHE   C C   
1964 O O   . PHE   C 15  ? 0.2392 0.1505 0.2069 -0.0315 0.0350  0.0092  29  PHE   C O   
1965 C CB  . PHE   C 15  ? 0.2342 0.1533 0.1867 -0.0214 0.0301  -0.0060 29  PHE   C CB  
1966 C CG  . PHE   C 15  ? 0.2050 0.1570 0.1799 -0.0367 0.0080  -0.0083 29  PHE   C CG  
1967 C CD1 . PHE   C 15  ? 0.2091 0.1666 0.1722 -0.0189 0.0040  -0.0033 29  PHE   C CD1 
1968 C CD2 . PHE   C 15  ? 0.2048 0.1534 0.1872 -0.0137 -0.0017 0.0049  29  PHE   C CD2 
1969 C CE1 . PHE   C 15  ? 0.1859 0.1675 0.1837 -0.0240 0.0227  -0.0098 29  PHE   C CE1 
1970 C CE2 . PHE   C 15  ? 0.2129 0.1574 0.1904 -0.0236 0.0071  -0.0082 29  PHE   C CE2 
1971 C CZ  . PHE   C 15  ? 0.2036 0.1533 0.1727 -0.0353 0.0013  -0.0112 29  PHE   C CZ  
1972 N N   . ILE   C 16  ? 0.2213 0.1363 0.1848 -0.0220 0.0285  0.0090  30  ILE   C N   
1973 C CA  . ILE   C 16  ? 0.2189 0.1359 0.1976 -0.0277 0.0156  0.0022  30  ILE   C CA  
1974 C C   . ILE   C 16  ? 0.2226 0.1621 0.2044 -0.0176 0.0189  0.0087  30  ILE   C C   
1975 O O   . ILE   C 16  ? 0.2527 0.2102 0.2144 0.0017  0.0407  0.0378  30  ILE   C O   
1976 C CB  . ILE   C 16  ? 0.2639 0.1359 0.2220 -0.0078 -0.0111 0.0123  30  ILE   C CB  
1977 C CG1 . ILE   C 16  ? 0.2905 0.1498 0.2526 0.0101  0.0022  0.0106  30  ILE   C CG1 
1978 C CG2 . ILE   C 16  ? 0.2752 0.1382 0.2515 -0.0097 -0.0252 0.0106  30  ILE   C CG2 
1979 C CD1 . ILE   C 16  ? 0.3094 0.1506 0.2730 0.0020  0.0226  0.0007  30  ILE   C CD1 
1980 N N   . VAL   C 17  ? 0.2153 0.1573 0.2053 -0.0200 0.0051  0.0050  31  VAL   C N   
1981 C CA  . VAL   C 17  ? 0.2055 0.1661 0.1901 -0.0325 -0.0114 -0.0095 31  VAL   C CA  
1982 C C   . VAL   C 17  ? 0.2148 0.1761 0.1801 -0.0488 0.0099  -0.0045 31  VAL   C C   
1983 O O   . VAL   C 17  ? 0.2078 0.1802 0.2109 -0.0683 0.0051  -0.0094 31  VAL   C O   
1984 C CB  . VAL   C 17  ? 0.1973 0.1545 0.1954 -0.0256 0.0084  -0.0009 31  VAL   C CB  
1985 C CG1 . VAL   C 17  ? 0.1999 0.1613 0.2097 -0.0147 0.0259  -0.0096 31  VAL   C CG1 
1986 C CG2 . VAL   C 17  ? 0.2291 0.1595 0.1971 -0.0242 -0.0133 0.0038  31  VAL   C CG2 
1987 N N   . THR   C 18  ? 0.2353 0.1809 0.1822 -0.0463 0.0015  -0.0214 32  THR   C N   
1988 C CA  . THR   C 18  ? 0.2638 0.1962 0.2026 -0.0565 0.0131  -0.0163 32  THR   C CA  
1989 C C   . THR   C 18  ? 0.2205 0.2198 0.1708 -0.0642 0.0167  -0.0116 32  THR   C C   
1990 O O   . THR   C 18  ? 0.2139 0.2250 0.1723 -0.0472 0.0106  0.0055  32  THR   C O   
1991 C CB  . THR   C 18  ? 0.2920 0.2057 0.2474 -0.0631 -0.0123 -0.0212 32  THR   C CB  
1992 O OG1 . THR   C 18  ? 0.3288 0.2066 0.2828 -0.0456 0.0120  -0.0158 32  THR   C OG1 
1993 C CG2 . THR   C 18  ? 0.2879 0.2240 0.2727 -0.0761 -0.0227 -0.0330 32  THR   C CG2 
1994 N N   . ALA   C 19  ? 0.2235 0.2413 0.1828 -0.0557 0.0034  -0.0252 33  ALA   C N   
1995 C CA  . ALA   C 19  ? 0.2179 0.2634 0.1697 -0.0640 -0.0068 -0.0248 33  ALA   C CA  
1996 C C   . ALA   C 19  ? 0.2430 0.2729 0.1979 -0.1136 -0.0134 -0.0153 33  ALA   C C   
1997 O O   . ALA   C 19  ? 0.2514 0.2925 0.2382 -0.1412 -0.0104 0.0108  33  ALA   C O   
1998 C CB  . ALA   C 19  ? 0.2043 0.2700 0.1608 -0.0257 0.0175  -0.0199 33  ALA   C CB  
1999 N N   . GLY   C 20  ? 0.2623 0.2690 0.1761 -0.1032 -0.0109 -0.0296 34  GLY   C N   
2000 C CA  . GLY   C 20  ? 0.2957 0.2620 0.1987 -0.1223 -0.0253 -0.0374 34  GLY   C CA  
2001 C C   . GLY   C 20  ? 0.2986 0.2712 0.2091 -0.1069 -0.0625 -0.0318 34  GLY   C C   
2002 O O   . GLY   C 20  ? 0.3042 0.2798 0.2299 -0.0859 -0.0543 -0.0145 34  GLY   C O   
2003 N N   . ALA   C 21  ? 0.3356 0.2793 0.2425 -0.1049 -0.0776 -0.0170 35  ALA   C N   
2004 C CA  . ALA   C 21  ? 0.3593 0.2925 0.2914 -0.1028 -0.1088 -0.0105 35  ALA   C CA  
2005 C C   . ALA   C 21  ? 0.3805 0.3009 0.3110 -0.0982 -0.1337 -0.0003 35  ALA   C C   
2006 O O   . ALA   C 21  ? 0.4131 0.3068 0.3405 -0.0685 -0.1416 0.0054  35  ALA   C O   
2007 C CB  . ALA   C 21  ? 0.3652 0.3066 0.3115 -0.0959 -0.1154 -0.0151 35  ALA   C CB  
2008 N N   . ASP   C 22  ? 0.3567 0.2957 0.2667 -0.1310 -0.1228 0.0005  36  ASP   C N   
2009 C CA  . ASP   C 22  ? 0.3731 0.2963 0.2533 -0.1188 -0.1049 -0.0093 36  ASP   C CA  
2010 C C   . ASP   C 22  ? 0.3223 0.2933 0.2233 -0.1261 -0.0933 -0.0069 36  ASP   C C   
2011 O O   . ASP   C 22  ? 0.3915 0.2932 0.2320 -0.1442 -0.0509 0.0053  36  ASP   C O   
2012 C CB  . ASP   C 22  ? 0.4080 0.2953 0.3035 -0.1036 -0.0944 -0.0040 36  ASP   C CB  
2013 C CG  . ASP   C 22  ? 0.4300 0.2958 0.3419 -0.0764 -0.0749 0.0019  36  ASP   C CG  
2014 O OD1 . ASP   C 22  ? 0.4433 0.2919 0.3243 -0.0407 -0.1017 -0.0076 36  ASP   C OD1 
2015 O OD2 . ASP   C 22  ? 0.4353 0.3031 0.3941 -0.0865 -0.0551 0.0124  36  ASP   C OD2 
2016 N N   . GLY   C 23  ? 0.2399 0.2874 0.2049 -0.0954 -0.0540 -0.0009 37  GLY   C N   
2017 C CA  . GLY   C 23  ? 0.1820 0.2619 0.1764 -0.0504 -0.0247 -0.0254 37  GLY   C CA  
2018 C C   . GLY   C 23  ? 0.1699 0.2414 0.1407 -0.0408 -0.0024 -0.0338 37  GLY   C C   
2019 O O   . GLY   C 23  ? 0.1683 0.2522 0.1441 -0.0245 0.0004  -0.0491 37  GLY   C O   
2020 N N   . ALA   C 24  ? 0.1920 0.2214 0.1547 -0.0490 0.0202  -0.0322 38  ALA   C N   
2021 C CA  . ALA   C 24  ? 0.1793 0.2005 0.1698 -0.0363 0.0360  -0.0411 38  ALA   C CA  
2022 C C   . ALA   C 24  ? 0.1661 0.1864 0.1841 -0.0376 0.0201  -0.0359 38  ALA   C C   
2023 O O   . ALA   C 24  ? 0.1841 0.1862 0.2166 -0.0540 -0.0043 -0.0243 38  ALA   C O   
2024 C CB  . ALA   C 24  ? 0.2099 0.2119 0.2081 -0.0365 0.0487  -0.0489 38  ALA   C CB  
2025 N N   . LEU   C 25  ? 0.1641 0.1750 0.1701 -0.0286 0.0050  -0.0378 39  LEU   C N   
2026 C CA  . LEU   C 25  ? 0.1789 0.1631 0.1678 -0.0159 0.0216  -0.0366 39  LEU   C CA  
2027 C C   . LEU   C 25  ? 0.1653 0.1476 0.1656 -0.0223 0.0160  -0.0339 39  LEU   C C   
2028 O O   . LEU   C 25  ? 0.1846 0.1507 0.1843 -0.0359 0.0201  -0.0274 39  LEU   C O   
2029 C CB  . LEU   C 25  ? 0.1743 0.1544 0.1745 -0.0331 0.0262  -0.0454 39  LEU   C CB  
2030 C CG  . LEU   C 25  ? 0.1646 0.1586 0.1713 -0.0286 0.0159  -0.0498 39  LEU   C CG  
2031 C CD1 . LEU   C 25  ? 0.1656 0.1573 0.1835 -0.0248 0.0045  -0.0505 39  LEU   C CD1 
2032 C CD2 . LEU   C 25  ? 0.1704 0.1895 0.1805 -0.0368 0.0223  -0.0334 39  LEU   C CD2 
2033 N N   . THR   C 26  ? 0.1914 0.1474 0.1660 -0.0272 0.0105  -0.0340 40  THR   C N   
2034 C CA  . THR   C 26  ? 0.2055 0.1527 0.1771 -0.0400 0.0124  -0.0461 40  THR   C CA  
2035 C C   . THR   C 26  ? 0.1812 0.1508 0.1883 -0.0461 0.0084  -0.0289 40  THR   C C   
2036 O O   . THR   C 26  ? 0.1984 0.1917 0.2279 -0.0421 0.0204  -0.0002 40  THR   C O   
2037 C CB  . THR   C 26  ? 0.2597 0.1595 0.1795 -0.0462 -0.0137 -0.0406 40  THR   C CB  
2038 O OG1 . THR   C 26  ? 0.2731 0.1737 0.2071 -0.0575 -0.0201 -0.0274 40  THR   C OG1 
2039 C CG2 . THR   C 26  ? 0.2625 0.1747 0.1688 -0.0440 -0.0152 -0.0410 40  THR   C CG2 
2040 N N   . GLY   C 27  ? 0.1824 0.1546 0.2026 -0.0278 0.0246  -0.0031 41  GLY   C N   
2041 C CA  . GLY   C 27  ? 0.2112 0.1545 0.2158 -0.0183 0.0137  0.0032  41  GLY   C CA  
2042 C C   . GLY   C 27  ? 0.2037 0.1389 0.2083 -0.0086 0.0262  -0.0200 41  GLY   C C   
2043 O O   . GLY   C 27  ? 0.2076 0.1360 0.2086 -0.0070 0.0433  -0.0405 41  GLY   C O   
2044 N N   . THR   C 28  ? 0.2044 0.1308 0.2111 0.0049  0.0156  -0.0151 42  THR   C N   
2045 C CA  . THR   C 28  ? 0.2488 0.1332 0.1991 0.0056  0.0163  -0.0090 42  THR   C CA  
2046 C C   . THR   C 28  ? 0.2314 0.1399 0.1888 -0.0033 0.0273  -0.0001 42  THR   C C   
2047 O O   . THR   C 28  ? 0.2308 0.1522 0.2064 -0.0155 0.0151  0.0005  42  THR   C O   
2048 C CB  . THR   C 28  ? 0.2870 0.1379 0.2075 0.0187  0.0344  -0.0048 42  THR   C CB  
2049 O OG1 . THR   C 28  ? 0.2974 0.1384 0.2596 0.0047  0.0164  0.0094  42  THR   C OG1 
2050 C CG2 . THR   C 28  ? 0.3048 0.1510 0.2073 0.0325  0.0468  -0.0120 42  THR   C CG2 
2051 N N   . TYR   C 29  ? 0.2363 0.1323 0.1893 -0.0029 0.0163  -0.0026 43  TYR   C N   
2052 C CA  . TYR   C 29  ? 0.2212 0.1352 0.1862 0.0003  0.0195  -0.0017 43  TYR   C CA  
2053 C C   . TYR   C 29  ? 0.2305 0.1611 0.1840 0.0004  0.0322  -0.0065 43  TYR   C C   
2054 O O   . TYR   C 29  ? 0.2308 0.1843 0.2035 0.0050  0.0400  -0.0055 43  TYR   C O   
2055 C CB  . TYR   C 29  ? 0.2339 0.1220 0.1901 -0.0003 0.0365  0.0087  43  TYR   C CB  
2056 C CG  . TYR   C 29  ? 0.2246 0.1198 0.1709 -0.0143 0.0356  0.0109  43  TYR   C CG  
2057 C CD1 . TYR   C 29  ? 0.2384 0.1230 0.1800 -0.0040 0.0362  -0.0061 43  TYR   C CD1 
2058 C CD2 . TYR   C 29  ? 0.2431 0.1101 0.1996 -0.0024 0.0486  0.0148  43  TYR   C CD2 
2059 C CE1 . TYR   C 29  ? 0.2523 0.1270 0.1908 0.0018  0.0432  0.0244  43  TYR   C CE1 
2060 C CE2 . TYR   C 29  ? 0.2467 0.1198 0.1736 -0.0093 0.0286  0.0128  43  TYR   C CE2 
2061 C CZ  . TYR   C 29  ? 0.2502 0.1254 0.1771 0.0031  0.0420  0.0110  43  TYR   C CZ  
2062 O OH  . TYR   C 29  ? 0.2518 0.1272 0.1889 -0.0146 0.0415  0.0116  43  TYR   C OH  
2063 N N   . GLU   C 30  ? 0.2372 0.1841 0.1950 -0.0008 0.0028  0.0023  44  GLU   C N   
2064 C CA  A GLU   C 30  ? 0.2709 0.2081 0.2173 0.0035  0.0095  0.0008  44  GLU   C CA  
2065 C CA  B GLU   C 30  ? 0.2656 0.2154 0.2269 0.0000  0.0038  -0.0011 44  GLU   C CA  
2066 C C   . GLU   C 30  ? 0.2774 0.2363 0.2309 -0.0107 0.0061  -0.0222 44  GLU   C C   
2067 O O   . GLU   C 30  ? 0.2514 0.2588 0.2231 -0.0217 0.0407  -0.0346 44  GLU   C O   
2068 C CB  A GLU   C 30  ? 0.3041 0.2033 0.2418 0.0339  0.0095  0.0161  44  GLU   C CB  
2069 C CB  B GLU   C 30  ? 0.2821 0.2255 0.2594 0.0221  -0.0226 0.0128  44  GLU   C CB  
2070 C CG  A GLU   C 30  ? 0.3163 0.1927 0.2481 0.0546  0.0203  0.0381  44  GLU   C CG  
2071 C CG  B GLU   C 30  ? 0.2779 0.2319 0.2831 0.0371  -0.0495 0.0279  44  GLU   C CG  
2072 C CD  A GLU   C 30  ? 0.3083 0.1810 0.2567 0.0638  0.0251  0.0481  44  GLU   C CD  
2073 C CD  B GLU   C 30  ? 0.2807 0.2463 0.3166 0.0422  -0.0603 0.0301  44  GLU   C CD  
2074 O OE1 A GLU   C 30  ? 0.3342 0.1940 0.2908 0.0587  0.0453  0.0484  44  GLU   C OE1 
2075 O OE1 B GLU   C 30  ? 0.2893 0.2599 0.3367 0.0475  -0.0562 0.0425  44  GLU   C OE1 
2076 O OE2 A GLU   C 30  ? 0.2757 0.1584 0.2337 0.0512  0.0066  0.0420  44  GLU   C OE2 
2077 O OE2 B GLU   C 30  ? 0.2776 0.2526 0.3433 0.0394  -0.0586 0.0250  44  GLU   C OE2 
2078 N N   . SER   C 31  ? 0.3239 0.2445 0.2468 -0.0119 -0.0194 -0.0213 45  SER   C N   
2079 C CA  . SER   C 31  ? 0.3715 0.2611 0.2648 0.0003  -0.0333 -0.0162 45  SER   C CA  
2080 C C   . SER   C 31  ? 0.4289 0.3025 0.2796 0.0098  -0.0170 -0.0082 45  SER   C C   
2081 O O   . SER   C 31  ? 0.4392 0.3234 0.3001 0.0385  -0.0557 0.0128  45  SER   C O   
2082 C CB  . SER   C 31  ? 0.3628 0.2398 0.2718 -0.0036 -0.0405 -0.0283 45  SER   C CB  
2083 O OG  . SER   C 31  ? 0.3576 0.2393 0.2811 -0.0121 -0.0460 -0.0097 45  SER   C OG  
2084 N N   . ALA   C 32  ? 0.4846 0.3230 0.2986 -0.0034 -0.0023 0.0049  46  ALA   C N   
2085 C CA  . ALA   C 32  ? 0.5136 0.3400 0.3191 -0.0243 0.0065  0.0075  46  ALA   C CA  
2086 C C   . ALA   C 32  ? 0.5255 0.3609 0.3422 -0.0284 -0.0106 0.0105  46  ALA   C C   
2087 O O   . ALA   C 32  ? 0.6039 0.3755 0.3469 -0.0288 -0.0156 0.0192  46  ALA   C O   
2088 C CB  . ALA   C 32  ? 0.5292 0.3449 0.3375 -0.0292 0.0208  0.0113  46  ALA   C CB  
2089 N N   . VAL   C 33  ? 0.4876 0.3620 0.3540 -0.0327 -0.0091 -0.0023 47  VAL   C N   
2090 C CA  . VAL   C 33  ? 0.4467 0.3638 0.3618 -0.0345 -0.0190 -0.0220 47  VAL   C CA  
2091 C C   . VAL   C 33  ? 0.4083 0.3617 0.3224 -0.0156 -0.0409 -0.0132 47  VAL   C C   
2092 O O   . VAL   C 33  ? 0.3864 0.3591 0.3072 0.0053  -0.0564 -0.0001 47  VAL   C O   
2093 C CB  . VAL   C 33  ? 0.4452 0.3658 0.3911 -0.0415 -0.0212 -0.0460 47  VAL   C CB  
2094 C CG1 . VAL   C 33  ? 0.4542 0.3644 0.4055 -0.0540 -0.0137 -0.0585 47  VAL   C CG1 
2095 C CG2 . VAL   C 33  ? 0.4225 0.3668 0.4075 -0.0319 -0.0404 -0.0537 47  VAL   C CG2 
2096 N N   . GLY   C 34  ? 0.3719 0.3607 0.3163 -0.0095 -0.0494 -0.0185 48  GLY   C N   
2097 C CA  . GLY   C 34  ? 0.3834 0.3678 0.3323 -0.0058 -0.0328 -0.0265 48  GLY   C CA  
2098 C C   . GLY   C 34  ? 0.4159 0.3740 0.3502 -0.0103 -0.0423 -0.0313 48  GLY   C C   
2099 O O   . GLY   C 34  ? 0.4118 0.3746 0.3496 0.0018  -0.0679 -0.0302 48  GLY   C O   
2100 N N   . ASN   C 35  ? 0.4388 0.3759 0.3607 -0.0269 -0.0331 -0.0366 49  ASN   C N   
2101 C CA  . ASN   C 35  ? 0.4532 0.3732 0.3743 -0.0213 -0.0354 -0.0397 49  ASN   C CA  
2102 C C   . ASN   C 35  ? 0.4650 0.3614 0.3731 -0.0103 -0.0346 -0.0202 49  ASN   C C   
2103 O O   . ASN   C 35  ? 0.4961 0.3611 0.3706 -0.0134 -0.0147 -0.0144 49  ASN   C O   
2104 C CB  . ASN   C 35  ? 0.4698 0.3850 0.3840 -0.0187 -0.0360 -0.0483 49  ASN   C CB  
2105 C CG  . ASN   C 35  ? 0.4869 0.4002 0.3933 -0.0158 -0.0504 -0.0484 49  ASN   C CG  
2106 O OD1 . ASN   C 35  ? 0.4941 0.4082 0.4216 -0.0194 -0.0518 -0.0543 49  ASN   C OD1 
2107 N ND2 . ASN   C 35  ? 0.4842 0.4022 0.3789 -0.0061 -0.0725 -0.0465 49  ASN   C ND2 
2108 N N   . ALA   C 36  ? 0.4493 0.3477 0.3653 0.0063  -0.0649 -0.0054 50  ALA   C N   
2109 C CA  . ALA   C 36  ? 0.4106 0.3369 0.3570 0.0235  -0.1048 -0.0044 50  ALA   C CA  
2110 C C   . ALA   C 36  ? 0.4201 0.3345 0.3651 0.0424  -0.1017 0.0031  50  ALA   C C   
2111 O O   . ALA   C 36  ? 0.4391 0.3338 0.3576 0.0575  -0.0880 0.0171  50  ALA   C O   
2112 C CB  . ALA   C 36  ? 0.3561 0.3255 0.3333 0.0262  -0.1478 -0.0127 50  ALA   C CB  
2113 N N   . GLU   C 37  ? 0.4246 0.3283 0.3783 0.0588  -0.0976 0.0137  51  GLU   C N   
2114 C CA  . GLU   C 37  ? 0.4334 0.3260 0.3706 0.0595  -0.1164 0.0167  51  GLU   C CA  
2115 C C   . GLU   C 37  ? 0.4532 0.3078 0.3278 0.0530  -0.1185 0.0267  51  GLU   C C   
2116 O O   . GLU   C 37  ? 0.4751 0.2988 0.3127 0.0577  -0.0981 0.0264  51  GLU   C O   
2117 C CB  . GLU   C 37  ? 0.4416 0.3436 0.4027 0.0629  -0.1082 0.0083  51  GLU   C CB  
2118 C CG  . GLU   C 37  ? 0.4362 0.3531 0.4202 0.0579  -0.0922 -0.0001 51  GLU   C CG  
2119 C CD  . GLU   C 37  ? 0.4320 0.3565 0.4315 0.0605  -0.0736 0.0009  51  GLU   C CD  
2120 O OE1 . GLU   C 37  ? 0.4317 0.3569 0.4407 0.0763  -0.0568 0.0045  51  GLU   C OE1 
2121 O OE2 . GLU   C 37  ? 0.4305 0.3559 0.4294 0.0512  -0.0731 -0.0007 51  GLU   C OE2 
2122 N N   . SER   C 38  ? 0.4518 0.2999 0.3317 0.0436  -0.1064 0.0301  52  SER   C N   
2123 C CA  . SER   C 38  ? 0.4618 0.2909 0.3616 0.0488  -0.0689 0.0403  52  SER   C CA  
2124 C C   . SER   C 38  ? 0.4297 0.2760 0.3481 0.0469  -0.0547 0.0731  52  SER   C C   
2125 O O   . SER   C 38  ? 0.4340 0.2744 0.3680 0.0060  -0.0580 0.1316  52  SER   C O   
2126 C CB  . SER   C 38  ? 0.4854 0.3109 0.3962 0.0519  -0.0615 0.0097  52  SER   C CB  
2127 O OG  . SER   C 38  ? 0.4964 0.3277 0.4160 0.0542  -0.0765 -0.0166 52  SER   C OG  
2128 N N   . ARG   C 39  ? 0.4061 0.2648 0.3162 0.0766  -0.0070 0.0749  53  ARG   C N   
2129 C CA  . ARG   C 39  ? 0.3754 0.2407 0.3096 0.0577  0.0325  0.0383  53  ARG   C CA  
2130 C C   . ARG   C 39  ? 0.3103 0.1913 0.2581 0.0744  0.0546  0.0167  53  ARG   C C   
2131 O O   . ARG   C 39  ? 0.2965 0.1763 0.2866 0.1027  0.0608  0.0238  53  ARG   C O   
2132 C CB  . ARG   C 39  ? 0.4026 0.2471 0.3362 0.0187  0.0397  0.0282  53  ARG   C CB  
2133 C CG  . ARG   C 39  ? 0.4418 0.2763 0.3857 -0.0081 0.0322  0.0213  53  ARG   C CG  
2134 C CD  . ARG   C 39  ? 0.4670 0.2879 0.4221 -0.0334 0.0304  0.0143  53  ARG   C CD  
2135 N NE  . ARG   C 39  ? 0.4853 0.3018 0.4445 -0.0442 0.0199  0.0088  53  ARG   C NE  
2136 C CZ  . ARG   C 39  ? 0.4717 0.3103 0.4459 -0.0541 0.0111  -0.0036 53  ARG   C CZ  
2137 N NH1 . ARG   C 39  ? 0.4747 0.3147 0.4614 -0.0551 0.0189  -0.0183 53  ARG   C NH1 
2138 N NH2 . ARG   C 39  ? 0.4658 0.3080 0.4335 -0.0571 0.0056  -0.0016 53  ARG   C NH2 
2139 N N   . TYR   C 40  ? 0.2561 0.1540 0.2362 0.0429  0.0206  -0.0021 54  TYR   C N   
2140 C CA  . TYR   C 40  ? 0.2164 0.1424 0.1920 0.0219  0.0321  -0.0107 54  TYR   C CA  
2141 C C   . TYR   C 40  ? 0.2002 0.1422 0.1935 0.0160  0.0461  -0.0155 54  TYR   C C   
2142 O O   . TYR   C 40  ? 0.2178 0.1583 0.2033 -0.0039 0.0499  -0.0059 54  TYR   C O   
2143 C CB  . TYR   C 40  ? 0.2104 0.1348 0.1826 0.0221  0.0449  -0.0122 54  TYR   C CB  
2144 C CG  . TYR   C 40  ? 0.2150 0.1367 0.1839 0.0250  0.0079  -0.0130 54  TYR   C CG  
2145 C CD1 . TYR   C 40  ? 0.2361 0.1392 0.2021 0.0302  0.0149  -0.0195 54  TYR   C CD1 
2146 C CD2 . TYR   C 40  ? 0.2026 0.1305 0.1916 0.0295  0.0088  -0.0215 54  TYR   C CD2 
2147 C CE1 . TYR   C 40  ? 0.2395 0.1458 0.2219 0.0517  -0.0033 0.0030  54  TYR   C CE1 
2148 C CE2 . TYR   C 40  ? 0.2267 0.1334 0.1975 0.0358  -0.0115 -0.0146 54  TYR   C CE2 
2149 C CZ  . TYR   C 40  ? 0.2394 0.1553 0.2190 0.0433  -0.0326 -0.0011 54  TYR   C CZ  
2150 O OH  . TYR   C 40  ? 0.2746 0.1916 0.2469 0.0395  -0.0514 0.0086  54  TYR   C OH  
2151 N N   . VAL   C 41  ? 0.1896 0.1364 0.1983 0.0228  0.0237  -0.0217 55  VAL   C N   
2152 C CA  . VAL   C 41  ? 0.1816 0.1321 0.1998 0.0180  0.0395  -0.0326 55  VAL   C CA  
2153 C C   . VAL   C 41  ? 0.1555 0.1256 0.1859 0.0043  0.0344  -0.0300 55  VAL   C C   
2154 O O   . VAL   C 41  ? 0.1694 0.1235 0.1811 0.0071  0.0311  -0.0198 55  VAL   C O   
2155 C CB  . VAL   C 41  ? 0.2030 0.1496 0.2031 0.0127  0.0436  -0.0373 55  VAL   C CB  
2156 C CG1 . VAL   C 41  ? 0.1773 0.1430 0.1926 0.0065  0.0239  -0.0226 55  VAL   C CG1 
2157 C CG2 . VAL   C 41  ? 0.2270 0.1570 0.2332 0.0233  0.0564  -0.0588 55  VAL   C CG2 
2158 N N   . LEU   C 42  ? 0.1666 0.1233 0.1953 0.0005  0.0257  -0.0273 56  LEU   C N   
2159 C CA  . LEU   C 42  ? 0.1694 0.1308 0.1775 0.0040  0.0135  -0.0390 56  LEU   C CA  
2160 C C   . LEU   C 42  ? 0.1725 0.1311 0.1917 -0.0097 0.0130  -0.0324 56  LEU   C C   
2161 O O   . LEU   C 42  ? 0.1758 0.1416 0.1841 -0.0210 0.0010  -0.0419 56  LEU   C O   
2162 C CB  . LEU   C 42  ? 0.1884 0.1358 0.1771 -0.0127 0.0240  -0.0394 56  LEU   C CB  
2163 C CG  . LEU   C 42  ? 0.1982 0.1373 0.1920 -0.0063 0.0207  -0.0113 56  LEU   C CG  
2164 C CD1 . LEU   C 42  ? 0.1532 0.1519 0.1957 -0.0029 0.0153  -0.0121 56  LEU   C CD1 
2165 C CD2 . LEU   C 42  ? 0.2634 0.1439 0.2050 -0.0006 0.0236  0.0074  56  LEU   C CD2 
2166 N N   . THR   C 43  ? 0.1626 0.1312 0.1933 -0.0118 0.0260  -0.0296 57  THR   C N   
2167 C CA  A THR   C 43  ? 0.1718 0.1346 0.1642 -0.0108 0.0211  -0.0284 57  THR   C CA  
2168 C CA  B THR   C 43  ? 0.1707 0.1359 0.1470 -0.0139 0.0408  -0.0279 57  THR   C CA  
2169 C C   . THR   C 43  ? 0.1612 0.1372 0.1455 -0.0179 0.0049  -0.0350 57  THR   C C   
2170 O O   . THR   C 43  ? 0.1626 0.1231 0.1312 -0.0197 0.0006  -0.0209 57  THR   C O   
2171 C CB  A THR   C 43  ? 0.1996 0.1367 0.1668 -0.0060 0.0250  -0.0275 57  THR   C CB  
2172 C CB  B THR   C 43  ? 0.2241 0.1469 0.1825 -0.0081 0.0795  -0.0352 57  THR   C CB  
2173 O OG1 A THR   C 43  ? 0.2152 0.1400 0.1638 0.0048  0.0216  -0.0171 57  THR   C OG1 
2174 O OG1 B THR   C 43  ? 0.2329 0.1787 0.1902 -0.0177 0.0459  -0.0267 57  THR   C OG1 
2175 C CG2 A THR   C 43  ? 0.2077 0.1406 0.1664 -0.0124 0.0136  -0.0307 57  THR   C CG2 
2176 C CG2 B THR   C 43  ? 0.2767 0.1440 0.1968 0.0119  0.1096  -0.0385 57  THR   C CG2 
2177 N N   . GLY   C 44  ? 0.1426 0.1532 0.1536 -0.0188 -0.0050 -0.0368 58  GLY   C N   
2178 C CA  . GLY   C 44  ? 0.1373 0.1485 0.1603 -0.0068 -0.0007 -0.0388 58  GLY   C CA  
2179 C C   . GLY   C 44  ? 0.1326 0.1593 0.1291 -0.0174 0.0022  -0.0303 58  GLY   C C   
2180 O O   . GLY   C 44  ? 0.1408 0.1512 0.1360 -0.0265 0.0088  -0.0305 58  GLY   C O   
2181 N N   . ARG   C 45  ? 0.1329 0.1689 0.1384 -0.0106 0.0073  -0.0345 59  ARG   C N   
2182 C CA  . ARG   C 45  ? 0.1440 0.1835 0.1346 -0.0136 0.0050  -0.0219 59  ARG   C CA  
2183 C C   . ARG   C 45  ? 0.1398 0.1975 0.1259 -0.0271 0.0003  -0.0358 59  ARG   C C   
2184 O O   . ARG   C 45  ? 0.1506 0.1928 0.1312 -0.0160 -0.0038 -0.0430 59  ARG   C O   
2185 C CB  . ARG   C 45  ? 0.1604 0.1844 0.1354 -0.0087 0.0098  -0.0386 59  ARG   C CB  
2186 C CG  . ARG   C 45  ? 0.1729 0.1995 0.1261 -0.0055 -0.0079 -0.0293 59  ARG   C CG  
2187 C CD  . ARG   C 45  ? 0.1711 0.2081 0.1294 -0.0001 0.0034  -0.0216 59  ARG   C CD  
2188 N NE  . ARG   C 45  ? 0.1430 0.2041 0.1352 -0.0179 0.0060  -0.0224 59  ARG   C NE  
2189 C CZ  . ARG   C 45  ? 0.1599 0.1957 0.1503 0.0068  0.0045  -0.0118 59  ARG   C CZ  
2190 N NH1 . ARG   C 45  ? 0.1708 0.1985 0.1712 0.0114  0.0012  -0.0201 59  ARG   C NH1 
2191 N NH2 . ARG   C 45  ? 0.1642 0.2057 0.1729 0.0065  -0.0073 -0.0150 59  ARG   C NH2 
2192 N N   . TYR   C 46  ? 0.1467 0.2097 0.1309 -0.0231 0.0078  -0.0279 60  TYR   C N   
2193 C CA  . TYR   C 46  ? 0.1314 0.2180 0.1385 -0.0054 0.0134  -0.0195 60  TYR   C CA  
2194 C C   . TYR   C 46  ? 0.1143 0.2233 0.1341 -0.0246 0.0011  -0.0125 60  TYR   C C   
2195 O O   . TYR   C 46  ? 0.1491 0.2322 0.1334 -0.0256 -0.0118 -0.0123 60  TYR   C O   
2196 C CB  . TYR   C 46  ? 0.1558 0.2087 0.1619 -0.0217 0.0051  -0.0181 60  TYR   C CB  
2197 C CG  . TYR   C 46  ? 0.1550 0.1978 0.1780 -0.0280 -0.0210 -0.0103 60  TYR   C CG  
2198 C CD1 . TYR   C 46  ? 0.2028 0.1936 0.1804 -0.0503 -0.0285 -0.0248 60  TYR   C CD1 
2199 C CD2 . TYR   C 46  ? 0.1804 0.1988 0.2071 -0.0290 -0.0145 -0.0053 60  TYR   C CD2 
2200 C CE1 . TYR   C 46  ? 0.2070 0.2056 0.2018 -0.0595 -0.0488 -0.0162 60  TYR   C CE1 
2201 C CE2 . TYR   C 46  ? 0.2142 0.2038 0.2248 -0.0463 -0.0289 -0.0080 60  TYR   C CE2 
2202 C CZ  . TYR   C 46  ? 0.2064 0.2075 0.2205 -0.0665 -0.0653 -0.0154 60  TYR   C CZ  
2203 O OH  . TYR   C 46  ? 0.2501 0.2233 0.2781 -0.0593 -0.0613 -0.0228 60  TYR   C OH  
2204 N N   . ASP   C 47  ? 0.1205 0.2168 0.1578 -0.0254 0.0112  -0.0199 61  ASP   C N   
2205 C CA  . ASP   C 47  ? 0.1236 0.2208 0.1702 -0.0165 0.0011  -0.0411 61  ASP   C CA  
2206 C C   . ASP   C 47  ? 0.1284 0.2255 0.1657 -0.0359 -0.0074 -0.0355 61  ASP   C C   
2207 O O   . ASP   C 47  ? 0.1653 0.2239 0.1772 -0.0501 -0.0044 -0.0290 61  ASP   C O   
2208 C CB  . ASP   C 47  ? 0.1058 0.2225 0.1622 0.0053  0.0039  -0.0268 61  ASP   C CB  
2209 C CG  . ASP   C 47  ? 0.1215 0.2275 0.1620 -0.0063 -0.0074 -0.0289 61  ASP   C CG  
2210 O OD1 . ASP   C 47  ? 0.1397 0.2372 0.1816 -0.0218 -0.0305 -0.0156 61  ASP   C OD1 
2211 O OD2 . ASP   C 47  ? 0.1231 0.2200 0.1746 0.0016  0.0145  -0.0297 61  ASP   C OD2 
2212 N N   . SER   C 48  ? 0.1270 0.2310 0.1891 -0.0368 -0.0117 -0.0418 62  SER   C N   
2213 C CA  . SER   C 48  ? 0.1612 0.2469 0.1843 -0.0394 0.0036  -0.0394 62  SER   C CA  
2214 C C   . SER   C 48  ? 0.1598 0.2578 0.2021 -0.0443 0.0068  -0.0481 62  SER   C C   
2215 O O   . SER   C 48  ? 0.1662 0.2638 0.2353 -0.0661 0.0143  -0.0725 62  SER   C O   
2216 C CB  . SER   C 48  ? 0.2207 0.2572 0.2036 -0.0339 -0.0099 -0.0288 62  SER   C CB  
2217 O OG  . SER   C 48  ? 0.2653 0.2691 0.2244 -0.0159 0.0173  -0.0201 62  SER   C OG  
2218 N N   . ALA   C 49  ? 0.1424 0.2734 0.1860 -0.0229 0.0024  -0.0348 63  ALA   C N   
2219 C CA  . ALA   C 49  ? 0.1469 0.2822 0.2090 -0.0137 -0.0111 -0.0301 63  ALA   C CA  
2220 C C   . ALA   C 49  ? 0.1263 0.2743 0.2145 -0.0109 -0.0118 -0.0199 63  ALA   C C   
2221 O O   . ALA   C 49  ? 0.1535 0.2705 0.1979 -0.0295 -0.0110 -0.0238 63  ALA   C O   
2222 C CB  . ALA   C 49  ? 0.1731 0.2929 0.2320 -0.0239 -0.0283 -0.0259 63  ALA   C CB  
2223 N N   . PRO   C 50  ? 0.1504 0.2716 0.2001 -0.0158 0.0091  -0.0327 64  PRO   C N   
2224 C CA  . PRO   C 50  ? 0.1496 0.2674 0.1872 -0.0093 0.0040  -0.0271 64  PRO   C CA  
2225 C C   . PRO   C 50  ? 0.1709 0.2798 0.1932 -0.0351 0.0100  -0.0288 64  PRO   C C   
2226 O O   . PRO   C 50  ? 0.1739 0.2812 0.2097 -0.0454 0.0064  -0.0049 64  PRO   C O   
2227 C CB  . PRO   C 50  ? 0.1688 0.2537 0.1984 0.0039  0.0023  -0.0353 64  PRO   C CB  
2228 C CG  . PRO   C 50  ? 0.2034 0.2626 0.2168 -0.0062 0.0137  -0.0411 64  PRO   C CG  
2229 C CD  . PRO   C 50  ? 0.1980 0.2661 0.2015 0.0033  0.0165  -0.0331 64  PRO   C CD  
2230 N N   . ALA   C 51  ? 0.1540 0.2943 0.1885 -0.0255 0.0112  -0.0259 65  ALA   C N   
2231 C CA  . ALA   C 51  ? 0.1476 0.3123 0.2024 -0.0119 0.0187  -0.0101 65  ALA   C CA  
2232 C C   . ALA   C 51  ? 0.1852 0.3351 0.2009 -0.0154 0.0187  -0.0025 65  ALA   C C   
2233 O O   . ALA   C 51  ? 0.1737 0.3398 0.2226 -0.0230 0.0286  0.0102  65  ALA   C O   
2234 C CB  . ALA   C 51  ? 0.1550 0.3085 0.2148 -0.0002 0.0110  -0.0211 65  ALA   C CB  
2235 N N   . THR   C 52  ? 0.1994 0.3633 0.1910 -0.0137 0.0340  -0.0059 66  THR   C N   
2236 C CA  . THR   C 52  ? 0.1921 0.3816 0.1969 -0.0179 0.0279  -0.0019 66  THR   C CA  
2237 C C   . THR   C 52  ? 0.1918 0.4035 0.2012 -0.0296 0.0433  0.0013  66  THR   C C   
2238 O O   . THR   C 52  ? 0.2201 0.4185 0.2381 -0.0431 0.0700  0.0104  66  THR   C O   
2239 C CB  . THR   C 52  ? 0.2102 0.3793 0.2368 -0.0062 0.0217  0.0018  66  THR   C CB  
2240 O OG1 . THR   C 52  ? 0.1968 0.3797 0.2514 -0.0042 -0.0056 0.0085  66  THR   C OG1 
2241 C CG2 . THR   C 52  ? 0.2228 0.3823 0.2593 -0.0021 0.0287  0.0006  66  THR   C CG2 
2242 N N   . ASP   C 53  ? 0.1930 0.4100 0.2013 -0.0207 0.0203  -0.0078 67  ASP   C N   
2243 C CA  . ASP   C 53  ? 0.2210 0.4133 0.2435 -0.0054 0.0456  -0.0139 67  ASP   C CA  
2244 C C   . ASP   C 53  ? 0.2268 0.4206 0.2318 -0.0053 0.0343  -0.0200 67  ASP   C C   
2245 O O   . ASP   C 53  ? 0.2935 0.4404 0.2544 0.0028  0.0339  -0.0225 67  ASP   C O   
2246 C CB  . ASP   C 53  ? 0.2457 0.4013 0.2839 0.0104  0.0692  -0.0170 67  ASP   C CB  
2247 C CG  . ASP   C 53  ? 0.2936 0.3949 0.3312 0.0181  0.0450  -0.0272 67  ASP   C CG  
2248 O OD1 . ASP   C 53  ? 0.2548 0.3872 0.2596 0.0271  0.0397  -0.0475 67  ASP   C OD1 
2249 O OD2 . ASP   C 53  ? 0.3492 0.3992 0.4141 0.0139  0.0590  -0.0130 67  ASP   C OD2 
2250 N N   . GLY   C 54  ? 0.1884 0.4064 0.2375 -0.0337 0.0321  -0.0058 68  GLY   C N   
2251 C CA  . GLY   C 54  ? 0.1797 0.3901 0.2290 -0.0488 0.0288  -0.0093 68  GLY   C CA  
2252 C C   . GLY   C 54  ? 0.1795 0.3678 0.2425 -0.0355 0.0255  -0.0196 68  GLY   C C   
2253 O O   . GLY   C 54  ? 0.2162 0.3754 0.2596 -0.0400 0.0235  -0.0181 68  GLY   C O   
2254 N N   . SER   C 55  ? 0.1587 0.3436 0.2394 -0.0365 0.0591  -0.0364 69  SER   C N   
2255 C CA  . SER   C 55  ? 0.1607 0.3215 0.2398 -0.0387 0.0546  -0.0385 69  SER   C CA  
2256 C C   . SER   C 55  ? 0.1563 0.2936 0.2156 -0.0513 0.0505  -0.0506 69  SER   C C   
2257 O O   . SER   C 55  ? 0.1568 0.2892 0.2182 -0.0532 0.0269  -0.0464 69  SER   C O   
2258 C CB  . SER   C 55  ? 0.2187 0.3312 0.2954 -0.0293 0.0959  -0.0373 69  SER   C CB  
2259 O OG  . SER   C 55  ? 0.3117 0.3507 0.3217 -0.0419 0.0730  -0.0451 69  SER   C OG  
2260 N N   . GLY   C 56  ? 0.1598 0.2786 0.1839 -0.0317 0.0506  -0.0410 70  GLY   C N   
2261 C CA  . GLY   C 56  ? 0.1440 0.2622 0.1694 -0.0199 0.0262  -0.0435 70  GLY   C CA  
2262 C C   . GLY   C 56  ? 0.1287 0.2528 0.1618 -0.0385 0.0171  -0.0203 70  GLY   C C   
2263 O O   . GLY   C 56  ? 0.1485 0.2597 0.1710 -0.0377 0.0194  -0.0086 70  GLY   C O   
2264 N N   . THR   C 57  ? 0.1498 0.2405 0.1529 -0.0346 0.0333  -0.0152 71  THR   C N   
2265 C CA  . THR   C 57  ? 0.1388 0.2168 0.1438 -0.0403 0.0283  -0.0178 71  THR   C CA  
2266 C C   . THR   C 57  ? 0.1276 0.2107 0.1388 -0.0355 0.0145  -0.0098 71  THR   C C   
2267 O O   . THR   C 57  ? 0.1277 0.2141 0.1580 -0.0139 0.0013  -0.0156 71  THR   C O   
2268 C CB  . THR   C 57  ? 0.1565 0.2148 0.1712 -0.0510 0.0167  -0.0183 71  THR   C CB  
2269 O OG1 . THR   C 57  ? 0.1673 0.2317 0.1845 -0.0484 -0.0001 -0.0118 71  THR   C OG1 
2270 C CG2 . THR   C 57  ? 0.1921 0.2065 0.1740 -0.0369 0.0267  -0.0180 71  THR   C CG2 
2271 N N   . ALA   C 58  ? 0.1379 0.2065 0.1469 -0.0290 0.0151  -0.0100 72  ALA   C N   
2272 C CA  . ALA   C 58  ? 0.1380 0.1884 0.1439 -0.0274 0.0197  -0.0028 72  ALA   C CA  
2273 C C   . ALA   C 58  ? 0.1405 0.1886 0.1402 -0.0291 0.0154  -0.0303 72  ALA   C C   
2274 O O   . ALA   C 58  ? 0.1385 0.1910 0.1468 -0.0183 -0.0065 -0.0292 72  ALA   C O   
2275 C CB  . ALA   C 58  ? 0.1433 0.1835 0.1441 -0.0203 0.0059  0.0043  72  ALA   C CB  
2276 N N   . LEU   C 59  ? 0.1201 0.1862 0.1287 -0.0173 0.0115  -0.0169 73  LEU   C N   
2277 C CA  A LEU   C 59  ? 0.1261 0.1842 0.1258 -0.0246 0.0143  -0.0205 73  LEU   C CA  
2278 C CA  B LEU   C 59  ? 0.1269 0.1790 0.1318 -0.0164 0.0192  -0.0199 73  LEU   C CA  
2279 C C   . LEU   C 59  ? 0.1269 0.1715 0.1177 -0.0143 0.0103  -0.0243 73  LEU   C C   
2280 O O   . LEU   C 59  ? 0.1372 0.1778 0.1335 -0.0195 0.0050  -0.0348 73  LEU   C O   
2281 C CB  A LEU   C 59  ? 0.1444 0.1934 0.1298 -0.0321 0.0057  -0.0029 73  LEU   C CB  
2282 C CB  B LEU   C 59  ? 0.1537 0.1779 0.1468 -0.0073 0.0174  0.0014  73  LEU   C CB  
2283 C CG  A LEU   C 59  ? 0.1690 0.2019 0.1434 -0.0539 0.0172  -0.0022 73  LEU   C CG  
2284 C CG  B LEU   C 59  ? 0.1820 0.1784 0.1765 -0.0183 0.0403  0.0082  73  LEU   C CG  
2285 C CD1 A LEU   C 59  ? 0.1793 0.2088 0.1476 -0.0415 -0.0082 0.0096  73  LEU   C CD1 
2286 C CD1 B LEU   C 59  ? 0.1956 0.1789 0.1882 -0.0458 0.0358  0.0128  73  LEU   C CD1 
2287 C CD2 A LEU   C 59  ? 0.1757 0.2007 0.1520 -0.0694 0.0277  0.0022  73  LEU   C CD2 
2288 C CD2 B LEU   C 59  ? 0.1842 0.1822 0.1897 0.0072  0.0611  0.0085  73  LEU   C CD2 
2289 N N   . GLY   C 60  ? 0.1217 0.1523 0.1250 0.0015  0.0026  -0.0156 74  GLY   C N   
2290 C CA  . GLY   C 60  ? 0.1142 0.1493 0.1308 0.0016  -0.0085 -0.0192 74  GLY   C CA  
2291 C C   . GLY   C 60  ? 0.1192 0.1383 0.1299 -0.0036 0.0164  -0.0101 74  GLY   C C   
2292 O O   . GLY   C 60  ? 0.1334 0.1411 0.1199 -0.0138 0.0005  -0.0162 74  GLY   C O   
2293 N N   . TRP   C 61  ? 0.1308 0.1239 0.1441 -0.0040 0.0125  0.0000  75  TRP   C N   
2294 C CA  . TRP   C 61  ? 0.1214 0.1153 0.1326 0.0006  0.0137  -0.0054 75  TRP   C CA  
2295 C C   . TRP   C 61  ? 0.1335 0.1074 0.1074 0.0011  -0.0088 -0.0223 75  TRP   C C   
2296 O O   . TRP   C 61  ? 0.1380 0.1126 0.1160 -0.0046 0.0083  -0.0082 75  TRP   C O   
2297 C CB  . TRP   C 61  ? 0.1431 0.1149 0.1207 -0.0008 0.0063  -0.0129 75  TRP   C CB  
2298 C CG  . TRP   C 61  ? 0.1594 0.1210 0.1349 -0.0180 0.0025  -0.0152 75  TRP   C CG  
2299 C CD1 . TRP   C 61  ? 0.1624 0.1225 0.1375 -0.0180 0.0128  0.0006  75  TRP   C CD1 
2300 C CD2 . TRP   C 61  ? 0.1833 0.1318 0.1242 -0.0260 0.0054  -0.0125 75  TRP   C CD2 
2301 N NE1 . TRP   C 61  ? 0.2020 0.1361 0.1372 -0.0162 0.0107  0.0032  75  TRP   C NE1 
2302 C CE2 . TRP   C 61  ? 0.2030 0.1299 0.1265 -0.0239 0.0143  -0.0033 75  TRP   C CE2 
2303 C CE3 . TRP   C 61  ? 0.2021 0.1433 0.1326 -0.0238 0.0225  -0.0052 75  TRP   C CE3 
2304 C CZ2 . TRP   C 61  ? 0.2163 0.1289 0.1514 -0.0430 0.0073  -0.0127 75  TRP   C CZ2 
2305 C CZ3 . TRP   C 61  ? 0.2338 0.1287 0.1465 -0.0171 0.0165  0.0026  75  TRP   C CZ3 
2306 C CH2 . TRP   C 61  ? 0.2218 0.1291 0.1504 -0.0324 0.0234  -0.0152 75  TRP   C CH2 
2307 N N   . THR   C 62  ? 0.1289 0.1141 0.1112 0.0036  0.0069  -0.0129 76  THR   C N   
2308 C CA  . THR   C 62  ? 0.1174 0.1069 0.1196 0.0072  0.0094  -0.0077 76  THR   C CA  
2309 C C   . THR   C 62  ? 0.1423 0.1061 0.1286 -0.0025 0.0010  -0.0225 76  THR   C C   
2310 O O   . THR   C 62  ? 0.1515 0.1079 0.1386 -0.0095 0.0096  -0.0228 76  THR   C O   
2311 C CB  . THR   C 62  ? 0.1468 0.1143 0.1260 0.0038  0.0105  -0.0062 76  THR   C CB  
2312 O OG1 . THR   C 62  ? 0.1460 0.1091 0.1372 0.0159  0.0174  0.0103  76  THR   C OG1 
2313 C CG2 . THR   C 62  ? 0.1237 0.1298 0.1373 0.0032  0.0090  -0.0081 76  THR   C CG2 
2314 N N   . VAL   C 63  ? 0.1436 0.1076 0.1298 0.0135  0.0207  -0.0050 77  VAL   C N   
2315 C CA  . VAL   C 63  ? 0.1579 0.1109 0.1330 0.0189  0.0086  0.0033  77  VAL   C CA  
2316 C C   . VAL   C 63  ? 0.1677 0.1190 0.1261 0.0143  0.0069  -0.0200 77  VAL   C C   
2317 O O   . VAL   C 63  ? 0.1534 0.1324 0.1357 0.0223  -0.0086 -0.0356 77  VAL   C O   
2318 C CB  . VAL   C 63  ? 0.1818 0.1177 0.1590 0.0192  0.0066  0.0012  77  VAL   C CB  
2319 C CG1 . VAL   C 63  ? 0.1858 0.1302 0.1757 0.0283  -0.0050 0.0050  77  VAL   C CG1 
2320 C CG2 . VAL   C 63  ? 0.2039 0.1239 0.1554 -0.0035 -0.0072 -0.0109 77  VAL   C CG2 
2321 N N   . ALA   C 64  ? 0.1485 0.1177 0.1304 0.0087  0.0008  -0.0092 78  ALA   C N   
2322 C CA  . ALA   C 64  ? 0.1457 0.1217 0.1400 0.0220  0.0051  0.0018  78  ALA   C CA  
2323 C C   . ALA   C 64  ? 0.1395 0.1212 0.1397 0.0227  -0.0059 -0.0068 78  ALA   C C   
2324 O O   . ALA   C 64  ? 0.1651 0.1111 0.1669 0.0198  0.0114  -0.0115 78  ALA   C O   
2325 C CB  . ALA   C 64  ? 0.1693 0.1392 0.1379 0.0104  0.0184  -0.0030 78  ALA   C CB  
2326 N N   . TRP   C 65  ? 0.1602 0.1355 0.1518 0.0276  -0.0122 -0.0055 79  TRP   C N   
2327 C CA  . TRP   C 65  ? 0.1693 0.1394 0.1356 0.0409  -0.0119 -0.0046 79  TRP   C CA  
2328 C C   . TRP   C 65  ? 0.1700 0.1451 0.1509 0.0447  -0.0133 -0.0073 79  TRP   C C   
2329 O O   . TRP   C 65  ? 0.1823 0.1637 0.1661 0.0453  -0.0053 -0.0074 79  TRP   C O   
2330 C CB  . TRP   C 65  ? 0.1717 0.1456 0.1433 0.0416  0.0163  -0.0245 79  TRP   C CB  
2331 C CG  . TRP   C 65  ? 0.1578 0.1308 0.1253 0.0278  -0.0005 -0.0091 79  TRP   C CG  
2332 C CD1 . TRP   C 65  ? 0.1513 0.1348 0.1269 0.0266  0.0083  -0.0098 79  TRP   C CD1 
2333 C CD2 . TRP   C 65  ? 0.2036 0.1209 0.1403 0.0186  0.0031  -0.0010 79  TRP   C CD2 
2334 N NE1 . TRP   C 65  ? 0.1664 0.1366 0.1320 0.0228  0.0098  0.0002  79  TRP   C NE1 
2335 C CE2 . TRP   C 65  ? 0.1837 0.1237 0.1374 0.0146  0.0029  0.0075  79  TRP   C CE2 
2336 C CE3 . TRP   C 65  ? 0.2101 0.1250 0.1443 0.0208  -0.0145 0.0076  79  TRP   C CE3 
2337 C CZ2 . TRP   C 65  ? 0.1870 0.1265 0.1524 0.0183  -0.0181 0.0218  79  TRP   C CZ2 
2338 C CZ3 . TRP   C 65  ? 0.2352 0.1325 0.1535 0.0276  0.0171  0.0091  79  TRP   C CZ3 
2339 C CH2 . TRP   C 65  ? 0.2326 0.1326 0.1658 0.0203  0.0006  0.0191  79  TRP   C CH2 
2340 N N   . LYS   C 66  ? 0.1953 0.1506 0.1582 0.0641  0.0037  -0.0115 80  LYS   C N   
2341 C CA  . LYS   C 66  ? 0.1949 0.1605 0.1658 0.0593  0.0015  -0.0111 80  LYS   C CA  
2342 C C   . LYS   C 66  ? 0.1752 0.1677 0.1801 0.0538  -0.0116 -0.0125 80  LYS   C C   
2343 O O   . LYS   C 66  ? 0.1695 0.1679 0.1904 0.0483  0.0081  -0.0175 80  LYS   C O   
2344 C CB  . LYS   C 66  ? 0.2025 0.1771 0.1796 0.0507  0.0102  -0.0176 80  LYS   C CB  
2345 C CG  . LYS   C 66  ? 0.2228 0.2020 0.1743 0.0405  0.0208  -0.0239 80  LYS   C CG  
2346 C CD  . LYS   C 66  ? 0.2412 0.2281 0.2167 0.0372  0.0329  -0.0317 80  LYS   C CD  
2347 C CE  . LYS   C 66  ? 0.2674 0.2529 0.2646 0.0407  0.0376  -0.0580 80  LYS   C CE  
2348 N NZ  . LYS   C 66  ? 0.3124 0.2731 0.3062 0.0458  0.0604  -0.0558 80  LYS   C NZ  
2349 N N   . ASN   C 67  ? 0.1864 0.1723 0.1962 0.0467  -0.0086 -0.0400 81  ASN   C N   
2350 C CA  . ASN   C 67  ? 0.1953 0.1817 0.2497 0.0480  0.0103  -0.0469 81  ASN   C CA  
2351 C C   . ASN   C 67  ? 0.2365 0.1949 0.3319 0.0633  0.0244  -0.0715 81  ASN   C C   
2352 O O   . ASN   C 67  ? 0.2346 0.2135 0.3666 0.0682  0.0140  -0.0765 81  ASN   C O   
2353 C CB  . ASN   C 67  ? 0.2255 0.1804 0.2468 0.0329  -0.0007 -0.0284 81  ASN   C CB  
2354 C CG  . ASN   C 67  ? 0.2423 0.1794 0.2650 0.0445  -0.0143 -0.0238 81  ASN   C CG  
2355 O OD1 . ASN   C 67  ? 0.2777 0.1855 0.2762 0.0529  -0.0439 -0.0020 81  ASN   C OD1 
2356 N ND2 . ASN   C 67  ? 0.2740 0.1822 0.2681 0.0384  -0.0184 -0.0283 81  ASN   C ND2 
2357 N N   . ASN   C 68  ? 0.2896 0.2038 0.3752 0.0842  0.0252  -0.0943 82  ASN   C N   
2358 C CA  . ASN   C 68  ? 0.3250 0.2229 0.4542 0.1001  0.0334  -0.0995 82  ASN   C CA  
2359 C C   . ASN   C 68  ? 0.3068 0.2423 0.5158 0.1138  -0.0116 -0.0833 82  ASN   C C   
2360 O O   . ASN   C 68  ? 0.3032 0.2681 0.5640 0.1272  -0.0056 -0.0730 82  ASN   C O   
2361 C CB  . ASN   C 68  ? 0.3762 0.2328 0.4658 0.0874  0.0582  -0.1025 82  ASN   C CB  
2362 C CG  . ASN   C 68  ? 0.4239 0.2530 0.4618 0.0655  0.0693  -0.0957 82  ASN   C CG  
2363 O OD1 . ASN   C 68  ? 0.4765 0.2720 0.4691 0.0466  0.0820  -0.0935 82  ASN   C OD1 
2364 N ND2 . ASN   C 68  ? 0.4225 0.2634 0.4617 0.0527  0.0742  -0.0945 82  ASN   C ND2 
2365 N N   . TYR   C 69  ? 0.3207 0.2480 0.5206 0.0955  -0.0778 -0.0657 83  TYR   C N   
2366 C CA  . TYR   C 69  ? 0.3395 0.2633 0.5332 0.0879  -0.0869 -0.0558 83  TYR   C CA  
2367 C C   . TYR   C 69  ? 0.2949 0.2579 0.4977 0.0884  -0.0969 -0.0423 83  TYR   C C   
2368 O O   . TYR   C 69  ? 0.2843 0.2657 0.5228 0.0862  -0.0899 -0.0335 83  TYR   C O   
2369 C CB  . TYR   C 69  ? 0.4099 0.2926 0.5824 0.0580  -0.0707 -0.0578 83  TYR   C CB  
2370 C CG  . TYR   C 69  ? 0.4865 0.3266 0.6405 0.0268  -0.0229 -0.0593 83  TYR   C CG  
2371 C CD1 . TYR   C 69  ? 0.5384 0.3495 0.6676 -0.0011 0.0121  -0.0644 83  TYR   C CD1 
2372 C CD2 . TYR   C 69  ? 0.5085 0.3424 0.6695 0.0217  -0.0100 -0.0590 83  TYR   C CD2 
2373 C CE1 . TYR   C 69  ? 0.5678 0.3624 0.6897 -0.0132 0.0205  -0.0678 83  TYR   C CE1 
2374 C CE2 . TYR   C 69  ? 0.5385 0.3562 0.6904 0.0099  -0.0040 -0.0629 83  TYR   C CE2 
2375 C CZ  . TYR   C 69  ? 0.5735 0.3714 0.7070 -0.0098 0.0076  -0.0669 83  TYR   C CZ  
2376 O OH  . TYR   C 69  ? 0.5997 0.3851 0.7256 -0.0163 -0.0028 -0.0669 83  TYR   C OH  
2377 N N   . ARG   C 70  ? 0.2785 0.2362 0.4323 0.1103  -0.0914 -0.0173 84  ARG   C N   
2378 C CA  . ARG   C 70  ? 0.2916 0.2370 0.3851 0.0947  -0.0717 -0.0094 84  ARG   C CA  
2379 C C   . ARG   C 70  ? 0.2308 0.2012 0.3203 0.0782  -0.0609 -0.0254 84  ARG   C C   
2380 O O   . ARG   C 70  ? 0.2180 0.2014 0.3371 0.0634  -0.0507 -0.0356 84  ARG   C O   
2381 C CB  . ARG   C 70  ? 0.3451 0.2770 0.4081 0.1033  -0.0619 0.0153  84  ARG   C CB  
2382 C CG  . ARG   C 70  ? 0.4105 0.3174 0.4576 0.0871  -0.0473 0.0138  84  ARG   C CG  
2383 C CD  . ARG   C 70  ? 0.4880 0.3554 0.5046 0.0672  -0.0305 0.0047  84  ARG   C CD  
2384 N NE  . ARG   C 70  ? 0.5415 0.3804 0.5519 0.0536  -0.0292 0.0019  84  ARG   C NE  
2385 C CZ  . ARG   C 70  ? 0.5673 0.3940 0.5803 0.0462  -0.0269 0.0001  84  ARG   C CZ  
2386 N NH1 . ARG   C 70  ? 0.5731 0.3984 0.6007 0.0445  -0.0180 0.0006  84  ARG   C NH1 
2387 N NH2 . ARG   C 70  ? 0.5779 0.3956 0.5800 0.0427  -0.0258 -0.0079 84  ARG   C NH2 
2388 N N   . ASN   C 71  ? 0.2243 0.1878 0.2695 0.0617  -0.0427 -0.0249 85  ASN   C N   
2389 C CA  . ASN   C 71  ? 0.2250 0.1862 0.2182 0.0725  -0.0437 -0.0166 85  ASN   C CA  
2390 C C   . ASN   C 71  ? 0.2249 0.1967 0.2157 0.0577  -0.0390 -0.0195 85  ASN   C C   
2391 O O   . ASN   C 71  ? 0.2340 0.2121 0.2440 0.0645  -0.0371 -0.0241 85  ASN   C O   
2392 C CB  . ASN   C 71  ? 0.2213 0.1938 0.2052 0.0649  -0.0281 -0.0264 85  ASN   C CB  
2393 C CG  . ASN   C 71  ? 0.1880 0.1939 0.1956 0.0676  -0.0164 -0.0362 85  ASN   C CG  
2394 O OD1 . ASN   C 71  ? 0.1826 0.1845 0.2061 0.0641  -0.0304 -0.0468 85  ASN   C OD1 
2395 N ND2 . ASN   C 71  ? 0.2146 0.2139 0.1947 0.0866  -0.0003 -0.0334 85  ASN   C ND2 
2396 N N   . ALA   C 72  ? 0.2066 0.1906 0.1900 0.0648  -0.0254 -0.0066 86  ALA   C N   
2397 C CA  . ALA   C 72  ? 0.2034 0.1893 0.1794 0.0456  -0.0361 -0.0110 86  ALA   C CA  
2398 C C   . ALA   C 72  ? 0.1755 0.1819 0.1798 0.0368  -0.0418 -0.0248 86  ALA   C C   
2399 O O   . ALA   C 72  ? 0.1906 0.1914 0.1837 0.0253  -0.0183 -0.0336 86  ALA   C O   
2400 C CB  . ALA   C 72  ? 0.2076 0.1940 0.1877 0.0392  -0.0191 0.0005  86  ALA   C CB  
2401 N N   . HIS   C 73  ? 0.1488 0.1842 0.1816 0.0314  -0.0207 -0.0229 87  HIS   C N   
2402 C CA  . HIS   C 73  ? 0.1515 0.1785 0.1687 0.0347  -0.0124 -0.0177 87  HIS   C CA  
2403 C C   . HIS   C 73  ? 0.1717 0.1465 0.1454 0.0246  -0.0050 -0.0203 87  HIS   C C   
2404 O O   . HIS   C 73  ? 0.1654 0.1462 0.1528 0.0190  -0.0018 -0.0189 87  HIS   C O   
2405 C CB  . HIS   C 73  ? 0.1514 0.2143 0.1659 0.0393  -0.0069 -0.0252 87  HIS   C CB  
2406 C CG  . HIS   C 73  ? 0.1419 0.2446 0.1609 0.0452  -0.0311 -0.0355 87  HIS   C CG  
2407 N ND1 . HIS   C 73  ? 0.1482 0.2552 0.1704 0.0470  0.0028  -0.0281 87  HIS   C ND1 
2408 C CD2 . HIS   C 73  ? 0.1820 0.2659 0.2000 0.0494  -0.0066 -0.0388 87  HIS   C CD2 
2409 C CE1 . HIS   C 73  ? 0.1585 0.2650 0.1997 0.0480  -0.0206 -0.0278 87  HIS   C CE1 
2410 N NE2 . HIS   C 73  ? 0.1691 0.2739 0.2117 0.0662  -0.0265 -0.0368 87  HIS   C NE2 
2411 N N   . SER   C 74  ? 0.1723 0.1481 0.1305 0.0302  0.0006  -0.0012 88  SER   C N   
2412 C CA  . SER   C 74  ? 0.1615 0.1451 0.1088 0.0106  0.0025  -0.0016 88  SER   C CA  
2413 C C   . SER   C 74  ? 0.1540 0.1413 0.1201 0.0060  0.0034  -0.0171 88  SER   C C   
2414 O O   . SER   C 74  ? 0.1606 0.1397 0.1332 0.0159  0.0021  -0.0212 88  SER   C O   
2415 C CB  . SER   C 74  ? 0.1934 0.1546 0.1367 0.0182  -0.0147 0.0082  88  SER   C CB  
2416 O OG  . SER   C 74  ? 0.2161 0.1625 0.1828 0.0117  -0.0199 0.0067  88  SER   C OG  
2417 N N   . ALA   C 75  ? 0.1527 0.1493 0.1244 0.0032  -0.0120 -0.0154 89  ALA   C N   
2418 C CA  . ALA   C 75  ? 0.1354 0.1520 0.1127 -0.0007 -0.0044 -0.0126 89  ALA   C CA  
2419 C C   . ALA   C 75  ? 0.1443 0.1457 0.1074 -0.0014 -0.0030 -0.0093 89  ALA   C C   
2420 O O   . ALA   C 75  ? 0.1590 0.1211 0.1262 -0.0124 0.0062  -0.0051 89  ALA   C O   
2421 C CB  . ALA   C 75  ? 0.1585 0.1633 0.1146 0.0054  -0.0092 -0.0060 89  ALA   C CB  
2422 N N   . THR   C 76  ? 0.1220 0.1409 0.1084 0.0159  -0.0029 -0.0046 90  THR   C N   
2423 C CA  . THR   C 76  ? 0.1365 0.1264 0.1092 0.0003  0.0144  -0.0025 90  THR   C CA  
2424 C C   . THR   C 76  ? 0.1308 0.1199 0.1224 -0.0104 0.0089  -0.0006 90  THR   C C   
2425 O O   . THR   C 76  ? 0.1418 0.1144 0.1292 -0.0029 -0.0033 -0.0173 90  THR   C O   
2426 C CB  . THR   C 76  ? 0.1454 0.1228 0.1129 -0.0013 0.0089  0.0095  90  THR   C CB  
2427 O OG1 . THR   C 76  ? 0.1617 0.1227 0.1246 0.0088  -0.0098 0.0052  90  THR   C OG1 
2428 C CG2 . THR   C 76  ? 0.1334 0.1456 0.1248 -0.0019 0.0072  0.0061  90  THR   C CG2 
2429 N N   . THR   C 77  ? 0.1416 0.1216 0.1120 0.0088  0.0053  -0.0034 91  THR   C N   
2430 C CA  . THR   C 77  ? 0.1225 0.1218 0.1061 0.0008  0.0084  -0.0057 91  THR   C CA  
2431 C C   . THR   C 77  ? 0.1316 0.1243 0.0988 -0.0170 0.0041  -0.0062 91  THR   C C   
2432 O O   . THR   C 77  ? 0.1688 0.1573 0.1123 -0.0314 0.0195  -0.0206 91  THR   C O   
2433 C CB  . THR   C 77  ? 0.1593 0.1135 0.1073 0.0122  0.0109  -0.0066 91  THR   C CB  
2434 O OG1 . THR   C 77  ? 0.1858 0.1094 0.1360 -0.0028 0.0296  -0.0062 91  THR   C OG1 
2435 C CG2 . THR   C 77  ? 0.1606 0.1315 0.1248 0.0045  0.0164  0.0107  91  THR   C CG2 
2436 N N   . TRP   C 78  ? 0.1170 0.1175 0.1199 0.0012  0.0134  0.0089  92  TRP   C N   
2437 C CA  . TRP   C 78  ? 0.1339 0.1154 0.1229 0.0066  0.0106  0.0079  92  TRP   C CA  
2438 C C   . TRP   C 78  ? 0.1287 0.1256 0.1115 -0.0178 0.0072  -0.0225 92  TRP   C C   
2439 O O   . TRP   C 78  ? 0.1394 0.1425 0.1179 -0.0169 0.0056  -0.0086 92  TRP   C O   
2440 C CB  . TRP   C 78  ? 0.1663 0.1182 0.1190 -0.0015 -0.0078 0.0095  92  TRP   C CB  
2441 C CG  . TRP   C 78  ? 0.1726 0.1075 0.1190 -0.0036 0.0038  0.0089  92  TRP   C CG  
2442 C CD1 . TRP   C 78  ? 0.1503 0.1099 0.1202 -0.0045 0.0157  0.0214  92  TRP   C CD1 
2443 C CD2 . TRP   C 78  ? 0.1623 0.1000 0.1212 -0.0042 -0.0069 0.0005  92  TRP   C CD2 
2444 N NE1 . TRP   C 78  ? 0.1512 0.1221 0.1463 0.0030  0.0038  0.0162  92  TRP   C NE1 
2445 C CE2 . TRP   C 78  ? 0.1478 0.1121 0.1415 -0.0018 0.0167  0.0006  92  TRP   C CE2 
2446 C CE3 . TRP   C 78  ? 0.1631 0.1057 0.1308 0.0073  -0.0058 -0.0057 92  TRP   C CE3 
2447 C CZ2 . TRP   C 78  ? 0.1782 0.1120 0.1513 0.0017  0.0107  0.0068  92  TRP   C CZ2 
2448 C CZ3 . TRP   C 78  ? 0.1900 0.1126 0.1439 0.0015  0.0116  0.0108  92  TRP   C CZ3 
2449 C CH2 . TRP   C 78  ? 0.1923 0.1055 0.1600 -0.0010 0.0296  0.0165  92  TRP   C CH2 
2450 N N   . SER   C 79  ? 0.1352 0.1291 0.1253 -0.0012 0.0044  0.0005  93  SER   C N   
2451 C CA  . SER   C 79  ? 0.1433 0.1269 0.1517 0.0018  0.0134  0.0014  93  SER   C CA  
2452 C C   . SER   C 79  ? 0.1267 0.1291 0.1398 -0.0106 0.0195  -0.0054 93  SER   C C   
2453 O O   . SER   C 79  ? 0.1543 0.1642 0.1139 -0.0135 0.0020  -0.0196 93  SER   C O   
2454 C CB  . SER   C 79  ? 0.1402 0.1306 0.1684 -0.0017 -0.0007 0.0049  93  SER   C CB  
2455 O OG  . SER   C 79  ? 0.1267 0.1487 0.2009 0.0026  0.0226  0.0183  93  SER   C OG  
2456 N N   . GLY   C 80  ? 0.1375 0.1498 0.1350 -0.0187 0.0189  -0.0036 94  GLY   C N   
2457 C CA  . GLY   C 80  ? 0.1352 0.1702 0.1363 -0.0368 0.0167  -0.0013 94  GLY   C CA  
2458 C C   . GLY   C 80  ? 0.1262 0.1715 0.1186 -0.0243 0.0038  0.0110  94  GLY   C C   
2459 O O   . GLY   C 80  ? 0.1466 0.1773 0.1352 -0.0197 0.0091  -0.0028 94  GLY   C O   
2460 N N   . GLN   C 81  ? 0.1319 0.1760 0.1552 -0.0330 0.0187  0.0125  95  GLN   C N   
2461 C CA  . GLN   C 81  ? 0.1265 0.1950 0.1721 -0.0369 0.0112  0.0121  95  GLN   C CA  
2462 C C   . GLN   C 81  ? 0.1285 0.2012 0.1368 -0.0379 0.0097  0.0154  95  GLN   C C   
2463 O O   . GLN   C 81  ? 0.1598 0.1908 0.1477 -0.0348 0.0031  0.0141  95  GLN   C O   
2464 C CB  . GLN   C 81  ? 0.1382 0.2218 0.1843 -0.0283 0.0011  -0.0025 95  GLN   C CB  
2465 C CG  . GLN   C 81  ? 0.1719 0.2438 0.1989 -0.0257 0.0174  -0.0028 95  GLN   C CG  
2466 C CD  . GLN   C 81  ? 0.1642 0.2466 0.1861 -0.0222 0.0147  -0.0419 95  GLN   C CD  
2467 O OE1 . GLN   C 81  ? 0.1660 0.2480 0.1926 -0.0277 0.0248  -0.0424 95  GLN   C OE1 
2468 N NE2 . GLN   C 81  ? 0.1959 0.2502 0.2009 -0.0229 0.0112  -0.0498 95  GLN   C NE2 
2469 N N   . TYR   C 82  ? 0.1426 0.2031 0.1581 -0.0390 0.0078  0.0131  96  TYR   C N   
2470 C CA  . TYR   C 82  ? 0.1578 0.2064 0.1751 -0.0478 -0.0001 0.0109  96  TYR   C CA  
2471 C C   . TYR   C 82  ? 0.1761 0.2307 0.1840 -0.0525 -0.0015 0.0257  96  TYR   C C   
2472 O O   . TYR   C 82  ? 0.1764 0.2517 0.1879 -0.0396 0.0249  0.0206  96  TYR   C O   
2473 C CB  . TYR   C 82  ? 0.1842 0.1990 0.1442 -0.0528 -0.0045 0.0046  96  TYR   C CB  
2474 C CG  . TYR   C 82  ? 0.1939 0.2016 0.1712 -0.0602 -0.0031 0.0172  96  TYR   C CG  
2475 C CD1 . TYR   C 82  ? 0.2198 0.1983 0.2007 -0.0769 0.0072  0.0187  96  TYR   C CD1 
2476 C CD2 . TYR   C 82  ? 0.2161 0.2137 0.2125 -0.0728 -0.0075 0.0117  96  TYR   C CD2 
2477 C CE1 . TYR   C 82  ? 0.2302 0.2109 0.2359 -0.0900 0.0035  0.0023  96  TYR   C CE1 
2478 C CE2 . TYR   C 82  ? 0.2558 0.2208 0.2436 -0.0880 0.0019  0.0112  96  TYR   C CE2 
2479 C CZ  . TYR   C 82  ? 0.2589 0.2171 0.2531 -0.1105 0.0074  0.0094  96  TYR   C CZ  
2480 O OH  . TYR   C 82  ? 0.3208 0.2335 0.3148 -0.1254 0.0121  0.0047  96  TYR   C OH  
2481 N N   . VAL   C 83  ? 0.1902 0.2642 0.2024 -0.0533 0.0300  0.0341  97  VAL   C N   
2482 C CA  . VAL   C 83  ? 0.2308 0.3114 0.2312 -0.0330 0.0356  0.0535  97  VAL   C CA  
2483 C C   . VAL   C 83  ? 0.2122 0.3413 0.2444 -0.0598 0.0315  0.0813  97  VAL   C C   
2484 O O   . VAL   C 83  ? 0.2165 0.3343 0.2855 -0.0680 0.0056  0.0871  97  VAL   C O   
2485 C CB  . VAL   C 83  ? 0.3012 0.3191 0.2733 -0.0235 0.1015  0.0382  97  VAL   C CB  
2486 C CG1 . VAL   C 83  ? 0.3203 0.3265 0.2942 -0.0247 0.1230  0.0422  97  VAL   C CG1 
2487 C CG2 . VAL   C 83  ? 0.3567 0.3232 0.2971 -0.0143 0.0964  0.0322  97  VAL   C CG2 
2488 N N   . GLY   C 84  ? 0.2366 0.3743 0.2524 -0.0756 0.0139  0.0936  98  GLY   C N   
2489 C CA  . GLY   C 84  ? 0.2690 0.4006 0.2864 -0.0942 0.0123  0.0888  98  GLY   C CA  
2490 C C   . GLY   C 84  ? 0.3326 0.4236 0.3348 -0.1027 0.0524  0.0785  98  GLY   C C   
2491 O O   . GLY   C 84  ? 0.3490 0.4348 0.3408 -0.1044 0.0639  0.0644  98  GLY   C O   
2492 N N   . GLY   C 85  ? 0.4111 0.4336 0.3821 -0.0993 0.1012  0.0960  99  GLY   C N   
2493 C CA  . GLY   C 85  ? 0.4222 0.4417 0.4136 -0.1099 0.1310  0.1037  99  GLY   C CA  
2494 C C   . GLY   C 85  ? 0.4426 0.4506 0.4477 -0.1097 0.1175  0.0985  99  GLY   C C   
2495 O O   . GLY   C 85  ? 0.4562 0.4499 0.4602 -0.1266 0.1074  0.0995  99  GLY   C O   
2496 N N   . ALA   C 86  ? 0.4509 0.4597 0.4556 -0.0986 0.1145  0.1010  100 ALA   C N   
2497 C CA  . ALA   C 86  ? 0.4819 0.4685 0.4573 -0.0812 0.1140  0.1019  100 ALA   C CA  
2498 C C   . ALA   C 86  ? 0.4908 0.4719 0.4568 -0.0768 0.1096  0.0905  100 ALA   C C   
2499 O O   . ALA   C 86  ? 0.5187 0.4765 0.4705 -0.0825 0.1419  0.0838  100 ALA   C O   
2500 C CB  . ALA   C 86  ? 0.5034 0.4719 0.4634 -0.0686 0.1158  0.1006  100 ALA   C CB  
2501 N N   . GLU   C 87  ? 0.4520 0.4647 0.4297 -0.0837 0.0852  0.1001  101 GLU   C N   
2502 C CA  . GLU   C 87  ? 0.4144 0.4549 0.3876 -0.0880 0.0651  0.1154  101 GLU   C CA  
2503 C C   . GLU   C 87  ? 0.3699 0.4341 0.3322 -0.0914 0.0549  0.1078  101 GLU   C C   
2504 O O   . GLU   C 87  ? 0.3766 0.4363 0.3113 -0.0795 0.0594  0.1120  101 GLU   C O   
2505 C CB  . GLU   C 87  ? 0.4423 0.4625 0.4147 -0.0774 0.0579  0.1345  101 GLU   C CB  
2506 C CG  . GLU   C 87  ? 0.4512 0.4682 0.4425 -0.0641 0.0512  0.1524  101 GLU   C CG  
2507 C CD  . GLU   C 87  ? 0.4534 0.4719 0.4659 -0.0544 0.0544  0.1770  101 GLU   C CD  
2508 O OE1 . GLU   C 87  ? 0.4598 0.4730 0.4692 -0.0468 0.0468  0.1795  101 GLU   C OE1 
2509 O OE2 . GLU   C 87  ? 0.4544 0.4732 0.4779 -0.0571 0.0722  0.2002  101 GLU   C OE2 
2510 N N   . ALA   C 88  ? 0.3160 0.4084 0.3072 -0.0991 0.0243  0.0981  102 ALA   C N   
2511 C CA  . ALA   C 88  ? 0.2497 0.3683 0.2627 -0.1198 0.0064  0.0992  102 ALA   C CA  
2512 C C   . ALA   C 88  ? 0.2269 0.3342 0.2316 -0.1028 -0.0019 0.0914  102 ALA   C C   
2513 O O   . ALA   C 88  ? 0.2454 0.3384 0.2494 -0.1013 0.0017  0.1038  102 ALA   C O   
2514 C CB  . ALA   C 88  ? 0.2695 0.3714 0.2788 -0.1248 -0.0317 0.0760  102 ALA   C CB  
2515 N N   . ARG   C 89  ? 0.2069 0.2899 0.2107 -0.0969 0.0113  0.0753  103 ARG   C N   
2516 C CA  . ARG   C 89  ? 0.2226 0.2681 0.1807 -0.0762 0.0188  0.0498  103 ARG   C CA  
2517 C C   . ARG   C 89  ? 0.1920 0.2251 0.1756 -0.0680 0.0051  0.0448  103 ARG   C C   
2518 O O   . ARG   C 89  ? 0.1916 0.2316 0.2032 -0.0684 -0.0064 0.0282  103 ARG   C O   
2519 C CB  . ARG   C 89  ? 0.2722 0.2997 0.2143 -0.0712 0.0238  0.0207  103 ARG   C CB  
2520 C CG  . ARG   C 89  ? 0.2934 0.3137 0.2208 -0.0787 0.0503  0.0339  103 ARG   C CG  
2521 C CD  . ARG   C 89  ? 0.3163 0.3260 0.2322 -0.0772 0.0619  0.0383  103 ARG   C CD  
2522 N NE  . ARG   C 89  ? 0.3355 0.3279 0.2467 -0.0572 0.0754  0.0267  103 ARG   C NE  
2523 C CZ  . ARG   C 89  ? 0.3452 0.3168 0.2803 -0.0634 0.0883  0.0513  103 ARG   C CZ  
2524 N NH1 . ARG   C 89  ? 0.3386 0.3115 0.2807 -0.0677 0.0633  0.0455  103 ARG   C NH1 
2525 N NH2 . ARG   C 89  ? 0.3906 0.3124 0.3107 -0.0610 0.0822  0.0579  103 ARG   C NH2 
2526 N N   . ILE   C 90  ? 0.1729 0.1943 0.1694 -0.0482 0.0298  0.0253  104 ILE   C N   
2527 C CA  . ILE   C 90  ? 0.1896 0.1700 0.1527 -0.0527 0.0214  0.0100  104 ILE   C CA  
2528 C C   . ILE   C 90  ? 0.1834 0.1712 0.1466 -0.0561 0.0140  0.0025  104 ILE   C C   
2529 O O   . ILE   C 90  ? 0.2172 0.1742 0.1665 -0.0430 -0.0074 0.0043  104 ILE   C O   
2530 C CB  . ILE   C 90  ? 0.2058 0.1671 0.1490 -0.0517 0.0243  0.0157  104 ILE   C CB  
2531 C CG1 . ILE   C 90  ? 0.2373 0.1839 0.1586 -0.0261 0.0360  0.0079  104 ILE   C CG1 
2532 C CG2 . ILE   C 90  ? 0.2324 0.1789 0.1715 -0.0581 0.0520  0.0016  104 ILE   C CG2 
2533 C CD1 . ILE   C 90  ? 0.2750 0.1873 0.1730 -0.0167 0.0397  0.0109  104 ILE   C CD1 
2534 N N   . ASN   C 91  ? 0.1699 0.1730 0.1539 -0.0448 0.0175  0.0019  105 ASN   C N   
2535 C CA  . ASN   C 91  ? 0.1661 0.1702 0.1315 -0.0314 0.0332  0.0005  105 ASN   C CA  
2536 C C   . ASN   C 91  ? 0.1626 0.1680 0.1214 -0.0432 0.0140  0.0055  105 ASN   C C   
2537 O O   . ASN   C 91  ? 0.1645 0.1846 0.1391 -0.0429 -0.0059 0.0145  105 ASN   C O   
2538 C CB  . ASN   C 91  ? 0.1945 0.1978 0.1847 -0.0077 0.0547  0.0133  105 ASN   C CB  
2539 C CG  . ASN   C 91  ? 0.2440 0.2340 0.2133 0.0218  0.0615  0.0380  105 ASN   C CG  
2540 O OD1 . ASN   C 91  ? 0.2450 0.2543 0.2096 0.0267  0.0622  0.0512  105 ASN   C OD1 
2541 N ND2 . ASN   C 91  ? 0.2940 0.2546 0.2611 0.0086  0.0774  0.0370  105 ASN   C ND2 
2542 N N   . THR   C 92  ? 0.1623 0.1670 0.1059 -0.0383 0.0086  -0.0092 106 THR   C N   
2543 C CA  . THR   C 92  ? 0.1687 0.1547 0.1245 -0.0365 0.0325  -0.0125 106 THR   C CA  
2544 C C   . THR   C 92  ? 0.1588 0.1542 0.1129 -0.0176 0.0237  -0.0034 106 THR   C C   
2545 O O   . THR   C 92  ? 0.1465 0.1595 0.1237 -0.0125 0.0218  -0.0024 106 THR   C O   
2546 C CB  . THR   C 92  ? 0.1535 0.1450 0.1287 -0.0107 0.0063  -0.0010 106 THR   C CB  
2547 O OG1 . THR   C 92  ? 0.1737 0.1495 0.1370 -0.0087 0.0079  -0.0047 106 THR   C OG1 
2548 C CG2 . THR   C 92  ? 0.1618 0.1489 0.1541 -0.0187 0.0100  -0.0046 106 THR   C CG2 
2549 N N   . GLN   C 93  ? 0.1556 0.1406 0.1226 -0.0267 0.0289  -0.0162 107 GLN   C N   
2550 C CA  A GLN   C 93  ? 0.1413 0.1324 0.1346 -0.0092 0.0257  -0.0057 107 GLN   C CA  
2551 C CA  B GLN   C 93  ? 0.1309 0.1321 0.1171 -0.0239 0.0264  -0.0228 107 GLN   C CA  
2552 C C   . GLN   C 93  ? 0.1320 0.1202 0.1112 -0.0187 0.0117  -0.0068 107 GLN   C C   
2553 O O   . GLN   C 93  ? 0.1410 0.1453 0.1240 -0.0107 -0.0050 -0.0155 107 GLN   C O   
2554 C CB  A GLN   C 93  ? 0.1934 0.1584 0.1785 -0.0075 0.0532  -0.0175 107 GLN   C CB  
2555 C CB  B GLN   C 93  ? 0.1208 0.1419 0.1166 -0.0339 0.0365  -0.0491 107 GLN   C CB  
2556 C CG  A GLN   C 93  ? 0.2054 0.1772 0.1835 -0.0123 0.0369  -0.0053 107 GLN   C CG  
2557 C CG  B GLN   C 93  ? 0.1115 0.1569 0.1167 -0.0194 0.0448  -0.0504 107 GLN   C CG  
2558 C CD  A GLN   C 93  ? 0.1908 0.1847 0.1949 -0.0139 0.0025  -0.0032 107 GLN   C CD  
2559 C CD  B GLN   C 93  ? 0.1001 0.1653 0.1063 -0.0050 0.0270  -0.0429 107 GLN   C CD  
2560 O OE1 A GLN   C 93  ? 0.2037 0.2014 0.2171 0.0047  -0.0150 -0.0088 107 GLN   C OE1 
2561 O OE1 B GLN   C 93  ? 0.1069 0.1641 0.1101 0.0046  -0.0096 -0.0447 107 GLN   C OE1 
2562 N NE2 A GLN   C 93  ? 0.1968 0.1918 0.1601 0.0107  -0.0150 -0.0094 107 GLN   C NE2 
2563 N NE2 B GLN   C 93  ? 0.1125 0.1795 0.1020 0.0121  0.0255  -0.0366 107 GLN   C NE2 
2564 N N   . TRP   C 94  ? 0.1286 0.1099 0.1059 -0.0090 0.0226  0.0043  108 TRP   C N   
2565 C CA  . TRP   C 94  ? 0.1316 0.1133 0.1259 -0.0060 0.0168  0.0013  108 TRP   C CA  
2566 C C   . TRP   C 94  ? 0.1217 0.1100 0.1161 0.0096  -0.0027 0.0016  108 TRP   C C   
2567 O O   . TRP   C 94  ? 0.1440 0.1045 0.1149 -0.0053 0.0054  0.0023  108 TRP   C O   
2568 C CB  . TRP   C 94  ? 0.1539 0.1176 0.1078 0.0030  0.0001  -0.0109 108 TRP   C CB  
2569 C CG  . TRP   C 94  ? 0.1679 0.1110 0.1079 -0.0053 0.0101  -0.0025 108 TRP   C CG  
2570 C CD1 . TRP   C 94  ? 0.1973 0.1256 0.1152 -0.0054 0.0181  -0.0034 108 TRP   C CD1 
2571 C CD2 . TRP   C 94  ? 0.1529 0.1211 0.1205 -0.0096 0.0124  0.0118  108 TRP   C CD2 
2572 N NE1 . TRP   C 94  ? 0.1889 0.1388 0.1209 -0.0061 0.0074  0.0039  108 TRP   C NE1 
2573 C CE2 . TRP   C 94  ? 0.1598 0.1381 0.1262 -0.0066 0.0050  -0.0061 108 TRP   C CE2 
2574 C CE3 . TRP   C 94  ? 0.1236 0.1232 0.1170 -0.0039 -0.0033 -0.0077 108 TRP   C CE3 
2575 C CZ2 . TRP   C 94  ? 0.1655 0.1349 0.1463 -0.0006 0.0001  0.0061  108 TRP   C CZ2 
2576 C CZ3 . TRP   C 94  ? 0.1323 0.1140 0.1229 0.0068  0.0026  -0.0186 108 TRP   C CZ3 
2577 C CH2 . TRP   C 94  ? 0.1470 0.1227 0.1359 0.0112  -0.0097 -0.0090 108 TRP   C CH2 
2578 N N   . LEU   C 95  ? 0.1191 0.1186 0.1188 -0.0089 0.0096  -0.0007 109 LEU   C N   
2579 C CA  . LEU   C 95  ? 0.1392 0.1095 0.1170 -0.0007 0.0058  0.0008  109 LEU   C CA  
2580 C C   . LEU   C 95  ? 0.1659 0.1152 0.1199 0.0090  -0.0060 -0.0143 109 LEU   C C   
2581 O O   . LEU   C 95  ? 0.1520 0.1508 0.1602 0.0109  -0.0217 -0.0575 109 LEU   C O   
2582 C CB  . LEU   C 95  ? 0.1484 0.1196 0.1134 0.0038  -0.0052 0.0163  109 LEU   C CB  
2583 C CG  . LEU   C 95  ? 0.1674 0.1258 0.1264 0.0163  0.0002  0.0087  109 LEU   C CG  
2584 C CD1 . LEU   C 95  ? 0.1969 0.1307 0.1387 0.0214  0.0108  0.0305  109 LEU   C CD1 
2585 C CD2 . LEU   C 95  ? 0.2049 0.1401 0.1631 0.0266  0.0057  -0.0128 109 LEU   C CD2 
2586 N N   . LEU   C 96  ? 0.1361 0.1136 0.1154 0.0066  -0.0051 -0.0058 110 LEU   C N   
2587 C CA  . LEU   C 96  ? 0.1318 0.1243 0.1212 0.0052  0.0052  0.0060  110 LEU   C CA  
2588 C C   . LEU   C 96  ? 0.1344 0.1219 0.1095 -0.0024 0.0041  -0.0019 110 LEU   C C   
2589 O O   . LEU   C 96  ? 0.1468 0.1287 0.1101 -0.0079 0.0039  -0.0088 110 LEU   C O   
2590 C CB  . LEU   C 96  ? 0.1601 0.1338 0.1232 0.0130  0.0041  0.0031  110 LEU   C CB  
2591 C CG  . LEU   C 96  ? 0.1614 0.1423 0.1330 0.0311  0.0123  0.0213  110 LEU   C CG  
2592 C CD1 . LEU   C 96  ? 0.1820 0.1498 0.1379 0.0348  0.0238  0.0063  110 LEU   C CD1 
2593 C CD2 . LEU   C 96  ? 0.2071 0.1496 0.1651 0.0217  0.0135  0.0402  110 LEU   C CD2 
2594 N N   . THR   C 97  ? 0.1500 0.1196 0.1005 0.0066  0.0210  -0.0023 111 THR   C N   
2595 C CA  . THR   C 97  ? 0.1403 0.1308 0.0989 -0.0012 0.0161  0.0026  111 THR   C CA  
2596 C C   . THR   C 97  ? 0.1349 0.1419 0.1045 -0.0132 0.0209  -0.0173 111 THR   C C   
2597 O O   . THR   C 97  ? 0.1505 0.1440 0.1299 -0.0157 0.0051  -0.0206 111 THR   C O   
2598 C CB  . THR   C 97  ? 0.1418 0.1417 0.1374 0.0083  -0.0043 0.0146  111 THR   C CB  
2599 O OG1 . THR   C 97  ? 0.1609 0.1270 0.1390 0.0173  -0.0021 0.0026  111 THR   C OG1 
2600 C CG2 . THR   C 97  ? 0.1654 0.1519 0.1426 0.0074  0.0068  0.0135  111 THR   C CG2 
2601 N N   . SER   C 98  ? 0.1237 0.1535 0.1416 0.0081  0.0058  0.0005  112 SER   C N   
2602 C CA  . SER   C 98  ? 0.1288 0.1734 0.1526 0.0078  0.0073  -0.0107 112 SER   C CA  
2603 C C   . SER   C 98  ? 0.1431 0.1663 0.1568 0.0184  0.0183  -0.0106 112 SER   C C   
2604 O O   . SER   C 98  ? 0.1471 0.1639 0.1813 -0.0060 0.0344  -0.0100 112 SER   C O   
2605 C CB  . SER   C 98  ? 0.1461 0.1754 0.1584 0.0131  -0.0073 -0.0048 112 SER   C CB  
2606 O OG  . SER   C 98  ? 0.1808 0.1814 0.1865 0.0123  0.0067  0.0116  112 SER   C OG  
2607 N N   . GLY   C 99  ? 0.1380 0.1726 0.1435 0.0092  0.0146  -0.0025 113 GLY   C N   
2608 C CA  . GLY   C 99  ? 0.1408 0.1766 0.1774 0.0132  0.0126  -0.0014 113 GLY   C CA  
2609 C C   . GLY   C 99  ? 0.1285 0.1824 0.2062 0.0243  0.0009  -0.0016 113 GLY   C C   
2610 O O   . GLY   C 99  ? 0.1568 0.2035 0.2437 0.0184  -0.0224 0.0086  113 GLY   C O   
2611 N N   . THR   C 100 ? 0.1373 0.1794 0.1803 0.0048  0.0174  -0.0115 114 THR   C N   
2612 C CA  . THR   C 100 ? 0.1377 0.2018 0.1727 -0.0115 0.0000  -0.0137 114 THR   C CA  
2613 C C   . THR   C 100 ? 0.1157 0.2156 0.1738 -0.0269 -0.0030 -0.0281 114 THR   C C   
2614 O O   . THR   C 100 ? 0.1353 0.2164 0.1581 -0.0298 0.0098  -0.0175 114 THR   C O   
2615 C CB  . THR   C 100 ? 0.1430 0.2071 0.1675 -0.0084 0.0135  -0.0048 114 THR   C CB  
2616 O OG1 . THR   C 100 ? 0.1509 0.1961 0.1720 -0.0100 0.0079  -0.0190 114 THR   C OG1 
2617 C CG2 . THR   C 100 ? 0.1760 0.2199 0.1761 -0.0296 0.0171  0.0105  114 THR   C CG2 
2618 N N   . THR   C 101 ? 0.1377 0.2401 0.2034 -0.0307 0.0401  -0.0241 115 THR   C N   
2619 C CA  . THR   C 101 ? 0.1336 0.2551 0.2296 -0.0484 0.0287  -0.0402 115 THR   C CA  
2620 C C   . THR   C 101 ? 0.1643 0.2425 0.2084 -0.0475 0.0329  -0.0285 115 THR   C C   
2621 O O   . THR   C 101 ? 0.1787 0.2405 0.1856 -0.0251 0.0359  -0.0115 115 THR   C O   
2622 C CB  . THR   C 101 ? 0.1540 0.2914 0.2790 -0.0487 0.0130  -0.0487 115 THR   C CB  
2623 O OG1 . THR   C 101 ? 0.1773 0.3073 0.2980 -0.0496 0.0059  -0.0389 115 THR   C OG1 
2624 C CG2 . THR   C 101 ? 0.1839 0.3032 0.3071 -0.0298 0.0173  -0.0476 115 THR   C CG2 
2625 N N   . GLU   C 102 ? 0.2337 0.2360 0.2104 -0.0403 0.0344  -0.0146 116 GLU   C N   
2626 C CA  . GLU   C 102 ? 0.2782 0.2397 0.2158 -0.0436 0.0489  0.0074  116 GLU   C CA  
2627 C C   . GLU   C 102 ? 0.2590 0.2355 0.2178 -0.0649 0.0502  -0.0222 116 GLU   C C   
2628 O O   . GLU   C 102 ? 0.2637 0.2377 0.2285 -0.0616 0.0936  -0.0275 116 GLU   C O   
2629 C CB  . GLU   C 102 ? 0.3317 0.2552 0.2408 -0.0260 0.0380  0.0388  116 GLU   C CB  
2630 C CG  . GLU   C 102 ? 0.3629 0.2766 0.2830 -0.0221 0.0295  0.0358  116 GLU   C CG  
2631 C CD  . GLU   C 102 ? 0.3611 0.2833 0.3117 -0.0219 0.0200  0.0396  116 GLU   C CD  
2632 O OE1 . GLU   C 102 ? 0.3652 0.2856 0.3336 -0.0206 0.0209  0.0418  116 GLU   C OE1 
2633 O OE2 . GLU   C 102 ? 0.3584 0.2878 0.3203 -0.0242 0.0127  0.0437  116 GLU   C OE2 
2634 N N   . ALA   C 103 ? 0.2468 0.2475 0.2314 -0.0903 0.0460  -0.0373 117 ALA   C N   
2635 C CA  . ALA   C 103 ? 0.2343 0.2685 0.2580 -0.1076 0.0439  -0.0449 117 ALA   C CA  
2636 C C   . ALA   C 103 ? 0.2201 0.2713 0.2182 -0.0877 0.0330  -0.0501 117 ALA   C C   
2637 O O   . ALA   C 103 ? 0.2441 0.2714 0.2305 -0.0921 0.0238  -0.0557 117 ALA   C O   
2638 C CB  . ALA   C 103 ? 0.2305 0.2770 0.3076 -0.1173 0.0588  -0.0312 117 ALA   C CB  
2639 N N   . ASN   C 104 ? 0.2024 0.2672 0.1854 -0.0805 0.0346  -0.0370 118 ASN   C N   
2640 C CA  . ASN   C 104 ? 0.1780 0.2747 0.1931 -0.0652 0.0067  -0.0227 118 ASN   C CA  
2641 C C   . ASN   C 104 ? 0.1696 0.2528 0.1533 -0.0574 0.0139  -0.0094 118 ASN   C C   
2642 O O   . ASN   C 104 ? 0.1784 0.2559 0.1547 -0.0553 0.0232  -0.0184 118 ASN   C O   
2643 C CB  . ASN   C 104 ? 0.1894 0.3116 0.2228 -0.0496 -0.0380 -0.0163 118 ASN   C CB  
2644 C CG  . ASN   C 104 ? 0.2377 0.3496 0.2432 -0.0415 -0.0547 -0.0343 118 ASN   C CG  
2645 O OD1 . ASN   C 104 ? 0.2429 0.3723 0.2764 -0.0459 -0.0683 -0.0349 118 ASN   C OD1 
2646 N ND2 . ASN   C 104 ? 0.2875 0.3665 0.2755 -0.0168 -0.0579 -0.0177 118 ASN   C ND2 
2647 N N   . ALA   C 105 ? 0.1648 0.2201 0.1452 -0.0375 0.0165  -0.0176 119 ALA   C N   
2648 C CA  . ALA   C 105 ? 0.1564 0.2045 0.1506 -0.0248 0.0120  -0.0174 119 ALA   C CA  
2649 C C   . ALA   C 105 ? 0.1721 0.1774 0.1624 -0.0227 0.0213  -0.0222 119 ALA   C C   
2650 O O   . ALA   C 105 ? 0.1557 0.1683 0.1844 -0.0196 0.0199  -0.0137 119 ALA   C O   
2651 C CB  . ALA   C 105 ? 0.1924 0.2228 0.1428 -0.0177 0.0216  -0.0208 119 ALA   C CB  
2652 N N   . TRP   C 106 ? 0.1864 0.1803 0.1692 -0.0330 0.0295  -0.0353 120 TRP   C N   
2653 C CA  . TRP   C 106 ? 0.2065 0.1855 0.1825 -0.0590 0.0524  -0.0371 120 TRP   C CA  
2654 C C   . TRP   C 106 ? 0.1687 0.1767 0.1826 -0.0535 0.0377  -0.0359 120 TRP   C C   
2655 O O   . TRP   C 106 ? 0.2022 0.1734 0.2154 -0.0463 0.0777  -0.0456 120 TRP   C O   
2656 C CB  . TRP   C 106 ? 0.2422 0.2082 0.2132 -0.0813 0.0665  -0.0561 120 TRP   C CB  
2657 C CG  . TRP   C 106 ? 0.2652 0.2277 0.2059 -0.1064 0.0439  -0.0731 120 TRP   C CG  
2658 C CD1 . TRP   C 106 ? 0.2584 0.2431 0.2201 -0.1190 0.0385  -0.0688 120 TRP   C CD1 
2659 C CD2 . TRP   C 106 ? 0.2755 0.2439 0.2018 -0.1135 0.0403  -0.0740 120 TRP   C CD2 
2660 N NE1 . TRP   C 106 ? 0.2625 0.2590 0.2148 -0.0959 0.0495  -0.0621 120 TRP   C NE1 
2661 C CE2 . TRP   C 106 ? 0.2775 0.2601 0.1945 -0.1071 0.0259  -0.0624 120 TRP   C CE2 
2662 C CE3 . TRP   C 106 ? 0.3039 0.2542 0.1993 -0.1095 0.0550  -0.0784 120 TRP   C CE3 
2663 C CZ2 . TRP   C 106 ? 0.3097 0.2777 0.2260 -0.0892 0.0250  -0.0585 120 TRP   C CZ2 
2664 C CZ3 . TRP   C 106 ? 0.3066 0.2614 0.2193 -0.1036 0.0256  -0.0668 120 TRP   C CZ3 
2665 C CH2 . TRP   C 106 ? 0.3080 0.2670 0.2145 -0.1011 0.0129  -0.0627 120 TRP   C CH2 
2666 N N   . LYS   C 107 ? 0.1649 0.1927 0.1675 -0.0489 0.0164  -0.0099 121 LYS   C N   
2667 C CA  . LYS   C 107 ? 0.1507 0.2066 0.1522 -0.0403 0.0107  -0.0105 121 LYS   C CA  
2668 C C   . LYS   C 107 ? 0.1483 0.1847 0.1387 -0.0145 -0.0051 -0.0087 121 LYS   C C   
2669 O O   . LYS   C 107 ? 0.1490 0.1914 0.1753 -0.0025 -0.0229 0.0061  121 LYS   C O   
2670 C CB  . LYS   C 107 ? 0.1732 0.2430 0.1887 -0.0395 0.0190  -0.0179 121 LYS   C CB  
2671 C CG  . LYS   C 107 ? 0.1751 0.2793 0.2054 -0.0257 -0.0305 -0.0058 121 LYS   C CG  
2672 C CD  . LYS   C 107 ? 0.1810 0.3129 0.2521 -0.0258 -0.0348 0.0180  121 LYS   C CD  
2673 C CE  . LYS   C 107 ? 0.1961 0.3442 0.2935 -0.0094 -0.0586 0.0350  121 LYS   C CE  
2674 N NZ  . LYS   C 107 ? 0.2373 0.3613 0.3391 -0.0008 -0.0648 0.0396  121 LYS   C NZ  
2675 N N   . SER   C 108 ? 0.1515 0.1529 0.1358 -0.0163 0.0036  -0.0119 122 SER   C N   
2676 C CA  . SER   C 108 ? 0.1678 0.1455 0.1249 -0.0205 0.0154  -0.0111 122 SER   C CA  
2677 C C   . SER   C 108 ? 0.1491 0.1309 0.1169 0.0069  0.0083  -0.0038 122 SER   C C   
2678 O O   . SER   C 108 ? 0.1246 0.1289 0.1449 0.0126  0.0103  -0.0217 122 SER   C O   
2679 C CB  . SER   C 108 ? 0.1775 0.1544 0.1499 -0.0091 0.0221  -0.0120 122 SER   C CB  
2680 O OG  . SER   C 108 ? 0.2152 0.1580 0.1573 -0.0169 -0.0164 0.0053  122 SER   C OG  
2681 N N   . THR   C 109 ? 0.1529 0.1159 0.1064 -0.0070 0.0082  -0.0020 123 THR   C N   
2682 C CA  . THR   C 109 ? 0.1489 0.1120 0.1073 -0.0074 0.0066  0.0098  123 THR   C CA  
2683 C C   . THR   C 109 ? 0.1521 0.1138 0.0947 0.0001  -0.0038 -0.0056 123 THR   C C   
2684 O O   . THR   C 109 ? 0.1697 0.1147 0.1126 0.0113  0.0020  -0.0040 123 THR   C O   
2685 C CB  . THR   C 109 ? 0.1562 0.1282 0.1051 0.0111  -0.0046 0.0285  123 THR   C CB  
2686 O OG1 . THR   C 109 ? 0.1702 0.1503 0.1194 0.0084  0.0056  0.0267  123 THR   C OG1 
2687 C CG2 . THR   C 109 ? 0.1482 0.1214 0.1342 0.0162  -0.0029 -0.0032 123 THR   C CG2 
2688 N N   . LEU   C 110 ? 0.1469 0.1146 0.1057 -0.0111 0.0100  0.0115  124 LEU   C N   
2689 C CA  . LEU   C 110 ? 0.1324 0.1197 0.1108 -0.0102 0.0104  0.0090  124 LEU   C CA  
2690 C C   . LEU   C 110 ? 0.1235 0.1199 0.1068 -0.0028 0.0058  -0.0045 124 LEU   C C   
2691 O O   . LEU   C 110 ? 0.1442 0.1286 0.1114 0.0000  -0.0005 -0.0092 124 LEU   C O   
2692 C CB  . LEU   C 110 ? 0.1582 0.1320 0.1301 -0.0168 -0.0149 0.0080  124 LEU   C CB  
2693 C CG  . LEU   C 110 ? 0.1667 0.1454 0.1217 0.0061  -0.0222 -0.0201 124 LEU   C CG  
2694 C CD1 . LEU   C 110 ? 0.2214 0.1464 0.1641 0.0313  -0.0140 -0.0294 124 LEU   C CD1 
2695 C CD2 . LEU   C 110 ? 0.1457 0.1624 0.1412 -0.0011 -0.0247 -0.0194 124 LEU   C CD2 
2696 N N   . VAL   C 111 ? 0.1393 0.1320 0.1039 -0.0069 0.0064  -0.0044 125 VAL   C N   
2697 C CA  . VAL   C 111 ? 0.1365 0.1255 0.1221 0.0033  0.0131  -0.0034 125 VAL   C CA  
2698 C C   . VAL   C 111 ? 0.1203 0.1319 0.1012 0.0057  0.0040  0.0041  125 VAL   C C   
2699 O O   . VAL   C 111 ? 0.1314 0.1470 0.1144 -0.0027 -0.0010 0.0074  125 VAL   C O   
2700 C CB  . VAL   C 111 ? 0.1623 0.1170 0.1283 -0.0033 0.0107  -0.0163 125 VAL   C CB  
2701 C CG1 . VAL   C 111 ? 0.2003 0.1127 0.1298 -0.0032 0.0064  -0.0115 125 VAL   C CG1 
2702 C CG2 . VAL   C 111 ? 0.1490 0.1232 0.1408 0.0031  0.0112  -0.0084 125 VAL   C CG2 
2703 N N   . GLY   C 112 ? 0.1226 0.1185 0.1159 -0.0139 0.0104  0.0023  126 GLY   C N   
2704 C CA  . GLY   C 112 ? 0.1290 0.1249 0.1126 -0.0218 0.0130  0.0069  126 GLY   C CA  
2705 C C   . GLY   C 112 ? 0.1337 0.1420 0.0945 -0.0261 0.0032  -0.0101 126 GLY   C C   
2706 O O   . GLY   C 112 ? 0.1439 0.1567 0.0954 -0.0271 0.0023  -0.0161 126 GLY   C O   
2707 N N   . HIS   C 113 ? 0.1524 0.1420 0.1276 -0.0294 0.0089  -0.0066 127 HIS   C N   
2708 C CA  . HIS   C 113 ? 0.1753 0.1390 0.1314 -0.0294 0.0159  -0.0070 127 HIS   C CA  
2709 C C   . HIS   C 113 ? 0.1869 0.1390 0.1211 -0.0178 0.0016  0.0150  127 HIS   C C   
2710 O O   . HIS   C 113 ? 0.2316 0.1528 0.1520 -0.0209 -0.0290 0.0230  127 HIS   C O   
2711 C CB  . HIS   C 113 ? 0.1983 0.1595 0.1282 0.0037  0.0082  0.0016  127 HIS   C CB  
2712 C CG  . HIS   C 113 ? 0.2568 0.1646 0.1397 0.0251  0.0329  -0.0031 127 HIS   C CG  
2713 N ND1 . HIS   C 113 ? 0.3306 0.1866 0.1582 0.0372  0.0314  -0.0025 127 HIS   C ND1 
2714 C CD2 . HIS   C 113 ? 0.2661 0.1737 0.1135 0.0326  -0.0019 -0.0345 127 HIS   C CD2 
2715 C CE1 . HIS   C 113 ? 0.3575 0.1944 0.1554 0.0441  0.0089  -0.0044 127 HIS   C CE1 
2716 N NE2 . HIS   C 113 ? 0.3220 0.1934 0.1604 0.0452  -0.0069 -0.0417 127 HIS   C NE2 
2717 N N   . ASP   C 114 ? 0.1746 0.1342 0.1361 -0.0302 0.0149  0.0078  128 ASP   C N   
2718 C CA  . ASP   C 114 ? 0.1681 0.1354 0.1502 -0.0449 0.0042  0.0128  128 ASP   C CA  
2719 C C   . ASP   C 114 ? 0.1715 0.1440 0.1659 -0.0445 0.0028  0.0204  128 ASP   C C   
2720 O O   . ASP   C 114 ? 0.1601 0.1542 0.1598 -0.0276 0.0019  0.0314  128 ASP   C O   
2721 C CB  . ASP   C 114 ? 0.1751 0.1484 0.1454 -0.0222 0.0028  0.0057  128 ASP   C CB  
2722 C CG  . ASP   C 114 ? 0.1989 0.1506 0.1334 -0.0134 -0.0003 0.0141  128 ASP   C CG  
2723 O OD1 . ASP   C 114 ? 0.2055 0.1679 0.1698 -0.0169 -0.0060 0.0287  128 ASP   C OD1 
2724 O OD2 . ASP   C 114 ? 0.2066 0.1415 0.1386 -0.0097 0.0077  0.0244  128 ASP   C OD2 
2725 N N   . THR   C 115 ? 0.1665 0.1494 0.1627 -0.0521 0.0101  0.0085  129 THR   C N   
2726 C CA  A THR   C 115 ? 0.1892 0.1667 0.1672 -0.0579 0.0172  0.0111  129 THR   C CA  
2727 C CA  B THR   C 115 ? 0.1916 0.1567 0.1680 -0.0515 0.0220  0.0179  129 THR   C CA  
2728 C C   . THR   C 115 ? 0.2008 0.1661 0.1549 -0.0349 0.0162  0.0238  129 THR   C C   
2729 O O   . THR   C 115 ? 0.2197 0.1727 0.1601 -0.0215 0.0136  0.0293  129 THR   C O   
2730 C CB  A THR   C 115 ? 0.2234 0.2057 0.1968 -0.0516 0.0275  -0.0026 129 THR   C CB  
2731 C CB  B THR   C 115 ? 0.1964 0.1574 0.1846 -0.0581 0.0344  0.0222  129 THR   C CB  
2732 O OG1 A THR   C 115 ? 0.2235 0.2106 0.2048 -0.0411 0.0419  -0.0070 129 THR   C OG1 
2733 O OG1 B THR   C 115 ? 0.2081 0.1639 0.1904 -0.0556 0.0415  0.0243  129 THR   C OG1 
2734 C CG2 A THR   C 115 ? 0.2623 0.2284 0.2058 -0.0465 0.0493  0.0007  129 THR   C CG2 
2735 C CG2 B THR   C 115 ? 0.1909 0.1505 0.1940 -0.0669 0.0449  0.0229  129 THR   C CG2 
2736 N N   . PHE   C 116 ? 0.1815 0.1716 0.1542 -0.0374 0.0125  0.0091  130 PHE   C N   
2737 C CA  . PHE   C 116 ? 0.1915 0.1568 0.1581 -0.0548 0.0233  0.0107  130 PHE   C CA  
2738 C C   . PHE   C 116 ? 0.2068 0.1667 0.1689 -0.0460 0.0211  0.0226  130 PHE   C C   
2739 O O   . PHE   C 116 ? 0.1936 0.1694 0.1678 -0.0350 0.0173  0.0289  130 PHE   C O   
2740 C CB  . PHE   C 116 ? 0.2030 0.1592 0.1523 -0.0503 0.0321  0.0126  130 PHE   C CB  
2741 C CG  . PHE   C 116 ? 0.1968 0.1454 0.1460 -0.0284 0.0196  0.0189  130 PHE   C CG  
2742 C CD1 . PHE   C 116 ? 0.1992 0.1480 0.1414 -0.0435 0.0214  0.0071  130 PHE   C CD1 
2743 C CD2 . PHE   C 116 ? 0.2037 0.1394 0.1379 -0.0331 0.0238  0.0153  130 PHE   C CD2 
2744 C CE1 . PHE   C 116 ? 0.2093 0.1453 0.1223 -0.0308 0.0325  -0.0018 130 PHE   C CE1 
2745 C CE2 . PHE   C 116 ? 0.2218 0.1402 0.1618 -0.0304 0.0186  0.0230  130 PHE   C CE2 
2746 C CZ  . PHE   C 116 ? 0.2073 0.1400 0.1374 -0.0288 0.0127  0.0031  130 PHE   C CZ  
2747 N N   . THR   C 117 ? 0.2352 0.1666 0.1738 -0.0670 0.0370  0.0345  131 THR   C N   
2748 C CA  . THR   C 117 ? 0.2395 0.1854 0.1778 -0.0564 0.0333  0.0434  131 THR   C CA  
2749 C C   . THR   C 117 ? 0.2205 0.1864 0.2138 -0.0646 0.0157  0.0419  131 THR   C C   
2750 O O   . THR   C 117 ? 0.2075 0.1816 0.2018 -0.0733 0.0097  0.0372  131 THR   C O   
2751 C CB  . THR   C 117 ? 0.2938 0.2197 0.1896 -0.0181 0.0310  0.0419  131 THR   C CB  
2752 O OG1 . THR   C 117 ? 0.3421 0.2571 0.2043 0.0330  0.0159  0.0538  131 THR   C OG1 
2753 C CG2 . THR   C 117 ? 0.2997 0.2223 0.2105 -0.0097 0.0464  0.0341  131 THR   C CG2 
2754 N N   . LYS   C 118 ? 0.2226 0.1968 0.2461 -0.0667 -0.0024 0.0342  132 LYS   C N   
2755 C CA  . LYS   C 118 ? 0.2458 0.2090 0.2786 -0.0582 -0.0283 0.0316  132 LYS   C CA  
2756 C C   . LYS   C 118 ? 0.2464 0.2051 0.2570 -0.0549 -0.0110 0.0397  132 LYS   C C   
2757 O O   . LYS   C 118 ? 0.2831 0.2019 0.2924 -0.0420 0.0006  0.0300  132 LYS   C O   
2758 C CB  . LYS   C 118 ? 0.2904 0.2312 0.3177 -0.0315 -0.0310 0.0269  132 LYS   C CB  
2759 C CG  . LYS   C 118 ? 0.3612 0.2617 0.3369 -0.0152 -0.0084 0.0278  132 LYS   C CG  
2760 C CD  . LYS   C 118 ? 0.4419 0.2960 0.3837 -0.0017 0.0387  0.0396  132 LYS   C CD  
2761 C CE  . LYS   C 118 ? 0.5118 0.3180 0.4239 -0.0093 0.0642  0.0341  132 LYS   C CE  
2762 N NZ  . LYS   C 118 ? 0.5612 0.3321 0.4570 -0.0200 0.0918  0.0265  132 LYS   C NZ  
2763 N N   . VAL   C 119 ? 0.2588 0.2200 0.2421 -0.0496 -0.0098 0.0561  133 VAL   C N   
2764 C CA  . VAL   C 119 ? 0.2937 0.2460 0.2700 -0.0768 0.0112  0.0791  133 VAL   C CA  
2765 C C   . VAL   C 119 ? 0.3258 0.2546 0.2817 -0.0760 -0.0023 0.0773  133 VAL   C C   
2766 O O   . VAL   C 119 ? 0.3691 0.2541 0.2896 -0.0782 -0.0313 0.0770  133 VAL   C O   
2767 C CB  . VAL   C 119 ? 0.3404 0.2806 0.3249 -0.0875 0.0436  0.0804  133 VAL   C CB  
2768 C CG1 . VAL   C 119 ? 0.3745 0.3006 0.3620 -0.0701 0.0303  0.0778  133 VAL   C CG1 
2769 C CG2 . VAL   C 119 ? 0.3382 0.2909 0.3506 -0.0983 0.0742  0.0706  133 VAL   C CG2 
2770 N N   . LYS   C 120 ? 0.3388 0.2767 0.3074 -0.0711 0.0311  0.0579  134 LYS   C N   
2771 C CA  . LYS   C 120 ? 0.3758 0.3062 0.3211 -0.0408 0.0312  0.0573  134 LYS   C CA  
2772 C C   . LYS   C 120 ? 0.4189 0.3277 0.3376 -0.0714 0.0418  0.0636  134 LYS   C C   
2773 O O   . LYS   C 120 ? 0.4340 0.3432 0.3286 -0.0815 0.0502  0.0615  134 LYS   C O   
2774 C CB  . LYS   C 120 ? 0.3934 0.3220 0.3172 0.0025  0.0190  0.0416  134 LYS   C CB  
2775 C CG  . LYS   C 120 ? 0.4146 0.3348 0.3464 0.0398  0.0361  0.0241  134 LYS   C CG  
2776 C CD  . LYS   C 120 ? 0.4507 0.3442 0.3837 0.0629  0.0520  0.0188  134 LYS   C CD  
2777 C CE  . LYS   C 120 ? 0.4757 0.3487 0.4222 0.0814  0.0643  0.0106  134 LYS   C CE  
2778 N NZ  . LYS   C 120 ? 0.4946 0.3535 0.4444 0.0905  0.0760  0.0088  134 LYS   C NZ  
2779 N N   . PRO   C 121 ? 0.4621 0.3369 0.3477 -0.0794 0.0541  0.0609  135 PRO   C N   
2780 C CA  . PRO   C 121 ? 0.4965 0.3535 0.3666 -0.0599 0.0493  0.0519  135 PRO   C CA  
2781 C C   . PRO   C 121 ? 0.5319 0.3758 0.3848 -0.0277 0.0415  0.0388  135 PRO   C C   
2782 O O   . PRO   C 121 ? 0.5197 0.3829 0.3851 -0.0138 0.0018  0.0485  135 PRO   C O   
2783 C CB  . PRO   C 121 ? 0.4843 0.3470 0.3584 -0.0749 0.0673  0.0502  135 PRO   C CB  
2784 C CG  . PRO   C 121 ? 0.4786 0.3431 0.3492 -0.0802 0.0657  0.0463  135 PRO   C CG  
2785 C CD  . PRO   C 121 ? 0.4718 0.3365 0.3387 -0.0849 0.0651  0.0521  135 PRO   C CD  
2786 O OXT . PRO   C 121 ? 0.5642 0.3859 0.4108 -0.0179 0.0604  0.0325  135 PRO   C OXT 
2787 N N   . ALA   D 1   ? 0.4175 0.4007 0.2770 -0.0223 0.0246  -0.0279 15  ALA   D N   
2788 C CA  . ALA   D 1   ? 0.3822 0.3927 0.2655 -0.0211 -0.0115 -0.0079 15  ALA   D CA  
2789 C C   . ALA   D 1   ? 0.3394 0.3825 0.2422 -0.0065 -0.0377 0.0038  15  ALA   D C   
2790 O O   . ALA   D 1   ? 0.3483 0.3949 0.2398 0.0150  -0.0036 -0.0019 15  ALA   D O   
2791 C CB  . ALA   D 1   ? 0.3916 0.3979 0.2633 -0.0303 -0.0213 -0.0009 15  ALA   D CB  
2792 N N   . GLY   D 2   ? 0.3255 0.3573 0.2373 0.0021  -0.0592 0.0302  16  GLY   D N   
2793 C CA  . GLY   D 2   ? 0.3048 0.3229 0.2098 -0.0067 -0.0581 0.0415  16  GLY   D CA  
2794 C C   . GLY   D 2   ? 0.2506 0.2977 0.1795 -0.0282 -0.0434 0.0304  16  GLY   D C   
2795 O O   . GLY   D 2   ? 0.2840 0.2982 0.1886 -0.0461 -0.0265 0.0341  16  GLY   D O   
2796 N N   . ILE   D 3   ? 0.2181 0.2834 0.1662 -0.0289 -0.0226 0.0283  17  ILE   D N   
2797 C CA  . ILE   D 3   ? 0.1900 0.2579 0.1410 -0.0337 -0.0177 0.0258  17  ILE   D CA  
2798 C C   . ILE   D 3   ? 0.1729 0.2468 0.1198 -0.0401 -0.0136 0.0162  17  ILE   D C   
2799 O O   . ILE   D 3   ? 0.1634 0.2365 0.1448 -0.0476 -0.0204 0.0057  17  ILE   D O   
2800 C CB  . ILE   D 3   ? 0.1995 0.2397 0.1555 -0.0292 0.0139  0.0180  17  ILE   D CB  
2801 C CG1 . ILE   D 3   ? 0.1858 0.2391 0.1944 -0.0383 0.0214  0.0189  17  ILE   D CG1 
2802 C CG2 . ILE   D 3   ? 0.2001 0.2422 0.1577 -0.0354 -0.0047 0.0310  17  ILE   D CG2 
2803 C CD1 . ILE   D 3   ? 0.1974 0.2365 0.2133 -0.0370 0.0381  0.0257  17  ILE   D CD1 
2804 N N   . THR   D 4   ? 0.1701 0.2537 0.1232 -0.0391 0.0027  0.0124  18  THR   D N   
2805 C CA  . THR   D 4   ? 0.1841 0.2631 0.1142 -0.0557 0.0055  0.0041  18  THR   D CA  
2806 C C   . THR   D 4   ? 0.1991 0.2590 0.1274 -0.0682 -0.0093 0.0211  18  THR   D C   
2807 O O   . THR   D 4   ? 0.2194 0.2691 0.1351 -0.0717 -0.0120 0.0326  18  THR   D O   
2808 C CB  . THR   D 4   ? 0.1908 0.2861 0.1297 -0.0531 0.0010  0.0072  18  THR   D CB  
2809 O OG1 . THR   D 4   ? 0.1899 0.2979 0.1367 -0.0705 -0.0045 0.0213  18  THR   D OG1 
2810 C CG2 . THR   D 4   ? 0.2321 0.2959 0.1349 -0.0487 -0.0058 -0.0119 18  THR   D CG2 
2811 N N   . GLY   D 5   ? 0.1779 0.2556 0.1255 -0.0697 -0.0142 0.0025  19  GLY   D N   
2812 C CA  . GLY   D 5   ? 0.1633 0.2491 0.1188 -0.0619 0.0111  0.0146  19  GLY   D CA  
2813 C C   . GLY   D 5   ? 0.1602 0.2458 0.1190 -0.0517 0.0158  0.0064  19  GLY   D C   
2814 O O   . GLY   D 5   ? 0.1726 0.2422 0.1379 -0.0368 0.0005  0.0183  19  GLY   D O   
2815 N N   . THR   D 6   ? 0.1654 0.2558 0.1089 -0.0478 0.0073  0.0178  20  THR   D N   
2816 C CA  . THR   D 6   ? 0.1698 0.2562 0.1204 -0.0341 0.0142  -0.0026 20  THR   D CA  
2817 C C   . THR   D 6   ? 0.1839 0.2212 0.1004 -0.0281 0.0121  0.0309  20  THR   D C   
2818 O O   . THR   D 6   ? 0.2308 0.2234 0.1247 -0.0123 0.0169  0.0460  20  THR   D O   
2819 C CB  . THR   D 6   ? 0.1721 0.2954 0.1316 -0.0402 0.0063  -0.0375 20  THR   D CB  
2820 O OG1 . THR   D 6   ? 0.1998 0.3146 0.1677 -0.0416 0.0222  -0.0728 20  THR   D OG1 
2821 C CG2 . THR   D 6   ? 0.1823 0.3043 0.1532 -0.0244 0.0151  -0.0458 20  THR   D CG2 
2822 N N   . TRP   D 7   ? 0.1725 0.2074 0.1006 -0.0354 -0.0092 0.0153  21  TRP   D N   
2823 C CA  . TRP   D 7   ? 0.1664 0.1978 0.1106 -0.0349 -0.0046 0.0082  21  TRP   D CA  
2824 C C   . TRP   D 7   ? 0.1681 0.1870 0.1215 -0.0404 -0.0188 0.0198  21  TRP   D C   
2825 O O   . TRP   D 7   ? 0.1742 0.1910 0.1457 -0.0266 -0.0101 0.0193  21  TRP   D O   
2826 C CB  . TRP   D 7   ? 0.1625 0.1992 0.1486 -0.0167 -0.0111 0.0048  21  TRP   D CB  
2827 C CG  . TRP   D 7   ? 0.1611 0.1945 0.1538 -0.0344 0.0004  0.0073  21  TRP   D CG  
2828 C CD1 . TRP   D 7   ? 0.1648 0.2024 0.1591 -0.0133 -0.0206 0.0146  21  TRP   D CD1 
2829 C CD2 . TRP   D 7   ? 0.1604 0.1962 0.1498 -0.0310 0.0096  0.0154  21  TRP   D CD2 
2830 N NE1 . TRP   D 7   ? 0.1798 0.2070 0.1693 -0.0146 -0.0302 0.0170  21  TRP   D NE1 
2831 C CE2 . TRP   D 7   ? 0.1703 0.1968 0.1702 -0.0145 -0.0079 0.0160  21  TRP   D CE2 
2832 C CE3 . TRP   D 7   ? 0.1709 0.1955 0.1405 -0.0148 0.0018  0.0210  21  TRP   D CE3 
2833 C CZ2 . TRP   D 7   ? 0.1759 0.2001 0.1652 -0.0164 -0.0068 0.0185  21  TRP   D CZ2 
2834 C CZ3 . TRP   D 7   ? 0.1783 0.2065 0.1506 -0.0009 0.0190  0.0288  21  TRP   D CZ3 
2835 C CH2 . TRP   D 7   ? 0.1992 0.2118 0.1574 -0.0137 0.0191  0.0293  21  TRP   D CH2 
2836 N N   . TYR   D 8   ? 0.1694 0.1954 0.1165 -0.0466 -0.0095 0.0030  22  TYR   D N   
2837 C CA  . TYR   D 8   ? 0.1767 0.2143 0.1155 -0.0359 0.0028  -0.0059 22  TYR   D CA  
2838 C C   . TYR   D 8   ? 0.1572 0.2200 0.1193 -0.0314 -0.0022 -0.0028 22  TYR   D C   
2839 O O   . TYR   D 8   ? 0.1772 0.2001 0.1344 -0.0240 0.0048  0.0031  22  TYR   D O   
2840 C CB  . TYR   D 8   ? 0.1825 0.2306 0.1267 -0.0373 0.0108  0.0037  22  TYR   D CB  
2841 C CG  . TYR   D 8   ? 0.1643 0.2330 0.1322 -0.0207 0.0056  0.0042  22  TYR   D CG  
2842 C CD1 . TYR   D 8   ? 0.1645 0.2611 0.1700 0.0006  0.0144  0.0077  22  TYR   D CD1 
2843 C CD2 . TYR   D 8   ? 0.1732 0.2344 0.1230 -0.0042 -0.0007 0.0133  22  TYR   D CD2 
2844 C CE1 . TYR   D 8   ? 0.1733 0.2766 0.1589 0.0164  0.0024  0.0166  22  TYR   D CE1 
2845 C CE2 . TYR   D 8   ? 0.1629 0.2488 0.1373 0.0119  -0.0010 0.0031  22  TYR   D CE2 
2846 C CZ  . TYR   D 8   ? 0.1571 0.2673 0.1374 0.0095  0.0058  0.0061  22  TYR   D CZ  
2847 O OH  . TYR   D 8   ? 0.1987 0.2680 0.1475 0.0197  0.0148  -0.0084 22  TYR   D OH  
2848 N N   . ASN   D 9   ? 0.1847 0.2384 0.1173 -0.0253 -0.0289 -0.0067 23  ASN   D N   
2849 C CA  . ASN   D 9   ? 0.2406 0.2531 0.1234 -0.0174 -0.0201 0.0021  23  ASN   D CA  
2850 C C   . ASN   D 9   ? 0.2436 0.2578 0.1707 -0.0294 0.0125  -0.0051 23  ASN   D C   
2851 O O   . ASN   D 9   ? 0.2342 0.2677 0.2388 -0.0468 0.0272  -0.0172 23  ASN   D O   
2852 C CB  . ASN   D 9   ? 0.2844 0.2563 0.1294 0.0052  -0.0088 0.0005  23  ASN   D CB  
2853 C CG  . ASN   D 9   ? 0.3277 0.2556 0.1545 0.0225  0.0121  -0.0165 23  ASN   D CG  
2854 O OD1 . ASN   D 9   ? 0.2709 0.2527 0.1848 0.0331  -0.0624 -0.0254 23  ASN   D OD1 
2855 N ND2 . ASN   D 9   ? 0.4028 0.2728 0.1875 0.0282  0.0450  0.0052  23  ASN   D ND2 
2856 N N   . GLN   D 10  ? 0.2706 0.2663 0.1793 -0.0484 0.0147  -0.0304 24  GLN   D N   
2857 C CA  . GLN   D 10  ? 0.3008 0.2944 0.2365 -0.0590 0.0180  -0.0466 24  GLN   D CA  
2858 C C   . GLN   D 10  ? 0.3272 0.3164 0.3319 -0.0609 0.0060  -0.0787 24  GLN   D C   
2859 O O   . GLN   D 10  ? 0.3337 0.3341 0.3951 -0.0817 0.0201  -0.0838 24  GLN   D O   
2860 C CB  . GLN   D 10  ? 0.2995 0.2873 0.2049 -0.0586 0.0152  -0.0376 24  GLN   D CB  
2861 C CG  . GLN   D 10  ? 0.2808 0.2844 0.1959 -0.0492 0.0154  -0.0091 24  GLN   D CG  
2862 C CD  . GLN   D 10  ? 0.2657 0.2837 0.1702 -0.0375 0.0020  0.0054  24  GLN   D CD  
2863 O OE1 . GLN   D 10  ? 0.2399 0.2879 0.1626 -0.0402 -0.0057 -0.0325 24  GLN   D OE1 
2864 N NE2 . GLN   D 10  ? 0.2993 0.2832 0.2067 -0.0210 0.0048  0.0134  24  GLN   D NE2 
2865 N N   . LEU   D 11  ? 0.3438 0.3180 0.3618 -0.0343 -0.0140 -0.0905 25  LEU   D N   
2866 C CA  . LEU   D 11  ? 0.3747 0.3227 0.3956 -0.0187 0.0220  -0.0876 25  LEU   D CA  
2867 C C   . LEU   D 11  ? 0.3853 0.3137 0.4254 -0.0258 0.0547  -0.0759 25  LEU   D C   
2868 O O   . LEU   D 11  ? 0.3675 0.3234 0.4695 -0.0387 0.0577  -0.0575 25  LEU   D O   
2869 C CB  . LEU   D 11  ? 0.4042 0.3377 0.4010 -0.0023 0.0163  -0.0781 25  LEU   D CB  
2870 C CG  . LEU   D 11  ? 0.4413 0.3524 0.4257 -0.0119 0.0274  -0.0731 25  LEU   D CG  
2871 C CD1 . LEU   D 11  ? 0.4577 0.3622 0.4313 -0.0141 0.0391  -0.0607 25  LEU   D CD1 
2872 C CD2 . LEU   D 11  ? 0.4539 0.3588 0.4300 -0.0085 0.0295  -0.0751 25  LEU   D CD2 
2873 N N   . GLY   D 12  ? 0.3893 0.3004 0.4026 -0.0355 0.0811  -0.0791 26  GLY   D N   
2874 C CA  . GLY   D 12  ? 0.3797 0.2974 0.3729 -0.0285 0.0846  -0.0680 26  GLY   D CA  
2875 C C   . GLY   D 12  ? 0.3247 0.2856 0.3106 -0.0253 0.0429  -0.0545 26  GLY   D C   
2876 O O   . GLY   D 12  ? 0.3337 0.2988 0.3323 -0.0060 0.0329  -0.0286 26  GLY   D O   
2877 N N   . SER   D 13  ? 0.2582 0.2643 0.2247 -0.0291 0.0072  -0.0426 27  SER   D N   
2878 C CA  . SER   D 13  ? 0.2466 0.2609 0.1670 -0.0146 -0.0144 -0.0276 27  SER   D CA  
2879 C C   . SER   D 13  ? 0.2216 0.2533 0.1563 0.0202  -0.0206 -0.0028 27  SER   D C   
2880 O O   . SER   D 13  ? 0.2880 0.2569 0.1638 0.0523  -0.0052 -0.0069 27  SER   D O   
2881 C CB  . SER   D 13  ? 0.2692 0.2783 0.1463 -0.0177 -0.0346 -0.0129 27  SER   D CB  
2882 O OG  . SER   D 13  ? 0.2887 0.3055 0.1756 -0.0256 -0.0520 -0.0159 27  SER   D OG  
2883 N N   . THR   D 14  ? 0.1850 0.2502 0.1531 0.0203  -0.0390 -0.0101 28  THR   D N   
2884 C CA  . THR   D 14  ? 0.1873 0.2713 0.1496 -0.0044 -0.0293 -0.0133 28  THR   D CA  
2885 C C   . THR   D 14  ? 0.1900 0.2377 0.1823 -0.0082 -0.0428 -0.0005 28  THR   D C   
2886 O O   . THR   D 14  ? 0.2192 0.2474 0.2423 0.0316  -0.0426 0.0094  28  THR   D O   
2887 C CB  . THR   D 14  ? 0.2170 0.3190 0.1607 -0.0283 -0.0155 -0.0291 28  THR   D CB  
2888 O OG1 . THR   D 14  ? 0.2246 0.3371 0.2045 -0.0301 0.0094  -0.0178 28  THR   D OG1 
2889 C CG2 . THR   D 14  ? 0.2604 0.3407 0.1494 -0.0394 -0.0160 -0.0255 28  THR   D CG2 
2890 N N   A PHE   D 15  ? 0.1712 0.2219 0.1727 -0.0403 -0.0639 -0.0033 29  PHE   D N   
2891 N N   B PHE   D 15  ? 0.2061 0.2292 0.2044 -0.0279 -0.0479 0.0018  29  PHE   D N   
2892 C CA  A PHE   D 15  ? 0.2053 0.2263 0.2097 -0.0207 -0.0824 0.0060  29  PHE   D CA  
2893 C CA  B PHE   D 15  ? 0.2191 0.2235 0.2337 -0.0325 -0.0365 0.0066  29  PHE   D CA  
2894 C C   A PHE   D 15  ? 0.2205 0.2091 0.2027 -0.0208 -0.0906 0.0052  29  PHE   D C   
2895 C C   B PHE   D 15  ? 0.2040 0.2176 0.2487 -0.0202 -0.0302 -0.0021 29  PHE   D C   
2896 O O   A PHE   D 15  ? 0.2941 0.1913 0.1770 -0.0231 -0.1122 0.0172  29  PHE   D O   
2897 O O   B PHE   D 15  ? 0.2195 0.2158 0.2705 -0.0155 -0.0088 0.0036  29  PHE   D O   
2898 C CB  A PHE   D 15  ? 0.2160 0.2281 0.2167 0.0002  -0.0652 0.0370  29  PHE   D CB  
2899 C CB  B PHE   D 15  ? 0.2467 0.2242 0.2420 -0.0506 -0.0076 0.0236  29  PHE   D CB  
2900 C CG  A PHE   D 15  ? 0.2306 0.2218 0.1862 -0.0168 -0.0269 0.0416  29  PHE   D CG  
2901 C CG  B PHE   D 15  ? 0.2582 0.2180 0.2319 -0.0636 0.0008  0.0298  29  PHE   D CG  
2902 C CD1 A PHE   D 15  ? 0.2218 0.2286 0.1591 -0.0312 0.0217  0.0307  29  PHE   D CD1 
2903 C CD1 B PHE   D 15  ? 0.2608 0.2134 0.2289 -0.0702 -0.0031 0.0257  29  PHE   D CD1 
2904 C CD2 A PHE   D 15  ? 0.1826 0.2194 0.1947 -0.0356 0.0058  0.0513  29  PHE   D CD2 
2905 C CD2 B PHE   D 15  ? 0.2663 0.2118 0.2257 -0.0740 0.0114  0.0404  29  PHE   D CD2 
2906 C CE1 A PHE   D 15  ? 0.2344 0.2310 0.1743 -0.0008 0.0162  0.0157  29  PHE   D CE1 
2907 C CE1 B PHE   D 15  ? 0.2764 0.2111 0.2217 -0.0665 0.0050  0.0306  29  PHE   D CE1 
2908 C CE2 A PHE   D 15  ? 0.2168 0.2285 0.1923 0.0021  0.0075  0.0495  29  PHE   D CE2 
2909 C CE2 B PHE   D 15  ? 0.2829 0.2145 0.2263 -0.0693 0.0294  0.0448  29  PHE   D CE2 
2910 C CZ  A PHE   D 15  ? 0.2354 0.2251 0.1793 -0.0137 0.0208  0.0210  29  PHE   D CZ  
2911 C CZ  B PHE   D 15  ? 0.2862 0.2110 0.2246 -0.0706 0.0244  0.0417  29  PHE   D CZ  
2912 N N   . ILE   D 16  ? 0.1726 0.2194 0.2502 -0.0124 -0.0457 -0.0177 30  ILE   D N   
2913 C CA  . ILE   D 16  ? 0.1922 0.2246 0.2403 -0.0228 0.0486  -0.0278 30  ILE   D CA  
2914 C C   . ILE   D 16  ? 0.1639 0.2238 0.2258 -0.0587 0.0191  -0.0091 30  ILE   D C   
2915 O O   . ILE   D 16  ? 0.1701 0.2394 0.2949 -0.0634 -0.0310 0.0167  30  ILE   D O   
2916 C CB  . ILE   D 16  ? 0.2502 0.2538 0.2741 -0.0239 0.0492  -0.0549 30  ILE   D CB  
2917 C CG1 . ILE   D 16  ? 0.2501 0.2631 0.3167 -0.0049 0.0472  -0.0564 30  ILE   D CG1 
2918 C CG2 . ILE   D 16  ? 0.2775 0.2771 0.2431 -0.0192 0.0471  -0.0695 30  ILE   D CG2 
2919 C CD1 . ILE   D 16  ? 0.2752 0.2694 0.3605 0.0013  0.0571  -0.0585 30  ILE   D CD1 
2920 N N   . VAL   D 17  ? 0.1648 0.2094 0.1586 -0.0405 0.0335  -0.0029 31  VAL   D N   
2921 C CA  . VAL   D 17  ? 0.1614 0.2112 0.1576 -0.0251 0.0234  0.0058  31  VAL   D CA  
2922 C C   . VAL   D 17  ? 0.1694 0.2162 0.1620 -0.0402 0.0202  -0.0029 31  VAL   D C   
2923 O O   . VAL   D 17  ? 0.1842 0.2260 0.1581 -0.0489 0.0138  0.0052  31  VAL   D O   
2924 C CB  . VAL   D 17  ? 0.1696 0.2061 0.1698 -0.0060 0.0257  0.0232  31  VAL   D CB  
2925 C CG1 . VAL   D 17  ? 0.1795 0.1965 0.1691 0.0083  0.0120  0.0301  31  VAL   D CG1 
2926 C CG2 . VAL   D 17  ? 0.1520 0.2187 0.1734 -0.0173 0.0212  0.0205  31  VAL   D CG2 
2927 N N   . THR   D 18  ? 0.1778 0.2254 0.1758 -0.0453 0.0139  -0.0183 32  THR   D N   
2928 C CA  . THR   D 18  ? 0.1949 0.2352 0.1684 -0.0672 0.0262  -0.0291 32  THR   D CA  
2929 C C   . THR   D 18  ? 0.1633 0.2251 0.1444 -0.0672 0.0094  -0.0067 32  THR   D C   
2930 O O   . THR   D 18  ? 0.1766 0.2221 0.1569 -0.0530 0.0149  -0.0144 32  THR   D O   
2931 C CB  . THR   D 18  ? 0.2318 0.2619 0.2206 -0.0766 0.0379  -0.0542 32  THR   D CB  
2932 O OG1 . THR   D 18  ? 0.2683 0.2849 0.2684 -0.0534 0.0856  -0.0523 32  THR   D OG1 
2933 C CG2 . THR   D 18  ? 0.2968 0.2721 0.2167 -0.0758 0.0121  -0.0585 32  THR   D CG2 
2934 N N   . ALA   D 19  ? 0.1727 0.2378 0.1416 -0.0473 0.0021  0.0065  33  ALA   D N   
2935 C CA  . ALA   D 19  ? 0.1882 0.2427 0.1458 -0.0374 -0.0155 0.0186  33  ALA   D CA  
2936 C C   . ALA   D 19  ? 0.1922 0.2693 0.1141 -0.0471 -0.0224 0.0269  33  ALA   D C   
2937 O O   . ALA   D 19  ? 0.2260 0.2864 0.1563 -0.0408 -0.0228 0.0323  33  ALA   D O   
2938 C CB  . ALA   D 19  ? 0.2063 0.2291 0.1553 -0.0338 0.0032  0.0047  33  ALA   D CB  
2939 N N   . GLY   D 20  ? 0.1769 0.2767 0.1320 -0.0491 -0.0138 0.0098  34  GLY   D N   
2940 C CA  . GLY   D 20  ? 0.1782 0.3015 0.1601 -0.0618 -0.0274 0.0003  34  GLY   D CA  
2941 C C   . GLY   D 20  ? 0.2050 0.3248 0.1470 -0.0605 -0.0319 0.0064  34  GLY   D C   
2942 O O   . GLY   D 20  ? 0.2118 0.3053 0.1591 -0.0514 0.0000  -0.0023 34  GLY   D O   
2943 N N   . ALA   D 21  ? 0.2187 0.3640 0.1556 -0.0756 -0.0459 0.0195  35  ALA   D N   
2944 C CA  . ALA   D 21  ? 0.2438 0.4083 0.1472 -0.0680 -0.0594 0.0119  35  ALA   D CA  
2945 C C   . ALA   D 21  ? 0.2757 0.4394 0.1760 -0.0626 -0.0419 0.0118  35  ALA   D C   
2946 O O   . ALA   D 21  ? 0.2959 0.4653 0.2130 -0.0373 -0.0394 0.0089  35  ALA   D O   
2947 C CB  . ALA   D 21  ? 0.2567 0.4187 0.1614 -0.0667 -0.0647 -0.0031 35  ALA   D CB  
2948 N N   . ASP   D 22  ? 0.2645 0.4340 0.1475 -0.1192 -0.0492 0.0145  36  ASP   D N   
2949 C CA  . ASP   D 22  ? 0.3034 0.4331 0.1561 -0.1174 -0.0429 0.0108  36  ASP   D CA  
2950 C C   . ASP   D 22  ? 0.2402 0.3986 0.1461 -0.1039 -0.0335 0.0139  36  ASP   D C   
2951 O O   . ASP   D 22  ? 0.2575 0.4117 0.1724 -0.1401 -0.0154 0.0109  36  ASP   D O   
2952 C CB  . ASP   D 22  ? 0.4086 0.4588 0.2195 -0.1007 -0.0438 0.0124  36  ASP   D CB  
2953 C CG  . ASP   D 22  ? 0.4577 0.4827 0.2933 -0.0893 -0.0652 0.0229  36  ASP   D CG  
2954 O OD1 . ASP   D 22  ? 0.4298 0.4974 0.3193 -0.0876 -0.1174 0.0274  36  ASP   D OD1 
2955 O OD2 . ASP   D 22  ? 0.4946 0.4916 0.3331 -0.0991 -0.0584 0.0137  36  ASP   D OD2 
2956 N N   . GLY   D 23  ? 0.1458 0.3439 0.1478 -0.0505 -0.0363 0.0117  37  GLY   D N   
2957 C CA  . GLY   D 23  ? 0.1257 0.2879 0.1372 -0.0170 -0.0209 0.0070  37  GLY   D CA  
2958 C C   . GLY   D 23  ? 0.1382 0.2241 0.1217 -0.0196 -0.0186 -0.0037 37  GLY   D C   
2959 O O   . GLY   D 23  ? 0.1566 0.2013 0.1329 -0.0209 -0.0210 -0.0133 37  GLY   D O   
2960 N N   . ALA   D 24  ? 0.1392 0.2123 0.1299 -0.0144 -0.0128 -0.0088 38  ALA   D N   
2961 C CA  . ALA   D 24  ? 0.1359 0.2124 0.1493 -0.0205 -0.0042 -0.0090 38  ALA   D CA  
2962 C C   . ALA   D 24  ? 0.1332 0.2165 0.1163 -0.0286 -0.0152 -0.0068 38  ALA   D C   
2963 O O   . ALA   D 24  ? 0.1597 0.2400 0.1321 -0.0336 -0.0243 0.0130  38  ALA   D O   
2964 C CB  . ALA   D 24  ? 0.1986 0.2098 0.1648 -0.0274 0.0046  -0.0252 38  ALA   D CB  
2965 N N   . LEU   D 25  ? 0.1228 0.1967 0.1269 -0.0128 0.0070  -0.0169 39  LEU   D N   
2966 C CA  . LEU   D 25  ? 0.1221 0.1984 0.1316 -0.0167 -0.0010 -0.0176 39  LEU   D CA  
2967 C C   . LEU   D 25  ? 0.1371 0.2008 0.1221 -0.0070 -0.0060 -0.0227 39  LEU   D C   
2968 O O   . LEU   D 25  ? 0.1467 0.2065 0.1336 -0.0035 0.0010  -0.0282 39  LEU   D O   
2969 C CB  . LEU   D 25  ? 0.1476 0.1924 0.1279 -0.0109 0.0113  -0.0156 39  LEU   D CB  
2970 C CG  . LEU   D 25  ? 0.1582 0.1753 0.1221 -0.0088 -0.0105 -0.0064 39  LEU   D CG  
2971 C CD1 . LEU   D 25  ? 0.1725 0.1818 0.1250 -0.0231 -0.0074 -0.0201 39  LEU   D CD1 
2972 C CD2 . LEU   D 25  ? 0.1725 0.1879 0.1278 -0.0042 -0.0153 -0.0120 39  LEU   D CD2 
2973 N N   . THR   D 26  ? 0.1300 0.2022 0.1319 -0.0148 0.0010  -0.0215 40  THR   D N   
2974 C CA  . THR   D 26  ? 0.1381 0.2025 0.1404 -0.0285 0.0176  -0.0410 40  THR   D CA  
2975 C C   . THR   D 26  ? 0.1348 0.2179 0.1498 -0.0210 0.0231  -0.0199 40  THR   D C   
2976 O O   . THR   D 26  ? 0.1605 0.2185 0.2593 -0.0314 0.0293  0.0250  40  THR   D O   
2977 C CB  . THR   D 26  ? 0.1715 0.2247 0.1330 -0.0390 0.0154  -0.0474 40  THR   D CB  
2978 O OG1 . THR   D 26  ? 0.2330 0.2394 0.1561 -0.0373 0.0175  -0.0496 40  THR   D OG1 
2979 C CG2 . THR   D 26  ? 0.1750 0.2303 0.1659 -0.0402 0.0280  -0.0450 40  THR   D CG2 
2980 N N   . GLY   D 27  ? 0.1405 0.2331 0.1381 -0.0335 0.0028  -0.0106 41  GLY   D N   
2981 C CA  . GLY   D 27  ? 0.1383 0.2338 0.1341 -0.0412 -0.0099 -0.0218 41  GLY   D CA  
2982 C C   . GLY   D 27  ? 0.1412 0.2235 0.1288 -0.0212 0.0033  -0.0348 41  GLY   D C   
2983 O O   . GLY   D 27  ? 0.1361 0.2162 0.1313 -0.0119 0.0189  -0.0453 41  GLY   D O   
2984 N N   . THR   D 28  ? 0.1437 0.2131 0.1485 -0.0007 -0.0227 -0.0290 42  THR   D N   
2985 C CA  A THR   D 28  ? 0.1490 0.2108 0.1631 0.0073  -0.0212 -0.0293 42  THR   D CA  
2986 C CA  B THR   D 28  ? 0.1431 0.2136 0.1628 0.0053  -0.0188 -0.0347 42  THR   D CA  
2987 C C   . THR   D 28  ? 0.1545 0.2091 0.1570 0.0015  -0.0123 -0.0248 42  THR   D C   
2988 O O   . THR   D 28  ? 0.2028 0.2212 0.1850 -0.0074 -0.0408 -0.0059 42  THR   D O   
2989 C CB  A THR   D 28  ? 0.1686 0.2114 0.1893 0.0132  -0.0051 -0.0358 42  THR   D CB  
2990 C CB  B THR   D 28  ? 0.1714 0.2207 0.1910 0.0006  0.0028  -0.0434 42  THR   D CB  
2991 O OG1 A THR   D 28  ? 0.1857 0.2175 0.1876 0.0153  0.0004  -0.0353 42  THR   D OG1 
2992 O OG1 B THR   D 28  ? 0.2086 0.2314 0.1806 -0.0027 0.0174  -0.0351 42  THR   D OG1 
2993 C CG2 A THR   D 28  ? 0.1766 0.2072 0.2088 0.0137  0.0082  -0.0365 42  THR   D CG2 
2994 C CG2 B THR   D 28  ? 0.1751 0.2161 0.2237 -0.0081 -0.0031 -0.0439 42  THR   D CG2 
2995 N N   . TYR   D 29  ? 0.1302 0.2013 0.1380 0.0131  0.0065  -0.0440 43  TYR   D N   
2996 C CA  . TYR   D 29  ? 0.1441 0.1973 0.1492 -0.0022 -0.0088 -0.0450 43  TYR   D CA  
2997 C C   . TYR   D 29  ? 0.1140 0.2016 0.1639 0.0002  -0.0211 -0.0437 43  TYR   D C   
2998 O O   . TYR   D 29  ? 0.1486 0.1928 0.1889 0.0094  -0.0142 -0.0356 43  TYR   D O   
2999 C CB  . TYR   D 29  ? 0.1963 0.1996 0.1429 -0.0152 0.0136  -0.0412 43  TYR   D CB  
3000 C CG  . TYR   D 29  ? 0.1850 0.1956 0.1124 0.0070  -0.0030 -0.0224 43  TYR   D CG  
3001 C CD1 . TYR   D 29  ? 0.1842 0.2023 0.1216 0.0043  0.0244  -0.0202 43  TYR   D CD1 
3002 C CD2 . TYR   D 29  ? 0.2237 0.2076 0.1356 0.0097  -0.0082 -0.0231 43  TYR   D CD2 
3003 C CE1 . TYR   D 29  ? 0.1980 0.2029 0.1204 -0.0064 0.0048  -0.0174 43  TYR   D CE1 
3004 C CE2 . TYR   D 29  ? 0.2200 0.2052 0.1261 0.0143  0.0035  -0.0266 43  TYR   D CE2 
3005 C CZ  . TYR   D 29  ? 0.2010 0.1926 0.1299 -0.0033 0.0106  -0.0164 43  TYR   D CZ  
3006 O OH  . TYR   D 29  ? 0.2179 0.1921 0.1655 0.0194  0.0313  0.0000  43  TYR   D OH  
3007 N N   . GLU   D 30  ? 0.1294 0.2175 0.1703 -0.0073 -0.0190 -0.0365 44  GLU   D N   
3008 C CA  . GLU   D 30  ? 0.1317 0.2414 0.1850 -0.0050 0.0037  -0.0288 44  GLU   D CA  
3009 C C   . GLU   D 30  ? 0.1469 0.2445 0.2162 -0.0131 -0.0187 -0.0259 44  GLU   D C   
3010 O O   . GLU   D 30  ? 0.1802 0.2323 0.2011 0.0086  -0.0223 -0.0182 44  GLU   D O   
3011 C CB  . GLU   D 30  ? 0.2053 0.2721 0.2195 0.0034  0.0004  -0.0261 44  GLU   D CB  
3012 C CG  . GLU   D 30  ? 0.2634 0.2879 0.2383 -0.0044 0.0098  -0.0264 44  GLU   D CG  
3013 C CD  . GLU   D 30  ? 0.3342 0.3051 0.2681 -0.0200 0.0324  -0.0319 44  GLU   D CD  
3014 O OE1 . GLU   D 30  ? 0.3662 0.3172 0.2824 -0.0087 0.0157  -0.0505 44  GLU   D OE1 
3015 O OE2 . GLU   D 30  ? 0.4044 0.3271 0.2905 -0.0279 0.0428  -0.0394 44  GLU   D OE2 
3016 N N   . SER   D 31  ? 0.1520 0.2443 0.2368 -0.0228 -0.0258 -0.0334 45  SER   D N   
3017 C CA  . SER   D 31  ? 0.1871 0.2450 0.2726 -0.0263 -0.0428 -0.0172 45  SER   D CA  
3018 C C   . SER   D 31  ? 0.2019 0.2494 0.3369 -0.0207 -0.0182 0.0175  45  SER   D C   
3019 O O   . SER   D 31  ? 0.2154 0.2513 0.3340 -0.0039 0.0189  0.0307  45  SER   D O   
3020 C CB  . SER   D 31  ? 0.1817 0.2558 0.2889 0.0118  -0.0265 -0.0073 45  SER   D CB  
3021 O OG  . SER   D 31  ? 0.1892 0.2671 0.2911 -0.0022 -0.0081 0.0070  45  SER   D OG  
3022 N N   . ALA   D 32  ? 0.1996 0.2621 0.3861 -0.0199 0.0033  0.0412  46  ALA   D N   
3023 C CA  . ALA   D 32  ? 0.2362 0.2837 0.4146 -0.0053 0.0319  0.0552  46  ALA   D CA  
3024 C C   . ALA   D 32  ? 0.2812 0.3102 0.4474 0.0116  0.0799  0.0709  46  ALA   D C   
3025 O O   . ALA   D 32  ? 0.3100 0.3220 0.4546 0.0270  0.0925  0.0828  46  ALA   D O   
3026 C CB  . ALA   D 32  ? 0.2311 0.2823 0.4246 -0.0208 0.0251  0.0464  46  ALA   D CB  
3027 N N   . VAL   D 33  ? 0.2896 0.3254 0.4675 0.0203  0.0821  0.0527  47  VAL   D N   
3028 C CA  . VAL   D 33  ? 0.3198 0.3341 0.4651 0.0259  0.0784  0.0398  47  VAL   D CA  
3029 C C   . VAL   D 33  ? 0.3234 0.3362 0.4374 0.0372  0.0539  0.0421  47  VAL   D C   
3030 O O   . VAL   D 33  ? 0.3690 0.3497 0.4270 0.0295  0.0617  0.0507  47  VAL   D O   
3031 C CB  . VAL   D 33  ? 0.3254 0.3427 0.4761 0.0334  0.0618  0.0263  47  VAL   D CB  
3032 C CG1 . VAL   D 33  ? 0.3444 0.3459 0.4719 0.0339  0.0731  0.0243  47  VAL   D CG1 
3033 C CG2 . VAL   D 33  ? 0.3487 0.3495 0.4908 0.0447  0.0544  0.0237  47  VAL   D CG2 
3034 N N   . GLY   D 34  ? 0.2967 0.3231 0.4233 0.0516  0.0288  0.0290  48  GLY   D N   
3035 C CA  . GLY   D 34  ? 0.2964 0.3211 0.3954 0.0561  0.0259  0.0161  48  GLY   D CA  
3036 C C   . GLY   D 34  ? 0.2559 0.3138 0.3442 0.0576  0.0122  0.0164  48  GLY   D C   
3037 O O   . GLY   D 34  ? 0.2630 0.3314 0.3256 0.0513  -0.0025 0.0194  48  GLY   D O   
3038 N N   . ASN   D 35  ? 0.1984 0.2885 0.2927 0.0412  0.0032  0.0309  49  ASN   D N   
3039 C CA  . ASN   D 35  ? 0.1706 0.2746 0.2799 0.0255  0.0054  0.0194  49  ASN   D CA  
3040 C C   . ASN   D 35  ? 0.1634 0.2630 0.2521 0.0292  0.0035  0.0003  49  ASN   D C   
3041 O O   . ASN   D 35  ? 0.1618 0.2695 0.2302 0.0190  0.0105  -0.0113 49  ASN   D O   
3042 C CB  . ASN   D 35  ? 0.1622 0.2745 0.2901 0.0103  0.0229  0.0280  49  ASN   D CB  
3043 C CG  . ASN   D 35  ? 0.1628 0.2723 0.2832 0.0286  0.0140  0.0331  49  ASN   D CG  
3044 O OD1 . ASN   D 35  ? 0.1993 0.2675 0.3024 0.0410  0.0398  0.0170  49  ASN   D OD1 
3045 N ND2 . ASN   D 35  ? 0.1696 0.2663 0.2925 0.0144  0.0028  0.0313  49  ASN   D ND2 
3046 N N   . ALA   D 36  ? 0.2136 0.2518 0.2595 0.0178  0.0173  -0.0100 50  ALA   D N   
3047 C CA  . ALA   D 36  ? 0.2103 0.2438 0.2566 0.0153  0.0189  -0.0362 50  ALA   D CA  
3048 C C   . ALA   D 36  ? 0.1732 0.2315 0.2497 0.0234  0.0090  -0.0410 50  ALA   D C   
3049 O O   . ALA   D 36  ? 0.1748 0.2188 0.2640 0.0360  0.0060  -0.0534 50  ALA   D O   
3050 C CB  . ALA   D 36  ? 0.2609 0.2498 0.2796 -0.0071 0.0548  -0.0431 50  ALA   D CB  
3051 N N   . GLU   D 37  ? 0.1367 0.2329 0.2527 0.0159  -0.0040 -0.0395 51  GLU   D N   
3052 C CA  . GLU   D 37  ? 0.1332 0.2466 0.2765 0.0151  0.0007  -0.0330 51  GLU   D CA  
3053 C C   . GLU   D 37  ? 0.1209 0.2478 0.2500 0.0127  -0.0316 -0.0314 51  GLU   D C   
3054 O O   . GLU   D 37  ? 0.1593 0.2582 0.2692 -0.0024 -0.0272 -0.0307 51  GLU   D O   
3055 C CB  . GLU   D 37  ? 0.1311 0.2600 0.2866 0.0218  -0.0021 -0.0411 51  GLU   D CB  
3056 C CG  . GLU   D 37  ? 0.1530 0.2749 0.2771 0.0224  0.0028  -0.0410 51  GLU   D CG  
3057 C CD  . GLU   D 37  ? 0.1646 0.3027 0.2798 0.0010  0.0014  -0.0433 51  GLU   D CD  
3058 O OE1 . GLU   D 37  ? 0.1437 0.3196 0.2932 -0.0116 0.0070  -0.0238 51  GLU   D OE1 
3059 O OE2 . GLU   D 37  ? 0.1835 0.3124 0.2925 -0.0215 -0.0161 -0.0645 51  GLU   D OE2 
3060 N N   . SER   D 38  ? 0.1223 0.2440 0.2636 0.0133  -0.0152 -0.0229 52  SER   D N   
3061 C CA  . SER   D 38  ? 0.1477 0.2397 0.2559 0.0013  -0.0287 -0.0216 52  SER   D CA  
3062 C C   . SER   D 38  ? 0.1476 0.2343 0.2036 0.0189  -0.0350 -0.0183 52  SER   D C   
3063 O O   . SER   D 38  ? 0.1625 0.2526 0.1993 0.0354  -0.0237 -0.0404 52  SER   D O   
3064 C CB  . SER   D 38  ? 0.2137 0.2581 0.3067 -0.0055 0.0138  -0.0157 52  SER   D CB  
3065 O OG  . SER   D 38  ? 0.2249 0.2745 0.3786 -0.0095 0.0527  -0.0314 52  SER   D OG  
3066 N N   . ARG   D 39  ? 0.1264 0.2266 0.1896 -0.0053 -0.0126 -0.0294 53  ARG   D N   
3067 C CA  . ARG   D 39  ? 0.1244 0.2420 0.1706 -0.0016 -0.0061 -0.0378 53  ARG   D CA  
3068 C C   . ARG   D 39  ? 0.1328 0.2216 0.1657 0.0015  -0.0092 -0.0342 53  ARG   D C   
3069 O O   . ARG   D 39  ? 0.1611 0.2221 0.1572 0.0231  -0.0046 -0.0398 53  ARG   D O   
3070 C CB  . ARG   D 39  ? 0.1703 0.2819 0.1691 0.0127  0.0128  -0.0327 53  ARG   D CB  
3071 C CG  . ARG   D 39  ? 0.2260 0.3258 0.2102 0.0056  0.0100  -0.0361 53  ARG   D CG  
3072 C CD  . ARG   D 39  ? 0.3131 0.3671 0.2615 0.0029  0.0395  -0.0207 53  ARG   D CD  
3073 N NE  . ARG   D 39  ? 0.4073 0.4091 0.3111 0.0220  0.0719  -0.0170 53  ARG   D NE  
3074 C CZ  . ARG   D 39  ? 0.4716 0.4425 0.3639 0.0287  0.0600  0.0081  53  ARG   D CZ  
3075 N NH1 . ARG   D 39  ? 0.4732 0.4543 0.3809 0.0222  0.0297  0.0219  53  ARG   D NH1 
3076 N NH2 . ARG   D 39  ? 0.5110 0.4597 0.3927 0.0364  0.0575  0.0148  53  ARG   D NH2 
3077 N N   . TYR   D 40  ? 0.1116 0.2168 0.1520 0.0074  0.0060  -0.0378 54  TYR   D N   
3078 C CA  . TYR   D 40  ? 0.1338 0.2091 0.1354 0.0092  -0.0022 -0.0348 54  TYR   D CA  
3079 C C   . TYR   D 40  ? 0.1249 0.2211 0.1317 0.0064  -0.0007 -0.0242 54  TYR   D C   
3080 O O   . TYR   D 40  ? 0.1311 0.2272 0.1488 0.0118  0.0110  -0.0355 54  TYR   D O   
3081 C CB  . TYR   D 40  ? 0.1511 0.2141 0.1352 0.0208  -0.0131 -0.0469 54  TYR   D CB  
3082 C CG  . TYR   D 40  ? 0.1505 0.2094 0.1184 0.0171  -0.0190 -0.0490 54  TYR   D CG  
3083 C CD1 . TYR   D 40  ? 0.1529 0.2226 0.1480 0.0015  -0.0173 -0.0504 54  TYR   D CD1 
3084 C CD2 . TYR   D 40  ? 0.1601 0.2063 0.1338 0.0187  -0.0064 -0.0596 54  TYR   D CD2 
3085 C CE1 . TYR   D 40  ? 0.1603 0.2382 0.1441 0.0036  -0.0202 -0.0416 54  TYR   D CE1 
3086 C CE2 . TYR   D 40  ? 0.1634 0.2258 0.1566 0.0166  -0.0098 -0.0523 54  TYR   D CE2 
3087 C CZ  . TYR   D 40  ? 0.1494 0.2474 0.1665 0.0081  -0.0223 -0.0347 54  TYR   D CZ  
3088 O OH  . TYR   D 40  ? 0.1601 0.2781 0.1978 -0.0159 -0.0275 -0.0261 54  TYR   D OH  
3089 N N   . VAL   D 41  ? 0.1346 0.2314 0.1312 0.0001  0.0167  -0.0514 55  VAL   D N   
3090 C CA  . VAL   D 41  ? 0.1250 0.2389 0.1377 0.0010  0.0109  -0.0488 55  VAL   D CA  
3091 C C   . VAL   D 41  ? 0.1273 0.2551 0.1270 0.0146  0.0122  -0.0474 55  VAL   D C   
3092 O O   . VAL   D 41  ? 0.1408 0.2601 0.1267 0.0075  0.0099  -0.0468 55  VAL   D O   
3093 C CB  . VAL   D 41  ? 0.1479 0.2339 0.1587 -0.0055 -0.0009 -0.0514 55  VAL   D CB  
3094 C CG1 . VAL   D 41  ? 0.1486 0.2465 0.1775 -0.0007 0.0091  -0.0464 55  VAL   D CG1 
3095 C CG2 . VAL   D 41  ? 0.1766 0.2391 0.1588 -0.0100 0.0217  -0.0608 55  VAL   D CG2 
3096 N N   . LEU   D 42  ? 0.1279 0.2700 0.1374 0.0411  -0.0071 -0.0719 56  LEU   D N   
3097 C CA  . LEU   D 42  ? 0.1462 0.2839 0.1727 0.0399  0.0033  -0.0738 56  LEU   D CA  
3098 C C   . LEU   D 42  ? 0.1445 0.2883 0.1346 0.0368  -0.0053 -0.0754 56  LEU   D C   
3099 O O   . LEU   D 42  ? 0.1620 0.3158 0.1434 0.0463  0.0064  -0.0744 56  LEU   D O   
3100 C CB  . LEU   D 42  ? 0.1729 0.2762 0.1996 0.0352  -0.0236 -0.0334 56  LEU   D CB  
3101 C CG  . LEU   D 42  ? 0.1907 0.2713 0.1892 0.0153  0.0042  -0.0051 56  LEU   D CG  
3102 C CD1 . LEU   D 42  ? 0.1662 0.2790 0.1661 -0.0078 -0.0130 -0.0138 56  LEU   D CD1 
3103 C CD2 . LEU   D 42  ? 0.2047 0.2704 0.2268 0.0077  0.0415  -0.0107 56  LEU   D CD2 
3104 N N   . THR   D 43  ? 0.1522 0.2447 0.1394 0.0351  0.0016  -0.0654 57  THR   D N   
3105 C CA  A THR   D 43  ? 0.1393 0.2051 0.1430 0.0148  -0.0062 -0.0590 57  THR   D CA  
3106 C CA  B THR   D 43  ? 0.1635 0.2080 0.1235 0.0430  0.0046  -0.0386 57  THR   D CA  
3107 C C   . THR   D 43  ? 0.1327 0.1804 0.1149 0.0149  0.0035  -0.0451 57  THR   D C   
3108 O O   . THR   D 43  ? 0.1393 0.1712 0.1100 -0.0013 0.0047  -0.0209 57  THR   D O   
3109 C CB  A THR   D 43  ? 0.1926 0.1963 0.1824 0.0081  0.0096  -0.0566 57  THR   D CB  
3110 C CB  B THR   D 43  ? 0.2771 0.2127 0.1472 0.0969  0.0449  0.0053  57  THR   D CB  
3111 O OG1 A THR   D 43  ? 0.1889 0.1895 0.2090 -0.0141 0.0442  -0.0463 57  THR   D OG1 
3112 O OG1 B THR   D 43  ? 0.2868 0.2319 0.1974 0.0776  0.0282  -0.0074 57  THR   D OG1 
3113 C CG2 A THR   D 43  ? 0.2133 0.1973 0.1852 0.0019  -0.0165 -0.0681 57  THR   D CG2 
3114 C CG2 B THR   D 43  ? 0.3257 0.2136 0.1523 0.1294  0.0734  0.0214  57  THR   D CG2 
3115 N N   . GLY   D 44  ? 0.1230 0.1725 0.1436 0.0193  -0.0053 -0.0375 58  GLY   D N   
3116 C CA  . GLY   D 44  ? 0.1124 0.1744 0.1452 0.0134  -0.0116 -0.0420 58  GLY   D CA  
3117 C C   . GLY   D 44  ? 0.1172 0.1691 0.1189 0.0066  -0.0112 -0.0303 58  GLY   D C   
3118 O O   . GLY   D 44  ? 0.1427 0.1726 0.1085 -0.0140 -0.0033 -0.0188 58  GLY   D O   
3119 N N   . ARG   D 45  ? 0.1279 0.1564 0.1229 0.0146  -0.0097 -0.0177 59  ARG   D N   
3120 C CA  . ARG   D 45  ? 0.1318 0.1489 0.1350 -0.0006 -0.0055 -0.0015 59  ARG   D CA  
3121 C C   . ARG   D 45  ? 0.1233 0.1492 0.1073 -0.0167 -0.0255 0.0007  59  ARG   D C   
3122 O O   . ARG   D 45  ? 0.1360 0.1575 0.1239 -0.0112 -0.0204 -0.0184 59  ARG   D O   
3123 C CB  . ARG   D 45  ? 0.1449 0.1473 0.1177 -0.0248 0.0071  0.0055  59  ARG   D CB  
3124 C CG  . ARG   D 45  ? 0.1448 0.1533 0.1254 -0.0204 0.0089  -0.0055 59  ARG   D CG  
3125 C CD  . ARG   D 45  ? 0.1308 0.1492 0.1553 -0.0232 0.0007  -0.0242 59  ARG   D CD  
3126 N NE  . ARG   D 45  ? 0.1387 0.1522 0.1415 -0.0381 -0.0058 -0.0057 59  ARG   D NE  
3127 C CZ  . ARG   D 45  ? 0.1524 0.1660 0.1476 -0.0207 0.0022  -0.0132 59  ARG   D CZ  
3128 N NH1 . ARG   D 45  ? 0.1778 0.1747 0.1478 -0.0114 0.0150  -0.0172 59  ARG   D NH1 
3129 N NH2 . ARG   D 45  ? 0.1673 0.1838 0.1557 -0.0393 -0.0187 0.0082  59  ARG   D NH2 
3130 N N   . TYR   D 46  ? 0.1292 0.1509 0.1340 -0.0059 -0.0188 0.0043  60  TYR   D N   
3131 C CA  . TYR   D 46  ? 0.1257 0.1714 0.1339 -0.0012 -0.0176 0.0128  60  TYR   D CA  
3132 C C   . TYR   D 46  ? 0.1210 0.1730 0.1287 0.0068  -0.0187 0.0189  60  TYR   D C   
3133 O O   . TYR   D 46  ? 0.1389 0.1776 0.1326 -0.0134 -0.0139 0.0038  60  TYR   D O   
3134 C CB  . TYR   D 46  ? 0.1286 0.2004 0.1370 -0.0212 -0.0203 0.0163  60  TYR   D CB  
3135 C CG  . TYR   D 46  ? 0.1344 0.2059 0.1439 -0.0319 -0.0181 0.0203  60  TYR   D CG  
3136 C CD1 . TYR   D 46  ? 0.1567 0.2152 0.1323 -0.0389 -0.0067 0.0169  60  TYR   D CD1 
3137 C CD2 . TYR   D 46  ? 0.1495 0.2203 0.1578 -0.0364 -0.0212 0.0228  60  TYR   D CD2 
3138 C CE1 . TYR   D 46  ? 0.1703 0.2365 0.1269 -0.0400 -0.0235 0.0154  60  TYR   D CE1 
3139 C CE2 . TYR   D 46  ? 0.1499 0.2382 0.1610 -0.0307 -0.0104 0.0136  60  TYR   D CE2 
3140 C CZ  . TYR   D 46  ? 0.1763 0.2478 0.1242 -0.0420 -0.0240 0.0185  60  TYR   D CZ  
3141 O OH  . TYR   D 46  ? 0.2138 0.2728 0.1286 -0.0285 -0.0248 0.0134  60  TYR   D OH  
3142 N N   . ASP   D 47  ? 0.1158 0.1827 0.1387 0.0186  -0.0059 0.0247  61  ASP   D N   
3143 C CA  . ASP   D 47  ? 0.1247 0.1843 0.1285 0.0104  -0.0093 0.0051  61  ASP   D CA  
3144 C C   . ASP   D 47  ? 0.1372 0.1998 0.1337 -0.0094 -0.0248 0.0067  61  ASP   D C   
3145 O O   . ASP   D 47  ? 0.1377 0.2055 0.1296 -0.0111 -0.0179 0.0087  61  ASP   D O   
3146 C CB  . ASP   D 47  ? 0.1231 0.1795 0.1397 0.0036  -0.0012 -0.0091 61  ASP   D CB  
3147 C CG  . ASP   D 47  ? 0.1426 0.1801 0.1493 0.0096  -0.0112 -0.0047 61  ASP   D CG  
3148 O OD1 . ASP   D 47  ? 0.1332 0.1908 0.1615 -0.0052 -0.0314 -0.0056 61  ASP   D OD1 
3149 O OD2 . ASP   D 47  ? 0.1368 0.1746 0.1450 0.0059  -0.0200 0.0077  61  ASP   D OD2 
3150 N N   . SER   D 48  ? 0.1446 0.2093 0.1257 0.0007  -0.0287 -0.0042 62  SER   D N   
3151 C CA  . SER   D 48  ? 0.1849 0.2273 0.1327 0.0074  -0.0305 -0.0152 62  SER   D CA  
3152 C C   . SER   D 48  ? 0.1774 0.2502 0.1450 0.0086  -0.0342 -0.0029 62  SER   D C   
3153 O O   . SER   D 48  ? 0.2205 0.2799 0.1518 0.0459  -0.0499 -0.0003 62  SER   D O   
3154 C CB  . SER   D 48  ? 0.2158 0.2378 0.1489 -0.0297 0.0339  -0.0196 62  SER   D CB  
3155 O OG  . SER   D 48  ? 0.2560 0.2559 0.1898 -0.0582 0.0382  -0.0284 62  SER   D OG  
3156 N N   . ALA   D 49  ? 0.1568 0.2432 0.1565 0.0081  -0.0461 0.0107  63  ALA   D N   
3157 C CA  . ALA   D 49  ? 0.1539 0.2502 0.1788 0.0177  -0.0536 0.0179  63  ALA   D CA  
3158 C C   . ALA   D 49  ? 0.1749 0.2429 0.1841 0.0227  -0.0442 0.0219  63  ALA   D C   
3159 O O   . ALA   D 49  ? 0.1854 0.2413 0.1887 0.0337  -0.0336 0.0051  63  ALA   D O   
3160 C CB  . ALA   D 49  ? 0.1524 0.2613 0.2054 0.0161  -0.0412 0.0041  63  ALA   D CB  
3161 N N   . PRO   D 50  ? 0.1882 0.2477 0.1665 0.0061  -0.0405 0.0213  64  PRO   D N   
3162 C CA  . PRO   D 50  ? 0.1870 0.2415 0.1908 0.0177  -0.0385 0.0393  64  PRO   D CA  
3163 C C   . PRO   D 50  ? 0.2052 0.2354 0.2103 0.0197  -0.0766 0.0510  64  PRO   D C   
3164 O O   . PRO   D 50  ? 0.2375 0.2456 0.2171 0.0183  -0.0797 0.0460  64  PRO   D O   
3165 C CB  . PRO   D 50  ? 0.1886 0.2446 0.2026 -0.0090 -0.0176 0.0372  64  PRO   D CB  
3166 C CG  . PRO   D 50  ? 0.2081 0.2490 0.1988 -0.0277 -0.0170 0.0290  64  PRO   D CG  
3167 C CD  . PRO   D 50  ? 0.2082 0.2511 0.1774 -0.0198 -0.0204 0.0236  64  PRO   D CD  
3168 N N   . ALA   D 51  ? 0.2063 0.2267 0.2407 0.0281  -0.0691 0.0503  65  ALA   D N   
3169 C CA  . ALA   D 51  ? 0.2586 0.2374 0.2465 0.0328  -0.0820 0.0374  65  ALA   D CA  
3170 C C   . ALA   D 51  ? 0.3136 0.2489 0.2678 0.0365  -0.1125 0.0486  65  ALA   D C   
3171 O O   . ALA   D 51  ? 0.3201 0.2493 0.2787 0.0180  -0.0811 0.0524  65  ALA   D O   
3172 C CB  . ALA   D 51  ? 0.2547 0.2383 0.2690 0.0399  -0.0474 0.0181  65  ALA   D CB  
3173 N N   . THR   D 52  ? 0.3614 0.2626 0.3005 0.0583  -0.1427 0.0757  66  THR   D N   
3174 C CA  . THR   D 52  ? 0.4087 0.2902 0.3468 0.0772  -0.1552 0.0818  66  THR   D CA  
3175 C C   . THR   D 52  ? 0.4227 0.2825 0.3946 0.0866  -0.1313 0.0893  66  THR   D C   
3176 O O   . THR   D 52  ? 0.4548 0.2956 0.4280 0.1022  -0.1262 0.1017  66  THR   D O   
3177 C CB  . THR   D 52  ? 0.4386 0.3274 0.3686 0.0714  -0.1543 0.0670  66  THR   D CB  
3178 O OG1 . THR   D 52  ? 0.4496 0.3475 0.3934 0.0665  -0.1489 0.0646  66  THR   D OG1 
3179 C CG2 . THR   D 52  ? 0.4632 0.3401 0.3740 0.0625  -0.1364 0.0541  66  THR   D CG2 
3180 N N   . ASP   D 53  ? 0.3912 0.2673 0.4049 0.0745  -0.1265 0.0766  67  ASP   D N   
3181 C CA  . ASP   D 53  ? 0.3496 0.2612 0.4199 0.0728  -0.1017 0.0764  67  ASP   D CA  
3182 C C   . ASP   D 53  ? 0.3375 0.2549 0.4174 0.0563  -0.0881 0.0732  67  ASP   D C   
3183 O O   . ASP   D 53  ? 0.3696 0.2720 0.4637 0.0583  -0.0457 0.0561  67  ASP   D O   
3184 C CB  . ASP   D 53  ? 0.3205 0.2625 0.4269 0.0634  -0.0653 0.0791  67  ASP   D CB  
3185 C CG  . ASP   D 53  ? 0.2982 0.2702 0.4359 0.0438  -0.0302 0.0721  67  ASP   D CG  
3186 O OD1 . ASP   D 53  ? 0.2552 0.2578 0.4127 0.0162  -0.0371 0.0613  67  ASP   D OD1 
3187 O OD2 . ASP   D 53  ? 0.3305 0.2889 0.4680 0.0468  0.0094  0.0708  67  ASP   D OD2 
3188 N N   . GLY   D 54  ? 0.3169 0.2456 0.3668 0.0490  -0.1009 0.0996  68  GLY   D N   
3189 C CA  . GLY   D 54  ? 0.3212 0.2395 0.3199 0.0278  -0.0840 0.1038  68  GLY   D CA  
3190 C C   . GLY   D 54  ? 0.2946 0.2253 0.2884 0.0086  -0.0920 0.0897  68  GLY   D C   
3191 O O   . GLY   D 54  ? 0.3178 0.2440 0.3160 -0.0119 -0.0615 0.0770  68  GLY   D O   
3192 N N   . SER   D 55  ? 0.2718 0.1917 0.2448 0.0068  -0.0609 0.0666  69  SER   D N   
3193 C CA  . SER   D 55  ? 0.2492 0.1865 0.2050 0.0185  -0.0553 0.0619  69  SER   D CA  
3194 C C   . SER   D 55  ? 0.2386 0.1740 0.1849 0.0091  -0.0473 0.0480  69  SER   D C   
3195 O O   . SER   D 55  ? 0.2332 0.1840 0.1767 0.0010  -0.0558 0.0387  69  SER   D O   
3196 C CB  . SER   D 55  ? 0.2813 0.1970 0.2307 0.0327  -0.0198 0.0504  69  SER   D CB  
3197 O OG  . SER   D 55  ? 0.3273 0.2233 0.2759 0.0177  -0.0172 0.0228  69  SER   D OG  
3198 N N   . GLY   D 56  ? 0.2204 0.1618 0.1756 0.0101  -0.0341 0.0413  70  GLY   D N   
3199 C CA  . GLY   D 56  ? 0.2238 0.1572 0.1546 0.0086  -0.0083 0.0370  70  GLY   D CA  
3200 C C   . GLY   D 56  ? 0.1934 0.1575 0.1463 0.0051  -0.0288 0.0350  70  GLY   D C   
3201 O O   . GLY   D 56  ? 0.1662 0.1625 0.1505 0.0054  -0.0170 0.0233  70  GLY   D O   
3202 N N   . THR   D 57  ? 0.1892 0.1591 0.1379 0.0047  -0.0303 0.0232  71  THR   D N   
3203 C CA  . THR   D 57  ? 0.1775 0.1548 0.1343 -0.0017 -0.0221 0.0299  71  THR   D CA  
3204 C C   . THR   D 57  ? 0.1532 0.1456 0.1205 -0.0149 -0.0239 0.0313  71  THR   D C   
3205 O O   . THR   D 57  ? 0.1469 0.1513 0.1355 -0.0092 -0.0221 0.0196  71  THR   D O   
3206 C CB  . THR   D 57  ? 0.1875 0.1656 0.1260 -0.0124 -0.0210 0.0373  71  THR   D CB  
3207 O OG1 . THR   D 57  ? 0.1987 0.1783 0.1319 -0.0077 -0.0285 0.0318  71  THR   D OG1 
3208 C CG2 . THR   D 57  ? 0.1810 0.1665 0.1500 -0.0189 -0.0068 0.0197  71  THR   D CG2 
3209 N N   . ALA   D 58  ? 0.1442 0.1399 0.1179 -0.0134 -0.0069 0.0304  72  ALA   D N   
3210 C CA  . ALA   D 58  ? 0.1458 0.1404 0.1299 0.0015  -0.0090 0.0403  72  ALA   D CA  
3211 C C   . ALA   D 58  ? 0.1227 0.1489 0.1349 -0.0038 -0.0265 0.0214  72  ALA   D C   
3212 O O   . ALA   D 58  ? 0.1359 0.1591 0.1390 -0.0096 -0.0267 0.0134  72  ALA   D O   
3213 C CB  . ALA   D 58  ? 0.1607 0.1431 0.1346 -0.0192 -0.0116 0.0301  72  ALA   D CB  
3214 N N   . LEU   D 59  ? 0.1364 0.1425 0.1233 0.0067  -0.0292 0.0244  73  LEU   D N   
3215 C CA  A LEU   D 59  ? 0.1331 0.1444 0.1213 -0.0025 -0.0218 0.0229  73  LEU   D CA  
3216 C CA  B LEU   D 59  ? 0.1417 0.1465 0.1224 -0.0033 -0.0051 0.0171  73  LEU   D CA  
3217 C C   . LEU   D 59  ? 0.1303 0.1389 0.1241 0.0069  -0.0218 0.0080  73  LEU   D C   
3218 O O   . LEU   D 59  ? 0.1599 0.1265 0.1522 0.0127  -0.0348 -0.0064 73  LEU   D O   
3219 C CB  A LEU   D 59  ? 0.1373 0.1497 0.1278 -0.0265 -0.0263 0.0357  73  LEU   D CB  
3220 C CB  B LEU   D 59  ? 0.1636 0.1558 0.1326 -0.0331 0.0071  0.0151  73  LEU   D CB  
3221 C CG  A LEU   D 59  ? 0.1667 0.1535 0.1238 -0.0328 -0.0093 0.0259  73  LEU   D CG  
3222 C CG  B LEU   D 59  ? 0.1952 0.1608 0.1221 -0.0262 0.0165  -0.0010 73  LEU   D CG  
3223 C CD1 A LEU   D 59  ? 0.1811 0.1556 0.1333 -0.0319 0.0020  0.0369  73  LEU   D CD1 
3224 C CD1 B LEU   D 59  ? 0.1975 0.1676 0.1276 -0.0180 0.0073  0.0011  73  LEU   D CD1 
3225 C CD2 A LEU   D 59  ? 0.1684 0.1501 0.1130 -0.0311 0.0042  0.0415  73  LEU   D CD2 
3226 C CD2 B LEU   D 59  ? 0.2118 0.1692 0.1550 -0.0126 0.0337  -0.0302 73  LEU   D CD2 
3227 N N   . GLY   D 60  ? 0.1203 0.1395 0.1185 0.0111  0.0102  0.0103  74  GLY   D N   
3228 C CA  . GLY   D 60  ? 0.1256 0.1435 0.1103 0.0119  0.0020  -0.0033 74  GLY   D CA  
3229 C C   . GLY   D 60  ? 0.1188 0.1427 0.0919 -0.0119 0.0070  0.0083  74  GLY   D C   
3230 O O   . GLY   D 60  ? 0.1189 0.1594 0.0996 0.0011  -0.0024 -0.0128 74  GLY   D O   
3231 N N   . TRP   D 61  ? 0.1116 0.1449 0.1118 0.0011  -0.0021 0.0075  75  TRP   D N   
3232 C CA  . TRP   D 61  ? 0.1114 0.1550 0.0952 0.0145  0.0098  -0.0016 75  TRP   D CA  
3233 C C   . TRP   D 61  ? 0.1281 0.1559 0.0900 0.0049  0.0040  -0.0148 75  TRP   D C   
3234 O O   . TRP   D 61  ? 0.1214 0.1414 0.1136 0.0075  0.0050  -0.0174 75  TRP   D O   
3235 C CB  . TRP   D 61  ? 0.1381 0.1567 0.1061 -0.0141 0.0039  0.0005  75  TRP   D CB  
3236 C CG  . TRP   D 61  ? 0.1221 0.1733 0.1057 -0.0136 0.0117  -0.0038 75  TRP   D CG  
3237 C CD1 . TRP   D 61  ? 0.1445 0.1902 0.1165 -0.0189 0.0028  -0.0074 75  TRP   D CD1 
3238 C CD2 . TRP   D 61  ? 0.1320 0.1768 0.1069 -0.0053 0.0044  -0.0129 75  TRP   D CD2 
3239 N NE1 . TRP   D 61  ? 0.1294 0.1913 0.1286 -0.0240 -0.0163 0.0165  75  TRP   D NE1 
3240 C CE2 . TRP   D 61  ? 0.1407 0.1790 0.1253 -0.0243 0.0099  -0.0013 75  TRP   D CE2 
3241 C CE3 . TRP   D 61  ? 0.1521 0.1768 0.1432 -0.0144 0.0087  -0.0155 75  TRP   D CE3 
3242 C CZ2 . TRP   D 61  ? 0.1771 0.1917 0.1247 -0.0151 0.0255  -0.0230 75  TRP   D CZ2 
3243 C CZ3 . TRP   D 61  ? 0.1526 0.1789 0.1635 -0.0283 0.0186  -0.0151 75  TRP   D CZ3 
3244 C CH2 . TRP   D 61  ? 0.1785 0.1849 0.1408 -0.0184 0.0380  -0.0240 75  TRP   D CH2 
3245 N N   . THR   D 62  ? 0.1221 0.1566 0.1080 0.0150  0.0057  0.0024  76  THR   D N   
3246 C CA  . THR   D 62  ? 0.1198 0.1543 0.1178 0.0163  0.0167  -0.0015 76  THR   D CA  
3247 C C   . THR   D 62  ? 0.1150 0.1682 0.1056 0.0220  0.0000  -0.0303 76  THR   D C   
3248 O O   . THR   D 62  ? 0.1326 0.1803 0.1164 0.0266  0.0038  -0.0350 76  THR   D O   
3249 C CB  . THR   D 62  ? 0.1396 0.1434 0.1261 0.0079  -0.0019 -0.0111 76  THR   D CB  
3250 O OG1 . THR   D 62  ? 0.1317 0.1418 0.1161 0.0185  0.0240  -0.0141 76  THR   D OG1 
3251 C CG2 . THR   D 62  ? 0.1298 0.1628 0.1267 0.0389  -0.0212 0.0020  76  THR   D CG2 
3252 N N   . VAL   D 63  ? 0.1147 0.1781 0.1255 0.0415  -0.0027 -0.0190 77  VAL   D N   
3253 C CA  . VAL   D 63  ? 0.1182 0.1803 0.1445 0.0346  -0.0103 -0.0464 77  VAL   D CA  
3254 C C   . VAL   D 63  ? 0.1263 0.1743 0.1409 0.0535  -0.0183 -0.0579 77  VAL   D C   
3255 O O   . VAL   D 63  ? 0.1741 0.1714 0.1548 0.0575  -0.0174 -0.0562 77  VAL   D O   
3256 C CB  . VAL   D 63  ? 0.1173 0.2093 0.1673 0.0156  -0.0036 -0.0602 77  VAL   D CB  
3257 C CG1 . VAL   D 63  ? 0.1393 0.2235 0.2204 0.0045  0.0183  -0.0762 77  VAL   D CG1 
3258 C CG2 . VAL   D 63  ? 0.1494 0.2149 0.1377 -0.0185 -0.0032 -0.0494 77  VAL   D CG2 
3259 N N   . ALA   D 64  ? 0.1286 0.1862 0.1401 0.0510  -0.0163 -0.0411 78  ALA   D N   
3260 C CA  . ALA   D 64  ? 0.1203 0.1904 0.1578 0.0461  -0.0180 -0.0517 78  ALA   D CA  
3261 C C   . ALA   D 64  ? 0.1218 0.2021 0.1562 0.0524  -0.0259 -0.0516 78  ALA   D C   
3262 O O   . ALA   D 64  ? 0.1603 0.2002 0.1558 0.0472  -0.0104 -0.0527 78  ALA   D O   
3263 C CB  . ALA   D 64  ? 0.1778 0.1890 0.1652 0.0465  -0.0185 -0.0405 78  ALA   D CB  
3264 N N   . TRP   D 65  ? 0.1258 0.1911 0.1512 0.0486  -0.0339 -0.0400 79  TRP   D N   
3265 C CA  . TRP   D 65  ? 0.1457 0.1789 0.1496 0.0531  -0.0210 -0.0390 79  TRP   D CA  
3266 C C   . TRP   D 65  ? 0.1581 0.1891 0.1482 0.0425  -0.0143 -0.0457 79  TRP   D C   
3267 O O   . TRP   D 65  ? 0.1840 0.2070 0.1880 0.0606  -0.0247 -0.0495 79  TRP   D O   
3268 C CB  . TRP   D 65  ? 0.1461 0.1802 0.1665 0.0409  -0.0119 -0.0389 79  TRP   D CB  
3269 C CG  . TRP   D 65  ? 0.1563 0.1804 0.1405 0.0412  -0.0266 -0.0374 79  TRP   D CG  
3270 C CD1 . TRP   D 65  ? 0.1611 0.1820 0.1583 0.0381  -0.0127 -0.0264 79  TRP   D CD1 
3271 C CD2 . TRP   D 65  ? 0.1704 0.1752 0.1564 0.0223  -0.0097 -0.0321 79  TRP   D CD2 
3272 N NE1 . TRP   D 65  ? 0.1810 0.1746 0.1565 0.0303  -0.0056 -0.0299 79  TRP   D NE1 
3273 C CE2 . TRP   D 65  ? 0.1530 0.1689 0.1823 0.0170  -0.0078 -0.0295 79  TRP   D CE2 
3274 C CE3 . TRP   D 65  ? 0.1588 0.1756 0.1589 0.0125  -0.0026 -0.0284 79  TRP   D CE3 
3275 C CZ2 . TRP   D 65  ? 0.1675 0.1829 0.1672 0.0049  -0.0256 -0.0275 79  TRP   D CZ2 
3276 C CZ3 . TRP   D 65  ? 0.1635 0.1741 0.1583 0.0198  0.0034  -0.0500 79  TRP   D CZ3 
3277 C CH2 . TRP   D 65  ? 0.1639 0.1783 0.1646 0.0063  0.0045  -0.0525 79  TRP   D CH2 
3278 N N   . LYS   D 66  ? 0.1685 0.1773 0.1616 0.0467  -0.0054 -0.0640 80  LYS   D N   
3279 C CA  . LYS   D 66  ? 0.1821 0.1776 0.1710 0.0464  0.0033  -0.0542 80  LYS   D CA  
3280 C C   . LYS   D 66  ? 0.1569 0.1822 0.1774 0.0355  -0.0006 -0.0534 80  LYS   D C   
3281 O O   . LYS   D 66  ? 0.1379 0.1855 0.1884 0.0299  0.0030  -0.0524 80  LYS   D O   
3282 C CB  . LYS   D 66  ? 0.2087 0.1692 0.1865 0.0539  0.0002  -0.0430 80  LYS   D CB  
3283 C CG  . LYS   D 66  ? 0.2419 0.1805 0.2382 0.0509  -0.0200 -0.0206 80  LYS   D CG  
3284 C CD  . LYS   D 66  ? 0.2723 0.1998 0.2660 0.0465  -0.0302 -0.0199 80  LYS   D CD  
3285 C CE  . LYS   D 66  ? 0.3236 0.2152 0.2855 0.0400  -0.0156 -0.0315 80  LYS   D CE  
3286 N NZ  . LYS   D 66  ? 0.3544 0.2212 0.3046 0.0366  0.0150  -0.0489 80  LYS   D NZ  
3287 N N   . ASN   D 67  ? 0.1623 0.1778 0.1924 0.0195  0.0106  -0.0705 81  ASN   D N   
3288 C CA  . ASN   D 67  ? 0.1490 0.1806 0.2058 0.0161  0.0069  -0.0662 81  ASN   D CA  
3289 C C   . ASN   D 67  ? 0.1440 0.1867 0.2306 0.0049  0.0148  -0.0851 81  ASN   D C   
3290 O O   . ASN   D 67  ? 0.1681 0.1948 0.2326 0.0197  0.0140  -0.0677 81  ASN   D O   
3291 C CB  . ASN   D 67  ? 0.1552 0.1926 0.2127 0.0094  0.0149  -0.0574 81  ASN   D CB  
3292 C CG  . ASN   D 67  ? 0.1490 0.1907 0.2046 0.0131  0.0105  -0.0547 81  ASN   D CG  
3293 O OD1 . ASN   D 67  ? 0.1538 0.1949 0.1958 0.0216  -0.0028 -0.0454 81  ASN   D OD1 
3294 N ND2 . ASN   D 67  ? 0.1465 0.1968 0.2199 -0.0004 0.0304  -0.0417 81  ASN   D ND2 
3295 N N   . ASN   D 68  ? 0.1412 0.1817 0.2566 0.0034  0.0168  -0.1010 82  ASN   D N   
3296 C CA  . ASN   D 68  ? 0.1509 0.2117 0.2938 0.0146  0.0272  -0.1021 82  ASN   D CA  
3297 C C   . ASN   D 68  ? 0.1516 0.2022 0.3165 0.0309  0.0153  -0.0883 82  ASN   D C   
3298 O O   . ASN   D 68  ? 0.1719 0.2066 0.3770 0.0270  0.0256  -0.0808 82  ASN   D O   
3299 C CB  . ASN   D 68  ? 0.2222 0.2546 0.3446 0.0042  0.0466  -0.1148 82  ASN   D CB  
3300 C CG  . ASN   D 68  ? 0.3374 0.3054 0.4080 -0.0220 0.0709  -0.1075 82  ASN   D CG  
3301 O OD1 . ASN   D 68  ? 0.3849 0.3218 0.4245 -0.0414 0.0721  -0.1001 82  ASN   D OD1 
3302 N ND2 . ASN   D 68  ? 0.4021 0.3296 0.4489 -0.0296 0.0732  -0.0995 82  ASN   D ND2 
3303 N N   . TYR   D 69  ? 0.1479 0.1990 0.2690 0.0181  0.0321  -0.0929 83  TYR   D N   
3304 C CA  . TYR   D 69  ? 0.1491 0.2041 0.2555 0.0233  0.0139  -0.0579 83  TYR   D CA  
3305 C C   . TYR   D 69  ? 0.1314 0.1989 0.2482 0.0246  -0.0078 -0.0382 83  TYR   D C   
3306 O O   . TYR   D 69  ? 0.1456 0.2183 0.2731 0.0228  0.0105  -0.0114 83  TYR   D O   
3307 C CB  . TYR   D 69  ? 0.1528 0.2161 0.2531 0.0101  0.0121  -0.0545 83  TYR   D CB  
3308 C CG  . TYR   D 69  ? 0.1706 0.2397 0.2296 0.0034  0.0414  -0.0543 83  TYR   D CG  
3309 C CD1 . TYR   D 69  ? 0.2168 0.2566 0.2411 0.0157  0.0670  -0.0534 83  TYR   D CD1 
3310 C CD2 . TYR   D 69  ? 0.1940 0.2427 0.2301 0.0148  0.0420  -0.0564 83  TYR   D CD2 
3311 C CE1 . TYR   D 69  ? 0.2348 0.2747 0.2344 0.0132  0.0771  -0.0679 83  TYR   D CE1 
3312 C CE2 . TYR   D 69  ? 0.2143 0.2584 0.2326 -0.0084 0.0532  -0.0692 83  TYR   D CE2 
3313 C CZ  . TYR   D 69  ? 0.2483 0.2797 0.2211 0.0088  0.0610  -0.0705 83  TYR   D CZ  
3314 O OH  . TYR   D 69  ? 0.2772 0.2968 0.2343 0.0039  0.0413  -0.0750 83  TYR   D OH  
3315 N N   . ARG   D 70  ? 0.1473 0.1953 0.2276 0.0266  0.0118  -0.0595 84  ARG   D N   
3316 C CA  A ARG   D 70  ? 0.1569 0.1993 0.2358 0.0294  -0.0100 -0.0701 84  ARG   D CA  
3317 C CA  B ARG   D 70  ? 0.1773 0.2059 0.2463 0.0276  0.0002  -0.0679 84  ARG   D CA  
3318 C C   . ARG   D 70  ? 0.1635 0.2071 0.2271 0.0324  -0.0138 -0.0746 84  ARG   D C   
3319 O O   . ARG   D 70  ? 0.1533 0.2124 0.2174 0.0243  -0.0168 -0.0693 84  ARG   D O   
3320 C CB  A ARG   D 70  ? 0.1510 0.2016 0.2525 0.0463  -0.0266 -0.0473 84  ARG   D CB  
3321 C CB  B ARG   D 70  ? 0.2197 0.2186 0.2765 0.0348  0.0027  -0.0571 84  ARG   D CB  
3322 C CG  A ARG   D 70  ? 0.1261 0.1968 0.2208 0.0429  -0.0279 -0.0464 84  ARG   D CG  
3323 C CG  B ARG   D 70  ? 0.2510 0.2281 0.2819 0.0365  0.0097  -0.0546 84  ARG   D CG  
3324 C CD  A ARG   D 70  ? 0.1360 0.1998 0.2211 0.0407  -0.0225 -0.0277 84  ARG   D CD  
3325 C CD  B ARG   D 70  ? 0.2660 0.2402 0.2788 0.0332  0.0204  -0.0525 84  ARG   D CD  
3326 N NE  A ARG   D 70  ? 0.1504 0.2107 0.2209 0.0306  0.0007  -0.0306 84  ARG   D NE  
3327 N NE  B ARG   D 70  ? 0.2729 0.2463 0.2722 0.0272  0.0213  -0.0501 84  ARG   D NE  
3328 C CZ  A ARG   D 70  ? 0.1500 0.2166 0.2106 0.0283  0.0093  -0.0291 84  ARG   D CZ  
3329 C CZ  B ARG   D 70  ? 0.2346 0.2420 0.2392 0.0180  -0.0155 -0.0563 84  ARG   D CZ  
3330 N NH1 A ARG   D 70  ? 0.1481 0.2166 0.2003 0.0283  0.0226  -0.0278 84  ARG   D NH1 
3331 N NH1 B ARG   D 70  ? 0.2641 0.2576 0.2674 0.0308  -0.0063 -0.0332 84  ARG   D NH1 
3332 N NH2 A ARG   D 70  ? 0.1647 0.2298 0.2053 0.0433  -0.0180 -0.0203 84  ARG   D NH2 
3333 N NH2 B ARG   D 70  ? 0.1542 0.2264 0.1782 0.0252  -0.0757 -0.0574 84  ARG   D NH2 
3334 N N   . ASN   D 71  ? 0.1804 0.2209 0.2126 0.0628  -0.0096 -0.0684 85  ASN   D N   
3335 C CA  . ASN   D 71  ? 0.1917 0.2241 0.2122 0.0631  -0.0021 -0.0612 85  ASN   D CA  
3336 C C   . ASN   D 71  ? 0.2058 0.2289 0.1976 0.0650  -0.0291 -0.0659 85  ASN   D C   
3337 O O   . ASN   D 71  ? 0.2211 0.2506 0.2196 0.0728  -0.0490 -0.0598 85  ASN   D O   
3338 C CB  . ASN   D 71  ? 0.1623 0.2174 0.2173 0.0743  -0.0150 -0.0378 85  ASN   D CB  
3339 C CG  . ASN   D 71  ? 0.1921 0.2144 0.1799 0.0748  -0.0070 -0.0502 85  ASN   D CG  
3340 O OD1 . ASN   D 71  ? 0.2025 0.2120 0.1868 0.0831  -0.0203 -0.0561 85  ASN   D OD1 
3341 N ND2 . ASN   D 71  ? 0.2152 0.2150 0.1885 0.0642  -0.0079 -0.0503 85  ASN   D ND2 
3342 N N   . ALA   D 72  ? 0.1950 0.2227 0.1780 0.0580  -0.0303 -0.0677 86  ALA   D N   
3343 C CA  . ALA   D 72  ? 0.2237 0.2173 0.1968 0.0699  -0.0269 -0.0709 86  ALA   D CA  
3344 C C   . ALA   D 72  ? 0.2137 0.2208 0.1672 0.0743  -0.0485 -0.0694 86  ALA   D C   
3345 O O   . ALA   D 72  ? 0.2269 0.2377 0.1953 0.0640  -0.0374 -0.0591 86  ALA   D O   
3346 C CB  . ALA   D 72  ? 0.2690 0.2177 0.2121 0.0512  -0.0301 -0.0679 86  ALA   D CB  
3347 N N   . HIS   D 73  ? 0.2200 0.2176 0.1724 0.0831  -0.0431 -0.0521 87  HIS   D N   
3348 C CA  . HIS   D 73  ? 0.2304 0.2220 0.1623 0.0903  -0.0449 -0.0510 87  HIS   D CA  
3349 C C   . HIS   D 73  ? 0.2292 0.2152 0.1444 0.0896  -0.0414 -0.0420 87  HIS   D C   
3350 O O   . HIS   D 73  ? 0.2496 0.2159 0.1604 0.0882  -0.0273 -0.0266 87  HIS   D O   
3351 C CB  . HIS   D 73  ? 0.2252 0.2234 0.1647 0.0968  -0.0502 -0.0405 87  HIS   D CB  
3352 C CG  . HIS   D 73  ? 0.2331 0.2249 0.1654 0.0924  -0.0397 -0.0367 87  HIS   D CG  
3353 N ND1 . HIS   D 73  ? 0.2363 0.2193 0.1953 0.1079  -0.0169 -0.0198 87  HIS   D ND1 
3354 C CD2 . HIS   D 73  ? 0.2375 0.2295 0.2019 0.0845  -0.0339 -0.0354 87  HIS   D CD2 
3355 C CE1 . HIS   D 73  ? 0.2352 0.2254 0.1966 0.0911  -0.0311 -0.0264 87  HIS   D CE1 
3356 N NE2 . HIS   D 73  ? 0.2363 0.2255 0.2140 0.0894  -0.0371 -0.0343 87  HIS   D NE2 
3357 N N   . SER   D 74  ? 0.2022 0.2085 0.1656 0.0931  -0.0279 -0.0323 88  SER   D N   
3358 C CA  . SER   D 74  ? 0.2004 0.1964 0.1599 0.0771  -0.0560 -0.0621 88  SER   D CA  
3359 C C   . SER   D 74  ? 0.1924 0.1830 0.1390 0.0732  -0.0372 -0.0352 88  SER   D C   
3360 O O   . SER   D 74  ? 0.1941 0.1875 0.1295 0.0626  -0.0263 -0.0415 88  SER   D O   
3361 C CB  . SER   D 74  ? 0.2444 0.2387 0.2062 0.0375  -0.0656 -0.0489 88  SER   D CB  
3362 O OG  . SER   D 74  ? 0.2747 0.2631 0.2680 0.0431  -0.0751 -0.0584 88  SER   D OG  
3363 N N   . ALA   D 75  ? 0.1952 0.1731 0.1293 0.0644  -0.0393 -0.0286 89  ALA   D N   
3364 C CA  . ALA   D 75  ? 0.1980 0.1494 0.1297 0.0474  -0.0356 -0.0252 89  ALA   D CA  
3365 C C   . ALA   D 75  ? 0.1561 0.1357 0.1172 0.0338  -0.0208 -0.0270 89  ALA   D C   
3366 O O   . ALA   D 75  ? 0.1915 0.1414 0.1146 0.0270  -0.0131 -0.0306 89  ALA   D O   
3367 C CB  . ALA   D 75  ? 0.1979 0.1504 0.1552 0.0282  -0.0393 -0.0230 89  ALA   D CB  
3368 N N   . THR   D 76  ? 0.1504 0.1472 0.1201 0.0418  -0.0238 -0.0263 90  THR   D N   
3369 C CA  . THR   D 76  ? 0.1369 0.1508 0.1073 0.0381  -0.0096 -0.0341 90  THR   D CA  
3370 C C   . THR   D 76  ? 0.1460 0.1515 0.1043 0.0318  0.0044  -0.0195 90  THR   D C   
3371 O O   . THR   D 76  ? 0.1440 0.1478 0.1145 0.0225  -0.0055 -0.0246 90  THR   D O   
3372 C CB  . THR   D 76  ? 0.1324 0.1700 0.1199 0.0235  -0.0084 -0.0348 90  THR   D CB  
3373 O OG1 . THR   D 76  ? 0.1476 0.1828 0.1278 0.0312  -0.0135 -0.0382 90  THR   D OG1 
3374 C CG2 . THR   D 76  ? 0.1417 0.1684 0.1224 0.0113  0.0043  -0.0350 90  THR   D CG2 
3375 N N   . THR   D 77  ? 0.1437 0.1462 0.1003 0.0231  -0.0013 -0.0114 91  THR   D N   
3376 C CA  . THR   D 77  ? 0.1306 0.1484 0.1041 0.0226  -0.0111 0.0028  91  THR   D CA  
3377 C C   . THR   D 77  ? 0.1526 0.1405 0.1020 0.0179  -0.0180 -0.0115 91  THR   D C   
3378 O O   . THR   D 77  ? 0.2279 0.1453 0.1121 0.0243  -0.0474 -0.0124 91  THR   D O   
3379 C CB  . THR   D 77  ? 0.1440 0.1507 0.1034 0.0164  0.0152  0.0024  91  THR   D CB  
3380 O OG1 . THR   D 77  ? 0.1730 0.1613 0.1054 0.0374  0.0172  0.0010  91  THR   D OG1 
3381 C CG2 . THR   D 77  ? 0.1721 0.1423 0.1331 0.0162  0.0090  -0.0015 91  THR   D CG2 
3382 N N   . TRP   D 78  ? 0.1317 0.1363 0.1066 0.0071  -0.0035 0.0048  92  TRP   D N   
3383 C CA  . TRP   D 78  ? 0.1179 0.1272 0.1097 0.0043  0.0061  -0.0019 92  TRP   D CA  
3384 C C   . TRP   D 78  ? 0.1424 0.1229 0.0978 -0.0134 -0.0049 -0.0030 92  TRP   D C   
3385 O O   . TRP   D 78  ? 0.1501 0.1335 0.1100 0.0051  -0.0015 -0.0085 92  TRP   D O   
3386 C CB  . TRP   D 78  ? 0.1184 0.1475 0.1235 0.0093  0.0027  -0.0048 92  TRP   D CB  
3387 C CG  . TRP   D 78  ? 0.1145 0.1540 0.1002 0.0030  0.0047  -0.0097 92  TRP   D CG  
3388 C CD1 . TRP   D 78  ? 0.1367 0.1627 0.0939 -0.0059 -0.0061 -0.0030 92  TRP   D CD1 
3389 C CD2 . TRP   D 78  ? 0.1317 0.1497 0.1123 0.0140  0.0082  -0.0080 92  TRP   D CD2 
3390 N NE1 . TRP   D 78  ? 0.1281 0.1675 0.1264 -0.0027 0.0007  -0.0015 92  TRP   D NE1 
3391 C CE2 . TRP   D 78  ? 0.1284 0.1573 0.1186 0.0217  0.0085  -0.0049 92  TRP   D CE2 
3392 C CE3 . TRP   D 78  ? 0.1457 0.1533 0.1066 0.0325  0.0017  -0.0070 92  TRP   D CE3 
3393 C CZ2 . TRP   D 78  ? 0.1521 0.1670 0.1189 0.0024  0.0071  0.0072  92  TRP   D CZ2 
3394 C CZ3 . TRP   D 78  ? 0.1652 0.1687 0.1270 0.0226  0.0071  -0.0022 92  TRP   D CZ3 
3395 C CH2 . TRP   D 78  ? 0.1509 0.1670 0.1156 0.0233  0.0003  0.0070  92  TRP   D CH2 
3396 N N   . SER   D 79  ? 0.1143 0.1281 0.1120 0.0054  -0.0101 -0.0031 93  SER   D N   
3397 C CA  . SER   D 79  ? 0.1421 0.1474 0.1164 0.0214  -0.0089 0.0126  93  SER   D CA  
3398 C C   . SER   D 79  ? 0.1157 0.1431 0.1117 0.0244  -0.0149 0.0149  93  SER   D C   
3399 O O   . SER   D 79  ? 0.1359 0.1381 0.1239 -0.0086 -0.0041 0.0011  93  SER   D O   
3400 C CB  . SER   D 79  ? 0.1555 0.1727 0.1130 0.0242  0.0005  0.0031  93  SER   D CB  
3401 O OG  . SER   D 79  ? 0.1506 0.1883 0.1306 0.0457  0.0009  0.0246  93  SER   D OG  
3402 N N   . GLY   D 80  ? 0.1297 0.1421 0.1032 0.0182  0.0022  0.0266  94  GLY   D N   
3403 C CA  . GLY   D 80  ? 0.1467 0.1512 0.1135 0.0126  -0.0241 0.0371  94  GLY   D CA  
3404 C C   . GLY   D 80  ? 0.1365 0.1408 0.1023 -0.0046 -0.0016 0.0226  94  GLY   D C   
3405 O O   . GLY   D 80  ? 0.1393 0.1440 0.1227 -0.0123 -0.0101 0.0131  94  GLY   D O   
3406 N N   . GLN   D 81  ? 0.1548 0.1535 0.0971 0.0118  -0.0090 0.0293  95  GLN   D N   
3407 C CA  . GLN   D 81  ? 0.1691 0.1691 0.1002 0.0163  -0.0134 0.0231  95  GLN   D CA  
3408 C C   . GLN   D 81  ? 0.1621 0.1658 0.1281 -0.0053 -0.0186 0.0350  95  GLN   D C   
3409 O O   . GLN   D 81  ? 0.1532 0.1573 0.1385 -0.0041 -0.0201 0.0180  95  GLN   D O   
3410 C CB  . GLN   D 81  ? 0.2004 0.1840 0.1436 0.0309  -0.0279 -0.0023 95  GLN   D CB  
3411 C CG  . GLN   D 81  ? 0.2096 0.1889 0.1813 0.0196  -0.0423 0.0063  95  GLN   D CG  
3412 C CD  . GLN   D 81  ? 0.2096 0.1722 0.1652 0.0305  -0.0446 0.0121  95  GLN   D CD  
3413 O OE1 . GLN   D 81  ? 0.1944 0.1534 0.1578 0.0117  -0.0299 0.0227  95  GLN   D OE1 
3414 N NE2 . GLN   D 81  ? 0.2322 0.1735 0.1706 0.0146  -0.0399 -0.0094 95  GLN   D NE2 
3415 N N   . TYR   D 82  ? 0.1654 0.1744 0.1154 -0.0072 0.0001  0.0338  96  TYR   D N   
3416 C CA  . TYR   D 82  ? 0.1807 0.1803 0.0934 0.0051  -0.0089 0.0367  96  TYR   D CA  
3417 C C   . TYR   D 82  ? 0.1731 0.1885 0.1450 -0.0084 -0.0184 0.0503  96  TYR   D C   
3418 O O   . TYR   D 82  ? 0.1925 0.1762 0.1671 -0.0027 -0.0190 0.0652  96  TYR   D O   
3419 C CB  . TYR   D 82  ? 0.1845 0.2127 0.0911 -0.0087 -0.0112 0.0282  96  TYR   D CB  
3420 C CG  . TYR   D 82  ? 0.2016 0.2395 0.1037 -0.0280 -0.0132 0.0316  96  TYR   D CG  
3421 C CD1 . TYR   D 82  ? 0.2051 0.2513 0.1098 -0.0316 0.0170  0.0271  96  TYR   D CD1 
3422 C CD2 . TYR   D 82  ? 0.2316 0.2687 0.1293 -0.0285 -0.0308 0.0454  96  TYR   D CD2 
3423 C CE1 . TYR   D 82  ? 0.2428 0.2745 0.1252 -0.0132 0.0006  0.0453  96  TYR   D CE1 
3424 C CE2 . TYR   D 82  ? 0.2645 0.2948 0.1339 -0.0213 -0.0309 0.0503  96  TYR   D CE2 
3425 C CZ  . TYR   D 82  ? 0.2825 0.3004 0.1139 -0.0210 0.0026  0.0603  96  TYR   D CZ  
3426 O OH  . TYR   D 82  ? 0.3125 0.3353 0.1573 -0.0098 0.0096  0.0664  96  TYR   D OH  
3427 N N   . VAL   D 83  ? 0.2010 0.2023 0.1731 -0.0086 -0.0181 0.0873  97  VAL   D N   
3428 C CA  . VAL   D 83  ? 0.2344 0.2337 0.2526 -0.0223 -0.0292 0.1196  97  VAL   D CA  
3429 C C   . VAL   D 83  ? 0.2489 0.2766 0.2617 -0.0430 -0.0623 0.1430  97  VAL   D C   
3430 O O   . VAL   D 83  ? 0.2443 0.2983 0.2559 -0.0565 -0.0475 0.1539  97  VAL   D O   
3431 C CB  . VAL   D 83  ? 0.2654 0.2300 0.3102 0.0022  -0.0066 0.1028  97  VAL   D CB  
3432 C CG1 . VAL   D 83  ? 0.2813 0.2310 0.3442 0.0133  -0.0037 0.1087  97  VAL   D CG1 
3433 C CG2 . VAL   D 83  ? 0.2895 0.2316 0.3390 0.0072  0.0071  0.0726  97  VAL   D CG2 
3434 N N   . GLY   D 84  ? 0.2831 0.3033 0.2903 -0.0616 -0.0815 0.1435  98  GLY   D N   
3435 C CA  . GLY   D 84  ? 0.3247 0.3233 0.3010 -0.0552 -0.0794 0.1641  98  GLY   D CA  
3436 C C   . GLY   D 84  ? 0.3987 0.3421 0.3152 -0.0314 -0.0619 0.1673  98  GLY   D C   
3437 O O   . GLY   D 84  ? 0.4855 0.3410 0.3548 -0.0011 -0.0614 0.1749  98  GLY   D O   
3438 N N   . GLY   D 85  ? 0.4033 0.3570 0.3124 -0.0305 -0.0162 0.1705  99  GLY   D N   
3439 C CA  . GLY   D 85  ? 0.3807 0.3609 0.3073 -0.0092 0.0007  0.1556  99  GLY   D CA  
3440 C C   . GLY   D 85  ? 0.3673 0.3523 0.2752 0.0065  0.0028  0.1540  99  GLY   D C   
3441 O O   . GLY   D 85  ? 0.3826 0.3491 0.2767 0.0130  -0.0151 0.1409  99  GLY   D O   
3442 N N   . ALA   D 86  ? 0.3338 0.3479 0.2661 0.0128  0.0352  0.1401  100 ALA   D N   
3443 C CA  . ALA   D 86  ? 0.3129 0.3364 0.2548 0.0143  0.0365  0.1295  100 ALA   D CA  
3444 C C   . ALA   D 86  ? 0.3270 0.3393 0.2629 0.0006  0.0259  0.1179  100 ALA   D C   
3445 O O   . ALA   D 86  ? 0.3524 0.3606 0.2861 -0.0100 0.0255  0.1017  100 ALA   D O   
3446 C CB  . ALA   D 86  ? 0.3178 0.3309 0.2630 0.0310  0.0305  0.1268  100 ALA   D CB  
3447 N N   . GLU   D 87  ? 0.3609 0.3202 0.2513 -0.0067 0.0153  0.1369  101 GLU   D N   
3448 C CA  . GLU   D 87  ? 0.3815 0.3191 0.2617 -0.0235 0.0152  0.1149  101 GLU   D CA  
3449 C C   . GLU   D 87  ? 0.3310 0.2878 0.2269 -0.0368 0.0147  0.1035  101 GLU   D C   
3450 O O   . GLU   D 87  ? 0.3377 0.2830 0.2522 -0.0358 0.0222  0.0746  101 GLU   D O   
3451 C CB  . GLU   D 87  ? 0.4289 0.3404 0.3390 -0.0368 0.0236  0.1111  101 GLU   D CB  
3452 C CG  . GLU   D 87  ? 0.4621 0.3687 0.4170 -0.0336 0.0337  0.1044  101 GLU   D CG  
3453 C CD  . GLU   D 87  ? 0.5073 0.3916 0.4740 -0.0362 0.0325  0.1071  101 GLU   D CD  
3454 O OE1 . GLU   D 87  ? 0.5176 0.4027 0.5066 -0.0338 0.0392  0.0971  101 GLU   D OE1 
3455 O OE2 . GLU   D 87  ? 0.5405 0.3994 0.5063 -0.0407 0.0388  0.1100  101 GLU   D OE2 
3456 N N   . ALA   D 88  ? 0.2708 0.2698 0.1979 -0.0401 0.0061  0.0992  102 ALA   D N   
3457 C CA  . ALA   D 88  ? 0.2802 0.2552 0.1755 -0.0307 -0.0069 0.0853  102 ALA   D CA  
3458 C C   . ALA   D 88  ? 0.2483 0.2301 0.1599 -0.0300 0.0036  0.0665  102 ALA   D C   
3459 O O   . ALA   D 88  ? 0.2297 0.2288 0.1634 -0.0374 0.0031  0.0685  102 ALA   D O   
3460 C CB  . ALA   D 88  ? 0.2986 0.2669 0.1844 -0.0269 -0.0621 0.0612  102 ALA   D CB  
3461 N N   . ARG   D 89  ? 0.2342 0.2049 0.1273 -0.0349 0.0034  0.0598  103 ARG   D N   
3462 C CA  . ARG   D 89  ? 0.2230 0.2037 0.1218 -0.0387 0.0007  0.0445  103 ARG   D CA  
3463 C C   . ARG   D 89  ? 0.1976 0.2108 0.1211 -0.0512 0.0026  0.0429  103 ARG   D C   
3464 O O   . ARG   D 89  ? 0.2131 0.2430 0.1558 -0.0583 -0.0131 0.0621  103 ARG   D O   
3465 C CB  . ARG   D 89  ? 0.2847 0.2016 0.1806 -0.0157 -0.0034 0.0303  103 ARG   D CB  
3466 C CG  . ARG   D 89  ? 0.3021 0.2094 0.2203 -0.0220 -0.0017 0.0213  103 ARG   D CG  
3467 C CD  . ARG   D 89  ? 0.3274 0.2162 0.2770 -0.0340 -0.0214 0.0123  103 ARG   D CD  
3468 N NE  . ARG   D 89  ? 0.3712 0.2355 0.3476 -0.0470 -0.0019 0.0276  103 ARG   D NE  
3469 C CZ  . ARG   D 89  ? 0.4140 0.2526 0.3948 -0.0791 0.0205  0.0205  103 ARG   D CZ  
3470 N NH1 . ARG   D 89  ? 0.4164 0.2636 0.4048 -0.0865 0.0342  0.0179  103 ARG   D NH1 
3471 N NH2 . ARG   D 89  ? 0.4389 0.2630 0.4264 -0.0878 0.0126  0.0297  103 ARG   D NH2 
3472 N N   . ILE   D 90  ? 0.1899 0.1818 0.1075 -0.0281 -0.0095 0.0313  104 ILE   D N   
3473 C CA  . ILE   D 90  ? 0.1946 0.1767 0.1143 -0.0292 -0.0035 0.0269  104 ILE   D CA  
3474 C C   . ILE   D 90  ? 0.1748 0.1783 0.1117 -0.0106 -0.0063 0.0282  104 ILE   D C   
3475 O O   . ILE   D 90  ? 0.1804 0.2022 0.1206 -0.0225 -0.0006 0.0160  104 ILE   D O   
3476 C CB  . ILE   D 90  ? 0.1773 0.1848 0.1171 -0.0468 -0.0055 0.0277  104 ILE   D CB  
3477 C CG1 . ILE   D 90  ? 0.2035 0.1837 0.1360 -0.0282 -0.0166 0.0156  104 ILE   D CG1 
3478 C CG2 . ILE   D 90  ? 0.2191 0.1966 0.1280 -0.0421 -0.0193 0.0339  104 ILE   D CG2 
3479 C CD1 . ILE   D 90  ? 0.2275 0.1823 0.1740 -0.0350 -0.0108 0.0107  104 ILE   D CD1 
3480 N N   . ASN   D 91  ? 0.1791 0.1578 0.1055 -0.0033 0.0060  0.0182  105 ASN   D N   
3481 C CA  . ASN   D 91  ? 0.1828 0.1454 0.1200 0.0119  0.0084  0.0192  105 ASN   D CA  
3482 C C   . ASN   D 91  ? 0.1768 0.1425 0.0950 -0.0072 -0.0028 0.0132  105 ASN   D C   
3483 O O   . ASN   D 91  ? 0.1695 0.1471 0.1294 -0.0096 -0.0027 0.0222  105 ASN   D O   
3484 C CB  . ASN   D 91  ? 0.2075 0.1524 0.1756 0.0250  0.0188  0.0444  105 ASN   D CB  
3485 C CG  . ASN   D 91  ? 0.2221 0.1729 0.2384 0.0079  0.0347  0.0612  105 ASN   D CG  
3486 O OD1 . ASN   D 91  ? 0.2385 0.1842 0.2552 -0.0022 0.0511  0.0701  105 ASN   D OD1 
3487 N ND2 . ASN   D 91  ? 0.2527 0.1755 0.2765 0.0175  0.0178  0.0659  105 ASN   D ND2 
3488 N N   . THR   D 92  ? 0.1722 0.1422 0.1007 0.0084  0.0028  0.0093  106 THR   D N   
3489 C CA  . THR   D 92  ? 0.1681 0.1469 0.0884 0.0110  0.0124  0.0149  106 THR   D CA  
3490 C C   . THR   D 92  ? 0.1500 0.1399 0.1087 0.0037  0.0019  0.0152  106 THR   D C   
3491 O O   . THR   D 92  ? 0.1592 0.1382 0.1188 -0.0060 0.0035  0.0018  106 THR   D O   
3492 C CB  . THR   D 92  ? 0.1471 0.1572 0.1162 0.0058  -0.0001 -0.0092 106 THR   D CB  
3493 O OG1 . THR   D 92  ? 0.1373 0.1473 0.1384 -0.0033 0.0067  -0.0051 106 THR   D OG1 
3494 C CG2 . THR   D 92  ? 0.1918 0.1578 0.1064 0.0094  0.0029  -0.0072 106 THR   D CG2 
3495 N N   . GLN   D 93  ? 0.1471 0.1354 0.0943 -0.0006 0.0056  -0.0019 107 GLN   D N   
3496 C CA  . GLN   D 93  ? 0.1489 0.1351 0.0861 0.0191  -0.0013 -0.0093 107 GLN   D CA  
3497 C C   . GLN   D 93  ? 0.1220 0.1277 0.1165 0.0122  0.0058  -0.0121 107 GLN   D C   
3498 O O   . GLN   D 93  ? 0.1382 0.1416 0.1412 0.0038  -0.0238 -0.0055 107 GLN   D O   
3499 C CB  . GLN   D 93  ? 0.1775 0.1317 0.1172 0.0428  0.0031  -0.0070 107 GLN   D CB  
3500 C CG  . GLN   D 93  ? 0.1965 0.1352 0.1422 0.0260  0.0188  -0.0157 107 GLN   D CG  
3501 C CD  . GLN   D 93  ? 0.1767 0.1562 0.1432 0.0260  -0.0069 -0.0018 107 GLN   D CD  
3502 O OE1 . GLN   D 93  ? 0.1996 0.1821 0.1865 -0.0006 0.0037  0.0072  107 GLN   D OE1 
3503 N NE2 . GLN   D 93  ? 0.1599 0.1820 0.1446 0.0446  -0.0049 -0.0082 107 GLN   D NE2 
3504 N N   . TRP   D 94  ? 0.1425 0.1277 0.1142 0.0288  -0.0023 0.0078  108 TRP   D N   
3505 C CA  . TRP   D 94  ? 0.1365 0.1352 0.1065 0.0141  -0.0143 0.0016  108 TRP   D CA  
3506 C C   . TRP   D 94  ? 0.1464 0.1259 0.1027 0.0089  -0.0084 -0.0079 108 TRP   D C   
3507 O O   . TRP   D 94  ? 0.1411 0.1370 0.1059 0.0040  -0.0079 -0.0152 108 TRP   D O   
3508 C CB  . TRP   D 94  ? 0.1518 0.1613 0.0939 0.0061  -0.0092 -0.0052 108 TRP   D CB  
3509 C CG  . TRP   D 94  ? 0.1435 0.1622 0.1112 0.0077  -0.0007 -0.0054 108 TRP   D CG  
3510 C CD1 . TRP   D 94  ? 0.1575 0.1757 0.1287 0.0009  0.0072  0.0099  108 TRP   D CD1 
3511 C CD2 . TRP   D 94  ? 0.1453 0.1699 0.1203 0.0177  0.0034  -0.0032 108 TRP   D CD2 
3512 N NE1 . TRP   D 94  ? 0.1612 0.1806 0.1389 0.0085  0.0095  0.0147  108 TRP   D NE1 
3513 C CE2 . TRP   D 94  ? 0.1594 0.1836 0.1141 0.0172  0.0035  0.0070  108 TRP   D CE2 
3514 C CE3 . TRP   D 94  ? 0.1423 0.1782 0.1125 0.0285  -0.0062 -0.0110 108 TRP   D CE3 
3515 C CZ2 . TRP   D 94  ? 0.1590 0.2000 0.1383 0.0206  0.0029  0.0033  108 TRP   D CZ2 
3516 C CZ3 . TRP   D 94  ? 0.1561 0.1874 0.1283 0.0036  -0.0057 -0.0010 108 TRP   D CZ3 
3517 C CH2 . TRP   D 94  ? 0.1669 0.1984 0.1308 0.0058  0.0069  -0.0124 108 TRP   D CH2 
3518 N N   . LEU   D 95  ? 0.1387 0.1281 0.1054 0.0124  -0.0004 -0.0015 109 LEU   D N   
3519 C CA  . LEU   D 95  ? 0.1661 0.1371 0.1081 0.0316  0.0006  0.0075  109 LEU   D CA  
3520 C C   . LEU   D 95  ? 0.1586 0.1460 0.1162 0.0397  -0.0234 -0.0250 109 LEU   D C   
3521 O O   . LEU   D 95  ? 0.1932 0.1741 0.1564 0.0551  -0.0482 -0.0671 109 LEU   D O   
3522 C CB  . LEU   D 95  ? 0.1608 0.1338 0.1255 0.0191  -0.0184 0.0022  109 LEU   D CB  
3523 C CG  . LEU   D 95  ? 0.1596 0.1334 0.1460 0.0217  0.0074  -0.0024 109 LEU   D CG  
3524 C CD1 . LEU   D 95  ? 0.1836 0.1401 0.1850 0.0171  0.0242  0.0246  109 LEU   D CD1 
3525 C CD2 . LEU   D 95  ? 0.1830 0.1540 0.1799 0.0055  0.0119  -0.0272 109 LEU   D CD2 
3526 N N   . LEU   D 96  ? 0.1593 0.1384 0.1228 0.0350  -0.0216 -0.0174 110 LEU   D N   
3527 C CA  A LEU   D 96  ? 0.1638 0.1482 0.1235 0.0289  -0.0071 -0.0187 110 LEU   D CA  
3528 C CA  B LEU   D 96  ? 0.1639 0.1460 0.1236 0.0376  -0.0150 -0.0144 110 LEU   D CA  
3529 C C   . LEU   D 96  ? 0.1713 0.1424 0.1205 0.0365  -0.0156 -0.0158 110 LEU   D C   
3530 O O   . LEU   D 96  ? 0.1863 0.1544 0.1175 0.0341  -0.0305 -0.0314 110 LEU   D O   
3531 C CB  A LEU   D 96  ? 0.1763 0.1613 0.1402 0.0194  -0.0137 -0.0190 110 LEU   D CB  
3532 C CB  B LEU   D 96  ? 0.1753 0.1547 0.1326 0.0453  -0.0312 -0.0059 110 LEU   D CB  
3533 C CG  A LEU   D 96  ? 0.1799 0.1754 0.1409 0.0086  -0.0228 -0.0216 110 LEU   D CG  
3534 C CG  B LEU   D 96  ? 0.1840 0.1665 0.1215 0.0503  -0.0350 0.0018  110 LEU   D CG  
3535 C CD1 A LEU   D 96  ? 0.1733 0.1817 0.1380 -0.0025 -0.0241 -0.0353 110 LEU   D CD1 
3536 C CD1 B LEU   D 96  ? 0.1929 0.1689 0.1104 0.0593  -0.0120 -0.0194 110 LEU   D CD1 
3537 C CD2 A LEU   D 96  ? 0.2024 0.1881 0.1623 0.0200  -0.0059 -0.0183 110 LEU   D CD2 
3538 C CD2 B LEU   D 96  ? 0.1814 0.1744 0.1143 0.0528  -0.0335 0.0147  110 LEU   D CD2 
3539 N N   . THR   D 97  ? 0.1754 0.1393 0.1442 0.0336  -0.0253 -0.0142 111 THR   D N   
3540 C CA  . THR   D 97  ? 0.1825 0.1438 0.1307 0.0498  -0.0375 -0.0111 111 THR   D CA  
3541 C C   . THR   D 97  ? 0.2261 0.1543 0.1227 0.0669  -0.0484 -0.0464 111 THR   D C   
3542 O O   . THR   D 97  ? 0.2358 0.1723 0.1382 0.0673  -0.0540 -0.0455 111 THR   D O   
3543 C CB  . THR   D 97  ? 0.1901 0.1532 0.1519 0.0538  -0.0275 0.0062  111 THR   D CB  
3544 O OG1 . THR   D 97  ? 0.1971 0.1554 0.1540 0.0461  -0.0035 0.0034  111 THR   D OG1 
3545 C CG2 . THR   D 97  ? 0.2295 0.1634 0.1619 0.0431  -0.0304 0.0165  111 THR   D CG2 
3546 N N   . SER   D 98  ? 0.2151 0.1739 0.1306 0.0851  -0.0537 -0.0362 112 SER   D N   
3547 C CA  . SER   D 98  ? 0.2369 0.1927 0.1508 0.0982  -0.0675 -0.0405 112 SER   D CA  
3548 C C   . SER   D 98  ? 0.2594 0.1914 0.1498 0.1239  -0.0466 -0.0439 112 SER   D C   
3549 O O   . SER   D 98  ? 0.2902 0.2028 0.1410 0.1278  -0.0226 -0.0231 112 SER   D O   
3550 C CB  . SER   D 98  ? 0.2483 0.2082 0.2048 0.0905  -0.0651 -0.0259 112 SER   D CB  
3551 O OG  . SER   D 98  ? 0.2622 0.2249 0.2707 0.0761  -0.0345 -0.0344 112 SER   D OG  
3552 N N   . GLY   D 99  ? 0.2795 0.1946 0.1465 0.1277  -0.0498 -0.0354 113 GLY   D N   
3553 C CA  . GLY   D 99  ? 0.3064 0.2205 0.1580 0.1254  -0.0611 -0.0222 113 GLY   D CA  
3554 C C   . GLY   D 99  ? 0.3051 0.2538 0.1699 0.1278  -0.0559 -0.0187 113 GLY   D C   
3555 O O   . GLY   D 99  ? 0.3206 0.2908 0.1899 0.1119  -0.0641 0.0003  113 GLY   D O   
3556 N N   . THR   D 100 ? 0.2952 0.2475 0.1493 0.1281  -0.0690 -0.0226 114 THR   D N   
3557 C CA  . THR   D 100 ? 0.3237 0.2519 0.1545 0.1294  -0.0574 -0.0173 114 THR   D CA  
3558 C C   . THR   D 100 ? 0.3535 0.2555 0.1577 0.1436  -0.0755 -0.0212 114 THR   D C   
3559 O O   . THR   D 100 ? 0.3976 0.2537 0.1637 0.1526  -0.0701 -0.0246 114 THR   D O   
3560 C CB  . THR   D 100 ? 0.3071 0.2472 0.1814 0.1099  -0.0778 -0.0209 114 THR   D CB  
3561 O OG1 . THR   D 100 ? 0.3067 0.2300 0.2072 0.1206  -0.0719 -0.0390 114 THR   D OG1 
3562 C CG2 . THR   D 100 ? 0.2972 0.2524 0.1974 0.1166  -0.0546 -0.0078 114 THR   D CG2 
3563 N N   . THR   D 101 ? 0.3811 0.2688 0.1699 0.1663  -0.0610 -0.0122 115 THR   D N   
3564 C CA  . THR   D 101 ? 0.3920 0.2858 0.1768 0.1668  -0.0714 -0.0130 115 THR   D CA  
3565 C C   . THR   D 101 ? 0.4197 0.2835 0.1738 0.1540  -0.0463 -0.0048 115 THR   D C   
3566 O O   . THR   D 101 ? 0.3732 0.2732 0.1594 0.1547  -0.0628 -0.0171 115 THR   D O   
3567 C CB  . THR   D 101 ? 0.4265 0.3117 0.2043 0.1867  -0.0886 -0.0258 115 THR   D CB  
3568 O OG1 . THR   D 101 ? 0.4731 0.3294 0.2251 0.1870  -0.1048 -0.0392 115 THR   D OG1 
3569 C CG2 . THR   D 101 ? 0.4273 0.3166 0.2220 0.1962  -0.0772 -0.0155 115 THR   D CG2 
3570 N N   . GLU   D 102 ? 0.4605 0.2895 0.2109 0.1317  -0.0174 0.0023  116 GLU   D N   
3571 C CA  . GLU   D 102 ? 0.4496 0.2902 0.2190 0.1225  -0.0197 0.0052  116 GLU   D CA  
3572 C C   . GLU   D 102 ? 0.4467 0.2708 0.1920 0.1433  -0.0518 0.0013  116 GLU   D C   
3573 O O   . GLU   D 102 ? 0.4519 0.2568 0.1930 0.1450  -0.0310 0.0230  116 GLU   D O   
3574 C CB  . GLU   D 102 ? 0.4606 0.3107 0.2599 0.0766  -0.0051 -0.0109 116 GLU   D CB  
3575 C CG  . GLU   D 102 ? 0.4493 0.3298 0.3009 0.0488  -0.0033 -0.0128 116 GLU   D CG  
3576 C CD  . GLU   D 102 ? 0.4249 0.3427 0.3082 0.0355  0.0014  -0.0210 116 GLU   D CD  
3577 O OE1 . GLU   D 102 ? 0.4231 0.3428 0.3136 0.0354  0.0201  -0.0176 116 GLU   D OE1 
3578 O OE2 . GLU   D 102 ? 0.4053 0.3530 0.3069 0.0281  -0.0123 -0.0334 116 GLU   D OE2 
3579 N N   . ALA   D 103 ? 0.4699 0.2710 0.1831 0.1630  -0.0683 -0.0052 117 ALA   D N   
3580 C CA  . ALA   D 103 ? 0.4430 0.2756 0.1929 0.1626  -0.0962 -0.0230 117 ALA   D CA  
3581 C C   . ALA   D 103 ? 0.4320 0.2725 0.1850 0.1768  -0.0968 -0.0487 117 ALA   D C   
3582 O O   . ALA   D 103 ? 0.4543 0.2794 0.2149 0.1761  -0.1218 -0.0547 117 ALA   D O   
3583 C CB  . ALA   D 103 ? 0.4660 0.2892 0.2094 0.1553  -0.1102 -0.0144 117 ALA   D CB  
3584 N N   . ASN   D 104 ? 0.3800 0.2762 0.1868 0.1602  -0.1018 -0.0470 118 ASN   D N   
3585 C CA  . ASN   D 104 ? 0.3445 0.2812 0.1958 0.1501  -0.1054 -0.0445 118 ASN   D CA  
3586 C C   . ASN   D 104 ? 0.2947 0.2436 0.1685 0.1166  -0.0934 -0.0264 118 ASN   D C   
3587 O O   . ASN   D 104 ? 0.3039 0.2383 0.1668 0.1095  -0.0840 -0.0457 118 ASN   D O   
3588 C CB  . ASN   D 104 ? 0.3402 0.3190 0.2571 0.1279  -0.1230 -0.0449 118 ASN   D CB  
3589 C CG  . ASN   D 104 ? 0.3470 0.3421 0.3067 0.1010  -0.1408 -0.0735 118 ASN   D CG  
3590 O OD1 . ASN   D 104 ? 0.3733 0.3527 0.3460 0.0915  -0.1370 -0.0812 118 ASN   D OD1 
3591 N ND2 . ASN   D 104 ? 0.3489 0.3511 0.3457 0.0732  -0.1377 -0.0813 118 ASN   D ND2 
3592 N N   . ALA   D 105 ? 0.2831 0.2284 0.1695 0.1178  -0.0572 -0.0026 119 ALA   D N   
3593 C CA  . ALA   D 105 ? 0.2708 0.2156 0.1647 0.0994  -0.0848 -0.0194 119 ALA   D CA  
3594 C C   . ALA   D 105 ? 0.3116 0.2118 0.1323 0.1095  -0.0408 -0.0201 119 ALA   D C   
3595 O O   . ALA   D 105 ? 0.2850 0.2175 0.1296 0.1045  -0.0361 -0.0097 119 ALA   D O   
3596 C CB  . ALA   D 105 ? 0.2667 0.2278 0.1997 0.0800  -0.0922 -0.0181 119 ALA   D CB  
3597 N N   . TRP   D 106 ? 0.3547 0.2162 0.1555 0.1415  -0.0563 -0.0327 120 TRP   D N   
3598 C CA  . TRP   D 106 ? 0.4170 0.2206 0.1468 0.1323  -0.0402 -0.0345 120 TRP   D CA  
3599 C C   . TRP   D 106 ? 0.4301 0.2052 0.1576 0.1227  -0.0792 -0.0287 120 TRP   D C   
3600 O O   . TRP   D 106 ? 0.4801 0.2002 0.1625 0.1406  -0.0718 -0.0256 120 TRP   D O   
3601 C CB  . TRP   D 106 ? 0.4468 0.2385 0.1541 0.1265  -0.0640 -0.0419 120 TRP   D CB  
3602 C CG  . TRP   D 106 ? 0.4811 0.2516 0.1776 0.0857  -0.1099 -0.0463 120 TRP   D CG  
3603 C CD1 . TRP   D 106 ? 0.4860 0.2491 0.1919 0.0867  -0.1203 -0.0444 120 TRP   D CD1 
3604 C CD2 . TRP   D 106 ? 0.5143 0.2618 0.2179 0.0533  -0.1576 -0.0254 120 TRP   D CD2 
3605 N NE1 . TRP   D 106 ? 0.5004 0.2528 0.2155 0.0611  -0.1470 -0.0348 120 TRP   D NE1 
3606 C CE2 . TRP   D 106 ? 0.5242 0.2689 0.2552 0.0346  -0.1550 -0.0313 120 TRP   D CE2 
3607 C CE3 . TRP   D 106 ? 0.5591 0.2799 0.2720 0.0225  -0.1535 -0.0117 120 TRP   D CE3 
3608 C CZ2 . TRP   D 106 ? 0.5247 0.2899 0.2876 0.0064  -0.1874 -0.0224 120 TRP   D CZ2 
3609 C CZ3 . TRP   D 106 ? 0.5569 0.2912 0.3093 0.0075  -0.1708 -0.0044 120 TRP   D CZ3 
3610 C CH2 . TRP   D 106 ? 0.5468 0.2971 0.3170 -0.0002 -0.1744 -0.0104 120 TRP   D CH2 
3611 N N   . LYS   D 107 ? 0.3904 0.2188 0.1638 0.0646  -0.0999 -0.0389 121 LYS   D N   
3612 C CA  A LYS   D 107 ? 0.3549 0.2293 0.2176 0.0411  -0.1317 -0.0228 121 LYS   D CA  
3613 C CA  B LYS   D 107 ? 0.3377 0.2183 0.1837 0.0478  -0.0994 -0.0300 121 LYS   D CA  
3614 C C   . LYS   D 107 ? 0.3025 0.2093 0.1841 0.0476  -0.1154 -0.0205 121 LYS   D C   
3615 O O   . LYS   D 107 ? 0.2938 0.2284 0.2156 0.0175  -0.1062 -0.0032 121 LYS   D O   
3616 C CB  A LYS   D 107 ? 0.3708 0.2482 0.2973 0.0358  -0.1665 0.0007  121 LYS   D CB  
3617 C CB  B LYS   D 107 ? 0.3213 0.2240 0.2031 0.0326  -0.0927 -0.0316 121 LYS   D CB  
3618 C CG  A LYS   D 107 ? 0.3655 0.2719 0.3499 0.0104  -0.1900 0.0006  121 LYS   D CG  
3619 C CG  B LYS   D 107 ? 0.2998 0.2288 0.2177 0.0177  -0.0931 -0.0333 121 LYS   D CG  
3620 C CD  A LYS   D 107 ? 0.3647 0.2967 0.3928 0.0016  -0.1900 0.0039  121 LYS   D CD  
3621 C CD  B LYS   D 107 ? 0.2837 0.2300 0.2251 0.0079  -0.0883 -0.0335 121 LYS   D CD  
3622 C CE  A LYS   D 107 ? 0.3542 0.3180 0.4290 0.0013  -0.1900 0.0063  121 LYS   D CE  
3623 C CE  B LYS   D 107 ? 0.2712 0.2301 0.2237 0.0021  -0.0905 -0.0348 121 LYS   D CE  
3624 N NZ  A LYS   D 107 ? 0.3857 0.3318 0.4787 -0.0023 -0.1858 0.0047  121 LYS   D NZ  
3625 N NZ  B LYS   D 107 ? 0.2642 0.2300 0.2208 0.0001  -0.0943 -0.0363 121 LYS   D NZ  
3626 N N   . SER   D 108 ? 0.2789 0.1693 0.1454 0.0630  -0.0648 -0.0292 122 SER   D N   
3627 C CA  . SER   D 108 ? 0.2413 0.1569 0.1185 0.0500  -0.0326 -0.0076 122 SER   D CA  
3628 C C   . SER   D 108 ? 0.1846 0.1536 0.1219 0.0514  -0.0315 -0.0205 122 SER   D C   
3629 O O   . SER   D 108 ? 0.2138 0.1576 0.1290 0.0513  -0.0255 -0.0245 122 SER   D O   
3630 C CB  . SER   D 108 ? 0.2318 0.1602 0.1361 0.0536  -0.0355 -0.0023 122 SER   D CB  
3631 O OG  . SER   D 108 ? 0.2331 0.1851 0.1887 0.0034  0.0029  -0.0121 122 SER   D OG  
3632 N N   . THR   D 109 ? 0.1565 0.1486 0.1282 0.0396  -0.0289 -0.0300 123 THR   D N   
3633 C CA  . THR   D 109 ? 0.1670 0.1327 0.1342 0.0296  -0.0213 -0.0131 123 THR   D CA  
3634 C C   . THR   D 109 ? 0.1527 0.1334 0.1113 0.0202  -0.0107 -0.0258 123 THR   D C   
3635 O O   . THR   D 109 ? 0.1701 0.1368 0.1364 0.0199  -0.0067 -0.0244 123 THR   D O   
3636 C CB  . THR   D 109 ? 0.1632 0.1350 0.1475 0.0380  -0.0148 -0.0097 123 THR   D CB  
3637 O OG1 . THR   D 109 ? 0.1940 0.1396 0.1834 0.0289  -0.0167 0.0057  123 THR   D OG1 
3638 C CG2 . THR   D 109 ? 0.1592 0.1508 0.1342 0.0470  -0.0245 -0.0059 123 THR   D CG2 
3639 N N   . LEU   D 110 ? 0.1649 0.1312 0.1042 0.0227  -0.0242 -0.0104 124 LEU   D N   
3640 C CA  . LEU   D 110 ? 0.1652 0.1393 0.1055 0.0184  -0.0057 -0.0038 124 LEU   D CA  
3641 C C   . LEU   D 110 ? 0.1717 0.1371 0.0954 0.0169  -0.0248 -0.0101 124 LEU   D C   
3642 O O   . LEU   D 110 ? 0.1745 0.1434 0.1167 0.0261  -0.0314 -0.0292 124 LEU   D O   
3643 C CB  . LEU   D 110 ? 0.1527 0.1632 0.1327 0.0211  -0.0128 -0.0189 124 LEU   D CB  
3644 C CG  . LEU   D 110 ? 0.1658 0.1878 0.1484 0.0258  -0.0160 -0.0259 124 LEU   D CG  
3645 C CD1 . LEU   D 110 ? 0.1542 0.1961 0.1849 0.0142  0.0096  -0.0367 124 LEU   D CD1 
3646 C CD2 . LEU   D 110 ? 0.1786 0.1965 0.1641 0.0137  -0.0346 -0.0165 124 LEU   D CD2 
3647 N N   . VAL   D 111 ? 0.1688 0.1421 0.1126 0.0047  -0.0158 -0.0045 125 VAL   D N   
3648 C CA  . VAL   D 111 ? 0.1480 0.1444 0.1071 0.0108  -0.0052 -0.0084 125 VAL   D CA  
3649 C C   . VAL   D 111 ? 0.1588 0.1446 0.1101 -0.0037 -0.0094 -0.0274 125 VAL   D C   
3650 O O   . VAL   D 111 ? 0.1640 0.1495 0.1253 -0.0004 -0.0126 -0.0184 125 VAL   D O   
3651 C CB  . VAL   D 111 ? 0.1629 0.1554 0.1261 0.0058  0.0017  -0.0191 125 VAL   D CB  
3652 C CG1 . VAL   D 111 ? 0.1922 0.1630 0.1222 0.0173  0.0152  -0.0296 125 VAL   D CG1 
3653 C CG2 . VAL   D 111 ? 0.1539 0.1645 0.1351 0.0269  0.0036  -0.0073 125 VAL   D CG2 
3654 N N   . GLY   D 112 ? 0.1593 0.1400 0.0967 0.0195  -0.0029 -0.0041 126 GLY   D N   
3655 C CA  . GLY   D 112 ? 0.1793 0.1437 0.1045 0.0011  -0.0005 -0.0037 126 GLY   D CA  
3656 C C   . GLY   D 112 ? 0.1661 0.1337 0.1040 0.0022  0.0056  -0.0011 126 GLY   D C   
3657 O O   . GLY   D 112 ? 0.1531 0.1489 0.1225 0.0048  0.0045  0.0012  126 GLY   D O   
3658 N N   . HIS   D 113 ? 0.1614 0.1440 0.1220 -0.0167 -0.0138 0.0121  127 HIS   D N   
3659 C CA  . HIS   D 113 ? 0.1684 0.1588 0.1117 -0.0183 0.0054  -0.0094 127 HIS   D CA  
3660 C C   . HIS   D 113 ? 0.1650 0.1801 0.1244 -0.0234 -0.0008 0.0024  127 HIS   D C   
3661 O O   . HIS   D 113 ? 0.2038 0.2070 0.1359 -0.0369 0.0007  0.0021  127 HIS   D O   
3662 C CB  . HIS   D 113 ? 0.1951 0.1657 0.1709 -0.0263 0.0016  -0.0153 127 HIS   D CB  
3663 C CG  . HIS   D 113 ? 0.2260 0.1885 0.2041 -0.0089 -0.0136 -0.0159 127 HIS   D CG  
3664 N ND1 . HIS   D 113 ? 0.2430 0.1977 0.2538 -0.0072 0.0014  -0.0411 127 HIS   D ND1 
3665 C CD2 . HIS   D 113 ? 0.2558 0.1977 0.2642 -0.0253 0.0200  -0.0213 127 HIS   D CD2 
3666 C CE1 . HIS   D 113 ? 0.2664 0.2074 0.2878 -0.0066 0.0042  -0.0353 127 HIS   D CE1 
3667 N NE2 . HIS   D 113 ? 0.2849 0.2043 0.3099 -0.0239 0.0123  -0.0291 127 HIS   D NE2 
3668 N N   . ASP   D 114 ? 0.1518 0.1779 0.1202 -0.0065 0.0073  -0.0002 128 ASP   D N   
3669 C CA  . ASP   D 114 ? 0.1487 0.1791 0.1055 -0.0138 -0.0034 -0.0067 128 ASP   D CA  
3670 C C   . ASP   D 114 ? 0.1644 0.1747 0.1144 -0.0218 -0.0056 -0.0011 128 ASP   D C   
3671 O O   . ASP   D 114 ? 0.1441 0.1689 0.1387 -0.0077 0.0011  0.0119  128 ASP   D O   
3672 C CB  . ASP   D 114 ? 0.1550 0.1962 0.1256 -0.0038 -0.0073 -0.0126 128 ASP   D CB  
3673 C CG  . ASP   D 114 ? 0.1780 0.2080 0.1734 -0.0134 -0.0150 -0.0254 128 ASP   D CG  
3674 O OD1 . ASP   D 114 ? 0.1888 0.2241 0.1810 -0.0185 -0.0240 -0.0119 128 ASP   D OD1 
3675 O OD2 . ASP   D 114 ? 0.1696 0.2117 0.1801 -0.0139 0.0029  0.0055  128 ASP   D OD2 
3676 N N   . THR   D 115 ? 0.2162 0.1842 0.0955 -0.0196 -0.0043 0.0097  129 THR   D N   
3677 C CA  A THR   D 115 ? 0.2401 0.1967 0.0909 0.0007  0.0006  0.0068  129 THR   D CA  
3678 C CA  B THR   D 115 ? 0.2221 0.1881 0.1055 -0.0173 0.0075  0.0104  129 THR   D CA  
3679 C C   . THR   D 115 ? 0.2062 0.1878 0.1129 -0.0136 0.0157  0.0125  129 THR   D C   
3680 O O   . THR   D 115 ? 0.1747 0.1735 0.1576 -0.0248 0.0208  -0.0015 129 THR   D O   
3681 C CB  A THR   D 115 ? 0.3242 0.2297 0.1356 0.0341  -0.0141 -0.0002 129 THR   D CB  
3682 C CB  B THR   D 115 ? 0.2462 0.1934 0.1313 -0.0187 0.0046  0.0100  129 THR   D CB  
3683 O OG1 A THR   D 115 ? 0.3595 0.2611 0.2085 0.0384  0.0108  -0.0052 129 THR   D OG1 
3684 O OG1 B THR   D 115 ? 0.2442 0.1925 0.1503 -0.0260 0.0016  0.0094  129 THR   D OG1 
3685 C CG2 A THR   D 115 ? 0.3198 0.2311 0.1343 0.0658  -0.0383 -0.0016 129 THR   D CG2 
3686 C CG2 B THR   D 115 ? 0.2512 0.1994 0.1522 -0.0096 0.0034  0.0150  129 THR   D CG2 
3687 N N   . PHE   D 116 ? 0.1908 0.1800 0.0939 -0.0163 -0.0160 0.0101  130 PHE   D N   
3688 C CA  . PHE   D 116 ? 0.2032 0.1729 0.0939 -0.0126 0.0049  0.0060  130 PHE   D CA  
3689 C C   . PHE   D 116 ? 0.1818 0.1840 0.1123 -0.0208 0.0064  0.0101  130 PHE   D C   
3690 O O   . PHE   D 116 ? 0.1792 0.1929 0.1257 -0.0175 0.0108  0.0169  130 PHE   D O   
3691 C CB  . PHE   D 116 ? 0.2046 0.1753 0.1089 -0.0190 -0.0011 0.0019  130 PHE   D CB  
3692 C CG  . PHE   D 116 ? 0.1851 0.1811 0.1142 -0.0208 0.0050  0.0092  130 PHE   D CG  
3693 C CD1 . PHE   D 116 ? 0.2105 0.1772 0.1076 -0.0321 -0.0028 0.0077  130 PHE   D CD1 
3694 C CD2 . PHE   D 116 ? 0.2025 0.1953 0.1360 -0.0132 0.0115  0.0047  130 PHE   D CD2 
3695 C CE1 . PHE   D 116 ? 0.2051 0.1684 0.1150 -0.0294 0.0052  0.0007  130 PHE   D CE1 
3696 C CE2 . PHE   D 116 ? 0.2188 0.1871 0.1354 -0.0149 0.0195  0.0143  130 PHE   D CE2 
3697 C CZ  . PHE   D 116 ? 0.2044 0.1730 0.1287 -0.0337 0.0083  0.0074  130 PHE   D CZ  
3698 N N   . THR   D 117 ? 0.1840 0.1878 0.0945 -0.0171 0.0065  0.0079  131 THR   D N   
3699 C CA  A THR   D 117 ? 0.2112 0.1913 0.1347 -0.0163 0.0042  -0.0023 131 THR   D CA  
3700 C CA  B THR   D 117 ? 0.1853 0.1938 0.1068 -0.0122 -0.0043 0.0122  131 THR   D CA  
3701 C C   . THR   D 117 ? 0.1824 0.1992 0.1056 -0.0083 0.0064  0.0107  131 THR   D C   
3702 O O   . THR   D 117 ? 0.1558 0.1847 0.1283 -0.0165 0.0003  0.0177  131 THR   D O   
3703 C CB  A THR   D 117 ? 0.3065 0.2016 0.2399 -0.0315 0.0407  -0.0134 131 THR   D CB  
3704 C CB  B THR   D 117 ? 0.1777 0.1937 0.1208 -0.0119 -0.0364 0.0170  131 THR   D CB  
3705 O OG1 A THR   D 117 ? 0.3480 0.2186 0.3363 -0.0498 0.0846  -0.0325 131 THR   D OG1 
3706 O OG1 B THR   D 117 ? 0.1682 0.1961 0.1290 -0.0081 -0.0636 0.0167  131 THR   D OG1 
3707 C CG2 A THR   D 117 ? 0.3579 0.2098 0.2844 -0.0347 0.0514  -0.0137 131 THR   D CG2 
3708 C CG2 B THR   D 117 ? 0.1734 0.1938 0.1366 -0.0175 -0.0431 0.0195  131 THR   D CG2 
3709 N N   . LYS   D 118 ? 0.1922 0.2284 0.1253 0.0114  0.0234  0.0133  132 LYS   D N   
3710 C CA  . LYS   D 118 ? 0.1769 0.2664 0.1186 0.0156  -0.0082 0.0241  132 LYS   D CA  
3711 C C   . LYS   D 118 ? 0.1915 0.2559 0.1351 -0.0055 0.0252  0.0485  132 LYS   D C   
3712 O O   . LYS   D 118 ? 0.1846 0.2384 0.1305 -0.0152 0.0260  0.0229  132 LYS   D O   
3713 C CB  . LYS   D 118 ? 0.1930 0.3182 0.1459 0.0035  -0.0177 -0.0050 132 LYS   D CB  
3714 C CG  . LYS   D 118 ? 0.1725 0.3559 0.1575 0.0004  -0.0188 -0.0342 132 LYS   D CG  
3715 C CD  . LYS   D 118 ? 0.2194 0.3885 0.2302 -0.0163 -0.0289 -0.0322 132 LYS   D CD  
3716 C CE  . LYS   D 118 ? 0.2483 0.4120 0.2694 -0.0254 -0.0321 -0.0405 132 LYS   D CE  
3717 N NZ  . LYS   D 118 ? 0.3044 0.4288 0.2948 -0.0178 -0.0310 -0.0471 132 LYS   D NZ  
3718 N N   . VAL   D 119 ? 0.2222 0.2730 0.1966 -0.0701 0.0325  0.0508  133 VAL   D N   
3719 C CA  . VAL   D 119 ? 0.2970 0.2957 0.2867 -0.1109 0.0375  0.0660  133 VAL   D CA  
3720 C C   . VAL   D 119 ? 0.2976 0.3282 0.4080 -0.1216 0.0479  0.0712  133 VAL   D C   
3721 O O   . VAL   D 119 ? 0.3275 0.3417 0.4096 -0.1136 -0.0359 0.0534  133 VAL   D O   
3722 C CB  . VAL   D 119 ? 0.3374 0.2971 0.3115 -0.1200 -0.0058 0.0605  133 VAL   D CB  
3723 C CG1 . VAL   D 119 ? 0.3400 0.3081 0.3422 -0.1345 -0.0114 0.0463  133 VAL   D CG1 
3724 C CG2 . VAL   D 119 ? 0.3763 0.2970 0.3290 -0.1065 -0.0104 0.0678  133 VAL   D CG2 
3725 N N   . LYS   D 120 ? 0.3945 0.3626 0.5056 -0.0984 0.0765  0.0734  134 LYS   D N   
3726 C CA  . LYS   D 120 ? 0.4349 0.3865 0.5573 -0.0950 0.0792  0.0473  134 LYS   D CA  
3727 C C   . LYS   D 120 ? 0.4315 0.3854 0.5358 -0.1154 0.0404  0.0341  134 LYS   D C   
3728 O O   . LYS   D 120 ? 0.4388 0.3890 0.5263 -0.1188 0.0187  0.0137  134 LYS   D O   
3729 C CB  . LYS   D 120 ? 0.4443 0.3982 0.5969 -0.1022 0.0907  0.0399  134 LYS   D CB  
3730 C CG  . LYS   D 120 ? 0.4700 0.4009 0.6213 -0.0998 0.0960  0.0300  134 LYS   D CG  
3731 C CD  . LYS   D 120 ? 0.4972 0.4086 0.6337 -0.0877 0.1029  0.0286  134 LYS   D CD  
3732 C CE  . LYS   D 120 ? 0.5025 0.4208 0.6482 -0.0785 0.0994  0.0291  134 LYS   D CE  
3733 N NZ  . LYS   D 120 ? 0.5013 0.4279 0.6583 -0.0704 0.0871  0.0320  134 LYS   D NZ  
3734 S S   . DMS   E .   ? 0.2084 0.2756 0.2366 -0.0136 0.0195  0.0231  301 DMS   A S   
3735 O O   . DMS   E .   ? 0.2684 0.2643 0.2824 -0.0106 0.0246  0.0023  301 DMS   A O   
3736 C C1  . DMS   E .   ? 0.2383 0.2887 0.2193 0.0135  0.0087  -0.0100 301 DMS   A C1  
3737 C C2  . DMS   E .   ? 0.1938 0.2797 0.2209 0.0019  0.0043  0.0415  301 DMS   A C2  
3738 S S   . DMS   F .   ? 0.1856 0.1568 0.1602 -0.0087 0.0044  -0.0129 302 DMS   A S   
3739 O O   . DMS   F .   ? 0.1706 0.1512 0.1375 -0.0307 0.0164  -0.0052 302 DMS   A O   
3740 C C1  . DMS   F .   ? 0.1441 0.1572 0.1405 -0.0165 -0.0143 -0.0044 302 DMS   A C1  
3741 C C2  . DMS   F .   ? 0.2096 0.1757 0.1850 -0.0028 0.0213  -0.0174 302 DMS   A C2  
3742 C C1  . A1LXQ G .   ? 0.3647 0.3601 0.3934 0.0304  -0.0542 -0.0513 201 A1LXQ B C1  
3743 C C10 . A1LXQ G .   ? 0.1915 0.2240 0.2328 -0.0079 -0.0031 -0.0609 201 A1LXQ B C10 
3744 C C11 . A1LXQ G .   ? 0.2965 0.2312 0.2882 0.0269  -0.0157 -0.0299 201 A1LXQ B C11 
3745 C C12 . A1LXQ G .   ? 0.1349 0.1536 0.1467 0.0054  0.0015  -0.0321 201 A1LXQ B C12 
3746 C C13 . A1LXQ G .   ? 0.0459 0.0859 0.0662 0.0166  -0.0179 -0.0399 201 A1LXQ B C13 
3747 C C14 . A1LXQ G .   ? 0.3970 0.3656 0.4209 0.0704  -0.0495 -0.0346 201 A1LXQ B C14 
3748 C C15 . A1LXQ G .   ? 0.3624 0.3432 0.3842 0.0894  -0.0640 -0.0423 201 A1LXQ B C15 
3749 C C16 . A1LXQ G .   ? 0.3894 0.3872 0.4331 0.0163  -0.0333 -0.0568 201 A1LXQ B C16 
3750 C C17 . A1LXQ G .   ? 0.4244 0.4020 0.4615 -0.0121 -0.0194 -0.0570 201 A1LXQ B C17 
3751 C C2  . A1LXQ G .   ? 0.3587 0.3620 0.3942 0.0258  -0.0518 -0.0528 201 A1LXQ B C2  
3752 C C3  . A1LXQ G .   ? 0.3295 0.3391 0.3621 0.0384  -0.0612 -0.0456 201 A1LXQ B C3  
3753 C C4  . A1LXQ G .   ? 0.3159 0.3183 0.3518 0.0415  -0.0467 -0.0398 201 A1LXQ B C4  
3754 C C5  . A1LXQ G .   ? 0.3366 0.3360 0.3578 0.0473  -0.0699 -0.0365 201 A1LXQ B C5  
3755 C C6  . A1LXQ G .   ? 0.3690 0.3552 0.3950 0.0477  -0.0565 -0.0387 201 A1LXQ B C6  
3756 C C7  . A1LXQ G .   ? 0.2856 0.2870 0.3265 0.0182  -0.0229 -0.0418 201 A1LXQ B C7  
3757 C C8  . A1LXQ G .   ? 0.2845 0.2662 0.3191 0.0105  -0.0248 -0.0424 201 A1LXQ B C8  
3758 C C9  . A1LXQ G .   ? 0.2473 0.2409 0.3065 0.0048  -0.0108 -0.0449 201 A1LXQ B C9  
3759 N N1  . A1LXQ G .   ? 0.2216 0.1977 0.2534 0.0251  -0.0227 -0.0291 201 A1LXQ B N1  
3760 O O1  . A1LXQ G .   ? 0.2316 0.2668 0.3090 0.0082  -0.0177 -0.0465 201 A1LXQ B O1  
3761 O O2  . A1LXQ G .   ? 0.3597 0.2401 0.3228 0.0388  -0.0467 -0.0210 201 A1LXQ B O2  
3762 O O3  . A1LXQ G .   ? 0.4058 0.3817 0.4449 0.0674  -0.0470 -0.0259 201 A1LXQ B O3  
3763 O O4  . A1LXQ G .   ? 0.3936 0.3556 0.4111 0.0922  -0.0524 -0.0405 201 A1LXQ B O4  
3764 O O5  . A1LXQ G .   ? 0.4109 0.3955 0.4394 0.0238  -0.0309 -0.0580 201 A1LXQ B O5  
3765 O O6  . A1LXQ G .   ? 0.4108 0.3986 0.4596 -0.0055 -0.0231 -0.0593 201 A1LXQ B O6  
3766 S S   . DMS   H .   ? 0.4565 0.2751 0.2754 0.0823  -0.0693 -0.0084 301 DMS   C S   
3767 O O   . DMS   H .   ? 0.4935 0.2904 0.2986 0.0790  -0.0533 -0.0118 301 DMS   C O   
3768 C C1  . DMS   H .   ? 0.4395 0.2775 0.2880 0.0897  -0.0546 -0.0233 301 DMS   C C1  
3769 C C2  . DMS   H .   ? 0.4316 0.2582 0.2223 0.0680  -0.0914 0.0046  301 DMS   C C2  
3770 S S   . DMS   I .   ? 0.2329 0.1835 0.2011 0.0170  -0.0115 -0.0261 302 DMS   C S   
3771 O O   . DMS   I .   ? 0.2549 0.1686 0.2005 0.0197  -0.0037 -0.0338 302 DMS   C O   
3772 C C1  . DMS   I .   ? 0.1971 0.1808 0.1910 0.0019  0.0063  -0.0392 302 DMS   C C1  
3773 C C2  . DMS   I .   ? 0.2758 0.2065 0.1768 0.0211  -0.0209 -0.0362 302 DMS   C C2  
3774 C C1  . A1LXQ J .   ? 0.1897 0.2649 0.2409 -0.0127 -0.0003 -0.0282 201 A1LXQ D C1  
3775 C C10 . A1LXQ J .   ? 0.1381 0.2418 0.1829 0.0019  -0.0331 -0.0263 201 A1LXQ D C10 
3776 C C11 . A1LXQ J .   ? 0.2146 0.2537 0.1772 0.0027  -0.0174 0.0012  201 A1LXQ D C11 
3777 C C12 . A1LXQ J .   ? 0.1788 0.2227 0.1706 0.0303  -0.0079 -0.0099 201 A1LXQ D C12 
3778 C C13 . A1LXQ J .   ? 0.1367 0.2360 0.2515 0.0085  -0.0036 -0.0507 201 A1LXQ D C13 
3779 C C14 . A1LXQ J .   ? 0.1893 0.2576 0.2313 0.0244  -0.0106 -0.0247 201 A1LXQ D C14 
3780 C C15 . A1LXQ J .   ? 0.2460 0.2714 0.2180 0.0520  0.0003  0.0100  201 A1LXQ D C15 
3781 C C16 . A1LXQ J .   ? 0.2019 0.2873 0.2666 -0.0107 -0.0044 -0.0438 201 A1LXQ D C16 
3782 C C17 . A1LXQ J .   ? 0.2986 0.3257 0.3368 0.0104  0.0202  -0.0324 201 A1LXQ D C17 
3783 C C2  . A1LXQ J .   ? 0.1744 0.2708 0.2291 -0.0162 -0.0077 -0.0409 201 A1LXQ D C2  
3784 C C3  . A1LXQ J .   ? 0.1817 0.2554 0.2123 -0.0142 0.0001  -0.0381 201 A1LXQ D C3  
3785 C C4  . A1LXQ J .   ? 0.1517 0.2451 0.1765 -0.0073 -0.0085 -0.0197 201 A1LXQ D C4  
3786 C C5  . A1LXQ J .   ? 0.1605 0.2404 0.1778 -0.0059 -0.0194 -0.0155 201 A1LXQ D C5  
3787 C C6  . A1LXQ J .   ? 0.1661 0.2530 0.2084 -0.0067 -0.0174 -0.0266 201 A1LXQ D C6  
3788 C C7  . A1LXQ J .   ? 0.1658 0.2457 0.1684 -0.0005 -0.0103 -0.0183 201 A1LXQ D C7  
3789 C C8  . A1LXQ J .   ? 0.1232 0.2304 0.1366 0.0171  0.0039  -0.0281 201 A1LXQ D C8  
3790 C C9  . A1LXQ J .   ? 0.1774 0.2420 0.1717 0.0027  -0.0057 -0.0137 201 A1LXQ D C9  
3791 N N1  . A1LXQ J .   ? 0.2185 0.2288 0.1972 0.0206  -0.0322 0.0023  201 A1LXQ D N1  
3792 O O1  . A1LXQ J .   ? 0.2065 0.2540 0.2394 -0.0123 -0.0056 -0.0303 201 A1LXQ D O1  
3793 O O2  . A1LXQ J .   ? 0.2355 0.2791 0.2133 -0.0110 -0.0145 -0.0097 201 A1LXQ D O2  
3794 O O3  . A1LXQ J .   ? 0.1925 0.2654 0.2464 0.0255  -0.0167 -0.0323 201 A1LXQ D O3  
3795 O O4  . A1LXQ J .   ? 0.2144 0.2660 0.2211 0.0545  -0.0092 -0.0056 201 A1LXQ D O4  
3796 O O5  . A1LXQ J .   ? 0.1732 0.2891 0.2282 -0.0293 -0.0082 -0.0498 201 A1LXQ D O5  
3797 O O6  . A1LXQ J .   ? 0.2562 0.3129 0.2940 0.0070  0.0328  -0.0443 201 A1LXQ D O6  
3798 O O   . HOH   K .   ? 0.3890 0.4275 0.5152 0.0957  0.0426  0.0063  401 HOH   A O   
3799 O O   . HOH   K .   ? 0.4329 0.4624 0.4746 -0.0908 0.0899  -0.0099 402 HOH   A O   
3800 O O   . HOH   K .   ? 0.4886 0.3539 0.4683 0.1607  -0.0766 0.1234  403 HOH   A O   
3801 O O   . HOH   K .   ? 0.5991 0.4301 0.5288 0.0026  0.2749  0.1420  404 HOH   A O   
3802 O O   . HOH   K .   ? 0.2648 0.3324 0.7634 0.0000  -0.0211 0.0980  405 HOH   A O   
3803 O O   . HOH   K .   ? 0.3343 0.2398 0.3568 0.0528  0.0072  -0.1047 406 HOH   A O   
3804 O O   . HOH   K .   ? 0.2906 0.4198 0.3076 0.0190  0.0382  0.1765  407 HOH   A O   
3805 O O   . HOH   K .   ? 0.5632 0.6105 0.4270 -0.0239 0.0625  -0.0672 408 HOH   A O   
3806 O O   . HOH   K .   ? 0.5860 0.7202 0.7734 -0.1041 -0.0886 0.0388  409 HOH   A O   
3807 O O   . HOH   K .   ? 0.5572 0.4748 0.3565 0.0447  -0.1785 -0.0381 410 HOH   A O   
3808 O O   . HOH   K .   ? 0.5202 0.2944 0.4675 0.0898  -0.1864 -0.0982 411 HOH   A O   
3809 O O   . HOH   K .   ? 0.3514 0.2041 0.1876 0.0058  0.0098  -0.0055 412 HOH   A O   
3810 O O   . HOH   K .   ? 0.2734 0.2220 0.2373 -0.0545 0.0573  0.0086  413 HOH   A O   
3811 O O   . HOH   K .   ? 0.3377 0.4093 0.3473 0.0225  -0.1334 -0.0338 414 HOH   A O   
3812 O O   . HOH   K .   ? 0.3883 0.4964 0.5692 0.0611  0.1455  -0.0893 415 HOH   A O   
3813 O O   . HOH   K .   ? 0.6590 0.6107 0.6271 0.0592  0.1148  0.0226  416 HOH   A O   
3814 O O   . HOH   K .   ? 0.1584 0.1750 0.2339 0.0002  0.0280  -0.0020 417 HOH   A O   
3815 O O   . HOH   K .   ? 0.3185 0.5825 0.3762 0.1389  0.0505  0.2017  418 HOH   A O   
3816 O O   . HOH   K .   ? 0.3318 0.7877 0.3202 0.0208  0.1165  -0.0068 419 HOH   A O   
3817 O O   . HOH   K .   ? 0.3010 0.7726 0.3791 0.1229  0.0685  0.1052  420 HOH   A O   
3818 O O   . HOH   K .   ? 0.1575 0.1272 0.1329 -0.0095 0.0021  -0.0175 421 HOH   A O   
3819 O O   . HOH   K .   ? 0.3314 0.5859 0.4698 0.1487  -0.1420 -0.0637 422 HOH   A O   
3820 O O   . HOH   K .   ? 0.2189 0.2514 0.2003 0.0131  0.0214  -0.0531 423 HOH   A O   
3821 O O   . HOH   K .   ? 0.3559 0.5288 0.5341 0.1285  0.1994  0.2457  424 HOH   A O   
3822 O O   . HOH   K .   ? 0.6817 0.2514 0.2507 -0.1567 -0.0761 0.0498  425 HOH   A O   
3823 O O   . HOH   K .   ? 0.6831 0.5657 0.4337 -0.0351 -0.0371 0.1739  426 HOH   A O   
3824 O O   . HOH   K .   ? 0.2480 0.2598 0.1721 0.1105  -0.0519 -0.0189 427 HOH   A O   
3825 O O   . HOH   K .   ? 0.2401 0.2628 0.3969 -0.0895 0.0621  -0.0885 428 HOH   A O   
3826 O O   . HOH   K .   ? 0.1990 0.1965 0.2480 0.0063  0.0270  -0.0194 429 HOH   A O   
3827 O O   . HOH   K .   ? 0.3999 0.2757 0.4331 -0.0846 -0.0226 0.0132  430 HOH   A O   
3828 O O   . HOH   K .   ? 0.1295 0.1478 0.1272 0.0081  0.0029  -0.0127 431 HOH   A O   
3829 O O   . HOH   K .   ? 0.3686 0.2849 0.3459 -0.0435 0.0434  -0.0144 432 HOH   A O   
3830 O O   . HOH   K .   ? 0.6648 0.3827 0.2497 -0.1900 -0.0737 0.0472  433 HOH   A O   
3831 O O   . HOH   K .   ? 0.4737 0.3671 0.4645 0.1660  0.0130  -0.1217 434 HOH   A O   
3832 O O   . HOH   K .   ? 0.4035 0.2238 0.2517 -0.0128 0.0599  -0.0530 435 HOH   A O   
3833 O O   . HOH   K .   ? 0.4737 0.1936 0.2083 0.1222  -0.0764 -0.0126 436 HOH   A O   
3834 O O   . HOH   K .   ? 0.4730 0.2476 0.4331 0.1015  -0.1410 -0.0285 437 HOH   A O   
3835 O O   . HOH   K .   ? 0.5025 0.4064 0.4893 0.1838  0.1029  -0.0502 438 HOH   A O   
3836 O O   . HOH   K .   ? 0.1978 0.1792 0.2448 0.0114  0.0525  -0.0075 439 HOH   A O   
3837 O O   . HOH   K .   ? 0.3915 0.1945 0.2252 0.0314  -0.0394 -0.0381 440 HOH   A O   
3838 O O   . HOH   K .   ? 0.4263 0.2833 0.4161 0.1186  -0.0031 -0.0021 441 HOH   A O   
3839 O O   . HOH   K .   ? 0.2221 0.2702 0.3222 -0.0500 -0.0147 -0.0230 442 HOH   A O   
3840 O O   . HOH   K .   ? 0.6334 0.4121 0.7496 0.2610  -0.0208 0.1283  443 HOH   A O   
3841 O O   . HOH   K .   ? 0.4791 0.4765 0.2393 -0.0242 0.0794  0.1213  444 HOH   A O   
3842 O O   . HOH   K .   ? 0.3277 0.3411 0.3669 0.1428  0.0595  0.1687  445 HOH   A O   
3843 O O   . HOH   K .   ? 0.1923 0.1836 0.1380 0.0101  -0.0083 0.0001  446 HOH   A O   
3844 O O   . HOH   K .   ? 0.3298 0.2417 0.3867 -0.0580 0.0557  -0.0567 447 HOH   A O   
3845 O O   . HOH   K .   ? 0.2781 0.1365 0.2615 0.0083  -0.1145 -0.0102 448 HOH   A O   
3846 O O   . HOH   K .   ? 0.1631 0.1347 0.1542 -0.0033 -0.0038 0.0102  449 HOH   A O   
3847 O O   . HOH   K .   ? 0.2608 0.1741 0.2057 -0.0515 0.0534  -0.0227 450 HOH   A O   
3848 O O   . HOH   K .   ? 0.2300 0.2316 0.2295 -0.0021 0.0695  -0.0396 451 HOH   A O   
3849 O O   . HOH   K .   ? 0.4587 0.5471 0.4749 0.2157  -0.0295 -0.0236 452 HOH   A O   
3850 O O   . HOH   K .   ? 0.2657 0.2282 0.2459 0.0198  0.0155  0.0535  453 HOH   A O   
3851 O O   . HOH   K .   ? 0.2391 0.1739 0.2047 -0.0106 0.0212  -0.0050 454 HOH   A O   
3852 O O   . HOH   K .   ? 0.2252 0.1812 0.3111 -0.0311 0.0230  0.0339  455 HOH   A O   
3853 O O   . HOH   K .   ? 0.3131 0.5436 0.3175 -0.0048 0.0048  0.0629  456 HOH   A O   
3854 O O   . HOH   K .   ? 0.6077 0.2583 0.4427 0.1078  -0.0205 -0.0611 457 HOH   A O   
3855 O O   . HOH   K .   ? 0.3758 0.1803 0.2408 0.0930  -0.0467 -0.0353 458 HOH   A O   
3856 O O   . HOH   K .   ? 0.5163 0.5221 0.3072 -0.0846 0.0803  -0.1327 459 HOH   A O   
3857 O O   . HOH   K .   ? 0.3248 0.2540 0.5110 0.1087  -0.1811 -0.1402 460 HOH   A O   
3858 O O   . HOH   K .   ? 0.1536 0.1672 0.1484 -0.0132 -0.0110 -0.0109 461 HOH   A O   
3859 O O   . HOH   K .   ? 0.4329 0.5065 0.6555 0.1958  -0.0829 0.1045  462 HOH   A O   
3860 O O   . HOH   K .   ? 0.2474 0.1976 0.2351 0.0028  -0.0074 -0.0445 463 HOH   A O   
3861 O O   . HOH   K .   ? 0.6441 0.4733 0.4334 -0.0271 0.2388  0.1361  464 HOH   A O   
3862 O O   . HOH   K .   ? 0.4400 0.5119 0.5862 -0.0319 0.0862  -0.0317 465 HOH   A O   
3863 O O   . HOH   K .   ? 0.7302 0.5353 0.4760 0.1323  -0.0812 -0.1801 466 HOH   A O   
3864 O O   . HOH   K .   ? 0.6364 0.3843 0.4247 0.0886  0.1526  0.1607  467 HOH   A O   
3865 O O   . HOH   K .   ? 0.4366 0.2842 0.5421 0.1140  -0.0654 -0.0556 468 HOH   A O   
3866 O O   . HOH   K .   ? 0.6737 0.2408 0.2116 -0.0977 -0.0329 -0.0118 469 HOH   A O   
3867 O O   . HOH   K .   ? 0.3503 0.5016 0.2758 0.0500  -0.0518 -0.0230 470 HOH   A O   
3868 O O   . HOH   K .   ? 0.2807 0.2180 0.2051 -0.0564 -0.0280 0.0541  471 HOH   A O   
3869 O O   . HOH   K .   ? 0.3978 0.4166 0.3652 0.1051  -0.0131 -0.1556 472 HOH   A O   
3870 O O   . HOH   K .   ? 0.1724 0.1845 0.1632 0.0079  0.0122  0.0011  473 HOH   A O   
3871 O O   . HOH   K .   ? 0.6621 0.4233 0.6380 0.2027  0.1501  -0.0819 474 HOH   A O   
3872 O O   . HOH   K .   ? 0.4627 0.2162 0.5044 0.0378  -0.1698 0.0830  475 HOH   A O   
3873 O O   . HOH   K .   ? 0.5268 0.7097 0.3548 -0.1781 -0.0673 0.2401  476 HOH   A O   
3874 O O   . HOH   K .   ? 0.1651 0.2429 0.2367 -0.0286 0.0043  -0.0270 477 HOH   A O   
3875 O O   . HOH   K .   ? 0.3508 0.3276 0.4487 0.0916  0.0668  -0.0207 478 HOH   A O   
3876 O O   . HOH   K .   ? 0.2392 0.2786 0.2029 0.0410  -0.0331 0.0264  479 HOH   A O   
3877 O O   . HOH   K .   ? 0.3859 0.4544 0.4916 -0.0010 -0.0194 -0.1900 480 HOH   A O   
3878 O O   . HOH   K .   ? 0.3861 0.3982 0.5547 0.0837  -0.1152 0.0673  481 HOH   A O   
3879 O O   . HOH   K .   ? 0.3644 0.3298 0.3449 -0.1235 -0.0405 0.1408  482 HOH   A O   
3880 O O   . HOH   K .   ? 0.3311 0.2476 0.1615 0.0716  0.0363  0.0425  483 HOH   A O   
3881 O O   . HOH   K .   ? 0.2982 0.2670 0.5976 -0.0035 0.1552  -0.0294 484 HOH   A O   
3882 O O   . HOH   K .   ? 0.3038 0.3021 0.2010 0.1533  -0.0268 0.0182  485 HOH   A O   
3883 O O   . HOH   K .   ? 0.2411 0.4755 0.2507 -0.0053 0.0161  -0.0489 486 HOH   A O   
3884 O O   . HOH   K .   ? 0.3435 0.2520 0.3046 -0.0099 0.0215  -0.0233 487 HOH   A O   
3885 O O   . HOH   K .   ? 0.4516 0.6530 0.7662 0.1352  -0.0938 0.0864  488 HOH   A O   
3886 O O   . HOH   K .   ? 0.3269 0.2461 0.2397 -0.0451 -0.0595 0.0534  489 HOH   A O   
3887 O O   . HOH   K .   ? 0.1706 0.3049 0.3079 -0.0029 -0.0102 -0.0228 490 HOH   A O   
3888 O O   . HOH   K .   ? 0.3185 0.1822 0.3518 -0.0439 -0.0679 -0.0004 491 HOH   A O   
3889 O O   . HOH   K .   ? 0.6042 0.3624 0.3310 -0.1317 -0.0163 -0.0461 492 HOH   A O   
3890 O O   . HOH   K .   ? 0.3839 0.6528 0.6227 0.2058  0.0383  0.2004  493 HOH   A O   
3891 O O   . HOH   K .   ? 0.5311 0.3822 0.4563 0.0910  -0.1126 0.0238  494 HOH   A O   
3892 O O   . HOH   K .   ? 0.3067 0.2087 0.2152 0.0713  -0.0333 0.0042  495 HOH   A O   
3893 O O   . HOH   K .   ? 0.2616 0.5054 0.2435 -0.0213 -0.0226 -0.0740 496 HOH   A O   
3894 O O   . HOH   K .   ? 0.4911 0.5415 0.2895 0.2414  -0.0807 -0.0381 497 HOH   A O   
3895 O O   . HOH   K .   ? 0.5233 0.3202 0.6027 -0.1895 0.0616  0.0565  498 HOH   A O   
3896 O O   . HOH   K .   ? 0.5353 0.4322 0.7006 -0.1009 0.1596  -0.1900 499 HOH   A O   
3897 O O   . HOH   K .   ? 0.2745 0.4572 0.4698 0.0244  0.0819  -0.1900 500 HOH   A O   
3898 O O   . HOH   K .   ? 0.2786 0.2892 0.4387 0.0751  0.0218  -0.1538 501 HOH   A O   
3899 O O   . HOH   K .   ? 0.2082 0.2236 0.2913 0.0504  0.0067  0.0628  502 HOH   A O   
3900 O O   . HOH   K .   ? 0.3730 0.2323 0.2952 0.0005  -0.0564 0.0228  503 HOH   A O   
3901 O O   . HOH   K .   ? 0.7004 0.3696 0.2426 -0.1868 0.0408  -0.0045 504 HOH   A O   
3902 O O   . HOH   K .   ? 0.4202 0.5442 0.2540 0.0386  0.0275  -0.0418 505 HOH   A O   
3903 O O   . HOH   K .   ? 0.5251 0.5108 0.8164 0.1555  0.0116  0.2248  506 HOH   A O   
3904 O O   . HOH   K .   ? 0.3553 0.2920 0.3100 0.1025  0.0184  -0.0861 507 HOH   A O   
3905 O O   . HOH   K .   ? 0.3065 0.4789 0.6238 0.1080  0.1770  -0.0188 508 HOH   A O   
3906 O O   . HOH   K .   ? 0.3158 0.2117 0.2352 0.0686  -0.0474 0.0850  509 HOH   A O   
3907 O O   . HOH   K .   ? 0.6907 0.2705 0.3450 0.0551  0.1289  0.0139  510 HOH   A O   
3908 O O   . HOH   K .   ? 0.2547 0.2261 0.2786 0.0566  0.1082  0.0719  511 HOH   A O   
3909 O O   . HOH   K .   ? 0.4716 0.1558 0.3244 -0.0118 0.0305  0.0794  512 HOH   A O   
3910 O O   . HOH   K .   ? 0.1850 0.2878 0.5681 0.0473  0.0260  -0.0136 513 HOH   A O   
3911 O O   . HOH   K .   ? 0.3594 0.2113 0.5272 -0.0582 0.1506  0.0578  514 HOH   A O   
3912 O O   . HOH   K .   ? 0.4368 0.1963 0.2824 0.0105  -0.0210 -0.0472 515 HOH   A O   
3913 O O   . HOH   K .   ? 0.6093 0.6271 0.5861 0.0788  0.1857  0.1255  516 HOH   A O   
3914 O O   . HOH   K .   ? 0.4159 0.6344 0.6214 0.1932  0.0606  0.0207  517 HOH   A O   
3915 O O   . HOH   K .   ? 0.4710 0.2874 0.3787 -0.0505 -0.0511 0.0690  518 HOH   A O   
3916 O O   . HOH   K .   ? 0.6289 0.3561 0.3347 0.0360  -0.0329 -0.0700 519 HOH   A O   
3917 O O   . HOH   K .   ? 0.2185 0.1687 0.2171 0.0055  -0.0262 0.0319  520 HOH   A O   
3918 O O   . HOH   K .   ? 0.4561 0.5159 0.6416 -0.1833 -0.0613 0.0351  521 HOH   A O   
3919 O O   . HOH   K .   ? 0.3157 0.3013 0.2699 0.0221  -0.0020 0.0164  522 HOH   A O   
3920 O O   . HOH   K .   ? 0.3083 0.2412 0.2246 0.0260  0.0055  -0.0591 523 HOH   A O   
3921 O O   . HOH   K .   ? 0.2424 0.3347 0.7342 -0.0608 0.0304  0.0225  524 HOH   A O   
3922 O O   . HOH   K .   ? 0.4300 0.4219 0.5793 0.1537  0.1857  0.0079  525 HOH   A O   
3923 O O   . HOH   K .   ? 0.3656 0.7567 0.5103 -0.1228 0.1201  -0.0678 526 HOH   A O   
3924 O O   . HOH   K .   ? 0.4169 0.3054 0.6922 -0.0927 0.2505  -0.0642 527 HOH   A O   
3925 O O   . HOH   K .   ? 0.5197 0.2198 0.2625 0.0167  -0.0052 0.0022  528 HOH   A O   
3926 O O   . HOH   K .   ? 0.7554 0.4598 0.3091 -0.1091 0.0647  0.1390  529 HOH   A O   
3927 O O   . HOH   K .   ? 0.6324 0.5536 0.5696 -0.0130 0.1605  -0.1562 530 HOH   A O   
3928 O O   . HOH   K .   ? 0.3514 0.4867 0.2539 0.1596  0.0014  -0.0220 531 HOH   A O   
3929 O O   . HOH   K .   ? 0.4725 0.3366 0.3095 -0.0811 -0.0511 -0.1092 532 HOH   A O   
3930 O O   . HOH   K .   ? 0.6223 0.7955 0.7458 -0.0316 -0.0559 0.0575  533 HOH   A O   
3931 O O   . HOH   K .   ? 0.7621 0.6277 0.6124 -0.0459 0.0784  -0.0362 534 HOH   A O   
3932 O O   . HOH   K .   ? 0.4351 0.5920 0.5353 0.0088  -0.0535 -0.0625 535 HOH   A O   
3933 O O   . HOH   K .   ? 0.2190 0.2480 0.2121 -0.0054 0.0194  -0.0591 536 HOH   A O   
3934 O O   . HOH   K .   ? 0.8364 0.5928 0.5763 -0.0607 -0.0751 0.0457  537 HOH   A O   
3935 O O   . HOH   K .   ? 0.3219 0.4184 0.3591 -0.0341 0.0220  -0.0223 538 HOH   A O   
3936 O O   . HOH   K .   ? 0.4542 0.5181 0.2856 -0.0400 0.0840  -0.0895 539 HOH   A O   
3937 O O   . HOH   K .   ? 0.3391 0.2406 0.2560 0.0139  0.0292  0.0123  540 HOH   A O   
3938 O O   . HOH   K .   ? 0.5272 0.4050 0.7248 -0.0808 -0.1309 0.1413  541 HOH   A O   
3939 O O   . HOH   K .   ? 0.6725 0.5331 0.5837 -0.0413 -0.0381 -0.0712 542 HOH   A O   
3940 O O   . HOH   K .   ? 0.3703 0.6544 0.6011 0.0852  0.1866  0.2613  543 HOH   A O   
3941 O O   . HOH   K .   ? 0.4116 0.4623 0.3227 0.1725  -0.0252 -0.0997 544 HOH   A O   
3942 O O   . HOH   K .   ? 0.4116 0.4342 0.8306 0.0818  -0.0511 0.2693  545 HOH   A O   
3943 O O   . HOH   K .   ? 0.2737 0.5101 0.4039 -0.0433 -0.0469 -0.0330 546 HOH   A O   
3944 O O   . HOH   K .   ? 0.2036 0.2446 0.2478 -0.0155 0.0072  -0.0045 547 HOH   A O   
3945 O O   . HOH   K .   ? 0.2436 0.2539 0.4583 -0.0175 0.0038  0.0474  548 HOH   A O   
3946 O O   . HOH   K .   ? 0.5158 0.3894 0.5989 -0.0329 0.0878  -0.0594 549 HOH   A O   
3947 O O   . HOH   K .   ? 0.5584 0.2721 0.4110 -0.0820 -0.1401 0.1253  550 HOH   A O   
3948 O O   . HOH   K .   ? 0.4840 0.7446 0.3290 0.2044  -0.1184 0.0069  551 HOH   A O   
3949 O O   . HOH   K .   ? 0.4573 0.4761 0.3613 0.0240  -0.0556 0.1363  552 HOH   A O   
3950 O O   . HOH   K .   ? 0.3981 0.3981 0.3247 -0.1761 -0.0140 -0.0120 553 HOH   A O   
3951 O O   . HOH   K .   ? 0.5463 0.6140 0.8180 0.1536  0.1131  -0.0711 554 HOH   A O   
3952 O O   . HOH   K .   ? 0.5137 0.5972 0.7447 0.1730  -0.0723 0.0808  555 HOH   A O   
3953 O O   . HOH   K .   ? 0.7621 0.5100 0.4870 -0.0293 0.1201  -0.0203 556 HOH   A O   
3954 O O   . HOH   K .   ? 0.5809 0.6136 0.4254 0.0525  0.0754  0.1207  557 HOH   A O   
3955 O O   . HOH   K .   ? 0.5662 0.5312 0.6608 0.1674  0.2258  0.1948  558 HOH   A O   
3956 O O   . HOH   K .   ? 0.4307 0.4324 0.7175 -0.0732 0.1110  -0.0501 559 HOH   A O   
3957 O O   . HOH   K .   ? 0.6444 0.5651 0.5344 0.0137  0.0394  0.0039  560 HOH   A O   
3958 O O   . HOH   K .   ? 0.4470 0.3622 0.7793 -0.1220 0.1156  -0.0512 561 HOH   A O   
3959 O O   . HOH   K .   ? 0.3854 0.2842 0.1799 -0.0472 0.0005  0.0063  562 HOH   A O   
3960 O O   . HOH   K .   ? 0.4120 0.6026 0.5908 0.0613  -0.0696 -0.0657 563 HOH   A O   
3961 O O   . HOH   K .   ? 0.3434 0.5750 0.5371 -0.1201 -0.0195 -0.0361 564 HOH   A O   
3962 O O   . HOH   K .   ? 0.6217 0.5770 0.6168 -0.0870 -0.0100 0.1740  565 HOH   A O   
3963 O O   . HOH   K .   ? 0.4903 0.2954 0.5195 -0.0984 -0.0225 -0.0683 566 HOH   A O   
3964 O O   . HOH   K .   ? 0.2474 0.3729 0.4872 0.0073  0.0084  0.1374  567 HOH   A O   
3965 O O   . HOH   K .   ? 0.4216 0.3975 0.4623 0.0058  0.0217  -0.0048 568 HOH   A O   
3966 O O   . HOH   K .   ? 0.5954 0.5964 0.3901 -0.0231 -0.1472 -0.0826 569 HOH   A O   
3967 O O   . HOH   K .   ? 0.5840 0.5556 0.7404 -0.0837 0.0466  0.0500  570 HOH   A O   
3968 O O   . HOH   K .   ? 0.3946 0.7212 0.4600 0.2289  0.0323  -0.0566 571 HOH   A O   
3969 O O   . HOH   K .   ? 0.6579 0.6450 0.8157 0.0553  -0.0282 -0.1062 572 HOH   A O   
3970 O O   . HOH   K .   ? 0.6163 0.3663 0.5186 -0.0157 -0.1592 -0.1900 573 HOH   A O   
3971 O O   . HOH   K .   ? 0.3466 0.2652 0.6331 -0.0245 -0.0334 -0.0655 574 HOH   A O   
3972 O O   . HOH   K .   ? 0.4232 0.6706 0.7214 0.2306  0.0571  0.0745  575 HOH   A O   
3973 O O   . HOH   K .   ? 0.7424 0.4147 0.5314 0.0335  0.0149  -0.1342 576 HOH   A O   
3974 O O   . HOH   K .   ? 0.5493 0.4100 0.3484 -0.1418 0.0986  -0.0288 577 HOH   A O   
3975 O O   . HOH   K .   ? 0.5215 0.5240 0.4838 -0.1046 -0.1015 0.1443  578 HOH   A O   
3976 O O   . HOH   K .   ? 0.5258 0.6736 0.5952 -0.0328 0.1896  -0.1330 579 HOH   A O   
3977 O O   . HOH   K .   ? 0.6809 0.3446 0.4119 0.1052  0.0439  -0.0901 580 HOH   A O   
3978 O O   . HOH   K .   ? 0.5259 0.2723 0.4185 0.0818  -0.0683 0.0679  581 HOH   A O   
3979 O O   . HOH   K .   ? 0.4639 0.5229 0.6085 -0.0139 -0.0492 0.0085  582 HOH   A O   
3980 O O   . HOH   K .   ? 0.4818 0.4104 0.4888 -0.0540 0.1861  0.0862  583 HOH   A O   
3981 O O   . HOH   K .   ? 0.6879 0.3704 0.5129 -0.0695 -0.0361 0.0264  584 HOH   A O   
3982 O O   . HOH   K .   ? 0.5354 0.5648 0.7517 -0.1497 -0.0759 -0.0832 585 HOH   A O   
3983 O O   . HOH   K .   ? 0.6300 0.4538 0.4446 0.1373  -0.0067 0.0383  586 HOH   A O   
3984 O O   . HOH   K .   ? 0.4946 0.5966 0.7965 0.2130  0.1522  0.1056  587 HOH   A O   
3985 O O   . HOH   K .   ? 0.5679 0.1967 0.3940 0.1119  -0.0342 -0.0002 588 HOH   A O   
3986 O O   . HOH   K .   ? 0.6197 0.4683 0.2697 0.1257  -0.0900 -0.1512 589 HOH   A O   
3987 O O   . HOH   K .   ? 0.3931 0.4339 0.3020 -0.0538 -0.0795 -0.0193 590 HOH   A O   
3988 O O   . HOH   K .   ? 0.5959 0.5393 0.5681 -0.1211 0.2265  -0.0645 591 HOH   A O   
3989 O O   . HOH   K .   ? 0.2605 0.3243 0.2935 0.0764  0.0634  0.0554  592 HOH   A O   
3990 O O   . HOH   K .   ? 0.7965 0.3974 0.4983 -0.1133 -0.0630 -0.0908 593 HOH   A O   
3991 O O   . HOH   K .   ? 0.3877 0.4536 0.3831 -0.0189 -0.0310 -0.1780 594 HOH   A O   
3992 O O   . HOH   K .   ? 0.4251 0.6105 0.4659 -0.1420 -0.0012 0.1056  595 HOH   A O   
3993 O O   . HOH   K .   ? 0.6752 0.4570 0.6276 -0.1456 -0.0111 -0.1644 596 HOH   A O   
3994 O O   . HOH   K .   ? 0.5141 0.4303 0.3809 0.0120  -0.0940 0.1836  597 HOH   A O   
3995 O O   . HOH   K .   ? 0.7258 0.4707 0.5422 0.0437  -0.0732 -0.1110 598 HOH   A O   
3996 O O   . HOH   K .   ? 0.5291 0.6075 0.5794 -0.0456 0.0692  -0.0211 599 HOH   A O   
3997 O O   . HOH   K .   ? 0.5648 0.3935 0.3869 -0.0266 -0.0363 -0.1900 600 HOH   A O   
3998 O O   . HOH   K .   ? 0.6838 0.3949 0.3681 0.1068  -0.0096 0.1845  601 HOH   A O   
3999 O O   . HOH   K .   ? 0.6141 0.5234 0.4240 -0.1416 0.1570  -0.0332 602 HOH   A O   
4000 O O   . HOH   K .   ? 0.5133 0.3622 0.3505 -0.1053 0.0497  -0.0014 603 HOH   A O   
4001 O O   . HOH   K .   ? 0.7461 0.4809 0.4891 0.1480  0.1212  -0.1728 604 HOH   A O   
4002 O O   . HOH   K .   ? 0.4614 0.3282 0.2969 0.1028  -0.0938 -0.0480 605 HOH   A O   
4003 O O   . HOH   K .   ? 0.5446 0.3360 0.3167 -0.0274 0.0737  -0.0166 606 HOH   A O   
4004 O O   . HOH   K .   ? 0.6189 0.4973 0.4331 0.0466  0.0668  0.2672  607 HOH   A O   
4005 O O   . HOH   K .   ? 0.4231 0.4467 0.4757 0.0325  0.0262  0.0702  608 HOH   A O   
4006 O O   . HOH   K .   ? 0.6171 0.4860 0.3670 0.1801  0.1374  0.0981  609 HOH   A O   
4007 O O   . HOH   K .   ? 0.5907 0.6237 0.6737 0.0359  0.1047  0.2524  610 HOH   A O   
4008 O O   . HOH   K .   ? 0.5384 0.6007 0.5857 -0.0380 0.1014  0.1016  611 HOH   A O   
4009 O O   . HOH   K .   ? 0.3973 0.4052 0.3577 -0.1165 0.0800  -0.1900 612 HOH   A O   
4010 O O   . HOH   K .   ? 0.6445 0.4990 0.2938 -0.0767 -0.0261 -0.0619 613 HOH   A O   
4011 O O   . HOH   K .   ? 0.4504 0.6095 0.4093 -0.0137 -0.0144 -0.1166 614 HOH   A O   
4012 O O   . HOH   K .   ? 0.5451 0.7895 0.4208 0.0485  0.0346  -0.0790 615 HOH   A O   
4013 O O   . HOH   K .   ? 0.5220 0.8140 0.6118 0.0553  0.0787  -0.0268 616 HOH   A O   
4014 O O   . HOH   K .   ? 0.5467 0.7094 0.5985 -0.0448 0.0976  0.0198  617 HOH   A O   
4015 O O   . HOH   K .   ? 0.7644 0.5207 0.5303 0.0108  0.0095  0.3136  618 HOH   A O   
4016 O O   . HOH   L .   ? 0.5504 0.3901 0.4583 -0.0974 -0.1767 0.1126  301 HOH   B O   
4017 O O   . HOH   L .   ? 0.6548 0.3896 0.5683 0.1275  -0.0680 0.0670  302 HOH   B O   
4018 O O   . HOH   L .   ? 0.2465 0.4794 0.5551 0.0299  -0.0663 -0.0942 303 HOH   B O   
4019 O O   . HOH   L .   ? 0.5056 0.4742 0.6659 0.0935  0.1185  0.1230  304 HOH   B O   
4020 O O   . HOH   L .   ? 0.6750 0.6370 0.5783 0.2289  -0.1143 -0.0191 305 HOH   B O   
4021 O O   . HOH   L .   ? 0.3504 0.3676 0.3525 0.1364  -0.0134 -0.0499 306 HOH   B O   
4022 O O   . HOH   L .   ? 0.7504 0.5382 0.7420 0.1413  0.2272  -0.1848 307 HOH   B O   
4023 O O   . HOH   L .   ? 0.6599 0.6343 0.8148 -0.0777 0.1754  -0.0423 308 HOH   B O   
4024 O O   . HOH   L .   ? 0.2309 0.3204 0.3478 0.0017  0.0389  -0.0908 309 HOH   B O   
4025 O O   . HOH   L .   ? 0.4165 0.7155 0.5261 0.0125  0.2759  -0.0070 310 HOH   B O   
4026 O O   . HOH   L .   ? 0.4085 0.3000 0.2658 0.0266  -0.0684 0.0650  311 HOH   B O   
4027 O O   . HOH   L .   ? 0.4999 0.2899 0.2561 0.1560  0.0233  0.0144  312 HOH   B O   
4028 O O   . HOH   L .   ? 0.6651 0.4513 0.4898 0.1072  -0.1900 -0.1385 313 HOH   B O   
4029 O O   . HOH   L .   ? 0.2920 0.4877 0.3304 -0.0447 -0.0891 0.0129  314 HOH   B O   
4030 O O   . HOH   L .   ? 0.3264 0.4835 0.1549 -0.1741 -0.0137 0.0339  315 HOH   B O   
4031 O O   . HOH   L .   ? 0.3823 0.3785 0.5718 0.0563  0.0171  -0.0893 316 HOH   B O   
4032 O O   . HOH   L .   ? 0.3435 0.3457 0.2646 -0.1508 -0.1107 0.1325  317 HOH   B O   
4033 O O   . HOH   L .   ? 0.3203 0.3678 0.4028 -0.0773 0.0843  -0.1900 318 HOH   B O   
4034 O O   . HOH   L .   ? 0.4903 0.4491 0.5914 0.2402  -0.1465 0.0233  319 HOH   B O   
4035 O O   . HOH   L .   ? 0.1701 0.2128 0.1396 -0.0096 -0.0172 -0.0598 320 HOH   B O   
4036 O O   . HOH   L .   ? 0.6540 0.5362 0.4705 0.1196  0.1866  0.0626  321 HOH   B O   
4037 O O   . HOH   L .   ? 0.3692 0.4443 0.4699 0.0085  0.0301  0.0914  322 HOH   B O   
4038 O O   . HOH   L .   ? 0.4105 0.4081 0.6731 0.0125  -0.1324 -0.0198 323 HOH   B O   
4039 O O   . HOH   L .   ? 0.6058 0.3543 0.3001 0.1660  0.1965  0.0457  324 HOH   B O   
4040 O O   . HOH   L .   ? 0.6074 0.5994 0.3743 0.2643  0.0390  0.0065  325 HOH   B O   
4041 O O   . HOH   L .   ? 0.2144 0.4047 0.1906 0.0125  0.0103  -0.0194 326 HOH   B O   
4042 O O   . HOH   L .   ? 0.2483 0.2104 0.2214 -0.0250 0.0385  -0.0306 327 HOH   B O   
4043 O O   . HOH   L .   ? 0.1719 0.3402 0.1823 -0.0625 0.0531  -0.0604 328 HOH   B O   
4044 O O   . HOH   L .   ? 0.3498 0.6281 0.2037 0.0630  -0.0279 0.0290  329 HOH   B O   
4045 O O   . HOH   L .   ? 0.3306 0.4908 0.3443 -0.0845 0.1025  -0.0027 330 HOH   B O   
4046 O O   . HOH   L .   ? 0.3124 0.4412 0.3921 0.1198  -0.0828 -0.0742 331 HOH   B O   
4047 O O   . HOH   L .   ? 0.1411 0.1505 0.1800 0.0197  -0.0053 -0.0146 332 HOH   B O   
4048 O O   . HOH   L .   ? 0.2198 0.2012 0.1885 0.0278  0.0138  -0.0349 333 HOH   B O   
4049 O O   . HOH   L .   ? 0.1894 0.1672 0.1954 0.0449  -0.0029 -0.0331 334 HOH   B O   
4050 O O   . HOH   L .   ? 0.2753 0.5202 0.2492 -0.0925 -0.0161 0.0388  335 HOH   B O   
4051 O O   . HOH   L .   ? 0.2882 0.6265 0.4792 0.1360  0.1441  -0.0262 336 HOH   B O   
4052 O O   . HOH   L .   ? 0.3204 0.2738 0.5954 -0.0931 0.2159  -0.1409 337 HOH   B O   
4053 O O   . HOH   L .   ? 0.2721 0.2582 0.1572 0.0318  -0.0043 -0.0165 338 HOH   B O   
4054 O O   . HOH   L .   ? 0.2174 0.2156 0.2633 -0.0315 0.0191  -0.0225 339 HOH   B O   
4055 O O   . HOH   L .   ? 0.1427 0.3423 0.2947 -0.0195 0.0258  -0.0597 340 HOH   B O   
4056 O O   . HOH   L .   ? 0.3074 0.2904 0.2141 -0.0769 0.0183  -0.0085 341 HOH   B O   
4057 O O   . HOH   L .   ? 0.3902 0.7213 0.4009 0.2196  -0.0305 -0.0889 342 HOH   B O   
4058 O O   . HOH   L .   ? 0.2590 0.2316 0.3513 0.0031  0.0450  -0.0647 343 HOH   B O   
4059 O O   . HOH   L .   ? 0.5409 0.3487 0.2677 0.0855  -0.0216 -0.0549 344 HOH   B O   
4060 O O   . HOH   L .   ? 0.7035 0.4353 0.5331 -0.0721 -0.0565 0.0351  345 HOH   B O   
4061 O O   . HOH   L .   ? 0.2674 0.4606 0.4771 0.0837  0.1600  0.1378  346 HOH   B O   
4062 O O   . HOH   L .   ? 0.5503 0.4774 0.6716 -0.0267 0.1380  -0.1062 347 HOH   B O   
4063 O O   . HOH   L .   ? 0.4883 0.3260 0.4015 0.0157  0.1811  -0.0813 348 HOH   B O   
4064 O O   . HOH   L .   ? 0.4769 0.3289 0.4265 -0.1031 -0.1177 0.0585  349 HOH   B O   
4065 O O   . HOH   L .   ? 0.2478 0.6183 0.2996 0.0225  0.0085  -0.1855 350 HOH   B O   
4066 O O   . HOH   L .   ? 0.1695 0.3780 0.2634 -0.0686 0.0013  -0.0070 351 HOH   B O   
4067 O O   . HOH   L .   ? 0.2267 0.3854 0.2427 -0.0315 -0.0337 -0.0144 352 HOH   B O   
4068 O O   . HOH   L .   ? 0.3065 0.4331 0.3268 0.0767  0.0764  0.0093  353 HOH   B O   
4069 O O   . HOH   L .   ? 0.1460 0.2265 0.1614 -0.0007 -0.0094 -0.0458 354 HOH   B O   
4070 O O   . HOH   L .   ? 0.3825 0.2852 0.4641 -0.0323 0.1567  -0.1208 355 HOH   B O   
4071 O O   . HOH   L .   ? 0.1729 0.1978 0.1810 0.0103  -0.0096 -0.0081 356 HOH   B O   
4072 O O   . HOH   L .   ? 0.7998 0.6475 0.5444 -0.0347 0.1778  0.1468  357 HOH   B O   
4073 O O   . HOH   L .   ? 0.2377 0.4742 0.5710 0.1396  -0.0247 0.0072  358 HOH   B O   
4074 O O   . HOH   L .   ? 0.1407 0.2943 0.1947 -0.0110 -0.0082 -0.0118 359 HOH   B O   
4075 O O   . HOH   L .   ? 0.3237 0.4688 0.3591 0.0908  0.0403  -0.0372 360 HOH   B O   
4076 O O   . HOH   L .   ? 0.7395 0.4904 0.4029 -0.0355 0.1919  0.0121  361 HOH   B O   
4077 O O   . HOH   L .   ? 0.2612 0.4051 0.1910 -0.0526 0.0372  -0.0210 362 HOH   B O   
4078 O O   . HOH   L .   ? 0.2094 0.5064 0.5127 -0.0368 -0.0050 0.0870  363 HOH   B O   
4079 O O   . HOH   L .   ? 0.4263 0.5116 0.2933 0.1061  0.1317  0.0023  364 HOH   B O   
4080 O O   . HOH   L .   ? 0.2314 0.2464 0.3449 -0.0114 -0.0150 -0.0093 365 HOH   B O   
4081 O O   . HOH   L .   ? 0.2100 0.2461 0.3427 0.0359  0.0451  -0.0605 366 HOH   B O   
4082 O O   . HOH   L .   ? 0.2365 0.3659 0.2570 -0.0481 0.0073  -0.0111 367 HOH   B O   
4083 O O   . HOH   L .   ? 0.4448 0.4719 0.5912 -0.1900 0.0155  0.0108  368 HOH   B O   
4084 O O   . HOH   L .   ? 0.6016 0.5616 0.4887 -0.0633 -0.0760 0.0489  369 HOH   B O   
4085 O O   . HOH   L .   ? 0.1245 0.2233 0.2096 -0.0154 -0.0030 -0.0052 370 HOH   B O   
4086 O O   . HOH   L .   ? 0.2441 0.2554 0.1987 -0.0646 -0.0195 0.0698  371 HOH   B O   
4087 O O   . HOH   L .   ? 0.4060 0.3211 0.6235 -0.0073 -0.0001 0.2381  372 HOH   B O   
4088 O O   . HOH   L .   ? 0.3745 0.3447 0.5519 -0.0203 -0.0287 -0.0982 373 HOH   B O   
4089 O O   . HOH   L .   ? 0.6528 0.4007 0.4000 0.1025  0.0961  -0.1740 374 HOH   B O   
4090 O O   . HOH   L .   ? 0.3168 0.3422 0.2953 0.0286  0.0548  -0.0603 375 HOH   B O   
4091 O O   . HOH   L .   ? 0.3893 0.4110 0.4105 0.0426  -0.1900 -0.0045 376 HOH   B O   
4092 O O   . HOH   L .   ? 0.1890 0.2706 0.5121 0.0556  -0.0078 -0.1081 377 HOH   B O   
4093 O O   . HOH   L .   ? 0.3875 0.6628 0.6955 0.1681  0.1846  -0.0802 378 HOH   B O   
4094 O O   . HOH   L .   ? 0.6862 0.5586 0.3194 0.2741  -0.1388 -0.0350 379 HOH   B O   
4095 O O   . HOH   L .   ? 0.2066 0.2909 0.3705 -0.0114 0.1114  -0.0828 380 HOH   B O   
4096 O O   . HOH   L .   ? 0.2556 0.4885 0.3083 0.1001  -0.0243 -0.1900 381 HOH   B O   
4097 O O   . HOH   L .   ? 0.3047 0.3602 0.3529 0.0585  0.0598  0.0887  382 HOH   B O   
4098 O O   . HOH   L .   ? 0.3587 0.6199 0.4729 0.0816  -0.0197 0.1174  383 HOH   B O   
4099 O O   . HOH   L .   ? 0.3776 0.3971 0.2615 0.1206  -0.0711 -0.1464 384 HOH   B O   
4100 O O   . HOH   L .   ? 0.2182 0.3906 0.2799 0.0426  0.0110  -0.0575 385 HOH   B O   
4101 O O   . HOH   L .   ? 0.2991 0.5608 0.3146 -0.1704 0.1189  -0.1172 386 HOH   B O   
4102 O O   . HOH   L .   ? 0.2059 0.2724 0.2345 0.0024  0.0370  -0.0489 387 HOH   B O   
4103 O O   . HOH   L .   ? 0.4232 0.3317 0.2412 -0.0506 0.0419  -0.0873 388 HOH   B O   
4104 O O   . HOH   L .   ? 0.3831 0.5078 0.3701 0.1913  -0.0854 0.0095  389 HOH   B O   
4105 O O   . HOH   L .   ? 0.2735 0.4314 0.2229 -0.0466 0.0110  -0.0370 390 HOH   B O   
4106 O O   . HOH   L .   ? 0.1942 0.2601 0.1709 -0.0344 0.0011  -0.0172 391 HOH   B O   
4107 O O   . HOH   L .   ? 0.2911 0.1954 0.2305 0.1007  0.0422  0.0431  392 HOH   B O   
4108 O O   . HOH   L .   ? 0.3925 0.6286 0.2301 -0.1800 -0.0141 0.1187  393 HOH   B O   
4109 O O   . HOH   L .   ? 0.2891 0.3795 0.6391 -0.0123 0.0615  0.1783  394 HOH   B O   
4110 O O   . HOH   L .   ? 0.5199 0.4757 0.4716 0.1384  -0.0565 0.0006  395 HOH   B O   
4111 O O   . HOH   L .   ? 0.5389 0.5042 0.2413 0.1653  0.0612  -0.0150 396 HOH   B O   
4112 O O   . HOH   L .   ? 0.4922 0.6366 0.6564 0.0543  0.2646  -0.1178 397 HOH   B O   
4113 O O   . HOH   L .   ? 0.7802 0.5386 0.5214 -0.0308 0.0538  0.2204  398 HOH   B O   
4114 O O   . HOH   L .   ? 0.2113 0.4647 0.2974 -0.0508 -0.0397 -0.1045 399 HOH   B O   
4115 O O   . HOH   L .   ? 0.3705 0.6325 0.3145 0.2242  0.0094  0.0825  400 HOH   B O   
4116 O O   . HOH   L .   ? 0.5649 0.6763 0.3810 -0.1103 -0.1755 0.0340  401 HOH   B O   
4117 O O   . HOH   L .   ? 0.7280 0.5865 0.5500 -0.0388 -0.0899 0.0237  402 HOH   B O   
4118 O O   . HOH   L .   ? 0.3095 0.3579 0.4534 -0.1343 -0.0341 0.1397  403 HOH   B O   
4119 O O   . HOH   L .   ? 0.4193 0.3915 0.3558 0.0175  -0.0329 -0.1469 404 HOH   B O   
4120 O O   . HOH   L .   ? 0.3218 0.2461 0.2369 0.0225  -0.0484 -0.0773 405 HOH   B O   
4121 O O   . HOH   L .   ? 0.5217 0.3509 0.2893 0.1575  -0.0574 0.0461  406 HOH   B O   
4122 O O   . HOH   L .   ? 0.2295 0.3417 0.5611 -0.0456 -0.1387 0.0859  407 HOH   B O   
4123 O O   . HOH   L .   ? 0.2739 0.3501 0.4881 0.0374  0.0348  -0.1420 408 HOH   B O   
4124 O O   . HOH   L .   ? 0.2595 0.3470 0.2527 0.0575  0.0408  -0.0354 409 HOH   B O   
4125 O O   . HOH   L .   ? 0.2615 0.2308 0.4030 0.0147  0.1138  -0.0422 410 HOH   B O   
4126 O O   . HOH   L .   ? 0.4388 0.2893 0.2373 -0.0460 0.0162  -0.0365 411 HOH   B O   
4127 O O   . HOH   L .   ? 0.3016 0.3089 0.2777 -0.0195 0.0115  -0.0612 412 HOH   B O   
4128 O O   . HOH   L .   ? 0.3425 0.4379 0.4366 -0.0970 0.2042  -0.1445 413 HOH   B O   
4129 O O   . HOH   L .   ? 0.3874 0.6935 0.3697 -0.0823 0.0422  -0.0039 414 HOH   B O   
4130 O O   . HOH   L .   ? 0.5413 0.6160 0.6095 -0.1039 0.1024  -0.0969 415 HOH   B O   
4131 O O   . HOH   L .   ? 0.5311 0.5122 0.2450 0.0820  0.0049  -0.0221 416 HOH   B O   
4132 O O   . HOH   L .   ? 0.3791 0.2625 0.2173 -0.0475 0.0550  -0.0260 417 HOH   B O   
4133 O O   . HOH   L .   ? 0.5717 0.6672 0.6975 -0.0619 -0.0487 -0.0399 418 HOH   B O   
4134 O O   . HOH   L .   ? 0.4970 0.3410 0.3655 0.0031  -0.1118 -0.0214 419 HOH   B O   
4135 O O   . HOH   L .   ? 0.4545 0.6204 0.6647 0.1629  -0.0450 -0.0168 420 HOH   B O   
4136 O O   . HOH   L .   ? 0.4655 0.3782 0.4338 -0.1610 0.0157  0.0530  421 HOH   B O   
4137 O O   . HOH   L .   ? 0.3112 0.3051 0.4055 0.0541  -0.1180 0.0352  422 HOH   B O   
4138 O O   . HOH   L .   ? 0.4721 0.4951 0.4330 -0.1209 0.1943  -0.1870 423 HOH   B O   
4139 O O   . HOH   L .   ? 0.4730 0.6542 0.4576 0.2185  -0.1013 -0.0683 424 HOH   B O   
4140 O O   . HOH   L .   ? 0.2779 0.4621 0.3881 0.0373  0.0048  0.0634  425 HOH   B O   
4141 O O   . HOH   L .   ? 0.5746 0.5022 0.7388 0.0874  0.0671  0.0014  426 HOH   B O   
4142 O O   . HOH   L .   ? 0.2555 0.4626 0.4230 -0.0200 0.1130  -0.0284 427 HOH   B O   
4143 O O   . HOH   L .   ? 0.4473 0.6822 0.3696 0.0751  -0.0285 0.1575  428 HOH   B O   
4144 O O   . HOH   L .   ? 0.3031 0.2727 0.2144 -0.0363 -0.0156 -0.0582 429 HOH   B O   
4145 O O   . HOH   L .   ? 0.4086 0.6726 0.4359 -0.1037 0.0447  -0.0812 430 HOH   B O   
4146 O O   . HOH   L .   ? 0.4697 0.5374 0.5000 -0.0478 0.1227  -0.1146 431 HOH   B O   
4147 O O   . HOH   L .   ? 0.3903 0.5214 0.4158 0.0138  -0.1129 -0.0894 432 HOH   B O   
4148 O O   . HOH   L .   ? 0.3782 0.6643 0.2259 0.2391  -0.0475 -0.0657 433 HOH   B O   
4149 O O   . HOH   L .   ? 0.5678 0.6163 0.6231 0.0525  -0.0974 0.0696  434 HOH   B O   
4150 O O   . HOH   L .   ? 0.2758 0.3986 0.4052 -0.0618 0.0423  -0.1716 435 HOH   B O   
4151 O O   . HOH   L .   ? 0.6521 0.5067 0.4872 0.2251  -0.0314 -0.0997 436 HOH   B O   
4152 O O   . HOH   L .   ? 0.7948 0.7284 0.7566 0.0491  -0.0771 0.1213  437 HOH   B O   
4153 O O   . HOH   L .   ? 0.5117 0.3804 0.5601 -0.0894 0.2494  0.0815  438 HOH   B O   
4154 O O   . HOH   L .   ? 0.3479 0.6098 0.5160 0.0242  0.0489  -0.0651 439 HOH   B O   
4155 O O   . HOH   L .   ? 0.7573 0.5162 0.4105 -0.1201 0.0308  -0.0040 440 HOH   B O   
4156 O O   . HOH   L .   ? 0.8016 0.7890 0.9609 -0.0600 -0.0719 -0.0353 441 HOH   B O   
4157 O O   . HOH   L .   ? 0.5329 0.7050 0.5109 -0.0523 -0.0570 -0.0800 442 HOH   B O   
4158 O O   . HOH   L .   ? 0.6257 0.4327 0.3687 0.2673  -0.0111 -0.0949 443 HOH   B O   
4159 O O   . HOH   L .   ? 0.6205 0.2858 0.3846 -0.0664 0.1441  -0.0718 444 HOH   B O   
4160 O O   . HOH   L .   ? 0.6859 0.7117 0.4946 0.1560  -0.0236 -0.0181 445 HOH   B O   
4161 O O   . HOH   L .   ? 0.7032 0.5336 0.4282 -0.0520 0.1377  0.0645  446 HOH   B O   
4162 O O   . HOH   L .   ? 0.6868 0.5890 0.6275 0.0080  0.1903  -0.1742 447 HOH   B O   
4163 O O   . HOH   L .   ? 0.3061 0.4532 0.5288 0.0629  -0.0222 0.0167  448 HOH   B O   
4164 O O   . HOH   L .   ? 0.2430 0.5497 0.4619 0.0905  0.1332  0.1279  449 HOH   B O   
4165 O O   . HOH   L .   ? 0.3885 0.3523 0.3665 -0.0273 0.0824  -0.1356 450 HOH   B O   
4166 O O   . HOH   L .   ? 0.4591 0.7174 0.5980 0.0561  -0.0444 -0.0020 451 HOH   B O   
4167 O O   . HOH   L .   ? 0.3683 0.6425 0.5258 -0.0031 0.0375  -0.0755 452 HOH   B O   
4168 O O   . HOH   L .   ? 0.6676 0.4716 0.4342 -0.0384 0.1645  -0.0639 453 HOH   B O   
4169 O O   . HOH   L .   ? 0.3863 0.3685 0.5142 -0.1476 -0.0822 -0.0600 454 HOH   B O   
4170 O O   . HOH   L .   ? 0.4776 0.5806 0.4855 -0.0150 0.0631  0.0147  455 HOH   B O   
4171 O O   . HOH   M .   ? 0.5703 0.5864 0.6075 0.1302  -0.0596 0.1972  401 HOH   C O   
4172 O O   . HOH   M .   ? 0.3784 0.6448 0.5261 -0.1184 0.2320  -0.0642 402 HOH   C O   
4173 O O   . HOH   M .   ? 0.2831 0.3707 0.2732 -0.1058 -0.0456 0.0200  403 HOH   C O   
4174 O O   . HOH   M .   ? 0.6021 0.5871 0.8334 0.0598  -0.0322 0.1157  404 HOH   C O   
4175 O O   . HOH   M .   ? 0.4318 0.4082 0.4409 -0.1084 0.0605  -0.1167 405 HOH   C O   
4176 O O   . HOH   M .   ? 0.6445 0.3651 0.5029 -0.0877 0.0994  -0.0363 406 HOH   C O   
4177 O O   . HOH   M .   ? 0.2707 0.5271 0.2457 0.0622  0.0415  0.1393  407 HOH   C O   
4178 O O   . HOH   M .   ? 0.5110 0.6637 0.4100 -0.0615 0.1658  -0.1262 408 HOH   C O   
4179 O O   . HOH   M .   ? 0.5387 0.4912 0.3194 -0.0819 0.0457  0.1869  409 HOH   C O   
4180 O O   . HOH   M .   ? 0.5069 0.4846 0.3368 -0.1051 0.1109  -0.0682 410 HOH   C O   
4181 O O   . HOH   M .   ? 0.6722 0.5218 0.6972 0.0988  -0.0833 0.2053  411 HOH   C O   
4182 O O   . HOH   M .   ? 0.6833 0.3935 0.3093 0.1775  0.0387  0.0346  412 HOH   C O   
4183 O O   . HOH   M .   ? 0.2561 0.2891 0.1904 -0.0798 0.0227  -0.0015 413 HOH   C O   
4184 O O   . HOH   M .   ? 0.2713 0.2501 0.2943 0.0468  -0.0614 0.0278  414 HOH   C O   
4185 O O   . HOH   M .   ? 0.3704 0.3647 0.6444 0.0257  -0.1349 -0.0899 415 HOH   C O   
4186 O O   . HOH   M .   ? 0.1822 0.1262 0.1514 -0.0062 0.0113  -0.0240 416 HOH   C O   
4187 O O   . HOH   M .   ? 0.2379 0.2529 0.4158 -0.0515 0.0584  0.0508  417 HOH   C O   
4188 O O   . HOH   M .   ? 0.5435 0.2334 0.2295 0.0256  0.0728  0.0631  418 HOH   C O   
4189 O O   . HOH   M .   ? 0.3829 0.2608 0.4203 0.0255  0.0691  -0.0281 419 HOH   C O   
4190 O O   . HOH   M .   ? 0.2514 0.3841 0.5061 -0.0829 0.0672  -0.1340 420 HOH   C O   
4191 O O   . HOH   M .   ? 0.2084 0.2493 0.3274 0.0134  -0.0632 -0.0056 421 HOH   C O   
4192 O O   . HOH   M .   ? 0.2952 0.4354 0.4488 -0.1550 0.0046  -0.0144 422 HOH   C O   
4193 O O   . HOH   M .   ? 0.2351 0.2818 0.1972 -0.0482 -0.0246 -0.0023 423 HOH   C O   
4194 O O   . HOH   M .   ? 0.5257 0.3044 0.5937 0.0968  0.1019  0.1817  424 HOH   C O   
4195 O O   . HOH   M .   ? 0.4061 0.2557 0.4655 0.0260  -0.0659 -0.0261 425 HOH   C O   
4196 O O   . HOH   M .   ? 0.5778 0.4732 0.5904 -0.1095 -0.0450 0.1437  426 HOH   C O   
4197 O O   . HOH   M .   ? 0.2358 0.5890 0.4727 -0.0900 -0.0190 -0.1242 427 HOH   C O   
4198 O O   . HOH   M .   ? 0.5393 0.6721 0.4745 0.0778  -0.0027 0.0749  428 HOH   C O   
4199 O O   . HOH   M .   ? 0.3451 0.2889 0.3352 -0.1082 0.0647  -0.1441 429 HOH   C O   
4200 O O   . HOH   M .   ? 0.3620 0.4148 0.5168 0.0642  0.0489  -0.1117 430 HOH   C O   
4201 O O   . HOH   M .   ? 0.4392 0.3117 0.2467 0.0110  -0.0130 0.0087  431 HOH   C O   
4202 O O   . HOH   M .   ? 0.3404 0.2739 0.2748 -0.0428 -0.0551 0.0975  432 HOH   C O   
4203 O O   . HOH   M .   ? 0.5096 0.4417 0.5193 -0.1086 -0.1900 -0.1099 433 HOH   C O   
4204 O O   . HOH   M .   ? 0.5382 0.2049 0.2455 -0.1033 0.0615  -0.0317 434 HOH   C O   
4205 O O   . HOH   M .   ? 0.3660 0.2729 0.3163 0.0176  -0.0655 0.0609  435 HOH   C O   
4206 O O   . HOH   M .   ? 0.3606 0.1697 0.3654 -0.0923 0.0252  0.0191  436 HOH   C O   
4207 O O   . HOH   M .   ? 0.2057 0.2103 0.4261 -0.0518 0.0983  -0.1468 437 HOH   C O   
4208 O O   . HOH   M .   ? 0.5030 0.7247 0.5378 0.1919  -0.0459 -0.0814 438 HOH   C O   
4209 O O   . HOH   M .   ? 0.1508 0.1302 0.1267 -0.0024 0.0003  -0.0056 439 HOH   C O   
4210 O O   . HOH   M .   ? 0.2569 0.4997 0.3136 0.0598  0.0051  0.1097  440 HOH   C O   
4211 O O   . HOH   M .   ? 0.4738 0.5578 0.5948 0.0020  -0.0814 0.1665  441 HOH   C O   
4212 O O   . HOH   M .   ? 0.3343 0.4707 0.6697 -0.1900 -0.0221 0.0732  442 HOH   C O   
4213 O O   . HOH   M .   ? 0.2186 0.2384 0.2165 -0.0390 -0.0293 -0.0085 443 HOH   C O   
4214 O O   . HOH   M .   ? 0.2005 0.2769 0.1690 0.0105  -0.0213 -0.0074 444 HOH   C O   
4215 O O   . HOH   M .   ? 0.3058 0.3160 0.2856 0.0159  0.0682  0.1172  445 HOH   C O   
4216 O O   . HOH   M .   ? 0.2075 0.2335 0.2399 -0.0528 0.0351  -0.0066 446 HOH   C O   
4217 O O   . HOH   M .   ? 0.4694 0.2888 0.3564 -0.0160 0.0851  -0.1415 447 HOH   C O   
4218 O O   . HOH   M .   ? 0.3034 0.2000 0.2284 -0.0163 -0.0734 0.0101  448 HOH   C O   
4219 O O   . HOH   M .   ? 0.2272 0.4382 0.1855 -0.0749 0.0000  -0.0271 449 HOH   C O   
4220 O O   . HOH   M .   ? 0.3785 0.4931 0.5944 0.1180  0.0262  0.0951  450 HOH   C O   
4221 O O   . HOH   M .   ? 0.1293 0.2584 0.1657 -0.0016 -0.0047 -0.0023 451 HOH   C O   
4222 O O   . HOH   M .   ? 0.3309 0.1824 0.2208 -0.0098 0.0066  0.0050  452 HOH   C O   
4223 O O   . HOH   M .   ? 0.4145 0.6247 0.3026 -0.0293 0.0722  -0.0580 453 HOH   C O   
4224 O O   . HOH   M .   ? 0.2446 0.3999 0.3470 0.0911  0.0359  0.1033  454 HOH   C O   
4225 O O   . HOH   M .   ? 0.2984 0.4101 0.4531 -0.0136 -0.1743 -0.0563 455 HOH   C O   
4226 O O   . HOH   M .   ? 0.1759 0.1647 0.1493 0.0077  -0.0003 -0.0029 456 HOH   C O   
4227 O O   . HOH   M .   ? 0.3598 0.5083 0.4892 0.1065  -0.0586 -0.0069 457 HOH   C O   
4228 O O   . HOH   M .   ? 0.5111 0.4002 0.4611 0.1464  -0.1069 -0.0660 458 HOH   C O   
4229 O O   . HOH   M .   ? 0.8101 0.6698 0.7290 -0.1717 0.1875  0.1753  459 HOH   C O   
4230 O O   . HOH   M .   ? 0.4603 0.2760 0.2996 0.1041  0.0221  -0.0154 460 HOH   C O   
4231 O O   . HOH   M .   ? 0.2504 0.2386 0.2659 0.0058  0.0603  -0.0044 461 HOH   C O   
4232 O O   . HOH   M .   ? 0.5524 0.2537 0.3287 0.0351  0.1131  0.0626  462 HOH   C O   
4233 O O   . HOH   M .   ? 0.5994 0.5176 0.2963 0.2295  0.0453  -0.0582 463 HOH   C O   
4234 O O   . HOH   M .   ? 0.2538 0.3815 0.4671 -0.0001 -0.0884 -0.0041 464 HOH   C O   
4235 O O   . HOH   M .   ? 0.3736 0.3528 0.1903 0.0285  -0.0580 -0.0261 465 HOH   C O   
4236 O O   . HOH   M .   ? 0.3757 0.5457 0.4681 0.0112  0.0134  -0.0115 466 HOH   C O   
4237 O O   . HOH   M .   ? 0.2695 0.6240 0.5244 0.0860  0.0357  0.0200  467 HOH   C O   
4238 O O   . HOH   M .   ? 0.3494 0.5000 0.6082 -0.1403 0.1374  -0.0914 468 HOH   C O   
4239 O O   . HOH   M .   ? 0.1832 0.1602 0.1553 -0.0124 0.0028  -0.0152 469 HOH   C O   
4240 O O   . HOH   M .   ? 0.2688 0.1824 0.2578 -0.0467 0.0518  -0.0442 470 HOH   C O   
4241 O O   . HOH   M .   ? 0.4231 0.3198 0.4264 -0.0230 -0.1900 0.0546  471 HOH   C O   
4242 O O   . HOH   M .   ? 0.1495 0.2771 0.1757 -0.0162 0.0088  -0.0118 472 HOH   C O   
4243 O O   . HOH   M .   ? 0.1688 0.1579 0.1766 0.0396  -0.0077 -0.0093 473 HOH   C O   
4244 O O   . HOH   M .   ? 0.3322 0.6219 0.4973 0.0889  0.0629  -0.1383 474 HOH   C O   
4245 O O   . HOH   M .   ? 0.3658 0.5124 0.2706 0.0993  0.0906  0.1179  475 HOH   C O   
4246 O O   . HOH   M .   ? 0.3286 0.6629 0.4989 0.1336  -0.0724 -0.0268 476 HOH   C O   
4247 O O   . HOH   M .   ? 0.6124 0.4998 0.4953 0.0910  0.2449  0.1969  477 HOH   C O   
4248 O O   . HOH   M .   ? 0.2806 0.4600 0.3589 -0.0405 -0.0917 0.0921  478 HOH   C O   
4249 O O   . HOH   M .   ? 0.3538 0.4929 0.3454 -0.0763 0.0381  0.2124  479 HOH   C O   
4250 O O   . HOH   M .   ? 0.1852 0.1916 0.2318 0.0203  0.0477  -0.0252 480 HOH   C O   
4251 O O   . HOH   M .   ? 0.2210 0.4079 0.3497 -0.0382 -0.0167 -0.0887 481 HOH   C O   
4252 O O   . HOH   M .   ? 0.2406 0.3534 0.1771 -0.0309 0.0413  0.0117  482 HOH   C O   
4253 O O   . HOH   M .   ? 0.5371 0.7464 0.4059 0.0132  0.2531  0.0866  483 HOH   C O   
4254 O O   . HOH   M .   ? 0.2102 0.3453 0.2111 0.0650  0.0110  0.0151  484 HOH   C O   
4255 O O   . HOH   M .   ? 0.2621 0.2209 0.2531 0.0211  0.0480  -0.0221 485 HOH   C O   
4256 O O   . HOH   M .   ? 0.4145 0.3670 0.3523 -0.0592 -0.0273 0.1051  486 HOH   C O   
4257 O O   . HOH   M .   ? 0.5797 0.6544 0.6869 0.0890  -0.0856 0.2087  487 HOH   C O   
4258 O O   . HOH   M .   ? 0.4286 0.2540 0.4061 -0.0602 0.0393  -0.1160 488 HOH   C O   
4259 O O   . HOH   M .   ? 0.2450 0.2432 0.2473 -0.0286 0.0164  -0.0386 489 HOH   C O   
4260 O O   . HOH   M .   ? 0.3946 0.5085 0.5612 -0.1900 -0.0208 -0.1295 490 HOH   C O   
4261 O O   . HOH   M .   ? 0.3593 0.2605 0.1916 -0.0661 0.0000  -0.0409 491 HOH   C O   
4262 O O   . HOH   M .   ? 0.3137 0.6649 0.5228 0.1125  -0.1638 0.0744  492 HOH   C O   
4263 O O   . HOH   M .   ? 0.3616 0.3387 0.2944 -0.0281 -0.0778 0.0197  493 HOH   C O   
4264 O O   . HOH   M .   ? 0.3810 0.2471 0.6230 -0.0560 -0.0141 0.0170  494 HOH   C O   
4265 O O   . HOH   M .   ? 0.3653 0.2057 0.3563 -0.0791 0.0472  -0.0038 495 HOH   C O   
4266 O O   . HOH   M .   ? 0.2029 0.2123 0.1904 0.0510  -0.0092 -0.0266 496 HOH   C O   
4267 O O   . HOH   M .   ? 0.6788 0.4643 0.5917 -0.0918 -0.0814 -0.0178 497 HOH   C O   
4268 O O   . HOH   M .   ? 0.2318 0.3724 0.3795 -0.0013 -0.0429 -0.1277 498 HOH   C O   
4269 O O   . HOH   M .   ? 0.4709 0.4642 0.5232 0.1654  0.1721  0.1827  499 HOH   C O   
4270 O O   . HOH   M .   ? 0.4191 0.3361 0.3135 -0.1900 0.0380  0.0488  500 HOH   C O   
4271 O O   . HOH   M .   ? 0.5309 0.4765 0.5802 -0.0083 -0.1105 -0.0789 501 HOH   C O   
4272 O O   . HOH   M .   ? 0.4812 0.5505 0.5116 0.0116  0.2810  0.1044  502 HOH   C O   
4273 O O   . HOH   M .   ? 0.1968 0.4333 0.3051 -0.0151 -0.0769 0.0844  503 HOH   C O   
4274 O O   . HOH   M .   ? 0.2613 0.3418 0.2856 0.0526  0.0737  -0.0230 504 HOH   C O   
4275 O O   . HOH   M .   ? 0.3644 0.2948 0.2877 0.0286  -0.0850 -0.0710 505 HOH   C O   
4276 O O   . HOH   M .   ? 0.2549 0.2048 0.2214 -0.0181 -0.0431 0.0599  506 HOH   C O   
4277 O O   . HOH   M .   ? 0.3404 0.4308 0.5889 -0.0455 -0.1900 0.0972  507 HOH   C O   
4278 O O   . HOH   M .   ? 0.4939 0.5827 0.3176 0.3156  0.0231  -0.0032 508 HOH   C O   
4279 O O   . HOH   M .   ? 0.4855 0.3826 0.4607 -0.1470 -0.1900 -0.0426 509 HOH   C O   
4280 O O   . HOH   M .   ? 0.5090 0.7174 0.3556 0.1802  -0.0145 0.0923  510 HOH   C O   
4281 O O   . HOH   M .   ? 0.3590 0.3709 0.3499 -0.1564 0.1683  -0.0719 511 HOH   C O   
4282 O O   . HOH   M .   ? 0.5118 0.4904 0.4001 -0.0790 -0.0094 0.2530  512 HOH   C O   
4283 O O   . HOH   M .   ? 0.6654 0.5162 0.3559 -0.0176 -0.0803 0.0183  513 HOH   C O   
4284 O O   . HOH   M .   ? 0.3728 0.3507 0.4416 -0.0106 -0.1526 0.0641  514 HOH   C O   
4285 O O   . HOH   M .   ? 0.5072 0.3083 0.4596 0.0473  -0.0989 -0.1667 515 HOH   C O   
4286 O O   . HOH   M .   ? 0.2972 0.4453 0.3048 -0.0416 0.0470  -0.0277 516 HOH   C O   
4287 O O   . HOH   M .   ? 0.4321 0.2389 0.2593 -0.0697 -0.0629 0.0044  517 HOH   C O   
4288 O O   . HOH   M .   ? 0.6107 0.3434 0.4036 -0.1900 -0.1900 0.0218  518 HOH   C O   
4289 O O   . HOH   M .   ? 0.2878 0.3324 0.3026 -0.0429 0.0761  -0.0315 519 HOH   C O   
4290 O O   . HOH   M .   ? 0.5887 0.5962 0.5230 0.0121  0.2126  0.1787  520 HOH   C O   
4291 O O   . HOH   M .   ? 0.4049 0.2885 0.3977 -0.0750 0.0030  0.0791  521 HOH   C O   
4292 O O   . HOH   M .   ? 0.5117 0.4344 0.3974 -0.1069 -0.0337 0.1086  522 HOH   C O   
4293 O O   . HOH   M .   ? 0.4942 0.3996 0.3172 0.2326  0.0113  -0.0146 523 HOH   C O   
4294 O O   . HOH   M .   ? 0.4804 0.4830 0.4010 -0.0745 -0.1116 -0.1158 524 HOH   C O   
4295 O O   . HOH   M .   ? 0.6800 0.4908 0.4196 -0.1320 0.0930  -0.0484 525 HOH   C O   
4296 O O   . HOH   M .   ? 0.3640 0.2174 0.3144 0.0139  0.0049  -0.0402 526 HOH   C O   
4297 O O   . HOH   M .   ? 0.4444 0.5856 0.5140 0.0446  -0.1900 0.1695  527 HOH   C O   
4298 O O   . HOH   M .   ? 0.4514 0.5754 0.5351 0.0167  0.0585  -0.0276 528 HOH   C O   
4299 O O   . HOH   M .   ? 0.7084 0.8131 0.8331 -0.0951 -0.0402 -0.0257 529 HOH   C O   
4300 O O   . HOH   M .   ? 0.6174 0.4878 0.5418 -0.1172 0.0363  0.2029  530 HOH   C O   
4301 O O   . HOH   M .   ? 0.5081 0.4083 0.3921 -0.1292 0.0488  0.0834  531 HOH   C O   
4302 O O   . HOH   M .   ? 0.4194 0.3163 0.3463 0.0129  -0.1273 -0.0763 532 HOH   C O   
4303 O O   . HOH   M .   ? 0.4273 0.3289 0.3103 0.0469  0.0356  0.0065  533 HOH   C O   
4304 O O   . HOH   M .   ? 0.5320 0.6403 0.7686 -0.1298 -0.1219 0.2543  534 HOH   C O   
4305 O O   . HOH   M .   ? 0.4605 0.4571 0.4742 -0.0966 0.0946  -0.1121 535 HOH   C O   
4306 O O   . HOH   M .   ? 0.2511 0.4974 0.2707 -0.0327 0.0231  -0.0343 536 HOH   C O   
4307 O O   . HOH   M .   ? 0.4770 0.6211 0.6390 0.1580  -0.0652 0.0731  537 HOH   C O   
4308 O O   . HOH   M .   ? 0.6802 0.6444 0.5349 -0.0914 -0.0676 0.0649  538 HOH   C O   
4309 O O   . HOH   M .   ? 0.5514 0.4142 0.3433 -0.0640 -0.1318 -0.0644 539 HOH   C O   
4310 O O   . HOH   M .   ? 0.3349 0.3349 0.9330 0.0237  0.0370  0.1290  540 HOH   C O   
4311 O O   . HOH   M .   ? 0.3277 0.2348 0.5589 -0.0028 -0.0494 -0.0637 541 HOH   C O   
4312 O O   . HOH   M .   ? 0.5155 0.4559 0.3202 -0.0149 0.0157  0.0294  542 HOH   C O   
4313 O O   . HOH   M .   ? 0.3355 0.3082 0.4135 0.0188  0.0258  -0.0263 543 HOH   C O   
4314 O O   . HOH   M .   ? 0.3193 0.3192 0.3162 -0.0570 -0.0201 0.0014  544 HOH   C O   
4315 O O   . HOH   M .   ? 0.7309 0.6026 0.5879 0.1879  -0.0202 -0.0578 545 HOH   C O   
4316 O O   . HOH   M .   ? 0.2616 0.2853 0.3234 0.0287  0.0443  0.0154  546 HOH   C O   
4317 O O   . HOH   M .   ? 0.4077 0.3021 0.6885 -0.0826 -0.0970 0.0104  547 HOH   C O   
4318 O O   . HOH   M .   ? 0.4222 0.6297 0.4450 -0.0562 -0.0750 0.0829  548 HOH   C O   
4319 O O   . HOH   M .   ? 0.7017 0.6301 0.5930 -0.0176 0.0435  0.2009  549 HOH   C O   
4320 O O   . HOH   M .   ? 0.6638 0.3336 0.5239 0.0666  -0.1252 0.1817  550 HOH   C O   
4321 O O   . HOH   M .   ? 0.3364 0.4706 0.4255 0.0532  -0.0862 0.0795  551 HOH   C O   
4322 O O   . HOH   M .   ? 0.3321 0.6902 0.2369 0.2185  0.0153  -0.0230 552 HOH   C O   
4323 O O   . HOH   M .   ? 0.6040 0.6099 0.4958 -0.0472 0.0147  -0.0934 553 HOH   C O   
4324 O O   . HOH   M .   ? 0.2655 0.2963 0.4393 0.0260  0.0175  -0.0644 554 HOH   C O   
4325 O O   . HOH   M .   ? 0.4163 0.3084 0.2014 -0.1131 0.0785  -0.0300 555 HOH   C O   
4326 O O   . HOH   M .   ? 0.5165 0.2152 0.3562 -0.0017 0.1186  0.0073  556 HOH   C O   
4327 O O   . HOH   M .   ? 0.6051 0.5245 0.5726 -0.0721 0.2322  -0.0772 557 HOH   C O   
4328 O O   . HOH   M .   ? 0.1733 0.2370 0.2141 0.0038  -0.0010 -0.0091 558 HOH   C O   
4329 O O   . HOH   M .   ? 0.4716 0.2914 0.5047 -0.0870 0.2071  0.0595  559 HOH   C O   
4330 O O   . HOH   M .   ? 0.4726 0.5952 0.6490 0.0579  0.2277  -0.1311 560 HOH   C O   
4331 O O   . HOH   M .   ? 0.7069 0.4648 0.6085 0.0001  0.0021  -0.1333 561 HOH   C O   
4332 O O   . HOH   M .   ? 0.4618 0.4852 0.4251 0.0504  0.0768  -0.1307 562 HOH   C O   
4333 O O   . HOH   M .   ? 0.6033 0.6396 0.5785 0.2910  0.1337  0.0622  563 HOH   C O   
4334 O O   . HOH   M .   ? 0.4122 0.6486 0.7205 0.0068  0.0390  0.0449  564 HOH   C O   
4335 O O   . HOH   M .   ? 0.4946 0.6045 0.5982 0.1925  -0.0751 0.1508  565 HOH   C O   
4336 O O   . HOH   M .   ? 0.4522 0.4042 0.5514 -0.0732 -0.0472 -0.0940 566 HOH   C O   
4337 O O   . HOH   M .   ? 0.5115 0.5199 0.4390 0.1847  -0.0845 0.0072  567 HOH   C O   
4338 O O   . HOH   M .   ? 0.6301 0.4057 0.4694 -0.1642 0.2677  -0.0116 568 HOH   C O   
4339 O O   . HOH   M .   ? 0.6794 0.6097 0.5176 0.1391  -0.0613 -0.0698 569 HOH   C O   
4340 O O   . HOH   M .   ? 0.6046 0.4319 0.5078 0.0538  0.2469  0.1970  570 HOH   C O   
4341 O O   . HOH   M .   ? 0.6390 0.5054 0.7173 0.2419  -0.0713 0.0649  571 HOH   C O   
4342 O O   . HOH   M .   ? 0.4338 0.2365 0.2856 -0.0307 -0.0165 -0.0409 572 HOH   C O   
4343 O O   . HOH   M .   ? 0.3852 0.5828 0.4515 -0.1067 0.0889  0.0773  573 HOH   C O   
4344 O O   . HOH   M .   ? 0.3221 0.4903 0.2725 0.1309  -0.0839 -0.0527 574 HOH   C O   
4345 O O   . HOH   M .   ? 0.5885 0.2474 0.5241 -0.0770 0.0164  0.0367  575 HOH   C O   
4346 O O   . HOH   M .   ? 0.2538 0.3077 0.3370 -0.0491 -0.0309 -0.0086 576 HOH   C O   
4347 O O   . HOH   M .   ? 0.2974 0.3529 0.4921 -0.1321 0.0395  -0.0210 577 HOH   C O   
4348 O O   . HOH   M .   ? 0.5795 0.4070 0.5484 0.0011  -0.0777 0.0326  578 HOH   C O   
4349 O O   . HOH   M .   ? 0.6222 0.3349 0.5582 -0.0551 0.1282  -0.1216 579 HOH   C O   
4350 O O   . HOH   M .   ? 0.5541 0.5832 0.6201 0.1761  0.2645  0.1455  580 HOH   C O   
4351 O O   . HOH   M .   ? 0.6829 0.5931 0.4615 0.0825  -0.1900 0.2147  581 HOH   C O   
4352 O O   . HOH   M .   ? 0.6042 0.2957 0.4803 -0.0194 0.0407  0.0483  582 HOH   C O   
4353 O O   . HOH   M .   ? 0.4613 0.3039 0.5697 0.1284  -0.0955 -0.0873 583 HOH   C O   
4354 O O   . HOH   M .   ? 0.5357 0.4166 0.3920 -0.0686 -0.1082 -0.0869 584 HOH   C O   
4355 O O   . HOH   M .   ? 0.7202 0.4813 0.3244 0.0092  0.2383  -0.0274 585 HOH   C O   
4356 O O   . HOH   M .   ? 0.4190 0.5326 0.5717 -0.1552 -0.0322 -0.0475 586 HOH   C O   
4357 O O   . HOH   M .   ? 0.7077 0.5516 0.3807 -0.1773 -0.0350 -0.1220 587 HOH   C O   
4358 O O   . HOH   M .   ? 0.5538 0.3816 0.5129 -0.1189 0.0086  0.0942  588 HOH   C O   
4359 O O   . HOH   M .   ? 0.4436 0.2826 0.4133 -0.0989 -0.0272 0.0227  589 HOH   C O   
4360 O O   . HOH   M .   ? 0.6651 0.5994 0.3580 -0.1464 0.0675  0.1523  590 HOH   C O   
4361 O O   . HOH   M .   ? 0.4193 0.4052 0.4450 -0.1108 0.1531  -0.1836 591 HOH   C O   
4362 O O   . HOH   M .   ? 0.4246 0.3557 0.3927 -0.0301 0.0155  -0.0482 592 HOH   C O   
4363 O O   . HOH   M .   ? 0.6706 0.3847 0.3387 0.1115  0.0487  -0.0210 593 HOH   C O   
4364 O O   . HOH   M .   ? 0.3561 0.4482 0.6508 -0.0827 -0.0212 0.0612  594 HOH   C O   
4365 O O   . HOH   M .   ? 0.5004 0.5465 0.2913 0.0202  -0.0445 0.0328  595 HOH   C O   
4366 O O   . HOH   M .   ? 0.2617 0.2473 0.3231 0.0305  0.0359  0.0242  596 HOH   C O   
4367 O O   . HOH   M .   ? 0.6679 0.5585 0.5342 0.2290  -0.0218 0.0218  597 HOH   C O   
4368 O O   . HOH   M .   ? 0.2602 0.3486 0.4198 -0.0614 0.1223  0.0191  598 HOH   C O   
4369 O O   . HOH   M .   ? 0.4093 0.4564 0.4513 0.0467  -0.0141 -0.1247 599 HOH   C O   
4370 O O   . HOH   M .   ? 0.4921 0.5028 0.6695 -0.1129 0.0487  -0.0950 600 HOH   C O   
4371 O O   . HOH   M .   ? 0.6164 0.7456 0.5033 0.1150  0.3110  -0.0079 601 HOH   C O   
4372 O O   . HOH   M .   ? 0.7137 0.6494 0.5762 0.0067  0.1698  0.2154  602 HOH   C O   
4373 O O   . HOH   N .   ? 0.4708 0.5804 0.3769 0.1871  -0.0269 -0.0113 301 HOH   D O   
4374 O O   . HOH   N .   ? 0.5128 0.5457 0.4553 -0.0881 -0.0720 -0.0208 302 HOH   D O   
4375 O O   . HOH   N .   ? 0.5571 0.5607 0.3804 0.1412  0.0415  -0.1679 303 HOH   D O   
4376 O O   . HOH   N .   ? 0.3273 0.3265 0.2954 0.0185  -0.0404 0.0091  304 HOH   D O   
4377 O O   . HOH   N .   ? 0.4614 0.7780 0.3309 -0.0482 0.0097  0.0187  305 HOH   D O   
4378 O O   . HOH   N .   ? 0.5134 0.4892 0.2598 0.0101  -0.0151 0.0472  306 HOH   D O   
4379 O O   . HOH   N .   ? 0.3177 0.5767 0.3016 0.0929  -0.0986 -0.0040 307 HOH   D O   
4380 O O   . HOH   N .   ? 0.1725 0.2120 0.1664 0.0306  0.0008  -0.0738 308 HOH   D O   
4381 O O   . HOH   N .   ? 0.7864 0.6363 0.7171 -0.1222 -0.0481 0.1693  309 HOH   D O   
4382 O O   . HOH   N .   ? 0.2442 0.2126 0.2046 -0.0319 0.0041  -0.0337 310 HOH   D O   
4383 O O   . HOH   N .   ? 0.4265 0.6681 0.3495 0.0876  0.1963  -0.0199 311 HOH   D O   
4384 O O   . HOH   N .   ? 0.2667 0.4970 0.4887 0.1573  -0.0212 -0.1299 312 HOH   D O   
4385 O O   . HOH   N .   ? 0.7729 0.5690 0.6989 0.1070  -0.0765 0.1077  313 HOH   D O   
4386 O O   . HOH   N .   ? 0.3707 0.6630 0.2998 0.1083  -0.0876 0.1198  314 HOH   D O   
4387 O O   . HOH   N .   ? 0.2384 0.2102 0.1255 0.0116  0.0465  0.0207  315 HOH   D O   
4388 O O   . HOH   N .   ? 0.2977 0.6557 0.2218 -0.1770 -0.0371 -0.0144 316 HOH   D O   
4389 O O   . HOH   N .   ? 0.5539 0.5563 0.3566 -0.0135 -0.1102 0.2298  317 HOH   D O   
4390 O O   . HOH   N .   ? 0.2205 0.2512 0.3355 -0.0130 -0.0349 -0.0316 318 HOH   D O   
4391 O O   . HOH   N .   ? 0.5972 0.5620 0.5816 -0.1870 0.0459  -0.1155 319 HOH   D O   
4392 O O   . HOH   N .   ? 0.6736 0.4797 0.2856 0.0461  0.0119  0.0430  320 HOH   D O   
4393 O O   . HOH   N .   ? 0.4612 0.3214 0.1751 0.2201  -0.0628 -0.0461 321 HOH   D O   
4394 O O   . HOH   N .   ? 0.4699 0.5912 0.2733 0.1298  -0.0130 -0.0553 322 HOH   D O   
4395 O O   . HOH   N .   ? 0.5877 0.4880 0.5929 -0.1233 -0.0768 0.0716  323 HOH   D O   
4396 O O   . HOH   N .   ? 0.1859 0.3046 0.2749 0.0101  0.0340  -0.0915 324 HOH   D O   
4397 O O   . HOH   N .   ? 0.2127 0.3516 0.1776 -0.0495 0.0203  0.0160  325 HOH   D O   
4398 O O   . HOH   N .   ? 0.3994 0.2527 0.1486 0.1033  -0.0686 0.0118  326 HOH   D O   
4399 O O   . HOH   N .   ? 0.1981 0.6020 0.2115 -0.1125 0.0334  -0.1282 327 HOH   D O   
4400 O O   . HOH   N .   ? 0.1472 0.1758 0.1673 -0.0009 -0.0069 0.0158  328 HOH   D O   
4401 O O   . HOH   N .   ? 0.1497 0.2286 0.2593 -0.0227 0.0072  -0.0238 329 HOH   D O   
4402 O O   . HOH   N .   ? 0.2488 0.3094 0.4155 0.0281  -0.1033 -0.0256 330 HOH   D O   
4403 O O   . HOH   N .   ? 0.5774 0.6210 0.5396 0.3276  0.0749  -0.0767 331 HOH   D O   
4404 O O   . HOH   N .   ? 0.5441 0.3028 0.4701 -0.0865 0.1517  0.0088  332 HOH   D O   
4405 O O   . HOH   N .   ? 0.3306 0.4036 0.5522 -0.1144 -0.0476 0.2417  333 HOH   D O   
4406 O O   . HOH   N .   ? 0.2024 0.1869 0.1879 -0.0015 -0.0178 -0.0265 334 HOH   D O   
4407 O O   . HOH   N .   ? 0.4098 0.6700 0.7048 0.2921  0.0041  0.0472  335 HOH   D O   
4408 O O   . HOH   N .   ? 0.2809 0.2688 0.2566 0.0895  0.0927  0.1091  336 HOH   D O   
4409 O O   . HOH   N .   ? 0.6132 0.2186 0.3129 0.0806  -0.1749 -0.0706 337 HOH   D O   
4410 O O   . HOH   N .   ? 1.1487 1.1252 1.1135 -0.0521 -0.0320 0.0908  338 HOH   D O   
4411 O O   . HOH   N .   ? 0.3565 0.2656 0.4683 0.0247  -0.1900 0.0193  339 HOH   D O   
4412 O O   . HOH   N .   ? 0.2047 0.2484 0.2268 0.0342  0.0032  -0.0314 340 HOH   D O   
4413 O O   . HOH   N .   ? 0.4257 0.6346 0.5669 0.0724  0.2008  0.0372  341 HOH   D O   
4414 O O   . HOH   N .   ? 0.5853 0.7186 0.3807 -0.1084 0.2102  -0.0508 342 HOH   D O   
4415 O O   . HOH   N .   ? 0.3523 0.4619 0.5032 -0.1163 -0.1900 0.1526  343 HOH   D O   
4416 O O   . HOH   N .   ? 0.2354 0.3693 0.4187 0.0413  -0.0534 -0.1191 344 HOH   D O   
4417 O O   . HOH   N .   ? 0.2991 0.3985 0.2423 0.0414  0.0120  -0.0076 345 HOH   D O   
4418 O O   . HOH   N .   ? 0.4087 0.5268 0.5468 0.0802  0.0449  -0.0519 346 HOH   D O   
4419 O O   . HOH   N .   ? 0.2369 0.3519 0.1517 -0.0319 -0.0303 0.0275  347 HOH   D O   
4420 O O   . HOH   N .   ? 0.3509 0.4114 0.2494 0.0112  -0.0305 -0.0607 348 HOH   D O   
4421 O O   . HOH   N .   ? 0.3343 0.5930 0.3615 -0.0006 -0.1386 0.0317  349 HOH   D O   
4422 O O   . HOH   N .   ? 0.3208 0.5763 0.3487 0.0509  -0.0566 0.1653  350 HOH   D O   
4423 O O   . HOH   N .   ? 0.1610 0.2360 0.1700 0.0220  0.0035  -0.0218 351 HOH   D O   
4424 O O   . HOH   N .   ? 0.2070 0.3469 0.6399 -0.0360 0.0983  -0.1680 352 HOH   D O   
4425 O O   . HOH   N .   ? 0.5969 0.5693 0.3394 0.0031  0.1360  0.0626  353 HOH   D O   
4426 O O   . HOH   N .   ? 0.3812 0.2492 0.3687 -0.0286 -0.0863 0.0371  354 HOH   D O   
4427 O O   . HOH   N .   ? 0.4521 0.6492 0.5477 -0.0188 -0.0570 -0.0781 355 HOH   D O   
4428 O O   . HOH   N .   ? 0.4327 0.3570 0.1801 0.1488  -0.0332 0.0033  356 HOH   D O   
4429 O O   . HOH   N .   ? 0.4230 0.6129 0.6170 -0.0735 -0.0497 -0.1210 357 HOH   D O   
4430 O O   . HOH   N .   ? 0.2073 0.3164 0.2257 -0.0214 -0.0279 -0.0030 358 HOH   D O   
4431 O O   . HOH   N .   ? 0.2101 0.1858 0.1782 0.0696  -0.0248 -0.0532 359 HOH   D O   
4432 O O   . HOH   N .   ? 0.2146 0.2409 0.2757 0.0311  0.0486  -0.0326 360 HOH   D O   
4433 O O   . HOH   N .   ? 0.5274 0.4366 0.4119 0.1171  -0.1900 -0.0423 361 HOH   D O   
4434 O O   . HOH   N .   ? 0.5176 0.6528 0.2909 0.3198  -0.0024 0.0164  362 HOH   D O   
4435 O O   . HOH   N .   ? 0.3103 0.2013 0.4499 0.0764  -0.0681 -0.0474 363 HOH   D O   
4436 O O   . HOH   N .   ? 0.4647 0.4084 0.2389 -0.0838 0.0271  -0.0845 364 HOH   D O   
4437 O O   . HOH   N .   ? 0.1838 0.1794 0.2359 0.0161  -0.0488 0.0445  365 HOH   D O   
4438 O O   . HOH   N .   ? 0.3008 0.2417 0.1878 0.0420  0.0596  0.0527  366 HOH   D O   
4439 O O   . HOH   N .   ? 0.5692 0.2647 0.2273 0.0417  0.0613  -0.0144 367 HOH   D O   
4440 O O   . HOH   N .   ? 0.4537 0.5367 0.3154 0.2212  -0.1590 -0.1681 368 HOH   D O   
4441 O O   . HOH   N .   ? 0.5244 0.3919 0.7412 0.1015  0.1390  0.1950  369 HOH   D O   
4442 O O   . HOH   N .   ? 0.1663 0.2314 0.2202 0.0108  0.0043  -0.0468 370 HOH   D O   
4443 O O   . HOH   N .   ? 0.3559 0.3455 0.4382 -0.0189 -0.0829 0.0859  371 HOH   D O   
4444 O O   . HOH   N .   ? 0.6177 0.5308 0.3346 0.2946  0.1864  0.1358  372 HOH   D O   
4445 O O   . HOH   N .   ? 0.4655 0.5696 0.7216 0.0275  -0.1118 -0.0026 373 HOH   D O   
4446 O O   . HOH   N .   ? 0.3174 0.2942 0.3522 0.0453  -0.0466 -0.0442 374 HOH   D O   
4447 O O   . HOH   N .   ? 0.4152 0.6429 0.5051 -0.1867 -0.0168 -0.0161 375 HOH   D O   
4448 O O   . HOH   N .   ? 0.4292 0.6636 0.4317 -0.0486 -0.0277 -0.1319 376 HOH   D O   
4449 O O   . HOH   N .   ? 0.2503 0.4038 0.5059 -0.0495 0.0999  -0.1900 377 HOH   D O   
4450 O O   . HOH   N .   ? 0.4710 0.3514 0.3452 0.0114  0.1318  0.1485  378 HOH   D O   
4451 O O   . HOH   N .   ? 0.7431 0.4334 0.4505 0.0160  -0.0100 0.0525  379 HOH   D O   
4452 O O   . HOH   N .   ? 0.6697 0.3636 0.2231 -0.1164 -0.0419 -0.0197 380 HOH   D O   
4453 O O   . HOH   N .   ? 0.2180 0.2682 0.1918 0.0182  -0.0040 0.0384  381 HOH   D O   
4454 O O   . HOH   N .   ? 0.6401 0.7085 0.4897 0.1097  0.2530  -0.0669 382 HOH   D O   
4455 O O   . HOH   N .   ? 0.3157 0.3911 0.3111 0.1569  -0.1280 -0.0928 383 HOH   D O   
4456 O O   . HOH   N .   ? 0.4023 0.4385 0.3456 0.0178  0.0696  0.1333  384 HOH   D O   
4457 O O   . HOH   N .   ? 0.2065 0.6695 0.3317 -0.0628 -0.0482 0.0030  385 HOH   D O   
4458 O O   . HOH   N .   ? 0.2888 0.4310 0.6385 0.1224  -0.0163 -0.0944 386 HOH   D O   
4459 O O   . HOH   N .   ? 0.3048 0.5265 0.5706 0.1075  -0.1196 0.0509  387 HOH   D O   
4460 O O   . HOH   N .   ? 0.1800 0.3304 0.2555 -0.0670 0.0029  -0.0167 388 HOH   D O   
4461 O O   . HOH   N .   ? 0.4678 0.4854 0.2393 0.1088  -0.0800 -0.0528 389 HOH   D O   
4462 O O   . HOH   N .   ? 0.3316 0.6120 0.2611 -0.1458 -0.0501 -0.0293 390 HOH   D O   
4463 O O   . HOH   N .   ? 0.6520 0.2887 0.3084 0.1602  -0.0311 0.0727  391 HOH   D O   
4464 O O   . HOH   N .   ? 0.2573 0.3804 0.3263 0.0126  -0.0967 -0.0452 392 HOH   D O   
4465 O O   . HOH   N .   ? 0.2138 0.3399 0.2347 -0.0005 -0.0005 -0.0970 393 HOH   D O   
4466 O O   . HOH   N .   ? 0.4055 0.4468 0.4169 0.0704  0.0028  -0.0588 394 HOH   D O   
4467 O O   . HOH   N .   ? 0.4594 0.7420 0.4363 0.2751  -0.0332 0.1119  395 HOH   D O   
4468 O O   . HOH   N .   ? 0.8690 0.6675 0.6916 -0.0296 0.2008  0.0854  396 HOH   D O   
4469 O O   . HOH   N .   ? 0.3067 0.7055 0.4041 0.1164  -0.0974 -0.1308 397 HOH   D O   
4470 O O   . HOH   N .   ? 0.5193 0.5793 0.4753 0.0052  0.2165  0.0231  398 HOH   D O   
4471 O O   . HOH   N .   ? 0.3426 0.3215 0.4715 0.1133  0.0697  -0.0730 399 HOH   D O   
4472 O O   . HOH   N .   ? 0.5255 0.4865 0.5646 0.0754  0.0857  -0.0732 400 HOH   D O   
4473 O O   . HOH   N .   ? 0.3775 0.2537 0.3665 0.0195  -0.0141 -0.0693 401 HOH   D O   
4474 O O   . HOH   N .   ? 0.6201 0.6932 0.6351 -0.0884 0.1271  0.2554  402 HOH   D O   
4475 O O   . HOH   N .   ? 0.6208 0.5010 0.3230 0.0739  -0.1460 -0.0389 403 HOH   D O   
4476 O O   . HOH   N .   ? 0.2812 0.5802 0.2531 0.0096  -0.0164 0.0716  404 HOH   D O   
4477 O O   . HOH   N .   ? 0.2837 0.6723 0.2511 0.2032  0.0241  0.0582  405 HOH   D O   
4478 O O   . HOH   N .   ? 0.5377 0.3457 0.3893 -0.0043 -0.0108 -0.0978 406 HOH   D O   
4479 O O   . HOH   N .   ? 0.4687 0.8613 0.3987 -0.0352 0.0088  0.0088  407 HOH   D O   
4480 O O   . HOH   N .   ? 0.3967 0.6859 0.6614 0.1091  -0.1097 -0.0244 408 HOH   D O   
4481 O O   . HOH   N .   ? 0.2484 0.5843 0.5214 0.1408  -0.0067 -0.1368 409 HOH   D O   
4482 O O   . HOH   N .   ? 0.6731 0.6933 0.4344 0.0161  -0.0852 -0.1737 410 HOH   D O   
4483 O O   . HOH   N .   ? 0.3366 0.3349 0.2221 0.1098  -0.0566 -0.0086 411 HOH   D O   
4484 O O   . HOH   N .   ? 0.5661 0.3879 0.3592 0.1400  0.0476  0.0768  412 HOH   D O   
4485 O O   . HOH   N .   ? 0.4321 0.4174 0.3655 -0.0812 -0.0559 0.1351  413 HOH   D O   
4486 O O   . HOH   N .   ? 0.5818 0.6611 0.4202 -0.0970 -0.0796 -0.0748 414 HOH   D O   
4487 O O   . HOH   N .   ? 0.3957 0.5072 0.6336 0.2071  -0.0645 0.0365  415 HOH   D O   
4488 O O   . HOH   N .   ? 0.4276 0.4827 0.3841 0.0346  0.0159  -0.0439 416 HOH   D O   
4489 O O   . HOH   N .   ? 0.2573 0.2920 0.2198 -0.0488 -0.0386 -0.0097 417 HOH   D O   
4490 O O   . HOH   N .   ? 0.4770 0.5004 0.6480 0.0685  -0.1305 -0.0716 418 HOH   D O   
4491 O O   . HOH   N .   ? 0.6146 0.4299 0.4965 0.2358  0.0230  0.0244  419 HOH   D O   
4492 O O   . HOH   N .   ? 0.6914 0.3049 0.4351 -0.0737 0.2829  0.0116  420 HOH   D O   
4493 O O   . HOH   N .   ? 0.5791 0.5568 0.3638 0.2399  -0.0628 0.0062  421 HOH   D O   
4494 O O   . HOH   N .   ? 0.4362 0.4661 0.6669 0.1667  -0.0476 -0.1712 422 HOH   D O   
4495 O O   . HOH   N .   ? 0.2797 0.3287 0.3129 -0.0142 0.0457  -0.0885 423 HOH   D O   
4496 O O   . HOH   N .   ? 0.3904 0.2086 0.2612 -0.0390 0.0381  -0.0294 424 HOH   D O   
4497 O O   . HOH   N .   ? 0.3302 0.5326 0.4920 -0.0576 -0.1176 -0.0624 425 HOH   D O   
4498 O O   . HOH   N .   ? 0.3125 0.3912 0.4523 0.0219  -0.0709 -0.1277 426 HOH   D O   
4499 O O   . HOH   N .   ? 0.6840 0.5739 0.3507 0.1305  0.0388  0.0438  427 HOH   D O   
4500 O O   . HOH   N .   ? 0.6183 0.4315 0.5602 -0.0538 0.1335  0.1152  428 HOH   D O   
4501 O O   . HOH   N .   ? 0.3935 0.4897 0.7306 0.0257  -0.1255 0.1556  429 HOH   D O   
4502 O O   . HOH   N .   ? 0.6185 0.6178 0.5118 0.0759  0.0710  -0.0651 430 HOH   D O   
4503 O O   . HOH   N .   ? 0.7753 0.3866 0.3124 0.0873  0.0810  -0.0235 431 HOH   D O   
4504 O O   . HOH   N .   ? 0.5694 0.4604 0.3997 0.0870  0.0982  0.0161  432 HOH   D O   
4505 O O   . HOH   N .   ? 0.5521 0.4528 0.2462 0.1751  -0.0885 -0.0672 433 HOH   D O   
4506 O O   . HOH   N .   ? 0.4897 0.5514 0.7278 -0.0335 -0.0597 0.1633  434 HOH   D O   
4507 O O   . HOH   N .   ? 0.4945 0.6948 0.7093 0.1224  -0.0925 0.0227  435 HOH   D O   
4508 O O   . HOH   N .   ? 0.5879 0.4892 0.4212 0.1127  0.2653  0.1385  436 HOH   D O   
4509 O O   . HOH   N .   ? 0.3615 0.3168 0.4550 0.0496  0.0145  0.1014  437 HOH   D O   
4510 O O   . HOH   N .   ? 0.6443 0.6626 0.6596 0.1128  0.0769  0.1601  438 HOH   D O   
4511 O O   . HOH   N .   ? 0.4449 0.4483 0.6068 -0.0309 -0.1896 -0.1768 439 HOH   D O   
4512 O O   . HOH   N .   ? 0.2026 0.3489 0.1927 0.0606  -0.0014 -0.0689 440 HOH   D O   
4513 O O   . HOH   N .   ? 0.4678 0.4873 0.5005 0.1610  0.1698  -0.0070 441 HOH   D O   
4514 O O   . HOH   N .   ? 0.2809 0.6213 0.5074 0.0570  -0.0210 -0.0908 442 HOH   D O   
4515 O O   . HOH   N .   ? 0.6426 0.4944 0.2671 0.0677  -0.1020 0.1280  443 HOH   D O   
4516 O O   . HOH   N .   ? 0.6167 0.4952 0.5317 0.1895  0.1393  0.2431  444 HOH   D O   
4517 O O   . HOH   N .   ? 0.4734 0.3597 0.2686 0.0026  -0.1726 0.0374  445 HOH   D O   
4518 O O   . HOH   N .   ? 0.6703 0.6447 0.7574 -0.0795 -0.1332 -0.1466 446 HOH   D O   
4519 O O   . HOH   N .   ? 0.4460 0.5896 0.8362 0.0722  -0.0048 0.0570  447 HOH   D O   
4520 O O   . HOH   N .   ? 0.4634 0.4135 0.3546 -0.1026 0.1331  -0.1570 448 HOH   D O   
4521 O O   . HOH   N .   ? 0.4193 0.5361 0.4551 0.0924  -0.0359 -0.0747 449 HOH   D O   
4522 O O   . HOH   N .   ? 0.3579 0.3588 0.4110 -0.0386 -0.0250 -0.1563 450 HOH   D O   
4523 O O   . HOH   N .   ? 0.5609 0.6009 0.3854 0.1359  -0.0916 0.2138  451 HOH   D O   
4524 O O   . HOH   N .   ? 0.3282 0.6819 0.4138 -0.1194 0.0064  -0.1005 452 HOH   D O   
4525 O O   . HOH   N .   ? 0.3677 0.5301 0.5334 0.1906  -0.0382 -0.0829 453 HOH   D O   
4526 O O   . HOH   N .   ? 0.5149 0.3082 0.2759 0.0903  -0.1051 -0.0396 454 HOH   D O   
4527 O O   . HOH   N .   ? 0.5158 0.6886 0.4539 -0.0229 -0.0597 0.1214  455 HOH   D O   
4528 O O   . HOH   N .   ? 0.2889 0.3402 0.4663 0.1055  -0.0238 0.0115  456 HOH   D O   
4529 O O   . HOH   N .   ? 0.3851 0.6967 0.5560 -0.0134 -0.0195 -0.1618 457 HOH   D O   
4530 O O   . HOH   N .   ? 0.5661 0.5036 0.3336 -0.0608 0.1398  -0.0535 458 HOH   D O   
4531 O O   . HOH   N .   ? 0.4916 0.5420 0.3841 0.1018  -0.0496 -0.1900 459 HOH   D O   
4532 O O   . HOH   N .   ? 0.6688 0.3684 0.4850 -0.0571 -0.1057 0.0082  460 HOH   D O   
4533 O O   . HOH   N .   ? 0.5062 0.4554 0.4438 -0.1092 -0.0706 0.0693  461 HOH   D O   
4534 O O   . HOH   N .   ? 0.5772 0.5147 0.5941 0.1246  0.2804  -0.1021 462 HOH   D O   
4535 O O   . HOH   N .   ? 0.4890 0.5192 0.6421 0.0559  -0.0872 0.0506  463 HOH   D O   
4536 O O   . HOH   N .   ? 0.6269 0.4079 0.3205 -0.1104 -0.0570 -0.1298 464 HOH   D O   
4537 O O   . HOH   N .   ? 0.3726 0.4598 0.5136 0.0845  0.0327  0.0203  465 HOH   D O   
4538 O O   . HOH   N .   ? 0.4153 0.4958 0.4824 0.1549  0.0076  -0.1900 466 HOH   D O   
4539 O O   . HOH   N .   ? 0.6865 0.6536 0.5701 0.0563  -0.0475 -0.0080 467 HOH   D O   
4540 O O   . HOH   N .   ? 0.4175 0.4785 0.3799 0.0498  -0.1325 -0.0595 468 HOH   D O   
4541 O O   . HOH   N .   ? 0.7153 0.7817 0.9423 0.0691  0.0177  -0.0788 469 HOH   D O   
4542 O O   . HOH   N .   ? 0.5001 0.4786 0.6614 -0.0128 -0.0117 0.1041  470 HOH   D O   
4543 O O   . HOH   N .   ? 0.6352 0.6269 0.5700 -0.0521 0.0910  0.1078  471 HOH   D O   
4544 O O   . HOH   N .   ? 0.7110 0.6963 0.5127 0.0558  -0.0523 -0.1328 472 HOH   D O   
# 
