data_9NC1
# 
_entry.id   9NC1 
# 
_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   9NC1         pdb_00009nc1 10.2210/pdb9nc1/pdb 
WWPDB D_1000293030 ?            ?                   
# 
_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                        9NC1 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-14 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        'MicroED structure of the same protein in apo-form' 
_pdbx_database_related.db_id          9NAG 
_pdbx_database_related.content_type   unspecified 
# 
_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 ? 
'Rodriguez, J.A.' 2 ? 
# 
_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 nat 'N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE' 360.429   1  ?        ? ? ? 
3 water       nat water                                                               18.015    12 ?        ? ? ? 
# 
_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-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE' E64 
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 
E64 non-polymer         . 'N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE' ? 'C15 H30 N5 O5 1' 360.429 
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        E64 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   E64 
_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 E64 1  301 301 E64 E64 A . 
C 3 HOH 1  401 11  HOH HOH A . 
C 3 HOH 2  402 8   HOH HOH A . 
C 3 HOH 3  403 6   HOH HOH A . 
C 3 HOH 4  404 7   HOH HOH A . 
C 3 HOH 5  405 4   HOH HOH A . 
C 3 HOH 6  406 2   HOH HOH A . 
C 3 HOH 7  407 1   HOH HOH A . 
C 3 HOH 8  408 3   HOH HOH A . 
C 3 HOH 9  409 12  HOH HOH A . 
C 3 HOH 10 410 10  HOH HOH A . 
C 3 HOH 11 411 5   HOH HOH A . 
C 3 HOH 12 412 9   HOH HOH A . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NC1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.570 
_cell.length_a_esd                 ? 
_cell.length_b                     48.850 
_cell.length_b_esd                 ? 
_cell.length_c                     99.860 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9NC1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_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                   9NC1 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON CRYSTALLOGRAPHY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NC1 
_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                            2.40 
_refine.ls_d_res_low                             49.93 
_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                     8197 
_refine.ls_number_reflns_R_free                  819 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.21 
_refine.ls_percent_reflns_R_free                 9.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2090 
_refine.ls_R_factor_R_free                       0.2609 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2033 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.77 
_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                            0.33 
_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                    ? 
# 
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' ? 0.006 ? 1723 ? f_bond_d           ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.914 ? 2338 ? f_angle_d          ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 6.844 ? 250  ? f_dihedral_angle_d ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.066 ? 235  ? f_chiral_restr     ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.008 ? 307  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'ELECTRON CRYSTALLOGRAPHY' 2.40 2.55  . . 134 1205 97.00 . . . . 0.2852 . . . . . . . . . . . . . . . 0.3433 
'ELECTRON CRYSTALLOGRAPHY' 2.55 2.75  . . 135 1220 96.00 . . . . 0.2673 . . . . . . . . . . . . . . . 0.3389 
'ELECTRON CRYSTALLOGRAPHY' 2.75 3.02  . . 138 1239 97.00 . . . . 0.2271 . . . . . . . . . . . . . . . 0.3297 
'ELECTRON CRYSTALLOGRAPHY' 3.02 3.46  . . 136 1230 96.00 . . . . 0.2120 . . . . . . . . . . . . . . . 0.2451 
'ELECTRON CRYSTALLOGRAPHY' 3.46 4.36  . . 137 1231 94.00 . . . . 0.1568 . . . . . . . . . . . . . . . 0.2386 
'ELECTRON CRYSTALLOGRAPHY' 4.36 49.93 . . 139 1253 91.00 . . . . 0.1753 . . . . . . . . . . . . . . . 0.2012 
# 
_struct.entry_id                     9NC1 
_struct.title                        
'MicroED structure of papain-E-64 complex from microcrystals soaked with protease inhibitor cocktail' 
_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        9NC1 
_struct_keywords.text            'Inhibitor, Complex, MicroED, Cocktail, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/INHIBITOR 
# 
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              9NC1 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 640  ? 
1 MORE         3    ? 
1 'SSA (A^2)'  9350 ? 
# 
_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 ? ? ? ? ? ? ? 2.040 ? ? 
disulf2 disulf ?    ? A CYS 56  SG ? ? ? 1_555 A CYS 95  SG ? ? A CYS 56  A CYS 95  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf3 disulf ?    ? A CYS 153 SG ? ? ? 1_555 A CYS 200 SG ? ? A CYS 153 A CYS 200 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
covale1 covale none ? A CYS 25  SG ? ? ? 1_555 B E64 .   C2 ? ? A CYS 25  A E64 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 E64 B .   ? CYS A 25  ? E64 A 301 ? 1_555 CYS A 25  ? 1_555 C2 SG CYS 1 E64 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       3.75 
# 
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 ARG A 111 ? N ARG A 111 O TYR A 208 ? O TYR A 208 
# 
_pdbx_entry_details.entry_id                   9NC1 
_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    ASP 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     158 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -152.56 
_pdbx_validate_torsion.psi             7.37 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9NC1 
_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                    9NC1 
_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                  2.4 
_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-64 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                        9NC1 
_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             10000 
_em_imaging.nominal_defocus_max             10000 
_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_imaging.objective_aperture              ? 
_em_imaging.microscope_serial_number        ? 
_em_imaging.microscope_version              ? 
# 
_em_vitrification.entry_id              9NC1 
_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                9NC1 
_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  
E64 C1   C N N 88  
E64 O1   O N N 89  
E64 O2   O N N 90  
E64 C2   C N N 91  
E64 C3   C N S 92  
E64 O3   O N N 93  
E64 C4   C N N 94  
E64 O4   O N N 95  
E64 N1   N N N 96  
E64 C6   C N S 97  
E64 C7   C N N 98  
E64 C8   C N N 99  
E64 C9   C N N 100 
E64 C10  C N N 101 
E64 C11  C N N 102 
E64 O5   O N N 103 
E64 N2   N N N 104 
E64 C12  C N N 105 
E64 C13  C N N 106 
E64 C14  C N N 107 
E64 C15  C N N 108 
E64 N3   N N N 109 
E64 C16  C N N 110 
E64 N4   N N N 111 
E64 N5   N N N 112 
E64 HO2  H N N 113 
E64 H21  H N N 114 
E64 H22  H N N 115 
E64 H3   H N N 116 
E64 HO3  H N N 117 
E64 HN1  H N N 118 
E64 H6   H N N 119 
E64 H71  H N N 120 
E64 H72  H N N 121 
E64 H8   H N N 122 
E64 H91  H N N 123 
E64 H92  H N N 124 
E64 H93  H N N 125 
E64 H101 H N N 126 
E64 H102 H N N 127 
E64 H103 H N N 128 
E64 HN2  H N N 129 
E64 H121 H N N 130 
E64 H122 H N N 131 
E64 H131 H N N 132 
E64 H132 H N N 133 
E64 H141 H N N 134 
E64 H142 H N N 135 
E64 H151 H N N 136 
E64 H152 H N N 137 
E64 HN3  H N N 138 
E64 HN41 H N N 139 
E64 HN42 H N N 140 
E64 HN51 H N N 141 
E64 HN52 H N N 142 
GLN N    N N N 143 
GLN CA   C N S 144 
GLN C    C N N 145 
GLN O    O N N 146 
GLN CB   C N N 147 
GLN CG   C N N 148 
GLN CD   C N N 149 
GLN OE1  O N N 150 
GLN NE2  N N N 151 
GLN OXT  O N N 152 
GLN H    H N N 153 
GLN H2   H N N 154 
GLN HA   H N N 155 
GLN HB2  H N N 156 
GLN HB3  H N N 157 
GLN HG2  H N N 158 
GLN HG3  H N N 159 
GLN HE21 H N N 160 
GLN HE22 H N N 161 
GLN HXT  H N N 162 
GLU N    N N N 163 
GLU CA   C N S 164 
GLU C    C N N 165 
GLU O    O N N 166 
GLU CB   C N N 167 
GLU CG   C N N 168 
GLU CD   C N N 169 
GLU OE1  O N N 170 
GLU OE2  O N N 171 
GLU OXT  O N N 172 
GLU H    H N N 173 
GLU H2   H N N 174 
GLU HA   H N N 175 
GLU HB2  H N N 176 
GLU HB3  H N N 177 
GLU HG2  H N N 178 
GLU HG3  H N N 179 
GLU HE2  H N N 180 
GLU HXT  H N N 181 
GLY N    N N N 182 
GLY CA   C N N 183 
GLY C    C N N 184 
GLY O    O N N 185 
GLY OXT  O N N 186 
GLY H    H N N 187 
GLY H2   H N N 188 
GLY HA2  H N N 189 
GLY HA3  H N N 190 
GLY HXT  H N N 191 
HIS N    N N N 192 
HIS CA   C N S 193 
HIS C    C N N 194 
HIS O    O N N 195 
HIS CB   C N N 196 
HIS CG   C Y N 197 
HIS ND1  N Y N 198 
HIS CD2  C Y N 199 
HIS CE1  C Y N 200 
HIS NE2  N Y N 201 
HIS OXT  O N N 202 
HIS H    H N N 203 
HIS H2   H N N 204 
HIS HA   H N N 205 
HIS HB2  H N N 206 
HIS HB3  H N N 207 
HIS HD1  H N N 208 
HIS HD2  H N N 209 
HIS HE1  H N N 210 
HIS HE2  H N N 211 
HIS HXT  H N N 212 
HOH O    O N N 213 
HOH H1   H N N 214 
HOH H2   H N N 215 
ILE N    N N N 216 
ILE CA   C N S 217 
ILE C    C N N 218 
ILE O    O N N 219 
ILE CB   C N S 220 
ILE CG1  C N N 221 
ILE CG2  C N N 222 
ILE CD1  C N N 223 
ILE OXT  O N N 224 
ILE H    H N N 225 
ILE H2   H N N 226 
ILE HA   H N N 227 
ILE HB   H N N 228 
ILE HG12 H N N 229 
ILE HG13 H N N 230 
ILE HG21 H N N 231 
ILE HG22 H N N 232 
ILE HG23 H N N 233 
ILE HD11 H N N 234 
ILE HD12 H N N 235 
ILE HD13 H N N 236 
ILE HXT  H N N 237 
LEU N    N N N 238 
LEU CA   C N S 239 
LEU C    C N N 240 
LEU O    O N N 241 
LEU CB   C N N 242 
LEU CG   C N N 243 
LEU CD1  C N N 244 
LEU CD2  C N N 245 
LEU OXT  O N N 246 
LEU H    H N N 247 
LEU H2   H N N 248 
LEU HA   H N N 249 
LEU HB2  H N N 250 
LEU HB3  H N N 251 
LEU HG   H N N 252 
LEU HD11 H N N 253 
LEU HD12 H N N 254 
LEU HD13 H N N 255 
LEU HD21 H N N 256 
LEU HD22 H N N 257 
LEU HD23 H N N 258 
LEU HXT  H N N 259 
LYS N    N N N 260 
LYS CA   C N S 261 
LYS C    C N N 262 
LYS O    O N N 263 
LYS CB   C N N 264 
LYS CG   C N N 265 
LYS CD   C N N 266 
LYS CE   C N N 267 
LYS NZ   N N N 268 
LYS OXT  O N N 269 
LYS H    H N N 270 
LYS H2   H N N 271 
LYS HA   H N N 272 
LYS HB2  H N N 273 
LYS HB3  H N N 274 
LYS HG2  H N N 275 
LYS HG3  H N N 276 
LYS HD2  H N N 277 
LYS HD3  H N N 278 
LYS HE2  H N N 279 
LYS HE3  H N N 280 
LYS HZ1  H N N 281 
LYS HZ2  H N N 282 
LYS HZ3  H N N 283 
LYS HXT  H N N 284 
PHE N    N N N 285 
PHE CA   C N S 286 
PHE C    C N N 287 
PHE O    O N N 288 
PHE CB   C N N 289 
PHE CG   C Y N 290 
PHE CD1  C Y N 291 
PHE CD2  C Y N 292 
PHE CE1  C Y N 293 
PHE CE2  C Y N 294 
PHE CZ   C Y N 295 
PHE OXT  O N N 296 
PHE H    H N N 297 
PHE H2   H N N 298 
PHE HA   H N N 299 
PHE HB2  H N N 300 
PHE HB3  H N N 301 
PHE HD1  H N N 302 
PHE HD2  H N N 303 
PHE HE1  H N N 304 
PHE HE2  H N N 305 
PHE HZ   H N N 306 
PHE HXT  H N N 307 
PRO N    N N N 308 
PRO CA   C N S 309 
PRO C    C N N 310 
PRO O    O N N 311 
PRO CB   C N N 312 
PRO CG   C N N 313 
PRO CD   C N N 314 
PRO OXT  O N N 315 
PRO H    H N N 316 
PRO HA   H N N 317 
PRO HB2  H N N 318 
PRO HB3  H N N 319 
PRO HG2  H N N 320 
PRO HG3  H N N 321 
PRO HD2  H N N 322 
PRO HD3  H N N 323 
PRO HXT  H N N 324 
SER N    N N N 325 
SER CA   C N S 326 
SER C    C N N 327 
SER O    O N N 328 
SER CB   C N N 329 
SER OG   O N N 330 
SER OXT  O N N 331 
SER H    H N N 332 
SER H2   H N N 333 
SER HA   H N N 334 
SER HB2  H N N 335 
SER HB3  H N N 336 
SER HG   H N N 337 
SER HXT  H N N 338 
THR N    N N N 339 
THR CA   C N S 340 
THR C    C N N 341 
THR O    O N N 342 
THR CB   C N R 343 
THR OG1  O N N 344 
THR CG2  C N N 345 
THR OXT  O N N 346 
THR H    H N N 347 
THR H2   H N N 348 
THR HA   H N N 349 
THR HB   H N N 350 
THR HG1  H N N 351 
THR HG21 H N N 352 
THR HG22 H N N 353 
THR HG23 H N N 354 
THR HXT  H N N 355 
TRP N    N N N 356 
TRP CA   C N S 357 
TRP C    C N N 358 
TRP O    O N N 359 
TRP CB   C N N 360 
TRP CG   C Y N 361 
TRP CD1  C Y N 362 
TRP CD2  C Y N 363 
TRP NE1  N Y N 364 
TRP CE2  C Y N 365 
TRP CE3  C Y N 366 
TRP CZ2  C Y N 367 
TRP CZ3  C Y N 368 
TRP CH2  C Y N 369 
TRP OXT  O N N 370 
TRP H    H N N 371 
TRP H2   H N N 372 
TRP HA   H N N 373 
TRP HB2  H N N 374 
TRP HB3  H N N 375 
TRP HD1  H N N 376 
TRP HE1  H N N 377 
TRP HE3  H N N 378 
TRP HZ2  H N N 379 
TRP HZ3  H N N 380 
TRP HH2  H N N 381 
TRP HXT  H N N 382 
TYR N    N N N 383 
TYR CA   C N S 384 
TYR C    C N N 385 
TYR O    O N N 386 
TYR CB   C N N 387 
TYR CG   C Y N 388 
TYR CD1  C Y N 389 
TYR CD2  C Y N 390 
TYR CE1  C Y N 391 
TYR CE2  C Y N 392 
TYR CZ   C Y N 393 
TYR OH   O N N 394 
TYR OXT  O N N 395 
TYR H    H N N 396 
TYR H2   H N N 397 
TYR HA   H N N 398 
TYR HB2  H N N 399 
TYR HB3  H N N 400 
TYR HD1  H N N 401 
TYR HD2  H N N 402 
TYR HE1  H N N 403 
TYR HE2  H N N 404 
TYR HH   H N N 405 
TYR HXT  H N N 406 
VAL N    N N N 407 
VAL CA   C N S 408 
VAL C    C N N 409 
VAL O    O N N 410 
VAL CB   C N N 411 
VAL CG1  C N N 412 
VAL CG2  C N N 413 
VAL OXT  O N N 414 
VAL H    H N N 415 
VAL H2   H N N 416 
VAL HA   H N N 417 
VAL HB   H N N 418 
VAL HG11 H N N 419 
VAL HG12 H N N 420 
VAL HG13 H N N 421 
VAL HG21 H N N 422 
VAL HG22 H N N 423 
VAL HG23 H N N 424 
VAL HXT  H N N 425 
# 
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  
E64 C1  O1   doub N N 83  
E64 C1  O2   sing N N 84  
E64 C1  C2   sing N N 85  
E64 O2  HO2  sing N N 86  
E64 C2  C3   sing N N 87  
E64 C2  H21  sing N N 88  
E64 C2  H22  sing N N 89  
E64 C3  O3   sing N N 90  
E64 C3  C4   sing N N 91  
E64 C3  H3   sing N N 92  
E64 O3  HO3  sing N N 93  
E64 C4  O4   doub N N 94  
E64 C4  N1   sing N N 95  
E64 N1  C6   sing N N 96  
E64 N1  HN1  sing N N 97  
E64 C6  C7   sing N N 98  
E64 C6  C11  sing N N 99  
E64 C6  H6   sing N N 100 
E64 C7  C8   sing N N 101 
E64 C7  H71  sing N N 102 
E64 C7  H72  sing N N 103 
E64 C8  C9   sing N N 104 
E64 C8  C10  sing N N 105 
E64 C8  H8   sing N N 106 
E64 C9  H91  sing N N 107 
E64 C9  H92  sing N N 108 
E64 C9  H93  sing N N 109 
E64 C10 H101 sing N N 110 
E64 C10 H102 sing N N 111 
E64 C10 H103 sing N N 112 
E64 C11 O5   doub N N 113 
E64 C11 N2   sing N N 114 
E64 N2  C12  sing N N 115 
E64 N2  HN2  sing N N 116 
E64 C12 C13  sing N N 117 
E64 C12 H121 sing N N 118 
E64 C12 H122 sing N N 119 
E64 C13 C14  sing N N 120 
E64 C13 H131 sing N N 121 
E64 C13 H132 sing N N 122 
E64 C14 C15  sing N N 123 
E64 C14 H141 sing N N 124 
E64 C14 H142 sing N N 125 
E64 C15 N3   sing N N 126 
E64 C15 H151 sing N N 127 
E64 C15 H152 sing N N 128 
E64 N3  C16  sing N N 129 
E64 N3  HN3  sing N N 130 
E64 C16 N4   sing N N 131 
E64 C16 N5   doub N N 132 
E64 N4  HN41 sing N N 133 
E64 N4  HN42 sing N N 134 
E64 N5  HN51 sing N N 135 
E64 N5  HN52 sing N N 136 
GLN N   CA   sing N N 137 
GLN N   H    sing N N 138 
GLN N   H2   sing N N 139 
GLN CA  C    sing N N 140 
GLN CA  CB   sing N N 141 
GLN CA  HA   sing N N 142 
GLN C   O    doub N N 143 
GLN C   OXT  sing N N 144 
GLN CB  CG   sing N N 145 
GLN CB  HB2  sing N N 146 
GLN CB  HB3  sing N N 147 
GLN CG  CD   sing N N 148 
GLN CG  HG2  sing N N 149 
GLN CG  HG3  sing N N 150 
GLN CD  OE1  doub N N 151 
GLN CD  NE2  sing N N 152 
GLN NE2 HE21 sing N N 153 
GLN NE2 HE22 sing N N 154 
GLN OXT HXT  sing N N 155 
GLU N   CA   sing N N 156 
GLU N   H    sing N N 157 
GLU N   H2   sing N N 158 
GLU CA  C    sing N N 159 
GLU CA  CB   sing N N 160 
GLU CA  HA   sing N N 161 
GLU C   O    doub N N 162 
GLU C   OXT  sing N N 163 
GLU CB  CG   sing N N 164 
GLU CB  HB2  sing N N 165 
GLU CB  HB3  sing N N 166 
GLU CG  CD   sing N N 167 
GLU CG  HG2  sing N N 168 
GLU CG  HG3  sing N N 169 
GLU CD  OE1  doub N N 170 
GLU CD  OE2  sing N N 171 
GLU OE2 HE2  sing N N 172 
GLU OXT HXT  sing N N 173 
GLY N   CA   sing N N 174 
GLY N   H    sing N N 175 
GLY N   H2   sing N N 176 
GLY CA  C    sing N N 177 
GLY CA  HA2  sing N N 178 
GLY CA  HA3  sing N N 179 
GLY C   O    doub N N 180 
GLY C   OXT  sing N N 181 
GLY OXT HXT  sing N N 182 
HIS N   CA   sing N N 183 
HIS N   H    sing N N 184 
HIS N   H2   sing N N 185 
HIS CA  C    sing N N 186 
HIS CA  CB   sing N N 187 
HIS CA  HA   sing N N 188 
HIS C   O    doub N N 189 
HIS C   OXT  sing N N 190 
HIS CB  CG   sing N N 191 
HIS CB  HB2  sing N N 192 
HIS CB  HB3  sing N N 193 
HIS CG  ND1  sing Y N 194 
HIS CG  CD2  doub Y N 195 
HIS ND1 CE1  doub Y N 196 
HIS ND1 HD1  sing N N 197 
HIS CD2 NE2  sing Y N 198 
HIS CD2 HD2  sing N N 199 
HIS CE1 NE2  sing Y N 200 
HIS CE1 HE1  sing N N 201 
HIS NE2 HE2  sing N N 202 
HIS OXT HXT  sing N N 203 
HOH O   H1   sing N N 204 
HOH O   H2   sing N N 205 
ILE N   CA   sing N N 206 
ILE N   H    sing N N 207 
ILE N   H2   sing N N 208 
ILE CA  C    sing N N 209 
ILE CA  CB   sing N N 210 
ILE CA  HA   sing N N 211 
ILE C   O    doub N N 212 
ILE C   OXT  sing N N 213 
ILE CB  CG1  sing N N 214 
ILE CB  CG2  sing N N 215 
ILE CB  HB   sing N N 216 
ILE CG1 CD1  sing N N 217 
ILE CG1 HG12 sing N N 218 
ILE CG1 HG13 sing N N 219 
ILE CG2 HG21 sing N N 220 
ILE CG2 HG22 sing N N 221 
ILE CG2 HG23 sing N N 222 
ILE CD1 HD11 sing N N 223 
ILE CD1 HD12 sing N N 224 
ILE CD1 HD13 sing N N 225 
ILE OXT HXT  sing N N 226 
LEU N   CA   sing N N 227 
LEU N   H    sing N N 228 
LEU N   H2   sing N N 229 
LEU CA  C    sing N N 230 
LEU CA  CB   sing N N 231 
LEU CA  HA   sing N N 232 
LEU C   O    doub N N 233 
LEU C   OXT  sing N N 234 
LEU CB  CG   sing N N 235 
LEU CB  HB2  sing N N 236 
LEU CB  HB3  sing N N 237 
LEU CG  CD1  sing N N 238 
LEU CG  CD2  sing N N 239 
LEU CG  HG   sing N N 240 
LEU CD1 HD11 sing N N 241 
LEU CD1 HD12 sing N N 242 
LEU CD1 HD13 sing N N 243 
LEU CD2 HD21 sing N N 244 
LEU CD2 HD22 sing N N 245 
LEU CD2 HD23 sing N N 246 
LEU OXT HXT  sing N N 247 
LYS N   CA   sing N N 248 
LYS N   H    sing N N 249 
LYS N   H2   sing N N 250 
LYS CA  C    sing N N 251 
LYS CA  CB   sing N N 252 
LYS CA  HA   sing N N 253 
LYS C   O    doub N N 254 
LYS C   OXT  sing N N 255 
LYS CB  CG   sing N N 256 
LYS CB  HB2  sing N N 257 
LYS CB  HB3  sing N N 258 
LYS CG  CD   sing N N 259 
LYS CG  HG2  sing N N 260 
LYS CG  HG3  sing N N 261 
LYS CD  CE   sing N N 262 
LYS CD  HD2  sing N N 263 
LYS CD  HD3  sing N N 264 
LYS CE  NZ   sing N N 265 
LYS CE  HE2  sing N N 266 
LYS CE  HE3  sing N N 267 
LYS NZ  HZ1  sing N N 268 
LYS NZ  HZ2  sing N N 269 
LYS NZ  HZ3  sing N N 270 
LYS OXT HXT  sing N N 271 
PHE N   CA   sing N N 272 
PHE N   H    sing N N 273 
PHE N   H2   sing N N 274 
PHE CA  C    sing N N 275 
PHE CA  CB   sing N N 276 
PHE CA  HA   sing N N 277 
PHE C   O    doub N N 278 
PHE C   OXT  sing N N 279 
PHE CB  CG   sing N N 280 
PHE CB  HB2  sing N N 281 
PHE CB  HB3  sing N N 282 
PHE CG  CD1  doub Y N 283 
PHE CG  CD2  sing Y N 284 
PHE CD1 CE1  sing Y N 285 
PHE CD1 HD1  sing N N 286 
PHE CD2 CE2  doub Y N 287 
PHE CD2 HD2  sing N N 288 
PHE CE1 CZ   doub Y N 289 
PHE CE1 HE1  sing N N 290 
PHE CE2 CZ   sing Y N 291 
PHE CE2 HE2  sing N N 292 
PHE CZ  HZ   sing N N 293 
PHE OXT HXT  sing N N 294 
PRO N   CA   sing N N 295 
PRO N   CD   sing N N 296 
PRO N   H    sing N N 297 
PRO CA  C    sing N N 298 
PRO CA  CB   sing N N 299 
PRO CA  HA   sing N N 300 
PRO C   O    doub N N 301 
PRO C   OXT  sing N N 302 
PRO CB  CG   sing N N 303 
PRO CB  HB2  sing N N 304 
PRO CB  HB3  sing N N 305 
PRO CG  CD   sing N N 306 
PRO CG  HG2  sing N N 307 
PRO CG  HG3  sing N N 308 
PRO CD  HD2  sing N N 309 
PRO CD  HD3  sing N N 310 
PRO OXT HXT  sing N N 311 
SER N   CA   sing N N 312 
SER N   H    sing N N 313 
SER N   H2   sing N N 314 
SER CA  C    sing N N 315 
SER CA  CB   sing N N 316 
SER CA  HA   sing N N 317 
SER C   O    doub N N 318 
SER C   OXT  sing N N 319 
SER CB  OG   sing N N 320 
SER CB  HB2  sing N N 321 
SER CB  HB3  sing N N 322 
SER OG  HG   sing N N 323 
SER OXT HXT  sing N N 324 
THR N   CA   sing N N 325 
THR N   H    sing N N 326 
THR N   H2   sing N N 327 
THR CA  C    sing N N 328 
THR CA  CB   sing N N 329 
THR CA  HA   sing N N 330 
THR C   O    doub N N 331 
THR C   OXT  sing N N 332 
THR CB  OG1  sing N N 333 
THR CB  CG2  sing N N 334 
THR CB  HB   sing N N 335 
THR OG1 HG1  sing N N 336 
THR CG2 HG21 sing N N 337 
THR CG2 HG22 sing N N 338 
THR CG2 HG23 sing N N 339 
THR OXT HXT  sing N N 340 
TRP N   CA   sing N N 341 
TRP N   H    sing N N 342 
TRP N   H2   sing N N 343 
TRP CA  C    sing N N 344 
TRP CA  CB   sing N N 345 
TRP CA  HA   sing N N 346 
TRP C   O    doub N N 347 
TRP C   OXT  sing N N 348 
TRP CB  CG   sing N N 349 
TRP CB  HB2  sing N N 350 
TRP CB  HB3  sing N N 351 
TRP CG  CD1  doub Y N 352 
TRP CG  CD2  sing Y N 353 
TRP CD1 NE1  sing Y N 354 
TRP CD1 HD1  sing N N 355 
TRP CD2 CE2  doub Y N 356 
TRP CD2 CE3  sing Y N 357 
TRP NE1 CE2  sing Y N 358 
TRP NE1 HE1  sing N N 359 
TRP CE2 CZ2  sing Y N 360 
TRP CE3 CZ3  doub Y N 361 
TRP CE3 HE3  sing N N 362 
TRP CZ2 CH2  doub Y N 363 
TRP CZ2 HZ2  sing N N 364 
TRP CZ3 CH2  sing Y N 365 
TRP CZ3 HZ3  sing N N 366 
TRP CH2 HH2  sing N N 367 
TRP OXT HXT  sing N N 368 
TYR N   CA   sing N N 369 
TYR N   H    sing N N 370 
TYR N   H2   sing N N 371 
TYR CA  C    sing N N 372 
TYR CA  CB   sing N N 373 
TYR CA  HA   sing N N 374 
TYR C   O    doub N N 375 
TYR C   OXT  sing N N 376 
TYR CB  CG   sing N N 377 
TYR CB  HB2  sing N N 378 
TYR CB  HB3  sing N N 379 
TYR CG  CD1  doub Y N 380 
TYR CG  CD2  sing Y N 381 
TYR CD1 CE1  sing Y N 382 
TYR CD1 HD1  sing N N 383 
TYR CD2 CE2  doub Y N 384 
TYR CD2 HD2  sing N N 385 
TYR CE1 CZ   doub Y N 386 
TYR CE1 HE1  sing N N 387 
TYR CE2 CZ   sing Y N 388 
TYR CE2 HE2  sing N N 389 
TYR CZ  OH   sing N N 390 
TYR OH  HH   sing N N 391 
TYR OXT HXT  sing N N 392 
VAL N   CA   sing N N 393 
VAL N   H    sing N N 394 
VAL N   H2   sing N N 395 
VAL CA  C    sing N N 396 
VAL CA  CB   sing N N 397 
VAL CA  HA   sing N N 398 
VAL C   O    doub N N 399 
VAL C   OXT  sing N N 400 
VAL CB  CG1  sing N N 401 
VAL CB  CG2  sing N N 402 
VAL CB  HB   sing N N 403 
VAL CG1 HG11 sing N N 404 
VAL CG1 HG12 sing N N 405 
VAL CG1 HG13 sing N N 406 
VAL CG2 HG21 sing N N 407 
VAL CG2 HG22 sing N N 408 
VAL CG2 HG23 sing N N 409 
VAL OXT HXT  sing N N 410 
# 
_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              42.57 
_em_3d_crystal_entity.length_b              48.85 
_em_3d_crystal_entity.length_c              99.86 
_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    96.7 
_em_diffraction_shell.high_resolution           2.5 
_em_diffraction_shell.id                        1 
_em_diffraction_shell.low_resolution            2.4 
_em_diffraction_shell.multiplicity              4.5 
_em_diffraction_shell.num_structure_factors     940 
_em_diffraction_shell.phase_residual            33.6 
# 
_em_diffraction_stats.details                          ? 
_em_diffraction_stats.fourier_space_coverage           95.2 
_em_diffraction_stats.high_resolution                  2.4 
_em_diffraction_stats.id                               1 
_em_diffraction_stats.image_processing_id              1 
_em_diffraction_stats.num_intensities_measured         36267 
_em_diffraction_stats.num_structure_factors            8231 
_em_diffraction_stats.overall_phase_error              ? 
_em_diffraction_stats.overall_phase_residual           ? 
_em_diffraction_stats.phase_error_rejection_criteria   0 
_em_diffraction_stats.r_merge                          24.6 
_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         0.09 
_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                 ? 
_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 
'National Science Foundation (NSF, United States)' 'United States' DMR-1548924       1 
'Howard Hughes Medical Institute (HHMI)'           'United States' HHMI-EPI          2 
'Department of Energy (DOE, United States)'        'United States' DE-FC02-02ER63421 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          ? 
# 
_atom_sites.entry_id                    9NC1 
_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]   0.023491 
_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]   0.020471 
_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]   0.010014 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ILE A 1 1   ? 22.633  -10.434 20.576 1.00 16.10  ? 1   ILE A N   1 
ATOM   2    C CA  . ILE A 1 1   ? 22.465  -9.441  19.519 1.00 20.01  ? 1   ILE A CA  1 
ATOM   3    C C   . ILE A 1 1   ? 23.766  -8.648  19.330 1.00 17.66  ? 1   ILE A C   1 
ATOM   4    O O   . ILE A 1 1   ? 24.550  -8.520  20.265 1.00 18.82  ? 1   ILE A O   1 
ATOM   5    C CB  . ILE A 1 1   ? 21.281  -8.496  19.836 1.00 16.94  ? 1   ILE A CB  1 
ATOM   6    C CG1 . ILE A 1 1   ? 21.605  -7.619  21.047 1.00 14.76  ? 1   ILE A CG1 1 
ATOM   7    C CG2 . ILE A 1 1   ? 20.011  -9.308  20.095 1.00 11.29  ? 1   ILE A CG2 1 
ATOM   8    C CD1 . ILE A 1 1   ? 20.479  -6.703  21.451 1.00 18.03  ? 1   ILE A CD1 1 
ATOM   9    N N   . PRO A 1 2   ? 23.999  -8.132  18.124 1.00 18.05  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 2   ? 25.308  -7.546  17.802 1.00 21.90  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 2   ? 25.459  -6.108  18.296 1.00 18.08  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 2   ? 24.522  -5.465  18.770 1.00 18.85  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 2   ? 25.363  -7.618  16.271 1.00 21.75  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 2   ? 23.929  -7.553  15.842 1.00 14.74  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 2   ? 23.130  -8.243  16.933 1.00 11.79  ? 2   PRO A CD  1 
ATOM   16   N N   . GLU A 1 3   ? 26.695  -5.619  18.180 1.00 23.62  ? 3   GLU A N   1 
ATOM   17   C CA  . GLU A 1 3   ? 27.040  -4.304  18.709 1.00 22.64  ? 3   GLU A CA  1 
ATOM   18   C C   . GLU A 1 3   ? 26.347  -3.197  17.934 1.00 17.95  ? 3   GLU A C   1 
ATOM   19   O O   . GLU A 1 3   ? 25.979  -2.166  18.506 1.00 15.37  ? 3   GLU A O   1 
ATOM   20   C CB  . GLU A 1 3   ? 28.550  -4.107  18.659 1.00 19.19  ? 3   GLU A CB  1 
ATOM   21   C CG  . GLU A 1 3   ? 29.313  -5.045  19.565 1.00 30.74  ? 3   GLU A CG  1 
ATOM   22   C CD  . GLU A 1 3   ? 29.553  -4.445  20.941 1.00 40.65  ? 3   GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 3   ? 28.930  -4.913  21.916 1.00 29.76  ? 3   GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 3   ? 30.363  -3.498  21.048 1.00 41.47  ? 3   GLU A OE2 1 
ATOM   25   N N   . TYR A 1 4   ? 26.168  -3.390  16.631 1.00 21.13  ? 4   TYR A N   1 
ATOM   26   C CA  . TYR A 1 4   ? 25.548  -2.396  15.771 1.00 17.90  ? 4   TYR A CA  1 
ATOM   27   C C   . TYR A 1 4   ? 24.417  -3.009  14.968 1.00 13.61  ? 4   TYR A C   1 
ATOM   28   O O   . TYR A 1 4   ? 24.553  -4.126  14.452 1.00 16.63  ? 4   TYR A O   1 
ATOM   29   C CB  . TYR A 1 4   ? 26.553  -1.801  14.795 1.00 15.47  ? 4   TYR A CB  1 
ATOM   30   C CG  . TYR A 1 4   ? 27.519  -0.834  15.401 1.00 20.49  ? 4   TYR A CG  1 
ATOM   31   C CD1 . TYR A 1 4   ? 27.186  0.506   15.499 1.00 20.16  ? 4   TYR A CD1 1 
ATOM   32   C CD2 . TYR A 1 4   ? 28.778  -1.238  15.841 1.00 23.23  ? 4   TYR A CD2 1 
ATOM   33   C CE1 . TYR A 1 4   ? 28.059  1.414   16.042 1.00 21.65  ? 4   TYR A CE1 1 
ATOM   34   C CE2 . TYR A 1 4   ? 29.662  -0.331  16.386 1.00 16.87  ? 4   TYR A CE2 1 
ATOM   35   C CZ  . TYR A 1 4   ? 29.293  0.998   16.474 1.00 19.02  ? 4   TYR A CZ  1 
ATOM   36   O OH  . TYR A 1 4   ? 30.148  1.919   17.020 1.00 28.03  ? 4   TYR A OH  1 
ATOM   37   N N   . VAL A 1 5   ? 23.303  -2.272  14.868 1.00 11.60  ? 5   VAL A N   1 
ATOM   38   C CA  . VAL A 1 5   ? 22.217  -2.615  13.959 1.00 14.57  ? 5   VAL A CA  1 
ATOM   39   C C   . VAL A 1 5   ? 21.843  -1.360  13.199 1.00 15.09  ? 5   VAL A C   1 
ATOM   40   O O   . VAL A 1 5   ? 21.815  -0.270  13.776 1.00 15.76  ? 5   VAL A O   1 
ATOM   41   C CB  . VAL A 1 5   ? 20.996  -3.224  14.666 1.00 19.38  ? 5   VAL A CB  1 
ATOM   42   C CG1 . VAL A 1 5   ? 19.809  -3.327  13.699 1.00 18.72  ? 5   VAL A CG1 1 
ATOM   43   C CG2 . VAL A 1 5   ? 21.341  -4.600  15.174 1.00 17.55  ? 5   VAL A CG2 1 
ATOM   44   N N   . ASP A 1 6   ? 21.593  -1.505  11.908 1.00 11.15  ? 6   ASP A N   1 
ATOM   45   C CA  . ASP A 1 6   ? 21.156  -0.387  11.083 1.00 18.40  ? 6   ASP A CA  1 
ATOM   46   C C   . ASP A 1 6   ? 20.335  -0.991  9.949  1.00 18.87  ? 6   ASP A C   1 
ATOM   47   O O   . ASP A 1 6   ? 20.900  -1.529  8.994  1.00 19.42  ? 6   ASP A O   1 
ATOM   48   C CB  . ASP A 1 6   ? 22.356  0.392   10.572 1.00 17.71  ? 6   ASP A CB  1 
ATOM   49   C CG  . ASP A 1 6   ? 21.970  1.655   9.825  1.00 21.40  ? 6   ASP A CG  1 
ATOM   50   O OD1 . ASP A 1 6   ? 20.797  1.783   9.416  1.00 20.52  ? 6   ASP A OD1 1 
ATOM   51   O OD2 . ASP A 1 6   ? 22.850  2.531   9.650  1.00 17.91  ? 6   ASP A OD2 1 
ATOM   52   N N   . TRP A 1 7   ? 19.010  -1.002  10.118 1.00 12.58  ? 7   TRP A N   1 
ATOM   53   C CA  . TRP A 1 7   ? 18.160  -1.629  9.114  1.00 14.99  ? 7   TRP A CA  1 
ATOM   54   C C   . TRP A 1 7   ? 18.202  -0.943  7.756  1.00 16.04  ? 7   TRP A C   1 
ATOM   55   O O   . TRP A 1 7   ? 17.778  -1.555  6.769  1.00 19.97  ? 7   TRP A O   1 
ATOM   56   C CB  . TRP A 1 7   ? 16.712  -1.706  9.623  1.00 15.39  ? 7   TRP A CB  1 
ATOM   57   C CG  . TRP A 1 7   ? 16.530  -2.821  10.593 1.00 13.16  ? 7   TRP A CG  1 
ATOM   58   C CD1 . TRP A 1 7   ? 16.334  -2.727  11.943 1.00 13.83  ? 7   TRP A CD1 1 
ATOM   59   C CD2 . TRP A 1 7   ? 16.607  -4.223  10.293 1.00 13.50  ? 7   TRP A CD2 1 
ATOM   60   N NE1 . TRP A 1 7   ? 16.249  -3.988  12.497 1.00 15.11  ? 7   TRP A NE1 1 
ATOM   61   C CE2 . TRP A 1 7   ? 16.419  -4.923  11.509 1.00 13.58  ? 7   TRP A CE2 1 
ATOM   62   C CE3 . TRP A 1 7   ? 16.804  -4.955  9.110  1.00 15.09  ? 7   TRP A CE3 1 
ATOM   63   C CZ2 . TRP A 1 7   ? 16.423  -6.321  11.579 1.00 13.48  ? 7   TRP A CZ2 1 
ATOM   64   C CZ3 . TRP A 1 7   ? 16.802  -6.342  9.179  1.00 20.30  ? 7   TRP A CZ3 1 
ATOM   65   C CH2 . TRP A 1 7   ? 16.615  -7.012  10.408 1.00 19.23  ? 7   TRP A CH2 1 
ATOM   66   N N   . ARG A 1 8   ? 18.678  0.306   7.669  1.00 15.15  ? 8   ARG A N   1 
ATOM   67   C CA  . ARG A 1 8   ? 18.852  0.934   6.356  1.00 16.42  ? 8   ARG A CA  1 
ATOM   68   C C   . ARG A 1 8   ? 19.876  0.195   5.511  1.00 15.82  ? 8   ARG A C   1 
ATOM   69   O O   . ARG A 1 8   ? 19.734  0.069   4.288  1.00 24.81  ? 8   ARG A O   1 
ATOM   70   C CB  . ARG A 1 8   ? 19.316  2.372   6.541  1.00 14.84  ? 8   ARG A CB  1 
ATOM   71   C CG  . ARG A 1 8   ? 18.385  3.254   7.322  1.00 18.29  ? 8   ARG A CG  1 
ATOM   72   C CD  . ARG A 1 8   ? 19.038  4.597   7.526  1.00 12.26  ? 8   ARG A CD  1 
ATOM   73   N NE  . ARG A 1 8   ? 20.214  4.490   8.378  1.00 11.57  ? 8   ARG A NE  1 
ATOM   74   C CZ  . ARG A 1 8   ? 20.942  5.522   8.781  1.00 16.93  ? 8   ARG A CZ  1 
ATOM   75   N NH1 . ARG A 1 8   ? 20.650  6.760   8.414  1.00 14.22  ? 8   ARG A NH1 1 
ATOM   76   N NH2 . ARG A 1 8   ? 21.969  5.313   9.601  1.00 12.49  ? 8   ARG A NH2 1 
ATOM   77   N N   . GLN A 1 9   ? 20.922  -0.287  6.165  1.00 17.46  ? 9   GLN A N   1 
ATOM   78   C CA  . GLN A 1 9   ? 22.019  -0.993  5.533  1.00 19.75  ? 9   GLN A CA  1 
ATOM   79   C C   . GLN A 1 9   ? 21.609  -2.386  5.073  1.00 23.71  ? 9   GLN A C   1 
ATOM   80   O O   . GLN A 1 9   ? 22.264  -2.964  4.198  1.00 26.33  ? 9   GLN A O   1 
ATOM   81   C CB  . GLN A 1 9   ? 23.173  -0.916  6.522  1.00 22.11  ? 9   GLN A CB  1 
ATOM   82   C CG  . GLN A 1 9   ? 23.515  -2.083  7.373  1.00 42.93  ? 9   GLN A CG  1 
ATOM   83   C CD  . GLN A 1 9   ? 24.701  -1.699  8.239  1.00 42.07  ? 9   GLN A CD  1 
ATOM   84   O OE1 . GLN A 1 9   ? 25.405  -0.731  7.934  1.00 33.47  ? 9   GLN A OE1 1 
ATOM   85   N NE2 . GLN A 1 9   ? 24.922  -2.436  9.323  1.00 39.11  ? 9   GLN A NE2 1 
ATOM   86   N N   . LYS A 1 10  ? 20.498  -2.903  5.596  1.00 20.41  ? 10  LYS A N   1 
ATOM   87   C CA  . LYS A 1 10  ? 19.907  -4.149  5.142  1.00 24.07  ? 10  LYS A CA  1 
ATOM   88   C C   . LYS A 1 10  ? 18.673  -3.928  4.270  1.00 23.82  ? 10  LYS A C   1 
ATOM   89   O O   . LYS A 1 10  ? 17.848  -4.838  4.125  1.00 28.37  ? 10  LYS A O   1 
ATOM   90   C CB  . LYS A 1 10  ? 19.584  -5.028  6.346  1.00 31.66  ? 10  LYS A CB  1 
ATOM   91   C CG  . LYS A 1 10  ? 20.748  -5.940  6.705  1.00 32.81  ? 10  LYS A CG  1 
ATOM   92   C CD  . LYS A 1 10  ? 20.754  -6.347  8.151  1.00 26.47  ? 10  LYS A CD  1 
ATOM   93   C CE  . LYS A 1 10  ? 21.952  -7.237  8.413  1.00 32.10  ? 10  LYS A CE  1 
ATOM   94   N NZ  . LYS A 1 10  ? 22.328  -7.972  7.167  1.00 42.22  ? 10  LYS A NZ  1 
ATOM   95   N N   . GLY A 1 11  ? 18.536  -2.738  3.688  1.00 17.89  ? 11  GLY A N   1 
ATOM   96   C CA  . GLY A 1 11  ? 17.483  -2.445  2.725  1.00 19.41  ? 11  GLY A CA  1 
ATOM   97   C C   . GLY A 1 11  ? 16.064  -2.565  3.242  1.00 22.19  ? 11  GLY A C   1 
ATOM   98   O O   . GLY A 1 11  ? 15.162  -2.919  2.474  1.00 18.61  ? 11  GLY A O   1 
ATOM   99   N N   . ALA A 1 12  ? 15.840  -2.282  4.529  1.00 19.33  ? 12  ALA A N   1 
ATOM   100  C CA  . ALA A 1 12  ? 14.542  -2.472  5.170  1.00 17.48  ? 12  ALA A CA  1 
ATOM   101  C C   . ALA A 1 12  ? 13.886  -1.153  5.559  1.00 12.96  ? 12  ALA A C   1 
ATOM   102  O O   . ALA A 1 12  ? 12.869  -1.161  6.255  1.00 12.83  ? 12  ALA A O   1 
ATOM   103  C CB  . ALA A 1 12  ? 14.663  -3.369  6.407  1.00 12.83  ? 12  ALA A CB  1 
ATOM   104  N N   . VAL A 1 13  ? 14.422  -0.025  5.107  1.00 15.75  ? 13  VAL A N   1 
ATOM   105  C CA  . VAL A 1 13  ? 13.927  1.292   5.487  1.00 14.31  ? 13  VAL A CA  1 
ATOM   106  C C   . VAL A 1 13  ? 13.728  2.105   4.218  1.00 13.15  ? 13  VAL A C   1 
ATOM   107  O O   . VAL A 1 13  ? 14.637  2.197   3.387  1.00 17.89  ? 13  VAL A O   1 
ATOM   108  C CB  . VAL A 1 13  ? 14.891  1.998   6.463  1.00 14.87  ? 13  VAL A CB  1 
ATOM   109  C CG1 . VAL A 1 13  ? 14.311  3.297   6.957  1.00 13.35  ? 13  VAL A CG1 1 
ATOM   110  C CG2 . VAL A 1 13  ? 15.179  1.095   7.649  1.00 13.71  ? 13  VAL A CG2 1 
ATOM   111  N N   . THR A 1 14  ? 12.531  2.654   4.050  1.00 15.44  ? 14  THR A N   1 
ATOM   112  C CA  . THR A 1 14  ? 12.216  3.496   2.904  1.00 14.63  ? 14  THR A CA  1 
ATOM   113  C C   . THR A 1 14  ? 12.680  4.924   3.167  1.00 15.48  ? 14  THR A C   1 
ATOM   114  O O   . THR A 1 14  ? 13.145  5.249   4.260  1.00 17.70  ? 14  THR A O   1 
ATOM   115  C CB  . THR A 1 14  ? 10.712  3.437   2.622  1.00 17.88  ? 14  THR A CB  1 
ATOM   116  O OG1 . THR A 1 14  ? 9.991   4.117   3.658  1.00 18.95  ? 14  THR A OG1 1 
ATOM   117  C CG2 . THR A 1 14  ? 10.231  2.004   2.520  1.00 16.69  ? 14  THR A CG2 1 
ATOM   118  N N   . PRO A 1 15  ? 12.629  5.794   2.159  1.00 17.55  ? 15  PRO A N   1 
ATOM   119  C CA  . PRO A 1 15  ? 13.055  7.184   2.375  1.00 11.99  ? 15  PRO A CA  1 
ATOM   120  C C   . PRO A 1 15  ? 12.285  7.872   3.495  1.00 13.17  ? 15  PRO A C   1 
ATOM   121  O O   . PRO A 1 15  ? 11.126  7.554   3.772  1.00 14.49  ? 15  PRO A O   1 
ATOM   122  C CB  . PRO A 1 15  ? 12.782  7.848   1.021  1.00 13.42  ? 15  PRO A CB  1 
ATOM   123  C CG  . PRO A 1 15  ? 12.962  6.738   0.037  1.00 16.63  ? 15  PRO A CG  1 
ATOM   124  C CD  . PRO A 1 15  ? 12.405  5.507   0.726  1.00 15.82  ? 15  PRO A CD  1 
ATOM   125  N N   . VAL A 1 16  ? 12.949  8.853   4.117  1.00 13.35  ? 16  VAL A N   1 
ATOM   126  C CA  . VAL A 1 16  ? 12.341  9.658   5.175  1.00 13.62  ? 16  VAL A CA  1 
ATOM   127  C C   . VAL A 1 16  ? 11.173  10.474  4.637  1.00 11.35  ? 16  VAL A C   1 
ATOM   128  O O   . VAL A 1 16  ? 11.249  11.070  3.554  1.00 15.73  ? 16  VAL A O   1 
ATOM   129  C CB  . VAL A 1 16  ? 13.395  10.578  5.813  1.00 13.08  ? 16  VAL A CB  1 
ATOM   130  C CG1 . VAL A 1 16  ? 12.728  11.706  6.612  1.00 9.35   ? 16  VAL A CG1 1 
ATOM   131  C CG2 . VAL A 1 16  ? 14.327  9.765   6.694  1.00 14.07  ? 16  VAL A CG2 1 
ATOM   132  N N   . LYS A 1 17  ? 10.086  10.523  5.407  1.00 15.17  ? 17  LYS A N   1 
ATOM   133  C CA  . LYS A 1 17  ? 8.867   11.228  5.026  1.00 19.06  ? 17  LYS A CA  1 
ATOM   134  C C   . LYS A 1 17  ? 8.697   12.487  5.869  1.00 14.80  ? 17  LYS A C   1 
ATOM   135  O O   . LYS A 1 17  ? 9.373   12.687  6.882  1.00 14.55  ? 17  LYS A O   1 
ATOM   136  C CB  . LYS A 1 17  ? 7.636   10.326  5.198  1.00 20.88  ? 17  LYS A CB  1 
ATOM   137  C CG  . LYS A 1 17  ? 7.708   8.962   4.533  1.00 22.20  ? 17  LYS A CG  1 
ATOM   138  C CD  . LYS A 1 17  ? 8.039   9.078   3.059  1.00 19.52  ? 17  LYS A CD  1 
ATOM   139  C CE  . LYS A 1 17  ? 7.810   7.751   2.366  1.00 24.01  ? 17  LYS A CE  1 
ATOM   140  N NZ  . LYS A 1 17  ? 8.557   6.669   3.059  1.00 22.11  ? 17  LYS A NZ  1 
ATOM   141  N N   . ASN A 1 18  ? 7.761   13.331  5.443  1.00 14.72  ? 18  ASN A N   1 
ATOM   142  C CA  . ASN A 1 18  ? 7.388   14.537  6.173  1.00 16.12  ? 18  ASN A CA  1 
ATOM   143  C C   . ASN A 1 18  ? 5.889   14.525  6.426  1.00 15.41  ? 18  ASN A C   1 
ATOM   144  O O   . ASN A 1 18  ? 5.093   14.633  5.486  1.00 14.26  ? 18  ASN A O   1 
ATOM   145  C CB  . ASN A 1 18  ? 7.778   15.797  5.398  1.00 12.83  ? 18  ASN A CB  1 
ATOM   146  C CG  . ASN A 1 18  ? 7.540   17.063  6.197  1.00 17.22  ? 18  ASN A CG  1 
ATOM   147  O OD1 . ASN A 1 18  ? 7.086   17.009  7.336  1.00 18.40  ? 18  ASN A OD1 1 
ATOM   148  N ND2 . ASN A 1 18  ? 7.823   18.211  5.593  1.00 20.57  ? 18  ASN A ND2 1 
ATOM   149  N N   . GLN A 1 19  ? 5.509   14.453  7.705  1.00 19.74  ? 19  GLN A N   1 
ATOM   150  C CA  . GLN A 1 19  ? 4.096   14.451  8.052  1.00 17.11  ? 19  GLN A CA  1 
ATOM   151  C C   . GLN A 1 19  ? 3.463   15.820  7.892  1.00 15.58  ? 19  GLN A C   1 
ATOM   152  O O   . GLN A 1 19  ? 2.231   15.918  7.882  1.00 20.90  ? 19  GLN A O   1 
ATOM   153  C CB  . GLN A 1 19  ? 3.904   13.971  9.485  1.00 18.26  ? 19  GLN A CB  1 
ATOM   154  C CG  . GLN A 1 19  ? 4.456   14.944  10.522 1.00 18.63  ? 19  GLN A CG  1 
ATOM   155  C CD  . GLN A 1 19  ? 4.390   14.388  11.932 1.00 16.95  ? 19  GLN A CD  1 
ATOM   156  O OE1 . GLN A 1 19  ? 5.261   13.631  12.362 1.00 16.29  ? 19  GLN A OE1 1 
ATOM   157  N NE2 . GLN A 1 19  ? 3.339   14.752  12.655 1.00 16.33  ? 19  GLN A NE2 1 
ATOM   158  N N   . GLY A 1 20  ? 4.266   16.881  7.801  1.00 20.74  ? 20  GLY A N   1 
ATOM   159  C CA  . GLY A 1 20  ? 3.632   18.171  7.692  1.00 13.36  ? 20  GLY A CA  1 
ATOM   160  C C   . GLY A 1 20  ? 3.035   18.579  9.023  1.00 14.49  ? 20  GLY A C   1 
ATOM   161  O O   . GLY A 1 20  ? 3.420   18.109  10.096 1.00 19.46  ? 20  GLY A O   1 
ATOM   162  N N   . SER A 1 21  ? 2.042   19.458  8.930  1.00 19.85  ? 21  SER A N   1 
ATOM   163  C CA  . SER A 1 21  ? 1.408   20.007  10.116 1.00 22.61  ? 21  SER A CA  1 
ATOM   164  C C   . SER A 1 21  ? 0.475   18.999  10.777 1.00 19.85  ? 21  SER A C   1 
ATOM   165  O O   . SER A 1 21  ? 0.108   19.182  11.943 1.00 21.00  ? 21  SER A O   1 
ATOM   166  C CB  . SER A 1 21  ? 0.637   21.272  9.739  1.00 18.50  ? 21  SER A CB  1 
ATOM   167  O OG  . SER A 1 21  ? -0.283  20.975  8.704  1.00 14.08  ? 21  SER A OG  1 
ATOM   168  N N   . CYS A 1 22  ? 0.063   17.966  10.045 1.00 19.15  ? 22  CYS A N   1 
ATOM   169  C CA  . CYS A 1 22  ? -0.874  16.983  10.567 1.00 21.92  ? 22  CYS A CA  1 
ATOM   170  C C   . CYS A 1 22  ? -0.213  16.163  11.673 1.00 17.75  ? 22  CYS A C   1 
ATOM   171  O O   . CYS A 1 22  ? 0.923   15.705  11.537 1.00 15.86  ? 22  CYS A O   1 
ATOM   172  C CB  . CYS A 1 22  ? -1.358  16.070  9.434  1.00 17.15  ? 22  CYS A CB  1 
ATOM   173  S SG  . CYS A 1 22  ? -2.420  14.681  9.932  1.00 31.81  ? 22  CYS A SG  1 
ATOM   174  N N   . GLY A 1 23  ? -0.946  15.944  12.754 1.00 17.72  ? 23  GLY A N   1 
ATOM   175  C CA  . GLY A 1 23  ? -0.464  15.117  13.841 1.00 18.13  ? 23  GLY A CA  1 
ATOM   176  C C   . GLY A 1 23  ? -0.604  13.644  13.525 1.00 19.87  ? 23  GLY A C   1 
ATOM   177  O O   . GLY A 1 23  ? -1.298  12.905  14.229 1.00 22.22  ? 23  GLY A O   1 
ATOM   178  N N   . SER A 1 24  ? 0.066   13.201  12.468 1.00 20.30  ? 24  SER A N   1 
ATOM   179  C CA  . SER A 1 24  ? -0.069  11.839  11.975 1.00 19.18  ? 24  SER A CA  1 
ATOM   180  C C   . SER A 1 24  ? 1.148   10.983  12.273 1.00 17.69  ? 24  SER A C   1 
ATOM   181  O O   . SER A 1 24  ? 1.307   9.916   11.679 1.00 17.20  ? 24  SER A O   1 
ATOM   182  C CB  . SER A 1 24  ? -0.320  11.877  10.473 1.00 15.72  ? 24  SER A CB  1 
ATOM   183  O OG  . SER A 1 24  ? 0.671   12.676  9.847  1.00 14.36  ? 24  SER A OG  1 
ATOM   184  N N   . CYS A 1 25  ? 2.003   11.424  13.193 1.00 19.22  ? 25  CYS A N   1 
ATOM   185  C CA  . CYS A 1 25  ? 3.240   10.699  13.462 1.00 18.58  ? 25  CYS A CA  1 
ATOM   186  C C   . CYS A 1 25  ? 2.979   9.244   13.841 1.00 16.72  ? 25  CYS A C   1 
ATOM   187  O O   . CYS A 1 25  ? 3.787   8.368   13.513 1.00 15.41  ? 25  CYS A O   1 
ATOM   188  C CB  . CYS A 1 25  ? 4.017   11.408  14.572 1.00 20.40  ? 25  CYS A CB  1 
ATOM   189  S SG  . CYS A 1 25  ? 3.004   11.720  16.052 1.00 17.96  ? 25  CYS A SG  1 
ATOM   190  N N   . TRP A 1 26  ? 1.869   8.971   14.539 1.00 17.40  ? 26  TRP A N   1 
ATOM   191  C CA  . TRP A 1 26  ? 1.545   7.603   14.941 1.00 17.19  ? 26  TRP A CA  1 
ATOM   192  C C   . TRP A 1 26  ? 1.378   6.683   13.739 1.00 12.00  ? 26  TRP A C   1 
ATOM   193  O O   . TRP A 1 26  ? 1.898   5.555   13.725 1.00 14.40  ? 26  TRP A O   1 
ATOM   194  C CB  . TRP A 1 26  ? 0.275   7.613   15.799 1.00 14.98  ? 26  TRP A CB  1 
ATOM   195  C CG  . TRP A 1 26  ? -0.898  8.290   15.127 1.00 19.14  ? 26  TRP A CG  1 
ATOM   196  C CD1 . TRP A 1 26  ? -1.172  9.632   15.135 1.00 20.60  ? 26  TRP A CD1 1 
ATOM   197  C CD2 . TRP A 1 26  ? -1.937  7.675   14.339 1.00 14.09  ? 26  TRP A CD2 1 
ATOM   198  N NE1 . TRP A 1 26  ? -2.313  9.886   14.407 1.00 24.58  ? 26  TRP A NE1 1 
ATOM   199  C CE2 . TRP A 1 26  ? -2.799  8.705   13.907 1.00 20.99  ? 26  TRP A CE2 1 
ATOM   200  C CE3 . TRP A 1 26  ? -2.217  6.361   13.956 1.00 15.35  ? 26  TRP A CE3 1 
ATOM   201  C CZ2 . TRP A 1 26  ? -3.925  8.458   13.121 1.00 15.86  ? 26  TRP A CZ2 1 
ATOM   202  C CZ3 . TRP A 1 26  ? -3.334  6.119   13.174 1.00 12.27  ? 26  TRP A CZ3 1 
ATOM   203  C CH2 . TRP A 1 26  ? -4.171  7.163   12.764 1.00 14.76  ? 26  TRP A CH2 1 
ATOM   204  N N   . ALA A 1 27  ? 0.813   7.209   12.660 1.00 12.65  ? 27  ALA A N   1 
ATOM   205  C CA  . ALA A 1 27  ? 0.659   6.422   11.448 1.00 14.07  ? 27  ALA A CA  1 
ATOM   206  C C   . ALA A 1 27  ? 1.977   6.256   10.701 1.00 12.83  ? 27  ALA A C   1 
ATOM   207  O O   . ALA A 1 27  ? 2.259   5.164   10.196 1.00 13.83  ? 27  ALA A O   1 
ATOM   208  C CB  . ALA A 1 27  ? -0.397  7.064   10.541 1.00 10.53  ? 27  ALA A CB  1 
ATOM   209  N N   . PHE A 1 28  ? 2.815   7.295   10.661 1.00 12.51  ? 28  PHE A N   1 
ATOM   210  C CA  . PHE A 1 28  ? 4.118   7.165   10.008 1.00 16.43  ? 28  PHE A CA  1 
ATOM   211  C C   . PHE A 1 28  ? 4.984   6.133   10.718 1.00 13.42  ? 28  PHE A C   1 
ATOM   212  O O   . PHE A 1 28  ? 5.638   5.304   10.076 1.00 14.57  ? 28  PHE A O   1 
ATOM   213  C CB  . PHE A 1 28  ? 4.812   8.528   9.966  1.00 14.73  ? 28  PHE A CB  1 
ATOM   214  C CG  . PHE A 1 28  ? 4.314   9.399   8.859  1.00 18.44  ? 28  PHE A CG  1 
ATOM   215  C CD1 . PHE A 1 28  ? 3.136   10.111  9.014  1.00 18.14  ? 28  PHE A CD1 1 
ATOM   216  C CD2 . PHE A 1 28  ? 4.959   9.446   7.641  1.00 20.97  ? 28  PHE A CD2 1 
ATOM   217  C CE1 . PHE A 1 28  ? 2.638   10.906  7.983  1.00 21.28  ? 28  PHE A CE1 1 
ATOM   218  C CE2 . PHE A 1 28  ? 4.464   10.237  6.608  1.00 23.52  ? 28  PHE A CE2 1 
ATOM   219  C CZ  . PHE A 1 28  ? 3.306   10.966  6.779  1.00 17.15  ? 28  PHE A CZ  1 
ATOM   220  N N   . SER A 1 29  ? 5.031   6.209   12.047 1.00 16.21  ? 29  SER A N   1 
ATOM   221  C CA  . SER A 1 29  ? 5.769   5.243   12.857 1.00 15.17  ? 29  SER A CA  1 
ATOM   222  C C   . SER A 1 29  ? 5.295   3.820   12.565 1.00 18.06  ? 29  SER A C   1 
ATOM   223  O O   . SER A 1 29  ? 6.104   2.909   12.284 1.00 15.93  ? 29  SER A O   1 
ATOM   224  C CB  . SER A 1 29  ? 5.601   5.599   14.334 1.00 13.75  ? 29  SER A CB  1 
ATOM   225  O OG  . SER A 1 29  ? 6.148   4.608   15.178 1.00 16.32  ? 29  SER A OG  1 
ATOM   226  N N   . ALA A 1 30  ? 3.971   3.613   12.608 1.00 19.93  ? 30  ALA A N   1 
ATOM   227  C CA  . ALA A 1 30  ? 3.454   2.284   12.316 1.00 20.63  ? 30  ALA A CA  1 
ATOM   228  C C   . ALA A 1 30  ? 3.892   1.835   10.928 1.00 12.75  ? 30  ALA A C   1 
ATOM   229  O O   . ALA A 1 30  ? 4.335   0.691   10.748 1.00 16.35  ? 30  ALA A O   1 
ATOM   230  C CB  . ALA A 1 30  ? 1.925   2.285   12.438 1.00 12.31  ? 30  ALA A CB  1 
ATOM   231  N N   . VAL A 1 31  ? 3.775   2.723   9.932  1.00 14.45  ? 31  VAL A N   1 
ATOM   232  C CA  . VAL A 1 31  ? 4.125   2.357   8.559  1.00 18.26  ? 31  VAL A CA  1 
ATOM   233  C C   . VAL A 1 31  ? 5.607   1.990   8.439  1.00 17.62  ? 31  VAL A C   1 
ATOM   234  O O   . VAL A 1 31  ? 5.973   1.081   7.684  1.00 21.41  ? 31  VAL A O   1 
ATOM   235  C CB  . VAL A 1 31  ? 3.746   3.494   7.590  1.00 24.14  ? 31  VAL A CB  1 
ATOM   236  C CG1 . VAL A 1 31  ? 4.453   3.304   6.253  1.00 23.28  ? 31  VAL A CG1 1 
ATOM   237  C CG2 . VAL A 1 31  ? 2.231   3.562   7.403  1.00 16.98  ? 31  VAL A CG2 1 
ATOM   238  N N   . VAL A 1 32  ? 6.489   2.719   9.133  1.00 16.42  ? 32  VAL A N   1 
ATOM   239  C CA  . VAL A 1 32  ? 7.906   2.355   9.085  1.00 13.90  ? 32  VAL A CA  1 
ATOM   240  C C   . VAL A 1 32  ? 8.090   0.919   9.537  1.00 17.86  ? 32  VAL A C   1 
ATOM   241  O O   . VAL A 1 32  ? 8.796   0.124   8.891  1.00 18.35  ? 32  VAL A O   1 
ATOM   242  C CB  . VAL A 1 32  ? 8.764   3.310   9.939  1.00 17.32  ? 32  VAL A CB  1 
ATOM   243  C CG1 . VAL A 1 32  ? 10.235  2.840   9.932  1.00 19.07  ? 32  VAL A CG1 1 
ATOM   244  C CG2 . VAL A 1 32  ? 8.687   4.720   9.415  1.00 11.33  ? 32  VAL A CG2 1 
ATOM   245  N N   . THR A 1 33  ? 7.395   0.541   10.622 1.00 16.23  ? 33  THR A N   1 
ATOM   246  C CA  . THR A 1 33  ? 7.577   -0.825  11.120 1.00 14.73  ? 33  THR A CA  1 
ATOM   247  C C   . THR A 1 33  ? 6.960   -1.864  10.175 1.00 19.11  ? 33  THR A C   1 
ATOM   248  O O   . THR A 1 33  ? 7.481   -2.987  10.063 1.00 20.63  ? 33  THR A O   1 
ATOM   249  C CB  . THR A 1 33  ? 7.003   -0.978  12.530 1.00 21.50  ? 33  THR A CB  1 
ATOM   250  O OG1 . THR A 1 33  ? 5.568   -0.924  12.496 1.00 22.24  ? 33  THR A OG1 1 
ATOM   251  C CG2 . THR A 1 33  ? 7.503   0.156   13.403 1.00 16.97  ? 33  THR A CG2 1 
ATOM   252  N N   . ILE A 1 34  ? 5.889   -1.505  9.458  1.00 14.58  ? 34  ILE A N   1 
ATOM   253  C CA  . ILE A 1 34  ? 5.294   -2.449  8.505  1.00 18.95  ? 34  ILE A CA  1 
ATOM   254  C C   . ILE A 1 34  ? 6.203   -2.646  7.295  1.00 22.88  ? 34  ILE A C   1 
ATOM   255  O O   . ILE A 1 34  ? 6.436   -3.780  6.858  1.00 21.31  ? 34  ILE A O   1 
ATOM   256  C CB  . ILE A 1 34  ? 3.885   -1.989  8.091  1.00 17.21  ? 34  ILE A CB  1 
ATOM   257  C CG1 . ILE A 1 34  ? 2.982   -1.935  9.321  1.00 15.92  ? 34  ILE A CG1 1 
ATOM   258  C CG2 . ILE A 1 34  ? 3.304   -2.882  7.019  1.00 16.26  ? 34  ILE A CG2 1 
ATOM   259  C CD1 . ILE A 1 34  ? 1.844   -0.975  9.168  1.00 20.66  ? 34  ILE A CD1 1 
ATOM   260  N N   . GLU A 1 35  ? 6.696   -1.551  6.716  1.00 17.96  ? 35  GLU A N   1 
ATOM   261  C CA  . GLU A 1 35  ? 7.650   -1.650  5.614  1.00 21.59  ? 35  GLU A CA  1 
ATOM   262  C C   . GLU A 1 35  ? 8.837   -2.517  6.015  1.00 17.60  ? 35  GLU A C   1 
ATOM   263  O O   . GLU A 1 35  ? 9.258   -3.406  5.257  1.00 21.78  ? 35  GLU A O   1 
ATOM   264  C CB  . GLU A 1 35  ? 8.114   -0.252  5.222  1.00 18.81  ? 35  GLU A CB  1 
ATOM   265  C CG  . GLU A 1 35  ? 6.989   0.585   4.656  1.00 25.39  ? 35  GLU A CG  1 
ATOM   266  C CD  . GLU A 1 35  ? 7.341   2.054   4.530  1.00 24.50  ? 35  GLU A CD  1 
ATOM   267  O OE1 . GLU A 1 35  ? 8.357   2.482   5.124  1.00 22.66  ? 35  GLU A OE1 1 
ATOM   268  O OE2 . GLU A 1 35  ? 6.601   2.781   3.827  1.00 29.80  ? 35  GLU A OE2 1 
ATOM   269  N N   . GLY A 1 36  ? 9.299   -2.359  7.259  1.00 15.61  ? 36  GLY A N   1 
ATOM   270  C CA  . GLY A 1 36  ? 10.456  -3.121  7.699  1.00 15.32  ? 36  GLY A CA  1 
ATOM   271  C C   . GLY A 1 36  ? 10.146  -4.597  7.803  1.00 18.21  ? 36  GLY A C   1 
ATOM   272  O O   . GLY A 1 36  ? 10.900  -5.431  7.295  1.00 19.63  ? 36  GLY A O   1 
ATOM   273  N N   . ILE A 1 37  ? 9.041   -4.944  8.468  1.00 26.98  ? 37  ILE A N   1 
ATOM   274  C CA  . ILE A 1 37  ? 8.764   -6.363  8.665  1.00 21.42  ? 37  ILE A CA  1 
ATOM   275  C C   . ILE A 1 37  ? 8.408   -7.040  7.340  1.00 23.35  ? 37  ILE A C   1 
ATOM   276  O O   . ILE A 1 37  ? 8.731   -8.217  7.141  1.00 23.70  ? 37  ILE A O   1 
ATOM   277  C CB  . ILE A 1 37  ? 7.665   -6.540  9.733  1.00 22.29  ? 37  ILE A CB  1 
ATOM   278  C CG1 . ILE A 1 37  ? 7.669   -7.967  10.281 1.00 22.46  ? 37  ILE A CG1 1 
ATOM   279  C CG2 . ILE A 1 37  ? 6.310   -6.161  9.180  1.00 20.98  ? 37  ILE A CG2 1 
ATOM   280  C CD1 . ILE A 1 37  ? 8.981   -8.363  10.907 1.00 22.07  ? 37  ILE A CD1 1 
ATOM   281  N N   . ILE A 1 38  ? 7.790   -6.317  6.394  1.00 24.69  ? 38  ILE A N   1 
ATOM   282  C CA  . ILE A 1 38  ? 7.495   -6.927  5.095  1.00 25.27  ? 38  ILE A CA  1 
ATOM   283  C C   . ILE A 1 38  ? 8.792   -7.185  4.333  1.00 22.83  ? 38  ILE A C   1 
ATOM   284  O O   . ILE A 1 38  ? 8.931   -8.209  3.656  1.00 26.20  ? 38  ILE A O   1 
ATOM   285  C CB  . ILE A 1 38  ? 6.492   -6.084  4.280  1.00 24.38  ? 38  ILE A CB  1 
ATOM   286  C CG1 . ILE A 1 38  ? 5.115   -6.066  4.958  1.00 20.42  ? 38  ILE A CG1 1 
ATOM   287  C CG2 . ILE A 1 38  ? 6.318   -6.661  2.869  1.00 18.93  ? 38  ILE A CG2 1 
ATOM   288  C CD1 . ILE A 1 38  ? 4.515   -7.445  5.246  1.00 14.38  ? 38  ILE A CD1 1 
ATOM   289  N N   . LYS A 1 39  ? 9.758   -6.265  4.417  1.00 21.02  ? 39  LYS A N   1 
ATOM   290  C CA  . LYS A 1 39  ? 11.050  -6.527  3.784  1.00 29.26  ? 39  LYS A CA  1 
ATOM   291  C C   . LYS A 1 39  ? 11.751  -7.717  4.433  1.00 25.05  ? 39  LYS A C   1 
ATOM   292  O O   . LYS A 1 39  ? 12.301  -8.588  3.746  1.00 24.21  ? 39  LYS A O   1 
ATOM   293  C CB  . LYS A 1 39  ? 11.957  -5.296  3.854  1.00 23.19  ? 39  LYS A CB  1 
ATOM   294  C CG  . LYS A 1 39  ? 13.422  -5.621  3.490  1.00 20.53  ? 39  LYS A CG  1 
ATOM   295  C CD  . LYS A 1 39  ? 13.586  -6.005  2.025  1.00 26.90  ? 39  LYS A CD  1 
ATOM   296  C CE  . LYS A 1 39  ? 15.044  -6.316  1.649  1.00 27.21  ? 39  LYS A CE  1 
ATOM   297  N NZ  . LYS A 1 39  ? 15.902  -6.655  2.823  1.00 25.23  ? 39  LYS A NZ  1 
ATOM   298  N N   . ILE A 1 40  ? 11.752  -7.756  5.762  1.00 21.22  ? 40  ILE A N   1 
ATOM   299  C CA  . ILE A 1 40  ? 12.404  -8.841  6.490  1.00 23.36  ? 40  ILE A CA  1 
ATOM   300  C C   . ILE A 1 40  ? 11.790  -10.197 6.144  1.00 20.87  ? 40  ILE A C   1 
ATOM   301  O O   . ILE A 1 40  ? 12.509  -11.188 5.962  1.00 18.73  ? 40  ILE A O   1 
ATOM   302  C CB  . ILE A 1 40  ? 12.362  -8.532  7.997  1.00 24.70  ? 40  ILE A CB  1 
ATOM   303  C CG1 . ILE A 1 40  ? 13.359  -7.414  8.301  1.00 15.34  ? 40  ILE A CG1 1 
ATOM   304  C CG2 . ILE A 1 40  ? 12.672  -9.767  8.829  1.00 29.12  ? 40  ILE A CG2 1 
ATOM   305  C CD1 . ILE A 1 40  ? 13.091  -6.720  9.598  1.00 19.42  ? 40  ILE A CD1 1 
ATOM   306  N N   . ARG A 1 41  ? 10.457  -10.270 6.052  1.00 23.02  ? 41  ARG A N   1 
ATOM   307  C CA  . ARG A 1 41  ? 9.786   -11.549 5.820  1.00 26.80  ? 41  ARG A CA  1 
ATOM   308  C C   . ARG A 1 41  ? 9.716   -11.944 4.346  1.00 30.81  ? 41  ARG A C   1 
ATOM   309  O O   . ARG A 1 41  ? 9.769   -13.142 4.037  1.00 31.54  ? 41  ARG A O   1 
ATOM   310  C CB  . ARG A 1 41  ? 8.371   -11.506 6.407  1.00 21.19  ? 41  ARG A CB  1 
ATOM   311  C CG  . ARG A 1 41  ? 8.357   -11.435 7.926  1.00 28.62  ? 41  ARG A CG  1 
ATOM   312  C CD  . ARG A 1 41  ? 8.786   -12.770 8.513  1.00 26.41  ? 41  ARG A CD  1 
ATOM   313  N NE  . ARG A 1 41  ? 8.831   -12.745 9.969  1.00 29.12  ? 41  ARG A NE  1 
ATOM   314  C CZ  . ARG A 1 41  ? 9.940   -12.548 10.670 1.00 34.98  ? 41  ARG A CZ  1 
ATOM   315  N NH1 . ARG A 1 41  ? 11.118  -12.422 10.079 1.00 33.98  ? 41  ARG A NH1 1 
ATOM   316  N NH2 . ARG A 1 41  ? 9.870   -12.502 11.998 1.00 28.25  ? 41  ARG A NH2 1 
ATOM   317  N N   . THR A 1 42  ? 9.642   -10.982 3.420  1.00 27.06  ? 42  THR A N   1 
ATOM   318  C CA  . THR A 1 42  ? 9.396   -11.300 2.021  1.00 30.02  ? 42  THR A CA  1 
ATOM   319  C C   . THR A 1 42  ? 10.539  -10.924 1.093  1.00 27.08  ? 42  THR A C   1 
ATOM   320  O O   . THR A 1 42  ? 10.563  -11.404 -0.048 1.00 32.10  ? 42  THR A O   1 
ATOM   321  C CB  . THR A 1 42  ? 8.112   -10.607 1.520  1.00 29.54  ? 42  THR A CB  1 
ATOM   322  O OG1 . THR A 1 42  ? 8.367   -9.214  1.282  1.00 28.18  ? 42  THR A OG1 1 
ATOM   323  C CG2 . THR A 1 42  ? 6.974   -10.751 2.528  1.00 24.93  ? 42  THR A CG2 1 
ATOM   324  N N   . GLY A 1 43  ? 11.486  -10.103 1.539  1.00 24.03  ? 43  GLY A N   1 
ATOM   325  C CA  . GLY A 1 43  ? 12.587  -9.685  0.705  1.00 22.53  ? 43  GLY A CA  1 
ATOM   326  C C   . GLY A 1 43  ? 12.341  -8.434  -0.108 1.00 28.00  ? 43  GLY A C   1 
ATOM   327  O O   . GLY A 1 43  ? 13.279  -7.937  -0.747 1.00 23.52  ? 43  GLY A O   1 
ATOM   328  N N   . ASN A 1 44  ? 11.127  -7.892  -0.085 1.00 25.22  ? 44  ASN A N   1 
ATOM   329  C CA  . ASN A 1 44  ? 10.775  -6.720  -0.875 1.00 28.45  ? 44  ASN A CA  1 
ATOM   330  C C   . ASN A 1 44  ? 10.531  -5.524  0.033  1.00 24.12  ? 44  ASN A C   1 
ATOM   331  O O   . ASN A 1 44  ? 9.827   -5.633  1.041  1.00 22.24  ? 44  ASN A O   1 
ATOM   332  C CB  . ASN A 1 44  ? 9.540   -6.984  -1.744 1.00 27.79  ? 44  ASN A CB  1 
ATOM   333  C CG  . ASN A 1 44  ? 9.699   -8.201  -2.641 1.00 32.83  ? 44  ASN A CG  1 
ATOM   334  O OD1 . ASN A 1 44  ? 10.729  -8.378  -3.303 1.00 33.51  ? 44  ASN A OD1 1 
ATOM   335  N ND2 . ASN A 1 44  ? 8.665   -9.034  -2.688 1.00 34.86  ? 44  ASN A ND2 1 
ATOM   336  N N   . LEU A 1 45  ? 11.127  -4.394  -0.324 1.00 26.83  ? 45  LEU A N   1 
ATOM   337  C CA  . LEU A 1 45  ? 10.884  -3.120  0.344  1.00 24.72  ? 45  LEU A CA  1 
ATOM   338  C C   . LEU A 1 45  ? 9.836   -2.336  -0.436 1.00 23.31  ? 45  LEU A C   1 
ATOM   339  O O   . LEU A 1 45  ? 10.081  -1.940  -1.580 1.00 30.28  ? 45  LEU A O   1 
ATOM   340  C CB  . LEU A 1 45  ? 12.173  -2.304  0.421  1.00 24.31  ? 45  LEU A CB  1 
ATOM   341  C CG  . LEU A 1 45  ? 12.083  -0.993  1.199  1.00 21.81  ? 45  LEU A CG  1 
ATOM   342  C CD1 . LEU A 1 45  ? 11.765  -1.233  2.678  1.00 13.77  ? 45  LEU A CD1 1 
ATOM   343  C CD2 . LEU A 1 45  ? 13.305  -0.112  0.986  1.00 22.35  ? 45  LEU A CD2 1 
ATOM   344  N N   . ASN A 1 46  ? 8.693   -2.084  0.191  1.00 25.27  ? 46  ASN A N   1 
ATOM   345  C CA  . ASN A 1 46  ? 7.622   -1.302  -0.410 1.00 19.68  ? 46  ASN A CA  1 
ATOM   346  C C   . ASN A 1 46  ? 7.280   -0.176  0.546  1.00 17.74  ? 46  ASN A C   1 
ATOM   347  O O   . ASN A 1 46  ? 7.571   -0.242  1.741  1.00 20.18  ? 46  ASN A O   1 
ATOM   348  C CB  . ASN A 1 46  ? 6.378   -2.142  -0.721 1.00 22.66  ? 46  ASN A CB  1 
ATOM   349  C CG  . ASN A 1 46  ? 6.716   -3.406  -1.471 1.00 28.73  ? 46  ASN A CG  1 
ATOM   350  O OD1 . ASN A 1 46  ? 6.712   -4.504  -0.915 1.00 24.05  ? 46  ASN A OD1 1 
ATOM   351  N ND2 . ASN A 1 46  ? 7.006   -3.256  -2.762 1.00 34.35  ? 46  ASN A ND2 1 
ATOM   352  N N   . GLU A 1 47  ? 6.646   0.858   0.014  1.00 21.84  ? 47  GLU A N   1 
ATOM   353  C CA  . GLU A 1 47  ? 6.106   1.922   0.841  1.00 17.73  ? 47  GLU A CA  1 
ATOM   354  C C   . GLU A 1 47  ? 4.619   1.690   1.050  1.00 17.66  ? 47  GLU A C   1 
ATOM   355  O O   . GLU A 1 47  ? 3.891   1.365   0.112  1.00 20.10  ? 47  GLU A O   1 
ATOM   356  C CB  . GLU A 1 47  ? 6.337   3.262   0.155  1.00 19.21  ? 47  GLU A CB  1 
ATOM   357  C CG  . GLU A 1 47  ? 7.780   3.662   0.162  1.00 22.47  ? 47  GLU A CG  1 
ATOM   358  C CD  . GLU A 1 47  ? 8.045   4.989   -0.516 1.00 29.45  ? 47  GLU A CD  1 
ATOM   359  O OE1 . GLU A 1 47  ? 7.260   5.360   -1.437 1.00 34.14  ? 47  GLU A OE1 1 
ATOM   360  O OE2 . GLU A 1 47  ? 9.051   5.641   -0.138 1.00 31.17  ? 47  GLU A OE2 1 
ATOM   361  N N   . TYR A 1 48  ? 4.160   1.868   2.282  1.00 17.21  ? 48  TYR A N   1 
ATOM   362  C CA  . TYR A 1 48  ? 2.765   1.653   2.600  1.00 13.90  ? 48  TYR A CA  1 
ATOM   363  C C   . TYR A 1 48  ? 2.124   2.953   3.050  1.00 16.08  ? 48  TYR A C   1 
ATOM   364  O O   . TYR A 1 48  ? 2.794   3.961   3.278  1.00 19.44  ? 48  TYR A O   1 
ATOM   365  C CB  . TYR A 1 48  ? 2.613   0.538   3.630  1.00 14.60  ? 48  TYR A CB  1 
ATOM   366  C CG  . TYR A 1 48  ? 3.065   -0.787  3.069  1.00 19.37  ? 48  TYR A CG  1 
ATOM   367  C CD1 . TYR A 1 48  ? 2.289   -1.461  2.128  1.00 15.93  ? 48  TYR A CD1 1 
ATOM   368  C CD2 . TYR A 1 48  ? 4.276   -1.347  3.445  1.00 16.30  ? 48  TYR A CD2 1 
ATOM   369  C CE1 . TYR A 1 48  ? 2.695   -2.669  1.607  1.00 19.14  ? 48  TYR A CE1 1 
ATOM   370  C CE2 . TYR A 1 48  ? 4.695   -2.548  2.928  1.00 16.60  ? 48  TYR A CE2 1 
ATOM   371  C CZ  . TYR A 1 48  ? 3.907   -3.204  2.004  1.00 23.40  ? 48  TYR A CZ  1 
ATOM   372  O OH  . TYR A 1 48  ? 4.329   -4.406  1.483  1.00 26.60  ? 48  TYR A OH  1 
ATOM   373  N N   . SER A 1 49  ? 0.799   2.917   3.188  1.00 20.70  ? 49  SER A N   1 
ATOM   374  C CA  . SER A 1 49  ? -0.013  4.133   3.248  1.00 16.11  ? 49  SER A CA  1 
ATOM   375  C C   . SER A 1 49  ? -0.205  4.619   4.680  1.00 13.11  ? 49  SER A C   1 
ATOM   376  O O   . SER A 1 49  ? -0.958  4.022   5.450  1.00 19.06  ? 49  SER A O   1 
ATOM   377  C CB  . SER A 1 49  ? -1.360  3.874   2.575  1.00 11.66  ? 49  SER A CB  1 
ATOM   378  O OG  . SER A 1 49  ? -2.187  5.021   2.640  1.00 18.88  ? 49  SER A OG  1 
ATOM   379  N N   . GLU A 1 50  ? 0.457   5.730   5.021  1.00 15.69  ? 50  GLU A N   1 
ATOM   380  C CA  . GLU A 1 50  ? 0.115   6.453   6.246  1.00 16.90  ? 50  GLU A CA  1 
ATOM   381  C C   . GLU A 1 50  ? -1.302  7.011   6.171  1.00 15.13  ? 50  GLU A C   1 
ATOM   382  O O   . GLU A 1 50  ? -2.026  7.029   7.176  1.00 14.01  ? 50  GLU A O   1 
ATOM   383  C CB  . GLU A 1 50  ? 1.109   7.597   6.485  1.00 15.95  ? 50  GLU A CB  1 
ATOM   384  C CG  . GLU A 1 50  ? 2.567   7.165   6.666  1.00 17.56  ? 50  GLU A CG  1 
ATOM   385  C CD  . GLU A 1 50  ? 3.364   7.159   5.355  1.00 25.55  ? 50  GLU A CD  1 
ATOM   386  O OE1 . GLU A 1 50  ? 4.475   6.578   5.332  1.00 23.44  ? 50  GLU A OE1 1 
ATOM   387  O OE2 . GLU A 1 50  ? 2.882   7.726   4.344  1.00 22.56  ? 50  GLU A OE2 1 
ATOM   388  N N   . GLN A 1 51  ? -1.712  7.479   4.987  1.00 13.46  ? 51  GLN A N   1 
ATOM   389  C CA  . GLN A 1 51  ? -3.033  8.086   4.841  1.00 20.16  ? 51  GLN A CA  1 
ATOM   390  C C   . GLN A 1 51  ? -4.138  7.086   5.168  1.00 22.27  ? 51  GLN A C   1 
ATOM   391  O O   . GLN A 1 51  ? -5.166  7.455   5.746  1.00 15.71  ? 51  GLN A O   1 
ATOM   392  C CB  . GLN A 1 51  ? -3.215  8.632   3.425  1.00 14.63  ? 51  GLN A CB  1 
ATOM   393  C CG  . GLN A 1 51  ? -4.521  9.360   3.218  1.00 13.62  ? 51  GLN A CG  1 
ATOM   394  C CD  . GLN A 1 51  ? -4.535  10.700  3.914  1.00 16.88  ? 51  GLN A CD  1 
ATOM   395  O OE1 . GLN A 1 51  ? -3.521  11.391  3.968  1.00 21.03  ? 51  GLN A OE1 1 
ATOM   396  N NE2 . GLN A 1 51  ? -5.682  11.070  4.465  1.00 19.58  ? 51  GLN A NE2 1 
ATOM   397  N N   . GLU A 1 52  ? -3.961  5.824   4.771  1.00 13.08  ? 52  GLU A N   1 
ATOM   398  C CA  . GLU A 1 52  ? -4.973  4.825   5.073  1.00 13.82  ? 52  GLU A CA  1 
ATOM   399  C C   . GLU A 1 52  ? -5.165  4.679   6.576  1.00 20.20  ? 52  GLU A C   1 
ATOM   400  O O   . GLU A 1 52  ? -6.300  4.609   7.059  1.00 22.50  ? 52  GLU A O   1 
ATOM   401  C CB  . GLU A 1 52  ? -4.589  3.490   4.439  1.00 17.83  ? 52  GLU A CB  1 
ATOM   402  C CG  . GLU A 1 52  ? -5.640  2.404   4.584  1.00 18.61  ? 52  GLU A CG  1 
ATOM   403  C CD  . GLU A 1 52  ? -5.359  1.239   3.674  1.00 19.53  ? 52  GLU A CD  1 
ATOM   404  O OE1 . GLU A 1 52  ? -4.183  1.054   3.303  1.00 23.58  ? 52  GLU A OE1 1 
ATOM   405  O OE2 . GLU A 1 52  ? -6.301  0.500   3.332  1.00 29.05  ? 52  GLU A OE2 1 
ATOM   406  N N   . LEU A 1 53  ? -4.069  4.644   7.335  1.00 21.08  ? 53  LEU A N   1 
ATOM   407  C CA  . LEU A 1 53  ? -4.198  4.533   8.784  1.00 19.73  ? 53  LEU A CA  1 
ATOM   408  C C   . LEU A 1 53  ? -4.812  5.798   9.369  1.00 18.77  ? 53  LEU A C   1 
ATOM   409  O O   . LEU A 1 53  ? -5.643  5.733   10.284 1.00 23.92  ? 53  LEU A O   1 
ATOM   410  C CB  . LEU A 1 53  ? -2.831  4.248   9.401  1.00 20.88  ? 53  LEU A CB  1 
ATOM   411  C CG  . LEU A 1 53  ? -2.097  3.017   8.844  1.00 27.15  ? 53  LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 53  ? -0.737  2.810   9.517  1.00 17.16  ? 53  LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 53  ? -2.973  1.781   9.028  1.00 18.76  ? 53  LEU A CD2 1 
ATOM   414  N N   . LEU A 1 54  ? -4.394  6.958   8.862  1.00 19.50  ? 54  LEU A N   1 
ATOM   415  C CA  . LEU A 1 54  ? -4.960  8.232   9.291  1.00 17.41  ? 54  LEU A CA  1 
ATOM   416  C C   . LEU A 1 54  ? -6.484  8.254   9.117  1.00 21.30  ? 54  LEU A C   1 
ATOM   417  O O   . LEU A 1 54  ? -7.219  8.674   10.016 1.00 21.75  ? 54  LEU A O   1 
ATOM   418  C CB  . LEU A 1 54  ? -4.286  9.357   8.510  1.00 16.05  ? 54  LEU A CB  1 
ATOM   419  C CG  . LEU A 1 54  ? -4.653  10.788  8.867  1.00 25.52  ? 54  LEU A CG  1 
ATOM   420  C CD1 . LEU A 1 54  ? -4.156  11.048  10.262 1.00 24.09  ? 54  LEU A CD1 1 
ATOM   421  C CD2 . LEU A 1 54  ? -3.991  11.746  7.896  1.00 27.65  ? 54  LEU A CD2 1 
ATOM   422  N N   . ASP A 1 55  ? -6.976  7.801   7.956  1.00 25.49  ? 55  ASP A N   1 
ATOM   423  C CA  . ASP A 1 55  ? -8.417  7.841   7.661  1.00 25.10  ? 55  ASP A CA  1 
ATOM   424  C C   . ASP A 1 55  ? -9.188  6.740   8.374  1.00 19.09  ? 55  ASP A C   1 
ATOM   425  O O   . ASP A 1 55  ? -10.335 6.956   8.773  1.00 18.34  ? 55  ASP A O   1 
ATOM   426  C CB  . ASP A 1 55  ? -8.685  7.754   6.156  1.00 18.33  ? 55  ASP A CB  1 
ATOM   427  C CG  . ASP A 1 55  ? -8.167  8.958   5.395  1.00 19.62  ? 55  ASP A CG  1 
ATOM   428  O OD1 . ASP A 1 55  ? -7.879  10.007  6.023  1.00 21.64  ? 55  ASP A OD1 1 
ATOM   429  O OD2 . ASP A 1 55  ? -8.027  8.832   4.158  1.00 22.83  ? 55  ASP A OD2 1 
ATOM   430  N N   . CYS A 1 56  ? -8.601  5.549   8.503  1.00 21.36  ? 56  CYS A N   1 
ATOM   431  C CA  . CYS A 1 56  ? -9.346  4.337   8.808  1.00 17.03  ? 56  CYS A CA  1 
ATOM   432  C C   . CYS A 1 56  ? -9.181  3.820   10.226 1.00 19.77  ? 56  CYS A C   1 
ATOM   433  O O   . CYS A 1 56  ? -9.996  2.996   10.652 1.00 18.49  ? 56  CYS A O   1 
ATOM   434  C CB  . CYS A 1 56  ? -8.963  3.207   7.844  1.00 13.40  ? 56  CYS A CB  1 
ATOM   435  S SG  . CYS A 1 56  ? -9.222  3.627   6.137  1.00 19.19  ? 56  CYS A SG  1 
ATOM   436  N N   . ASP A 1 57  ? -8.178  4.272   10.971 1.00 16.29  ? 57  ASP A N   1 
ATOM   437  C CA  . ASP A 1 57  ? -8.033  3.788   12.341 1.00 18.40  ? 57  ASP A CA  1 
ATOM   438  C C   . ASP A 1 57  ? -9.041  4.521   13.219 1.00 20.66  ? 57  ASP A C   1 
ATOM   439  O O   . ASP A 1 57  ? -8.808  5.654   13.650 1.00 22.31  ? 57  ASP A O   1 
ATOM   440  C CB  . ASP A 1 57  ? -6.612  3.983   12.846 1.00 20.52  ? 57  ASP A CB  1 
ATOM   441  C CG  . ASP A 1 57  ? -6.434  3.475   14.262 1.00 20.13  ? 57  ASP A CG  1 
ATOM   442  O OD1 . ASP A 1 57  ? -7.398  2.893   14.805 1.00 14.92  ? 57  ASP A OD1 1 
ATOM   443  O OD2 . ASP A 1 57  ? -5.341  3.681   14.841 1.00 18.08  ? 57  ASP A OD2 1 
ATOM   444  N N   . ARG A 1 58  ? -10.163 3.857   13.503 1.00 24.27  ? 58  ARG A N   1 
ATOM   445  C CA  . ARG A 1 58  ? -11.248 4.454   14.272 1.00 20.84  ? 58  ARG A CA  1 
ATOM   446  C C   . ARG A 1 58  ? -10.913 4.666   15.743 1.00 18.78  ? 58  ARG A C   1 
ATOM   447  O O   . ARG A 1 58  ? -11.634 5.411   16.416 1.00 21.51  ? 58  ARG A O   1 
ATOM   448  C CB  . ARG A 1 58  ? -12.502 3.594   14.118 1.00 20.82  ? 58  ARG A CB  1 
ATOM   449  C CG  . ARG A 1 58  ? -13.101 3.694   12.727 1.00 18.18  ? 58  ARG A CG  1 
ATOM   450  C CD  . ARG A 1 58  ? -14.261 2.743   12.507 1.00 18.29  ? 58  ARG A CD  1 
ATOM   451  N NE  . ARG A 1 58  ? -13.825 1.353   12.438 1.00 20.08  ? 58  ARG A NE  1 
ATOM   452  C CZ  . ARG A 1 58  ? -14.598 0.346   12.054 1.00 21.97  ? 58  ARG A CZ  1 
ATOM   453  N NH1 . ARG A 1 58  ? -15.863 0.539   11.708 1.00 17.96  ? 58  ARG A NH1 1 
ATOM   454  N NH2 . ARG A 1 58  ? -14.092 -0.884  12.016 1.00 15.29  ? 58  ARG A NH2 1 
ATOM   455  N N   . ARG A 1 59  ? -9.865  4.036   16.266 1.00 20.62  ? 59  ARG A N   1 
ATOM   456  C CA  . ARG A 1 59  ? -9.437  4.323   17.630 1.00 21.33  ? 59  ARG A CA  1 
ATOM   457  C C   . ARG A 1 59  ? -8.517  5.528   17.714 1.00 22.36  ? 59  ARG A C   1 
ATOM   458  O O   . ARG A 1 59  ? -8.218  5.981   18.824 1.00 28.93  ? 59  ARG A O   1 
ATOM   459  C CB  . ARG A 1 59  ? -8.728  3.116   18.251 1.00 14.07  ? 59  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 59  ? -9.467  1.798   18.071 1.00 31.83  ? 59  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 59  ? -8.781  0.638   18.809 1.00 40.29  ? 59  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 59  ? -9.732  -0.219  19.507 1.00 47.00  ? 59  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 59  ? -10.315 -1.283  18.970 1.00 63.09  ? 59  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 59  ? -10.076 -1.648  17.719 1.00 73.28  ? 59  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 59  ? -11.163 -1.998  19.705 1.00 44.04  ? 59  ARG A NH2 1 
ATOM   466  N N   . SER A 1 60  ? -8.056  6.047   16.578 1.00 21.86  ? 60  SER A N   1 
ATOM   467  C CA  . SER A 1 60  ? -7.193  7.213   16.539 1.00 19.49  ? 60  SER A CA  1 
ATOM   468  C C   . SER A 1 60  ? -8.014  8.449   16.197 1.00 15.78  ? 60  SER A C   1 
ATOM   469  O O   . SER A 1 60  ? -9.209  8.376   15.908 1.00 20.12  ? 60  SER A O   1 
ATOM   470  C CB  . SER A 1 60  ? -6.058  7.004   15.540 1.00 17.76  ? 60  SER A CB  1 
ATOM   471  O OG  . SER A 1 60  ? -5.125  6.055   16.021 1.00 18.24  ? 60  SER A OG  1 
ATOM   472  N N   . TYR A 1 61  ? -7.360  9.605   16.221 1.00 19.65  ? 61  TYR A N   1 
ATOM   473  C CA  . TYR A 1 61  ? -8.060  10.876  16.113 1.00 21.51  ? 61  TYR A CA  1 
ATOM   474  C C   . TYR A 1 61  ? -7.574  11.691  14.920 1.00 21.10  ? 61  TYR A C   1 
ATOM   475  O O   . TYR A 1 61  ? -7.546  12.925  14.968 1.00 18.62  ? 61  TYR A O   1 
ATOM   476  C CB  . TYR A 1 61  ? -7.932  11.651  17.424 1.00 21.76  ? 61  TYR A CB  1 
ATOM   477  C CG  . TYR A 1 61  ? -8.525  10.875  18.586 1.00 27.82  ? 61  TYR A CG  1 
ATOM   478  C CD1 . TYR A 1 61  ? -7.714  10.162  19.464 1.00 28.97  ? 61  TYR A CD1 1 
ATOM   479  C CD2 . TYR A 1 61  ? -9.904  10.813  18.775 1.00 32.27  ? 61  TYR A CD2 1 
ATOM   480  C CE1 . TYR A 1 61  ? -8.260  9.430   20.519 1.00 26.93  ? 61  TYR A CE1 1 
ATOM   481  C CE2 . TYR A 1 61  ? -10.457 10.086  19.824 1.00 34.25  ? 61  TYR A CE2 1 
ATOM   482  C CZ  . TYR A 1 61  ? -9.632  9.395   20.689 1.00 33.64  ? 61  TYR A CZ  1 
ATOM   483  O OH  . TYR A 1 61  ? -10.191 8.682   21.728 1.00 35.96  ? 61  TYR A OH  1 
ATOM   484  N N   . GLY A 1 62  ? -7.217  11.000  13.837 1.00 16.39  ? 62  GLY A N   1 
ATOM   485  C CA  . GLY A 1 62  ? -6.819  11.675  12.612 1.00 18.73  ? 62  GLY A CA  1 
ATOM   486  C C   . GLY A 1 62  ? -5.582  12.513  12.835 1.00 17.94  ? 62  GLY A C   1 
ATOM   487  O O   . GLY A 1 62  ? -4.578  12.042  13.379 1.00 20.48  ? 62  GLY A O   1 
ATOM   488  N N   . CYS A 1 63  ? -5.641  13.769  12.395 1.00 21.48  ? 63  CYS A N   1 
ATOM   489  C CA  . CYS A 1 63  ? -4.530  14.697  12.567 1.00 18.47  ? 63  CYS A CA  1 
ATOM   490  C C   . CYS A 1 63  ? -4.438  15.238  13.983 1.00 21.06  ? 63  CYS A C   1 
ATOM   491  O O   . CYS A 1 63  ? -3.529  16.023  14.275 1.00 24.68  ? 63  CYS A O   1 
ATOM   492  C CB  . CYS A 1 63  ? -4.631  15.861  11.575 1.00 14.42  ? 63  CYS A CB  1 
ATOM   493  S SG  . CYS A 1 63  ? -4.329  15.399  9.882  1.00 20.71  ? 63  CYS A SG  1 
ATOM   494  N N   . ASN A 1 64  ? -5.346  14.842  14.864 1.00 20.21  ? 64  ASN A N   1 
ATOM   495  C CA  . ASN A 1 64  ? -5.272  15.227  16.261 1.00 26.10  ? 64  ASN A CA  1 
ATOM   496  C C   . ASN A 1 64  ? -4.537  14.205  17.104 1.00 28.56  ? 64  ASN A C   1 
ATOM   497  O O   . ASN A 1 64  ? -4.584  14.286  18.336 1.00 36.01  ? 64  ASN A O   1 
ATOM   498  C CB  . ASN A 1 64  ? -6.679  15.441  16.817 1.00 32.00  ? 64  ASN A CB  1 
ATOM   499  C CG  . ASN A 1 64  ? -7.355  16.668  16.236 1.00 35.97  ? 64  ASN A CG  1 
ATOM   500  O OD1 . ASN A 1 64  ? -6.694  17.632  15.853 1.00 35.21  ? 64  ASN A OD1 1 
ATOM   501  N ND2 . ASN A 1 64  ? -8.681  16.633  16.158 1.00 47.93  ? 64  ASN A ND2 1 
ATOM   502  N N   . GLY A 1 65  ? -3.854  13.260  16.477 1.00 22.21  ? 65  GLY A N   1 
ATOM   503  C CA  . GLY A 1 65  ? -3.055  12.290  17.193 1.00 22.83  ? 65  GLY A CA  1 
ATOM   504  C C   . GLY A 1 65  ? -3.701  10.920  17.127 1.00 20.40  ? 65  GLY A C   1 
ATOM   505  O O   . GLY A 1 65  ? -4.791  10.737  16.584 1.00 20.41  ? 65  GLY A O   1 
ATOM   506  N N   . GLY A 1 66  ? -3.008  9.951   17.705 1.00 19.75  ? 66  GLY A N   1 
ATOM   507  C CA  . GLY A 1 66  ? -3.453  8.583   17.569 1.00 17.72  ? 66  GLY A CA  1 
ATOM   508  C C   . GLY A 1 66  ? -2.484  7.636   18.226 1.00 17.39  ? 66  GLY A C   1 
ATOM   509  O O   . GLY A 1 66  ? -1.597  8.044   18.978 1.00 24.79  ? 66  GLY A O   1 
ATOM   510  N N   . TYR A 1 67  ? -2.670  6.354   17.926 1.00 17.71  ? 67  TYR A N   1 
ATOM   511  C CA  . TYR A 1 67  ? -2.012  5.280   18.659 1.00 22.71  ? 67  TYR A CA  1 
ATOM   512  C C   . TYR A 1 67  ? -1.299  4.376   17.664 1.00 19.90  ? 67  TYR A C   1 
ATOM   513  O O   . TYR A 1 67  ? -1.963  3.771   16.797 1.00 19.00  ? 67  TYR A O   1 
ATOM   514  C CB  . TYR A 1 67  ? -3.026  4.493   19.482 1.00 22.10  ? 67  TYR A CB  1 
ATOM   515  C CG  . TYR A 1 67  ? -3.846  5.365   20.402 1.00 23.63  ? 67  TYR A CG  1 
ATOM   516  C CD1 . TYR A 1 67  ? -3.320  5.845   21.593 1.00 27.80  ? 67  TYR A CD1 1 
ATOM   517  C CD2 . TYR A 1 67  ? -5.156  5.692   20.085 1.00 27.75  ? 67  TYR A CD2 1 
ATOM   518  C CE1 . TYR A 1 67  ? -4.073  6.643   22.438 1.00 37.32  ? 67  TYR A CE1 1 
ATOM   519  C CE2 . TYR A 1 67  ? -5.924  6.485   20.927 1.00 33.27  ? 67  TYR A CE2 1 
ATOM   520  C CZ  . TYR A 1 67  ? -5.377  6.955   22.102 1.00 36.72  ? 67  TYR A CZ  1 
ATOM   521  O OH  . TYR A 1 67  ? -6.135  7.744   22.937 1.00 37.04  ? 67  TYR A OH  1 
ATOM   522  N N   . PRO A 1 68  ? 0.029   4.286   17.707 1.00 13.36  ? 68  PRO A N   1 
ATOM   523  C CA  . PRO A 1 68  ? 0.723   3.306   16.855 1.00 13.76  ? 68  PRO A CA  1 
ATOM   524  C C   . PRO A 1 68  ? 0.218   1.879   17.023 1.00 20.10  ? 68  PRO A C   1 
ATOM   525  O O   . PRO A 1 68  ? 0.137   1.134   16.031 1.00 20.61  ? 68  PRO A O   1 
ATOM   526  C CB  . PRO A 1 68  ? 2.188   3.446   17.296 1.00 19.83  ? 68  PRO A CB  1 
ATOM   527  C CG  . PRO A 1 68  ? 2.294   4.866   17.788 1.00 15.62  ? 68  PRO A CG  1 
ATOM   528  C CD  . PRO A 1 68  ? 0.964   5.147   18.453 1.00 16.73  ? 68  PRO A CD  1 
ATOM   529  N N   . TRP A 1 69  ? -0.105  1.463   18.253 1.00 15.08  ? 69  TRP A N   1 
ATOM   530  C CA  . TRP A 1 69  ? -0.580  0.098   18.439 1.00 18.90  ? 69  TRP A CA  1 
ATOM   531  C C   . TRP A 1 69  ? -1.908  -0.108  17.724 1.00 22.67  ? 69  TRP A C   1 
ATOM   532  O O   . TRP A 1 69  ? -2.160  -1.180  17.164 1.00 28.16  ? 69  TRP A O   1 
ATOM   533  C CB  . TRP A 1 69  ? -0.702  -0.253  19.930 1.00 25.72  ? 69  TRP A CB  1 
ATOM   534  C CG  . TRP A 1 69  ? -1.637  0.630   20.718 1.00 33.14  ? 69  TRP A CG  1 
ATOM   535  C CD1 . TRP A 1 69  ? -1.289  1.716   21.479 1.00 38.51  ? 69  TRP A CD1 1 
ATOM   536  C CD2 . TRP A 1 69  ? -3.067  0.505   20.828 1.00 30.37  ? 69  TRP A CD2 1 
ATOM   537  N NE1 . TRP A 1 69  ? -2.413  2.274   22.050 1.00 40.72  ? 69  TRP A NE1 1 
ATOM   538  C CE2 . TRP A 1 69  ? -3.516  1.556   21.665 1.00 35.61  ? 69  TRP A CE2 1 
ATOM   539  C CE3 . TRP A 1 69  ? -4.009  -0.391  20.306 1.00 29.67  ? 69  TRP A CE3 1 
ATOM   540  C CZ2 . TRP A 1 69  ? -4.867  1.741   21.981 1.00 34.49  ? 69  TRP A CZ2 1 
ATOM   541  C CZ3 . TRP A 1 69  ? -5.352  -0.203  20.622 1.00 37.95  ? 69  TRP A CZ3 1 
ATOM   542  C CH2 . TRP A 1 69  ? -5.766  0.855   21.453 1.00 33.85  ? 69  TRP A CH2 1 
ATOM   543  N N   . SER A 1 70  ? -2.755  0.917   17.698 1.00 22.18  ? 70  SER A N   1 
ATOM   544  C CA  . SER A 1 70  ? -4.049  0.778   17.036 1.00 24.06  ? 70  SER A CA  1 
ATOM   545  C C   . SER A 1 70  ? -3.891  0.690   15.526 1.00 20.90  ? 70  SER A C   1 
ATOM   546  O O   . SER A 1 70  ? -4.572  -0.105  14.870 1.00 26.04  ? 70  SER A O   1 
ATOM   547  C CB  . SER A 1 70  ? -4.956  1.945   17.415 1.00 19.96  ? 70  SER A CB  1 
ATOM   548  O OG  . SER A 1 70  ? -6.301  1.545   17.372 1.00 30.06  ? 70  SER A OG  1 
ATOM   549  N N   . ALA A 1 71  ? -3.004  1.501   14.956 1.00 16.04  ? 71  ALA A N   1 
ATOM   550  C CA  . ALA A 1 71  ? -2.714  1.408   13.529 1.00 16.58  ? 71  ALA A CA  1 
ATOM   551  C C   . ALA A 1 71  ? -2.136  0.044   13.163 1.00 17.98  ? 71  ALA A C   1 
ATOM   552  O O   . ALA A 1 71  ? -2.487  -0.539  12.124 1.00 20.34  ? 71  ALA A O   1 
ATOM   553  C CB  . ALA A 1 71  ? -1.760  2.527   13.117 1.00 16.16  ? 71  ALA A CB  1 
ATOM   554  N N   . LEU A 1 72  ? -1.269  -0.500  14.016 1.00 14.87  ? 72  LEU A N   1 
ATOM   555  C CA  . LEU A 1 72  ? -0.707  -1.809  13.704 1.00 22.57  ? 72  LEU A CA  1 
ATOM   556  C C   . LEU A 1 72  ? -1.766  -2.899  13.829 1.00 23.11  ? 72  LEU A C   1 
ATOM   557  O O   . LEU A 1 72  ? -1.805  -3.840  13.022 1.00 20.50  ? 72  LEU A O   1 
ATOM   558  C CB  . LEU A 1 72  ? 0.473   -2.096  14.632 1.00 18.43  ? 72  LEU A CB  1 
ATOM   559  C CG  . LEU A 1 72  ? 1.726   -1.271  14.341 1.00 24.61  ? 72  LEU A CG  1 
ATOM   560  C CD1 . LEU A 1 72  ? 2.812   -1.508  15.395 1.00 14.18  ? 72  LEU A CD1 1 
ATOM   561  C CD2 . LEU A 1 72  ? 2.231   -1.498  12.911 1.00 16.18  ? 72  LEU A CD2 1 
ATOM   562  N N   . GLN A 1 73  ? -2.646  -2.773  14.824 1.00 25.42  ? 73  GLN A N   1 
ATOM   563  C CA  . GLN A 1 73  ? -3.766  -3.691  14.959 1.00 25.26  ? 73  GLN A CA  1 
ATOM   564  C C   . GLN A 1 73  ? -4.681  -3.609  13.744 1.00 25.08  ? 73  GLN A C   1 
ATOM   565  O O   . GLN A 1 73  ? -5.209  -4.628  13.281 1.00 27.10  ? 73  GLN A O   1 
ATOM   566  C CB  . GLN A 1 73  ? -4.511  -3.379  16.260 1.00 30.01  ? 73  GLN A CB  1 
ATOM   567  C CG  . GLN A 1 73  ? -5.906  -3.972  16.400 1.00 44.89  ? 73  GLN A CG  1 
ATOM   568  C CD  . GLN A 1 73  ? -6.835  -3.056  17.193 1.00 69.49  ? 73  GLN A CD  1 
ATOM   569  O OE1 . GLN A 1 73  ? -7.298  -2.028  16.686 1.00 58.07  ? 73  GLN A OE1 1 
ATOM   570  N NE2 . GLN A 1 73  ? -7.098  -3.418  18.445 1.00 68.46  ? 73  GLN A NE2 1 
ATOM   571  N N   . LEU A 1 74  ? -4.856  -2.407  13.197 1.00 19.16  ? 74  LEU A N   1 
ATOM   572  C CA  . LEU A 1 74  ? -5.648  -2.255  11.983 1.00 20.54  ? 74  LEU A CA  1 
ATOM   573  C C   . LEU A 1 74  ? -5.012  -2.995  10.818 1.00 22.79  ? 74  LEU A C   1 
ATOM   574  O O   . LEU A 1 74  ? -5.711  -3.648  10.036 1.00 26.10  ? 74  LEU A O   1 
ATOM   575  C CB  . LEU A 1 74  ? -5.820  -0.774  11.648 1.00 22.95  ? 74  LEU A CB  1 
ATOM   576  C CG  . LEU A 1 74  ? -6.744  -0.385  10.488 1.00 26.35  ? 74  LEU A CG  1 
ATOM   577  C CD1 . LEU A 1 74  ? -8.163  -0.857  10.739 1.00 29.68  ? 74  LEU A CD1 1 
ATOM   578  C CD2 . LEU A 1 74  ? -6.733  1.124   10.286 1.00 23.41  ? 74  LEU A CD2 1 
ATOM   579  N N   . VAL A 1 75  ? -3.684  -2.908  10.685 1.00 22.51  ? 75  VAL A N   1 
ATOM   580  C CA  . VAL A 1 75  ? -3.021  -3.614  9.587  1.00 19.92  ? 75  VAL A CA  1 
ATOM   581  C C   . VAL A 1 75  ? -3.070  -5.125  9.786  1.00 23.85  ? 75  VAL A C   1 
ATOM   582  O O   . VAL A 1 75  ? -3.139  -5.882  8.810  1.00 28.31  ? 75  VAL A O   1 
ATOM   583  C CB  . VAL A 1 75  ? -1.574  -3.119  9.422  1.00 22.33  ? 75  VAL A CB  1 
ATOM   584  C CG1 . VAL A 1 75  ? -0.857  -3.847  8.268  1.00 17.03  ? 75  VAL A CG1 1 
ATOM   585  C CG2 . VAL A 1 75  ? -1.585  -1.634  9.186  1.00 22.25  ? 75  VAL A CG2 1 
ATOM   586  N N   . ALA A 1 76  ? -3.075  -5.597  11.032 1.00 26.44  ? 76  ALA A N   1 
ATOM   587  C CA  . ALA A 1 76  ? -3.165  -7.043  11.228 1.00 27.14  ? 76  ALA A CA  1 
ATOM   588  C C   . ALA A 1 76  ? -4.588  -7.554  11.029 1.00 29.16  ? 76  ALA A C   1 
ATOM   589  O O   . ALA A 1 76  ? -4.772  -8.683  10.559 1.00 32.04  ? 76  ALA A O   1 
ATOM   590  C CB  . ALA A 1 76  ? -2.654  -7.433  12.615 1.00 19.70  ? 76  ALA A CB  1 
ATOM   591  N N   . GLN A 1 77  ? -5.594  -6.733  11.348 1.00 23.59  ? 77  GLN A N   1 
ATOM   592  C CA  . GLN A 1 77  ? -6.993  -7.141  11.245 1.00 31.38  ? 77  GLN A CA  1 
ATOM   593  C C   . GLN A 1 77  ? -7.478  -7.117  9.801  1.00 36.86  ? 77  GLN A C   1 
ATOM   594  O O   . GLN A 1 77  ? -8.158  -8.045  9.345  1.00 30.04  ? 77  GLN A O   1 
ATOM   595  C CB  . GLN A 1 77  ? -7.865  -6.226  12.105 1.00 35.81  ? 77  GLN A CB  1 
ATOM   596  C CG  . GLN A 1 77  ? -9.182  -6.841  12.529 1.00 54.90  ? 77  GLN A CG  1 
ATOM   597  C CD  . GLN A 1 77  ? -10.290 -5.816  12.644 1.00 77.25  ? 77  GLN A CD  1 
ATOM   598  O OE1 . GLN A 1 77  ? -11.427 -6.064  12.240 1.00 82.78  ? 77  GLN A OE1 1 
ATOM   599  N NE2 . GLN A 1 77  ? -9.959  -4.646  13.184 1.00 76.13  ? 77  GLN A NE2 1 
ATOM   600  N N   . TYR A 1 78  ? -7.146  -6.050  9.077  1.00 32.03  ? 78  TYR A N   1 
ATOM   601  C CA  . TYR A 1 78  ? -7.552  -5.877  7.688  1.00 30.76  ? 78  TYR A CA  1 
ATOM   602  C C   . TYR A 1 78  ? -6.341  -5.961  6.767  1.00 32.25  ? 78  TYR A C   1 
ATOM   603  O O   . TYR A 1 78  ? -6.202  -6.931  6.019  1.00 36.30  ? 78  TYR A O   1 
ATOM   604  C CB  . TYR A 1 78  ? -8.307  -4.564  7.495  1.00 29.21  ? 78  TYR A CB  1 
ATOM   605  C CG  . TYR A 1 78  ? -9.568  -4.494  8.318  1.00 41.36  ? 78  TYR A CG  1 
ATOM   606  C CD1 . TYR A 1 78  ? -10.754 -5.074  7.872  1.00 41.67  ? 78  TYR A CD1 1 
ATOM   607  C CD2 . TYR A 1 78  ? -9.584  -3.818  9.527  1.00 43.41  ? 78  TYR A CD2 1 
ATOM   608  C CE1 . TYR A 1 78  ? -11.912 -5.007  8.630  1.00 38.04  ? 78  TYR A CE1 1 
ATOM   609  C CE2 . TYR A 1 78  ? -10.735 -3.731  10.280 1.00 50.81  ? 78  TYR A CE2 1 
ATOM   610  C CZ  . TYR A 1 78  ? -11.895 -4.329  9.834  1.00 51.74  ? 78  TYR A CZ  1 
ATOM   611  O OH  . TYR A 1 78  ? -13.034 -4.243  10.604 1.00 44.67  ? 78  TYR A OH  1 
ATOM   612  N N   . GLY A 1 79  ? -5.466  -4.971  6.801  1.00 29.79  ? 79  GLY A N   1 
ATOM   613  C CA  . GLY A 1 79  ? -4.327  -4.914  5.911  1.00 27.73  ? 79  GLY A CA  1 
ATOM   614  C C   . GLY A 1 79  ? -4.006  -3.462  5.621  1.00 28.72  ? 79  GLY A C   1 
ATOM   615  O O   . GLY A 1 79  ? -4.537  -2.556  6.256  1.00 24.08  ? 79  GLY A O   1 
ATOM   616  N N   . ILE A 1 80  ? -3.151  -3.251  4.621  1.00 25.68  ? 80  ILE A N   1 
ATOM   617  C CA  . ILE A 1 80  ? -2.740  -1.899  4.264  1.00 23.01  ? 80  ILE A CA  1 
ATOM   618  C C   . ILE A 1 80  ? -2.431  -1.854  2.777  1.00 19.34  ? 80  ILE A C   1 
ATOM   619  O O   . ILE A 1 80  ? -1.961  -2.829  2.187  1.00 24.77  ? 80  ILE A O   1 
ATOM   620  C CB  . ILE A 1 80  ? -1.515  -1.447  5.097  1.00 23.65  ? 80  ILE A CB  1 
ATOM   621  C CG1 . ILE A 1 80  ? -1.279  0.056   4.940  1.00 20.73  ? 80  ILE A CG1 1 
ATOM   622  C CG2 . ILE A 1 80  ? -0.273  -2.256  4.721  1.00 21.30  ? 80  ILE A CG2 1 
ATOM   623  C CD1 . ILE A 1 80  ? -0.332  0.622   5.978  1.00 20.61  ? 80  ILE A CD1 1 
ATOM   624  N N   . HIS A 1 81  ? -2.711  -0.706  2.174  1.00 20.58  ? 81  HIS A N   1 
ATOM   625  C CA  . HIS A 1 81  ? -2.441  -0.475  0.766  1.00 19.56  ? 81  HIS A CA  1 
ATOM   626  C C   . HIS A 1 81  ? -1.073  0.161   0.568  1.00 14.71  ? 81  HIS A C   1 
ATOM   627  O O   . HIS A 1 81  ? -0.496  0.766   1.476  1.00 18.69  ? 81  HIS A O   1 
ATOM   628  C CB  . HIS A 1 81  ? -3.533  0.419   0.165  1.00 19.12  ? 81  HIS A CB  1 
ATOM   629  C CG  . HIS A 1 81  ? -4.839  -0.286  -0.044 1.00 17.96  ? 81  HIS A CG  1 
ATOM   630  N ND1 . HIS A 1 81  ? -5.835  -0.308  0.909  1.00 18.94  ? 81  HIS A ND1 1 
ATOM   631  C CD2 . HIS A 1 81  ? -5.321  -0.975  -1.106 1.00 21.87  ? 81  HIS A CD2 1 
ATOM   632  C CE1 . HIS A 1 81  ? -6.865  -0.997  0.451  1.00 20.06  ? 81  HIS A CE1 1 
ATOM   633  N NE2 . HIS A 1 81  ? -6.580  -1.410  -0.771 1.00 21.08  ? 81  HIS A NE2 1 
ATOM   634  N N   . TYR A 1 82  ? -0.573  0.035   -0.654 1.00 14.97  ? 82  TYR A N   1 
ATOM   635  C CA  . TYR A 1 82  ? 0.645   0.722   -1.048 1.00 17.86  ? 82  TYR A CA  1 
ATOM   636  C C   . TYR A 1 82  ? 0.454   2.228   -0.947 1.00 22.14  ? 82  TYR A C   1 
ATOM   637  O O   . TYR A 1 82  ? -0.657  2.749   -1.083 1.00 25.36  ? 82  TYR A O   1 
ATOM   638  C CB  . TYR A 1 82  ? 1.024   0.357   -2.473 1.00 17.01  ? 82  TYR A CB  1 
ATOM   639  C CG  . TYR A 1 82  ? 1.548   -1.043  -2.644 1.00 19.13  ? 82  TYR A CG  1 
ATOM   640  C CD1 . TYR A 1 82  ? 2.573   -1.534  -1.844 1.00 20.59  ? 82  TYR A CD1 1 
ATOM   641  C CD2 . TYR A 1 82  ? 1.019   -1.875  -3.620 1.00 16.18  ? 82  TYR A CD2 1 
ATOM   642  C CE1 . TYR A 1 82  ? 3.053   -2.822  -2.019 1.00 22.32  ? 82  TYR A CE1 1 
ATOM   643  C CE2 . TYR A 1 82  ? 1.488   -3.158  -3.798 1.00 24.63  ? 82  TYR A CE2 1 
ATOM   644  C CZ  . TYR A 1 82  ? 2.505   -3.625  -3.003 1.00 19.48  ? 82  TYR A CZ  1 
ATOM   645  O OH  . TYR A 1 82  ? 2.958   -4.904  -3.189 1.00 29.05  ? 82  TYR A OH  1 
ATOM   646  N N   . ARG A 1 83  ? 1.550   2.929   -0.687 1.00 11.43  ? 83  ARG A N   1 
ATOM   647  C CA  . ARG A 1 83  ? 1.462   4.372   -0.580 1.00 14.84  ? 83  ARG A CA  1 
ATOM   648  C C   . ARG A 1 83  ? 0.969   4.998   -1.881 1.00 18.92  ? 83  ARG A C   1 
ATOM   649  O O   . ARG A 1 83  ? 0.173   5.943   -1.848 1.00 17.66  ? 83  ARG A O   1 
ATOM   650  C CB  . ARG A 1 83  ? 2.816   4.934   -0.156 1.00 26.74  ? 83  ARG A CB  1 
ATOM   651  C CG  . ARG A 1 83  ? 2.742   6.299   0.488  1.00 26.04  ? 83  ARG A CG  1 
ATOM   652  C CD  . ARG A 1 83  ? 4.122   6.781   0.909  1.00 32.41  ? 83  ARG A CD  1 
ATOM   653  N NE  . ARG A 1 83  ? 4.028   7.806   1.943  1.00 32.88  ? 83  ARG A NE  1 
ATOM   654  C CZ  . ARG A 1 83  ? 4.520   9.031   1.825  1.00 27.19  ? 83  ARG A CZ  1 
ATOM   655  N NH1 . ARG A 1 83  ? 5.190   9.402   0.749  1.00 22.45  ? 83  ARG A NH1 1 
ATOM   656  N NH2 . ARG A 1 83  ? 4.337   9.902   2.812  1.00 24.77  ? 83  ARG A NH2 1 
ATOM   657  N N   . ASN A 1 84  ? 1.422   4.487   -3.036 1.00 22.07  ? 84  ASN A N   1 
ATOM   658  C CA  . ASN A 1 84  ? 0.943   5.014   -4.317 1.00 25.17  ? 84  ASN A CA  1 
ATOM   659  C C   . ASN A 1 84  ? -0.571  4.924   -4.398 1.00 23.60  ? 84  ASN A C   1 
ATOM   660  O O   . ASN A 1 84  ? -1.247  5.876   -4.807 1.00 21.97  ? 84  ASN A O   1 
ATOM   661  C CB  . ASN A 1 84  ? 1.548   4.254   -5.502 1.00 28.44  ? 84  ASN A CB  1 
ATOM   662  C CG  . ASN A 1 84  ? 2.989   3.882   -5.291 1.00 52.39  ? 84  ASN A CG  1 
ATOM   663  O OD1 . ASN A 1 84  ? 3.324   3.132   -4.371 1.00 54.88  ? 84  ASN A OD1 1 
ATOM   664  N ND2 . ASN A 1 84  ? 3.861   4.388   -6.159 1.00 65.05  ? 84  ASN A ND2 1 
ATOM   665  N N   . THR A 1 85  ? -1.115  3.766   -4.023 1.00 17.59  ? 85  THR A N   1 
ATOM   666  C CA  . THR A 1 85  ? -2.552  3.541   -4.112 1.00 15.98  ? 85  THR A CA  1 
ATOM   667  C C   . THR A 1 85  ? -3.327  4.497   -3.216 1.00 16.66  ? 85  THR A C   1 
ATOM   668  O O   . THR A 1 85  ? -4.481  4.834   -3.513 1.00 15.83  ? 85  THR A O   1 
ATOM   669  C CB  . THR A 1 85  ? -2.863  2.083   -3.761 1.00 21.16  ? 85  THR A CB  1 
ATOM   670  O OG1 . THR A 1 85  ? -2.045  1.220   -4.564 1.00 13.98  ? 85  THR A OG1 1 
ATOM   671  C CG2 . THR A 1 85  ? -4.327  1.760   -4.021 1.00 15.07  ? 85  THR A CG2 1 
ATOM   672  N N   . TYR A 1 86  ? -2.720  4.934   -2.113 1.00 15.21  ? 86  TYR A N   1 
ATOM   673  C CA  . TYR A 1 86  ? -3.413  5.676   -1.058 1.00 14.98  ? 86  TYR A CA  1 
ATOM   674  C C   . TYR A 1 86  ? -2.441  6.729   -0.543 1.00 14.32  ? 86  TYR A C   1 
ATOM   675  O O   . TYR A 1 86  ? -1.951  6.652   0.589  1.00 12.20  ? 86  TYR A O   1 
ATOM   676  C CB  . TYR A 1 86  ? -3.869  4.708   0.037  1.00 12.56  ? 86  TYR A CB  1 
ATOM   677  C CG  . TYR A 1 86  ? -5.055  5.111   0.886  1.00 13.16  ? 86  TYR A CG  1 
ATOM   678  C CD1 . TYR A 1 86  ? -5.328  6.436   1.174  1.00 12.22  ? 86  TYR A CD1 1 
ATOM   679  C CD2 . TYR A 1 86  ? -5.909  4.134   1.403  1.00 17.05  ? 86  TYR A CD2 1 
ATOM   680  C CE1 . TYR A 1 86  ? -6.418  6.781   1.958  1.00 17.20  ? 86  TYR A CE1 1 
ATOM   681  C CE2 . TYR A 1 86  ? -6.998  4.463   2.183  1.00 15.24  ? 86  TYR A CE2 1 
ATOM   682  C CZ  . TYR A 1 86  ? -7.246  5.786   2.463  1.00 20.61  ? 86  TYR A CZ  1 
ATOM   683  O OH  . TYR A 1 86  ? -8.325  6.112   3.246  1.00 19.88  ? 86  TYR A OH  1 
ATOM   684  N N   . PRO A 1 87  ? -2.164  7.755   -1.347 1.00 17.33  ? 87  PRO A N   1 
ATOM   685  C CA  . PRO A 1 87  ? -1.080  8.679   -1.004 1.00 17.82  ? 87  PRO A CA  1 
ATOM   686  C C   . PRO A 1 87  ? -1.439  9.591   0.151  1.00 13.53  ? 87  PRO A C   1 
ATOM   687  O O   . PRO A 1 87  ? -2.601  9.751   0.521  1.00 17.23  ? 87  PRO A O   1 
ATOM   688  C CB  . PRO A 1 87  ? -0.871  9.483   -2.296 1.00 11.91  ? 87  PRO A CB  1 
ATOM   689  C CG  . PRO A 1 87  ? -2.154  9.386   -2.983 1.00 16.55  ? 87  PRO A CG  1 
ATOM   690  C CD  . PRO A 1 87  ? -2.655  8.004   -2.711 1.00 16.21  ? 87  PRO A CD  1 
ATOM   691  N N   . TYR A 1 88  ? -0.392  10.203  0.708  1.00 15.61  ? 88  TYR A N   1 
ATOM   692  C CA  . TYR A 1 88  ? -0.501  11.019  1.904  1.00 14.64  ? 88  TYR A CA  1 
ATOM   693  C C   . TYR A 1 88  ? -1.013  12.392  1.519  1.00 17.93  ? 88  TYR A C   1 
ATOM   694  O O   . TYR A 1 88  ? -0.478  13.034  0.610  1.00 20.33  ? 88  TYR A O   1 
ATOM   695  C CB  . TYR A 1 88  ? 0.849   11.137  2.610  1.00 17.53  ? 88  TYR A CB  1 
ATOM   696  C CG  . TYR A 1 88  ? 0.757   11.877  3.927  1.00 21.09  ? 88  TYR A CG  1 
ATOM   697  C CD1 . TYR A 1 88  ? -0.008  11.376  4.974  1.00 17.51  ? 88  TYR A CD1 1 
ATOM   698  C CD2 . TYR A 1 88  ? 1.410   13.087  4.114  1.00 15.72  ? 88  TYR A CD2 1 
ATOM   699  C CE1 . TYR A 1 88  ? -0.102  12.047  6.177  1.00 14.89  ? 88  TYR A CE1 1 
ATOM   700  C CE2 . TYR A 1 88  ? 1.321   13.763  5.317  1.00 18.01  ? 88  TYR A CE2 1 
ATOM   701  C CZ  . TYR A 1 88  ? 0.568   13.235  6.346  1.00 18.87  ? 88  TYR A CZ  1 
ATOM   702  O OH  . TYR A 1 88  ? 0.475   13.909  7.543  1.00 17.55  ? 88  TYR A OH  1 
ATOM   703  N N   . GLU A 1 89  ? -2.046  12.841  2.222  1.00 18.14  ? 89  GLU A N   1 
ATOM   704  C CA  . GLU A 1 89  ? -2.715  14.096  1.923  1.00 20.14  ? 89  GLU A CA  1 
ATOM   705  C C   . GLU A 1 89  ? -2.575  15.134  3.022  1.00 21.69  ? 89  GLU A C   1 
ATOM   706  O O   . GLU A 1 89  ? -2.896  16.305  2.789  1.00 24.24  ? 89  GLU A O   1 
ATOM   707  C CB  . GLU A 1 89  ? -4.201  13.794  1.737  1.00 20.50  ? 89  GLU A CB  1 
ATOM   708  C CG  . GLU A 1 89  ? -4.425  12.692  0.730  1.00 25.86  ? 89  GLU A CG  1 
ATOM   709  C CD  . GLU A 1 89  ? -5.878  12.440  0.468  1.00 25.22  ? 89  GLU A CD  1 
ATOM   710  O OE1 . GLU A 1 89  ? -6.587  13.376  0.048  1.00 32.59  ? 89  GLU A OE1 1 
ATOM   711  O OE2 . GLU A 1 89  ? -6.313  11.294  0.723  1.00 32.21  ? 89  GLU A OE2 1 
ATOM   712  N N   . GLY A 1 90  ? -2.095  14.742  4.199  1.00 19.03  ? 90  GLY A N   1 
ATOM   713  C CA  . GLY A 1 90  ? -1.831  15.662  5.284  1.00 17.30  ? 90  GLY A CA  1 
ATOM   714  C C   . GLY A 1 90  ? -3.087  16.140  5.969  1.00 15.12  ? 90  GLY A C   1 
ATOM   715  O O   . GLY A 1 90  ? -3.051  17.132  6.703  1.00 18.39  ? 90  GLY A O   1 
ATOM   716  N N   . VAL A 1 91  ? -4.201  15.466  5.734  1.00 16.88  ? 91  VAL A N   1 
ATOM   717  C CA  . VAL A 1 91  ? -5.471  15.790  6.356  1.00 21.05  ? 91  VAL A CA  1 
ATOM   718  C C   . VAL A 1 91  ? -6.288  14.511  6.424  1.00 20.09  ? 91  VAL A C   1 
ATOM   719  O O   . VAL A 1 91  ? -6.196  13.659  5.535  1.00 21.01  ? 91  VAL A O   1 
ATOM   720  C CB  . VAL A 1 91  ? -6.209  16.895  5.566  1.00 20.80  ? 91  VAL A CB  1 
ATOM   721  C CG1 . VAL A 1 91  ? -6.436  16.449  4.116  1.00 10.63  ? 91  VAL A CG1 1 
ATOM   722  C CG2 . VAL A 1 91  ? -7.523  17.265  6.251  1.00 22.20  ? 91  VAL A CG2 1 
ATOM   723  N N   . GLN A 1 92  ? -7.055  14.347  7.492  1.00 16.35  ? 92  GLN A N   1 
ATOM   724  C CA  . GLN A 1 92  ? -7.897  13.170  7.585  1.00 16.80  ? 92  GLN A CA  1 
ATOM   725  C C   . GLN A 1 92  ? -9.094  13.320  6.659  1.00 19.97  ? 92  GLN A C   1 
ATOM   726  O O   . GLN A 1 92  ? -9.733  14.375  6.603  1.00 20.03  ? 92  GLN A O   1 
ATOM   727  C CB  . GLN A 1 92  ? -8.399  12.954  9.011  1.00 17.51  ? 92  GLN A CB  1 
ATOM   728  C CG  . GLN A 1 92  ? -9.152  11.640  9.149  1.00 16.23  ? 92  GLN A CG  1 
ATOM   729  C CD  . GLN A 1 92  ? -9.741  11.421  10.522 1.00 15.72  ? 92  GLN A CD  1 
ATOM   730  O OE1 . GLN A 1 92  ? -10.385 12.307  11.089 1.00 13.78  ? 92  GLN A OE1 1 
ATOM   731  N NE2 . GLN A 1 92  ? -9.588  10.206  11.036 1.00 16.22  ? 92  GLN A NE2 1 
ATOM   732  N N   . ARG A 1 93  ? -9.393  12.250  5.938  1.00 15.97  ? 93  ARG A N   1 
ATOM   733  C CA  . ARG A 1 93  ? -10.523 12.165  5.026  1.00 21.88  ? 93  ARG A CA  1 
ATOM   734  C C   . ARG A 1 93  ? -11.294 10.889  5.354  1.00 23.41  ? 93  ARG A C   1 
ATOM   735  O O   . ARG A 1 93  ? -10.956 10.165  6.297  1.00 23.77  ? 93  ARG A O   1 
ATOM   736  C CB  . ARG A 1 93  ? -10.051 12.203  3.571  1.00 28.61  ? 93  ARG A CB  1 
ATOM   737  C CG  . ARG A 1 93  ? -9.364  13.508  3.198  1.00 15.23  ? 93  ARG A CG  1 
ATOM   738  C CD  . ARG A 1 93  ? -8.988  13.492  1.750  1.00 15.75  ? 93  ARG A CD  1 
ATOM   739  N NE  . ARG A 1 93  ? -10.149 13.389  0.875  1.00 21.74  ? 93  ARG A NE  1 
ATOM   740  C CZ  . ARG A 1 93  ? -10.081 13.358  -0.448 1.00 21.13  ? 93  ARG A CZ  1 
ATOM   741  N NH1 . ARG A 1 93  ? -8.919  13.414  -1.084 1.00 21.80  ? 93  ARG A NH1 1 
ATOM   742  N NH2 . ARG A 1 93  ? -11.205 13.295  -1.153 1.00 16.03  ? 93  ARG A NH2 1 
ATOM   743  N N   . TYR A 1 94  ? -12.334 10.600  4.579  1.00 24.57  ? 94  TYR A N   1 
ATOM   744  C CA  . TYR A 1 94  ? -13.060 9.354   4.789  1.00 35.60  ? 94  TYR A CA  1 
ATOM   745  C C   . TYR A 1 94  ? -12.159 8.150   4.534  1.00 23.13  ? 94  TYR A C   1 
ATOM   746  O O   . TYR A 1 94  ? -11.238 8.195   3.716  1.00 25.34  ? 94  TYR A O   1 
ATOM   747  C CB  . TYR A 1 94  ? -14.280 9.269   3.870  1.00 44.19  ? 94  TYR A CB  1 
ATOM   748  C CG  . TYR A 1 94  ? -15.250 10.418  3.991  1.00 65.31  ? 94  TYR A CG  1 
ATOM   749  C CD1 . TYR A 1 94  ? -15.831 10.975  2.863  1.00 78.12  ? 94  TYR A CD1 1 
ATOM   750  C CD2 . TYR A 1 94  ? -15.603 10.932  5.234  1.00 89.68  ? 94  TYR A CD2 1 
ATOM   751  C CE1 . TYR A 1 94  ? -16.729 12.019  2.963  1.00 80.91  ? 94  TYR A CE1 1 
ATOM   752  C CE2 . TYR A 1 94  ? -16.501 11.977  5.345  1.00 92.69  ? 94  TYR A CE2 1 
ATOM   753  C CZ  . TYR A 1 94  ? -17.061 12.516  4.206  1.00 79.69  ? 94  TYR A CZ  1 
ATOM   754  O OH  . TYR A 1 94  ? -17.955 13.556  4.314  1.00 66.67  ? 94  TYR A OH  1 
ATOM   755  N N   . CYS A 1 95  ? -12.436 7.064   5.252  1.00 20.30  ? 95  CYS A N   1 
ATOM   756  C CA  . CYS A 1 95  ? -11.731 5.812   5.019  1.00 20.42  ? 95  CYS A CA  1 
ATOM   757  C C   . CYS A 1 95  ? -12.088 5.257   3.647  1.00 20.50  ? 95  CYS A C   1 
ATOM   758  O O   . CYS A 1 95  ? -13.257 4.985   3.358  1.00 20.05  ? 95  CYS A O   1 
ATOM   759  C CB  . CYS A 1 95  ? -12.069 4.799   6.113  1.00 11.27  ? 95  CYS A CB  1 
ATOM   760  S SG  . CYS A 1 95  ? -11.201 3.204   5.952  1.00 21.50  ? 95  CYS A SG  1 
ATOM   761  N N   . ARG A 1 96  ? -11.071 5.109   2.802  1.00 20.07  ? 96  ARG A N   1 
ATOM   762  C CA  . ARG A 1 96  ? -11.237 4.691   1.417  1.00 16.70  ? 96  ARG A CA  1 
ATOM   763  C C   . ARG A 1 96  ? -10.572 3.351   1.140  1.00 17.45  ? 96  ARG A C   1 
ATOM   764  O O   . ARG A 1 96  ? -10.286 3.036   -0.019 1.00 22.99  ? 96  ARG A O   1 
ATOM   765  C CB  . ARG A 1 96  ? -10.713 5.784   0.484  1.00 19.79  ? 96  ARG A CB  1 
ATOM   766  C CG  . ARG A 1 96  ? -11.545 7.067   0.562  1.00 17.62  ? 96  ARG A CG  1 
ATOM   767  C CD  . ARG A 1 96  ? -10.799 8.265   0.046  1.00 23.53  ? 96  ARG A CD  1 
ATOM   768  N NE  . ARG A 1 96  ? -9.906  8.791   1.074  1.00 25.46  ? 96  ARG A NE  1 
ATOM   769  C CZ  . ARG A 1 96  ? -8.899  9.621   0.840  1.00 19.36  ? 96  ARG A CZ  1 
ATOM   770  N NH1 . ARG A 1 96  ? -8.593  10.006  -0.388 1.00 13.15  ? 96  ARG A NH1 1 
ATOM   771  N NH2 . ARG A 1 96  ? -8.177  10.071  1.862  1.00 19.40  ? 96  ARG A NH2 1 
ATOM   772  N N   . SER A 1 97  ? -10.306 2.561   2.183  1.00 16.07  ? 97  SER A N   1 
ATOM   773  C CA  . SER A 1 97  ? -9.756  1.223   1.981  1.00 21.57  ? 97  SER A CA  1 
ATOM   774  C C   . SER A 1 97  ? -10.656 0.384   1.078  1.00 24.64  ? 97  SER A C   1 
ATOM   775  O O   . SER A 1 97  ? -10.170 -0.371  0.230  1.00 27.57  ? 97  SER A O   1 
ATOM   776  C CB  . SER A 1 97  ? -9.581  0.522   3.327  1.00 24.46  ? 97  SER A CB  1 
ATOM   777  O OG  . SER A 1 97  ? -8.982  1.375   4.278  1.00 23.53  ? 97  SER A OG  1 
ATOM   778  N N   . ARG A 1 98  ? -11.973 0.499   1.249  1.00 27.32  ? 98  ARG A N   1 
ATOM   779  C CA  . ARG A 1 98  ? -12.884 -0.342  0.483  1.00 29.16  ? 98  ARG A CA  1 
ATOM   780  C C   . ARG A 1 98  ? -12.893 0.038   -0.990 1.00 27.89  ? 98  ARG A C   1 
ATOM   781  O O   . ARG A 1 98  ? -13.093 -0.826  -1.850 1.00 32.95  ? 98  ARG A O   1 
ATOM   782  C CB  . ARG A 1 98  ? -14.287 -0.245  1.073  1.00 45.10  ? 98  ARG A CB  1 
ATOM   783  C CG  . ARG A 1 98  ? -15.292 -1.267  0.551  1.00 74.20  ? 98  ARG A CG  1 
ATOM   784  C CD  . ARG A 1 98  ? -16.342 -1.613  1.618  1.00 74.59  ? 98  ARG A CD  1 
ATOM   785  N NE  . ARG A 1 98  ? -15.762 -2.277  2.782  1.00 89.64  ? 98  ARG A NE  1 
ATOM   786  C CZ  . ARG A 1 98  ? -15.341 -1.662  3.882  1.00 100.37 ? 98  ARG A CZ  1 
ATOM   787  N NH1 . ARG A 1 98  ? -15.427 -0.349  4.019  1.00 105.30 ? 98  ARG A NH1 1 
ATOM   788  N NH2 . ARG A 1 98  ? -14.818 -2.385  4.869  1.00 91.71  ? 98  ARG A NH2 1 
ATOM   789  N N   . GLU A 1 99  ? -12.661 1.309   -1.304 1.00 28.44  ? 99  GLU A N   1 
ATOM   790  C CA  . GLU A 1 99  ? -12.709 1.774   -2.684 1.00 26.37  ? 99  GLU A CA  1 
ATOM   791  C C   . GLU A 1 99  ? -11.383 1.632   -3.410 1.00 28.18  ? 99  GLU A C   1 
ATOM   792  O O   . GLU A 1 99  ? -11.301 2.002   -4.586 1.00 33.40  ? 99  GLU A O   1 
ATOM   793  C CB  . GLU A 1 99  ? -13.087 3.267   -2.743 1.00 27.32  ? 99  GLU A CB  1 
ATOM   794  C CG  . GLU A 1 99  ? -14.085 3.778   -1.715 1.00 34.21  ? 99  GLU A CG  1 
ATOM   795  C CD  . GLU A 1 99  ? -15.196 2.791   -1.446 1.00 54.83  ? 99  GLU A CD  1 
ATOM   796  O OE1 . GLU A 1 99  ? -15.352 2.381   -0.269 1.00 49.25  ? 99  GLU A OE1 1 
ATOM   797  O OE2 . GLU A 1 99  ? -15.903 2.422   -2.416 1.00 48.49  ? 99  GLU A OE2 1 
ATOM   798  N N   . LYS A 1 100 ? -10.338 1.138   -2.746 1.00 24.91  ? 100 LYS A N   1 
ATOM   799  C CA  . LYS A 1 100 ? -9.022  1.042   -3.365 1.00 21.06  ? 100 LYS A CA  1 
ATOM   800  C C   . LYS A 1 100 ? -8.563  -0.381  -3.662 1.00 22.75  ? 100 LYS A C   1 
ATOM   801  O O   . LYS A 1 100 ? -7.360  -0.619  -3.801 1.00 23.95  ? 100 LYS A O   1 
ATOM   802  C CB  . LYS A 1 100 ? -8.016  1.799   -2.506 1.00 19.89  ? 100 LYS A CB  1 
ATOM   803  C CG  . LYS A 1 100 ? -8.258  3.311   -2.611 1.00 17.58  ? 100 LYS A CG  1 
ATOM   804  C CD  . LYS A 1 100 ? -7.381  4.098   -1.686 1.00 17.06  ? 100 LYS A CD  1 
ATOM   805  C CE  . LYS A 1 100 ? -7.640  5.593   -1.789 1.00 18.24  ? 100 LYS A CE  1 
ATOM   806  N NZ  . LYS A 1 100 ? -6.989  6.199   -2.983 1.00 16.80  ? 100 LYS A NZ  1 
ATOM   807  N N   . GLY A 1 101 ? -9.476  -1.338  -3.747 1.00 30.79  ? 101 GLY A N   1 
ATOM   808  C CA  . GLY A 1 101 ? -9.081  -2.661  -4.162 1.00 29.92  ? 101 GLY A CA  1 
ATOM   809  C C   . GLY A 1 101 ? -8.478  -3.462  -3.031 1.00 28.88  ? 101 GLY A C   1 
ATOM   810  O O   . GLY A 1 101 ? -8.483  -3.049  -1.868 1.00 24.23  ? 101 GLY A O   1 
ATOM   811  N N   . PRO A 1 102 ? -7.949  -4.637  -3.357 1.00 37.65  ? 102 PRO A N   1 
ATOM   812  C CA  . PRO A 1 102 ? -7.394  -5.509  -2.315 1.00 30.19  ? 102 PRO A CA  1 
ATOM   813  C C   . PRO A 1 102 ? -6.213  -4.859  -1.609 1.00 32.51  ? 102 PRO A C   1 
ATOM   814  O O   . PRO A 1 102 ? -5.488  -4.041  -2.180 1.00 33.94  ? 102 PRO A O   1 
ATOM   815  C CB  . PRO A 1 102 ? -6.958  -6.759  -3.091 1.00 35.33  ? 102 PRO A CB  1 
ATOM   816  C CG  . PRO A 1 102 ? -6.951  -6.350  -4.546 1.00 44.00  ? 102 PRO A CG  1 
ATOM   817  C CD  . PRO A 1 102 ? -7.978  -5.283  -4.680 1.00 35.90  ? 102 PRO A CD  1 
ATOM   818  N N   . TYR A 1 103 ? -6.043  -5.216  -0.339 1.00 24.00  ? 103 TYR A N   1 
ATOM   819  C CA  . TYR A 1 103 ? -4.895  -4.748  0.423  1.00 26.68  ? 103 TYR A CA  1 
ATOM   820  C C   . TYR A 1 103 ? -3.595  -5.212  -0.226 1.00 24.60  ? 103 TYR A C   1 
ATOM   821  O O   . TYR A 1 103 ? -3.541  -6.239  -0.906 1.00 29.63  ? 103 TYR A O   1 
ATOM   822  C CB  . TYR A 1 103 ? -4.974  -5.244  1.866  1.00 27.61  ? 103 TYR A CB  1 
ATOM   823  C CG  . TYR A 1 103 ? -6.066  -4.561  2.645  1.00 32.24  ? 103 TYR A CG  1 
ATOM   824  C CD1 . TYR A 1 103 ? -5.965  -3.211  2.974  1.00 31.25  ? 103 TYR A CD1 1 
ATOM   825  C CD2 . TYR A 1 103 ? -7.210  -5.253  3.035  1.00 41.21  ? 103 TYR A CD2 1 
ATOM   826  C CE1 . TYR A 1 103 ? -6.968  -2.569  3.682  1.00 31.27  ? 103 TYR A CE1 1 
ATOM   827  C CE2 . TYR A 1 103 ? -8.223  -4.618  3.741  1.00 44.89  ? 103 TYR A CE2 1 
ATOM   828  C CZ  . TYR A 1 103 ? -8.097  -3.277  4.060  1.00 34.76  ? 103 TYR A CZ  1 
ATOM   829  O OH  . TYR A 1 103 ? -9.100  -2.646  4.762  1.00 35.78  ? 103 TYR A OH  1 
ATOM   830  N N   . ALA A 1 104 ? -2.534  -4.449  0.004  1.00 20.33  ? 104 ALA A N   1 
ATOM   831  C CA  . ALA A 1 104 ? -1.229  -4.803  -0.533 1.00 24.63  ? 104 ALA A CA  1 
ATOM   832  C C   . ALA A 1 104 ? -0.460  -5.721  0.404  1.00 25.96  ? 104 ALA A C   1 
ATOM   833  O O   . ALA A 1 104 ? 0.285   -6.594  -0.057 1.00 18.47  ? 104 ALA A O   1 
ATOM   834  C CB  . ALA A 1 104 ? -0.424  -3.534  -0.811 1.00 19.26  ? 104 ALA A CB  1 
ATOM   835  N N   . ALA A 1 105 ? -0.637  -5.539  1.708  1.00 24.61  ? 105 ALA A N   1 
ATOM   836  C CA  . ALA A 1 105 ? 0.060   -6.329  2.701  1.00 20.60  ? 105 ALA A CA  1 
ATOM   837  C C   . ALA A 1 105 ? -0.846  -6.475  3.909  1.00 21.27  ? 105 ALA A C   1 
ATOM   838  O O   . ALA A 1 105 ? -1.761  -5.678  4.124  1.00 26.27  ? 105 ALA A O   1 
ATOM   839  C CB  . ALA A 1 105 ? 1.395   -5.692  3.097  1.00 19.34  ? 105 ALA A CB  1 
ATOM   840  N N   . LYS A 1 106 ? -0.586  -7.515  4.690  1.00 24.25  ? 106 LYS A N   1 
ATOM   841  C CA  . LYS A 1 106 ? -1.322  -7.769  5.916  1.00 27.12  ? 106 LYS A CA  1 
ATOM   842  C C   . LYS A 1 106 ? -0.355  -8.418  6.890  1.00 27.09  ? 106 LYS A C   1 
ATOM   843  O O   . LYS A 1 106 ? 0.491   -9.223  6.490  1.00 28.13  ? 106 LYS A O   1 
ATOM   844  C CB  . LYS A 1 106 ? -2.541  -8.689  5.729  1.00 26.90  ? 106 LYS A CB  1 
ATOM   845  C CG  . LYS A 1 106 ? -3.324  -8.834  7.036  1.00 31.50  ? 106 LYS A CG  1 
ATOM   846  C CD  . LYS A 1 106 ? -4.516  -9.783  7.011  1.00 36.59  ? 106 LYS A CD  1 
ATOM   847  C CE  . LYS A 1 106 ? -4.344  -10.819 8.145  1.00 35.89  ? 106 LYS A CE  1 
ATOM   848  N NZ  . LYS A 1 106 ? -5.613  -11.290 8.783  1.00 28.14  ? 106 LYS A NZ  1 
ATOM   849  N N   . THR A 1 107 ? -0.480  -8.071  8.159  1.00 27.33  ? 107 THR A N   1 
ATOM   850  C CA  . THR A 1 107 ? 0.350   -8.665  9.189  1.00 24.22  ? 107 THR A CA  1 
ATOM   851  C C   . THR A 1 107 ? -0.510  -9.624  10.004 1.00 30.69  ? 107 THR A C   1 
ATOM   852  O O   . THR A 1 107 ? -1.709  -9.789  9.758  1.00 33.34  ? 107 THR A O   1 
ATOM   853  C CB  . THR A 1 107 ? 0.971   -7.587  10.079 1.00 24.24  ? 107 THR A CB  1 
ATOM   854  O OG1 . THR A 1 107 ? -0.061  -6.751  10.607 1.00 19.66  ? 107 THR A OG1 1 
ATOM   855  C CG2 . THR A 1 107 ? 1.945   -6.721  9.276  1.00 28.27  ? 107 THR A CG2 1 
ATOM   856  N N   . ASP A 1 108 ? 0.106   -10.244 11.003 1.00 33.21  ? 108 ASP A N   1 
ATOM   857  C CA  . ASP A 1 108 ? -0.550  -11.276 11.786 1.00 23.89  ? 108 ASP A CA  1 
ATOM   858  C C   . ASP A 1 108 ? -0.763  -10.853 13.223 1.00 24.57  ? 108 ASP A C   1 
ATOM   859  O O   . ASP A 1 108 ? -1.410  -11.585 13.978 1.00 34.43  ? 108 ASP A O   1 
ATOM   860  C CB  . ASP A 1 108 ? 0.241   -12.590 11.741 1.00 31.87  ? 108 ASP A CB  1 
ATOM   861  C CG  . ASP A 1 108 ? 0.339   -13.157 10.332 1.00 41.26  ? 108 ASP A CG  1 
ATOM   862  O OD1 . ASP A 1 108 ? -0.717  -13.390 9.705  1.00 34.55  ? 108 ASP A OD1 1 
ATOM   863  O OD2 . ASP A 1 108 ? 1.472   -13.367 9.851  1.00 40.26  ? 108 ASP A OD2 1 
ATOM   864  N N   . GLY A 1 109 ? -0.257  -9.694  13.619 1.00 26.29  ? 109 GLY A N   1 
ATOM   865  C CA  . GLY A 1 109 ? -0.517  -9.236  14.965 1.00 21.64  ? 109 GLY A CA  1 
ATOM   866  C C   . GLY A 1 109 ? 0.365   -8.065  15.337 1.00 22.07  ? 109 GLY A C   1 
ATOM   867  O O   . GLY A 1 109 ? 1.076   -7.499  14.505 1.00 21.29  ? 109 GLY A O   1 
ATOM   868  N N   . VAL A 1 110 ? 0.335   -7.750  16.625 1.00 21.31  ? 110 VAL A N   1 
ATOM   869  C CA  . VAL A 1 110 ? 1.054   -6.617  17.191 1.00 20.84  ? 110 VAL A CA  1 
ATOM   870  C C   . VAL A 1 110 ? 1.561   -7.047  18.552 1.00 16.02  ? 110 VAL A C   1 
ATOM   871  O O   . VAL A 1 110 ? 0.798   -7.595  19.352 1.00 20.88  ? 110 VAL A O   1 
ATOM   872  C CB  . VAL A 1 110 ? 0.137   -5.385  17.355 1.00 17.90  ? 110 VAL A CB  1 
ATOM   873  C CG1 . VAL A 1 110 ? 0.936   -4.166  17.806 1.00 21.27  ? 110 VAL A CG1 1 
ATOM   874  C CG2 . VAL A 1 110 ? -0.663  -5.117  16.100 1.00 29.36  ? 110 VAL A CG2 1 
ATOM   875  N N   . ARG A 1 111 ? 2.831   -6.806  18.828 1.00 20.70  ? 111 ARG A N   1 
ATOM   876  C CA  . ARG A 1 111 ? 3.363   -7.141  20.140 1.00 26.56  ? 111 ARG A CA  1 
ATOM   877  C C   . ARG A 1 111 ? 4.095   -5.943  20.719 1.00 22.75  ? 111 ARG A C   1 
ATOM   878  O O   . ARG A 1 111 ? 4.815   -5.229  20.009 1.00 23.30  ? 111 ARG A O   1 
ATOM   879  C CB  . ARG A 1 111 ? 4.265   -8.378  20.070 1.00 24.26  ? 111 ARG A CB  1 
ATOM   880  C CG  . ARG A 1 111 ? 3.454   -9.657  19.961 1.00 31.27  ? 111 ARG A CG  1 
ATOM   881  C CD  . ARG A 1 111 ? 4.171   -10.865 20.527 1.00 49.41  ? 111 ARG A CD  1 
ATOM   882  N NE  . ARG A 1 111 ? 4.425   -11.867 19.497 1.00 68.42  ? 111 ARG A NE  1 
ATOM   883  C CZ  . ARG A 1 111 ? 5.626   -12.331 19.177 1.00 70.81  ? 111 ARG A CZ  1 
ATOM   884  N NH1 . ARG A 1 111 ? 6.716   -11.923 19.808 1.00 76.54  ? 111 ARG A NH1 1 
ATOM   885  N NH2 . ARG A 1 111 ? 5.735   -13.233 18.204 1.00 58.49  ? 111 ARG A NH2 1 
ATOM   886  N N   . GLN A 1 112 ? 3.875   -5.716  22.007 1.00 18.17  ? 112 GLN A N   1 
ATOM   887  C CA  . GLN A 1 112 ? 4.460   -4.592  22.719 1.00 23.10  ? 112 GLN A CA  1 
ATOM   888  C C   . GLN A 1 112 ? 5.797   -5.008  23.331 1.00 23.36  ? 112 GLN A C   1 
ATOM   889  O O   . GLN A 1 112 ? 5.915   -6.088  23.918 1.00 24.72  ? 112 GLN A O   1 
ATOM   890  C CB  . GLN A 1 112 ? 3.508   -4.078  23.803 1.00 21.66  ? 112 GLN A CB  1 
ATOM   891  C CG  . GLN A 1 112 ? 4.003   -2.803  24.469 1.00 23.18  ? 112 GLN A CG  1 
ATOM   892  C CD  . GLN A 1 112 ? 3.029   -2.242  25.476 1.00 25.67  ? 112 GLN A CD  1 
ATOM   893  O OE1 . GLN A 1 112 ? 1.940   -2.779  25.670 1.00 31.45  ? 112 GLN A OE1 1 
ATOM   894  N NE2 . GLN A 1 112 ? 3.420   -1.153  26.130 1.00 20.18  ? 112 GLN A NE2 1 
ATOM   895  N N   . VAL A 1 113 ? 6.794   -4.129  23.212 1.00 17.07  ? 113 VAL A N   1 
ATOM   896  C CA  . VAL A 1 113 ? 8.040   -4.294  23.951 1.00 17.06  ? 113 VAL A CA  1 
ATOM   897  C C   . VAL A 1 113 ? 7.793   -4.026  25.428 1.00 19.77  ? 113 VAL A C   1 
ATOM   898  O O   . VAL A 1 113 ? 6.995   -3.149  25.784 1.00 20.81  ? 113 VAL A O   1 
ATOM   899  C CB  . VAL A 1 113 ? 9.101   -3.321  23.404 1.00 15.08  ? 113 VAL A CB  1 
ATOM   900  C CG1 . VAL A 1 113 ? 10.436  -3.526  24.099 1.00 14.57  ? 113 VAL A CG1 1 
ATOM   901  C CG2 . VAL A 1 113 ? 9.227   -3.441  21.893 1.00 14.50  ? 113 VAL A CG2 1 
ATOM   902  N N   . GLN A 1 114 ? 8.441   -4.811  26.298 1.00 21.84  ? 114 GLN A N   1 
ATOM   903  C CA  . GLN A 1 114 ? 8.441   -4.511  27.723 1.00 28.18  ? 114 GLN A CA  1 
ATOM   904  C C   . GLN A 1 114 ? 8.850   -3.056  27.920 1.00 20.23  ? 114 GLN A C   1 
ATOM   905  O O   . GLN A 1 114 ? 9.990   -2.695  27.598 1.00 24.52  ? 114 GLN A O   1 
ATOM   906  C CB  . GLN A 1 114 ? 9.401   -5.419  28.490 1.00 36.85  ? 114 GLN A CB  1 
ATOM   907  C CG  . GLN A 1 114 ? 8.961   -5.777  29.907 1.00 43.32  ? 114 GLN A CG  1 
ATOM   908  C CD  . GLN A 1 114 ? 8.013   -6.969  29.944 1.00 85.47  ? 114 GLN A CD  1 
ATOM   909  O OE1 . GLN A 1 114 ? 8.448   -8.123  29.948 1.00 76.82  ? 114 GLN A OE1 1 
ATOM   910  N NE2 . GLN A 1 114 ? 6.712   -6.694  29.977 1.00 72.26  ? 114 GLN A NE2 1 
ATOM   911  N N   . PRO A 1 115 ? 7.960   -2.192  28.399 1.00 23.57  ? 115 PRO A N   1 
ATOM   912  C CA  . PRO A 1 115 ? 8.314   -0.774  28.486 1.00 22.07  ? 115 PRO A CA  1 
ATOM   913  C C   . PRO A 1 115 ? 9.389   -0.554  29.540 1.00 23.83  ? 115 PRO A C   1 
ATOM   914  O O   . PRO A 1 115 ? 9.597   -1.371  30.441 1.00 26.36  ? 115 PRO A O   1 
ATOM   915  C CB  . PRO A 1 115 ? 6.990   -0.095  28.866 1.00 19.37  ? 115 PRO A CB  1 
ATOM   916  C CG  . PRO A 1 115 ? 6.171   -1.181  29.491 1.00 20.21  ? 115 PRO A CG  1 
ATOM   917  C CD  . PRO A 1 115 ? 6.579   -2.461  28.845 1.00 18.27  ? 115 PRO A CD  1 
ATOM   918  N N   . TYR A 1 116 ? 10.078  0.578   29.412 1.00 25.09  ? 116 TYR A N   1 
ATOM   919  C CA  . TYR A 1 116 ? 11.051  1.027   30.411 1.00 28.66  ? 116 TYR A CA  1 
ATOM   920  C C   . TYR A 1 116 ? 12.182  0.012   30.581 1.00 27.13  ? 116 TYR A C   1 
ATOM   921  O O   . TYR A 1 116 ? 12.687  -0.206  31.686 1.00 33.62  ? 116 TYR A O   1 
ATOM   922  C CB  . TYR A 1 116 ? 10.370  1.319   31.749 1.00 17.21  ? 116 TYR A CB  1 
ATOM   923  C CG  . TYR A 1 116 ? 9.172   2.224   31.629 1.00 25.15  ? 116 TYR A CG  1 
ATOM   924  C CD1 . TYR A 1 116 ? 9.306   3.529   31.159 1.00 22.30  ? 116 TYR A CD1 1 
ATOM   925  C CD2 . TYR A 1 116 ? 7.898   1.783   31.985 1.00 36.20  ? 116 TYR A CD2 1 
ATOM   926  C CE1 . TYR A 1 116 ? 8.204   4.370   31.045 1.00 23.09  ? 116 TYR A CE1 1 
ATOM   927  C CE2 . TYR A 1 116 ? 6.788   2.623   31.875 1.00 36.78  ? 116 TYR A CE2 1 
ATOM   928  C CZ  . TYR A 1 116 ? 6.952   3.914   31.404 1.00 20.05  ? 116 TYR A CZ  1 
ATOM   929  O OH  . TYR A 1 116 ? 5.868   4.754   31.291 1.00 32.37  ? 116 TYR A OH  1 
ATOM   930  N N   . ASN A 1 117 ? 12.626  -0.572  29.465 1.00 19.61  ? 117 ASN A N   1 
ATOM   931  C CA  . ASN A 1 117 ? 13.606  -1.661  29.507 1.00 21.86  ? 117 ASN A CA  1 
ATOM   932  C C   . ASN A 1 117 ? 14.485  -1.549  28.263 1.00 20.91  ? 117 ASN A C   1 
ATOM   933  O O   . ASN A 1 117 ? 14.043  -1.906  27.167 1.00 19.41  ? 117 ASN A O   1 
ATOM   934  C CB  . ASN A 1 117 ? 12.906  -3.008  29.589 1.00 16.82  ? 117 ASN A CB  1 
ATOM   935  C CG  . ASN A 1 117 ? 13.879  -4.165  29.769 1.00 15.50  ? 117 ASN A CG  1 
ATOM   936  O OD1 . ASN A 1 117 ? 14.995  -4.152  29.251 1.00 17.42  ? 117 ASN A OD1 1 
ATOM   937  N ND2 . ASN A 1 117 ? 13.448  -5.183  30.497 1.00 17.80  ? 117 ASN A ND2 1 
ATOM   938  N N   . GLU A 1 118 ? 15.711  -1.039  28.431 1.00 21.88  ? 118 GLU A N   1 
ATOM   939  C CA  . GLU A 1 118 ? 16.575  -0.782  27.276 1.00 23.36  ? 118 GLU A CA  1 
ATOM   940  C C   . GLU A 1 118 ? 16.918  -2.064  26.510 1.00 22.12  ? 118 GLU A C   1 
ATOM   941  O O   . GLU A 1 118 ? 16.855  -2.095  25.274 1.00 17.94  ? 118 GLU A O   1 
ATOM   942  C CB  . GLU A 1 118 ? 17.852  -0.088  27.729 1.00 25.97  ? 118 GLU A CB  1 
ATOM   943  C CG  . GLU A 1 118 ? 18.848  0.148   26.602 1.00 28.82  ? 118 GLU A CG  1 
ATOM   944  C CD  . GLU A 1 118 ? 19.989  1.045   27.033 1.00 29.88  ? 118 GLU A CD  1 
ATOM   945  O OE1 . GLU A 1 118 ? 21.133  0.525   27.044 1.00 44.74  ? 118 GLU A OE1 1 
ATOM   946  O OE2 . GLU A 1 118 ? 19.769  2.236   27.318 1.00 33.96  ? 118 GLU A OE2 1 
ATOM   947  N N   . GLY A 1 119 ? 17.327  -3.118  27.215 1.00 25.03  ? 119 GLY A N   1 
ATOM   948  C CA  . GLY A 1 119 ? 17.708  -4.339  26.521 1.00 20.76  ? 119 GLY A CA  1 
ATOM   949  C C   . GLY A 1 119 ? 16.562  -4.961  25.742 1.00 17.82  ? 119 GLY A C   1 
ATOM   950  O O   . GLY A 1 119 ? 16.765  -5.505  24.656 1.00 18.47  ? 119 GLY A O   1 
ATOM   951  N N   . ALA A 1 120 ? 15.336  -4.879  26.276 1.00 20.56  ? 120 ALA A N   1 
ATOM   952  C CA  . ALA A 1 120 ? 14.186  -5.430  25.558 1.00 17.14  ? 120 ALA A CA  1 
ATOM   953  C C   . ALA A 1 120 ? 13.957  -4.687  24.249 1.00 20.32  ? 120 ALA A C   1 
ATOM   954  O O   . ALA A 1 120 ? 13.689  -5.302  23.206 1.00 20.46  ? 120 ALA A O   1 
ATOM   955  C CB  . ALA A 1 120 ? 12.939  -5.363  26.439 1.00 16.69  ? 120 ALA A CB  1 
ATOM   956  N N   . LEU A 1 121 ? 14.117  -3.361  24.275 1.00 15.22  ? 121 LEU A N   1 
ATOM   957  C CA  . LEU A 1 121 ? 13.947  -2.584  23.060 1.00 14.17  ? 121 LEU A CA  1 
ATOM   958  C C   . LEU A 1 121 ? 15.081  -2.874  22.082 1.00 19.29  ? 121 LEU A C   1 
ATOM   959  O O   . LEU A 1 121 ? 14.848  -2.980  20.873 1.00 21.27  ? 121 LEU A O   1 
ATOM   960  C CB  . LEU A 1 121 ? 13.860  -1.086  23.378 1.00 16.54  ? 121 LEU A CB  1 
ATOM   961  C CG  . LEU A 1 121 ? 13.767  -0.198  22.124 1.00 18.30  ? 121 LEU A CG  1 
ATOM   962  C CD1 . LEU A 1 121 ? 12.511  -0.585  21.343 1.00 17.15  ? 121 LEU A CD1 1 
ATOM   963  C CD2 . LEU A 1 121 ? 13.794  1.298   22.422 1.00 12.25  ? 121 LEU A CD2 1 
ATOM   964  N N   . LEU A 1 122 ? 16.325  -2.966  22.575 1.00 21.11  ? 122 LEU A N   1 
ATOM   965  C CA  . LEU A 1 122 ? 17.431  -3.315  21.682 1.00 21.78  ? 122 LEU A CA  1 
ATOM   966  C C   . LEU A 1 122 ? 17.202  -4.675  21.040 1.00 16.69  ? 122 LEU A C   1 
ATOM   967  O O   . LEU A 1 122 ? 17.490  -4.860  19.853 1.00 20.00  ? 122 LEU A O   1 
ATOM   968  C CB  . LEU A 1 122 ? 18.776  -3.280  22.415 1.00 20.35  ? 122 LEU A CB  1 
ATOM   969  C CG  . LEU A 1 122 ? 19.161  -1.927  23.003 1.00 20.86  ? 122 LEU A CG  1 
ATOM   970  C CD1 . LEU A 1 122 ? 20.474  -2.033  23.764 1.00 20.54  ? 122 LEU A CD1 1 
ATOM   971  C CD2 . LEU A 1 122 ? 19.210  -0.856  21.926 1.00 16.77  ? 122 LEU A CD2 1 
ATOM   972  N N   . TYR A 1 123 ? 16.713  -5.648  21.810 1.00 15.68  ? 123 TYR A N   1 
ATOM   973  C CA  . TYR A 1 123 ? 16.424  -6.961  21.247 1.00 15.91  ? 123 TYR A CA  1 
ATOM   974  C C   . TYR A 1 123 ? 15.403  -6.841  20.124 1.00 16.57  ? 123 TYR A C   1 
ATOM   975  O O   . TYR A 1 123 ? 15.618  -7.327  18.998 1.00 19.42  ? 123 TYR A O   1 
ATOM   976  C CB  . TYR A 1 123 ? 15.914  -7.887  22.347 1.00 18.21  ? 123 TYR A CB  1 
ATOM   977  C CG  . TYR A 1 123 ? 15.597  -9.278  21.876 1.00 20.64  ? 123 TYR A CG  1 
ATOM   978  C CD1 . TYR A 1 123 ? 16.584  -10.240 21.733 1.00 21.92  ? 123 TYR A CD1 1 
ATOM   979  C CD2 . TYR A 1 123 ? 14.288  -9.625  21.557 1.00 20.68  ? 123 TYR A CD2 1 
ATOM   980  C CE1 . TYR A 1 123 ? 16.268  -11.518 21.291 1.00 29.52  ? 123 TYR A CE1 1 
ATOM   981  C CE2 . TYR A 1 123 ? 13.964  -10.890 21.113 1.00 24.61  ? 123 TYR A CE2 1 
ATOM   982  C CZ  . TYR A 1 123 ? 14.950  -11.833 20.982 1.00 31.63  ? 123 TYR A CZ  1 
ATOM   983  O OH  . TYR A 1 123 ? 14.610  -13.093 20.537 1.00 39.48  ? 123 TYR A OH  1 
ATOM   984  N N   . SER A 1 124 ? 14.281  -6.175  20.417 1.00 16.76  ? 124 SER A N   1 
ATOM   985  C CA  . SER A 1 124 ? 13.267  -5.936  19.397 1.00 20.12  ? 124 SER A CA  1 
ATOM   986  C C   . SER A 1 124 ? 13.887  -5.327  18.147 1.00 17.42  ? 124 SER A C   1 
ATOM   987  O O   . SER A 1 124 ? 13.715  -5.849  17.040 1.00 16.93  ? 124 SER A O   1 
ATOM   988  C CB  . SER A 1 124 ? 12.162  -5.036  19.949 1.00 14.08  ? 124 SER A CB  1 
ATOM   989  O OG  . SER A 1 124 ? 11.197  -5.795  20.653 1.00 21.91  ? 124 SER A OG  1 
ATOM   990  N N   . ILE A 1 125 ? 14.643  -4.235  18.309 1.00 18.11  ? 125 ILE A N   1 
ATOM   991  C CA  . ILE A 1 125 ? 15.247  -3.584  17.150 1.00 19.89  ? 125 ILE A CA  1 
ATOM   992  C C   . ILE A 1 125 ? 16.172  -4.532  16.406 1.00 14.12  ? 125 ILE A C   1 
ATOM   993  O O   . ILE A 1 125 ? 16.250  -4.495  15.173 1.00 19.58  ? 125 ILE A O   1 
ATOM   994  C CB  . ILE A 1 125 ? 16.010  -2.314  17.585 1.00 21.77  ? 125 ILE A CB  1 
ATOM   995  C CG1 . ILE A 1 125 ? 15.077  -1.288  18.236 1.00 18.32  ? 125 ILE A CG1 1 
ATOM   996  C CG2 . ILE A 1 125 ? 16.830  -1.735  16.434 1.00 15.60  ? 125 ILE A CG2 1 
ATOM   997  C CD1 . ILE A 1 125 ? 15.830  -0.175  18.956 1.00 17.33  ? 125 ILE A CD1 1 
ATOM   998  N N   . ALA A 1 126 ? 16.866  -5.408  17.125 1.00 12.83  ? 126 ALA A N   1 
ATOM   999  C CA  . ALA A 1 126 ? 17.696  -6.393  16.454 1.00 13.27  ? 126 ALA A CA  1 
ATOM   1000 C C   . ALA A 1 126 ? 16.861  -7.299  15.563 1.00 12.83  ? 126 ALA A C   1 
ATOM   1001 O O   . ALA A 1 126 ? 17.360  -7.802  14.552 1.00 15.86  ? 126 ALA A O   1 
ATOM   1002 C CB  . ALA A 1 126 ? 18.503  -7.198  17.472 1.00 16.79  ? 126 ALA A CB  1 
ATOM   1003 N N   . ASN A 1 127 ? 15.600  -7.532  15.910 1.00 15.33  ? 127 ASN A N   1 
ATOM   1004 C CA  . ASN A 1 127 ? 14.797  -8.351  15.003 1.00 19.37  ? 127 ASN A CA  1 
ATOM   1005 C C   . ASN A 1 127 ? 14.074  -7.558  13.917 1.00 16.64  ? 127 ASN A C   1 
ATOM   1006 O O   . ASN A 1 127 ? 13.786  -8.134  12.862 1.00 17.57  ? 127 ASN A O   1 
ATOM   1007 C CB  . ASN A 1 127 ? 13.777  -9.194  15.771 1.00 13.36  ? 127 ASN A CB  1 
ATOM   1008 C CG  . ASN A 1 127 ? 14.335  -9.723  17.079 1.00 31.71  ? 127 ASN A CG  1 
ATOM   1009 O OD1 . ASN A 1 127 ? 15.334  -10.447 17.098 1.00 23.40  ? 127 ASN A OD1 1 
ATOM   1010 N ND2 . ASN A 1 127 ? 13.702  -9.344  18.187 1.00 33.00  ? 127 ASN A ND2 1 
ATOM   1011 N N   . GLN A 1 128 ? 13.822  -6.249  14.112 1.00 13.72  ? 128 GLN A N   1 
ATOM   1012 C CA  . GLN A 1 128 ? 13.016  -5.459  13.179 1.00 10.80  ? 128 GLN A CA  1 
ATOM   1013 C C   . GLN A 1 128 ? 12.901  -3.999  13.606 1.00 14.13  ? 128 GLN A C   1 
ATOM   1014 O O   . GLN A 1 128 ? 13.172  -3.672  14.767 1.00 20.03  ? 128 GLN A O   1 
ATOM   1015 C CB  . GLN A 1 128 ? 11.625  -6.064  13.066 1.00 15.25  ? 128 GLN A CB  1 
ATOM   1016 C CG  . GLN A 1 128 ? 10.830  -5.919  14.334 1.00 14.35  ? 128 GLN A CG  1 
ATOM   1017 C CD  . GLN A 1 128 ? 9.668   -6.855  14.353 1.00 14.31  ? 128 GLN A CD  1 
ATOM   1018 O OE1 . GLN A 1 128 ? 8.710   -6.699  13.593 1.00 16.41  ? 128 GLN A OE1 1 
ATOM   1019 N NE2 . GLN A 1 128 ? 9.757   -7.872  15.196 1.00 13.95  ? 128 GLN A NE2 1 
ATOM   1020 N N   . PRO A 1 129 ? 12.543  -3.086  12.704 1.00 14.66  ? 129 PRO A N   1 
ATOM   1021 C CA  . PRO A 1 129 ? 12.230  -1.720  13.139 1.00 12.43  ? 129 PRO A CA  1 
ATOM   1022 C C   . PRO A 1 129 ? 11.044  -1.717  14.100 1.00 20.70  ? 129 PRO A C   1 
ATOM   1023 O O   . PRO A 1 129 ? 10.093  -2.488  13.948 1.00 16.49  ? 129 PRO A O   1 
ATOM   1024 C CB  . PRO A 1 129 ? 11.871  -1.013  11.830 1.00 18.21  ? 129 PRO A CB  1 
ATOM   1025 C CG  . PRO A 1 129 ? 12.606  -1.768  10.787 1.00 17.04  ? 129 PRO A CG  1 
ATOM   1026 C CD  . PRO A 1 129 ? 12.552  -3.200  11.233 1.00 10.32  ? 129 PRO A CD  1 
ATOM   1027 N N   . VAL A 1 130 ? 11.083  -0.821  15.080 1.00 16.99  ? 130 VAL A N   1 
ATOM   1028 C CA  . VAL A 1 130 ? 10.106  -0.821  16.163 1.00 13.32  ? 130 VAL A CA  1 
ATOM   1029 C C   . VAL A 1 130 ? 9.497   0.566   16.242 1.00 12.03  ? 130 VAL A C   1 
ATOM   1030 O O   . VAL A 1 130 ? 10.202  1.568   16.121 1.00 15.02  ? 130 VAL A O   1 
ATOM   1031 C CB  . VAL A 1 130 ? 10.732  -1.246  17.507 1.00 12.08  ? 130 VAL A CB  1 
ATOM   1032 C CG1 . VAL A 1 130 ? 9.720   -1.143  18.637 1.00 14.41  ? 130 VAL A CG1 1 
ATOM   1033 C CG2 . VAL A 1 130 ? 11.207  -2.684  17.397 1.00 14.19  ? 130 VAL A CG2 1 
ATOM   1034 N N   . SER A 1 131 ? 8.198   0.635   16.493 1.00 13.42  ? 131 SER A N   1 
ATOM   1035 C CA  . SER A 1 131 ? 7.566   1.926   16.722 1.00 14.71  ? 131 SER A CA  1 
ATOM   1036 C C   . SER A 1 131 ? 7.816   2.348   18.161 1.00 12.53  ? 131 SER A C   1 
ATOM   1037 O O   . SER A 1 131 ? 7.540   1.586   19.090 1.00 16.28  ? 131 SER A O   1 
ATOM   1038 C CB  . SER A 1 131 ? 6.070   1.849   16.418 1.00 12.71  ? 131 SER A CB  1 
ATOM   1039 O OG  . SER A 1 131 ? 5.393   2.995   16.907 1.00 11.62  ? 131 SER A OG  1 
ATOM   1040 N N   . VAL A 1 132 ? 8.349   3.558   18.350 1.00 10.04  ? 132 VAL A N   1 
ATOM   1041 C CA  . VAL A 1 132 ? 8.664   4.062   19.682 1.00 13.38  ? 132 VAL A CA  1 
ATOM   1042 C C   . VAL A 1 132 ? 8.122   5.475   19.800 1.00 12.30  ? 132 VAL A C   1 
ATOM   1043 O O   . VAL A 1 132 ? 7.765   6.116   18.812 1.00 13.55  ? 132 VAL A O   1 
ATOM   1044 C CB  . VAL A 1 132 ? 10.178  4.045   19.999 1.00 10.93  ? 132 VAL A CB  1 
ATOM   1045 C CG1 . VAL A 1 132 ? 10.707  2.628   19.935 1.00 14.54  ? 132 VAL A CG1 1 
ATOM   1046 C CG2 . VAL A 1 132 ? 10.949  4.947   19.037 1.00 8.77   ? 132 VAL A CG2 1 
ATOM   1047 N N   . VAL A 1 133 ? 8.039   5.951   21.032 1.00 12.50  ? 133 VAL A N   1 
ATOM   1048 C CA  . VAL A 1 133 ? 7.576   7.307   21.270 1.00 17.15  ? 133 VAL A CA  1 
ATOM   1049 C C   . VAL A 1 133 ? 8.630   8.068   22.057 1.00 15.66  ? 133 VAL A C   1 
ATOM   1050 O O   . VAL A 1 133 ? 9.501   7.493   22.713 1.00 17.79  ? 133 VAL A O   1 
ATOM   1051 C CB  . VAL A 1 133 ? 6.222   7.329   22.024 1.00 22.08  ? 133 VAL A CB  1 
ATOM   1052 C CG1 . VAL A 1 133 ? 5.145   6.657   21.199 1.00 21.05  ? 133 VAL A CG1 1 
ATOM   1053 C CG2 . VAL A 1 133 ? 6.344   6.651   23.405 1.00 20.23  ? 133 VAL A CG2 1 
ATOM   1054 N N   . LEU A 1 134 ? 8.552   9.387   21.967 1.00 15.69  ? 134 LEU A N   1 
ATOM   1055 C CA  . LEU A 1 134 ? 9.499   10.225  22.681 1.00 19.60  ? 134 LEU A CA  1 
ATOM   1056 C C   . LEU A 1 134 ? 8.893   11.609  22.843 1.00 20.03  ? 134 LEU A C   1 
ATOM   1057 O O   . LEU A 1 134 ? 7.858   11.936  22.248 1.00 21.04  ? 134 LEU A O   1 
ATOM   1058 C CB  . LEU A 1 134 ? 10.850  10.245  21.947 1.00 16.08  ? 134 LEU A CB  1 
ATOM   1059 C CG  . LEU A 1 134 ? 10.913  10.559  20.439 1.00 17.61  ? 134 LEU A CG  1 
ATOM   1060 C CD1 . LEU A 1 134 ? 10.646  12.013  20.051 1.00 19.24  ? 134 LEU A CD1 1 
ATOM   1061 C CD2 . LEU A 1 134 ? 12.219  10.056  19.836 1.00 9.89   ? 134 LEU A CD2 1 
ATOM   1062 N N   . GLU A 1 135 ? 9.534   12.405  23.696 1.00 16.07  ? 135 GLU A N   1 
ATOM   1063 C CA  . GLU A 1 135 ? 9.191   13.808  23.871 1.00 18.87  ? 135 GLU A CA  1 
ATOM   1064 C C   . GLU A 1 135 ? 9.975   14.616  22.849 1.00 25.38  ? 135 GLU A C   1 
ATOM   1065 O O   . GLU A 1 135 ? 11.207  14.689  22.920 1.00 22.13  ? 135 GLU A O   1 
ATOM   1066 C CB  . GLU A 1 135 ? 9.455   14.290  25.293 1.00 23.38  ? 135 GLU A CB  1 
ATOM   1067 C CG  . GLU A 1 135 ? 9.017   15.745  25.553 1.00 28.84  ? 135 GLU A CG  1 
ATOM   1068 C CD  . GLU A 1 135 ? 9.596   16.312  26.841 1.00 36.86  ? 135 GLU A CD  1 
ATOM   1069 O OE1 . GLU A 1 135 ? 9.010   16.010  27.911 1.00 59.05  ? 135 GLU A OE1 1 
ATOM   1070 O OE2 . GLU A 1 135 ? 10.585  17.073  26.791 1.00 40.35  ? 135 GLU A OE2 1 
ATOM   1071 N N   . ALA A 1 136 ? 9.268   15.169  21.871 1.00 15.12  ? 136 ALA A N   1 
ATOM   1072 C CA  . ALA A 1 136 ? 9.872   15.979  20.835 1.00 14.71  ? 136 ALA A CA  1 
ATOM   1073 C C   . ALA A 1 136 ? 9.569   17.468  20.980 1.00 19.46  ? 136 ALA A C   1 
ATOM   1074 O O   . ALA A 1 136 ? 9.999   18.254  20.132 1.00 24.96  ? 136 ALA A O   1 
ATOM   1075 C CB  . ALA A 1 136 ? 9.403   15.486  19.465 1.00 17.63  ? 136 ALA A CB  1 
ATOM   1076 N N   . ALA A 1 137 ? 8.822   17.878  22.011 1.00 26.71  ? 137 ALA A N   1 
ATOM   1077 C CA  . ALA A 1 137 ? 8.379   19.269  22.112 1.00 18.70  ? 137 ALA A CA  1 
ATOM   1078 C C   . ALA A 1 137 ? 9.520   20.212  22.478 1.00 24.55  ? 137 ALA A C   1 
ATOM   1079 O O   . ALA A 1 137 ? 9.463   21.403  22.154 1.00 29.13  ? 137 ALA A O   1 
ATOM   1080 C CB  . ALA A 1 137 ? 7.254   19.392  23.140 1.00 19.69  ? 137 ALA A CB  1 
ATOM   1081 N N   . GLY A 1 138 ? 10.558  19.703  23.140 1.00 22.33  ? 138 GLY A N   1 
ATOM   1082 C CA  . GLY A 1 138 ? 11.651  20.557  23.573 1.00 19.31  ? 138 GLY A CA  1 
ATOM   1083 C C   . GLY A 1 138 ? 12.453  21.131  22.414 1.00 25.99  ? 138 GLY A C   1 
ATOM   1084 O O   . GLY A 1 138 ? 12.665  20.480  21.392 1.00 25.60  ? 138 GLY A O   1 
ATOM   1085 N N   . LYS A 1 139 ? 12.936  22.364  22.603 1.00 30.10  ? 139 LYS A N   1 
ATOM   1086 C CA  . LYS A 1 139 ? 13.620  23.086  21.534 1.00 24.13  ? 139 LYS A CA  1 
ATOM   1087 C C   . LYS A 1 139 ? 14.907  22.383  21.120 1.00 23.39  ? 139 LYS A C   1 
ATOM   1088 O O   . LYS A 1 139 ? 15.279  22.400  19.943 1.00 27.40  ? 139 LYS A O   1 
ATOM   1089 C CB  . LYS A 1 139 ? 13.910  24.519  21.988 1.00 32.44  ? 139 LYS A CB  1 
ATOM   1090 C CG  . LYS A 1 139 ? 13.580  25.593  20.958 1.00 47.47  ? 139 LYS A CG  1 
ATOM   1091 C CD  . LYS A 1 139 ? 12.207  25.401  20.313 1.00 70.97  ? 139 LYS A CD  1 
ATOM   1092 C CE  . LYS A 1 139 ? 11.064  25.747  21.262 1.00 91.47  ? 139 LYS A CE  1 
ATOM   1093 N NZ  . LYS A 1 139 ? 9.728   25.490  20.645 1.00 99.71  ? 139 LYS A NZ  1 
ATOM   1094 N N   . ASP A 1 140 ? 15.587  21.743  22.067 1.00 21.89  ? 140 ASP A N   1 
ATOM   1095 C CA  . ASP A 1 140 ? 16.806  21.017  21.737 1.00 19.95  ? 140 ASP A CA  1 
ATOM   1096 C C   . ASP A 1 140 ? 16.532  19.895  20.739 1.00 22.53  ? 140 ASP A C   1 
ATOM   1097 O O   . ASP A 1 140 ? 17.333  19.647  19.827 1.00 19.10  ? 140 ASP A O   1 
ATOM   1098 C CB  . ASP A 1 140 ? 17.436  20.482  23.014 1.00 18.49  ? 140 ASP A CB  1 
ATOM   1099 C CG  . ASP A 1 140 ? 17.945  21.603  23.880 1.00 29.41  ? 140 ASP A CG  1 
ATOM   1100 O OD1 . ASP A 1 140 ? 19.079  22.054  23.590 1.00 31.71  ? 140 ASP A OD1 1 
ATOM   1101 O OD2 . ASP A 1 140 ? 17.192  22.026  24.807 1.00 23.30  ? 140 ASP A OD2 1 
ATOM   1102 N N   . PHE A 1 141 ? 15.433  19.171  20.933 1.00 27.69  ? 141 PHE A N   1 
ATOM   1103 C CA  . PHE A 1 141 ? 15.035  18.145  19.975 1.00 23.57  ? 141 PHE A CA  1 
ATOM   1104 C C   . PHE A 1 141 ? 14.585  18.776  18.665 1.00 18.89  ? 141 PHE A C   1 
ATOM   1105 O O   . PHE A 1 141 ? 14.916  18.276  17.586 1.00 20.67  ? 141 PHE A O   1 
ATOM   1106 C CB  . PHE A 1 141 ? 13.919  17.255  20.533 1.00 16.48  ? 141 PHE A CB  1 
ATOM   1107 C CG  . PHE A 1 141 ? 13.584  16.074  19.651 1.00 18.08  ? 141 PHE A CG  1 
ATOM   1108 C CD1 . PHE A 1 141 ? 12.710  16.195  18.579 1.00 17.54  ? 141 PHE A CD1 1 
ATOM   1109 C CD2 . PHE A 1 141 ? 14.131  14.825  19.920 1.00 16.59  ? 141 PHE A CD2 1 
ATOM   1110 C CE1 . PHE A 1 141 ? 12.411  15.081  17.779 1.00 22.04  ? 141 PHE A CE1 1 
ATOM   1111 C CE2 . PHE A 1 141 ? 13.829  13.709  19.136 1.00 18.26  ? 141 PHE A CE2 1 
ATOM   1112 C CZ  . PHE A 1 141 ? 12.971  13.835  18.065 1.00 13.28  ? 141 PHE A CZ  1 
ATOM   1113 N N   . GLN A 1 142 ? 13.820  19.876  18.741 1.00 20.94  ? 142 GLN A N   1 
ATOM   1114 C CA  . GLN A 1 142 ? 13.305  20.512  17.529 1.00 26.25  ? 142 GLN A CA  1 
ATOM   1115 C C   . GLN A 1 142 ? 14.452  20.928  16.607 1.00 26.63  ? 142 GLN A C   1 
ATOM   1116 O O   . GLN A 1 142 ? 14.380  20.748  15.385 1.00 22.56  ? 142 GLN A O   1 
ATOM   1117 C CB  . GLN A 1 142 ? 12.541  21.780  17.946 1.00 29.51  ? 142 GLN A CB  1 
ATOM   1118 C CG  . GLN A 1 142 ? 11.334  21.604  18.893 1.00 37.84  ? 142 GLN A CG  1 
ATOM   1119 C CD  . GLN A 1 142 ? 9.975   21.566  18.236 1.00 40.23  ? 142 GLN A CD  1 
ATOM   1120 O OE1 . GLN A 1 142 ? 9.543   20.528  17.735 1.00 23.74  ? 142 GLN A OE1 1 
ATOM   1121 N NE2 . GLN A 1 142 ? 9.259   22.691  18.299 1.00 49.17  ? 142 GLN A NE2 1 
ATOM   1122 N N   . LEU A 1 143 ? 15.545  21.423  17.193 1.00 21.99  ? 143 LEU A N   1 
ATOM   1123 C CA  . LEU A 1 143 ? 16.703  21.982  16.500 1.00 23.49  ? 143 LEU A CA  1 
ATOM   1124 C C   . LEU A 1 143 ? 17.850  20.986  16.302 1.00 25.38  ? 143 LEU A C   1 
ATOM   1125 O O   . LEU A 1 143 ? 18.939  21.401  15.890 1.00 30.17  ? 143 LEU A O   1 
ATOM   1126 C CB  . LEU A 1 143 ? 17.184  23.294  17.145 1.00 31.21  ? 143 LEU A CB  1 
ATOM   1127 C CG  . LEU A 1 143 ? 16.315  24.573  17.031 1.00 31.82  ? 143 LEU A CG  1 
ATOM   1128 C CD1 . LEU A 1 143 ? 15.089  24.643  17.905 1.00 31.70  ? 143 LEU A CD1 1 
ATOM   1129 C CD2 . LEU A 1 143 ? 17.193  25.798  17.285 1.00 45.19  ? 143 LEU A CD2 1 
ATOM   1130 N N   . TYR A 1 144 ? 17.660  19.706  16.644 1.00 20.63  ? 144 TYR A N   1 
ATOM   1131 C CA  . TYR A 1 144 ? 18.746  18.737  16.544 1.00 17.84  ? 144 TYR A CA  1 
ATOM   1132 C C   . TYR A 1 144 ? 19.300  18.776  15.129 1.00 19.54  ? 144 TYR A C   1 
ATOM   1133 O O   . TYR A 1 144 ? 18.546  18.753  14.153 1.00 20.28  ? 144 TYR A O   1 
ATOM   1134 C CB  . TYR A 1 144 ? 18.209  17.349  16.869 1.00 22.04  ? 144 TYR A CB  1 
ATOM   1135 C CG  . TYR A 1 144 ? 19.137  16.225  16.509 1.00 25.24  ? 144 TYR A CG  1 
ATOM   1136 C CD1 . TYR A 1 144 ? 20.177  15.854  17.350 1.00 19.02  ? 144 TYR A CD1 1 
ATOM   1137 C CD2 . TYR A 1 144 ? 18.992  15.553  15.304 1.00 16.94  ? 144 TYR A CD2 1 
ATOM   1138 C CE1 . TYR A 1 144 ? 21.016  14.819  17.010 1.00 17.26  ? 144 TYR A CE1 1 
ATOM   1139 C CE2 . TYR A 1 144 ? 19.829  14.535  14.955 1.00 12.23  ? 144 TYR A CE2 1 
ATOM   1140 C CZ  . TYR A 1 144 ? 20.836  14.163  15.811 1.00 15.18  ? 144 TYR A CZ  1 
ATOM   1141 O OH  . TYR A 1 144 ? 21.667  13.122  15.476 1.00 15.39  ? 144 TYR A OH  1 
ATOM   1142 N N   . ARG A 1 145 ? 20.628  18.851  15.019 1.00 22.09  ? 145 ARG A N   1 
ATOM   1143 C CA  . ARG A 1 145 ? 21.278  18.866  13.717 1.00 21.21  ? 145 ARG A CA  1 
ATOM   1144 C C   . ARG A 1 145 ? 22.102  17.636  13.429 1.00 18.73  ? 145 ARG A C   1 
ATOM   1145 O O   . ARG A 1 145 ? 22.251  17.261  12.268 1.00 19.80  ? 145 ARG A O   1 
ATOM   1146 C CB  . ARG A 1 145 ? 22.267  20.022  13.735 1.00 25.81  ? 145 ARG A CB  1 
ATOM   1147 C CG  . ARG A 1 145 ? 21.570  21.294  14.067 1.00 37.65  ? 145 ARG A CG  1 
ATOM   1148 C CD  . ARG A 1 145 ? 22.539  22.416  14.267 1.00 55.16  ? 145 ARG A CD  1 
ATOM   1149 N NE  . ARG A 1 145 ? 21.843  23.502  14.944 1.00 60.42  ? 145 ARG A NE  1 
ATOM   1150 C CZ  . ARG A 1 145 ? 22.430  24.576  15.449 1.00 69.54  ? 145 ARG A CZ  1 
ATOM   1151 N NH1 . ARG A 1 145 ? 23.737  24.745  15.371 1.00 51.34  ? 145 ARG A NH1 1 
ATOM   1152 N NH2 . ARG A 1 145 ? 21.689  25.475  16.094 1.00 66.60  ? 145 ARG A NH2 1 
ATOM   1153 N N   . GLY A 1 146 ? 22.613  16.987  14.454 1.00 17.23  ? 146 GLY A N   1 
ATOM   1154 C CA  . GLY A 1 146 ? 23.439  15.816  14.256 1.00 18.96  ? 146 GLY A CA  1 
ATOM   1155 C C   . GLY A 1 146 ? 24.209  15.490  15.514 1.00 22.80  ? 146 GLY A C   1 
ATOM   1156 O O   . GLY A 1 146 ? 24.275  16.279  16.461 1.00 19.72  ? 146 GLY A O   1 
ATOM   1157 N N   . GLY A 1 147 ? 24.825  14.308  15.498 1.00 22.95  ? 147 GLY A N   1 
ATOM   1158 C CA  . GLY A 1 147 ? 25.547  13.809  16.651 1.00 14.09  ? 147 GLY A CA  1 
ATOM   1159 C C   . GLY A 1 147 ? 24.649  12.907  17.476 1.00 19.29  ? 147 GLY A C   1 
ATOM   1160 O O   . GLY A 1 147 ? 23.481  12.646  17.149 1.00 18.71  ? 147 GLY A O   1 
ATOM   1161 N N   . ILE A 1 148 ? 25.222  12.389  18.557 1.00 18.26  ? 148 ILE A N   1 
ATOM   1162 C CA  . ILE A 1 148 ? 24.439  11.564  19.477 1.00 15.01  ? 148 ILE A CA  1 
ATOM   1163 C C   . ILE A 1 148 ? 23.714  12.487  20.462 1.00 15.79  ? 148 ILE A C   1 
ATOM   1164 O O   . ILE A 1 148 ? 24.353  13.209  21.234 1.00 19.76  ? 148 ILE A O   1 
ATOM   1165 C CB  . ILE A 1 148 ? 25.304  10.514  20.175 1.00 14.85  ? 148 ILE A CB  1 
ATOM   1166 C CG1 . ILE A 1 148 ? 25.801  9.513   19.110 1.00 13.49  ? 148 ILE A CG1 1 
ATOM   1167 C CG2 . ILE A 1 148 ? 24.451  9.818   21.255 1.00 20.08  ? 148 ILE A CG2 1 
ATOM   1168 C CD1 . ILE A 1 148 ? 26.853  8.579   19.642 1.00 26.06  ? 148 ILE A CD1 1 
ATOM   1169 N N   . PHE A 1 149 ? 22.396  12.553  20.352 1.00 13.60  ? 149 PHE A N   1 
ATOM   1170 C CA  . PHE A 1 149 ? 21.570  13.478  21.118 1.00 17.80  ? 149 PHE A CA  1 
ATOM   1171 C C   . PHE A 1 149 ? 21.386  12.982  22.534 1.00 15.77  ? 149 PHE A C   1 
ATOM   1172 O O   . PHE A 1 149 ? 20.958  11.844  22.742 1.00 19.88  ? 149 PHE A O   1 
ATOM   1173 C CB  . PHE A 1 149 ? 20.215  13.617  20.434 1.00 12.40  ? 149 PHE A CB  1 
ATOM   1174 C CG  . PHE A 1 149 ? 19.328  14.636  21.043 1.00 17.10  ? 149 PHE A CG  1 
ATOM   1175 C CD1 . PHE A 1 149 ? 19.611  15.988  20.910 1.00 18.21  ? 149 PHE A CD1 1 
ATOM   1176 C CD2 . PHE A 1 149 ? 18.174  14.257  21.720 1.00 19.12  ? 149 PHE A CD2 1 
ATOM   1177 C CE1 . PHE A 1 149 ? 18.779  16.949  21.480 1.00 14.20  ? 149 PHE A CE1 1 
ATOM   1178 C CE2 . PHE A 1 149 ? 17.333  15.223  22.279 1.00 15.86  ? 149 PHE A CE2 1 
ATOM   1179 C CZ  . PHE A 1 149 ? 17.646  16.570  22.150 1.00 12.87  ? 149 PHE A CZ  1 
ATOM   1180 N N   . VAL A 1 150 ? 21.700  13.845  23.498 1.00 16.70  ? 150 VAL A N   1 
ATOM   1181 C CA  . VAL A 1 150 ? 21.573  13.531  24.913 1.00 20.78  ? 150 VAL A CA  1 
ATOM   1182 C C   . VAL A 1 150 ? 20.491  14.353  25.588 1.00 23.42  ? 150 VAL A C   1 
ATOM   1183 O O   . VAL A 1 150 ? 20.303  14.223  26.807 1.00 19.02  ? 150 VAL A O   1 
ATOM   1184 C CB  . VAL A 1 150 ? 22.919  13.686  25.658 1.00 18.64  ? 150 VAL A CB  1 
ATOM   1185 C CG1 . VAL A 1 150 ? 24.012  12.892  24.977 1.00 19.17  ? 150 VAL A CG1 1 
ATOM   1186 C CG2 . VAL A 1 150 ? 23.333  15.160  25.776 1.00 17.49  ? 150 VAL A CG2 1 
ATOM   1187 N N   . GLY A 1 151 ? 19.765  15.189  24.839 1.00 22.03  ? 151 GLY A N   1 
ATOM   1188 C CA  . GLY A 1 151 ? 18.875  16.174  25.407 1.00 15.52  ? 151 GLY A CA  1 
ATOM   1189 C C   . GLY A 1 151 ? 19.460  17.573  25.390 1.00 19.07  ? 151 GLY A C   1 
ATOM   1190 O O   . GLY A 1 151 ? 20.371  17.874  24.610 1.00 18.64  ? 151 GLY A O   1 
ATOM   1191 N N   . PRO A 1 152 ? 18.962  18.464  26.265 1.00 22.58  ? 152 PRO A N   1 
ATOM   1192 C CA  . PRO A 1 152 ? 17.954  18.258  27.317 1.00 22.39  ? 152 PRO A CA  1 
ATOM   1193 C C   . PRO A 1 152 ? 16.595  17.806  26.790 1.00 25.88  ? 152 PRO A C   1 
ATOM   1194 O O   . PRO A 1 152 ? 16.193  18.212  25.703 1.00 30.65  ? 152 PRO A O   1 
ATOM   1195 C CB  . PRO A 1 152 ? 17.831  19.651  27.949 1.00 24.51  ? 152 PRO A CB  1 
ATOM   1196 C CG  . PRO A 1 152 ? 19.152  20.292  27.715 1.00 21.88  ? 152 PRO A CG  1 
ATOM   1197 C CD  . PRO A 1 152 ? 19.548  19.815  26.341 1.00 23.63  ? 152 PRO A CD  1 
ATOM   1198 N N   . CYS A 1 153 ? 15.875  16.969  27.528 1.00 26.11  ? 153 CYS A N   1 
ATOM   1199 C CA  . CYS A 1 153 ? 14.501  16.609  27.198 1.00 26.76  ? 153 CYS A CA  1 
ATOM   1200 C C   . CYS A 1 153 ? 13.916  15.932  28.424 1.00 25.27  ? 153 CYS A C   1 
ATOM   1201 O O   . CYS A 1 153 ? 14.646  15.334  29.221 1.00 27.10  ? 153 CYS A O   1 
ATOM   1202 C CB  . CYS A 1 153 ? 14.373  15.689  25.978 1.00 22.09  ? 153 CYS A CB  1 
ATOM   1203 S SG  . CYS A 1 153 ? 15.367  14.208  25.975 1.00 38.50  ? 153 CYS A SG  1 
ATOM   1204 N N   . GLY A 1 154 ? 12.597  16.013  28.557 1.00 23.52  ? 154 GLY A N   1 
ATOM   1205 C CA  . GLY A 1 154 ? 11.887  15.276  29.574 1.00 30.25  ? 154 GLY A CA  1 
ATOM   1206 C C   . GLY A 1 154 ? 11.371  13.957  29.042 1.00 30.12  ? 154 GLY A C   1 
ATOM   1207 O O   . GLY A 1 154 ? 11.762  13.486  27.974 1.00 24.54  ? 154 GLY A O   1 
ATOM   1208 N N   . ASN A 1 155 ? 10.485  13.343  29.823 1.00 33.84  ? 155 ASN A N   1 
ATOM   1209 C CA  . ASN A 1 155 ? 9.891   12.061  29.471 1.00 28.11  ? 155 ASN A CA  1 
ATOM   1210 C C   . ASN A 1 155 ? 8.413   12.173  29.105 1.00 30.21  ? 155 ASN A C   1 
ATOM   1211 O O   . ASN A 1 155 ? 7.732   11.147  28.999 1.00 31.34  ? 155 ASN A O   1 
ATOM   1212 C CB  . ASN A 1 155 ? 10.074  11.062  30.618 1.00 30.51  ? 155 ASN A CB  1 
ATOM   1213 C CG  . ASN A 1 155 ? 11.465  11.117  31.235 1.00 47.00  ? 155 ASN A CG  1 
ATOM   1214 O OD1 . ASN A 1 155 ? 12.460  10.764  30.593 1.00 40.75  ? 155 ASN A OD1 1 
ATOM   1215 N ND2 . ASN A 1 155 ? 11.539  11.544  32.497 1.00 45.77  ? 155 ASN A ND2 1 
ATOM   1216 N N   . LYS A 1 156 ? 7.899   13.391  28.910 1.00 33.27  ? 156 LYS A N   1 
ATOM   1217 C CA  . LYS A 1 156 ? 6.496   13.609  28.542 1.00 28.96  ? 156 LYS A CA  1 
ATOM   1218 C C   . LYS A 1 156 ? 6.350   13.318  27.051 1.00 25.71  ? 156 LYS A C   1 
ATOM   1219 O O   . LYS A 1 156 ? 6.355   14.215  26.204 1.00 27.20  ? 156 LYS A O   1 
ATOM   1220 C CB  . LYS A 1 156 ? 6.064   15.036  28.869 1.00 41.80  ? 156 LYS A CB  1 
ATOM   1221 C CG  . LYS A 1 156 ? 5.967   15.388  30.359 1.00 64.30  ? 156 LYS A CG  1 
ATOM   1222 C CD  . LYS A 1 156 ? 5.865   14.159  31.260 1.00 74.75  ? 156 LYS A CD  1 
ATOM   1223 C CE  . LYS A 1 156 ? 5.972   14.538  32.728 1.00 91.96  ? 156 LYS A CE  1 
ATOM   1224 N NZ  . LYS A 1 156 ? 5.063   13.720  33.576 1.00 97.30  ? 156 LYS A NZ  1 
ATOM   1225 N N   . VAL A 1 157 ? 6.225   12.032  26.724 1.00 16.23  ? 157 VAL A N   1 
ATOM   1226 C CA  . VAL A 1 157 ? 6.266   11.621  25.327 1.00 17.24  ? 157 VAL A CA  1 
ATOM   1227 C C   . VAL A 1 157 ? 5.053   12.168  24.590 1.00 23.96  ? 157 VAL A C   1 
ATOM   1228 O O   . VAL A 1 157 ? 3.952   12.280  25.147 1.00 20.30  ? 157 VAL A O   1 
ATOM   1229 C CB  . VAL A 1 157 ? 6.356   10.090  25.187 1.00 23.72  ? 157 VAL A CB  1 
ATOM   1230 C CG1 . VAL A 1 157 ? 7.650   9.572   25.814 1.00 24.78  ? 157 VAL A CG1 1 
ATOM   1231 C CG2 . VAL A 1 157 ? 5.129   9.386   25.757 1.00 19.19  ? 157 VAL A CG2 1 
ATOM   1232 N N   . ASP A 1 158 ? 5.274   12.559  23.335 1.00 21.22  ? 158 ASP A N   1 
ATOM   1233 C CA  . ASP A 1 158 ? 4.252   13.256  22.564 1.00 18.74  ? 158 ASP A CA  1 
ATOM   1234 C C   . ASP A 1 158 ? 4.427   13.009  21.070 1.00 26.75  ? 158 ASP A C   1 
ATOM   1235 O O   . ASP A 1 158 ? 3.700   13.617  20.271 1.00 24.50  ? 158 ASP A O   1 
ATOM   1236 C CB  . ASP A 1 158 ? 4.289   14.781  22.846 1.00 14.83  ? 158 ASP A CB  1 
ATOM   1237 C CG  . ASP A 1 158 ? 5.654   15.415  22.555 1.00 21.89  ? 158 ASP A CG  1 
ATOM   1238 O OD1 . ASP A 1 158 ? 6.410   14.916  21.692 1.00 21.26  ? 158 ASP A OD1 1 
ATOM   1239 O OD2 . ASP A 1 158 ? 5.980   16.433  23.200 1.00 29.96  ? 158 ASP A OD2 1 
ATOM   1240 N N   . HIS A 1 159 ? 5.331   12.121  20.664 1.00 18.38  ? 159 HIS A N   1 
ATOM   1241 C CA  . HIS A 1 159 ? 5.724   12.022  19.266 1.00 17.42  ? 159 HIS A CA  1 
ATOM   1242 C C   . HIS A 1 159 ? 6.134   10.594  18.972 1.00 17.10  ? 159 HIS A C   1 
ATOM   1243 O O   . HIS A 1 159 ? 7.025   10.053  19.630 1.00 23.19  ? 159 HIS A O   1 
ATOM   1244 C CB  . HIS A 1 159 ? 6.877   12.971  18.934 1.00 13.70  ? 159 HIS A CB  1 
ATOM   1245 C CG  . HIS A 1 159 ? 7.203   13.022  17.475 1.00 19.57  ? 159 HIS A CG  1 
ATOM   1246 N ND1 . HIS A 1 159 ? 6.252   13.264  16.507 1.00 15.85  ? 159 HIS A ND1 1 
ATOM   1247 C CD2 . HIS A 1 159 ? 8.375   12.848  16.816 1.00 18.02  ? 159 HIS A CD2 1 
ATOM   1248 C CE1 . HIS A 1 159 ? 6.824   13.240  15.316 1.00 13.19  ? 159 HIS A CE1 1 
ATOM   1249 N NE2 . HIS A 1 159 ? 8.111   12.989  15.475 1.00 14.33  ? 159 HIS A NE2 1 
ATOM   1250 N N   . ALA A 1 160 ? 5.507   9.999   17.967 1.00 16.55  ? 160 ALA A N   1 
ATOM   1251 C CA  . ALA A 1 160 ? 5.802   8.632   17.582 1.00 14.57  ? 160 ALA A CA  1 
ATOM   1252 C C   . ALA A 1 160 ? 6.776   8.645   16.413 1.00 11.55  ? 160 ALA A C   1 
ATOM   1253 O O   . ALA A 1 160 ? 6.596   9.401   15.455 1.00 15.96  ? 160 ALA A O   1 
ATOM   1254 C CB  . ALA A 1 160 ? 4.513   7.891   17.207 1.00 12.13  ? 160 ALA A CB  1 
ATOM   1255 N N   . VAL A 1 161 ? 7.801   7.800   16.501 1.00 12.95  ? 161 VAL A N   1 
ATOM   1256 C CA  . VAL A 1 161 ? 8.879   7.709   15.525 1.00 10.99  ? 161 VAL A CA  1 
ATOM   1257 C C   . VAL A 1 161 ? 9.209   6.235   15.394 1.00 14.11  ? 161 VAL A C   1 
ATOM   1258 O O   . VAL A 1 161 ? 8.533   5.386   15.992 1.00 15.50  ? 161 VAL A O   1 
ATOM   1259 C CB  . VAL A 1 161 ? 10.122  8.495   15.979 1.00 12.68  ? 161 VAL A CB  1 
ATOM   1260 C CG1 . VAL A 1 161 ? 9.854   9.973   16.003 1.00 11.95  ? 161 VAL A CG1 1 
ATOM   1261 C CG2 . VAL A 1 161 ? 10.546  8.025   17.368 1.00 14.53  ? 161 VAL A CG2 1 
ATOM   1262 N N   . ALA A 1 162 ? 10.293  5.905   14.696 1.00 12.39  ? 162 ALA A N   1 
ATOM   1263 C CA  . ALA A 1 162 ? 10.616  4.494   14.538 1.00 13.76  ? 162 ALA A CA  1 
ATOM   1264 C C   . ALA A 1 162 ? 12.085  4.246   14.822 1.00 10.47  ? 162 ALA A C   1 
ATOM   1265 O O   . ALA A 1 162 ? 12.936  5.001   14.359 1.00 14.69  ? 162 ALA A O   1 
ATOM   1266 C CB  . ALA A 1 162 ? 10.257  4.011   13.137 1.00 13.11  ? 162 ALA A CB  1 
ATOM   1267 N N   . ALA A 1 163 ? 12.384  3.234   15.623 1.00 9.50   ? 163 ALA A N   1 
ATOM   1268 C CA  . ALA A 1 163 ? 13.762  2.840   15.878 1.00 12.75  ? 163 ALA A CA  1 
ATOM   1269 C C   . ALA A 1 163 ? 14.159  1.806   14.833 1.00 16.79  ? 163 ALA A C   1 
ATOM   1270 O O   . ALA A 1 163 ? 13.511  0.757   14.716 1.00 19.46  ? 163 ALA A O   1 
ATOM   1271 C CB  . ALA A 1 163 ? 13.911  2.276   17.288 1.00 14.46  ? 163 ALA A CB  1 
ATOM   1272 N N   . VAL A 1 164 ? 15.214  2.102   14.073 1.00 17.63  ? 164 VAL A N   1 
ATOM   1273 C CA  . VAL A 1 164 ? 15.671  1.264   12.973 1.00 20.32  ? 164 VAL A CA  1 
ATOM   1274 C C   . VAL A 1 164 ? 17.100  0.778   13.177 1.00 15.49  ? 164 VAL A C   1 
ATOM   1275 O O   . VAL A 1 164 ? 17.679  0.173   12.277 1.00 19.35  ? 164 VAL A O   1 
ATOM   1276 C CB  . VAL A 1 164 ? 15.529  1.991   11.621 1.00 23.40  ? 164 VAL A CB  1 
ATOM   1277 C CG1 . VAL A 1 164 ? 14.052  2.303   11.340 1.00 16.84  ? 164 VAL A CG1 1 
ATOM   1278 C CG2 . VAL A 1 164 ? 16.374  3.266   11.620 1.00 18.34  ? 164 VAL A CG2 1 
ATOM   1279 N N   . GLY A 1 165 ? 17.681  1.027   14.342 1.00 13.83  ? 165 GLY A N   1 
ATOM   1280 C CA  . GLY A 1 165 ? 19.012  0.524   14.613 1.00 15.24  ? 165 GLY A CA  1 
ATOM   1281 C C   . GLY A 1 165 ? 19.503  1.006   15.958 1.00 11.00  ? 165 GLY A C   1 
ATOM   1282 O O   . GLY A 1 165 ? 18.776  1.655   16.710 1.00 16.22  ? 165 GLY A O   1 
ATOM   1283 N N   . TYR A 1 166 ? 20.758  0.696   16.246 1.00 13.43  ? 166 TYR A N   1 
ATOM   1284 C CA  . TYR A 1 166 ? 21.376  1.132   17.492 1.00 14.06  ? 166 TYR A CA  1 
ATOM   1285 C C   . TYR A 1 166 ? 22.881  0.937   17.367 1.00 18.08  ? 166 TYR A C   1 
ATOM   1286 O O   . TYR A 1 166 ? 23.375  0.270   16.452 1.00 17.85  ? 166 TYR A O   1 
ATOM   1287 C CB  . TYR A 1 166 ? 20.816  0.380   18.710 1.00 11.34  ? 166 TYR A CB  1 
ATOM   1288 C CG  . TYR A 1 166 ? 21.092  -1.106  18.719 1.00 17.89  ? 166 TYR A CG  1 
ATOM   1289 C CD1 . TYR A 1 166 ? 22.341  -1.591  19.077 1.00 13.39  ? 166 TYR A CD1 1 
ATOM   1290 C CD2 . TYR A 1 166 ? 20.101  -2.031  18.365 1.00 17.45  ? 166 TYR A CD2 1 
ATOM   1291 C CE1 . TYR A 1 166 ? 22.611  -2.946  19.080 1.00 16.39  ? 166 TYR A CE1 1 
ATOM   1292 C CE2 . TYR A 1 166 ? 20.362  -3.398  18.367 1.00 15.44  ? 166 TYR A CE2 1 
ATOM   1293 C CZ  . TYR A 1 166 ? 21.633  -3.847  18.731 1.00 19.19  ? 166 TYR A CZ  1 
ATOM   1294 O OH  . TYR A 1 166 ? 21.961  -5.189  18.756 1.00 15.45  ? 166 TYR A OH  1 
ATOM   1295 N N   . GLY A 1 167 ? 23.601  1.525   18.309 1.00 19.23  ? 167 GLY A N   1 
ATOM   1296 C CA  . GLY A 1 167 ? 25.013  1.278   18.439 1.00 15.00  ? 167 GLY A CA  1 
ATOM   1297 C C   . GLY A 1 167 ? 25.356  1.222   19.905 1.00 15.01  ? 167 GLY A C   1 
ATOM   1298 O O   . GLY A 1 167 ? 24.467  1.217   20.763 1.00 18.79  ? 167 GLY A O   1 
ATOM   1299 N N   . PRO A 1 168 ? 26.646  1.122   20.227 1.00 18.50  ? 168 PRO A N   1 
ATOM   1300 C CA  . PRO A 1 168 ? 27.031  0.999   21.640 1.00 18.23  ? 168 PRO A CA  1 
ATOM   1301 C C   . PRO A 1 168 ? 26.496  2.107   22.532 1.00 10.94  ? 168 PRO A C   1 
ATOM   1302 O O   . PRO A 1 168 ? 26.229  1.856   23.712 1.00 16.89  ? 168 PRO A O   1 
ATOM   1303 C CB  . PRO A 1 168 ? 28.563  1.000   21.576 1.00 16.59  ? 168 PRO A CB  1 
ATOM   1304 C CG  . PRO A 1 168 ? 28.861  0.372   20.252 1.00 18.04  ? 168 PRO A CG  1 
ATOM   1305 C CD  . PRO A 1 168 ? 27.770  0.824   19.324 1.00 15.19  ? 168 PRO A CD  1 
ATOM   1306 N N   . ASN A 1 169 ? 26.300  3.317   22.019 1.00 16.65  ? 169 ASN A N   1 
ATOM   1307 C CA  . ASN A 1 169 ? 25.851  4.401   22.886 1.00 20.55  ? 169 ASN A CA  1 
ATOM   1308 C C   . ASN A 1 169 ? 24.669  5.176   22.307 1.00 20.99  ? 169 ASN A C   1 
ATOM   1309 O O   . ASN A 1 169 ? 24.424  6.313   22.725 1.00 22.51  ? 169 ASN A O   1 
ATOM   1310 C CB  . ASN A 1 169 ? 27.014  5.353   23.208 1.00 22.88  ? 169 ASN A CB  1 
ATOM   1311 C CG  . ASN A 1 169 ? 27.819  5.738   21.977 1.00 31.14  ? 169 ASN A CG  1 
ATOM   1312 O OD1 . ASN A 1 169 ? 27.620  5.189   20.888 1.00 25.66  ? 169 ASN A OD1 1 
ATOM   1313 N ND2 . ASN A 1 169 ? 28.745  6.678   22.148 1.00 43.41  ? 169 ASN A ND2 1 
ATOM   1314 N N   . TYR A 1 170 ? 23.913  4.589   21.381 1.00 15.39  ? 170 TYR A N   1 
ATOM   1315 C CA  . TYR A 1 170 ? 22.767  5.296   20.819 1.00 18.86  ? 170 TYR A CA  1 
ATOM   1316 C C   . TYR A 1 170 ? 21.756  4.291   20.275 1.00 17.70  ? 170 TYR A C   1 
ATOM   1317 O O   . TYR A 1 170 ? 22.042  3.105   20.099 1.00 15.82  ? 170 TYR A O   1 
ATOM   1318 C CB  . TYR A 1 170 ? 23.192  6.269   19.706 1.00 14.20  ? 170 TYR A CB  1 
ATOM   1319 C CG  . TYR A 1 170 ? 23.762  5.555   18.505 1.00 16.39  ? 170 TYR A CG  1 
ATOM   1320 C CD1 . TYR A 1 170 ? 25.118  5.254   18.431 1.00 17.65  ? 170 TYR A CD1 1 
ATOM   1321 C CD2 . TYR A 1 170 ? 22.937  5.156   17.447 1.00 18.05  ? 170 TYR A CD2 1 
ATOM   1322 C CE1 . TYR A 1 170 ? 25.643  4.578   17.328 1.00 20.65  ? 170 TYR A CE1 1 
ATOM   1323 C CE2 . TYR A 1 170 ? 23.451  4.479   16.345 1.00 17.37  ? 170 TYR A CE2 1 
ATOM   1324 C CZ  . TYR A 1 170 ? 24.804  4.197   16.292 1.00 14.26  ? 170 TYR A CZ  1 
ATOM   1325 O OH  . TYR A 1 170 ? 25.323  3.527   15.208 1.00 24.64  ? 170 TYR A OH  1 
ATOM   1326 N N   . ILE A 1 171 ? 20.559  4.800   20.029 1.00 13.26  ? 171 ILE A N   1 
ATOM   1327 C CA  . ILE A 1 171 ? 19.517  4.133   19.268 1.00 14.23  ? 171 ILE A CA  1 
ATOM   1328 C C   . ILE A 1 171 ? 19.229  5.009   18.058 1.00 12.69  ? 171 ILE A C   1 
ATOM   1329 O O   . ILE A 1 171 ? 19.163  6.239   18.174 1.00 14.75  ? 171 ILE A O   1 
ATOM   1330 C CB  . ILE A 1 171 ? 18.257  3.887   20.127 1.00 17.76  ? 171 ILE A CB  1 
ATOM   1331 C CG1 . ILE A 1 171 ? 18.554  2.806   21.174 1.00 16.09  ? 171 ILE A CG1 1 
ATOM   1332 C CG2 . ILE A 1 171 ? 17.082  3.428   19.259 1.00 17.41  ? 171 ILE A CG2 1 
ATOM   1333 C CD1 . ILE A 1 171 ? 17.486  2.669   22.260 1.00 30.26  ? 171 ILE A CD1 1 
ATOM   1334 N N   . LEU A 1 172 ? 19.096  4.385   16.897 1.00 10.06  ? 172 LEU A N   1 
ATOM   1335 C CA  . LEU A 1 172 ? 18.949  5.102   15.639 1.00 9.97   ? 172 LEU A CA  1 
ATOM   1336 C C   . LEU A 1 172 ? 17.476  5.262   15.302 1.00 12.68  ? 172 LEU A C   1 
ATOM   1337 O O   . LEU A 1 172 ? 16.747  4.268   15.227 1.00 20.84  ? 172 LEU A O   1 
ATOM   1338 C CB  . LEU A 1 172 ? 19.672  4.352   14.527 1.00 12.40  ? 172 LEU A CB  1 
ATOM   1339 C CG  . LEU A 1 172 ? 19.515  4.890   13.111 1.00 11.12  ? 172 LEU A CG  1 
ATOM   1340 C CD1 . LEU A 1 172 ? 20.129  6.252   13.003 1.00 7.14   ? 172 LEU A CD1 1 
ATOM   1341 C CD2 . LEU A 1 172 ? 20.154  3.911   12.139 1.00 15.94  ? 172 LEU A CD2 1 
ATOM   1342 N N   . ILE A 1 173 ? 17.031  6.504   15.110 1.00 11.35  ? 173 ILE A N   1 
ATOM   1343 C CA  . ILE A 1 173 ? 15.616  6.829   15.009 1.00 13.68  ? 173 ILE A CA  1 
ATOM   1344 C C   . ILE A 1 173 ? 15.339  7.476   13.658 1.00 17.75  ? 173 ILE A C   1 
ATOM   1345 O O   . ILE A 1 173 ? 16.020  8.436   13.269 1.00 16.29  ? 173 ILE A O   1 
ATOM   1346 C CB  . ILE A 1 173 ? 15.165  7.767   16.144 1.00 13.58  ? 173 ILE A CB  1 
ATOM   1347 C CG1 . ILE A 1 173 ? 15.347  7.119   17.513 1.00 15.72  ? 173 ILE A CG1 1 
ATOM   1348 C CG2 . ILE A 1 173 ? 13.720  8.185   15.931 1.00 12.77  ? 173 ILE A CG2 1 
ATOM   1349 C CD1 . ILE A 1 173 ? 14.500  5.870   17.718 1.00 21.85  ? 173 ILE A CD1 1 
ATOM   1350 N N   . LYS A 1 174 ? 14.342  6.935   12.952 1.00 15.66  ? 174 LYS A N   1 
ATOM   1351 C CA  . LYS A 1 174 ? 13.751  7.522   11.759 1.00 10.48  ? 174 LYS A CA  1 
ATOM   1352 C C   . LYS A 1 174 ? 12.592  8.413   12.194 1.00 13.22  ? 174 LYS A C   1 
ATOM   1353 O O   . LYS A 1 174 ? 11.589  7.926   12.748 1.00 13.36  ? 174 LYS A O   1 
ATOM   1354 C CB  . LYS A 1 174 ? 13.261  6.437   10.801 1.00 12.81  ? 174 LYS A CB  1 
ATOM   1355 C CG  . LYS A 1 174 ? 12.728  6.985   9.471  1.00 20.51  ? 174 LYS A CG  1 
ATOM   1356 C CD  . LYS A 1 174 ? 12.214  5.884   8.551  1.00 19.70  ? 174 LYS A CD  1 
ATOM   1357 C CE  . LYS A 1 174 ? 11.912  6.409   7.155  1.00 15.46  ? 174 LYS A CE  1 
ATOM   1358 N NZ  . LYS A 1 174 ? 11.106  5.423   6.371  1.00 20.99  ? 174 LYS A NZ  1 
ATOM   1359 N N   . ASN A 1 175 ? 12.754  9.713   11.981 1.00 13.11  ? 175 ASN A N   1 
ATOM   1360 C CA  . ASN A 1 175 ? 11.728  10.706  12.250 1.00 14.24  ? 175 ASN A CA  1 
ATOM   1361 C C   . ASN A 1 175 ? 10.914  10.967  10.982 1.00 14.93  ? 175 ASN A C   1 
ATOM   1362 O O   . ASN A 1 175 ? 11.282  10.563  9.876  1.00 13.65  ? 175 ASN A O   1 
ATOM   1363 C CB  . ASN A 1 175 ? 12.370  11.987  12.773 1.00 12.75  ? 175 ASN A CB  1 
ATOM   1364 C CG  . ASN A 1 175 ? 11.400  12.860  13.524 1.00 15.22  ? 175 ASN A CG  1 
ATOM   1365 O OD1 . ASN A 1 175 ? 10.230  12.507  13.695 1.00 10.76  ? 175 ASN A OD1 1 
ATOM   1366 N ND2 . ASN A 1 175 ? 11.890  14.002  14.017 1.00 14.34  ? 175 ASN A ND2 1 
ATOM   1367 N N   . SER A 1 176 ? 9.800   11.662  11.152 1.00 11.50  ? 176 SER A N   1 
ATOM   1368 C CA  . SER A 1 176 ? 8.884   11.976  10.068 1.00 12.55  ? 176 SER A CA  1 
ATOM   1369 C C   . SER A 1 176 ? 8.797   13.477  9.876  1.00 17.04  ? 176 SER A C   1 
ATOM   1370 O O   . SER A 1 176 ? 7.717   14.035  9.654  1.00 17.96  ? 176 SER A O   1 
ATOM   1371 C CB  . SER A 1 176 ? 7.501   11.395  10.331 1.00 14.88  ? 176 SER A CB  1 
ATOM   1372 O OG  . SER A 1 176 ? 7.058   11.753  11.628 1.00 12.60  ? 176 SER A OG  1 
ATOM   1373 N N   . TRP A 1 177 ? 9.947   14.148  9.939  1.00 14.81  ? 177 TRP A N   1 
ATOM   1374 C CA  . TRP A 1 177 ? 10.012  15.592  9.780  1.00 13.66  ? 177 TRP A CA  1 
ATOM   1375 C C   . TRP A 1 177 ? 10.762  16.009  8.522  1.00 16.13  ? 177 TRP A C   1 
ATOM   1376 O O   . TRP A 1 177 ? 11.260  17.139  8.444  1.00 10.40  ? 177 TRP A O   1 
ATOM   1377 C CB  . TRP A 1 177 ? 10.673  16.206  11.005 1.00 15.45  ? 177 TRP A CB  1 
ATOM   1378 C CG  . TRP A 1 177 ? 9.791   16.176  12.192 1.00 12.06  ? 177 TRP A CG  1 
ATOM   1379 C CD1 . TRP A 1 177 ? 8.474   15.816  12.230 1.00 9.37   ? 177 TRP A CD1 1 
ATOM   1380 C CD2 . TRP A 1 177 ? 10.141  16.577  13.517 1.00 13.02  ? 177 TRP A CD2 1 
ATOM   1381 N NE1 . TRP A 1 177 ? 7.986   15.948  13.510 1.00 13.80  ? 177 TRP A NE1 1 
ATOM   1382 C CE2 . TRP A 1 177 ? 8.989   16.418  14.320 1.00 15.01  ? 177 TRP A CE2 1 
ATOM   1383 C CE3 . TRP A 1 177 ? 11.320  17.055  14.105 1.00 13.27  ? 177 TRP A CE3 1 
ATOM   1384 C CZ2 . TRP A 1 177 ? 8.979   16.714  15.681 1.00 10.12  ? 177 TRP A CZ2 1 
ATOM   1385 C CZ3 . TRP A 1 177 ? 11.313  17.343  15.464 1.00 18.83  ? 177 TRP A CZ3 1 
ATOM   1386 C CH2 . TRP A 1 177 ? 10.146  17.175  16.235 1.00 16.52  ? 177 TRP A CH2 1 
ATOM   1387 N N   . GLY A 1 178 ? 10.859  15.117  7.541  1.00 13.84  ? 178 GLY A N   1 
ATOM   1388 C CA  . GLY A 1 178 ? 11.535  15.414  6.299  1.00 13.48  ? 178 GLY A CA  1 
ATOM   1389 C C   . GLY A 1 178 ? 13.017  15.124  6.381  1.00 11.23  ? 178 GLY A C   1 
ATOM   1390 O O   . GLY A 1 178 ? 13.587  14.885  7.448  1.00 11.12  ? 178 GLY A O   1 
ATOM   1391 N N   . THR A 1 179 ? 13.650  15.144  5.215  1.00 11.41  ? 179 THR A N   1 
ATOM   1392 C CA  . THR A 1 179 ? 15.067  14.817  5.131  1.00 14.03  ? 179 THR A CA  1 
ATOM   1393 C C   . THR A 1 179 ? 15.988  15.953  5.576  1.00 12.87  ? 179 THR A C   1 
ATOM   1394 O O   . THR A 1 179 ? 17.180  15.708  5.785  1.00 11.23  ? 179 THR A O   1 
ATOM   1395 C CB  . THR A 1 179 ? 15.406  14.392  3.699  1.00 12.87  ? 179 THR A CB  1 
ATOM   1396 O OG1 . THR A 1 179 ? 15.069  15.453  2.794  1.00 18.02  ? 179 THR A OG1 1 
ATOM   1397 C CG2 . THR A 1 179 ? 14.622  13.140  3.311  1.00 9.45   ? 179 THR A CG2 1 
ATOM   1398 N N   . GLY A 1 180 ? 15.469  17.166  5.786  1.00 14.24  ? 180 GLY A N   1 
ATOM   1399 C CA  . GLY A 1 180 ? 16.296  18.274  6.222  1.00 12.31  ? 180 GLY A CA  1 
ATOM   1400 C C   . GLY A 1 180 ? 16.487  18.406  7.710  1.00 15.97  ? 180 GLY A C   1 
ATOM   1401 O O   . GLY A 1 180 ? 17.295  19.222  8.159  1.00 25.84  ? 180 GLY A O   1 
ATOM   1402 N N   . TRP A 1 181 ? 15.760  17.626  8.495  1.00 15.65  ? 181 TRP A N   1 
ATOM   1403 C CA  . TRP A 1 181 ? 15.878  17.635  9.945  1.00 12.45  ? 181 TRP A CA  1 
ATOM   1404 C C   . TRP A 1 181 ? 16.879  16.577  10.389 1.00 13.31  ? 181 TRP A C   1 
ATOM   1405 O O   . TRP A 1 181 ? 16.926  15.484  9.819  1.00 13.93  ? 181 TRP A O   1 
ATOM   1406 C CB  . TRP A 1 181 ? 14.522  17.388  10.608 1.00 16.43  ? 181 TRP A CB  1 
ATOM   1407 C CG  . TRP A 1 181 ? 14.601  17.391  12.114 1.00 20.20  ? 181 TRP A CG  1 
ATOM   1408 C CD1 . TRP A 1 181 ? 14.522  18.476  12.951 1.00 15.04  ? 181 TRP A CD1 1 
ATOM   1409 C CD2 . TRP A 1 181 ? 14.781  16.245  12.959 1.00 16.94  ? 181 TRP A CD2 1 
ATOM   1410 N NE1 . TRP A 1 181 ? 14.646  18.070  14.259 1.00 14.13  ? 181 TRP A NE1 1 
ATOM   1411 C CE2 . TRP A 1 181 ? 14.808  16.709  14.294 1.00 14.83  ? 181 TRP A CE2 1 
ATOM   1412 C CE3 . TRP A 1 181 ? 14.932  14.870  12.715 1.00 13.84  ? 181 TRP A CE3 1 
ATOM   1413 C CZ2 . TRP A 1 181 ? 14.963  15.843  15.389 1.00 14.77  ? 181 TRP A CZ2 1 
ATOM   1414 C CZ3 . TRP A 1 181 ? 15.099  14.007  13.808 1.00 15.26  ? 181 TRP A CZ3 1 
ATOM   1415 C CH2 . TRP A 1 181 ? 15.109  14.501  15.128 1.00 12.03  ? 181 TRP A CH2 1 
ATOM   1416 N N   . GLY A 1 182 ? 17.722  16.933  11.357 1.00 9.94   ? 182 GLY A N   1 
ATOM   1417 C CA  . GLY A 1 182 ? 18.606  15.955  11.970 1.00 9.55   ? 182 GLY A CA  1 
ATOM   1418 C C   . GLY A 1 182 ? 19.623  15.442  10.978 1.00 9.97   ? 182 GLY A C   1 
ATOM   1419 O O   . GLY A 1 182 ? 20.104  16.182  10.114 1.00 13.40  ? 182 GLY A O   1 
ATOM   1420 N N   . GLU A 1 183 ? 19.950  14.152  11.095 1.00 11.68  ? 183 GLU A N   1 
ATOM   1421 C CA  . GLU A 1 183 ? 20.945  13.501  10.241 1.00 9.36   ? 183 GLU A CA  1 
ATOM   1422 C C   . GLU A 1 183 ? 20.214  12.878  9.059  1.00 13.99  ? 183 GLU A C   1 
ATOM   1423 O O   . GLU A 1 183 ? 19.868  11.694  9.042  1.00 12.81  ? 183 GLU A O   1 
ATOM   1424 C CB  . GLU A 1 183 ? 21.791  12.486  11.006 1.00 13.20  ? 183 GLU A CB  1 
ATOM   1425 C CG  . GLU A 1 183 ? 22.547  13.141  12.184 1.00 17.25  ? 183 GLU A CG  1 
ATOM   1426 C CD  . GLU A 1 183 ? 23.513  12.193  12.907 1.00 24.37  ? 183 GLU A CD  1 
ATOM   1427 O OE1 . GLU A 1 183 ? 23.199  10.987  13.014 1.00 18.77  ? 183 GLU A OE1 1 
ATOM   1428 O OE2 . GLU A 1 183 ? 24.591  12.652  13.368 1.00 19.27  ? 183 GLU A OE2 1 
ATOM   1429 N N   . ASN A 1 184 ? 19.919  13.737  8.077  1.00 17.15  ? 184 ASN A N   1 
ATOM   1430 C CA  . ASN A 1 184 ? 19.154  13.379  6.880  1.00 18.35  ? 184 ASN A CA  1 
ATOM   1431 C C   . ASN A 1 184 ? 17.805  12.758  7.253  1.00 16.01  ? 184 ASN A C   1 
ATOM   1432 O O   . ASN A 1 184 ? 17.307  11.844  6.590  1.00 12.01  ? 184 ASN A O   1 
ATOM   1433 C CB  . ASN A 1 184 ? 19.966  12.402  6.025  1.00 17.55  ? 184 ASN A CB  1 
ATOM   1434 C CG  . ASN A 1 184 ? 21.216  13.020  5.455  1.00 19.19  ? 184 ASN A CG  1 
ATOM   1435 O OD1 . ASN A 1 184 ? 21.359  14.242  5.389  1.00 21.06  ? 184 ASN A OD1 1 
ATOM   1436 N ND2 . ASN A 1 184 ? 22.147  12.171  5.054  1.00 33.13  ? 184 ASN A ND2 1 
ATOM   1437 N N   . GLY A 1 185 ? 17.212  13.266  8.331  1.00 11.15  ? 185 GLY A N   1 
ATOM   1438 C CA  . GLY A 1 185 ? 15.909  12.836  8.780  1.00 12.61  ? 185 GLY A CA  1 
ATOM   1439 C C   . GLY A 1 185 ? 15.974  11.907  9.966  1.00 11.31  ? 185 GLY A C   1 
ATOM   1440 O O   . GLY A 1 185 ? 14.927  11.538  10.508 1.00 10.23  ? 185 GLY A O   1 
ATOM   1441 N N   . TYR A 1 186 ? 17.178  11.524  10.381 1.00 15.58  ? 186 TYR A N   1 
ATOM   1442 C CA  . TYR A 1 186 ? 17.385  10.599  11.477 1.00 14.65  ? 186 TYR A CA  1 
ATOM   1443 C C   . TYR A 1 186 ? 17.948  11.342  12.680 1.00 16.16  ? 186 TYR A C   1 
ATOM   1444 O O   . TYR A 1 186 ? 18.514  12.434  12.571 1.00 11.77  ? 186 TYR A O   1 
ATOM   1445 C CB  . TYR A 1 186 ? 18.330  9.476   11.030 1.00 16.08  ? 186 TYR A CB  1 
ATOM   1446 C CG  . TYR A 1 186 ? 17.690  8.547   9.999  1.00 13.83  ? 186 TYR A CG  1 
ATOM   1447 C CD1 . TYR A 1 186 ? 17.655  8.904   8.652  1.00 12.08  ? 186 TYR A CD1 1 
ATOM   1448 C CD2 . TYR A 1 186 ? 17.117  7.335   10.366 1.00 15.06  ? 186 TYR A CD2 1 
ATOM   1449 C CE1 . TYR A 1 186 ? 17.086  8.083   7.693  1.00 11.95  ? 186 TYR A CE1 1 
ATOM   1450 C CE2 . TYR A 1 186 ? 16.537  6.493   9.402  1.00 19.01  ? 186 TYR A CE2 1 
ATOM   1451 C CZ  . TYR A 1 186 ? 16.522  6.880   8.068  1.00 18.47  ? 186 TYR A CZ  1 
ATOM   1452 O OH  . TYR A 1 186 ? 15.951  6.077   7.101  1.00 13.96  ? 186 TYR A OH  1 
ATOM   1453 N N   . ILE A 1 187 ? 17.794  10.719  13.836 1.00 15.99  ? 187 ILE A N   1 
ATOM   1454 C CA  . ILE A 1 187 ? 18.451  11.165  15.056 1.00 13.04  ? 187 ILE A CA  1 
ATOM   1455 C C   . ILE A 1 187 ? 19.027  9.951   15.755 1.00 10.81  ? 187 ILE A C   1 
ATOM   1456 O O   . ILE A 1 187 ? 18.394  8.894   15.821 1.00 12.83  ? 187 ILE A O   1 
ATOM   1457 C CB  . ILE A 1 187 ? 17.475  11.941  15.974 1.00 18.07  ? 187 ILE A CB  1 
ATOM   1458 C CG1 . ILE A 1 187 ? 18.161  12.398  17.264 1.00 11.51  ? 187 ILE A CG1 1 
ATOM   1459 C CG2 . ILE A 1 187 ? 16.197  11.134  16.258 1.00 15.11  ? 187 ILE A CG2 1 
ATOM   1460 C CD1 . ILE A 1 187 ? 17.353  13.432  18.029 1.00 14.93  ? 187 ILE A CD1 1 
ATOM   1461 N N   . ARG A 1 188 ? 20.217  10.098  16.286 1.00 11.90  ? 188 ARG A N   1 
ATOM   1462 C CA  . ARG A 1 188 ? 20.792  9.091   17.155 1.00 11.25  ? 188 ARG A CA  1 
ATOM   1463 C C   . ARG A 1 188 ? 20.623  9.583   18.578 1.00 15.99  ? 188 ARG A C   1 
ATOM   1464 O O   . ARG A 1 188 ? 21.074  10.681  18.917 1.00 18.35  ? 188 ARG A O   1 
ATOM   1465 C CB  . ARG A 1 188 ? 22.254  8.843   16.801 1.00 11.49  ? 188 ARG A CB  1 
ATOM   1466 C CG  . ARG A 1 188 ? 22.394  8.106   15.474 1.00 10.90  ? 188 ARG A CG  1 
ATOM   1467 C CD  . ARG A 1 188 ? 23.827  7.947   15.078 1.00 14.94  ? 188 ARG A CD  1 
ATOM   1468 N NE  . ARG A 1 188 ? 24.411  9.251   14.799 1.00 22.11  ? 188 ARG A NE  1 
ATOM   1469 C CZ  . ARG A 1 188 ? 25.652  9.590   15.116 1.00 20.00  ? 188 ARG A CZ  1 
ATOM   1470 N NH1 . ARG A 1 188 ? 26.481  8.720   15.668 1.00 15.70  ? 188 ARG A NH1 1 
ATOM   1471 N NH2 . ARG A 1 188 ? 26.060  10.837  14.899 1.00 12.71  ? 188 ARG A NH2 1 
ATOM   1472 N N   . ILE A 1 189 ? 19.920  8.814   19.395 1.00 18.24  ? 189 ILE A N   1 
ATOM   1473 C CA  . ILE A 1 189 ? 19.605  9.247   20.744 1.00 20.02  ? 189 ILE A CA  1 
ATOM   1474 C C   . ILE A 1 189 ? 20.455  8.424   21.688 1.00 18.23  ? 189 ILE A C   1 
ATOM   1475 O O   . ILE A 1 189 ? 20.546  7.203   21.538 1.00 19.75  ? 189 ILE A O   1 
ATOM   1476 C CB  . ILE A 1 189 ? 18.104  9.082   21.045 1.00 22.36  ? 189 ILE A CB  1 
ATOM   1477 C CG1 . ILE A 1 189 ? 17.284  9.933   20.077 1.00 14.21  ? 189 ILE A CG1 1 
ATOM   1478 C CG2 . ILE A 1 189 ? 17.778  9.430   22.498 1.00 22.05  ? 189 ILE A CG2 1 
ATOM   1479 C CD1 . ILE A 1 189 ? 15.813  9.949   20.388 1.00 16.89  ? 189 ILE A CD1 1 
ATOM   1480 N N   . LYS A 1 190 ? 21.139  9.102   22.607 1.00 15.74  ? 190 LYS A N   1 
ATOM   1481 C CA  . LYS A 1 190 ? 22.017  8.417   23.548 1.00 19.57  ? 190 LYS A CA  1 
ATOM   1482 C C   . LYS A 1 190 ? 21.271  7.321   24.295 1.00 19.19  ? 190 LYS A C   1 
ATOM   1483 O O   . LYS A 1 190 ? 20.111  7.486   24.680 1.00 23.31  ? 190 LYS A O   1 
ATOM   1484 C CB  . LYS A 1 190 ? 22.656  9.402   24.525 1.00 22.23  ? 190 LYS A CB  1 
ATOM   1485 C CG  . LYS A 1 190 ? 23.546  8.715   25.553 1.00 27.39  ? 190 LYS A CG  1 
ATOM   1486 C CD  . LYS A 1 190 ? 25.006  9.110   25.445 1.00 23.88  ? 190 LYS A CD  1 
ATOM   1487 C CE  . LYS A 1 190 ? 25.767  8.654   26.683 1.00 31.73  ? 190 LYS A CE  1 
ATOM   1488 N NZ  . LYS A 1 190 ? 26.885  9.570   27.068 1.00 30.63  ? 190 LYS A NZ  1 
ATOM   1489 N N   . ARG A 1 191 ? 21.944  6.195   24.498 1.00 20.40  ? 191 ARG A N   1 
ATOM   1490 C CA  . ARG A 1 191 ? 21.425  5.145   25.356 1.00 20.61  ? 191 ARG A CA  1 
ATOM   1491 C C   . ARG A 1 191 ? 22.489  4.803   26.391 1.00 18.97  ? 191 ARG A C   1 
ATOM   1492 O O   . ARG A 1 191 ? 23.610  5.314   26.358 1.00 22.98  ? 191 ARG A O   1 
ATOM   1493 C CB  . ARG A 1 191 ? 21.027  3.897   24.550 1.00 19.53  ? 191 ARG A CB  1 
ATOM   1494 C CG  . ARG A 1 191 ? 22.206  3.060   24.052 1.00 16.99  ? 191 ARG A CG  1 
ATOM   1495 C CD  . ARG A 1 191 ? 21.702  1.809   23.352 1.00 18.74  ? 191 ARG A CD  1 
ATOM   1496 N NE  . ARG A 1 191 ? 22.781  0.899   22.980 1.00 19.75  ? 191 ARG A NE  1 
ATOM   1497 C CZ  . ARG A 1 191 ? 23.323  0.002   23.793 1.00 15.54  ? 191 ARG A CZ  1 
ATOM   1498 N NH1 . ARG A 1 191 ? 22.966  -0.087  25.065 1.00 14.58  ? 191 ARG A NH1 1 
ATOM   1499 N NH2 . ARG A 1 191 ? 24.261  -0.811  23.323 1.00 17.95  ? 191 ARG A NH2 1 
ATOM   1500 N N   . GLY A 1 192 ? 22.115  3.958   27.345 1.00 16.63  ? 192 GLY A N   1 
ATOM   1501 C CA  . GLY A 1 192 ? 23.060  3.522   28.346 1.00 16.79  ? 192 GLY A CA  1 
ATOM   1502 C C   . GLY A 1 192 ? 23.253  4.494   29.486 1.00 27.27  ? 192 GLY A C   1 
ATOM   1503 O O   . GLY A 1 192 ? 24.254  4.399   30.204 1.00 30.42  ? 192 GLY A O   1 
ATOM   1504 N N   . THR A 1 193 ? 22.323  5.430   29.678 1.00 22.06  ? 193 THR A N   1 
ATOM   1505 C CA  . THR A 1 193 ? 22.422  6.425   30.736 1.00 19.56  ? 193 THR A CA  1 
ATOM   1506 C C   . THR A 1 193 ? 21.901  5.922   32.073 1.00 24.16  ? 193 THR A C   1 
ATOM   1507 O O   . THR A 1 193 ? 22.077  6.609   33.084 1.00 25.50  ? 193 THR A O   1 
ATOM   1508 C CB  . THR A 1 193 ? 21.651  7.691   30.354 1.00 31.52  ? 193 THR A CB  1 
ATOM   1509 O OG1 . THR A 1 193 ? 20.237  7.442   30.442 1.00 27.51  ? 193 THR A OG1 1 
ATOM   1510 C CG2 . THR A 1 193 ? 22.018  8.142   28.969 1.00 16.23  ? 193 THR A CG2 1 
ATOM   1511 N N   . GLY A 1 194 ? 21.232  4.775   32.097 1.00 24.72  ? 194 GLY A N   1 
ATOM   1512 C CA  . GLY A 1 194 ? 20.694  4.243   33.327 1.00 27.48  ? 194 GLY A CA  1 
ATOM   1513 C C   . GLY A 1 194 ? 19.371  4.835   33.737 1.00 29.51  ? 194 GLY A C   1 
ATOM   1514 O O   . GLY A 1 194 ? 18.838  4.452   34.786 1.00 40.46  ? 194 GLY A O   1 
ATOM   1515 N N   . ASN A 1 195 ? 18.834  5.764   32.956 1.00 27.89  ? 195 ASN A N   1 
ATOM   1516 C CA  . ASN A 1 195 ? 17.517  6.327   33.200 1.00 34.36  ? 195 ASN A CA  1 
ATOM   1517 C C   . ASN A 1 195 ? 16.505  5.388   32.553 1.00 39.99  ? 195 ASN A C   1 
ATOM   1518 O O   . ASN A 1 195 ? 16.588  5.116   31.350 1.00 38.56  ? 195 ASN A O   1 
ATOM   1519 C CB  . ASN A 1 195 ? 17.428  7.746   32.637 1.00 34.34  ? 195 ASN A CB  1 
ATOM   1520 C CG  . ASN A 1 195 ? 16.005  8.255   32.528 1.00 39.30  ? 195 ASN A CG  1 
ATOM   1521 O OD1 . ASN A 1 195 ? 15.106  7.805   33.246 1.00 40.97  ? 195 ASN A OD1 1 
ATOM   1522 N ND2 . ASN A 1 195 ? 15.794  9.216   31.634 1.00 31.65  ? 195 ASN A ND2 1 
ATOM   1523 N N   . SER A 1 196 ? 15.562  4.876   33.346 1.00 35.85  ? 196 SER A N   1 
ATOM   1524 C CA  . SER A 1 196 ? 14.707  3.810   32.833 1.00 37.03  ? 196 SER A CA  1 
ATOM   1525 C C   . SER A 1 196 ? 13.681  4.332   31.836 1.00 29.10  ? 196 SER A C   1 
ATOM   1526 O O   . SER A 1 196 ? 13.187  3.563   31.003 1.00 27.28  ? 196 SER A O   1 
ATOM   1527 C CB  . SER A 1 196 ? 14.014  3.078   33.987 1.00 29.91  ? 196 SER A CB  1 
ATOM   1528 O OG  . SER A 1 196 ? 14.768  1.942   34.384 1.00 30.13  ? 196 SER A OG  1 
ATOM   1529 N N   . TYR A 1 197 ? 13.328  5.615   31.914 1.00 29.33  ? 197 TYR A N   1 
ATOM   1530 C CA  . TYR A 1 197 ? 12.460  6.186   30.895 1.00 29.26  ? 197 TYR A CA  1 
ATOM   1531 C C   . TYR A 1 197 ? 13.108  6.179   29.520 1.00 28.84  ? 197 TYR A C   1 
ATOM   1532 O O   . TYR A 1 197 ? 12.391  6.197   28.513 1.00 22.32  ? 197 TYR A O   1 
ATOM   1533 C CB  . TYR A 1 197 ? 12.017  7.609   31.250 1.00 32.15  ? 197 TYR A CB  1 
ATOM   1534 C CG  . TYR A 1 197 ? 11.004  7.705   32.369 1.00 42.11  ? 197 TYR A CG  1 
ATOM   1535 C CD1 . TYR A 1 197 ? 9.657   7.460   32.119 1.00 40.64  ? 197 TYR A CD1 1 
ATOM   1536 C CD2 . TYR A 1 197 ? 11.370  8.112   33.649 1.00 41.70  ? 197 TYR A CD2 1 
ATOM   1537 C CE1 . TYR A 1 197 ? 8.712   7.562   33.119 1.00 48.57  ? 197 TYR A CE1 1 
ATOM   1538 C CE2 . TYR A 1 197 ? 10.423  8.222   34.659 1.00 46.57  ? 197 TYR A CE2 1 
ATOM   1539 C CZ  . TYR A 1 197 ? 9.095   7.945   34.385 1.00 52.76  ? 197 TYR A CZ  1 
ATOM   1540 O OH  . TYR A 1 197 ? 8.139   8.047   35.370 1.00 52.97  ? 197 TYR A OH  1 
ATOM   1541 N N   . GLY A 1 198 ? 14.438  6.142   29.449 1.00 27.47  ? 198 GLY A N   1 
ATOM   1542 C CA  . GLY A 1 198 ? 15.136  6.420   28.208 1.00 26.73  ? 198 GLY A CA  1 
ATOM   1543 C C   . GLY A 1 198 ? 15.316  7.908   28.017 1.00 21.50  ? 198 GLY A C   1 
ATOM   1544 O O   . GLY A 1 198 ? 14.522  8.704   28.526 1.00 26.42  ? 198 GLY A O   1 
ATOM   1545 N N   . VAL A 1 199 ? 16.345  8.303   27.274 1.00 19.00  ? 199 VAL A N   1 
ATOM   1546 C CA  . VAL A 1 199 ? 16.472  9.702   26.902 1.00 19.71  ? 199 VAL A CA  1 
ATOM   1547 C C   . VAL A 1 199 ? 15.224  10.131  26.151 1.00 17.07  ? 199 VAL A C   1 
ATOM   1548 O O   . VAL A 1 199 ? 14.781  9.462   25.211 1.00 22.32  ? 199 VAL A O   1 
ATOM   1549 C CB  . VAL A 1 199 ? 17.739  9.907   26.058 1.00 28.94  ? 199 VAL A CB  1 
ATOM   1550 C CG1 . VAL A 1 199 ? 17.810  11.339  25.522 1.00 19.80  ? 199 VAL A CG1 1 
ATOM   1551 C CG2 . VAL A 1 199 ? 18.986  9.543   26.867 1.00 21.50  ? 199 VAL A CG2 1 
ATOM   1552 N N   . CYS A 1 200 ? 14.655  11.265  26.567 1.00 18.19  ? 200 CYS A N   1 
ATOM   1553 C CA  . CYS A 1 200 ? 13.397  11.781  26.029 1.00 16.46  ? 200 CYS A CA  1 
ATOM   1554 C C   . CYS A 1 200 ? 12.246  10.784  26.165 1.00 18.39  ? 200 CYS A C   1 
ATOM   1555 O O   . CYS A 1 200 ? 11.324  10.787  25.346 1.00 21.81  ? 200 CYS A O   1 
ATOM   1556 C CB  . CYS A 1 200 ? 13.535  12.216  24.567 1.00 20.75  ? 200 CYS A CB  1 
ATOM   1557 S SG  . CYS A 1 200 ? 14.905  13.328  24.191 1.00 34.33  ? 200 CYS A SG  1 
ATOM   1558 N N   . GLY A 1 201 ? 12.273  9.921   27.183 1.00 21.37  ? 201 GLY A N   1 
ATOM   1559 C CA  . GLY A 1 201 ? 11.186  8.965   27.365 1.00 18.32  ? 201 GLY A CA  1 
ATOM   1560 C C   . GLY A 1 201 ? 11.127  7.875   26.323 1.00 20.55  ? 201 GLY A C   1 
ATOM   1561 O O   . GLY A 1 201 ? 10.068  7.268   26.131 1.00 17.89  ? 201 GLY A O   1 
ATOM   1562 N N   . LEU A 1 202 ? 12.256  7.597   25.660 1.00 20.27  ? 202 LEU A N   1 
ATOM   1563 C CA  . LEU A 1 202 ? 12.297  6.711   24.499 1.00 22.56  ? 202 LEU A CA  1 
ATOM   1564 C C   . LEU A 1 202 ? 11.795  5.296   24.777 1.00 21.12  ? 202 LEU A C   1 
ATOM   1565 O O   . LEU A 1 202 ? 11.452  4.580   23.831 1.00 20.93  ? 202 LEU A O   1 
ATOM   1566 C CB  . LEU A 1 202 ? 13.737  6.654   23.974 1.00 23.99  ? 202 LEU A CB  1 
ATOM   1567 C CG  . LEU A 1 202 ? 14.011  5.919   22.657 1.00 25.94  ? 202 LEU A CG  1 
ATOM   1568 C CD1 . LEU A 1 202 ? 13.206  6.513   21.501 1.00 16.02  ? 202 LEU A CD1 1 
ATOM   1569 C CD2 . LEU A 1 202 ? 15.486  5.911   22.343 1.00 21.95  ? 202 LEU A CD2 1 
ATOM   1570 N N   . TYR A 1 203 ? 11.752  4.862   26.031 1.00 23.16  ? 203 TYR A N   1 
ATOM   1571 C CA  . TYR A 1 203 ? 11.336  3.504   26.360 1.00 23.32  ? 203 TYR A CA  1 
ATOM   1572 C C   . TYR A 1 203 ? 9.894   3.431   26.856 1.00 19.39  ? 203 TYR A C   1 
ATOM   1573 O O   . TYR A 1 203 ? 9.494   2.401   27.410 1.00 23.59  ? 203 TYR A O   1 
ATOM   1574 C CB  . TYR A 1 203 ? 12.286  2.894   27.398 1.00 20.42  ? 203 TYR A CB  1 
ATOM   1575 C CG  . TYR A 1 203 ? 13.766  2.996   27.061 1.00 30.81  ? 203 TYR A CG  1 
ATOM   1576 C CD1 . TYR A 1 203 ? 14.204  3.064   25.738 1.00 26.29  ? 203 TYR A CD1 1 
ATOM   1577 C CD2 . TYR A 1 203 ? 14.726  3.038   28.071 1.00 31.90  ? 203 TYR A CD2 1 
ATOM   1578 C CE1 . TYR A 1 203 ? 15.549  3.152   25.433 1.00 22.34  ? 203 TYR A CE1 1 
ATOM   1579 C CE2 . TYR A 1 203 ? 16.083  3.141   27.775 1.00 33.13  ? 203 TYR A CE2 1 
ATOM   1580 C CZ  . TYR A 1 203 ? 16.488  3.197   26.456 1.00 38.12  ? 203 TYR A CZ  1 
ATOM   1581 O OH  . TYR A 1 203 ? 17.832  3.296   26.164 1.00 29.44  ? 203 TYR A OH  1 
ATOM   1582 N N   . THR A 1 204 ? 9.099   4.484   26.651 1.00 17.03  ? 204 THR A N   1 
ATOM   1583 C CA  . THR A 1 204 ? 7.770   4.543   27.261 1.00 19.63  ? 204 THR A CA  1 
ATOM   1584 C C   . THR A 1 204 ? 6.779   3.568   26.633 1.00 18.05  ? 204 THR A C   1 
ATOM   1585 O O   . THR A 1 204 ? 6.035   2.892   27.350 1.00 21.05  ? 204 THR A O   1 
ATOM   1586 C CB  . THR A 1 204 ? 7.213   5.960   27.137 1.00 19.48  ? 204 THR A CB  1 
ATOM   1587 O OG1 . THR A 1 204 ? 8.062   6.879   27.834 1.00 23.92  ? 204 THR A OG1 1 
ATOM   1588 C CG2 . THR A 1 204 ? 5.804   6.034   27.706 1.00 15.74  ? 204 THR A CG2 1 
ATOM   1589 N N   . SER A 1 205 ? 6.774   3.448   25.305 1.00 21.90  ? 205 SER A N   1 
ATOM   1590 C CA  . SER A 1 205 ? 5.674   2.750   24.639 1.00 21.34  ? 205 SER A CA  1 
ATOM   1591 C C   . SER A 1 205 ? 6.145   2.313   23.254 1.00 16.11  ? 205 SER A C   1 
ATOM   1592 O O   . SER A 1 205 ? 6.209   3.135   22.336 1.00 19.18  ? 205 SER A O   1 
ATOM   1593 C CB  . SER A 1 205 ? 4.436   3.635   24.556 1.00 21.33  ? 205 SER A CB  1 
ATOM   1594 O OG  . SER A 1 205 ? 3.329   2.942   24.002 1.00 21.85  ? 205 SER A OG  1 
ATOM   1595 N N   . SER A 1 206 ? 6.478   1.034   23.118 1.00 15.24  ? 206 SER A N   1 
ATOM   1596 C CA  . SER A 1 206 ? 7.091   0.528   21.902 1.00 14.82  ? 206 SER A CA  1 
ATOM   1597 C C   . SER A 1 206 ? 6.338   -0.701  21.416 1.00 13.52  ? 206 SER A C   1 
ATOM   1598 O O   . SER A 1 206 ? 6.058   -1.614  22.196 1.00 19.69  ? 206 SER A O   1 
ATOM   1599 C CB  . SER A 1 206 ? 8.560   0.199   22.125 1.00 11.58  ? 206 SER A CB  1 
ATOM   1600 O OG  . SER A 1 206 ? 9.218   1.311   22.692 1.00 16.77  ? 206 SER A OG  1 
ATOM   1601 N N   . PHE A 1 207 ? 6.026   -0.724  20.125 1.00 15.61  ? 207 PHE A N   1 
ATOM   1602 C CA  . PHE A 1 207 ? 5.216   -1.777  19.536 1.00 24.44  ? 207 PHE A CA  1 
ATOM   1603 C C   . PHE A 1 207 ? 5.857   -2.188  18.223 1.00 18.71  ? 207 PHE A C   1 
ATOM   1604 O O   . PHE A 1 207 ? 6.539   -1.392  17.573 1.00 17.36  ? 207 PHE A O   1 
ATOM   1605 C CB  . PHE A 1 207 ? 3.765   -1.334  19.255 1.00 15.98  ? 207 PHE A CB  1 
ATOM   1606 C CG  . PHE A 1 207 ? 2.948   -1.083  20.492 1.00 19.65  ? 207 PHE A CG  1 
ATOM   1607 C CD1 . PHE A 1 207 ? 2.952   0.165   21.098 1.00 21.93  ? 207 PHE A CD1 1 
ATOM   1608 C CD2 . PHE A 1 207 ? 2.182   -2.088  21.054 1.00 21.62  ? 207 PHE A CD2 1 
ATOM   1609 C CE1 . PHE A 1 207 ? 2.195   0.410   22.241 1.00 20.96  ? 207 PHE A CE1 1 
ATOM   1610 C CE2 . PHE A 1 207 ? 1.430   -1.854  22.195 1.00 20.48  ? 207 PHE A CE2 1 
ATOM   1611 C CZ  . PHE A 1 207 ? 1.438   -0.605  22.788 1.00 24.02  ? 207 PHE A CZ  1 
ATOM   1612 N N   . TYR A 1 208 ? 5.615   -3.429  17.825 1.00 20.14  ? 208 TYR A N   1 
ATOM   1613 C CA  . TYR A 1 208 ? 6.098   -3.877  16.534 1.00 21.74  ? 208 TYR A CA  1 
ATOM   1614 C C   . TYR A 1 208 ? 5.076   -4.839  15.954 1.00 18.02  ? 208 TYR A C   1 
ATOM   1615 O O   . TYR A 1 208 ? 4.382   -5.544  16.699 1.00 17.17  ? 208 TYR A O   1 
ATOM   1616 C CB  . TYR A 1 208 ? 7.485   -4.543  16.633 1.00 19.44  ? 208 TYR A CB  1 
ATOM   1617 C CG  . TYR A 1 208 ? 7.610   -5.685  17.623 1.00 22.78  ? 208 TYR A CG  1 
ATOM   1618 C CD1 . TYR A 1 208 ? 7.931   -5.447  18.955 1.00 23.33  ? 208 TYR A CD1 1 
ATOM   1619 C CD2 . TYR A 1 208 ? 7.443   -7.009  17.217 1.00 25.43  ? 208 TYR A CD2 1 
ATOM   1620 C CE1 . TYR A 1 208 ? 8.067   -6.498  19.865 1.00 19.78  ? 208 TYR A CE1 1 
ATOM   1621 C CE2 . TYR A 1 208 ? 7.577   -8.067  18.118 1.00 25.38  ? 208 TYR A CE2 1 
ATOM   1622 C CZ  . TYR A 1 208 ? 7.885   -7.803  19.439 1.00 27.06  ? 208 TYR A CZ  1 
ATOM   1623 O OH  . TYR A 1 208 ? 7.998   -8.846  20.330 1.00 23.02  ? 208 TYR A OH  1 
ATOM   1624 N N   . PRO A 1 209 ? 4.981   -4.910  14.630 1.00 19.41  ? 209 PRO A N   1 
ATOM   1625 C CA  . PRO A 1 209 ? 4.070   -5.871  14.012 1.00 13.19  ? 209 PRO A CA  1 
ATOM   1626 C C   . PRO A 1 209 ? 4.668   -7.259  13.980 1.00 17.33  ? 209 PRO A C   1 
ATOM   1627 O O   . PRO A 1 209 ? 5.886   -7.447  13.941 1.00 21.55  ? 209 PRO A O   1 
ATOM   1628 C CB  . PRO A 1 209 ? 3.907   -5.320  12.593 1.00 21.52  ? 209 PRO A CB  1 
ATOM   1629 C CG  . PRO A 1 209 ? 5.273   -4.727  12.314 1.00 19.83  ? 209 PRO A CG  1 
ATOM   1630 C CD  . PRO A 1 209 ? 5.633   -4.052  13.623 1.00 20.19  ? 209 PRO A CD  1 
ATOM   1631 N N   . VAL A 1 210 ? 3.787   -8.245  14.014 1.00 21.49  ? 210 VAL A N   1 
ATOM   1632 C CA  . VAL A 1 210 ? 4.179   -9.634  13.889 1.00 20.72  ? 210 VAL A CA  1 
ATOM   1633 C C   . VAL A 1 210 ? 3.641   -10.143 12.565 1.00 23.21  ? 210 VAL A C   1 
ATOM   1634 O O   . VAL A 1 210 ? 2.462   -9.927  12.239 1.00 26.09  ? 210 VAL A O   1 
ATOM   1635 C CB  . VAL A 1 210 ? 3.652   -10.468 15.064 1.00 23.72  ? 210 VAL A CB  1 
ATOM   1636 C CG1 . VAL A 1 210 ? 3.803   -11.951 14.765 1.00 30.22  ? 210 VAL A CG1 1 
ATOM   1637 C CG2 . VAL A 1 210 ? 4.379   -10.083 16.331 1.00 24.36  ? 210 VAL A CG2 1 
ATOM   1638 N N   . LYS A 1 211 ? 4.498   -10.847 11.831 1.00 27.19  ? 211 LYS A N   1 
ATOM   1639 C CA  . LYS A 1 211 ? 4.189   -11.403 10.524 1.00 28.48  ? 211 LYS A CA  1 
ATOM   1640 C C   . LYS A 1 211 ? 4.895   -12.745 10.438 1.00 33.08  ? 211 LYS A C   1 
ATOM   1641 O O   . LYS A 1 211 ? 6.127   -12.803 10.474 1.00 34.51  ? 211 LYS A O   1 
ATOM   1642 C CB  . LYS A 1 211 ? 4.619   -10.481 9.389  1.00 29.54  ? 211 LYS A CB  1 
ATOM   1643 C CG  . LYS A 1 211 ? 3.721   -10.606 8.165  1.00 34.61  ? 211 LYS A CG  1 
ATOM   1644 C CD  . LYS A 1 211 ? 4.450   -11.150 6.957  1.00 35.51  ? 211 LYS A CD  1 
ATOM   1645 C CE  . LYS A 1 211 ? 3.559   -11.073 5.733  1.00 29.01  ? 211 LYS A CE  1 
ATOM   1646 N NZ  . LYS A 1 211 ? 2.303   -11.842 5.984  1.00 36.81  ? 211 LYS A NZ  1 
ATOM   1647 N N   . ASN A 1 212 ? 4.120   -13.814 10.305 1.00 41.70  ? 212 ASN A N   1 
ATOM   1648 C CA  . ASN A 1 212 ? 4.661   -15.164 10.208 1.00 50.27  ? 212 ASN A CA  1 
ATOM   1649 C C   . ASN A 1 212 ? 5.228   -15.478 8.821  1.00 61.44  ? 212 ASN A C   1 
ATOM   1650 O O   . ASN A 1 212 ? 6.144   -16.296 8.693  1.00 67.32  ? 212 ASN A O   1 
ATOM   1651 C CB  . ASN A 1 212 ? 3.571   -16.174 10.565 1.00 42.68  ? 212 ASN A CB  1 
ATOM   1652 C CG  . ASN A 1 212 ? 2.947   -15.899 11.926 1.00 57.49  ? 212 ASN A CG  1 
ATOM   1653 O OD1 . ASN A 1 212 ? 3.639   -15.537 12.883 1.00 45.24  ? 212 ASN A OD1 1 
ATOM   1654 N ND2 . ASN A 1 212 ? 1.625   -16.063 12.016 1.00 50.12  ? 212 ASN A ND2 1 
ATOM   1655 O OXT . ASN A 1 212 ? 4.797   -14.931 7.801  1.00 55.25  ? 212 ASN A OXT 1 
HETATM 1656 C C1  . E64 B 2 .   ? 2.815   14.456  16.446 0.76 31.23  ? 301 E64 A C1  1 
HETATM 1657 O O1  . E64 B 2 .   ? 2.438   15.169  15.508 0.76 28.91  ? 301 E64 A O1  1 
HETATM 1658 O O2  . E64 B 2 .   ? 3.781   14.730  17.232 0.76 25.16  ? 301 E64 A O2  1 
HETATM 1659 C C2  . E64 B 2 .   ? 2.088   13.128  16.703 0.76 23.56  ? 301 E64 A C2  1 
HETATM 1660 C C3  . E64 B 2 .   ? 0.770   13.298  17.464 0.76 33.13  ? 301 E64 A C3  1 
HETATM 1661 O O3  . E64 B 2 .   ? 0.766   14.523  18.175 0.76 31.24  ? 301 E64 A O3  1 
HETATM 1662 C C4  . E64 B 2 .   ? 0.424   12.063  18.321 0.76 28.27  ? 301 E64 A C4  1 
HETATM 1663 O O4  . E64 B 2 .   ? 0.295   10.963  17.798 0.76 22.60  ? 301 E64 A O4  1 
HETATM 1664 N N1  . E64 B 2 .   ? 0.272   12.260  19.644 0.76 32.47  ? 301 E64 A N1  1 
HETATM 1665 C C6  . E64 B 2 .   ? -0.053  11.175  20.557 0.76 35.12  ? 301 E64 A C6  1 
HETATM 1666 C C7  . E64 B 2 .   ? 1.057   10.969  21.579 0.76 26.23  ? 301 E64 A C7  1 
HETATM 1667 C C8  . E64 B 2 .   ? 2.125   9.973   21.124 0.76 26.06  ? 301 E64 A C8  1 
HETATM 1668 C C9  . E64 B 2 .   ? 2.549   9.118   22.315 0.76 28.46  ? 301 E64 A C9  1 
HETATM 1669 C C10 . E64 B 2 .   ? 1.665   9.100   19.951 0.76 20.78  ? 301 E64 A C10 1 
HETATM 1670 C C11 . E64 B 2 .   ? -1.386  11.442  21.271 0.76 37.07  ? 301 E64 A C11 1 
HETATM 1671 O O5  . E64 B 2 .   ? -1.694  12.573  21.630 0.76 36.34  ? 301 E64 A O5  1 
HETATM 1672 N N2  . E64 B 2 .   ? -2.146  10.349  21.453 0.76 26.05  ? 301 E64 A N2  1 
HETATM 1673 C C12 . E64 B 2 .   ? -3.438  10.332  22.101 0.76 25.15  ? 301 E64 A C12 1 
HETATM 1674 C C13 . E64 B 2 .   ? -4.606  10.467  21.137 0.76 24.60  ? 301 E64 A C13 1 
HETATM 1675 C C14 . E64 B 2 .   ? -4.716  11.855  20.528 0.76 27.99  ? 301 E64 A C14 1 
HETATM 1676 C C15 . E64 B 2 .   ? -5.101  12.898  21.570 0.76 34.31  ? 301 E64 A C15 1 
HETATM 1677 N N3  . E64 B 2 .   ? -6.498  12.804  21.945 0.76 28.24  ? 301 E64 A N3  1 
HETATM 1678 C C16 . E64 B 2 .   ? -7.500  13.201  21.161 0.76 31.69  ? 301 E64 A C16 1 
HETATM 1679 N N4  . E64 B 2 .   ? -7.298  13.726  19.967 0.76 37.78  ? 301 E64 A N4  1 
HETATM 1680 N N5  . E64 B 2 .   ? -8.759  13.077  21.586 0.76 26.46  ? 301 E64 A N5  1 
HETATM 1681 O O   . HOH C 3 .   ? 5.104   3.357   20.143 1.00 13.94  ? 401 HOH A O   1 
HETATM 1682 O O   . HOH C 3 .   ? 6.621   -0.792  25.158 1.00 11.30  ? 402 HOH A O   1 
HETATM 1683 O O   . HOH C 3 .   ? 24.868  3.145   11.014 1.00 13.14  ? 403 HOH A O   1 
HETATM 1684 O O   . HOH C 3 .   ? 22.177  16.642  23.224 1.00 18.14  ? 404 HOH A O   1 
HETATM 1685 O O   . HOH C 3 .   ? 7.534   -9.290  14.792 1.00 13.53  ? 405 HOH A O   1 
HETATM 1686 O O   . HOH C 3 .   ? 8.909   3.988   23.373 1.00 14.85  ? 406 HOH A O   1 
HETATM 1687 O O   . HOH C 3 .   ? 11.085  0.598   7.465  1.00 14.20  ? 407 HOH A O   1 
HETATM 1688 O O   . HOH C 3 .   ? -0.085  7.544   2.710  1.00 12.10  ? 408 HOH A O   1 
HETATM 1689 O O   . HOH C 3 .   ? 5.766   7.974   -1.630 1.00 18.44  ? 409 HOH A O   1 
HETATM 1690 O O   . HOH C 3 .   ? 11.974  17.321  23.755 1.00 19.68  ? 410 HOH A O   1 
HETATM 1691 O O   . HOH C 3 .   ? 5.193   16.441  14.922 1.00 14.71  ? 411 HOH A O   1 
HETATM 1692 O O   . HOH C 3 .   ? 1.385   17.724  5.199  1.00 12.37  ? 412 HOH A O   1 
# 
