data_9CS9
# 
_entry.id   9CS9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9CS9         pdb_00009cs9 10.2210/pdb9cs9/pdb 
WWPDB D_1000286231 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_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                        9CS9 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-23 
_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 mohi@umich.edu     Melanie Ohi   D. 'principal investigator/group leader' 0000-0003-1750-4793 
3 janetsmi@umich.edu Janet   Smith L. 'principal investigator/group leader' 0000-0002-0664-9228 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yeoh, Z.C.'  1 0000-0002-2694-9068 
'Ohi, M.D.'   2 0000-0003-1750-4793 
'Smith, J.L.' 3 0000-0002-0664-9228 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            121 
_citation.language                  ? 
_citation.page_first                e2415048121 
_citation.page_last                 e2415048121 
_citation.title                     
'A minimal complex of KHNYN and zinc-finger antiviral protein binds and degrades single-stranded RNA.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2415048121 
_citation.pdbx_database_id_PubMed   39693345 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yeoh, Z.C.'     1 0000-0002-2694-9068 
primary 'Meagher, J.L.'  2 0000-0003-1250-4575 
primary 'Kang, C.Y.'     3 ?                   
primary 'Bieniasz, P.D.' 4 0000-0002-2368-3719 
primary 'Smith, J.L.'    5 0000-0002-0664-9228 
primary 'Ohi, M.D.'      6 0000-0003-1750-4793 
# 
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 'Protein KHNYN' 20752.457 2  ? ? 'KH1 and KH2 domains' ? 
2 non-polymer syn 'SULFATE ION'   96.063    4  ? ? ?                     ? 
3 water       nat water           18.015    45 ? ? ?                     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'KH and NYN domain-containing protein' 
# 
_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       
;SNADRFAVSAEAENKVREQQPHVERIFSVGVSVLPKDCPDNPHIWLQLEGPKENASRAKEYLKGLCSPELQDEIHYPPKL
HCIFLGAQGFFLDCLAWSTSAHLVPRAPGSLMISGLTEAFVMAQSRVEELAERLSWDFTPGPSSGASQCTGVLRDFSALL
QSPGDAHREALLQLPLAVQEELLSLVQEA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNADRFAVSAEAENKVREQQPHVERIFSVGVSVLPKDCPDNPHIWLQLEGPKENASRAKEYLKGLCSPELQDEIHYPPKL
HCIFLGAQGFFLDCLAWSTSAHLVPRAPGSLMISGLTEAFVMAQSRVEELAERLSWDFTPGPSSGASQCTGVLRDFSALL
QSPGDAHREALLQLPLAVQEELLSLVQEA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '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   SER n 
1 2   ASN n 
1 3   ALA n 
1 4   ASP n 
1 5   ARG n 
1 6   PHE n 
1 7   ALA n 
1 8   VAL n 
1 9   SER n 
1 10  ALA n 
1 11  GLU n 
1 12  ALA n 
1 13  GLU n 
1 14  ASN n 
1 15  LYS n 
1 16  VAL n 
1 17  ARG n 
1 18  GLU n 
1 19  GLN n 
1 20  GLN n 
1 21  PRO n 
1 22  HIS n 
1 23  VAL n 
1 24  GLU n 
1 25  ARG n 
1 26  ILE n 
1 27  PHE n 
1 28  SER n 
1 29  VAL n 
1 30  GLY n 
1 31  VAL n 
1 32  SER n 
1 33  VAL n 
1 34  LEU n 
1 35  PRO n 
1 36  LYS n 
1 37  ASP n 
1 38  CYS n 
1 39  PRO n 
1 40  ASP n 
1 41  ASN n 
1 42  PRO n 
1 43  HIS n 
1 44  ILE n 
1 45  TRP n 
1 46  LEU n 
1 47  GLN n 
1 48  LEU n 
1 49  GLU n 
1 50  GLY n 
1 51  PRO n 
1 52  LYS n 
1 53  GLU n 
1 54  ASN n 
1 55  ALA n 
1 56  SER n 
1 57  ARG n 
1 58  ALA n 
1 59  LYS n 
1 60  GLU n 
1 61  TYR n 
1 62  LEU n 
1 63  LYS n 
1 64  GLY n 
1 65  LEU n 
1 66  CYS n 
1 67  SER n 
1 68  PRO n 
1 69  GLU n 
1 70  LEU n 
1 71  GLN n 
1 72  ASP n 
1 73  GLU n 
1 74  ILE n 
1 75  HIS n 
1 76  TYR n 
1 77  PRO n 
1 78  PRO n 
1 79  LYS n 
1 80  LEU n 
1 81  HIS n 
1 82  CYS n 
1 83  ILE n 
1 84  PHE n 
1 85  LEU n 
1 86  GLY n 
1 87  ALA n 
1 88  GLN n 
1 89  GLY n 
1 90  PHE n 
1 91  PHE n 
1 92  LEU n 
1 93  ASP n 
1 94  CYS n 
1 95  LEU n 
1 96  ALA n 
1 97  TRP n 
1 98  SER n 
1 99  THR n 
1 100 SER n 
1 101 ALA n 
1 102 HIS n 
1 103 LEU n 
1 104 VAL n 
1 105 PRO n 
1 106 ARG n 
1 107 ALA n 
1 108 PRO n 
1 109 GLY n 
1 110 SER n 
1 111 LEU n 
1 112 MET n 
1 113 ILE n 
1 114 SER n 
1 115 GLY n 
1 116 LEU n 
1 117 THR n 
1 118 GLU n 
1 119 ALA n 
1 120 PHE n 
1 121 VAL n 
1 122 MET n 
1 123 ALA n 
1 124 GLN n 
1 125 SER n 
1 126 ARG n 
1 127 VAL n 
1 128 GLU n 
1 129 GLU n 
1 130 LEU n 
1 131 ALA n 
1 132 GLU n 
1 133 ARG n 
1 134 LEU n 
1 135 SER n 
1 136 TRP n 
1 137 ASP n 
1 138 PHE n 
1 139 THR n 
1 140 PRO n 
1 141 GLY n 
1 142 PRO n 
1 143 SER n 
1 144 SER n 
1 145 GLY n 
1 146 ALA n 
1 147 SER n 
1 148 GLN n 
1 149 CYS n 
1 150 THR n 
1 151 GLY n 
1 152 VAL n 
1 153 LEU n 
1 154 ARG n 
1 155 ASP n 
1 156 PHE n 
1 157 SER n 
1 158 ALA n 
1 159 LEU n 
1 160 LEU n 
1 161 GLN n 
1 162 SER n 
1 163 PRO n 
1 164 GLY n 
1 165 ASP n 
1 166 ALA n 
1 167 HIS n 
1 168 ARG n 
1 169 GLU n 
1 170 ALA n 
1 171 LEU n 
1 172 LEU n 
1 173 GLN n 
1 174 LEU n 
1 175 PRO n 
1 176 LEU n 
1 177 ALA n 
1 178 VAL n 
1 179 GLN n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 SER n 
1 185 LEU n 
1 186 VAL n 
1 187 GLN n 
1 188 GLU n 
1 189 ALA 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                   189 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'KHNYN, KIAA0323' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
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   SER 1   50  ?   ?   ?   A . n 
A 1 2   ASN 2   51  ?   ?   ?   A . n 
A 1 3   ALA 3   52  52  ALA ALA A . n 
A 1 4   ASP 4   53  53  ASP ASP A . n 
A 1 5   ARG 5   54  54  ARG ARG A . n 
A 1 6   PHE 6   55  55  PHE PHE A . n 
A 1 7   ALA 7   56  56  ALA ALA A . n 
A 1 8   VAL 8   57  57  VAL VAL A . n 
A 1 9   SER 9   58  58  SER SER A . n 
A 1 10  ALA 10  59  59  ALA ALA A . n 
A 1 11  GLU 11  60  60  GLU GLU A . n 
A 1 12  ALA 12  61  61  ALA ALA A . n 
A 1 13  GLU 13  62  62  GLU GLU A . n 
A 1 14  ASN 14  63  63  ASN ASN A . n 
A 1 15  LYS 15  64  64  LYS LYS A . n 
A 1 16  VAL 16  65  65  VAL VAL A . n 
A 1 17  ARG 17  66  66  ARG ARG A . n 
A 1 18  GLU 18  67  67  GLU GLU A . n 
A 1 19  GLN 19  68  68  GLN GLN A . n 
A 1 20  GLN 20  69  69  GLN GLN A . n 
A 1 21  PRO 21  70  70  PRO PRO A . n 
A 1 22  HIS 22  71  71  HIS HIS A . n 
A 1 23  VAL 23  72  72  VAL VAL A . n 
A 1 24  GLU 24  73  73  GLU GLU A . n 
A 1 25  ARG 25  74  74  ARG ARG A . n 
A 1 26  ILE 26  75  75  ILE ILE A . n 
A 1 27  PHE 27  76  76  PHE PHE A . n 
A 1 28  SER 28  77  77  SER SER A . n 
A 1 29  VAL 29  78  78  VAL VAL A . n 
A 1 30  GLY 30  79  79  GLY GLY A . n 
A 1 31  VAL 31  80  80  VAL VAL A . n 
A 1 32  SER 32  81  81  SER SER A . n 
A 1 33  VAL 33  82  82  VAL VAL A . n 
A 1 34  LEU 34  83  83  LEU LEU A . n 
A 1 35  PRO 35  84  84  PRO PRO A . n 
A 1 36  LYS 36  85  85  LYS LYS A . n 
A 1 37  ASP 37  86  86  ASP ASP A . n 
A 1 38  CYS 38  87  87  CYS CYS A . n 
A 1 39  PRO 39  88  88  PRO PRO A . n 
A 1 40  ASP 40  89  89  ASP ASP A . n 
A 1 41  ASN 41  90  90  ASN ASN A . n 
A 1 42  PRO 42  91  91  PRO PRO A . n 
A 1 43  HIS 43  92  92  HIS HIS A . n 
A 1 44  ILE 44  93  93  ILE ILE A . n 
A 1 45  TRP 45  94  94  TRP TRP A . n 
A 1 46  LEU 46  95  95  LEU LEU A . n 
A 1 47  GLN 47  96  96  GLN GLN A . n 
A 1 48  LEU 48  97  97  LEU LEU A . n 
A 1 49  GLU 49  98  98  GLU GLU A . n 
A 1 50  GLY 50  99  99  GLY GLY A . n 
A 1 51  PRO 51  100 100 PRO PRO A . n 
A 1 52  LYS 52  101 101 LYS LYS A . n 
A 1 53  GLU 53  102 102 GLU GLU A . n 
A 1 54  ASN 54  103 103 ASN ASN A . n 
A 1 55  ALA 55  104 104 ALA ALA A . n 
A 1 56  SER 56  105 105 SER SER A . n 
A 1 57  ARG 57  106 106 ARG ARG A . n 
A 1 58  ALA 58  107 107 ALA ALA A . n 
A 1 59  LYS 59  108 108 LYS LYS A . n 
A 1 60  GLU 60  109 109 GLU GLU A . n 
A 1 61  TYR 61  110 110 TYR TYR A . n 
A 1 62  LEU 62  111 111 LEU LEU A . n 
A 1 63  LYS 63  112 112 LYS LYS A . n 
A 1 64  GLY 64  113 113 GLY GLY A . n 
A 1 65  LEU 65  114 114 LEU LEU A . n 
A 1 66  CYS 66  115 115 CYS CYS A . n 
A 1 67  SER 67  116 116 SER SER A . n 
A 1 68  PRO 68  117 117 PRO PRO A . n 
A 1 69  GLU 69  118 118 GLU GLU A . n 
A 1 70  LEU 70  119 119 LEU LEU A . n 
A 1 71  GLN 71  120 120 GLN GLN A . n 
A 1 72  ASP 72  121 121 ASP ASP A . n 
A 1 73  GLU 73  122 122 GLU GLU A . n 
A 1 74  ILE 74  123 123 ILE ILE A . n 
A 1 75  HIS 75  124 124 HIS HIS A . n 
A 1 76  TYR 76  125 125 TYR TYR A . n 
A 1 77  PRO 77  126 126 PRO PRO A . n 
A 1 78  PRO 78  127 127 PRO PRO A . n 
A 1 79  LYS 79  128 128 LYS LYS A . n 
A 1 80  LEU 80  129 129 LEU LEU A . n 
A 1 81  HIS 81  130 130 HIS HIS A . n 
A 1 82  CYS 82  131 131 CYS CYS A . n 
A 1 83  ILE 83  132 132 ILE ILE A . n 
A 1 84  PHE 84  133 133 PHE PHE A . n 
A 1 85  LEU 85  134 134 LEU LEU A . n 
A 1 86  GLY 86  135 135 GLY GLY A . n 
A 1 87  ALA 87  136 136 ALA ALA A . n 
A 1 88  GLN 88  137 137 GLN GLN A . n 
A 1 89  GLY 89  138 138 GLY GLY A . n 
A 1 90  PHE 90  139 139 PHE PHE A . n 
A 1 91  PHE 91  140 140 PHE PHE A . n 
A 1 92  LEU 92  141 141 LEU LEU A . n 
A 1 93  ASP 93  142 142 ASP ASP A . n 
A 1 94  CYS 94  143 143 CYS CYS A . n 
A 1 95  LEU 95  144 144 LEU LEU A . n 
A 1 96  ALA 96  145 145 ALA ALA A . n 
A 1 97  TRP 97  146 146 TRP TRP A . n 
A 1 98  SER 98  147 147 SER SER A . n 
A 1 99  THR 99  148 148 THR THR A . n 
A 1 100 SER 100 149 149 SER SER A . n 
A 1 101 ALA 101 150 150 ALA ALA A . n 
A 1 102 HIS 102 151 151 HIS HIS A . n 
A 1 103 LEU 103 152 152 LEU LEU A . n 
A 1 104 VAL 104 153 153 VAL VAL A . n 
A 1 105 PRO 105 154 154 PRO PRO A . n 
A 1 106 ARG 106 155 155 ARG ARG A . n 
A 1 107 ALA 107 156 156 ALA ALA A . n 
A 1 108 PRO 108 157 157 PRO PRO A . n 
A 1 109 GLY 109 158 158 GLY GLY A . n 
A 1 110 SER 110 159 159 SER SER A . n 
A 1 111 LEU 111 160 160 LEU LEU A . n 
A 1 112 MET 112 161 161 MET MET A . n 
A 1 113 ILE 113 162 162 ILE ILE A . n 
A 1 114 SER 114 163 163 SER SER A . n 
A 1 115 GLY 115 164 164 GLY GLY A . n 
A 1 116 LEU 116 165 165 LEU LEU A . n 
A 1 117 THR 117 166 166 THR THR A . n 
A 1 118 GLU 118 167 167 GLU GLU A . n 
A 1 119 ALA 119 168 168 ALA ALA A . n 
A 1 120 PHE 120 169 169 PHE PHE A . n 
A 1 121 VAL 121 170 170 VAL VAL A . n 
A 1 122 MET 122 171 171 MET MET A . n 
A 1 123 ALA 123 172 172 ALA ALA A . n 
A 1 124 GLN 124 173 173 GLN GLN A . n 
A 1 125 SER 125 174 174 SER SER A . n 
A 1 126 ARG 126 175 175 ARG ARG A . n 
A 1 127 VAL 127 176 176 VAL VAL A . n 
A 1 128 GLU 128 177 177 GLU GLU A . n 
A 1 129 GLU 129 178 178 GLU GLU A . n 
A 1 130 LEU 130 179 179 LEU LEU A . n 
A 1 131 ALA 131 180 180 ALA ALA A . n 
A 1 132 GLU 132 181 181 GLU GLU A . n 
A 1 133 ARG 133 182 182 ARG ARG A . n 
A 1 134 LEU 134 183 183 LEU LEU A . n 
A 1 135 SER 135 184 184 SER SER A . n 
A 1 136 TRP 136 185 185 TRP TRP A . n 
A 1 137 ASP 137 186 186 ASP ASP A . n 
A 1 138 PHE 138 187 187 PHE PHE A . n 
A 1 139 THR 139 187 ?   ?   ?   A A n 
A 1 140 PRO 140 187 ?   ?   ?   A B n 
A 1 141 GLY 141 187 ?   ?   ?   A C n 
A 1 142 PRO 142 187 ?   ?   ?   A D n 
A 1 143 SER 143 187 ?   ?   ?   A E n 
A 1 144 SER 144 187 ?   ?   ?   A F n 
A 1 145 GLY 145 187 ?   ?   ?   A G n 
A 1 146 ALA 146 187 ?   ?   ?   A H n 
A 1 147 SER 147 187 ?   ?   ?   A I n 
A 1 148 GLN 148 187 ?   ?   ?   A J n 
A 1 149 CYS 149 187 ?   ?   ?   A K n 
A 1 150 THR 150 196 196 THR THR A . n 
A 1 151 GLY 151 197 197 GLY GLY A . n 
A 1 152 VAL 152 198 198 VAL VAL A . n 
A 1 153 LEU 153 199 199 LEU LEU A . n 
A 1 154 ARG 154 200 200 ARG ARG A . n 
A 1 155 ASP 155 201 201 ASP ASP A . n 
A 1 156 PHE 156 202 202 PHE PHE A . n 
A 1 157 SER 157 203 203 SER SER A . n 
A 1 158 ALA 158 204 204 ALA ALA A . n 
A 1 159 LEU 159 205 205 LEU LEU A . n 
A 1 160 LEU 160 206 206 LEU LEU A . n 
A 1 161 GLN 161 207 207 GLN GLN A . n 
A 1 162 SER 162 208 208 SER SER A . n 
A 1 163 PRO 163 209 209 PRO PRO A . n 
A 1 164 GLY 164 210 210 GLY GLY A . n 
A 1 165 ASP 165 211 211 ASP ASP A . n 
A 1 166 ALA 166 212 212 ALA ALA A . n 
A 1 167 HIS 167 213 213 HIS HIS A . n 
A 1 168 ARG 168 214 214 ARG ARG A . n 
A 1 169 GLU 169 215 215 GLU GLU A . n 
A 1 170 ALA 170 216 216 ALA ALA A . n 
A 1 171 LEU 171 217 217 LEU LEU A . n 
A 1 172 LEU 172 218 218 LEU LEU A . n 
A 1 173 GLN 173 219 219 GLN GLN A . n 
A 1 174 LEU 174 220 220 LEU LEU A . n 
A 1 175 PRO 175 221 221 PRO PRO A . n 
A 1 176 LEU 176 222 222 LEU LEU A . n 
A 1 177 ALA 177 223 223 ALA ALA A . n 
A 1 178 VAL 178 224 224 VAL VAL A . n 
A 1 179 GLN 179 225 225 GLN GLN A . n 
A 1 180 GLU 180 226 226 GLU GLU A . n 
A 1 181 GLU 181 227 227 GLU GLU A . n 
A 1 182 LEU 182 228 228 LEU LEU A . n 
A 1 183 LEU 183 229 229 LEU LEU A . n 
A 1 184 SER 184 230 230 SER SER A . n 
A 1 185 LEU 185 231 231 LEU LEU A . n 
A 1 186 VAL 186 232 232 VAL VAL A . n 
A 1 187 GLN 187 233 233 GLN GLN A . n 
A 1 188 GLU 188 234 234 GLU GLU A . n 
A 1 189 ALA 189 235 235 ALA ALA A . n 
B 1 1   SER 1   50  ?   ?   ?   B . n 
B 1 2   ASN 2   51  ?   ?   ?   B . n 
B 1 3   ALA 3   52  52  ALA ALA B . n 
B 1 4   ASP 4   53  53  ASP ASP B . n 
B 1 5   ARG 5   54  54  ARG ARG B . n 
B 1 6   PHE 6   55  55  PHE PHE B . n 
B 1 7   ALA 7   56  56  ALA ALA B . n 
B 1 8   VAL 8   57  57  VAL VAL B . n 
B 1 9   SER 9   58  58  SER SER B . n 
B 1 10  ALA 10  59  59  ALA ALA B . n 
B 1 11  GLU 11  60  60  GLU GLU B . n 
B 1 12  ALA 12  61  61  ALA ALA B . n 
B 1 13  GLU 13  62  62  GLU GLU B . n 
B 1 14  ASN 14  63  63  ASN ASN B . n 
B 1 15  LYS 15  64  64  LYS LYS B . n 
B 1 16  VAL 16  65  65  VAL VAL B . n 
B 1 17  ARG 17  66  66  ARG ARG B . n 
B 1 18  GLU 18  67  67  GLU GLU B . n 
B 1 19  GLN 19  68  68  GLN GLN B . n 
B 1 20  GLN 20  69  69  GLN GLN B . n 
B 1 21  PRO 21  70  70  PRO PRO B . n 
B 1 22  HIS 22  71  71  HIS HIS B . n 
B 1 23  VAL 23  72  72  VAL VAL B . n 
B 1 24  GLU 24  73  73  GLU GLU B . n 
B 1 25  ARG 25  74  74  ARG ARG B . n 
B 1 26  ILE 26  75  75  ILE ILE B . n 
B 1 27  PHE 27  76  76  PHE PHE B . n 
B 1 28  SER 28  77  77  SER SER B . n 
B 1 29  VAL 29  78  78  VAL VAL B . n 
B 1 30  GLY 30  79  79  GLY GLY B . n 
B 1 31  VAL 31  80  80  VAL VAL B . n 
B 1 32  SER 32  81  81  SER SER B . n 
B 1 33  VAL 33  82  82  VAL VAL B . n 
B 1 34  LEU 34  83  83  LEU LEU B . n 
B 1 35  PRO 35  84  84  PRO PRO B . n 
B 1 36  LYS 36  85  85  LYS LYS B . n 
B 1 37  ASP 37  86  86  ASP ASP B . n 
B 1 38  CYS 38  87  87  CYS CYS B . n 
B 1 39  PRO 39  88  88  PRO PRO B . n 
B 1 40  ASP 40  89  89  ASP ASP B . n 
B 1 41  ASN 41  90  90  ASN ASN B . n 
B 1 42  PRO 42  91  91  PRO PRO B . n 
B 1 43  HIS 43  92  92  HIS HIS B . n 
B 1 44  ILE 44  93  93  ILE ILE B . n 
B 1 45  TRP 45  94  94  TRP TRP B . n 
B 1 46  LEU 46  95  95  LEU LEU B . n 
B 1 47  GLN 47  96  96  GLN GLN B . n 
B 1 48  LEU 48  97  97  LEU LEU B . n 
B 1 49  GLU 49  98  98  GLU GLU B . n 
B 1 50  GLY 50  99  99  GLY GLY B . n 
B 1 51  PRO 51  100 100 PRO PRO B . n 
B 1 52  LYS 52  101 101 LYS LYS B . n 
B 1 53  GLU 53  102 102 GLU GLU B . n 
B 1 54  ASN 54  103 103 ASN ASN B . n 
B 1 55  ALA 55  104 104 ALA ALA B . n 
B 1 56  SER 56  105 105 SER SER B . n 
B 1 57  ARG 57  106 106 ARG ARG B . n 
B 1 58  ALA 58  107 107 ALA ALA B . n 
B 1 59  LYS 59  108 108 LYS LYS B . n 
B 1 60  GLU 60  109 109 GLU GLU B . n 
B 1 61  TYR 61  110 110 TYR TYR B . n 
B 1 62  LEU 62  111 111 LEU LEU B . n 
B 1 63  LYS 63  112 112 LYS LYS B . n 
B 1 64  GLY 64  113 113 GLY GLY B . n 
B 1 65  LEU 65  114 114 LEU LEU B . n 
B 1 66  CYS 66  115 115 CYS CYS B . n 
B 1 67  SER 67  116 116 SER SER B . n 
B 1 68  PRO 68  117 117 PRO PRO B . n 
B 1 69  GLU 69  118 118 GLU GLU B . n 
B 1 70  LEU 70  119 119 LEU LEU B . n 
B 1 71  GLN 71  120 120 GLN GLN B . n 
B 1 72  ASP 72  121 121 ASP ASP B . n 
B 1 73  GLU 73  122 122 GLU GLU B . n 
B 1 74  ILE 74  123 123 ILE ILE B . n 
B 1 75  HIS 75  124 124 HIS HIS B . n 
B 1 76  TYR 76  125 125 TYR TYR B . n 
B 1 77  PRO 77  126 126 PRO PRO B . n 
B 1 78  PRO 78  127 127 PRO PRO B . n 
B 1 79  LYS 79  128 128 LYS LYS B . n 
B 1 80  LEU 80  129 129 LEU LEU B . n 
B 1 81  HIS 81  130 130 HIS HIS B . n 
B 1 82  CYS 82  131 131 CYS CYS B . n 
B 1 83  ILE 83  132 132 ILE ILE B . n 
B 1 84  PHE 84  133 133 PHE PHE B . n 
B 1 85  LEU 85  134 134 LEU LEU B . n 
B 1 86  GLY 86  135 135 GLY GLY B . n 
B 1 87  ALA 87  136 136 ALA ALA B . n 
B 1 88  GLN 88  137 137 GLN GLN B . n 
B 1 89  GLY 89  138 138 GLY GLY B . n 
B 1 90  PHE 90  139 139 PHE PHE B . n 
B 1 91  PHE 91  140 140 PHE PHE B . n 
B 1 92  LEU 92  141 141 LEU LEU B . n 
B 1 93  ASP 93  142 142 ASP ASP B . n 
B 1 94  CYS 94  143 143 CYS CYS B . n 
B 1 95  LEU 95  144 144 LEU LEU B . n 
B 1 96  ALA 96  145 145 ALA ALA B . n 
B 1 97  TRP 97  146 146 TRP TRP B . n 
B 1 98  SER 98  147 147 SER SER B . n 
B 1 99  THR 99  148 148 THR THR B . n 
B 1 100 SER 100 149 149 SER SER B . n 
B 1 101 ALA 101 150 150 ALA ALA B . n 
B 1 102 HIS 102 151 151 HIS HIS B . n 
B 1 103 LEU 103 152 152 LEU LEU B . n 
B 1 104 VAL 104 153 153 VAL VAL B . n 
B 1 105 PRO 105 154 154 PRO PRO B . n 
B 1 106 ARG 106 155 155 ARG ARG B . n 
B 1 107 ALA 107 156 156 ALA ALA B . n 
B 1 108 PRO 108 157 157 PRO PRO B . n 
B 1 109 GLY 109 158 158 GLY GLY B . n 
B 1 110 SER 110 159 159 SER SER B . n 
B 1 111 LEU 111 160 160 LEU LEU B . n 
B 1 112 MET 112 161 161 MET MET B . n 
B 1 113 ILE 113 162 162 ILE ILE B . n 
B 1 114 SER 114 163 163 SER SER B . n 
B 1 115 GLY 115 164 164 GLY GLY B . n 
B 1 116 LEU 116 165 165 LEU LEU B . n 
B 1 117 THR 117 166 166 THR THR B . n 
B 1 118 GLU 118 167 167 GLU GLU B . n 
B 1 119 ALA 119 168 168 ALA ALA B . n 
B 1 120 PHE 120 169 169 PHE PHE B . n 
B 1 121 VAL 121 170 170 VAL VAL B . n 
B 1 122 MET 122 171 171 MET MET B . n 
B 1 123 ALA 123 172 172 ALA ALA B . n 
B 1 124 GLN 124 173 173 GLN GLN B . n 
B 1 125 SER 125 174 174 SER SER B . n 
B 1 126 ARG 126 175 175 ARG ARG B . n 
B 1 127 VAL 127 176 176 VAL VAL B . n 
B 1 128 GLU 128 177 177 GLU GLU B . n 
B 1 129 GLU 129 178 178 GLU GLU B . n 
B 1 130 LEU 130 179 179 LEU LEU B . n 
B 1 131 ALA 131 180 180 ALA ALA B . n 
B 1 132 GLU 132 181 181 GLU GLU B . n 
B 1 133 ARG 133 182 182 ARG ARG B . n 
B 1 134 LEU 134 183 183 LEU LEU B . n 
B 1 135 SER 135 184 184 SER SER B . n 
B 1 136 TRP 136 185 185 TRP TRP B . n 
B 1 137 ASP 137 186 186 ASP ASP B . n 
B 1 138 PHE 138 187 187 PHE ALA B . n 
B 1 139 THR 139 187 ?   ?   ?   B A n 
B 1 140 PRO 140 187 ?   ?   ?   B B n 
B 1 141 GLY 141 187 ?   ?   ?   B C n 
B 1 142 PRO 142 187 ?   ?   ?   B D n 
B 1 143 SER 143 187 ?   ?   ?   B E n 
B 1 144 SER 144 187 ?   ?   ?   B F n 
B 1 145 GLY 145 187 ?   ?   ?   B G n 
B 1 146 ALA 146 187 ?   ?   ?   B H n 
B 1 147 SER 147 187 ?   ?   ?   B I n 
B 1 148 GLN 148 187 ?   ?   ?   B J n 
B 1 149 CYS 149 195 195 CYS CYS B . n 
B 1 150 THR 150 196 196 THR THR B . n 
B 1 151 GLY 151 197 197 GLY GLY B . n 
B 1 152 VAL 152 198 198 VAL VAL B . n 
B 1 153 LEU 153 199 199 LEU LEU B . n 
B 1 154 ARG 154 200 200 ARG ARG B . n 
B 1 155 ASP 155 201 201 ASP ASP B . n 
B 1 156 PHE 156 202 202 PHE PHE B . n 
B 1 157 SER 157 203 203 SER SER B . n 
B 1 158 ALA 158 204 204 ALA ALA B . n 
B 1 159 LEU 159 205 205 LEU LEU B . n 
B 1 160 LEU 160 206 206 LEU LEU B . n 
B 1 161 GLN 161 207 207 GLN GLN B . n 
B 1 162 SER 162 208 208 SER SER B . n 
B 1 163 PRO 163 209 209 PRO PRO B . n 
B 1 164 GLY 164 210 210 GLY GLY B . n 
B 1 165 ASP 165 211 211 ASP ASP B . n 
B 1 166 ALA 166 212 212 ALA ALA B . n 
B 1 167 HIS 167 213 213 HIS HIS B . n 
B 1 168 ARG 168 214 214 ARG ARG B . n 
B 1 169 GLU 169 215 215 GLU GLU B . n 
B 1 170 ALA 170 216 216 ALA ALA B . n 
B 1 171 LEU 171 217 217 LEU LEU B . n 
B 1 172 LEU 172 218 218 LEU LEU B . n 
B 1 173 GLN 173 219 219 GLN GLN B . n 
B 1 174 LEU 174 220 220 LEU LEU B . n 
B 1 175 PRO 175 221 221 PRO PRO B . n 
B 1 176 LEU 176 222 222 LEU LEU B . n 
B 1 177 ALA 177 223 223 ALA ALA B . n 
B 1 178 VAL 178 224 224 VAL VAL B . n 
B 1 179 GLN 179 225 225 GLN GLN B . n 
B 1 180 GLU 180 226 226 GLU GLU B . n 
B 1 181 GLU 181 227 227 GLU GLU B . n 
B 1 182 LEU 182 228 228 LEU LEU B . n 
B 1 183 LEU 183 229 229 LEU LEU B . n 
B 1 184 SER 184 230 230 SER SER B . n 
B 1 185 LEU 185 231 231 LEU LEU B . n 
B 1 186 VAL 186 232 232 VAL VAL B . n 
B 1 187 GLN 187 233 233 GLN GLN B . n 
B 1 188 GLU 188 234 234 GLU GLU B . n 
B 1 189 ALA 189 235 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SO4 1  301 9   SO4 SO4 A . 
D 2 SO4 1  302 10  SO4 SO4 A . 
E 2 SO4 1  301 11  SO4 SO4 B . 
F 2 SO4 1  302 12  SO4 SO4 B . 
G 3 HOH 1  401 117 HOH HOH A . 
G 3 HOH 2  402 96  HOH HOH A . 
G 3 HOH 3  403 53  HOH HOH A . 
G 3 HOH 4  404 84  HOH HOH A . 
G 3 HOH 5  405 106 HOH HOH A . 
G 3 HOH 6  406 116 HOH HOH A . 
G 3 HOH 7  407 40  HOH HOH A . 
G 3 HOH 8  408 35  HOH HOH A . 
G 3 HOH 9  409 1   HOH HOH A . 
G 3 HOH 10 410 112 HOH HOH A . 
G 3 HOH 11 411 88  HOH HOH A . 
G 3 HOH 12 412 50  HOH HOH A . 
G 3 HOH 13 413 32  HOH HOH A . 
G 3 HOH 14 414 21  HOH HOH A . 
G 3 HOH 15 415 119 HOH HOH A . 
G 3 HOH 16 416 52  HOH HOH A . 
H 3 HOH 1  401 51  HOH HOH B . 
H 3 HOH 2  402 11  HOH HOH B . 
H 3 HOH 3  403 22  HOH HOH B . 
H 3 HOH 4  404 102 HOH HOH B . 
H 3 HOH 5  405 30  HOH HOH B . 
H 3 HOH 6  406 5   HOH HOH B . 
H 3 HOH 7  407 3   HOH HOH B . 
H 3 HOH 8  408 2   HOH HOH B . 
H 3 HOH 9  409 23  HOH HOH B . 
H 3 HOH 10 410 62  HOH HOH B . 
H 3 HOH 11 411 13  HOH HOH B . 
H 3 HOH 12 412 17  HOH HOH B . 
H 3 HOH 13 413 48  HOH HOH B . 
H 3 HOH 14 414 105 HOH HOH B . 
H 3 HOH 15 415 59  HOH HOH B . 
H 3 HOH 16 416 81  HOH HOH B . 
H 3 HOH 17 417 15  HOH HOH B . 
H 3 HOH 18 418 67  HOH HOH B . 
H 3 HOH 19 419 14  HOH HOH B . 
H 3 HOH 20 420 57  HOH HOH B . 
H 3 HOH 21 421 20  HOH HOH B . 
H 3 HOH 22 422 18  HOH HOH B . 
H 3 HOH 23 423 39  HOH HOH B . 
H 3 HOH 24 424 94  HOH HOH B . 
H 3 HOH 25 425 61  HOH HOH B . 
H 3 HOH 26 426 31  HOH HOH B . 
H 3 HOH 27 427 43  HOH HOH B . 
H 3 HOH 28 428 42  HOH HOH B . 
H 3 HOH 29 429 33  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B PHE 187 ? CG  ? B PHE 138 CG  
2 1 Y 1 B PHE 187 ? CD1 ? B PHE 138 CD1 
3 1 Y 1 B PHE 187 ? CD2 ? B PHE 138 CD2 
4 1 Y 1 B PHE 187 ? CE1 ? B PHE 138 CE1 
5 1 Y 1 B PHE 187 ? CE2 ? B PHE 138 CE2 
6 1 Y 1 B PHE 187 ? CZ  ? B PHE 138 CZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.9.8.93        1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1-4487-000 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .               3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .               4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .               5 
# 
_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                     9CS9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.269 
_cell.length_a_esd                 ? 
_cell.length_b                     82.269 
_cell.length_b_esd                 ? 
_cell.length_c                     177.224 
_cell.length_c_esd                 ? 
_cell.volume                       1199485.414 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9CS9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            'P 4nw 2abw' 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_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                   9CS9 
_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             3.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          67.92 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM Tris pH 8.0, 1.4 M Li2SO4, 5% methanol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-30 
_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   1.033167 
_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 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033167 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          58.70 
_reflns.entry_id                                       9CS9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.5 
_reflns.d_resolution_low                               48.63 
_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                                     40169 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          0.15 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.5 
_reflns_shell.d_res_low                                     2.65 
_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                             21967 
_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                               12.4 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.876 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_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                               58.13 
_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                                 9CS9 
_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                            2.50 
_refine.ls_d_res_low                             48.63 
_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                     40169 
_refine.ls_number_reflns_R_free                  2359 
_refine.ls_number_reflns_R_work                  37810 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 5.87 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2005 
_refine.ls_R_factor_R_free                       0.2401 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1981 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_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                 26.9924 
_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                            0.3793 
_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                       2.50 
_refine_hist.d_res_low                        48.63 
_refine_hist.number_atoms_solvent             45 
_refine_hist.number_atoms_total               2814 
_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        2749 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_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' ? 0.0089  ? 2849 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9903  ? 3876 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0578  ? 429  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0092  ? 508  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 17.3862 ? 1053 ? 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.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' 2.50 2.55  . . 140 2232 99.92  . . . . 0.3422 . . . . . . . . . . . 0.3643 
'X-RAY DIFFRACTION' 2.55 2.61  . . 139 2196 99.91  . . . . 0.3088 . . . . . . . . . . . 0.3472 
'X-RAY DIFFRACTION' 2.61 2.67  . . 143 2237 100.00 . . . . 0.2903 . . . . . . . . . . . 0.3250 
'X-RAY DIFFRACTION' 2.67 2.73  . . 136 2223 100.00 . . . . 0.2819 . . . . . . . . . . . 0.3794 
'X-RAY DIFFRACTION' 2.73 2.81  . . 140 2213 100.00 . . . . 0.2812 . . . . . . . . . . . 0.4483 
'X-RAY DIFFRACTION' 2.81 2.89  . . 135 2229 99.96  . . . . 0.2854 . . . . . . . . . . . 0.3503 
'X-RAY DIFFRACTION' 2.89 2.98  . . 141 2255 100.00 . . . . 0.2781 . . . . . . . . . . . 0.3033 
'X-RAY DIFFRACTION' 2.98 3.09  . . 132 2203 99.87  . . . . 0.2993 . . . . . . . . . . . 0.3689 
'X-RAY DIFFRACTION' 3.09 3.21  . . 143 2230 99.92  . . . . 0.2833 . . . . . . . . . . . 0.3456 
'X-RAY DIFFRACTION' 3.21 3.36  . . 136 2228 99.92  . . . . 0.2338 . . . . . . . . . . . 0.2903 
'X-RAY DIFFRACTION' 3.36 3.54  . . 133 2232 100.00 . . . . 0.1964 . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 3.54 3.76  . . 141 2240 99.96  . . . . 0.1883 . . . . . . . . . . . 0.2790 
'X-RAY DIFFRACTION' 3.76 4.05  . . 139 2192 99.96  . . . . 0.1667 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 4.05 4.46  . . 138 2227 100.00 . . . . 0.1562 . . . . . . . . . . . 0.1791 
'X-RAY DIFFRACTION' 4.46 5.10  . . 141 2235 99.96  . . . . 0.1377 . . . . . . . . . . . 0.1653 
'X-RAY DIFFRACTION' 5.10 6.42  . . 141 2221 100.00 . . . . 0.1740 . . . . . . . . . . . 0.1993 
'X-RAY DIFFRACTION' 6.42 48.63 . . 141 2217 99.45  . . . . 0.1494 . . . . . . . . . . . 0.1692 
# 
_struct.entry_id                     9CS9 
_struct.title                        'KHNYN KH1-KH2' 
_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        9CS9 
_struct_keywords.text            'Antiviral protein, KH' 
_struct_keywords.pdbx_keywords   'ANTIVIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    KHNYN_HUMAN 
_struct_ref.pdbx_db_accession          O15037 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DRFAVSAEAENKVREQQPHVERIFSVGVSVLPKDCPDNPHIWLQLEGPKENASRAKEYLKGLCSPELQDEIHYPPKLHCI
FLGAQGFFLDCLAWSTSAHLVPRAPGSLMISGLTEAFVMAQSRVEELAERLSWDFTPGPSSGASQCTGVLRDFSALLQSP
GDAHREALLQLPLAVQEELLSLVQEA
;
_struct_ref.pdbx_align_begin           12 
# 
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 9CS9 A 4 ? 189 ? O15037 12 ? 197 ? 53 235 
2 1 9CS9 B 4 ? 189 ? O15037 12 ? 197 ? 53 235 
# 
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 9CS9 SER A 1 ? UNP O15037 ? ? 'expression tag' 50 1 
1 9CS9 ASN A 2 ? UNP O15037 ? ? 'expression tag' 51 2 
1 9CS9 ALA A 3 ? UNP O15037 ? ? 'expression tag' 52 3 
2 9CS9 SER B 1 ? UNP O15037 ? ? 'expression tag' 50 4 
2 9CS9 ASN B 2 ? UNP O15037 ? ? 'expression tag' 51 5 
2 9CS9 ALA B 3 ? UNP O15037 ? ? 'expression tag' 52 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_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 ALA A 12  ? SER A 28  ? ALA A 61  SER A 77  1 ? 17 
HELX_P HELX_P2  AA2 PRO A 51  ? SER A 67  ? PRO A 100 SER A 116 1 ? 17 
HELX_P HELX_P3  AA3 PRO A 77  ? LEU A 80  ? PRO A 126 LEU A 129 5 ? 4  
HELX_P HELX_P4  AA4 HIS A 81  ? GLY A 86  ? HIS A 130 GLY A 135 1 ? 6  
HELX_P HELX_P5  AA5 GLY A 89  ? SER A 100 ? GLY A 138 SER A 149 1 ? 12 
HELX_P HELX_P6  AA6 LEU A 116 ? LEU A 134 ? LEU A 165 LEU A 183 1 ? 19 
HELX_P HELX_P7  AA7 GLY A 151 ? ALA A 158 ? GLY A 197 ALA A 204 1 ? 8  
HELX_P HELX_P8  AA8 HIS A 167 ? GLN A 173 ? HIS A 213 GLN A 219 1 ? 7  
HELX_P HELX_P9  AA9 PRO A 175 ? GLN A 187 ? PRO A 221 GLN A 233 1 ? 13 
HELX_P HELX_P10 AB1 ALA B 12  ? SER B 28  ? ALA B 61  SER B 77  1 ? 17 
HELX_P HELX_P11 AB2 PRO B 51  ? SER B 67  ? PRO B 100 SER B 116 1 ? 17 
HELX_P HELX_P12 AB3 PRO B 77  ? LEU B 80  ? PRO B 126 LEU B 129 5 ? 4  
HELX_P HELX_P13 AB4 HIS B 81  ? GLY B 86  ? HIS B 130 GLY B 135 1 ? 6  
HELX_P HELX_P14 AB5 GLY B 89  ? SER B 100 ? GLY B 138 SER B 149 1 ? 12 
HELX_P HELX_P15 AB6 LEU B 116 ? LEU B 134 ? LEU B 165 LEU B 183 1 ? 19 
HELX_P HELX_P16 AB7 GLY B 151 ? LEU B 160 ? GLY B 197 LEU B 206 1 ? 10 
HELX_P HELX_P17 AB8 HIS B 167 ? GLN B 173 ? HIS B 213 GLN B 219 1 ? 7  
HELX_P HELX_P18 AB9 PRO B 175 ? GLN B 187 ? PRO B 221 GLN B 233 1 ? 13 
# 
_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 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 5   ? SER A 9   ? ARG A 54  SER A 58  
AA1 2 HIS A 43  ? GLU A 49  ? HIS A 92  GLU A 98  
AA1 3 GLY A 30  ? VAL A 33  ? GLY A 79  VAL A 82  
AA2 1 LEU A 70  ? HIS A 75  ? LEU A 119 HIS A 124 
AA2 2 SER A 110 ? GLY A 115 ? SER A 159 GLY A 164 
AA2 3 HIS A 102 ? PRO A 105 ? HIS A 151 PRO A 154 
AA3 1 ARG B 5   ? SER B 9   ? ARG B 54  SER B 58  
AA3 2 HIS B 43  ? GLU B 49  ? HIS B 92  GLU B 98  
AA3 3 GLY B 30  ? VAL B 33  ? GLY B 79  VAL B 82  
AA4 1 LEU B 70  ? HIS B 75  ? LEU B 119 HIS B 124 
AA4 2 SER B 110 ? GLY B 115 ? SER B 159 GLY B 164 
AA4 3 HIS B 102 ? PRO B 105 ? HIS B 151 PRO B 154 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 6   ? N PHE A 55  O LEU A 46  ? O LEU A 95  
AA1 2 3 O GLN A 47  ? O GLN A 96  N SER A 32  ? N SER A 81  
AA2 1 2 N ILE A 74  ? N ILE A 123 O LEU A 111 ? O LEU A 160 
AA2 2 3 O SER A 114 ? O SER A 163 N HIS A 102 ? N HIS A 151 
AA3 1 2 N PHE B 6   ? N PHE B 55  O LEU B 46  ? O LEU B 95  
AA3 2 3 O GLU B 49  ? O GLU B 98  N GLY B 30  ? N GLY B 79  
AA4 1 2 N ILE B 74  ? N ILE B 123 O LEU B 111 ? O LEU B 160 
AA4 2 3 O SER B 114 ? O SER B 163 N HIS B 102 ? N HIS B 151 
# 
_pdbx_entry_details.entry_id                   9CS9 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 155 ? ? -120.70 -141.93 
2 1 GLN A 233 ? ? -100.44 44.66   
3 1 ARG B 155 ? ? -121.07 -140.72 
4 1 ASP B 186 ? ? 56.53   102.88  
5 1 THR B 196 ? ? -16.81  -86.95  
6 1 GLN B 233 ? ? -101.74 46.53   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -y+1/2,x+1/2,z+3/4  
3 y+1/2,-x+1/2,z+1/4  
4 x+1/2,-y+1/2,-z+1/4 
5 -x+1/2,y+1/2,-z+3/4 
6 -x,-y,z+1/2         
7 y,x,-z              
8 -y,-x,-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 SER 50  ? A SER 1   
2  1 Y 1 A ASN 51  ? A ASN 2   
3  1 Y 1 A THR 187 A A THR 139 
4  1 Y 1 A PRO 187 B A PRO 140 
5  1 Y 1 A GLY 187 C A GLY 141 
6  1 Y 1 A PRO 187 D A PRO 142 
7  1 Y 1 A SER 187 E A SER 143 
8  1 Y 1 A SER 187 F A SER 144 
9  1 Y 1 A GLY 187 G A GLY 145 
10 1 Y 1 A ALA 187 H A ALA 146 
11 1 Y 1 A SER 187 I A SER 147 
12 1 Y 1 A GLN 187 J A GLN 148 
13 1 Y 1 A CYS 187 K A CYS 149 
14 1 Y 1 B SER 50  ? B SER 1   
15 1 Y 1 B ASN 51  ? B ASN 2   
16 1 Y 1 B THR 187 A B THR 139 
17 1 Y 1 B PRO 187 B B PRO 140 
18 1 Y 1 B GLY 187 C B GLY 141 
19 1 Y 1 B PRO 187 D B PRO 142 
20 1 Y 1 B SER 187 E B SER 143 
21 1 Y 1 B SER 187 F B SER 144 
22 1 Y 1 B GLY 187 G B GLY 145 
23 1 Y 1 B ALA 187 H B ALA 146 
24 1 Y 1 B SER 187 I B SER 147 
25 1 Y 1 B GLN 187 J B GLN 148 
26 1 Y 1 B ALA 235 ? B ALA 189 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U54AI170660-01 
_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   6Q3V 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 43 21 2' 
_space_group.name_Hall        'P 4nw 2abw' 
_space_group.IT_number        96 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CS9 
_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]   0.012155 
_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]   0.012155 
_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]   0.005643 
_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   . ALA A 1 3   ? -15.41600 -18.47000 -28.52100 1.000 92.79000  ? 52  ALA A N   1 
ATOM   2    C CA  . ALA A 1 3   ? -14.26600 -18.62400 -29.41200 1.000 102.47000 ? 52  ALA A CA  1 
ATOM   3    C C   . ALA A 1 3   ? -12.96200 -18.82500 -28.61600 1.000 103.29000 ? 52  ALA A C   1 
ATOM   4    O O   . ALA A 1 3   ? -11.85200 -18.75500 -29.16500 1.000 96.00000  ? 52  ALA A O   1 
ATOM   5    C CB  . ALA A 1 3   ? -14.15200 -17.40900 -30.34900 1.000 93.56000  ? 52  ALA A CB  1 
ATOM   6    N N   . ASP A 1 4   ? -13.12000 -19.10200 -27.31700 1.000 99.51000  ? 53  ASP A N   1 
ATOM   7    C CA  . ASP A 1 4   ? -12.00900 -19.29700 -26.38600 1.000 98.75000  ? 53  ASP A CA  1 
ATOM   8    C C   . ASP A 1 4   ? -11.61500 -20.76700 -26.24300 1.000 92.53000  ? 53  ASP A C   1 
ATOM   9    O O   . ASP A 1 4   ? -10.49300 -21.06800 -25.80200 1.000 78.82000  ? 53  ASP A O   1 
ATOM   10   C CB  . ASP A 1 4   ? -12.40400 -18.72400 -25.00700 1.000 96.07000  ? 53  ASP A CB  1 
ATOM   11   C CG  . ASP A 1 4   ? -11.27900 -17.94000 -24.33200 1.000 98.17000  ? 53  ASP A CG  1 
ATOM   12   O OD1 . ASP A 1 4   ? -10.11200 -18.08900 -24.76400 1.000 95.28000  ? 53  ASP A OD1 1 
ATOM   13   O OD2 . ASP A 1 4   ? -11.56700 -17.17900 -23.37000 1.000 83.75000  ? 53  ASP A OD2 1 
ATOM   14   N N   . ARG A 1 5   ? -12.51000 -21.67600 -26.62300 1.000 79.08000  ? 54  ARG A N   1 
ATOM   15   C CA  . ARG A 1 5   ? -12.34200 -23.10800 -26.46500 1.000 75.04000  ? 54  ARG A CA  1 
ATOM   16   C C   . ARG A 1 5   ? -12.06700 -23.76300 -27.81000 1.000 71.50000  ? 54  ARG A C   1 
ATOM   17   O O   . ARG A 1 5   ? -12.45900 -23.25100 -28.86400 1.000 69.73000  ? 54  ARG A O   1 
ATOM   18   C CB  . ARG A 1 5   ? -13.57600 -23.74900 -25.81500 1.000 67.64000  ? 54  ARG A CB  1 
ATOM   19   C CG  . ARG A 1 5   ? -14.86200 -23.57000 -26.57900 1.000 69.02000  ? 54  ARG A CG  1 
ATOM   20   C CD  . ARG A 1 5   ? -16.07800 -23.76800 -25.68700 1.000 71.80000  ? 54  ARG A CD  1 
ATOM   21   N NE  . ARG A 1 5   ? -16.52200 -25.15900 -25.61000 1.000 87.86000  ? 54  ARG A NE  1 
ATOM   22   C CZ  . ARG A 1 5   ? -17.16300 -25.80900 -26.57700 1.000 82.22000  ? 54  ARG A CZ  1 
ATOM   23   N NH1 . ARG A 1 5   ? -17.42400 -25.23600 -27.74300 1.000 71.51000  ? 54  ARG A NH1 1 
ATOM   24   N NH2 . ARG A 1 5   ? -17.57300 -27.05800 -26.36200 1.000 74.72000  ? 54  ARG A NH2 1 
ATOM   25   N N   . PHE A 1 6   ? -11.33600 -24.87500 -27.76100 1.000 59.40000  ? 55  PHE A N   1 
ATOM   26   C CA  . PHE A 1 6   ? -11.00300 -25.63900 -28.95300 1.000 62.43000  ? 55  PHE A CA  1 
ATOM   27   C C   . PHE A 1 6   ? -10.95400 -27.10300 -28.56300 1.000 59.32000  ? 55  PHE A C   1 
ATOM   28   O O   . PHE A 1 6   ? -10.78900 -27.44500 -27.39000 1.000 63.80000  ? 55  PHE A O   1 
ATOM   29   C CB  . PHE A 1 6   ? -9.66900  -25.20300 -29.56900 1.000 58.93000  ? 55  PHE A CB  1 
ATOM   30   C CG  . PHE A 1 6   ? -8.48700  -25.51400 -28.70900 1.000 61.52000  ? 55  PHE A CG  1 
ATOM   31   C CD1 . PHE A 1 6   ? -8.11000  -24.64800 -27.69000 1.000 56.67000  ? 55  PHE A CD1 1 
ATOM   32   C CD2 . PHE A 1 6   ? -7.76500  -26.68000 -28.89700 1.000 56.76000  ? 55  PHE A CD2 1 
ATOM   33   C CE1 . PHE A 1 6   ? -7.03000  -24.93400 -26.87900 1.000 55.24000  ? 55  PHE A CE1 1 
ATOM   34   C CE2 . PHE A 1 6   ? -6.69100  -26.97000 -28.09800 1.000 56.76000  ? 55  PHE A CE2 1 
ATOM   35   C CZ  . PHE A 1 6   ? -6.32200  -26.09000 -27.07700 1.000 57.05000  ? 55  PHE A CZ  1 
ATOM   36   N N   . ALA A 1 7   ? -11.11200 -27.96500 -29.55800 1.000 59.19000  ? 56  ALA A N   1 
ATOM   37   C CA  . ALA A 1 7   ? -11.26800 -29.39300 -29.33000 1.000 58.97000  ? 56  ALA A CA  1 
ATOM   38   C C   . ALA A 1 7   ? -10.05300 -30.17200 -29.81100 1.000 54.04000  ? 56  ALA A C   1 
ATOM   39   O O   . ALA A 1 7   ? -9.41700  -29.82500 -30.80600 1.000 53.75000  ? 56  ALA A O   1 
ATOM   40   C CB  . ALA A 1 7   ? -12.52200 -29.92500 -30.02900 1.000 65.99000  ? 56  ALA A CB  1 
ATOM   41   N N   . VAL A 1 8   ? -9.74800  -31.24100 -29.08400 1.000 54.26000  ? 57  VAL A N   1 
ATOM   42   C CA  . VAL A 1 8   ? -8.69700  -32.17700 -29.43400 1.000 56.86000  ? 57  VAL A CA  1 
ATOM   43   C C   . VAL A 1 8   ? -9.29200  -33.57300 -29.31100 1.000 57.80000  ? 57  VAL A C   1 
ATOM   44   O O   . VAL A 1 8   ? -10.36400 -33.76300 -28.73200 1.000 57.89000  ? 57  VAL A O   1 
ATOM   45   C CB  . VAL A 1 8   ? -7.45400  -32.02100 -28.53500 1.000 55.11000  ? 57  VAL A CB  1 
ATOM   46   C CG1 . VAL A 1 8   ? -6.98700  -30.53900 -28.46300 1.000 38.10000  ? 57  VAL A CG1 1 
ATOM   47   C CG2 . VAL A 1 8   ? -7.76600  -32.55800 -27.14500 1.000 56.11000  ? 57  VAL A CG2 1 
ATOM   48   N N   . SER A 1 9   ? -8.58500  -34.55500 -29.87200 1.000 50.58000  ? 58  SER A N   1 
ATOM   49   C CA  . SER A 1 9   ? -9.04500  -35.93700 -29.79600 1.000 57.78000  ? 58  SER A CA  1 
ATOM   50   C C   . SER A 1 9   ? -9.18500  -36.38400 -28.34800 1.000 61.50000  ? 58  SER A C   1 
ATOM   51   O O   . SER A 1 9   ? -8.28500  -36.17400 -27.53200 1.000 63.46000  ? 58  SER A O   1 
ATOM   52   C CB  . SER A 1 9   ? -8.08000  -36.87100 -30.52200 1.000 58.23000  ? 58  SER A CB  1 
ATOM   53   O OG  . SER A 1 9   ? -8.23600  -38.19700 -30.04000 1.000 65.11000  ? 58  SER A OG  1 
ATOM   54   N N   . ALA A 1 10  ? -10.30300 -37.05300 -28.05200 1.000 67.00000  ? 59  ALA A N   1 
ATOM   55   C CA  . ALA A 1 10  ? -10.59200 -37.50300 -26.69100 1.000 67.88000  ? 59  ALA A CA  1 
ATOM   56   C C   . ALA A 1 10  ? -9.50100  -38.41400 -26.14100 1.000 64.67000  ? 59  ALA A C   1 
ATOM   57   O O   . ALA A 1 10  ? -9.28800  -38.46300 -24.92200 1.000 64.08000  ? 59  ALA A O   1 
ATOM   58   C CB  . ALA A 1 10  ? -11.94400 -38.22000 -26.65400 1.000 51.59000  ? 59  ALA A CB  1 
ATOM   59   N N   . GLU A 1 11  ? -8.81000  -39.14600 -27.00600 1.000 61.78000  ? 60  GLU A N   1 
ATOM   60   C CA  . GLU A 1 11  ? -7.80800  -40.07700 -26.51900 1.000 64.17000  ? 60  GLU A CA  1 
ATOM   61   C C   . GLU A 1 11  ? -6.48800  -39.40400 -26.15800 1.000 67.24000  ? 60  GLU A C   1 
ATOM   62   O O   . GLU A 1 11  ? -5.54400  -40.09300 -25.74800 1.000 63.53000  ? 60  GLU A O   1 
ATOM   63   C CB  . GLU A 1 11  ? -7.61400  -41.19200 -27.54100 1.000 70.10000  ? 60  GLU A CB  1 
ATOM   64   C CG  . GLU A 1 11  ? -6.84100  -40.81400 -28.75500 1.000 75.14000  ? 60  GLU A CG  1 
ATOM   65   C CD  . GLU A 1 11  ? -6.69400  -42.00400 -29.68300 1.000 96.13000  ? 60  GLU A CD  1 
ATOM   66   O OE1 . GLU A 1 11  ? -7.39200  -43.02000 -29.43100 1.000 90.57000  ? 60  GLU A OE1 1 
ATOM   67   O OE2 . GLU A 1 11  ? -5.90400  -41.92400 -30.65800 1.000 91.22000  ? 60  GLU A OE2 1 
ATOM   68   N N   . ALA A 1 12  ? -6.39900  -38.08300 -26.27700 1.000 66.35000  ? 61  ALA A N   1 
ATOM   69   C CA  . ALA A 1 12  ? -5.22300  -37.34100 -25.84600 1.000 58.59000  ? 61  ALA A CA  1 
ATOM   70   C C   . ALA A 1 12  ? -5.38200  -36.76000 -24.45300 1.000 57.56000  ? 61  ALA A C   1 
ATOM   71   O O   . ALA A 1 12  ? -4.48200  -36.05800 -23.98600 1.000 60.39000  ? 61  ALA A O   1 
ATOM   72   C CB  . ALA A 1 12  ? -4.91200  -36.21100 -26.83400 1.000 54.55000  ? 61  ALA A CB  1 
ATOM   73   N N   . GLU A 1 13  ? -6.51100  -37.02500 -23.78700 1.000 61.53000  ? 62  GLU A N   1 
ATOM   74   C CA  . GLU A 1 13  ? -6.76700  -36.44500 -22.47100 1.000 58.00000  ? 62  GLU A CA  1 
ATOM   75   C C   . GLU A 1 13  ? -5.60400  -36.69100 -21.51900 1.000 61.19000  ? 62  GLU A C   1 
ATOM   76   O O   . GLU A 1 13  ? -5.21300  -35.79300 -20.76400 1.000 60.24000  ? 62  GLU A O   1 
ATOM   77   C CB  . GLU A 1 13  ? -8.06900  -37.01100 -21.90500 1.000 60.36000  ? 62  GLU A CB  1 
ATOM   78   C CG  . GLU A 1 13  ? -8.62000  -36.25500 -20.71300 1.000 67.91000  ? 62  GLU A CG  1 
ATOM   79   C CD  . GLU A 1 13  ? -10.06100 -36.63500 -20.36700 1.000 83.09000  ? 62  GLU A CD  1 
ATOM   80   O OE1 . GLU A 1 13  ? -10.87500 -36.90700 -21.29500 1.000 77.94000  ? 62  GLU A OE1 1 
ATOM   81   O OE2 . GLU A 1 13  ? -10.37600 -36.64800 -19.15400 1.000 81.02000  ? 62  GLU A OE2 1 
ATOM   82   N N   . ASN A 1 14  ? -5.00100  -37.88300 -21.58200 1.000 64.52000  ? 63  ASN A N   1 
ATOM   83   C CA  . ASN A 1 14  ? -3.89000  -38.21700 -20.69400 1.000 64.76000  ? 63  ASN A CA  1 
ATOM   84   C C   . ASN A 1 14  ? -2.75200  -37.22200 -20.86300 1.000 65.51000  ? 63  ASN A C   1 
ATOM   85   O O   . ASN A 1 14  ? -2.32500  -36.57300 -19.89800 1.000 67.18000  ? 63  ASN A O   1 
ATOM   86   C CB  . ASN A 1 14  ? -3.38500  -39.63100 -20.99000 1.000 69.48000  ? 63  ASN A CB  1 
ATOM   87   C CG  . ASN A 1 14  ? -4.31700  -40.70200 -20.47100 1.000 83.05000  ? 63  ASN A CG  1 
ATOM   88   O OD1 . ASN A 1 14  ? -5.00100  -40.51800 -19.45300 1.000 67.88000  ? 63  ASN A OD1 1 
ATOM   89   N ND2 . ASN A 1 14  ? -4.34700  -41.84100 -21.16800 1.000 82.76000  ? 63  ASN A ND2 1 
ATOM   90   N N   . LYS A 1 15  ? -2.24400  -37.10500 -22.09800 1.000 63.64000  ? 64  LYS A N   1 
ATOM   91   C CA  . LYS A 1 15  ? -1.17400  -36.15900 -22.40400 1.000 57.49000  ? 64  LYS A CA  1 
ATOM   92   C C   . LYS A 1 15  ? -1.52600  -34.74600 -21.93800 1.000 57.53000  ? 64  LYS A C   1 
ATOM   93   O O   . LYS A 1 15  ? -0.68800  -34.04500 -21.35600 1.000 55.77000  ? 64  LYS A O   1 
ATOM   94   C CB  . LYS A 1 15  ? -0.87700  -36.18600 -23.90300 1.000 63.35000  ? 64  LYS A CB  1 
ATOM   95   C CG  . LYS A 1 15  ? 0.20600   -37.18300 -24.34600 1.000 69.61000  ? 64  LYS A CG  1 
ATOM   96   C CD  . LYS A 1 15  ? -0.00400  -37.63200 -25.81600 1.000 79.41000  ? 64  LYS A CD  1 
ATOM   97   C CE  . LYS A 1 15  ? -0.84300  -38.91000 -25.95600 1.000 86.58000  ? 64  LYS A CE  1 
ATOM   98   N NZ  . LYS A 1 15  ? -0.01600  -40.15400 -26.17100 1.000 93.98000  ? 64  LYS A NZ  1 
ATOM   99   N N   . VAL A 1 16  ? -2.76400  -34.30800 -22.16900 1.000 58.13000  ? 65  VAL A N   1 
ATOM   100  C CA  . VAL A 1 16  ? -3.12600  -32.95100 -21.77000 1.000 58.99000  ? 65  VAL A CA  1 
ATOM   101  C C   . VAL A 1 16  ? -3.02200  -32.80300 -20.26300 1.000 55.87000  ? 65  VAL A C   1 
ATOM   102  O O   . VAL A 1 16  ? -2.40900  -31.85500 -19.75700 1.000 57.51000  ? 65  VAL A O   1 
ATOM   103  C CB  . VAL A 1 16  ? -4.53300  -32.58100 -22.26300 1.000 57.50000  ? 65  VAL A CB  1 
ATOM   104  C CG1 . VAL A 1 16  ? -4.92900  -31.21500 -21.70100 1.000 46.41000  ? 65  VAL A CG1 1 
ATOM   105  C CG2 . VAL A 1 16  ? -4.57000  -32.58200 -23.74900 1.000 48.64000  ? 65  VAL A CG2 1 
ATOM   106  N N   . ARG A 1 17  ? -3.63800  -33.72500 -19.51900 1.000 60.04000  ? 66  ARG A N   1 
ATOM   107  C CA  . ARG A 1 17  ? -3.64400  -33.58300 -18.06700 1.000 58.96000  ? 66  ARG A CA  1 
ATOM   108  C C   . ARG A 1 17  ? -2.24000  -33.64800 -17.50100 1.000 58.15000  ? 66  ARG A C   1 
ATOM   109  O O   . ARG A 1 17  ? -1.92300  -32.91400 -16.55800 1.000 59.82000  ? 66  ARG A O   1 
ATOM   110  C CB  . ARG A 1 17  ? -4.52900  -34.64900 -17.42700 1.000 53.92000  ? 66  ARG A CB  1 
ATOM   111  C CG  . ARG A 1 17  ? -5.91500  -34.13900 -17.19200 1.000 59.26000  ? 66  ARG A CG  1 
ATOM   112  C CD  . ARG A 1 17  ? -6.83900  -35.23000 -16.68900 1.000 64.96000  ? 66  ARG A CD  1 
ATOM   113  N NE  . ARG A 1 17  ? -8.24100  -35.00600 -17.03400 1.000 71.87000  ? 66  ARG A NE  1 
ATOM   114  C CZ  . ARG A 1 17  ? -8.95500  -33.92100 -16.73500 1.000 70.92000  ? 66  ARG A CZ  1 
ATOM   115  N NH1 . ARG A 1 17  ? -8.43600  -32.90100 -16.06100 1.000 66.44000  ? 66  ARG A NH1 1 
ATOM   116  N NH2 . ARG A 1 17  ? -10.23200 -33.86100 -17.11700 1.000 70.75000  ? 66  ARG A NH2 1 
ATOM   117  N N   . GLU A 1 18  ? -1.37000  -34.47100 -18.09400 1.000 53.49000  ? 67  GLU A N   1 
ATOM   118  C CA  . GLU A 1 18  ? 0.00100   -34.55500 -17.60500 1.000 49.70000  ? 67  GLU A CA  1 
ATOM   119  C C   . GLU A 1 18  ? 0.76900   -33.25500 -17.87400 1.000 63.20000  ? 67  GLU A C   1 
ATOM   120  O O   . GLU A 1 18  ? 1.48900   -32.76100 -16.99500 1.000 67.20000  ? 67  GLU A O   1 
ATOM   121  C CB  . GLU A 1 18  ? 0.68700   -35.78300 -18.20500 1.000 57.32000  ? 67  GLU A CB  1 
ATOM   122  C CG  . GLU A 1 18  ? 2.20600   -35.74900 -18.28400 1.000 66.94000  ? 67  GLU A CG  1 
ATOM   123  C CD  . GLU A 1 18  ? 2.77900   -36.99500 -18.99500 1.000 94.08000  ? 67  GLU A CD  1 
ATOM   124  O OE1 . GLU A 1 18  ? 1.98700   -37.76900 -19.58700 1.000 91.88000  ? 67  GLU A OE1 1 
ATOM   125  O OE2 . GLU A 1 18  ? 4.01800   -37.20600 -18.95700 1.000 93.53000  ? 67  GLU A OE2 1 
ATOM   126  N N   . GLN A 1 19  ? 0.61700   -32.66300 -19.06400 1.000 59.11000  ? 68  GLN A N   1 
ATOM   127  C CA  . GLN A 1 19  ? 1.34900   -31.43500 -19.37900 1.000 56.02000  ? 68  GLN A CA  1 
ATOM   128  C C   . GLN A 1 19  ? 0.66400   -30.16400 -18.87900 1.000 56.57000  ? 68  GLN A C   1 
ATOM   129  O O   . GLN A 1 19  ? 1.22400   -29.07500 -19.06400 1.000 57.96000  ? 68  GLN A O   1 
ATOM   130  C CB  . GLN A 1 19  ? 1.58300   -31.32700 -20.88500 1.000 59.31000  ? 68  GLN A CB  1 
ATOM   131  C CG  . GLN A 1 19  ? 2.32400   -32.50100 -21.45700 1.000 55.00000  ? 68  GLN A CG  1 
ATOM   132  C CD  . GLN A 1 19  ? 3.71800   -32.61400 -20.91100 1.000 55.00000  ? 68  GLN A CD  1 
ATOM   133  O OE1 . GLN A 1 19  ? 4.32300   -31.62300 -20.52800 1.000 60.14000  ? 68  GLN A OE1 1 
ATOM   134  N NE2 . GLN A 1 19  ? 4.24500   -33.82400 -20.88800 1.000 60.25000  ? 68  GLN A NE2 1 
ATOM   135  N N   . GLN A 1 20  ? -0.51500  -30.26500 -18.25800 1.000 52.67000  ? 69  GLN A N   1 
ATOM   136  C CA  . GLN A 1 20  ? -1.22300  -29.08000 -17.77500 1.000 55.41000  ? 69  GLN A CA  1 
ATOM   137  C C   . GLN A 1 20  ? -0.36200  -28.13600 -16.94000 1.000 55.10000  ? 69  GLN A C   1 
ATOM   138  O O   . GLN A 1 20  ? -0.27700  -26.94800 -17.29200 1.000 53.97000  ? 69  GLN A O   1 
ATOM   139  C CB  . GLN A 1 20  ? -2.43700  -29.51000 -16.94100 1.000 58.80000  ? 69  GLN A CB  1 
ATOM   140  C CG  . GLN A 1 20  ? -3.64200  -28.62000 -17.06400 1.000 65.63000  ? 69  GLN A CG  1 
ATOM   141  C CD  . GLN A 1 20  ? -4.86800  -29.22600 -16.41400 1.000 77.14000  ? 69  GLN A CD  1 
ATOM   142  O OE1 . GLN A 1 20  ? -5.70800  -29.84300 -17.08200 1.000 73.32000  ? 69  GLN A OE1 1 
ATOM   143  N NE2 . GLN A 1 20  ? -5.00000  -29.02200 -15.10400 1.000 74.14000  ? 69  GLN A NE2 1 
ATOM   144  N N   . PRO A 1 21  ? 0.30100   -28.57500 -15.85100 1.000 58.36000  ? 70  PRO A N   1 
ATOM   145  C CA  . PRO A 1 21  ? 1.10500   -27.61500 -15.06700 1.000 59.39000  ? 70  PRO A CA  1 
ATOM   146  C C   . PRO A 1 21  ? 2.18900   -26.95900 -15.88800 1.000 55.97000  ? 70  PRO A C   1 
ATOM   147  O O   . PRO A 1 21  ? 2.50000   -25.77000 -15.71900 1.000 50.28000  ? 70  PRO A O   1 
ATOM   148  C CB  . PRO A 1 21  ? 1.69400   -28.48600 -13.94300 1.000 50.20000  ? 70  PRO A CB  1 
ATOM   149  C CG  . PRO A 1 21  ? 1.71800   -29.84500 -14.50100 1.000 59.18000  ? 70  PRO A CG  1 
ATOM   150  C CD  . PRO A 1 21  ? 0.48700   -29.95500 -15.35200 1.000 51.99000  ? 70  PRO A CD  1 
ATOM   151  N N   . HIS A 1 22  ? 2.76700   -27.73000 -16.79800 1.000 55.89000  ? 71  HIS A N   1 
ATOM   152  C CA  . HIS A 1 22  ? 3.89300   -27.24500 -17.55900 1.000 48.09000  ? 71  HIS A CA  1 
ATOM   153  C C   . HIS A 1 22  ? 3.42600   -26.23700 -18.61800 1.000 56.77000  ? 71  HIS A C   1 
ATOM   154  O O   . HIS A 1 22  ? 4.10700   -25.23400 -18.86400 1.000 55.55000  ? 71  HIS A O   1 
ATOM   155  C CB  . HIS A 1 22  ? 4.59800   -28.47400 -18.12800 1.000 58.73000  ? 71  HIS A CB  1 
ATOM   156  C CG  . HIS A 1 22  ? 5.41700   -28.21000 -19.34700 1.000 73.23000  ? 71  HIS A CG  1 
ATOM   157  N ND1 . HIS A 1 22  ? 4.96000   -28.46900 -20.62200 1.000 71.96000  ? 71  HIS A ND1 1 
ATOM   158  C CD2 . HIS A 1 22  ? 6.71400   -27.83600 -19.47800 1.000 72.83000  ? 71  HIS A CD2 1 
ATOM   159  C CE1 . HIS A 1 22  ? 5.91400   -28.17800 -21.49200 1.000 77.74000  ? 71  HIS A CE1 1 
ATOM   160  N NE2 . HIS A 1 22  ? 6.99200   -27.80700 -20.82400 1.000 78.08000  ? 71  HIS A NE2 1 
ATOM   161  N N   . VAL A 1 23  ? 2.23200   -26.42700 -19.18700 1.000 50.97000  ? 72  VAL A N   1 
ATOM   162  C CA  . VAL A 1 23  ? 1.67700   -25.40100 -20.06800 1.000 50.11000  ? 72  VAL A CA  1 
ATOM   163  C C   . VAL A 1 23  ? 1.34000   -24.15100 -19.27500 1.000 47.00000  ? 72  VAL A C   1 
ATOM   164  O O   . VAL A 1 23  ? 1.67400   -23.03300 -19.67900 1.000 48.39000  ? 72  VAL A O   1 
ATOM   165  C CB  . VAL A 1 23  ? 0.43500   -25.92600 -20.81700 1.000 48.60000  ? 72  VAL A CB  1 
ATOM   166  C CG1 . VAL A 1 23  ? -0.22100  -24.80200 -21.60900 1.000 40.19000  ? 72  VAL A CG1 1 
ATOM   167  C CG2 . VAL A 1 23  ? 0.80600   -27.07900 -21.73700 1.000 46.52000  ? 72  VAL A CG2 1 
ATOM   168  N N   . GLU A 1 24  ? 0.69000   -24.32300 -18.12100 1.000 47.57000  ? 73  GLU A N   1 
ATOM   169  C CA  . GLU A 1 24  ? 0.29000   -23.15900 -17.33500 1.000 52.35000  ? 73  GLU A CA  1 
ATOM   170  C C   . GLU A 1 24  ? 1.50700   -22.35200 -16.89500 1.000 50.15000  ? 73  GLU A C   1 
ATOM   171  O O   . GLU A 1 24  ? 1.48100   -21.11600 -16.91800 1.000 53.04000  ? 73  GLU A O   1 
ATOM   172  C CB  . GLU A 1 24  ? -0.55600  -23.59000 -16.12900 1.000 54.41000  ? 73  GLU A CB  1 
ATOM   173  C CG  . GLU A 1 24  ? -2.00500  -24.00300 -16.50000 1.000 57.26000  ? 73  GLU A CG  1 
ATOM   174  C CD  . GLU A 1 24  ? -2.77500  -24.69900 -15.36600 1.000 72.29000  ? 73  GLU A CD  1 
ATOM   175  O OE1 . GLU A 1 24  ? -2.12100  -25.14600 -14.38500 1.000 79.48000  ? 73  GLU A OE1 1 
ATOM   176  O OE2 . GLU A 1 24  ? -4.03100  -24.82300 -15.47800 1.000 64.68000  ? 73  GLU A OE2 1 
ATOM   177  N N   . ARG A 1 25  ? 2.60400   -23.03000 -16.54700 1.000 46.02000  ? 74  ARG A N   1 
ATOM   178  C CA  . ARG A 1 25  ? 3.78600   -22.31600 -16.07300 1.000 46.31000  ? 74  ARG A CA  1 
ATOM   179  C C   . ARG A 1 25  ? 4.47600   -21.56100 -17.20300 1.000 47.37000  ? 74  ARG A C   1 
ATOM   180  O O   . ARG A 1 25  ? 4.86900   -20.40300 -17.02400 1.000 46.76000  ? 74  ARG A O   1 
ATOM   181  C CB  . ARG A 1 25  ? 4.77300   -23.28000 -15.40100 1.000 41.51000  ? 74  ARG A CB  1 
ATOM   182  C CG  . ARG A 1 25  ? 5.97500   -22.54300 -14.76600 1.000 46.45000  ? 74  ARG A CG  1 
ATOM   183  C CD  . ARG A 1 25  ? 6.98700   -23.49700 -14.12900 1.000 43.59000  ? 74  ARG A CD  1 
ATOM   184  N NE  . ARG A 1 25  ? 7.51400   -24.45500 -15.08800 1.000 51.04000  ? 74  ARG A NE  1 
ATOM   185  C CZ  . ARG A 1 25  ? 8.56400   -24.23100 -15.86200 1.000 51.08000  ? 74  ARG A CZ  1 
ATOM   186  N NH1 . ARG A 1 25  ? 9.25500   -23.10400 -15.77600 1.000 45.28000  ? 74  ARG A NH1 1 
ATOM   187  N NH2 . ARG A 1 25  ? 8.96000   -25.18100 -16.70700 1.000 44.84000  ? 74  ARG A NH2 1 
ATOM   188  N N   . ILE A 1 26  ? 4.67700   -22.21800 -18.35600 1.000 44.68000  ? 75  ILE A N   1 
ATOM   189  C CA  . ILE A 1 26  ? 5.45900   -21.62200 -19.44300 1.000 48.92000  ? 75  ILE A CA  1 
ATOM   190  C C   . ILE A 1 26  ? 4.69000   -20.51800 -20.14600 1.000 52.06000  ? 75  ILE A C   1 
ATOM   191  O O   . ILE A 1 26  ? 5.25700   -19.47100 -20.48900 1.000 51.48000  ? 75  ILE A O   1 
ATOM   192  C CB  . ILE A 1 26  ? 5.89700   -22.69700 -20.45000 1.000 50.24000  ? 75  ILE A CB  1 
ATOM   193  C CG1 . ILE A 1 26  ? 7.15100   -23.39000 -19.95400 1.000 46.97000  ? 75  ILE A CG1 1 
ATOM   194  C CG2 . ILE A 1 26  ? 6.12800   -22.09700 -21.84200 1.000 46.91000  ? 75  ILE A CG2 1 
ATOM   195  C CD1 . ILE A 1 26  ? 7.20300   -24.76900 -20.42200 1.000 50.52000  ? 75  ILE A CD1 1 
ATOM   196  N N   . PHE A 1 27  ? 3.39800   -20.73500 -20.39300 1.000 47.65000  ? 76  PHE A N   1 
ATOM   197  C CA  . PHE A 1 27  ? 2.60400   -19.79000 -21.17000 1.000 53.30000  ? 76  PHE A CA  1 
ATOM   198  C C   . PHE A 1 27  ? 1.75500   -18.86500 -20.30500 1.000 51.10000  ? 76  PHE A C   1 
ATOM   199  O O   . PHE A 1 27  ? 1.05300   -18.00900 -20.85700 1.000 42.55000  ? 76  PHE A O   1 
ATOM   200  C CB  . PHE A 1 27  ? 1.69900   -20.54000 -22.15300 1.000 42.87000  ? 76  PHE A CB  1 
ATOM   201  C CG  . PHE A 1 27  ? 2.44500   -21.32000 -23.17700 1.000 45.90000  ? 76  PHE A CG  1 
ATOM   202  C CD1 . PHE A 1 27  ? 2.93700   -20.69500 -24.31000 1.000 45.28000  ? 76  PHE A CD1 1 
ATOM   203  C CD2 . PHE A 1 27  ? 2.66600   -22.67700 -23.01100 1.000 41.61000  ? 76  PHE A CD2 1 
ATOM   204  C CE1 . PHE A 1 27  ? 3.62800   -21.41600 -25.27600 1.000 47.55000  ? 76  PHE A CE1 1 
ATOM   205  C CE2 . PHE A 1 27  ? 3.36100   -23.40400 -23.96600 1.000 43.23000  ? 76  PHE A CE2 1 
ATOM   206  C CZ  . PHE A 1 27  ? 3.84200   -22.77700 -25.10100 1.000 50.35000  ? 76  PHE A CZ  1 
ATOM   207  N N   . SER A 1 28  ? 1.84000   -18.99600 -18.97900 1.000 43.86000  ? 77  SER A N   1 
ATOM   208  C CA  . SER A 1 28  ? 1.04100   -18.23600 -18.00300 1.000 52.50000  ? 77  SER A CA  1 
ATOM   209  C C   . SER A 1 28  ? -0.42400  -18.15800 -18.43300 1.000 48.05000  ? 77  SER A C   1 
ATOM   210  O O   . SER A 1 28  ? -1.02500  -17.09100 -18.56300 1.000 48.85000  ? 77  SER A O   1 
ATOM   211  C CB  . SER A 1 28  ? 1.61600   -16.83100 -17.74300 1.000 49.64000  ? 77  SER A CB  1 
ATOM   212  O OG  . SER A 1 28  ? 2.31300   -16.28900 -18.86000 1.000 59.44000  ? 77  SER A OG  1 
ATOM   213  N N   . VAL A 1 29  ? -0.99900  -19.33300 -18.63900 1.000 46.76000  ? 78  VAL A N   1 
ATOM   214  C CA  . VAL A 1 29  ? -2.41800  -19.46400 -18.90800 1.000 49.72000  ? 78  VAL A CA  1 
ATOM   215  C C   . VAL A 1 29  ? -3.00300  -20.42800 -17.89400 1.000 54.57000  ? 78  VAL A C   1 
ATOM   216  O O   . VAL A 1 29  ? -2.29400  -21.04100 -17.09700 1.000 58.56000  ? 78  VAL A O   1 
ATOM   217  C CB  . VAL A 1 29  ? -2.70400  -19.97100 -20.33100 1.000 50.42000  ? 78  VAL A CB  1 
ATOM   218  C CG1 . VAL A 1 29  ? -2.01900  -19.09400 -21.38900 1.000 49.06000  ? 78  VAL A CG1 1 
ATOM   219  C CG2 . VAL A 1 29  ? -2.26700  -21.43000 -20.42600 1.000 44.99000  ? 78  VAL A CG2 1 
ATOM   220  N N   . GLY A 1 30  ? -4.32700  -20.53000 -17.91200 1.000 54.56000  ? 79  GLY A N   1 
ATOM   221  C CA  . GLY A 1 30  ? -5.02800  -21.62500 -17.28200 1.000 48.16000  ? 79  GLY A CA  1 
ATOM   222  C C   . GLY A 1 30  ? -5.60000  -22.50700 -18.38100 1.000 54.83000  ? 79  GLY A C   1 
ATOM   223  O O   . GLY A 1 30  ? -6.18500  -22.00400 -19.34200 1.000 56.77000  ? 79  GLY A O   1 
ATOM   224  N N   . VAL A 1 31  ? -5.40700  -23.81000 -18.23200 1.000 50.86000  ? 80  VAL A N   1 
ATOM   225  C CA  . VAL A 1 31  ? -6.00700  -24.77600 -19.13600 1.000 51.05000  ? 80  VAL A CA  1 
ATOM   226  C C   . VAL A 1 31  ? -6.95700  -25.64500 -18.33000 1.000 59.50000  ? 80  VAL A C   1 
ATOM   227  O O   . VAL A 1 31  ? -6.59100  -26.15100 -17.26400 1.000 63.29000  ? 80  VAL A O   1 
ATOM   228  C CB  . VAL A 1 31  ? -4.95700  -25.62200 -19.87200 1.000 49.11000  ? 80  VAL A CB  1 
ATOM   229  C CG1 . VAL A 1 31  ? -3.72400  -25.71100 -19.07700 1.000 59.16000  ? 80  VAL A CG1 1 
ATOM   230  C CG2 . VAL A 1 31  ? -5.52500  -27.00400 -20.17800 1.000 50.42000  ? 80  VAL A CG2 1 
ATOM   231  N N   . SER A 1 32  ? -8.19000  -25.76900 -18.81700 1.000 60.75000  ? 81  SER A N   1 
ATOM   232  C CA  . SER A 1 32  ? -9.19900  -26.63500 -18.23200 1.000 63.06000  ? 81  SER A CA  1 
ATOM   233  C C   . SER A 1 32  ? -9.72500  -27.59300 -19.29300 1.000 69.58000  ? 81  SER A C   1 
ATOM   234  O O   . SER A 1 32  ? -9.95000  -27.20500 -20.44700 1.000 69.92000  ? 81  SER A O   1 
ATOM   235  C CB  . SER A 1 32  ? -10.34600 -25.80900 -17.63900 1.000 64.69000  ? 81  SER A CB  1 
ATOM   236  O OG  . SER A 1 32  ? -10.48100 -24.57800 -18.33300 1.000 72.84000  ? 81  SER A OG  1 
ATOM   237  N N   . VAL A 1 33  ? -9.88500  -28.85300 -18.90000 1.000 67.03000  ? 82  VAL A N   1 
ATOM   238  C CA  . VAL A 1 33  ? -10.58900 -29.84700 -19.69700 1.000 61.81000  ? 82  VAL A CA  1 
ATOM   239  C C   . VAL A 1 33  ? -12.07200 -29.76500 -19.35100 1.000 69.50000  ? 82  VAL A C   1 
ATOM   240  O O   . VAL A 1 33  ? -12.48600 -30.13200 -18.24600 1.000 70.44000  ? 82  VAL A O   1 
ATOM   241  C CB  . VAL A 1 33  ? -10.03800 -31.25100 -19.43700 1.000 62.90000  ? 82  VAL A CB  1 
ATOM   242  C CG1 . VAL A 1 33  ? -10.65200 -32.26600 -20.39500 1.000 64.28000  ? 82  VAL A CG1 1 
ATOM   243  C CG2 . VAL A 1 33  ? -8.52400  -31.23900 -19.52200 1.000 52.38000  ? 82  VAL A CG2 1 
ATOM   244  N N   . LEU A 1 34  ? -12.87000 -29.24600 -20.28500 1.000 70.89000  ? 83  LEU A N   1 
ATOM   245  C CA  . LEU A 1 34  ? -14.29800 -29.14600 -20.06000 1.000 67.42000  ? 83  LEU A CA  1 
ATOM   246  C C   . LEU A 1 34  ? -14.88200 -30.55300 -19.92400 1.000 75.55000  ? 83  LEU A C   1 
ATOM   247  O O   . LEU A 1 34  ? -14.38400 -31.49800 -20.54800 1.000 80.46000  ? 83  LEU A O   1 
ATOM   248  C CB  . LEU A 1 34  ? -14.96600 -28.40000 -21.21100 1.000 58.95000  ? 83  LEU A CB  1 
ATOM   249  C CG  . LEU A 1 34  ? -14.50500 -26.95800 -21.47800 1.000 64.59000  ? 83  LEU A CG  1 
ATOM   250  C CD1 . LEU A 1 34  ? -15.35700 -26.26800 -22.54700 1.000 69.92000  ? 83  LEU A CD1 1 
ATOM   251  C CD2 . LEU A 1 34  ? -14.48000 -26.12700 -20.21800 1.000 62.19000  ? 83  LEU A CD2 1 
ATOM   252  N N   . PRO A 1 35  ? -15.90000 -30.73100 -19.07900 1.000 81.91000  ? 84  PRO A N   1 
ATOM   253  C CA  . PRO A 1 35  ? -16.55500 -32.04700 -18.96200 1.000 81.88000  ? 84  PRO A CA  1 
ATOM   254  C C   . PRO A 1 35  ? -17.28700 -32.39900 -20.24800 1.000 85.18000  ? 84  PRO A C   1 
ATOM   255  O O   . PRO A 1 35  ? -18.03800 -31.57600 -20.77800 1.000 89.02000  ? 84  PRO A O   1 
ATOM   256  C CB  . PRO A 1 35  ? -17.53300 -31.85400 -17.79600 1.000 79.19000  ? 84  PRO A CB  1 
ATOM   257  C CG  . PRO A 1 35  ? -17.04800 -30.60800 -17.09000 1.000 78.11000  ? 84  PRO A CG  1 
ATOM   258  C CD  . PRO A 1 35  ? -16.53400 -29.73700 -18.20100 1.000 75.87000  ? 84  PRO A CD  1 
ATOM   259  N N   . LYS A 1 36  ? -17.06600 -33.60700 -20.76900 1.000 104.04000 ? 85  LYS A N   1 
ATOM   260  C CA  . LYS A 1 36  ? -17.66400 -33.82700 -22.08100 1.000 100.03000 ? 85  LYS A CA  1 
ATOM   261  C C   . LYS A 1 36  ? -19.11600 -34.27700 -21.91800 1.000 95.30000  ? 85  LYS A C   1 
ATOM   262  O O   . LYS A 1 36  ? -19.50600 -34.87000 -20.90700 1.000 88.99000  ? 85  LYS A O   1 
ATOM   263  C CB  . LYS A 1 36  ? -16.86700 -34.80000 -22.96500 1.000 81.52000  ? 85  LYS A CB  1 
ATOM   264  C CG  . LYS A 1 36  ? -16.72700 -36.24700 -22.56100 1.000 95.66000  ? 85  LYS A CG  1 
ATOM   265  C CD  . LYS A 1 36  ? -15.25100 -36.62500 -22.64600 1.000 91.02000  ? 85  LYS A CD  1 
ATOM   266  C CE  . LYS A 1 36  ? -14.97700 -38.11900 -22.77700 1.000 95.67000  ? 85  LYS A CE  1 
ATOM   267  N NZ  . LYS A 1 36  ? -15.06200 -38.57300 -24.20100 1.000 90.17000  ? 85  LYS A NZ  1 
ATOM   268  N N   . ASP A 1 37  ? -19.90700 -34.00600 -22.96000 1.000 83.26000  ? 86  ASP A N   1 
ATOM   269  C CA  . ASP A 1 37  ? -21.35500 -34.18000 -22.93500 1.000 97.91000  ? 86  ASP A CA  1 
ATOM   270  C C   . ASP A 1 37  ? -21.81100 -35.61500 -23.16800 1.000 98.87000  ? 86  ASP A C   1 
ATOM   271  O O   . ASP A 1 37  ? -22.96300 -35.93600 -22.85300 1.000 93.82000  ? 86  ASP A O   1 
ATOM   272  C CB  . ASP A 1 37  ? -21.97500 -33.26200 -23.99300 1.000 94.77000  ? 86  ASP A CB  1 
ATOM   273  C CG  . ASP A 1 37  ? -21.28200 -31.90600 -24.05300 1.000 100.91000 ? 86  ASP A CG  1 
ATOM   274  O OD1 . ASP A 1 37  ? -20.16600 -31.82500 -24.62800 1.000 96.26000  ? 86  ASP A OD1 1 
ATOM   275  O OD2 . ASP A 1 37  ? -21.84800 -30.92300 -23.52000 1.000 101.37000 ? 86  ASP A OD2 1 
ATOM   276  N N   . CYS A 1 38  ? -20.95000 -36.47900 -23.70600 1.000 83.94000  ? 87  CYS A N   1 
ATOM   277  C CA  . CYS A 1 38  ? -21.29800 -37.86300 -23.91300 1.000 75.79000  ? 87  CYS A CA  1 
ATOM   278  C C   . CYS A 1 38  ? -19.95700 -38.57600 -23.87100 1.000 84.65000  ? 87  CYS A C   1 
ATOM   279  O O   . CYS A 1 38  ? -19.01300 -38.11600 -24.52500 1.000 82.55000  ? 87  CYS A O   1 
ATOM   280  C CB  . CYS A 1 38  ? -22.01600 -38.12100 -25.23500 1.000 88.24000  ? 87  CYS A CB  1 
ATOM   281  S SG  . CYS A 1 38  ? -22.25900 -39.86800 -25.63900 1.000 93.32000  ? 87  CYS A SG  1 
ATOM   282  N N   . PRO A 1 39  ? -19.82400 -39.65800 -23.09900 1.000 87.07000  ? 88  PRO A N   1 
ATOM   283  C CA  . PRO A 1 39  ? -18.49900 -40.29200 -22.94800 1.000 86.77000  ? 88  PRO A CA  1 
ATOM   284  C C   . PRO A 1 39  ? -18.00400 -41.00500 -24.19500 1.000 78.15000  ? 88  PRO A C   1 
ATOM   285  O O   . PRO A 1 39  ? -16.81400 -41.34100 -24.25300 1.000 75.87000  ? 88  PRO A O   1 
ATOM   286  C CB  . PRO A 1 39  ? -18.69200 -41.28700 -21.78900 1.000 84.87000  ? 88  PRO A CB  1 
ATOM   287  C CG  . PRO A 1 39  ? -20.06100 -41.06500 -21.25100 1.000 92.70000  ? 88  PRO A CG  1 
ATOM   288  C CD  . PRO A 1 39  ? -20.83000 -40.16100 -22.14900 1.000 83.02000  ? 88  PRO A CD  1 
ATOM   289  N N   . ASP A 1 40  ? -18.85900 -41.24300 -25.19000 1.000 80.25000  ? 89  ASP A N   1 
ATOM   290  C CA  . ASP A 1 40  ? -18.41900 -41.82800 -26.45300 1.000 84.44000  ? 89  ASP A CA  1 
ATOM   291  C C   . ASP A 1 40  ? -17.99400 -40.79400 -27.48300 1.000 82.49000  ? 89  ASP A C   1 
ATOM   292  O O   . ASP A 1 40  ? -17.61900 -41.18000 -28.59700 1.000 78.25000  ? 89  ASP A O   1 
ATOM   293  C CB  . ASP A 1 40  ? -19.51300 -42.70300 -27.07600 1.000 88.97000  ? 89  ASP A CB  1 
ATOM   294  C CG  . ASP A 1 40  ? -20.17700 -43.61000 -26.07600 1.000 96.46000  ? 89  ASP A CG  1 
ATOM   295  O OD1 . ASP A 1 40  ? -19.47000 -44.48400 -25.51400 1.000 88.15000  ? 89  ASP A OD1 1 
ATOM   296  O OD2 . ASP A 1 40  ? -21.40400 -43.46200 -25.87600 1.000 98.39000  ? 89  ASP A OD2 1 
ATOM   297  N N   . ASN A 1 41  ? -18.00700 -39.51100 -27.13900 1.000 77.43000  ? 90  ASN A N   1 
ATOM   298  C CA  . ASN A 1 41  ? -17.56700 -38.50900 -28.09100 1.000 69.67000  ? 90  ASN A CA  1 
ATOM   299  C C   . ASN A 1 41  ? -16.11600 -38.76700 -28.47700 1.000 68.95000  ? 90  ASN A C   1 
ATOM   300  O O   . ASN A 1 41  ? -15.31400 -39.20800 -27.64300 1.000 67.59000  ? 90  ASN A O   1 
ATOM   301  C CB  . ASN A 1 41  ? -17.71900 -37.11300 -27.49600 1.000 69.07000  ? 90  ASN A CB  1 
ATOM   302  C CG  . ASN A 1 41  ? -19.09500 -36.55800 -27.70800 1.000 77.05000  ? 90  ASN A CG  1 
ATOM   303  O OD1 . ASN A 1 41  ? -20.04900 -37.31800 -27.87000 1.000 74.41000  ? 90  ASN A OD1 1 
ATOM   304  N ND2 . ASN A 1 41  ? -19.22700 -35.23300 -27.64800 1.000 81.19000  ? 90  ASN A ND2 1 
ATOM   305  N N   . PRO A 1 42  ? -15.75200 -38.52700 -29.73900 1.000 66.89000  ? 91  PRO A N   1 
ATOM   306  C CA  . PRO A 1 42  ? -14.36800 -38.75600 -30.16500 1.000 62.68000  ? 91  PRO A CA  1 
ATOM   307  C C   . PRO A 1 42  ? -13.43700 -37.64800 -29.72900 1.000 61.66000  ? 91  PRO A C   1 
ATOM   308  O O   . PRO A 1 42  ? -12.21800 -37.77900 -29.90400 1.000 60.11000  ? 91  PRO A O   1 
ATOM   309  C CB  . PRO A 1 42  ? -14.48800 -38.80700 -31.68700 1.000 55.60000  ? 91  PRO A CB  1 
ATOM   310  C CG  . PRO A 1 42  ? -15.62500 -37.84000 -31.98000 1.000 64.42000  ? 91  PRO A CG  1 
ATOM   311  C CD  . PRO A 1 42  ? -16.56300 -37.88200 -30.79000 1.000 62.96000  ? 91  PRO A CD  1 
ATOM   312  N N   . HIS A 1 43  ? -13.98300 -36.57400 -29.16700 1.000 51.40000  ? 92  HIS A N   1 
ATOM   313  C CA  . HIS A 1 43  ? -13.24800 -35.36000 -28.89200 1.000 59.56000  ? 92  HIS A CA  1 
ATOM   314  C C   . HIS A 1 43  ? -13.54000 -34.88200 -27.47800 1.000 66.16000  ? 92  HIS A C   1 
ATOM   315  O O   . HIS A 1 43  ? -14.52800 -35.27500 -26.84400 1.000 65.92000  ? 92  HIS A O   1 
ATOM   316  C CB  . HIS A 1 43  ? -13.63200 -34.26100 -29.88000 1.000 58.26000  ? 92  HIS A CB  1 
ATOM   317  C CG  . HIS A 1 43  ? -15.06700 -33.85000 -29.78600 1.000 57.34000  ? 92  HIS A CG  1 
ATOM   318  N ND1 . HIS A 1 43  ? -16.10900 -34.72700 -30.00700 1.000 62.08000  ? 92  HIS A ND1 1 
ATOM   319  C CD2 . HIS A 1 43  ? -15.63400 -32.65400 -29.48900 1.000 56.89000  ? 92  HIS A CD2 1 
ATOM   320  C CE1 . HIS A 1 43  ? -17.25600 -34.08400 -29.85600 1.000 65.28000  ? 92  HIS A CE1 1 
ATOM   321  N NE2 . HIS A 1 43  ? -16.99500 -32.82500 -29.54200 1.000 54.19000  ? 92  HIS A NE2 1 
ATOM   322  N N   . ILE A 1 44  ? -12.67100 -33.99800 -27.00000 1.000 60.28000  ? 93  ILE A N   1 
ATOM   323  C CA  . ILE A 1 44  ? -12.86600 -33.29700 -25.73700 1.000 56.48000  ? 93  ILE A CA  1 
ATOM   324  C C   . ILE A 1 44  ? -12.53600 -31.84300 -25.98700 1.000 60.50000  ? 93  ILE A C   1 
ATOM   325  O O   . ILE A 1 44  ? -11.72700 -31.51100 -26.85900 1.000 64.81000  ? 93  ILE A O   1 
ATOM   326  C CB  . ILE A 1 44  ? -11.98800 -33.84100 -24.59500 1.000 61.96000  ? 93  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 44  ? -10.51300 -33.56300 -24.92800 1.000 58.86000  ? 93  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 44  ? -12.28900 -35.29800 -24.32700 1.000 62.01000  ? 93  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 44  ? -9.52200  -34.20600 -24.02200 1.000 62.97000  ? 93  ILE A CD1 1 
ATOM   330  N N   . TRP A 1 45  ? -13.16100 -30.97700 -25.21200 1.000 58.08000  ? 94  TRP A N   1 
ATOM   331  C CA  . TRP A 1 45  ? -13.00300 -29.54600 -25.36600 1.000 58.72000  ? 94  TRP A CA  1 
ATOM   332  C C   . TRP A 1 45  ? -12.03300 -29.03200 -24.31700 1.000 64.03000  ? 94  TRP A C   1 
ATOM   333  O O   . TRP A 1 45  ? -12.09500 -29.43200 -23.15200 1.000 61.97000  ? 94  TRP A O   1 
ATOM   334  C CB  . TRP A 1 45  ? -14.35300 -28.84900 -25.23700 1.000 63.38000  ? 94  TRP A CB  1 
ATOM   335  C CG  . TRP A 1 45  ? -15.21800 -29.11100 -26.41600 1.000 70.13000  ? 94  TRP A CG  1 
ATOM   336  C CD1 . TRP A 1 45  ? -16.21400 -30.04700 -26.52700 1.000 69.42000  ? 94  TRP A CD1 1 
ATOM   337  C CD2 . TRP A 1 45  ? -15.16600 -28.42900 -27.66600 1.000 66.73000  ? 94  TRP A CD2 1 
ATOM   338  N NE1 . TRP A 1 45  ? -16.78500 -29.98200 -27.77600 1.000 64.65000  ? 94  TRP A NE1 1 
ATOM   339  C CE2 . TRP A 1 45  ? -16.15500 -29.00000 -28.49500 1.000 68.87000  ? 94  TRP A CE2 1 
ATOM   340  C CE3 . TRP A 1 45  ? -14.38600 -27.38000 -28.16400 1.000 67.01000  ? 94  TRP A CE3 1 
ATOM   341  C CZ2 . TRP A 1 45  ? -16.37400 -28.56100 -29.79900 1.000 64.22000  ? 94  TRP A CZ2 1 
ATOM   342  C CZ3 . TRP A 1 45  ? -14.60500 -26.94800 -29.46200 1.000 63.07000  ? 94  TRP A CZ3 1 
ATOM   343  C CH2 . TRP A 1 45  ? -15.59100 -27.53500 -30.26100 1.000 57.07000  ? 94  TRP A CH2 1 
ATOM   344  N N   . LEU A 1 46  ? -11.12100 -28.17000 -24.74400 1.000 56.84000  ? 95  LEU A N   1 
ATOM   345  C CA  . LEU A 1 46  ? -10.20900 -27.49900 -23.84200 1.000 55.98000  ? 95  LEU A CA  1 
ATOM   346  C C   . LEU A 1 46  ? -10.52000 -26.01500 -23.83900 1.000 59.91000  ? 95  LEU A C   1 
ATOM   347  O O   . LEU A 1 46  ? -10.96600 -25.45400 -24.83800 1.000 60.41000  ? 95  LEU A O   1 
ATOM   348  C CB  . LEU A 1 46  ? -8.76000  -27.73100 -24.24400 1.000 57.28000  ? 95  LEU A CB  1 
ATOM   349  C CG  . LEU A 1 46  ? -8.41000  -29.19800 -24.45400 1.000 57.17000  ? 95  LEU A CG  1 
ATOM   350  C CD1 . LEU A 1 46  ? -7.01100  -29.29500 -25.02300 1.000 52.65000  ? 95  LEU A CD1 1 
ATOM   351  C CD2 . LEU A 1 46  ? -8.52000  -29.95700 -23.13500 1.000 60.33000  ? 95  LEU A CD2 1 
ATOM   352  N N   . GLN A 1 47  ? -10.28900 -25.39700 -22.69000 1.000 65.40000  ? 96  GLN A N   1 
ATOM   353  C CA  . GLN A 1 47  ? -10.62400 -24.00800 -22.43500 1.000 62.59000  ? 96  GLN A CA  1 
ATOM   354  C C   . GLN A 1 47  ? -9.37600  -23.34800 -21.87700 1.000 55.18000  ? 96  GLN A C   1 
ATOM   355  O O   . GLN A 1 47  ? -8.77000  -23.86500 -20.93400 1.000 61.31000  ? 96  GLN A O   1 
ATOM   356  C CB  . GLN A 1 47  ? -11.79600 -23.91700 -21.44100 1.000 69.39000  ? 96  GLN A CB  1 
ATOM   357  C CG  . GLN A 1 47  ? -12.20900 -22.51500 -21.02500 1.000 73.52000  ? 96  GLN A CG  1 
ATOM   358  C CD  . GLN A 1 47  ? -12.89800 -21.76800 -22.15600 1.000 82.55000  ? 96  GLN A CD  1 
ATOM   359  O OE1 . GLN A 1 47  ? -12.27100 -20.96800 -22.85200 1.000 87.57000  ? 96  GLN A OE1 1 
ATOM   360  N NE2 . GLN A 1 47  ? -14.19500 -22.03100 -22.34800 1.000 77.30000  ? 96  GLN A NE2 1 
ATOM   361  N N   . LEU A 1 48  ? -8.97600  -22.23400 -22.47000 1.000 53.16000  ? 97  LEU A N   1 
ATOM   362  C CA  . LEU A 1 48  ? -7.78200  -21.50800 -22.06200 1.000 53.79000  ? 97  LEU A CA  1 
ATOM   363  C C   . LEU A 1 48  ? -8.15800  -20.15800 -21.45300 1.000 64.64000  ? 97  LEU A C   1 
ATOM   364  O O   . LEU A 1 48  ? -9.13400  -19.52300 -21.87000 1.000 67.79000  ? 97  LEU A O   1 
ATOM   365  C CB  . LEU A 1 48  ? -6.82300  -21.32500 -23.25100 1.000 47.07000  ? 97  LEU A CB  1 
ATOM   366  C CG  . LEU A 1 48  ? -6.17500  -22.63800 -23.74200 1.000 51.64000  ? 97  LEU A CG  1 
ATOM   367  C CD1 . LEU A 1 48  ? -5.10400  -22.37900 -24.79700 1.000 53.03000  ? 97  LEU A CD1 1 
ATOM   368  C CD2 . LEU A 1 48  ? -5.58400  -23.43400 -22.58600 1.000 54.43000  ? 97  LEU A CD2 1 
ATOM   369  N N   . GLU A 1 49  ? -7.39800  -19.73800 -20.44300 1.000 59.53000  ? 98  GLU A N   1 
ATOM   370  C CA  . GLU A 1 49  ? -7.63500  -18.48400 -19.74200 1.000 59.71000  ? 98  GLU A CA  1 
ATOM   371  C C   . GLU A 1 49  ? -6.35800  -17.67300 -19.74100 1.000 55.06000  ? 98  GLU A C   1 
ATOM   372  O O   . GLU A 1 49  ? -5.30500  -18.18900 -19.36600 1.000 60.35000  ? 98  GLU A O   1 
ATOM   373  C CB  . GLU A 1 49  ? -8.05400  -18.74300 -18.30300 1.000 60.06000  ? 98  GLU A CB  1 
ATOM   374  C CG  . GLU A 1 49  ? -9.44500  -19.30300 -18.14200 1.000 80.33000  ? 98  GLU A CG  1 
ATOM   375  C CD  . GLU A 1 49  ? -10.39200 -18.29100 -17.53700 1.000 95.31000  ? 98  GLU A CD  1 
ATOM   376  O OE1 . GLU A 1 49  ? -10.07000 -17.07900 -17.58500 1.000 86.80000  ? 98  GLU A OE1 1 
ATOM   377  O OE2 . GLU A 1 49  ? -11.44500 -18.71100 -16.99400 1.000 98.76000  ? 98  GLU A OE2 1 
ATOM   378  N N   . GLY A 1 50  ? -6.44700  -16.41500 -20.13600 1.000 50.97000  ? 99  GLY A N   1 
ATOM   379  C CA  . GLY A 1 50  ? -5.31400  -15.52700 -20.05400 1.000 45.08000  ? 99  GLY A CA  1 
ATOM   380  C C   . GLY A 1 50  ? -5.22700  -14.63300 -21.26200 1.000 54.34000  ? 99  GLY A C   1 
ATOM   381  O O   . GLY A 1 50  ? -6.10100  -14.64600 -22.13100 1.000 53.82000  ? 99  GLY A O   1 
ATOM   382  N N   . PRO A 1 51  ? -4.15600  -13.84500 -21.34400 1.000 56.61000  ? 100 PRO A N   1 
ATOM   383  C CA  . PRO A 1 51  ? -3.99900  -12.90100 -22.46100 1.000 52.79000  ? 100 PRO A CA  1 
ATOM   384  C C   . PRO A 1 51  ? -4.07700  -13.58400 -23.81800 1.000 55.27000  ? 100 PRO A C   1 
ATOM   385  O O   . PRO A 1 51  ? -3.86200  -14.78900 -23.96400 1.000 54.39000  ? 100 PRO A O   1 
ATOM   386  C CB  . PRO A 1 51  ? -2.61100  -12.29700 -22.23200 1.000 47.77000  ? 100 PRO A CB  1 
ATOM   387  C CG  . PRO A 1 51  ? -2.23600  -12.68300 -20.81300 1.000 46.30000  ? 100 PRO A CG  1 
ATOM   388  C CD  . PRO A 1 51  ? -2.94800  -13.94200 -20.51200 1.000 44.90000  ? 100 PRO A CD  1 
ATOM   389  N N   . LYS A 1 52  ? -4.38800  -12.77600 -24.83000 1.000 59.46000  ? 101 LYS A N   1 
ATOM   390  C CA  . LYS A 1 52  ? -4.65100  -13.30000 -26.16400 1.000 60.67000  ? 101 LYS A CA  1 
ATOM   391  C C   . LYS A 1 52  ? -3.41100  -13.96600 -26.76200 1.000 56.93000  ? 101 LYS A C   1 
ATOM   392  O O   . LYS A 1 52  ? -3.50800  -15.04700 -27.35700 1.000 58.68000  ? 101 LYS A O   1 
ATOM   393  C CB  . LYS A 1 52  ? -5.15300  -12.15600 -27.05300 1.000 69.48000  ? 101 LYS A CB  1 
ATOM   394  C CG  . LYS A 1 52  ? -6.02400  -12.55700 -28.22900 1.000 75.48000  ? 101 LYS A CG  1 
ATOM   395  C CD  . LYS A 1 52  ? -5.70200  -11.73800 -29.49200 1.000 83.33000  ? 101 LYS A CD  1 
ATOM   396  C CE  . LYS A 1 52  ? -6.10700  -12.47800 -30.78500 1.000 86.60000  ? 101 LYS A CE  1 
ATOM   397  N NZ  . LYS A 1 52  ? -5.06200  -13.40900 -31.34700 1.000 79.08000  ? 101 LYS A NZ  1 
ATOM   398  N N   . GLU A 1 53  ? -2.23300  -13.35100 -26.58800 1.000 52.31000  ? 102 GLU A N   1 
ATOM   399  C CA  . GLU A 1 53  ? -1.00300  -13.88800 -27.17500 1.000 54.83000  ? 102 GLU A CA  1 
ATOM   400  C C   . GLU A 1 53  ? -0.62500  -15.22700 -26.55500 1.000 54.34000  ? 102 GLU A C   1 
ATOM   401  O O   . GLU A 1 53  ? -0.32700  -16.19300 -27.26800 1.000 59.13000  ? 102 GLU A O   1 
ATOM   402  C CB  . GLU A 1 53  ? 0.14300   -12.88800 -27.00900 1.000 53.29000  ? 102 GLU A CB  1 
ATOM   403  C CG  . GLU A 1 53  ? 1.41600   -13.27600 -27.76000 1.000 60.62000  ? 102 GLU A CG  1 
ATOM   404  C CD  . GLU A 1 53  ? 1.20300   -13.46100 -29.27000 1.000 71.01000  ? 102 GLU A CD  1 
ATOM   405  O OE1 . GLU A 1 53  ? 0.21900   -12.90700 -29.81100 1.000 79.17000  ? 102 GLU A OE1 1 
ATOM   406  O OE2 . GLU A 1 53  ? 2.01300   -14.17700 -29.91600 1.000 67.24000  ? 102 GLU A OE2 1 
ATOM   407  N N   . ASN A 1 54  ? -0.64000  -15.29500 -25.22600 1.000 48.00000  ? 103 ASN A N   1 
ATOM   408  C CA  . ASN A 1 54  ? -0.32600  -16.52200 -24.51000 1.000 45.33000  ? 103 ASN A CA  1 
ATOM   409  C C   . ASN A 1 54  ? -1.24700  -17.65700 -24.93000 1.000 48.08000  ? 103 ASN A C   1 
ATOM   410  O O   . ASN A 1 54  ? -0.78700  -18.76500 -25.23800 1.000 49.88000  ? 103 ASN A O   1 
ATOM   411  C CB  . ASN A 1 54  ? -0.44000  -16.27000 -23.00500 1.000 48.92000  ? 103 ASN A CB  1 
ATOM   412  C CG  . ASN A 1 54  ? 0.38600   -15.07900 -22.54400 1.000 51.70000  ? 103 ASN A CG  1 
ATOM   413  O OD1 . ASN A 1 54  ? 0.26500   -13.97500 -23.06900 1.000 48.48000  ? 103 ASN A OD1 1 
ATOM   414  N ND2 . ASN A 1 54  ? 1.23100   -15.30200 -21.53800 1.000 64.25000  ? 103 ASN A ND2 1 
ATOM   415  N N   . ALA A 1 55  ? -2.55900  -17.40200 -24.93100 1.000 53.55000  ? 104 ALA A N   1 
ATOM   416  C CA  . ALA A 1 55  ? -3.53500  -18.43900 -25.25900 1.000 48.81000  ? 104 ALA A CA  1 
ATOM   417  C C   . ALA A 1 55  ? -3.31200  -18.97900 -26.65700 1.000 51.47000  ? 104 ALA A C   1 
ATOM   418  O O   . ALA A 1 55  ? -3.44500  -20.18500 -26.90200 1.000 53.34000  ? 104 ALA A O   1 
ATOM   419  C CB  . ALA A 1 55  ? -4.94500  -17.87700 -25.14700 1.000 43.64000  ? 104 ALA A CB  1 
ATOM   420  N N   . SER A 1 56  ? -2.99700  -18.09100 -27.59300 1.000 50.20000  ? 105 SER A N   1 
ATOM   421  C CA  . SER A 1 56  ? -2.73100  -18.50700 -28.96000 1.000 50.80000  ? 105 SER A CA  1 
ATOM   422  C C   . SER A 1 56  ? -1.52300  -19.43800 -29.01200 1.000 53.22000  ? 105 SER A C   1 
ATOM   423  O O   . SER A 1 56  ? -1.56900  -20.50800 -29.64100 1.000 42.71000  ? 105 SER A O   1 
ATOM   424  C CB  . SER A 1 56  ? -2.53200  -17.25500 -29.82500 1.000 54.45000  ? 105 SER A CB  1 
ATOM   425  O OG  . SER A 1 56  ? -1.83900  -17.54300 -31.02000 1.000 65.98000  ? 105 SER A OG  1 
ATOM   426  N N   . ARG A 1 57  ? -0.42500  -19.04600 -28.35000 1.000 48.69000  ? 106 ARG A N   1 
ATOM   427  C CA  . ARG A 1 57  ? 0.75600   -19.90200 -28.33500 1.000 48.19000  ? 106 ARG A CA  1 
ATOM   428  C C   . ARG A 1 57  ? 0.49000   -21.18200 -27.55300 1.000 49.16000  ? 106 ARG A C   1 
ATOM   429  O O   . ARG A 1 57  ? 0.96100   -22.25700 -27.94500 1.000 51.44000  ? 106 ARG A O   1 
ATOM   430  C CB  . ARG A 1 57  ? 1.96000   -19.16100 -27.77100 1.000 48.47000  ? 106 ARG A CB  1 
ATOM   431  C CG  . ARG A 1 57  ? 2.21300   -17.81600 -28.41200 1.000 48.24000  ? 106 ARG A CG  1 
ATOM   432  C CD  . ARG A 1 57  ? 3.52500   -17.18600 -27.93700 1.000 47.77000  ? 106 ARG A CD  1 
ATOM   433  N NE  . ARG A 1 57  ? 3.90700   -16.05400 -28.77600 1.000 48.85000  ? 106 ARG A NE  1 
ATOM   434  C CZ  . ARG A 1 57  ? 5.14800   -15.68600 -29.06900 1.000 51.39000  ? 106 ARG A CZ  1 
ATOM   435  N NH1 . ARG A 1 57  ? 6.19900   -16.36000 -28.63300 1.000 53.89000  ? 106 ARG A NH1 1 
ATOM   436  N NH2 . ARG A 1 57  ? 5.34100   -14.60300 -29.81200 1.000 64.76000  ? 106 ARG A NH2 1 
ATOM   437  N N   . ALA A 1 58  ? -0.27100  -21.09700 -26.45600 1.000 42.49000  ? 107 ALA A N   1 
ATOM   438  C CA  . ALA A 1 58  ? -0.56900  -22.31100 -25.69300 1.000 42.99000  ? 107 ALA A CA  1 
ATOM   439  C C   . ALA A 1 58  ? -1.44200  -23.26800 -26.49200 1.000 45.35000  ? 107 ALA A C   1 
ATOM   440  O O   . ALA A 1 58  ? -1.34100  -24.49100 -26.31600 1.000 41.45000  ? 107 ALA A O   1 
ATOM   441  C CB  . ALA A 1 58  ? -1.24900  -21.97400 -24.36200 1.000 44.10000  ? 107 ALA A CB  1 
ATOM   442  N N   . LYS A 1 59  ? -2.31000  -22.73500 -27.36300 1.000 45.92000  ? 108 LYS A N   1 
ATOM   443  C CA  . LYS A 1 59  ? -3.14100  -23.60500 -28.19200 1.000 47.20000  ? 108 LYS A CA  1 
ATOM   444  C C   . LYS A 1 59  ? -2.28300  -24.36900 -29.19500 1.000 46.96000  ? 108 LYS A C   1 
ATOM   445  O O   . LYS A 1 59  ? -2.42000  -25.58900 -29.34200 1.000 46.79000  ? 108 LYS A O   1 
ATOM   446  C CB  . LYS A 1 59  ? -4.22200  -22.79600 -28.92700 1.000 52.93000  ? 108 LYS A CB  1 
ATOM   447  C CG  . LYS A 1 59  ? -5.29200  -23.69400 -29.60000 1.000 59.41000  ? 108 LYS A CG  1 
ATOM   448  C CD  . LYS A 1 59  ? -5.97900  -23.08600 -30.83000 1.000 59.49000  ? 108 LYS A CD  1 
ATOM   449  C CE  . LYS A 1 59  ? -6.89700  -21.92200 -30.51600 1.000 61.40000  ? 108 LYS A CE  1 
ATOM   450  N NZ  . LYS A 1 59  ? -7.07200  -21.05900 -31.73300 1.000 76.28000  ? 108 LYS A NZ  1 
ATOM   451  N N   . GLU A 1 60  ? -1.37800  -23.66600 -29.87800 1.000 41.22000  ? 109 GLU A N   1 
ATOM   452  C CA  . GLU A 1 60  ? -0.45300  -24.32300 -30.79000 1.000 47.43000  ? 109 GLU A CA  1 
ATOM   453  C C   . GLU A 1 60  ? 0.29800   -25.43600 -30.07200 1.000 49.34000  ? 109 GLU A C   1 
ATOM   454  O O   . GLU A 1 60  ? 0.41500   -26.56400 -30.57600 1.000 45.77000  ? 109 GLU A O   1 
ATOM   455  C CB  . GLU A 1 60  ? 0.51100   -23.28300 -31.37400 1.000 52.36000  ? 109 GLU A CB  1 
ATOM   456  C CG  . GLU A 1 60  ? 0.48600   -23.14800 -32.88900 1.000 58.42000  ? 109 GLU A CG  1 
ATOM   457  C CD  . GLU A 1 60  ? 1.65700   -22.31400 -33.44000 1.000 78.58000  ? 109 GLU A CD  1 
ATOM   458  O OE1 . GLU A 1 60  ? 1.61000   -21.06400 -33.31100 1.000 85.81000  ? 109 GLU A OE1 1 
ATOM   459  O OE2 . GLU A 1 60  ? 2.60700   -22.89900 -34.02100 1.000 69.65000  ? 109 GLU A OE2 1 
ATOM   460  N N   . TYR A 1 61  ? 0.78200   -25.14100 -28.86300 1.000 45.62000  ? 110 TYR A N   1 
ATOM   461  C CA  . TYR A 1 61  ? 1.48300   -26.15700 -28.08900 1.000 41.86000  ? 110 TYR A CA  1 
ATOM   462  C C   . TYR A 1 61  ? 0.57000   -27.34400 -27.80400 1.000 39.85000  ? 110 TYR A C   1 
ATOM   463  O O   . TYR A 1 61  ? 0.93000   -28.49400 -28.05800 1.000 43.16000  ? 110 TYR A O   1 
ATOM   464  C CB  . TYR A 1 61  ? 2.01100   -25.54200 -26.79100 1.000 48.44000  ? 110 TYR A CB  1 
ATOM   465  C CG  . TYR A 1 61  ? 2.78600   -26.52500 -25.96000 1.000 49.06000  ? 110 TYR A CG  1 
ATOM   466  C CD1 . TYR A 1 61  ? 2.13300   -27.41600 -25.12700 1.000 45.20000  ? 110 TYR A CD1 1 
ATOM   467  C CD2 . TYR A 1 61  ? 4.16600   -26.59400 -26.04600 1.000 53.56000  ? 110 TYR A CD2 1 
ATOM   468  C CE1 . TYR A 1 61  ? 2.82500   -28.33800 -24.38700 1.000 59.65000  ? 110 TYR A CE1 1 
ATOM   469  C CE2 . TYR A 1 61  ? 4.87800   -27.51400 -25.30600 1.000 56.41000  ? 110 TYR A CE2 1 
ATOM   470  C CZ  . TYR A 1 61  ? 4.19800   -28.38200 -24.46900 1.000 65.05000  ? 110 TYR A CZ  1 
ATOM   471  O OH  . TYR A 1 61  ? 4.88100   -29.32000 -23.72000 1.000 75.20000  ? 110 TYR A OH  1 
ATOM   472  N N   . LEU A 1 62  ? -0.63300  -27.08100 -27.30400 1.000 38.87000  ? 111 LEU A N   1 
ATOM   473  C CA  . LEU A 1 62  ? -1.54200  -28.17000 -26.96500 1.000 42.29000  ? 111 LEU A CA  1 
ATOM   474  C C   . LEU A 1 62  ? -1.94400  -28.98100 -28.18900 1.000 49.38000  ? 111 LEU A C   1 
ATOM   475  O O   . LEU A 1 62  ? -2.04700  -30.21000 -28.10800 1.000 51.25000  ? 111 LEU A O   1 
ATOM   476  C CB  . LEU A 1 62  ? -2.76800  -27.62000 -26.24600 1.000 42.84000  ? 111 LEU A CB  1 
ATOM   477  C CG  . LEU A 1 62  ? -2.45800  -27.27300 -24.78100 1.000 43.60000  ? 111 LEU A CG  1 
ATOM   478  C CD1 . LEU A 1 62  ? -3.60500  -26.54400 -24.15800 1.000 47.12000  ? 111 LEU A CD1 1 
ATOM   479  C CD2 . LEU A 1 62  ? -2.11700  -28.49600 -23.98000 1.000 42.78000  ? 111 LEU A CD2 1 
ATOM   480  N N   . LYS A 1 63  ? -2.23900  -28.31800 -29.31400 1.000 44.95000  ? 112 LYS A N   1 
ATOM   481  C CA  . LYS A 1 63  ? -2.57700  -29.06500 -30.52200 1.000 46.47000  ? 112 LYS A CA  1 
ATOM   482  C C   . LYS A 1 63  ? -1.39500  -29.91500 -30.98800 1.000 55.86000  ? 112 LYS A C   1 
ATOM   483  O O   . LYS A 1 63  ? -1.57600  -31.07800 -31.37700 1.000 55.67000  ? 112 LYS A O   1 
ATOM   484  C CB  . LYS A 1 63  ? -3.03700  -28.11700 -31.64300 1.000 50.22000  ? 112 LYS A CB  1 
ATOM   485  C CG  . LYS A 1 63  ? -4.35000  -27.35900 -31.40400 1.000 51.42000  ? 112 LYS A CG  1 
ATOM   486  C CD  . LYS A 1 63  ? -4.92300  -26.77500 -32.71300 1.000 49.02000  ? 112 LYS A CD  1 
ATOM   487  C CE  . LYS A 1 63  ? -6.46100  -26.79900 -32.73300 1.000 67.81000  ? 112 LYS A CE  1 
ATOM   488  N NZ  . LYS A 1 63  ? -7.06200  -25.59500 -33.40600 1.000 65.83000  ? 112 LYS A NZ  1 
ATOM   489  N N   . GLY A 1 64  ? -0.17200  -29.35400 -30.95100 1.000 49.45000  ? 113 GLY A N   1 
ATOM   490  C CA  . GLY A 1 64  ? 1.01300   -30.12600 -31.32100 1.000 50.91000  ? 113 GLY A CA  1 
ATOM   491  C C   . GLY A 1 64  ? 1.31500   -31.27700 -30.36900 1.000 53.25000  ? 113 GLY A C   1 
ATOM   492  O O   . GLY A 1 64  ? 1.94600   -32.27200 -30.75000 1.000 51.22000  ? 113 GLY A O   1 
ATOM   493  N N   . LEU A 1 65  ? 0.88300   -31.15500 -29.12100 1.000 50.92000  ? 114 LEU A N   1 
ATOM   494  C CA  . LEU A 1 65  ? 1.04900   -32.24400 -28.16800 1.000 53.99000  ? 114 LEU A CA  1 
ATOM   495  C C   . LEU A 1 65  ? 0.07900   -33.38300 -28.46400 1.000 53.92000  ? 114 LEU A C   1 
ATOM   496  O O   . LEU A 1 65  ? 0.45100   -34.56000 -28.39200 1.000 50.71000  ? 114 LEU A O   1 
ATOM   497  C CB  . LEU A 1 65  ? 0.83600   -31.69700 -26.75800 1.000 48.72000  ? 114 LEU A CB  1 
ATOM   498  C CG  . LEU A 1 65  ? 1.20400   -32.58000 -25.58200 1.000 57.87000  ? 114 LEU A CG  1 
ATOM   499  C CD1 . LEU A 1 65  ? 2.68200   -32.49700 -25.31100 1.000 60.47000  ? 114 LEU A CD1 1 
ATOM   500  C CD2 . LEU A 1 65  ? 0.42400   -32.11100 -24.37600 1.000 61.89000  ? 114 LEU A CD2 1 
ATOM   501  N N   . CYS A 1 66  ? -1.15200  -33.04700 -28.86500 1.000 53.89000  ? 115 CYS A N   1 
ATOM   502  C CA  . CYS A 1 66  ? -2.20800  -34.04300 -29.01700 1.000 51.10000  ? 115 CYS A CA  1 
ATOM   503  C C   . CYS A 1 66  ? -2.15400  -34.76700 -30.36100 1.000 55.34000  ? 115 CYS A C   1 
ATOM   504  O O   . CYS A 1 66  ? -2.60400  -35.91200 -30.46600 1.000 50.79000  ? 115 CYS A O   1 
ATOM   505  C CB  . CYS A 1 66  ? -3.56300  -33.37500 -28.80800 1.000 49.53000  ? 115 CYS A CB  1 
ATOM   506  S SG  . CYS A 1 66  ? -3.72400  -32.60200 -27.13800 1.000 58.66000  ? 115 CYS A SG  1 
ATOM   507  N N   . SER A 1 67  ? -1.67200  -34.11300 -31.40600 1.000 56.18000  ? 116 SER A N   1 
ATOM   508  C CA  . SER A 1 67  ? -1.41000  -34.77600 -32.68000 1.000 58.60000  ? 116 SER A CA  1 
ATOM   509  C C   . SER A 1 67  ? -0.18700  -34.10600 -33.28200 1.000 53.56000  ? 116 SER A C   1 
ATOM   510  O O   . SER A 1 67  ? -0.29400  -33.16100 -34.07200 1.000 60.28000  ? 116 SER A O   1 
ATOM   511  C CB  . SER A 1 67  ? -2.64000  -34.73500 -33.59700 1.000 56.59000  ? 116 SER A CB  1 
ATOM   512  O OG  . SER A 1 67  ? -2.65400  -33.59200 -34.43900 1.000 69.11000  ? 116 SER A OG  1 
ATOM   513  N N   . PRO A 1 68  ? 1.00600   -34.53400 -32.88700 1.000 51.87000  ? 117 PRO A N   1 
ATOM   514  C CA  . PRO A 1 68  ? 2.20600   -33.94200 -33.47400 1.000 47.38000  ? 117 PRO A CA  1 
ATOM   515  C C   . PRO A 1 68  ? 2.25200   -34.26300 -34.96000 1.000 53.19000  ? 117 PRO A C   1 
ATOM   516  O O   . PRO A 1 68  ? 1.91100   -35.36900 -35.37700 1.000 53.72000  ? 117 PRO A O   1 
ATOM   517  C CB  . PRO A 1 68  ? 3.35400   -34.60500 -32.69900 1.000 47.51000  ? 117 PRO A CB  1 
ATOM   518  C CG  . PRO A 1 68  ? 2.78200   -35.84600 -32.10500 1.000 41.44000  ? 117 PRO A CG  1 
ATOM   519  C CD  . PRO A 1 68  ? 1.32100   -35.57900 -31.89400 1.000 51.66000  ? 117 PRO A CD  1 
ATOM   520  N N   . GLU A 1 69  ? 2.60900   -33.26500 -35.76700 1.000 46.28000  ? 118 GLU A N   1 
ATOM   521  C CA  . GLU A 1 69  ? 2.81900   -33.51000 -37.18400 1.000 52.86000  ? 118 GLU A CA  1 
ATOM   522  C C   . GLU A 1 69  ? 4.25700   -33.91300 -37.47600 1.000 55.40000  ? 118 GLU A C   1 
ATOM   523  O O   . GLU A 1 69  ? 4.50600   -34.62000 -38.45900 1.000 56.07000  ? 118 GLU A O   1 
ATOM   524  C CB  . GLU A 1 69  ? 2.43700   -32.26700 -38.00800 1.000 48.35000  ? 118 GLU A CB  1 
ATOM   525  C CG  . GLU A 1 69  ? 0.95500   -31.88800 -37.88200 1.000 46.85000  ? 118 GLU A CG  1 
ATOM   526  C CD  . GLU A 1 69  ? 0.65500   -30.39600 -38.12400 1.000 59.98000  ? 118 GLU A CD  1 
ATOM   527  O OE1 . GLU A 1 69  ? 1.59900   -29.57600 -38.27400 1.000 61.53000  ? 118 GLU A OE1 1 
ATOM   528  O OE2 . GLU A 1 69  ? -0.54800  -30.03700 -38.13400 1.000 55.99000  ? 118 GLU A OE2 1 
ATOM   529  N N   . LEU A 1 70  ? 5.20400   -33.49900 -36.63200 1.000 49.60000  ? 119 LEU A N   1 
ATOM   530  C CA  . LEU A 1 70  ? 6.60500   -33.85700 -36.79300 1.000 48.46000  ? 119 LEU A CA  1 
ATOM   531  C C   . LEU A 1 70  ? 7.19600   -34.16900 -35.43200 1.000 53.33000  ? 119 LEU A C   1 
ATOM   532  O O   . LEU A 1 70  ? 6.83300   -33.56600 -34.41700 1.000 55.73000  ? 119 LEU A O   1 
ATOM   533  C CB  . LEU A 1 70  ? 7.41500   -32.74500 -37.45300 1.000 43.27000  ? 119 LEU A CB  1 
ATOM   534  C CG  . LEU A 1 70  ? 7.11400   -32.45000 -38.91800 1.000 48.65000  ? 119 LEU A CG  1 
ATOM   535  C CD1 . LEU A 1 70  ? 8.00300   -31.31400 -39.37700 1.000 42.45000  ? 119 LEU A CD1 1 
ATOM   536  C CD2 . LEU A 1 70  ? 7.32000   -33.68200 -39.78900 1.000 40.24000  ? 119 LEU A CD2 1 
ATOM   537  N N   . GLN A 1 71  ? 8.15600   -35.08000 -35.43700 1.000 51.33000  ? 120 GLN A N   1 
ATOM   538  C CA  . GLN A 1 71  ? 8.70000   -35.63000 -34.20900 1.000 57.04000  ? 120 GLN A CA  1 
ATOM   539  C C   . GLN A 1 71  ? 10.08800  -36.14100 -34.51300 1.000 53.38000  ? 120 GLN A C   1 
ATOM   540  O O   . GLN A 1 71  ? 10.25500  -36.89600 -35.47200 1.000 62.80000  ? 120 GLN A O   1 
ATOM   541  C CB  . GLN A 1 71  ? 7.82100   -36.77300 -33.72900 1.000 52.79000  ? 120 GLN A CB  1 
ATOM   542  C CG  . GLN A 1 71  ? 7.99700   -37.16800 -32.31200 1.000 69.51000  ? 120 GLN A CG  1 
ATOM   543  C CD  . GLN A 1 71  ? 6.74000   -37.81900 -31.79100 1.000 80.47000  ? 120 GLN A CD  1 
ATOM   544  O OE1 . GLN A 1 71  ? 5.87600   -38.26300 -32.57700 1.000 71.31000  ? 120 GLN A OE1 1 
ATOM   545  N NE2 . GLN A 1 71  ? 6.60700   -37.85800 -30.46400 1.000 66.30000  ? 120 GLN A NE2 1 
ATOM   546  N N   . ASP A 1 72  ? 11.06600  -35.75700 -33.70200 1.000 48.31000  ? 121 ASP A N   1 
ATOM   547  C CA  . ASP A 1 72  ? 12.39800  -36.29800 -33.91900 1.000 56.05000  ? 121 ASP A CA  1 
ATOM   548  C C   . ASP A 1 72  ? 13.28600  -35.94700 -32.73900 1.000 59.07000  ? 121 ASP A C   1 
ATOM   549  O O   . ASP A 1 72  ? 13.02300  -34.99900 -31.99800 1.000 64.64000  ? 121 ASP A O   1 
ATOM   550  C CB  . ASP A 1 72  ? 13.02800  -35.78400 -35.22200 1.000 55.32000  ? 121 ASP A CB  1 
ATOM   551  C CG  . ASP A 1 72  ? 14.01900  -36.78900 -35.82700 1.000 65.05000  ? 121 ASP A CG  1 
ATOM   552  O OD1 . ASP A 1 72  ? 14.23000  -37.86500 -35.21800 1.000 64.73000  ? 121 ASP A OD1 1 
ATOM   553  O OD2 . ASP A 1 72  ? 14.59500  -36.50500 -36.90300 1.000 63.18000  ? 121 ASP A OD2 1 
ATOM   554  N N   . GLU A 1 73  ? 14.33800  -36.74200 -32.57800 1.000 54.28000  ? 122 GLU A N   1 
ATOM   555  C CA  . GLU A 1 73  ? 15.42500  -36.45800 -31.65500 1.000 54.38000  ? 122 GLU A CA  1 
ATOM   556  C C   . GLU A 1 73  ? 16.47300  -35.64800 -32.39400 1.000 55.07000  ? 122 GLU A C   1 
ATOM   557  O O   . GLU A 1 73  ? 16.91300  -36.04300 -33.47500 1.000 63.16000  ? 122 GLU A O   1 
ATOM   558  C CB  . GLU A 1 73  ? 16.03200  -37.76200 -31.13800 1.000 58.32000  ? 122 GLU A CB  1 
ATOM   559  C CG  . GLU A 1 73  ? 16.67100  -37.73000 -29.76400 1.000 67.38000  ? 122 GLU A CG  1 
ATOM   560  C CD  . GLU A 1 73  ? 17.17500  -39.11300 -29.31900 1.000 80.32000  ? 122 GLU A CD  1 
ATOM   561  O OE1 . GLU A 1 73  ? 17.17700  -40.05400 -30.15500 1.000 77.68000  ? 122 GLU A OE1 1 
ATOM   562  O OE2 . GLU A 1 73  ? 17.57500  -39.25400 -28.13600 1.000 81.70000  ? 122 GLU A OE2 1 
ATOM   563  N N   . ILE A 1 74  ? 16.85700  -34.51900 -31.82700 1.000 52.86000  ? 123 ILE A N   1 
ATOM   564  C CA  . ILE A 1 74  ? 17.90300  -33.67700 -32.38600 1.000 52.05000  ? 123 ILE A CA  1 
ATOM   565  C C   . ILE A 1 74  ? 19.16200  -33.89400 -31.57900 1.000 52.94000  ? 123 ILE A C   1 
ATOM   566  O O   . ILE A 1 74  ? 19.12400  -33.83500 -30.34600 1.000 63.70000  ? 123 ILE A O   1 
ATOM   567  C CB  . ILE A 1 74  ? 17.49000  -32.19800 -32.37500 1.000 50.74000  ? 123 ILE A CB  1 
ATOM   568  C CG1 . ILE A 1 74  ? 16.04600  -32.10600 -32.83400 1.000 62.35000  ? 123 ILE A CG1 1 
ATOM   569  C CG2 . ILE A 1 74  ? 18.41000  -31.35400 -33.25000 1.000 44.46000  ? 123 ILE A CG2 1 
ATOM   570  C CD1 . ILE A 1 74  ? 15.87100  -32.36100 -34.30600 1.000 53.97000  ? 123 ILE A CD1 1 
ATOM   571  N N   . HIS A 1 75  ? 20.27700  -34.11000 -32.26700 1.000 48.72000  ? 124 HIS A N   1 
ATOM   572  C CA  . HIS A 1 75  ? 21.55600  -34.37200 -31.62800 1.000 50.45000  ? 124 HIS A CA  1 
ATOM   573  C C   . HIS A 1 75  ? 22.46900  -33.16400 -31.78700 1.000 51.86000  ? 124 HIS A C   1 
ATOM   574  O O   . HIS A 1 75  ? 22.29300  -32.34400 -32.69100 1.000 50.69000  ? 124 HIS A O   1 
ATOM   575  C CB  . HIS A 1 75  ? 22.18300  -35.65200 -32.21500 1.000 55.36000  ? 124 HIS A CB  1 
ATOM   576  C CG  . HIS A 1 75  ? 21.31200  -36.85900 -32.03700 1.000 57.11000  ? 124 HIS A CG  1 
ATOM   577  N ND1 . HIS A 1 75  ? 21.18600  -37.51300 -30.83000 1.000 56.19000  ? 124 HIS A ND1 1 
ATOM   578  C CD2 . HIS A 1 75  ? 20.45200  -37.47200 -32.88400 1.000 62.91000  ? 124 HIS A CD2 1 
ATOM   579  C CE1 . HIS A 1 75  ? 20.31500  -38.49800 -30.95200 1.000 52.23000  ? 124 HIS A CE1 1 
ATOM   580  N NE2 . HIS A 1 75  ? 19.85200  -38.49400 -32.18600 1.000 57.54000  ? 124 HIS A NE2 1 
ATOM   581  N N   . TYR A 1 76  ? 23.44300  -33.05300 -30.89100 1.000 47.13000  ? 125 TYR A N   1 
ATOM   582  C CA  . TYR A 1 76  ? 24.32600  -31.89700 -30.85200 1.000 45.38000  ? 125 TYR A CA  1 
ATOM   583  C C   . TYR A 1 76  ? 25.45700  -32.18400 -29.86200 1.000 48.42000  ? 125 TYR A C   1 
ATOM   584  O O   . TYR A 1 76  ? 25.33400  -33.08400 -29.02600 1.000 59.73000  ? 125 TYR A O   1 
ATOM   585  C CB  . TYR A 1 76  ? 23.55900  -30.63100 -30.44800 1.000 50.96000  ? 125 TYR A CB  1 
ATOM   586  C CG  . TYR A 1 76  ? 22.70300  -30.81700 -29.22100 1.000 52.93000  ? 125 TYR A CG  1 
ATOM   587  C CD1 . TYR A 1 76  ? 23.27000  -30.83400 -27.94500 1.000 50.76000  ? 125 TYR A CD1 1 
ATOM   588  C CD2 . TYR A 1 76  ? 21.33200  -30.97400 -29.33000 1.000 52.31000  ? 125 TYR A CD2 1 
ATOM   589  C CE1 . TYR A 1 76  ? 22.49100  -30.99900 -26.82100 1.000 50.51000  ? 125 TYR A CE1 1 
ATOM   590  C CE2 . TYR A 1 76  ? 20.54400  -31.14200 -28.20300 1.000 52.23000  ? 125 TYR A CE2 1 
ATOM   591  C CZ  . TYR A 1 76  ? 21.12800  -31.14800 -26.96000 1.000 53.14000  ? 125 TYR A CZ  1 
ATOM   592  O OH  . TYR A 1 76  ? 20.34000  -31.31400 -25.85000 1.000 51.40000  ? 125 TYR A OH  1 
ATOM   593  N N   . PRO A 1 77  ? 26.56200  -31.45100 -29.95100 1.000 50.25000  ? 126 PRO A N   1 
ATOM   594  C CA  . PRO A 1 77  ? 27.68900  -31.67200 -29.01600 1.000 52.09000  ? 126 PRO A CA  1 
ATOM   595  C C   . PRO A 1 77  ? 27.24000  -31.53400 -27.57100 1.000 53.46000  ? 126 PRO A C   1 
ATOM   596  O O   . PRO A 1 77  ? 26.56100  -30.56400 -27.21600 1.000 55.74000  ? 126 PRO A O   1 
ATOM   597  C CB  . PRO A 1 77  ? 28.69400  -30.57300 -29.39400 1.000 53.46000  ? 126 PRO A CB  1 
ATOM   598  C CG  . PRO A 1 77  ? 28.29200  -30.13300 -30.80400 1.000 47.88000  ? 126 PRO A CG  1 
ATOM   599  C CD  . PRO A 1 77  ? 26.80900  -30.32500 -30.87700 1.000 48.13000  ? 126 PRO A CD  1 
ATOM   600  N N   . PRO A 1 78  ? 27.59300  -32.49000 -26.71300 1.000 55.89000  ? 127 PRO A N   1 
ATOM   601  C CA  . PRO A 1 78  ? 27.07800  -32.46400 -25.33400 1.000 53.40000  ? 127 PRO A CA  1 
ATOM   602  C C   . PRO A 1 78  ? 27.39600  -31.20500 -24.54900 1.000 54.71000  ? 127 PRO A C   1 
ATOM   603  O O   . PRO A 1 78  ? 26.71300  -30.94700 -23.55200 1.000 53.88000  ? 127 PRO A O   1 
ATOM   604  C CB  . PRO A 1 78  ? 27.73100  -33.69600 -24.69000 1.000 54.33000  ? 127 PRO A CB  1 
ATOM   605  C CG  . PRO A 1 78  ? 27.96600  -34.63300 -25.82400 1.000 63.30000  ? 127 PRO A CG  1 
ATOM   606  C CD  . PRO A 1 78  ? 28.01900  -33.83800 -27.12100 1.000 61.26000  ? 127 PRO A CD  1 
ATOM   607  N N   . LYS A 1 79  ? 28.38700  -30.40100 -24.93800 1.000 50.15000  ? 128 LYS A N   1 
ATOM   608  C CA  . LYS A 1 79  ? 28.62500  -29.23200 -24.09600 1.000 52.97000  ? 128 LYS A CA  1 
ATOM   609  C C   . LYS A 1 79  ? 27.53800  -28.18300 -24.26300 1.000 61.01000  ? 128 LYS A C   1 
ATOM   610  O O   . LYS A 1 79  ? 27.44400  -27.26800 -23.42800 1.000 58.50000  ? 128 LYS A O   1 
ATOM   611  C CB  . LYS A 1 79  ? 30.01000  -28.62100 -24.35600 1.000 52.33000  ? 128 LYS A CB  1 
ATOM   612  C CG  . LYS A 1 79  ? 30.46700  -28.54900 -25.79800 1.000 61.31000  ? 128 LYS A CG  1 
ATOM   613  C CD  . LYS A 1 79  ? 31.71300  -27.64700 -25.91100 1.000 68.76000  ? 128 LYS A CD  1 
ATOM   614  C CE  . LYS A 1 79  ? 32.78900  -28.27300 -26.81800 1.000 78.25000  ? 128 LYS A CE  1 
ATOM   615  N NZ  . LYS A 1 79  ? 32.26800  -28.66700 -28.18000 1.000 71.90000  ? 128 LYS A NZ  1 
ATOM   616  N N   . LEU A 1 80  ? 26.69500  -28.32700 -25.29200 1.000 49.93000  ? 129 LEU A N   1 
ATOM   617  C CA  . LEU A 1 80  ? 25.53200  -27.47600 -25.47600 1.000 48.59000  ? 129 LEU A CA  1 
ATOM   618  C C   . LEU A 1 80  ? 24.38900  -27.85900 -24.54900 1.000 52.12000  ? 129 LEU A C   1 
ATOM   619  O O   . LEU A 1 80  ? 23.50500  -27.03500 -24.30400 1.000 54.75000  ? 129 LEU A O   1 
ATOM   620  C CB  . LEU A 1 80  ? 25.07500  -27.53700 -26.92800 1.000 44.24000  ? 129 LEU A CB  1 
ATOM   621  C CG  . LEU A 1 80  ? 24.37100  -26.31900 -27.50700 1.000 51.80000  ? 129 LEU A CG  1 
ATOM   622  C CD1 . LEU A 1 80  ? 25.36000  -25.20500 -27.86300 1.000 44.96000  ? 129 LEU A CD1 1 
ATOM   623  C CD2 . LEU A 1 80  ? 23.52200  -26.71200 -28.72800 1.000 49.18000  ? 129 LEU A CD2 1 
ATOM   624  N N   . HIS A 1 81  ? 24.41100  -29.07000 -23.99500 1.000 48.82000  ? 130 HIS A N   1 
ATOM   625  C CA  . HIS A 1 81  ? 23.25700  -29.57300 -23.25300 1.000 46.79000  ? 130 HIS A CA  1 
ATOM   626  C C   . HIS A 1 81  ? 22.89100  -28.69100 -22.06400 1.000 48.87000  ? 130 HIS A C   1 
ATOM   627  O O   . HIS A 1 81  ? 21.70700  -28.57200 -21.72400 1.000 48.12000  ? 130 HIS A O   1 
ATOM   628  C CB  . HIS A 1 81  ? 23.52300  -30.99500 -22.77000 1.000 43.38000  ? 130 HIS A CB  1 
ATOM   629  C CG  . HIS A 1 81  ? 22.27800  -31.76400 -22.48300 1.000 53.20000  ? 130 HIS A CG  1 
ATOM   630  N ND1 . HIS A 1 81  ? 21.41000  -32.16100 -23.47700 1.000 50.05000  ? 130 HIS A ND1 1 
ATOM   631  C CD2 . HIS A 1 81  ? 21.74300  -32.19600 -21.31500 1.000 53.47000  ? 130 HIS A CD2 1 
ATOM   632  C CE1 . HIS A 1 81  ? 20.39600  -32.81300 -22.93500 1.000 51.88000  ? 130 HIS A CE1 1 
ATOM   633  N NE2 . HIS A 1 81  ? 20.57500  -32.84900 -21.62500 1.000 57.76000  ? 130 HIS A NE2 1 
ATOM   634  N N   . CYS A 1 82  ? 23.87300  -28.04200 -21.43800 1.000 52.26000  ? 131 CYS A N   1 
ATOM   635  C CA  . CYS A 1 82  ? 23.56500  -27.20500 -20.28600 1.000 43.57000  ? 131 CYS A CA  1 
ATOM   636  C C   . CYS A 1 82  ? 22.56500  -26.09400 -20.62900 1.000 51.86000  ? 131 CYS A C   1 
ATOM   637  O O   . CYS A 1 82  ? 21.84800  -25.62500 -19.73900 1.000 42.30000  ? 131 CYS A O   1 
ATOM   638  C CB  . CYS A 1 82  ? 24.85700  -26.60700 -19.72400 1.000 47.87000  ? 131 CYS A CB  1 
ATOM   639  S SG  . CYS A 1 82  ? 25.84000  -25.63300 -20.93600 1.000 58.25000  ? 131 CYS A SG  1 
ATOM   640  N N   . ILE A 1 83  ? 22.48100  -25.66900 -21.90300 1.000 52.17000  ? 132 ILE A N   1 
ATOM   641  C CA  . ILE A 1 83  ? 21.47200  -24.67300 -22.25900 1.000 50.77000  ? 132 ILE A CA  1 
ATOM   642  C C   . ILE A 1 83  ? 20.08100  -25.17000 -21.90700 1.000 49.09000  ? 132 ILE A C   1 
ATOM   643  O O   . ILE A 1 83  ? 19.25200  -24.41000 -21.38900 1.000 47.89000  ? 132 ILE A O   1 
ATOM   644  C CB  . ILE A 1 83  ? 21.54700  -24.28800 -23.75000 1.000 52.26000  ? 132 ILE A CB  1 
ATOM   645  C CG1 . ILE A 1 83  ? 22.87700  -23.63900 -24.12000 1.000 55.43000  ? 132 ILE A CG1 1 
ATOM   646  C CG2 . ILE A 1 83  ? 20.30900  -23.50500 -24.20700 1.000 50.49000  ? 132 ILE A CG2 1 
ATOM   647  C CD1 . ILE A 1 83  ? 23.02200  -23.56200 -25.59100 1.000 43.36000  ? 132 ILE A CD1 1 
ATOM   648  N N   . PHE A 1 84  ? 19.80200  -26.44100 -22.17300 1.000 45.11000  ? 133 PHE A N   1 
ATOM   649  C CA  . PHE A 1 84  ? 18.45100  -26.94200 -22.01200 1.000 51.30000  ? 133 PHE A CA  1 
ATOM   650  C C   . PHE A 1 84  ? 18.12900  -27.39300 -20.58900 1.000 47.94000  ? 133 PHE A C   1 
ATOM   651  O O   . PHE A 1 84  ? 16.94700  -27.58000 -20.27100 1.000 56.48000  ? 133 PHE A O   1 
ATOM   652  C CB  . PHE A 1 84  ? 18.22500  -28.07300 -23.00900 1.000 37.00000  ? 133 PHE A CB  1 
ATOM   653  C CG  . PHE A 1 84  ? 18.59800  -27.69400 -24.39400 1.000 50.31000  ? 133 PHE A CG  1 
ATOM   654  C CD1 . PHE A 1 84  ? 17.86800  -26.72100 -25.07000 1.000 48.20000  ? 133 PHE A CD1 1 
ATOM   655  C CD2 . PHE A 1 84  ? 19.68400  -28.28300 -25.02900 1.000 51.22000  ? 133 PHE A CD2 1 
ATOM   656  C CE1 . PHE A 1 84  ? 18.20300  -26.34500 -26.32500 1.000 48.39000  ? 133 PHE A CE1 1 
ATOM   657  C CE2 . PHE A 1 84  ? 20.02600  -27.91200 -26.31300 1.000 50.75000  ? 133 PHE A CE2 1 
ATOM   658  C CZ  . PHE A 1 84  ? 19.28500  -26.93500 -26.96300 1.000 54.65000  ? 133 PHE A CZ  1 
ATOM   659  N N   . LEU A 1 85  ? 19.12600  -27.53200 -19.71900 1.000 46.81000  ? 134 LEU A N   1 
ATOM   660  C CA  . LEU A 1 85  ? 18.88000  -27.85000 -18.31300 1.000 52.79000  ? 134 LEU A CA  1 
ATOM   661  C C   . LEU A 1 85  ? 19.14600  -26.68900 -17.37600 1.000 53.96000  ? 134 LEU A C   1 
ATOM   662  O O   . LEU A 1 85  ? 18.56300  -26.64500 -16.28800 1.000 47.69000  ? 134 LEU A O   1 
ATOM   663  C CB  . LEU A 1 85  ? 19.76200  -29.02300 -17.85700 1.000 45.50000  ? 134 LEU A CB  1 
ATOM   664  C CG  . LEU A 1 85  ? 19.63300  -30.32400 -18.63700 1.000 53.02000  ? 134 LEU A CG  1 
ATOM   665  C CD1 . LEU A 1 85  ? 20.55400  -31.37700 -18.06800 1.000 45.90000  ? 134 LEU A CD1 1 
ATOM   666  C CD2 . LEU A 1 85  ? 18.19500  -30.77600 -18.60000 1.000 47.73000  ? 134 LEU A CD2 1 
ATOM   667  N N   . GLY A 1 86  ? 20.01500  -25.74800 -17.76800 1.000 45.12000  ? 135 GLY A N   1 
ATOM   668  C CA  . GLY A 1 86  ? 20.50000  -24.77600 -16.81400 1.000 51.12000  ? 135 GLY A CA  1 
ATOM   669  C C   . GLY A 1 86  ? 19.51100  -23.68500 -16.49200 1.000 50.85000  ? 135 GLY A C   1 
ATOM   670  O O   . GLY A 1 86  ? 18.47800  -23.51700 -17.14800 1.000 50.08000  ? 135 GLY A O   1 
ATOM   671  N N   . ALA A 1 87  ? 19.87000  -22.91500 -15.46600 1.000 44.05000  ? 136 ALA A N   1 
ATOM   672  C CA  . ALA A 1 87  ? 19.07900  -21.76800 -15.02300 1.000 47.21000  ? 136 ALA A CA  1 
ATOM   673  C C   . ALA A 1 87  ? 17.63000  -22.16600 -14.74800 1.000 48.72000  ? 136 ALA A C   1 
ATOM   674  O O   . ALA A 1 87  ? 16.68400  -21.48900 -15.16700 1.000 46.44000  ? 136 ALA A O   1 
ATOM   675  C CB  . ALA A 1 87  ? 19.15900  -20.62500 -16.04000 1.000 48.93000  ? 136 ALA A CB  1 
ATOM   676  N N   . GLN A 1 88  ? 17.45700  -23.30400 -14.07500 1.000 47.84000  ? 137 GLN A N   1 
ATOM   677  C CA  . GLN A 1 88  ? 16.13300  -23.79900 -13.72100 1.000 46.03000  ? 137 GLN A CA  1 
ATOM   678  C C   . GLN A 1 88  ? 15.22200  -23.89800 -14.95100 1.000 48.83000  ? 137 GLN A C   1 
ATOM   679  O O   . GLN A 1 88  ? 14.01900  -23.63300 -14.88200 1.000 56.99000  ? 137 GLN A O   1 
ATOM   680  C CB  . GLN A 1 88  ? 15.51600  -22.88000 -12.67200 1.000 52.49000  ? 137 GLN A CB  1 
ATOM   681  C CG  . GLN A 1 88  ? 15.90000  -23.17500 -11.23500 1.000 55.45000  ? 137 GLN A CG  1 
ATOM   682  C CD  . GLN A 1 88  ? 15.19500  -22.23200 -10.27200 1.000 69.06000  ? 137 GLN A CD  1 
ATOM   683  O OE1 . GLN A 1 88  ? 14.51700  -21.27400 -10.70100 1.000 60.52000  ? 137 GLN A OE1 1 
ATOM   684  N NE2 . GLN A 1 88  ? 15.32600  -22.51000 -8.96000  1.000 68.22000  ? 137 GLN A NE2 1 
ATOM   685  N N   . GLY A 1 89  ? 15.79500  -24.28600 -16.09500 1.000 44.92000  ? 138 GLY A N   1 
ATOM   686  C CA  . GLY A 1 89  ? 15.01900  -24.50200 -17.31500 1.000 46.30000  ? 138 GLY A CA  1 
ATOM   687  C C   . GLY A 1 89  ? 14.65800  -23.25600 -18.09800 1.000 49.29000  ? 138 GLY A C   1 
ATOM   688  O O   . GLY A 1 89  ? 13.86100  -23.34100 -19.03800 1.000 47.43000  ? 138 GLY A O   1 
ATOM   689  N N   . PHE A 1 90  ? 15.25800  -22.11400 -17.76200 1.000 44.75000  ? 139 PHE A N   1 
ATOM   690  C CA  . PHE A 1 90  ? 14.83100  -20.83300 -18.30100 1.000 44.31000  ? 139 PHE A CA  1 
ATOM   691  C C   . PHE A 1 90  ? 14.93500  -20.80100 -19.82400 1.000 53.57000  ? 139 PHE A C   1 
ATOM   692  O O   . PHE A 1 90  ? 13.98500  -20.40000 -20.51400 1.000 46.05000  ? 139 PHE A O   1 
ATOM   693  C CB  . PHE A 1 90  ? 15.67900  -19.73900 -17.64900 1.000 45.20000  ? 139 PHE A CB  1 
ATOM   694  C CG  . PHE A 1 90  ? 15.49900  -18.38300 -18.23700 1.000 41.35000  ? 139 PHE A CG  1 
ATOM   695  C CD1 . PHE A 1 90  ? 14.28900  -17.71000 -18.11400 1.000 51.16000  ? 139 PHE A CD1 1 
ATOM   696  C CD2 . PHE A 1 90  ? 16.54400  -17.77300 -18.92100 1.000 44.48000  ? 139 PHE A CD2 1 
ATOM   697  C CE1 . PHE A 1 90  ? 14.12100  -16.44000 -18.66800 1.000 52.83000  ? 139 PHE A CE1 1 
ATOM   698  C CE2 . PHE A 1 90  ? 16.39300  -16.50500 -19.47900 1.000 45.90000  ? 139 PHE A CE2 1 
ATOM   699  C CZ  . PHE A 1 90  ? 15.18000  -15.83700 -19.35500 1.000 48.10000  ? 139 PHE A CZ  1 
ATOM   700  N N   . PHE A 1 91  ? 16.07700  -21.25000 -20.37000 1.000 50.69000  ? 140 PHE A N   1 
ATOM   701  C CA  . PHE A 1 91  ? 16.30100  -21.15500 -21.81200 1.000 43.94000  ? 140 PHE A CA  1 
ATOM   702  C C   . PHE A 1 91  ? 15.42200  -22.13900 -22.57500 1.000 44.80000  ? 140 PHE A C   1 
ATOM   703  O O   . PHE A 1 91  ? 14.93900  -21.82900 -23.67400 1.000 48.71000  ? 140 PHE A O   1 
ATOM   704  C CB  . PHE A 1 91  ? 17.77700  -21.39100 -22.12900 1.000 45.78000  ? 140 PHE A CB  1 
ATOM   705  C CG  . PHE A 1 91  ? 18.68500  -20.32900 -21.58200 1.000 46.90000  ? 140 PHE A CG  1 
ATOM   706  C CD1 . PHE A 1 91  ? 18.70200  -19.06000 -22.13800 1.000 49.72000  ? 140 PHE A CD1 1 
ATOM   707  C CD2 . PHE A 1 91  ? 19.52900  -20.60200 -20.51500 1.000 46.15000  ? 140 PHE A CD2 1 
ATOM   708  C CE1 . PHE A 1 91  ? 19.52900  -18.07200 -21.63700 1.000 48.44000  ? 140 PHE A CE1 1 
ATOM   709  C CE2 . PHE A 1 91  ? 20.37300  -19.62000 -20.00000 1.000 43.31000  ? 140 PHE A CE2 1 
ATOM   710  C CZ  . PHE A 1 91  ? 20.37700  -18.35000 -20.56300 1.000 46.09000  ? 140 PHE A CZ  1 
ATOM   711  N N   . LEU A 1 92  ? 15.23200  -23.33900 -22.02300 1.000 46.27000  ? 141 LEU A N   1 
ATOM   712  C CA  . LEU A 1 92  ? 14.26200  -24.28300 -22.56900 1.000 48.94000  ? 141 LEU A CA  1 
ATOM   713  C C   . LEU A 1 92  ? 12.85900  -23.68700 -22.55500 1.000 47.06000  ? 141 LEU A C   1 
ATOM   714  O O   . LEU A 1 92  ? 12.09900  -23.84600 -23.51500 1.000 48.81000  ? 141 LEU A O   1 
ATOM   715  C CB  . LEU A 1 92  ? 14.29400  -25.59100 -21.76700 1.000 40.96000  ? 141 LEU A CB  1 
ATOM   716  C CG  . LEU A 1 92  ? 13.60900  -26.78800 -22.41900 1.000 41.24000  ? 141 LEU A CG  1 
ATOM   717  C CD1 . LEU A 1 92  ? 14.31600  -27.11300 -23.72500 1.000 38.31000  ? 141 LEU A CD1 1 
ATOM   718  C CD2 . LEU A 1 92  ? 13.59500  -28.00300 -21.49200 1.000 37.90000  ? 141 LEU A CD2 1 
ATOM   719  N N   . ASP A 1 93  ? 12.50200  -23.00000 -21.46600 1.000 44.98000  ? 142 ASP A N   1 
ATOM   720  C CA  . ASP A 1 93  ? 11.17500  -22.40300 -21.34300 1.000 40.76000  ? 142 ASP A CA  1 
ATOM   721  C C   . ASP A 1 93  ? 10.96600  -21.33100 -22.39600 1.000 45.39000  ? 142 ASP A C   1 
ATOM   722  O O   . ASP A 1 93  ? 9.88400   -21.23500 -22.98800 1.000 45.90000  ? 142 ASP A O   1 
ATOM   723  C CB  . ASP A 1 93  ? 11.00800  -21.78900 -19.94500 1.000 57.98000  ? 142 ASP A CB  1 
ATOM   724  C CG  . ASP A 1 93  ? 10.95200  -22.83200 -18.82100 1.000 60.04000  ? 142 ASP A CG  1 
ATOM   725  O OD1 . ASP A 1 93  ? 10.90400  -24.06700 -19.07600 1.000 58.74000  ? 142 ASP A OD1 1 
ATOM   726  O OD2 . ASP A 1 93  ? 11.05300  -22.39800 -17.65400 1.000 71.71000  ? 142 ASP A OD2 1 
ATOM   727  N N   . CYS A 1 94  ? 11.99000  -20.50800 -22.63700 1.000 43.88000  ? 143 CYS A N   1 
ATOM   728  C CA  . CYS A 1 94  ? 11.89300  -19.48900 -23.67700 1.000 49.66000  ? 143 CYS A CA  1 
ATOM   729  C C   . CYS A 1 94  ? 11.76500  -20.11900 -25.05700 1.000 46.86000  ? 143 CYS A C   1 
ATOM   730  O O   . CYS A 1 94  ? 11.05900  -19.59000 -25.92200 1.000 47.43000  ? 143 CYS A O   1 
ATOM   731  C CB  . CYS A 1 94  ? 13.10400  -18.56200 -23.63100 1.000 45.30000  ? 143 CYS A CB  1 
ATOM   732  S SG  . CYS A 1 94  ? 13.22700  -17.57300 -22.12400 1.000 54.65000  ? 143 CYS A SG  1 
ATOM   733  N N   A LEU A 1 95  ? 12.44500  -21.23900 -25.28500 0.720 44.46000  ? 144 LEU A N   1 
ATOM   734  N N   B LEU A 1 95  ? 12.46200  -21.23300 -25.29000 0.280 44.60000  ? 144 LEU A N   1 
ATOM   735  C CA  A LEU A 1 95  ? 12.33600  -21.89500 -26.57800 0.720 47.90000  ? 144 LEU A CA  1 
ATOM   736  C CA  B LEU A 1 95  ? 12.34300  -21.92200 -26.56900 0.280 47.67000  ? 144 LEU A CA  1 
ATOM   737  C C   A LEU A 1 95  ? 10.93700  -22.47400 -26.77500 0.720 47.85000  ? 144 LEU A C   1 
ATOM   738  C C   B LEU A 1 95  ? 10.93500  -22.46500 -26.76700 0.280 47.44000  ? 144 LEU A C   1 
ATOM   739  O O   A LEU A 1 95  ? 10.39700  -22.45900 -27.89400 0.720 44.88000  ? 144 LEU A O   1 
ATOM   740  O O   B LEU A 1 95  ? 10.39400  -22.43100 -27.88100 0.280 44.84000  ? 144 LEU A O   1 
ATOM   741  C CB  A LEU A 1 95  ? 13.41300  -22.97600 -26.70700 0.720 44.90000  ? 144 LEU A CB  1 
ATOM   742  C CB  B LEU A 1 95  ? 13.36800  -23.05300 -26.65400 0.280 44.85000  ? 144 LEU A CB  1 
ATOM   743  C CG  A LEU A 1 95  ? 13.50800  -23.67200 -28.06600 0.720 39.96000  ? 144 LEU A CG  1 
ATOM   744  C CG  B LEU A 1 95  ? 14.79200  -22.60500 -26.96600 0.280 44.89000  ? 144 LEU A CG  1 
ATOM   745  C CD1 A LEU A 1 95  ? 13.58500  -22.66700 -29.22400 0.720 40.53000  ? 144 LEU A CD1 1 
ATOM   746  C CD1 B LEU A 1 95  ? 15.80700  -23.65600 -26.54900 0.280 43.29000  ? 144 LEU A CD1 1 
ATOM   747  C CD2 A LEU A 1 95  ? 14.68600  -24.62800 -28.07500 0.720 37.69000  ? 144 LEU A CD2 1 
ATOM   748  C CD2 B LEU A 1 95  ? 14.93400  -22.25700 -28.44000 0.280 41.77000  ? 144 LEU A CD2 1 
ATOM   749  N N   . ALA A 1 96  ? 10.32700  -22.96800 -25.69200 1.000 46.56000  ? 145 ALA A N   1 
ATOM   750  C CA  . ALA A 1 96  ? 8.95500   -23.45600 -25.77700 1.000 47.93000  ? 145 ALA A CA  1 
ATOM   751  C C   . ALA A 1 96  ? 7.98800   -22.30800 -26.02700 1.000 48.83000  ? 145 ALA A C   1 
ATOM   752  O O   . ALA A 1 96  ? 7.07400   -22.41800 -26.84500 1.000 50.59000  ? 145 ALA A O   1 
ATOM   753  C CB  . ALA A 1 96  ? 8.58700   -24.18900 -24.48900 1.000 49.80000  ? 145 ALA A CB  1 
ATOM   754  N N   . TRP A 1 97  ? 8.17400   -21.19600 -25.32400 1.000 54.83000  ? 146 TRP A N   1 
ATOM   755  C CA  . TRP A 1 97  ? 7.34800   -20.02800 -25.57000 1.000 52.29000  ? 146 TRP A CA  1 
ATOM   756  C C   . TRP A 1 97  ? 7.55100   -19.50800 -26.98600 1.000 48.86000  ? 146 TRP A C   1 
ATOM   757  O O   . TRP A 1 97  ? 6.58800   -19.12100 -27.65700 1.000 48.92000  ? 146 TRP A O   1 
ATOM   758  C CB  . TRP A 1 97  ? 7.67400   -18.94500 -24.54800 1.000 43.01000  ? 146 TRP A CB  1 
ATOM   759  C CG  . TRP A 1 97  ? 7.14000   -17.62200 -24.96000 1.000 50.92000  ? 146 TRP A CG  1 
ATOM   760  C CD1 . TRP A 1 97  ? 7.79100   -16.66100 -25.66300 1.000 45.76000  ? 146 TRP A CD1 1 
ATOM   761  C CD2 . TRP A 1 97  ? 5.83600   -17.11000 -24.68900 1.000 49.47000  ? 146 TRP A CD2 1 
ATOM   762  N NE1 . TRP A 1 97  ? 6.97800   -15.57600 -25.84300 1.000 54.33000  ? 146 TRP A NE1 1 
ATOM   763  C CE2 . TRP A 1 97  ? 5.76900   -15.82800 -25.25400 1.000 50.46000  ? 146 TRP A CE2 1 
ATOM   764  C CE3 . TRP A 1 97  ? 4.72500   -17.60700 -24.00900 1.000 45.38000  ? 146 TRP A CE3 1 
ATOM   765  C CZ2 . TRP A 1 97  ? 4.63100   -15.04700 -25.18000 1.000 49.31000  ? 146 TRP A CZ2 1 
ATOM   766  C CZ3 . TRP A 1 97  ? 3.60600   -16.83300 -23.93100 1.000 49.53000  ? 146 TRP A CZ3 1 
ATOM   767  C CH2 . TRP A 1 97  ? 3.56200   -15.56400 -24.51600 1.000 55.79000  ? 146 TRP A CH2 1 
ATOM   768  N N   . SER A 1 98  ? 8.80200   -19.47100 -27.44800 1.000 48.13000  ? 147 SER A N   1 
ATOM   769  C CA  . SER A 1 98  ? 9.09300   -18.94300 -28.78000 1.000 44.80000  ? 147 SER A CA  1 
ATOM   770  C C   . SER A 1 98  ? 8.48800   -19.80700 -29.88300 1.000 46.30000  ? 147 SER A C   1 
ATOM   771  O O   . SER A 1 98  ? 8.06700   -19.27900 -30.91600 1.000 47.04000  ? 147 SER A O   1 
ATOM   772  C CB  . SER A 1 98  ? 10.60100  -18.81900 -28.98200 1.000 45.22000  ? 147 SER A CB  1 
ATOM   773  O OG  . SER A 1 98  ? 10.90900  -18.16600 -30.20100 1.000 61.83000  ? 147 SER A OG  1 
ATOM   774  N N   . THR A 1 99  ? 8.44500   -21.13600 -29.70500 1.000 45.29000  ? 148 THR A N   1 
ATOM   775  C CA  . THR A 1 99  ? 8.10000   -22.02400 -30.81300 1.000 47.30000  ? 148 THR A CA  1 
ATOM   776  C C   . THR A 1 99  ? 6.80800   -22.80100 -30.62800 1.000 48.11000  ? 148 THR A C   1 
ATOM   777  O O   . THR A 1 99  ? 6.23800   -23.24200 -31.62800 1.000 48.10000  ? 148 THR A O   1 
ATOM   778  C CB  . THR A 1 99  ? 9.22000   -23.05300 -31.07800 1.000 49.37000  ? 148 THR A CB  1 
ATOM   779  O OG1 . THR A 1 99  ? 9.37300   -23.90100 -29.93700 1.000 44.40000  ? 148 THR A OG1 1 
ATOM   780  C CG2 . THR A 1 99  ? 10.56100  -22.38000 -31.41200 1.000 42.67000  ? 148 THR A CG2 1 
ATOM   781  N N   . SER A 1 100 ? 6.33400   -22.98600 -29.39800 1.000 43.96000  ? 149 SER A N   1 
ATOM   782  C CA  . SER A 1 100 ? 5.20500   -23.86300 -29.08500 1.000 41.52000  ? 149 SER A CA  1 
ATOM   783  C C   . SER A 1 100 ? 5.50000   -25.30800 -29.43600 1.000 42.95000  ? 149 SER A C   1 
ATOM   784  O O   . SER A 1 100 ? 4.57700   -26.10600 -29.59800 1.000 49.63000  ? 149 SER A O   1 
ATOM   785  C CB  . SER A 1 100 ? 3.91300   -23.42500 -29.78600 1.000 49.93000  ? 149 SER A CB  1 
ATOM   786  O OG  . SER A 1 100 ? 3.50500   -22.14600 -29.35300 1.000 53.47000  ? 149 SER A OG  1 
ATOM   787  N N   . ALA A 1 101 ? 6.77100   -25.65800 -29.56600 1.000 41.79000  ? 150 ALA A N   1 
ATOM   788  C CA  . ALA A 1 101 ? 7.17600   -27.04800 -29.71700 1.000 50.29000  ? 150 ALA A CA  1 
ATOM   789  C C   . ALA A 1 101 ? 7.34200   -27.70200 -28.34500 1.000 47.23000  ? 150 ALA A C   1 
ATOM   790  O O   . ALA A 1 101 ? 7.71600   -27.04700 -27.37100 1.000 45.07000  ? 150 ALA A O   1 
ATOM   791  C CB  . ALA A 1 101 ? 8.49500   -27.14600 -30.48800 1.000 39.32000  ? 150 ALA A CB  1 
ATOM   792  N N   . HIS A 1 102 ? 7.06200   -29.00600 -28.28500 1.000 47.99000  ? 151 HIS A N   1 
ATOM   793  C CA  . HIS A 1 102 ? 7.26900   -29.81800 -27.08600 1.000 44.92000  ? 151 HIS A CA  1 
ATOM   794  C C   . HIS A 1 102 ? 8.71900   -30.29800 -27.05800 1.000 52.29000  ? 151 HIS A C   1 
ATOM   795  O O   . HIS A 1 102 ? 9.15100   -31.03000 -27.96200 1.000 50.48000  ? 151 HIS A O   1 
ATOM   796  C CB  . HIS A 1 102 ? 6.29400   -30.99400 -27.09400 1.000 49.11000  ? 151 HIS A CB  1 
ATOM   797  C CG  . HIS A 1 102 ? 6.37400   -31.87500 -25.88700 1.000 57.18000  ? 151 HIS A CG  1 
ATOM   798  N ND1 . HIS A 1 102 ? 6.19100   -31.40800 -24.60300 1.000 61.23000  ? 151 HIS A ND1 1 
ATOM   799  C CD2 . HIS A 1 102 ? 6.61400   -33.20500 -25.77400 1.000 55.06000  ? 151 HIS A CD2 1 
ATOM   800  C CE1 . HIS A 1 102 ? 6.31800   -32.41000 -23.75100 1.000 55.45000  ? 151 HIS A CE1 1 
ATOM   801  N NE2 . HIS A 1 102 ? 6.58100   -33.50900 -24.43500 1.000 57.10000  ? 151 HIS A NE2 1 
ATOM   802  N N   . LEU A 1 103 ? 9.47100   -29.86800 -26.03700 1.000 42.82000  ? 152 LEU A N   1 
ATOM   803  C CA  . LEU A 1 103 ? 10.91700  -30.04500 -25.96500 1.000 41.50000  ? 152 LEU A CA  1 
ATOM   804  C C   . LEU A 1 103 ? 11.30000  -30.83300 -24.71700 1.000 51.70000  ? 152 LEU A C   1 
ATOM   805  O O   . LEU A 1 103 ? 11.03000  -30.39400 -23.59100 1.000 54.08000  ? 152 LEU A O   1 
ATOM   806  C CB  . LEU A 1 103 ? 11.61400  -28.68800 -25.95400 1.000 42.93000  ? 152 LEU A CB  1 
ATOM   807  C CG  . LEU A 1 103 ? 11.19900  -27.74200 -27.08000 1.000 53.83000  ? 152 LEU A CG  1 
ATOM   808  C CD1 . LEU A 1 103 ? 11.65300  -26.35700 -26.71500 1.000 50.65000  ? 152 LEU A CD1 1 
ATOM   809  C CD2 . LEU A 1 103 ? 11.80900  -28.16400 -28.41400 1.000 38.98000  ? 152 LEU A CD2 1 
ATOM   810  N N   . VAL A 1 104 ? 11.97200  -31.96300 -24.91200 1.000 47.95000  ? 153 VAL A N   1 
ATOM   811  C CA  . VAL A 1 104 ? 12.31700  -32.85900 -23.81500 1.000 40.66000  ? 153 VAL A CA  1 
ATOM   812  C C   . VAL A 1 104 ? 13.78200  -33.27200 -23.89800 1.000 49.24000  ? 153 VAL A C   1 
ATOM   813  O O   . VAL A 1 104 ? 14.12900  -34.11200 -24.73600 1.000 52.61000  ? 153 VAL A O   1 
ATOM   814  C CB  . VAL A 1 104 ? 11.41600  -34.09600 -23.83400 1.000 50.61000  ? 153 VAL A CB  1 
ATOM   815  C CG1 . VAL A 1 104 ? 11.85500  -35.06100 -22.75300 1.000 45.30000  ? 153 VAL A CG1 1 
ATOM   816  C CG2 . VAL A 1 104 ? 9.94500   -33.69000 -23.67400 1.000 42.99000  ? 153 VAL A CG2 1 
ATOM   817  N N   . PRO A 1 105 ? 14.67200  -32.71700 -23.06800 1.000 54.82000  ? 154 PRO A N   1 
ATOM   818  C CA  . PRO A 1 105 ? 16.07700  -33.16400 -23.07300 1.000 51.94000  ? 154 PRO A CA  1 
ATOM   819  C C   . PRO A 1 105 ? 16.18600  -34.66000 -22.81500 1.000 52.08000  ? 154 PRO A C   1 
ATOM   820  O O   . PRO A 1 105 ? 15.36600  -35.24400 -22.10300 1.000 54.34000  ? 154 PRO A O   1 
ATOM   821  C CB  . PRO A 1 105 ? 16.71200  -32.36500 -21.92300 1.000 48.87000  ? 154 PRO A CB  1 
ATOM   822  C CG  . PRO A 1 105 ? 15.83700  -31.16500 -21.75000 1.000 48.21000  ? 154 PRO A CG  1 
ATOM   823  C CD  . PRO A 1 105 ? 14.43400  -31.67100 -22.06000 1.000 49.23000  ? 154 PRO A CD  1 
ATOM   824  N N   . ARG A 1 106 ? 17.19600  -35.29200 -23.42200 1.000 58.63000  ? 155 ARG A N   1 
ATOM   825  C CA  . ARG A 1 106 ? 17.47000  -36.69400 -23.10400 1.000 58.48000  ? 155 ARG A CA  1 
ATOM   826  C C   . ARG A 1 106 ? 18.88700  -36.84600 -22.56200 1.000 57.36000  ? 155 ARG A C   1 
ATOM   827  O O   . ARG A 1 106 ? 19.34400  -36.00900 -21.77600 1.000 63.42000  ? 155 ARG A O   1 
ATOM   828  C CB  . ARG A 1 106 ? 17.26000  -37.58200 -24.31500 1.000 56.65000  ? 155 ARG A CB  1 
ATOM   829  C CG  . ARG A 1 106 ? 15.82600  -37.64400 -24.71900 1.000 66.06000  ? 155 ARG A CG  1 
ATOM   830  C CD  . ARG A 1 106 ? 15.20600  -38.94500 -24.32300 1.000 80.51000  ? 155 ARG A CD  1 
ATOM   831  N NE  . ARG A 1 106 ? 15.37400  -39.93900 -25.37500 1.000 88.41000  ? 155 ARG A NE  1 
ATOM   832  C CZ  . ARG A 1 106 ? 14.37300  -40.61000 -25.93100 1.000 98.20000  ? 155 ARG A CZ  1 
ATOM   833  N NH1 . ARG A 1 106 ? 13.12600  -40.47400 -25.50200 1.000 96.97000  ? 155 ARG A NH1 1 
ATOM   834  N NH2 . ARG A 1 106 ? 14.63300  -41.45400 -26.92700 1.000 88.18000  ? 155 ARG A NH2 1 
ATOM   835  N N   . ALA A 1 107 ? 19.56900  -37.92400 -22.92600 1.000 63.25000  ? 156 ALA A N   1 
ATOM   836  C CA  . ALA A 1 107 ? 20.96600  -38.06400 -22.54000 1.000 61.15000  ? 156 ALA A CA  1 
ATOM   837  C C   . ALA A 1 107 ? 21.75500  -36.87800 -23.09200 1.000 64.05000  ? 156 ALA A C   1 
ATOM   838  O O   . ALA A 1 107 ? 21.48000  -36.41900 -24.21300 1.000 66.45000  ? 156 ALA A O   1 
ATOM   839  C CB  . ALA A 1 107 ? 21.54900  -39.37800 -23.06600 1.000 50.31000  ? 156 ALA A CB  1 
ATOM   840  N N   . PRO A 1 108 ? 22.71000  -36.33600 -22.32600 1.000 61.68000  ? 157 PRO A N   1 
ATOM   841  C CA  . PRO A 1 108 ? 23.44700  -35.14200 -22.77800 1.000 60.75000  ? 157 PRO A CA  1 
ATOM   842  C C   . PRO A 1 108 ? 23.88500  -35.24600 -24.22600 1.000 61.17000  ? 157 PRO A C   1 
ATOM   843  O O   . PRO A 1 108 ? 24.54800  -36.21300 -24.61400 1.000 63.22000  ? 157 PRO A O   1 
ATOM   844  C CB  . PRO A 1 108 ? 24.65400  -35.09200 -21.83100 1.000 60.21000  ? 157 PRO A CB  1 
ATOM   845  C CG  . PRO A 1 108 ? 24.18200  -35.77300 -20.55400 1.000 57.45000  ? 157 PRO A CG  1 
ATOM   846  C CD  . PRO A 1 108 ? 22.99300  -36.67300 -20.91800 1.000 61.41000  ? 157 PRO A CD  1 
ATOM   847  N N   . GLY A 1 109 ? 23.50200  -34.24200 -25.02000 1.000 65.57000  ? 158 GLY A N   1 
ATOM   848  C CA  . GLY A 1 109 ? 23.70000  -34.21500 -26.45800 1.000 56.61000  ? 158 GLY A CA  1 
ATOM   849  C C   . GLY A 1 109 ? 22.43500  -34.41000 -27.26900 1.000 58.81000  ? 158 GLY A C   1 
ATOM   850  O O   . GLY A 1 109 ? 22.50100  -34.40300 -28.50100 1.000 59.15000  ? 158 GLY A O   1 
ATOM   851  N N   . SER A 1 110 ? 21.27900  -34.56400 -26.63700 1.000 61.04000  ? 159 SER A N   1 
ATOM   852  C CA  . SER A 1 110 ? 20.10300  -34.97500 -27.38500 1.000 61.66000  ? 159 SER A CA  1 
ATOM   853  C C   . SER A 1 110 ? 18.84500  -34.34700 -26.78700 1.000 57.96000  ? 159 SER A C   1 
ATOM   854  O O   . SER A 1 110 ? 18.72400  -34.22100 -25.56600 1.000 61.52000  ? 159 SER A O   1 
ATOM   855  C CB  . SER A 1 110 ? 20.02900  -36.50600 -27.41800 1.000 64.62000  ? 159 SER A CB  1 
ATOM   856  O OG  . SER A 1 110 ? 18.69500  -36.95800 -27.49500 1.000 73.54000  ? 159 SER A OG  1 
ATOM   857  N N   . LEU A 1 111 ? 17.93500  -33.92000 -27.66600 1.000 57.05000  ? 160 LEU A N   1 
ATOM   858  C CA  . LEU A 1 111 ? 16.69500  -33.23500 -27.30800 1.000 53.29000  ? 160 LEU A CA  1 
ATOM   859  C C   . LEU A 1 111 ? 15.55500  -33.75200 -28.17800 1.000 54.57000  ? 160 LEU A C   1 
ATOM   860  O O   . LEU A 1 111 ? 15.67500  -33.76500 -29.40400 1.000 55.23000  ? 160 LEU A O   1 
ATOM   861  C CB  . LEU A 1 111 ? 16.85100  -31.71900 -27.49500 1.000 50.72000  ? 160 LEU A CB  1 
ATOM   862  C CG  . LEU A 1 111 ? 15.68500  -30.79000 -27.18700 1.000 49.12000  ? 160 LEU A CG  1 
ATOM   863  C CD1 . LEU A 1 111 ? 15.49800  -30.76300 -25.70600 1.000 48.73000  ? 160 LEU A CD1 1 
ATOM   864  C CD2 . LEU A 1 111 ? 15.99200  -29.40300 -27.69700 1.000 53.00000  ? 160 LEU A CD2 1 
ATOM   865  N N   . MET A 1 112 ? 14.46300  -34.19800 -27.56100 1.000 53.71000  ? 161 MET A N   1 
ATOM   866  C CA  . MET A 1 112 ? 13.28100  -34.59700 -28.32100 1.000 44.29000  ? 161 MET A CA  1 
ATOM   867  C C   . MET A 1 112 ? 12.43000  -33.38600 -28.65900 1.000 48.16000  ? 161 MET A C   1 
ATOM   868  O O   . MET A 1 112 ? 12.03000  -32.62600 -27.76400 1.000 48.37000  ? 161 MET A O   1 
ATOM   869  C CB  . MET A 1 112 ? 12.42300  -35.60000 -27.54300 1.000 48.27000  ? 161 MET A CB  1 
ATOM   870  C CG  . MET A 1 112 ? 13.12900  -36.85200 -27.06400 1.000 69.02000  ? 161 MET A CG  1 
ATOM   871  S SD  . MET A 1 112 ? 13.44700  -37.98200 -28.45400 1.000 94.45000  ? 161 MET A SD  1 
ATOM   872  C CE  . MET A 1 112 ? 11.95900  -37.75500 -29.47400 1.000 58.04000  ? 161 MET A CE  1 
ATOM   873  N N   . ILE A 1 113 ? 12.09900  -33.24400 -29.93900 1.000 45.96000  ? 162 ILE A N   1 
ATOM   874  C CA  . ILE A 1 113 ? 11.31000  -32.12400 -30.44000 1.000 40.73000  ? 162 ILE A CA  1 
ATOM   875  C C   . ILE A 1 113 ? 10.07300  -32.67000 -31.13000 1.000 47.40000  ? 162 ILE A C   1 
ATOM   876  O O   . ILE A 1 113 ? 10.16800  -33.55200 -31.99300 1.000 50.32000  ? 162 ILE A O   1 
ATOM   877  C CB  . ILE A 1 113 ? 12.10300  -31.24600 -31.41700 1.000 45.30000  ? 162 ILE A CB  1 
ATOM   878  C CG1 . ILE A 1 113 ? 13.45100  -30.84300 -30.82000 1.000 52.15000  ? 162 ILE A CG1 1 
ATOM   879  C CG2 . ILE A 1 113 ? 11.28300  -30.01100 -31.78300 1.000 42.67000  ? 162 ILE A CG2 1 
ATOM   880  C CD1 . ILE A 1 113 ? 14.09000  -29.61600 -31.50100 1.000 44.78000  ? 162 ILE A CD1 1 
ATOM   881  N N   . SER A 1 114 ? 8.91500   -32.13100 -30.77100 1.000 46.15000  ? 163 SER A N   1 
ATOM   882  C CA  . SER A 1 114 ? 7.68800   -32.53000 -31.43700 1.000 46.59000  ? 163 SER A CA  1 
ATOM   883  C C   . SER A 1 114 ? 6.71500   -31.35600 -31.42700 1.000 50.63000  ? 163 SER A C   1 
ATOM   884  O O   . SER A 1 114 ? 6.79300   -30.45500 -30.57300 1.000 35.73000  ? 163 SER A O   1 
ATOM   885  C CB  . SER A 1 114 ? 7.07400   -33.78200 -30.78500 1.000 51.47000  ? 163 SER A CB  1 
ATOM   886  O OG  . SER A 1 114 ? 6.29900   -33.46000 -29.63400 1.000 49.49000  ? 163 SER A OG  1 
ATOM   887  N N   . GLY A 1 115 ? 5.81800   -31.36100 -32.40600 1.000 41.46000  ? 164 GLY A N   1 
ATOM   888  C CA  . GLY A 1 115 ? 4.75500   -30.38100 -32.41700 1.000 46.04000  ? 164 GLY A CA  1 
ATOM   889  C C   . GLY A 1 115 ? 4.13900   -30.28400 -33.79800 1.000 44.05000  ? 164 GLY A C   1 
ATOM   890  O O   . GLY A 1 115 ? 4.27600   -31.18300 -34.61700 1.000 46.87000  ? 164 GLY A O   1 
ATOM   891  N N   . LEU A 1 116 ? 3.41600   -29.19200 -34.00200 1.000 42.38000  ? 165 LEU A N   1 
ATOM   892  C CA  . LEU A 1 116 ? 2.94300   -28.86600 -35.32700 1.000 50.23000  ? 165 LEU A CA  1 
ATOM   893  C C   . LEU A 1 116 ? 4.14300   -28.60000 -36.23900 1.000 50.22000  ? 165 LEU A C   1 
ATOM   894  O O   . LEU A 1 116 ? 5.25700   -28.29800 -35.78900 1.000 45.36000  ? 165 LEU A O   1 
ATOM   895  C CB  . LEU A 1 116 ? 2.01100   -27.65900 -35.25900 1.000 44.75000  ? 165 LEU A CB  1 
ATOM   896  C CG  . LEU A 1 116 ? 0.76100   -27.79200 -34.38700 1.000 52.12000  ? 165 LEU A CG  1 
ATOM   897  C CD1 . LEU A 1 116 ? -0.13200  -26.58200 -34.54500 1.000 37.28000  ? 165 LEU A CD1 1 
ATOM   898  C CD2 . LEU A 1 116 ? -0.02300  -29.08900 -34.65800 1.000 45.45000  ? 165 LEU A CD2 1 
ATOM   899  N N   . THR A 1 117 ? 3.91100   -28.73100 -37.53800 1.000 45.87000  ? 166 THR A N   1 
ATOM   900  C CA  . THR A 1 117 ? 5.01300   -28.66900 -38.49500 1.000 48.00000  ? 166 THR A CA  1 
ATOM   901  C C   . THR A 1 117 ? 5.89300   -27.44600 -38.28900 1.000 47.23000  ? 166 THR A C   1 
ATOM   902  O O   . THR A 1 117 ? 7.11200   -27.56000 -38.12500 1.000 50.30000  ? 166 THR A O   1 
ATOM   903  C CB  . THR A 1 117 ? 4.45400   -28.69000 -39.90000 1.000 41.08000  ? 166 THR A CB  1 
ATOM   904  O OG1 . THR A 1 117 ? 3.70100   -29.89200 -40.05400 1.000 51.65000  ? 166 THR A OG1 1 
ATOM   905  C CG2 . THR A 1 117 ? 5.56700   -28.63500 -40.92000 1.000 56.55000  ? 166 THR A CG2 1 
ATOM   906  N N   . GLU A 1 118 ? 5.29000   -26.26600 -38.26700 1.000 49.10000  ? 167 GLU A N   1 
ATOM   907  C CA  . GLU A 1 118 ? 6.09900   -25.06400 -38.14700 1.000 51.87000  ? 167 GLU A CA  1 
ATOM   908  C C   . GLU A 1 118 ? 6.72000   -24.92300 -36.75600 1.000 52.18000  ? 167 GLU A C   1 
ATOM   909  O O   . GLU A 1 118 ? 7.84600   -24.42200 -36.64400 1.000 47.96000  ? 167 GLU A O   1 
ATOM   910  C CB  . GLU A 1 118 ? 5.26100   -23.84400 -38.52200 1.000 47.82000  ? 167 GLU A CB  1 
ATOM   911  C CG  . GLU A 1 118 ? 4.85100   -23.89700 -39.98300 1.000 56.11000  ? 167 GLU A CG  1 
ATOM   912  C CD  . GLU A 1 118 ? 4.33700   -22.57200 -40.52000 1.000 64.29000  ? 167 GLU A CD  1 
ATOM   913  O OE1 . GLU A 1 118 ? 4.90900   -21.52200 -40.12400 1.000 55.10000  ? 167 GLU A OE1 1 
ATOM   914  O OE2 . GLU A 1 118 ? 3.38800   -22.59600 -41.35300 1.000 57.81000  ? 167 GLU A OE2 1 
ATOM   915  N N   . ALA A 1 119 ? 6.03800   -25.36700 -35.69300 1.000 49.97000  ? 168 ALA A N   1 
ATOM   916  C CA  . ALA A 1 119 ? 6.65300   -25.30400 -34.36400 1.000 46.45000  ? 168 ALA A CA  1 
ATOM   917  C C   . ALA A 1 119 ? 7.91200   -26.16800 -34.30200 1.000 45.08000  ? 168 ALA A C   1 
ATOM   918  O O   . ALA A 1 119 ? 8.97400   -25.70800 -33.86200 1.000 48.05000  ? 168 ALA A O   1 
ATOM   919  C CB  . ALA A 1 119 ? 5.65100   -25.72200 -33.28400 1.000 43.56000  ? 168 ALA A CB  1 
ATOM   920  N N   . PHE A 1 120 ? 7.81400   -27.41800 -34.75600 1.000 39.95000  ? 169 PHE A N   1 
ATOM   921  C CA  . PHE A 1 120 ? 8.98400   -28.29400 -34.85500 1.000 43.26000  ? 169 PHE A CA  1 
ATOM   922  C C   . PHE A 1 120 ? 10.10800  -27.65600 -35.66100 1.000 46.66000  ? 169 PHE A C   1 
ATOM   923  O O   . PHE A 1 120 ? 11.26300  -27.62200 -35.22100 1.000 48.15000  ? 169 PHE A O   1 
ATOM   924  C CB  . PHE A 1 120 ? 8.59500   -29.62300 -35.51200 1.000 46.50000  ? 169 PHE A CB  1 
ATOM   925  C CG  . PHE A 1 120 ? 9.74500   -30.57100 -35.69500 1.000 46.83000  ? 169 PHE A CG  1 
ATOM   926  C CD1 . PHE A 1 120 ? 10.58800  -30.46900 -36.79400 1.000 42.16000  ? 169 PHE A CD1 1 
ATOM   927  C CD2 . PHE A 1 120 ? 9.98900   -31.57100 -34.74800 1.000 44.50000  ? 169 PHE A CD2 1 
ATOM   928  C CE1 . PHE A 1 120 ? 11.65000  -31.34900 -36.96600 1.000 41.47000  ? 169 PHE A CE1 1 
ATOM   929  C CE2 . PHE A 1 120 ? 11.03500  -32.44100 -34.89600 1.000 49.66000  ? 169 PHE A CE2 1 
ATOM   930  C CZ  . PHE A 1 120 ? 11.87700  -32.34000 -36.00800 1.000 52.00000  ? 169 PHE A CZ  1 
ATOM   931  N N   . VAL A 1 121 ? 9.80300   -27.19800 -36.87600 1.000 43.07000  ? 170 VAL A N   1 
ATOM   932  C CA  . VAL A 1 121 ? 10.86600  -26.69700 -37.73900 1.000 43.70000  ? 170 VAL A CA  1 
ATOM   933  C C   . VAL A 1 121 ? 11.54600  -25.50800 -37.08200 1.000 40.37000  ? 170 VAL A C   1 
ATOM   934  O O   . VAL A 1 121 ? 12.77000  -25.36100 -37.13300 1.000 46.60000  ? 170 VAL A O   1 
ATOM   935  C CB  . VAL A 1 121 ? 10.31000  -26.36300 -39.13100 1.000 44.48000  ? 170 VAL A CB  1 
ATOM   936  C CG1 . VAL A 1 121 ? 11.37100  -25.68100 -39.97400 1.000 30.97000  ? 170 VAL A CG1 1 
ATOM   937  C CG2 . VAL A 1 121 ? 9.83000   -27.64000 -39.80500 1.000 38.81000  ? 170 VAL A CG2 1 
ATOM   938  N N   . MET A 1 122 ? 10.76800  -24.67900 -36.40400 1.000 42.72000  ? 171 MET A N   1 
ATOM   939  C CA  . MET A 1 122 ? 11.31300  -23.47800 -35.78900 1.000 41.68000  ? 171 MET A CA  1 
ATOM   940  C C   . MET A 1 122 ? 12.21000  -23.82800 -34.60500 1.000 45.95000  ? 171 MET A C   1 
ATOM   941  O O   . MET A 1 122 ? 13.25400  -23.20300 -34.40500 1.000 50.03000  ? 171 MET A O   1 
ATOM   942  C CB  . MET A 1 122 ? 10.15900  -22.56200 -35.36800 1.000 40.23000  ? 171 MET A CB  1 
ATOM   943  C CG  . MET A 1 122 ? 10.54600  -21.12300 -35.06500 1.000 54.77000  ? 171 MET A CG  1 
ATOM   944  S SD  . MET A 1 122 ? 9.13800   -20.16700 -34.40700 1.000 82.95000  ? 171 MET A SD  1 
ATOM   945  C CE  . MET A 1 122 ? 10.01100  -18.88000 -33.48300 1.000 47.62000  ? 171 MET A CE  1 
ATOM   946  N N   . ALA A 1 123 ? 11.83300  -24.82900 -33.81400 1.000 43.95000  ? 172 ALA A N   1 
ATOM   947  C CA  . ALA A 1 123 ? 12.69000  -25.22700 -32.70000 1.000 45.24000  ? 172 ALA A CA  1 
ATOM   948  C C   . ALA A 1 123 ? 13.94500  -25.92300 -33.19900 1.000 43.14000  ? 172 ALA A C   1 
ATOM   949  O O   . ALA A 1 123 ? 15.04700  -25.66300 -32.70200 1.000 42.12000  ? 172 ALA A O   1 
ATOM   950  C CB  . ALA A 1 123 ? 11.93400  -26.13900 -31.72800 1.000 39.96000  ? 172 ALA A CB  1 
ATOM   951  N N   . GLN A 1 124 ? 13.80200  -26.81200 -34.18300 1.000 46.40000  ? 173 GLN A N   1 
ATOM   952  C CA  . GLN A 1 124 ? 14.97200  -27.50000 -34.71500 1.000 43.39000  ? 173 GLN A CA  1 
ATOM   953  C C   . GLN A 1 124 ? 15.96900  -26.52500 -35.32700 1.000 45.27000  ? 173 GLN A C   1 
ATOM   954  O O   . GLN A 1 124 ? 17.18300  -26.64400 -35.11100 1.000 48.49000  ? 173 GLN A O   1 
ATOM   955  C CB  . GLN A 1 124 ? 14.55300  -28.53100 -35.74200 1.000 39.48000  ? 173 GLN A CB  1 
ATOM   956  C CG  . GLN A 1 124 ? 15.70300  -28.96400 -36.59900 1.000 47.36000  ? 173 GLN A CG  1 
ATOM   957  C CD  . GLN A 1 124 ? 15.31200  -30.05200 -37.55800 1.000 60.33000  ? 173 GLN A CD  1 
ATOM   958  O OE1 . GLN A 1 124 ? 15.87800  -31.13600 -37.50000 1.000 61.03000  ? 173 GLN A OE1 1 
ATOM   959  N NE2 . GLN A 1 124 ? 14.32600  -29.78000 -38.44600 1.000 46.66000  ? 173 GLN A NE2 1 
ATOM   960  N N   . SER A 1 125 ? 15.48300  -25.55300 -36.09400 1.000 42.34000  ? 174 SER A N   1 
ATOM   961  C CA  . SER A 1 125 ? 16.40400  -24.59600 -36.69300 1.000 47.62000  ? 174 SER A CA  1 
ATOM   962  C C   . SER A 1 125 ? 17.14200  -23.80000 -35.61600 1.000 50.27000  ? 174 SER A C   1 
ATOM   963  O O   . SER A 1 125 ? 18.30800  -23.42500 -35.80000 1.000 50.31000  ? 174 SER A O   1 
ATOM   964  C CB  . SER A 1 125 ? 15.65000  -23.69500 -37.67000 1.000 42.59000  ? 174 SER A CB  1 
ATOM   965  O OG  . SER A 1 125 ? 15.05800  -22.62500 -36.96000 1.000 67.45000  ? 174 SER A OG  1 
ATOM   966  N N   . ARG A 1 126 ? 16.48400  -23.53800 -34.48600 1.000 45.94000  ? 175 ARG A N   1 
ATOM   967  C CA  . ARG A 1 126 ? 17.10400  -22.73300 -33.44400 1.000 48.38000  ? 175 ARG A CA  1 
ATOM   968  C C   . ARG A 1 126 ? 18.19700  -23.50500 -32.72700 1.000 51.10000  ? 175 ARG A C   1 
ATOM   969  O O   . ARG A 1 126 ? 19.21000  -22.92400 -32.30900 1.000 54.31000  ? 175 ARG A O   1 
ATOM   970  C CB  . ARG A 1 126 ? 16.05500  -22.27800 -32.43400 1.000 52.46000  ? 175 ARG A CB  1 
ATOM   971  C CG  . ARG A 1 126 ? 16.50500  -21.09300 -31.63800 1.000 54.83000  ? 175 ARG A CG  1 
ATOM   972  C CD  . ARG A 1 126 ? 16.13600  -19.89400 -32.46000 1.000 63.79000  ? 175 ARG A CD  1 
ATOM   973  N NE  . ARG A 1 126 ? 16.88700  -18.70100 -32.12200 1.000 51.29000  ? 175 ARG A NE  1 
ATOM   974  C CZ  . ARG A 1 126 ? 16.30900  -17.57500 -31.74900 1.000 58.42000  ? 175 ARG A CZ  1 
ATOM   975  N NH1 . ARG A 1 126 ? 14.99700  -17.50400 -31.57900 1.000 53.44000  ? 175 ARG A NH1 1 
ATOM   976  N NH2 . ARG A 1 126 ? 17.06200  -16.49400 -31.55400 1.000 54.50000  ? 175 ARG A NH2 1 
ATOM   977  N N   . VAL A 1 127 ? 17.96800  -24.79900 -32.50200 1.000 42.46000  ? 176 VAL A N   1 
ATOM   978  C CA  . VAL A 1 127 ? 18.97700  -25.62900 -31.85100 1.000 47.63000  ? 176 VAL A CA  1 
ATOM   979  C C   . VAL A 1 127 ? 20.18200  -25.80000 -32.76100 1.000 52.54000  ? 176 VAL A C   1 
ATOM   980  O O   . VAL A 1 127 ? 21.33500  -25.73100 -32.31200 1.000 53.68000  ? 176 VAL A O   1 
ATOM   981  C CB  . VAL A 1 127 ? 18.37600  -26.98000 -31.43700 1.000 41.68000  ? 176 VAL A CB  1 
ATOM   982  C CG1 . VAL A 1 127 ? 19.47300  -27.93100 -31.03900 1.000 38.38000  ? 176 VAL A CG1 1 
ATOM   983  C CG2 . VAL A 1 127 ? 17.39300  -26.76300 -30.29800 1.000 46.83000  ? 176 VAL A CG2 1 
ATOM   984  N N   . GLU A 1 128 ? 19.93300  -25.99400 -34.06100 1.000 51.88000  ? 177 GLU A N   1 
ATOM   985  C CA  . GLU A 1 128 ? 21.03100  -26.13900 -35.01000 1.000 53.95000  ? 177 GLU A CA  1 
ATOM   986  C C   . GLU A 1 128 ? 21.86300  -24.87000 -35.06800 1.000 49.15000  ? 177 GLU A C   1 
ATOM   987  O O   . GLU A 1 128 ? 23.09300  -24.93200 -35.16300 1.000 48.46000  ? 177 GLU A O   1 
ATOM   988  C CB  . GLU A 1 128 ? 20.48400  -26.48000 -36.39000 1.000 36.75000  ? 177 GLU A CB  1 
ATOM   989  C CG  . GLU A 1 128 ? 20.62300  -27.94200 -36.74700 1.000 59.62000  ? 177 GLU A CG  1 
ATOM   990  C CD  . GLU A 1 128 ? 19.41900  -28.48400 -37.53500 1.000 77.17000  ? 177 GLU A CD  1 
ATOM   991  O OE1 . GLU A 1 128 ? 18.69700  -27.67400 -38.18000 1.000 76.00000  ? 177 GLU A OE1 1 
ATOM   992  O OE2 . GLU A 1 128 ? 19.19000  -29.72600 -37.49200 1.000 76.60000  ? 177 GLU A OE2 1 
ATOM   993  N N   . GLU A 1 129 ? 21.21100  -23.70900 -34.96400 1.000 48.13000  ? 178 GLU A N   1 
ATOM   994  C CA  . GLU A 1 129 ? 21.95200  -22.45400 -34.93600 1.000 50.70000  ? 178 GLU A CA  1 
ATOM   995  C C   . GLU A 1 129 ? 22.82600  -22.35800 -33.68600 1.000 53.04000  ? 178 GLU A C   1 
ATOM   996  O O   . GLU A 1 129 ? 24.00900  -22.00000 -33.77400 1.000 47.38000  ? 178 GLU A O   1 
ATOM   997  C CB  . GLU A 1 129 ? 20.97500  -21.27500 -35.02300 1.000 43.41000  ? 178 GLU A CB  1 
ATOM   998  C CG  . GLU A 1 129 ? 21.63100  -19.88400 -34.93900 1.000 56.60000  ? 178 GLU A CG  1 
ATOM   999  C CD  . GLU A 1 129 ? 22.33000  -19.45300 -36.24700 1.000 61.03000  ? 178 GLU A CD  1 
ATOM   1000 O OE1 . GLU A 1 129 ? 21.99700  -20.01100 -37.32300 1.000 55.01000  ? 178 GLU A OE1 1 
ATOM   1001 O OE2 . GLU A 1 129 ? 23.20400  -18.54900 -36.20200 1.000 62.69000  ? 178 GLU A OE2 1 
ATOM   1002 N N   . LEU A 1 130 ? 22.28200  -22.73100 -32.52300 1.000 47.73000  ? 179 LEU A N   1 
ATOM   1003 C CA  . LEU A 1 130 ? 23.08500  -22.71400 -31.30700 1.000 48.64000  ? 179 LEU A CA  1 
ATOM   1004 C C   . LEU A 1 130 ? 24.25800  -23.69400 -31.42000 1.000 49.19000  ? 179 LEU A C   1 
ATOM   1005 O O   . LEU A 1 130 ? 25.40700  -23.34900 -31.10700 1.000 41.14000  ? 179 LEU A O   1 
ATOM   1006 C CB  . LEU A 1 130 ? 22.19300  -23.03700 -30.10200 1.000 45.53000  ? 179 LEU A CB  1 
ATOM   1007 C CG  . LEU A 1 130 ? 21.26700  -21.92100 -29.60800 1.000 44.02000  ? 179 LEU A CG  1 
ATOM   1008 C CD1 . LEU A 1 130 ? 20.13100  -22.43700 -28.68400 1.000 33.62000  ? 179 LEU A CD1 1 
ATOM   1009 C CD2 . LEU A 1 130 ? 22.05600  -20.83300 -28.90800 1.000 43.27000  ? 179 LEU A CD2 1 
ATOM   1010 N N   . ALA A 1 131 ? 23.99100  -24.91000 -31.91400 1.000 39.83000  ? 180 ALA A N   1 
ATOM   1011 C CA  . ALA A 1 131 ? 25.06000  -25.88900 -32.10200 1.000 48.08000  ? 180 ALA A CA  1 
ATOM   1012 C C   . ALA A 1 131 ? 26.08300  -25.40400 -33.11800 1.000 48.46000  ? 180 ALA A C   1 
ATOM   1013 O O   . ALA A 1 131 ? 27.29300  -25.59600 -32.94200 1.000 52.28000  ? 180 ALA A O   1 
ATOM   1014 C CB  . ALA A 1 131 ? 24.48000  -27.23000 -32.54600 1.000 47.72000  ? 180 ALA A CB  1 
ATOM   1015 N N   . GLU A 1 132 ? 25.61100  -24.78400 -34.19400 1.000 55.04000  ? 181 GLU A N   1 
ATOM   1016 C CA  . GLU A 1 132 ? 26.51500  -24.24800 -35.20400 1.000 51.68000  ? 181 GLU A CA  1 
ATOM   1017 C C   . GLU A 1 132 ? 27.45100  -23.21300 -34.60500 1.000 54.28000  ? 181 GLU A C   1 
ATOM   1018 O O   . GLU A 1 132 ? 28.66400  -23.25100 -34.83700 1.000 53.49000  ? 181 GLU A O   1 
ATOM   1019 C CB  . GLU A 1 132 ? 25.67900  -23.64200 -36.33800 1.000 51.71000  ? 181 GLU A CB  1 
ATOM   1020 C CG  . GLU A 1 132 ? 26.36100  -22.55900 -37.14900 1.000 72.53000  ? 181 GLU A CG  1 
ATOM   1021 C CD  . GLU A 1 132 ? 27.22000  -23.11900 -38.26700 1.000 82.81000  ? 181 GLU A CD  1 
ATOM   1022 O OE1 . GLU A 1 132 ? 26.92600  -24.25400 -38.71000 1.000 74.51000  ? 181 GLU A OE1 1 
ATOM   1023 O OE2 . GLU A 1 132 ? 28.18900  -22.42800 -38.68200 1.000 81.73000  ? 181 GLU A OE2 1 
ATOM   1024 N N   . ARG A 1 133 ? 26.91300  -22.33400 -33.76100 1.000 55.80000  ? 182 ARG A N   1 
ATOM   1025 C CA  . ARG A 1 133 ? 27.68700  -21.25200 -33.19000 1.000 45.26000  ? 182 ARG A CA  1 
ATOM   1026 C C   . ARG A 1 133 ? 28.71600  -21.73100 -32.18200 1.000 52.45000  ? 182 ARG A C   1 
ATOM   1027 O O   . ARG A 1 133 ? 29.59300  -20.95100 -31.80900 1.000 57.03000  ? 182 ARG A O   1 
ATOM   1028 C CB  . ARG A 1 133 ? 26.72500  -20.24100 -32.57400 1.000 47.34000  ? 182 ARG A CB  1 
ATOM   1029 C CG  . ARG A 1 133 ? 25.91200  -19.51600 -33.64300 1.000 54.19000  ? 182 ARG A CG  1 
ATOM   1030 C CD  . ARG A 1 133 ? 24.74100  -18.74500 -33.06600 1.000 51.42000  ? 182 ARG A CD  1 
ATOM   1031 N NE  . ARG A 1 133 ? 25.11400  -17.36400 -32.80000 1.000 59.91000  ? 182 ARG A NE  1 
ATOM   1032 C CZ  . ARG A 1 133 ? 24.74900  -16.33800 -33.54900 1.000 52.36000  ? 182 ARG A CZ  1 
ATOM   1033 N NH1 . ARG A 1 133 ? 24.00600  -16.51000 -34.62400 1.000 46.55000  ? 182 ARG A NH1 1 
ATOM   1034 N NH2 . ARG A 1 133 ? 25.13700  -15.11000 -33.20300 1.000 57.82000  ? 182 ARG A NH2 1 
ATOM   1035 N N   . LEU A 1 134 ? 28.66600  -23.00100 -31.77900 1.000 55.65000  ? 183 LEU A N   1 
ATOM   1036 C CA  . LEU A 1 134 ? 29.69100  -23.53700 -30.88900 1.000 57.61000  ? 183 LEU A CA  1 
ATOM   1037 C C   . LEU A 1 134 ? 31.10100  -23.36000 -31.45700 1.000 63.70000  ? 183 LEU A C   1 
ATOM   1038 O O   . LEU A 1 134 ? 32.05700  -23.19600 -30.68600 1.000 62.02000  ? 183 LEU A O   1 
ATOM   1039 C CB  . LEU A 1 134 ? 29.42200  -25.01600 -30.62100 1.000 56.64000  ? 183 LEU A CB  1 
ATOM   1040 C CG  . LEU A 1 134 ? 28.67400  -25.33700 -29.33800 1.000 56.40000  ? 183 LEU A CG  1 
ATOM   1041 C CD1 . LEU A 1 134 ? 28.25200  -26.79500 -29.32900 1.000 56.08000  ? 183 LEU A CD1 1 
ATOM   1042 C CD2 . LEU A 1 134 ? 29.53900  -25.00900 -28.13200 1.000 53.98000  ? 183 LEU A CD2 1 
ATOM   1043 N N   . SER A 1 135 ? 31.26200  -23.35600 -32.79000 1.000 59.19000  ? 184 SER A N   1 
ATOM   1044 C CA  . SER A 1 135 ? 32.60000  -23.37200 -33.37600 1.000 63.51000  ? 184 SER A CA  1 
ATOM   1045 C C   . SER A 1 135 ? 33.01700  -22.04300 -33.99900 1.000 63.13000  ? 184 SER A C   1 
ATOM   1046 O O   . SER A 1 135 ? 33.99800  -22.00700 -34.74200 1.000 66.22000  ? 184 SER A O   1 
ATOM   1047 C CB  . SER A 1 135 ? 32.67900  -24.44800 -34.44900 1.000 55.38000  ? 184 SER A CB  1 
ATOM   1048 O OG  . SER A 1 135 ? 31.77800  -24.11900 -35.48500 1.000 59.22000  ? 184 SER A OG  1 
ATOM   1049 N N   . TRP A 1 136 ? 32.38100  -20.94300 -33.62400 1.000 65.76000  ? 185 TRP A N   1 
ATOM   1050 C CA  . TRP A 1 136 ? 32.71800  -19.63400 -34.16100 1.000 63.69000  ? 185 TRP A CA  1 
ATOM   1051 C C   . TRP A 1 136 ? 33.77000  -18.97000 -33.27700 1.000 74.78000  ? 185 TRP A C   1 
ATOM   1052 O O   . TRP A 1 136 ? 33.95000  -19.33900 -32.11300 1.000 70.85000  ? 185 TRP A O   1 
ATOM   1053 C CB  . TRP A 1 136 ? 31.47600  -18.74100 -34.23700 1.000 57.63000  ? 185 TRP A CB  1 
ATOM   1054 C CG  . TRP A 1 136 ? 30.42600  -19.20200 -35.20200 1.000 56.25000  ? 185 TRP A CG  1 
ATOM   1055 C CD1 . TRP A 1 136 ? 30.41600  -20.37000 -35.90000 1.000 51.76000  ? 185 TRP A CD1 1 
ATOM   1056 C CD2 . TRP A 1 136 ? 29.22100  -18.50300 -35.56600 1.000 48.01000  ? 185 TRP A CD2 1 
ATOM   1057 N NE1 . TRP A 1 136 ? 29.28300  -20.44400 -36.67100 1.000 47.13000  ? 185 TRP A NE1 1 
ATOM   1058 C CE2 . TRP A 1 136 ? 28.53100  -19.31400 -36.48400 1.000 46.72000  ? 185 TRP A CE2 1 
ATOM   1059 C CE3 . TRP A 1 136 ? 28.65600  -17.27200 -35.19700 1.000 52.21000  ? 185 TRP A CE3 1 
ATOM   1060 C CZ2 . TRP A 1 136 ? 27.29900  -18.93600 -37.05100 1.000 53.35000  ? 185 TRP A CZ2 1 
ATOM   1061 C CZ3 . TRP A 1 136 ? 27.41600  -16.89600 -35.75900 1.000 50.48000  ? 185 TRP A CZ3 1 
ATOM   1062 C CH2 . TRP A 1 136 ? 26.76000  -17.72700 -36.67300 1.000 47.68000  ? 185 TRP A CH2 1 
ATOM   1063 N N   . ASP A 1 137 ? 34.45100  -17.96200 -33.83200 1.000 74.24000  ? 186 ASP A N   1 
ATOM   1064 C CA  . ASP A 1 137 ? 35.42000  -17.16300 -33.08400 1.000 84.63000  ? 186 ASP A CA  1 
ATOM   1065 C C   . ASP A 1 137 ? 35.07800  -15.67500 -33.14700 1.000 86.99000  ? 186 ASP A C   1 
ATOM   1066 O O   . ASP A 1 137 ? 35.01600  -15.09000 -34.23400 1.000 84.34000  ? 186 ASP A O   1 
ATOM   1067 C CB  . ASP A 1 137 ? 36.84300  -17.39000 -33.59000 1.000 82.70000  ? 186 ASP A CB  1 
ATOM   1068 C CG  . ASP A 1 137 ? 37.87900  -16.75400 -32.67000 1.000 97.08000  ? 186 ASP A CG  1 
ATOM   1069 O OD1 . ASP A 1 137 ? 37.78500  -16.96500 -31.43700 1.000 91.63000  ? 186 ASP A OD1 1 
ATOM   1070 O OD2 . ASP A 1 137 ? 38.76700  -16.02400 -33.17700 1.000 101.11000 ? 186 ASP A OD2 1 
ATOM   1071 N N   . PHE A 1 138 ? 34.89900  -15.06300 -31.97500 1.000 87.58000  ? 187 PHE A N   1 
ATOM   1072 C CA  . PHE A 1 138 ? 34.65700  -13.62200 -31.85600 1.000 92.29000  ? 187 PHE A CA  1 
ATOM   1073 C C   . PHE A 1 138 ? 35.80700  -12.91400 -31.12100 1.000 97.88000  ? 187 PHE A C   1 
ATOM   1074 O O   . PHE A 1 138 ? 36.98000  -13.01500 -31.50600 1.000 98.29000  ? 187 PHE A O   1 
ATOM   1075 C CB  . PHE A 1 138 ? 33.32600  -13.35900 -31.12900 1.000 84.83000  ? 187 PHE A CB  1 
ATOM   1076 C CG  . PHE A 1 138 ? 32.09100  -13.57300 -31.99500 1.000 87.58000  ? 187 PHE A CG  1 
ATOM   1077 C CD1 . PHE A 1 138 ? 32.20600  -13.95300 -33.33900 1.000 78.08000  ? 187 PHE A CD1 1 
ATOM   1078 C CD2 . PHE A 1 138 ? 30.81400  -13.36900 -31.47200 1.000 89.17000  ? 187 PHE A CD2 1 
ATOM   1079 C CE1 . PHE A 1 138 ? 31.06200  -14.14600 -34.14100 1.000 72.27000  ? 187 PHE A CE1 1 
ATOM   1080 C CE2 . PHE A 1 138 ? 29.66200  -13.55800 -32.26300 1.000 77.22000  ? 187 PHE A CE2 1 
ATOM   1081 C CZ  . PHE A 1 138 ? 29.78600  -13.94500 -33.59500 1.000 72.27000  ? 187 PHE A CZ  1 
ATOM   1082 N N   . THR A 1 150 ? 32.72100  -5.70300  -26.77800 1.000 90.20000  ? 196 THR A N   1 
ATOM   1083 C CA  . THR A 1 150 ? 31.31900  -5.60800  -26.37900 1.000 99.69000  ? 196 THR A CA  1 
ATOM   1084 C C   . THR A 1 150 ? 31.12700  -6.32000  -25.03200 1.000 106.12000 ? 196 THR A C   1 
ATOM   1085 O O   . THR A 1 150 ? 31.94800  -7.16700  -24.65000 1.000 104.68000 ? 196 THR A O   1 
ATOM   1086 C CB  . THR A 1 150 ? 30.39600  -6.21700  -27.45100 1.000 30.00000  ? 196 THR A CB  1 
ATOM   1087 O OG1 . THR A 1 150 ? 30.75300  -7.58600  -27.67000 1.000 30.00000  ? 196 THR A OG1 1 
ATOM   1088 C CG2 . THR A 1 150 ? 30.64700  -5.56800  -28.80300 1.000 30.00000  ? 196 THR A CG2 1 
ATOM   1089 N N   . GLY A 1 151 ? 30.07500  -5.93300  -24.29700 1.000 104.74000 ? 197 GLY A N   1 
ATOM   1090 C CA  . GLY A 1 151 ? 29.68000  -6.59200  -23.06200 1.000 93.67000  ? 197 GLY A CA  1 
ATOM   1091 C C   . GLY A 1 151 ? 28.59600  -7.65300  -23.21000 1.000 84.60000  ? 197 GLY A C   1 
ATOM   1092 O O   . GLY A 1 151 ? 27.53300  -7.55600  -22.59100 1.000 77.75000  ? 197 GLY A O   1 
ATOM   1093 N N   . VAL A 1 152 ? 28.83100  -8.66300  -24.04700 1.000 82.82000  ? 198 VAL A N   1 
ATOM   1094 C CA  . VAL A 1 152 ? 27.85200  -9.73400  -24.20700 1.000 73.56000  ? 198 VAL A CA  1 
ATOM   1095 C C   . VAL A 1 152 ? 27.89700  -10.66700 -23.00200 1.000 71.72000  ? 198 VAL A C   1 
ATOM   1096 O O   . VAL A 1 152 ? 26.85600  -11.05700 -22.45800 1.000 69.95000  ? 198 VAL A O   1 
ATOM   1097 C CB  . VAL A 1 152 ? 28.08500  -10.49000 -25.52800 1.000 72.36000  ? 198 VAL A CB  1 
ATOM   1098 C CG1 . VAL A 1 152 ? 27.58500  -11.93000 -25.42800 1.000 63.85000  ? 198 VAL A CG1 1 
ATOM   1099 C CG2 . VAL A 1 152 ? 27.37900  -9.77900  -26.65700 1.000 77.12000  ? 198 VAL A CG2 1 
ATOM   1100 N N   . LEU A 1 153 ? 29.10500  -11.05500 -22.57900 1.000 68.95000  ? 199 LEU A N   1 
ATOM   1101 C CA  . LEU A 1 153 ? 29.23900  -11.79200 -21.32900 1.000 66.81000  ? 199 LEU A CA  1 
ATOM   1102 C C   . LEU A 1 153 ? 28.49400  -11.09700 -20.20000 1.000 65.83000  ? 199 LEU A C   1 
ATOM   1103 O O   . LEU A 1 153 ? 27.90400  -11.76900 -19.34800 1.000 68.42000  ? 199 LEU A O   1 
ATOM   1104 C CB  . LEU A 1 153 ? 30.71400  -11.97800 -20.95600 1.000 55.24000  ? 199 LEU A CB  1 
ATOM   1105 C CG  . LEU A 1 153 ? 30.94000  -12.96300 -19.80200 1.000 61.92000  ? 199 LEU A CG  1 
ATOM   1106 C CD1 . LEU A 1 153 ? 30.37300  -14.32000 -20.13300 1.000 62.10000  ? 199 LEU A CD1 1 
ATOM   1107 C CD2 . LEU A 1 153 ? 32.40700  -13.11000 -19.49200 1.000 58.75000  ? 199 LEU A CD2 1 
ATOM   1108 N N   . ARG A 1 154 ? 28.46400  -9.75900  -20.19700 1.000 66.53000  ? 200 ARG A N   1 
ATOM   1109 C CA  . ARG A 1 154 ? 27.82800  -9.04000  -19.09300 1.000 68.22000  ? 200 ARG A CA  1 
ATOM   1110 C C   . ARG A 1 154 ? 26.31600  -9.23000  -19.12900 1.000 67.99000  ? 200 ARG A C   1 
ATOM   1111 O O   . ARG A 1 154 ? 25.70400  -9.60100  -18.11900 1.000 56.99000  ? 200 ARG A O   1 
ATOM   1112 C CB  . ARG A 1 154 ? 28.19700  -7.54700  -19.13300 1.000 78.88000  ? 200 ARG A CB  1 
ATOM   1113 C CG  . ARG A 1 154 ? 27.20300  -6.60100  -18.38600 1.000 90.44000  ? 200 ARG A CG  1 
ATOM   1114 C CD  . ARG A 1 154 ? 27.59500  -5.09900  -18.41900 1.000 90.75000  ? 200 ARG A CD  1 
ATOM   1115 N NE  . ARG A 1 154 ? 27.36000  -4.41600  -17.14300 1.000 105.35000 ? 200 ARG A NE  1 
ATOM   1116 C CZ  . ARG A 1 154 ? 27.97000  -3.30100  -16.74700 1.000 101.91000 ? 200 ARG A CZ  1 
ATOM   1117 N NH1 . ARG A 1 154 ? 28.85400  -2.68200  -17.51700 1.000 94.90000  ? 200 ARG A NH1 1 
ATOM   1118 N NH2 . ARG A 1 154 ? 27.67400  -2.78400  -15.55400 1.000 80.38000  ? 200 ARG A NH2 1 
ATOM   1119 N N   . ASP A 1 155 ? 25.69500  -8.98200  -20.28900 1.000 69.19000  ? 201 ASP A N   1 
ATOM   1120 C CA  . ASP A 1 155 ? 24.24700  -9.13700  -20.40100 1.000 71.14000  ? 201 ASP A CA  1 
ATOM   1121 C C   . ASP A 1 155 ? 23.82500  -10.58900 -20.24500 1.000 63.94000  ? 201 ASP A C   1 
ATOM   1122 O O   . ASP A 1 155 ? 22.72300  -10.86700 -19.76100 1.000 57.10000  ? 201 ASP A O   1 
ATOM   1123 C CB  . ASP A 1 155 ? 23.74200  -8.59700  -21.74200 1.000 73.94000  ? 201 ASP A CB  1 
ATOM   1124 C CG  . ASP A 1 155 ? 24.32000  -7.23500  -22.08700 1.000 83.87000  ? 201 ASP A CG  1 
ATOM   1125 O OD1 . ASP A 1 155 ? 24.91900  -6.59900  -21.18600 1.000 83.99000  ? 201 ASP A OD1 1 
ATOM   1126 O OD2 . ASP A 1 155 ? 24.17400  -6.80600  -23.26400 1.000 83.85000  ? 201 ASP A OD2 1 
ATOM   1127 N N   . PHE A 1 156 ? 24.67400  -11.52300 -20.66700 1.000 63.61000  ? 202 PHE A N   1 
ATOM   1128 C CA  . PHE A 1 156 ? 24.32000  -12.93000 -20.54400 1.000 59.91000  ? 202 PHE A CA  1 
ATOM   1129 C C   . PHE A 1 156 ? 24.34700  -13.37400 -19.08600 1.000 51.69000  ? 202 PHE A C   1 
ATOM   1130 O O   . PHE A 1 156 ? 23.41300  -14.02300 -18.61400 1.000 55.54000  ? 202 PHE A O   1 
ATOM   1131 C CB  . PHE A 1 156 ? 25.25600  -13.79400 -21.39300 1.000 56.94000  ? 202 PHE A CB  1 
ATOM   1132 C CG  . PHE A 1 156 ? 24.95400  -15.26000 -21.30800 1.000 53.49000  ? 202 PHE A CG  1 
ATOM   1133 C CD1 . PHE A 1 156 ? 23.80100  -15.78300 -21.89400 1.000 49.65000  ? 202 PHE A CD1 1 
ATOM   1134 C CD2 . PHE A 1 156 ? 25.79200  -16.11100 -20.61000 1.000 52.61000  ? 202 PHE A CD2 1 
ATOM   1135 C CE1 . PHE A 1 156 ? 23.50500  -17.13800 -21.79500 1.000 49.17000  ? 202 PHE A CE1 1 
ATOM   1136 C CE2 . PHE A 1 156 ? 25.50300  -17.47000 -20.51600 1.000 51.00000  ? 202 PHE A CE2 1 
ATOM   1137 C CZ  . PHE A 1 156 ? 24.36200  -17.98100 -21.10900 1.000 48.77000  ? 202 PHE A CZ  1 
ATOM   1138 N N   . SER A 1 157 ? 25.39900  -13.00900 -18.34900 1.000 59.36000  ? 203 SER A N   1 
ATOM   1139 C CA  . SER A 1 157 ? 25.46500  -13.34300 -16.92700 1.000 58.10000  ? 203 SER A CA  1 
ATOM   1140 C C   . SER A 1 157 ? 24.25000  -12.84100 -16.18400 1.000 49.04000  ? 203 SER A C   1 
ATOM   1141 O O   . SER A 1 157 ? 23.76100  -13.51200 -15.27100 1.000 57.57000  ? 203 SER A O   1 
ATOM   1142 C CB  . SER A 1 157 ? 26.71200  -12.73800 -16.28800 1.000 54.74000  ? 203 SER A CB  1 
ATOM   1143 O OG  . SER A 1 157 ? 27.87300  -13.38300 -16.77200 1.000 70.13000  ? 203 SER A OG  1 
ATOM   1144 N N   . ALA A 1 158 ? 23.72700  -11.68600 -16.58700 1.000 51.33000  ? 204 ALA A N   1 
ATOM   1145 C CA  . ALA A 1 158 ? 22.56000  -11.12300 -15.92600 1.000 54.33000  ? 204 ALA A CA  1 
ATOM   1146 C C   . ALA A 1 158 ? 21.33200  -12.02200 -16.03800 1.000 58.47000  ? 204 ALA A C   1 
ATOM   1147 O O   . ALA A 1 158 ? 20.41900  -11.89600 -15.21300 1.000 65.33000  ? 204 ALA A O   1 
ATOM   1148 C CB  . ALA A 1 158 ? 22.26500  -9.74400  -16.50700 1.000 57.41000  ? 204 ALA A CB  1 
ATOM   1149 N N   . LEU A 1 159 ? 21.26800  -12.89600 -17.05700 1.000 46.69000  ? 205 LEU A N   1 
ATOM   1150 C CA  . LEU A 1 159 ? 20.14900  -13.83800 -17.16200 1.000 55.35000  ? 205 LEU A CA  1 
ATOM   1151 C C   . LEU A 1 159 ? 20.23400  -14.92400 -16.09900 1.000 52.45000  ? 205 LEU A C   1 
ATOM   1152 O O   . LEU A 1 159 ? 19.20600  -15.48100 -15.69800 1.000 59.86000  ? 205 LEU A O   1 
ATOM   1153 C CB  . LEU A 1 159 ? 20.09700  -14.48500 -18.55500 1.000 52.18000  ? 205 LEU A CB  1 
ATOM   1154 C CG  . LEU A 1 159 ? 20.00100  -13.54800 -19.75700 1.000 52.34000  ? 205 LEU A CG  1 
ATOM   1155 C CD1 . LEU A 1 159 ? 20.42200  -14.27500 -21.00700 1.000 51.65000  ? 205 LEU A CD1 1 
ATOM   1156 C CD2 . LEU A 1 159 ? 18.59800  -12.98400 -19.89400 1.000 55.41000  ? 205 LEU A CD2 1 
ATOM   1157 N N   . LEU A 1 160 ? 21.44100  -15.23500 -15.63100 1.000 51.41000  ? 206 LEU A N   1 
ATOM   1158 C CA  . LEU A 1 160 ? 21.65500  -16.34600 -14.70200 1.000 57.45000  ? 206 LEU A CA  1 
ATOM   1159 C C   . LEU A 1 160 ? 21.43500  -15.86100 -13.26200 1.000 59.25000  ? 206 LEU A C   1 
ATOM   1160 O O   . LEU A 1 160 ? 22.35000  -15.70600 -12.45100 1.000 60.87000  ? 206 LEU A O   1 
ATOM   1161 C CB  . LEU A 1 160 ? 23.04400  -16.94400 -14.91700 1.000 48.61000  ? 206 LEU A CB  1 
ATOM   1162 C CG  . LEU A 1 160 ? 23.42700  -17.17700 -16.39100 1.000 47.58000  ? 206 LEU A CG  1 
ATOM   1163 C CD1 . LEU A 1 160 ? 24.82000  -17.74300 -16.53700 1.000 46.79000  ? 206 LEU A CD1 1 
ATOM   1164 C CD2 . LEU A 1 160 ? 22.44200  -18.11000 -17.09300 1.000 43.23000  ? 206 LEU A CD2 1 
ATOM   1165 N N   . GLN A 1 161 ? 20.17300  -15.63200 -12.94300 1.000 57.15000  ? 207 GLN A N   1 
ATOM   1166 C CA  A GLN A 1 161 ? 19.79300  -15.10100 -11.64600 0.580 57.82000  ? 207 GLN A CA  1 
ATOM   1167 C CA  B GLN A 1 161 ? 19.80300  -15.09900 -11.64300 0.420 57.85000  ? 207 GLN A CA  1 
ATOM   1168 C C   . GLN A 1 161 ? 19.21900  -16.16300 -10.71800 1.000 57.76000  ? 207 GLN A C   1 
ATOM   1169 O O   . GLN A 1 161 ? 18.93000  -15.86300 -9.55400  1.000 63.41000  ? 207 GLN A O   1 
ATOM   1170 C CB  A GLN A 1 161 ? 18.78300  -13.96300 -11.82300 0.580 59.98000  ? 207 GLN A CB  1 
ATOM   1171 C CB  B GLN A 1 161 ? 18.82300  -13.92900 -11.83400 0.420 59.98000  ? 207 GLN A CB  1 
ATOM   1172 C CG  A GLN A 1 161 ? 17.36100  -14.44200 -12.04500 0.580 61.64000  ? 207 GLN A CG  1 
ATOM   1173 C CG  B GLN A 1 161 ? 18.51900  -13.08200 -10.59900 0.420 63.63000  ? 207 GLN A CG  1 
ATOM   1174 C CD  A GLN A 1 161 ? 16.61300  -13.61300 -13.05800 0.580 58.49000  ? 207 GLN A CD  1 
ATOM   1175 C CD  B GLN A 1 161 ? 19.75500  -12.50700 -9.94300  0.420 59.30000  ? 207 GLN A CD  1 
ATOM   1176 O OE1 A GLN A 1 161 ? 17.20600  -12.83000 -13.79900 0.580 66.18000  ? 207 GLN A OE1 1 
ATOM   1177 O OE1 B GLN A 1 161 ? 20.09600  -12.86200 -8.81500  0.420 62.32000  ? 207 GLN A OE1 1 
ATOM   1178 N NE2 A GLN A 1 161 ? 15.29800  -13.76500 -13.08200 0.580 50.18000  ? 207 GLN A NE2 1 
ATOM   1179 N NE2 B GLN A 1 161 ? 20.44200  -11.62800 -10.65300 0.420 59.97000  ? 207 GLN A NE2 1 
ATOM   1180 N N   . SER A 1 162 ? 19.06400  -17.41300 -11.19700 1.000 59.86000  ? 208 SER A N   1 
ATOM   1181 C CA  . SER A 1 162 ? 18.46400  -18.47100 -10.38500 1.000 58.48000  ? 208 SER A CA  1 
ATOM   1182 C C   . SER A 1 162 ? 19.46900  -19.01000 -9.35300  1.000 62.53000  ? 208 SER A C   1 
ATOM   1183 O O   . SER A 1 162 ? 20.66100  -19.15900 -9.64600  1.000 61.38000  ? 208 SER A O   1 
ATOM   1184 C CB  . SER A 1 162 ? 17.93100  -19.60600 -11.27200 1.000 54.67000  ? 208 SER A CB  1 
ATOM   1185 O OG  . SER A 1 162 ? 18.96600  -20.27700 -11.95000 1.000 59.83000  ? 208 SER A OG  1 
ATOM   1186 N N   . PRO A 1 163 ? 19.01800  -19.30400 -8.13900  1.000 68.85000  ? 209 PRO A N   1 
ATOM   1187 C CA  . PRO A 1 163 ? 19.94300  -19.78500 -7.10400  1.000 68.44000  ? 209 PRO A CA  1 
ATOM   1188 C C   . PRO A 1 163 ? 20.31000  -21.25600 -7.25100  1.000 64.02000  ? 209 PRO A C   1 
ATOM   1189 O O   . PRO A 1 163 ? 19.52400  -22.08700 -7.71400  1.000 62.43000  ? 209 PRO A O   1 
ATOM   1190 C CB  . PRO A 1 163 ? 19.17600  -19.53000 -5.79600  1.000 56.69000  ? 209 PRO A CB  1 
ATOM   1191 C CG  . PRO A 1 163 ? 17.72500  -19.57900 -6.19000  1.000 65.56000  ? 209 PRO A CG  1 
ATOM   1192 C CD  . PRO A 1 163 ? 17.61600  -19.31200 -7.68800  1.000 63.99000  ? 209 PRO A CD  1 
ATOM   1193 N N   . GLY A 1 164 ? 21.55700  -21.55000 -6.88200  1.000 63.84000  ? 210 GLY A N   1 
ATOM   1194 C CA  . GLY A 1 164 ? 22.07400  -22.90500 -6.85600  1.000 56.11000  ? 210 GLY A CA  1 
ATOM   1195 C C   . GLY A 1 164 ? 22.17500  -23.59100 -8.19800  1.000 61.07000  ? 210 GLY A C   1 
ATOM   1196 O O   . GLY A 1 164 ? 22.03900  -24.81500 -8.27400  1.000 65.52000  ? 210 GLY A O   1 
ATOM   1197 N N   . ASP A 1 165 ? 22.44800  -22.84600 -9.25500  1.000 53.21000  ? 211 ASP A N   1 
ATOM   1198 C CA  . ASP A 1 165 ? 22.45700  -23.42700 -10.59000 1.000 59.55000  ? 211 ASP A CA  1 
ATOM   1199 C C   . ASP A 1 165 ? 23.68500  -24.31500 -10.77300 1.000 53.48000  ? 211 ASP A C   1 
ATOM   1200 O O   . ASP A 1 165 ? 24.80700  -23.82000 -10.90900 1.000 52.35000  ? 211 ASP A O   1 
ATOM   1201 C CB  . ASP A 1 165 ? 22.41300  -22.32100 -11.64100 1.000 57.19000  ? 211 ASP A CB  1 
ATOM   1202 C CG  . ASP A 1 165 ? 22.17300  -22.86600 -13.03600 1.000 56.31000  ? 211 ASP A CG  1 
ATOM   1203 O OD1 . ASP A 1 165 ? 21.86300  -24.08300 -13.14500 1.000 48.87000  ? 211 ASP A OD1 1 
ATOM   1204 O OD2 . ASP A 1 165 ? 22.29900  -22.08100 -14.00400 1.000 53.85000  ? 211 ASP A OD2 1 
ATOM   1205 N N   . ALA A 1 166 ? 23.47100  -25.63400 -10.78200 1.000 57.59000  ? 212 ALA A N   1 
ATOM   1206 C CA  . ALA A 1 166 ? 24.56500  -26.57900 -11.01200 1.000 50.92000  ? 212 ALA A CA  1 
ATOM   1207 C C   . ALA A 1 166 ? 25.22600  -26.38800 -12.37300 1.000 54.68000  ? 212 ALA A C   1 
ATOM   1208 O O   . ALA A 1 166 ? 26.38300  -26.77300 -12.55700 1.000 54.64000  ? 212 ALA A O   1 
ATOM   1209 C CB  . ALA A 1 166 ? 24.05200  -28.01200 -10.90100 1.000 52.88000  ? 212 ALA A CB  1 
ATOM   1210 N N   . HIS A 1 167 ? 24.50300  -25.84000 -13.34800 1.000 61.23000  ? 213 HIS A N   1 
ATOM   1211 C CA  . HIS A 1 167 ? 25.01600  -25.67300 -14.69600 1.000 49.81000  ? 213 HIS A CA  1 
ATOM   1212 C C   . HIS A 1 167 ? 25.52400  -24.26100 -14.96800 1.000 55.50000  ? 213 HIS A C   1 
ATOM   1213 O O   . HIS A 1 167 ? 25.87500  -23.95500 -16.11900 1.000 57.03000  ? 213 HIS A O   1 
ATOM   1214 C CB  . HIS A 1 167 ? 23.93800  -26.05100 -15.73200 1.000 52.93000  ? 213 HIS A CB  1 
ATOM   1215 C CG  . HIS A 1 167 ? 23.24400  -27.35200 -15.45400 1.000 49.34000  ? 213 HIS A CG  1 
ATOM   1216 N ND1 . HIS A 1 167 ? 23.78300  -28.57300 -15.80400 1.000 48.87000  ? 213 HIS A ND1 1 
ATOM   1217 C CD2 . HIS A 1 167 ? 22.03300  -27.62000 -14.89600 1.000 49.55000  ? 213 HIS A CD2 1 
ATOM   1218 C CE1 . HIS A 1 167 ? 22.95200  -29.53900 -15.44000 1.000 56.47000  ? 213 HIS A CE1 1 
ATOM   1219 N NE2 . HIS A 1 167 ? 21.88300  -28.98800 -14.88700 1.000 52.44000  ? 213 HIS A NE2 1 
ATOM   1220 N N   . ARG A 1 168 ? 25.62500  -23.41300 -13.93600 1.000 53.51000  ? 214 ARG A N   1 
ATOM   1221 C CA  . ARG A 1 168 ? 26.05600  -22.03300 -14.15900 1.000 53.93000  ? 214 ARG A CA  1 
ATOM   1222 C C   . ARG A 1 168 ? 27.44200  -21.97000 -14.78500 1.000 60.99000  ? 214 ARG A C   1 
ATOM   1223 O O   . ARG A 1 168 ? 27.69200  -21.12900 -15.65400 1.000 64.48000  ? 214 ARG A O   1 
ATOM   1224 C CB  . ARG A 1 168 ? 26.02800  -21.24300 -12.84800 1.000 58.84000  ? 214 ARG A CB  1 
ATOM   1225 C CG  . ARG A 1 168 ? 26.19100  -19.71600 -13.01100 1.000 60.11000  ? 214 ARG A CG  1 
ATOM   1226 C CD  . ARG A 1 168 ? 26.96200  -19.07900 -11.82500 1.000 56.19000  ? 214 ARG A CD  1 
ATOM   1227 N NE  . ARG A 1 168 ? 27.19400  -17.64300 -11.99100 1.000 60.49000  ? 214 ARG A NE  1 
ATOM   1228 C CZ  . ARG A 1 168 ? 26.24100  -16.72100 -12.07200 1.000 63.89000  ? 214 ARG A CZ  1 
ATOM   1229 N NH1 . ARG A 1 168 ? 24.95900  -17.02900 -11.90600 1.000 60.87000  ? 214 ARG A NH1 1 
ATOM   1230 N NH2 . ARG A 1 168 ? 26.58100  -15.45600 -12.31500 1.000 59.33000  ? 214 ARG A NH2 1 
ATOM   1231 N N   . GLU A 1 169 ? 28.33700  -22.88700 -14.41500 1.000 63.59000  ? 215 GLU A N   1 
ATOM   1232 C CA  . GLU A 1 169 ? 29.69500  -22.82000 -14.94100 1.000 63.22000  ? 215 GLU A CA  1 
ATOM   1233 C C   . GLU A 1 169 ? 29.72200  -23.16500 -16.42300 1.000 60.31000  ? 215 GLU A C   1 
ATOM   1234 O O   . GLU A 1 169 ? 30.29300  -22.42300 -17.22900 1.000 61.04000  ? 215 GLU A O   1 
ATOM   1235 C CB  . GLU A 1 169 ? 30.62500  -23.72400 -14.12800 1.000 63.17000  ? 215 GLU A CB  1 
ATOM   1236 C CG  . GLU A 1 169 ? 31.98200  -23.07300 -13.80200 1.000 79.88000  ? 215 GLU A CG  1 
ATOM   1237 C CD  . GLU A 1 169 ? 31.88200  -21.57500 -13.41200 1.000 94.08000  ? 215 GLU A CD  1 
ATOM   1238 O OE1 . GLU A 1 169 ? 31.22600  -21.22300 -12.39500 1.000 86.09000  ? 215 GLU A OE1 1 
ATOM   1239 O OE2 . GLU A 1 169 ? 32.49000  -20.74200 -14.13800 1.000 88.13000  ? 215 GLU A OE2 1 
ATOM   1240 N N   . ALA A 1 170 ? 29.10400  -24.28500 -16.79900 1.000 55.81000  ? 216 ALA A N   1 
ATOM   1241 C CA  . ALA A 1 170 ? 29.05000  -24.67600 -18.20200 1.000 52.17000  ? 216 ALA A CA  1 
ATOM   1242 C C   . ALA A 1 170 ? 28.43300  -23.57400 -19.07200 1.000 58.77000  ? 216 ALA A C   1 
ATOM   1243 O O   . ALA A 1 170 ? 28.90900  -23.31500 -20.18600 1.000 59.80000  ? 216 ALA A O   1 
ATOM   1244 C CB  . ALA A 1 170 ? 28.27600  -25.99200 -18.34400 1.000 41.74000  ? 216 ALA A CB  1 
ATOM   1245 N N   . LEU A 1 171 ? 27.39700  -22.89500 -18.56700 1.000 50.41000  ? 217 LEU A N   1 
ATOM   1246 C CA  . LEU A 1 171 ? 26.77100  -21.81500 -19.32300 1.000 50.30000  ? 217 LEU A CA  1 
ATOM   1247 C C   . LEU A 1 171 ? 27.76700  -20.69300 -19.58400 1.000 57.63000  ? 217 LEU A C   1 
ATOM   1248 O O   . LEU A 1 171 ? 27.90000  -20.21300 -20.71800 1.000 58.23000  ? 217 LEU A O   1 
ATOM   1249 C CB  . LEU A 1 171 ? 25.54300  -21.28400 -18.57200 1.000 46.89000  ? 217 LEU A CB  1 
ATOM   1250 C CG  . LEU A 1 171 ? 24.31300  -22.20000 -18.48000 1.000 46.01000  ? 217 LEU A CG  1 
ATOM   1251 C CD1 . LEU A 1 171 ? 23.24600  -21.61500 -17.59400 1.000 44.31000  ? 217 LEU A CD1 1 
ATOM   1252 C CD2 . LEU A 1 171 ? 23.73700  -22.53600 -19.85300 1.000 47.95000  ? 217 LEU A CD2 1 
ATOM   1253 N N   . LEU A 1 172 ? 28.49000  -20.27400 -18.54700 1.000 52.91000  ? 218 LEU A N   1 
ATOM   1254 C CA  . LEU A 1 172 ? 29.42700  -19.16800 -18.68500 1.000 52.38000  ? 218 LEU A CA  1 
ATOM   1255 C C   . LEU A 1 172 ? 30.66000  -19.53400 -19.51100 1.000 57.31000  ? 218 LEU A C   1 
ATOM   1256 O O   . LEU A 1 172 ? 31.32400  -18.63100 -20.02800 1.000 58.91000  ? 218 LEU A O   1 
ATOM   1257 C CB  . LEU A 1 172 ? 29.84000  -18.67200 -17.30700 1.000 59.34000  ? 218 LEU A CB  1 
ATOM   1258 C CG  . LEU A 1 172 ? 28.68400  -18.02300 -16.55400 1.000 62.42000  ? 218 LEU A CG  1 
ATOM   1259 C CD1 . LEU A 1 172 ? 29.06500  -17.69800 -15.12000 1.000 52.28000  ? 218 LEU A CD1 1 
ATOM   1260 C CD2 . LEU A 1 172 ? 28.25400  -16.77900 -17.29600 1.000 59.59000  ? 218 LEU A CD2 1 
ATOM   1261 N N   . GLN A 1 173 ? 30.99700  -20.81600 -19.64500 1.000 53.74000  ? 219 GLN A N   1 
ATOM   1262 C CA  . GLN A 1 173 ? 32.05600  -21.20500 -20.57200 1.000 63.18000  ? 219 GLN A CA  1 
ATOM   1263 C C   . GLN A 1 173 ? 31.55000  -21.44000 -21.99400 1.000 62.19000  ? 219 GLN A C   1 
ATOM   1264 O O   . GLN A 1 173 ? 32.28800  -21.96800 -22.82700 1.000 59.72000  ? 219 GLN A O   1 
ATOM   1265 C CB  . GLN A 1 173 ? 32.78200  -22.45000 -20.07200 1.000 63.60000  ? 219 GLN A CB  1 
ATOM   1266 C CG  . GLN A 1 173 ? 33.41000  -22.25000 -18.71100 1.000 79.86000  ? 219 GLN A CG  1 
ATOM   1267 C CD  . GLN A 1 173 ? 33.49100  -23.54800 -17.93400 1.000 95.59000  ? 219 GLN A CD  1 
ATOM   1268 O OE1 . GLN A 1 173 ? 34.04900  -23.59200 -16.82400 1.000 95.64000  ? 219 GLN A OE1 1 
ATOM   1269 N NE2 . GLN A 1 173 ? 32.98300  -24.63900 -18.54300 1.000 80.61000  ? 219 GLN A NE2 1 
ATOM   1270 N N   . LEU A 1 174 ? 30.30900  -21.09200 -22.28700 1.000 54.68000  ? 220 LEU A N   1 
ATOM   1271 C CA  . LEU A 1 174 ? 29.86800  -21.16500 -23.65600 1.000 54.06000  ? 220 LEU A CA  1 
ATOM   1272 C C   . LEU A 1 174 ? 30.56300  -20.07000 -24.46500 1.000 55.35000  ? 220 LEU A C   1 
ATOM   1273 O O   . LEU A 1 174 ? 30.83500  -18.97800 -23.94900 1.000 51.83000  ? 220 LEU A O   1 
ATOM   1274 C CB  . LEU A 1 174 ? 28.35300  -21.00800 -23.74200 1.000 58.84000  ? 220 LEU A CB  1 
ATOM   1275 C CG  . LEU A 1 174 ? 27.53100  -22.17900 -23.21000 1.000 58.85000  ? 220 LEU A CG  1 
ATOM   1276 C CD1 . LEU A 1 174 ? 26.09100  -21.74200 -22.96200 1.000 56.61000  ? 220 LEU A CD1 1 
ATOM   1277 C CD2 . LEU A 1 174 ? 27.59000  -23.36800 -24.16900 1.000 52.47000  ? 220 LEU A CD2 1 
ATOM   1278 N N   . PRO A 1 175 ? 30.89100  -20.35500 -25.72200 1.000 46.62000  ? 221 PRO A N   1 
ATOM   1279 C CA  . PRO A 1 175 ? 31.46300  -19.32300 -26.58600 1.000 42.25000  ? 221 PRO A CA  1 
ATOM   1280 C C   . PRO A 1 175 ? 30.51900  -18.14100 -26.70000 1.000 54.05000  ? 221 PRO A C   1 
ATOM   1281 O O   . PRO A 1 175 ? 29.29900  -18.27100 -26.58600 1.000 56.94000  ? 221 PRO A O   1 
ATOM   1282 C CB  . PRO A 1 175 ? 31.62200  -20.03400 -27.93000 1.000 51.56000  ? 221 PRO A CB  1 
ATOM   1283 C CG  . PRO A 1 175 ? 31.59500  -21.50100 -27.58800 1.000 53.99000  ? 221 PRO A CG  1 
ATOM   1284 C CD  . PRO A 1 175 ? 30.67800  -21.62600 -26.43100 1.000 45.40000  ? 221 PRO A CD  1 
ATOM   1285 N N   . LEU A 1 176 ? 31.10500  -16.97500 -26.94800 1.000 51.75000  ? 222 LEU A N   1 
ATOM   1286 C CA  . LEU A 1 176 ? 30.31900  -15.75000 -26.98700 1.000 60.59000  ? 222 LEU A CA  1 
ATOM   1287 C C   . LEU A 1 176 ? 29.23100  -15.81500 -28.05000 1.000 52.15000  ? 222 LEU A C   1 
ATOM   1288 O O   . LEU A 1 176 ? 28.14600  -15.24400 -27.87100 1.000 52.21000  ? 222 LEU A O   1 
ATOM   1289 C CB  . LEU A 1 176 ? 31.24500  -14.55900 -27.23900 1.000 59.96000  ? 222 LEU A CB  1 
ATOM   1290 C CG  . LEU A 1 176 ? 31.90300  -14.03800 -25.96000 1.000 68.03000  ? 222 LEU A CG  1 
ATOM   1291 C CD1 . LEU A 1 176 ? 33.27100  -13.42900 -26.27300 1.000 54.94000  ? 222 LEU A CD1 1 
ATOM   1292 C CD2 . LEU A 1 176 ? 30.99900  -13.06000 -25.20200 1.000 65.53000  ? 222 LEU A CD2 1 
ATOM   1293 N N   . ALA A 1 177 ? 29.49800  -16.51200 -29.15600 1.000 56.47000  ? 223 ALA A N   1 
ATOM   1294 C CA  . ALA A 1 177 ? 28.52000  -16.59500 -30.23100 1.000 53.44000  ? 223 ALA A CA  1 
ATOM   1295 C C   . ALA A 1 177 ? 27.24300  -17.26800 -29.75400 1.000 55.15000  ? 223 ALA A C   1 
ATOM   1296 O O   . ALA A 1 177 ? 26.13400  -16.84200 -30.10800 1.000 52.72000  ? 223 ALA A O   1 
ATOM   1297 C CB  . ALA A 1 177 ? 29.11900  -17.35200 -31.41500 1.000 51.91000  ? 223 ALA A CB  1 
ATOM   1298 N N   . VAL A 1 178 ? 27.38300  -18.31400 -28.93700 1.000 51.89000  ? 224 VAL A N   1 
ATOM   1299 C CA  . VAL A 1 178 ? 26.22000  -19.00100 -28.39200 1.000 48.75000  ? 224 VAL A CA  1 
ATOM   1300 C C   . VAL A 1 178 ? 25.51300  -18.12300 -27.36900 1.000 49.21000  ? 224 VAL A C   1 
ATOM   1301 O O   . VAL A 1 178 ? 24.28100  -18.01500 -27.37400 1.000 48.94000  ? 224 VAL A O   1 
ATOM   1302 C CB  . VAL A 1 178 ? 26.64900  -20.35200 -27.79900 1.000 49.94000  ? 224 VAL A CB  1 
ATOM   1303 C CG1 . VAL A 1 178 ? 25.47600  -21.05300 -27.09500 1.000 48.13000  ? 224 VAL A CG1 1 
ATOM   1304 C CG2 . VAL A 1 178 ? 27.23000  -21.21400 -28.89300 1.000 46.41000  ? 224 VAL A CG2 1 
ATOM   1305 N N   . GLN A 1 179 ? 26.27500  -17.46700 -26.49200 1.000 49.94000  ? 225 GLN A N   1 
ATOM   1306 C CA  . GLN A 1 179 ? 25.65400  -16.61400 -25.48400 1.000 52.26000  ? 225 GLN A CA  1 
ATOM   1307 C C   . GLN A 1 179 ? 24.82400  -15.51900 -26.12900 1.000 50.64000  ? 225 GLN A C   1 
ATOM   1308 O O   . GLN A 1 179 ? 23.68000  -15.27500 -25.72500 1.000 51.40000  ? 225 GLN A O   1 
ATOM   1309 C CB  . GLN A 1 179 ? 26.72200  -16.00700 -24.58200 1.000 50.09000  ? 225 GLN A CB  1 
ATOM   1310 C CG  . GLN A 1 179 ? 27.38600  -17.02300 -23.71200 1.000 57.13000  ? 225 GLN A CG  1 
ATOM   1311 C CD  . GLN A 1 179 ? 28.63200  -16.49100 -23.04100 1.000 61.65000  ? 225 GLN A CD  1 
ATOM   1312 O OE1 . GLN A 1 179 ? 29.11600  -15.40900 -23.37300 1.000 69.39000  ? 225 GLN A OE1 1 
ATOM   1313 N NE2 . GLN A 1 179 ? 29.16800  -17.25900 -22.09900 1.000 56.43000  ? 225 GLN A NE2 1 
ATOM   1314 N N   . GLU A 1 180 ? 25.37100  -14.88100 -27.16700 1.000 55.18000  ? 226 GLU A N   1 
ATOM   1315 C CA  . GLU A 1 180 ? 24.67200  -13.77900 -27.81900 1.000 52.10000  ? 226 GLU A CA  1 
ATOM   1316 C C   . GLU A 1 180 ? 23.39000  -14.26800 -28.46800 1.000 43.44000  ? 226 GLU A C   1 
ATOM   1317 O O   . GLU A 1 180 ? 22.36200  -13.57900 -28.43300 1.000 45.20000  ? 226 GLU A O   1 
ATOM   1318 C CB  . GLU A 1 180 ? 25.59400  -13.11000 -28.84100 1.000 48.58000  ? 226 GLU A CB  1 
ATOM   1319 C CG  . GLU A 1 180 ? 25.01400  -11.85700 -29.50000 1.000 62.24000  ? 226 GLU A CG  1 
ATOM   1320 C CD  . GLU A 1 180 ? 26.05200  -11.05300 -30.28500 1.000 68.75000  ? 226 GLU A CD  1 
ATOM   1321 O OE1 . GLU A 1 180 ? 26.51700  -11.51800 -31.35600 1.000 77.09000  ? 226 GLU A OE1 1 
ATOM   1322 O OE2 . GLU A 1 180 ? 26.39000  -9.94100  -29.83800 1.000 77.11000  ? 226 GLU A OE2 1 
ATOM   1323 N N   . GLU A 1 181 ? 23.42800  -15.46700 -29.04900 1.000 39.40000  ? 227 GLU A N   1 
ATOM   1324 C CA  . GLU A 1 181 ? 22.23000  -16.00500 -29.67600 1.000 42.67000  ? 227 GLU A CA  1 
ATOM   1325 C C   . GLU A 1 181 ? 21.18400  -16.38300 -28.63800 1.000 52.07000  ? 227 GLU A C   1 
ATOM   1326 O O   . GLU A 1 181 ? 19.98200  -16.32200 -28.92100 1.000 47.86000  ? 227 GLU A O   1 
ATOM   1327 C CB  . GLU A 1 181 ? 22.57900  -17.20700 -30.54300 1.000 38.20000  ? 227 GLU A CB  1 
ATOM   1328 C CG  . GLU A 1 181 ? 21.37300  -17.86600 -31.16000 1.000 44.72000  ? 227 GLU A CG  1 
ATOM   1329 C CD  . GLU A 1 181 ? 20.71700  -17.01300 -32.26800 1.000 53.67000  ? 227 GLU A CD  1 
ATOM   1330 O OE1 . GLU A 1 181 ? 21.32400  -16.01600 -32.71500 1.000 53.48000  ? 227 GLU A OE1 1 
ATOM   1331 O OE2 . GLU A 1 181 ? 19.57000  -17.32800 -32.66100 1.000 53.27000  ? 227 GLU A OE2 1 
ATOM   1332 N N   . LEU A 1 182 ? 21.61700  -16.82000 -27.45300 1.000 48.91000  ? 228 LEU A N   1 
ATOM   1333 C CA  . LEU A 1 182 ? 20.66300  -17.09400 -26.38700 1.000 48.51000  ? 228 LEU A CA  1 
ATOM   1334 C C   . LEU A 1 182 ? 20.01500  -15.81000 -25.89500 1.000 52.58000  ? 228 LEU A C   1 
ATOM   1335 O O   . LEU A 1 182 ? 18.80900  -15.78100 -25.61400 1.000 50.00000  ? 228 LEU A O   1 
ATOM   1336 C CB  . LEU A 1 182 ? 21.36200  -17.84200 -25.24800 1.000 52.31000  ? 228 LEU A CB  1 
ATOM   1337 C CG  . LEU A 1 182 ? 21.71500  -19.29600 -25.59500 1.000 47.59000  ? 228 LEU A CG  1 
ATOM   1338 C CD1 . LEU A 1 182 ? 22.62900  -19.89500 -24.55900 1.000 39.99000  ? 228 LEU A CD1 1 
ATOM   1339 C CD2 . LEU A 1 182 ? 20.45300  -20.15000 -25.75800 1.000 41.20000  ? 228 LEU A CD2 1 
ATOM   1340 N N   . LEU A 1 183 ? 20.80300  -14.73300 -25.81300 1.000 54.54000  ? 229 LEU A N   1 
ATOM   1341 C CA  . LEU A 1 183 ? 20.26200  -13.41700 -25.48900 1.000 55.11000  ? 229 LEU A CA  1 
ATOM   1342 C C   . LEU A 1 183 ? 19.19700  -12.99400 -26.49200 1.000 59.37000  ? 229 LEU A C   1 
ATOM   1343 O O   . LEU A 1 183 ? 18.16000  -12.42800 -26.12000 1.000 63.02000  ? 229 LEU A O   1 
ATOM   1344 C CB  . LEU A 1 183 ? 21.38800  -12.39400 -25.48700 1.000 53.53000  ? 229 LEU A CB  1 
ATOM   1345 C CG  . LEU A 1 183 ? 21.98500  -12.04900 -24.14100 1.000 56.95000  ? 229 LEU A CG  1 
ATOM   1346 C CD1 . LEU A 1 183 ? 23.32800  -11.39200 -24.37200 1.000 55.34000  ? 229 LEU A CD1 1 
ATOM   1347 C CD2 . LEU A 1 183 ? 21.02700  -11.13100 -23.43500 1.000 53.45000  ? 229 LEU A CD2 1 
ATOM   1348 N N   . SER A 1 184 ? 19.44000  -13.24500 -27.77300 1.000 49.19000  ? 230 SER A N   1 
ATOM   1349 C CA  . SER A 1 184 ? 18.43100  -12.91800 -28.76800 1.000 58.70000  ? 230 SER A CA  1 
ATOM   1350 C C   . SER A 1 184 ? 17.15700  -13.70700 -28.51500 1.000 61.89000  ? 230 SER A C   1 
ATOM   1351 O O   . SER A 1 184 ? 16.04800  -13.17300 -28.66200 1.000 65.27000  ? 230 SER A O   1 
ATOM   1352 C CB  . SER A 1 184 ? 18.97500  -13.17200 -30.17600 1.000 50.93000  ? 230 SER A CB  1 
ATOM   1353 O OG  . SER A 1 184 ? 20.13000  -12.36500 -30.40300 1.000 61.59000  ? 230 SER A OG  1 
ATOM   1354 N N   . LEU A 1 185 ? 17.29500  -14.97400 -28.10800 1.000 51.74000  ? 231 LEU A N   1 
ATOM   1355 C CA  . LEU A 1 185 ? 16.11600  -15.81300 -27.90100 1.000 55.96000  ? 231 LEU A CA  1 
ATOM   1356 C C   . LEU A 1 185 ? 15.24900  -15.27900 -26.77400 1.000 52.58000  ? 231 LEU A C   1 
ATOM   1357 O O   . LEU A 1 185 ? 14.02900  -15.15200 -26.92100 1.000 51.51000  ? 231 LEU A O   1 
ATOM   1358 C CB  . LEU A 1 185 ? 16.53800  -17.24800 -27.61700 1.000 52.04000  ? 231 LEU A CB  1 
ATOM   1359 C CG  . LEU A 1 185 ? 15.55000  -18.18400 -26.92100 1.000 53.06000  ? 231 LEU A CG  1 
ATOM   1360 C CD1 . LEU A 1 185 ? 14.30100  -18.40200 -27.74900 1.000 54.16000  ? 231 LEU A CD1 1 
ATOM   1361 C CD2 . LEU A 1 185 ? 16.22800  -19.51300 -26.64100 1.000 41.33000  ? 231 LEU A CD2 1 
ATOM   1362 N N   . VAL A 1 186 ? 15.86800  -14.92000 -25.65000 1.000 54.21000  ? 232 VAL A N   1 
ATOM   1363 C CA  . VAL A 1 186 ? 15.09000  -14.49800 -24.49600 1.000 55.17000  ? 232 VAL A CA  1 
ATOM   1364 C C   . VAL A 1 186 ? 14.49100  -13.12200 -24.70300 1.000 59.53000  ? 232 VAL A C   1 
ATOM   1365 O O   . VAL A 1 186 ? 13.46500  -12.79600 -24.09000 1.000 64.32000  ? 232 VAL A O   1 
ATOM   1366 C CB  . VAL A 1 186 ? 15.94300  -14.53400 -23.21200 1.000 59.02000  ? 232 VAL A CB  1 
ATOM   1367 C CG1 . VAL A 1 186 ? 16.64700  -15.87600 -23.08900 1.000 52.62000  ? 232 VAL A CG1 1 
ATOM   1368 C CG2 . VAL A 1 186 ? 16.94200  -13.40400 -23.19400 1.000 61.48000  ? 232 VAL A CG2 1 
ATOM   1369 N N   . GLN A 1 187 ? 15.09000  -12.30900 -25.56200 1.000 61.65000  ? 233 GLN A N   1 
ATOM   1370 C CA  . GLN A 1 187 ? 14.66900  -10.92000 -25.72600 1.000 67.21000  ? 233 GLN A CA  1 
ATOM   1371 C C   . GLN A 1 187 ? 13.80100  -10.77800 -26.96000 1.000 67.08000  ? 233 GLN A C   1 
ATOM   1372 O O   . GLN A 1 187 ? 13.94200  -9.85100  -27.74900 1.000 80.29000  ? 233 GLN A O   1 
ATOM   1373 C CB  . GLN A 1 187 ? 15.89400  -10.02300 -25.80800 1.000 62.93000  ? 233 GLN A CB  1 
ATOM   1374 C CG  . GLN A 1 187 ? 16.53400  -9.78800  -24.45000 1.000 67.85000  ? 233 GLN A CG  1 
ATOM   1375 C CD  . GLN A 1 187 ? 17.91500  -9.16300  -24.56100 1.000 78.24000  ? 233 GLN A CD  1 
ATOM   1376 O OE1 . GLN A 1 187 ? 18.51100  -9.13200  -25.64600 1.000 69.92000  ? 233 GLN A OE1 1 
ATOM   1377 N NE2 . GLN A 1 187 ? 18.44900  -8.69900  -23.43100 1.000 75.13000  ? 233 GLN A NE2 1 
ATOM   1378 N N   . GLU A 1 188 ? 12.87200  -11.70900 -27.11500 1.000 69.20000  ? 234 GLU A N   1 
ATOM   1379 C CA  . GLU A 1 188 ? 12.00800  -11.76700 -28.27500 1.000 65.59000  ? 234 GLU A CA  1 
ATOM   1380 C C   . GLU A 1 188 ? 10.55500  -11.71500 -27.82500 1.000 70.78000  ? 234 GLU A C   1 
ATOM   1381 O O   . GLU A 1 188 ? 10.24700  -11.79800 -26.63000 1.000 76.93000  ? 234 GLU A O   1 
ATOM   1382 C CB  . GLU A 1 188 ? 12.25200  -13.04800 -29.06900 1.000 61.55000  ? 234 GLU A CB  1 
ATOM   1383 C CG  . GLU A 1 188 ? 13.10500  -12.86900 -30.29800 1.000 67.28000  ? 234 GLU A CG  1 
ATOM   1384 C CD  . GLU A 1 188 ? 13.78600  -14.17800 -30.71400 1.000 78.12000  ? 234 GLU A CD  1 
ATOM   1385 O OE1 . GLU A 1 188 ? 13.21700  -15.26900 -30.41000 1.000 70.70000  ? 234 GLU A OE1 1 
ATOM   1386 O OE2 . GLU A 1 188 ? 14.89500  -14.11500 -31.31100 1.000 72.53000  ? 234 GLU A OE2 1 
ATOM   1387 N N   . ALA A 1 189 ? 9.67100   -11.60000 -28.81800 1.000 83.15000  ? 235 ALA A N   1 
ATOM   1388 C CA  . ALA A 1 189 ? 8.20800   -11.61000 -28.65800 1.000 87.90000  ? 235 ALA A CA  1 
ATOM   1389 C C   . ALA A 1 189 ? 7.70400   -12.70800 -27.70700 1.000 76.42000  ? 235 ALA A C   1 
ATOM   1390 O O   . ALA A 1 189 ? 7.41300   -12.45300 -26.53000 1.000 72.28000  ? 235 ALA A O   1 
ATOM   1391 C CB  . ALA A 1 189 ? 7.52900   -11.76200 -30.05300 1.000 70.55000  ? 235 ALA A CB  1 
ATOM   1392 N N   . ALA B 1 3   ? 27.34700  -39.04100 -5.51700  1.000 69.11000  ? 52  ALA B N   1 
ATOM   1393 C CA  . ALA B 1 3   ? 25.98000  -39.50200 -5.75300  1.000 79.39000  ? 52  ALA B CA  1 
ATOM   1394 C C   . ALA B 1 3   ? 25.43400  -40.27800 -4.53900  1.000 82.88000  ? 52  ALA B C   1 
ATOM   1395 O O   . ALA B 1 3   ? 25.86000  -41.40900 -4.27800  1.000 85.62000  ? 52  ALA B O   1 
ATOM   1396 C CB  . ALA B 1 3   ? 25.92700  -40.37200 -7.02500  1.000 74.36000  ? 52  ALA B CB  1 
ATOM   1397 N N   . ASP B 1 4   ? 24.49800  -39.69800 -3.78500  1.000 73.32000  ? 53  ASP B N   1 
ATOM   1398 C CA  . ASP B 1 4   ? 23.99200  -40.37900 -2.59800  1.000 85.62000  ? 53  ASP B CA  1 
ATOM   1399 C C   . ASP B 1 4   ? 22.69800  -41.14200 -2.87000  1.000 82.46000  ? 53  ASP B C   1 
ATOM   1400 O O   . ASP B 1 4   ? 21.77500  -40.63600 -3.53000  1.000 68.00000  ? 53  ASP B O   1 
ATOM   1401 C CB  . ASP B 1 4   ? 23.77600  -39.41700 -1.43500  1.000 89.68000  ? 53  ASP B CB  1 
ATOM   1402 C CG  . ASP B 1 4   ? 24.24400  -40.01400 -0.11300  1.000 103.14000 ? 53  ASP B CG  1 
ATOM   1403 O OD1 . ASP B 1 4   ? 24.69200  -41.19300 -0.11100  1.000 93.38000  ? 53  ASP B OD1 1 
ATOM   1404 O OD2 . ASP B 1 4   ? 24.18000  -39.30500 0.91600   1.000 110.33000 ? 53  ASP B OD2 1 
ATOM   1405 N N   . ARG B 1 5   ? 22.64500  -42.36800 -2.34600  1.000 67.47000  ? 54  ARG B N   1 
ATOM   1406 C CA  . ARG B 1 5   ? 21.52000  -43.26600 -2.53400  1.000 59.16000  ? 54  ARG B CA  1 
ATOM   1407 C C   . ARG B 1 5   ? 20.73800  -43.35100 -1.22800  1.000 56.53000  ? 54  ARG B C   1 
ATOM   1408 O O   . ARG B 1 5   ? 21.32900  -43.49800 -0.15000  1.000 54.03000  ? 54  ARG B O   1 
ATOM   1409 C CB  . ARG B 1 5   ? 22.03100  -44.64200 -2.96600  1.000 52.01000  ? 54  ARG B CB  1 
ATOM   1410 C CG  . ARG B 1 5   ? 20.98000  -45.70200 -3.13300  1.000 55.49000  ? 54  ARG B CG  1 
ATOM   1411 C CD  . ARG B 1 5   ? 21.59600  -47.05100 -3.52400  1.000 56.42000  ? 54  ARG B CD  1 
ATOM   1412 N NE  . ARG B 1 5   ? 21.78500  -47.91900 -2.36600  1.000 60.20000  ? 54  ARG B NE  1 
ATOM   1413 C CZ  . ARG B 1 5   ? 21.24400  -49.12300 -2.24500  1.000 55.35000  ? 54  ARG B CZ  1 
ATOM   1414 N NH1 . ARG B 1 5   ? 20.48700  -49.63600 -3.20300  1.000 52.78000  ? 54  ARG B NH1 1 
ATOM   1415 N NH2 . ARG B 1 5   ? 21.49200  -49.84200 -1.15000  1.000 59.14000  ? 54  ARG B NH2 1 
ATOM   1416 N N   . PHE B 1 6   ? 19.40700  -43.28300 -1.32800  1.000 48.99000  ? 55  PHE B N   1 
ATOM   1417 C CA  . PHE B 1 6   ? 18.55600  -43.30700 -0.14500  1.000 50.51000  ? 55  PHE B CA  1 
ATOM   1418 C C   . PHE B 1 6   ? 17.21000  -43.92500 -0.48500  1.000 46.84000  ? 55  PHE B C   1 
ATOM   1419 O O   . PHE B 1 6   ? 16.75200  -43.88200 -1.62600  1.000 51.74000  ? 55  PHE B O   1 
ATOM   1420 C CB  . PHE B 1 6   ? 18.36200  -41.90000 0.44800   1.000 42.01000  ? 55  PHE B CB  1 
ATOM   1421 C CG  . PHE B 1 6   ? 17.52800  -40.98800 -0.40200  1.000 50.52000  ? 55  PHE B CG  1 
ATOM   1422 C CD1 . PHE B 1 6   ? 18.08200  -40.33800 -1.50500  1.000 48.97000  ? 55  PHE B CD1 1 
ATOM   1423 C CD2 . PHE B 1 6   ? 16.18900  -40.76700 -0.09900  1.000 44.97000  ? 55  PHE B CD2 1 
ATOM   1424 C CE1 . PHE B 1 6   ? 17.30900  -39.48600 -2.29700  1.000 42.38000  ? 55  PHE B CE1 1 
ATOM   1425 C CE2 . PHE B 1 6   ? 15.41400  -39.92700 -0.88100  1.000 45.11000  ? 55  PHE B CE2 1 
ATOM   1426 C CZ  . PHE B 1 6   ? 15.97500  -39.28600 -1.99000  1.000 42.11000  ? 55  PHE B CZ  1 
ATOM   1427 N N   . ALA B 1 7   ? 16.54500  -44.43600 0.54300   1.000 53.88000  ? 56  ALA B N   1 
ATOM   1428 C CA  . ALA B 1 7   ? 15.33500  -45.22200 0.37800   1.000 48.89000  ? 56  ALA B CA  1 
ATOM   1429 C C   . ALA B 1 7   ? 14.10900  -44.44600 0.84000   1.000 50.09000  ? 56  ALA B C   1 
ATOM   1430 O O   . ALA B 1 7   ? 14.16700  -43.63500 1.76800   1.000 47.96000  ? 56  ALA B O   1 
ATOM   1431 C CB  . ALA B 1 7   ? 15.42200  -46.53500 1.15800   1.000 49.84000  ? 56  ALA B CB  1 
ATOM   1432 N N   . VAL B 1 8   ? 13.00200  -44.69700 0.15600   1.000 45.20000  ? 57  VAL B N   1 
ATOM   1433 C CA  . VAL B 1 8   ? 11.70000  -44.16500 0.50000   1.000 39.95000  ? 57  VAL B CA  1 
ATOM   1434 C C   . VAL B 1 8   ? 10.72900  -45.33000 0.46800   1.000 51.73000  ? 57  VAL B C   1 
ATOM   1435 O O   . VAL B 1 8   ? 11.02200  -46.40200 -0.07500  1.000 52.13000  ? 57  VAL B O   1 
ATOM   1436 C CB  . VAL B 1 8   ? 11.23100  -43.05900 -0.46600  1.000 43.10000  ? 57  VAL B CB  1 
ATOM   1437 C CG1 . VAL B 1 8   ? 12.11200  -41.84600 -0.33000  1.000 36.10000  ? 57  VAL B CG1 1 
ATOM   1438 C CG2 . VAL B 1 8   ? 11.19600  -43.57300 -1.94900  1.000 40.72000  ? 57  VAL B CG2 1 
ATOM   1439 N N   . SER B 1 9   ? 9.55800   -45.09900 1.04400   1.000 49.91000  ? 58  SER B N   1 
ATOM   1440 C CA  . SER B 1 9   ? 8.50900   -46.10300 1.00600   1.000 54.12000  ? 58  SER B CA  1 
ATOM   1441 C C   . SER B 1 9   ? 8.11200   -46.45200 -0.43100  1.000 51.75000  ? 58  SER B C   1 
ATOM   1442 O O   . SER B 1 9   ? 7.97200   -45.57800 -1.29000  1.000 56.64000  ? 58  SER B O   1 
ATOM   1443 C CB  . SER B 1 9   ? 7.29000   -45.60900 1.77100   1.000 49.30000  ? 58  SER B CB  1 
ATOM   1444 O OG  . SER B 1 9   ? 6.15200   -46.32900 1.33500   1.000 59.06000  ? 58  SER B OG  1 
ATOM   1445 N N   . ALA B 1 10  ? 7.92000   -47.74900 -0.68300  1.000 50.17000  ? 59  ALA B N   1 
ATOM   1446 C CA  . ALA B 1 10  ? 7.52000   -48.19800 -2.01500  1.000 50.40000  ? 59  ALA B CA  1 
ATOM   1447 C C   . ALA B 1 10  ? 6.22000   -47.55000 -2.47400  1.000 59.62000  ? 59  ALA B C   1 
ATOM   1448 O O   . ALA B 1 10  ? 6.02800   -47.34100 -3.67900  1.000 53.55000  ? 59  ALA B O   1 
ATOM   1449 C CB  . ALA B 1 10  ? 7.36300   -49.71800 -2.04900  1.000 38.75000  ? 59  ALA B CB  1 
ATOM   1450 N N   . GLU B 1 11  ? 5.32000   -47.19900 -1.55200  1.000 60.01000  ? 60  GLU B N   1 
ATOM   1451 C CA  . GLU B 1 11  ? 4.05100   -46.69300 -2.06200  1.000 64.43000  ? 60  GLU B CA  1 
ATOM   1452 C C   . GLU B 1 11  ? 4.14600   -45.24500 -2.53700  1.000 63.43000  ? 60  GLU B C   1 
ATOM   1453 O O   . GLU B 1 11  ? 3.14700   -44.69100 -3.01700  1.000 60.98000  ? 60  GLU B O   1 
ATOM   1454 C CB  . GLU B 1 11  ? 2.94800   -46.83200 -1.01500  1.000 56.44000  ? 60  GLU B CB  1 
ATOM   1455 C CG  . GLU B 1 11  ? 3.27800   -46.27700 0.33700   1.000 75.51000  ? 60  GLU B CG  1 
ATOM   1456 C CD  . GLU B 1 11  ? 2.38400   -46.85200 1.43100   1.000 97.81000  ? 60  GLU B CD  1 
ATOM   1457 O OE1 . GLU B 1 11  ? 1.89400   -47.99700 1.25700   1.000 91.03000  ? 60  GLU B OE1 1 
ATOM   1458 O OE2 . GLU B 1 11  ? 2.18300   -46.16400 2.46400   1.000 96.74000  ? 60  GLU B OE2 1 
ATOM   1459 N N   . ALA B 1 12  ? 5.32500   -44.63400 -2.45400  1.000 61.11000  ? 61  ALA B N   1 
ATOM   1460 C CA  . ALA B 1 12  ? 5.53400   -43.28000 -2.93400  1.000 53.57000  ? 61  ALA B CA  1 
ATOM   1461 C C   . ALA B 1 12  ? 6.13700   -43.23500 -4.32600  1.000 50.86000  ? 61  ALA B C   1 
ATOM   1462 O O   . ALA B 1 12  ? 6.40700   -42.14000 -4.82900  1.000 59.39000  ? 61  ALA B O   1 
ATOM   1463 C CB  . ALA B 1 12  ? 6.42600   -42.50700 -1.94800  1.000 55.13000  ? 61  ALA B CB  1 
ATOM   1464 N N   . GLU B 1 13  ? 6.36300   -44.39300 -4.95800  1.000 58.33000  ? 62  GLU B N   1 
ATOM   1465 C CA  . GLU B 1 13  ? 6.99900   -44.40800 -6.27300  1.000 51.32000  ? 62  GLU B CA  1 
ATOM   1466 C C   . GLU B 1 13  ? 6.26300   -43.51200 -7.26100  1.000 61.88000  ? 62  GLU B C   1 
ATOM   1467 O O   . GLU B 1 13  ? 6.89600   -42.79800 -8.05100  1.000 58.45000  ? 62  GLU B O   1 
ATOM   1468 C CB  . GLU B 1 13  ? 7.09700   -45.83600 -6.82600  1.000 54.28000  ? 62  GLU B CB  1 
ATOM   1469 C CG  . GLU B 1 13  ? 7.97000   -45.90400 -8.09400  1.000 55.44000  ? 62  GLU B CG  1 
ATOM   1470 C CD  . GLU B 1 13  ? 8.01500   -47.27200 -8.79200  1.000 67.65000  ? 62  GLU B CD  1 
ATOM   1471 O OE1 . GLU B 1 13  ? 7.78900   -48.31300 -8.12000  1.000 59.76000  ? 62  GLU B OE1 1 
ATOM   1472 O OE2 . GLU B 1 13  ? 8.29600   -47.28800 -10.02800 1.000 67.08000  ? 62  GLU B OE2 1 
ATOM   1473 N N   . ASN B 1 14  ? 4.92600   -43.52500 -7.21900  1.000 62.76000  ? 63  ASN B N   1 
ATOM   1474 C CA  . ASN B 1 14  ? 4.14100   -42.70600 -8.13900  1.000 58.04000  ? 63  ASN B CA  1 
ATOM   1475 C C   . ASN B 1 14  ? 4.45300   -41.23100 -7.95800  1.000 59.31000  ? 63  ASN B C   1 
ATOM   1476 O O   . ASN B 1 14  ? 4.83000   -40.54100 -8.91800  1.000 63.28000  ? 63  ASN B O   1 
ATOM   1477 C CB  . ASN B 1 14  ? 2.65200   -42.96200 -7.93600  1.000 78.43000  ? 63  ASN B CB  1 
ATOM   1478 C CG  . ASN B 1 14  ? 2.13700   -44.05400 -8.84300  1.000 85.38000  ? 63  ASN B CG  1 
ATOM   1479 O OD1 . ASN B 1 14  ? 2.84500   -44.49200 -9.75700  1.000 81.52000  ? 63  ASN B OD1 1 
ATOM   1480 N ND2 . ASN B 1 14  ? 0.90700   -44.51800 -8.59000  1.000 83.69000  ? 63  ASN B ND2 1 
ATOM   1481 N N   . LYS B 1 15  ? 4.28400   -40.72600 -6.72600  1.000 58.38000  ? 64  LYS B N   1 
ATOM   1482 C CA  . LYS B 1 15  ? 4.59800   -39.32800 -6.45400  1.000 56.07000  ? 64  LYS B CA  1 
ATOM   1483 C C   . LYS B 1 15  ? 5.99100   -38.99300 -6.97900  1.000 58.86000  ? 64  LYS B C   1 
ATOM   1484 O O   . LYS B 1 15  ? 6.18400   -37.97900 -7.65800  1.000 59.09000  ? 64  LYS B O   1 
ATOM   1485 C CB  . LYS B 1 15  ? 4.51200   -39.02600 -4.95100  1.000 53.33000  ? 64  LYS B CB  1 
ATOM   1486 C CG  . LYS B 1 15  ? 3.21300   -38.35600 -4.42800  1.000 71.64000  ? 64  LYS B CG  1 
ATOM   1487 C CD  . LYS B 1 15  ? 2.59500   -39.13000 -3.21700  1.000 79.13000  ? 64  LYS B CD  1 
ATOM   1488 C CE  . LYS B 1 15  ? 1.54700   -38.31900 -2.39800  1.000 87.66000  ? 64  LYS B CE  1 
ATOM   1489 N NZ  . LYS B 1 15  ? 0.27100   -37.90900 -3.11100  1.000 77.89000  ? 64  LYS B NZ  1 
ATOM   1490 N N   . VAL B 1 16  ? 6.96300   -39.87200 -6.73700  1.000 57.54000  ? 65  VAL B N   1 
ATOM   1491 C CA  . VAL B 1 16  ? 8.32700   -39.56700 -7.14900  1.000 57.07000  ? 65  VAL B CA  1 
ATOM   1492 C C   . VAL B 1 16  ? 8.40700   -39.44300 -8.66000  1.000 55.49000  ? 65  VAL B C   1 
ATOM   1493 O O   . VAL B 1 16  ? 8.87400   -38.42600 -9.18800  1.000 49.76000  ? 65  VAL B O   1 
ATOM   1494 C CB  . VAL B 1 16  ? 9.31000   -40.62000 -6.61400  1.000 53.25000  ? 65  VAL B CB  1 
ATOM   1495 C CG1 . VAL B 1 16  ? 10.70800  -40.32100 -7.11800  1.000 44.91000  ? 65  VAL B CG1 1 
ATOM   1496 C CG2 . VAL B 1 16  ? 9.31100   -40.59500 -5.11700  1.000 44.68000  ? 65  VAL B CG2 1 
ATOM   1497 N N   . ARG B 1 17  ? 7.93300   -40.46400 -9.38100  1.000 59.12000  ? 66  ARG B N   1 
ATOM   1498 C CA  . ARG B 1 17  ? 8.04400   -40.41900 -10.83500 1.000 56.75000  ? 66  ARG B CA  1 
ATOM   1499 C C   . ARG B 1 17  ? 7.26600   -39.24300 -11.39200 1.000 64.05000  ? 66  ARG B C   1 
ATOM   1500 O O   . ARG B 1 17  ? 7.69100   -38.62600 -12.37700 1.000 59.73000  ? 66  ARG B O   1 
ATOM   1501 C CB  . ARG B 1 17  ? 7.57400   -41.72700 -11.47300 1.000 53.20000  ? 66  ARG B CB  1 
ATOM   1502 C CG  . ARG B 1 17  ? 8.59300   -42.86100 -11.34500 1.000 58.15000  ? 66  ARG B CG  1 
ATOM   1503 C CD  . ARG B 1 17  ? 8.04900   -44.23400 -11.79100 1.000 60.44000  ? 66  ARG B CD  1 
ATOM   1504 N NE  . ARG B 1 17  ? 9.01900   -45.33400 -11.76000 1.000 58.44000  ? 66  ARG B NE  1 
ATOM   1505 C CZ  . ARG B 1 17  ? 10.22900  -45.32900 -12.31300 1.000 64.47000  ? 66  ARG B CZ  1 
ATOM   1506 N NH1 . ARG B 1 17  ? 10.68600  -44.28700 -12.99800 1.000 61.96000  ? 66  ARG B NH1 1 
ATOM   1507 N NH2 . ARG B 1 17  ? 11.00800  -46.39500 -12.16600 1.000 65.60000  ? 66  ARG B NH2 1 
ATOM   1508 N N   . GLU B 1 18  ? 6.15400   -38.88700 -10.74500 1.000 57.53000  ? 67  GLU B N   1 
ATOM   1509 C CA  . GLU B 1 18  ? 5.38500   -37.73800 -11.20200 1.000 54.32000  ? 67  GLU B CA  1 
ATOM   1510 C C   . GLU B 1 18  ? 6.17400   -36.43700 -11.03700 1.000 61.32000  ? 67  GLU B C   1 
ATOM   1511 O O   . GLU B 1 18  ? 6.26200   -35.63100 -11.97000 1.000 60.50000  ? 67  GLU B O   1 
ATOM   1512 C CB  . GLU B 1 18  ? 4.06800   -37.66600 -10.43300 1.000 61.76000  ? 67  GLU B CB  1 
ATOM   1513 C CG  . GLU B 1 18  ? 3.52900   -36.25300 -10.32900 1.000 73.86000  ? 67  GLU B CG  1 
ATOM   1514 C CD  . GLU B 1 18  ? 2.02600   -36.21600 -10.20700 1.000 86.81000  ? 67  GLU B CD  1 
ATOM   1515 O OE1 . GLU B 1 18  ? 1.35600   -36.41400 -11.24800 1.000 85.44000  ? 67  GLU B OE1 1 
ATOM   1516 O OE2 . GLU B 1 18  ? 1.51900   -35.96900 -9.08400  1.000 88.50000  ? 67  GLU B OE2 1 
ATOM   1517 N N   . GLN B 1 19  ? 6.79200   -36.23500 -9.86800  1.000 68.35000  ? 68  GLN B N   1 
ATOM   1518 C CA  . GLN B 1 19  ? 7.51800   -35.00500 -9.55800  1.000 61.71000  ? 68  GLN B CA  1 
ATOM   1519 C C   . GLN B 1 19  ? 8.97000   -35.00300 -10.03000 1.000 54.63000  ? 68  GLN B C   1 
ATOM   1520 O O   . GLN B 1 19  ? 9.64400   -33.97500 -9.90200  1.000 55.68000  ? 68  GLN B O   1 
ATOM   1521 C CB  . GLN B 1 19  ? 7.48300   -34.75300 -8.04900  1.000 56.64000  ? 68  GLN B CB  1 
ATOM   1522 C CG  . GLN B 1 19  ? 6.11500   -34.47100 -7.51500  1.000 53.71000  ? 68  GLN B CG  1 
ATOM   1523 C CD  . GLN B 1 19  ? 5.60800   -33.14300 -8.00700  1.000 66.76000  ? 68  GLN B CD  1 
ATOM   1524 O OE1 . GLN B 1 19  ? 6.35300   -32.16300 -8.03900  1.000 72.60000  ? 68  GLN B OE1 1 
ATOM   1525 N NE2 . GLN B 1 19  ? 4.34100   -33.09900 -8.41400  1.000 64.65000  ? 68  GLN B NE2 1 
ATOM   1526 N N   . GLN B 1 20  ? 9.46100   -36.11300 -10.57400 1.000 53.15000  ? 69  GLN B N   1 
ATOM   1527 C CA  . GLN B 1 20  ? 10.86400  -36.21400 -10.97100 1.000 53.59000  ? 69  GLN B CA  1 
ATOM   1528 C C   . GLN B 1 20  ? 11.33200  -35.08100 -11.87500 1.000 50.53000  ? 69  GLN B C   1 
ATOM   1529 O O   . GLN B 1 20  ? 12.35700  -34.45700 -11.55000 1.000 45.64000  ? 69  GLN B O   1 
ATOM   1530 C CB  . GLN B 1 20  ? 11.08500  -37.61200 -11.55800 1.000 58.15000  ? 69  GLN B CB  1 
ATOM   1531 C CG  . GLN B 1 20  ? 12.14400  -37.70700 -12.58800 1.000 63.09000  ? 69  GLN B CG  1 
ATOM   1532 C CD  . GLN B 1 20  ? 12.57000  -39.14200 -12.80700 1.000 72.37000  ? 69  GLN B CD  1 
ATOM   1533 O OE1 . GLN B 1 20  ? 13.74600  -39.41100 -12.99900 1.000 84.87000  ? 69  GLN B OE1 1 
ATOM   1534 N NE2 . GLN B 1 20  ? 11.62600  -40.07900 -12.70000 1.000 64.71000  ? 69  GLN B NE2 1 
ATOM   1535 N N   . PRO B 1 21  ? 10.65100  -34.75000 -12.98500 1.000 54.89000  ? 70  PRO B N   1 
ATOM   1536 C CA  . PRO B 1 21  ? 11.08800  -33.59200 -13.79200 1.000 49.21000  ? 70  PRO B CA  1 
ATOM   1537 C C   . PRO B 1 21  ? 11.15000  -32.27000 -13.03500 1.000 50.36000  ? 70  PRO B C   1 
ATOM   1538 O O   . PRO B 1 21  ? 12.06600  -31.47200 -13.28300 1.000 50.86000  ? 70  PRO B O   1 
ATOM   1539 C CB  . PRO B 1 21  ? 10.02900  -33.53500 -14.90900 1.000 52.60000  ? 70  PRO B CB  1 
ATOM   1540 C CG  . PRO B 1 21  ? 8.89100   -34.35700 -14.43000 1.000 46.44000  ? 70  PRO B CG  1 
ATOM   1541 C CD  . PRO B 1 21  ? 9.52800   -35.44800 -13.63400 1.000 50.97000  ? 70  PRO B CD  1 
ATOM   1542 N N   . HIS B 1 22  ? 10.20900  -32.00500 -12.11800 1.000 50.30000  ? 71  HIS B N   1 
ATOM   1543 C CA  . HIS B 1 22  ? 10.19900  -30.72200 -11.41600 1.000 48.91000  ? 71  HIS B CA  1 
ATOM   1544 C C   . HIS B 1 22  ? 11.29400  -30.64100 -10.35500 1.000 50.91000  ? 71  HIS B C   1 
ATOM   1545 O O   . HIS B 1 22  ? 11.82100  -29.55600 -10.09200 1.000 51.40000  ? 71  HIS B O   1 
ATOM   1546 C CB  . HIS B 1 22  ? 8.82900   -30.47100 -10.78700 1.000 59.57000  ? 71  HIS B CB  1 
ATOM   1547 C CG  . HIS B 1 22  ? 7.68900   -30.78500 -11.70700 1.000 77.36000  ? 71  HIS B CG  1 
ATOM   1548 N ND1 . HIS B 1 22  ? 7.29900   -29.93800 -12.72500 1.000 69.70000  ? 71  HIS B ND1 1 
ATOM   1549 C CD2 . HIS B 1 22  ? 6.88300   -31.87500 -11.79200 1.000 71.17000  ? 71  HIS B CD2 1 
ATOM   1550 C CE1 . HIS B 1 22  ? 6.28700   -30.48500 -13.38100 1.000 72.70000  ? 71  HIS B CE1 1 
ATOM   1551 N NE2 . HIS B 1 22  ? 6.01600   -31.65900 -12.83600 1.000 63.44000  ? 71  HIS B NE2 1 
ATOM   1552 N N   . VAL B 1 23  ? 11.64600  -31.76700 -9.73700  1.000 45.54000  ? 72  VAL B N   1 
ATOM   1553 C CA  . VAL B 1 23  ? 12.78500  -31.79100 -8.82300  1.000 47.75000  ? 72  VAL B CA  1 
ATOM   1554 C C   . VAL B 1 23  ? 14.07600  -31.53500 -9.58500  1.000 45.12000  ? 72  VAL B C   1 
ATOM   1555 O O   . VAL B 1 23  ? 14.93900  -30.76300 -9.14000  1.000 38.96000  ? 72  VAL B O   1 
ATOM   1556 C CB  . VAL B 1 23  ? 12.81300  -33.13500 -8.07100  1.000 48.88000  ? 72  VAL B CB  1 
ATOM   1557 C CG1 . VAL B 1 23  ? 14.12100  -33.32500 -7.27400  1.000 38.16000  ? 72  VAL B CG1 1 
ATOM   1558 C CG2 . VAL B 1 23  ? 11.58700  -33.22900 -7.19100  1.000 42.38000  ? 72  VAL B CG2 1 
ATOM   1559 N N   . GLU B 1 24  ? 14.22000  -32.16400 -10.75500 1.000 48.33000  ? 73  GLU B N   1 
ATOM   1560 C CA  . GLU B 1 24  ? 15.41500  -31.95700 -11.55700 1.000 43.25000  ? 73  GLU B CA  1 
ATOM   1561 C C   . GLU B 1 24  ? 15.53400  -30.50600 -11.97900 1.000 46.64000  ? 73  GLU B C   1 
ATOM   1562 O O   . GLU B 1 24  ? 16.62800  -29.93100 -11.93900 1.000 49.68000  ? 73  GLU B O   1 
ATOM   1563 C CB  . GLU B 1 24  ? 15.40100  -32.88800 -12.76800 1.000 40.71000  ? 73  GLU B CB  1 
ATOM   1564 C CG  . GLU B 1 24  ? 15.71400  -34.34000 -12.39400 1.000 55.68000  ? 73  GLU B CG  1 
ATOM   1565 C CD  . GLU B 1 24  ? 15.69200  -35.29400 -13.57600 1.000 66.89000  ? 73  GLU B CD  1 
ATOM   1566 O OE1 . GLU B 1 24  ? 15.17700  -34.88500 -14.65200 1.000 70.63000  ? 73  GLU B OE1 1 
ATOM   1567 O OE2 . GLU B 1 24  ? 16.18400  -36.44700 -13.41500 1.000 63.96000  ? 73  GLU B OE2 1 
ATOM   1568 N N   . ARG B 1 25  ? 14.41300  -29.87100 -12.32100 1.000 44.01000  ? 74  ARG B N   1 
ATOM   1569 C CA  . ARG B 1 25  ? 14.47500  -28.48000 -12.75500 1.000 43.91000  ? 74  ARG B CA  1 
ATOM   1570 C C   . ARG B 1 25  ? 14.79100  -27.54600 -11.59100 1.000 46.94000  ? 74  ARG B C   1 
ATOM   1571 O O   . ARG B 1 25  ? 15.69700  -26.70900 -11.68500 1.000 50.08000  ? 74  ARG B O   1 
ATOM   1572 C CB  . ARG B 1 25  ? 13.15200  -28.09000 -13.41400 1.000 48.32000  ? 74  ARG B CB  1 
ATOM   1573 C CG  . ARG B 1 25  ? 13.19000  -26.78700 -14.17600 1.000 45.26000  ? 74  ARG B CG  1 
ATOM   1574 C CD  . ARG B 1 25  ? 11.88600  -26.60500 -14.93800 1.000 53.34000  ? 74  ARG B CD  1 
ATOM   1575 N NE  . ARG B 1 25  ? 10.78100  -26.56200 -13.99300 1.000 53.76000  ? 74  ARG B NE  1 
ATOM   1576 C CZ  . ARG B 1 25  ? 10.55700  -25.53700 -13.18700 1.000 52.60000  ? 74  ARG B CZ  1 
ATOM   1577 N NH1 . ARG B 1 25  ? 11.30200  -24.44200 -13.25000 1.000 49.77000  ? 74  ARG B NH1 1 
ATOM   1578 N NH2 . ARG B 1 25  ? 9.58600   -25.62500 -12.27700 1.000 49.15000  ? 74  ARG B NH2 1 
ATOM   1579 N N   . ILE B 1 26  ? 14.07300  -27.69600 -10.47000 1.000 46.33000  ? 75  ILE B N   1 
ATOM   1580 C CA  . ILE B 1 26  ? 14.20500  -26.75500 -9.35500  1.000 46.36000  ? 75  ILE B CA  1 
ATOM   1581 C C   . ILE B 1 26  ? 15.55800  -26.88900 -8.66400  1.000 48.32000  ? 75  ILE B C   1 
ATOM   1582 O O   . ILE B 1 26  ? 16.13800  -25.88400 -8.22100  1.000 41.77000  ? 75  ILE B O   1 
ATOM   1583 C CB  . ILE B 1 26  ? 13.04000  -26.93700 -8.36000  1.000 45.81000  ? 75  ILE B CB  1 
ATOM   1584 C CG1 . ILE B 1 26  ? 11.69400  -26.62800 -9.02100  1.000 49.53000  ? 75  ILE B CG1 1 
ATOM   1585 C CG2 . ILE B 1 26  ? 13.30000  -26.22100 -7.02300  1.000 45.42000  ? 75  ILE B CG2 1 
ATOM   1586 C CD1 . ILE B 1 26  ? 10.51800  -27.15200 -8.22400  1.000 54.24000  ? 75  ILE B CD1 1 
ATOM   1587 N N   . PHE B 1 27  ? 16.05600  -28.12100 -8.49000  1.000 41.85000  ? 76  PHE B N   1 
ATOM   1588 C CA  . PHE B 1 27  ? 17.29500  -28.31700 -7.74200  1.000 45.10000  ? 76  PHE B CA  1 
ATOM   1589 C C   . PHE B 1 27  ? 18.50100  -28.62000 -8.62900  1.000 48.35000  ? 76  PHE B C   1 
ATOM   1590 O O   . PHE B 1 27  ? 19.60500  -28.80100 -8.10100  1.000 44.85000  ? 76  PHE B O   1 
ATOM   1591 C CB  . PHE B 1 27  ? 17.10900  -29.42000 -6.68400  1.000 42.87000  ? 76  PHE B CB  1 
ATOM   1592 C CG  . PHE B 1 27  ? 16.05100  -29.09200 -5.64300  1.000 44.03000  ? 76  PHE B CG  1 
ATOM   1593 C CD1 . PHE B 1 27  ? 16.38700  -28.38700 -4.47600  1.000 44.48000  ? 76  PHE B CD1 1 
ATOM   1594 C CD2 . PHE B 1 27  ? 14.71500  -29.46800 -5.84200  1.000 38.70000  ? 76  PHE B CD2 1 
ATOM   1595 C CE1 . PHE B 1 27  ? 15.41200  -28.08800 -3.50000  1.000 43.45000  ? 76  PHE B CE1 1 
ATOM   1596 C CE2 . PHE B 1 27  ? 13.72600  -29.17200 -4.88800  1.000 42.39000  ? 76  PHE B CE2 1 
ATOM   1597 C CZ  . PHE B 1 27  ? 14.06600  -28.48200 -3.71800  1.000 45.84000  ? 76  PHE B CZ  1 
ATOM   1598 N N   . SER B 1 28  ? 18.32100  -28.65500 -9.95100  1.000 40.54000  ? 77  SER B N   1 
ATOM   1599 C CA  . SER B 1 28  ? 19.36500  -29.00600 -10.92600 1.000 47.60000  ? 77  SER B CA  1 
ATOM   1600 C C   . SER B 1 28  ? 20.20200  -30.19300 -10.45100 1.000 40.41000  ? 77  SER B C   1 
ATOM   1601 O O   . SER B 1 28  ? 21.41700  -30.11700 -10.27800 1.000 46.89000  ? 77  SER B O   1 
ATOM   1602 C CB  . SER B 1 28  ? 20.25600  -27.81700 -11.30600 1.000 41.18000  ? 77  SER B CB  1 
ATOM   1603 O OG  . SER B 1 28  ? 20.45600  -26.92900 -10.23300 1.000 54.53000  ? 77  SER B OG  1 
ATOM   1604 N N   . VAL B 1 29  ? 19.50600  -31.30000 -10.21400 1.000 37.96000  ? 78  VAL B N   1 
ATOM   1605 C CA  . VAL B 1 29  ? 20.13100  -32.58300 -9.94400  1.000 48.18000  ? 78  VAL B CA  1 
ATOM   1606 C C   . VAL B 1 29  ? 19.54700  -33.57100 -10.93300 1.000 45.95000  ? 78  VAL B C   1 
ATOM   1607 O O   . VAL B 1 29  ? 18.60200  -33.26900 -11.65200 1.000 47.90000  ? 78  VAL B O   1 
ATOM   1608 C CB  . VAL B 1 29  ? 19.90400  -33.07600 -8.49800  1.000 46.48000  ? 78  VAL B CB  1 
ATOM   1609 C CG1 . VAL B 1 29  ? 20.43200  -32.05300 -7.49700  1.000 42.56000  ? 78  VAL B CG1 1 
ATOM   1610 C CG2 . VAL B 1 29  ? 18.43100  -33.35000 -8.27400  1.000 40.15000  ? 78  VAL B CG2 1 
ATOM   1611 N N   . GLY B 1 30  ? 20.08400  -34.78400 -10.93000 1.000 47.67000  ? 79  GLY B N   1 
ATOM   1612 C CA  . GLY B 1 30  ? 19.44200  -35.89400 -11.59800 1.000 44.53000  ? 79  GLY B CA  1 
ATOM   1613 C C   . GLY B 1 30  ? 18.78000  -36.76600 -10.55400 1.000 53.76000  ? 79  GLY B C   1 
ATOM   1614 O O   . GLY B 1 30  ? 19.37000  -37.07900 -9.51500  1.000 55.55000  ? 79  GLY B O   1 
ATOM   1615 N N   . VAL B 1 31  ? 17.53700  -37.14200 -10.82700 1.000 50.65000  ? 80  VAL B N   1 
ATOM   1616 C CA  . VAL B 1 31  ? 16.79400  -38.04800 -9.96500  1.000 56.71000  ? 80  VAL B CA  1 
ATOM   1617 C C   . VAL B 1 31  ? 16.55600  -39.31100 -10.75500 1.000 58.12000  ? 80  VAL B C   1 
ATOM   1618 O O   . VAL B 1 31  ? 15.97900  -39.25600 -11.84100 1.000 62.44000  ? 80  VAL B O   1 
ATOM   1619 C CB  . VAL B 1 31  ? 15.44900  -37.46300 -9.52200  1.000 54.00000  ? 80  VAL B CB  1 
ATOM   1620 C CG1 . VAL B 1 31  ? 14.82500  -38.36000 -8.50600  1.000 45.44000  ? 80  VAL B CG1 1 
ATOM   1621 C CG2 . VAL B 1 31  ? 15.62300  -36.06700 -9.00800  1.000 53.08000  ? 80  VAL B CG2 1 
ATOM   1622 N N   . SER B 1 32  ? 16.98400  -40.44100 -10.21800 1.000 55.79000  ? 81  SER B N   1 
ATOM   1623 C CA  . SER B 1 32  ? 16.68200  -41.71900 -10.82700 1.000 54.97000  ? 81  SER B CA  1 
ATOM   1624 C C   . SER B 1 32  ? 16.04000  -42.60900 -9.78100  1.000 57.83000  ? 81  SER B C   1 
ATOM   1625 O O   . SER B 1 32  ? 16.42100  -42.58900 -8.60600  1.000 49.19000  ? 81  SER B O   1 
ATOM   1626 C CB  . SER B 1 32  ? 17.91700  -42.39300 -11.41100 1.000 54.72000  ? 81  SER B CB  1 
ATOM   1627 O OG  . SER B 1 32  ? 19.06000  -42.10600 -10.63100 1.000 68.52000  ? 81  SER B OG  1 
ATOM   1628 N N   . VAL B 1 33  ? 15.01700  -43.33200 -10.20600 1.000 54.47000  ? 82  VAL B N   1 
ATOM   1629 C CA  . VAL B 1 33  ? 14.51400  -44.46100 -9.45100  1.000 56.60000  ? 82  VAL B CA  1 
ATOM   1630 C C   . VAL B 1 33  ? 15.39100  -45.63600 -9.87700  1.000 56.91000  ? 82  VAL B C   1 
ATOM   1631 O O   . VAL B 1 33  ? 15.30600  -46.11100 -11.01400 1.000 63.21000  ? 82  VAL B O   1 
ATOM   1632 C CB  . VAL B 1 33  ? 13.02600  -44.70300 -9.72800  1.000 62.26000  ? 82  VAL B CB  1 
ATOM   1633 C CG1 . VAL B 1 33  ? 12.46100  -45.73000 -8.75900  1.000 53.56000  ? 82  VAL B CG1 1 
ATOM   1634 C CG2 . VAL B 1 33  ? 12.26100  -43.37800 -9.63200  1.000 56.11000  ? 82  VAL B CG2 1 
ATOM   1635 N N   . LEU B 1 34  ? 16.24800  -46.08800 -8.96400  1.000 52.10000  ? 83  LEU B N   1 
ATOM   1636 C CA  . LEU B 1 34  ? 17.19600  -47.14700 -9.25600  1.000 51.98000  ? 83  LEU B CA  1 
ATOM   1637 C C   . LEU B 1 34  ? 16.46600  -48.40000 -9.72500  1.000 51.85000  ? 83  LEU B C   1 
ATOM   1638 O O   . LEU B 1 34  ? 15.29800  -48.61100 -9.37400  1.000 54.66000  ? 83  LEU B O   1 
ATOM   1639 C CB  . LEU B 1 34  ? 18.02900  -47.44700 -8.01100  1.000 47.10000  ? 83  LEU B CB  1 
ATOM   1640 C CG  . LEU B 1 34  ? 19.02200  -46.33600 -7.70000  1.000 60.10000  ? 83  LEU B CG  1 
ATOM   1641 C CD1 . LEU B 1 34  ? 20.13100  -46.82500 -6.78800  1.000 59.87000  ? 83  LEU B CD1 1 
ATOM   1642 C CD2 . LEU B 1 34  ? 19.63500  -45.91200 -9.03900  1.000 49.60000  ? 83  LEU B CD2 1 
ATOM   1643 N N   . PRO B 1 35  ? 17.11300  -49.22200 -10.55000 1.000 57.91000  ? 84  PRO B N   1 
ATOM   1644 C CA  . PRO B 1 35  ? 16.47500  -50.47500 -10.97500 1.000 61.32000  ? 84  PRO B CA  1 
ATOM   1645 C C   . PRO B 1 35  ? 16.04700  -51.23900 -9.73700  1.000 56.45000  ? 84  PRO B C   1 
ATOM   1646 O O   . PRO B 1 35  ? 16.80500  -51.38200 -8.77800  1.000 52.69000  ? 84  PRO B O   1 
ATOM   1647 C CB  . PRO B 1 35  ? 17.57500  -51.20200 -11.76600 1.000 49.00000  ? 84  PRO B CB  1 
ATOM   1648 C CG  . PRO B 1 35  ? 18.85100  -50.40500 -11.53700 1.000 59.71000  ? 84  PRO B CG  1 
ATOM   1649 C CD  . PRO B 1 35  ? 18.40500  -48.99700 -11.22100 1.000 58.99000  ? 84  PRO B CD  1 
ATOM   1650 N N   . LYS B 1 36  ? 14.80000  -51.68600 -9.74500  1.000 55.43000  ? 85  LYS B N   1 
ATOM   1651 C CA  . LYS B 1 36  ? 14.16000  -52.10500 -8.51400  1.000 51.59000  ? 85  LYS B CA  1 
ATOM   1652 C C   . LYS B 1 36  ? 14.53900  -53.52800 -8.13200  1.000 53.22000  ? 85  LYS B C   1 
ATOM   1653 O O   . LYS B 1 36  ? 14.83900  -54.37100 -8.98000  1.000 61.77000  ? 85  LYS B O   1 
ATOM   1654 C CB  . LYS B 1 36  ? 12.63800  -52.00200 -8.67200  1.000 52.92000  ? 85  LYS B CB  1 
ATOM   1655 C CG  . LYS B 1 36  ? 12.07400  -50.56700 -8.55100  1.000 50.24000  ? 85  LYS B CG  1 
ATOM   1656 C CD  . LYS B 1 36  ? 10.60700  -50.53500 -8.11700  1.000 56.05000  ? 85  LYS B CD  1 
ATOM   1657 C CE  . LYS B 1 36  ? 9.71900   -51.24600 -9.15400  1.000 63.43000  ? 85  LYS B CE  1 
ATOM   1658 N NZ  . LYS B 1 36  ? 8.44000   -50.53800 -9.47100  1.000 66.60000  ? 85  LYS B NZ  1 
ATOM   1659 N N   . ASP B 1 37  ? 14.53800  -53.77300 -6.82900  1.000 53.86000  ? 86  ASP B N   1 
ATOM   1660 C CA  . ASP B 1 37  ? 14.74900  -55.09200 -6.26300  1.000 51.57000  ? 86  ASP B CA  1 
ATOM   1661 C C   . ASP B 1 37  ? 13.38700  -55.78200 -6.18300  1.000 53.69000  ? 86  ASP B C   1 
ATOM   1662 O O   . ASP B 1 37  ? 12.41900  -55.32700 -6.80500  1.000 52.02000  ? 86  ASP B O   1 
ATOM   1663 C CB  . ASP B 1 37  ? 15.45600  -54.98100 -4.91300  1.000 53.05000  ? 86  ASP B CB  1 
ATOM   1664 C CG  . ASP B 1 37  ? 16.87800  -54.49600 -5.05800  1.000 60.83000  ? 86  ASP B CG  1 
ATOM   1665 O OD1 . ASP B 1 37  ? 17.58800  -55.06100 -5.92300  1.000 48.40000  ? 86  ASP B OD1 1 
ATOM   1666 O OD2 . ASP B 1 37  ? 17.28200  -53.55300 -4.32700  1.000 58.84000  ? 86  ASP B OD2 1 
ATOM   1667 N N   . CYS B 1 38  ? 13.29800  -56.85900 -5.39600  1.000 52.85000  ? 87  CYS B N   1 
ATOM   1668 C CA  . CYS B 1 38  ? 12.08000  -57.64400 -5.29100  1.000 50.18000  ? 87  CYS B CA  1 
ATOM   1669 C C   . CYS B 1 38  ? 10.87100  -56.75000 -5.00000  1.000 60.48000  ? 87  CYS B C   1 
ATOM   1670 O O   . CYS B 1 38  ? 10.94200  -55.88200 -4.11300  1.000 47.69000  ? 87  CYS B O   1 
ATOM   1671 C CB  . CYS B 1 38  ? 12.23400  -58.70600 -4.21000  1.000 56.22000  ? 87  CYS B CB  1 
ATOM   1672 S SG  . CYS B 1 38  ? 10.69900  -59.59100 -3.87400  1.000 70.03000  ? 87  CYS B SG  1 
ATOM   1673 N N   . PRO B 1 39  ? 9.75500   -56.92500 -5.72200  1.000 63.04000  ? 88  PRO B N   1 
ATOM   1674 C CA  . PRO B 1 39  ? 8.61200   -56.00900 -5.57400  1.000 58.75000  ? 88  PRO B CA  1 
ATOM   1675 C C   . PRO B 1 39  ? 7.88300   -56.11000 -4.25200  1.000 57.53000  ? 88  PRO B C   1 
ATOM   1676 O O   . PRO B 1 39  ? 7.06900   -55.22600 -3.97000  1.000 57.69000  ? 88  PRO B O   1 
ATOM   1677 C CB  . PRO B 1 39  ? 7.67700   -56.40700 -6.73200  1.000 63.50000  ? 88  PRO B CB  1 
ATOM   1678 C CG  . PRO B 1 39  ? 8.40900   -57.40200 -7.53700  1.000 67.35000  ? 88  PRO B CG  1 
ATOM   1679 C CD  . PRO B 1 39  ? 9.45900   -58.00900 -6.66700  1.000 61.40000  ? 88  PRO B CD  1 
ATOM   1680 N N   . ASP B 1 40  ? 8.13400   -57.12500 -3.43100  1.000 58.82000  ? 89  ASP B N   1 
ATOM   1681 C CA  . ASP B 1 40  ? 7.50700   -57.18000 -2.11600  1.000 62.99000  ? 89  ASP B CA  1 
ATOM   1682 C C   . ASP B 1 40  ? 8.31200   -56.43700 -1.05600  1.000 66.14000  ? 89  ASP B C   1 
ATOM   1683 O O   . ASP B 1 40  ? 7.95800   -56.49300 0.13100   1.000 60.54000  ? 89  ASP B O   1 
ATOM   1684 C CB  . ASP B 1 40  ? 7.27800   -58.63400 -1.64900  1.000 62.69000  ? 89  ASP B CB  1 
ATOM   1685 C CG  . ASP B 1 40  ? 6.52700   -59.48800 -2.67900  1.000 71.08000  ? 89  ASP B CG  1 
ATOM   1686 O OD1 . ASP B 1 40  ? 5.43800   -59.05400 -3.13500  1.000 78.36000  ? 89  ASP B OD1 1 
ATOM   1687 O OD2 . ASP B 1 40  ? 6.99800   -60.62000 -2.97600  1.000 69.95000  ? 89  ASP B OD2 1 
ATOM   1688 N N   . ASN B 1 41  ? 9.41500   -55.80300 -1.43400  1.000 52.63000  ? 90  ASN B N   1 
ATOM   1689 C CA  . ASN B 1 41  ? 10.10100  -54.96300 -0.48000  1.000 52.10000  ? 90  ASN B CA  1 
ATOM   1690 C C   . ASN B 1 41  ? 9.21600   -53.76800 -0.14100  1.000 53.37000  ? 90  ASN B C   1 
ATOM   1691 O O   . ASN B 1 41  ? 8.36000   -53.36900 -0.93300  1.000 55.26000  ? 90  ASN B O   1 
ATOM   1692 C CB  . ASN B 1 41  ? 11.46500  -54.53700 -1.00500  1.000 52.96000  ? 90  ASN B CB  1 
ATOM   1693 C CG  . ASN B 1 41  ? 12.47400  -55.68600 -0.96100  1.000 56.34000  ? 90  ASN B CG  1 
ATOM   1694 O OD1 . ASN B 1 41  ? 12.15100  -56.77900 -0.50100  1.000 61.61000  ? 90  ASN B OD1 1 
ATOM   1695 N ND2 . ASN B 1 41  ? 13.67500  -55.45600 -1.47700  1.000 55.93000  ? 90  ASN B ND2 1 
ATOM   1696 N N   . PRO B 1 42  ? 9.30300   -53.26300 1.08600   1.000 51.06000  ? 91  PRO B N   1 
ATOM   1697 C CA  . PRO B 1 42  ? 8.47700   -52.11300 1.45100   1.000 51.23000  ? 91  PRO B CA  1 
ATOM   1698 C C   . PRO B 1 42  ? 9.02300   -50.79800 0.93600   1.000 51.38000  ? 91  PRO B C   1 
ATOM   1699 O O   . PRO B 1 42  ? 8.33300   -49.77300 1.04800   1.000 51.30000  ? 91  PRO B O   1 
ATOM   1700 C CB  . PRO B 1 42  ? 8.49500   -52.15800 2.98700   1.000 40.51000  ? 91  PRO B CB  1 
ATOM   1701 C CG  . PRO B 1 42  ? 9.82700   -52.74100 3.30400   1.000 41.29000  ? 91  PRO B CG  1 
ATOM   1702 C CD  . PRO B 1 42  ? 10.08200  -53.77400 2.23100   1.000 44.57000  ? 91  PRO B CD  1 
ATOM   1703 N N   . HIS B 1 43  ? 10.22800  -50.80100 0.37500   1.000 44.86000  ? 92  HIS B N   1 
ATOM   1704 C CA  . HIS B 1 43  ? 10.96100  -49.58600 0.08500   1.000 47.19000  ? 92  HIS B CA  1 
ATOM   1705 C C   . HIS B 1 43  ? 11.52300  -49.64000 -1.32600  1.000 49.63000  ? 92  HIS B C   1 
ATOM   1706 O O   . HIS B 1 43  ? 11.65100  -50.71300 -1.93100  1.000 51.91000  ? 92  HIS B O   1 
ATOM   1707 C CB  . HIS B 1 43  ? 12.12400  -49.41900 1.06200   1.000 44.88000  ? 92  HIS B CB  1 
ATOM   1708 C CG  . HIS B 1 43  ? 13.14900  -50.50500 0.94600   1.000 45.26000  ? 92  HIS B CG  1 
ATOM   1709 N ND1 . HIS B 1 43  ? 12.82600  -51.84400 1.03100   1.000 46.47000  ? 92  HIS B ND1 1 
ATOM   1710 C CD2 . HIS B 1 43  ? 14.48200  -50.45600 0.69300   1.000 41.98000  ? 92  HIS B CD2 1 
ATOM   1711 C CE1 . HIS B 1 43  ? 13.92300  -52.57000 0.88200   1.000 45.25000  ? 92  HIS B CE1 1 
ATOM   1712 N NE2 . HIS B 1 43  ? 14.94400  -51.75200 0.68500   1.000 41.71000  ? 92  HIS B NE2 1 
ATOM   1713 N N   . ILE B 1 44  ? 11.91000  -48.46600 -1.82700  1.000 49.38000  ? 93  ILE B N   1 
ATOM   1714 C CA  . ILE B 1 44  ? 12.62800  -48.34800 -3.09500  1.000 42.34000  ? 93  ILE B CA  1 
ATOM   1715 C C   . ILE B 1 44  ? 13.77300  -47.36700 -2.91000  1.000 42.90000  ? 93  ILE B C   1 
ATOM   1716 O O   . ILE B 1 44  ? 13.73600  -46.50000 -2.03400  1.000 54.94000  ? 93  ILE B O   1 
ATOM   1717 C CB  . ILE B 1 44  ? 11.72700  -47.89400 -4.26200  1.000 39.39000  ? 93  ILE B CB  1 
ATOM   1718 C CG1 . ILE B 1 44  ? 11.20000  -46.49100 -4.01800  1.000 44.84000  ? 93  ILE B CG1 1 
ATOM   1719 C CG2 . ILE B 1 44  ? 10.58700  -48.86000 -4.47900  1.000 42.18000  ? 93  ILE B CG2 1 
ATOM   1720 C CD1 . ILE B 1 44  ? 10.32300  -45.99300 -5.12400  1.000 41.39000  ? 93  ILE B CD1 1 
ATOM   1721 N N   . TRP B 1 45  ? 14.80600  -47.52400 -3.71800  1.000 43.45000  ? 94  TRP B N   1 
ATOM   1722 C CA  . TRP B 1 45  ? 15.99300  -46.68600 -3.64400  1.000 48.95000  ? 94  TRP B CA  1 
ATOM   1723 C C   . TRP B 1 45  ? 15.98700  -45.60000 -4.72400  1.000 51.00000  ? 94  TRP B C   1 
ATOM   1724 O O   . TRP B 1 45  ? 15.65800  -45.85700 -5.88900  1.000 49.51000  ? 94  TRP B O   1 
ATOM   1725 C CB  . TRP B 1 45  ? 17.24500  -47.55200 -3.77000  1.000 51.45000  ? 94  TRP B CB  1 
ATOM   1726 C CG  . TRP B 1 45  ? 17.42600  -48.46500 -2.61100  1.000 50.73000  ? 94  TRP B CG  1 
ATOM   1727 C CD1 . TRP B 1 45  ? 17.03700  -49.77300 -2.51600  1.000 51.41000  ? 94  TRP B CD1 1 
ATOM   1728 C CD2 . TRP B 1 45  ? 18.03300  -48.13400 -1.35900  1.000 47.68000  ? 94  TRP B CD2 1 
ATOM   1729 N NE1 . TRP B 1 45  ? 17.37700  -50.27900 -1.27600  1.000 45.26000  ? 94  TRP B NE1 1 
ATOM   1730 C CE2 . TRP B 1 45  ? 17.98700  -49.29000 -0.54900  1.000 46.14000  ? 94  TRP B CE2 1 
ATOM   1731 C CE3 . TRP B 1 45  ? 18.61200  -46.96900 -0.84100  1.000 51.81000  ? 94  TRP B CE3 1 
ATOM   1732 C CZ2 . TRP B 1 45  ? 18.50000  -49.31300 0.75100   1.000 47.04000  ? 94  TRP B CZ2 1 
ATOM   1733 C CZ3 . TRP B 1 45  ? 19.12600  -46.99800 0.44700   1.000 51.30000  ? 94  TRP B CZ3 1 
ATOM   1734 C CH2 . TRP B 1 45  ? 19.07000  -48.16300 1.22400   1.000 43.79000  ? 94  TRP B CH2 1 
ATOM   1735 N N   . LEU B 1 46  ? 16.33800  -44.38200 -4.32300  1.000 49.10000  ? 95  LEU B N   1 
ATOM   1736 C CA  . LEU B 1 46  ? 16.50600  -43.25800 -5.23100  1.000 44.27000  ? 95  LEU B CA  1 
ATOM   1737 C C   . LEU B 1 46  ? 17.96100  -42.80400 -5.23000  1.000 51.26000  ? 95  LEU B C   1 
ATOM   1738 O O   . LEU B 1 46  ? 18.66800  -42.94000 -4.22300  1.000 45.43000  ? 95  LEU B O   1 
ATOM   1739 C CB  . LEU B 1 46  ? 15.61600  -42.08700 -4.83700  1.000 46.45000  ? 95  LEU B CB  1 
ATOM   1740 C CG  . LEU B 1 46  ? 14.14700  -42.33800 -4.53300  1.000 45.13000  ? 95  LEU B CG  1 
ATOM   1741 C CD1 . LEU B 1 46  ? 13.51700  -40.99700 -4.13800  1.000 44.11000  ? 95  LEU B CD1 1 
ATOM   1742 C CD2 . LEU B 1 46  ? 13.46000  -42.93300 -5.74300  1.000 39.62000  ? 95  LEU B CD2 1 
ATOM   1743 N N   . GLN B 1 47  ? 18.39500  -42.25100 -6.36700  1.000 50.04000  ? 96  GLN B N   1 
ATOM   1744 C CA  . GLN B 1 47  ? 19.77500  -41.83000 -6.58700  1.000 49.45000  ? 96  GLN B CA  1 
ATOM   1745 C C   . GLN B 1 47  ? 19.79100  -40.38500 -7.05700  1.000 49.73000  ? 96  GLN B C   1 
ATOM   1746 O O   . GLN B 1 47  ? 19.08400  -40.03100 -8.00800  1.000 51.53000  ? 96  GLN B O   1 
ATOM   1747 C CB  . GLN B 1 47  ? 20.46300  -42.72700 -7.62500  1.000 63.29000  ? 96  GLN B CB  1 
ATOM   1748 C CG  . GLN B 1 47  ? 21.95400  -42.48000 -7.84700  1.000 65.07000  ? 96  GLN B CG  1 
ATOM   1749 C CD  . GLN B 1 47  ? 22.82200  -43.35800 -6.94600  1.000 75.22000  ? 96  GLN B CD  1 
ATOM   1750 O OE1 . GLN B 1 47  ? 23.14100  -44.51400 -7.27200  1.000 59.51000  ? 96  GLN B OE1 1 
ATOM   1751 N NE2 . GLN B 1 47  ? 23.21200  -42.80400 -5.80100  1.000 75.04000  ? 96  GLN B NE2 1 
ATOM   1752 N N   . LEU B 1 48  ? 20.58300  -39.55200 -6.38800  1.000 54.07000  ? 97  LEU B N   1 
ATOM   1753 C CA  . LEU B 1 48  ? 20.71200  -38.14900 -6.74500  1.000 52.42000  ? 97  LEU B CA  1 
ATOM   1754 C C   . LEU B 1 48  ? 22.10600  -37.88300 -7.29200  1.000 53.34000  ? 97  LEU B C   1 
ATOM   1755 O O   . LEU B 1 48  ? 23.09600  -38.41200 -6.78000  1.000 59.44000  ? 97  LEU B O   1 
ATOM   1756 C CB  . LEU B 1 48  ? 20.43300  -37.26000 -5.53800  1.000 47.76000  ? 97  LEU B CB  1 
ATOM   1757 C CG  . LEU B 1 48  ? 18.97000  -37.27700 -5.11100  1.000 52.14000  ? 97  LEU B CG  1 
ATOM   1758 C CD1 . LEU B 1 48  ? 18.73800  -36.31900 -3.97000  1.000 47.07000  ? 97  LEU B CD1 1 
ATOM   1759 C CD2 . LEU B 1 48  ? 18.10300  -36.89600 -6.28600  1.000 54.00000  ? 97  LEU B CD2 1 
ATOM   1760 N N   . GLU B 1 49  ? 22.17500  -37.07000 -8.34400  1.000 54.93000  ? 98  GLU B N   1 
ATOM   1761 C CA  . GLU B 1 49  ? 23.42700  -36.72600 -9.01100  1.000 55.58000  ? 98  GLU B CA  1 
ATOM   1762 C C   . GLU B 1 49  ? 23.51000  -35.21900 -9.12800  1.000 48.07000  ? 98  GLU B C   1 
ATOM   1763 O O   . GLU B 1 49  ? 22.56200  -34.58200 -9.59600  1.000 53.25000  ? 98  GLU B O   1 
ATOM   1764 C CB  . GLU B 1 49  ? 23.50600  -37.34600 -10.39500 1.000 52.99000  ? 98  GLU B CB  1 
ATOM   1765 C CG  . GLU B 1 49  ? 23.15900  -38.80800 -10.38100 1.000 70.18000  ? 98  GLU B CG  1 
ATOM   1766 C CD  . GLU B 1 49  ? 23.98000  -39.58900 -11.37900 1.000 96.60000  ? 98  GLU B CD  1 
ATOM   1767 O OE1 . GLU B 1 49  ? 24.28600  -39.03500 -12.47500 1.000 90.04000  ? 98  GLU B OE1 1 
ATOM   1768 O OE2 . GLU B 1 49  ? 24.33200  -40.75000 -11.04500 1.000 100.97000 ? 98  GLU B OE2 1 
ATOM   1769 N N   . GLY B 1 50  ? 24.63500  -34.65900 -8.72200  1.000 49.50000  ? 99  GLY B N   1 
ATOM   1770 C CA  . GLY B 1 50  ? 24.85300  -33.24000 -8.80800  1.000 43.66000  ? 99  GLY B CA  1 
ATOM   1771 C C   . GLY B 1 50  ? 25.58500  -32.76000 -7.57600  1.000 48.28000  ? 99  GLY B C   1 
ATOM   1772 O O   . GLY B 1 50  ? 25.94400  -33.54100 -6.69500  1.000 47.62000  ? 99  GLY B O   1 
ATOM   1773 N N   . PRO B 1 51  ? 25.79800  -31.46600 -7.48500  1.000 53.77000  ? 100 PRO B N   1 
ATOM   1774 C CA  . PRO B 1 51  ? 26.56600  -30.91400 -6.35900  1.000 53.56000  ? 100 PRO B CA  1 
ATOM   1775 C C   . PRO B 1 51  ? 26.01600  -31.32400 -5.00600  1.000 61.47000  ? 100 PRO B C   1 
ATOM   1776 O O   . PRO B 1 51  ? 24.84000  -31.68300 -4.89800  1.000 56.22000  ? 100 PRO B O   1 
ATOM   1777 C CB  . PRO B 1 51  ? 26.45100  -29.40000 -6.56200  1.000 45.37000  ? 100 PRO B CB  1 
ATOM   1778 C CG  . PRO B 1 51  ? 26.16700  -29.24300 -8.00200  1.000 53.25000  ? 100 PRO B CG  1 
ATOM   1779 C CD  . PRO B 1 51  ? 25.38200  -30.43500 -8.44100  1.000 42.74000  ? 100 PRO B CD  1 
ATOM   1780 N N   . LYS B 1 52  ? 26.87300  -31.27000 -3.97800  1.000 62.92000  ? 101 LYS B N   1 
ATOM   1781 C CA  . LYS B 1 52  ? 26.50200  -31.74900 -2.65500  1.000 53.33000  ? 101 LYS B CA  1 
ATOM   1782 C C   . LYS B 1 52  ? 25.35900  -30.91900 -2.07500  1.000 58.61000  ? 101 LYS B C   1 
ATOM   1783 O O   . LYS B 1 52  ? 24.45600  -31.46100 -1.42300  1.000 59.08000  ? 101 LYS B O   1 
ATOM   1784 C CB  . LYS B 1 52  ? 27.73200  -31.71800 -1.73800  1.000 62.34000  ? 101 LYS B CB  1 
ATOM   1785 C CG  . LYS B 1 52  ? 27.52900  -32.29400 -0.32500  1.000 68.41000  ? 101 LYS B CG  1 
ATOM   1786 C CD  . LYS B 1 52  ? 28.86400  -32.34100 0.46200   1.000 70.49000  ? 101 LYS B CD  1 
ATOM   1787 C CE  . LYS B 1 52  ? 28.67400  -32.32400 1.98600   1.000 77.64000  ? 101 LYS B CE  1 
ATOM   1788 N NZ  . LYS B 1 52  ? 27.31300  -31.87900 2.42900   1.000 78.15000  ? 101 LYS B NZ  1 
ATOM   1789 N N   . GLU B 1 53  ? 25.38700  -29.59800 -2.29100  1.000 55.43000  ? 102 GLU B N   1 
ATOM   1790 C CA  . GLU B 1 53  ? 24.34800  -28.73300 -1.73400  1.000 52.43000  ? 102 GLU B CA  1 
ATOM   1791 C C   . GLU B 1 53  ? 23.00000  -29.02500 -2.37300  1.000 58.21000  ? 102 GLU B C   1 
ATOM   1792 O O   . GLU B 1 53  ? 21.98400  -29.15200 -1.67400  1.000 56.31000  ? 102 GLU B O   1 
ATOM   1793 C CB  . GLU B 1 53  ? 24.70600  -27.25900 -1.92600  1.000 50.05000  ? 102 GLU B CB  1 
ATOM   1794 C CG  . GLU B 1 53  ? 23.75700  -26.29300 -1.17700  1.000 57.66000  ? 102 GLU B CG  1 
ATOM   1795 C CD  . GLU B 1 53  ? 23.81600  -26.42600 0.36200   1.000 63.38000  ? 102 GLU B CD  1 
ATOM   1796 O OE1 . GLU B 1 53  ? 24.83500  -26.91100 0.90800   1.000 61.51000  ? 102 GLU B OE1 1 
ATOM   1797 O OE2 . GLU B 1 53  ? 22.82600  -26.05300 1.03600   1.000 61.91000  ? 102 GLU B OE2 1 
ATOM   1798 N N   . ASN B 1 54  ? 22.97900  -29.11700 -3.70700  1.000 53.87000  ? 103 ASN B N   1 
ATOM   1799 C CA  . ASN B 1 54  ? 21.75600  -29.42600 -4.43900  1.000 47.07000  ? 103 ASN B CA  1 
ATOM   1800 C C   . ASN B 1 54  ? 21.16800  -30.75800 -3.98900  1.000 45.70000  ? 103 ASN B C   1 
ATOM   1801 O O   . ASN B 1 54  ? 19.96800  -30.86000 -3.71200  1.000 45.87000  ? 103 ASN B O   1 
ATOM   1802 C CB  . ASN B 1 54  ? 22.02700  -29.44800 -5.95000  1.000 45.46000  ? 103 ASN B CB  1 
ATOM   1803 C CG  . ASN B 1 54  ? 22.71000  -28.17900 -6.46200  1.000 48.68000  ? 103 ASN B CG  1 
ATOM   1804 O OD1 . ASN B 1 54  ? 23.79000  -27.81800 -6.01200  1.000 50.47000  ? 103 ASN B OD1 1 
ATOM   1805 N ND2 . ASN B 1 54  ? 22.09000  -27.52000 -7.43300  1.000 52.15000  ? 103 ASN B ND2 1 
ATOM   1806 N N   . ALA B 1 55  ? 21.99200  -31.80300 -3.93900  1.000 48.76000  ? 104 ALA B N   1 
ATOM   1807 C CA  . ALA B 1 55  ? 21.47400  -33.12000 -3.58000  1.000 53.03000  ? 104 ALA B CA  1 
ATOM   1808 C C   . ALA B 1 55  ? 20.89000  -33.10900 -2.17700  1.000 50.82000  ? 104 ALA B C   1 
ATOM   1809 O O   . ALA B 1 55  ? 19.83100  -33.70000 -1.92600  1.000 50.07000  ? 104 ALA B O   1 
ATOM   1810 C CB  . ALA B 1 55  ? 22.57100  -34.17900 -3.69600  1.000 44.47000  ? 104 ALA B CB  1 
ATOM   1811 N N   . SER B 1 56  ? 21.55600  -32.41900 -1.25500  1.000 43.28000  ? 105 SER B N   1 
ATOM   1812 C CA  . SER B 1 56  ? 21.05500  -32.35800 0.10400   1.000 53.62000  ? 105 SER B CA  1 
ATOM   1813 C C   . SER B 1 56  ? 19.66900  -31.71200 0.13600   1.000 49.77000  ? 105 SER B C   1 
ATOM   1814 O O   . SER B 1 56  ? 18.73500  -32.24600 0.74500   1.000 43.51000  ? 105 SER B O   1 
ATOM   1815 C CB  . SER B 1 56  ? 22.06300  -31.61600 0.98200   1.000 50.18000  ? 105 SER B CB  1 
ATOM   1816 O OG  . SER B 1 56  ? 21.41200  -31.00600 2.08200   1.000 62.49000  ? 105 SER B OG  1 
ATOM   1817 N N   . ARG B 1 57  ? 19.50100  -30.58200 -0.55900  1.000 47.66000  ? 106 ARG B N   1 
ATOM   1818 C CA  . ARG B 1 57  ? 18.19100  -29.93300 -0.57700  1.000 46.35000  ? 106 ARG B CA  1 
ATOM   1819 C C   . ARG B 1 57  ? 17.15800  -30.77000 -1.31700  1.000 49.89000  ? 106 ARG B C   1 
ATOM   1820 O O   . ARG B 1 57  ? 16.01900  -30.90800 -0.85300  1.000 44.49000  ? 106 ARG B O   1 
ATOM   1821 C CB  . ARG B 1 57  ? 18.29700  -28.55200 -1.20300  1.000 48.61000  ? 106 ARG B CB  1 
ATOM   1822 C CG  . ARG B 1 57  ? 19.28100  -27.66300 -0.48500  1.000 47.68000  ? 106 ARG B CG  1 
ATOM   1823 C CD  . ARG B 1 57  ? 19.39300  -26.33500 -1.17100  1.000 48.40000  ? 106 ARG B CD  1 
ATOM   1824 N NE  . ARG B 1 57  ? 20.26200  -25.44500 -0.41800  1.000 50.67000  ? 106 ARG B NE  1 
ATOM   1825 C CZ  . ARG B 1 57  ? 19.96100  -24.20000 -0.09100  1.000 49.14000  ? 106 ARG B CZ  1 
ATOM   1826 N NH1 . ARG B 1 57  ? 18.79200  -23.66700 -0.40800  1.000 50.15000  ? 106 ARG B NH1 1 
ATOM   1827 N NH2 . ARG B 1 57  ? 20.85500  -23.47400 0.57200   1.000 50.23000  ? 106 ARG B NH2 1 
ATOM   1828 N N   . ALA B 1 58  ? 17.55000  -31.38700 -2.43600  1.000 47.08000  ? 107 ALA B N   1 
ATOM   1829 C CA  . ALA B 1 58  ? 16.58900  -32.17700 -3.19000  1.000 39.15000  ? 107 ALA B CA  1 
ATOM   1830 C C   . ALA B 1 58  ? 16.14100  -33.38900 -2.40800  1.000 45.30000  ? 107 ALA B C   1 
ATOM   1831 O O   . ALA B 1 58  ? 14.98400  -33.81800 -2.54800  1.000 45.57000  ? 107 ALA B O   1 
ATOM   1832 C CB  . ALA B 1 58  ? 17.18200  -32.61100 -4.53100  1.000 42.59000  ? 107 ALA B CB  1 
ATOM   1833 N N   . LYS B 1 59  ? 17.03000  -33.95200 -1.58000  1.000 42.21000  ? 108 LYS B N   1 
ATOM   1834 C CA  . LYS B 1 59  ? 16.65400  -35.14100 -0.82200  1.000 40.90000  ? 108 LYS B CA  1 
ATOM   1835 C C   . LYS B 1 59  ? 15.60100  -34.79500 0.22300   1.000 47.94000  ? 108 LYS B C   1 
ATOM   1836 O O   . LYS B 1 59  ? 14.58500  -35.48800 0.35400   1.000 47.26000  ? 108 LYS B O   1 
ATOM   1837 C CB  . LYS B 1 59  ? 17.88600  -35.77500 -0.19100  1.000 40.91000  ? 108 LYS B CB  1 
ATOM   1838 C CG  . LYS B 1 59  ? 17.53400  -37.06800 0.49900   1.000 49.89000  ? 108 LYS B CG  1 
ATOM   1839 C CD  . LYS B 1 59  ? 18.73200  -37.92900 0.76800   1.000 55.37000  ? 108 LYS B CD  1 
ATOM   1840 C CE  . LYS B 1 59  ? 19.39000  -37.58500 2.05900   1.000 51.79000  ? 108 LYS B CE  1 
ATOM   1841 N NZ  . LYS B 1 59  ? 20.53600  -38.52700 2.24300   1.000 65.63000  ? 108 LYS B NZ  1 
ATOM   1842 N N   . GLU B 1 60  ? 15.81900  -33.69700 0.94700   1.000 46.45000  ? 109 GLU B N   1 
ATOM   1843 C CA  . GLU B 1 60  ? 14.82000  -33.17200 1.86700   1.000 47.11000  ? 109 GLU B CA  1 
ATOM   1844 C C   . GLU B 1 60  ? 13.47100  -32.99100 1.17600   1.000 50.54000  ? 109 GLU B C   1 
ATOM   1845 O O   . GLU B 1 60  ? 12.41600  -33.34500 1.73300   1.000 50.22000  ? 109 GLU B O   1 
ATOM   1846 C CB  . GLU B 1 60  ? 15.31600  -31.83700 2.41100   1.000 44.58000  ? 109 GLU B CB  1 
ATOM   1847 C CG  . GLU B 1 60  ? 15.31500  -31.68300 3.89300   1.000 60.09000  ? 109 GLU B CG  1 
ATOM   1848 C CD  . GLU B 1 60  ? 15.76100  -30.27900 4.31800   1.000 71.23000  ? 109 GLU B CD  1 
ATOM   1849 O OE1 . GLU B 1 60  ? 16.81400  -29.79000 3.82000   1.000 69.96000  ? 109 GLU B OE1 1 
ATOM   1850 O OE2 . GLU B 1 60  ? 15.02600  -29.65700 5.12900   1.000 69.35000  ? 109 GLU B OE2 1 
ATOM   1851 N N   . TYR B 1 61  ? 13.48800  -32.41900 -0.03700  1.000 41.09000  ? 110 TYR B N   1 
ATOM   1852 C CA  . TYR B 1 61  ? 12.26000  -32.22600 -0.80800  1.000 39.07000  ? 110 TYR B CA  1 
ATOM   1853 C C   . TYR B 1 61  ? 11.60600  -33.55900 -1.13900  1.000 42.18000  ? 110 TYR B C   1 
ATOM   1854 O O   . TYR B 1 61  ? 10.39900  -33.72800 -0.96200  1.000 45.47000  ? 110 TYR B O   1 
ATOM   1855 C CB  . TYR B 1 61  ? 12.56900  -31.43900 -2.08500  1.000 45.15000  ? 110 TYR B CB  1 
ATOM   1856 C CG  . TYR B 1 61  ? 11.37300  -31.02000 -2.92600  1.000 45.24000  ? 110 TYR B CG  1 
ATOM   1857 C CD1 . TYR B 1 61  ? 10.78300  -31.89900 -3.83000  1.000 45.03000  ? 110 TYR B CD1 1 
ATOM   1858 C CD2 . TYR B 1 61  ? 10.85800  -29.72800 -2.83700  1.000 45.21000  ? 110 TYR B CD2 1 
ATOM   1859 C CE1 . TYR B 1 61  ? 9.69900   -31.50700 -4.61800  1.000 48.83000  ? 110 TYR B CE1 1 
ATOM   1860 C CE2 . TYR B 1 61  ? 9.78800   -29.32400 -3.60600  1.000 50.53000  ? 110 TYR B CE2 1 
ATOM   1861 C CZ  . TYR B 1 61  ? 9.21400   -30.21100 -4.50400  1.000 58.12000  ? 110 TYR B CZ  1 
ATOM   1862 O OH  . TYR B 1 61  ? 8.14700   -29.79000 -5.27100  1.000 66.71000  ? 110 TYR B OH  1 
ATOM   1863 N N   . LEU B 1 62  ? 12.38300  -34.50900 -1.66100  1.000 45.18000  ? 111 LEU B N   1 
ATOM   1864 C CA  . LEU B 1 62  ? 11.81800  -35.80400 -2.02100  1.000 41.33000  ? 111 LEU B CA  1 
ATOM   1865 C C   . LEU B 1 62  ? 11.24600  -36.50700 -0.79200  1.000 52.64000  ? 111 LEU B C   1 
ATOM   1866 O O   . LEU B 1 62  ? 10.12000  -37.02100 -0.82400  1.000 51.41000  ? 111 LEU B O   1 
ATOM   1867 C CB  . LEU B 1 62  ? 12.89100  -36.67600 -2.66100  1.000 38.46000  ? 111 LEU B CB  1 
ATOM   1868 C CG  . LEU B 1 62  ? 13.06700  -36.83200 -4.17400  1.000 46.85000  ? 111 LEU B CG  1 
ATOM   1869 C CD1 . LEU B 1 62  ? 11.93000  -36.24300 -5.01900  1.000 41.37000  ? 111 LEU B CD1 1 
ATOM   1870 C CD2 . LEU B 1 62  ? 14.44200  -36.35500 -4.62400  1.000 40.33000  ? 111 LEU B CD2 1 
ATOM   1871 N N   . LYS B 1 63  ? 11.99600  -36.51600 0.31700   1.000 45.04000  ? 112 LYS B N   1 
ATOM   1872 C CA  . LYS B 1 63  ? 11.47800  -37.15600 1.52200   1.000 46.62000  ? 112 LYS B CA  1 
ATOM   1873 C C   . LYS B 1 63  ? 10.20600  -36.46300 1.99000   1.000 49.45000  ? 112 LYS B C   1 
ATOM   1874 O O   . LYS B 1 63  ? 9.23500   -37.12900 2.36600   1.000 49.14000  ? 112 LYS B O   1 
ATOM   1875 C CB  . LYS B 1 63  ? 12.52900  -37.16300 2.63700   1.000 43.36000  ? 112 LYS B CB  1 
ATOM   1876 C CG  . LYS B 1 63  ? 13.67100  -38.15800 2.44600   1.000 44.45000  ? 112 LYS B CG  1 
ATOM   1877 C CD  . LYS B 1 63  ? 14.77000  -37.89400 3.47900   1.000 45.00000  ? 112 LYS B CD  1 
ATOM   1878 C CE  . LYS B 1 63  ? 15.67000  -39.11000 3.71500   1.000 49.43000  ? 112 LYS B CE  1 
ATOM   1879 N NZ  . LYS B 1 63  ? 16.82100  -38.69500 4.57900   1.000 58.85000  ? 112 LYS B NZ  1 
ATOM   1880 N N   . GLY B 1 64  ? 10.17200  -35.12200 1.93900   1.000 53.27000  ? 113 GLY B N   1 
ATOM   1881 C CA  . GLY B 1 64  ? 8.94400   -34.42400 2.31300   1.000 50.79000  ? 113 GLY B CA  1 
ATOM   1882 C C   . GLY B 1 64  ? 7.78600   -34.73500 1.38000   1.000 52.55000  ? 113 GLY B C   1 
ATOM   1883 O O   . GLY B 1 64  ? 6.62200   -34.72400 1.78800   1.000 53.64000  ? 113 GLY B O   1 
ATOM   1884 N N   . LEU B 1 65  ? 8.08900   -35.06500 0.13200   1.000 47.27000  ? 114 LEU B N   1 
ATOM   1885 C CA  . LEU B 1 65  ? 7.04600   -35.44600 -0.81100  1.000 51.49000  ? 114 LEU B CA  1 
ATOM   1886 C C   . LEU B 1 65  ? 6.52400   -36.85500 -0.53000  1.000 56.75000  ? 114 LEU B C   1 
ATOM   1887 O O   . LEU B 1 65  ? 5.32400   -37.12000 -0.66000  1.000 56.08000  ? 114 LEU B O   1 
ATOM   1888 C CB  . LEU B 1 65  ? 7.60300   -35.30800 -2.21700  1.000 45.20000  ? 114 LEU B CB  1 
ATOM   1889 C CG  . LEU B 1 65  ? 6.64200   -35.43800 -3.37000  1.000 59.48000  ? 114 LEU B CG  1 
ATOM   1890 C CD1 . LEU B 1 65  ? 6.02800   -34.08200 -3.62500  1.000 61.26000  ? 114 LEU B CD1 1 
ATOM   1891 C CD2 . LEU B 1 65  ? 7.46800   -35.87300 -4.57300  1.000 62.82000  ? 114 LEU B CD2 1 
ATOM   1892 N N   . CYS B 1 66  ? 7.40800   -37.76100 -0.11200  1.000 55.81000  ? 115 CYS B N   1 
ATOM   1893 C CA  . CYS B 1 66  ? 7.04100   -39.15600 0.06800   1.000 51.88000  ? 115 CYS B CA  1 
ATOM   1894 C C   . CYS B 1 66  ? 6.35600   -39.41200 1.40800   1.000 57.85000  ? 115 CYS B C   1 
ATOM   1895 O O   . CYS B 1 66  ? 5.49400   -40.29500 1.51100   1.000 52.45000  ? 115 CYS B O   1 
ATOM   1896 C CB  . CYS B 1 66  ? 8.29600   -40.02500 -0.04100  1.000 56.31000  ? 115 CYS B CB  1 
ATOM   1897 S SG  . CYS B 1 66  ? 9.03600   -40.04100 -1.71000  1.000 56.14000  ? 115 CYS B SG  1 
ATOM   1898 N N   . SER B 1 67  ? 6.73000   -38.67500 2.44500   1.000 51.36000  ? 116 SER B N   1 
ATOM   1899 C CA  . SER B 1 67  ? 6.04100   -38.74300 3.73200   1.000 63.35000  ? 116 SER B CA  1 
ATOM   1900 C C   . SER B 1 67  ? 6.07000   -37.35500 4.36300   1.000 59.31000  ? 116 SER B C   1 
ATOM   1901 O O   . SER B 1 67  ? 6.94700   -37.03200 5.17900   1.000 60.52000  ? 116 SER B O   1 
ATOM   1902 C CB  . SER B 1 67  ? 6.67200   -39.81100 4.63500   1.000 58.64000  ? 116 SER B CB  1 
ATOM   1903 O OG  . SER B 1 67  ? 7.65600   -39.27100 5.49700   1.000 71.14000  ? 116 SER B OG  1 
ATOM   1904 N N   . PRO B 1 68  ? 5.13200   -36.48400 3.98800   1.000 55.68000  ? 117 PRO B N   1 
ATOM   1905 C CA  . PRO B 1 68  ? 5.11500   -35.14100 4.57700   1.000 52.69000  ? 117 PRO B CA  1 
ATOM   1906 C C   . PRO B 1 68  ? 4.83000   -35.22000 6.06900   1.000 58.89000  ? 117 PRO B C   1 
ATOM   1907 O O   . PRO B 1 68  ? 3.94500   -35.95700 6.50900   1.000 56.60000  ? 117 PRO B O   1 
ATOM   1908 C CB  . PRO B 1 68  ? 3.99500   -34.42000 3.81400   1.000 55.18000  ? 117 PRO B CB  1 
ATOM   1909 C CG  . PRO B 1 68  ? 3.15700   -35.48500 3.21700   1.000 50.62000  ? 117 PRO B CG  1 
ATOM   1910 C CD  . PRO B 1 68  ? 4.03000   -36.70100 3.03000   1.000 50.33000  ? 117 PRO B CD  1 
ATOM   1911 N N   . GLU B 1 69  ? 5.60700   -34.46100 6.84500   1.000 58.60000  ? 118 GLU B N   1 
ATOM   1912 C CA  . GLU B 1 69  ? 5.40100   -34.35000 8.28200   1.000 54.01000  ? 118 GLU B CA  1 
ATOM   1913 C C   . GLU B 1 69  ? 4.44500   -33.22400 8.63100   1.000 59.87000  ? 118 GLU B C   1 
ATOM   1914 O O   . GLU B 1 69  ? 3.82900   -33.26200 9.70100   1.000 58.10000  ? 118 GLU B O   1 
ATOM   1915 C CB  . GLU B 1 69  ? 6.74600   -34.15400 9.00000   1.000 57.34000  ? 118 GLU B CB  1 
ATOM   1916 C CG  . GLU B 1 69  ? 7.73900   -35.32200 8.78100   1.000 58.20000  ? 118 GLU B CG  1 
ATOM   1917 C CD  . GLU B 1 69  ? 9.19800   -34.99400 9.14800   1.000 63.75000  ? 118 GLU B CD  1 
ATOM   1918 O OE1 . GLU B 1 69  ? 9.49800   -33.85700 9.60600   1.000 55.54000  ? 118 GLU B OE1 1 
ATOM   1919 O OE2 . GLU B 1 69  ? 10.05800  -35.89100 8.95200   1.000 75.18000  ? 118 GLU B OE2 1 
ATOM   1920 N N   . LEU B 1 70  ? 4.32300   -32.21300 7.76700   1.000 53.46000  ? 119 LEU B N   1 
ATOM   1921 C CA  . LEU B 1 70  ? 3.34300   -31.15200 7.95600   1.000 49.46000  ? 119 LEU B CA  1 
ATOM   1922 C C   . LEU B 1 70  ? 2.73600   -30.79300 6.60900   1.000 59.30000  ? 119 LEU B C   1 
ATOM   1923 O O   . LEU B 1 70  ? 3.38900   -30.89000 5.56300   1.000 61.97000  ? 119 LEU B O   1 
ATOM   1924 C CB  . LEU B 1 70  ? 3.94700   -29.91000 8.61600   1.000 47.25000  ? 119 LEU B CB  1 
ATOM   1925 C CG  . LEU B 1 70  ? 4.24800   -30.03200 10.12100  1.000 54.32000  ? 119 LEU B CG  1 
ATOM   1926 C CD1 . LEU B 1 70  ? 4.78700   -28.72800 10.72500  1.000 51.68000  ? 119 LEU B CD1 1 
ATOM   1927 C CD2 . LEU B 1 70  ? 3.01600   -30.47000 10.87000  1.000 45.38000  ? 119 LEU B CD2 1 
ATOM   1928 N N   . GLN B 1 71  ? 1.47400   -30.37600 6.64600   1.000 59.99000  ? 120 GLN B N   1 
ATOM   1929 C CA  . GLN B 1 71  ? 0.70700   -30.13000 5.43500   1.000 59.73000  ? 120 GLN B CA  1 
ATOM   1930 C C   . GLN B 1 71  ? -0.43000  -29.19000 5.78000   1.000 61.64000  ? 120 GLN B C   1 
ATOM   1931 O O   . GLN B 1 71  ? -1.11900  -29.42000 6.77500   1.000 62.12000  ? 120 GLN B O   1 
ATOM   1932 C CB  . GLN B 1 71  ? 0.16800   -31.43700 4.87200   1.000 62.72000  ? 120 GLN B CB  1 
ATOM   1933 C CG  . GLN B 1 71  ? -0.07700  -31.40200 3.39300   1.000 75.57000  ? 120 GLN B CG  1 
ATOM   1934 C CD  . GLN B 1 71  ? -0.43800  -32.76600 2.84800   1.000 88.41000  ? 120 GLN B CD  1 
ATOM   1935 O OE1 . GLN B 1 71  ? -0.62200  -32.92800 1.63400   1.000 81.01000  ? 120 GLN B OE1 1 
ATOM   1936 N NE2 . GLN B 1 71  ? -0.52400  -33.76900 3.74200   1.000 76.98000  ? 120 GLN B NE2 1 
ATOM   1937 N N   . ASP B 1 72  ? -0.62300  -28.14200 4.97400   1.000 64.32000  ? 121 ASP B N   1 
ATOM   1938 C CA  . ASP B 1 72  ? -1.72500  -27.22000 5.22700   1.000 63.43000  ? 121 ASP B CA  1 
ATOM   1939 C C   . ASP B 1 72  ? -1.87000  -26.25200 4.05500   1.000 69.30000  ? 121 ASP B C   1 
ATOM   1940 O O   . ASP B 1 72  ? -0.92200  -26.00200 3.30300   1.000 66.43000  ? 121 ASP B O   1 
ATOM   1941 C CB  . ASP B 1 72  ? -1.50000  -26.44700 6.53800   1.000 70.05000  ? 121 ASP B CB  1 
ATOM   1942 C CG  . ASP B 1 72  ? -2.75400  -25.74500 7.03300   1.000 81.64000  ? 121 ASP B CG  1 
ATOM   1943 O OD1 . ASP B 1 72  ? -3.83000  -25.93400 6.41800   1.000 84.61000  ? 121 ASP B OD1 1 
ATOM   1944 O OD2 . ASP B 1 72  ? -2.66300  -25.01000 8.04500   1.000 79.94000  ? 121 ASP B OD2 1 
ATOM   1945 N N   . GLU B 1 73  ? -3.07600  -25.70100 3.92400   1.000 71.67000  ? 122 GLU B N   1 
ATOM   1946 C CA  . GLU B 1 73  ? -3.35900  -24.61800 2.99200   1.000 67.27000  ? 122 GLU B CA  1 
ATOM   1947 C C   . GLU B 1 73  ? -3.12000  -23.27500 3.67500   1.000 67.12000  ? 122 GLU B C   1 
ATOM   1948 O O   . GLU B 1 73  ? -3.65900  -23.02400 4.75400   1.000 69.04000  ? 122 GLU B O   1 
ATOM   1949 C CB  . GLU B 1 73  ? -4.80500  -24.70400 2.49800   1.000 67.95000  ? 122 GLU B CB  1 
ATOM   1950 C CG  . GLU B 1 73  ? -4.99900  -24.30600 1.03300   1.000 75.96000  ? 122 GLU B CG  1 
ATOM   1951 C CD  . GLU B 1 73  ? -6.45800  -24.38600 0.56900   1.000 83.40000  ? 122 GLU B CD  1 
ATOM   1952 O OE1 . GLU B 1 73  ? -7.37500  -24.36700 1.42700   1.000 87.26000  ? 122 GLU B OE1 1 
ATOM   1953 O OE2 . GLU B 1 73  ? -6.68300  -24.49200 -0.65900  1.000 78.47000  ? 122 GLU B OE2 1 
ATOM   1954 N N   . ILE B 1 74  ? -2.30800  -22.42000 3.04900   1.000 61.93000  ? 123 ILE B N   1 
ATOM   1955 C CA  . ILE B 1 74  ? -2.02800  -21.07500 3.54100   1.000 53.77000  ? 123 ILE B CA  1 
ATOM   1956 C C   . ILE B 1 74  ? -2.78400  -20.06500 2.70000   1.000 64.29000  ? 123 ILE B C   1 
ATOM   1957 O O   . ILE B 1 74  ? -2.75800  -20.13400 1.46400   1.000 68.41000  ? 123 ILE B O   1 
ATOM   1958 C CB  . ILE B 1 74  ? -0.52700  -20.77000 3.50600   1.000 55.23000  ? 123 ILE B CB  1 
ATOM   1959 C CG1 . ILE B 1 74  ? 0.20000   -21.93500 4.13300   1.000 65.19000  ? 123 ILE B CG1 1 
ATOM   1960 C CG2 . ILE B 1 74  ? -0.23300  -19.49800 4.28400   1.000 56.28000  ? 123 ILE B CG2 1 
ATOM   1961 C CD1 . ILE B 1 74  ? -0.03300  -22.01900 5.60200   1.000 60.27000  ? 123 ILE B CD1 1 
ATOM   1962 N N   . HIS B 1 75  ? -3.44700  -19.12100 3.35900   1.000 62.42000  ? 124 HIS B N   1 
ATOM   1963 C CA  . HIS B 1 75  ? -4.18900  -18.08400 2.66200   1.000 56.25000  ? 124 HIS B CA  1 
ATOM   1964 C C   . HIS B 1 75  ? -3.48900  -16.74400 2.82600   1.000 57.88000  ? 124 HIS B C   1 
ATOM   1965 O O   . HIS B 1 75  ? -2.67500  -16.54700 3.73400   1.000 51.44000  ? 124 HIS B O   1 
ATOM   1966 C CB  . HIS B 1 75  ? -5.62400  -18.01500 3.16500   1.000 56.73000  ? 124 HIS B CB  1 
ATOM   1967 C CG  . HIS B 1 75  ? -6.29300  -19.35100 3.20500   1.000 64.13000  ? 124 HIS B CG  1 
ATOM   1968 N ND1 . HIS B 1 75  ? -6.76300  -19.97900 2.07200   1.000 63.06000  ? 124 HIS B ND1 1 
ATOM   1969 C CD2 . HIS B 1 75  ? -6.53900  -20.19500 4.23600   1.000 64.02000  ? 124 HIS B CD2 1 
ATOM   1970 C CE1 . HIS B 1 75  ? -7.28500  -21.14600 2.40300   1.000 61.95000  ? 124 HIS B CE1 1 
ATOM   1971 N NE2 . HIS B 1 75  ? -7.16200  -21.30100 3.71000   1.000 74.35000  ? 124 HIS B NE2 1 
ATOM   1972 N N   . TYR B 1 76  ? -3.80100  -15.82800 1.92000   1.000 52.36000  ? 125 TYR B N   1 
ATOM   1973 C CA  . TYR B 1 76  ? -3.14400  -14.53100 1.87400   1.000 53.74000  ? 125 TYR B CA  1 
ATOM   1974 C C   . TYR B 1 76  ? -3.90800  -13.65100 0.88600   1.000 58.08000  ? 125 TYR B C   1 
ATOM   1975 O O   . TYR B 1 76  ? -4.63900  -14.16900 0.03500   1.000 55.02000  ? 125 TYR B O   1 
ATOM   1976 C CB  . TYR B 1 76  ? -1.66900  -14.67200 1.45100   1.000 59.16000  ? 125 TYR B CB  1 
ATOM   1977 C CG  . TYR B 1 76  ? -1.49300  -15.56600 0.23800   1.000 59.27000  ? 125 TYR B CG  1 
ATOM   1978 C CD1 . TYR B 1 76  ? -1.72600  -15.07800 -1.04900  1.000 60.48000  ? 125 TYR B CD1 1 
ATOM   1979 C CD2 . TYR B 1 76  ? -1.11600  -16.89900 0.37900   1.000 57.76000  ? 125 TYR B CD2 1 
ATOM   1980 C CE1 . TYR B 1 76  ? -1.58500  -15.89500 -2.16200  1.000 58.37000  ? 125 TYR B CE1 1 
ATOM   1981 C CE2 . TYR B 1 76  ? -0.97200  -17.72300 -0.72900  1.000 57.10000  ? 125 TYR B CE2 1 
ATOM   1982 C CZ  . TYR B 1 76  ? -1.21300  -17.21300 -1.99300  1.000 57.43000  ? 125 TYR B CZ  1 
ATOM   1983 O OH  . TYR B 1 76  ? -1.07800  -18.01800 -3.09500  1.000 58.23000  ? 125 TYR B OH  1 
ATOM   1984 N N   . PRO B 1 77  ? -3.74000  -12.33500 0.96700   1.000 58.48000  ? 126 PRO B N   1 
ATOM   1985 C CA  . PRO B 1 77  ? -4.43800  -11.44100 0.02900   1.000 50.69000  ? 126 PRO B CA  1 
ATOM   1986 C C   . PRO B 1 77  ? -4.17400  -11.85300 -1.40500  1.000 60.10000  ? 126 PRO B C   1 
ATOM   1987 O O   . PRO B 1 77  ? -3.02600  -12.11700 -1.78500  1.000 59.55000  ? 126 PRO B O   1 
ATOM   1988 C CB  . PRO B 1 77  ? -3.83700  -10.06200 0.32900   1.000 54.83000  ? 126 PRO B CB  1 
ATOM   1989 C CG  . PRO B 1 77  ? -3.25700  -10.18000 1.73800   1.000 50.26000  ? 126 PRO B CG  1 
ATOM   1990 C CD  . PRO B 1 77  ? -2.93100  -11.60900 1.97500   1.000 49.47000  ? 126 PRO B CD  1 
ATOM   1991 N N   . PRO B 1 78  ? -5.22100  -11.95700 -2.21900  1.000 58.84000  ? 127 PRO B N   1 
ATOM   1992 C CA  . PRO B 1 78  ? -5.04700  -12.46900 -3.58300  1.000 59.98000  ? 127 PRO B CA  1 
ATOM   1993 C C   . PRO B 1 78  ? -4.09400  -11.66400 -4.44400  1.000 52.25000  ? 127 PRO B C   1 
ATOM   1994 O O   . PRO B 1 78  ? -3.60300  -12.19100 -5.44700  1.000 56.59000  ? 127 PRO B O   1 
ATOM   1995 C CB  . PRO B 1 78  ? -6.47400  -12.43600 -4.14500  1.000 58.69000  ? 127 PRO B CB  1 
ATOM   1996 C CG  . PRO B 1 78  ? -7.33500  -12.59700 -2.94900  1.000 57.17000  ? 127 PRO B CG  1 
ATOM   1997 C CD  . PRO B 1 78  ? -6.63800  -11.86700 -1.84000  1.000 62.10000  ? 127 PRO B CD  1 
ATOM   1998 N N   . LYS B 1 79  ? -3.80900  -10.41500 -4.11100  1.000 57.80000  ? 128 LYS B N   1 
ATOM   1999 C CA  . LYS B 1 79  ? -2.88500  -9.69300  -4.97400  1.000 66.37000  ? 128 LYS B CA  1 
ATOM   2000 C C   . LYS B 1 79  ? -1.45500  -10.19500 -4.81600  1.000 65.27000  ? 128 LYS B C   1 
ATOM   2001 O O   . LYS B 1 79  ? -0.58800  -9.80100  -5.60600  1.000 58.58000  ? 128 LYS B O   1 
ATOM   2002 C CB  . LYS B 1 79  ? -2.96800  -8.17700  -4.71600  1.000 65.80000  ? 128 LYS B CB  1 
ATOM   2003 C CG  . LYS B 1 79  ? -2.43300  -7.69400  -3.37000  1.000 60.40000  ? 128 LYS B CG  1 
ATOM   2004 C CD  . LYS B 1 79  ? -2.77600  -6.19700  -3.14300  1.000 75.83000  ? 128 LYS B CD  1 
ATOM   2005 C CE  . LYS B 1 79  ? -3.46800  -5.91200  -1.79300  1.000 66.81000  ? 128 LYS B CE  1 
ATOM   2006 N NZ  . LYS B 1 79  ? -4.81100  -6.55700  -1.63300  1.000 73.50000  ? 128 LYS B NZ  1 
ATOM   2007 N N   . LEU B 1 80  ? -1.19800  -11.02900 -3.79800  1.000 56.02000  ? 129 LEU B N   1 
ATOM   2008 C CA  . LEU B 1 80  ? 0.07500   -11.71200 -3.60700  1.000 53.39000  ? 129 LEU B CA  1 
ATOM   2009 C C   . LEU B 1 80  ? 0.23600   -12.92900 -4.51200  1.000 55.46000  ? 129 LEU B C   1 
ATOM   2010 O O   . LEU B 1 80  ? 1.36500   -13.37800 -4.72100  1.000 58.47000  ? 129 LEU B O   1 
ATOM   2011 C CB  . LEU B 1 80  ? 0.20000   -12.16400 -2.14100  1.000 55.02000  ? 129 LEU B CB  1 
ATOM   2012 C CG  . LEU B 1 80  ? 1.54900   -12.17600 -1.42000  1.000 49.06000  ? 129 LEU B CG  1 
ATOM   2013 C CD1 . LEU B 1 80  ? 2.09700   -10.77300 -1.24300  1.000 47.70000  ? 129 LEU B CD1 1 
ATOM   2014 C CD2 . LEU B 1 80  ? 1.43000   -12.85500 -0.08300  1.000 50.91000  ? 129 LEU B CD2 1 
ATOM   2015 N N   . HIS B 1 81  ? -0.86500  -13.47200 -5.03900  1.000 50.97000  ? 130 HIS B N   1 
ATOM   2016 C CA  . HIS B 1 81  ? -0.82800  -14.75400 -5.73100  1.000 48.63000  ? 130 HIS B CA  1 
ATOM   2017 C C   . HIS B 1 81  ? 0.07500   -14.71800 -6.94900  1.000 54.94000  ? 130 HIS B C   1 
ATOM   2018 O O   . HIS B 1 81  ? 0.65000   -15.74500 -7.33700  1.000 51.09000  ? 130 HIS B O   1 
ATOM   2019 C CB  . HIS B 1 81  ? -2.23300  -15.14900 -6.14500  1.000 49.75000  ? 130 HIS B CB  1 
ATOM   2020 C CG  . HIS B 1 81  ? -2.37200  -16.59800 -6.48000  1.000 55.68000  ? 130 HIS B CG  1 
ATOM   2021 N ND1 . HIS B 1 81  ? -2.28300  -17.59200 -5.52800  1.000 54.83000  ? 130 HIS B ND1 1 
ATOM   2022 C CD2 . HIS B 1 81  ? -2.62600  -17.22000 -7.65600  1.000 57.55000  ? 130 HIS B CD2 1 
ATOM   2023 C CE1 . HIS B 1 81  ? -2.46500  -18.76700 -6.10600  1.000 59.88000  ? 130 HIS B CE1 1 
ATOM   2024 N NE2 . HIS B 1 81  ? -2.67500  -18.56900 -7.39700  1.000 61.78000  ? 130 HIS B NE2 1 
ATOM   2025 N N   . CYS B 1 82  ? 0.19300   -13.55000 -7.57100  1.000 56.23000  ? 131 CYS B N   1 
ATOM   2026 C CA  . CYS B 1 82  ? 1.03900   -13.38900 -8.73800  1.000 45.98000  ? 131 CYS B CA  1 
ATOM   2027 C C   . CYS B 1 82  ? 2.48600   -13.74900 -8.45200  1.000 50.22000  ? 131 CYS B C   1 
ATOM   2028 O O   . CYS B 1 82  ? 3.23400   -14.04000 -9.39100  1.000 45.33000  ? 131 CYS B O   1 
ATOM   2029 C CB  . CYS B 1 82  ? 0.94100   -11.95000 -9.22600  1.000 49.69000  ? 131 CYS B CB  1 
ATOM   2030 S SG  . CYS B 1 82  ? 1.64300   -10.72200 -8.06800  1.000 54.98000  ? 131 CYS B SG  1 
ATOM   2031 N N   . ILE B 1 83  ? 2.91200   -13.69700 -7.18300  1.000 49.27000  ? 132 ILE B N   1 
ATOM   2032 C CA  . ILE B 1 83  ? 4.27700   -14.10200 -6.85900  1.000 48.75000  ? 132 ILE B CA  1 
ATOM   2033 C C   . ILE B 1 83  ? 4.50200   -15.57100 -7.22200  1.000 52.95000  ? 132 ILE B C   1 
ATOM   2034 O O   . ILE B 1 83  ? 5.52100   -15.93300 -7.81900  1.000 49.35000  ? 132 ILE B O   1 
ATOM   2035 C CB  . ILE B 1 83  ? 4.56100   -13.86300 -5.37700  1.000 50.64000  ? 132 ILE B CB  1 
ATOM   2036 C CG1 . ILE B 1 83  ? 4.75600   -12.38100 -5.10000  1.000 55.08000  ? 132 ILE B CG1 1 
ATOM   2037 C CG2 . ILE B 1 83  ? 5.84500   -14.54300 -5.02000  1.000 44.55000  ? 132 ILE B CG2 1 
ATOM   2038 C CD1 . ILE B 1 83  ? 4.71500   -12.07700 -3.59800  1.000 50.82000  ? 132 ILE B CD1 1 
ATOM   2039 N N   . PHE B 1 84  ? 3.53400   -16.43000 -6.91100  1.000 51.80000  ? 133 PHE B N   1 
ATOM   2040 C CA  . PHE B 1 84  ? 3.70800   -17.87200 -7.02600  1.000 55.19000  ? 133 PHE B CA  1 
ATOM   2041 C C   . PHE B 1 84  ? 3.42100   -18.43000 -8.42100  1.000 50.04000  ? 133 PHE B C   1 
ATOM   2042 O O   . PHE B 1 84  ? 3.73700   -19.60100 -8.67300  1.000 49.65000  ? 133 PHE B O   1 
ATOM   2043 C CB  . PHE B 1 84  ? 2.83300   -18.56800 -5.96800  1.000 42.30000  ? 133 PHE B CB  1 
ATOM   2044 C CG  . PHE B 1 84  ? 2.94900   -17.94600 -4.63900  1.000 54.78000  ? 133 PHE B CG  1 
ATOM   2045 C CD1 . PHE B 1 84  ? 4.12400   -18.06400 -3.91600  1.000 58.17000  ? 133 PHE B CD1 1 
ATOM   2046 C CD2 . PHE B 1 84  ? 1.91900   -17.18400 -4.12200  1.000 54.08000  ? 133 PHE B CD2 1 
ATOM   2047 C CE1 . PHE B 1 84  ? 4.25400   -17.46400 -2.69100  1.000 49.15000  ? 133 PHE B CE1 1 
ATOM   2048 C CE2 . PHE B 1 84  ? 2.04900   -16.57900 -2.89700  1.000 49.92000  ? 133 PHE B CE2 1 
ATOM   2049 C CZ  . PHE B 1 84  ? 3.22000   -16.72400 -2.17600  1.000 49.89000  ? 133 PHE B CZ  1 
ATOM   2050 N N   . LEU B 1 85  ? 2.81900   -17.64700 -9.32000  1.000 46.21000  ? 134 LEU B N   1 
ATOM   2051 C CA  . LEU B 1 85  ? 2.66600   -18.05800 -10.71300 1.000 51.60000  ? 134 LEU B CA  1 
ATOM   2052 C C   . LEU B 1 85  ? 3.52400   -17.27500 -11.68500 1.000 47.66000  ? 134 LEU B C   1 
ATOM   2053 O O   . LEU B 1 85  ? 3.79500   -17.77600 -12.78000 1.000 51.34000  ? 134 LEU B O   1 
ATOM   2054 C CB  . LEU B 1 85  ? 1.20900   -17.95100 -11.18100 1.000 50.46000  ? 134 LEU B CB  1 
ATOM   2055 C CG  . LEU B 1 85  ? 0.12500   -18.38700 -10.21100 1.000 52.66000  ? 134 LEU B CG  1 
ATOM   2056 C CD1 . LEU B 1 85  ? -1.24300  -17.92000 -10.70200 1.000 53.78000  ? 134 LEU B CD1 1 
ATOM   2057 C CD2 . LEU B 1 85  ? 0.18000   -19.89500 -10.07800 1.000 46.17000  ? 134 LEU B CD2 1 
ATOM   2058 N N   . GLY B 1 86  ? 3.92700   -16.06500 -11.33300 1.000 47.53000  ? 135 GLY B N   1 
ATOM   2059 C CA  . GLY B 1 86  ? 4.55800   -15.19100 -12.29600 1.000 52.79000  ? 135 GLY B CA  1 
ATOM   2060 C C   . GLY B 1 86  ? 6.00100   -15.56400 -12.59700 1.000 52.15000  ? 135 GLY B C   1 
ATOM   2061 O O   . GLY B 1 86  ? 6.61000   -16.41300 -11.94000 1.000 47.89000  ? 135 GLY B O   1 
ATOM   2062 N N   . ALA B 1 87  ? 6.53900   -14.89200 -13.61700 1.000 45.75000  ? 136 ALA B N   1 
ATOM   2063 C CA  . ALA B 1 87  ? 7.92000   -15.08100 -14.05100 1.000 51.05000  ? 136 ALA B CA  1 
ATOM   2064 C C   . ALA B 1 87  ? 8.21700   -16.55500 -14.33500 1.000 49.07000  ? 136 ALA B C   1 
ATOM   2065 O O   . ALA B 1 87  ? 9.25900   -17.08900 -13.94100 1.000 47.79000  ? 136 ALA B O   1 
ATOM   2066 C CB  . ALA B 1 87  ? 8.89200   -14.49700 -13.02300 1.000 33.99000  ? 136 ALA B CB  1 
ATOM   2067 N N   . GLN B 1 88  ? 7.27200   -17.22500 -14.99800 1.000 48.38000  ? 137 GLN B N   1 
ATOM   2068 C CA  . GLN B 1 88  ? 7.41300   -18.64000 -15.35000 1.000 48.64000  ? 137 GLN B CA  1 
ATOM   2069 C C   . GLN B 1 88  ? 7.80400   -19.47900 -14.12100 1.000 51.68000  ? 137 GLN B C   1 
ATOM   2070 O O   . GLN B 1 88  ? 8.66400   -20.35800 -14.17200 1.000 56.24000  ? 137 GLN B O   1 
ATOM   2071 C CB  . GLN B 1 88  ? 8.39000   -18.81300 -16.51900 1.000 51.86000  ? 137 GLN B CB  1 
ATOM   2072 C CG  . GLN B 1 88  ? 7.80700   -18.31300 -17.89900 1.000 50.81000  ? 137 GLN B CG  1 
ATOM   2073 C CD  . GLN B 1 88  ? 8.75400   -18.54000 -19.10800 1.000 68.51000  ? 137 GLN B CD  1 
ATOM   2074 O OE1 . GLN B 1 88  ? 9.98200   -18.38900 -18.99300 1.000 62.58000  ? 137 GLN B OE1 1 
ATOM   2075 N NE2 . GLN B 1 88  ? 8.17400   -18.88900 -20.27700 1.000 57.60000  ? 137 GLN B NE2 1 
ATOM   2076 N N   . GLY B 1 89  ? 7.19300   -19.16700 -12.98500 1.000 45.39000  ? 138 GLY B N   1 
ATOM   2077 C CA  . GLY B 1 89  ? 7.39700   -19.92800 -11.77900 1.000 45.43000  ? 138 GLY B CA  1 
ATOM   2078 C C   . GLY B 1 89  ? 8.66700   -19.61200 -11.02600 1.000 47.39000  ? 138 GLY B C   1 
ATOM   2079 O O   . GLY B 1 89  ? 9.00700   -20.34400 -10.09900 1.000 38.41000  ? 138 GLY B O   1 
ATOM   2080 N N   . PHE B 1 90  ? 9.36400   -18.53600 -11.38400 1.000 46.54000  ? 139 PHE B N   1 
ATOM   2081 C CA  . PHE B 1 90  ? 10.70000  -18.27900 -10.85600 1.000 45.28000  ? 139 PHE B CA  1 
ATOM   2082 C C   . PHE B 1 90  ? 10.69800  -18.14800 -9.33700  1.000 46.89000  ? 139 PHE B C   1 
ATOM   2083 O O   . PHE B 1 90  ? 11.55300  -18.71400 -8.65400  1.000 44.88000  ? 139 PHE B O   1 
ATOM   2084 C CB  . PHE B 1 90  ? 11.25500  -17.00800 -11.50200 1.000 45.40000  ? 139 PHE B CB  1 
ATOM   2085 C CG  . PHE B 1 90  ? 12.55100  -16.56400 -10.93100 1.000 47.04000  ? 139 PHE B CG  1 
ATOM   2086 C CD1 . PHE B 1 90  ? 13.68000  -17.35900 -11.05100 1.000 49.92000  ? 139 PHE B CD1 1 
ATOM   2087 C CD2 . PHE B 1 90  ? 12.64600  -15.35900 -10.25100 1.000 53.26000  ? 139 PHE B CD2 1 
ATOM   2088 C CE1 . PHE B 1 90  ? 14.89200  -16.95700 -10.52000 1.000 50.52000  ? 139 PHE B CE1 1 
ATOM   2089 C CE2 . PHE B 1 90  ? 13.85600  -14.94000 -9.70600  1.000 53.50000  ? 139 PHE B CE2 1 
ATOM   2090 C CZ  . PHE B 1 90  ? 14.98200  -15.74000 -9.84200  1.000 55.92000  ? 139 PHE B CZ  1 
ATOM   2091 N N   . PHE B 1 91  ? 9.76400   -17.37200 -8.78900  1.000 50.62000  ? 140 PHE B N   1 
ATOM   2092 C CA  . PHE B 1 91  ? 9.76700   -17.13600 -7.35000  1.000 45.97000  ? 140 PHE B CA  1 
ATOM   2093 C C   . PHE B 1 91  ? 9.31100   -18.36500 -6.58600  1.000 48.18000  ? 140 PHE B C   1 
ATOM   2094 O O   . PHE B 1 91  ? 9.83800   -18.65800 -5.50400  1.000 42.97000  ? 140 PHE B O   1 
ATOM   2095 C CB  . PHE B 1 91  ? 8.89500   -15.93300 -7.01400  1.000 37.42000  ? 140 PHE B CB  1 
ATOM   2096 C CG  . PHE B 1 91  ? 9.43100   -14.65700 -7.56800  1.000 43.84000  ? 140 PHE B CG  1 
ATOM   2097 C CD1 . PHE B 1 91  ? 10.57400  -14.08900 -7.03500  1.000 42.84000  ? 140 PHE B CD1 1 
ATOM   2098 C CD2 . PHE B 1 91  ? 8.81100   -14.04200 -8.65800  1.000 45.62000  ? 140 PHE B CD2 1 
ATOM   2099 C CE1 . PHE B 1 91  ? 11.08100  -12.91900 -7.54200  1.000 44.39000  ? 140 PHE B CE1 1 
ATOM   2100 C CE2 . PHE B 1 91  ? 9.31300   -12.88500 -9.18800  1.000 42.14000  ? 140 PHE B CE2 1 
ATOM   2101 C CZ  . PHE B 1 91  ? 10.45300  -12.31400 -8.62200  1.000 54.52000  ? 140 PHE B CZ  1 
ATOM   2102 N N   . LEU B 1 92  ? 8.32500   -19.09000 -7.12900  1.000 47.55000  ? 141 LEU B N   1 
ATOM   2103 C CA  . LEU B 1 92  ? 7.94900   -20.36500 -6.53600  1.000 48.96000  ? 141 LEU B CA  1 
ATOM   2104 C C   . LEU B 1 92  ? 9.14200   -21.29600 -6.46300  1.000 50.38000  ? 141 LEU B C   1 
ATOM   2105 O O   . LEU B 1 92  ? 9.38800   -21.91200 -5.41600  1.000 47.48000  ? 141 LEU B O   1 
ATOM   2106 C CB  . LEU B 1 92  ? 6.83100   -21.03500 -7.34100  1.000 45.54000  ? 141 LEU B CB  1 
ATOM   2107 C CG  . LEU B 1 92  ? 6.09800   -22.08300 -6.49300  1.000 47.76000  ? 141 LEU B CG  1 
ATOM   2108 C CD1 . LEU B 1 92  ? 5.64500   -21.45100 -5.20300  1.000 43.30000  ? 141 LEU B CD1 1 
ATOM   2109 C CD2 . LEU B 1 92  ? 4.92600   -22.70300 -7.20200  1.000 45.46000  ? 141 LEU B CD2 1 
ATOM   2110 N N   . ASP B 1 93  ? 9.92000   -21.36400 -7.55300  1.000 42.25000  ? 142 ASP B N   1 
ATOM   2111 C CA  . ASP B 1 93  ? 11.07200  -22.25600 -7.61600  1.000 47.23000  ? 142 ASP B CA  1 
ATOM   2112 C C   . ASP B 1 93  ? 12.13100  -21.86000 -6.59400  1.000 51.30000  ? 142 ASP B C   1 
ATOM   2113 O O   . ASP B 1 93  ? 12.73100  -22.72500 -5.94800  1.000 49.29000  ? 142 ASP B O   1 
ATOM   2114 C CB  . ASP B 1 93  ? 11.67500  -22.26600 -9.03200  1.000 45.90000  ? 142 ASP B CB  1 
ATOM   2115 C CG  . ASP B 1 93  ? 10.76200  -22.93800 -10.08000 1.000 54.08000  ? 142 ASP B CG  1 
ATOM   2116 O OD1 . ASP B 1 93  ? 9.92300   -23.80900 -9.73300  1.000 56.25000  ? 142 ASP B OD1 1 
ATOM   2117 O OD2 . ASP B 1 93  ? 10.89300  -22.59200 -11.27900 1.000 63.17000  ? 142 ASP B OD2 1 
ATOM   2118 N N   . CYS B 1 94  ? 12.38500  -20.55700 -6.43500  1.000 48.49000  ? 143 CYS B N   1 
ATOM   2119 C CA  . CYS B 1 94  ? 13.34000  -20.13400 -5.41200  1.000 48.27000  ? 143 CYS B CA  1 
ATOM   2120 C C   . CYS B 1 94  ? 12.83900  -20.46800 -4.01600  1.000 49.66000  ? 143 CYS B C   1 
ATOM   2121 O O   . CYS B 1 94  ? 13.62900  -20.78800 -3.12100  1.000 47.31000  ? 143 CYS B O   1 
ATOM   2122 C CB  . CYS B 1 94  ? 13.60800  -18.63900 -5.50100  1.000 40.38000  ? 143 CYS B CB  1 
ATOM   2123 S SG  . CYS B 1 94  ? 14.38800  -18.11000 -7.04900  1.000 54.73000  ? 143 CYS B SG  1 
ATOM   2124 N N   . LEU B 1 95  ? 11.53500  -20.38600 -3.80500  1.000 47.49000  ? 144 LEU B N   1 
ATOM   2125 C CA  . LEU B 1 95  ? 11.01200  -20.68500 -2.48900  1.000 50.45000  ? 144 LEU B CA  1 
ATOM   2126 C C   . LEU B 1 95  ? 11.18700  -22.16700 -2.17500  1.000 55.48000  ? 144 LEU B C   1 
ATOM   2127 O O   . LEU B 1 95  ? 11.59500  -22.53500 -1.06400  1.000 49.60000  ? 144 LEU B O   1 
ATOM   2128 C CB  . LEU B 1 95  ? 9.56100   -20.23000 -2.44200  1.000 49.51000  ? 144 LEU B CB  1 
ATOM   2129 C CG  . LEU B 1 95  ? 8.85800   -20.07200 -1.11400  1.000 60.57000  ? 144 LEU B CG  1 
ATOM   2130 C CD1 . LEU B 1 95  ? 9.80700   -19.53700 -0.06600  1.000 57.33000  ? 144 LEU B CD1 1 
ATOM   2131 C CD2 . LEU B 1 95  ? 7.74100   -19.09100 -1.35900  1.000 66.05000  ? 144 LEU B CD2 1 
ATOM   2132 N N   . ALA B 1 96  ? 10.94800  -23.02800 -3.16700  1.000 52.16000  ? 145 ALA B N   1 
ATOM   2133 C CA  . ALA B 1 96  ? 11.21900  -24.44800 -2.98400  1.000 45.29000  ? 145 ALA B CA  1 
ATOM   2134 C C   . ALA B 1 96  ? 12.70900  -24.70300 -2.81100  1.000 42.54000  ? 145 ALA B C   1 
ATOM   2135 O O   . ALA B 1 96  ? 13.11400  -25.54800 -2.00800  1.000 47.91000  ? 145 ALA B O   1 
ATOM   2136 C CB  . ALA B 1 96  ? 10.66700  -25.24700 -4.15900  1.000 51.09000  ? 145 ALA B CB  1 
ATOM   2137 N N   . TRP B 1 97  ? 13.54600  -24.00200 -3.56600  1.000 45.20000  ? 146 TRP B N   1 
ATOM   2138 C CA  . TRP B 1 97  ? 14.98100  -24.17200 -3.37000  1.000 49.52000  ? 146 TRP B CA  1 
ATOM   2139 C C   . TRP B 1 97  ? 15.39700  -23.75800 -1.95800  1.000 49.41000  ? 146 TRP B C   1 
ATOM   2140 O O   . TRP B 1 97  ? 16.18200  -24.45100 -1.30500  1.000 45.89000  ? 146 TRP B O   1 
ATOM   2141 C CB  . TRP B 1 97  ? 15.76500  -23.38100 -4.42700  1.000 37.68000  ? 146 TRP B CB  1 
ATOM   2142 C CG  . TRP B 1 97  ? 17.18700  -23.22600 -4.03200  1.000 48.01000  ? 146 TRP B CG  1 
ATOM   2143 C CD1 . TRP B 1 97  ? 17.73400  -22.19200 -3.31800  1.000 49.92000  ? 146 TRP B CD1 1 
ATOM   2144 C CD2 . TRP B 1 97  ? 18.24400  -24.15600 -4.26100  1.000 44.03000  ? 146 TRP B CD2 1 
ATOM   2145 N NE1 . TRP B 1 97  ? 19.07200  -22.41300 -3.11400  1.000 51.33000  ? 146 TRP B NE1 1 
ATOM   2146 C CE2 . TRP B 1 97  ? 19.41400  -23.61000 -3.68300  1.000 42.50000  ? 146 TRP B CE2 1 
ATOM   2147 C CE3 . TRP B 1 97  ? 18.32500  -25.39000 -4.91800  1.000 41.21000  ? 146 TRP B CE3 1 
ATOM   2148 C CZ2 . TRP B 1 97  ? 20.64600  -24.25500 -3.73700  1.000 44.61000  ? 146 TRP B CZ2 1 
ATOM   2149 C CZ3 . TRP B 1 97  ? 19.56200  -26.03100 -4.98700  1.000 43.92000  ? 146 TRP B CZ3 1 
ATOM   2150 C CH2 . TRP B 1 97  ? 20.70400  -25.46100 -4.39600  1.000 50.21000  ? 146 TRP B CH2 1 
ATOM   2151 N N   . SER B 1 98  ? 14.86200  -22.63800 -1.47100  1.000 47.18000  ? 147 SER B N   1 
ATOM   2152 C CA  . SER B 1 98  ? 15.23800  -22.11500 -0.16400  1.000 49.08000  ? 147 SER B CA  1 
ATOM   2153 C C   . SER B 1 98  ? 14.82700  -23.05400 0.96500   1.000 52.00000  ? 147 SER B C   1 
ATOM   2154 O O   . SER B 1 98  ? 15.53600  -23.16100 1.97700   1.000 50.33000  ? 147 SER B O   1 
ATOM   2155 C CB  . SER B 1 98  ? 14.58800  -20.74100 0.04100   1.000 51.78000  ? 147 SER B CB  1 
ATOM   2156 O OG  . SER B 1 98  ? 15.33400  -19.91500 0.92600   1.000 63.90000  ? 147 SER B OG  1 
ATOM   2157 N N   . THR B 1 99  ? 13.66800  -23.71600 0.82200   1.000 49.97000  ? 148 THR B N   1 
ATOM   2158 C CA  . THR B 1 99  ? 13.00800  -24.42500 1.91700   1.000 51.98000  ? 148 THR B CA  1 
ATOM   2159 C C   . THR B 1 99  ? 12.86400  -25.92600 1.72600   1.000 50.62000  ? 148 THR B C   1 
ATOM   2160 O O   . THR B 1 99  ? 12.67000  -26.62700 2.72100   1.000 51.38000  ? 148 THR B O   1 
ATOM   2161 C CB  . THR B 1 99  ? 11.58900  -23.87000 2.16500   1.000 53.77000  ? 148 THR B CB  1 
ATOM   2162 O OG1 . THR B 1 99  ? 10.76400  -24.12000 1.01800   1.000 46.16000  ? 148 THR B OG1 1 
ATOM   2163 C CG2 . THR B 1 99  ? 11.61200  -22.37600 2.47900   1.000 45.04000  ? 148 THR B CG2 1 
ATOM   2164 N N   . SER B 1 100 ? 12.90200  -26.43200 0.49200   1.000 52.74000  ? 149 SER B N   1 
ATOM   2165 C CA  . SER B 1 100 ? 12.62300  -27.83900 0.18100   1.000 51.12000  ? 149 SER B CA  1 
ATOM   2166 C C   . SER B 1 100 ? 11.20000  -28.25400 0.56700   1.000 53.90000  ? 149 SER B C   1 
ATOM   2167 O O   . SER B 1 100 ? 10.92900  -29.44800 0.74800   1.000 50.74000  ? 149 SER B O   1 
ATOM   2168 C CB  . SER B 1 100 ? 13.63800  -28.78200 0.83600   1.000 46.49000  ? 149 SER B CB  1 
ATOM   2169 O OG  . SER B 1 100 ? 14.95000  -28.37500 0.50800   1.000 46.26000  ? 149 SER B OG  1 
ATOM   2170 N N   . ALA B 1 101 ? 10.29100  -27.28900 0.71200   1.000 49.88000  ? 150 ALA B N   1 
ATOM   2171 C CA  . ALA B 1 101 ? 8.87600   -27.57400 0.88400   1.000 52.72000  ? 150 ALA B CA  1 
ATOM   2172 C C   . ALA B 1 101 ? 8.22100   -27.72000 -0.48900  1.000 50.90000  ? 150 ALA B C   1 
ATOM   2173 O O   . ALA B 1 101 ? 8.62800   -27.07100 -1.45100  1.000 47.84000  ? 150 ALA B O   1 
ATOM   2174 C CB  . ALA B 1 101 ? 8.19400   -26.45300 1.67500   1.000 42.45000  ? 150 ALA B CB  1 
ATOM   2175 N N   . HIS B 1 102 ? 7.20500   -28.57900 -0.57000  1.000 48.17000  ? 151 HIS B N   1 
ATOM   2176 C CA  . HIS B 1 102 ? 6.41900   -28.77900 -1.78300  1.000 44.56000  ? 151 HIS B CA  1 
ATOM   2177 C C   . HIS B 1 102 ? 5.30200   -27.73900 -1.82100  1.000 51.59000  ? 151 HIS B C   1 
ATOM   2178 O O   . HIS B 1 102 ? 4.47200   -27.68300 -0.90600  1.000 54.80000  ? 151 HIS B O   1 
ATOM   2179 C CB  . HIS B 1 102 ? 5.86400   -30.20300 -1.81600  1.000 46.38000  ? 151 HIS B CB  1 
ATOM   2180 C CG  . HIS B 1 102 ? 5.07800   -30.53800 -3.04700  1.000 53.42000  ? 151 HIS B CG  1 
ATOM   2181 N ND1 . HIS B 1 102 ? 5.60700   -30.45800 -4.31900  1.000 61.50000  ? 151 HIS B ND1 1 
ATOM   2182 C CD2 . HIS B 1 102 ? 3.81100   -30.99800 -3.19800  1.000 54.91000  ? 151 HIS B CD2 1 
ATOM   2183 C CE1 . HIS B 1 102 ? 4.69100   -30.82800 -5.20000  1.000 58.39000  ? 151 HIS B CE1 1 
ATOM   2184 N NE2 . HIS B 1 102 ? 3.59300   -31.16100 -4.54600  1.000 54.66000  ? 151 HIS B NE2 1 
ATOM   2185 N N   . LEU B 1 103 ? 5.30500   -26.89500 -2.85400  1.000 46.88000  ? 152 LEU B N   1 
ATOM   2186 C CA  . LEU B 1 103 ? 4.41800   -25.73900 -2.94100  1.000 51.47000  ? 152 LEU B CA  1 
ATOM   2187 C C   . LEU B 1 103 ? 3.51500   -25.87800 -4.16100  1.000 50.32000  ? 152 LEU B C   1 
ATOM   2188 O O   . LEU B 1 103 ? 4.00200   -25.93700 -5.29700  1.000 52.84000  ? 152 LEU B O   1 
ATOM   2189 C CB  . LEU B 1 103 ? 5.22200   -24.43700 -3.02600  1.000 43.17000  ? 152 LEU B CB  1 
ATOM   2190 C CG  . LEU B 1 103 ? 6.27300   -24.27500 -1.93600  1.000 50.10000  ? 152 LEU B CG  1 
ATOM   2191 C CD1 . LEU B 1 103 ? 7.31700   -23.27300 -2.35600  1.000 55.25000  ? 152 LEU B CD1 1 
ATOM   2192 C CD2 . LEU B 1 103 ? 5.61900   -23.86200 -0.61600  1.000 47.92000  ? 152 LEU B CD2 1 
ATOM   2193 N N   . VAL B 1 104 ? 2.20600   -25.91000 -3.92700  1.000 51.77000  ? 153 VAL B N   1 
ATOM   2194 C CA  A VAL B 1 104 ? 1.21900   -26.04800 -4.99500  0.740 53.01000  ? 153 VAL B CA  1 
ATOM   2195 C CA  B VAL B 1 104 ? 1.24800   -26.02100 -5.02200  0.260 53.05000  ? 153 VAL B CA  1 
ATOM   2196 C C   . VAL B 1 104 ? 0.22400   -24.89900 -4.87700  1.000 53.63000  ? 153 VAL B C   1 
ATOM   2197 O O   . VAL B 1 104 ? -0.58600  -24.89100 -3.93700  1.000 54.77000  ? 153 VAL B O   1 
ATOM   2198 C CB  A VAL B 1 104 ? 0.49000   -27.40300 -4.92300  0.740 54.81000  ? 153 VAL B CB  1 
ATOM   2199 C CB  B VAL B 1 104 ? 0.60600   -27.42200 -5.06400  0.260 54.72000  ? 153 VAL B CB  1 
ATOM   2200 C CG1 A VAL B 1 104 ? -0.66900  -27.43100 -5.90200  0.740 51.13000  ? 153 VAL B CG1 1 
ATOM   2201 C CG1 B VAL B 1 104 ? 0.75700   -28.13200 -3.72200  0.260 53.70000  ? 153 VAL B CG1 1 
ATOM   2202 C CG2 A VAL B 1 104 ? 1.43800   -28.56600 -5.19200  0.740 47.58000  ? 153 VAL B CG2 1 
ATOM   2203 C CG2 B VAL B 1 104 ? -0.85000  -27.37800 -5.53700  0.260 53.93000  ? 153 VAL B CG2 1 
ATOM   2204 N N   . PRO B 1 105 ? 0.25300   -23.91300 -5.77300  1.000 56.67000  ? 154 PRO B N   1 
ATOM   2205 C CA  . PRO B 1 105 ? -0.74200  -22.83700 -5.73000  1.000 55.38000  ? 154 PRO B CA  1 
ATOM   2206 C C   . PRO B 1 105 ? -2.14400  -23.34300 -6.03700  1.000 56.87000  ? 154 PRO B C   1 
ATOM   2207 O O   . PRO B 1 105 ? -2.34400  -24.24800 -6.85200  1.000 54.21000  ? 154 PRO B O   1 
ATOM   2208 C CB  . PRO B 1 105 ? -0.25200  -21.87900 -6.81800  1.000 59.28000  ? 154 PRO B CB  1 
ATOM   2209 C CG  . PRO B 1 105 ? 1.23300   -22.12200 -6.85800  1.000 52.67000  ? 154 PRO B CG  1 
ATOM   2210 C CD  . PRO B 1 105 ? 1.34200   -23.60500 -6.71000  1.000 47.86000  ? 154 PRO B CD  1 
ATOM   2211 N N   . ARG B 1 106 ? -3.13100  -22.73600 -5.37400  1.000 57.20000  ? 155 ARG B N   1 
ATOM   2212 C CA  . ARG B 1 106 ? -4.51100  -23.11700 -5.64800  1.000 66.82000  ? 155 ARG B CA  1 
ATOM   2213 C C   . ARG B 1 106 ? -5.30700  -21.91200 -6.12400  1.000 67.23000  ? 155 ARG B C   1 
ATOM   2214 O O   . ARG B 1 106 ? -4.80400  -21.11000 -6.91400  1.000 69.01000  ? 155 ARG B O   1 
ATOM   2215 C CB  . ARG B 1 106 ? -5.15200  -23.76000 -4.42200  1.000 59.83000  ? 155 ARG B CB  1 
ATOM   2216 C CG  . ARG B 1 106 ? -4.54200  -25.11700 -4.10300  1.000 70.68000  ? 155 ARG B CG  1 
ATOM   2217 C CD  . ARG B 1 106 ? -5.42400  -26.26700 -4.55600  1.000 86.09000  ? 155 ARG B CD  1 
ATOM   2218 N NE  . ARG B 1 106 ? -5.40000  -27.37600 -3.60800  1.000 97.77000  ? 155 ARG B NE  1 
ATOM   2219 C CZ  . ARG B 1 106 ? -6.24100  -27.50400 -2.58500  1.000 98.83000  ? 155 ARG B CZ  1 
ATOM   2220 N NH1 . ARG B 1 106 ? -7.11300  -26.55100 -2.28000  1.000 96.23000  ? 155 ARG B NH1 1 
ATOM   2221 N NH2 . ARG B 1 106 ? -6.20200  -28.61000 -1.84400  1.000 86.47000  ? 155 ARG B NH2 1 
ATOM   2222 N N   . ALA B 1 107 ? -6.55100  -21.79400 -5.68700  1.000 68.73000  ? 156 ALA B N   1 
ATOM   2223 C CA  . ALA B 1 107 ? -7.31700  -20.61300 -6.04200  1.000 71.63000  ? 156 ALA B CA  1 
ATOM   2224 C C   . ALA B 1 107 ? -6.57300  -19.36900 -5.56200  1.000 71.44000  ? 156 ALA B C   1 
ATOM   2225 O O   . ALA B 1 107 ? -5.91800  -19.40600 -4.50800  1.000 66.27000  ? 156 ALA B O   1 
ATOM   2226 C CB  . ALA B 1 107 ? -8.72000  -20.67000 -5.43700  1.000 62.99000  ? 156 ALA B CB  1 
ATOM   2227 N N   . PRO B 1 108 ? -6.57200  -18.29300 -6.35200  1.000 69.32000  ? 157 PRO B N   1 
ATOM   2228 C CA  . PRO B 1 108 ? -5.83100  -17.08100 -5.98000  1.000 60.36000  ? 157 PRO B CA  1 
ATOM   2229 C C   . PRO B 1 108 ? -6.09400  -16.69500 -4.53800  1.000 63.14000  ? 157 PRO B C   1 
ATOM   2230 O O   . PRO B 1 108 ? -7.24100  -16.61000 -4.09700  1.000 70.25000  ? 157 PRO B O   1 
ATOM   2231 C CB  . PRO B 1 108 ? -6.35800  -16.02200 -6.95200  1.000 57.78000  ? 157 PRO B CB  1 
ATOM   2232 C CG  . PRO B 1 108 ? -7.02600  -16.79200 -8.08300  1.000 70.79000  ? 157 PRO B CG  1 
ATOM   2233 C CD  . PRO B 1 108 ? -7.00800  -18.26900 -7.75800  1.000 65.83000  ? 157 PRO B CD  1 
ATOM   2234 N N   . GLY B 1 109 ? -5.01000  -16.52500 -3.79000  1.000 62.20000  ? 158 GLY B N   1 
ATOM   2235 C CA  . GLY B 1 109 ? -5.07400  -16.24700 -2.37500  1.000 59.41000  ? 158 GLY B CA  1 
ATOM   2236 C C   . GLY B 1 109 ? -4.71700  -17.42400 -1.51300  1.000 55.22000  ? 158 GLY B C   1 
ATOM   2237 O O   . GLY B 1 109 ? -4.69500  -17.28700 -0.28700  1.000 61.09000  ? 158 GLY B O   1 
ATOM   2238 N N   . SER B 1 110 ? -4.39500  -18.56700 -2.10200  1.000 58.44000  ? 159 SER B N   1 
ATOM   2239 C CA  . SER B 1 110 ? -4.26100  -19.77800 -1.31000  1.000 59.06000  ? 159 SER B CA  1 
ATOM   2240 C C   . SER B 1 110 ? -3.15700  -20.64700 -1.90000  1.000 61.37000  ? 159 SER B C   1 
ATOM   2241 O O   . SER B 1 110 ? -3.09900  -20.83700 -3.11900  1.000 60.15000  ? 159 SER B O   1 
ATOM   2242 C CB  . SER B 1 110 ? -5.60500  -20.50400 -1.27200  1.000 52.02000  ? 159 SER B CB  1 
ATOM   2243 O OG  . SER B 1 110 ? -5.45600  -21.83400 -0.86900  1.000 67.42000  ? 159 SER B OG  1 
ATOM   2244 N N   . LEU B 1 111 ? -2.29800  -21.18900 -1.02900  1.000 62.28000  ? 160 LEU B N   1 
ATOM   2245 C CA  . LEU B 1 111 ? -1.12200  -21.95300 -1.44500  1.000 62.48000  ? 160 LEU B CA  1 
ATOM   2246 C C   . LEU B 1 111 ? -0.98200  -23.19500 -0.57000  1.000 60.92000  ? 160 LEU B C   1 
ATOM   2247 O O   . LEU B 1 111 ? -0.91700  -23.09400 0.65700   1.000 55.59000  ? 160 LEU B O   1 
ATOM   2248 C CB  . LEU B 1 111 ? 0.14100   -21.09000 -1.35000  1.000 59.58000  ? 160 LEU B CB  1 
ATOM   2249 C CG  . LEU B 1 111 ? 1.48200   -21.72700 -1.69700  1.000 58.71000  ? 160 LEU B CG  1 
ATOM   2250 C CD1 . LEU B 1 111 ? 1.58500   -21.85600 -3.20200  1.000 55.05000  ? 160 LEU B CD1 1 
ATOM   2251 C CD2 . LEU B 1 111 ? 2.64300   -20.90300 -1.13700  1.000 53.93000  ? 160 LEU B CD2 1 
ATOM   2252 N N   . MET B 1 112 ? -0.91900  -24.36100 -1.20200  1.000 59.71000  ? 161 MET B N   1 
ATOM   2253 C CA  . MET B 1 112 ? -0.75800  -25.61300 -0.47800  1.000 51.51000  ? 161 MET B CA  1 
ATOM   2254 C C   . MET B 1 112 ? 0.71600   -25.85000 -0.18800  1.000 57.44000  ? 161 MET B C   1 
ATOM   2255 O O   . MET B 1 112 ? 1.55200   -25.79700 -1.10100  1.000 55.30000  ? 161 MET B O   1 
ATOM   2256 C CB  . MET B 1 112 ? -1.33400  -26.76700 -1.29700  1.000 53.54000  ? 161 MET B CB  1 
ATOM   2257 C CG  . MET B 1 112 ? -1.30200  -28.10400 -0.58600  1.000 69.32000  ? 161 MET B CG  1 
ATOM   2258 S SD  . MET B 1 112 ? -2.46300  -28.10000 0.79500   1.000 95.04000  ? 161 MET B SD  1 
ATOM   2259 C CE  . MET B 1 112 ? -3.91400  -27.45300 -0.05600  1.000 71.18000  ? 161 MET B CE  1 
ATOM   2260 N N   . ILE B 1 113 ? 1.03500   -26.10800 1.08000   1.000 55.40000  ? 162 ILE B N   1 
ATOM   2261 C CA  . ILE B 1 113 ? 2.40900   -26.29400 1.53700   1.000 47.84000  ? 162 ILE B CA  1 
ATOM   2262 C C   . ILE B 1 113 ? 2.51000   -27.62800 2.26000   1.000 51.86000  ? 162 ILE B C   1 
ATOM   2263 O O   . ILE B 1 113 ? 1.69900   -27.92300 3.14400   1.000 59.57000  ? 162 ILE B O   1 
ATOM   2264 C CB  . ILE B 1 113 ? 2.85200   -25.14500 2.45600   1.000 47.98000  ? 162 ILE B CB  1 
ATOM   2265 C CG1 . ILE B 1 113 ? 2.73900   -23.81600 1.70100   1.000 53.13000  ? 162 ILE B CG1 1 
ATOM   2266 C CG2 . ILE B 1 113 ? 4.25200   -25.39400 2.99400   1.000 45.15000  ? 162 ILE B CG2 1 
ATOM   2267 C CD1 . ILE B 1 113 ? 3.30400   -22.62700 2.44200   1.000 51.40000  ? 162 ILE B CD1 1 
ATOM   2268 N N   . SER B 1 114 ? 3.51200   -28.42400 1.89900   1.000 53.65000  ? 163 SER B N   1 
ATOM   2269 C CA  . SER B 1 114 ? 3.74700   -29.70400 2.54800   1.000 55.51000  ? 163 SER B CA  1 
ATOM   2270 C C   . SER B 1 114 ? 5.23900   -30.00500 2.52500   1.000 58.76000  ? 163 SER B C   1 
ATOM   2271 O O   . SER B 1 114 ? 5.96300   -29.53300 1.64200   1.000 56.15000  ? 163 SER B O   1 
ATOM   2272 C CB  . SER B 1 114 ? 2.96600   -30.82100 1.84900   1.000 48.04000  ? 163 SER B CB  1 
ATOM   2273 O OG  . SER B 1 114 ? 3.59800   -31.16200 0.63400   1.000 50.15000  ? 163 SER B OG  1 
ATOM   2274 N N   . GLY B 1 115 ? 5.69300   -30.79300 3.49600   1.000 55.43000  ? 164 GLY B N   1 
ATOM   2275 C CA  . GLY B 1 115 ? 7.06600   -31.27100 3.48200   1.000 49.95000  ? 164 GLY B CA  1 
ATOM   2276 C C   . GLY B 1 115 ? 7.50000   -31.74500 4.85800   1.000 52.58000  ? 164 GLY B C   1 
ATOM   2277 O O   . GLY B 1 115 ? 6.67800   -31.96400 5.74600   1.000 57.15000  ? 164 GLY B O   1 
ATOM   2278 N N   . LEU B 1 116 ? 8.80800   -31.90300 5.00900   1.000 55.11000  ? 165 LEU B N   1 
ATOM   2279 C CA  . LEU B 1 116 ? 9.33400   -32.19700 6.33200   1.000 48.75000  ? 165 LEU B CA  1 
ATOM   2280 C C   . LEU B 1 116 ? 9.05900   -31.01700 7.25800   1.000 54.91000  ? 165 LEU B C   1 
ATOM   2281 O O   . LEU B 1 116 ? 8.85700   -29.88600 6.81500   1.000 56.42000  ? 165 LEU B O   1 
ATOM   2282 C CB  . LEU B 1 116 ? 10.83100  -32.49900 6.26600   1.000 46.90000  ? 165 LEU B CB  1 
ATOM   2283 C CG  . LEU B 1 116 ? 11.24700  -33.65500 5.34000   1.000 52.15000  ? 165 LEU B CG  1 
ATOM   2284 C CD1 . LEU B 1 116 ? 12.75900  -33.77200 5.26800   1.000 46.37000  ? 165 LEU B CD1 1 
ATOM   2285 C CD2 . LEU B 1 116 ? 10.60100  -34.98900 5.69300   1.000 42.22000  ? 165 LEU B CD2 1 
ATOM   2286 N N   . THR B 1 117 ? 9.05900   -31.30000 8.56200   1.000 59.90000  ? 166 THR B N   1 
ATOM   2287 C CA  . THR B 1 117 ? 8.62100   -30.33000 9.56700   1.000 56.14000  ? 166 THR B CA  1 
ATOM   2288 C C   . THR B 1 117 ? 9.29800   -28.97500 9.40500   1.000 50.94000  ? 166 THR B C   1 
ATOM   2289 O O   . THR B 1 117 ? 8.62800   -27.93700 9.33700   1.000 51.31000  ? 166 THR B O   1 
ATOM   2290 C CB  . THR B 1 117 ? 8.85700   -30.89900 10.96700  1.000 56.68000  ? 166 THR B CB  1 
ATOM   2291 O OG1 . THR B 1 117 ? 8.21200   -32.17500 11.06600  1.000 50.32000  ? 166 THR B OG1 1 
ATOM   2292 C CG2 . THR B 1 117 ? 8.26900   -29.97900 12.03700  1.000 60.84000  ? 166 THR B CG2 1 
ATOM   2293 N N   . GLU B 1 118 ? 10.62600  -28.95900 9.34100   1.000 50.18000  ? 167 GLU B N   1 
ATOM   2294 C CA  . GLU B 1 118 ? 11.31100  -27.67400 9.23300   1.000 56.79000  ? 167 GLU B CA  1 
ATOM   2295 C C   . GLU B 1 118 ? 11.10500  -27.01500 7.86200   1.000 56.34000  ? 167 GLU B C   1 
ATOM   2296 O O   . GLU B 1 118 ? 11.01800  -25.78100 7.77800   1.000 54.31000  ? 167 GLU B O   1 
ATOM   2297 C CB  . GLU B 1 118 ? 12.79100  -27.85700 9.55200   1.000 45.12000  ? 167 GLU B CB  1 
ATOM   2298 C CG  . GLU B 1 118 ? 13.00700  -28.22000 11.00300  1.000 60.35000  ? 167 GLU B CG  1 
ATOM   2299 C CD  . GLU B 1 118 ? 14.46300  -28.36500 11.37400  1.000 69.66000  ? 167 GLU B CD  1 
ATOM   2300 O OE1 . GLU B 1 118 ? 15.22500  -27.44300 10.98400  1.000 62.08000  ? 167 GLU B OE1 1 
ATOM   2301 O OE2 . GLU B 1 118 ? 14.82600  -29.36100 12.07000  1.000 62.08000  ? 167 GLU B OE2 1 
ATOM   2302 N N   . ALA B 1 119 ? 11.00500  -27.80600 6.78700   1.000 52.43000  ? 168 ALA B N   1 
ATOM   2303 C CA  . ALA B 1 119 ? 10.74000  -27.23700 5.46200   1.000 50.49000  ? 168 ALA B CA  1 
ATOM   2304 C C   . ALA B 1 119 ? 9.39500   -26.51400 5.43300   1.000 50.02000  ? 168 ALA B C   1 
ATOM   2305 O O   . ALA B 1 119 ? 9.29100   -25.37800 4.94800   1.000 45.25000  ? 168 ALA B O   1 
ATOM   2306 C CB  . ALA B 1 119 ? 10.77600  -28.34100 4.39800   1.000 45.88000  ? 168 ALA B CB  1 
ATOM   2307 N N   . PHE B 1 120 ? 8.35200   -27.17600 5.93500   1.000 50.49000  ? 169 PHE B N   1 
ATOM   2308 C CA  . PHE B 1 120 ? 7.04300   -26.55500 6.06800   1.000 50.67000  ? 169 PHE B CA  1 
ATOM   2309 C C   . PHE B 1 120 ? 7.11500   -25.25300 6.85400   1.000 50.17000  ? 169 PHE B C   1 
ATOM   2310 O O   . PHE B 1 120 ? 6.58800   -24.22500 6.42600   1.000 52.13000  ? 169 PHE B O   1 
ATOM   2311 C CB  . PHE B 1 120 ? 6.07700   -27.50900 6.76200   1.000 50.67000  ? 169 PHE B CB  1 
ATOM   2312 C CG  . PHE B 1 120 ? 4.75100   -26.89900 7.01500   1.000 56.30000  ? 169 PHE B CG  1 
ATOM   2313 C CD1 . PHE B 1 120 ? 4.51300   -26.17400 8.17600   1.000 56.11000  ? 169 PHE B CD1 1 
ATOM   2314 C CD2 . PHE B 1 120 ? 3.74400   -27.01300 6.07000   1.000 55.40000  ? 169 PHE B CD2 1 
ATOM   2315 C CE1 . PHE B 1 120 ? 3.28300   -25.57300 8.39700   1.000 56.83000  ? 169 PHE B CE1 1 
ATOM   2316 C CE2 . PHE B 1 120 ? 2.51200   -26.42800 6.28200   1.000 61.76000  ? 169 PHE B CE2 1 
ATOM   2317 C CZ  . PHE B 1 120 ? 2.27900   -25.69800 7.45400   1.000 56.15000  ? 169 PHE B CZ  1 
ATOM   2318 N N   . VAL B 1 121 ? 7.71100   -25.29300 8.04200   1.000 54.46000  ? 170 VAL B N   1 
ATOM   2319 C CA  . VAL B 1 121 ? 7.72600   -24.10100 8.88600   1.000 55.09000  ? 170 VAL B CA  1 
ATOM   2320 C C   . VAL B 1 121 ? 8.43500   -22.95900 8.17000   1.000 52.10000  ? 170 VAL B C   1 
ATOM   2321 O O   . VAL B 1 121 ? 8.00100   -21.80200 8.22100   1.000 54.75000  ? 170 VAL B O   1 
ATOM   2322 C CB  . VAL B 1 121 ? 8.37800   -24.41800 10.24800  1.000 55.74000  ? 170 VAL B CB  1 
ATOM   2323 C CG1 . VAL B 1 121 ? 8.69000   -23.14300 11.01400  1.000 44.63000  ? 170 VAL B CG1 1 
ATOM   2324 C CG2 . VAL B 1 121 ? 7.45200   -25.28900 11.06200  1.000 51.48000  ? 170 VAL B CG2 1 
ATOM   2325 N N   . MET B 1 122 ? 9.50300   -23.27300 7.44700   1.000 44.14000  ? 171 MET B N   1 
ATOM   2326 C CA  . MET B 1 122 ? 10.28400  -22.21300 6.83000   1.000 48.13000  ? 171 MET B CA  1 
ATOM   2327 C C   . MET B 1 122 ? 9.52000   -21.56700 5.66900   1.000 55.94000  ? 171 MET B C   1 
ATOM   2328 O O   . MET B 1 122 ? 9.52500   -20.34000 5.52200   1.000 56.40000  ? 171 MET B O   1 
ATOM   2329 C CB  . MET B 1 122 ? 11.63000  -22.80300 6.42500   1.000 43.48000  ? 171 MET B CB  1 
ATOM   2330 C CG  . MET B 1 122 ? 12.72600  -21.79800 6.26500   1.000 61.35000  ? 171 MET B CG  1 
ATOM   2331 S SD  . MET B 1 122 ? 14.24400  -22.59600 5.69200   1.000 80.85000  ? 171 MET B SD  1 
ATOM   2332 C CE  . MET B 1 122 ? 14.90500  -21.29200 4.62800   1.000 68.41000  ? 171 MET B CE  1 
ATOM   2333 N N   . ALA B 1 123 ? 8.79400   -22.37300 4.88200   1.000 49.19000  ? 172 ALA B N   1 
ATOM   2334 C CA  . ALA B 1 123 ? 8.01100   -21.84000 3.77400   1.000 51.33000  ? 172 ALA B CA  1 
ATOM   2335 C C   . ALA B 1 123 ? 6.81100   -21.04200 4.27000   1.000 49.65000  ? 172 ALA B C   1 
ATOM   2336 O O   . ALA B 1 123 ? 6.50000   -19.97100 3.73100   1.000 44.32000  ? 172 ALA B O   1 
ATOM   2337 C CB  . ALA B 1 123 ? 7.54700   -22.98100 2.86500   1.000 53.03000  ? 172 ALA B CB  1 
ATOM   2338 N N   . GLN B 1 124 ? 6.11800   -21.55600 5.28500   1.000 52.13000  ? 173 GLN B N   1 
ATOM   2339 C CA  . GLN B 1 124 ? 5.00500   -20.82000 5.87500   1.000 51.37000  ? 173 GLN B CA  1 
ATOM   2340 C C   . GLN B 1 124 ? 5.46200   -19.47000 6.41700   1.000 54.49000  ? 173 GLN B C   1 
ATOM   2341 O O   . GLN B 1 124 ? 4.81600   -18.44300 6.16600   1.000 55.16000  ? 173 GLN B O   1 
ATOM   2342 C CB  . GLN B 1 124 ? 4.38800   -21.64500 6.99600   1.000 50.94000  ? 173 GLN B CB  1 
ATOM   2343 C CG  . GLN B 1 124 ? 3.73500   -20.82300 8.08500   1.000 54.14000  ? 173 GLN B CG  1 
ATOM   2344 C CD  . GLN B 1 124 ? 2.59000   -21.55100 8.71400   1.000 62.90000  ? 173 GLN B CD  1 
ATOM   2345 O OE1 . GLN B 1 124 ? 1.45700   -21.46700 8.25200   1.000 64.49000  ? 173 GLN B OE1 1 
ATOM   2346 N NE2 . GLN B 1 124 ? 2.88500   -22.30500 9.78200   1.000 66.56000  ? 173 GLN B NE2 1 
ATOM   2347 N N   . SER B 1 125 ? 6.60300   -19.44200 7.12300   1.000 43.93000  ? 174 SER B N   1 
ATOM   2348 C CA  . SER B 1 125 ? 7.08700   -18.17900 7.67400   1.000 45.80000  ? 174 SER B CA  1 
ATOM   2349 C C   . SER B 1 125 ? 7.37000   -17.17800 6.57600   1.000 52.11000  ? 174 SER B C   1 
ATOM   2350 O O   . SER B 1 125 ? 7.03200   -15.99500 6.70400   1.000 54.77000  ? 174 SER B O   1 
ATOM   2351 C CB  . SER B 1 125 ? 8.37000   -18.39300 8.47200   1.000 37.62000  ? 174 SER B CB  1 
ATOM   2352 O OG  . SER B 1 125 ? 8.25300   -19.51800 9.31100   1.000 64.28000  ? 174 SER B OG  1 
ATOM   2353 N N   . ARG B 1 126 ? 7.95000   -17.64900 5.46900   1.000 44.53000  ? 175 ARG B N   1 
ATOM   2354 C CA  . ARG B 1 126 ? 8.34600   -16.74500 4.40400   1.000 45.82000  ? 175 ARG B CA  1 
ATOM   2355 C C   . ARG B 1 126 ? 7.12800   -16.20200 3.67900   1.000 50.08000  ? 175 ARG B C   1 
ATOM   2356 O O   . ARG B 1 126 ? 7.08800   -15.02100 3.32700   1.000 49.02000  ? 175 ARG B O   1 
ATOM   2357 C CB  . ARG B 1 126 ? 9.27800   -17.46200 3.42900   1.000 54.29000  ? 175 ARG B CB  1 
ATOM   2358 C CG  . ARG B 1 126 ? 10.14500  -16.54000 2.58600   1.000 56.80000  ? 175 ARG B CG  1 
ATOM   2359 C CD  . ARG B 1 126 ? 11.50800  -16.49300 3.20000   1.000 65.18000  ? 175 ARG B CD  1 
ATOM   2360 N NE  . ARG B 1 126 ? 12.24500  -15.28900 2.85400   1.000 56.57000  ? 175 ARG B NE  1 
ATOM   2361 C CZ  . ARG B 1 126 ? 13.48000  -15.31100 2.38200   1.000 66.80000  ? 175 ARG B CZ  1 
ATOM   2362 N NH1 . ARG B 1 126 ? 14.09600  -16.45900 2.12600   1.000 60.44000  ? 175 ARG B NH1 1 
ATOM   2363 N NH2 . ARG B 1 126 ? 14.11900  -14.15900 2.17400   1.000 65.68000  ? 175 ARG B NH2 1 
ATOM   2364 N N   . VAL B 1 127 ? 6.11500   -17.04500 3.46600   1.000 52.07000  ? 176 VAL B N   1 
ATOM   2365 C CA  . VAL B 1 127 ? 4.90400   -16.57200 2.80600   1.000 55.26000  ? 176 VAL B CA  1 
ATOM   2366 C C   . VAL B 1 127 ? 4.21500   -15.53400 3.67600   1.000 56.01000  ? 176 VAL B C   1 
ATOM   2367 O O   . VAL B 1 127 ? 3.75100   -14.49600 3.18900   1.000 61.11000  ? 176 VAL B O   1 
ATOM   2368 C CB  . VAL B 1 127 ? 3.96100   -17.74800 2.48000   1.000 56.53000  ? 176 VAL B CB  1 
ATOM   2369 C CG1 . VAL B 1 127 ? 2.62100   -17.22800 1.96100   1.000 48.65000  ? 176 VAL B CG1 1 
ATOM   2370 C CG2 . VAL B 1 127 ? 4.59700   -18.69300 1.45600   1.000 46.53000  ? 176 VAL B CG2 1 
ATOM   2371 N N   . GLU B 1 128 ? 4.16100   -15.78100 4.98000   1.000 58.01000  ? 177 GLU B N   1 
ATOM   2372 C CA  . GLU B 1 128 ? 3.55100   -14.81000 5.88200   1.000 59.70000  ? 177 GLU B CA  1 
ATOM   2373 C C   . GLU B 1 128 ? 4.33800   -13.50500 5.91100   1.000 57.59000  ? 177 GLU B C   1 
ATOM   2374 O O   . GLU B 1 128 ? 3.75300   -12.42400 6.02200   1.000 61.18000  ? 177 GLU B O   1 
ATOM   2375 C CB  . GLU B 1 128 ? 3.42300   -15.42300 7.26600   1.000 42.33000  ? 177 GLU B CB  1 
ATOM   2376 C CG  . GLU B 1 128 ? 2.01300   -15.93200 7.52100   1.000 58.31000  ? 177 GLU B CG  1 
ATOM   2377 C CD  . GLU B 1 128 ? 1.96300   -17.20800 8.35900   1.000 80.27000  ? 177 GLU B CD  1 
ATOM   2378 O OE1 . GLU B 1 128 ? 2.66000   -17.28300 9.41200   1.000 77.69000  ? 177 GLU B OE1 1 
ATOM   2379 O OE2 . GLU B 1 128 ? 1.21400   -18.13500 7.95400   1.000 78.72000  ? 177 GLU B OE2 1 
ATOM   2380 N N   . GLU B 1 129 ? 5.66300   -13.58500 5.80500   1.000 56.56000  ? 178 GLU B N   1 
ATOM   2381 C CA  . GLU B 1 129 ? 6.47400   -12.37100 5.73700   1.000 58.90000  ? 178 GLU B CA  1 
ATOM   2382 C C   . GLU B 1 129 ? 6.16400   -11.56700 4.47200   1.000 61.03000  ? 178 GLU B C   1 
ATOM   2383 O O   . GLU B 1 129 ? 6.12600   -10.32700 4.49800   1.000 60.10000  ? 178 GLU B O   1 
ATOM   2384 C CB  . GLU B 1 129 ? 7.96400   -12.72900 5.80900   1.000 52.84000  ? 178 GLU B CB  1 
ATOM   2385 C CG  . GLU B 1 129 ? 8.92500   -11.54900 5.64700   1.000 64.19000  ? 178 GLU B CG  1 
ATOM   2386 C CD  . GLU B 1 129 ? 8.89400   -10.57000 6.83900   1.000 73.14000  ? 178 GLU B CD  1 
ATOM   2387 O OE1 . GLU B 1 129 ? 8.25900   -10.90000 7.87100   1.000 74.52000  ? 178 GLU B OE1 1 
ATOM   2388 O OE2 . GLU B 1 129 ? 9.51200   -9.47400  6.74000   1.000 72.16000  ? 178 GLU B OE2 1 
ATOM   2389 N N   . LEU B 1 130 ? 5.98800   -12.25100 3.34300   1.000 55.47000  ? 179 LEU B N   1 
ATOM   2390 C CA  . LEU B 1 130 ? 5.56400   -11.56900 2.12700   1.000 49.35000  ? 179 LEU B CA  1 
ATOM   2391 C C   . LEU B 1 130 ? 4.15600   -10.99400 2.28000   1.000 56.10000  ? 179 LEU B C   1 
ATOM   2392 O O   . LEU B 1 130 ? 3.90400   -9.85500  1.87600   1.000 53.55000  ? 179 LEU B O   1 
ATOM   2393 C CB  . LEU B 1 130 ? 5.64100   -12.52800 0.95100   1.000 52.31000  ? 179 LEU B CB  1 
ATOM   2394 C CG  . LEU B 1 130 ? 7.05900   -12.93400 0.55600   1.000 50.05000  ? 179 LEU B CG  1 
ATOM   2395 C CD1 . LEU B 1 130 ? 7.02800   -14.17800 -0.30800  1.000 42.20000  ? 179 LEU B CD1 1 
ATOM   2396 C CD2 . LEU B 1 130 ? 7.73900   -11.79000 -0.16900  1.000 50.96000  ? 179 LEU B CD2 1 
ATOM   2397 N N   . ALA B 1 131 ? 3.22900   -11.75800 2.87300   1.000 54.36000  ? 180 ALA B N   1 
ATOM   2398 C CA  . ALA B 1 131 ? 1.87000   -11.25600 3.10000   1.000 54.97000  ? 180 ALA B CA  1 
ATOM   2399 C C   . ALA B 1 131 ? 1.84900   -10.06200 4.04600   1.000 57.18000  ? 180 ALA B C   1 
ATOM   2400 O O   . ALA B 1 131 ? 1.11800   -9.09300  3.81700   1.000 65.56000  ? 180 ALA B O   1 
ATOM   2401 C CB  . ALA B 1 131 ? 0.97900   -12.36400 3.65600   1.000 50.72000  ? 180 ALA B CB  1 
ATOM   2402 N N   . GLU B 1 132 ? 2.63400   -10.11400 5.12000   1.000 60.44000  ? 181 GLU B N   1 
ATOM   2403 C CA  . GLU B 1 132 ? 2.69800   -8.99700  6.05800   1.000 58.71000  ? 181 GLU B CA  1 
ATOM   2404 C C   . GLU B 1 132 ? 3.21900   -7.72900  5.38400   1.000 59.29000  ? 181 GLU B C   1 
ATOM   2405 O O   . GLU B 1 132 ? 2.77400   -6.62000  5.70400   1.000 61.90000  ? 181 GLU B O   1 
ATOM   2406 C CB  . GLU B 1 132 ? 3.55400   -9.38900  7.26500   1.000 71.91000  ? 181 GLU B CB  1 
ATOM   2407 C CG  . GLU B 1 132 ? 3.65400   -8.35400  8.39100   1.000 75.48000  ? 181 GLU B CG  1 
ATOM   2408 C CD  . GLU B 1 132 ? 4.71400   -8.74600  9.41700   1.000 90.46000  ? 181 GLU B CD  1 
ATOM   2409 O OE1 . GLU B 1 132 ? 5.10600   -9.93200  9.43700   1.000 91.00000  ? 181 GLU B OE1 1 
ATOM   2410 O OE2 . GLU B 1 132 ? 5.18700   -7.86800  10.17200  1.000 91.12000  ? 181 GLU B OE2 1 
ATOM   2411 N N   . ARG B 1 133 ? 4.19200   -7.85900  4.47800   1.000 57.16000  ? 182 ARG B N   1 
ATOM   2412 C CA  . ARG B 1 133 ? 4.73700   -6.66600  3.83700   1.000 57.11000  ? 182 ARG B CA  1 
ATOM   2413 C C   . ARG B 1 133 ? 3.77200   -6.02600  2.84500   1.000 62.24000  ? 182 ARG B C   1 
ATOM   2414 O O   . ARG B 1 133 ? 4.04500   -4.91700  2.37600   1.000 58.35000  ? 182 ARG B O   1 
ATOM   2415 C CB  . ARG B 1 133 ? 6.06700   -6.98700  3.15800   1.000 59.06000  ? 182 ARG B CB  1 
ATOM   2416 C CG  . ARG B 1 133 ? 7.17800   -7.20500  4.15800   1.000 59.34000  ? 182 ARG B CG  1 
ATOM   2417 C CD  . ARG B 1 133 ? 8.32300   -8.01100  3.59300   1.000 57.18000  ? 182 ARG B CD  1 
ATOM   2418 N NE  . ARG B 1 133 ? 9.47000   -7.94400  4.49100   1.000 60.17000  ? 182 ARG B NE  1 
ATOM   2419 C CZ  . ARG B 1 133 ? 10.50300  -7.12500  4.33600   1.000 65.58000  ? 182 ARG B CZ  1 
ATOM   2420 N NH1 . ARG B 1 133 ? 10.58900  -6.30200  3.29300   1.000 55.60000  ? 182 ARG B NH1 1 
ATOM   2421 N NH2 . ARG B 1 133 ? 11.47000  -7.12100  5.25400   1.000 59.90000  ? 182 ARG B NH2 1 
ATOM   2422 N N   . LEU B 1 134 ? 2.66500   -6.69400  2.50600   1.000 63.73000  ? 183 LEU B N   1 
ATOM   2423 C CA  . LEU B 1 134 ? 1.65400   -6.07000  1.65500   1.000 63.43000  ? 183 LEU B CA  1 
ATOM   2424 C C   . LEU B 1 134 ? 1.08300   -4.79200  2.26900   1.000 73.17000  ? 183 LEU B C   1 
ATOM   2425 O O   . LEU B 1 134 ? 0.73200   -3.85300  1.53800   1.000 67.87000  ? 183 LEU B O   1 
ATOM   2426 C CB  . LEU B 1 134 ? 0.51500   -7.04700  1.39300   1.000 50.14000  ? 183 LEU B CB  1 
ATOM   2427 C CG  . LEU B 1 134 ? 0.51500   -7.87800  0.12600   1.000 57.11000  ? 183 LEU B CG  1 
ATOM   2428 C CD1 . LEU B 1 134 ? -0.84400  -8.46000  -0.00500  1.000 57.19000  ? 183 LEU B CD1 1 
ATOM   2429 C CD2 . LEU B 1 134 ? 0.85100   -7.05500  -1.11100  1.000 50.94000  ? 183 LEU B CD2 1 
ATOM   2430 N N   . SER B 1 135 ? 0.96200   -4.74200  3.59700   1.000 71.05000  ? 184 SER B N   1 
ATOM   2431 C CA  . SER B 1 135 ? 0.25500   -3.67300  4.30200   1.000 73.26000  ? 184 SER B CA  1 
ATOM   2432 C C   . SER B 1 135 ? 1.18600   -2.80100  5.13500   1.000 71.39000  ? 184 SER B C   1 
ATOM   2433 O O   . SER B 1 135 ? 0.84400   -2.41800  6.25400   1.000 74.04000  ? 184 SER B O   1 
ATOM   2434 C CB  . SER B 1 135 ? -0.86200  -4.22900  5.18800   1.000 74.24000  ? 184 SER B CB  1 
ATOM   2435 O OG  . SER B 1 135 ? -0.52400  -5.49500  5.72500   1.000 79.28000  ? 184 SER B OG  1 
ATOM   2436 N N   . TRP B 1 136 ? 2.39500   -2.51600  4.65000   1.000 75.09000  ? 185 TRP B N   1 
ATOM   2437 C CA  . TRP B 1 136 ? 3.29300   -1.71400  5.47300   1.000 78.87000  ? 185 TRP B CA  1 
ATOM   2438 C C   . TRP B 1 136 ? 3.13000   -0.21800  5.24200   1.000 80.11000  ? 185 TRP B C   1 
ATOM   2439 O O   . TRP B 1 136 ? 3.47000   0.56800   6.14000   1.000 79.27000  ? 185 TRP B O   1 
ATOM   2440 C CB  . TRP B 1 136 ? 4.75700   -2.13600  5.25300   1.000 74.43000  ? 185 TRP B CB  1 
ATOM   2441 C CG  . TRP B 1 136 ? 5.13800   -3.36400  6.06600   1.000 70.22000  ? 185 TRP B CG  1 
ATOM   2442 C CD1 . TRP B 1 136 ? 4.28500   -4.16100  6.78900   1.000 72.17000  ? 185 TRP B CD1 1 
ATOM   2443 C CD2 . TRP B 1 136 ? 6.45000   -3.93400  6.23300   1.000 59.82000  ? 185 TRP B CD2 1 
ATOM   2444 N NE1 . TRP B 1 136 ? 4.98400   -5.18600  7.38600   1.000 73.18000  ? 185 TRP B NE1 1 
ATOM   2445 C CE2 . TRP B 1 136 ? 6.31100   -5.07000  7.06400   1.000 58.04000  ? 185 TRP B CE2 1 
ATOM   2446 C CE3 . TRP B 1 136 ? 7.72100   -3.60100  5.75700   1.000 58.13000  ? 185 TRP B CE3 1 
ATOM   2447 C CZ2 . TRP B 1 136 ? 7.39300   -5.86000  7.43800   1.000 45.63000  ? 185 TRP B CZ2 1 
ATOM   2448 C CZ3 . TRP B 1 136 ? 8.79700   -4.40000  6.12500   1.000 57.39000  ? 185 TRP B CZ3 1 
ATOM   2449 C CH2 . TRP B 1 136 ? 8.62200   -5.51300  6.95900   1.000 53.18000  ? 185 TRP B CH2 1 
ATOM   2450 N N   . ASP B 1 137 ? 2.56900   0.18000   4.09400   1.000 77.60000  ? 186 ASP B N   1 
ATOM   2451 C CA  . ASP B 1 137 ? 2.28500   1.58000   3.79800   1.000 89.54000  ? 186 ASP B CA  1 
ATOM   2452 C C   . ASP B 1 137 ? 3.58200   2.39000   3.91200   1.000 92.70000  ? 186 ASP B C   1 
ATOM   2453 O O   . ASP B 1 137 ? 4.04800   2.68600   5.02500   1.000 89.25000  ? 186 ASP B O   1 
ATOM   2454 C CB  . ASP B 1 137 ? 1.15900   2.10000   4.73300   1.000 91.28000  ? 186 ASP B CB  1 
ATOM   2455 C CG  . ASP B 1 137 ? 0.86300   3.61100   4.57300   1.000 91.84000  ? 186 ASP B CG  1 
ATOM   2456 O OD1 . ASP B 1 137 ? 0.41300   3.99600   3.46700   1.000 84.94000  ? 186 ASP B OD1 1 
ATOM   2457 O OD2 . ASP B 1 137 ? 1.06000   4.40100   5.55100   1.000 86.35000  ? 186 ASP B OD2 1 
ATOM   2458 N N   . PHE B 1 138 ? 4.17700   2.73500   2.76100   1.000 80.79000  ? 187 PHE B N   1 
ATOM   2459 C CA  . PHE B 1 138 ? 5.39600   3.56400   2.69800   1.000 87.85000  ? 187 PHE B CA  1 
ATOM   2460 C C   . PHE B 1 138 ? 5.27500   4.85900   3.51800   1.000 94.15000  ? 187 PHE B C   1 
ATOM   2461 O O   . PHE B 1 138 ? 5.79100   5.91100   3.13700   1.000 90.80000  ? 187 PHE B O   1 
ATOM   2462 C CB  . PHE B 1 138 ? 5.73600   3.89300   1.24800   1.000 78.29000  ? 187 PHE B CB  1 
ATOM   2463 N N   . CYS B 1 149 ? 12.56100  2.72100   -2.24500  1.000 105.14000 ? 195 CYS B N   1 
ATOM   2464 C CA  . CYS B 1 149 ? 13.83600  2.43600   -1.58700  1.000 114.91000 ? 195 CYS B CA  1 
ATOM   2465 C C   . CYS B 1 149 ? 14.97000  2.49400   -2.62300  1.000 113.68000 ? 195 CYS B C   1 
ATOM   2466 O O   . CYS B 1 149 ? 14.69500  2.63300   -3.82800  1.000 107.22000 ? 195 CYS B O   1 
ATOM   2467 C CB  . CYS B 1 149 ? 13.78300  1.06700   -0.87900  1.000 113.94000 ? 195 CYS B CB  1 
ATOM   2468 S SG  . CYS B 1 149 ? 15.23000  0.60600   0.15900   1.000 124.05000 ? 195 CYS B SG  1 
ATOM   2469 N N   . THR B 1 150 ? 16.21800  2.39100   -2.12800  1.000 113.72000 ? 196 THR B N   1 
ATOM   2470 C CA  . THR B 1 150 ? 17.47500  2.53100   -2.87400  1.000 115.17000 ? 196 THR B CA  1 
ATOM   2471 C C   . THR B 1 150 ? 17.29400  2.41400   -4.39100  1.000 107.22000 ? 196 THR B C   1 
ATOM   2472 O O   . THR B 1 150 ? 17.10800  3.42800   -5.08000  1.000 110.39000 ? 196 THR B O   1 
ATOM   2473 C CB  . THR B 1 150 ? 18.50500  1.50100   -2.36100  1.000 113.36000 ? 196 THR B CB  1 
ATOM   2474 O OG1 . THR B 1 150 ? 18.08000  0.16500   -2.67000  1.000 104.56000 ? 196 THR B OG1 1 
ATOM   2475 C CG2 . THR B 1 150 ? 18.68400  1.62500   -0.83800  1.000 99.73000  ? 196 THR B CG2 1 
ATOM   2476 N N   . GLY B 1 151 ? 17.33200  1.18700   -4.91500  1.000 97.32000  ? 197 GLY B N   1 
ATOM   2477 C CA  . GLY B 1 151 ? 16.92500  0.90500   -6.28100  1.000 85.76000  ? 197 GLY B CA  1 
ATOM   2478 C C   . GLY B 1 151 ? 16.20000  -0.42400  -6.32800  1.000 77.51000  ? 197 GLY B C   1 
ATOM   2479 O O   . GLY B 1 151 ? 16.62200  -1.33800  -7.04200  1.000 67.25000  ? 197 GLY B O   1 
ATOM   2480 N N   . VAL B 1 152 ? 15.12800  -0.54100  -5.53200  1.000 80.29000  ? 198 VAL B N   1 
ATOM   2481 C CA  . VAL B 1 152 ? 14.37000  -1.78700  -5.42000  1.000 64.83000  ? 198 VAL B CA  1 
ATOM   2482 C C   . VAL B 1 152 ? 13.45500  -1.98500  -6.62200  1.000 61.49000  ? 198 VAL B C   1 
ATOM   2483 O O   . VAL B 1 152 ? 13.47900  -3.04200  -7.26000  1.000 63.79000  ? 198 VAL B O   1 
ATOM   2484 C CB  . VAL B 1 152 ? 13.57700  -1.81600  -4.09500  1.000 69.53000  ? 198 VAL B CB  1 
ATOM   2485 C CG1 . VAL B 1 152 ? 12.53300  -2.93400  -4.09800  1.000 57.16000  ? 198 VAL B CG1 1 
ATOM   2486 C CG2 . VAL B 1 152 ? 14.51800  -1.96500  -2.90600  1.000 75.09000  ? 198 VAL B CG2 1 
ATOM   2487 N N   . LEU B 1 153 ? 12.64800  -0.97900  -6.97500  1.000 65.00000  ? 199 LEU B N   1 
ATOM   2488 C CA  . LEU B 1 153 ? 11.85900  -1.10000  -8.19800  1.000 58.18000  ? 199 LEU B CA  1 
ATOM   2489 C C   . LEU B 1 153 ? 12.74300  -1.50900  -9.36900  1.000 67.56000  ? 199 LEU B C   1 
ATOM   2490 O O   . LEU B 1 153 ? 12.33400  -2.30700  -10.22200 1.000 66.88000  ? 199 LEU B O   1 
ATOM   2491 C CB  . LEU B 1 153 ? 11.14000  0.21100   -8.50500  1.000 50.93000  ? 199 LEU B CB  1 
ATOM   2492 C CG  . LEU B 1 153 ? 9.78300   0.17100   -9.23000  1.000 63.51000  ? 199 LEU B CG  1 
ATOM   2493 C CD1 . LEU B 1 153 ? 9.82000   -0.62700  -10.52500 1.000 64.03000  ? 199 LEU B CD1 1 
ATOM   2494 C CD2 . LEU B 1 153 ? 8.68000   -0.37200  -8.31200  1.000 63.75000  ? 199 LEU B CD2 1 
ATOM   2495 N N   . ARG B 1 154 ? 13.97800  -1.00300  -9.39600  1.000 64.55000  ? 200 ARG B N   1 
ATOM   2496 C CA  . ARG B 1 154 ? 14.89200  -1.26600  -10.50300 1.000 57.99000  ? 200 ARG B CA  1 
ATOM   2497 C C   . ARG B 1 154 ? 15.42700  -2.69200  -10.45100 1.000 62.52000  ? 200 ARG B C   1 
ATOM   2498 O O   . ARG B 1 154 ? 15.32400  -3.44700  -11.43000 1.000 61.85000  ? 200 ARG B O   1 
ATOM   2499 C CB  . ARG B 1 154 ? 16.03300  -0.24800  -10.45700 1.000 66.39000  ? 200 ARG B CB  1 
ATOM   2500 C CG  . ARG B 1 154 ? 16.79900  0.00900   -11.75100 1.000 61.51000  ? 200 ARG B CG  1 
ATOM   2501 C CD  . ARG B 1 154 ? 17.89600  1.06200   -11.48200 1.000 68.36000  ? 200 ARG B CD  1 
ATOM   2502 N NE  . ARG B 1 154 ? 17.42300  2.18600   -10.66400 1.000 77.59000  ? 200 ARG B NE  1 
ATOM   2503 C CZ  . ARG B 1 154 ? 17.93800  2.56500   -9.49300  1.000 88.39000  ? 200 ARG B CZ  1 
ATOM   2504 N NH1 . ARG B 1 154 ? 18.98400  1.94200   -8.95300  1.000 77.76000  ? 200 ARG B NH1 1 
ATOM   2505 N NH2 . ARG B 1 154 ? 17.39400  3.60200   -8.84700  1.000 80.80000  ? 200 ARG B NH2 1 
ATOM   2506 N N   . ASP B 1 155 ? 15.99000  -3.08500  -9.30800  1.000 54.57000  ? 201 ASP B N   1 
ATOM   2507 C CA  . ASP B 1 155 ? 16.55900  -4.42000  -9.19600  1.000 57.45000  ? 201 ASP B CA  1 
ATOM   2508 C C   . ASP B 1 155 ? 15.48500  -5.49000  -9.29100  1.000 63.74000  ? 201 ASP B C   1 
ATOM   2509 O O   . ASP B 1 155 ? 15.73500  -6.57300  -9.83600  1.000 66.84000  ? 201 ASP B O   1 
ATOM   2510 C CB  . ASP B 1 155 ? 17.31700  -4.56400  -7.87400  1.000 69.04000  ? 201 ASP B CB  1 
ATOM   2511 C CG  . ASP B 1 155 ? 18.69600  -3.92400  -7.91400  1.000 76.48000  ? 201 ASP B CG  1 
ATOM   2512 O OD1 . ASP B 1 155 ? 18.93900  -3.09700  -8.82100  1.000 76.46000  ? 201 ASP B OD1 1 
ATOM   2513 O OD2 . ASP B 1 155 ? 19.53300  -4.24900  -7.03900  1.000 83.16000  ? 201 ASP B OD2 1 
ATOM   2514 N N   . PHE B 1 156 ? 14.28200  -5.20100  -8.79400  1.000 59.00000  ? 202 PHE B N   1 
ATOM   2515 C CA  . PHE B 1 156 ? 13.22600  -6.19500  -8.85800  1.000 56.61000  ? 202 PHE B CA  1 
ATOM   2516 C C   . PHE B 1 156 ? 12.74000  -6.37800  -10.28700 1.000 56.32000  ? 202 PHE B C   1 
ATOM   2517 O O   . PHE B 1 156 ? 12.52200  -7.51200  -10.72700 1.000 56.36000  ? 202 PHE B O   1 
ATOM   2518 C CB  . PHE B 1 156 ? 12.07600  -5.82200  -7.93400  1.000 52.02000  ? 202 PHE B CB  1 
ATOM   2519 C CG  . PHE B 1 156 ? 10.90000  -6.73900  -8.05100  1.000 52.06000  ? 202 PHE B CG  1 
ATOM   2520 C CD1 . PHE B 1 156 ? 10.88800  -7.95600  -7.39600  1.000 52.92000  ? 202 PHE B CD1 1 
ATOM   2521 C CD2 . PHE B 1 156 ? 9.80900   -6.39300  -8.83100  1.000 48.11000  ? 202 PHE B CD2 1 
ATOM   2522 C CE1 . PHE B 1 156 ? 9.79400   -8.80500  -7.50500  1.000 53.68000  ? 202 PHE B CE1 1 
ATOM   2523 C CE2 . PHE B 1 156 ? 8.71800   -7.22700  -8.94400  1.000 51.02000  ? 202 PHE B CE2 1 
ATOM   2524 C CZ  . PHE B 1 156 ? 8.70800   -8.43500  -8.28200  1.000 51.26000  ? 202 PHE B CZ  1 
ATOM   2525 N N   . SER B 1 157 ? 12.53600  -5.27800  -11.01700 1.000 56.86000  ? 203 SER B N   1 
ATOM   2526 C CA  . SER B 1 157 ? 12.14800  -5.38400  -12.42300 1.000 52.47000  ? 203 SER B CA  1 
ATOM   2527 C C   . SER B 1 157 ? 13.15900  -6.18000  -13.23400 1.000 55.61000  ? 203 SER B C   1 
ATOM   2528 O O   . SER B 1 157 ? 12.78100  -6.89200  -14.17800 1.000 59.71000  ? 203 SER B O   1 
ATOM   2529 C CB  . SER B 1 157 ? 11.97600  -4.00000  -13.03000 1.000 53.14000  ? 203 SER B CB  1 
ATOM   2530 O OG  . SER B 1 157 ? 10.90700  -3.32400  -12.39500 1.000 70.49000  ? 203 SER B OG  1 
ATOM   2531 N N   . ALA B 1 158 ? 14.44400  -6.07200  -12.89800 1.000 57.25000  ? 204 ALA B N   1 
ATOM   2532 C CA  . ALA B 1 158 ? 15.45000  -6.83400  -13.62800 1.000 60.30000  ? 204 ALA B CA  1 
ATOM   2533 C C   . ALA B 1 158 ? 15.26600  -8.35000  -13.46400 1.000 61.43000  ? 204 ALA B C   1 
ATOM   2534 O O   . ALA B 1 158 ? 15.72000  -9.11700  -14.32300 1.000 57.66000  ? 204 ALA B O   1 
ATOM   2535 C CB  . ALA B 1 158 ? 16.84400  -6.38800  -13.19300 1.000 47.66000  ? 204 ALA B CB  1 
ATOM   2536 N N   . LEU B 1 159 ? 14.60600  -8.79900  -12.38500 1.000 54.68000  ? 205 LEU B N   1 
ATOM   2537 C CA  . LEU B 1 159 ? 14.34000  -10.22200 -12.21400 1.000 53.08000  ? 205 LEU B CA  1 
ATOM   2538 C C   . LEU B 1 159 ? 13.34700  -10.74500 -13.24100 1.000 60.74000  ? 205 LEU B C   1 
ATOM   2539 O O   . LEU B 1 159 ? 13.35300  -11.94400 -13.54600 1.000 60.95000  ? 205 LEU B O   1 
ATOM   2540 C CB  . LEU B 1 159 ? 13.79700  -10.50400 -10.81800 1.000 56.42000  ? 205 LEU B CB  1 
ATOM   2541 C CG  . LEU B 1 159 ? 14.69700  -10.11800 -9.65400  1.000 57.38000  ? 205 LEU B CG  1 
ATOM   2542 C CD1 . LEU B 1 159 ? 13.88900  -10.17300 -8.40200  1.000 57.47000  ? 205 LEU B CD1 1 
ATOM   2543 C CD2 . LEU B 1 159 ? 15.86600  -11.05700 -9.56100  1.000 55.06000  ? 205 LEU B CD2 1 
ATOM   2544 N N   . LEU B 1 160 ? 12.48000  -9.87700  -13.76700 1.000 54.40000  ? 206 LEU B N   1 
ATOM   2545 C CA  . LEU B 1 160 ? 11.37900  -10.30500 -14.63000 1.000 55.26000  ? 206 LEU B CA  1 
ATOM   2546 C C   . LEU B 1 160 ? 11.83600  -10.37600 -16.09700 1.000 62.35000  ? 206 LEU B C   1 
ATOM   2547 O O   . LEU B 1 160 ? 11.48800  -9.55600  -16.94700 1.000 61.57000  ? 206 LEU B O   1 
ATOM   2548 C CB  . LEU B 1 160 ? 10.18000  -9.38200  -14.41900 1.000 52.16000  ? 206 LEU B CB  1 
ATOM   2549 C CG  . LEU B 1 160 ? 9.85000   -9.08900  -12.93300 1.000 59.80000  ? 206 LEU B CG  1 
ATOM   2550 C CD1 . LEU B 1 160 ? 8.65300   -8.16800  -12.75300 1.000 53.46000  ? 206 LEU B CD1 1 
ATOM   2551 C CD2 . LEU B 1 160 ? 9.63600   -10.36500 -12.07900 1.000 49.29000  ? 206 LEU B CD2 1 
ATOM   2552 N N   . GLN B 1 161 ? 12.61900  -11.42000 -16.38700 1.000 62.11000  ? 207 GLN B N   1 
ATOM   2553 C CA  . GLN B 1 161 ? 13.17200  -11.69800 -17.71400 1.000 59.04000  ? 207 GLN B CA  1 
ATOM   2554 C C   . GLN B 1 161 ? 12.30200  -12.64600 -18.54100 1.000 64.78000  ? 207 GLN B C   1 
ATOM   2555 O O   . GLN B 1 161 ? 12.56200  -12.81400 -19.73900 1.000 57.65000  ? 207 GLN B O   1 
ATOM   2556 C CB  . GLN B 1 161 ? 14.57300  -12.31500 -17.56900 1.000 58.73000  ? 207 GLN B CB  1 
ATOM   2557 C CG  . GLN B 1 161 ? 15.65000  -11.38600 -17.02100 1.000 73.53000  ? 207 GLN B CG  1 
ATOM   2558 C CD  . GLN B 1 161 ? 16.14300  -10.31500 -18.01900 1.000 92.82000  ? 207 GLN B CD  1 
ATOM   2559 O OE1 . GLN B 1 161 ? 15.50000  -10.02500 -19.04600 1.000 80.09000  ? 207 GLN B OE1 1 
ATOM   2560 N NE2 . GLN B 1 161 ? 17.29300  -9.71000  -17.69900 1.000 80.49000  ? 207 GLN B NE2 1 
ATOM   2561 N N   . SER B 1 162 ? 11.30500  -13.28200 -17.91900 1.000 67.09000  ? 208 SER B N   1 
ATOM   2562 C CA  . SER B 1 162 ? 10.40800  -14.19400 -18.61000 1.000 59.03000  ? 208 SER B CA  1 
ATOM   2563 C C   . SER B 1 162 ? 9.71200   -13.51100 -19.78700 1.000 63.60000  ? 208 SER B C   1 
ATOM   2564 O O   . SER B 1 162 ? 9.19000   -12.39600 -19.64200 1.000 55.84000  ? 208 SER B O   1 
ATOM   2565 C CB  . SER B 1 162 ? 9.33000   -14.69500 -17.64600 1.000 59.96000  ? 208 SER B CB  1 
ATOM   2566 O OG  . SER B 1 162 ? 9.56800   -16.01300 -17.23300 1.000 65.43000  ? 208 SER B OG  1 
ATOM   2567 N N   . PRO B 1 163 ? 9.62100   -14.17600 -20.93600 1.000 62.08000  ? 209 PRO B N   1 
ATOM   2568 C CA  . PRO B 1 163 ? 8.84700   -13.62700 -22.06000 1.000 63.55000  ? 209 PRO B CA  1 
ATOM   2569 C C   . PRO B 1 163 ? 7.36200   -13.91300 -21.89100 1.000 62.30000  ? 209 PRO B C   1 
ATOM   2570 O O   . PRO B 1 163 ? 6.96300   -14.99700 -21.45000 1.000 65.55000  ? 209 PRO B O   1 
ATOM   2571 C CB  . PRO B 1 163 ? 9.40400   -14.37300 -23.28000 1.000 60.64000  ? 209 PRO B CB  1 
ATOM   2572 C CG  . PRO B 1 163 ? 9.83800   -15.71400 -22.71500 1.000 71.78000  ? 209 PRO B CG  1 
ATOM   2573 C CD  . PRO B 1 163 ? 10.18500  -15.50300 -21.23000 1.000 61.95000  ? 209 PRO B CD  1 
ATOM   2574 N N   . GLY B 1 164 ? 6.54100   -12.93500 -22.27300 1.000 57.15000  ? 210 GLY B N   1 
ATOM   2575 C CA  . GLY B 1 164 ? 5.09500   -13.10700 -22.21800 1.000 55.90000  ? 210 GLY B CA  1 
ATOM   2576 C C   . GLY B 1 164 ? 4.52600   -13.30800 -20.82900 1.000 61.69000  ? 210 GLY B C   1 
ATOM   2577 O O   . GLY B 1 164 ? 3.54400   -14.03800 -20.67000 1.000 67.98000  ? 210 GLY B O   1 
ATOM   2578 N N   . ASP B 1 165 ? 5.10900   -12.69000 -19.81500 1.000 51.41000  ? 211 ASP B N   1 
ATOM   2579 C CA  . ASP B 1 165 ? 4.66300   -12.95300 -18.45300 1.000 54.48000  ? 211 ASP B CA  1 
ATOM   2580 C C   . ASP B 1 165 ? 3.30500   -12.29700 -18.21000 1.000 55.76000  ? 211 ASP B C   1 
ATOM   2581 O O   . ASP B 1 165 ? 3.21200   -11.09400 -17.97000 1.000 57.89000  ? 211 ASP B O   1 
ATOM   2582 C CB  . ASP B 1 165 ? 5.70500   -12.45300 -17.46500 1.000 56.31000  ? 211 ASP B CB  1 
ATOM   2583 C CG  . ASP B 1 165 ? 5.40600   -12.87500 -16.04000 1.000 60.71000  ? 211 ASP B CG  1 
ATOM   2584 O OD1 . ASP B 1 165 ? 4.39500   -13.60900 -15.83400 1.000 52.23000  ? 211 ASP B OD1 1 
ATOM   2585 O OD2 . ASP B 1 165 ? 6.18800   -12.46000 -15.13500 1.000 58.34000  ? 211 ASP B OD2 1 
ATOM   2586 N N   . ALA B 1 166 ? 2.24800   -13.10800 -18.19100 1.000 57.24000  ? 212 ALA B N   1 
ATOM   2587 C CA  . ALA B 1 166 ? 0.90900   -12.58700 -17.93000 1.000 52.09000  ? 212 ALA B CA  1 
ATOM   2588 C C   . ALA B 1 166 ? 0.81000   -11.89500 -16.57700 1.000 57.94000  ? 212 ALA B C   1 
ATOM   2589 O O   . ALA B 1 166 ? -0.05000  -11.02500 -16.39000 1.000 59.02000  ? 212 ALA B O   1 
ATOM   2590 C CB  . ALA B 1 166 ? -0.11400  -13.71900 -17.99400 1.000 54.47000  ? 212 ALA B CB  1 
ATOM   2591 N N   . HIS B 1 167 ? 1.65700   -12.27000 -15.61900 1.000 59.39000  ? 213 HIS B N   1 
ATOM   2592 C CA  . HIS B 1 167 ? 1.59800   -11.70700 -14.28000 1.000 49.94000  ? 213 HIS B CA  1 
ATOM   2593 C C   . HIS B 1 167 ? 2.62100   -10.60500 -14.06700 1.000 59.56000  ? 213 HIS B C   1 
ATOM   2594 O O   . HIS B 1 167 ? 2.79100   -10.14600 -12.93000 1.000 59.40000  ? 213 HIS B O   1 
ATOM   2595 C CB  . HIS B 1 167 ? 1.79200   -12.80200 -13.24000 1.000 55.38000  ? 213 HIS B CB  1 
ATOM   2596 C CG  . HIS B 1 167 ? 1.00200   -14.03800 -13.51900 1.000 51.17000  ? 213 HIS B CG  1 
ATOM   2597 N ND1 . HIS B 1 167 ? -0.31200  -14.18500 -13.12800 1.000 47.70000  ? 213 HIS B ND1 1 
ATOM   2598 C CD2 . HIS B 1 167 ? 1.34000   -15.18300 -14.16300 1.000 51.84000  ? 213 HIS B CD2 1 
ATOM   2599 C CE1 . HIS B 1 167 ? -0.74700  -15.37400 -13.50900 1.000 58.50000  ? 213 HIS B CE1 1 
ATOM   2600 N NE2 . HIS B 1 167 ? 0.23500   -15.99900 -14.14100 1.000 59.74000  ? 213 HIS B NE2 1 
ATOM   2601 N N   . ARG B 1 168 ? 3.29000   -10.15300 -15.13200 1.000 55.49000  ? 214 ARG B N   1 
ATOM   2602 C CA  . ARG B 1 168 ? 4.26900   -9.09100  -14.96700 1.000 53.25000  ? 214 ARG B CA  1 
ATOM   2603 C C   . ARG B 1 168 ? 3.63200   -7.85100  -14.36000 1.000 60.24000  ? 214 ARG B C   1 
ATOM   2604 O O   . ARG B 1 168 ? 4.24400   -7.18100  -13.51600 1.000 60.01000  ? 214 ARG B O   1 
ATOM   2605 C CB  . ARG B 1 168 ? 4.87800   -8.71800  -16.31400 1.000 49.93000  ? 214 ARG B CB  1 
ATOM   2606 C CG  . ARG B 1 168 ? 6.05300   -7.76600  -16.21400 1.000 45.93000  ? 214 ARG B CG  1 
ATOM   2607 C CD  . ARG B 1 168 ? 6.35900   -7.15100  -17.57500 1.000 51.48000  ? 214 ARG B CD  1 
ATOM   2608 N NE  . ARG B 1 168 ? 7.44600   -6.18500  -17.46500 1.000 52.63000  ? 214 ARG B NE  1 
ATOM   2609 C CZ  . ARG B 1 168 ? 8.71500   -6.51800  -17.27100 1.000 51.46000  ? 214 ARG B CZ  1 
ATOM   2610 N NH1 . ARG B 1 168 ? 9.10500   -7.78600  -17.26800 1.000 53.10000  ? 214 ARG B NH1 1 
ATOM   2611 N NH2 . ARG B 1 168 ? 9.61200   -5.55900  -17.06600 1.000 53.97000  ? 214 ARG B NH2 1 
ATOM   2612 N N   . GLU B 1 169 ? 2.38300   -7.55500  -14.72700 1.000 60.52000  ? 215 GLU B N   1 
ATOM   2613 C CA  . GLU B 1 169 ? 1.78300   -6.34000  -14.21000 1.000 68.08000  ? 215 GLU B CA  1 
ATOM   2614 C C   . GLU B 1 169 ? 1.51300   -6.45900  -12.71900 1.000 60.78000  ? 215 GLU B C   1 
ATOM   2615 O O   . GLU B 1 169 ? 1.94000   -5.60100  -11.94600 1.000 63.99000  ? 215 GLU B O   1 
ATOM   2616 C CB  . GLU B 1 169 ? 0.48500   -5.99500  -14.94000 1.000 83.11000  ? 215 GLU B CB  1 
ATOM   2617 C CG  . GLU B 1 169 ? 0.59600   -4.73300  -15.76600 1.000 97.08000  ? 215 GLU B CG  1 
ATOM   2618 C CD  . GLU B 1 169 ? 1.20200   -3.51400  -14.99900 1.000 116.56000 ? 215 GLU B CD  1 
ATOM   2619 O OE1 . GLU B 1 169 ? 1.13200   -3.41500  -13.73000 1.000 105.84000 ? 215 GLU B OE1 1 
ATOM   2620 O OE2 . GLU B 1 169 ? 1.81600   -2.69100  -15.69500 1.000 121.08000 ? 215 GLU B OE2 1 
ATOM   2621 N N   . ALA B 1 170 ? 0.81700   -7.51700  -12.29300 1.000 54.16000  ? 216 ALA B N   1 
ATOM   2622 C CA  . ALA B 1 170 ? 0.54700   -7.67300  -10.87500 1.000 53.15000  ? 216 ALA B CA  1 
ATOM   2623 C C   . ALA B 1 170 ? 1.84300   -7.63900  -10.06100 1.000 60.80000  ? 216 ALA B C   1 
ATOM   2624 O O   . ALA B 1 170 ? 1.90100   -7.00800  -8.99600  1.000 62.76000  ? 216 ALA B O   1 
ATOM   2625 C CB  . ALA B 1 170 ? -0.24500  -8.95800  -10.64400 1.000 58.86000  ? 216 ALA B CB  1 
ATOM   2626 N N   . LEU B 1 171 ? 2.91100   -8.25300  -10.57800 1.000 56.23000  ? 217 LEU B N   1 
ATOM   2627 C CA  . LEU B 1 171 ? 4.17600   -8.25300  -9.85200  1.000 57.07000  ? 217 LEU B CA  1 
ATOM   2628 C C   . LEU B 1 171 ? 4.67800   -6.83700  -9.65700  1.000 55.78000  ? 217 LEU B C   1 
ATOM   2629 O O   . LEU B 1 171 ? 5.08600   -6.46500  -8.55300  1.000 58.31000  ? 217 LEU B O   1 
ATOM   2630 C CB  . LEU B 1 171 ? 5.22700   -9.10700  -10.57700 1.000 53.17000  ? 217 LEU B CB  1 
ATOM   2631 C CG  . LEU B 1 171 ? 4.99400   -10.62100 -10.56100 1.000 49.82000  ? 217 LEU B CG  1 
ATOM   2632 C CD1 . LEU B 1 171 ? 6.01100   -11.31100 -11.41300 1.000 48.47000  ? 217 LEU B CD1 1 
ATOM   2633 C CD2 . LEU B 1 171 ? 4.99500   -11.21300 -9.12900  1.000 41.50000  ? 217 LEU B CD2 1 
ATOM   2634 N N   . LEU B 1 172 ? 4.64300   -6.02500  -10.71700 1.000 58.50000  ? 218 LEU B N   1 
ATOM   2635 C CA  . LEU B 1 172 ? 5.17600   -4.66900  -10.64900 1.000 55.36000  ? 218 LEU B CA  1 
ATOM   2636 C C   . LEU B 1 172 ? 4.32600   -3.74700  -9.77300  1.000 59.01000  ? 218 LEU B C   1 
ATOM   2637 O O   . LEU B 1 172 ? 4.85500   -2.77000  -9.22400  1.000 57.43000  ? 218 LEU B O   1 
ATOM   2638 C CB  . LEU B 1 172 ? 5.30700   -4.10500  -12.06200 1.000 61.59000  ? 218 LEU B CB  1 
ATOM   2639 C CG  . LEU B 1 172 ? 6.52600   -4.64600  -12.81700 1.000 60.96000  ? 218 LEU B CG  1 
ATOM   2640 C CD1 . LEU B 1 172 ? 6.55100   -4.20100  -14.27900 1.000 52.93000  ? 218 LEU B CD1 1 
ATOM   2641 C CD2 . LEU B 1 172 ? 7.78600   -4.21400  -12.10500 1.000 55.13000  ? 218 LEU B CD2 1 
ATOM   2642 N N   . GLN B 1 173 ? 3.04800   -4.06500  -9.57100  1.000 54.35000  ? 219 GLN B N   1 
ATOM   2643 C CA  . GLN B 1 173 ? 2.23600   -3.33700  -8.60300  1.000 65.42000  ? 219 GLN B CA  1 
ATOM   2644 C C   . GLN B 1 173 ? 2.36400   -3.86200  -7.17300  1.000 66.40000  ? 219 GLN B C   1 
ATOM   2645 O O   . GLN B 1 173 ? 1.61600   -3.40600  -6.29700  1.000 68.60000  ? 219 GLN B O   1 
ATOM   2646 C CB  . GLN B 1 173 ? 0.75600   -3.35800  -9.01200  1.000 65.30000  ? 219 GLN B CB  1 
ATOM   2647 C CG  . GLN B 1 173 ? 0.51700   -3.50900  -10.49200 1.000 74.36000  ? 219 GLN B CG  1 
ATOM   2648 C CD  . GLN B 1 173 ? -0.95100  -3.41600  -10.89200 1.000 79.48000  ? 219 GLN B CD  1 
ATOM   2649 O OE1 . GLN B 1 173 ? -1.78100  -4.24400  -10.48100 1.000 63.82000  ? 219 GLN B OE1 1 
ATOM   2650 N NE2 . GLN B 1 173 ? -1.27300  -2.42500  -11.72500 1.000 80.26000  ? 219 GLN B NE2 1 
ATOM   2651 N N   . LEU B 1 174 ? 3.28400   -4.78700  -6.90100  1.000 60.04000  ? 220 LEU B N   1 
ATOM   2652 C CA  . LEU B 1 174 ? 3.50900   -5.16300  -5.51500  1.000 59.28000  ? 220 LEU B CA  1 
ATOM   2653 C C   . LEU B 1 174 ? 4.17000   -3.99300  -4.79500  1.000 56.79000  ? 220 LEU B C   1 
ATOM   2654 O O   . LEU B 1 174 ? 4.97500   -3.27500  -5.39900  1.000 59.45000  ? 220 LEU B O   1 
ATOM   2655 C CB  . LEU B 1 174 ? 4.38900   -6.40700  -5.40300  1.000 51.97000  ? 220 LEU B CB  1 
ATOM   2656 C CG  . LEU B 1 174 ? 3.75500   -7.72500  -5.84800  1.000 54.81000  ? 220 LEU B CG  1 
ATOM   2657 C CD1 . LEU B 1 174 ? 4.80800   -8.81400  -6.03800  1.000 54.15000  ? 220 LEU B CD1 1 
ATOM   2658 C CD2 . LEU B 1 174 ? 2.70300   -8.17400  -4.86200  1.000 55.27000  ? 220 LEU B CD2 1 
ATOM   2659 N N   . PRO B 1 175 ? 3.82900   -3.75800  -3.53000  1.000 53.62000  ? 221 PRO B N   1 
ATOM   2660 C CA  . PRO B 1 175 ? 4.50300   -2.70300  -2.76100  1.000 57.58000  ? 221 PRO B CA  1 
ATOM   2661 C C   . PRO B 1 175 ? 6.00600   -2.92200  -2.71300  1.000 55.63000  ? 221 PRO B C   1 
ATOM   2662 O O   . PRO B 1 175 ? 6.50300   -4.03400  -2.88900  1.000 54.42000  ? 221 PRO B O   1 
ATOM   2663 C CB  . PRO B 1 175 ? 3.88100   -2.82200  -1.37200  1.000 56.70000  ? 221 PRO B CB  1 
ATOM   2664 C CG  . PRO B 1 175 ? 2.53000   -3.44300  -1.62300  1.000 53.96000  ? 221 PRO B CG  1 
ATOM   2665 C CD  . PRO B 1 175 ? 2.67400   -4.33000  -2.82000  1.000 50.39000  ? 221 PRO B CD  1 
ATOM   2666 N N   . LEU B 1 176 ? 6.74000   -1.82800  -2.51900  1.000 62.81000  ? 222 LEU B N   1 
ATOM   2667 C CA  . LEU B 1 176 ? 8.19500   -1.92700  -2.52200  1.000 53.04000  ? 222 LEU B CA  1 
ATOM   2668 C C   . LEU B 1 176 ? 8.68100   -2.87700  -1.43300  1.000 55.31000  ? 222 LEU B C   1 
ATOM   2669 O O   . LEU B 1 176 ? 9.66800   -3.59000  -1.62200  1.000 57.91000  ? 222 LEU B O   1 
ATOM   2670 C CB  . LEU B 1 176 ? 8.80500   -0.54100  -2.34600  1.000 59.44000  ? 222 LEU B CB  1 
ATOM   2671 C CG  . LEU B 1 176 ? 9.11600   0.25800   -3.62200  1.000 70.00000  ? 222 LEU B CG  1 
ATOM   2672 C CD1 . LEU B 1 176 ? 10.33300  -0.25300  -4.34200  1.000 74.95000  ? 222 LEU B CD1 1 
ATOM   2673 C CD2 . LEU B 1 176 ? 7.92400   0.27200   -4.58200  1.000 72.53000  ? 222 LEU B CD2 1 
ATOM   2674 N N   . ALA B 1 177 ? 7.98600   -2.93200  -0.30000  1.000 55.46000  ? 223 ALA B N   1 
ATOM   2675 C CA  . ALA B 1 177 ? 8.42000   -3.82200  0.77400   1.000 55.40000  ? 223 ALA B CA  1 
ATOM   2676 C C   . ALA B 1 177 ? 8.37300   -5.28500  0.34600   1.000 59.31000  ? 223 ALA B C   1 
ATOM   2677 O O   . ALA B 1 177 ? 9.20700   -6.08800  0.78300   1.000 61.15000  ? 223 ALA B O   1 
ATOM   2678 C CB  . ALA B 1 177 ? 7.56700   -3.60700  2.02200   1.000 46.58000  ? 223 ALA B CB  1 
ATOM   2679 N N   . VAL B 1 178 ? 7.36200   -5.66600  -0.44300  1.000 56.89000  ? 224 VAL B N   1 
ATOM   2680 C CA  . VAL B 1 178 ? 7.29300   -7.03700  -0.93900  1.000 51.84000  ? 224 VAL B CA  1 
ATOM   2681 C C   . VAL B 1 178 ? 8.38100   -7.27000  -1.96700  1.000 48.62000  ? 224 VAL B C   1 
ATOM   2682 O O   . VAL B 1 178 ? 9.07500   -8.29500  -1.93400  1.000 50.54000  ? 224 VAL B O   1 
ATOM   2683 C CB  . VAL B 1 178 ? 5.89800   -7.34900  -1.51000  1.000 55.31000  ? 224 VAL B CB  1 
ATOM   2684 C CG1 . VAL B 1 178 ? 5.90100   -8.70200  -2.18400  1.000 57.10000  ? 224 VAL B CG1 1 
ATOM   2685 C CG2 . VAL B 1 178 ? 4.85100   -7.33200  -0.39800  1.000 56.72000  ? 224 VAL B CG2 1 
ATOM   2686 N N   . GLN B 1 179 ? 8.56700   -6.31500  -2.88000  1.000 52.21000  ? 225 GLN B N   1 
ATOM   2687 C CA  . GLN B 1 179 ? 9.60500   -6.45200  -3.89300  1.000 52.06000  ? 225 GLN B CA  1 
ATOM   2688 C C   . GLN B 1 179 ? 10.96200  -6.62700  -3.23700  1.000 52.53000  ? 225 GLN B C   1 
ATOM   2689 O O   . GLN B 1 179 ? 11.77100  -7.45500  -3.66900  1.000 51.24000  ? 225 GLN B O   1 
ATOM   2690 C CB  . GLN B 1 179 ? 9.59800   -5.24300  -4.83200  1.000 51.56000  ? 225 GLN B CB  1 
ATOM   2691 C CG  . GLN B 1 179 ? 8.44300   -5.25000  -5.81800  1.000 59.62000  ? 225 GLN B CG  1 
ATOM   2692 C CD  . GLN B 1 179 ? 8.31700   -3.97300  -6.62300  1.000 56.79000  ? 225 GLN B CD  1 
ATOM   2693 O OE1 . GLN B 1 179 ? 8.74500   -2.91200  -6.18900  1.000 65.58000  ? 225 GLN B OE1 1 
ATOM   2694 N NE2 . GLN B 1 179 ? 7.73500   -4.07600  -7.81400  1.000 63.16000  ? 225 GLN B NE2 1 
ATOM   2695 N N   . GLU B 1 180 ? 11.21700  -5.86200  -2.17500  1.000 57.69000  ? 226 GLU B N   1 
ATOM   2696 C CA  . GLU B 1 180 ? 12.49700  -5.94400  -1.48400  1.000 57.98000  ? 226 GLU B CA  1 
ATOM   2697 C C   . GLU B 1 180 ? 12.69500  -7.31500  -0.85900  1.000 56.74000  ? 226 GLU B C   1 
ATOM   2698 O O   . GLU B 1 180 ? 13.80600  -7.85500  -0.88500  1.000 56.39000  ? 226 GLU B O   1 
ATOM   2699 C CB  . GLU B 1 180 ? 12.58900  -4.84900  -0.42400  1.000 58.31000  ? 226 GLU B CB  1 
ATOM   2700 C CG  . GLU B 1 180 ? 13.65900  -5.09800  0.60200   1.000 63.23000  ? 226 GLU B CG  1 
ATOM   2701 C CD  . GLU B 1 180 ? 13.83700  -3.93400  1.56100   1.000 85.63000  ? 226 GLU B CD  1 
ATOM   2702 O OE1 . GLU B 1 180 ? 14.50300  -2.94400  1.17200   1.000 92.28000  ? 226 GLU B OE1 1 
ATOM   2703 O OE2 . GLU B 1 180 ? 13.31100  -4.00800  2.69900   1.000 84.25000  ? 226 GLU B OE2 1 
ATOM   2704 N N   . GLU B 1 181 ? 11.61900  -7.90100  -0.30900  1.000 53.45000  ? 227 GLU B N   1 
ATOM   2705 C CA  . GLU B 1 181 ? 11.72300  -9.22400  0.30200   1.000 51.61000  ? 227 GLU B CA  1 
ATOM   2706 C C   . GLU B 1 181 ? 11.92000  -10.32200 -0.73600  1.000 60.42000  ? 227 GLU B C   1 
ATOM   2707 O O   . GLU B 1 181 ? 12.64200  -11.29500 -0.48200  1.000 53.84000  ? 227 GLU B O   1 
ATOM   2708 C CB  . GLU B 1 181 ? 10.48800  -9.52700  1.13700   1.000 49.02000  ? 227 GLU B CB  1 
ATOM   2709 C CG  . GLU B 1 181 ? 10.57500  -10.86000 1.86400   1.000 50.24000  ? 227 GLU B CG  1 
ATOM   2710 C CD  . GLU B 1 181 ? 11.69900  -10.91200 2.92100   1.000 62.35000  ? 227 GLU B CD  1 
ATOM   2711 O OE1 . GLU B 1 181 ? 12.36100  -9.88200  3.17900   1.000 66.52000  ? 227 GLU B OE1 1 
ATOM   2712 O OE2 . GLU B 1 181 ? 11.93700  -12.00200 3.48600   1.000 62.96000  ? 227 GLU B OE2 1 
ATOM   2713 N N   . LEU B 1 182 ? 11.29000  -10.18700 -1.91000  1.000 52.29000  ? 228 LEU B N   1 
ATOM   2714 C CA  . LEU B 1 182 ? 11.53900  -11.14300 -2.97800  1.000 46.80000  ? 228 LEU B CA  1 
ATOM   2715 C C   . LEU B 1 182 ? 12.99100  -11.06300 -3.43400  1.000 54.18000  ? 228 LEU B C   1 
ATOM   2716 O O   . LEU B 1 182 ? 13.59800  -12.08000 -3.78300  1.000 56.09000  ? 228 LEU B O   1 
ATOM   2717 C CB  . LEU B 1 182 ? 10.58800  -10.88400 -4.14200  1.000 46.60000  ? 228 LEU B CB  1 
ATOM   2718 C CG  . LEU B 1 182 ? 9.16500   -11.35800 -3.85100  1.000 50.90000  ? 228 LEU B CG  1 
ATOM   2719 C CD1 . LEU B 1 182 ? 8.21900   -11.00100 -4.97700  1.000 40.99000  ? 228 LEU B CD1 1 
ATOM   2720 C CD2 . LEU B 1 182 ? 9.14900   -12.85000 -3.60000  1.000 43.53000  ? 228 LEU B CD2 1 
ATOM   2721 N N   . LEU B 1 183 ? 13.56800  -9.85900  -3.44900  1.000 58.57000  ? 229 LEU B N   1 
ATOM   2722 C CA  . LEU B 1 183 ? 14.99300  -9.74300  -3.75100  1.000 60.24000  ? 229 LEU B CA  1 
ATOM   2723 C C   . LEU B 1 183 ? 15.83600  -10.48900 -2.71900  1.000 53.71000  ? 229 LEU B C   1 
ATOM   2724 O O   . LEU B 1 183 ? 16.79800  -11.17800 -3.06600  1.000 62.25000  ? 229 LEU B O   1 
ATOM   2725 C CB  . LEU B 1 183 ? 15.40100  -8.27100  -3.83100  1.000 52.15000  ? 229 LEU B CB  1 
ATOM   2726 C CG  . LEU B 1 183 ? 15.13300  -7.57700  -5.16400  1.000 60.02000  ? 229 LEU B CG  1 
ATOM   2727 C CD1 . LEU B 1 183 ? 15.18300  -6.05900  -5.02200  1.000 58.86000  ? 229 LEU B CD1 1 
ATOM   2728 C CD2 . LEU B 1 183 ? 16.08700  -8.03500  -6.27100  1.000 63.63000  ? 229 LEU B CD2 1 
ATOM   2729 N N   . SER B 1 184 ? 15.48900  -10.37700 -1.44600  1.000 60.21000  ? 230 SER B N   1 
ATOM   2730 C CA  . SER B 1 184 ? 16.25500  -11.10700 -0.43700  1.000 66.48000  ? 230 SER B CA  1 
ATOM   2731 C C   . SER B 1 184 ? 16.15900  -12.61300 -0.65500  1.000 64.73000  ? 230 SER B C   1 
ATOM   2732 O O   . SER B 1 184 ? 17.16700  -13.32500 -0.56800  1.000 57.45000  ? 230 SER B O   1 
ATOM   2733 C CB  . SER B 1 184 ? 15.78300  -10.71600 0.95900   1.000 54.56000  ? 230 SER B CB  1 
ATOM   2734 O OG  . SER B 1 184 ? 16.50300  -9.57100  1.37800   1.000 74.07000  ? 230 SER B OG  1 
ATOM   2735 N N   . LEU B 1 185 ? 14.96300  -13.10200 -1.00400  1.000 61.70000  ? 231 LEU B N   1 
ATOM   2736 C CA  . LEU B 1 185 ? 14.77200  -14.52800 -1.24200  1.000 58.34000  ? 231 LEU B CA  1 
ATOM   2737 C C   . LEU B 1 185 ? 15.62800  -15.01200 -2.41000  1.000 59.05000  ? 231 LEU B C   1 
ATOM   2738 O O   . LEU B 1 185 ? 16.25400  -16.07500 -2.33100  1.000 63.20000  ? 231 LEU B O   1 
ATOM   2739 C CB  . LEU B 1 185 ? 13.29600  -14.81400 -1.50400  1.000 48.88000  ? 231 LEU B CB  1 
ATOM   2740 C CG  . LEU B 1 185 ? 12.98700  -16.18300 -2.08900  1.000 52.42000  ? 231 LEU B CG  1 
ATOM   2741 C CD1 . LEU B 1 185 ? 13.40000  -17.26400 -1.11500  1.000 45.57000  ? 231 LEU B CD1 1 
ATOM   2742 C CD2 . LEU B 1 185 ? 11.50800  -16.29300 -2.40700  1.000 49.23000  ? 231 LEU B CD2 1 
ATOM   2743 N N   . VAL B 1 186 ? 15.69000  -14.22600 -3.49000  1.000 61.72000  ? 232 VAL B N   1 
ATOM   2744 C CA  . VAL B 1 186 ? 16.39100  -14.63100 -4.71100  1.000 64.70000  ? 232 VAL B CA  1 
ATOM   2745 C C   . VAL B 1 186 ? 17.91200  -14.62800 -4.53600  1.000 55.98000  ? 232 VAL B C   1 
ATOM   2746 O O   . VAL B 1 186 ? 18.61400  -15.39700 -5.20200  1.000 66.91000  ? 232 VAL B O   1 
ATOM   2747 C CB  . VAL B 1 186 ? 15.94000  -13.71100 -5.86100  1.000 56.42000  ? 232 VAL B CB  1 
ATOM   2748 C CG1 . VAL B 1 186 ? 16.93500  -13.70800 -7.00100  1.000 58.62000  ? 232 VAL B CG1 1 
ATOM   2749 C CG2 . VAL B 1 186 ? 14.56300  -14.12000 -6.33600  1.000 50.58000  ? 232 VAL B CG2 1 
ATOM   2750 N N   . GLN B 1 187 ? 18.44500  -13.81100 -3.63300  1.000 62.57000  ? 233 GLN B N   1 
ATOM   2751 C CA  . GLN B 1 187 ? 19.89500  -13.63800 -3.46400  1.000 68.64000  ? 233 GLN B CA  1 
ATOM   2752 C C   . GLN B 1 187 ? 20.46600  -14.40100 -2.26800  1.000 63.66000  ? 233 GLN B C   1 
ATOM   2753 O O   . GLN B 1 187 ? 21.28200  -13.83800 -1.54500  1.000 78.46000  ? 233 GLN B O   1 
ATOM   2754 C CB  . GLN B 1 187 ? 20.25800  -12.14800 -3.35200  1.000 62.93000  ? 233 GLN B CB  1 
ATOM   2755 C CG  . GLN B 1 187 ? 20.47900  -11.35700 -4.67200  1.000 70.88000  ? 233 GLN B CG  1 
ATOM   2756 C CD  . GLN B 1 187 ? 19.58800  -10.11800 -4.84100  1.000 79.67000  ? 233 GLN B CD  1 
ATOM   2757 O OE1 . GLN B 1 187 ? 18.37200  -10.21800 -4.97700  1.000 84.39000  ? 233 GLN B OE1 1 
ATOM   2758 N NE2 . GLN B 1 187 ? 20.20200  -8.93700  -4.78300  1.000 72.57000  ? 233 GLN B NE2 1 
ATOM   2759 N N   . GLU B 1 188 ? 20.13800  -15.67400 -2.04900  1.000 69.77000  ? 234 GLU B N   1 
ATOM   2760 C CA  . GLU B 1 188 ? 20.69400  -16.39000 -0.88200  1.000 72.39000  ? 234 GLU B CA  1 
ATOM   2761 C C   . GLU B 1 188 ? 21.49100  -17.64800 -1.24700  1.000 71.34000  ? 234 GLU B C   1 
ATOM   2762 O O   . GLU B 1 188 ? 21.02200  -18.50300 -2.00800  1.000 80.83000  ? 234 GLU B O   1 
ATOM   2763 C CB  . GLU B 1 188 ? 19.57900  -16.76900 0.08600   1.000 74.62000  ? 234 GLU B CB  1 
ATOM   2764 C CG  . GLU B 1 188 ? 18.87600  -15.58500 0.71600   1.000 72.97000  ? 234 GLU B CG  1 
ATOM   2765 C CD  . GLU B 1 188 ? 17.61200  -15.98900 1.46600   1.000 81.87000  ? 234 GLU B CD  1 
ATOM   2766 O OE1 . GLU B 1 188 ? 17.18900  -17.17000 1.32000   1.000 81.59000  ? 234 GLU B OE1 1 
ATOM   2767 O OE2 . GLU B 1 188 ? 17.03800  -15.12600 2.18600   1.000 72.72000  ? 234 GLU B OE2 1 
HETATM 2768 S S   . SO4 C 2 .   ? -5.51900  -9.29000  -24.00200 1.000 111.77000 ? 301 SO4 A S   1 
HETATM 2769 O O1  . SO4 C 2 .   ? -4.05800  -9.22700  -23.88500 1.000 76.87000  ? 301 SO4 A O1  1 
HETATM 2770 O O2  . SO4 C 2 .   ? -5.92400  -9.62000  -25.38000 1.000 92.57000  ? 301 SO4 A O2  1 
HETATM 2771 O O3  . SO4 C 2 .   ? -6.05700  -10.30100 -23.07500 1.000 95.53000  ? 301 SO4 A O3  1 
HETATM 2772 O O4  . SO4 C 2 .   ? -6.04000  -7.96700  -23.63600 1.000 115.75000 ? 301 SO4 A O4  1 
HETATM 2773 S S   . SO4 D 2 .   ? -9.81900  -29.09100 -14.99700 0.740 101.15000 ? 302 SO4 A S   1 
HETATM 2774 O O1  . SO4 D 2 .   ? -8.93500  -29.96200 -15.78500 0.740 71.83000  ? 302 SO4 A O1  1 
HETATM 2775 O O2  . SO4 D 2 .   ? -10.98400 -28.72600 -15.80300 0.740 74.87000  ? 302 SO4 A O2  1 
HETATM 2776 O O3  . SO4 D 2 .   ? -10.28200 -29.80100 -13.79700 0.740 88.60000  ? 302 SO4 A O3  1 
HETATM 2777 O O4  . SO4 D 2 .   ? -9.09400  -27.87200 -14.61000 0.740 89.03000  ? 302 SO4 A O4  1 
HETATM 2778 S S   . SO4 E 2 .   ? 14.56700  -43.21000 -14.06500 0.720 89.56000  ? 301 SO4 B S   1 
HETATM 2779 O O1  . SO4 E 2 .   ? 16.03100  -43.19800 -14.12700 0.720 78.20000  ? 301 SO4 B O1  1 
HETATM 2780 O O2  . SO4 E 2 .   ? 14.06600  -42.29000 -15.09800 0.720 81.05000  ? 301 SO4 B O2  1 
HETATM 2781 O O3  . SO4 E 2 .   ? 14.04500  -44.57400 -14.24100 0.720 85.52000  ? 301 SO4 B O3  1 
HETATM 2782 O O4  . SO4 E 2 .   ? 14.11900  -42.75500 -12.74900 0.720 78.64000  ? 301 SO4 B O4  1 
HETATM 2783 S S   . SO4 F 2 .   ? 30.43300  -30.59900 -4.99600  0.790 102.76000 ? 302 SO4 B S   1 
HETATM 2784 O O1  . SO4 F 2 .   ? 31.73700  -30.22200 -4.44500  0.790 96.08000  ? 302 SO4 B O1  1 
HETATM 2785 O O2  . SO4 F 2 .   ? 30.56200  -31.17900 -6.34900  0.790 79.21000  ? 302 SO4 B O2  1 
HETATM 2786 O O3  . SO4 F 2 .   ? 29.83100  -31.57300 -4.09000  0.790 87.07000  ? 302 SO4 B O3  1 
HETATM 2787 O O4  . SO4 F 2 .   ? 29.58400  -29.40800 -5.02500  0.790 78.18000  ? 302 SO4 B O4  1 
HETATM 2788 O O   . HOH G 3 .   ? 12.01600  -21.69600 -15.77600 1.000 58.45000  ? 401 HOH A O   1 
HETATM 2789 O O   . HOH G 3 .   ? 39.26300  -13.01400 -32.20400 1.000 72.34000  ? 402 HOH A O   1 
HETATM 2790 O O   . HOH G 3 .   ? 23.40400  -18.92900 -11.06600 1.000 56.94000  ? 403 HOH A O   1 
HETATM 2791 O O   . HOH G 3 .   ? 19.42000  -29.48500 -14.17300 1.000 53.45000  ? 404 HOH A O   1 
HETATM 2792 O O   . HOH G 3 .   ? -5.31900  -9.36100  -20.73800 1.000 54.46000  ? 405 HOH A O   1 
HETATM 2793 O O   . HOH G 3 .   ? 23.464    -16.790   -38.142   1.000 49.74000  ? 406 HOH A O   1 
HETATM 2794 O O   . HOH G 3 .   ? 4.83600   -19.80300 -29.63400 1.000 53.00000  ? 407 HOH A O   1 
HETATM 2795 O O   . HOH G 3 .   ? 5.35500   -21.87300 -33.83600 1.000 51.85000  ? 408 HOH A O   1 
HETATM 2796 O O   . HOH G 3 .   ? 2.92500   -27.29400 -31.51900 1.000 45.35000  ? 409 HOH A O   1 
HETATM 2797 O O   . HOH G 3 .   ? 17.15700  -23.71700 -19.61700 1.000 42.96000  ? 410 HOH A O   1 
HETATM 2798 O O   . HOH G 3 .   ? -1.96800  -10.75200 -25.56000 1.000 50.55000  ? 411 HOH A O   1 
HETATM 2799 O O   . HOH G 3 .   ? -9.45900  -24.05100 -33.24100 1.000 53.70000  ? 412 HOH A O   1 
HETATM 2800 O O   . HOH G 3 .   ? 3.53200   -29.19300 -29.16600 1.000 50.48000  ? 413 HOH A O   1 
HETATM 2801 O O   . HOH G 3 .   ? 15.06200  -28.04000 -18.09500 1.000 42.16000  ? 414 HOH A O   1 
HETATM 2802 O O   . HOH G 3 .   ? -13.58900 -35.60400 -20.39600 1.000 62.40000  ? 415 HOH A O   1 
HETATM 2803 O O   . HOH G 3 .   ? -17.79700 -29.51300 -23.34300 1.000 71.45000  ? 416 HOH A O   1 
HETATM 2804 O O   . HOH H 3 .   ? 11.70300  -21.13900 -12.74800 1.000 56.39000  ? 401 HOH B O   1 
HETATM 2805 O O   . HOH H 3 .   ? 4.52600   0.08400   8.08900   1.000 55.55000  ? 402 HOH B O   1 
HETATM 2806 O O   . HOH H 3 .   ? 16.52900  -53.26300 -2.00200  1.000 52.49000  ? 403 HOH B O   1 
HETATM 2807 O O   . HOH H 3 .   ? 11.48300  -19.32100 -17.18600 1.000 62.58000  ? 404 HOH B O   1 
HETATM 2808 O O   . HOH H 3 .   ? 18.94600  -25.24100 -9.04600  1.000 56.57000  ? 405 HOH B O   1 
HETATM 2809 O O   . HOH H 3 .   ? 16.35300  -26.23600 0.97100   1.000 42.75000  ? 406 HOH B O   1 
HETATM 2810 O O   . HOH H 3 .   ? 4.87300   -16.15800 -16.19600 1.000 46.06000  ? 407 HOH B O   1 
HETATM 2811 O O   . HOH H 3 .   ? 7.17900   -17.43900 -9.47200  1.000 45.81000  ? 408 HOH B O   1 
HETATM 2812 O O   . HOH H 3 .   ? 7.36700   -27.17900 -4.59400  1.000 53.38000  ? 409 HOH B O   1 
HETATM 2813 O O   . HOH H 3 .   ? 19.39500  -29.30300 3.13900   1.000 56.66000  ? 410 HOH B O   1 
HETATM 2814 O O   . HOH H 3 .   ? 6.60000   -49.14800 -5.62500  1.000 48.73000  ? 411 HOH B O   1 
HETATM 2815 O O   . HOH H 3 .   ? 10.66600  -31.48800 2.69100   1.000 49.15000  ? 412 HOH B O   1 
HETATM 2816 O O   . HOH H 3 .   ? 19.23200  -31.90100 -13.97300 1.000 49.86000  ? 413 HOH B O   1 
HETATM 2817 O O   . HOH H 3 .   ? 11.15700  -53.07300 -5.77500  1.000 46.81000  ? 414 HOH B O   1 
HETATM 2818 O O   . HOH H 3 .   ? 3.33600   -18.49100 -15.44200 1.000 55.09000  ? 415 HOH B O   1 
HETATM 2819 O O   . HOH H 3 .   ? 13.51700  -51.71800 -5.21900  1.000 49.44000  ? 416 HOH B O   1 
HETATM 2820 O O   . HOH H 3 .   ? -0.52100  -7.60000  -7.34400  1.000 48.33000  ? 417 HOH B O   1 
HETATM 2821 O O   . HOH H 3 .   ? 6.13200   -1.12000  0.83700   1.000 49.50000  ? 418 HOH B O   1 
HETATM 2822 O O   . HOH H 3 .   ? 18.55300  -40.93600 4.23500   1.000 54.60000  ? 419 HOH B O   1 
HETATM 2823 O O   . HOH H 3 .   ? 8.59200   -57.77800 2.68700   1.000 57.09000  ? 420 HOH B O   1 
HETATM 2824 O O   . HOH H 3 .   ? 15.60000  -58.34300 -4.32300  1.000 43.60000  ? 421 HOH B O   1 
HETATM 2825 O O   . HOH H 3 .   ? 13.93000  -52.50900 -2.65000  1.000 48.24000  ? 422 HOH B O   1 
HETATM 2826 O O   . HOH H 3 .   ? 0.21500   -18.95000 -14.76000 1.000 54.65000  ? 423 HOH B O   1 
HETATM 2827 O O   . HOH H 3 .   ? 15.99500  -57.33200 -1.95700  1.000 50.93000  ? 424 HOH B O   1 
HETATM 2828 O O   . HOH H 3 .   ? 14.69300  -49.27700 -6.24700  1.000 50.37000  ? 425 HOH B O   1 
HETATM 2829 O O   . HOH H 3 .   ? 17.85900  -52.99900 1.17700   1.000 53.58000  ? 426 HOH B O   1 
HETATM 2830 O O   . HOH H 3 .   ? 19.95100  -52.85500 -0.46200  1.000 50.54000  ? 427 HOH B O   1 
HETATM 2831 O O   . HOH H 3 .   ? 17.70000  -55.61300 -1.06100  1.000 57.35000  ? 428 HOH B O   1 
HETATM 2832 O O   . HOH H 3 .   ? 19.14600  -51.70600 3.16600   1.000 48.78000  ? 429 HOH B O   1 
# 
