data_9NF9
# 
_entry.id   9NF9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9NF9         pdb_00009nf9 10.2210/pdb9nf9/pdb 
WWPDB D_1000293294 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9NF9 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 geiger@chemistry.msu.edu James Geiger H. 'principal investigator/group leader' 0000-0002-9443-4488 
3 draths@chemistry.msu.edu Karen Draths ?  'principal investigator/group leader' 0000-0001-7852-1090 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Silva, K.'    1 ? 
'Geiger, J.H.' 2 ? 
'Draths, K.'   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                     'cis-CaaD E114N mutant apo' 
_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 'Silva, K.'    1 ? 
primary 'Geiger, J.H.' 2 ? 
primary 'Draths, K.'   3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cis-3-chloroacrylic acid dehalogenase' 18683.770 3  ? E114N ? ? 
2 non-polymer syn 'SULFATE ION'                           96.063    3  ? ?     ? ? 
3 water       nat water                                   18.015    57 ? ?     ? ? 
# 
_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       
;MPVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKG
QLAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVNYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQGLEH
HHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKG
QLAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVNYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQGLEH
HHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   VAL n 
1 4   TYR n 
1 5   MET n 
1 6   VAL n 
1 7   TYR n 
1 8   VAL n 
1 9   SER n 
1 10  GLN n 
1 11  ASP n 
1 12  ARG n 
1 13  LEU n 
1 14  THR n 
1 15  PRO n 
1 16  SER n 
1 17  ALA n 
1 18  LYS n 
1 19  HIS n 
1 20  ALA n 
1 21  VAL n 
1 22  ALA n 
1 23  LYS n 
1 24  ALA n 
1 25  ILE n 
1 26  THR n 
1 27  ASP n 
1 28  ALA n 
1 29  HIS n 
1 30  ARG n 
1 31  GLY n 
1 32  LEU n 
1 33  THR n 
1 34  GLY n 
1 35  THR n 
1 36  GLN n 
1 37  HIS n 
1 38  PHE n 
1 39  LEU n 
1 40  ALA n 
1 41  GLN n 
1 42  VAL n 
1 43  ASN n 
1 44  PHE n 
1 45  GLN n 
1 46  GLU n 
1 47  GLN n 
1 48  PRO n 
1 49  ALA n 
1 50  GLY n 
1 51  ASN n 
1 52  VAL n 
1 53  PHE n 
1 54  LEU n 
1 55  GLY n 
1 56  GLY n 
1 57  VAL n 
1 58  GLN n 
1 59  GLN n 
1 60  GLY n 
1 61  GLY n 
1 62  ASP n 
1 63  THR n 
1 64  ILE n 
1 65  PHE n 
1 66  VAL n 
1 67  HIS n 
1 68  GLY n 
1 69  LEU n 
1 70  HIS n 
1 71  ARG n 
1 72  GLU n 
1 73  GLY n 
1 74  ARG n 
1 75  SER n 
1 76  ALA n 
1 77  ASP n 
1 78  LEU n 
1 79  LYS n 
1 80  GLY n 
1 81  GLN n 
1 82  LEU n 
1 83  ALA n 
1 84  GLN n 
1 85  ARG n 
1 86  ILE n 
1 87  VAL n 
1 88  ASP n 
1 89  ASP n 
1 90  VAL n 
1 91  SER n 
1 92  VAL n 
1 93  ALA n 
1 94  ALA n 
1 95  GLU n 
1 96  ILE n 
1 97  ASP n 
1 98  ARG n 
1 99  LYS n 
1 100 HIS n 
1 101 ILE n 
1 102 TRP n 
1 103 VAL n 
1 104 TYR n 
1 105 PHE n 
1 106 GLY n 
1 107 GLU n 
1 108 MET n 
1 109 PRO n 
1 110 ALA n 
1 111 GLN n 
1 112 GLN n 
1 113 MET n 
1 114 VAL n 
1 115 ASN n 
1 116 TYR n 
1 117 GLY n 
1 118 ARG n 
1 119 PHE n 
1 120 LEU n 
1 121 PRO n 
1 122 GLN n 
1 123 PRO n 
1 124 GLY n 
1 125 HIS n 
1 126 GLU n 
1 127 GLY n 
1 128 GLU n 
1 129 TRP n 
1 130 PHE n 
1 131 ASP n 
1 132 ASN n 
1 133 LEU n 
1 134 SER n 
1 135 SER n 
1 136 ASP n 
1 137 GLU n 
1 138 ARG n 
1 139 ALA n 
1 140 PHE n 
1 141 MET n 
1 142 GLU n 
1 143 THR n 
1 144 ASN n 
1 145 VAL n 
1 146 ASP n 
1 147 VAL n 
1 148 SER n 
1 149 ARG n 
1 150 THR n 
1 151 GLU n 
1 152 ASN n 
1 153 LEU n 
1 154 TYR n 
1 155 PHE n 
1 156 GLN n 
1 157 GLY n 
1 158 LEU n 
1 159 GLU n 
1 160 HIS n 
1 161 HIS n 
1 162 HIS n 
1 163 HIS n 
1 164 HIS n 
1 165 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   165 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 cis-caaD 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'coryneform bacterium' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1728 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   PRO 2   1   1   PRO PRO A . n 
A 1 3   VAL 3   2   2   VAL VAL A . n 
A 1 4   TYR 4   3   3   TYR TYR A . n 
A 1 5   MET 5   4   4   MET MET A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   TYR 7   6   6   TYR TYR A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   SER 9   8   8   SER SER A . n 
A 1 10  GLN 10  9   9   GLN GLN A . n 
A 1 11  ASP 11  10  10  ASP ASP A . n 
A 1 12  ARG 12  11  11  ARG ARG A . n 
A 1 13  LEU 13  12  12  LEU LEU A . n 
A 1 14  THR 14  13  13  THR THR A . n 
A 1 15  PRO 15  14  14  PRO PRO A . n 
A 1 16  SER 16  15  15  SER SER A . n 
A 1 17  ALA 17  16  16  ALA ALA A . n 
A 1 18  LYS 18  17  17  LYS LYS A . n 
A 1 19  HIS 19  18  18  HIS HIS A . n 
A 1 20  ALA 20  19  19  ALA ALA A . n 
A 1 21  VAL 21  20  20  VAL VAL A . n 
A 1 22  ALA 22  21  21  ALA ALA A . n 
A 1 23  LYS 23  22  22  LYS LYS A . n 
A 1 24  ALA 24  23  23  ALA ALA A . n 
A 1 25  ILE 25  24  24  ILE ILE A . n 
A 1 26  THR 26  25  25  THR THR A . n 
A 1 27  ASP 27  26  26  ASP ASP A . n 
A 1 28  ALA 28  27  27  ALA ALA A . n 
A 1 29  HIS 29  28  28  HIS HIS A . n 
A 1 30  ARG 30  29  29  ARG ARG A . n 
A 1 31  GLY 31  30  30  GLY GLY A . n 
A 1 32  LEU 32  31  31  LEU LEU A . n 
A 1 33  THR 33  32  32  THR THR A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  THR 35  34  34  THR THR A . n 
A 1 36  GLN 36  35  35  GLN GLN A . n 
A 1 37  HIS 37  36  36  HIS HIS A . n 
A 1 38  PHE 38  37  37  PHE PHE A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  ALA 40  39  39  ALA ALA A . n 
A 1 41  GLN 41  40  40  GLN GLN A . n 
A 1 42  VAL 42  41  41  VAL VAL A . n 
A 1 43  ASN 43  42  42  ASN ASN A . n 
A 1 44  PHE 44  43  43  PHE PHE A . n 
A 1 45  GLN 45  44  44  GLN GLN A . n 
A 1 46  GLU 46  45  45  GLU GLU A . n 
A 1 47  GLN 47  46  46  GLN GLN A . n 
A 1 48  PRO 48  47  47  PRO PRO A . n 
A 1 49  ALA 49  48  48  ALA ALA A . n 
A 1 50  GLY 50  49  49  GLY GLY A . n 
A 1 51  ASN 51  50  50  ASN ASN A . n 
A 1 52  VAL 52  51  51  VAL VAL A . n 
A 1 53  PHE 53  52  52  PHE PHE A . n 
A 1 54  LEU 54  53  53  LEU LEU A . n 
A 1 55  GLY 55  54  54  GLY GLY A . n 
A 1 56  GLY 56  55  55  GLY GLY A . n 
A 1 57  VAL 57  56  56  VAL VAL A . n 
A 1 58  GLN 58  57  57  GLN GLN A . n 
A 1 59  GLN 59  58  58  GLN GLN A . n 
A 1 60  GLY 60  59  59  GLY GLY A . n 
A 1 61  GLY 61  60  60  GLY GLY A . n 
A 1 62  ASP 62  61  61  ASP ASP A . n 
A 1 63  THR 63  62  62  THR THR A . n 
A 1 64  ILE 64  63  63  ILE ILE A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  VAL 66  65  65  VAL VAL A . n 
A 1 67  HIS 67  66  66  HIS HIS A . n 
A 1 68  GLY 68  67  67  GLY GLY A . n 
A 1 69  LEU 69  68  68  LEU LEU A . n 
A 1 70  HIS 70  69  69  HIS HIS A . n 
A 1 71  ARG 71  70  70  ARG ARG A . n 
A 1 72  GLU 72  71  71  GLU GLU A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  ARG 74  73  73  ARG ARG A . n 
A 1 75  SER 75  74  74  SER SER A . n 
A 1 76  ALA 76  75  75  ALA ALA A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  LEU 78  77  77  LEU LEU A . n 
A 1 79  LYS 79  78  78  LYS LYS A . n 
A 1 80  GLY 80  79  79  GLY GLY A . n 
A 1 81  GLN 81  80  80  GLN GLN A . n 
A 1 82  LEU 82  81  81  LEU LEU A . n 
A 1 83  ALA 83  82  82  ALA ALA A . n 
A 1 84  GLN 84  83  83  GLN GLN A . n 
A 1 85  ARG 85  84  84  ARG ARG A . n 
A 1 86  ILE 86  85  85  ILE ILE A . n 
A 1 87  VAL 87  86  86  VAL VAL A . n 
A 1 88  ASP 88  87  87  ASP ASP A . n 
A 1 89  ASP 89  88  88  ASP ASP A . n 
A 1 90  VAL 90  89  89  VAL VAL A . n 
A 1 91  SER 91  90  90  SER SER A . n 
A 1 92  VAL 92  91  91  VAL VAL A . n 
A 1 93  ALA 93  92  92  ALA ALA A . n 
A 1 94  ALA 94  93  93  ALA ALA A . n 
A 1 95  GLU 95  94  94  GLU GLU A . n 
A 1 96  ILE 96  95  95  ILE ILE A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  ARG 98  97  97  ARG ARG A . n 
A 1 99  LYS 99  98  98  LYS LYS A . n 
A 1 100 HIS 100 99  99  HIS HIS A . n 
A 1 101 ILE 101 100 100 ILE ILE A . n 
A 1 102 TRP 102 101 101 TRP TRP A . n 
A 1 103 VAL 103 102 102 VAL VAL A . n 
A 1 104 TYR 104 103 103 TYR TYR A . n 
A 1 105 PHE 105 104 104 PHE PHE A . n 
A 1 106 GLY 106 105 105 GLY GLY A . n 
A 1 107 GLU 107 106 106 GLU GLU A . n 
A 1 108 MET 108 107 107 MET MET A . n 
A 1 109 PRO 109 108 108 PRO PRO A . n 
A 1 110 ALA 110 109 109 ALA ALA A . n 
A 1 111 GLN 111 110 110 GLN GLN A . n 
A 1 112 GLN 112 111 111 GLN GLN A . n 
A 1 113 MET 113 112 112 MET MET A . n 
A 1 114 VAL 114 113 113 VAL VAL A . n 
A 1 115 ASN 115 114 114 ASN ASN A . n 
A 1 116 TYR 116 115 115 TYR TYR A . n 
A 1 117 GLY 117 116 116 GLY GLY A . n 
A 1 118 ARG 118 117 117 ARG ARG A . n 
A 1 119 PHE 119 118 118 PHE PHE A . n 
A 1 120 LEU 120 119 119 LEU LEU A . n 
A 1 121 PRO 121 120 120 PRO PRO A . n 
A 1 122 GLN 122 121 121 GLN GLN A . n 
A 1 123 PRO 123 122 122 PRO PRO A . n 
A 1 124 GLY 124 123 123 GLY GLY A . n 
A 1 125 HIS 125 124 124 HIS HIS A . n 
A 1 126 GLU 126 125 125 GLU GLU A . n 
A 1 127 GLY 127 126 126 GLY GLY A . n 
A 1 128 GLU 128 127 127 GLU GLU A . n 
A 1 129 TRP 129 128 128 TRP TRP A . n 
A 1 130 PHE 130 129 129 PHE PHE A . n 
A 1 131 ASP 131 130 130 ASP ASP A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 LEU 133 132 132 LEU LEU A . n 
A 1 134 SER 134 133 133 SER SER A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 ASP 136 135 135 ASP ASP A . n 
A 1 137 GLU 137 136 136 GLU GLU A . n 
A 1 138 ARG 138 137 137 ARG ARG A . n 
A 1 139 ALA 139 138 138 ALA ALA A . n 
A 1 140 PHE 140 139 139 PHE PHE A . n 
A 1 141 MET 141 140 140 MET MET A . n 
A 1 142 GLU 142 141 141 GLU GLU A . n 
A 1 143 THR 143 142 142 THR THR A . n 
A 1 144 ASN 144 143 143 ASN ASN A . n 
A 1 145 VAL 145 144 144 VAL VAL A . n 
A 1 146 ASP 146 145 145 ASP ASP A . n 
A 1 147 VAL 147 146 ?   ?   ?   A . n 
A 1 148 SER 148 147 ?   ?   ?   A . n 
A 1 149 ARG 149 148 ?   ?   ?   A . n 
A 1 150 THR 150 149 ?   ?   ?   A . n 
A 1 151 GLU 151 150 ?   ?   ?   A . n 
A 1 152 ASN 152 151 ?   ?   ?   A . n 
A 1 153 LEU 153 152 ?   ?   ?   A . n 
A 1 154 TYR 154 153 ?   ?   ?   A . n 
A 1 155 PHE 155 154 ?   ?   ?   A . n 
A 1 156 GLN 156 155 ?   ?   ?   A . n 
A 1 157 GLY 157 156 ?   ?   ?   A . n 
A 1 158 LEU 158 157 ?   ?   ?   A . n 
A 1 159 GLU 159 158 ?   ?   ?   A . n 
A 1 160 HIS 160 159 ?   ?   ?   A . n 
A 1 161 HIS 161 160 ?   ?   ?   A . n 
A 1 162 HIS 162 161 ?   ?   ?   A . n 
A 1 163 HIS 163 162 ?   ?   ?   A . n 
A 1 164 HIS 164 163 ?   ?   ?   A . n 
A 1 165 HIS 165 164 ?   ?   ?   A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   PRO 2   1   1   PRO PRO B . n 
B 1 3   VAL 3   2   2   VAL VAL B . n 
B 1 4   TYR 4   3   3   TYR TYR B . n 
B 1 5   MET 5   4   4   MET MET B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   TYR 7   6   6   TYR TYR B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   SER 9   8   8   SER SER B . n 
B 1 10  GLN 10  9   9   GLN GLN B . n 
B 1 11  ASP 11  10  10  ASP ASP B . n 
B 1 12  ARG 12  11  11  ARG ARG B . n 
B 1 13  LEU 13  12  12  LEU LEU B . n 
B 1 14  THR 14  13  13  THR THR B . n 
B 1 15  PRO 15  14  14  PRO PRO B . n 
B 1 16  SER 16  15  15  SER SER B . n 
B 1 17  ALA 17  16  16  ALA ALA B . n 
B 1 18  LYS 18  17  17  LYS LYS B . n 
B 1 19  HIS 19  18  18  HIS HIS B . n 
B 1 20  ALA 20  19  19  ALA ALA B . n 
B 1 21  VAL 21  20  20  VAL VAL B . n 
B 1 22  ALA 22  21  21  ALA ALA B . n 
B 1 23  LYS 23  22  22  LYS LYS B . n 
B 1 24  ALA 24  23  23  ALA ALA B . n 
B 1 25  ILE 25  24  24  ILE ILE B . n 
B 1 26  THR 26  25  25  THR THR B . n 
B 1 27  ASP 27  26  26  ASP ASP B . n 
B 1 28  ALA 28  27  27  ALA ALA B . n 
B 1 29  HIS 29  28  28  HIS HIS B . n 
B 1 30  ARG 30  29  29  ARG ARG B . n 
B 1 31  GLY 31  30  30  GLY GLY B . n 
B 1 32  LEU 32  31  31  LEU LEU B . n 
B 1 33  THR 33  32  32  THR THR B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  THR 35  34  34  THR THR B . n 
B 1 36  GLN 36  35  35  GLN GLN B . n 
B 1 37  HIS 37  36  36  HIS HIS B . n 
B 1 38  PHE 38  37  37  PHE PHE B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  ALA 40  39  39  ALA ALA B . n 
B 1 41  GLN 41  40  40  GLN GLN B . n 
B 1 42  VAL 42  41  41  VAL VAL B . n 
B 1 43  ASN 43  42  42  ASN ASN B . n 
B 1 44  PHE 44  43  43  PHE PHE B . n 
B 1 45  GLN 45  44  44  GLN GLN B . n 
B 1 46  GLU 46  45  45  GLU GLU B . n 
B 1 47  GLN 47  46  46  GLN GLN B . n 
B 1 48  PRO 48  47  47  PRO PRO B . n 
B 1 49  ALA 49  48  48  ALA ALA B . n 
B 1 50  GLY 50  49  49  GLY GLY B . n 
B 1 51  ASN 51  50  50  ASN ASN B . n 
B 1 52  VAL 52  51  51  VAL VAL B . n 
B 1 53  PHE 53  52  52  PHE PHE B . n 
B 1 54  LEU 54  53  53  LEU LEU B . n 
B 1 55  GLY 55  54  54  GLY GLY B . n 
B 1 56  GLY 56  55  55  GLY GLY B . n 
B 1 57  VAL 57  56  56  VAL VAL B . n 
B 1 58  GLN 58  57  57  GLN GLN B . n 
B 1 59  GLN 59  58  58  GLN GLN B . n 
B 1 60  GLY 60  59  59  GLY GLY B . n 
B 1 61  GLY 61  60  60  GLY GLY B . n 
B 1 62  ASP 62  61  61  ASP ASP B . n 
B 1 63  THR 63  62  62  THR THR B . n 
B 1 64  ILE 64  63  63  ILE ILE B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  VAL 66  65  65  VAL VAL B . n 
B 1 67  HIS 67  66  66  HIS HIS B . n 
B 1 68  GLY 68  67  67  GLY GLY B . n 
B 1 69  LEU 69  68  68  LEU LEU B . n 
B 1 70  HIS 70  69  69  HIS HIS B . n 
B 1 71  ARG 71  70  70  ARG ARG B . n 
B 1 72  GLU 72  71  71  GLU GLU B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  ARG 74  73  73  ARG ARG B . n 
B 1 75  SER 75  74  74  SER SER B . n 
B 1 76  ALA 76  75  75  ALA ALA B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  LEU 78  77  77  LEU LEU B . n 
B 1 79  LYS 79  78  78  LYS LYS B . n 
B 1 80  GLY 80  79  79  GLY GLY B . n 
B 1 81  GLN 81  80  80  GLN GLN B . n 
B 1 82  LEU 82  81  81  LEU LEU B . n 
B 1 83  ALA 83  82  82  ALA ALA B . n 
B 1 84  GLN 84  83  83  GLN GLN B . n 
B 1 85  ARG 85  84  84  ARG ARG B . n 
B 1 86  ILE 86  85  85  ILE ILE B . n 
B 1 87  VAL 87  86  86  VAL VAL B . n 
B 1 88  ASP 88  87  87  ASP ASP B . n 
B 1 89  ASP 89  88  88  ASP ASP B . n 
B 1 90  VAL 90  89  89  VAL VAL B . n 
B 1 91  SER 91  90  90  SER SER B . n 
B 1 92  VAL 92  91  91  VAL VAL B . n 
B 1 93  ALA 93  92  92  ALA ALA B . n 
B 1 94  ALA 94  93  93  ALA ALA B . n 
B 1 95  GLU 95  94  94  GLU GLU B . n 
B 1 96  ILE 96  95  95  ILE ILE B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  ARG 98  97  97  ARG ARG B . n 
B 1 99  LYS 99  98  98  LYS LYS B . n 
B 1 100 HIS 100 99  99  HIS HIS B . n 
B 1 101 ILE 101 100 100 ILE ILE B . n 
B 1 102 TRP 102 101 101 TRP TRP B . n 
B 1 103 VAL 103 102 102 VAL VAL B . n 
B 1 104 TYR 104 103 103 TYR TYR B . n 
B 1 105 PHE 105 104 104 PHE PHE B . n 
B 1 106 GLY 106 105 105 GLY GLY B . n 
B 1 107 GLU 107 106 106 GLU GLU B . n 
B 1 108 MET 108 107 107 MET MET B . n 
B 1 109 PRO 109 108 108 PRO PRO B . n 
B 1 110 ALA 110 109 109 ALA ALA B . n 
B 1 111 GLN 111 110 110 GLN GLN B . n 
B 1 112 GLN 112 111 111 GLN GLN B . n 
B 1 113 MET 113 112 112 MET MET B . n 
B 1 114 VAL 114 113 113 VAL VAL B . n 
B 1 115 ASN 115 114 114 ASN ASN B . n 
B 1 116 TYR 116 115 115 TYR TYR B . n 
B 1 117 GLY 117 116 116 GLY GLY B . n 
B 1 118 ARG 118 117 117 ARG ARG B . n 
B 1 119 PHE 119 118 118 PHE PHE B . n 
B 1 120 LEU 120 119 119 LEU LEU B . n 
B 1 121 PRO 121 120 120 PRO PRO B . n 
B 1 122 GLN 122 121 121 GLN GLN B . n 
B 1 123 PRO 123 122 122 PRO PRO B . n 
B 1 124 GLY 124 123 123 GLY GLY B . n 
B 1 125 HIS 125 124 124 HIS ALA B . n 
B 1 126 GLU 126 125 125 GLU GLU B . n 
B 1 127 GLY 127 126 126 GLY GLY B . n 
B 1 128 GLU 128 127 127 GLU GLU B . n 
B 1 129 TRP 129 128 128 TRP TRP B . n 
B 1 130 PHE 130 129 129 PHE PHE B . n 
B 1 131 ASP 131 130 130 ASP ASP B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 LEU 133 132 132 LEU LEU B . n 
B 1 134 SER 134 133 133 SER SER B . n 
B 1 135 SER 135 134 134 SER SER B . n 
B 1 136 ASP 136 135 135 ASP ASP B . n 
B 1 137 GLU 137 136 136 GLU GLU B . n 
B 1 138 ARG 138 137 137 ARG ARG B . n 
B 1 139 ALA 139 138 138 ALA ALA B . n 
B 1 140 PHE 140 139 139 PHE PHE B . n 
B 1 141 MET 141 140 140 MET MET B . n 
B 1 142 GLU 142 141 141 GLU GLU B . n 
B 1 143 THR 143 142 142 THR THR B . n 
B 1 144 ASN 144 143 143 ASN ASN B . n 
B 1 145 VAL 145 144 144 VAL VAL B . n 
B 1 146 ASP 146 145 145 ASP ASP B . n 
B 1 147 VAL 147 146 ?   ?   ?   B . n 
B 1 148 SER 148 147 ?   ?   ?   B . n 
B 1 149 ARG 149 148 ?   ?   ?   B . n 
B 1 150 THR 150 149 ?   ?   ?   B . n 
B 1 151 GLU 151 150 ?   ?   ?   B . n 
B 1 152 ASN 152 151 ?   ?   ?   B . n 
B 1 153 LEU 153 152 ?   ?   ?   B . n 
B 1 154 TYR 154 153 ?   ?   ?   B . n 
B 1 155 PHE 155 154 ?   ?   ?   B . n 
B 1 156 GLN 156 155 ?   ?   ?   B . n 
B 1 157 GLY 157 156 ?   ?   ?   B . n 
B 1 158 LEU 158 157 ?   ?   ?   B . n 
B 1 159 GLU 159 158 ?   ?   ?   B . n 
B 1 160 HIS 160 159 ?   ?   ?   B . n 
B 1 161 HIS 161 160 ?   ?   ?   B . n 
B 1 162 HIS 162 161 ?   ?   ?   B . n 
B 1 163 HIS 163 162 ?   ?   ?   B . n 
B 1 164 HIS 164 163 ?   ?   ?   B . n 
B 1 165 HIS 165 164 ?   ?   ?   B . n 
C 1 1   MET 1   0   ?   ?   ?   C . n 
C 1 2   PRO 2   1   1   PRO PRO C . n 
C 1 3   VAL 3   2   2   VAL VAL C . n 
C 1 4   TYR 4   3   3   TYR TYR C . n 
C 1 5   MET 5   4   4   MET MET C . n 
C 1 6   VAL 6   5   5   VAL VAL C . n 
C 1 7   TYR 7   6   6   TYR TYR C . n 
C 1 8   VAL 8   7   7   VAL VAL C . n 
C 1 9   SER 9   8   8   SER SER C . n 
C 1 10  GLN 10  9   9   GLN GLN C . n 
C 1 11  ASP 11  10  10  ASP ASP C . n 
C 1 12  ARG 12  11  11  ARG ARG C . n 
C 1 13  LEU 13  12  12  LEU LEU C . n 
C 1 14  THR 14  13  13  THR THR C . n 
C 1 15  PRO 15  14  14  PRO PRO C . n 
C 1 16  SER 16  15  15  SER SER C . n 
C 1 17  ALA 17  16  16  ALA ALA C . n 
C 1 18  LYS 18  17  17  LYS LYS C . n 
C 1 19  HIS 19  18  18  HIS HIS C . n 
C 1 20  ALA 20  19  19  ALA ALA C . n 
C 1 21  VAL 21  20  20  VAL VAL C . n 
C 1 22  ALA 22  21  21  ALA ALA C . n 
C 1 23  LYS 23  22  22  LYS LYS C . n 
C 1 24  ALA 24  23  23  ALA ALA C . n 
C 1 25  ILE 25  24  24  ILE ILE C . n 
C 1 26  THR 26  25  25  THR THR C . n 
C 1 27  ASP 27  26  26  ASP ASP C . n 
C 1 28  ALA 28  27  27  ALA ALA C . n 
C 1 29  HIS 29  28  28  HIS HIS C . n 
C 1 30  ARG 30  29  29  ARG ARG C . n 
C 1 31  GLY 31  30  30  GLY GLY C . n 
C 1 32  LEU 32  31  31  LEU LEU C . n 
C 1 33  THR 33  32  32  THR THR C . n 
C 1 34  GLY 34  33  33  GLY GLY C . n 
C 1 35  THR 35  34  34  THR THR C . n 
C 1 36  GLN 36  35  35  GLN GLN C . n 
C 1 37  HIS 37  36  36  HIS HIS C . n 
C 1 38  PHE 38  37  37  PHE PHE C . n 
C 1 39  LEU 39  38  38  LEU LEU C . n 
C 1 40  ALA 40  39  39  ALA ALA C . n 
C 1 41  GLN 41  40  40  GLN GLN C . n 
C 1 42  VAL 42  41  41  VAL VAL C . n 
C 1 43  ASN 43  42  42  ASN ASN C . n 
C 1 44  PHE 44  43  43  PHE PHE C . n 
C 1 45  GLN 45  44  44  GLN GLN C . n 
C 1 46  GLU 46  45  45  GLU GLU C . n 
C 1 47  GLN 47  46  46  GLN GLN C . n 
C 1 48  PRO 48  47  47  PRO PRO C . n 
C 1 49  ALA 49  48  48  ALA ALA C . n 
C 1 50  GLY 50  49  49  GLY GLY C . n 
C 1 51  ASN 51  50  50  ASN ASN C . n 
C 1 52  VAL 52  51  51  VAL VAL C . n 
C 1 53  PHE 53  52  52  PHE PHE C . n 
C 1 54  LEU 54  53  53  LEU LEU C . n 
C 1 55  GLY 55  54  54  GLY GLY C . n 
C 1 56  GLY 56  55  55  GLY GLY C . n 
C 1 57  VAL 57  56  56  VAL VAL C . n 
C 1 58  GLN 58  57  57  GLN GLN C . n 
C 1 59  GLN 59  58  58  GLN GLN C . n 
C 1 60  GLY 60  59  59  GLY GLY C . n 
C 1 61  GLY 61  60  60  GLY GLY C . n 
C 1 62  ASP 62  61  61  ASP ASP C . n 
C 1 63  THR 63  62  62  THR THR C . n 
C 1 64  ILE 64  63  63  ILE ILE C . n 
C 1 65  PHE 65  64  64  PHE PHE C . n 
C 1 66  VAL 66  65  65  VAL VAL C . n 
C 1 67  HIS 67  66  66  HIS HIS C . n 
C 1 68  GLY 68  67  67  GLY GLY C . n 
C 1 69  LEU 69  68  68  LEU LEU C . n 
C 1 70  HIS 70  69  69  HIS HIS C . n 
C 1 71  ARG 71  70  70  ARG ARG C . n 
C 1 72  GLU 72  71  71  GLU GLU C . n 
C 1 73  GLY 73  72  72  GLY GLY C . n 
C 1 74  ARG 74  73  73  ARG ARG C . n 
C 1 75  SER 75  74  74  SER SER C . n 
C 1 76  ALA 76  75  75  ALA ALA C . n 
C 1 77  ASP 77  76  76  ASP ASP C . n 
C 1 78  LEU 78  77  77  LEU LEU C . n 
C 1 79  LYS 79  78  78  LYS LYS C . n 
C 1 80  GLY 80  79  79  GLY GLY C . n 
C 1 81  GLN 81  80  80  GLN GLN C . n 
C 1 82  LEU 82  81  81  LEU LEU C . n 
C 1 83  ALA 83  82  82  ALA ALA C . n 
C 1 84  GLN 84  83  83  GLN GLN C . n 
C 1 85  ARG 85  84  84  ARG ARG C . n 
C 1 86  ILE 86  85  85  ILE ILE C . n 
C 1 87  VAL 87  86  86  VAL VAL C . n 
C 1 88  ASP 88  87  87  ASP ASP C . n 
C 1 89  ASP 89  88  88  ASP ASP C . n 
C 1 90  VAL 90  89  89  VAL VAL C . n 
C 1 91  SER 91  90  90  SER SER C . n 
C 1 92  VAL 92  91  91  VAL VAL C . n 
C 1 93  ALA 93  92  92  ALA ALA C . n 
C 1 94  ALA 94  93  93  ALA ALA C . n 
C 1 95  GLU 95  94  94  GLU GLU C . n 
C 1 96  ILE 96  95  95  ILE ILE C . n 
C 1 97  ASP 97  96  96  ASP ASP C . n 
C 1 98  ARG 98  97  97  ARG ARG C . n 
C 1 99  LYS 99  98  98  LYS LYS C . n 
C 1 100 HIS 100 99  99  HIS HIS C . n 
C 1 101 ILE 101 100 100 ILE ILE C . n 
C 1 102 TRP 102 101 101 TRP TRP C . n 
C 1 103 VAL 103 102 102 VAL VAL C . n 
C 1 104 TYR 104 103 103 TYR TYR C . n 
C 1 105 PHE 105 104 104 PHE PHE C . n 
C 1 106 GLY 106 105 105 GLY GLY C . n 
C 1 107 GLU 107 106 106 GLU GLU C . n 
C 1 108 MET 108 107 107 MET MET C . n 
C 1 109 PRO 109 108 108 PRO PRO C . n 
C 1 110 ALA 110 109 109 ALA ALA C . n 
C 1 111 GLN 111 110 110 GLN GLN C . n 
C 1 112 GLN 112 111 111 GLN GLN C . n 
C 1 113 MET 113 112 112 MET MET C . n 
C 1 114 VAL 114 113 113 VAL VAL C . n 
C 1 115 ASN 115 114 114 ASN ASN C . n 
C 1 116 TYR 116 115 115 TYR TYR C . n 
C 1 117 GLY 117 116 116 GLY GLY C . n 
C 1 118 ARG 118 117 117 ARG ARG C . n 
C 1 119 PHE 119 118 118 PHE PHE C . n 
C 1 120 LEU 120 119 119 LEU LEU C . n 
C 1 121 PRO 121 120 120 PRO PRO C . n 
C 1 122 GLN 122 121 121 GLN GLN C . n 
C 1 123 PRO 123 122 122 PRO PRO C . n 
C 1 124 GLY 124 123 123 GLY GLY C . n 
C 1 125 HIS 125 124 124 HIS HIS C . n 
C 1 126 GLU 126 125 125 GLU GLU C . n 
C 1 127 GLY 127 126 126 GLY GLY C . n 
C 1 128 GLU 128 127 127 GLU GLU C . n 
C 1 129 TRP 129 128 128 TRP TRP C . n 
C 1 130 PHE 130 129 129 PHE PHE C . n 
C 1 131 ASP 131 130 130 ASP ASP C . n 
C 1 132 ASN 132 131 131 ASN ASN C . n 
C 1 133 LEU 133 132 132 LEU LEU C . n 
C 1 134 SER 134 133 133 SER SER C . n 
C 1 135 SER 135 134 134 SER SER C . n 
C 1 136 ASP 136 135 135 ASP ASP C . n 
C 1 137 GLU 137 136 136 GLU GLU C . n 
C 1 138 ARG 138 137 137 ARG ARG C . n 
C 1 139 ALA 139 138 138 ALA ALA C . n 
C 1 140 PHE 140 139 139 PHE PHE C . n 
C 1 141 MET 141 140 140 MET MET C . n 
C 1 142 GLU 142 141 141 GLU GLU C . n 
C 1 143 THR 143 142 142 THR THR C . n 
C 1 144 ASN 144 143 143 ASN ASN C . n 
C 1 145 VAL 145 144 144 VAL VAL C . n 
C 1 146 ASP 146 145 145 ASP ASP C . n 
C 1 147 VAL 147 146 ?   ?   ?   C . n 
C 1 148 SER 148 147 ?   ?   ?   C . n 
C 1 149 ARG 149 148 ?   ?   ?   C . n 
C 1 150 THR 150 149 ?   ?   ?   C . n 
C 1 151 GLU 151 150 ?   ?   ?   C . n 
C 1 152 ASN 152 151 ?   ?   ?   C . n 
C 1 153 LEU 153 152 ?   ?   ?   C . n 
C 1 154 TYR 154 153 ?   ?   ?   C . n 
C 1 155 PHE 155 154 ?   ?   ?   C . n 
C 1 156 GLN 156 155 ?   ?   ?   C . n 
C 1 157 GLY 157 156 ?   ?   ?   C . n 
C 1 158 LEU 158 157 ?   ?   ?   C . n 
C 1 159 GLU 159 158 ?   ?   ?   C . n 
C 1 160 HIS 160 159 ?   ?   ?   C . n 
C 1 161 HIS 161 160 ?   ?   ?   C . n 
C 1 162 HIS 162 161 ?   ?   ?   C . n 
C 1 163 HIS 163 162 ?   ?   ?   C . n 
C 1 164 HIS 164 163 ?   ?   ?   C . n 
C 1 165 HIS 165 164 ?   ?   ?   C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4 1  201 1  SO4 SO4 A . 
E 2 SO4 1  201 2  SO4 SO4 B . 
F 2 SO4 1  201 3  SO4 SO4 C . 
G 3 HOH 1  301 22 HOH HOH A . 
G 3 HOH 2  302 28 HOH HOH A . 
G 3 HOH 3  303 20 HOH HOH A . 
G 3 HOH 4  304 25 HOH HOH A . 
G 3 HOH 5  305 41 HOH HOH A . 
G 3 HOH 6  306 46 HOH HOH A . 
G 3 HOH 7  307 21 HOH HOH A . 
G 3 HOH 8  308 14 HOH HOH A . 
G 3 HOH 9  309 19 HOH HOH A . 
G 3 HOH 10 310 18 HOH HOH A . 
G 3 HOH 11 311 17 HOH HOH A . 
G 3 HOH 12 312 54 HOH HOH A . 
G 3 HOH 13 313 9  HOH HOH A . 
G 3 HOH 14 314 37 HOH HOH A . 
G 3 HOH 15 315 35 HOH HOH A . 
G 3 HOH 16 316 49 HOH HOH A . 
G 3 HOH 17 317 7  HOH HOH A . 
G 3 HOH 18 318 32 HOH HOH A . 
G 3 HOH 19 319 23 HOH HOH A . 
H 3 HOH 1  301 31 HOH HOH B . 
H 3 HOH 2  302 42 HOH HOH B . 
H 3 HOH 3  303 39 HOH HOH B . 
H 3 HOH 4  304 2  HOH HOH B . 
H 3 HOH 5  305 11 HOH HOH B . 
H 3 HOH 6  306 12 HOH HOH B . 
H 3 HOH 7  307 24 HOH HOH B . 
H 3 HOH 8  308 34 HOH HOH B . 
H 3 HOH 9  309 44 HOH HOH B . 
H 3 HOH 10 310 5  HOH HOH B . 
H 3 HOH 11 311 6  HOH HOH B . 
H 3 HOH 12 312 1  HOH HOH B . 
H 3 HOH 13 313 47 HOH HOH B . 
H 3 HOH 14 314 33 HOH HOH B . 
H 3 HOH 15 315 52 HOH HOH B . 
H 3 HOH 16 316 53 HOH HOH B . 
H 3 HOH 17 317 26 HOH HOH B . 
H 3 HOH 18 318 45 HOH HOH B . 
H 3 HOH 19 319 27 HOH HOH B . 
H 3 HOH 20 320 29 HOH HOH B . 
H 3 HOH 21 321 50 HOH HOH B . 
I 3 HOH 1  301 40 HOH HOH C . 
I 3 HOH 2  302 3  HOH HOH C . 
I 3 HOH 3  303 51 HOH HOH C . 
I 3 HOH 4  304 15 HOH HOH C . 
I 3 HOH 5  305 13 HOH HOH C . 
I 3 HOH 6  306 10 HOH HOH C . 
I 3 HOH 7  307 56 HOH HOH C . 
I 3 HOH 8  308 16 HOH HOH C . 
I 3 HOH 9  309 30 HOH HOH C . 
I 3 HOH 10 310 57 HOH HOH C . 
I 3 HOH 11 311 8  HOH HOH C . 
I 3 HOH 12 312 4  HOH HOH C . 
I 3 HOH 13 313 55 HOH HOH C . 
I 3 HOH 14 314 36 HOH HOH C . 
I 3 HOH 15 315 43 HOH HOH C . 
I 3 HOH 16 316 48 HOH HOH C . 
I 3 HOH 17 317 38 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B HIS 124 ? CG  ? B HIS 125 CG  
2 1 Y 1 B HIS 124 ? ND1 ? B HIS 125 ND1 
3 1 Y 1 B HIS 124 ? CD2 ? B HIS 125 CD2 
4 1 Y 1 B HIS 124 ? CE1 ? B HIS 125 CE1 
5 1 Y 1 B HIS 124 ? NE2 ? B HIS 125 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.2_5419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NF9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.222 
_cell.length_a_esd                 ? 
_cell.length_b                     99.020 
_cell.length_b_esd                 ? 
_cell.length_c                     137.557 
_cell.length_c_esd                 ? 
_cell.volume                       793035.699 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9NF9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9NF9 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.77 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          30.64 
_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, HANGING 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    '(0.03 M citric acid, 0.07 M BIS-TRIS propane) pH 7.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-09 
_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   1.13 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.13 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          38.60 
_reflns.entry_id                                       9NF9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.50 
_reflns.d_resolution_low                               50.00 
_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                                     13174 
_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                           94.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.53 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.061 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_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                                    2.50 
_reflns_shell.d_res_low                                     2.54 
_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                             664 
_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                               0.318 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_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                               38.17 
_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                                 9NF9 
_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                            2.51 
_refine.ls_d_res_low                             28.71 
_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                     12430 
_refine.ls_number_reflns_R_free                  1265 
_refine.ls_number_reflns_R_work                  11165 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    89.21 
_refine.ls_percent_reflns_R_free                 10.18 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2227 
_refine.ls_R_factor_R_free                       0.2901 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2150 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.6340 
_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                            0.3860 
_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                       2.51 
_refine_hist.d_res_low                        28.71 
_refine_hist.number_atoms_solvent             57 
_refine_hist.number_atoms_total               3490 
_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        3418 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         15 
_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' ? 0.0140  ? 3513 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.6660  ? 4759 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0796  ? 495  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0157  ? 638  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 20.3256 ? 1258 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.51 2.61  . . 119 992  72.33 . . . . 0.2451 . . . . . . . . . . . . . . . 0.3444 
'X-RAY DIFFRACTION' 2.61 2.73  . . 127 1177 86.47 . . . . 0.2721 . . . . . . . . . . . . . . . 0.4569 
'X-RAY DIFFRACTION' 2.73 2.88  . . 154 1357 98.37 . . . . 0.2414 . . . . . . . . . . . . . . . 0.3586 
'X-RAY DIFFRACTION' 2.88 3.06  . . 152 1328 97.30 . . . . 0.2368 . . . . . . . . . . . . . . . 0.3241 
'X-RAY DIFFRACTION' 3.06 3.29  . . 145 1274 93.73 . . . . 0.2283 . . . . . . . . . . . . . . . 0.3118 
'X-RAY DIFFRACTION' 3.29 3.62  . . 125 1110 79.37 . . . . 0.2286 . . . . . . . . . . . . . . . 0.3036 
'X-RAY DIFFRACTION' 3.62 4.14  . . 133 1128 80.73 . . . . 0.2180 . . . . . . . . . . . . . . . 0.3210 
'X-RAY DIFFRACTION' 4.14 5.21  . . 151 1367 97.56 . . . . 0.1769 . . . . . . . . . . . . . . . 0.2271 
'X-RAY DIFFRACTION' 5.22 28.71 . . 159 1432 96.78 . . . . 0.1998 . . . . . . . . . . . . . . . 0.2346 
# 
_struct.entry_id                     9NF9 
_struct.title                        'cis-CaaD E114N mutant apo' 
_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        9NF9 
_struct_keywords.text            'Tautomerase, cis-CaaD, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q6VPE5_9CORY 
_struct_ref.pdbx_db_accession          Q6VPE5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKG
QLAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVEYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRT
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9NF9 A 1 ? 150 ? Q6VPE5 1 ? 150 ? 0 149 
2 1 9NF9 B 1 ? 150 ? Q6VPE5 1 ? 150 ? 0 149 
3 1 9NF9 C 1 ? 150 ? Q6VPE5 1 ? 150 ? 0 149 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9NF9 ASN A 115 ? UNP Q6VPE5 GLU 115 'engineered mutation' 114 1  
1 9NF9 GLU A 151 ? UNP Q6VPE5 ?   ?   'expression tag'      150 2  
1 9NF9 ASN A 152 ? UNP Q6VPE5 ?   ?   'expression tag'      151 3  
1 9NF9 LEU A 153 ? UNP Q6VPE5 ?   ?   'expression tag'      152 4  
1 9NF9 TYR A 154 ? UNP Q6VPE5 ?   ?   'expression tag'      153 5  
1 9NF9 PHE A 155 ? UNP Q6VPE5 ?   ?   'expression tag'      154 6  
1 9NF9 GLN A 156 ? UNP Q6VPE5 ?   ?   'expression tag'      155 7  
1 9NF9 GLY A 157 ? UNP Q6VPE5 ?   ?   'expression tag'      156 8  
1 9NF9 LEU A 158 ? UNP Q6VPE5 ?   ?   'expression tag'      157 9  
1 9NF9 GLU A 159 ? UNP Q6VPE5 ?   ?   'expression tag'      158 10 
1 9NF9 HIS A 160 ? UNP Q6VPE5 ?   ?   'expression tag'      159 11 
1 9NF9 HIS A 161 ? UNP Q6VPE5 ?   ?   'expression tag'      160 12 
1 9NF9 HIS A 162 ? UNP Q6VPE5 ?   ?   'expression tag'      161 13 
1 9NF9 HIS A 163 ? UNP Q6VPE5 ?   ?   'expression tag'      162 14 
1 9NF9 HIS A 164 ? UNP Q6VPE5 ?   ?   'expression tag'      163 15 
1 9NF9 HIS A 165 ? UNP Q6VPE5 ?   ?   'expression tag'      164 16 
2 9NF9 ASN B 115 ? UNP Q6VPE5 GLU 115 'engineered mutation' 114 17 
2 9NF9 GLU B 151 ? UNP Q6VPE5 ?   ?   'expression tag'      150 18 
2 9NF9 ASN B 152 ? UNP Q6VPE5 ?   ?   'expression tag'      151 19 
2 9NF9 LEU B 153 ? UNP Q6VPE5 ?   ?   'expression tag'      152 20 
2 9NF9 TYR B 154 ? UNP Q6VPE5 ?   ?   'expression tag'      153 21 
2 9NF9 PHE B 155 ? UNP Q6VPE5 ?   ?   'expression tag'      154 22 
2 9NF9 GLN B 156 ? UNP Q6VPE5 ?   ?   'expression tag'      155 23 
2 9NF9 GLY B 157 ? UNP Q6VPE5 ?   ?   'expression tag'      156 24 
2 9NF9 LEU B 158 ? UNP Q6VPE5 ?   ?   'expression tag'      157 25 
2 9NF9 GLU B 159 ? UNP Q6VPE5 ?   ?   'expression tag'      158 26 
2 9NF9 HIS B 160 ? UNP Q6VPE5 ?   ?   'expression tag'      159 27 
2 9NF9 HIS B 161 ? UNP Q6VPE5 ?   ?   'expression tag'      160 28 
2 9NF9 HIS B 162 ? UNP Q6VPE5 ?   ?   'expression tag'      161 29 
2 9NF9 HIS B 163 ? UNP Q6VPE5 ?   ?   'expression tag'      162 30 
2 9NF9 HIS B 164 ? UNP Q6VPE5 ?   ?   'expression tag'      163 31 
2 9NF9 HIS B 165 ? UNP Q6VPE5 ?   ?   'expression tag'      164 32 
3 9NF9 ASN C 115 ? UNP Q6VPE5 GLU 115 'engineered mutation' 114 33 
3 9NF9 GLU C 151 ? UNP Q6VPE5 ?   ?   'expression tag'      150 34 
3 9NF9 ASN C 152 ? UNP Q6VPE5 ?   ?   'expression tag'      151 35 
3 9NF9 LEU C 153 ? UNP Q6VPE5 ?   ?   'expression tag'      152 36 
3 9NF9 TYR C 154 ? UNP Q6VPE5 ?   ?   'expression tag'      153 37 
3 9NF9 PHE C 155 ? UNP Q6VPE5 ?   ?   'expression tag'      154 38 
3 9NF9 GLN C 156 ? UNP Q6VPE5 ?   ?   'expression tag'      155 39 
3 9NF9 GLY C 157 ? UNP Q6VPE5 ?   ?   'expression tag'      156 40 
3 9NF9 LEU C 158 ? UNP Q6VPE5 ?   ?   'expression tag'      157 41 
3 9NF9 GLU C 159 ? UNP Q6VPE5 ?   ?   'expression tag'      158 42 
3 9NF9 HIS C 160 ? UNP Q6VPE5 ?   ?   'expression tag'      159 43 
3 9NF9 HIS C 161 ? UNP Q6VPE5 ?   ?   'expression tag'      160 44 
3 9NF9 HIS C 162 ? UNP Q6VPE5 ?   ?   'expression tag'      161 45 
3 9NF9 HIS C 163 ? UNP Q6VPE5 ?   ?   'expression tag'      162 46 
3 9NF9 HIS C 164 ? UNP Q6VPE5 ?   ?   'expression tag'      163 47 
3 9NF9 HIS C 165 ? UNP Q6VPE5 ?   ?   'expression tag'      164 48 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9070  ? 
1 MORE         -104  ? 
1 'SSA (A^2)'  15050 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 14  ? GLY A 34  ? THR A 13  GLY A 33  1 ? 21 
HELX_P HELX_P2  AA2 GLN A 36  ? LEU A 39  ? GLN A 35  LEU A 38  5 ? 4  
HELX_P HELX_P3  AA3 SER A 75  ? ALA A 94  ? SER A 74  ALA A 93  1 ? 20 
HELX_P HELX_P4  AA4 ASP A 97  ? LYS A 99  ? ASP A 96  LYS A 98  5 ? 3  
HELX_P HELX_P5  AA5 PRO A 109 ? GLN A 111 ? PRO A 108 GLN A 110 5 ? 3  
HELX_P HELX_P6  AA6 HIS A 125 ? ASN A 132 ? HIS A 124 ASN A 131 1 ? 8  
HELX_P HELX_P7  AA7 SER A 134 ? ASN A 144 ? SER A 133 ASN A 143 1 ? 11 
HELX_P HELX_P8  AA8 THR B 14  ? GLY B 34  ? THR B 13  GLY B 33  1 ? 21 
HELX_P HELX_P9  AA9 GLN B 36  ? LEU B 39  ? GLN B 35  LEU B 38  5 ? 4  
HELX_P HELX_P10 AB1 SER B 75  ? GLU B 95  ? SER B 74  GLU B 94  1 ? 21 
HELX_P HELX_P11 AB2 ASP B 97  ? LYS B 99  ? ASP B 96  LYS B 98  5 ? 3  
HELX_P HELX_P12 AB3 PRO B 109 ? GLN B 111 ? PRO B 108 GLN B 110 5 ? 3  
HELX_P HELX_P13 AB4 GLU B 137 ? ASN B 144 ? GLU B 136 ASN B 143 1 ? 8  
HELX_P HELX_P14 AB5 THR C 14  ? GLY C 34  ? THR C 13  GLY C 33  1 ? 21 
HELX_P HELX_P15 AB6 GLN C 36  ? LEU C 39  ? GLN C 35  LEU C 38  5 ? 4  
HELX_P HELX_P16 AB7 SER C 75  ? GLU C 95  ? SER C 74  GLU C 94  1 ? 21 
HELX_P HELX_P17 AB8 ASP C 97  ? LYS C 99  ? ASP C 96  LYS C 98  5 ? 3  
HELX_P HELX_P18 AB9 PRO C 109 ? GLN C 111 ? PRO C 108 GLN C 110 5 ? 3  
HELX_P HELX_P19 AC1 HIS C 125 ? ASN C 132 ? HIS C 124 ASN C 131 1 ? 8  
HELX_P HELX_P20 AC2 SER C 134 ? ASN C 144 ? SER C 133 ASN C 143 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
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 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? parallel      
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG B 118 ? PHE B 119 ? ARG B 117 PHE B 118 
AA1 2 MET B 113 ? ASN B 115 ? MET B 112 ASN B 114 
AA1 3 ILE A 101 ? MET A 108 ? ILE A 100 MET A 107 
AA1 4 ILE A 64  ? ARG A 71  ? ILE A 63  ARG A 70  
AA1 5 VAL A 3   ? SER A 9   ? VAL A 2   SER A 8   
AA1 6 GLN A 41  ? GLN A 47  ? GLN A 40  GLN A 46  
AA1 7 VAL C 52  ? LEU C 54  ? VAL C 51  LEU C 53  
AA1 8 VAL C 57  ? GLN C 58  ? VAL C 56  GLN C 57  
AA2 1 VAL A 57  ? GLN A 58  ? VAL A 56  GLN A 57  
AA2 2 VAL A 52  ? LEU A 54  ? VAL A 51  LEU A 53  
AA2 3 GLN B 41  ? GLN B 47  ? GLN B 40  GLN B 46  
AA2 4 VAL B 3   ? SER B 9   ? VAL B 2   SER B 8   
AA2 5 ILE B 64  ? ARG B 71  ? ILE B 63  ARG B 70  
AA2 6 ILE B 101 ? MET B 108 ? ILE B 100 MET B 107 
AA2 7 MET C 113 ? ASN C 115 ? MET C 112 ASN C 114 
AA2 8 ARG C 118 ? PHE C 119 ? ARG C 117 PHE C 118 
AA3 1 ARG A 118 ? PHE A 119 ? ARG A 117 PHE A 118 
AA3 2 MET A 113 ? ASN A 115 ? MET A 112 ASN A 114 
AA3 3 ILE C 101 ? MET C 108 ? ILE C 100 MET C 107 
AA3 4 ILE C 64  ? ARG C 71  ? ILE C 63  ARG C 70  
AA3 5 VAL C 3   ? SER C 9   ? VAL C 2   SER C 8   
AA3 6 GLN C 41  ? GLN C 47  ? GLN C 40  GLN C 46  
AA3 7 VAL B 52  ? LEU B 54  ? VAL B 51  LEU B 53  
AA3 8 VAL B 57  ? GLN B 58  ? VAL B 56  GLN B 57  
# 
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 O ARG B 118 ? O ARG B 117 N ASN B 115 ? N ASN B 114 
AA1 2 3 O VAL B 114 ? O VAL B 113 N VAL A 103 ? N VAL A 102 
AA1 3 4 O GLY A 106 ? O GLY A 105 N GLY A 68  ? N GLY A 67  
AA1 4 5 O PHE A 65  ? O PHE A 64  N TYR A 7   ? N TYR A 6   
AA1 5 6 N TYR A 4   ? N TYR A 3   O ASN A 43  ? O ASN A 42  
AA1 6 7 N VAL A 42  ? N VAL A 41  O PHE C 53  ? O PHE C 52  
AA1 7 8 N LEU C 54  ? N LEU C 53  O VAL C 57  ? O VAL C 56  
AA2 1 2 O VAL A 57  ? O VAL A 56  N LEU A 54  ? N LEU A 53  
AA2 2 3 N PHE A 53  ? N PHE A 52  O VAL B 42  ? O VAL B 41  
AA2 3 4 O ASN B 43  ? O ASN B 42  N TYR B 4   ? N TYR B 3   
AA2 4 5 N VAL B 3   ? N VAL B 2   O LEU B 69  ? O LEU B 68  
AA2 5 6 N GLY B 68  ? N GLY B 67  O TYR B 104 ? O TYR B 103 
AA2 6 7 N VAL B 103 ? N VAL B 102 O VAL C 114 ? O VAL C 113 
AA2 7 8 N ASN C 115 ? N ASN C 114 O ARG C 118 ? O ARG C 117 
AA3 1 2 O ARG A 118 ? O ARG A 117 N ASN A 115 ? N ASN A 114 
AA3 2 3 N VAL A 114 ? N VAL A 113 O VAL C 103 ? O VAL C 102 
AA3 3 4 O GLY C 106 ? O GLY C 105 N HIS C 70  ? N HIS C 69  
AA3 4 5 O PHE C 65  ? O PHE C 64  N TYR C 7   ? N TYR C 6   
AA3 5 6 N VAL C 6   ? N VAL C 5   O GLN C 45  ? O GLN C 44  
AA3 6 7 O VAL C 42  ? O VAL C 41  N PHE B 53  ? N PHE B 52  
AA3 7 8 N LEU B 54  ? N LEU B 53  O VAL B 57  ? O VAL B 56  
# 
_pdbx_entry_details.entry_id                   9NF9 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 NE2 C HIS 28  ? ? O4  C SO4 201 ? ? 1.82 
2  1 CB  B PRO 1   ? ? O4  B SO4 201 ? ? 1.90 
3  1 O   C GLU 125 ? ? O   C HOH 301 ? ? 1.93 
4  1 O   B HOH 301 ? ? O   B HOH 316 ? ? 1.96 
5  1 NE2 B GLN 58  ? ? O   B HOH 301 ? ? 1.97 
6  1 OE1 B GLU 127 ? ? O   B HOH 302 ? ? 2.02 
7  1 O   B LYS 98  ? ? O   B HOH 303 ? ? 2.03 
8  1 O   B GLY 126 ? ? O   B HOH 304 ? ? 2.06 
9  1 O   A GLY 123 ? ? O   A HOH 301 ? ? 2.09 
10 1 O   B ASP 10  ? ? O   B HOH 305 ? ? 2.14 
11 1 O   C PHE 139 ? ? OG1 C THR 142 ? ? 2.14 
12 1 OE2 A GLU 127 ? ? O   A HOH 302 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OG1 B THR 13  ? ? 1_555 OE1 B GLU 94  ? ? 4_565 1.92 
2 1 O   B HOH 318 ? ? 1_555 O   C HOH 316 ? ? 3_554 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            B 
_pdbx_validate_rmsd_bond.auth_comp_id_1            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             22 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CE 
_pdbx_validate_rmsd_bond.auth_asym_id_2            B 
_pdbx_validate_rmsd_bond.auth_comp_id_2            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             22 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.713 
_pdbx_validate_rmsd_bond.bond_target_value         1.508 
_pdbx_validate_rmsd_bond.bond_deviation            0.205 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.025 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA B GLN 121 ? ? CB B GLN 121 ? ? CG  B GLN 121 ? ? 96.43  113.40 -16.97 2.20 N 
2 1 CB B GLN 121 ? ? CG B GLN 121 ? ? CD  B GLN 121 ? ? 129.32 111.60 17.72  2.60 N 
3 1 C  B ASP 135 ? ? N  B GLU 136 ? ? CA  B GLU 136 ? ? 140.52 121.70 18.82  2.50 Y 
4 1 CG B GLU 136 ? ? CD B GLU 136 ? ? OE2 B GLU 136 ? ? 104.44 118.30 -13.86 2.00 N 
5 1 CA C LYS 22  ? ? CB C LYS 22  ? ? CG  C LYS 22  ? ? 132.01 113.40 18.61  2.20 N 
6 1 CG C LYS 22  ? ? CD C LYS 22  ? ? CE  C LYS 22  ? ? 140.02 111.90 28.12  3.00 N 
7 1 CD C LYS 22  ? ? CE C LYS 22  ? ? NZ  C LYS 22  ? ? 136.37 111.70 24.67  2.30 N 
8 1 NE C ARG 70  ? ? CZ C ARG 70  ? ? NH2 C ARG 70  ? ? 115.15 120.30 -5.15  0.50 N 
9 1 CB C ASN 114 ? ? CA C ASN 114 ? ? C   C ASN 114 ? ? 122.55 110.40 12.15  2.00 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 HIS A 124 ? ? 175.82  -13.43  
2 1 GLU B 125 ? ? 128.45  -20.50  
3 1 PHE B 129 ? ? -59.81  76.48   
4 1 ASP B 130 ? ? -135.50 -84.67  
5 1 ASN B 131 ? ? 93.35   -142.02 
6 1 SER B 133 ? ? -37.48  161.07  
7 1 SER B 134 ? ? 98.19   -97.86  
8 1 HIS C 36  ? ? 5.68    -75.02  
9 1 HIS C 124 ? ? 98.25   86.75   
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 ASP B 130 ? ? ASN B 131 ? ? 148.68 
2 1 VAL B 144 ? ? ASP B 145 ? ? 148.52 
3 1 GLN C 35  ? ? HIS C 36  ? ? 136.37 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 GLU B 136 ? ? 0.084 'SIDE CHAIN' 
2 1 ARG C 29  ? ? 0.121 'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 0   ? A MET 1   
2  1 Y 1 A VAL 146 ? A VAL 147 
3  1 Y 1 A SER 147 ? A SER 148 
4  1 Y 1 A ARG 148 ? A ARG 149 
5  1 Y 1 A THR 149 ? A THR 150 
6  1 Y 1 A GLU 150 ? A GLU 151 
7  1 Y 1 A ASN 151 ? A ASN 152 
8  1 Y 1 A LEU 152 ? A LEU 153 
9  1 Y 1 A TYR 153 ? A TYR 154 
10 1 Y 1 A PHE 154 ? A PHE 155 
11 1 Y 1 A GLN 155 ? A GLN 156 
12 1 Y 1 A GLY 156 ? A GLY 157 
13 1 Y 1 A LEU 157 ? A LEU 158 
14 1 Y 1 A GLU 158 ? A GLU 159 
15 1 Y 1 A HIS 159 ? A HIS 160 
16 1 Y 1 A HIS 160 ? A HIS 161 
17 1 Y 1 A HIS 161 ? A HIS 162 
18 1 Y 1 A HIS 162 ? A HIS 163 
19 1 Y 1 A HIS 163 ? A HIS 164 
20 1 Y 1 A HIS 164 ? A HIS 165 
21 1 Y 1 B MET 0   ? B MET 1   
22 1 Y 1 B VAL 146 ? B VAL 147 
23 1 Y 1 B SER 147 ? B SER 148 
24 1 Y 1 B ARG 148 ? B ARG 149 
25 1 Y 1 B THR 149 ? B THR 150 
26 1 Y 1 B GLU 150 ? B GLU 151 
27 1 Y 1 B ASN 151 ? B ASN 152 
28 1 Y 1 B LEU 152 ? B LEU 153 
29 1 Y 1 B TYR 153 ? B TYR 154 
30 1 Y 1 B PHE 154 ? B PHE 155 
31 1 Y 1 B GLN 155 ? B GLN 156 
32 1 Y 1 B GLY 156 ? B GLY 157 
33 1 Y 1 B LEU 157 ? B LEU 158 
34 1 Y 1 B GLU 158 ? B GLU 159 
35 1 Y 1 B HIS 159 ? B HIS 160 
36 1 Y 1 B HIS 160 ? B HIS 161 
37 1 Y 1 B HIS 161 ? B HIS 162 
38 1 Y 1 B HIS 162 ? B HIS 163 
39 1 Y 1 B HIS 163 ? B HIS 164 
40 1 Y 1 B HIS 164 ? B HIS 165 
41 1 Y 1 C MET 0   ? C MET 1   
42 1 Y 1 C VAL 146 ? C VAL 147 
43 1 Y 1 C SER 147 ? C SER 148 
44 1 Y 1 C ARG 148 ? C ARG 149 
45 1 Y 1 C THR 149 ? C THR 150 
46 1 Y 1 C GLU 150 ? C GLU 151 
47 1 Y 1 C ASN 151 ? C ASN 152 
48 1 Y 1 C LEU 152 ? C LEU 153 
49 1 Y 1 C TYR 153 ? C TYR 154 
50 1 Y 1 C PHE 154 ? C PHE 155 
51 1 Y 1 C GLN 155 ? C GLN 156 
52 1 Y 1 C GLY 156 ? C GLY 157 
53 1 Y 1 C LEU 157 ? C LEU 158 
54 1 Y 1 C GLU 158 ? C GLU 159 
55 1 Y 1 C HIS 159 ? C HIS 160 
56 1 Y 1 C HIS 160 ? C HIS 161 
57 1 Y 1 C HIS 161 ? C HIS 162 
58 1 Y 1 C HIS 162 ? C HIS 163 
59 1 Y 1 C HIS 163 ? C HIS 164 
60 1 Y 1 C HIS 164 ? C HIS 165 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
SO4 S    S N N 290 
SO4 O1   O N N 291 
SO4 O2   O N N 292 
SO4 O3   O N N 293 
SO4 O4   O N N 294 
THR N    N N N 295 
THR CA   C N S 296 
THR C    C N N 297 
THR O    O N N 298 
THR CB   C N R 299 
THR OG1  O N N 300 
THR CG2  C N N 301 
THR OXT  O N N 302 
THR H    H N N 303 
THR H2   H N N 304 
THR HA   H N N 305 
THR HB   H N N 306 
THR HG1  H N N 307 
THR HG21 H N N 308 
THR HG22 H N N 309 
THR HG23 H N N 310 
THR HXT  H N N 311 
TRP N    N N N 312 
TRP CA   C N S 313 
TRP C    C N N 314 
TRP O    O N N 315 
TRP CB   C N N 316 
TRP CG   C Y N 317 
TRP CD1  C Y N 318 
TRP CD2  C Y N 319 
TRP NE1  N Y N 320 
TRP CE2  C Y N 321 
TRP CE3  C Y N 322 
TRP CZ2  C Y N 323 
TRP CZ3  C Y N 324 
TRP CH2  C Y N 325 
TRP OXT  O N N 326 
TRP H    H N N 327 
TRP H2   H N N 328 
TRP HA   H N N 329 
TRP HB2  H N N 330 
TRP HB3  H N N 331 
TRP HD1  H N N 332 
TRP HE1  H N N 333 
TRP HE3  H N N 334 
TRP HZ2  H N N 335 
TRP HZ3  H N N 336 
TRP HH2  H N N 337 
TRP HXT  H N N 338 
TYR N    N N N 339 
TYR CA   C N S 340 
TYR C    C N N 341 
TYR O    O N N 342 
TYR CB   C N N 343 
TYR CG   C Y N 344 
TYR CD1  C Y N 345 
TYR CD2  C Y N 346 
TYR CE1  C Y N 347 
TYR CE2  C Y N 348 
TYR CZ   C Y N 349 
TYR OH   O N N 350 
TYR OXT  O N N 351 
TYR H    H N N 352 
TYR H2   H N N 353 
TYR HA   H N N 354 
TYR HB2  H N N 355 
TYR HB3  H N N 356 
TYR HD1  H N N 357 
TYR HD2  H N N 358 
TYR HE1  H N N 359 
TYR HE2  H N N 360 
TYR HH   H N N 361 
TYR HXT  H N N 362 
VAL N    N N N 363 
VAL CA   C N S 364 
VAL C    C N N 365 
VAL O    O N N 366 
VAL CB   C N N 367 
VAL CG1  C N N 368 
VAL CG2  C N N 369 
VAL OXT  O N N 370 
VAL H    H N N 371 
VAL H2   H N N 372 
VAL HA   H N N 373 
VAL HB   H N N 374 
VAL HG11 H N N 375 
VAL HG12 H N N 376 
VAL HG13 H N N 377 
VAL HG21 H N N 378 
VAL HG22 H N N 379 
VAL HG23 H N N 380 
VAL HXT  H N N 381 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
SO4 S   O1   doub N N 277 
SO4 S   O2   doub N N 278 
SO4 S   O3   sing N N 279 
SO4 S   O4   sing N N 280 
THR N   CA   sing N N 281 
THR N   H    sing N N 282 
THR N   H2   sing N N 283 
THR CA  C    sing N N 284 
THR CA  CB   sing N N 285 
THR CA  HA   sing N N 286 
THR C   O    doub N N 287 
THR C   OXT  sing N N 288 
THR CB  OG1  sing N N 289 
THR CB  CG2  sing N N 290 
THR CB  HB   sing N N 291 
THR OG1 HG1  sing N N 292 
THR CG2 HG21 sing N N 293 
THR CG2 HG22 sing N N 294 
THR CG2 HG23 sing N N 295 
THR OXT HXT  sing N N 296 
TRP N   CA   sing N N 297 
TRP N   H    sing N N 298 
TRP N   H2   sing N N 299 
TRP CA  C    sing N N 300 
TRP CA  CB   sing N N 301 
TRP CA  HA   sing N N 302 
TRP C   O    doub N N 303 
TRP C   OXT  sing N N 304 
TRP CB  CG   sing N N 305 
TRP CB  HB2  sing N N 306 
TRP CB  HB3  sing N N 307 
TRP CG  CD1  doub Y N 308 
TRP CG  CD2  sing Y N 309 
TRP CD1 NE1  sing Y N 310 
TRP CD1 HD1  sing N N 311 
TRP CD2 CE2  doub Y N 312 
TRP CD2 CE3  sing Y N 313 
TRP NE1 CE2  sing Y N 314 
TRP NE1 HE1  sing N N 315 
TRP CE2 CZ2  sing Y N 316 
TRP CE3 CZ3  doub Y N 317 
TRP CE3 HE3  sing N N 318 
TRP CZ2 CH2  doub Y N 319 
TRP CZ2 HZ2  sing N N 320 
TRP CZ3 CH2  sing Y N 321 
TRP CZ3 HZ3  sing N N 322 
TRP CH2 HH2  sing N N 323 
TRP OXT HXT  sing N N 324 
TYR N   CA   sing N N 325 
TYR N   H    sing N N 326 
TYR N   H2   sing N N 327 
TYR CA  C    sing N N 328 
TYR CA  CB   sing N N 329 
TYR CA  HA   sing N N 330 
TYR C   O    doub N N 331 
TYR C   OXT  sing N N 332 
TYR CB  CG   sing N N 333 
TYR CB  HB2  sing N N 334 
TYR CB  HB3  sing N N 335 
TYR CG  CD1  doub Y N 336 
TYR CG  CD2  sing Y N 337 
TYR CD1 CE1  sing Y N 338 
TYR CD1 HD1  sing N N 339 
TYR CD2 CE2  doub Y N 340 
TYR CD2 HD2  sing N N 341 
TYR CE1 CZ   doub Y N 342 
TYR CE1 HE1  sing N N 343 
TYR CE2 CZ   sing Y N 344 
TYR CE2 HE2  sing N N 345 
TYR CZ  OH   sing N N 346 
TYR OH  HH   sing N N 347 
TYR OXT HXT  sing N N 348 
VAL N   CA   sing N N 349 
VAL N   H    sing N N 350 
VAL N   H2   sing N N 351 
VAL CA  C    sing N N 352 
VAL CA  CB   sing N N 353 
VAL CA  HA   sing N N 354 
VAL C   O    doub N N 355 
VAL C   OXT  sing N N 356 
VAL CB  CG1  sing N N 357 
VAL CB  CG2  sing N N 358 
VAL CB  HB   sing N N 359 
VAL CG1 HG11 sing N N 360 
VAL CG1 HG12 sing N N 361 
VAL CG1 HG13 sing N N 362 
VAL CG2 HG21 sing N N 363 
VAL CG2 HG22 sing N N 364 
VAL CG2 HG23 sing N N 365 
VAL OXT HXT  sing N N 366 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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   3MF8 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9NF9 
_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]   0.017176 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010099 
_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]   0.007270 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . PRO A 1 2   ? 10.04900  19.71400 -21.84600 1.000 43.62977 ? 1   PRO A N   1 
ATOM   2    C CA  . PRO A 1 2   ? 9.00500   20.60000 -21.33100 1.000 38.03429 ? 1   PRO A CA  1 
ATOM   3    C C   . PRO A 1 2   ? 9.32500   21.15000 -19.97100 1.000 39.99954 ? 1   PRO A C   1 
ATOM   4    O O   . PRO A 1 2   ? 10.06600  20.49800 -19.21900 1.000 36.22847 ? 1   PRO A O   1 
ATOM   5    C CB  . PRO A 1 2   ? 7.80600   19.68400 -21.20800 1.000 31.20903 ? 1   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 2   ? 8.41500   18.36800 -20.89100 1.000 39.04693 ? 1   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 2   ? 9.68000   18.29900 -21.68900 1.000 40.43176 ? 1   PRO A CD  1 
ATOM   8    N N   . VAL A 1 3   ? 8.77700   22.32000 -19.64300 1.000 33.92180 ? 2   VAL A N   1 
ATOM   9    C CA  . VAL A 1 3   ? 8.76600   22.77500 -18.25700 1.000 31.50401 ? 2   VAL A CA  1 
ATOM   10   C C   . VAL A 1 3   ? 7.32100   22.74900 -17.76500 1.000 30.94385 ? 2   VAL A C   1 
ATOM   11   O O   . VAL A 1 3   ? 6.42300   23.30600 -18.40500 1.000 26.34382 ? 2   VAL A O   1 
ATOM   12   C CB  . VAL A 1 3   ? 9.41200   24.15600 -18.07100 1.000 35.36655 ? 2   VAL A CB  1 
ATOM   13   C CG1 . VAL A 1 3   ? 9.56600   24.44100 -16.59600 1.000 32.38198 ? 2   VAL A CG1 1 
ATOM   14   C CG2 . VAL A 1 3   ? 10.77800  24.19200 -18.73200 1.000 32.99877 ? 2   VAL A CG2 1 
ATOM   15   N N   . TYR A 1 4   ? 7.08800   22.07200 -16.65600 1.000 31.85738 ? 3   TYR A N   1 
ATOM   16   C CA  . TYR A 1 4   ? 5.75600   21.96800 -16.07800 1.000 31.23274 ? 3   TYR A CA  1 
ATOM   17   C C   . TYR A 1 4   ? 5.78500   22.76100 -14.77400 1.000 31.51272 ? 3   TYR A C   1 
ATOM   18   O O   . TYR A 1 4   ? 6.33600   22.30600 -13.76900 1.000 28.16459 ? 3   TYR A O   1 
ATOM   19   C CB  . TYR A 1 4   ? 5.37100   20.50900 -15.85100 1.000 30.27889 ? 3   TYR A CB  1 
ATOM   20   C CG  . TYR A 1 4   ? 4.89600   19.79700 -17.09000 1.000 27.73616 ? 3   TYR A CG  1 
ATOM   21   C CD1 . TYR A 1 4   ? 3.56100   19.86100 -17.48200 1.000 31.57655 ? 3   TYR A CD1 1 
ATOM   22   C CD2 . TYR A 1 4   ? 5.77400   19.05000 -17.87600 1.000 28.11559 ? 3   TYR A CD2 1 
ATOM   23   C CE1 . TYR A 1 4   ? 3.10000   19.19700 -18.62200 1.000 21.65344 ? 3   TYR A CE1 1 
ATOM   24   C CE2 . TYR A 1 4   ? 5.32300   18.38500 -19.02500 1.000 29.29813 ? 3   TYR A CE2 1 
ATOM   25   C CZ  . TYR A 1 4   ? 3.98000   18.46600 -19.38000 1.000 25.38836 ? 3   TYR A CZ  1 
ATOM   26   O OH  . TYR A 1 4   ? 3.51700   17.82600 -20.49900 1.000 29.14548 ? 3   TYR A OH  1 
ATOM   27   N N   . MET A 1 5   ? 5.18700   23.94900 -14.81300 1.000 36.96043 ? 4   MET A N   1 
ATOM   28   C CA  . MET A 1 5   ? 4.97300   24.79800 -13.65200 1.000 30.73367 ? 4   MET A CA  1 
ATOM   29   C C   . MET A 1 5   ? 3.76200   24.25200 -12.91400 1.000 32.00120 ? 4   MET A C   1 
ATOM   30   O O   . MET A 1 5   ? 2.68300   24.13200 -13.51000 1.000 30.89659 ? 4   MET A O   1 
ATOM   31   C CB  . MET A 1 5   ? 4.68400   26.22300 -14.12100 1.000 31.47606 ? 4   MET A CB  1 
ATOM   32   C CG  . MET A 1 5   ? 5.82800   27.01000 -14.74900 1.000 34.96498 ? 4   MET A CG  1 
ATOM   33   S SD  . MET A 1 5   ? 7.46500   26.67400 -14.11900 1.000 36.56318 ? 4   MET A SD  1 
ATOM   34   C CE  . MET A 1 5   ? 7.24000   27.39500 -12.48900 1.000 32.00236 ? 4   MET A CE  1 
ATOM   35   N N   . VAL A 1 6   ? 3.91900   23.91600 -11.63600 1.000 28.98953 ? 5   VAL A N   1 
ATOM   36   C CA  . VAL A 1 6   ? 2.82400   23.31000 -10.87900 1.000 39.41946 ? 5   VAL A CA  1 
ATOM   37   C C   . VAL A 1 6   ? 2.52000   24.18000 -9.66700  1.000 37.08634 ? 5   VAL A C   1 
ATOM   38   O O   . VAL A 1 6   ? 3.31500   24.23400 -8.72700  1.000 37.40587 ? 5   VAL A O   1 
ATOM   39   C CB  . VAL A 1 6   ? 3.15300   21.87100 -10.46400 1.000 32.47551 ? 5   VAL A CB  1 
ATOM   40   C CG1 . VAL A 1 6   ? 1.93300   21.20700 -9.88600  1.000 36.84838 ? 5   VAL A CG1 1 
ATOM   41   C CG2 . VAL A 1 6   ? 3.66600   21.11100 -11.65000 1.000 29.30516 ? 5   VAL A CG2 1 
ATOM   42   N N   . TYR A 1 7   ? 1.33600   24.78600 -9.64700  1.000 37.79567 ? 6   TYR A N   1 
ATOM   43   C CA  . TYR A 1 7   ? 0.93600   25.72100 -8.60400  1.000 32.47680 ? 6   TYR A CA  1 
ATOM   44   C C   . TYR A 1 7   ? 0.07800   24.99300 -7.58800  1.000 37.42585 ? 6   TYR A C   1 
ATOM   45   O O   . TYR A 1 7   ? -0.98200  24.44500 -7.93600  1.000 39.63248 ? 6   TYR A O   1 
ATOM   46   C CB  . TYR A 1 7   ? 0.19700   26.90600 -9.21300  1.000 31.76578 ? 6   TYR A CB  1 
ATOM   47   C CG  . TYR A 1 7   ? 1.10100   27.59100 -10.19400 1.000 34.62108 ? 6   TYR A CG  1 
ATOM   48   C CD1 . TYR A 1 7   ? 2.12800   28.43600 -9.74800  1.000 33.98831 ? 6   TYR A CD1 1 
ATOM   49   C CD2 . TYR A 1 7   ? 0.98800   27.34400 -11.55800 1.000 31.31632 ? 6   TYR A CD2 1 
ATOM   50   C CE1 . TYR A 1 7   ? 3.00100   29.03400 -10.64400 1.000 31.81084 ? 6   TYR A CE1 1 
ATOM   51   C CE2 . TYR A 1 7   ? 1.85300   27.94200 -12.46000 1.000 31.36832 ? 6   TYR A CE2 1 
ATOM   52   C CZ  . TYR A 1 7   ? 2.85100   28.77900 -12.00100 1.000 29.42721 ? 6   TYR A CZ  1 
ATOM   53   O OH  . TYR A 1 7   ? 3.69000   29.35400 -12.90400 1.000 29.92641 ? 6   TYR A OH  1 
ATOM   54   N N   . VAL A 1 8   ? 0.52800   25.04600 -6.33100  1.000 38.83441 ? 7   VAL A N   1 
ATOM   55   C CA  . VAL A 1 8   ? 0.03700   24.22300 -5.23600  1.000 38.57742 ? 7   VAL A CA  1 
ATOM   56   C C   . VAL A 1 8   ? -0.00500  25.06300 -3.97000  1.000 36.57280 ? 7   VAL A C   1 
ATOM   57   O O   . VAL A 1 8   ? 0.67200   26.08300 -3.84300  1.000 35.85413 ? 7   VAL A O   1 
ATOM   58   C CB  . VAL A 1 8   ? 0.94600   23.00200 -4.97500  1.000 32.20779 ? 7   VAL A CB  1 
ATOM   59   C CG1 . VAL A 1 8   ? 0.81000   21.99100 -6.06000  1.000 40.21395 ? 7   VAL A CG1 1 
ATOM   60   C CG2 . VAL A 1 8   ? 2.38200   23.45600 -4.85700  1.000 36.12147 ? 7   VAL A CG2 1 
ATOM   61   N N   . SER A 1 9   ? -0.82400  24.62900 -3.02900  1.000 38.78155 ? 8   SER A N   1 
ATOM   62   C CA  . SER A 1 9   ? -0.83500  25.28500 -1.74100  1.000 34.68305 ? 8   SER A CA  1 
ATOM   63   C C   . SER A 1 9   ? 0.30100   24.76100 -0.88400  1.000 43.44090 ? 8   SER A C   1 
ATOM   64   O O   . SER A 1 9   ? 0.72500   23.60600 -1.00400  1.000 40.51487 ? 8   SER A O   1 
ATOM   65   C CB  . SER A 1 9   ? -2.16800  25.09800 -1.04100  1.000 41.14294 ? 8   SER A CB  1 
ATOM   66   O OG  . SER A 1 9   ? -3.01500  26.19400 -1.35300  1.000 47.60825 ? 8   SER A OG  1 
ATOM   67   N N   . GLN A 1 10  ? 0.79600   25.64100 -0.02100  1.000 49.79405 ? 9   GLN A N   1 
ATOM   68   C CA  . GLN A 1 10  ? 1.99500   25.36700 0.75100   1.000 41.08432 ? 9   GLN A CA  1 
ATOM   69   C C   . GLN A 1 10  ? 1.81200   24.15700 1.64500   1.000 46.03867 ? 9   GLN A C   1 
ATOM   70   O O   . GLN A 1 10  ? 0.74500   23.94900 2.23000   1.000 51.80284 ? 9   GLN A O   1 
ATOM   71   C CB  . GLN A 1 10  ? 2.32500   26.58800 1.57300   1.000 40.70482 ? 9   GLN A CB  1 
ATOM   72   C CG  . GLN A 1 10  ? 3.68200   26.58500 2.18300   1.000 50.56564 ? 9   GLN A CG  1 
ATOM   73   C CD  . GLN A 1 10  ? 4.36400   27.92900 1.99300   1.000 48.64731 ? 9   GLN A CD  1 
ATOM   74   O OE1 . GLN A 1 10  ? 4.37000   28.49400 0.88200   1.000 40.97965 ? 9   GLN A OE1 1 
ATOM   75   N NE2 . GLN A 1 10  ? 4.87300   28.48600 3.08600   1.000 40.84736 ? 9   GLN A NE2 1 
ATOM   76   N N   . ASP A 1 11  ? 2.83500   23.30700 1.66500   1.000 56.02448 ? 10  ASP A N   1 
ATOM   77   C CA  . ASP A 1 11  ? 2.91900   22.13800 2.54800   1.000 59.20354 ? 10  ASP A CA  1 
ATOM   78   C C   . ASP A 1 11  ? 1.68100   21.24500 2.44600   1.000 57.93658 ? 10  ASP A C   1 
ATOM   79   O O   . ASP A 1 11  ? 1.34500   20.52400 3.39300   1.000 65.53178 ? 10  ASP A O   1 
ATOM   80   C CB  . ASP A 1 11  ? 3.21000   22.54800 3.99900   1.000 59.47996 ? 10  ASP A CB  1 
ATOM   81   C CG  . ASP A 1 11  ? 4.68100   22.99300 4.20800   1.000 59.13592 ? 10  ASP A CG  1 
ATOM   82   O OD1 . ASP A 1 11  ? 5.59000   22.55800 3.44100   1.000 39.39647 ? 10  ASP A OD1 1 
ATOM   83   O OD2 . ASP A 1 11  ? 4.92000   23.78600 5.15200   1.000 61.67040 ? 10  ASP A OD2 1 
ATOM   84   N N   . ARG A 1 12  ? 0.98400   21.32100 1.31000   1.000 54.26559 ? 11  ARG A N   1 
ATOM   85   C CA  . ARG A 1 12  ? -0.05500  20.35900 0.96400   1.000 49.03369 ? 11  ARG A CA  1 
ATOM   86   C C   . ARG A 1 12  ? 0.56100   19.08900 0.37800   1.000 46.66501 ? 11  ARG A C   1 
ATOM   87   O O   . ARG A 1 12  ? 0.06300   17.98800 0.62200   1.000 43.73795 ? 11  ARG A O   1 
ATOM   88   C CB  . ARG A 1 12  ? -1.03700  21.02700 -0.01100  1.000 42.79844 ? 11  ARG A CB  1 
ATOM   89   C CG  . ARG A 1 12  ? -2.01700  20.15800 -0.78200  1.000 43.75291 ? 11  ARG A CG  1 
ATOM   90   C CD  . ARG A 1 12  ? -2.55000  18.96200 -0.00800  1.000 53.11672 ? 11  ARG A CD  1 
ATOM   91   N NE  . ARG A 1 12  ? -3.93800  18.65000 -0.32000  1.000 49.03647 ? 11  ARG A NE  1 
ATOM   92   C CZ  . ARG A 1 12  ? -4.32100  18.01800 -1.41700  1.000 49.72594 ? 11  ARG A CZ  1 
ATOM   93   N NH1 . ARG A 1 12  ? -3.45200  17.68400 -2.35300  1.000 52.48167 ? 11  ARG A NH1 1 
ATOM   94   N NH2 . ARG A 1 12  ? -5.60300  17.70200 -1.57200  1.000 48.56314 ? 11  ARG A NH2 1 
ATOM   95   N N   . LEU A 1 13  ? 1.66800   19.19700 -0.34000  1.000 39.52178 ? 12  LEU A N   1 
ATOM   96   C CA  . LEU A 1 13  ? 2.32700   18.01300 -0.86100  1.000 43.98301 ? 12  LEU A CA  1 
ATOM   97   C C   . LEU A 1 13  ? 3.50200   17.65700 0.03300   1.000 43.83601 ? 12  LEU A C   1 
ATOM   98   O O   . LEU A 1 13  ? 4.46100   18.43300 0.15500   1.000 40.45212 ? 12  LEU A O   1 
ATOM   99   C CB  . LEU A 1 13  ? 2.79700   18.23300 -2.30000  1.000 43.40943 ? 12  LEU A CB  1 
ATOM   100  C CG  . LEU A 1 13  ? 1.68400   18.46100 -3.32000  1.000 37.95277 ? 12  LEU A CG  1 
ATOM   101  C CD1 . LEU A 1 13  ? 2.27500   18.50000 -4.71800  1.000 39.95093 ? 12  LEU A CD1 1 
ATOM   102  C CD2 . LEU A 1 13  ? 0.57900   17.38900 -3.20000  1.000 34.30593 ? 12  LEU A CD2 1 
ATOM   103  N N   . THR A 1 14  ? 3.46300   16.45500 0.59000   1.000 32.45720 ? 13  THR A N   1 
ATOM   104  C CA  . THR A 1 14  ? 4.65300   15.96400 1.23400   1.000 38.95941 ? 13  THR A CA  1 
ATOM   105  C C   . THR A 1 14  ? 5.71800   15.74300 0.16500   1.000 41.64932 ? 13  THR A C   1 
ATOM   106  O O   . THR A 1 14  ? 5.39300   15.59600 -1.01900  1.000 39.01342 ? 13  THR A O   1 
ATOM   107  C CB  . THR A 1 14  ? 4.35800   14.67400 1.99100   1.000 40.47748 ? 13  THR A CB  1 
ATOM   108  O OG1 . THR A 1 14  ? 4.05800   13.62800 1.05700   1.000 45.76774 ? 13  THR A OG1 1 
ATOM   109  C CG2 . THR A 1 14  ? 3.18300   14.87200 2.94700   1.000 43.84339 ? 13  THR A CG2 1 
ATOM   110  N N   . PRO A 1 15  ? 7.00000   15.75500 0.55100   1.000 45.29038 ? 14  PRO A N   1 
ATOM   111  C CA  . PRO A 1 15  ? 8.07100   15.42700 -0.40500  1.000 39.37055 ? 14  PRO A CA  1 
ATOM   112  C C   . PRO A 1 15  ? 7.76700   14.20200 -1.26600  1.000 39.48077 ? 14  PRO A C   1 
ATOM   113  O O   . PRO A 1 15  ? 7.92700   14.24500 -2.49100  1.000 40.17171 ? 14  PRO A O   1 
ATOM   114  C CB  . PRO A 1 15  ? 9.28300   15.20000 0.50100   1.000 32.91177 ? 14  PRO A CB  1 
ATOM   115  C CG  . PRO A 1 15  ? 9.02500   16.05200 1.70200   1.000 44.55798 ? 14  PRO A CG  1 
ATOM   116  C CD  . PRO A 1 15  ? 7.52500   16.20200 1.85700   1.000 41.97097 ? 14  PRO A CD  1 
ATOM   117  N N   . SER A 1 16  ? 7.31800   13.10800 -0.64400  1.000 42.52851 ? 15  SER A N   1 
ATOM   118  C CA  . SER A 1 16  ? 6.95500   11.91400 -1.40700  1.000 42.95899 ? 15  SER A CA  1 
ATOM   119  C C   . SER A 1 16  ? 5.78800   12.16500 -2.36100  1.000 45.12686 ? 15  SER A C   1 
ATOM   120  O O   . SER A 1 16  ? 5.76500   11.61200 -3.47300  1.000 38.18715 ? 15  SER A O   1 
ATOM   121  C CB  . SER A 1 16  ? 6.65900   10.76500 -0.45700  1.000 34.14313 ? 15  SER A CB  1 
ATOM   122  O OG  . SER A 1 16  ? 7.78500   10.53500 0.38000   1.000 54.69040 ? 15  SER A OG  1 
ATOM   123  N N   . ALA A 1 17  ? 4.82700   13.00600 -1.96300  1.000 40.97563 ? 16  ALA A N   1 
ATOM   124  C CA  . ALA A 1 17  ? 3.74200   13.33900 -2.88100  1.000 40.83785 ? 16  ALA A CA  1 
ATOM   125  C C   . ALA A 1 17  ? 4.23800   14.21500 -4.03100  1.000 45.91358 ? 16  ALA A C   1 
ATOM   126  O O   . ALA A 1 17  ? 3.76000   14.07600 -5.16700  1.000 46.63620 ? 16  ALA A O   1 
ATOM   127  C CB  . ALA A 1 17  ? 2.60000   14.01900 -2.13200  1.000 34.18736 ? 16  ALA A CB  1 
ATOM   128  N N   . LYS A 1 18  ? 5.21500   15.09000 -3.77600  1.000 40.66174 ? 17  LYS A N   1 
ATOM   129  C CA  . LYS A 1 18  ? 5.87400   15.78900 -4.87700  1.000 41.84993 ? 17  LYS A CA  1 
ATOM   130  C C   . LYS A 1 18  ? 6.56900   14.81500 -5.82300  1.000 39.44072 ? 17  LYS A C   1 
ATOM   131  O O   . LYS A 1 18  ? 6.45600   14.94300 -7.04600  1.000 39.85261 ? 17  LYS A O   1 
ATOM   132  C CB  . LYS A 1 18  ? 6.89900   16.78700 -4.34800  1.000 38.29423 ? 17  LYS A CB  1 
ATOM   133  C CG  . LYS A 1 18  ? 6.37000   18.13900 -4.00100  1.000 37.64564 ? 17  LYS A CG  1 
ATOM   134  C CD  . LYS A 1 18  ? 6.93400   18.53500 -2.66800  1.000 37.97317 ? 17  LYS A CD  1 
ATOM   135  C CE  . LYS A 1 18  ? 6.83500   20.02100 -2.47700  1.000 43.50750 ? 17  LYS A CE  1 
ATOM   136  N NZ  . LYS A 1 18  ? 8.02000   20.47900 -1.70200  1.000 42.46063 ? 17  LYS A NZ  1 
ATOM   137  N N   . HIS A 1 19  ? 7.32700   13.85500 -5.28100  1.000 41.59404 ? 18  HIS A N   1 
ATOM   138  C CA  . HIS A 1 19  ? 7.97100   12.87000 -6.15500  1.000 48.30706 ? 18  HIS A CA  1 
ATOM   139  C C   . HIS A 1 19  ? 6.94400   12.12800 -6.99900  1.000 41.58112 ? 18  HIS A C   1 
ATOM   140  O O   . HIS A 1 19  ? 7.14900   11.93400 -8.20400  1.000 33.79602 ? 18  HIS A O   1 
ATOM   141  C CB  . HIS A 1 19  ? 8.81200   11.86900 -5.35100  1.000 50.01792 ? 18  HIS A CB  1 
ATOM   142  C CG  . HIS A 1 19  ? 9.91400   11.23800 -6.15100  1.000 46.91048 ? 18  HIS A CG  1 
ATOM   143  N ND1 . HIS A 1 19  ? 9.73100   10.09900 -6.90700  1.000 50.52025 ? 18  HIS A ND1 1 
ATOM   144  C CD2 . HIS A 1 19  ? 11.20200  11.61000 -6.34400  1.000 52.29584 ? 18  HIS A CD2 1 
ATOM   145  C CE1 . HIS A 1 19  ? 10.86000  9.79000  -7.52400  1.000 53.28845 ? 18  HIS A CE1 1 
ATOM   146  N NE2 . HIS A 1 19  ? 11.77000  10.69000 -7.19800  1.000 48.99792 ? 18  HIS A NE2 1 
ATOM   147  N N   . ALA A 1 20  ? 5.79900   11.78200 -6.39700  1.000 41.11547 ? 19  ALA A N   1 
ATOM   148  C CA  . ALA A 1 20  ? 4.76000   11.03900 -7.11100  1.000 45.63083 ? 19  ALA A CA  1 
ATOM   149  C C   . ALA A 1 20  ? 4.12600   11.88100 -8.21200  1.000 41.23275 ? 19  ALA A C   1 
ATOM   150  O O   . ALA A 1 20  ? 3.89600   11.39100 -9.32400  1.000 44.16343 ? 19  ALA A O   1 
ATOM   151  C CB  . ALA A 1 20  ? 3.68600   10.55100 -6.13200  1.000 44.47241 ? 19  ALA A CB  1 
ATOM   152  N N   . VAL A 1 21  ? 3.85000   13.14900 -7.93000  1.000 41.10347 ? 20  VAL A N   1 
ATOM   153  C CA  . VAL A 1 21  ? 3.24400   14.02000 -8.93400  1.000 42.13142 ? 20  VAL A CA  1 
ATOM   154  C C   . VAL A 1 21  ? 4.21800   14.28800 -10.08600 1.000 38.45559 ? 20  VAL A C   1 
ATOM   155  O O   . VAL A 1 21  ? 3.85500   14.20200 -11.26700 1.000 36.18029 ? 20  VAL A O   1 
ATOM   156  C CB  . VAL A 1 21  ? 2.79300   15.33100 -8.26600  1.000 39.82610 ? 20  VAL A CB  1 
ATOM   157  C CG1 . VAL A 1 21  ? 2.66600   16.45100 -9.30000  1.000 40.86092 ? 20  VAL A CG1 1 
ATOM   158  C CG2 . VAL A 1 21  ? 1.51100   15.10700 -7.50800  1.000 31.63359 ? 20  VAL A CG2 1 
ATOM   159  N N   . ALA A 1 22  ? 5.46500   14.62700 -9.75400  1.000 35.75866 ? 21  ALA A N   1 
ATOM   160  C CA  . ALA A 1 22  ? 6.46600   14.87000 -10.78000 1.000 32.02682 ? 21  ALA A CA  1 
ATOM   161  C C   . ALA A 1 22  ? 6.65000   13.64700 -11.65500 1.000 34.37752 ? 21  ALA A C   1 
ATOM   162  O O   . ALA A 1 22  ? 6.64200   13.74200 -12.88500 1.000 28.51268 ? 21  ALA A O   1 
ATOM   163  C CB  . ALA A 1 22  ? 7.79300   15.25300 -10.13100 1.000 31.02341 ? 21  ALA A CB  1 
ATOM   164  N N   . LYS A 1 23  ? 6.83300   12.48400 -11.02900 1.000 37.92158 ? 22  LYS A N   1 
ATOM   165  C CA  . LYS A 1 23  ? 6.96100   11.24700 -11.77800 1.000 36.48865 ? 22  LYS A CA  1 
ATOM   166  C C   . LYS A 1 23  ? 5.74000   11.02000 -12.65800 1.000 30.74175 ? 22  LYS A C   1 
ATOM   167  O O   . LYS A 1 23  ? 5.88200   10.67000 -13.82600 1.000 31.15787 ? 22  LYS A O   1 
ATOM   168  C CB  . LYS A 1 23  ? 7.19900   10.09000 -10.80700 1.000 42.96475 ? 22  LYS A CB  1 
ATOM   169  C CG  . LYS A 1 23  ? 7.90900   8.88400  -11.41200 1.000 43.83968 ? 22  LYS A CG  1 
ATOM   170  C CD  . LYS A 1 23  ? 6.93800   7.73000  -11.63900 1.000 45.99608 ? 22  LYS A CD  1 
ATOM   171  C CE  . LYS A 1 23  ? 6.34100   7.26100  -10.33000 1.000 44.02388 ? 22  LYS A CE  1 
ATOM   172  N NZ  . LYS A 1 23  ? 5.86400   5.86500  -10.45000 1.000 63.95744 ? 22  LYS A NZ  1 
ATOM   173  N N   . ALA A 1 24  ? 4.53800   11.26500 -12.13700 1.000 32.34932 ? 23  ALA A N   1 
ATOM   174  C CA  . ALA A 1 24  ? 3.33300   11.09200 -12.93500 1.000 31.46274 ? 23  ALA A CA  1 
ATOM   175  C C   . ALA A 1 24  ? 3.37100   11.96400 -14.19900 1.000 34.05509 ? 23  ALA A C   1 
ATOM   176  O O   . ALA A 1 24  ? 3.10600   11.48000 -15.30800 1.000 33.25697 ? 23  ALA A O   1 
ATOM   177  C CB  . ALA A 1 24  ? 2.11900   11.42200 -12.06300 1.000 28.94794 ? 23  ALA A CB  1 
ATOM   178  N N   . ILE A 1 25  ? 3.75900   13.24100 -14.05300 1.000 34.03240 ? 24  ILE A N   1 
ATOM   179  C CA  . ILE A 1 25  ? 3.80300   14.17200 -15.18900 1.000 28.87374 ? 24  ILE A CA  1 
ATOM   180  C C   . ILE A 1 25  ? 4.94400   13.80600 -16.15400 1.000 31.19501 ? 24  ILE A C   1 
ATOM   181  O O   . ILE A 1 25  ? 4.76400   13.79800 -17.38000 1.000 39.23232 ? 24  ILE A O   1 
ATOM   182  C CB  . ILE A 1 25  ? 3.92700   15.62500 -14.67600 1.000 26.00951 ? 24  ILE A CB  1 
ATOM   183  C CG1 . ILE A 1 25  ? 2.74300   16.00200 -13.80100 1.000 26.73929 ? 24  ILE A CG1 1 
ATOM   184  C CG2 . ILE A 1 25  ? 4.04800   16.62500 -15.78400 1.000 21.21713 ? 24  ILE A CG2 1 
ATOM   185  C CD1 . ILE A 1 25  ? 2.88500   17.35000 -13.16400 1.000 26.22839 ? 24  ILE A CD1 1 
ATOM   186  N N   . THR A 1 26  ? 6.14200   13.53400 -15.62100 1.000 27.39412 ? 25  THR A N   1 
ATOM   187  C CA  . THR A 1 26  ? 7.26800   13.10500 -16.45600 1.000 32.18097 ? 25  THR A CA  1 
ATOM   188  C C   . THR A 1 26  ? 6.91600   11.86500 -17.26900 1.000 37.90285 ? 25  THR A C   1 
ATOM   189  O O   . THR A 1 26  ? 7.16600   11.81000 -18.48000 1.000 39.36910 ? 25  THR A O   1 
ATOM   190  C CB  . THR A 1 26  ? 8.50700   12.81600 -15.59400 1.000 33.23478 ? 25  THR A CB  1 
ATOM   191  O OG1 . THR A 1 26  ? 9.21800   14.02400 -15.33900 1.000 41.44898 ? 25  THR A OG1 1 
ATOM   192  C CG2 . THR A 1 26  ? 9.46300   11.82800 -16.28100 1.000 31.21846 ? 25  THR A CG2 1 
ATOM   193  N N   . ASP A 1 27  ? 6.38900   10.83600 -16.60800 1.000 27.24547 ? 26  ASP A N   1 
ATOM   194  C CA  . ASP A 1 27  ? 6.03600   9.61900  -17.31700 1.000 33.06986 ? 26  ASP A CA  1 
ATOM   195  C C   . ASP A 1 27  ? 4.94800   9.87500  -18.35100 1.000 38.38756 ? 26  ASP A C   1 
ATOM   196  O O   . ASP A 1 27  ? 4.99600   9.30700  -19.44600 1.000 39.91021 ? 26  ASP A O   1 
ATOM   197  C CB  . ASP A 1 27  ? 5.66800   8.51800  -16.32500 1.000 39.58680 ? 26  ASP A CB  1 
ATOM   198  C CG  . ASP A 1 27  ? 6.88300   8.06100  -15.49800 1.000 42.49458 ? 26  ASP A CG  1 
ATOM   199  O OD1 . ASP A 1 27  ? 7.95100   8.69800  -15.61000 1.000 38.50573 ? 26  ASP A OD1 1 
ATOM   200  O OD2 . ASP A 1 27  ? 6.77200   7.09200  -14.71600 1.000 42.83555 ? 26  ASP A OD2 1 
ATOM   201  N N   . ALA A 1 28  ? 3.96500   10.72900 -18.04300 1.000 33.53175 ? 27  ALA A N   1 
ATOM   202  C CA  . ALA A 1 28  ? 2.93900   11.02100 -19.04100 1.000 36.59341 ? 27  ALA A CA  1 
ATOM   203  C C   . ALA A 1 28  ? 3.55600   11.65400 -20.29000 1.000 38.06706 ? 27  ALA A C   1 
ATOM   204  O O   . ALA A 1 28  ? 3.28700   11.22500 -21.42300 1.000 33.54351 ? 27  ALA A O   1 
ATOM   205  C CB  . ALA A 1 28  ? 1.87200   11.94200 -18.44300 1.000 38.54849 ? 27  ALA A CB  1 
ATOM   206  N N   . HIS A 1 29  ? 4.41000   12.66400 -20.09800 1.000 36.81850 ? 28  HIS A N   1 
ATOM   207  C CA  . HIS A 1 29  ? 5.00800   13.34900 -21.24000 1.000 37.67264 ? 28  HIS A CA  1 
ATOM   208  C C   . HIS A 1 29  ? 5.89000   12.39200 -22.03500 1.000 40.56137 ? 28  HIS A C   1 
ATOM   209  O O   . HIS A 1 29  ? 5.79100   12.30300 -23.26800 1.000 39.51855 ? 28  HIS A O   1 
ATOM   210  C CB  . HIS A 1 29  ? 5.80300   14.56300 -20.76400 1.000 37.91477 ? 28  HIS A CB  1 
ATOM   211  C CG  . HIS A 1 29  ? 6.14600   15.53500 -21.85400 1.000 34.58250 ? 28  HIS A CG  1 
ATOM   212  N ND1 . HIS A 1 29  ? 5.27500   16.51100 -22.28400 1.000 28.26464 ? 28  HIS A ND1 1 
ATOM   213  C CD2 . HIS A 1 29  ? 7.28200   15.70800 -22.56800 1.000 38.21843 ? 28  HIS A CD2 1 
ATOM   214  C CE1 . HIS A 1 29  ? 5.84300   17.22500 -23.23500 1.000 28.60414 ? 28  HIS A CE1 1 
ATOM   215  N NE2 . HIS A 1 29  ? 7.06600   16.76400 -23.42300 1.000 37.75322 ? 28  HIS A NE2 1 
ATOM   216  N N   . ARG A 1 30  ? 6.75500   11.65100 -21.33700 1.000 44.57069 ? 29  ARG A N   1 
ATOM   217  C CA  . ARG A 1 30  ? 7.67100   10.75200 -22.02600 1.000 45.12327 ? 29  ARG A CA  1 
ATOM   218  C C   . ARG A 1 30  ? 6.91200   9.66400  -22.75300 1.000 39.78422 ? 29  ARG A C   1 
ATOM   219  O O   . ARG A 1 30  ? 7.21000   9.35700  -23.91000 1.000 42.49243 ? 29  ARG A O   1 
ATOM   220  C CB  . ARG A 1 30  ? 8.63700   10.11200 -21.02500 1.000 47.77563 ? 29  ARG A CB  1 
ATOM   221  C CG  . ARG A 1 30  ? 9.67800   9.21800  -21.67500 1.000 52.67295 ? 29  ARG A CG  1 
ATOM   222  C CD  . ARG A 1 30  ? 9.79800   7.86300  -20.97900 1.000 63.39815 ? 29  ARG A CD  1 
ATOM   223  N NE  . ARG A 1 30  ? 11.10000  7.23700  -21.19500 1.000 56.10293 ? 29  ARG A NE  1 
ATOM   224  C CZ  . ARG A 1 30  ? 11.53200  6.78700  -22.36500 1.000 65.70583 ? 29  ARG A CZ  1 
ATOM   225  N NH1 . ARG A 1 30  ? 10.80200  6.90600  -23.46700 1.000 63.46588 ? 29  ARG A NH1 1 
ATOM   226  N NH2 . ARG A 1 30  ? 12.73200  6.21500  -22.43500 1.000 60.79217 ? 29  ARG A NH2 1 
ATOM   227  N N   . GLY A 1 31  ? 5.88700   9.11000  -22.11200 1.000 38.54683 ? 30  GLY A N   1 
ATOM   228  C CA  . GLY A 1 31  ? 5.14800   8.02500  -22.72200 1.000 42.36434 ? 30  GLY A CA  1 
ATOM   229  C C   . GLY A 1 31  ? 4.37000   8.44800  -23.94500 1.000 34.56638 ? 30  GLY A C   1 
ATOM   230  O O   . GLY A 1 31  ? 4.39500   7.76200  -24.96600 1.000 30.80289 ? 30  GLY A O   1 
ATOM   231  N N   . LEU A 1 32  ? 3.71100   9.60700  -23.88200 1.000 37.84772 ? 31  LEU A N   1 
ATOM   232  C CA  . LEU A 1 32  ? 2.83000   9.98800  -24.96700 1.000 31.94110 ? 31  LEU A CA  1 
ATOM   233  C C   . LEU A 1 32  ? 3.56000   10.70700 -26.09100 1.000 40.59447 ? 31  LEU A C   1 
ATOM   234  O O   . LEU A 1 32  ? 3.06300   10.71200 -27.22800 1.000 35.30937 ? 31  LEU A O   1 
ATOM   235  C CB  . LEU A 1 32  ? 1.69900   10.86000 -24.43300 1.000 34.56258 ? 31  LEU A CB  1 
ATOM   236  C CG  . LEU A 1 32  ? 0.50300   10.14900 -23.79200 1.000 41.97607 ? 31  LEU A CG  1 
ATOM   237  C CD1 . LEU A 1 32  ? -0.47100  11.18700 -23.18700 1.000 31.80955 ? 31  LEU A CD1 1 
ATOM   238  C CD2 . LEU A 1 32  ? -0.23000  9.21100  -24.79500 1.000 38.07883 ? 31  LEU A CD2 1 
ATOM   239  N N   . THR A 1 33  ? 4.74700   11.26400 -25.82100 1.000 41.40574 ? 32  THR A N   1 
ATOM   240  C CA  . THR A 1 33  ? 5.45200   12.04100 -26.82300 1.000 33.11051 ? 32  THR A CA  1 
ATOM   241  C C   . THR A 1 33  ? 6.72200   11.39000 -27.35000 1.000 41.70848 ? 32  THR A C   1 
ATOM   242  O O   . THR A 1 33  ? 7.02700   11.55000 -28.53300 1.000 42.93579 ? 32  THR A O   1 
ATOM   243  C CB  . THR A 1 33  ? 5.82600   13.39800 -26.23000 1.000 37.96188 ? 32  THR A CB  1 
ATOM   244  O OG1 . THR A 1 33  ? 6.71800   13.17500 -25.13000 1.000 41.73886 ? 32  THR A OG1 1 
ATOM   245  C CG2 . THR A 1 33  ? 4.56600   14.10400 -25.72200 1.000 35.21162 ? 32  THR A CG2 1 
ATOM   246  N N   . GLY A 1 34  ? 7.41700   10.58600 -26.53900 1.000 39.61558 ? 33  GLY A N   1 
ATOM   247  C CA  . GLY A 1 34  ? 8.71700   10.05500 -26.89300 1.000 33.95270 ? 33  GLY A CA  1 
ATOM   248  C C   . GLY A 1 34  ? 9.91900   10.85100 -26.40000 1.000 38.59600 ? 33  GLY A C   1 
ATOM   249  O O   . GLY A 1 34  ? 11.04700  10.37200 -26.53200 1.000 38.49970 ? 33  GLY A O   1 
ATOM   250  N N   . THR A 1 35  ? 9.73100   12.03200 -25.81600 1.000 39.33341 ? 34  THR A N   1 
ATOM   251  C CA  . THR A 1 35  ? 10.87600  12.77800 -25.29700 1.000 47.10323 ? 34  THR A CA  1 
ATOM   252  C C   . THR A 1 35  ? 11.61700  11.97400 -24.22100 1.000 45.19584 ? 34  THR A C   1 
ATOM   253  O O   . THR A 1 35  ? 11.07800  11.05900 -23.60400 1.000 44.55029 ? 34  THR A O   1 
ATOM   254  C CB  . THR A 1 35  ? 10.45400  14.15500 -24.75700 1.000 47.15061 ? 34  THR A CB  1 
ATOM   255  O OG1 . THR A 1 35  ? 10.06600  14.06600 -23.37700 1.000 45.67261 ? 34  THR A OG1 1 
ATOM   256  C CG2 . THR A 1 35  ? 9.32000   14.71800 -25.57100 1.000 43.82844 ? 34  THR A CG2 1 
ATOM   257  N N   . GLN A 1 36  ? 12.89000  12.29600 -24.04000 1.000 43.97199 ? 35  GLN A N   1 
ATOM   258  C CA  . GLN A 1 36  ? 13.69300  11.63000 -23.02700 1.000 39.77378 ? 35  GLN A CA  1 
ATOM   259  C C   . GLN A 1 36  ? 13.30000  12.08700 -21.62500 1.000 45.27798 ? 35  GLN A C   1 
ATOM   260  O O   . GLN A 1 36  ? 12.87500  13.22900 -21.42100 1.000 44.57423 ? 35  GLN A O   1 
ATOM   261  C CB  . GLN A 1 36  ? 15.17900  11.88500 -23.27400 1.000 45.51348 ? 35  GLN A CB  1 
ATOM   262  C CG  . GLN A 1 36  ? 15.83900  10.97000 -24.32900 1.000 39.20004 ? 35  GLN A CG  1 
ATOM   263  C CD  . GLN A 1 36  ? 16.60000  11.77100 -25.37300 1.000 41.27174 ? 35  GLN A CD  1 
ATOM   264  O OE1 . GLN A 1 36  ? 16.54300  13.00400 -25.37100 1.000 41.81923 ? 35  GLN A OE1 1 
ATOM   265  N NE2 . GLN A 1 36  ? 17.31900  11.08200 -26.26600 1.000 39.50322 ? 35  GLN A NE2 1 
ATOM   266  N N   . HIS A 1 37  ? 13.36100  11.14200 -20.67600 1.000 43.76964 ? 36  HIS A N   1 
ATOM   267  C CA  . HIS A 1 37  ? 13.01000  11.39900 -19.27900 1.000 47.61085 ? 36  HIS A CA  1 
ATOM   268  C C   . HIS A 1 37  ? 13.56800  12.72800 -18.78200 1.000 48.91607 ? 36  HIS A C   1 
ATOM   269  O O   . HIS A 1 37  ? 12.84000  13.54700 -18.20700 1.000 47.85671 ? 36  HIS A O   1 
ATOM   270  C CB  . HIS A 1 37  ? 13.57400  10.30300 -18.37100 1.000 50.60294 ? 36  HIS A CB  1 
ATOM   271  C CG  . HIS A 1 37  ? 12.81800  9.01100  -18.38200 1.000 61.20516 ? 36  HIS A CG  1 
ATOM   272  N ND1 . HIS A 1 37  ? 13.44100  7.79900  -18.59900 1.000 61.87803 ? 36  HIS A ND1 1 
ATOM   273  C CD2 . HIS A 1 37  ? 11.51700  8.72600  -18.13800 1.000 63.44671 ? 36  HIS A CD2 1 
ATOM   274  C CE1 . HIS A 1 37  ? 12.55300  6.82700  -18.51500 1.000 59.22617 ? 36  HIS A CE1 1 
ATOM   275  N NE2 . HIS A 1 37  ? 11.37700  7.36200  -18.23500 1.000 61.51310 ? 36  HIS A NE2 1 
ATOM   276  N N   . PHE A 1 38  ? 14.87500  12.94900 -18.98400 1.000 45.37159 ? 37  PHE A N   1 
ATOM   277  C CA  . PHE A 1 38  ? 15.54700  14.09800 -18.38500 1.000 42.11897 ? 37  PHE A CA  1 
ATOM   278  C C   . PHE A 1 38  ? 15.07600  15.42500 -18.95500 1.000 43.48813 ? 37  PHE A C   1 
ATOM   279  O O   . PHE A 1 38  ? 15.35400  16.46000 -18.35000 1.000 46.24467 ? 37  PHE A O   1 
ATOM   280  C CB  . PHE A 1 38  ? 17.07500  13.99500 -18.55700 1.000 43.46636 ? 37  PHE A CB  1 
ATOM   281  C CG  . PHE A 1 38  ? 17.51500  13.40900 -19.88600 1.000 42.83535 ? 37  PHE A CG  1 
ATOM   282  C CD1 . PHE A 1 38  ? 17.60300  14.20600 -21.03000 1.000 43.65699 ? 37  PHE A CD1 1 
ATOM   283  C CD2 . PHE A 1 38  ? 17.84600  12.06300 -19.99000 1.000 45.35560 ? 37  PHE A CD2 1 
ATOM   284  C CE1 . PHE A 1 38  ? 18.00100  13.66300 -22.25200 1.000 42.85769 ? 37  PHE A CE1 1 
ATOM   285  C CE2 . PHE A 1 38  ? 18.23600  11.50600 -21.21200 1.000 45.25034 ? 37  PHE A CE2 1 
ATOM   286  C CZ  . PHE A 1 38  ? 18.32200  12.31200 -22.34100 1.000 38.43830 ? 37  PHE A CZ  1 
ATOM   287  N N   . LEU A 1 39  ? 14.33600  15.43100 -20.06200 1.000 42.46701 ? 38  LEU A N   1 
ATOM   288  C CA  . LEU A 1 39  ? 13.84200  16.69100 -20.59800 1.000 41.78555 ? 38  LEU A CA  1 
ATOM   289  C C   . LEU A 1 39  ? 12.61400  17.19800 -19.85500 1.000 39.18637 ? 38  LEU A C   1 
ATOM   290  O O   . LEU A 1 39  ? 12.17500  18.32900 -20.09000 1.000 37.00090 ? 38  LEU A O   1 
ATOM   291  C CB  . LEU A 1 39  ? 13.52800  16.53900 -22.08200 1.000 39.08814 ? 38  LEU A CB  1 
ATOM   292  C CG  . LEU A 1 39  ? 14.85700  16.52800 -22.80300 1.000 44.49307 ? 38  LEU A CG  1 
ATOM   293  C CD1 . LEU A 1 39  ? 14.70300  16.07200 -24.24100 1.000 43.02004 ? 38  LEU A CD1 1 
ATOM   294  C CD2 . LEU A 1 39  ? 15.48700  17.91900 -22.68500 1.000 44.11562 ? 38  LEU A CD2 1 
ATOM   295  N N   . ALA A 1 40  ? 12.07400  16.40800 -18.94400 1.000 36.51093 ? 39  ALA A N   1 
ATOM   296  C CA  . ALA A 1 40  ? 10.88000  16.79400 -18.21300 1.000 41.44603 ? 39  ALA A CA  1 
ATOM   297  C C   . ALA A 1 40  ? 11.34100  17.56600 -16.98400 1.000 40.26475 ? 39  ALA A C   1 
ATOM   298  O O   . ALA A 1 40  ? 12.06100  17.02800 -16.13300 1.000 39.47171 ? 39  ALA A O   1 
ATOM   299  C CB  . ALA A 1 40  ? 10.03700  15.57300 -17.84500 1.000 38.62392 ? 39  ALA A CB  1 
ATOM   300  N N   . GLN A 1 41  ? 11.03500  18.85700 -16.96100 1.000 37.90083 ? 40  GLN A N   1 
ATOM   301  C CA  . GLN A 1 41  ? 11.20900  19.67900 -15.77900 1.000 36.26401 ? 40  GLN A CA  1 
ATOM   302  C C   . GLN A 1 41  ? 9.87400   19.74600 -15.05800 1.000 35.87786 ? 40  GLN A C   1 
ATOM   303  O O   . GLN A 1 41  ? 8.83600   19.98500 -15.68900 1.000 37.91838 ? 40  GLN A O   1 
ATOM   304  C CB  . GLN A 1 41  ? 11.71000  21.07600 -16.14700 1.000 30.17321 ? 40  GLN A CB  1 
ATOM   305  C CG  . GLN A 1 41  ? 11.67400  22.03000 -14.97500 1.000 35.92536 ? 40  GLN A CG  1 
ATOM   306  C CD  . GLN A 1 41  ? 12.88800  22.97400 -14.92500 1.000 40.56798 ? 40  GLN A CD  1 
ATOM   307  O OE1 . GLN A 1 41  ? 13.82600  22.86800 -15.74300 1.000 33.87485 ? 40  GLN A OE1 1 
ATOM   308  N NE2 . GLN A 1 41  ? 12.88400  23.88600 -13.93800 1.000 32.70152 ? 40  GLN A NE2 1 
ATOM   309  N N   . VAL A 1 42  ? 9.88700   19.50300 -13.75500 1.000 33.46270 ? 41  VAL A N   1 
ATOM   310  C CA  . VAL A 1 42  ? 8.72500   19.75800 -12.91200 1.000 31.34732 ? 41  VAL A CA  1 
ATOM   311  C C   . VAL A 1 42  ? 9.14200   20.78800 -11.87600 1.000 38.41125 ? 41  VAL A C   1 
ATOM   312  O O   . VAL A 1 42  ? 10.12100  20.57800 -11.14400 1.000 39.31205 ? 41  VAL A O   1 
ATOM   313  C CB  . VAL A 1 42  ? 8.18700   18.47700 -12.25500 1.000 31.24342 ? 41  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 42  ? 7.38300   18.80200 -11.00500 1.000 33.61785 ? 41  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 42  ? 7.34800   17.66500 -13.24800 1.000 25.28774 ? 41  VAL A CG2 1 
ATOM   316  N N   . ASN A 1 43  ? 8.42800   21.91700 -11.83300 1.000 33.22283 ? 42  ASN A N   1 
ATOM   317  C CA  . ASN A 1 43  ? 8.79000   23.04300 -10.98400 1.000 28.61024 ? 42  ASN A CA  1 
ATOM   318  C C   . ASN A 1 43  ? 7.60700   23.36400 -10.07400 1.000 32.66893 ? 42  ASN A C   1 
ATOM   319  O O   . ASN A 1 43  ? 6.59200   23.90800 -10.53100 1.000 34.26322 ? 42  ASN A O   1 
ATOM   320  C CB  . ASN A 1 43  ? 9.18700   24.24900 -11.83900 1.000 34.42996 ? 42  ASN A CB  1 
ATOM   321  C CG  . ASN A 1 43  ? 10.25800  25.09800 -11.18300 1.000 34.15837 ? 42  ASN A CG  1 
ATOM   322  O OD1 . ASN A 1 43  ? 10.16700  25.41100 -9.98900  1.000 32.87662 ? 42  ASN A OD1 1 
ATOM   323  N ND2 . ASN A 1 43  ? 11.26000  25.51400 -11.96600 1.000 32.25152 ? 42  ASN A ND2 1 
ATOM   324  N N   . PHE A 1 44  ? 7.73300   23.04800 -8.78300  1.000 34.06004 ? 43  PHE A N   1 
ATOM   325  C CA  . PHE A 1 44  ? 6.63000   23.23300 -7.84700  1.000 35.28766 ? 43  PHE A CA  1 
ATOM   326  C C   . PHE A 1 44  ? 6.64100   24.65100 -7.28200  1.000 30.94656 ? 43  PHE A C   1 
ATOM   327  O O   . PHE A 1 44  ? 7.57300   25.03000 -6.57300  1.000 30.72154 ? 43  PHE A O   1 
ATOM   328  C CB  . PHE A 1 44  ? 6.71100   22.18800 -6.73600  1.000 35.63000 ? 43  PHE A CB  1 
ATOM   329  C CG  . PHE A 1 44  ? 6.15600   20.84200 -7.13600  1.000 31.01433 ? 43  PHE A CG  1 
ATOM   330  C CD1 . PHE A 1 44  ? 4.79100   20.62200 -7.16100  1.000 33.96414 ? 43  PHE A CD1 1 
ATOM   331  C CD2 . PHE A 1 44  ? 6.99300   19.81100 -7.48800  1.000 34.47209 ? 43  PHE A CD2 1 
ATOM   332  C CE1 . PHE A 1 44  ? 4.27500   19.39700 -7.52300  1.000 34.19240 ? 43  PHE A CE1 1 
ATOM   333  C CE2 . PHE A 1 44  ? 6.48000   18.58000 -7.84500  1.000 39.33632 ? 43  PHE A CE2 1 
ATOM   334  C CZ  . PHE A 1 44  ? 5.11700   18.37900 -7.87200  1.000 35.37119 ? 43  PHE A CZ  1 
ATOM   335  N N   . GLN A 1 45  ? 5.57700   25.42000 -7.56800  1.000 36.62577 ? 44  GLN A N   1 
ATOM   336  C CA  . GLN A 1 45  ? 5.35600   26.74700 -7.00000  1.000 33.53257 ? 44  GLN A CA  1 
ATOM   337  C C   . GLN A 1 45  ? 4.26800   26.65100 -5.93700  1.000 36.88509 ? 44  GLN A C   1 
ATOM   338  O O   . GLN A 1 45  ? 3.07800   26.53700 -6.26300  1.000 36.02743 ? 44  GLN A O   1 
ATOM   339  C CB  . GLN A 1 45  ? 4.95500   27.75200 -8.06700  1.000 30.77939 ? 44  GLN A CB  1 
ATOM   340  C CG  . GLN A 1 45  ? 5.98700   27.96700 -9.16700  1.000 39.09660 ? 44  GLN A CG  1 
ATOM   341  C CD  . GLN A 1 45  ? 7.39800   28.29700 -8.65800  1.000 31.33758 ? 44  GLN A CD  1 
ATOM   342  O OE1 . GLN A 1 45  ? 8.33000   27.56200 -8.93000  1.000 35.61296 ? 44  GLN A OE1 1 
ATOM   343  N NE2 . GLN A 1 45  ? 7.55400   29.41000 -7.95900  1.000 31.38262 ? 44  GLN A NE2 1 
ATOM   344  N N   . GLU A 1 46  ? 4.68700   26.71000 -4.66900  1.000 34.78352 ? 45  GLU A N   1 
ATOM   345  C CA  . GLU A 1 46  ? 3.81300   26.63100 -3.50500  1.000 33.61495 ? 45  GLU A CA  1 
ATOM   346  C C   . GLU A 1 46  ? 3.50300   28.04200 -3.03400  1.000 35.81768 ? 45  GLU A C   1 
ATOM   347  O O   . GLU A 1 46  ? 4.38800   28.90000 -3.01000  1.000 34.73182 ? 45  GLU A O   1 
ATOM   348  C CB  . GLU A 1 46  ? 4.45700   25.81600 -2.37200  1.000 36.46276 ? 45  GLU A CB  1 
ATOM   349  C CG  . GLU A 1 46  ? 5.41300   24.71100 -2.86600  1.000 35.25208 ? 45  GLU A CG  1 
ATOM   350  C CD  . GLU A 1 46  ? 5.61100   23.54500 -1.89300  1.000 39.60828 ? 45  GLU A CD  1 
ATOM   351  O OE1 . GLU A 1 46  ? 4.76000   22.63400 -1.83500  1.000 46.29486 ? 45  GLU A OE1 1 
ATOM   352  O OE2 . GLU A 1 46  ? 6.65200   23.50200 -1.21200  1.000 38.74360 ? 45  GLU A OE2 1 
ATOM   353  N N   . GLN A 1 47  ? 2.23400   28.30000 -2.75300  1.000 39.65604 ? 46  GLN A N   1 
ATOM   354  C CA  . GLN A 1 47  ? 1.77400   29.52400 -2.11900  1.000 33.35109 ? 46  GLN A CA  1 
ATOM   355  C C   . GLN A 1 47  ? 0.90400   29.14400 -0.93700  1.000 35.00630 ? 46  GLN A C   1 
ATOM   356  O O   . GLN A 1 47  ? 0.29400   28.06900 -0.93900  1.000 36.90796 ? 46  GLN A O   1 
ATOM   357  C CB  . GLN A 1 47  ? 0.98400   30.39900 -3.10100  1.000 29.34974 ? 46  GLN A CB  1 
ATOM   358  C CG  . GLN A 1 47  ? 1.84600   30.97000 -4.20300  1.000 32.18702 ? 46  GLN A CG  1 
ATOM   359  C CD  . GLN A 1 47  ? 2.87300   31.98300 -3.68800  1.000 31.65836 ? 46  GLN A CD  1 
ATOM   360  O OE1 . GLN A 1 47  ? 2.68200   32.60600 -2.64200  1.000 28.04247 ? 46  GLN A OE1 1 
ATOM   361  N NE2 . GLN A 1 47  ? 3.95600   32.16300 -4.44000  1.000 31.35874 ? 46  GLN A NE2 1 
ATOM   362  N N   . PRO A 1 48  ? 0.83800   29.98600 0.09300   1.000 31.31485 ? 47  PRO A N   1 
ATOM   363  C CA  . PRO A 1 48  ? 0.02900   29.63500 1.25800   1.000 36.04674 ? 47  PRO A CA  1 
ATOM   364  C C   . PRO A 1 48  ? -1.44200  29.53800 0.88500   1.000 37.46290 ? 47  PRO A C   1 
ATOM   365  O O   . PRO A 1 48  ? -1.95100  30.32300 0.08300   1.000 39.81379 ? 47  PRO A O   1 
ATOM   366  C CB  . PRO A 1 48  ? 0.30300   30.77700 2.23100   1.000 29.16157 ? 47  PRO A CB  1 
ATOM   367  C CG  . PRO A 1 48  ? 0.51100   31.92300 1.32500   1.000 34.90324 ? 47  PRO A CG  1 
ATOM   368  C CD  . PRO A 1 48  ? 1.28700   31.38100 0.16900   1.000 37.79333 ? 47  PRO A CD  1 
ATOM   369  N N   . ALA A 1 49  ? -2.11900  28.54700 1.46200   1.000 39.72599 ? 48  ALA A N   1 
ATOM   370  C CA  . ALA A 1 49  ? -3.53900  28.38100 1.20300   1.000 38.06633 ? 48  ALA A CA  1 
ATOM   371  C C   . ALA A 1 49  ? -4.25200  29.70400 1.42100   1.000 37.49989 ? 48  ALA A C   1 
ATOM   372  O O   . ALA A 1 49  ? -4.05600  30.36400 2.43900   1.000 40.57649 ? 48  ALA A O   1 
ATOM   373  C CB  . ALA A 1 49  ? -4.12100  27.30800 2.12100   1.000 35.47349 ? 48  ALA A CB  1 
ATOM   374  N N   . GLY A 1 50  ? -5.13300  30.04600 0.48800   1.000 38.94810 ? 49  GLY A N   1 
ATOM   375  C CA  . GLY A 1 50  ? -5.83300  31.31500 0.46100   1.000 37.80180 ? 49  GLY A CA  1 
ATOM   376  C C   . GLY A 1 50  ? -5.35200  32.25200 -0.62200  1.000 40.08559 ? 49  GLY A C   1 
ATOM   377  O O   . GLY A 1 50  ? -6.01800  33.26600 -0.88600  1.000 25.96785 ? 49  GLY A O   1 
ATOM   378  N N   . ASN A 1 51  ? -4.25300  31.91900 -1.30500  1.000 39.39021 ? 50  ASN A N   1 
ATOM   379  C CA  . ASN A 1 51  ? -3.83100  32.75900 -2.41500  1.000 34.24556 ? 50  ASN A CA  1 
ATOM   380  C C   . ASN A 1 51  ? -4.65000  32.53300 -3.67300  1.000 31.34736 ? 50  ASN A C   1 
ATOM   381  O O   . ASN A 1 51  ? -4.56300  33.36700 -4.57900  1.000 29.48132 ? 50  ASN A O   1 
ATOM   382  C CB  . ASN A 1 51  ? -2.35800  32.51700 -2.74600  1.000 30.49456 ? 50  ASN A CB  1 
ATOM   383  C CG  . ASN A 1 51  ? -1.42000  33.41000 -1.94200  1.000 35.89538 ? 50  ASN A CG  1 
ATOM   384  O OD1 . ASN A 1 51  ? -1.83300  34.07400 -0.98000  1.000 33.12708 ? 50  ASN A OD1 1 
ATOM   385  N ND2 . ASN A 1 51  ? -0.14300  33.43000 -2.33900  1.000 35.85656 ? 50  ASN A ND2 1 
ATOM   386  N N   . VAL A 1 52  ? -5.47000  31.46900 -3.72700  1.000 27.41513 ? 51  VAL A N   1 
ATOM   387  C CA  . VAL A 1 52  ? -6.19200  31.05100 -4.93500  1.000 28.09146 ? 51  VAL A CA  1 
ATOM   388  C C   . VAL A 1 52  ? -7.64900  31.45300 -4.80300  1.000 29.24645 ? 51  VAL A C   1 
ATOM   389  O O   . VAL A 1 52  ? -8.29300  31.12700 -3.80100  1.000 35.07571 ? 51  VAL A O   1 
ATOM   390  C CB  . VAL A 1 52  ? -6.08100  29.52500 -5.15100  1.000 35.14118 ? 51  VAL A CB  1 
ATOM   391  C CG1 . VAL A 1 52  ? -7.16700  29.02000 -6.10300  1.000 21.67113 ? 51  VAL A CG1 1 
ATOM   392  C CG2 . VAL A 1 52  ? -4.68000  29.09700 -5.60500  1.000 19.62797 ? 51  VAL A CG2 1 
ATOM   393  N N   . PHE A 1 53  ? -8.17300  32.17500 -5.78600  1.000 29.52732 ? 52  PHE A N   1 
ATOM   394  C CA  . PHE A 1 53  ? -9.59800  32.49600 -5.83000  1.000 30.98258 ? 52  PHE A CA  1 
ATOM   395  C C   . PHE A 1 53  ? -10.26300 31.93100 -7.08200  1.000 31.69234 ? 52  PHE A C   1 
ATOM   396  O O   . PHE A 1 53  ? -9.70200  31.99100 -8.18200  1.000 33.02873 ? 52  PHE A O   1 
ATOM   397  C CB  . PHE A 1 53  ? -9.84000  34.00700 -5.77300  1.000 30.09506 ? 52  PHE A CB  1 
ATOM   398  C CG  . PHE A 1 53  ? -9.54100  34.61300 -4.44300  1.000 37.03766 ? 52  PHE A CG  1 
ATOM   399  C CD1 . PHE A 1 53  ? -8.22500  34.79900 -4.02000  1.000 35.51548 ? 52  PHE A CD1 1 
ATOM   400  C CD2 . PHE A 1 53  ? -10.56500 34.97900 -3.59700  1.000 33.97038 ? 52  PHE A CD2 1 
ATOM   401  C CE1 . PHE A 1 53  ? -7.95000  35.36900 -2.78200  1.000 34.04998 ? 52  PHE A CE1 1 
ATOM   402  C CE2 . PHE A 1 53  ? -10.28600 35.52900 -2.36800  1.000 35.14183 ? 52  PHE A CE2 1 
ATOM   403  C CZ  . PHE A 1 53  ? -8.97500  35.73000 -1.96700  1.000 32.22364 ? 52  PHE A CZ  1 
ATOM   404  N N   . LEU A 1 54  ? -11.45900 31.38500 -6.91700  1.000 24.37915 ? 53  LEU A N   1 
ATOM   405  C CA  . LEU A 1 54  ? -12.27400 30.91500 -8.03000  1.000 31.57119 ? 53  LEU A CA  1 
ATOM   406  C C   . LEU A 1 54  ? -13.61200 31.61500 -7.91300  1.000 32.08417 ? 53  LEU A C   1 
ATOM   407  O O   . LEU A 1 54  ? -14.21600 31.60200 -6.84000  1.000 33.73880 ? 53  LEU A O   1 
ATOM   408  C CB  . LEU A 1 54  ? -12.45700 29.39200 -8.01300  1.000 31.92306 ? 53  LEU A CB  1 
ATOM   409  C CG  . LEU A 1 54  ? -11.45200 28.46000 -8.68600  1.000 30.10363 ? 53  LEU A CG  1 
ATOM   410  C CD1 . LEU A 1 54  ? -10.06500 28.95300 -8.55600  1.000 33.69822 ? 53  LEU A CD1 1 
ATOM   411  C CD2 . LEU A 1 54  ? -11.51200 27.10000 -8.02400  1.000 40.93384 ? 53  LEU A CD2 1 
ATOM   412  N N   . GLY A 1 55  ? -14.03400 32.28500 -8.98200  1.000 37.35764 ? 54  GLY A N   1 
ATOM   413  C CA  . GLY A 1 55  ? -15.24600 33.07500 -8.95500  1.000 31.87061 ? 54  GLY A CA  1 
ATOM   414  C C   . GLY A 1 55  ? -15.28600 34.06300 -7.80700  1.000 34.65488 ? 54  GLY A C   1 
ATOM   415  O O   . GLY A 1 55  ? -16.37000 34.42300 -7.34700  1.000 42.01655 ? 54  GLY A O   1 
ATOM   416  N N   . GLY A 1 56  ? -14.12800 34.51400 -7.32300  1.000 32.88483 ? 55  GLY A N   1 
ATOM   417  C CA  . GLY A 1 56  ? -14.10100 35.42200 -6.19400  1.000 33.71347 ? 55  GLY A CA  1 
ATOM   418  C C   . GLY A 1 56  ? -14.12200 34.77100 -4.82200  1.000 37.14763 ? 55  GLY A C   1 
ATOM   419  O O   . GLY A 1 56  ? -14.10500 35.48600 -3.81500  1.000 36.64907 ? 55  GLY A O   1 
ATOM   420  N N   . VAL A 1 57  ? -14.24100 33.45100 -4.74100  1.000 33.68596 ? 56  VAL A N   1 
ATOM   421  C CA  . VAL A 1 57  ? -14.28500 32.74300 -3.47000  1.000 32.56306 ? 56  VAL A CA  1 
ATOM   422  C C   . VAL A 1 57  ? -12.89600 32.19500 -3.16000  1.000 32.26850 ? 56  VAL A C   1 
ATOM   423  O O   . VAL A 1 57  ? -12.27600 31.52300 -3.98900  1.000 31.02874 ? 56  VAL A O   1 
ATOM   424  C CB  . VAL A 1 57  ? -15.34100 31.62500 -3.50400  1.000 32.19180 ? 56  VAL A CB  1 
ATOM   425  C CG1 . VAL A 1 57  ? -15.26400 30.80000 -2.25600  1.000 22.40896 ? 56  VAL A CG1 1 
ATOM   426  C CG2 . VAL A 1 57  ? -16.74600 32.22600 -3.69600  1.000 28.93952 ? 56  VAL A CG2 1 
ATOM   427  N N   . GLN A 1 58  ? -12.39800 32.49100 -1.98100  1.000 33.39780 ? 57  GLN A N   1 
ATOM   428  C CA  . GLN A 1 58  ? -11.10600 31.95200 -1.60300  1.000 36.05044 ? 57  GLN A CA  1 
ATOM   429  C C   . GLN A 1 58  ? -11.21900 30.45200 -1.33600  1.000 35.79392 ? 57  GLN A C   1 
ATOM   430  O O   . GLN A 1 58  ? -12.23200 29.96500 -0.82800  1.000 39.80463 ? 57  GLN A O   1 
ATOM   431  C CB  . GLN A 1 58  ? -10.57000 32.71300 -0.38700  1.000 33.81536 ? 57  GLN A CB  1 
ATOM   432  C CG  . GLN A 1 58  ? -9.66000  31.93000 0.51000   1.000 33.73955 ? 57  GLN A CG  1 
ATOM   433  C CD  . GLN A 1 58  ? -9.32900  32.70300 1.74200   1.000 35.34100 ? 57  GLN A CD  1 
ATOM   434  O OE1 . GLN A 1 58  ? -8.16900  32.79200 2.12800   1.000 40.01930 ? 57  GLN A OE1 1 
ATOM   435  N NE2 . GLN A 1 58  ? -10.33900 33.29300 2.36300   1.000 35.17946 ? 57  GLN A NE2 1 
ATOM   436  N N   . GLN A 1 59  ? -10.15800 29.71900 -1.65700  1.000 36.79148 ? 58  GLN A N   1 
ATOM   437  C CA  . GLN A 1 59  ? -10.15000 28.26900 -1.53200  1.000 37.52938 ? 58  GLN A CA  1 
ATOM   438  C C   . GLN A 1 59  ? -9.22600  27.83600 -0.39600  1.000 38.20372 ? 58  GLN A C   1 
ATOM   439  O O   . GLN A 1 59  ? -8.24700  28.51200 -0.05500  1.000 35.62167 ? 58  GLN A O   1 
ATOM   440  C CB  . GLN A 1 59  ? -9.67600  27.60000 -2.83700  1.000 39.90821 ? 58  GLN A CB  1 
ATOM   441  C CG  . GLN A 1 59  ? -10.25300 28.15000 -4.15700  1.000 35.22215 ? 58  GLN A CG  1 
ATOM   442  C CD  . GLN A 1 59  ? -11.63300 27.58000 -4.50600  1.000 35.97419 ? 58  GLN A CD  1 
ATOM   443  O OE1 . GLN A 1 59  ? -11.74600 26.43900 -4.97400  1.000 38.87909 ? 58  GLN A OE1 1 
ATOM   444  N NE2 . GLN A 1 59  ? -12.68500 28.37900 -4.29100  1.000 26.54379 ? 58  GLN A NE2 1 
ATOM   445  N N   . GLY A 1 60  ? -9.50700  26.65300 0.14200   1.000 38.79956 ? 59  GLY A N   1 
ATOM   446  C CA  . GLY A 1 60  ? -8.54300  25.98400 0.99000   1.000 41.24194 ? 59  GLY A CA  1 
ATOM   447  C C   . GLY A 1 60  ? -7.33700  25.55700 0.17200   1.000 40.54236 ? 59  GLY A C   1 
ATOM   448  O O   . GLY A 1 60  ? -7.13900  26.03100 -0.95300  1.000 45.39518 ? 59  GLY A O   1 
ATOM   449  N N   . GLY A 1 61  ? -6.54400  24.63200 0.67200   1.000 45.80075 ? 60  GLY A N   1 
ATOM   450  C CA  . GLY A 1 61  ? -5.24300  24.45900 0.04200   1.000 55.82637 ? 60  GLY A CA  1 
ATOM   451  C C   . GLY A 1 61  ? -5.17500  23.46400 -1.10300  1.000 49.88606 ? 60  GLY A C   1 
ATOM   452  O O   . GLY A 1 61  ? -4.14600  22.81400 -1.29700  1.000 52.67666 ? 60  GLY A O   1 
ATOM   453  N N   . ASP A 1 62  ? -6.26500  23.31800 -1.85200  1.000 48.99961 ? 61  ASP A N   1 
ATOM   454  C CA  . ASP A 1 62  ? -6.43200  22.14900 -2.69300  1.000 47.11580 ? 61  ASP A CA  1 
ATOM   455  C C   . ASP A 1 62  ? -6.36600  22.38400 -4.19600  1.000 47.83016 ? 61  ASP A C   1 
ATOM   456  O O   . ASP A 1 62  ? -6.09200  21.43200 -4.93200  1.000 45.38171 ? 61  ASP A O   1 
ATOM   457  C CB  . ASP A 1 62  ? -7.75500  21.46700 -2.34900  1.000 50.63662 ? 61  ASP A CB  1 
ATOM   458  C CG  . ASP A 1 62  ? -7.62500  19.97800 -2.36400  1.000 54.17200 ? 61  ASP A CG  1 
ATOM   459  O OD1 . ASP A 1 62  ? -7.42400  19.42200 -3.47000  1.000 52.52000 ? 61  ASP A OD1 1 
ATOM   460  O OD2 . ASP A 1 62  ? -7.60800  19.38500 -1.25900  1.000 47.87421 ? 61  ASP A OD2 1 
ATOM   461  N N   . THR A 1 63  ? -6.61900  23.59400 -4.67700  1.000 48.01406 ? 62  THR A N   1 
ATOM   462  C CA  . THR A 1 63  ? -6.57400  23.84100 -6.11200  1.000 43.24070 ? 62  THR A CA  1 
ATOM   463  C C   . THR A 1 63  ? -5.16500  23.58200 -6.63700  1.000 40.98254 ? 62  THR A C   1 
ATOM   464  O O   . THR A 1 63  ? -4.19100  24.02700 -6.03000  1.000 44.74954 ? 62  THR A O   1 
ATOM   465  C CB  . THR A 1 63  ? -6.97200  25.28700 -6.40000  1.000 39.81357 ? 62  THR A CB  1 
ATOM   466  O OG1 . THR A 1 63  ? -8.37000  25.44800 -6.15900  1.000 40.02174 ? 62  THR A OG1 1 
ATOM   467  C CG2 . THR A 1 63  ? -6.65100  25.65900 -7.87100  1.000 36.47488 ? 62  THR A CG2 1 
ATOM   468  N N   . ILE A 1 64  ? -5.05800  22.83200 -7.73900  1.000 32.08360 ? 63  ILE A N   1 
ATOM   469  C CA  . ILE A 1 64  ? -3.79100  22.60100 -8.43700  1.000 40.35175 ? 63  ILE A CA  1 
ATOM   470  C C   . ILE A 1 64  ? -3.87200  23.10300 -9.87000  1.000 36.27032 ? 63  ILE A C   1 
ATOM   471  O O   . ILE A 1 64  ? -4.79300  22.72600 -10.60900 1.000 33.74516 ? 63  ILE A O   1 
ATOM   472  C CB  . ILE A 1 64  ? -3.41000  21.11800 -8.46300  1.000 39.25729 ? 63  ILE A CB  1 
ATOM   473  C CG1 . ILE A 1 64  ? -3.55500  20.55600 -7.05800  1.000 41.21325 ? 63  ILE A CG1 1 
ATOM   474  C CG2 . ILE A 1 64  ? -2.02500  20.96700 -9.09400  1.000 30.12669 ? 63  ILE A CG2 1 
ATOM   475  C CD1 . ILE A 1 64  ? -2.29400  20.62600 -6.20800  1.000 47.95912 ? 63  ILE A CD1 1 
ATOM   476  N N   . PHE A 1 65  ? -2.88800  23.91000 -10.27500 1.000 30.76679 ? 64  PHE A N   1 
ATOM   477  C CA  . PHE A 1 65  ? -2.82300  24.38600 -11.65400 1.000 31.57933 ? 64  PHE A CA  1 
ATOM   478  C C   . PHE A 1 65  ? -1.51400  23.99500 -12.33300 1.000 30.85286 ? 64  PHE A C   1 
ATOM   479  O O   . PHE A 1 65  ? -0.43100  24.26000 -11.81100 1.000 32.98594 ? 64  PHE A O   1 
ATOM   480  C CB  . PHE A 1 65  ? -3.00700  25.89200 -11.73600 1.000 34.63953 ? 64  PHE A CB  1 
ATOM   481  C CG  . PHE A 1 65  ? -2.84100  26.43600 -13.13000 1.000 32.92081 ? 64  PHE A CG  1 
ATOM   482  C CD1 . PHE A 1 65  ? -3.56900  25.89100 -14.19000 1.000 28.61149 ? 64  PHE A CD1 1 
ATOM   483  C CD2 . PHE A 1 65  ? -1.99900  27.51100 -13.38100 1.000 30.35549 ? 64  PHE A CD2 1 
ATOM   484  C CE1 . PHE A 1 65  ? -3.43600  26.39800 -15.47000 1.000 27.11508 ? 64  PHE A CE1 1 
ATOM   485  C CE2 . PHE A 1 65  ? -1.86700  28.02000 -14.67200 1.000 28.88110 ? 64  PHE A CE2 1 
ATOM   486  C CZ  . PHE A 1 65  ? -2.58800  27.47200 -15.70500 1.000 26.82937 ? 64  PHE A CZ  1 
ATOM   487  N N   . VAL A 1 66  ? -1.61600  23.39300 -13.50600 1.000 26.09529 ? 65  VAL A N   1 
ATOM   488  C CA  . VAL A 1 66  ? -0.45900  22.91500 -14.24600 1.000 30.16756 ? 65  VAL A CA  1 
ATOM   489  C C   . VAL A 1 66  ? -0.33900  23.75000 -15.51700 1.000 28.97077 ? 65  VAL A C   1 
ATOM   490  O O   . VAL A 1 66  ? -1.15000  23.63800 -16.44500 1.000 28.85087 ? 65  VAL A O   1 
ATOM   491  C CB  . VAL A 1 66  ? -0.57500  21.41100 -14.54800 1.000 27.48735 ? 65  VAL A CB  1 
ATOM   492  C CG1 . VAL A 1 66  ? 0.48200   20.96200 -15.53500 1.000 23.82372 ? 65  VAL A CG1 1 
ATOM   493  C CG2 . VAL A 1 66  ? -0.47300  20.63100 -13.25600 1.000 23.86665 ? 65  VAL A CG2 1 
ATOM   494  N N   . HIS A 1 67  ? 0.70000   24.55000 -15.58600 1.000 28.00458 ? 66  HIS A N   1 
ATOM   495  C CA  . HIS A 1 67  ? 1.01300   25.29700 -16.79400 1.000 30.40056 ? 66  HIS A CA  1 
ATOM   496  C C   . HIS A 1 67  ? 2.19100   24.59200 -17.45300 1.000 25.72580 ? 66  HIS A C   1 
ATOM   497  O O   . HIS A 1 67  ? 3.29900   24.55800 -16.92000 1.000 23.28125 ? 66  HIS A O   1 
ATOM   498  C CB  . HIS A 1 67  ? 1.31800   26.76700 -16.49100 1.000 23.17845 ? 66  HIS A CB  1 
ATOM   499  C CG  . HIS A 1 67  ? 1.31900   27.62200 -17.71600 1.000 22.88500 ? 66  HIS A CG  1 
ATOM   500  N ND1 . HIS A 1 67  ? 1.65900   28.95100 -17.70200 1.000 18.21563 ? 66  HIS A ND1 1 
ATOM   501  C CD2 . HIS A 1 67  ? 1.04400   27.31700 -19.00700 1.000 22.01798 ? 66  HIS A CD2 1 
ATOM   502  C CE1 . HIS A 1 67  ? 1.59200   29.42900 -18.93000 1.000 26.97948 ? 66  HIS A CE1 1 
ATOM   503  N NE2 . HIS A 1 67  ? 1.21700   28.45800 -19.74200 1.000 19.18014 ? 66  HIS A NE2 1 
ATOM   504  N N   . GLY A 1 68  ? 1.91300   23.93000 -18.58500 1.000 23.09933 ? 67  GLY A N   1 
ATOM   505  C CA  . GLY A 1 68  ? 2.92400   23.20100 -19.30700 1.000 24.58903 ? 67  GLY A CA  1 
ATOM   506  C C   . GLY A 1 68  ? 3.42000   24.02900 -20.45600 1.000 27.77410 ? 67  GLY A C   1 
ATOM   507  O O   . GLY A 1 68  ? 2.63300   24.59100 -21.22200 1.000 27.67630 ? 67  GLY A O   1 
ATOM   508  N N   . LEU A 1 69  ? 4.75100   24.14100 -20.56500 1.000 31.76468 ? 68  LEU A N   1 
ATOM   509  C CA  . LEU A 1 69  ? 5.43100   24.84900 -21.63600 1.000 25.84456 ? 68  LEU A CA  1 
ATOM   510  C C   . LEU A 1 69  ? 6.09600   23.82700 -22.55400 1.000 27.00405 ? 68  LEU A C   1 
ATOM   511  O O   . LEU A 1 69  ? 7.04600   23.12400 -22.14900 1.000 28.25077 ? 68  LEU A O   1 
ATOM   512  C CB  . LEU A 1 69  ? 6.41600   25.84500 -21.04700 1.000 26.78106 ? 68  LEU A CB  1 
ATOM   513  C CG  . LEU A 1 69  ? 5.70100   26.74600 -20.04800 1.000 26.01496 ? 68  LEU A CG  1 
ATOM   514  C CD1 . LEU A 1 69  ? 6.67300   27.72000 -19.37800 1.000 25.39381 ? 68  LEU A CD1 1 
ATOM   515  C CD2 . LEU A 1 69  ? 4.61500   27.47500 -20.79300 1.000 24.66726 ? 68  LEU A CD2 1 
ATOM   516  N N   . HIS A 1 70  ? 5.59700   23.79900 -23.79600 1.000 28.01036 ? 69  HIS A N   1 
ATOM   517  C CA  . HIS A 1 70  ? 5.86500   22.83000 -24.85000 1.000 31.19602 ? 69  HIS A CA  1 
ATOM   518  C C   . HIS A 1 70  ? 6.50700   23.50500 -26.05000 1.000 30.15113 ? 69  HIS A C   1 
ATOM   519  O O   . HIS A 1 70  ? 6.35500   24.72000 -26.26200 1.000 30.65402 ? 69  HIS A O   1 
ATOM   520  C CB  . HIS A 1 70  ? 4.55200   22.15900 -25.34600 1.000 26.31375 ? 69  HIS A CB  1 
ATOM   521  C CG  . HIS A 1 70  ? 3.91900   21.22900 -24.36000 1.000 29.61612 ? 69  HIS A CG  1 
ATOM   522  N ND1 . HIS A 1 70  ? 4.30800   21.16300 -23.03800 1.000 30.30800 ? 69  HIS A ND1 1 
ATOM   523  C CD2 . HIS A 1 70  ? 2.94600   20.29300 -24.51800 1.000 32.59792 ? 69  HIS A CD2 1 
ATOM   524  C CE1 . HIS A 1 70  ? 3.59200   20.23200 -22.42200 1.000 32.90089 ? 69  HIS A CE1 1 
ATOM   525  N NE2 . HIS A 1 70  ? 2.76800   19.68200 -23.29800 1.000 29.63783 ? 69  HIS A NE2 1 
ATOM   526  N N   . ARG A 1 71  ? 7.18300   22.69400 -26.86600 1.000 25.62708 ? 70  ARG A N   1 
ATOM   527  C CA  . ARG A 1 71  ? 7.49800   23.11700 -28.22500 1.000 32.07030 ? 70  ARG A CA  1 
ATOM   528  C C   . ARG A 1 71  ? 6.30300   22.93600 -29.16700 1.000 29.51498 ? 70  ARG A C   1 
ATOM   529  O O   . ARG A 1 71  ? 5.35300   22.20900 -28.89300 1.000 40.12491 ? 70  ARG A O   1 
ATOM   530  C CB  . ARG A 1 71  ? 8.70700   22.37300 -28.80200 1.000 34.07595 ? 70  ARG A CB  1 
ATOM   531  C CG  . ARG A 1 71  ? 9.99800   22.42700 -28.01300 1.000 38.67773 ? 70  ARG A CG  1 
ATOM   532  C CD  . ARG A 1 71  ? 10.86400  21.26200 -28.44200 1.000 51.50404 ? 70  ARG A CD  1 
ATOM   533  N NE  . ARG A 1 71  ? 10.08400  20.03200 -28.54000 1.000 53.80008 ? 70  ARG A NE  1 
ATOM   534  C CZ  . ARG A 1 71  ? 10.60700  18.81500 -28.56100 1.000 51.08851 ? 70  ARG A CZ  1 
ATOM   535  N NH1 . ARG A 1 71  ? 11.90200  18.61800 -28.42400 1.000 50.22360 ? 70  ARG A NH1 1 
ATOM   536  N NH2 . ARG A 1 71  ? 9.80300   17.76800 -28.68700 1.000 54.58273 ? 70  ARG A NH2 1 
ATOM   537  N N   . GLU A 1 72  ? 6.32800   23.68500 -30.25200 1.000 31.00834 ? 71  GLU A N   1 
ATOM   538  C CA  . GLU A 1 72  ? 5.34500   23.55100 -31.31000 1.000 34.47880 ? 71  GLU A CA  1 
ATOM   539  C C   . GLU A 1 72  ? 5.59000   22.31000 -32.15300 1.000 30.64435 ? 71  GLU A C   1 
ATOM   540  O O   . GLU A 1 72  ? 6.70400   21.79200 -32.23400 1.000 33.85934 ? 71  GLU A O   1 
ATOM   541  C CB  . GLU A 1 72  ? 5.36100   24.77400 -32.22000 1.000 36.99062 ? 71  GLU A CB  1 
ATOM   542  C CG  . GLU A 1 72  ? 4.35200   25.81300 -31.82500 1.000 32.91563 ? 71  GLU A CG  1 
ATOM   543  C CD  . GLU A 1 72  ? 4.77800   27.16700 -32.27500 1.000 35.07018 ? 71  GLU A CD  1 
ATOM   544  O OE1 . GLU A 1 72  ? 5.57000   27.23700 -33.23800 1.000 36.77782 ? 71  GLU A OE1 1 
ATOM   545  O OE2 . GLU A 1 72  ? 4.33300   28.15700 -31.66500 1.000 47.69371 ? 71  GLU A OE2 1 
ATOM   546  N N   . GLY A 1 73  ? 4.51300   21.84200 -32.77800 1.000 24.72930 ? 72  GLY A N   1 
ATOM   547  C CA  . GLY A 1 73  ? 4.54400   20.76600 -33.75400 1.000 31.23557 ? 72  GLY A CA  1 
ATOM   548  C C   . GLY A 1 73  ? 3.65500   19.58100 -33.42600 1.000 29.56863 ? 72  GLY A C   1 
ATOM   549  O O   . GLY A 1 73  ? 3.36800   18.76800 -34.31800 1.000 23.02742 ? 72  GLY A O   1 
ATOM   550  N N   . ARG A 1 74  ? 3.17500   19.47000 -32.19700 1.000 25.64137 ? 73  ARG A N   1 
ATOM   551  C CA  . ARG A 1 74  ? 2.38300   18.32000 -31.81200 1.000 27.87302 ? 73  ARG A CA  1 
ATOM   552  C C   . ARG A 1 74  ? 0.90800   18.58500 -32.06900 1.000 25.75482 ? 73  ARG A C   1 
ATOM   553  O O   . ARG A 1 74  ? 0.44700   19.73500 -32.15000 1.000 28.79218 ? 73  ARG A O   1 
ATOM   554  C CB  . ARG A 1 74  ? 2.65900   17.96200 -30.34800 1.000 28.28276 ? 73  ARG A CB  1 
ATOM   555  C CG  . ARG A 1 74  ? 4.06600   17.39000 -30.15700 1.000 25.41451 ? 73  ARG A CG  1 
ATOM   556  C CD  . ARG A 1 74  ? 4.25300   16.72500 -28.78300 1.000 33.77063 ? 73  ARG A CD  1 
ATOM   557  N NE  . ARG A 1 74  ? 5.29500   17.36400 -27.98100 1.000 31.62481 ? 73  ARG A NE  1 
ATOM   558  C CZ  . ARG A 1 74  ? 6.50400   16.86000 -27.76800 1.000 31.09639 ? 73  ARG A CZ  1 
ATOM   559  N NH1 . ARG A 1 74  ? 6.89200   15.72500 -28.32300 1.000 40.92771 ? 73  ARG A NH1 1 
ATOM   560  N NH2 . ARG A 1 74  ? 7.32900   17.48600 -26.93700 1.000 36.25625 ? 73  ARG A NH2 1 
ATOM   561  N N   . SER A 1 75  ? 0.18200   17.50400 -32.26700 1.000 21.61258 ? 74  SER A N   1 
ATOM   562  C CA  . SER A 1 75  ? -1.19800  17.62500 -32.70300 1.000 26.24055 ? 74  SER A CA  1 
ATOM   563  C C   . SER A 1 75  ? -2.12500  17.97700 -31.53900 1.000 24.75148 ? 74  SER A C   1 
ATOM   564  O O   . SER A 1 75  ? -1.78100  17.85100 -30.36500 1.000 31.34671 ? 74  SER A O   1 
ATOM   565  C CB  . SER A 1 75  ? -1.64300  16.34600 -33.41900 1.000 24.42039 ? 74  SER A CB  1 
ATOM   566  O OG  . SER A 1 75  ? -2.16800  15.37600 -32.53700 1.000 24.12931 ? 74  SER A OG  1 
ATOM   567  N N   . ALA A 1 76  ? -3.28100  18.52100 -31.87600 1.000 20.50188 ? 75  ALA A N   1 
ATOM   568  C CA  . ALA A 1 76  ? -4.26600  18.76000 -30.83900 1.000 23.81382 ? 75  ALA A CA  1 
ATOM   569  C C   . ALA A 1 76  ? -4.70200  17.44300 -30.20700 1.000 24.51905 ? 75  ALA A C   1 
ATOM   570  O O   . ALA A 1 76  ? -4.90200  17.36000 -28.99200 1.000 24.61776 ? 75  ALA A O   1 
ATOM   571  C CB  . ALA A 1 76  ? -5.45400  19.53600 -31.41500 1.000 20.05784 ? 75  ALA A CB  1 
ATOM   572  N N   . ASP A 1 77  ? -4.84300  16.39800 -31.01800 1.000 31.49062 ? 76  ASP A N   1 
ATOM   573  C CA  . ASP A 1 77  ? -5.21800  15.07800 -30.50200 1.000 30.97165 ? 76  ASP A CA  1 
ATOM   574  C C   . ASP A 1 77  ? -4.26000  14.61100 -29.41000 1.000 28.84994 ? 76  ASP A C   1 
ATOM   575  O O   . ASP A 1 77  ? -4.68400  14.21700 -28.31400 1.000 31.20403 ? 76  ASP A O   1 
ATOM   576  C CB  . ASP A 1 77  ? -5.27300  14.09100 -31.66700 1.000 24.20372 ? 76  ASP A CB  1 
ATOM   577  C CG  . ASP A 1 77  ? -5.76200  12.72100 -31.25300 1.000 43.55993 ? 76  ASP A CG  1 
ATOM   578  O OD1 . ASP A 1 77  ? -6.45500  12.65200 -30.20900 1.000 48.89084 ? 76  ASP A OD1 1 
ATOM   579  O OD2 . ASP A 1 77  ? -5.55000  11.73700 -32.02400 1.000 39.36598 ? 76  ASP A OD2 1 
ATOM   580  N N   . LEU A 1 78  ? -2.95700  14.70100 -29.68200 1.000 27.03253 ? 77  LEU A N   1 
ATOM   581  C CA  . LEU A 1 78  ? -1.95800  14.25200 -28.73300 1.000 29.53934 ? 77  LEU A CA  1 
ATOM   582  C C   . LEU A 1 78  ? -1.92500  15.15000 -27.50200 1.000 29.17781 ? 77  LEU A C   1 
ATOM   583  O O   . LEU A 1 78  ? -1.78400  14.66700 -26.36900 1.000 24.78557 ? 77  LEU A O   1 
ATOM   584  C CB  . LEU A 1 78  ? -0.60200  14.21900 -29.43100 1.000 27.98268 ? 77  LEU A CB  1 
ATOM   585  C CG  . LEU A 1 78  ? 0.53200   13.44000 -28.74400 1.000 40.98159 ? 77  LEU A CG  1 
ATOM   586  C CD1 . LEU A 1 78  ? 1.31600   14.28800 -27.72300 1.000 39.11331 ? 77  LEU A CD1 1 
ATOM   587  C CD2 . LEU A 1 78  ? -0.04900  12.19400 -28.06200 1.000 34.87302 ? 77  LEU A CD2 1 
ATOM   588  N N   . LYS A 1 79  ? -2.11200  16.45600 -27.69800 1.000 28.00748 ? 78  LYS A N   1 
ATOM   589  C CA  . LYS A 1 79  ? -2.15800  17.35900 -26.55600 1.000 25.60325 ? 78  LYS A CA  1 
ATOM   590  C C   . LYS A 1 79  ? -3.37700  17.07600 -25.68900 1.000 21.79583 ? 78  LYS A C   1 
ATOM   591  O O   . LYS A 1 79  ? -3.30100  17.11800 -24.45600 1.000 20.05983 ? 78  LYS A O   1 
ATOM   592  C CB  . LYS A 1 79  ? -2.16100  18.81500 -27.02900 1.000 22.24087 ? 78  LYS A CB  1 
ATOM   593  C CG  . LYS A 1 79  ? -0.89300  19.28500 -27.73300 1.000 27.35034 ? 78  LYS A CG  1 
ATOM   594  C CD  . LYS A 1 79  ? -0.91900  20.79800 -28.01700 1.000 28.47762 ? 78  LYS A CD  1 
ATOM   595  C CE  . LYS A 1 79  ? -1.51700  21.10700 -29.40100 1.000 25.63338 ? 78  LYS A CE  1 
ATOM   596  N NZ  . LYS A 1 79  ? -1.48100  22.57700 -29.66200 1.000 27.90284 ? 78  LYS A NZ  1 
ATOM   597  N N   . GLY A 1 80  ? -4.50500  16.77800 -26.31300 1.000 21.29026 ? 79  GLY A N   1 
ATOM   598  C CA  . GLY A 1 80  ? -5.69000  16.48400 -25.54200 1.000 22.45240 ? 79  GLY A CA  1 
ATOM   599  C C   . GLY A 1 80  ? -5.53200  15.23700 -24.71000 1.000 22.32109 ? 79  GLY A C   1 
ATOM   600  O O   . GLY A 1 80  ? -5.88400  15.21800 -23.52800 1.000 29.34831 ? 79  GLY A O   1 
ATOM   601  N N   . GLN A 1 81  ? -4.97800  14.18600 -25.30600 1.000 21.78575 ? 80  GLN A N   1 
ATOM   602  C CA  . GLN A 1 81  ? -4.77200  12.98700 -24.51700 1.000 25.93760 ? 80  GLN A CA  1 
ATOM   603  C C   . GLN A 1 81  ? -3.81500  13.28300 -23.38000 1.000 29.17474 ? 80  GLN A C   1 
ATOM   604  O O   . GLN A 1 81  ? -4.06100  12.87700 -22.23900 1.000 23.53285 ? 80  GLN A O   1 
ATOM   605  C CB  . GLN A 1 81  ? -4.24600  11.85700 -25.38000 1.000 27.35667 ? 80  GLN A CB  1 
ATOM   606  C CG  . GLN A 1 81  ? -5.14300  11.48500 -26.50700 1.000 30.84702 ? 80  GLN A CG  1 
ATOM   607  C CD  . GLN A 1 81  ? -4.37300  10.68900 -27.52600 1.000 43.28390 ? 80  GLN A CD  1 
ATOM   608  O OE1 . GLN A 1 81  ? -3.36400  10.05200 -27.19200 1.000 36.76418 ? 80  GLN A OE1 1 
ATOM   609  N NE2 . GLN A 1 81  ? -4.82800  10.71800 -28.77100 1.000 39.76567 ? 80  GLN A NE2 1 
ATOM   610  N N   . LEU A 1 82  ? -2.73900  14.03200 -23.67600 1.000 25.02011 ? 81  LEU A N   1 
ATOM   611  C CA  . LEU A 1 82  ? -1.74500  14.36700 -22.66600 1.000 23.86939 ? 81  LEU A CA  1 
ATOM   612  C C   . LEU A 1 82  ? -2.35700  15.14400 -21.51300 1.000 26.07372 ? 81  LEU A C   1 
ATOM   613  O O   . LEU A 1 82  ? -2.07300  14.85100 -20.34900 1.000 29.70532 ? 81  LEU A O   1 
ATOM   614  C CB  . LEU A 1 82  ? -0.61300  15.16900 -23.29800 1.000 24.38468 ? 81  LEU A CB  1 
ATOM   615  C CG  . LEU A 1 82  ? 0.49100   15.48100 -22.29900 1.000 23.78234 ? 81  LEU A CG  1 
ATOM   616  C CD1 . LEU A 1 82  ? 1.02000   14.15600 -21.76900 1.000 35.14205 ? 81  LEU A CD1 1 
ATOM   617  C CD2 . LEU A 1 82  ? 1.59400   16.32200 -22.92900 1.000 24.06422 ? 81  LEU A CD2 1 
ATOM   618  N N   . ALA A 1 83  ? -3.19900  16.14100 -21.81200 1.000 22.73145 ? 82  ALA A N   1 
ATOM   619  C CA  . ALA A 1 83  ? -3.82400  16.91500 -20.74600 1.000 23.93664 ? 82  ALA A CA  1 
ATOM   620  C C   . ALA A 1 83  ? -4.74500  16.03600 -19.90300 1.000 25.27643 ? 82  ALA A C   1 
ATOM   621  O O   . ALA A 1 83  ? -4.73900  16.11800 -18.66800 1.000 27.51462 ? 82  ALA A O   1 
ATOM   622  C CB  . ALA A 1 83  ? -4.58800  18.09700 -21.34400 1.000 24.02008 ? 82  ALA A CB  1 
ATOM   623  N N   . GLN A 1 84  ? -5.53300  15.17800 -20.55800 1.000 22.45648 ? 83  GLN A N   1 
ATOM   624  C CA  . GLN A 1 84  ? -6.39600  14.23700 -19.84400 1.000 30.49040 ? 83  GLN A CA  1 
ATOM   625  C C   . GLN A 1 84  ? -5.58800  13.27400 -18.96300 1.000 32.86936 ? 83  GLN A C   1 
ATOM   626  O O   . GLN A 1 84  ? -5.97400  12.97400 -17.81700 1.000 34.88304 ? 83  GLN A O   1 
ATOM   627  C CB  . GLN A 1 84  ? -7.25400  13.46500 -20.85600 1.000 28.90890 ? 83  GLN A CB  1 
ATOM   628  C CG  . GLN A 1 84  ? -8.24700  12.49900 -20.20900 1.000 28.99475 ? 83  GLN A CG  1 
ATOM   629  C CD  . GLN A 1 84  ? -9.10200  13.19000 -19.15900 1.000 32.35411 ? 83  GLN A CD  1 
ATOM   630  O OE1 . GLN A 1 84  ? -8.90900  12.99500 -17.96200 1.000 40.61875 ? 83  GLN A OE1 1 
ATOM   631  N NE2 . GLN A 1 84  ? -10.04800 13.99300 -19.60100 1.000 26.67649 ? 83  GLN A NE2 1 
ATOM   632  N N   . ARG A 1 85  ? -4.47900  12.76100 -19.49500 1.000 28.11990 ? 84  ARG A N   1 
ATOM   633  C CA  . ARG A 1 85  ? -3.66600  11.81100 -18.75500 1.000 31.53791 ? 84  ARG A CA  1 
ATOM   634  C C   . ARG A 1 85  ? -3.03900  12.48000 -17.56300 1.000 35.12655 ? 84  ARG A C   1 
ATOM   635  O O   . ARG A 1 85  ? -2.92900  11.88100 -16.48800 1.000 40.98044 ? 84  ARG A O   1 
ATOM   636  C CB  . ARG A 1 85  ? -2.57600  11.23200 -19.64500 1.000 32.03801 ? 84  ARG A CB  1 
ATOM   637  C CG  . ARG A 1 85  ? -2.72400  9.76100  -19.99400 1.000 40.44328 ? 84  ARG A CG  1 
ATOM   638  C CD  . ARG A 1 85  ? -1.34400  9.14600  -20.30100 1.000 43.38957 ? 84  ARG A CD  1 
ATOM   639  N NE  . ARG A 1 85  ? -0.61800  8.75700  -19.09300 1.000 44.24261 ? 84  ARG A NE  1 
ATOM   640  C CZ  . ARG A 1 85  ? 0.60500   8.23700  -19.08800 1.000 45.13567 ? 84  ARG A CZ  1 
ATOM   641  N NH1 . ARG A 1 85  ? 1.27000   8.01200  -20.21200 1.000 43.99026 ? 84  ARG A NH1 1 
ATOM   642  N NH2 . ARG A 1 85  ? 1.16200   7.90100  -17.93000 1.000 45.95489 ? 84  ARG A NH2 1 
ATOM   643  N N   . ILE A 1 86  ? -2.66000  13.74200 -17.72300 1.000 31.04742 ? 85  ILE A N   1 
ATOM   644  C CA  . ILE A 1 86  ? -2.10500  14.47600 -16.60200 1.000 33.69108 ? 85  ILE A CA  1 
ATOM   645  C C   . ILE A 1 86  ? -3.16500  14.67600 -15.52900 1.000 30.59438 ? 85  ILE A C   1 
ATOM   646  O O   . ILE A 1 86  ? -2.93900  14.38500 -14.35200 1.000 31.53624 ? 85  ILE A O   1 
ATOM   647  C CB  . ILE A 1 86  ? -1.49700  15.79400 -17.10900 1.000 31.19070 ? 85  ILE A CB  1 
ATOM   648  C CG1 . ILE A 1 86  ? -0.11000  15.48400 -17.67400 1.000 25.32485 ? 85  ILE A CG1 1 
ATOM   649  C CG2 . ILE A 1 86  ? -1.50800  16.88000 -16.03300 1.000 23.39954 ? 85  ILE A CG2 1 
ATOM   650  C CD1 . ILE A 1 86  ? 0.64900   16.65300 -18.06000 1.000 19.51997 ? 85  ILE A CD1 1 
ATOM   651  N N   . VAL A 1 87  ? -4.35800  15.11200 -15.92800 1.000 34.31422 ? 86  VAL A N   1 
ATOM   652  C CA  . VAL A 1 87  ? -5.44600  15.26600 -14.95900 1.000 41.12056 ? 86  VAL A CA  1 
ATOM   653  C C   . VAL A 1 87  ? -5.63500  13.98400 -14.13500 1.000 40.29512 ? 86  VAL A C   1 
ATOM   654  O O   . VAL A 1 87  ? -5.53800  13.99500 -12.90300 1.000 34.73665 ? 86  VAL A O   1 
ATOM   655  C CB  . VAL A 1 87  ? -6.74300  15.66800 -15.68100 1.000 37.68847 ? 86  VAL A CB  1 
ATOM   656  C CG1 . VAL A 1 87  ? -7.95300  15.44000 -14.75400 1.000 34.75957 ? 86  VAL A CG1 1 
ATOM   657  C CG2 . VAL A 1 87  ? -6.64500  17.11900 -16.14900 1.000 32.46833 ? 86  VAL A CG2 1 
ATOM   658  N N   . ASP A 1 88  ? -5.84600  12.84700 -14.81400 1.000 42.03887 ? 87  ASP A N   1 
ATOM   659  C CA  . ASP A 1 88  ? -6.07700  11.57600 -14.11500 1.000 39.81591 ? 87  ASP A CA  1 
ATOM   660  C C   . ASP A 1 88  ? -4.88800  11.17700 -13.23300 1.000 39.85106 ? 87  ASP A C   1 
ATOM   661  O O   . ASP A 1 88  ? -5.05400  10.85200 -12.04400 1.000 48.20739 ? 87  ASP A O   1 
ATOM   662  C CB  . ASP A 1 88  ? -6.35700  10.46000 -15.13200 1.000 42.99506 ? 87  ASP A CB  1 
ATOM   663  C CG  . ASP A 1 88  ? -7.62600  10.69400 -15.96300 1.000 47.27312 ? 87  ASP A CG  1 
ATOM   664  O OD1 . ASP A 1 88  ? -8.56100  11.39700 -15.50000 1.000 48.28398 ? 87  ASP A OD1 1 
ATOM   665  O OD2 . ASP A 1 88  ? -7.67400  10.17000 -17.10100 1.000 45.38597 ? 87  ASP A OD2 1 
ATOM   666  N N   . ASP A 1 89  ? -3.67400  11.19800 -13.79300 1.000 38.16988 ? 88  ASP A N   1 
ATOM   667  C CA  . ASP A 1 89  ? -2.52200  10.64600 -13.09300 1.000 38.85455 ? 88  ASP A CA  1 
ATOM   668  C C   . ASP A 1 89  ? -2.10900  11.50500 -11.91600 1.000 38.81108 ? 88  ASP A C   1 
ATOM   669  O O   . ASP A 1 89  ? -1.62200  10.97100 -10.91400 1.000 42.63906 ? 88  ASP A O   1 
ATOM   670  C CB  . ASP A 1 89  ? -1.34900  10.50600 -14.05800 1.000 41.93142 ? 88  ASP A CB  1 
ATOM   671  C CG  . ASP A 1 89  ? -1.49100  9.31100  -14.94900 1.000 41.65685 ? 88  ASP A CG  1 
ATOM   672  O OD1 . ASP A 1 89  ? -2.37100  8.47800  -14.64300 1.000 42.30059 ? 88  ASP A OD1 1 
ATOM   673  O OD2 . ASP A 1 89  ? -0.75500  9.22300  -15.95500 1.000 38.75568 ? 88  ASP A OD2 1 
ATOM   674  N N   . VAL A 1 90  ? -2.32000  12.82300 -12.00900 1.000 40.87205 ? 89  VAL A N   1 
ATOM   675  C CA  . VAL A 1 90  ? -2.10900  13.71600 -10.87100 1.000 36.71965 ? 89  VAL A CA  1 
ATOM   676  C C   . VAL A 1 90  ? -3.20600  13.54100 -9.82300  1.000 34.44140 ? 89  VAL A C   1 
ATOM   677  O O   . VAL A 1 90  ? -2.92800  13.48000 -8.62300  1.000 33.74873 ? 89  VAL A O   1 
ATOM   678  C CB  . VAL A 1 90  ? -2.05900  15.17000 -11.37500 1.000 37.29963 ? 89  VAL A CB  1 
ATOM   679  C CG1 . VAL A 1 90  ? -2.43800  16.14100 -10.27500 1.000 28.79366 ? 89  VAL A CG1 1 
ATOM   680  C CG2 . VAL A 1 90  ? -0.69000  15.49600 -11.99100 1.000 41.08597 ? 89  VAL A CG2 1 
ATOM   681  N N   . SER A 1 91  ? -4.46100  13.41800 -10.25800 1.000 35.45477 ? 90  SER A N   1 
ATOM   682  C CA  . SER A 1 91  ? -5.54500  13.16400 -9.32300  1.000 37.24831 ? 90  SER A CA  1 
ATOM   683  C C   . SER A 1 91  ? -5.21100  11.98300 -8.43100  1.000 39.13941 ? 90  SER A C   1 
ATOM   684  O O   . SER A 1 91  ? -5.42000  12.02300 -7.21300  1.000 40.99985 ? 90  SER A O   1 
ATOM   685  C CB  . SER A 1 91  ? -6.84000  12.92000 -10.09600 1.000 39.97625 ? 90  SER A CB  1 
ATOM   686  O OG  . SER A 1 91  ? -7.97100  13.01200 -9.25700  1.000 45.16947 ? 90  SER A OG  1 
ATOM   687  N N   . VAL A 1 92  ? -4.65000  10.93300 -9.00700  1.000 40.04125 ? 91  VAL A N   1 
ATOM   688  C CA  . VAL A 1 92  ? -4.31900  9.79400  -8.15900  1.000 40.35677 ? 91  VAL A CA  1 
ATOM   689  C C   . VAL A 1 92  ? -3.00200  10.02400 -7.38900  1.000 35.26363 ? 91  VAL A C   1 
ATOM   690  O O   . VAL A 1 92  ? -2.94500  9.84500  -6.17000  1.000 34.88580 ? 91  VAL A O   1 
ATOM   691  C CB  . VAL A 1 92  ? -4.33400  8.49400  -8.98900  1.000 40.96003 ? 91  VAL A CB  1 
ATOM   692  C CG1 . VAL A 1 92  ? -3.08800  8.36000  -9.86300  1.000 36.68928 ? 91  VAL A CG1 1 
ATOM   693  C CG2 . VAL A 1 92  ? -4.51300  7.29600  -8.06300  1.000 42.28037 ? 91  VAL A CG2 1 
ATOM   694  N N   . ALA A 1 93  ? -1.92000  10.42900 -8.06200  1.000 36.89143 ? 92  ALA A N   1 
ATOM   695  C CA  . ALA A 1 93  ? -0.64500  10.58400 -7.36700  1.000 34.28658 ? 92  ALA A CA  1 
ATOM   696  C C   . ALA A 1 93  ? -0.76500  11.54200 -6.19200  1.000 43.43050 ? 92  ALA A C   1 
ATOM   697  O O   . ALA A 1 93  ? -0.33900  11.22700 -5.07000  1.000 51.01523 ? 92  ALA A O   1 
ATOM   698  C CB  . ALA A 1 93  ? 0.42800   11.06800 -8.33700  1.000 36.31611 ? 92  ALA A CB  1 
ATOM   699  N N   . ALA A 1 94  ? -1.36600  12.70900 -6.42600  1.000 32.66750 ? 93  ALA A N   1 
ATOM   700  C CA  . ALA A 1 94  ? -1.53900  13.71100 -5.38800  1.000 36.62184 ? 93  ALA A CA  1 
ATOM   701  C C   . ALA A 1 94  ? -2.73800  13.44800 -4.49100  1.000 34.08667 ? 93  ALA A C   1 
ATOM   702  O O   . ALA A 1 94  ? -2.91900  14.18100 -3.51700  1.000 41.18192 ? 93  ALA A O   1 
ATOM   703  C CB  . ALA A 1 94  ? -1.67100  15.09700 -6.01700  1.000 38.99956 ? 93  ALA A CB  1 
ATOM   704  N N   . GLU A 1 95  ? -3.59000  12.48000 -4.82300  1.000 39.28679 ? 94  GLU A N   1 
ATOM   705  C CA  . GLU A 1 95  ? -4.76300  12.15000 -4.00700  1.000 49.77480 ? 94  GLU A CA  1 
ATOM   706  C C   . GLU A 1 95  ? -5.75000  13.33700 -3.98200  1.000 48.65507 ? 94  GLU A C   1 
ATOM   707  O O   . GLU A 1 95  ? -6.26700  13.73900 -2.93400  1.000 51.74890 ? 94  GLU A O   1 
ATOM   708  C CB  . GLU A 1 95  ? -4.30300  11.73000 -2.59600  1.000 48.51472 ? 94  GLU A CB  1 
ATOM   709  C CG  . GLU A 1 95  ? -5.35900  11.35300 -1.57700  1.000 50.92408 ? 94  GLU A CG  1 
ATOM   710  C CD  . GLU A 1 95  ? -5.83300  9.93500  -1.71400  1.000 64.12362 ? 94  GLU A CD  1 
ATOM   711  O OE1 . GLU A 1 95  ? -6.39800  9.59200  -2.78200  1.000 62.18325 ? 94  GLU A OE1 1 
ATOM   712  O OE2 . GLU A 1 95  ? -5.65600  9.17100  -0.73500  1.000 70.55550 ? 94  GLU A OE2 1 
ATOM   713  N N   . ILE A 1 96  ? -6.03200  13.88400 -5.15900  1.000 39.11204 ? 95  ILE A N   1 
ATOM   714  C CA  . ILE A 1 96  ? -6.87700  15.06700 -5.27000  1.000 43.39895 ? 95  ILE A CA  1 
ATOM   715  C C   . ILE A 1 96  ? -8.00500  14.74700 -6.22800  1.000 41.51288 ? 95  ILE A C   1 
ATOM   716  O O   . ILE A 1 96  ? -7.83100  13.96800 -7.17000  1.000 41.41189 ? 95  ILE A O   1 
ATOM   717  C CB  . ILE A 1 96  ? -6.09300  16.29000 -5.79600  1.000 46.13453 ? 95  ILE A CB  1 
ATOM   718  C CG1 . ILE A 1 96  ? -4.93500  16.62300 -4.89000  1.000 44.12939 ? 95  ILE A CG1 1 
ATOM   719  C CG2 . ILE A 1 96  ? -6.97100  17.53400 -5.87600  1.000 38.63673 ? 95  ILE A CG2 1 
ATOM   720  C CD1 . ILE A 1 96  ? -4.17600  17.76100 -5.39700  1.000 32.88382 ? 95  ILE A CD1 1 
ATOM   721  N N   . ASP A 1 97  ? -9.14800  15.39100 -6.02000  1.000 37.61441 ? 96  ASP A N   1 
ATOM   722  C CA  . ASP A 1 97  ? -10.25500 15.19800 -6.94500  1.000 44.40591 ? 96  ASP A CA  1 
ATOM   723  C C   . ASP A 1 97  ? -9.95700  15.88400 -8.28200  1.000 40.85100 ? 96  ASP A C   1 
ATOM   724  O O   . ASP A 1 97  ? -9.24800  16.88900 -8.35000  1.000 40.83131 ? 96  ASP A O   1 
ATOM   725  C CB  . ASP A 1 97  ? -11.56100 15.73100 -6.36300  1.000 39.09367 ? 96  ASP A CB  1 
ATOM   726  C CG  . ASP A 1 97  ? -12.76200 15.31900 -7.18800  1.000 48.31326 ? 96  ASP A CG  1 
ATOM   727  O OD1 . ASP A 1 97  ? -13.16900 14.13300 -7.15200  1.000 50.52955 ? 96  ASP A OD1 1 
ATOM   728  O OD2 . ASP A 1 97  ? -13.31500 16.18700 -7.87700  1.000 42.91377 ? 96  ASP A OD2 1 
ATOM   729  N N   . ARG A 1 98  ? -10.51700 15.32500 -9.35700  1.000 47.98723 ? 97  ARG A N   1 
ATOM   730  C CA  . ARG A 1 98  ? -10.38100 15.93600 -10.67500 1.000 37.37743 ? 97  ARG A CA  1 
ATOM   731  C C   . ARG A 1 98  ? -10.88600 17.37300 -10.72600 1.000 38.06689 ? 97  ARG A C   1 
ATOM   732  O O   . ARG A 1 98  ? -10.35000 18.17200 -11.49000 1.000 45.58138 ? 97  ARG A O   1 
ATOM   733  C CB  . ARG A 1 98  ? -11.10500 15.09300 -11.72100 1.000 36.73865 ? 97  ARG A CB  1 
ATOM   734  C CG  . ARG A 1 98  ? -10.21900 14.00700 -12.28100 1.000 45.99586 ? 97  ARG A CG  1 
ATOM   735  C CD  . ARG A 1 98  ? -10.40600 12.69400 -11.53000 1.000 50.65945 ? 97  ARG A CD  1 
ATOM   736  N NE  . ARG A 1 98  ? -9.91200  11.57600 -12.31600 1.000 54.26625 ? 97  ARG A NE  1 
ATOM   737  C CZ  . ARG A 1 98  ? -9.46400  10.44600 -11.78500 1.000 50.51948 ? 97  ARG A CZ  1 
ATOM   738  N NH1 . ARG A 1 98  ? -9.65000  10.16200 -10.50100 1.000 50.01824 ? 97  ARG A NH1 1 
ATOM   739  N NH2 . ARG A 1 98  ? -8.74100  9.62400  -12.52800 1.000 44.76521 ? 97  ARG A NH2 1 
ATOM   740  N N   . LYS A 1 99  ? -11.93200 17.72600 -9.96700  1.000 43.98722 ? 98  LYS A N   1 
ATOM   741  C CA  . LYS A 1 99  ? -12.42400 19.10700 -10.03500 1.000 39.74289 ? 98  LYS A CA  1 
ATOM   742  C C   . LYS A 1 99  ? -11.43500 20.12000 -9.47700  1.000 36.45764 ? 98  LYS A C   1 
ATOM   743  O O   . LYS A 1 99  ? -11.63600 21.31600 -9.69400  1.000 39.74930 ? 98  LYS A O   1 
ATOM   744  C CB  . LYS A 1 99  ? -13.78500 19.31100 -9.34900  1.000 40.57681 ? 98  LYS A CB  1 
ATOM   745  C CG  . LYS A 1 99  ? -13.92300 19.01000 -7.86100  1.000 40.87972 ? 98  LYS A CG  1 
ATOM   746  C CD  . LYS A 1 99  ? -15.29700 18.35400 -7.63000  1.000 47.35034 ? 98  LYS A CD  1 
ATOM   747  C CE  . LYS A 1 99  ? -15.38100 17.58900 -6.31500  1.000 48.78940 ? 98  LYS A CE  1 
ATOM   748  N NZ  . LYS A 1 99  ? -15.88600 18.39700 -5.17700  1.000 49.22869 ? 98  LYS A NZ  1 
ATOM   749  N N   . HIS A 1 100 ? -10.39200 19.69600 -8.75700  1.000 35.65070 ? 99  HIS A N   1 
ATOM   750  C CA  . HIS A 1 100 ? -9.41400  20.64900 -8.26100  1.000 37.28530 ? 99  HIS A CA  1 
ATOM   751  C C   . HIS A 1 100 ? -8.24800  20.83500 -9.23200  1.000 40.36521 ? 99  HIS A C   1 
ATOM   752  O O   . HIS A 1 100 ? -7.29100  21.55000 -8.89300  1.000 40.62646 ? 99  HIS A O   1 
ATOM   753  C CB  . HIS A 1 100 ? -8.85500  20.21700 -6.90100  1.000 36.55949 ? 99  HIS A CB  1 
ATOM   754  C CG  . HIS A 1 100 ? -9.83800  20.28000 -5.76500  1.000 46.06149 ? 99  HIS A CG  1 
ATOM   755  N ND1 . HIS A 1 100 ? -10.52900 19.17200 -5.31000  1.000 42.71142 ? 99  HIS A ND1 1 
ATOM   756  C CD2 . HIS A 1 100 ? -10.23800 21.31400 -4.98700  1.000 42.15901 ? 99  HIS A CD2 1 
ATOM   757  C CE1 . HIS A 1 100 ? -11.30300 19.52200 -4.30000  1.000 38.65962 ? 99  HIS A CE1 1 
ATOM   758  N NE2 . HIS A 1 100 ? -11.15100 20.81600 -4.09000  1.000 40.45319 ? 99  HIS A NE2 1 
ATOM   759  N N   . ILE A 1 101 ? -8.31200  20.24000 -10.43100 1.000 30.64379 ? 100 ILE A N   1 
ATOM   760  C CA  . ILE A 1 101 ? -7.16800  20.18000 -11.33900 1.000 38.10339 ? 100 ILE A CA  1 
ATOM   761  C C   . ILE A 1 101 ? -7.44200  21.00700 -12.58500 1.000 35.92382 ? 100 ILE A C   1 
ATOM   762  O O   . ILE A 1 101 ? -8.41600  20.75500 -13.30800 1.000 32.71731 ? 100 ILE A O   1 
ATOM   763  C CB  . ILE A 1 101 ? -6.79400  18.74000 -11.72800 1.000 35.80878 ? 100 ILE A CB  1 
ATOM   764  C CG1 . ILE A 1 101 ? -6.54300  17.88500 -10.49900 1.000 30.18882 ? 100 ILE A CG1 1 
ATOM   765  C CG2 . ILE A 1 101 ? -5.57300  18.73300 -12.66400 1.000 31.94327 ? 100 ILE A CG2 1 
ATOM   766  C CD1 . ILE A 1 101 ? -6.49700  16.47400 -10.81600 1.000 31.89134 ? 100 ILE A CD1 1 
ATOM   767  N N   . TRP A 1 102 ? -6.55700  21.97500 -12.84200 1.000 31.95788 ? 101 TRP A N   1 
ATOM   768  C CA  . TRP A 1 102 ? -6.53800  22.78000 -14.05700 1.000 31.41457 ? 101 TRP A CA  1 
ATOM   769  C C   . TRP A 1 102 ? -5.23200  22.53100 -14.80000 1.000 33.62410 ? 101 TRP A C   1 
ATOM   770  O O   . TRP A 1 102 ? -4.16600  22.43600 -14.17000 1.000 24.10437 ? 101 TRP A O   1 
ATOM   771  C CB  . TRP A 1 102 ? -6.64500  24.26700 -13.73300 1.000 31.01643 ? 101 TRP A CB  1 
ATOM   772  C CG  . TRP A 1 102 ? -7.80500  24.63100 -12.89500 1.000 32.57551 ? 101 TRP A CG  1 
ATOM   773  C CD1 . TRP A 1 102 ? -8.26900  23.97700 -11.78600 1.000 32.31308 ? 101 TRP A CD1 1 
ATOM   774  C CD2 . TRP A 1 102 ? -8.65000  25.76400 -13.07600 1.000 33.91291 ? 101 TRP A CD2 1 
ATOM   775  N NE1 . TRP A 1 102 ? -9.36500  24.61600 -11.29400 1.000 36.59862 ? 101 TRP A NE1 1 
ATOM   776  C CE2 . TRP A 1 102 ? -9.61700  25.72600 -12.06100 1.000 34.97757 ? 101 TRP A CE2 1 
ATOM   777  C CE3 . TRP A 1 102 ? -8.68300  26.81400 -14.00300 1.000 36.99508 ? 101 TRP A CE3 1 
ATOM   778  C CZ2 . TRP A 1 102 ? -10.61400 26.70400 -11.94300 1.000 36.11954 ? 101 TRP A CZ2 1 
ATOM   779  C CZ3 . TRP A 1 102 ? -9.66700  27.77700 -13.88500 1.000 33.80930 ? 101 TRP A CZ3 1 
ATOM   780  C CH2 . TRP A 1 102 ? -10.62800 27.71100 -12.87000 1.000 30.90223 ? 101 TRP A CH2 1 
ATOM   781  N N   . VAL A 1 103 ? -5.31400  22.43400 -16.13400 1.000 29.66637 ? 102 VAL A N   1 
ATOM   782  C CA  . VAL A 1 103 ? -4.14700  22.12900 -16.96900 1.000 26.76795 ? 102 VAL A CA  1 
ATOM   783  C C   . VAL A 1 103 ? -4.19000  22.98100 -18.22400 1.000 24.27225 ? 102 VAL A C   1 
ATOM   784  O O   . VAL A 1 103 ? -5.17200  22.92800 -18.97300 1.000 26.34573 ? 102 VAL A O   1 
ATOM   785  C CB  . VAL A 1 103 ? -4.09600  20.64000 -17.35200 1.000 25.09398 ? 102 VAL A CB  1 
ATOM   786  C CG1 . VAL A 1 103 ? -3.08700  20.41400 -18.46700 1.000 23.07986 ? 102 VAL A CG1 1 
ATOM   787  C CG2 . VAL A 1 103 ? -3.78400  19.79700 -16.11700 1.000 26.56977 ? 102 VAL A CG2 1 
ATOM   788  N N   . TYR A 1 104 ? -3.12700  23.75100 -18.47000 1.000 26.41274 ? 103 TYR A N   1 
ATOM   789  C CA  . TYR A 1 104 ? -3.00400  24.63000 -19.64200 1.000 29.92524 ? 103 TYR A CA  1 
ATOM   790  C C   . TYR A 1 104 ? -1.66800  24.39000 -20.33000 1.000 28.10465 ? 103 TYR A C   1 
ATOM   791  O O   . TYR A 1 104 ? -0.61800  24.48500 -19.68900 1.000 32.20393 ? 103 TYR A O   1 
ATOM   792  C CB  . TYR A 1 104 ? -3.03500  26.11300 -19.27900 1.000 33.98632 ? 103 TYR A CB  1 
ATOM   793  C CG  . TYR A 1 104 ? -4.36100  26.71600 -18.96300 1.000 32.78626 ? 103 TYR A CG  1 
ATOM   794  C CD1 . TYR A 1 104 ? -5.48700  25.93600 -18.80900 1.000 27.20433 ? 103 TYR A CD1 1 
ATOM   795  C CD2 . TYR A 1 104 ? -4.48000  28.10300 -18.81300 1.000 35.37283 ? 103 TYR A CD2 1 
ATOM   796  C CE1 . TYR A 1 104 ? -6.72100  26.51300 -18.51600 1.000 31.35784 ? 103 TYR A CE1 1 
ATOM   797  C CE2 . TYR A 1 104 ? -5.69900  28.68300 -18.50600 1.000 33.85314 ? 103 TYR A CE2 1 
ATOM   798  C CZ  . TYR A 1 104 ? -6.81700  27.88300 -18.35100 1.000 26.49232 ? 103 TYR A CZ  1 
ATOM   799  O OH  . TYR A 1 104 ? -8.02500  28.46700 -18.06900 1.000 29.47497 ? 103 TYR A OH  1 
ATOM   800  N N   . PHE A 1 105 ? -1.69000  24.18000 -21.63500 1.000 25.26885 ? 104 PHE A N   1 
ATOM   801  C CA  . PHE A 1 105 ? -0.46600  23.99600 -22.39900 1.000 21.09548 ? 104 PHE A CA  1 
ATOM   802  C C   . PHE A 1 105 ? -0.21700  25.21700 -23.27900 1.000 28.51504 ? 104 PHE A C   1 
ATOM   803  O O   . PHE A 1 105 ? -1.06100  25.58400 -24.10700 1.000 25.10956 ? 104 PHE A O   1 
ATOM   804  C CB  . PHE A 1 105 ? -0.55900  22.72500 -23.24600 1.000 24.90245 ? 104 PHE A CB  1 
ATOM   805  C CG  . PHE A 1 105 ? -0.56800  21.42800 -22.43900 1.000 26.65640 ? 104 PHE A CG  1 
ATOM   806  C CD1 . PHE A 1 105 ? -0.19200  21.41500 -21.09500 1.000 26.55093 ? 104 PHE A CD1 1 
ATOM   807  C CD2 . PHE A 1 105 ? -0.94900  20.22900 -23.03300 1.000 21.94617 ? 104 PHE A CD2 1 
ATOM   808  C CE1 . PHE A 1 105 ? -0.18900  20.23200 -20.36000 1.000 26.55933 ? 104 PHE A CE1 1 
ATOM   809  C CE2 . PHE A 1 105 ? -0.96000  19.05100 -22.31700 1.000 20.50836 ? 104 PHE A CE2 1 
ATOM   810  C CZ  . PHE A 1 105 ? -0.57500  19.04000 -20.97400 1.000 22.62546 ? 104 PHE A CZ  1 
ATOM   811  N N   . GLY A 1 106 ? 0.96000   25.81100 -23.13900 1.000 29.46935 ? 105 GLY A N   1 
ATOM   812  C CA  . GLY A 1 106 ? 1.41500   26.86300 -24.02200 1.000 25.99506 ? 105 GLY A CA  1 
ATOM   813  C C   . GLY A 1 106 ? 2.59700   26.35500 -24.83600 1.000 23.98704 ? 105 GLY A C   1 
ATOM   814  O O   . GLY A 1 106 ? 3.26600   25.39600 -24.44100 1.000 26.34203 ? 105 GLY A O   1 
ATOM   815  N N   . GLU A 1 107 ? 2.70800   26.86200 -26.05600 1.000 19.31554 ? 106 GLU A N   1 
ATOM   816  C CA  . GLU A 1 107 ? 3.66500   26.35500 -27.03200 1.000 23.46777 ? 106 GLU A CA  1 
ATOM   817  C C   . GLU A 1 107 ? 4.50400   27.48200 -27.61100 1.000 23.10712 ? 106 GLU A C   1 
ATOM   818  O O   . GLU A 1 107 ? 3.98800   28.54600 -27.94000 1.000 23.70891 ? 106 GLU A O   1 
ATOM   819  C CB  . GLU A 1 107 ? 2.96700   25.61300 -28.20000 1.000 28.65488 ? 106 GLU A CB  1 
ATOM   820  C CG  . GLU A 1 107 ? 1.98400   24.53800 -27.79400 1.000 25.22115 ? 106 GLU A CG  1 
ATOM   821  C CD  . GLU A 1 107 ? 0.98700   24.24700 -28.87100 1.000 30.89477 ? 106 GLU A CD  1 
ATOM   822  O OE1 . GLU A 1 107 ? -0.05700  24.93100 -28.88400 1.000 40.76047 ? 106 GLU A OE1 1 
ATOM   823  O OE2 . GLU A 1 107 ? 1.22100   23.33900 -29.70100 1.000 35.30251 ? 106 GLU A OE2 1 
ATOM   824  N N   . MET A 1 108 ? 5.77900   27.22100 -27.81300 1.000 29.44626 ? 107 MET A N   1 
ATOM   825  C CA  . MET A 1 108 ? 6.66600   28.18100 -28.44400 1.000 28.07994 ? 107 MET A CA  1 
ATOM   826  C C   . MET A 1 108 ? 7.44900   27.47200 -29.54000 1.000 30.85908 ? 107 MET A C   1 
ATOM   827  O O   . MET A 1 108 ? 7.51900   26.24100 -29.55400 1.000 33.31872 ? 107 MET A O   1 
ATOM   828  C CB  . MET A 1 108 ? 7.61700   28.82000 -27.42100 1.000 25.96856 ? 107 MET A CB  1 
ATOM   829  C CG  . MET A 1 108 ? 6.91500   29.55400 -26.29400 1.000 24.28717 ? 107 MET A CG  1 
ATOM   830  S SD  . MET A 1 108 ? 7.58700   29.22000 -24.64100 1.000 37.10678 ? 107 MET A SD  1 
ATOM   831  C CE  . MET A 1 108 ? 6.84200   27.60400 -24.30000 1.000 29.10342 ? 107 MET A CE  1 
ATOM   832  N N   . PRO A 1 109 ? 8.01600   28.21700 -30.48200 1.000 27.93549 ? 108 PRO A N   1 
ATOM   833  C CA  . PRO A 1 109 ? 8.92500   27.58600 -31.44000 1.000 31.43801 ? 108 PRO A CA  1 
ATOM   834  C C   . PRO A 1 109 ? 10.14100  27.01400 -30.73600 1.000 34.41932 ? 108 PRO A C   1 
ATOM   835  O O   . PRO A 1 109 ? 10.70300  27.63500 -29.83100 1.000 33.78698 ? 108 PRO A O   1 
ATOM   836  C CB  . PRO A 1 109 ? 9.30700   28.73600 -32.37800 1.000 28.19690 ? 108 PRO A CB  1 
ATOM   837  C CG  . PRO A 1 109 ? 8.17900   29.63400 -32.30800 1.000 29.18593 ? 108 PRO A CG  1 
ATOM   838  C CD  . PRO A 1 109 ? 7.71600   29.59600 -30.86800 1.000 29.88578 ? 108 PRO A CD  1 
ATOM   839  N N   . ALA A 1 110 ? 10.54300  25.81800 -31.17800 1.000 33.12634 ? 109 ALA A N   1 
ATOM   840  C CA  . ALA A 1 110 ? 11.70000  25.15100 -30.60800 1.000 32.58666 ? 109 ALA A CA  1 
ATOM   841  C C   . ALA A 1 110 ? 12.94500  26.02200 -30.69100 1.000 34.29318 ? 109 ALA A C   1 
ATOM   842  O O   . ALA A 1 110 ? 13.81200  25.92300 -29.80800 1.000 35.72329 ? 109 ALA A O   1 
ATOM   843  C CB  . ALA A 1 110 ? 11.94500  23.81500 -31.30100 1.000 37.08087 ? 109 ALA A CB  1 
ATOM   844  N N   . GLN A 1 111 ? 13.06500  26.88500 -31.71800 1.000 31.06813 ? 110 GLN A N   1 
ATOM   845  C CA  . GLN A 1 111 ? 14.24300  27.77600 -31.74400 1.000 38.60845 ? 110 GLN A CA  1 
ATOM   846  C C   . GLN A 1 111 ? 14.31100  28.84300 -30.64900 1.000 32.71731 ? 110 GLN A C   1 
ATOM   847  O O   . GLN A 1 111 ? 15.33200  29.52100 -30.57900 1.000 30.47637 ? 110 GLN A O   1 
ATOM   848  C CB  . GLN A 1 111 ? 14.44600  28.68200 -32.97700 1.000 43.64352 ? 110 GLN A CB  1 
ATOM   849  C CG  . GLN A 1 111 ? 15.26100  28.32300 -34.18900 1.000 51.41914 ? 110 GLN A CG  1 
ATOM   850  C CD  . GLN A 1 111 ? 14.53700  28.39500 -35.51900 1.000 59.19200 ? 110 GLN A CD  1 
ATOM   851  O OE1 . GLN A 1 111 ? 13.71300  29.28100 -35.73000 1.000 56.04430 ? 110 GLN A OE1 1 
ATOM   852  N NE2 . GLN A 1 111 ? 15.02000  27.62400 -36.48300 1.000 62.88514 ? 110 GLN A NE2 1 
ATOM   853  N N   . GLN A 1 112 ? 13.27900  29.07500 -29.84700 1.000 35.44009 ? 111 GLN A N   1 
ATOM   854  C CA  . GLN A 1 112 ? 13.37200  30.07700 -28.78500 1.000 34.72767 ? 111 GLN A CA  1 
ATOM   855  C C   . GLN A 1 112 ? 13.23700  29.41900 -27.42100 1.000 38.02457 ? 111 GLN A C   1 
ATOM   856  O O   . GLN A 1 112 ? 12.71900  30.01900 -26.46700 1.000 30.47768 ? 111 GLN A O   1 
ATOM   857  C CB  . GLN A 1 112 ? 12.34600  31.19600 -28.97100 1.000 26.78971 ? 111 GLN A CB  1 
ATOM   858  C CG  . GLN A 1 112 ? 10.91600  30.79300 -29.04400 1.000 27.43344 ? 111 GLN A CG  1 
ATOM   859  C CD  . GLN A 1 112 ? 10.09500  31.80300 -29.83000 1.000 26.97772 ? 111 GLN A CD  1 
ATOM   860  O OE1 . GLN A 1 112 ? 10.29200  31.98200 -31.03500 1.000 24.47941 ? 111 GLN A OE1 1 
ATOM   861  N NE2 . GLN A 1 112 ? 9.16700   32.46000 -29.15300 1.000 24.55389 ? 111 GLN A NE2 1 
ATOM   862  N N   . MET A 1 113 ? 13.72600  28.18100 -27.33800 1.000 33.16805 ? 112 MET A N   1 
ATOM   863  C CA  . MET A 1 113 ? 13.59600  27.33900 -26.16800 1.000 32.00755 ? 112 MET A CA  1 
ATOM   864  C C   . MET A 1 113 ? 14.91400  26.65000 -25.82900 1.000 32.40562 ? 112 MET A C   1 
ATOM   865  O O   . MET A 1 113 ? 15.50000  25.96200 -26.67000 1.000 32.59293 ? 112 MET A O   1 
ATOM   866  C CB  . MET A 1 113 ? 12.49800  26.31400 -26.42000 1.000 29.13704 ? 112 MET A CB  1 
ATOM   867  C CG  . MET A 1 113 ? 11.12400  26.87800 -26.25800 1.000 26.08428 ? 112 MET A CG  1 
ATOM   868  S SD  . MET A 1 113 ? 9.87000   25.70300 -26.78600 1.000 28.92447 ? 112 MET A SD  1 
ATOM   869  C CE  . MET A 1 113 ? 9.30400   25.20800 -25.13600 1.000 27.22394 ? 112 MET A CE  1 
ATOM   870  N N   . VAL A 1 114 ? 15.35900  26.80700 -24.58900 1.000 30.91772 ? 113 VAL A N   1 
ATOM   871  C CA  . VAL A 1 114 ? 16.60800  26.22300 -24.11600 1.000 31.05881 ? 113 VAL A CA  1 
ATOM   872  C C   . VAL A 1 114 ? 16.32900  25.30300 -22.92400 1.000 32.07892 ? 113 VAL A C   1 
ATOM   873  O O   . VAL A 1 114 ? 15.68600  25.71400 -21.95300 1.000 31.86412 ? 113 VAL A O   1 
ATOM   874  C CB  . VAL A 1 114 ? 17.59500  27.34400 -23.72200 1.000 31.01321 ? 113 VAL A CB  1 
ATOM   875  C CG1 . VAL A 1 114 ? 18.95400  26.81900 -23.40600 1.000 24.88911 ? 113 VAL A CG1 1 
ATOM   876  C CG2 . VAL A 1 114 ? 17.66200  28.41800 -24.81300 1.000 29.10901 ? 113 VAL A CG2 1 
ATOM   877  N N   . ASN A 1 115 ? 16.91400  24.10500 -22.94100 1.000 37.83999 ? 114 ASN A N   1 
ATOM   878  C CA  . ASN A 1 115 ? 17.00500  23.27800 -21.74400 1.000 33.18243 ? 114 ASN A CA  1 
ATOM   879  C C   . ASN A 1 115 ? 18.47100  22.96000 -21.56300 1.000 33.37729 ? 114 ASN A C   1 
ATOM   880  O O   . ASN A 1 115 ? 19.20700  22.83100 -22.55000 1.000 30.06787 ? 114 ASN A O   1 
ATOM   881  C CB  . ASN A 1 115 ? 16.25200  21.89500 -21.74100 1.000 31.08181 ? 114 ASN A CB  1 
ATOM   882  C CG  . ASN A 1 115 ? 14.83700  21.92400 -22.30500 1.000 40.99500 ? 114 ASN A CG  1 
ATOM   883  O OD1 . ASN A 1 115 ? 14.45300  21.02300 -23.07500 1.000 40.13536 ? 114 ASN A OD1 1 
ATOM   884  N ND2 . ASN A 1 115 ? 14.04600  22.93700 -21.92400 1.000 35.40742 ? 114 ASN A ND2 1 
ATOM   885  N N   . TYR A 1 116 ? 18.89100  22.87000 -20.29500 1.000 34.96104 ? 115 TYR A N   1 
ATOM   886  C CA  . TYR A 1 116 ? 20.27600  22.54900 -19.94500 1.000 34.25348 ? 115 TYR A CA  1 
ATOM   887  C C   . TYR A 1 116 ? 21.27700  23.43200 -20.67200 1.000 37.54687 ? 115 TYR A C   1 
ATOM   888  O O   . TYR A 1 116 ? 22.34400  22.96000 -21.07500 1.000 39.26892 ? 115 TYR A O   1 
ATOM   889  C CB  . TYR A 1 116 ? 20.58900  21.08300 -20.25200 1.000 36.82620 ? 115 TYR A CB  1 
ATOM   890  C CG  . TYR A 1 116 ? 19.77000  20.09600 -19.45500 1.000 37.48837 ? 115 TYR A CG  1 
ATOM   891  C CD1 . TYR A 1 116 ? 18.50500  19.70000 -19.87600 1.000 35.05905 ? 115 TYR A CD1 1 
ATOM   892  C CD2 . TYR A 1 116 ? 20.28900  19.52700 -18.29100 1.000 38.28841 ? 115 TYR A CD2 1 
ATOM   893  C CE1 . TYR A 1 116 ? 17.76400  18.78400 -19.13400 1.000 43.08616 ? 115 TYR A CE1 1 
ATOM   894  C CE2 . TYR A 1 116 ? 19.56200  18.63100 -17.54200 1.000 39.88537 ? 115 TYR A CE2 1 
ATOM   895  C CZ  . TYR A 1 116 ? 18.30100  18.26300 -17.95600 1.000 42.86298 ? 115 TYR A CZ  1 
ATOM   896  O OH  . TYR A 1 116 ? 17.59400  17.35900 -17.19500 1.000 40.57727 ? 115 TYR A OH  1 
ATOM   897  N N   . GLY A 1 117 ? 20.91100  24.69300 -20.91300 1.000 37.55631 ? 116 GLY A N   1 
ATOM   898  C CA  . GLY A 1 117 ? 21.79400  25.60200 -21.60400 1.000 23.46108 ? 116 GLY A CA  1 
ATOM   899  C C   . GLY A 1 117 ? 21.92800  25.36300 -23.08200 1.000 26.31161 ? 116 GLY A C   1 
ATOM   900  O O   . GLY A 1 117 ? 22.76100  26.00900 -23.70400 1.000 29.25832 ? 116 GLY A O   1 
ATOM   901  N N   . ARG A 1 118 ? 21.11500  24.48200 -23.67900 1.000 33.16959 ? 117 ARG A N   1 
ATOM   902  C CA  . ARG A 1 118 ? 21.19700  24.16500 -25.10700 1.000 33.63558 ? 117 ARG A CA  1 
ATOM   903  C C   . ARG A 1 118 ? 19.83700  24.33300 -25.79100 1.000 30.05041 ? 117 ARG A C   1 
ATOM   904  O O   . ARG A 1 118 ? 18.77500  24.11800 -25.18700 1.000 32.11346 ? 117 ARG A O   1 
ATOM   905  C CB  . ARG A 1 118 ? 21.73800  22.72400 -25.34600 1.000 31.38835 ? 117 ARG A CB  1 
ATOM   906  C CG  . ARG A 1 118 ? 23.20400  22.51500 -24.91300 1.000 31.93539 ? 117 ARG A CG  1 
ATOM   907  C CD  . ARG A 1 118 ? 24.18500  23.18000 -25.88100 1.000 33.12105 ? 117 ARG A CD  1 
ATOM   908  N NE  . ARG A 1 118 ? 24.72000  22.26400 -26.88400 1.000 39.95951 ? 117 ARG A NE  1 
ATOM   909  C CZ  . ARG A 1 118 ? 24.09600  21.94800 -28.01400 1.000 46.39994 ? 117 ARG A CZ  1 
ATOM   910  N NH1 . ARG A 1 118 ? 22.89700  22.44300 -28.30400 1.000 42.72963 ? 117 ARG A NH1 1 
ATOM   911  N NH2 . ARG A 1 118 ? 24.70300  21.14600 -28.89500 1.000 40.51171 ? 117 ARG A NH2 1 
ATOM   912  N N   . PHE A 1 119 ? 19.88300  24.74900 -27.05400 1.000 24.45745 ? 118 PHE A N   1 
ATOM   913  C CA  . PHE A 1 119 ? 18.67300  24.91800 -27.84900 1.000 29.35093 ? 118 PHE A CA  1 
ATOM   914  C C   . PHE A 1 119 ? 17.97100  23.60200 -28.15400 1.000 36.46007 ? 118 PHE A C   1 
ATOM   915  O O   . PHE A 1 119 ? 18.59500  22.63300 -28.59200 1.000 40.41014 ? 118 PHE A O   1 
ATOM   916  C CB  . PHE A 1 119 ? 18.99300  25.64900 -29.13500 1.000 26.65302 ? 118 PHE A CB  1 
ATOM   917  C CG  . PHE A 1 119 ? 18.91400  27.12800 -28.98300 1.000 28.71640 ? 118 PHE A CG  1 
ATOM   918  C CD1 . PHE A 1 119 ? 17.67800  27.75500 -28.94500 1.000 26.67054 ? 118 PHE A CD1 1 
ATOM   919  C CD2 . PHE A 1 119 ? 20.06000  27.88000 -28.81700 1.000 25.41985 ? 118 PHE A CD2 1 
ATOM   920  C CE1 . PHE A 1 119 ? 17.58100  29.09500 -28.77200 1.000 28.99318 ? 118 PHE A CE1 1 
ATOM   921  C CE2 . PHE A 1 119 ? 19.98000  29.23600 -28.65600 1.000 33.35754 ? 118 PHE A CE2 1 
ATOM   922  C CZ  . PHE A 1 119 ? 18.72400  29.85600 -28.63700 1.000 35.48858 ? 118 PHE A CZ  1 
ATOM   923  N N   . LEU A 1 120 ? 16.66200  23.57600 -27.92200 1.000 31.56899 ? 119 LEU A N   1 
ATOM   924  C CA  . LEU A 1 120 ? 15.89200  22.38500 -28.18700 1.000 35.20918 ? 119 LEU A CA  1 
ATOM   925  C C   . LEU A 1 120 ? 15.82800  22.14500 -29.68300 1.000 39.27540 ? 119 LEU A C   1 
ATOM   926  O O   . LEU A 1 120 ? 16.00800  23.06300 -30.47900 1.000 40.25615 ? 119 LEU A O   1 
ATOM   927  C CB  . LEU A 1 120 ? 14.47300  22.49400 -27.63200 1.000 31.41034 ? 119 LEU A CB  1 
ATOM   928  C CG  . LEU A 1 120 ? 14.32600  22.02500 -26.18000 1.000 34.87510 ? 119 LEU A CG  1 
ATOM   929  C CD1 . LEU A 1 120 ? 15.04800  22.99800 -25.29900 1.000 36.55526 ? 119 LEU A CD1 1 
ATOM   930  C CD2 . LEU A 1 120 ? 12.88800  21.90500 -25.73800 1.000 39.97550 ? 119 LEU A CD2 1 
ATOM   931  N N   . PRO A 1 121 ? 15.60200  20.91500 -30.07600 1.000 47.84587 ? 120 PRO A N   1 
ATOM   932  C CA  . PRO A 1 121 ? 15.32900  20.62200 -31.47900 1.000 44.71772 ? 120 PRO A CA  1 
ATOM   933  C C   . PRO A 1 121 ? 13.85300  20.65100 -31.77300 1.000 45.08987 ? 120 PRO A C   1 
ATOM   934  O O   . PRO A 1 121 ? 13.03800  20.92400 -30.89100 1.000 47.35107 ? 120 PRO A O   1 
ATOM   935  C CB  . PRO A 1 121 ? 15.85700  19.20500 -31.62700 1.000 54.07668 ? 120 PRO A CB  1 
ATOM   936  C CG  . PRO A 1 121 ? 15.63100  18.59400 -30.26700 1.000 52.32237 ? 120 PRO A CG  1 
ATOM   937  C CD  . PRO A 1 121 ? 15.63300  19.69800 -29.25400 1.000 46.00032 ? 120 PRO A CD  1 
ATOM   938  N N   . GLN A 1 122 ? 13.50400  20.24100 -32.97800 1.000 49.29284 ? 121 GLN A N   1 
ATOM   939  C CA  . GLN A 1 122 ? 12.11300  20.01900 -33.29800 1.000 55.70024 ? 121 GLN A CA  1 
ATOM   940  C C   . GLN A 1 122 ? 11.73900  18.64900 -32.73100 1.000 58.44992 ? 121 GLN A C   1 
ATOM   941  O O   . GLN A 1 122 ? 12.62000  17.83000 -32.45900 1.000 51.52895 ? 121 GLN A O   1 
ATOM   942  C CB  . GLN A 1 122 ? 11.93800  20.05500 -34.81500 1.000 51.77386 ? 121 GLN A CB  1 
ATOM   943  C CG  . GLN A 1 122 ? 11.70400  21.43100 -35.49000 1.000 55.96997 ? 121 GLN A CG  1 
ATOM   944  C CD  . GLN A 1 122 ? 10.76100  22.36400 -34.74200 1.000 58.55328 ? 121 GLN A CD  1 
ATOM   945  O OE1 . GLN A 1 122 ? 9.79000   21.91700 -34.13100 1.000 67.65613 ? 121 GLN A OE1 1 
ATOM   946  N NE2 . GLN A 1 122 ? 11.01300  23.66700 -34.83000 1.000 50.96689 ? 121 GLN A NE2 1 
ATOM   947  N N   . PRO A 1 123 ? 10.45800  18.37800 -32.47900 1.000 63.32249 ? 122 PRO A N   1 
ATOM   948  C CA  . PRO A 1 123 ? 10.11100  17.06700 -31.88500 1.000 63.21916 ? 122 PRO A CA  1 
ATOM   949  C C   . PRO A 1 123 ? 10.58900  15.88200 -32.71500 1.000 65.07223 ? 122 PRO A C   1 
ATOM   950  O O   . PRO A 1 123 ? 10.75400  14.78300 -32.16300 1.000 67.41176 ? 122 PRO A O   1 
ATOM   951  C CB  . PRO A 1 123 ? 8.57700   17.09700 -31.74700 1.000 55.33192 ? 122 PRO A CB  1 
ATOM   952  C CG  . PRO A 1 123 ? 8.10700   18.36100 -32.38000 1.000 60.87950 ? 122 PRO A CG  1 
ATOM   953  C CD  . PRO A 1 123 ? 9.27800   19.14700 -32.92000 1.000 59.65965 ? 122 PRO A CD  1 
ATOM   954  N N   . GLY A 1 124 ? 10.83600  16.07300 -34.01200 1.000 62.79404 ? 123 GLY A N   1 
ATOM   955  C CA  . GLY A 1 124 ? 11.50400  15.06200 -34.81200 1.000 69.60175 ? 123 GLY A CA  1 
ATOM   956  C C   . GLY A 1 124 ? 13.01200  15.26300 -34.82800 1.000 73.51086 ? 123 GLY A C   1 
ATOM   957  O O   . GLY A 1 124 ? 13.55800  15.75900 -35.83000 1.000 65.39422 ? 123 GLY A O   1 
ATOM   958  N N   . HIS A 1 125 ? 13.69600  14.86600 -33.74000 1.000 62.35018 ? 124 HIS A N   1 
ATOM   959  C CA  . HIS A 1 125 ? 15.09900  15.22100 -33.56300 1.000 62.44085 ? 124 HIS A CA  1 
ATOM   960  C C   . HIS A 1 125 ? 15.70500  14.77900 -32.22700 1.000 57.02365 ? 124 HIS A C   1 
ATOM   961  O O   . HIS A 1 125 ? 16.93100  14.76400 -32.09800 1.000 60.46536 ? 124 HIS A O   1 
ATOM   962  C CB  . HIS A 1 125 ? 15.22600  16.74000 -33.75000 1.000 66.45392 ? 124 HIS A CB  1 
ATOM   963  C CG  . HIS A 1 125 ? 16.59800  17.21500 -34.09800 1.000 69.88737 ? 124 HIS A CG  1 
ATOM   964  N ND1 . HIS A 1 125 ? 17.72900  16.46500 -33.86300 1.000 73.34307 ? 124 HIS A ND1 1 
ATOM   965  C CD2 . HIS A 1 125 ? 17.01700  18.35300 -34.70200 1.000 70.89600 ? 124 HIS A CD2 1 
ATOM   966  C CE1 . HIS A 1 125 ? 18.79000  17.13300 -34.27600 1.000 71.64225 ? 124 HIS A CE1 1 
ATOM   967  N NE2 . HIS A 1 125 ? 18.38500  18.27700 -34.80200 1.000 71.44083 ? 124 HIS A NE2 1 
ATOM   968  N N   . GLU A 1 126 ? 14.88500  14.37400 -31.25000 1.000 56.11525 ? 125 GLU A N   1 
ATOM   969  C CA  . GLU A 1 126 ? 15.31400  14.28800 -29.85400 1.000 54.59042 ? 125 GLU A CA  1 
ATOM   970  C C   . GLU A 1 126 ? 16.48200  13.33500 -29.61400 1.000 53.47720 ? 125 GLU A C   1 
ATOM   971  O O   . GLU A 1 126 ? 17.41800  13.69200 -28.88500 1.000 49.14855 ? 125 GLU A O   1 
ATOM   972  C CB  . GLU A 1 126 ? 14.10400  13.89000 -29.01500 1.000 58.81475 ? 125 GLU A CB  1 
ATOM   973  C CG  . GLU A 1 126 ? 12.88600  14.68000 -29.45500 1.000 60.53811 ? 125 GLU A CG  1 
ATOM   974  C CD  . GLU A 1 126 ? 11.99800  15.04900 -28.31200 1.000 67.37608 ? 125 GLU A CD  1 
ATOM   975  O OE1 . GLU A 1 126 ? 12.55600  15.40400 -27.24300 1.000 72.91386 ? 125 GLU A OE1 1 
ATOM   976  O OE2 . GLU A 1 126 ? 10.74900  15.03600 -28.49100 1.000 64.40436 ? 125 GLU A OE2 1 
ATOM   977  N N   . GLY A 1 127 ? 16.48100  12.18500 -30.27100 1.000 58.10096 ? 126 GLY A N   1 
ATOM   978  C CA  . GLY A 1 127 ? 17.58500  11.26400 -30.20300 1.000 48.99939 ? 126 GLY A CA  1 
ATOM   979  C C   . GLY A 1 127 ? 18.79500  11.71700 -30.99300 1.000 60.75166 ? 126 GLY A C   1 
ATOM   980  O O   . GLY A 1 127 ? 19.90500  11.74800 -30.43800 1.000 62.40251 ? 126 GLY A O   1 
ATOM   981  N N   . GLU A 1 128 ? 18.63200  12.02500 -32.28500 1.000 53.83562 ? 127 GLU A N   1 
ATOM   982  C CA  . GLU A 1 128 ? 19.74700  12.62900 -33.00800 1.000 60.59099 ? 127 GLU A CA  1 
ATOM   983  C C   . GLU A 1 128 ? 20.23700  13.88000 -32.28600 1.000 60.47535 ? 127 GLU A C   1 
ATOM   984  O O   . GLU A 1 128 ? 21.44200  14.10900 -32.19200 1.000 63.68928 ? 127 GLU A O   1 
ATOM   985  C CB  . GLU A 1 128 ? 19.41000  12.81000 -34.50400 1.000 65.69574 ? 127 GLU A CB  1 
ATOM   986  C CG  . GLU A 1 128 ? 18.34300  13.77200 -34.97000 1.000 68.14151 ? 127 GLU A CG  1 
ATOM   987  C CD  . GLU A 1 128 ? 18.66900  14.35100 -36.35300 1.000 73.64114 ? 127 GLU A CD  1 
ATOM   988  O OE1 . GLU A 1 128 ? 19.64600  15.13200 -36.45100 1.000 77.80873 ? 127 GLU A OE1 1 
ATOM   989  O OE2 . GLU A 1 128 ? 17.96500  14.00600 -37.33400 1.000 68.97876 ? 127 GLU A OE2 1 
ATOM   990  N N   . TRP A 1 129 ? 19.32400  14.70400 -31.77000 1.000 52.49976 ? 128 TRP A N   1 
ATOM   991  C CA  . TRP A 1 129 ? 19.73000  15.87400 -30.99300 1.000 49.59971 ? 128 TRP A CA  1 
ATOM   992  C C   . TRP A 1 129 ? 20.65200  15.50100 -29.83900 1.000 47.69732 ? 128 TRP A C   1 
ATOM   993  O O   . TRP A 1 129 ? 21.67400  16.14800 -29.61200 1.000 43.62978 ? 128 TRP A O   1 
ATOM   994  C CB  . TRP A 1 129 ? 18.48800  16.60100 -30.45800 1.000 53.35060 ? 128 TRP A CB  1 
ATOM   995  C CG  . TRP A 1 129 ? 18.73600  17.76400 -29.54300 1.000 47.59191 ? 128 TRP A CG  1 
ATOM   996  C CD1 . TRP A 1 129 ? 19.12300  19.01700 -29.91100 1.000 40.58483 ? 128 TRP A CD1 1 
ATOM   997  C CD2 . TRP A 1 129 ? 18.55600  17.79800 -28.11900 1.000 43.72605 ? 128 TRP A CD2 1 
ATOM   998  N NE1 . TRP A 1 129 ? 19.22600  19.81900 -28.80500 1.000 43.83715 ? 128 TRP A NE1 1 
ATOM   999  C CE2 . TRP A 1 129 ? 18.87700  19.09900 -27.69300 1.000 46.58554 ? 128 TRP A CE2 1 
ATOM   1000 C CE3 . TRP A 1 129 ? 18.16100  16.85500 -27.16300 1.000 48.04060 ? 128 TRP A CE3 1 
ATOM   1001 C CZ2 . TRP A 1 129 ? 18.81400  19.48600 -26.35300 1.000 41.75268 ? 128 TRP A CZ2 1 
ATOM   1002 C CZ3 . TRP A 1 129 ? 18.09800  17.24400 -25.82700 1.000 46.17691 ? 128 TRP A CZ3 1 
ATOM   1003 C CH2 . TRP A 1 129 ? 18.43000  18.54800 -25.43900 1.000 42.54943 ? 128 TRP A CH2 1 
ATOM   1004 N N   . PHE A 1 130 ? 20.29400  14.46400 -29.08400 1.000 50.95001 ? 129 PHE A N   1 
ATOM   1005 C CA  . PHE A 1 130 ? 21.01400  14.17300 -27.84900 1.000 52.62978 ? 129 PHE A CA  1 
ATOM   1006 C C   . PHE A 1 130 ? 22.49500  13.85500 -28.07700 1.000 54.77962 ? 129 PHE A C   1 
ATOM   1007 O O   . PHE A 1 130 ? 23.37700  14.53900 -27.54100 1.000 57.45767 ? 129 PHE A O   1 
ATOM   1008 C CB  . PHE A 1 130 ? 20.32500  13.02700 -27.11000 1.000 48.06301 ? 129 PHE A CB  1 
ATOM   1009 C CG  . PHE A 1 130 ? 20.92000  12.75500 -25.76800 1.000 46.55374 ? 129 PHE A CG  1 
ATOM   1010 C CD1 . PHE A 1 130 ? 20.72700  13.63400 -24.72200 1.000 45.23098 ? 129 PHE A CD1 1 
ATOM   1011 C CD2 . PHE A 1 130 ? 21.70400  11.64200 -25.55600 1.000 42.37095 ? 129 PHE A CD2 1 
ATOM   1012 C CE1 . PHE A 1 130 ? 21.28700  13.38600 -23.47700 1.000 42.82120 ? 129 PHE A CE1 1 
ATOM   1013 C CE2 . PHE A 1 130 ? 22.26300  11.40600 -24.31300 1.000 46.15776 ? 129 PHE A CE2 1 
ATOM   1014 C CZ  . PHE A 1 130 ? 22.05400  12.27400 -23.27900 1.000 34.22234 ? 129 PHE A CZ  1 
ATOM   1015 N N   . ASP A 1 131 ? 22.79300  12.83800 -28.89000 1.000 50.43259 ? 130 ASP A N   1 
ATOM   1016 C CA  . ASP A 1 131 ? 24.17000  12.35600 -29.04100 1.000 59.03543 ? 130 ASP A CA  1 
ATOM   1017 C C   . ASP A 1 131 ? 25.19600  13.45200 -29.34500 1.000 59.65272 ? 130 ASP A C   1 
ATOM   1018 O O   . ASP A 1 131 ? 26.36100  13.31000 -28.95500 1.000 62.43910 ? 130 ASP A O   1 
ATOM   1019 C CB  . ASP A 1 131 ? 24.26500  11.27400 -30.12100 1.000 59.55276 ? 130 ASP A CB  1 
ATOM   1020 C CG  . ASP A 1 131 ? 23.05000  10.37800 -30.15800 1.000 53.60309 ? 130 ASP A CG  1 
ATOM   1021 O OD1 . ASP A 1 131 ? 22.41100  10.19100 -29.10500 1.000 62.18312 ? 130 ASP A OD1 1 
ATOM   1022 O OD2 . ASP A 1 131 ? 22.69100  9.90600  -31.25000 1.000 48.66539 ? 130 ASP A OD2 1 
ATOM   1023 N N   . ASN A 1 132 ? 24.81100  14.52000 -30.03700 1.000 55.15373 ? 131 ASN A N   1 
ATOM   1024 C CA  . ASN A 1 132 ? 25.72900  15.61000 -30.35000 1.000 53.72014 ? 131 ASN A CA  1 
ATOM   1025 C C   . ASN A 1 132 ? 25.86600  16.65600 -29.26000 1.000 50.95636 ? 131 ASN A C   1 
ATOM   1026 O O   . ASN A 1 132 ? 26.55300  17.65400 -29.48600 1.000 44.09641 ? 131 ASN A O   1 
ATOM   1027 C CB  . ASN A 1 132 ? 25.29900  16.30100 -31.63500 1.000 59.28493 ? 131 ASN A CB  1 
ATOM   1028 C CG  . ASN A 1 132 ? 24.84300  15.32000 -32.66300 1.000 63.90859 ? 131 ASN A CG  1 
ATOM   1029 O OD1 . ASN A 1 132 ? 23.99100  14.48300 -32.37900 1.000 62.70309 ? 131 ASN A OD1 1 
ATOM   1030 N ND2 . ASN A 1 132 ? 25.40800  15.39600 -33.86100 1.000 69.91062 ? 131 ASN A ND2 1 
ATOM   1031 N N   . LEU A 1 133 ? 25.24500  16.46900 -28.10000 1.000 53.37219 ? 132 LEU A N   1 
ATOM   1032 C CA  . LEU A 1 133 ? 25.58600  17.33300 -26.98000 1.000 48.34130 ? 132 LEU A CA  1 
ATOM   1033 C C   . LEU A 1 133 ? 26.91000  16.86700 -26.39300 1.000 46.45559 ? 132 LEU A C   1 
ATOM   1034 O O   . LEU A 1 133 ? 27.33400  15.72700 -26.58700 1.000 48.81790 ? 132 LEU A O   1 
ATOM   1035 C CB  . LEU A 1 133 ? 24.51600  17.27800 -25.89000 1.000 40.11667 ? 132 LEU A CB  1 
ATOM   1036 C CG  . LEU A 1 133 ? 23.07600  17.49100 -26.34500 1.000 44.50699 ? 132 LEU A CG  1 
ATOM   1037 C CD1 . LEU A 1 133 ? 22.15900  17.32600 -25.17000 1.000 43.89634 ? 132 LEU A CD1 1 
ATOM   1038 C CD2 . LEU A 1 133 ? 22.87100  18.85700 -26.99200 1.000 42.34947 ? 132 LEU A CD2 1 
ATOM   1039 N N   . SER A 1 134 ? 27.60100  17.78300 -25.72100 1.000 51.87825 ? 133 SER A N   1 
ATOM   1040 C CA  . SER A 1 134 ? 28.89700  17.45200 -25.14500 1.000 46.87369 ? 133 SER A CA  1 
ATOM   1041 C C   . SER A 1 134 ? 28.75800  16.20300 -24.27900 1.000 47.79632 ? 133 SER A C   1 
ATOM   1042 O O   . SER A 1 134 ? 27.64600  15.84800 -23.86700 1.000 48.53015 ? 133 SER A O   1 
ATOM   1043 C CB  . SER A 1 134 ? 29.42500  18.60800 -24.30500 1.000 48.90009 ? 133 SER A CB  1 
ATOM   1044 O OG  . SER A 1 134 ? 28.63600  18.74200 -23.14200 1.000 49.20037 ? 133 SER A OG  1 
ATOM   1045 N N   . SER A 1 135 ? 29.85700  15.50500 -24.01200 1.000 46.10108 ? 134 SER A N   1 
ATOM   1046 C CA  . SER A 1 135 ? 29.71300  14.28900 -23.22700 1.000 46.21905 ? 134 SER A CA  1 
ATOM   1047 C C   . SER A 1 135 ? 29.30700  14.62000 -21.78900 1.000 39.78649 ? 134 SER A C   1 
ATOM   1048 O O   . SER A 1 135 ? 28.59500  13.83600 -21.15500 1.000 44.52039 ? 134 SER A O   1 
ATOM   1049 C CB  . SER A 1 135 ? 30.99800  13.45600 -23.29200 1.000 44.47557 ? 134 SER A CB  1 
ATOM   1050 O OG  . SER A 1 135 ? 32.14900  14.24400 -23.06000 1.000 54.39166 ? 134 SER A OG  1 
ATOM   1051 N N   . ASP A 1 136 ? 29.76000  15.75300 -21.24900 1.000 41.68462 ? 135 ASP A N   1 
ATOM   1052 C CA  . ASP A 1 136 ? 29.30200  16.16000 -19.92000 1.000 50.38547 ? 135 ASP A CA  1 
ATOM   1053 C C   . ASP A 1 136 ? 27.81800  16.55400 -19.90700 1.000 49.59190 ? 135 ASP A C   1 
ATOM   1054 O O   . ASP A 1 136 ? 27.11300  16.31400 -18.91700 1.000 44.24794 ? 135 ASP A O   1 
ATOM   1055 C CB  . ASP A 1 136 ? 30.16600  17.28600 -19.37900 1.000 52.05999 ? 135 ASP A CB  1 
ATOM   1056 C CG  . ASP A 1 136 ? 30.36800  17.16200 -17.90000 1.000 57.97499 ? 135 ASP A CG  1 
ATOM   1057 O OD1 . ASP A 1 136 ? 31.09000  16.22600 -17.49700 1.000 63.81451 ? 135 ASP A OD1 1 
ATOM   1058 O OD2 . ASP A 1 136 ? 29.77200  17.95900 -17.14300 1.000 63.90684 ? 135 ASP A OD2 1 
ATOM   1059 N N   . GLU A 1 137 ? 27.32100  17.15500 -20.99000 1.000 46.34824 ? 136 GLU A N   1 
ATOM   1060 C CA  . GLU A 1 137 ? 25.93000  17.58300 -21.00300 1.000 40.59653 ? 136 GLU A CA  1 
ATOM   1061 C C   . GLU A 1 137 ? 25.03200  16.36700 -21.14900 1.000 43.83427 ? 136 GLU A C   1 
ATOM   1062 O O   . GLU A 1 137 ? 24.02500  16.22100 -20.43100 1.000 44.85723 ? 136 GLU A O   1 
ATOM   1063 C CB  . GLU A 1 137 ? 25.70400  18.58100 -22.13600 1.000 44.59713 ? 136 GLU A CB  1 
ATOM   1064 C CG  . GLU A 1 137 ? 26.18200  20.02800 -21.85200 1.000 37.40098 ? 136 GLU A CG  1 
ATOM   1065 C CD  . GLU A 1 137 ? 26.21400  20.90800 -23.11900 1.000 32.65928 ? 136 GLU A CD  1 
ATOM   1066 O OE1 . GLU A 1 137 ? 26.08600  20.38200 -24.23500 1.000 34.19005 ? 136 GLU A OE1 1 
ATOM   1067 O OE2 . GLU A 1 137 ? 26.35600  22.14100 -23.00600 1.000 52.54174 ? 136 GLU A OE2 1 
ATOM   1068 N N   . ARG A 1 138 ? 25.42200  15.45200 -22.03200 1.000 43.32832 ? 137 ARG A N   1 
ATOM   1069 C CA  . ARG A 1 138 ? 24.77200  14.14600 -22.08600 1.000 44.83052 ? 137 ARG A CA  1 
ATOM   1070 C C   . ARG A 1 138 ? 24.77400  13.43500 -20.72100 1.000 42.24984 ? 137 ARG A C   1 
ATOM   1071 O O   . ARG A 1 138 ? 23.73900  12.92900 -20.28600 1.000 38.60686 ? 137 ARG A O   1 
ATOM   1072 C CB  . ARG A 1 138 ? 25.43000  13.27600 -23.15800 1.000 41.24250 ? 137 ARG A CB  1 
ATOM   1073 C CG  . ARG A 1 138 ? 25.03700  13.65100 -24.57700 1.000 43.10254 ? 137 ARG A CG  1 
ATOM   1074 C CD  . ARG A 1 138 ? 25.44800  12.57600 -25.56700 1.000 43.04900 ? 137 ARG A CD  1 
ATOM   1075 N NE  . ARG A 1 138 ? 26.55400  11.77400 -25.06900 1.000 44.91905 ? 137 ARG A NE  1 
ATOM   1076 C CZ  . ARG A 1 138 ? 27.83200  12.07500 -25.25400 1.000 48.22309 ? 137 ARG A CZ  1 
ATOM   1077 N NH1 . ARG A 1 138 ? 28.19500  13.14800 -25.93800 1.000 46.04886 ? 137 ARG A NH1 1 
ATOM   1078 N NH2 . ARG A 1 138 ? 28.76800  11.29200 -24.72500 1.000 43.65946 ? 137 ARG A NH2 1 
ATOM   1079 N N   . ALA A 1 139 ? 25.91400  13.39100 -20.01600 1.000 39.92426 ? 138 ALA A N   1 
ATOM   1080 C CA  . ALA A 1 139 ? 25.91800  12.63800 -18.75700 1.000 40.37709 ? 138 ALA A CA  1 
ATOM   1081 C C   . ALA A 1 139 ? 25.13600  13.33800 -17.63400 1.000 43.62349 ? 138 ALA A C   1 
ATOM   1082 O O   . ALA A 1 139 ? 24.45200  12.65800 -16.83700 1.000 42.00840 ? 138 ALA A O   1 
ATOM   1083 C CB  . ALA A 1 139 ? 27.35000  12.33900 -18.32400 1.000 38.65821 ? 138 ALA A CB  1 
ATOM   1084 N N   . PHE A 1 140 ? 25.14400  14.68200 -17.58700 1.000 44.80262 ? 139 PHE A N   1 
ATOM   1085 C CA  . PHE A 1 140 ? 24.32400  15.34600 -16.57200 1.000 43.37071 ? 139 PHE A CA  1 
ATOM   1086 C C   . PHE A 1 140 ? 22.86300  15.06100 -16.82300 1.000 39.57477 ? 139 PHE A C   1 
ATOM   1087 O O   . PHE A 1 140 ? 22.09000  14.87400 -15.87500 1.000 36.07649 ? 139 PHE A O   1 
ATOM   1088 C CB  . PHE A 1 140 ? 24.52900  16.86400 -16.53700 1.000 41.85304 ? 139 PHE A CB  1 
ATOM   1089 C CG  . PHE A 1 140 ? 23.60400  17.56200 -15.55400 1.000 41.67855 ? 139 PHE A CG  1 
ATOM   1090 C CD1 . PHE A 1 140 ? 23.61900  17.21500 -14.20200 1.000 38.43287 ? 139 PHE A CD1 1 
ATOM   1091 C CD2 . PHE A 1 140 ? 22.69900  18.52800 -15.97900 1.000 41.40045 ? 139 PHE A CD2 1 
ATOM   1092 C CE1 . PHE A 1 140 ? 22.77400  17.82900 -13.29400 1.000 34.94847 ? 139 PHE A CE1 1 
ATOM   1093 C CE2 . PHE A 1 140 ? 21.86300  19.17300 -15.06600 1.000 36.86904 ? 139 PHE A CE2 1 
ATOM   1094 C CZ  . PHE A 1 140 ? 21.89300  18.81900 -13.72100 1.000 35.35330 ? 139 PHE A CZ  1 
ATOM   1095 N N   . MET A 1 141 ? 22.47900  14.99300 -18.10600 1.000 42.57288 ? 140 MET A N   1 
ATOM   1096 C CA  . MET A 1 141 ? 21.11200  14.63400 -18.45400 1.000 38.83894 ? 140 MET A CA  1 
ATOM   1097 C C   . MET A 1 141 ? 20.79800  13.19100 -18.07100 1.000 44.24877 ? 140 MET A C   1 
ATOM   1098 O O   . MET A 1 141 ? 19.75500  12.92700 -17.45800 1.000 42.00879 ? 140 MET A O   1 
ATOM   1099 C CB  . MET A 1 141 ? 20.90300  14.85400 -19.95500 1.000 36.44711 ? 140 MET A CB  1 
ATOM   1100 C CG  . MET A 1 141 ? 20.59800  16.31100 -20.32800 1.000 38.30393 ? 140 MET A CG  1 
ATOM   1101 S SD  . MET A 1 141 ? 20.66500  16.68500 -22.09200 1.000 49.11194 ? 140 MET A SD  1 
ATOM   1102 C CE  . MET A 1 141 ? 21.26300  18.35000 -22.05300 1.000 40.56547 ? 140 MET A CE  1 
ATOM   1103 N N   . GLU A 1 142 ? 21.71400  12.25000 -18.36800 1.000 43.28317 ? 141 GLU A N   1 
ATOM   1104 C CA  . GLU A 1 142 ? 21.44700  10.83300 -18.09700 1.000 46.63723 ? 141 GLU A CA  1 
ATOM   1105 C C   . GLU A 1 142 ? 21.20200  10.57400 -16.61600 1.000 47.24610 ? 141 GLU A C   1 
ATOM   1106 O O   . GLU A 1 142 ? 20.38400  9.70600  -16.26800 1.000 48.39510 ? 141 GLU A O   1 
ATOM   1107 C CB  . GLU A 1 142 ? 22.58300  9.93500  -18.61300 1.000 48.81732 ? 141 GLU A CB  1 
ATOM   1108 C CG  . GLU A 1 142 ? 23.02400  10.28800 -20.03200 1.000 53.28924 ? 141 GLU A CG  1 
ATOM   1109 C CD  . GLU A 1 142 ? 24.09000  9.39300  -20.64800 1.000 52.91830 ? 141 GLU A CD  1 
ATOM   1110 O OE1 . GLU A 1 142 ? 23.71000  8.28400  -21.08700 1.000 50.33837 ? 141 GLU A OE1 1 
ATOM   1111 O OE2 . GLU A 1 142 ? 25.28500  9.80900  -20.69800 1.000 46.88558 ? 141 GLU A OE2 1 
ATOM   1112 N N   . THR A 1 143 ? 21.85100  11.33400 -15.72100 1.000 46.33804 ? 142 THR A N   1 
ATOM   1113 C CA  . THR A 1 143 ? 21.51200  11.10000 -14.31200 1.000 41.90108 ? 142 THR A CA  1 
ATOM   1114 C C   . THR A 1 143 ? 20.09600  11.58300 -13.98300 1.000 40.83159 ? 142 THR A C   1 
ATOM   1115 O O   . THR A 1 143 ? 19.46900  11.06000 -13.06000 1.000 43.15050 ? 142 THR A O   1 
ATOM   1116 C CB  . THR A 1 143 ? 22.53400  11.71100 -13.34200 1.000 37.84593 ? 142 THR A CB  1 
ATOM   1117 O OG1 . THR A 1 143 ? 22.19600  13.06500 -13.03300 1.000 46.46152 ? 142 THR A OG1 1 
ATOM   1118 C CG2 . THR A 1 143 ? 23.93800  11.63100 -13.90600 1.000 45.05224 ? 142 THR A CG2 1 
ATOM   1119 N N   . ASN A 1 144 ? 19.56200  12.54900 -14.71800 1.000 46.32819 ? 143 ASN A N   1 
ATOM   1120 C CA  . ASN A 1 144 ? 18.21600  13.02400 -14.41200 1.000 46.19198 ? 143 ASN A CA  1 
ATOM   1121 C C   . ASN A 1 144 ? 17.13100  12.11600 -15.00000 1.000 52.24340 ? 143 ASN A C   1 
ATOM   1122 O O   . ASN A 1 144 ? 16.22000  12.58800 -15.69800 1.000 51.78517 ? 143 ASN A O   1 
ATOM   1123 C CB  . ASN A 1 144 ? 18.05800  14.45400 -14.90500 1.000 39.67729 ? 143 ASN A CB  1 
ATOM   1124 C CG  . ASN A 1 144 ? 18.72500  15.43000 -14.00000 1.000 40.44061 ? 143 ASN A CG  1 
ATOM   1125 O OD1 . ASN A 1 144 ? 18.73200  15.25300 -12.77600 1.000 42.05953 ? 143 ASN A OD1 1 
ATOM   1126 N ND2 . ASN A 1 144 ? 19.32800  16.46100 -14.58700 1.000 42.38650 ? 143 ASN A ND2 1 
ATOM   1127 N N   . VAL A 1 145 ? 17.20900  10.81400 -14.70900 1.000 48.27702 ? 144 VAL A N   1 
ATOM   1128 C CA  . VAL A 1 145 ? 16.24800  9.83300  -15.20400 1.000 46.86302 ? 144 VAL A CA  1 
ATOM   1129 C C   . VAL A 1 145 ? 15.90600  8.87700  -14.06700 1.000 53.39773 ? 144 VAL A C   1 
ATOM   1130 O O   . VAL A 1 145 ? 16.78900  8.41300  -13.33800 1.000 53.65336 ? 144 VAL A O   1 
ATOM   1131 C CB  . VAL A 1 145 ? 16.79500  9.06500  -16.43100 1.000 52.08244 ? 144 VAL A CB  1 
ATOM   1132 C CG1 . VAL A 1 145 ? 15.90200  7.89200  -16.79100 1.000 47.54418 ? 144 VAL A CG1 1 
ATOM   1133 C CG2 . VAL A 1 145 ? 16.93300  9.98600  -17.61600 1.000 50.41855 ? 144 VAL A CG2 1 
ATOM   1134 N N   . ASP A 1 146 ? 14.61500  8.61100  -13.89200 1.000 62.03577 ? 145 ASP A N   1 
ATOM   1135 C CA  . ASP A 1 146 ? 14.14700  7.83500  -12.74300 1.000 61.45094 ? 145 ASP A CA  1 
ATOM   1136 C C   . ASP A 1 146 ? 13.07900  6.80900  -13.15100 1.000 58.25822 ? 145 ASP A C   1 
ATOM   1137 O O   . ASP A 1 146 ? 13.31200  5.93700  -13.99900 1.000 66.29775 ? 145 ASP A O   1 
ATOM   1138 C CB  . ASP A 1 146 ? 13.60900  8.77900  -11.66800 1.000 55.48061 ? 145 ASP A CB  1 
ATOM   1139 C CG  . ASP A 1 146 ? 12.89100  8.05500  -10.56700 1.000 58.24858 ? 145 ASP A CG  1 
ATOM   1140 O OD1 . ASP A 1 146 ? 13.55200  7.66200  -9.58500  1.000 58.65123 ? 145 ASP A OD1 1 
ATOM   1141 O OD2 . ASP A 1 146 ? 11.66100  7.88000  -10.69200 1.000 65.60589 ? 145 ASP A OD2 1 
ATOM   1142 N N   . PRO B 1 2   ? -10.72700 31.36300 -17.14600 1.000 35.47426 ? 1   PRO B N   1 
ATOM   1143 C CA  . PRO B 1 2   ? -9.40400  31.80100 -17.57000 1.000 33.61529 ? 1   PRO B CA  1 
ATOM   1144 C C   . PRO B 1 2   ? -8.50900  31.77400 -16.32600 1.000 30.35431 ? 1   PRO B C   1 
ATOM   1145 O O   . PRO B 1 2   ? -9.06200  31.71400 -15.23000 1.000 26.75298 ? 1   PRO B O   1 
ATOM   1146 C CB  . PRO B 1 2   ? -9.68700  33.19300 -18.11700 1.000 37.34623 ? 1   PRO B CB  1 
ATOM   1147 C CG  . PRO B 1 2   ? -10.62700 33.70900 -17.05200 1.000 36.00570 ? 1   PRO B CG  1 
ATOM   1148 C CD  . PRO B 1 2   ? -11.55800 32.53100 -16.79600 1.000 36.88399 ? 1   PRO B CD  1 
ATOM   1149 N N   . VAL B 1 3   ? -7.18300  31.71600 -16.44700 1.000 28.27145 ? 2   VAL B N   1 
ATOM   1150 C CA  . VAL B 1 3   ? -6.31800  31.69400 -15.26600 1.000 27.63369 ? 2   VAL B CA  1 
ATOM   1151 C C   . VAL B 1 3   ? -5.58200  33.02600 -15.13500 1.000 26.99242 ? 2   VAL B C   1 
ATOM   1152 O O   . VAL B 1 3   ? -4.93000  33.47200 -16.07900 1.000 21.08293 ? 2   VAL B O   1 
ATOM   1153 C CB  . VAL B 1 3   ? -5.32500  30.52000 -15.32900 1.000 28.11939 ? 2   VAL B CB  1 
ATOM   1154 C CG1 . VAL B 1 3   ? -4.30100  30.63100 -14.22600 1.000 26.32505 ? 2   VAL B CG1 1 
ATOM   1155 C CG2 . VAL B 1 3   ? -6.06600  29.18000 -15.23900 1.000 33.69762 ? 2   VAL B CG2 1 
ATOM   1156 N N   . TYR B 1 4   ? -5.69600  33.68200 -13.97700 1.000 24.61589 ? 3   TYR B N   1 
ATOM   1157 C CA  . TYR B 1 4   ? -5.01800  34.95800 -13.74400 1.000 28.65061 ? 3   TYR B CA  1 
ATOM   1158 C C   . TYR B 1 4   ? -3.94800  34.76300 -12.67700 1.000 31.75398 ? 3   TYR B C   1 
ATOM   1159 O O   . TYR B 1 4   ? -4.25000  34.70100 -11.48700 1.000 37.94317 ? 3   TYR B O   1 
ATOM   1160 C CB  . TYR B 1 4   ? -6.00000  36.05000 -13.33700 1.000 25.93186 ? 3   TYR B CB  1 
ATOM   1161 C CG  . TYR B 1 4   ? -6.72900  36.65700 -14.50200 1.000 25.08611 ? 3   TYR B CG  1 
ATOM   1162 C CD1 . TYR B 1 4   ? -6.09900  37.50800 -15.37200 1.000 23.21119 ? 3   TYR B CD1 1 
ATOM   1163 C CD2 . TYR B 1 4   ? -8.05800  36.35200 -14.74300 1.000 35.08115 ? 3   TYR B CD2 1 
ATOM   1164 C CE1 . TYR B 1 4   ? -6.77100  38.06200 -16.44200 1.000 27.79896 ? 3   TYR B CE1 1 
ATOM   1165 C CE2 . TYR B 1 4   ? -8.75300  36.91700 -15.82000 1.000 31.44920 ? 3   TYR B CE2 1 
ATOM   1166 C CZ  . TYR B 1 4   ? -8.10900  37.76400 -16.66300 1.000 25.57762 ? 3   TYR B CZ  1 
ATOM   1167 O OH  . TYR B 1 4   ? -8.79900  38.29500 -17.73200 1.000 18.34369 ? 3   TYR B OH  1 
ATOM   1168 N N   . MET B 1 5   ? -2.70000  34.69200 -13.10500 1.000 30.97737 ? 4   MET B N   1 
ATOM   1169 C CA  . MET B 1 5   ? -1.56300  34.69200 -12.20300 1.000 34.08595 ? 4   MET B CA  1 
ATOM   1170 C C   . MET B 1 5   ? -1.29900  36.14900 -11.83300 1.000 38.63091 ? 4   MET B C   1 
ATOM   1171 O O   . MET B 1 5   ? -1.18400  37.00600 -12.72300 1.000 29.75208 ? 4   MET B O   1 
ATOM   1172 C CB  . MET B 1 5   ? -0.34400  34.09700 -12.90500 1.000 31.72009 ? 4   MET B CB  1 
ATOM   1173 C CG  . MET B 1 5   ? -0.34400  32.58100 -13.19500 1.000 43.00117 ? 4   MET B CG  1 
ATOM   1174 S SD  . MET B 1 5   ? -1.24800  31.48000 -12.07300 1.000 36.64790 ? 4   MET B SD  1 
ATOM   1175 C CE  . MET B 1 5   ? 0.16100   30.91300 -11.12000 1.000 34.90002 ? 4   MET B CE  1 
ATOM   1176 N N   . VAL B 1 6   ? -1.28000  36.45600 -10.54000 1.000 36.79819 ? 5   VAL B N   1 
ATOM   1177 C CA  . VAL B 1 6   ? -1.02300  37.81600 -10.07800 1.000 31.29200 ? 5   VAL B CA  1 
ATOM   1178 C C   . VAL B 1 6   ? 0.19400   37.78700 -9.17500  1.000 28.26516 ? 5   VAL B C   1 
ATOM   1179 O O   . VAL B 1 6   ? 0.13100   37.25600 -8.06300  1.000 28.03714 ? 5   VAL B O   1 
ATOM   1180 C CB  . VAL B 1 6   ? -2.22300  38.42800 -9.34300  1.000 30.89903 ? 5   VAL B CB  1 
ATOM   1181 C CG1 . VAL B 1 6   ? -1.91600  39.89600 -9.03700  1.000 29.93729 ? 5   VAL B CG1 1 
ATOM   1182 C CG2 . VAL B 1 6   ? -3.49500  38.27900 -10.18000 1.000 25.29150 ? 5   VAL B CG2 1 
ATOM   1183 N N   . TYR B 1 7   ? 1.26200   38.43500 -9.61400  1.000 27.92340 ? 6   TYR B N   1 
ATOM   1184 C CA  . TYR B 1 7   ? 2.53600   38.46400 -8.91700  1.000 32.94869 ? 6   TYR B CA  1 
ATOM   1185 C C   . TYR B 1 7   ? 2.64900   39.74900 -8.11400  1.000 33.31891 ? 6   TYR B C   1 
ATOM   1186 O O   . TYR B 1 7   ? 2.48300   40.84600 -8.66700  1.000 34.61131 ? 6   TYR B O   1 
ATOM   1187 C CB  . TYR B 1 7   ? 3.67500   38.35300 -9.92900  1.000 33.17491 ? 6   TYR B CB  1 
ATOM   1188 C CG  . TYR B 1 7   ? 3.66600   37.01300 -10.64200 1.000 30.43981 ? 6   TYR B CG  1 
ATOM   1189 C CD1 . TYR B 1 7   ? 4.33100   35.93100 -10.10800 1.000 27.76267 ? 6   TYR B CD1 1 
ATOM   1190 C CD2 . TYR B 1 7   ? 2.93400   36.81900 -11.82200 1.000 34.36792 ? 6   TYR B CD2 1 
ATOM   1191 C CE1 . TYR B 1 7   ? 4.32200   34.69800 -10.73800 1.000 34.08867 ? 6   TYR B CE1 1 
ATOM   1192 C CE2 . TYR B 1 7   ? 2.91400   35.57700 -12.47000 1.000 30.01368 ? 6   TYR B CE2 1 
ATOM   1193 C CZ  . TYR B 1 7   ? 3.61300   34.51800 -11.91200 1.000 32.20225 ? 6   TYR B CZ  1 
ATOM   1194 O OH  . TYR B 1 7   ? 3.62100   33.26400 -12.48600 1.000 33.44159 ? 6   TYR B OH  1 
ATOM   1195 N N   . VAL B 1 8   ? 2.88900   39.59600 -6.80500  1.000 32.16241 ? 7   VAL B N   1 
ATOM   1196 C CA  . VAL B 1 8   ? 2.89000   40.69500 -5.84200  1.000 29.12825 ? 7   VAL B CA  1 
ATOM   1197 C C   . VAL B 1 8   ? 3.94800   40.42000 -4.78900  1.000 30.43984 ? 7   VAL B C   1 
ATOM   1198 O O   . VAL B 1 8   ? 4.34200   39.28100 -4.54200  1.000 27.10611 ? 7   VAL B O   1 
ATOM   1199 C CB  . VAL B 1 8   ? 1.53800   40.91100 -5.11800  1.000 29.19269 ? 7   VAL B CB  1 
ATOM   1200 C CG1 . VAL B 1 8   ? 0.50800   41.48100 -6.05400  1.000 29.21209 ? 7   VAL B CG1 1 
ATOM   1201 C CG2 . VAL B 1 8   ? 1.05400   39.61600 -4.44000  1.000 30.63931 ? 7   VAL B CG2 1 
ATOM   1202 N N   . SER B 1 9   ? 4.37800   41.47800 -4.12800  1.000 39.51891 ? 8   SER B N   1 
ATOM   1203 C CA  . SER B 1 9   ? 5.29500   41.31300 -3.01800  1.000 40.23781 ? 8   SER B CA  1 
ATOM   1204 C C   . SER B 1 9   ? 4.53700   40.87300 -1.77100  1.000 35.62796 ? 8   SER B C   1 
ATOM   1205 O O   . SER B 1 9   ? 3.35000   41.16100 -1.60800  1.000 33.43842 ? 8   SER B O   1 
ATOM   1206 C CB  . SER B 1 9   ? 6.05700   42.61200 -2.77000  1.000 35.34380 ? 8   SER B CB  1 
ATOM   1207 O OG  . SER B 1 9   ? 7.00700   42.79700 -3.81200  1.000 40.95721 ? 8   SER B OG  1 
ATOM   1208 N N   . GLN B 1 10  ? 5.21000   40.09500 -0.93000  1.000 38.10095 ? 9   GLN B N   1 
ATOM   1209 C CA  . GLN B 1 10  ? 4.55900   39.59400 0.26800   1.000 36.49144 ? 9   GLN B CA  1 
ATOM   1210 C C   . GLN B 1 10  ? 4.11900   40.77000 1.14100   1.000 37.72665 ? 9   GLN B C   1 
ATOM   1211 O O   . GLN B 1 10  ? 4.84200   41.76000 1.29700   1.000 41.09990 ? 9   GLN B O   1 
ATOM   1212 C CB  . GLN B 1 10  ? 5.49200   38.65400 1.03500   1.000 37.63858 ? 9   GLN B CB  1 
ATOM   1213 C CG  . GLN B 1 10  ? 6.87800   39.22200 1.31500   1.000 42.92849 ? 9   GLN B CG  1 
ATOM   1214 C CD  . GLN B 1 10  ? 7.59500   38.54800 2.48500   1.000 41.90525 ? 9   GLN B CD  1 
ATOM   1215 O OE1 . GLN B 1 10  ? 8.07500   37.42100 2.36500   1.000 41.68103 ? 9   GLN B OE1 1 
ATOM   1216 N NE2 . GLN B 1 10  ? 7.68600   39.24800 3.61600   1.000 46.13328 ? 9   GLN B NE2 1 
ATOM   1217 N N   . ASP B 1 11  ? 2.91100   40.65800 1.69400   1.000 34.61605 ? 10  ASP B N   1 
ATOM   1218 C CA  . ASP B 1 11  ? 2.29200   41.63400 2.59300   1.000 43.04047 ? 10  ASP B CA  1 
ATOM   1219 C C   . ASP B 1 11  ? 2.02000   43.01300 1.96100   1.000 42.82078 ? 10  ASP B C   1 
ATOM   1220 O O   . ASP B 1 11  ? 1.93200   44.00700 2.69200   1.000 48.32379 ? 10  ASP B O   1 
ATOM   1221 C CB  . ASP B 1 11  ? 3.15800   41.83200 3.85000   1.000 50.05085 ? 10  ASP B CB  1 
ATOM   1222 C CG  . ASP B 1 11  ? 3.10400   40.65300 4.80000   1.000 45.31231 ? 10  ASP B CG  1 
ATOM   1223 O OD1 . ASP B 1 11  ? 2.04400   40.00600 4.88700   1.000 52.98413 ? 10  ASP B OD1 1 
ATOM   1224 O OD2 . ASP B 1 11  ? 4.12700   40.37100 5.45900   1.000 49.69179 ? 10  ASP B OD2 1 
ATOM   1225 N N   . ARG B 1 12  ? 1.92400   43.15500 0.63200   1.000 32.12374 ? 11  ARG B N   1 
ATOM   1226 C CA  . ARG B 1 12  ? 1.37300   44.40100 0.08400   1.000 35.20580 ? 11  ARG B CA  1 
ATOM   1227 C C   . ARG B 1 12  ? -0.15000  44.32800 -0.05900  1.000 36.36818 ? 11  ARG B C   1 
ATOM   1228 O O   . ARG B 1 12  ? -0.86500  45.33400 0.07500   1.000 27.63619 ? 11  ARG B O   1 
ATOM   1229 C CB  . ARG B 1 12  ? 2.03100   44.75100 -1.26200  1.000 34.14256 ? 11  ARG B CB  1 
ATOM   1230 C CG  . ARG B 1 12  ? 1.41300   45.96300 -1.98400  1.000 36.44809 ? 11  ARG B CG  1 
ATOM   1231 C CD  . ARG B 1 12  ? 1.28300   47.18800 -1.08500  1.000 36.65722 ? 11  ARG B CD  1 
ATOM   1232 N NE  . ARG B 1 12  ? 1.29800   48.43200 -1.84800  1.000 43.16153 ? 11  ARG B NE  1 
ATOM   1233 C CZ  . ARG B 1 12  ? 0.27200   49.27600 -1.91500  1.000 44.31213 ? 11  ARG B CZ  1 
ATOM   1234 N NH1 . ARG B 1 12  ? -0.88300  49.00900 -1.31600  1.000 43.20354 ? 11  ARG B NH1 1 
ATOM   1235 N NH2 . ARG B 1 12  ? 0.39900   50.40500 -2.61400  1.000 36.04183 ? 11  ARG B NH2 1 
ATOM   1236 N N   . LEU B 1 13  ? -0.66200  43.16100 -0.36300  1.000 36.10972 ? 12  LEU B N   1 
ATOM   1237 C CA  . LEU B 1 13  ? -2.08400  42.94200 -0.33300  1.000 26.93741 ? 12  LEU B CA  1 
ATOM   1238 C C   . LEU B 1 13  ? -2.36500  42.20500 0.96400   1.000 31.00665 ? 12  LEU B C   1 
ATOM   1239 O O   . LEU B 1 13  ? -1.73600  41.18400 1.24400   1.000 30.68342 ? 12  LEU B O   1 
ATOM   1240 C CB  . LEU B 1 13  ? -2.53900  42.14400 -1.54900  1.000 27.28571 ? 12  LEU B CB  1 
ATOM   1241 C CG  . LEU B 1 13  ? -1.97000  42.63800 -2.87900  1.000 29.23374 ? 12  LEU B CG  1 
ATOM   1242 C CD1 . LEU B 1 13  ? -2.41400  41.75400 -4.04900  1.000 20.35550 ? 12  LEU B CD1 1 
ATOM   1243 C CD2 . LEU B 1 13  ? -2.26500  44.11600 -3.12900  1.000 25.55193 ? 12  LEU B CD2 1 
ATOM   1244 N N   . THR B 1 14  ? -3.24200  42.77600 1.78400   1.000 36.51097 ? 13  THR B N   1 
ATOM   1245 C CA  . THR B 1 14  ? -3.86700  42.07700 2.90400   1.000 40.87863 ? 13  THR B CA  1 
ATOM   1246 C C   . THR B 1 14  ? -4.85700  41.04000 2.37500   1.000 33.69058 ? 13  THR B C   1 
ATOM   1247 O O   . THR B 1 14  ? -5.13500  40.99200 1.17100   1.000 30.87799 ? 13  THR B O   1 
ATOM   1248 C CB  . THR B 1 14  ? -4.58000  43.06900 3.82900   1.000 32.98133 ? 13  THR B CB  1 
ATOM   1249 O OG1 . THR B 1 14  ? -5.59200  43.73900 3.07800   1.000 32.09551 ? 13  THR B OG1 1 
ATOM   1250 C CG2 . THR B 1 14  ? -3.61300  44.11200 4.42000   1.000 28.48752 ? 13  THR B CG2 1 
ATOM   1251 N N   . PRO B 1 15  ? -5.30800  40.11500 3.23300   1.000 32.60578 ? 14  PRO B N   1 
ATOM   1252 C CA  . PRO B 1 15  ? -6.40900  39.21200 2.83900   1.000 31.60292 ? 14  PRO B CA  1 
ATOM   1253 C C   . PRO B 1 15  ? -7.61200  39.90500 2.20100   1.000 36.33884 ? 14  PRO B C   1 
ATOM   1254 O O   . PRO B 1 15  ? -8.10800  39.43100 1.16100   1.000 34.85459 ? 14  PRO B O   1 
ATOM   1255 C CB  . PRO B 1 15  ? -6.77700  38.52600 4.15400   1.000 24.73503 ? 14  PRO B CB  1 
ATOM   1256 C CG  . PRO B 1 15  ? -5.50800  38.51800 4.95200   1.000 35.28660 ? 14  PRO B CG  1 
ATOM   1257 C CD  . PRO B 1 15  ? -4.61200  39.64200 4.44300   1.000 37.82082 ? 14  PRO B CD  1 
ATOM   1258 N N   . SER B 1 16  ? -8.11200  40.99900 2.80600   1.000 32.66974 ? 15  SER B N   1 
ATOM   1259 C CA  . SER B 1 16  ? -9.23700  41.72700 2.21300   1.000 31.08129 ? 15  SER B CA  1 
ATOM   1260 C C   . SER B 1 16  ? -8.89000  42.30500 0.85100   1.000 38.34628 ? 15  SER B C   1 
ATOM   1261 O O   . SER B 1 16  ? -9.72800  42.29700 -0.05900  1.000 34.01122 ? 15  SER B O   1 
ATOM   1262 C CB  . SER B 1 16  ? -9.70400  42.85700 3.12100   1.000 28.16898 ? 15  SER B CB  1 
ATOM   1263 O OG  . SER B 1 16  ? -10.43700 42.35000 4.21100   1.000 45.18176 ? 15  SER B OG  1 
ATOM   1264 N N   . ALA B 1 17  ? -7.65600  42.80900 0.68900   1.000 37.33209 ? 16  ALA B N   1 
ATOM   1265 C CA  . ALA B 1 17  ? -7.22800  43.38300 -0.58400  1.000 31.89742 ? 16  ALA B CA  1 
ATOM   1266 C C   . ALA B 1 17  ? -7.01900  42.30400 -1.64900  1.000 35.49582 ? 16  ALA B C   1 
ATOM   1267 O O   . ALA B 1 17  ? -7.22200  42.55300 -2.84800  1.000 29.89409 ? 16  ALA B O   1 
ATOM   1268 C CB  . ALA B 1 17  ? -5.96100  44.20000 -0.37300  1.000 27.40606 ? 16  ALA B CB  1 
ATOM   1269 N N   . LYS B 1 18  ? -6.58200  41.11300 -1.24100  1.000 36.14944 ? 17  LYS B N   1 
ATOM   1270 C CA  . LYS B 1 18  ? -6.56400  39.98400 -2.16700  1.000 36.04864 ? 17  LYS B CA  1 
ATOM   1271 C C   . LYS B 1 18  ? -7.98100  39.61600 -2.60300  1.000 35.40918 ? 17  LYS B C   1 
ATOM   1272 O O   . LYS B 1 18  ? -8.24500  39.42600 -3.80200  1.000 31.71041 ? 17  LYS B O   1 
ATOM   1273 C CB  . LYS B 1 18  ? -5.85000  38.79000 -1.53000  1.000 33.30428 ? 17  LYS B CB  1 
ATOM   1274 C CG  . LYS B 1 18  ? -4.36100  38.88000 -1.60000  1.000 23.07239 ? 17  LYS B CG  1 
ATOM   1275 C CD  . LYS B 1 18  ? -3.75500  37.57200 -1.23500  1.000 24.32701 ? 17  LYS B CD  1 
ATOM   1276 C CE  . LYS B 1 18  ? -2.44800  37.74700 -0.52400  1.000 24.63633 ? 17  LYS B CE  1 
ATOM   1277 N NZ  . LYS B 1 18  ? -2.61600  37.47900 0.92300   1.000 27.25227 ? 17  LYS B NZ  1 
ATOM   1278 N N   . HIS B 1 19  ? -8.91800  39.52200 -1.64300  1.000 33.87362 ? 18  HIS B N   1 
ATOM   1279 C CA  . HIS B 1 19  ? -10.30500 39.27200 -2.04000  1.000 35.84034 ? 18  HIS B CA  1 
ATOM   1280 C C   . HIS B 1 19  ? -10.82400 40.36000 -2.98300  1.000 34.18751 ? 18  HIS B C   1 
ATOM   1281 O O   . HIS B 1 19  ? -11.54300 40.06400 -3.95100  1.000 32.27523 ? 18  HIS B O   1 
ATOM   1282 C CB  . HIS B 1 19  ? -11.23100 39.14700 -0.83900  1.000 30.90738 ? 18  HIS B CB  1 
ATOM   1283 C CG  . HIS B 1 19  ? -12.63500 38.84400 -1.24400  1.000 40.19161 ? 18  HIS B CG  1 
ATOM   1284 N ND1 . HIS B 1 19  ? -13.69100 39.70200 -1.00000  1.000 51.50808 ? 18  HIS B ND1 1 
ATOM   1285 C CD2 . HIS B 1 19  ? -13.15000 37.80200 -1.94300  1.000 40.04320 ? 18  HIS B CD2 1 
ATOM   1286 C CE1 . HIS B 1 19  ? -14.80100 39.18500 -1.50200  1.000 50.41083 ? 18  HIS B CE1 1 
ATOM   1287 N NE2 . HIS B 1 19  ? -14.50000 38.03600 -2.08500  1.000 48.80208 ? 18  HIS B NE2 1 
ATOM   1288 N N   . ALA B 1 20  ? -10.43900 41.62000 -2.73500  1.000 32.96234 ? 19  ALA B N   1 
ATOM   1289 C CA  . ALA B 1 20  ? -10.90100 42.73700 -3.55000  1.000 31.17773 ? 19  ALA B CA  1 
ATOM   1290 C C   . ALA B 1 20  ? -10.32300 42.69000 -4.95900  1.000 32.82846 ? 19  ALA B C   1 
ATOM   1291 O O   . ALA B 1 20  ? -11.05000 42.89700 -5.94100  1.000 36.02949 ? 19  ALA B O   1 
ATOM   1292 C CB  . ALA B 1 20  ? -10.52700 44.05700 -2.87900  1.000 30.02370 ? 19  ALA B CB  1 
ATOM   1293 N N   . VAL B 1 21  ? -9.02200  42.41900 -5.08300  1.000 34.26823 ? 20  VAL B N   1 
ATOM   1294 C CA  . VAL B 1 21  ? -8.38700  42.39500 -6.40200  1.000 37.74800 ? 20  VAL B CA  1 
ATOM   1295 C C   . VAL B 1 21  ? -8.91900  41.21700 -7.21100  1.000 35.04491 ? 20  VAL B C   1 
ATOM   1296 O O   . VAL B 1 21  ? -9.25100  41.35700 -8.39300  1.000 37.27205 ? 20  VAL B O   1 
ATOM   1297 C CB  . VAL B 1 21  ? -6.84500  42.37500 -6.28000  1.000 25.45439 ? 20  VAL B CB  1 
ATOM   1298 C CG1 . VAL B 1 21  ? -6.21900  42.08900 -7.59400  1.000 20.80342 ? 20  VAL B CG1 1 
ATOM   1299 C CG2 . VAL B 1 21  ? -6.34200  43.71600 -5.78500  1.000 28.74624 ? 20  VAL B CG2 1 
ATOM   1300 N N   . ALA B 1 22  ? -9.03600  40.04800 -6.57300  1.000 34.53681 ? 21  ALA B N   1 
ATOM   1301 C CA  . ALA B 1 22  ? -9.57900  38.87100 -7.24600  1.000 33.73981 ? 21  ALA B CA  1 
ATOM   1302 C C   . ALA B 1 22  ? -11.01900 39.10900 -7.72800  1.000 28.48430 ? 21  ALA B C   1 
ATOM   1303 O O   . ALA B 1 22  ? -11.36400 38.72200 -8.85700  1.000 33.93611 ? 21  ALA B O   1 
ATOM   1304 C CB  . ALA B 1 22  ? -9.44200  37.65100 -6.32300  1.000 33.42368 ? 21  ALA B CB  1 
ATOM   1305 N N   . LYS B 1 23  ? -11.86800 39.72400 -6.88100  1.000 32.05591 ? 22  LYS B N   1 
ATOM   1306 C CA  . LYS B 1 23  ? -13.21200 40.13900 -7.29000  1.000 37.83062 ? 22  LYS B CA  1 
ATOM   1307 C C   . LYS B 1 23  ? -13.16300 41.04600 -8.48900  1.000 38.98863 ? 22  LYS B C   1 
ATOM   1308 O O   . LYS B 1 23  ? -13.90100 40.83500 -9.44500  1.000 36.68738 ? 22  LYS B O   1 
ATOM   1309 C CB  . LYS B 1 23  ? -13.91200 40.86900 -6.12700  1.000 33.27458 ? 22  LYS B CB  1 
ATOM   1310 C CG  . LYS B 1 23  ? -15.26400 41.52600 -6.44000  1.000 49.18532 ? 22  LYS B CG  1 
ATOM   1311 C CD  . LYS B 1 23  ? -15.40700 42.71500 -5.42900  1.000 51.50969 ? 22  LYS B CD  1 
ATOM   1312 C CE  . LYS B 1 23  ? -14.00000 43.64200 -5.73600  1.000 37.47109 ? 22  LYS B CE  1 
ATOM   1313 N NZ  . LYS B 1 23  ? -14.23100 45.00600 -5.91600  1.000 41.81723 ? 22  LYS B NZ  1 
ATOM   1314 N N   . ALA B 1 24  ? -12.31500 42.08000 -8.44800  1.000 39.53314 ? 23  ALA B N   1 
ATOM   1315 C CA  . ALA B 1 24  ? -12.27600 43.03000 -9.55100  1.000 30.18067 ? 23  ALA B CA  1 
ATOM   1316 C C   . ALA B 1 24  ? -11.90200 42.32600 -10.85800 1.000 31.48756 ? 23  ALA B C   1 
ATOM   1317 O O   . ALA B 1 24  ? -12.55100 42.53000 -11.89600 1.000 32.53199 ? 23  ALA B O   1 
ATOM   1318 C CB  . ALA B 1 24  ? -11.31800 44.18600 -9.23300  1.000 28.96120 ? 23  ALA B CB  1 
ATOM   1319 N N   . ILE B 1 25  ? -10.91100 41.43600 -10.80700 1.000 28.10177 ? 24  ILE B N   1 
ATOM   1320 C CA  . ILE B 1 25  ? -10.43000 40.77100 -12.01400 1.000 27.45882 ? 24  ILE B CA  1 
ATOM   1321 C C   . ILE B 1 25  ? -11.49000 39.83300 -12.56300 1.000 29.67707 ? 24  ILE B C   1 
ATOM   1322 O O   . ILE B 1 25  ? -11.75100 39.83100 -13.77700 1.000 26.76464 ? 24  ILE B O   1 
ATOM   1323 C CB  . ILE B 1 25  ? -9.12000  40.02500 -11.72500 1.000 28.19725 ? 24  ILE B CB  1 
ATOM   1324 C CG1 . ILE B 1 25  ? -7.93700  40.98800 -11.77700 1.000 19.15775 ? 24  ILE B CG1 1 
ATOM   1325 C CG2 . ILE B 1 25  ? -8.92400  38.94900 -12.73900 1.000 26.98060 ? 24  ILE B CG2 1 
ATOM   1326 C CD1 . ILE B 1 25  ? -6.64200  40.27900 -11.58200 1.000 22.42960 ? 24  ILE B CD1 1 
ATOM   1327 N N   . THR B 1 26  ? -12.10900 39.01700 -11.68400 1.000 27.45344 ? 25  THR B N   1 
ATOM   1328 C CA  . THR B 1 26  ? -13.20900 38.14800 -12.10400 1.000 28.92172 ? 25  THR B CA  1 
ATOM   1329 C C   . THR B 1 26  ? -14.35600 38.96300 -12.70600 1.000 35.47597 ? 25  THR B C   1 
ATOM   1330 O O   . THR B 1 26  ? -14.91400 38.59500 -13.75000 1.000 33.98033 ? 25  THR B O   1 
ATOM   1331 C CB  . THR B 1 26  ? -13.70100 37.26200 -10.94600 1.000 38.59845 ? 25  THR B CB  1 
ATOM   1332 O OG1 . THR B 1 26  ? -12.60400 36.82300 -10.12800 1.000 36.91763 ? 25  THR B OG1 1 
ATOM   1333 C CG2 . THR B 1 26  ? -14.44400 36.03100 -11.47800 1.000 39.88025 ? 25  THR B CG2 1 
ATOM   1334 N N   . ASP B 1 27  ? -14.74000 40.05800 -12.03600 1.000 36.34415 ? 26  ASP B N   1 
ATOM   1335 C CA  . ASP B 1 27  ? -15.80400 40.93500 -12.51800 1.000 38.49393 ? 26  ASP B CA  1 
ATOM   1336 C C   . ASP B 1 27  ? -15.50500 41.49600 -13.89900 1.000 34.36105 ? 26  ASP B C   1 
ATOM   1337 O O   . ASP B 1 27  ? -16.37100 41.49900 -14.77600 1.000 36.15937 ? 26  ASP B O   1 
ATOM   1338 C CB  . ASP B 1 27  ? -16.00700 42.07800 -11.52800 1.000 39.21750 ? 26  ASP B CB  1 
ATOM   1339 C CG  . ASP B 1 27  ? -16.91300 41.69400 -10.39300 1.000 52.69222 ? 26  ASP B CG  1 
ATOM   1340 O OD1 . ASP B 1 27  ? -16.46200 40.91500 -9.52400  1.000 57.66687 ? 26  ASP B OD1 1 
ATOM   1341 O OD2 . ASP B 1 27  ? -18.07200 42.17700 -10.35800 1.000 57.75193 ? 26  ASP B OD2 1 
ATOM   1342 N N   . ALA B 1 28  ? -14.27400 41.93500 -14.12200 1.000 32.31978 ? 27  ALA B N   1 
ATOM   1343 C CA  . ALA B 1 28  ? -13.90400 42.45900 -15.43000 1.000 30.33910 ? 27  ALA B CA  1 
ATOM   1344 C C   . ALA B 1 28  ? -13.99400 41.37000 -16.48700 1.000 30.66833 ? 27  ALA B C   1 
ATOM   1345 O O   . ALA B 1 28  ? -14.56900 41.57700 -17.56400 1.000 28.36577 ? 27  ALA B O   1 
ATOM   1346 C CB  . ALA B 1 28  ? -12.48600 43.03800 -15.36800 1.000 27.45220 ? 27  ALA B CB  1 
ATOM   1347 N N   . HIS B 1 29  ? -13.43300 40.19000 -16.18400 1.000 30.81936 ? 28  HIS B N   1 
ATOM   1348 C CA  . HIS B 1 29  ? -13.38200 39.13200 -17.18100 1.000 31.84845 ? 28  HIS B CA  1 
ATOM   1349 C C   . HIS B 1 29  ? -14.78700 38.69600 -17.56500 1.000 32.74042 ? 28  HIS B C   1 
ATOM   1350 O O   . HIS B 1 29  ? -15.11900 38.59300 -18.75900 1.000 30.91616 ? 28  HIS B O   1 
ATOM   1351 C CB  . HIS B 1 29  ? -12.56700 37.93500 -16.68500 1.000 31.67735 ? 28  HIS B CB  1 
ATOM   1352 C CG  . HIS B 1 29  ? -12.38800 36.88000 -17.73500 1.000 29.70965 ? 28  HIS B CG  1 
ATOM   1353 N ND1 . HIS B 1 29  ? -11.29100 36.83400 -18.56200 1.000 29.74515 ? 28  HIS B ND1 1 
ATOM   1354 C CD2 . HIS B 1 29  ? -13.22000 35.90100 -18.16900 1.000 34.56518 ? 28  HIS B CD2 1 
ATOM   1355 C CE1 . HIS B 1 29  ? -11.42900 35.84700 -19.43000 1.000 30.80735 ? 28  HIS B CE1 1 
ATOM   1356 N NE2 . HIS B 1 29  ? -12.59400 35.26800 -19.21800 1.000 31.58497 ? 28  HIS B NE2 1 
ATOM   1357 N N   . ARG B 1 30  ? -15.62800 38.42000 -16.56500 1.000 30.81168 ? 29  ARG B N   1 
ATOM   1358 C CA  . ARG B 1 30  ? -16.97700 37.96400 -16.87900 1.000 34.58662 ? 29  ARG B CA  1 
ATOM   1359 C C   . ARG B 1 30  ? -17.77900 39.07300 -17.55100 1.000 37.92273 ? 29  ARG B C   1 
ATOM   1360 O O   . ARG B 1 30  ? -18.58900 38.80100 -18.44500 1.000 38.39193 ? 29  ARG B O   1 
ATOM   1361 C CB  . ARG B 1 30  ? -17.68700 37.43800 -15.62700 1.000 38.63841 ? 29  ARG B CB  1 
ATOM   1362 C CG  . ARG B 1 30  ? -18.41900 38.48600 -14.83700 1.000 42.72708 ? 29  ARG B CG  1 
ATOM   1363 C CD  . ARG B 1 30  ? -19.73500 37.93500 -14.43000 1.000 44.32362 ? 29  ARG B CD  1 
ATOM   1364 N NE  . ARG B 1 30  ? -20.55800 37.59300 -15.58500 1.000 52.91921 ? 29  ARG B NE  1 
ATOM   1365 C CZ  . ARG B 1 30  ? -21.78400 37.09200 -15.50400 1.000 50.25462 ? 29  ARG B CZ  1 
ATOM   1366 N NH1 . ARG B 1 30  ? -22.37800 36.91000 -14.33600 1.000 48.23838 ? 29  ARG B NH1 1 
ATOM   1367 N NH2 . ARG B 1 30  ? -22.42800 36.76800 -16.62400 1.000 41.70804 ? 29  ARG B NH2 1 
ATOM   1368 N N   . GLY B 1 31  ? -17.56500 40.33100 -17.14800 1.000 35.48455 ? 30  GLY B N   1 
ATOM   1369 C CA  . GLY B 1 31  ? -18.31600 41.41300 -17.75100 1.000 32.12844 ? 30  GLY B CA  1 
ATOM   1370 C C   . GLY B 1 31  ? -18.01900 41.56400 -19.22900 1.000 35.92761 ? 30  GLY B C   1 
ATOM   1371 O O   . GLY B 1 31  ? -18.91400 41.86800 -20.01900 1.000 37.10655 ? 30  GLY B O   1 
ATOM   1372 N N   . LEU B 1 32  ? -16.75100 41.38800 -19.61800 1.000 38.18955 ? 31  LEU B N   1 
ATOM   1373 C CA  . LEU B 1 32  ? -16.36000 41.62200 -21.00700 1.000 35.08003 ? 31  LEU B CA  1 
ATOM   1374 C C   . LEU B 1 32  ? -16.42200 40.38300 -21.90300 1.000 34.77983 ? 31  LEU B C   1 
ATOM   1375 O O   . LEU B 1 32  ? -16.47900 40.52600 -23.12600 1.000 30.68908 ? 31  LEU B O   1 
ATOM   1376 C CB  . LEU B 1 32  ? -14.94700 42.21900 -21.04000 1.000 33.02595 ? 31  LEU B CB  1 
ATOM   1377 C CG  . LEU B 1 32  ? -14.97600 43.66200 -20.52400 1.000 39.12990 ? 31  LEU B CG  1 
ATOM   1378 C CD1 . LEU B 1 32  ? -13.82500 44.53600 -21.05200 1.000 29.68241 ? 31  LEU B CD1 1 
ATOM   1379 C CD2 . LEU B 1 32  ? -16.32900 44.27000 -20.87100 1.000 34.52751 ? 31  LEU B CD2 1 
ATOM   1380 N N   . THR B 1 33  ? -16.37500 39.17700 -21.34400 1.000 34.36499 ? 32  THR B N   1 
ATOM   1381 C CA  . THR B 1 33  ? -16.35600 37.97900 -22.16500 1.000 32.90503 ? 32  THR B CA  1 
ATOM   1382 C C   . THR B 1 33  ? -17.62200 37.14700 -22.04300 1.000 34.51381 ? 32  THR B C   1 
ATOM   1383 O O   . THR B 1 33  ? -17.90600 36.36300 -22.94900 1.000 37.13917 ? 32  THR B O   1 
ATOM   1384 C CB  . THR B 1 33  ? -15.12700 37.09800 -21.84300 1.000 34.73532 ? 32  THR B CB  1 
ATOM   1385 O OG1 . THR B 1 33  ? -15.29000 36.43900 -20.58100 1.000 32.31719 ? 32  THR B OG1 1 
ATOM   1386 C CG2 . THR B 1 33  ? -13.85100 37.91600 -21.81000 1.000 31.46774 ? 32  THR B CG2 1 
ATOM   1387 N N   . GLY B 1 34  ? -18.36700 37.26700 -20.94100 1.000 42.17051 ? 33  GLY B N   1 
ATOM   1388 C CA  . GLY B 1 34  ? -19.52700 36.42200 -20.72300 1.000 38.92081 ? 33  GLY B CA  1 
ATOM   1389 C C   . GLY B 1 34  ? -19.21400 35.14000 -19.99100 1.000 32.72359 ? 33  GLY B C   1 
ATOM   1390 O O   . GLY B 1 34  ? -20.12200 34.34700 -19.73900 1.000 39.29697 ? 33  GLY B O   1 
ATOM   1391 N N   . THR B 1 35  ? -17.94500 34.89400 -19.69700 1.000 41.52720 ? 34  THR B N   1 
ATOM   1392 C CA  . THR B 1 35  ? -17.53100 33.69400 -18.99000 1.000 43.25367 ? 34  THR B CA  1 
ATOM   1393 C C   . THR B 1 35  ? -18.26900 33.61100 -17.65900 1.000 39.89785 ? 34  THR B C   1 
ATOM   1394 O O   . THR B 1 35  ? -18.52700 34.62400 -17.00600 1.000 46.48376 ? 34  THR B O   1 
ATOM   1395 C CB  . THR B 1 35  ? -16.00000 33.75500 -18.78900 1.000 34.09703 ? 34  THR B CB  1 
ATOM   1396 O OG1 . THR B 1 35  ? -15.35200 33.44100 -20.02500 1.000 38.88596 ? 34  THR B OG1 1 
ATOM   1397 C CG2 . THR B 1 35  ? -15.48700 32.81200 -17.70800 1.000 39.00325 ? 34  THR B CG2 1 
ATOM   1398 N N   . GLN B 1 36  ? -18.57100 32.39200 -17.22800 1.000 40.27403 ? 35  GLN B N   1 
ATOM   1399 C CA  . GLN B 1 36  ? -19.21800 32.23200 -15.93600 1.000 46.77882 ? 35  GLN B CA  1 
ATOM   1400 C C   . GLN B 1 36  ? -18.23100 32.55000 -14.82200 1.000 42.41449 ? 35  GLN B C   1 
ATOM   1401 O O   . GLN B 1 36  ? -17.03800 32.25300 -14.92600 1.000 42.88662 ? 35  GLN B O   1 
ATOM   1402 C CB  . GLN B 1 36  ? -19.79900 30.83000 -15.79100 1.000 52.00977 ? 35  GLN B CB  1 
ATOM   1403 C CG  . GLN B 1 36  ? -20.97000 30.57900 -16.72600 1.000 51.40984 ? 35  GLN B CG  1 
ATOM   1404 C CD  . GLN B 1 36  ? -20.64600 29.52800 -17.76600 1.000 52.92984 ? 35  GLN B CD  1 
ATOM   1405 O OE1 . GLN B 1 36  ? -19.47300 29.32600 -18.10700 1.000 47.16670 ? 35  GLN B OE1 1 
ATOM   1406 N NE2 . GLN B 1 36  ? -21.68300 28.84700 -18.28100 1.000 52.27295 ? 35  GLN B NE2 1 
ATOM   1407 N N   . HIS B 1 37  ? -18.73100 33.23800 -13.79500 1.000 41.19252 ? 36  HIS B N   1 
ATOM   1408 C CA  . HIS B 1 37  ? -17.89800 33.72600 -12.69700 1.000 49.93916 ? 36  HIS B CA  1 
ATOM   1409 C C   . HIS B 1 37  ? -16.86200 32.70400 -12.23300 1.000 45.54153 ? 36  HIS B C   1 
ATOM   1410 O O   . HIS B 1 37  ? -15.66200 32.99700 -12.15600 1.000 43.09248 ? 36  HIS B O   1 
ATOM   1411 C CB  . HIS B 1 37  ? -18.79200 34.08200 -11.50600 1.000 51.16369 ? 36  HIS B CB  1 
ATOM   1412 C CG  . HIS B 1 37  ? -19.06000 35.54000 -11.33100 1.000 47.65133 ? 36  HIS B CG  1 
ATOM   1413 N ND1 . HIS B 1 37  ? -18.33300 36.32800 -10.46600 1.000 50.46763 ? 36  HIS B ND1 1 
ATOM   1414 C CD2 . HIS B 1 37  ? -20.04500 36.32800 -11.81500 1.000 48.85916 ? 36  HIS B CD2 1 
ATOM   1415 C CE1 . HIS B 1 37  ? -18.82100 37.55300 -10.47100 1.000 38.75948 ? 36  HIS B CE1 1 
ATOM   1416 N NE2 . HIS B 1 37  ? -19.85700 37.58200 -11.28700 1.000 51.46727 ? 36  HIS B NE2 1 
ATOM   1417 N N   . PHE B 1 38  ? -17.32500 31.48800 -11.93500 1.000 43.54972 ? 37  PHE B N   1 
ATOM   1418 C CA  . PHE B 1 38  ? -16.53000 30.45300 -11.28900 1.000 39.90476 ? 37  PHE B CA  1 
ATOM   1419 C C   . PHE B 1 38  ? -15.41500 29.89500 -12.15600 1.000 41.43108 ? 37  PHE B C   1 
ATOM   1420 O O   . PHE B 1 38  ? -14.60300 29.11300 -11.65100 1.000 36.97402 ? 37  PHE B O   1 
ATOM   1421 C CB  . PHE B 1 38  ? -17.43500 29.30600 -10.85000 1.000 44.64011 ? 37  PHE B CB  1 
ATOM   1422 C CG  . PHE B 1 38  ? -18.42400 28.87700 -11.88600 1.000 39.75836 ? 37  PHE B CG  1 
ATOM   1423 C CD1 . PHE B 1 38  ? -18.00600 28.22800 -13.02900 1.000 36.79529 ? 37  PHE B CD1 1 
ATOM   1424 C CD2 . PHE B 1 38  ? -19.77600 29.08800 -11.69200 1.000 48.67837 ? 37  PHE B CD2 1 
ATOM   1425 C CE1 . PHE B 1 38  ? -18.90200 27.82200 -13.96800 1.000 42.74940 ? 37  PHE B CE1 1 
ATOM   1426 C CE2 . PHE B 1 38  ? -20.69700 28.68300 -12.63700 1.000 51.57731 ? 37  PHE B CE2 1 
ATOM   1427 C CZ  . PHE B 1 38  ? -20.25700 28.05400 -13.78000 1.000 54.62816 ? 37  PHE B CZ  1 
ATOM   1428 N N   . LEU B 1 39  ? -15.38400 30.23400 -13.44200 1.000 43.28202 ? 38  LEU B N   1 
ATOM   1429 C CA  . LEU B 1 39  ? -14.33200 29.76500 -14.33500 1.000 44.55229 ? 38  LEU B CA  1 
ATOM   1430 C C   . LEU B 1 39  ? -13.05600 30.58200 -14.20300 1.000 44.17161 ? 38  LEU B C   1 
ATOM   1431 O O   . LEU B 1 39  ? -12.04000 30.21700 -14.80300 1.000 40.41259 ? 38  LEU B O   1 
ATOM   1432 C CB  . LEU B 1 39  ? -14.82500 29.82000 -15.78300 1.000 41.26863 ? 38  LEU B CB  1 
ATOM   1433 C CG  . LEU B 1 39  ? -15.51100 28.53300 -16.26200 1.000 47.52575 ? 38  LEU B CG  1 
ATOM   1434 C CD1 . LEU B 1 39  ? -16.58100 28.86100 -17.27800 1.000 45.91502 ? 38  LEU B CD1 1 
ATOM   1435 C CD2 . LEU B 1 39  ? -14.51200 27.57400 -16.85700 1.000 42.49031 ? 38  LEU B CD2 1 
ATOM   1436 N N   . ALA B 1 40  ? -13.09300 31.68300 -13.45500 1.000 41.03235 ? 39  ALA B N   1 
ATOM   1437 C CA  . ALA B 1 40  ? -11.94300 32.56100 -13.31800 1.000 40.41413 ? 39  ALA B CA  1 
ATOM   1438 C C   . ALA B 1 40  ? -11.13800 32.17200 -12.08900 1.000 33.43176 ? 39  ALA B C   1 
ATOM   1439 O O   . ALA B 1 40  ? -11.63400 32.22600 -10.95500 1.000 32.54949 ? 39  ALA B O   1 
ATOM   1440 C CB  . ALA B 1 40  ? -12.36100 34.02500 -13.25600 1.000 38.92043 ? 39  ALA B CB  1 
ATOM   1441 N N   . GLN B 1 41  ? -9.92700  31.72100 -12.32800 1.000 22.15322 ? 40  GLN B N   1 
ATOM   1442 C CA  . GLN B 1 41  ? -8.96600  31.55700 -11.26400 1.000 28.47856 ? 40  GLN B CA  1 
ATOM   1443 C C   . GLN B 1 41  ? -8.17400  32.85300 -11.16100 1.000 31.66691 ? 40  GLN B C   1 
ATOM   1444 O O   . GLN B 1 41  ? -7.78900  33.42200 -12.18300 1.000 35.69724 ? 40  GLN B O   1 
ATOM   1445 C CB  . GLN B 1 41  ? -8.02800  30.39700 -11.56100 1.000 22.36012 ? 40  GLN B CB  1 
ATOM   1446 C CG  . GLN B 1 41  ? -7.02000  30.22100 -10.49800 1.000 25.53301 ? 40  GLN B CG  1 
ATOM   1447 C CD  . GLN B 1 41  ? -6.49600  28.80100 -10.48700 1.000 34.88132 ? 40  GLN B CD  1 
ATOM   1448 O OE1 . GLN B 1 41  ? -7.11700  27.89200 -11.05800 1.000 36.17328 ? 40  GLN B OE1 1 
ATOM   1449 N NE2 . GLN B 1 41  ? -5.35000  28.59500 -9.84000  1.000 25.64104 ? 40  GLN B NE2 1 
ATOM   1450 N N   . VAL B 1 42  ? -8.02600  33.37400 -9.95200  1.000 27.15876 ? 41  VAL B N   1 
ATOM   1451 C CA  . VAL B 1 42  ? -7.03500  34.39600 -9.66900  1.000 25.04419 ? 41  VAL B CA  1 
ATOM   1452 C C   . VAL B 1 42  ? -6.13300  33.74700 -8.64900  1.000 28.00996 ? 41  VAL B C   1 
ATOM   1453 O O   . VAL B 1 42  ? -6.60700  33.32800 -7.58600  1.000 30.03076 ? 41  VAL B O   1 
ATOM   1454 C CB  . VAL B 1 42  ? -7.65000  35.70400 -9.14200  1.000 26.82633 ? 41  VAL B CB  1 
ATOM   1455 C CG1 . VAL B 1 42  ? -6.56500  36.66800 -8.69600  1.000 26.17547 ? 41  VAL B CG1 1 
ATOM   1456 C CG2 . VAL B 1 42  ? -8.49900  36.35600 -10.19700 1.000 28.30884 ? 41  VAL B CG2 1 
ATOM   1457 N N   . ASN B 1 43  ? -4.85200  33.63000 -8.98300  1.000 30.42072 ? 42  ASN B N   1 
ATOM   1458 C CA  . ASN B 1 43  ? -3.86700  32.85000 -8.23700  1.000 29.31976 ? 42  ASN B CA  1 
ATOM   1459 C C   . ASN B 1 43  ? -2.72200  33.78400 -7.87600  1.000 26.47645 ? 42  ASN B C   1 
ATOM   1460 O O   . ASN B 1 43  ? -1.96100  34.21800 -8.74900  1.000 34.34743 ? 42  ASN B O   1 
ATOM   1461 C CB  . ASN B 1 43  ? -3.40200  31.65900 -9.08200  1.000 30.92325 ? 42  ASN B CB  1 
ATOM   1462 C CG  . ASN B 1 43  ? -2.60700  30.62400 -8.29100  1.000 31.41965 ? 42  ASN B CG  1 
ATOM   1463 O OD1 . ASN B 1 43  ? -1.56900  30.94200 -7.70400  1.000 31.38226 ? 42  ASN B OD1 1 
ATOM   1464 N ND2 . ASN B 1 43  ? -3.05800  29.36200 -8.33300  1.000 24.50468 ? 42  ASN B ND2 1 
ATOM   1465 N N   . PHE B 1 44  ? -2.61700  34.11400 -6.60200  1.000 26.56281 ? 43  PHE B N   1 
ATOM   1466 C CA  . PHE B 1 44  ? -1.66200  35.10900 -6.14100  1.000 32.00372 ? 43  PHE B CA  1 
ATOM   1467 C C   . PHE B 1 44  ? -0.31200  34.44500 -5.89400  1.000 35.30539 ? 43  PHE B C   1 
ATOM   1468 O O   . PHE B 1 44  ? -0.20700  33.52900 -5.07100  1.000 35.30004 ? 43  PHE B O   1 
ATOM   1469 C CB  . PHE B 1 44  ? -2.15600  35.81100 -4.86000  1.000 31.13513 ? 43  PHE B CB  1 
ATOM   1470 C CG  . PHE B 1 44  ? -3.33200  36.76400 -5.07200  1.000 25.47759 ? 43  PHE B CG  1 
ATOM   1471 C CD1 . PHE B 1 44  ? -3.12800  38.05500 -5.52800  1.000 20.27139 ? 43  PHE B CD1 1 
ATOM   1472 C CD2 . PHE B 1 44  ? -4.64700  36.35300 -4.80200  1.000 27.01005 ? 43  PHE B CD2 1 
ATOM   1473 C CE1 . PHE B 1 44  ? -4.19600  38.91600 -5.72100  1.000 23.98092 ? 43  PHE B CE1 1 
ATOM   1474 C CE2 . PHE B 1 44  ? -5.72600  37.21700 -4.99300  1.000 26.08587 ? 43  PHE B CE2 1 
ATOM   1475 C CZ  . PHE B 1 44  ? -5.49900  38.50400 -5.44800  1.000 25.52575 ? 43  PHE B CZ  1 
ATOM   1476 N N   . GLN B 1 45  ? 0.71800   34.92800 -6.59500  1.000 35.04776 ? 44  GLN B N   1 
ATOM   1477 C CA  . GLN B 1 45  ? 2.11100   34.56300 -6.37900  1.000 28.88174 ? 44  GLN B CA  1 
ATOM   1478 C C   . GLN B 1 45  ? 2.79900   35.71900 -5.66000  1.000 28.85026 ? 44  GLN B C   1 
ATOM   1479 O O   . GLN B 1 45  ? 3.09700   36.75500 -6.26700  1.000 29.02824 ? 44  GLN B O   1 
ATOM   1480 C CB  . GLN B 1 45  ? 2.78900   34.27200 -7.70600  1.000 32.44979 ? 44  GLN B CB  1 
ATOM   1481 C CG  . GLN B 1 45  ? 2.15700   33.16200 -8.44400  1.000 29.17604 ? 44  GLN B CG  1 
ATOM   1482 C CD  . GLN B 1 45  ? 2.22800   31.91200 -7.63500  1.000 28.99757 ? 44  GLN B CD  1 
ATOM   1483 O OE1 . GLN B 1 45  ? 1.20300   31.37700 -7.20600  1.000 26.50229 ? 44  GLN B OE1 1 
ATOM   1484 N NE2 . GLN B 1 45  ? 3.45200   31.44700 -7.38200  1.000 30.28327 ? 44  GLN B NE2 1 
ATOM   1485 N N   . GLU B 1 46  ? 3.03800   35.53600 -4.36700  1.000 31.30412 ? 45  GLU B N   1 
ATOM   1486 C CA  . GLU B 1 46  ? 3.70500   36.51100 -3.51200  1.000 34.18677 ? 45  GLU B CA  1 
ATOM   1487 C C   . GLU B 1 46  ? 5.17600   36.14000 -3.36200  1.000 35.44566 ? 45  GLU B C   1 
ATOM   1488 O O   . GLU B 1 46  ? 5.49200   34.98100 -3.07900  1.000 40.14079 ? 45  GLU B O   1 
ATOM   1489 C CB  . GLU B 1 46  ? 3.05600   36.57100 -2.12100  1.000 33.87727 ? 45  GLU B CB  1 
ATOM   1490 C CG  . GLU B 1 46  ? 1.54000   36.93800 -2.06200  1.000 34.54244 ? 45  GLU B CG  1 
ATOM   1491 C CD  . GLU B 1 46  ? 0.99900   36.91000 -0.62600  1.000 35.15683 ? 45  GLU B CD  1 
ATOM   1492 O OE1 . GLU B 1 46  ? 1.08800   35.83500 0.02300   1.000 37.35731 ? 45  GLU B OE1 1 
ATOM   1493 O OE2 . GLU B 1 46  ? 0.52300   37.96600 -0.13700  1.000 29.01615 ? 45  GLU B OE2 1 
ATOM   1494 N N   . GLN B 1 47  ? 6.06100   37.11600 -3.52700  1.000 29.89440 ? 46  GLN B N   1 
ATOM   1495 C CA  . GLN B 1 47  ? 7.47800   36.97700 -3.23000  1.000 35.51471 ? 46  GLN B CA  1 
ATOM   1496 C C   . GLN B 1 47  ? 7.95500   38.11000 -2.30400  1.000 37.49224 ? 46  GLN B C   1 
ATOM   1497 O O   . GLN B 1 47  ? 7.25700   39.10900 -2.13700  1.000 33.37776 ? 46  GLN B O   1 
ATOM   1498 C CB  . GLN B 1 47  ? 8.33200   36.95000 -4.50500  1.000 34.80046 ? 46  GLN B CB  1 
ATOM   1499 C CG  . GLN B 1 47  ? 7.99500   35.77100 -5.36000  1.000 32.74851 ? 46  GLN B CG  1 
ATOM   1500 C CD  . GLN B 1 47  ? 8.51100   34.48700 -4.76700  1.000 33.48160 ? 46  GLN B CD  1 
ATOM   1501 O OE1 . GLN B 1 47  ? 9.61700   34.43700 -4.22900  1.000 34.48659 ? 46  GLN B OE1 1 
ATOM   1502 N NE2 . GLN B 1 47  ? 7.68200   33.43900 -4.81400  1.000 39.59265 ? 46  GLN B NE2 1 
ATOM   1503 N N   . PRO B 1 48  ? 9.08900   37.91300 -1.63000  1.000 33.22571 ? 47  PRO B N   1 
ATOM   1504 C CA  . PRO B 1 48  ? 9.57500   38.99200 -0.75600  1.000 37.28262 ? 47  PRO B CA  1 
ATOM   1505 C C   . PRO B 1 48  ? 9.80000   40.27300 -1.54300  1.000 39.57285 ? 47  PRO B C   1 
ATOM   1506 O O   . PRO B 1 48  ? 10.39100  40.26000 -2.62600  1.000 33.99347 ? 47  PRO B O   1 
ATOM   1507 C CB  . PRO B 1 48  ? 10.90700  38.43500 -0.21900  1.000 39.62579 ? 47  PRO B CB  1 
ATOM   1508 C CG  . PRO B 1 48  ? 11.21300  37.19900 -1.03400  1.000 31.16336 ? 47  PRO B CG  1 
ATOM   1509 C CD  . PRO B 1 48  ? 9.85700   36.67900 -1.42100  1.000 35.85296 ? 47  PRO B CD  1 
ATOM   1510 N N   . ALA B 1 49  ? 9.33800   41.39400 -0.96800  1.000 43.13659 ? 48  ALA B N   1 
ATOM   1511 C CA  . ALA B 1 49  ? 9.57800   42.69300 -1.57900  1.000 32.09796 ? 48  ALA B CA  1 
ATOM   1512 C C   . ALA B 1 49  ? 11.06700  42.81400 -1.87100  1.000 38.48997 ? 48  ALA B C   1 
ATOM   1513 O O   . ALA B 1 49  ? 11.90000  42.29300 -1.12000  1.000 42.20722 ? 48  ALA B O   1 
ATOM   1514 C CB  . ALA B 1 49  ? 9.12100   43.83300 -0.66400  1.000 27.82482 ? 48  ALA B CB  1 
ATOM   1515 N N   . GLY B 1 50  ? 11.39600  43.39300 -3.02300  1.000 33.05346 ? 49  GLY B N   1 
ATOM   1516 C CA  . GLY B 1 50  ? 12.77500  43.49100 -3.44700  1.000 37.73807 ? 49  GLY B CA  1 
ATOM   1517 C C   . GLY B 1 50  ? 13.17100  42.43200 -4.45100  1.000 44.84926 ? 49  GLY B C   1 
ATOM   1518 O O   . GLY B 1 50  ? 14.28300  42.49700 -5.00300  1.000 35.33928 ? 49  GLY B O   1 
ATOM   1519 N N   . ASN B 1 51  ? 12.29200  41.45100 -4.68400  1.000 36.28930 ? 50  ASN B N   1 
ATOM   1520 C CA  . ASN B 1 51  ? 12.50600  40.43900 -5.69900  1.000 34.32138 ? 50  ASN B CA  1 
ATOM   1521 C C   . ASN B 1 51  ? 12.22300  40.96400 -7.10100  1.000 31.54523 ? 50  ASN B C   1 
ATOM   1522 O O   . ASN B 1 51  ? 12.53700  40.27100 -8.07300  1.000 31.29421 ? 50  ASN B O   1 
ATOM   1523 C CB  . ASN B 1 51  ? 11.63800  39.21100 -5.39800  1.000 35.65642 ? 50  ASN B CB  1 
ATOM   1524 C CG  . ASN B 1 51  ? 12.38700  38.16200 -4.59300  1.000 39.97046 ? 50  ASN B CG  1 
ATOM   1525 O OD1 . ASN B 1 51  ? 13.43400  38.45200 -3.99200  1.000 42.02067 ? 50  ASN B OD1 1 
ATOM   1526 N ND2 . ASN B 1 51  ? 11.87200  36.92900 -4.59300  1.000 33.25111 ? 50  ASN B ND2 1 
ATOM   1527 N N   . VAL B 1 52  ? 11.66600  42.17100 -7.21900  1.000 27.60140 ? 51  VAL B N   1 
ATOM   1528 C CA  . VAL B 1 52  ? 11.27600  42.75300 -8.49300  1.000 29.71318 ? 51  VAL B CA  1 
ATOM   1529 C C   . VAL B 1 52  ? 12.33500  43.76800 -8.91500  1.000 35.47774 ? 51  VAL B C   1 
ATOM   1530 O O   . VAL B 1 52  ? 12.69000  44.66800 -8.14100  1.000 33.13816 ? 51  VAL B O   1 
ATOM   1531 C CB  . VAL B 1 52  ? 9.89500   43.42600 -8.39000  1.000 34.03275 ? 51  VAL B CB  1 
ATOM   1532 C CG1 . VAL B 1 52  ? 9.77500   44.54200 -9.42300  1.000 33.09359 ? 51  VAL B CG1 1 
ATOM   1533 C CG2 . VAL B 1 52  ? 8.77000   42.41300 -8.55600  1.000 23.71941 ? 51  VAL B CG2 1 
ATOM   1534 N N   . PHE B 1 53  ? 12.87500  43.60600 -10.12400 1.000 31.88424 ? 52  PHE B N   1 
ATOM   1535 C CA  . PHE B 1 53  ? 13.76700  44.60500 -10.69500 1.000 29.25340 ? 52  PHE B CA  1 
ATOM   1536 C C   . PHE B 1 53  ? 13.21000  45.16300 -11.99800 1.000 33.15987 ? 52  PHE B C   1 
ATOM   1537 O O   . PHE B 1 53  ? 12.68700  44.43000 -12.84400 1.000 30.14980 ? 52  PHE B O   1 
ATOM   1538 C CB  . PHE B 1 53  ? 15.16400  44.07900 -10.93200 1.000 28.41316 ? 52  PHE B CB  1 
ATOM   1539 C CG  . PHE B 1 53  ? 15.80600  43.49800 -9.70800  1.000 31.50574 ? 52  PHE B CG  1 
ATOM   1540 C CD1 . PHE B 1 53  ? 15.29200  42.37300 -9.10500  1.000 33.47686 ? 52  PHE B CD1 1 
ATOM   1541 C CD2 . PHE B 1 53  ? 16.92200  44.08000 -9.16200  1.000 35.70121 ? 52  PHE B CD2 1 
ATOM   1542 C CE1 . PHE B 1 53  ? 15.88000  41.82100 -7.98200  1.000 40.30728 ? 52  PHE B CE1 1 
ATOM   1543 C CE2 . PHE B 1 53  ? 17.51800  43.54100 -8.03300  1.000 46.30745 ? 52  PHE B CE2 1 
ATOM   1544 C CZ  . PHE B 1 53  ? 16.98700  42.40500 -7.43300  1.000 42.08263 ? 52  PHE B CZ  1 
ATOM   1545 N N   . LEU B 1 54  ? 13.31300  46.47800 -12.13800 1.000 34.95085 ? 53  LEU B N   1 
ATOM   1546 C CA  . LEU B 1 54  ? 12.98100  47.18200 -13.36100 1.000 34.96667 ? 53  LEU B CA  1 
ATOM   1547 C C   . LEU B 1 54  ? 14.22600  47.97200 -13.76100 1.000 36.95685 ? 53  LEU B C   1 
ATOM   1548 O O   . LEU B 1 54  ? 14.80900  48.68200 -12.93500 1.000 35.13965 ? 53  LEU B O   1 
ATOM   1549 C CB  . LEU B 1 54  ? 11.75100  48.08700 -13.17800 1.000 33.75295 ? 53  LEU B CB  1 
ATOM   1550 C CG  . LEU B 1 54  ? 10.58300  47.56900 -12.32200 1.000 35.51972 ? 53  LEU B CG  1 
ATOM   1551 C CD1 . LEU B 1 54  ? 9.45900   48.60200 -12.20600 1.000 45.23811 ? 53  LEU B CD1 1 
ATOM   1552 C CD2 . LEU B 1 54  ? 10.01100  46.25000 -12.82900 1.000 37.32168 ? 53  LEU B CD2 1 
ATOM   1553 N N   . GLY B 1 55  ? 14.67600  47.78600 -14.99600 1.000 39.73225 ? 54  GLY B N   1 
ATOM   1554 C CA  . GLY B 1 55  ? 15.89300  48.42000 -15.46600 1.000 39.47453 ? 54  GLY B CA  1 
ATOM   1555 C C   . GLY B 1 55  ? 17.09400  48.15000 -14.59100 1.000 34.74804 ? 54  GLY B C   1 
ATOM   1556 O O   . GLY B 1 55  ? 18.01800  48.96000 -14.52800 1.000 30.61378 ? 54  GLY B O   1 
ATOM   1557 N N   . GLY B 1 56  ? 17.08000  47.01600 -13.89700 1.000 34.12984 ? 55  GLY B N   1 
ATOM   1558 C CA  . GLY B 1 56  ? 18.16200  46.67100 -13.00500 1.000 43.40771 ? 55  GLY B CA  1 
ATOM   1559 C C   . GLY B 1 56  ? 18.07600  47.27500 -11.61400 1.000 41.97771 ? 55  GLY B C   1 
ATOM   1560 O O   . GLY B 1 56  ? 18.86100  46.88200 -10.74500 1.000 35.53307 ? 55  GLY B O   1 
ATOM   1561 N N   . VAL B 1 57  ? 17.11700  48.16800 -11.35500 1.000 36.65112 ? 56  VAL B N   1 
ATOM   1562 C CA  . VAL B 1 57  ? 16.98600  48.81300 -10.05700 1.000 33.02231 ? 56  VAL B CA  1 
ATOM   1563 C C   . VAL B 1 57  ? 16.04300  47.97000 -9.21500  1.000 33.39191 ? 56  VAL B C   1 
ATOM   1564 O O   . VAL B 1 57  ? 14.95100  47.61500 -9.66400  1.000 36.43179 ? 56  VAL B O   1 
ATOM   1565 C CB  . VAL B 1 57  ? 16.47100  50.25600 -10.20700 1.000 34.51942 ? 56  VAL B CB  1 
ATOM   1566 C CG1 . VAL B 1 57  ? 15.81600  50.74300 -8.92500  1.000 35.76130 ? 56  VAL B CG1 1 
ATOM   1567 C CG2 . VAL B 1 57  ? 17.60800  51.17400 -10.54400 1.000 42.53619 ? 56  VAL B CG2 1 
ATOM   1568 N N   . GLN B 1 58  ? 16.47600  47.63000 -8.00200  1.000 37.00096 ? 57  GLN B N   1 
ATOM   1569 C CA  . GLN B 1 58  ? 15.64200  46.85000 -7.09600  1.000 37.26290 ? 57  GLN B CA  1 
ATOM   1570 C C   . GLN B 1 58  ? 14.44100  47.67600 -6.66700  1.000 38.03141 ? 57  GLN B C   1 
ATOM   1571 O O   . GLN B 1 58  ? 14.57100  48.86900 -6.36900  1.000 38.22934 ? 57  GLN B O   1 
ATOM   1572 C CB  . GLN B 1 58  ? 16.44800  46.45300 -5.86800  1.000 31.29883 ? 57  GLN B CB  1 
ATOM   1573 C CG  . GLN B 1 58  ? 16.14800  45.10200 -5.30800  1.000 40.68406 ? 57  GLN B CG  1 
ATOM   1574 C CD  . GLN B 1 58  ? 16.58500  44.98700 -3.86300  1.000 45.84843 ? 57  GLN B CD  1 
ATOM   1575 O OE1 . GLN B 1 58  ? 15.80400  44.58000 -3.00800  1.000 50.34118 ? 57  GLN B OE1 1 
ATOM   1576 N NE2 . GLN B 1 58  ? 17.82100  45.39000 -3.57400  1.000 42.02300 ? 57  GLN B NE2 1 
ATOM   1577 N N   . GLN B 1 59  ? 13.28900  47.02300 -6.54300  1.000 30.91688 ? 58  GLN B N   1 
ATOM   1578 C CA  . GLN B 1 59  ? 12.04800  47.73900 -6.28900  1.000 36.59794 ? 58  GLN B CA  1 
ATOM   1579 C C   . GLN B 1 59  ? 11.54000  47.42700 -4.88900  1.000 39.05314 ? 58  GLN B C   1 
ATOM   1580 O O   . GLN B 1 59  ? 11.89500  46.40700 -4.29300  1.000 41.63930 ? 58  GLN B O   1 
ATOM   1581 C CB  . GLN B 1 59  ? 10.98300  47.38200 -7.34200  1.000 36.31185 ? 58  GLN B CB  1 
ATOM   1582 C CG  . GLN B 1 59  ? 11.15600  48.10600 -8.66900  1.000 34.12390 ? 58  GLN B CG  1 
ATOM   1583 C CD  . GLN B 1 59  ? 10.71000  49.55600 -8.61100  1.000 47.07607 ? 58  GLN B CD  1 
ATOM   1584 O OE1 . GLN B 1 59  ? 11.52100  50.48800 -8.64800  1.000 42.01408 ? 58  GLN B OE1 1 
ATOM   1585 N NE2 . GLN B 1 59  ? 9.40300   49.75400 -8.52800  1.000 54.12850 ? 58  GLN B NE2 1 
ATOM   1586 N N   . GLY B 1 60  ? 10.72700  48.34200 -4.36000  1.000 37.53812 ? 59  GLY B N   1 
ATOM   1587 C CA  . GLY B 1 60  ? 9.93400   48.08100 -3.17800  1.000 40.32938 ? 59  GLY B CA  1 
ATOM   1588 C C   . GLY B 1 60  ? 8.79500   47.11700 -3.44200  1.000 42.06373 ? 59  GLY B C   1 
ATOM   1589 O O   . GLY B 1 60  ? 8.82200   46.36100 -4.41700  1.000 47.33775 ? 59  GLY B O   1 
ATOM   1590 N N   . GLY B 1 61  ? 7.78800   47.11300 -2.58000  1.000 40.19327 ? 60  GLY B N   1 
ATOM   1591 C CA  . GLY B 1 61  ? 6.82500   46.03300 -2.66300  1.000 45.64079 ? 60  GLY B CA  1 
ATOM   1592 C C   . GLY B 1 61  ? 5.56800   46.29600 -3.46500  1.000 42.12498 ? 60  GLY B C   1 
ATOM   1593 O O   . GLY B 1 61  ? 4.54700   45.64700 -3.22200  1.000 40.87662 ? 60  GLY B O   1 
ATOM   1594 N N   . ASP B 1 62  ? 5.61900   47.19800 -4.44800  1.000 41.30148 ? 61  ASP B N   1 
ATOM   1595 C CA  . ASP B 1 62  ? 4.38400   47.72500 -5.01000  1.000 41.74976 ? 61  ASP B CA  1 
ATOM   1596 C C   . ASP B 1 62  ? 4.05100   47.21000 -6.40000  1.000 41.59814 ? 61  ASP B C   1 
ATOM   1597 O O   . ASP B 1 62  ? 2.87200   47.25200 -6.78000  1.000 38.57491 ? 61  ASP B O   1 
ATOM   1598 C CB  . ASP B 1 62  ? 4.41300   49.26300 -5.05800  1.000 40.10069 ? 61  ASP B CB  1 
ATOM   1599 C CG  . ASP B 1 62  ? 3.78800   49.90800 -3.81200  1.000 46.06932 ? 61  ASP B CG  1 
ATOM   1600 O OD1 . ASP B 1 62  ? 3.96700   49.38500 -2.68100  1.000 38.92387 ? 61  ASP B OD1 1 
ATOM   1601 O OD2 . ASP B 1 62  ? 3.09200   50.94200 -3.97500  1.000 43.88567 ? 61  ASP B OD2 1 
ATOM   1602 N N   . THR B 1 63  ? 5.03600   46.73300 -7.16200  1.000 32.23253 ? 62  THR B N   1 
ATOM   1603 C CA  . THR B 1 63  ? 4.76300   46.30500 -8.52600  1.000 32.90356 ? 62  THR B CA  1 
ATOM   1604 C C   . THR B 1 63  ? 3.82600   45.09600 -8.55100  1.000 34.04925 ? 62  THR B C   1 
ATOM   1605 O O   . THR B 1 63  ? 4.08200   44.08000 -7.90400  1.000 33.80119 ? 62  THR B O   1 
ATOM   1606 C CB  . THR B 1 63  ? 6.07500   45.99600 -9.23700  1.000 29.93644 ? 62  THR B CB  1 
ATOM   1607 O OG1 . THR B 1 63  ? 6.98500   47.08500 -9.02100  1.000 37.85209 ? 62  THR B OG1 1 
ATOM   1608 C CG2 . THR B 1 63  ? 5.84400   45.81300 -10.73900 1.000 29.90618 ? 62  THR B CG2 1 
ATOM   1609 N N   . ILE B 1 64  ? 2.76800   45.18800 -9.34900  1.000 33.04593 ? 63  ILE B N   1 
ATOM   1610 C CA  . ILE B 1 64  ? 1.83200   44.09000 -9.54900  1.000 34.60565 ? 63  ILE B CA  1 
ATOM   1611 C C   . ILE B 1 64  ? 1.89100   43.67500 -11.00800 1.000 34.82342 ? 63  ILE B C   1 
ATOM   1612 O O   . ILE B 1 64  ? 1.68500   44.50800 -11.90000 1.000 35.35396 ? 63  ILE B O   1 
ATOM   1613 C CB  . ILE B 1 64  ? 0.39700   44.49100 -9.17500  1.000 35.04582 ? 63  ILE B CB  1 
ATOM   1614 C CG1 . ILE B 1 64  ? 0.25600   44.57300 -7.66100  1.000 34.44253 ? 63  ILE B CG1 1 
ATOM   1615 C CG2 . ILE B 1 64  ? -0.60500  43.48100 -9.75200  1.000 33.29145 ? 63  ILE B CG2 1 
ATOM   1616 C CD1 . ILE B 1 64  ? -0.55200  45.74000 -7.21200  1.000 29.69290 ? 63  ILE B CD1 1 
ATOM   1617 N N   . PHE B 1 65  ? 2.11600   42.38300 -11.24500 1.000 34.72890 ? 64  PHE B N   1 
ATOM   1618 C CA  . PHE B 1 65  ? 2.14300   41.84100 -12.59600 1.000 32.45824 ? 64  PHE B CA  1 
ATOM   1619 C C   . PHE B 1 65  ? 1.01700   40.83900 -12.74900 1.000 29.03701 ? 64  PHE B C   1 
ATOM   1620 O O   . PHE B 1 65  ? 0.93800   39.87800 -11.99500 1.000 32.35347 ? 64  PHE B O   1 
ATOM   1621 C CB  . PHE B 1 65  ? 3.49200   41.15900 -12.89900 1.000 34.17065 ? 64  PHE B CB  1 
ATOM   1622 C CG  . PHE B 1 65  ? 3.52400   40.40800 -14.22400 1.000 34.83806 ? 64  PHE B CG  1 
ATOM   1623 C CD1 . PHE B 1 65  ? 2.82300   40.87700 -15.33700 1.000 33.83848 ? 64  PHE B CD1 1 
ATOM   1624 C CD2 . PHE B 1 65  ? 4.22600   39.21700 -14.34600 1.000 30.64306 ? 64  PHE B CD2 1 
ATOM   1625 C CE1 . PHE B 1 65  ? 2.83700   40.17600 -16.53500 1.000 34.48761 ? 64  PHE B CE1 1 
ATOM   1626 C CE2 . PHE B 1 65  ? 4.23000   38.51600 -15.54100 1.000 27.37347 ? 64  PHE B CE2 1 
ATOM   1627 C CZ  . PHE B 1 65  ? 3.54900   38.99400 -16.63200 1.000 29.80423 ? 64  PHE B CZ  1 
ATOM   1628 N N   . VAL B 1 66  ? 0.18900   41.03100 -13.75900 1.000 31.69772 ? 65  VAL B N   1 
ATOM   1629 C CA  . VAL B 1 66  ? -0.94200  40.15900 -14.03900 1.000 31.95549 ? 65  VAL B CA  1 
ATOM   1630 C C   . VAL B 1 66  ? -0.65500  39.42400 -15.33500 1.000 30.93227 ? 65  VAL B C   1 
ATOM   1631 O O   . VAL B 1 66  ? -0.66600  40.03900 -16.40600 1.000 27.60909 ? 65  VAL B O   1 
ATOM   1632 C CB  . VAL B 1 66  ? -2.25400  40.93300 -14.17100 1.000 28.21489 ? 65  VAL B CB  1 
ATOM   1633 C CG1 . VAL B 1 66  ? -3.35700  39.93900 -14.52000 1.000 28.26097 ? 65  VAL B CG1 1 
ATOM   1634 C CG2 . VAL B 1 66  ? -2.54900  41.71800 -12.87900 1.000 29.11481 ? 65  VAL B CG2 1 
ATOM   1635 N N   . HIS B 1 67  ? -0.47100  38.10200 -15.24400 1.000 32.08463 ? 66  HIS B N   1 
ATOM   1636 C CA  . HIS B 1 67  ? -0.35900  37.21300 -16.38900 1.000 26.20773 ? 66  HIS B CA  1 
ATOM   1637 C C   . HIS B 1 67  ? -1.72400  36.50100 -16.56200 1.000 33.20827 ? 66  HIS B C   1 
ATOM   1638 O O   . HIS B 1 67  ? -2.04900  35.65400 -15.67700 1.000 28.14436 ? 66  HIS B O   1 
ATOM   1639 C CB  . HIS B 1 67  ? 0.80000   36.24300 -16.19600 1.000 28.44807 ? 66  HIS B CB  1 
ATOM   1640 C CG  . HIS B 1 67  ? 1.26100   35.56400 -17.45100 1.000 29.05384 ? 66  HIS B CG  1 
ATOM   1641 N ND1 . HIS B 1 67  ? 2.36200   34.73700 -17.48600 1.000 28.30926 ? 66  HIS B ND1 1 
ATOM   1642 C CD2 . HIS B 1 67  ? 0.78100   35.60000 -18.71500 1.000 28.66708 ? 66  HIS B CD2 1 
ATOM   1643 C CE1 . HIS B 1 67  ? 2.54200   34.29500 -18.71600 1.000 25.80263 ? 66  HIS B CE1 1 
ATOM   1644 N NE2 . HIS B 1 67  ? 1.59400   34.80000 -19.48100 1.000 21.34622 ? 66  HIS B NE2 1 
ATOM   1645 N N   . GLY B 1 68  ? -2.46100  36.84900 -17.51600 1.000 31.41341 ? 67  GLY B N   1 
ATOM   1646 C CA  . GLY B 1 68  ? -3.76800  36.25500 -17.79500 1.000 24.34625 ? 67  GLY B CA  1 
ATOM   1647 C C   . GLY B 1 68  ? -3.65800  35.16800 -18.96700 1.000 22.94942 ? 67  GLY B C   1 
ATOM   1648 O O   . GLY B 1 68  ? -3.08800  35.47900 -19.97900 1.000 25.63160 ? 67  GLY B O   1 
ATOM   1649 N N   . LEU B 1 69  ? -4.19200  34.02400 -18.65900 1.000 25.77397 ? 68  LEU B N   1 
ATOM   1650 C CA  . LEU B 1 69  ? -4.21000  32.93800 -19.64400 1.000 22.38585 ? 68  LEU B CA  1 
ATOM   1651 C C   . LEU B 1 69  ? -5.65000  32.71900 -20.11300 1.000 20.29773 ? 68  LEU B C   1 
ATOM   1652 O O   . LEU B 1 69  ? -6.51000  32.26100 -19.34800 1.000 20.48808 ? 68  LEU B O   1 
ATOM   1653 C CB  . LEU B 1 69  ? -3.56400  31.68900 -19.04500 1.000 18.91125 ? 68  LEU B CB  1 
ATOM   1654 C CG  . LEU B 1 69  ? -2.19400  32.05500 -18.45800 1.000 20.20272 ? 68  LEU B CG  1 
ATOM   1655 C CD1 . LEU B 1 69  ? -1.38700  30.86700 -17.84500 1.000 21.53802 ? 68  LEU B CD1 1 
ATOM   1656 C CD2 . LEU B 1 69  ? -1.34600  32.76200 -19.50900 1.000 26.52488 ? 68  LEU B CD2 1 
ATOM   1657 N N   . HIS B 1 70  ? -5.86900  32.98000 -21.40200 1.000 27.06589 ? 69  HIS B N   1 
ATOM   1658 C CA  . HIS B 1 70  ? -7.16400  33.04400 -22.06000 1.000 33.68585 ? 69  HIS B CA  1 
ATOM   1659 C C   . HIS B 1 70  ? -7.27000  31.94100 -23.11200 1.000 32.48432 ? 69  HIS B C   1 
ATOM   1660 O O   . HIS B 1 70  ? -6.26600  31.42200 -23.62500 1.000 32.65423 ? 69  HIS B O   1 
ATOM   1661 C CB  . HIS B 1 70  ? -7.38000  34.40800 -22.77300 1.000 30.61634 ? 69  HIS B CB  1 
ATOM   1662 C CG  . HIS B 1 70  ? -7.31900  35.61900 -21.88000 1.000 28.43123 ? 69  HIS B CG  1 
ATOM   1663 N ND1 . HIS B 1 70  ? -7.19200  35.55300 -20.50800 1.000 30.98734 ? 69  HIS B ND1 1 
ATOM   1664 C CD2 . HIS B 1 70  ? -7.38900  36.94000 -22.18300 1.000 29.29379 ? 69  HIS B CD2 1 
ATOM   1665 C CE1 . HIS B 1 70  ? -7.18600  36.77600 -20.00400 1.000 28.09552 ? 69  HIS B CE1 1 
ATOM   1666 N NE2 . HIS B 1 70  ? -7.30900  37.63600 -21.00000 1.000 30.78281 ? 69  HIS B NE2 1 
ATOM   1667 N N   . ARG B 1 71  ? -8.50700  31.63200 -23.47300 1.000 27.58193 ? 70  ARG B N   1 
ATOM   1668 C CA  . ARG B 1 71  ? -8.72500  30.86600 -24.68000 1.000 33.01965 ? 70  ARG B CA  1 
ATOM   1669 C C   . ARG B 1 71  ? -8.54500  31.76300 -25.88900 1.000 30.82377 ? 70  ARG B C   1 
ATOM   1670 O O   . ARG B 1 71  ? -8.79800  32.96700 -25.83900 1.000 32.81984 ? 70  ARG B O   1 
ATOM   1671 C CB  . ARG B 1 71  ? -10.14500 30.27900 -24.72900 1.000 36.05119 ? 70  ARG B CB  1 
ATOM   1672 C CG  . ARG B 1 71  ? -10.40100 29.18000 -23.75400 1.000 32.03236 ? 70  ARG B CG  1 
ATOM   1673 C CD  . ARG B 1 71  ? -11.86800 28.85900 -23.62900 1.000 42.21922 ? 70  ARG B CD  1 
ATOM   1674 N NE  . ARG B 1 71  ? -12.63400 29.87500 -22.92000 1.000 41.80074 ? 70  ARG B NE  1 
ATOM   1675 C CZ  . ARG B 1 71  ? -13.87700 30.21700 -23.24100 1.000 53.45402 ? 70  ARG B CZ  1 
ATOM   1676 N NH1 . ARG B 1 71  ? -14.54500 29.58000 -24.19500 1.000 56.55402 ? 70  ARG B NH1 1 
ATOM   1677 N NH2 . ARG B 1 71  ? -14.44300 31.25900 -22.63600 1.000 53.07804 ? 70  ARG B NH2 1 
ATOM   1678 N N   . GLU B 1 72  ? -8.12900  31.15600 -26.98900 1.000 28.92117 ? 71  GLU B N   1 
ATOM   1679 C CA  . GLU B 1 72  ? -8.05600  31.87200 -28.24600 1.000 27.61648 ? 71  GLU B CA  1 
ATOM   1680 C C   . GLU B 1 72  ? -9.47000  32.13100 -28.74400 1.000 31.32994 ? 71  GLU B C   1 
ATOM   1681 O O   . GLU B 1 72  ? -10.40600 31.39400 -28.40800 1.000 30.50721 ? 71  GLU B O   1 
ATOM   1682 C CB  . GLU B 1 72  ? -7.28400  31.05500 -29.28200 1.000 29.66724 ? 71  GLU B CB  1 
ATOM   1683 C CG  . GLU B 1 72  ? -5.77800  30.99800 -29.10200 1.000 33.27697 ? 71  GLU B CG  1 
ATOM   1684 C CD  . GLU B 1 72  ? -5.11500  30.14600 -30.16800 1.000 37.68138 ? 71  GLU B CD  1 
ATOM   1685 O OE1 . GLU B 1 72  ? -5.84500  29.40200 -30.87200 1.000 28.56911 ? 71  GLU B OE1 1 
ATOM   1686 O OE2 . GLU B 1 72  ? -3.87500  30.25900 -30.33000 1.000 41.42914 ? 71  GLU B OE2 1 
ATOM   1687 N N   . GLY B 1 73  ? -9.63100  33.18000 -29.55600 1.000 26.49509 ? 72  GLY B N   1 
ATOM   1688 C CA  . GLY B 1 73  ? -10.94900 33.40300 -30.11000 1.000 26.40418 ? 72  GLY B CA  1 
ATOM   1689 C C   . GLY B 1 73  ? -11.56200 34.76300 -29.86000 1.000 32.30198 ? 72  GLY B C   1 
ATOM   1690 O O   . GLY B 1 73  ? -12.65400 35.03000 -30.36600 1.000 32.52631 ? 72  GLY B O   1 
ATOM   1691 N N   . ARG B 1 74  ? -10.95300 35.58400 -29.00600 1.000 31.80620 ? 73  ARG B N   1 
ATOM   1692 C CA  . ARG B 1 74  ? -11.45600 36.92700 -28.72800 1.000 25.69288 ? 73  ARG B CA  1 
ATOM   1693 C C   . ARG B 1 74  ? -10.79400 37.99700 -29.60400 1.000 26.07542 ? 73  ARG B C   1 
ATOM   1694 O O   . ARG B 1 74  ? -9.63600  37.88700 -30.02100 1.000 23.65121 ? 73  ARG B O   1 
ATOM   1695 C CB  . ARG B 1 74  ? -11.24900 37.28700 -27.25700 1.000 26.50964 ? 73  ARG B CB  1 
ATOM   1696 C CG  . ARG B 1 74  ? -12.08300 36.41600 -26.33000 1.000 29.31132 ? 73  ARG B CG  1 
ATOM   1697 C CD  . ARG B 1 74  ? -12.04800 36.89000 -24.89200 1.000 33.14796 ? 73  ARG B CD  1 
ATOM   1698 N NE  . ARG B 1 74  ? -12.81700 35.98700 -24.04400 1.000 40.53517 ? 73  ARG B NE  1 
ATOM   1699 C CZ  . ARG B 1 74  ? -12.43400 34.75200 -23.75300 1.000 43.29428 ? 73  ARG B CZ  1 
ATOM   1700 N NH1 . ARG B 1 74  ? -11.29000 34.25700 -24.20800 1.000 40.17033 ? 73  ARG B NH1 1 
ATOM   1701 N NH2 . ARG B 1 74  ? -13.20400 34.00100 -22.97600 1.000 37.66617 ? 73  ARG B NH2 1 
ATOM   1702 N N   . SER B 1 75  ? -11.52800 39.07500 -29.83400 1.000 28.79058 ? 74  SER B N   1 
ATOM   1703 C CA  . SER B 1 75  ? -10.99800 40.09000 -30.72000 1.000 28.34534 ? 74  SER B CA  1 
ATOM   1704 C C   . SER B 1 75  ? -9.92300  40.88600 -30.00400 1.000 21.49392 ? 74  SER B C   1 
ATOM   1705 O O   . SER B 1 75  ? -9.91400  41.00000 -28.78200 1.000 20.75628 ? 74  SER B O   1 
ATOM   1706 C CB  . SER B 1 75  ? -12.10500 41.01500 -31.21600 1.000 22.76249 ? 74  SER B CB  1 
ATOM   1707 O OG  . SER B 1 75  ? -12.32100 42.04800 -30.29000 1.000 25.97213 ? 74  SER B OG  1 
ATOM   1708 N N   . ALA B 1 76  ? -9.00400  41.43700 -30.79100 1.000 23.91550 ? 75  ALA B N   1 
ATOM   1709 C CA  . ALA B 1 76  ? -7.98300  42.31000 -30.22500 1.000 26.38382 ? 75  ALA B CA  1 
ATOM   1710 C C   . ALA B 1 76  ? -8.60400  43.53900 -29.54400 1.000 28.98692 ? 75  ALA B C   1 
ATOM   1711 O O   . ALA B 1 76  ? -8.09700  44.02000 -28.52100 1.000 30.17478 ? 75  ALA B O   1 
ATOM   1712 C CB  . ALA B 1 76  ? -6.99800  42.70400 -31.32700 1.000 23.88468 ? 75  ALA B CB  1 
ATOM   1713 N N   . ASP B 1 77  ? -9.67900  44.09000 -30.10800 1.000 28.02737 ? 76  ASP B N   1 
ATOM   1714 C CA  . ASP B 1 77  ? -10.32400 45.22100 -29.44500 1.000 35.79695 ? 76  ASP B CA  1 
ATOM   1715 C C   . ASP B 1 77  ? -10.79900 44.86000 -28.03400 1.000 35.34609 ? 76  ASP B C   1 
ATOM   1716 O O   . ASP B 1 77  ? -10.50800 45.57400 -27.06300 1.000 36.07311 ? 76  ASP B O   1 
ATOM   1717 C CB  . ASP B 1 77  ? -11.49700 45.73500 -30.26700 1.000 34.07073 ? 76  ASP B CB  1 
ATOM   1718 C CG  . ASP B 1 77  ? -12.21700 46.86300 -29.56000 1.000 42.06722 ? 76  ASP B CG  1 
ATOM   1719 O OD1 . ASP B 1 77  ? -11.52500 47.72100 -28.94300 1.000 40.08907 ? 76  ASP B OD1 1 
ATOM   1720 O OD2 . ASP B 1 77  ? -13.46500 46.87600 -29.59700 1.000 46.57004 ? 76  ASP B OD2 1 
ATOM   1721 N N   . LEU B 1 78  ? -11.53700 43.75400 -27.90900 1.000 25.83193 ? 77  LEU B N   1 
ATOM   1722 C CA  . LEU B 1 78  ? -12.08400 43.34900 -26.62100 1.000 30.63570 ? 77  LEU B CA  1 
ATOM   1723 C C   . LEU B 1 78  ? -10.98200 42.95900 -25.63000 1.000 31.54908 ? 77  LEU B C   1 
ATOM   1724 O O   . LEU B 1 78  ? -11.13000 43.19800 -24.42600 1.000 33.91503 ? 77  LEU B O   1 
ATOM   1725 C CB  . LEU B 1 78  ? -13.06400 42.18900 -26.82100 1.000 29.47667 ? 77  LEU B CB  1 
ATOM   1726 C CG  . LEU B 1 78  ? -13.88900 41.73700 -25.61500 1.000 30.99748 ? 77  LEU B CG  1 
ATOM   1727 C CD1 . LEU B 1 78  ? -14.94600 42.76400 -25.34700 1.000 33.65535 ? 77  LEU B CD1 1 
ATOM   1728 C CD2 . LEU B 1 78  ? -14.53100 40.34400 -25.81300 1.000 32.28802 ? 77  LEU B CD2 1 
ATOM   1729 N N   . LYS B 1 79  ? -9.87600  42.35900 -26.09900 1.000 26.83280 ? 78  LYS B N   1 
ATOM   1730 C CA  . LYS B 1 79  ? -8.74700  42.12500 -25.19700 1.000 29.27388 ? 78  LYS B CA  1 
ATOM   1731 C C   . LYS B 1 79  ? -8.14700  43.45800 -24.72200 1.000 27.54324 ? 78  LYS B C   1 
ATOM   1732 O O   . LYS B 1 79  ? -7.74400  43.59200 -23.55900 1.000 25.73062 ? 78  LYS B O   1 
ATOM   1733 C CB  . LYS B 1 79  ? -7.68300  41.25900 -25.88200 1.000 30.89368 ? 78  LYS B CB  1 
ATOM   1734 C CG  . LYS B 1 79  ? -7.84000  39.71700 -25.72200 1.000 31.94820 ? 78  LYS B CG  1 
ATOM   1735 C CD  . LYS B 1 79  ? -6.83400  38.92500 -26.63400 1.000 27.44081 ? 78  LYS B CD  1 
ATOM   1736 C CE  . LYS B 1 79  ? -7.06600  39.23800 -28.12200 1.000 25.11906 ? 78  LYS B CE  1 
ATOM   1737 N NZ  . LYS B 1 79  ? -6.19600  38.54000 -29.10100 1.000 25.21754 ? 78  LYS B NZ  1 
ATOM   1738 N N   . GLY B 1 80  ? -8.10300  44.46400 -25.59800 1.000 26.91700 ? 79  GLY B N   1 
ATOM   1739 C CA  . GLY B 1 80  ? -7.62200  45.77400 -25.17700 1.000 24.88544 ? 79  GLY B CA  1 
ATOM   1740 C C   . GLY B 1 80  ? -8.50000  46.39200 -24.11000 1.000 27.94141 ? 79  GLY B C   1 
ATOM   1741 O O   . GLY B 1 80  ? -8.00000  46.94100 -23.12100 1.000 28.20354 ? 79  GLY B O   1 
ATOM   1742 N N   . GLN B 1 81  ? -9.82200  46.29600 -24.28800 1.000 25.45501 ? 80  GLN B N   1 
ATOM   1743 C CA  . GLN B 1 81  ? -10.73400 46.82400 -23.28000 1.000 29.62280 ? 80  GLN B CA  1 
ATOM   1744 C C   . GLN B 1 81  ? -10.57000 46.08500 -21.97100 1.000 28.55236 ? 80  GLN B C   1 
ATOM   1745 O O   . GLN B 1 81  ? -10.48400 46.70600 -20.90700 1.000 31.48292 ? 80  GLN B O   1 
ATOM   1746 C CB  . GLN B 1 81  ? -12.19100 46.70900 -23.70900 1.000 27.96152 ? 80  GLN B CB  1 
ATOM   1747 C CG  . GLN B 1 81  ? -12.59300 47.38600 -24.94000 1.000 25.45025 ? 80  GLN B CG  1 
ATOM   1748 C CD  . GLN B 1 81  ? -14.09400 47.38500 -25.00500 1.000 41.51816 ? 80  GLN B CD  1 
ATOM   1749 O OE1 . GLN B 1 81  ? -14.76300 48.00800 -24.15900 1.000 41.52624 ? 80  GLN B OE1 1 
ATOM   1750 N NE2 . GLN B 1 81  ? -14.65000 46.64500 -25.97000 1.000 36.41406 ? 80  GLN B NE2 1 
ATOM   1751 N N   . LEU B 1 82  ? -10.52500 44.74700 -22.03400 1.000 34.19868 ? 81  LEU B N   1 
ATOM   1752 C CA  . LEU B 1 82  ? -10.43900 43.94200 -20.81600 1.000 31.98474 ? 81  LEU B CA  1 
ATOM   1753 C C   . LEU B 1 82  ? -9.16800  44.25600 -20.04000 1.000 27.90587 ? 81  LEU B C   1 
ATOM   1754 O O   . LEU B 1 82  ? -9.20100  44.40000 -18.81000 1.000 29.25602 ? 81  LEU B O   1 
ATOM   1755 C CB  . LEU B 1 82  ? -10.51700 42.44900 -21.15800 1.000 28.15409 ? 81  LEU B CB  1 
ATOM   1756 C CG  . LEU B 1 82  ? -10.26700 41.58200 -19.91600 1.000 31.23303 ? 81  LEU B CG  1 
ATOM   1757 C CD1 . LEU B 1 82  ? -11.25900 41.97800 -18.78400 1.000 29.22144 ? 81  LEU B CD1 1 
ATOM   1758 C CD2 . LEU B 1 82  ? -10.26400 40.06900 -20.20500 1.000 24.83655 ? 81  LEU B CD2 1 
ATOM   1759 N N   . ALA B 1 83  ? -8.03800  44.36700 -20.74000 1.000 24.68227 ? 82  ALA B N   1 
ATOM   1760 C CA  . ALA B 1 83  ? -6.78500  44.67400 -20.06100 1.000 25.01430 ? 82  ALA B CA  1 
ATOM   1761 C C   . ALA B 1 83  ? -6.81100  46.08500 -19.45900 1.000 27.71095 ? 82  ALA B C   1 
ATOM   1762 O O   . ALA B 1 83  ? -6.35800  46.28300 -18.32400 1.000 28.02699 ? 82  ALA B O   1 
ATOM   1763 C CB  . ALA B 1 83  ? -5.61400  44.47300 -21.03600 1.000 25.34686 ? 82  ALA B CB  1 
ATOM   1764 N N   . GLN B 1 84  ? -7.33300  47.08100 -20.19000 1.000 26.06679 ? 83  GLN B N   1 
ATOM   1765 C CA  . GLN B 1 84  ? -7.46900  48.41400 -19.59100 1.000 29.98807 ? 83  GLN B CA  1 
ATOM   1766 C C   . GLN B 1 84  ? -8.35100  48.37700 -18.35500 1.000 31.36815 ? 83  GLN B C   1 
ATOM   1767 O O   . GLN B 1 84  ? -8.08700  49.06000 -17.35400 1.000 26.20344 ? 83  GLN B O   1 
ATOM   1768 C CB  . GLN B 1 84  ? -8.08500  49.41500 -20.56700 1.000 29.40081 ? 83  GLN B CB  1 
ATOM   1769 C CG  . GLN B 1 84  ? -8.19200  50.84500 -19.97900 1.000 38.39999 ? 83  GLN B CG  1 
ATOM   1770 C CD  . GLN B 1 84  ? -6.81900  51.44300 -19.64700 1.000 35.95476 ? 83  GLN B CD  1 
ATOM   1771 O OE1 . GLN B 1 84  ? -6.00800  51.71300 -20.54300 1.000 39.66254 ? 83  GLN B OE1 1 
ATOM   1772 N NE2 . GLN B 1 84  ? -6.54100  51.61700 -18.35300 1.000 36.36293 ? 83  GLN B NE2 1 
ATOM   1773 N N   . ARG B 1 85  ? -9.45100  47.64500 -18.43500 1.000 31.74617 ? 84  ARG B N   1 
ATOM   1774 C CA  . ARG B 1 85  ? -10.34400 47.65300 -17.30200 1.000 29.77582 ? 84  ARG B CA  1 
ATOM   1775 C C   . ARG B 1 85  ? -9.70700  46.95200 -16.11200 1.000 31.23900 ? 84  ARG B C   1 
ATOM   1776 O O   . ARG B 1 85  ? -9.92100  47.37700 -14.98100 1.000 30.99397 ? 84  ARG B O   1 
ATOM   1777 C CB  . ARG B 1 85  ? -11.69200 47.07600 -17.70400 1.000 28.47502 ? 84  ARG B CB  1 
ATOM   1778 C CG  . ARG B 1 85  ? -12.67400 47.14100 -16.57900 1.000 34.46366 ? 84  ARG B CG  1 
ATOM   1779 C CD  . ARG B 1 85  ? -13.41900 45.86500 -16.53100 1.000 37.10749 ? 84  ARG B CD  1 
ATOM   1780 N NE  . ARG B 1 85  ? -14.45700 45.89600 -17.54500 1.000 40.07337 ? 84  ARG B NE  1 
ATOM   1781 C CZ  . ARG B 1 85  ? -15.75400 45.90500 -17.29000 1.000 38.36739 ? 84  ARG B CZ  1 
ATOM   1782 N NH1 . ARG B 1 85  ? -16.21200 45.78100 -16.05600 1.000 38.40607 ? 84  ARG B NH1 1 
ATOM   1783 N NH2 . ARG B 1 85  ? -16.60700 46.10500 -18.29000 1.000 33.40539 ? 84  ARG B NH2 1 
ATOM   1784 N N   . ILE B 1 86  ? -8.89000  45.91600 -16.34500 1.000 32.14902 ? 85  ILE B N   1 
ATOM   1785 C CA  . ILE B 1 86  ? -8.13100  45.29800 -15.25600 1.000 27.11336 ? 85  ILE B CA  1 
ATOM   1786 C C   . ILE B 1 86  ? -7.13100  46.29800 -14.67100 1.000 26.19796 ? 85  ILE B C   1 
ATOM   1787 O O   . ILE B 1 86  ? -6.93200  46.35600 -13.45300 1.000 24.39593 ? 85  ILE B O   1 
ATOM   1788 C CB  . ILE B 1 86  ? -7.41500  44.02200 -15.74100 1.000 29.05067 ? 85  ILE B CB  1 
ATOM   1789 C CG1 . ILE B 1 86  ? -8.36900  42.83100 -15.81500 1.000 27.43772 ? 85  ILE B CG1 1 
ATOM   1790 C CG2 . ILE B 1 86  ? -6.17100  43.72000 -14.86200 1.000 26.30510 ? 85  ILE B CG2 1 
ATOM   1791 C CD1 . ILE B 1 86  ? -7.72800  41.59600 -16.44400 1.000 20.68614 ? 85  ILE B CD1 1 
ATOM   1792 N N   . VAL B 1 87  ? -6.43800  47.04700 -15.52900 1.000 24.30368 ? 86  VAL B N   1 
ATOM   1793 C CA  . VAL B 1 87  ? -5.55800  48.12000 -15.04200 1.000 27.43208 ? 86  VAL B CA  1 
ATOM   1794 C C   . VAL B 1 87  ? -6.32200  49.03800 -14.08300 1.000 31.11677 ? 86  VAL B C   1 
ATOM   1795 O O   . VAL B 1 87  ? -5.91400  49.25400 -12.93300 1.000 32.28949 ? 86  VAL B O   1 
ATOM   1796 C CB  . VAL B 1 87  ? -4.96700  48.91100 -16.22600 1.000 29.31922 ? 86  VAL B CB  1 
ATOM   1797 C CG1 . VAL B 1 87  ? -4.47200  50.28400 -15.77600 1.000 29.28374 ? 86  VAL B CG1 1 
ATOM   1798 C CG2 . VAL B 1 87  ? -3.85100  48.11100 -16.90400 1.000 24.66314 ? 86  VAL B CG2 1 
ATOM   1799 N N   . ASP B 1 88  ? -7.47200  49.54800 -14.53200 1.000 23.09862 ? 87  ASP B N   1 
ATOM   1800 C CA  . ASP B 1 88  ? -8.26700  50.45700 -13.70800 1.000 34.52375 ? 87  ASP B CA  1 
ATOM   1801 C C   . ASP B 1 88  ? -8.72600  49.78800 -12.41300 1.000 33.32908 ? 87  ASP B C   1 
ATOM   1802 O O   . ASP B 1 88  ? -8.59700  50.35400 -11.31500 1.000 30.19886 ? 87  ASP B O   1 
ATOM   1803 C CB  . ASP B 1 88  ? -9.49000  50.93800 -14.49400 1.000 37.63172 ? 87  ASP B CB  1 
ATOM   1804 C CG  . ASP B 1 88  ? -10.28600 52.02300 -13.74900 1.000 55.22686 ? 87  ASP B CG  1 
ATOM   1805 O OD1 . ASP B 1 88  ? -9.92000  52.36900 -12.59900 1.000 52.96335 ? 87  ASP B OD1 1 
ATOM   1806 O OD2 . ASP B 1 88  ? -11.24800 52.58100 -14.34100 1.000 72.92796 ? 87  ASP B OD2 1 
ATOM   1807 N N   . ASP B 1 89  ? -9.31100  48.59800 -12.53100 1.000 32.01660 ? 88  ASP B N   1 
ATOM   1808 C CA  . ASP B 1 89  ? -9.96700  47.96300 -11.40500 1.000 24.80688 ? 88  ASP B CA  1 
ATOM   1809 C C   . ASP B 1 89  ? -8.97800  47.38800 -10.40500 1.000 27.98225 ? 88  ASP B C   1 
ATOM   1810 O O   . ASP B 1 89  ? -9.28400  47.34800 -9.21300  1.000 34.45194 ? 88  ASP B O   1 
ATOM   1811 C CB  . ASP B 1 89  ? -10.94000 46.90900 -11.92400 1.000 29.45001 ? 88  ASP B CB  1 
ATOM   1812 C CG  . ASP B 1 89  ? -12.01900 47.52500 -12.80300 1.000 28.61399 ? 88  ASP B CG  1 
ATOM   1813 O OD1 . ASP B 1 89  ? -11.90000 48.73800 -13.05800 1.000 38.65508 ? 88  ASP B OD1 1 
ATOM   1814 O OD2 . ASP B 1 89  ? -12.95300 46.82900 -13.26300 1.000 29.58133 ? 88  ASP B OD2 1 
ATOM   1815 N N   . VAL B 1 90  ? -7.79400  46.95200 -10.83200 1.000 24.28945 ? 89  VAL B N   1 
ATOM   1816 C CA  . VAL B 1 90  ? -6.78500  46.59500 -9.84000  1.000 25.09314 ? 89  VAL B CA  1 
ATOM   1817 C C   . VAL B 1 90  ? -6.22500  47.85800 -9.19100  1.000 30.41593 ? 89  VAL B C   1 
ATOM   1818 O O   . VAL B 1 90  ? -5.92700  47.85600 -7.99100  1.000 35.88624 ? 89  VAL B O   1 
ATOM   1819 C CB  . VAL B 1 90  ? -5.68600  45.71400 -10.45700 1.000 29.49117 ? 89  VAL B CB  1 
ATOM   1820 C CG1 . VAL B 1 90  ? -4.56700  45.45400 -9.44100  1.000 23.47767 ? 89  VAL B CG1 1 
ATOM   1821 C CG2 . VAL B 1 90  ? -6.29300  44.37600 -10.97300 1.000 29.00855 ? 89  VAL B CG2 1 
ATOM   1822 N N   . SER B 1 91  ? -6.08000  48.95700 -9.95200  1.000 27.25530 ? 90  SER B N   1 
ATOM   1823 C CA  . SER B 1 91  ? -5.74200  50.23700 -9.33200  1.000 28.26166 ? 90  SER B CA  1 
ATOM   1824 C C   . SER B 1 91  ? -6.67300  50.54200 -8.17900  1.000 30.94251 ? 90  SER B C   1 
ATOM   1825 O O   . SER B 1 91  ? -6.22500  50.90900 -7.08600  1.000 27.17500 ? 90  SER B O   1 
ATOM   1826 C CB  . SER B 1 91  ? -5.86800  51.38400 -10.33800 1.000 28.12555 ? 90  SER B CB  1 
ATOM   1827 O OG  . SER B 1 91  ? -4.66300  51.69000 -10.98000 1.000 37.49024 ? 90  SER B OG  1 
ATOM   1828 N N   . VAL B 1 92  ? -7.97600  50.32900 -8.39100  1.000 32.12044 ? 91  VAL B N   1 
ATOM   1829 C CA  . VAL B 1 92  ? -8.95300  50.69600 -7.36900  1.000 34.94216 ? 91  VAL B CA  1 
ATOM   1830 C C   . VAL B 1 92  ? -8.98300  49.67500 -6.23100  1.000 32.40057 ? 91  VAL B C   1 
ATOM   1831 O O   . VAL B 1 92  ? -8.86000  50.04300 -5.05600  1.000 31.05065 ? 91  VAL B O   1 
ATOM   1832 C CB  . VAL B 1 92  ? -10.33900 50.88200 -8.00700  1.000 35.64693 ? 91  VAL B CB  1 
ATOM   1833 C CG1 . VAL B 1 92  ? -11.41400 50.89900 -6.92000  1.000 31.13220 ? 91  VAL B CG1 1 
ATOM   1834 C CG2 . VAL B 1 92  ? -10.36400 52.15400 -8.80600  1.000 25.99604 ? 91  VAL B CG2 1 
ATOM   1835 N N   . ALA B 1 93  ? -9.13800  48.38300 -6.55700  1.000 33.28872 ? 92  ALA B N   1 
ATOM   1836 C CA  . ALA B 1 93  ? -9.22300  47.33800 -5.53800  1.000 31.98549 ? 92  ALA B CA  1 
ATOM   1837 C C   . ALA B 1 93  ? -7.99300  47.33100 -4.63300  1.000 35.40629 ? 92  ALA B C   1 
ATOM   1838 O O   . ALA B 1 93  ? -8.11100  47.27500 -3.40300  1.000 34.33775 ? 92  ALA B O   1 
ATOM   1839 C CB  . ALA B 1 93  ? -9.40000  45.97100 -6.20700  1.000 33.38230 ? 92  ALA B CB  1 
ATOM   1840 N N   . ALA B 1 94  ? -6.79800  47.36500 -5.22500  1.000 34.46234 ? 93  ALA B N   1 
ATOM   1841 C CA  . ALA B 1 94  ? -5.57400  47.35000 -4.43800  1.000 31.91977 ? 93  ALA B CA  1 
ATOM   1842 C C   . ALA B 1 94  ? -5.20000  48.72700 -3.91400  1.000 34.10539 ? 93  ALA B C   1 
ATOM   1843 O O   . ALA B 1 94  ? -4.30400  48.83100 -3.06500  1.000 35.92180 ? 93  ALA B O   1 
ATOM   1844 C CB  . ALA B 1 94  ? -4.41600  46.81800 -5.28800  1.000 35.26649 ? 93  ALA B CB  1 
ATOM   1845 N N   . GLU B 1 95  ? -5.83800  49.77700 -4.43200  1.000 32.93533 ? 94  GLU B N   1 
ATOM   1846 C CA  . GLU B 1 95  ? -5.59100  51.15600 -4.01100  1.000 37.04736 ? 94  GLU B CA  1 
ATOM   1847 C C   . GLU B 1 95  ? -4.12800  51.52200 -4.25800  1.000 33.81224 ? 94  GLU B C   1 
ATOM   1848 O O   . GLU B 1 95  ? -3.41800  51.96700 -3.36100  1.000 36.90771 ? 94  GLU B O   1 
ATOM   1849 C CB  . GLU B 1 95  ? -5.98500  51.40200 -2.55600  1.000 33.95908 ? 94  GLU B CB  1 
ATOM   1850 C CG  . GLU B 1 95  ? -7.34000  52.10200 -2.36200  1.000 37.65323 ? 94  GLU B CG  1 
ATOM   1851 C CD  . GLU B 1 95  ? -7.68200  53.13200 -3.44900  1.000 37.11071 ? 94  GLU B CD  1 
ATOM   1852 O OE1 . GLU B 1 95  ? -6.88300  54.03000 -3.73900  1.000 40.76875 ? 94  GLU B OE1 1 
ATOM   1853 O OE2 . GLU B 1 95  ? -8.81900  53.13300 -3.94600  1.000 44.49524 ? 94  GLU B OE2 1 
ATOM   1854 N N   . ILE B 1 96  ? -3.67000  51.23400 -5.47400  1.000 30.03757 ? 95  ILE B N   1 
ATOM   1855 C CA  . ILE B 1 96  ? -2.30700  51.44900 -5.92500  1.000 27.55499 ? 95  ILE B CA  1 
ATOM   1856 C C   . ILE B 1 96  ? -2.33600  52.18800 -7.27100  1.000 37.22433 ? 95  ILE B C   1 
ATOM   1857 O O   . ILE B 1 96  ? -3.27900  52.04800 -8.05700  1.000 33.26964 ? 95  ILE B O   1 
ATOM   1858 C CB  . ILE B 1 96  ? -1.57500  50.09000 -6.01400  1.000 30.93934 ? 95  ILE B CB  1 
ATOM   1859 C CG1 . ILE B 1 96  ? -0.07600  50.29300 -6.16600  1.000 36.64398 ? 95  ILE B CG1 1 
ATOM   1860 C CG2 . ILE B 1 96  ? -2.09600  49.25500 -7.17400  1.000 34.51323 ? 95  ILE B CG2 1 
ATOM   1861 C CD1 . ILE B 1 96  ? 0.61200   49.05400 -6.49500  1.000 37.33807 ? 95  ILE B CD1 1 
ATOM   1862 N N   . ASP B 1 97  ? -1.28900  52.97500 -7.54100  1.000 30.28723 ? 96  ASP B N   1 
ATOM   1863 C CA  . ASP B 1 97  ? -1.20700  53.66600 -8.81900  1.000 34.05731 ? 96  ASP B CA  1 
ATOM   1864 C C   . ASP B 1 97  ? -0.97500  52.68900 -9.96700  1.000 36.13218 ? 96  ASP B C   1 
ATOM   1865 O O   . ASP B 1 97  ? -0.32700  51.65200 -9.81200  1.000 39.72535 ? 96  ASP B O   1 
ATOM   1866 C CB  . ASP B 1 97  ? -0.08000  54.70800 -8.82900  1.000 38.54116 ? 96  ASP B CB  1 
ATOM   1867 C CG  . ASP B 1 97  ? -0.12600  55.61500 -10.08300 1.000 46.33608 ? 96  ASP B CG  1 
ATOM   1868 O OD1 . ASP B 1 97  ? -0.95800  55.38700 -10.99400 1.000 45.66206 ? 96  ASP B OD1 1 
ATOM   1869 O OD2 . ASP B 1 97  ? 0.69200   56.54900 -10.18000 1.000 50.96286 ? 96  ASP B OD2 1 
ATOM   1870 N N   . ARG B 1 98  ? -1.49000  53.08200 -11.14200 1.000 36.60141 ? 97  ARG B N   1 
ATOM   1871 C CA  . ARG B 1 98  ? -1.32500  52.35200 -12.39500 1.000 34.98351 ? 97  ARG B CA  1 
ATOM   1872 C C   . ARG B 1 98  ? 0.12800   52.09800 -12.76600 1.000 35.40357 ? 97  ARG B C   1 
ATOM   1873 O O   . ARG B 1 98  ? 0.42900   51.07200 -13.38500 1.000 32.35396 ? 97  ARG B O   1 
ATOM   1874 C CB  . ARG B 1 98  ? -2.02400  53.11900 -13.52100 1.000 37.54803 ? 97  ARG B CB  1 
ATOM   1875 C CG  . ARG B 1 98  ? -3.53400  53.07200 -13.40300 1.000 39.86215 ? 97  ARG B CG  1 
ATOM   1876 C CD  . ARG B 1 98  ? -4.25100  54.15900 -14.16000 1.000 40.67989 ? 97  ARG B CD  1 
ATOM   1877 N NE  . ARG B 1 98  ? -5.67400  54.17500 -13.82000 1.000 57.61112 ? 97  ARG B NE  1 
ATOM   1878 C CZ  . ARG B 1 98  ? -6.18100  54.54600 -12.64700 1.000 52.51164 ? 97  ARG B CZ  1 
ATOM   1879 N NH1 . ARG B 1 98  ? -5.44600  55.18300 -11.74600 1.000 39.88564 ? 97  ARG B NH1 1 
ATOM   1880 N NH2 . ARG B 1 98  ? -7.47900  54.33800 -12.40400 1.000 44.56963 ? 97  ARG B NH2 1 
ATOM   1881 N N   . LYS B 1 99  ? 1.05300   52.98700 -12.38900 1.000 38.33758 ? 98  LYS B N   1 
ATOM   1882 C CA  . LYS B 1 99  ? 2.41300   52.82800 -12.89500 1.000 41.85028 ? 98  LYS B CA  1 
ATOM   1883 C C   . LYS B 1 99  ? 3.01700   51.49500 -12.48300 1.000 46.74324 ? 98  LYS B C   1 
ATOM   1884 O O   . LYS B 1 99  ? 3.97100   51.02200 -13.12900 1.000 42.24809 ? 98  LYS B O   1 
ATOM   1885 C CB  . LYS B 1 99  ? 3.34900   53.91300 -12.36600 1.000 41.55186 ? 98  LYS B CB  1 
ATOM   1886 C CG  . LYS B 1 99  ? 2.96700   54.56200 -11.04800 1.000 45.98666 ? 98  LYS B CG  1 
ATOM   1887 C CD  . LYS B 1 99  ? 4.05500   55.58500 -10.64500 1.000 54.21948 ? 98  LYS B CD  1 
ATOM   1888 C CE  . LYS B 1 99  ? 3.65000   56.53700 -9.51700  1.000 54.17009 ? 98  LYS B CE  1 
ATOM   1889 N NZ  . LYS B 1 99  ? 4.78100   56.80800 -8.58000  1.000 56.32143 ? 98  LYS B NZ  1 
ATOM   1890 N N   . HIS B 1 100 ? 2.43700   50.86800 -11.45500 1.000 43.55963 ? 99  HIS B N   1 
ATOM   1891 C CA  . HIS B 1 100 ? 2.90400   49.62500 -10.86700 1.000 42.16536 ? 99  HIS B CA  1 
ATOM   1892 C C   . HIS B 1 100 ? 2.18600   48.40500 -11.42300 1.000 39.15448 ? 99  HIS B C   1 
ATOM   1893 O O   . HIS B 1 100 ? 2.35600   47.30200 -10.88500 1.000 35.11826 ? 99  HIS B O   1 
ATOM   1894 C CB  . HIS B 1 100 ? 2.71300   49.70000 -9.35600  1.000 38.12239 ? 99  HIS B CB  1 
ATOM   1895 C CG  . HIS B 1 100 ? 3.66300   50.62700 -8.67700  1.000 38.61696 ? 99  HIS B CG  1 
ATOM   1896 N ND1 . HIS B 1 100 ? 3.28800   51.43800 -7.62900  1.000 38.66474 ? 99  HIS B ND1 1 
ATOM   1897 C CD2 . HIS B 1 100 ? 4.97500   50.87500 -8.89900  1.000 43.16752 ? 99  HIS B CD2 1 
ATOM   1898 C CE1 . HIS B 1 100 ? 4.33100   52.15000 -7.23700  1.000 46.01169 ? 99  HIS B CE1 1 
ATOM   1899 N NE2 . HIS B 1 100 ? 5.36700   51.82700 -7.98900  1.000 42.66942 ? 99  HIS B NE2 1 
ATOM   1900 N N   . ILE B 1 101 ? 1.35500   48.58600 -12.45100 1.000 38.69392 ? 100 ILE B N   1 
ATOM   1901 C CA  . ILE B 1 101 ? 0.47100   47.53300 -12.94400 1.000 36.47366 ? 100 ILE B CA  1 
ATOM   1902 C C   . ILE B 1 101 ? 0.91300   47.15600 -14.34900 1.000 30.66897 ? 100 ILE B C   1 
ATOM   1903 O O   . ILE B 1 101 ? 0.74900   47.94800 -15.29200 1.000 26.93022 ? 100 ILE B O   1 
ATOM   1904 C CB  . ILE B 1 101 ? -1.00500  47.96700 -12.93600 1.000 34.66064 ? 100 ILE B CB  1 
ATOM   1905 C CG1 . ILE B 1 101 ? -1.33300  48.72900 -11.65200 1.000 30.58534 ? 100 ILE B CG1 1 
ATOM   1906 C CG2 . ILE B 1 101 ? -1.91800  46.73600 -13.08800 1.000 28.01257 ? 100 ILE B CG2 1 
ATOM   1907 C CD1 . ILE B 1 101 ? -2.83400  48.83300 -11.34700 1.000 27.95702 ? 100 ILE B CD1 1 
ATOM   1908 N N   . TRP B 1 102 ? 1.34200   45.89900 -14.49400 1.000 26.14682 ? 101 TRP B N   1 
ATOM   1909 C CA  . TRP B 1 102 ? 1.72200   45.29000 -15.76500 1.000 26.85352 ? 101 TRP B CA  1 
ATOM   1910 C C   . TRP B 1 102 ? 0.69700   44.21200 -16.09300 1.000 29.50484 ? 101 TRP B C   1 
ATOM   1911 O O   . TRP B 1 102 ? 0.30800   43.44800 -15.21200 1.000 30.67857 ? 101 TRP B O   1 
ATOM   1912 C CB  . TRP B 1 102 ? 3.14200   44.67600 -15.66000 1.000 32.08683 ? 101 TRP B CB  1 
ATOM   1913 C CG  . TRP B 1 102 ? 4.23700   45.70100 -15.32900 1.000 32.20152 ? 101 TRP B CG  1 
ATOM   1914 C CD1 . TRP B 1 102 ? 4.14900   46.71100 -14.42900 1.000 30.28320 ? 101 TRP B CD1 1 
ATOM   1915 C CD2 . TRP B 1 102 ? 5.54900   45.81600 -15.93000 1.000 34.12192 ? 101 TRP B CD2 1 
ATOM   1916 N NE1 . TRP B 1 102 ? 5.30200   47.45300 -14.43000 1.000 37.83681 ? 101 TRP B NE1 1 
ATOM   1917 C CE2 . TRP B 1 102 ? 6.17400   46.93400 -15.34700 1.000 33.30177 ? 101 TRP B CE2 1 
ATOM   1918 C CE3 . TRP B 1 102 ? 6.24400   45.09100 -16.91000 1.000 32.59910 ? 101 TRP B CE3 1 
ATOM   1919 C CZ2 . TRP B 1 102 ? 7.47100   47.32900 -15.68000 1.000 32.45349 ? 101 TRP B CZ2 1 
ATOM   1920 C CZ3 . TRP B 1 102 ? 7.52400   45.51400 -17.27100 1.000 34.46632 ? 101 TRP B CZ3 1 
ATOM   1921 C CH2 . TRP B 1 102 ? 8.12600   46.61400 -16.64700 1.000 28.81922 ? 101 TRP B CH2 1 
ATOM   1922 N N   . VAL B 1 103 ? 0.24000   44.14400 -17.34600 1.000 28.68440 ? 102 VAL B N   1 
ATOM   1923 C CA  . VAL B 1 103 ? -0.81800  43.20200 -17.71100 1.000 23.28661 ? 102 VAL B CA  1 
ATOM   1924 C C   . VAL B 1 103 ? -0.50700  42.54000 -19.04700 1.000 25.29753 ? 102 VAL B C   1 
ATOM   1925 O O   . VAL B 1 103 ? -0.34500  43.22700 -20.06100 1.000 27.23726 ? 102 VAL B O   1 
ATOM   1926 C CB  . VAL B 1 103 ? -2.19600  43.87300 -17.77700 1.000 24.08395 ? 102 VAL B CB  1 
ATOM   1927 C CG1 . VAL B 1 103 ? -3.22200  42.87700 -18.33500 1.000 24.94704 ? 102 VAL B CG1 1 
ATOM   1928 C CG2 . VAL B 1 103 ? -2.60100  44.35900 -16.38400 1.000 24.58000 ? 102 VAL B CG2 1 
ATOM   1929 N N   . TYR B 1 104 ? -0.45900  41.20100 -19.05200 1.000 23.86981 ? 103 TYR B N   1 
ATOM   1930 C CA  . TYR B 1 104 ? -0.13600  40.39200 -20.22300 1.000 25.46332 ? 103 TYR B CA  1 
ATOM   1931 C C   . TYR B 1 104 ? -1.18000  39.30500 -20.37700 1.000 30.16823 ? 103 TYR B C   1 
ATOM   1932 O O   . TYR B 1 104 ? -1.43800  38.56600 -19.42300 1.000 29.77812 ? 103 TYR B O   1 
ATOM   1933 C CB  . TYR B 1 104 ? 1.22800   39.69800 -20.08600 1.000 29.28858 ? 103 TYR B CB  1 
ATOM   1934 C CG  . TYR B 1 104 ? 2.45000   40.54000 -20.40700 1.000 31.14643 ? 103 TYR B CG  1 
ATOM   1935 C CD1 . TYR B 1 104 ? 2.33600   41.89800 -20.56600 1.000 26.39494 ? 103 TYR B CD1 1 
ATOM   1936 C CD2 . TYR B 1 104 ? 3.72000   39.96900 -20.50300 1.000 27.93547 ? 103 TYR B CD2 1 
ATOM   1937 C CE1 . TYR B 1 104 ? 3.41100   42.67100 -20.82700 1.000 28.50412 ? 103 TYR B CE1 1 
ATOM   1938 C CE2 . TYR B 1 104 ? 4.81900   40.74800 -20.77500 1.000 34.81568 ? 103 TYR B CE2 1 
ATOM   1939 C CZ  . TYR B 1 104 ? 4.64300   42.12000 -20.92500 1.000 29.62217 ? 103 TYR B CZ  1 
ATOM   1940 O OH  . TYR B 1 104 ? 5.68900   42.95500 -21.20800 1.000 33.27034 ? 103 TYR B OH  1 
ATOM   1941 N N   . PHE B 1 105 ? -1.73600  39.17500 -21.57700 1.000 26.56216 ? 104 PHE B N   1 
ATOM   1942 C CA  . PHE B 1 105 ? -2.65200  38.09400 -21.92000 1.000 20.89952 ? 104 PHE B CA  1 
ATOM   1943 C C   . PHE B 1 105 ? -1.97300  37.13300 -22.89300 1.000 26.53405 ? 104 PHE B C   1 
ATOM   1944 O O   . PHE B 1 105 ? -1.53500  37.54700 -23.97700 1.000 24.03239 ? 104 PHE B O   1 
ATOM   1945 C CB  . PHE B 1 105 ? -3.90900  38.65800 -22.56200 1.000 19.43595 ? 104 PHE B CB  1 
ATOM   1946 C CG  . PHE B 1 105 ? -4.73100  39.46500 -21.63200 1.000 25.52415 ? 104 PHE B CG  1 
ATOM   1947 C CD1 . PHE B 1 105 ? -4.52800  39.37600 -20.26400 1.000 25.33896 ? 104 PHE B CD1 1 
ATOM   1948 C CD2 . PHE B 1 105 ? -5.70500  40.32900 -22.11600 1.000 28.38894 ? 104 PHE B CD2 1 
ATOM   1949 C CE1 . PHE B 1 105 ? -5.28300  40.11600 -19.40300 1.000 22.17442 ? 104 PHE B CE1 1 
ATOM   1950 C CE2 . PHE B 1 105 ? -6.47900  41.08600 -21.25500 1.000 21.65824 ? 104 PHE B CE2 1 
ATOM   1951 C CZ  . PHE B 1 105 ? -6.26900  40.97600 -19.90200 1.000 22.94094 ? 104 PHE B CZ  1 
ATOM   1952 N N   . GLY B 1 106 ? -1.93500  35.85300 -22.53400 1.000 29.09225 ? 105 GLY B N   1 
ATOM   1953 C CA  . GLY B 1 106 ? -1.51700  34.79600 -23.45500 1.000 32.14362 ? 105 GLY B CA  1 
ATOM   1954 C C   . GLY B 1 106 ? -2.67700  33.85500 -23.76800 1.000 25.29585 ? 105 GLY B C   1 
ATOM   1955 O O   . GLY B 1 106 ? -3.50100  33.57300 -22.90000 1.000 30.08067 ? 105 GLY B O   1 
ATOM   1956 N N   . GLU B 1 107 ? -2.73700  33.39400 -25.01000 1.000 29.60378 ? 106 GLU B N   1 
ATOM   1957 C CA  . GLU B 1 107 ? -3.90600  32.65400 -25.47900 1.000 30.90777 ? 106 GLU B CA  1 
ATOM   1958 C C   . GLU B 1 107 ? -3.52200  31.27100 -25.98600 1.000 32.50471 ? 106 GLU B C   1 
ATOM   1959 O O   . GLU B 1 107 ? -2.47700  31.09100 -26.63400 1.000 33.76630 ? 106 GLU B O   1 
ATOM   1960 C CB  . GLU B 1 107 ? -4.63900  33.40500 -26.59100 1.000 30.07671 ? 106 GLU B CB  1 
ATOM   1961 C CG  . GLU B 1 107 ? -4.89500  34.87100 -26.29900 1.000 30.94964 ? 106 GLU B CG  1 
ATOM   1962 C CD  . GLU B 1 107 ? -5.19300  35.63600 -27.56900 1.000 32.14107 ? 106 GLU B CD  1 
ATOM   1963 O OE1 . GLU B 1 107 ? -4.22000  35.94900 -28.30800 1.000 42.25610 ? 106 GLU B OE1 1 
ATOM   1964 O OE2 . GLU B 1 107 ? -6.38700  35.91700 -27.83600 1.000 28.29596 ? 106 GLU B OE2 1 
ATOM   1965 N N   . MET B 1 108 ? -4.39000  30.30400 -25.70500 1.000 33.55308 ? 107 MET B N   1 
ATOM   1966 C CA  . MET B 1 108 ? -4.22500  28.93300 -26.15700 1.000 31.70481 ? 107 MET B CA  1 
ATOM   1967 C C   . MET B 1 108 ? -5.50600  28.40000 -26.80200 1.000 28.85345 ? 107 MET B C   1 
ATOM   1968 O O   . MET B 1 108 ? -6.58300  28.93900 -26.57600 1.000 39.16265 ? 107 MET B O   1 
ATOM   1969 C CB  . MET B 1 108 ? -3.86600  27.99000 -25.00100 1.000 25.43235 ? 107 MET B CB  1 
ATOM   1970 C CG  . MET B 1 108 ? -2.53100  28.29300 -24.36900 1.000 23.85238 ? 107 MET B CG  1 
ATOM   1971 S SD  . MET B 1 108 ? -2.63700  28.34100 -22.58000 1.000 29.19409 ? 107 MET B SD  1 
ATOM   1972 C CE  . MET B 1 108 ? -3.82700  29.69000 -22.40600 1.000 31.04120 ? 107 MET B CE  1 
ATOM   1973 N N   . PRO B 1 109 ? -5.39400  27.33000 -27.58400 1.000 31.59729 ? 108 PRO B N   1 
ATOM   1974 C CA  . PRO B 1 109 ? -6.62100  26.59100 -27.94900 1.000 26.62485 ? 108 PRO B CA  1 
ATOM   1975 C C   . PRO B 1 109 ? -7.22900  25.95700 -26.71200 1.000 26.44977 ? 108 PRO B C   1 
ATOM   1976 O O   . PRO B 1 109 ? -6.54000  25.41300 -25.85300 1.000 26.57103 ? 108 PRO B O   1 
ATOM   1977 C CB  . PRO B 1 109 ? -6.12500  25.52800 -28.93200 1.000 25.58919 ? 108 PRO B CB  1 
ATOM   1978 C CG  . PRO B 1 109 ? -4.82000  26.00800 -29.41700 1.000 32.98623 ? 108 PRO B CG  1 
ATOM   1979 C CD  . PRO B 1 109 ? -4.20900  26.80900 -28.27900 1.000 30.96790 ? 108 PRO B CD  1 
ATOM   1980 N N   . ALA B 1 110 ? -8.54300  26.10700 -26.58600 1.000 35.31546 ? 109 ALA B N   1 
ATOM   1981 C CA  . ALA B 1 110 ? -9.25700  25.52800 -25.44500 1.000 36.34455 ? 109 ALA B CA  1 
ATOM   1982 C C   . ALA B 1 110 ? -9.08200  24.02200 -25.41500 1.000 31.92483 ? 109 ALA B C   1 
ATOM   1983 O O   . ALA B 1 110 ? -9.08300  23.42100 -24.33500 1.000 30.95896 ? 109 ALA B O   1 
ATOM   1984 C CB  . ALA B 1 110 ? -10.73500 25.89100 -25.42600 1.000 33.25626 ? 109 ALA B CB  1 
ATOM   1985 N N   . GLN B 1 111 ? -8.91800  23.39900 -26.58800 1.000 28.33030 ? 110 GLN B N   1 
ATOM   1986 C CA  . GLN B 1 111 ? -8.72000  21.95500 -26.68500 1.000 26.96205 ? 110 GLN B CA  1 
ATOM   1987 C C   . GLN B 1 111 ? -7.49200  21.48800 -25.91800 1.000 25.49834 ? 110 GLN B C   1 
ATOM   1988 O O   . GLN B 1 111 ? -7.33100  20.27800 -25.72700 1.000 26.70854 ? 110 GLN B O   1 
ATOM   1989 C CB  . GLN B 1 111 ? -8.52700  21.52300 -28.14600 1.000 34.29209 ? 110 GLN B CB  1 
ATOM   1990 C CG  . GLN B 1 111 ? -9.06200  22.48600 -29.22100 1.000 32.12187 ? 110 GLN B CG  1 
ATOM   1991 C CD  . GLN B 1 111 ? -8.98000  21.85200 -30.60200 1.000 45.68849 ? 110 GLN B CD  1 
ATOM   1992 O OE1 . GLN B 1 111 ? -9.66200  20.85500 -30.86800 1.000 39.55007 ? 110 GLN B OE1 1 
ATOM   1993 N NE2 . GLN B 1 111 ? -8.12000  22.40100 -31.47800 1.000 43.28250 ? 110 GLN B NE2 1 
ATOM   1994 N N   . GLN B 1 112 ? -6.63200  22.41400 -25.46300 1.000 23.84147 ? 111 GLN B N   1 
ATOM   1995 C CA  . GLN B 1 112 ? -5.50800  22.12300 -24.57000 1.000 28.37377 ? 111 GLN B CA  1 
ATOM   1996 C C   . GLN B 1 112 ? -5.64900  22.87900 -23.25400 1.000 31.11474 ? 111 GLN B C   1 
ATOM   1997 O O   . GLN B 1 112 ? -4.64800  23.18100 -22.58200 1.000 28.60605 ? 111 GLN B O   1 
ATOM   1998 C CB  . GLN B 1 112 ? -4.15000  22.43800 -25.20400 1.000 18.42498 ? 111 GLN B CB  1 
ATOM   1999 C CG  . GLN B 1 112 ? -4.00900  23.78400 -25.77900 1.000 18.93048 ? 111 GLN B CG  1 
ATOM   2000 C CD  . GLN B 1 112 ? -3.27700  23.73900 -27.10300 1.000 32.85917 ? 111 GLN B CD  1 
ATOM   2001 O OE1 . GLN B 1 112 ? -3.83900  23.31500 -28.13800 1.000 32.43477 ? 111 GLN B OE1 1 
ATOM   2002 N NE2 . GLN B 1 112 ? -2.00100  24.14100 -27.08500 1.000 31.63980 ? 111 GLN B NE2 1 
ATOM   2003 N N   . MET B 1 113 ? -6.88400  23.15400 -22.85300 1.000 25.13703 ? 112 MET B N   1 
ATOM   2004 C CA  . MET B 1 113 ? -7.16100  23.94400 -21.66100 1.000 31.77971 ? 112 MET B CA  1 
ATOM   2005 C C   . MET B 1 113 ? -8.19200  23.16700 -20.86900 1.000 33.57319 ? 112 MET B C   1 
ATOM   2006 O O   . MET B 1 113 ? -9.29000  22.87800 -21.35900 1.000 30.55682 ? 112 MET B O   1 
ATOM   2007 C CB  . MET B 1 113 ? -7.68400  25.38400 -21.95900 1.000 26.80364 ? 112 MET B CB  1 
ATOM   2008 C CG  . MET B 1 113 ? -6.95800  26.21300 -23.00900 1.000 28.66982 ? 112 MET B CG  1 
ATOM   2009 S SD  . MET B 1 113 ? -7.26400  28.03900 -23.06900 1.000 27.37527 ? 112 MET B SD  1 
ATOM   2010 C CE  . MET B 1 113 ? -7.53200  28.53900 -21.36600 1.000 23.74841 ? 112 MET B CE  1 
ATOM   2011 N N   . VAL B 1 114 ? -7.84300  22.86300 -19.63500 1.000 37.42366 ? 113 VAL B N   1 
ATOM   2012 C CA  . VAL B 1 114 ? -8.69000  22.10000 -18.75200 1.000 30.07901 ? 113 VAL B CA  1 
ATOM   2013 C C   . VAL B 1 114 ? -8.99900  22.98800 -17.57500 1.000 31.13041 ? 113 VAL B C   1 
ATOM   2014 O O   . VAL B 1 114 ? -8.07900  23.49300 -16.91800 1.000 33.97124 ? 113 VAL B O   1 
ATOM   2015 C CB  . VAL B 1 114 ? -7.98100  20.82000 -18.30700 1.000 26.00623 ? 113 VAL B CB  1 
ATOM   2016 C CG1 . VAL B 1 114 ? -8.70100  20.21500 -17.12400 1.000 34.11944 ? 113 VAL B CG1 1 
ATOM   2017 C CG2 . VAL B 1 114 ? -7.87500  19.89100 -19.46500 1.000 26.11040 ? 113 VAL B CG2 1 
ATOM   2018 N N   . ASN B 1 115 ? -10.26500 23.06200 -17.23000 1.000 28.95946 ? 114 ASN B N   1 
ATOM   2019 C CA  . ASN B 1 115 ? -10.69500 23.76600 -16.04700 1.000 30.78295 ? 114 ASN B CA  1 
ATOM   2020 C C   . ASN B 1 115 ? -11.54500 22.81200 -15.26300 1.000 30.25451 ? 114 ASN B C   1 
ATOM   2021 O O   . ASN B 1 115 ? -12.36700 22.10800 -15.84900 1.000 29.69430 ? 114 ASN B O   1 
ATOM   2022 C CB  . ASN B 1 115 ? -11.57100 24.95700 -16.39600 1.000 31.36850 ? 114 ASN B CB  1 
ATOM   2023 C CG  . ASN B 1 115 ? -10.80700 26.17300 -16.54900 1.000 34.20503 ? 114 ASN B CG  1 
ATOM   2024 O OD1 . ASN B 1 115 ? -9.60400  26.12400 -16.78500 1.000 35.00536 ? 114 ASN B OD1 1 
ATOM   2025 N ND2 . ASN B 1 115 ? -11.47300 27.30900 -16.40700 1.000 41.77300 ? 114 ASN B ND2 1 
ATOM   2026 N N   . TYR B 1 116 ? -11.37500 22.82000 -13.94900 1.000 26.00693 ? 115 TYR B N   1 
ATOM   2027 C CA  . TYR B 1 116 ? -12.13200 21.91800 -13.11100 1.000 33.53700 ? 115 TYR B CA  1 
ATOM   2028 C C   . TYR B 1 116 ? -12.06300 20.48800 -13.65000 1.000 31.59646 ? 115 TYR B C   1 
ATOM   2029 O O   . TYR B 1 116 ? -13.05100 19.76200 -13.63200 1.000 36.91481 ? 115 TYR B O   1 
ATOM   2030 C CB  . TYR B 1 116 ? -13.58400 22.38200 -13.02500 1.000 35.46316 ? 115 TYR B CB  1 
ATOM   2031 C CG  . TYR B 1 116 ? -13.84300 23.66600 -12.26100 1.000 35.60099 ? 115 TYR B CG  1 
ATOM   2032 C CD1 . TYR B 1 116 ? -13.77600 23.70300 -10.87400 1.000 38.06403 ? 115 TYR B CD1 1 
ATOM   2033 C CD2 . TYR B 1 116 ? -14.19200 24.83900 -12.92900 1.000 34.87207 ? 115 TYR B CD2 1 
ATOM   2034 C CE1 . TYR B 1 116 ? -14.05900 24.87600 -10.16700 1.000 38.61414 ? 115 TYR B CE1 1 
ATOM   2035 C CE2 . TYR B 1 116 ? -14.46500 26.01700 -12.23200 1.000 34.63615 ? 115 TYR B CE2 1 
ATOM   2036 C CZ  . TYR B 1 116 ? -14.40400 26.02000 -10.85200 1.000 35.01762 ? 115 TYR B CZ  1 
ATOM   2037 O OH  . TYR B 1 116 ? -14.67800 27.16300 -10.16400 1.000 33.99001 ? 115 TYR B OH  1 
ATOM   2038 N N   . GLY B 1 117 ? -10.93600 20.10000 -14.23700 1.000 28.03749 ? 116 GLY B N   1 
ATOM   2039 C CA  . GLY B 1 117 ? -10.85100 18.76600 -14.76300 1.000 25.89127 ? 116 GLY B CA  1 
ATOM   2040 C C   . GLY B 1 117 ? -11.57400 18.53200 -16.06400 1.000 33.42422 ? 116 GLY B C   1 
ATOM   2041 O O   . GLY B 1 117 ? -11.84000 17.36900 -16.40200 1.000 32.62365 ? 116 GLY B O   1 
ATOM   2042 N N   . ARG B 1 118 ? -12.00300 19.58700 -16.75900 1.000 31.66396 ? 117 ARG B N   1 
ATOM   2043 C CA  . ARG B 1 118 ? -12.67600 19.40800 -18.04000 1.000 37.63423 ? 117 ARG B CA  1 
ATOM   2044 C C   . ARG B 1 118 ? -12.08500 20.29900 -19.11500 1.000 33.15735 ? 117 ARG B C   1 
ATOM   2045 O O   . ARG B 1 118 ? -11.73700 21.45700 -18.85700 1.000 39.70938 ? 117 ARG B O   1 
ATOM   2046 C CB  . ARG B 1 118 ? -14.18200 19.64600 -17.92700 1.000 33.12617 ? 117 ARG B CB  1 
ATOM   2047 C CG  . ARG B 1 118 ? -14.82000 18.43300 -17.31000 1.000 44.05466 ? 117 ARG B CG  1 
ATOM   2048 C CD  . ARG B 1 118 ? -15.30000 17.46300 -18.39500 1.000 55.59180 ? 117 ARG B CD  1 
ATOM   2049 N NE  . ARG B 1 118 ? -16.32800 16.52500 -17.94700 1.000 66.02405 ? 117 ARG B NE  1 
ATOM   2050 C CZ  . ARG B 1 118 ? -17.31300 16.02700 -18.68600 1.000 65.13177 ? 117 ARG B CZ  1 
ATOM   2051 N NH1 . ARG B 1 118 ? -17.48600 16.38400 -19.94400 1.000 62.32370 ? 117 ARG B NH1 1 
ATOM   2052 N NH2 . ARG B 1 118 ? -18.11300 15.09900 -18.16800 1.000 65.55554 ? 117 ARG B NH2 1 
ATOM   2053 N N   . PHE B 1 119 ? -12.02300 19.75900 -20.33100 1.000 27.84901 ? 118 PHE B N   1 
ATOM   2054 C CA  . PHE B 1 119 ? -11.58400 20.53500 -21.48300 1.000 30.42366 ? 118 PHE B CA  1 
ATOM   2055 C C   . PHE B 1 119 ? -12.55200 21.67300 -21.73600 1.000 33.78546 ? 118 PHE B C   1 
ATOM   2056 O O   . PHE B 1 119 ? -13.76900 21.47300 -21.75400 1.000 35.84900 ? 118 PHE B O   1 
ATOM   2057 C CB  . PHE B 1 119 ? -11.48300 19.65300 -22.71500 1.000 20.52492 ? 118 PHE B CB  1 
ATOM   2058 C CG  . PHE B 1 119 ? -10.24600 18.81300 -22.72500 1.000 24.59465 ? 118 PHE B CG  1 
ATOM   2059 C CD1 . PHE B 1 119 ? -9.02700  19.35700 -23.10900 1.000 23.17651 ? 118 PHE B CD1 1 
ATOM   2060 C CD2 . PHE B 1 119 ? -10.27800 17.49100 -22.28600 1.000 25.07293 ? 118 PHE B CD2 1 
ATOM   2061 C CE1 . PHE B 1 119 ? -7.86900  18.59200 -23.09000 1.000 22.09642 ? 118 PHE B CE1 1 
ATOM   2062 C CE2 . PHE B 1 119 ? -9.11100  16.71900 -22.25600 1.000 24.99633 ? 118 PHE B CE2 1 
ATOM   2063 C CZ  . PHE B 1 119 ? -7.90800  17.28000 -22.65900 1.000 23.70054 ? 118 PHE B CZ  1 
ATOM   2064 N N   . LEU B 1 120 ? -12.01300 22.87800 -21.89000 1.000 31.26511 ? 119 LEU B N   1 
ATOM   2065 C CA  . LEU B 1 120 ? -12.86200 24.02700 -22.11500 1.000 38.22593 ? 119 LEU B CA  1 
ATOM   2066 C C   . LEU B 1 120 ? -13.50600 23.91300 -23.50000 1.000 36.09309 ? 119 LEU B C   1 
ATOM   2067 O O   . LEU B 1 120 ? -12.92300 23.30900 -24.40800 1.000 30.04684 ? 119 LEU B O   1 
ATOM   2068 C CB  . LEU B 1 120 ? -12.02500 25.29800 -21.97500 1.000 33.29120 ? 119 LEU B CB  1 
ATOM   2069 C CG  . LEU B 1 120 ? -12.04500 26.05000 -20.64600 1.000 34.77844 ? 119 LEU B CG  1 
ATOM   2070 C CD1 . LEU B 1 120 ? -10.75700 26.86100 -20.48000 1.000 28.85412 ? 119 LEU B CD1 1 
ATOM   2071 C CD2 . LEU B 1 120 ? -13.25100 26.97200 -20.55800 1.000 37.35307 ? 119 LEU B CD2 1 
ATOM   2072 N N   . PRO B 1 121 ? -14.72000 24.54500 -23.69600 1.000 40.79764 ? 120 PRO B N   1 
ATOM   2073 C CA  . PRO B 1 121 ? -15.33800 24.61300 -25.02400 1.000 42.25486 ? 120 PRO B CA  1 
ATOM   2074 C C   . PRO B 1 121 ? -14.77100 25.83500 -25.66200 1.000 50.64254 ? 120 PRO B C   1 
ATOM   2075 O O   . PRO B 1 121 ? -13.87900 26.47400 -25.08900 1.000 51.35384 ? 120 PRO B O   1 
ATOM   2076 C CB  . PRO B 1 121 ? -16.81500 24.87400 -24.74400 1.000 42.14568 ? 120 PRO B CB  1 
ATOM   2077 C CG  . PRO B 1 121 ? -16.77600 25.64800 -23.47500 1.000 41.61077 ? 120 PRO B CG  1 
ATOM   2078 C CD  . PRO B 1 121 ? -15.46100 25.40700 -22.76200 1.000 38.98804 ? 120 PRO B CD  1 
ATOM   2079 N N   . GLN B 1 122 ? -15.29900 26.28900 -26.76900 1.000 55.26085 ? 121 GLN B N   1 
ATOM   2080 C CA  . GLN B 1 122 ? -14.71100 27.57500 -27.07900 1.000 53.09766 ? 121 GLN B CA  1 
ATOM   2081 C C   . GLN B 1 122 ? -15.82900 28.62600 -27.07000 1.000 60.26007 ? 121 GLN B C   1 
ATOM   2082 O O   . GLN B 1 122 ? -17.02100 28.27200 -26.99700 1.000 68.65120 ? 121 GLN B O   1 
ATOM   2083 C CB  . GLN B 1 122 ? -13.83800 27.52900 -28.37900 1.000 56.65896 ? 121 GLN B CB  1 
ATOM   2084 C CG  . GLN B 1 122 ? -12.56800 27.15600 -27.71300 1.000 63.45017 ? 121 GLN B CG  1 
ATOM   2085 C CD  . GLN B 1 122 ? -11.15000 26.96600 -28.32800 1.000 63.23264 ? 121 GLN B CD  1 
ATOM   2086 O OE1 . GLN B 1 122 ? -10.68600 27.80600 -29.13000 1.000 56.79770 ? 121 GLN B OE1 1 
ATOM   2087 N NE2 . GLN B 1 122 ? -10.68700 25.79700 -28.28600 1.000 60.26278 ? 121 GLN B NE2 1 
ATOM   2088 N N   . PRO B 1 123 ? -15.51400 29.95000 -27.02600 1.000 65.30451 ? 122 PRO B N   1 
ATOM   2089 C CA  . PRO B 1 123 ? -16.60000 30.91300 -26.73200 1.000 62.94739 ? 122 PRO B CA  1 
ATOM   2090 C C   . PRO B 1 123 ? -17.81100 30.74500 -27.65400 1.000 73.29768 ? 122 PRO B C   1 
ATOM   2091 O O   . PRO B 1 123 ? -18.88800 31.23200 -27.29300 1.000 76.48843 ? 122 PRO B O   1 
ATOM   2092 C CB  . PRO B 1 123 ? -15.93800 32.29700 -26.84500 1.000 55.50715 ? 122 PRO B CB  1 
ATOM   2093 C CG  . PRO B 1 123 ? -14.47300 32.06000 -26.65800 1.000 53.24355 ? 122 PRO B CG  1 
ATOM   2094 C CD  . PRO B 1 123 ? -14.18500 30.60100 -27.07500 1.000 54.84183 ? 122 PRO B CD  1 
ATOM   2095 N N   . GLY B 1 124 ? -17.68000 29.94400 -28.74400 1.000 68.41768 ? 123 GLY B N   1 
ATOM   2096 C CA  . GLY B 1 124 ? -18.78300 29.39300 -29.55900 1.000 64.45529 ? 123 GLY B CA  1 
ATOM   2097 C C   . GLY B 1 124 ? -19.65300 28.44100 -28.73700 1.000 73.91852 ? 123 GLY B C   1 
ATOM   2098 O O   . GLY B 1 124 ? -20.61600 27.84300 -29.24100 1.000 69.41626 ? 123 GLY B O   1 
ATOM   2099 N N   . HIS B 1 125 ? -19.27900 28.27900 -27.47200 1.000 69.03948 ? 124 HIS B N   1 
ATOM   2100 C CA  . HIS B 1 125 ? -20.04000 27.59800 -26.44700 1.000 59.80671 ? 124 HIS B CA  1 
ATOM   2101 C C   . HIS B 1 125 ? -19.73900 28.31300 -25.14000 1.000 57.97192 ? 124 HIS B C   1 
ATOM   2102 O O   . HIS B 1 125 ? -19.13900 29.39100 -25.14200 1.000 59.22405 ? 124 HIS B O   1 
ATOM   2103 C CB  . HIS B 1 125 ? -19.67700 26.10800 -26.38600 1.000 65.42144 ? 124 HIS B CB  1 
ATOM   2104 N N   . GLU B 1 126 ? -20.19200 27.70400 -24.04200 1.000 49.03600 ? 125 GLU B N   1 
ATOM   2105 C CA  . GLU B 1 126 ? -19.88700 27.95500 -22.63400 1.000 53.36236 ? 125 GLU B CA  1 
ATOM   2106 C C   . GLU B 1 126 ? -21.21300 28.10400 -21.90700 1.000 52.34456 ? 125 GLU B C   1 
ATOM   2107 O O   . GLU B 1 126 ? -21.28400 27.93300 -20.68900 1.000 53.89995 ? 125 GLU B O   1 
ATOM   2108 C CB  . GLU B 1 126 ? -18.97400 29.16400 -22.39900 1.000 50.77417 ? 125 GLU B CB  1 
ATOM   2109 C CG  . GLU B 1 126 ? -19.68600 30.48500 -22.23100 1.000 59.52816 ? 125 GLU B CG  1 
ATOM   2110 C CD  . GLU B 1 126 ? -18.89700 31.65100 -22.82900 1.000 56.24289 ? 125 GLU B CD  1 
ATOM   2111 O OE1 . GLU B 1 126 ? -17.70500 31.44800 -23.17500 1.000 52.76352 ? 125 GLU B OE1 1 
ATOM   2112 O OE2 . GLU B 1 126 ? -19.48200 32.76100 -22.96400 1.000 44.10638 ? 125 GLU B OE2 1 
ATOM   2113 N N   . GLY B 1 127 ? -22.27400 28.40500 -22.64400 1.000 56.98223 ? 126 GLY B N   1 
ATOM   2114 C CA  . GLY B 1 127 ? -23.60000 28.26400 -22.07800 1.000 54.16425 ? 126 GLY B CA  1 
ATOM   2115 C C   . GLY B 1 127 ? -23.99000 26.80400 -22.19300 1.000 54.22053 ? 126 GLY B C   1 
ATOM   2116 O O   . GLY B 1 127 ? -24.22400 26.11700 -21.18700 1.000 48.27744 ? 126 GLY B O   1 
ATOM   2117 N N   . GLU B 1 128 ? -24.02200 26.32400 -23.44300 1.000 49.83331 ? 127 GLU B N   1 
ATOM   2118 C CA  . GLU B 1 128 ? -24.18800 24.89900 -23.70400 1.000 51.51184 ? 127 GLU B CA  1 
ATOM   2119 C C   . GLU B 1 128 ? -23.14500 24.07600 -22.95600 1.000 57.95872 ? 127 GLU B C   1 
ATOM   2120 O O   . GLU B 1 128 ? -23.46400 23.00300 -22.42700 1.000 51.19816 ? 127 GLU B O   1 
ATOM   2121 C CB  . GLU B 1 128 ? -24.17900 24.60700 -25.20700 1.000 54.78164 ? 127 GLU B CB  1 
ATOM   2122 C CG  . GLU B 1 128 ? -23.07800 25.22400 -26.03400 1.000 62.88470 ? 127 GLU B CG  1 
ATOM   2123 C CD  . GLU B 1 128 ? -22.96100 24.57400 -27.41400 1.000 70.65375 ? 127 GLU B CD  1 
ATOM   2124 O OE1 . GLU B 1 128 ? -22.64500 23.36500 -27.49700 1.000 71.20009 ? 127 GLU B OE1 1 
ATOM   2125 O OE2 . GLU B 1 128 ? -23.21400 25.27300 -28.42000 1.000 74.37909 ? 127 GLU B OE2 1 
ATOM   2126 N N   . TRP B 1 129 ? -21.88900 24.54600 -22.92700 1.000 55.82084 ? 128 TRP B N   1 
ATOM   2127 C CA  . TRP B 1 129 ? -20.82600 23.79000 -22.26800 1.000 47.08406 ? 128 TRP B CA  1 
ATOM   2128 C C   . TRP B 1 129 ? -21.23900 23.32400 -20.89000 1.000 50.21285 ? 128 TRP B C   1 
ATOM   2129 O O   . TRP B 1 129 ? -21.03200 22.16100 -20.52800 1.000 53.00235 ? 128 TRP B O   1 
ATOM   2130 C CB  . TRP B 1 129 ? -19.57600 24.63100 -22.10700 1.000 47.80176 ? 128 TRP B CB  1 
ATOM   2131 C CG  . TRP B 1 129 ? -18.43600 23.85800 -21.54000 1.000 42.08236 ? 128 TRP B CG  1 
ATOM   2132 C CD1 . TRP B 1 129 ? -17.81700 22.78000 -22.10500 1.000 39.01376 ? 128 TRP B CD1 1 
ATOM   2133 C CD2 . TRP B 1 129 ? -17.77000 24.09100 -20.29200 1.000 47.22777 ? 128 TRP B CD2 1 
ATOM   2134 N NE1 . TRP B 1 129 ? -16.80000 22.33700 -21.29600 1.000 39.59484 ? 128 TRP B NE1 1 
ATOM   2135 C CE2 . TRP B 1 129 ? -16.75300 23.12100 -20.17400 1.000 40.85736 ? 128 TRP B CE2 1 
ATOM   2136 C CE3 . TRP B 1 129 ? -17.92900 25.02800 -19.26400 1.000 46.70738 ? 128 TRP B CE3 1 
ATOM   2137 C CZ2 . TRP B 1 129 ? -15.90600 23.06200 -19.07800 1.000 36.32948 ? 128 TRP B CZ2 1 
ATOM   2138 C CZ3 . TRP B 1 129 ? -17.07400 24.96300 -18.17300 1.000 39.85868 ? 128 TRP B CZ3 1 
ATOM   2139 C CH2 . TRP B 1 129 ? -16.08100 23.99100 -18.09500 1.000 36.27619 ? 128 TRP B CH2 1 
ATOM   2140 N N   . PHE B 1 130 ? -21.81300 24.22700 -20.10600 1.000 45.10397 ? 129 PHE B N   1 
ATOM   2141 C CA  . PHE B 1 130 ? -22.17500 23.94000 -18.73300 1.000 52.24323 ? 129 PHE B CA  1 
ATOM   2142 C C   . PHE B 1 130 ? -23.17500 22.77700 -18.64100 1.000 55.68721 ? 129 PHE B C   1 
ATOM   2143 O O   . PHE B 1 130 ? -24.37900 22.96000 -18.47000 1.000 49.95288 ? 129 PHE B O   1 
ATOM   2144 C CB  . PHE B 1 130 ? -22.68400 25.22200 -18.07200 1.000 52.55642 ? 129 PHE B CB  1 
ATOM   2145 C CG  . PHE B 1 130 ? -22.49400 25.24000 -16.58900 1.000 50.17813 ? 129 PHE B CG  1 
ATOM   2146 C CD1 . PHE B 1 130 ? -21.31100 24.81300 -16.02300 1.000 47.12966 ? 129 PHE B CD1 1 
ATOM   2147 C CD2 . PHE B 1 130 ? -23.49300 25.71000 -15.75900 1.000 51.69007 ? 129 PHE B CD2 1 
ATOM   2148 C CE1 . PHE B 1 130 ? -21.13600 24.82400 -14.64400 1.000 45.84404 ? 129 PHE B CE1 1 
ATOM   2149 C CE2 . PHE B 1 130 ? -23.33600 25.70800 -14.38200 1.000 51.49737 ? 129 PHE B CE2 1 
ATOM   2150 C CZ  . PHE B 1 130 ? -22.14900 25.26800 -13.82600 1.000 49.51539 ? 129 PHE B CZ  1 
ATOM   2151 N N   . ASP B 1 131 ? -22.65700 21.56200 -18.81100 1.000 65.86011 ? 130 ASP B N   1 
ATOM   2152 C CA  . ASP B 1 131 ? -23.34400 20.27200 -18.71400 1.000 58.61931 ? 130 ASP B CA  1 
ATOM   2153 C C   . ASP B 1 131 ? -22.37200 19.42100 -17.90100 1.000 60.88554 ? 130 ASP B C   1 
ATOM   2154 O O   . ASP B 1 131 ? -22.44400 19.45900 -16.68600 1.000 62.60940 ? 130 ASP B O   1 
ATOM   2155 C CB  . ASP B 1 131 ? -23.64800 19.69000 -20.09000 1.000 41.02960 ? 130 ASP B CB  1 
ATOM   2156 C CG  . ASP B 1 131 ? -24.88300 20.27900 -20.69200 1.000 54.76462 ? 130 ASP B CG  1 
ATOM   2157 O OD1 . ASP B 1 131 ? -25.10800 21.46800 -20.48300 1.000 54.78227 ? 130 ASP B OD1 1 
ATOM   2158 O OD2 . ASP B 1 131 ? -25.66900 19.55500 -21.34100 1.000 60.01832 ? 130 ASP B OD2 1 
ATOM   2159 N N   . ASN B 1 132 ? -21.37100 18.79100 -18.52500 1.000 63.90406 ? 131 ASN B N   1 
ATOM   2160 C CA  . ASN B 1 132 ? -20.04600 18.51400 -17.91200 1.000 73.48745 ? 131 ASN B CA  1 
ATOM   2161 C C   . ASN B 1 132 ? -19.96100 17.12100 -17.25000 1.000 73.01204 ? 131 ASN B C   1 
ATOM   2162 O O   . ASN B 1 132 ? -20.46800 16.12500 -17.79100 1.000 71.80955 ? 131 ASN B O   1 
ATOM   2163 C CB  . ASN B 1 132 ? -19.65500 19.52100 -16.82000 1.000 63.61036 ? 131 ASN B CB  1 
ATOM   2164 C CG  . ASN B 1 132 ? -19.57200 20.97300 -17.29100 1.000 60.95174 ? 131 ASN B CG  1 
ATOM   2165 O OD1 . ASN B 1 132 ? -20.48900 21.46800 -17.84400 1.000 62.03630 ? 131 ASN B OD1 1 
ATOM   2166 N ND2 . ASN B 1 132 ? -18.40800 21.63400 -17.10200 1.000 57.15590 ? 131 ASN B ND2 1 
ATOM   2167 N N   . LEU B 1 133 ? -19.27300 17.01800 -16.10400 1.000 71.74294 ? 132 LEU B N   1 
ATOM   2168 C CA  . LEU B 1 133 ? -19.53900 15.92800 -15.17200 1.000 73.22847 ? 132 LEU B CA  1 
ATOM   2169 C C   . LEU B 1 133 ? -20.68600 16.26200 -14.21700 1.000 65.41140 ? 132 LEU B C   1 
ATOM   2170 O O   . LEU B 1 133 ? -20.77700 15.70100 -13.11500 1.000 56.75132 ? 132 LEU B O   1 
ATOM   2171 C CB  . LEU B 1 133 ? -18.26200 15.59700 -14.43600 1.000 59.83090 ? 132 LEU B CB  1 
ATOM   2172 C CG  . LEU B 1 133 ? -17.03700 15.16900 -15.36100 1.000 65.33859 ? 132 LEU B CG  1 
ATOM   2173 C CD1 . LEU B 1 133 ? -15.73200 16.04200 -15.21400 1.000 60.45541 ? 132 LEU B CD1 1 
ATOM   2174 C CD2 . LEU B 1 133 ? -16.69200 13.74400 -15.16400 1.000 57.98068 ? 132 LEU B CD2 1 
ATOM   2175 N N   . SER B 1 134 ? -21.61900 17.10000 -14.68800 1.000 61.38328 ? 133 SER B N   1 
ATOM   2176 C CA  . SER B 1 134 ? -22.65500 17.81300 -13.94300 1.000 62.35478 ? 133 SER B CA  1 
ATOM   2177 C C   . SER B 1 134 ? -23.25500 17.02800 -12.81800 1.000 59.68169 ? 133 SER B C   1 
ATOM   2178 O O   . SER B 1 134 ? -23.24300 15.79200 -12.83900 1.000 71.87954 ? 133 SER B O   1 
ATOM   2179 C CB  . SER B 1 134 ? -23.80700 18.20300 -14.85700 1.000 58.51201 ? 133 SER B CB  1 
ATOM   2180 O OG  . SER B 1 134 ? -23.81400 17.51800 -16.09900 1.000 52.18232 ? 133 SER B OG  1 
ATOM   2181 N N   . SER B 1 135 ? -23.88300 17.78300 -11.91600 1.000 59.39341 ? 134 SER B N   1 
ATOM   2182 C CA  . SER B 1 135 ? -24.37000 17.35700 -10.59900 1.000 63.77280 ? 134 SER B CA  1 
ATOM   2183 C C   . SER B 1 135 ? -23.26500 17.81700 -9.67000  1.000 54.07965 ? 134 SER B C   1 
ATOM   2184 O O   . SER B 1 135 ? -23.15100 19.01900 -9.38500  1.000 53.83915 ? 134 SER B O   1 
ATOM   2185 C CB  . SER B 1 135 ? -24.62400 15.82100 -10.40800 1.000 69.84315 ? 134 SER B CB  1 
ATOM   2186 O OG  . SER B 1 135 ? -24.70400 15.42200 -9.03200  1.000 80.59575 ? 134 SER B OG  1 
ATOM   2187 N N   . ASP B 1 136 ? -22.37500 16.87300 -9.32500  1.000 51.02226 ? 135 ASP B N   1 
ATOM   2188 C CA  . ASP B 1 136 ? -21.32700 17.11200 -8.31700  1.000 66.06918 ? 135 ASP B CA  1 
ATOM   2189 C C   . ASP B 1 136 ? -20.42900 18.28200 -8.67600  1.000 60.16976 ? 135 ASP B C   1 
ATOM   2190 O O   . ASP B 1 136 ? -19.92800 19.00600 -7.81200  1.000 57.35540 ? 135 ASP B O   1 
ATOM   2191 C CB  . ASP B 1 136 ? -20.45500 15.86600 -8.16600  1.000 72.74852 ? 135 ASP B CB  1 
ATOM   2192 C CG  . ASP B 1 136 ? -20.95200 14.90900 -7.09300  1.000 76.50800 ? 135 ASP B CG  1 
ATOM   2193 O OD1 . ASP B 1 136 ? -21.60200 15.37500 -6.14000  1.000 82.84345 ? 135 ASP B OD1 1 
ATOM   2194 O OD2 . ASP B 1 136 ? -20.75200 13.66900 -7.24200  1.000 66.32007 ? 135 ASP B OD2 1 
ATOM   2195 N N   . GLU B 1 137 ? -20.22400 18.44200 -9.96600  1.000 55.33488 ? 136 GLU B N   1 
ATOM   2196 C CA  . GLU B 1 137 ? -19.47100 19.28400 -10.89200 1.000 56.32615 ? 136 GLU B CA  1 
ATOM   2197 C C   . GLU B 1 137 ? -20.14300 20.60100 -11.24500 1.000 51.35165 ? 136 GLU B C   1 
ATOM   2198 O O   . GLU B 1 137 ? -19.58700 21.68200 -11.05700 1.000 50.97067 ? 136 GLU B O   1 
ATOM   2199 C CB  . GLU B 1 137 ? -19.24300 18.38900 -12.14100 1.000 57.85836 ? 136 GLU B CB  1 
ATOM   2200 C CG  . GLU B 1 137 ? -18.08600 17.53700 -11.82000 1.000 70.01857 ? 136 GLU B CG  1 
ATOM   2201 C CD  . GLU B 1 137 ? -16.79600 17.88700 -12.43700 1.000 70.70601 ? 136 GLU B CD  1 
ATOM   2202 O OE1 . GLU B 1 137 ? -16.05800 18.91300 -12.22200 1.000 68.73975 ? 136 GLU B OE1 1 
ATOM   2203 O OE2 . GLU B 1 137 ? -16.26800 16.75200 -12.74400 1.000 73.58691 ? 136 GLU B OE2 1 
ATOM   2204 N N   . ARG B 1 138 ? -21.35800 20.52000 -11.73900 1.000 50.76888 ? 137 ARG B N   1 
ATOM   2205 C CA  . ARG B 1 138 ? -22.15900 21.71400 -11.91400 1.000 54.35550 ? 137 ARG B CA  1 
ATOM   2206 C C   . ARG B 1 138 ? -22.27800 22.43100 -10.58200 1.000 53.08719 ? 137 ARG B C   1 
ATOM   2207 O O   . ARG B 1 138 ? -21.89400 23.59900 -10.44900 1.000 54.33524 ? 137 ARG B O   1 
ATOM   2208 C CB  . ARG B 1 138 ? -23.51100 21.29000 -12.45400 1.000 57.03764 ? 137 ARG B CB  1 
ATOM   2209 C CG  . ARG B 1 138 ? -24.25600 22.21900 -13.28000 1.000 57.39999 ? 137 ARG B CG  1 
ATOM   2210 C CD  . ARG B 1 138 ? -24.97900 21.28100 -14.23300 1.000 59.87938 ? 137 ARG B CD  1 
ATOM   2211 N NE  . ARG B 1 138 ? -26.29600 21.75800 -14.59000 1.000 63.76074 ? 137 ARG B NE  1 
ATOM   2212 C CZ  . ARG B 1 138 ? -26.53700 22.89400 -15.21300 1.000 62.17611 ? 137 ARG B CZ  1 
ATOM   2213 N NH1 . ARG B 1 138 ? -25.56400 23.67600 -15.62400 1.000 60.53711 ? 137 ARG B NH1 1 
ATOM   2214 N NH2 . ARG B 1 138 ? -27.78800 23.27300 -15.38900 1.000 63.55227 ? 137 ARG B NH2 1 
ATOM   2215 N N   . ALA B 1 139 ? -22.64100 21.67700 -9.54100  1.000 53.08718 ? 138 ALA B N   1 
ATOM   2216 C CA  . ALA B 1 139 ? -22.83700 22.25500 -8.21700  1.000 53.66447 ? 138 ALA B CA  1 
ATOM   2217 C C   . ALA B 1 139 ? -21.52700 22.64300 -7.54200  1.000 51.77916 ? 138 ALA B C   1 
ATOM   2218 O O   . ALA B 1 139 ? -21.53900 23.52000 -6.67700  1.000 50.35928 ? 138 ALA B O   1 
ATOM   2219 C CB  . ALA B 1 139 ? -23.63700 21.31700 -7.31600  1.000 46.23990 ? 138 ALA B CB  1 
ATOM   2220 N N   . PHE B 1 140 ? -20.41300 21.96700 -7.84200  1.000 49.43644 ? 139 PHE B N   1 
ATOM   2221 C CA  . PHE B 1 140 ? -19.13100 22.41400 -7.28300  1.000 50.72589 ? 139 PHE B CA  1 
ATOM   2222 C C   . PHE B 1 140 ? -18.72000 23.77200 -7.84200  1.000 51.23938 ? 139 PHE B C   1 
ATOM   2223 O O   . PHE B 1 140 ? -18.02100 24.53500 -7.17100  1.000 48.37055 ? 139 PHE B O   1 
ATOM   2224 C CB  . PHE B 1 140 ? -18.04600 21.36500 -7.53600  1.000 47.42409 ? 139 PHE B CB  1 
ATOM   2225 C CG  . PHE B 1 140 ? -16.63000 21.82800 -7.25200  1.000 43.99223 ? 139 PHE B CG  1 
ATOM   2226 C CD1 . PHE B 1 140 ? -16.16000 21.91000 -5.94700  1.000 47.96004 ? 139 PHE B CD1 1 
ATOM   2227 C CD2 . PHE B 1 140 ? -15.73500 22.06700 -8.28700  1.000 44.05823 ? 139 PHE B CD2 1 
ATOM   2228 C CE1 . PHE B 1 140 ? -14.84500 22.28500 -5.67500  1.000 48.11431 ? 139 PHE B CE1 1 
ATOM   2229 C CE2 . PHE B 1 140 ? -14.41700 22.43300 -8.01600  1.000 46.10615 ? 139 PHE B CE2 1 
ATOM   2230 C CZ  . PHE B 1 140 ? -13.97200 22.55000 -6.70700  1.000 44.15088 ? 139 PHE B CZ  1 
ATOM   2231 N N   . MET B 1 141 ? -19.05400 24.02900 -9.10400  1.000 52.09240 ? 140 MET B N   1 
ATOM   2232 C CA  . MET B 1 141 ? -18.84000 25.33000 -9.71800  1.000 42.88979 ? 140 MET B CA  1 
ATOM   2233 C C   . MET B 1 141 ? -19.79100 26.39200 -9.17200  1.000 48.14968 ? 140 MET B C   1 
ATOM   2234 O O   . MET B 1 141 ? -19.37700 27.53300 -8.95000  1.000 46.00075 ? 140 MET B O   1 
ATOM   2235 C CB  . MET B 1 141 ? -18.97900 25.18700 -11.22500 1.000 44.34312 ? 140 MET B CB  1 
ATOM   2236 C CG  . MET B 1 141 ? -17.96600 24.22700 -11.79600 1.000 41.01750 ? 140 MET B CG  1 
ATOM   2237 S SD  . MET B 1 141 ? -18.20100 24.02700 -13.55100 1.000 53.03251 ? 140 MET B SD  1 
ATOM   2238 C CE  . MET B 1 141 ? -16.88900 22.88300 -13.93700 1.000 48.48744 ? 140 MET B CE  1 
ATOM   2239 N N   . GLU B 1 142 ? -21.06600 26.04400 -8.95000  1.000 52.08184 ? 141 GLU B N   1 
ATOM   2240 C CA  . GLU B 1 142 ? -22.03200 27.05100 -8.49900  1.000 53.36886 ? 141 GLU B CA  1 
ATOM   2241 C C   . GLU B 1 142 ? -21.56900 27.76100 -7.23000  1.000 56.12842 ? 141 GLU B C   1 
ATOM   2242 O O   . GLU B 1 142 ? -21.83700 28.96200 -7.05700  1.000 52.87228 ? 141 GLU B O   1 
ATOM   2243 C CB  . GLU B 1 142 ? -23.38700 26.41700 -8.14700  1.000 48.99976 ? 141 GLU B CB  1 
ATOM   2244 C CG  . GLU B 1 142 ? -24.18000 25.59900 -9.15600  1.000 59.12408 ? 141 GLU B CG  1 
ATOM   2245 C CD  . GLU B 1 142 ? -24.39900 26.25200 -10.51200 1.000 67.14170 ? 141 GLU B CD  1 
ATOM   2246 O OE1 . GLU B 1 142 ? -24.34400 27.50200 -10.61200 1.000 60.18110 ? 141 GLU B OE1 1 
ATOM   2247 O OE2 . GLU B 1 142 ? -24.64100 25.49800 -11.47800 1.000 62.79735 ? 141 GLU B OE2 1 
ATOM   2248 N N   . THR B 1 143 ? -20.87400 27.03700 -6.33500  1.000 49.70459 ? 142 THR B N   1 
ATOM   2249 C CA  . THR B 1 143 ? -20.46500 27.62100 -5.06000  1.000 48.26681 ? 142 THR B CA  1 
ATOM   2250 C C   . THR B 1 143 ? -19.30000 28.58300 -5.21500  1.000 47.95738 ? 142 THR B C   1 
ATOM   2251 O O   . THR B 1 143 ? -19.26200 29.61900 -4.54600  1.000 47.95442 ? 142 THR B O   1 
ATOM   2252 C CB  . THR B 1 143 ? -20.06900 26.53700 -4.05600  1.000 50.89727 ? 142 THR B CB  1 
ATOM   2253 O OG1 . THR B 1 143 ? -18.67900 26.22900 -4.20100  1.000 49.43349 ? 142 THR B OG1 1 
ATOM   2254 C CG2 . THR B 1 143 ? -20.84200 25.27700 -4.29300  1.000 57.28039 ? 142 THR B CG2 1 
ATOM   2255 N N   . ASN B 1 144 ? -18.38000 28.30200 -6.13600  1.000 46.52874 ? 143 ASN B N   1 
ATOM   2256 C CA  . ASN B 1 144 ? -17.20800 29.14900 -6.26900  1.000 38.29061 ? 143 ASN B CA  1 
ATOM   2257 C C   . ASN B 1 144 ? -17.65500 30.38500 -7.03000  1.000 40.77189 ? 143 ASN B C   1 
ATOM   2258 O O   . ASN B 1 144 ? -17.08300 30.71400 -8.06900  1.000 42.14886 ? 143 ASN B O   1 
ATOM   2259 C CB  . ASN B 1 144 ? -16.05700 28.43100 -6.99900  1.000 37.88283 ? 143 ASN B CB  1 
ATOM   2260 C CG  . ASN B 1 144 ? -15.31600 27.40700 -6.11300  1.000 37.60514 ? 143 ASN B CG  1 
ATOM   2261 O OD1 . ASN B 1 144 ? -15.05600 27.64600 -4.93400  1.000 36.95835 ? 143 ASN B OD1 1 
ATOM   2262 N ND2 . ASN B 1 144 ? -14.99200 26.25300 -6.68900  1.000 41.30778 ? 143 ASN B ND2 1 
ATOM   2263 N N   . VAL B 1 145 ? -18.71600 31.04600 -6.56300  1.000 43.61353 ? 144 VAL B N   1 
ATOM   2264 C CA  . VAL B 1 145 ? -19.15700 32.28300 -7.19100  1.000 44.79553 ? 144 VAL B CA  1 
ATOM   2265 C C   . VAL B 1 145 ? -19.59800 33.27100 -6.11200  1.000 49.16197 ? 144 VAL B C   1 
ATOM   2266 O O   . VAL B 1 145 ? -20.50600 32.99100 -5.32300  1.000 44.23470 ? 144 VAL B O   1 
ATOM   2267 C CB  . VAL B 1 145 ? -20.29400 32.05300 -8.19100  1.000 51.17560 ? 144 VAL B CB  1 
ATOM   2268 C CG1 . VAL B 1 145 ? -21.14700 33.29200 -8.34200  1.000 50.86697 ? 144 VAL B CG1 1 
ATOM   2269 C CG2 . VAL B 1 145 ? -19.73200 31.62200 -9.51600  1.000 50.83098 ? 144 VAL B CG2 1 
ATOM   2270 N N   . ASP B 1 146 ? -18.93600 34.41900 -6.09800  1.000 49.51835 ? 145 ASP B N   1 
ATOM   2271 C CA  . ASP B 1 146 ? -19.41900 35.72400 -5.71400  1.000 52.49291 ? 145 ASP B CA  1 
ATOM   2272 C C   . ASP B 1 146 ? -20.83000 36.04800 -6.23900  1.000 64.60522 ? 145 ASP B C   1 
ATOM   2273 O O   . ASP B 1 146 ? -21.78500 35.25400 -6.09300  1.000 66.30839 ? 145 ASP B O   1 
ATOM   2274 C CB  . ASP B 1 146 ? -18.38200 36.71000 -6.25800  1.000 56.69818 ? 145 ASP B CB  1 
ATOM   2275 C CG  . ASP B 1 146 ? -18.89300 38.10100 -6.39900  1.000 62.50049 ? 145 ASP B CG  1 
ATOM   2276 O OD1 . ASP B 1 146 ? -18.79200 38.87600 -5.43300  1.000 69.17048 ? 145 ASP B OD1 1 
ATOM   2277 O OD2 . ASP B 1 146 ? -19.42500 38.40800 -7.49000  1.000 65.18687 ? 145 ASP B OD2 1 
ATOM   2278 N N   . PRO C 1 2   ? 10.08900  43.92600 -21.46800 1.000 41.84477 ? 1   PRO C N   1 
ATOM   2279 C CA  . PRO C 1 2   ? 9.92300   42.49700 -21.21100 1.000 34.46224 ? 1   PRO C CA  1 
ATOM   2280 C C   . PRO C 1 2   ? 9.63100   42.19200 -19.76800 1.000 29.04994 ? 1   PRO C C   1 
ATOM   2281 O O   . PRO C 1 2   ? 10.07800  42.96100 -18.91000 1.000 36.19389 ? 1   PRO C O   1 
ATOM   2282 C CB  . PRO C 1 2   ? 11.29000  41.93500 -21.58300 1.000 35.19224 ? 1   PRO C CB  1 
ATOM   2283 C CG  . PRO C 1 2   ? 12.22800  43.06300 -21.31400 1.000 32.33435 ? 1   PRO C CG  1 
ATOM   2284 C CD  . PRO C 1 2   ? 11.48200  44.25600 -21.81000 1.000 38.15323 ? 1   PRO C CD  1 
ATOM   2285 N N   . VAL C 1 3   ? 8.90600   41.10900 -19.49800 1.000 26.04446 ? 2   VAL C N   1 
ATOM   2286 C CA  . VAL C 1 3   ? 8.80900   40.55400 -18.14900 1.000 29.94251 ? 2   VAL C CA  1 
ATOM   2287 C C   . VAL C 1 3   ? 9.55900   39.21400 -18.13700 1.000 31.65706 ? 2   VAL C C   1 
ATOM   2288 O O   . VAL C 1 3   ? 9.20600   38.28400 -18.88100 1.000 25.56728 ? 2   VAL C O   1 
ATOM   2289 C CB  . VAL C 1 3   ? 7.35500   40.37800 -17.69800 1.000 30.25255 ? 2   VAL C CB  1 
ATOM   2290 C CG1 . VAL C 1 3   ? 7.30500   39.42600 -16.52000 1.000 28.49091 ? 2   VAL C CG1 1 
ATOM   2291 C CG2 . VAL C 1 3   ? 6.71600   41.73100 -17.35300 1.000 28.10081 ? 2   VAL C CG2 1 
ATOM   2292 N N   . TYR C 1 4   ? 10.56300  39.10400 -17.25900 1.000 24.54881 ? 3   TYR C N   1 
ATOM   2293 C CA  . TYR C 1 4   ? 11.41000  37.92100 -17.13300 1.000 29.26854 ? 3   TYR C CA  1 
ATOM   2294 C C   . TYR C 1 4   ? 11.07700  37.25500 -15.80500 1.000 29.27158 ? 3   TYR C C   1 
ATOM   2295 O O   . TYR C 1 4   ? 11.41000  37.77700 -14.73400 1.000 32.62515 ? 3   TYR C O   1 
ATOM   2296 C CB  . TYR C 1 4   ? 12.89900  38.28100 -17.23400 1.000 24.98099 ? 3   TYR C CB  1 
ATOM   2297 C CG  . TYR C 1 4   ? 13.37400  38.54100 -18.66900 1.000 31.45423 ? 3   TYR C CG  1 
ATOM   2298 C CD1 . TYR C 1 4   ? 13.59700  37.48700 -19.56300 1.000 22.30215 ? 3   TYR C CD1 1 
ATOM   2299 C CD2 . TYR C 1 4   ? 13.57500  39.84700 -19.13900 1.000 33.93409 ? 3   TYR C CD2 1 
ATOM   2300 C CE1 . TYR C 1 4   ? 14.00900  37.72200 -20.88100 1.000 23.32490 ? 3   TYR C CE1 1 
ATOM   2301 C CE2 . TYR C 1 4   ? 13.99500  40.08800 -20.46100 1.000 29.56180 ? 3   TYR C CE2 1 
ATOM   2302 C CZ  . TYR C 1 4   ? 14.21000  39.02600 -21.31800 1.000 29.77638 ? 3   TYR C CZ  1 
ATOM   2303 O OH  . TYR C 1 4   ? 14.63000  39.27000 -22.60700 1.000 34.10665 ? 3   TYR C OH  1 
ATOM   2304 N N   . MET C 1 5   ? 10.37100  36.13700 -15.87400 1.000 25.25632 ? 4   MET C N   1 
ATOM   2305 C CA  . MET C 1 5   ? 10.13000  35.31500 -14.70500 1.000 25.99284 ? 4   MET C CA  1 
ATOM   2306 C C   . MET C 1 5   ? 11.34200  34.41800 -14.47100 1.000 30.19566 ? 4   MET C C   1 
ATOM   2307 O O   . MET C 1 5   ? 11.68500  33.59400 -15.32500 1.000 27.44297 ? 4   MET C O   1 
ATOM   2308 C CB  . MET C 1 5   ? 8.87500   34.48900 -14.93400 1.000 26.07794 ? 4   MET C CB  1 
ATOM   2309 C CG  . MET C 1 5   ? 7.59100   35.26400 -14.75200 1.000 37.71005 ? 4   MET C CG  1 
ATOM   2310 S SD  . MET C 1 5   ? 7.75900   36.57300 -13.52700 1.000 42.49789 ? 4   MET C SD  1 
ATOM   2311 C CE  . MET C 1 5   ? 6.13700   36.55300 -12.86600 1.000 38.10041 ? 4   MET C CE  1 
ATOM   2312 N N   . VAL C 1 6   ? 11.97500  34.54000 -13.31000 1.000 28.67064 ? 5   VAL C N   1 
ATOM   2313 C CA  . VAL C 1 6   ? 13.18800  33.78400 -13.02000 1.000 30.91093 ? 5   VAL C CA  1 
ATOM   2314 C C   . VAL C 1 6   ? 12.89500  32.91300 -11.81400 1.000 31.06734 ? 5   VAL C C   1 
ATOM   2315 O O   . VAL C 1 6   ? 12.73700  33.41900 -10.70100 1.000 36.94627 ? 5   VAL C O   1 
ATOM   2316 C CB  . VAL C 1 6   ? 14.40000  34.70300 -12.76600 1.000 33.10902 ? 5   VAL C CB  1 
ATOM   2317 C CG1 . VAL C 1 6   ? 15.63500  33.86800 -12.40600 1.000 29.73550 ? 5   VAL C CG1 1 
ATOM   2318 C CG2 . VAL C 1 6   ? 14.67700  35.59400 -14.00500 1.000 22.30317 ? 5   VAL C CG2 1 
ATOM   2319 N N   . TYR C 1 7   ? 12.84300  31.60900 -12.02400 1.000 30.30100 ? 6   TYR C N   1 
ATOM   2320 C CA  . TYR C 1 7   ? 12.51600  30.65800 -10.97800 1.000 27.68505 ? 6   TYR C CA  1 
ATOM   2321 C C   . TYR C 1 7   ? 13.80800  30.02000 -10.47500 1.000 34.38079 ? 6   TYR C C   1 
ATOM   2322 O O   . TYR C 1 7   ? 14.60900  29.47000 -11.25700 1.000 30.45629 ? 6   TYR C O   1 
ATOM   2323 C CB  . TYR C 1 7   ? 11.53400  29.61000 -11.47200 1.000 26.63136 ? 6   TYR C CB  1 
ATOM   2324 C CG  . TYR C 1 7   ? 10.30100  30.22100 -12.07000 1.000 30.99933 ? 6   TYR C CG  1 
ATOM   2325 C CD1 . TYR C 1 7   ? 10.33000  30.74900 -13.36800 1.000 30.39510 ? 6   TYR C CD1 1 
ATOM   2326 C CD2 . TYR C 1 7   ? 9.09700   30.25300 -11.36000 1.000 23.68714 ? 6   TYR C CD2 1 
ATOM   2327 C CE1 . TYR C 1 7   ? 9.20100   31.29600 -13.93500 1.000 28.57646 ? 6   TYR C CE1 1 
ATOM   2328 C CE2 . TYR C 1 7   ? 7.97100   30.80500 -11.91100 1.000 23.21135 ? 6   TYR C CE2 1 
ATOM   2329 C CZ  . TYR C 1 7   ? 8.03000   31.32700 -13.19800 1.000 26.81064 ? 6   TYR C CZ  1 
ATOM   2330 O OH  . TYR C 1 7   ? 6.93500   31.89000 -13.77200 1.000 29.81782 ? 6   TYR C OH  1 
ATOM   2331 N N   . VAL C 1 8   ? 14.01000  30.14100 -9.16900  1.000 31.85899 ? 7   VAL C N   1 
ATOM   2332 C CA  . VAL C 1 8   ? 15.25700  29.79500 -8.52800  1.000 29.16416 ? 7   VAL C CA  1 
ATOM   2333 C C   . VAL C 1 8   ? 14.92900  29.27600 -7.14200  1.000 30.62680 ? 7   VAL C C   1 
ATOM   2334 O O   . VAL C 1 8   ? 13.89600  29.61400 -6.55600  1.000 29.26557 ? 7   VAL C O   1 
ATOM   2335 C CB  . VAL C 1 8   ? 16.20100  31.01900 -8.47100  1.000 30.19956 ? 7   VAL C CB  1 
ATOM   2336 C CG1 . VAL C 1 8   ? 16.91400  31.17700 -9.77300  1.000 29.81707 ? 7   VAL C CG1 1 
ATOM   2337 C CG2 . VAL C 1 8   ? 15.42500  32.28100 -8.15200  1.000 29.60982 ? 7   VAL C CG2 1 
ATOM   2338 N N   . SER C 1 9   ? 15.84400  28.48600 -6.59200  1.000 30.49414 ? 8   SER C N   1 
ATOM   2339 C CA  . SER C 1 9   ? 15.63800  28.00800 -5.24600  1.000 32.19910 ? 8   SER C CA  1 
ATOM   2340 C C   . SER C 1 9   ? 15.98000  29.10200 -4.24300  1.000 40.56123 ? 8   SER C C   1 
ATOM   2341 O O   . SER C 1 9   ? 16.87600  29.92700 -4.46300  1.000 34.63803 ? 8   SER C O   1 
ATOM   2342 C CB  . SER C 1 9   ? 16.44700  26.75200 -4.97700  1.000 32.11038 ? 8   SER C CB  1 
ATOM   2343 O OG  . SER C 1 9   ? 16.10700  25.73700 -5.89800  1.000 39.16135 ? 8   SER C OG  1 
ATOM   2344 N N   . GLN C 1 10  ? 15.25800  29.07100 -3.11900  1.000 39.18985 ? 9   GLN C N   1 
ATOM   2345 C CA  . GLN C 1 10  ? 15.31500  30.13000 -2.12500  1.000 39.29423 ? 9   GLN C CA  1 
ATOM   2346 C C   . GLN C 1 10  ? 16.72300  30.32400 -1.57600  1.000 48.89246 ? 9   GLN C C   1 
ATOM   2347 O O   . GLN C 1 10  ? 17.41400  29.36200 -1.20600  1.000 34.48796 ? 9   GLN C O   1 
ATOM   2348 C CB  . GLN C 1 10  ? 14.36700  29.82100 -0.97500  1.000 34.09109 ? 9   GLN C CB  1 
ATOM   2349 C CG  . GLN C 1 10  ? 14.25700  30.92800 0.06800   1.000 38.23315 ? 9   GLN C CG  1 
ATOM   2350 C CD  . GLN C 1 10  ? 13.02500  31.78800 -0.15800  1.000 50.56476 ? 9   GLN C CD  1 
ATOM   2351 O OE1 . GLN C 1 10  ? 13.10500  33.01900 -0.15900  1.000 50.10975 ? 9   GLN C OE1 1 
ATOM   2352 N NE2 . GLN C 1 10  ? 11.87500  31.13300 -0.40700  1.000 48.92609 ? 9   GLN C NE2 1 
ATOM   2353 N N   . ASP C 1 11  ? 17.11900  31.60200 -1.51400  1.000 49.94556 ? 10  ASP C N   1 
ATOM   2354 C CA  . ASP C 1 11  ? 18.37200  32.08500 -0.95500  1.000 46.92452 ? 10  ASP C CA  1 
ATOM   2355 C C   . ASP C 1 11  ? 19.59800  31.42700 -1.59400  1.000 51.14810 ? 10  ASP C C   1 
ATOM   2356 O O   . ASP C 1 11  ? 20.68700  31.44800 -1.01100  1.000 53.95923 ? 10  ASP C O   1 
ATOM   2357 C CB  . ASP C 1 11  ? 18.37300  31.94300 0.57300   1.000 48.20055 ? 10  ASP C CB  1 
ATOM   2358 C CG  . ASP C 1 11  ? 17.45500  32.97500 1.25100   1.000 52.24247 ? 10  ASP C CG  1 
ATOM   2359 O OD1 . ASP C 1 11  ? 16.78100  33.74300 0.50500   1.000 48.99057 ? 10  ASP C OD1 1 
ATOM   2360 O OD2 . ASP C 1 11  ? 17.43400  33.04200 2.51200   1.000 38.81771 ? 10  ASP C OD2 1 
ATOM   2361 N N   . ARG C 1 12  ? 19.45600  30.90900 -2.82200  1.000 42.17612 ? 11  ARG C N   1 
ATOM   2362 C CA  . ARG C 1 12  ? 20.60900  30.46600 -3.58400  1.000 32.83173 ? 11  ARG C CA  1 
ATOM   2363 C C   . ARG C 1 12  ? 21.36700  31.64500 -4.16000  1.000 39.18333 ? 11  ARG C C   1 
ATOM   2364 O O   . ARG C 1 12  ? 22.60200  31.63600 -4.20300  1.000 38.84950 ? 11  ARG C O   1 
ATOM   2365 C CB  . ARG C 1 12  ? 20.14900  29.54900 -4.71200  1.000 44.73420 ? 11  ARG C CB  1 
ATOM   2366 C CG  . ARG C 1 12  ? 21.23200  29.19700 -5.71100  1.000 49.54663 ? 11  ARG C CG  1 
ATOM   2367 C CD  . ARG C 1 12  ? 21.99500  27.97400 -5.23400  1.000 49.80240 ? 11  ARG C CD  1 
ATOM   2368 N NE  . ARG C 1 12  ? 22.91200  27.45900 -6.24000  1.000 52.46279 ? 11  ARG C NE  1 
ATOM   2369 C CZ  . ARG C 1 12  ? 24.03300  28.05500 -6.61500  1.000 55.75676 ? 11  ARG C CZ  1 
ATOM   2370 N NH1 . ARG C 1 12  ? 24.38900  29.23500 -6.12300  1.000 51.59199 ? 11  ARG C NH1 1 
ATOM   2371 N NH2 . ARG C 1 12  ? 24.82300  27.44800 -7.50000  1.000 57.54240 ? 11  ARG C NH2 1 
ATOM   2372 N N   . LEU C 1 13  ? 20.65500  32.67900 -4.56100  1.000 42.58274 ? 12  LEU C N   1 
ATOM   2373 C CA  . LEU C 1 13  ? 21.27000  33.93800 -4.92800  1.000 42.84436 ? 12  LEU C CA  1 
ATOM   2374 C C   . LEU C 1 13  ? 21.10500  34.86700 -3.73900  1.000 46.49382 ? 12  LEU C C   1 
ATOM   2375 O O   . LEU C 1 13  ? 20.01400  34.94900 -3.15800  1.000 41.54280 ? 12  LEU C O   1 
ATOM   2376 C CB  . LEU C 1 13  ? 20.65500  34.55300 -6.18600  1.000 33.73627 ? 12  LEU C CB  1 
ATOM   2377 C CG  . LEU C 1 13  ? 20.17600  33.64500 -7.32200  1.000 38.55238 ? 12  LEU C CG  1 
ATOM   2378 C CD1 . LEU C 1 13  ? 19.54000  34.49800 -8.41100  1.000 38.89130 ? 12  LEU C CD1 1 
ATOM   2379 C CD2 . LEU C 1 13  ? 21.29100  32.78700 -7.89600  1.000 37.71066 ? 12  LEU C CD2 1 
ATOM   2380 N N   . THR C 1 14  ? 22.21300  35.47000 -3.31200  1.000 45.30243 ? 13  THR C N   1 
ATOM   2381 C CA  . THR C 1 14  ? 22.14500  36.59200 -2.40400  1.000 46.33099 ? 13  THR C CA  1 
ATOM   2382 C C   . THR C 1 14  ? 21.52600  37.77800 -3.13000  1.000 46.89978 ? 13  THR C C   1 
ATOM   2383 O O   . THR C 1 14  ? 21.54000  37.83000 -4.36200  1.000 50.49080 ? 13  THR C O   1 
ATOM   2384 C CB  . THR C 1 14  ? 23.54000  36.97000 -1.92300  1.000 49.82262 ? 13  THR C CB  1 
ATOM   2385 O OG1 . THR C 1 14  ? 24.38500  37.19500 -3.06200  1.000 39.58911 ? 13  THR C OG1 1 
ATOM   2386 C CG2 . THR C 1 14  ? 24.12200  35.84700 -1.05200  1.000 54.27780 ? 13  THR C CG2 1 
ATOM   2387 N N   . PRO C 1 15  ? 20.96800  38.74600 -2.38900  1.000 53.71271 ? 14  PRO C N   1 
ATOM   2388 C CA  . PRO C 1 15  ? 20.48900  39.98200 -3.02800  1.000 50.67212 ? 14  PRO C CA  1 
ATOM   2389 C C   . PRO C 1 15  ? 21.45900  40.56000 -4.06200  1.000 48.21394 ? 14  PRO C C   1 
ATOM   2390 O O   . PRO C 1 15  ? 21.05300  40.89800 -5.17800  1.000 43.04768 ? 14  PRO C O   1 
ATOM   2391 C CB  . PRO C 1 15  ? 20.29500  40.91600 -1.82800  1.000 50.39158 ? 14  PRO C CB  1 
ATOM   2392 C CG  . PRO C 1 15  ? 19.83000  39.98100 -0.74500  1.000 51.13807 ? 14  PRO C CG  1 
ATOM   2393 C CD  . PRO C 1 15  ? 20.52500  38.65500 -0.98100  1.000 48.98500 ? 14  PRO C CD  1 
ATOM   2394 N N   . SER C 1 16  ? 22.74900  40.62900 -3.71600  1.000 50.25613 ? 15  SER C N   1 
ATOM   2395 C CA  . SER C 1 16  ? 23.74800  41.15200 -4.64600  1.000 45.70266 ? 15  SER C CA  1 
ATOM   2396 C C   . SER C 1 16  ? 23.80300  40.33300 -5.93000  1.000 42.66117 ? 15  SER C C   1 
ATOM   2397 O O   . SER C 1 16  ? 24.00900  40.88300 -7.02200  1.000 46.71424 ? 15  SER C O   1 
ATOM   2398 C CB  . SER C 1 16  ? 25.11900  41.17200 -3.96600  1.000 49.45355 ? 15  SER C CB  1 
ATOM   2399 O OG  . SER C 1 16  ? 25.92900  42.20100 -4.50600  1.000 53.88181 ? 15  SER C OG  1 
ATOM   2400 N N   . ALA C 1 17  ? 23.62200  39.01000 -5.82300  1.000 40.78811 ? 16  ALA C N   1 
ATOM   2401 C CA  . ALA C 1 17  ? 23.60300  38.14500 -6.99900  1.000 38.63794 ? 16  ALA C CA  1 
ATOM   2402 C C   . ALA C 1 17  ? 22.32500  38.30000 -7.79200  1.000 40.33039 ? 16  ALA C C   1 
ATOM   2403 O O   . ALA C 1 17  ? 22.34900  38.21600 -9.02500  1.000 36.10523 ? 16  ALA C O   1 
ATOM   2404 C CB  . ALA C 1 17  ? 23.76300  36.68100 -6.59800  1.000 37.03430 ? 16  ALA C CB  1 
ATOM   2405 N N   . LYS C 1 18  ? 21.20400  38.52100 -7.09800  1.000 44.17529 ? 17  LYS C N   1 
ATOM   2406 C CA  . LYS C 1 18  ? 19.96900  38.86300 -7.79300  1.000 44.47282 ? 17  LYS C CA  1 
ATOM   2407 C C   . LYS C 1 18  ? 20.15400  40.13700 -8.59900  1.000 46.94600 ? 17  LYS C C   1 
ATOM   2408 O O   . LYS C 1 18  ? 19.72800  40.21700 -9.75800  1.000 41.86592 ? 17  LYS C O   1 
ATOM   2409 C CB  . LYS C 1 18  ? 18.82400  39.02600 -6.79900  1.000 38.71669 ? 17  LYS C CB  1 
ATOM   2410 C CG  . LYS C 1 18  ? 18.22900  37.72000 -6.34000  1.000 31.13496 ? 17  LYS C CG  1 
ATOM   2411 C CD  . LYS C 1 18  ? 17.34200  37.92800 -5.13900  1.000 39.73694 ? 17  LYS C CD  1 
ATOM   2412 C CE  . LYS C 1 18  ? 16.61500  36.65300 -4.71400  1.000 39.42461 ? 17  LYS C CE  1 
ATOM   2413 N NZ  . LYS C 1 18  ? 15.54100  36.91300 -3.71300  1.000 33.26698 ? 17  LYS C NZ  1 
ATOM   2414 N N   . HIS C 1 19  ? 20.77700  41.15000 -7.99200  1.000 43.35939 ? 18  HIS C N   1 
ATOM   2415 C CA  . HIS C 1 19  ? 21.11100  42.35300 -8.74100  1.000 45.61834 ? 18  HIS C CA  1 
ATOM   2416 C C   . HIS C 1 19  ? 21.98400  42.02700 -9.94700  1.000 44.79389 ? 18  HIS C C   1 
ATOM   2417 O O   . HIS C 1 19  ? 21.81200  42.61300 -11.02700 1.000 50.68779 ? 18  HIS C O   1 
ATOM   2418 C CB  . HIS C 1 19  ? 21.81100  43.36300 -7.83600  1.000 44.20104 ? 18  HIS C CB  1 
ATOM   2419 C CG  . HIS C 1 19  ? 21.77100  44.76400 -8.36200  1.000 48.02473 ? 18  HIS C CG  1 
ATOM   2420 N ND1 . HIS C 1 19  ? 22.66500  45.73500 -7.96800  1.000 56.34993 ? 18  HIS C ND1 1 
ATOM   2421 C CD2 . HIS C 1 19  ? 20.95600  45.35300 -9.26700  1.000 45.13535 ? 18  HIS C CD2 1 
ATOM   2422 C CE1 . HIS C 1 19  ? 22.39100  46.86700 -8.59100  1.000 48.94008 ? 18  HIS C CE1 1 
ATOM   2423 N NE2 . HIS C 1 19  ? 21.36200  46.66100 -9.38900  1.000 47.45226 ? 18  HIS C NE2 1 
ATOM   2424 N N   . ALA C 1 20  ? 22.92400  41.09600 -9.79500  1.000 40.93870 ? 19  ALA C N   1 
ATOM   2425 C CA  . ALA C 1 20  ? 23.78300  40.81300 -10.93800 1.000 46.50564 ? 19  ALA C CA  1 
ATOM   2426 C C   . ALA C 1 20  ? 23.00000  40.13200 -12.06400 1.000 40.59331 ? 19  ALA C C   1 
ATOM   2427 O O   . ALA C 1 20  ? 23.16500  40.47000 -13.23600 1.000 40.79506 ? 19  ALA C O   1 
ATOM   2428 C CB  . ALA C 1 20  ? 24.98700  39.97300 -10.50600 1.000 46.52823 ? 19  ALA C CB  1 
ATOM   2429 N N   . VAL C 1 21  ? 22.13800  39.17700 -11.72900 1.000 42.32890 ? 20  VAL C N   1 
ATOM   2430 C CA  . VAL C 1 21  ? 21.35000  38.48200 -12.75200 1.000 39.44929 ? 20  VAL C CA  1 
ATOM   2431 C C   . VAL C 1 21  ? 20.34300  39.44100 -13.39700 1.000 41.34570 ? 20  VAL C C   1 
ATOM   2432 O O   . VAL C 1 21  ? 20.15400  39.44000 -14.62600 1.000 43.34484 ? 20  VAL C O   1 
ATOM   2433 C CB  . VAL C 1 21  ? 20.67700  37.22800 -12.16900 1.000 34.98266 ? 20  VAL C CB  1 
ATOM   2434 C CG1 . VAL C 1 21  ? 19.54400  36.76500 -13.07300 1.000 35.80895 ? 20  VAL C CG1 1 
ATOM   2435 C CG2 . VAL C 1 21  ? 21.71800  36.12800 -12.00600 1.000 36.55658 ? 20  VAL C CG2 1 
ATOM   2436 N N   . ALA C 1 22  ? 19.69100  40.28800 -12.60200 1.000 37.17000 ? 21  ALA C N   1 
ATOM   2437 C CA  . ALA C 1 22  ? 18.78300  41.26600 -13.19700 1.000 35.53283 ? 21  ALA C CA  1 
ATOM   2438 C C   . ALA C 1 22  ? 19.49900  42.24100 -14.16100 1.000 40.44174 ? 21  ALA C C   1 
ATOM   2439 O O   . ALA C 1 22  ? 19.07700  42.36300 -15.32000 1.000 39.66459 ? 21  ALA C O   1 
ATOM   2440 C CB  . ALA C 1 22  ? 17.96100  41.91800 -12.09200 1.000 36.12137 ? 21  ALA C CB  1 
ATOM   2441 N N   . LYS C 1 23  ? 20.62400  42.87500 -13.75300 1.000 31.53804 ? 22  LYS C N   1 
ATOM   2442 C CA  . LYS C 1 23  ? 21.48400  43.45600 -14.80700 1.000 40.59716 ? 22  LYS C CA  1 
ATOM   2443 C C   . LYS C 1 23  ? 22.02300  42.57000 -15.96400 1.000 44.78464 ? 22  LYS C C   1 
ATOM   2444 O O   . LYS C 1 23  ? 22.05500  43.07100 -17.12100 1.000 39.53580 ? 22  LYS C O   1 
ATOM   2445 C CB  . LYS C 1 23  ? 22.48100  44.57700 -14.26800 1.000 49.49659 ? 22  LYS C CB  1 
ATOM   2446 C CG  . LYS C 1 23  ? 23.80600  45.21300 -14.88600 1.000 53.55601 ? 22  LYS C CG  1 
ATOM   2447 C CD  . LYS C 1 23  ? 25.06200  44.19100 -15.04000 1.000 60.45603 ? 22  LYS C CD  1 
ATOM   2448 C CE  . LYS C 1 23  ? 25.91600  43.16700 -14.16900 1.000 62.07954 ? 22  LYS C CE  1 
ATOM   2449 N NZ  . LYS C 1 23  ? 27.06100  42.09600 -14.44400 1.000 72.83808 ? 22  LYS C NZ  1 
ATOM   2450 N N   . ALA C 1 24  ? 22.31800  41.26900 -15.79700 1.000 43.09934 ? 23  ALA C N   1 
ATOM   2451 C CA  . ALA C 1 24  ? 22.67600  40.54900 -17.02700 1.000 37.23024 ? 23  ALA C CA  1 
ATOM   2452 C C   . ALA C 1 24  ? 21.51800  40.58100 -18.03000 1.000 37.04115 ? 23  ALA C C   1 
ATOM   2453 O O   . ALA C 1 24  ? 21.68900  40.90000 -19.22400 1.000 36.36724 ? 23  ALA C O   1 
ATOM   2454 C CB  . ALA C 1 24  ? 23.06800  39.10000 -16.73700 1.000 43.37052 ? 23  ALA C CB  1 
ATOM   2455 N N   . ILE C 1 25  ? 20.32300  40.29700 -17.52300 1.000 40.29262 ? 24  ILE C N   1 
ATOM   2456 C CA  . ILE C 1 25  ? 19.17000  40.11800 -18.37900 1.000 32.68753 ? 24  ILE C CA  1 
ATOM   2457 C C   . ILE C 1 25  ? 18.75400  41.43700 -18.99900 1.000 34.40422 ? 24  ILE C C   1 
ATOM   2458 O O   . ILE C 1 25  ? 18.55800  41.52400 -20.21900 1.000 37.73949 ? 24  ILE C O   1 
ATOM   2459 C CB  . ILE C 1 25  ? 18.04900  39.46000 -17.57300 1.000 30.17746 ? 24  ILE C CB  1 
ATOM   2460 C CG1 . ILE C 1 25  ? 18.48500  38.04300 -17.18400 1.000 26.40539 ? 24  ILE C CG1 1 
ATOM   2461 C CG2 . ILE C 1 25  ? 16.81600  39.38800 -18.41700 1.000 33.55222 ? 24  ILE C CG2 1 
ATOM   2462 C CD1 . ILE C 1 25  ? 17.63400  37.45600 -16.14500 1.000 25.52635 ? 24  ILE C CD1 1 
ATOM   2463 N N   . THR C 1 26  ? 18.66700  42.48800 -18.17800 1.000 37.66475 ? 25  THR C N   1 
ATOM   2464 C CA  . THR C 1 26  ? 18.32100  43.81700 -18.66400 1.000 34.72401 ? 25  THR C CA  1 
ATOM   2465 C C   . THR C 1 26  ? 19.26000  44.25600 -19.77300 1.000 31.81647 ? 25  THR C C   1 
ATOM   2466 O O   . THR C 1 26  ? 18.81700  44.68700 -20.85000 1.000 33.10846 ? 25  THR C O   1 
ATOM   2467 C CB  . THR C 1 26  ? 18.36600  44.78600 -17.49000 1.000 35.53947 ? 25  THR C CB  1 
ATOM   2468 O OG1 . THR C 1 26  ? 17.73800  44.16600 -16.36200 1.000 31.10430 ? 25  THR C OG1 1 
ATOM   2469 C CG2 . THR C 1 26  ? 17.66900  46.10700 -17.82200 1.000 37.42161 ? 25  THR C CG2 1 
ATOM   2470 N N   . ASP C 1 27  ? 20.57100  44.12600 -19.52300 1.000 39.48233 ? 26  ASP C N   1 
ATOM   2471 C CA  . ASP C 1 27  ? 21.57600  44.49900 -20.50900 1.000 31.23620 ? 26  ASP C CA  1 
ATOM   2472 C C   . ASP C 1 27  ? 21.39000  43.72700 -21.79600 1.000 30.63219 ? 26  ASP C C   1 
ATOM   2473 O O   . ASP C 1 27  ? 21.49200  44.30000 -22.88300 1.000 34.32195 ? 26  ASP C O   1 
ATOM   2474 C CB  . ASP C 1 27  ? 22.97000  44.25700 -19.93500 1.000 32.49907 ? 26  ASP C CB  1 
ATOM   2475 C CG  . ASP C 1 27  ? 23.40300  45.36100 -18.98700 1.000 44.26958 ? 26  ASP C CG  1 
ATOM   2476 O OD1 . ASP C 1 27  ? 23.00800  46.53700 -19.18400 1.000 54.38662 ? 26  ASP C OD1 1 
ATOM   2477 O OD2 . ASP C 1 27  ? 24.14900  45.05600 -18.04100 1.000 48.43630 ? 26  ASP C OD2 1 
ATOM   2478 N N   . ALA C 1 28  ? 21.07700  42.43100 -21.69300 1.000 33.22298 ? 27  ALA C N   1 
ATOM   2479 C CA  . ALA C 1 28  ? 20.91800  41.60000 -22.88200 1.000 27.58613 ? 27  ALA C CA  1 
ATOM   2480 C C   . ALA C 1 28  ? 19.74200  42.05600 -23.74000 1.000 34.65056 ? 27  ALA C C   1 
ATOM   2481 O O   . ALA C 1 28  ? 19.87400  42.22900 -24.97100 1.000 29.22577 ? 27  ALA C O   1 
ATOM   2482 C CB  . ALA C 1 28  ? 20.74200  40.15400 -22.45200 1.000 31.99721 ? 27  ALA C CB  1 
ATOM   2483 N N   . HIS C 1 29  ? 18.57900  42.26500 -23.10200 1.000 38.19918 ? 28  HIS C N   1 
ATOM   2484 C CA  . HIS C 1 29  ? 17.38300  42.66700 -23.85500 1.000 39.66092 ? 28  HIS C CA  1 
ATOM   2485 C C   . HIS C 1 29  ? 17.62600  44.02700 -24.50300 1.000 36.29601 ? 28  HIS C C   1 
ATOM   2486 O O   . HIS C 1 29  ? 17.40200  44.21000 -25.71300 1.000 30.84544 ? 28  HIS C O   1 
ATOM   2487 C CB  . HIS C 1 29  ? 16.12700  42.67100 -22.95100 1.000 29.74657 ? 28  HIS C CB  1 
ATOM   2488 C CG  . HIS C 1 29  ? 14.79300  42.64800 -23.68000 1.000 35.15516 ? 28  HIS C CG  1 
ATOM   2489 N ND1 . HIS C 1 29  ? 14.11500  41.47700 -23.96700 1.000 37.75915 ? 28  HIS C ND1 1 
ATOM   2490 C CD2 . HIS C 1 29  ? 13.97100  43.65400 -24.08500 1.000 33.50238 ? 28  HIS C CD2 1 
ATOM   2491 C CE1 . HIS C 1 29  ? 12.95700  41.75900 -24.54600 1.000 36.68600 ? 28  HIS C CE1 1 
ATOM   2492 N NE2 . HIS C 1 29  ? 12.83300  43.07700 -24.62200 1.000 42.97938 ? 28  HIS C NE2 1 
ATOM   2493 N N   . ARG C 1 30  ? 18.13700  44.99000 -23.73600 1.000 32.01507 ? 29  ARG C N   1 
ATOM   2494 C CA  . ARG C 1 30  ? 18.29200  46.28100 -24.39600 1.000 41.55070 ? 29  ARG C CA  1 
ATOM   2495 C C   . ARG C 1 30  ? 19.34000  46.20600 -25.52000 1.000 34.04253 ? 29  ARG C C   1 
ATOM   2496 O O   . ARG C 1 30  ? 19.11300  46.74000 -26.60600 1.000 31.66164 ? 29  ARG C O   1 
ATOM   2497 C CB  . ARG C 1 30  ? 18.67200  47.38800 -23.41300 1.000 42.74764 ? 29  ARG C CB  1 
ATOM   2498 C CG  . ARG C 1 30  ? 19.79000  48.14700 -24.02100 1.000 52.45653 ? 29  ARG C CG  1 
ATOM   2499 C CD  . ARG C 1 30  ? 20.67900  49.10000 -23.28000 1.000 55.84907 ? 29  ARG C CD  1 
ATOM   2500 N NE  . ARG C 1 30  ? 20.80100  50.22500 -24.19700 1.000 61.93836 ? 29  ARG C NE  1 
ATOM   2501 C CZ  . ARG C 1 30  ? 20.71600  51.51000 -23.88400 1.000 67.87851 ? 29  ARG C CZ  1 
ATOM   2502 N NH1 . ARG C 1 30  ? 21.05900  51.96000 -22.67900 1.000 72.39529 ? 29  ARG C NH1 1 
ATOM   2503 N NH2 . ARG C 1 30  ? 20.34200  52.38100 -24.81200 1.000 63.49590 ? 29  ARG C NH2 1 
ATOM   2504 N N   . GLY C 1 31  ? 20.44300  45.47400 -25.32200 1.000 35.79202 ? 30  GLY C N   1 
ATOM   2505 C CA  . GLY C 1 31  ? 21.48200  45.43700 -26.34100 1.000 33.62192 ? 30  GLY C CA  1 
ATOM   2506 C C   . GLY C 1 31  ? 20.98900  44.85100 -27.64500 1.000 38.84853 ? 30  GLY C C   1 
ATOM   2507 O O   . GLY C 1 31  ? 21.27800  45.38000 -28.72100 1.000 34.80424 ? 30  GLY C O   1 
ATOM   2508 N N   . LEU C 1 32  ? 20.19100  43.78700 -27.57100 1.000 35.01282 ? 31  LEU C N   1 
ATOM   2509 C CA  . LEU C 1 32  ? 19.76100  43.15900 -28.80600 1.000 27.42682 ? 31  LEU C CA  1 
ATOM   2510 C C   . LEU C 1 32  ? 18.45700  43.71000 -29.37300 1.000 29.24898 ? 31  LEU C C   1 
ATOM   2511 O O   . LEU C 1 32  ? 18.18300  43.49600 -30.55300 1.000 28.53593 ? 31  LEU C O   1 
ATOM   2512 C CB  . LEU C 1 32  ? 19.64200  41.65700 -28.58300 1.000 36.07055 ? 31  LEU C CB  1 
ATOM   2513 C CG  . LEU C 1 32  ? 21.00100  41.03800 -28.31200 1.000 35.84926 ? 31  LEU C CG  1 
ATOM   2514 C CD1 . LEU C 1 32  ? 20.84900  39.56500 -28.06600 1.000 30.92927 ? 31  LEU C CD1 1 
ATOM   2515 C CD2 . LEU C 1 32  ? 21.83800  41.26600 -29.55400 1.000 37.51270 ? 31  LEU C CD2 1 
ATOM   2516 N N   . THR C 1 33  ? 17.62800  44.38400 -28.57700 1.000 34.81594 ? 32  THR C N   1 
ATOM   2517 C CA  . THR C 1 33  ? 16.32200  44.83200 -29.05500 1.000 34.74091 ? 32  THR C CA  1 
ATOM   2518 C C   . THR C 1 33  ? 16.19200  46.33600 -29.20200 1.000 33.68842 ? 32  THR C C   1 
ATOM   2519 O O   . THR C 1 33  ? 15.30000  46.78400 -29.92400 1.000 39.26730 ? 32  THR C O   1 
ATOM   2520 C CB  . THR C 1 33  ? 15.20300  44.36800 -28.11700 1.000 34.81089 ? 32  THR C CB  1 
ATOM   2521 O OG1 . THR C 1 33  ? 15.37700  44.98600 -26.83300 1.000 41.66063 ? 32  THR C OG1 1 
ATOM   2522 C CG2 . THR C 1 33  ? 15.24500  42.88000 -27.95100 1.000 29.03577 ? 32  THR C CG2 1 
ATOM   2523 N N   . GLY C 1 34  ? 16.98000  47.11700 -28.47300 1.000 30.60544 ? 33  GLY C N   1 
ATOM   2524 C CA  . GLY C 1 34  ? 16.87700  48.55700 -28.49600 1.000 32.28285 ? 33  GLY C CA  1 
ATOM   2525 C C   . GLY C 1 34  ? 15.92500  49.12000 -27.48000 1.000 35.25945 ? 33  GLY C C   1 
ATOM   2526 O O   . GLY C 1 34  ? 15.93500  50.33300 -27.24100 1.000 35.66303 ? 33  GLY C O   1 
ATOM   2527 N N   . THR C 1 35  ? 15.14800  48.26900 -26.83300 1.000 42.21427 ? 34  THR C N   1 
ATOM   2528 C CA  . THR C 1 35  ? 14.21100  48.71200 -25.81900 1.000 44.17494 ? 34  THR C CA  1 
ATOM   2529 C C   . THR C 1 35  ? 14.94000  49.44700 -24.69900 1.000 45.58351 ? 34  THR C C   1 
ATOM   2530 O O   . THR C 1 35  ? 16.16400  49.35800 -24.53200 1.000 42.79889 ? 34  THR C O   1 
ATOM   2531 C CB  . THR C 1 35  ? 13.43000  47.51900 -25.26400 1.000 43.71163 ? 34  THR C CB  1 
ATOM   2532 O OG1 . THR C 1 35  ? 13.14200  46.60200 -26.32900 1.000 43.17682 ? 34  THR C OG1 1 
ATOM   2533 C CG2 . THR C 1 35  ? 12.14800  47.96000 -24.63300 1.000 44.41674 ? 34  THR C CG2 1 
ATOM   2534 N N   . GLN C 1 36  ? 14.18600  50.26100 -23.98600 1.000 47.12110 ? 35  GLN C N   1 
ATOM   2535 C CA  . GLN C 1 36  ? 14.74600  50.91100 -22.82200 1.000 41.71821 ? 35  GLN C CA  1 
ATOM   2536 C C   . GLN C 1 36  ? 14.90500  49.88100 -21.71100 1.000 44.76389 ? 35  GLN C C   1 
ATOM   2537 O O   . GLN C 1 36  ? 14.00500  49.06500 -21.45800 1.000 44.21036 ? 35  GLN C O   1 
ATOM   2538 C CB  . GLN C 1 36  ? 13.84800  52.06300 -22.39000 1.000 36.43695 ? 35  GLN C CB  1 
ATOM   2539 C CG  . GLN C 1 36  ? 13.77400  53.16200 -23.44500 1.000 39.44852 ? 35  GLN C CG  1 
ATOM   2540 C CD  . GLN C 1 36  ? 12.46900  53.17100 -24.23800 1.000 41.22946 ? 35  GLN C CD  1 
ATOM   2541 O OE1 . GLN C 1 36  ? 12.02100  52.13400 -24.70200 1.000 42.09078 ? 35  GLN C OE1 1 
ATOM   2542 N NE2 . GLN C 1 36  ? 11.86900  54.34500 -24.40800 1.000 37.32669 ? 35  GLN C NE2 1 
ATOM   2543 N N   . HIS C 1 37  ? 16.11000  49.85100 -21.16300 1.000 45.97443 ? 36  HIS C N   1 
ATOM   2544 C CA  . HIS C 1 37  ? 16.43900  49.76200 -19.75100 1.000 40.30166 ? 36  HIS C CA  1 
ATOM   2545 C C   . HIS C 1 37  ? 15.23200  49.56100 -18.84400 1.000 42.89298 ? 36  HIS C C   1 
ATOM   2546 O O   . HIS C 1 37  ? 14.97900  48.45000 -18.37100 1.000 34.72411 ? 36  HIS C O   1 
ATOM   2547 C CB  . HIS C 1 37  ? 17.15600  51.07400 -19.43700 1.000 48.46830 ? 36  HIS C CB  1 
ATOM   2548 C CG  . HIS C 1 37  ? 18.63800  50.94900 -19.39100 1.000 60.49955 ? 36  HIS C CG  1 
ATOM   2549 N ND1 . HIS C 1 37  ? 19.32200  50.51600 -18.27800 1.000 60.48346 ? 36  HIS C ND1 1 
ATOM   2550 C CD2 . HIS C 1 37  ? 19.56000  51.07600 -20.38000 1.000 57.20564 ? 36  HIS C CD2 1 
ATOM   2551 C CE1 . HIS C 1 37  ? 20.61400  50.45900 -18.55600 1.000 66.16110 ? 36  HIS C CE1 1 
ATOM   2552 N NE2 . HIS C 1 37  ? 20.78300  50.79000 -19.82700 1.000 59.58552 ? 36  HIS C NE2 1 
ATOM   2553 N N   . PHE C 1 38  ? 14.45000  50.62900 -18.63100 1.000 45.64672 ? 37  PHE C N   1 
ATOM   2554 C CA  . PHE C 1 38  ? 13.36200  50.60300 -17.65200 1.000 38.97309 ? 37  PHE C CA  1 
ATOM   2555 C C   . PHE C 1 38  ? 12.17500  49.73100 -18.06300 1.000 37.77716 ? 37  PHE C C   1 
ATOM   2556 O O   . PHE C 1 38  ? 11.30600  49.45700 -17.22100 1.000 38.32744 ? 37  PHE C O   1 
ATOM   2557 C CB  . PHE C 1 38  ? 12.87200  52.02400 -17.35400 1.000 38.58313 ? 37  PHE C CB  1 
ATOM   2558 C CG  . PHE C 1 38  ? 12.47200  52.80200 -18.57500 1.000 43.34259 ? 37  PHE C CG  1 
ATOM   2559 C CD1 . PHE C 1 38  ? 11.35600  52.43800 -19.31600 1.000 38.80995 ? 37  PHE C CD1 1 
ATOM   2560 C CD2 . PHE C 1 38  ? 13.21200  53.90600 -18.98600 1.000 42.92485 ? 37  PHE C CD2 1 
ATOM   2561 C CE1 . PHE C 1 38  ? 10.99400  53.14600 -20.43400 1.000 35.75306 ? 37  PHE C CE1 1 
ATOM   2562 C CE2 . PHE C 1 38  ? 12.84300  54.62700 -20.10800 1.000 37.66207 ? 37  PHE C CE2 1 
ATOM   2563 C CZ  . PHE C 1 38  ? 11.73800  54.24400 -20.82900 1.000 37.33475 ? 37  PHE C CZ  1 
ATOM   2564 N N   . LEU C 1 39  ? 12.09800  49.29100 -19.31700 1.000 33.29479 ? 38  LEU C N   1 
ATOM   2565 C CA  . LEU C 1 39  ? 10.99500  48.42900 -19.71300 1.000 33.54149 ? 38  LEU C CA  1 
ATOM   2566 C C   . LEU C 1 39  ? 11.24400  46.97900 -19.32300 1.000 35.05321 ? 38  LEU C C   1 
ATOM   2567 O O   . LEU C 1 39  ? 10.33400  46.15200 -19.47000 1.000 31.08064 ? 38  LEU C O   1 
ATOM   2568 C CB  . LEU C 1 39  ? 10.75800  48.52000 -21.22700 1.000 34.97642 ? 38  LEU C CB  1 
ATOM   2569 C CG  . LEU C 1 39  ? 9.68700   49.51600 -21.68700 1.000 41.72916 ? 38  LEU C CG  1 
ATOM   2570 C CD1 . LEU C 1 39  ? 9.46700   49.51000 -23.19700 1.000 35.20450 ? 38  LEU C CD1 1 
ATOM   2571 C CD2 . LEU C 1 39  ? 8.37100   49.30700 -20.94500 1.000 44.26753 ? 38  LEU C CD2 1 
ATOM   2572 N N   . ALA C 1 40  ? 12.45100  46.66300 -18.82900 1.000 31.84131 ? 39  ALA C N   1 
ATOM   2573 C CA  . ALA C 1 40  ? 12.85300  45.29600 -18.51500 1.000 32.87553 ? 39  ALA C CA  1 
ATOM   2574 C C   . ALA C 1 40  ? 12.52000  44.98000 -17.06500 1.000 31.20733 ? 39  ALA C C   1 
ATOM   2575 O O   . ALA C 1 40  ? 13.21700  45.42700 -16.15400 1.000 30.72675 ? 39  ALA C O   1 
ATOM   2576 C CB  . ALA C 1 40  ? 14.34400  45.11400 -18.76900 1.000 31.82880 ? 39  ALA C CB  1 
ATOM   2577 N N   . GLN C 1 41  ? 11.49200  44.15700 -16.85500 1.000 31.04701 ? 40  GLN C N   1 
ATOM   2578 C CA  . GLN C 1 41  ? 11.16600  43.67700 -15.52700 1.000 27.37970 ? 40  GLN C CA  1 
ATOM   2579 C C   . GLN C 1 41  ? 11.80700  42.32000 -15.30400 1.000 24.64472 ? 40  GLN C C   1 
ATOM   2580 O O   . GLN C 1 41  ? 11.72600  41.44400 -16.16100 1.000 26.36671 ? 40  GLN C O   1 
ATOM   2581 C CB  . GLN C 1 41  ? 9.65700   43.59000 -15.32500 1.000 26.43991 ? 40  GLN C CB  1 
ATOM   2582 C CG  . GLN C 1 41  ? 9.28100   42.85300 -14.03500 1.000 27.60183 ? 40  GLN C CG  1 
ATOM   2583 C CD  . GLN C 1 41  ? 7.81100   43.01300 -13.65000 1.000 32.97054 ? 40  GLN C CD  1 
ATOM   2584 O OE1 . GLN C 1 41  ? 7.13400   43.95500 -14.07900 1.000 28.95346 ? 40  GLN C OE1 1 
ATOM   2585 N NE2 . GLN C 1 41  ? 7.32900   42.11400 -12.81000 1.000 23.57442 ? 40  GLN C NE2 1 
ATOM   2586 N N   . VAL C 1 42  ? 12.45500  42.16100 -14.16200 1.000 26.16109 ? 41  VAL C N   1 
ATOM   2587 C CA  . VAL C 1 42  ? 12.94300  40.87500 -13.68200 1.000 28.43715 ? 41  VAL C CA  1 
ATOM   2588 C C   . VAL C 1 42  ? 12.22700  40.56500 -12.36700 1.000 27.35464 ? 41  VAL C C   1 
ATOM   2589 O O   . VAL C 1 42  ? 12.27200  41.35600 -11.41500 1.000 19.90925 ? 41  VAL C O   1 
ATOM   2590 C CB  . VAL C 1 42  ? 14.47600  40.87200 -13.51100 1.000 26.64837 ? 41  VAL C CB  1 
ATOM   2591 C CG1 . VAL C 1 42  ? 14.92000  39.64300 -12.75100 1.000 22.02245 ? 41  VAL C CG1 1 
ATOM   2592 C CG2 . VAL C 1 42  ? 15.16700  40.95800 -14.88800 1.000 20.06690 ? 41  VAL C CG2 1 
ATOM   2593 N N   . ASN C 1 43  ? 11.55300  39.42100 -12.32700 1.000 29.18458 ? 42  ASN C N   1 
ATOM   2594 C CA  . ASN C 1 43  ? 10.69900  39.02200 -11.21600 1.000 26.94662 ? 42  ASN C CA  1 
ATOM   2595 C C   . ASN C 1 43  ? 11.18100  37.64600 -10.74100 1.000 29.03366 ? 42  ASN C C   1 
ATOM   2596 O O   . ASN C 1 43  ? 11.02700  36.63900 -11.45000 1.000 26.06687 ? 42  ASN C O   1 
ATOM   2597 C CB  . ASN C 1 43  ? 9.23700   39.02500 -11.68800 1.000 25.04456 ? 42  ASN C CB  1 
ATOM   2598 C CG  . ASN C 1 43  ? 8.23900   39.19600 -10.56600 1.000 30.89512 ? 42  ASN C CG  1 
ATOM   2599 O OD1 . ASN C 1 43  ? 8.32400   38.54200 -9.51600  1.000 32.30290 ? 42  ASN C OD1 1 
ATOM   2600 N ND2 . ASN C 1 43  ? 7.25400   40.06100 -10.79400 1.000 31.33558 ? 42  ASN C ND2 1 
ATOM   2601 N N   . PHE C 1 44  ? 11.81700  37.61100 -9.57600  1.000 32.01948 ? 43  PHE C N   1 
ATOM   2602 C CA  . PHE C 1 44  ? 12.40200  36.38500 -9.04200  1.000 31.63671 ? 43  PHE C CA  1 
ATOM   2603 C C   . PHE C 1 44  ? 11.36400  35.61600 -8.24400  1.000 34.04483 ? 43  PHE C C   1 
ATOM   2604 O O   . PHE C 1 44  ? 10.82100  36.14200 -7.26700  1.000 35.23960 ? 43  PHE C O   1 
ATOM   2605 C CB  . PHE C 1 44  ? 13.59200  36.68700 -8.13900  1.000 35.51990 ? 43  PHE C CB  1 
ATOM   2606 C CG  . PHE C 1 44  ? 14.77800  37.14600 -8.86500  1.000 28.37587 ? 43  PHE C CG  1 
ATOM   2607 C CD1 . PHE C 1 44  ? 15.67400  36.23600 -9.38500  1.000 31.80586 ? 43  PHE C CD1 1 
ATOM   2608 C CD2 . PHE C 1 44  ? 14.99800  38.49700 -9.04700  1.000 27.02279 ? 43  PHE C CD2 1 
ATOM   2609 C CE1 . PHE C 1 44  ? 16.80000  36.66900 -10.08200 1.000 30.09279 ? 43  PHE C CE1 1 
ATOM   2610 C CE2 . PHE C 1 44  ? 16.11300  38.93800 -9.72300  1.000 33.87038 ? 43  PHE C CE2 1 
ATOM   2611 C CZ  . PHE C 1 44  ? 17.01700  38.02000 -10.25500 1.000 35.02689 ? 43  PHE C CZ  1 
ATOM   2612 N N   . GLN C 1 45  ? 11.10700  34.37100 -8.64100  1.000 33.10964 ? 44  GLN C N   1 
ATOM   2613 C CA  . GLN C 1 45  ? 10.23400  33.47000 -7.91000  1.000 28.86055 ? 44  GLN C CA  1 
ATOM   2614 C C   . GLN C 1 45  ? 11.11300  32.43500 -7.22700  1.000 36.10503 ? 44  GLN C C   1 
ATOM   2615 O O   . GLN C 1 45  ? 11.70900  31.56300 -7.88100  1.000 32.30712 ? 44  GLN C O   1 
ATOM   2616 C CB  . GLN C 1 45  ? 9.21100   32.84500 -8.83700  1.000 31.31153 ? 44  GLN C CB  1 
ATOM   2617 C CG  . GLN C 1 45  ? 8.48100   33.90000 -9.65400  1.000 32.17770 ? 44  GLN C CG  1 
ATOM   2618 C CD  . GLN C 1 45  ? 7.35600   34.55300 -8.89100  1.000 25.97997 ? 44  GLN C CD  1 
ATOM   2619 O OE1 . GLN C 1 45  ? 6.37000   33.91100 -8.59300  1.000 32.80470 ? 44  GLN C OE1 1 
ATOM   2620 N NE2 . GLN C 1 45  ? 7.49300   35.83600 -8.57700  1.000 29.90792 ? 44  GLN C NE2 1 
ATOM   2621 N N   . GLU C 1 46  ? 11.21500  32.57200 -5.90900  1.000 38.20838 ? 45  GLU C N   1 
ATOM   2622 C CA  . GLU C 1 46  ? 12.03100  31.71300 -5.07600  1.000 31.94839 ? 45  GLU C CA  1 
ATOM   2623 C C   . GLU C 1 46  ? 11.16100  30.61600 -4.49100  1.000 34.85801 ? 45  GLU C C   1 
ATOM   2624 O O   . GLU C 1 46  ? 10.10200  30.90100 -3.91900  1.000 39.37289 ? 45  GLU C O   1 
ATOM   2625 C CB  . GLU C 1 46  ? 12.67200  32.53800 -3.96300  1.000 32.79542 ? 45  GLU C CB  1 
ATOM   2626 C CG  . GLU C 1 46  ? 13.52600  33.66300 -4.50500  1.000 33.99330 ? 45  GLU C CG  1 
ATOM   2627 C CD  . GLU C 1 46  ? 14.50900  34.16500 -3.49400  1.000 42.41326 ? 45  GLU C CD  1 
ATOM   2628 O OE1 . GLU C 1 46  ? 14.05600  34.72700 -2.47400  1.000 50.60693 ? 45  GLU C OE1 1 
ATOM   2629 O OE2 . GLU C 1 46  ? 15.72900  33.93600 -3.68700  1.000 44.70159 ? 45  GLU C OE2 1 
ATOM   2630 N N   . GLN C 1 47  ? 11.61300  29.37400 -4.64100  1.000 30.44706 ? 46  GLN C N   1 
ATOM   2631 C CA  . GLN C 1 47  ? 11.02800  28.21400 -3.98700  1.000 39.04257 ? 46  GLN C CA  1 
ATOM   2632 C C   . GLN C 1 47  ? 12.12300  27.44300 -3.27000  1.000 39.00790 ? 46  GLN C C   1 
ATOM   2633 O O   . GLN C 1 47  ? 13.26800  27.44000 -3.71800  1.000 35.44680 ? 46  GLN C O   1 
ATOM   2634 C CB  . GLN C 1 47  ? 10.33800  27.26400 -4.99000  1.000 32.62952 ? 46  GLN C CB  1 
ATOM   2635 C CG  . GLN C 1 47  ? 9.07000   27.78400 -5.60300  1.000 30.51273 ? 46  GLN C CG  1 
ATOM   2636 C CD  . GLN C 1 47  ? 7.92500   27.87600 -4.61100  1.000 31.26507 ? 46  GLN C CD  1 
ATOM   2637 O OE1 . GLN C 1 47  ? 7.53400   26.88800 -3.98900  1.000 36.37045 ? 46  GLN C OE1 1 
ATOM   2638 N NE2 . GLN C 1 47  ? 7.39500   29.07300 -4.44300  1.000 29.17313 ? 46  GLN C NE2 1 
ATOM   2639 N N   . PRO C 1 48  ? 11.79300  26.74700 -2.18100  1.000 38.22366 ? 47  PRO C N   1 
ATOM   2640 C CA  . PRO C 1 48  ? 12.79700  25.93000 -1.47700  1.000 32.98481 ? 47  PRO C CA  1 
ATOM   2641 C C   . PRO C 1 48  ? 13.37600  24.82200 -2.35600  1.000 34.71930 ? 47  PRO C C   1 
ATOM   2642 O O   . PRO C 1 48  ? 12.71500  24.32000 -3.26800  1.000 38.47005 ? 47  PRO C O   1 
ATOM   2643 C CB  . PRO C 1 48  ? 12.01900  25.36000 -0.28800  1.000 32.71667 ? 47  PRO C CB  1 
ATOM   2644 C CG  . PRO C 1 48  ? 10.53400  25.69600 -0.55200  1.000 36.58531 ? 47  PRO C CG  1 
ATOM   2645 C CD  . PRO C 1 48  ? 10.55600  26.91900 -1.39400  1.000 35.89445 ? 47  PRO C CD  1 
ATOM   2646 N N   . ALA C 1 49  ? 14.65700  24.51300 -2.14000  1.000 29.41384 ? 48  ALA C N   1 
ATOM   2647 C CA  . ALA C 1 49  ? 15.30400  23.41200 -2.85800  1.000 39.44931 ? 48  ALA C CA  1 
ATOM   2648 C C   . ALA C 1 49  ? 14.50800  22.11100 -2.74100  1.000 33.10860 ? 48  ALA C C   1 
ATOM   2649 O O   . ALA C 1 49  ? 13.89200  21.81900 -1.70900  1.000 29.23468 ? 48  ALA C O   1 
ATOM   2650 C CB  . ALA C 1 49  ? 16.73900  23.19400 -2.36100  1.000 30.26085 ? 48  ALA C CB  1 
ATOM   2651 N N   . GLY C 1 50  ? 14.48000  21.35800 -3.83500  1.000 28.31170 ? 49  GLY C N   1 
ATOM   2652 C CA  . GLY C 1 50  ? 13.73700  20.12500 -3.89800  1.000 33.38275 ? 49  GLY C CA  1 
ATOM   2653 C C   . GLY C 1 50  ? 12.43400  20.25100 -4.63500  1.000 39.26019 ? 49  GLY C C   1 
ATOM   2654 O O   . GLY C 1 50  ? 11.72600  19.24100 -4.80600  1.000 33.94032 ? 49  GLY C O   1 
ATOM   2655 N N   . ASN C 1 51  ? 12.07500  21.48700 -4.99800  1.000 38.95561 ? 50  ASN C N   1 
ATOM   2656 C CA  . ASN C 1 51  ? 10.88800  21.82500 -5.76200  1.000 34.33822 ? 50  ASN C CA  1 
ATOM   2657 C C   . ASN C 1 51  ? 11.06300  21.62400 -7.26200  1.000 39.13775 ? 50  ASN C C   1 
ATOM   2658 O O   . ASN C 1 51  ? 10.07700  21.69300 -8.00000  1.000 40.00446 ? 50  ASN C O   1 
ATOM   2659 C CB  . ASN C 1 51  ? 10.52300  23.27600 -5.47400  1.000 31.55426 ? 50  ASN C CB  1 
ATOM   2660 C CG  . ASN C 1 51  ? 9.55100   23.39100 -4.34500  1.000 38.45353 ? 50  ASN C CG  1 
ATOM   2661 O OD1 . ASN C 1 51  ? 9.31100   22.41000 -3.61500  1.000 37.90148 ? 50  ASN C OD1 1 
ATOM   2662 N ND2 . ASN C 1 51  ? 8.95900   24.56700 -4.19100  1.000 35.93830 ? 50  ASN C ND2 1 
ATOM   2663 N N   . VAL C 1 52  ? 12.28600  21.42800 -7.73300  1.000 38.26189 ? 51  VAL C N   1 
ATOM   2664 C CA  . VAL C 1 52  ? 12.56400  21.24700 -9.14200  1.000 30.89695 ? 51  VAL C CA  1 
ATOM   2665 C C   . VAL C 1 52  ? 12.88700  19.77200 -9.32800  1.000 38.68901 ? 51  VAL C C   1 
ATOM   2666 O O   . VAL C 1 52  ? 13.83800  19.26300 -8.72200  1.000 42.43974 ? 51  VAL C O   1 
ATOM   2667 C CB  . VAL C 1 52  ? 13.70900  22.16900 -9.58900  1.000 35.69686 ? 51  VAL C CB  1 
ATOM   2668 C CG1 . VAL C 1 52  ? 13.92900  22.14300 -11.11100 1.000 33.54233 ? 51  VAL C CG1 1 
ATOM   2669 C CG2 . VAL C 1 52  ? 13.42200  23.58200 -9.13800  1.000 30.73482 ? 51  VAL C CG2 1 
ATOM   2670 N N   . PHE C 1 53  ? 12.12400  19.09300 -10.18600 1.000 36.12181 ? 52  PHE C N   1 
ATOM   2671 C CA  . PHE C 1 53  ? 12.36000  17.70000 -10.55000 1.000 34.09375 ? 52  PHE C CA  1 
ATOM   2672 C C   . PHE C 1 53  ? 12.72900  17.61600 -12.02400 1.000 38.48052 ? 52  PHE C C   1 
ATOM   2673 O O   . PHE C 1 53  ? 12.12800  18.28200 -12.87600 1.000 34.67983 ? 52  PHE C O   1 
ATOM   2674 C CB  . PHE C 1 53  ? 11.12900  16.82000 -10.26500 1.000 37.27874 ? 52  PHE C CB  1 
ATOM   2675 C CG  . PHE C 1 53  ? 10.92600  16.51500 -8.80000  1.000 39.96942 ? 52  PHE C CG  1 
ATOM   2676 C CD1 . PHE C 1 53  ? 10.47900  17.49700 -7.93100  1.000 36.45173 ? 52  PHE C CD1 1 
ATOM   2677 C CD2 . PHE C 1 53  ? 11.22400  15.25300 -8.28600  1.000 42.53667 ? 52  PHE C CD2 1 
ATOM   2678 C CE1 . PHE C 1 53  ? 10.31300  17.22800 -6.57200  1.000 46.13169 ? 52  PHE C CE1 1 
ATOM   2679 C CE2 . PHE C 1 53  ? 11.06400  14.97000 -6.92000  1.000 41.37520 ? 52  PHE C CE2 1 
ATOM   2680 C CZ  . PHE C 1 53  ? 10.60700  15.96000 -6.06200  1.000 43.68154 ? 52  PHE C CZ  1 
ATOM   2681 N N   . LEU C 1 54  ? 13.74700  16.82000 -12.31300 1.000 36.24827 ? 53  LEU C N   1 
ATOM   2682 C CA  . LEU C 1 54  ? 14.20600  16.60000 -13.67200 1.000 37.64917 ? 53  LEU C CA  1 
ATOM   2683 C C   . LEU C 1 54  ? 14.19200  15.10000 -13.92500 1.000 39.53852 ? 53  LEU C C   1 
ATOM   2684 O O   . LEU C 1 54  ? 14.79700  14.33600 -13.16600 1.000 41.81941 ? 53  LEU C O   1 
ATOM   2685 C CB  . LEU C 1 54  ? 15.59500  17.22600 -13.88400 1.000 34.64579 ? 53  LEU C CB  1 
ATOM   2686 C CG  . LEU C 1 54  ? 15.83600  18.76200 -13.88000 1.000 37.66362 ? 53  LEU C CG  1 
ATOM   2687 C CD1 . LEU C 1 54  ? 15.13000  19.46700 -15.00800 1.000 37.62562 ? 53  LEU C CD1 1 
ATOM   2688 C CD2 . LEU C 1 54  ? 15.35300  19.42200 -12.66400 1.000 39.99778 ? 53  LEU C CD2 1 
ATOM   2689 N N   . GLY C 1 55  ? 13.46100  14.68400 -14.95900 1.000 40.32174 ? 54  GLY C N   1 
ATOM   2690 C CA  . GLY C 1 55  ? 13.27100  13.27800 -15.24600 1.000 42.68312 ? 54  GLY C CA  1 
ATOM   2691 C C   . GLY C 1 55  ? 12.75900  12.47600 -14.06800 1.000 47.62769 ? 54  GLY C C   1 
ATOM   2692 O O   . GLY C 1 55  ? 13.04200  11.27300 -13.97100 1.000 49.47171 ? 54  GLY C O   1 
ATOM   2693 N N   . GLY C 1 56  ? 12.01300  13.13100 -13.15700 1.000 45.50110 ? 55  GLY C N   1 
ATOM   2694 C CA  . GLY C 1 56  ? 11.52300  12.50700 -11.93900 1.000 43.77191 ? 55  GLY C CA  1 
ATOM   2695 C C   . GLY C 1 56  ? 12.50400  12.54100 -10.78000 1.000 46.94381 ? 55  GLY C C   1 
ATOM   2696 O O   . GLY C 1 56  ? 12.15400  12.11500 -9.66200  1.000 39.24994 ? 55  GLY C O   1 
ATOM   2697 N N   . VAL C 1 57  ? 13.72100  13.03000 -11.01300 1.000 42.93099 ? 56  VAL C N   1 
ATOM   2698 C CA  . VAL C 1 57  ? 14.74800  13.10800 -9.98700  1.000 38.77446 ? 56  VAL C CA  1 
ATOM   2699 C C   . VAL C 1 57  ? 14.67800  14.49100 -9.36200  1.000 39.96352 ? 56  VAL C C   1 
ATOM   2700 O O   . VAL C 1 57  ? 14.62300  15.50700 -10.06800 1.000 40.97214 ? 56  VAL C O   1 
ATOM   2701 C CB  . VAL C 1 57  ? 16.14200  12.83400 -10.58700 1.000 44.66516 ? 56  VAL C CB  1 
ATOM   2702 C CG1 . VAL C 1 57  ? 17.25800  13.19200 -9.59500  1.000 33.20988 ? 56  VAL C CG1 1 
ATOM   2703 C CG2 . VAL C 1 57  ? 16.26300  11.38900 -11.04400 1.000 41.80168 ? 56  VAL C CG2 1 
ATOM   2704 N N   . GLN C 1 58  ? 14.63200  14.53000 -8.04500  1.000 36.76104 ? 57  GLN C N   1 
ATOM   2705 C CA  . GLN C 1 58  ? 14.64600  15.79700 -7.33500  1.000 35.45870 ? 57  GLN C CA  1 
ATOM   2706 C C   . GLN C 1 58  ? 16.00900  16.47900 -7.45500  1.000 45.82412 ? 57  GLN C C   1 
ATOM   2707 O O   . GLN C 1 58  ? 17.03700  15.82300 -7.65300  1.000 48.09027 ? 57  GLN C O   1 
ATOM   2708 C CB  . GLN C 1 58  ? 14.31300  15.57200 -5.86600  1.000 37.45449 ? 57  GLN C CB  1 
ATOM   2709 C CG  . GLN C 1 58  ? 14.00100  16.84000 -5.14600  1.000 40.52553 ? 57  GLN C CG  1 
ATOM   2710 C CD  . GLN C 1 58  ? 14.57300  16.84000 -3.78500  1.000 44.26782 ? 57  GLN C CD  1 
ATOM   2711 O OE1 . GLN C 1 58  ? 14.02400  16.22700 -2.87900  1.000 43.77083 ? 57  GLN C OE1 1 
ATOM   2712 N NE2 . GLN C 1 58  ? 15.71200  17.51300 -3.62000  1.000 45.06091 ? 57  GLN C NE2 1 
ATOM   2713 N N   . GLN C 1 59  ? 16.00800  17.81600 -7.40000  1.000 41.58299 ? 58  GLN C N   1 
ATOM   2714 C CA  . GLN C 1 59  ? 17.22800  18.61300 -7.49300  1.000 37.87008 ? 58  GLN C CA  1 
ATOM   2715 C C   . GLN C 1 59  ? 17.53100  19.39400 -6.21500  1.000 42.31507 ? 58  GLN C C   1 
ATOM   2716 O O   . GLN C 1 59  ? 16.66500  19.62400 -5.36000  1.000 39.26456 ? 58  GLN C O   1 
ATOM   2717 C CB  . GLN C 1 59  ? 17.17800  19.62300 -8.64300  1.000 41.53394 ? 58  GLN C CB  1 
ATOM   2718 C CG  . GLN C 1 59  ? 16.92800  19.00200 -9.97900  1.000 43.99184 ? 58  GLN C CG  1 
ATOM   2719 C CD  . GLN C 1 59  ? 18.10100  18.19600 -10.52500 1.000 42.43848 ? 58  GLN C CD  1 
ATOM   2720 O OE1 . GLN C 1 59  ? 19.24800  18.66000 -10.57100 1.000 50.22355 ? 58  GLN C OE1 1 
ATOM   2721 N NE2 . GLN C 1 59  ? 17.81200  16.97300 -10.93700 1.000 37.73314 ? 58  GLN C NE2 1 
ATOM   2722 N N   . GLY C 1 60  ? 18.80200  19.78100 -6.09500  1.000 43.74192 ? 59  GLY C N   1 
ATOM   2723 C CA  . GLY C 1 60  ? 19.22600  20.84900 -5.20700  1.000 48.35883 ? 59  GLY C CA  1 
ATOM   2724 C C   . GLY C 1 60  ? 18.82900  22.22500 -5.71800  1.000 45.64055 ? 59  GLY C C   1 
ATOM   2725 O O   . GLY C 1 60  ? 17.88900  22.35700 -6.51100  1.000 48.93417 ? 59  GLY C O   1 
ATOM   2726 N N   . GLY C 1 61  ? 19.51400  23.26900 -5.25400  1.000 46.96208 ? 60  GLY C N   1 
ATOM   2727 C CA  . GLY C 1 61  ? 19.01800  24.61500 -5.49800  1.000 49.02448 ? 60  GLY C CA  1 
ATOM   2728 C C   . GLY C 1 61  ? 19.57400  25.35500 -6.69800  1.000 46.29271 ? 60  GLY C C   1 
ATOM   2729 O O   . GLY C 1 61  ? 19.53800  26.58800 -6.74200  1.000 48.31962 ? 60  GLY C O   1 
ATOM   2730 N N   . ASP C 1 62  ? 20.00500  24.62300 -7.71800  1.000 49.71706 ? 61  ASP C N   1 
ATOM   2731 C CA  . ASP C 1 62  ? 20.86800  25.19200 -8.74200  1.000 46.19865 ? 61  ASP C CA  1 
ATOM   2732 C C   . ASP C 1 62  ? 20.13000  25.49700 -10.03900 1.000 38.96613 ? 61  ASP C C   1 
ATOM   2733 O O   . ASP C 1 62  ? 20.64300  26.26100 -10.85500 1.000 39.77284 ? 61  ASP C O   1 
ATOM   2734 C CB  . ASP C 1 62  ? 22.03200  24.24200 -9.04900  1.000 42.18809 ? 61  ASP C CB  1 
ATOM   2735 C CG  . ASP C 1 62  ? 23.26200  24.52400 -8.20500  1.000 42.45751 ? 61  ASP C CG  1 
ATOM   2736 O OD1 . ASP C 1 62  ? 23.12100  25.01900 -7.07000  1.000 47.73233 ? 61  ASP C OD1 1 
ATOM   2737 O OD2 . ASP C 1 62  ? 24.37400  24.17300 -8.63900  1.000 45.17725 ? 61  ASP C OD2 1 
ATOM   2738 N N   . THR C 1 63  ? 18.97200  24.88800 -10.26200 1.000 39.38955 ? 62  THR C N   1 
ATOM   2739 C CA  . THR C 1 63  ? 18.20800  25.12700 -11.48000 1.000 38.01105 ? 62  THR C CA  1 
ATOM   2740 C C   . THR C 1 63  ? 17.72500  26.56800 -11.56600 1.000 38.16424 ? 62  THR C C   1 
ATOM   2741 O O   . THR C 1 63  ? 17.12600  27.09900 -10.62800 1.000 38.04861 ? 62  THR C O   1 
ATOM   2742 C CB  . THR C 1 63  ? 17.00000  24.20100 -11.52600 1.000 36.68383 ? 62  THR C CB  1 
ATOM   2743 O OG1 . THR C 1 63  ? 17.44100  22.84300 -11.61700 1.000 52.67577 ? 62  THR C OG1 1 
ATOM   2744 C CG2 . THR C 1 63  ? 16.16500  24.51900 -12.72000 1.000 34.68775 ? 62  THR C CG2 1 
ATOM   2745 N N   . ILE C 1 64  ? 17.96400  27.19400 -12.70800 1.000 41.58496 ? 63  ILE C N   1 
ATOM   2746 C CA  . ILE C 1 64  ? 17.39800  28.49600 -13.01600 1.000 38.15477 ? 63  ILE C CA  1 
ATOM   2747 C C   . ILE C 1 64  ? 16.50200  28.32000 -14.22500 1.000 36.52829 ? 63  ILE C C   1 
ATOM   2748 O O   . ILE C 1 64  ? 16.92800  27.76300 -15.25200 1.000 28.33952 ? 63  ILE C O   1 
ATOM   2749 C CB  . ILE C 1 64  ? 18.46700  29.56600 -13.29500 1.000 33.55901 ? 63  ILE C CB  1 
ATOM   2750 C CG1 . ILE C 1 64  ? 19.49900  29.57100 -12.19200 1.000 37.21884 ? 63  ILE C CG1 1 
ATOM   2751 C CG2 . ILE C 1 64  ? 17.83100  30.93100 -13.38300 1.000 27.96884 ? 63  ILE C CG2 1 
ATOM   2752 C CD1 . ILE C 1 64  ? 20.88000  29.76000 -12.68500 1.000 41.91005 ? 63  ILE C CD1 1 
ATOM   2753 N N   . PHE C 1 65  ? 15.25600  28.75500 -14.09900 1.000 31.94146 ? 64  PHE C N   1 
ATOM   2754 C CA  . PHE C 1 65  ? 14.37900  28.72400 -15.25500 1.000 30.98219 ? 64  PHE C CA  1 
ATOM   2755 C C   . PHE C 1 65  ? 13.92700  30.14400 -15.54800 1.000 28.56622 ? 64  PHE C C   1 
ATOM   2756 O O   . PHE C 1 65  ? 13.45500  30.84800 -14.65800 1.000 31.48021 ? 64  PHE C O   1 
ATOM   2757 C CB  . PHE C 1 65  ? 13.18100  27.77200 -15.07500 1.000 31.10680 ? 64  PHE C CB  1 
ATOM   2758 C CG  . PHE C 1 65  ? 12.18600  27.85500 -16.21200 1.000 31.50789 ? 64  PHE C CG  1 
ATOM   2759 C CD1 . PHE C 1 65  ? 12.62900  27.89400 -17.53000 1.000 25.55524 ? 64  PHE C CD1 1 
ATOM   2760 C CD2 . PHE C 1 65  ? 10.83400  27.92000 -15.97200 1.000 29.64210 ? 64  PHE C CD2 1 
ATOM   2761 C CE1 . PHE C 1 65  ? 11.73900  27.99100 -18.58100 1.000 27.04362 ? 64  PHE C CE1 1 
ATOM   2762 C CE2 . PHE C 1 65  ? 9.94900   28.03200 -17.02600 1.000 33.03431 ? 64  PHE C CE2 1 
ATOM   2763 C CZ  . PHE C 1 65  ? 10.41100  28.06400 -18.32900 1.000 30.04115 ? 64  PHE C CZ  1 
ATOM   2764 N N   . VAL C 1 66  ? 14.11100  30.56900 -16.78300 1.000 24.78507 ? 65  VAL C N   1 
ATOM   2765 C CA  . VAL C 1 66  ? 13.75600  31.90800 -17.21900 1.000 33.18615 ? 65  VAL C CA  1 
ATOM   2766 C C   . VAL C 1 66  ? 12.62100  31.81100 -18.23300 1.000 35.24829 ? 65  VAL C C   1 
ATOM   2767 O O   . VAL C 1 66  ? 12.74400  31.13600 -19.26500 1.000 33.47937 ? 65  VAL C O   1 
ATOM   2768 C CB  . VAL C 1 66  ? 14.96900  32.65500 -17.78500 1.000 29.77649 ? 65  VAL C CB  1 
ATOM   2769 C CG1 . VAL C 1 66  ? 14.54700  34.06700 -18.26700 1.000 27.59463 ? 65  VAL C CG1 1 
ATOM   2770 C CG2 . VAL C 1 66  ? 16.01000  32.74300 -16.70400 1.000 21.22166 ? 65  VAL C CG2 1 
ATOM   2771 N N   . HIS C 1 67  ? 11.48800  32.39700 -17.89000 1.000 30.58385 ? 66  HIS C N   1 
ATOM   2772 C CA  . HIS C 1 67  ? 10.37800  32.55200 -18.81200 1.000 29.75897 ? 66  HIS C CA  1 
ATOM   2773 C C   . HIS C 1 67  ? 10.30900  34.03700 -19.17800 1.000 33.22480 ? 66  HIS C C   1 
ATOM   2774 O O   . HIS C 1 67  ? 9.83000   34.86400 -18.39700 1.000 33.37930 ? 66  HIS C O   1 
ATOM   2775 C CB  . HIS C 1 67  ? 9.08800   32.02700 -18.17900 1.000 22.88956 ? 66  HIS C CB  1 
ATOM   2776 C CG  . HIS C 1 67  ? 7.99600   31.75800 -19.16800 1.000 21.51922 ? 66  HIS C CG  1 
ATOM   2777 N ND1 . HIS C 1 67  ? 6.73000   31.36900 -18.79300 1.000 21.27137 ? 66  HIS C ND1 1 
ATOM   2778 C CD2 . HIS C 1 67  ? 7.98300   31.82500 -20.51600 1.000 20.47892 ? 66  HIS C CD2 1 
ATOM   2779 C CE1 . HIS C 1 67  ? 5.97500   31.22800 -19.86600 1.000 23.02086 ? 66  HIS C CE1 1 
ATOM   2780 N NE2 . HIS C 1 67  ? 6.71500   31.49600 -20.92800 1.000 25.79093 ? 66  HIS C NE2 1 
ATOM   2781 N N   . GLY C 1 68  ? 10.77000  34.38100 -20.37900 1.000 30.99463 ? 67  GLY C N   1 
ATOM   2782 C CA  . GLY C 1 68  ? 10.70600  35.74900 -20.85500 1.000 30.11140 ? 67  GLY C CA  1 
ATOM   2783 C C   . GLY C 1 68  ? 9.47600   35.92900 -21.73500 1.000 36.24520 ? 67  GLY C C   1 
ATOM   2784 O O   . GLY C 1 68  ? 9.24600   35.15800 -22.67800 1.000 29.51821 ? 67  GLY C O   1 
ATOM   2785 N N   . LEU C 1 69  ? 8.70600   36.96900 -21.42600 1.000 29.97833 ? 68  LEU C N   1 
ATOM   2786 C CA  . LEU C 1 69  ? 7.50700   37.30900 -22.17600 1.000 28.39956 ? 68  LEU C CA  1 
ATOM   2787 C C   . LEU C 1 69  ? 7.77900   38.53000 -23.05300 1.000 26.09736 ? 68  LEU C C   1 
ATOM   2788 O O   . LEU C 1 69  ? 8.16600   39.59000 -22.54800 1.000 30.39309 ? 68  LEU C O   1 
ATOM   2789 C CB  . LEU C 1 69  ? 6.34600   37.55300 -21.21500 1.000 27.43149 ? 68  LEU C CB  1 
ATOM   2790 C CG  . LEU C 1 69  ? 6.25900   36.39500 -20.22800 1.000 28.59159 ? 68  LEU C CG  1 
ATOM   2791 C CD1 . LEU C 1 69  ? 5.29000   36.67200 -19.10500 1.000 21.24672 ? 68  LEU C CD1 1 
ATOM   2792 C CD2 . LEU C 1 69  ? 5.90600   35.07100 -20.95800 1.000 22.51420 ? 68  LEU C CD2 1 
ATOM   2793 N N   . HIS C 1 70  ? 7.64900   38.35600 -24.36400 1.000 27.57383 ? 69  HIS C N   1 
ATOM   2794 C CA  . HIS C 1 70  ? 7.96200   39.38200 -25.35100 1.000 35.64023 ? 69  HIS C CA  1 
ATOM   2795 C C   . HIS C 1 70  ? 6.70000   39.73400 -26.12400 1.000 35.64317 ? 69  HIS C C   1 
ATOM   2796 O O   . HIS C 1 70  ? 5.72800   38.95700 -26.15900 1.000 30.12020 ? 69  HIS C O   1 
ATOM   2797 C CB  . HIS C 1 70  ? 9.04200   38.92600 -26.35100 1.000 22.88819 ? 69  HIS C CB  1 
ATOM   2798 C CG  . HIS C 1 70  ? 10.31700  38.48600 -25.70400 1.000 30.89890 ? 69  HIS C CG  1 
ATOM   2799 N ND1 . HIS C 1 70  ? 10.59600  38.70900 -24.37000 1.000 31.26846 ? 69  HIS C ND1 1 
ATOM   2800 C CD2 . HIS C 1 70  ? 11.38900  37.83000 -26.20600 1.000 29.90245 ? 69  HIS C CD2 1 
ATOM   2801 C CE1 . HIS C 1 70  ? 11.78500  38.21600 -24.07900 1.000 24.61045 ? 69  HIS C CE1 1 
ATOM   2802 N NE2 . HIS C 1 70  ? 12.27900  37.66000 -25.17100 1.000 32.45234 ? 69  HIS C NE2 1 
ATOM   2803 N N   . ARG C 1 71  ? 6.78400   40.81300 -26.85900 1.000 30.73732 ? 70  ARG C N   1 
ATOM   2804 C CA  . ARG C 1 71  ? 5.75600   41.01700 -27.80000 1.000 34.83864 ? 70  ARG C CA  1 
ATOM   2805 C C   . ARG C 1 71  ? 6.29300   40.47500 -29.11200 1.000 36.10529 ? 70  ARG C C   1 
ATOM   2806 O O   . ARG C 1 71  ? 7.47100   40.42300 -29.36200 1.000 40.24311 ? 70  ARG C O   1 
ATOM   2807 C CB  . ARG C 1 71  ? 5.25800   42.42900 -27.88500 1.000 33.07192 ? 70  ARG C CB  1 
ATOM   2808 C CG  . ARG C 1 71  ? 6.26700   43.46200 -28.16900 1.000 40.18836 ? 70  ARG C CG  1 
ATOM   2809 C CD  . ARG C 1 71  ? 6.04000   44.65600 -27.28200 1.000 39.73944 ? 70  ARG C CD  1 
ATOM   2810 N NE  . ARG C 1 71  ? 7.32200   45.16000 -27.00800 1.000 29.95203 ? 70  ARG C NE  1 
ATOM   2811 C CZ  . ARG C 1 71  ? 7.89800   46.19900 -27.54700 1.000 39.60771 ? 70  ARG C CZ  1 
ATOM   2812 N NH1 . ARG C 1 71  ? 7.26000   47.00900 -28.34300 1.000 46.10358 ? 70  ARG C NH1 1 
ATOM   2813 N NH2 . ARG C 1 71  ? 9.12600   46.41800 -27.15700 1.000 34.22500 ? 70  ARG C NH2 1 
ATOM   2814 N N   . GLU C 1 72  ? 5.38600   40.05700 -29.95900 1.000 33.46941 ? 71  GLU C N   1 
ATOM   2815 C CA  . GLU C 1 72  ? 5.65900   39.49200 -31.27400 1.000 28.27759 ? 71  GLU C CA  1 
ATOM   2816 C C   . GLU C 1 72  ? 6.23800   40.53800 -32.22600 1.000 27.92903 ? 71  GLU C C   1 
ATOM   2817 O O   . GLU C 1 72  ? 6.05300   41.74400 -32.04100 1.000 30.25172 ? 71  GLU C O   1 
ATOM   2818 C CB  . GLU C 1 72  ? 4.35600   38.92300 -31.83800 1.000 33.14200 ? 71  GLU C CB  1 
ATOM   2819 C CG  . GLU C 1 72  ? 3.74600   37.86100 -30.90100 1.000 32.60169 ? 71  GLU C CG  1 
ATOM   2820 C CD  . GLU C 1 72  ? 2.45800   37.23800 -31.40100 1.000 36.16652 ? 71  GLU C CD  1 
ATOM   2821 O OE1 . GLU C 1 72  ? 1.68500   37.92500 -32.09100 1.000 41.38100 ? 71  GLU C OE1 1 
ATOM   2822 O OE2 . GLU C 1 72  ? 2.23000   36.03300 -31.13000 1.000 48.35332 ? 71  GLU C OE2 1 
ATOM   2823 N N   . GLY C 1 73  ? 6.96500   40.05700 -33.24700 1.000 23.02107 ? 72  GLY C N   1 
ATOM   2824 C CA  . GLY C 1 73  ? 7.55300   40.91600 -34.27100 1.000 26.72867 ? 72  GLY C CA  1 
ATOM   2825 C C   . GLY C 1 73  ? 9.05300   40.78400 -34.55900 1.000 30.11708 ? 72  GLY C C   1 
ATOM   2826 O O   . GLY C 1 73  ? 9.54500   41.25700 -35.59400 1.000 27.37746 ? 72  GLY C O   1 
ATOM   2827 N N   . ARG C 1 74  ? 9.79100   40.11300 -33.68400 1.000 28.91531 ? 73  ARG C N   1 
ATOM   2828 C CA  . ARG C 1 74  ? 11.21900  39.88500 -33.84900 1.000 26.34970 ? 73  ARG C CA  1 
ATOM   2829 C C   . ARG C 1 74  ? 11.53400  38.55400 -34.56600 1.000 24.78830 ? 73  ARG C C   1 
ATOM   2830 O O   . ARG C 1 74  ? 10.75600  37.60500 -34.56200 1.000 19.65707 ? 73  ARG C O   1 
ATOM   2831 C CB  . ARG C 1 74  ? 11.88400  39.90200 -32.48000 1.000 25.74409 ? 73  ARG C CB  1 
ATOM   2832 C CG  . ARG C 1 74  ? 11.36600  40.99600 -31.59700 1.000 29.84095 ? 73  ARG C CG  1 
ATOM   2833 C CD  . ARG C 1 74  ? 12.41700  41.45800 -30.59600 1.000 24.05955 ? 73  ARG C CD  1 
ATOM   2834 N NE  . ARG C 1 74  ? 11.96800  42.65700 -29.90700 1.000 22.69353 ? 73  ARG C NE  1 
ATOM   2835 C CZ  . ARG C 1 74  ? 11.68400  42.72500 -28.61700 1.000 31.17183 ? 73  ARG C CZ  1 
ATOM   2836 N NH1 . ARG C 1 74  ? 11.83800  41.68300 -27.81400 1.000 27.87481 ? 73  ARG C NH1 1 
ATOM   2837 N NH2 . ARG C 1 74  ? 11.23400  43.86700 -28.11600 1.000 35.37295 ? 73  ARG C NH2 1 
ATOM   2838 N N   . SER C 1 75  ? 12.70400  38.49700 -35.18600 1.000 30.18418 ? 74  SER C N   1 
ATOM   2839 C CA  . SER C 1 75  ? 13.10300  37.30100 -35.91400 1.000 27.50943 ? 74  SER C CA  1 
ATOM   2840 C C   . SER C 1 75  ? 13.58200  36.19300 -34.97700 1.000 30.83603 ? 74  SER C C   1 
ATOM   2841 O O   . SER C 1 75  ? 14.09600  36.43300 -33.87800 1.000 30.03714 ? 74  SER C O   1 
ATOM   2842 C CB  . SER C 1 75  ? 14.21000  37.61900 -36.91800 1.000 29.33649 ? 74  SER C CB  1 
ATOM   2843 O OG  . SER C 1 75  ? 15.44700  37.86200 -36.27300 1.000 30.26387 ? 74  SER C OG  1 
ATOM   2844 N N   . ALA C 1 76  ? 13.44200  34.95900 -35.46200 1.000 36.15925 ? 75  ALA C N   1 
ATOM   2845 C CA  . ALA C 1 76  ? 13.93100  33.79000 -34.74000 1.000 31.45171 ? 75  ALA C CA  1 
ATOM   2846 C C   . ALA C 1 76  ? 15.43500  33.87500 -34.48700 1.000 32.25438 ? 75  ALA C C   1 
ATOM   2847 O O   . ALA C 1 76  ? 15.92600  33.51000 -33.40900 1.000 29.37824 ? 75  ALA C O   1 
ATOM   2848 C CB  . ALA C 1 76  ? 13.59300  32.54200 -35.55200 1.000 25.09586 ? 75  ALA C CB  1 
ATOM   2849 N N   . ASP C 1 77  ? 16.17400  34.37000 -35.47300 1.000 37.24717 ? 76  ASP C N   1 
ATOM   2850 C CA  . ASP C 1 77  ? 17.62500  34.51000 -35.37200 1.000 36.74425 ? 76  ASP C CA  1 
ATOM   2851 C C   . ASP C 1 77  ? 18.03000  35.34000 -34.15100 1.000 31.56261 ? 76  ASP C C   1 
ATOM   2852 O O   . ASP C 1 77  ? 18.84000  34.91600 -33.31300 1.000 32.58345 ? 76  ASP C O   1 
ATOM   2853 C CB  . ASP C 1 77  ? 18.07800  35.13100 -36.69000 1.000 26.52434 ? 76  ASP C CB  1 
ATOM   2854 C CG  . ASP C 1 77  ? 19.34900  35.84200 -36.58800 1.000 39.02310 ? 76  ASP C CG  1 
ATOM   2855 O OD1 . ASP C 1 77  ? 20.39900  35.17700 -36.46100 1.000 47.09866 ? 76  ASP C OD1 1 
ATOM   2856 O OD2 . ASP C 1 77  ? 19.28500  37.08200 -36.65400 1.000 41.93546 ? 76  ASP C OD2 1 
ATOM   2857 N N   . LEU C 1 78  ? 17.41500  36.50500 -34.01800 1.000 27.79001 ? 77  LEU C N   1 
ATOM   2858 C CA  . LEU C 1 78  ? 17.70400  37.44200 -32.94500 1.000 28.23141 ? 77  LEU C CA  1 
ATOM   2859 C C   . LEU C 1 78  ? 17.22500  36.92200 -31.59400 1.000 28.65316 ? 77  LEU C C   1 
ATOM   2860 O O   . LEU C 1 78  ? 17.86000  37.17300 -30.56200 1.000 24.03209 ? 77  LEU C O   1 
ATOM   2861 C CB  . LEU C 1 78  ? 17.01700  38.76600 -33.28500 1.000 30.18462 ? 77  LEU C CB  1 
ATOM   2862 C CG  . LEU C 1 78  ? 16.65000  39.68700 -32.14200 1.000 27.89738 ? 77  LEU C CG  1 
ATOM   2863 C CD1 . LEU C 1 78  ? 17.87400  40.47200 -31.72400 1.000 29.42744 ? 77  LEU C CD1 1 
ATOM   2864 C CD2 . LEU C 1 78  ? 15.53900  40.57200 -32.61700 1.000 32.37793 ? 77  LEU C CD2 1 
ATOM   2865 N N   . LYS C 1 79  ? 16.08500  36.21700 -31.57700 1.000 29.50684 ? 78  LYS C N   1 
ATOM   2866 C CA  . LYS C 1 79  ? 15.60700  35.63900 -30.33100 1.000 26.73765 ? 78  LYS C CA  1 
ATOM   2867 C C   . LYS C 1 79  ? 16.56800  34.56500 -29.84400 1.000 27.53222 ? 78  LYS C C   1 
ATOM   2868 O O   . LYS C 1 79  ? 16.87800  34.50000 -28.64800 1.000 25.70547 ? 78  LYS C O   1 
ATOM   2869 C CB  . LYS C 1 79  ? 14.19500  35.08500 -30.51900 1.000 32.00080 ? 78  LYS C CB  1 
ATOM   2870 C CG  . LYS C 1 79  ? 13.04800  36.10300 -30.34500 1.000 27.33914 ? 78  LYS C CG  1 
ATOM   2871 C CD  . LYS C 1 79  ? 11.69600  35.39600 -30.50100 1.000 23.04693 ? 78  LYS C CD  1 
ATOM   2872 C CE  . LYS C 1 79  ? 11.41500  35.21700 -31.97400 1.000 29.34861 ? 78  LYS C CE  1 
ATOM   2873 N NZ  . LYS C 1 79  ? 10.22800  34.39100 -32.32700 1.000 26.22095 ? 78  LYS C NZ  1 
ATOM   2874 N N   . GLY C 1 80  ? 17.09700  33.75700 -30.76800 1.000 28.55094 ? 79  GLY C N   1 
ATOM   2875 C CA  . GLY C 1 80  ? 18.11000  32.78200 -30.39800 1.000 25.12160 ? 79  GLY C CA  1 
ATOM   2876 C C   . GLY C 1 80  ? 19.36400  33.44700 -29.86400 1.000 27.29618 ? 79  GLY C C   1 
ATOM   2877 O O   . GLY C 1 80  ? 19.97800  32.97000 -28.90100 1.000 22.17157 ? 79  GLY C O   1 
ATOM   2878 N N   . GLN C 1 81  ? 19.77000  34.55200 -30.49100 1.000 28.40421 ? 80  GLN C N   1 
ATOM   2879 C CA  . GLN C 1 81  ? 20.92700  35.27900 -29.98300 1.000 25.71857 ? 80  GLN C CA  1 
ATOM   2880 C C   . GLN C 1 81  ? 20.66900  35.79800 -28.57900 1.000 25.44281 ? 80  GLN C C   1 
ATOM   2881 O O   . GLN C 1 81  ? 21.54700  35.71800 -27.71500 1.000 26.06858 ? 80  GLN C O   1 
ATOM   2882 C CB  . GLN C 1 81  ? 21.27600  36.42000 -30.91100 1.000 24.91195 ? 80  GLN C CB  1 
ATOM   2883 C CG  . GLN C 1 81  ? 22.22400  36.06000 -31.99600 1.000 26.19324 ? 80  GLN C CG  1 
ATOM   2884 C CD  . GLN C 1 81  ? 22.47700  37.26500 -32.85400 1.000 32.83090 ? 80  GLN C CD  1 
ATOM   2885 O OE1 . GLN C 1 81  ? 22.44600  38.40700 -32.36200 1.000 26.29471 ? 80  GLN C OE1 1 
ATOM   2886 N NE2 . GLN C 1 81  ? 22.74700  37.03800 -34.12800 1.000 31.55698 ? 80  GLN C NE2 1 
ATOM   2887 N N   . LEU C 1 82  ? 19.46700  36.34100 -28.34100 1.000 25.60544 ? 81  LEU C N   1 
ATOM   2888 C CA  . LEU C 1 82  ? 19.10100  36.85900 -27.02500 1.000 24.40601 ? 81  LEU C CA  1 
ATOM   2889 C C   . LEU C 1 82  ? 19.07500  35.76100 -25.96700 1.000 26.25647 ? 81  LEU C C   1 
ATOM   2890 O O   . LEU C 1 82  ? 19.56100  35.95900 -24.84300 1.000 27.05403 ? 81  LEU C O   1 
ATOM   2891 C CB  . LEU C 1 82  ? 17.74900  37.56900 -27.10800 1.000 22.39365 ? 81  LEU C CB  1 
ATOM   2892 C CG  . LEU C 1 82  ? 17.09600  38.03500 -25.80500 1.000 21.83054 ? 81  LEU C CG  1 
ATOM   2893 C CD1 . LEU C 1 82  ? 18.17300  38.81800 -25.02000 1.000 30.24020 ? 81  LEU C CD1 1 
ATOM   2894 C CD2 . LEU C 1 82  ? 15.81000  38.90400 -26.04600 1.000 18.61040 ? 81  LEU C CD2 1 
ATOM   2895 N N   . ALA C 1 83  ? 18.48500  34.60400 -26.30100 1.000 25.52771 ? 82  ALA C N   1 
ATOM   2896 C CA  . ALA C 1 83  ? 18.42000  33.48900 -25.36100 1.000 24.93309 ? 82  ALA C CA  1 
ATOM   2897 C C   . ALA C 1 83  ? 19.80900  32.95900 -25.05000 1.000 27.33532 ? 82  ALA C C   1 
ATOM   2898 O O   . ALA C 1 83  ? 20.13500  32.70700 -23.88300 1.000 30.12513 ? 82  ALA C O   1 
ATOM   2899 C CB  . ALA C 1 83  ? 17.54300  32.36200 -25.91600 1.000 22.18802 ? 82  ALA C CB  1 
ATOM   2900 N N   . GLN C 1 84  ? 20.64300  32.79600 -26.07600 1.000 23.09407 ? 83  GLN C N   1 
ATOM   2901 C CA  . GLN C 1 84  ? 22.01500  32.36100 -25.85000 1.000 25.03035 ? 83  GLN C CA  1 
ATOM   2902 C C   . GLN C 1 84  ? 22.76700  33.33900 -24.95200 1.000 27.84904 ? 83  GLN C C   1 
ATOM   2903 O O   . GLN C 1 84  ? 23.42600  32.92000 -23.98400 1.000 29.85450 ? 83  GLN C O   1 
ATOM   2904 C CB  . GLN C 1 84  ? 22.73100  32.19800 -27.19000 1.000 23.92544 ? 83  GLN C CB  1 
ATOM   2905 C CG  . GLN C 1 84  ? 24.14700  31.70500 -27.05400 1.000 28.54576 ? 83  GLN C CG  1 
ATOM   2906 C CD  . GLN C 1 84  ? 24.20600  30.34500 -26.42200 1.000 30.28449 ? 83  GLN C CD  1 
ATOM   2907 O OE1 . GLN C 1 84  ? 23.93900  29.34900 -27.07700 1.000 35.54032 ? 83  GLN C OE1 1 
ATOM   2908 N NE2 . GLN C 1 84  ? 24.54900  30.29000 -25.14200 1.000 37.22681 ? 83  GLN C NE2 1 
ATOM   2909 N N   . ARG C 1 85  ? 22.65900  34.65400 -25.23200 1.000 22.95872 ? 84  ARG C N   1 
ATOM   2910 C CA  . ARG C 1 85  ? 23.37000  35.61000 -24.39600 1.000 27.90999 ? 84  ARG C CA  1 
ATOM   2911 C C   . ARG C 1 85  ? 22.83000  35.58300 -22.97900 1.000 30.67494 ? 84  ARG C C   1 
ATOM   2912 O O   . ARG C 1 85  ? 23.58000  35.75700 -22.02100 1.000 30.92433 ? 84  ARG C O   1 
ATOM   2913 C CB  . ARG C 1 85  ? 23.27600  37.03600 -24.93500 1.000 28.95891 ? 84  ARG C CB  1 
ATOM   2914 C CG  . ARG C 1 85  ? 24.07100  37.99400 -24.03000 1.000 34.96589 ? 84  ARG C CG  1 
ATOM   2915 C CD  . ARG C 1 85  ? 23.84900  39.46500 -24.26200 1.000 36.26031 ? 84  ARG C CD  1 
ATOM   2916 N NE  . ARG C 1 85  ? 24.09700  39.88300 -25.63500 1.000 43.47615 ? 84  ARG C NE  1 
ATOM   2917 C CZ  . ARG C 1 85  ? 23.99300  41.13900 -26.06100 1.000 50.85720 ? 84  ARG C CZ  1 
ATOM   2918 N NH1 . ARG C 1 85  ? 23.62000  42.12100 -25.24600 1.000 47.43314 ? 84  ARG C NH1 1 
ATOM   2919 N NH2 . ARG C 1 85  ? 24.26100  41.41900 -27.33700 1.000 50.15608 ? 84  ARG C NH2 1 
ATOM   2920 N N   . ILE C 1 86  ? 21.53700  35.33400 -22.81600 1.000 36.20921 ? 85  ILE C N   1 
ATOM   2921 C CA  . ILE C 1 86  ? 21.00600  35.22600 -21.46800 1.000 33.91591 ? 85  ILE C CA  1 
ATOM   2922 C C   . ILE C 1 86  ? 21.60200  34.01800 -20.76200 1.000 30.50332 ? 85  ILE C C   1 
ATOM   2923 O O   . ILE C 1 86  ? 22.06400  34.12900 -19.62100 1.000 34.37003 ? 85  ILE C O   1 
ATOM   2924 C CB  . ILE C 1 86  ? 19.46800  35.21400 -21.49900 1.000 30.58974 ? 85  ILE C CB  1 
ATOM   2925 C CG1 . ILE C 1 86  ? 18.98000  36.66200 -21.38500 1.000 25.68452 ? 85  ILE C CG1 1 
ATOM   2926 C CG2 . ILE C 1 86  ? 18.86400  34.24800 -20.43900 1.000 28.55433 ? 85  ILE C CG2 1 
ATOM   2927 C CD1 . ILE C 1 86  ? 17.55800  36.87800 -21.79900 1.000 26.20095 ? 85  ILE C CD1 1 
ATOM   2928 N N   . VAL C 1 87  ? 21.64800  32.86800 -21.44500 1.000 31.53239 ? 86  VAL C N   1 
ATOM   2929 C CA  . VAL C 1 87  ? 22.26100  31.66200 -20.88000 1.000 31.86446 ? 86  VAL C CA  1 
ATOM   2930 C C   . VAL C 1 87  ? 23.65900  31.97200 -20.35400 1.000 32.86816 ? 86  VAL C C   1 
ATOM   2931 O O   . VAL C 1 87  ? 23.96000  31.77500 -19.16900 1.000 33.28373 ? 86  VAL C O   1 
ATOM   2932 C CB  . VAL C 1 87  ? 22.29900  30.54000 -21.93600 1.000 33.13379 ? 86  VAL C CB  1 
ATOM   2933 C CG1 . VAL C 1 87  ? 23.44200  29.54200 -21.65600 1.000 30.21133 ? 86  VAL C CG1 1 
ATOM   2934 C CG2 . VAL C 1 87  ? 20.95700  29.83100 -22.01300 1.000 30.72035 ? 86  VAL C CG2 1 
ATOM   2935 N N   . ASP C 1 88  ? 24.50300  32.53400 -21.21900 1.000 34.36708 ? 87  ASP C N   1 
ATOM   2936 C CA  . ASP C 1 88  ? 25.89800  32.81200 -20.86000 1.000 36.36723 ? 87  ASP C CA  1 
ATOM   2937 C C   . ASP C 1 88  ? 26.01900  33.84200 -19.73100 1.000 40.33906 ? 87  ASP C C   1 
ATOM   2938 O O   . ASP C 1 88  ? 26.73000  33.62100 -18.73200 1.000 49.70791 ? 87  ASP C O   1 
ATOM   2939 C CB  . ASP C 1 88  ? 26.66600  33.28900 -22.10000 1.000 36.39905 ? 87  ASP C CB  1 
ATOM   2940 C CG  . ASP C 1 88  ? 26.62200  32.27700 -23.26400 1.000 41.67960 ? 87  ASP C CG  1 
ATOM   2941 O OD1 . ASP C 1 88  ? 26.40100  31.04900 -23.03200 1.000 37.34365 ? 87  ASP C OD1 1 
ATOM   2942 O OD2 . ASP C 1 88  ? 26.85100  32.71900 -24.41300 1.000 38.07387 ? 87  ASP C OD2 1 
ATOM   2943 N N   . ASP C 1 89  ? 25.36100  34.99400 -19.87700 1.000 32.75438 ? 88  ASP C N   1 
ATOM   2944 C CA  . ASP C 1 89  ? 25.59700  36.07600 -18.93100 1.000 38.87891 ? 88  ASP C CA  1 
ATOM   2945 C C   . ASP C 1 89  ? 24.94500  35.82000 -17.58200 1.000 42.53687 ? 88  ASP C C   1 
ATOM   2946 O O   . ASP C 1 89  ? 25.44400  36.31100 -16.56300 1.000 48.85853 ? 88  ASP C O   1 
ATOM   2947 C CB  . ASP C 1 89  ? 25.14000  37.41300 -19.51300 1.000 43.64232 ? 88  ASP C CB  1 
ATOM   2948 C CG  . ASP C 1 89  ? 26.04700  37.88600 -20.61100 1.000 41.21812 ? 88  ASP C CG  1 
ATOM   2949 O OD1 . ASP C 1 89  ? 26.81800  37.05100 -21.13300 1.000 44.09565 ? 88  ASP C OD1 1 
ATOM   2950 O OD2 . ASP C 1 89  ? 26.02000  39.07900 -20.93500 1.000 45.09191 ? 88  ASP C OD2 1 
ATOM   2951 N N   . VAL C 1 90  ? 23.84400  35.06600 -17.54000 1.000 43.87046 ? 89  VAL C N   1 
ATOM   2952 C CA  . VAL C 1 90  ? 23.32000  34.64000 -16.24800 1.000 42.34741 ? 89  VAL C CA  1 
ATOM   2953 C C   . VAL C 1 90  ? 24.23700  33.59700 -15.63200 1.000 41.52392 ? 89  VAL C C   1 
ATOM   2954 O O   . VAL C 1 90  ? 24.46700  33.60200 -14.41500 1.000 36.96729 ? 89  VAL C O   1 
ATOM   2955 C CB  . VAL C 1 90  ? 21.88400  34.12500 -16.39900 1.000 36.62816 ? 89  VAL C CB  1 
ATOM   2956 C CG1 . VAL C 1 90  ? 21.41700  33.49500 -15.09900 1.000 32.24920 ? 89  VAL C CG1 1 
ATOM   2957 C CG2 . VAL C 1 90  ? 20.98700  35.28000 -16.80300 1.000 40.53743 ? 89  VAL C CG2 1 
ATOM   2958 N N   . SER C 1 91  ? 24.80100  32.70500 -16.46600 1.000 43.33679 ? 90  SER C N   1 
ATOM   2959 C CA  . SER C 1 91  ? 25.80800  31.76500 -15.97800 1.000 46.50761 ? 90  SER C CA  1 
ATOM   2960 C C   . SER C 1 91  ? 26.91600  32.48100 -15.22500 1.000 44.22021 ? 90  SER C C   1 
ATOM   2961 O O   . SER C 1 91  ? 27.41000  31.98700 -14.20600 1.000 43.14326 ? 90  SER C O   1 
ATOM   2962 C CB  . SER C 1 91  ? 26.42600  30.98300 -17.13400 1.000 36.44921 ? 90  SER C CB  1 
ATOM   2963 O OG  . SER C 1 91  ? 27.56200  30.30700 -16.64500 1.000 40.49711 ? 90  SER C OG  1 
ATOM   2964 N N   . VAL C 1 92  ? 27.35400  33.62600 -15.74400 1.000 44.63413 ? 91  VAL C N   1 
ATOM   2965 C CA  . VAL C 1 92  ? 28.43300  34.34100 -15.07000 1.000 43.39400 ? 91  VAL C CA  1 
ATOM   2966 C C   . VAL C 1 92  ? 27.90500  35.13200 -13.87600 1.000 46.39326 ? 91  VAL C C   1 
ATOM   2967 O O   . VAL C 1 92  ? 28.38800  34.96500 -12.74800 1.000 49.29859 ? 91  VAL C O   1 
ATOM   2968 C CB  . VAL C 1 92  ? 29.20500  35.22000 -16.07000 1.000 36.58322 ? 91  VAL C CB  1 
ATOM   2969 C CG1 . VAL C 1 92  ? 29.85000  36.41000 -15.37500 1.000 34.64679 ? 91  VAL C CG1 1 
ATOM   2970 C CG2 . VAL C 1 92  ? 30.26900  34.37500 -16.73200 1.000 40.46529 ? 91  VAL C CG2 1 
ATOM   2971 N N   . ALA C 1 93  ? 26.87900  35.96000 -14.08100 1.000 39.76073 ? 92  ALA C N   1 
ATOM   2972 C CA  . ALA C 1 93  ? 26.37100  36.78000 -12.98600 1.000 44.79384 ? 92  ALA C CA  1 
ATOM   2973 C C   . ALA C 1 93  ? 25.99100  35.93200 -11.77100 1.000 45.73010 ? 92  ALA C C   1 
ATOM   2974 O O   . ALA C 1 93  ? 26.35600  36.26100 -10.63800 1.000 48.33842 ? 92  ALA C O   1 
ATOM   2975 C CB  . ALA C 1 93  ? 25.17100  37.60700 -13.46400 1.000 47.97687 ? 92  ALA C CB  1 
ATOM   2976 N N   . ALA C 1 94  ? 25.25400  34.83500 -11.98900 1.000 42.32269 ? 93  ALA C N   1 
ATOM   2977 C CA  . ALA C 1 94  ? 24.79900  33.94700 -10.92200 1.000 44.80706 ? 93  ALA C CA  1 
ATOM   2978 C C   . ALA C 1 94  ? 25.82600  32.90000 -10.49800 1.000 47.20671 ? 93  ALA C C   1 
ATOM   2979 O O   . ALA C 1 94  ? 25.65600  32.28700 -9.43800  1.000 42.55623 ? 93  ALA C O   1 
ATOM   2980 C CB  . ALA C 1 94  ? 23.51600  33.22000 -11.34700 1.000 41.63148 ? 93  ALA C CB  1 
ATOM   2981 N N   . GLU C 1 95  ? 26.89000  32.70400 -11.27500 1.000 49.01517 ? 94  GLU C N   1 
ATOM   2982 C CA  . GLU C 1 95  ? 27.93200  31.72100 -10.98500 1.000 49.02869 ? 94  GLU C CA  1 
ATOM   2983 C C   . GLU C 1 95  ? 27.38400  30.29800 -11.03800 1.000 50.29959 ? 94  GLU C C   1 
ATOM   2984 O O   . GLU C 1 95  ? 27.64200  29.47700 -10.15300 1.000 51.74634 ? 94  GLU C O   1 
ATOM   2985 C CB  . GLU C 1 95  ? 28.59800  31.98500 -9.63500  1.000 42.55155 ? 94  GLU C CB  1 
ATOM   2986 C CG  . GLU C 1 95  ? 29.84500  32.78700 -9.76300  1.000 45.31819 ? 94  GLU C CG  1 
ATOM   2987 C CD  . GLU C 1 95  ? 30.11900  33.61400 -8.55200  1.000 57.69201 ? 94  GLU C CD  1 
ATOM   2988 O OE1 . GLU C 1 95  ? 29.15000  33.99900 -7.86400  1.000 58.01759 ? 94  GLU C OE1 1 
ATOM   2989 O OE2 . GLU C 1 95  ? 31.31700  33.85600 -8.27600  1.000 66.61116 ? 94  GLU C OE2 1 
ATOM   2990 N N   . ILE C 1 96  ? 26.63900  30.00400 -12.09700 1.000 46.85140 ? 95  ILE C N   1 
ATOM   2991 C CA  . ILE C 1 96  ? 26.03200  28.69400 -12.27400 1.000 44.89066 ? 95  ILE C CA  1 
ATOM   2992 C C   . ILE C 1 96  ? 26.39400  28.20800 -13.67400 1.000 48.40139 ? 95  ILE C C   1 
ATOM   2993 O O   . ILE C 1 96  ? 26.57800  29.01200 -14.59300 1.000 48.43007 ? 95  ILE C O   1 
ATOM   2994 C CB  . ILE C 1 96  ? 24.51300  28.78300 -12.06000 1.000 46.19302 ? 95  ILE C CB  1 
ATOM   2995 C CG1 . ILE C 1 96  ? 24.24000  29.08600 -10.60300 1.000 53.96784 ? 95  ILE C CG1 1 
ATOM   2996 C CG2 . ILE C 1 96  ? 23.85200  27.46600 -12.31000 1.000 47.66163 ? 95  ILE C CG2 1 
ATOM   2997 C CD1 . ILE C 1 96  ? 22.85400  28.67700 -10.13300 1.000 56.02871 ? 95  ILE C CD1 1 
ATOM   2998 N N   . ASP C 1 97  ? 26.50000  26.89100 -13.83500 1.000 40.81642 ? 96  ASP C N   1 
ATOM   2999 C CA  . ASP C 1 97  ? 26.80300  26.33400 -15.14400 1.000 40.00192 ? 96  ASP C CA  1 
ATOM   3000 C C   . ASP C 1 97  ? 25.64700  26.43900 -16.13300 1.000 36.20908 ? 96  ASP C C   1 
ATOM   3001 O O   . ASP C 1 97  ? 24.48200  26.45200 -15.76300 1.000 35.58048 ? 96  ASP C O   1 
ATOM   3002 C CB  . ASP C 1 97  ? 27.18800  24.86900 -15.07300 1.000 49.49011 ? 96  ASP C CB  1 
ATOM   3003 C CG  . ASP C 1 97  ? 28.14200  24.50400 -16.19300 1.000 55.99902 ? 96  ASP C CG  1 
ATOM   3004 O OD1 . ASP C 1 97  ? 29.06200  25.31600 -16.45800 1.000 52.54157 ? 96  ASP C OD1 1 
ATOM   3005 O OD2 . ASP C 1 97  ? 28.01900  23.41000 -16.78900 1.000 49.13887 ? 96  ASP C OD2 1 
ATOM   3006 N N   . ARG C 1 98  ? 26.00600  26.45100 -17.42500 1.000 42.58159 ? 97  ARG C N   1 
ATOM   3007 C CA  . ARG C 1 98  ? 25.01900  26.39900 -18.50000 1.000 39.28797 ? 97  ARG C CA  1 
ATOM   3008 C C   . ARG C 1 98  ? 24.06800  25.21100 -18.35100 1.000 41.85748 ? 97  ARG C C   1 
ATOM   3009 O O   . ARG C 1 98  ? 22.86900  25.34600 -18.63500 1.000 36.15675 ? 97  ARG C O   1 
ATOM   3010 C CB  . ARG C 1 98  ? 25.71600  26.32100 -19.87800 1.000 38.57087 ? 97  ARG C CB  1 
ATOM   3011 C CG  . ARG C 1 98  ? 26.90400  27.28000 -20.13200 1.000 47.10421 ? 97  ARG C CG  1 
ATOM   3012 C CD  . ARG C 1 98  ? 28.11200  26.52600 -20.75500 1.000 58.51341 ? 97  ARG C CD  1 
ATOM   3013 N NE  . ARG C 1 98  ? 28.86700  25.72300 -19.78000 1.000 65.97143 ? 97  ARG C NE  1 
ATOM   3014 C CZ  . ARG C 1 98  ? 30.11900  25.28900 -19.93600 1.000 54.17046 ? 97  ARG C CZ  1 
ATOM   3015 N NH1 . ARG C 1 98  ? 30.88800  25.72500 -20.92400 1.000 49.35207 ? 97  ARG C NH1 1 
ATOM   3016 N NH2 . ARG C 1 98  ? 30.63900  24.45400 -19.03400 1.000 51.34908 ? 97  ARG C NH2 1 
ATOM   3017 N N   . LYS C 1 99  ? 24.56100  24.06100 -17.85700 1.000 42.13273 ? 98  LYS C N   1 
ATOM   3018 C CA  . LYS C 1 99  ? 23.70500  22.87800 -17.75400 1.000 44.06285 ? 98  LYS C CA  1 
ATOM   3019 C C   . LYS C 1 99  ? 22.54100  23.07600 -16.78800 1.000 42.53539 ? 98  LYS C C   1 
ATOM   3020 O O   . LYS C 1 99  ? 21.62600  22.24300 -16.77900 1.000 42.58867 ? 98  LYS C O   1 
ATOM   3021 C CB  . LYS C 1 99  ? 24.47900  21.61200 -17.32700 1.000 46.86031 ? 98  LYS C CB  1 
ATOM   3022 C CG  . LYS C 1 99  ? 25.72200  21.82400 -16.49200 1.000 48.99595 ? 98  LYS C CG  1 
ATOM   3023 C CD  . LYS C 1 99  ? 26.38300  20.51100 -16.05600 1.000 49.21926 ? 98  LYS C CD  1 
ATOM   3024 C CE  . LYS C 1 99  ? 27.75000  20.77800 -15.38500 1.000 55.86935 ? 98  LYS C CE  1 
ATOM   3025 N NZ  . LYS C 1 99  ? 27.71700  21.16900 -13.93400 1.000 46.10244 ? 98  LYS C NZ  1 
ATOM   3026 N N   . HIS C 1 100 ? 22.57300  24.11300 -15.94800 1.000 37.24703 ? 99  HIS C N   1 
ATOM   3027 C CA  . HIS C 1 100 ? 21.48800  24.40200 -15.01500 1.000 41.90726 ? 99  HIS C CA  1 
ATOM   3028 C C   . HIS C 1 100 ? 20.51900  25.48000 -15.52000 1.000 39.43829 ? 99  HIS C C   1 
ATOM   3029 O O   . HIS C 1 100 ? 19.61900  25.88800 -14.77000 1.000 37.18652 ? 99  HIS C O   1 
ATOM   3030 C CB  . HIS C 1 100 ? 22.06400  24.82700 -13.65500 1.000 36.78115 ? 99  HIS C CB  1 
ATOM   3031 C CG  . HIS C 1 100 ? 22.59000  23.68600 -12.83400 1.000 41.56945 ? 99  HIS C CG  1 
ATOM   3032 N ND1 . HIS C 1 100 ? 21.76600  22.81000 -12.15700 1.000 47.03332 ? 99  HIS C ND1 1 
ATOM   3033 C CD2 . HIS C 1 100 ? 23.85500  23.27900 -12.57800 1.000 41.26111 ? 99  HIS C CD2 1 
ATOM   3034 C CE1 . HIS C 1 100 ? 22.50000  21.91200 -11.52600 1.000 40.76996 ? 99  HIS C CE1 1 
ATOM   3035 N NE2 . HIS C 1 100 ? 23.77100  22.17300 -11.76700 1.000 40.16678 ? 99  HIS C NE2 1 
ATOM   3036 N N   . ILE C 1 101 ? 20.66900  25.94800 -16.75900 1.000 35.34928 ? 100 ILE C N   1 
ATOM   3037 C CA  . ILE C 1 101 ? 19.97300  27.14600 -17.23200 1.000 34.18025 ? 100 ILE C CA  1 
ATOM   3038 C C   . ILE C 1 101 ? 18.94900  26.73800 -18.28100 1.000 35.02363 ? 100 ILE C C   1 
ATOM   3039 O O   . ILE C 1 101 ? 19.30400  26.19200 -19.34100 1.000 29.78083 ? 100 ILE C O   1 
ATOM   3040 C CB  . ILE C 1 101 ? 20.92700  28.19200 -17.84300 1.000 36.35612 ? 100 ILE C CB  1 
ATOM   3041 C CG1 . ILE C 1 101 ? 22.09600  28.61500 -16.94400 1.000 32.48404 ? 100 ILE C CG1 1 
ATOM   3042 C CG2 . ILE C 1 101 ? 20.14400  29.39600 -18.27400 1.000 32.24967 ? 100 ILE C CG2 1 
ATOM   3043 C CD1 . ILE C 1 101 ? 21.95600  28.36900 -15.52400 1.000 32.59726 ? 100 ILE C CD1 1 
ATOM   3044 N N   . TRP C 1 102 ? 17.68500  27.05100 -18.01700 1.000 36.19498 ? 101 TRP C N   1 
ATOM   3045 C CA  . TRP C 1 102 ? 16.63000  26.87800 -19.00000 1.000 31.35817 ? 101 TRP C CA  1 
ATOM   3046 C C   . TRP C 1 102 ? 16.08100  28.25900 -19.34200 1.000 27.73154 ? 101 TRP C C   1 
ATOM   3047 O O   . TRP C 1 102 ? 15.95900  29.10800 -18.45800 1.000 32.06744 ? 101 TRP C O   1 
ATOM   3048 C CB  . TRP C 1 102 ? 15.53600  25.95300 -18.46000 1.000 31.71508 ? 101 TRP C CB  1 
ATOM   3049 C CG  . TRP C 1 102 ? 16.00900  24.55700 -18.02900 1.000 37.69793 ? 101 TRP C CG  1 
ATOM   3050 C CD1 . TRP C 1 102 ? 17.15100  24.23600 -17.33200 1.000 34.42290 ? 101 TRP C CD1 1 
ATOM   3051 C CD2 . TRP C 1 102 ? 15.32500  23.31100 -18.26200 1.000 30.78920 ? 101 TRP C CD2 1 
ATOM   3052 N NE1 . TRP C 1 102 ? 17.22100  22.87500 -17.14000 1.000 36.93377 ? 101 TRP C NE1 1 
ATOM   3053 C CE2 . TRP C 1 102 ? 16.11100  22.29000 -17.69400 1.000 34.08780 ? 101 TRP C CE2 1 
ATOM   3054 C CE3 . TRP C 1 102 ? 14.13200  22.96600 -18.90600 1.000 25.05390 ? 101 TRP C CE3 1 
ATOM   3055 C CZ2 . TRP C 1 102 ? 15.74200  20.94800 -17.75100 1.000 37.02217 ? 101 TRP C CZ2 1 
ATOM   3056 C CZ3 . TRP C 1 102 ? 13.76900  21.63600 -18.96800 1.000 37.22981 ? 101 TRP C CZ3 1 
ATOM   3057 C CH2 . TRP C 1 102 ? 14.56700  20.63700 -18.38300 1.000 35.62642 ? 101 TRP C CH2 1 
ATOM   3058 N N   . VAL C 1 103 ? 15.81500  28.50500 -20.63100 1.000 29.37352 ? 102 VAL C N   1 
ATOM   3059 C CA  . VAL C 1 103 ? 15.31900  29.79000 -21.13700 1.000 26.90069 ? 102 VAL C CA  1 
ATOM   3060 C C   . VAL C 1 103 ? 14.24100  29.54500 -22.18300 1.000 27.46768 ? 102 VAL C C   1 
ATOM   3061 O O   . VAL C 1 103 ? 14.50100  28.89800 -23.20900 1.000 25.68158 ? 102 VAL C O   1 
ATOM   3062 C CB  . VAL C 1 103 ? 16.41900  30.66600 -21.75800 1.000 23.85433 ? 102 VAL C CB  1 
ATOM   3063 C CG1 . VAL C 1 103 ? 15.86200  32.04600 -22.06000 1.000 19.40509 ? 102 VAL C CG1 1 
ATOM   3064 C CG2 . VAL C 1 103 ? 17.60100  30.78000 -20.82100 1.000 32.30238 ? 102 VAL C CG2 1 
ATOM   3065 N N   . TYR C 1 104 ? 13.05600  30.11300 -21.95300 1.000 19.34253 ? 103 TYR C N   1 
ATOM   3066 C CA  . TYR C 1 104 ? 11.91200  29.99500 -22.84300 1.000 27.15009 ? 103 TYR C CA  1 
ATOM   3067 C C   . TYR C 1 104 ? 11.38100  31.39800 -23.12100 1.000 28.24093 ? 103 TYR C C   1 
ATOM   3068 O O   . TYR C 1 104 ? 11.13300  32.16600 -22.18700 1.000 26.18705 ? 103 TYR C O   1 
ATOM   3069 C CB  . TYR C 1 104 ? 10.77900  29.14300 -22.22700 1.000 25.60613 ? 103 TYR C CB  1 
ATOM   3070 C CG  . TYR C 1 104 ? 10.90900  27.62800 -22.16700 1.000 29.09139 ? 103 TYR C CG  1 
ATOM   3071 C CD1 . TYR C 1 104 ? 12.11200  26.96000 -22.46700 1.000 27.23526 ? 103 TYR C CD1 1 
ATOM   3072 C CD2 . TYR C 1 104 ? 9.78800   26.84700 -21.82900 1.000 32.99918 ? 103 TYR C CD2 1 
ATOM   3073 C CE1 . TYR C 1 104 ? 12.20400  25.56200 -22.41500 1.000 25.58541 ? 103 TYR C CE1 1 
ATOM   3074 C CE2 . TYR C 1 104 ? 9.86100   25.44400 -21.76800 1.000 32.82309 ? 103 TYR C CE2 1 
ATOM   3075 C CZ  . TYR C 1 104 ? 11.07800  24.79900 -22.06400 1.000 35.01622 ? 103 TYR C CZ  1 
ATOM   3076 O OH  . TYR C 1 104 ? 11.14900  23.40900 -22.00700 1.000 36.07215 ? 103 TYR C OH  1 
ATOM   3077 N N   . PHE C 1 105 ? 11.17700  31.71500 -24.39500 1.000 28.21748 ? 104 PHE C N   1 
ATOM   3078 C CA  . PHE C 1 105 ? 10.57800  32.97600 -24.81600 1.000 30.09587 ? 104 PHE C CA  1 
ATOM   3079 C C   . PHE C 1 105 ? 9.16300   32.70800 -25.32600 1.000 35.83351 ? 104 PHE C C   1 
ATOM   3080 O O   . PHE C 1 105 ? 8.97400   31.96300 -26.29900 1.000 29.81172 ? 104 PHE C O   1 
ATOM   3081 C CB  . PHE C 1 105 ? 11.39200  33.65500 -25.93100 1.000 33.14093 ? 104 PHE C CB  1 
ATOM   3082 C CG  . PHE C 1 105 ? 12.77500  34.15300 -25.50600 1.000 32.72970 ? 104 PHE C CG  1 
ATOM   3083 C CD1 . PHE C 1 105 ? 13.11600  34.26600 -24.17800 1.000 26.36853 ? 104 PHE C CD1 1 
ATOM   3084 C CD2 . PHE C 1 105 ? 13.71900  34.50700 -26.46100 1.000 30.63873 ? 104 PHE C CD2 1 
ATOM   3085 C CE1 . PHE C 1 105 ? 14.35400  34.71900 -23.81100 1.000 27.47286 ? 104 PHE C CE1 1 
ATOM   3086 C CE2 . PHE C 1 105 ? 14.97200  34.97000 -26.09400 1.000 33.61466 ? 104 PHE C CE2 1 
ATOM   3087 C CZ  . PHE C 1 105 ? 15.28900  35.07700 -24.77000 1.000 29.83454 ? 104 PHE C CZ  1 
ATOM   3088 N N   . GLY C 1 106 ? 8.18600   33.37500 -24.72800 1.000 30.16076 ? 105 GLY C N   1 
ATOM   3089 C CA  . GLY C 1 106 ? 6.82400   33.34500 -25.22400 1.000 27.40639 ? 105 GLY C CA  1 
ATOM   3090 C C   . GLY C 1 106 ? 6.49100   34.72700 -25.74800 1.000 30.40123 ? 105 GLY C C   1 
ATOM   3091 O O   . GLY C 1 106 ? 6.98900   35.71800 -25.23100 1.000 27.51318 ? 105 GLY C O   1 
ATOM   3092 N N   . GLU C 1 107 ? 5.71400   34.77300 -26.82800 1.000 27.22768 ? 106 GLU C N   1 
ATOM   3093 C CA  . GLU C 1 107 ? 5.43100   36.00500 -27.53900 1.000 29.59120 ? 106 GLU C CA  1 
ATOM   3094 C C   . GLU C 1 107 ? 3.92500   36.23700 -27.57600 1.000 33.09174 ? 106 GLU C C   1 
ATOM   3095 O O   . GLU C 1 107 ? 3.14500   35.30200 -27.82100 1.000 28.29254 ? 106 GLU C O   1 
ATOM   3096 C CB  . GLU C 1 107 ? 5.97500   35.97600 -28.98800 1.000 27.58829 ? 106 GLU C CB  1 
ATOM   3097 C CG  . GLU C 1 107 ? 7.42200   35.66000 -29.11500 1.000 24.44872 ? 106 GLU C CG  1 
ATOM   3098 C CD  . GLU C 1 107 ? 7.80600   35.40900 -30.53900 1.000 29.68629 ? 106 GLU C CD  1 
ATOM   3099 O OE1 . GLU C 1 107 ? 7.66700   34.24900 -30.99400 1.000 29.32885 ? 106 GLU C OE1 1 
ATOM   3100 O OE2 . GLU C 1 107 ? 8.25300   36.37400 -31.21500 1.000 31.40564 ? 106 GLU C OE2 1 
ATOM   3101 N N   . MET C 1 108 ? 3.54200   37.50400 -27.40800 1.000 32.73288 ? 107 MET C N   1 
ATOM   3102 C CA  . MET C 1 108 ? 2.18000   38.02300 -27.43200 1.000 30.10858 ? 107 MET C CA  1 
ATOM   3103 C C   . MET C 1 108 ? 2.09900   39.20500 -28.36400 1.000 31.64538 ? 107 MET C C   1 
ATOM   3104 O O   . MET C 1 108 ? 3.08800   39.92800 -28.54300 1.000 27.05779 ? 107 MET C O   1 
ATOM   3105 C CB  . MET C 1 108 ? 1.78500   38.51800 -26.03900 1.000 29.38832 ? 107 MET C CB  1 
ATOM   3106 C CG  . MET C 1 108 ? 1.27800   37.48800 -25.09000 1.000 35.19979 ? 107 MET C CG  1 
ATOM   3107 S SD  . MET C 1 108 ? 1.99100   37.82100 -23.47000 1.000 38.07359 ? 107 MET C SD  1 
ATOM   3108 C CE  . MET C 1 108 ? 3.72200   37.43000 -23.77400 1.000 30.06593 ? 107 MET C CE  1 
ATOM   3109 N N   . PRO C 1 109 ? 0.92600   39.50800 -28.92900 1.000 33.50919 ? 108 PRO C N   1 
ATOM   3110 C CA  . PRO C 1 109 ? 0.76300   40.78200 -29.64100 1.000 31.08286 ? 108 PRO C CA  1 
ATOM   3111 C C   . PRO C 1 109 ? 0.92100   41.95300 -28.67200 1.000 36.99258 ? 108 PRO C C   1 
ATOM   3112 O O   . PRO C 1 109 ? 0.43200   41.91800 -27.53500 1.000 32.45563 ? 108 PRO C O   1 
ATOM   3113 C CB  . PRO C 1 109 ? -0.65100  40.71400 -30.22900 1.000 29.32776 ? 108 PRO C CB  1 
ATOM   3114 C CG  . PRO C 1 109 ? -1.01400  39.24800 -30.21800 1.000 31.32050 ? 108 PRO C CG  1 
ATOM   3115 C CD  . PRO C 1 109 ? -0.24000  38.61100 -29.08400 1.000 28.42862 ? 108 PRO C CD  1 
ATOM   3116 N N   . ALA C 1 110 ? 1.62400   42.98800 -29.12800 1.000 28.08829 ? 109 ALA C N   1 
ATOM   3117 C CA  . ALA C 1 110 ? 1.83900   44.13600 -28.26900 1.000 29.95164 ? 109 ALA C CA  1 
ATOM   3118 C C   . ALA C 1 110 ? 0.52600   44.74800 -27.79100 1.000 29.75661 ? 109 ALA C C   1 
ATOM   3119 O O   . ALA C 1 110 ? 0.45400   45.23300 -26.65700 1.000 35.49728 ? 109 ALA C O   1 
ATOM   3120 C CB  . ALA C 1 110 ? 2.68100   45.17900 -29.00100 1.000 33.07525 ? 109 ALA C CB  1 
ATOM   3121 N N   . GLN C 1 111 ? -0.53300  44.68900 -28.60800 1.000 33.66860 ? 110 GLN C N   1 
ATOM   3122 C CA  . GLN C 1 111 ? -1.81000  45.31400 -28.26100 1.000 28.86607 ? 110 GLN C CA  1 
ATOM   3123 C C   . GLN C 1 111 ? -2.52900  44.64600 -27.09600 1.000 27.87800 ? 110 GLN C C   1 
ATOM   3124 O O   . GLN C 1 111 ? -3.55300  45.17200 -26.63800 1.000 27.72471 ? 110 GLN C O   1 
ATOM   3125 C CB  . GLN C 1 111 ? -2.74600  45.37300 -29.48300 1.000 22.38905 ? 110 GLN C CB  1 
ATOM   3126 C CG  . GLN C 1 111 ? -2.09800  45.77100 -30.81200 1.000 30.98997 ? 110 GLN C CG  1 
ATOM   3127 C CD  . GLN C 1 111 ? -1.36600  44.61500 -31.52400 1.000 41.49778 ? 110 GLN C CD  1 
ATOM   3128 O OE1 . GLN C 1 111 ? -0.14300  44.60200 -31.63000 1.000 44.57599 ? 110 GLN C OE1 1 
ATOM   3129 N NE2 . GLN C 1 111 ? -2.13600  43.67400 -32.07100 1.000 47.03002 ? 110 GLN C NE2 1 
ATOM   3130 N N   . GLN C 1 112 ? -2.05000  43.51700 -26.60400 1.000 21.62289 ? 111 GLN C N   1 
ATOM   3131 C CA  . GLN C 1 112 ? -2.71500  42.90500 -25.46600 1.000 24.99544 ? 111 GLN C CA  1 
ATOM   3132 C C   . GLN C 1 112 ? -1.77300  42.82800 -24.27600 1.000 24.08257 ? 111 GLN C C   1 
ATOM   3133 O O   . GLN C 1 112 ? -1.89300  41.95500 -23.41700 1.000 28.08918 ? 111 GLN C O   1 
ATOM   3134 C CB  . GLN C 1 112 ? -3.29200  41.53400 -25.83500 1.000 27.15101 ? 111 GLN C CB  1 
ATOM   3135 C CG  . GLN C 1 112 ? -2.30800  40.48000 -26.37900 1.000 27.77857 ? 111 GLN C CG  1 
ATOM   3136 C CD  . GLN C 1 112 ? -2.99700  39.18700 -26.85700 1.000 22.22323 ? 111 GLN C CD  1 
ATOM   3137 O OE1 . GLN C 1 112 ? -3.44500  39.07700 -27.98600 1.000 21.85611 ? 111 GLN C OE1 1 
ATOM   3138 N NE2 . GLN C 1 112 ? -3.07300  38.21100 -25.96700 1.000 22.78688 ? 111 GLN C NE2 1 
ATOM   3139 N N   . MET C 1 113 ? -0.82700  43.74800 -24.23600 1.000 21.97655 ? 112 MET C N   1 
ATOM   3140 C CA  . MET C 1 113 ? 0.19500   43.79600 -23.20500 1.000 28.48866 ? 112 MET C CA  1 
ATOM   3141 C C   . MET C 1 113 ? 0.38400   45.23400 -22.75500 1.000 30.70339 ? 112 MET C C   1 
ATOM   3142 O O   . MET C 1 113 ? 0.58100   46.14500 -23.57300 1.000 23.22701 ? 112 MET C O   1 
ATOM   3143 C CB  . MET C 1 113 ? 1.53600   43.22400 -23.67200 1.000 34.74795 ? 112 MET C CB  1 
ATOM   3144 C CG  . MET C 1 113 ? 1.45500   41.93100 -24.39500 1.000 24.87488 ? 112 MET C CG  1 
ATOM   3145 S SD  . MET C 1 113 ? 2.97400   41.62200 -25.32000 1.000 35.81996 ? 112 MET C SD  1 
ATOM   3146 C CE  . MET C 1 113 ? 4.25000   41.74500 -24.07400 1.000 31.51305 ? 112 MET C CE  1 
ATOM   3147 N N   . VAL C 1 114 ? 0.28100   45.42900 -21.46200 1.000 27.07741 ? 113 VAL C N   1 
ATOM   3148 C CA  . VAL C 1 114 ? 0.42400   46.74500 -20.87000 1.000 32.52569 ? 113 VAL C CA  1 
ATOM   3149 C C   . VAL C 1 114 ? 1.57800   46.69800 -19.89200 1.000 29.96412 ? 113 VAL C C   1 
ATOM   3150 O O   . VAL C 1 114 ? 1.79400   45.65900 -19.25000 1.000 26.18635 ? 113 VAL C O   1 
ATOM   3151 C CB  . VAL C 1 114 ? -0.84500  47.24600 -20.11500 1.000 24.04192 ? 113 VAL C CB  1 
ATOM   3152 C CG1 . VAL C 1 114 ? -2.03800  46.52000 -20.45000 1.000 26.85818 ? 113 VAL C CG1 1 
ATOM   3153 C CG2 . VAL C 1 114 ? -0.60300  47.34000 -18.58800 1.000 23.12454 ? 113 VAL C CG2 1 
ATOM   3154 N N   . ASN C 1 115 ? 2.31500   47.81600 -19.80300 1.000 29.01241 ? 114 ASN C N   1 
ATOM   3155 C CA  . ASN C 1 115 ? 3.02400   47.98700 -18.55400 1.000 33.20702 ? 114 ASN C CA  1 
ATOM   3156 C C   . ASN C 1 115 ? 3.51300   49.41400 -18.36900 1.000 32.18023 ? 114 ASN C C   1 
ATOM   3157 O O   . ASN C 1 115 ? 3.45500   50.25500 -19.27800 1.000 33.83777 ? 114 ASN C O   1 
ATOM   3158 C CB  . ASN C 1 115 ? 3.95700   46.74400 -18.35700 1.000 41.34997 ? 114 ASN C CB  1 
ATOM   3159 C CG  . ASN C 1 115 ? 4.76900   46.35700 -19.64300 1.000 43.75158 ? 114 ASN C CG  1 
ATOM   3160 O OD1 . ASN C 1 115 ? 4.97700   47.11800 -20.49800 1.000 46.22214 ? 114 ASN C OD1 1 
ATOM   3161 N ND2 . ASN C 1 115 ? 5.16600   45.09600 -19.79400 1.000 41.18202 ? 114 ASN C ND2 1 
ATOM   3162 N N   . TYR C 1 116 ? 3.82300   49.67900 -17.09100 1.000 32.03328 ? 115 TYR C N   1 
ATOM   3163 C CA  . TYR C 1 116 ? 3.73400   50.98800 -16.44800 1.000 30.64056 ? 115 TYR C CA  1 
ATOM   3164 C C   . TYR C 1 116 ? 2.35700   51.60000 -16.63900 1.000 35.96805 ? 115 TYR C C   1 
ATOM   3165 O O   . TYR C 1 116 ? 2.19800   52.81300 -16.54000 1.000 39.61182 ? 115 TYR C O   1 
ATOM   3166 C CB  . TYR C 1 116 ? 4.84200   51.91100 -16.93800 1.000 35.03296 ? 115 TYR C CB  1 
ATOM   3167 C CG  . TYR C 1 116 ? 6.20300   51.51200 -16.41000 1.000 35.60086 ? 115 TYR C CG  1 
ATOM   3168 C CD1 . TYR C 1 116 ? 6.51700   51.58900 -15.04900 1.000 37.98975 ? 115 TYR C CD1 1 
ATOM   3169 C CD2 . TYR C 1 116 ? 7.14500   50.99000 -17.27100 1.000 29.93260 ? 115 TYR C CD2 1 
ATOM   3170 C CE1 . TYR C 1 116 ? 7.76800   51.18700 -14.58200 1.000 36.24448 ? 115 TYR C CE1 1 
ATOM   3171 C CE2 . TYR C 1 116 ? 8.37900   50.60400 -16.82200 1.000 34.61717 ? 115 TYR C CE2 1 
ATOM   3172 C CZ  . TYR C 1 116 ? 8.69400   50.70300 -15.47800 1.000 31.35655 ? 115 TYR C CZ  1 
ATOM   3173 O OH  . TYR C 1 116 ? 9.93300   50.30900 -15.02500 1.000 34.39042 ? 115 TYR C OH  1 
ATOM   3174 N N   . GLY C 1 117 ? 1.34400   50.73500 -16.73600 1.000 30.35758 ? 116 GLY C N   1 
ATOM   3175 C CA  . GLY C 1 117 ? -0.02300  51.11500 -16.95000 1.000 27.28526 ? 116 GLY C CA  1 
ATOM   3176 C C   . GLY C 1 117 ? -0.39200  51.44900 -18.37100 1.000 29.02583 ? 116 GLY C C   1 
ATOM   3177 O O   . GLY C 1 117 ? -1.52600  51.86800 -18.59000 1.000 25.99306 ? 116 GLY C O   1 
ATOM   3178 N N   . ARG C 1 118 ? 0.48900   51.21000 -19.35300 1.000 29.29517 ? 117 ARG C N   1 
ATOM   3179 C CA  . ARG C 1 118 ? 0.20600   51.55200 -20.74300 1.000 27.39391 ? 117 ARG C CA  1 
ATOM   3180 C C   . ARG C 1 118 ? 0.44500   50.37800 -21.69300 1.000 27.56339 ? 117 ARG C C   1 
ATOM   3181 O O   . ARG C 1 118 ? 1.31000   49.52800 -21.45700 1.000 25.61742 ? 117 ARG C O   1 
ATOM   3182 C CB  . ARG C 1 118 ? 1.03500   52.74600 -21.23200 1.000 31.33553 ? 117 ARG C CB  1 
ATOM   3183 C CG  . ARG C 1 118 ? 1.15300   53.94600 -20.27600 1.000 38.94794 ? 117 ARG C CG  1 
ATOM   3184 C CD  . ARG C 1 118 ? -0.16400  54.35100 -19.63900 1.000 40.02665 ? 117 ARG C CD  1 
ATOM   3185 N NE  . ARG C 1 118 ? -1.07800  55.00700 -20.56000 1.000 39.79725 ? 117 ARG C NE  1 
ATOM   3186 C CZ  . ARG C 1 118 ? -1.70000  56.15100 -20.31200 1.000 46.85636 ? 117 ARG C CZ  1 
ATOM   3187 N NH1 . ARG C 1 118 ? -1.52300  56.80200 -19.17300 1.000 42.93525 ? 117 ARG C NH1 1 
ATOM   3188 N NH2 . ARG C 1 118 ? -2.50900  56.65900 -21.23500 1.000 49.29950 ? 117 ARG C NH2 1 
ATOM   3189 N N   . PHE C 1 119 ? -0.36500  50.34200 -22.76600 1.000 23.49765 ? 118 PHE C N   1 
ATOM   3190 C CA  . PHE C 1 119 ? -0.20500  49.37300 -23.85400 1.000 28.66659 ? 118 PHE C CA  1 
ATOM   3191 C C   . PHE C 1 119 ? 1.12200   49.58000 -24.58300 1.000 30.12026 ? 118 PHE C C   1 
ATOM   3192 O O   . PHE C 1 119 ? 1.50300   50.70700 -24.91300 1.000 27.35439 ? 118 PHE C O   1 
ATOM   3193 C CB  . PHE C 1 119 ? -1.37600  49.43800 -24.86000 1.000 20.49161 ? 118 PHE C CB  1 
ATOM   3194 C CG  . PHE C 1 119 ? -2.72400  49.12000 -24.26100 1.000 23.82042 ? 118 PHE C CG  1 
ATOM   3195 C CD1 . PHE C 1 119 ? -3.39600  50.04500 -23.47600 1.000 25.07931 ? 118 PHE C CD1 1 
ATOM   3196 C CD2 . PHE C 1 119 ? -3.30400  47.85700 -24.44800 1.000 27.84086 ? 118 PHE C CD2 1 
ATOM   3197 C CE1 . PHE C 1 119 ? -4.64900  49.74300 -22.89400 1.000 25.55630 ? 118 PHE C CE1 1 
ATOM   3198 C CE2 . PHE C 1 119 ? -4.56200  47.53200 -23.87700 1.000 30.37595 ? 118 PHE C CE2 1 
ATOM   3199 C CZ  . PHE C 1 119 ? -5.22900  48.48600 -23.09100 1.000 30.76462 ? 118 PHE C CZ  1 
ATOM   3200 N N   . LEU C 1 120 ? 1.83600   48.47300 -24.79900 1.000 30.07253 ? 119 LEU C N   1 
ATOM   3201 C CA  . LEU C 1 120 ? 3.14500   48.49500 -25.42500 1.000 29.21844 ? 119 LEU C CA  1 
ATOM   3202 C C   . LEU C 1 120 ? 3.02900   48.91200 -26.88400 1.000 30.82320 ? 119 LEU C C   1 
ATOM   3203 O O   . LEU C 1 120 ? 1.95800   48.80000 -27.47600 1.000 31.32997 ? 119 LEU C O   1 
ATOM   3204 C CB  . LEU C 1 120 ? 3.78900   47.11600 -25.29600 1.000 30.56276 ? 119 LEU C CB  1 
ATOM   3205 C CG  . LEU C 1 120 ? 5.03900   47.13500 -24.42700 1.000 31.61971 ? 119 LEU C CG  1 
ATOM   3206 C CD1 . LEU C 1 120 ? 4.76400   48.03700 -23.26100 1.000 36.83386 ? 119 LEU C CD1 1 
ATOM   3207 C CD2 . LEU C 1 120 ? 5.39800   45.75700 -23.94500 1.000 27.82627 ? 119 LEU C CD2 1 
ATOM   3208 N N   . PRO C 1 121 ? 4.11500   49.45700 -27.47700 1.000 36.80728 ? 120 PRO C N   1 
ATOM   3209 C CA  . PRO C 1 121 ? 4.11800   49.73900 -28.92400 1.000 31.66757 ? 120 PRO C CA  1 
ATOM   3210 C C   . PRO C 1 121 ? 4.64900   48.55100 -29.69300 1.000 35.38241 ? 120 PRO C C   1 
ATOM   3211 O O   . PRO C 1 121 ? 4.90700   47.50800 -29.09200 1.000 41.15397 ? 120 PRO C O   1 
ATOM   3212 C CB  . PRO C 1 121 ? 5.05300   50.94700 -29.04100 1.000 27.29233 ? 120 PRO C CB  1 
ATOM   3213 C CG  . PRO C 1 121 ? 6.00700   50.78700 -27.86800 1.000 36.72330 ? 120 PRO C CG  1 
ATOM   3214 C CD  . PRO C 1 121 ? 5.41300   49.80400 -26.87000 1.000 34.41000 ? 120 PRO C CD  1 
ATOM   3215 N N   . GLN C 1 122 ? 4.89400   48.69700 -30.98200 1.000 41.19321 ? 121 GLN C N   1 
ATOM   3216 C CA  . GLN C 1 122 ? 5.56900   47.61000 -31.66800 1.000 39.68825 ? 121 GLN C CA  1 
ATOM   3217 C C   . GLN C 1 122 ? 7.07600   47.68500 -31.46300 1.000 45.66980 ? 121 GLN C C   1 
ATOM   3218 O O   . GLN C 1 122 ? 7.60900   48.72900 -31.07400 1.000 45.64490 ? 121 GLN C O   1 
ATOM   3219 C CB  . GLN C 1 122 ? 5.25800   47.65000 -33.16700 1.000 36.33006 ? 121 GLN C CB  1 
ATOM   3220 C CG  . GLN C 1 122 ? 3.78200   47.71600 -33.49800 1.000 39.79185 ? 121 GLN C CG  1 
ATOM   3221 C CD  . GLN C 1 122 ? 3.07500   46.41400 -33.18400 1.000 42.99310 ? 121 GLN C CD  1 
ATOM   3222 O OE1 . GLN C 1 122 ? 3.72000   45.37300 -33.02700 1.000 44.41646 ? 121 GLN C OE1 1 
ATOM   3223 N NE2 . GLN C 1 122 ? 1.75300   46.47000 -33.04600 1.000 36.03330 ? 121 GLN C NE2 1 
ATOM   3224 N N   . PRO C 1 123 ? 7.77700   46.56000 -31.64000 1.000 41.60242 ? 122 PRO C N   1 
ATOM   3225 C CA  . PRO C 1 123 ? 9.24000   46.59200 -31.50600 1.000 43.78013 ? 122 PRO C CA  1 
ATOM   3226 C C   . PRO C 1 123 ? 9.90000   47.59600 -32.43500 1.000 48.13798 ? 122 PRO C C   1 
ATOM   3227 O O   . PRO C 1 123 ? 10.90100  48.22500 -32.05900 1.000 51.86847 ? 122 PRO C O   1 
ATOM   3228 C CB  . PRO C 1 123 ? 9.66000   45.14800 -31.81500 1.000 40.14154 ? 122 PRO C CB  1 
ATOM   3229 C CG  . PRO C 1 123 ? 8.37400   44.34000 -31.84900 1.000 39.68551 ? 122 PRO C CG  1 
ATOM   3230 C CD  . PRO C 1 123 ? 7.23100   45.20600 -31.48200 1.000 35.75610 ? 122 PRO C CD  1 
ATOM   3231 N N   . GLY C 1 124 ? 9.35600   47.79100 -33.62900 1.000 48.76296 ? 123 GLY C N   1 
ATOM   3232 C CA  . GLY C 1 124 ? 9.76400   48.93200 -34.42800 1.000 67.25247 ? 123 GLY C CA  1 
ATOM   3233 C C   . GLY C 1 124 ? 9.31900   50.27100 -33.85400 1.000 70.41161 ? 123 GLY C C   1 
ATOM   3234 O O   . GLY C 1 124 ? 8.19200   50.71300 -34.13500 1.000 61.34691 ? 123 GLY C O   1 
ATOM   3235 N N   . HIS C 1 125 ? 10.19900  50.88600 -33.03000 1.000 61.05693 ? 124 HIS C N   1 
ATOM   3236 C CA  . HIS C 1 125 ? 10.11000  52.23400 -32.45300 1.000 66.48786 ? 124 HIS C CA  1 
ATOM   3237 C C   . HIS C 1 125 ? 9.57600   52.25700 -31.01100 1.000 59.70852 ? 124 HIS C C   1 
ATOM   3238 O O   . HIS C 1 125 ? 8.38000   52.46300 -30.77900 1.000 53.46814 ? 124 HIS C O   1 
ATOM   3239 C CB  . HIS C 1 125 ? 9.25500   53.19700 -33.31600 1.000 75.81412 ? 124 HIS C CB  1 
ATOM   3240 C CG  . HIS C 1 125 ? 9.78400   53.44200 -34.70800 1.000 80.22690 ? 124 HIS C CG  1 
ATOM   3241 N ND1 . HIS C 1 125 ? 8.95900   53.54900 -35.81100 1.000 78.31784 ? 124 HIS C ND1 1 
ATOM   3242 C CD2 . HIS C 1 125 ? 11.04600  53.62400 -35.17000 1.000 79.17915 ? 124 HIS C CD2 1 
ATOM   3243 C CE1 . HIS C 1 125 ? 9.68900   53.77700 -36.88900 1.000 76.17007 ? 124 HIS C CE1 1 
ATOM   3244 N NE2 . HIS C 1 125 ? 10.95900  53.82400 -36.52900 1.000 79.32566 ? 124 HIS C NE2 1 
ATOM   3245 N N   . GLU C 1 126 ? 10.46700  52.09600 -30.03300 1.000 59.30559 ? 125 GLU C N   1 
ATOM   3246 C CA  . GLU C 1 126 ? 10.20000  52.43300 -28.63200 1.000 51.00091 ? 125 GLU C CA  1 
ATOM   3247 C C   . GLU C 1 126 ? 10.55300  53.88600 -28.26800 1.000 45.72029 ? 125 GLU C C   1 
ATOM   3248 O O   . GLU C 1 126 ? 10.31900  54.29200 -27.13200 1.000 43.12929 ? 125 GLU C O   1 
ATOM   3249 C CB  . GLU C 1 126 ? 10.94500  51.48700 -27.67000 1.000 43.98067 ? 125 GLU C CB  1 
ATOM   3250 C CG  . GLU C 1 126 ? 10.47500  50.01800 -27.59600 1.000 46.25802 ? 125 GLU C CG  1 
ATOM   3251 C CD  . GLU C 1 126 ? 11.02000  49.18200 -28.74800 1.000 45.28526 ? 125 GLU C CD  1 
ATOM   3252 O OE1 . GLU C 1 126 ? 12.23200  49.27700 -29.03800 1.000 48.96228 ? 125 GLU C OE1 1 
ATOM   3253 O OE2 . GLU C 1 126 ? 10.26800  48.38800 -29.32400 1.000 40.25850 ? 125 GLU C OE2 1 
ATOM   3254 N N   . GLY C 1 127 ? 11.14100  54.67700 -29.15600 1.000 51.14233 ? 126 GLY C N   1 
ATOM   3255 C CA  . GLY C 1 127 ? 11.35500  56.08400 -28.82700 1.000 42.67027 ? 126 GLY C CA  1 
ATOM   3256 C C   . GLY C 1 127 ? 10.09000  56.93000 -28.80800 1.000 46.22663 ? 126 GLY C C   1 
ATOM   3257 O O   . GLY C 1 127 ? 9.82300   57.66100 -27.83200 1.000 44.11238 ? 126 GLY C O   1 
ATOM   3258 N N   . GLU C 1 128 ? 9.30900   56.82500 -29.89200 1.000 40.90430 ? 127 GLU C N   1 
ATOM   3259 C CA  . GLU C 1 128 ? 7.99000   57.43500 -30.00600 1.000 44.44339 ? 127 GLU C CA  1 
ATOM   3260 C C   . GLU C 1 128 ? 7.16900   57.26800 -28.74600 1.000 44.92774 ? 127 GLU C C   1 
ATOM   3261 O O   . GLU C 1 128 ? 6.81500   58.25000 -28.07800 1.000 46.89979 ? 127 GLU C O   1 
ATOM   3262 C CB  . GLU C 1 128 ? 7.25200   56.71000 -31.13300 1.000 53.95792 ? 127 GLU C CB  1 
ATOM   3263 C CG  . GLU C 1 128 ? 5.72000   56.75700 -31.13300 1.000 59.45654 ? 127 GLU C CG  1 
ATOM   3264 C CD  . GLU C 1 128 ? 5.13600   55.41500 -31.59700 1.000 69.92660 ? 127 GLU C CD  1 
ATOM   3265 O OE1 . GLU C 1 128 ? 5.91500   54.58800 -32.14200 1.000 74.27651 ? 127 GLU C OE1 1 
ATOM   3266 O OE2 . GLU C 1 128 ? 3.91500   55.15300 -31.38700 1.000 69.99124 ? 127 GLU C OE2 1 
ATOM   3267 N N   . TRP C 1 129 ? 6.93800   56.00400 -28.39900 1.000 44.25948 ? 128 TRP C N   1 
ATOM   3268 C CA  . TRP C 1 129 ? 6.06800   55.67900 -27.28300 1.000 44.23598 ? 128 TRP C CA  1 
ATOM   3269 C C   . TRP C 1 129 ? 6.52900   56.39700 -26.01900 1.000 41.62717 ? 128 TRP C C   1 
ATOM   3270 O O   . TRP C 1 129 ? 5.72000   57.02300 -25.32900 1.000 43.74574 ? 128 TRP C O   1 
ATOM   3271 C CB  . TRP C 1 129 ? 5.99300   54.15500 -27.13800 1.000 35.37459 ? 128 TRP C CB  1 
ATOM   3272 C CG  . TRP C 1 129 ? 5.21600   53.60100 -26.01200 1.000 38.90565 ? 128 TRP C CG  1 
ATOM   3273 C CD1 . TRP C 1 129 ? 3.87800   53.41600 -25.95300 1.000 39.17769 ? 128 TRP C CD1 1 
ATOM   3274 C CD2 . TRP C 1 129 ? 5.74500   53.12800 -24.76600 1.000 39.94387 ? 128 TRP C CD2 1 
ATOM   3275 N NE1 . TRP C 1 129 ? 3.53100   52.86800 -24.74100 1.000 39.35070 ? 128 TRP C NE1 1 
ATOM   3276 C CE2 . TRP C 1 129 ? 4.66200   52.68300 -23.99700 1.000 33.73604 ? 128 TRP C CE2 1 
ATOM   3277 C CE3 . TRP C 1 129 ? 7.02600   53.04600 -24.22900 1.000 34.76352 ? 128 TRP C CE3 1 
ATOM   3278 C CZ2 . TRP C 1 129 ? 4.81900   52.15200 -22.73500 1.000 36.02123 ? 128 TRP C CZ2 1 
ATOM   3279 C CZ3 . TRP C 1 129 ? 7.18400   52.52500 -22.98000 1.000 43.91251 ? 128 TRP C CZ3 1 
ATOM   3280 C CH2 . TRP C 1 129 ? 6.09000   52.08400 -22.24000 1.000 45.28918 ? 128 TRP C CH2 1 
ATOM   3281 N N   . PHE C 1 130 ? 7.83900   56.35900 -25.73100 1.000 39.53323 ? 129 PHE C N   1 
ATOM   3282 C CA  . PHE C 1 130 ? 8.34900   56.98700 -24.51500 1.000 39.64606 ? 129 PHE C CA  1 
ATOM   3283 C C   . PHE C 1 130 ? 8.06500   58.48100 -24.52100 1.000 42.15048 ? 129 PHE C C   1 
ATOM   3284 O O   . PHE C 1 130 ? 7.47100   59.01200 -23.57500 1.000 42.06541 ? 129 PHE C O   1 
ATOM   3285 C CB  . PHE C 1 130 ? 9.85000   56.71600 -24.32000 1.000 34.38845 ? 129 PHE C CB  1 
ATOM   3286 C CG  . PHE C 1 130 ? 10.44400  57.41700 -23.08600 1.000 41.58507 ? 129 PHE C CG  1 
ATOM   3287 C CD1 . PHE C 1 130 ? 10.21300  56.91700 -21.81000 1.000 42.97383 ? 129 PHE C CD1 1 
ATOM   3288 C CD2 . PHE C 1 130 ? 11.14100  58.61300 -23.18900 1.000 34.37783 ? 129 PHE C CD2 1 
ATOM   3289 C CE1 . PHE C 1 130 ? 10.70700  57.56100 -20.66700 1.000 38.22608 ? 129 PHE C CE1 1 
ATOM   3290 C CE2 . PHE C 1 130 ? 11.64100  59.24500 -22.05600 1.000 34.33551 ? 129 PHE C CE2 1 
ATOM   3291 C CZ  . PHE C 1 130 ? 11.41100  58.71900 -20.79700 1.000 39.65295 ? 129 PHE C CZ  1 
ATOM   3292 N N   . ASP C 1 131 ? 8.46500   59.17400 -25.58900 1.000 40.38135 ? 130 ASP C N   1 
ATOM   3293 C CA  . ASP C 1 131 ? 8.28900   60.62300 -25.62800 1.000 47.78792 ? 130 ASP C CA  1 
ATOM   3294 C C   . ASP C 1 131 ? 6.82200   61.03400 -25.57300 1.000 47.45780 ? 130 ASP C C   1 
ATOM   3295 O O   . ASP C 1 131 ? 6.50800   62.12600 -25.08400 1.000 45.41707 ? 130 ASP C O   1 
ATOM   3296 C CB  . ASP C 1 131 ? 8.94700   61.20600 -26.88000 1.000 39.80258 ? 130 ASP C CB  1 
ATOM   3297 C CG  . ASP C 1 131 ? 10.39200  60.78700 -27.01200 1.000 49.60408 ? 130 ASP C CG  1 
ATOM   3298 O OD1 . ASP C 1 131 ? 11.05200  60.70700 -25.94600 1.000 49.30452 ? 130 ASP C OD1 1 
ATOM   3299 O OD2 . ASP C 1 131 ? 10.87200  60.55800 -28.15800 1.000 45.03178 ? 130 ASP C OD2 1 
ATOM   3300 N N   . ASN C 1 132 ? 5.92600   60.19100 -26.06600 1.000 47.64151 ? 131 ASN C N   1 
ATOM   3301 C CA  . ASN C 1 132 ? 4.49700   60.43100 -26.01700 1.000 41.19407 ? 131 ASN C CA  1 
ATOM   3302 C C   . ASN C 1 132 ? 3.82000   59.99300 -24.73400 1.000 42.35767 ? 131 ASN C C   1 
ATOM   3303 O O   . ASN C 1 132 ? 2.60300   60.15800 -24.62200 1.000 51.41380 ? 131 ASN C O   1 
ATOM   3304 C CB  . ASN C 1 132 ? 3.83000   59.68200 -27.15300 1.000 38.45290 ? 131 ASN C CB  1 
ATOM   3305 C CG  . ASN C 1 132 ? 3.77900   60.47400 -28.38500 1.000 45.95055 ? 131 ASN C CG  1 
ATOM   3306 O OD1 . ASN C 1 132 ? 4.32700   61.56900 -28.44800 1.000 49.70058 ? 131 ASN C OD1 1 
ATOM   3307 N ND2 . ASN C 1 132 ? 3.08700   59.95700 -29.38600 1.000 63.02159 ? 131 ASN C ND2 1 
ATOM   3308 N N   . LEU C 1 133 ? 4.52900   59.45400 -23.76600 1.000 38.37089 ? 132 LEU C N   1 
ATOM   3309 C CA  . LEU C 1 133 ? 3.81200   59.16500 -22.53600 1.000 45.74411 ? 132 LEU C CA  1 
ATOM   3310 C C   . LEU C 1 133 ? 3.72800   60.37600 -21.61700 1.000 45.32336 ? 132 LEU C C   1 
ATOM   3311 O O   . LEU C 1 133 ? 4.43200   61.38600 -21.77700 1.000 38.76395 ? 132 LEU C O   1 
ATOM   3312 C CB  . LEU C 1 133 ? 4.44200   57.98600 -21.78900 1.000 40.50830 ? 132 LEU C CB  1 
ATOM   3313 C CG  . LEU C 1 133 ? 4.38900   56.62000 -22.47800 1.000 44.70255 ? 132 LEU C CG  1 
ATOM   3314 C CD1 . LEU C 1 133 ? 4.79600   55.53000 -21.50000 1.000 40.75939 ? 132 LEU C CD1 1 
ATOM   3315 C CD2 . LEU C 1 133 ? 2.98100   56.33200 -23.06700 1.000 37.68471 ? 132 LEU C CD2 1 
ATOM   3316 N N   . SER C 1 134 ? 2.82900   60.24000 -20.63600 1.000 44.57178 ? 133 SER C N   1 
ATOM   3317 C CA  . SER C 1 134 ? 2.55900   61.25200 -19.62700 1.000 45.35037 ? 133 SER C CA  1 
ATOM   3318 C C   . SER C 1 134 ? 3.87200   61.68600 -18.98400 1.000 50.08087 ? 133 SER C C   1 
ATOM   3319 O O   . SER C 1 134 ? 4.86400   60.94700 -18.98600 1.000 46.73662 ? 133 SER C O   1 
ATOM   3320 C CB  . SER C 1 134 ? 1.58600   60.68500 -18.58700 1.000 42.10126 ? 133 SER C CB  1 
ATOM   3321 O OG  . SER C 1 134 ? 1.76000   61.26400 -17.31300 1.000 52.34351 ? 133 SER C OG  1 
ATOM   3322 N N   . SER C 1 135 ? 3.91300   62.90000 -18.46600 1.000 47.55116 ? 134 SER C N   1 
ATOM   3323 C CA  . SER C 1 135 ? 5.17900   63.38100 -17.94200 1.000 49.33639 ? 134 SER C CA  1 
ATOM   3324 C C   . SER C 1 135 ? 5.50800   62.71000 -16.60400 1.000 48.02448 ? 134 SER C C   1 
ATOM   3325 O O   . SER C 1 135 ? 6.66300   62.33100 -16.35400 1.000 44.52384 ? 134 SER C O   1 
ATOM   3326 C CB  . SER C 1 135 ? 5.09100   64.89400 -17.83900 1.000 49.65197 ? 134 SER C CB  1 
ATOM   3327 O OG  . SER C 1 135 ? 6.31500   65.51500 -18.13100 1.000 54.80011 ? 134 SER C OG  1 
ATOM   3328 N N   . ASP C 1 136 ? 4.49100   62.50900 -15.75200 1.000 48.75011 ? 135 ASP C N   1 
ATOM   3329 C CA  . ASP C 1 136 ? 4.68100   61.79700 -14.49000 1.000 54.29161 ? 135 ASP C CA  1 
ATOM   3330 C C   . ASP C 1 136 ? 5.12300   60.35700 -14.74000 1.000 48.73186 ? 135 ASP C C   1 
ATOM   3331 O O   . ASP C 1 136 ? 5.95600   59.81500 -13.99600 1.000 35.40047 ? 135 ASP C O   1 
ATOM   3332 C CB  . ASP C 1 136 ? 3.39600   61.85000 -13.65800 1.000 51.64515 ? 135 ASP C CB  1 
ATOM   3333 C CG  . ASP C 1 136 ? 2.80100   63.26100 -13.58900 1.000 68.58535 ? 135 ASP C CG  1 
ATOM   3334 O OD1 . ASP C 1 136 ? 3.44100   64.19100 -14.12400 1.000 63.02027 ? 135 ASP C OD1 1 
ATOM   3335 O OD2 . ASP C 1 136 ? 1.70400   63.44900 -13.00700 1.000 66.93586 ? 135 ASP C OD2 1 
ATOM   3336 N N   . GLU C 1 137 ? 4.63100   59.75900 -15.82900 1.000 41.89022 ? 136 GLU C N   1 
ATOM   3337 C CA  . GLU C 1 137 ? 4.95900   58.37800 -16.14100 1.000 42.20832 ? 136 GLU C CA  1 
ATOM   3338 C C   . GLU C 1 137 ? 6.37300   58.27600 -16.70600 1.000 40.29421 ? 136 GLU C C   1 
ATOM   3339 O O   . GLU C 1 137 ? 7.14700   57.41000 -16.29000 1.000 30.46100 ? 136 GLU C O   1 
ATOM   3340 C CB  . GLU C 1 137 ? 3.93300   57.82000 -17.13700 1.000 43.91566 ? 136 GLU C CB  1 
ATOM   3341 C CG  . GLU C 1 137 ? 2.54700   57.57100 -16.54800 1.000 41.72142 ? 136 GLU C CG  1 
ATOM   3342 C CD  . GLU C 1 137 ? 1.43000   57.38900 -17.60300 1.000 50.61060 ? 136 GLU C CD  1 
ATOM   3343 O OE1 . GLU C 1 137 ? 1.64400   57.65200 -18.81400 1.000 48.86771 ? 136 GLU C OE1 1 
ATOM   3344 O OE2 . GLU C 1 137 ? 0.31300   56.98800 -17.21200 1.000 51.63212 ? 136 GLU C OE2 1 
ATOM   3345 N N   . ARG C 1 138 ? 6.72400   59.16500 -17.63900 1.000 41.35470 ? 137 ARG C N   1 
ATOM   3346 C CA  . ARG C 1 138 ? 8.09500   59.24400 -18.12100 1.000 38.53334 ? 137 ARG C CA  1 
ATOM   3347 C C   . ARG C 1 138 ? 9.07300   59.38100 -16.96400 1.000 42.13822 ? 137 ARG C C   1 
ATOM   3348 O O   . ARG C 1 138 ? 10.12700  58.73500 -16.95800 1.000 36.09181 ? 137 ARG C O   1 
ATOM   3349 C CB  . ARG C 1 138 ? 8.24600   60.40400 -19.10400 1.000 42.35806 ? 137 ARG C CB  1 
ATOM   3350 C CG  . ARG C 1 138 ? 8.11700   59.96000 -20.54000 1.000 41.51692 ? 137 ARG C CG  1 
ATOM   3351 C CD  . ARG C 1 138 ? 8.62300   60.99200 -21.51100 1.000 38.31992 ? 137 ARG C CD  1 
ATOM   3352 N NE  . ARG C 1 138 ? 8.75700   62.32000 -20.94200 1.000 35.54919 ? 137 ARG C NE  1 
ATOM   3353 C CZ  . ARG C 1 138 ? 7.80000   63.23300 -20.92800 1.000 36.06229 ? 137 ARG C CZ  1 
ATOM   3354 N NH1 . ARG C 1 138 ? 6.60200   62.98400 -21.42800 1.000 40.20616 ? 137 ARG C NH1 1 
ATOM   3355 N NH2 . ARG C 1 138 ? 8.06200   64.43700 -20.43000 1.000 39.61719 ? 137 ARG C NH2 1 
ATOM   3356 N N   . ALA C 1 139 ? 8.74600   60.22700 -15.97700 1.000 43.78395 ? 138 ALA C N   1 
ATOM   3357 C CA  . ALA C 1 139 ? 9.66400   60.44100 -14.86200 1.000 37.29613 ? 138 ALA C CA  1 
ATOM   3358 C C   . ALA C 1 139 ? 9.73900   59.22400 -13.94300 1.000 37.71723 ? 138 ALA C C   1 
ATOM   3359 O O   . ALA C 1 139 ? 10.83200  58.85500 -13.47800 1.000 39.04476 ? 138 ALA C O   1 
ATOM   3360 C CB  . ALA C 1 139 ? 9.23200   61.68000 -14.08200 1.000 42.15887 ? 138 ALA C CB  1 
ATOM   3361 N N   . PHE C 1 140 ? 8.61100   58.52900 -13.73500 1.000 37.87777 ? 139 PHE C N   1 
ATOM   3362 C CA  . PHE C 1 140 ? 8.67800   57.30400 -12.94100 1.000 35.81675 ? 139 PHE C CA  1 
ATOM   3363 C C   . PHE C 1 140 ? 9.49000   56.22100 -13.64900 1.000 39.04239 ? 139 PHE C C   1 
ATOM   3364 O O   . PHE C 1 140 ? 10.33100  55.56800 -13.02300 1.000 41.32853 ? 139 PHE C O   1 
ATOM   3365 C CB  . PHE C 1 140 ? 7.27800   56.77300 -12.61800 1.000 34.25424 ? 139 PHE C CB  1 
ATOM   3366 C CG  . PHE C 1 140 ? 7.30000   55.50000 -11.80300 1.000 44.60204 ? 139 PHE C CG  1 
ATOM   3367 C CD1 . PHE C 1 140 ? 8.01600   55.43900 -10.61200 1.000 39.49156 ? 139 PHE C CD1 1 
ATOM   3368 C CD2 . PHE C 1 140 ? 6.65600   54.35100 -12.24800 1.000 44.14842 ? 139 PHE C CD2 1 
ATOM   3369 C CE1 . PHE C 1 140 ? 8.06700   54.27000 -9.86900  1.000 45.55034 ? 139 PHE C CE1 1 
ATOM   3370 C CE2 . PHE C 1 140 ? 6.68900   53.17000 -11.50000 1.000 40.88610 ? 139 PHE C CE2 1 
ATOM   3371 C CZ  . PHE C 1 140 ? 7.40000   53.12600 -10.31900 1.000 46.02778 ? 139 PHE C CZ  1 
ATOM   3372 N N   . MET C 1 141 ? 9.32600   56.07800 -14.96600 1.000 36.20021 ? 140 MET C N   1 
ATOM   3373 C CA  . MET C 1 141 ? 10.12600  55.09900 -15.70400 1.000 43.08152 ? 140 MET C CA  1 
ATOM   3374 C C   . MET C 1 141 ? 11.60200  55.46400 -15.67100 1.000 39.63244 ? 140 MET C C   1 
ATOM   3375 O O   . MET C 1 141 ? 12.46600  54.58700 -15.53300 1.000 34.88284 ? 140 MET C O   1 
ATOM   3376 C CB  . MET C 1 141 ? 9.62800   54.96600 -17.15100 1.000 38.36267 ? 140 MET C CB  1 
ATOM   3377 C CG  . MET C 1 141 ? 8.16900   54.52200 -17.25700 1.000 32.59489 ? 140 MET C CG  1 
ATOM   3378 S SD  . MET C 1 141 ? 7.56600   54.39000 -18.95000 1.000 41.27241 ? 140 MET C SD  1 
ATOM   3379 C CE  . MET C 1 141 ? 7.84500   56.01100 -19.61500 1.000 44.34816 ? 140 MET C CE  1 
ATOM   3380 N N   . GLU C 1 142 ? 11.89900  56.76000 -15.80600 1.000 44.89036 ? 141 GLU C N   1 
ATOM   3381 C CA  . GLU C 1 142 ? 13.27100  57.24500 -15.75100 1.000 47.96242 ? 141 GLU C CA  1 
ATOM   3382 C C   . GLU C 1 142 ? 13.92600  56.94300 -14.40500 1.000 42.49285 ? 141 GLU C C   1 
ATOM   3383 O O   . GLU C 1 142 ? 15.14900  56.83300 -14.33900 1.000 44.16714 ? 141 GLU C O   1 
ATOM   3384 C CB  . GLU C 1 142 ? 13.31200  58.72400 -16.08300 1.000 44.20361 ? 141 GLU C CB  1 
ATOM   3385 C CG  . GLU C 1 142 ? 13.55400  58.98000 -17.57200 1.000 46.21614 ? 141 GLU C CG  1 
ATOM   3386 C CD  . GLU C 1 142 ? 13.14800  60.39700 -17.89500 1.000 44.24878 ? 141 GLU C CD  1 
ATOM   3387 O OE1 . GLU C 1 142 ? 13.09100  61.13600 -16.91100 1.000 43.94727 ? 141 GLU C OE1 1 
ATOM   3388 O OE2 . GLU C 1 142 ? 12.94600  60.79500 -19.06500 1.000 50.73985 ? 141 GLU C OE2 1 
ATOM   3389 N N   . THR C 1 143 ? 13.14500  56.79500 -13.32600 1.000 44.28045 ? 142 THR C N   1 
ATOM   3390 C CA  . THR C 1 143 ? 13.77000  56.40900 -12.05000 1.000 48.57629 ? 142 THR C CA  1 
ATOM   3391 C C   . THR C 1 143 ? 14.31200  54.95900 -12.04900 1.000 48.26750 ? 142 THR C C   1 
ATOM   3392 O O   . THR C 1 143 ? 15.28600  54.67200 -11.34500 1.000 44.92069 ? 142 THR C O   1 
ATOM   3393 C CB  . THR C 1 143 ? 12.75800  56.50800 -10.91100 1.000 47.31259 ? 142 THR C CB  1 
ATOM   3394 O OG1 . THR C 1 143 ? 11.57500  55.79400 -11.29700 1.000 46.58251 ? 142 THR C OG1 1 
ATOM   3395 C CG2 . THR C 1 143 ? 12.39900  57.98000 -10.58700 1.000 37.13997 ? 142 THR C CG2 1 
ATOM   3396 N N   . ASN C 1 144 ? 13.67900  54.02500 -12.76500 1.000 49.20419 ? 143 ASN C N   1 
ATOM   3397 C CA  . ASN C 1 144 ? 14.07800  52.60600 -12.78500 1.000 46.42509 ? 143 ASN C CA  1 
ATOM   3398 C C   . ASN C 1 144 ? 15.15300  52.27900 -13.82300 1.000 47.09040 ? 143 ASN C C   1 
ATOM   3399 O O   . ASN C 1 144 ? 15.05300  51.29800 -14.56900 1.000 42.25538 ? 143 ASN C O   1 
ATOM   3400 C CB  . ASN C 1 144 ? 12.84500  51.74600 -13.00600 1.000 38.26712 ? 143 ASN C CB  1 
ATOM   3401 C CG  . ASN C 1 144 ? 11.91500  51.80200 -11.84000 1.000 40.76178 ? 143 ASN C CG  1 
ATOM   3402 O OD1 . ASN C 1 144 ? 12.36200  51.77500 -10.70200 1.000 44.41005 ? 143 ASN C OD1 1 
ATOM   3403 N ND2 . ASN C 1 144 ? 10.61700  51.94800 -12.10300 1.000 44.12200 ? 143 ASN C ND2 1 
ATOM   3404 N N   . VAL C 1 145 ? 16.24100  53.03100 -13.83000 1.000 45.12012 ? 144 VAL C N   1 
ATOM   3405 C CA  . VAL C 1 145 ? 17.29500  52.83000 -14.81000 1.000 46.55770 ? 144 VAL C CA  1 
ATOM   3406 C C   . VAL C 1 145 ? 18.61200  52.88700 -14.05500 1.000 50.37399 ? 144 VAL C C   1 
ATOM   3407 O O   . VAL C 1 145 ? 18.76700  53.65400 -13.10100 1.000 51.83673 ? 144 VAL C O   1 
ATOM   3408 C CB  . VAL C 1 145 ? 17.24100  53.87300 -15.95300 1.000 47.26564 ? 144 VAL C CB  1 
ATOM   3409 C CG1 . VAL C 1 145 ? 18.61200  54.02500 -16.61800 1.000 48.77750 ? 144 VAL C CG1 1 
ATOM   3410 C CG2 . VAL C 1 145 ? 16.16000  53.49400 -16.96300 1.000 47.05909 ? 144 VAL C CG2 1 
ATOM   3411 N N   . ASP C 1 146 ? 19.52800  52.00700 -14.42200 1.000 47.86450 ? 145 ASP C N   1 
ATOM   3412 C CA  . ASP C 1 146 ? 20.71400  51.80400 -13.62500 1.000 49.50174 ? 145 ASP C CA  1 
ATOM   3413 C C   . ASP C 1 146 ? 21.93300  51.47100 -14.51400 1.000 54.25936 ? 145 ASP C C   1 
ATOM   3414 O O   . ASP C 1 146 ? 22.47000  52.34000 -15.21700 1.000 50.17980 ? 145 ASP C O   1 
ATOM   3415 C CB  . ASP C 1 146 ? 20.37600  50.70000 -12.61300 1.000 47.22132 ? 145 ASP C CB  1 
ATOM   3416 C CG  . ASP C 1 146 ? 21.57700  49.95800 -12.11100 1.000 48.10663 ? 145 ASP C CG  1 
ATOM   3417 O OD1 . ASP C 1 146 ? 21.93400  48.96500 -12.77700 1.000 45.45781 ? 145 ASP C OD1 1 
ATOM   3418 O OD2 . ASP C 1 146 ? 22.08400  50.29000 -11.01800 1.000 46.63221 ? 145 ASP C OD2 1 
HETATM 3419 S S   . SO4 D 2 .   ? 8.32800   19.57500 -25.29500 1.000 40.66083 ? 201 SO4 A S   1 
HETATM 3420 O O1  . SO4 D 2 .   ? 9.41500   20.41500 -25.17900 1.000 49.32434 ? 201 SO4 A O1  1 
HETATM 3421 O O2  . SO4 D 2 .   ? 7.52500   19.96400 -26.35100 1.000 34.34650 ? 201 SO4 A O2  1 
HETATM 3422 O O3  . SO4 D 2 .   ? 9.08900   18.42500 -25.37900 1.000 44.52745 ? 201 SO4 A O3  1 
HETATM 3423 O O4  . SO4 D 2 .   ? 7.63200   19.74700 -24.09600 1.000 39.12153 ? 201 SO4 A O4  1 
HETATM 3424 S S   . SO4 E 2 .   ? -10.98500 32.51600 -20.99000 1.000 39.51374 ? 201 SO4 B S   1 
HETATM 3425 O O1  . SO4 E 2 .   ? -10.44800 32.72000 -22.24700 1.000 35.57945 ? 201 SO4 B O1  1 
HETATM 3426 O O2  . SO4 E 2 .   ? -12.24600 33.04800 -20.77700 1.000 38.08814 ? 201 SO4 B O2  1 
HETATM 3427 O O3  . SO4 E 2 .   ? -11.13200 31.16400 -20.90200 1.000 45.60115 ? 201 SO4 B O3  1 
HETATM 3428 O O4  . SO4 E 2 .   ? -10.15000 32.94100 -19.93800 1.000 41.11201 ? 201 SO4 B O4  1 
HETATM 3429 S S   . SO4 F 2 .   ? 9.75400   43.08900 -25.19400 1.000 35.37649 ? 201 SO4 C S   1 
HETATM 3430 O O1  . SO4 F 2 .   ? 9.76700   42.59100 -26.46700 1.000 37.01500 ? 201 SO4 C O1  1 
HETATM 3431 O O2  . SO4 F 2 .   ? 8.92200   44.18600 -25.33700 1.000 41.88961 ? 201 SO4 C O2  1 
HETATM 3432 O O3  . SO4 F 2 .   ? 9.13300   42.19900 -24.38000 1.000 36.02564 ? 201 SO4 C O3  1 
HETATM 3433 O O4  . SO4 F 2 .   ? 11.05000  43.41300 -24.77500 1.000 40.11981 ? 201 SO4 C O4  1 
HETATM 3434 O O   . HOH G 3 .   ? 13.38900  14.39200 -37.40300 1.000 52.86191 ? 301 HOH A O   1 
HETATM 3435 O O   . HOH G 3 .   ? 17.57200  14.42400 -39.44100 1.000 44.98939 ? 302 HOH A O   1 
HETATM 3436 O O   . HOH G 3 .   ? 3.37000   21.45400 -29.52500 1.000 29.32643 ? 303 HOH A O   1 
HETATM 3437 O O   . HOH G 3 .   ? -11.37300 23.49200 -9.27900  1.000 34.09559 ? 304 HOH A O   1 
HETATM 3438 O O   . HOH G 3 .   ? 11.64800  12.75400 -32.63100 1.000 62.64108 ? 305 HOH A O   1 
HETATM 3439 O O   . HOH G 3 .   ? -0.70800  27.60200 3.18200   1.000 36.42165 ? 306 HOH A O   1 
HETATM 3440 O O   . HOH G 3 .   ? 15.97700  7.34000  -10.16000 1.000 42.38077 ? 307 HOH A O   1 
HETATM 3441 O O   . HOH G 3 .   ? -11.63900 15.85200 -18.93900 1.000 42.96601 ? 308 HOH A O   1 
HETATM 3442 O O   . HOH G 3 .   ? 4.91000   16.75000 -34.61400 1.000 27.78491 ? 309 HOH A O   1 
HETATM 3443 O O   . HOH G 3 .   ? 27.87200  11.35900 -21.69600 1.000 41.30121 ? 310 HOH A O   1 
HETATM 3444 O O   . HOH G 3 .   ? 1.90000   8.92400  -15.32100 1.000 27.65831 ? 311 HOH A O   1 
HETATM 3445 O O   . HOH G 3 .   ? -6.60200  11.41500 -34.65900 1.000 43.38576 ? 312 HOH A O   1 
HETATM 3446 O O   . HOH G 3 .   ? 10.86000  28.64000 -8.03000  1.000 30.31855 ? 313 HOH A O   1 
HETATM 3447 O O   . HOH G 3 .   ? -2.65100  28.58800 -2.94500  1.000 38.63539 ? 314 HOH A O   1 
HETATM 3448 O O   . HOH G 3 .   ? 1.05400   23.19500 -32.74700 1.000 28.67240 ? 315 HOH A O   1 
HETATM 3449 O O   . HOH G 3 .   ? -0.70100  27.92000 -28.56100 1.000 30.61467 ? 316 HOH A O   1 
HETATM 3450 O O   . HOH G 3 .   ? 0.10400   28.55300 -5.75000  1.000 37.61940 ? 317 HOH A O   1 
HETATM 3451 O O   . HOH G 3 .   ? -7.220    17.525   -33.409   1.000 38.27276 ? 318 HOH A O   1 
HETATM 3452 O O   . HOH G 3 .   ? 5.68300   15.19400 -32.18000 1.000 39.19406 ? 319 HOH A O   1 
HETATM 3453 O O   . HOH H 3 .   ? 8.03100   49.76600 -7.11500  1.000 40.60173 ? 301 HOH B O   1 
HETATM 3454 O O   . HOH H 3 .   ? -21.76600 21.61700 -27.99000 1.000 35.56767 ? 302 HOH B O   1 
HETATM 3455 O O   . HOH H 3 .   ? 5.57000   49.94900 -12.47100 1.000 38.56294 ? 303 HOH B O   1 
HETATM 3456 O O   . HOH H 3 .   ? -25.03800 26.83800 -19.43600 1.000 58.60191 ? 304 HOH B O   1 
HETATM 3457 O O   . HOH H 3 .   ? 2.01500   46.10500 2.28200   1.000 39.66124 ? 305 HOH B O   1 
HETATM 3458 O O   . HOH H 3 .   ? 5.46700   43.48100 -6.25100  1.000 33.65210 ? 306 HOH B O   1 
HETATM 3459 O O   . HOH H 3 .   ? -15.86900 45.19200 -13.85300 1.000 35.74786 ? 307 HOH B O   1 
HETATM 3460 O O   . HOH H 3 .   ? -8.63100  35.50300 -27.14700 1.000 23.53524 ? 308 HOH B O   1 
HETATM 3461 O O   . HOH H 3 .   ? -3.00800  50.12200 -1.03800  1.000 33.44935 ? 309 HOH B O   1 
HETATM 3462 O O   . HOH H 3 .   ? 0.54500   40.42300 -0.67900  1.000 29.80216 ? 310 HOH B O   1 
HETATM 3463 O O   . HOH H 3 .   ? 3.35100   43.91900 -4.72800  1.000 32.08275 ? 311 HOH B O   1 
HETATM 3464 O O   . HOH H 3 .   ? -3.35300  45.74000 0.89900   1.000 29.08779 ? 312 HOH B O   1 
HETATM 3465 O O   . HOH H 3 .   ? 19.99500  45.77600 -5.25400  1.000 41.94157 ? 313 HOH B O   1 
HETATM 3466 O O   . HOH H 3 .   ? 1.88500   34.63400 -22.24600 1.000 21.15975 ? 314 HOH B O   1 
HETATM 3467 O O   . HOH H 3 .   ? -19.87400 19.70800 -21.38000 1.000 50.23804 ? 315 HOH B O   1 
HETATM 3468 O O   . HOH H 3 .   ? 7.70000   49.09000 -5.30000  1.000 47.04206 ? 316 HOH B O   1 
HETATM 3469 O O   . HOH H 3 .   ? -15.37900 42.03900 -29.80100 1.000 37.16241 ? 317 HOH B O   1 
HETATM 3470 O O   . HOH H 3 .   ? -6.80400  38.99800 -32.12800 1.000 24.74434 ? 318 HOH B O   1 
HETATM 3471 O O   . HOH H 3 .   ? 5.65500   41.12200 -8.09400  1.000 27.01213 ? 319 HOH B O   1 
HETATM 3472 O O   . HOH H 3 .   ? -7.87800  35.42300 -31.23800 1.000 26.89723 ? 320 HOH B O   1 
HETATM 3473 O O   . HOH H 3 .   ? 7.49200   39.64400 -6.19600  1.000 31.67098 ? 321 HOH B O   1 
HETATM 3474 O O   . HOH I 3 .   ? 8.63600   53.82300 -26.31300 1.000 42.22939 ? 301 HOH C O   1 
HETATM 3475 O O   . HOH I 3 .   ? 8.34400   45.10200 -22.33900 1.000 30.42715 ? 302 HOH C O   1 
HETATM 3476 O O   . HOH I 3 .   ? 8.54400   28.89500 -2.47600  1.000 37.30869 ? 303 HOH C O   1 
HETATM 3477 O O   . HOH I 3 .   ? 2.92100   42.56600 -31.15900 1.000 31.76319 ? 304 HOH C O   1 
HETATM 3478 O O   . HOH I 3 .   ? 18.87100  21.84600 -15.61000 1.000 33.21399 ? 305 HOH C O   1 
HETATM 3479 O O   . HOH I 3 .   ? 6.57700   51.78500 -32.59600 1.000 45.82906 ? 306 HOH C O   1 
HETATM 3480 O O   . HOH I 3 .   ? 26.18400  25.86100 -8.94500  1.000 47.13139 ? 307 HOH C O   1 
HETATM 3481 O O   . HOH I 3 .   ? 14.70100  22.27200 -6.15900  1.000 35.49739 ? 308 HOH C O   1 
HETATM 3482 O O   . HOH I 3 .   ? 24.28700  51.89100 -16.93800 1.000 34.65217 ? 309 HOH C O   1 
HETATM 3483 O O   . HOH I 3 .   ? 30.86300  34.12900 -12.46300 1.000 41.52844 ? 310 HOH C O   1 
HETATM 3484 O O   . HOH I 3 .   ? 28.72900  27.65100 -17.66700 1.000 45.61870 ? 311 HOH C O   1 
HETATM 3485 O O   . HOH I 3 .   ? 23.53100  34.99800 -35.64000 1.000 27.28514 ? 312 HOH C O   1 
HETATM 3486 O O   . HOH I 3 .   ? 15.67600  44.60100 -14.71700 1.000 38.94507 ? 313 HOH C O   1 
HETATM 3487 O O   . HOH I 3 .   ? -0.166    58.164   -21.344   1.000 45.09300 ? 314 HOH C O   1 
HETATM 3488 O O   . HOH I 3 .   ? 15.01300  46.38100 -22.25200 1.000 37.35501 ? 315 HOH C O   1 
HETATM 3489 O O   . HOH I 3 .   ? 7.770     37.619   -35.248   1.000 30.58695 ? 316 HOH C O   1 
HETATM 3490 O O   . HOH I 3 .   ? 22.43000  44.69400 -3.60000  1.000 42.44831 ? 317 HOH C O   1 
# 
