data_9N9D
# 
_entry.id   9N9D 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9N9D         pdb_00009n9d 10.2210/pdb9n9d/pdb 
WWPDB D_1000292826 ?            ?                   
# 
_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       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9N9D 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-10 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jrodriguez@mbi.ucla.edu 
_pdbx_contact_author.name_first         Jose 
_pdbx_contact_author.name_last          Rodriguez 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0248-4964 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vlahakis, N.'    1 0000-0002-5092-0265 
'Rodriguez, J.A.' 2 0000-0002-0248-4964 
# 
_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            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Combining MicroED and native mass spectrometry for structural discovery of enzyme-biosynthetic inhibitor complexes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2025.02.20.638743 
_citation.pdbx_database_id_PubMed   40060639 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vlahakis, N.W.'  1  0000-0002-5092-0265 
primary 'Flowers, C.W.'   2  ?                   
primary 'Liu, M.'         3  ?                   
primary 'Agdanowski, M.'  4  ?                   
primary 'Johnson, S.'     5  ?                   
primary 'Summers, J.A.'   6  ?                   
primary 'Keyser, C.'      7  ?                   
primary 'Russell, P.'     8  ?                   
primary 'Rose, S.'        9  ?                   
primary 'Orlans, J.'      10 ?                   
primary 'Adhami, N.'      11 ?                   
primary 'Chen, Y.'        12 ?                   
primary 'Sawaya, M.R.'    13 ?                   
primary 'Basu, S.'        14 ?                   
primary 'de Sanctis, D.'  15 ?                   
primary 'Wakatsuki, S.'   16 ?                   
primary 'Nelson, H.M.'    17 ?                   
primary 'Loo, J.A.'       18 ?                   
primary 'Tang, Y.'        19 ?                   
primary 'Rodriguez, J.A.' 20 0000-0002-0248-4964 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat Papain                                                          23452.301 1  3.4.22.2 ? ? ? 
2 non-polymer syn 'N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-2-METHYL-BUTANE' 316.393   1  ?        ? ? ? 
3 water       nat water                                                           18.015    41 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Papaya proteinase I,PPI' 
# 
_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       
;IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGI
HYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHA
VAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGI
HYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHA
VAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-2-METHYL-BUTANE' E6C 
3 water                                                           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   PRO n 
1 3   GLU n 
1 4   TYR n 
1 5   VAL n 
1 6   ASP n 
1 7   TRP n 
1 8   ARG n 
1 9   GLN n 
1 10  LYS n 
1 11  GLY n 
1 12  ALA n 
1 13  VAL n 
1 14  THR n 
1 15  PRO n 
1 16  VAL n 
1 17  LYS n 
1 18  ASN n 
1 19  GLN n 
1 20  GLY n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  SER n 
1 25  CYS n 
1 26  TRP n 
1 27  ALA n 
1 28  PHE n 
1 29  SER n 
1 30  ALA n 
1 31  VAL n 
1 32  VAL n 
1 33  THR n 
1 34  ILE n 
1 35  GLU n 
1 36  GLY n 
1 37  ILE n 
1 38  ILE n 
1 39  LYS n 
1 40  ILE n 
1 41  ARG n 
1 42  THR n 
1 43  GLY n 
1 44  ASN n 
1 45  LEU n 
1 46  ASN n 
1 47  GLU n 
1 48  TYR n 
1 49  SER n 
1 50  GLU n 
1 51  GLN n 
1 52  GLU n 
1 53  LEU n 
1 54  LEU n 
1 55  ASP n 
1 56  CYS n 
1 57  ASP n 
1 58  ARG n 
1 59  ARG n 
1 60  SER n 
1 61  TYR n 
1 62  GLY n 
1 63  CYS n 
1 64  ASN n 
1 65  GLY n 
1 66  GLY n 
1 67  TYR n 
1 68  PRO n 
1 69  TRP n 
1 70  SER n 
1 71  ALA n 
1 72  LEU n 
1 73  GLN n 
1 74  LEU n 
1 75  VAL n 
1 76  ALA n 
1 77  GLN n 
1 78  TYR n 
1 79  GLY n 
1 80  ILE n 
1 81  HIS n 
1 82  TYR n 
1 83  ARG n 
1 84  ASN n 
1 85  THR n 
1 86  TYR n 
1 87  PRO n 
1 88  TYR n 
1 89  GLU n 
1 90  GLY n 
1 91  VAL n 
1 92  GLN n 
1 93  ARG n 
1 94  TYR n 
1 95  CYS n 
1 96  ARG n 
1 97  SER n 
1 98  ARG n 
1 99  GLU n 
1 100 LYS n 
1 101 GLY n 
1 102 PRO n 
1 103 TYR n 
1 104 ALA n 
1 105 ALA n 
1 106 LYS n 
1 107 THR n 
1 108 ASP n 
1 109 GLY n 
1 110 VAL n 
1 111 ARG n 
1 112 GLN n 
1 113 VAL n 
1 114 GLN n 
1 115 PRO n 
1 116 TYR n 
1 117 ASN n 
1 118 GLU n 
1 119 GLY n 
1 120 ALA n 
1 121 LEU n 
1 122 LEU n 
1 123 TYR n 
1 124 SER n 
1 125 ILE n 
1 126 ALA n 
1 127 ASN n 
1 128 GLN n 
1 129 PRO n 
1 130 VAL n 
1 131 SER n 
1 132 VAL n 
1 133 VAL n 
1 134 LEU n 
1 135 GLU n 
1 136 ALA n 
1 137 ALA n 
1 138 GLY n 
1 139 LYS n 
1 140 ASP n 
1 141 PHE n 
1 142 GLN n 
1 143 LEU n 
1 144 TYR n 
1 145 ARG n 
1 146 GLY n 
1 147 GLY n 
1 148 ILE n 
1 149 PHE n 
1 150 VAL n 
1 151 GLY n 
1 152 PRO n 
1 153 CYS n 
1 154 GLY n 
1 155 ASN n 
1 156 LYS n 
1 157 VAL n 
1 158 ASP n 
1 159 HIS n 
1 160 ALA n 
1 161 VAL n 
1 162 ALA n 
1 163 ALA n 
1 164 VAL n 
1 165 GLY n 
1 166 TYR n 
1 167 GLY n 
1 168 PRO n 
1 169 ASN n 
1 170 TYR n 
1 171 ILE n 
1 172 LEU n 
1 173 ILE n 
1 174 LYS n 
1 175 ASN n 
1 176 SER n 
1 177 TRP n 
1 178 GLY n 
1 179 THR n 
1 180 GLY n 
1 181 TRP n 
1 182 GLY n 
1 183 GLU n 
1 184 ASN n 
1 185 GLY n 
1 186 TYR n 
1 187 ILE n 
1 188 ARG n 
1 189 ILE n 
1 190 LYS n 
1 191 ARG n 
1 192 GLY n 
1 193 THR n 
1 194 GLY n 
1 195 ASN n 
1 196 SER n 
1 197 TYR n 
1 198 GLY n 
1 199 VAL n 
1 200 CYS n 
1 201 GLY n 
1 202 LEU n 
1 203 TYR n 
1 204 THR n 
1 205 SER n 
1 206 SER n 
1 207 PHE n 
1 208 TYR n 
1 209 PRO n 
1 210 VAL n 
1 211 LYS n 
1 212 ASN n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           212 
_entity_src_nat.common_name                papaya 
_entity_src_nat.pdbx_organism_scientific   'Carica papaya' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      3649 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
E6C non-polymer         . 'N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-2-METHYL-BUTANE' ? 'C15 H28 N2 O5'  316.393 
GLN 'L-peptide linking' y GLUTAMINE                                                       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                 ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                          ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE                                                   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ILE 1   1   1   ILE ILE A . n 
A 1 2   PRO 2   2   2   PRO PRO A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   TYR 4   4   4   TYR TYR A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   TRP 7   7   7   TRP TRP A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  THR 14  14  14  THR THR A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  CYS 25  25  25  CYS CYS A . n 
A 1 26  TRP 26  26  26  TRP TRP A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  CYS 56  56  56  CYS CYS A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  TYR 61  61  61  TYR TYR A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  CYS 63  63  63  CYS CYS A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  TRP 69  69  69  TRP TRP A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  HIS 81  81  81  HIS HIS A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  CYS 95  95  95  CYS CYS A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 GLN 112 112 112 GLN GLN A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 TYR 123 123 123 TYR TYR A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 GLN 142 142 142 GLN GLN A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 TYR 144 144 144 TYR TYR A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 CYS 153 153 153 CYS CYS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 HIS 159 159 159 HIS HIS A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 ASN 169 169 169 ASN ASN A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 TRP 177 177 177 TRP TRP A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 TRP 181 181 181 TRP TRP A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ASN 184 184 184 ASN ASN A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 ASN 195 195 195 ASN ASN A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 CYS 200 200 200 CYS CYS A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LYS 211 211 211 LYS LYS A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        E6C 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   E6C 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 E6C 1  301 301 E6C E6C A . 
C 3 HOH 1  401 5   HOH HOH A . 
C 3 HOH 2  402 42  HOH HOH A . 
C 3 HOH 3  403 21  HOH HOH A . 
C 3 HOH 4  404 1   HOH HOH A . 
C 3 HOH 5  405 18  HOH HOH A . 
C 3 HOH 6  406 11  HOH HOH A . 
C 3 HOH 7  407 23  HOH HOH A . 
C 3 HOH 8  408 2   HOH HOH A . 
C 3 HOH 9  409 13  HOH HOH A . 
C 3 HOH 10 410 36  HOH HOH A . 
C 3 HOH 11 411 9   HOH HOH A . 
C 3 HOH 12 412 29  HOH HOH A . 
C 3 HOH 13 413 28  HOH HOH A . 
C 3 HOH 14 414 35  HOH HOH A . 
C 3 HOH 15 415 19  HOH HOH A . 
C 3 HOH 16 416 16  HOH HOH A . 
C 3 HOH 17 417 43  HOH HOH A . 
C 3 HOH 18 418 17  HOH HOH A . 
C 3 HOH 19 419 6   HOH HOH A . 
C 3 HOH 20 420 24  HOH HOH A . 
C 3 HOH 21 421 15  HOH HOH A . 
C 3 HOH 22 422 32  HOH HOH A . 
C 3 HOH 23 423 38  HOH HOH A . 
C 3 HOH 24 424 30  HOH HOH A . 
C 3 HOH 25 425 10  HOH HOH A . 
C 3 HOH 26 426 4   HOH HOH A . 
C 3 HOH 27 427 39  HOH HOH A . 
C 3 HOH 28 428 40  HOH HOH A . 
C 3 HOH 29 429 14  HOH HOH A . 
C 3 HOH 30 430 20  HOH HOH A . 
C 3 HOH 31 431 33  HOH HOH A . 
C 3 HOH 32 432 25  HOH HOH A . 
C 3 HOH 33 433 26  HOH HOH A . 
C 3 HOH 34 434 7   HOH HOH A . 
C 3 HOH 35 435 34  HOH HOH A . 
C 3 HOH 36 436 27  HOH HOH A . 
C 3 HOH 37 437 22  HOH HOH A . 
C 3 HOH 38 438 12  HOH HOH A . 
C 3 HOH 39 439 37  HOH HOH A . 
C 3 HOH 40 440 8   HOH HOH A . 
C 3 HOH 41 441 31  HOH HOH A . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.location 
_software.classification 
_software.language 
_software.date 
_software.citation_id 
1 PHENIX 1.20.1_4487 program 'Paul D. Adams' pdadams@lbl.gov https://www.phenix-online.org/ refinement       Python/C++ ? ? 
2 XSCALE .           ?       ?               ?               ?                              'data scaling'   ?          ? ? 
3 XDS    .           ?       ?               ?               ?                              'data reduction' ?          ? ? 
4 PHASER .           ?       ?               ?               ?                              phasing          ?          ? ? 
# 
_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                     9N9D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.880 
_cell.length_a_esd                 ? 
_cell.length_b                     48.930 
_cell.length_b_esd                 ? 
_cell.length_c                     100.930 
_cell.length_c_esd                 ? 
_cell.volume                       206824.585 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9N9D 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9N9D 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON CRYSTALLOGRAPHY' 
_exptl.method_details             ? 
# 
_reflns.B_iso_Wilson_estimate                          24.58 
_reflns.entry_id                                       9N9D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              ? 
_reflns.d_resolution_low                               ? 
_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                                     ? 
_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                           ? 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          ? 
_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                                   ? 
_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                        ? 
# 
_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                               23.07 
_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                                 9N9D 
_refine.pdbx_refine_id                           'ELECTRON CRYSTALLOGRAPHY' 
_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                            2.20 
_refine.ls_d_res_low                             50.46 
_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                     10926 
_refine.ls_number_reflns_R_free                  1089 
_refine.ls_number_reflns_R_work                  9837 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.85 
_refine.ls_percent_reflns_R_free                 9.97 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1867 
_refine.ls_R_factor_R_free                       0.2363 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1812 
_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                 21.9301 
_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                            0.2816 
_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                   'ELECTRON CRYSTALLOGRAPHY' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        50.46 
_refine_hist.number_atoms_solvent             41 
_refine_hist.number_atoms_total               1718 
_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        1655 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         22 
_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 
'ELECTRON CRYSTALLOGRAPHY' ? 0.0090 ? 1805 ? f_bond_d           ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 1.3267 ? 2462 ? f_angle_d          ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.0884 ? 242  ? f_chiral_restr     ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.0137 ? 326  ? f_plane_restr      ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 6.4805 ? 265  ? 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 
'ELECTRON CRYSTALLOGRAPHY' 2.20 2.30 . . 131 1183 97.91 . . . . 0.2407 . . . . . . . . . . . 0.3143 
'ELECTRON CRYSTALLOGRAPHY' 2.30 2.42 . . 134 1205 99.78 . . . . 0.2406 . . . . . . . . . . . 0.3085 
'ELECTRON CRYSTALLOGRAPHY' 2.42 2.57 . . 136 1228 99.63 . . . . 0.2400 . . . . . . . . . . . 0.3070 
'ELECTRON CRYSTALLOGRAPHY' 2.57 2.77 . . 136 1218 99.71 . . . . 0.2401 . . . . . . . . . . . 0.2805 
'ELECTRON CRYSTALLOGRAPHY' 2.77 3.05 . . 138 1238 99.57 . . . . 0.2086 . . . . . . . . . . . 0.2960 
'ELECTRON CRYSTALLOGRAPHY' 3.05 3.49 . . 136 1232 99.27 . . . . 0.1718 . . . . . . . . . . . 0.2433 
'ELECTRON CRYSTALLOGRAPHY' 3.49 4.40 . . 137 1240 98.92 . . . . 0.1308 . . . . . . . . . . . 0.1621 
# 
_struct.entry_id                     9N9D 
_struct.title                        'MicroED structure of papain co-crystallized with E-64C' 
_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        9N9D 
_struct_keywords.text            'Inhibitor, Complex, Protease, MicroED, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PAPA1_CARPA 
_struct_ref.pdbx_db_accession          P00784 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGI
HYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHA
VAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
;
_struct_ref.pdbx_align_begin           134 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9N9D 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 212 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00784 
_struct_ref_seq.db_align_beg                  134 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  345 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       212 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 SER A 24  ? GLY A 43  ? SER A 24  GLY A 43  1 ? 20 
HELX_P HELX_P2 AA2 SER A 49  ? ASP A 57  ? SER A 49  ASP A 57  1 ? 9  
HELX_P HELX_P3 AA3 TYR A 61  ? GLY A 65  ? TYR A 61  GLY A 65  5 ? 5  
HELX_P HELX_P4 AA4 TYR A 67  ? TYR A 78  ? TYR A 67  TYR A 78  1 ? 12 
HELX_P HELX_P5 AA5 SER A 97  ? GLY A 101 ? SER A 97  GLY A 101 5 ? 5  
HELX_P HELX_P6 AA6 ASN A 117 ? GLN A 128 ? ASN A 117 GLN A 128 1 ? 12 
HELX_P HELX_P7 AA7 GLY A 138 ? LEU A 143 ? GLY A 138 LEU A 143 1 ? 6  
HELX_P HELX_P8 AA8 GLY A 198 ? LEU A 202 ? GLY A 198 LEU A 202 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 22  SG ? ? ? 1_555 A CYS 63  SG ? ? A CYS 22  A CYS 63  1_555 ? ? ? ? ? ? ? 2.054 ? ? 
disulf2 disulf ?    ? A CYS 56  SG ? ? ? 1_555 A CYS 95  SG ? ? A CYS 56  A CYS 95  1_555 ? ? ? ? ? ? ? 2.064 ? ? 
disulf3 disulf ?    ? A CYS 153 SG ? ? ? 1_555 A CYS 200 SG ? ? A CYS 153 A CYS 200 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
covale1 covale none ? A CYS 25  SG ? ? ? 1_555 B E6C .   C2 ? ? A CYS 25  A E6C 301 1_555 ? ? ? ? ? ? ? 1.801 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 E6C B .   ? CYS A 25  ? E6C A 301 ? 1_555 CYS A 25  ? 1_555 C2 SG CYS 1 E6C None 'Covalent chemical modification' 
2 CYS A 22  ? CYS A 63  ? CYS A 22  ? 1_555 CYS A 63  ? 1_555 SG SG .   . .   None 'Disulfide bridge'               
3 CYS A 56  ? CYS A 95  ? CYS A 56  ? 1_555 CYS A 95  ? 1_555 SG SG .   . .   None 'Disulfide bridge'               
4 CYS A 153 ? CYS A 200 ? CYS A 153 ? 1_555 CYS A 200 ? 1_555 SG SG .   . .   None 'Disulfide bridge'               
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           151 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            151 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    152 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     152 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       3.45 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 5   ? ASP A 6   ? VAL A 5   ASP A 6   
AA1 2 HIS A 159 ? GLY A 167 ? HIS A 159 GLY A 167 
AA1 3 VAL A 130 ? LEU A 134 ? VAL A 130 LEU A 134 
AA2 1 VAL A 5   ? ASP A 6   ? VAL A 5   ASP A 6   
AA2 2 HIS A 159 ? GLY A 167 ? HIS A 159 GLY A 167 
AA2 3 TYR A 170 ? LYS A 174 ? TYR A 170 LYS A 174 
AA2 4 TYR A 186 ? LYS A 190 ? TYR A 186 LYS A 190 
AA2 5 ILE A 148 ? PHE A 149 ? ILE A 148 PHE A 149 
AA3 1 GLY A 109 ? GLN A 112 ? GLY A 109 GLN A 112 
AA3 2 PHE A 207 ? VAL A 210 ? PHE A 207 VAL A 210 
# 
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 VAL A 5   ? N VAL A 5   O TYR A 166 ? O TYR A 166 
AA1 2 3 O ALA A 163 ? O ALA A 163 N VAL A 130 ? N VAL A 130 
AA2 1 2 N VAL A 5   ? N VAL A 5   O TYR A 166 ? O TYR A 166 
AA2 2 3 N ALA A 162 ? N ALA A 162 O LYS A 174 ? O LYS A 174 
AA2 3 4 N ILE A 173 ? N ILE A 173 O ILE A 187 ? O ILE A 187 
AA2 4 5 O ARG A 188 ? O ARG A 188 N PHE A 149 ? N PHE A 149 
AA3 1 2 N GLY A 109 ? N GLY A 109 O VAL A 210 ? O VAL A 210 
# 
_pdbx_entry_details.entry_id                   9N9D 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    PRO 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     15 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -48.29 
_pdbx_validate_torsion.psi             156.26 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9N9D 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  9PAP 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                9PAP 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9N9D 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.2 
_em_3d_reconstruction.resolution_method           'DIFFRACTION PATTERN/LAYERLINES' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               ? 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               '3D CRYSTAL' 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               NATURAL 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Papain-E-64C complex' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9N9D 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS TALOS F200C' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'GATAN 626 SINGLE TILT LIQUID NITROGEN CRYO TRANSFER HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            DIFFRACTION 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             1000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   100 
_em_imaging.recording_temperature_maximum   100 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            70 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9N9D 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9N9D 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   CRYSTALLOGRAPHY 
_em_experiment.aggregation_state       '3D ARRAY' 
_em_experiment.entity_assembly_id      1 
# 
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  
E6C O1   O N N 88  
E6C C2   C N N 89  
E6C C3   C N S 90  
E6C C4   C N N 91  
E6C O5   O N N 92  
E6C N6   N N N 93  
E6C C7   C N S 94  
E6C C8   C N N 95  
E6C O9   O N N 96  
E6C N10  N N N 97  
E6C C11  C N N 98  
E6C C12  C N N 99  
E6C C13  C N N 100 
E6C C14  C N N 101 
E6C C15  C N N 102 
E6C C16  C N N 103 
E6C O17  O N N 104 
E6C O18  O N N 105 
E6C C19  C N N 106 
E6C C20  C N N 107 
E6C C21  C N N 108 
E6C C22  C N N 109 
E6C HO1  H N N 110 
E6C H21  H N N 111 
E6C H22  H N N 112 
E6C H3   H N N 113 
E6C HN6  H N N 114 
E6C H7   H N N 115 
E6C HN1  H N N 116 
E6C H111 H N N 117 
E6C H112 H N N 118 
E6C H121 H N N 119 
E6C H122 H N N 120 
E6C H13  H N N 121 
E6C H141 H N N 122 
E6C H142 H N N 123 
E6C H143 H N N 124 
E6C H151 H N N 125 
E6C H152 H N N 126 
E6C H153 H N N 127 
E6C HO8  H N N 128 
E6C H191 H N N 129 
E6C H192 H N N 130 
E6C H20  H N N 131 
E6C H211 H N N 132 
E6C H212 H N N 133 
E6C H213 H N N 134 
E6C H221 H N N 135 
E6C H222 H N N 136 
E6C H223 H N N 137 
GLN N    N N N 138 
GLN CA   C N S 139 
GLN C    C N N 140 
GLN O    O N N 141 
GLN CB   C N N 142 
GLN CG   C N N 143 
GLN CD   C N N 144 
GLN OE1  O N N 145 
GLN NE2  N N N 146 
GLN OXT  O N N 147 
GLN H    H N N 148 
GLN H2   H N N 149 
GLN HA   H N N 150 
GLN HB2  H N N 151 
GLN HB3  H N N 152 
GLN HG2  H N N 153 
GLN HG3  H N N 154 
GLN HE21 H N N 155 
GLN HE22 H N N 156 
GLN HXT  H N N 157 
GLU N    N N N 158 
GLU CA   C N S 159 
GLU C    C N N 160 
GLU O    O N N 161 
GLU CB   C N N 162 
GLU CG   C N N 163 
GLU CD   C N N 164 
GLU OE1  O N N 165 
GLU OE2  O N N 166 
GLU OXT  O N N 167 
GLU H    H N N 168 
GLU H2   H N N 169 
GLU HA   H N N 170 
GLU HB2  H N N 171 
GLU HB3  H N N 172 
GLU HG2  H N N 173 
GLU HG3  H N N 174 
GLU HE2  H N N 175 
GLU HXT  H N N 176 
GLY N    N N N 177 
GLY CA   C N N 178 
GLY C    C N N 179 
GLY O    O N N 180 
GLY OXT  O N N 181 
GLY H    H N N 182 
GLY H2   H N N 183 
GLY HA2  H N N 184 
GLY HA3  H N N 185 
GLY HXT  H N N 186 
HIS N    N N N 187 
HIS CA   C N S 188 
HIS C    C N N 189 
HIS O    O N N 190 
HIS CB   C N N 191 
HIS CG   C Y N 192 
HIS ND1  N Y N 193 
HIS CD2  C Y N 194 
HIS CE1  C Y N 195 
HIS NE2  N Y N 196 
HIS OXT  O N N 197 
HIS H    H N N 198 
HIS H2   H N N 199 
HIS HA   H N N 200 
HIS HB2  H N N 201 
HIS HB3  H N N 202 
HIS HD1  H N N 203 
HIS HD2  H N N 204 
HIS HE1  H N N 205 
HIS HE2  H N N 206 
HIS HXT  H N N 207 
HOH O    O N N 208 
HOH H1   H N N 209 
HOH H2   H N N 210 
ILE N    N N N 211 
ILE CA   C N S 212 
ILE C    C N N 213 
ILE O    O N N 214 
ILE CB   C N S 215 
ILE CG1  C N N 216 
ILE CG2  C N N 217 
ILE CD1  C N N 218 
ILE OXT  O N N 219 
ILE H    H N N 220 
ILE H2   H N N 221 
ILE HA   H N N 222 
ILE HB   H N N 223 
ILE HG12 H N N 224 
ILE HG13 H N N 225 
ILE HG21 H N N 226 
ILE HG22 H N N 227 
ILE HG23 H N N 228 
ILE HD11 H N N 229 
ILE HD12 H N N 230 
ILE HD13 H N N 231 
ILE HXT  H N N 232 
LEU N    N N N 233 
LEU CA   C N S 234 
LEU C    C N N 235 
LEU O    O N N 236 
LEU CB   C N N 237 
LEU CG   C N N 238 
LEU CD1  C N N 239 
LEU CD2  C N N 240 
LEU OXT  O N N 241 
LEU H    H N N 242 
LEU H2   H N N 243 
LEU HA   H N N 244 
LEU HB2  H N N 245 
LEU HB3  H N N 246 
LEU HG   H N N 247 
LEU HD11 H N N 248 
LEU HD12 H N N 249 
LEU HD13 H N N 250 
LEU HD21 H N N 251 
LEU HD22 H N N 252 
LEU HD23 H N N 253 
LEU HXT  H N N 254 
LYS N    N N N 255 
LYS CA   C N S 256 
LYS C    C N N 257 
LYS O    O N N 258 
LYS CB   C N N 259 
LYS CG   C N N 260 
LYS CD   C N N 261 
LYS CE   C N N 262 
LYS NZ   N N N 263 
LYS OXT  O N N 264 
LYS H    H N N 265 
LYS H2   H N N 266 
LYS HA   H N N 267 
LYS HB2  H N N 268 
LYS HB3  H N N 269 
LYS HG2  H N N 270 
LYS HG3  H N N 271 
LYS HD2  H N N 272 
LYS HD3  H N N 273 
LYS HE2  H N N 274 
LYS HE3  H N N 275 
LYS HZ1  H N N 276 
LYS HZ2  H N N 277 
LYS HZ3  H N N 278 
LYS HXT  H N N 279 
PHE N    N N N 280 
PHE CA   C N S 281 
PHE C    C N N 282 
PHE O    O N N 283 
PHE CB   C N N 284 
PHE CG   C Y N 285 
PHE CD1  C Y N 286 
PHE CD2  C Y N 287 
PHE CE1  C Y N 288 
PHE CE2  C Y N 289 
PHE CZ   C Y N 290 
PHE OXT  O N N 291 
PHE H    H N N 292 
PHE H2   H N N 293 
PHE HA   H N N 294 
PHE HB2  H N N 295 
PHE HB3  H N N 296 
PHE HD1  H N N 297 
PHE HD2  H N N 298 
PHE HE1  H N N 299 
PHE HE2  H N N 300 
PHE HZ   H N N 301 
PHE HXT  H N N 302 
PRO N    N N N 303 
PRO CA   C N S 304 
PRO C    C N N 305 
PRO O    O N N 306 
PRO CB   C N N 307 
PRO CG   C N N 308 
PRO CD   C N N 309 
PRO OXT  O N N 310 
PRO H    H N N 311 
PRO HA   H N N 312 
PRO HB2  H N N 313 
PRO HB3  H N N 314 
PRO HG2  H N N 315 
PRO HG3  H N N 316 
PRO HD2  H N N 317 
PRO HD3  H N N 318 
PRO HXT  H N N 319 
SER N    N N N 320 
SER CA   C N S 321 
SER C    C N N 322 
SER O    O N N 323 
SER CB   C N N 324 
SER OG   O N N 325 
SER OXT  O N N 326 
SER H    H N N 327 
SER H2   H N N 328 
SER HA   H N N 329 
SER HB2  H N N 330 
SER HB3  H N N 331 
SER HG   H N N 332 
SER HXT  H N N 333 
THR N    N N N 334 
THR CA   C N S 335 
THR C    C N N 336 
THR O    O N N 337 
THR CB   C N R 338 
THR OG1  O N N 339 
THR CG2  C N N 340 
THR OXT  O N N 341 
THR H    H N N 342 
THR H2   H N N 343 
THR HA   H N N 344 
THR HB   H N N 345 
THR HG1  H N N 346 
THR HG21 H N N 347 
THR HG22 H N N 348 
THR HG23 H N N 349 
THR HXT  H N N 350 
TRP N    N N N 351 
TRP CA   C N S 352 
TRP C    C N N 353 
TRP O    O N N 354 
TRP CB   C N N 355 
TRP CG   C Y N 356 
TRP CD1  C Y N 357 
TRP CD2  C Y N 358 
TRP NE1  N Y N 359 
TRP CE2  C Y N 360 
TRP CE3  C Y N 361 
TRP CZ2  C Y N 362 
TRP CZ3  C Y N 363 
TRP CH2  C Y N 364 
TRP OXT  O N N 365 
TRP H    H N N 366 
TRP H2   H N N 367 
TRP HA   H N N 368 
TRP HB2  H N N 369 
TRP HB3  H N N 370 
TRP HD1  H N N 371 
TRP HE1  H N N 372 
TRP HE3  H N N 373 
TRP HZ2  H N N 374 
TRP HZ3  H N N 375 
TRP HH2  H N N 376 
TRP HXT  H N N 377 
TYR N    N N N 378 
TYR CA   C N S 379 
TYR C    C N N 380 
TYR O    O N N 381 
TYR CB   C N N 382 
TYR CG   C Y N 383 
TYR CD1  C Y N 384 
TYR CD2  C Y N 385 
TYR CE1  C Y N 386 
TYR CE2  C Y N 387 
TYR CZ   C Y N 388 
TYR OH   O N N 389 
TYR OXT  O N N 390 
TYR H    H N N 391 
TYR H2   H N N 392 
TYR HA   H N N 393 
TYR HB2  H N N 394 
TYR HB3  H N N 395 
TYR HD1  H N N 396 
TYR HD2  H N N 397 
TYR HE1  H N N 398 
TYR HE2  H N N 399 
TYR HH   H N N 400 
TYR HXT  H N N 401 
VAL N    N N N 402 
VAL CA   C N S 403 
VAL C    C N N 404 
VAL O    O N N 405 
VAL CB   C N N 406 
VAL CG1  C N N 407 
VAL CG2  C N N 408 
VAL OXT  O N N 409 
VAL H    H N N 410 
VAL H2   H N N 411 
VAL HA   H N N 412 
VAL HB   H N N 413 
VAL HG11 H N N 414 
VAL HG12 H N N 415 
VAL HG13 H N N 416 
VAL HG21 H N N 417 
VAL HG22 H N N 418 
VAL HG23 H N N 419 
VAL HXT  H N N 420 
# 
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  
E6C O1  C3   sing N N 83  
E6C O1  HO1  sing N N 84  
E6C C2  C3   sing N N 85  
E6C C2  C16  sing N N 86  
E6C C2  H21  sing N N 87  
E6C C2  H22  sing N N 88  
E6C C3  C4   sing N N 89  
E6C C3  H3   sing N N 90  
E6C C4  O5   doub N N 91  
E6C C4  N6   sing N N 92  
E6C N6  C7   sing N N 93  
E6C N6  HN6  sing N N 94  
E6C C7  C8   sing N N 95  
E6C C7  C19  sing N N 96  
E6C C7  H7   sing N N 97  
E6C C8  O9   doub N N 98  
E6C C8  N10  sing N N 99  
E6C N10 C11  sing N N 100 
E6C N10 HN1  sing N N 101 
E6C C11 C12  sing N N 102 
E6C C11 H111 sing N N 103 
E6C C11 H112 sing N N 104 
E6C C12 C13  sing N N 105 
E6C C12 H121 sing N N 106 
E6C C12 H122 sing N N 107 
E6C C13 C14  sing N N 108 
E6C C13 C15  sing N N 109 
E6C C13 H13  sing N N 110 
E6C C14 H141 sing N N 111 
E6C C14 H142 sing N N 112 
E6C C14 H143 sing N N 113 
E6C C15 H151 sing N N 114 
E6C C15 H152 sing N N 115 
E6C C15 H153 sing N N 116 
E6C C16 O17  doub N N 117 
E6C C16 O18  sing N N 118 
E6C O18 HO8  sing N N 119 
E6C C19 C20  sing N N 120 
E6C C19 H191 sing N N 121 
E6C C19 H192 sing N N 122 
E6C C20 C21  sing N N 123 
E6C C20 C22  sing N N 124 
E6C C20 H20  sing N N 125 
E6C C21 H211 sing N N 126 
E6C C21 H212 sing N N 127 
E6C C21 H213 sing N N 128 
E6C C22 H221 sing N N 129 
E6C C22 H222 sing N N 130 
E6C C22 H223 sing N N 131 
GLN N   CA   sing N N 132 
GLN N   H    sing N N 133 
GLN N   H2   sing N N 134 
GLN CA  C    sing N N 135 
GLN CA  CB   sing N N 136 
GLN CA  HA   sing N N 137 
GLN C   O    doub N N 138 
GLN C   OXT  sing N N 139 
GLN CB  CG   sing N N 140 
GLN CB  HB2  sing N N 141 
GLN CB  HB3  sing N N 142 
GLN CG  CD   sing N N 143 
GLN CG  HG2  sing N N 144 
GLN CG  HG3  sing N N 145 
GLN CD  OE1  doub N N 146 
GLN CD  NE2  sing N N 147 
GLN NE2 HE21 sing N N 148 
GLN NE2 HE22 sing N N 149 
GLN OXT HXT  sing N N 150 
GLU N   CA   sing N N 151 
GLU N   H    sing N N 152 
GLU N   H2   sing N N 153 
GLU CA  C    sing N N 154 
GLU CA  CB   sing N N 155 
GLU CA  HA   sing N N 156 
GLU C   O    doub N N 157 
GLU C   OXT  sing N N 158 
GLU CB  CG   sing N N 159 
GLU CB  HB2  sing N N 160 
GLU CB  HB3  sing N N 161 
GLU CG  CD   sing N N 162 
GLU CG  HG2  sing N N 163 
GLU CG  HG3  sing N N 164 
GLU CD  OE1  doub N N 165 
GLU CD  OE2  sing N N 166 
GLU OE2 HE2  sing N N 167 
GLU OXT HXT  sing N N 168 
GLY N   CA   sing N N 169 
GLY N   H    sing N N 170 
GLY N   H2   sing N N 171 
GLY CA  C    sing N N 172 
GLY CA  HA2  sing N N 173 
GLY CA  HA3  sing N N 174 
GLY C   O    doub N N 175 
GLY C   OXT  sing N N 176 
GLY OXT HXT  sing N N 177 
HIS N   CA   sing N N 178 
HIS N   H    sing N N 179 
HIS N   H2   sing N N 180 
HIS CA  C    sing N N 181 
HIS CA  CB   sing N N 182 
HIS CA  HA   sing N N 183 
HIS C   O    doub N N 184 
HIS C   OXT  sing N N 185 
HIS CB  CG   sing N N 186 
HIS CB  HB2  sing N N 187 
HIS CB  HB3  sing N N 188 
HIS CG  ND1  sing Y N 189 
HIS CG  CD2  doub Y N 190 
HIS ND1 CE1  doub Y N 191 
HIS ND1 HD1  sing N N 192 
HIS CD2 NE2  sing Y N 193 
HIS CD2 HD2  sing N N 194 
HIS CE1 NE2  sing Y N 195 
HIS CE1 HE1  sing N N 196 
HIS NE2 HE2  sing N N 197 
HIS OXT HXT  sing N N 198 
HOH O   H1   sing N N 199 
HOH O   H2   sing N N 200 
ILE N   CA   sing N N 201 
ILE N   H    sing N N 202 
ILE N   H2   sing N N 203 
ILE CA  C    sing N N 204 
ILE CA  CB   sing N N 205 
ILE CA  HA   sing N N 206 
ILE C   O    doub N N 207 
ILE C   OXT  sing N N 208 
ILE CB  CG1  sing N N 209 
ILE CB  CG2  sing N N 210 
ILE CB  HB   sing N N 211 
ILE CG1 CD1  sing N N 212 
ILE CG1 HG12 sing N N 213 
ILE CG1 HG13 sing N N 214 
ILE CG2 HG21 sing N N 215 
ILE CG2 HG22 sing N N 216 
ILE CG2 HG23 sing N N 217 
ILE CD1 HD11 sing N N 218 
ILE CD1 HD12 sing N N 219 
ILE CD1 HD13 sing N N 220 
ILE OXT HXT  sing N N 221 
LEU N   CA   sing N N 222 
LEU N   H    sing N N 223 
LEU N   H2   sing N N 224 
LEU CA  C    sing N N 225 
LEU CA  CB   sing N N 226 
LEU CA  HA   sing N N 227 
LEU C   O    doub N N 228 
LEU C   OXT  sing N N 229 
LEU CB  CG   sing N N 230 
LEU CB  HB2  sing N N 231 
LEU CB  HB3  sing N N 232 
LEU CG  CD1  sing N N 233 
LEU CG  CD2  sing N N 234 
LEU CG  HG   sing N N 235 
LEU CD1 HD11 sing N N 236 
LEU CD1 HD12 sing N N 237 
LEU CD1 HD13 sing N N 238 
LEU CD2 HD21 sing N N 239 
LEU CD2 HD22 sing N N 240 
LEU CD2 HD23 sing N N 241 
LEU OXT HXT  sing N N 242 
LYS N   CA   sing N N 243 
LYS N   H    sing N N 244 
LYS N   H2   sing N N 245 
LYS CA  C    sing N N 246 
LYS CA  CB   sing N N 247 
LYS CA  HA   sing N N 248 
LYS C   O    doub N N 249 
LYS C   OXT  sing N N 250 
LYS CB  CG   sing N N 251 
LYS CB  HB2  sing N N 252 
LYS CB  HB3  sing N N 253 
LYS CG  CD   sing N N 254 
LYS CG  HG2  sing N N 255 
LYS CG  HG3  sing N N 256 
LYS CD  CE   sing N N 257 
LYS CD  HD2  sing N N 258 
LYS CD  HD3  sing N N 259 
LYS CE  NZ   sing N N 260 
LYS CE  HE2  sing N N 261 
LYS CE  HE3  sing N N 262 
LYS NZ  HZ1  sing N N 263 
LYS NZ  HZ2  sing N N 264 
LYS NZ  HZ3  sing N N 265 
LYS OXT HXT  sing N N 266 
PHE N   CA   sing N N 267 
PHE N   H    sing N N 268 
PHE N   H2   sing N N 269 
PHE CA  C    sing N N 270 
PHE CA  CB   sing N N 271 
PHE CA  HA   sing N N 272 
PHE C   O    doub N N 273 
PHE C   OXT  sing N N 274 
PHE CB  CG   sing N N 275 
PHE CB  HB2  sing N N 276 
PHE CB  HB3  sing N N 277 
PHE CG  CD1  doub Y N 278 
PHE CG  CD2  sing Y N 279 
PHE CD1 CE1  sing Y N 280 
PHE CD1 HD1  sing N N 281 
PHE CD2 CE2  doub Y N 282 
PHE CD2 HD2  sing N N 283 
PHE CE1 CZ   doub Y N 284 
PHE CE1 HE1  sing N N 285 
PHE CE2 CZ   sing Y N 286 
PHE CE2 HE2  sing N N 287 
PHE CZ  HZ   sing N N 288 
PHE OXT HXT  sing N N 289 
PRO N   CA   sing N N 290 
PRO N   CD   sing N N 291 
PRO N   H    sing N N 292 
PRO CA  C    sing N N 293 
PRO CA  CB   sing N N 294 
PRO CA  HA   sing N N 295 
PRO C   O    doub N N 296 
PRO C   OXT  sing N N 297 
PRO CB  CG   sing N N 298 
PRO CB  HB2  sing N N 299 
PRO CB  HB3  sing N N 300 
PRO CG  CD   sing N N 301 
PRO CG  HG2  sing N N 302 
PRO CG  HG3  sing N N 303 
PRO CD  HD2  sing N N 304 
PRO CD  HD3  sing N N 305 
PRO OXT HXT  sing N N 306 
SER N   CA   sing N N 307 
SER N   H    sing N N 308 
SER N   H2   sing N N 309 
SER CA  C    sing N N 310 
SER CA  CB   sing N N 311 
SER CA  HA   sing N N 312 
SER C   O    doub N N 313 
SER C   OXT  sing N N 314 
SER CB  OG   sing N N 315 
SER CB  HB2  sing N N 316 
SER CB  HB3  sing N N 317 
SER OG  HG   sing N N 318 
SER OXT HXT  sing N N 319 
THR N   CA   sing N N 320 
THR N   H    sing N N 321 
THR N   H2   sing N N 322 
THR CA  C    sing N N 323 
THR CA  CB   sing N N 324 
THR CA  HA   sing N N 325 
THR C   O    doub N N 326 
THR C   OXT  sing N N 327 
THR CB  OG1  sing N N 328 
THR CB  CG2  sing N N 329 
THR CB  HB   sing N N 330 
THR OG1 HG1  sing N N 331 
THR CG2 HG21 sing N N 332 
THR CG2 HG22 sing N N 333 
THR CG2 HG23 sing N N 334 
THR OXT HXT  sing N N 335 
TRP N   CA   sing N N 336 
TRP N   H    sing N N 337 
TRP N   H2   sing N N 338 
TRP CA  C    sing N N 339 
TRP CA  CB   sing N N 340 
TRP CA  HA   sing N N 341 
TRP C   O    doub N N 342 
TRP C   OXT  sing N N 343 
TRP CB  CG   sing N N 344 
TRP CB  HB2  sing N N 345 
TRP CB  HB3  sing N N 346 
TRP CG  CD1  doub Y N 347 
TRP CG  CD2  sing Y N 348 
TRP CD1 NE1  sing Y N 349 
TRP CD1 HD1  sing N N 350 
TRP CD2 CE2  doub Y N 351 
TRP CD2 CE3  sing Y N 352 
TRP NE1 CE2  sing Y N 353 
TRP NE1 HE1  sing N N 354 
TRP CE2 CZ2  sing Y N 355 
TRP CE3 CZ3  doub Y N 356 
TRP CE3 HE3  sing N N 357 
TRP CZ2 CH2  doub Y N 358 
TRP CZ2 HZ2  sing N N 359 
TRP CZ3 CH2  sing Y N 360 
TRP CZ3 HZ3  sing N N 361 
TRP CH2 HH2  sing N N 362 
TRP OXT HXT  sing N N 363 
TYR N   CA   sing N N 364 
TYR N   H    sing N N 365 
TYR N   H2   sing N N 366 
TYR CA  C    sing N N 367 
TYR CA  CB   sing N N 368 
TYR CA  HA   sing N N 369 
TYR C   O    doub N N 370 
TYR C   OXT  sing N N 371 
TYR CB  CG   sing N N 372 
TYR CB  HB2  sing N N 373 
TYR CB  HB3  sing N N 374 
TYR CG  CD1  doub Y N 375 
TYR CG  CD2  sing Y N 376 
TYR CD1 CE1  sing Y N 377 
TYR CD1 HD1  sing N N 378 
TYR CD2 CE2  doub Y N 379 
TYR CD2 HD2  sing N N 380 
TYR CE1 CZ   doub Y N 381 
TYR CE1 HE1  sing N N 382 
TYR CE2 CZ   sing Y N 383 
TYR CE2 HE2  sing N N 384 
TYR CZ  OH   sing N N 385 
TYR OH  HH   sing N N 386 
TYR OXT HXT  sing N N 387 
VAL N   CA   sing N N 388 
VAL N   H    sing N N 389 
VAL N   H2   sing N N 390 
VAL CA  C    sing N N 391 
VAL CA  CB   sing N N 392 
VAL CA  HA   sing N N 393 
VAL C   O    doub N N 394 
VAL C   OXT  sing N N 395 
VAL CB  CG1  sing N N 396 
VAL CB  CG2  sing N N 397 
VAL CB  HB   sing N N 398 
VAL CG1 HG11 sing N N 399 
VAL CG1 HG12 sing N N 400 
VAL CG1 HG13 sing N N 401 
VAL CG2 HG21 sing N N 402 
VAL CG2 HG22 sing N N 403 
VAL CG2 HG23 sing N N 404 
VAL OXT HXT  sing N N 405 
# 
_em_3d_crystal_entity.angle_alpha           90 
_em_3d_crystal_entity.angle_beta            90 
_em_3d_crystal_entity.angle_gamma           90 
_em_3d_crystal_entity.image_processing_id   1 
_em_3d_crystal_entity.id                    1 
_em_3d_crystal_entity.length_a              41.88 
_em_3d_crystal_entity.length_b              48.93 
_em_3d_crystal_entity.length_c              100.93 
_em_3d_crystal_entity.space_group_name      'P 21 21 21' 
_em_3d_crystal_entity.space_group_num       19 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_diffraction_shell.em_diffraction_stats_id   1 
_em_diffraction_shell.fourier_space_coverage    97.8 
_em_diffraction_shell.high_resolution           2.2 
_em_diffraction_shell.id                        1 
_em_diffraction_shell.low_resolution            2.3 
_em_diffraction_shell.multiplicity              4.0 
_em_diffraction_shell.num_structure_factors     5189 
_em_diffraction_shell.phase_residual            31.4 
# 
_em_diffraction_stats.details                          ? 
_em_diffraction_stats.fourier_space_coverage           98.7 
_em_diffraction_stats.high_resolution                  2.2 
_em_diffraction_stats.id                               1 
_em_diffraction_stats.image_processing_id              1 
_em_diffraction_stats.num_intensities_measured         43354 
_em_diffraction_stats.num_structure_factors            10957 
_em_diffraction_stats.overall_phase_error              ? 
_em_diffraction_stats.overall_phase_residual           ? 
_em_diffraction_stats.phase_error_rejection_criteria   NULL 
_em_diffraction_stats.r_merge                          26.8 
_em_diffraction_stats.r_sym                            ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          3649 
_em_entity_assembly_naturalsource.organism             'Carica papaya' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         0.045 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'DIRECT ELECTRON APOLLO (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'IMAGE ACQUISITION'             ? 1  ? ? 1 ? ? 
MASKING                         ? 2  ? ? ? ? ? 
'CTF CORRECTION'                ? 3  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 4  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 5  ? ? ? ? ? 
'MODEL FITTING'                 ? 6  ? 1 ? ? ? 
OTHER                           ? 7  ? ? ? ? ? 
'MOLECULAR REPLACEMENT'         ? 8  1 ? ? ? ? 
'LATTICE DISTORTION CORRECTION' ? 9  1 ? ? ? ? 
'SYMMETRY DETERMINATION'        ? 10 1 ? ? ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 11 1 ? ? ? ? 
RECONSTRUCTION                  ? 12 1 ? ? ? ? 
'MODEL REFINEMENT'              ? 13 ? 1 ? ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 'Crystallized in the presence of E-64C' 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Howard Hughes Medical Institute (HHMI)'           'United States' HHMI-EPI          1 
'Department of Energy (DOE, United States)'        'United States' DE-FC02-02ER63421 2 
'National Science Foundation (NSF, United States)' 'United States' DMR-1548924       3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9PAP 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9N9D 
_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]   0.023878 
_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]   0.020437 
_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]   0.009908 
_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.pdbx_scat_Cromer_Mann_a5 
_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.pdbx_scat_Cromer_Mann_b5 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 0.08930 0.25630 0.75700 1.04870 0.35750 0.24650 1.71000 6.40940 18.61130 50.25230 0.0 
;5-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 0.10220 0.32190 0.79820 0.81970 0.17150 0.24510 1.74810 6.19250 17.38940 48.14310 0.0 
;5-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 0.09740 0.29210 0.69100 0.69900 0.20390 0.20670 1.38150 4.69430 12.71050 32.47260 0.0 
;5-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 0.24970 0.56280 1.38990 2.18650 0.77150 0.26810 1.67110 7.02670 19.53770 50.38880 0.0 
;5-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   . ILE A 1 1   ? 22.42588  -10.30303 20.71029 1.000 23.82518 ? 1   ILE A N   1 
ATOM   2    C CA  . ILE A 1 1   ? 22.17666  -9.33158  19.64550 1.000 23.70341 ? 1   ILE A CA  1 
ATOM   3    C C   . ILE A 1 1   ? 23.44587  -8.50461  19.36349 1.000 15.52335 ? 1   ILE A C   1 
ATOM   4    O O   . ILE A 1 1   ? 24.21460  -8.20966  20.28077 1.000 27.24164 ? 1   ILE A O   1 
ATOM   5    C CB  . ILE A 1 1   ? 20.97597  -8.42510  19.99895 1.000 24.33528 ? 1   ILE A CB  1 
ATOM   6    C CG1 . ILE A 1 1   ? 21.25594  -7.61303  21.27106 1.000 14.22777 ? 1   ILE A CG1 1 
ATOM   7    C CG2 . ILE A 1 1   ? 19.74844  -9.28120  20.21322 1.000 17.75679 ? 1   ILE A CG2 1 
ATOM   8    C CD1 . ILE A 1 1   ? 20.04044  -6.84004  21.80300 1.000 19.99507 ? 1   ILE A CD1 1 
ATOM   9    N N   . PRO A 1 2   ? 23.63534  -8.11482  18.10013 1.000 20.99140 ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 2   ? 24.83332  -7.35405  17.70144 1.000 21.51536 ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 2   ? 24.95212  -6.01566  18.41309 1.000 20.66633 ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 2   ? 23.99998  -5.48786  18.98992 1.000 14.87105 ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 2   ? 24.65319  -7.13274  16.19350 1.000 9.98788  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 2   ? 23.44630  -7.88882  15.79791 1.000 25.66144 ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 2   ? 22.65594  -8.23294  17.00983 1.000 18.87678 ? 2   PRO A CD  1 
ATOM   16   N N   . GLU A 1 3   ? 26.16629  -5.47484  18.36537 1.000 15.39763 ? 3   GLU A N   1 
ATOM   17   C CA  . GLU A 1 3   ? 26.42382  -4.15457  18.92378 1.000 22.50663 ? 3   GLU A CA  1 
ATOM   18   C C   . GLU A 1 3   ? 25.76363  -3.06896  18.08749 1.000 17.98006 ? 3   GLU A C   1 
ATOM   19   O O   . GLU A 1 3   ? 25.26276  -2.08333  18.63578 1.000 18.23290 ? 3   GLU A O   1 
ATOM   20   C CB  . GLU A 1 3   ? 27.93262  -3.89266  18.99805 1.000 22.53605 ? 3   GLU A CB  1 
ATOM   21   C CG  . GLU A 1 3   ? 28.71594  -4.90704  19.81717 1.000 41.87462 ? 3   GLU A CG  1 
ATOM   22   C CD  . GLU A 1 3   ? 29.15809  -4.35080  21.16602 1.000 43.41840 ? 3   GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 3   ? 30.14488  -3.58283  21.20621 1.000 45.84156 ? 3   GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 3   ? 28.51162  -4.66569  22.18643 1.000 53.07185 ? 3   GLU A OE2 1 
ATOM   25   N N   . TYR A 1 4   ? 25.71095  -3.25305  16.77159 1.000 9.64349  ? 4   TYR A N   1 
ATOM   26   C CA  . TYR A 1 4   ? 25.08420  -2.30548  15.86838 1.000 14.59459 ? 4   TYR A CA  1 
ATOM   27   C C   . TYR A 1 4   ? 23.96097  -2.98204  15.10215 1.000 21.03088 ? 4   TYR A C   1 
ATOM   28   O O   . TYR A 1 4   ? 24.12482  -4.09155  14.58556 1.000 20.42685 ? 4   TYR A O   1 
ATOM   29   C CB  . TYR A 1 4   ? 26.12176  -1.78284  14.86790 1.000 11.69551 ? 4   TYR A CB  1 
ATOM   30   C CG  . TYR A 1 4   ? 27.09652  -0.81978  15.50063 1.000 17.47190 ? 4   TYR A CG  1 
ATOM   31   C CD1 . TYR A 1 4   ? 26.83063  0.54010   15.57615 1.000 19.88144 ? 4   TYR A CD1 1 
ATOM   32   C CD2 . TYR A 1 4   ? 28.31175  -1.28734  16.01151 1.000 29.03763 ? 4   TYR A CD2 1 
ATOM   33   C CE1 . TYR A 1 4   ? 27.73888  1.41848   16.15603 1.000 19.47703 ? 4   TYR A CE1 1 
ATOM   34   C CE2 . TYR A 1 4   ? 29.22419  -0.42321  16.58577 1.000 23.50610 ? 4   TYR A CE2 1 
ATOM   35   C CZ  . TYR A 1 4   ? 28.92981  0.92565   16.65623 1.000 23.30002 ? 4   TYR A CZ  1 
ATOM   36   O OH  . TYR A 1 4   ? 29.82439  1.79895   17.23202 1.000 30.83619 ? 4   TYR A OH  1 
ATOM   37   N N   . VAL A 1 5   ? 22.83064  -2.29129  15.00600 1.000 18.11539 ? 5   VAL A N   1 
ATOM   38   C CA  . VAL A 1 5   ? 21.73283  -2.68047  14.13520 1.000 12.73840 ? 5   VAL A CA  1 
ATOM   39   C C   . VAL A 1 5   ? 21.33624  -1.43584  13.36194 1.000 8.80426  ? 5   VAL A C   1 
ATOM   40   O O   . VAL A 1 5   ? 21.30551  -0.34889  13.93958 1.000 12.75311 ? 5   VAL A O   1 
ATOM   41   C CB  . VAL A 1 5   ? 20.52636  -3.22735  14.92402 1.000 13.71128 ? 5   VAL A CB  1 
ATOM   42   C CG1 . VAL A 1 5   ? 19.27643  -3.15947  14.06585 1.000 14.41993 ? 5   VAL A CG1 1 
ATOM   43   C CG2 . VAL A 1 5   ? 20.78509  -4.65573  15.45851 1.000 15.22881 ? 5   VAL A CG2 1 
ATOM   44   N N   . ASP A 1 6   ? 21.25069  -1.54988  12.03337 1.000 16.29911 ? 6   ASP A N   1 
ATOM   45   C CA  . ASP A 1 6   ? 20.75946  -0.45088  11.19592 1.000 18.53924 ? 6   ASP A CA  1 
ATOM   46   C C   . ASP A 1 6   ? 19.84795  -1.04809  10.12724 1.000 16.63738 ? 6   ASP A C   1 
ATOM   47   O O   . ASP A 1 6   ? 20.33867  -1.57001  9.12209  1.000 17.17271 ? 6   ASP A O   1 
ATOM   48   C CB  . ASP A 1 6   ? 21.90428  0.33961   10.56728 1.000 23.55190 ? 6   ASP A CB  1 
ATOM   49   C CG  . ASP A 1 6   ? 21.44010  1.67086   9.93997  1.000 20.15511 ? 6   ASP A CG  1 
ATOM   50   O OD1 . ASP A 1 6   ? 20.28454  1.78144   9.46124  1.000 15.25016 ? 6   ASP A OD1 1 
ATOM   51   O OD2 . ASP A 1 6   ? 22.25456  2.62074   9.94177  1.000 20.27810 ? 6   ASP A OD2 1 
ATOM   52   N N   . TRP A 1 7   ? 18.53694  -0.92998  10.30023 1.000 12.48265 ? 7   TRP A N   1 
ATOM   53   C CA  . TRP A 1 7   ? 17.64635  -1.48058  9.28670  1.000 13.66057 ? 7   TRP A CA  1 
ATOM   54   C C   . TRP A 1 7   ? 17.75220  -0.79407  7.93562  1.000 8.34140  ? 7   TRP A C   1 
ATOM   55   O O   . TRP A 1 7   ? 17.29654  -1.35938  6.94382  1.000 15.05671 ? 7   TRP A O   1 
ATOM   56   C CB  . TRP A 1 7   ? 16.23109  -1.53089  9.81827  1.000 12.88585 ? 7   TRP A CB  1 
ATOM   57   C CG  . TRP A 1 7   ? 16.16239  -2.63991  10.78845 1.000 19.15927 ? 7   TRP A CG  1 
ATOM   58   C CD1 . TRP A 1 7   ? 15.99006  -2.58967  12.15052 1.000 18.90098 ? 7   TRP A CD1 1 
ATOM   59   C CD2 . TRP A 1 7   ? 16.26786  -4.02144  10.43916 1.000 24.25824 ? 7   TRP A CD2 1 
ATOM   60   N NE1 . TRP A 1 7   ? 15.98579  -3.87970  12.66584 1.000 17.35358 ? 7   TRP A NE1 1 
ATOM   61   C CE2 . TRP A 1 7   ? 16.15694  -4.76779  11.63151 1.000 19.76701 ? 7   TRP A CE2 1 
ATOM   62   C CE3 . TRP A 1 7   ? 16.44023  -4.70449  9.21773  1.000 19.10484 ? 7   TRP A CE3 1 
ATOM   63   C CZ2 . TRP A 1 7   ? 16.20784  -6.15705  11.63665 1.000 19.87151 ? 7   TRP A CZ2 1 
ATOM   64   C CZ3 . TRP A 1 7   ? 16.48580  -6.08126  9.22683  1.000 27.45254 ? 7   TRP A CZ3 1 
ATOM   65   C CH2 . TRP A 1 7   ? 16.36891  -6.79430  10.42435 1.000 27.93642 ? 7   TRP A CH2 1 
ATOM   66   N N   . ARG A 1 8   ? 18.36276  0.38057   7.85737  1.000 17.57433 ? 8   ARG A N   1 
ATOM   67   C CA  . ARG A 1 8   ? 18.51288  1.01062   6.54852  1.000 15.22900 ? 8   ARG A CA  1 
ATOM   68   C C   . ARG A 1 8   ? 19.52635  0.22874   5.71605  1.000 14.76094 ? 8   ARG A C   1 
ATOM   69   O O   . ARG A 1 8   ? 19.34906  0.03876   4.50954  1.000 15.74230 ? 8   ARG A O   1 
ATOM   70   C CB  . ARG A 1 8   ? 18.93593  2.46325   6.68577  1.000 10.68988 ? 8   ARG A CB  1 
ATOM   71   C CG  . ARG A 1 8   ? 18.05953  3.28909   7.55410  1.000 20.63328 ? 8   ARG A CG  1 
ATOM   72   C CD  . ARG A 1 8   ? 18.71104  4.63490   7.67617  1.000 18.02888 ? 8   ARG A CD  1 
ATOM   73   N NE  . ARG A 1 8   ? 19.93571  4.58334   8.46188  1.000 12.16376 ? 8   ARG A NE  1 
ATOM   74   C CZ  . ARG A 1 8   ? 20.51183  5.65837   8.97312  1.000 22.88695 ? 8   ARG A CZ  1 
ATOM   75   N NH1 . ARG A 1 8   ? 20.02028  6.87532   8.75367  1.000 14.41151 ? 8   ARG A NH1 1 
ATOM   76   N NH2 . ARG A 1 8   ? 21.58812  5.51409   9.73831  1.000 15.52082 ? 8   ARG A NH2 1 
ATOM   77   N N   . GLN A 1 9   ? 20.57549  -0.26883  6.35742  1.000 28.89818 ? 9   GLN A N   1 
ATOM   78   C CA  . GLN A 1 9   ? 21.60530  -1.00043  5.63632  1.000 19.74099 ? 9   GLN A CA  1 
ATOM   79   C C   . GLN A 1 9   ? 21.05096  -2.31131  5.11596  1.000 26.73847 ? 9   GLN A C   1 
ATOM   80   O O   . GLN A 1 9   ? 21.50162  -2.81567  4.08278  1.000 34.64940 ? 9   GLN A O   1 
ATOM   81   C CB  . GLN A 1 9   ? 22.78943  -1.25147  6.56656  1.000 24.47083 ? 9   GLN A CB  1 
ATOM   82   C CG  . GLN A 1 9   ? 23.60352  -0.01800  6.80568  1.000 24.43943 ? 9   GLN A CG  1 
ATOM   83   C CD  . GLN A 1 9   ? 24.72422  -0.24502  7.81078  1.000 50.14372 ? 9   GLN A CD  1 
ATOM   84   O OE1 . GLN A 1 9   ? 24.85569  -1.32368  8.38587  1.000 41.37059 ? 9   GLN A OE1 1 
ATOM   85   N NE2 . GLN A 1 9   ? 25.43139  0.82986   8.14492  1.000 45.94468 ? 9   GLN A NE2 1 
ATOM   86   N N   . LYS A 1 10  ? 20.10648  -2.89317  5.83776  1.000 24.80204 ? 10  LYS A N   1 
ATOM   87   C CA  . LYS A 1 10  ? 19.53443  -4.16753  5.45062  1.000 14.91158 ? 10  LYS A CA  1 
ATOM   88   C C   . LYS A 1 10  ? 18.41334  -4.01521  4.42818  1.000 20.25002 ? 10  LYS A C   1 
ATOM   89   O O   . LYS A 1 10  ? 17.81787  -5.02437  4.03406  1.000 26.72910 ? 10  LYS A O   1 
ATOM   90   C CB  . LYS A 1 10  ? 19.05025  -4.88047  6.71720  1.000 27.96107 ? 10  LYS A CB  1 
ATOM   91   C CG  . LYS A 1 10  ? 20.21835  -5.58659  7.45926  1.000 27.24478 ? 10  LYS A CG  1 
ATOM   92   C CD  . LYS A 1 10  ? 20.36724  -7.05518  7.09311  1.000 50.76015 ? 10  LYS A CD  1 
ATOM   93   C CE  . LYS A 1 10  ? 19.31524  -7.89393  7.81203  1.000 59.19963 ? 10  LYS A CE  1 
ATOM   94   N NZ  . LYS A 1 10  ? 19.34103  -9.30984  7.38295  1.000 45.61410 ? 10  LYS A NZ  1 
ATOM   95   N N   . GLY A 1 11  ? 18.13770  -2.78885  3.96648  1.000 14.81634 ? 11  GLY A N   1 
ATOM   96   C CA  . GLY A 1 11  ? 17.13944  -2.57010  2.93374  1.000 17.21314 ? 11  GLY A CA  1 
ATOM   97   C C   . GLY A 1 11  ? 15.71009  -2.59489  3.41892  1.000 22.72501 ? 11  GLY A C   1 
ATOM   98   O O   . GLY A 1 11  ? 14.79836  -2.80148  2.61212  1.000 25.54129 ? 11  GLY A O   1 
ATOM   99   N N   . ALA A 1 12  ? 15.48175  -2.33334  4.70718  1.000 23.77367 ? 12  ALA A N   1 
ATOM   100  C CA  . ALA A 1 12  ? 14.16793  -2.43380  5.33838  1.000 16.06472 ? 12  ALA A CA  1 
ATOM   101  C C   . ALA A 1 12  ? 13.53019  -1.08191  5.64469  1.000 11.24366 ? 12  ALA A C   1 
ATOM   102  O O   . ALA A 1 12  ? 12.50680  -1.04189  6.33277  1.000 12.98058 ? 12  ALA A O   1 
ATOM   103  C CB  . ALA A 1 12  ? 14.23873  -3.29156  6.60808  1.000 7.24582  ? 12  ALA A CB  1 
ATOM   104  N N   . VAL A 1 13  ? 14.07735  0.02798   5.14567  1.000 13.59240 ? 13  VAL A N   1 
ATOM   105  C CA  . VAL A 1 13  ? 13.57916  1.35948   5.49340  1.000 10.76406 ? 13  VAL A CA  1 
ATOM   106  C C   . VAL A 1 13  ? 13.37594  2.18798   4.24161  1.000 9.81837  ? 13  VAL A C   1 
ATOM   107  O O   . VAL A 1 13  ? 14.26809  2.28621   3.39096  1.000 19.83847 ? 13  VAL A O   1 
ATOM   108  C CB  . VAL A 1 13  ? 14.50154  2.10208   6.47644  1.000 17.84524 ? 13  VAL A CB  1 
ATOM   109  C CG1 . VAL A 1 13  ? 13.87681  3.40811   6.89316  1.000 15.93411 ? 13  VAL A CG1 1 
ATOM   110  C CG2 . VAL A 1 13  ? 14.67484  1.27561   7.73971  1.000 12.49487 ? 13  VAL A CG2 1 
ATOM   111  N N   . THR A 1 14  ? 12.17334  2.72740   4.10396  1.000 13.85208 ? 14  THR A N   1 
ATOM   112  C CA  . THR A 1 14  ? 11.84014  3.54428   2.95739  1.000 20.60762 ? 14  THR A CA  1 
ATOM   113  C C   . THR A 1 14  ? 12.29105  4.97699   3.19993  1.000 12.33910 ? 14  THR A C   1 
ATOM   114  O O   . THR A 1 14  ? 12.63988  5.34454   4.31872  1.000 16.98331 ? 14  THR A O   1 
ATOM   115  C CB  . THR A 1 14  ? 10.34262  3.45619   2.69921  1.000 18.73092 ? 14  THR A CB  1 
ATOM   116  O OG1 . THR A 1 14  ? 9.64851   4.23101   3.68621  1.000 21.15663 ? 14  THR A OG1 1 
ATOM   117  C CG2 . THR A 1 14  ? 9.87583   2.00300   2.68480  1.000 18.46008 ? 14  THR A CG2 1 
ATOM   118  N N   . PRO A 1 15  ? 12.33039  5.80614   2.14589  1.000 21.65411 ? 15  PRO A N   1 
ATOM   119  C CA  . PRO A 1 15  ? 12.76634  7.19430   2.33138  1.000 25.43054 ? 15  PRO A CA  1 
ATOM   120  C C   . PRO A 1 15  ? 12.07864  7.87948   3.50495  1.000 13.71945 ? 15  PRO A C   1 
ATOM   121  O O   . PRO A 1 15  ? 10.97311  7.50274   3.89550  1.000 14.62263 ? 15  PRO A O   1 
ATOM   122  C CB  . PRO A 1 15  ? 12.39875  7.82770   0.98739  1.000 20.70716 ? 15  PRO A CB  1 
ATOM   123  C CG  . PRO A 1 15  ? 12.73046  6.68308   0.02717  1.000 25.76895 ? 15  PRO A CG  1 
ATOM   124  C CD  . PRO A 1 15  ? 11.97153  5.56656   0.72526  1.000 22.45176 ? 15  PRO A CD  1 
ATOM   125  N N   . VAL A 1 16  ? 12.71397  8.90829   4.05159  1.000 20.88014 ? 16  VAL A N   1 
ATOM   126  C CA  . VAL A 1 16  ? 12.15087  9.60359   5.19521  1.000 15.07952 ? 16  VAL A CA  1 
ATOM   127  C C   . VAL A 1 16  ? 10.97751  10.42701  4.68906  1.000 9.80615  ? 16  VAL A C   1 
ATOM   128  O O   . VAL A 1 16  ? 11.01893  10.99655  3.58021  1.000 5.87170  ? 16  VAL A O   1 
ATOM   129  C CB  . VAL A 1 16  ? 13.22278  10.48099  5.87824  1.000 11.84268 ? 16  VAL A CB  1 
ATOM   130  C CG1 . VAL A 1 16  ? 12.62827  11.71457  6.56005  1.000 16.55223 ? 16  VAL A CG1 1 
ATOM   131  C CG2 . VAL A 1 16  ? 14.06124  9.69751   6.87669  1.000 15.63175 ? 16  VAL A CG2 1 
ATOM   132  N N   . LYS A 1 17  ? 9.93471   10.52569  5.49896  1.000 10.66705 ? 17  LYS A N   1 
ATOM   133  C CA  . LYS A 1 17  ? 8.78458   11.33371  5.13568  1.000 13.87884 ? 17  LYS A CA  1 
ATOM   134  C C   . LYS A 1 17  ? 8.66037   12.54072  6.04543  1.000 11.47108 ? 17  LYS A C   1 
ATOM   135  O O   . LYS A 1 17  ? 9.30743   12.65339  7.08698  1.000 14.89957 ? 17  LYS A O   1 
ATOM   136  C CB  . LYS A 1 17  ? 7.47430   10.53180  5.19955  1.000 15.75131 ? 17  LYS A CB  1 
ATOM   137  C CG  . LYS A 1 17  ? 7.43338   9.10073   4.69974  1.000 12.20565 ? 17  LYS A CG  1 
ATOM   138  C CD  . LYS A 1 17  ? 7.95712   9.04618   3.28017  1.000 19.07060 ? 17  LYS A CD  1 
ATOM   139  C CE  . LYS A 1 17  ? 7.54185   7.76711   2.55168  1.000 26.99267 ? 17  LYS A CE  1 
ATOM   140  N NZ  . LYS A 1 17  ? 8.27786   6.55066   3.00467  1.000 28.36331 ? 17  LYS A NZ  1 
ATOM   141  N N   . ASN A 1 18  ? 7.79431   13.44897  5.60577  1.000 14.24126 ? 18  ASN A N   1 
ATOM   142  C CA  . ASN A 1 18  ? 7.42481   14.65115  6.33218  1.000 19.84930 ? 18  ASN A CA  1 
ATOM   143  C C   . ASN A 1 18  ? 5.92986   14.59413  6.57193  1.000 18.61876 ? 18  ASN A C   1 
ATOM   144  O O   . ASN A 1 18  ? 5.15308   14.49984  5.61554  1.000 17.86648 ? 18  ASN A O   1 
ATOM   145  C CB  . ASN A 1 18  ? 7.78982   15.91275  5.53306  1.000 12.49165 ? 18  ASN A CB  1 
ATOM   146  C CG  . ASN A 1 18  ? 7.66007   17.19367  6.34466  1.000 16.47025 ? 18  ASN A CG  1 
ATOM   147  O OD1 . ASN A 1 18  ? 7.04459   17.22054  7.40700  1.000 19.08976 ? 18  ASN A OD1 1 
ATOM   148  N ND2 . ASN A 1 18  ? 8.24764   18.26684  5.84129  1.000 28.01007 ? 18  ASN A ND2 1 
ATOM   149  N N   . GLN A 1 19  ? 5.53604   14.58635  7.85052  1.000 15.76499 ? 19  GLN A N   1 
ATOM   150  C CA  . GLN A 1 19  ? 4.13431   14.41906  8.18414  1.000 20.14017 ? 19  GLN A CA  1 
ATOM   151  C C   . GLN A 1 19  ? 3.38172   15.72815  7.98429  1.000 16.84828 ? 19  GLN A C   1 
ATOM   152  O O   . GLN A 1 19  ? 2.15385   15.70940  7.86934  1.000 21.00717 ? 19  GLN A O   1 
ATOM   153  C CB  . GLN A 1 19  ? 3.90016   14.00081  9.63060  1.000 9.61120  ? 19  GLN A CB  1 
ATOM   154  C CG  . GLN A 1 19  ? 4.48246   14.94543  10.62859 1.000 11.55310 ? 19  GLN A CG  1 
ATOM   155  C CD  . GLN A 1 19  ? 4.46419   14.35780  12.00885 1.000 14.37554 ? 19  GLN A CD  1 
ATOM   156  O OE1 . GLN A 1 19  ? 5.25714   13.47211  12.33383 1.000 17.78763 ? 19  GLN A OE1 1 
ATOM   157  N NE2 . GLN A 1 19  ? 3.51676   14.81038  12.82217 1.000 23.45568 ? 19  GLN A NE2 1 
ATOM   158  N N   . GLY A 1 20  ? 4.10660   16.84695  7.85689  1.000 8.85417  ? 20  GLY A N   1 
ATOM   159  C CA  . GLY A 1 20  ? 3.52339   18.16626  7.68450  1.000 8.87754  ? 20  GLY A CA  1 
ATOM   160  C C   . GLY A 1 20  ? 2.90212   18.68588  8.97196  1.000 26.36276 ? 20  GLY A C   1 
ATOM   161  O O   . GLY A 1 20  ? 3.34220   18.35494  10.07609 1.000 24.53977 ? 20  GLY A O   1 
ATOM   162  N N   . SER A 1 21  ? 1.82646   19.44772  8.85895  1.000 24.51697 ? 21  SER A N   1 
ATOM   163  C CA  . SER A 1 21  ? 1.28048   20.05260  10.06377 1.000 31.09969 ? 21  SER A CA  1 
ATOM   164  C C   . SER A 1 21  ? 0.20381   19.21119  10.72735 1.000 27.23234 ? 21  SER A C   1 
ATOM   165  O O   . SER A 1 21  ? -0.41389  19.65485  11.70286 1.000 41.62886 ? 21  SER A O   1 
ATOM   166  C CB  . SER A 1 21  ? 0.71856   21.43213  9.70293  1.000 14.98792 ? 21  SER A CB  1 
ATOM   167  O OG  . SER A 1 21  ? 0.35336   22.16120  10.86583 1.000 56.88913 ? 21  SER A OG  1 
ATOM   168  N N   . CYS A 1 22  ? 0.06876   17.97211  10.30844 1.000 23.61368 ? 22  CYS A N   1 
ATOM   169  C CA  . CYS A 1 22  ? -0.97352  17.06531  10.75338 1.000 24.81276 ? 22  CYS A CA  1 
ATOM   170  C C   . CYS A 1 22  ? -0.37874  16.12127  11.79846 1.000 25.92772 ? 22  CYS A C   1 
ATOM   171  O O   . CYS A 1 22  ? 0.76012   15.66830  11.65000 1.000 17.62564 ? 22  CYS A O   1 
ATOM   172  C CB  . CYS A 1 22  ? -1.56260  16.30418  9.56381  1.000 29.88743 ? 22  CYS A CB  1 
ATOM   173  S SG  . CYS A 1 22  ? -2.53394  14.88572  9.98825  1.000 33.75009 ? 22  CYS A SG  1 
ATOM   174  N N   . GLY A 1 23  ? -1.08943  15.88680  12.90116 1.000 20.05152 ? 23  GLY A N   1 
ATOM   175  C CA  . GLY A 1 23  ? -0.42628  15.09676  13.92514 1.000 22.04547 ? 23  GLY A CA  1 
ATOM   176  C C   . GLY A 1 23  ? -0.69064  13.62139  13.66455 1.000 28.30892 ? 23  GLY A C   1 
ATOM   177  O O   . GLY A 1 23  ? -1.37764  12.88821  14.38924 1.000 23.27269 ? 23  GLY A O   1 
ATOM   178  N N   . SER A 1 24  ? -0.07360  13.18937  12.56783 1.000 18.85152 ? 24  SER A N   1 
ATOM   179  C CA  . SER A 1 24  ? -0.14849  11.83591  12.04268 1.000 16.38323 ? 24  SER A CA  1 
ATOM   180  C C   . SER A 1 24  ? 1.10225   11.01922  12.34669 1.000 13.83540 ? 24  SER A C   1 
ATOM   181  O O   . SER A 1 24  ? 1.28456   9.94591   11.76280 1.000 21.54610 ? 24  SER A O   1 
ATOM   182  C CB  . SER A 1 24  ? -0.39044  11.90411  10.53818 1.000 17.26727 ? 24  SER A CB  1 
ATOM   183  O OG  . SER A 1 24  ? 0.63507   12.64768  9.91021  1.000 22.86311 ? 24  SER A OG  1 
ATOM   184  N N   . CYS A 1 25  ? 1.96305   11.50611  13.24466 1.000 12.86404 ? 25  CYS A N   1 
ATOM   185  C CA  . CYS A 1 25  ? 3.18258   10.78155  13.57939 1.000 13.53620 ? 25  CYS A CA  1 
ATOM   186  C C   . CYS A 1 25  ? 2.88954   9.33224   13.94286 1.000 9.02115  ? 25  CYS A C   1 
ATOM   187  O O   . CYS A 1 25  ? 3.65345   8.43212   13.58043 1.000 20.25835 ? 25  CYS A O   1 
ATOM   188  C CB  . CYS A 1 25  ? 3.94599   11.50538  14.69960 1.000 17.64065 ? 25  CYS A CB  1 
ATOM   189  S SG  . CYS A 1 25  ? 3.03971   11.72801  16.24985 1.000 22.38874 ? 25  CYS A SG  1 
ATOM   190  N N   . TRP A 1 26  ? 1.83527   9.09324   14.71999 1.000 8.61880  ? 26  TRP A N   1 
ATOM   191  C CA  . TRP A 1 26  ? 1.48142   7.72622   15.10425 1.000 9.27679  ? 26  TRP A CA  1 
ATOM   192  C C   . TRP A 1 26  ? 1.37961   6.81661   13.88895 1.000 12.61111 ? 26  TRP A C   1 
ATOM   193  O O   . TRP A 1 26  ? 1.78123   5.65131   13.94228 1.000 15.15818 ? 26  TRP A O   1 
ATOM   194  C CB  . TRP A 1 26  ? 0.19737   7.73996   15.92704 1.000 15.12517 ? 26  TRP A CB  1 
ATOM   195  C CG  . TRP A 1 26  ? -0.94951  8.38703   15.21605 1.000 10.40335 ? 26  TRP A CG  1 
ATOM   196  C CD1 . TRP A 1 26  ? -1.21729  9.72924   15.15668 1.000 8.77663  ? 26  TRP A CD1 1 
ATOM   197  C CD2 . TRP A 1 26  ? -1.95013  7.74330   14.42477 1.000 15.04706 ? 26  TRP A CD2 1 
ATOM   198  N NE1 . TRP A 1 26  ? -2.34285  9.95728   14.39526 1.000 14.63912 ? 26  TRP A NE1 1 
ATOM   199  C CE2 . TRP A 1 26  ? -2.81220  8.75110   13.93824 1.000 17.97115 ? 26  TRP A CE2 1 
ATOM   200  C CE3 . TRP A 1 26  ? -2.21325  6.41640   14.09411 1.000 25.71843 ? 26  TRP A CE3 1 
ATOM   201  C CZ2 . TRP A 1 26  ? -3.90466  8.46866   13.13299 1.000 16.94113 ? 26  TRP A CZ2 1 
ATOM   202  C CZ3 . TRP A 1 26  ? -3.31817  6.14169   13.30217 1.000 19.13816 ? 26  TRP A CZ3 1 
ATOM   203  C CH2 . TRP A 1 26  ? -4.14716  7.16234   12.83883 1.000 10.00497 ? 26  TRP A CH2 1 
ATOM   204  N N   . ALA A 1 27  ? 0.87910   7.34270   12.77261 1.000 14.09200 ? 27  ALA A N   1 
ATOM   205  C CA  . ALA A 1 27  ? 0.61868   6.52842   11.59174 1.000 20.98072 ? 27  ALA A CA  1 
ATOM   206  C C   . ALA A 1 27  ? 1.91604   6.37429   10.82191 1.000 15.73672 ? 27  ALA A C   1 
ATOM   207  O O   . ALA A 1 27  ? 2.18135   5.32073   10.22784 1.000 15.50688 ? 27  ALA A O   1 
ATOM   208  C CB  . ALA A 1 27  ? -0.46126  7.15790   10.70023 1.000 19.05305 ? 27  ALA A CB  1 
ATOM   209  N N   . PHE A 1 28  ? 2.70892   7.44332   10.79811 1.000 11.33415 ? 28  PHE A N   1 
ATOM   210  C CA  . PHE A 1 28  ? 4.02477   7.38835   10.16819 1.000 16.80360 ? 28  PHE A CA  1 
ATOM   211  C C   . PHE A 1 28  ? 4.90035   6.38409   10.89856 1.000 9.60043  ? 28  PHE A C   1 
ATOM   212  O O   . PHE A 1 28  ? 5.61359   5.59014   10.27841 1.000 11.60473 ? 28  PHE A O   1 
ATOM   213  C CB  . PHE A 1 28  ? 4.61999   8.79763   10.16814 1.000 10.80343 ? 28  PHE A CB  1 
ATOM   214  C CG  . PHE A 1 28  ? 4.16879   9.59242   8.99115  1.000 16.99413 ? 28  PHE A CG  1 
ATOM   215  C CD1 . PHE A 1 28  ? 3.00443   10.34257  9.05433  1.000 16.90940 ? 28  PHE A CD1 1 
ATOM   216  C CD2 . PHE A 1 28  ? 4.87992   9.55396   7.80010  1.000 12.45922 ? 28  PHE A CD2 1 
ATOM   217  C CE1 . PHE A 1 28  ? 2.53747   11.05898  7.93852  1.000 16.85012 ? 28  PHE A CE1 1 
ATOM   218  C CE2 . PHE A 1 28  ? 4.43146   10.28141  6.67092  1.000 17.31118 ? 28  PHE A CE2 1 
ATOM   219  C CZ  . PHE A 1 28  ? 3.26067   11.03454  6.74738  1.000 17.87705 ? 28  PHE A CZ  1 
ATOM   220  N N   . SER A 1 29  ? 4.87854   6.44457   12.22978 1.000 12.58459 ? 29  SER A N   1 
ATOM   221  C CA  . SER A 1 29  ? 5.63917   5.51959   13.05322 1.000 11.87169 ? 29  SER A CA  1 
ATOM   222  C C   . SER A 1 29  ? 5.16777   4.10148   12.75980 1.000 16.83333 ? 29  SER A C   1 
ATOM   223  O O   . SER A 1 29  ? 5.97393   3.19996   12.50151 1.000 21.90942 ? 29  SER A O   1 
ATOM   224  C CB  . SER A 1 29  ? 5.45458   5.90504   14.52705 1.000 12.01490 ? 29  SER A CB  1 
ATOM   225  O OG  . SER A 1 29  ? 6.07163   4.99926   15.41544 1.000 16.07110 ? 29  SER A OG  1 
ATOM   226  N N   . ALA A 1 30  ? 3.84959   3.88736   12.81153 1.000 12.72582 ? 30  ALA A N   1 
ATOM   227  C CA  . ALA A 1 30  ? 3.29138   2.56312   12.56568 1.000 20.38693 ? 30  ALA A CA  1 
ATOM   228  C C   . ALA A 1 30  ? 3.69943   2.06130   11.18312 1.000 19.40356 ? 30  ALA A C   1 
ATOM   229  O O   . ALA A 1 30  ? 4.01514   0.87902   11.01091 1.000 13.83355 ? 30  ALA A O   1 
ATOM   230  C CB  . ALA A 1 30  ? 1.77250   2.60475   12.71992 1.000 8.14641  ? 30  ALA A CB  1 
ATOM   231  N N   . VAL A 1 31  ? 3.65841   2.94108   10.17795 1.000 11.30060 ? 31  VAL A N   1 
ATOM   232  C CA  . VAL A 1 31  ? 3.95774   2.52468   8.80925  1.000 14.33331 ? 31  VAL A CA  1 
ATOM   233  C C   . VAL A 1 31  ? 5.42763   2.11681   8.65635  1.000 13.27277 ? 31  VAL A C   1 
ATOM   234  O O   . VAL A 1 31  ? 5.74599   1.17993   7.91521  1.000 9.97006  ? 31  VAL A O   1 
ATOM   235  C CB  . VAL A 1 31  ? 3.57131   3.61034   7.78655  1.000 15.03733 ? 31  VAL A CB  1 
ATOM   236  C CG1 . VAL A 1 31  ? 4.34755   3.37634   6.48639  1.000 13.81477 ? 31  VAL A CG1 1 
ATOM   237  C CG2 . VAL A 1 31  ? 2.08777   3.54307   7.46677  1.000 12.02899 ? 31  VAL A CG2 1 
ATOM   238  N N   . VAL A 1 32  ? 6.35110   2.79237   9.34047  1.000 14.07330 ? 32  VAL A N   1 
ATOM   239  C CA  . VAL A 1 32  ? 7.74313   2.35487   9.23217  1.000 11.40267 ? 32  VAL A CA  1 
ATOM   240  C C   . VAL A 1 32  ? 7.88925   0.89558   9.65797  1.000 18.06717 ? 32  VAL A C   1 
ATOM   241  O O   . VAL A 1 32  ? 8.58732   0.10669   9.01164  1.000 10.59901 ? 32  VAL A O   1 
ATOM   242  C CB  . VAL A 1 32  ? 8.63897   3.24806   10.09943 1.000 22.60907 ? 32  VAL A CB  1 
ATOM   243  C CG1 . VAL A 1 32  ? 10.08006  2.73884   10.05834 1.000 14.86571 ? 32  VAL A CG1 1 
ATOM   244  C CG2 . VAL A 1 32  ? 8.51555   4.68728   9.66771  1.000 11.93256 ? 32  VAL A CG2 1 
ATOM   245  N N   . THR A 1 33  ? 7.24713   0.52296   10.75966 1.000 17.58321 ? 33  THR A N   1 
ATOM   246  C CA  . THR A 1 33  ? 7.34959   -0.83196  11.29171 1.000 17.09112 ? 33  THR A CA  1 
ATOM   247  C C   . THR A 1 33  ? 6.71047   -1.85512  10.36417 1.000 12.66648 ? 33  THR A C   1 
ATOM   248  O O   . THR A 1 33  ? 7.17271   -2.99657  10.28473 1.000 13.07245 ? 33  THR A O   1 
ATOM   249  C CB  . THR A 1 33  ? 6.71990   -0.91485  12.67924 1.000 15.61819 ? 33  THR A CB  1 
ATOM   250  O OG1 . THR A 1 33  ? 5.30013   -0.89757  12.54981 1.000 14.23619 ? 33  THR A OG1 1 
ATOM   251  C CG2 . THR A 1 33  ? 7.14566   0.27988   13.50534 1.000 14.99530 ? 33  THR A CG2 1 
ATOM   252  N N   . ILE A 1 34  ? 5.64381   -1.46415  9.66322  1.000 15.90200 ? 34  ILE A N   1 
ATOM   253  C CA  . ILE A 1 34  ? 5.01045   -2.36989  8.71346  1.000 14.91766 ? 34  ILE A CA  1 
ATOM   254  C C   . ILE A 1 34  ? 5.89833   -2.59158  7.49517  1.000 20.34072 ? 34  ILE A C   1 
ATOM   255  O O   . ILE A 1 34  ? 6.16957   -3.73582  7.11236  1.000 26.92391 ? 34  ILE A O   1 
ATOM   256  C CB  . ILE A 1 34  ? 3.65291   -1.79118  8.27444  1.000 18.34939 ? 34  ILE A CB  1 
ATOM   257  C CG1 . ILE A 1 34  ? 2.67775   -1.69689  9.43965  1.000 7.79131  ? 34  ILE A CG1 1 
ATOM   258  C CG2 . ILE A 1 34  ? 3.02567   -2.72984  7.22209  1.000 19.32745 ? 34  ILE A CG2 1 
ATOM   259  C CD1 . ILE A 1 34  ? 2.41029   -3.02770  10.11621 1.000 25.05514 ? 34  ILE A CD1 1 
ATOM   260  N N   . GLU A 1 35  ? 6.38028   -1.51605  6.88251  1.000 17.28544 ? 35  GLU A N   1 
ATOM   261  C CA  . GLU A 1 35  ? 7.33484   -1.62412  5.77578  1.000 14.90364 ? 35  GLU A CA  1 
ATOM   262  C C   . GLU A 1 35  ? 8.52867   -2.48644  6.15057  1.000 20.94863 ? 35  GLU A C   1 
ATOM   263  O O   . GLU A 1 35  ? 8.95002   -3.36631  5.38935  1.000 21.45046 ? 35  GLU A O   1 
ATOM   264  C CB  . GLU A 1 35  ? 7.80114   -0.21712  5.39400  1.000 20.43900 ? 35  GLU A CB  1 
ATOM   265  C CG  . GLU A 1 35  ? 6.65833   0.65042   4.84349  1.000 31.79169 ? 35  GLU A CG  1 
ATOM   266  C CD  . GLU A 1 35  ? 7.05161   2.10836   4.60739  1.000 43.36494 ? 35  GLU A CD  1 
ATOM   267  O OE1 . GLU A 1 35  ? 6.33418   2.80972   3.84173  1.000 37.39096 ? 35  GLU A OE1 1 
ATOM   268  O OE2 . GLU A 1 35  ? 8.06149   2.55124   5.18556  1.000 24.45830 ? 35  GLU A OE2 1 
ATOM   269  N N   . GLY A 1 36  ? 9.03250   -2.29204  7.36844  1.000 19.98517 ? 36  GLY A N   1 
ATOM   270  C CA  . GLY A 1 36  ? 10.13854  -3.09185  7.86491  1.000 14.33864 ? 36  GLY A CA  1 
ATOM   271  C C   . GLY A 1 36  ? 9.84012   -4.57395  7.92901  1.000 19.07911 ? 36  GLY A C   1 
ATOM   272  O O   . GLY A 1 36  ? 10.59297  -5.39501  7.39657  1.000 18.36419 ? 36  GLY A O   1 
ATOM   273  N N   . ILE A 1 37  ? 8.72418   -4.93811  8.56449  1.000 17.49455 ? 37  ILE A N   1 
ATOM   274  C CA  . ILE A 1 37  ? 8.43711   -6.35315  8.75892  1.000 23.05293 ? 37  ILE A CA  1 
ATOM   275  C C   . ILE A 1 37  ? 8.08789   -7.01505  7.42609  1.000 31.73600 ? 37  ILE A C   1 
ATOM   276  O O   . ILE A 1 37  ? 8.39029   -8.19903  7.22595  1.000 20.59459 ? 37  ILE A O   1 
ATOM   277  C CB  . ILE A 1 37  ? 7.33940   -6.54323  9.83584  1.000 20.19620 ? 37  ILE A CB  1 
ATOM   278  C CG1 . ILE A 1 37  ? 7.34541   -7.97661  10.35500 1.000 18.26954 ? 37  ILE A CG1 1 
ATOM   279  C CG2 . ILE A 1 37  ? 5.95169   -6.19272  9.29911  1.000 23.79719 ? 37  ILE A CG2 1 
ATOM   280  C CD1 . ILE A 1 37  ? 8.64368   -8.36234  10.95458 1.000 23.00655 ? 37  ILE A CD1 1 
ATOM   281  N N   . ILE A 1 38  ? 7.48956   -6.28208  6.48260  1.000 18.11985 ? 38  ILE A N   1 
ATOM   282  C CA  . ILE A 1 38  ? 7.21871   -6.89541  5.18487  1.000 23.08146 ? 38  ILE A CA  1 
ATOM   283  C C   . ILE A 1 38  ? 8.54094   -7.17391  4.46469  1.000 29.43835 ? 38  ILE A C   1 
ATOM   284  O O   . ILE A 1 38  ? 8.68791   -8.20968  3.80917  1.000 30.41927 ? 38  ILE A O   1 
ATOM   285  C CB  . ILE A 1 38  ? 6.27289   -6.02241  4.33967  1.000 23.52309 ? 38  ILE A CB  1 
ATOM   286  C CG1 . ILE A 1 38  ? 4.93200   -5.84273  5.05399  1.000 19.26170 ? 38  ILE A CG1 1 
ATOM   287  C CG2 . ILE A 1 38  ? 6.04960   -6.65511  2.98170  1.000 20.67652 ? 38  ILE A CG2 1 
ATOM   288  C CD1 . ILE A 1 38  ? 4.26586   -7.10185  5.42823  1.000 15.94665 ? 38  ILE A CD1 1 
ATOM   289  N N   . LYS A 1 39  ? 9.49968   -6.23577  4.51629  1.000 19.58970 ? 39  LYS A N   1 
ATOM   290  C CA  . LYS A 1 39  ? 10.80226  -6.47114  3.88184  1.000 20.51947 ? 39  LYS A CA  1 
ATOM   291  C C   . LYS A 1 39  ? 11.48202  -7.69272  4.50229  1.000 21.99099 ? 39  LYS A C   1 
ATOM   292  O O   . LYS A 1 39  ? 12.00472  -8.56450  3.79628  1.000 26.63540 ? 39  LYS A O   1 
ATOM   293  C CB  . LYS A 1 39  ? 11.69779  -5.24485  4.02349  1.000 24.39532 ? 39  LYS A CB  1 
ATOM   294  C CG  . LYS A 1 39  ? 13.17964  -5.50355  3.72871  1.000 18.40041 ? 39  LYS A CG  1 
ATOM   295  C CD  . LYS A 1 39  ? 13.39580  -5.87580  2.27025  1.000 33.75180 ? 39  LYS A CD  1 
ATOM   296  C CE  . LYS A 1 39  ? 14.83019  -6.36527  2.01628  1.000 25.64446 ? 39  LYS A CE  1 
ATOM   297  N NZ  . LYS A 1 39  ? 15.13888  -6.22598  0.57123  1.000 35.22314 ? 39  LYS A NZ  1 
ATOM   298  N N   . ILE A 1 40  ? 11.54819  -7.72355  5.83030  1.000 20.04626 ? 40  ILE A N   1 
ATOM   299  C CA  . ILE A 1 40  ? 12.21800  -8.80875  6.54354  1.000 21.92087 ? 40  ILE A CA  1 
ATOM   300  C C   . ILE A 1 40  ? 11.62078  -10.15955 6.15285  1.000 24.84052 ? 40  ILE A C   1 
ATOM   301  O O   . ILE A 1 40  ? 12.34147  -11.12063 5.85497  1.000 26.19556 ? 40  ILE A O   1 
ATOM   302  C CB  . ILE A 1 40  ? 12.14903  -8.56065  8.06320  1.000 27.36042 ? 40  ILE A CB  1 
ATOM   303  C CG1 . ILE A 1 40  ? 13.05543  -7.39057  8.43613  1.000 21.73999 ? 40  ILE A CG1 1 
ATOM   304  C CG2 . ILE A 1 40  ? 12.49616  -9.81477  8.87840  1.000 30.26952 ? 40  ILE A CG2 1 
ATOM   305  C CD1 . ILE A 1 40  ? 12.78110  -6.80653  9.80693  1.000 25.99313 ? 40  ILE A CD1 1 
ATOM   306  N N   . ARG A 1 41  ? 10.28813  -10.25522 6.16928  1.000 21.37214 ? 41  ARG A N   1 
ATOM   307  C CA  . ARG A 1 41  ? 9.61102   -11.51876 5.87842  1.000 29.76636 ? 41  ARG A CA  1 
ATOM   308  C C   . ARG A 1 41  ? 9.44882   -11.84068 4.38079  1.000 27.97016 ? 41  ARG A C   1 
ATOM   309  O O   . ARG A 1 41  ? 9.41306   -13.02383 4.02259  1.000 30.14732 ? 41  ARG A O   1 
ATOM   310  C CB  . ARG A 1 41  ? 8.27079   -11.51290 6.61442  1.000 26.71577 ? 41  ARG A CB  1 
ATOM   311  C CG  . ARG A 1 41  ? 8.57849   -11.45592 8.11593  1.000 30.65621 ? 41  ARG A CG  1 
ATOM   312  C CD  . ARG A 1 41  ? 8.64853   -12.75099 8.85077  1.000 34.38818 ? 41  ARG A CD  1 
ATOM   313  N NE  . ARG A 1 41  ? 8.78015   -12.42583 10.26072 1.000 34.85466 ? 41  ARG A NE  1 
ATOM   314  C CZ  . ARG A 1 41  ? 9.94588   -12.35351 10.88946 1.000 32.92781 ? 41  ARG A CZ  1 
ATOM   315  N NH1 . ARG A 1 41  ? 11.05531  -12.82649 10.34406 1.000 45.21933 ? 41  ARG A NH1 1 
ATOM   316  N NH2 . ARG A 1 41  ? 9.98573   -11.87710 12.13005 1.000 43.04559 ? 41  ARG A NH2 1 
ATOM   317  N N   . THR A 1 42  ? 9.37240   -10.84810 3.48542  1.000 22.88430 ? 42  THR A N   1 
ATOM   318  C CA  . THR A 1 42  ? 9.10126   -11.13367 2.07379  1.000 20.79156 ? 42  THR A CA  1 
ATOM   319  C C   . THR A 1 42  ? 10.30551  -10.91187 1.17700  1.000 18.91791 ? 42  THR A C   1 
ATOM   320  O O   . THR A 1 42  ? 10.34617  -11.46248 0.07409  1.000 37.38303 ? 42  THR A O   1 
ATOM   321  C CB  . THR A 1 42  ? 7.91652   -10.31186 1.53127  1.000 26.47798 ? 42  THR A CB  1 
ATOM   322  O OG1 . THR A 1 42  ? 8.27051   -8.92403  1.42201  1.000 29.95048 ? 42  THR A OG1 1 
ATOM   323  C CG2 . THR A 1 42  ? 6.69507   -10.47102 2.41749  1.000 28.93789 ? 42  THR A CG2 1 
ATOM   324  N N   . GLY A 1 43  ? 11.23108  -10.06760 1.59061  1.000 26.76310 ? 43  GLY A N   1 
ATOM   325  C CA  . GLY A 1 43  ? 12.33324  -9.58511  0.79247  1.000 19.97081 ? 43  GLY A CA  1 
ATOM   326  C C   . GLY A 1 43  ? 12.06176  -8.32313  0.01673  1.000 20.63108 ? 43  GLY A C   1 
ATOM   327  O O   . GLY A 1 43  ? 12.98152  -7.81180  -0.63311 1.000 25.26939 ? 43  GLY A O   1 
ATOM   328  N N   . ASN A 1 44  ? 10.80939  -7.87930  -0.03927 1.000 30.51044 ? 44  ASN A N   1 
ATOM   329  C CA  . ASN A 1 44  ? 10.39249  -6.75184  -0.86577 1.000 22.92947 ? 44  ASN A CA  1 
ATOM   330  C C   . ASN A 1 44  ? 10.25583  -5.51259  0.02093  1.000 26.62219 ? 44  ASN A C   1 
ATOM   331  O O   . ASN A 1 44  ? 9.61452   -5.58470  1.07021  1.000 17.42190 ? 44  ASN A O   1 
ATOM   332  C CB  . ASN A 1 44  ? 9.09539   -7.06572  -1.60124 1.000 29.57711 ? 44  ASN A CB  1 
ATOM   333  C CG  . ASN A 1 44  ? 9.30035   -8.08814  -2.67785 1.000 32.85050 ? 44  ASN A CG  1 
ATOM   334  O OD1 . ASN A 1 44  ? 10.31248  -8.06705  -3.38563 1.000 23.26087 ? 44  ASN A OD1 1 
ATOM   335  N ND2 . ASN A 1 44  ? 8.35575   -9.01345  -2.79821 1.000 41.65309 ? 44  ASN A ND2 1 
ATOM   336  N N   . LEU A 1 45  ? 10.80824  -4.38318  -0.39992 1.000 22.45000 ? 45  LEU A N   1 
ATOM   337  C CA  . LEU A 1 45  ? 10.63148  -3.11656  0.31024  1.000 16.30905 ? 45  LEU A CA  1 
ATOM   338  C C   . LEU A 1 45  ? 9.59518   -2.26560  -0.40288 1.000 17.10212 ? 45  LEU A C   1 
ATOM   339  O O   . LEU A 1 45  ? 9.81813   -1.84414  -1.54582 1.000 19.25267 ? 45  LEU A O   1 
ATOM   340  C CB  . LEU A 1 45  ? 11.93978  -2.34849  0.43504  1.000 11.77091 ? 45  LEU A CB  1 
ATOM   341  C CG  . LEU A 1 45  ? 11.84673  -1.07091  1.27455  1.000 21.54425 ? 45  LEU A CG  1 
ATOM   342  C CD1 . LEU A 1 45  ? 11.51891  -1.30583  2.76528  1.000 16.52639 ? 45  LEU A CD1 1 
ATOM   343  C CD2 . LEU A 1 45  ? 13.18439  -0.29739  1.11939  1.000 17.23645 ? 45  LEU A CD2 1 
ATOM   344  N N   . ASN A 1 46  ? 8.46313   -2.01608  0.25679  1.000 18.09902 ? 46  ASN A N   1 
ATOM   345  C CA  . ASN A 1 46  ? 7.38103   -1.24197  -0.33695 1.000 21.61279 ? 46  ASN A CA  1 
ATOM   346  C C   . ASN A 1 46  ? 7.05499   -0.07805  0.58148  1.000 19.95566 ? 46  ASN A C   1 
ATOM   347  O O   . ASN A 1 46  ? 7.32280   -0.12143  1.78185  1.000 16.42501 ? 46  ASN A O   1 
ATOM   348  C CB  . ASN A 1 46  ? 6.11975   -2.07267  -0.55370 1.000 26.08582 ? 46  ASN A CB  1 
ATOM   349  C CG  . ASN A 1 46  ? 6.39081   -3.34300  -1.31970 1.000 32.67241 ? 46  ASN A CG  1 
ATOM   350  O OD1 . ASN A 1 46  ? 6.69746   -3.30728  -2.51111 1.000 38.63558 ? 46  ASN A OD1 1 
ATOM   351  N ND2 . ASN A 1 46  ? 6.28458   -4.48587  -0.63044 1.000 28.69890 ? 46  ASN A ND2 1 
ATOM   352  N N   . GLU A 1 47  ? 6.46364   0.96451   0.02241  1.000 11.94596 ? 47  GLU A N   1 
ATOM   353  C CA  . GLU A 1 47  ? 5.93901   2.02547   0.85264  1.000 13.88719 ? 47  GLU A CA  1 
ATOM   354  C C   . GLU A 1 47  ? 4.47398   1.72420   1.12176  1.000 12.53261 ? 47  GLU A C   1 
ATOM   355  O O   . GLU A 1 47  ? 3.72678   1.37291   0.20486  1.000 21.01014 ? 47  GLU A O   1 
ATOM   356  C CB  . GLU A 1 47  ? 6.11216   3.39496   0.19479  1.000 22.59369 ? 47  GLU A CB  1 
ATOM   357  C CG  . GLU A 1 47  ? 7.50833   3.99493   0.35689  1.000 22.37371 ? 47  GLU A CG  1 
ATOM   358  C CD  . GLU A 1 47  ? 7.87792   4.98144   -0.74050 1.000 46.37337 ? 47  GLU A CD  1 
ATOM   359  O OE1 . GLU A 1 47  ? 8.20423   4.56040   -1.87925 1.000 57.58925 ? 47  GLU A OE1 1 
ATOM   360  O OE2 . GLU A 1 47  ? 7.85555   6.19241   -0.45319 1.000 36.04589 ? 47  GLU A OE2 1 
ATOM   361  N N   . TYR A 1 48  ? 4.06906   1.83930   2.37532  1.000 15.46658 ? 48  TYR A N   1 
ATOM   362  C CA  . TYR A 1 48  ? 2.68193   1.60969   2.73333  1.000 10.95485 ? 48  TYR A CA  1 
ATOM   363  C C   . TYR A 1 48  ? 2.05869   2.91711   3.18378  1.000 15.92299 ? 48  TYR A C   1 
ATOM   364  O O   . TYR A 1 48  ? 2.75060   3.89951   3.44796  1.000 14.32984 ? 48  TYR A O   1 
ATOM   365  C CB  . TYR A 1 48  ? 2.58626   0.51729   3.78856  1.000 10.75858 ? 48  TYR A CB  1 
ATOM   366  C CG  . TYR A 1 48  ? 2.99041   -0.81553  3.18565  1.000 18.07542 ? 48  TYR A CG  1 
ATOM   367  C CD1 . TYR A 1 48  ? 2.21809   -1.41754  2.20293  1.000 17.10848 ? 48  TYR A CD1 1 
ATOM   368  C CD2 . TYR A 1 48  ? 4.16510   -1.43429  3.55801  1.000 20.89870 ? 48  TYR A CD2 1 
ATOM   369  C CE1 . TYR A 1 48  ? 2.59527   -2.61984  1.63337  1.000 22.51929 ? 48  TYR A CE1 1 
ATOM   370  C CE2 . TYR A 1 48  ? 4.55285   -2.62499  2.99676  1.000 26.99406 ? 48  TYR A CE2 1 
ATOM   371  C CZ  . TYR A 1 48  ? 3.77158   -3.21419  2.03316  1.000 25.52090 ? 48  TYR A CZ  1 
ATOM   372  O OH  . TYR A 1 48  ? 4.17561   -4.40429  1.49194  1.000 15.50714 ? 48  TYR A OH  1 
ATOM   373  N N   . SER A 1 49  ? 0.73692   2.91057   3.29741  1.000 20.15501 ? 49  SER A N   1 
ATOM   374  C CA  . SER A 1 49  ? -0.02566  4.14752   3.39256  1.000 14.79838 ? 49  SER A CA  1 
ATOM   375  C C   . SER A 1 49  ? -0.19930  4.64628   4.82255  1.000 12.10580 ? 49  SER A C   1 
ATOM   376  O O   . SER A 1 49  ? -0.99207  4.08738   5.59500  1.000 9.20804  ? 49  SER A O   1 
ATOM   377  C CB  . SER A 1 49  ? -1.39263  3.90357   2.74429  1.000 13.45717 ? 49  SER A CB  1 
ATOM   378  O OG  . SER A 1 49  ? -2.19920  5.05645   2.82064  1.000 14.98725 ? 49  SER A OG  1 
ATOM   379  N N   . GLU A 1 50  ? 0.37418   5.82112   5.09992  1.000 21.93821 ? 50  GLU A N   1 
ATOM   380  C CA  . GLU A 1 50  ? 0.07907   6.50114   6.35578  1.000 13.60614 ? 50  GLU A CA  1 
ATOM   381  C C   . GLU A 1 50  ? -1.30878  7.05634   6.29115  1.000 15.40422 ? 50  GLU A C   1 
ATOM   382  O O   . GLU A 1 50  ? -2.00364  7.11259   7.31352  1.000 15.72096 ? 50  GLU A O   1 
ATOM   383  C CB  . GLU A 1 50  ? 1.09561   7.60059   6.65757  1.000 17.12392 ? 50  GLU A CB  1 
ATOM   384  C CG  . GLU A 1 50  ? 2.52817   7.07587   6.79139  1.000 15.83530 ? 50  GLU A CG  1 
ATOM   385  C CD  . GLU A 1 50  ? 3.27508   7.02592   5.47441  1.000 28.62616 ? 50  GLU A CD  1 
ATOM   386  O OE1 . GLU A 1 50  ? 2.64796   7.31732   4.42777  1.000 27.82929 ? 50  GLU A OE1 1 
ATOM   387  O OE2 . GLU A 1 50  ? 4.48821   6.69298   5.48194  1.000 24.83532 ? 50  GLU A OE2 1 
ATOM   388  N N   . GLN A 1 51  ? -1.72160  7.49180   5.09923  1.000 15.83760 ? 51  GLN A N   1 
ATOM   389  C CA  . GLN A 1 51  ? -3.00606  8.16361   5.00080  1.000 29.06082 ? 51  GLN A CA  1 
ATOM   390  C C   . GLN A 1 51  ? -4.09978  7.17873   5.37890  1.000 19.36672 ? 51  GLN A C   1 
ATOM   391  O O   . GLN A 1 51  ? -5.07058  7.53653   6.05773  1.000 18.12657 ? 51  GLN A O   1 
ATOM   392  C CB  . GLN A 1 51  ? -3.22700  8.69817   3.57554  1.000 14.47333 ? 51  GLN A CB  1 
ATOM   393  C CG  . GLN A 1 51  ? -4.54681  9.41551   3.39215  1.000 11.46426 ? 51  GLN A CG  1 
ATOM   394  C CD  . GLN A 1 51  ? -4.54805  10.78114  4.01346  1.000 26.27927 ? 51  GLN A CD  1 
ATOM   395  O OE1 . GLN A 1 51  ? -3.50739  11.44209  4.08352  1.000 20.37074 ? 51  GLN A OE1 1 
ATOM   396  N NE2 . GLN A 1 51  ? -5.69478  11.17878  4.56859  1.000 23.32439 ? 51  GLN A NE2 1 
ATOM   397  N N   . GLU A 1 52  ? -3.92542  5.92178   4.97456  1.000 11.36122 ? 52  GLU A N   1 
ATOM   398  C CA  . GLU A 1 52  ? -4.91525  4.89793   5.24829  1.000 13.07753 ? 52  GLU A CA  1 
ATOM   399  C C   . GLU A 1 52  ? -5.09654  4.66803   6.73579  1.000 16.45241 ? 52  GLU A C   1 
ATOM   400  O O   . GLU A 1 52  ? -6.22206  4.46239   7.19391  1.000 18.40080 ? 52  GLU A O   1 
ATOM   401  C CB  . GLU A 1 52  ? -4.48483  3.57463   4.63310  1.000 16.69278 ? 52  GLU A CB  1 
ATOM   402  C CG  . GLU A 1 52  ? -5.48791  2.47007   4.84690  1.000 21.88867 ? 52  GLU A CG  1 
ATOM   403  C CD  . GLU A 1 52  ? -5.22683  1.30905   3.93097  1.000 24.92064 ? 52  GLU A CD  1 
ATOM   404  O OE1 . GLU A 1 52  ? -4.62530  1.53237   2.86773  1.000 31.54053 ? 52  GLU A OE1 1 
ATOM   405  O OE2 . GLU A 1 52  ? -5.64456  0.18579   4.25571  1.000 42.83928 ? 52  GLU A OE2 1 
ATOM   406  N N   . LEU A 1 53  ? -4.00819  4.72102   7.51591  1.000 19.72610 ? 53  LEU A N   1 
ATOM   407  C CA  . LEU A 1 53  ? -4.17447  4.56948   8.95471  1.000 16.83673 ? 53  LEU A CA  1 
ATOM   408  C C   . LEU A 1 53  ? -4.80978  5.80871   9.54889  1.000 19.30682 ? 53  LEU A C   1 
ATOM   409  O O   . LEU A 1 53  ? -5.72347  5.71398   10.38222 1.000 20.62123 ? 53  LEU A O   1 
ATOM   410  C CB  . LEU A 1 53  ? -2.83095  4.30714   9.63674  1.000 16.12440 ? 53  LEU A CB  1 
ATOM   411  C CG  . LEU A 1 53  ? -2.07773  3.07537   9.10322  1.000 24.90263 ? 53  LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 53  ? -0.62128  3.08474   9.59298  1.000 16.61031 ? 53  LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 53  ? -2.77378  1.75445   9.32774  1.000 15.81538 ? 53  LEU A CD2 1 
ATOM   414  N N   . LEU A 1 54  ? -4.33947  6.97591   9.11671  1.000 15.31566 ? 54  LEU A N   1 
ATOM   415  C CA  . LEU A 1 54  ? -4.93407  8.24742   9.49800  1.000 13.18952 ? 54  LEU A CA  1 
ATOM   416  C C   . LEU A 1 54  ? -6.43971  8.26127   9.26002  1.000 19.46286 ? 54  LEU A C   1 
ATOM   417  O O   . LEU A 1 54  ? -7.21357  8.63507   10.14646 1.000 21.77554 ? 54  LEU A O   1 
ATOM   418  C CB  . LEU A 1 54  ? -4.23285  9.36030   8.71860  1.000 22.53049 ? 54  LEU A CB  1 
ATOM   419  C CG  . LEU A 1 54  ? -4.50426  10.77472  9.18024  1.000 25.75973 ? 54  LEU A CG  1 
ATOM   420  C CD1 . LEU A 1 54  ? -3.89221  10.93724  10.54542 1.000 32.61312 ? 54  LEU A CD1 1 
ATOM   421  C CD2 . LEU A 1 54  ? -3.84770  11.72285  8.20997  1.000 29.65173 ? 54  LEU A CD2 1 
ATOM   422  N N   . ASP A 1 55  ? -6.87982  7.80624   8.07445  1.000 21.82019 ? 55  ASP A N   1 
ATOM   423  C CA  . ASP A 1 55  ? -8.31071  7.84149   7.75210  1.000 27.61138 ? 55  ASP A CA  1 
ATOM   424  C C   . ASP A 1 55  ? -9.09431  6.76770   8.50287  1.000 15.46606 ? 55  ASP A C   1 
ATOM   425  O O   . ASP A 1 55  ? -10.21345 7.02686   8.96034  1.000 25.16761 ? 55  ASP A O   1 
ATOM   426  C CB  . ASP A 1 55  ? -8.57020  7.67075   6.24350  1.000 25.40937 ? 55  ASP A CB  1 
ATOM   427  C CG  . ASP A 1 55  ? -8.16564  8.88231   5.39601  1.000 18.34291 ? 55  ASP A CG  1 
ATOM   428  O OD1 . ASP A 1 55  ? -7.85852  9.96383   5.93624  1.000 25.64930 ? 55  ASP A OD1 1 
ATOM   429  O OD2 . ASP A 1 55  ? -8.24771  8.76435   4.15376  1.000 17.60325 ? 55  ASP A OD2 1 
ATOM   430  N N   . CYS A 1 56  ? -8.54271  5.55622   8.60975  1.000 22.55553 ? 56  CYS A N   1 
ATOM   431  C CA  . CYS A 1 56  ? -9.28260  4.33999   8.96689  1.000 31.68065 ? 56  CYS A CA  1 
ATOM   432  C C   . CYS A 1 56  ? -9.08450  3.84466   10.38867 1.000 18.59398 ? 56  CYS A C   1 
ATOM   433  O O   . CYS A 1 56  ? -9.86524  2.99663   10.82797 1.000 13.76597 ? 56  CYS A O   1 
ATOM   434  C CB  . CYS A 1 56  ? -9.01466  3.19005   7.98635  1.000 19.39730 ? 56  CYS A CB  1 
ATOM   435  S SG  . CYS A 1 56  ? -9.18026  3.65720   6.25699  1.000 31.77849 ? 56  CYS A SG  1 
ATOM   436  N N   . ASP A 1 57  ? -8.11425  4.36061   11.13622 1.000 25.12370 ? 57  ASP A N   1 
ATOM   437  C CA  . ASP A 1 57  ? -7.90645  3.88469   12.49822 1.000 19.51195 ? 57  ASP A CA  1 
ATOM   438  C C   . ASP A 1 57  ? -8.86686  4.69924   13.34852 1.000 29.72992 ? 57  ASP A C   1 
ATOM   439  O O   . ASP A 1 57  ? -8.60569  5.86729   13.66682 1.000 27.82850 ? 57  ASP A O   1 
ATOM   440  C CB  . ASP A 1 57  ? -6.47853  4.07402   12.97513 1.000 16.32583 ? 57  ASP A CB  1 
ATOM   441  C CG  . ASP A 1 57  ? -6.28351  3.56733   14.39713 1.000 26.01046 ? 57  ASP A CG  1 
ATOM   442  O OD1 . ASP A 1 57  ? -7.24224  2.98871   14.94594 1.000 31.18500 ? 57  ASP A OD1 1 
ATOM   443  O OD2 . ASP A 1 57  ? -5.20063  3.78639   14.98523 1.000 28.76324 ? 57  ASP A OD2 1 
ATOM   444  N N   . ARG A 1 58  ? -9.94202  4.04344   13.78411 1.000 15.58090 ? 58  ARG A N   1 
ATOM   445  C CA  . ARG A 1 58  ? -10.98214 4.72400   14.51592 1.000 23.09295 ? 58  ARG A CA  1 
ATOM   446  C C   . ARG A 1 58  ? -10.76675 4.69388   16.00899 1.000 20.27952 ? 58  ARG A C   1 
ATOM   447  O O   . ARG A 1 58  ? -11.60860 5.21133   16.75227 1.000 35.64326 ? 58  ARG A O   1 
ATOM   448  C CB  . ARG A 1 58  ? -12.28519 3.95073   14.25903 1.000 17.24768 ? 58  ARG A CB  1 
ATOM   449  C CG  . ARG A 1 58  ? -12.80956 3.95358   12.83303 1.000 27.09935 ? 58  ARG A CG  1 
ATOM   450  C CD  . ARG A 1 58  ? -13.93953 2.92356   12.66797 1.000 24.92346 ? 58  ARG A CD  1 
ATOM   451  N NE  . ARG A 1 58  ? -13.46442 1.54077   12.68794 1.000 21.57907 ? 58  ARG A NE  1 
ATOM   452  C CZ  . ARG A 1 58  ? -14.21508 0.48750   12.38063 1.000 42.37658 ? 58  ARG A CZ  1 
ATOM   453  N NH1 . ARG A 1 58  ? -15.49274 0.62029   12.05978 1.000 30.37154 ? 58  ARG A NH1 1 
ATOM   454  N NH2 . ARG A 1 58  ? -13.67572 -0.73183  12.41407 1.000 20.85131 ? 58  ARG A NH2 1 
ATOM   455  N N   . ARG A 1 59  ? -9.63510  4.17400   16.46933 1.000 16.88737 ? 59  ARG A N   1 
ATOM   456  C CA  . ARG A 1 59  ? -9.24609  4.39298   17.85923 1.000 23.48425 ? 59  ARG A CA  1 
ATOM   457  C C   . ARG A 1 59  ? -8.52414  5.71509   17.97567 1.000 22.00356 ? 59  ARG A C   1 
ATOM   458  O O   . ARG A 1 59  ? -8.52466  6.33485   19.04337 1.000 30.99823 ? 59  ARG A O   1 
ATOM   459  C CB  . ARG A 1 59  ? -8.44117  3.22120   18.40633 1.000 23.87484 ? 59  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 59  ? -9.18555  1.90579   18.23926 1.000 28.25056 ? 59  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 59  ? -8.52339  0.74841   18.94092 1.000 38.06553 ? 59  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 59  ? -9.36284  0.27160   20.03041 1.000 39.73597 ? 59  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 59  ? -10.08691 -0.83883  19.98877 1.000 53.72190 ? 59  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 59  ? -10.23246 -1.53102  18.86433 1.000 43.86724 ? 59  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 59  ? -10.74196 -1.22405  21.08336 1.000 48.47878 ? 59  ARG A NH2 1 
ATOM   466  N N   . SER A 1 60  ? -7.90013  6.14223   16.87444 1.000 24.73467 ? 60  SER A N   1 
ATOM   467  C CA  . SER A 1 60  ? -7.09298  7.34772   16.81736 1.000 24.02902 ? 60  SER A CA  1 
ATOM   468  C C   . SER A 1 60  ? -7.94844  8.53476   16.40737 1.000 19.32377 ? 60  SER A C   1 
ATOM   469  O O   . SER A 1 60  ? -9.13519  8.40987   16.10266 1.000 27.84031 ? 60  SER A O   1 
ATOM   470  C CB  . SER A 1 60  ? -5.96746  7.18865   15.79530 1.000 15.60236 ? 60  SER A CB  1 
ATOM   471  O OG  . SER A 1 60  ? -4.97614  6.28418   16.23360 1.000 24.90259 ? 60  SER A OG  1 
ATOM   472  N N   . TYR A 1 61  ? -7.31349  9.69761   16.32759 1.000 24.92331 ? 61  TYR A N   1 
ATOM   473  C CA  . TYR A 1 61  ? -8.01166  10.96161  16.12142 1.000 20.89010 ? 61  TYR A CA  1 
ATOM   474  C C   . TYR A 1 61  ? -7.52633  11.70550  14.88302 1.000 21.29302 ? 61  TYR A C   1 
ATOM   475  O O   . TYR A 1 61  ? -7.48593  12.93454  14.85627 1.000 23.18008 ? 61  TYR A O   1 
ATOM   476  C CB  . TYR A 1 61  ? -7.97412  11.82791  17.38832 1.000 25.64080 ? 61  TYR A CB  1 
ATOM   477  C CG  . TYR A 1 61  ? -8.41584  11.06584  18.62875 1.000 33.89507 ? 61  TYR A CG  1 
ATOM   478  C CD1 . TYR A 1 61  ? -9.75844  10.73440  18.77689 1.000 36.74839 ? 61  TYR A CD1 1 
ATOM   479  C CD2 . TYR A 1 61  ? -7.52340  10.62177  19.59903 1.000 40.28150 ? 61  TYR A CD2 1 
ATOM   480  C CE1 . TYR A 1 61  ? -10.22266 10.04304  19.86420 1.000 44.25695 ? 61  TYR A CE1 1 
ATOM   481  C CE2 . TYR A 1 61  ? -7.99358  9.90878   20.70947 1.000 49.96786 ? 61  TYR A CE2 1 
ATOM   482  C CZ  . TYR A 1 61  ? -9.34705  9.62633   20.82547 1.000 48.91105 ? 61  TYR A CZ  1 
ATOM   483  O OH  . TYR A 1 61  ? -9.84421  8.92970   21.90704 1.000 63.06350 ? 61  TYR A OH  1 
ATOM   484  N N   . GLY A 1 62  ? -7.15898  10.95530  13.85094 1.000 17.16992 ? 62  GLY A N   1 
ATOM   485  C CA  . GLY A 1 62  ? -6.64155  11.57099  12.66449 1.000 20.93537 ? 62  GLY A CA  1 
ATOM   486  C C   . GLY A 1 62  ? -5.51643  12.54258  12.90915 1.000 15.99003 ? 62  GLY A C   1 
ATOM   487  O O   . GLY A 1 62  ? -4.47490  12.20145  13.47249 1.000 24.66788 ? 62  GLY A O   1 
ATOM   488  N N   . CYS A 1 63  ? -5.72494  13.76852  12.44430 1.000 15.04541 ? 63  CYS A N   1 
ATOM   489  C CA  . CYS A 1 63  ? -4.72409  14.80712  12.58841 1.000 22.11319 ? 63  CYS A CA  1 
ATOM   490  C C   . CYS A 1 63  ? -4.60752  15.32929  14.00828 1.000 18.17008 ? 63  CYS A C   1 
ATOM   491  O O   . CYS A 1 63  ? -3.77289  16.20612  14.25771 1.000 45.51050 ? 63  CYS A O   1 
ATOM   492  C CB  . CYS A 1 63  ? -5.02932  15.93328  11.60053 1.000 27.26821 ? 63  CYS A CB  1 
ATOM   493  S SG  . CYS A 1 63  ? -4.48502  15.52378  9.90589  1.000 42.72104 ? 63  CYS A SG  1 
ATOM   494  N N   . ASN A 1 64  ? -5.33542  14.77026  14.96218 1.000 15.92771 ? 64  ASN A N   1 
ATOM   495  C CA  . ASN A 1 64  ? -5.27443  15.25003  16.33268 1.000 25.68192 ? 64  ASN A CA  1 
ATOM   496  C C   . ASN A 1 64  ? -4.56509  14.23246  17.20513 1.000 24.48531 ? 64  ASN A C   1 
ATOM   497  O O   . ASN A 1 64  ? -4.71212  14.24987  18.42838 1.000 38.80700 ? 64  ASN A O   1 
ATOM   498  C CB  . ASN A 1 64  ? -6.66969  15.54787  16.89541 1.000 26.59738 ? 64  ASN A CB  1 
ATOM   499  C CG  . ASN A 1 64  ? -7.33555  16.74630  16.22866 1.000 31.15018 ? 64  ASN A CG  1 
ATOM   500  O OD1 . ASN A 1 64  ? -8.31913  16.59123  15.51108 1.000 55.39447 ? 64  ASN A OD1 1 
ATOM   501  N ND2 . ASN A 1 64  ? -6.79803  17.94084  16.45741 1.000 29.47388 ? 64  ASN A ND2 1 
ATOM   502  N N   . GLY A 1 65  ? -3.75304  13.37933  16.59044 1.000 26.50091 ? 65  GLY A N   1 
ATOM   503  C CA  . GLY A 1 65  ? -3.00718  12.38960  17.33108 1.000 25.45986 ? 65  GLY A CA  1 
ATOM   504  C C   . GLY A 1 65  ? -3.67601  11.03663  17.29389 1.000 21.06454 ? 65  GLY A C   1 
ATOM   505  O O   . GLY A 1 65  ? -4.75575  10.84490  16.72692 1.000 26.01646 ? 65  GLY A O   1 
ATOM   506  N N   . GLY A 1 66  ? -2.98009  10.06762  17.87557 1.000 21.77109 ? 66  GLY A N   1 
ATOM   507  C CA  . GLY A 1 66  ? -3.41146  8.69043   17.79254 1.000 17.14298 ? 66  GLY A CA  1 
ATOM   508  C C   . GLY A 1 66  ? -2.35039  7.75602   18.33042 1.000 19.42302 ? 66  GLY A C   1 
ATOM   509  O O   . GLY A 1 66  ? -1.34656  8.18276   18.90547 1.000 25.21735 ? 66  GLY A O   1 
ATOM   510  N N   . TYR A 1 67  ? -2.60154  6.47013   18.14195 1.000 18.80271 ? 67  TYR A N   1 
ATOM   511  C CA  . TYR A 1 67  ? -1.81792  5.46532   18.82818 1.000 17.83623 ? 67  TYR A CA  1 
ATOM   512  C C   . TYR A 1 67  ? -1.14507  4.48910   17.88573 1.000 25.32021 ? 67  TYR A C   1 
ATOM   513  O O   . TYR A 1 67  ? -1.83240  3.84035   17.08044 1.000 21.29903 ? 67  TYR A O   1 
ATOM   514  C CB  . TYR A 1 67  ? -2.70029  4.69446   19.79173 1.000 19.47608 ? 67  TYR A CB  1 
ATOM   515  C CG  . TYR A 1 67  ? -3.58262  5.54635   20.67015 1.000 20.66296 ? 67  TYR A CG  1 
ATOM   516  C CD1 . TYR A 1 67  ? -3.08151  6.13035   21.83864 1.000 28.57670 ? 67  TYR A CD1 1 
ATOM   517  C CD2 . TYR A 1 67  ? -4.92039  5.74066   20.35649 1.000 31.02181 ? 67  TYR A CD2 1 
ATOM   518  C CE1 . TYR A 1 67  ? -3.90920  6.89950   22.66717 1.000 35.67516 ? 67  TYR A CE1 1 
ATOM   519  C CE2 . TYR A 1 67  ? -5.74508  6.49853   21.16579 1.000 45.53558 ? 67  TYR A CE2 1 
ATOM   520  C CZ  . TYR A 1 67  ? -5.24370  7.07321   22.31937 1.000 38.91820 ? 67  TYR A CZ  1 
ATOM   521  O OH  . TYR A 1 67  ? -6.09417  7.82572   23.10163 1.000 46.42417 ? 67  TYR A OH  1 
ATOM   522  N N   . PRO A 1 68  ? 0.17592   4.34178   17.95388 1.000 16.68219 ? 68  PRO A N   1 
ATOM   523  C CA  . PRO A 1 68  ? 0.83509   3.40112   17.05312 1.000 15.61942 ? 68  PRO A CA  1 
ATOM   524  C C   . PRO A 1 68  ? 0.34106   1.99085   17.28247 1.000 25.54232 ? 68  PRO A C   1 
ATOM   525  O O   . PRO A 1 68  ? 0.35037   1.18310   16.34472 1.000 24.88972 ? 68  PRO A O   1 
ATOM   526  C CB  . PRO A 1 68  ? 2.31183   3.55206   17.42007 1.000 16.83512 ? 68  PRO A CB  1 
ATOM   527  C CG  . PRO A 1 68  ? 2.39878   4.94663   17.91080 1.000 15.73084 ? 68  PRO A CG  1 
ATOM   528  C CD  . PRO A 1 68  ? 1.14407   5.16104   18.69697 1.000 18.63847 ? 68  PRO A CD  1 
ATOM   529  N N   A TRP A 1 69  ? -0.12677  1.66416   18.49229 0.494 22.84162 ? 69  TRP A N   1 
ATOM   530  N N   B TRP A 1 69  ? -0.06919  1.66660   18.51531 0.506 22.81830 ? 69  TRP A N   1 
ATOM   531  C CA  A TRP A 1 69  ? -0.58861  0.30182   18.72519 0.494 21.69142 ? 69  TRP A CA  1 
ATOM   532  C CA  B TRP A 1 69  ? -0.62484  0.34717   18.78482 0.506 21.71308 ? 69  TRP A CA  1 
ATOM   533  C C   A TRP A 1 69  ? -1.91268  0.03935   18.01836 0.494 21.22303 ? 69  TRP A C   1 
ATOM   534  C C   B TRP A 1 69  ? -1.85553  0.10409   17.93287 0.506 21.14071 ? 69  TRP A C   1 
ATOM   535  O O   A TRP A 1 69  ? -2.11500  -1.04999  17.46713 0.494 24.80809 ? 69  TRP A O   1 
ATOM   536  O O   B TRP A 1 69  ? -1.94486  -0.90241  17.21855 0.506 24.76282 ? 69  TRP A O   1 
ATOM   537  C CB  A TRP A 1 69  ? -0.69573  -0.00169  20.22615 0.494 22.09584 ? 69  TRP A CB  1 
ATOM   538  C CB  B TRP A 1 69  ? -0.98773  0.18873   20.26559 0.506 22.01106 ? 69  TRP A CB  1 
ATOM   539  C CG  A TRP A 1 69  ? -1.40017  1.02153   21.06004 0.494 23.92719 ? 69  TRP A CG  1 
ATOM   540  C CG  B TRP A 1 69  ? -1.83213  -1.04317  20.49551 0.506 16.44915 ? 69  TRP A CG  1 
ATOM   541  C CD1 A TRP A 1 69  ? -0.82624  2.04416   21.76252 0.494 22.74938 ? 69  TRP A CD1 1 
ATOM   542  C CD1 B TRP A 1 69  ? -1.38625  -2.33016  20.56969 0.506 22.47584 ? 69  TRP A CD1 1 
ATOM   543  C CD2 A TRP A 1 69  ? -2.81149  1.10645   21.30775 0.494 20.08623 ? 69  TRP A CD2 1 
ATOM   544  C CD2 B TRP A 1 69  ? -3.25929  -1.10861  20.65041 0.506 21.75510 ? 69  TRP A CD2 1 
ATOM   545  N NE1 A TRP A 1 69  ? -1.79694  2.76473   22.42476 0.494 23.21637 ? 69  TRP A NE1 1 
ATOM   546  N NE1 B TRP A 1 69  ? -2.43893  -3.19252  20.76446 0.506 22.73209 ? 69  TRP A NE1 1 
ATOM   547  C CE2 A TRP A 1 69  ? -3.02269  2.21190   22.15642 0.494 22.27345 ? 69  TRP A CE2 1 
ATOM   548  C CE2 B TRP A 1 69  ? -3.60023  -2.46942  20.81991 0.506 29.24954 ? 69  TRP A CE2 1 
ATOM   549  C CE3 A TRP A 1 69  ? -3.91553  0.36551   20.88316 0.494 23.68646 ? 69  TRP A CE3 1 
ATOM   550  C CE3 B TRP A 1 69  ? -4.28048  -0.15447  20.66522 0.506 25.87654 ? 69  TRP A CE3 1 
ATOM   551  C CZ2 A TRP A 1 69  ? -4.29511  2.59447   22.58204 0.494 21.51465 ? 69  TRP A CZ2 1 
ATOM   552  C CZ2 B TRP A 1 69  ? -4.92053  -2.89816  21.00013 0.506 23.67115 ? 69  TRP A CZ2 1 
ATOM   553  C CZ3 A TRP A 1 69  ? -5.17954  0.74872   21.30974 0.494 22.65255 ? 69  TRP A CZ3 1 
ATOM   554  C CZ3 B TRP A 1 69  ? -5.59675  -0.58537  20.84363 0.506 20.09211 ? 69  TRP A CZ3 1 
ATOM   555  C CH2 A TRP A 1 69  ? -5.35739  1.85204   22.14462 0.494 19.54708 ? 69  TRP A CH2 1 
ATOM   556  C CH2 B TRP A 1 69  ? -5.89975  -1.94322  21.00896 0.506 22.76087 ? 69  TRP A CH2 1 
ATOM   557  N N   . SER A 1 70  ? -2.82333  1.01721   18.00491 1.000 15.12699 ? 70  SER A N   1 
ATOM   558  C CA  . SER A 1 70  ? -4.08872  0.81346   17.29497 1.000 23.71529 ? 70  SER A CA  1 
ATOM   559  C C   . SER A 1 70  ? -3.87222  0.74766   15.78386 1.000 18.22485 ? 70  SER A C   1 
ATOM   560  O O   . SER A 1 70  ? -4.52740  -0.04269  15.09601 1.000 35.71454 ? 70  SER A O   1 
ATOM   561  C CB  . SER A 1 70  ? -5.09428  1.89861   17.66576 1.000 26.36408 ? 70  SER A CB  1 
ATOM   562  O OG  . SER A 1 70  ? -4.67882  3.15795   17.17465 1.000 30.50228 ? 70  SER A OG  1 
ATOM   563  N N   . ALA A 1 71  ? -2.99486  1.60187   15.24121 1.000 18.12832 ? 71  ALA A N   1 
ATOM   564  C CA  . ALA A 1 71  ? -2.69210  1.54525   13.80883 1.000 22.35800 ? 71  ALA A CA  1 
ATOM   565  C C   . ALA A 1 71  ? -2.07219  0.20778   13.42619 1.000 16.21820 ? 71  ALA A C   1 
ATOM   566  O O   . ALA A 1 71  ? -2.33635  -0.32663  12.34601 1.000 18.06548 ? 71  ALA A O   1 
ATOM   567  C CB  . ALA A 1 71  ? -1.75385  2.68625   13.42539 1.000 13.07883 ? 71  ALA A CB  1 
ATOM   568  N N   . LEU A 1 72  ? -1.22194  -0.33637  14.29094 1.000 11.27382 ? 72  LEU A N   1 
ATOM   569  C CA  . LEU A 1 72  ? -0.59139  -1.60960  13.97916 1.000 22.95799 ? 72  LEU A CA  1 
ATOM   570  C C   . LEU A 1 72  ? -1.64817  -2.69123  14.03824 1.000 21.33348 ? 72  LEU A C   1 
ATOM   571  O O   . LEU A 1 72  ? -1.63798  -3.64958  13.25818 1.000 19.35354 ? 72  LEU A O   1 
ATOM   572  C CB  . LEU A 1 72  ? 0.55226   -1.87758  14.95638 1.000 24.26504 ? 72  LEU A CB  1 
ATOM   573  C CG  . LEU A 1 72  ? 1.80537   -1.05898  14.59693 1.000 23.06072 ? 72  LEU A CG  1 
ATOM   574  C CD1 . LEU A 1 72  ? 2.94144   -1.35730  15.52413 1.000 21.57672 ? 72  LEU A CD1 1 
ATOM   575  C CD2 . LEU A 1 72  ? 2.22585   -1.30820  13.15257 1.000 16.42548 ? 72  LEU A CD2 1 
ATOM   576  N N   . GLN A 1 73  ? -2.56633  -2.53035  14.98413 1.000 20.81134 ? 73  GLN A N   1 
ATOM   577  C CA  . GLN A 1 73  ? -3.63995  -3.47844  15.18794 1.000 27.31001 ? 73  GLN A CA  1 
ATOM   578  C C   . GLN A 1 73  ? -4.54670  -3.50063  13.95325 1.000 23.88263 ? 73  GLN A C   1 
ATOM   579  O O   . GLN A 1 73  ? -5.01077  -4.56302  13.52240 1.000 19.07741 ? 73  GLN A O   1 
ATOM   580  C CB  . GLN A 1 73  ? -4.39869  -3.06551  16.44648 1.000 29.92947 ? 73  GLN A CB  1 
ATOM   581  C CG  . GLN A 1 73  ? -5.62888  -3.82863  16.71221 1.000 36.99638 ? 73  GLN A CG  1 
ATOM   582  C CD  . GLN A 1 73  ? -5.18370  -5.19718  17.17563 1.000 63.05197 ? 73  GLN A CD  1 
ATOM   583  O OE1 . GLN A 1 73  ? -4.92393  -6.11970  16.39610 1.000 45.56150 ? 73  GLN A OE1 1 
ATOM   584  N NE2 . GLN A 1 73  ? -4.92867  -5.26807  18.48030 1.000 63.33375 ? 73  GLN A NE2 1 
ATOM   585  N N   . LEU A 1 74  ? -4.77051  -2.32806  13.34636 1.000 20.97049 ? 74  LEU A N   1 
ATOM   586  C CA  . LEU A 1 74  ? -5.58764  -2.22979  12.13443 1.000 12.52490 ? 74  LEU A CA  1 
ATOM   587  C C   . LEU A 1 74  ? -4.97363  -2.99412  10.97661 1.000 19.44801 ? 74  LEU A C   1 
ATOM   588  O O   . LEU A 1 74  ? -5.69233  -3.61347  10.18254 1.000 27.98748 ? 74  LEU A O   1 
ATOM   589  C CB  . LEU A 1 74  ? -5.75409  -0.76079  11.74757 1.000 31.21684 ? 74  LEU A CB  1 
ATOM   590  C CG  . LEU A 1 74  ? -6.82127  -0.35698  10.73883 1.000 27.06576 ? 74  LEU A CG  1 
ATOM   591  C CD1 . LEU A 1 74  ? -8.22065  -0.58902  11.30987 1.000 32.75694 ? 74  LEU A CD1 1 
ATOM   592  C CD2 . LEU A 1 74  ? -6.63232  1.11403   10.40534 1.000 26.65268 ? 74  LEU A CD2 1 
ATOM   593  N N   . VAL A 1 75  ? -3.65721  -2.89784  10.81075 1.000 15.65467 ? 75  VAL A N   1 
ATOM   594  C CA  . VAL A 1 75  ? -3.01703  -3.58721  9.69893  1.000 14.53589 ? 75  VAL A CA  1 
ATOM   595  C C   . VAL A 1 75  ? -3.00984  -5.09667  9.92139  1.000 15.81063 ? 75  VAL A C   1 
ATOM   596  O O   . VAL A 1 75  ? -3.06692  -5.87758  8.96122  1.000 21.71610 ? 75  VAL A O   1 
ATOM   597  C CB  . VAL A 1 75  ? -1.58295  -3.03524  9.51373  1.000 20.52524 ? 75  VAL A CB  1 
ATOM   598  C CG1 . VAL A 1 75  ? -0.80364  -3.82695  8.47109  1.000 15.63586 ? 75  VAL A CG1 1 
ATOM   599  C CG2 . VAL A 1 75  ? -1.62088  -1.54922  9.13954  1.000 17.01724 ? 75  VAL A CG2 1 
ATOM   600  N N   . ALA A 1 76  ? -2.97530  -5.53724  11.18054 1.000 21.95806 ? 76  ALA A N   1 
ATOM   601  C CA  . ALA A 1 76  ? -3.14536  -6.95669  11.47633 1.000 27.81669 ? 76  ALA A CA  1 
ATOM   602  C C   . ALA A 1 76  ? -4.58302  -7.41664  11.30167 1.000 21.50010 ? 76  ALA A C   1 
ATOM   603  O O   . ALA A 1 76  ? -4.82631  -8.57947  10.96384 1.000 26.66209 ? 76  ALA A O   1 
ATOM   604  C CB  . ALA A 1 76  ? -2.66205  -7.26240  12.89447 1.000 15.64349 ? 76  ALA A CB  1 
ATOM   605  N N   . GLN A 1 77  ? -5.53647  -6.51545  11.46829 1.000 28.32150 ? 77  GLN A N   1 
ATOM   606  C CA  . GLN A 1 77  ? -6.94003  -6.87546  11.33608 1.000 32.02127 ? 77  GLN A CA  1 
ATOM   607  C C   . GLN A 1 77  ? -7.37544  -6.82909  9.87473  1.000 26.24351 ? 77  GLN A C   1 
ATOM   608  O O   . GLN A 1 77  ? -7.98087  -7.78049  9.37603  1.000 33.75628 ? 77  GLN A O   1 
ATOM   609  C CB  . GLN A 1 77  ? -7.77145  -5.93772  12.22852 1.000 20.30652 ? 77  GLN A CB  1 
ATOM   610  C CG  . GLN A 1 77  ? -9.29722  -5.98254  12.08402 1.000 48.50021 ? 77  GLN A CG  1 
ATOM   611  C CD  . GLN A 1 77  ? -9.92608  -7.19203  12.73071 1.000 68.40914 ? 77  GLN A CD  1 
ATOM   612  O OE1 . GLN A 1 77  ? -10.38888 -8.10656  12.04689 1.000 66.15192 ? 77  GLN A OE1 1 
ATOM   613  N NE2 . GLN A 1 77  ? -9.95839  -7.20153  14.06139 1.000 70.87460 ? 77  GLN A NE2 1 
ATOM   614  N N   . TYR A 1 78  ? -7.11296  -5.71963  9.18866  1.000 27.47748 ? 78  TYR A N   1 
ATOM   615  C CA  . TYR A 1 78  ? -7.57004  -5.48899  7.82157  1.000 27.32452 ? 78  TYR A CA  1 
ATOM   616  C C   . TYR A 1 78  ? -6.45723  -5.58039  6.78950  1.000 29.86973 ? 78  TYR A C   1 
ATOM   617  O O   . TYR A 1 78  ? -6.57009  -6.32173  5.81410  1.000 50.94728 ? 78  TYR A O   1 
ATOM   618  C CB  . TYR A 1 78  ? -8.27516  -4.13285  7.72613  1.000 32.87634 ? 78  TYR A CB  1 
ATOM   619  C CG  . TYR A 1 78  ? -9.53589  -4.14946  8.55655  1.000 52.70034 ? 78  TYR A CG  1 
ATOM   620  C CD1 . TYR A 1 78  ? -10.64998 -4.88561  8.15417  1.000 39.83894 ? 78  TYR A CD1 1 
ATOM   621  C CD2 . TYR A 1 78  ? -9.61434  -3.43530  9.74495  1.000 53.85234 ? 78  TYR A CD2 1 
ATOM   622  C CE1 . TYR A 1 78  ? -11.80830 -4.91494  8.92673  1.000 59.61293 ? 78  TYR A CE1 1 
ATOM   623  C CE2 . TYR A 1 78  ? -10.76852 -3.44837  10.51707 1.000 70.48458 ? 78  TYR A CE2 1 
ATOM   624  C CZ  . TYR A 1 78  ? -11.86138 -4.18967  10.10533 1.000 66.61061 ? 78  TYR A CZ  1 
ATOM   625  O OH  . TYR A 1 78  ? -13.00057 -4.20372  10.87929 1.000 61.84849 ? 78  TYR A OH  1 
ATOM   626  N N   . GLY A 1 79  ? -5.38973  -4.84597  6.98699  1.000 23.42483 ? 79  GLY A N   1 
ATOM   627  C CA  . GLY A 1 79  ? -4.22093  -4.74976  6.14961  1.000 25.94489 ? 79  GLY A CA  1 
ATOM   628  C C   . GLY A 1 79  ? -3.97444  -3.30033  5.80113  1.000 29.30787 ? 79  GLY A C   1 
ATOM   629  O O   . GLY A 1 79  ? -4.60282  -2.38437  6.35207  1.000 17.46575 ? 79  GLY A O   1 
ATOM   630  N N   . ILE A 1 80  ? -3.07336  -3.07053  4.84896  1.000 15.54919 ? 80  ILE A N   1 
ATOM   631  C CA  . ILE A 1 80  ? -2.68913  -1.71057  4.48385  1.000 20.09591 ? 80  ILE A CA  1 
ATOM   632  C C   . ILE A 1 80  ? -2.45913  -1.66835  2.98773  1.000 17.04503 ? 80  ILE A C   1 
ATOM   633  O O   . ILE A 1 80  ? -1.97533  -2.63193  2.38504  1.000 22.00714 ? 80  ILE A O   1 
ATOM   634  C CB  . ILE A 1 80  ? -1.44785  -1.23290  5.27228  1.000 17.91637 ? 80  ILE A CB  1 
ATOM   635  C CG1 . ILE A 1 80  ? -1.28766  0.28438   5.17001  1.000 12.01673 ? 80  ILE A CG1 1 
ATOM   636  C CG2 . ILE A 1 80  ? -0.19688  -2.01087  4.86092  1.000 17.49048 ? 80  ILE A CG2 1 
ATOM   637  C CD1 . ILE A 1 80  ? -0.46797  0.83866   6.32402  1.000 20.44213 ? 80  ILE A CD1 1 
ATOM   638  N N   . HIS A 1 81  ? -2.74493  -0.52126  2.39509  1.000 16.33340 ? 81  HIS A N   1 
ATOM   639  C CA  . HIS A 1 81  ? -2.45605  -0.36953  0.98189  1.000 17.39559 ? 81  HIS A CA  1 
ATOM   640  C C   . HIS A 1 81  ? -1.05645  0.16110   0.75548  1.000 11.35764 ? 81  HIS A C   1 
ATOM   641  O O   . HIS A 1 81  ? -0.42577  0.71054   1.65819  1.000 15.59724 ? 81  HIS A O   1 
ATOM   642  C CB  . HIS A 1 81  ? -3.48138  0.57816   0.37427  1.000 21.88198 ? 81  HIS A CB  1 
ATOM   643  C CG  . HIS A 1 81  ? -4.75694  -0.11515  0.04150  1.000 15.19446 ? 81  HIS A CG  1 
ATOM   644  N ND1 . HIS A 1 81  ? -4.92886  -0.85863  -1.10384 1.000 17.82011 ? 81  HIS A ND1 1 
ATOM   645  C CD2 . HIS A 1 81  ? -5.90753  -0.22668  0.74306  1.000 23.85886 ? 81  HIS A CD2 1 
ATOM   646  C CE1 . HIS A 1 81  ? -6.14222  -1.37996  -1.10721 1.000 24.19020 ? 81  HIS A CE1 1 
ATOM   647  N NE2 . HIS A 1 81  ? -6.75851  -1.01017  0.00078  1.000 19.07444 ? 81  HIS A NE2 1 
ATOM   648  N N   . TYR A 1 82  ? -0.58609  0.03204   -0.48592 1.000 12.60771 ? 82  TYR A N   1 
ATOM   649  C CA  . TYR A 1 82  ? 0.61928   0.75572   -0.87733 1.000 14.73736 ? 82  TYR A CA  1 
ATOM   650  C C   . TYR A 1 82  ? 0.41290   2.25352   -0.79744 1.000 17.45448 ? 82  TYR A C   1 
ATOM   651  O O   . TYR A 1 82  ? -0.71088  2.75624   -0.91801 1.000 21.04438 ? 82  TYR A O   1 
ATOM   652  C CB  . TYR A 1 82  ? 1.06217   0.41536   -2.30200 1.000 15.18709 ? 82  TYR A CB  1 
ATOM   653  C CG  . TYR A 1 82  ? 1.51717   -1.00041  -2.48992 1.000 17.10450 ? 82  TYR A CG  1 
ATOM   654  C CD1 . TYR A 1 82  ? 2.51984   -1.52009  -1.69087 1.000 18.44428 ? 82  TYR A CD1 1 
ATOM   655  C CD2 . TYR A 1 82  ? 0.98429   -1.81269  -3.50032 1.000 23.99246 ? 82  TYR A CD2 1 
ATOM   656  C CE1 . TYR A 1 82  ? 2.96756   -2.83165  -1.86513 1.000 36.38680 ? 82  TYR A CE1 1 
ATOM   657  C CE2 . TYR A 1 82  ? 1.42965   -3.12452  -3.68019 1.000 30.76206 ? 82  TYR A CE2 1 
ATOM   658  C CZ  . TYR A 1 82  ? 2.42086   -3.62743  -2.86049 1.000 26.86113 ? 82  TYR A CZ  1 
ATOM   659  O OH  . TYR A 1 82  ? 2.88604   -4.91953  -3.00806 1.000 25.56700 ? 82  TYR A OH  1 
ATOM   660  N N   . ARG A 1 83  ? 1.49810   2.95995   -0.47733 1.000 10.49502 ? 83  ARG A N   1 
ATOM   661  C CA  . ARG A 1 83  ? 1.39167   4.40594   -0.36393 1.000 17.80338 ? 83  ARG A CA  1 
ATOM   662  C C   . ARG A 1 83  ? 0.90482   4.98024   -1.68893 1.000 12.91295 ? 83  ARG A C   1 
ATOM   663  O O   . ARG A 1 83  ? 0.02723   5.84527   -1.72973 1.000 16.86061 ? 83  ARG A O   1 
ATOM   664  C CB  . ARG A 1 83  ? 2.73928   4.99489   0.02279  1.000 20.74448 ? 83  ARG A CB  1 
ATOM   665  C CG  . ARG A 1 83  ? 2.66479   6.40974   0.50328  1.000 33.22461 ? 83  ARG A CG  1 
ATOM   666  C CD  . ARG A 1 83  ? 3.95505   6.76935   1.17678  1.000 43.85084 ? 83  ARG A CD  1 
ATOM   667  N NE  . ARG A 1 83  ? 3.79677   7.85549   2.13176  1.000 40.82787 ? 83  ARG A NE  1 
ATOM   668  C CZ  . ARG A 1 83  ? 4.12995   9.11600   1.89950  1.000 50.44750 ? 83  ARG A CZ  1 
ATOM   669  N NH1 . ARG A 1 83  ? 4.81631   9.46090   0.81855  1.000 30.13818 ? 83  ARG A NH1 1 
ATOM   670  N NH2 . ARG A 1 83  ? 3.84318   10.03797  2.81888  1.000 35.48334 ? 83  ARG A NH2 1 
ATOM   671  N N   . ASN A 1 84  ? 1.43499   4.43907   -2.78902 1.000 15.24578 ? 84  ASN A N   1 
ATOM   672  C CA  . ASN A 1 84  ? 1.02726   4.78515   -4.14455 1.000 13.26986 ? 84  ASN A CA  1 
ATOM   673  C C   . ASN A 1 84  ? -0.47101  4.66206   -4.35290 1.000 28.31303 ? 84  ASN A C   1 
ATOM   674  O O   . ASN A 1 84  ? -1.07168  5.45497   -5.08406 1.000 22.12164 ? 84  ASN A O   1 
ATOM   675  C CB  . ASN A 1 84  ? 1.77462   3.91810   -5.15549 1.000 29.88904 ? 84  ASN A CB  1 
ATOM   676  C CG  . ASN A 1 84  ? 1.72185   4.49816   -6.53423 1.000 41.93827 ? 84  ASN A CG  1 
ATOM   677  O OD1 . ASN A 1 84  ? 0.91421   4.07305   -7.36090 1.000 36.99710 ? 84  ASN A OD1 1 
ATOM   678  N ND2 . ASN A 1 84  ? 2.52680   5.53175   -6.77497 1.000 37.41582 ? 84  ASN A ND2 1 
ATOM   679  N N   . THR A 1 85  ? -1.09638  3.66788   -3.74423 1.000 17.24582 ? 85  THR A N   1 
ATOM   680  C CA  . THR A 1 85  ? -2.51832  3.52406   -3.99305 1.000 24.05480 ? 85  THR A CA  1 
ATOM   681  C C   . THR A 1 85  ? -3.34326  4.41055   -3.07670 1.000 22.53260 ? 85  THR A C   1 
ATOM   682  O O   . THR A 1 85  ? -4.47591  4.76775   -3.42632 1.000 28.81491 ? 85  THR A O   1 
ATOM   683  C CB  . THR A 1 85  ? -2.94962  2.07209   -3.70328 1.000 23.24858 ? 85  THR A CB  1 
ATOM   684  O OG1 . THR A 1 85  ? -1.93119  1.15177   -4.12150 1.000 21.40898 ? 85  THR A OG1 1 
ATOM   685  C CG2 . THR A 1 85  ? -4.25491  1.74025   -4.39454 1.000 36.42067 ? 85  THR A CG2 1 
ATOM   686  N N   . TYR A 1 86  ? -2.76919  4.84817   -1.96010 1.000 29.10642 ? 86  TYR A N   1 
ATOM   687  C CA  . TYR A 1 86  ? -3.49395  5.61667   -0.94868 1.000 12.51802 ? 86  TYR A CA  1 
ATOM   688  C C   . TYR A 1 86  ? -2.48507  6.64064   -0.43254 1.000 18.75143 ? 86  TYR A C   1 
ATOM   689  O O   . TYR A 1 86  ? -1.89441  6.48420   0.64477  1.000 12.89882 ? 86  TYR A O   1 
ATOM   690  C CB  . TYR A 1 86  ? -3.99586  4.65794   0.13263  1.000 17.65136 ? 86  TYR A CB  1 
ATOM   691  C CG  . TYR A 1 86  ? -5.15274  5.08586   1.00474  1.000 13.48233 ? 86  TYR A CG  1 
ATOM   692  C CD1 . TYR A 1 86  ? -5.36567  6.39745   1.33011  1.000 10.70508 ? 86  TYR A CD1 1 
ATOM   693  C CD2 . TYR A 1 86  ? -6.05177  4.13352   1.48355  1.000 17.05535 ? 86  TYR A CD2 1 
ATOM   694  C CE1 . TYR A 1 86  ? -6.44321  6.77478   2.11228  1.000 24.63520 ? 86  TYR A CE1 1 
ATOM   695  C CE2 . TYR A 1 86  ? -7.14515  4.49060   2.25722  1.000 7.60371  ? 86  TYR A CE2 1 
ATOM   696  C CZ  . TYR A 1 86  ? -7.32608  5.82126   2.57568  1.000 18.84498 ? 86  TYR A CZ  1 
ATOM   697  O OH  . TYR A 1 86  ? -8.39520  6.21374   3.35475  1.000 22.77597 ? 86  TYR A OH  1 
ATOM   698  N N   . PRO A 1 87  ? -2.16924  7.63835   -1.25947 1.000 22.43088 ? 87  PRO A N   1 
ATOM   699  C CA  . PRO A 1 87  ? -1.08613  8.58469   -0.95428 1.000 19.88314 ? 87  PRO A CA  1 
ATOM   700  C C   . PRO A 1 87  ? -1.43589  9.56676   0.14926  1.000 16.19862 ? 87  PRO A C   1 
ATOM   701  O O   . PRO A 1 87  ? -2.60510  9.79532   0.46489  1.000 21.30164 ? 87  PRO A O   1 
ATOM   702  C CB  . PRO A 1 87  ? -0.86959  9.31864   -2.28283 1.000 18.79297 ? 87  PRO A CB  1 
ATOM   703  C CG  . PRO A 1 87  ? -2.21072  9.30544   -2.93117 1.000 20.34261 ? 87  PRO A CG  1 
ATOM   704  C CD  . PRO A 1 87  ? -2.89006  8.00967   -2.49534 1.000 18.04120 ? 87  PRO A CD  1 
ATOM   705  N N   . TYR A 1 88  ? -0.38595  10.11533  0.76885  1.000 14.65598 ? 88  TYR A N   1 
ATOM   706  C CA  . TYR A 1 88  ? -0.54660  10.94941  1.95047  1.000 19.57940 ? 88  TYR A CA  1 
ATOM   707  C C   . TYR A 1 88  ? -1.08152  12.29751  1.47265  1.000 14.35239 ? 88  TYR A C   1 
ATOM   708  O O   . TYR A 1 88  ? -0.57047  12.87186  0.51017  1.000 25.89018 ? 88  TYR A O   1 
ATOM   709  C CB  . TYR A 1 88  ? 0.79713   11.17504  2.63056  1.000 20.73972 ? 88  TYR A CB  1 
ATOM   710  C CG  . TYR A 1 88  ? 0.74856   11.93202  3.94714  1.000 16.88447 ? 88  TYR A CG  1 
ATOM   711  C CD1 . TYR A 1 88  ? -0.02528  11.45561  5.02064  1.000 9.47332  ? 88  TYR A CD1 1 
ATOM   712  C CD2 . TYR A 1 88  ? 1.39836   13.16065  4.08699  1.000 11.98540 ? 88  TYR A CD2 1 
ATOM   713  C CE1 . TYR A 1 88  ? -0.07799  12.14228  6.23591  1.000 15.23064 ? 88  TYR A CE1 1 
ATOM   714  C CE2 . TYR A 1 88  ? 1.34833   13.85443  5.27552  1.000 11.96935 ? 88  TYR A CE2 1 
ATOM   715  C CZ  . TYR A 1 88  ? 0.60330   13.35081  6.34516  1.000 20.26060 ? 88  TYR A CZ  1 
ATOM   716  O OH  . TYR A 1 88  ? 0.57379   14.06351  7.51560  1.000 22.91034 ? 88  TYR A OH  1 
ATOM   717  N N   . GLU A 1 89  ? -2.06878  12.83235  2.18255  1.000 14.40727 ? 89  GLU A N   1 
ATOM   718  C CA  . GLU A 1 89  ? -2.61560  14.16322  1.93708  1.000 24.07959 ? 89  GLU A CA  1 
ATOM   719  C C   . GLU A 1 89  ? -2.42138  15.15574  3.07016  1.000 20.84356 ? 89  GLU A C   1 
ATOM   720  O O   . GLU A 1 89  ? -2.61921  16.35448  2.85279  1.000 25.44271 ? 89  GLU A O   1 
ATOM   721  C CB  . GLU A 1 89  ? -4.11259  14.04457  1.61952  1.000 23.91566 ? 89  GLU A CB  1 
ATOM   722  C CG  . GLU A 1 89  ? -4.40702  12.80502  0.76117  1.000 25.42717 ? 89  GLU A CG  1 
ATOM   723  C CD  . GLU A 1 89  ? -5.85034  12.70488  0.27730  1.000 22.40313 ? 89  GLU A CD  1 
ATOM   724  O OE1 . GLU A 1 89  ? -6.45219  13.73040  -0.13433 1.000 25.43037 ? 89  GLU A OE1 1 
ATOM   725  O OE2 . GLU A 1 89  ? -6.37800  11.57726  0.31567  1.000 22.34256 ? 89  GLU A OE2 1 
ATOM   726  N N   . GLY A 1 90  ? -2.12115  14.68747  4.27547  1.000 23.34390 ? 90  GLY A N   1 
ATOM   727  C CA  . GLY A 1 90  ? -1.85613  15.53640  5.41674  1.000 26.71305 ? 90  GLY A CA  1 
ATOM   728  C C   . GLY A 1 90  ? -3.09935  16.12668  6.01820  1.000 23.39991 ? 90  GLY A C   1 
ATOM   729  O O   . GLY A 1 90  ? -3.03526  17.15256  6.70087  1.000 32.46864 ? 90  GLY A O   1 
ATOM   730  N N   . VAL A 1 91  ? -4.23441  15.48776  5.77395  1.000 23.95182 ? 91  VAL A N   1 
ATOM   731  C CA  . VAL A 1 91  ? -5.54072  15.82873  6.32295  1.000 29.67285 ? 91  VAL A CA  1 
ATOM   732  C C   . VAL A 1 91  ? -6.25502  14.50835  6.48765  1.000 21.26643 ? 91  VAL A C   1 
ATOM   733  O O   . VAL A 1 91  ? -6.10278  13.60240  5.66414  1.000 25.92730 ? 91  VAL A O   1 
ATOM   734  C CB  . VAL A 1 91  ? -6.36905  16.83156  5.47764  1.000 25.28265 ? 91  VAL A CB  1 
ATOM   735  C CG1 . VAL A 1 91  ? -5.61620  18.13343  5.25430  1.000 39.66385 ? 91  VAL A CG1 1 
ATOM   736  C CG2 . VAL A 1 91  ? -6.72681  16.23461  4.11626  1.000 24.21144 ? 91  VAL A CG2 1 
ATOM   737  N N   . GLN A 1 92  ? -6.98539  14.36317  7.56586  1.000 17.42795 ? 92  GLN A N   1 
ATOM   738  C CA  . GLN A 1 92  ? -7.78809  13.17004  7.67278  1.000 19.23592 ? 92  GLN A CA  1 
ATOM   739  C C   . GLN A 1 92  ? -8.99924  13.31787  6.76194  1.000 20.01671 ? 92  GLN A C   1 
ATOM   740  O O   . GLN A 1 92  ? -9.60640  14.38917  6.67379  1.000 21.48035 ? 92  GLN A O   1 
ATOM   741  C CB  . GLN A 1 92  ? -8.30009  12.95098  9.08535  1.000 11.30074 ? 92  GLN A CB  1 
ATOM   742  C CG  . GLN A 1 92  ? -9.20340  11.74450  9.12994  1.000 13.03441 ? 92  GLN A CG  1 
ATOM   743  C CD  . GLN A 1 92  ? -9.62835  11.34765  10.53558 1.000 24.37667 ? 92  GLN A CD  1 
ATOM   744  O OE1 . GLN A 1 92  ? -9.46280  10.19963  10.96297 1.000 18.53114 ? 92  GLN A OE1 1 
ATOM   745  N NE2 . GLN A 1 92  ? -10.23152 12.29516  11.24350 1.000 18.65780 ? 92  GLN A NE2 1 
ATOM   746  N N   . ARG A 1 93  ? -9.29904  12.26167  6.02467  1.000 21.58422 ? 93  ARG A N   1 
ATOM   747  C CA  . ARG A 1 93  ? -10.41437 12.24833  5.09113  1.000 29.03343 ? 93  ARG A CA  1 
ATOM   748  C C   . ARG A 1 93  ? -11.23734 11.00671  5.43862  1.000 25.04304 ? 93  ARG A C   1 
ATOM   749  O O   . ARG A 1 93  ? -10.92006 10.28602  6.39112  1.000 26.41832 ? 93  ARG A O   1 
ATOM   750  C CB  . ARG A 1 93  ? -9.91667  12.25251  3.63995  1.000 23.22302 ? 93  ARG A CB  1 
ATOM   751  C CG  . ARG A 1 93  ? -9.44632  13.60379  3.19049  1.000 13.75084 ? 93  ARG A CG  1 
ATOM   752  C CD  . ARG A 1 93  ? -8.99787  13.55720  1.74716  1.000 18.96326 ? 93  ARG A CD  1 
ATOM   753  N NE  . ARG A 1 93  ? -10.16031 13.56013  0.87205  1.000 17.57549 ? 93  ARG A NE  1 
ATOM   754  C CZ  . ARG A 1 93  ? -10.11487 13.35450  -0.43427 1.000 24.80827 ? 93  ARG A CZ  1 
ATOM   755  N NH1 . ARG A 1 93  ? -8.96857  13.14002  -1.06218 1.000 17.48781 ? 93  ARG A NH1 1 
ATOM   756  N NH2 . ARG A 1 93  ? -11.24758 13.37714  -1.13277 1.000 26.76936 ? 93  ARG A NH2 1 
ATOM   757  N N   A TYR A 1 94  ? -12.30851 10.76956  4.68557  0.471 27.85923 ? 94  TYR A N   1 
ATOM   758  N N   B TYR A 1 94  ? -12.29858 10.74837  4.67772  0.529 27.85966 ? 94  TYR A N   1 
ATOM   759  C CA  A TYR A 1 94  ? -13.08140 9.54690   4.86352  0.471 29.38011 ? 94  TYR A CA  1 
ATOM   760  C CA  B TYR A 1 94  ? -13.09210 9.54894   4.92017  0.529 29.35748 ? 94  TYR A CA  1 
ATOM   761  C C   A TYR A 1 94  ? -12.19957 8.32996   4.60466  0.471 26.40931 ? 94  TYR A C   1 
ATOM   762  C C   B TYR A 1 94  ? -12.30892 8.30228   4.51537  0.529 26.45590 ? 94  TYR A C   1 
ATOM   763  O O   A TYR A 1 94  ? -11.23733 8.38928   3.83408  0.471 28.50038 ? 94  TYR A O   1 
ATOM   764  O O   B TYR A 1 94  ? -11.52182 8.31846   3.56532  0.529 29.54012 ? 94  TYR A O   1 
ATOM   765  C CB  A TYR A 1 94  ? -14.28136 9.53644   3.91751  0.471 32.76291 ? 94  TYR A CB  1 
ATOM   766  C CB  B TYR A 1 94  ? -14.42753 9.62092   4.17222  0.529 33.27817 ? 94  TYR A CB  1 
ATOM   767  C CG  A TYR A 1 94  ? -15.20174 10.72171  4.08629  0.471 32.57663 ? 94  TYR A CG  1 
ATOM   768  C CG  B TYR A 1 94  ? -14.36808 9.38368   2.67473  0.529 30.07009 ? 94  TYR A CG  1 
ATOM   769  C CD1 A TYR A 1 94  ? -15.64500 11.10780  5.34566  0.471 26.38977 ? 94  TYR A CD1 1 
ATOM   770  C CD1 B TYR A 1 94  ? -13.82904 10.33744  1.81979  0.529 37.15664 ? 94  TYR A CD1 1 
ATOM   771  C CD2 A TYR A 1 94  ? -15.62679 11.45566  2.98577  0.471 33.31246 ? 94  TYR A CD2 1 
ATOM   772  C CD2 B TYR A 1 94  ? -14.89716 8.22263   2.11080  0.529 35.24681 ? 94  TYR A CD2 1 
ATOM   773  C CE1 A TYR A 1 94  ? -16.48459 12.18849  5.50202  0.471 20.47427 ? 94  TYR A CE1 1 
ATOM   774  C CE1 B TYR A 1 94  ? -13.79514 10.13221  0.44806  0.529 36.07422 ? 94  TYR A CE1 1 
ATOM   775  C CE2 A TYR A 1 94  ? -16.46993 12.53456  3.13250  0.471 32.82747 ? 94  TYR A CE2 1 
ATOM   776  C CE2 B TYR A 1 94  ? -14.87094 8.01250   0.74192  0.529 28.24408 ? 94  TYR A CE2 1 
ATOM   777  C CZ  A TYR A 1 94  ? -16.89522 12.89636  4.39159  0.471 34.25659 ? 94  TYR A CZ  1 
ATOM   778  C CZ  B TYR A 1 94  ? -14.31566 8.97073   -0.08414 0.529 31.18010 ? 94  TYR A CZ  1 
ATOM   779  O OH  A TYR A 1 94  ? -17.73379 13.97634  4.53742  0.471 40.07996 ? 94  TYR A OH  1 
ATOM   780  O OH  B TYR A 1 94  ? -14.27029 8.77034   -1.44827 0.529 29.73521 ? 94  TYR A OH  1 
ATOM   781  N N   . CYS A 1 95  ? -12.52414 7.21517   5.25905  1.000 26.41386 ? 95  CYS A N   1 
ATOM   782  C CA  . CYS A 1 95  ? -11.72988 6.00106   5.08806  1.000 17.60098 ? 95  CYS A CA  1 
ATOM   783  C C   . CYS A 1 95  ? -12.03571 5.31152   3.76142  1.000 22.70342 ? 95  CYS A C   1 
ATOM   784  O O   . CYS A 1 95  ? -13.17610 4.91959   3.49913  1.000 26.66917 ? 95  CYS A O   1 
ATOM   785  C CB  . CYS A 1 95  ? -11.98653 5.02501   6.23069  1.000 27.56889 ? 95  CYS A CB  1 
ATOM   786  S SG  . CYS A 1 95  ? -11.20208 3.40131   5.93144  1.000 34.16904 ? 95  CYS A SG  1 
ATOM   787  N N   . ARG A 1 96  ? -11.01067 5.14273   2.93145  1.000 21.64273 ? 96  ARG A N   1 
ATOM   788  C CA  . ARG A 1 96  ? -11.22168 4.66125   1.57629  1.000 20.89242 ? 96  ARG A CA  1 
ATOM   789  C C   . ARG A 1 96  ? -10.64164 3.27123   1.31318  1.000 23.26532 ? 96  ARG A C   1 
ATOM   790  O O   . ARG A 1 96  ? -10.51305 2.89667   0.14422  1.000 33.04932 ? 96  ARG A O   1 
ATOM   791  C CB  . ARG A 1 96  ? -10.61783 5.69183   0.62606  1.000 21.98835 ? 96  ARG A CB  1 
ATOM   792  C CG  . ARG A 1 96  ? -11.37166 7.00564   0.64539  1.000 22.53766 ? 96  ARG A CG  1 
ATOM   793  C CD  . ARG A 1 96  ? -10.51482 8.04802   0.04844  1.000 23.77500 ? 96  ARG A CD  1 
ATOM   794  N NE  . ARG A 1 96  ? -9.67167  8.63607   1.08354  1.000 21.93193 ? 96  ARG A NE  1 
ATOM   795  C CZ  . ARG A 1 96  ? -8.71079  9.51923   0.85097  1.000 19.78656 ? 96  ARG A CZ  1 
ATOM   796  N NH1 . ARG A 1 96  ? -8.47942  9.98270   -0.36850 1.000 17.31042 ? 96  ARG A NH1 1 
ATOM   797  N NH2 . ARG A 1 96  ? -7.93407  9.91358   1.85833  1.000 21.92963 ? 96  ARG A NH2 1 
ATOM   798  N N   . SER A 1 97  ? -10.20572 2.53564   2.34721  1.000 20.22901 ? 97  SER A N   1 
ATOM   799  C CA  . SER A 1 97  ? -9.58660  1.23146   2.11904  1.000 29.94864 ? 97  SER A CA  1 
ATOM   800  C C   . SER A 1 97  ? -10.35048 0.39172   1.09814  1.000 25.64732 ? 97  SER A C   1 
ATOM   801  O O   . SER A 1 97  ? -9.81743  -0.00238  0.05687  1.000 48.58851 ? 97  SER A O   1 
ATOM   802  C CB  . SER A 1 97  ? -9.50683  0.49933   3.45844  1.000 25.34560 ? 97  SER A CB  1 
ATOM   803  O OG  . SER A 1 97  ? -8.66782  1.21210   4.33600  1.000 33.60523 ? 97  SER A OG  1 
ATOM   804  N N   . ARG A 1 98  ? -11.61086 0.09914   1.42166  1.000 18.33688 ? 98  ARG A N   1 
ATOM   805  C CA  . ARG A 1 98  ? -12.48200 -0.72654  0.58125  1.000 36.05558 ? 98  ARG A CA  1 
ATOM   806  C C   . ARG A 1 98  ? -12.53321 -0.27507  -0.86663 1.000 27.85262 ? 98  ARG A C   1 
ATOM   807  O O   . ARG A 1 98  ? -12.46112 -1.08982  -1.79436 1.000 41.44279 ? 98  ARG A O   1 
ATOM   808  C CB  . ARG A 1 98  ? -13.89708 -0.91393  1.13185  1.000 53.77244 ? 98  ARG A CB  1 
ATOM   809  C CG  . ARG A 1 98  ? -14.15368 -0.83790  2.60692  1.000 69.16501 ? 98  ARG A CG  1 
ATOM   810  C CD  . ARG A 1 98  ? -15.68190 -0.78726  2.78752  1.000 98.63598 ? 98  ARG A CD  1 
ATOM   811  N NE  . ARG A 1 98  ? -16.37327 -1.79143  1.97593  1.000 93.19563 ? 98  ARG A NE  1 
ATOM   812  C CZ  . ARG A 1 98  ? -17.15945 -2.75752  2.43181  1.000 81.06924 ? 98  ARG A CZ  1 
ATOM   813  N NH1 . ARG A 1 98  ? -17.23937 -3.03470  3.72221  1.000 75.19323 ? 98  ARG A NH1 1 
ATOM   814  N NH2 . ARG A 1 98  ? -17.84299 -3.49958  1.56338  1.000 78.93288 ? 98  ARG A NH2 1 
ATOM   815  N N   . GLU A 1 99  ? -12.61709 1.03221   -1.07124 1.000 25.38864 ? 99  GLU A N   1 
ATOM   816  C CA  . GLU A 1 99  ? -12.69064 1.63818   -2.39191 1.000 31.03944 ? 99  GLU A CA  1 
ATOM   817  C C   . GLU A 1 99  ? -11.40008 1.61607   -3.19120 1.000 28.31032 ? 99  GLU A C   1 
ATOM   818  O O   . GLU A 1 99  ? -11.40979 2.06905   -4.33768 1.000 34.77494 ? 99  GLU A O   1 
ATOM   819  C CB  . GLU A 1 99  ? -13.08175 3.08904   -2.12227 1.000 20.78974 ? 99  GLU A CB  1 
ATOM   820  C CG  . GLU A 1 99  ? -14.12758 3.74109   -2.95256 1.000 60.00475 ? 99  GLU A CG  1 
ATOM   821  C CD  . GLU A 1 99  ? -14.34203 5.17857   -2.48212 1.000 68.70057 ? 99  GLU A CD  1 
ATOM   822  O OE1 . GLU A 1 99  ? -13.49921 6.05856   -2.79539 1.000 53.16632 ? 99  GLU A OE1 1 
ATOM   823  O OE2 . GLU A 1 99  ? -15.34265 5.42487   -1.78213 1.000 88.12084 ? 99  GLU A OE2 1 
ATOM   824  N N   . LYS A 1 100 ? -10.31043 1.07790   -2.66497 1.000 29.46610 ? 100 LYS A N   1 
ATOM   825  C CA  . LYS A 1 100 ? -9.01155  1.13268   -3.31716 1.000 18.49684 ? 100 LYS A CA  1 
ATOM   826  C C   . LYS A 1 100 ? -8.55605  -0.25270  -3.75122 1.000 37.82218 ? 100 LYS A C   1 
ATOM   827  O O   . LYS A 1 100 ? -7.43839  -0.40033  -4.26943 1.000 37.07283 ? 100 LYS A O   1 
ATOM   828  C CB  . LYS A 1 100 ? -7.96326  1.90481   -2.51047 1.000 27.57345 ? 100 LYS A CB  1 
ATOM   829  C CG  . LYS A 1 100 ? -8.31583  3.39333   -2.43313 1.000 25.75462 ? 100 LYS A CG  1 
ATOM   830  C CD  . LYS A 1 100 ? -7.27065  4.20226   -1.70292 1.000 26.01701 ? 100 LYS A CD  1 
ATOM   831  C CE  . LYS A 1 100 ? -7.51869  5.71380   -1.76753 1.000 20.46048 ? 100 LYS A CE  1 
ATOM   832  N NZ  . LYS A 1 100 ? -7.04211  6.28200   -3.07005 1.000 18.02069 ? 100 LYS A NZ  1 
ATOM   833  N N   . GLY A 1 101 ? -9.39225  -1.27391  -3.53193 1.000 31.74914 ? 101 GLY A N   1 
ATOM   834  C CA  . GLY A 1 101 ? -9.05502  -2.64710  -3.83455 1.000 30.37544 ? 101 GLY A CA  1 
ATOM   835  C C   . GLY A 1 101 ? -8.46606  -3.43073  -2.68151 1.000 28.09169 ? 101 GLY A C   1 
ATOM   836  O O   . GLY A 1 101 ? -8.47649  -2.99672  -1.52872 1.000 21.55459 ? 101 GLY A O   1 
ATOM   837  N N   . PRO A 1 102 ? -8.10096  -4.67725  -2.96554 1.000 32.92314 ? 102 PRO A N   1 
ATOM   838  C CA  . PRO A 1 102 ? -7.52770  -5.54452  -1.93006 1.000 31.35488 ? 102 PRO A CA  1 
ATOM   839  C C   . PRO A 1 102 ? -6.32494  -4.89031  -1.26490 1.000 27.66961 ? 102 PRO A C   1 
ATOM   840  O O   . PRO A 1 102 ? -5.51134  -4.23112  -1.91955 1.000 24.30771 ? 102 PRO A O   1 
ATOM   841  C CB  . PRO A 1 102 ? -7.14126  -6.81415  -2.71446 1.000 29.13593 ? 102 PRO A CB  1 
ATOM   842  C CG  . PRO A 1 102 ? -7.69299  -6.56538  -4.12802 1.000 47.95782 ? 102 PRO A CG  1 
ATOM   843  C CD  . PRO A 1 102 ? -7.61866  -5.10010  -4.27973 1.000 44.79897 ? 102 PRO A CD  1 
ATOM   844  N N   A TYR A 1 103 ? -6.22283  -5.05844  0.05271  0.474 24.19898 ? 103 TYR A N   1 
ATOM   845  N N   B TYR A 1 103 ? -6.21554  -5.10267  0.05099  0.526 24.19423 ? 103 TYR A N   1 
ATOM   846  C CA  A TYR A 1 103 ? -5.06994  -4.54296  0.78071  0.474 21.35833 ? 103 TYR A CA  1 
ATOM   847  C CA  B TYR A 1 103 ? -5.05326  -4.64256  0.79825  0.526 21.37777 ? 103 TYR A CA  1 
ATOM   848  C C   A TYR A 1 103 ? -3.78880  -5.13624  0.20587  0.474 18.23524 ? 103 TYR A C   1 
ATOM   849  C C   B TYR A 1 103 ? -3.78497  -5.10840  0.10144  0.526 18.16541 ? 103 TYR A C   1 
ATOM   850  O O   A TYR A 1 103 ? -3.78682  -6.23829  -0.34488 0.474 21.63461 ? 103 TYR A O   1 
ATOM   851  O O   B TYR A 1 103 ? -3.78991  -6.09108  -0.64445 0.526 21.50473 ? 103 TYR A O   1 
ATOM   852  C CB  A TYR A 1 103 ? -5.19228  -4.86756  2.27387  0.474 19.80434 ? 103 TYR A CB  1 
ATOM   853  C CB  B TYR A 1 103 ? -5.09759  -5.14256  2.25840  0.526 20.02875 ? 103 TYR A CB  1 
ATOM   854  C CG  A TYR A 1 103 ? -6.37839  -4.21622  2.95695  0.474 20.87680 ? 103 TYR A CG  1 
ATOM   855  C CG  B TYR A 1 103 ? -5.02071  -6.65778  2.47659  0.526 18.82557 ? 103 TYR A CG  1 
ATOM   856  C CD1 A TYR A 1 103 ? -6.30173  -2.91339  3.43864  0.474 21.19045 ? 103 TYR A CD1 1 
ATOM   857  C CD1 B TYR A 1 103 ? -3.87244  -7.38572  2.15279  0.526 20.85425 ? 103 TYR A CD1 1 
ATOM   858  C CD2 A TYR A 1 103 ? -7.57744  -4.90343  3.11690  0.474 27.10066 ? 103 TYR A CD2 1 
ATOM   859  C CD2 B TYR A 1 103 ? -6.08167  -7.35060  3.04230  0.526 16.74974 ? 103 TYR A CD2 1 
ATOM   860  C CE1 A TYR A 1 103 ? -7.37774  -2.31785  4.06144  0.474 21.44644 ? 103 TYR A CE1 1 
ATOM   861  C CE1 B TYR A 1 103 ? -3.79996  -8.76077  2.34867  0.526 16.66587 ? 103 TYR A CE1 1 
ATOM   862  C CE2 A TYR A 1 103 ? -8.66330  -4.31183  3.74058  0.474 29.03679 ? 103 TYR A CE2 1 
ATOM   863  C CE2 B TYR A 1 103 ? -6.01358  -8.73044  3.25289  0.526 23.84433 ? 103 TYR A CE2 1 
ATOM   864  C CZ  A TYR A 1 103 ? -8.55515  -3.01768  4.20879  0.474 29.97154 ? 103 TYR A CZ  1 
ATOM   865  C CZ  B TYR A 1 103 ? -4.86912  -9.42573  2.89990  0.526 16.57439 ? 103 TYR A CZ  1 
ATOM   866  O OH  A TYR A 1 103 ? -9.62659  -2.41686  4.82963  0.474 33.69498 ? 103 TYR A OH  1 
ATOM   867  O OH  B TYR A 1 103 ? -4.78433  -10.78356 3.09464  0.526 13.03021 ? 103 TYR A OH  1 
ATOM   868  N N   . ALA A 1 104 ? -2.68563  -4.39549  0.33416  1.000 18.95701 ? 104 ALA A N   1 
ATOM   869  C CA  . ALA A 1 104 ? -1.43007  -4.80038  -0.28944 1.000 21.15126 ? 104 ALA A CA  1 
ATOM   870  C C   . ALA A 1 104 ? -0.54661  -5.63739  0.60979  1.000 30.22369 ? 104 ALA A C   1 
ATOM   871  O O   . ALA A 1 104 ? 0.30047   -6.38325  0.10159  1.000 31.95458 ? 104 ALA A O   1 
ATOM   872  C CB  . ALA A 1 104 ? -0.62661  -3.57458  -0.72976 1.000 23.34144 ? 104 ALA A CB  1 
ATOM   873  N N   . ALA A 1 105 ? -0.73203  -5.53525  1.91969  1.000 25.63981 ? 105 ALA A N   1 
ATOM   874  C CA  . ALA A 1 105 ? 0.03304   -6.29678  2.89148  1.000 16.53761 ? 105 ALA A CA  1 
ATOM   875  C C   . ALA A 1 105 ? -0.83706  -6.46402  4.12357  1.000 19.56542 ? 105 ALA A C   1 
ATOM   876  O O   . ALA A 1 105 ? -1.79668  -5.72049  4.33156  1.000 26.08407 ? 105 ALA A O   1 
ATOM   877  C CB  . ALA A 1 105 ? 1.36874   -5.62892  3.23057  1.000 25.39961 ? 105 ALA A CB  1 
ATOM   878  N N   . LYS A 1 106 ? -0.49643  -7.45338  4.93658  1.000 15.01547 ? 106 LYS A N   1 
ATOM   879  C CA  . LYS A 1 106 ? -1.20242  -7.69483  6.18623  1.000 23.02415 ? 106 LYS A CA  1 
ATOM   880  C C   . LYS A 1 106 ? -0.27255  -8.35078  7.18694  1.000 23.27638 ? 106 LYS A C   1 
ATOM   881  O O   . LYS A 1 106 ? 0.55919   -9.17993  6.81801  1.000 18.84342 ? 106 LYS A O   1 
ATOM   882  C CB  . LYS A 1 106 ? -2.44419  -8.56614  5.90953  1.000 29.09882 ? 106 LYS A CB  1 
ATOM   883  C CG  . LYS A 1 106 ? -3.29667  -8.93801  7.11992  1.000 43.35753 ? 106 LYS A CG  1 
ATOM   884  C CD  . LYS A 1 106 ? -4.70156  -9.39921  6.70218  1.000 31.42170 ? 106 LYS A CD  1 
ATOM   885  C CE  . LYS A 1 106 ? -5.55336  -9.75150  7.91657  1.000 38.30047 ? 106 LYS A CE  1 
ATOM   886  N NZ  . LYS A 1 106 ? -4.67246  -10.25141 9.03341  1.000 32.49496 ? 106 LYS A NZ  1 
ATOM   887  N N   . THR A 1 107 ? -0.43409  -7.99894  8.45576  1.000 26.63396 ? 107 THR A N   1 
ATOM   888  C CA  . THR A 1 107 ? 0.43200   -8.56446  9.47129  1.000 20.71237 ? 107 THR A CA  1 
ATOM   889  C C   . THR A 1 107 ? -0.41398  -9.51721  10.30559 1.000 36.69414 ? 107 THR A C   1 
ATOM   890  O O   . THR A 1 107 ? -1.63014  -9.62838  10.11119 1.000 38.59732 ? 107 THR A O   1 
ATOM   891  C CB  . THR A 1 107 ? 1.04281   -7.44707  10.32587 1.000 28.78766 ? 107 THR A CB  1 
ATOM   892  O OG1 . THR A 1 107 ? 0.00232   -6.59547  10.80945 1.000 22.57336 ? 107 THR A OG1 1 
ATOM   893  C CG2 . THR A 1 107 ? 1.97298   -6.56825  9.48331  1.000 24.02278 ? 107 THR A CG2 1 
ATOM   894  N N   . ASP A 1 108 ? 0.22256   -10.21408 11.24284 1.000 30.19051 ? 108 ASP A N   1 
ATOM   895  C CA  . ASP A 1 108 ? -0.49637  -11.17338 12.07064 1.000 24.08161 ? 108 ASP A CA  1 
ATOM   896  C C   . ASP A 1 108 ? -0.70819  -10.73322 13.50679 1.000 20.38133 ? 108 ASP A C   1 
ATOM   897  O O   . ASP A 1 108 ? -1.22475  -11.52120 14.30492 1.000 38.66043 ? 108 ASP A O   1 
ATOM   898  C CB  . ASP A 1 108 ? 0.27313   -12.48517 12.05876 1.000 26.69230 ? 108 ASP A CB  1 
ATOM   899  C CG  . ASP A 1 108 ? 0.53394   -12.96755 10.65439 1.000 47.44163 ? 108 ASP A CG  1 
ATOM   900  O OD1 . ASP A 1 108 ? -0.43627  -13.04270 9.87356  1.000 41.82483 ? 108 ASP A OD1 1 
ATOM   901  O OD2 . ASP A 1 108 ? 1.70701   -13.24428 10.32026 1.000 48.14763 ? 108 ASP A OD2 1 
ATOM   902  N N   . GLY A 1 109 ? -0.39964  -9.50537  13.85037 1.000 18.68630 ? 109 GLY A N   1 
ATOM   903  C CA  . GLY A 1 109 ? -0.71344  -9.01664  15.17262 1.000 17.00607 ? 109 GLY A CA  1 
ATOM   904  C C   . GLY A 1 109 ? 0.24995   -7.91966  15.58530 1.000 21.06455 ? 109 GLY A C   1 
ATOM   905  O O   . GLY A 1 109 ? 1.02741   -7.40454  14.78471 1.000 21.49556 ? 109 GLY A O   1 
ATOM   906  N N   . VAL A 1 110 ? 0.22862   -7.62624  16.87919 1.000 17.21141 ? 110 VAL A N   1 
ATOM   907  C CA  . VAL A 1 110 ? 1.00917   -6.54620  17.46796 1.000 23.81777 ? 110 VAL A CA  1 
ATOM   908  C C   . VAL A 1 110 ? 1.45061   -6.98808  18.83782 1.000 18.58579 ? 110 VAL A C   1 
ATOM   909  O O   . VAL A 1 110 ? 0.62596   -7.42808  19.64424 1.000 25.40078 ? 110 VAL A O   1 
ATOM   910  C CB  . VAL A 1 110 ? 0.18950   -5.24640  17.64792 1.000 20.52858 ? 110 VAL A CB  1 
ATOM   911  C CG1 . VAL A 1 110 ? 1.10366   -4.06097  17.92795 1.000 18.13175 ? 110 VAL A CG1 1 
ATOM   912  C CG2 . VAL A 1 110 ? -0.71170  -4.97902  16.47501 1.000 35.09276 ? 110 VAL A CG2 1 
ATOM   913  N N   A ARG A 1 111 ? 2.74299   -6.85407  19.10943 0.523 19.51523 ? 111 ARG A N   1 
ATOM   914  N N   B ARG A 1 111 ? 2.73302   -6.84454  19.12986 0.477 19.54774 ? 111 ARG A N   1 
ATOM   915  C CA  A ARG A 1 111 ? 3.31217   -7.12528  20.41973 0.523 21.91063 ? 111 ARG A CA  1 
ATOM   916  C CA  B ARG A 1 111 ? 3.22306   -7.12816  20.46788 0.477 21.83610 ? 111 ARG A CA  1 
ATOM   917  C C   A ARG A 1 111 ? 3.85648   -5.82251  20.98696 0.523 21.07037 ? 111 ARG A C   1 
ATOM   918  C C   B ARG A 1 111 ? 3.94201   -5.90371  21.00933 0.477 21.14837 ? 111 ARG A C   1 
ATOM   919  O O   A ARG A 1 111 ? 4.33169   -4.96362  20.23854 0.523 23.14060 ? 111 ARG A O   1 
ATOM   920  O O   B ARG A 1 111 ? 4.60601   -5.17821  20.26376 0.477 23.96392 ? 111 ARG A O   1 
ATOM   921  C CB  A ARG A 1 111 ? 4.42058   -8.19232  20.32960 0.523 23.05790 ? 111 ARG A CB  1 
ATOM   922  C CB  B ARG A 1 111 ? 4.12646   -8.36841  20.48004 0.477 24.56497 ? 111 ARG A CB  1 
ATOM   923  C CG  A ARG A 1 111 ? 3.90479   -9.63084  20.12809 0.523 23.38947 ? 111 ARG A CG  1 
ATOM   924  C CG  B ARG A 1 111 ? 3.45571   -9.56594  21.17455 0.477 22.56981 ? 111 ARG A CG  1 
ATOM   925  C CD  A ARG A 1 111 ? 5.04807   -10.66389 20.20176 0.523 30.11380 ? 111 ARG A CD  1 
ATOM   926  C CD  B ARG A 1 111 ? 3.64745   -10.89297 20.43350 0.477 26.29975 ? 111 ARG A CD  1 
ATOM   927  N NE  A ARG A 1 111 ? 4.74552   -11.91742 19.51150 0.523 24.70393 ? 111 ARG A NE  1 
ATOM   928  N NE  B ARG A 1 111 ? 2.58684   -11.16136 19.46625 0.477 33.04059 ? 111 ARG A NE  1 
ATOM   929  C CZ  A ARG A 1 111 ? 5.45522   -12.41914 18.50502 0.523 26.55215 ? 111 ARG A CZ  1 
ATOM   930  C CZ  B ARG A 1 111 ? 1.30275   -11.32269 19.76382 0.477 23.84393 ? 111 ARG A CZ  1 
ATOM   931  N NH1 A ARG A 1 111 ? 6.50409   -11.78105 18.00701 0.523 26.13252 ? 111 ARG A NH1 1 
ATOM   932  N NH1 B ARG A 1 111 ? 0.86803   -11.29591 21.01600 0.477 29.54376 ? 111 ARG A NH1 1 
ATOM   933  N NH2 A ARG A 1 111 ? 5.10801   -13.59428 17.98828 0.523 24.42853 ? 111 ARG A NH2 1 
ATOM   934  N NH2 B ARG A 1 111 ? 0.43138   -11.51299 18.77970 0.477 21.03132 ? 111 ARG A NH2 1 
ATOM   935  N N   . GLN A 1 112 ? 3.76599   -5.66351  22.30238 1.000 21.50495 ? 112 GLN A N   1 
ATOM   936  C CA  . GLN A 1 112 ? 4.33927   -4.51282  22.99645 1.000 18.00297 ? 112 GLN A CA  1 
ATOM   937  C C   . GLN A 1 112 ? 5.67831   -4.89039  23.58997 1.000 16.91718 ? 112 GLN A C   1 
ATOM   938  O O   . GLN A 1 112 ? 5.84424   -6.00152  24.09638 1.000 24.43691 ? 112 GLN A O   1 
ATOM   939  C CB  . GLN A 1 112 ? 3.44148   -3.97670  24.11703 1.000 20.05617 ? 112 GLN A CB  1 
ATOM   940  C CG  . GLN A 1 112 ? 3.95016   -2.63393  24.69920 1.000 23.64553 ? 112 GLN A CG  1 
ATOM   941  C CD  . GLN A 1 112 ? 3.08806   -2.06353  25.80681 1.000 33.07089 ? 112 GLN A CD  1 
ATOM   942  O OE1 . GLN A 1 112 ? 2.06322   -2.63854  26.17720 1.000 36.18795 ? 112 GLN A OE1 1 
ATOM   943  N NE2 . GLN A 1 112 ? 3.52063   -0.93389  26.36777 1.000 26.88289 ? 112 GLN A NE2 1 
ATOM   944  N N   . VAL A 1 113 ? 6.63597   -3.97319  23.54085 1.000 18.66984 ? 113 VAL A N   1 
ATOM   945  C CA  . VAL A 1 113 ? 7.88010   -4.28156  24.22227 1.000 15.72780 ? 113 VAL A CA  1 
ATOM   946  C C   . VAL A 1 113 ? 7.63289   -3.97902  25.69447 1.000 20.74277 ? 113 VAL A C   1 
ATOM   947  O O   . VAL A 1 113 ? 6.90447   -3.03061  26.01639 1.000 16.69393 ? 113 VAL A O   1 
ATOM   948  C CB  . VAL A 1 113 ? 8.98008   -3.35184  23.67443 1.000 10.84776 ? 113 VAL A CB  1 
ATOM   949  C CG1 . VAL A 1 113 ? 10.27988  -3.52179  24.42339 1.000 18.84020 ? 113 VAL A CG1 1 
ATOM   950  C CG2 . VAL A 1 113 ? 9.13038   -3.47273  22.16362 1.000 14.06010 ? 113 VAL A CG2 1 
ATOM   951  N N   . GLN A 1 114 ? 8.20773   -4.77625  26.60124 1.000 12.56731 ? 114 GLN A N   1 
ATOM   952  C CA  . GLN A 1 114 ? 8.08717   -4.45252  28.01923 1.000 16.21671 ? 114 GLN A CA  1 
ATOM   953  C C   . GLN A 1 114 ? 8.56145   -3.01365  28.22577 1.000 28.06996 ? 114 GLN A C   1 
ATOM   954  O O   . GLN A 1 114 ? 9.70395   -2.69083  27.86061 1.000 12.87276 ? 114 GLN A O   1 
ATOM   955  C CB  . GLN A 1 114 ? 8.82769   -5.43894  28.92414 1.000 28.91973 ? 114 GLN A CB  1 
ATOM   956  C CG  . GLN A 1 114 ? 9.03270   -4.92426  30.36873 1.000 34.98904 ? 114 GLN A CG  1 
ATOM   957  C CD  . GLN A 1 114 ? 10.14303  -5.66347  31.10665 1.000 52.11496 ? 114 GLN A CD  1 
ATOM   958  O OE1 . GLN A 1 114 ? 10.34384  -5.47294  32.30719 1.000 38.48241 ? 114 GLN A OE1 1 
ATOM   959  N NE2 . GLN A 1 114 ? 10.84216  -6.54471  30.39409 1.000 51.73815 ? 114 GLN A NE2 1 
ATOM   960  N N   . PRO A 1 115 ? 7.76766   -2.14545  28.83943 1.000 17.53215 ? 115 PRO A N   1 
ATOM   961  C CA  . PRO A 1 115 ? 8.17701   -0.74418  28.90775 1.000 13.92927 ? 115 PRO A CA  1 
ATOM   962  C C   . PRO A 1 115 ? 9.24813   -0.53693  29.95832 1.000 16.77390 ? 115 PRO A C   1 
ATOM   963  O O   . PRO A 1 115 ? 9.48093   -1.36599  30.83991 1.000 30.98478 ? 115 PRO A O   1 
ATOM   964  C CB  . PRO A 1 115 ? 6.90077   0.01596   29.30335 1.000 12.26405 ? 115 PRO A CB  1 
ATOM   965  C CG  . PRO A 1 115 ? 5.95259   -1.00986  29.77893 1.000 19.80773 ? 115 PRO A CG  1 
ATOM   966  C CD  . PRO A 1 115 ? 6.37259   -2.35474  29.24680 1.000 20.63939 ? 115 PRO A CD  1 
ATOM   967  N N   . TYR A 1 116 ? 9.90546   0.60538   29.82339 1.000 17.99145 ? 116 TYR A N   1 
ATOM   968  C CA  . TYR A 1 116 ? 10.92104  1.05564   30.76263 1.000 31.44792 ? 116 TYR A CA  1 
ATOM   969  C C   . TYR A 1 116 ? 12.05236  0.03971   30.90410 1.000 23.72031 ? 116 TYR A C   1 
ATOM   970  O O   . TYR A 1 116 ? 12.64165  -0.11417  31.97373 1.000 38.37700 ? 116 TYR A O   1 
ATOM   971  C CB  . TYR A 1 116 ? 10.25448  1.32927   32.10958 1.000 13.53402 ? 116 TYR A CB  1 
ATOM   972  C CG  . TYR A 1 116 ? 9.07879   2.26792   31.95401 1.000 22.33230 ? 116 TYR A CG  1 
ATOM   973  C CD1 . TYR A 1 116 ? 9.23081   3.51817   31.36295 1.000 20.67207 ? 116 TYR A CD1 1 
ATOM   974  C CD2 . TYR A 1 116 ? 7.81958   1.91997   32.44256 1.000 32.93630 ? 116 TYR A CD2 1 
ATOM   975  C CE1 . TYR A 1 116 ? 8.14537   4.38999   31.23683 1.000 33.04240 ? 116 TYR A CE1 1 
ATOM   976  C CE2 . TYR A 1 116 ? 6.73015   2.78339   32.32468 1.000 37.56874 ? 116 TYR A CE2 1 
ATOM   977  C CZ  . TYR A 1 116 ? 6.90030   4.01928   31.72502 1.000 37.63434 ? 116 TYR A CZ  1 
ATOM   978  O OH  . TYR A 1 116 ? 5.82989   4.87931   31.60142 1.000 42.07770 ? 116 TYR A OH  1 
ATOM   979  N N   . ASN A 1 117 ? 12.41299  -0.60248  29.79490 1.000 18.51075 ? 117 ASN A N   1 
ATOM   980  C CA  . ASN A 1 117 ? 13.40279  -1.68019  29.79965 1.000 22.40999 ? 117 ASN A CA  1 
ATOM   981  C C   . ASN A 1 117 ? 14.22675  -1.52375  28.52876 1.000 20.36428 ? 117 ASN A C   1 
ATOM   982  O O   . ASN A 1 117 ? 13.75443  -1.87485  27.44473 1.000 16.41104 ? 117 ASN A O   1 
ATOM   983  C CB  . ASN A 1 117 ? 12.69765  -3.03905  29.84856 1.000 20.95164 ? 117 ASN A CB  1 
ATOM   984  C CG  . ASN A 1 117 ? 13.64773  -4.21527  29.96600 1.000 14.50155 ? 117 ASN A CG  1 
ATOM   985  O OD1 . ASN A 1 117 ? 14.68256  -4.28296  29.29840 1.000 18.24419 ? 117 ASN A OD1 1 
ATOM   986  N ND2 . ASN A 1 117 ? 13.27613  -5.17457  30.79092 1.000 23.39802 ? 117 ASN A ND2 1 
ATOM   987  N N   . GLU A 1 118 ? 15.45660  -1.01820  28.66789 1.000 10.35736 ? 118 GLU A N   1 
ATOM   988  C CA  . GLU A 1 118 ? 16.26338  -0.70584  27.49227 1.000 21.27286 ? 118 GLU A CA  1 
ATOM   989  C C   . GLU A 1 118 ? 16.57544  -1.95917  26.68337 1.000 22.65590 ? 118 GLU A C   1 
ATOM   990  O O   . GLU A 1 118 ? 16.40075  -1.98751  25.45886 1.000 18.31829 ? 118 GLU A O   1 
ATOM   991  C CB  . GLU A 1 118 ? 17.55550  -0.00966  27.91517 1.000 22.04576 ? 118 GLU A CB  1 
ATOM   992  C CG  . GLU A 1 118 ? 18.44618  0.34878   26.72749 1.000 22.38948 ? 118 GLU A CG  1 
ATOM   993  C CD  . GLU A 1 118 ? 19.66680  1.17726   27.13131 1.000 29.87024 ? 118 GLU A CD  1 
ATOM   994  O OE1 . GLU A 1 118 ? 19.48454  2.27481   27.71311 1.000 32.65840 ? 118 GLU A OE1 1 
ATOM   995  O OE2 . GLU A 1 118 ? 20.80505  0.74799   26.84566 1.000 22.48541 ? 118 GLU A OE2 1 
ATOM   996  N N   . GLY A 1 119 ? 17.05684  -2.99676  27.36447 1.000 17.12879 ? 119 GLY A N   1 
ATOM   997  C CA  . GLY A 1 119 ? 17.36386  -4.26380  26.72385 1.000 15.57765 ? 119 GLY A CA  1 
ATOM   998  C C   . GLY A 1 119 ? 16.24448  -4.80858  25.86312 1.000 14.00597 ? 119 GLY A C   1 
ATOM   999  O O   . GLY A 1 119 ? 16.46330  -5.20764  24.71815 1.000 14.93469 ? 119 GLY A O   1 
ATOM   1000 N N   . ALA A 1 120 ? 15.03153  -4.87059  26.41858 1.000 9.23022  ? 120 ALA A N   1 
ATOM   1001 C CA  . ALA A 1 120 ? 13.90266  -5.41395  25.66752 1.000 18.95101 ? 120 ALA A CA  1 
ATOM   1002 C C   . ALA A 1 120 ? 13.61206  -4.60711  24.40822 1.000 15.35351 ? 120 ALA A C   1 
ATOM   1003 O O   . ALA A 1 120 ? 13.28411  -5.17956  23.36265 1.000 18.11575 ? 120 ALA A O   1 
ATOM   1004 C CB  . ALA A 1 120 ? 12.66334  -5.45721  26.55951 1.000 13.06495 ? 120 ALA A CB  1 
ATOM   1005 N N   . LEU A 1 121 ? 13.74441  -3.28378  24.47987 1.000 18.60767 ? 121 LEU A N   1 
ATOM   1006 C CA  . LEU A 1 121 ? 13.62435  -2.47060  23.27574 1.000 19.45560 ? 121 LEU A CA  1 
ATOM   1007 C C   . LEU A 1 121 ? 14.69857  -2.88244  22.27870 1.000 19.15412 ? 121 LEU A C   1 
ATOM   1008 O O   . LEU A 1 121 ? 14.41467  -3.11570  21.09874 1.000 26.21878 ? 121 LEU A O   1 
ATOM   1009 C CB  . LEU A 1 121 ? 13.72647  -0.97874  23.60828 1.000 17.53640 ? 121 LEU A CB  1 
ATOM   1010 C CG  . LEU A 1 121 ? 13.63413  -0.12145  22.34416 1.000 10.32707 ? 121 LEU A CG  1 
ATOM   1011 C CD1 . LEU A 1 121 ? 12.35793  -0.53428  21.55084 1.000 10.72795 ? 121 LEU A CD1 1 
ATOM   1012 C CD2 . LEU A 1 121 ? 13.61849  1.34292   22.65180 1.000 14.56196 ? 121 LEU A CD2 1 
ATOM   1013 N N   . LEU A 1 122 ? 15.94434  -3.01070  22.75375 1.000 15.45094 ? 122 LEU A N   1 
ATOM   1014 C CA  . LEU A 1 122 ? 17.05458  -3.32916  21.86769 1.000 18.28084 ? 122 LEU A CA  1 
ATOM   1015 C C   . LEU A 1 122 ? 16.86977  -4.70904  21.26712 1.000 24.38104 ? 122 LEU A C   1 
ATOM   1016 O O   . LEU A 1 122 ? 17.23682  -4.93826  20.10778 1.000 19.53181 ? 122 LEU A O   1 
ATOM   1017 C CB  . LEU A 1 122 ? 18.39156  -3.27191  22.60886 1.000 14.25527 ? 122 LEU A CB  1 
ATOM   1018 C CG  . LEU A 1 122 ? 18.81503  -1.91210  23.19076 1.000 20.86165 ? 122 LEU A CG  1 
ATOM   1019 C CD1 . LEU A 1 122 ? 20.04839  -2.12465  24.04297 1.000 6.95533  ? 122 LEU A CD1 1 
ATOM   1020 C CD2 . LEU A 1 122 ? 19.02336  -0.81395  22.14717 1.000 18.71055 ? 122 LEU A CD2 1 
ATOM   1021 N N   . TYR A 1 123 ? 16.27387  -5.63204  22.01726 1.000 14.87816 ? 123 TYR A N   1 
ATOM   1022 C CA  . TYR A 1 123 ? 16.05866  -6.95221  21.44567 1.000 20.97543 ? 123 TYR A CA  1 
ATOM   1023 C C   . TYR A 1 123 ? 15.00532  -6.91884  20.34430 1.000 13.14847 ? 123 TYR A C   1 
ATOM   1024 O O   . TYR A 1 123 ? 15.20242  -7.51766  19.28522 1.000 19.23634 ? 123 TYR A O   1 
ATOM   1025 C CB  . TYR A 1 123 ? 15.69195  -7.92264  22.58228 1.000 23.31778 ? 123 TYR A CB  1 
ATOM   1026 C CG  . TYR A 1 123 ? 15.34942  -9.31197  22.11952 1.000 33.18129 ? 123 TYR A CG  1 
ATOM   1027 C CD1 . TYR A 1 123 ? 14.04018  -9.59589  21.71398 1.000 22.19822 ? 123 TYR A CD1 1 
ATOM   1028 C CD2 . TYR A 1 123 ? 16.32998  -10.26890 21.88291 1.000 23.83805 ? 123 TYR A CD2 1 
ATOM   1029 C CE1 . TYR A 1 123 ? 13.68059  -10.83249 21.22584 1.000 29.79590 ? 123 TYR A CE1 1 
ATOM   1030 C CE2 . TYR A 1 123 ? 15.97749  -11.53968 21.37568 1.000 37.67089 ? 123 TYR A CE2 1 
ATOM   1031 C CZ  . TYR A 1 123 ? 14.65088  -11.80853 21.04978 1.000 37.37097 ? 123 TYR A CZ  1 
ATOM   1032 O OH  . TYR A 1 123 ? 14.28137  -13.04246 20.55287 1.000 46.00211 ? 123 TYR A OH  1 
ATOM   1033 N N   . SER A 1 124 ? 13.95949  -6.12172  20.50693 1.000 10.63761 ? 124 SER A N   1 
ATOM   1034 C CA  . SER A 1 124 ? 12.99657  -5.95165  19.42593 1.000 21.96908 ? 124 SER A CA  1 
ATOM   1035 C C   . SER A 1 124 ? 13.66792  -5.35689  18.18415 1.000 11.23141 ? 124 SER A C   1 
ATOM   1036 O O   . SER A 1 124 ? 13.54325  -5.89868  17.08425 1.000 17.04302 ? 124 SER A O   1 
ATOM   1037 C CB  . SER A 1 124 ? 11.81551  -5.13412  19.91177 1.000 9.91600  ? 124 SER A CB  1 
ATOM   1038 O OG  . SER A 1 124 ? 11.21010  -5.80051  21.00751 1.000 33.99044 ? 124 SER A OG  1 
ATOM   1039 N N   . ILE A 1 125 ? 14.31007  -4.18764  18.33139 1.000 11.78111 ? 125 ILE A N   1 
ATOM   1040 C CA  . ILE A 1 125 ? 14.99410  -3.54063  17.20409 1.000 12.80823 ? 125 ILE A CA  1 
ATOM   1041 C C   . ILE A 1 125 ? 15.92998  -4.50739  16.48900 1.000 10.07867 ? 125 ILE A C   1 
ATOM   1042 O O   . ILE A 1 125 ? 16.03480  -4.49574  15.25592 1.000 20.21658 ? 125 ILE A O   1 
ATOM   1043 C CB  . ILE A 1 125 ? 15.78840  -2.29995  17.68214 1.000 15.74717 ? 125 ILE A CB  1 
ATOM   1044 C CG1 . ILE A 1 125 ? 14.93851  -1.30439  18.48064 1.000 15.17740 ? 125 ILE A CG1 1 
ATOM   1045 C CG2 . ILE A 1 125 ? 16.61669  -1.69050  16.51128 1.000 14.57242 ? 125 ILE A CG2 1 
ATOM   1046 C CD1 . ILE A 1 125 ? 15.77413  -0.13864  19.08732 1.000 12.62766 ? 125 ILE A CD1 1 
ATOM   1047 N N   . ALA A 1 126 ? 16.61305  -5.36916  17.23914 1.000 8.17156  ? 126 ALA A N   1 
ATOM   1048 C CA  . ALA A 1 126 ? 17.49723  -6.33202  16.59409 1.000 17.02854 ? 126 ALA A CA  1 
ATOM   1049 C C   . ALA A 1 126 ? 16.74911  -7.24661  15.64139 1.000 15.90453 ? 126 ALA A C   1 
ATOM   1050 O O   . ALA A 1 126 ? 17.35374  -7.79134  14.71407 1.000 22.21935 ? 126 ALA A O   1 
ATOM   1051 C CB  . ALA A 1 126 ? 18.22569  -7.15923  17.65180 1.000 17.93502 ? 126 ALA A CB  1 
ATOM   1052 N N   . ASN A 1 127 ? 15.43799  -7.36931  15.82142 1.000 16.81622 ? 127 ASN A N   1 
ATOM   1053 C CA  . ASN A 1 127 ? 14.55594  -8.25671  15.07641 1.000 24.07903 ? 127 ASN A CA  1 
ATOM   1054 C C   . ASN A 1 127 ? 13.80037  -7.52143  13.99553 1.000 25.97656 ? 127 ASN A C   1 
ATOM   1055 O O   . ASN A 1 127 ? 13.47845  -8.12703  12.96805 1.000 37.31084 ? 127 ASN A O   1 
ATOM   1056 C CB  . ASN A 1 127 ? 13.55475  -8.94994  16.00255 1.000 25.46885 ? 127 ASN A CB  1 
ATOM   1057 C CG  . ASN A 1 127 ? 14.19474  -10.05134 16.81288 1.000 37.07379 ? 127 ASN A CG  1 
ATOM   1058 O OD1 . ASN A 1 127 ? 14.74305  -9.81904  17.89286 1.000 39.65883 ? 127 ASN A OD1 1 
ATOM   1059 N ND2 . ASN A 1 127 ? 14.15514  -11.26570 16.27686 1.000 54.16355 ? 127 ASN A ND2 1 
ATOM   1060 N N   . GLN A 1 128 ? 13.48981  -6.23452  14.21943 1.000 18.92444 ? 128 GLN A N   1 
ATOM   1061 C CA  . GLN A 1 128 ? 12.76095  -5.43791  13.24904 1.000 17.65896 ? 128 GLN A CA  1 
ATOM   1062 C C   . GLN A 1 128 ? 12.61410  -3.99631  13.70607 1.000 15.84542 ? 128 GLN A C   1 
ATOM   1063 O O   . GLN A 1 128 ? 12.87648  -3.68986  14.87350 1.000 20.24304 ? 128 GLN A O   1 
ATOM   1064 C CB  . GLN A 1 128 ? 11.38065  -6.04745  13.09265 1.000 9.40321  ? 128 GLN A CB  1 
ATOM   1065 C CG  . GLN A 1 128 ? 10.68734  -5.95076  14.39853 1.000 20.06401 ? 128 GLN A CG  1 
ATOM   1066 C CD  . GLN A 1 128 ? 9.44241   -6.73035  14.42605 1.000 18.10354 ? 128 GLN A CD  1 
ATOM   1067 O OE1 . GLN A 1 128 ? 9.40301   -7.82282  14.98901 1.000 25.76446 ? 128 GLN A OE1 1 
ATOM   1068 N NE2 . GLN A 1 128 ? 8.38742   -6.18050  13.83759 1.000 20.49942 ? 128 GLN A NE2 1 
ATOM   1069 N N   . PRO A 1 129 ? 12.19877  -3.08395  12.82570 1.000 17.51615 ? 129 PRO A N   1 
ATOM   1070 C CA  . PRO A 1 129 ? 11.94879  -1.70776  13.26659 1.000 20.10154 ? 129 PRO A CA  1 
ATOM   1071 C C   . PRO A 1 129 ? 10.79688  -1.69868  14.26272 1.000 11.40875 ? 129 PRO A C   1 
ATOM   1072 O O   . PRO A 1 129 ? 9.84290   -2.46970  14.15682 1.000 13.48478 ? 129 PRO A O   1 
ATOM   1073 C CB  . PRO A 1 129 ? 11.62720  -0.96580  11.96354 1.000 16.04136 ? 129 PRO A CB  1 
ATOM   1074 C CG  . PRO A 1 129 ? 12.41802  -1.78173  10.91613 1.000 15.41560 ? 129 PRO A CG  1 
ATOM   1075 C CD  . PRO A 1 129 ? 12.23893  -3.19247  11.35390 1.000 20.49312 ? 129 PRO A CD  1 
ATOM   1076 N N   . VAL A 1 130 ? 10.87073  -0.79501  15.22696 1.000 11.88754 ? 130 VAL A N   1 
ATOM   1077 C CA  . VAL A 1 130 ? 9.88457   -0.78089  16.29620 1.000 14.77658 ? 130 VAL A CA  1 
ATOM   1078 C C   . VAL A 1 130 ? 9.30972   0.61226   16.37962 1.000 10.76523 ? 130 VAL A C   1 
ATOM   1079 O O   . VAL A 1 130 ? 10.01114  1.61478   16.20511 1.000 14.65588 ? 130 VAL A O   1 
ATOM   1080 C CB  . VAL A 1 130 ? 10.54008  -1.19983  17.65033 1.000 15.02287 ? 130 VAL A CB  1 
ATOM   1081 C CG1 . VAL A 1 130 ? 9.61403   -1.05052  18.84042 1.000 13.08306 ? 130 VAL A CG1 1 
ATOM   1082 C CG2 . VAL A 1 130 ? 11.05697  -2.62839  17.57765 1.000 13.72098 ? 130 VAL A CG2 1 
ATOM   1083 N N   . SER A 1 131 ? 8.04609   0.67534   16.75481 1.000 11.73682 ? 131 SER A N   1 
ATOM   1084 C CA  . SER A 1 131 ? 7.40081   1.95846   16.94670 1.000 15.89196 ? 131 SER A CA  1 
ATOM   1085 C C   . SER A 1 131 ? 7.61136   2.37043   18.38840 1.000 14.34694 ? 131 SER A C   1 
ATOM   1086 O O   . SER A 1 131 ? 7.32923   1.60192   19.30753 1.000 19.32468 ? 131 SER A O   1 
ATOM   1087 C CB  . SER A 1 131 ? 5.91006   1.84659   16.63902 1.000 14.73489 ? 131 SER A CB  1 
ATOM   1088 O OG  . SER A 1 131 ? 5.25037   3.06742   16.90195 1.000 15.91043 ? 131 SER A OG  1 
ATOM   1089 N N   . VAL A 1 132 ? 8.08893   3.59109   18.57595 1.000 15.39543 ? 132 VAL A N   1 
ATOM   1090 C CA  . VAL A 1 132 ? 8.38733   4.12588   19.89430 1.000 20.78840 ? 132 VAL A CA  1 
ATOM   1091 C C   . VAL A 1 132 ? 7.86755   5.54684   19.97538 1.000 13.78372 ? 132 VAL A C   1 
ATOM   1092 O O   . VAL A 1 132 ? 7.64660   6.22022   18.96804 1.000 31.85919 ? 132 VAL A O   1 
ATOM   1093 C CB  . VAL A 1 132 ? 9.89610   4.10860   20.20834 1.000 21.09562 ? 132 VAL A CB  1 
ATOM   1094 C CG1 . VAL A 1 132 ? 10.46739  2.71080   20.01511 1.000 12.44574 ? 132 VAL A CG1 1 
ATOM   1095 C CG2 . VAL A 1 132 ? 10.60739  5.06269   19.24995 1.000 18.92508 ? 132 VAL A CG2 1 
ATOM   1096 N N   . VAL A 1 133 ? 7.70116   6.00342   21.20031 1.000 12.23968 ? 133 VAL A N   1 
ATOM   1097 C CA  . VAL A 1 133 ? 7.25494   7.35220   21.48735 1.000 12.31559 ? 133 VAL A CA  1 
ATOM   1098 C C   . VAL A 1 133 ? 8.35734   8.02313   22.28463 1.000 20.38396 ? 133 VAL A C   1 
ATOM   1099 O O   . VAL A 1 133 ? 9.21093   7.36121   22.88294 1.000 16.71809 ? 133 VAL A O   1 
ATOM   1100 C CB  . VAL A 1 133 ? 5.91319   7.39305   22.23454 1.000 17.32713 ? 133 VAL A CB  1 
ATOM   1101 C CG1 . VAL A 1 133 ? 4.85329   6.66615   21.41436 1.000 19.89739 ? 133 VAL A CG1 1 
ATOM   1102 C CG2 . VAL A 1 133 ? 6.05400   6.78947   23.63688 1.000 19.57275 ? 133 VAL A CG2 1 
ATOM   1103 N N   . LEU A 1 134 ? 8.33549   9.35540   22.28732 1.000 15.86272 ? 134 LEU A N   1 
ATOM   1104 C CA  . LEU A 1 134 ? 9.35038   10.11295  23.00382 1.000 17.00798 ? 134 LEU A CA  1 
ATOM   1105 C C   . LEU A 1 134 ? 8.82845   11.52631  23.22522 1.000 19.17930 ? 134 LEU A C   1 
ATOM   1106 O O   . LEU A 1 134 ? 7.73703   11.88338  22.77486 1.000 21.72490 ? 134 LEU A O   1 
ATOM   1107 C CB  . LEU A 1 134 ? 10.67341  10.10432  22.22444 1.000 13.03395 ? 134 LEU A CB  1 
ATOM   1108 C CG  . LEU A 1 134 ? 10.59885  10.47869  20.72814 1.000 17.30560 ? 134 LEU A CG  1 
ATOM   1109 C CD1 . LEU A 1 134 ? 10.15485  11.91180  20.46687 1.000 28.98534 ? 134 LEU A CD1 1 
ATOM   1110 C CD2 . LEU A 1 134 ? 11.88900  10.19658  19.98677 1.000 18.10115 ? 134 LEU A CD2 1 
ATOM   1111 N N   . GLU A 1 135 ? 9.59418   12.30583  23.98195 1.000 18.40116 ? 135 GLU A N   1 
ATOM   1112 C CA  . GLU A 1 135 ? 9.26514   13.70362  24.21976 1.000 16.57940 ? 135 GLU A CA  1 
ATOM   1113 C C   . GLU A 1 135 ? 9.95757   14.55252  23.16873 1.000 17.36763 ? 135 GLU A C   1 
ATOM   1114 O O   . GLU A 1 135 ? 11.18137  14.68776  23.17797 1.000 29.85525 ? 135 GLU A O   1 
ATOM   1115 C CB  . GLU A 1 135 ? 9.67076   14.15874  25.61515 1.000 19.51660 ? 135 GLU A CB  1 
ATOM   1116 C CG  . GLU A 1 135 ? 9.20562   15.59807  25.86477 1.000 33.38546 ? 135 GLU A CG  1 
ATOM   1117 C CD  . GLU A 1 135 ? 9.94854   16.30222  26.99585 1.000 41.85121 ? 135 GLU A CD  1 
ATOM   1118 O OE1 . GLU A 1 135 ? 11.03230  16.87797  26.74218 1.000 33.58065 ? 135 GLU A OE1 1 
ATOM   1119 O OE2 . GLU A 1 135 ? 9.43241   16.29707  28.13791 1.000 52.91538 ? 135 GLU A OE2 1 
ATOM   1120 N N   . ALA A 1 136 ? 9.16471   15.15197  22.28738 1.000 18.87119 ? 136 ALA A N   1 
ATOM   1121 C CA  . ALA A 1 136 ? 9.66598   15.95752  21.19089 1.000 14.98153 ? 136 ALA A CA  1 
ATOM   1122 C C   . ALA A 1 136 ? 9.43239   17.44777  21.37036 1.000 19.48624 ? 136 ALA A C   1 
ATOM   1123 O O   . ALA A 1 136 ? 9.90827   18.22871  20.54316 1.000 32.92921 ? 136 ALA A O   1 
ATOM   1124 C CB  . ALA A 1 136 ? 9.02865   15.50726  19.87307 1.000 29.89320 ? 136 ALA A CB  1 
ATOM   1125 N N   . ALA A 1 137 ? 8.70537   17.86267  22.41005 1.000 29.42844 ? 137 ALA A N   1 
ATOM   1126 C CA  . ALA A 1 137 ? 8.26746   19.24975  22.53286 1.000 36.52068 ? 137 ALA A CA  1 
ATOM   1127 C C   . ALA A 1 137 ? 9.40142   20.21608  22.86887 1.000 27.70139 ? 137 ALA A C   1 
ATOM   1128 O O   . ALA A 1 137 ? 9.26674   21.41494  22.61171 1.000 36.03639 ? 137 ALA A O   1 
ATOM   1129 C CB  . ALA A 1 137 ? 7.18623   19.34870  23.61178 1.000 24.48410 ? 137 ALA A CB  1 
ATOM   1130 N N   . GLY A 1 138 ? 10.51665  19.73156  23.40722 1.000 18.91175 ? 138 GLY A N   1 
ATOM   1131 C CA  . GLY A 1 138 ? 11.61104  20.62276  23.74066 1.000 29.11783 ? 138 GLY A CA  1 
ATOM   1132 C C   . GLY A 1 138 ? 12.25646  21.21902  22.50516 1.000 20.40296 ? 138 GLY A C   1 
ATOM   1133 O O   . GLY A 1 138 ? 12.28465  20.61793  21.43361 1.000 29.01154 ? 138 GLY A O   1 
ATOM   1134 N N   A LYS A 1 139 ? 12.77868  22.43664  22.65530 0.358 29.51243 ? 139 LYS A N   1 
ATOM   1135 N N   B LYS A 1 139 ? 12.77944  22.43499  22.66120 0.642 29.50467 ? 139 LYS A N   1 
ATOM   1136 C CA  A LYS A 1 139 ? 13.47813  23.04604  21.53106 0.358 31.45868 ? 139 LYS A CA  1 
ATOM   1137 C CA  B LYS A 1 139 ? 13.48671  23.06197  21.55124 0.642 31.47705 ? 139 LYS A CA  1 
ATOM   1138 C C   A LYS A 1 139 ? 14.73906  22.27528  21.17692 0.358 30.92292 ? 139 LYS A C   1 
ATOM   1139 C C   B LYS A 1 139 ? 14.72985  22.26921  21.17825 0.642 31.00718 ? 139 LYS A C   1 
ATOM   1140 O O   A LYS A 1 139 ? 15.09423  22.19812  19.99759 0.358 29.45018 ? 139 LYS A O   1 
ATOM   1141 O O   B LYS A 1 139 ? 15.06520  22.16391  19.99509 0.642 29.47534 ? 139 LYS A O   1 
ATOM   1142 C CB  A LYS A 1 139 ? 13.81927  24.50793  21.82061 0.358 29.88657 ? 139 LYS A CB  1 
ATOM   1143 C CB  B LYS A 1 139 ? 13.85030  24.50978  21.88795 0.642 29.74213 ? 139 LYS A CB  1 
ATOM   1144 C CG  A LYS A 1 139 ? 12.61784  25.44315  21.75814 0.358 42.48544 ? 139 LYS A CG  1 
ATOM   1145 C CG  B LYS A 1 139 ? 12.63177  25.40796  22.10384 0.642 42.41635 ? 139 LYS A CG  1 
ATOM   1146 C CD  A LYS A 1 139 ? 11.83229  25.29383  20.44709 0.358 45.86942 ? 139 LYS A CD  1 
ATOM   1147 C CD  B LYS A 1 139 ? 11.76418  25.48766  20.83956 0.642 49.81550 ? 139 LYS A CD  1 
ATOM   1148 C CE  A LYS A 1 139 ? 12.62072  25.76789  19.23184 0.358 52.32632 ? 139 LYS A CE  1 
ATOM   1149 C CE  B LYS A 1 139 ? 10.55372  26.40922  21.03049 0.642 53.25020 ? 139 LYS A CE  1 
ATOM   1150 N NZ  A LYS A 1 139 ? 11.93027  25.43690  17.94921 0.358 30.64613 ? 139 LYS A NZ  1 
ATOM   1151 N NZ  B LYS A 1 139 ? 9.70357   26.47149  19.81189 0.642 44.97142 ? 139 LYS A NZ  1 
ATOM   1152 N N   . ASP A 1 140 ? 15.42142  21.69165  22.16738 1.000 20.32905 ? 140 ASP A N   1 
ATOM   1153 C CA  . ASP A 1 140 ? 16.64954  20.95493  21.86696 1.000 25.48718 ? 140 ASP A CA  1 
ATOM   1154 C C   . ASP A 1 140 ? 16.37447  19.85106  20.85384 1.000 16.97487 ? 140 ASP A C   1 
ATOM   1155 O O   . ASP A 1 140 ? 17.16188  19.63080  19.92808 1.000 15.13397 ? 140 ASP A O   1 
ATOM   1156 C CB  . ASP A 1 140 ? 17.21683  20.37206  23.16050 1.000 21.74039 ? 140 ASP A CB  1 
ATOM   1157 C CG  . ASP A 1 140 ? 17.48507  21.44193  24.19513 1.000 39.06168 ? 140 ASP A CG  1 
ATOM   1158 O OD1 . ASP A 1 140 ? 18.52444  22.12877  24.09697 1.000 37.16732 ? 140 ASP A OD1 1 
ATOM   1159 O OD2 . ASP A 1 140 ? 16.60725  21.65534  25.05942 1.000 34.22615 ? 140 ASP A OD2 1 
ATOM   1160 N N   . PHE A 1 141 ? 15.28676  19.10176  21.06514 1.000 22.62965 ? 141 PHE A N   1 
ATOM   1161 C CA  . PHE A 1 141 ? 14.85827  18.07080  20.12307 1.000 24.93444 ? 141 PHE A CA  1 
ATOM   1162 C C   . PHE A 1 141 ? 14.38496  18.62694  18.77429 1.000 16.19070 ? 141 PHE A C   1 
ATOM   1163 O O   . PHE A 1 141 ? 14.79808  18.15269  17.70987 1.000 25.14958 ? 141 PHE A O   1 
ATOM   1164 C CB  . PHE A 1 141 ? 13.74981  17.23290  20.73988 1.000 15.71909 ? 141 PHE A CB  1 
ATOM   1165 C CG  . PHE A 1 141 ? 13.36522  16.07454  19.88874 1.000 17.10556 ? 141 PHE A CG  1 
ATOM   1166 C CD1 . PHE A 1 141 ? 12.52006  16.23491  18.80537 1.000 16.43781 ? 141 PHE A CD1 1 
ATOM   1167 C CD2 . PHE A 1 141 ? 13.87326  14.81726  20.14908 1.000 26.98935 ? 141 PHE A CD2 1 
ATOM   1168 C CE1 . PHE A 1 141 ? 12.17957  15.14684  18.01363 1.000 22.93865 ? 141 PHE A CE1 1 
ATOM   1169 C CE2 . PHE A 1 141 ? 13.52922  13.72844  19.34343 1.000 15.99432 ? 141 PHE A CE2 1 
ATOM   1170 C CZ  . PHE A 1 141 ? 12.69083  13.89598  18.29336 1.000 13.54345 ? 141 PHE A CZ  1 
ATOM   1171 N N   . GLN A 1 142 ? 13.55071  19.66411  18.80286 1.000 17.37941 ? 142 GLN A N   1 
ATOM   1172 C CA  . GLN A 1 142 ? 13.10410  20.33345  17.57645 1.000 22.95260 ? 142 GLN A CA  1 
ATOM   1173 C C   . GLN A 1 142 ? 14.25648  20.90464  16.75824 1.000 23.71720 ? 142 GLN A C   1 
ATOM   1174 O O   . GLN A 1 142 ? 14.27531  20.79367  15.52788 1.000 17.97869 ? 142 GLN A O   1 
ATOM   1175 C CB  . GLN A 1 142 ? 12.13509  21.43061  17.99718 1.000 23.07088 ? 142 GLN A CB  1 
ATOM   1176 C CG  . GLN A 1 142 ? 10.76847  20.88598  18.37909 1.000 32.19429 ? 142 GLN A CG  1 
ATOM   1177 C CD  . GLN A 1 142 ? 9.81041   21.97821  18.80216 1.000 49.33636 ? 142 GLN A CD  1 
ATOM   1178 O OE1 . GLN A 1 142 ? 9.85095   23.10157  18.29463 1.000 61.07467 ? 142 GLN A OE1 1 
ATOM   1179 N NE2 . GLN A 1 142 ? 8.96279   21.66242  19.78627 1.000 47.70146 ? 142 GLN A NE2 1 
ATOM   1180 N N   . LEU A 1 143 ? 15.26372  21.41376  17.43128 1.000 24.03092 ? 143 LEU A N   1 
ATOM   1181 C CA  . LEU A 1 143 ? 16.42468  22.04501  16.84218 1.000 29.15516 ? 143 LEU A CA  1 
ATOM   1182 C C   . LEU A 1 143 ? 17.57624  21.08151  16.67429 1.000 23.11153 ? 143 LEU A C   1 
ATOM   1183 O O   . LEU A 1 143 ? 18.68392  21.51661  16.34186 1.000 34.78817 ? 143 LEU A O   1 
ATOM   1184 C CB  . LEU A 1 143 ? 16.85906  23.25023  17.67979 1.000 31.52486 ? 143 LEU A CB  1 
ATOM   1185 C CG  . LEU A 1 143 ? 15.79916  24.35790  17.70274 1.000 32.54923 ? 143 LEU A CG  1 
ATOM   1186 C CD1 . LEU A 1 143 ? 16.33066  25.60937  18.38692 1.000 41.38286 ? 143 LEU A CD1 1 
ATOM   1187 C CD2 . LEU A 1 143 ? 15.30638  24.65188  16.30190 1.000 30.77048 ? 143 LEU A CD2 1 
ATOM   1188 N N   . TYR A 1 144 ? 17.33784  19.78800  16.85050 1.000 19.25582 ? 144 TYR A N   1 
ATOM   1189 C CA  . TYR A 1 144 ? 18.42187  18.82882  16.72321 1.000 26.14057 ? 144 TYR A CA  1 
ATOM   1190 C C   . TYR A 1 144 ? 18.93849  18.82084  15.29263 1.000 18.57369 ? 144 TYR A C   1 
ATOM   1191 O O   . TYR A 1 144 ? 18.17626  18.83385  14.32446 1.000 17.77423 ? 144 TYR A O   1 
ATOM   1192 C CB  . TYR A 1 144 ? 17.90363  17.44677  17.11580 1.000 15.35240 ? 144 TYR A CB  1 
ATOM   1193 C CG  . TYR A 1 144 ? 18.81501  16.29554  16.77146 1.000 21.41586 ? 144 TYR A CG  1 
ATOM   1194 C CD1 . TYR A 1 144 ? 19.90089  15.96093  17.57401 1.000 14.69043 ? 144 TYR A CD1 1 
ATOM   1195 C CD2 . TYR A 1 144 ? 18.57306  15.53448  15.62925 1.000 16.97698 ? 144 TYR A CD2 1 
ATOM   1196 C CE1 . TYR A 1 144 ? 20.71388  14.89239  17.25562 1.000 16.77659 ? 144 TYR A CE1 1 
ATOM   1197 C CE2 . TYR A 1 144 ? 19.38185  14.47241  15.29425 1.000 16.30942 ? 144 TYR A CE2 1 
ATOM   1198 C CZ  . TYR A 1 144 ? 20.44431  14.14307  16.11147 1.000 13.88850 ? 144 TYR A CZ  1 
ATOM   1199 O OH  . TYR A 1 144 ? 21.23889  13.07863  15.76335 1.000 16.32403 ? 144 TYR A OH  1 
ATOM   1200 N N   . ARG A 1 145 ? 20.25343  18.84998  15.17391 1.000 19.98792 ? 145 ARG A N   1 
ATOM   1201 C CA  . ARG A 1 145 ? 20.89481  18.89571  13.87692 1.000 33.81360 ? 145 ARG A CA  1 
ATOM   1202 C C   . ARG A 1 145 ? 21.94310  17.81877  13.66841 1.000 26.03308 ? 145 ARG A C   1 
ATOM   1203 O O   . ARG A 1 145 ? 22.51424  17.74775  12.57457 1.000 38.04587 ? 145 ARG A O   1 
ATOM   1204 C CB  . ARG A 1 145 ? 21.55871  20.27687  13.70636 1.000 30.25602 ? 145 ARG A CB  1 
ATOM   1205 C CG  . ARG A 1 145 ? 20.70502  21.31364  12.96836 1.000 49.22245 ? 145 ARG A CG  1 
ATOM   1206 C CD  . ARG A 1 145 ? 20.92952  22.76512  13.46491 1.000 59.91584 ? 145 ARG A CD  1 
ATOM   1207 N NE  . ARG A 1 145 ? 22.31355  23.23740  13.45314 1.000 70.14434 ? 145 ARG A NE  1 
ATOM   1208 C CZ  . ARG A 1 145 ? 23.10426  23.30068  14.51993 1.000 70.16609 ? 145 ARG A CZ  1 
ATOM   1209 N NH1 . ARG A 1 145 ? 22.63305  23.12570  15.74585 1.000 49.63264 ? 145 ARG A NH1 1 
ATOM   1210 N NH2 . ARG A 1 145 ? 24.38110  23.63588  14.36058 1.000 61.76938 ? 145 ARG A NH2 1 
ATOM   1211 N N   . GLY A 1 146 ? 22.18825  16.96655  14.64800 1.000 16.88986 ? 146 GLY A N   1 
ATOM   1212 C CA  . GLY A 1 146 ? 23.08029  15.84440  14.44290 1.000 12.75640 ? 146 GLY A CA  1 
ATOM   1213 C C   . GLY A 1 146 ? 23.76599  15.45735  15.73201 1.000 23.10156 ? 146 GLY A C   1 
ATOM   1214 O O   . GLY A 1 146 ? 23.71822  16.16613  16.73268 1.000 17.79856 ? 146 GLY A O   1 
ATOM   1215 N N   . GLY A 1 147 ? 24.37946  14.28396  15.71182 1.000 27.65623 ? 147 GLY A N   1 
ATOM   1216 C CA  . GLY A 1 147 ? 25.06823  13.82322  16.89224 1.000 19.11389 ? 147 GLY A CA  1 
ATOM   1217 C C   . GLY A 1 147 ? 24.17992  12.94556  17.72971 1.000 18.84174 ? 147 GLY A C   1 
ATOM   1218 O O   . GLY A 1 147 ? 23.00033  12.73488  17.44588 1.000 26.87217 ? 147 GLY A O   1 
ATOM   1219 N N   . ILE A 1 148 ? 24.76502  12.37487  18.76793 1.000 23.44433 ? 148 ILE A N   1 
ATOM   1220 C CA  . ILE A 1 148 ? 23.96503  11.51318  19.61931 1.000 17.65796 ? 148 ILE A CA  1 
ATOM   1221 C C   . ILE A 1 148 ? 23.21775  12.45972  20.54538 1.000 12.06769 ? 148 ILE A C   1 
ATOM   1222 O O   . ILE A 1 148 ? 23.81435  13.23657  21.28840 1.000 20.95743 ? 148 ILE A O   1 
ATOM   1223 C CB  . ILE A 1 148 ? 24.83120  10.51130  20.37787 1.000 27.11805 ? 148 ILE A CB  1 
ATOM   1224 C CG1 . ILE A 1 148 ? 25.53320  9.62986   19.33570 1.000 23.23699 ? 148 ILE A CG1 1 
ATOM   1225 C CG2 . ILE A 1 148 ? 23.95356  9.68117   21.34291 1.000 23.05831 ? 148 ILE A CG2 1 
ATOM   1226 C CD1 . ILE A 1 148 ? 25.89505  8.23080   19.79391 1.000 39.90929 ? 148 ILE A CD1 1 
ATOM   1227 N N   . PHE A 1 149 ? 21.90531  12.39026  20.49477 1.000 27.00973 ? 149 PHE A N   1 
ATOM   1228 C CA  . PHE A 1 149 ? 21.09196  13.30587  21.25362 1.000 20.82193 ? 149 PHE A CA  1 
ATOM   1229 C C   . PHE A 1 149 ? 20.89517  12.79711  22.66610 1.000 20.33429 ? 149 PHE A C   1 
ATOM   1230 O O   . PHE A 1 149 ? 20.59719  11.61904  22.88958 1.000 20.09508 ? 149 PHE A O   1 
ATOM   1231 C CB  . PHE A 1 149 ? 19.75305  13.53708  20.56029 1.000 18.59531 ? 149 PHE A CB  1 
ATOM   1232 C CG  . PHE A 1 149 ? 18.87862  14.51228  21.26645 1.000 26.03644 ? 149 PHE A CG  1 
ATOM   1233 C CD1 . PHE A 1 149 ? 19.05337  15.87202  21.07141 1.000 16.10197 ? 149 PHE A CD1 1 
ATOM   1234 C CD2 . PHE A 1 149 ? 17.84205  14.07443  22.07061 1.000 14.23639 ? 149 PHE A CD2 1 
ATOM   1235 C CE1 . PHE A 1 149 ? 18.26383  16.78156  21.71758 1.000 14.31570 ? 149 PHE A CE1 1 
ATOM   1236 C CE2 . PHE A 1 149 ? 17.03163  14.98964  22.71020 1.000 22.23634 ? 149 PHE A CE2 1 
ATOM   1237 C CZ  . PHE A 1 149 ? 17.24120  16.34528  22.52779 1.000 13.36757 ? 149 PHE A CZ  1 
ATOM   1238 N N   . VAL A 1 150 ? 21.21530  13.67226  23.60475 1.000 10.14344 ? 150 VAL A N   1 
ATOM   1239 C CA  . VAL A 1 150 ? 21.23544  13.39283  25.02334 1.000 32.45094 ? 150 VAL A CA  1 
ATOM   1240 C C   . VAL A 1 150 ? 20.24377  14.26065  25.77751 1.000 26.16218 ? 150 VAL A C   1 
ATOM   1241 O O   . VAL A 1 150 ? 20.14571  14.14759  27.00371 1.000 24.73074 ? 150 VAL A O   1 
ATOM   1242 C CB  . VAL A 1 150 ? 22.66249  13.51420  25.60021 1.000 26.19060 ? 150 VAL A CB  1 
ATOM   1243 C CG1 . VAL A 1 150 ? 22.97300  14.93511  26.06135 1.000 14.15971 ? 150 VAL A CG1 1 
ATOM   1244 C CG2 . VAL A 1 150 ? 22.80892  12.52075  26.75499 1.000 42.48757 ? 150 VAL A CG2 1 
ATOM   1245 N N   . GLY A 1 151 ? 19.44143  15.06264  25.07053 1.000 15.75799 ? 151 GLY A N   1 
ATOM   1246 C CA  . GLY A 1 151 ? 18.58475  16.01930  25.71869 1.000 13.54653 ? 151 GLY A CA  1 
ATOM   1247 C C   . GLY A 1 151 ? 19.19663  17.40883  25.67805 1.000 18.10027 ? 151 GLY A C   1 
ATOM   1248 O O   . GLY A 1 151 ? 20.04842  17.70588  24.82909 1.000 26.07966 ? 151 GLY A O   1 
ATOM   1249 N N   . PRO A 1 152 ? 18.73088  18.31383  26.54287 1.000 14.22217 ? 152 PRO A N   1 
ATOM   1250 C CA  . PRO A 1 152 ? 17.72366  18.08495  27.59094 1.000 21.54269 ? 152 PRO A CA  1 
ATOM   1251 C C   . PRO A 1 152 ? 16.35566  17.78531  27.02886 1.000 21.25991 ? 152 PRO A C   1 
ATOM   1252 O O   . PRO A 1 152 ? 15.97338  18.23539  25.94903 1.000 31.72370 ? 152 PRO A O   1 
ATOM   1253 C CB  . PRO A 1 152 ? 17.71220  19.39982  28.38065 1.000 19.15837 ? 152 PRO A CB  1 
ATOM   1254 C CG  . PRO A 1 152 ? 18.68125  20.34847  27.71658 1.000 26.14489 ? 152 PRO A CG  1 
ATOM   1255 C CD  . PRO A 1 152 ? 19.21904  19.70237  26.48258 1.000 22.26945 ? 152 PRO A CD  1 
ATOM   1256 N N   . CYS A 1 153 ? 15.61482  16.99101  27.78601 1.000 20.05170 ? 153 CYS A N   1 
ATOM   1257 C CA  . CYS A 1 153 ? 14.25063  16.62127  27.45314 1.000 28.72211 ? 153 CYS A CA  1 
ATOM   1258 C C   . CYS A 1 153 ? 13.71614  15.84570  28.63117 1.000 29.10833 ? 153 CYS A C   1 
ATOM   1259 O O   . CYS A 1 153 ? 14.47481  15.18493  29.34631 1.000 32.91030 ? 153 CYS A O   1 
ATOM   1260 C CB  . CYS A 1 153 ? 14.13453  15.75658  26.16586 1.000 28.84612 ? 153 CYS A CB  1 
ATOM   1261 S SG  . CYS A 1 153 ? 15.07424  14.17136  26.08506 1.000 63.80344 ? 153 CYS A SG  1 
ATOM   1262 N N   . GLY A 1 154 ? 12.41028  15.93789  28.82416 1.000 14.84216 ? 154 GLY A N   1 
ATOM   1263 C CA  . GLY A 1 154 ? 11.75102  15.26481  29.91225 1.000 27.38874 ? 154 GLY A CA  1 
ATOM   1264 C C   . GLY A 1 154 ? 11.27660  13.93935  29.36127 1.000 26.36054 ? 154 GLY A C   1 
ATOM   1265 O O   . GLY A 1 154 ? 11.70363  13.49352  28.29511 1.000 25.40945 ? 154 GLY A O   1 
ATOM   1266 N N   A ASN A 1 155 ? 10.38591  13.29678  30.10683 0.421 21.51080 ? 155 ASN A N   1 
ATOM   1267 N N   B ASN A 1 155 ? 10.37572  13.29775  30.10324 0.579 21.46201 ? 155 ASN A N   1 
ATOM   1268 C CA  A ASN A 1 155 ? 9.82464   12.01986  29.69200 0.421 16.64170 ? 155 ASN A CA  1 
ATOM   1269 C CA  B ASN A 1 155 ? 9.82445   12.00916  29.70679 0.579 16.54951 ? 155 ASN A CA  1 
ATOM   1270 C C   A ASN A 1 155 ? 8.31071   12.12000  29.49133 0.421 19.96740 ? 155 ASN A C   1 
ATOM   1271 C C   B ASN A 1 155 ? 8.35347   12.09103  29.30357 0.579 19.67809 ? 155 ASN A C   1 
ATOM   1272 O O   A ASN A 1 155 ? 7.58052   11.15411  29.71788 0.421 29.06496 ? 155 ASN A O   1 
ATOM   1273 O O   B ASN A 1 155 ? 7.69066   11.05551  29.19596 0.579 29.13798 ? 155 ASN A O   1 
ATOM   1274 C CB  A ASN A 1 155 ? 10.19010  10.92197  30.69643 0.421 20.68935 ? 155 ASN A CB  1 
ATOM   1275 C CB  B ASN A 1 155 ? 10.01968  10.98552  30.83381 0.579 20.82364 ? 155 ASN A CB  1 
ATOM   1276 C CG  A ASN A 1 155 ? 11.64860  11.00615  31.16854 0.421 26.09097 ? 155 ASN A CG  1 
ATOM   1277 C CG  B ASN A 1 155 ? 9.47884   11.46825  32.18026 0.579 24.26896 ? 155 ASN A CG  1 
ATOM   1278 O OD1 A ASN A 1 155 ? 11.92790  10.95791  32.36768 0.421 30.81441 ? 155 ASN A OD1 1 
ATOM   1279 O OD1 B ASN A 1 155 ? 8.48710   12.19970  32.24711 0.579 26.65331 ? 155 ASN A OD1 1 
ATOM   1280 N ND2 A ASN A 1 155 ? 12.57852  11.11823  30.22574 0.421 23.12893 ? 155 ASN A ND2 1 
ATOM   1281 N ND2 B ASN A 1 155 ? 10.14126  11.06106  33.26125 0.579 30.92502 ? 155 ASN A ND2 1 
ATOM   1282 N N   . LYS A 1 156 ? 7.82840   13.29374  29.06852 1.000 14.08189 ? 156 LYS A N   1 
ATOM   1283 C CA  . LYS A 1 156 ? 6.42329   13.48483  28.67439 1.000 31.11532 ? 156 LYS A CA  1 
ATOM   1284 C C   . LYS A 1 156 ? 6.21087   13.17999  27.19449 1.000 19.51914 ? 156 LYS A C   1 
ATOM   1285 O O   . LYS A 1 156 ? 6.08078   14.06635  26.34916 1.000 33.59350 ? 156 LYS A O   1 
ATOM   1286 C CB  . LYS A 1 156 ? 5.92996   14.88233  29.00600 1.000 30.35861 ? 156 LYS A CB  1 
ATOM   1287 C CG  . LYS A 1 156 ? 6.31363   15.40886  30.34465 1.000 39.92030 ? 156 LYS A CG  1 
ATOM   1288 C CD  . LYS A 1 156 ? 5.52232   16.68884  30.59342 1.000 67.35944 ? 156 LYS A CD  1 
ATOM   1289 C CE  . LYS A 1 156 ? 4.04787   16.52076  31.12238 1.000 92.26643 ? 156 LYS A CE  1 
ATOM   1290 N NZ  . LYS A 1 156 ? 2.97031   15.90756  30.25492 1.000 54.44121 ? 156 LYS A NZ  1 
ATOM   1291 N N   . VAL A 1 157 ? 6.20947   11.88595  26.88882 1.000 21.57517 ? 157 VAL A N   1 
ATOM   1292 C CA  . VAL A 1 157 ? 6.11979   11.46324  25.49982 1.000 28.49210 ? 157 VAL A CA  1 
ATOM   1293 C C   . VAL A 1 157 ? 4.87887   12.04843  24.83687 1.000 19.08581 ? 157 VAL A C   1 
ATOM   1294 O O   . VAL A 1 157 ? 3.77975   12.06208  25.40349 1.000 23.47783 ? 157 VAL A O   1 
ATOM   1295 C CB  . VAL A 1 157 ? 6.16629   9.93240   25.41760 1.000 35.37639 ? 157 VAL A CB  1 
ATOM   1296 C CG1 . VAL A 1 157 ? 7.45483   9.42894   26.07175 1.000 24.61131 ? 157 VAL A CG1 1 
ATOM   1297 C CG2 . VAL A 1 157 ? 4.93160   9.30443   26.06203 1.000 17.76768 ? 157 VAL A CG2 1 
ATOM   1298 N N   . ASP A 1 158 ? 5.08793   12.59291  23.65491 1.000 13.12104 ? 158 ASP A N   1 
ATOM   1299 C CA  . ASP A 1 158 ? 4.05028   13.22127  22.85071 1.000 20.79342 ? 158 ASP A CA  1 
ATOM   1300 C C   . ASP A 1 158 ? 4.28112   13.00920  21.35255 1.000 19.33060 ? 158 ASP A C   1 
ATOM   1301 O O   . ASP A 1 158 ? 3.53344   13.57389  20.54506 1.000 23.22590 ? 158 ASP A O   1 
ATOM   1302 C CB  . ASP A 1 158 ? 4.00253   14.72279  23.16507 1.000 17.00467 ? 158 ASP A CB  1 
ATOM   1303 C CG  . ASP A 1 158 ? 5.37470   15.40051  23.00103 1.000 34.37033 ? 158 ASP A CG  1 
ATOM   1304 O OD1 . ASP A 1 158 ? 5.81077   16.09442  23.95285 1.000 39.28066 ? 158 ASP A OD1 1 
ATOM   1305 O OD2 . ASP A 1 158 ? 6.05698   15.16924  21.98061 1.000 25.17632 ? 158 ASP A OD2 1 
ATOM   1306 N N   . HIS A 1 159 ? 5.26698   12.21932  20.94594 1.000 14.32729 ? 159 HIS A N   1 
ATOM   1307 C CA  . HIS A 1 159 ? 5.59279   12.08464  19.53333 1.000 18.75545 ? 159 HIS A CA  1 
ATOM   1308 C C   . HIS A 1 159 ? 5.92239   10.63827  19.24052 1.000 14.89335 ? 159 HIS A C   1 
ATOM   1309 O O   . HIS A 1 159 ? 6.66898   10.00888  19.99142 1.000 23.04405 ? 159 HIS A O   1 
ATOM   1310 C CB  . HIS A 1 159 ? 6.76846   13.00533  19.17011 1.000 11.94624 ? 159 HIS A CB  1 
ATOM   1311 C CG  . HIS A 1 159 ? 7.04359   13.09717  17.70217 1.000 29.47463 ? 159 HIS A CG  1 
ATOM   1312 N ND1 . HIS A 1 159 ? 6.11080   13.55479  16.78990 1.000 14.29853 ? 159 HIS A ND1 1 
ATOM   1313 C CD2 . HIS A 1 159 ? 8.16331   12.80885  16.99042 1.000 20.38023 ? 159 HIS A CD2 1 
ATOM   1314 C CE1 . HIS A 1 159 ? 6.63911   13.51732  15.57639 1.000 24.16962 ? 159 HIS A CE1 1 
ATOM   1315 N NE2 . HIS A 1 159 ? 7.87751   13.06183  15.66765 1.000 14.82801 ? 159 HIS A NE2 1 
ATOM   1316 N N   . ALA A 1 160 ? 5.40391   10.12611  18.12931 1.000 12.57243 ? 160 ALA A N   1 
ATOM   1317 C CA  . ALA A 1 160 ? 5.63317   8.74184   17.75736 1.000 12.25836 ? 160 ALA A CA  1 
ATOM   1318 C C   . ALA A 1 160 ? 6.60095   8.70643   16.59922 1.000 10.47592 ? 160 ALA A C   1 
ATOM   1319 O O   . ALA A 1 160 ? 6.42295   9.41824   15.60503 1.000 21.47491 ? 160 ALA A O   1 
ATOM   1320 C CB  . ALA A 1 160 ? 4.33851   8.03832   17.34267 1.000 12.92021 ? 160 ALA A CB  1 
ATOM   1321 N N   . VAL A 1 161 ? 7.59897   7.84083   16.72536 1.000 10.78587 ? 161 VAL A N   1 
ATOM   1322 C CA  . VAL A 1 161 ? 8.68576   7.70102   15.77810 1.000 8.78279  ? 161 VAL A CA  1 
ATOM   1323 C C   . VAL A 1 161 ? 8.97590   6.21448   15.69203 1.000 8.60521  ? 161 VAL A C   1 
ATOM   1324 O O   . VAL A 1 161 ? 8.32684   5.40133   16.34851 1.000 13.72120 ? 161 VAL A O   1 
ATOM   1325 C CB  . VAL A 1 161 ? 9.94177   8.46864   16.21715 1.000 19.63499 ? 161 VAL A CB  1 
ATOM   1326 C CG1 . VAL A 1 161 ? 9.73281   9.94952   16.07212 1.000 10.83284 ? 161 VAL A CG1 1 
ATOM   1327 C CG2 . VAL A 1 161 ? 10.25796  8.12868   17.63700 1.000 25.98163 ? 161 VAL A CG2 1 
ATOM   1328 N N   . ALA A 1 162 ? 9.96180   5.85993   14.89753 1.000 11.82972 ? 162 ALA A N   1 
ATOM   1329 C CA  . ALA A 1 162 ? 10.26213  4.46212   14.68169 1.000 7.15630  ? 162 ALA A CA  1 
ATOM   1330 C C   . ALA A 1 162 ? 11.73311  4.23603   14.97389 1.000 15.45802 ? 162 ALA A C   1 
ATOM   1331 O O   . ALA A 1 162 ? 12.57559  5.06741   14.60697 1.000 14.04597 ? 162 ALA A O   1 
ATOM   1332 C CB  . ALA A 1 162 ? 9.91930   4.05290   13.26199 1.000 14.67422 ? 162 ALA A CB  1 
ATOM   1333 N N   . ALA A 1 163 ? 12.03727  3.18243   15.72656 1.000 7.98168  ? 163 ALA A N   1 
ATOM   1334 C CA  . ALA A 1 163 ? 13.42104  2.87128   16.02604 1.000 10.70574 ? 163 ALA A CA  1 
ATOM   1335 C C   . ALA A 1 163 ? 13.87021  1.88519   14.96830 1.000 8.38590  ? 163 ALA A C   1 
ATOM   1336 O O   . ALA A 1 163 ? 13.29249  0.79843   14.85981 1.000 24.98972 ? 163 ALA A O   1 
ATOM   1337 C CB  . ALA A 1 163 ? 13.60210  2.28049   17.42424 1.000 11.72095 ? 163 ALA A CB  1 
ATOM   1338 N N   . VAL A 1 164 ? 14.89173  2.24291   14.19066 1.000 7.61383  ? 164 VAL A N   1 
ATOM   1339 C CA  . VAL A 1 164 ? 15.27789  1.40505   13.06489 1.000 8.53436  ? 164 VAL A CA  1 
ATOM   1340 C C   . VAL A 1 164 ? 16.69352  0.87757   13.23510 1.000 10.38520 ? 164 VAL A C   1 
ATOM   1341 O O   . VAL A 1 164 ? 17.25715  0.28718   12.30709 1.000 8.40843  ? 164 VAL A O   1 
ATOM   1342 C CB  . VAL A 1 164 ? 15.16698  2.16264   11.73088 1.000 12.38799 ? 164 VAL A CB  1 
ATOM   1343 C CG1 . VAL A 1 164 ? 13.68826  2.43141   11.35281 1.000 15.25842 ? 164 VAL A CG1 1 
ATOM   1344 C CG2 . VAL A 1 164 ? 16.04623  3.38266   11.76273 1.000 8.35388  ? 164 VAL A CG2 1 
ATOM   1345 N N   . GLY A 1 165 ? 17.26991  1.06271   14.41184 1.000 14.18130 ? 165 GLY A N   1 
ATOM   1346 C CA  . GLY A 1 165 ? 18.60827  0.58761   14.67231 1.000 9.07485  ? 165 GLY A CA  1 
ATOM   1347 C C   . GLY A 1 165 ? 19.07391  1.09776   16.01312 1.000 8.48009  ? 165 GLY A C   1 
ATOM   1348 O O   . GLY A 1 165 ? 18.34132  1.76924   16.74504 1.000 6.10824  ? 165 GLY A O   1 
ATOM   1349 N N   . TYR A 1 166 ? 20.30183  0.73470   16.33572 1.000 8.54040  ? 166 TYR A N   1 
ATOM   1350 C CA  . TYR A 1 166 ? 20.91983  1.17156   17.57917 1.000 19.16718 ? 166 TYR A CA  1 
ATOM   1351 C C   . TYR A 1 166 ? 22.41265  0.92678   17.48350 1.000 12.32287 ? 166 TYR A C   1 
ATOM   1352 O O   . TYR A 1 166 ? 22.89253  0.18983   16.61690 1.000 15.64139 ? 166 TYR A O   1 
ATOM   1353 C CB  . TYR A 1 166 ? 20.38844  0.45072   18.82595 1.000 10.64986 ? 166 TYR A CB  1 
ATOM   1354 C CG  . TYR A 1 166 ? 20.67801  -1.02627  18.85760 1.000 16.31910 ? 166 TYR A CG  1 
ATOM   1355 C CD1 . TYR A 1 166 ? 21.89945  -1.49288  19.32005 1.000 13.79772 ? 166 TYR A CD1 1 
ATOM   1356 C CD2 . TYR A 1 166 ? 19.70219  -1.96305  18.53487 1.000 13.84144 ? 166 TYR A CD2 1 
ATOM   1357 C CE1 . TYR A 1 166 ? 22.18933  -2.84690  19.37280 1.000 14.31395 ? 166 TYR A CE1 1 
ATOM   1358 C CE2 . TYR A 1 166 ? 19.96686  -3.31975  18.60953 1.000 14.85405 ? 166 TYR A CE2 1 
ATOM   1359 C CZ  . TYR A 1 166 ? 21.22200  -3.75876  19.03277 1.000 19.63277 ? 166 TYR A CZ  1 
ATOM   1360 O OH  . TYR A 1 166 ? 21.53427  -5.11103  19.09454 1.000 10.86699 ? 166 TYR A OH  1 
ATOM   1361 N N   . GLY A 1 167 ? 23.13534  1.49269   18.43136 1.000 13.01692 ? 167 GLY A N   1 
ATOM   1362 C CA  . GLY A 1 167 ? 24.52918  1.16411   18.54239 1.000 15.27561 ? 167 GLY A CA  1 
ATOM   1363 C C   . GLY A 1 167 ? 24.89170  1.24052   20.00651 1.000 15.68498 ? 167 GLY A C   1 
ATOM   1364 O O   . GLY A 1 167 ? 24.02016  1.35801   20.87652 1.000 16.47942 ? 167 GLY A O   1 
ATOM   1365 N N   . PRO A 1 168 ? 26.17402  1.10571   20.31469 1.000 18.42207 ? 168 PRO A N   1 
ATOM   1366 C CA  . PRO A 1 168 ? 26.58031  0.95653   21.72324 1.000 21.89076 ? 168 PRO A CA  1 
ATOM   1367 C C   . PRO A 1 168 ? 26.08763  2.06482   22.63631 1.000 15.26095 ? 168 PRO A C   1 
ATOM   1368 O O   . PRO A 1 168 ? 25.80914  1.79833   23.80653 1.000 24.93060 ? 168 PRO A O   1 
ATOM   1369 C CB  . PRO A 1 168 ? 28.11088  0.91446   21.62860 1.000 15.71539 ? 168 PRO A CB  1 
ATOM   1370 C CG  . PRO A 1 168 ? 28.35963  0.41267   20.22330 1.000 21.88788 ? 168 PRO A CG  1 
ATOM   1371 C CD  . PRO A 1 168 ? 27.32412  1.07195   19.40319 1.000 15.56062 ? 168 PRO A CD  1 
ATOM   1372 N N   A ASN A 1 169 ? 25.98099  3.30950   22.14719 0.663 20.55885 ? 169 ASN A N   1 
ATOM   1373 N N   B ASN A 1 169 ? 25.94990  3.29637   22.13696 0.337 20.41699 ? 169 ASN A N   1 
ATOM   1374 C CA  A ASN A 1 169 ? 25.56290  4.42754   22.98914 0.663 17.38443 ? 169 ASN A CA  1 
ATOM   1375 C CA  B ASN A 1 169 ? 25.55483  4.41277   22.98708 0.337 17.31646 ? 169 ASN A CA  1 
ATOM   1376 C C   A ASN A 1 169 ? 24.33777  5.17421   22.44799 0.663 14.52078 ? 169 ASN A C   1 
ATOM   1377 C C   B ASN A 1 169 ? 24.34660  5.17418   22.44126 0.337 14.25380 ? 169 ASN A C   1 
ATOM   1378 O O   A ASN A 1 169 ? 24.12354  6.33264   22.81152 0.663 13.16622 ? 169 ASN A O   1 
ATOM   1379 O O   B ASN A 1 169 ? 24.15984  6.34365   22.78781 0.337 13.94438 ? 169 ASN A O   1 
ATOM   1380 C CB  A ASN A 1 169 ? 26.72328  5.41161   23.20365 0.663 14.95061 ? 169 ASN A CB  1 
ATOM   1381 C CB  B ASN A 1 169 ? 26.73641  5.36939   23.18741 0.337 15.47042 ? 169 ASN A CB  1 
ATOM   1382 C CG  A ASN A 1 169 ? 27.37403  5.86584   21.89970 0.663 16.04054 ? 169 ASN A CG  1 
ATOM   1383 C CG  B ASN A 1 169 ? 27.81657  4.78390   24.07991 0.337 15.64433 ? 169 ASN A CG  1 
ATOM   1384 O OD1 A ASN A 1 169 ? 27.05212  5.37296   20.80912 0.663 11.80320 ? 169 ASN A OD1 1 
ATOM   1385 O OD1 B ASN A 1 169 ? 27.52841  4.04823   25.02442 0.337 18.39342 ? 169 ASN A OD1 1 
ATOM   1386 N ND2 A ASN A 1 169 ? 28.30348  6.81189   22.01071 0.663 19.80345 ? 169 ASN A ND2 1 
ATOM   1387 N ND2 B ASN A 1 169 ? 29.07324  5.10154   23.77689 0.337 17.14140 ? 169 ASN A ND2 1 
ATOM   1388 N N   . TYR A 1 170 ? 23.51299  4.55105   21.60898 1.000 15.57445 ? 170 TYR A N   1 
ATOM   1389 C CA  . TYR A 1 170 ? 22.37723  5.27751   21.04277 1.000 17.34797 ? 170 TYR A CA  1 
ATOM   1390 C C   . TYR A 1 170 ? 21.36241  4.29379   20.49063 1.000 16.61033 ? 170 TYR A C   1 
ATOM   1391 O O   . TYR A 1 170 ? 21.62976  3.10315   20.31430 1.000 17.12928 ? 170 TYR A O   1 
ATOM   1392 C CB  . TYR A 1 170 ? 22.77381  6.23984   19.90440 1.000 11.57934 ? 170 TYR A CB  1 
ATOM   1393 C CG  . TYR A 1 170 ? 23.26849  5.51844   18.67884 1.000 16.38290 ? 170 TYR A CG  1 
ATOM   1394 C CD1 . TYR A 1 170 ? 24.61774  5.24973   18.48990 1.000 18.47420 ? 170 TYR A CD1 1 
ATOM   1395 C CD2 . TYR A 1 170 ? 22.37756  5.18335   17.64992 1.000 11.36623 ? 170 TYR A CD2 1 
ATOM   1396 C CE1 . TYR A 1 170 ? 25.07420  4.57361   17.32767 1.000 17.07448 ? 170 TYR A CE1 1 
ATOM   1397 C CE2 . TYR A 1 170 ? 22.81027  4.51931   16.50682 1.000 20.95454 ? 170 TYR A CE2 1 
ATOM   1398 C CZ  . TYR A 1 170 ? 24.16113  4.22350   16.34401 1.000 15.65675 ? 170 TYR A CZ  1 
ATOM   1399 O OH  . TYR A 1 170 ? 24.56902  3.56985   15.20520 1.000 24.41791 ? 170 TYR A OH  1 
ATOM   1400 N N   . ILE A 1 171 ? 20.18175  4.83004   20.23137 1.000 18.95140 ? 171 ILE A N   1 
ATOM   1401 C CA  . ILE A 1 171 ? 19.13133  4.17284   19.48026 1.000 11.91470 ? 171 ILE A CA  1 
ATOM   1402 C C   . ILE A 1 171 ? 18.86530  5.05839   18.27034 1.000 13.11649 ? 171 ILE A C   1 
ATOM   1403 O O   . ILE A 1 171 ? 18.82961  6.28706   18.40184 1.000 14.47707 ? 171 ILE A O   1 
ATOM   1404 C CB  . ILE A 1 171 ? 17.87730  3.97429   20.34759 1.000 20.32418 ? 171 ILE A CB  1 
ATOM   1405 C CG1 . ILE A 1 171 ? 18.13067  2.84745   21.34447 1.000 16.77185 ? 171 ILE A CG1 1 
ATOM   1406 C CG2 . ILE A 1 171 ? 16.68267  3.57413   19.49747 1.000 12.08535 ? 171 ILE A CG2 1 
ATOM   1407 C CD1 . ILE A 1 171 ? 17.10707  2.83115   22.43207 1.000 19.28230 ? 171 ILE A CD1 1 
ATOM   1408 N N   . LEU A 1 172 ? 18.74773  4.45193   17.09140 1.000 13.41124 ? 172 LEU A N   1 
ATOM   1409 C CA  . LEU A 1 172 ? 18.59594  5.20298   15.84867 1.000 12.61774 ? 172 LEU A CA  1 
ATOM   1410 C C   . LEU A 1 172 ? 17.11709  5.35311   15.54792 1.000 11.18544 ? 172 LEU A C   1 
ATOM   1411 O O   . LEU A 1 172 ? 16.41075  4.35830   15.36051 1.000 14.29978 ? 172 LEU A O   1 
ATOM   1412 C CB  . LEU A 1 172 ? 19.32672  4.49920   14.71379 1.000 7.00638  ? 172 LEU A CB  1 
ATOM   1413 C CG  . LEU A 1 172 ? 19.05679  5.07569   13.33666 1.000 11.78519 ? 172 LEU A CG  1 
ATOM   1414 C CD1 . LEU A 1 172 ? 19.72299  6.40895   13.23070 1.000 13.53382 ? 172 LEU A CD1 1 
ATOM   1415 C CD2 . LEU A 1 172 ? 19.67431  4.09621   12.29901 1.000 18.32874 ? 172 LEU A CD2 1 
ATOM   1416 N N   . ILE A 1 173 ? 16.66433  6.60145   15.46752 1.000 11.29506 ? 173 ILE A N   1 
ATOM   1417 C CA  . ILE A 1 173 ? 15.25764  6.92741   15.31477 1.000 10.48550 ? 173 ILE A CA  1 
ATOM   1418 C C   . ILE A 1 173 ? 15.02145  7.54088   13.94197 1.000 16.13865 ? 173 ILE A C   1 
ATOM   1419 O O   . ILE A 1 173 ? 15.78024  8.40699   13.50030 1.000 20.97993 ? 173 ILE A O   1 
ATOM   1420 C CB  . ILE A 1 173 ? 14.79901  7.86411   16.44937 1.000 16.25765 ? 173 ILE A CB  1 
ATOM   1421 C CG1 . ILE A 1 173 ? 14.88090  7.20109   17.84204 1.000 14.46862 ? 173 ILE A CG1 1 
ATOM   1422 C CG2 . ILE A 1 173 ? 13.39911  8.39084   16.20639 1.000 11.04974 ? 173 ILE A CG2 1 
ATOM   1423 C CD1 . ILE A 1 173 ? 14.16802  5.89494   18.00679 1.000 14.16461 ? 173 ILE A CD1 1 
ATOM   1424 N N   . LYS A 1 174 ? 13.98541  7.05135   13.25584 1.000 13.56717 ? 174 LYS A N   1 
ATOM   1425 C CA  . LYS A 1 174 ? 13.51395  7.63253   12.01130 1.000 9.72828  ? 174 LYS A CA  1 
ATOM   1426 C C   . LYS A 1 174 ? 12.39170  8.58059   12.35713 1.000 10.62135 ? 174 LYS A C   1 
ATOM   1427 O O   . LYS A 1 174 ? 11.31490  8.13616   12.77007 1.000 12.53596 ? 174 LYS A O   1 
ATOM   1428 C CB  . LYS A 1 174 ? 12.99279  6.54282   11.07078 1.000 19.14022 ? 174 LYS A CB  1 
ATOM   1429 C CG  . LYS A 1 174 ? 12.71863  7.03617   9.67124  1.000 14.66512 ? 174 LYS A CG  1 
ATOM   1430 C CD  . LYS A 1 174 ? 11.98781  5.99172   8.80819  1.000 13.40773 ? 174 LYS A CD  1 
ATOM   1431 C CE  . LYS A 1 174 ? 11.93696  6.44913   7.36491  1.000 14.95429 ? 174 LYS A CE  1 
ATOM   1432 N NZ  . LYS A 1 174 ? 11.18027  5.52243   6.49128  1.000 24.00429 ? 174 LYS A NZ  1 
ATOM   1433 N N   . ASN A 1 175 ? 12.59052  9.86211   12.07994 1.000 7.32179  ? 175 ASN A N   1 
ATOM   1434 C CA  . ASN A 1 175 ? 11.51412  10.80339  12.32489 1.000 10.88955 ? 175 ASN A CA  1 
ATOM   1435 C C   . ASN A 1 175 ? 10.70700  11.02602  11.05020 1.000 12.50891 ? 175 ASN A C   1 
ATOM   1436 O O   . ASN A 1 175 ? 11.07716  10.57694  9.96678  1.000 14.44830 ? 175 ASN A O   1 
ATOM   1437 C CB  . ASN A 1 175 ? 12.09586  12.10954  12.86304 1.000 6.80595  ? 175 ASN A CB  1 
ATOM   1438 C CG  . ASN A 1 175 ? 11.09052  12.90144  13.67068 1.000 15.82916 ? 175 ASN A CG  1 
ATOM   1439 O OD1 . ASN A 1 175 ? 9.96065   12.44536  13.87481 1.000 17.47742 ? 175 ASN A OD1 1 
ATOM   1440 N ND2 . ASN A 1 175 ? 11.51766  14.05412  14.20922 1.000 9.93150  ? 175 ASN A ND2 1 
ATOM   1441 N N   . SER A 1 176 ? 9.60564   11.76602  11.17874 1.000 15.26557 ? 176 SER A N   1 
ATOM   1442 C CA  . SER A 1 176 ? 8.71547   12.02478  10.05638 1.000 15.55354 ? 176 SER A CA  1 
ATOM   1443 C C   . SER A 1 176 ? 8.54903   13.52463  9.88362  1.000 7.80241  ? 176 SER A C   1 
ATOM   1444 O O   . SER A 1 176 ? 7.46488   14.02268  9.56120  1.000 8.17733  ? 176 SER A O   1 
ATOM   1445 C CB  . SER A 1 176 ? 7.36067   11.34333  10.25337 1.000 15.25043 ? 176 SER A CB  1 
ATOM   1446 O OG  . SER A 1 176 ? 6.89096   11.55257  11.57087 1.000 16.30419 ? 176 SER A OG  1 
ATOM   1447 N N   . TRP A 1 177 ? 9.66530   14.24348  9.97508  1.000 13.89902 ? 177 TRP A N   1 
ATOM   1448 C CA  . TRP A 1 177 ? 9.72011   15.68340  9.76937  1.000 12.98937 ? 177 TRP A CA  1 
ATOM   1449 C C   . TRP A 1 177 ? 10.54327  16.03534  8.51713  1.000 9.27304  ? 177 TRP A C   1 
ATOM   1450 O O   . TRP A 1 177 ? 11.10835  17.12444  8.41218  1.000 11.01274 ? 177 TRP A O   1 
ATOM   1451 C CB  . TRP A 1 177 ? 10.37232  16.29647  11.00625 1.000 12.65545 ? 177 TRP A CB  1 
ATOM   1452 C CG  . TRP A 1 177 ? 9.51570   16.30614  12.23204 1.000 17.15983 ? 177 TRP A CG  1 
ATOM   1453 C CD1 . TRP A 1 177 ? 8.23245   15.87670  12.33972 1.000 18.53620 ? 177 TRP A CD1 1 
ATOM   1454 C CD2 . TRP A 1 177 ? 9.91074   16.72134  13.54110 1.000 16.08245 ? 177 TRP A CD2 1 
ATOM   1455 N NE1 . TRP A 1 177 ? 7.78677   16.02139  13.62808 1.000 15.57229 ? 177 TRP A NE1 1 
ATOM   1456 C CE2 . TRP A 1 177 ? 8.80184   16.53448  14.39062 1.000 20.04231 ? 177 TRP A CE2 1 
ATOM   1457 C CE3 . TRP A 1 177 ? 11.09074  17.25398  14.07646 1.000 26.81248 ? 177 TRP A CE3 1 
ATOM   1458 C CZ2 . TRP A 1 177 ? 8.83338   16.85810  15.75747 1.000 17.52825 ? 177 TRP A CZ2 1 
ATOM   1459 C CZ3 . TRP A 1 177 ? 11.12163  17.57479  15.44329 1.000 25.08777 ? 177 TRP A CZ3 1 
ATOM   1460 C CH2 . TRP A 1 177 ? 9.99609   17.37611  16.26080 1.000 20.98445 ? 177 TRP A CH2 1 
ATOM   1461 N N   . GLY A 1 178 ? 10.50734  15.15931  7.53353  1.000 8.38728  ? 178 GLY A N   1 
ATOM   1462 C CA  . GLY A 1 178 ? 11.21888  15.27874  6.27128  1.000 22.81976 ? 178 GLY A CA  1 
ATOM   1463 C C   . GLY A 1 178 ? 12.73621  15.14400  6.38871  1.000 15.35012 ? 178 GLY A C   1 
ATOM   1464 O O   . GLY A 1 178 ? 13.30213  15.00514  7.46295  1.000 11.91387 ? 178 GLY A O   1 
ATOM   1465 N N   . THR A 1 179 ? 13.40138  15.25651  5.22799  1.000 13.41315 ? 179 THR A N   1 
ATOM   1466 C CA  . THR A 1 179 ? 14.84058  14.98321  5.16353  1.000 16.91618 ? 179 THR A CA  1 
ATOM   1467 C C   . THR A 1 179 ? 15.67200  16.09156  5.79940  1.000 12.99131 ? 179 THR A C   1 
ATOM   1468 O O   . THR A 1 179 ? 16.83596  15.86942  6.13437  1.000 8.88043  ? 179 THR A O   1 
ATOM   1469 C CB  . THR A 1 179 ? 15.27223  14.67172  3.72624  1.000 13.61703 ? 179 THR A CB  1 
ATOM   1470 O OG1 . THR A 1 179 ? 14.71352  15.60533  2.79197  1.000 14.58117 ? 179 THR A OG1 1 
ATOM   1471 C CG2 . THR A 1 179 ? 14.75202  13.29730  3.38050  1.000 12.84826 ? 179 THR A CG2 1 
ATOM   1472 N N   . GLY A 1 180 ? 15.13164  17.30731  5.83277  1.000 11.69171 ? 180 GLY A N   1 
ATOM   1473 C CA  . GLY A 1 180 ? 15.75431  18.54742  6.25271  1.000 13.14656 ? 180 GLY A CA  1 
ATOM   1474 C C   . GLY A 1 180 ? 15.93949  18.71719  7.75302  1.000 22.80508 ? 180 GLY A C   1 
ATOM   1475 O O   . GLY A 1 180 ? 16.42847  19.75461  8.20989  1.000 41.10373 ? 180 GLY A O   1 
ATOM   1476 N N   . TRP A 1 181 ? 15.61837  17.69032  8.52209  1.000 14.58802 ? 181 TRP A N   1 
ATOM   1477 C CA  . TRP A 1 181 ? 15.68490  17.72694  9.97225  1.000 12.05473 ? 181 TRP A CA  1 
ATOM   1478 C C   . TRP A 1 181 ? 16.56885  16.62360  10.49490 1.000 7.37708  ? 181 TRP A C   1 
ATOM   1479 O O   . TRP A 1 181 ? 16.57962  15.51493  9.95088  1.000 15.70790 ? 181 TRP A O   1 
ATOM   1480 C CB  . TRP A 1 181 ? 14.29106  17.52779  10.61819 1.000 17.59011 ? 181 TRP A CB  1 
ATOM   1481 C CG  . TRP A 1 181 ? 14.34922  17.52138  12.15487 1.000 11.05477 ? 181 TRP A CG  1 
ATOM   1482 C CD1 . TRP A 1 181 ? 14.23353  18.59835  12.98211 1.000 15.97888 ? 181 TRP A CD1 1 
ATOM   1483 C CD2 . TRP A 1 181 ? 14.46414  16.36942  13.01975 1.000 19.78382 ? 181 TRP A CD2 1 
ATOM   1484 N NE1 . TRP A 1 181 ? 14.33995  18.20705  14.29109 1.000 14.36353 ? 181 TRP A NE1 1 
ATOM   1485 C CE2 . TRP A 1 181 ? 14.46602  16.84675  14.34783 1.000 10.69608 ? 181 TRP A CE2 1 
ATOM   1486 C CE3 . TRP A 1 181 ? 14.59240  14.98298  12.79865 1.000 17.39305 ? 181 TRP A CE3 1 
ATOM   1487 C CZ2 . TRP A 1 181 ? 14.59247  15.98873  15.46744 1.000 14.48611 ? 181 TRP A CZ2 1 
ATOM   1488 C CZ3 . TRP A 1 181 ? 14.73224  14.12377  13.92281 1.000 10.24993 ? 181 TRP A CZ3 1 
ATOM   1489 C CH2 . TRP A 1 181 ? 14.72296  14.63670  15.22792 1.000 15.65766 ? 181 TRP A CH2 1 
ATOM   1490 N N   . GLY A 1 182 ? 17.35519  16.95957  11.53162 1.000 8.10174  ? 182 GLY A N   1 
ATOM   1491 C CA  . GLY A 1 182 ? 18.16836  15.92026  12.13719 1.000 7.00712  ? 182 GLY A CA  1 
ATOM   1492 C C   . GLY A 1 182 ? 19.24151  15.46173  11.16976 1.000 13.73153 ? 182 GLY A C   1 
ATOM   1493 O O   . GLY A 1 182 ? 19.75689  16.23651  10.36116 1.000 22.26610 ? 182 GLY A O   1 
ATOM   1494 N N   . GLU A 1 183 ? 19.57705  14.17501  11.25092 1.000 11.31261 ? 183 GLU A N   1 
ATOM   1495 C CA  . GLU A 1 183 ? 20.59983  13.56692  10.39566 1.000 10.24953 ? 183 GLU A CA  1 
ATOM   1496 C C   . GLU A 1 183 ? 19.93503  12.92320  9.17986  1.000 14.38415 ? 183 GLU A C   1 
ATOM   1497 O O   . GLU A 1 183 ? 19.63092  11.72773  9.15109  1.000 14.67005 ? 183 GLU A O   1 
ATOM   1498 C CB  . GLU A 1 183 ? 21.40037  12.55199  11.20304 1.000 15.37787 ? 183 GLU A CB  1 
ATOM   1499 C CG  . GLU A 1 183 ? 22.01315  13.18563  12.46035 1.000 14.82305 ? 183 GLU A CG  1 
ATOM   1500 C CD  . GLU A 1 183 ? 23.04241  12.30693  13.13743 1.000 20.49726 ? 183 GLU A CD  1 
ATOM   1501 O OE1 . GLU A 1 183 ? 22.84721  11.06941  13.16995 1.000 14.19176 ? 183 GLU A OE1 1 
ATOM   1502 O OE2 . GLU A 1 183 ? 24.03291  12.85275  13.67347 1.000 30.85276 ? 183 GLU A OE2 1 
ATOM   1503 N N   . ASN A 1 184 ? 19.59815  13.76814  8.20834  1.000 17.95619 ? 184 ASN A N   1 
ATOM   1504 C CA  . ASN A 1 184 ? 18.89401  13.34342  7.00033  1.000 12.50228 ? 184 ASN A CA  1 
ATOM   1505 C C   . ASN A 1 184 ? 17.53555  12.75393  7.36271  1.000 13.66262 ? 184 ASN A C   1 
ATOM   1506 O O   . ASN A 1 184 ? 17.07176  11.78634  6.75914  1.000 11.17976 ? 184 ASN A O   1 
ATOM   1507 C CB  . ASN A 1 184 ? 19.73610  12.30983  6.25037  1.000 17.91414 ? 184 ASN A CB  1 
ATOM   1508 C CG  . ASN A 1 184 ? 20.89353  12.93880  5.49205  1.000 18.07549 ? 184 ASN A CG  1 
ATOM   1509 O OD1 . ASN A 1 184 ? 20.93338  14.14870  5.28079  1.000 16.32760 ? 184 ASN A OD1 1 
ATOM   1510 N ND2 . ASN A 1 184 ? 21.86563  12.11567  5.12144  1.000 19.39990 ? 184 ASN A ND2 1 
ATOM   1511 N N   . GLY A 1 185 ? 16.91283  13.32311  8.38975  1.000 23.55590 ? 185 GLY A N   1 
ATOM   1512 C CA  . GLY A 1 185 ? 15.61630  12.89509  8.85852  1.000 17.79639 ? 185 GLY A CA  1 
ATOM   1513 C C   . GLY A 1 185 ? 15.64464  11.97000  10.04349 1.000 9.44583  ? 185 GLY A C   1 
ATOM   1514 O O   . GLY A 1 185 ? 14.57410  11.62510  10.56221 1.000 13.02380 ? 185 GLY A O   1 
ATOM   1515 N N   . TYR A 1 186 ? 16.82425  11.57712  10.50145 1.000 12.88844 ? 186 TYR A N   1 
ATOM   1516 C CA  . TYR A 1 186 ? 17.00777  10.62266  11.58849 1.000 10.54414 ? 186 TYR A CA  1 
ATOM   1517 C C   . TYR A 1 186 ? 17.53694  11.31311  12.83713 1.000 14.12276 ? 186 TYR A C   1 
ATOM   1518 O O   . TYR A 1 186 ? 18.05424  12.42956  12.77913 1.000 8.67118  ? 186 TYR A O   1 
ATOM   1519 C CB  . TYR A 1 186 ? 17.97392  9.51899   11.15625 1.000 13.91238 ? 186 TYR A CB  1 
ATOM   1520 C CG  . TYR A 1 186 ? 17.38237  8.53150   10.17935 1.000 19.96285 ? 186 TYR A CG  1 
ATOM   1521 C CD1 . TYR A 1 186 ? 16.76123  7.36776   10.61842 1.000 16.26136 ? 186 TYR A CD1 1 
ATOM   1522 C CD2 . TYR A 1 186 ? 17.37119  8.81257   8.81455  1.000 19.93933 ? 186 TYR A CD2 1 
ATOM   1523 C CE1 . TYR A 1 186 ? 16.21413  6.46979   9.71059  1.000 25.82885 ? 186 TYR A CE1 1 
ATOM   1524 C CE2 . TYR A 1 186 ? 16.81208  7.91985   7.89156  1.000 13.96396 ? 186 TYR A CE2 1 
ATOM   1525 C CZ  . TYR A 1 186 ? 16.21731  6.76807   8.35292  1.000 19.86155 ? 186 TYR A CZ  1 
ATOM   1526 O OH  . TYR A 1 186 ? 15.67826  5.88295   7.45549  1.000 11.31437 ? 186 TYR A OH  1 
ATOM   1527 N N   . ILE A 1 187 ? 17.37622  10.65947  13.98825 1.000 12.67614 ? 187 ILE A N   1 
ATOM   1528 C CA  . ILE A 1 187 ? 18.04279  11.14912  15.18737 1.000 15.90043 ? 187 ILE A CA  1 
ATOM   1529 C C   . ILE A 1 187 ? 18.64402  9.92675   15.85180 1.000 13.56885 ? 187 ILE A C   1 
ATOM   1530 O O   . ILE A 1 187 ? 18.03309  8.85665   15.89139 1.000 21.28361 ? 187 ILE A O   1 
ATOM   1531 C CB  . ILE A 1 187 ? 17.11422  11.93490  16.14800 1.000 18.96520 ? 187 ILE A CB  1 
ATOM   1532 C CG1 . ILE A 1 187 ? 17.80390  12.20791  17.48352 1.000 15.48707 ? 187 ILE A CG1 1 
ATOM   1533 C CG2 . ILE A 1 187 ? 15.85735  11.13770  16.50259 1.000 7.67380  ? 187 ILE A CG2 1 
ATOM   1534 C CD1 . ILE A 1 187 ? 17.11006  13.27806  18.29718 1.000 16.16506 ? 187 ILE A CD1 1 
ATOM   1535 N N   . ARG A 1 188 ? 19.82563  10.09482  16.40033 1.000 8.35293  ? 188 ARG A N   1 
ATOM   1536 C CA  . ARG A 1 188 ? 20.40177  9.12694   17.31053 1.000 17.64557 ? 188 ARG A CA  1 
ATOM   1537 C C   . ARG A 1 188 ? 20.26247  9.62681   18.74254 1.000 10.12876 ? 188 ARG A C   1 
ATOM   1538 O O   . ARG A 1 188 ? 20.74983  10.71529  19.07362 1.000 9.30911  ? 188 ARG A O   1 
ATOM   1539 C CB  . ARG A 1 188 ? 21.86684  8.87423   16.95068 1.000 9.11254  ? 188 ARG A CB  1 
ATOM   1540 C CG  . ARG A 1 188 ? 22.07397  8.21462   15.53780 1.000 9.85782  ? 188 ARG A CG  1 
ATOM   1541 C CD  . ARG A 1 188 ? 23.56705  8.07435   15.35108 1.000 8.91023  ? 188 ARG A CD  1 
ATOM   1542 N NE  . ARG A 1 188 ? 24.16067  9.38770   15.15943 1.000 8.28330  ? 188 ARG A NE  1 
ATOM   1543 C CZ  . ARG A 1 188 ? 25.42566  9.67569   15.41266 1.000 14.22792 ? 188 ARG A CZ  1 
ATOM   1544 N NH1 . ARG A 1 188 ? 26.28272  8.74299   15.79165 1.000 15.85138 ? 188 ARG A NH1 1 
ATOM   1545 N NH2 . ARG A 1 188 ? 25.85259  10.92188  15.23559 1.000 23.05378 ? 188 ARG A NH2 1 
ATOM   1546 N N   . ILE A 1 189 ? 19.50498  8.89166   19.54562 1.000 7.12991  ? 189 ILE A N   1 
ATOM   1547 C CA  . ILE A 1 189 ? 19.19954  9.27910   20.91357 1.000 16.21973 ? 189 ILE A CA  1 
ATOM   1548 C C   . ILE A 1 189 ? 20.08004  8.42802   21.82156 1.000 18.70719 ? 189 ILE A C   1 
ATOM   1549 O O   . ILE A 1 189 ? 20.16483  7.20177   21.64905 1.000 13.45213 ? 189 ILE A O   1 
ATOM   1550 C CB  . ILE A 1 189 ? 17.70981  9.06928   21.22514 1.000 14.14618 ? 189 ILE A CB  1 
ATOM   1551 C CG1 . ILE A 1 189 ? 16.86605  10.03353  20.37893 1.000 20.35138 ? 189 ILE A CG1 1 
ATOM   1552 C CG2 . ILE A 1 189 ? 17.45002  9.18966   22.72679 1.000 21.90067 ? 189 ILE A CG2 1 
ATOM   1553 C CD1 . ILE A 1 189 ? 15.40886  9.92736   20.62327 1.000 29.35274 ? 189 ILE A CD1 1 
ATOM   1554 N N   . LYS A 1 190 ? 20.71921  9.06581   22.79426 1.000 13.58978 ? 190 LYS A N   1 
ATOM   1555 C CA  . LYS A 1 190 ? 21.52992  8.34468   23.76891 1.000 10.95205 ? 190 LYS A CA  1 
ATOM   1556 C C   . LYS A 1 190 ? 20.74583  7.24760   24.45888 1.000 17.87551 ? 190 LYS A C   1 
ATOM   1557 O O   . LYS A 1 190 ? 19.59306  7.44292   24.84634 1.000 13.62307 ? 190 LYS A O   1 
ATOM   1558 C CB  . LYS A 1 190 ? 22.11454  9.30340   24.81398 1.000 25.32222 ? 190 LYS A CB  1 
ATOM   1559 C CG  . LYS A 1 190 ? 23.10896  8.60465   25.77284 1.000 22.03700 ? 190 LYS A CG  1 
ATOM   1560 C CD  . LYS A 1 190 ? 24.57427  8.85351   25.43372 1.000 32.83973 ? 190 LYS A CD  1 
ATOM   1561 C CE  . LYS A 1 190 ? 25.48799  8.85287   26.68212 1.000 23.85854 ? 190 LYS A CE  1 
ATOM   1562 N NZ  . LYS A 1 190 ? 25.15885  9.98171   27.59772 1.000 51.28693 ? 190 LYS A NZ  1 
ATOM   1563 N N   . ARG A 1 191 ? 21.41531  6.11430   24.69336 1.000 20.28662 ? 191 ARG A N   1 
ATOM   1564 C CA  . ARG A 1 191 ? 20.87013  5.05915   25.53664 1.000 18.60635 ? 191 ARG A CA  1 
ATOM   1565 C C   . ARG A 1 191 ? 21.88738  4.75517   26.62653 1.000 16.08589 ? 191 ARG A C   1 
ATOM   1566 O O   . ARG A 1 191 ? 22.97764  5.32529   26.65599 1.000 20.58345 ? 191 ARG A O   1 
ATOM   1567 C CB  . ARG A 1 191 ? 20.53076  3.79523   24.73653 1.000 17.91456 ? 191 ARG A CB  1 
ATOM   1568 C CG  . ARG A 1 191 ? 21.73481  3.07917   24.12853 1.000 18.06634 ? 191 ARG A CG  1 
ATOM   1569 C CD  . ARG A 1 191 ? 21.29165  1.75031   23.48129 1.000 21.33710 ? 191 ARG A CD  1 
ATOM   1570 N NE  . ARG A 1 191 ? 22.40805  0.84565   23.22158 1.000 16.34964 ? 191 ARG A NE  1 
ATOM   1571 C CZ  . ARG A 1 191 ? 22.85426  -0.06720  24.07329 1.000 18.59867 ? 191 ARG A CZ  1 
ATOM   1572 N NH1 . ARG A 1 191 ? 22.34064  -0.18842  25.29354 1.000 5.81626  ? 191 ARG A NH1 1 
ATOM   1573 N NH2 . ARG A 1 191 ? 23.83089  -0.88507  23.68940 1.000 19.72939 ? 191 ARG A NH2 1 
ATOM   1574 N N   . GLY A 1 192 ? 21.53169  3.83877   27.51673 1.000 15.68110 ? 192 GLY A N   1 
ATOM   1575 C CA  . GLY A 1 192 ? 22.48204  3.33019   28.48996 1.000 17.15633 ? 192 GLY A CA  1 
ATOM   1576 C C   . GLY A 1 192 ? 22.86172  4.40501   29.49863 1.000 29.33614 ? 192 GLY A C   1 
ATOM   1577 O O   . GLY A 1 192 ? 24.01368  4.44401   29.94685 1.000 23.07282 ? 192 GLY A O   1 
ATOM   1578 N N   . THR A 1 193 ? 21.90217  5.24802   29.90912 1.000 12.86039 ? 193 THR A N   1 
ATOM   1579 C CA  . THR A 1 193 ? 22.13810  6.31696   30.88163 1.000 17.49441 ? 193 THR A CA  1 
ATOM   1580 C C   . THR A 1 193 ? 21.57789  5.98075   32.25550 1.000 26.55140 ? 193 THR A C   1 
ATOM   1581 O O   . THR A 1 193 ? 21.73174  6.77897   33.18647 1.000 42.41811 ? 193 THR A O   1 
ATOM   1582 C CB  . THR A 1 193 ? 21.46832  7.64254   30.44009 1.000 28.48425 ? 193 THR A CB  1 
ATOM   1583 O OG1 . THR A 1 193 ? 20.04069  7.48081   30.39929 1.000 29.83922 ? 193 THR A OG1 1 
ATOM   1584 C CG2 . THR A 1 193 ? 21.93060  8.11648   29.10429 1.000 22.97178 ? 193 THR A CG2 1 
ATOM   1585 N N   . GLY A 1 194 ? 20.94702  4.81722   32.40365 1.000 19.83180 ? 194 GLY A N   1 
ATOM   1586 C CA  . GLY A 1 194 ? 20.38560  4.35970   33.65571 1.000 31.21378 ? 194 GLY A CA  1 
ATOM   1587 C C   . GLY A 1 194 ? 19.01495  4.89485   33.96309 1.000 29.29205 ? 194 GLY A C   1 
ATOM   1588 O O   . GLY A 1 194 ? 18.39459  4.45303   34.94183 1.000 39.77668 ? 194 GLY A O   1 
ATOM   1589 N N   . ASN A 1 195 ? 18.52856  5.83439   33.16775 1.000 44.38916 ? 195 ASN A N   1 
ATOM   1590 C CA  . ASN A 1 195 ? 17.16410  6.33036   33.26905 1.000 36.82010 ? 195 ASN A CA  1 
ATOM   1591 C C   . ASN A 1 195 ? 16.21299  5.25725   32.74494 1.000 28.40083 ? 195 ASN A C   1 
ATOM   1592 O O   . ASN A 1 195 ? 16.31197  4.84059   31.58580 1.000 36.07275 ? 195 ASN A O   1 
ATOM   1593 C CB  . ASN A 1 195 ? 17.04951  7.64621   32.50643 1.000 34.59907 ? 195 ASN A CB  1 
ATOM   1594 C CG  . ASN A 1 195 ? 15.74643  8.34730   32.73748 1.000 31.49468 ? 195 ASN A CG  1 
ATOM   1595 O OD1 . ASN A 1 195 ? 14.86137  7.85203   33.44440 1.000 49.82312 ? 195 ASN A OD1 1 
ATOM   1596 N ND2 . ASN A 1 195 ? 15.63526  9.54927   32.18650 1.000 31.72340 ? 195 ASN A ND2 1 
ATOM   1597 N N   . SER A 1 196 ? 15.28040  4.82598   33.58432 1.000 32.85625 ? 196 SER A N   1 
ATOM   1598 C CA  . SER A 1 196 ? 14.34362  3.78778   33.17005 1.000 36.91184 ? 196 SER A CA  1 
ATOM   1599 C C   . SER A 1 196 ? 13.40057  4.28893   32.08824 1.000 29.11633 ? 196 SER A C   1 
ATOM   1600 O O   . SER A 1 196 ? 12.98236  3.51522   31.22407 1.000 28.71801 ? 196 SER A O   1 
ATOM   1601 C CB  . SER A 1 196 ? 13.55653  3.27256   34.37465 1.000 35.94783 ? 196 SER A CB  1 
ATOM   1602 O OG  . SER A 1 196 ? 13.21743  1.90910   34.19365 1.000 53.72732 ? 196 SER A OG  1 
ATOM   1603 N N   . TYR A 1 197 ? 13.05171  5.56839   32.11917 1.000 20.18103 ? 197 TYR A N   1 
ATOM   1604 C CA  . TYR A 1 197 ? 12.27575  6.13348   31.02465 1.000 21.10386 ? 197 TYR A CA  1 
ATOM   1605 C C   . TYR A 1 197 ? 13.05033  6.17818   29.71520 1.000 21.76463 ? 197 TYR A C   1 
ATOM   1606 O O   . TYR A 1 197 ? 12.42834  6.13220   28.64775 1.000 19.70025 ? 197 TYR A O   1 
ATOM   1607 C CB  . TYR A 1 197 ? 11.76260  7.53322   31.38825 1.000 28.33806 ? 197 TYR A CB  1 
ATOM   1608 C CG  . TYR A 1 197 ? 10.94520  7.59270   32.66173 1.000 21.70282 ? 197 TYR A CG  1 
ATOM   1609 C CD1 . TYR A 1 197 ? 9.70846   6.97305   32.71162 1.000 40.99224 ? 197 TYR A CD1 1 
ATOM   1610 C CD2 . TYR A 1 197 ? 11.39633  8.25300   33.80399 1.000 47.94982 ? 197 TYR A CD2 1 
ATOM   1611 C CE1 . TYR A 1 197 ? 8.92201   7.00025   33.83431 1.000 54.07993 ? 197 TYR A CE1 1 
ATOM   1612 C CE2 . TYR A 1 197 ? 10.60164  8.28446   34.95761 1.000 58.06501 ? 197 TYR A CE2 1 
ATOM   1613 C CZ  . TYR A 1 197 ? 9.36365   7.65270   34.95797 1.000 54.13929 ? 197 TYR A CZ  1 
ATOM   1614 O OH  . TYR A 1 197 ? 8.54989   7.65681   36.07051 1.000 61.19659 ? 197 TYR A OH  1 
ATOM   1615 N N   . GLY A 1 198 ? 14.36985  6.30346   29.75708 1.000 18.93642 ? 198 GLY A N   1 
ATOM   1616 C CA  . GLY A 1 198 ? 15.11371  6.50791   28.53478 1.000 19.88433 ? 198 GLY A CA  1 
ATOM   1617 C C   . GLY A 1 198 ? 15.18902  7.98999   28.22520 1.000 12.45962 ? 198 GLY A C   1 
ATOM   1618 O O   . GLY A 1 198 ? 14.39221  8.79178   28.70214 1.000 18.43162 ? 198 GLY A O   1 
ATOM   1619 N N   . VAL A 1 199 ? 16.16566  8.36712   27.40893 1.000 14.30108 ? 199 VAL A N   1 
ATOM   1620 C CA  . VAL A 1 199 ? 16.25830  9.77664   27.07080 1.000 10.92690 ? 199 VAL A CA  1 
ATOM   1621 C C   . VAL A 1 199 ? 15.01307  10.16425  26.29364 1.000 13.31873 ? 199 VAL A C   1 
ATOM   1622 O O   . VAL A 1 199 ? 14.57909  9.43752   25.39215 1.000 19.51309 ? 199 VAL A O   1 
ATOM   1623 C CB  . VAL A 1 199 ? 17.53334  10.04835  26.26465 1.000 23.65557 ? 199 VAL A CB  1 
ATOM   1624 C CG1 . VAL A 1 199 ? 17.53782  11.48231  25.78764 1.000 16.57900 ? 199 VAL A CG1 1 
ATOM   1625 C CG2 . VAL A 1 199 ? 18.76840  9.73807   27.11476 1.000 28.98153 ? 199 VAL A CG2 1 
ATOM   1626 N N   . CYS A 1 200 ? 14.37800  11.27192  26.70638 1.000 22.70389 ? 200 CYS A N   1 
ATOM   1627 C CA  . CYS A 1 200 ? 13.07075  11.71686  26.18973 1.000 21.95636 ? 200 CYS A CA  1 
ATOM   1628 C C   . CYS A 1 200 ? 11.97920  10.65802  26.32608 1.000 18.83507 ? 200 CYS A C   1 
ATOM   1629 O O   . CYS A 1 200 ? 11.04328  10.61686  25.52816 1.000 19.36501 ? 200 CYS A O   1 
ATOM   1630 C CB  . CYS A 1 200 ? 13.14530  12.21713  24.73573 1.000 17.81004 ? 200 CYS A CB  1 
ATOM   1631 S SG  . CYS A 1 200 ? 14.57914  13.21420  24.31906 1.000 35.20004 ? 200 CYS A SG  1 
ATOM   1632 N N   . GLY A 1 201 ? 12.04467  9.86287   27.38740 1.000 18.73379 ? 201 GLY A N   1 
ATOM   1633 C CA  . GLY A 1 201 ? 11.04737  8.83713   27.65309 1.000 16.39984 ? 201 GLY A CA  1 
ATOM   1634 C C   . GLY A 1 201 ? 10.94207  7.81061   26.55537 1.000 15.59218 ? 201 GLY A C   1 
ATOM   1635 O O   . GLY A 1 201 ? 9.86746   7.24684   26.34035 1.000 13.42831 ? 201 GLY A O   1 
ATOM   1636 N N   . LEU A 1 202 ? 12.05917  7.50835   25.89412 1.000 15.01894 ? 202 LEU A N   1 
ATOM   1637 C CA  . LEU A 1 202 ? 12.03798  6.65637   24.71770 1.000 12.91219 ? 202 LEU A CA  1 
ATOM   1638 C C   . LEU A 1 202 ? 11.52218  5.25474   25.02916 1.000 22.91668 ? 202 LEU A C   1 
ATOM   1639 O O   . LEU A 1 202 ? 11.13019  4.53186   24.10578 1.000 34.72702 ? 202 LEU A O   1 
ATOM   1640 C CB  . LEU A 1 202 ? 13.43650  6.59683   24.08558 1.000 15.42481 ? 202 LEU A CB  1 
ATOM   1641 C CG  . LEU A 1 202 ? 13.63268  5.78246   22.81948 1.000 28.45124 ? 202 LEU A CG  1 
ATOM   1642 C CD1 . LEU A 1 202 ? 12.66660  6.35233   21.78231 1.000 21.76216 ? 202 LEU A CD1 1 
ATOM   1643 C CD2 . LEU A 1 202 ? 15.06539  5.88415   22.33975 1.000 29.30764 ? 202 LEU A CD2 1 
ATOM   1644 N N   . TYR A 1 203 ? 11.54793  4.82136   26.28776 1.000 16.47924 ? 203 TYR A N   1 
ATOM   1645 C CA  . TYR A 1 203 ? 11.12280  3.46612   26.61378 1.000 15.98564 ? 203 TYR A CA  1 
ATOM   1646 C C   . TYR A 1 203 ? 9.71748   3.45074   27.17636 1.000 11.80486 ? 203 TYR A C   1 
ATOM   1647 O O   . TYR A 1 203 ? 9.33722   2.51729   27.88789 1.000 24.20912 ? 203 TYR A O   1 
ATOM   1648 C CB  . TYR A 1 203 ? 12.08272  2.81098   27.61547 1.000 18.80416 ? 203 TYR A CB  1 
ATOM   1649 C CG  . TYR A 1 203 ? 13.55396  3.00197   27.30760 1.000 28.38724 ? 203 TYR A CG  1 
ATOM   1650 C CD1 . TYR A 1 203 ? 14.00304  3.16472   25.99319 1.000 27.59494 ? 203 TYR A CD1 1 
ATOM   1651 C CD2 . TYR A 1 203 ? 14.50329  3.02524   28.33897 1.000 25.13760 ? 203 TYR A CD2 1 
ATOM   1652 C CE1 . TYR A 1 203 ? 15.35375  3.35132   25.71863 1.000 25.34756 ? 203 TYR A CE1 1 
ATOM   1653 C CE2 . TYR A 1 203 ? 15.85077  3.20813   28.07217 1.000 26.63506 ? 203 TYR A CE2 1 
ATOM   1654 C CZ  . TYR A 1 203 ? 16.27177  3.36878   26.76003 1.000 20.90501 ? 203 TYR A CZ  1 
ATOM   1655 O OH  . TYR A 1 203 ? 17.60446  3.55691   26.48071 1.000 18.94475 ? 203 TYR A OH  1 
ATOM   1656 N N   . THR A 1 204 ? 8.91753   4.43837   26.81845 1.000 23.39033 ? 204 THR A N   1 
ATOM   1657 C CA  . THR A 1 204 ? 7.59341   4.57811   27.40500 1.000 22.01658 ? 204 THR A CA  1 
ATOM   1658 C C   . THR A 1 204 ? 6.60642   3.58273   26.81420 1.000 22.93241 ? 204 THR A C   1 
ATOM   1659 O O   . THR A 1 204 ? 5.91353   2.87428   27.54710 1.000 17.75776 ? 204 THR A O   1 
ATOM   1660 C CB  . THR A 1 204 ? 7.08514   5.99391   27.23045 1.000 22.57042 ? 204 THR A CB  1 
ATOM   1661 O OG1 . THR A 1 204 ? 7.92567   6.86626   27.98042 1.000 23.22797 ? 204 THR A OG1 1 
ATOM   1662 C CG2 . THR A 1 204 ? 5.65215   6.09936   27.78310 1.000 16.91685 ? 204 THR A CG2 1 
ATOM   1663 N N   . SER A 1 205 ? 6.50939   3.52795   25.49228 1.000 15.68956 ? 205 SER A N   1 
ATOM   1664 C CA  . SER A 1 205 ? 5.48066   2.71287   24.85587 1.000 26.20994 ? 205 SER A CA  1 
ATOM   1665 C C   . SER A 1 205 ? 6.00073   2.28481   23.49252 1.000 21.86421 ? 205 SER A C   1 
ATOM   1666 O O   . SER A 1 205 ? 6.07307   3.09611   22.56909 1.000 20.21488 ? 205 SER A O   1 
ATOM   1667 C CB  . SER A 1 205 ? 4.18138   3.52139   24.73301 1.000 19.09036 ? 205 SER A CB  1 
ATOM   1668 O OG  . SER A 1 205 ? 3.09095   2.70735   24.33957 1.000 40.19698 ? 205 SER A OG  1 
ATOM   1669 N N   . SER A 1 206 ? 6.33707   1.00809   23.35865 1.000 10.02054 ? 206 SER A N   1 
ATOM   1670 C CA  . SER A 1 206 ? 6.96451   0.53072   22.14631 1.000 12.03339 ? 206 SER A CA  1 
ATOM   1671 C C   . SER A 1 206 ? 6.25319   -0.72203  21.67807 1.000 20.12907 ? 206 SER A C   1 
ATOM   1672 O O   . SER A 1 206 ? 6.05396   -1.66289  22.45035 1.000 22.62494 ? 206 SER A O   1 
ATOM   1673 C CB  . SER A 1 206 ? 8.44896   0.23936   22.36601 1.000 15.53557 ? 206 SER A CB  1 
ATOM   1674 O OG  . SER A 1 206 ? 9.12074   1.37721   22.88506 1.000 16.42558 ? 206 SER A OG  1 
ATOM   1675 N N   . PHE A 1 207 ? 5.93040   -0.74098  20.38988 1.000 16.27500 ? 207 PHE A N   1 
ATOM   1676 C CA  . PHE A 1 207 ? 5.11060   -1.76435  19.78100 1.000 19.33396 ? 207 PHE A CA  1 
ATOM   1677 C C   . PHE A 1 207 ? 5.82517   -2.18623  18.51404 1.000 21.49199 ? 207 PHE A C   1 
ATOM   1678 O O   . PHE A 1 207 ? 6.68344   -1.46792  17.99885 1.000 17.76007 ? 207 PHE A O   1 
ATOM   1679 C CB  . PHE A 1 207 ? 3.70984   -1.21719  19.46351 1.000 15.97694 ? 207 PHE A CB  1 
ATOM   1680 C CG  . PHE A 1 207 ? 2.86597   -0.98532  20.69075 1.000 19.26775 ? 207 PHE A CG  1 
ATOM   1681 C CD1 . PHE A 1 207 ? 2.11239   -2.00443  21.25290 1.000 21.36704 ? 207 PHE A CD1 1 
ATOM   1682 C CD2 . PHE A 1 207 ? 2.87544   0.25251   21.31421 1.000 20.88913 ? 207 PHE A CD2 1 
ATOM   1683 C CE1 . PHE A 1 207 ? 1.37412   -1.78106  22.40518 1.000 16.90791 ? 207 PHE A CE1 1 
ATOM   1684 C CE2 . PHE A 1 207 ? 2.13184   0.48726   22.46047 1.000 21.78863 ? 207 PHE A CE2 1 
ATOM   1685 C CZ  . PHE A 1 207 ? 1.37940   -0.53392  23.00217 1.000 26.67602 ? 207 PHE A CZ  1 
ATOM   1686 N N   . TYR A 1 208 ? 5.39392   -3.30440  17.94970 1.000 15.37815 ? 208 TYR A N   1 
ATOM   1687 C CA  . TYR A 1 208 ? 5.94143   -3.74741  16.67748 1.000 11.39414 ? 208 TYR A CA  1 
ATOM   1688 C C   . TYR A 1 208 ? 4.97755   -4.74224  16.07258 1.000 13.69187 ? 208 TYR A C   1 
ATOM   1689 O O   . TYR A 1 208 ? 4.31363   -5.48612  16.80407 1.000 18.82965 ? 208 TYR A O   1 
ATOM   1690 C CB  . TYR A 1 208 ? 7.33505   -4.37340  16.87847 1.000 17.56990 ? 208 TYR A CB  1 
ATOM   1691 C CG  . TYR A 1 208 ? 7.42637   -5.55219  17.86117 1.000 15.06970 ? 208 TYR A CG  1 
ATOM   1692 C CD1 . TYR A 1 208 ? 7.68380   -5.32733  19.21579 1.000 26.57498 ? 208 TYR A CD1 1 
ATOM   1693 C CD2 . TYR A 1 208 ? 7.30665   -6.87690  17.43352 1.000 19.63049 ? 208 TYR A CD2 1 
ATOM   1694 C CE1 . TYR A 1 208 ? 7.78257   -6.38316  20.12893 1.000 24.24028 ? 208 TYR A CE1 1 
ATOM   1695 C CE2 . TYR A 1 208 ? 7.41426   -7.94953  18.33870 1.000 25.66285 ? 208 TYR A CE2 1 
ATOM   1696 C CZ  . TYR A 1 208 ? 7.65655   -7.68958  19.69023 1.000 31.75790 ? 208 TYR A CZ  1 
ATOM   1697 O OH  . TYR A 1 208 ? 7.75538   -8.72634  20.60896 1.000 31.70379 ? 208 TYR A OH  1 
ATOM   1698 N N   . PRO A 1 209 ? 4.87953   -4.78828  14.75582 1.000 18.29224 ? 209 PRO A N   1 
ATOM   1699 C CA  . PRO A 1 209 ? 4.02611   -5.79075  14.13938 1.000 17.31008 ? 209 PRO A CA  1 
ATOM   1700 C C   . PRO A 1 209 ? 4.61565   -7.18867  14.23519 1.000 19.90951 ? 209 PRO A C   1 
ATOM   1701 O O   . PRO A 1 209 ? 5.82896   -7.39585  14.33568 1.000 19.22911 ? 209 PRO A O   1 
ATOM   1702 C CB  . PRO A 1 209 ? 3.92495   -5.30509  12.69461 1.000 15.07255 ? 209 PRO A CB  1 
ATOM   1703 C CG  . PRO A 1 209 ? 5.21124   -4.65170  12.44696 1.000 14.01938 ? 209 PRO A CG  1 
ATOM   1704 C CD  . PRO A 1 209 ? 5.72230   -4.10991  13.75734 1.000 14.43246 ? 209 PRO A CD  1 
ATOM   1705 N N   . VAL A 1 210 ? 3.72452   -8.15548  14.18631 1.000 12.22969 ? 210 VAL A N   1 
ATOM   1706 C CA  . VAL A 1 210 ? 4.07907   -9.56043  14.14580 1.000 19.80121 ? 210 VAL A CA  1 
ATOM   1707 C C   . VAL A 1 210 ? 3.60697   -10.07271 12.79654 1.000 19.86639 ? 210 VAL A C   1 
ATOM   1708 O O   . VAL A 1 210 ? 2.47726   -9.79323  12.38189 1.000 20.94463 ? 210 VAL A O   1 
ATOM   1709 C CB  . VAL A 1 210 ? 3.42023   -10.32730 15.30135 1.000 28.53015 ? 210 VAL A CB  1 
ATOM   1710 C CG1 . VAL A 1 210 ? 3.60850   -11.84643 15.13903 1.000 37.18078 ? 210 VAL A CG1 1 
ATOM   1711 C CG2 . VAL A 1 210 ? 3.94830   -9.81783  16.61439 1.000 24.33239 ? 210 VAL A CG2 1 
ATOM   1712 N N   . LYS A 1 211 ? 4.47410   -10.79607 12.10761 1.000 36.16109 ? 211 LYS A N   1 
ATOM   1713 C CA  . LYS A 1 211 ? 4.15716   -11.40939 10.82661 1.000 31.51813 ? 211 LYS A CA  1 
ATOM   1714 C C   . LYS A 1 211 ? 4.81384   -12.77666 10.81352 1.000 52.81077 ? 211 LYS A C   1 
ATOM   1715 O O   . LYS A 1 211 ? 6.03496   -12.88989 10.96701 1.000 48.78593 ? 211 LYS A O   1 
ATOM   1716 C CB  . LYS A 1 211 ? 4.59346   -10.54902 9.64412  1.000 25.18600 ? 211 LYS A CB  1 
ATOM   1717 C CG  . LYS A 1 211 ? 4.14976   -11.14520 8.33440  1.000 41.79932 ? 211 LYS A CG  1 
ATOM   1718 C CD  . LYS A 1 211 ? 3.97402   -10.13220 7.24350  1.000 30.73836 ? 211 LYS A CD  1 
ATOM   1719 C CE  . LYS A 1 211 ? 3.57164   -10.83447 5.94336  1.000 56.30695 ? 211 LYS A CE  1 
ATOM   1720 N NZ  . LYS A 1 211 ? 2.12427   -11.19686 5.83793  1.000 18.78745 ? 211 LYS A NZ  1 
ATOM   1721 N N   . ASN A 1 212 ? 3.99399   -13.80058 10.62727 1.000 53.89075 ? 212 ASN A N   1 
ATOM   1722 C CA  . ASN A 1 212 ? 4.43026   -15.18420 10.58257 1.000 64.49543 ? 212 ASN A CA  1 
ATOM   1723 C C   . ASN A 1 212 ? 5.11543   -15.52699 9.26095  1.000 77.85064 ? 212 ASN A C   1 
ATOM   1724 O O   . ASN A 1 212 ? 5.97741   -16.40720 9.21249  1.000 81.22440 ? 212 ASN A O   1 
ATOM   1725 C CB  . ASN A 1 212 ? 3.19668   -16.06202 10.76357 1.000 51.22554 ? 212 ASN A CB  1 
ATOM   1726 C CG  . ASN A 1 212 ? 2.66612   -16.02058 12.17848 1.000 70.96262 ? 212 ASN A CG  1 
ATOM   1727 O OD1 . ASN A 1 212 ? 3.40832   -15.75012 13.12991 1.000 45.32007 ? 212 ASN A OD1 1 
ATOM   1728 N ND2 . ASN A 1 212 ? 1.34980   -16.20572 12.31668 1.000 48.84103 ? 212 ASN A ND2 1 
ATOM   1729 O OXT . ASN A 1 212 ? 4.84290   -14.92738 8.21729  1.000 69.99179 ? 212 ASN A OXT 1 
HETATM 1730 O O1  . E6C B 2 .   ? 0.52050   14.53763  18.01292 0.811 36.77002 ? 301 E6C A O1  1 
HETATM 1731 C C2  . E6C B 2 .   ? 2.34988   13.10608  17.18246 0.811 45.76994 ? 301 E6C A C2  1 
HETATM 1732 C C3  . E6C B 2 .   ? 0.84745   13.29667  17.44362 0.811 36.19800 ? 301 E6C A C3  1 
HETATM 1733 C C4  . E6C B 2 .   ? 0.40482   12.10959  18.31321 0.811 40.51567 ? 301 E6C A C4  1 
HETATM 1734 O O5  . E6C B 2 .   ? -0.29876  11.22446  17.85938 0.811 42.36611 ? 301 E6C A O5  1 
HETATM 1735 N N6  . E6C B 2 .   ? 0.84313   12.02392  19.58357 0.811 42.08722 ? 301 E6C A N6  1 
HETATM 1736 C C7  . E6C B 2 .   ? 0.43875   10.89760  20.39575 0.811 42.96523 ? 301 E6C A C7  1 
HETATM 1737 C C8  . E6C B 2 .   ? -0.71139  11.30043  21.32871 0.811 33.25240 ? 301 E6C A C8  1 
HETATM 1738 O O9  . E6C B 2 .   ? -0.65377  12.31315  22.01043 0.811 47.66679 ? 301 E6C A O9  1 
HETATM 1739 N N10 . E6C B 2 .   ? -1.76148  10.46431  21.31643 0.811 34.48985 ? 301 E6C A N10 1 
HETATM 1740 C C11 . E6C B 2 .   ? -2.96136  10.64590  22.11052 0.811 38.15667 ? 301 E6C A C11 1 
HETATM 1741 C C12 . E6C B 2 .   ? -4.11863  11.10668  21.23713 0.811 23.78960 ? 301 E6C A C12 1 
HETATM 1742 C C13 . E6C B 2 .   ? -4.63107  12.51112  21.57812 0.811 60.84805 ? 301 E6C A C13 1 
HETATM 1743 C C14 . E6C B 2 .   ? -5.13051  12.56835  23.02200 0.811 52.04029 ? 301 E6C A C14 1 
HETATM 1744 C C15 . E6C B 2 .   ? -3.61548  13.62765  21.29381 0.811 38.55530 ? 301 E6C A C15 1 
HETATM 1745 C C16 . E6C B 2 .   ? 3.00850   14.03256  16.14169 0.811 41.26239 ? 301 E6C A C16 1 
HETATM 1746 O O17 . E6C B 2 .   ? 4.09997   14.54309  16.47440 0.811 29.92435 ? 301 E6C A O17 1 
HETATM 1747 O O18 . E6C B 2 .   ? 2.39697   14.18293  15.06400 0.811 24.37245 ? 301 E6C A O18 1 
HETATM 1748 C C19 . E6C B 2 .   ? 1.61102   10.31155  21.19784 0.811 41.17387 ? 301 E6C A C19 1 
HETATM 1749 C C20 . E6C B 2 .   ? 1.28871   9.03108   21.98591 0.811 30.77684 ? 301 E6C A C20 1 
HETATM 1750 C C21 . E6C B 2 .   ? 1.05779   7.86984   21.02571 0.811 40.36639 ? 301 E6C A C21 1 
HETATM 1751 C C22 . E6C B 2 .   ? 2.36155   8.67801   23.01216 0.811 35.18380 ? 301 E6C A C22 1 
HETATM 1752 O O   . HOH C 3 .   ? 8.94784   4.06888   23.44036 1.000 18.08209 ? 401 HOH A O   1 
HETATM 1753 O O   . HOH C 3 .   ? 4.19636   16.03999  18.26895 1.000 20.18525 ? 402 HOH A O   1 
HETATM 1754 O O   . HOH C 3 .   ? 10.99908  0.41724   7.41691  1.000 14.96388 ? 403 HOH A O   1 
HETATM 1755 O O   . HOH C 3 .   ? 7.13493   9.72465   13.10105 1.000 8.23500  ? 404 HOH A O   1 
HETATM 1756 O O   . HOH C 3 .   ? 6.72443   -0.64547  25.71084 1.000 16.43192 ? 405 HOH A O   1 
HETATM 1757 O O   . HOH C 3 .   ? 11.28365  -0.90285  27.29059 1.000 13.78601 ? 406 HOH A O   1 
HETATM 1758 O O   . HOH C 3 .   ? 20.97789  9.62415   9.20038  1.000 12.85460 ? 407 HOH A O   1 
HETATM 1759 O O   . HOH C 3 .   ? 17.91099  6.03728   26.32679 1.000 10.90038 ? 408 HOH A O   1 
HETATM 1760 O O   . HOH C 3 .   ? -5.22245  9.43753   -0.32028 1.000 13.68905 ? 409 HOH A O   1 
HETATM 1761 O O   . HOH C 3 .   ? 8.82372   -3.96024  12.39907 1.000 16.23354 ? 410 HOH A O   1 
HETATM 1762 O O   . HOH C 3 .   ? 2.85210   -5.81660  -0.15855 1.000 19.66789 ? 411 HOH A O   1 
HETATM 1763 O O   . HOH C 3 .   ? 9.49804   -6.82571  25.76832 1.000 17.00478 ? 412 HOH A O   1 
HETATM 1764 O O   . HOH C 3 .   ? -17.299   2.503     11.787   1.000 23.58055 ? 413 HOH A O   1 
HETATM 1765 O O   . HOH C 3 .   ? 15.09948  6.18085   4.70181  1.000 14.86949 ? 414 HOH A O   1 
HETATM 1766 O O   . HOH C 3 .   ? -2.43929  -0.89484  -2.54561 1.000 12.16150 ? 415 HOH A O   1 
HETATM 1767 O O   . HOH C 3 .   ? 8.84239   7.61916   11.96745 1.000 6.44104  ? 416 HOH A O   1 
HETATM 1768 O O   . HOH C 3 .   ? 1.18863   14.70374  21.11360 1.000 27.51929 ? 417 HOH A O   1 
HETATM 1769 O O   . HOH C 3 .   ? 8.28028   -3.52225  2.44840  1.000 17.30362 ? 418 HOH A O   1 
HETATM 1770 O O   . HOH C 3 .   ? 12.26670  13.54827  10.06500 1.000 18.54477 ? 419 HOH A O   1 
HETATM 1771 O O   . HOH C 3 .   ? 16.09230  0.24916   30.96473 1.000 19.29711 ? 420 HOH A O   1 
HETATM 1772 O O   . HOH C 3 .   ? 7.00785   -11.43642 13.02750 1.000 21.96052 ? 421 HOH A O   1 
HETATM 1773 O O   . HOH C 3 .   ? -11.76040 7.81126   17.48532 1.000 27.44022 ? 422 HOH A O   1 
HETATM 1774 O O   . HOH C 3 .   ? 7.36093   -9.54925  15.43168 1.000 26.70113 ? 423 HOH A O   1 
HETATM 1775 O O   . HOH C 3 .   ? -10.70661 9.21962   14.03361 1.000 16.48606 ? 424 HOH A O   1 
HETATM 1776 O O   . HOH C 3 .   ? 11.52204  15.29918  3.25172  1.000 16.30927 ? 425 HOH A O   1 
HETATM 1777 O O   . HOH C 3 .   ? -0.21338  7.46449   2.55982  1.000 19.43104 ? 426 HOH A O   1 
HETATM 1778 O O   . HOH C 3 .   ? 11.80982  -7.47356  23.58955 1.000 14.27306 ? 427 HOH A O   1 
HETATM 1779 O O   . HOH C 3 .   ? -10.894   6.586     -3.470   1.000 11.38031 ? 428 HOH A O   1 
HETATM 1780 O O   . HOH C 3 .   ? 10.43171  2.79567   6.59798  1.000 16.35753 ? 429 HOH A O   1 
HETATM 1781 O O   . HOH C 3 .   ? 9.58986   0.59071   25.53638 1.000 19.47724 ? 430 HOH A O   1 
HETATM 1782 O O   . HOH C 3 .   ? 2.06716   9.67713   -0.56646 1.000 25.63733 ? 431 HOH A O   1 
HETATM 1783 O O   . HOH C 3 .   ? 21.75475  -4.01146  10.72845 1.000 15.83307 ? 432 HOH A O   1 
HETATM 1784 O O   . HOH C 3 .   ? 28.33594  -7.05993  17.43414 1.000 24.11839 ? 433 HOH A O   1 
HETATM 1785 O O   . HOH C 3 .   ? 4.76779   2.92920   19.97431 1.000 19.05626 ? 434 HOH A O   1 
HETATM 1786 O O   . HOH C 3 .   ? -12.36006 -4.01861  -1.91332 1.000 28.04528 ? 435 HOH A O   1 
HETATM 1787 O O   . HOH C 3 .   ? 25.68706  13.54056  23.53862 1.000 20.56235 ? 436 HOH A O   1 
HETATM 1788 O O   . HOH C 3 .   ? 26.30870  5.81420   14.35639 1.000 14.03333 ? 437 HOH A O   1 
HETATM 1789 O O   . HOH C 3 .   ? 19.06224  5.17576   28.60187 1.000 17.42768 ? 438 HOH A O   1 
HETATM 1790 O O   . HOH C 3 .   ? 0.86703   -9.69114  3.36936  1.000 11.01083 ? 439 HOH A O   1 
HETATM 1791 O O   . HOH C 3 .   ? 2.16881   4.20110   21.61093 1.000 12.69196 ? 440 HOH A O   1 
HETATM 1792 O O   . HOH C 3 .   ? 31.63434  6.13831   25.62095 1.000 15.72659 ? 441 HOH A O   1 
# 
