data_9NG8
# 
_entry.id   9NG8 
# 
_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   9NG8         pdb_00009ng8 10.2210/pdb9ng8/pdb 
WWPDB D_1000293331 ?            ?                   
# 
_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                        9NG8 
_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 T34A 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' 18668.754 3  ? T34A ? ? 
2 non-polymer syn 'SULFATE ION'                           96.063    3  ? ?    ? ? 
3 water       nat water                                   18.015    59 ? ?    ? ? 
# 
_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       
;MPVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGAQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKG
QLAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVEYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQGLEH
HHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGAQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKG
QLAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVEYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQGLEH
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  ALA 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 GLU 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  ALA 35  34  34  ALA ALA 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 GLU 115 114 114 GLU GLU 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 147 146 146 VAL VAL 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  ALA 35  34  34  ALA ALA 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 GLU 115 114 114 GLU GLU 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 HIS 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  ALA 35  34  34  ALA ALA 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 GLU 115 114 114 GLU GLU 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 14 HOH HOH A . 
G 3 HOH 2  302 21 HOH HOH A . 
G 3 HOH 3  303 41 HOH HOH A . 
G 3 HOH 4  304 15 HOH HOH A . 
G 3 HOH 5  305 58 HOH HOH A . 
G 3 HOH 6  306 40 HOH HOH A . 
G 3 HOH 7  307 43 HOH HOH A . 
G 3 HOH 8  308 8  HOH HOH A . 
G 3 HOH 9  309 27 HOH HOH A . 
G 3 HOH 10 310 24 HOH HOH A . 
G 3 HOH 11 311 56 HOH HOH A . 
H 3 HOH 1  301 55 HOH HOH B . 
H 3 HOH 2  302 36 HOH HOH B . 
H 3 HOH 3  303 45 HOH HOH B . 
H 3 HOH 4  304 5  HOH HOH B . 
H 3 HOH 5  305 6  HOH HOH B . 
H 3 HOH 6  306 49 HOH HOH B . 
H 3 HOH 7  307 54 HOH HOH B . 
H 3 HOH 8  308 38 HOH HOH B . 
H 3 HOH 9  309 44 HOH HOH B . 
H 3 HOH 10 310 57 HOH HOH B . 
H 3 HOH 11 311 22 HOH HOH B . 
H 3 HOH 12 312 11 HOH HOH B . 
H 3 HOH 13 313 42 HOH HOH B . 
H 3 HOH 14 314 13 HOH HOH B . 
H 3 HOH 15 315 35 HOH HOH B . 
H 3 HOH 16 316 17 HOH HOH B . 
H 3 HOH 17 317 9  HOH HOH B . 
H 3 HOH 18 318 20 HOH HOH B . 
H 3 HOH 19 319 16 HOH HOH B . 
H 3 HOH 20 320 59 HOH HOH B . 
H 3 HOH 21 321 53 HOH HOH B . 
H 3 HOH 22 322 34 HOH HOH B . 
H 3 HOH 23 323 52 HOH HOH B . 
H 3 HOH 24 324 46 HOH HOH B . 
H 3 HOH 25 325 28 HOH HOH B . 
H 3 HOH 26 326 50 HOH HOH B . 
H 3 HOH 27 327 51 HOH HOH B . 
I 3 HOH 1  301 19 HOH HOH C . 
I 3 HOH 2  302 48 HOH HOH C . 
I 3 HOH 3  303 2  HOH HOH C . 
I 3 HOH 4  304 10 HOH HOH C . 
I 3 HOH 5  305 26 HOH HOH C . 
I 3 HOH 6  306 3  HOH HOH C . 
I 3 HOH 7  307 7  HOH HOH C . 
I 3 HOH 8  308 1  HOH HOH C . 
I 3 HOH 9  309 12 HOH HOH C . 
I 3 HOH 10 310 37 HOH HOH C . 
I 3 HOH 11 311 4  HOH HOH C . 
I 3 HOH 12 312 39 HOH HOH C . 
I 3 HOH 13 313 23 HOH HOH C . 
I 3 HOH 14 314 25 HOH HOH C . 
I 3 HOH 15 315 31 HOH HOH C . 
I 3 HOH 16 316 18 HOH HOH C . 
I 3 HOH 17 317 32 HOH HOH C . 
I 3 HOH 18 318 29 HOH HOH C . 
I 3 HOH 19 319 33 HOH HOH C . 
I 3 HOH 20 320 30 HOH HOH C . 
I 3 HOH 21 321 47 HOH HOH C . 
# 
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                     9NG8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     59.749 
_cell.length_a_esd                 ? 
_cell.length_b                     100.399 
_cell.length_b_esd                 ? 
_cell.length_c                     145.774 
_cell.length_c_esd                 ? 
_cell.volume                       874460.303 
_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                         9NG8 
_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                   9NG8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.96 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.18 
_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    '0.2 M ammonium sulfate 20% w/v PEG 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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         2021-09-22 
_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                          37.24 
_reflns.entry_id                                       9NG8 
_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                                     15048 
_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                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.156 
_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                             723 
_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                               0.586 
_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                               33.51 
_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                                 9NG8 
_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                             35.29 
_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                     13477 
_refine.ls_number_reflns_R_free                  1360 
_refine.ls_number_reflns_R_work                  12117 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    87.29 
_refine.ls_percent_reflns_R_free                 10.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2096 
_refine.ls_R_factor_R_free                       0.2835 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2014 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.0529 
_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                            0.4066 
_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                        35.29 
_refine_hist.number_atoms_solvent             59 
_refine_hist.number_atoms_total               3501 
_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        3427 
_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' ? 0.0080  ? 3523 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9647  ? 4771 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0493  ? 494  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0077  ? 640  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 19.8699 ? 1262 ? 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 2.60  . . 84  688  50.86 . . . . 0.3082 . . . . . . . . . . . . . . . 0.4433 
'X-RAY DIFFRACTION' 2.60 2.70  . . 95  866  63.10 . . . . 0.2669 . . . . . . . . . . . . . . . 0.3406 
'X-RAY DIFFRACTION' 2.70 2.82  . . 132 1203 88.35 . . . . 0.2602 . . . . . . . . . . . . . . . 0.3509 
'X-RAY DIFFRACTION' 2.82 2.97  . . 141 1271 92.47 . . . . 0.2252 . . . . . . . . . . . . . . . 0.3348 
'X-RAY DIFFRACTION' 2.97 3.16  . . 146 1325 96.33 . . . . 0.2351 . . . . . . . . . . . . . . . 0.3102 
'X-RAY DIFFRACTION' 3.16 3.40  . . 145 1300 93.95 . . . . 0.2309 . . . . . . . . . . . . . . . 0.3097 
'X-RAY DIFFRACTION' 3.40 3.74  . . 153 1299 94.35 . . . . 0.1845 . . . . . . . . . . . . . . . 0.2981 
'X-RAY DIFFRACTION' 3.74 4.28  . . 153 1347 96.84 . . . . 0.1595 . . . . . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 4.29 5.40  . . 152 1384 97.65 . . . . 0.1700 . . . . . . . . . . . . . . . 0.2104 
'X-RAY DIFFRACTION' 5.40 35.29 . . 159 1434 97.55 . . . . 0.1964 . . . . . . . . . . . . . . . 0.2833 
# 
_struct.entry_id                     9NG8 
_struct.title                        'cis-CaaD T34A 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        9NG8 
_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 9NG8 A 1 ? 150 ? Q6VPE5 1 ? 150 ? 0 149 
2 1 9NG8 B 1 ? 150 ? Q6VPE5 1 ? 150 ? 0 149 
3 1 9NG8 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 9NG8 ALA A 35  ? UNP Q6VPE5 THR 35 'engineered mutation' 34  1  
1 9NG8 GLU A 151 ? UNP Q6VPE5 ?   ?  'expression tag'      150 2  
1 9NG8 ASN A 152 ? UNP Q6VPE5 ?   ?  'expression tag'      151 3  
1 9NG8 LEU A 153 ? UNP Q6VPE5 ?   ?  'expression tag'      152 4  
1 9NG8 TYR A 154 ? UNP Q6VPE5 ?   ?  'expression tag'      153 5  
1 9NG8 PHE A 155 ? UNP Q6VPE5 ?   ?  'expression tag'      154 6  
1 9NG8 GLN A 156 ? UNP Q6VPE5 ?   ?  'expression tag'      155 7  
1 9NG8 GLY A 157 ? UNP Q6VPE5 ?   ?  'expression tag'      156 8  
1 9NG8 LEU A 158 ? UNP Q6VPE5 ?   ?  'expression tag'      157 9  
1 9NG8 GLU A 159 ? UNP Q6VPE5 ?   ?  'expression tag'      158 10 
1 9NG8 HIS A 160 ? UNP Q6VPE5 ?   ?  'expression tag'      159 11 
1 9NG8 HIS A 161 ? UNP Q6VPE5 ?   ?  'expression tag'      160 12 
1 9NG8 HIS A 162 ? UNP Q6VPE5 ?   ?  'expression tag'      161 13 
1 9NG8 HIS A 163 ? UNP Q6VPE5 ?   ?  'expression tag'      162 14 
1 9NG8 HIS A 164 ? UNP Q6VPE5 ?   ?  'expression tag'      163 15 
1 9NG8 HIS A 165 ? UNP Q6VPE5 ?   ?  'expression tag'      164 16 
2 9NG8 ALA B 35  ? UNP Q6VPE5 THR 35 'engineered mutation' 34  17 
2 9NG8 GLU B 151 ? UNP Q6VPE5 ?   ?  'expression tag'      150 18 
2 9NG8 ASN B 152 ? UNP Q6VPE5 ?   ?  'expression tag'      151 19 
2 9NG8 LEU B 153 ? UNP Q6VPE5 ?   ?  'expression tag'      152 20 
2 9NG8 TYR B 154 ? UNP Q6VPE5 ?   ?  'expression tag'      153 21 
2 9NG8 PHE B 155 ? UNP Q6VPE5 ?   ?  'expression tag'      154 22 
2 9NG8 GLN B 156 ? UNP Q6VPE5 ?   ?  'expression tag'      155 23 
2 9NG8 GLY B 157 ? UNP Q6VPE5 ?   ?  'expression tag'      156 24 
2 9NG8 LEU B 158 ? UNP Q6VPE5 ?   ?  'expression tag'      157 25 
2 9NG8 GLU B 159 ? UNP Q6VPE5 ?   ?  'expression tag'      158 26 
2 9NG8 HIS B 160 ? UNP Q6VPE5 ?   ?  'expression tag'      159 27 
2 9NG8 HIS B 161 ? UNP Q6VPE5 ?   ?  'expression tag'      160 28 
2 9NG8 HIS B 162 ? UNP Q6VPE5 ?   ?  'expression tag'      161 29 
2 9NG8 HIS B 163 ? UNP Q6VPE5 ?   ?  'expression tag'      162 30 
2 9NG8 HIS B 164 ? UNP Q6VPE5 ?   ?  'expression tag'      163 31 
2 9NG8 HIS B 165 ? UNP Q6VPE5 ?   ?  'expression tag'      164 32 
3 9NG8 ALA C 35  ? UNP Q6VPE5 THR 35 'engineered mutation' 34  33 
3 9NG8 GLU C 151 ? UNP Q6VPE5 ?   ?  'expression tag'      150 34 
3 9NG8 ASN C 152 ? UNP Q6VPE5 ?   ?  'expression tag'      151 35 
3 9NG8 LEU C 153 ? UNP Q6VPE5 ?   ?  'expression tag'      152 36 
3 9NG8 TYR C 154 ? UNP Q6VPE5 ?   ?  'expression tag'      153 37 
3 9NG8 PHE C 155 ? UNP Q6VPE5 ?   ?  'expression tag'      154 38 
3 9NG8 GLN C 156 ? UNP Q6VPE5 ?   ?  'expression tag'      155 39 
3 9NG8 GLY C 157 ? UNP Q6VPE5 ?   ?  'expression tag'      156 40 
3 9NG8 LEU C 158 ? UNP Q6VPE5 ?   ?  'expression tag'      157 41 
3 9NG8 GLU C 159 ? UNP Q6VPE5 ?   ?  'expression tag'      158 42 
3 9NG8 HIS C 160 ? UNP Q6VPE5 ?   ?  'expression tag'      159 43 
3 9NG8 HIS C 161 ? UNP Q6VPE5 ?   ?  'expression tag'      160 44 
3 9NG8 HIS C 162 ? UNP Q6VPE5 ?   ?  'expression tag'      161 45 
3 9NG8 HIS C 163 ? UNP Q6VPE5 ?   ?  'expression tag'      162 46 
3 9NG8 HIS C 164 ? UNP Q6VPE5 ?   ?  'expression tag'      163 47 
3 9NG8 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)' 9030  ? 
1 MORE         -102  ? 
1 'SSA (A^2)'  15240 ? 
# 
_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 GLN A 122 ? GLY A 124 ? GLN A 121 GLY A 123 5 ? 3  
HELX_P HELX_P7  AA7 HIS A 125 ? PHE A 130 ? HIS A 124 PHE A 129 1 ? 6  
HELX_P HELX_P8  AA8 ASP A 131 ? LEU A 133 ? ASP A 130 LEU A 132 5 ? 3  
HELX_P HELX_P9  AA9 SER A 134 ? THR A 143 ? SER A 133 THR A 142 1 ? 10 
HELX_P HELX_P10 AB1 THR B 14  ? GLY B 34  ? THR B 13  GLY B 33  1 ? 21 
HELX_P HELX_P11 AB2 GLN B 36  ? LEU B 39  ? GLN B 35  LEU B 38  5 ? 4  
HELX_P HELX_P12 AB3 SER B 75  ? GLU B 95  ? SER B 74  GLU B 94  1 ? 21 
HELX_P HELX_P13 AB4 ASP B 97  ? LYS B 99  ? ASP B 96  LYS B 98  5 ? 3  
HELX_P HELX_P14 AB5 PRO B 109 ? GLN B 111 ? PRO B 108 GLN B 110 5 ? 3  
HELX_P HELX_P15 AB6 HIS B 125 ? ASN B 132 ? HIS B 124 ASN B 131 1 ? 8  
HELX_P HELX_P16 AB7 SER B 134 ? ASN B 144 ? SER B 133 ASN B 143 1 ? 11 
HELX_P HELX_P17 AB8 THR C 14  ? GLY C 34  ? THR C 13  GLY C 33  1 ? 21 
HELX_P HELX_P18 AB9 GLN C 36  ? LEU C 39  ? GLN C 35  LEU C 38  5 ? 4  
HELX_P HELX_P19 AC1 SER C 75  ? GLU C 95  ? SER C 74  GLU C 94  1 ? 21 
HELX_P HELX_P20 AC2 ASP C 97  ? LYS C 99  ? ASP C 96  LYS C 98  5 ? 3  
HELX_P HELX_P21 AC3 PRO C 109 ? GLN C 111 ? PRO C 108 GLN C 110 5 ? 3  
HELX_P HELX_P22 AC4 HIS C 125 ? ASP C 131 ? HIS C 124 ASP C 130 1 ? 7  
HELX_P HELX_P23 AC5 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 VAL B 57  ? GLN B 58  ? VAL B 56  GLN B 57  
AA1 2 VAL B 52  ? LEU B 54  ? VAL B 51  LEU B 53  
AA1 3 GLN A 41  ? GLN A 47  ? GLN A 40  GLN A 46  
AA1 4 VAL A 3   ? SER A 9   ? VAL A 2   SER A 8   
AA1 5 ILE A 64  ? ARG A 71  ? ILE A 63  ARG A 70  
AA1 6 ILE A 101 ? MET A 108 ? ILE A 100 MET A 107 
AA1 7 MET C 113 ? GLU C 115 ? MET C 112 GLU C 114 
AA1 8 ARG C 118 ? PHE C 119 ? ARG C 117 PHE C 118 
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 C 41  ? GLN C 47  ? GLN C 40  GLN C 46  
AA2 4 VAL C 3   ? SER C 9   ? VAL C 2   SER C 8   
AA2 5 ILE C 64  ? ARG C 71  ? ILE C 63  ARG C 70  
AA2 6 ILE C 101 ? MET C 108 ? ILE C 100 MET C 107 
AA2 7 MET B 113 ? GLU B 115 ? MET B 112 GLU B 114 
AA2 8 ARG B 118 ? PHE B 119 ? ARG B 117 PHE B 118 
AA3 1 ARG A 118 ? PHE A 119 ? ARG A 117 PHE A 118 
AA3 2 MET A 113 ? GLU A 115 ? MET A 112 GLU A 114 
AA3 3 ILE B 101 ? MET B 108 ? ILE B 100 MET B 107 
AA3 4 ILE B 64  ? ARG B 71  ? ILE B 63  ARG B 70  
AA3 5 VAL B 3   ? SER B 9   ? VAL B 2   SER B 8   
AA3 6 GLN B 41  ? GLN B 47  ? GLN B 40  GLN B 46  
AA3 7 VAL C 52  ? LEU C 54  ? VAL C 51  LEU C 53  
AA3 8 VAL C 57  ? GLN C 58  ? VAL C 56  GLN C 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 VAL B 57  ? O VAL B 56  N LEU B 54  ? N LEU B 53  
AA1 2 3 O PHE B 53  ? O PHE B 52  N VAL A 42  ? N VAL A 41  
AA1 3 4 O ASN A 43  ? O ASN A 42  N TYR A 4   ? N TYR A 3   
AA1 4 5 N MET A 5   ? N MET A 4   O HIS A 67  ? O HIS A 66  
AA1 5 6 N GLY A 68  ? N GLY A 67  O GLY A 106 ? O GLY A 105 
AA1 6 7 N VAL A 103 ? N VAL A 102 O VAL C 114 ? O VAL C 113 
AA1 7 8 N GLU C 115 ? N GLU C 114 O ARG C 118 ? O ARG C 117 
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 C 42  ? O VAL C 41  
AA2 3 4 O GLN C 45  ? O GLN C 44  N VAL C 6   ? N VAL C 5   
AA2 4 5 N MET C 5   ? N MET C 4   O HIS C 67  ? O HIS C 66  
AA2 5 6 N VAL C 66  ? N VAL C 65  O TRP C 102 ? O TRP C 101 
AA2 6 7 O VAL C 103 ? O VAL C 102 N VAL B 114 ? N VAL B 113 
AA2 7 8 N GLU B 115 ? N GLU B 114 O ARG B 118 ? O ARG B 117 
AA3 1 2 O ARG A 118 ? O ARG A 117 N GLU A 115 ? N GLU A 114 
AA3 2 3 N VAL A 114 ? N VAL A 113 O VAL B 103 ? O VAL B 102 
AA3 3 4 O TYR B 104 ? O TYR B 103 N VAL B 66  ? N VAL B 65  
AA3 4 5 O LEU B 69  ? O LEU B 68  N VAL B 3   ? N VAL B 2   
AA3 5 6 N VAL B 6   ? N VAL B 5   O ASN B 43  ? O ASN B 42  
AA3 6 7 N VAL B 42  ? N VAL B 41  O PHE C 53  ? O PHE C 52  
AA3 7 8 N LEU C 54  ? N LEU C 53  O VAL C 57  ? O VAL C 56  
# 
_pdbx_entry_details.entry_id                   9NG8 
_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 B GLN 110 ? ? O   B HOH 301 ? ? 2.13 
2 1 NH1 C ARG 73  ? ? O1  C SO4 201 ? ? 2.16 
3 1 OG  A SER 15  ? ? O   A HOH 301 ? ? 2.17 
4 1 NH2 A ARG 73  ? ? O3  A SO4 201 ? ? 2.19 
5 1 O   A LEU 132 ? ? NH1 A ARG 137 ? ? 2.19 
# 
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 ? ? -170.59 26.44  
2 1 ASN A 143 ? ? -103.24 47.45  
3 1 GLN B 9   ? ? -38.81  119.40 
4 1 PHE C 37  ? ? -54.22  -6.41  
5 1 ASP C 130 ? ? -75.22  42.73  
6 1 ASN C 131 ? ? -156.61 1.20   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     310 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   G 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 SER 147 ? A SER 148 
3  1 Y 1 A ARG 148 ? A ARG 149 
4  1 Y 1 A THR 149 ? A THR 150 
5  1 Y 1 A GLU 150 ? A GLU 151 
6  1 Y 1 A ASN 151 ? A ASN 152 
7  1 Y 1 A LEU 152 ? A LEU 153 
8  1 Y 1 A TYR 153 ? A TYR 154 
9  1 Y 1 A PHE 154 ? A PHE 155 
10 1 Y 1 A GLN 155 ? A GLN 156 
11 1 Y 1 A GLY 156 ? A GLY 157 
12 1 Y 1 A LEU 157 ? A LEU 158 
13 1 Y 1 A GLU 158 ? A GLU 159 
14 1 Y 1 A HIS 159 ? A HIS 160 
15 1 Y 1 A HIS 160 ? A HIS 161 
16 1 Y 1 A HIS 161 ? A HIS 162 
17 1 Y 1 A HIS 162 ? A HIS 163 
18 1 Y 1 A HIS 163 ? A HIS 164 
19 1 Y 1 A HIS 164 ? A HIS 165 
20 1 Y 1 B MET 0   ? B MET 1   
21 1 Y 1 B VAL 146 ? B VAL 147 
22 1 Y 1 B SER 147 ? B SER 148 
23 1 Y 1 B ARG 148 ? B ARG 149 
24 1 Y 1 B THR 149 ? B THR 150 
25 1 Y 1 B GLU 150 ? B GLU 151 
26 1 Y 1 B ASN 151 ? B ASN 152 
27 1 Y 1 B LEU 152 ? B LEU 153 
28 1 Y 1 B TYR 153 ? B TYR 154 
29 1 Y 1 B PHE 154 ? B PHE 155 
30 1 Y 1 B GLN 155 ? B GLN 156 
31 1 Y 1 B GLY 156 ? B GLY 157 
32 1 Y 1 B LEU 157 ? B LEU 158 
33 1 Y 1 B GLU 158 ? B GLU 159 
34 1 Y 1 B HIS 159 ? B HIS 160 
35 1 Y 1 B HIS 160 ? B HIS 161 
36 1 Y 1 B HIS 161 ? B HIS 162 
37 1 Y 1 B HIS 162 ? B HIS 163 
38 1 Y 1 B HIS 163 ? B HIS 164 
39 1 Y 1 B HIS 164 ? B HIS 165 
40 1 Y 1 C MET 0   ? C MET 1   
41 1 Y 1 C VAL 146 ? C VAL 147 
42 1 Y 1 C SER 147 ? C SER 148 
43 1 Y 1 C ARG 148 ? C ARG 149 
44 1 Y 1 C THR 149 ? C THR 150 
45 1 Y 1 C GLU 150 ? C GLU 151 
46 1 Y 1 C ASN 151 ? C ASN 152 
47 1 Y 1 C LEU 152 ? C LEU 153 
48 1 Y 1 C TYR 153 ? C TYR 154 
49 1 Y 1 C PHE 154 ? C PHE 155 
50 1 Y 1 C GLN 155 ? C GLN 156 
51 1 Y 1 C GLY 156 ? C GLY 157 
52 1 Y 1 C LEU 157 ? C LEU 158 
53 1 Y 1 C GLU 158 ? C GLU 159 
54 1 Y 1 C HIS 159 ? C HIS 160 
55 1 Y 1 C HIS 160 ? C HIS 161 
56 1 Y 1 C HIS 161 ? C HIS 162 
57 1 Y 1 C HIS 162 ? C HIS 163 
58 1 Y 1 C HIS 163 ? C HIS 164 
59 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                    9NG8 
_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]   0.016737 
_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]   0.009960 
_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]   0.006860 
_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   ? 9.97600   9.69800  -24.26000 1.000 29.75808 ? 1   PRO A N   1 
ATOM   2    C CA  . PRO A 1 2   ? 8.90500   10.41700 -23.56900 1.000 26.79334 ? 1   PRO A CA  1 
ATOM   3    C C   . PRO A 1 2   ? 9.29400   10.92700 -22.18300 1.000 30.84039 ? 1   PRO A C   1 
ATOM   4    O O   . PRO A 1 2   ? 10.15100  10.34600 -21.50400 1.000 29.82592 ? 1   PRO A O   1 
ATOM   5    C CB  . PRO A 1 2   ? 7.81800   9.36400  -23.44500 1.000 24.96566 ? 1   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 2   ? 8.54900   8.10700  -23.37500 1.000 25.79824 ? 1   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 2   ? 9.76700   8.24300  -24.22500 1.000 25.86966 ? 1   PRO A CD  1 
ATOM   8    N N   . VAL A 1 3   ? 8.66400   12.02100 -21.76600 1.000 27.47433 ? 2   VAL A N   1 
ATOM   9    C CA  . VAL A 1 3   ? 8.68900   12.46300 -20.37500 1.000 30.45868 ? 2   VAL A CA  1 
ATOM   10   C C   . VAL A 1 3   ? 7.24500   12.47700 -19.88300 1.000 27.46344 ? 2   VAL A C   1 
ATOM   11   O O   . VAL A 1 3   ? 6.39200   13.19200 -20.43000 1.000 26.18641 ? 2   VAL A O   1 
ATOM   12   C CB  . VAL A 1 3   ? 9.33500   13.84900 -20.19600 1.000 24.72088 ? 2   VAL A CB  1 
ATOM   13   C CG1 . VAL A 1 3   ? 8.99800   14.38300 -18.84800 1.000 24.02582 ? 2   VAL A CG1 1 
ATOM   14   C CG2 . VAL A 1 3   ? 10.81800  13.78500 -20.33300 1.000 21.00534 ? 2   VAL A CG2 1 
ATOM   15   N N   . TYR A 1 4   ? 6.96200   11.68400 -18.87200 1.000 26.91596 ? 3   TYR A N   1 
ATOM   16   C CA  . TYR A 1 4   ? 5.64500   11.67700 -18.27000 1.000 26.66482 ? 3   TYR A CA  1 
ATOM   17   C C   . TYR A 1 4   ? 5.73100   12.50700 -16.99900 1.000 30.23817 ? 3   TYR A C   1 
ATOM   18   O O   . TYR A 1 4   ? 6.38700   12.09800 -16.02800 1.000 32.68525 ? 3   TYR A O   1 
ATOM   19   C CB  . TYR A 1 4   ? 5.19200   10.25200 -17.99500 1.000 26.24206 ? 3   TYR A CB  1 
ATOM   20   C CG  . TYR A 1 4   ? 4.79300   9.49400  -19.23700 1.000 23.41249 ? 3   TYR A CG  1 
ATOM   21   C CD1 . TYR A 1 4   ? 5.72700   8.77900  -19.97600 1.000 24.87992 ? 3   TYR A CD1 1 
ATOM   22   C CD2 . TYR A 1 4   ? 3.47600   9.48100  -19.66200 1.000 30.27348 ? 3   TYR A CD2 1 
ATOM   23   C CE1 . TYR A 1 4   ? 5.35600   8.08500  -21.10900 1.000 24.24507 ? 3   TYR A CE1 1 
ATOM   24   C CE2 . TYR A 1 4   ? 3.09300   8.78100  -20.78500 1.000 27.42336 ? 3   TYR A CE2 1 
ATOM   25   C CZ  . TYR A 1 4   ? 4.03000   8.08900  -21.50300 1.000 29.15184 ? 3   TYR A CZ  1 
ATOM   26   O OH  . TYR A 1 4   ? 3.61900   7.39900  -22.62500 1.000 36.91640 ? 3   TYR A OH  1 
ATOM   27   N N   . MET A 1 5   ? 5.12700   13.69700 -17.03100 1.000 20.50838 ? 4   MET A N   1 
ATOM   28   C CA  . MET A 1 5   ? 4.96400   14.48900 -15.82100 1.000 23.87004 ? 4   MET A CA  1 
ATOM   29   C C   . MET A 1 5   ? 3.75400   13.95400 -15.06400 1.000 20.06664 ? 4   MET A C   1 
ATOM   30   O O   . MET A 1 5   ? 2.68800   13.77300 -15.65400 1.000 23.28356 ? 4   MET A O   1 
ATOM   31   C CB  . MET A 1 5   ? 4.76800   15.96200 -16.17500 1.000 23.01179 ? 4   MET A CB  1 
ATOM   32   C CG  . MET A 1 5   ? 5.88600   16.59800 -16.96900 1.000 18.44278 ? 4   MET A CG  1 
ATOM   33   S SD  . MET A 1 5   ? 7.51300   16.31000 -16.26900 1.000 29.30816 ? 4   MET A SD  1 
ATOM   34   C CE  . MET A 1 5   ? 7.46800   17.27100 -14.74300 1.000 20.88994 ? 4   MET A CE  1 
ATOM   35   N N   . VAL A 1 6   ? 3.90600   13.67800 -13.77500 1.000 15.13038 ? 5   VAL A N   1 
ATOM   36   C CA  . VAL A 1 6   ? 2.82500   13.06700 -13.00500 1.000 19.02036 ? 5   VAL A CA  1 
ATOM   37   C C   . VAL A 1 6   ? 2.54800   13.91900 -11.76600 1.000 24.20112 ? 5   VAL A C   1 
ATOM   38   O O   . VAL A 1 6   ? 3.33800   13.92100 -10.81200 1.000 21.85087 ? 5   VAL A O   1 
ATOM   39   C CB  . VAL A 1 6   ? 3.12200   11.60900 -12.61800 1.000 22.17967 ? 5   VAL A CB  1 
ATOM   40   C CG1 . VAL A 1 6   ? 1.85400   10.93900 -12.12000 1.000 26.12963 ? 5   VAL A CG1 1 
ATOM   41   C CG2 . VAL A 1 6   ? 3.66700   10.82100 -13.79200 1.000 18.25288 ? 5   VAL A CG2 1 
ATOM   42   N N   . TYR A 1 7   ? 1.40800   14.61900 -11.77100 1.000 25.92826 ? 6   TYR A N   1 
ATOM   43   C CA  . TYR A 1 7   ? 1.06100   15.58900 -10.73500 1.000 22.09039 ? 6   TYR A CA  1 
ATOM   44   C C   . TYR A 1 7   ? 0.22300   14.88600 -9.68900  1.000 24.55060 ? 6   TYR A C   1 
ATOM   45   O O   . TYR A 1 7   ? -0.91500  14.49000 -9.95700  1.000 32.18256 ? 6   TYR A O   1 
ATOM   46   C CB  . TYR A 1 7   ? 0.32900   16.78800 -11.33400 1.000 16.73002 ? 6   TYR A CB  1 
ATOM   47   C CG  . TYR A 1 7   ? 1.17300   17.45700 -12.37700 1.000 18.93539 ? 6   TYR A CG  1 
ATOM   48   C CD1 . TYR A 1 7   ? 2.15900   18.36100 -12.01000 1.000 19.83581 ? 6   TYR A CD1 1 
ATOM   49   C CD2 . TYR A 1 7   ? 1.03500   17.13500 -13.72300 1.000 22.23240 ? 6   TYR A CD2 1 
ATOM   50   C CE1 . TYR A 1 7   ? 2.97300   18.95700 -12.94500 1.000 25.49189 ? 6   TYR A CE1 1 
ATOM   51   C CE2 . TYR A 1 7   ? 1.83500   17.73700 -14.68500 1.000 29.74811 ? 6   TYR A CE2 1 
ATOM   52   C CZ  . TYR A 1 7   ? 2.81600   18.65000 -14.29000 1.000 31.91047 ? 6   TYR A CZ  1 
ATOM   53   O OH  . TYR A 1 7   ? 3.63900   19.24700 -15.24000 1.000 24.54853 ? 6   TYR A OH  1 
ATOM   54   N N   . VAL A 1 8   ? 0.79400   14.70100 -8.50400  1.000 27.00872 ? 7   VAL A N   1 
ATOM   55   C CA  . VAL A 1 8   ? 0.11300   13.98300 -7.43600  1.000 26.75809 ? 7   VAL A CA  1 
ATOM   56   C C   . VAL A 1 8   ? 0.20700   14.79600 -6.15800  1.000 23.81629 ? 7   VAL A C   1 
ATOM   57   O O   . VAL A 1 8   ? 1.07900   15.65200 -5.98900  1.000 26.26544 ? 7   VAL A O   1 
ATOM   58   C CB  . VAL A 1 8   ? 0.66200   12.55100 -7.21100  1.000 27.08827 ? 7   VAL A CB  1 
ATOM   59   C CG1 . VAL A 1 8   ? 0.33900   11.67600 -8.41100  1.000 26.81676 ? 7   VAL A CG1 1 
ATOM   60   C CG2 . VAL A 1 8   ? 2.17700   12.53800 -6.89900  1.000 21.87925 ? 7   VAL A CG2 1 
ATOM   61   N N   . SER A 1 9   ? -0.75100  14.54700 -5.28400  1.000 25.89034 ? 8   SER A N   1 
ATOM   62   C CA  . SER A 1 9   ? -0.77000  15.17700 -3.97700  1.000 28.00118 ? 8   SER A CA  1 
ATOM   63   C C   . SER A 1 9   ? 0.32200   14.56500 -3.12000  1.000 25.80240 ? 8   SER A C   1 
ATOM   64   O O   . SER A 1 9   ? 0.67500   13.39200 -3.27300  1.000 30.45502 ? 8   SER A O   1 
ATOM   65   C CB  . SER A 1 9   ? -2.13600  14.98600 -3.32600  1.000 32.36540 ? 8   SER A CB  1 
ATOM   66   O OG  . SER A 1 9   ? -3.16000  15.52100 -4.15000  1.000 33.93576 ? 8   SER A OG  1 
ATOM   67   N N   . GLN A 1 10  ? 0.88800   15.37700 -2.23900  1.000 27.14126 ? 9   GLN A N   1 
ATOM   68   C CA  . GLN A 1 10  ? 1.98300   14.91100 -1.40500  1.000 31.54553 ? 9   GLN A CA  1 
ATOM   69   C C   . GLN A 1 10  ? 1.52900   13.74100 -0.52900  1.000 34.76416 ? 9   GLN A C   1 
ATOM   70   O O   . GLN A 1 10  ? 0.41100   13.73800 -0.00500  1.000 35.04740 ? 9   GLN A O   1 
ATOM   71   C CB  . GLN A 1 10  ? 2.49700   16.06700 -0.55800  1.000 30.65719 ? 9   GLN A CB  1 
ATOM   72   C CG  . GLN A 1 10  ? 3.40300   15.65400 0.54200   1.000 32.78082 ? 9   GLN A CG  1 
ATOM   73   C CD  . GLN A 1 10  ? 4.83700   15.57200 0.08700   1.000 42.61326 ? 9   GLN A CD  1 
ATOM   74   O OE1 . GLN A 1 10  ? 5.27000   14.56800 -0.49300  1.000 46.78643 ? 9   GLN A OE1 1 
ATOM   75   N NE2 . GLN A 1 10  ? 5.59100   16.63800 0.33600   1.000 52.04575 ? 9   GLN A NE2 1 
ATOM   76   N N   . ASP A 1 11  ? 2.39400   12.72300 -0.41700  1.000 35.48763 ? 10  ASP A N   1 
ATOM   77   C CA  . ASP A 1 11  ? 2.23400   11.46500 0.32900   1.000 36.68305 ? 10  ASP A CA  1 
ATOM   78   C C   . ASP A 1 11  ? 1.14200   10.55400 -0.21700  1.000 39.47636 ? 10  ASP A C   1 
ATOM   79   O O   . ASP A 1 11  ? 0.88700   9.50000  0.38200   1.000 47.28906 ? 10  ASP A O   1 
ATOM   80   C CB  . ASP A 1 11  ? 1.93900   11.66300 1.83100   1.000 37.14741 ? 10  ASP A CB  1 
ATOM   81   C CG  . ASP A 1 11  ? 2.99100   12.49100 2.54000   1.000 38.00172 ? 10  ASP A CG  1 
ATOM   82   O OD1 . ASP A 1 11  ? 4.20900   12.27000 2.33400   1.000 40.04929 ? 10  ASP A OD1 1 
ATOM   83   O OD2 . ASP A 1 11  ? 2.59100   13.39900 3.29000   1.000 45.68918 ? 10  ASP A OD2 1 
ATOM   84   N N   . ARG A 1 12  ? 0.47500   10.90800 -1.31700  1.000 40.39075 ? 11  ARG A N   1 
ATOM   85   C CA  . ARG A 1 12  ? -0.52100  9.99200  -1.86400  1.000 36.91459 ? 11  ARG A CA  1 
ATOM   86   C C   . ARG A 1 12  ? 0.11500   8.70600  -2.38000  1.000 36.19579 ? 11  ARG A C   1 
ATOM   87   O O   . ARG A 1 12  ? -0.56400  7.67700  -2.49700  1.000 35.41386 ? 11  ARG A O   1 
ATOM   88   C CB  . ARG A 1 12  ? -1.31500  10.68100 -2.96900  1.000 31.50722 ? 11  ARG A CB  1 
ATOM   89   C CG  . ARG A 1 12  ? -2.40800  9.81200  -3.57000  1.000 34.40681 ? 11  ARG A CG  1 
ATOM   90   C CD  . ARG A 1 12  ? -3.42100  9.40100  -2.53400  1.000 35.70641 ? 11  ARG A CD  1 
ATOM   91   N NE  . ARG A 1 12  ? -4.49000  8.63500  -3.15300  1.000 39.28563 ? 11  ARG A NE  1 
ATOM   92   C CZ  . ARG A 1 12  ? -4.39200  7.35600  -3.47300  1.000 41.70378 ? 11  ARG A CZ  1 
ATOM   93   N NH1 . ARG A 1 12  ? -3.32200  6.64600  -3.15200  1.000 34.96375 ? 11  ARG A NH1 1 
ATOM   94   N NH2 . ARG A 1 12  ? -5.38800  6.77700  -4.13900  1.000 44.18573 ? 11  ARG A NH2 1 
ATOM   95   N N   . LEU A 1 13  ? 1.39900   8.73600  -2.69000  1.000 31.54833 ? 12  LEU A N   1 
ATOM   96   C CA  . LEU A 1 13  ? 2.09400   7.54800  -3.14000  1.000 34.20532 ? 12  LEU A CA  1 
ATOM   97   C C   . LEU A 1 13  ? 3.35000   7.40900  -2.30000  1.000 36.73366 ? 12  LEU A C   1 
ATOM   98   O O   . LEU A 1 13  ? 4.11600   8.36600  -2.16700  1.000 38.41145 ? 12  LEU A O   1 
ATOM   99   C CB  . LEU A 1 13  ? 2.42300   7.63200  -4.63700  1.000 32.85509 ? 12  LEU A CB  1 
ATOM   100  C CG  . LEU A 1 13  ? 1.20400   7.83600  -5.56300  1.000 32.75723 ? 12  LEU A CG  1 
ATOM   101  C CD1 . LEU A 1 13  ? 1.62500   8.25800  -6.95500  1.000 27.54708 ? 12  LEU A CD1 1 
ATOM   102  C CD2 . LEU A 1 13  ? 0.32600   6.59100  -5.65100  1.000 34.29102 ? 12  LEU A CD2 1 
ATOM   103  N N   . THR A 1 14  ? 3.53500   6.23300  -1.70300  1.000 37.00575 ? 13  THR A N   1 
ATOM   104  C CA  . THR A 1 14  ? 4.77900   5.88600  -1.03800  1.000 39.45560 ? 13  THR A CA  1 
ATOM   105  C C   . THR A 1 14  ? 5.91100   5.77200  -2.06900  1.000 39.50960 ? 13  THR A C   1 
ATOM   106  O O   . THR A 1 14  ? 5.69400   5.92100  -3.27400  1.000 36.67816 ? 13  THR A O   1 
ATOM   107  C CB  . THR A 1 14  ? 4.59600   4.57600  -0.27000  1.000 40.41093 ? 13  THR A CB  1 
ATOM   108  O OG1 . THR A 1 14  ? 4.42500   3.49800  -1.20200  1.000 42.68749 ? 13  THR A OG1 1 
ATOM   109  C CG2 . THR A 1 14  ? 3.36900   4.65200  0.62100   1.000 21.82715 ? 13  THR A CG2 1 
ATOM   110  N N   . PRO A 1 15  ? 7.15100   5.55500  -1.62600  1.000 40.89344 ? 14  PRO A N   1 
ATOM   111  C CA  . PRO A 1 15  ? 8.19200   5.16400  -2.59500  1.000 37.88356 ? 14  PRO A CA  1 
ATOM   112  C C   . PRO A 1 15  ? 7.79500   3.98100  -3.46400  1.000 36.19546 ? 14  PRO A C   1 
ATOM   113  O O   . PRO A 1 15  ? 7.97300   4.02600  -4.69100  1.000 35.31844 ? 14  PRO A O   1 
ATOM   114  C CB  . PRO A 1 15  ? 9.39200   4.86400  -1.68500  1.000 33.10910 ? 14  PRO A CB  1 
ATOM   115  C CG  . PRO A 1 15  ? 9.25200   5.87700  -0.60700  1.000 26.23629 ? 14  PRO A CG  1 
ATOM   116  C CD  . PRO A 1 15  ? 7.74900   6.05100  -0.37600  1.000 28.83691 ? 14  PRO A CD  1 
ATOM   117  N N   . SER A 1 16  ? 7.23400   2.92400  -2.86700  1.000 39.23833 ? 15  SER A N   1 
ATOM   118  C CA  . SER A 1 16  ? 6.88700   1.74200  -3.65600  1.000 39.20449 ? 15  SER A CA  1 
ATOM   119  C C   . SER A 1 16  ? 5.70100   2.01800  -4.58000  1.000 39.70195 ? 15  SER A C   1 
ATOM   120  O O   . SER A 1 16  ? 5.64800   1.50700  -5.70700  1.000 36.58624 ? 15  SER A O   1 
ATOM   121  C CB  . SER A 1 16  ? 6.59700   0.56600  -2.72900  1.000 39.86709 ? 15  SER A CB  1 
ATOM   122  O OG  . SER A 1 16  ? 6.13600   1.01200  -1.46500  1.000 48.86172 ? 15  SER A OG  1 
ATOM   123  N N   . ALA A 1 17  ? 4.73800   2.82000  -4.12000  1.000 37.71074 ? 16  ALA A N   1 
ATOM   124  C CA  . ALA A 1 17  ? 3.66600   3.26600  -5.00400  1.000 35.89477 ? 16  ALA A CA  1 
ATOM   125  C C   . ALA A 1 17  ? 4.23100   3.97400  -6.22900  1.000 35.38699 ? 16  ALA A C   1 
ATOM   126  O O   . ALA A 1 17  ? 3.85300   3.66500  -7.36500  1.000 37.04283 ? 16  ALA A O   1 
ATOM   127  C CB  . ALA A 1 17  ? 2.71100   4.17800  -4.23900  1.000 37.15254 ? 16  ALA A CB  1 
ATOM   128  N N   . LYS A 1 18  ? 5.16300   4.91400  -6.01300  1.000 36.75012 ? 17  LYS A N   1 
ATOM   129  C CA  . LYS A 1 18  ? 5.79100   5.63000  -7.12000  1.000 31.78821 ? 17  LYS A CA  1 
ATOM   130  C C   . LYS A 1 18  ? 6.46000   4.67300  -8.09700  1.000 34.60664 ? 17  LYS A C   1 
ATOM   131  O O   . LYS A 1 18  ? 6.34200   4.84200  -9.31400  1.000 39.02041 ? 17  LYS A O   1 
ATOM   132  C CB  . LYS A 1 18  ? 6.80400   6.64300  -6.59000  1.000 24.99780 ? 17  LYS A CB  1 
ATOM   133  C CG  . LYS A 1 18  ? 6.21200   7.99500  -6.23400  1.000 26.59157 ? 17  LYS A CG  1 
ATOM   134  C CD  . LYS A 1 18  ? 7.10200   8.72000  -5.22800  1.000 25.92473 ? 17  LYS A CD  1 
ATOM   135  C CE  . LYS A 1 18  ? 6.48300   10.00500 -4.72400  1.000 27.95094 ? 17  LYS A CE  1 
ATOM   136  N NZ  . LYS A 1 18  ? 7.01200   10.35300 -3.37500  1.000 33.10398 ? 17  LYS A NZ  1 
ATOM   137  N N   . HIS A 1 19  ? 7.16400   3.66200  -7.58900  1.000 32.91256 ? 18  HIS A N   1 
ATOM   138  C CA  . HIS A 1 19  ? 7.77400   2.68300  -8.48200  1.000 34.08889 ? 18  HIS A CA  1 
ATOM   139  C C   . HIS A 1 19  ? 6.73100   2.00200  -9.35700  1.000 37.34311 ? 18  HIS A C   1 
ATOM   140  O O   . HIS A 1 19  ? 6.90100   1.90200  -10.58100 1.000 36.12532 ? 18  HIS A O   1 
ATOM   141  C CB  . HIS A 1 19  ? 8.53600   1.63100  -7.68300  1.000 34.91769 ? 18  HIS A CB  1 
ATOM   142  C CG  . HIS A 1 19  ? 9.76600   1.14000  -8.37300  1.000 35.35778 ? 18  HIS A CG  1 
ATOM   143  N ND1 . HIS A 1 19  ? 10.76500  1.98700  -8.79700  1.000 42.29082 ? 18  HIS A ND1 1 
ATOM   144  C CD2 . HIS A 1 19  ? 10.14200  -0.10400 -8.74900  1.000 38.01619 ? 18  HIS A CD2 1 
ATOM   145  C CE1 . HIS A 1 19  ? 11.72300  1.28300  -9.37300  1.000 43.23070 ? 18  HIS A CE1 1 
ATOM   146  N NE2 . HIS A 1 19  ? 11.36600  0.01100  -9.36400  1.000 43.13533 ? 18  HIS A NE2 1 
ATOM   147  N N   . ALA A 1 20  ? 5.65600   1.49700  -8.73300  1.000 34.97931 ? 19  ALA A N   1 
ATOM   148  C CA  . ALA A 1 20  ? 4.64500   0.75800  -9.47700  1.000 34.68268 ? 19  ALA A CA  1 
ATOM   149  C C   . ALA A 1 20  ? 4.01100   1.64200  -10.53200 1.000 36.57054 ? 19  ALA A C   1 
ATOM   150  O O   . ALA A 1 20  ? 3.74300   1.19500  -11.66000 1.000 30.49745 ? 19  ALA A O   1 
ATOM   151  C CB  . ALA A 1 20  ? 3.58100   0.20700  -8.52900  1.000 29.00676 ? 19  ALA A CB  1 
ATOM   152  N N   . VAL A 1 21  ? 3.78300   2.90900  -10.18200 1.000 30.35290 ? 20  VAL A N   1 
ATOM   153  C CA  . VAL A 1 21  ? 3.26600   3.86700  -11.14800 1.000 33.97912 ? 20  VAL A CA  1 
ATOM   154  C C   . VAL A 1 21  ? 4.28300   4.09800  -12.25800 1.000 32.32257 ? 20  VAL A C   1 
ATOM   155  O O   . VAL A 1 21  ? 3.96000   4.02500  -13.44900 1.000 30.49533 ? 20  VAL A O   1 
ATOM   156  C CB  . VAL A 1 21  ? 2.89800   5.18100  -10.44500 1.000 27.65441 ? 20  VAL A CB  1 
ATOM   157  C CG1 . VAL A 1 21  ? 2.86300   6.30500  -11.46700 1.000 32.65687 ? 20  VAL A CG1 1 
ATOM   158  C CG2 . VAL A 1 21  ? 1.56700   5.03300  -9.73300  1.000 31.76143 ? 20  VAL A CG2 1 
ATOM   159  N N   . ALA A 1 22  ? 5.53100   4.37400  -11.87700 1.000 31.23902 ? 21  ALA A N   1 
ATOM   160  C CA  . ALA A 1 22  ? 6.54900   4.68900  -12.86100 1.000 30.03394 ? 21  ALA A CA  1 
ATOM   161  C C   . ALA A 1 22  ? 6.82200   3.49700  -13.75700 1.000 31.97437 ? 21  ALA A C   1 
ATOM   162  O O   . ALA A 1 22  ? 7.24000   3.66700  -14.90900 1.000 28.07397 ? 21  ALA A O   1 
ATOM   163  C CB  . ALA A 1 22  ? 7.82100   5.14500  -12.15800 1.000 26.18678 ? 21  ALA A CB  1 
ATOM   164  N N   . LYS A 1 23  ? 6.59300   2.28800  -13.24000 1.000 34.20657 ? 22  LYS A N   1 
ATOM   165  C CA  . LYS A 1 23  ? 6.77400   1.07600  -14.02600 1.000 38.17187 ? 22  LYS A CA  1 
ATOM   166  C C   . LYS A 1 23  ? 5.55300   0.77800  -14.88400 1.000 35.42055 ? 22  LYS A C   1 
ATOM   167  O O   . LYS A 1 23  ? 5.69400   0.29200  -16.01400 1.000 30.79170 ? 22  LYS A O   1 
ATOM   168  C CB  . LYS A 1 23  ? 7.08000   -0.10100 -13.10200 1.000 37.26525 ? 22  LYS A CB  1 
ATOM   169  C CG  . LYS A 1 23  ? 8.56900   -0.44700 -13.02300 1.000 46.68594 ? 22  LYS A CG  1 
ATOM   170  C CD  . LYS A 1 23  ? 8.95800   -1.05300 -11.66500 1.000 47.93063 ? 22  LYS A CD  1 
ATOM   171  C CE  . LYS A 1 23  ? 8.28000   -2.40000 -11.39500 1.000 52.28193 ? 22  LYS A CE  1 
ATOM   172  N NZ  . LYS A 1 23  ? 7.99000   -2.60100 -9.92700  1.000 53.38598 ? 22  LYS A NZ  1 
ATOM   173  N N   . ALA A 1 24  ? 4.35700   1.06700  -14.36600 1.000 32.72837 ? 23  ALA A N   1 
ATOM   174  C CA  . ALA A 1 24  ? 3.15400   0.90900  -15.16600 1.000 26.51209 ? 23  ALA A CA  1 
ATOM   175  C C   . ALA A 1 24  ? 3.20700   1.80500  -16.39600 1.000 34.51689 ? 23  ALA A C   1 
ATOM   176  O O   . ALA A 1 24  ? 2.94700   1.35400  -17.51800 1.000 36.75815 ? 23  ALA A O   1 
ATOM   177  C CB  . ALA A 1 24  ? 1.91700   1.21200  -14.32300 1.000 26.26320 ? 23  ALA A CB  1 
ATOM   178  N N   . ILE A 1 25  ? 3.55000   3.07900  -16.21100 1.000 26.85711 ? 24  ILE A N   1 
ATOM   179  C CA  . ILE A 1 25  ? 3.60300   3.98100  -17.35100 1.000 25.57719 ? 24  ILE A CA  1 
ATOM   180  C C   . ILE A 1 25  ? 4.68400   3.54100  -18.33100 1.000 36.31523 ? 24  ILE A C   1 
ATOM   181  O O   . ILE A 1 25  ? 4.44400   3.44800  -19.54300 1.000 29.85297 ? 24  ILE A O   1 
ATOM   182  C CB  . ILE A 1 25  ? 3.82900   5.42200  -16.88400 1.000 26.55310 ? 24  ILE A CB  1 
ATOM   183  C CG1 . ILE A 1 25  ? 2.70500   5.85300  -15.95600 1.000 24.70540 ? 24  ILE A CG1 1 
ATOM   184  C CG2 . ILE A 1 25  ? 3.93700   6.33700  -18.09100 1.000 25.37196 ? 24  ILE A CG2 1 
ATOM   185  C CD1 . ILE A 1 25  ? 3.01400   7.11400  -15.20200 1.000 22.41532 ? 24  ILE A CD1 1 
ATOM   186  N N   . THR A 1 26  ? 5.88800   3.25800  -17.81300 1.000 29.47433 ? 25  THR A N   1 
ATOM   187  C CA  . THR A 1 26  ? 7.02200   2.89900  -18.65900 1.000 31.63484 ? 25  THR A CA  1 
ATOM   188  C C   . THR A 1 26  ? 6.76600   1.60500  -19.42700 1.000 38.37125 ? 25  THR A C   1 
ATOM   189  O O   . THR A 1 26  ? 7.12700   1.48500  -20.60700 1.000 35.39308 ? 25  THR A O   1 
ATOM   190  C CB  . THR A 1 26  ? 8.27100   2.76900  -17.79100 1.000 28.66243 ? 25  THR A CB  1 
ATOM   191  O OG1 . THR A 1 26  ? 8.58100   4.04700  -17.23900 1.000 35.73445 ? 25  THR A OG1 1 
ATOM   192  C CG2 . THR A 1 26  ? 9.46200   2.27500  -18.59300 1.000 34.50639 ? 25  THR A CG2 1 
ATOM   193  N N   . ASP A 1 27  ? 6.16100   0.61600  -18.76700 1.000 37.81286 ? 26  ASP A N   1 
ATOM   194  C CA  . ASP A 1 27  ? 5.87700   -0.64600 -19.44000 1.000 43.07668 ? 26  ASP A CA  1 
ATOM   195  C C   . ASP A 1 27  ? 4.82100   -0.46300 -20.52300 1.000 38.83770 ? 26  ASP A C   1 
ATOM   196  O O   . ASP A 1 27  ? 4.89000   -1.09000 -21.58800 1.000 40.03578 ? 26  ASP A O   1 
ATOM   197  C CB  . ASP A 1 27  ? 5.41800   -1.68800 -18.42000 1.000 45.34194 ? 26  ASP A CB  1 
ATOM   198  C CG  . ASP A 1 27  ? 6.53700   -2.12800 -17.47500 1.000 47.30598 ? 26  ASP A CG  1 
ATOM   199  O OD1 . ASP A 1 27  ? 7.71800   -1.73900 -17.67200 1.000 41.04039 ? 26  ASP A OD1 1 
ATOM   200  O OD2 . ASP A 1 27  ? 6.21600   -2.87200 -16.52500 1.000 54.05335 ? 26  ASP A OD2 1 
ATOM   201  N N   . ALA A 1 28  ? 3.82600   0.37800  -20.25500 1.000 39.64095 ? 27  ALA A N   1 
ATOM   202  C CA  . ALA A 1 28  ? 2.81000   0.66800  -21.25400 1.000 35.72318 ? 27  ALA A CA  1 
ATOM   203  C C   . ALA A 1 28  ? 3.43700   1.33000  -22.47200 1.000 38.68925 ? 27  ALA A C   1 
ATOM   204  O O   . ALA A 1 28  ? 3.18600   0.92400  -23.61300 1.000 43.26318 ? 27  ALA A O   1 
ATOM   205  C CB  . ALA A 1 28  ? 1.73000   1.55700  -20.64100 1.000 37.52369 ? 27  ALA A CB  1 
ATOM   206  N N   . HIS A 1 29  ? 4.28500   2.33500  -22.24500 1.000 29.64736 ? 28  HIS A N   1 
ATOM   207  C CA  . HIS A 1 29  ? 4.92600   3.01900  -23.35900 1.000 32.68647 ? 28  HIS A CA  1 
ATOM   208  C C   . HIS A 1 29  ? 5.80800   2.06500  -24.15200 1.000 40.20099 ? 28  HIS A C   1 
ATOM   209  O O   . HIS A 1 29  ? 5.67300   1.95700  -25.37800 1.000 42.46101 ? 28  HIS A O   1 
ATOM   210  C CB  . HIS A 1 29  ? 5.74000   4.21500  -22.86100 1.000 33.70573 ? 28  HIS A CB  1 
ATOM   211  C CG  . HIS A 1 29  ? 6.16000   5.14000  -23.95700 1.000 36.94487 ? 28  HIS A CG  1 
ATOM   212  N ND1 . HIS A 1 29  ? 5.44700   6.27400  -24.28300 1.000 32.02078 ? 28  HIS A ND1 1 
ATOM   213  C CD2 . HIS A 1 29  ? 7.19500   5.08200  -24.82900 1.000 37.69297 ? 28  HIS A CD2 1 
ATOM   214  C CE1 . HIS A 1 29  ? 6.03500   6.88400  -25.29800 1.000 32.90393 ? 28  HIS A CE1 1 
ATOM   215  N NE2 . HIS A 1 29  ? 7.09800   6.18300  -25.64800 1.000 34.83376 ? 28  HIS A NE2 1 
ATOM   216  N N   . ARG A 1 30  ? 6.71900   1.36100  -23.46500 1.000 38.92162 ? 29  ARG A N   1 
ATOM   217  C CA  . ARG A 1 30  ? 7.60200   0.41100  -24.13400 1.000 38.05148 ? 29  ARG A CA  1 
ATOM   218  C C   . ARG A 1 30  ? 6.80500   -0.59800 -24.94800 1.000 40.27089 ? 29  ARG A C   1 
ATOM   219  O O   . ARG A 1 30  ? 6.98100   -0.72000 -26.16800 1.000 39.03182 ? 29  ARG A O   1 
ATOM   220  C CB  . ARG A 1 30  ? 8.47200   -0.32500 -23.11500 1.000 45.42857 ? 29  ARG A CB  1 
ATOM   221  C CG  . ARG A 1 30  ? 9.71400   -0.94200 -23.75200 1.000 48.46188 ? 29  ARG A CG  1 
ATOM   222  C CD  . ARG A 1 30  ? 9.63600   -2.46200 -23.83100 1.000 48.81637 ? 29  ARG A CD  1 
ATOM   223  N NE  . ARG A 1 30  ? 10.95600  -3.08500 -23.80100 1.000 62.20045 ? 29  ARG A NE  1 
ATOM   224  C CZ  . ARG A 1 30  ? 11.84500  -3.03600 -24.78800 1.000 67.82527 ? 29  ARG A CZ  1 
ATOM   225  N NH1 . ARG A 1 30  ? 11.56000  -2.46500 -25.95000 1.000 70.18445 ? 29  ARG A NH1 1 
ATOM   226  N NH2 . ARG A 1 30  ? 13.05000  -3.57900 -24.60700 1.000 67.54835 ? 29  ARG A NH2 1 
ATOM   227  N N   . GLY A 1 31  ? 5.90900   -1.32400 -24.27500 1.000 39.01588 ? 30  GLY A N   1 
ATOM   228  C CA  . GLY A 1 31  ? 5.16900   -2.37800 -24.93900 1.000 39.81933 ? 30  GLY A CA  1 
ATOM   229  C C   . GLY A 1 31  ? 4.36900   -1.89600 -26.13000 1.000 41.17162 ? 30  GLY A C   1 
ATOM   230  O O   . GLY A 1 31  ? 4.20800   -2.62600 -27.10900 1.000 49.42190 ? 30  GLY A O   1 
ATOM   231  N N   . LEU A 1 32  ? 3.86300   -0.66900 -26.07600 1.000 36.05677 ? 31  LEU A N   1 
ATOM   232  C CA  . LEU A 1 32  ? 3.00600   -0.18500 -27.14500 1.000 34.05970 ? 31  LEU A CA  1 
ATOM   233  C C   . LEU A 1 32  ? 3.76500   0.55900  -28.23200 1.000 36.62233 ? 31  LEU A C   1 
ATOM   234  O O   . LEU A 1 32  ? 3.33600   0.56600  -29.39100 1.000 36.84758 ? 31  LEU A O   1 
ATOM   235  C CB  . LEU A 1 32  ? 1.93100   0.72600  -26.57100 1.000 36.09390 ? 31  LEU A CB  1 
ATOM   236  C CG  . LEU A 1 32  ? 0.73000   -0.03700 -26.06300 1.000 29.91952 ? 31  LEU A CG  1 
ATOM   237  C CD1 . LEU A 1 32  ? -0.22500  0.90200  -25.34100 1.000 20.71279 ? 31  LEU A CD1 1 
ATOM   238  C CD2 . LEU A 1 32  ? 0.07900   -0.69400 -27.25300 1.000 30.86277 ? 31  LEU A CD2 1 
ATOM   239  N N   . THR A 1 33  ? 4.87500   1.19500  -27.90000 1.000 41.46493 ? 32  THR A N   1 
ATOM   240  C CA  . THR A 1 33  ? 5.63200   1.88800  -28.92600 1.000 39.14804 ? 32  THR A CA  1 
ATOM   241  C C   . THR A 1 33  ? 6.79400   1.06800  -29.46500 1.000 42.53079 ? 32  THR A C   1 
ATOM   242  O O   . THR A 1 33  ? 7.14100   1.21800  -30.64100 1.000 40.16072 ? 32  THR A O   1 
ATOM   243  C CB  . THR A 1 33  ? 6.15800   3.21600  -28.38000 1.000 41.28635 ? 32  THR A CB  1 
ATOM   244  O OG1 . THR A 1 33  ? 7.05100   2.96100  -27.28800 1.000 42.96979 ? 32  THR A OG1 1 
ATOM   245  C CG2 . THR A 1 33  ? 5.00200   4.06100  -27.86900 1.000 35.51785 ? 32  THR A CG2 1 
ATOM   246  N N   . GLY A 1 34  ? 7.39100   0.19500  -28.64300 1.000 40.58783 ? 33  GLY A N   1 
ATOM   247  C CA  . GLY A 1 34  ? 8.64600   -0.44400 -28.98500 1.000 42.76122 ? 33  GLY A CA  1 
ATOM   248  C C   . GLY A 1 34  ? 9.88900   0.37000  -28.67500 1.000 45.05585 ? 33  GLY A C   1 
ATOM   249  O O   . GLY A 1 34  ? 10.98900  -0.20100 -28.62100 1.000 51.56683 ? 33  GLY A O   1 
ATOM   250  N N   . ALA A 1 35  ? 9.75800   1.68500  -28.48700 1.000 40.23865 ? 34  ALA A N   1 
ATOM   251  C CA  . ALA A 1 35  ? 10.86500  2.50400  -28.00800 1.000 51.10322 ? 34  ALA A CA  1 
ATOM   252  C C   . ALA A 1 35  ? 11.49700  1.87100  -26.77800 1.000 58.14570 ? 34  ALA A C   1 
ATOM   253  O O   . ALA A 1 35  ? 10.79800  1.50700  -25.82700 1.000 52.58571 ? 34  ALA A O   1 
ATOM   254  C CB  . ALA A 1 35  ? 10.38800  3.91700  -27.67300 1.000 39.41996 ? 34  ALA A CB  1 
ATOM   255  N N   . GLN A 1 36  ? 12.82500  1.74000  -26.81400 1.000 55.66627 ? 35  GLN A N   1 
ATOM   256  C CA  . GLN A 1 36  ? 13.55400  1.05400  -25.76100 1.000 54.47971 ? 35  GLN A CA  1 
ATOM   257  C C   . GLN A 1 36  ? 13.17200  1.60000  -24.39500 1.000 53.97058 ? 35  GLN A C   1 
ATOM   258  O O   . GLN A 1 36  ? 12.89900  2.79400  -24.22600 1.000 52.82119 ? 35  GLN A O   1 
ATOM   259  C CB  . GLN A 1 36  ? 15.06100  1.20000  -25.97400 1.000 60.97406 ? 35  GLN A CB  1 
ATOM   260  C CG  . GLN A 1 36  ? 15.56700  0.55800  -27.24900 1.000 60.31073 ? 35  GLN A CG  1 
ATOM   261  C CD  . GLN A 1 36  ? 16.20000  1.55800  -28.19400 1.000 60.03773 ? 35  GLN A CD  1 
ATOM   262  O OE1 . GLN A 1 36  ? 15.54700  2.49300  -28.65800 1.000 66.64662 ? 35  GLN A OE1 1 
ATOM   263  N NE2 . GLN A 1 36  ? 17.47900  1.36500  -28.48600 1.000 62.73243 ? 35  GLN A NE2 1 
ATOM   264  N N   . HIS A 1 37  ? 13.17200  0.69300  -23.42000 1.000 52.41334 ? 36  HIS A N   1 
ATOM   265  C CA  . HIS A 1 37  ? 12.71400  0.98700  -22.06800 1.000 51.61154 ? 36  HIS A CA  1 
ATOM   266  C C   . HIS A 1 37  ? 13.27100  2.30900  -21.53300 1.000 48.84569 ? 36  HIS A C   1 
ATOM   267  O O   . HIS A 1 37  ? 12.51500  3.21700  -21.17300 1.000 46.44463 ? 36  HIS A O   1 
ATOM   268  C CB  . HIS A 1 37  ? 13.11200  -0.17700 -21.16300 1.000 52.56914 ? 36  HIS A CB  1 
ATOM   269  C CG  . HIS A 1 37  ? 12.03500  -0.59600 -20.22400 1.000 54.26928 ? 36  HIS A CG  1 
ATOM   270  N ND1 . HIS A 1 37  ? 11.00600  -1.43200 -20.60200 1.000 54.05612 ? 36  HIS A ND1 1 
ATOM   271  C CD2 . HIS A 1 37  ? 11.82300  -0.29900 -18.91900 1.000 56.34968 ? 36  HIS A CD2 1 
ATOM   272  C CE1 . HIS A 1 37  ? 10.20300  -1.62900 -19.57100 1.000 62.59196 ? 36  HIS A CE1 1 
ATOM   273  N NE2 . HIS A 1 37  ? 10.67500  -0.95100 -18.53700 1.000 58.48354 ? 36  HIS A NE2 1 
ATOM   274  N N   . PHE A 1 38  ? 14.60000  2.44200  -21.50300 1.000 51.50010 ? 37  PHE A N   1 
ATOM   275  C CA  . PHE A 1 38  ? 15.25600  3.52000  -20.76100 1.000 50.91689 ? 37  PHE A CA  1 
ATOM   276  C C   . PHE A 1 38  ? 14.89700  4.91700  -21.26000 1.000 51.06293 ? 37  PHE A C   1 
ATOM   277  O O   . PHE A 1 38  ? 15.12300  5.89200  -20.52900 1.000 44.38807 ? 37  PHE A O   1 
ATOM   278  C CB  . PHE A 1 38  ? 16.78300  3.34800  -20.81800 1.000 51.06347 ? 37  PHE A CB  1 
ATOM   279  C CG  . PHE A 1 38  ? 17.31300  3.07700  -22.20100 1.000 52.47905 ? 37  PHE A CG  1 
ATOM   280  C CD1 . PHE A 1 38  ? 17.55700  4.12600  -23.08200 1.000 48.44625 ? 37  PHE A CD1 1 
ATOM   281  C CD2 . PHE A 1 38  ? 17.55900  1.77700  -22.62000 1.000 53.80880 ? 37  PHE A CD2 1 
ATOM   282  C CE1 . PHE A 1 38  ? 18.02700  3.88900  -24.34400 1.000 44.01739 ? 37  PHE A CE1 1 
ATOM   283  C CE2 . PHE A 1 38  ? 18.03100  1.52800  -23.89100 1.000 55.79896 ? 37  PHE A CE2 1 
ATOM   284  C CZ  . PHE A 1 38  ? 18.26600  2.58600  -24.75400 1.000 56.61894 ? 37  PHE A CZ  1 
ATOM   285  N N   . LEU A 1 39  ? 14.36800  5.04500  -22.48500 1.000 47.69013 ? 38  LEU A N   1 
ATOM   286  C CA  . LEU A 1 39  ? 14.12100  6.37000  -23.04100 1.000 40.73215 ? 38  LEU A CA  1 
ATOM   287  C C   . LEU A 1 39  ? 12.98800  7.09700  -22.33500 1.000 35.15890 ? 38  LEU A C   1 
ATOM   288  O O   . LEU A 1 39  ? 12.85000  8.30900  -22.51300 1.000 39.81147 ? 38  LEU A O   1 
ATOM   289  C CB  . LEU A 1 39  ? 13.80600  6.27600  -24.53700 1.000 38.17439 ? 38  LEU A CB  1 
ATOM   290  C CG  . LEU A 1 39  ? 14.95600  6.26000  -25.54600 1.000 41.05741 ? 38  LEU A CG  1 
ATOM   291  C CD1 . LEU A 1 39  ? 14.40700  6.18300  -26.97100 1.000 52.57668 ? 38  LEU A CD1 1 
ATOM   292  C CD2 . LEU A 1 39  ? 15.84800  7.47300  -25.39800 1.000 43.16306 ? 38  LEU A CD2 1 
ATOM   293  N N   . ALA A 1 40  ? 12.17700  6.39600  -21.54700 1.000 31.66226 ? 39  ALA A N   1 
ATOM   294  C CA  . ALA A 1 40  ? 11.00300  6.98700  -20.91700 1.000 30.68072 ? 39  ALA A CA  1 
ATOM   295  C C   . ALA A 1 40  ? 11.34400  7.47600  -19.51400 1.000 36.01081 ? 39  ALA A C   1 
ATOM   296  O O   . ALA A 1 40  ? 11.79500  6.69600  -18.66700 1.000 37.68327 ? 39  ALA A O   1 
ATOM   297  C CB  . ALA A 1 40  ? 9.85600   5.97900  -20.85900 1.000 28.35846 ? 39  ALA A CB  1 
ATOM   298  N N   . GLN A 1 41  ? 11.11700  8.76000  -19.26700 1.000 32.62378 ? 40  GLN A N   1 
ATOM   299  C CA  . GLN A 1 41  ? 11.25200  9.34500  -17.94400 1.000 29.25075 ? 40  GLN A CA  1 
ATOM   300  C C   . GLN A 1 41  ? 9.86600   9.50300  -17.32900 1.000 29.26892 ? 40  GLN A C   1 
ATOM   301  O O   . GLN A 1 41  ? 8.94000   9.98600  -17.98600 1.000 32.56185 ? 40  GLN A O   1 
ATOM   302  C CB  . GLN A 1 41  ? 11.96000  10.70200 -18.01900 1.000 26.02704 ? 40  GLN A CB  1 
ATOM   303  C CG  . GLN A 1 41  ? 11.98200  11.44900 -16.70300 1.000 30.23041 ? 40  GLN A CG  1 
ATOM   304  C CD  . GLN A 1 41  ? 12.61900  12.82700 -16.78900 1.000 28.98850 ? 40  GLN A CD  1 
ATOM   305  O OE1 . GLN A 1 41  ? 12.36200  13.68900 -15.94800 1.000 26.45255 ? 40  GLN A OE1 1 
ATOM   306  N NE2 . GLN A 1 41  ? 13.46000  13.03900 -17.80200 1.000 26.58775 ? 40  GLN A NE2 1 
ATOM   307  N N   . VAL A 1 42  ? 9.72300   9.10800  -16.07300 1.000 28.03081 ? 41  VAL A N   1 
ATOM   308  C CA  . VAL A 1 42  ? 8.51000   9.36000  -15.30500 1.000 28.65284 ? 41  VAL A CA  1 
ATOM   309  C C   . VAL A 1 42  ? 8.89400   10.28300 -14.15700 1.000 30.54644 ? 41  VAL A C   1 
ATOM   310  O O   . VAL A 1 42  ? 9.76700   9.95100  -13.34800 1.000 29.97104 ? 41  VAL A O   1 
ATOM   311  C CB  . VAL A 1 42  ? 7.87400   8.05700  -14.79700 1.000 31.02174 ? 41  VAL A CB  1 
ATOM   312  C CG1 . VAL A 1 42  ? 6.87900   8.34500  -13.67900 1.000 25.99860 ? 41  VAL A CG1 1 
ATOM   313  C CG2 . VAL A 1 42  ? 7.22000   7.28900  -15.95500 1.000 22.95562 ? 41  VAL A CG2 1 
ATOM   314  N N   . ASN A 1 43  ? 8.26200   11.44900 -14.09300 1.000 27.45650 ? 42  ASN A N   1 
ATOM   315  C CA  . ASN A 1 43  ? 8.69900   12.50100 -13.19100 1.000 24.80903 ? 42  ASN A CA  1 
ATOM   316  C C   . ASN A 1 43  ? 7.53900   12.94300 -12.31500 1.000 21.29065 ? 42  ASN A C   1 
ATOM   317  O O   . ASN A 1 43  ? 6.58300   13.53900 -12.80700 1.000 24.39062 ? 42  ASN A O   1 
ATOM   318  C CB  . ASN A 1 43  ? 9.24400   13.68300 -13.97900 1.000 22.93836 ? 42  ASN A CB  1 
ATOM   319  C CG  . ASN A 1 43  ? 9.95600   14.66400 -13.10600 1.000 23.45245 ? 42  ASN A CG  1 
ATOM   320  O OD1 . ASN A 1 43  ? 9.98200   14.52200 -11.88000 1.000 28.54905 ? 42  ASN A OD1 1 
ATOM   321  N ND2 . ASN A 1 43  ? 10.52000  15.69000 -13.72000 1.000 20.51304 ? 42  ASN A ND2 1 
ATOM   322  N N   . PHE A 1 44  ? 7.63500   12.69200 -11.02300 1.000 21.85249 ? 43  PHE A N   1 
ATOM   323  C CA  . PHE A 1 44  ? 6.56600   13.05300 -10.10300 1.000 23.79367 ? 43  PHE A CA  1 
ATOM   324  C C   . PHE A 1 44  ? 6.69400   14.51000 -9.66400  1.000 25.50946 ? 43  PHE A C   1 
ATOM   325  O O   . PHE A 1 44  ? 7.77000   14.95800 -9.25400  1.000 27.74444 ? 43  PHE A O   1 
ATOM   326  C CB  . PHE A 1 44  ? 6.57300   12.10600 -8.90600  1.000 19.25613 ? 43  PHE A CB  1 
ATOM   327  C CG  . PHE A 1 44  ? 6.17200   10.71900 -9.27100  1.000 21.29989 ? 43  PHE A CG  1 
ATOM   328  C CD1 . PHE A 1 44  ? 7.11800   9.79300  -9.67400  1.000 20.70627 ? 43  PHE A CD1 1 
ATOM   329  C CD2 . PHE A 1 44  ? 4.83500   10.36400 -9.30000  1.000 21.82414 ? 43  PHE A CD2 1 
ATOM   330  C CE1 . PHE A 1 44  ? 6.75000   8.51200  -10.05000 1.000 24.11873 ? 43  PHE A CE1 1 
ATOM   331  C CE2 . PHE A 1 44  ? 4.45400   9.07900  -9.67700  1.000 24.71948 ? 43  PHE A CE2 1 
ATOM   332  C CZ  . PHE A 1 44  ? 5.42200   8.15100  -10.05200 1.000 24.04837 ? 43  PHE A CZ  1 
ATOM   333  N N   . GLN A 1 45  ? 5.59800   15.25400 -9.79300  1.000 27.02703 ? 44  GLN A N   1 
ATOM   334  C CA  . GLN A 1 45  ? 5.44700   16.58000 -9.20400  1.000 25.82737 ? 44  GLN A CA  1 
ATOM   335  C C   . GLN A 1 45  ? 4.40900   16.46300 -8.09500  1.000 24.33577 ? 44  GLN A C   1 
ATOM   336  O O   . GLN A 1 45  ? 3.21200   16.30600 -8.36400  1.000 25.44292 ? 44  GLN A O   1 
ATOM   337  C CB  . GLN A 1 45  ? 5.01600   17.60900 -10.24200 1.000 25.47736 ? 44  GLN A CB  1 
ATOM   338  C CG  . GLN A 1 45  ? 6.00700   17.83100 -11.37300 1.000 24.96371 ? 44  GLN A CG  1 
ATOM   339  C CD  . GLN A 1 45  ? 7.38100   18.28000 -10.91500 1.000 25.44151 ? 44  GLN A CD  1 
ATOM   340  O OE1 . GLN A 1 45  ? 8.35400   17.53800 -11.04400 1.000 21.99197 ? 44  GLN A OE1 1 
ATOM   341  N NE2 . GLN A 1 45  ? 7.47600   19.52000 -10.41700 1.000 27.67289 ? 44  GLN A NE2 1 
ATOM   342  N N   . GLU A 1 46  ? 4.86800   16.50800 -6.85700  1.000 25.67621 ? 45  GLU A N   1 
ATOM   343  C CA  . GLU A 1 46  ? 3.99800   16.41300 -5.69700  1.000 28.87292 ? 45  GLU A CA  1 
ATOM   344  C C   . GLU A 1 46  ? 3.64100   17.80500 -5.19600  1.000 26.89072 ? 45  GLU A C   1 
ATOM   345  O O   . GLU A 1 46  ? 4.50200   18.68400 -5.10700  1.000 24.59974 ? 45  GLU A O   1 
ATOM   346  C CB  . GLU A 1 46  ? 4.67100   15.63500 -4.56900  1.000 29.95984 ? 45  GLU A CB  1 
ATOM   347  C CG  . GLU A 1 46  ? 4.51600   14.15000 -4.62700  1.000 30.26882 ? 45  GLU A CG  1 
ATOM   348  C CD  . GLU A 1 46  ? 5.53900   13.45200 -3.74400  1.000 34.68667 ? 45  GLU A CD  1 
ATOM   349  O OE1 . GLU A 1 46  ? 6.65900   13.98600 -3.60400  1.000 33.78944 ? 45  GLU A OE1 1 
ATOM   350  O OE2 . GLU A 1 46  ? 5.21000   12.38800 -3.17400  1.000 35.35090 ? 45  GLU A OE2 1 
ATOM   351  N N   . GLN A 1 47  ? 2.37900   18.00000 -4.85900  1.000 28.31608 ? 46  GLN A N   1 
ATOM   352  C CA  . GLN A 1 47  ? 1.95400   19.24600 -4.24800  1.000 27.23846 ? 46  GLN A CA  1 
ATOM   353  C C   . GLN A 1 47  ? 1.18500   18.92200 -2.98800  1.000 30.04189 ? 46  GLN A C   1 
ATOM   354  O O   . GLN A 1 47  ? 0.73700   17.78400 -2.79600  1.000 31.14150 ? 46  GLN A O   1 
ATOM   355  C CB  . GLN A 1 47  ? 1.09500   20.08000 -5.20500  1.000 26.91057 ? 46  GLN A CB  1 
ATOM   356  C CG  . GLN A 1 47  ? 1.89300   20.69700 -6.33900  1.000 24.33194 ? 46  GLN A CG  1 
ATOM   357  C CD  . GLN A 1 47  ? 2.88400   21.74800 -5.85800  1.000 26.10366 ? 46  GLN A CD  1 
ATOM   358  O OE1 . GLN A 1 47  ? 2.56100   22.56700 -4.99400  1.000 28.84110 ? 46  GLN A OE1 1 
ATOM   359  N NE2 . GLN A 1 47  ? 4.09300   21.73600 -6.42800  1.000 22.45708 ? 46  GLN A NE2 1 
ATOM   360  N N   . PRO A 1 48  ? 1.07100   19.88000 -2.07200  1.000 28.75822 ? 47  PRO A N   1 
ATOM   361  C CA  . PRO A 1 48  ? 0.17400   19.70000 -0.92700  1.000 27.43101 ? 47  PRO A CA  1 
ATOM   362  C C   . PRO A 1 48  ? -1.22800  19.33000 -1.38400  1.000 30.87523 ? 47  PRO A C   1 
ATOM   363  O O   . PRO A 1 48  ? -1.70100  19.75100 -2.44800  1.000 33.90759 ? 47  PRO A O   1 
ATOM   364  C CB  . PRO A 1 48  ? 0.18400   21.06300 -0.22800  1.000 27.94720 ? 47  PRO A CB  1 
ATOM   365  C CG  . PRO A 1 48  ? 1.34700   21.82600 -0.81500  1.000 34.58843 ? 47  PRO A CG  1 
ATOM   366  C CD  . PRO A 1 48  ? 1.90300   21.09500 -1.98900  1.000 26.98181 ? 47  PRO A CD  1 
ATOM   367  N N   . ALA A 1 49  ? -1.88700  18.51200 -0.57900  1.000 29.37653 ? 48  ALA A N   1 
ATOM   368  C CA  . ALA A 1 49  ? -3.28200  18.22000 -0.85100  1.000 30.41356 ? 48  ALA A CA  1 
ATOM   369  C C   . ALA A 1 49  ? -4.08300  19.51400 -0.76000  1.000 27.66483 ? 48  ALA A C   1 
ATOM   370  O O   . ALA A 1 49  ? -3.78300  20.39400 0.04900   1.000 33.46140 ? 48  ALA A O   1 
ATOM   371  C CB  . ALA A 1 49  ? -3.79400  17.16700 0.12600   1.000 25.72451 ? 48  ALA A CB  1 
ATOM   372  N N   . GLY A 1 50  ? -5.08300  19.65200 -1.61500  1.000 26.72266 ? 49  GLY A N   1 
ATOM   373  C CA  . GLY A 1 50  ? -5.82300  20.89000 -1.68100  1.000 26.09496 ? 49  GLY A CA  1 
ATOM   374  C C   . GLY A 1 50  ? -5.36200  21.85700 -2.74900  1.000 27.65286 ? 49  GLY A C   1 
ATOM   375  O O   . GLY A 1 50  ? -5.99300  22.90300 -2.92400  1.000 24.09582 ? 49  GLY A O   1 
ATOM   376  N N   . ASN A 1 51  ? -4.28500  21.54900 -3.46800  1.000 25.56492 ? 50  ASN A N   1 
ATOM   377  C CA  . ASN A 1 51  ? -3.85300  22.35100 -4.59900  1.000 19.24988 ? 50  ASN A CA  1 
ATOM   378  C C   . ASN A 1 51  ? -4.54500  21.95400 -5.89700  1.000 23.82709 ? 50  ASN A C   1 
ATOM   379  O O   . ASN A 1 51  ? -4.14600  22.42400 -6.96700  1.000 29.05909 ? 50  ASN A O   1 
ATOM   380  C CB  . ASN A 1 51  ? -2.33000  22.24100 -4.76300  1.000 24.76582 ? 50  ASN A CB  1 
ATOM   381  C CG  . ASN A 1 51  ? -1.56900  23.33000 -4.00000  1.000 32.30402 ? 50  ASN A CG  1 
ATOM   382  O OD1 . ASN A 1 51  ? -0.74500  24.04600 -4.57600  1.000 35.66076 ? 50  ASN A OD1 1 
ATOM   383  N ND2 . ASN A 1 51  ? -1.84400  23.45800 -2.69800  1.000 28.48519 ? 50  ASN A ND2 1 
ATOM   384  N N   . VAL A 1 52  ? -5.55400  21.08900 -5.84600  1.000 25.87695 ? 51  VAL A N   1 
ATOM   385  C CA  . VAL A 1 52  ? -6.28100  20.66300 -7.03700  1.000 25.59803 ? 51  VAL A CA  1 
ATOM   386  C C   . VAL A 1 52  ? -7.74300  21.05900 -6.89200  1.000 25.48048 ? 51  VAL A C   1 
ATOM   387  O O   . VAL A 1 52  ? -8.39400  20.71300 -5.90300  1.000 32.69438 ? 51  VAL A O   1 
ATOM   388  C CB  . VAL A 1 52  ? -6.15100  19.15200 -7.28300  1.000 22.30303 ? 51  VAL A CB  1 
ATOM   389  C CG1 . VAL A 1 52  ? -7.13000  18.73100 -8.33900  1.000 28.00140 ? 51  VAL A CG1 1 
ATOM   390  C CG2 . VAL A 1 52  ? -4.75700  18.82200 -7.74500  1.000 17.09239 ? 51  VAL A CG2 1 
ATOM   391  N N   . PHE A 1 53  ? -8.24800  21.79400 -7.86700  1.000 26.40556 ? 52  PHE A N   1 
ATOM   392  C CA  . PHE A 1 53  ? -9.64900  22.16300 -7.94300  1.000 25.82530 ? 52  PHE A CA  1 
ATOM   393  C C   . PHE A 1 53  ? -10.24600 21.61200 -9.22800  1.000 28.30962 ? 52  PHE A C   1 
ATOM   394  O O   . PHE A 1 53  ? -9.64100  21.71300 -10.30400 1.000 27.84409 ? 52  PHE A O   1 
ATOM   395  C CB  . PHE A 1 53  ? -9.81900  23.67800 -7.90000  1.000 26.81643 ? 52  PHE A CB  1 
ATOM   396  C CG  . PHE A 1 53  ? -9.34200  24.28700 -6.63000  1.000 29.69725 ? 52  PHE A CG  1 
ATOM   397  C CD1 . PHE A 1 53  ? -7.98400  24.41200 -6.37500  1.000 23.82340 ? 52  PHE A CD1 1 
ATOM   398  C CD2 . PHE A 1 53  ? -10.24900 24.72200 -5.67600  1.000 29.07671 ? 52  PHE A CD2 1 
ATOM   399  C CE1 . PHE A 1 53  ? -7.53400  24.96600 -5.19000  1.000 20.25872 ? 52  PHE A CE1 1 
ATOM   400  C CE2 . PHE A 1 53  ? -9.80800  25.27300 -4.48500  1.000 28.52853 ? 52  PHE A CE2 1 
ATOM   401  C CZ  . PHE A 1 53  ? -8.43700  25.39000 -4.24500  1.000 29.30154 ? 52  PHE A CZ  1 
ATOM   402  N N   . LEU A 1 54  ? -11.42000 21.00900 -9.10100  1.000 22.63113 ? 53  LEU A N   1 
ATOM   403  C CA  . LEU A 1 54  ? -12.21000 20.56200 -10.23500 1.000 27.39722 ? 53  LEU A CA  1 
ATOM   404  C C   . LEU A 1 54  ? -13.50700 21.35500 -10.21700 1.000 37.88275 ? 53  LEU A C   1 
ATOM   405  O O   . LEU A 1 54  ? -14.22400 21.33900 -9.20700  1.000 32.71651 ? 53  LEU A O   1 
ATOM   406  C CB  . LEU A 1 54  ? -12.50300 19.07100 -10.15700 1.000 24.40622 ? 53  LEU A CB  1 
ATOM   407  C CG  . LEU A 1 54  ? -11.30800 18.14400 -10.09300 1.000 23.50105 ? 53  LEU A CG  1 
ATOM   408  C CD1 . LEU A 1 54  ? -11.79800 16.71100 -10.15800 1.000 24.00868 ? 53  LEU A CD1 1 
ATOM   409  C CD2 . LEU A 1 54  ? -10.38800 18.44000 -11.23400 1.000 24.98988 ? 53  LEU A CD2 1 
ATOM   410  N N   . GLY A 1 55  ? -13.80600 22.03900 -11.33200 1.000 33.12740 ? 54  GLY A N   1 
ATOM   411  C CA  . GLY A 1 55  ? -14.92300 22.96900 -11.39700 1.000 33.11296 ? 54  GLY A CA  1 
ATOM   412  C C   . GLY A 1 55  ? -15.05300 23.84200 -10.16100 1.000 36.01679 ? 54  GLY A C   1 
ATOM   413  O O   . GLY A 1 55  ? -16.16100 24.02200 -9.64100  1.000 37.93978 ? 54  GLY A O   1 
ATOM   414  N N   . GLY A 1 56  ? -13.92200 24.35300 -9.66200  1.000 31.23025 ? 55  GLY A N   1 
ATOM   415  C CA  . GLY A 1 56  ? -13.88000 25.24200 -8.51800  1.000 28.39059 ? 55  GLY A CA  1 
ATOM   416  C C   . GLY A 1 56  ? -13.99900 24.59500 -7.15200  1.000 31.91112 ? 55  GLY A C   1 
ATOM   417  O O   . GLY A 1 56  ? -14.03100 25.31800 -6.15100  1.000 33.66536 ? 55  GLY A O   1 
ATOM   418  N N   . VAL A 1 57  ? -14.05500 23.26700 -7.06200  1.000 32.08859 ? 56  VAL A N   1 
ATOM   419  C CA  . VAL A 1 57  ? -14.15400 22.57400 -5.78200  1.000 28.90961 ? 56  VAL A CA  1 
ATOM   420  C C   . VAL A 1 57  ? -12.79600 21.98900 -5.43000  1.000 29.25941 ? 56  VAL A C   1 
ATOM   421  O O   . VAL A 1 57  ? -12.21300 21.23600 -6.22000  1.000 28.81067 ? 56  VAL A O   1 
ATOM   422  C CB  . VAL A 1 57  ? -15.21800 21.46200 -5.82500  1.000 33.57145 ? 56  VAL A CB  1 
ATOM   423  C CG1 . VAL A 1 57  ? -15.20400 20.67200 -4.50400  1.000 25.05969 ? 56  VAL A CG1 1 
ATOM   424  C CG2 . VAL A 1 57  ? -16.59600 22.03500 -6.11700  1.000 30.28334 ? 56  VAL A CG2 1 
ATOM   425  N N   . GLN A 1 58  ? -12.29800 22.31000 -4.23600  1.000 34.53700 ? 57  GLN A N   1 
ATOM   426  C CA  . GLN A 1 58  ? -11.02100 21.75800 -3.78800  1.000 32.49930 ? 57  GLN A CA  1 
ATOM   427  C C   . GLN A 1 58  ? -11.09900 20.23400 -3.68000  1.000 25.55985 ? 57  GLN A C   1 
ATOM   428  O O   . GLN A 1 58  ? -12.12500 19.67600 -3.29900  1.000 27.46771 ? 57  GLN A O   1 
ATOM   429  C CB  . GLN A 1 58  ? -10.63700 22.37700 -2.43800  1.000 30.68954 ? 57  GLN A CB  1 
ATOM   430  C CG  . GLN A 1 58  ? -9.22100  22.01900 -1.97600  1.000 29.68478 ? 57  GLN A CG  1 
ATOM   431  C CD  . GLN A 1 58  ? -8.79300  22.78600 -0.74400  1.000 28.95200 ? 57  GLN A CD  1 
ATOM   432  O OE1 . GLN A 1 58  ? -9.50000  22.82900 0.25500   1.000 29.09609 ? 57  GLN A OE1 1 
ATOM   433  N NE2 . GLN A 1 58  ? -7.62900  23.41200 -0.81600  1.000 40.82269 ? 57  GLN A NE2 1 
ATOM   434  N N   . GLN A 1 59  ? -10.02200 19.54400 -4.03400  1.000 28.51235 ? 58  GLN A N   1 
ATOM   435  C CA  . GLN A 1 59  ? -10.00600 18.09400 -3.89500  1.000 28.31091 ? 58  GLN A CA  1 
ATOM   436  C C   . GLN A 1 59  ? -9.12600  17.67400 -2.72900  1.000 27.71423 ? 58  GLN A C   1 
ATOM   437  O O   . GLN A 1 59  ? -8.31200  18.44900 -2.20900  1.000 30.61215 ? 58  GLN A O   1 
ATOM   438  C CB  . GLN A 1 59  ? -9.51100  17.38500 -5.16400  1.000 24.56209 ? 58  GLN A CB  1 
ATOM   439  C CG  . GLN A 1 59  ? -10.07200 17.93400 -6.46300  1.000 29.87894 ? 58  GLN A CG  1 
ATOM   440  C CD  . GLN A 1 59  ? -11.57200 17.76100 -6.58500  1.000 29.80423 ? 58  GLN A CD  1 
ATOM   441  O OE1 . GLN A 1 59  ? -12.06700 16.71600 -6.99300  1.000 27.39492 ? 58  GLN A OE1 1 
ATOM   442  N NE2 . GLN A 1 59  ? -12.30300 18.80000 -6.22400  1.000 27.92608 ? 58  GLN A NE2 1 
ATOM   443  N N   . GLY A 1 60  ? -9.32000  16.42400 -2.31900  1.000 24.46103 ? 59  GLY A N   1 
ATOM   444  C CA  . GLY A 1 60  ? -8.39900  15.76000 -1.42900  1.000 28.60853 ? 59  GLY A CA  1 
ATOM   445  C C   . GLY A 1 60  ? -7.12800  15.40600 -2.15900  1.000 31.51432 ? 59  GLY A C   1 
ATOM   446  O O   . GLY A 1 60  ? -6.57100  16.23200 -2.88700  1.000 39.00317 ? 59  GLY A O   1 
ATOM   447  N N   . GLY A 1 61  ? -6.67000  14.17300 -2.00900  1.000 38.58381 ? 60  GLY A N   1 
ATOM   448  C CA  . GLY A 1 61  ? -5.38300  13.81700 -2.56700  1.000 40.09966 ? 60  GLY A CA  1 
ATOM   449  C C   . GLY A 1 61  ? -5.40800  12.68900 -3.57500  1.000 39.87383 ? 60  GLY A C   1 
ATOM   450  O O   . GLY A 1 61  ? -4.35800  12.13200 -3.89500  1.000 41.57102 ? 60  GLY A O   1 
ATOM   451  N N   . ASP A 1 62  ? -6.57200  12.34500 -4.10600  1.000 33.16926 ? 61  ASP A N   1 
ATOM   452  C CA  . ASP A 1 62  ? -6.62100  11.23900 -5.04500  1.000 33.63224 ? 61  ASP A CA  1 
ATOM   453  C C   . ASP A 1 62  ? -6.40300  11.64800 -6.49600  1.000 36.13461 ? 61  ASP A C   1 
ATOM   454  O O   . ASP A 1 62  ? -6.25500  10.76600 -7.34500  1.000 44.33326 ? 61  ASP A O   1 
ATOM   455  C CB  . ASP A 1 62  ? -7.95600  10.51300 -4.92700  1.000 37.24207 ? 61  ASP A CB  1 
ATOM   456  C CG  . ASP A 1 62  ? -8.00900  9.62700  -3.71100  1.000 41.56791 ? 61  ASP A CG  1 
ATOM   457  O OD1 . ASP A 1 62  ? -7.21600  9.90200  -2.78700  1.000 43.06347 ? 61  ASP A OD1 1 
ATOM   458  O OD2 . ASP A 1 62  ? -8.82300  8.67200  -3.67700  1.000 40.28354 ? 61  ASP A OD2 1 
ATOM   459  N N   . THR A 1 63  ? -6.37200  12.93700 -6.81900  1.000 33.50338 ? 62  THR A N   1 
ATOM   460  C CA  . THR A 1 63  ? -6.30700  13.31400 -8.22300  1.000 38.34391 ? 62  THR A CA  1 
ATOM   461  C C   . THR A 1 63  ? -4.90700  13.08600 -8.76300  1.000 35.71232 ? 62  THR A C   1 
ATOM   462  O O   . THR A 1 63  ? -3.92600  13.49800 -8.14400  1.000 36.51442 ? 62  THR A O   1 
ATOM   463  C CB  . THR A 1 63  ? -6.68600  14.77600 -8.43900  1.000 38.15564 ? 62  THR A CB  1 
ATOM   464  O OG1 . THR A 1 63  ? -7.70300  15.17100 -7.51200  1.000 41.71064 ? 62  THR A OG1 1 
ATOM   465  C CG2 . THR A 1 63  ? -7.23300  14.94000 -9.85500  1.000 39.56293 ? 62  THR A CG2 1 
ATOM   466  N N   . ILE A 1 64  ? -4.82200  12.44600 -9.92600  1.000 32.45663 ? 63  ILE A N   1 
ATOM   467  C CA  . ILE A 1 64  ? -3.56800  12.23900 -10.63800 1.000 30.25317 ? 63  ILE A CA  1 
ATOM   468  C C   . ILE A 1 64  ? -3.71700  12.82700 -12.03700 1.000 27.54406 ? 63  ILE A C   1 
ATOM   469  O O   . ILE A 1 64  ? -4.68300  12.51800 -12.74800 1.000 28.14666 ? 63  ILE A O   1 
ATOM   470  C CB  . ILE A 1 64  ? -3.18700  10.74400 -10.70800 1.000 27.91680 ? 63  ILE A CB  1 
ATOM   471  C CG1 . ILE A 1 64  ? -2.75300  10.23200 -9.33300  1.000 30.88157 ? 63  ILE A CG1 1 
ATOM   472  C CG2 . ILE A 1 64  ? -2.05200  10.52200 -11.70800 1.000 24.04034 ? 63  ILE A CG2 1 
ATOM   473  C CD1 . ILE A 1 64  ? -2.51100  8.72900  -9.25000  1.000 29.11846 ? 63  ILE A CD1 1 
ATOM   474  N N   . PHE A 1 65  ? -2.77700  13.68100 -12.43000 1.000 22.11969 ? 64  PHE A N   1 
ATOM   475  C CA  . PHE A 1 65  ? -2.73100  14.19300 -13.79600 1.000 27.26937 ? 64  PHE A CA  1 
ATOM   476  C C   . PHE A 1 65  ? -1.42900  13.73400 -14.44600 1.000 22.97504 ? 64  PHE A C   1 
ATOM   477  O O   . PHE A 1 65  ? -0.34000  13.98600 -13.91500 1.000 20.22465 ? 64  PHE A O   1 
ATOM   478  C CB  . PHE A 1 65  ? -2.86700  15.72500 -13.83200 1.000 22.94370 ? 64  PHE A CB  1 
ATOM   479  C CG  . PHE A 1 65  ? -2.73000  16.31000 -15.22300 1.000 22.35541 ? 64  PHE A CG  1 
ATOM   480  C CD1 . PHE A 1 65  ? -3.37500  15.72900 -16.29700 1.000 23.64984 ? 64  PHE A CD1 1 
ATOM   481  C CD2 . PHE A 1 65  ? -1.94300  17.42300 -15.45100 1.000 20.35474 ? 64  PHE A CD2 1 
ATOM   482  C CE1 . PHE A 1 65  ? -3.23500  16.25300 -17.57400 1.000 25.82301 ? 64  PHE A CE1 1 
ATOM   483  C CE2 . PHE A 1 65  ? -1.79900  17.94300 -16.72000 1.000 17.86948 ? 64  PHE A CE2 1 
ATOM   484  C CZ  . PHE A 1 65  ? -2.43600  17.36200 -17.78000 1.000 20.98653 ? 64  PHE A CZ  1 
ATOM   485  N N   . VAL A 1 66  ? -1.54500  13.03800 -15.57100 1.000 19.31671 ? 65  VAL A N   1 
ATOM   486  C CA  . VAL A 1 66  ? -0.39300  12.58300 -16.33800 1.000 24.33197 ? 65  VAL A CA  1 
ATOM   487  C C   . VAL A 1 66  ? -0.29500  13.45800 -17.58300 1.000 25.43938 ? 65  VAL A C   1 
ATOM   488  O O   . VAL A 1 66  ? -1.11600  13.34000 -18.50400 1.000 25.13051 ? 65  VAL A O   1 
ATOM   489  C CB  . VAL A 1 66  ? -0.49400  11.09500 -16.71800 1.000 27.98870 ? 65  VAL A CB  1 
ATOM   490  C CG1 . VAL A 1 66  ? 0.69500   10.67000 -17.58600 1.000 24.51478 ? 65  VAL A CG1 1 
ATOM   491  C CG2 . VAL A 1 66  ? -0.56500  10.21100 -15.48500 1.000 21.23294 ? 65  VAL A CG2 1 
ATOM   492  N N   . HIS A 1 67  ? 0.70500   14.34100 -17.61600 1.000 24.47662 ? 66  HIS A N   1 
ATOM   493  C CA  . HIS A 1 67  ? 1.09000   15.04100 -18.84000 1.000 24.94196 ? 66  HIS A CA  1 
ATOM   494  C C   . HIS A 1 67  ? 2.19600   14.24600 -19.54600 1.000 24.86697 ? 66  HIS A C   1 
ATOM   495  O O   . HIS A 1 67  ? 3.28300   14.04100 -18.98800 1.000 27.78724 ? 66  HIS A O   1 
ATOM   496  C CB  . HIS A 1 67  ? 1.54400   16.47300 -18.53500 1.000 18.59776 ? 66  HIS A CB  1 
ATOM   497  C CG  . HIS A 1 67  ? 1.46200   17.38800 -19.71900 1.000 22.28624 ? 66  HIS A CG  1 
ATOM   498  N ND1 . HIS A 1 67  ? 1.67300   18.74800 -19.63100 1.000 20.34139 ? 66  HIS A ND1 1 
ATOM   499  C CD2 . HIS A 1 67  ? 1.20200   17.13100 -21.02500 1.000 22.28764 ? 66  HIS A CD2 1 
ATOM   500  C CE1 . HIS A 1 67  ? 1.54000   19.29000 -20.83000 1.000 19.69220 ? 66  HIS A CE1 1 
ATOM   501  N NE2 . HIS A 1 67  ? 1.26200   18.32900 -21.69500 1.000 21.14543 ? 66  HIS A NE2 1 
ATOM   502  N N   . GLY A 1 68  ? 1.91400   13.78400 -20.76000 1.000 25.05813 ? 67  GLY A N   1 
ATOM   503  C CA  . GLY A 1 68  ? 2.85200   12.99500 -21.52700 1.000 25.63402 ? 67  GLY A CA  1 
ATOM   504  C C   . GLY A 1 68  ? 3.38500   13.80000 -22.70800 1.000 24.69355 ? 67  GLY A C   1 
ATOM   505  O O   . GLY A 1 68  ? 2.61500   14.31000 -23.52700 1.000 23.82031 ? 67  GLY A O   1 
ATOM   506  N N   . LEU A 1 69  ? 4.70200   13.90100 -22.77100 1.000 22.94266 ? 68  LEU A N   1 
ATOM   507  C CA  . LEU A 1 69  ? 5.36400   14.72200 -23.77500 1.000 22.99176 ? 68  LEU A CA  1 
ATOM   508  C C   . LEU A 1 69  ? 6.09400   13.79500 -24.75200 1.000 25.88151 ? 68  LEU A C   1 
ATOM   509  O O   . LEU A 1 69  ? 7.07000   13.13600 -24.37500 1.000 28.81154 ? 68  LEU A O   1 
ATOM   510  C CB  . LEU A 1 69  ? 6.29500   15.72200 -23.08300 1.000 19.78682 ? 68  LEU A CB  1 
ATOM   511  C CG  . LEU A 1 69  ? 5.56700   16.81900 -22.28700 1.000 22.78485 ? 68  LEU A CG  1 
ATOM   512  C CD1 . LEU A 1 69  ? 6.19500   17.09700 -20.91900 1.000 25.71842 ? 68  LEU A CD1 1 
ATOM   513  C CD2 . LEU A 1 69  ? 5.47600   18.10200 -23.08100 1.000 25.11372 ? 68  LEU A CD2 1 
ATOM   514  N N   . HIS A 1 70  ? 5.60900   13.72900 -26.00100 1.000 24.45582 ? 69  HIS A N   1 
ATOM   515  C CA  . HIS A 1 70  ? 6.03400   12.72600 -26.97700 1.000 26.93109 ? 69  HIS A CA  1 
ATOM   516  C C   . HIS A 1 70  ? 6.62400   13.35900 -28.22600 1.000 25.58922 ? 69  HIS A C   1 
ATOM   517  O O   . HIS A 1 70  ? 6.33800   14.51400 -28.55600 1.000 28.13853 ? 69  HIS A O   1 
ATOM   518  C CB  . HIS A 1 70  ? 4.87300   11.83400 -27.45500 1.000 24.45022 ? 69  HIS A CB  1 
ATOM   519  C CG  . HIS A 1 70  ? 4.12500   11.14400 -26.36200 1.000 23.36297 ? 69  HIS A CG  1 
ATOM   520  N ND1 . HIS A 1 70  ? 3.04500   10.32800 -26.61400 1.000 29.23128 ? 69  HIS A ND1 1 
ATOM   521  C CD2 . HIS A 1 70  ? 4.28600   11.14800 -25.02000 1.000 27.10806 ? 69  HIS A CD2 1 
ATOM   522  C CE1 . HIS A 1 70  ? 2.57400   9.85200  -25.47500 1.000 27.11737 ? 69  HIS A CE1 1 
ATOM   523  N NE2 . HIS A 1 70  ? 3.31000   10.33500 -24.49200 1.000 30.74868 ? 69  HIS A NE2 1 
ATOM   524  N N   . ARG A 1 71  ? 7.41500   12.56400 -28.94600 1.000 24.06536 ? 70  ARG A N   1 
ATOM   525  C CA  . ARG A 1 71  ? 7.69800   12.86600 -30.34600 1.000 29.85218 ? 70  ARG A CA  1 
ATOM   526  C C   . ARG A 1 71  ? 6.43700   12.76600 -31.19700 1.000 24.27201 ? 70  ARG A C   1 
ATOM   527  O O   . ARG A 1 71  ? 5.60300   11.88900 -30.99600 1.000 23.82985 ? 70  ARG A O   1 
ATOM   528  C CB  . ARG A 1 71  ? 8.72900   11.90500 -30.92500 1.000 33.09960 ? 70  ARG A CB  1 
ATOM   529  C CG  . ARG A 1 71  ? 10.06200  11.92500 -30.28100 1.000 33.20876 ? 70  ARG A CG  1 
ATOM   530  C CD  . ARG A 1 71  ? 10.82400  10.72600 -30.75800 1.000 38.40877 ? 70  ARG A CD  1 
ATOM   531  N NE  . ARG A 1 71  ? 10.90300  9.70100  -29.72900 1.000 41.57286 ? 70  ARG A NE  1 
ATOM   532  C CZ  . ARG A 1 71  ? 11.29300  8.45100  -29.93600 1.000 43.61292 ? 70  ARG A CZ  1 
ATOM   533  N NH1 . ARG A 1 71  ? 11.66300  8.03300  -31.13500 1.000 41.67188 ? 70  ARG A NH1 1 
ATOM   534  N NH2 . ARG A 1 71  ? 11.33400  7.60600  -28.90700 1.000 43.62116 ? 70  ARG A NH2 1 
ATOM   535  N N   . GLU A 1 72  ? 6.32200   13.64800 -32.17900 1.000 25.45984 ? 71  GLU A N   1 
ATOM   536  C CA  . GLU A 1 72  ? 5.30200   13.48900 -33.20100 1.000 26.98512 ? 71  GLU A CA  1 
ATOM   537  C C   . GLU A 1 72  ? 5.57400   12.25600 -34.05600 1.000 27.06690 ? 71  GLU A C   1 
ATOM   538  O O   . GLU A 1 72  ? 6.72400   11.84200 -34.25400 1.000 30.05389 ? 71  GLU A O   1 
ATOM   539  C CB  . GLU A 1 72  ? 5.24700   14.71800 -34.10900 1.000 31.85872 ? 71  GLU A CB  1 
ATOM   540  C CG  . GLU A 1 72  ? 4.88900   16.02400 -33.40900 1.000 32.70373 ? 71  GLU A CG  1 
ATOM   541  C CD  . GLU A 1 72  ? 5.09300   17.21400 -34.31600 1.000 34.21427 ? 71  GLU A CD  1 
ATOM   542  O OE1 . GLU A 1 72  ? 5.53500   16.99000 -35.46600 1.000 31.16711 ? 71  GLU A OE1 1 
ATOM   543  O OE2 . GLU A 1 72  ? 4.80400   18.35600 -33.89000 1.000 37.49426 ? 71  GLU A OE2 1 
ATOM   544  N N   . GLY A 1 73  ? 4.49700   11.67900 -34.58500 1.000 22.96869 ? 72  GLY A N   1 
ATOM   545  C CA  . GLY A 1 73  ? 4.64500   10.64900 -35.59000 1.000 29.42710 ? 72  GLY A CA  1 
ATOM   546  C C   . GLY A 1 73  ? 3.81600   9.41100  -35.34600 1.000 33.98353 ? 72  GLY A C   1 
ATOM   547  O O   . GLY A 1 73  ? 3.79000   8.50500  -36.18500 1.000 33.21615 ? 72  GLY A O   1 
ATOM   548  N N   . ARG A 1 74  ? 3.12900   9.35600  -34.21200 1.000 31.57968 ? 73  ARG A N   1 
ATOM   549  C CA  . ARG A 1 74  ? 2.37400   8.17400  -33.83300 1.000 29.88113 ? 73  ARG A CA  1 
ATOM   550  C C   . ARG A 1 74  ? 0.89100   8.41800  -34.06400 1.000 28.66928 ? 73  ARG A C   1 
ATOM   551  O O   . ARG A 1 74  ? 0.39000   9.51600  -33.82400 1.000 30.42443 ? 73  ARG A O   1 
ATOM   552  C CB  . ARG A 1 74  ? 2.65300   7.81200  -32.37500 1.000 28.17589 ? 73  ARG A CB  1 
ATOM   553  C CG  . ARG A 1 74  ? 4.11500   7.48200  -32.15600 1.000 30.43153 ? 73  ARG A CG  1 
ATOM   554  C CD  . ARG A 1 74  ? 4.35000   6.60300  -30.93500 1.000 42.00439 ? 73  ARG A CD  1 
ATOM   555  N NE  . ARG A 1 74  ? 5.76800   6.57300  -30.57200 1.000 46.89817 ? 73  ARG A NE  1 
ATOM   556  C CZ  . ARG A 1 74  ? 6.35200   7.40600  -29.71600 1.000 44.71779 ? 73  ARG A CZ  1 
ATOM   557  N NH1 . ARG A 1 74  ? 5.66200   8.33200  -29.06000 1.000 31.74735 ? 73  ARG A NH1 1 
ATOM   558  N NH2 . ARG A 1 74  ? 7.66400   7.31300  -29.51800 1.000 40.79892 ? 73  ARG A NH2 1 
ATOM   559  N N   . SER A 1 75  ? 0.20000   7.39300  -34.54800 1.000 24.19133 ? 74  SER A N   1 
ATOM   560  C CA  . SER A 1 75  ? -1.19300  7.53500  -34.93700 1.000 23.24774 ? 74  SER A CA  1 
ATOM   561  C C   . SER A 1 75  ? -2.08200  7.83400  -33.73900 1.000 24.38089 ? 74  SER A C   1 
ATOM   562  O O   . SER A 1 75  ? -1.71800  7.60900  -32.58100 1.000 28.04769 ? 74  SER A O   1 
ATOM   563  C CB  . SER A 1 75  ? -1.69400  6.26200  -35.60300 1.000 22.78314 ? 74  SER A CB  1 
ATOM   564  O OG  . SER A 1 75  ? -1.70600  5.19100  -34.68100 1.000 12.98602 ? 74  SER A OG  1 
ATOM   565  N N   . ALA A 1 76  ? -3.28500  8.32200  -34.04300 1.000 24.02240 ? 75  ALA A N   1 
ATOM   566  C CA  . ALA A 1 76  ? -4.27100  8.58900  -33.00000 1.000 26.30442 ? 75  ALA A CA  1 
ATOM   567  C C   . ALA A 1 76  ? -4.72900  7.29900  -32.32700 1.000 28.59626 ? 75  ALA A C   1 
ATOM   568  O O   . ALA A 1 76  ? -4.92400  7.25800  -31.10400 1.000 32.12695 ? 75  ALA A O   1 
ATOM   569  C CB  . ALA A 1 76  ? -5.46600  9.33800  -33.59200 1.000 25.66882 ? 75  ALA A CB  1 
ATOM   570  N N   . ASP A 1 77  ? -4.91300  6.23800  -33.11100 1.000 32.65708 ? 76  ASP A N   1 
ATOM   571  C CA  . ASP A 1 77  ? -5.34200  4.96500  -32.54800 1.000 25.28592 ? 76  ASP A CA  1 
ATOM   572  C C   . ASP A 1 77  ? -4.32500  4.47100  -31.53300 1.000 26.70359 ? 76  ASP A C   1 
ATOM   573  O O   . ASP A 1 77  ? -4.69000  4.02600  -30.43900 1.000 24.71422 ? 76  ASP A O   1 
ATOM   574  C CB  . ASP A 1 77  ? -5.55400  3.96700  -33.69300 1.000 25.99733 ? 76  ASP A CB  1 
ATOM   575  C CG  . ASP A 1 77  ? -5.68000  2.51800  -33.23300 1.000 43.74222 ? 76  ASP A CG  1 
ATOM   576  O OD1 . ASP A 1 77  ? -6.43400  2.24900  -32.26600 1.000 44.90270 ? 76  ASP A OD1 1 
ATOM   577  O OD2 . ASP A 1 77  ? -5.05100  1.63800  -33.87100 1.000 42.57167 ? 76  ASP A OD2 1 
ATOM   578  N N   . LEU A 1 78  ? -3.03500  4.59800  -31.85800 1.000 25.72475 ? 77  LEU A N   1 
ATOM   579  C CA  . LEU A 1 78  ? -1.99300  4.22700  -30.90800 1.000 26.27174 ? 77  LEU A CA  1 
ATOM   580  C C   . LEU A 1 78  ? -2.06600  5.09300  -29.65500 1.000 27.31764 ? 77  LEU A C   1 
ATOM   581  O O   . LEU A 1 78  ? -2.12900  4.57900  -28.53600 1.000 23.33569 ? 77  LEU A O   1 
ATOM   582  C CB  . LEU A 1 78  ? -0.61100  4.34300  -31.55500 1.000 22.28583 ? 77  LEU A CB  1 
ATOM   583  C CG  . LEU A 1 78  ? 0.51300   3.68900  -30.73400 1.000 31.86072 ? 77  LEU A CG  1 
ATOM   584  C CD1 . LEU A 1 78  ? 1.10900   4.58400  -29.58900 1.000 20.37202 ? 77  LEU A CD1 1 
ATOM   585  C CD2 . LEU A 1 78  ? 0.00700   2.35900  -30.18700 1.000 28.22807 ? 77  LEU A CD2 1 
ATOM   586  N N   . LYS A 1 79  ? -2.03000  6.41800  -29.82800 1.000 28.63555 ? 78  LYS A N   1 
ATOM   587  C CA  . LYS A 1 79  ? -2.07300  7.30700  -28.68000 1.000 25.79754 ? 78  LYS A CA  1 
ATOM   588  C C   . LYS A 1 79  ? -3.30000  7.02800  -27.81300 1.000 29.84983 ? 78  LYS A C   1 
ATOM   589  O O   . LYS A 1 79  ? -3.21900  7.06900  -26.57400 1.000 26.26888 ? 78  LYS A O   1 
ATOM   590  C CB  . LYS A 1 79  ? -2.01800  8.75600  -29.15700 1.000 30.07649 ? 78  LYS A CB  1 
ATOM   591  C CG  . LYS A 1 79  ? -0.64600  9.13400  -29.75600 1.000 28.08394 ? 78  LYS A CG  1 
ATOM   592  C CD  . LYS A 1 79  ? -0.62400  10.57000 -30.24300 1.000 28.03280 ? 78  LYS A CD  1 
ATOM   593  C CE  . LYS A 1 79  ? -1.36200  10.71800 -31.57800 1.000 27.89886 ? 78  LYS A CE  1 
ATOM   594  N NZ  . LYS A 1 79  ? -1.34900  12.12900 -32.05200 1.000 25.04836 ? 78  LYS A NZ  1 
ATOM   595  N N   . GLY A 1 80  ? -4.42500  6.67100  -28.43900 1.000 23.54942 ? 79  GLY A N   1 
ATOM   596  C CA  . GLY A 1 80  ? -5.59100  6.27300  -27.66200 1.000 26.41586 ? 79  GLY A CA  1 
ATOM   597  C C   . GLY A 1 80  ? -5.33600  5.03200  -26.82400 1.000 28.24229 ? 79  GLY A C   1 
ATOM   598  O O   . GLY A 1 80  ? -5.63900  4.99300  -25.62400 1.000 31.06727 ? 79  GLY A O   1 
ATOM   599  N N   . GLN A 1 81  ? -4.76200  4.00200  -27.44000 1.000 25.51954 ? 80  GLN A N   1 
ATOM   600  C CA  . GLN A 1 81  ? -4.44800  2.79000  -26.69700 1.000 27.00226 ? 80  GLN A CA  1 
ATOM   601  C C   . GLN A 1 81  ? -3.57400  3.10100  -25.48600 1.000 27.29538 ? 80  GLN A C   1 
ATOM   602  O O   . GLN A 1 81  ? -3.92100  2.76900  -24.34500 1.000 26.07563 ? 80  GLN A O   1 
ATOM   603  C CB  . GLN A 1 81  ? -3.77500  1.78800  -27.62600 1.000 24.76726 ? 80  GLN A CB  1 
ATOM   604  C CG  . GLN A 1 81  ? -4.75800  0.84300  -28.28900 1.000 35.44879 ? 80  GLN A CG  1 
ATOM   605  C CD  . GLN A 1 81  ? -4.08000  -0.19400 -29.16300 1.000 43.74755 ? 80  GLN A CD  1 
ATOM   606  O OE1 . GLN A 1 81  ? -3.95000  -0.01700 -30.38100 1.000 44.48231 ? 80  GLN A OE1 1 
ATOM   607  N NE2 . GLN A 1 81  ? -3.62800  -1.28600 -28.53900 1.000 40.11140 ? 80  GLN A NE2 1 
ATOM   608  N N   . LEU A 1 82  ? -2.45700  3.79500  -25.71100 1.000 30.54547 ? 81  LEU A N   1 
ATOM   609  C CA  . LEU A 1 82  ? -1.50100  4.05100  -24.63800 1.000 26.11564 ? 81  LEU A CA  1 
ATOM   610  C C   . LEU A 1 82  ? -2.09800  4.91300  -23.53000 1.000 27.47071 ? 81  LEU A C   1 
ATOM   611  O O   . LEU A 1 82  ? -1.73700  4.74600  -22.36100 1.000 30.33391 ? 81  LEU A O   1 
ATOM   612  C CB  . LEU A 1 82  ? -0.25300  4.69400  -25.22700 1.000 25.69851 ? 81  LEU A CB  1 
ATOM   613  C CG  . LEU A 1 82  ? 0.82000   5.28500  -24.33100 1.000 24.44743 ? 81  LEU A CG  1 
ATOM   614  C CD1 . LEU A 1 82  ? 1.37100   4.26500  -23.36100 1.000 27.32068 ? 81  LEU A CD1 1 
ATOM   615  C CD2 . LEU A 1 82  ? 1.90200   5.83600  -25.22600 1.000 26.13299 ? 81  LEU A CD2 1 
ATOM   616  N N   . ALA A 1 83  ? -3.00700  5.83300  -23.86300 1.000 28.67999 ? 82  ALA A N   1 
ATOM   617  C CA  . ALA A 1 83  ? -3.63500  6.62300  -22.81100 1.000 28.02764 ? 82  ALA A CA  1 
ATOM   618  C C   . ALA A 1 83  ? -4.59600  5.77100  -22.00400 1.000 26.89157 ? 82  ALA A C   1 
ATOM   619  O O   . ALA A 1 83  ? -4.65300  5.88200  -20.77400 1.000 25.76111 ? 82  ALA A O   1 
ATOM   620  C CB  . ALA A 1 83  ? -4.35800  7.83700  -23.39900 1.000 26.65330 ? 82  ALA A CB  1 
ATOM   621  N N   . GLN A 1 84  ? -5.34700  4.89700  -22.68000 1.000 30.84006 ? 83  GLN A N   1 
ATOM   622  C CA  . GLN A 1 84  ? -6.29400  4.04200  -21.97000 1.000 28.26051 ? 83  GLN A CA  1 
ATOM   623  C C   . GLN A 1 84  ? -5.57300  3.06400  -21.05800 1.000 29.78430 ? 83  GLN A C   1 
ATOM   624  O O   . GLN A 1 84  ? -6.03500  2.77900  -19.94500 1.000 31.80896 ? 83  GLN A O   1 
ATOM   625  C CB  . GLN A 1 84  ? -7.16600  3.28000  -22.95500 1.000 24.22002 ? 83  GLN A CB  1 
ATOM   626  C CG  . GLN A 1 84  ? -8.11800  2.34300  -22.25300 1.000 28.95210 ? 83  GLN A CG  1 
ATOM   627  C CD  . GLN A 1 84  ? -9.12500  3.09700  -21.41300 1.000 30.06120 ? 83  GLN A CD  1 
ATOM   628  O OE1 . GLN A 1 84  ? -9.96600  3.82200  -21.93900 1.000 32.53839 ? 83  GLN A OE1 1 
ATOM   629  N NE2 . GLN A 1 84  ? -9.03500  2.94400  -20.10100 1.000 31.12882 ? 83  GLN A NE2 1 
ATOM   630  N N   . ARG A 1 85  ? -4.43000  2.54800  -21.51600 1.000 25.71460 ? 84  ARG A N   1 
ATOM   631  C CA  . ARG A 1 85  ? -3.67800  1.59200  -20.72700 1.000 26.05626 ? 84  ARG A CA  1 
ATOM   632  C C   . ARG A 1 85  ? -2.92700  2.28100  -19.58800 1.000 28.02651 ? 84  ARG A C   1 
ATOM   633  O O   . ARG A 1 85  ? -2.72700  1.67900  -18.52800 1.000 23.63185 ? 84  ARG A O   1 
ATOM   634  C CB  . ARG A 1 85  ? -2.74300  0.82200  -21.64700 1.000 25.36551 ? 84  ARG A CB  1 
ATOM   635  C CG  . ARG A 1 85  ? -2.16500  -0.43300 -21.03400 1.000 42.38984 ? 84  ARG A CG  1 
ATOM   636  C CD  . ARG A 1 85  ? -0.82400  -0.70400 -21.66100 1.000 41.75700 ? 84  ARG A CD  1 
ATOM   637  N NE  . ARG A 1 85  ? 0.14000   -1.24700 -20.71000 1.000 53.42763 ? 84  ARG A NE  1 
ATOM   638  C CZ  . ARG A 1 85  ? 0.93000   -2.28700 -20.94600 1.000 55.16035 ? 84  ARG A CZ  1 
ATOM   639  N NH1 . ARG A 1 85  ? 0.86100   -2.96300 -22.08400 1.000 55.58253 ? 84  ARG A NH1 1 
ATOM   640  N NH2 . ARG A 1 85  ? 1.84000   -2.63200 -20.03300 1.000 50.11226 ? 84  ARG A NH2 1 
ATOM   641  N N   . ILE A 1 86  ? -2.53100  3.54400  -19.77000 1.000 26.61338 ? 85  ILE A N   1 
ATOM   642  C CA  . ILE A 1 86  ? -1.97500  4.29700  -18.65500 1.000 26.73925 ? 85  ILE A CA  1 
ATOM   643  C C   . ILE A 1 86  ? -3.03100  4.47800  -17.58400 1.000 29.90201 ? 85  ILE A C   1 
ATOM   644  O O   . ILE A 1 86  ? -2.75700  4.34800  -16.38400 1.000 31.78131 ? 85  ILE A O   1 
ATOM   645  C CB  . ILE A 1 86  ? -1.42100  5.65200  -19.13000 1.000 30.36363 ? 85  ILE A CB  1 
ATOM   646  C CG1 . ILE A 1 86  ? -0.06800  5.46100  -19.82400 1.000 30.89288 ? 85  ILE A CG1 1 
ATOM   647  C CG2 . ILE A 1 86  ? -1.27000  6.62100  -17.94900 1.000 22.58856 ? 85  ILE A CG2 1 
ATOM   648  C CD1 . ILE A 1 86  ? 0.28800   6.56800  -20.78900 1.000 26.34461 ? 85  ILE A CD1 1 
ATOM   649  N N   . VAL A 1 87  ? -4.26100  4.76800  -18.00300 1.000 29.81456 ? 86  VAL A N   1 
ATOM   650  C CA  . VAL A 1 87  ? -5.34000  4.99700  -17.05100 1.000 31.69377 ? 86  VAL A CA  1 
ATOM   651  C C   . VAL A 1 87  ? -5.60600  3.73800  -16.23200 1.000 35.98763 ? 86  VAL A C   1 
ATOM   652  O O   . VAL A 1 87  ? -5.70300  3.78500  -14.99800 1.000 30.71680 ? 86  VAL A O   1 
ATOM   653  C CB  . VAL A 1 87  ? -6.59800  5.47000  -17.79100 1.000 24.86473 ? 86  VAL A CB  1 
ATOM   654  C CG1 . VAL A 1 87  ? -7.79700  5.44400  -16.85000 1.000 32.44917 ? 86  VAL A CG1 1 
ATOM   655  C CG2 . VAL A 1 87  ? -6.36500  6.84300  -18.32000 1.000 26.96880 ? 86  VAL A CG2 1 
ATOM   656  N N   . ASP A 1 88  ? -5.71700  2.58900  -16.91200 1.000 32.30089 ? 87  ASP A N   1 
ATOM   657  C CA  . ASP A 1 88  ? -5.93200  1.31900  -16.22200 1.000 34.78535 ? 87  ASP A CA  1 
ATOM   658  C C   . ASP A 1 88  ? -4.71500  0.91800  -15.39000 1.000 33.45990 ? 87  ASP A C   1 
ATOM   659  O O   . ASP A 1 88  ? -4.83600  0.60800  -14.19700 1.000 35.16428 ? 87  ASP A O   1 
ATOM   660  C CB  . ASP A 1 88  ? -6.25100  0.22400  -17.23600 1.000 37.33232 ? 87  ASP A CB  1 
ATOM   661  C CG  . ASP A 1 88  ? -7.52400  0.49400  -17.99900 1.000 34.90172 ? 87  ASP A CG  1 
ATOM   662  O OD1 . ASP A 1 88  ? -8.41000  1.17300  -17.44600 1.000 34.64439 ? 87  ASP A OD1 1 
ATOM   663  O OD2 . ASP A 1 88  ? -7.62900  0.02500  -19.15100 1.000 38.18611 ? 87  ASP A OD2 1 
ATOM   664  N N   . ASP A 1 89  ? -3.53200  0.90500  -15.99900 1.000 28.85618 ? 88  ASP A N   1 
ATOM   665  C CA  . ASP A 1 89  ? -2.38300  0.39400  -15.26800 1.000 28.87980 ? 88  ASP A CA  1 
ATOM   666  C C   . ASP A 1 89  ? -1.95400  1.32400  -14.13400 1.000 31.46471 ? 88  ASP A C   1 
ATOM   667  O O   . ASP A 1 89  ? -1.51900  0.83700  -13.08500 1.000 30.66342 ? 88  ASP A O   1 
ATOM   668  C CB  . ASP A 1 89  ? -1.24400  0.10200  -16.23600 1.000 30.29574 ? 88  ASP A CB  1 
ATOM   669  C CG  . ASP A 1 89  ? -1.55400  -1.10900 -17.13000 1.000 36.02430 ? 88  ASP A CG  1 
ATOM   670  O OD1 . ASP A 1 89  ? -2.61700  -1.71800 -16.89800 1.000 30.23037 ? 88  ASP A OD1 1 
ATOM   671  O OD2 . ASP A 1 89  ? -0.76900  -1.44300 -18.05800 1.000 35.29592 ? 88  ASP A OD2 1 
ATOM   672  N N   . VAL A 1 90  ? -2.09200  2.64400  -14.28900 1.000 30.17057 ? 89  VAL A N   1 
ATOM   673  C CA  . VAL A 1 90  ? -1.83000  3.51600  -13.14400 1.000 31.29050 ? 89  VAL A CA  1 
ATOM   674  C C   . VAL A 1 90  ? -2.88900  3.30800  -12.06600 1.000 31.22120 ? 89  VAL A C   1 
ATOM   675  O O   . VAL A 1 90  ? -2.58000  3.28500  -10.86900 1.000 34.32874 ? 89  VAL A O   1 
ATOM   676  C CB  . VAL A 1 90  ? -1.73200  4.98900  -13.58000 1.000 32.18343 ? 89  VAL A CB  1 
ATOM   677  C CG1 . VAL A 1 90  ? -1.67000  5.90200  -12.36300 1.000 27.20614 ? 89  VAL A CG1 1 
ATOM   678  C CG2 . VAL A 1 90  ? -0.48900  5.19300  -14.44600 1.000 29.14529 ? 89  VAL A CG2 1 
ATOM   679  N N   . SER A 1 91  ? -4.14800  3.12500  -12.47000 1.000 34.08557 ? 90  SER A N   1 
ATOM   680  C CA  . SER A 1 91  ? -5.22100  2.88000  -11.50900 1.000 31.62896 ? 90  SER A CA  1 
ATOM   681  C C   . SER A 1 91  ? -4.90900  1.69100  -10.61400 1.000 34.18520 ? 90  SER A C   1 
ATOM   682  O O   . SER A 1 91  ? -4.98500  1.79200  -9.38500  1.000 37.46298 ? 90  SER A O   1 
ATOM   683  C CB  . SER A 1 91  ? -6.53700  2.65100  -12.24100 1.000 34.65822 ? 90  SER A CB  1 
ATOM   684  O OG  . SER A 1 91  ? -7.44900  1.96200  -11.41400 1.000 38.85890 ? 90  SER A OG  1 
ATOM   685  N N   . VAL A 1 92  ? -4.57800  0.54700  -11.21300 1.000 28.95344 ? 91  VAL A N   1 
ATOM   686  C CA  . VAL A 1 92  ? -4.19300  -0.61400 -10.41700 1.000 28.29817 ? 91  VAL A CA  1 
ATOM   687  C C   . VAL A 1 92  ? -3.03900  -0.26000 -9.49000  1.000 31.19605 ? 91  VAL A C   1 
ATOM   688  O O   . VAL A 1 92  ? -3.11000  -0.47100 -8.27300  1.000 35.45361 ? 91  VAL A O   1 
ATOM   689  C CB  . VAL A 1 92  ? -3.81900  -1.80300 -11.32300 1.000 32.89156 ? 91  VAL A CB  1 
ATOM   690  C CG1 . VAL A 1 92  ? -3.72500  -3.06000 -10.49800 1.000 33.60187 ? 91  VAL A CG1 1 
ATOM   691  C CG2 . VAL A 1 92  ? -4.81100  -1.98900 -12.46600 1.000 29.31420 ? 91  VAL A CG2 1 
ATOM   692  N N   . ALA A 1 93  ? -1.96700  0.30900  -10.05900 1.000 31.40716 ? 92  ALA A N   1 
ATOM   693  C CA  . ALA A 1 93  ? -0.68500  0.48000  -9.37700  1.000 25.72653 ? 92  ALA A CA  1 
ATOM   694  C C   . ALA A 1 93  ? -0.69500  1.58000  -8.31900  1.000 35.80744 ? 92  ALA A C   1 
ATOM   695  O O   . ALA A 1 93  ? 0.14700   1.56400  -7.42000  1.000 36.04606 ? 92  ALA A O   1 
ATOM   696  C CB  . ALA A 1 93  ? 0.40500   0.79000  -10.40000 1.000 30.00978 ? 92  ALA A CB  1 
ATOM   697  N N   . ALA A 1 94  ? -1.58900  2.55400  -8.41800  1.000 33.76345 ? 93  ALA A N   1 
ATOM   698  C CA  . ALA A 1 94  ? -1.70400  3.57400  -7.39600  1.000 32.35159 ? 93  ALA A CA  1 
ATOM   699  C C   . ALA A 1 94  ? -2.88300  3.32200  -6.48100  1.000 34.37839 ? 93  ALA A C   1 
ATOM   700  O O   . ALA A 1 94  ? -3.19900  4.18000  -5.64700  1.000 32.91152 ? 93  ALA A O   1 
ATOM   701  C CB  . ALA A 1 94  ? -1.81800  4.95600  -8.03600  1.000 37.48764 ? 93  ALA A CB  1 
ATOM   702  N N   . GLU A 1 95  ? -3.52300  2.15600  -6.61200  1.000 32.06083 ? 94  GLU A N   1 
ATOM   703  C CA  . GLU A 1 95  ? -4.75500  1.82200  -5.90400  1.000 34.79913 ? 94  GLU A CA  1 
ATOM   704  C C   . GLU A 1 95  ? -5.67900  3.03300  -5.90200  1.000 32.93294 ? 94  GLU A C   1 
ATOM   705  O O   . GLU A 1 95  ? -5.91400  3.64800  -4.85900  1.000 34.65178 ? 94  GLU A O   1 
ATOM   706  C CB  . GLU A 1 95  ? -4.44800  1.35200  -4.47900  1.000 39.16795 ? 94  GLU A CB  1 
ATOM   707  C CG  . GLU A 1 95  ? -3.87200  -0.06400 -4.37400  1.000 40.61477 ? 94  GLU A CG  1 
ATOM   708  C CD  . GLU A 1 95  ? -2.90100  -0.22700 -3.18800  1.000 50.38769 ? 94  GLU A CD  1 
ATOM   709  O OE1 . GLU A 1 95  ? -2.12100  0.71200  -2.90200  1.000 50.92188 ? 94  GLU A OE1 1 
ATOM   710  O OE2 . GLU A 1 95  ? -2.91700  -1.29700 -2.54200  1.000 43.61209 ? 94  GLU A OE2 1 
ATOM   711  N N   . ILE A 1 96  ? -6.16900  3.40600  -7.07800  1.000 38.26582 ? 95  ILE A N   1 
ATOM   712  C CA  . ILE A 1 96  ? -6.86300  4.67400  -7.27500  1.000 42.49909 ? 95  ILE A CA  1 
ATOM   713  C C   . ILE A 1 96  ? -7.91300  4.46900  -8.36600  1.000 42.82292 ? 95  ILE A C   1 
ATOM   714  O O   . ILE A 1 96  ? -7.64800  3.83600  -9.39400  1.000 43.39686 ? 95  ILE A O   1 
ATOM   715  C CB  . ILE A 1 96  ? -5.85200  5.79900  -7.61900  1.000 38.81774 ? 95  ILE A CB  1 
ATOM   716  C CG1 . ILE A 1 96  ? -6.51700  7.17100  -7.75700  1.000 39.33135 ? 95  ILE A CG1 1 
ATOM   717  C CG2 . ILE A 1 96  ? -5.14300  5.49200  -8.91300  1.000 41.54309 ? 95  ILE A CG2 1 
ATOM   718  C CD1 . ILE A 1 96  ? -7.52500  7.47700  -6.70700  1.000 41.59570 ? 95  ILE A CD1 1 
ATOM   719  N N   . ASP A 1 97  ? -9.11500  4.99200  -8.12000  1.000 39.28773 ? 96  ASP A N   1 
ATOM   720  C CA  . ASP A 1 97  ? -10.23400 4.84900  -9.04800  1.000 41.73790 ? 96  ASP A CA  1 
ATOM   721  C C   . ASP A 1 97  ? -10.00600 5.62600  -10.35000 1.000 41.89965 ? 96  ASP A C   1 
ATOM   722  O O   . ASP A 1 97  ? -9.39800  6.70700  -10.36900 1.000 36.14016 ? 96  ASP A O   1 
ATOM   723  C CB  . ASP A 1 97  ? -11.52700 5.32200  -8.37800  1.000 41.38533 ? 96  ASP A CB  1 
ATOM   724  C CG  . ASP A 1 97  ? -12.77800 4.87000  -9.11500  1.000 53.37435 ? 96  ASP A CG  1 
ATOM   725  O OD1 . ASP A 1 97  ? -12.66800 4.40700  -10.27200 1.000 52.78829 ? 96  ASP A OD1 1 
ATOM   726  O OD2 . ASP A 1 97  ? -13.88300 4.98300  -8.52900  1.000 58.28181 ? 96  ASP A OD2 1 
ATOM   727  N N   . ARG A 1 98  ? -10.55700 5.07400  -11.44000 1.000 45.97387 ? 97  ARG A N   1 
ATOM   728  C CA  . ARG A 1 98  ? -10.26000 5.56200  -12.78600 1.000 36.92290 ? 97  ARG A CA  1 
ATOM   729  C C   . ARG A 1 98  ? -10.75300 6.98500  -12.99800 1.000 34.74925 ? 97  ARG A C   1 
ATOM   730  O O   . ARG A 1 98  ? -10.06800 7.79500  -13.63400 1.000 36.58118 ? 97  ARG A O   1 
ATOM   731  C CB  . ARG A 1 98  ? -10.85800 4.60900  -13.82100 1.000 39.40014 ? 97  ARG A CB  1 
ATOM   732  C CG  . ARG A 1 98  ? -9.93500  3.42600  -14.12700 1.000 47.81498 ? 97  ARG A CG  1 
ATOM   733  C CD  . ARG A 1 98  ? -10.69800 2.13800  -14.37500 1.000 48.52092 ? 97  ARG A CD  1 
ATOM   734  N NE  . ARG A 1 98  ? -10.80600 1.84000  -15.79700 1.000 47.63745 ? 97  ARG A NE  1 
ATOM   735  C CZ  . ARG A 1 98  ? -11.10200 0.64300  -16.28700 1.000 58.87936 ? 97  ARG A CZ  1 
ATOM   736  N NH1 . ARG A 1 98  ? -11.32100 -0.39400 -15.49100 1.000 58.76018 ? 97  ARG A NH1 1 
ATOM   737  N NH2 . ARG A 1 98  ? -11.18500 0.48300  -17.60900 1.000 56.93682 ? 97  ARG A NH2 1 
ATOM   738  N N   . LYS A 1 99  ? -11.93300 7.31300  -12.46900 1.000 35.15904 ? 98  LYS A N   1 
ATOM   739  C CA  . LYS A 1 99  ? -12.45000 8.67900  -12.52200 1.000 34.60598 ? 98  LYS A CA  1 
ATOM   740  C C   . LYS A 1 99  ? -11.46400 9.71800  -11.97800 1.000 39.72229 ? 98  LYS A C   1 
ATOM   741  O O   . LYS A 1 99  ? -11.61000 10.91300 -12.27400 1.000 38.68322 ? 98  LYS A O   1 
ATOM   742  C CB  . LYS A 1 99  ? -13.74600 8.75000  -11.71900 1.000 35.23887 ? 98  LYS A CB  1 
ATOM   743  C CG  . LYS A 1 99  ? -13.49200 8.69500  -10.21000 1.000 37.36888 ? 98  LYS A CG  1 
ATOM   744  C CD  . LYS A 1 99  ? -14.73900 8.40500  -9.39200  1.000 36.84762 ? 98  LYS A CD  1 
ATOM   745  C CE  . LYS A 1 99  ? -14.38700 8.40500  -7.91800  1.000 38.30039 ? 98  LYS A CE  1 
ATOM   746  N NZ  . LYS A 1 99  ? -15.45400 7.83500  -7.06000  1.000 47.76499 ? 98  LYS A NZ  1 
ATOM   747  N N   . HIS A 1 100 ? -10.47400 9.30300  -11.18000 1.000 30.88528 ? 99  HIS A N   1 
ATOM   748  C CA  . HIS A 1 100 ? -9.52200  10.23800 -10.60100 1.000 36.89168 ? 99  HIS A CA  1 
ATOM   749  C C   . HIS A 1 100 ? -8.32200  10.51600 -11.49500 1.000 33.51072 ? 99  HIS A C   1 
ATOM   750  O O   . HIS A 1 100 ? -7.46200  11.31600 -11.10600 1.000 34.58284 ? 99  HIS A O   1 
ATOM   751  C CB  . HIS A 1 100 ? -9.01000  9.72500  -9.25700  1.000 33.20892 ? 99  HIS A CB  1 
ATOM   752  C CG  . HIS A 1 100 ? -9.97400  9.91000  -8.13700  1.000 31.98219 ? 99  HIS A CG  1 
ATOM   753  N ND1 . HIS A 1 100 ? -10.34700 8.87900  -7.29900  1.000 33.53046 ? 99  HIS A ND1 1 
ATOM   754  C CD2 . HIS A 1 100 ? -10.64900 11.00300 -7.71600  1.000 31.82638 ? 99  HIS A CD2 1 
ATOM   755  C CE1 . HIS A 1 100 ? -11.21700 9.33100  -6.41500  1.000 36.86885 ? 99  HIS A CE1 1 
ATOM   756  N NE2 . HIS A 1 100 ? -11.41700 10.61700 -6.64400  1.000 37.00981 ? 99  HIS A NE2 1 
ATOM   757  N N   . ILE A 1 101 ? -8.22900  9.87800  -12.65800 1.000 29.58311 ? 100 ILE A N   1 
ATOM   758  C CA  . ILE A 1 101 ? -7.01600  9.89600  -13.47100 1.000 28.05340 ? 100 ILE A CA  1 
ATOM   759  C C   . ILE A 1 101 ? -7.28500  10.71100 -14.72500 1.000 27.18891 ? 100 ILE A C   1 
ATOM   760  O O   . ILE A 1 101 ? -8.21400  10.41200 -15.48900 1.000 25.13785 ? 100 ILE A O   1 
ATOM   761  C CB  . ILE A 1 101 ? -6.54500  8.47300  -13.81800 1.000 32.55517 ? 100 ILE A CB  1 
ATOM   762  C CG1 . ILE A 1 101 ? -6.08100  7.74200  -12.55400 1.000 31.28697 ? 100 ILE A CG1 1 
ATOM   763  C CG2 . ILE A 1 101 ? -5.42600  8.50000  -14.85600 1.000 24.58857 ? 100 ILE A CG2 1 
ATOM   764  C CD1 . ILE A 1 101 ? -6.70800  6.36700  -12.35300 1.000 31.21104 ? 100 ILE A CD1 1 
ATOM   765  N N   . TRP A 1 102 ? -6.47100  11.74200 -14.93400 1.000 32.94056 ? 101 TRP A N   1 
ATOM   766  C CA  . TRP A 1 102 ? -6.48800  12.54400 -16.15400 1.000 27.80975 ? 101 TRP A CA  1 
ATOM   767  C C   . TRP A 1 102 ? -5.16800  12.35800 -16.90000 1.000 23.55827 ? 101 TRP A C   1 
ATOM   768  O O   . TRP A 1 102 ? -4.10900  12.25200 -16.27500 1.000 20.78367 ? 101 TRP A O   1 
ATOM   769  C CB  . TRP A 1 102 ? -6.71000  14.02600 -15.84000 1.000 26.75951 ? 101 TRP A CB  1 
ATOM   770  C CG  . TRP A 1 102 ? -7.93500  14.32400 -15.02300 1.000 25.89056 ? 101 TRP A CG  1 
ATOM   771  C CD1 . TRP A 1 102 ? -8.50000  13.54100 -14.05300 1.000 23.22567 ? 101 TRP A CD1 1 
ATOM   772  C CD2 . TRP A 1 102 ? -8.73600  15.50800 -15.09500 1.000 25.79146 ? 101 TRP A CD2 1 
ATOM   773  N NE1 . TRP A 1 102 ? -9.61500  14.15700 -13.53500 1.000 24.95110 ? 101 TRP A NE1 1 
ATOM   774  C CE2 . TRP A 1 102 ? -9.77300  15.37100 -14.15000 1.000 24.87190 ? 101 TRP A CE2 1 
ATOM   775  C CE3 . TRP A 1 102 ? -8.67300  16.67400 -15.86100 1.000 24.90903 ? 101 TRP A CE3 1 
ATOM   776  C CZ2 . TRP A 1 102 ? -10.73500 16.35500 -13.95400 1.000 27.78322 ? 101 TRP A CZ2 1 
ATOM   777  C CZ3 . TRP A 1 102 ? -9.63800  17.65100 -15.67200 1.000 25.71502 ? 101 TRP A CZ3 1 
ATOM   778  C CH2 . TRP A 1 102 ? -10.65000 17.48900 -14.72400 1.000 30.36925 ? 101 TRP A CH2 1 
ATOM   779  N N   . VAL A 1 103 ? -5.23800  12.30900 -18.23500 1.000 24.14963 ? 102 VAL A N   1 
ATOM   780  C CA  . VAL A 1 103 ? -4.10900  11.93600 -19.08900 1.000 21.21983 ? 102 VAL A CA  1 
ATOM   781  C C   . VAL A 1 103 ? -4.13600  12.77500 -20.35700 1.000 24.12509 ? 102 VAL A C   1 
ATOM   782  O O   . VAL A 1 103 ? -4.94300  12.51300 -21.25300 1.000 23.90947 ? 102 VAL A O   1 
ATOM   783  C CB  . VAL A 1 103 ? -4.13300  10.45000 -19.45600 1.000 24.48208 ? 102 VAL A CB  1 
ATOM   784  C CG1 . VAL A 1 103 ? -3.06500  10.15000 -20.50500 1.000 24.55531 ? 102 VAL A CG1 1 
ATOM   785  C CG2 . VAL A 1 103 ? -3.93100  9.59500  -18.21800 1.000 28.66490 ? 102 VAL A CG2 1 
ATOM   786  N N   . TYR A 1 104 ? -3.24100  13.76200 -20.45200 1.000 27.59988 ? 103 TYR A N   1 
ATOM   787  C CA  . TYR A 1 104 ? -3.04900  14.54200 -21.66900 1.000 24.24785 ? 103 TYR A CA  1 
ATOM   788  C C   . TYR A 1 104 ? -1.74100  14.13900 -22.33400 1.000 24.98210 ? 103 TYR A C   1 
ATOM   789  O O   . TYR A 1 104 ? -0.73400  13.92900 -21.65200 1.000 26.77756 ? 103 TYR A O   1 
ATOM   790  C CB  . TYR A 1 104 ? -2.99500  16.04900 -21.38700 1.000 27.94128 ? 103 TYR A CB  1 
ATOM   791  C CG  . TYR A 1 104 ? -4.29100  16.70400 -20.95000 1.000 26.22507 ? 103 TYR A CG  1 
ATOM   792  C CD1 . TYR A 1 104 ? -5.47200  15.97200 -20.81600 1.000 27.78773 ? 103 TYR A CD1 1 
ATOM   793  C CD2 . TYR A 1 104 ? -4.32300  18.05600 -20.64700 1.000 22.52396 ? 103 TYR A CD2 1 
ATOM   794  C CE1 . TYR A 1 104 ? -6.65800  16.58600 -20.39600 1.000 25.72574 ? 103 TYR A CE1 1 
ATOM   795  C CE2 . TYR A 1 104 ? -5.48900  18.67100 -20.22700 1.000 24.83192 ? 103 TYR A CE2 1 
ATOM   796  C CZ  . TYR A 1 104 ? -6.65500  17.93500 -20.10800 1.000 24.01864 ? 103 TYR A CZ  1 
ATOM   797  O OH  . TYR A 1 104 ? -7.80900  18.56800 -19.70200 1.000 23.86464 ? 103 TYR A OH  1 
ATOM   798  N N   . PHE A 1 105 ? -1.73800  14.08100 -23.66400 1.000 24.64750 ? 104 PHE A N   1 
ATOM   799  C CA  . PHE A 1 105 ? -0.51900  13.85800 -24.43600 1.000 22.92137 ? 104 PHE A CA  1 
ATOM   800  C C   . PHE A 1 105 ? -0.21900  15.07200 -25.30500 1.000 19.46167 ? 104 PHE A C   1 
ATOM   801  O O   . PHE A 1 105 ? -1.09100  15.54400 -26.03200 1.000 24.90055 ? 104 PHE A O   1 
ATOM   802  C CB  . PHE A 1 105 ? -0.63800  12.61300 -25.31700 1.000 25.59075 ? 104 PHE A CB  1 
ATOM   803  C CG  . PHE A 1 105 ? -0.60700  11.31100 -24.55200 1.000 31.44245 ? 104 PHE A CG  1 
ATOM   804  C CD1 . PHE A 1 105 ? 0.03300   11.22000 -23.32200 1.000 26.66228 ? 104 PHE A CD1 1 
ATOM   805  C CD2 . PHE A 1 105 ? -1.21900  10.17300 -25.06700 1.000 32.03942 ? 104 PHE A CD2 1 
ATOM   806  C CE1 . PHE A 1 105 ? 0.05600   10.01800 -22.61400 1.000 23.92895 ? 104 PHE A CE1 1 
ATOM   807  C CE2 . PHE A 1 105 ? -1.19500  8.98000  -24.36800 1.000 29.81756 ? 104 PHE A CE2 1 
ATOM   808  C CZ  . PHE A 1 105 ? -0.55300  8.90700  -23.13700 1.000 27.18052 ? 104 PHE A CZ  1 
ATOM   809  N N   . GLY A 1 106 ? 1.02100   15.55800 -25.25000 1.000 21.03759 ? 105 GLY A N   1 
ATOM   810  C CA  . GLY A 1 106 ? 1.50800   16.58500 -26.16000 1.000 22.42509 ? 105 GLY A CA  1 
ATOM   811  C C   . GLY A 1 106 ? 2.58900   16.05400 -27.08800 1.000 20.00344 ? 105 GLY A C   1 
ATOM   812  O O   . GLY A 1 106 ? 3.35100   15.16000 -26.72500 1.000 21.40059 ? 105 GLY A O   1 
ATOM   813  N N   . GLU A 1 107 ? 2.65900   16.61200 -28.29000 1.000 18.71067 ? 106 GLU A N   1 
ATOM   814  C CA  . GLU A 1 107 ? 3.56700   16.12700 -29.31700 1.000 20.86558 ? 106 GLU A CA  1 
ATOM   815  C C   . GLU A 1 107 ? 4.42300   17.28100 -29.82300 1.000 28.47632 ? 106 GLU A C   1 
ATOM   816  O O   . GLU A 1 107 ? 3.90000   18.35300 -30.15100 1.000 26.09151 ? 106 GLU A O   1 
ATOM   817  C CB  . GLU A 1 107 ? 2.79200   15.49100 -30.49500 1.000 23.02130 ? 106 GLU A CB  1 
ATOM   818  C CG  . GLU A 1 107 ? 2.01200   14.21800 -30.15800 1.000 26.07450 ? 106 GLU A CG  1 
ATOM   819  C CD  . GLU A 1 107 ? 0.97400   13.83600 -31.22800 1.000 26.70741 ? 106 GLU A CD  1 
ATOM   820  O OE1 . GLU A 1 107 ? -0.12000  14.42600 -31.25100 1.000 24.47154 ? 106 GLU A OE1 1 
ATOM   821  O OE2 . GLU A 1 107 ? 1.23200   12.92300 -32.03800 1.000 28.11205 ? 106 GLU A OE2 1 
ATOM   822  N N   . MET A 1 108 ? 5.72700   17.05700 -29.90000 1.000 24.74596 ? 107 MET A N   1 
ATOM   823  C CA  . MET A 1 108 ? 6.65700   17.97600 -30.53000 1.000 24.28773 ? 107 MET A CA  1 
ATOM   824  C C   . MET A 1 108 ? 7.45000   17.22800 -31.58500 1.000 30.98517 ? 107 MET A C   1 
ATOM   825  O O   . MET A 1 108 ? 7.51900   15.99400 -31.55600 1.000 32.80105 ? 107 MET A O   1 
ATOM   826  C CB  . MET A 1 108 ? 7.59200   18.58100 -29.48400 1.000 27.73383 ? 107 MET A CB  1 
ATOM   827  C CG  . MET A 1 108 ? 6.82700   19.05700 -28.25100 1.000 35.85642 ? 107 MET A CG  1 
ATOM   828  S SD  . MET A 1 108 ? 7.56500   18.54900 -26.67900 1.000 33.15148 ? 107 MET A SD  1 
ATOM   829  C CE  . MET A 1 108 ? 6.49500   17.14200 -26.35600 1.000 21.32850 ? 107 MET A CE  1 
ATOM   830  N N   . PRO A 1 109 ? 8.03000   17.93400 -32.55700 1.000 32.80845 ? 108 PRO A N   1 
ATOM   831  C CA  . PRO A 1 109 ? 8.96200   17.26500 -33.47900 1.000 28.72145 ? 108 PRO A CA  1 
ATOM   832  C C   . PRO A 1 109 ? 10.16700  16.71600 -32.72900 1.000 30.15924 ? 108 PRO A C   1 
ATOM   833  O O   . PRO A 1 109 ? 10.68500  17.34400 -31.79800 1.000 31.19771 ? 108 PRO A O   1 
ATOM   834  C CB  . PRO A 1 109 ? 9.37600   18.37000 -34.46300 1.000 28.54484 ? 108 PRO A CB  1 
ATOM   835  C CG  . PRO A 1 109 ? 8.41700   19.49200 -34.26900 1.000 30.63476 ? 108 PRO A CG  1 
ATOM   836  C CD  . PRO A 1 109 ? 7.74200   19.33000 -32.93900 1.000 34.27867 ? 108 PRO A CD  1 
ATOM   837  N N   . ALA A 1 110 ? 10.60200  15.52300 -33.14700 1.000 34.82491 ? 109 ALA A N   1 
ATOM   838  C CA  . ALA A 1 110 ? 11.80100  14.90500 -32.58400 1.000 31.83164 ? 109 ALA A CA  1 
ATOM   839  C C   . ALA A 1 110 ? 12.99100  15.85500 -32.61200 1.000 31.67254 ? 109 ALA A C   1 
ATOM   840  O O   . ALA A 1 110 ? 13.79100  15.87600 -31.67300 1.000 34.69460 ? 109 ALA A O   1 
ATOM   841  C CB  . ALA A 1 110 ? 12.13800  13.62000 -33.34800 1.000 29.79008 ? 109 ALA A CB  1 
ATOM   842  N N   . GLN A 1 111 ? 13.10100  16.67100 -33.67300 1.000 35.57083 ? 110 GLN A N   1 
ATOM   843  C CA  . GLN A 1 111 ? 14.23800  17.56900 -33.87100 1.000 29.37207 ? 110 GLN A CA  1 
ATOM   844  C C   . GLN A 1 111 ? 14.39300  18.61100 -32.77000 1.000 25.95191 ? 110 GLN A C   1 
ATOM   845  O O   . GLN A 1 111 ? 15.45500  19.22300 -32.66600 1.000 29.48340 ? 110 GLN A O   1 
ATOM   846  C CB  . GLN A 1 111 ? 14.11700  18.31400 -35.20900 1.000 28.01175 ? 110 GLN A CB  1 
ATOM   847  C CG  . GLN A 1 111 ? 14.10200  17.45000 -36.45900 1.000 37.11134 ? 110 GLN A CG  1 
ATOM   848  C CD  . GLN A 1 111 ? 14.96300  18.03800 -37.58000 1.000 50.01817 ? 110 GLN A CD  1 
ATOM   849  O OE1 . GLN A 1 111 ? 14.47000  18.73500 -38.47300 1.000 49.66014 ? 110 GLN A OE1 1 
ATOM   850  N NE2 . GLN A 1 111 ? 16.25500  17.75400 -37.53600 1.000 56.46121 ? 110 GLN A NE2 1 
ATOM   851  N N   . GLN A 1 112 ? 13.36800  18.87700 -31.97700 1.000 27.51020 ? 111 GLN A N   1 
ATOM   852  C CA  . GLN A 1 112 ? 13.49300  19.89300 -30.94500 1.000 27.71732 ? 111 GLN A CA  1 
ATOM   853  C C   . GLN A 1 112 ? 13.32500  19.29700 -29.56000 1.000 28.01424 ? 111 GLN A C   1 
ATOM   854  O O   . GLN A 1 112 ? 12.93000  19.99200 -28.62300 1.000 30.64469 ? 111 GLN A O   1 
ATOM   855  C CB  . GLN A 1 112 ? 12.49000  21.01700 -31.16000 1.000 29.79418 ? 111 GLN A CB  1 
ATOM   856  C CG  . GLN A 1 112 ? 11.05000  20.60500 -31.07400 1.000 27.56526 ? 111 GLN A CG  1 
ATOM   857  C CD  . GLN A 1 112 ? 10.19700  21.55400 -31.84400 1.000 28.10109 ? 111 GLN A CD  1 
ATOM   858  O OE1 . GLN A 1 112 ? 10.43000  21.77700 -33.02500 1.000 25.59663 ? 111 GLN A OE1 1 
ATOM   859  N NE2 . GLN A 1 112 ? 9.22500   22.16100 -31.17400 1.000 33.75492 ? 111 GLN A NE2 1 
ATOM   860  N N   . MET A 1 113 ? 13.59600  18.00500 -29.43400 1.000 26.48659 ? 112 MET A N   1 
ATOM   861  C CA  . MET A 1 113 ? 13.51700  17.29600 -28.16800 1.000 30.97613 ? 112 MET A CA  1 
ATOM   862  C C   . MET A 1 113 ? 14.85400  16.63300 -27.91200 1.000 33.94700 ? 112 MET A C   1 
ATOM   863  O O   . MET A 1 113 ? 15.44800  16.04400 -28.82400 1.000 34.98830 ? 112 MET A O   1 
ATOM   864  C CB  . MET A 1 113 ? 12.42100  16.22300 -28.16500 1.000 32.34076 ? 112 MET A CB  1 
ATOM   865  C CG  . MET A 1 113 ? 11.07600  16.66600 -28.67700 1.000 29.03008 ? 112 MET A CG  1 
ATOM   866  S SD  . MET A 1 113 ? 10.02900  15.20900 -28.84800 1.000 32.75039 ? 112 MET A SD  1 
ATOM   867  C CE  . MET A 1 113 ? 9.96600   14.62500 -27.16000 1.000 26.90885 ? 112 MET A CE  1 
ATOM   868  N N   . VAL A 1 114 ? 15.32000  16.72200 -26.67100 1.000 29.88571 ? 113 VAL A N   1 
ATOM   869  C CA  . VAL A 1 114 ? 16.62700  16.20800 -26.28600 1.000 26.97985 ? 113 VAL A CA  1 
ATOM   870  C C   . VAL A 1 114 ? 16.47000  15.27400 -25.09400 1.000 30.04964 ? 113 VAL A C   1 
ATOM   871  O O   . VAL A 1 114 ? 15.66400  15.52600 -24.19000 1.000 29.44339 ? 113 VAL A O   1 
ATOM   872  C CB  . VAL A 1 114 ? 17.59900  17.35500 -25.95300 1.000 31.44667 ? 113 VAL A CB  1 
ATOM   873  C CG1 . VAL A 1 114 ? 18.88200  16.81200 -25.32200 1.000 26.84527 ? 113 VAL A CG1 1 
ATOM   874  C CG2 . VAL A 1 114 ? 17.87900  18.19200 -27.21000 1.000 30.06680 ? 113 VAL A CG2 1 
ATOM   875  N N   . GLU A 1 115 ? 17.24100  14.18700 -25.10400 1.000 36.43996 ? 114 GLU A N   1 
ATOM   876  C CA  . GLU A 1 115 ? 17.34900  13.25000 -23.99000 1.000 35.89351 ? 114 GLU A CA  1 
ATOM   877  C C   . GLU A 1 115 ? 18.79200  12.79400 -23.87200 1.000 34.14778 ? 114 GLU A C   1 
ATOM   878  O O   . GLU A 1 115 ? 19.47000  12.60800 -24.88900 1.000 34.03397 ? 114 GLU A O   1 
ATOM   879  C CB  . GLU A 1 115 ? 16.45100  12.02400 -24.17200 1.000 29.01981 ? 114 GLU A CB  1 
ATOM   880  C CG  . GLU A 1 115 ? 15.01400  12.35800 -24.37800 1.000 30.55106 ? 114 GLU A CG  1 
ATOM   881  C CD  . GLU A 1 115 ? 14.15600  11.16000 -24.18000 1.000 31.70869 ? 114 GLU A CD  1 
ATOM   882  O OE1 . GLU A 1 115 ? 14.71000  10.04800 -24.09800 1.000 32.03652 ? 114 GLU A OE1 1 
ATOM   883  O OE2 . GLU A 1 115 ? 12.92900  11.33400 -24.09300 1.000 30.42656 ? 114 GLU A OE2 1 
ATOM   884  N N   . TYR A 1 116 ? 19.24600  12.59400 -22.63000 1.000 31.89481 ? 115 TYR A N   1 
ATOM   885  C CA  . TYR A 1 116 ? 20.62700  12.18700 -22.36300 1.000 34.59792 ? 115 TYR A CA  1 
ATOM   886  C C   . TYR A 1 116 ? 21.59800  13.05700 -23.15400 1.000 33.33727 ? 115 TYR A C   1 
ATOM   887  O O   . TYR A 1 116 ? 22.53600  12.56800 -23.78500 1.000 36.21653 ? 115 TYR A O   1 
ATOM   888  C CB  . TYR A 1 116 ? 20.83600  10.69900 -22.67900 1.000 34.24187 ? 115 TYR A CB  1 
ATOM   889  C CG  . TYR A 1 116 ? 19.97700  9.76100  -21.86300 1.000 32.16097 ? 115 TYR A CG  1 
ATOM   890  C CD1 . TYR A 1 116 ? 20.25200  9.53900  -20.52100 1.000 38.76747 ? 115 TYR A CD1 1 
ATOM   891  C CD2 . TYR A 1 116 ? 18.88400  9.10100  -22.43000 1.000 31.48890 ? 115 TYR A CD2 1 
ATOM   892  C CE1 . TYR A 1 116 ? 19.47000  8.67600  -19.75800 1.000 40.62104 ? 115 TYR A CE1 1 
ATOM   893  C CE2 . TYR A 1 116 ? 18.09300  8.23800  -21.67800 1.000 32.29585 ? 115 TYR A CE2 1 
ATOM   894  C CZ  . TYR A 1 116 ? 18.39800  8.03400  -20.33700 1.000 37.74277 ? 115 TYR A CZ  1 
ATOM   895  O OH  . TYR A 1 116 ? 17.64500  7.18900  -19.56200 1.000 33.21199 ? 115 TYR A OH  1 
ATOM   896  N N   . GLY A 1 117 ? 21.33800  14.36300 -23.15900 1.000 37.16019 ? 116 GLY A N   1 
ATOM   897  C CA  . GLY A 1 117 ? 22.12500  15.30700 -23.92900 1.000 34.82810 ? 116 GLY A CA  1 
ATOM   898  C C   . GLY A 1 117 ? 22.08400  15.14500 -25.44000 1.000 33.48265 ? 116 GLY A C   1 
ATOM   899  O O   . GLY A 1 117 ? 22.73700  15.93100 -26.13700 1.000 31.51964 ? 116 GLY A O   1 
ATOM   900  N N   . ARG A 1 118 ? 21.33800  14.17600 -25.98100 1.000 35.89080 ? 117 ARG A N   1 
ATOM   901  C CA  . ARG A 1 118 ? 21.31500  13.93300 -27.42100 1.000 43.77416 ? 117 ARG A CA  1 
ATOM   902  C C   . ARG A 1 118 ? 19.93200  14.16700 -28.03300 1.000 37.87816 ? 117 ARG A C   1 
ATOM   903  O O   . ARG A 1 118 ? 18.90000  14.05400 -27.36500 1.000 31.37982 ? 117 ARG A O   1 
ATOM   904  C CB  . ARG A 1 118 ? 21.79000  12.50800 -27.74400 1.000 40.36542 ? 117 ARG A CB  1 
ATOM   905  C CG  . ARG A 1 118 ? 23.27800  12.29700 -27.46700 1.000 43.20779 ? 117 ARG A CG  1 
ATOM   906  C CD  . ARG A 1 118 ? 24.12200  12.67900 -28.67200 1.000 45.18021 ? 117 ARG A CD  1 
ATOM   907  N NE  . ARG A 1 118 ? 24.43800  11.52300 -29.50100 1.000 51.07316 ? 117 ARG A NE  1 
ATOM   908  C CZ  . ARG A 1 118 ? 25.49700  11.42700 -30.29500 1.000 61.12044 ? 117 ARG A CZ  1 
ATOM   909  N NH1 . ARG A 1 118 ? 26.36900  12.41800 -30.40600 1.000 58.47217 ? 117 ARG A NH1 1 
ATOM   910  N NH2 . ARG A 1 118 ? 25.68600  10.30900 -30.99700 1.000 68.24753 ? 117 ARG A NH2 1 
ATOM   911  N N   . PHE A 1 119 ? 19.93500  14.46500 -29.33900 1.000 31.08227 ? 118 PHE A N   1 
ATOM   912  C CA  . PHE A 1 119 ? 18.71800  14.74400 -30.09500 1.000 31.50690 ? 118 PHE A CA  1 
ATOM   913  C C   . PHE A 1 119 ? 18.04200  13.44800 -30.53700 1.000 34.57688 ? 118 PHE A C   1 
ATOM   914  O O   . PHE A 1 119 ? 18.65200  12.63300 -31.23700 1.000 39.34990 ? 118 PHE A O   1 
ATOM   915  C CB  . PHE A 1 119 ? 19.04900  15.60400 -31.30900 1.000 28.61828 ? 118 PHE A CB  1 
ATOM   916  C CG  . PHE A 1 119 ? 18.97500  17.06900 -31.04300 1.000 26.07627 ? 118 PHE A CG  1 
ATOM   917  C CD1 . PHE A 1 119 ? 17.76100  17.68300 -30.81700 1.000 31.73962 ? 118 PHE A CD1 1 
ATOM   918  C CD2 . PHE A 1 119 ? 20.12100  17.83500 -31.01500 1.000 29.74697 ? 118 PHE A CD2 1 
ATOM   919  C CE1 . PHE A 1 119 ? 17.68900  19.03900 -30.56500 1.000 28.61228 ? 118 PHE A CE1 1 
ATOM   920  C CE2 . PHE A 1 119 ? 20.06200  19.19500 -30.77500 1.000 27.71028 ? 118 PHE A CE2 1 
ATOM   921  C CZ  . PHE A 1 119 ? 18.84400  19.79700 -30.54800 1.000 29.28916 ? 118 PHE A CZ  1 
ATOM   922  N N   . LEU A 1 120 ? 16.76900  13.28500 -30.17000 1.000 34.18869 ? 119 LEU A N   1 
ATOM   923  C CA  . LEU A 1 120 ? 16.03400  12.04800 -30.41600 1.000 34.76613 ? 119 LEU A CA  1 
ATOM   924  C C   . LEU A 1 120 ? 15.87900  11.78800 -31.91400 1.000 31.37360 ? 119 LEU A C   1 
ATOM   925  O O   . LEU A 1 120 ? 15.99700  12.70700 -32.72200 1.000 30.10010 ? 119 LEU A O   1 
ATOM   926  C CB  . LEU A 1 120 ? 14.65100  12.12400 -29.76400 1.000 31.91287 ? 119 LEU A CB  1 
ATOM   927  C CG  . LEU A 1 120 ? 14.57300  12.20100 -28.24300 1.000 25.57678 ? 119 LEU A CG  1 
ATOM   928  C CD1 . LEU A 1 120 ? 13.15800  11.98200 -27.77000 1.000 21.05062 ? 119 LEU A CD1 1 
ATOM   929  C CD2 . LEU A 1 120 ? 15.48200  11.14900 -27.65600 1.000 31.44605 ? 119 LEU A CD2 1 
ATOM   930  N N   . PRO A 1 121 ? 15.61400  10.52400 -32.31000 1.000 37.64044 ? 120 PRO A N   1 
ATOM   931  C CA  . PRO A 1 121 ? 15.22700  10.24800 -33.70000 1.000 42.22912 ? 120 PRO A CA  1 
ATOM   932  C C   . PRO A 1 121 ? 13.71300  10.18100 -33.83400 1.000 43.07947 ? 120 PRO A C   1 
ATOM   933  O O   . PRO A 1 121 ? 13.00700  10.38100 -32.84200 1.000 48.04636 ? 120 PRO A O   1 
ATOM   934  C CB  . PRO A 1 121 ? 15.85900  8.87900  -33.95700 1.000 42.09395 ? 120 PRO A CB  1 
ATOM   935  C CG  . PRO A 1 121 ? 15.72200  8.19000  -32.60500 1.000 39.73967 ? 120 PRO A CG  1 
ATOM   936  C CD  . PRO A 1 121 ? 15.69400  9.27300  -31.53000 1.000 38.29464 ? 120 PRO A CD  1 
ATOM   937  N N   . GLN A 1 122 ? 13.19000  9.86600  -35.01000 1.000 36.64844 ? 121 GLN A N   1 
ATOM   938  C CA  . GLN A 1 122 ? 11.76500  9.60100  -35.08200 1.000 42.67461 ? 121 GLN A CA  1 
ATOM   939  C C   . GLN A 1 122 ? 11.46500  8.22700  -34.49100 1.000 48.68397 ? 121 GLN A C   1 
ATOM   940  O O   . GLN A 1 122 ? 12.36900  7.40200  -34.33300 1.000 52.71843 ? 121 GLN A O   1 
ATOM   941  C CB  . GLN A 1 122 ? 11.28300  9.68600  -36.52800 1.000 50.67471 ? 121 GLN A CB  1 
ATOM   942  C CG  . GLN A 1 122 ? 10.08000  10.60100 -36.71300 1.000 45.60786 ? 121 GLN A CG  1 
ATOM   943  C CD  . GLN A 1 122 ? 10.42000  12.04000 -36.37000 1.000 50.47442 ? 121 GLN A CD  1 
ATOM   944  O OE1 . GLN A 1 122 ? 11.40000  12.58500 -36.88100 1.000 43.61712 ? 121 GLN A OE1 1 
ATOM   945  N NE2 . GLN A 1 122 ? 9.62800   12.65700 -35.47400 1.000 50.00552 ? 121 GLN A NE2 1 
ATOM   946  N N   . PRO A 1 123 ? 10.19100  7.95100  -34.13300 1.000 51.17888 ? 122 PRO A N   1 
ATOM   947  C CA  . PRO A 1 123 ? 9.83900   6.60300  -33.64800 1.000 45.04994 ? 122 PRO A CA  1 
ATOM   948  C C   . PRO A 1 123 ? 10.29000  5.48300  -34.57500 1.000 55.26153 ? 122 PRO A C   1 
ATOM   949  O O   . PRO A 1 123 ? 10.41900  4.33000  -34.15000 1.000 54.40463 ? 122 PRO A O   1 
ATOM   950  C CB  . PRO A 1 123 ? 8.30900   6.65600  -33.55500 1.000 43.35570 ? 122 PRO A CB  1 
ATOM   951  C CG  . PRO A 1 123 ? 8.01100   8.07600  -33.24700 1.000 43.64253 ? 122 PRO A CG  1 
ATOM   952  C CD  . PRO A 1 123 ? 9.09200   8.91200  -33.92400 1.000 43.57313 ? 122 PRO A CD  1 
ATOM   953  N N   . GLY A 1 124 ? 10.52500  5.80600  -35.84600 1.000 57.45356 ? 123 GLY A N   1 
ATOM   954  C CA  . GLY A 1 124 ? 11.02000  4.81800  -36.78500 1.000 64.88410 ? 123 GLY A CA  1 
ATOM   955  C C   . GLY A 1 124 ? 12.52400  4.82600  -36.97000 1.000 63.65841 ? 123 GLY A C   1 
ATOM   956  O O   . GLY A 1 124 ? 13.00600  4.85600  -38.10700 1.000 63.43610 ? 123 GLY A O   1 
ATOM   957  N N   . HIS A 1 125 ? 13.27100  4.79100  -35.86200 1.000 61.56610 ? 124 HIS A N   1 
ATOM   958  C CA  . HIS A 1 125 ? 14.73100  4.79800  -35.91100 1.000 68.07219 ? 124 HIS A CA  1 
ATOM   959  C C   . HIS A 1 125 ? 15.34200  4.52100  -34.53800 1.000 60.85060 ? 124 HIS A C   1 
ATOM   960  O O   . HIS A 1 125 ? 16.48000  4.91900  -34.26400 1.000 59.09196 ? 124 HIS A O   1 
ATOM   961  C CB  . HIS A 1 125 ? 15.25000  6.13400  -36.45900 1.000 64.72816 ? 124 HIS A CB  1 
ATOM   962  C CG  . HIS A 1 125 ? 15.68200  6.06900  -37.89400 1.000 77.63581 ? 124 HIS A CG  1 
ATOM   963  N ND1 . HIS A 1 125 ? 14.78400  6.00000  -38.94000 1.000 75.90647 ? 124 HIS A ND1 1 
ATOM   964  C CD2 . HIS A 1 125 ? 16.91600  6.04000  -38.45300 1.000 74.50284 ? 124 HIS A CD2 1 
ATOM   965  C CE1 . HIS A 1 125 ? 15.44900  5.94000  -40.08200 1.000 77.35325 ? 124 HIS A CE1 1 
ATOM   966  N NE2 . HIS A 1 125 ? 16.74300  5.96000  -39.81400 1.000 71.86655 ? 124 HIS A NE2 1 
ATOM   967  N N   . GLU A 1 126 ? 14.60300  3.81000  -33.68500 1.000 59.50418 ? 125 GLU A N   1 
ATOM   968  C CA  . GLU A 1 126 ? 14.98600  3.68200  -32.28000 1.000 62.50053 ? 125 GLU A CA  1 
ATOM   969  C C   . GLU A 1 126 ? 16.32000  2.96100  -32.11000 1.000 66.28893 ? 125 GLU A C   1 
ATOM   970  O O   . GLU A 1 126 ? 17.12600  3.32400  -31.24000 1.000 57.79646 ? 125 GLU A O   1 
ATOM   971  C CB  . GLU A 1 126 ? 13.89500  2.93500  -31.51300 1.000 67.76951 ? 125 GLU A CB  1 
ATOM   972  C CG  . GLU A 1 126 ? 12.50900  3.50700  -31.67400 1.000 62.13388 ? 125 GLU A CG  1 
ATOM   973  C CD  . GLU A 1 126 ? 12.31300  4.74100  -30.83700 1.000 61.95889 ? 125 GLU A CD  1 
ATOM   974  O OE1 . GLU A 1 126 ? 13.22600  5.04300  -30.03300 1.000 68.18148 ? 125 GLU A OE1 1 
ATOM   975  O OE2 . GLU A 1 126 ? 11.25000  5.39100  -30.96700 1.000 56.53125 ? 125 GLU A OE2 1 
ATOM   976  N N   . GLY A 1 127 ? 16.56200  1.92500  -32.91800 1.000 64.96659 ? 126 GLY A N   1 
ATOM   977  C CA  . GLY A 1 127 ? 17.66600  1.00900  -32.69100 1.000 65.46847 ? 126 GLY A CA  1 
ATOM   978  C C   . GLY A 1 127 ? 18.97200  1.39300  -33.35400 1.000 66.33418 ? 126 GLY A C   1 
ATOM   979  O O   . GLY A 1 127 ? 20.05300  1.07700  -32.84500 1.000 63.57106 ? 126 GLY A O   1 
ATOM   980  N N   . GLU A 1 128 ? 18.87600  2.06900  -34.50000 1.000 65.61680 ? 127 GLU A N   1 
ATOM   981  C CA  . GLU A 1 128 ? 20.05000  2.59500  -35.18500 1.000 59.28056 ? 127 GLU A CA  1 
ATOM   982  C C   . GLU A 1 128 ? 20.58100  3.85500  -34.51000 1.000 61.08542 ? 127 GLU A C   1 
ATOM   983  O O   . GLU A 1 128 ? 21.80000  4.08000  -34.50100 1.000 55.28677 ? 127 GLU A O   1 
ATOM   984  C CB  . GLU A 1 128 ? 19.71000  2.87900  -36.65100 1.000 65.80415 ? 127 GLU A CB  1 
ATOM   985  C CG  . GLU A 1 128 ? 18.99300  1.72500  -37.35500 1.000 81.30156 ? 127 GLU A CG  1 
ATOM   986  C CD  . GLU A 1 128 ? 17.48300  1.70300  -37.09300 1.000 84.77290 ? 127 GLU A CD  1 
ATOM   987  O OE1 . GLU A 1 128 ? 16.94300  2.73600  -36.63600 1.000 73.86186 ? 127 GLU A OE1 1 
ATOM   988  O OE2 . GLU A 1 128 ? 16.84300  0.64900  -37.33300 1.000 83.12572 ? 127 GLU A OE2 1 
ATOM   989  N N   . TRP A 1 129 ? 19.68400  4.68400  -33.95700 1.000 58.39501 ? 128 TRP A N   1 
ATOM   990  C CA  . TRP A 1 129 ? 20.10700  5.85300  -33.18400 1.000 58.22915 ? 128 TRP A CA  1 
ATOM   991  C C   . TRP A 1 129 ? 20.96600  5.43500  -32.00100 1.000 53.06362 ? 128 TRP A C   1 
ATOM   992  O O   . TRP A 1 129 ? 22.07000  5.95900  -31.79600 1.000 47.34476 ? 128 TRP A O   1 
ATOM   993  C CB  . TRP A 1 129 ? 18.87700  6.61900  -32.70700 1.000 51.35231 ? 128 TRP A CB  1 
ATOM   994  C CG  . TRP A 1 129 ? 19.11200  7.72700  -31.68600 1.000 48.19551 ? 128 TRP A CG  1 
ATOM   995  C CD1 . TRP A 1 129 ? 19.38400  9.03500  -31.95200 1.000 41.55883 ? 128 TRP A CD1 1 
ATOM   996  C CD2 . TRP A 1 129 ? 19.01700  7.62400  -30.24900 1.000 45.30620 ? 128 TRP A CD2 1 
ATOM   997  N NE1 . TRP A 1 129 ? 19.48500  9.74500  -30.78100 1.000 36.40095 ? 128 TRP A NE1 1 
ATOM   998  C CE2 . TRP A 1 129 ? 19.27100  8.90100  -29.72300 1.000 42.24482 ? 128 TRP A CE2 1 
ATOM   999  C CE3 . TRP A 1 129 ? 18.77300  6.57000  -29.36200 1.000 45.00238 ? 128 TRP A CE3 1 
ATOM   1000 C CZ2 . TRP A 1 129 ? 19.28000  9.15500  -28.35300 1.000 36.32837 ? 128 TRP A CZ2 1 
ATOM   1001 C CZ3 . TRP A 1 129 ? 18.78600  6.82700  -28.00000 1.000 35.65610 ? 128 TRP A CZ3 1 
ATOM   1002 C CH2 . TRP A 1 129 ? 19.03000  8.10300  -27.51400 1.000 36.81661 ? 128 TRP A CH2 1 
ATOM   1003 N N   . PHE A 1 130 ? 20.46900  4.47300  -31.22200 1.000 53.55516 ? 129 PHE A N   1 
ATOM   1004 C CA  . PHE A 1 130 ? 21.20100  3.90600  -30.10200 1.000 52.76083 ? 129 PHE A CA  1 
ATOM   1005 C C   . PHE A 1 130 ? 22.58700  3.42400  -30.49800 1.000 59.98903 ? 129 PHE A C   1 
ATOM   1006 O O   . PHE A 1 130 ? 23.45000  3.26100  -29.62800 1.000 62.07173 ? 129 PHE A O   1 
ATOM   1007 C CB  . PHE A 1 130 ? 20.38500  2.75200  -29.52600 1.000 52.82466 ? 129 PHE A CB  1 
ATOM   1008 C CG  . PHE A 1 130 ? 20.91600  2.20800  -28.24000 1.000 59.99342 ? 129 PHE A CG  1 
ATOM   1009 C CD1 . PHE A 1 130 ? 20.98200  3.00100  -27.10700 1.000 55.51708 ? 129 PHE A CD1 1 
ATOM   1010 C CD2 . PHE A 1 130 ? 21.32200  0.88700  -28.15000 1.000 65.82286 ? 129 PHE A CD2 1 
ATOM   1011 C CE1 . PHE A 1 130 ? 21.46500  2.48900  -25.90900 1.000 54.53528 ? 129 PHE A CE1 1 
ATOM   1012 C CE2 . PHE A 1 130 ? 21.80400  0.36900  -26.94700 1.000 65.91509 ? 129 PHE A CE2 1 
ATOM   1013 C CZ  . PHE A 1 130 ? 21.86200  1.17500  -25.82400 1.000 61.59676 ? 129 PHE A CZ  1 
ATOM   1014 N N   . ASP A 1 131 ? 22.83000  3.20600  -31.78800 1.000 54.71625 ? 130 ASP A N   1 
ATOM   1015 C CA  . ASP A 1 131 ? 24.07500  2.60400  -32.22500 1.000 53.62599 ? 130 ASP A CA  1 
ATOM   1016 C C   . ASP A 1 131 ? 25.08900  3.62100  -32.72800 1.000 57.47720 ? 130 ASP A C   1 
ATOM   1017 O O   . ASP A 1 131 ? 26.25900  3.26500  -32.89100 1.000 64.03499 ? 130 ASP A O   1 
ATOM   1018 C CB  . ASP A 1 131 ? 23.79500  1.54800  -33.30500 1.000 60.99964 ? 130 ASP A CB  1 
ATOM   1019 C CG  . ASP A 1 131 ? 23.55300  0.15600  -32.71500 1.000 66.23755 ? 130 ASP A CG  1 
ATOM   1020 O OD1 . ASP A 1 131 ? 24.46600  -0.37200 -32.04700 1.000 79.49528 ? 130 ASP A OD1 1 
ATOM   1021 O OD2 . ASP A 1 131 ? 22.45300  -0.41000 -32.90400 1.000 61.77443 ? 130 ASP A OD2 1 
ATOM   1022 N N   . ASN A 1 132 ? 24.68500  4.87000  -32.97100 1.000 61.63669 ? 131 ASN A N   1 
ATOM   1023 C CA  . ASN A 1 132 ? 25.62800  5.95400  -33.23200 1.000 58.56803 ? 131 ASN A CA  1 
ATOM   1024 C C   . ASN A 1 132 ? 25.94600  6.74000  -31.96400 1.000 59.26094 ? 131 ASN A C   1 
ATOM   1025 O O   . ASN A 1 132 ? 26.31900  7.92300  -32.02600 1.000 62.24113 ? 131 ASN A O   1 
ATOM   1026 C CB  . ASN A 1 132 ? 25.09900  6.88600  -34.32600 1.000 58.76506 ? 131 ASN A CB  1 
ATOM   1027 C CG  . ASN A 1 132 ? 26.19700  7.75100  -34.93800 1.000 65.32863 ? 131 ASN A CG  1 
ATOM   1028 O OD1 . ASN A 1 132 ? 27.37500  7.61500  -34.59500 1.000 70.39287 ? 131 ASN A OD1 1 
ATOM   1029 N ND2 . ASN A 1 132 ? 25.81600  8.64700  -35.84100 1.000 67.57540 ? 131 ASN A ND2 1 
ATOM   1030 N N   . LEU A 1 133 ? 25.79500  6.09900  -30.80800 1.000 59.02184 ? 132 LEU A N   1 
ATOM   1031 C CA  . LEU A 1 133 ? 26.05000  6.72400  -29.51800 1.000 60.69258 ? 132 LEU A CA  1 
ATOM   1032 C C   . LEU A 1 133 ? 27.40000  6.28500  -28.97100 1.000 52.60680 ? 132 LEU A C   1 
ATOM   1033 O O   . LEU A 1 133 ? 27.81500  5.13900  -29.16000 1.000 55.48595 ? 132 LEU A O   1 
ATOM   1034 C CB  . LEU A 1 133 ? 24.94800  6.36900  -28.52200 1.000 55.49332 ? 132 LEU A CB  1 
ATOM   1035 C CG  . LEU A 1 133 ? 23.64700  7.14200  -28.71600 1.000 54.56558 ? 132 LEU A CG  1 
ATOM   1036 C CD1 . LEU A 1 133 ? 22.54700  6.54100  -27.86600 1.000 57.42288 ? 132 LEU A CD1 1 
ATOM   1037 C CD2 . LEU A 1 133 ? 23.85100  8.60800  -28.38400 1.000 50.33084 ? 132 LEU A CD2 1 
ATOM   1038 N N   . SER A 1 134 ? 28.08500  7.20500  -28.29800 1.000 51.22045 ? 133 SER A N   1 
ATOM   1039 C CA  . SER A 1 134 ? 29.35400  6.87200  -27.66800 1.000 49.96099 ? 133 SER A CA  1 
ATOM   1040 C C   . SER A 1 134 ? 29.14300  5.79200  -26.60900 1.000 60.91793 ? 133 SER A C   1 
ATOM   1041 O O   . SER A 1 134 ? 28.15400  5.81800  -25.86800 1.000 64.48279 ? 133 SER A O   1 
ATOM   1042 C CB  . SER A 1 134 ? 29.96200  8.12100  -27.04300 1.000 46.42216 ? 133 SER A CB  1 
ATOM   1043 O OG  . SER A 1 134 ? 29.70000  8.16600  -25.65600 1.000 39.78117 ? 133 SER A OG  1 
ATOM   1044 N N   . SER A 1 135 ? 30.08100  4.83600  -26.54000 1.000 54.80945 ? 134 SER A N   1 
ATOM   1045 C CA  . SER A 1 135 ? 29.90400  3.67600  -25.66500 1.000 54.15588 ? 134 SER A CA  1 
ATOM   1046 C C   . SER A 1 135 ? 29.61600  4.08100  -24.22700 1.000 53.05704 ? 134 SER A C   1 
ATOM   1047 O O   . SER A 1 135 ? 28.97100  3.33300  -23.48300 1.000 54.16194 ? 134 SER A O   1 
ATOM   1048 C CB  . SER A 1 135 ? 31.14100  2.77800  -25.70200 1.000 49.67455 ? 134 SER A CB  1 
ATOM   1049 O OG  . SER A 1 135 ? 32.33900  3.53700  -25.69400 1.000 55.25062 ? 134 SER A OG  1 
ATOM   1050 N N   . ASP A 1 136 ? 30.07800  5.25600  -23.81400 1.000 48.73986 ? 135 ASP A N   1 
ATOM   1051 C CA  . ASP A 1 136 ? 29.82800  5.67500  -22.44600 1.000 50.59924 ? 135 ASP A CA  1 
ATOM   1052 C C   . ASP A 1 136 ? 28.38300  6.09400  -22.25200 1.000 54.06925 ? 135 ASP A C   1 
ATOM   1053 O O   . ASP A 1 136 ? 27.82600  5.89800  -21.16600 1.000 56.79474 ? 135 ASP A O   1 
ATOM   1054 C CB  . ASP A 1 136 ? 30.78000  6.79900  -22.07900 1.000 54.80692 ? 135 ASP A CB  1 
ATOM   1055 C CG  . ASP A 1 136 ? 32.18300  6.29600  -21.87300 1.000 54.50226 ? 135 ASP A CG  1 
ATOM   1056 O OD1 . ASP A 1 136 ? 32.34700  5.39300  -21.02500 1.000 48.93375 ? 135 ASP A OD1 1 
ATOM   1057 O OD2 . ASP A 1 136 ? 33.10600  6.77500  -22.57700 1.000 62.95580 ? 135 ASP A OD2 1 
ATOM   1058 N N   . GLU A 1 137 ? 27.76600  6.65800  -23.29800 1.000 56.02821 ? 136 GLU A N   1 
ATOM   1059 C CA  . GLU A 1 137 ? 26.33700  6.96500  -23.27600 1.000 52.57239 ? 136 GLU A CA  1 
ATOM   1060 C C   . GLU A 1 137 ? 25.49700  5.69500  -23.34200 1.000 56.12483 ? 136 GLU A C   1 
ATOM   1061 O O   . GLU A 1 137 ? 24.51400  5.54800  -22.60300 1.000 54.23996 ? 136 GLU A O   1 
ATOM   1062 C CB  . GLU A 1 137 ? 26.01000  7.89100  -24.43900 1.000 50.79968 ? 136 GLU A CB  1 
ATOM   1063 C CG  . GLU A 1 137 ? 27.03100  8.97800  -24.56300 1.000 51.47236 ? 136 GLU A CG  1 
ATOM   1064 C CD  . GLU A 1 137 ? 26.64000  10.06000 -25.51500 1.000 48.30487 ? 136 GLU A CD  1 
ATOM   1065 O OE1 . GLU A 1 137 ? 26.75400  9.85500  -26.73700 1.000 44.53643 ? 136 GLU A OE1 1 
ATOM   1066 O OE2 . GLU A 1 137 ? 26.21700  11.12400 -25.02800 1.000 56.89056 ? 136 GLU A OE2 1 
ATOM   1067 N N   . ARG A 1 138 ? 25.88000  4.76700  -24.22300 1.000 61.46735 ? 137 ARG A N   1 
ATOM   1068 C CA  . ARG A 1 138 ? 25.18700  3.48800  -24.35500 1.000 59.43680 ? 137 ARG A CA  1 
ATOM   1069 C C   . ARG A 1 138 ? 25.20700  2.69200  -23.05600 1.000 53.43333 ? 137 ARG A C   1 
ATOM   1070 O O   . ARG A 1 138 ? 24.26500  1.94400  -22.77400 1.000 57.73279 ? 137 ARG A O   1 
ATOM   1071 C CB  . ARG A 1 138 ? 25.83600  2.67900  -25.48200 1.000 59.32829 ? 137 ARG A CB  1 
ATOM   1072 C CG  . ARG A 1 138 ? 24.88800  1.97100  -26.42200 1.000 55.80770 ? 137 ARG A CG  1 
ATOM   1073 C CD  . ARG A 1 138 ? 25.55300  1.66700  -27.76500 1.000 59.05628 ? 137 ARG A CD  1 
ATOM   1074 N NE  . ARG A 1 138 ? 26.94500  1.25800  -27.60500 1.000 64.20644 ? 137 ARG A NE  1 
ATOM   1075 C CZ  . ARG A 1 138 ? 27.98600  1.89800  -28.12600 1.000 60.53615 ? 137 ARG A CZ  1 
ATOM   1076 N NH1 . ARG A 1 138 ? 27.83100  2.96100  -28.89800 1.000 56.52800 ? 137 ARG A NH1 1 
ATOM   1077 N NH2 . ARG A 1 138 ? 29.21400  1.45700  -27.86700 1.000 53.70697 ? 137 ARG A NH2 1 
ATOM   1078 N N   . ALA A 1 139 ? 26.27700  2.81800  -22.26500 1.000 54.72408 ? 138 ALA A N   1 
ATOM   1079 C CA  . ALA A 1 139 ? 26.35800  2.07900  -21.01000 1.000 56.38558 ? 138 ALA A CA  1 
ATOM   1080 C C   . ALA A 1 139 ? 25.63500  2.80100  -19.88200 1.000 58.20313 ? 138 ALA A C   1 
ATOM   1081 O O   . ALA A 1 139 ? 25.13900  2.14800  -18.95500 1.000 53.02299 ? 138 ALA A O   1 
ATOM   1082 C CB  . ALA A 1 139 ? 27.82000  1.84100  -20.63000 1.000 48.99361 ? 138 ALA A CB  1 
ATOM   1083 N N   . PHE A 1 140 ? 25.57300  4.14000  -19.94300 1.000 56.79042 ? 139 PHE A N   1 
ATOM   1084 C CA  . PHE A 1 140 ? 24.83800  4.90900  -18.94100 1.000 51.78294 ? 139 PHE A CA  1 
ATOM   1085 C C   . PHE A 1 140 ? 23.33800  4.70600  -19.10000 1.000 52.87760 ? 139 PHE A C   1 
ATOM   1086 O O   . PHE A 1 140 ? 22.62300  4.46600  -18.11800 1.000 49.37829 ? 139 PHE A O   1 
ATOM   1087 C CB  . PHE A 1 140 ? 25.19200  6.39500  -19.04500 1.000 47.49134 ? 139 PHE A CB  1 
ATOM   1088 C CG  . PHE A 1 140 ? 24.57300  7.23700  -17.97300 1.000 43.24293 ? 139 PHE A CG  1 
ATOM   1089 C CD1 . PHE A 1 140 ? 24.31300  6.70600  -16.71600 1.000 52.27041 ? 139 PHE A CD1 1 
ATOM   1090 C CD2 . PHE A 1 140 ? 24.21700  8.54500  -18.22500 1.000 44.51119 ? 139 PHE A CD2 1 
ATOM   1091 C CE1 . PHE A 1 140 ? 23.73200  7.47600  -15.72200 1.000 51.58359 ? 139 PHE A CE1 1 
ATOM   1092 C CE2 . PHE A 1 140 ? 23.63200  9.32500  -17.23800 1.000 46.98451 ? 139 PHE A CE2 1 
ATOM   1093 C CZ  . PHE A 1 140 ? 23.39000  8.79000  -15.98400 1.000 43.44657 ? 139 PHE A CZ  1 
ATOM   1094 N N   . MET A 1 141 ? 22.84200  4.80600  -20.33600 1.000 54.00181 ? 140 MET A N   1 
ATOM   1095 C CA  . MET A 1 141 ? 21.43600  4.51700  -20.57900 1.000 50.09997 ? 140 MET A CA  1 
ATOM   1096 C C   . MET A 1 141 ? 21.10700  3.07300  -20.24700 1.000 51.73394 ? 140 MET A C   1 
ATOM   1097 O O   . MET A 1 141 ? 19.99200  2.77900  -19.80800 1.000 52.53108 ? 140 MET A O   1 
ATOM   1098 C CB  . MET A 1 141 ? 21.07400  4.86600  -22.02600 1.000 47.95122 ? 140 MET A CB  1 
ATOM   1099 C CG  . MET A 1 141 ? 21.09800  6.37200  -22.25700 1.000 46.92974 ? 140 MET A CG  1 
ATOM   1100 S SD  . MET A 1 141 ? 20.99600  7.00700  -23.95600 1.000 67.05586 ? 140 MET A SD  1 
ATOM   1101 C CE  . MET A 1 141 ? 21.16900  5.52500  -24.89300 1.000 50.29361 ? 140 MET A CE  1 
ATOM   1102 N N   . GLU A 1 142 ? 22.07800  2.17200  -20.40300 1.000 59.02633 ? 141 GLU A N   1 
ATOM   1103 C CA  . GLU A 1 142 ? 21.86400  0.76500  -20.07800 1.000 58.08855 ? 141 GLU A CA  1 
ATOM   1104 C C   . GLU A 1 142 ? 21.41500  0.59500  -18.63000 1.000 55.29845 ? 141 GLU A C   1 
ATOM   1105 O O   . GLU A 1 142 ? 20.46000  -0.13800 -18.34300 1.000 48.73251 ? 141 GLU A O   1 
ATOM   1106 C CB  . GLU A 1 142 ? 23.14800  -0.02500 -20.33400 1.000 59.29204 ? 141 GLU A CB  1 
ATOM   1107 C CG  . GLU A 1 142 ? 23.00700  -1.12900 -21.36300 1.000 60.60253 ? 141 GLU A CG  1 
ATOM   1108 C CD  . GLU A 1 142 ? 24.33200  -1.78800 -21.67500 1.000 64.17204 ? 141 GLU A CD  1 
ATOM   1109 O OE1 . GLU A 1 142 ? 24.91800  -2.39700 -20.75100 1.000 53.80691 ? 141 GLU A OE1 1 
ATOM   1110 O OE2 . GLU A 1 142 ? 24.78100  -1.69500 -22.83900 1.000 66.97746 ? 141 GLU A OE2 1 
ATOM   1111 N N   . THR A 1 143 ? 22.08400  1.28100  -17.70000 1.000 53.16056 ? 142 THR A N   1 
ATOM   1112 C CA  . THR A 1 143 ? 21.74300  1.12100  -16.29200 1.000 53.97625 ? 142 THR A CA  1 
ATOM   1113 C C   . THR A 1 143 ? 20.33100  1.61100  -15.97300 1.000 56.39450 ? 142 THR A C   1 
ATOM   1114 O O   . THR A 1 143 ? 19.86400  1.41500  -14.84400 1.000 47.25138 ? 142 THR A O   1 
ATOM   1115 C CB  . THR A 1 143 ? 22.77000  1.85000  -15.41400 1.000 53.18009 ? 142 THR A CB  1 
ATOM   1116 O OG1 . THR A 1 143 ? 22.82200  1.22300  -14.12600 1.000 55.73560 ? 142 THR A OG1 1 
ATOM   1117 C CG2 . THR A 1 143 ? 22.40000  3.33900  -15.23500 1.000 48.77224 ? 142 THR A CG2 1 
ATOM   1118 N N   . ASN A 1 144 ? 19.63900  2.22500  -16.93000 1.000 52.72121 ? 143 ASN A N   1 
ATOM   1119 C CA  . ASN A 1 144 ? 18.29600  2.76400  -16.70700 1.000 51.29981 ? 143 ASN A CA  1 
ATOM   1120 C C   . ASN A 1 144 ? 17.21900  1.86200  -17.31000 1.000 53.01804 ? 143 ASN A C   1 
ATOM   1121 O O   . ASN A 1 144 ? 16.31700  2.32600  -18.00500 1.000 43.81792 ? 143 ASN A O   1 
ATOM   1122 C CB  . ASN A 1 144 ? 18.20300  4.17900  -17.26200 1.000 43.40150 ? 143 ASN A CB  1 
ATOM   1123 C CG  . ASN A 1 144 ? 18.96900  5.18100  -16.42600 1.000 44.26421 ? 143 ASN A CG  1 
ATOM   1124 O OD1 . ASN A 1 144 ? 19.32200  4.91000  -15.28100 1.000 45.99722 ? 143 ASN A OD1 1 
ATOM   1125 N ND2 . ASN A 1 144 ? 19.23000  6.34900  -16.99600 1.000 48.58784 ? 143 ASN A ND2 1 
ATOM   1126 N N   . VAL A 1 145 ? 17.31300  0.55500  -17.04900 1.000 51.78796 ? 144 VAL A N   1 
ATOM   1127 C CA  . VAL A 1 145 ? 16.28700  -0.41600 -17.41500 1.000 51.86093 ? 144 VAL A CA  1 
ATOM   1128 C C   . VAL A 1 145 ? 16.00400  -1.25400 -16.18000 1.000 55.65367 ? 144 VAL A C   1 
ATOM   1129 O O   . VAL A 1 145 ? 16.91900  -1.88700 -15.63400 1.000 55.89974 ? 144 VAL A O   1 
ATOM   1130 C CB  . VAL A 1 145 ? 16.69800  -1.31900 -18.59300 1.000 54.95111 ? 144 VAL A CB  1 
ATOM   1131 C CG1 . VAL A 1 145 ? 15.62300  -2.39900 -18.83100 1.000 44.38894 ? 144 VAL A CG1 1 
ATOM   1132 C CG2 . VAL A 1 145 ? 16.95200  -0.49200 -19.86400 1.000 44.78149 ? 144 VAL A CG2 1 
ATOM   1133 N N   . ASP A 1 146 ? 14.74000  -1.26600 -15.75400 1.000 58.93344 ? 145 ASP A N   1 
ATOM   1134 C CA  . ASP A 1 146 ? 14.35900  -1.86900 -14.48400 1.000 53.70238 ? 145 ASP A CA  1 
ATOM   1135 C C   . ASP A 1 146 ? 14.45500  -3.38700 -14.54400 1.000 59.59724 ? 145 ASP A C   1 
ATOM   1136 O O   . ASP A 1 146 ? 14.09800  -4.00900 -15.55000 1.000 52.86934 ? 145 ASP A O   1 
ATOM   1137 C CB  . ASP A 1 146 ? 12.94300  -1.45200 -14.10400 1.000 48.47940 ? 145 ASP A CB  1 
ATOM   1138 C CG  . ASP A 1 146 ? 12.63900  -1.73500 -12.65500 1.000 51.14418 ? 145 ASP A CG  1 
ATOM   1139 O OD1 . ASP A 1 146 ? 13.42500  -1.28300 -11.78700 1.000 43.54509 ? 145 ASP A OD1 1 
ATOM   1140 O OD2 . ASP A 1 146 ? 11.63400  -2.43300 -12.38900 1.000 54.84646 ? 145 ASP A OD2 1 
ATOM   1141 N N   . VAL A 1 147 ? 14.90800  -3.97400 -13.43300 1.000 57.65919 ? 146 VAL A N   1 
ATOM   1142 C CA  . VAL A 1 147 ? 15.34500  -5.37100 -13.35700 1.000 68.31277 ? 146 VAL A CA  1 
ATOM   1143 C C   . VAL A 1 147 ? 16.23700  -5.71000 -14.55100 1.000 73.72834 ? 146 VAL A C   1 
ATOM   1144 O O   . VAL A 1 147 ? 17.45000  -5.88600 -14.40600 1.000 69.42013 ? 146 VAL A O   1 
ATOM   1145 C CB  . VAL A 1 147 ? 14.14800  -6.36700 -13.26100 1.000 71.82705 ? 146 VAL A CB  1 
ATOM   1146 C CG1 . VAL A 1 147 ? 13.04900  -5.83100 -12.31900 1.000 67.37270 ? 146 VAL A CG1 1 
ATOM   1147 C CG2 . VAL A 1 147 ? 13.60900  -6.77000 -14.65300 1.000 64.54337 ? 146 VAL A CG2 1 
ATOM   1148 N N   . PRO B 1 2   ? 9.35800   33.39700 -24.06900 1.000 28.48257 ? 1   PRO B N   1 
ATOM   1149 C CA  . PRO B 1 2   ? 9.39800   32.00200 -23.62100 1.000 25.28986 ? 1   PRO B CA  1 
ATOM   1150 C C   . PRO B 1 2   ? 9.32600   31.80500 -22.10700 1.000 24.57519 ? 1   PRO B C   1 
ATOM   1151 O O   . PRO B 1 2   ? 9.81800   32.62300 -21.33400 1.000 23.17717 ? 1   PRO B O   1 
ATOM   1152 C CB  . PRO B 1 2   ? 10.74700  31.53100 -24.12700 1.000 25.13467 ? 1   PRO B CB  1 
ATOM   1153 C CG  . PRO B 1 2   ? 11.59400  32.75700 -24.04400 1.000 29.73592 ? 1   PRO B CG  1 
ATOM   1154 C CD  . PRO B 1 2   ? 10.70100  33.90700 -24.38500 1.000 27.06655 ? 1   PRO B CD  1 
ATOM   1155 N N   . VAL B 1 3   ? 8.72200   30.69500 -21.69900 1.000 26.56097 ? 2   VAL B N   1 
ATOM   1156 C CA  . VAL B 1 3   ? 8.82700   30.18100 -20.34100 1.000 21.11409 ? 2   VAL B CA  1 
ATOM   1157 C C   . VAL B 1 3   ? 9.60000   28.87500 -20.40700 1.000 25.50816 ? 2   VAL B C   1 
ATOM   1158 O O   . VAL B 1 3   ? 9.33800   28.03800 -21.28400 1.000 25.25281 ? 2   VAL B O   1 
ATOM   1159 C CB  . VAL B 1 3   ? 7.44400   29.96300 -19.70700 1.000 24.18100 ? 2   VAL B CB  1 
ATOM   1160 C CG1 . VAL B 1 3   ? 7.56900   29.27100 -18.31900 1.000 19.81381 ? 2   VAL B CG1 1 
ATOM   1161 C CG2 . VAL B 1 3   ? 6.69300   31.26400 -19.62900 1.000 22.27476 ? 2   VAL B CG2 1 
ATOM   1162 N N   . TYR B 1 4   ? 10.55000  28.70300 -19.48800 1.000 25.23714 ? 3   TYR B N   1 
ATOM   1163 C CA  . TYR B 1 4   ? 11.38800  27.51000 -19.40600 1.000 22.67130 ? 3   TYR B CA  1 
ATOM   1164 C C   . TYR B 1 4   ? 11.12600  26.87900 -18.04300 1.000 22.23310 ? 3   TYR B C   1 
ATOM   1165 O O   . TYR B 1 4   ? 11.62500  27.33700 -17.01200 1.000 21.79473 ? 3   TYR B O   1 
ATOM   1166 C CB  . TYR B 1 4   ? 12.86700  27.83800 -19.59300 1.000 23.06272 ? 3   TYR B CB  1 
ATOM   1167 C CG  . TYR B 1 4   ? 13.28000  28.13400 -21.01300 1.000 25.00010 ? 3   TYR B CG  1 
ATOM   1168 C CD1 . TYR B 1 4   ? 13.56100  27.10500 -21.90300 1.000 28.24842 ? 3   TYR B CD1 1 
ATOM   1169 C CD2 . TYR B 1 4   ? 13.41200  29.44000 -21.46300 1.000 26.83143 ? 3   TYR B CD2 1 
ATOM   1170 C CE1 . TYR B 1 4   ? 13.95000  27.37300 -23.21300 1.000 32.44896 ? 3   TYR B CE1 1 
ATOM   1171 C CE2 . TYR B 1 4   ? 13.80300  29.71900 -22.77300 1.000 26.94367 ? 3   TYR B CE2 1 
ATOM   1172 C CZ  . TYR B 1 4   ? 14.07000  28.68300 -23.64200 1.000 29.68458 ? 3   TYR B CZ  1 
ATOM   1173 O OH  . TYR B 1 4   ? 14.46200  28.94500 -24.94300 1.000 28.75363 ? 3   TYR B OH  1 
ATOM   1174 N N   . MET B 1 5   ? 10.29000  25.86400 -18.04300 1.000 24.46557 ? 4   MET B N   1 
ATOM   1175 C CA  . MET B 1 5   ? 10.10400  25.02000 -16.88400 1.000 21.23589 ? 4   MET B CA  1 
ATOM   1176 C C   . MET B 1 5   ? 11.35200  24.17100 -16.70200 1.000 26.88333 ? 4   MET B C   1 
ATOM   1177 O O   . MET B 1 5   ? 11.69200  23.35600 -17.57200 1.000 26.72992 ? 4   MET B O   1 
ATOM   1178 C CB  . MET B 1 5   ? 8.87700   24.14400 -17.10100 1.000 20.96506 ? 4   MET B CB  1 
ATOM   1179 C CG  . MET B 1 5   ? 7.55000   24.87500 -17.17300 1.000 19.46463 ? 4   MET B CG  1 
ATOM   1180 S SD  . MET B 1 5   ? 7.42800   26.39300 -16.20900 1.000 30.84603 ? 4   MET B SD  1 
ATOM   1181 C CE  . MET B 1 5   ? 6.83600   25.73100 -14.64600 1.000 18.49371 ? 4   MET B CE  1 
ATOM   1182 N N   . VAL B 1 6   ? 12.04900  24.35100 -15.59000 1.000 23.86169 ? 5   VAL B N   1 
ATOM   1183 C CA  . VAL B 1 6   ? 13.30500  23.65000 -15.39100 1.000 25.14601 ? 5   VAL B CA  1 
ATOM   1184 C C   . VAL B 1 6   ? 13.16500  22.82200 -14.12500 1.000 28.56180 ? 5   VAL B C   1 
ATOM   1185 O O   . VAL B 1 6   ? 13.29700  23.34400 -13.00600 1.000 24.95303 ? 5   VAL B O   1 
ATOM   1186 C CB  . VAL B 1 6   ? 14.49900  24.59700 -15.32500 1.000 21.18756 ? 5   VAL B CB  1 
ATOM   1187 C CG1 . VAL B 1 6   ? 15.69700  23.82800 -14.88900 1.000 30.16851 ? 5   VAL B CG1 1 
ATOM   1188 C CG2 . VAL B 1 6   ? 14.75200  25.20200 -16.70900 1.000 20.24878 ? 5   VAL B CG2 1 
ATOM   1189 N N   . TYR B 1 7   ? 12.90200  21.52100 -14.31400 1.000 26.70129 ? 6   TYR B N   1 
ATOM   1190 C CA  . TYR B 1 7   ? 12.69500  20.56900 -13.22600 1.000 26.19647 ? 6   TYR B CA  1 
ATOM   1191 C C   . TYR B 1 7   ? 14.04300  20.02700 -12.75800 1.000 25.11834 ? 6   TYR B C   1 
ATOM   1192 O O   . TYR B 1 7   ? 14.88500  19.63300 -13.57300 1.000 26.53884 ? 6   TYR B O   1 
ATOM   1193 C CB  . TYR B 1 7   ? 11.75500  19.43200 -13.66400 1.000 20.28918 ? 6   TYR B CB  1 
ATOM   1194 C CG  . TYR B 1 7   ? 10.45500  19.93500 -14.26700 1.000 23.29899 ? 6   TYR B CG  1 
ATOM   1195 C CD1 . TYR B 1 7   ? 10.36300  20.20500 -15.63500 1.000 20.18296 ? 6   TYR B CD1 1 
ATOM   1196 C CD2 . TYR B 1 7   ? 9.32300   20.16900 -13.46800 1.000 23.47329 ? 6   TYR B CD2 1 
ATOM   1197 C CE1 . TYR B 1 7   ? 9.19800   20.69900 -16.19400 1.000 23.10607 ? 6   TYR B CE1 1 
ATOM   1198 C CE2 . TYR B 1 7   ? 8.12900   20.66400 -14.02100 1.000 23.44360 ? 6   TYR B CE2 1 
ATOM   1199 C CZ  . TYR B 1 7   ? 8.07500   20.92400 -15.39600 1.000 28.46988 ? 6   TYR B CZ  1 
ATOM   1200 O OH  . TYR B 1 7   ? 6.92400   21.40800 -16.00600 1.000 19.29475 ? 6   TYR B OH  1 
ATOM   1201 N N   . VAL B 1 8   ? 14.24900  20.04100 -11.43800 1.000 23.21257 ? 7   VAL B N   1 
ATOM   1202 C CA  . VAL B 1 8   ? 15.50900  19.63500 -10.82300 1.000 26.75503 ? 7   VAL B CA  1 
ATOM   1203 C C   . VAL B 1 8   ? 15.19800  19.11900 -9.43300  1.000 21.03797 ? 7   VAL B C   1 
ATOM   1204 O O   . VAL B 1 8   ? 14.16800  19.44300 -8.84400  1.000 22.75834 ? 7   VAL B O   1 
ATOM   1205 C CB  . VAL B 1 8   ? 16.54200  20.77900 -10.70500 1.000 20.88418 ? 7   VAL B CB  1 
ATOM   1206 C CG1 . VAL B 1 8   ? 17.26400  21.00400 -12.01700 1.000 26.44650 ? 7   VAL B CG1 1 
ATOM   1207 C CG2 . VAL B 1 8   ? 15.84500  22.03800 -10.22600 1.000 23.10359 ? 7   VAL B CG2 1 
ATOM   1208 N N   . SER B 1 9   ? 16.11600  18.33200 -8.89700  1.000 25.54414 ? 8   SER B N   1 
ATOM   1209 C CA  . SER B 1 9   ? 15.95700  17.83800 -7.54100  1.000 23.81019 ? 8   SER B CA  1 
ATOM   1210 C C   . SER B 1 9   ? 16.15200  18.96400 -6.54100  1.000 27.39112 ? 8   SER B C   1 
ATOM   1211 O O   . SER B 1 9   ? 16.99600  19.85000 -6.72700  1.000 26.44237 ? 8   SER B O   1 
ATOM   1212 C CB  . SER B 1 9   ? 16.95000  16.72400 -7.26100  1.000 27.40188 ? 8   SER B CB  1 
ATOM   1213 O OG  . SER B 1 9   ? 16.43700  15.49000 -7.73900  1.000 32.28272 ? 8   SER B OG  1 
ATOM   1214 N N   . GLN B 1 10  ? 15.32200  18.94300 -5.50400  1.000 27.72843 ? 9   GLN B N   1 
ATOM   1215 C CA  . GLN B 1 10  ? 15.46900  19.77900 -4.32200  1.000 31.41853 ? 9   GLN B CA  1 
ATOM   1216 C C   . GLN B 1 10  ? 16.92800  19.94300 -3.88900  1.000 24.06285 ? 9   GLN B C   1 
ATOM   1217 O O   . GLN B 1 10  ? 17.60800  18.96800 -3.56400  1.000 19.52822 ? 9   GLN B O   1 
ATOM   1218 C CB  . GLN B 1 10  ? 14.66200  19.15000 -3.19300  1.000 31.83955 ? 9   GLN B CB  1 
ATOM   1219 C CG  . GLN B 1 10  ? 14.75000  19.92700 -1.91800  1.000 35.51876 ? 9   GLN B CG  1 
ATOM   1220 C CD  . GLN B 1 10  ? 13.66600  20.94300 -1.84800  1.000 39.59166 ? 9   GLN B CD  1 
ATOM   1221 O OE1 . GLN B 1 10  ? 12.50900  20.61100 -1.57000  1.000 46.73833 ? 9   GLN B OE1 1 
ATOM   1222 N NE2 . GLN B 1 10  ? 14.01100  22.19200 -2.14900  1.000 42.06551 ? 9   GLN B NE2 1 
ATOM   1223 N N   . ASP B 1 11  ? 17.40300  21.18000 -3.88100  1.000 26.59723 ? 10  ASP B N   1 
ATOM   1224 C CA  . ASP B 1 11  ? 18.73300  21.57800 -3.43700  1.000 31.65309 ? 10  ASP B CA  1 
ATOM   1225 C C   . ASP B 1 11  ? 19.83600  21.19700 -4.40200  1.000 31.25748 ? 10  ASP B C   1 
ATOM   1226 O O   . ASP B 1 11  ? 21.01400  21.43600 -4.09700  1.000 36.03528 ? 10  ASP B O   1 
ATOM   1227 C CB  . ASP B 1 11  ? 19.10400  20.99700 -2.06700  1.000 32.44667 ? 10  ASP B CB  1 
ATOM   1228 C CG  . ASP B 1 11  ? 18.32100  21.59800 -0.97600  1.000 29.08162 ? 10  ASP B CG  1 
ATOM   1229 O OD1 . ASP B 1 11  ? 18.27100  22.83100 -0.93100  1.000 34.41412 ? 10  ASP B OD1 1 
ATOM   1230 O OD2 . ASP B 1 11  ? 17.72500  20.84500 -0.19100  1.000 30.99142 ? 10  ASP B OD2 1 
ATOM   1231 N N   . ARG B 1 12  ? 19.52200  20.58000 -5.53400  1.000 30.93679 ? 11  ARG B N   1 
ATOM   1232 C CA  . ARG B 1 12  ? 20.59000  20.28500 -6.47300  1.000 30.23751 ? 11  ARG B CA  1 
ATOM   1233 C C   . ARG B 1 12  ? 21.25200  21.57300 -6.93800  1.000 36.16581 ? 11  ARG B C   1 
ATOM   1234 O O   . ARG B 1 12  ? 22.47400  21.62800 -7.10000  1.000 36.38670 ? 11  ARG B O   1 
ATOM   1235 C CB  . ARG B 1 12  ? 20.05600  19.48100 -7.65300  1.000 37.14730 ? 11  ARG B CB  1 
ATOM   1236 C CG  . ARG B 1 12  ? 21.16200  18.96000 -8.55000  1.000 39.04406 ? 11  ARG B CG  1 
ATOM   1237 C CD  . ARG B 1 12  ? 22.09800  18.11200 -7.72600  1.000 37.00449 ? 11  ARG B CD  1 
ATOM   1238 N NE  . ARG B 1 12  ? 23.13100  17.47300 -8.52700  1.000 38.73077 ? 11  ARG B NE  1 
ATOM   1239 C CZ  . ARG B 1 12  ? 24.07300  18.12400 -9.19100  1.000 40.86710 ? 11  ARG B CZ  1 
ATOM   1240 N NH1 . ARG B 1 12  ? 24.11200  19.44900 -9.21400  1.000 41.95272 ? 11  ARG B NH1 1 
ATOM   1241 N NH2 . ARG B 1 12  ? 25.00900  17.42800 -9.83400  1.000 37.57389 ? 11  ARG B NH2 1 
ATOM   1242 N N   . LEU B 1 13  ? 20.46800  22.63400 -7.10400  1.000 33.64043 ? 12  LEU B N   1 
ATOM   1243 C CA  . LEU B 1 13  ? 20.98700  23.93800 -7.48500  1.000 28.72100 ? 12  LEU B CA  1 
ATOM   1244 C C   . LEU B 1 13  ? 20.95100  24.89000 -6.29300  1.000 32.10890 ? 12  LEU B C   1 
ATOM   1245 O O   . LEU B 1 13  ? 19.88600  25.14400 -5.71700  1.000 29.07368 ? 12  LEU B O   1 
ATOM   1246 C CB  . LEU B 1 13  ? 20.20700  24.51500 -8.66600  1.000 28.79719 ? 12  LEU B CB  1 
ATOM   1247 C CG  . LEU B 1 13  ? 19.98900  23.58400 -9.86100  1.000 33.09005 ? 12  LEU B CG  1 
ATOM   1248 C CD1 . LEU B 1 13  ? 19.28700  24.34200 -10.97700 1.000 24.25050 ? 12  LEU B CD1 1 
ATOM   1249 C CD2 . LEU B 1 13  ? 21.32100  22.99700 -10.34800 1.000 30.46865 ? 12  LEU B CD2 1 
ATOM   1250 N N   . THR B 1 14  ? 22.12300  25.40600 -5.92800  1.000 30.94381 ? 13  THR B N   1 
ATOM   1251 C CA  . THR B 1 14  ? 22.22000  26.50500 -4.99400  1.000 28.08753 ? 13  THR B CA  1 
ATOM   1252 C C   . THR B 1 14  ? 21.61800  27.75400 -5.62700  1.000 30.01162 ? 13  THR B C   1 
ATOM   1253 O O   . THR B 1 14  ? 21.50900  27.84100 -6.85200  1.000 30.60282 ? 13  THR B O   1 
ATOM   1254 C CB  . THR B 1 14  ? 23.67300  26.76700 -4.65900  1.000 27.23678 ? 13  THR B CB  1 
ATOM   1255 O OG1 . THR B 1 14  ? 24.28900  27.33000 -5.82300  1.000 30.36842 ? 13  THR B OG1 1 
ATOM   1256 C CG2 . THR B 1 14  ? 24.38500  25.48600 -4.29200  1.000 22.06251 ? 13  THR B CG2 1 
ATOM   1257 N N   . PRO B 1 15  ? 21.23200  28.74300 -4.81200  1.000 32.13046 ? 14  PRO B N   1 
ATOM   1258 C CA  . PRO B 1 15  ? 20.69600  29.98900 -5.39400  1.000 26.36767 ? 14  PRO B CA  1 
ATOM   1259 C C   . PRO B 1 15  ? 21.51600  30.51800 -6.55900  1.000 26.36688 ? 14  PRO B C   1 
ATOM   1260 O O   . PRO B 1 15  ? 20.95500  30.85200 -7.60500  1.000 29.26555 ? 14  PRO B O   1 
ATOM   1261 C CB  . PRO B 1 15  ? 20.70100  30.93800 -4.19400  1.000 18.13222 ? 14  PRO B CB  1 
ATOM   1262 C CG  . PRO B 1 15  ? 20.45300  30.04000 -3.03900  1.000 26.18744 ? 14  PRO B CG  1 
ATOM   1263 C CD  . PRO B 1 15  ? 21.19400  28.76300 -3.33700  1.000 24.40975 ? 14  PRO B CD  1 
ATOM   1264 N N   . SER B 1 16  ? 22.84200  30.56900 -6.40300  1.000 26.36979 ? 15  SER B N   1 
ATOM   1265 C CA  . SER B 1 16  ? 23.73500  31.06300 -7.44400  1.000 27.07723 ? 15  SER B CA  1 
ATOM   1266 C C   . SER B 1 16  ? 23.83300  30.08900 -8.61600  1.000 35.31758 ? 15  SER B C   1 
ATOM   1267 O O   . SER B 1 16  ? 23.84900  30.50300 -9.78400  1.000 29.12615 ? 15  SER B O   1 
ATOM   1268 C CB  . SER B 1 16  ? 25.10900  31.29900 -6.83600  1.000 26.94993 ? 15  SER B CB  1 
ATOM   1269 O OG  . SER B 1 16  ? 25.38500  30.23800 -5.94500  1.000 26.70763 ? 15  SER B OG  1 
ATOM   1270 N N   . ALA B 1 17  ? 23.94400  28.79300 -8.32200  1.000 27.47577 ? 16  ALA B N   1 
ATOM   1271 C CA  . ALA B 1 17  ? 23.77900  27.78800 -9.35800  1.000 25.48183 ? 16  ALA B CA  1 
ATOM   1272 C C   . ALA B 1 17  ? 22.48200  28.01800 -10.12600 1.000 33.25335 ? 16  ALA B C   1 
ATOM   1273 O O   . ALA B 1 17  ? 22.46500  28.01800 -11.36500 1.000 28.52983 ? 16  ALA B O   1 
ATOM   1274 C CB  . ALA B 1 17  ? 23.79700  26.39400 -8.73200  1.000 26.72106 ? 16  ALA B CB  1 
ATOM   1275 N N   . LYS B 1 18  ? 21.37800  28.21600 -9.39800  1.000 27.39320 ? 17  LYS B N   1 
ATOM   1276 C CA  . LYS B 1 18  ? 20.11600  28.53000 -10.05700 1.000 29.74051 ? 17  LYS B CA  1 
ATOM   1277 C C   . LYS B 1 18  ? 20.26300  29.77100 -10.92000 1.000 30.29567 ? 17  LYS B C   1 
ATOM   1278 O O   . LYS B 1 18  ? 19.91700  29.77300 -12.10800 1.000 28.68913 ? 17  LYS B O   1 
ATOM   1279 C CB  . LYS B 1 18  ? 19.00600  28.72900 -9.01900  1.000 25.01276 ? 17  LYS B CB  1 
ATOM   1280 C CG  . LYS B 1 18  ? 18.20700  27.48700 -8.68100  1.000 24.63909 ? 17  LYS B CG  1 
ATOM   1281 C CD  . LYS B 1 18  ? 17.28400  27.74500 -7.47600  1.000 26.01855 ? 17  LYS B CD  1 
ATOM   1282 C CE  . LYS B 1 18  ? 16.57700  26.48100 -7.00400  1.000 31.39101 ? 17  LYS B CE  1 
ATOM   1283 N NZ  . LYS B 1 18  ? 16.14900  26.57600 -5.57300  1.000 39.24973 ? 17  LYS B NZ  1 
ATOM   1284 N N   . HIS B 1 19  ? 20.79600  30.83700 -10.33300 1.000 30.57188 ? 18  HIS B N   1 
ATOM   1285 C CA  . HIS B 1 19  ? 21.00400  32.06800 -11.07700 1.000 30.91993 ? 18  HIS B CA  1 
ATOM   1286 C C   . HIS B 1 19  ? 21.75300  31.80100 -12.37800 1.000 27.10372 ? 18  HIS B C   1 
ATOM   1287 O O   . HIS B 1 19  ? 21.36400  32.29300 -13.43900 1.000 29.98134 ? 18  HIS B O   1 
ATOM   1288 C CB  . HIS B 1 19  ? 21.75200  33.05900 -10.18600 1.000 26.80737 ? 18  HIS B CB  1 
ATOM   1289 C CG  . HIS B 1 19  ? 21.71800  34.46400 -10.68200 1.000 27.44849 ? 18  HIS B CG  1 
ATOM   1290 N ND1 . HIS B 1 19  ? 21.82400  34.78000 -12.01600 1.000 38.36783 ? 18  HIS B ND1 1 
ATOM   1291 C CD2 . HIS B 1 19  ? 21.60400  35.64100 -10.02400 1.000 36.73550 ? 18  HIS B CD2 1 
ATOM   1292 C CE1 . HIS B 1 19  ? 21.76900  36.09300 -12.16200 1.000 43.32696 ? 18  HIS B CE1 1 
ATOM   1293 N NE2 . HIS B 1 19  ? 21.64000  36.64000 -10.96800 1.000 41.07306 ? 18  HIS B NE2 1 
ATOM   1294 N N   . ALA B 1 20  ? 22.81300  30.98600 -12.31500 1.000 27.96740 ? 19  ALA B N   1 
ATOM   1295 C CA  . ALA B 1 20  ? 23.69700  30.79400 -13.46200 1.000 28.30924 ? 19  ALA B CA  1 
ATOM   1296 C C   . ALA B 1 20  ? 23.03200  29.97300 -14.55300 1.000 29.51120 ? 19  ALA B C   1 
ATOM   1297 O O   . ALA B 1 20  ? 23.30400  30.17500 -15.74200 1.000 29.64106 ? 19  ALA B O   1 
ATOM   1298 C CB  . ALA B 1 20  ? 24.98800  30.11300 -13.01900 1.000 30.11268 ? 19  ALA B CB  1 
ATOM   1299 N N   . VAL B 1 21  ? 22.17800  29.03300 -14.15900 1.000 30.50127 ? 20  VAL B N   1 
ATOM   1300 C CA  . VAL B 1 21  ? 21.40600  28.26000 -15.11600 1.000 25.20791 ? 20  VAL B CA  1 
ATOM   1301 C C   . VAL B 1 21  ? 20.36600  29.14400 -15.79500 1.000 26.38061 ? 20  VAL B C   1 
ATOM   1302 O O   . VAL B 1 21  ? 20.13500  29.03000 -17.01000 1.000 22.87850 ? 20  VAL B O   1 
ATOM   1303 C CB  . VAL B 1 21  ? 20.78500  27.04900 -14.39500 1.000 28.94970 ? 20  VAL B CB  1 
ATOM   1304 C CG1 . VAL B 1 21  ? 19.65900  26.42900 -15.19900 1.000 28.67936 ? 20  VAL B CG1 1 
ATOM   1305 C CG2 . VAL B 1 21  ? 21.87700  26.02100 -14.07900 1.000 25.05082 ? 20  VAL B CG2 1 
ATOM   1306 N N   . ALA B 1 22  ? 19.75700  30.07100 -15.04500 1.000 20.19369 ? 21  ALA B N   1 
ATOM   1307 C CA  . ALA B 1 22  ? 18.82000  31.00300 -15.67300 1.000 21.49370 ? 21  ALA B CA  1 
ATOM   1308 C C   . ALA B 1 22  ? 19.53500  31.87600 -16.68700 1.000 29.70225 ? 21  ALA B C   1 
ATOM   1309 O O   . ALA B 1 22  ? 19.11400  31.98400 -17.84700 1.000 27.72764 ? 21  ALA B O   1 
ATOM   1310 C CB  . ALA B 1 22  ? 18.13100  31.87200 -14.63100 1.000 20.30000 ? 21  ALA B CB  1 
ATOM   1311 N N   . LYS B 1 23  ? 20.63600  32.50000 -16.26400 1.000 30.60199 ? 22  LYS B N   1 
ATOM   1312 C CA  . LYS B 1 23  ? 21.37900  33.35500 -17.17100 1.000 29.04350 ? 22  LYS B CA  1 
ATOM   1313 C C   . LYS B 1 23  ? 21.92500  32.57000 -18.35800 1.000 29.70368 ? 22  LYS B C   1 
ATOM   1314 O O   . LYS B 1 23  ? 22.06900  33.12300 -19.45100 1.000 34.96851 ? 22  LYS B O   1 
ATOM   1315 C CB  . LYS B 1 23  ? 22.49800  34.07100 -16.41300 1.000 30.19143 ? 22  LYS B CB  1 
ATOM   1316 C CG  . LYS B 1 23  ? 22.02200  35.28900 -15.59100 1.000 39.86090 ? 22  LYS B CG  1 
ATOM   1317 C CD  . LYS B 1 23  ? 21.26000  36.35000 -16.43400 1.000 44.74960 ? 22  LYS B CD  1 
ATOM   1318 C CE  . LYS B 1 23  ? 21.81400  36.54700 -17.86500 1.000 38.11596 ? 22  LYS B CE  1 
ATOM   1319 N NZ  . LYS B 1 23  ? 20.80700  37.12700 -18.77500 1.000 35.61460 ? 22  LYS B NZ  1 
ATOM   1320 N N   . ALA B 1 24  ? 22.20400  31.28100 -18.17500 1.000 27.13272 ? 23  ALA B N   1 
ATOM   1321 C CA  . ALA B 1 24  ? 22.65000  30.45500 -19.29100 1.000 26.89114 ? 23  ALA B CA  1 
ATOM   1322 C C   . ALA B 1 24  ? 21.53300  30.26200 -20.31900 1.000 33.65855 ? 23  ALA B C   1 
ATOM   1323 O O   . ALA B 1 24  ? 21.74100  30.46700 -21.52400 1.000 28.91878 ? 23  ALA B O   1 
ATOM   1324 C CB  . ALA B 1 24  ? 23.15700  29.11000 -18.77100 1.000 23.52536 ? 23  ALA B CB  1 
ATOM   1325 N N   . ILE B 1 25  ? 20.33900  29.86400 -19.86600 1.000 29.17477 ? 24  ILE B N   1 
ATOM   1326 C CA  . ILE B 1 25  ? 19.22600  29.71000 -20.79200 1.000 23.39569 ? 24  ILE B CA  1 
ATOM   1327 C C   . ILE B 1 25  ? 18.85500  31.05800 -21.39300 1.000 29.09444 ? 24  ILE B C   1 
ATOM   1328 O O   . ILE B 1 25  ? 18.78900  31.21100 -22.62100 1.000 33.79098 ? 24  ILE B O   1 
ATOM   1329 C CB  . ILE B 1 25  ? 18.02400  29.05300 -20.09300 1.000 27.39544 ? 24  ILE B CB  1 
ATOM   1330 C CG1 . ILE B 1 25  ? 18.43900  27.73200 -19.44000 1.000 30.38998 ? 24  ILE B CG1 1 
ATOM   1331 C CG2 . ILE B 1 25  ? 16.89200  28.80800 -21.08300 1.000 24.79704 ? 24  ILE B CG2 1 
ATOM   1332 C CD1 . ILE B 1 25  ? 17.34600  27.13500 -18.55600 1.000 23.09106 ? 24  ILE B CD1 1 
ATOM   1333 N N   . THR B 1 26  ? 18.61800  32.05600 -20.53400 1.000 28.14942 ? 25  THR B N   1 
ATOM   1334 C CA  . THR B 1 26  ? 18.15300  33.36000 -20.99700 1.000 25.55458 ? 25  THR B CA  1 
ATOM   1335 C C   . THR B 1 26  ? 19.04800  33.89700 -22.09100 1.000 27.76722 ? 25  THR B C   1 
ATOM   1336 O O   . THR B 1 26  ? 18.57100  34.34200 -23.14000 1.000 25.88504 ? 25  THR B O   1 
ATOM   1337 C CB  . THR B 1 26  ? 18.11400  34.34200 -19.83200 1.000 29.71705 ? 25  THR B CB  1 
ATOM   1338 O OG1 . THR B 1 26  ? 17.49800  33.71100 -18.70600 1.000 34.63469 ? 25  THR B OG1 1 
ATOM   1339 C CG2 . THR B 1 26  ? 17.33000  35.58900 -20.20200 1.000 27.46810 ? 25  THR B CG2 1 
ATOM   1340 N N   . ASP B 1 27  ? 20.36200  33.84700 -21.85600 1.000 32.56504 ? 26  ASP B N   1 
ATOM   1341 C CA  . ASP B 1 27  ? 21.32300  34.35400 -22.82400 1.000 26.22264 ? 26  ASP B CA  1 
ATOM   1342 C C   . ASP B 1 27  ? 21.24500  33.57900 -24.12200 1.000 27.32764 ? 26  ASP B C   1 
ATOM   1343 O O   . ASP B 1 27  ? 21.24300  34.17900 -25.20500 1.000 30.88227 ? 26  ASP B O   1 
ATOM   1344 C CB  . ASP B 1 27  ? 22.73600  34.30300 -22.23700 1.000 30.11465 ? 26  ASP B CB  1 
ATOM   1345 C CG  . ASP B 1 27  ? 23.02800  35.50200 -21.33700 1.000 40.98801 ? 26  ASP B CG  1 
ATOM   1346 O OD1 . ASP B 1 27  ? 22.28800  36.50600 -21.46000 1.000 41.73732 ? 26  ASP B OD1 1 
ATOM   1347 O OD2 . ASP B 1 27  ? 23.97900  35.45600 -20.52000 1.000 39.80408 ? 26  ASP B OD2 1 
ATOM   1348 N N   . ALA B 1 28  ? 21.16500  32.24700 -24.03300 1.000 24.56536 ? 27  ALA B N   1 
ATOM   1349 C CA  . ALA B 1 28  ? 21.06900  31.42000 -25.23400 1.000 25.30893 ? 27  ALA B CA  1 
ATOM   1350 C C   . ALA B 1 28  ? 19.87500  31.81800 -26.07500 1.000 26.61936 ? 27  ALA B C   1 
ATOM   1351 O O   . ALA B 1 28  ? 19.97300  31.91500 -27.30300 1.000 24.71357 ? 27  ALA B O   1 
ATOM   1352 C CB  . ALA B 1 28  ? 20.95800  29.94500 -24.86400 1.000 29.97492 ? 27  ALA B CB  1 
ATOM   1353 N N   . HIS B 1 29  ? 18.73700  32.05000 -25.42100 1.000 31.49496 ? 28  HIS B N   1 
ATOM   1354 C CA  . HIS B 1 29  ? 17.53900  32.47200 -26.12800 1.000 27.34184 ? 28  HIS B CA  1 
ATOM   1355 C C   . HIS B 1 29  ? 17.72500  33.85600 -26.73400 1.000 28.32054 ? 28  HIS B C   1 
ATOM   1356 O O   . HIS B 1 29  ? 17.42600  34.06900 -27.91700 1.000 31.63592 ? 28  HIS B O   1 
ATOM   1357 C CB  . HIS B 1 29  ? 16.34100  32.44600 -25.18100 1.000 33.35658 ? 28  HIS B CB  1 
ATOM   1358 C CG  . HIS B 1 29  ? 15.02800  32.56100 -25.88600 1.000 35.90851 ? 28  HIS B CG  1 
ATOM   1359 N ND1 . HIS B 1 29  ? 14.27000  31.46100 -26.22400 1.000 32.86553 ? 28  HIS B ND1 1 
ATOM   1360 C CD2 . HIS B 1 29  ? 14.35800  33.64200 -26.35100 1.000 31.20667 ? 28  HIS B CD2 1 
ATOM   1361 C CE1 . HIS B 1 29  ? 13.18400  31.86000 -26.85800 1.000 29.52304 ? 28  HIS B CE1 1 
ATOM   1362 N NE2 . HIS B 1 29  ? 13.21100  33.17800 -26.94300 1.000 34.14592 ? 28  HIS B NE2 1 
ATOM   1363 N N   . ARG B 1 30  ? 18.21400  34.81300 -25.93800 1.000 28.36212 ? 29  ARG B N   1 
ATOM   1364 C CA  . ARG B 1 30  ? 18.52400  36.14000 -26.47200 1.000 30.69551 ? 29  ARG B CA  1 
ATOM   1365 C C   . ARG B 1 30  ? 19.48000  36.03500 -27.65600 1.000 30.61657 ? 29  ARG B C   1 
ATOM   1366 O O   . ARG B 1 30  ? 19.22700  36.59300 -28.73100 1.000 31.18973 ? 29  ARG B O   1 
ATOM   1367 C CB  . ARG B 1 30  ? 19.12800  37.03100 -25.37900 1.000 32.55321 ? 29  ARG B CB  1 
ATOM   1368 C CG  . ARG B 1 30  ? 18.84900  38.52500 -25.52700 1.000 32.31765 ? 29  ARG B CG  1 
ATOM   1369 C CD  . ARG B 1 30  ? 19.54400  39.11800 -26.73800 1.000 35.30872 ? 29  ARG B CD  1 
ATOM   1370 N NE  . ARG B 1 30  ? 19.97300  40.49800 -26.54400 1.000 46.29841 ? 29  ARG B NE  1 
ATOM   1371 C CZ  . ARG B 1 30  ? 19.21800  41.57000 -26.75100 1.000 51.57719 ? 29  ARG B CZ  1 
ATOM   1372 N NH1 . ARG B 1 30  ? 17.97500  41.47000 -27.20700 1.000 46.83557 ? 29  ARG B NH1 1 
ATOM   1373 N NH2 . ARG B 1 30  ? 19.73200  42.77700 -26.51900 1.000 50.26916 ? 29  ARG B NH2 1 
ATOM   1374 N N   . GLY B 1 31  ? 20.59100  35.32300 -27.47500 1.000 28.39366 ? 30  GLY B N   1 
ATOM   1375 C CA  . GLY B 1 31  ? 21.57400  35.24000 -28.53700 1.000 28.52800 ? 30  GLY B CA  1 
ATOM   1376 C C   . GLY B 1 31  ? 21.00700  34.65400 -29.80700 1.000 32.54584 ? 30  GLY B C   1 
ATOM   1377 O O   . GLY B 1 31  ? 21.38000  35.06200 -30.90700 1.000 39.74424 ? 30  GLY B O   1 
ATOM   1378 N N   . LEU B 1 32  ? 20.07700  33.72100 -29.68300 1.000 33.48786 ? 31  LEU B N   1 
ATOM   1379 C CA  . LEU B 1 32  ? 19.63600  33.02000 -30.87400 1.000 32.70350 ? 31  LEU B CA  1 
ATOM   1380 C C   . LEU B 1 32  ? 18.38000  33.64400 -31.48000 1.000 35.48757 ? 31  LEU B C   1 
ATOM   1381 O O   . LEU B 1 32  ? 18.34500  33.90500 -32.68600 1.000 30.08601 ? 31  LEU B O   1 
ATOM   1382 C CB  . LEU B 1 32  ? 19.44000  31.53900 -30.53500 1.000 35.36364 ? 31  LEU B CB  1 
ATOM   1383 C CG  . LEU B 1 32  ? 20.81700  30.87600 -30.39700 1.000 32.47569 ? 31  LEU B CG  1 
ATOM   1384 C CD1 . LEU B 1 32  ? 20.79800  29.73700 -29.41700 1.000 27.18510 ? 31  LEU B CD1 1 
ATOM   1385 C CD2 . LEU B 1 32  ? 21.30700  30.40100 -31.75400 1.000 29.30116 ? 31  LEU B CD2 1 
ATOM   1386 N N   . THR B 1 33  ? 17.34800  33.91200 -30.66600 1.000 38.04700 ? 32  THR B N   1 
ATOM   1387 C CA  . THR B 1 33  ? 16.08900  34.40100 -31.22700 1.000 33.60718 ? 32  THR B CA  1 
ATOM   1388 C C   . THR B 1 33  ? 16.13400  35.88900 -31.53700 1.000 38.91384 ? 32  THR B C   1 
ATOM   1389 O O   . THR B 1 33  ? 15.50000  36.34400 -32.50300 1.000 36.47559 ? 32  THR B O   1 
ATOM   1390 C CB  . THR B 1 33  ? 14.92800  34.12500 -30.27200 1.000 33.74988 ? 32  THR B CB  1 
ATOM   1391 O OG1 . THR B 1 33  ? 15.02500  35.00400 -29.14500 1.000 36.14767 ? 32  THR B OG1 1 
ATOM   1392 C CG2 . THR B 1 33  ? 14.92600  32.66800 -29.81200 1.000 28.71910 ? 32  THR B CG2 1 
ATOM   1393 N N   . GLY B 1 34  ? 16.88000  36.65300 -30.74100 1.000 36.03215 ? 33  GLY B N   1 
ATOM   1394 C CA  . GLY B 1 34  ? 16.83600  38.09000 -30.77800 1.000 31.76148 ? 33  GLY B CA  1 
ATOM   1395 C C   . GLY B 1 34  ? 15.89900  38.70000 -29.76400 1.000 37.51217 ? 33  GLY B C   1 
ATOM   1396 O O   . GLY B 1 34  ? 16.04000  39.89300 -29.44200 1.000 39.69142 ? 33  GLY B O   1 
ATOM   1397 N N   . ALA B 1 35  ? 14.95000  37.91200 -29.25200 1.000 40.37331 ? 34  ALA B N   1 
ATOM   1398 C CA  . ALA B 1 35  ? 14.02100  38.40400 -28.24600 1.000 42.22988 ? 34  ALA B CA  1 
ATOM   1399 C C   . ALA B 1 35  ? 14.80000  39.02300 -27.10200 1.000 35.52849 ? 34  ALA B C   1 
ATOM   1400 O O   . ALA B 1 35  ? 15.88000  38.54800 -26.74500 1.000 40.62574 ? 34  ALA B O   1 
ATOM   1401 C CB  . ALA B 1 35  ? 13.12900  37.27100 -27.73000 1.000 35.67769 ? 34  ALA B CB  1 
ATOM   1402 N N   . GLN B 1 36  ? 14.26500  40.10700 -26.55500 1.000 42.48365 ? 35  GLN B N   1 
ATOM   1403 C CA  . GLN B 1 36  ? 14.91500  40.77400 -25.43700 1.000 48.12314 ? 35  GLN B CA  1 
ATOM   1404 C C   . GLN B 1 36  ? 14.76700  39.94400 -24.16300 1.000 44.15555 ? 35  GLN B C   1 
ATOM   1405 O O   . GLN B 1 36  ? 13.73800  39.30100 -23.92400 1.000 37.18574 ? 35  GLN B O   1 
ATOM   1406 C CB  . GLN B 1 36  ? 14.33800  42.18600 -25.23200 1.000 47.93477 ? 35  GLN B CB  1 
ATOM   1407 C CG  . GLN B 1 36  ? 12.82800  42.30700 -25.47100 1.000 47.15552 ? 35  GLN B CG  1 
ATOM   1408 C CD  . GLN B 1 36  ? 12.45800  42.71600 -26.89800 1.000 48.11851 ? 35  GLN B CD  1 
ATOM   1409 O OE1 . GLN B 1 36  ? 12.93800  42.13200 -27.87200 1.000 56.83093 ? 35  GLN B OE1 1 
ATOM   1410 N NE2 . GLN B 1 36  ? 11.59500  43.72400 -27.02200 1.000 30.70975 ? 35  GLN B NE2 1 
ATOM   1411 N N   . HIS B 1 37  ? 15.82300  39.98700 -23.34100 1.000 44.49256 ? 36  HIS B N   1 
ATOM   1412 C CA  . HIS B 1 37  ? 15.94400  39.23500 -22.09400 1.000 37.47738 ? 36  HIS B CA  1 
ATOM   1413 C C   . HIS B 1 37  ? 14.64400  39.11100 -21.30000 1.000 39.92307 ? 36  HIS B C   1 
ATOM   1414 O O   . HIS B 1 37  ? 14.16400  38.00400 -21.02700 1.000 42.63688 ? 36  HIS B O   1 
ATOM   1415 C CB  . HIS B 1 37  ? 17.02000  39.89500 -21.22000 1.000 38.85811 ? 36  HIS B CB  1 
ATOM   1416 C CG  . HIS B 1 37  ? 18.41600  39.69300 -21.73100 1.000 48.85943 ? 36  HIS B CG  1 
ATOM   1417 N ND1 . HIS B 1 37  ? 19.03300  40.57800 -22.59200 1.000 51.47561 ? 36  HIS B ND1 1 
ATOM   1418 C CD2 . HIS B 1 37  ? 19.30100  38.68700 -21.52700 1.000 40.61888 ? 36  HIS B CD2 1 
ATOM   1419 C CE1 . HIS B 1 37  ? 20.24400  40.13300 -22.88200 1.000 46.35324 ? 36  HIS B CE1 1 
ATOM   1420 N NE2 . HIS B 1 37  ? 20.42700  38.98300 -22.25700 1.000 51.14733 ? 36  HIS B NE2 1 
ATOM   1421 N N   . PHE B 1 38  ? 14.06800  40.24400 -20.90700 1.000 36.40661 ? 37  PHE B N   1 
ATOM   1422 C CA  . PHE B 1 38  ? 12.96800  40.25100 -19.94700 1.000 39.27643 ? 37  PHE B CA  1 
ATOM   1423 C C   . PHE B 1 38  ? 11.69100  39.55100 -20.43600 1.000 45.48847 ? 37  PHE B C   1 
ATOM   1424 O O   . PHE B 1 38  ? 10.68300  39.53500 -19.71500 1.000 42.78953 ? 37  PHE B O   1 
ATOM   1425 C CB  . PHE B 1 38  ? 12.64200  41.69600 -19.55900 1.000 40.43113 ? 37  PHE B CB  1 
ATOM   1426 C CG  . PHE B 1 38  ? 12.36000  42.58800 -20.74100 1.000 40.71455 ? 37  PHE B CG  1 
ATOM   1427 C CD1 . PHE B 1 38  ? 11.12200  42.56000 -21.35000 1.000 38.42355 ? 37  PHE B CD1 1 
ATOM   1428 C CD2 . PHE B 1 38  ? 13.35000  43.39100 -21.28300 1.000 38.29927 ? 37  PHE B CD2 1 
ATOM   1429 C CE1 . PHE B 1 38  ? 10.85800  43.35700 -22.43600 1.000 46.23119 ? 37  PHE B CE1 1 
ATOM   1430 C CE2 . PHE B 1 38  ? 13.09500  44.18800 -22.37000 1.000 40.78177 ? 37  PHE B CE2 1 
ATOM   1431 C CZ  . PHE B 1 38  ? 11.84800  44.17600 -22.94700 1.000 44.23236 ? 37  PHE B CZ  1 
ATOM   1432 N N   . LEU B 1 39  ? 11.69000  39.01100 -21.66100 1.000 37.86010 ? 38  LEU B N   1 
ATOM   1433 C CA  . LEU B 1 39  ? 10.60200  38.14300 -22.09800 1.000 36.89468 ? 38  LEU B CA  1 
ATOM   1434 C C   . LEU B 1 39  ? 10.88600  36.69000 -21.77100 1.000 39.30549 ? 38  LEU B C   1 
ATOM   1435 O O   . LEU B 1 39  ? 9.98600   35.84900 -21.90800 1.000 36.37001 ? 38  LEU B O   1 
ATOM   1436 C CB  . LEU B 1 39  ? 10.34100  38.26000 -23.61500 1.000 37.38833 ? 38  LEU B CB  1 
ATOM   1437 C CG  . LEU B 1 39  ? 10.12800  39.60900 -24.30500 1.000 39.76280 ? 38  LEU B CG  1 
ATOM   1438 C CD1 . LEU B 1 39  ? 9.96700   39.42600 -25.82000 1.000 44.94305 ? 38  LEU B CD1 1 
ATOM   1439 C CD2 . LEU B 1 39  ? 8.92700   40.30800 -23.72000 1.000 37.48562 ? 38  LEU B CD2 1 
ATOM   1440 N N   . ALA B 1 40  ? 12.11900  36.39100 -21.35100 1.000 34.49789 ? 39  ALA B N   1 
ATOM   1441 C CA  . ALA B 1 40  ? 12.56100  35.02800 -21.07800 1.000 30.26709 ? 39  ALA B CA  1 
ATOM   1442 C C   . ALA B 1 40  ? 12.35100  34.74000 -19.60000 1.000 29.76502 ? 39  ALA B C   1 
ATOM   1443 O O   . ALA B 1 40  ? 13.02400  35.32000 -18.74100 1.000 32.07411 ? 39  ALA B O   1 
ATOM   1444 C CB  . ALA B 1 40  ? 14.02400  34.84600 -21.46700 1.000 26.79567 ? 39  ALA B CB  1 
ATOM   1445 N N   . GLN B 1 41  ? 11.39400  33.87600 -19.30100 1.000 26.02768 ? 40  GLN B N   1 
ATOM   1446 C CA  . GLN B 1 41  ? 11.14100  33.45100 -17.93900 1.000 23.41132 ? 40  GLN B CA  1 
ATOM   1447 C C   . GLN B 1 41  ? 11.81200  32.10000 -17.72400 1.000 26.05698 ? 40  GLN B C   1 
ATOM   1448 O O   . GLN B 1 41  ? 11.75400  31.22200 -18.58600 1.000 28.98207 ? 40  GLN B O   1 
ATOM   1449 C CB  . GLN B 1 41  ? 9.63900   33.35600 -17.64900 1.000 18.36145 ? 40  GLN B CB  1 
ATOM   1450 C CG  . GLN B 1 41  ? 9.34800   32.65900 -16.33100 1.000 25.16502 ? 40  GLN B CG  1 
ATOM   1451 C CD  . GLN B 1 41  ? 7.90900   32.73500 -15.85200 1.000 24.47711 ? 40  GLN B CD  1 
ATOM   1452 O OE1 . GLN B 1 41  ? 7.54800   32.04600 -14.89000 1.000 28.65389 ? 40  GLN B OE1 1 
ATOM   1453 N NE2 . GLN B 1 41  ? 7.09100   33.57300 -16.48900 1.000 17.57006 ? 40  GLN B NE2 1 
ATOM   1454 N N   . VAL B 1 42  ? 12.47800  31.93900 -16.58900 1.000 20.61252 ? 41  VAL B N   1 
ATOM   1455 C CA  . VAL B 1 42  ? 12.99300  30.64400 -16.19000 1.000 23.14969 ? 41  VAL B CA  1 
ATOM   1456 C C   . VAL B 1 42  ? 12.35100  30.32900 -14.84800 1.000 26.36284 ? 41  VAL B C   1 
ATOM   1457 O O   . VAL B 1 42  ? 12.46800  31.10900 -13.89500 1.000 27.60055 ? 41  VAL B O   1 
ATOM   1458 C CB  . VAL B 1 42  ? 14.53000  30.60800 -16.12400 1.000 19.24652 ? 41  VAL B CB  1 
ATOM   1459 C CG1 . VAL B 1 42  ? 15.01200  29.24000 -15.67700 1.000 21.76423 ? 41  VAL B CG1 1 
ATOM   1460 C CG2 . VAL B 1 42  ? 15.11600  30.91600 -17.47300 1.000 18.41674 ? 41  VAL B CG2 1 
ATOM   1461 N N   . ASN B 1 43  ? 11.65000  29.20500 -14.79200 1.000 26.25263 ? 42  ASN B N   1 
ATOM   1462 C CA  . ASN B 1 43  ? 10.82100  28.79800 -13.66900 1.000 26.07383 ? 42  ASN B CA  1 
ATOM   1463 C C   . ASN B 1 43  ? 11.39700  27.49400 -13.14500 1.000 24.97879 ? 42  ASN B C   1 
ATOM   1464 O O   . ASN B 1 43  ? 11.25700  26.45100 -13.79000 1.000 30.17332 ? 42  ASN B O   1 
ATOM   1465 C CB  . ASN B 1 43  ? 9.38100   28.60500 -14.13500 1.000 26.85051 ? 42  ASN B CB  1 
ATOM   1466 C CG  . ASN B 1 43  ? 8.38100   28.85300 -13.05400 1.000 25.55912 ? 42  ASN B CG  1 
ATOM   1467 O OD1 . ASN B 1 43  ? 8.44800   28.24900 -11.99100 1.000 24.16431 ? 42  ASN B OD1 1 
ATOM   1468 N ND2 . ASN B 1 43  ? 7.44000   29.76000 -13.31600 1.000 19.90293 ? 42  ASN B ND2 1 
ATOM   1469 N N   . PHE B 1 44  ? 12.05400  27.53900 -11.99900 1.000 24.93789 ? 43  PHE B N   1 
ATOM   1470 C CA  . PHE B 1 44  ? 12.62600  26.32000 -11.44900 1.000 22.70494 ? 43  PHE B CA  1 
ATOM   1471 C C   . PHE B 1 44  ? 11.56100  25.53400 -10.70800 1.000 24.10999 ? 43  PHE B C   1 
ATOM   1472 O O   . PHE B 1 44  ? 10.84300  26.09400 -9.86900  1.000 24.54821 ? 43  PHE B O   1 
ATOM   1473 C CB  . PHE B 1 44  ? 13.77800  26.64800 -10.51300 1.000 23.39167 ? 43  PHE B CB  1 
ATOM   1474 C CG  . PHE B 1 44  ? 15.02000  27.02500 -11.22200 1.000 23.25535 ? 43  PHE B CG  1 
ATOM   1475 C CD1 . PHE B 1 44  ? 15.81700  26.05500 -11.79100 1.000 23.84936 ? 43  PHE B CD1 1 
ATOM   1476 C CD2 . PHE B 1 44  ? 15.39800  28.34700 -11.32800 1.000 25.10260 ? 43  PHE B CD2 1 
ATOM   1477 C CE1 . PHE B 1 44  ? 16.96200  26.39300 -12.45400 1.000 20.59097 ? 43  PHE B CE1 1 
ATOM   1478 C CE2 . PHE B 1 44  ? 16.55800  28.69400 -11.99700 1.000 27.26664 ? 43  PHE B CE2 1 
ATOM   1479 C CZ  . PHE B 1 44  ? 17.33800  27.71100 -12.55500 1.000 22.28416 ? 43  PHE B CZ  1 
ATOM   1480 N N   . GLN B 1 45  ? 11.47300  24.23200 -10.99700 1.000 23.80168 ? 44  GLN B N   1 
ATOM   1481 C CA  . GLN B 1 45  ? 10.52200  23.34600 -10.32400 1.000 25.85716 ? 44  GLN B CA  1 
ATOM   1482 C C   . GLN B 1 45  ? 11.29700  22.29800 -9.53800  1.000 22.87435 ? 44  GLN B C   1 
ATOM   1483 O O   . GLN B 1 45  ? 11.69300  21.26300 -10.07900 1.000 22.75171 ? 44  GLN B O   1 
ATOM   1484 C CB  . GLN B 1 45  ? 9.56400   22.68200 -11.30800 1.000 22.17224 ? 44  GLN B CB  1 
ATOM   1485 C CG  . GLN B 1 45  ? 8.65600   23.62300 -12.04700 1.000 23.50266 ? 44  GLN B CG  1 
ATOM   1486 C CD  . GLN B 1 45  ? 7.71200   24.36600 -11.13500 1.000 18.91624 ? 44  GLN B CD  1 
ATOM   1487 O OE1 . GLN B 1 45  ? 7.80400   25.58000 -10.98500 1.000 18.07655 ? 44  GLN B OE1 1 
ATOM   1488 N NE2 . GLN B 1 45  ? 6.77200   23.64500 -10.55100 1.000 22.69945 ? 44  GLN B NE2 1 
ATOM   1489 N N   . GLU B 1 46  ? 11.46200  22.54500 -8.25000  1.000 20.97967 ? 45  GLU B N   1 
ATOM   1490 C CA  . GLU B 1 46  ? 12.18400  21.62500 -7.39100  1.000 22.04809 ? 45  GLU B CA  1 
ATOM   1491 C C   . GLU B 1 46  ? 11.28400  20.49700 -6.91300  1.000 24.78885 ? 45  GLU B C   1 
ATOM   1492 O O   . GLU B 1 46  ? 10.15400  20.73300 -6.46600  1.000 31.50061 ? 45  GLU B O   1 
ATOM   1493 C CB  . GLU B 1 46  ? 12.75700  22.38200 -6.19100  1.000 33.78712 ? 45  GLU B CB  1 
ATOM   1494 C CG  . GLU B 1 46  ? 13.96300  23.27800 -6.51700  1.000 29.20716 ? 45  GLU B CG  1 
ATOM   1495 C CD  . GLU B 1 46  ? 14.46600  24.01700 -5.30500  1.000 32.01647 ? 45  GLU B CD  1 
ATOM   1496 O OE1 . GLU B 1 46  ? 13.62900  24.65900 -4.63300  1.000 38.11602 ? 45  GLU B OE1 1 
ATOM   1497 O OE2 . GLU B 1 46  ? 15.68600  23.96100 -5.02600  1.000 32.36128 ? 45  GLU B OE2 1 
ATOM   1498 N N   . GLN B 1 47  ? 11.79400  19.27400 -6.98900  1.000 27.53661 ? 46  GLN B N   1 
ATOM   1499 C CA  . GLN B 1 47  ? 11.19300  18.11000 -6.35200  1.000 28.72189 ? 46  GLN B CA  1 
ATOM   1500 C C   . GLN B 1 47  ? 12.26500  17.35100 -5.58700  1.000 26.17547 ? 46  GLN B C   1 
ATOM   1501 O O   . GLN B 1 47  ? 13.43300  17.34700 -5.99000  1.000 26.31156 ? 46  GLN B O   1 
ATOM   1502 C CB  . GLN B 1 47  ? 10.53900  17.15500 -7.36700  1.000 25.91643 ? 46  GLN B CB  1 
ATOM   1503 C CG  . GLN B 1 47  ? 9.30600   17.68600 -8.06300  1.000 24.63083 ? 46  GLN B CG  1 
ATOM   1504 C CD  . GLN B 1 47  ? 8.13900   17.78500 -7.15500  1.000 25.45913 ? 46  GLN B CD  1 
ATOM   1505 O OE1 . GLN B 1 47  ? 7.75300   16.80700 -6.50600  1.000 27.50363 ? 46  GLN B OE1 1 
ATOM   1506 N NE2 . GLN B 1 47  ? 7.55700   18.97200 -7.08700  1.000 25.29517 ? 46  GLN B NE2 1 
ATOM   1507 N N   . PRO B 1 48  ? 11.89600  16.68400 -4.49900  1.000 23.04397 ? 47  PRO B N   1 
ATOM   1508 C CA  . PRO B 1 48  ? 12.88600  15.90800 -3.74800  1.000 27.30190 ? 47  PRO B CA  1 
ATOM   1509 C C   . PRO B 1 48  ? 13.39900  14.73100 -4.55800  1.000 28.10861 ? 47  PRO B C   1 
ATOM   1510 O O   . PRO B 1 48  ? 12.70800  14.18800 -5.42500  1.000 30.38985 ? 47  PRO B O   1 
ATOM   1511 C CB  . PRO B 1 48  ? 12.11600  15.43500 -2.51200  1.000 29.64729 ? 47  PRO B CB  1 
ATOM   1512 C CG  . PRO B 1 48  ? 10.67200  15.52400 -2.88400  1.000 28.79049 ? 47  PRO B CG  1 
ATOM   1513 C CD  . PRO B 1 48  ? 10.55600  16.62700 -3.89300  1.000 30.68065 ? 47  PRO B CD  1 
ATOM   1514 N N   . ALA B 1 49  ? 14.63400  14.33700 -4.25800  1.000 27.73996 ? 48  ALA B N   1 
ATOM   1515 C CA  . ALA B 1 49  ? 15.29800  13.29700 -5.02000  1.000 32.59714 ? 48  ALA B CA  1 
ATOM   1516 C C   . ALA B 1 49  ? 14.48700  11.99800 -4.98000  1.000 33.85889 ? 48  ALA B C   1 
ATOM   1517 O O   . ALA B 1 49  ? 13.69000  11.75300 -4.07000  1.000 35.64632 ? 48  ALA B O   1 
ATOM   1518 C CB  . ALA B 1 49  ? 16.71200  13.09200 -4.48300  1.000 29.90153 ? 48  ALA B CB  1 
ATOM   1519 N N   . GLY B 1 50  ? 14.67500  11.16500 -6.00000  1.000 30.10539 ? 49  GLY B N   1 
ATOM   1520 C CA  . GLY B 1 50  ? 13.87600  9.95800  -6.08100  1.000 29.38857 ? 49  GLY B CA  1 
ATOM   1521 C C   . GLY B 1 50  ? 12.48200  10.14500 -6.63500  1.000 27.66145 ? 49  GLY B C   1 
ATOM   1522 O O   . GLY B 1 50  ? 11.71000  9.18300  -6.65900  1.000 32.14887 ? 49  GLY B O   1 
ATOM   1523 N N   . ASN B 1 51  ? 12.12500  11.34600 -7.08600  1.000 26.66912 ? 50  ASN B N   1 
ATOM   1524 C CA  . ASN B 1 51  ? 10.86500  11.53300 -7.78800  1.000 25.69317 ? 50  ASN B CA  1 
ATOM   1525 C C   . ASN B 1 51  ? 10.96600  11.30200 -9.29700  1.000 27.27764 ? 50  ASN B C   1 
ATOM   1526 O O   . ASN B 1 51  ? 9.93100   11.17600 -9.95900  1.000 27.39470 ? 50  ASN B O   1 
ATOM   1527 C CB  . ASN B 1 51  ? 10.31700  12.93300 -7.50100  1.000 25.00850 ? 50  ASN B CB  1 
ATOM   1528 C CG  . ASN B 1 51  ? 9.73000   13.04500 -6.09800  1.000 33.57343 ? 50  ASN B CG  1 
ATOM   1529 O OD1 . ASN B 1 51  ? 10.30900  12.53600 -5.13100  1.000 36.45225 ? 50  ASN B OD1 1 
ATOM   1530 N ND2 . ASN B 1 51  ? 8.57800   13.69900 -5.97900  1.000 33.92387 ? 50  ASN B ND2 1 
ATOM   1531 N N   . VAL B 1 52  ? 12.15800  11.23400 -9.86700  1.000 23.06960 ? 51  VAL B N   1 
ATOM   1532 C CA  . VAL B 1 52  ? 12.27700  10.96100 -11.29400 1.000 26.22332 ? 51  VAL B CA  1 
ATOM   1533 C C   . VAL B 1 52  ? 12.60700  9.48900  -11.47600 1.000 29.74118 ? 51  VAL B C   1 
ATOM   1534 O O   . VAL B 1 52  ? 13.22800  8.85600  -10.61500 1.000 35.05340 ? 51  VAL B O   1 
ATOM   1535 C CB  . VAL B 1 52  ? 13.32800  11.85200 -11.98700 1.000 21.38163 ? 51  VAL B CB  1 
ATOM   1536 C CG1 . VAL B 1 52  ? 13.09900  11.83400 -13.47300 1.000 27.35065 ? 51  VAL B CG1 1 
ATOM   1537 C CG2 . VAL B 1 52  ? 13.26400  13.26100 -11.46300 1.000 17.72395 ? 51  VAL B CG2 1 
ATOM   1538 N N   . PHE B 1 53  ? 12.17900  8.93400  -12.60400 1.000 27.41077 ? 52  PHE B N   1 
ATOM   1539 C CA  . PHE B 1 53  ? 12.35500  7.51700  -12.90500 1.000 30.71798 ? 52  PHE B CA  1 
ATOM   1540 C C   . PHE B 1 53  ? 12.71800  7.37200  -14.37600 1.000 37.57598 ? 52  PHE B C   1 
ATOM   1541 O O   . PHE B 1 53  ? 12.01600  7.90200  -15.24500 1.000 34.73152 ? 52  PHE B O   1 
ATOM   1542 C CB  . PHE B 1 53  ? 11.08000  6.72300  -12.59200 1.000 25.40824 ? 52  PHE B CB  1 
ATOM   1543 C CG  . PHE B 1 53  ? 10.86000  6.49100  -11.12900 1.000 30.31939 ? 52  PHE B CG  1 
ATOM   1544 C CD1 . PHE B 1 53  ? 10.37800  7.50500  -10.31300 1.000 29.32209 ? 52  PHE B CD1 1 
ATOM   1545 C CD2 . PHE B 1 53  ? 11.13800  5.25800  -10.56000 1.000 31.35644 ? 52  PHE B CD2 1 
ATOM   1546 C CE1 . PHE B 1 53  ? 10.18500  7.30100  -8.95800  1.000 26.35342 ? 52  PHE B CE1 1 
ATOM   1547 C CE2 . PHE B 1 53  ? 10.94500  5.04600  -9.20600  1.000 31.72437 ? 52  PHE B CE2 1 
ATOM   1548 C CZ  . PHE B 1 53  ? 10.46700  6.07000  -8.40300  1.000 32.58634 ? 52  PHE B CZ  1 
ATOM   1549 N N   . LEU B 1 54  ? 13.82200  6.68400  -14.65600 1.000 33.68230 ? 53  LEU B N   1 
ATOM   1550 C CA  . LEU B 1 54  ? 14.24800  6.43700  -16.02600 1.000 28.35011 ? 53  LEU B CA  1 
ATOM   1551 C C   . LEU B 1 54  ? 14.22300  4.93700  -16.27300 1.000 34.33958 ? 53  LEU B C   1 
ATOM   1552 O O   . LEU B 1 54  ? 14.77200  4.17100  -15.47800 1.000 38.92876 ? 53  LEU B O   1 
ATOM   1553 C CB  . LEU B 1 54  ? 15.63100  7.00800  -16.27900 1.000 26.65960 ? 53  LEU B CB  1 
ATOM   1554 C CG  . LEU B 1 54  ? 15.80700  8.49900  -16.02400 1.000 29.94157 ? 53  LEU B CG  1 
ATOM   1555 C CD1 . LEU B 1 54  ? 17.24300  8.90700  -16.36000 1.000 32.61197 ? 53  LEU B CD1 1 
ATOM   1556 C CD2 . LEU B 1 54  ? 14.85300  9.29200  -16.82400 1.000 26.93865 ? 53  LEU B CD2 1 
ATOM   1557 N N   . GLY B 1 55  ? 13.56800  4.52200  -17.35900 1.000 37.32937 ? 54  GLY B N   1 
ATOM   1558 C CA  . GLY B 1 55  ? 13.29800  3.11600  -17.60500 1.000 39.50117 ? 54  GLY B CA  1 
ATOM   1559 C C   . GLY B 1 55  ? 12.76000  2.36900  -16.39700 1.000 40.21329 ? 54  GLY B C   1 
ATOM   1560 O O   . GLY B 1 55  ? 13.02200  1.17300  -16.22700 1.000 41.32929 ? 54  GLY B O   1 
ATOM   1561 N N   . GLY B 1 56  ? 12.00800  3.06000  -15.54400 1.000 34.27068 ? 55  GLY B N   1 
ATOM   1562 C CA  . GLY B 1 56  ? 11.50900  2.45900  -14.32800 1.000 36.68895 ? 55  GLY B CA  1 
ATOM   1563 C C   . GLY B 1 56  ? 12.49900  2.37700  -13.18600 1.000 36.21427 ? 55  GLY B C   1 
ATOM   1564 O O   . GLY B 1 56  ? 12.21400  1.69100  -12.20000 1.000 30.80182 ? 55  GLY B O   1 
ATOM   1565 N N   . VAL B 1 57  ? 13.64800  3.04900  -13.29200 1.000 34.10791 ? 56  VAL B N   1 
ATOM   1566 C CA  . VAL B 1 57  ? 14.70700  3.03300  -12.28400 1.000 35.08504 ? 56  VAL B CA  1 
ATOM   1567 C C   . VAL B 1 57  ? 14.67300  4.36400  -11.54300 1.000 34.18453 ? 56  VAL B C   1 
ATOM   1568 O O   . VAL B 1 57  ? 14.77700  5.42800  -12.16700 1.000 36.16195 ? 56  VAL B O   1 
ATOM   1569 C CB  . VAL B 1 57  ? 16.08900  2.81000  -12.92100 1.000 34.56663 ? 56  VAL B CB  1 
ATOM   1570 C CG1 . VAL B 1 57  ? 17.16200  3.00300  -11.89600 1.000 26.85611 ? 56  VAL B CG1 1 
ATOM   1571 C CG2 . VAL B 1 57  ? 16.18500  1.43900  -13.56000 1.000 35.79610 ? 56  VAL B CG2 1 
ATOM   1572 N N   . GLN B 1 58  ? 14.52400  4.31600  -10.22000 1.000 30.96605 ? 57  GLN B N   1 
ATOM   1573 C CA  . GLN B 1 58  ? 14.53300  5.54800  -9.43900  1.000 33.04934 ? 57  GLN B CA  1 
ATOM   1574 C C   . GLN B 1 58  ? 15.87100  6.27400  -9.59300  1.000 34.01663 ? 57  GLN B C   1 
ATOM   1575 O O   . GLN B 1 58  ? 16.93800  5.65300  -9.61600  1.000 29.64328 ? 57  GLN B O   1 
ATOM   1576 C CB  . GLN B 1 58  ? 14.25000  5.23900  -7.96400  1.000 32.16912 ? 57  GLN B CB  1 
ATOM   1577 C CG  . GLN B 1 58  ? 13.83900  6.45300  -7.12100  1.000 32.72224 ? 57  GLN B CG  1 
ATOM   1578 C CD  . GLN B 1 58  ? 13.80600  6.14400  -5.63400  1.000 28.89765 ? 57  GLN B CD  1 
ATOM   1579 O OE1 . GLN B 1 58  ? 13.61200  7.02800  -4.80300  1.000 31.86169 ? 57  GLN B OE1 1 
ATOM   1580 N NE2 . GLN B 1 58  ? 13.98100  4.87900  -5.29500  1.000 31.76115 ? 57  GLN B NE2 1 
ATOM   1581 N N   . GLN B 1 59  ? 15.81200  7.60000  -9.71800  1.000 33.73582 ? 58  GLN B N   1 
ATOM   1582 C CA  . GLN B 1 59  ? 17.00000  8.41900  -9.92300  1.000 38.10463 ? 58  GLN B CA  1 
ATOM   1583 C C   . GLN B 1 59  ? 17.32900  9.22600  -8.67000  1.000 40.30997 ? 58  GLN B C   1 
ATOM   1584 O O   . GLN B 1 59  ? 16.45000  9.55000  -7.86000  1.000 40.41027 ? 58  GLN B O   1 
ATOM   1585 C CB  . GLN B 1 59  ? 16.82600  9.37200  -11.11200 1.000 31.13337 ? 58  GLN B CB  1 
ATOM   1586 C CG  . GLN B 1 59  ? 16.53400  8.65900  -12.45500 1.000 39.50924 ? 58  GLN B CG  1 
ATOM   1587 C CD  . GLN B 1 59  ? 17.71400  7.85000  -13.01000 1.000 30.21296 ? 58  GLN B CD  1 
ATOM   1588 O OE1 . GLN B 1 59  ? 18.66000  8.41200  -13.55900 1.000 31.49385 ? 58  GLN B OE1 1 
ATOM   1589 N NE2 . GLN B 1 59  ? 17.63700  6.52700  -12.89600 1.000 28.91752 ? 58  GLN B NE2 1 
ATOM   1590 N N   . GLY B 1 60  ? 18.61200  9.54600  -8.52000  1.000 31.45587 ? 59  GLY B N   1 
ATOM   1591 C CA  . GLY B 1 60  ? 19.04900  10.38600 -7.42900  1.000 28.74753 ? 59  GLY B CA  1 
ATOM   1592 C C   . GLY B 1 60  ? 18.59300  11.82700 -7.57300  1.000 37.86703 ? 59  GLY B C   1 
ATOM   1593 O O   . GLY B 1 60  ? 17.39600  12.12300 -7.50400  1.000 38.52133 ? 59  GLY B O   1 
ATOM   1594 N N   . GLY B 1 61  ? 19.54100  12.73800 -7.77800  1.000 39.10044 ? 60  GLY B N   1 
ATOM   1595 C CA  . GLY B 1 61  ? 19.20600  14.14300 -7.80600  1.000 31.53472 ? 60  GLY B CA  1 
ATOM   1596 C C   . GLY B 1 61  ? 19.87100  14.93000 -8.90900  1.000 30.75445 ? 60  GLY B C   1 
ATOM   1597 O O   . GLY B 1 61  ? 19.86800  16.15800 -8.86600  1.000 35.78779 ? 60  GLY B O   1 
ATOM   1598 N N   . ASP B 1 62  ? 20.42400  14.25100 -9.90600  1.000 25.76321 ? 61  ASP B N   1 
ATOM   1599 C CA  . ASP B 1 62  ? 21.18300  14.90700 -10.96100 1.000 33.55325 ? 61  ASP B CA  1 
ATOM   1600 C C   . ASP B 1 62  ? 20.38900  15.18300 -12.23900 1.000 32.04532 ? 61  ASP B C   1 
ATOM   1601 O O   . ASP B 1 62  ? 20.94500  15.80400 -13.14600 1.000 38.76259 ? 61  ASP B O   1 
ATOM   1602 C CB  . ASP B 1 62  ? 22.42100  14.07000 -11.32300 1.000 41.43248 ? 61  ASP B CB  1 
ATOM   1603 C CG  . ASP B 1 62  ? 23.65200  14.44700 -10.51000 1.000 44.93205 ? 61  ASP B CG  1 
ATOM   1604 O OD1 . ASP B 1 62  ? 23.51900  15.22300 -9.53400  1.000 38.42290 ? 61  ASP B OD1 1 
ATOM   1605 O OD2 . ASP B 1 62  ? 24.74800  13.93900 -10.83300 1.000 50.81348 ? 61  ASP B OD2 1 
ATOM   1606 N N   . THR B 1 63  ? 19.13000  14.75100 -12.35900 1.000 28.05120 ? 62  THR B N   1 
ATOM   1607 C CA  . THR B 1 63  ? 18.41300  14.93800 -13.61800 1.000 25.45122 ? 62  THR B CA  1 
ATOM   1608 C C   . THR B 1 63  ? 17.97000  16.38900 -13.78400 1.000 25.79787 ? 62  THR B C   1 
ATOM   1609 O O   . THR B 1 63  ? 17.63100  17.06400 -12.81000 1.000 27.40578 ? 62  THR B O   1 
ATOM   1610 C CB  . THR B 1 63  ? 17.19000  14.02700 -13.71600 1.000 27.75114 ? 62  THR B CB  1 
ATOM   1611 O OG1 . THR B 1 63  ? 17.52400  12.69500 -13.31900 1.000 23.07942 ? 62  THR B OG1 1 
ATOM   1612 C CG2 . THR B 1 63  ? 16.69900  13.97700 -15.16600 1.000 33.63375 ? 62  THR B CG2 1 
ATOM   1613 N N   . ILE B 1 64  ? 18.00400  16.87600 -15.02300 1.000 24.11401 ? 63  ILE B N   1 
ATOM   1614 C CA  . ILE B 1 64  ? 17.48500  18.19400 -15.37200 1.000 29.09448 ? 63  ILE B CA  1 
ATOM   1615 C C   . ILE B 1 64  ? 16.59800  18.04600 -16.59400 1.000 27.26782 ? 63  ILE B C   1 
ATOM   1616 O O   . ILE B 1 64  ? 17.05800  17.59600 -17.65100 1.000 32.04472 ? 63  ILE B O   1 
ATOM   1617 C CB  . ILE B 1 64  ? 18.58500  19.22100 -15.67000 1.000 31.54021 ? 63  ILE B CB  1 
ATOM   1618 C CG1 . ILE B 1 64  ? 19.69000  19.19000 -14.63300 1.000 31.32037 ? 63  ILE B CG1 1 
ATOM   1619 C CG2 . ILE B 1 64  ? 17.99300  20.62900 -15.75300 1.000 30.37311 ? 63  ILE B CG2 1 
ATOM   1620 C CD1 . ILE B 1 64  ? 20.91600  19.91900 -15.11800 1.000 29.38536 ? 63  ILE B CD1 1 
ATOM   1621 N N   . PHE B 1 65  ? 15.34300  18.44100 -16.46400 1.000 25.33856 ? 64  PHE B N   1 
ATOM   1622 C CA  . PHE B 1 65  ? 14.41800  18.46200 -17.58800 1.000 25.18702 ? 64  PHE B CA  1 
ATOM   1623 C C   . PHE B 1 65  ? 14.09200  19.91800 -17.89400 1.000 27.12694 ? 64  PHE B C   1 
ATOM   1624 O O   . PHE B 1 65  ? 13.63400  20.66100 -17.02200 1.000 29.31989 ? 64  PHE B O   1 
ATOM   1625 C CB  . PHE B 1 65  ? 13.16100  17.64600 -17.28300 1.000 24.51948 ? 64  PHE B CB  1 
ATOM   1626 C CG  . PHE B 1 65  ? 12.12600  17.66800 -18.38400 1.000 26.16043 ? 64  PHE B CG  1 
ATOM   1627 C CD1 . PHE B 1 65  ? 12.49900  17.59100 -19.72300 1.000 29.85398 ? 64  PHE B CD1 1 
ATOM   1628 C CD2 . PHE B 1 65  ? 10.77500  17.76100 -18.07700 1.000 22.85266 ? 64  PHE B CD2 1 
ATOM   1629 C CE1 . PHE B 1 65  ? 11.54200  17.60200 -20.74500 1.000 22.34098 ? 64  PHE B CE1 1 
ATOM   1630 C CE2 . PHE B 1 65  ? 9.81600   17.76800 -19.09000 1.000 26.50623 ? 64  PHE B CE2 1 
ATOM   1631 C CZ  . PHE B 1 65  ? 10.20800  17.69200 -20.42800 1.000 25.49098 ? 64  PHE B CZ  1 
ATOM   1632 N N   . VAL B 1 66  ? 14.37800  20.33700 -19.11600 1.000 28.31300 ? 65  VAL B N   1 
ATOM   1633 C CA  . VAL B 1 66  ? 14.05000  21.67000 -19.57500 1.000 23.12079 ? 65  VAL B CA  1 
ATOM   1634 C C   . VAL B 1 66  ? 12.84800  21.52000 -20.49500 1.000 24.74587 ? 65  VAL B C   1 
ATOM   1635 O O   . VAL B 1 66  ? 12.90400  20.79500 -21.49400 1.000 24.80718 ? 65  VAL B O   1 
ATOM   1636 C CB  . VAL B 1 66  ? 15.25500  22.33500 -20.25600 1.000 24.90121 ? 65  VAL B CB  1 
ATOM   1637 C CG1 . VAL B 1 66  ? 14.91400  23.75100 -20.74500 1.000 21.89367 ? 65  VAL B CG1 1 
ATOM   1638 C CG2 . VAL B 1 66  ? 16.42500  22.37200 -19.25900 1.000 20.38221 ? 65  VAL B CG2 1 
ATOM   1639 N N   . HIS B 1 67  ? 11.73500  22.12000 -20.10500 1.000 26.18826 ? 66  HIS B N   1 
ATOM   1640 C CA  . HIS B 1 67  ? 10.55700  22.20400 -20.95100 1.000 25.16696 ? 66  HIS B CA  1 
ATOM   1641 C C   . HIS B 1 67  ? 10.46200  23.66200 -21.37400 1.000 25.81425 ? 66  HIS B C   1 
ATOM   1642 O O   . HIS B 1 67  ? 9.96400   24.49600 -20.61600 1.000 25.76828 ? 66  HIS B O   1 
ATOM   1643 C CB  . HIS B 1 67  ? 9.29800   21.73200 -20.22700 1.000 22.99993 ? 66  HIS B CB  1 
ATOM   1644 C CG  . HIS B 1 67  ? 8.12200   21.49900 -21.14100 1.000 28.93115 ? 66  HIS B CG  1 
ATOM   1645 N ND1 . HIS B 1 67  ? 6.84500   21.24200 -20.67500 1.000 22.16890 ? 66  HIS B ND1 1 
ATOM   1646 C CD2 . HIS B 1 67  ? 8.03700   21.48400 -22.49400 1.000 22.57406 ? 66  HIS B CD2 1 
ATOM   1647 C CE1 . HIS B 1 67  ? 6.03300   21.06700 -21.70100 1.000 21.96269 ? 66  HIS B CE1 1 
ATOM   1648 N NE2 . HIS B 1 67  ? 6.73100   21.20500 -22.81500 1.000 24.40199 ? 66  HIS B NE2 1 
ATOM   1649 N N   . GLY B 1 68  ? 10.94900  23.96900 -22.57300 1.000 27.68387 ? 67  GLY B N   1 
ATOM   1650 C CA  . GLY B 1 68  ? 10.78800  25.29400 -23.13700 1.000 26.56571 ? 67  GLY B CA  1 
ATOM   1651 C C   . GLY B 1 68  ? 9.47500   25.42300 -23.90200 1.000 26.92043 ? 67  GLY B C   1 
ATOM   1652 O O   . GLY B 1 68  ? 9.16900   24.61600 -24.78900 1.000 32.03107 ? 67  GLY B O   1 
ATOM   1653 N N   . LEU B 1 69  ? 8.71100   26.44500 -23.56600 1.000 25.92199 ? 68  LEU B N   1 
ATOM   1654 C CA  . LEU B 1 69  ? 7.50300   26.78700 -24.29700 1.000 25.18597 ? 68  LEU B CA  1 
ATOM   1655 C C   . LEU B 1 69  ? 7.78200   28.06700 -25.07700 1.000 30.07243 ? 68  LEU B C   1 
ATOM   1656 O O   . LEU B 1 69  ? 8.02200   29.12200 -24.47500 1.000 29.97748 ? 68  LEU B O   1 
ATOM   1657 C CB  . LEU B 1 69  ? 6.33900   26.92900 -23.32800 1.000 26.43893 ? 68  LEU B CB  1 
ATOM   1658 C CG  . LEU B 1 69  ? 6.43500   25.79000 -22.31300 1.000 23.42464 ? 68  LEU B CG  1 
ATOM   1659 C CD1 . LEU B 1 69  ? 5.55700   25.97500 -21.09700 1.000 17.58004 ? 68  LEU B CD1 1 
ATOM   1660 C CD2 . LEU B 1 69  ? 6.10400   24.50400 -22.99500 1.000 20.06606 ? 68  LEU B CD2 1 
ATOM   1661 N N   . HIS B 1 70  ? 7.79000   27.95400 -26.41500 1.000 26.10946 ? 69  HIS B N   1 
ATOM   1662 C CA  . HIS B 1 70  ? 8.12600   29.04300 -27.32000 1.000 22.86264 ? 69  HIS B CA  1 
ATOM   1663 C C   . HIS B 1 70  ? 6.92100   29.41900 -28.18000 1.000 26.42917 ? 69  HIS B C   1 
ATOM   1664 O O   . HIS B 1 70  ? 5.95400   28.65900 -28.30700 1.000 26.48285 ? 69  HIS B O   1 
ATOM   1665 C CB  . HIS B 1 70  ? 9.28800   28.68100 -28.26500 1.000 23.56428 ? 69  HIS B CB  1 
ATOM   1666 C CG  . HIS B 1 70  ? 10.55100  28.25000 -27.57700 1.000 26.16090 ? 69  HIS B CG  1 
ATOM   1667 N ND1 . HIS B 1 70  ? 11.58600  27.63700 -28.25100 1.000 27.67509 ? 69  HIS B ND1 1 
ATOM   1668 C CD2 . HIS B 1 70  ? 10.95500  28.34600 -26.28700 1.000 31.09991 ? 69  HIS B CD2 1 
ATOM   1669 C CE1 . HIS B 1 70  ? 12.56600  27.36400 -27.41100 1.000 23.89830 ? 69  HIS B CE1 1 
ATOM   1670 N NE2 . HIS B 1 70  ? 12.20900  27.78500 -26.21100 1.000 28.78749 ? 69  HIS B NE2 1 
ATOM   1671 N N   . ARG B 1 71  ? 7.00300   30.60700 -28.78000 1.000 20.94473 ? 70  ARG B N   1 
ATOM   1672 C CA  . ARG B 1 71  ? 6.09900   30.96800 -29.85500 1.000 19.32657 ? 70  ARG B CA  1 
ATOM   1673 C C   . ARG B 1 71  ? 6.45200   30.20000 -31.12300 1.000 24.51607 ? 70  ARG B C   1 
ATOM   1674 O O   . ARG B 1 71  ? 7.62700   29.99700 -31.44400 1.000 23.87533 ? 70  ARG B O   1 
ATOM   1675 C CB  . ARG B 1 71  ? 6.15600   32.46700 -30.14000 1.000 20.50077 ? 70  ARG B CB  1 
ATOM   1676 C CG  . ARG B 1 71  ? 6.05500   33.33700 -28.92200 1.000 19.20051 ? 70  ARG B CG  1 
ATOM   1677 C CD  . ARG B 1 71  ? 6.40400   34.74700 -29.25200 1.000 24.42071 ? 70  ARG B CD  1 
ATOM   1678 N NE  . ARG B 1 71  ? 7.63300   35.16500 -28.58700 1.000 32.32502 ? 70  ARG B NE  1 
ATOM   1679 C CZ  . ARG B 1 71  ? 8.47500   36.07900 -29.05600 1.000 33.82205 ? 70  ARG B CZ  1 
ATOM   1680 N NH1 . ARG B 1 71  ? 8.25000   36.71100 -30.20200 1.000 31.96809 ? 70  ARG B NH1 1 
ATOM   1681 N NH2 . ARG B 1 71  ? 9.57300   36.36400 -28.36300 1.000 33.61471 ? 70  ARG B NH2 1 
ATOM   1682 N N   . GLU B 1 72  ? 5.41200   29.75000 -31.82600 1.000 25.64802 ? 71  GLU B N   1 
ATOM   1683 C CA  . GLU B 1 72  ? 5.53100   29.29900 -33.20300 1.000 19.19793 ? 71  GLU B CA  1 
ATOM   1684 C C   . GLU B 1 72  ? 6.23100   30.35200 -34.05100 1.000 18.66364 ? 71  GLU B C   1 
ATOM   1685 O O   . GLU B 1 72  ? 6.08700   31.55500 -33.82600 1.000 22.78274 ? 71  GLU B O   1 
ATOM   1686 C CB  . GLU B 1 72  ? 4.13000   29.02400 -33.77500 1.000 21.78827 ? 71  GLU B CB  1 
ATOM   1687 C CG  . GLU B 1 72  ? 3.43300   27.80200 -33.16300 1.000 20.90524 ? 71  GLU B CG  1 
ATOM   1688 C CD  . GLU B 1 72  ? 2.10400   27.46500 -33.81300 1.000 25.92723 ? 71  GLU B CD  1 
ATOM   1689 O OE1 . GLU B 1 72  ? 1.54800   28.30800 -34.55400 1.000 26.22277 ? 71  GLU B OE1 1 
ATOM   1690 O OE2 . GLU B 1 72  ? 1.59700   26.35100 -33.55800 1.000 28.51287 ? 71  GLU B OE2 1 
ATOM   1691 N N   . GLY B 1 73  ? 6.98700   29.90000 -35.04000 1.000 20.87287 ? 72  GLY B N   1 
ATOM   1692 C CA  . GLY B 1 73  ? 7.51800   30.80800 -36.03300 1.000 20.94688 ? 72  GLY B CA  1 
ATOM   1693 C C   . GLY B 1 73  ? 8.95000   30.51700 -36.42600 1.000 25.70902 ? 72  GLY B C   1 
ATOM   1694 O O   . GLY B 1 73  ? 9.37500   30.82600 -37.54400 1.000 24.70002 ? 72  GLY B O   1 
ATOM   1695 N N   . ARG B 1 74  ? 9.70000   29.90500 -35.52600 1.000 21.59292 ? 73  ARG B N   1 
ATOM   1696 C CA  . ARG B 1 74  ? 11.11400  29.69400 -35.76200 1.000 22.82770 ? 73  ARG B CA  1 
ATOM   1697 C C   . ARG B 1 74  ? 11.36500  28.33800 -36.42700 1.000 26.93085 ? 73  ARG B C   1 
ATOM   1698 O O   . ARG B 1 74  ? 10.54500  27.41600 -36.35600 1.000 20.14815 ? 73  ARG B O   1 
ATOM   1699 C CB  . ARG B 1 74  ? 11.87400  29.81400 -34.44200 1.000 26.02733 ? 73  ARG B CB  1 
ATOM   1700 C CG  . ARG B 1 74  ? 11.56100  31.12400 -33.74800 1.000 28.85197 ? 73  ARG B CG  1 
ATOM   1701 C CD  . ARG B 1 74  ? 12.62300  31.55500 -32.77400 1.000 24.80686 ? 73  ARG B CD  1 
ATOM   1702 N NE  . ARG B 1 74  ? 12.25300  32.79300 -32.10500 1.000 27.21158 ? 73  ARG B NE  1 
ATOM   1703 C CZ  . ARG B 1 74  ? 11.56300  32.86000 -30.97000 1.000 37.74740 ? 73  ARG B CZ  1 
ATOM   1704 N NH1 . ARG B 1 74  ? 11.15700  31.76900 -30.33300 1.000 33.84201 ? 73  ARG B NH1 1 
ATOM   1705 N NH2 . ARG B 1 74  ? 11.28500  34.05300 -30.45200 1.000 39.02791 ? 73  ARG B NH2 1 
ATOM   1706 N N   . SER B 1 75  ? 12.53300  28.22500 -37.06600 1.000 26.84490 ? 74  SER B N   1 
ATOM   1707 C CA  . SER B 1 75  ? 12.85500  27.09200 -37.92100 1.000 26.30645 ? 74  SER B CA  1 
ATOM   1708 C C   . SER B 1 75  ? 13.36400  25.91300 -37.10300 1.000 24.95707 ? 74  SER B C   1 
ATOM   1709 O O   . SER B 1 75  ? 13.81400  26.06900 -35.96900 1.000 29.03096 ? 74  SER B O   1 
ATOM   1710 C CB  . SER B 1 75  ? 13.91200  27.48200 -38.94800 1.000 26.29691 ? 74  SER B CB  1 
ATOM   1711 O OG  . SER B 1 75  ? 15.10900  27.87300 -38.30000 1.000 29.65054 ? 74  SER B OG  1 
ATOM   1712 N N   . ALA B 1 76  ? 13.30300  24.71900 -37.71000 1.000 22.91101 ? 75  ALA B N   1 
ATOM   1713 C CA  . ALA B 1 76  ? 13.85900  23.52000 -37.07900 1.000 27.97948 ? 75  ALA B CA  1 
ATOM   1714 C C   . ALA B 1 76  ? 15.34000  23.69700 -36.76300 1.000 31.52346 ? 75  ALA B C   1 
ATOM   1715 O O   . ALA B 1 76  ? 15.79900  23.38300 -35.65400 1.000 29.14986 ? 75  ALA B O   1 
ATOM   1716 C CB  . ALA B 1 76  ? 13.65900  22.30500 -37.98300 1.000 22.86677 ? 75  ALA B CB  1 
ATOM   1717 N N   . ASP B 1 77  ? 16.09900  24.22900 -37.72300 1.000 28.80971 ? 76  ASP B N   1 
ATOM   1718 C CA  . ASP B 1 77  ? 17.53000  24.42900 -37.51200 1.000 34.81765 ? 76  ASP B CA  1 
ATOM   1719 C C   . ASP B 1 77  ? 17.80700  25.33500 -36.31100 1.000 30.85897 ? 76  ASP B C   1 
ATOM   1720 O O   . ASP B 1 77  ? 18.65800  25.02300 -35.47400 1.000 28.21175 ? 76  ASP B O   1 
ATOM   1721 C CB  . ASP B 1 77  ? 18.17000  25.00800 -38.76900 1.000 26.90087 ? 76  ASP B CB  1 
ATOM   1722 C CG  . ASP B 1 77  ? 19.61200  25.30500 -38.56000 1.000 36.08965 ? 76  ASP B CG  1 
ATOM   1723 O OD1 . ASP B 1 77  ? 20.42000  24.35600 -38.65000 1.000 34.48790 ? 76  ASP B OD1 1 
ATOM   1724 O OD2 . ASP B 1 77  ? 19.92800  26.47500 -38.24500 1.000 41.31870 ? 76  ASP B OD2 1 
ATOM   1725 N N   . LEU B 1 78  ? 17.10200  26.46900 -36.22300 1.000 29.92267 ? 77  LEU B N   1 
ATOM   1726 C CA  . LEU B 1 78  ? 17.29900  27.40200 -35.11600 1.000 31.46640 ? 77  LEU B CA  1 
ATOM   1727 C C   . LEU B 1 78  ? 16.97400  26.75400 -33.77400 1.000 31.27106 ? 77  LEU B C   1 
ATOM   1728 O O   . LEU B 1 78  ? 17.67800  26.97300 -32.78000 1.000 28.73875 ? 77  LEU B O   1 
ATOM   1729 C CB  . LEU B 1 78  ? 16.43200  28.64800 -35.33100 1.000 29.35985 ? 77  LEU B CB  1 
ATOM   1730 C CG  . LEU B 1 78  ? 16.65200  29.94000 -34.53400 1.000 30.23198 ? 77  LEU B CG  1 
ATOM   1731 C CD1 . LEU B 1 78  ? 16.17200  29.80600 -33.07300 1.000 30.40092 ? 77  LEU B CD1 1 
ATOM   1732 C CD2 . LEU B 1 78  ? 18.09800  30.40500 -34.59400 1.000 34.60111 ? 77  LEU B CD2 1 
ATOM   1733 N N   . LYS B 1 79  ? 15.90500  25.96100 -33.72500 1.000 27.59418 ? 78  LYS B N   1 
ATOM   1734 C CA  . LYS B 1 79  ? 15.47400  25.39600 -32.45700 1.000 26.50604 ? 78  LYS B CA  1 
ATOM   1735 C C   . LYS B 1 79  ? 16.44000  24.33100 -31.97600 1.000 29.02862 ? 78  LYS B C   1 
ATOM   1736 O O   . LYS B 1 79  ? 16.60300  24.14200 -30.76500 1.000 30.80251 ? 78  LYS B O   1 
ATOM   1737 C CB  . LYS B 1 79  ? 14.06600  24.82400 -32.60300 1.000 27.03952 ? 78  LYS B CB  1 
ATOM   1738 C CG  . LYS B 1 79  ? 13.02800  25.84500 -32.26200 1.000 31.07659 ? 78  LYS B CG  1 
ATOM   1739 C CD  . LYS B 1 79  ? 11.60600  25.37400 -32.48000 1.000 33.75100 ? 78  LYS B CD  1 
ATOM   1740 C CE  . LYS B 1 79  ? 11.25000  25.24600 -33.94700 1.000 27.76327 ? 78  LYS B CE  1 
ATOM   1741 N NZ  . LYS B 1 79  ? 10.50700  23.98200 -34.14600 1.000 29.42503 ? 78  LYS B NZ  1 
ATOM   1742 N N   . GLY B 1 80  ? 17.08000  23.62500 -32.90800 1.000 30.31345 ? 79  GLY B N   1 
ATOM   1743 C CA  . GLY B 1 80  ? 18.06000  22.63000 -32.53100 1.000 27.45924 ? 79  GLY B CA  1 
ATOM   1744 C C   . GLY B 1 80  ? 19.37700  23.23700 -32.11600 1.000 27.42229 ? 79  GLY B C   1 
ATOM   1745 O O   . GLY B 1 80  ? 20.07500  22.67700 -31.26700 1.000 27.20750 ? 79  GLY B O   1 
ATOM   1746 N N   . GLN B 1 81  ? 19.75300  24.36500 -32.72100 1.000 30.04897 ? 80  GLN B N   1 
ATOM   1747 C CA  . GLN B 1 81  ? 20.87800  25.12800 -32.19400 1.000 29.81382 ? 80  GLN B CA  1 
ATOM   1748 C C   . GLN B 1 81  ? 20.58700  25.58000 -30.77800 1.000 28.80572 ? 80  GLN B C   1 
ATOM   1749 O O   . GLN B 1 81  ? 21.47000  25.53900 -29.91200 1.000 24.80880 ? 80  GLN B O   1 
ATOM   1750 C CB  . GLN B 1 81  ? 21.15900  26.35400 -33.05600 1.000 27.00742 ? 80  GLN B CB  1 
ATOM   1751 C CG  . GLN B 1 81  ? 22.00700  26.13700 -34.26700 1.000 27.24752 ? 80  GLN B CG  1 
ATOM   1752 C CD  . GLN B 1 81  ? 22.17200  27.43400 -35.03400 1.000 30.70136 ? 80  GLN B CD  1 
ATOM   1753 O OE1 . GLN B 1 81  ? 21.56800  27.63000 -36.09100 1.000 28.42260 ? 80  GLN B OE1 1 
ATOM   1754 N NE2 . GLN B 1 81  ? 22.96000  28.34400 -34.48600 1.000 29.13414 ? 80  GLN B NE2 1 
ATOM   1755 N N   . LEU B 1 82  ? 19.35200  26.03800 -30.53300 1.000 26.19761 ? 81  LEU B N   1 
ATOM   1756 C CA  . LEU B 1 82  ? 19.02200  26.60500 -29.23400 1.000 21.96367 ? 81  LEU B CA  1 
ATOM   1757 C C   . LEU B 1 82  ? 18.86300  25.51100 -28.19100 1.000 30.33769 ? 81  LEU B C   1 
ATOM   1758 O O   . LEU B 1 82  ? 19.27000  25.69000 -27.03400 1.000 32.58629 ? 81  LEU B O   1 
ATOM   1759 C CB  . LEU B 1 82  ? 17.77600  27.47600 -29.34800 1.000 23.73917 ? 81  LEU B CB  1 
ATOM   1760 C CG  . LEU B 1 82  ? 17.14500  27.91500 -28.03000 1.000 31.86306 ? 81  LEU B CG  1 
ATOM   1761 C CD1 . LEU B 1 82  ? 18.00300  28.96500 -27.32300 1.000 33.47113 ? 81  LEU B CD1 1 
ATOM   1762 C CD2 . LEU B 1 82  ? 15.76000  28.47200 -28.28400 1.000 28.52921 ? 81  LEU B CD2 1 
ATOM   1763 N N   . ALA B 1 83  ? 18.31900  24.35300 -28.58500 1.000 26.07180 ? 82  ALA B N   1 
ATOM   1764 C CA  . ALA B 1 83  ? 18.31100  23.21000 -27.67600 1.000 24.02711 ? 82  ALA B CA  1 
ATOM   1765 C C   . ALA B 1 83  ? 19.73000  22.73300 -27.37400 1.000 30.13343 ? 82  ALA B C   1 
ATOM   1766 O O   . ALA B 1 83  ? 20.05700  22.44400 -26.21700 1.000 36.42792 ? 82  ALA B O   1 
ATOM   1767 C CB  . ALA B 1 83  ? 17.47500  22.06700 -28.25300 1.000 23.69648 ? 82  ALA B CB  1 
ATOM   1768 N N   . GLN B 1 84  ? 20.58700  22.64000 -28.40000 1.000 31.59384 ? 83  GLN B N   1 
ATOM   1769 C CA  . GLN B 1 84  ? 21.96900  22.19000 -28.19900 1.000 28.72959 ? 83  GLN B CA  1 
ATOM   1770 C C   . GLN B 1 84  ? 22.72900  23.12500 -27.26800 1.000 29.24454 ? 83  GLN B C   1 
ATOM   1771 O O   . GLN B 1 84  ? 23.43900  22.67400 -26.35800 1.000 26.95635 ? 83  GLN B O   1 
ATOM   1772 C CB  . GLN B 1 84  ? 22.68500  22.09200 -29.54200 1.000 24.51813 ? 83  GLN B CB  1 
ATOM   1773 C CG  . GLN B 1 84  ? 24.07200  21.53700 -29.48400 1.000 22.70319 ? 83  GLN B CG  1 
ATOM   1774 C CD  . GLN B 1 84  ? 24.13900  20.19500 -28.79100 1.000 27.18856 ? 83  GLN B CD  1 
ATOM   1775 O OE1 . GLN B 1 84  ? 24.74700  20.07300 -27.73000 1.000 30.59744 ? 83  GLN B OE1 1 
ATOM   1776 N NE2 . GLN B 1 84  ? 23.52100  19.17700 -29.38600 1.000 24.98547 ? 83  GLN B NE2 1 
ATOM   1777 N N   . ARG B 1 85  ? 22.58900  24.43800 -27.49000 1.000 25.98632 ? 84  ARG B N   1 
ATOM   1778 C CA  . ARG B 1 85  ? 23.23900  25.41200 -26.62800 1.000 24.14046 ? 84  ARG B CA  1 
ATOM   1779 C C   . ARG B 1 85  ? 22.69900  25.36000 -25.20200 1.000 30.14250 ? 84  ARG B C   1 
ATOM   1780 O O   . ARG B 1 85  ? 23.39900  25.73100 -24.25400 1.000 29.72965 ? 84  ARG B O   1 
ATOM   1781 C CB  . ARG B 1 85  ? 23.07700  26.81400 -27.19800 1.000 20.48609 ? 84  ARG B CB  1 
ATOM   1782 C CG  . ARG B 1 85  ? 23.62000  27.87300 -26.25300 1.000 28.12924 ? 84  ARG B CG  1 
ATOM   1783 C CD  . ARG B 1 85  ? 23.86700  29.18200 -26.92700 1.000 31.86302 ? 84  ARG B CD  1 
ATOM   1784 N NE  . ARG B 1 85  ? 24.32600  30.18500 -25.97900 1.000 28.79892 ? 84  ARG B NE  1 
ATOM   1785 C CZ  . ARG B 1 85  ? 24.59700  31.44100 -26.30500 1.000 30.27677 ? 84  ARG B CZ  1 
ATOM   1786 N NH1 . ARG B 1 85  ? 24.48000  31.86900 -27.55600 1.000 31.25792 ? 84  ARG B NH1 1 
ATOM   1787 N NH2 . ARG B 1 85  ? 24.95200  32.29800 -25.34800 1.000 30.43089 ? 84  ARG B NH2 1 
ATOM   1788 N N   . ILE B 1 86  ? 21.46600  24.91500 -25.01800 1.000 28.13903 ? 85  ILE B N   1 
ATOM   1789 C CA  . ILE B 1 86  ? 20.97100  24.82500 -23.65300 1.000 33.08865 ? 85  ILE B CA  1 
ATOM   1790 C C   . ILE B 1 86  ? 21.56000  23.60000 -22.96400 1.000 34.07593 ? 85  ILE B C   1 
ATOM   1791 O O   . ILE B 1 86  ? 21.96500  23.66100 -21.79500 1.000 35.39197 ? 85  ILE B O   1 
ATOM   1792 C CB  . ILE B 1 86  ? 19.42900  24.82700 -23.63300 1.000 28.67480 ? 85  ILE B CB  1 
ATOM   1793 C CG1 . ILE B 1 86  ? 18.90700  26.27000 -23.77800 1.000 23.58257 ? 85  ILE B CG1 1 
ATOM   1794 C CG2 . ILE B 1 86  ? 18.91600  24.13900 -22.35900 1.000 20.50525 ? 85  ILE B CG2 1 
ATOM   1795 C CD1 . ILE B 1 86  ? 17.50700  26.38900 -24.34700 1.000 21.92190 ? 85  ILE B CD1 1 
ATOM   1796 N N   . VAL B 1 87  ? 21.65600  22.48400 -23.68400 1.000 29.12532 ? 86  VAL B N   1 
ATOM   1797 C CA  . VAL B 1 87  ? 22.30900  21.30300 -23.13200 1.000 32.29362 ? 86  VAL B CA  1 
ATOM   1798 C C   . VAL B 1 87  ? 23.73800  21.62500 -22.70400 1.000 32.27528 ? 86  VAL B C   1 
ATOM   1799 O O   . VAL B 1 87  ? 24.20300  21.16300 -21.65500 1.000 32.60328 ? 86  VAL B O   1 
ATOM   1800 C CB  . VAL B 1 87  ? 22.27600  20.15200 -24.15100 1.000 30.28981 ? 86  VAL B CB  1 
ATOM   1801 C CG1 . VAL B 1 87  ? 23.11600  18.99200 -23.65500 1.000 32.80391 ? 86  VAL B CG1 1 
ATOM   1802 C CG2 . VAL B 1 87  ? 20.84800  19.72200 -24.40200 1.000 27.99560 ? 86  VAL B CG2 1 
ATOM   1803 N N   . ASP B 1 88  ? 24.45100  22.42900 -23.49800 1.000 29.75352 ? 87  ASP B N   1 
ATOM   1804 C CA  . ASP B 1 88  ? 25.86800  22.68100 -23.23800 1.000 31.93220 ? 87  ASP B CA  1 
ATOM   1805 C C   . ASP B 1 88  ? 26.08200  23.71300 -22.14100 1.000 33.05860 ? 87  ASP B C   1 
ATOM   1806 O O   . ASP B 1 88  ? 26.92000  23.51900 -21.25000 1.000 33.49963 ? 87  ASP B O   1 
ATOM   1807 C CB  . ASP B 1 88  ? 26.56500  23.14800 -24.51000 1.000 31.05436 ? 87  ASP B CB  1 
ATOM   1808 C CG  . ASP B 1 88  ? 26.70700  22.04900 -25.51400 1.000 36.63239 ? 87  ASP B CG  1 
ATOM   1809 O OD1 . ASP B 1 88  ? 26.67300  20.86200 -25.09500 1.000 33.11548 ? 87  ASP B OD1 1 
ATOM   1810 O OD2 . ASP B 1 88  ? 26.84700  22.37600 -26.71500 1.000 28.86699 ? 87  ASP B OD2 1 
ATOM   1811 N N   . ASP B 1 89  ? 25.37000  24.83900 -22.21600 1.000 31.03962 ? 88  ASP B N   1 
ATOM   1812 C CA  . ASP B 1 89  ? 25.60400  25.92100 -21.27700 1.000 27.91895 ? 88  ASP B CA  1 
ATOM   1813 C C   . ASP B 1 89  ? 24.97500  25.65400 -19.91900 1.000 33.31263 ? 88  ASP B C   1 
ATOM   1814 O O   . ASP B 1 89  ? 25.44600  26.21400 -18.91800 1.000 32.08863 ? 88  ASP B O   1 
ATOM   1815 C CB  . ASP B 1 89  ? 25.10300  27.23400 -21.86100 1.000 24.59850 ? 88  ASP B CB  1 
ATOM   1816 C CG  . ASP B 1 89  ? 26.02700  27.77000 -22.94200 1.000 28.54614 ? 88  ASP B CG  1 
ATOM   1817 O OD1 . ASP B 1 89  ? 27.04000  27.11600 -23.24100 1.000 32.39639 ? 88  ASP B OD1 1 
ATOM   1818 O OD2 . ASP B 1 89  ? 25.75300  28.85300 -23.48900 1.000 35.32990 ? 88  ASP B OD2 1 
ATOM   1819 N N   . VAL B 1 90  ? 23.94100  24.80400 -19.85400 1.000 33.52171 ? 89  VAL B N   1 
ATOM   1820 C CA  . VAL B 1 90  ? 23.44100  24.35400 -18.55600 1.000 32.56287 ? 89  VAL B CA  1 
ATOM   1821 C C   . VAL B 1 90  ? 24.42900  23.38900 -17.92500 1.000 31.71684 ? 89  VAL B C   1 
ATOM   1822 O O   . VAL B 1 90  ? 24.80600  23.53900 -16.75700 1.000 31.01512 ? 89  VAL B O   1 
ATOM   1823 C CB  . VAL B 1 90  ? 22.04600  23.71900 -18.68300 1.000 24.92657 ? 89  VAL B CB  1 
ATOM   1824 C CG1 . VAL B 1 90  ? 21.66900  23.01400 -17.37000 1.000 27.04176 ? 89  VAL B CG1 1 
ATOM   1825 C CG2 . VAL B 1 90  ? 21.02700  24.79000 -18.99100 1.000 27.77648 ? 89  VAL B CG2 1 
ATOM   1826 N N   . SER B 1 91  ? 24.84600  22.37600 -18.68800 1.000 33.21004 ? 90  SER B N   1 
ATOM   1827 C CA  . SER B 1 91  ? 25.90700  21.47200 -18.26400 1.000 28.95592 ? 90  SER B CA  1 
ATOM   1828 C C   . SER B 1 91  ? 27.00700  22.22300 -17.52600 1.000 31.94498 ? 90  SER B C   1 
ATOM   1829 O O   . SER B 1 91  ? 27.41000  21.81600 -16.43100 1.000 37.53351 ? 90  SER B O   1 
ATOM   1830 C CB  . SER B 1 91  ? 26.46300  20.73700 -19.48200 1.000 27.66428 ? 90  SER B CB  1 
ATOM   1831 O OG  . SER B 1 91  ? 27.42400  19.77300 -19.11700 1.000 33.95474 ? 90  SER B OG  1 
ATOM   1832 N N   . VAL B 1 92  ? 27.45800  23.36300 -18.07300 1.000 31.90926 ? 91  VAL B N   1 
ATOM   1833 C CA  . VAL B 1 92  ? 28.56600  24.09000 -17.45000 1.000 28.20070 ? 91  VAL B CA  1 
ATOM   1834 C C   . VAL B 1 92  ? 28.07900  24.92300 -16.27300 1.000 33.18775 ? 91  VAL B C   1 
ATOM   1835 O O   . VAL B 1 92  ? 28.70600  24.93000 -15.20600 1.000 36.34532 ? 91  VAL B O   1 
ATOM   1836 C CB  . VAL B 1 92  ? 29.32400  24.95500 -18.48200 1.000 29.28996 ? 91  VAL B CB  1 
ATOM   1837 C CG1 . VAL B 1 92  ? 29.74600  24.12600 -19.68800 1.000 23.19216 ? 91  VAL B CG1 1 
ATOM   1838 C CG2 . VAL B 1 92  ? 28.49700  26.16000 -18.93200 1.000 36.92140 ? 91  VAL B CG2 1 
ATOM   1839 N N   . ALA B 1 93  ? 26.95700  25.63000 -16.43500 1.000 30.67361 ? 92  ALA B N   1 
ATOM   1840 C CA  . ALA B 1 93  ? 26.46700  26.49800 -15.37100 1.000 28.84435 ? 92  ALA B CA  1 
ATOM   1841 C C   . ALA B 1 93  ? 26.11900  25.70900 -14.11900 1.000 28.55922 ? 92  ALA B C   1 
ATOM   1842 O O   . ALA B 1 93  ? 26.32300  26.19700 -13.00100 1.000 34.38397 ? 92  ALA B O   1 
ATOM   1843 C CB  . ALA B 1 93  ? 25.24900  27.28100 -15.85800 1.000 27.56012 ? 92  ALA B CB  1 
ATOM   1844 N N   . ALA B 1 94  ? 25.62700  24.48300 -14.28900 1.000 29.38480 ? 93  ALA B N   1 
ATOM   1845 C CA  . ALA B 1 94  ? 25.16400  23.64200 -13.19800 1.000 30.45595 ? 93  ALA B CA  1 
ATOM   1846 C C   . ALA B 1 94  ? 26.19100  22.60300 -12.74600 1.000 33.99485 ? 93  ALA B C   1 
ATOM   1847 O O   . ALA B 1 94  ? 25.97600  21.95500 -11.71200 1.000 33.58890 ? 93  ALA B O   1 
ATOM   1848 C CB  . ALA B 1 94  ? 23.86000  22.93700 -13.61200 1.000 29.90161 ? 93  ALA B CB  1 
ATOM   1849 N N   . GLU B 1 95  ? 27.29200  22.43600 -13.48000 1.000 33.67861 ? 94  GLU B N   1 
ATOM   1850 C CA  . GLU B 1 95  ? 28.28500  21.39500 -13.22000 1.000 31.19559 ? 94  GLU B CA  1 
ATOM   1851 C C   . GLU B 1 95  ? 27.58800  20.04800 -13.10500 1.000 28.34506 ? 94  GLU B C   1 
ATOM   1852 O O   . GLU B 1 95  ? 27.56500  19.39200 -12.06200 1.000 41.37285 ? 94  GLU B O   1 
ATOM   1853 C CB  . GLU B 1 95  ? 29.13000  21.70000 -11.97800 1.000 31.58420 ? 94  GLU B CB  1 
ATOM   1854 C CG  . GLU B 1 95  ? 30.03700  22.91500 -12.13100 1.000 39.14348 ? 94  GLU B CG  1 
ATOM   1855 C CD  . GLU B 1 95  ? 30.34600  23.61400 -10.81000 1.000 41.65559 ? 94  GLU B CD  1 
ATOM   1856 O OE1 . GLU B 1 95  ? 29.44600  24.27500 -10.25600 1.000 51.72996 ? 94  GLU B OE1 1 
ATOM   1857 O OE2 . GLU B 1 95  ? 31.49600  23.52100 -10.33300 1.000 39.64598 ? 94  GLU B OE2 1 
ATOM   1858 N N   . ILE B 1 96  ? 26.98000  19.66900 -14.21200 1.000 29.21797 ? 95  ILE B N   1 
ATOM   1859 C CA  . ILE B 1 96  ? 26.28000  18.40100 -14.34900 1.000 34.79790 ? 95  ILE B CA  1 
ATOM   1860 C C   . ILE B 1 96  ? 26.66400  17.86900 -15.71700 1.000 36.86759 ? 95  ILE B C   1 
ATOM   1861 O O   . ILE B 1 96  ? 26.87800  18.65100 -16.64800 1.000 36.45794 ? 95  ILE B O   1 
ATOM   1862 C CB  . ILE B 1 96  ? 24.74500  18.57500 -14.20100 1.000 34.67159 ? 95  ILE B CB  1 
ATOM   1863 C CG1 . ILE B 1 96  ? 24.23200  18.01500 -12.87800 1.000 36.29245 ? 95  ILE B CG1 1 
ATOM   1864 C CG2 . ILE B 1 96  ? 23.99900  17.95000 -15.35200 1.000 36.46516 ? 95  ILE B CG2 1 
ATOM   1865 C CD1 . ILE B 1 96  ? 22.86500  18.56800 -12.46400 1.000 33.67331 ? 95  ILE B CD1 1 
ATOM   1866 N N   . ASP B 1 97  ? 26.81700  16.55200 -15.82300 1.000 37.20875 ? 96  ASP B N   1 
ATOM   1867 C CA  . ASP B 1 97  ? 27.10200  15.94400 -17.11000 1.000 38.46452 ? 96  ASP B CA  1 
ATOM   1868 C C   . ASP B 1 97  ? 25.95100  16.19000 -18.08500 1.000 39.99830 ? 96  ASP B C   1 
ATOM   1869 O O   . ASP B 1 97  ? 24.78000  16.21900 -17.70000 1.000 34.51503 ? 96  ASP B O   1 
ATOM   1870 C CB  . ASP B 1 97  ? 27.32600  14.44500 -16.93900 1.000 46.37822 ? 96  ASP B CB  1 
ATOM   1871 C CG  . ASP B 1 97  ? 28.37300  13.90100 -17.88200 1.000 58.03699 ? 96  ASP B CG  1 
ATOM   1872 O OD1 . ASP B 1 97  ? 29.57600  14.20200 -17.67000 1.000 60.42632 ? 96  ASP B OD1 1 
ATOM   1873 O OD2 . ASP B 1 97  ? 27.97900  13.20900 -18.85600 1.000 50.59212 ? 96  ASP B OD2 1 
ATOM   1874 N N   . ARG B 1 98  ? 26.29400  16.36100 -19.36900 1.000 40.44185 ? 97  ARG B N   1 
ATOM   1875 C CA  . ARG B 1 98  ? 25.26800  16.47700 -20.40500 1.000 33.42179 ? 97  ARG B CA  1 
ATOM   1876 C C   . ARG B 1 98  ? 24.32200  15.28300 -20.39800 1.000 39.80124 ? 97  ARG B C   1 
ATOM   1877 O O   . ARG B 1 98  ? 23.11600  15.43700 -20.64400 1.000 37.69975 ? 97  ARG B O   1 
ATOM   1878 C CB  . ARG B 1 98  ? 25.92500  16.61100 -21.77900 1.000 33.92089 ? 97  ARG B CB  1 
ATOM   1879 C CG  . ARG B 1 98  ? 26.50600  17.98200 -22.03500 1.000 41.18382 ? 97  ARG B CG  1 
ATOM   1880 C CD  . ARG B 1 98  ? 27.88200  17.95200 -22.72300 1.000 41.17583 ? 97  ARG B CD  1 
ATOM   1881 N NE  . ARG B 1 98  ? 28.56600  19.21600 -22.45800 1.000 47.81977 ? 97  ARG B NE  1 
ATOM   1882 C CZ  . ARG B 1 98  ? 29.25900  19.91700 -23.34700 1.000 53.09195 ? 97  ARG B CZ  1 
ATOM   1883 N NH1 . ARG B 1 98  ? 29.43000  19.48500 -24.59100 1.000 56.06271 ? 97  ARG B NH1 1 
ATOM   1884 N NH2 . ARG B 1 98  ? 29.78400  21.08900 -22.98100 1.000 35.55345 ? 97  ARG B NH2 1 
ATOM   1885 N N   . LYS B 1 99  ? 24.85000  14.08900 -20.10800 1.000 43.35772 ? 98  LYS B N   1 
ATOM   1886 C CA  . LYS B 1 99  ? 24.08400  12.85100 -20.04200 1.000 37.41824 ? 98  LYS B CA  1 
ATOM   1887 C C   . LYS B 1 99  ? 22.87900  12.98600 -19.12100 1.000 40.74514 ? 98  LYS B C   1 
ATOM   1888 O O   . LYS B 1 99  ? 21.95900  12.16200 -19.17800 1.000 41.12172 ? 98  LYS B O   1 
ATOM   1889 C CB  . LYS B 1 99  ? 24.97100  11.70100 -19.55700 1.000 40.29169 ? 98  LYS B CB  1 
ATOM   1890 C CG  . LYS B 1 99  ? 25.63800  10.89500 -20.66900 1.000 50.53109 ? 98  LYS B CG  1 
ATOM   1891 C CD  . LYS B 1 99  ? 27.12500  10.65300 -20.35400 1.000 58.75335 ? 98  LYS B CD  1 
ATOM   1892 C CE  . LYS B 1 99  ? 27.93300  10.27900 -21.59800 1.000 59.94826 ? 98  LYS B CE  1 
ATOM   1893 N NZ  . LYS B 1 99  ? 27.95600  11.37600 -22.62700 1.000 58.32390 ? 98  LYS B NZ  1 
ATOM   1894 N N   . HIS B 1 100 ? 22.87800  14.01400 -18.26800 1.000 36.66309 ? 99  HIS B N   1 
ATOM   1895 C CA  . HIS B 1 100 ? 21.81400  14.22600 -17.29500 1.000 41.06072 ? 99  HIS B CA  1 
ATOM   1896 C C   . HIS B 1 100 ? 20.70100  15.17100 -17.76900 1.000 40.47852 ? 99  HIS B C   1 
ATOM   1897 O O   . HIS B 1 100 ? 19.68000  15.28500 -17.07400 1.000 37.54870 ? 99  HIS B O   1 
ATOM   1898 C CB  . HIS B 1 100 ? 22.41500  14.76400 -15.98900 1.000 35.82294 ? 99  HIS B CB  1 
ATOM   1899 C CG  . HIS B 1 100 ? 23.19900  13.74600 -15.22200 1.000 39.90682 ? 99  HIS B CG  1 
ATOM   1900 N ND1 . HIS B 1 100 ? 22.60100  12.72300 -14.51400 1.000 37.56607 ? 99  HIS B ND1 1 
ATOM   1901 C CD2 . HIS B 1 100 ? 24.53200  13.59300 -15.05100 1.000 35.86478 ? 99  HIS B CD2 1 
ATOM   1902 C CE1 . HIS B 1 100 ? 23.53200  11.98500 -13.94100 1.000 31.56839 ? 99  HIS B CE1 1 
ATOM   1903 N NE2 . HIS B 1 100 ? 24.71200  12.48700 -14.25700 1.000 34.59103 ? 99  HIS B NE2 1 
ATOM   1904 N N   . ILE B 1 101 ? 20.84800  15.82400 -18.92600 1.000 30.92642 ? 100 ILE B N   1 
ATOM   1905 C CA  . ILE B 1 101 ? 19.99500  16.94600 -19.32300 1.000 31.06857 ? 100 ILE B CA  1 
ATOM   1906 C C   . ILE B 1 101 ? 19.07400  16.52800 -20.47600 1.000 33.71060 ? 100 ILE B C   1 
ATOM   1907 O O   . ILE B 1 101 ? 19.54400  16.14200 -21.55400 1.000 29.52359 ? 100 ILE B O   1 
ATOM   1908 C CB  . ILE B 1 101 ? 20.85200  18.17400 -19.69100 1.000 32.86596 ? 100 ILE B CB  1 
ATOM   1909 C CG1 . ILE B 1 101 ? 21.84800  18.46500 -18.56300 1.000 33.88135 ? 100 ILE B CG1 1 
ATOM   1910 C CG2 . ILE B 1 101 ? 20.00200  19.40100 -19.92300 1.000 23.43002 ? 100 ILE B CG2 1 
ATOM   1911 C CD1 . ILE B 1 101 ? 22.86100  19.54700 -18.89000 1.000 32.40848 ? 100 ILE B CD1 1 
ATOM   1912 N N   . TRP B 1 102 ? 17.76000  16.60500 -20.25100 1.000 29.88701 ? 101 TRP B N   1 
ATOM   1913 C CA  . TRP B 1 102 ? 16.76600  16.47500 -21.30600 1.000 24.43414 ? 101 TRP B CA  1 
ATOM   1914 C C   . TRP B 1 102 ? 16.16800  17.84900 -21.59900 1.000 23.36215 ? 101 TRP B C   1 
ATOM   1915 O O   . TRP B 1 102 ? 15.93700  18.63200 -20.67700 1.000 21.70842 ? 101 TRP B O   1 
ATOM   1916 C CB  . TRP B 1 102 ? 15.64400  15.51300 -20.91200 1.000 30.02769 ? 101 TRP B CB  1 
ATOM   1917 C CG  . TRP B 1 102 ? 16.06700  14.14300 -20.40700 1.000 32.36274 ? 101 TRP B CG  1 
ATOM   1918 C CD1 . TRP B 1 102 ? 17.21900  13.81400 -19.75000 1.000 30.34203 ? 101 TRP B CD1 1 
ATOM   1919 C CD2 . TRP B 1 102 ? 15.30300  12.93000 -20.49600 1.000 32.04319 ? 101 TRP B CD2 1 
ATOM   1920 N NE1 . TRP B 1 102 ? 17.22600  12.47500 -19.44100 1.000 26.31390 ? 101 TRP B NE1 1 
ATOM   1921 C CE2 . TRP B 1 102 ? 16.06000  11.91200 -19.88900 1.000 26.21580 ? 101 TRP B CE2 1 
ATOM   1922 C CE3 . TRP B 1 102 ? 14.05600  12.60500 -21.04600 1.000 26.79028 ? 101 TRP B CE3 1 
ATOM   1923 C CZ2 . TRP B 1 102 ? 15.61400  10.60200 -19.82000 1.000 29.39378 ? 101 TRP B CZ2 1 
ATOM   1924 C CZ3 . TRP B 1 102 ? 13.61400  11.30300 -20.96800 1.000 25.74497 ? 101 TRP B CZ3 1 
ATOM   1925 C CH2 . TRP B 1 102 ? 14.38800  10.31700 -20.36400 1.000 30.08837 ? 101 TRP B CH2 1 
ATOM   1926 N N   . VAL B 1 103 ? 15.89500  18.13600 -22.87600 1.000 19.73822 ? 102 VAL B N   1 
ATOM   1927 C CA  . VAL B 1 103 ? 15.43300  19.45900 -23.30200 1.000 21.87297 ? 102 VAL B CA  1 
ATOM   1928 C C   . VAL B 1 103 ? 14.35800  19.29200 -24.36900 1.000 29.02203 ? 102 VAL B C   1 
ATOM   1929 O O   . VAL B 1 103 ? 14.67200  18.91500 -25.50700 1.000 31.58522 ? 102 VAL B O   1 
ATOM   1930 C CB  . VAL B 1 103 ? 16.57800  20.33700 -23.83400 1.000 23.23978 ? 102 VAL B CB  1 
ATOM   1931 C CG1 . VAL B 1 103 ? 16.05400  21.58200 -24.47400 1.000 22.15462 ? 102 VAL B CG1 1 
ATOM   1932 C CG2 . VAL B 1 103 ? 17.49700  20.72200 -22.72500 1.000 26.04993 ? 102 VAL B CG2 1 
ATOM   1933 N N   . TYR B 1 104 ? 13.09500  19.59400 -24.01500 1.000 23.25865 ? 103 TYR B N   1 
ATOM   1934 C CA  . TYR B 1 104 ? 11.97000  19.58500 -24.94700 1.000 23.98224 ? 103 TYR B CA  1 
ATOM   1935 C C   . TYR B 1 104 ? 11.50100  21.00600 -25.20000 1.000 27.48969 ? 103 TYR B C   1 
ATOM   1936 O O   . TYR B 1 104 ? 11.40400  21.80600 -24.25700 1.000 27.25410 ? 103 TYR B O   1 
ATOM   1937 C CB  . TYR B 1 104 ? 10.74200  18.82100 -24.42800 1.000 27.87235 ? 103 TYR B CB  1 
ATOM   1938 C CG  . TYR B 1 104 ? 10.79600  17.32100 -24.20900 1.000 28.86767 ? 103 TYR B CG  1 
ATOM   1939 C CD1 . TYR B 1 104 ? 11.98000  16.60400 -24.28300 1.000 26.30775 ? 103 TYR B CD1 1 
ATOM   1940 C CD2 . TYR B 1 104 ? 9.61800   16.61900 -23.90500 1.000 28.97250 ? 103 TYR B CD2 1 
ATOM   1941 C CE1 . TYR B 1 104 ? 11.98600  15.21400 -24.05600 1.000 28.75148 ? 103 TYR B CE1 1 
ATOM   1942 C CE2 . TYR B 1 104 ? 9.61900   15.25200 -23.67300 1.000 24.56038 ? 103 TYR B CE2 1 
ATOM   1943 C CZ  . TYR B 1 104 ? 10.80100  14.55400 -23.75000 1.000 26.22079 ? 103 TYR B CZ  1 
ATOM   1944 O OH  . TYR B 1 104 ? 10.78900  13.19900 -23.52600 1.000 25.66453 ? 103 TYR B OH  1 
ATOM   1945 N N   . PHE B 1 105 ? 11.13400  21.28100 -26.46000 1.000 25.67381 ? 104 PHE B N   1 
ATOM   1946 C CA  . PHE B 1 105 ? 10.58000  22.56200 -26.90800 1.000 25.09014 ? 104 PHE B CA  1 
ATOM   1947 C C   . PHE B 1 105 ? 9.17200   22.34700 -27.46300 1.000 35.65276 ? 104 PHE B C   1 
ATOM   1948 O O   . PHE B 1 105 ? 9.00200   21.68600 -28.49500 1.000 40.23754 ? 104 PHE B O   1 
ATOM   1949 C CB  . PHE B 1 105 ? 11.43600  23.19100 -28.01500 1.000 29.49158 ? 104 PHE B CB  1 
ATOM   1950 C CG  . PHE B 1 105 ? 12.77000  23.70900 -27.56400 1.000 31.29332 ? 104 PHE B CG  1 
ATOM   1951 C CD1 . PHE B 1 105 ? 13.07400  23.84200 -26.22500 1.000 25.41224 ? 104 PHE B CD1 1 
ATOM   1952 C CD2 . PHE B 1 105 ? 13.72300  24.07000 -28.50300 1.000 27.77573 ? 104 PHE B CD2 1 
ATOM   1953 C CE1 . PHE B 1 105 ? 14.30300  24.30800 -25.83600 1.000 27.32627 ? 104 PHE B CE1 1 
ATOM   1954 C CE2 . PHE B 1 105 ? 14.96100  24.54900 -28.11100 1.000 26.27494 ? 104 PHE B CE2 1 
ATOM   1955 C CZ  . PHE B 1 105 ? 15.24800  24.66700 -26.78100 1.000 23.27467 ? 104 PHE B CZ  1 
ATOM   1956 N N   . GLY B 1 106 ? 8.17300   22.94000 -26.82500 1.000 27.94718 ? 105 GLY B N   1 
ATOM   1957 C CA  . GLY B 1 106 ? 6.82500   22.96900 -27.36100 1.000 25.44036 ? 105 GLY B CA  1 
ATOM   1958 C C   . GLY B 1 106 ? 6.47900   24.37000 -27.82800 1.000 26.58115 ? 105 GLY B C   1 
ATOM   1959 O O   . GLY B 1 106 ? 6.96500   25.36000 -27.27500 1.000 24.73880 ? 105 GLY B O   1 
ATOM   1960 N N   . GLU B 1 107 ? 5.64800   24.45500 -28.86500 1.000 28.75924 ? 106 GLU B N   1 
ATOM   1961 C CA  . GLU B 1 107 ? 5.35600   25.72700 -29.50500 1.000 21.75839 ? 106 GLU B CA  1 
ATOM   1962 C C   . GLU B 1 107 ? 3.86000   25.98200 -29.53200 1.000 23.26551 ? 106 GLU B C   1 
ATOM   1963 O O   . GLU B 1 107 ? 3.06700   25.05500 -29.72000 1.000 27.25498 ? 106 GLU B O   1 
ATOM   1964 C CB  . GLU B 1 107 ? 5.89600   25.75200 -30.92100 1.000 21.02213 ? 106 GLU B CB  1 
ATOM   1965 C CG  . GLU B 1 107 ? 7.33700   25.36200 -31.02500 1.000 22.67581 ? 106 GLU B CG  1 
ATOM   1966 C CD  . GLU B 1 107 ? 7.68500   24.92900 -32.42600 1.000 25.26676 ? 106 GLU B CD  1 
ATOM   1967 O OE1 . GLU B 1 107 ? 7.49700   23.73900 -32.73200 1.000 27.41990 ? 106 GLU B OE1 1 
ATOM   1968 O OE2 . GLU B 1 107 ? 8.13200   25.78200 -33.21900 1.000 19.66600 ? 106 GLU B OE2 1 
ATOM   1969 N N   . MET B 1 108 ? 3.48200   27.24400 -29.36100 1.000 23.58866 ? 107 MET B N   1 
ATOM   1970 C CA  . MET B 1 108 ? 2.10000   27.68500 -29.47100 1.000 20.67389 ? 107 MET B CA  1 
ATOM   1971 C C   . MET B 1 108 ? 2.04100   28.96900 -30.28100 1.000 21.21256 ? 107 MET B C   1 
ATOM   1972 O O   . MET B 1 108 ? 3.01500   29.73300 -30.31400 1.000 19.27572 ? 107 MET B O   1 
ATOM   1973 C CB  . MET B 1 108 ? 1.47400   27.89100 -28.08100 1.000 17.08597 ? 107 MET B CB  1 
ATOM   1974 C CG  . MET B 1 108 ? 1.73400   26.72100 -27.13700 1.000 22.57563 ? 107 MET B CG  1 
ATOM   1975 S SD  . MET B 1 108 ? 1.93000   27.15800 -25.38400 1.000 29.38973 ? 107 MET B SD  1 
ATOM   1976 C CE  . MET B 1 108 ? 3.47500   28.01700 -25.46800 1.000 24.18144 ? 107 MET B CE  1 
ATOM   1977 N N   . PRO B 1 109 ? 0.93400   29.20900 -30.98300 1.000 20.18395 ? 108 PRO B N   1 
ATOM   1978 C CA  . PRO B 1 109 ? 0.73800   30.51200 -31.62600 1.000 19.96812 ? 108 PRO B CA  1 
ATOM   1979 C C   . PRO B 1 109 ? 0.95900   31.62400 -30.62200 1.000 23.97663 ? 108 PRO B C   1 
ATOM   1980 O O   . PRO B 1 109 ? 0.43500   31.58700 -29.50600 1.000 25.15958 ? 108 PRO B O   1 
ATOM   1981 C CB  . PRO B 1 109 ? -0.71800  30.46800 -32.09800 1.000 20.12296 ? 108 PRO B CB  1 
ATOM   1982 C CG  . PRO B 1 109 ? -1.06300  29.04500 -32.17100 1.000 22.30690 ? 108 PRO B CG  1 
ATOM   1983 C CD  . PRO B 1 109 ? -0.19900  28.29800 -31.20000 1.000 18.51927 ? 108 PRO B CD  1 
ATOM   1984 N N   . ALA B 1 110 ? 1.75500   32.61300 -31.02000 1.000 24.18989 ? 109 ALA B N   1 
ATOM   1985 C CA  . ALA B 1 110 ? 1.97400   33.77900 -30.17400 1.000 23.27812 ? 109 ALA B CA  1 
ATOM   1986 C C   . ALA B 1 110 ? 0.66800   34.41300 -29.68600 1.000 22.19577 ? 109 ALA B C   1 
ATOM   1987 O O   . ALA B 1 110 ? 0.61900   34.93500 -28.56800 1.000 27.89768 ? 109 ALA B O   1 
ATOM   1988 C CB  . ALA B 1 110 ? 2.81400   34.80800 -30.93400 1.000 25.70065 ? 109 ALA B CB  1 
ATOM   1989 N N   . GLN B 1 111 ? -0.39900  34.38000 -30.48200 1.000 21.89076 ? 110 GLN B N   1 
ATOM   1990 C CA  . GLN B 1 111 ? -1.62000  35.08800 -30.08800 1.000 24.28841 ? 110 GLN B CA  1 
ATOM   1991 C C   . GLN B 1 111 ? -2.44900  34.37500 -29.01300 1.000 23.36392 ? 110 GLN B C   1 
ATOM   1992 O O   . GLN B 1 111 ? -3.49600  34.90100 -28.62900 1.000 23.42254 ? 110 GLN B O   1 
ATOM   1993 C CB  . GLN B 1 111 ? -2.50500  35.35000 -31.30600 1.000 20.26679 ? 110 GLN B CB  1 
ATOM   1994 C CG  . GLN B 1 111 ? -2.76200  34.11900 -32.11600 1.000 31.36307 ? 110 GLN B CG  1 
ATOM   1995 C CD  . GLN B 1 111 ? -2.65500  34.35600 -33.61500 1.000 38.97581 ? 110 GLN B CD  1 
ATOM   1996 O OE1 . GLN B 1 111 ? -3.58500  34.88100 -34.25000 1.000 41.57970 ? 110 GLN B OE1 1 
ATOM   1997 N NE2 . GLN B 1 111 ? -1.50800  33.98100 -34.19100 1.000 29.14719 ? 110 GLN B NE2 1 
ATOM   1998 N N   . GLN B 1 112 ? -2.05400  33.18700 -28.54100 1.000 22.45810 ? 111 GLN B N   1 
ATOM   1999 C CA  . GLN B 1 112 ? -2.63700  32.59600 -27.34100 1.000 22.54915 ? 111 GLN B CA  1 
ATOM   2000 C C   . GLN B 1 112 ? -1.60100  32.53000 -26.22500 1.000 25.62207 ? 111 GLN B C   1 
ATOM   2001 O O   . GLN B 1 112 ? -1.67600  31.67500 -25.33700 1.000 25.56078 ? 111 GLN B O   1 
ATOM   2002 C CB  . GLN B 1 112 ? -3.23800  31.21200 -27.59500 1.000 18.82637 ? 111 GLN B CB  1 
ATOM   2003 C CG  . GLN B 1 112 ? -2.29600  30.17500 -28.13500 1.000 22.75324 ? 111 GLN B CG  1 
ATOM   2004 C CD  . GLN B 1 112 ? -3.03100  29.10600 -28.91700 1.000 23.47715 ? 111 GLN B CD  1 
ATOM   2005 O OE1 . GLN B 1 112 ? -3.80300  29.41700 -29.83800 1.000 18.02690 ? 111 GLN B OE1 1 
ATOM   2006 N NE2 . GLN B 1 112 ? -2.81300  27.83600 -28.54700 1.000 19.68244 ? 111 GLN B NE2 1 
ATOM   2007 N N   . MET B 1 113 ? -0.64500  33.45400 -26.26600 1.000 20.38089 ? 112 MET B N   1 
ATOM   2008 C CA  . MET B 1 113 ? 0.42300   33.57700 -25.28700 1.000 25.17313 ? 112 MET B CA  1 
ATOM   2009 C C   . MET B 1 113 ? 0.50000   35.00400 -24.77500 1.000 24.47948 ? 112 MET B C   1 
ATOM   2010 O O   . MET B 1 113 ? 0.50600   35.95400 -25.56200 1.000 25.70987 ? 112 MET B O   1 
ATOM   2011 C CB  . MET B 1 113 ? 1.74900   33.12800 -25.89000 1.000 20.49751 ? 112 MET B CB  1 
ATOM   2012 C CG  . MET B 1 113 ? 1.72100   31.71700 -26.39700 1.000 22.04474 ? 112 MET B CG  1 
ATOM   2013 S SD  . MET B 1 113 ? 3.08300   31.50100 -27.52900 1.000 24.09571 ? 112 MET B SD  1 
ATOM   2014 C CE  . MET B 1 113 ? 4.52000   31.42000 -26.44700 1.000 23.16230 ? 112 MET B CE  1 
ATOM   2015 N N   . VAL B 1 114 ? 0.56000   35.14600 -23.45700 1.000 19.10561 ? 113 VAL B N   1 
ATOM   2016 C CA  . VAL B 1 114 ? 0.46100   36.44000 -22.80200 1.000 27.70862 ? 113 VAL B CA  1 
ATOM   2017 C C   . VAL B 1 114 ? 1.55000   36.55900 -21.74500 1.000 27.52835 ? 113 VAL B C   1 
ATOM   2018 O O   . VAL B 1 114 ? 1.64200   35.71600 -20.84600 1.000 30.72740 ? 113 VAL B O   1 
ATOM   2019 C CB  . VAL B 1 114 ? -0.91700  36.63800 -22.16300 1.000 33.88253 ? 113 VAL B CB  1 
ATOM   2020 C CG1 . VAL B 1 114 ? -0.80500  37.56900 -20.95700 1.000 28.99933 ? 113 VAL B CG1 1 
ATOM   2021 C CG2 . VAL B 1 114 ? -1.90400  37.15400 -23.22000 1.000 34.36856 ? 113 VAL B CG2 1 
ATOM   2022 N N   . GLU B 1 115 ? 2.35800   37.61100 -21.84300 1.000 28.99837 ? 114 GLU B N   1 
ATOM   2023 C CA  . GLU B 1 115 ? 3.40700   37.92700 -20.88300 1.000 26.99884 ? 114 GLU B CA  1 
ATOM   2024 C C   . GLU B 1 115 ? 3.22800   39.35200 -20.38000 1.000 28.36071 ? 114 GLU B C   1 
ATOM   2025 O O   . GLU B 1 115 ? 2.79900   40.23900 -21.12800 1.000 23.55728 ? 114 GLU B O   1 
ATOM   2026 C CB  . GLU B 1 115 ? 4.79000   37.76800 -21.49600 1.000 23.68789 ? 114 GLU B CB  1 
ATOM   2027 C CG  . GLU B 1 115 ? 4.97500   36.42600 -22.10900 1.000 24.84911 ? 114 GLU B CG  1 
ATOM   2028 C CD  . GLU B 1 115 ? 6.40600   36.15900 -22.44000 1.000 29.45932 ? 114 GLU B CD  1 
ATOM   2029 O OE1 . GLU B 1 115 ? 7.22800   37.08800 -22.27100 1.000 28.22264 ? 114 GLU B OE1 1 
ATOM   2030 O OE2 . GLU B 1 115 ? 6.70100   35.02000 -22.86900 1.000 29.87962 ? 114 GLU B OE2 1 
ATOM   2031 N N   . TYR B 1 116 ? 3.55000   39.55800 -19.09900 1.000 31.60087 ? 115 TYR B N   1 
ATOM   2032 C CA  . TYR B 1 116 ? 3.29500   40.84100 -18.45600 1.000 29.93452 ? 115 TYR B CA  1 
ATOM   2033 C C   . TYR B 1 116 ? 1.90700   41.37200 -18.80000 1.000 33.44024 ? 115 TYR B C   1 
ATOM   2034 O O   . TYR B 1 116 ? 1.74800   42.58100 -18.99900 1.000 33.50991 ? 115 TYR B O   1 
ATOM   2035 C CB  . TYR B 1 116 ? 4.34500   41.86600 -18.87100 1.000 28.95966 ? 115 TYR B CB  1 
ATOM   2036 C CG  . TYR B 1 116 ? 5.75400   41.44800 -18.59400 1.000 33.79264 ? 115 TYR B CG  1 
ATOM   2037 C CD1 . TYR B 1 116 ? 6.33200   41.68800 -17.35100 1.000 36.82906 ? 115 TYR B CD1 1 
ATOM   2038 C CD2 . TYR B 1 116 ? 6.52200   40.81000 -19.57000 1.000 33.15259 ? 115 TYR B CD2 1 
ATOM   2039 C CE1 . TYR B 1 116 ? 7.63900   41.29600 -17.08200 1.000 38.54005 ? 115 TYR B CE1 1 
ATOM   2040 C CE2 . TYR B 1 116 ? 7.83500   40.42000 -19.31300 1.000 31.58810 ? 115 TYR B CE2 1 
ATOM   2041 C CZ  . TYR B 1 116 ? 8.38100   40.67200 -18.06700 1.000 34.43153 ? 115 TYR B CZ  1 
ATOM   2042 O OH  . TYR B 1 116 ? 9.66200   40.30100 -17.78600 1.000 34.66010 ? 115 TYR B OH  1 
ATOM   2043 N N   . GLY B 1 117 ? 0.91300   40.48300 -18.90900 1.000 28.32158 ? 116 GLY B N   1 
ATOM   2044 C CA  . GLY B 1 117 ? -0.45600  40.87700 -19.22000 1.000 26.54327 ? 116 GLY B CA  1 
ATOM   2045 C C   . GLY B 1 117 ? -0.76000  41.17400 -20.67800 1.000 22.04373 ? 116 GLY B C   1 
ATOM   2046 O O   . GLY B 1 117 ? -1.87200  41.62400 -20.98500 1.000 19.53969 ? 116 GLY B O   1 
ATOM   2047 N N   . ARG B 1 118 ? 0.17300   40.92300 -21.59400 1.000 29.60168 ? 117 ARG B N   1 
ATOM   2048 C CA  . ARG B 1 118 ? 0.01900   41.34900 -22.97800 1.000 27.42805 ? 117 ARG B CA  1 
ATOM   2049 C C   . ARG B 1 118 ? 0.33700   40.22200 -23.94600 1.000 26.38975 ? 117 ARG B C   1 
ATOM   2050 O O   . ARG B 1 118 ? 1.26100   39.43200 -23.72500 1.000 25.18184 ? 117 ARG B O   1 
ATOM   2051 C CB  . ARG B 1 118 ? 0.90600   42.55800 -23.26700 1.000 28.09250 ? 117 ARG B CB  1 
ATOM   2052 C CG  . ARG B 1 118 ? 0.41700   43.80300 -22.53300 1.000 31.64513 ? 117 ARG B CG  1 
ATOM   2053 C CD  . ARG B 1 118 ? -0.42000  44.71100 -23.41800 1.000 25.94039 ? 117 ARG B CD  1 
ATOM   2054 N NE  . ARG B 1 118 ? -0.20600  46.10000 -23.03400 1.000 42.98518 ? 117 ARG B NE  1 
ATOM   2055 C CZ  . ARG B 1 118 ? -0.27500  47.14000 -23.85600 1.000 49.21588 ? 117 ARG B CZ  1 
ATOM   2056 N NH1 . ARG B 1 118 ? -0.56300  46.99000 -25.14300 1.000 46.93722 ? 117 ARG B NH1 1 
ATOM   2057 N NH2 . ARG B 1 118 ? -0.04100  48.36300 -23.37500 1.000 40.16326 ? 117 ARG B NH2 1 
ATOM   2058 N N   . PHE B 1 119 ? -0.42600  40.16700 -25.02900 1.000 23.52411 ? 118 PHE B N   1 
ATOM   2059 C CA  . PHE B 1 119 ? -0.18900  39.16500 -26.05400 1.000 27.50386 ? 118 PHE B CA  1 
ATOM   2060 C C   . PHE B 1 119 ? 1.15000   39.39800 -26.73700 1.000 22.08582 ? 118 PHE B C   1 
ATOM   2061 O O   . PHE B 1 119 ? 1.52500   40.52600 -27.03600 1.000 26.00241 ? 118 PHE B O   1 
ATOM   2062 C CB  . PHE B 1 119 ? -1.33500  39.18100 -27.06300 1.000 23.72194 ? 118 PHE B CB  1 
ATOM   2063 C CG  . PHE B 1 119 ? -2.62700  38.71300 -26.47100 1.000 29.00237 ? 118 PHE B CG  1 
ATOM   2064 C CD1 . PHE B 1 119 ? -3.41400  39.57800 -25.71600 1.000 27.53979 ? 118 PHE B CD1 1 
ATOM   2065 C CD2 . PHE B 1 119 ? -3.01900  37.38900 -26.59400 1.000 25.70678 ? 118 PHE B CD2 1 
ATOM   2066 C CE1 . PHE B 1 119 ? -4.59600  39.13000 -25.13300 1.000 31.99094 ? 118 PHE B CE1 1 
ATOM   2067 C CE2 . PHE B 1 119 ? -4.20300  36.93200 -26.01500 1.000 27.81607 ? 118 PHE B CE2 1 
ATOM   2068 C CZ  . PHE B 1 119 ? -4.99500  37.79900 -25.28500 1.000 27.40590 ? 118 PHE B CZ  1 
ATOM   2069 N N   . LEU B 1 120 ? 1.88100   38.33100 -26.98000 1.000 22.58747 ? 119 LEU B N   1 
ATOM   2070 C CA  . LEU B 1 120 ? 3.17100   38.51200 -27.59700 1.000 26.73859 ? 119 LEU B CA  1 
ATOM   2071 C C   . LEU B 1 120 ? 3.01600   38.82500 -29.08100 1.000 31.07435 ? 119 LEU B C   1 
ATOM   2072 O O   . LEU B 1 120 ? 1.99000   38.51400 -29.69700 1.000 30.13193 ? 119 LEU B O   1 
ATOM   2073 C CB  . LEU B 1 120 ? 4.05900   37.28200 -27.40500 1.000 30.27775 ? 119 LEU B CB  1 
ATOM   2074 C CG  . LEU B 1 120 ? 4.38900   36.85900 -25.97300 1.000 29.17936 ? 119 LEU B CG  1 
ATOM   2075 C CD1 . LEU B 1 120 ? 4.48100   35.33800 -25.86100 1.000 27.33884 ? 119 LEU B CD1 1 
ATOM   2076 C CD2 . LEU B 1 120 ? 5.66700   37.54600 -25.48100 1.000 28.55701 ? 119 LEU B CD2 1 
ATOM   2077 N N   . PRO B 1 121 ? 4.01400   39.47200 -29.66400 1.000 35.01930 ? 120 PRO B N   1 
ATOM   2078 C CA  . PRO B 1 121 ? 4.06800   39.62900 -31.11300 1.000 34.12133 ? 120 PRO B CA  1 
ATOM   2079 C C   . PRO B 1 121 ? 4.61900   38.35200 -31.72500 1.000 36.43268 ? 120 PRO B C   1 
ATOM   2080 O O   . PRO B 1 121 ? 4.96800   37.39800 -31.02400 1.000 27.77010 ? 120 PRO B O   1 
ATOM   2081 C CB  . PRO B 1 121 ? 5.04100   40.78700 -31.29000 1.000 37.50735 ? 120 PRO B CB  1 
ATOM   2082 C CG  . PRO B 1 121 ? 5.99500   40.61400 -30.16600 1.000 34.73989 ? 120 PRO B CG  1 
ATOM   2083 C CD  . PRO B 1 121 ? 5.22700   40.01200 -29.01700 1.000 28.83254 ? 120 PRO B CD  1 
ATOM   2084 N N   . GLN B 1 122 ? 4.72200   38.35900 -33.04900 1.000 39.25949 ? 121 GLN B N   1 
ATOM   2085 C CA  . GLN B 1 122 ? 5.34200   37.24300 -33.73900 1.000 38.76492 ? 121 GLN B CA  1 
ATOM   2086 C C   . GLN B 1 122 ? 6.87100   37.34100 -33.64100 1.000 41.90996 ? 121 GLN B C   1 
ATOM   2087 O O   . GLN B 1 122 ? 7.42500   38.42900 -33.44800 1.000 45.07784 ? 121 GLN B O   1 
ATOM   2088 C CB  . GLN B 1 122 ? 4.87500   37.22000 -35.18800 1.000 37.64054 ? 121 GLN B CB  1 
ATOM   2089 C CG  . GLN B 1 122 ? 3.35600   37.01700 -35.34600 1.000 36.58310 ? 121 GLN B CG  1 
ATOM   2090 C CD  . GLN B 1 122 ? 2.85700   35.60100 -35.04700 1.000 39.69410 ? 121 GLN B CD  1 
ATOM   2091 O OE1 . GLN B 1 122 ? 3.29400   34.95300 -34.09700 1.000 44.75699 ? 121 GLN B OE1 1 
ATOM   2092 N NE2 . GLN B 1 122 ? 1.89800   35.13400 -35.84600 1.000 43.10808 ? 121 GLN B NE2 1 
ATOM   2093 N N   . PRO B 1 123 ? 7.57300   36.20900 -33.72000 1.000 39.93011 ? 122 PRO B N   1 
ATOM   2094 C CA  . PRO B 1 123 ? 9.04000   36.23100 -33.59700 1.000 41.65361 ? 122 PRO B CA  1 
ATOM   2095 C C   . PRO B 1 123 ? 9.69100   37.24500 -34.52600 1.000 45.59218 ? 122 PRO B C   1 
ATOM   2096 O O   . PRO B 1 123 ? 9.28900   37.39900 -35.68400 1.000 46.16793 ? 122 PRO B O   1 
ATOM   2097 C CB  . PRO B 1 123 ? 9.44200   34.80600 -33.98100 1.000 33.91526 ? 122 PRO B CB  1 
ATOM   2098 C CG  . PRO B 1 123 ? 8.27500   33.97400 -33.56900 1.000 35.78713 ? 122 PRO B CG  1 
ATOM   2099 C CD  . PRO B 1 123 ? 7.03900   34.83600 -33.73500 1.000 33.40201 ? 122 PRO B CD  1 
ATOM   2100 N N   . GLY B 1 124 ? 10.72100  37.93400 -34.00600 1.000 50.41844 ? 123 GLY B N   1 
ATOM   2101 C CA  . GLY B 1 124 ? 11.52700  38.86700 -34.78400 1.000 50.04444 ? 123 GLY B CA  1 
ATOM   2102 C C   . GLY B 1 124 ? 10.96800  40.27100 -34.88600 1.000 51.32288 ? 123 GLY B C   1 
ATOM   2103 O O   . GLY B 1 124 ? 11.67000  41.18000 -35.36100 1.000 34.46447 ? 123 GLY B O   1 
ATOM   2104 N N   . HIS B 1 125 ? 9.72700   40.47500 -34.46000 1.000 47.69672 ? 124 HIS B N   1 
ATOM   2105 C CA  . HIS B 1 125 ? 9.10300   41.78400 -34.47800 1.000 44.32052 ? 124 HIS B CA  1 
ATOM   2106 C C   . HIS B 1 125 ? 8.78900   42.21100 -33.03900 1.000 39.52754 ? 124 HIS B C   1 
ATOM   2107 O O   . HIS B 1 125 ? 7.88500   43.00200 -32.77500 1.000 46.13270 ? 124 HIS B O   1 
ATOM   2108 C CB  . HIS B 1 125 ? 7.94000   41.75800 -35.50100 1.000 42.00072 ? 124 HIS B CB  1 
ATOM   2109 C CG  . HIS B 1 125 ? 6.53900   41.90800 -34.97800 1.000 45.19045 ? 124 HIS B CG  1 
ATOM   2110 N ND1 . HIS B 1 125 ? 6.12900   42.95100 -34.16900 1.000 49.15539 ? 124 HIS B ND1 1 
ATOM   2111 C CD2 . HIS B 1 125 ? 5.41400   41.21100 -35.27900 1.000 50.89643 ? 124 HIS B CD2 1 
ATOM   2112 C CE1 . HIS B 1 125 ? 4.83000   42.84800 -33.93600 1.000 52.06880 ? 124 HIS B CE1 1 
ATOM   2113 N NE2 . HIS B 1 125 ? 4.37200   41.79900 -34.59800 1.000 51.71993 ? 124 HIS B NE2 1 
ATOM   2114 N N   . GLU B 1 126 ? 9.62500   41.73400 -32.10500 1.000 36.84217 ? 125 GLU B N   1 
ATOM   2115 C CA  . GLU B 1 126 ? 9.52400   42.07700 -30.68300 1.000 44.50292 ? 125 GLU B CA  1 
ATOM   2116 C C   . GLU B 1 126 ? 9.78200   43.55100 -30.39300 1.000 42.24245 ? 125 GLU B C   1 
ATOM   2117 O O   . GLU B 1 126 ? 9.32900   44.05400 -29.36000 1.000 42.27287 ? 125 GLU B O   1 
ATOM   2118 C CB  . GLU B 1 126 ? 10.53300  41.28100 -29.84600 1.000 41.47784 ? 125 GLU B CB  1 
ATOM   2119 C CG  . GLU B 1 126 ? 10.22100  39.81900 -29.65400 1.000 48.20740 ? 125 GLU B CG  1 
ATOM   2120 C CD  . GLU B 1 126 ? 10.82700  38.96800 -30.74600 1.000 44.21661 ? 125 GLU B CD  1 
ATOM   2121 O OE1 . GLU B 1 126 ? 11.70600  39.48500 -31.47300 1.000 41.33309 ? 125 GLU B OE1 1 
ATOM   2122 O OE2 . GLU B 1 126 ? 10.44100  37.77800 -30.84800 1.000 42.43993 ? 125 GLU B OE2 1 
ATOM   2123 N N   . GLY B 1 127 ? 10.53000  44.25200 -31.24200 1.000 44.55080 ? 126 GLY B N   1 
ATOM   2124 C CA  . GLY B 1 127 ? 10.94800  45.59700 -30.85800 1.000 41.66481 ? 126 GLY B CA  1 
ATOM   2125 C C   . GLY B 1 127 ? 9.81900   46.60800 -31.03000 1.000 42.34638 ? 126 GLY B C   1 
ATOM   2126 O O   . GLY B 1 127 ? 9.52400   47.37700 -30.10800 1.000 43.58535 ? 126 GLY B O   1 
ATOM   2127 N N   . GLU B 1 128 ? 9.18600   46.64400 -32.20200 1.000 36.90738 ? 127 GLU B N   1 
ATOM   2128 C CA  . GLU B 1 128 ? 8.06100   47.55600 -32.35300 1.000 41.17888 ? 127 GLU B CA  1 
ATOM   2129 C C   . GLU B 1 128 ? 6.97900   47.23600 -31.34100 1.000 41.49373 ? 127 GLU B C   1 
ATOM   2130 O O   . GLU B 1 128 ? 6.25500   48.13400 -30.89000 1.000 38.05632 ? 127 GLU B O   1 
ATOM   2131 C CB  . GLU B 1 128 ? 7.53000   47.50400 -33.78100 1.000 42.37984 ? 127 GLU B CB  1 
ATOM   2132 C CG  . GLU B 1 128 ? 6.99600   46.16000 -34.21600 1.000 46.32232 ? 127 GLU B CG  1 
ATOM   2133 C CD  . GLU B 1 128 ? 7.36300   45.84000 -35.66000 1.000 55.15995 ? 127 GLU B CD  1 
ATOM   2134 O OE1 . GLU B 1 128 ? 8.56600   45.95400 -36.01100 1.000 53.74994 ? 127 GLU B OE1 1 
ATOM   2135 O OE2 . GLU B 1 128 ? 6.43800   45.51000 -36.44500 1.000 50.20709 ? 127 GLU B OE2 1 
ATOM   2136 N N   . TRP B 1 129 ? 6.88700   45.96100 -30.95800 1.000 43.41209 ? 128 TRP B N   1 
ATOM   2137 C CA  . TRP B 1 129 ? 6.02900   45.53800 -29.85900 1.000 38.67367 ? 128 TRP B CA  1 
ATOM   2138 C C   . TRP B 1 129 ? 6.40800   46.24200 -28.56600 1.000 35.30195 ? 128 TRP B C   1 
ATOM   2139 O O   . TRP B 1 129 ? 5.58300   46.91200 -27.93200 1.000 38.86138 ? 128 TRP B O   1 
ATOM   2140 C CB  . TRP B 1 129 ? 6.14800   44.02700 -29.69300 1.000 37.03508 ? 128 TRP B CB  1 
ATOM   2141 C CG  . TRP B 1 129 ? 5.24200   43.43100 -28.66300 1.000 37.76368 ? 128 TRP B CG  1 
ATOM   2142 C CD1 . TRP B 1 129 ? 3.92300   43.12000 -28.81300 1.000 31.05345 ? 128 TRP B CD1 1 
ATOM   2143 C CD2 . TRP B 1 129 ? 5.59500   43.05200 -27.32500 1.000 36.76851 ? 128 TRP B CD2 1 
ATOM   2144 N NE1 . TRP B 1 129 ? 3.43200   42.57800 -27.65200 1.000 28.73383 ? 128 TRP B NE1 1 
ATOM   2145 C CE2 . TRP B 1 129 ? 4.43500   42.52900 -26.72100 1.000 29.64402 ? 128 TRP B CE2 1 
ATOM   2146 C CE3 . TRP B 1 129 ? 6.78100   43.09900 -26.58200 1.000 36.53593 ? 128 TRP B CE3 1 
ATOM   2147 C CZ2 . TRP B 1 129 ? 4.42400   42.05800 -25.41400 1.000 25.98501 ? 128 TRP B CZ2 1 
ATOM   2148 C CZ3 . TRP B 1 129 ? 6.76600   42.63500 -25.28000 1.000 32.14928 ? 128 TRP B CZ3 1 
ATOM   2149 C CH2 . TRP B 1 129 ? 5.59700   42.11800 -24.71200 1.000 30.58675 ? 128 TRP B CH2 1 
ATOM   2150 N N   . PHE B 1 130 ? 7.66800   46.09200 -28.16100 1.000 37.17547 ? 129 PHE B N   1 
ATOM   2151 C CA  . PHE B 1 130 ? 8.15100   46.72900 -26.94200 1.000 40.87694 ? 129 PHE B CA  1 
ATOM   2152 C C   . PHE B 1 130 ? 7.89500   48.22900 -26.93500 1.000 44.39460 ? 129 PHE B C   1 
ATOM   2153 O O   . PHE B 1 130 ? 7.75900   48.83300 -25.86600 1.000 47.21754 ? 129 PHE B O   1 
ATOM   2154 C CB  . PHE B 1 130 ? 9.64800   46.47100 -26.77000 1.000 36.86050 ? 129 PHE B CB  1 
ATOM   2155 C CG  . PHE B 1 130 ? 10.24300  47.16800 -25.58700 1.000 35.71307 ? 129 PHE B CG  1 
ATOM   2156 C CD1 . PHE B 1 130 ? 9.94400   46.76000 -24.30700 1.000 36.35121 ? 129 PHE B CD1 1 
ATOM   2157 C CD2 . PHE B 1 130 ? 11.07700  48.25300 -25.75600 1.000 35.39520 ? 129 PHE B CD2 1 
ATOM   2158 C CE1 . PHE B 1 130 ? 10.48600  47.40200 -23.20900 1.000 35.82847 ? 129 PHE B CE1 1 
ATOM   2159 C CE2 . PHE B 1 130 ? 11.61100  48.90400 -24.67000 1.000 33.13384 ? 129 PHE B CE2 1 
ATOM   2160 C CZ  . PHE B 1 130 ? 11.31300  48.47700 -23.39100 1.000 35.56346 ? 129 PHE B CZ  1 
ATOM   2161 N N   . ASP B 1 131 ? 7.82900   48.84900 -28.10600 1.000 42.78380 ? 130 ASP B N   1 
ATOM   2162 C CA  . ASP B 1 131 ? 7.72700   50.29700 -28.15200 1.000 43.29910 ? 130 ASP B CA  1 
ATOM   2163 C C   . ASP B 1 131 ? 6.29500   50.79700 -28.02100 1.000 45.73967 ? 130 ASP B C   1 
ATOM   2164 O O   . ASP B 1 131 ? 6.08000   51.90600 -27.52100 1.000 47.08489 ? 130 ASP B O   1 
ATOM   2165 C CB  . ASP B 1 131 ? 8.35900   50.80300 -29.44700 1.000 45.07390 ? 130 ASP B CB  1 
ATOM   2166 C CG  . ASP B 1 131 ? 9.87900   50.73800 -29.40600 1.000 47.78363 ? 130 ASP B CG  1 
ATOM   2167 O OD1 . ASP B 1 131 ? 10.47100  50.72000 -28.29900 1.000 44.43001 ? 130 ASP B OD1 1 
ATOM   2168 O OD2 . ASP B 1 131 ? 10.48700  50.70200 -30.49200 1.000 52.04572 ? 130 ASP B OD2 1 
ATOM   2169 N N   . ASN B 1 132 ? 5.30600   50.01700 -28.44600 1.000 40.46854 ? 131 ASN B N   1 
ATOM   2170 C CA  . ASN B 1 132 ? 3.92600   50.45300 -28.33400 1.000 43.22009 ? 131 ASN B CA  1 
ATOM   2171 C C   . ASN B 1 132 ? 3.32200   50.10600 -26.99900 1.000 45.20774 ? 131 ASN B C   1 
ATOM   2172 O O   . ASN B 1 132 ? 2.10900   50.25700 -26.82000 1.000 44.65154 ? 131 ASN B O   1 
ATOM   2173 C CB  . ASN B 1 132 ? 3.10100   49.87000 -29.47100 1.000 51.53590 ? 131 ASN B CB  1 
ATOM   2174 C CG  . ASN B 1 132 ? 3.53700   50.42100 -30.79600 1.000 64.37609 ? 131 ASN B CG  1 
ATOM   2175 O OD1 . ASN B 1 132 ? 3.12200   51.51300 -31.18700 1.000 64.57707 ? 131 ASN B OD1 1 
ATOM   2176 N ND2 . ASN B 1 132 ? 4.44500   49.70900 -31.46600 1.000 55.72552 ? 131 ASN B ND2 1 
ATOM   2177 N N   . LEU B 1 133 ? 4.13500   49.63600 -26.07100 1.000 39.11899 ? 132 LEU B N   1 
ATOM   2178 C CA  . LEU B 1 133 ? 3.69000   49.49900 -24.70800 1.000 36.88636 ? 132 LEU B CA  1 
ATOM   2179 C C   . LEU B 1 133 ? 3.82900   50.83400 -24.01000 1.000 40.62038 ? 132 LEU B C   1 
ATOM   2180 O O   . LEU B 1 133 ? 4.64400   51.67800 -24.40200 1.000 32.91901 ? 132 LEU B O   1 
ATOM   2181 C CB  . LEU B 1 133 ? 4.50500   48.43300 -23.99300 1.000 41.10633 ? 132 LEU B CB  1 
ATOM   2182 C CG  . LEU B 1 133 ? 4.50800   47.09100 -24.70800 1.000 40.26729 ? 132 LEU B CG  1 
ATOM   2183 C CD1 . LEU B 1 133 ? 5.65800   46.30200 -24.21600 1.000 39.41785 ? 132 LEU B CD1 1 
ATOM   2184 C CD2 . LEU B 1 133 ? 3.17200   46.31700 -24.46500 1.000 39.83302 ? 132 LEU B CD2 1 
ATOM   2185 N N   . SER B 1 134 ? 3.00900   51.02300 -22.97900 1.000 40.56074 ? 133 SER B N   1 
ATOM   2186 C CA  . SER B 1 134 ? 3.01000   52.27200 -22.24300 1.000 43.86026 ? 133 SER B CA  1 
ATOM   2187 C C   . SER B 1 134 ? 4.34500   52.45500 -21.51900 1.000 37.24840 ? 133 SER B C   1 
ATOM   2188 O O   . SER B 1 134 ? 5.20900   51.57900 -21.51900 1.000 34.72689 ? 133 SER B O   1 
ATOM   2189 C CB  . SER B 1 134 ? 1.81900   52.31500 -21.27400 1.000 44.37651 ? 133 SER B CB  1 
ATOM   2190 O OG  . SER B 1 134 ? 1.68700   51.11300 -20.53200 1.000 29.04314 ? 133 SER B OG  1 
ATOM   2191 N N   . SER B 1 135 ? 4.50400   53.63700 -20.91500 1.000 42.63954 ? 134 SER B N   1 
ATOM   2192 C CA  . SER B 1 135 ? 5.68500   53.93700 -20.10900 1.000 39.66772 ? 134 SER B CA  1 
ATOM   2193 C C   . SER B 1 135 ? 5.84400   52.94900 -18.95900 1.000 35.87686 ? 134 SER B C   1 
ATOM   2194 O O   . SER B 1 135 ? 6.91400   52.35600 -18.76900 1.000 35.76498 ? 134 SER B O   1 
ATOM   2195 C CB  . SER B 1 135 ? 5.58600   55.35200 -19.55100 1.000 37.68215 ? 134 SER B CB  1 
ATOM   2196 O OG  . SER B 1 135 ? 4.83100   56.18300 -20.40100 1.000 43.45196 ? 134 SER B OG  1 
ATOM   2197 N N   . ASP B 1 136 ? 4.80200   52.78100 -18.15600 1.000 28.20254 ? 135 ASP B N   1 
ATOM   2198 C CA  . ASP B 1 136 ? 4.97600   51.98300 -16.95800 1.000 34.03261 ? 135 ASP B CA  1 
ATOM   2199 C C   . ASP B 1 136 ? 5.28900   50.53300 -17.29700 1.000 36.05108 ? 135 ASP B C   1 
ATOM   2200 O O   . ASP B 1 136 ? 6.03600   49.87200 -16.56300 1.000 37.04492 ? 135 ASP B O   1 
ATOM   2201 C CB  . ASP B 1 136 ? 3.73700   52.10900 -16.08100 1.000 33.00883 ? 135 ASP B CB  1 
ATOM   2202 C CG  . ASP B 1 136 ? 3.66600   53.44700 -15.39400 1.000 34.70947 ? 135 ASP B CG  1 
ATOM   2203 O OD1 . ASP B 1 136 ? 4.74700   53.98500 -15.06100 1.000 37.51187 ? 135 ASP B OD1 1 
ATOM   2204 O OD2 . ASP B 1 136 ? 2.54400   53.96600 -15.19700 1.000 38.32601 ? 135 ASP B OD2 1 
ATOM   2205 N N   . GLU B 1 137 ? 4.76700   50.03300 -18.42000 1.000 38.76035 ? 136 GLU B N   1 
ATOM   2206 C CA  . GLU B 1 137 ? 4.99600   48.63600 -18.77500 1.000 33.94290 ? 136 GLU B CA  1 
ATOM   2207 C C   . GLU B 1 137 ? 6.43500   48.42600 -19.23100 1.000 33.79829 ? 136 GLU B C   1 
ATOM   2208 O O   . GLU B 1 137 ? 7.09300   47.46500 -18.81900 1.000 33.12948 ? 136 GLU B O   1 
ATOM   2209 C CB  . GLU B 1 137 ? 3.99500   48.20500 -19.84900 1.000 34.92587 ? 136 GLU B CB  1 
ATOM   2210 C CG  . GLU B 1 137 ? 2.61800   47.81900 -19.30200 1.000 27.64667 ? 136 GLU B CG  1 
ATOM   2211 C CD  . GLU B 1 137 ? 1.55400   47.63300 -20.39500 1.000 31.00536 ? 136 GLU B CD  1 
ATOM   2212 O OE1 . GLU B 1 137 ? 1.31500   48.58100 -21.16900 1.000 41.71918 ? 136 GLU B OE1 1 
ATOM   2213 O OE2 . GLU B 1 137 ? 0.93300   46.55100 -20.47700 1.000 29.54923 ? 136 GLU B OE2 1 
ATOM   2214 N N   . ARG B 1 138 ? 6.95200   49.33200 -20.06000 1.000 35.72562 ? 137 ARG B N   1 
ATOM   2215 C CA  . ARG B 1 138 ? 8.36000   49.27100 -20.43300 1.000 31.16159 ? 137 ARG B CA  1 
ATOM   2216 C C   . ARG B 1 138 ? 9.24100   49.31500 -19.19400 1.000 39.07259 ? 137 ARG B C   1 
ATOM   2217 O O   . ARG B 1 138 ? 10.12200  48.47000 -19.02300 1.000 40.38435 ? 137 ARG B O   1 
ATOM   2218 C CB  . ARG B 1 138 ? 8.70600   50.42300 -21.37000 1.000 29.10312 ? 137 ARG B CB  1 
ATOM   2219 C CG  . ARG B 1 138 ? 8.07500   50.32300 -22.72400 1.000 37.67000 ? 137 ARG B CG  1 
ATOM   2220 C CD  . ARG B 1 138 ? 8.49700   51.48300 -23.59600 1.000 41.88209 ? 137 ARG B CD  1 
ATOM   2221 N NE  . ARG B 1 138 ? 7.33400   52.17400 -24.13300 1.000 39.79233 ? 137 ARG B NE  1 
ATOM   2222 C CZ  . ARG B 1 138 ? 7.04800   53.44800 -23.90600 1.000 48.83561 ? 137 ARG B CZ  1 
ATOM   2223 N NH1 . ARG B 1 138 ? 7.85900   54.22300 -23.20300 1.000 42.68621 ? 137 ARG B NH1 1 
ATOM   2224 N NH2 . ARG B 1 138 ? 5.91500   53.95700 -24.39700 1.000 54.70400 ? 137 ARG B NH2 1 
ATOM   2225 N N   . ALA B 1 139 ? 8.99400   50.28500 -18.30300 1.000 38.53360 ? 138 ALA B N   1 
ATOM   2226 C CA  . ALA B 1 139 ? 9.79600   50.42300 -17.09200 1.000 32.40331 ? 138 ALA B CA  1 
ATOM   2227 C C   . ALA B 1 139 ? 9.90700   49.09900 -16.36100 1.000 34.46577 ? 138 ALA B C   1 
ATOM   2228 O O   . ALA B 1 139 ? 11.00900  48.64400 -16.04600 1.000 38.90752 ? 138 ALA B O   1 
ATOM   2229 C CB  . ALA B 1 139 ? 9.19100   51.48300 -16.17500 1.000 26.52357 ? 138 ALA B CB  1 
ATOM   2230 N N   . PHE B 1 140 ? 8.76600   48.44200 -16.13400 1.000 39.97976 ? 139 PHE B N   1 
ATOM   2231 C CA  . PHE B 1 140 ? 8.74100   47.20900 -15.35000 1.000 39.83424 ? 139 PHE B CA  1 
ATOM   2232 C C   . PHE B 1 140 ? 9.57200   46.11500 -16.00400 1.000 36.90033 ? 139 PHE B C   1 
ATOM   2233 O O   . PHE B 1 140 ? 10.43300  45.49800 -15.36700 1.000 34.04405 ? 139 PHE B O   1 
ATOM   2234 C CB  . PHE B 1 140 ? 7.30300   46.74000 -15.16900 1.000 35.40188 ? 139 PHE B CB  1 
ATOM   2235 C CG  . PHE B 1 140 ? 7.19700   45.44700 -14.45200 1.000 39.06933 ? 139 PHE B CG  1 
ATOM   2236 C CD1 . PHE B 1 140 ? 7.75500   45.29700 -13.19400 1.000 42.25326 ? 139 PHE B CD1 1 
ATOM   2237 C CD2 . PHE B 1 140 ? 6.57100   44.36500 -15.03700 1.000 37.90423 ? 139 PHE B CD2 1 
ATOM   2238 C CE1 . PHE B 1 140 ? 7.66800   44.09000 -12.52600 1.000 39.42410 ? 139 PHE B CE1 1 
ATOM   2239 C CE2 . PHE B 1 140 ? 6.47500   43.16200 -14.37000 1.000 34.75009 ? 139 PHE B CE2 1 
ATOM   2240 C CZ  . PHE B 1 140 ? 7.02300   43.02500 -13.11900 1.000 38.74774 ? 139 PHE B CZ  1 
ATOM   2241 N N   . MET B 1 141 ? 9.32300   45.86100 -17.28300 1.000 42.90654 ? 140 MET B N   1 
ATOM   2242 C CA  . MET B 1 141 ? 10.11800  44.88300 -18.01000 1.000 36.96900 ? 140 MET B CA  1 
ATOM   2243 C C   . MET B 1 141 ? 11.58100  45.31800 -18.10400 1.000 39.04143 ? 140 MET B C   1 
ATOM   2244 O O   . MET B 1 141 ? 12.48400  44.47700 -18.05300 1.000 42.57525 ? 140 MET B O   1 
ATOM   2245 C CB  . MET B 1 141 ? 9.53200   44.70600 -19.40000 1.000 35.38953 ? 140 MET B CB  1 
ATOM   2246 C CG  . MET B 1 141 ? 8.02500   44.68000 -19.46100 1.000 41.67533 ? 140 MET B CG  1 
ATOM   2247 S SD  . MET B 1 141 ? 7.59400   44.05500 -21.09100 1.000 43.08802 ? 140 MET B SD  1 
ATOM   2248 C CE  . MET B 1 141 ? 7.93700   45.55000 -21.98300 1.000 37.96622 ? 140 MET B CE  1 
ATOM   2249 N N   . GLU B 1 142 ? 11.83400  46.62700 -18.26200 1.000 42.97048 ? 141 GLU B N   1 
ATOM   2250 C CA  . GLU B 1 142 ? 13.20800  47.13200 -18.31100 1.000 35.11012 ? 141 GLU B CA  1 
ATOM   2251 C C   . GLU B 1 142 ? 14.01000  46.63000 -17.12500 1.000 40.02229 ? 141 GLU B C   1 
ATOM   2252 O O   . GLU B 1 142 ? 15.14900  46.17200 -17.28100 1.000 46.18839 ? 141 GLU B O   1 
ATOM   2253 C CB  . GLU B 1 142 ? 13.23800  48.66800 -18.34100 1.000 37.10385 ? 141 GLU B CB  1 
ATOM   2254 C CG  . GLU B 1 142 ? 12.80400  49.34100 -19.66900 1.000 41.97800 ? 141 GLU B CG  1 
ATOM   2255 C CD  . GLU B 1 142 ? 13.63100  50.55800 -20.05300 1.000 42.24675 ? 141 GLU B CD  1 
ATOM   2256 O OE1 . GLU B 1 142 ? 13.86800  51.42400 -19.17800 1.000 48.88698 ? 141 GLU B OE1 1 
ATOM   2257 O OE2 . GLU B 1 142 ? 14.01600  50.66700 -21.24100 1.000 44.74132 ? 141 GLU B OE2 1 
ATOM   2258 N N   . THR B 1 143 ? 13.42200  46.69200 -15.92800 1.000 38.72746 ? 142 THR B N   1 
ATOM   2259 C CA  . THR B 1 143 ? 14.13900  46.25700 -14.73400 1.000 41.01268 ? 142 THR B CA  1 
ATOM   2260 C C   . THR B 1 143 ? 14.68400  44.83700 -14.87200 1.000 46.23529 ? 142 THR B C   1 
ATOM   2261 O O   . THR B 1 143 ? 15.77400  44.53800 -14.37100 1.000 49.32178 ? 142 THR B O   1 
ATOM   2262 C CB  . THR B 1 143 ? 13.23300  46.33200 -13.50400 1.000 39.07218 ? 142 THR B CB  1 
ATOM   2263 O OG1 . THR B 1 143 ? 12.34800  45.20900 -13.51000 1.000 46.37768 ? 142 THR B OG1 1 
ATOM   2264 C CG2 . THR B 1 143 ? 12.41300  47.61200 -13.49500 1.000 35.83460 ? 142 THR B CG2 1 
ATOM   2265 N N   . ASN B 1 144 ? 13.96100  43.96000 -15.56600 1.000 46.89730 ? 143 ASN B N   1 
ATOM   2266 C CA  . ASN B 1 144 ? 14.27500  42.52800 -15.58200 1.000 44.49823 ? 143 ASN B CA  1 
ATOM   2267 C C   . ASN B 1 144 ? 15.32800  42.19900 -16.64900 1.000 43.03318 ? 143 ASN B C   1 
ATOM   2268 O O   . ASN B 1 144 ? 15.10300  41.42600 -17.57700 1.000 44.07792 ? 143 ASN B O   1 
ATOM   2269 C CB  . ASN B 1 144 ? 12.99600  41.71800 -15.78900 1.000 38.40947 ? 143 ASN B CB  1 
ATOM   2270 C CG  . ASN B 1 144 ? 12.00900  41.87200 -14.63200 1.000 41.83162 ? 143 ASN B CG  1 
ATOM   2271 O OD1 . ASN B 1 144 ? 12.40700  41.98000 -13.46800 1.000 39.77209 ? 143 ASN B OD1 1 
ATOM   2272 N ND2 . ASN B 1 144 ? 10.71700  41.90100 -14.95200 1.000 39.15957 ? 143 ASN B ND2 1 
ATOM   2273 N N   . VAL B 1 145 ? 16.50700  42.80700 -16.51300 1.000 44.01999 ? 144 VAL B N   1 
ATOM   2274 C CA  . VAL B 1 145 ? 17.64900  42.47700 -17.36800 1.000 46.60723 ? 144 VAL B CA  1 
ATOM   2275 C C   . VAL B 1 145 ? 18.87500  42.37400 -16.46500 1.000 54.43653 ? 144 VAL B C   1 
ATOM   2276 O O   . VAL B 1 145 ? 19.30900  43.37800 -15.88300 1.000 48.65718 ? 144 VAL B O   1 
ATOM   2277 C CB  . VAL B 1 145 ? 17.90000  43.50300 -18.49400 1.000 52.40952 ? 144 VAL B CB  1 
ATOM   2278 C CG1 . VAL B 1 145 ? 18.80200  42.89100 -19.56900 1.000 47.52581 ? 144 VAL B CG1 1 
ATOM   2279 C CG2 . VAL B 1 145 ? 16.59200  44.04800 -19.11400 1.000 44.12348 ? 144 VAL B CG2 1 
ATOM   2280 N N   . ASP B 1 146 ? 19.44100  41.17200 -16.36000 1.000 54.27268 ? 145 ASP B N   1 
ATOM   2281 C CA  . ASP B 1 146 ? 20.65000  40.95300 -15.57500 1.000 54.99840 ? 145 ASP B CA  1 
ATOM   2282 C C   . ASP B 1 146 ? 21.90300  41.14900 -16.44000 1.000 63.29044 ? 145 ASP B C   1 
ATOM   2283 O O   . ASP B 1 146 ? 22.24300  42.26900 -16.83300 1.000 60.78814 ? 145 ASP B O   1 
ATOM   2284 C CB  . ASP B 1 146 ? 20.63800  39.54600 -14.96100 1.000 48.67575 ? 145 ASP B CB  1 
ATOM   2285 C CG  . ASP B 1 146 ? 21.80200  39.30900 -13.99300 1.000 60.33180 ? 145 ASP B CG  1 
ATOM   2286 O OD1 . ASP B 1 146 ? 22.97700  39.36500 -14.43900 1.000 54.26637 ? 145 ASP B OD1 1 
ATOM   2287 O OD2 . ASP B 1 146 ? 21.54300  39.04900 -12.78900 1.000 56.03636 ? 145 ASP B OD2 1 
ATOM   2288 N N   . PRO C 1 2   ? -10.37000 21.16000 -19.72300 1.000 32.08607 ? 1   PRO C N   1 
ATOM   2289 C CA  . PRO C 1 2   ? -9.09000  21.86200 -19.54200 1.000 30.11596 ? 1   PRO C CA  1 
ATOM   2290 C C   . PRO C 1 2   ? -8.37000  21.49900 -18.25900 1.000 29.15477 ? 1   PRO C C   1 
ATOM   2291 O O   . PRO C 1 2   ? -9.00200  21.24700 -17.22900 1.000 27.75771 ? 1   PRO C O   1 
ATOM   2292 C CB  . PRO C 1 2   ? -9.50200  23.32300 -19.47900 1.000 20.01091 ? 1   PRO C CB  1 
ATOM   2293 C CG  . PRO C 1 2   ? -10.83900 23.26200 -18.86600 1.000 24.14878 ? 1   PRO C CG  1 
ATOM   2294 C CD  . PRO C 1 2   ? -11.51000 22.04300 -19.42600 1.000 23.79717 ? 1   PRO C CD  1 
ATOM   2295 N N   . VAL C 1 3   ? -7.04700  21.46400 -18.32300 1.000 23.35551 ? 2   VAL C N   1 
ATOM   2296 C CA  . VAL C 1 3   ? -6.21500  21.50300 -17.13600 1.000 24.07405 ? 2   VAL C CA  1 
ATOM   2297 C C   . VAL C 1 3   ? -5.45900  22.81300 -17.20700 1.000 22.38051 ? 2   VAL C C   1 
ATOM   2298 O O   . VAL C 1 3   ? -4.89300  23.15100 -18.25000 1.000 24.67092 ? 2   VAL C O   1 
ATOM   2299 C CB  . VAL C 1 3   ? -5.25900  20.29800 -17.04200 1.000 24.10884 ? 2   VAL C CB  1 
ATOM   2300 C CG1 . VAL C 1 3   ? -4.32500  20.45500 -15.85000 1.000 19.48383 ? 2   VAL C CG1 1 
ATOM   2301 C CG2 . VAL C 1 3   ? -6.04200  19.01500 -16.89200 1.000 24.59081 ? 2   VAL C CG2 1 
ATOM   2302 N N   . TYR C 1 4   ? -5.50900  23.56900 -16.13100 1.000 20.86927 ? 3   TYR C N   1 
ATOM   2303 C CA  . TYR C 1 4   ? -4.76800  24.81100 -15.98100 1.000 23.56844 ? 3   TYR C CA  1 
ATOM   2304 C C   . TYR C 1 4   ? -3.71200  24.58500 -14.89600 1.000 21.46911 ? 3   TYR C C   1 
ATOM   2305 O O   . TYR C 1 4   ? -4.05200  24.37800 -13.72800 1.000 17.30290 ? 3   TYR C O   1 
ATOM   2306 C CB  . TYR C 1 4   ? -5.71800  25.95100 -15.61000 1.000 24.02260 ? 3   TYR C CB  1 
ATOM   2307 C CG  . TYR C 1 4   ? -6.61100  26.44700 -16.73300 1.000 23.83066 ? 3   TYR C CG  1 
ATOM   2308 C CD1 . TYR C 1 4   ? -6.11000  27.29600 -17.72300 1.000 23.94447 ? 3   TYR C CD1 1 
ATOM   2309 C CD2 . TYR C 1 4   ? -7.96600  26.09400 -16.79000 1.000 22.79331 ? 3   TYR C CD2 1 
ATOM   2310 C CE1 . TYR C 1 4   ? -6.93200  27.76900 -18.74200 1.000 29.17958 ? 3   TYR C CE1 1 
ATOM   2311 C CE2 . TYR C 1 4   ? -8.80100  26.56700 -17.80500 1.000 19.58691 ? 3   TYR C CE2 1 
ATOM   2312 C CZ  . TYR C 1 4   ? -8.27700  27.39600 -18.77800 1.000 28.26233 ? 3   TYR C CZ  1 
ATOM   2313 O OH  . TYR C 1 4   ? -9.08000  27.86100 -19.79100 1.000 23.40109 ? 3   TYR C OH  1 
ATOM   2314 N N   . MET C 1 5   ? -2.44100  24.59200 -15.28000 1.000 20.67219 ? 4   MET C N   1 
ATOM   2315 C CA  . MET C 1 5   ? -1.33900  24.48300 -14.33000 1.000 19.81754 ? 4   MET C CA  1 
ATOM   2316 C C   . MET C 1 5   ? -0.95000  25.87600 -13.85800 1.000 22.17168 ? 4   MET C C   1 
ATOM   2317 O O   . MET C 1 5   ? -0.53800  26.71100 -14.66600 1.000 24.10806 ? 4   MET C O   1 
ATOM   2318 C CB  . MET C 1 5   ? -0.14600  23.79200 -14.98400 1.000 23.13787 ? 4   MET C CB  1 
ATOM   2319 C CG  . MET C 1 5   ? -0.50900  22.49800 -15.67800 1.000 23.21972 ? 4   MET C CG  1 
ATOM   2320 S SD  . MET C 1 5   ? -1.19700  21.26200 -14.53000 1.000 31.25271 ? 4   MET C SD  1 
ATOM   2321 C CE  . MET C 1 5   ? 0.12200   21.06900 -13.32300 1.000 22.69974 ? 4   MET C CE  1 
ATOM   2322 N N   . VAL C 1 6   ? -1.07300  26.13800 -12.56500 1.000 23.13894 ? 5   VAL C N   1 
ATOM   2323 C CA  . VAL C 1 6   ? -0.86800  27.48900 -12.05400 1.000 23.92672 ? 5   VAL C CA  1 
ATOM   2324 C C   . VAL C 1 6   ? 0.36400   27.47700 -11.16100 1.000 24.04271 ? 5   VAL C C   1 
ATOM   2325 O O   . VAL C 1 6   ? 0.36200   26.88300 -10.07600 1.000 27.46787 ? 5   VAL C O   1 
ATOM   2326 C CB  . VAL C 1 6   ? -2.11200  28.01800 -11.33200 1.000 18.59378 ? 5   VAL C CB  1 
ATOM   2327 C CG1 . VAL C 1 6   ? -1.96200  29.49800 -11.03500 1.000 16.89056 ? 5   VAL C CG1 1 
ATOM   2328 C CG2 . VAL C 1 6   ? -3.34200  27.78400 -12.22000 1.000 14.91037 ? 5   VAL C CG2 1 
ATOM   2329 N N   . TYR C 1 7   ? 1.41200   28.15900 -11.61800 1.000 29.52198 ? 6   TYR C N   1 
ATOM   2330 C CA  . TYR C 1 7   ? 2.73400   28.14400 -10.99600 1.000 23.01382 ? 6   TYR C CA  1 
ATOM   2331 C C   . TYR C 1 7   ? 2.90000   29.41400 -10.16700 1.000 25.13328 ? 6   TYR C C   1 
ATOM   2332 O O   . TYR C 1 7   ? 3.10200   30.50100 -10.71800 1.000 32.12124 ? 6   TYR C O   1 
ATOM   2333 C CB  . TYR C 1 7   ? 3.80300   28.03100 -12.08100 1.000 21.30881 ? 6   TYR C CB  1 
ATOM   2334 C CG  . TYR C 1 7   ? 3.63800   26.78400 -12.93700 1.000 20.60700 ? 6   TYR C CG  1 
ATOM   2335 C CD1 . TYR C 1 7   ? 4.04400   25.53000 -12.47300 1.000 20.82641 ? 6   TYR C CD1 1 
ATOM   2336 C CD2 . TYR C 1 7   ? 3.05700   26.85300 -14.18700 1.000 22.34559 ? 6   TYR C CD2 1 
ATOM   2337 C CE1 . TYR C 1 7   ? 3.90700   24.38000 -13.25300 1.000 20.99672 ? 6   TYR C CE1 1 
ATOM   2338 C CE2 . TYR C 1 7   ? 2.89300   25.70600 -14.97200 1.000 24.69010 ? 6   TYR C CE2 1 
ATOM   2339 C CZ  . TYR C 1 7   ? 3.32000   24.47700 -14.49800 1.000 25.05032 ? 6   TYR C CZ  1 
ATOM   2340 O OH  . TYR C 1 7   ? 3.15200   23.35700 -15.27800 1.000 25.89829 ? 6   TYR C OH  1 
ATOM   2341 N N   . VAL C 1 8   ? 2.80700   29.28000 -8.84300  1.000 24.65098 ? 7   VAL C N   1 
ATOM   2342 C CA  . VAL C 1 8   ? 2.85500   30.41600 -7.93200  1.000 22.75578 ? 7   VAL C CA  1 
ATOM   2343 C C   . VAL C 1 8   ? 3.97100   30.21500 -6.93000  1.000 21.45739 ? 7   VAL C C   1 
ATOM   2344 O O   . VAL C 1 8   ? 4.37000   29.09300 -6.62100  1.000 26.88820 ? 7   VAL C O   1 
ATOM   2345 C CB  . VAL C 1 8   ? 1.52800   30.61900 -7.18900  1.000 20.55415 ? 7   VAL C CB  1 
ATOM   2346 C CG1 . VAL C 1 8   ? 0.44000   31.12100 -8.15000  1.000 21.19298 ? 7   VAL C CG1 1 
ATOM   2347 C CG2 . VAL C 1 8   ? 1.13100   29.31400 -6.51900  1.000 20.99730 ? 7   VAL C CG2 1 
ATOM   2348 N N   . SER C 1 9   ? 4.46100   31.32400 -6.40400  1.000 23.33677 ? 8   SER C N   1 
ATOM   2349 C CA  . SER C 1 9   ? 5.42700   31.24700 -5.32100  1.000 24.78576 ? 8   SER C CA  1 
ATOM   2350 C C   . SER C 1 9   ? 4.73600   30.80400 -4.04400  1.000 19.01682 ? 8   SER C C   1 
ATOM   2351 O O   . SER C 1 9   ? 3.59500   31.17500 -3.78900  1.000 25.66124 ? 8   SER C O   1 
ATOM   2352 C CB  . SER C 1 9   ? 6.10000   32.59300 -5.10600  1.000 23.53056 ? 8   SER C CB  1 
ATOM   2353 O OG  . SER C 1 9   ? 7.19300   32.74200 -5.97900  1.000 30.57235 ? 8   SER C OG  1 
ATOM   2354 N N   . GLN C 1 10  ? 5.45200   30.03300 -3.23300  1.000 20.73578 ? 9   GLN C N   1 
ATOM   2355 C CA  . GLN C 1 10  ? 4.90800   29.44300 -2.01900  1.000 23.32171 ? 9   GLN C CA  1 
ATOM   2356 C C   . GLN C 1 10  ? 4.29200   30.49300 -1.09600  1.000 26.43625 ? 9   GLN C C   1 
ATOM   2357 O O   . GLN C 1 10  ? 4.89100   31.53600 -0.82800  1.000 25.34126 ? 9   GLN C O   1 
ATOM   2358 C CB  . GLN C 1 10  ? 6.02100   28.68200 -1.29700  1.000 27.01942 ? 9   GLN C CB  1 
ATOM   2359 C CG  . GLN C 1 10  ? 5.57100   28.03000 -0.03200  1.000 25.26541 ? 9   GLN C CG  1 
ATOM   2360 C CD  . GLN C 1 10  ? 5.02500   26.64600 -0.28800  1.000 37.83916 ? 9   GLN C CD  1 
ATOM   2361 O OE1 . GLN C 1 10  ? 5.57500   25.88800 -1.09600  1.000 41.93939 ? 9   GLN C OE1 1 
ATOM   2362 N NE2 . GLN C 1 10  ? 3.89100   26.32700 0.34900   1.000 35.55486 ? 9   GLN C NE2 1 
ATOM   2363 N N   . ASP C 1 11  ? 3.06700   30.21900 -0.63800  1.000 29.88804 ? 10  ASP C N   1 
ATOM   2364 C CA  . ASP C 1 11  ? 2.31400   31.02100 0.32900   1.000 32.96399 ? 10  ASP C CA  1 
ATOM   2365 C C   . ASP C 1 11  ? 1.85500   32.37200 -0.19600  1.000 34.09144 ? 10  ASP C C   1 
ATOM   2366 O O   . ASP C 1 11  ? 1.34700   33.18300 0.60500   1.000 33.77707 ? 10  ASP C O   1 
ATOM   2367 C CB  . ASP C 1 11  ? 3.09700   31.30300 1.61400   1.000 35.09912 ? 10  ASP C CB  1 
ATOM   2368 C CG  . ASP C 1 11  ? 3.55300   30.05100 2.30200   1.000 40.92126 ? 10  ASP C CG  1 
ATOM   2369 O OD1 . ASP C 1 11  ? 2.74500   29.08100 2.36900   1.000 33.88096 ? 10  ASP C OD1 1 
ATOM   2370 O OD2 . ASP C 1 11  ? 4.73700   30.04700 2.74100   1.000 36.17869 ? 10  ASP C OD2 1 
ATOM   2371 N N   . ARG C 1 12  ? 2.02100   32.67000 -1.49000  1.000 24.94125 ? 11  ARG C N   1 
ATOM   2372 C CA  . ARG C 1 12  ? 1.53900   33.96400 -1.95200  1.000 22.23033 ? 11  ARG C CA  1 
ATOM   2373 C C   . ARG C 1 12  ? 0.02100   33.97400 -2.02000  1.000 30.28839 ? 11  ARG C C   1 
ATOM   2374 O O   . ARG C 1 12  ? -0.62200  34.98700 -1.71200  1.000 33.56728 ? 11  ARG C O   1 
ATOM   2375 C CB  . ARG C 1 12  ? 2.12300   34.33300 -3.31000  1.000 26.57902 ? 11  ARG C CB  1 
ATOM   2376 C CG  . ARG C 1 12  ? 2.11100   35.83100 -3.43200  1.000 32.52172 ? 11  ARG C CG  1 
ATOM   2377 C CD  . ARG C 1 12  ? 1.78900   36.35700 -4.78800  1.000 33.33522 ? 11  ARG C CD  1 
ATOM   2378 N NE  . ARG C 1 12  ? 1.78100   37.82000 -4.76700  1.000 37.00908 ? 11  ARG C NE  1 
ATOM   2379 C CZ  . ARG C 1 12  ? 0.77200   38.56500 -4.32700  1.000 39.05201 ? 11  ARG C CZ  1 
ATOM   2380 N NH1 . ARG C 1 12  ? -0.35800  38.01900 -3.88400  1.000 26.65650 ? 11  ARG C NH1 1 
ATOM   2381 N NH2 . ARG C 1 12  ? 0.88800   39.89200 -4.35800  1.000 43.02681 ? 11  ARG C NH2 1 
ATOM   2382 N N   . LEU C 1 13  ? -0.56800  32.86300 -2.43500  1.000 28.57274 ? 12  LEU C N   1 
ATOM   2383 C CA  . LEU C 1 13  ? -2.00600  32.69900 -2.37400  1.000 25.24434 ? 12  LEU C CA  1 
ATOM   2384 C C   . LEU C 1 13  ? -2.33700  32.06300 -1.02800  1.000 26.39719 ? 12  LEU C C   1 
ATOM   2385 O O   . LEU C 1 13  ? -1.92500  30.93100 -0.74000  1.000 24.30180 ? 12  LEU C O   1 
ATOM   2386 C CB  . LEU C 1 13  ? -2.48900  31.86900 -3.55800  1.000 26.89653 ? 12  LEU C CB  1 
ATOM   2387 C CG  . LEU C 1 13  ? -2.07200  32.54000 -4.87900  1.000 30.10340 ? 12  LEU C CG  1 
ATOM   2388 C CD1 . LEU C 1 13  ? -2.51600  31.77900 -6.14100  1.000 15.27270 ? 12  LEU C CD1 1 
ATOM   2389 C CD2 . LEU C 1 13  ? -2.57800  33.96800 -4.89600  1.000 24.15168 ? 12  LEU C CD2 1 
ATOM   2390 N N   . THR C 1 14  ? -3.03400  32.80500 -0.17600  1.000 23.64629 ? 13  THR C N   1 
ATOM   2391 C CA  . THR C 1 14  ? -3.72100  32.14000 0.90800   1.000 30.31021 ? 13  THR C CA  1 
ATOM   2392 C C   . THR C 1 14  ? -4.65000  31.08300 0.31400   1.000 30.27312 ? 13  THR C C   1 
ATOM   2393 O O   . THR C 1 14  ? -5.05700  31.18300 -0.85600  1.000 27.35168 ? 13  THR C O   1 
ATOM   2394 C CB  . THR C 1 14  ? -4.54000  33.12000 1.74600   1.000 28.05790 ? 13  THR C CB  1 
ATOM   2395 O OG1 . THR C 1 14  ? -5.66300  33.57200 0.96900   1.000 28.86807 ? 13  THR C OG1 1 
ATOM   2396 C CG2 . THR C 1 14  ? -3.68900  34.29900 2.20200   1.000 26.03204 ? 13  THR C CG2 1 
ATOM   2397 N N   . PRO C 1 15  ? -4.96500  30.03700 1.08800   1.000 28.09110 ? 14  PRO C N   1 
ATOM   2398 C CA  . PRO C 1 15  ? -5.97900  29.07800 0.62500   1.000 29.06712 ? 14  PRO C CA  1 
ATOM   2399 C C   . PRO C 1 15  ? -7.19100  29.77100 0.04900   1.000 28.42745 ? 14  PRO C C   1 
ATOM   2400 O O   . PRO C 1 15  ? -7.65600  29.41400 -1.04300  1.000 26.34522 ? 14  PRO C O   1 
ATOM   2401 C CB  . PRO C 1 15  ? -6.29800  28.29200 1.89900   1.000 30.40551 ? 14  PRO C CB  1 
ATOM   2402 C CG  . PRO C 1 15  ? -4.96400  28.26800 2.61000   1.000 22.15397 ? 14  PRO C CG  1 
ATOM   2403 C CD  . PRO C 1 15  ? -4.33100  29.60700 2.34700   1.000 17.40051 ? 14  PRO C CD  1 
ATOM   2404 N N   . SER C 1 16  ? -7.65000  30.82700 0.72300   1.000 24.33349 ? 15  SER C N   1 
ATOM   2405 C CA  . SER C 1 16  ? -8.76500  31.60600 0.21100   1.000 28.85115 ? 15  SER C CA  1 
ATOM   2406 C C   . SER C 1 16  ? -8.45500  32.20100 -1.16600  1.000 30.19450 ? 15  SER C C   1 
ATOM   2407 O O   . SER C 1 16  ? -9.33600  32.27300 -2.03200  1.000 27.22123 ? 15  SER C O   1 
ATOM   2408 C CB  . SER C 1 16  ? -9.12200  32.69400 1.21500   1.000 26.08056 ? 15  SER C CB  1 
ATOM   2409 O OG  . SER C 1 16  ? -10.21000 33.47500 0.75300   1.000 37.64472 ? 15  SER C OG  1 
ATOM   2410 N N   . ALA C 1 17  ? -7.21300  32.62500 -1.39500  1.000 29.25393 ? 16  ALA C N   1 
ATOM   2411 C CA  . ALA C 1 17  ? -6.87000  33.21100 -2.68700  1.000 25.83609 ? 16  ALA C CA  1 
ATOM   2412 C C   . ALA C 1 17  ? -6.89900  32.14900 -3.78100  1.000 29.58048 ? 16  ALA C C   1 
ATOM   2413 O O   . ALA C 1 17  ? -7.61600  32.28900 -4.77900  1.000 23.04756 ? 16  ALA C O   1 
ATOM   2414 C CB  . ALA C 1 17  ? -5.49900  33.88700 -2.60700  1.000 30.31366 ? 16  ALA C CB  1 
ATOM   2415 N N   . LYS C 1 18  ? -6.12700  31.06800 -3.59100  1.000 32.24518 ? 17  LYS C N   1 
ATOM   2416 C CA  . LYS C 1 18  ? -6.17800  29.88500 -4.45300  1.000 28.43139 ? 17  LYS C CA  1 
ATOM   2417 C C   . LYS C 1 18  ? -7.60100  29.52400 -4.85700  1.000 26.69921 ? 17  LYS C C   1 
ATOM   2418 O O   . LYS C 1 18  ? -7.88500  29.22300 -6.02400  1.000 24.67748 ? 17  LYS C O   1 
ATOM   2419 C CB  . LYS C 1 18  ? -5.55800  28.68900 -3.72800  1.000 25.27750 ? 17  LYS C CB  1 
ATOM   2420 C CG  . LYS C 1 18  ? -4.05600  28.60200 -3.77400  1.000 22.83917 ? 17  LYS C CG  1 
ATOM   2421 C CD  . LYS C 1 18  ? -3.60200  27.71700 -2.64500  1.000 21.71383 ? 17  LYS C CD  1 
ATOM   2422 C CE  . LYS C 1 18  ? -2.11800  27.66900 -2.54200  1.000 29.81050 ? 17  LYS C CE  1 
ATOM   2423 N NZ  . LYS C 1 18  ? -1.77400  26.51600 -1.71400  1.000 29.68647 ? 17  LYS C NZ  1 
ATOM   2424 N N   . HIS C 1 19  ? -8.50700  29.50900 -3.88900  1.000 27.63896 ? 18  HIS C N   1 
ATOM   2425 C CA  . HIS C 1 19  ? -9.88700  29.21500 -4.23200  1.000 29.29122 ? 18  HIS C CA  1 
ATOM   2426 C C   . HIS C 1 19  ? -10.43000 30.26300 -5.19400  1.000 28.50223 ? 18  HIS C C   1 
ATOM   2427 O O   . HIS C 1 19  ? -11.01400 29.91900 -6.23200  1.000 28.47786 ? 18  HIS C O   1 
ATOM   2428 C CB  . HIS C 1 19  ? -10.75500 29.10300 -2.97300  1.000 22.85221 ? 18  HIS C CB  1 
ATOM   2429 C CG  . HIS C 1 19  ? -12.01300 28.33200 -3.20800  1.000 26.96202 ? 18  HIS C CG  1 
ATOM   2430 N ND1 . HIS C 1 19  ? -13.05000 28.28700 -2.30500  1.000 31.46998 ? 18  HIS C ND1 1 
ATOM   2431 C CD2 . HIS C 1 19  ? -12.40400 27.58200 -4.26800  1.000 33.97058 ? 18  HIS C CD2 1 
ATOM   2432 C CE1 . HIS C 1 19  ? -14.02000 27.53000 -2.79100  1.000 32.51761 ? 18  HIS C CE1 1 
ATOM   2433 N NE2 . HIS C 1 19  ? -13.65500 27.09300 -3.98200  1.000 28.51887 ? 18  HIS C NE2 1 
ATOM   2434 N N   . ALA C 1 20  ? -10.21600 31.55100 -4.88800  1.000 22.76529 ? 19  ALA C N   1 
ATOM   2435 C CA  . ALA C 1 20  ? -10.72900 32.59200 -5.77500  1.000 24.18538 ? 19  ALA C CA  1 
ATOM   2436 C C   . ALA C 1 20  ? -10.09300 32.49000 -7.15300  1.000 27.24859 ? 19  ALA C C   1 
ATOM   2437 O O   . ALA C 1 20  ? -10.75400 32.72000 -8.17000  1.000 29.46311 ? 19  ALA C O   1 
ATOM   2438 C CB  . ALA C 1 20  ? -10.49000 33.97900 -5.18700  1.000 19.74012 ? 19  ALA C CB  1 
ATOM   2439 N N   . VAL C 1 21  ? -8.81300  32.12400 -7.20500  1.000 21.66689 ? 20  VAL C N   1 
ATOM   2440 C CA  . VAL C 1 21  ? -8.11900  32.10200 -8.47600  1.000 24.09052 ? 20  VAL C CA  1 
ATOM   2441 C C   . VAL C 1 21  ? -8.57300  30.91200 -9.31000  1.000 30.29413 ? 20  VAL C C   1 
ATOM   2442 O O   . VAL C 1 21  ? -8.68700  31.01800 -10.54000 1.000 28.89626 ? 20  VAL C O   1 
ATOM   2443 C CB  . VAL C 1 21  ? -6.60100  32.12800 -8.23400  1.000 20.70903 ? 20  VAL C CB  1 
ATOM   2444 C CG1 . VAL C 1 21  ? -5.85400  31.94300 -9.51000  1.000 20.38053 ? 20  VAL C CG1 1 
ATOM   2445 C CG2 . VAL C 1 21  ? -6.23700  33.45300 -7.63800  1.000 21.84717 ? 20  VAL C CG2 1 
ATOM   2446 N N   . ALA C 1 22  ? -8.89100  29.78300 -8.66700  1.000 27.50396 ? 21  ALA C N   1 
ATOM   2447 C CA  . ALA C 1 22  ? -9.42500  28.64500 -9.41100  1.000 24.08319 ? 21  ALA C CA  1 
ATOM   2448 C C   . ALA C 1 22  ? -10.88000 28.87000 -9.82800  1.000 29.86164 ? 21  ALA C C   1 
ATOM   2449 O O   . ALA C 1 22  ? -11.26700 28.50500 -10.94700 1.000 30.53685 ? 21  ALA C O   1 
ATOM   2450 C CB  . ALA C 1 22  ? -9.29900  27.37400 -8.58700  1.000 20.19833 ? 21  ALA C CB  1 
ATOM   2451 N N   . LYS C 1 23  ? -11.69600 29.47000 -8.95000  1.000 28.88170 ? 22  LYS C N   1 
ATOM   2452 C CA  . LYS C 1 23  ? -13.06800 29.82100 -9.31900  1.000 27.19300 ? 22  LYS C CA  1 
ATOM   2453 C C   . LYS C 1 23  ? -13.10600 30.75200 -10.53100 1.000 30.75875 ? 22  LYS C C   1 
ATOM   2454 O O   . LYS C 1 23  ? -13.94600 30.58800 -11.42200 1.000 32.04598 ? 22  LYS C O   1 
ATOM   2455 C CB  . LYS C 1 23  ? -13.78800 30.47800 -8.13800  1.000 29.06876 ? 22  LYS C CB  1 
ATOM   2456 C CG  . LYS C 1 23  ? -15.17500 31.04900 -8.49800  1.000 41.18594 ? 22  LYS C CG  1 
ATOM   2457 C CD  . LYS C 1 23  ? -15.37300 32.51000 -8.02800  1.000 49.44887 ? 22  LYS C CD  1 
ATOM   2458 C CE  . LYS C 1 23  ? -16.44400 33.29600 -8.84900  1.000 57.22063 ? 22  LYS C CE  1 
ATOM   2459 N NZ  . LYS C 1 23  ? -15.98200 34.02800 -10.11400 1.000 38.15747 ? 22  LYS C NZ  1 
ATOM   2460 N N   . ALA C 1 24  ? -12.20800 31.74000 -10.58500 1.000 27.59031 ? 23  ALA C N   1 
ATOM   2461 C CA  . ALA C 1 24  ? -12.27500 32.71400 -11.67000 1.000 27.65067 ? 23  ALA C CA  1 
ATOM   2462 C C   . ALA C 1 24  ? -11.84600 32.09900 -12.99600 1.000 30.30336 ? 23  ALA C C   1 
ATOM   2463 O O   . ALA C 1 24  ? -12.50200 32.30200 -14.03000 1.000 29.55243 ? 23  ALA C O   1 
ATOM   2464 C CB  . ALA C 1 24  ? -11.42300 33.93400 -11.34300 1.000 19.10703 ? 23  ALA C CB  1 
ATOM   2465 N N   . ILE C 1 25  ? -10.74600 31.35000 -12.98800 1.000 27.94724 ? 24  ILE C N   1 
ATOM   2466 C CA  . ILE C 1 25  ? -10.31900 30.68100 -14.20600 1.000 32.26500 ? 24  ILE C CA  1 
ATOM   2467 C C   . ILE C 1 25  ? -11.41900 29.74900 -14.70400 1.000 32.82923 ? 24  ILE C C   1 
ATOM   2468 O O   . ILE C 1 25  ? -11.76800 29.74600 -15.89500 1.000 29.53209 ? 24  ILE C O   1 
ATOM   2469 C CB  . ILE C 1 25  ? -8.99700  29.93900 -13.95600 1.000 25.53697 ? 24  ILE C CB  1 
ATOM   2470 C CG1 . ILE C 1 25  ? -7.94000  30.93100 -13.49000 1.000 23.44712 ? 24  ILE C CG1 1 
ATOM   2471 C CG2 . ILE C 1 25  ? -8.54700  29.24100 -15.21300 1.000 25.77783 ? 24  ILE C CG2 1 
ATOM   2472 C CD1 . ILE C 1 25  ? -6.57900  30.31800 -13.34000 1.000 23.53316 ? 24  ILE C CD1 1 
ATOM   2473 N N   . THR C 1 26  ? -12.00900 28.97900 -13.78900 1.000 26.70556 ? 25  THR C N   1 
ATOM   2474 C CA  . THR C 1 26  ? -13.04800 28.03200 -14.15600 1.000 27.56557 ? 25  THR C CA  1 
ATOM   2475 C C   . THR C 1 26  ? -14.29300 28.74900 -14.66900 1.000 33.86773 ? 25  THR C C   1 
ATOM   2476 O O   . THR C 1 26  ? -14.91300 28.30300 -15.64300 1.000 36.49250 ? 25  THR C O   1 
ATOM   2477 C CB  . THR C 1 26  ? -13.36200 27.16200 -12.94200 1.000 32.32744 ? 25  THR C CB  1 
ATOM   2478 O OG1 . THR C 1 26  ? -12.13000 26.81900 -12.28100 1.000 24.59959 ? 25  THR C OG1 1 
ATOM   2479 C CG2 . THR C 1 26  ? -14.15500 25.88900 -13.32500 1.000 25.95060 ? 25  THR C CG2 1 
ATOM   2480 N N   . ASP C 1 27  ? -14.66800 29.86900 -14.04000 1.000 31.91488 ? 26  ASP C N   1 
ATOM   2481 C CA  . ASP C 1 27  ? -15.79600 30.64800 -14.55100 1.000 35.84561 ? 26  ASP C CA  1 
ATOM   2482 C C   . ASP C 1 27  ? -15.48500 31.21400 -15.92300 1.000 29.28707 ? 26  ASP C C   1 
ATOM   2483 O O   . ASP C 1 27  ? -16.35900 31.26900 -16.79400 1.000 30.59850 ? 26  ASP C O   1 
ATOM   2484 C CB  . ASP C 1 27  ? -16.14900 31.79800 -13.60500 1.000 32.82848 ? 26  ASP C CB  1 
ATOM   2485 C CG  . ASP C 1 27  ? -16.80200 31.32700 -12.33700 1.000 33.54646 ? 26  ASP C CG  1 
ATOM   2486 O OD1 . ASP C 1 27  ? -17.00600 30.10700 -12.19900 1.000 33.57547 ? 26  ASP C OD1 1 
ATOM   2487 O OD2 . ASP C 1 27  ? -17.10700 32.18500 -11.48200 1.000 40.54993 ? 26  ASP C OD2 1 
ATOM   2488 N N   . ALA C 1 28  ? -14.25600 31.67700 -16.11900 1.000 27.49801 ? 27  ALA C N   1 
ATOM   2489 C CA  . ALA C 1 28  ? -13.88000 32.22200 -17.41600 1.000 36.70837 ? 27  ALA C CA  1 
ATOM   2490 C C   . ALA C 1 28  ? -13.99800 31.15500 -18.49400 1.000 34.09164 ? 27  ALA C C   1 
ATOM   2491 O O   . ALA C 1 28  ? -14.62100 31.36800 -19.54200 1.000 30.13732 ? 27  ALA C O   1 
ATOM   2492 C CB  . ALA C 1 28  ? -12.46000 32.78000 -17.34600 1.000 29.56875 ? 27  ALA C CB  1 
ATOM   2493 N N   . HIS C 1 29  ? -13.44600 29.97600 -18.21900 1.000 32.88202 ? 28  HIS C N   1 
ATOM   2494 C CA  . HIS C 1 29  ? -13.43400 28.90000 -19.19000 1.000 26.28538 ? 28  HIS C CA  1 
ATOM   2495 C C   . HIS C 1 29  ? -14.81800 28.32700 -19.42700 1.000 34.62190 ? 28  HIS C C   1 
ATOM   2496 O O   . HIS C 1 29  ? -15.09300 27.84900 -20.53700 1.000 40.03771 ? 28  HIS C O   1 
ATOM   2497 C CB  . HIS C 1 29  ? -12.50300 27.79300 -18.72600 1.000 28.92775 ? 28  HIS C CB  1 
ATOM   2498 C CG  . HIS C 1 29  ? -12.20000 26.78900 -19.78600 1.000 26.79372 ? 28  HIS C CG  1 
ATOM   2499 N ND1 . HIS C 1 29  ? -11.00700 26.77800 -20.47400 1.000 26.87624 ? 28  HIS C ND1 1 
ATOM   2500 C CD2 . HIS C 1 29  ? -12.93900 25.77200 -20.28900 1.000 27.52298 ? 28  HIS C CD2 1 
ATOM   2501 C CE1 . HIS C 1 29  ? -11.02000 25.79400 -21.35200 1.000 28.15633 ? 28  HIS C CE1 1 
ATOM   2502 N NE2 . HIS C 1 29  ? -12.17900 25.16600 -21.26000 1.000 33.19042 ? 28  HIS C NE2 1 
ATOM   2503 N N   . ARG C 1 30  ? -15.69100 28.32000 -18.40600 1.000 29.45745 ? 29  ARG C N   1 
ATOM   2504 C CA  . ARG C 1 30  ? -17.05300 27.84900 -18.64700 1.000 33.38906 ? 29  ARG C CA  1 
ATOM   2505 C C   . ARG C 1 30  ? -17.86600 28.89100 -19.39200 1.000 33.84122 ? 29  ARG C C   1 
ATOM   2506 O O   . ARG C 1 30  ? -18.72300 28.53900 -20.20700 1.000 34.09974 ? 29  ARG C O   1 
ATOM   2507 C CB  . ARG C 1 30  ? -17.77800 27.49100 -17.35000 1.000 39.95259 ? 29  ARG C CB  1 
ATOM   2508 C CG  . ARG C 1 30  ? -19.21900 27.00400 -17.59400 1.000 44.20982 ? 29  ARG C CG  1 
ATOM   2509 C CD  . ARG C 1 30  ? -20.30000 27.98000 -17.10300 1.000 49.75296 ? 29  ARG C CD  1 
ATOM   2510 N NE  . ARG C 1 30  ? -21.43100 27.25900 -16.51600 1.000 58.79753 ? 29  ARG C NE  1 
ATOM   2511 C CZ  . ARG C 1 30  ? -22.42100 27.81300 -15.82400 1.000 58.18433 ? 29  ARG C CZ  1 
ATOM   2512 N NH1 . ARG C 1 30  ? -22.49000 29.12300 -15.63300 1.000 55.86353 ? 29  ARG C NH1 1 
ATOM   2513 N NH2 . ARG C 1 30  ? -23.35600 27.02900 -15.29400 1.000 62.33888 ? 29  ARG C NH2 1 
ATOM   2514 N N   . GLY C 1 31  ? -17.61000 30.17200 -19.13100 1.000 29.69740 ? 30  GLY C N   1 
ATOM   2515 C CA  . GLY C 1 31  ? -18.36000 31.20700 -19.81600 1.000 30.00359 ? 30  GLY C CA  1 
ATOM   2516 C C   . GLY C 1 31  ? -18.05800 31.24900 -21.30200 1.000 34.55819 ? 30  GLY C C   1 
ATOM   2517 O O   . GLY C 1 31  ? -18.96500 31.27000 -22.13600 1.000 32.83847 ? 30  GLY C O   1 
ATOM   2518 N N   . LEU C 1 32  ? -16.77700 31.22900 -21.65400 1.000 35.83825 ? 31  LEU C N   1 
ATOM   2519 C CA  . LEU C 1 32  ? -16.38800 31.47600 -23.03000 1.000 31.48919 ? 31  LEU C CA  1 
ATOM   2520 C C   . LEU C 1 32  ? -16.48300 30.24700 -23.92400 1.000 30.85824 ? 31  LEU C C   1 
ATOM   2521 O O   . LEU C 1 32  ? -16.56200 30.39800 -25.14700 1.000 35.57076 ? 31  LEU C O   1 
ATOM   2522 C CB  . LEU C 1 32  ? -14.97300 32.03600 -23.04600 1.000 33.78197 ? 31  LEU C CB  1 
ATOM   2523 C CG  . LEU C 1 32  ? -15.06200 33.50200 -22.62500 1.000 35.55168 ? 31  LEU C CG  1 
ATOM   2524 C CD1 . LEU C 1 32  ? -13.69200 34.10000 -22.35900 1.000 27.31323 ? 31  LEU C CD1 1 
ATOM   2525 C CD2 . LEU C 1 32  ? -15.82000 34.29100 -23.68300 1.000 40.03649 ? 31  LEU C CD2 1 
ATOM   2526 N N   . THR C 1 33  ? -16.49300 29.04400 -23.35700 1.000 37.71166 ? 32  THR C N   1 
ATOM   2527 C CA  . THR C 1 33  ? -16.44500 27.81500 -24.14000 1.000 30.78815 ? 32  THR C CA  1 
ATOM   2528 C C   . THR C 1 33  ? -17.65600 26.90600 -23.95300 1.000 34.30724 ? 32  THR C C   1 
ATOM   2529 O O   . THR C 1 33  ? -17.79500 25.92900 -24.69800 1.000 36.84106 ? 32  THR C O   1 
ATOM   2530 C CB  . THR C 1 33  ? -15.18200 27.02300 -23.78900 1.000 29.17956 ? 32  THR C CB  1 
ATOM   2531 O OG1 . THR C 1 33  ? -15.25900 26.61300 -22.41900 1.000 32.44865 ? 32  THR C OG1 1 
ATOM   2532 C CG2 . THR C 1 33  ? -13.95500 27.90500 -23.95900 1.000 29.93627 ? 32  THR C CG2 1 
ATOM   2533 N N   . GLY C 1 34  ? -18.52300 27.17600 -22.97800 1.000 36.65650 ? 33  GLY C N   1 
ATOM   2534 C CA  . GLY C 1 34  ? -19.70400 26.36900 -22.76100 1.000 36.99771 ? 33  GLY C CA  1 
ATOM   2535 C C   . GLY C 1 34  ? -19.47500 25.01200 -22.13400 1.000 36.91660 ? 33  GLY C C   1 
ATOM   2536 O O   . GLY C 1 34  ? -20.45700 24.34800 -21.78200 1.000 45.98625 ? 33  GLY C O   1 
ATOM   2537 N N   . ALA C 1 35  ? -18.22700 24.56300 -21.99600 1.000 34.70201 ? 34  ALA C N   1 
ATOM   2538 C CA  . ALA C 1 35  ? -17.95000 23.29700 -21.32300 1.000 34.49377 ? 34  ALA C CA  1 
ATOM   2539 C C   . ALA C 1 35  ? -18.44500 23.33500 -19.88300 1.000 39.39259 ? 34  ALA C C   1 
ATOM   2540 O O   . ALA C 1 35  ? -18.34700 24.36100 -19.20400 1.000 45.19518 ? 34  ALA C O   1 
ATOM   2541 C CB  . ALA C 1 35  ? -16.45200 23.00600 -21.34600 1.000 35.29843 ? 34  ALA C CB  1 
ATOM   2542 N N   . GLN C 1 36  ? -18.96700 22.20900 -19.40300 1.000 38.81773 ? 35  GLN C N   1 
ATOM   2543 C CA  . GLN C 1 36  ? -19.50800 22.19400 -18.04900 1.000 41.53510 ? 35  GLN C CA  1 
ATOM   2544 C C   . GLN C 1 36  ? -18.39300 22.41200 -17.03800 1.000 43.60787 ? 35  GLN C C   1 
ATOM   2545 O O   . GLN C 1 36  ? -17.24400 22.00800 -17.26000 1.000 38.85732 ? 35  GLN C O   1 
ATOM   2546 C CB  . GLN C 1 36  ? -20.21900 20.87900 -17.74500 1.000 38.97032 ? 35  GLN C CB  1 
ATOM   2547 C CG  . GLN C 1 36  ? -21.36500 20.56100 -18.67300 1.000 43.74895 ? 35  GLN C CG  1 
ATOM   2548 C CD  . GLN C 1 36  ? -20.94400 19.58000 -19.73600 1.000 41.42278 ? 35  GLN C CD  1 
ATOM   2549 O OE1 . GLN C 1 36  ? -19.76100 19.49400 -20.06300 1.000 42.28773 ? 35  GLN C OE1 1 
ATOM   2550 N NE2 . GLN C 1 36  ? -21.89800 18.81500 -20.26700 1.000 43.60573 ? 35  GLN C NE2 1 
ATOM   2551 N N   . HIS C 1 37  ? -18.75400 23.06100 -15.92200 1.000 37.45113 ? 36  HIS C N   1 
ATOM   2552 C CA  . HIS C 1 37  ? -17.78800 23.43300 -14.88900 1.000 38.01334 ? 36  HIS C CA  1 
ATOM   2553 C C   . HIS C 1 37  ? -16.85100 22.27600 -14.53100 1.000 37.63282 ? 36  HIS C C   1 
ATOM   2554 O O   . HIS C 1 37  ? -15.62800 22.37300 -14.69600 1.000 36.61468 ? 36  HIS C O   1 
ATOM   2555 C CB  . HIS C 1 37  ? -18.52800 23.90900 -13.64000 1.000 44.64609 ? 36  HIS C CB  1 
ATOM   2556 C CG  . HIS C 1 37  ? -19.00100 25.32800 -13.70500 1.000 49.71602 ? 36  HIS C CG  1 
ATOM   2557 N ND1 . HIS C 1 37  ? -18.20000 26.39700 -13.36100 1.000 45.80676 ? 36  HIS C ND1 1 
ATOM   2558 C CD2 . HIS C 1 37  ? -20.21000 25.85000 -14.02900 1.000 47.15638 ? 36  HIS C CD2 1 
ATOM   2559 C CE1 . HIS C 1 37  ? -18.89100 27.51700 -13.49000 1.000 48.46641 ? 36  HIS C CE1 1 
ATOM   2560 N NE2 . HIS C 1 37  ? -20.11500 27.21300 -13.88600 1.000 46.49453 ? 36  HIS C NE2 1 
ATOM   2561 N N   . PHE C 1 38  ? -17.41600 21.15900 -14.05700 1.000 37.91353 ? 37  PHE C N   1 
ATOM   2562 C CA  . PHE C 1 38  ? -16.62700 20.03500 -13.54300 1.000 39.96503 ? 37  PHE C CA  1 
ATOM   2563 C C   . PHE C 1 38  ? -15.57600 19.51600 -14.52800 1.000 39.49836 ? 37  PHE C C   1 
ATOM   2564 O O   . PHE C 1 38  ? -14.77400 18.64800 -14.15500 1.000 38.56355 ? 37  PHE C O   1 
ATOM   2565 C CB  . PHE C 1 38  ? -17.55000 18.88000 -13.12600 1.000 38.28387 ? 37  PHE C CB  1 
ATOM   2566 C CG  . PHE C 1 38  ? -18.63800 18.56100 -14.13400 1.000 42.45751 ? 37  PHE C CG  1 
ATOM   2567 C CD1 . PHE C 1 38  ? -18.37200 17.76900 -15.23900 1.000 43.53995 ? 37  PHE C CD1 1 
ATOM   2568 C CD2 . PHE C 1 38  ? -19.93200 19.06100 -13.97100 1.000 45.67563 ? 37  PHE C CD2 1 
ATOM   2569 C CE1 . PHE C 1 38  ? -19.38100 17.46700 -16.16300 1.000 50.26080 ? 37  PHE C CE1 1 
ATOM   2570 C CE2 . PHE C 1 38  ? -20.94200 18.77200 -14.89000 1.000 43.18730 ? 37  PHE C CE2 1 
ATOM   2571 C CZ  . PHE C 1 38  ? -20.66600 17.97400 -15.98600 1.000 45.27745 ? 37  PHE C CZ  1 
ATOM   2572 N N   . LEU C 1 39  ? -15.54900 20.01000 -15.76500 1.000 39.18789 ? 38  LEU C N   1 
ATOM   2573 C CA  . LEU C 1 39  ? -14.52200 19.59400 -16.71100 1.000 38.49103 ? 38  LEU C CA  1 
ATOM   2574 C C   . LEU C 1 39  ? -13.22200 20.36300 -16.54600 1.000 37.47537 ? 38  LEU C C   1 
ATOM   2575 O O   . LEU C 1 39  ? -12.21700 19.96800 -17.14200 1.000 35.84679 ? 38  LEU C O   1 
ATOM   2576 C CB  . LEU C 1 39  ? -15.02600 19.76400 -18.14700 1.000 37.43150 ? 38  LEU C CB  1 
ATOM   2577 C CG  . LEU C 1 39  ? -15.75300 18.55600 -18.74100 1.000 38.77621 ? 38  LEU C CG  1 
ATOM   2578 C CD1 . LEU C 1 39  ? -15.65600 18.54900 -20.26300 1.000 41.28701 ? 38  LEU C CD1 1 
ATOM   2579 C CD2 . LEU C 1 39  ? -15.22700 17.25200 -18.15000 1.000 35.08790 ? 38  LEU C CD2 1 
ATOM   2580 N N   . ALA C 1 40  ? -13.21800 21.44400 -15.76000 1.000 33.97975 ? 39  ALA C N   1 
ATOM   2581 C CA  . ALA C 1 40  ? -12.07400 22.33800 -15.65600 1.000 27.83477 ? 39  ALA C CA  1 
ATOM   2582 C C   . ALA C 1 40  ? -11.29100 22.04500 -14.37800 1.000 30.12063 ? 39  ALA C C   1 
ATOM   2583 O O   . ALA C 1 40  ? -11.83000 22.15700 -13.26800 1.000 33.38122 ? 39  ALA C O   1 
ATOM   2584 C CB  . ALA C 1 40  ? -12.53900 23.79200 -15.69500 1.000 24.16811 ? 39  ALA C CB  1 
ATOM   2585 N N   . GLN C 1 41  ? -10.02600 21.66500 -14.53600 1.000 26.09051 ? 40  GLN C N   1 
ATOM   2586 C CA  . GLN C 1 41  ? -9.11600  21.46000 -13.41700 1.000 21.23543 ? 40  GLN C CA  1 
ATOM   2587 C C   . GLN C 1 41  ? -8.18100  22.65600 -13.26200 1.000 23.61540 ? 40  GLN C C   1 
ATOM   2588 O O   . GLN C 1 41  ? -7.59700  23.12600 -14.23500 1.000 25.80348 ? 40  GLN C O   1 
ATOM   2589 C CB  . GLN C 1 41  ? -8.30200  20.18800 -13.62000 1.000 20.75342 ? 40  GLN C CB  1 
ATOM   2590 C CG  . GLN C 1 41  ? -6.99500  20.17000 -12.84700 1.000 26.51755 ? 40  GLN C CG  1 
ATOM   2591 C CD  . GLN C 1 41  ? -6.39100  18.77000 -12.65200 1.000 26.58954 ? 40  GLN C CD  1 
ATOM   2592 O OE1 . GLN C 1 41  ? -5.42200  18.62400 -11.91600 1.000 30.24978 ? 40  GLN C OE1 1 
ATOM   2593 N NE2 . GLN C 1 41  ? -6.96700  17.74800 -13.29400 1.000 20.03059 ? 40  GLN C NE2 1 
ATOM   2594 N N   . VAL C 1 42  ? -8.02900  23.14400 -12.04100 1.000 29.81721 ? 41  VAL C N   1 
ATOM   2595 C CA  . VAL C 1 42  ? -6.98600  24.11000 -11.72800 1.000 23.66466 ? 41  VAL C CA  1 
ATOM   2596 C C   . VAL C 1 42  ? -5.99200  23.42900 -10.80100 1.000 23.38884 ? 41  VAL C C   1 
ATOM   2597 O O   . VAL C 1 42  ? -6.34100  23.05400 -9.67800  1.000 30.45313 ? 41  VAL C O   1 
ATOM   2598 C CB  . VAL C 1 42  ? -7.55100  25.39000 -11.10200 1.000 23.04954 ? 41  VAL C CB  1 
ATOM   2599 C CG1 . VAL C 1 42  ? -6.42800  26.20400 -10.46800 1.000 18.62120 ? 41  VAL C CG1 1 
ATOM   2600 C CG2 . VAL C 1 42  ? -8.24300  26.20800 -12.17200 1.000 25.38255 ? 41  VAL C CG2 1 
ATOM   2601 N N   . ASN C 1 43  ? -4.76000  23.27100 -11.27300 1.000 21.93899 ? 42  ASN C N   1 
ATOM   2602 C CA  . ASN C 1 43  ? -3.69200  22.60000 -10.55100 1.000 19.31048 ? 42  ASN C CA  1 
ATOM   2603 C C   . ASN C 1 43  ? -2.64200  23.62700 -10.14900 1.000 20.57536 ? 42  ASN C C   1 
ATOM   2604 O O   . ASN C 1 43  ? -1.83400  24.05900 -10.97800 1.000 25.85520 ? 42  ASN C O   1 
ATOM   2605 C CB  . ASN C 1 43  ? -3.09800  21.50200 -11.41200 1.000 21.60605 ? 42  ASN C CB  1 
ATOM   2606 C CG  . ASN C 1 43  ? -2.32700  20.48400 -10.60300 1.000 29.44016 ? 42  ASN C CG  1 
ATOM   2607 O OD1 . ASN C 1 43  ? -1.38300  20.82400 -9.88800  1.000 28.23548 ? 42  ASN C OD1 1 
ATOM   2608 N ND2 . ASN C 1 43  ? -2.72800  19.22100 -10.70600 1.000 28.27314 ? 42  ASN C ND2 1 
ATOM   2609 N N   . PHE C 1 44  ? -2.64600  24.00600 -8.87200  1.000 21.40841 ? 43  PHE C N   1 
ATOM   2610 C CA  . PHE C 1 44  ? -1.69400  24.98000 -8.34300  1.000 22.56962 ? 43  PHE C CA  1 
ATOM   2611 C C   . PHE C 1 44  ? -0.34000  24.33800 -8.06100  1.000 26.92784 ? 43  PHE C C   1 
ATOM   2612 O O   . PHE C 1 44  ? -0.25400  23.33000 -7.35100  1.000 28.12747 ? 43  PHE C O   1 
ATOM   2613 C CB  . PHE C 1 44  ? -2.22500  25.59700 -7.05700  1.000 22.09013 ? 43  PHE C CB  1 
ATOM   2614 C CG  . PHE C 1 44  ? -3.17300  26.72200 -7.28200  1.000 23.19739 ? 43  PHE C CG  1 
ATOM   2615 C CD1 . PHE C 1 44  ? -2.70700  27.95800 -7.72800  1.000 17.73987 ? 43  PHE C CD1 1 
ATOM   2616 C CD2 . PHE C 1 44  ? -4.53200  26.55500 -7.04700  1.000 18.86011 ? 43  PHE C CD2 1 
ATOM   2617 C CE1 . PHE C 1 44  ? -3.58000  29.00100 -7.93000  1.000 22.82005 ? 43  PHE C CE1 1 
ATOM   2618 C CE2 . PHE C 1 44  ? -5.41700  27.59600 -7.26200  1.000 17.00106 ? 43  PHE C CE2 1 
ATOM   2619 C CZ  . PHE C 1 44  ? -4.94800  28.82500 -7.69800  1.000 18.69875 ? 43  PHE C CZ  1 
ATOM   2620 N N   . GLN C 1 45  ? 0.72200   24.93500 -8.59600  1.000 27.28299 ? 44  GLN C N   1 
ATOM   2621 C CA  . GLN C 1 45  ? 2.08400   24.46000 -8.37600  1.000 26.21999 ? 44  GLN C CA  1 
ATOM   2622 C C   . GLN C 1 45  ? 2.86500   25.54400 -7.64800  1.000 27.97322 ? 44  GLN C C   1 
ATOM   2623 O O   . GLN C 1 45  ? 3.08300   26.63500 -8.18900  1.000 26.34682 ? 44  GLN C O   1 
ATOM   2624 C CB  . GLN C 1 45  ? 2.75300   24.07700 -9.69400  1.000 22.94809 ? 44  GLN C CB  1 
ATOM   2625 C CG  . GLN C 1 45  ? 2.07300   22.88700 -10.35400 1.000 20.81075 ? 44  GLN C CG  1 
ATOM   2626 C CD  . GLN C 1 45  ? 2.30200   21.60000 -9.60400  1.000 19.14033 ? 44  GLN C CD  1 
ATOM   2627 O OE1 . GLN C 1 45  ? 3.42600   21.30100 -9.18800  1.000 21.12936 ? 44  GLN C OE1 1 
ATOM   2628 N NE2 . GLN C 1 45  ? 1.24500   20.81500 -9.43700  1.000 19.98239 ? 44  GLN C NE2 1 
ATOM   2629 N N   . GLU C 1 46  ? 3.26700   25.24400 -6.42000  1.000 26.93513 ? 45  GLU C N   1 
ATOM   2630 C CA  . GLU C 1 46  ? 3.84000   26.22200 -5.51000  1.000 27.14389 ? 45  GLU C CA  1 
ATOM   2631 C C   . GLU C 1 46  ? 5.33200   25.95800 -5.36100  1.000 23.82627 ? 45  GLU C C   1 
ATOM   2632 O O   . GLU C 1 46  ? 5.72600   24.87400 -4.93400  1.000 28.57940 ? 45  GLU C O   1 
ATOM   2633 C CB  . GLU C 1 46  ? 3.16200   26.13500 -4.14700  1.000 27.19033 ? 45  GLU C CB  1 
ATOM   2634 C CG  . GLU C 1 46  ? 1.69300   26.32700 -4.17900  1.000 30.28660 ? 45  GLU C CG  1 
ATOM   2635 C CD  . GLU C 1 46  ? 1.15100   26.73500 -2.82200  1.000 31.99762 ? 45  GLU C CD  1 
ATOM   2636 O OE1 . GLU C 1 46  ? 1.30800   27.92200 -2.45600  1.000 32.22311 ? 45  GLU C OE1 1 
ATOM   2637 O OE2 . GLU C 1 46  ? 0.56200   25.87800 -2.13600  1.000 30.14790 ? 45  GLU C OE2 1 
ATOM   2638 N N   . GLN C 1 47  ? 6.15200   26.94000 -5.67200  1.000 18.71420 ? 46  GLN C N   1 
ATOM   2639 C CA  . GLN C 1 47  ? 7.57800   26.80500 -5.45000  1.000 23.93030 ? 46  GLN C CA  1 
ATOM   2640 C C   . GLN C 1 47  ? 8.05500   27.90900 -4.51900  1.000 25.03699 ? 46  GLN C C   1 
ATOM   2641 O O   . GLN C 1 47  ? 7.42100   28.96500 -4.42100  1.000 26.14704 ? 46  GLN C O   1 
ATOM   2642 C CB  . GLN C 1 47  ? 8.35500   26.85900 -6.77400  1.000 26.04834 ? 46  GLN C CB  1 
ATOM   2643 C CG  . GLN C 1 47  ? 8.15600   25.62900 -7.66200  1.000 21.29288 ? 46  GLN C CG  1 
ATOM   2644 C CD  . GLN C 1 47  ? 8.68600   24.36100 -7.02600  1.000 23.80945 ? 46  GLN C CD  1 
ATOM   2645 O OE1 . GLN C 1 47  ? 9.67900   24.38800 -6.30900  1.000 23.51585 ? 46  GLN C OE1 1 
ATOM   2646 N NE2 . GLN C 1 47  ? 8.02000   23.23900 -7.28500  1.000 26.15375 ? 46  GLN C NE2 1 
ATOM   2647 N N   . PRO C 1 48  ? 9.16000   27.69500 -3.80200  1.000 30.37647 ? 47  PRO C N   1 
ATOM   2648 C CA  . PRO C 1 48  ? 9.74200   28.79400 -3.02000  1.000 26.85844 ? 47  PRO C CA  1 
ATOM   2649 C C   . PRO C 1 48  ? 10.01800  29.98300 -3.91100  1.000 25.28706 ? 47  PRO C C   1 
ATOM   2650 O O   . PRO C 1 48  ? 10.51300  29.83300 -5.02800  1.000 25.58363 ? 47  PRO C O   1 
ATOM   2651 C CB  . PRO C 1 48  ? 11.04800  28.20300 -2.48300  1.000 22.48366 ? 47  PRO C CB  1 
ATOM   2652 C CG  . PRO C 1 48  ? 11.35600  27.06800 -3.38100  1.000 25.24769 ? 47  PRO C CG  1 
ATOM   2653 C CD  . PRO C 1 48  ? 10.00000  26.48700 -3.74000  1.000 23.96506 ? 47  PRO C CD  1 
ATOM   2654 N N   . ALA C 1 49  ? 9.68500   31.16900 -3.40800  1.000 28.78746 ? 48  ALA C N   1 
ATOM   2655 C CA  . ALA C 1 49  ? 10.03200  32.39600 -4.10700  1.000 26.77064 ? 48  ALA C CA  1 
ATOM   2656 C C   . ALA C 1 49  ? 11.52500  32.41700 -4.42800  1.000 26.29999 ? 48  ALA C C   1 
ATOM   2657 O O   . ALA C 1 49  ? 12.33500  31.80100 -3.73600  1.000 23.29080 ? 48  ALA C O   1 
ATOM   2658 C CB  . ALA C 1 49  ? 9.64400   33.60300 -3.26200  1.000 24.74841 ? 48  ALA C CB  1 
ATOM   2659 N N   . GLY C 1 50  ? 11.89000  33.12200 -5.49900  1.000 26.89803 ? 49  GLY C N   1 
ATOM   2660 C CA  . GLY C 1 50  ? 13.23700  33.07600 -6.01000  1.000 27.50402 ? 49  GLY C CA  1 
ATOM   2661 C C   . GLY C 1 50  ? 13.47800  31.97600 -7.02000  1.000 33.44736 ? 49  GLY C C   1 
ATOM   2662 O O   . GLY C 1 50  ? 14.57300  31.91300 -7.60800  1.000 28.89207 ? 49  GLY C O   1 
ATOM   2663 N N   . ASN C 1 51  ? 12.49800  31.10000 -7.22800  1.000 27.23387 ? 50  ASN C N   1 
ATOM   2664 C CA  . ASN C 1 51  ? 12.58800  30.07800 -8.25500  1.000 24.84137 ? 50  ASN C CA  1 
ATOM   2665 C C   . ASN C 1 51  ? 12.20500  30.60200 -9.62200  1.000 27.92164 ? 50  ASN C C   1 
ATOM   2666 O O   . ASN C 1 51  ? 12.37300  29.88000 -10.61600 1.000 26.85536 ? 50  ASN C O   1 
ATOM   2667 C CB  . ASN C 1 51  ? 11.68900  28.89100 -7.90500  1.000 31.45145 ? 50  ASN C CB  1 
ATOM   2668 C CG  . ASN C 1 51  ? 12.45400  27.76600 -7.24100  1.000 30.74573 ? 50  ASN C CG  1 
ATOM   2669 O OD1 . ASN C 1 51  ? 13.57900  27.96200 -6.77000  1.000 25.29505 ? 50  ASN C OD1 1 
ATOM   2670 N ND2 . ASN C 1 51  ? 11.84800  26.58000 -7.19800  1.000 27.81993 ? 50  ASN C ND2 1 
ATOM   2671 N N   . VAL C 1 52  ? 11.70400  31.83000 -9.70000  1.000 24.22090 ? 51  VAL C N   1 
ATOM   2672 C CA  . VAL C 1 52  ? 11.24000  32.40300 -10.95300 1.000 27.17148 ? 51  VAL C CA  1 
ATOM   2673 C C   . VAL C 1 52  ? 12.22000  33.48300 -11.33900 1.000 23.64088 ? 51  VAL C C   1 
ATOM   2674 O O   . VAL C 1 52  ? 12.58000  34.31500 -10.50400 1.000 29.61427 ? 51  VAL C O   1 
ATOM   2675 C CB  . VAL C 1 52  ? 9.81600   32.97700 -10.84500 1.000 26.04114 ? 51  VAL C CB  1 
ATOM   2676 C CG1 . VAL C 1 52  ? 9.45500   33.67000 -12.13200 1.000 28.40997 ? 51  VAL C CG1 1 
ATOM   2677 C CG2 . VAL C 1 52  ? 8.80800   31.88700 -10.55300 1.000 21.92500 ? 51  VAL C CG2 1 
ATOM   2678 N N   . PHE C 1 53  ? 12.65900  33.46300 -12.59300 1.000 23.56148 ? 52  PHE C N   1 
ATOM   2679 C CA  . PHE C 1 53  ? 13.61900  34.42700 -13.11400 1.000 24.92067 ? 52  PHE C CA  1 
ATOM   2680 C C   . PHE C 1 53  ? 13.03500  35.04700 -14.36500 1.000 26.20809 ? 52  PHE C C   1 
ATOM   2681 O O   . PHE C 1 53  ? 12.58700  34.33800 -15.27300 1.000 23.77236 ? 52  PHE C O   1 
ATOM   2682 C CB  . PHE C 1 53  ? 14.97600  33.79200 -13.46700 1.000 22.71066 ? 52  PHE C CB  1 
ATOM   2683 C CG  . PHE C 1 53  ? 15.84200  33.44000 -12.27900 1.000 23.97202 ? 52  PHE C CG  1 
ATOM   2684 C CD1 . PHE C 1 53  ? 15.67400  32.24300 -11.60800 1.000 21.84469 ? 52  PHE C CD1 1 
ATOM   2685 C CD2 . PHE C 1 53  ? 16.86800  34.27600 -11.88300 1.000 29.45027 ? 52  PHE C CD2 1 
ATOM   2686 C CE1 . PHE C 1 53  ? 16.47800  31.90100 -10.54000 1.000 25.72241 ? 52  PHE C CE1 1 
ATOM   2687 C CE2 . PHE C 1 53  ? 17.68400  33.94400 -10.82000 1.000 27.55983 ? 52  PHE C CE2 1 
ATOM   2688 C CZ  . PHE C 1 53  ? 17.48700  32.75000 -10.14200 1.000 28.18907 ? 52  PHE C CZ  1 
ATOM   2689 N N   . LEU C 1 54  ? 13.02700  36.36400 -14.40600 1.000 28.73931 ? 53  LEU C N   1 
ATOM   2690 C CA  . LEU C 1 54  ? 12.75200  37.09800 -15.62400 1.000 30.73690 ? 53  LEU C CA  1 
ATOM   2691 C C   . LEU C 1 54  ? 14.05900  37.73200 -16.05500 1.000 26.93179 ? 53  LEU C C   1 
ATOM   2692 O O   . LEU C 1 54  ? 14.86900  38.10500 -15.20700 1.000 29.84670 ? 53  LEU C O   1 
ATOM   2693 C CB  . LEU C 1 54  ? 11.64500  38.14000 -15.40900 1.000 34.81509 ? 53  LEU C CB  1 
ATOM   2694 C CG  . LEU C 1 54  ? 10.44000  37.67400 -14.57500 1.000 29.20048 ? 53  LEU C CG  1 
ATOM   2695 C CD1 . LEU C 1 54  ? 9.30800   38.68800 -14.59700 1.000 32.32903 ? 53  LEU C CD1 1 
ATOM   2696 C CD2 . LEU C 1 54  ? 9.92200   36.32500 -15.04200 1.000 25.22302 ? 53  LEU C CD2 1 
ATOM   2697 N N   . GLY C 1 55  ? 14.30100  37.76100 -17.36200 1.000 28.81640 ? 54  GLY C N   1 
ATOM   2698 C CA  . GLY C 1 55  ? 15.55200  38.26300 -17.90400 1.000 31.18181 ? 54  GLY C CA  1 
ATOM   2699 C C   . GLY C 1 55  ? 16.80900  37.87100 -17.14800 1.000 33.23578 ? 54  GLY C C   1 
ATOM   2700 O O   . GLY C 1 55  ? 17.81300  38.58600 -17.19300 1.000 34.69014 ? 54  GLY C O   1 
ATOM   2701 N N   . GLY C 1 56  ? 16.76600  36.73500 -16.44900 1.000 34.65938 ? 55  GLY C N   1 
ATOM   2702 C CA  . GLY C 1 56  ? 17.87200  36.29700 -15.62600 1.000 30.42217 ? 55  GLY C CA  1 
ATOM   2703 C C   . GLY C 1 56  ? 17.95400  36.94000 -14.25800 1.000 35.57372 ? 55  GLY C C   1 
ATOM   2704 O O   . GLY C 1 56  ? 18.97300  36.77800 -13.57200 1.000 31.18712 ? 55  GLY C O   1 
ATOM   2705 N N   . VAL C 1 57  ? 16.91700  37.65300 -13.82300 1.000 32.06125 ? 56  VAL C N   1 
ATOM   2706 C CA  . VAL C 1 57  ? 16.90700  38.30000 -12.51700 1.000 29.55642 ? 56  VAL C CA  1 
ATOM   2707 C C   . VAL C 1 57  ? 15.96800  37.53700 -11.59300 1.000 29.03802 ? 56  VAL C C   1 
ATOM   2708 O O   . VAL C 1 57  ? 14.79500  37.32600 -11.92600 1.000 25.60966 ? 56  VAL C O   1 
ATOM   2709 C CB  . VAL C 1 57  ? 16.48800  39.77300 -12.62500 1.000 31.11963 ? 56  VAL C CB  1 
ATOM   2710 C CG1 . VAL C 1 57  ? 16.65600  40.43200 -11.28700 1.000 27.52529 ? 56  VAL C CG1 1 
ATOM   2711 C CG2 . VAL C 1 57  ? 17.30500  40.48200 -13.70400 1.000 31.81299 ? 56  VAL C CG2 1 
ATOM   2712 N N   . GLN C 1 58  ? 16.48200  37.13000 -10.42900 1.000 32.55679 ? 57  GLN C N   1 
ATOM   2713 C CA  . GLN C 1 58  ? 15.64300  36.47200 -9.43600  1.000 26.06333 ? 57  GLN C CA  1 
ATOM   2714 C C   . GLN C 1 58  ? 14.46500  37.35400 -9.06000  1.000 34.55278 ? 57  GLN C C   1 
ATOM   2715 O O   . GLN C 1 58  ? 14.61100  38.56400 -8.84600  1.000 36.20521 ? 57  GLN C O   1 
ATOM   2716 C CB  . GLN C 1 58  ? 16.43000  36.13700 -8.18300  1.000 23.75953 ? 57  GLN C CB  1 
ATOM   2717 C CG  . GLN C 1 58  ? 16.10000  34.76500 -7.66800  1.000 28.49056 ? 57  GLN C CG  1 
ATOM   2718 C CD  . GLN C 1 58  ? 16.61300  34.52900 -6.28100  1.000 31.87950 ? 57  GLN C CD  1 
ATOM   2719 O OE1 . GLN C 1 58  ? 16.50100  35.39800 -5.42600  1.000 26.08851 ? 57  GLN C OE1 1 
ATOM   2720 N NE2 . GLN C 1 58  ? 17.15900  33.33400 -6.03500  1.000 32.67241 ? 57  GLN C NE2 1 
ATOM   2721 N N   . GLN C 1 59  ? 13.29300  36.73900 -8.98900  1.000 27.56249 ? 58  GLN C N   1 
ATOM   2722 C CA  . GLN C 1 59  ? 12.05700  37.44100 -8.71400  1.000 32.34370 ? 58  GLN C CA  1 
ATOM   2723 C C   . GLN C 1 59  ? 11.62500  37.17500 -7.28400  1.000 32.87579 ? 58  GLN C C   1 
ATOM   2724 O O   . GLN C 1 59  ? 12.09200  36.23500 -6.63100  1.000 34.41051 ? 58  GLN C O   1 
ATOM   2725 C CB  . GLN C 1 59  ? 10.94700  37.00800 -9.67600  1.000 32.41635 ? 58  GLN C CB  1 
ATOM   2726 C CG  . GLN C 1 59  ? 11.21400  37.38200 -11.12500 1.000 32.87527 ? 58  GLN C CG  1 
ATOM   2727 C CD  . GLN C 1 59  ? 11.08600  38.87100 -11.37500 1.000 35.88354 ? 58  GLN C CD  1 
ATOM   2728 O OE1 . GLN C 1 59  ? 9.98800   39.43600 -11.31600 1.000 41.05457 ? 58  GLN C OE1 1 
ATOM   2729 N NE2 . GLN C 1 59  ? 12.20400  39.51400 -11.66900 1.000 32.91114 ? 58  GLN C NE2 1 
ATOM   2730 N N   . GLY C 1 60  ? 10.74200  38.04300 -6.80600  1.000 28.00091 ? 59  GLY C N   1 
ATOM   2731 C CA  . GLY C 1 60  ? 10.01300  37.81200 -5.58400  1.000 27.88400 ? 59  GLY C CA  1 
ATOM   2732 C C   . GLY C 1 60  ? 8.84400   36.89600 -5.84700  1.000 33.30941 ? 59  GLY C C   1 
ATOM   2733 O O   . GLY C 1 60  ? 8.67800   36.32600 -6.92800  1.000 42.68769 ? 59  GLY C O   1 
ATOM   2734 N N   . GLY C 1 61  ? 8.01000   36.76100 -4.83500  1.000 30.27261 ? 60  GLY C N   1 
ATOM   2735 C CA  . GLY C 1 61  ? 6.94100   35.79400 -4.92400  1.000 31.01090 ? 60  GLY C CA  1 
ATOM   2736 C C   . GLY C 1 61  ? 5.71700   36.21700 -5.71000  1.000 32.84280 ? 60  GLY C C   1 
ATOM   2737 O O   . GLY C 1 61  ? 4.65200   35.61600 -5.54300  1.000 33.93257 ? 60  GLY C O   1 
ATOM   2738 N N   . ASP C 1 62  ? 5.84100   37.22100 -6.58200  1.000 28.87149 ? 61  ASP C N   1 
ATOM   2739 C CA  . ASP C 1 62  ? 4.65600   37.84500 -7.16000  1.000 29.44827 ? 61  ASP C CA  1 
ATOM   2740 C C   . ASP C 1 62  ? 4.29200   37.35200 -8.55200  1.000 28.71983 ? 61  ASP C C   1 
ATOM   2741 O O   . ASP C 1 62  ? 3.24200   37.75400 -9.06000  1.000 32.56279 ? 61  ASP C O   1 
ATOM   2742 C CB  . ASP C 1 62  ? 4.82000   39.36700 -7.22200  1.000 37.16262 ? 61  ASP C CB  1 
ATOM   2743 C CG  . ASP C 1 62  ? 4.31100   40.05100 -5.97200  1.000 45.17000 ? 61  ASP C CG  1 
ATOM   2744 O OD1 . ASP C 1 62  ? 3.57000   39.38400 -5.21500  1.000 35.23658 ? 61  ASP C OD1 1 
ATOM   2745 O OD2 . ASP C 1 62  ? 4.62600   41.24700 -5.76600  1.000 47.32914 ? 61  ASP C OD2 1 
ATOM   2746 N N   . THR C 1 63  ? 5.11200   36.51000 -9.18500  1.000 26.09044 ? 62  THR C N   1 
ATOM   2747 C CA  . THR C 1 63  ? 4.83000   36.07800 -10.54900 1.000 24.60070 ? 62  THR C CA  1 
ATOM   2748 C C   . THR C 1 63  ? 3.79500   34.95800 -10.55400 1.000 26.80810 ? 62  THR C C   1 
ATOM   2749 O O   . THR C 1 63  ? 3.79700   34.09500 -9.67700  1.000 28.33531 ? 62  THR C O   1 
ATOM   2750 C CB  . THR C 1 63  ? 6.10000   35.59500 -11.24300 1.000 28.65743 ? 62  THR C CB  1 
ATOM   2751 O OG1 . THR C 1 63  ? 7.20300   36.41100 -10.83800 1.000 33.67867 ? 62  THR C OG1 1 
ATOM   2752 C CG2 . THR C 1 63  ? 5.94500   35.67100 -12.75900 1.000 30.65036 ? 62  THR C CG2 1 
ATOM   2753 N N   . ILE C 1 64  ? 2.90000   34.99000 -11.54300 1.000 25.31234 ? 63  ILE C N   1 
ATOM   2754 C CA  . ILE C 1 64  ? 1.88300   33.96400 -11.75300 1.000 26.61673 ? 63  ILE C CA  1 
ATOM   2755 C C   . ILE C 1 64  ? 1.94900   33.51500 -13.20500 1.000 26.12011 ? 63  ILE C C   1 
ATOM   2756 O O   . ILE C 1 64  ? 1.67600   34.31100 -14.11100 1.000 28.73793 ? 63  ILE C O   1 
ATOM   2757 C CB  . ILE C 1 64  ? 0.46000   34.46700 -11.45700 1.000 28.70012 ? 63  ILE C CB  1 
ATOM   2758 C CG1 . ILE C 1 64  ? 0.27700   34.86400 -10.00400 1.000 27.32358 ? 63  ILE C CG1 1 
ATOM   2759 C CG2 . ILE C 1 64  ? -0.58900  33.41800 -11.89400 1.000 23.40663 ? 63  ILE C CG2 1 
ATOM   2760 C CD1 . ILE C 1 64  ? -0.98800  35.62400 -9.83000  1.000 25.94776 ? 63  ILE C CD1 1 
ATOM   2761 N N   . PHE C 1 65  ? 2.26100   32.24300 -13.42800 1.000 23.81645 ? 64  PHE C N   1 
ATOM   2762 C CA  . PHE C 1 65  ? 2.24200   31.66400 -14.76600 1.000 28.53284 ? 64  PHE C CA  1 
ATOM   2763 C C   . PHE C 1 65  ? 1.09500   30.66600 -14.83300 1.000 27.34506 ? 64  PHE C C   1 
ATOM   2764 O O   . PHE C 1 65  ? 1.09500   29.67400 -14.09100 1.000 28.75810 ? 64  PHE C O   1 
ATOM   2765 C CB  . PHE C 1 65  ? 3.57500   30.98700 -15.11400 1.000 23.00066 ? 64  PHE C CB  1 
ATOM   2766 C CG  . PHE C 1 65  ? 3.56500   30.27700 -16.44200 1.000 17.75571 ? 64  PHE C CG  1 
ATOM   2767 C CD1 . PHE C 1 65  ? 3.06900   30.89900 -17.57500 1.000 21.33834 ? 64  PHE C CD1 1 
ATOM   2768 C CD2 . PHE C 1 65  ? 4.05100   28.99200 -16.56300 1.000 19.49081 ? 64  PHE C CD2 1 
ATOM   2769 C CE1 . PHE C 1 65  ? 3.06500   30.24900 -18.82300 1.000 19.13471 ? 64  PHE C CE1 1 
ATOM   2770 C CE2 . PHE C 1 65  ? 4.04900   28.33500 -17.80000 1.000 21.75994 ? 64  PHE C CE2 1 
ATOM   2771 C CZ  . PHE C 1 65  ? 3.54700   28.97100 -18.93100 1.000 19.30492 ? 64  PHE C CZ  1 
ATOM   2772 N N   . VAL C 1 66  ? 0.11400   30.95500 -15.69100 1.000 24.85976 ? 65  VAL C N   1 
ATOM   2773 C CA  . VAL C 1 66  ? -0.99200  30.05400 -16.00300 1.000 22.50260 ? 65  VAL C CA  1 
ATOM   2774 C C   . VAL C 1 66  ? -0.68000  29.30800 -17.29300 1.000 23.60923 ? 65  VAL C C   1 
ATOM   2775 O O   . VAL C 1 66  ? -0.52200  29.92700 -18.35400 1.000 23.14064 ? 65  VAL C O   1 
ATOM   2776 C CB  . VAL C 1 66  ? -2.30900  30.81700 -16.17400 1.000 24.01499 ? 65  VAL C CB  1 
ATOM   2777 C CG1 . VAL C 1 66  ? -3.41300  29.83800 -16.52500 1.000 19.12532 ? 65  VAL C CG1 1 
ATOM   2778 C CG2 . VAL C 1 66  ? -2.61600  31.63800 -14.94700 1.000 21.98469 ? 65  VAL C CG2 1 
ATOM   2779 N N   . HIS C 1 67  ? -0.64600  27.98000 -17.22300 1.000 23.11366 ? 66  HIS C N   1 
ATOM   2780 C CA  . HIS C 1 67  ? -0.45300  27.14000 -18.39800 1.000 18.81397 ? 66  HIS C CA  1 
ATOM   2781 C C   . HIS C 1 67  ? -1.72900  26.33900 -18.63700 1.000 21.66325 ? 66  HIS C C   1 
ATOM   2782 O O   . HIS C 1 67  ? -2.00000  25.35500 -17.94300 1.000 25.44265 ? 66  HIS C O   1 
ATOM   2783 C CB  . HIS C 1 67  ? 0.75000   26.22100 -18.21900 1.000 25.23770 ? 66  HIS C CB  1 
ATOM   2784 C CG  . HIS C 1 67  ? 1.19300   25.56500 -19.48800 1.000 20.99813 ? 66  HIS C CG  1 
ATOM   2785 N ND1 . HIS C 1 67  ? 2.31000   24.76400 -19.56300 1.000 21.05316 ? 66  HIS C ND1 1 
ATOM   2786 C CD2 . HIS C 1 67  ? 0.65900   25.58500 -20.73000 1.000 21.51445 ? 66  HIS C CD2 1 
ATOM   2787 C CE1 . HIS C 1 67  ? 2.45400   24.33200 -20.80300 1.000 24.17675 ? 66  HIS C CE1 1 
ATOM   2788 N NE2 . HIS C 1 67  ? 1.46600   24.81700 -21.53200 1.000 24.78010 ? 66  HIS C NE2 1 
ATOM   2789 N N   . GLY C 1 68  ? -2.50000  26.74200 -19.63900 1.000 22.77935 ? 67  GLY C N   1 
ATOM   2790 C CA  . GLY C 1 68  ? -3.72300  26.04500 -19.97300 1.000 25.16993 ? 67  GLY C CA  1 
ATOM   2791 C C   . GLY C 1 68  ? -3.51800  25.01800 -21.07500 1.000 21.64888 ? 67  GLY C C   1 
ATOM   2792 O O   . GLY C 1 68  ? -2.82600  25.26600 -22.05900 1.000 20.45485 ? 67  GLY C O   1 
ATOM   2793 N N   . LEU C 1 69  ? -4.16200  23.86700 -20.89600 1.000 23.32263 ? 68  LEU C N   1 
ATOM   2794 C CA  . LEU C 1 69  ? -4.08300  22.71800 -21.78600 1.000 19.21678 ? 68  LEU C CA  1 
ATOM   2795 C C   . LEU C 1 69  ? -5.50300  22.40200 -22.25000 1.000 25.21057 ? 68  LEU C C   1 
ATOM   2796 O O   . LEU C 1 69  ? -6.34800  21.98100 -21.45300 1.000 22.94967 ? 68  LEU C O   1 
ATOM   2797 C CB  . LEU C 1 69  ? -3.44300  21.53600 -21.06400 1.000 18.41415 ? 68  LEU C CB  1 
ATOM   2798 C CG  . LEU C 1 69  ? -2.05700  21.87200 -20.50600 1.000 17.89439 ? 68  LEU C CG  1 
ATOM   2799 C CD1 . LEU C 1 69  ? -1.59000  20.93000 -19.41300 1.000 13.52408 ? 68  LEU C CD1 1 
ATOM   2800 C CD2 . LEU C 1 69  ? -1.02900  21.93900 -21.65300 1.000 17.63590 ? 68  LEU C CD2 1 
ATOM   2801 N N   . HIS C 1 70  ? -5.77600  22.63100 -23.53200 1.000 30.49035 ? 69  HIS C N   1 
ATOM   2802 C CA  . HIS C 1 70  ? -7.12300  22.53100 -24.06500 1.000 23.87381 ? 69  HIS C CA  1 
ATOM   2803 C C   . HIS C 1 70  ? -7.19400  21.49300 -25.17300 1.000 24.95324 ? 69  HIS C C   1 
ATOM   2804 O O   . HIS C 1 70  ? -6.18900  20.97100 -25.66800 1.000 22.12654 ? 69  HIS C O   1 
ATOM   2805 C CB  . HIS C 1 70  ? -7.61300  23.86300 -24.64700 1.000 26.45615 ? 69  HIS C CB  1 
ATOM   2806 C CG  . HIS C 1 70  ? -7.39100  25.04900 -23.76600 1.000 22.27567 ? 69  HIS C CG  1 
ATOM   2807 N ND1 . HIS C 1 70  ? -7.13200  24.94600 -22.41900 1.000 29.19328 ? 69  HIS C ND1 1 
ATOM   2808 C CD2 . HIS C 1 70  ? -7.40700  26.37300 -24.04600 1.000 23.57732 ? 69  HIS C CD2 1 
ATOM   2809 C CE1 . HIS C 1 70  ? -6.98700  26.15600 -21.90700 1.000 28.99043 ? 69  HIS C CE1 1 
ATOM   2810 N NE2 . HIS C 1 70  ? -7.15800  27.04000 -22.87400 1.000 26.06462 ? 69  HIS C NE2 1 
ATOM   2811 N N   . ARG C 1 71  ? -8.42900  21.20700 -25.55400 1.000 27.67217 ? 70  ARG C N   1 
ATOM   2812 C CA  . ARG C 1 71  ? -8.68000  20.59900 -26.84000 1.000 24.84274 ? 70  ARG C CA  1 
ATOM   2813 C C   . ARG C 1 71  ? -8.24400  21.54600 -27.94900 1.000 29.52961 ? 70  ARG C C   1 
ATOM   2814 O O   . ARG C 1 71  ? -8.26300  22.77200 -27.78800 1.000 25.87654 ? 70  ARG C O   1 
ATOM   2815 C CB  . ARG C 1 71  ? -10.15800 20.28700 -26.99200 1.000 23.77564 ? 70  ARG C CB  1 
ATOM   2816 C CG  . ARG C 1 71  ? -10.48300 18.87300 -26.67600 1.000 33.71958 ? 70  ARG C CG  1 
ATOM   2817 C CD  . ARG C 1 71  ? -11.00800 18.69400 -25.27600 1.000 32.59387 ? 70  ARG C CD  1 
ATOM   2818 N NE  . ARG C 1 71  ? -12.07800 19.64000 -25.00400 1.000 36.02963 ? 70  ARG C NE  1 
ATOM   2819 C CZ  . ARG C 1 71  ? -13.35100 19.44100 -25.31600 1.000 40.89893 ? 70  ARG C CZ  1 
ATOM   2820 N NH1 . ARG C 1 71  ? -13.74900 18.34700 -25.94400 1.000 43.36417 ? 70  ARG C NH1 1 
ATOM   2821 N NH2 . ARG C 1 71  ? -14.25000 20.36600 -24.99100 1.000 43.37241 ? 70  ARG C NH2 1 
ATOM   2822 N N   . GLU C 1 72  ? -7.80600  20.96300 -29.06700 1.000 23.81737 ? 71  GLU C N   1 
ATOM   2823 C CA  . GLU C 1 72  ? -7.92300  21.64900 -30.33600 1.000 21.08821 ? 71  GLU C CA  1 
ATOM   2824 C C   . GLU C 1 72  ? -9.39700  21.80400 -30.63500 1.000 22.35549 ? 71  GLU C C   1 
ATOM   2825 O O   . GLU C 1 72  ? -10.20300 20.94500 -30.26800 1.000 21.61723 ? 71  GLU C O   1 
ATOM   2826 C CB  . GLU C 1 72  ? -7.24900  20.86600 -31.46000 1.000 24.58898 ? 71  GLU C CB  1 
ATOM   2827 C CG  . GLU C 1 72  ? -5.73200  20.73300 -31.36000 1.000 24.70088 ? 71  GLU C CG  1 
ATOM   2828 C CD  . GLU C 1 72  ? -5.18600  19.65800 -32.28100 1.000 27.27888 ? 71  GLU C CD  1 
ATOM   2829 O OE1 . GLU C 1 72  ? -5.98700  18.97400 -32.95500 1.000 28.05449 ? 71  GLU C OE1 1 
ATOM   2830 O OE2 . GLU C 1 72  ? -3.95500  19.48100 -32.33000 1.000 31.16050 ? 71  GLU C OE2 1 
ATOM   2831 N N   . GLY C 1 73  ? -9.75600  22.92600 -31.25900 1.000 26.16992 ? 72  GLY C N   1 
ATOM   2832 C CA  . GLY C 1 73  ? -11.11600 23.11000 -31.73900 1.000 26.84001 ? 72  GLY C CA  1 
ATOM   2833 C C   . GLY C 1 73  ? -11.59800 24.54600 -31.80000 1.000 29.43507 ? 72  GLY C C   1 
ATOM   2834 O O   . GLY C 1 73  ? -12.45100 24.89000 -32.63000 1.000 24.80715 ? 72  GLY C O   1 
ATOM   2835 N N   . ARG C 1 74  ? -11.04700 25.38800 -30.92800 1.000 26.44688 ? 73  ARG C N   1 
ATOM   2836 C CA  . ARG C 1 74  ? -11.48600 26.75900 -30.73100 1.000 22.46676 ? 73  ARG C CA  1 
ATOM   2837 C C   . ARG C 1 74  ? -10.72000 27.71700 -31.64300 1.000 29.00793 ? 73  ARG C C   1 
ATOM   2838 O O   . ARG C 1 74  ? -9.64200  27.40500 -32.16200 1.000 29.60289 ? 73  ARG C O   1 
ATOM   2839 C CB  . ARG C 1 74  ? -11.31100 27.14000 -29.26300 1.000 24.02544 ? 73  ARG C CB  1 
ATOM   2840 C CG  . ARG C 1 74  ? -11.98400 26.11400 -28.36100 1.000 32.26383 ? 73  ARG C CG  1 
ATOM   2841 C CD  . ARG C 1 74  ? -12.23600 26.54300 -26.91000 1.000 22.81518 ? 73  ARG C CD  1 
ATOM   2842 N NE  . ARG C 1 74  ? -13.22000 25.62500 -26.34600 1.000 27.43625 ? 73  ARG C NE  1 
ATOM   2843 C CZ  . ARG C 1 74  ? -12.92800 24.54200 -25.64200 1.000 29.35102 ? 73  ARG C CZ  1 
ATOM   2844 N NH1 . ARG C 1 74  ? -11.69200 24.28700 -25.24600 1.000 27.45436 ? 73  ARG C NH1 1 
ATOM   2845 N NH2 . ARG C 1 74  ? -13.90400 23.69800 -25.31900 1.000 28.34234 ? 73  ARG C NH2 1 
ATOM   2846 N N   . SER C 1 75  ? -11.30500 28.89100 -31.85000 1.000 24.49833 ? 74  SER C N   1 
ATOM   2847 C CA  . SER C 1 75  ? -10.73500 29.87300 -32.75500 1.000 20.56032 ? 74  SER C CA  1 
ATOM   2848 C C   . SER C 1 75  ? -9.71500  30.73300 -32.03500 1.000 24.61372 ? 74  SER C C   1 
ATOM   2849 O O   . SER C 1 75  ? -9.79100  30.92600 -30.81500 1.000 24.58811 ? 74  SER C O   1 
ATOM   2850 C CB  . SER C 1 75  ? -11.83500 30.76900 -33.31800 1.000 23.99340 ? 74  SER C CB  1 
ATOM   2851 O OG  . SER C 1 75  ? -12.45600 31.51000 -32.27400 1.000 17.09151 ? 74  SER C OG  1 
ATOM   2852 N N   . ALA C 1 76  ? -8.76700  31.28200 -32.80500 1.000 21.93582 ? 75  ALA C N   1 
ATOM   2853 C CA  . ALA C 1 76  ? -7.76700  32.16100 -32.20100 1.000 22.29143 ? 75  ALA C CA  1 
ATOM   2854 C C   . ALA C 1 76  ? -8.44000  33.30900 -31.45900 1.000 28.69219 ? 75  ALA C C   1 
ATOM   2855 O O   . ALA C 1 76  ? -7.93300  33.77900 -30.42200 1.000 21.61115 ? 75  ALA C O   1 
ATOM   2856 C CB  . ALA C 1 76  ? -6.80600  32.70000 -33.25900 1.000 13.32579 ? 75  ALA C CB  1 
ATOM   2857 N N   . ASP C 1 77  ? -9.61700  33.72200 -31.94200 1.000 19.25198 ? 76  ASP C N   1 
ATOM   2858 C CA  . ASP C 1 77  ? -10.31700 34.84300 -31.33400 1.000 26.43783 ? 76  ASP C CA  1 
ATOM   2859 C C   . ASP C 1 77  ? -10.89600 34.47100 -29.97600 1.000 29.36046 ? 76  ASP C C   1 
ATOM   2860 O O   . ASP C 1 77  ? -10.75000 35.22100 -29.00200 1.000 28.19559 ? 76  ASP C O   1 
ATOM   2861 C CB  . ASP C 1 77  ? -11.42000 35.34700 -32.25100 1.000 23.87107 ? 76  ASP C CB  1 
ATOM   2862 C CG  . ASP C 1 77  ? -12.22000 36.43800 -31.60400 1.000 43.88709 ? 76  ASP C CG  1 
ATOM   2863 O OD1 . ASP C 1 77  ? -11.72500 37.58300 -31.59800 1.000 57.58802 ? 76  ASP C OD1 1 
ATOM   2864 O OD2 . ASP C 1 77  ? -13.29900 36.15200 -31.04000 1.000 52.49100 ? 76  ASP C OD2 1 
ATOM   2865 N N   . LEU C 1 78  ? -11.58800 33.33400 -29.89900 1.000 27.40510 ? 77  LEU C N   1 
ATOM   2866 C CA  . LEU C 1 78  ? -12.12000 32.89500 -28.61700 1.000 25.72552 ? 77  LEU C CA  1 
ATOM   2867 C C   . LEU C 1 78  ? -10.99200 32.70600 -27.61100 1.000 27.90356 ? 77  LEU C C   1 
ATOM   2868 O O   . LEU C 1 78  ? -11.13000 33.05700 -26.43400 1.000 26.16795 ? 77  LEU C O   1 
ATOM   2869 C CB  . LEU C 1 78  ? -12.91400 31.59700 -28.79600 1.000 25.71374 ? 77  LEU C CB  1 
ATOM   2870 C CG  . LEU C 1 78  ? -13.69600 31.05000 -27.59100 1.000 34.63523 ? 77  LEU C CG  1 
ATOM   2871 C CD1 . LEU C 1 78  ? -12.85200 30.09800 -26.76100 1.000 33.75510 ? 77  LEU C CD1 1 
ATOM   2872 C CD2 . LEU C 1 78  ? -14.23900 32.16000 -26.71000 1.000 30.96634 ? 77  LEU C CD2 1 
ATOM   2873 N N   . LYS C 1 79  ? -9.85800  32.16700 -28.06800 1.000 31.21309 ? 78  LYS C N   1 
ATOM   2874 C CA  . LYS C 1 79  ? -8.77400  31.81000 -27.16300 1.000 24.63561 ? 78  LYS C CA  1 
ATOM   2875 C C   . LYS C 1 79  ? -8.08700  33.04700 -26.60100 1.000 23.53651 ? 78  LYS C C   1 
ATOM   2876 O O   . LYS C 1 79  ? -7.64900  33.03900 -25.45000 1.000 27.74556 ? 78  LYS C O   1 
ATOM   2877 C CB  . LYS C 1 79  ? -7.77400  30.92000 -27.89200 1.000 24.79557 ? 78  LYS C CB  1 
ATOM   2878 C CG  . LYS C 1 79  ? -8.24400  29.49200 -28.13700 1.000 20.70534 ? 78  LYS C CG  1 
ATOM   2879 C CD  . LYS C 1 79  ? -7.12000  28.67500 -28.80000 1.000 23.55030 ? 78  LYS C CD  1 
ATOM   2880 C CE  . LYS C 1 79  ? -7.11100  28.83300 -30.31800 1.000 21.17639 ? 78  LYS C CE  1 
ATOM   2881 N NZ  . LYS C 1 79  ? -5.86500  28.35400 -30.96600 1.000 18.59865 ? 78  LYS C NZ  1 
ATOM   2882 N N   . GLY C 1 80  ? -7.99300  34.11900 -27.38900 1.000 30.97443 ? 79  GLY C N   1 
ATOM   2883 C CA  . GLY C 1 80  ? -7.44700  35.36100 -26.86600 1.000 26.00261 ? 79  GLY C CA  1 
ATOM   2884 C C   . GLY C 1 80  ? -8.40200  36.05900 -25.91700 1.000 25.37719 ? 79  GLY C C   1 
ATOM   2885 O O   . GLY C 1 80  ? -7.97100  36.67800 -24.93800 1.000 29.28714 ? 79  GLY C O   1 
ATOM   2886 N N   . GLN C 1 81  ? -9.70600  35.99700 -26.20900 1.000 25.23999 ? 80  GLN C N   1 
ATOM   2887 C CA  . GLN C 1 81  ? -10.70900 36.40100 -25.22700 1.000 24.54779 ? 80  GLN C CA  1 
ATOM   2888 C C   . GLN C 1 81  ? -10.48900 35.66100 -23.90900 1.000 29.87664 ? 80  GLN C C   1 
ATOM   2889 O O   . GLN C 1 81  ? -10.37300 36.27900 -22.84300 1.000 30.54097 ? 80  GLN C O   1 
ATOM   2890 C CB  . GLN C 1 81  ? -12.12000 36.12400 -25.75700 1.000 21.80928 ? 80  GLN C CB  1 
ATOM   2891 C CG  . GLN C 1 81  ? -12.75000 37.21600 -26.60400 1.000 33.17882 ? 80  GLN C CG  1 
ATOM   2892 C CD  . GLN C 1 81  ? -14.29100 37.08600 -26.72000 1.000 45.09490 ? 80  GLN C CD  1 
ATOM   2893 O OE1 . GLN C 1 81  ? -15.04900 37.62100 -25.89500 1.000 32.27589 ? 80  GLN C OE1 1 
ATOM   2894 N NE2 . GLN C 1 81  ? -14.74500 36.36900 -27.74900 1.000 40.87008 ? 80  GLN C NE2 1 
ATOM   2895 N N   . LEU C 1 82  ? -10.40700 34.32300 -23.97600 1.000 31.87290 ? 81  LEU C N   1 
ATOM   2896 C CA  . LEU C 1 82  ? -10.24500 33.51100 -22.77400 1.000 28.09149 ? 81  LEU C CA  1 
ATOM   2897 C C   . LEU C 1 82  ? -8.94000  33.84000 -22.06200 1.000 32.43987 ? 81  LEU C C   1 
ATOM   2898 O O   . LEU C 1 82  ? -8.91600  34.00500 -20.83800 1.000 36.57302 ? 81  LEU C O   1 
ATOM   2899 C CB  . LEU C 1 82  ? -10.30200 32.02600 -23.12700 1.000 30.42365 ? 81  LEU C CB  1 
ATOM   2900 C CG  . LEU C 1 82  ? -10.16500 30.96600 -22.01600 1.000 24.87746 ? 81  LEU C CG  1 
ATOM   2901 C CD1 . LEU C 1 82  ? -11.17200 31.20700 -20.92100 1.000 22.48184 ? 81  LEU C CD1 1 
ATOM   2902 C CD2 . LEU C 1 82  ? -10.31200 29.54500 -22.59500 1.000 22.16900 ? 81  LEU C CD2 1 
ATOM   2903 N N   . ALA C 1 83  ? -7.84000  33.94000 -22.80800 1.000 26.77036 ? 82  ALA C N   1 
ATOM   2904 C CA  . ALA C 1 83  ? -6.58100  34.29900 -22.17000 1.000 25.98383 ? 82  ALA C CA  1 
ATOM   2905 C C   . ALA C 1 83  ? -6.69700  35.65500 -21.48900 1.000 27.42869 ? 82  ALA C C   1 
ATOM   2906 O O   . ALA C 1 83  ? -6.36700  35.79600 -20.30200 1.000 24.37798 ? 82  ALA C O   1 
ATOM   2907 C CB  . ALA C 1 83  ? -5.44500  34.28400 -23.19300 1.000 19.87229 ? 82  ALA C CB  1 
ATOM   2908 N N   . GLN C 1 84  ? -7.22300  36.65400 -22.21300 1.000 29.00887 ? 83  GLN C N   1 
ATOM   2909 C CA  . GLN C 1 84  ? -7.31500  38.01100 -21.67600 1.000 27.80362 ? 83  GLN C CA  1 
ATOM   2910 C C   . GLN C 1 84  ? -8.24500  38.08100 -20.46700 1.000 26.64523 ? 83  GLN C C   1 
ATOM   2911 O O   . GLN C 1 84  ? -7.96000  38.81000 -19.50900 1.000 24.97029 ? 83  GLN C O   1 
ATOM   2912 C CB  . GLN C 1 84  ? -7.76600  38.98400 -22.77100 1.000 29.30950 ? 83  GLN C CB  1 
ATOM   2913 C CG  . GLN C 1 84  ? -8.06400  40.40300 -22.28100 1.000 30.49960 ? 83  GLN C CG  1 
ATOM   2914 C CD  . GLN C 1 84  ? -6.80800  41.14600 -21.86600 1.000 36.30606 ? 83  GLN C CD  1 
ATOM   2915 O OE1 . GLN C 1 84  ? -5.89900  41.35800 -22.66900 1.000 29.93757 ? 83  GLN C OE1 1 
ATOM   2916 N NE2 . GLN C 1 84  ? -6.73600  41.51600 -20.58600 1.000 36.50082 ? 83  GLN C NE2 1 
ATOM   2917 N N   . ARG C 1 85  ? -9.35500  37.31700 -20.48600 1.000 25.87867 ? 84  ARG C N   1 
ATOM   2918 C CA  . ARG C 1 85  ? -10.24700 37.27600 -19.32600 1.000 30.82239 ? 84  ARG C CA  1 
ATOM   2919 C C   . ARG C 1 85  ? -9.59100  36.62600 -18.11300 1.000 29.24359 ? 84  ARG C C   1 
ATOM   2920 O O   . ARG C 1 85  ? -9.89700  37.01500 -16.98300 1.000 26.06801 ? 84  ARG C O   1 
ATOM   2921 C CB  . ARG C 1 85  ? -11.55700 36.54400 -19.63900 1.000 32.71033 ? 84  ARG C CB  1 
ATOM   2922 C CG  . ARG C 1 85  ? -12.72800 37.08500 -18.78500 1.000 31.13934 ? 84  ARG C CG  1 
ATOM   2923 C CD  . ARG C 1 85  ? -14.04000 36.34700 -18.95800 1.000 34.39127 ? 84  ARG C CD  1 
ATOM   2924 N NE  . ARG C 1 85  ? -14.58300 35.96600 -17.65700 1.000 40.18840 ? 84  ARG C NE  1 
ATOM   2925 C CZ  . ARG C 1 85  ? -15.69700 35.26400 -17.47700 1.000 41.46941 ? 84  ARG C CZ  1 
ATOM   2926 N NH1 . ARG C 1 85  ? -16.45000 34.88400 -18.50100 1.000 35.62193 ? 84  ARG C NH1 1 
ATOM   2927 N NH2 . ARG C 1 85  ? -16.05700 34.92400 -16.23800 1.000 32.66645 ? 84  ARG C NH2 1 
ATOM   2928 N N   . ILE C 1 86  ? -8.69700  35.64500 -18.33000 1.000 32.86623 ? 85  ILE C N   1 
ATOM   2929 C CA  . ILE C 1 86  ? -7.92900  35.02800 -17.24500 1.000 24.25842 ? 85  ILE C CA  1 
ATOM   2930 C C   . ILE C 1 86  ? -6.96100  36.03000 -16.62900 1.000 20.59728 ? 85  ILE C C   1 
ATOM   2931 O O   . ILE C 1 86  ? -6.81900  36.11200 -15.40400 1.000 22.78080 ? 85  ILE C O   1 
ATOM   2932 C CB  . ILE C 1 86  ? -7.17800  33.78200 -17.74800 1.000 25.97702 ? 85  ILE C CB  1 
ATOM   2933 C CG1 . ILE C 1 86  ? -8.12400  32.58400 -17.91400 1.000 24.11745 ? 85  ILE C CG1 1 
ATOM   2934 C CG2 . ILE C 1 86  ? -6.04900  33.42600 -16.80900 1.000 17.71307 ? 85  ILE C CG2 1 
ATOM   2935 C CD1 . ILE C 1 86  ? -7.59200  31.52900 -18.88600 1.000 23.32917 ? 85  ILE C CD1 1 
ATOM   2936 N N   . VAL C 1 87  ? -6.26000  36.79400 -17.45300 1.000 22.32414 ? 86  VAL C N   1 
ATOM   2937 C CA  . VAL C 1 87  ? -5.37500  37.80700 -16.88200 1.000 28.19544 ? 86  VAL C CA  1 
ATOM   2938 C C   . VAL C 1 87  ? -6.16400  38.75700 -15.97800 1.000 27.02901 ? 86  VAL C C   1 
ATOM   2939 O O   . VAL C 1 87  ? -5.84300  38.93600 -14.79600 1.000 24.04800 ? 86  VAL C O   1 
ATOM   2940 C CB  . VAL C 1 87  ? -4.63300  38.57000 -17.99400 1.000 26.81476 ? 86  VAL C CB  1 
ATOM   2941 C CG1 . VAL C 1 87  ? -3.86800  39.73400 -17.39300 1.000 24.82948 ? 86  VAL C CG1 1 
ATOM   2942 C CG2 . VAL C 1 87  ? -3.70300  37.62900 -18.77300 1.000 21.45239 ? 86  VAL C CG2 1 
ATOM   2943 N N   . ASP C 1 88  ? -7.22500  39.35900 -16.51700 1.000 25.58486 ? 87  ASP C N   1 
ATOM   2944 C CA  . ASP C 1 88  ? -7.96800  40.35400 -15.75400 1.000 25.27281 ? 87  ASP C CA  1 
ATOM   2945 C C   . ASP C 1 88  ? -8.57700  39.74700 -14.50700 1.000 28.08344 ? 87  ASP C C   1 
ATOM   2946 O O   . ASP C 1 88  ? -8.52200  40.34500 -13.42100 1.000 32.53713 ? 87  ASP C O   1 
ATOM   2947 C CB  . ASP C 1 88  ? -9.05500  40.97500 -16.62100 1.000 23.21103 ? 87  ASP C CB  1 
ATOM   2948 C CG  . ASP C 1 88  ? -8.48000  41.77000 -17.78200 1.000 38.38309 ? 87  ASP C CG  1 
ATOM   2949 O OD1 . ASP C 1 88  ? -7.47600  42.51100 -17.57700 1.000 42.65430 ? 87  ASP C OD1 1 
ATOM   2950 O OD2 . ASP C 1 88  ? -9.03700  41.64700 -18.89800 1.000 33.24018 ? 87  ASP C OD2 1 
ATOM   2951 N N   . ASP C 1 89  ? -9.15300  38.55700 -14.63600 1.000 19.69023 ? 88  ASP C N   1 
ATOM   2952 C CA  . ASP C 1 89  ? -9.83200  37.96300 -13.49600 1.000 21.22897 ? 88  ASP C CA  1 
ATOM   2953 C C   . ASP C 1 89  ? -8.84600  37.48100 -12.43900 1.000 25.71845 ? 88  ASP C C   1 
ATOM   2954 O O   . ASP C 1 89  ? -9.07400  37.69500 -11.24100 1.000 24.65879 ? 88  ASP C O   1 
ATOM   2955 C CB  . ASP C 1 89  ? -10.73500 36.82700 -13.96000 1.000 24.30699 ? 88  ASP C CB  1 
ATOM   2956 C CG  . ASP C 1 89  ? -11.96500 37.33100 -14.63300 1.000 23.69140 ? 88  ASP C CG  1 
ATOM   2957 O OD1 . ASP C 1 89  ? -12.21000 38.55400 -14.53900 1.000 28.90877 ? 88  ASP C OD1 1 
ATOM   2958 O OD2 . ASP C 1 89  ? -12.68200 36.52000 -15.24900 1.000 26.91175 ? 88  ASP C OD2 1 
ATOM   2959 N N   . VAL C 1 90  ? -7.75900  36.81000 -12.84800 1.000 23.78625 ? 89  VAL C N   1 
ATOM   2960 C CA  . VAL C 1 90  ? -6.76500  36.38500 -11.86600 1.000 20.79181 ? 89  VAL C CA  1 
ATOM   2961 C C   . VAL C 1 90  ? -6.21200  37.59600 -11.14600 1.000 24.40035 ? 89  VAL C C   1 
ATOM   2962 O O   . VAL C 1 90  ? -6.01200  37.57700 -9.92400  1.000 29.09387 ? 89  VAL C O   1 
ATOM   2963 C CB  . VAL C 1 90  ? -5.64400  35.56400 -12.52000 1.000 22.05078 ? 89  VAL C CB  1 
ATOM   2964 C CG1 . VAL C 1 90  ? -4.55000  35.26600 -11.48700 1.000 24.17659 ? 89  VAL C CG1 1 
ATOM   2965 C CG2 . VAL C 1 90  ? -6.18600  34.27500 -13.09200 1.000 17.54608 ? 89  VAL C CG2 1 
ATOM   2966 N N   . SER C 1 91  ? -6.00700  38.68600 -11.88500 1.000 23.11772 ? 90  SER C N   1 
ATOM   2967 C CA  . SER C 1 91  ? -5.58100  39.94100 -11.27800 1.000 27.61827 ? 90  SER C CA  1 
ATOM   2968 C C   . SER C 1 91  ? -6.48000  40.31600 -10.10200 1.000 27.01634 ? 90  SER C C   1 
ATOM   2969 O O   . SER C 1 91  ? -6.01700  40.40800 -8.96100  1.000 30.14213 ? 90  SER C O   1 
ATOM   2970 C CB  . SER C 1 91  ? -5.57200  41.03900 -12.33800 1.000 27.42776 ? 90  SER C CB  1 
ATOM   2971 O OG  . SER C 1 91  ? -5.14000  42.26100 -11.78100 1.000 35.41955 ? 90  SER C OG  1 
ATOM   2972 N N   . VAL C 1 92  ? -7.78200  40.48500 -10.36100 1.000 20.63887 ? 91  VAL C N   1 
ATOM   2973 C CA  . VAL C 1 92  ? -8.72500  40.83700 -9.30100  1.000 25.02305 ? 91  VAL C CA  1 
ATOM   2974 C C   . VAL C 1 92  ? -8.69000  39.80000 -8.17900  1.000 21.87980 ? 91  VAL C C   1 
ATOM   2975 O O   . VAL C 1 92  ? -8.48700  40.12700 -7.00300  1.000 21.27389 ? 91  VAL C O   1 
ATOM   2976 C CB  . VAL C 1 92  ? -10.14400 40.98700 -9.88100  1.000 29.65818 ? 91  VAL C CB  1 
ATOM   2977 C CG1 . VAL C 1 92  ? -11.20600 41.01300 -8.76400  1.000 15.66869 ? 91  VAL C CG1 1 
ATOM   2978 C CG2 . VAL C 1 92  ? -10.23800 42.22400 -10.76300 1.000 26.36058 ? 91  VAL C CG2 1 
ATOM   2979 N N   . ALA C 1 93  ? -8.86000  38.53300 -8.53900  1.000 23.02252 ? 92  ALA C N   1 
ATOM   2980 C CA  . ALA C 1 93  ? -9.04600  37.47100 -7.55400  1.000 26.60853 ? 92  ALA C CA  1 
ATOM   2981 C C   . ALA C 1 93  ? -7.87000  37.38000 -6.58400  1.000 31.85980 ? 92  ALA C C   1 
ATOM   2982 O O   . ALA C 1 93  ? -8.06000  37.29000 -5.36400  1.000 28.38770 ? 92  ALA C O   1 
ATOM   2983 C CB  . ALA C 1 93  ? -9.25600  36.14400 -8.28600  1.000 22.06033 ? 92  ALA C CB  1 
ATOM   2984 N N   . ALA C 1 94  ? -6.64600  37.40800 -7.11300  1.000 22.81518 ? 93  ALA C N   1 
ATOM   2985 C CA  . ALA C 1 94  ? -5.43300  37.27700 -6.32400  1.000 28.00666 ? 93  ALA C CA  1 
ATOM   2986 C C   . ALA C 1 94  ? -4.79400  38.62400 -5.96800  1.000 33.32440 ? 93  ALA C C   1 
ATOM   2987 O O   . ALA C 1 94  ? -3.72800  38.64400 -5.34400  1.000 30.50507 ? 93  ALA C O   1 
ATOM   2988 C CB  . ALA C 1 94  ? -4.42800  36.39900 -7.07800  1.000 28.55511 ? 93  ALA C CB  1 
ATOM   2989 N N   . GLU C 1 95  ? -5.42000  39.74200 -6.34300  1.000 35.43510 ? 94  GLU C N   1 
ATOM   2990 C CA  . GLU C 1 95  ? -4.93200  41.08600 -6.03100  1.000 32.70550 ? 94  GLU C CA  1 
ATOM   2991 C C   . GLU C 1 95  ? -3.46600  41.24500 -6.44000  1.000 28.38670 ? 94  GLU C C   1 
ATOM   2992 O O   . GLU C 1 95  ? -2.57100  41.44100 -5.62300  1.000 29.11634 ? 94  GLU C O   1 
ATOM   2993 C CB  . GLU C 1 95  ? -5.14400  41.40700 -4.55000  1.000 28.49330 ? 94  GLU C CB  1 
ATOM   2994 C CG  . GLU C 1 95  ? -6.57900  41.21300 -4.09100  1.000 26.31764 ? 94  GLU C CG  1 
ATOM   2995 C CD  . GLU C 1 95  ? -6.66000  40.82800 -2.61800  1.000 46.74040 ? 94  GLU C CD  1 
ATOM   2996 O OE1 . GLU C 1 95  ? -6.27700  41.67100 -1.78100  1.000 51.09091 ? 94  GLU C OE1 1 
ATOM   2997 O OE2 . GLU C 1 95  ? -7.08300  39.69000 -2.28900  1.000 44.02127 ? 94  GLU C OE2 1 
ATOM   2998 N N   . ILE C 1 96  ? -3.23600  41.14000 -7.74400  1.000 36.68387 ? 95  ILE C N   1 
ATOM   2999 C CA  . ILE C 1 96  ? -1.89700  41.19200 -8.32300  1.000 33.78353 ? 95  ILE C CA  1 
ATOM   3000 C C   . ILE C 1 96  ? -1.97900  41.97200 -9.62300  1.000 37.57925 ? 95  ILE C C   1 
ATOM   3001 O O   . ILE C 1 96  ? -2.88100  41.72800 -10.43300 1.000 45.21677 ? 95  ILE C O   1 
ATOM   3002 C CB  . ILE C 1 96  ? -1.32900  39.78000 -8.56300  1.000 29.88900 ? 95  ILE C CB  1 
ATOM   3003 C CG1 . ILE C 1 96  ? -0.76400  39.22700 -7.25600  1.000 36.82298 ? 95  ILE C CG1 1 
ATOM   3004 C CG2 . ILE C 1 96  ? -0.24600  39.80300 -9.59100  1.000 30.46410 ? 95  ILE C CG2 1 
ATOM   3005 C CD1 . ILE C 1 96  ? -1.07800  37.75300 -7.02400  1.000 40.41521 ? 95  ILE C CD1 1 
ATOM   3006 N N   . ASP C 1 97  ? -1.05600  42.91900 -9.82200  1.000 39.36549 ? 96  ASP C N   1 
ATOM   3007 C CA  . ASP C 1 97  ? -1.05400  43.69300 -11.06200 1.000 36.90946 ? 96  ASP C CA  1 
ATOM   3008 C C   . ASP C 1 97  ? -1.00800  42.77400 -12.28000 1.000 31.48426 ? 96  ASP C C   1 
ATOM   3009 O O   . ASP C 1 97  ? -0.47900  41.66100 -12.22800 1.000 29.76602 ? 96  ASP C O   1 
ATOM   3010 C CB  . ASP C 1 97  ? 0.13300   44.65400 -11.10800 1.000 35.55407 ? 96  ASP C CB  1 
ATOM   3011 C CG  . ASP C 1 97  ? -0.03600  45.72600 -12.17700 1.000 48.33034 ? 96  ASP C CG  1 
ATOM   3012 O OD1 . ASP C 1 97  ? -1.18600  45.98600 -12.58100 1.000 43.98450 ? 96  ASP C OD1 1 
ATOM   3013 O OD2 . ASP C 1 97  ? 0.96900   46.29000 -12.65100 1.000 52.12783 ? 96  ASP C OD2 1 
ATOM   3014 N N   . ARG C 1 98  ? -1.58800  43.24900 -13.38300 1.000 39.40341 ? 97  ARG C N   1 
ATOM   3015 C CA  . ARG C 1 98  ? -1.51100  42.53300 -14.65700 1.000 29.44248 ? 97  ARG C CA  1 
ATOM   3016 C C   . ARG C 1 98  ? -0.06800  42.20400 -15.03000 1.000 30.15226 ? 97  ARG C C   1 
ATOM   3017 O O   . ARG C 1 98  ? 0.23000   41.10000 -15.49000 1.000 33.40963 ? 97  ARG C O   1 
ATOM   3018 C CB  . ARG C 1 98  ? -2.15500  43.37600 -15.76900 1.000 40.49318 ? 97  ARG C CB  1 
ATOM   3019 C CG  . ARG C 1 98  ? -3.68300  43.22600 -15.94500 1.000 46.53074 ? 97  ARG C CG  1 
ATOM   3020 C CD  . ARG C 1 98  ? -4.39900  44.57200 -15.85600 1.000 48.61743 ? 97  ARG C CD  1 
ATOM   3021 N NE  . ARG C 1 98  ? -4.48000  45.01500 -14.46600 1.000 58.28844 ? 97  ARG C NE  1 
ATOM   3022 C CZ  . ARG C 1 98  ? -3.65200  45.88800 -13.90300 1.000 47.13972 ? 97  ARG C CZ  1 
ATOM   3023 N NH1 . ARG C 1 98  ? -2.69600  46.48900 -14.60100 1.000 48.50414 ? 97  ARG C NH1 1 
ATOM   3024 N NH2 . ARG C 1 98  ? -3.77500  46.15500 -12.60700 1.000 39.49530 ? 97  ARG C NH2 1 
ATOM   3025 N N   . LYS C 1 99  ? 0.84000   43.15700 -14.83800 1.000 33.09934 ? 98  LYS C N   1 
ATOM   3026 C CA  . LYS C 1 99  ? 2.23700   43.01200 -15.22900 1.000 34.18993 ? 98  LYS C CA  1 
ATOM   3027 C C   . LYS C 1 99  ? 2.88500   41.71500 -14.74600 1.000 35.45142 ? 98  LYS C C   1 
ATOM   3028 O O   . LYS C 1 99  ? 3.90700   41.30200 -15.31600 1.000 35.76440 ? 98  LYS C O   1 
ATOM   3029 C CB  . LYS C 1 99  ? 3.00300   44.22400 -14.69600 1.000 37.39732 ? 98  LYS C CB  1 
ATOM   3030 C CG  . LYS C 1 99  ? 3.02700   44.25600 -13.17700 1.000 43.84317 ? 98  LYS C CG  1 
ATOM   3031 C CD  . LYS C 1 99  ? 4.22500   44.98900 -12.58400 1.000 51.17665 ? 98  LYS C CD  1 
ATOM   3032 C CE  . LYS C 1 99  ? 4.12800   46.51600 -12.73500 1.000 51.10179 ? 98  LYS C CE  1 
ATOM   3033 N NZ  . LYS C 1 99  ? 4.42600   47.25700 -11.46300 1.000 43.76557 ? 98  LYS C NZ  1 
ATOM   3034 N N   . HIS C 1 100 ? 2.31800   41.06000 -13.72400 1.000 30.73478 ? 99  HIS C N   1 
ATOM   3035 C CA  . HIS C 1 100 ? 2.90100   39.85800 -13.11900 1.000 31.87747 ? 99  HIS C CA  1 
ATOM   3036 C C   . HIS C 1 100 ? 2.36700   38.55100 -13.69400 1.000 26.97734 ? 99  HIS C C   1 
ATOM   3037 O O   . HIS C 1 100 ? 2.84600   37.48400 -13.30100 1.000 26.64097 ? 99  HIS C O   1 
ATOM   3038 C CB  . HIS C 1 100 ? 2.66000   39.84000 -11.60100 1.000 28.71904 ? 99  HIS C CB  1 
ATOM   3039 C CG  . HIS C 1 100 ? 3.39100   40.90900 -10.85300 1.000 31.64069 ? 99  HIS C CG  1 
ATOM   3040 N ND1 . HIS C 1 100 ? 2.76100   41.76600 -9.97500  1.000 38.39642 ? 99  HIS C ND1 1 
ATOM   3041 C CD2 . HIS C 1 100 ? 4.70300   41.24200 -10.82500 1.000 36.18835 ? 99  HIS C CD2 1 
ATOM   3042 C CE1 . HIS C 1 100 ? 3.64800   42.59600 -9.45700  1.000 41.48660 ? 99  HIS C CE1 1 
ATOM   3043 N NE2 . HIS C 1 100 ? 4.83500   42.30000 -9.95800  1.000 42.17641 ? 99  HIS C NE2 1 
ATOM   3044 N N   . ILE C 1 101 ? 1.39400   38.60200 -14.60000 1.000 27.59809 ? 100 ILE C N   1 
ATOM   3045 C CA  . ILE C 1 101 ? 0.60500   37.44000 -14.98600 1.000 24.23471 ? 100 ILE C CA  1 
ATOM   3046 C C   . ILE C 1 101 ? 1.02300   37.00200 -16.38400 1.000 26.17770 ? 100 ILE C C   1 
ATOM   3047 O O   . ILE C 1 101 ? 1.04100   37.81400 -17.32400 1.000 26.63963 ? 100 ILE C O   1 
ATOM   3048 C CB  . ILE C 1 101 ? -0.90400  37.75600 -14.92100 1.000 29.11741 ? 100 ILE C CB  1 
ATOM   3049 C CG1 . ILE C 1 101 ? -1.25700  38.36600 -13.56400 1.000 24.81391 ? 100 ILE C CG1 1 
ATOM   3050 C CG2 . ILE C 1 101 ? -1.75900  36.50600 -15.12100 1.000 25.17977 ? 100 ILE C CG2 1 
ATOM   3051 C CD1 . ILE C 1 101 ? -2.72700  38.52200 -13.33800 1.000 23.72832 ? 100 ILE C CD1 1 
ATOM   3052 N N   . TRP C 1 102 ? 1.35200   35.71500 -16.52000 1.000 24.82465 ? 101 TRP C N   1 
ATOM   3053 C CA  . TRP C 1 102 ? 1.62900   35.08100 -17.80500 1.000 23.13894 ? 101 TRP C CA  1 
ATOM   3054 C C   . TRP C 1 102 ? 0.60400   33.98400 -18.06600 1.000 23.12171 ? 101 TRP C C   1 
ATOM   3055 O O   . TRP C 1 102 ? 0.22500   33.25000 -17.15200 1.000 17.35650 ? 101 TRP C O   1 
ATOM   3056 C CB  . TRP C 1 102 ? 3.04500   34.47700 -17.86000 1.000 19.95538 ? 101 TRP C CB  1 
ATOM   3057 C CG  . TRP C 1 102 ? 4.14700   35.44900 -17.57700 1.000 25.95997 ? 101 TRP C CG  1 
ATOM   3058 C CD1 . TRP C 1 102 ? 4.14700   36.45700 -16.64600 1.000 26.51671 ? 101 TRP C CD1 1 
ATOM   3059 C CD2 . TRP C 1 102 ? 5.41900   35.50700 -18.22700 1.000 22.28815 ? 101 TRP C CD2 1 
ATOM   3060 N NE1 . TRP C 1 102 ? 5.33800   37.13400 -16.68700 1.000 30.19774 ? 101 TRP C NE1 1 
ATOM   3061 C CE2 . TRP C 1 102 ? 6.14200   36.56000 -17.63700 1.000 23.67909 ? 101 TRP C CE2 1 
ATOM   3062 C CE3 . TRP C 1 102 ? 6.02000   34.76400 -19.24500 1.000 21.52675 ? 101 TRP C CE3 1 
ATOM   3063 C CZ2 . TRP C 1 102 ? 7.41900   36.89600 -18.03800 1.000 24.86086 ? 101 TRP C CZ2 1 
ATOM   3064 C CZ3 . TRP C 1 102 ? 7.28200   35.08700 -19.63400 1.000 23.81637 ? 101 TRP C CZ3 1 
ATOM   3065 C CH2 . TRP C 1 102 ? 7.97400   36.15200 -19.04100 1.000 29.02901 ? 101 TRP C CH2 1 
ATOM   3066 N N   . VAL C 1 103 ? 0.16900   33.86000 -19.32100 1.000 18.59190 ? 102 VAL C N   1 
ATOM   3067 C CA  . VAL C 1 103 ? -0.84800  32.88800 -19.69000 1.000 20.50979 ? 102 VAL C CA  1 
ATOM   3068 C C   . VAL C 1 103 ? -0.45700  32.25800 -21.01900 1.000 23.23178 ? 102 VAL C C   1 
ATOM   3069 O O   . VAL C 1 103 ? -0.35100  32.96200 -22.02800 1.000 22.90689 ? 102 VAL C O   1 
ATOM   3070 C CB  . VAL C 1 103 ? -2.23900  33.54200 -19.79000 1.000 25.10059 ? 102 VAL C CB  1 
ATOM   3071 C CG1 . VAL C 1 103 ? -3.24800  32.58400 -20.38600 1.000 23.51400 ? 102 VAL C CG1 1 
ATOM   3072 C CG2 . VAL C 1 103 ? -2.71000  34.06000 -18.41300 1.000 19.36047 ? 102 VAL C CG2 1 
ATOM   3073 N N   . TYR C 1 104 ? -0.24400  30.93800 -21.03000 1.000 20.10790 ? 103 TYR C N   1 
ATOM   3074 C CA  . TYR C 1 104 ? 0.02100   30.19700 -22.26200 1.000 19.62611 ? 103 TYR C CA  1 
ATOM   3075 C C   . TYR C 1 104 ? -1.07300  29.15500 -22.44900 1.000 25.00534 ? 103 TYR C C   1 
ATOM   3076 O O   . TYR C 1 104 ? -1.43300  28.45700 -21.49400 1.000 25.27801 ? 103 TYR C O   1 
ATOM   3077 C CB  . TYR C 1 104 ? 1.38900   29.49700 -22.24400 1.000 21.01384 ? 103 TYR C CB  1 
ATOM   3078 C CG  . TYR C 1 104 ? 2.63700   30.36600 -22.42600 1.000 24.86255 ? 103 TYR C CG  1 
ATOM   3079 C CD1 . TYR C 1 104 ? 2.56000   31.75600 -22.54600 1.000 25.14141 ? 103 TYR C CD1 1 
ATOM   3080 C CD2 . TYR C 1 104 ? 3.90500   29.78000 -22.46300 1.000 26.32268 ? 103 TYR C CD2 1 
ATOM   3081 C CE1 . TYR C 1 104 ? 3.72700   32.53600 -22.70000 1.000 26.83334 ? 103 TYR C CE1 1 
ATOM   3082 C CE2 . TYR C 1 104 ? 5.07500   30.54400 -22.62400 1.000 26.38847 ? 103 TYR C CE2 1 
ATOM   3083 C CZ  . TYR C 1 104 ? 4.97800   31.92000 -22.73800 1.000 28.43849 ? 103 TYR C CZ  1 
ATOM   3084 O OH  . TYR C 1 104 ? 6.13200   32.66100 -22.88300 1.000 23.99957 ? 103 TYR C OH  1 
ATOM   3085 N N   . PHE C 1 105 ? -1.59500  29.04900 -23.67500 1.000 20.68453 ? 104 PHE C N   1 
ATOM   3086 C CA  . PHE C 1 105 ? -2.60000  28.05500 -24.03000 1.000 18.23175 ? 104 PHE C CA  1 
ATOM   3087 C C   . PHE C 1 105 ? -1.97500  27.07500 -25.00400 1.000 21.54075 ? 104 PHE C C   1 
ATOM   3088 O O   . PHE C 1 105 ? -1.65300  27.44700 -26.13700 1.000 24.48642 ? 104 PHE C O   1 
ATOM   3089 C CB  . PHE C 1 105 ? -3.81600  28.69800 -24.68100 1.000 26.26163 ? 104 PHE C CB  1 
ATOM   3090 C CG  . PHE C 1 105 ? -4.74800  29.35700 -23.72800 1.000 26.69467 ? 104 PHE C CG  1 
ATOM   3091 C CD1 . PHE C 1 105 ? -4.52000  29.32700 -22.37200 1.000 24.53633 ? 104 PHE C CD1 1 
ATOM   3092 C CD2 . PHE C 1 105 ? -5.86000  30.02900 -24.20700 1.000 25.80199 ? 104 PHE C CD2 1 
ATOM   3093 C CE1 . PHE C 1 105 ? -5.38700  29.94900 -21.50600 1.000 27.26319 ? 104 PHE C CE1 1 
ATOM   3094 C CE2 . PHE C 1 105 ? -6.72400  30.65400 -23.35000 1.000 27.24910 ? 104 PHE C CE2 1 
ATOM   3095 C CZ  . PHE C 1 105 ? -6.49000  30.60900 -21.99200 1.000 31.41796 ? 104 PHE C CZ  1 
ATOM   3096 N N   . GLY C 1 106 ? -1.83000  25.82500 -24.57900 1.000 25.66585 ? 105 GLY C N   1 
ATOM   3097 C CA  . GLY C 1 106 ? -1.44100  24.73900 -25.45900 1.000 22.76660 ? 105 GLY C CA  1 
ATOM   3098 C C   . GLY C 1 106 ? -2.63500  23.83200 -25.69600 1.000 23.66207 ? 105 GLY C C   1 
ATOM   3099 O O   . GLY C 1 106 ? -3.45900  23.62500 -24.80300 1.000 24.20797 ? 105 GLY C O   1 
ATOM   3100 N N   . GLU C 1 107 ? -2.73200  23.29900 -26.90700 1.000 23.31871 ? 106 GLU C N   1 
ATOM   3101 C CA  . GLU C 1 107 ? -3.90300  22.55500 -27.34000 1.000 22.85014 ? 106 GLU C CA  1 
ATOM   3102 C C   . GLU C 1 107 ? -3.48400  21.19900 -27.87100 1.000 25.32681 ? 106 GLU C C   1 
ATOM   3103 O O   . GLU C 1 107 ? -2.37900  21.02000 -28.38500 1.000 25.44684 ? 106 GLU C O   1 
ATOM   3104 C CB  . GLU C 1 107 ? -4.65900  23.26800 -28.44000 1.000 22.79597 ? 106 GLU C CB  1 
ATOM   3105 C CG  . GLU C 1 107 ? -4.63300  24.76600 -28.33600 1.000 30.19107 ? 106 GLU C CG  1 
ATOM   3106 C CD  . GLU C 1 107 ? -4.99100  25.40800 -29.64800 1.000 29.62097 ? 106 GLU C CD  1 
ATOM   3107 O OE1 . GLU C 1 107 ? -6.20900  25.58800 -29.87700 1.000 33.39177 ? 106 GLU C OE1 1 
ATOM   3108 O OE2 . GLU C 1 107 ? -4.07700  25.69400 -30.45500 1.000 26.58566 ? 106 GLU C OE2 1 
ATOM   3109 N N   . MET C 1 108 ? -4.39600  20.24800 -27.77500 1.000 28.25545 ? 107 MET C N   1 
ATOM   3110 C CA  . MET C 1 108 ? -4.13100  18.87100 -28.16200 1.000 32.68311 ? 107 MET C CA  1 
ATOM   3111 C C   . MET C 1 108 ? -5.39500  18.28700 -28.77100 1.000 26.02099 ? 107 MET C C   1 
ATOM   3112 O O   . MET C 1 108 ? -6.49400  18.79000 -28.53100 1.000 28.50446 ? 107 MET C O   1 
ATOM   3113 C CB  . MET C 1 108 ? -3.66100  18.03500 -26.95300 1.000 35.32814 ? 107 MET C CB  1 
ATOM   3114 C CG  . MET C 1 108 ? -2.82600  18.85000 -25.93300 1.000 34.37583 ? 107 MET C CG  1 
ATOM   3115 S SD  . MET C 1 108 ? -2.47500  18.11200 -24.33500 1.000 37.97315 ? 107 MET C SD  1 
ATOM   3116 C CE  . MET C 1 108 ? -0.77500  18.67900 -24.09900 1.000 26.89701 ? 107 MET C CE  1 
ATOM   3117 N N   . PRO C 1 109 ? -5.27500  17.24500 -29.57500 1.000 25.67941 ? 108 PRO C N   1 
ATOM   3118 C CA  . PRO C 1 109 ? -6.49100  16.57900 -30.05800 1.000 30.26293 ? 108 PRO C CA  1 
ATOM   3119 C C   . PRO C 1 109 ? -7.20200  15.88700 -28.90800 1.000 30.30077 ? 108 PRO C C   1 
ATOM   3120 O O   . PRO C 1 109 ? -6.57100  15.29900 -28.02900 1.000 31.38201 ? 108 PRO C O   1 
ATOM   3121 C CB  . PRO C 1 109 ? -5.98500  15.58700 -31.11300 1.000 27.43373 ? 108 PRO C CB  1 
ATOM   3122 C CG  . PRO C 1 109 ? -4.51400  15.60200 -31.03500 1.000 33.95593 ? 108 PRO C CG  1 
ATOM   3123 C CD  . PRO C 1 109 ? -4.04400  16.72800 -30.17800 1.000 25.09112 ? 108 PRO C CD  1 
ATOM   3124 N N   . ALA C 1 110 ? -8.53100  16.00200 -28.89800 1.000 27.03162 ? 109 ALA C N   1 
ATOM   3125 C CA  . ALA C 1 110 ? -9.30700  15.42800 -27.81000 1.000 25.25607 ? 109 ALA C CA  1 
ATOM   3126 C C   . ALA C 1 110 ? -9.12300  13.91700 -27.71600 1.000 30.30157 ? 109 ALA C C   1 
ATOM   3127 O O   . ALA C 1 110 ? -9.25300  13.33800 -26.62800 1.000 26.56499 ? 109 ALA C O   1 
ATOM   3128 C CB  . ALA C 1 110 ? -10.78500 15.76600 -27.99000 1.000 28.65695 ? 109 ALA C CB  1 
ATOM   3129 N N   . GLN C 1 111 ? -8.82200  13.26000 -28.83500 1.000 35.97902 ? 110 GLN C N   1 
ATOM   3130 C CA  . GLN C 1 111 ? -8.72600  11.80400 -28.82600 1.000 37.09822 ? 110 GLN C CA  1 
ATOM   3131 C C   . GLN C 1 111 ? -7.49800  11.28600 -28.06600 1.000 31.33601 ? 110 GLN C C   1 
ATOM   3132 O O   . GLN C 1 111 ? -7.41900  10.07600 -27.81400 1.000 31.05142 ? 110 GLN C O   1 
ATOM   3133 C CB  . GLN C 1 111 ? -8.75500  11.27000 -30.27200 1.000 34.02485 ? 110 GLN C CB  1 
ATOM   3134 C CG  . GLN C 1 111 ? -7.91000  12.07300 -31.27800 1.000 44.51487 ? 110 GLN C CG  1 
ATOM   3135 C CD  . GLN C 1 111 ? -8.46800  12.05400 -32.70500 1.000 48.29890 ? 110 GLN C CD  1 
ATOM   3136 O OE1 . GLN C 1 111 ? -9.65500  11.77000 -32.92700 1.000 45.70340 ? 110 GLN C OE1 1 
ATOM   3137 N NE2 . GLN C 1 111 ? -7.60100  12.34700 -33.68100 1.000 33.40670 ? 110 GLN C NE2 1 
ATOM   3138 N N   . GLN C 1 112 ? -6.55000  12.14800 -27.67400 1.000 30.78505 ? 111 GLN C N   1 
ATOM   3139 C CA  . GLN C 1 112 ? -5.47800  11.75400 -26.75900 1.000 30.32220 ? 111 GLN C CA  1 
ATOM   3140 C C   . GLN C 1 112 ? -5.61000  12.43800 -25.39900 1.000 29.71673 ? 111 GLN C C   1 
ATOM   3141 O O   . GLN C 1 112 ? -4.60700  12.68800 -24.72100 1.000 24.69125 ? 111 GLN C O   1 
ATOM   3142 C CB  . GLN C 1 112 ? -4.09300  12.02700 -27.35300 1.000 27.08208 ? 111 GLN C CB  1 
ATOM   3143 C CG  . GLN C 1 112 ? -3.83300  13.41900 -27.89400 1.000 24.05262 ? 111 GLN C CG  1 
ATOM   3144 C CD  . GLN C 1 112 ? -2.93800  13.39200 -29.14500 1.000 31.06009 ? 111 GLN C CD  1 
ATOM   3145 O OE1 . GLN C 1 112 ? -3.25400  12.72600 -30.13300 1.000 33.02118 ? 111 GLN C OE1 1 
ATOM   3146 N NE2 . GLN C 1 112 ? -1.83100  14.12500 -29.10600 1.000 29.88974 ? 111 GLN C NE2 1 
ATOM   3147 N N   . MET C 1 113 ? -6.84900  12.71500 -24.98100 1.000 28.02214 ? 112 MET C N   1 
ATOM   3148 C CA  . MET C 1 113 ? -7.13900  13.54500 -23.81500 1.000 25.88456 ? 112 MET C CA  1 
ATOM   3149 C C   . MET C 1 113 ? -8.20200  12.84900 -22.96800 1.000 27.80954 ? 112 MET C C   1 
ATOM   3150 O O   . MET C 1 113 ? -9.33600  12.64700 -23.42300 1.000 28.05117 ? 112 MET C O   1 
ATOM   3151 C CB  . MET C 1 113 ? -7.59700  14.93700 -24.27000 1.000 25.20524 ? 112 MET C CB  1 
ATOM   3152 C CG  . MET C 1 113 ? -6.49400  15.97100 -24.30400 1.000 30.14055 ? 112 MET C CG  1 
ATOM   3153 S SD  . MET C 1 113 ? -6.95800  17.56000 -25.02700 1.000 32.51718 ? 112 MET C SD  1 
ATOM   3154 C CE  . MET C 1 113 ? -6.98700  18.52700 -23.50600 1.000 21.10240 ? 112 MET C CE  1 
ATOM   3155 N N   . VAL C 1 114 ? -7.83300  12.47700 -21.74500 1.000 24.71825 ? 113 VAL C N   1 
ATOM   3156 C CA  . VAL C 1 114 ? -8.69100  11.72000 -20.83800 1.000 20.42835 ? 113 VAL C CA  1 
ATOM   3157 C C   . VAL C 1 114 ? -8.92300  12.56200 -19.59900 1.000 21.00077 ? 113 VAL C C   1 
ATOM   3158 O O   . VAL C 1 114 ? -7.96300  12.98600 -18.94600 1.000 27.06018 ? 113 VAL C O   1 
ATOM   3159 C CB  . VAL C 1 114 ? -8.06200  10.37300 -20.45800 1.000 24.06662 ? 113 VAL C CB  1 
ATOM   3160 C CG1 . VAL C 1 114 ? -8.73000  9.79600  -19.21700 1.000 24.52169 ? 113 VAL C CG1 1 
ATOM   3161 C CG2 . VAL C 1 114 ? -8.12200  9.38600  -21.63600 1.000 24.94818 ? 113 VAL C CG2 1 
ATOM   3162 N N   . GLU C 1 115 ? -10.18900 12.82200 -19.28100 1.000 28.75540 ? 114 GLU C N   1 
ATOM   3163 C CA  . GLU C 1 115 ? -10.58000 13.38100 -17.98900 1.000 25.44397 ? 114 GLU C CA  1 
ATOM   3164 C C   . GLU C 1 115 ? -11.51400 12.40000 -17.30800 1.000 26.87105 ? 114 GLU C C   1 
ATOM   3165 O O   . GLU C 1 115 ? -12.29200 11.71200 -17.97600 1.000 24.46630 ? 114 GLU C O   1 
ATOM   3166 C CB  . GLU C 1 115 ? -11.28000 14.73600 -18.12600 1.000 25.05678 ? 114 GLU C CB  1 
ATOM   3167 C CG  . GLU C 1 115 ? -10.43600 15.80700 -18.79000 1.000 25.44245 ? 114 GLU C CG  1 
ATOM   3168 C CD  . GLU C 1 115 ? -11.00000 17.17200 -18.56400 1.000 28.94392 ? 114 GLU C CD  1 
ATOM   3169 O OE1 . GLU C 1 115 ? -11.88200 17.28200 -17.68300 1.000 34.93355 ? 114 GLU C OE1 1 
ATOM   3170 O OE2 . GLU C 1 115 ? -10.57000 18.12500 -19.25000 1.000 28.23015 ? 114 GLU C OE2 1 
ATOM   3171 N N   . TYR C 1 116 ? -11.42600 12.32300 -15.98600 1.000 25.22612 ? 115 TYR C N   1 
ATOM   3172 C CA  . TYR C 1 116 ? -12.31500 11.46400 -15.22100 1.000 27.32100 ? 115 TYR C CA  1 
ATOM   3173 C C   . TYR C 1 116 ? -12.30100 10.04800 -15.78600 1.000 36.59821 ? 115 TYR C C   1 
ATOM   3174 O O   . TYR C 1 116 ? -13.29600 9.31900  -15.72200 1.000 38.85767 ? 115 TYR C O   1 
ATOM   3175 C CB  . TYR C 1 116 ? -13.74000 12.02200 -15.20000 1.000 28.48946 ? 115 TYR C CB  1 
ATOM   3176 C CG  . TYR C 1 116 ? -13.90000 13.34200 -14.47500 1.000 30.69914 ? 115 TYR C CG  1 
ATOM   3177 C CD1 . TYR C 1 116 ? -14.02500 13.38800 -13.08900 1.000 32.76418 ? 115 TYR C CD1 1 
ATOM   3178 C CD2 . TYR C 1 116 ? -13.95600 14.54400 -15.17800 1.000 31.72360 ? 115 TYR C CD2 1 
ATOM   3179 C CE1 . TYR C 1 116 ? -14.18000 14.59700 -12.42000 1.000 31.43132 ? 115 TYR C CE1 1 
ATOM   3180 C CE2 . TYR C 1 116 ? -14.11500 15.75500 -14.51900 1.000 31.79426 ? 115 TYR C CE2 1 
ATOM   3181 C CZ  . TYR C 1 116 ? -14.22300 15.77200 -13.14100 1.000 29.03527 ? 115 TYR C CZ  1 
ATOM   3182 O OH  . TYR C 1 116 ? -14.38100 16.96200 -12.48200 1.000 27.27801 ? 115 TYR C OH  1 
ATOM   3183 N N   . GLY C 1 117 ? -11.17700 9.66500  -16.38800 1.000 30.24505 ? 116 GLY C N   1 
ATOM   3184 C CA  . GLY C 1 117 ? -11.04800 8.33700  -16.93800 1.000 27.72469 ? 116 GLY C CA  1 
ATOM   3185 C C   . GLY C 1 117 ? -11.71300 8.12700  -18.27700 1.000 32.42853 ? 116 GLY C C   1 
ATOM   3186 O O   . GLY C 1 117 ? -11.80800 6.97400  -18.72800 1.000 27.22910 ? 116 GLY C O   1 
ATOM   3187 N N   . ARG C 1 118 ? -12.17100 9.19300  -18.94100 1.000 32.59587 ? 117 ARG C N   1 
ATOM   3188 C CA  . ARG C 1 118 ? -12.76400 9.05900  -20.27000 1.000 34.24231 ? 117 ARG C CA  1 
ATOM   3189 C C   . ARG C 1 118 ? -12.15200 10.06800 -21.22200 1.000 23.90339 ? 117 ARG C C   1 
ATOM   3190 O O   . ARG C 1 118 ? -11.89400 11.21400 -20.84600 1.000 22.58438 ? 117 ARG C O   1 
ATOM   3191 C CB  . ARG C 1 118 ? -14.30200 9.23400  -20.25300 1.000 26.97712 ? 117 ARG C CB  1 
ATOM   3192 C CG  . ARG C 1 118 ? -15.02800 8.20000  -19.39000 1.000 35.97542 ? 117 ARG C CG  1 
ATOM   3193 C CD  . ARG C 1 118 ? -15.18400 6.85900  -20.09600 1.000 40.52917 ? 117 ARG C CD  1 
ATOM   3194 N NE  . ARG C 1 118 ? -16.53300 6.66300  -20.62300 1.000 53.92671 ? 117 ARG C NE  1 
ATOM   3195 C CZ  . ARG C 1 118 ? -17.39100 5.74300  -20.19600 1.000 54.02288 ? 117 ARG C CZ  1 
ATOM   3196 N NH1 . ARG C 1 118 ? -17.06900 4.88000  -19.23800 1.000 44.37241 ? 117 ARG C NH1 1 
ATOM   3197 N NH2 . ARG C 1 118 ? -18.60300 5.68300  -20.74800 1.000 48.59338 ? 117 ARG C NH2 1 
ATOM   3198 N N   . PHE C 1 119 ? -11.92100 9.61800  -22.45300 1.000 27.67569 ? 118 PHE C N   1 
ATOM   3199 C CA  . PHE C 1 119 ? -11.56600 10.51300 -23.54800 1.000 25.65815 ? 118 PHE C CA  1 
ATOM   3200 C C   . PHE C 1 119 ? -12.60600 11.61100 -23.69700 1.000 25.15467 ? 118 PHE C C   1 
ATOM   3201 O O   . PHE C 1 119 ? -13.81600 11.35100 -23.65200 1.000 22.27486 ? 118 PHE C O   1 
ATOM   3202 C CB  . PHE C 1 119 ? -11.43300 9.71600  -24.84700 1.000 17.21941 ? 118 PHE C CB  1 
ATOM   3203 C CG  . PHE C 1 119 ? -10.30600 8.76900  -24.81100 1.000 19.05173 ? 118 PHE C CG  1 
ATOM   3204 C CD1 . PHE C 1 119 ? -9.04300  9.17400  -25.16700 1.000 21.10271 ? 118 PHE C CD1 1 
ATOM   3205 C CD2 . PHE C 1 119 ? -10.47600 7.50200  -24.30400 1.000 20.65446 ? 118 PHE C CD2 1 
ATOM   3206 C CE1 . PHE C 1 119 ? -7.98000  8.30000  -25.07900 1.000 24.46916 ? 118 PHE C CE1 1 
ATOM   3207 C CE2 . PHE C 1 119 ? -9.41300  6.63200  -24.20900 1.000 24.35861 ? 118 PHE C CE2 1 
ATOM   3208 C CZ  . PHE C 1 119 ? -8.16900  7.03000  -24.59700 1.000 19.63842 ? 118 PHE C CZ  1 
ATOM   3209 N N   . LEU C 1 120 ? -12.12400 12.84800 -23.84800 1.000 26.56675 ? 119 LEU C N   1 
ATOM   3210 C CA  . LEU C 1 120 ? -13.02100 13.97900 -24.03400 1.000 28.85100 ? 119 LEU C CA  1 
ATOM   3211 C C   . LEU C 1 120 ? -13.54700 14.02000 -25.45300 1.000 32.26482 ? 119 LEU C C   1 
ATOM   3212 O O   . LEU C 1 120 ? -12.91300 13.48800 -26.37200 1.000 30.70221 ? 119 LEU C O   1 
ATOM   3213 C CB  . LEU C 1 120 ? -12.32900 15.29800 -23.70500 1.000 28.77611 ? 119 LEU C CB  1 
ATOM   3214 C CG  . LEU C 1 120 ? -11.64100 15.31100 -22.35900 1.000 24.70113 ? 119 LEU C CG  1 
ATOM   3215 C CD1 . LEU C 1 120 ? -10.85900 16.61800 -22.14300 1.000 22.96066 ? 119 LEU C CD1 1 
ATOM   3216 C CD2 . LEU C 1 120 ? -12.72700 15.10000 -21.34100 1.000 24.88732 ? 119 LEU C CD2 1 
ATOM   3217 N N   . PRO C 1 121 ? -14.73300 14.64700 -25.65400 1.000 31.88972 ? 120 PRO C N   1 
ATOM   3218 C CA  . PRO C 1 121 ? -15.28800 14.78700 -27.00900 1.000 34.31332 ? 120 PRO C CA  1 
ATOM   3219 C C   . PRO C 1 121 ? -14.70300 15.97600 -27.76700 1.000 39.31723 ? 120 PRO C C   1 
ATOM   3220 O O   . PRO C 1 121 ? -13.70500 16.56700 -27.34700 1.000 41.76703 ? 120 PRO C O   1 
ATOM   3221 C CB  . PRO C 1 121 ? -16.78400 14.98200 -26.73800 1.000 32.74132 ? 120 PRO C CB  1 
ATOM   3222 C CG  . PRO C 1 121 ? -16.81800 15.68500 -25.41200 1.000 31.29006 ? 120 PRO C CG  1 
ATOM   3223 C CD  . PRO C 1 121 ? -15.63200 15.20900 -24.62700 1.000 25.46960 ? 120 PRO C CD  1 
ATOM   3224 N N   . GLN C 1 122 ? -15.32300 16.34200 -28.87100 1.000 43.34693 ? 121 GLN C N   1 
ATOM   3225 C CA  . GLN C 1 122 ? -14.97300 17.58000 -29.53900 1.000 41.47983 ? 121 GLN C CA  1 
ATOM   3226 C C   . GLN C 1 122 ? -15.56000 18.77900 -28.78900 1.000 48.15707 ? 121 GLN C C   1 
ATOM   3227 O O   . GLN C 1 122 ? -16.68500 18.70900 -28.29300 1.000 45.13905 ? 121 GLN C O   1 
ATOM   3228 C CB  . GLN C 1 122 ? -15.46700 17.56900 -30.97300 1.000 44.11957 ? 121 GLN C CB  1 
ATOM   3229 C CG  . GLN C 1 122 ? -14.87300 16.44100 -31.78600 1.000 45.98575 ? 121 GLN C CG  1 
ATOM   3230 C CD  . GLN C 1 122 ? -13.36100 16.51500 -31.83800 1.000 56.19540 ? 121 GLN C CD  1 
ATOM   3231 O OE1 . GLN C 1 122 ? -12.76900 17.60500 -31.84500 1.000 52.91700 ? 121 GLN C OE1 1 
ATOM   3232 N NE2 . GLN C 1 122 ? -12.71800 15.34700 -31.84900 1.000 48.93917 ? 121 GLN C NE2 1 
ATOM   3233 N N   . PRO C 1 123 ? -14.80100 19.87000 -28.66500 1.000 50.40114 ? 122 PRO C N   1 
ATOM   3234 C CA  . PRO C 1 123 ? -15.31700 21.08500 -28.01100 1.000 48.53764 ? 122 PRO C CA  1 
ATOM   3235 C C   . PRO C 1 123 ? -16.69800 21.45300 -28.54300 1.000 43.07085 ? 122 PRO C C   1 
ATOM   3236 O O   . PRO C 1 123 ? -16.89300 21.60300 -29.75500 1.000 42.32847 ? 122 PRO C O   1 
ATOM   3237 C CB  . PRO C 1 123 ? -14.28200 22.15300 -28.39700 1.000 34.22550 ? 122 PRO C CB  1 
ATOM   3238 C CG  . PRO C 1 123 ? -13.01900 21.39900 -28.73300 1.000 39.28748 ? 122 PRO C CG  1 
ATOM   3239 C CD  . PRO C 1 123 ? -13.33200 19.90600 -28.77300 1.000 50.23880 ? 122 PRO C CD  1 
ATOM   3240 N N   . GLY C 1 124 ? -17.66200 21.59900 -27.63900 1.000 35.79453 ? 123 GLY C N   1 
ATOM   3241 C CA  . GLY C 1 124 ? -19.02200 21.92100 -28.01200 1.000 40.24055 ? 123 GLY C CA  1 
ATOM   3242 C C   . GLY C 1 124 ? -19.97600 20.74800 -27.98100 1.000 40.24860 ? 123 GLY C C   1 
ATOM   3243 O O   . GLY C 1 124 ? -21.19600 20.95700 -27.96000 1.000 46.76384 ? 123 GLY C O   1 
ATOM   3244 N N   . HIS C 1 125 ? -19.44700 19.52400 -27.97200 1.000 46.28508 ? 124 HIS C N   1 
ATOM   3245 C CA  . HIS C 1 125 ? -20.23200 18.31000 -27.81500 1.000 42.43214 ? 124 HIS C CA  1 
ATOM   3246 C C   . HIS C 1 125 ? -20.31500 17.86000 -26.37100 1.000 39.06188 ? 124 HIS C C   1 
ATOM   3247 O O   . HIS C 1 125 ? -20.59800 16.68500 -26.11600 1.000 41.86412 ? 124 HIS C O   1 
ATOM   3248 C CB  . HIS C 1 125 ? -19.65800 17.18800 -28.68000 1.000 40.05448 ? 124 HIS C CB  1 
ATOM   3249 C CG  . HIS C 1 125 ? -19.65300 17.51100 -30.13800 1.000 47.07157 ? 124 HIS C CG  1 
ATOM   3250 N ND1 . HIS C 1 125 ? -20.24300 18.65000 -30.64400 1.000 43.49305 ? 124 HIS C ND1 1 
ATOM   3251 C CD2 . HIS C 1 125 ? -19.14800 16.84200 -31.20100 1.000 57.50464 ? 124 HIS C CD2 1 
ATOM   3252 C CE1 . HIS C 1 125 ? -20.09400 18.67400 -31.95600 1.000 50.12503 ? 124 HIS C CE1 1 
ATOM   3253 N NE2 . HIS C 1 125 ? -19.43600 17.58800 -32.32100 1.000 60.38046 ? 124 HIS C NE2 1 
ATOM   3254 N N   . GLU C 1 126 ? -20.08900 18.77300 -25.42500 1.000 33.11453 ? 125 GLU C N   1 
ATOM   3255 C CA  . GLU C 1 126 ? -20.11800 18.39800 -24.01800 1.000 42.75809 ? 125 GLU C CA  1 
ATOM   3256 C C   . GLU C 1 126 ? -21.45800 17.80100 -23.62100 1.000 43.81774 ? 125 GLU C C   1 
ATOM   3257 O O   . GLU C 1 126 ? -21.51000 16.91200 -22.76400 1.000 42.41977 ? 125 GLU C O   1 
ATOM   3258 C CB  . GLU C 1 126 ? -19.80400 19.61200 -23.15100 1.000 42.30887 ? 125 GLU C CB  1 
ATOM   3259 C CG  . GLU C 1 126 ? -18.36700 20.05900 -23.24600 1.000 46.03367 ? 125 GLU C CG  1 
ATOM   3260 C CD  . GLU C 1 126 ? -18.18300 21.13200 -24.29300 1.000 46.25617 ? 125 GLU C CD  1 
ATOM   3261 O OE1 . GLU C 1 126 ? -19.21600 21.68700 -24.73900 1.000 41.85992 ? 125 GLU C OE1 1 
ATOM   3262 O OE2 . GLU C 1 126 ? -17.01300 21.41300 -24.65700 1.000 43.81676 ? 125 GLU C OE2 1 
ATOM   3263 N N   . GLY C 1 127 ? -22.54200 18.26000 -24.23700 1.000 42.49153 ? 126 GLY C N   1 
ATOM   3264 C CA  . GLY C 1 127 ? -23.85800 17.78100 -23.88200 1.000 40.96784 ? 126 GLY C CA  1 
ATOM   3265 C C   . GLY C 1 127 ? -24.02800 16.29000 -24.07900 1.000 43.17096 ? 126 GLY C C   1 
ATOM   3266 O O   . GLY C 1 127 ? -24.32100 15.56700 -23.11900 1.000 43.62670 ? 126 GLY C O   1 
ATOM   3267 N N   . GLU C 1 128 ? -23.83600 15.81200 -25.31300 1.000 37.76895 ? 127 GLU C N   1 
ATOM   3268 C CA  . GLU C 1 128 ? -24.14500 14.41400 -25.59600 1.000 41.51583 ? 127 GLU C CA  1 
ATOM   3269 C C   . GLU C 1 128 ? -23.12400 13.47300 -24.96000 1.000 47.81819 ? 127 GLU C C   1 
ATOM   3270 O O   . GLU C 1 128 ? -23.48100 12.36500 -24.54000 1.000 45.11984 ? 127 GLU C O   1 
ATOM   3271 C CB  . GLU C 1 128 ? -24.22700 14.18200 -27.10900 1.000 44.95672 ? 127 GLU C CB  1 
ATOM   3272 C CG  . GLU C 1 128 ? -22.99900 13.50400 -27.72600 1.000 49.28728 ? 127 GLU C CG  1 
ATOM   3273 C CD  . GLU C 1 128 ? -23.06400 13.41000 -29.24000 1.000 62.86892 ? 127 GLU C CD  1 
ATOM   3274 O OE1 . GLU C 1 128 ? -23.15900 14.46800 -29.91100 1.000 59.28236 ? 127 GLU C OE1 1 
ATOM   3275 O OE2 . GLU C 1 128 ? -22.99900 12.27400 -29.75700 1.000 68.54256 ? 127 GLU C OE2 1 
ATOM   3276 N N   . TRP C 1 129 ? -21.85600 13.89600 -24.88200 1.000 43.35878 ? 128 TRP C N   1 
ATOM   3277 C CA  . TRP C 1 129 ? -20.85000 13.11700 -24.17600 1.000 36.94866 ? 128 TRP C CA  1 
ATOM   3278 C C   . TRP C 1 129 ? -21.24900 12.92800 -22.71400 1.000 44.17580 ? 128 TRP C C   1 
ATOM   3279 O O   . TRP C 1 129 ? -21.18600 11.81400 -22.17500 1.000 36.50226 ? 128 TRP C O   1 
ATOM   3280 C CB  . TRP C 1 129 ? -19.50400 13.81900 -24.30600 1.000 33.67604 ? 128 TRP C CB  1 
ATOM   3281 C CG  . TRP C 1 129 ? -18.36600 13.26100 -23.48100 1.000 34.72607 ? 128 TRP C CG  1 
ATOM   3282 C CD1 . TRP C 1 129 ? -17.47300 12.30000 -23.86200 1.000 32.22410 ? 128 TRP C CD1 1 
ATOM   3283 C CD2 . TRP C 1 129 ? -17.97200 13.67100 -22.16400 1.000 31.98225 ? 128 TRP C CD2 1 
ATOM   3284 N NE1 . TRP C 1 129 ? -16.55300 12.08000 -22.86300 1.000 31.63284 ? 128 TRP C NE1 1 
ATOM   3285 C CE2 . TRP C 1 129 ? -16.83600 12.91000 -21.81100 1.000 30.30798 ? 128 TRP C CE2 1 
ATOM   3286 C CE3 . TRP C 1 129 ? -18.46700 14.60400 -21.25000 1.000 31.54740 ? 128 TRP C CE3 1 
ATOM   3287 C CZ2 . TRP C 1 129 ? -16.19700 13.05000 -20.58900 1.000 24.71159 ? 128 TRP C CZ2 1 
ATOM   3288 C CZ3 . TRP C 1 129 ? -17.82600 14.74300 -20.03800 1.000 36.37242 ? 128 TRP C CZ3 1 
ATOM   3289 C CH2 . TRP C 1 129 ? -16.70300 13.97200 -19.71800 1.000 32.23230 ? 128 TRP C CH2 1 
ATOM   3290 N N   . PHE C 1 130 ? -21.68300 14.01200 -22.06300 1.000 40.04644 ? 129 PHE C N   1 
ATOM   3291 C CA  . PHE C 1 130 ? -22.26800 13.89800 -20.73400 1.000 38.07568 ? 129 PHE C CA  1 
ATOM   3292 C C   . PHE C 1 130 ? -23.44000 12.92200 -20.73900 1.000 49.25281 ? 129 PHE C C   1 
ATOM   3293 O O   . PHE C 1 130 ? -23.53400 12.04500 -19.87100 1.000 49.80403 ? 129 PHE C O   1 
ATOM   3294 C CB  . PHE C 1 130 ? -22.71700 15.27400 -20.24600 1.000 49.27996 ? 129 PHE C CB  1 
ATOM   3295 C CG  . PHE C 1 130 ? -23.05900 15.31800 -18.77900 1.000 48.29513 ? 129 PHE C CG  1 
ATOM   3296 C CD1 . PHE C 1 130 ? -22.08700 15.06200 -17.82200 1.000 41.41668 ? 129 PHE C CD1 1 
ATOM   3297 C CD2 . PHE C 1 130 ? -24.34500 15.62100 -18.36400 1.000 39.77657 ? 129 PHE C CD2 1 
ATOM   3298 C CE1 . PHE C 1 130 ? -22.39900 15.10200 -16.48100 1.000 53.23422 ? 129 PHE C CE1 1 
ATOM   3299 C CE2 . PHE C 1 130 ? -24.66300 15.66400 -17.02900 1.000 46.88746 ? 129 PHE C CE2 1 
ATOM   3300 C CZ  . PHE C 1 130 ? -23.69600 15.40600 -16.08000 1.000 50.77068 ? 129 PHE C CZ  1 
ATOM   3301 N N   . ASP C 1 131 ? -24.33700 13.04900 -21.72500 1.000 45.66280 ? 130 ASP C N   1 
ATOM   3302 C CA  . ASP C 1 131 ? -25.47100 12.14200 -21.88800 1.000 43.64856 ? 130 ASP C CA  1 
ATOM   3303 C C   . ASP C 1 131 ? -25.05000 10.79200 -22.45800 1.000 53.98071 ? 130 ASP C C   1 
ATOM   3304 O O   . ASP C 1 131 ? -25.71700 10.24300 -23.34700 1.000 55.50969 ? 130 ASP C O   1 
ATOM   3305 C CB  . ASP C 1 131 ? -26.52700 12.75800 -22.80700 1.000 45.15111 ? 130 ASP C CB  1 
ATOM   3306 C CG  . ASP C 1 131 ? -27.35600 13.80900 -22.11500 1.000 52.76499 ? 130 ASP C CG  1 
ATOM   3307 O OD1 . ASP C 1 131 ? -26.97500 14.22100 -20.99400 1.000 56.86919 ? 130 ASP C OD1 1 
ATOM   3308 O OD2 . ASP C 1 131 ? -28.39400 14.21500 -22.69000 1.000 54.01908 ? 130 ASP C OD2 1 
ATOM   3309 N N   . ASN C 1 132 ? -23.94100 10.25500 -21.96200 1.000 54.08068 ? 131 ASN C N   1 
ATOM   3310 C CA  . ASN C 1 132 ? -23.48400 8.93700  -22.37000 1.000 49.48720 ? 131 ASN C CA  1 
ATOM   3311 C C   . ASN C 1 132 ? -22.59400 8.35300  -21.29100 1.000 43.53080 ? 131 ASN C C   1 
ATOM   3312 O O   . ASN C 1 132 ? -22.06700 7.25000  -21.44600 1.000 44.99989 ? 131 ASN C O   1 
ATOM   3313 C CB  . ASN C 1 132 ? -22.74100 8.99300  -23.70400 1.000 49.18038 ? 131 ASN C CB  1 
ATOM   3314 C CG  . ASN C 1 132 ? -22.77700 7.67100  -24.42900 1.000 62.34152 ? 131 ASN C CG  1 
ATOM   3315 O OD1 . ASN C 1 132 ? -23.73600 6.90400  -24.29200 1.000 69.49914 ? 131 ASN C OD1 1 
ATOM   3316 N ND2 . ASN C 1 132 ? -21.71300 7.37200  -25.17600 1.000 56.35379 ? 131 ASN C ND2 1 
ATOM   3317 N N   . LEU C 1 133 ? -22.41300 9.09100  -20.20500 1.000 41.54540 ? 132 LEU C N   1 
ATOM   3318 C CA  . LEU C 1 133 ? -21.62700 8.60800  -19.08600 1.000 42.24089 ? 132 LEU C CA  1 
ATOM   3319 C C   . LEU C 1 133 ? -22.52600 7.89100  -18.09900 1.000 39.53723 ? 132 LEU C C   1 
ATOM   3320 O O   . LEU C 1 133 ? -23.67900 8.27700  -17.89900 1.000 44.03693 ? 132 LEU C O   1 
ATOM   3321 C CB  . LEU C 1 133 ? -20.89200 9.75700  -18.39500 1.000 41.01789 ? 132 LEU C CB  1 
ATOM   3322 C CG  . LEU C 1 133 ? -19.81200 10.42800 -19.25100 1.000 38.06223 ? 132 LEU C CG  1 
ATOM   3323 C CD1 . LEU C 1 133 ? -19.65400 11.87000 -18.85600 1.000 39.34115 ? 132 LEU C CD1 1 
ATOM   3324 C CD2 . LEU C 1 133 ? -18.46800 9.70500  -19.15500 1.000 37.19477 ? 132 LEU C CD2 1 
ATOM   3325 N N   . SER C 1 134 ? -21.98600 6.84000  -17.48600 1.000 34.62967 ? 133 SER C N   1 
ATOM   3326 C CA  . SER C 1 134 ? -22.74100 6.06600  -16.52000 1.000 33.13194 ? 133 SER C CA  1 
ATOM   3327 C C   . SER C 1 134 ? -23.27900 6.96600  -15.40900 1.000 35.83413 ? 133 SER C C   1 
ATOM   3328 O O   . SER C 1 134 ? -22.75900 8.04500  -15.13500 1.000 37.74595 ? 133 SER C O   1 
ATOM   3329 C CB  . SER C 1 134 ? -21.87000 4.96400  -15.92900 1.000 39.83983 ? 133 SER C CB  1 
ATOM   3330 O OG  . SER C 1 134 ? -20.71700 5.49000  -15.30500 1.000 42.07072 ? 133 SER C OG  1 
ATOM   3331 N N   . SER C 1 135 ? -24.36200 6.51400  -14.78500 1.000 35.14723 ? 134 SER C N   1 
ATOM   3332 C CA  . SER C 1 135 ? -24.98600 7.29700  -13.72600 1.000 38.01223 ? 134 SER C CA  1 
ATOM   3333 C C   . SER C 1 135 ? -23.99000 7.64100  -12.61700 1.000 37.53960 ? 134 SER C C   1 
ATOM   3334 O O   . SER C 1 135 ? -24.04200 8.73700  -12.04600 1.000 36.94192 ? 134 SER C O   1 
ATOM   3335 C CB  . SER C 1 135 ? -26.18700 6.53600  -13.16000 1.000 33.74020 ? 134 SER C CB  1 
ATOM   3336 O OG  . SER C 1 135 ? -27.10000 6.19700  -14.18400 1.000 28.87678 ? 134 SER C OG  1 
ATOM   3337 N N   . ASP C 1 136 ? -23.07400 6.72000  -12.30300 1.000 37.96646 ? 135 ASP C N   1 
ATOM   3338 C CA  . ASP C 1 136 ? -22.07800 6.98600  -11.26600 1.000 38.63497 ? 135 ASP C CA  1 
ATOM   3339 C C   . ASP C 1 136 ? -21.11100 8.07500  -11.69200 1.000 38.27249 ? 135 ASP C C   1 
ATOM   3340 O O   . ASP C 1 136 ? -20.83200 9.00300  -10.92000 1.000 37.80732 ? 135 ASP C O   1 
ATOM   3341 C CB  . ASP C 1 136 ? -21.30700 5.71500  -10.89500 1.000 37.23405 ? 135 ASP C CB  1 
ATOM   3342 C CG  . ASP C 1 136 ? -22.18700 4.68300  -10.18400 1.000 54.72363 ? 135 ASP C CG  1 
ATOM   3343 O OD1 . ASP C 1 136 ? -23.26400 5.07000  -9.65400  1.000 46.19997 ? 135 ASP C OD1 1 
ATOM   3344 O OD2 . ASP C 1 136 ? -21.77500 3.49700  -10.11100 1.000 58.41600 ? 135 ASP C OD2 1 
ATOM   3345 N N   . GLU C 1 137 ? -20.57100 7.96500  -12.91000 1.000 38.32624 ? 136 GLU C N   1 
ATOM   3346 C CA  . GLU C 1 137 ? -19.71500 9.01900  -13.44500 1.000 36.75674 ? 136 GLU C CA  1 
ATOM   3347 C C   . GLU C 1 137 ? -20.45500 10.35200 -13.46600 1.000 38.15091 ? 136 GLU C C   1 
ATOM   3348 O O   . GLU C 1 137 ? -19.91800 11.37700 -13.02800 1.000 38.67470 ? 136 GLU C O   1 
ATOM   3349 C CB  . GLU C 1 137 ? -19.22600 8.64100  -14.84500 1.000 38.06302 ? 136 GLU C CB  1 
ATOM   3350 C CG  . GLU C 1 137 ? -18.05700 7.66800  -14.86200 1.000 40.30884 ? 136 GLU C CG  1 
ATOM   3351 C CD  . GLU C 1 137 ? -17.89500 6.93000  -16.19600 1.000 42.55701 ? 136 GLU C CD  1 
ATOM   3352 O OE1 . GLU C 1 137 ? -18.51000 5.85900  -16.38500 1.000 43.57894 ? 136 GLU C OE1 1 
ATOM   3353 O OE2 . GLU C 1 137 ? -17.13000 7.41200  -17.05500 1.000 42.38783 ? 136 GLU C OE2 1 
ATOM   3354 N N   . ARG C 1 138 ? -21.70300 10.34900 -13.95300 1.000 38.49943 ? 137 ARG C N   1 
ATOM   3355 C CA  . ARG C 1 138 ? -22.50500 11.57000 -13.99300 1.000 36.72640 ? 137 ARG C CA  1 
ATOM   3356 C C   . ARG C 1 138 ? -22.62900 12.17700 -12.60600 1.000 42.67336 ? 137 ARG C C   1 
ATOM   3357 O O   . ARG C 1 138 ? -22.43500 13.38300 -12.41800 1.000 41.56986 ? 137 ARG C O   1 
ATOM   3358 C CB  . ARG C 1 138 ? -23.89200 11.27300 -14.56400 1.000 43.32847 ? 137 ARG C CB  1 
ATOM   3359 C CG  . ARG C 1 138 ? -24.08400 11.55000 -16.06500 1.000 49.26082 ? 137 ARG C CG  1 
ATOM   3360 C CD  . ARG C 1 138 ? -25.43700 10.97000 -16.55100 1.000 59.19633 ? 137 ARG C CD  1 
ATOM   3361 N NE  . ARG C 1 138 ? -26.06800 11.73900 -17.62100 1.000 58.91390 ? 137 ARG C NE  1 
ATOM   3362 C CZ  . ARG C 1 138 ? -26.96000 12.70500 -17.44100 1.000 63.12524 ? 137 ARG C CZ  1 
ATOM   3363 N NH1 . ARG C 1 138 ? -27.37000 13.05300 -16.23100 1.000 65.03450 ? 137 ARG C NH1 1 
ATOM   3364 N NH2 . ARG C 1 138 ? -27.46000 13.33600 -18.50500 1.000 58.04378 ? 137 ARG C NH2 1 
ATOM   3365 N N   . ALA C 1 139 ? -22.94600 11.34300 -11.61500 1.000 42.79991 ? 138 ALA C N   1 
ATOM   3366 C CA  . ALA C 1 139 ? -23.02200 11.82400 -10.24500 1.000 37.20804 ? 138 ALA C CA  1 
ATOM   3367 C C   . ALA C 1 139 ? -21.66800 12.32200 -9.76600  1.000 36.33380 ? 138 ALA C C   1 
ATOM   3368 O O   . ALA C 1 139 ? -21.58000 13.37300 -9.12300  1.000 46.58221 ? 138 ALA C O   1 
ATOM   3369 C CB  . ALA C 1 139 ? -23.54800 10.71900 -9.32700  1.000 33.69893 ? 138 ALA C CB  1 
ATOM   3370 N N   . PHE C 1 140 ? -20.59600 11.59700 -10.08200 1.000 34.96159 ? 139 PHE C N   1 
ATOM   3371 C CA  . PHE C 1 140 ? -19.28600 11.99100 -9.57400  1.000 39.98949 ? 139 PHE C CA  1 
ATOM   3372 C C   . PHE C 1 140 ? -18.90000 13.39300 -10.04200 1.000 40.51867 ? 139 PHE C C   1 
ATOM   3373 O O   . PHE C 1 140 ? -18.51600 14.24500 -9.23400  1.000 41.35223 ? 139 PHE C O   1 
ATOM   3374 C CB  . PHE C 1 140 ? -18.21400 10.97800 -9.97900  1.000 32.36570 ? 139 PHE C CB  1 
ATOM   3375 C CG  . PHE C 1 140 ? -16.84700 11.32400 -9.45000  1.000 35.77929 ? 139 PHE C CG  1 
ATOM   3376 C CD1 . PHE C 1 140 ? -16.60300 11.33600 -8.07700  1.000 35.00567 ? 139 PHE C CD1 1 
ATOM   3377 C CD2 . PHE C 1 140 ? -15.81600 11.66700 -10.31400 1.000 33.87391 ? 139 PHE C CD2 1 
ATOM   3378 C CE1 . PHE C 1 140 ? -15.36200 11.66900 -7.57900  1.000 33.95997 ? 139 PHE C CE1 1 
ATOM   3379 C CE2 . PHE C 1 140 ? -14.56000 11.99800 -9.82400  1.000 37.66637 ? 139 PHE C CE2 1 
ATOM   3380 C CZ  . PHE C 1 140 ? -14.33000 11.99700 -8.45300  1.000 40.30413 ? 139 PHE C CZ  1 
ATOM   3381 N N   . MET C 1 141 ? -18.99000 13.65300 -11.34700 1.000 42.36206 ? 140 MET C N   1 
ATOM   3382 C CA  . MET C 1 141 ? -18.54300 14.94200 -11.85900 1.000 38.14258 ? 140 MET C CA  1 
ATOM   3383 C C   . MET C 1 141 ? -19.40600 16.07300 -11.32500 1.000 40.84398 ? 140 MET C C   1 
ATOM   3384 O O   . MET C 1 141 ? -18.88400 17.10600 -10.88800 1.000 41.25042 ? 140 MET C O   1 
ATOM   3385 C CB  . MET C 1 141 ? -18.55400 14.94800 -13.38300 1.000 39.53344 ? 140 MET C CB  1 
ATOM   3386 C CG  . MET C 1 141 ? -18.02200 13.71600 -14.00300 1.000 35.75476 ? 140 MET C CG  1 
ATOM   3387 S SD  . MET C 1 141 ? -18.54100 13.68500 -15.71100 1.000 44.90061 ? 140 MET C SD  1 
ATOM   3388 C CE  . MET C 1 141 ? -17.26700 12.61700 -16.39000 1.000 39.98386 ? 140 MET C CE  1 
ATOM   3389 N N   . GLU C 1 142 ? -20.73600 15.89700 -11.36500 1.000 42.65502 ? 141 GLU C N   1 
ATOM   3390 C CA  . GLU C 1 142 ? -21.66300 16.89400 -10.83800 1.000 41.50745 ? 141 GLU C CA  1 
ATOM   3391 C C   . GLU C 1 142 ? -21.30300 17.32600 -9.42000  1.000 47.20623 ? 141 GLU C C   1 
ATOM   3392 O O   . GLU C 1 142 ? -21.67100 18.43100 -9.00200  1.000 51.00838 ? 141 GLU C O   1 
ATOM   3393 C CB  . GLU C 1 142 ? -23.08800 16.34400 -10.87000 1.000 46.71092 ? 141 GLU C CB  1 
ATOM   3394 C CG  . GLU C 1 142 ? -23.83500 16.54800 -12.19000 1.000 51.24166 ? 141 GLU C CG  1 
ATOM   3395 C CD  . GLU C 1 142 ? -24.93800 15.49800 -12.42900 1.000 63.24004 ? 141 GLU C CD  1 
ATOM   3396 O OE1 . GLU C 1 142 ? -25.10800 14.57700 -11.58500 1.000 56.04267 ? 141 GLU C OE1 1 
ATOM   3397 O OE2 . GLU C 1 142 ? -25.64900 15.60600 -13.45800 1.000 64.85156 ? 141 GLU C OE2 1 
ATOM   3398 N N   . THR C 1 143 ? -20.57600 16.48600 -8.67700  1.000 40.60814 ? 142 THR C N   1 
ATOM   3399 C CA  . THR C 1 143 ? -20.07600 16.89000 -7.36600  1.000 50.68584 ? 142 THR C CA  1 
ATOM   3400 C C   . THR C 1 143 ? -19.12500 18.09100 -7.46900  1.000 46.55969 ? 142 THR C C   1 
ATOM   3401 O O   . THR C 1 143 ? -19.17100 19.00600 -6.63500  1.000 43.28815 ? 142 THR C O   1 
ATOM   3402 C CB  . THR C 1 143 ? -19.38800 15.69200 -6.69100  1.000 53.30867 ? 142 THR C CB  1 
ATOM   3403 O OG1 . THR C 1 143 ? -20.37600 14.78400 -6.16800  1.000 36.45926 ? 142 THR C OG1 1 
ATOM   3404 C CG2 . THR C 1 143 ? -18.44300 16.14200 -5.57000  1.000 45.43951 ? 142 THR C CG2 1 
ATOM   3405 N N   . ASN C 1 144 ? -18.26900 18.12100 -8.48900  1.000 40.54378 ? 143 ASN C N   1 
ATOM   3406 C CA  . ASN C 1 144 ? -17.23800 19.16000 -8.58100  1.000 42.46288 ? 143 ASN C CA  1 
ATOM   3407 C C   . ASN C 1 144 ? -17.71100 20.33800 -9.43800  1.000 41.01333 ? 143 ASN C C   1 
ATOM   3408 O O   . ASN C 1 144 ? -17.18700 20.62200 -10.51700 1.000 39.23948 ? 143 ASN C O   1 
ATOM   3409 C CB  . ASN C 1 144 ? -15.94800 18.56400 -9.11600  1.000 34.21063 ? 143 ASN C CB  1 
ATOM   3410 C CG  . ASN C 1 144 ? -15.42000 17.47100 -8.22300  1.000 39.85014 ? 143 ASN C CG  1 
ATOM   3411 O OD1 . ASN C 1 144 ? -15.37200 17.62500 -6.99000  1.000 36.07509 ? 143 ASN C OD1 1 
ATOM   3412 N ND2 . ASN C 1 144 ? -15.03900 16.34400 -8.82800  1.000 35.32289 ? 143 ASN C ND2 1 
ATOM   3413 N N   . VAL C 1 145 ? -18.74000 21.02500 -8.93200  1.000 41.87337 ? 144 VAL C N   1 
ATOM   3414 C CA  . VAL C 1 145 ? -19.21200 22.28300 -9.50500  1.000 39.54592 ? 144 VAL C CA  1 
ATOM   3415 C C   . VAL C 1 145 ? -19.48200 23.25600 -8.36000  1.000 43.13449 ? 144 VAL C C   1 
ATOM   3416 O O   . VAL C 1 145 ? -20.02000 22.87700 -7.31400  1.000 43.11793 ? 144 VAL C O   1 
ATOM   3417 C CB  . VAL C 1 145 ? -20.46600 22.09300 -10.40100 1.000 45.55226 ? 144 VAL C CB  1 
ATOM   3418 C CG1 . VAL C 1 145 ? -20.61700 20.63400 -10.86300 1.000 38.56790 ? 144 VAL C CG1 1 
ATOM   3419 C CG2 . VAL C 1 145 ? -21.75500 22.60900 -9.72700  1.000 43.03262 ? 144 VAL C CG2 1 
ATOM   3420 N N   . ASP C 1 146 ? -19.08000 24.50900 -8.54800  1.000 51.39334 ? 145 ASP C N   1 
ATOM   3421 C CA  . ASP C 1 146 ? -19.29400 25.55000 -7.54800  1.000 46.96425 ? 145 ASP C CA  1 
ATOM   3422 C C   . ASP C 1 146 ? -19.89700 26.79400 -8.21000  1.000 39.10518 ? 145 ASP C C   1 
ATOM   3423 O O   . ASP C 1 146 ? -21.03900 27.16300 -7.94800  1.000 37.72332 ? 145 ASP C O   1 
ATOM   3424 C CB  . ASP C 1 146 ? -17.97100 25.89000 -6.83900  1.000 49.94971 ? 145 ASP C CB  1 
ATOM   3425 C CG  . ASP C 1 146 ? -17.97200 27.29000 -6.20800  1.000 61.65304 ? 145 ASP C CG  1 
ATOM   3426 O OD1 . ASP C 1 146 ? -18.90200 27.61000 -5.42800  1.000 73.63346 ? 145 ASP C OD1 1 
ATOM   3427 O OD2 . ASP C 1 146 ? -17.04800 28.08000 -6.50700  1.000 51.55376 ? 145 ASP C OD2 1 
HETATM 3428 S S   . SO4 D 2 .   ? 8.29300   9.20900  -27.46900 1.000 47.01864 ? 201 SO4 A S   1 
HETATM 3429 O O1  . SO4 D 2 .   ? 9.52500   9.93100  -27.09100 1.000 37.39707 ? 201 SO4 A O1  1 
HETATM 3430 O O2  . SO4 D 2 .   ? 7.76100   9.70100  -28.74600 1.000 33.50120 ? 201 SO4 A O2  1 
HETATM 3431 O O3  . SO4 D 2 .   ? 8.57100   7.77500  -27.58100 1.000 37.48610 ? 201 SO4 A O3  1 
HETATM 3432 O O4  . SO4 D 2 .   ? 7.31100   9.43400  -26.41000 1.000 40.48246 ? 201 SO4 A O4  1 
HETATM 3433 S S   . SO4 E 2 .   ? 9.73900   32.95300 -27.70100 1.000 40.32162 ? 201 SO4 B S   1 
HETATM 3434 O O1  . SO4 E 2 .   ? 10.82800  33.91000 -27.90500 1.000 33.99863 ? 201 SO4 B O1  1 
HETATM 3435 O O2  . SO4 E 2 .   ? 9.13300   32.62500 -28.99500 1.000 34.33175 ? 201 SO4 B O2  1 
HETATM 3436 O O3  . SO4 E 2 .   ? 10.26900  31.72500 -27.13300 1.000 33.93835 ? 201 SO4 B O3  1 
HETATM 3437 O O4  . SO4 E 2 .   ? 8.76000   33.53600 -26.77900 1.000 28.77857 ? 201 SO4 B O4  1 
HETATM 3438 S S   . SO4 F 2 .   ? -11.34800 22.38600 -23.16300 1.000 41.73417 ? 201 SO4 C S   1 
HETATM 3439 O O1  . SO4 F 2 .   ? -10.84100 22.43500 -24.52800 1.000 34.59746 ? 201 SO4 C O1  1 
HETATM 3440 O O2  . SO4 F 2 .   ? -11.30500 20.99600 -22.68900 1.000 36.48292 ? 201 SO4 C O2  1 
HETATM 3441 O O3  . SO4 F 2 .   ? -10.46400 23.16200 -22.30900 1.000 38.11481 ? 201 SO4 C O3  1 
HETATM 3442 O O4  . SO4 F 2 .   ? -12.69100 22.96800 -23.13700 1.000 29.37161 ? 201 SO4 C O4  1 
HETATM 3443 O O   . HOH G 3 .   ? 7.43500   1.98100  -0.01700  1.000 39.55129 ? 301 HOH A O   1 
HETATM 3444 O O   . HOH G 3 .   ? 31.78200  4.41100  -18.87800 1.000 35.88279 ? 302 HOH A O   1 
HETATM 3445 O O   . HOH G 3 .   ? 7.56000   4.94400  -30.86000 1.000 37.97933 ? 303 HOH A O   1 
HETATM 3446 O O   . HOH G 3 .   ? 14.39200  -0.25000 -9.76700  1.000 33.11508 ? 304 HOH A O   1 
HETATM 3447 O O   . HOH G 3 .   ? 6.364     20.815   -8.611    1.000 32.65940 ? 305 HOH A O   1 
HETATM 3448 O O   . HOH G 3 .   ? -2.78400  12.30100 -5.85300  1.000 32.23876 ? 306 HOH A O   1 
HETATM 3449 O O   . HOH G 3 .   ? -11.37900 -3.10200 -14.59900 1.000 23.84714 ? 307 HOH A O   1 
HETATM 3450 O O   . HOH G 3 .   ? 2.59000   11.19500 -3.52600  1.000 25.95356 ? 308 HOH A O   1 
HETATM 3451 O O   . HOH G 3 .   ? 22.24000  14.19000 -31.22000 1.000 32.60656 ? 309 HOH A O   1 
HETATM 3452 O O   . HOH G 3 .   ? 3.72500   0.00000  0.00000   0.50  28.13892 ? 310 HOH A O   1 
HETATM 3453 O O   . HOH G 3 .   ? 4.97300   21.43100 -31.37400 1.000 29.46134 ? 311 HOH A O   1 
HETATM 3454 O O   . HOH H 3 .   ? 0.140     33.377   -32.979   1.000 33.14446 ? 301 HOH B O   1 
HETATM 3455 O O   . HOH H 3 .   ? 27.21100  21.09000 -28.46400 1.000 34.10421 ? 302 HOH B O   1 
HETATM 3456 O O   . HOH H 3 .   ? 0.05400   49.89600 -26.11500 1.000 43.31176 ? 303 HOH B O   1 
HETATM 3457 O O   . HOH H 3 .   ? 24.55500  30.79400 -23.05100 1.000 31.04672 ? 304 HOH B O   1 
HETATM 3458 O O   . HOH H 3 .   ? 17.99200  17.87900 -10.27200 1.000 24.26193 ? 305 HOH B O   1 
HETATM 3459 O O   . HOH H 3 .   ? 9.15300   28.70300 -33.51600 1.000 25.62968 ? 306 HOH B O   1 
HETATM 3460 O O   . HOH H 3 .   ? -4.550    31.129   -31.484   1.000 24.34321 ? 307 HOH B O   1 
HETATM 3461 O O   . HOH H 3 .   ? 10.75500  19.12000 -0.58400  1.000 38.19721 ? 308 HOH B O   1 
HETATM 3462 O O   . HOH H 3 .   ? 0.85200   53.38000 -17.02200 1.000 40.81800 ? 309 HOH B O   1 
HETATM 3463 O O   . HOH H 3 .   ? 4.876     21.480   -14.441   1.000 21.40057 ? 310 HOH B O   1 
HETATM 3464 O O   . HOH H 3 .   ? 14.35300  21.65300 -34.39700 1.000 25.67248 ? 311 HOH B O   1 
HETATM 3465 O O   . HOH H 3 .   ? 3.26300   32.52100 -33.16600 1.000 21.47803 ? 312 HOH B O   1 
HETATM 3466 O O   . HOH H 3 .   ? 17.83600  22.54600 -7.06300  1.000 33.06176 ? 313 HOH B O   1 
HETATM 3467 O O   . HOH H 3 .   ? 13.86300  14.93400 -7.87300  1.000 27.00714 ? 314 HOH B O   1 
HETATM 3468 O O   . HOH H 3 .   ? -4.58900  37.15500 -29.51400 1.000 33.91260 ? 315 HOH B O   1 
HETATM 3469 O O   . HOH H 3 .   ? 5.70100   21.45800 -11.66300 1.000 19.84613 ? 316 HOH B O   1 
HETATM 3470 O O   . HOH H 3 .   ? 10.88200  18.61500 -10.46900 1.000 17.58172 ? 317 HOH B O   1 
HETATM 3471 O O   . HOH H 3 .   ? 1.87200   40.54900 -34.06000 1.000 31.75996 ? 318 HOH B O   1 
HETATM 3472 O O   . HOH H 3 .   ? 14.63100  26.40300 -2.56500  1.000 32.23314 ? 319 HOH B O   1 
HETATM 3473 O O   . HOH H 3 .   ? 7.712     29.329   -9.353    1.000 26.62320 ? 320 HOH B O   1 
HETATM 3474 O O   . HOH H 3 .   ? -2.208    42.623   -25.435   1.000 24.79923 ? 321 HOH B O   1 
HETATM 3475 O O   . HOH H 3 .   ? 19.07800  25.89200 -2.85900  1.000 29.91696 ? 322 HOH B O   1 
HETATM 3476 O O   . HOH H 3 .   ? -0.751    38.371   -31.295   1.000 25.22185 ? 323 HOH B O   1 
HETATM 3477 O O   . HOH H 3 .   ? 11.687    37.782   -37.845   1.000 45.06211 ? 324 HOH B O   1 
HETATM 3478 O O   . HOH H 3 .   ? -3.93100  31.51100 -33.70600 1.000 24.01292 ? 325 HOH B O   1 
HETATM 3479 O O   . HOH H 3 .   ? 12.92300  33.09000 -35.91100 1.000 23.83032 ? 326 HOH B O   1 
HETATM 3480 O O   . HOH H 3 .   ? 7.66000   38.76700 -39.16800 1.000 63.11466 ? 327 HOH B O   1 
HETATM 3481 O O   . HOH I 3 .   ? -22.40800 28.92400 -7.87300  1.000 36.30720 ? 301 HOH C O   1 
HETATM 3482 O O   . HOH I 3 .   ? 3.74300   46.02100 -9.58000  1.000 50.60115 ? 302 HOH C O   1 
HETATM 3483 O O   . HOH I 3 .   ? -4.71700  11.89900 -31.85800 1.000 27.43808 ? 303 HOH C O   1 
HETATM 3484 O O   . HOH I 3 .   ? -2.94300  35.56100 -1.26000  1.000 23.82498 ? 304 HOH C O   1 
HETATM 3485 O O   . HOH I 3 .   ? -12.82500 33.99600 -7.89700  1.000 31.51729 ? 305 HOH C O   1 
HETATM 3486 O O   . HOH I 3 .   ? 5.67600   39.56800 -15.25600 1.000 27.71750 ? 306 HOH C O   1 
HETATM 3487 O O   . HOH I 3 .   ? -1.56500  20.72700 -7.38900  1.000 30.30776 ? 307 HOH C O   1 
HETATM 3488 O O   . HOH I 3 .   ? 3.14400   33.47200 -7.07400  1.000 16.72539 ? 308 HOH C O   1 
HETATM 3489 O O   . HOH I 3 .   ? 7.91900   30.44100 -7.10100  1.000 25.27728 ? 309 HOH C O   1 
HETATM 3490 O O   . HOH I 3 .   ? 16.22600  35.29000 -2.76500  1.000 29.71487 ? 310 HOH C O   1 
HETATM 3491 O O   . HOH I 3 .   ? -8.92200  25.18800 -29.24000 1.000 20.62374 ? 311 HOH C O   1 
HETATM 3492 O O   . HOH I 3 .   ? -6.87700  43.67900 -14.05500 1.000 38.62232 ? 312 HOH C O   1 
HETATM 3493 O O   . HOH I 3 .   ? 0.94800   18.35900 -8.16300  1.000 27.05382 ? 313 HOH C O   1 
HETATM 3494 O O   . HOH I 3 .   ? -26.41200 10.38100 -11.82600 1.000 26.58550 ? 314 HOH C O   1 
HETATM 3495 O O   . HOH I 3 .   ? -14.18700 28.89500 -30.93800 1.000 27.08241 ? 315 HOH C O   1 
HETATM 3496 O O   . HOH I 3 .   ? 6.90200   34.03400 -8.73300  1.000 27.84355 ? 316 HOH C O   1 
HETATM 3497 O O   . HOH I 3 .   ? -24.43500 18.97100 -18.56800 1.000 34.34948 ? 317 HOH C O   1 
HETATM 3498 O O   . HOH I 3 .   ? -9.05100  25.83300 -26.91000 1.000 24.89343 ? 318 HOH C O   1 
HETATM 3499 O O   . HOH I 3 .   ? 6.30800   39.26000 -12.59900 1.000 31.60617 ? 319 HOH C O   1 
HETATM 3500 O O   . HOH I 3 .   ? -4.61700  29.19200 -34.27500 1.000 22.26623 ? 320 HOH C O   1 
HETATM 3501 O O   . HOH I 3 .   ? -23.97100 20.26800 -16.26400 1.000 34.72292 ? 321 HOH C O   1 
# 
