data_9NAX
# 
_entry.id   9NAX 
# 
_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   9NAX         pdb_00009nax 10.2210/pdb9nax/pdb 
WWPDB D_1000292944 ?            ?                   
# 
_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                        9NAX 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'MicroED structure of the same protein in apo-form'                       9NAG unspecified 
PDB 'MicroED structure of the same protein complexed with a different ligand' 9N9D unspecified 
PDB 'MicroED structure of same protein co-crystallized with E-64'             9NAE unspecified 
PDB 'MicroED structure of the same protein complexed with a different ligand' 9NAO unspecified 
PDB 'MicroED structure of the same protein soaked with pure E-64 solution'    9NAR unspecified 
PDB 'XRD structure of the same protein complexed with a different ligand'     9NAT 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.W.'  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 syn 'N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE' 360.429   1  ?        ? ? ? 
3 water       nat water                                                               18.015    17 ?        ? ? ? 
# 
_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 2   HOH HOH A . 
C 3 HOH 2  402 1   HOH HOH A . 
C 3 HOH 3  403 6   HOH HOH A . 
C 3 HOH 4  404 8   HOH HOH A . 
C 3 HOH 5  405 3   HOH HOH A . 
C 3 HOH 6  406 4   HOH HOH A . 
C 3 HOH 7  407 13  HOH HOH A . 
C 3 HOH 8  408 17  HOH HOH A . 
C 3 HOH 9  409 14  HOH HOH A . 
C 3 HOH 10 410 10  HOH HOH A . 
C 3 HOH 11 411 7   HOH HOH A . 
C 3 HOH 12 412 15  HOH HOH A . 
C 3 HOH 13 413 12  HOH HOH A . 
C 3 HOH 14 414 16  HOH HOH A . 
C 3 HOH 15 415 9   HOH HOH A . 
C 3 HOH 16 416 5   HOH HOH A . 
C 3 HOH 17 417 11  HOH HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       PHENIX 1.20.1_4487 ? 1 
'data scaling'   XSCALE .           ? 2 
'data reduction' XDS    .           ? 3 
phasing          PHASER .           ? 4 
# 
_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                     9NAX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.850 
_cell.length_a_esd                 ? 
_cell.length_b                     48.630 
_cell.length_b_esd                 ? 
_cell.length_c                     99.870 
_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                         9NAX 
_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                   9NAX 
_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                                 9NAX 
_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                            2.30 
_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                     8304 
_refine.ls_number_reflns_R_free                  832 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    87.03 
_refine.ls_percent_reflns_R_free                 10.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1957 
_refine.ls_R_factor_R_free                       0.2475 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1899 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       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                 24.17 
_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                            0.29 
_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' ? 0.007 ? 1737 ? f_bond_d           ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.964 ? 2360 ? f_angle_d          ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 7.370 ? 252  ? f_dihedral_angle_d ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.060 ? 236  ? f_chiral_restr     ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.011 ? 309  ? 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.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' 2.30 2.44  . . 134 1203 87.00 . . . . 0.2447 . . . . . . . . . . . 0.3251 
'ELECTRON CRYSTALLOGRAPHY' 2.44 2.63  . . 136 1226 87.00 . . . . 0.2507 . . . . . . . . . . . 0.2920 
'ELECTRON CRYSTALLOGRAPHY' 2.63 2.90  . . 138 1236 88.00 . . . . 0.2221 . . . . . . . . . . . 0.2991 
'ELECTRON CRYSTALLOGRAPHY' 2.90 3.32  . . 138 1240 87.00 . . . . 0.2082 . . . . . . . . . . . 0.2876 
'ELECTRON CRYSTALLOGRAPHY' 3.32 4.18  . . 140 1256 87.00 . . . . 0.1505 . . . . . . . . . . . 0.2199 
'ELECTRON CRYSTALLOGRAPHY' 4.18 49.93 . . 146 1311 86.00 . . . . 0.1669 . . . . . . . . . . . 0.1885 
# 
_struct.entry_id                     9NAX 
_struct.title                        
'MicroED structure of the papain-E-64 complex from microcrystals soaked with crude biosynthetic reaction mixture' 
_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        9NAX 
_struct_keywords.text            'Inhibitor, Complex, Protease, MicroED, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PAPA1_CARPA 
_struct_ref.pdbx_db_accession          P00784 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGI
HYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHA
VAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
;
_struct_ref.pdbx_align_begin           134 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9NAX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 212 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00784 
_struct_ref_seq.db_align_beg                  134 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  345 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       212 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 SER A 24  ? GLY A 43  ? SER A 24  GLY A 43  1 ? 20 
HELX_P HELX_P2 AA2 SER A 49  ? ASP A 57  ? SER A 49  ASP A 57  1 ? 9  
HELX_P HELX_P3 AA3 TYR A 61  ? GLY A 65  ? TYR A 61  GLY A 65  5 ? 5  
HELX_P HELX_P4 AA4 TYR A 67  ? TYR A 78  ? TYR A 67  TYR A 78  1 ? 12 
HELX_P HELX_P5 AA5 SER A 97  ? GLY A 101 ? SER A 97  GLY A 101 5 ? 5  
HELX_P HELX_P6 AA6 ASN A 117 ? GLN A 128 ? ASN A 117 GLN A 128 1 ? 12 
HELX_P HELX_P7 AA7 GLY A 138 ? LEU A 143 ? GLY A 138 LEU A 143 1 ? 6  
HELX_P HELX_P8 AA8 GLY A 198 ? LEU A 202 ? GLY A 198 LEU A 202 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 22  SG ? ? ? 1_555 A CYS 63  SG ? ? A CYS 22  A CYS 63  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf2 disulf ?    ? A CYS 56  SG ? ? ? 1_555 A CYS 95  SG ? ? A CYS 56  A CYS 95  1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf3 disulf ?    ? A CYS 153 SG ? ? ? 1_555 A CYS 200 SG ? ? A CYS 153 A CYS 200 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
covale1 covale none ? A CYS 25  SG ? ? ? 1_555 B E64 .   C2 ? ? A CYS 25  A E64 301 1_555 ? ? ? ? ? ? ? 1.807 ? ? 
# 
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       2.96 
# 
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 ? TYR A 166 ? HIS A 159 TYR A 166 
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 ? TYR A 166 ? HIS A 159 TYR A 166 
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                   9NAX 
_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 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 78  ? ? -108.86 -69.63 
2 1 ASP A 158 ? ? -153.10 7.54   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9NAX 
_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                    9NAX 
_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                  2.3 
_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                 CELL 
_em_entity_assembly.name                 'Papain-E64-C 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                        9NAX 
_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_vitrification.entry_id              9NAX 
_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                9NAX 
_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              41.85 
_em_3d_crystal_entity.length_b              48.63 
_em_3d_crystal_entity.length_c              99.87 
_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    87.6 
_em_diffraction_shell.high_resolution           2.3 
_em_diffraction_shell.id                        1 
_em_diffraction_shell.low_resolution            2.4 
_em_diffraction_shell.multiplicity              8.3 
_em_diffraction_shell.num_structure_factors     958 
_em_diffraction_shell.phase_residual            30.3 
# 
_em_diffraction_stats.details                          ? 
_em_diffraction_stats.fourier_space_coverage           87.0 
_em_diffraction_stats.high_resolution                  2.3 
_em_diffraction_stats.id                               1 
_em_diffraction_stats.image_processing_id              1 
_em_diffraction_stats.num_intensities_measured         69072 
_em_diffraction_stats.num_structure_factors            8337 
_em_diffraction_stats.overall_phase_error              ? 
_em_diffraction_stats.overall_phase_residual           ? 
_em_diffraction_stats.phase_error_rejection_criteria   NULL 
_em_diffraction_stats.r_merge                          28.0 
_em_diffraction_stats.r_sym                            ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          3649 
_em_entity_assembly_naturalsource.organism             'Carica papaya' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         0.045 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'DIRECT ELECTRON APOLLO (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'IMAGE ACQUISITION'             ? 1  ? ? 1 ? ? 
MASKING                         ? 2  ? ? ? ? ? 
'CTF CORRECTION'                ? 3  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 4  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 5  ? ? ? ? ? 
'MODEL FITTING'                 ? 6  ? 1 ? ? ? 
OTHER                           ? 7  ? ? ? ? ? 
'MOLECULAR REPLACEMENT'         ? 8  1 ? ? ? ? 
'LATTICE DISTORTION CORRECTION' ? 9  1 ? ? ? ? 
'SYMMETRY DETERMINATION'        ? 10 1 ? ? ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 11 1 ? ? ? ? 
RECONSTRUCTION                  ? 12 1 ? ? ? ? 
'MODEL REFINEMENT'              ? 13 ? 1 ? ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_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 
'Department of Energy (DOE, United States)'        'United States' DE-FC02-02ER63421 2 
'Howard Hughes Medical Institute (HHMI)'           'United States' HHMI-EPI          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 
# 
_atom_sites.entry_id                    9NAX 
_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]   0.023895 
_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]   0.020563 
_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]   0.010013 
_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   ? 22.129  38.213 20.363 1.00 21.37 ? 1   ILE A N   1 
ATOM   2    C CA  . ILE A 1 1   ? 21.941  39.252 19.354 1.00 19.16 ? 1   ILE A CA  1 
ATOM   3    C C   . ILE A 1 1   ? 23.238  40.045 19.158 1.00 21.85 ? 1   ILE A C   1 
ATOM   4    O O   . ILE A 1 1   ? 24.055  40.145 20.072 1.00 22.23 ? 1   ILE A O   1 
ATOM   5    C CB  . ILE A 1 1   ? 20.775  40.171 19.729 1.00 19.77 ? 1   ILE A CB  1 
ATOM   6    C CG1 . ILE A 1 1   ? 21.115  40.993 20.970 1.00 16.85 ? 1   ILE A CG1 1 
ATOM   7    C CG2 . ILE A 1 1   ? 19.528  39.345 19.989 1.00 22.22 ? 1   ILE A CG2 1 
ATOM   8    C CD1 . ILE A 1 1   ? 19.977  41.886 21.412 1.00 20.96 ? 1   ILE A CD1 1 
ATOM   9    N N   . PRO A 1 2   ? 23.435  40.611 17.972 1.00 28.79 ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 2   ? 24.739  41.196 17.644 1.00 27.09 ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 2   ? 24.878  42.595 18.228 1.00 27.65 ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 2   ? 23.920  43.212 18.701 1.00 25.25 ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 2   ? 24.741  41.235 16.112 1.00 20.62 ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 2   ? 23.298  41.360 15.753 1.00 28.39 ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 2   ? 22.519  40.612 16.814 1.00 20.92 ? 2   PRO A CD  1 
ATOM   16   N N   . GLU A 1 3   ? 26.116  43.087 18.195 1.00 23.16 ? 3   GLU A N   1 
ATOM   17   C CA  . GLU A 1 3   ? 26.389  44.393 18.774 1.00 29.28 ? 3   GLU A CA  1 
ATOM   18   C C   . GLU A 1 3   ? 25.787  45.509 17.930 1.00 27.69 ? 3   GLU A C   1 
ATOM   19   O O   . GLU A 1 3   ? 25.450  46.575 18.458 1.00 24.51 ? 3   GLU A O   1 
ATOM   20   C CB  . GLU A 1 3   ? 27.894  44.572 18.952 1.00 21.33 ? 3   GLU A CB  1 
ATOM   21   C CG  . GLU A 1 3   ? 28.331  44.212 20.372 1.00 36.30 ? 3   GLU A CG  1 
ATOM   22   C CD  . GLU A 1 3   ? 29.420  45.119 20.920 1.00 59.99 ? 3   GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 3   ? 30.607  44.869 20.613 1.00 62.09 ? 3   GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 3   ? 29.088  46.084 21.652 1.00 46.22 ? 3   GLU A OE2 1 
ATOM   25   N N   . TYR A 1 4   ? 25.608  45.270 16.634 1.00 19.83 ? 4   TYR A N   1 
ATOM   26   C CA  . TYR A 1 4   ? 25.033  46.257 15.738 1.00 20.72 ? 4   TYR A CA  1 
ATOM   27   C C   . TYR A 1 4   ? 23.887  45.642 14.959 1.00 24.02 ? 4   TYR A C   1 
ATOM   28   O O   . TYR A 1 4   ? 23.966  44.497 14.502 1.00 23.43 ? 4   TYR A O   1 
ATOM   29   C CB  . TYR A 1 4   ? 26.070  46.788 14.745 1.00 22.40 ? 4   TYR A CB  1 
ATOM   30   C CG  . TYR A 1 4   ? 27.051  47.726 15.381 1.00 25.98 ? 4   TYR A CG  1 
ATOM   31   C CD1 . TYR A 1 4   ? 26.772  49.084 15.478 1.00 27.67 ? 4   TYR A CD1 1 
ATOM   32   C CD2 . TYR A 1 4   ? 28.269  47.264 15.866 1.00 25.22 ? 4   TYR A CD2 1 
ATOM   33   C CE1 . TYR A 1 4   ? 27.666  49.951 16.063 1.00 23.37 ? 4   TYR A CE1 1 
ATOM   34   C CE2 . TYR A 1 4   ? 29.175  48.129 16.453 1.00 25.28 ? 4   TYR A CE2 1 
ATOM   35   C CZ  . TYR A 1 4   ? 28.867  49.467 16.538 1.00 24.18 ? 4   TYR A CZ  1 
ATOM   36   O OH  . TYR A 1 4   ? 29.746  50.337 17.121 1.00 30.64 ? 4   TYR A OH  1 
ATOM   37   N N   . VAL A 1 5   ? 22.816  46.403 14.832 1.00 18.93 ? 5   VAL A N   1 
ATOM   38   C CA  . VAL A 1 5   ? 21.720  46.072 13.940 1.00 17.19 ? 5   VAL A CA  1 
ATOM   39   C C   . VAL A 1 5   ? 21.405  47.324 13.147 1.00 20.42 ? 5   VAL A C   1 
ATOM   40   O O   . VAL A 1 5   ? 21.488  48.439 13.674 1.00 21.97 ? 5   VAL A O   1 
ATOM   41   C CB  . VAL A 1 5   ? 20.477  45.550 14.694 1.00 30.81 ? 5   VAL A CB  1 
ATOM   42   C CG1 . VAL A 1 5   ? 19.279  45.443 13.749 1.00 19.34 ? 5   VAL A CG1 1 
ATOM   43   C CG2 . VAL A 1 5   ? 20.785  44.173 15.299 1.00 24.33 ? 5   VAL A CG2 1 
ATOM   44   N N   . ASP A 1 6   ? 21.157  47.152 11.857 1.00 17.29 ? 6   ASP A N   1 
ATOM   45   C CA  . ASP A 1 6   ? 20.761  48.278 11.027 1.00 18.26 ? 6   ASP A CA  1 
ATOM   46   C C   . ASP A 1 6   ? 19.940  47.677 9.892  1.00 21.31 ? 6   ASP A C   1 
ATOM   47   O O   . ASP A 1 6   ? 20.501  47.141 8.931  1.00 24.24 ? 6   ASP A O   1 
ATOM   48   C CB  . ASP A 1 6   ? 21.973  49.055 10.529 1.00 17.40 ? 6   ASP A CB  1 
ATOM   49   C CG  . ASP A 1 6   ? 21.595  50.326 9.790  1.00 24.55 ? 6   ASP A CG  1 
ATOM   50   O OD1 . ASP A 1 6   ? 20.422  50.460 9.373  1.00 22.81 ? 6   ASP A OD1 1 
ATOM   51   O OD2 . ASP A 1 6   ? 22.471  51.209 9.652  1.00 24.71 ? 6   ASP A OD2 1 
ATOM   52   N N   . TRP A 1 7   ? 18.617  47.690 10.057 1.00 17.62 ? 7   TRP A N   1 
ATOM   53   C CA  . TRP A 1 7   ? 17.742  47.087 9.064  1.00 13.88 ? 7   TRP A CA  1 
ATOM   54   C C   . TRP A 1 7   ? 17.800  47.796 7.720  1.00 19.20 ? 7   TRP A C   1 
ATOM   55   O O   . TRP A 1 7   ? 17.365  47.223 6.715  1.00 22.24 ? 7   TRP A O   1 
ATOM   56   C CB  . TRP A 1 7   ? 16.325  47.049 9.615  1.00 13.85 ? 7   TRP A CB  1 
ATOM   57   C CG  . TRP A 1 7   ? 16.211  45.928 10.582 1.00 18.89 ? 7   TRP A CG  1 
ATOM   58   C CD1 . TRP A 1 7   ? 16.106  46.024 11.943 1.00 17.81 ? 7   TRP A CD1 1 
ATOM   59   C CD2 . TRP A 1 7   ? 16.207  44.528 10.270 1.00 20.88 ? 7   TRP A CD2 1 
ATOM   60   N NE1 . TRP A 1 7   ? 16.036  44.759 12.499 1.00 24.99 ? 7   TRP A NE1 1 
ATOM   61   C CE2 . TRP A 1 7   ? 16.099  43.827 11.494 1.00 24.76 ? 7   TRP A CE2 1 
ATOM   62   C CE3 . TRP A 1 7   ? 16.286  43.799 9.077  1.00 19.14 ? 7   TRP A CE3 1 
ATOM   63   C CZ2 . TRP A 1 7   ? 16.074  42.434 11.557 1.00 14.63 ? 7   TRP A CZ2 1 
ATOM   64   C CZ3 . TRP A 1 7   ? 16.251  42.413 9.141  1.00 19.15 ? 7   TRP A CZ3 1 
ATOM   65   C CH2 . TRP A 1 7   ? 16.146  41.747 10.375 1.00 20.43 ? 7   TRP A CH2 1 
ATOM   66   N N   . ARG A 1 8   ? 18.313  49.029 7.674  1.00 19.44 ? 8   ARG A N   1 
ATOM   67   C CA  . ARG A 1 8   ? 18.505  49.683 6.384  1.00 19.86 ? 8   ARG A CA  1 
ATOM   68   C C   . ARG A 1 8   ? 19.506  48.911 5.541  1.00 18.93 ? 8   ARG A C   1 
ATOM   69   O O   . ARG A 1 8   ? 19.393  48.855 4.313  1.00 23.52 ? 8   ARG A O   1 
ATOM   70   C CB  . ARG A 1 8   ? 18.999  51.108 6.595  1.00 19.76 ? 8   ARG A CB  1 
ATOM   71   C CG  . ARG A 1 8   ? 18.068  51.962 7.403  1.00 20.05 ? 8   ARG A CG  1 
ATOM   72   C CD  . ARG A 1 8   ? 18.717  53.290 7.638  1.00 18.66 ? 8   ARG A CD  1 
ATOM   73   N NE  . ARG A 1 8   ? 19.903  53.164 8.476  1.00 22.30 ? 8   ARG A NE  1 
ATOM   74   C CZ  . ARG A 1 8   ? 20.620  54.197 8.892  1.00 22.58 ? 8   ARG A CZ  1 
ATOM   75   N NH1 . ARG A 1 8   ? 20.298  55.435 8.553  1.00 19.13 ? 8   ARG A NH1 1 
ATOM   76   N NH2 . ARG A 1 8   ? 21.681  53.984 9.666  1.00 19.66 ? 8   ARG A NH2 1 
ATOM   77   N N   . GLN A 1 9   ? 20.532  48.368 6.192  1.00 23.28 ? 9   GLN A N   1 
ATOM   78   C CA  . GLN A 1 9   ? 21.580  47.610 5.530  1.00 20.76 ? 9   GLN A CA  1 
ATOM   79   C C   . GLN A 1 9   ? 21.089  46.247 5.074  1.00 21.32 ? 9   GLN A C   1 
ATOM   80   O O   . GLN A 1 9   ? 21.665  45.665 4.151  1.00 24.71 ? 9   GLN A O   1 
ATOM   81   C CB  . GLN A 1 9   ? 22.773  47.530 6.474  1.00 26.40 ? 9   GLN A CB  1 
ATOM   82   C CG  . GLN A 1 9   ? 23.309  48.928 6.739  1.00 26.98 ? 9   GLN A CG  1 
ATOM   83   C CD  . GLN A 1 9   ? 24.448  48.973 7.727  1.00 45.04 ? 9   GLN A CD  1 
ATOM   84   O OE1 . GLN A 1 9   ? 25.257  48.053 7.811  1.00 38.66 ? 9   GLN A OE1 1 
ATOM   85   N NE2 . GLN A 1 9   ? 24.500  50.054 8.511  1.00 49.34 ? 9   GLN A NE2 1 
ATOM   86   N N   . LYS A 1 10  ? 20.045  45.729 5.708  1.00 21.62 ? 10  LYS A N   1 
ATOM   87   C CA  . LYS A 1 10  ? 19.410  44.494 5.289  1.00 27.72 ? 10  LYS A CA  1 
ATOM   88   C C   . LYS A 1 10  ? 18.342  44.738 4.239  1.00 28.61 ? 10  LYS A C   1 
ATOM   89   O O   . LYS A 1 10  ? 17.612  43.806 3.886  1.00 28.29 ? 10  LYS A O   1 
ATOM   90   C CB  . LYS A 1 10  ? 18.801  43.776 6.498  1.00 25.47 ? 10  LYS A CB  1 
ATOM   91   C CG  . LYS A 1 10  ? 19.826  43.192 7.464  1.00 24.60 ? 10  LYS A CG  1 
ATOM   92   C CD  . LYS A 1 10  ? 20.601  42.082 6.808  1.00 27.19 ? 10  LYS A CD  1 
ATOM   93   C CE  . LYS A 1 10  ? 21.817  41.704 7.622  1.00 34.19 ? 10  LYS A CE  1 
ATOM   94   N NZ  . LYS A 1 10  ? 21.416  40.936 8.830  1.00 41.15 ? 10  LYS A NZ  1 
ATOM   95   N N   . GLY A 1 11  ? 18.226  45.971 3.748  1.00 23.72 ? 11  GLY A N   1 
ATOM   96   C CA  . GLY A 1 11  ? 17.220  46.286 2.748  1.00 20.85 ? 11  GLY A CA  1 
ATOM   97   C C   . GLY A 1 11  ? 15.799  46.137 3.242  1.00 23.79 ? 11  GLY A C   1 
ATOM   98   O O   . GLY A 1 11  ? 14.912  45.797 2.455  1.00 27.15 ? 11  GLY A O   1 
ATOM   99   N N   . ALA A 1 12  ? 15.556  46.393 4.528  1.00 19.59 ? 12  ALA A N   1 
ATOM   100  C CA  . ALA A 1 12  ? 14.257  46.167 5.155  1.00 20.89 ? 12  ALA A CA  1 
ATOM   101  C C   . ALA A 1 12  ? 13.570  47.468 5.543  1.00 16.93 ? 12  ALA A C   1 
ATOM   102  O O   . ALA A 1 12  ? 12.543  47.439 6.230  1.00 16.75 ? 12  ALA A O   1 
ATOM   103  C CB  . ALA A 1 12  ? 14.400  45.264 6.388  1.00 16.46 ? 12  ALA A CB  1 
ATOM   104  N N   . VAL A 1 13  ? 14.089  48.606 5.086  1.00 17.33 ? 13  VAL A N   1 
ATOM   105  C CA  . VAL A 1 13  ? 13.584  49.919 5.462  1.00 16.85 ? 13  VAL A CA  1 
ATOM   106  C C   . VAL A 1 13  ? 13.352  50.728 4.195  1.00 16.46 ? 13  VAL A C   1 
ATOM   107  O O   . VAL A 1 13  ? 14.252  50.856 3.359  1.00 16.66 ? 13  VAL A O   1 
ATOM   108  C CB  . VAL A 1 13  ? 14.550  50.659 6.404  1.00 21.59 ? 13  VAL A CB  1 
ATOM   109  C CG1 . VAL A 1 13  ? 13.914  51.964 6.886  1.00 21.05 ? 13  VAL A CG1 1 
ATOM   110  C CG2 . VAL A 1 13  ? 14.940  49.771 7.582  1.00 22.00 ? 13  VAL A CG2 1 
ATOM   111  N N   . THR A 1 14  ? 12.153  51.273 4.058  1.00 17.42 ? 14  THR A N   1 
ATOM   112  C CA  . THR A 1 14  ? 11.824  52.095 2.907  1.00 20.61 ? 14  THR A CA  1 
ATOM   113  C C   . THR A 1 14  ? 12.330  53.516 3.137  1.00 16.79 ? 14  THR A C   1 
ATOM   114  O O   . THR A 1 14  ? 12.835  53.843 4.213  1.00 17.11 ? 14  THR A O   1 
ATOM   115  C CB  . THR A 1 14  ? 10.312  52.053 2.676  1.00 19.73 ? 14  THR A CB  1 
ATOM   116  O OG1 . THR A 1 14  ? 9.635   52.766 3.720  1.00 19.92 ? 14  THR A OG1 1 
ATOM   117  C CG2 . THR A 1 14  ? 9.819   50.621 2.652  1.00 25.09 ? 14  THR A CG2 1 
ATOM   118  N N   . PRO A 1 15  ? 12.275  54.373 2.117  1.00 17.43 ? 15  PRO A N   1 
ATOM   119  C CA  . PRO A 1 15  ? 12.750  55.748 2.300  1.00 13.51 ? 15  PRO A CA  1 
ATOM   120  C C   . PRO A 1 15  ? 12.028  56.451 3.438  1.00 13.57 ? 15  PRO A C   1 
ATOM   121  O O   . PRO A 1 15  ? 10.871  56.163 3.751  1.00 19.34 ? 15  PRO A O   1 
ATOM   122  C CB  . PRO A 1 15  ? 12.453  56.406 0.948  1.00 18.78 ? 15  PRO A CB  1 
ATOM   123  C CG  . PRO A 1 15  ? 12.564  55.278 -0.030 1.00 12.63 ? 15  PRO A CG  1 
ATOM   124  C CD  . PRO A 1 15  ? 11.994  54.082 0.692  1.00 17.57 ? 15  PRO A CD  1 
ATOM   125  N N   . VAL A 1 16  ? 12.720  57.416 4.034  1.00 17.22 ? 16  VAL A N   1 
ATOM   126  C CA  . VAL A 1 16  ? 12.125  58.202 5.106  1.00 19.20 ? 16  VAL A CA  1 
ATOM   127  C C   . VAL A 1 16  ? 10.936  58.988 4.582  1.00 17.58 ? 16  VAL A C   1 
ATOM   128  O O   . VAL A 1 16  ? 10.971  59.564 3.485  1.00 15.78 ? 16  VAL A O   1 
ATOM   129  C CB  . VAL A 1 16  ? 13.178  59.146 5.702  1.00 14.43 ? 16  VAL A CB  1 
ATOM   130  C CG1 . VAL A 1 16  ? 12.508  60.274 6.529  1.00 14.90 ? 16  VAL A CG1 1 
ATOM   131  C CG2 . VAL A 1 16  ? 14.176  58.344 6.528  1.00 14.34 ? 16  VAL A CG2 1 
ATOM   132  N N   . LYS A 1 17  ? 9.869   59.013 5.369  1.00 19.20 ? 17  LYS A N   1 
ATOM   133  C CA  . LYS A 1 17  ? 8.649   59.698 4.988  1.00 21.00 ? 17  LYS A CA  1 
ATOM   134  C C   . LYS A 1 17  ? 8.500   60.953 5.830  1.00 20.19 ? 17  LYS A C   1 
ATOM   135  O O   . LYS A 1 17  ? 9.192   61.153 6.828  1.00 22.78 ? 17  LYS A O   1 
ATOM   136  C CB  . LYS A 1 17  ? 7.438   58.778 5.162  1.00 26.51 ? 17  LYS A CB  1 
ATOM   137  C CG  . LYS A 1 17  ? 7.606   57.438 4.479  1.00 28.19 ? 17  LYS A CG  1 
ATOM   138  C CD  . LYS A 1 17  ? 7.963   57.627 3.009  1.00 25.69 ? 17  LYS A CD  1 
ATOM   139  C CE  . LYS A 1 17  ? 7.843   56.320 2.237  1.00 23.61 ? 17  LYS A CE  1 
ATOM   140  N NZ  . LYS A 1 17  ? 8.634   55.242 2.873  1.00 24.89 ? 17  LYS A NZ  1 
ATOM   141  N N   . ASN A 1 18  ? 7.575   61.805 5.417  1.00 24.73 ? 18  ASN A N   1 
ATOM   142  C CA  . ASN A 1 18  ? 7.260   63.008 6.165  1.00 25.73 ? 18  ASN A CA  1 
ATOM   143  C C   . ASN A 1 18  ? 5.770   63.016 6.449  1.00 20.67 ? 18  ASN A C   1 
ATOM   144  O O   . ASN A 1 18  ? 4.959   63.089 5.521  1.00 21.89 ? 18  ASN A O   1 
ATOM   145  C CB  . ASN A 1 18  ? 7.685   64.253 5.387  1.00 19.44 ? 18  ASN A CB  1 
ATOM   146  C CG  . ASN A 1 18  ? 7.525   65.521 6.189  1.00 27.52 ? 18  ASN A CG  1 
ATOM   147  O OD1 . ASN A 1 18  ? 6.481   65.762 6.791  1.00 30.57 ? 18  ASN A OD1 1 
ATOM   148  N ND2 . ASN A 1 18  ? 8.573   66.334 6.221  1.00 32.28 ? 18  ASN A ND2 1 
ATOM   149  N N   . GLN A 1 19  ? 5.414   62.940 7.727  1.00 17.22 ? 19  GLN A N   1 
ATOM   150  C CA  . GLN A 1 19  ? 4.003   62.955 8.078  1.00 24.36 ? 19  GLN A CA  1 
ATOM   151  C C   . GLN A 1 19  ? 3.366   64.333 7.936  1.00 20.86 ? 19  GLN A C   1 
ATOM   152  O O   . GLN A 1 19  ? 2.137   64.422 7.863  1.00 27.06 ? 19  GLN A O   1 
ATOM   153  C CB  . GLN A 1 19  ? 3.834   62.441 9.502  1.00 19.30 ? 19  GLN A CB  1 
ATOM   154  C CG  . GLN A 1 19  ? 4.434   63.390 10.538 1.00 19.12 ? 19  GLN A CG  1 
ATOM   155  C CD  . GLN A 1 19  ? 4.396   62.817 11.931 1.00 16.33 ? 19  GLN A CD  1 
ATOM   156  O OE1 . GLN A 1 19  ? 5.265   62.035 12.325 1.00 22.60 ? 19  GLN A OE1 1 
ATOM   157  N NE2 . GLN A 1 19  ? 3.382   63.201 12.691 1.00 20.19 ? 19  GLN A NE2 1 
ATOM   158  N N   . GLY A 1 20  ? 4.153   65.398 7.858  1.00 17.68 ? 20  GLY A N   1 
ATOM   159  C CA  . GLY A 1 20  ? 3.507   66.691 7.767  1.00 14.91 ? 20  GLY A CA  1 
ATOM   160  C C   . GLY A 1 20  ? 2.899   67.104 9.097  1.00 20.82 ? 20  GLY A C   1 
ATOM   161  O O   . GLY A 1 20  ? 3.287   66.634 10.168 1.00 26.38 ? 20  GLY A O   1 
ATOM   162  N N   . SER A 1 21  ? 1.905   67.990 9.012  1.00 19.62 ? 21  SER A N   1 
ATOM   163  C CA  . SER A 1 21  ? 1.280   68.532 10.214 1.00 25.44 ? 21  SER A CA  1 
ATOM   164  C C   . SER A 1 21  ? 0.337   67.547 10.888 1.00 27.70 ? 21  SER A C   1 
ATOM   165  O O   . SER A 1 21  ? 0.047   67.709 12.079 1.00 28.89 ? 21  SER A O   1 
ATOM   166  C CB  . SER A 1 21  ? 0.498   69.800 9.872  1.00 21.95 ? 21  SER A CB  1 
ATOM   167  O OG  . SER A 1 21  ? -0.443  69.517 8.852  1.00 17.09 ? 21  SER A OG  1 
ATOM   168  N N   . CYS A 1 22  ? -0.112  66.522 10.168 1.00 22.75 ? 22  CYS A N   1 
ATOM   169  C CA  . CYS A 1 22  ? -1.075  65.563 10.695 1.00 25.95 ? 22  CYS A CA  1 
ATOM   170  C C   . CYS A 1 22  ? -0.441  64.740 11.814 1.00 24.13 ? 22  CYS A C   1 
ATOM   171  O O   . CYS A 1 22  ? 0.699   64.285 11.701 1.00 26.07 ? 22  CYS A O   1 
ATOM   172  C CB  . CYS A 1 22  ? -1.562  64.665 9.546  1.00 21.96 ? 22  CYS A CB  1 
ATOM   173  S SG  . CYS A 1 22  ? -2.658  63.242 9.921  1.00 33.73 ? 22  CYS A SG  1 
ATOM   174  N N   . GLY A 1 23  ? -1.184  64.542 12.900 1.00 15.67 ? 23  GLY A N   1 
ATOM   175  C CA  . GLY A 1 23  ? -0.671  63.715 13.974 1.00 22.79 ? 23  GLY A CA  1 
ATOM   176  C C   . GLY A 1 23  ? -0.790  62.235 13.677 1.00 20.16 ? 23  GLY A C   1 
ATOM   177  O O   . GLY A 1 23  ? -1.456  61.485 14.398 1.00 23.98 ? 23  GLY A O   1 
ATOM   178  N N   . SER A 1 24  ? -0.130  61.811 12.602 1.00 17.82 ? 24  SER A N   1 
ATOM   179  C CA  . SER A 1 24  ? -0.221  60.452 12.091 1.00 19.55 ? 24  SER A CA  1 
ATOM   180  C C   . SER A 1 24  ? 1.037   59.643 12.340 1.00 14.35 ? 24  SER A C   1 
ATOM   181  O O   . SER A 1 24  ? 1.275   58.664 11.633 1.00 22.96 ? 24  SER A O   1 
ATOM   182  C CB  . SER A 1 24  ? -0.513  60.483 10.596 1.00 23.55 ? 24  SER A CB  1 
ATOM   183  O OG  . SER A 1 24  ? 0.418   61.322 9.934  1.00 23.94 ? 24  SER A OG  1 
ATOM   184  N N   . CYS A 1 25  ? 1.856   60.036 13.315 1.00 18.65 ? 25  CYS A N   1 
ATOM   185  C CA  . CYS A 1 25  ? 3.100   59.314 13.557 1.00 19.91 ? 25  CYS A CA  1 
ATOM   186  C C   . CYS A 1 25  ? 2.833   57.854 13.897 1.00 15.14 ? 25  CYS A C   1 
ATOM   187  O O   . CYS A 1 25  ? 3.593   56.973 13.497 1.00 19.16 ? 25  CYS A O   1 
ATOM   188  C CB  . CYS A 1 25  ? 3.895   59.975 14.682 1.00 24.20 ? 25  CYS A CB  1 
ATOM   189  S SG  . CYS A 1 25  ? 3.008   60.072 16.254 1.00 27.19 ? 25  CYS A SG  1 
ATOM   190  N N   . TRP A 1 26  ? 1.759   57.582 14.637 1.00 14.35 ? 26  TRP A N   1 
ATOM   191  C CA  . TRP A 1 26  ? 1.435   56.211 15.021 1.00 20.17 ? 26  TRP A CA  1 
ATOM   192  C C   . TRP A 1 26  ? 1.275   55.306 13.796 1.00 16.42 ? 26  TRP A C   1 
ATOM   193  O O   . TRP A 1 26  ? 1.756   54.164 13.782 1.00 15.67 ? 26  TRP A O   1 
ATOM   194  C CB  . TRP A 1 26  ? 0.150   56.229 15.854 1.00 22.65 ? 26  TRP A CB  1 
ATOM   195  C CG  . TRP A 1 26  ? -0.997  56.904 15.136 1.00 16.50 ? 26  TRP A CG  1 
ATOM   196  C CD1 . TRP A 1 26  ? -1.278  58.239 15.097 1.00 18.49 ? 26  TRP A CD1 1 
ATOM   197  C CD2 . TRP A 1 26  ? -2.018  56.254 14.365 1.00 17.75 ? 26  TRP A CD2 1 
ATOM   198  N NE1 . TRP A 1 26  ? -2.400  58.462 14.332 1.00 19.77 ? 26  TRP A NE1 1 
ATOM   199  C CE2 . TRP A 1 26  ? -2.878  57.257 13.882 1.00 19.00 ? 26  TRP A CE2 1 
ATOM   200  C CE3 . TRP A 1 26  ? -2.288  54.917 14.042 1.00 14.48 ? 26  TRP A CE3 1 
ATOM   201  C CZ2 . TRP A 1 26  ? -3.988  56.969 13.086 1.00 23.54 ? 26  TRP A CZ2 1 
ATOM   202  C CZ3 . TRP A 1 26  ? -3.391  54.631 13.255 1.00 20.43 ? 26  TRP A CZ3 1 
ATOM   203  C CH2 . TRP A 1 26  ? -4.226  55.656 12.779 1.00 19.74 ? 26  TRP A CH2 1 
ATOM   204  N N   . ALA A 1 27  ? 0.713   55.845 12.713 1.00 18.35 ? 27  ALA A N   1 
ATOM   205  C CA  . ALA A 1 27  ? 0.566   55.072 11.487 1.00 18.48 ? 27  ALA A CA  1 
ATOM   206  C C   . ALA A 1 27  ? 1.883   54.919 10.746 1.00 17.65 ? 27  ALA A C   1 
ATOM   207  O O   . ALA A 1 27  ? 2.159   53.851 10.196 1.00 20.65 ? 27  ALA A O   1 
ATOM   208  C CB  . ALA A 1 27  ? -0.471  55.732 10.572 1.00 16.63 ? 27  ALA A CB  1 
ATOM   209  N N   . PHE A 1 28  ? 2.712   55.962 10.718 1.00 19.09 ? 28  PHE A N   1 
ATOM   210  C CA  . PHE A 1 28  ? 4.016   55.838 10.076 1.00 13.77 ? 28  PHE A CA  1 
ATOM   211  C C   . PHE A 1 28  ? 4.872   54.812 10.799 1.00 17.05 ? 28  PHE A C   1 
ATOM   212  O O   . PHE A 1 28  ? 5.542   53.983 10.171 1.00 17.65 ? 28  PHE A O   1 
ATOM   213  C CB  . PHE A 1 28  ? 4.704   57.197 10.035 1.00 18.14 ? 28  PHE A CB  1 
ATOM   214  C CG  . PHE A 1 28  ? 4.217   58.061 8.926  1.00 21.58 ? 28  PHE A CG  1 
ATOM   215  C CD1 . PHE A 1 28  ? 3.032   58.779 9.064  1.00 20.73 ? 28  PHE A CD1 1 
ATOM   216  C CD2 . PHE A 1 28  ? 4.899   58.114 7.725  1.00 15.19 ? 28  PHE A CD2 1 
ATOM   217  C CE1 . PHE A 1 28  ? 2.550   59.577 8.025  1.00 20.28 ? 28  PHE A CE1 1 
ATOM   218  C CE2 . PHE A 1 28  ? 4.420   58.912 6.678  1.00 25.38 ? 28  PHE A CE2 1 
ATOM   219  C CZ  . PHE A 1 28  ? 3.244   59.639 6.833  1.00 19.02 ? 28  PHE A CZ  1 
ATOM   220  N N   . SER A 1 29  ? 4.898   54.897 12.127 1.00 11.43 ? 29  SER A N   1 
ATOM   221  C CA  . SER A 1 29  ? 5.622   53.935 12.945 1.00 15.96 ? 29  SER A CA  1 
ATOM   222  C C   . SER A 1 29  ? 5.149   52.507 12.650 1.00 18.58 ? 29  SER A C   1 
ATOM   223  O O   . SER A 1 29  ? 5.960   51.607 12.341 1.00 18.98 ? 29  SER A O   1 
ATOM   224  C CB  . SER A 1 29  ? 5.430   54.312 14.409 1.00 10.91 ? 29  SER A CB  1 
ATOM   225  O OG  . SER A 1 29  ? 5.961   53.330 15.263 1.00 18.39 ? 29  SER A OG  1 
ATOM   226  N N   . ALA A 1 30  ? 3.824   52.295 12.681 1.00 14.50 ? 30  ALA A N   1 
ATOM   227  C CA  . ALA A 1 30  ? 3.289   50.972 12.384 1.00 17.29 ? 30  ALA A CA  1 
ATOM   228  C C   . ALA A 1 30  ? 3.719   50.509 10.995 1.00 19.33 ? 30  ALA A C   1 
ATOM   229  O O   . ALA A 1 30  ? 4.172   49.370 10.817 1.00 22.06 ? 30  ALA A O   1 
ATOM   230  C CB  . ALA A 1 30  ? 1.764   51.012 12.474 1.00 15.30 ? 30  ALA A CB  1 
ATOM   231  N N   . VAL A 1 31  ? 3.601   51.392 10.002 1.00 18.17 ? 31  VAL A N   1 
ATOM   232  C CA  . VAL A 1 31  ? 3.938   51.035 8.630  1.00 16.83 ? 31  VAL A CA  1 
ATOM   233  C C   . VAL A 1 31  ? 5.416   50.670 8.494  1.00 20.03 ? 31  VAL A C   1 
ATOM   234  O O   . VAL A 1 31  ? 5.780   49.781 7.714  1.00 19.81 ? 31  VAL A O   1 
ATOM   235  C CB  . VAL A 1 31  ? 3.534   52.177 7.689  1.00 22.54 ? 31  VAL A CB  1 
ATOM   236  C CG1 . VAL A 1 31  ? 4.219   52.021 6.363  1.00 23.65 ? 31  VAL A CG1 1 
ATOM   237  C CG2 . VAL A 1 31  ? 2.038   52.142 7.495  1.00 20.80 ? 31  VAL A CG2 1 
ATOM   238  N N   . VAL A 1 32  ? 6.301   51.393 9.182  1.00 17.15 ? 32  VAL A N   1 
ATOM   239  C CA  . VAL A 1 32  ? 7.711   51.017 9.121  1.00 15.90 ? 32  VAL A CA  1 
ATOM   240  C C   . VAL A 1 32  ? 7.873   49.577 9.573  1.00 17.25 ? 32  VAL A C   1 
ATOM   241  O O   . VAL A 1 32  ? 8.582   48.781 8.941  1.00 25.70 ? 32  VAL A O   1 
ATOM   242  C CB  . VAL A 1 32  ? 8.587   51.975 9.941  1.00 18.44 ? 32  VAL A CB  1 
ATOM   243  C CG1 . VAL A 1 32  ? 10.024  51.492 9.922  1.00 17.09 ? 32  VAL A CG1 1 
ATOM   244  C CG2 . VAL A 1 32  ? 8.512   53.366 9.353  1.00 19.59 ? 32  VAL A CG2 1 
ATOM   245  N N   . THR A 1 33  ? 7.179   49.205 10.654 1.00 24.55 ? 33  THR A N   1 
ATOM   246  C CA  . THR A 1 33  ? 7.341   47.834 11.139 1.00 20.85 ? 33  THR A CA  1 
ATOM   247  C C   . THR A 1 33  ? 6.714   46.809 10.191 1.00 16.75 ? 33  THR A C   1 
ATOM   248  O O   . THR A 1 33  ? 7.230   45.691 10.066 1.00 15.65 ? 33  THR A O   1 
ATOM   249  C CB  . THR A 1 33  ? 6.747   47.689 12.533 1.00 17.13 ? 33  THR A CB  1 
ATOM   250  O OG1 . THR A 1 33  ? 5.319   47.747 12.448 1.00 19.91 ? 33  THR A OG1 1 
ATOM   251  C CG2 . THR A 1 33  ? 7.226   48.822 13.391 1.00 17.53 ? 33  THR A CG2 1 
ATOM   252  N N   . ILE A 1 34  ? 5.637   47.175 9.485  1.00 15.70 ? 34  ILE A N   1 
ATOM   253  C CA  . ILE A 1 34  ? 5.034   46.232 8.533  1.00 23.01 ? 34  ILE A CA  1 
ATOM   254  C C   . ILE A 1 34  ? 5.926   46.039 7.318  1.00 18.21 ? 34  ILE A C   1 
ATOM   255  O O   . ILE A 1 34  ? 6.147   44.910 6.867  1.00 24.91 ? 34  ILE A O   1 
ATOM   256  C CB  . ILE A 1 34  ? 3.624   46.677 8.121  1.00 26.70 ? 34  ILE A CB  1 
ATOM   257  C CG1 . ILE A 1 34  ? 2.718   46.729 9.340  1.00 25.87 ? 34  ILE A CG1 1 
ATOM   258  C CG2 . ILE A 1 34  ? 3.056   45.739 7.059  1.00 29.10 ? 34  ILE A CG2 1 
ATOM   259  C CD1 . ILE A 1 34  ? 1.588   47.691 9.160  1.00 30.40 ? 34  ILE A CD1 1 
ATOM   260  N N   . GLU A 1 35  ? 6.405   47.140 6.738  1.00 25.46 ? 35  GLU A N   1 
ATOM   261  C CA  . GLU A 1 35  ? 7.349   47.062 5.628  1.00 24.21 ? 35  GLU A CA  1 
ATOM   262  C C   . GLU A 1 35  ? 8.549   46.205 6.009  1.00 24.26 ? 35  GLU A C   1 
ATOM   263  O O   . GLU A 1 35  ? 8.994   45.350 5.229  1.00 22.32 ? 35  GLU A O   1 
ATOM   264  C CB  . GLU A 1 35  ? 7.757   48.479 5.229  1.00 22.43 ? 35  GLU A CB  1 
ATOM   265  C CG  . GLU A 1 35  ? 6.570   49.202 4.650  1.00 27.71 ? 35  GLU A CG  1 
ATOM   266  C CD  . GLU A 1 35  ? 6.753   50.691 4.527  1.00 33.16 ? 35  GLU A CD  1 
ATOM   267  O OE1 . GLU A 1 35  ? 7.724   51.231 5.099  1.00 24.93 ? 35  GLU A OE1 1 
ATOM   268  O OE2 . GLU A 1 35  ? 5.917   51.320 3.834  1.00 33.58 ? 35  GLU A OE2 1 
ATOM   269  N N   . GLY A 1 36  ? 9.026   46.357 7.248  1.00 19.69 ? 36  GLY A N   1 
ATOM   270  C CA  . GLY A 1 36  ? 10.183  45.593 7.671  1.00 15.38 ? 36  GLY A CA  1 
ATOM   271  C C   . GLY A 1 36  ? 9.876   44.111 7.779  1.00 16.83 ? 36  GLY A C   1 
ATOM   272  O O   . GLY A 1 36  ? 10.630  43.277 7.269  1.00 18.88 ? 36  GLY A O   1 
ATOM   273  N N   . ILE A 1 37  ? 8.779   43.755 8.455  1.00 16.33 ? 37  ILE A N   1 
ATOM   274  C CA  . ILE A 1 37  ? 8.518   42.331 8.647  1.00 18.91 ? 37  ILE A CA  1 
ATOM   275  C C   . ILE A 1 37  ? 8.171   41.676 7.316  1.00 22.16 ? 37  ILE A C   1 
ATOM   276  O O   . ILE A 1 37  ? 8.480   40.502 7.106  1.00 20.92 ? 37  ILE A O   1 
ATOM   277  C CB  . ILE A 1 37  ? 7.418   42.084 9.704  1.00 15.04 ? 37  ILE A CB  1 
ATOM   278  C CG1 . ILE A 1 37  ? 7.468   40.645 10.205 1.00 16.28 ? 37  ILE A CG1 1 
ATOM   279  C CG2 . ILE A 1 37  ? 6.046   42.322 9.141  1.00 21.40 ? 37  ILE A CG2 1 
ATOM   280  C CD1 . ILE A 1 37  ? 8.770   40.266 10.818 1.00 22.98 ? 37  ILE A CD1 1 
ATOM   281  N N   . ILE A 1 38  ? 7.555   42.411 6.384  1.00 21.93 ? 38  ILE A N   1 
ATOM   282  C CA  . ILE A 1 38  ? 7.277   41.810 5.083  1.00 22.19 ? 38  ILE A CA  1 
ATOM   283  C C   . ILE A 1 38  ? 8.574   41.572 4.315  1.00 25.69 ? 38  ILE A C   1 
ATOM   284  O O   . ILE A 1 38  ? 8.731   40.547 3.646  1.00 30.31 ? 38  ILE A O   1 
ATOM   285  C CB  . ILE A 1 38  ? 6.281   42.662 4.279  1.00 22.80 ? 38  ILE A CB  1 
ATOM   286  C CG1 . ILE A 1 38  ? 4.913   42.664 4.973  1.00 28.84 ? 38  ILE A CG1 1 
ATOM   287  C CG2 . ILE A 1 38  ? 6.125   42.091 2.859  1.00 19.93 ? 38  ILE A CG2 1 
ATOM   288  C CD1 . ILE A 1 38  ? 4.330   41.272 5.249  1.00 27.33 ? 38  ILE A CD1 1 
ATOM   289  N N   . LYS A 1 39  ? 9.528   42.503 4.394  1.00 21.74 ? 39  LYS A N   1 
ATOM   290  C CA  . LYS A 1 39  ? 10.819  42.257 3.753  1.00 23.39 ? 39  LYS A CA  1 
ATOM   291  C C   . LYS A 1 39  ? 11.537  41.073 4.393  1.00 26.33 ? 39  LYS A C   1 
ATOM   292  O O   . LYS A 1 39  ? 12.079  40.207 3.694  1.00 25.23 ? 39  LYS A O   1 
ATOM   293  C CB  . LYS A 1 39  ? 11.700  43.496 3.831  1.00 22.72 ? 39  LYS A CB  1 
ATOM   294  C CG  . LYS A 1 39  ? 13.153  43.218 3.473  1.00 27.79 ? 39  LYS A CG  1 
ATOM   295  C CD  . LYS A 1 39  ? 13.340  42.855 2.015  1.00 26.50 ? 39  LYS A CD  1 
ATOM   296  C CE  . LYS A 1 39  ? 14.818  42.621 1.740  1.00 29.28 ? 39  LYS A CE  1 
ATOM   297  N NZ  . LYS A 1 39  ? 15.097  42.410 0.286  1.00 33.80 ? 39  LYS A NZ  1 
ATOM   298  N N   . ILE A 1 40  ? 11.545  41.025 5.724  1.00 20.98 ? 40  ILE A N   1 
ATOM   299  C CA  . ILE A 1 40  ? 12.210  39.951 6.454  1.00 22.30 ? 40  ILE A CA  1 
ATOM   300  C C   . ILE A 1 40  ? 11.608  38.593 6.094  1.00 21.05 ? 40  ILE A C   1 
ATOM   301  O O   . ILE A 1 40  ? 12.332  37.611 5.887  1.00 17.61 ? 40  ILE A O   1 
ATOM   302  C CB  . ILE A 1 40  ? 12.134  40.247 7.962  1.00 22.17 ? 40  ILE A CB  1 
ATOM   303  C CG1 . ILE A 1 40  ? 13.090  41.384 8.308  1.00 19.14 ? 40  ILE A CG1 1 
ATOM   304  C CG2 . ILE A 1 40  ? 12.461  39.011 8.809  1.00 27.20 ? 40  ILE A CG2 1 
ATOM   305  C CD1 . ILE A 1 40  ? 12.764  42.053 9.615  1.00 17.99 ? 40  ILE A CD1 1 
ATOM   306  N N   . ARG A 1 41  ? 10.282  38.517 5.991  1.00 24.89 ? 41  ARG A N   1 
ATOM   307  C CA  . ARG A 1 41  ? 9.632   37.236 5.743  1.00 27.76 ? 41  ARG A CA  1 
ATOM   308  C C   . ARG A 1 41  ? 9.591   36.861 4.262  1.00 28.59 ? 41  ARG A C   1 
ATOM   309  O O   . ARG A 1 41  ? 9.612   35.669 3.939  1.00 30.58 ? 41  ARG A O   1 
ATOM   310  C CB  . ARG A 1 41  ? 8.211   37.252 6.303  1.00 25.22 ? 41  ARG A CB  1 
ATOM   311  C CG  . ARG A 1 41  ? 8.115   37.310 7.820  1.00 27.84 ? 41  ARG A CG  1 
ATOM   312  C CD  . ARG A 1 41  ? 8.519   36.010 8.472  1.00 26.05 ? 41  ARG A CD  1 
ATOM   313  N NE  . ARG A 1 41  ? 8.435   36.135 9.921  1.00 27.64 ? 41  ARG A NE  1 
ATOM   314  C CZ  . ARG A 1 41  ? 9.457   36.400 10.721 1.00 25.89 ? 41  ARG A CZ  1 
ATOM   315  N NH1 . ARG A 1 41  ? 10.689  36.509 10.258 1.00 29.69 ? 41  ARG A NH1 1 
ATOM   316  N NH2 . ARG A 1 41  ? 9.232   36.575 12.020 1.00 28.73 ? 41  ARG A NH2 1 
ATOM   317  N N   . THR A 1 42  ? 9.526   37.832 3.346  1.00 27.27 ? 42  THR A N   1 
ATOM   318  C CA  . THR A 1 42  ? 9.307   37.519 1.941  1.00 25.33 ? 42  THR A CA  1 
ATOM   319  C C   . THR A 1 42  ? 10.451  37.902 1.020  1.00 27.50 ? 42  THR A C   1 
ATOM   320  O O   . THR A 1 42  ? 10.471  37.433 -0.123 1.00 33.03 ? 42  THR A O   1 
ATOM   321  C CB  . THR A 1 42  ? 8.033   38.208 1.413  1.00 27.35 ? 42  THR A CB  1 
ATOM   322  O OG1 . THR A 1 42  ? 8.290   39.603 1.185  1.00 31.23 ? 42  THR A OG1 1 
ATOM   323  C CG2 . THR A 1 42  ? 6.873   38.065 2.387  1.00 25.35 ? 42  THR A CG2 1 
ATOM   324  N N   . GLY A 1 43  ? 11.389  38.733 1.465  1.00 22.86 ? 43  GLY A N   1 
ATOM   325  C CA  . GLY A 1 43  ? 12.487  39.152 0.623  1.00 18.77 ? 43  GLY A CA  1 
ATOM   326  C C   . GLY A 1 43  ? 12.213  40.390 -0.201 1.00 26.59 ? 43  GLY A C   1 
ATOM   327  O O   . GLY A 1 43  ? 13.131  40.884 -0.872 1.00 28.26 ? 43  GLY A O   1 
ATOM   328  N N   . ASN A 1 44  ? 10.984  40.907 -0.179 1.00 24.91 ? 44  ASN A N   1 
ATOM   329  C CA  . ASN A 1 44  ? 10.603  42.072 -0.970 1.00 36.87 ? 44  ASN A CA  1 
ATOM   330  C C   . ASN A 1 44  ? 10.334  43.241 -0.038 1.00 28.46 ? 44  ASN A C   1 
ATOM   331  O O   . ASN A 1 44  ? 9.556   43.121 0.913  1.00 27.46 ? 44  ASN A O   1 
ATOM   332  C CB  . ASN A 1 44  ? 9.371   41.803 -1.845 1.00 35.81 ? 44  ASN A CB  1 
ATOM   333  C CG  . ASN A 1 44  ? 9.547   40.602 -2.753 1.00 33.42 ? 44  ASN A CG  1 
ATOM   334  O OD1 . ASN A 1 44  ? 10.577  40.445 -3.412 1.00 37.18 ? 44  ASN A OD1 1 
ATOM   335  N ND2 . ASN A 1 44  ? 8.526   39.761 -2.814 1.00 31.84 ? 44  ASN A ND2 1 
ATOM   336  N N   . LEU A 1 45  ? 10.907  44.386 -0.367 1.00 27.31 ? 45  LEU A N   1 
ATOM   337  C CA  . LEU A 1 45  ? 10.646  45.625 0.340  1.00 23.76 ? 45  LEU A CA  1 
ATOM   338  C C   . LEU A 1 45  ? 9.576   46.392 -0.409 1.00 26.71 ? 45  LEU A C   1 
ATOM   339  O O   . LEU A 1 45  ? 9.790   46.803 -1.553 1.00 31.66 ? 45  LEU A O   1 
ATOM   340  C CB  . LEU A 1 45  ? 11.915  46.462 0.466  1.00 25.27 ? 45  LEU A CB  1 
ATOM   341  C CG  . LEU A 1 45  ? 11.734  47.721 1.300  1.00 29.56 ? 45  LEU A CG  1 
ATOM   342  C CD1 . LEU A 1 45  ? 11.364  47.353 2.751  1.00 20.02 ? 45  LEU A CD1 1 
ATOM   343  C CD2 . LEU A 1 45  ? 13.029  48.512 1.246  1.00 28.13 ? 45  LEU A CD2 1 
ATOM   344  N N   . ASN A 1 46  ? 8.442   46.607 0.242  1.00 23.39 ? 46  ASN A N   1 
ATOM   345  C CA  . ASN A 1 46  ? 7.363   47.368 -0.355 1.00 24.53 ? 46  ASN A CA  1 
ATOM   346  C C   . ASN A 1 46  ? 7.005   48.506 0.571  1.00 22.93 ? 46  ASN A C   1 
ATOM   347  O O   . ASN A 1 46  ? 7.289   48.468 1.765  1.00 30.22 ? 46  ASN A O   1 
ATOM   348  C CB  . ASN A 1 46  ? 6.105   46.524 -0.557 1.00 26.45 ? 46  ASN A CB  1 
ATOM   349  C CG  . ASN A 1 46  ? 6.382   45.223 -1.231 1.00 32.00 ? 46  ASN A CG  1 
ATOM   350  O OD1 . ASN A 1 46  ? 6.207   44.155 -0.638 1.00 24.07 ? 46  ASN A OD1 1 
ATOM   351  N ND2 . ASN A 1 46  ? 6.801   45.293 -2.494 1.00 35.02 ? 46  ASN A ND2 1 
ATOM   352  N N   . GLU A 1 47  ? 6.375   49.521 0.015  1.00 26.58 ? 47  GLU A N   1 
ATOM   353  C CA  . GLU A 1 47  ? 5.829   50.586 0.825  1.00 22.32 ? 47  GLU A CA  1 
ATOM   354  C C   . GLU A 1 47  ? 4.343   50.364 1.006  1.00 21.45 ? 47  GLU A C   1 
ATOM   355  O O   . GLU A 1 47  ? 3.625   50.066 0.047  1.00 26.53 ? 47  GLU A O   1 
ATOM   356  C CB  . GLU A 1 47  ? 6.146   51.934 0.193  1.00 25.24 ? 47  GLU A CB  1 
ATOM   357  C CG  . GLU A 1 47  ? 7.621   52.264 0.368  1.00 33.58 ? 47  GLU A CG  1 
ATOM   358  C CD  . GLU A 1 47  ? 8.029   53.564 -0.264 1.00 36.51 ? 47  GLU A CD  1 
ATOM   359  O OE1 . GLU A 1 47  ? 9.140   53.631 -0.832 1.00 37.40 ? 47  GLU A OE1 1 
ATOM   360  O OE2 . GLU A 1 47  ? 7.231   54.522 -0.186 1.00 35.09 ? 47  GLU A OE2 1 
ATOM   361  N N   . TYR A 1 48  ? 3.887   50.534 2.238  1.00 18.48 ? 48  TYR A N   1 
ATOM   362  C CA  . TYR A 1 48  ? 2.495   50.324 2.583  1.00 21.10 ? 48  TYR A CA  1 
ATOM   363  C C   . TYR A 1 48  ? 1.894   51.629 3.062  1.00 20.13 ? 48  TYR A C   1 
ATOM   364  O O   . TYR A 1 48  ? 2.593   52.618 3.284  1.00 19.15 ? 48  TYR A O   1 
ATOM   365  C CB  . TYR A 1 48  ? 2.353   49.202 3.609  1.00 18.17 ? 48  TYR A CB  1 
ATOM   366  C CG  . TYR A 1 48  ? 2.795   47.876 3.026  1.00 23.97 ? 48  TYR A CG  1 
ATOM   367  C CD1 . TYR A 1 48  ? 2.012   47.208 2.093  1.00 16.71 ? 48  TYR A CD1 1 
ATOM   368  C CD2 . TYR A 1 48  ? 4.011   47.315 3.378  1.00 25.12 ? 48  TYR A CD2 1 
ATOM   369  C CE1 . TYR A 1 48  ? 2.416   46.001 1.553  1.00 23.82 ? 48  TYR A CE1 1 
ATOM   370  C CE2 . TYR A 1 48  ? 4.425   46.109 2.837  1.00 25.38 ? 48  TYR A CE2 1 
ATOM   371  C CZ  . TYR A 1 48  ? 3.624   45.452 1.924  1.00 26.84 ? 48  TYR A CZ  1 
ATOM   372  O OH  . TYR A 1 48  ? 4.043   44.246 1.382  1.00 22.85 ? 48  TYR A OH  1 
ATOM   373  N N   . SER A 1 49  ? 0.581   51.606 3.230  1.00 18.81 ? 49  SER A N   1 
ATOM   374  C CA  . SER A 1 49  ? -0.206  52.822 3.327  1.00 19.46 ? 49  SER A CA  1 
ATOM   375  C C   . SER A 1 49  ? -0.344  53.282 4.772  1.00 16.72 ? 49  SER A C   1 
ATOM   376  O O   . SER A 1 49  ? -1.087  52.686 5.556  1.00 22.45 ? 49  SER A O   1 
ATOM   377  C CB  . SER A 1 49  ? -1.581  52.597 2.703  1.00 23.81 ? 49  SER A CB  1 
ATOM   378  O OG  . SER A 1 49  ? -2.380  53.762 2.820  1.00 22.11 ? 49  SER A OG  1 
ATOM   379  N N   . GLU A 1 50  ? 0.349   54.375 5.110  1.00 19.65 ? 50  GLU A N   1 
ATOM   380  C CA  . GLU A 1 50  ? 0.041   55.077 6.348  1.00 16.21 ? 50  GLU A CA  1 
ATOM   381  C C   . GLU A 1 50  ? -1.364  55.630 6.284  1.00 16.25 ? 50  GLU A C   1 
ATOM   382  O O   . GLU A 1 50  ? -2.095  55.608 7.282  1.00 17.10 ? 50  GLU A O   1 
ATOM   383  C CB  . GLU A 1 50  ? 1.062   56.185 6.605  1.00 20.47 ? 50  GLU A CB  1 
ATOM   384  C CG  . GLU A 1 50  ? 2.495   55.670 6.772  1.00 21.11 ? 50  GLU A CG  1 
ATOM   385  C CD  . GLU A 1 50  ? 3.265   55.635 5.471  1.00 26.12 ? 50  GLU A CD  1 
ATOM   386  O OE1 . GLU A 1 50  ? 2.655   55.954 4.425  1.00 26.09 ? 50  GLU A OE1 1 
ATOM   387  O OE2 . GLU A 1 50  ? 4.465   55.267 5.487  1.00 24.60 ? 50  GLU A OE2 1 
ATOM   388  N N   . GLN A 1 51  ? -1.764  56.109 5.102  1.00 19.27 ? 51  GLN A N   1 
ATOM   389  C CA  . GLN A 1 51  ? -3.082  56.708 4.939  1.00 22.87 ? 51  GLN A CA  1 
ATOM   390  C C   . GLN A 1 51  ? -4.175  55.699 5.242  1.00 19.34 ? 51  GLN A C   1 
ATOM   391  O O   . GLN A 1 51  ? -5.208  56.045 5.827  1.00 19.82 ? 51  GLN A O   1 
ATOM   392  C CB  . GLN A 1 51  ? -3.259  57.272 3.524  1.00 19.52 ? 51  GLN A CB  1 
ATOM   393  C CG  . GLN A 1 51  ? -4.581  57.963 3.377  1.00 13.96 ? 51  GLN A CG  1 
ATOM   394  C CD  . GLN A 1 51  ? -4.614  59.268 4.126  1.00 18.19 ? 51  GLN A CD  1 
ATOM   395  O OE1 . GLN A 1 51  ? -3.617  59.993 4.182  1.00 19.09 ? 51  GLN A OE1 1 
ATOM   396  N NE2 . GLN A 1 51  ? -5.748  59.556 4.756  1.00 20.09 ? 51  GLN A NE2 1 
ATOM   397  N N   . GLU A 1 52  ? -3.971  54.447 4.841  1.00 17.65 ? 52  GLU A N   1 
ATOM   398  C CA  . GLU A 1 52  ? -4.978  53.436 5.116  1.00 18.59 ? 52  GLU A CA  1 
ATOM   399  C C   . GLU A 1 52  ? -5.207  53.298 6.610  1.00 23.56 ? 52  GLU A C   1 
ATOM   400  O O   . GLU A 1 52  ? -6.354  53.228 7.062  1.00 25.05 ? 52  GLU A O   1 
ATOM   401  C CB  . GLU A 1 52  ? -4.573  52.110 4.485  1.00 20.19 ? 52  GLU A CB  1 
ATOM   402  C CG  . GLU A 1 52  ? -5.613  51.024 4.622  1.00 19.90 ? 52  GLU A CG  1 
ATOM   403  C CD  . GLU A 1 52  ? -5.316  49.885 3.689  1.00 31.71 ? 52  GLU A CD  1 
ATOM   404  O OE1 . GLU A 1 52  ? -4.132  49.719 3.326  1.00 33.75 ? 52  GLU A OE1 1 
ATOM   405  O OE2 . GLU A 1 52  ? -6.261  49.175 3.284  1.00 34.37 ? 52  GLU A OE2 1 
ATOM   406  N N   . LEU A 1 53  ? -4.129  53.291 7.398  1.00 23.97 ? 53  LEU A N   1 
ATOM   407  C CA  . LEU A 1 53  ? -4.280  53.191 8.844  1.00 20.20 ? 53  LEU A CA  1 
ATOM   408  C C   . LEU A 1 53  ? -4.938  54.441 9.404  1.00 19.20 ? 53  LEU A C   1 
ATOM   409  O O   . LEU A 1 53  ? -5.819  54.358 10.267 1.00 22.29 ? 53  LEU A O   1 
ATOM   410  C CB  . LEU A 1 53  ? -2.908  52.976 9.486  1.00 16.57 ? 53  LEU A CB  1 
ATOM   411  C CG  . LEU A 1 53  ? -2.120  51.777 8.939  1.00 23.01 ? 53  LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 53  ? -0.774  51.645 9.630  1.00 17.69 ? 53  LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 53  ? -2.921  50.488 9.098  1.00 15.69 ? 53  LEU A CD2 1 
ATOM   414  N N   . LEU A 1 54  ? -4.538  55.610 8.902  1.00 20.82 ? 54  LEU A N   1 
ATOM   415  C CA  . LEU A 1 54  ? -5.154  56.865 9.324  1.00 21.36 ? 54  LEU A CA  1 
ATOM   416  C C   . LEU A 1 54  ? -6.663  56.848 9.125  1.00 21.50 ? 54  LEU A C   1 
ATOM   417  O O   . LEU A 1 54  ? -7.425  57.278 9.999  1.00 22.17 ? 54  LEU A O   1 
ATOM   418  C CB  . LEU A 1 54  ? -4.557  58.029 8.541  1.00 24.81 ? 54  LEU A CB  1 
ATOM   419  C CG  . LEU A 1 54  ? -3.496  58.890 9.190  1.00 29.34 ? 54  LEU A CG  1 
ATOM   420  C CD1 . LEU A 1 54  ? -2.874  59.768 8.115  1.00 35.23 ? 54  LEU A CD1 1 
ATOM   421  C CD2 . LEU A 1 54  ? -4.124  59.722 10.257 1.00 29.72 ? 54  LEU A CD2 1 
ATOM   422  N N   . ASP A 1 55  ? -7.110  56.381 7.959  1.00 18.96 ? 55  ASP A N   1 
ATOM   423  C CA  . ASP A 1 55  ? -8.533  56.395 7.639  1.00 25.82 ? 55  ASP A CA  1 
ATOM   424  C C   . ASP A 1 55  ? -9.291  55.297 8.360  1.00 20.15 ? 55  ASP A C   1 
ATOM   425  O O   . ASP A 1 55  ? -10.428 55.505 8.786  1.00 29.32 ? 55  ASP A O   1 
ATOM   426  C CB  . ASP A 1 55  ? -8.734  56.215 6.133  1.00 25.91 ? 55  ASP A CB  1 
ATOM   427  C CG  . ASP A 1 55  ? -8.172  57.359 5.304  1.00 28.28 ? 55  ASP A CG  1 
ATOM   428  O OD1 . ASP A 1 55  ? -7.076  57.878 5.595  1.00 26.41 ? 55  ASP A OD1 1 
ATOM   429  O OD2 . ASP A 1 55  ? -8.790  57.656 4.259  1.00 34.52 ? 55  ASP A OD2 1 
ATOM   430  N N   . CYS A 1 56  ? -8.677  54.129 8.505  1.00 23.07 ? 56  CYS A N   1 
ATOM   431  C CA  . CYS A 1 56  ? -9.394  52.903 8.812  1.00 22.92 ? 56  CYS A CA  1 
ATOM   432  C C   . CYS A 1 56  ? -9.227  52.405 10.233 1.00 21.13 ? 56  CYS A C   1 
ATOM   433  O O   . CYS A 1 56  ? -9.978  51.519 10.646 1.00 24.91 ? 56  CYS A O   1 
ATOM   434  C CB  . CYS A 1 56  ? -8.972  51.792 7.844  1.00 22.98 ? 56  CYS A CB  1 
ATOM   435  S SG  . CYS A 1 56  ? -9.254  52.284 6.166  1.00 28.72 ? 56  CYS A SG  1 
ATOM   436  N N   . ASP A 1 57  ? -8.248  52.898 10.975 1.00 21.68 ? 57  ASP A N   1 
ATOM   437  C CA  . ASP A 1 57  ? -8.098  52.425 12.342 1.00 28.18 ? 57  ASP A CA  1 
ATOM   438  C C   . ASP A 1 57  ? -9.143  53.127 13.207 1.00 27.66 ? 57  ASP A C   1 
ATOM   439  O O   . ASP A 1 57  ? -8.937  54.248 13.684 1.00 29.94 ? 57  ASP A O   1 
ATOM   440  C CB  . ASP A 1 57  ? -6.682  52.674 12.838 1.00 23.04 ? 57  ASP A CB  1 
ATOM   441  C CG  . ASP A 1 57  ? -6.481  52.178 14.236 1.00 26.37 ? 57  ASP A CG  1 
ATOM   442  O OD1 . ASP A 1 57  ? -7.425  51.562 14.780 1.00 22.97 ? 57  ASP A OD1 1 
ATOM   443  O OD2 . ASP A 1 57  ? -5.386  52.395 14.792 1.00 34.80 ? 57  ASP A OD2 1 
ATOM   444  N N   . ARG A 1 58  ? -10.245 52.431 13.474 1.00 17.01 ? 58  ARG A N   1 
ATOM   445  C CA  . ARG A 1 58  ? -11.338 53.029 14.223 1.00 22.99 ? 58  ARG A CA  1 
ATOM   446  C C   . ARG A 1 58  ? -11.027 53.270 15.700 1.00 25.09 ? 58  ARG A C   1 
ATOM   447  O O   . ARG A 1 58  ? -11.820 53.946 16.366 1.00 23.17 ? 58  ARG A O   1 
ATOM   448  C CB  . ARG A 1 58  ? -12.574 52.152 14.055 1.00 31.23 ? 58  ARG A CB  1 
ATOM   449  C CG  . ARG A 1 58  ? -13.163 52.225 12.648 1.00 21.80 ? 58  ARG A CG  1 
ATOM   450  C CD  . ARG A 1 58  ? -14.300 51.233 12.473 1.00 28.99 ? 58  ARG A CD  1 
ATOM   451  N NE  . ARG A 1 58  ? -13.825 49.855 12.439 1.00 17.07 ? 58  ARG A NE  1 
ATOM   452  C CZ  . ARG A 1 58  ? -14.577 48.819 12.095 1.00 26.27 ? 58  ARG A CZ  1 
ATOM   453  N NH1 . ARG A 1 58  ? -15.852 48.967 11.763 1.00 25.55 ? 58  ARG A NH1 1 
ATOM   454  N NH2 . ARG A 1 58  ? -14.035 47.606 12.066 1.00 27.70 ? 58  ARG A NH2 1 
ATOM   455  N N   . ARG A 1 59  ? -9.923  52.738 16.239 1.00 25.00 ? 59  ARG A N   1 
ATOM   456  C CA  . ARG A 1 59  ? -9.552  53.069 17.617 1.00 27.48 ? 59  ARG A CA  1 
ATOM   457  C C   . ARG A 1 59  ? -8.688  54.306 17.703 1.00 26.33 ? 59  ARG A C   1 
ATOM   458  O O   . ARG A 1 59  ? -8.665  54.962 18.751 1.00 28.87 ? 59  ARG A O   1 
ATOM   459  C CB  . ARG A 1 59  ? -8.776  51.944 18.297 1.00 22.00 ? 59  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 59  ? -9.383  50.591 18.199 1.00 36.90 ? 59  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 59  ? -8.626  49.638 19.087 1.00 38.81 ? 59  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 59  ? -9.024  48.265 18.831 1.00 42.44 ? 59  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 59  ? -9.748  47.544 19.673 1.00 56.75 ? 59  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 59  ? -10.173 48.048 20.825 1.00 36.07 ? 59  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 59  ? -10.055 46.289 19.350 1.00 51.66 ? 59  ARG A NH2 1 
ATOM   466  N N   . SER A 1 60  ? -7.949  54.607 16.641 1.00 23.52 ? 60  SER A N   1 
ATOM   467  C CA  . SER A 1 60  ? -7.190  55.837 16.555 1.00 24.84 ? 60  SER A CA  1 
ATOM   468  C C   . SER A 1 60  ? -8.117  56.990 16.211 1.00 17.31 ? 60  SER A C   1 
ATOM   469  O O   . SER A 1 60  ? -9.291  56.808 15.884 1.00 24.70 ? 60  SER A O   1 
ATOM   470  C CB  . SER A 1 60  ? -6.085  55.712 15.512 1.00 23.11 ? 60  SER A CB  1 
ATOM   471  O OG  . SER A 1 60  ? -5.056  54.850 15.960 1.00 20.45 ? 60  SER A OG  1 
ATOM   472  N N   . TYR A 1 61  ? -7.573  58.191 16.265 1.00 24.71 ? 61  TYR A N   1 
ATOM   473  C CA  . TYR A 1 61  ? -8.351  59.395 16.029 1.00 26.31 ? 61  TYR A CA  1 
ATOM   474  C C   . TYR A 1 61  ? -7.817  60.163 14.827 1.00 31.06 ? 61  TYR A C   1 
ATOM   475  O O   . TYR A 1 61  ? -7.774  61.396 14.824 1.00 30.81 ? 61  TYR A O   1 
ATOM   476  C CB  . TYR A 1 61  ? -8.378  60.262 17.287 1.00 32.79 ? 61  TYR A CB  1 
ATOM   477  C CG  . TYR A 1 61  ? -8.743  59.467 18.529 1.00 38.23 ? 61  TYR A CG  1 
ATOM   478  C CD1 . TYR A 1 61  ? -10.072 59.162 18.821 1.00 34.65 ? 61  TYR A CD1 1 
ATOM   479  C CD2 . TYR A 1 61  ? -7.758  58.993 19.388 1.00 33.35 ? 61  TYR A CD2 1 
ATOM   480  C CE1 . TYR A 1 61  ? -10.407 58.413 19.943 1.00 43.14 ? 61  TYR A CE1 1 
ATOM   481  C CE2 . TYR A 1 61  ? -8.083  58.250 20.512 1.00 41.04 ? 61  TYR A CE2 1 
ATOM   482  C CZ  . TYR A 1 61  ? -9.408  57.960 20.783 1.00 42.02 ? 61  TYR A CZ  1 
ATOM   483  O OH  . TYR A 1 61  ? -9.728  57.223 21.903 1.00 49.68 ? 61  TYR A OH  1 
ATOM   484  N N   . GLY A 1 62  ? -7.400  59.437 13.789 1.00 23.99 ? 62  GLY A N   1 
ATOM   485  C CA  . GLY A 1 62  ? -6.953  60.105 12.578 1.00 24.48 ? 62  GLY A CA  1 
ATOM   486  C C   . GLY A 1 62  ? -5.726  60.965 12.822 1.00 26.26 ? 62  GLY A C   1 
ATOM   487  O O   . GLY A 1 62  ? -4.727  60.527 13.400 1.00 25.05 ? 62  GLY A O   1 
ATOM   488  N N   . CYS A 1 63  ? -5.794  62.212 12.365 1.00 30.65 ? 63  CYS A N   1 
ATOM   489  C CA  . CYS A 1 63  ? -4.697  63.149 12.545 1.00 23.33 ? 63  CYS A CA  1 
ATOM   490  C C   . CYS A 1 63  ? -4.616  63.703 13.952 1.00 26.33 ? 63  CYS A C   1 
ATOM   491  O O   . CYS A 1 63  ? -3.684  64.452 14.257 1.00 31.97 ? 63  CYS A O   1 
ATOM   492  C CB  . CYS A 1 63  ? -4.849  64.327 11.581 1.00 24.51 ? 63  CYS A CB  1 
ATOM   493  S SG  . CYS A 1 63  ? -4.579  63.905 9.880  1.00 39.87 ? 63  CYS A SG  1 
ATOM   494  N N   . ASN A 1 64  ? -5.519  63.319 14.830 1.00 25.24 ? 64  ASN A N   1 
ATOM   495  C CA  . ASN A 1 64  ? -5.421  63.743 16.209 1.00 26.76 ? 64  ASN A CA  1 
ATOM   496  C C   . ASN A 1 64  ? -4.673  62.734 17.055 1.00 32.68 ? 64  ASN A C   1 
ATOM   497  O O   . ASN A 1 64  ? -4.707  62.817 18.288 1.00 37.37 ? 64  ASN A O   1 
ATOM   498  C CB  . ASN A 1 64  ? -6.821  64.010 16.759 1.00 34.20 ? 64  ASN A CB  1 
ATOM   499  C CG  . ASN A 1 64  ? -7.461  65.237 16.120 1.00 35.87 ? 64  ASN A CG  1 
ATOM   500  O OD1 . ASN A 1 64  ? -8.567  65.165 15.586 1.00 39.71 ? 64  ASN A OD1 1 
ATOM   501  N ND2 . ASN A 1 64  ? -6.746  66.353 16.130 1.00 30.57 ? 64  ASN A ND2 1 
ATOM   502  N N   . GLY A 1 65  ? -4.006  61.783 16.423 1.00 29.23 ? 65  GLY A N   1 
ATOM   503  C CA  . GLY A 1 65  ? -3.193  60.823 17.133 1.00 26.24 ? 65  GLY A CA  1 
ATOM   504  C C   . GLY A 1 65  ? -3.834  59.451 17.097 1.00 20.34 ? 65  GLY A C   1 
ATOM   505  O O   . GLY A 1 65  ? -4.928  59.252 16.568 1.00 27.31 ? 65  GLY A O   1 
ATOM   506  N N   . GLY A 1 66  ? -3.125  58.500 17.681 1.00 19.95 ? 66  GLY A N   1 
ATOM   507  C CA  . GLY A 1 66  ? -3.558  57.125 17.588 1.00 21.57 ? 66  GLY A CA  1 
ATOM   508  C C   . GLY A 1 66  ? -2.569  56.212 18.265 1.00 26.16 ? 66  GLY A C   1 
ATOM   509  O O   . GLY A 1 66  ? -1.663  56.656 18.976 1.00 29.23 ? 66  GLY A O   1 
ATOM   510  N N   . TYR A 1 67  ? -2.747  54.919 18.014 1.00 22.20 ? 67  TYR A N   1 
ATOM   511  C CA  . TYR A 1 67  ? -2.069  53.886 18.778 1.00 21.46 ? 67  TYR A CA  1 
ATOM   512  C C   . TYR A 1 67  ? -1.373  52.990 17.771 1.00 24.57 ? 67  TYR A C   1 
ATOM   513  O O   . TYR A 1 67  ? -2.052  52.352 16.941 1.00 26.22 ? 67  TYR A O   1 
ATOM   514  C CB  . TYR A 1 67  ? -3.040  53.095 19.645 1.00 23.91 ? 67  TYR A CB  1 
ATOM   515  C CG  . TYR A 1 67  ? -3.865  53.967 20.551 1.00 24.25 ? 67  TYR A CG  1 
ATOM   516  C CD1 . TYR A 1 67  ? -3.325  54.498 21.716 1.00 26.02 ? 67  TYR A CD1 1 
ATOM   517  C CD2 . TYR A 1 67  ? -5.182  54.265 20.244 1.00 22.93 ? 67  TYR A CD2 1 
ATOM   518  C CE1 . TYR A 1 67  ? -4.078  55.308 22.550 1.00 29.85 ? 67  TYR A CE1 1 
ATOM   519  C CE2 . TYR A 1 67  ? -5.948  55.068 21.076 1.00 33.61 ? 67  TYR A CE2 1 
ATOM   520  C CZ  . TYR A 1 67  ? -5.393  55.585 22.227 1.00 28.51 ? 67  TYR A CZ  1 
ATOM   521  O OH  . TYR A 1 67  ? -6.153  56.387 23.051 1.00 34.12 ? 67  TYR A OH  1 
ATOM   522  N N   . PRO A 1 68  ? -0.045  52.930 17.784 1.00 21.91 ? 68  PRO A N   1 
ATOM   523  C CA  . PRO A 1 68  ? 0.648   51.970 16.922 1.00 22.56 ? 68  PRO A CA  1 
ATOM   524  C C   . PRO A 1 68  ? 0.154   50.548 17.113 1.00 20.11 ? 68  PRO A C   1 
ATOM   525  O O   . PRO A 1 68  ? 0.104   49.782 16.140 1.00 19.90 ? 68  PRO A O   1 
ATOM   526  C CB  . PRO A 1 68  ? 2.111   52.130 17.351 1.00 20.71 ? 68  PRO A CB  1 
ATOM   527  C CG  . PRO A 1 68  ? 2.200   53.519 17.846 1.00 21.14 ? 68  PRO A CG  1 
ATOM   528  C CD  . PRO A 1 68  ? 0.890   53.793 18.527 1.00 18.62 ? 68  PRO A CD  1 
ATOM   529  N N   . TRP A 1 69  ? -0.244  50.180 18.337 1.00 23.52 ? 69  TRP A N   1 
ATOM   530  C CA  A TRP A 1 69  ? -0.754  48.832 18.549 0.50 22.29 ? 69  TRP A CA  1 
ATOM   531  C CA  B TRP A 1 69  ? -0.769  48.838 18.570 0.50 21.88 ? 69  TRP A CA  1 
ATOM   532  C C   . TRP A 1 69  ? -2.067  48.625 17.812 1.00 22.36 ? 69  TRP A C   1 
ATOM   533  O O   . TRP A 1 69  ? -2.288  47.559 17.220 1.00 24.35 ? 69  TRP A O   1 
ATOM   534  C CB  A TRP A 1 69  ? -0.908  48.531 20.046 0.50 22.74 ? 69  TRP A CB  1 
ATOM   535  C CB  B TRP A 1 69  ? -0.992  48.595 20.066 0.50 22.95 ? 69  TRP A CB  1 
ATOM   536  C CG  A TRP A 1 69  ? -1.649  49.547 20.883 0.50 23.77 ? 69  TRP A CG  1 
ATOM   537  C CG  B TRP A 1 69  ? -1.967  47.472 20.331 0.50 23.56 ? 69  TRP A CG  1 
ATOM   538  C CD1 A TRP A 1 69  ? -1.105  50.599 21.569 0.50 25.30 ? 69  TRP A CD1 1 
ATOM   539  C CD1 B TRP A 1 69  ? -1.685  46.135 20.382 0.50 23.52 ? 69  TRP A CD1 1 
ATOM   540  C CD2 A TRP A 1 69  ? -3.056  49.566 21.175 0.50 26.75 ? 69  TRP A CD2 1 
ATOM   541  C CD2 B TRP A 1 69  ? -3.381  47.590 20.541 0.50 26.41 ? 69  TRP A CD2 1 
ATOM   542  N NE1 A TRP A 1 69  ? -2.090  51.282 22.250 0.50 25.70 ? 69  TRP A NE1 1 
ATOM   543  N NE1 B TRP A 1 69  ? -2.832  45.419 20.625 0.50 25.55 ? 69  TRP A NE1 1 
ATOM   544  C CE2 A TRP A 1 69  ? -3.294  50.669 22.023 0.50 24.09 ? 69  TRP A CE2 1 
ATOM   545  C CE2 B TRP A 1 69  ? -3.886  46.288 20.724 0.50 30.00 ? 69  TRP A CE2 1 
ATOM   546  C CE3 A TRP A 1 69  ? -4.137  48.763 20.794 0.50 29.32 ? 69  TRP A CE3 1 
ATOM   547  C CE3 B TRP A 1 69  ? -4.267  48.670 20.596 0.50 29.32 ? 69  TRP A CE3 1 
ATOM   548  C CZ2 A TRP A 1 69  ? -4.568  50.994 22.487 0.50 26.50 ? 69  TRP A CZ2 1 
ATOM   549  C CZ2 B TRP A 1 69  ? -5.238  46.039 20.961 0.50 38.21 ? 69  TRP A CZ2 1 
ATOM   550  C CZ3 A TRP A 1 69  ? -5.400  49.085 21.261 0.50 29.90 ? 69  TRP A CZ3 1 
ATOM   551  C CZ3 B TRP A 1 69  ? -5.607  48.420 20.830 0.50 29.33 ? 69  TRP A CZ3 1 
ATOM   552  C CH2 A TRP A 1 69  ? -5.605  50.192 22.097 0.50 27.30 ? 69  TRP A CH2 1 
ATOM   553  C CH2 B TRP A 1 69  ? -6.080  47.118 21.008 0.50 31.88 ? 69  TRP A CH2 1 
ATOM   554  N N   . SER A 1 70  ? -2.941  49.632 17.823 1.00 25.87 ? 70  SER A N   1 
ATOM   555  C CA  . SER A 1 70  ? -4.209  49.523 17.110 1.00 23.90 ? 70  SER A CA  1 
ATOM   556  C C   . SER A 1 70  ? -3.985  49.375 15.612 1.00 25.37 ? 70  SER A C   1 
ATOM   557  O O   . SER A 1 70  ? -4.652  48.565 14.954 1.00 31.37 ? 70  SER A O   1 
ATOM   558  C CB  . SER A 1 70  ? -5.069  50.749 17.406 1.00 28.87 ? 70  SER A CB  1 
ATOM   559  O OG  . SER A 1 70  ? -6.380  50.559 16.924 1.00 33.11 ? 70  SER A OG  1 
ATOM   560  N N   . ALA A 1 71  ? -3.039  50.140 15.053 1.00 24.02 ? 71  ALA A N   1 
ATOM   561  C CA  . ALA A 1 71  ? -2.756  50.058 13.620 1.00 22.94 ? 71  ALA A CA  1 
ATOM   562  C C   . ALA A 1 71  ? -2.171  48.705 13.239 1.00 18.91 ? 71  ALA A C   1 
ATOM   563  O O   . ALA A 1 71  ? -2.523  48.132 12.194 1.00 24.19 ? 71  ALA A O   1 
ATOM   564  C CB  . ALA A 1 71  ? -1.792  51.174 13.212 1.00 22.07 ? 71  ALA A CB  1 
ATOM   565  N N   . LEU A 1 72  ? -1.286  48.163 14.076 1.00 20.66 ? 72  LEU A N   1 
ATOM   566  C CA  . LEU A 1 72  ? -0.726  46.863 13.734 1.00 25.58 ? 72  LEU A CA  1 
ATOM   567  C C   . LEU A 1 72  ? -1.779  45.776 13.866 1.00 20.37 ? 72  LEU A C   1 
ATOM   568  O O   . LEU A 1 72  ? -1.799  44.818 13.078 1.00 22.45 ? 72  LEU A O   1 
ATOM   569  C CB  . LEU A 1 72  ? 0.478   46.556 14.624 1.00 25.89 ? 72  LEU A CB  1 
ATOM   570  C CG  . LEU A 1 72  ? 1.707   47.405 14.289 1.00 26.26 ? 72  LEU A CG  1 
ATOM   571  C CD1 . LEU A 1 72  ? 2.837   47.164 15.287 1.00 18.79 ? 72  LEU A CD1 1 
ATOM   572  C CD2 . LEU A 1 72  ? 2.145   47.209 12.847 1.00 20.24 ? 72  LEU A CD2 1 
ATOM   573  N N   . GLN A 1 73  ? -2.670  45.920 14.841 1.00 20.18 ? 73  GLN A N   1 
ATOM   574  C CA  . GLN A 1 73  ? -3.767  44.978 14.965 1.00 28.10 ? 73  GLN A CA  1 
ATOM   575  C C   . GLN A 1 73  ? -4.694  45.080 13.762 1.00 28.04 ? 73  GLN A C   1 
ATOM   576  O O   . GLN A 1 73  ? -5.262  44.071 13.332 1.00 31.16 ? 73  GLN A O   1 
ATOM   577  C CB  . GLN A 1 73  ? -4.494  45.229 16.291 1.00 27.87 ? 73  GLN A CB  1 
ATOM   578  C CG  . GLN A 1 73  ? -5.534  44.191 16.693 1.00 42.77 ? 73  GLN A CG  1 
ATOM   579  C CD  . GLN A 1 73  ? -6.761  44.824 17.339 1.00 49.81 ? 73  GLN A CD  1 
ATOM   580  O OE1 . GLN A 1 73  ? -6.962  46.042 17.272 1.00 48.39 ? 73  GLN A OE1 1 
ATOM   581  N NE2 . GLN A 1 73  ? -7.580  43.999 17.983 1.00 54.46 ? 73  GLN A NE2 1 
ATOM   582  N N   . LEU A 1 74  ? -4.829  46.278 13.185 1.00 24.54 ? 74  LEU A N   1 
ATOM   583  C CA  . LEU A 1 74  ? -5.633  46.433 11.976 1.00 25.44 ? 74  LEU A CA  1 
ATOM   584  C C   . LEU A 1 74  ? -5.000  45.707 10.794 1.00 27.67 ? 74  LEU A C   1 
ATOM   585  O O   . LEU A 1 74  ? -5.694  45.039 10.020 1.00 30.70 ? 74  LEU A O   1 
ATOM   586  C CB  . LEU A 1 74  ? -5.802  47.917 11.647 1.00 32.17 ? 74  LEU A CB  1 
ATOM   587  C CG  . LEU A 1 74  ? -6.741  48.285 10.497 1.00 29.29 ? 74  LEU A CG  1 
ATOM   588  C CD1 . LEU A 1 74  ? -8.136  47.795 10.824 1.00 42.70 ? 74  LEU A CD1 1 
ATOM   589  C CD2 . LEU A 1 74  ? -6.730  49.789 10.178 1.00 28.82 ? 74  LEU A CD2 1 
ATOM   590  N N   . VAL A 1 75  ? -3.680  45.815 10.646 1.00 28.00 ? 75  VAL A N   1 
ATOM   591  C CA  . VAL A 1 75  ? -3.027  45.124 9.534  1.00 25.85 ? 75  VAL A CA  1 
ATOM   592  C C   . VAL A 1 75  ? -3.061  43.616 9.731  1.00 26.65 ? 75  VAL A C   1 
ATOM   593  O O   . VAL A 1 75  ? -3.097  42.854 8.756  1.00 26.76 ? 75  VAL A O   1 
ATOM   594  C CB  . VAL A 1 75  ? -1.594  45.639 9.345  1.00 22.75 ? 75  VAL A CB  1 
ATOM   595  C CG1 . VAL A 1 75  ? -0.906  44.906 8.177  1.00 19.36 ? 75  VAL A CG1 1 
ATOM   596  C CG2 . VAL A 1 75  ? -1.657  47.128 9.111  1.00 25.74 ? 75  VAL A CG2 1 
ATOM   597  N N   . ALA A 1 76  ? -3.046  43.153 10.977 1.00 29.51 ? 76  ALA A N   1 
ATOM   598  C CA  . ALA A 1 76  ? -3.122  41.715 11.180 1.00 28.06 ? 76  ALA A CA  1 
ATOM   599  C C   . ALA A 1 76  ? -4.545  41.199 10.997 1.00 28.80 ? 76  ALA A C   1 
ATOM   600  O O   . ALA A 1 76  ? -4.734  40.074 10.519 1.00 36.18 ? 76  ALA A O   1 
ATOM   601  C CB  . ALA A 1 76  ? -2.582  41.356 12.562 1.00 18.18 ? 76  ALA A CB  1 
ATOM   602  N N   . GLN A 1 77  ? -5.553  42.004 11.335 1.00 28.12 ? 77  GLN A N   1 
ATOM   603  C CA  . GLN A 1 77  ? -6.940  41.559 11.233 1.00 33.62 ? 77  GLN A CA  1 
ATOM   604  C C   . GLN A 1 77  ? -7.426  41.593 9.790  1.00 30.18 ? 77  GLN A C   1 
ATOM   605  O O   . GLN A 1 77  ? -8.044  40.636 9.312  1.00 40.90 ? 77  GLN A O   1 
ATOM   606  C CB  . GLN A 1 77  ? -7.834  42.427 12.129 1.00 33.47 ? 77  GLN A CB  1 
ATOM   607  C CG  . GLN A 1 77  ? -9.336  42.220 11.942 1.00 40.97 ? 77  GLN A CG  1 
ATOM   608  C CD  . GLN A 1 77  ? -9.832  40.885 12.483 1.00 69.23 ? 77  GLN A CD  1 
ATOM   609  O OE1 . GLN A 1 77  ? -10.431 40.087 11.754 1.00 59.82 ? 77  GLN A OE1 1 
ATOM   610  N NE2 . GLN A 1 77  ? -9.596  40.641 13.774 1.00 58.36 ? 77  GLN A NE2 1 
ATOM   611  N N   . TYR A 1 78  ? -7.159  42.688 9.083  1.00 29.46 ? 78  TYR A N   1 
ATOM   612  C CA  . TYR A 1 78  ? -7.578  42.848 7.694  1.00 33.08 ? 78  TYR A CA  1 
ATOM   613  C C   . TYR A 1 78  ? -6.364  42.771 6.786  1.00 32.22 ? 78  TYR A C   1 
ATOM   614  O O   . TYR A 1 78  ? -6.203  41.804 6.033  1.00 39.76 ? 78  TYR A O   1 
ATOM   615  C CB  . TYR A 1 78  ? -8.341  44.159 7.489  1.00 38.88 ? 78  TYR A CB  1 
ATOM   616  C CG  . TYR A 1 78  ? -9.583  44.240 8.336  1.00 46.78 ? 78  TYR A CG  1 
ATOM   617  C CD1 . TYR A 1 78  ? -9.528  44.775 9.615  1.00 45.86 ? 78  TYR A CD1 1 
ATOM   618  C CD2 . TYR A 1 78  ? -10.789 43.698 7.903  1.00 46.13 ? 78  TYR A CD2 1 
ATOM   619  C CE1 . TYR A 1 78  ? -10.650 44.840 10.417 1.00 56.31 ? 78  TYR A CE1 1 
ATOM   620  C CE2 . TYR A 1 78  ? -11.923 43.749 8.706  1.00 56.90 ? 78  TYR A CE2 1 
ATOM   621  C CZ  . TYR A 1 78  ? -11.843 44.322 9.966  1.00 61.45 ? 78  TYR A CZ  1 
ATOM   622  O OH  . TYR A 1 78  ? -12.953 44.390 10.780 1.00 59.46 ? 78  TYR A OH  1 
ATOM   623  N N   . GLY A 1 79  ? -5.509  43.764 6.830  1.00 29.31 ? 79  GLY A N   1 
ATOM   624  C CA  . GLY A 1 79  ? -4.361  43.838 5.961  1.00 22.67 ? 79  GLY A CA  1 
ATOM   625  C C   . GLY A 1 79  ? -4.065  45.293 5.688  1.00 24.31 ? 79  GLY A C   1 
ATOM   626  O O   . GLY A 1 79  ? -4.658  46.189 6.285  1.00 20.29 ? 79  GLY A O   1 
ATOM   627  N N   . ILE A 1 80  ? -3.197  45.513 4.710  1.00 23.62 ? 80  ILE A N   1 
ATOM   628  C CA  . ILE A 1 80  ? -2.784  46.861 4.361  1.00 21.66 ? 80  ILE A CA  1 
ATOM   629  C C   . ILE A 1 80  ? -2.465  46.867 2.879  1.00 23.24 ? 80  ILE A C   1 
ATOM   630  O O   . ILE A 1 80  ? -2.005  45.871 2.316  1.00 25.13 ? 80  ILE A O   1 
ATOM   631  C CB  . ILE A 1 80  ? -1.578  47.321 5.220  1.00 24.99 ? 80  ILE A CB  1 
ATOM   632  C CG1 . ILE A 1 80  ? -1.344  48.827 5.070  1.00 20.24 ? 80  ILE A CG1 1 
ATOM   633  C CG2 . ILE A 1 80  ? -0.319  46.523 4.864  1.00 23.20 ? 80  ILE A CG2 1 
ATOM   634  C CD1 . ILE A 1 80  ? -0.433  49.407 6.122  1.00 15.45 ? 80  ILE A CD1 1 
ATOM   635  N N   . HIS A 1 81  ? -2.730  47.998 2.247  1.00 23.85 ? 81  HIS A N   1 
ATOM   636  C CA  . HIS A 1 81  ? -2.467  48.192 0.834  1.00 25.36 ? 81  HIS A CA  1 
ATOM   637  C C   . HIS A 1 81  ? -1.097  48.795 0.599  1.00 19.13 ? 81  HIS A C   1 
ATOM   638  O O   . HIS A 1 81  ? -0.477  49.368 1.496  1.00 24.95 ? 81  HIS A O   1 
ATOM   639  C CB  . HIS A 1 81  ? -3.544  49.093 0.228  1.00 22.19 ? 81  HIS A CB  1 
ATOM   640  C CG  . HIS A 1 81  ? -4.857  48.404 0.055  1.00 22.16 ? 81  HIS A CG  1 
ATOM   641  N ND1 . HIS A 1 81  ? -5.835  48.419 1.026  1.00 20.47 ? 81  HIS A ND1 1 
ATOM   642  C CD2 . HIS A 1 81  ? -5.354  47.679 -0.974 1.00 20.41 ? 81  HIS A CD2 1 
ATOM   643  C CE1 . HIS A 1 81  ? -6.879  47.732 0.602  1.00 28.88 ? 81  HIS A CE1 1 
ATOM   644  N NE2 . HIS A 1 81  ? -6.613  47.271 -0.608 1.00 30.09 ? 81  HIS A NE2 1 
ATOM   645  N N   . TYR A 1 82  ? -0.623  48.640 -0.629 1.00 17.96 ? 82  TYR A N   1 
ATOM   646  C CA  . TYR A 1 82  ? 0.596   49.312 -1.029 1.00 19.99 ? 82  TYR A CA  1 
ATOM   647  C C   . TYR A 1 82  ? 0.390   50.814 -0.918 1.00 24.95 ? 82  TYR A C   1 
ATOM   648  O O   . TYR A 1 82  ? -0.735  51.314 -0.995 1.00 25.84 ? 82  TYR A O   1 
ATOM   649  C CB  . TYR A 1 82  ? 0.967   48.948 -2.467 1.00 22.41 ? 82  TYR A CB  1 
ATOM   650  C CG  . TYR A 1 82  ? 1.475   47.536 -2.631 1.00 27.23 ? 82  TYR A CG  1 
ATOM   651  C CD1 . TYR A 1 82  ? 2.488   47.048 -1.827 1.00 22.88 ? 82  TYR A CD1 1 
ATOM   652  C CD2 . TYR A 1 82  ? 0.941   46.689 -3.603 1.00 29.53 ? 82  TYR A CD2 1 
ATOM   653  C CE1 . TYR A 1 82  ? 2.960   45.754 -1.985 1.00 29.25 ? 82  TYR A CE1 1 
ATOM   654  C CE2 . TYR A 1 82  ? 1.407   45.395 -3.761 1.00 30.35 ? 82  TYR A CE2 1 
ATOM   655  C CZ  . TYR A 1 82  ? 2.415   44.933 -2.950 1.00 27.09 ? 82  TYR A CZ  1 
ATOM   656  O OH  . TYR A 1 82  ? 2.884   43.645 -3.093 1.00 31.99 ? 82  TYR A OH  1 
ATOM   657  N N   . ARG A 1 83  ? 1.483   51.530 -0.659 1.00 22.50 ? 83  ARG A N   1 
ATOM   658  C CA  . ARG A 1 83  ? 1.400   52.982 -0.546 1.00 22.92 ? 83  ARG A CA  1 
ATOM   659  C C   . ARG A 1 83  ? 0.908   53.607 -1.848 1.00 23.95 ? 83  ARG A C   1 
ATOM   660  O O   . ARG A 1 83  ? 0.083   54.526 -1.830 1.00 27.09 ? 83  ARG A O   1 
ATOM   661  C CB  . ARG A 1 83  ? 2.764   53.535 -0.136 1.00 30.90 ? 83  ARG A CB  1 
ATOM   662  C CG  . ARG A 1 83  ? 2.733   54.900 0.531  1.00 32.56 ? 83  ARG A CG  1 
ATOM   663  C CD  . ARG A 1 83  ? 4.133   55.334 0.927  1.00 37.46 ? 83  ARG A CD  1 
ATOM   664  N NE  . ARG A 1 83  ? 4.086   56.335 1.984  1.00 32.73 ? 83  ARG A NE  1 
ATOM   665  C CZ  . ARG A 1 83  ? 4.603   57.550 1.891  1.00 31.92 ? 83  ARG A CZ  1 
ATOM   666  N NH1 . ARG A 1 83  ? 5.262   57.939 0.813  1.00 31.48 ? 83  ARG A NH1 1 
ATOM   667  N NH2 . ARG A 1 83  ? 4.451   58.397 2.905  1.00 33.14 ? 83  ARG A NH2 1 
ATOM   668  N N   . ASN A 1 84  ? 1.385   53.103 -2.993 1.00 25.76 ? 84  ASN A N   1 
ATOM   669  C CA  . ASN A 1 84  ? 0.982   53.657 -4.285 1.00 30.32 ? 84  ASN A CA  1 
ATOM   670  C C   . ASN A 1 84  ? -0.511  53.469 -4.546 1.00 25.14 ? 84  ASN A C   1 
ATOM   671  O O   . ASN A 1 84  ? -1.110  54.249 -5.293 1.00 24.07 ? 84  ASN A O   1 
ATOM   672  C CB  . ASN A 1 84  ? 1.823   53.026 -5.405 1.00 35.95 ? 84  ASN A CB  1 
ATOM   673  C CG  . ASN A 1 84  ? 1.251   51.700 -5.900 1.00 46.59 ? 84  ASN A CG  1 
ATOM   674  O OD1 . ASN A 1 84  ? 0.279   51.673 -6.663 1.00 44.08 ? 84  ASN A OD1 1 
ATOM   675  N ND2 . ASN A 1 84  ? 1.852   50.591 -5.463 1.00 35.31 ? 84  ASN A ND2 1 
ATOM   676  N N   . THR A 1 85  ? -1.123  52.451 -3.937 1.00 24.67 ? 85  THR A N   1 
ATOM   677  C CA  . THR A 1 85  ? -2.559  52.208 -4.053 1.00 24.90 ? 85  THR A CA  1 
ATOM   678  C C   . THR A 1 85  ? -3.385  53.139 -3.174 1.00 22.93 ? 85  THR A C   1 
ATOM   679  O O   . THR A 1 85  ? -4.536  53.447 -3.503 1.00 22.84 ? 85  THR A O   1 
ATOM   680  C CB  . THR A 1 85  ? -2.865  50.759 -3.680 1.00 25.16 ? 85  THR A CB  1 
ATOM   681  O OG1 . THR A 1 85  ? -2.023  49.892 -4.451 1.00 31.09 ? 85  THR A OG1 1 
ATOM   682  C CG2 . THR A 1 85  ? -4.336  50.426 -3.934 1.00 22.30 ? 85  THR A CG2 1 
ATOM   683  N N   . TYR A 1 86  ? -2.817  53.577 -2.057 1.00 22.77 ? 86  TYR A N   1 
ATOM   684  C CA  . TYR A 1 86  ? -3.540  54.294 -1.007 1.00 17.25 ? 86  TYR A CA  1 
ATOM   685  C C   . TYR A 1 86  ? -2.562  55.345 -0.504 1.00 16.38 ? 86  TYR A C   1 
ATOM   686  O O   . TYR A 1 86  ? -2.029  55.248 0.606  1.00 15.94 ? 86  TYR A O   1 
ATOM   687  C CB  . TYR A 1 86  ? -3.958  53.321 0.099  1.00 15.78 ? 86  TYR A CB  1 
ATOM   688  C CG  . TYR A 1 86  ? -5.165  53.701 0.922  1.00 18.45 ? 86  TYR A CG  1 
ATOM   689  C CD1 . TYR A 1 86  ? -5.489  55.020 1.164  1.00 18.15 ? 86  TYR A CD1 1 
ATOM   690  C CD2 . TYR A 1 86  ? -5.959  52.710 1.506  1.00 19.86 ? 86  TYR A CD2 1 
ATOM   691  C CE1 . TYR A 1 86  ? -6.606  55.349 1.938  1.00 26.73 ? 86  TYR A CE1 1 
ATOM   692  C CE2 . TYR A 1 86  ? -7.054  53.022 2.274  1.00 15.85 ? 86  TYR A CE2 1 
ATOM   693  C CZ  . TYR A 1 86  ? -7.381  54.337 2.491  1.00 22.97 ? 86  TYR A CZ  1 
ATOM   694  O OH  . TYR A 1 86  ? -8.479  54.641 3.262  1.00 21.06 ? 86  TYR A OH  1 
ATOM   695  N N   . PRO A 1 87  ? -2.289  56.367 -1.312 1.00 23.78 ? 87  PRO A N   1 
ATOM   696  C CA  . PRO A 1 87  ? -1.192  57.284 -0.987 1.00 23.80 ? 87  PRO A CA  1 
ATOM   697  C C   . PRO A 1 87  ? -1.518  58.204 0.175  1.00 17.46 ? 87  PRO A C   1 
ATOM   698  O O   . PRO A 1 87  ? -2.664  58.357 0.599  1.00 15.60 ? 87  PRO A O   1 
ATOM   699  C CB  . PRO A 1 87  ? -1.008  58.091 -2.275 1.00 17.12 ? 87  PRO A CB  1 
ATOM   700  C CG  . PRO A 1 87  ? -2.333  58.005 -2.938 1.00 20.09 ? 87  PRO A CG  1 
ATOM   701  C CD  . PRO A 1 87  ? -2.822  56.631 -2.660 1.00 23.22 ? 87  PRO A CD  1 
ATOM   702  N N   . TYR A 1 88  ? -0.459  58.803 0.700  1.00 15.81 ? 88  TYR A N   1 
ATOM   703  C CA  . TYR A 1 88  ? -0.565  59.625 1.888  1.00 15.83 ? 88  TYR A CA  1 
ATOM   704  C C   . TYR A 1 88  ? -1.077  61.013 1.535  1.00 19.32 ? 88  TYR A C   1 
ATOM   705  O O   . TYR A 1 88  ? -0.573  61.665 0.617  1.00 21.55 ? 88  TYR A O   1 
ATOM   706  C CB  . TYR A 1 88  ? 0.789   59.717 2.586  1.00 18.02 ? 88  TYR A CB  1 
ATOM   707  C CG  . TYR A 1 88  ? 0.742   60.483 3.887  1.00 20.14 ? 88  TYR A CG  1 
ATOM   708  C CD1 . TYR A 1 88  ? -0.030  60.043 4.958  1.00 19.71 ? 88  TYR A CD1 1 
ATOM   709  C CD2 . TYR A 1 88  ? 1.481   61.654 4.040  1.00 15.09 ? 88  TYR A CD2 1 
ATOM   710  C CE1 . TYR A 1 88  ? -0.076  60.755 6.152  1.00 21.43 ? 88  TYR A CE1 1 
ATOM   711  C CE2 . TYR A 1 88  ? 1.443   62.375 5.227  1.00 26.24 ? 88  TYR A CE2 1 
ATOM   712  C CZ  . TYR A 1 88  ? 0.665   61.916 6.283  1.00 23.90 ? 88  TYR A CZ  1 
ATOM   713  O OH  . TYR A 1 88  ? 0.622   62.623 7.465  1.00 19.17 ? 88  TYR A OH  1 
ATOM   714  N N   . GLU A 1 89  ? -2.105  61.442 2.248  1.00 18.85 ? 89  GLU A N   1 
ATOM   715  C CA  . GLU A 1 89  ? -2.738  62.714 1.982  1.00 25.09 ? 89  GLU A CA  1 
ATOM   716  C C   . GLU A 1 89  ? -2.589  63.690 3.133  1.00 27.28 ? 89  GLU A C   1 
ATOM   717  O O   . GLU A 1 89  ? -2.863  64.882 2.948  1.00 34.69 ? 89  GLU A O   1 
ATOM   718  C CB  . GLU A 1 89  ? -4.229  62.521 1.677  1.00 26.57 ? 89  GLU A CB  1 
ATOM   719  C CG  . GLU A 1 89  ? -4.502  61.510 0.569  1.00 21.67 ? 89  GLU A CG  1 
ATOM   720  C CD  . GLU A 1 89  ? -5.976  61.427 0.218  1.00 23.50 ? 89  GLU A CD  1 
ATOM   721  O OE1 . GLU A 1 89  ? -6.553  62.474 -0.158 1.00 24.33 ? 89  GLU A OE1 1 
ATOM   722  O OE2 . GLU A 1 89  ? -6.561  60.329 0.348  1.00 18.44 ? 89  GLU A OE2 1 
ATOM   723  N N   . GLY A 1 90  ? -2.137  63.233 4.301  1.00 24.10 ? 90  GLY A N   1 
ATOM   724  C CA  . GLY A 1 90  ? -1.896  64.145 5.395  1.00 29.87 ? 90  GLY A CA  1 
ATOM   725  C C   . GLY A 1 90  ? -3.163  64.619 6.057  1.00 29.79 ? 90  GLY A C   1 
ATOM   726  O O   . GLY A 1 90  ? -3.127  65.582 6.827  1.00 31.08 ? 90  GLY A O   1 
ATOM   727  N N   . VAL A 1 91  ? -4.278  63.938 5.814  1.00 25.98 ? 91  VAL A N   1 
ATOM   728  C CA  . VAL A 1 91  ? -5.563  64.276 6.408  1.00 24.91 ? 91  VAL A CA  1 
ATOM   729  C C   . VAL A 1 91  ? -6.375  62.998 6.526  1.00 24.21 ? 91  VAL A C   1 
ATOM   730  O O   . VAL A 1 91  ? -6.277  62.110 5.674  1.00 23.87 ? 91  VAL A O   1 
ATOM   731  C CB  . VAL A 1 91  ? -6.314  65.311 5.536  1.00 28.45 ? 91  VAL A CB  1 
ATOM   732  C CG1 . VAL A 1 91  ? -7.781  65.379 5.910  1.00 30.25 ? 91  VAL A CG1 1 
ATOM   733  C CG2 . VAL A 1 91  ? -5.700  66.692 5.669  1.00 40.61 ? 91  VAL A CG2 1 
ATOM   734  N N   . GLN A 1 92  ? -7.145  62.877 7.603  1.00 19.36 ? 92  GLN A N   1 
ATOM   735  C CA  . GLN A 1 92  ? -7.980  61.699 7.734  1.00 22.95 ? 92  GLN A CA  1 
ATOM   736  C C   . GLN A 1 92  ? -9.160  61.853 6.792  1.00 22.22 ? 92  GLN A C   1 
ATOM   737  O O   . GLN A 1 92  ? -9.766  62.923 6.698  1.00 29.81 ? 92  GLN A O   1 
ATOM   738  C CB  . GLN A 1 92  ? -8.486  61.494 9.165  1.00 20.06 ? 92  GLN A CB  1 
ATOM   739  C CG  . GLN A 1 92  ? -9.218  60.160 9.290  1.00 15.42 ? 92  GLN A CG  1 
ATOM   740  C CD  . GLN A 1 92  ? -9.825  59.911 10.642 1.00 18.89 ? 92  GLN A CD  1 
ATOM   741  O OE1 . GLN A 1 92  ? -10.505 60.774 11.206 1.00 23.55 ? 92  GLN A OE1 1 
ATOM   742  N NE2 . GLN A 1 92  ? -9.591  58.713 11.179 1.00 20.93 ? 92  GLN A NE2 1 
ATOM   743  N N   . ARG A 1 93  ? -9.467  60.787 6.079  1.00 20.77 ? 93  ARG A N   1 
ATOM   744  C CA  . ARG A 1 93  ? -10.590 60.736 5.162  1.00 26.24 ? 93  ARG A CA  1 
ATOM   745  C C   . ARG A 1 93  ? -11.380 59.479 5.482  1.00 25.23 ? 93  ARG A C   1 
ATOM   746  O O   . ARG A 1 93  ? -11.046 58.736 6.411  1.00 28.80 ? 93  ARG A O   1 
ATOM   747  C CB  . ARG A 1 93  ? -10.116 60.760 3.707  1.00 29.40 ? 93  ARG A CB  1 
ATOM   748  C CG  . ARG A 1 93  ? -9.381  62.043 3.330  1.00 22.81 ? 93  ARG A CG  1 
ATOM   749  C CD  . ARG A 1 93  ? -9.003  62.005 1.855  1.00 19.07 ? 93  ARG A CD  1 
ATOM   750  N NE  . ARG A 1 93  ? -10.177 61.947 0.992  1.00 21.07 ? 93  ARG A NE  1 
ATOM   751  C CZ  . ARG A 1 93  ? -10.127 61.905 -0.332 1.00 25.25 ? 93  ARG A CZ  1 
ATOM   752  N NH1 . ARG A 1 93  ? -8.972  61.900 -0.982 1.00 22.87 ? 93  ARG A NH1 1 
ATOM   753  N NH2 . ARG A 1 93  ? -11.263 61.903 -1.023 1.00 25.24 ? 93  ARG A NH2 1 
ATOM   754  N N   . TYR A 1 94  ? -12.414 59.218 4.694  1.00 28.06 ? 94  TYR A N   1 
ATOM   755  C CA  . TYR A 1 94  ? -13.161 57.986 4.880  1.00 36.23 ? 94  TYR A CA  1 
ATOM   756  C C   . TYR A 1 94  ? -12.242 56.798 4.628  1.00 30.26 ? 94  TYR A C   1 
ATOM   757  O O   . TYR A 1 94  ? -11.302 56.869 3.834  1.00 32.51 ? 94  TYR A O   1 
ATOM   758  C CB  . TYR A 1 94  ? -14.326 57.891 3.888  1.00 46.67 ? 94  TYR A CB  1 
ATOM   759  C CG  . TYR A 1 94  ? -15.288 59.052 3.897  1.00 65.35 ? 94  TYR A CG  1 
ATOM   760  C CD1 . TYR A 1 94  ? -15.785 59.575 5.090  1.00 67.91 ? 94  TYR A CD1 1 
ATOM   761  C CD2 . TYR A 1 94  ? -15.702 59.630 2.700  1.00 72.36 ? 94  TYR A CD2 1 
ATOM   762  C CE1 . TYR A 1 94  ? -16.669 60.648 5.087  1.00 59.27 ? 94  TYR A CE1 1 
ATOM   763  C CE2 . TYR A 1 94  ? -16.580 60.697 2.684  1.00 73.28 ? 94  TYR A CE2 1 
ATOM   764  C CZ  . TYR A 1 94  ? -17.061 61.204 3.879  1.00 71.56 ? 94  TYR A CZ  1 
ATOM   765  O OH  . TYR A 1 94  ? -17.936 62.267 3.859  1.00 65.69 ? 94  TYR A OH  1 
ATOM   766  N N   . CYS A 1 95  ? -12.514 55.704 5.319  1.00 25.00 ? 95  CYS A N   1 
ATOM   767  C CA  . CYS A 1 95  ? -11.795 54.465 5.072  1.00 27.53 ? 95  CYS A CA  1 
ATOM   768  C C   . CYS A 1 95  ? -12.124 53.923 3.687  1.00 25.28 ? 95  CYS A C   1 
ATOM   769  O O   . CYS A 1 95  ? -13.289 53.651 3.376  1.00 25.10 ? 95  CYS A O   1 
ATOM   770  C CB  . CYS A 1 95  ? -12.136 53.423 6.137  1.00 27.04 ? 95  CYS A CB  1 
ATOM   771  S SG  . CYS A 1 95  ? -11.239 51.868 5.904  1.00 28.87 ? 95  CYS A SG  1 
ATOM   772  N N   . ARG A 1 96  ? -11.096 53.778 2.854  1.00 27.40 ? 96  ARG A N   1 
ATOM   773  C CA  . ARG A 1 96  ? -11.253 53.366 1.469  1.00 22.45 ? 96  ARG A CA  1 
ATOM   774  C C   . ARG A 1 96  ? -10.601 52.018 1.206  1.00 31.38 ? 96  ARG A C   1 
ATOM   775  O O   . ARG A 1 96  ? -10.461 51.626 0.040  1.00 33.99 ? 96  ARG A O   1 
ATOM   776  C CB  . ARG A 1 96  ? -10.672 54.430 0.537  1.00 23.61 ? 96  ARG A CB  1 
ATOM   777  C CG  . ARG A 1 96  ? -11.441 55.730 0.592  1.00 29.27 ? 96  ARG A CG  1 
ATOM   778  C CD  . ARG A 1 96  ? -10.645 56.911 0.079  1.00 26.85 ? 96  ARG A CD  1 
ATOM   779  N NE  . ARG A 1 96  ? -9.747  57.424 1.105  1.00 23.64 ? 96  ARG A NE  1 
ATOM   780  C CZ  . ARG A 1 96  ? -8.720  58.226 0.864  1.00 22.85 ? 96  ARG A CZ  1 
ATOM   781  N NH1 . ARG A 1 96  ? -8.405  58.590 -0.368 1.00 19.66 ? 96  ARG A NH1 1 
ATOM   782  N NH2 . ARG A 1 96  ? -7.974  58.653 1.883  1.00 22.72 ? 96  ARG A NH2 1 
ATOM   783  N N   . SER A 1 97  ? -10.205 51.298 2.265  1.00 30.38 ? 97  SER A N   1 
ATOM   784  C CA  . SER A 1 97  ? -9.604  49.973 2.112  1.00 29.94 ? 97  SER A CA  1 
ATOM   785  C C   . SER A 1 97  ? -10.495 49.046 1.304  1.00 27.68 ? 97  SER A C   1 
ATOM   786  O O   . SER A 1 97  ? -10.009 48.226 0.517  1.00 32.12 ? 97  SER A O   1 
ATOM   787  C CB  . SER A 1 97  ? -9.348  49.360 3.483  1.00 28.89 ? 97  SER A CB  1 
ATOM   788  O OG  . SER A 1 97  ? -8.617  50.247 4.296  1.00 34.74 ? 97  SER A OG  1 
ATOM   789  N N   . ARG A 1 98  ? -11.807 49.145 1.507  1.00 32.84 ? 98  ARG A N   1 
ATOM   790  C CA  . ARG A 1 98  ? -12.736 48.357 0.711  1.00 35.11 ? 98  ARG A CA  1 
ATOM   791  C C   . ARG A 1 98  ? -12.574 48.675 -0.773 1.00 31.27 ? 98  ARG A C   1 
ATOM   792  O O   . ARG A 1 98  ? -12.474 47.768 -1.607 1.00 37.00 ? 98  ARG A O   1 
ATOM   793  C CB  . ARG A 1 98  ? -14.165 48.622 1.201  1.00 43.39 ? 98  ARG A CB  1 
ATOM   794  C CG  . ARG A 1 98  ? -15.229 47.578 0.823  1.00 49.63 ? 98  ARG A CG  1 
ATOM   795  C CD  . ARG A 1 98  ? -15.588 47.684 -0.649 1.00 65.66 ? 98  ARG A CD  1 
ATOM   796  N NE  . ARG A 1 98  ? -16.783 46.946 -1.039 1.00 70.43 ? 98  ARG A NE  1 
ATOM   797  C CZ  . ARG A 1 98  ? -17.959 47.514 -1.273 1.00 67.45 ? 98  ARG A CZ  1 
ATOM   798  N NH1 . ARG A 1 98  ? -18.147 48.811 -1.092 1.00 49.21 ? 98  ARG A NH1 1 
ATOM   799  N NH2 . ARG A 1 98  ? -18.969 46.762 -1.701 1.00 65.26 ? 98  ARG A NH2 1 
ATOM   800  N N   . GLU A 1 99  ? -12.508 49.961 -1.117 1.00 36.66 ? 99  GLU A N   1 
ATOM   801  C CA  . GLU A 1 99  ? -12.556 50.388 -2.509 1.00 31.88 ? 99  GLU A CA  1 
ATOM   802  C C   . GLU A 1 99  ? -11.248 50.198 -3.263 1.00 32.68 ? 99  GLU A C   1 
ATOM   803  O O   . GLU A 1 99  ? -11.192 50.520 -4.453 1.00 42.59 ? 99  GLU A O   1 
ATOM   804  C CB  . GLU A 1 99  ? -12.879 51.879 -2.580 1.00 31.05 ? 99  GLU A CB  1 
ATOM   805  C CG  . GLU A 1 99  ? -14.217 52.274 -2.048 1.00 43.69 ? 99  GLU A CG  1 
ATOM   806  C CD  . GLU A 1 99  ? -14.499 53.730 -2.358 1.00 44.97 ? 99  GLU A CD  1 
ATOM   807  O OE1 . GLU A 1 99  ? -13.933 54.593 -1.658 1.00 39.15 ? 99  GLU A OE1 1 
ATOM   808  O OE2 . GLU A 1 99  ? -15.252 54.010 -3.326 1.00 37.36 ? 99  GLU A OE2 1 
ATOM   809  N N   . LYS A 1 100 ? -10.183 49.712 -2.632 1.00 31.19 ? 100 LYS A N   1 
ATOM   810  C CA  . LYS A 1 100 ? -8.917  49.586 -3.340 1.00 23.89 ? 100 LYS A CA  1 
ATOM   811  C C   . LYS A 1 100 ? -8.541  48.142 -3.606 1.00 29.75 ? 100 LYS A C   1 
ATOM   812  O O   . LYS A 1 100 ? -7.371  47.843 -3.853 1.00 30.40 ? 100 LYS A O   1 
ATOM   813  C CB  . LYS A 1 100 ? -7.792  50.352 -2.640 1.00 27.88 ? 100 LYS A CB  1 
ATOM   814  C CG  . LYS A 1 100 ? -7.963  51.856 -2.811 1.00 21.37 ? 100 LYS A CG  1 
ATOM   815  C CD  . LYS A 1 100 ? -7.925  52.688 -1.558 1.00 32.45 ? 100 LYS A CD  1 
ATOM   816  C CE  . LYS A 1 100 ? -8.207  54.136 -1.914 1.00 22.01 ? 100 LYS A CE  1 
ATOM   817  N NZ  . LYS A 1 100 ? -6.996  54.796 -2.456 1.00 24.25 ? 100 LYS A NZ  1 
ATOM   818  N N   . GLY A 1 101 ? -9.513  47.239 -3.584 1.00 33.62 ? 101 GLY A N   1 
ATOM   819  C CA  . GLY A 1 101 ? -9.233  45.884 -3.963 1.00 33.80 ? 101 GLY A CA  1 
ATOM   820  C C   . GLY A 1 101 ? -8.606  45.132 -2.823 1.00 35.58 ? 101 GLY A C   1 
ATOM   821  O O   . GLY A 1 101 ? -8.536  45.612 -1.688 1.00 30.07 ? 101 GLY A O   1 
ATOM   822  N N   . PRO A 1 102 ? -8.153  43.918 -3.108 1.00 39.88 ? 102 PRO A N   1 
ATOM   823  C CA  . PRO A 1 102 ? -7.578  43.085 -2.052 1.00 34.59 ? 102 PRO A CA  1 
ATOM   824  C C   . PRO A 1 102 ? -6.340  43.743 -1.462 1.00 34.74 ? 102 PRO A C   1 
ATOM   825  O O   . PRO A 1 102 ? -5.643  44.522 -2.119 1.00 35.51 ? 102 PRO A O   1 
ATOM   826  C CB  . PRO A 1 102 ? -7.239  41.771 -2.774 1.00 34.88 ? 102 PRO A CB  1 
ATOM   827  C CG  . PRO A 1 102 ? -7.302  42.096 -4.257 1.00 30.75 ? 102 PRO A CG  1 
ATOM   828  C CD  . PRO A 1 102 ? -8.291  43.201 -4.388 1.00 35.72 ? 102 PRO A CD  1 
ATOM   829  N N   . TYR A 1 103 ? -6.108  43.453 -0.185 1.00 27.62 ? 103 TYR A N   1 
ATOM   830  C CA  . TYR A 1 103 ? -4.922  43.921 0.516  1.00 26.23 ? 103 TYR A CA  1 
ATOM   831  C C   . TYR A 1 103 ? -3.648  43.410 -0.145 1.00 27.02 ? 103 TYR A C   1 
ATOM   832  O O   . TYR A 1 103 ? -3.639  42.381 -0.827 1.00 26.48 ? 103 TYR A O   1 
ATOM   833  C CB  . TYR A 1 103 ? -4.974  43.495 1.981  1.00 27.25 ? 103 TYR A CB  1 
ATOM   834  C CG  . TYR A 1 103 ? -6.025  44.257 2.751  1.00 37.61 ? 103 TYR A CG  1 
ATOM   835  C CD1 . TYR A 1 103 ? -5.888  45.625 2.987  1.00 36.40 ? 103 TYR A CD1 1 
ATOM   836  C CD2 . TYR A 1 103 ? -7.168  43.621 3.228  1.00 42.62 ? 103 TYR A CD2 1 
ATOM   837  C CE1 . TYR A 1 103 ? -6.854  46.338 3.688  1.00 29.70 ? 103 TYR A CE1 1 
ATOM   838  C CE2 . TYR A 1 103 ? -8.143  44.326 3.929  1.00 39.54 ? 103 TYR A CE2 1 
ATOM   839  C CZ  . TYR A 1 103 ? -7.977  45.685 4.155  1.00 38.92 ? 103 TYR A CZ  1 
ATOM   840  O OH  . TYR A 1 103 ? -8.935  46.387 4.849  1.00 36.06 ? 103 TYR A OH  1 
ATOM   841  N N   . ALA A 1 104 ? -2.567  44.164 0.048  1.00 26.28 ? 104 ALA A N   1 
ATOM   842  C CA  . ALA A 1 104 ? -1.262  43.798 -0.488 1.00 24.33 ? 104 ALA A CA  1 
ATOM   843  C C   . ALA A 1 104 ? -0.497  42.894 0.457  1.00 29.06 ? 104 ALA A C   1 
ATOM   844  O O   . ALA A 1 104 ? 0.261   42.025 0.005  1.00 26.36 ? 104 ALA A O   1 
ATOM   845  C CB  . ALA A 1 104 ? -0.428  45.052 -0.754 1.00 21.99 ? 104 ALA A CB  1 
ATOM   846  N N   . ALA A 1 105 ? -0.670  43.093 1.759  1.00 24.11 ? 105 ALA A N   1 
ATOM   847  C CA  . ALA A 1 105 ? 0.022   42.311 2.765  1.00 20.91 ? 105 ALA A CA  1 
ATOM   848  C C   . ALA A 1 105 ? -0.888  42.196 3.972  1.00 24.29 ? 105 ALA A C   1 
ATOM   849  O O   . ALA A 1 105 ? -1.801  43.001 4.169  1.00 28.66 ? 105 ALA A O   1 
ATOM   850  C CB  . ALA A 1 105 ? 1.365   42.935 3.158  1.00 26.06 ? 105 ALA A CB  1 
ATOM   851  N N   . LYS A 1 106 ? -0.648  41.170 4.770  1.00 19.99 ? 106 LYS A N   1 
ATOM   852  C CA  . LYS A 1 106 ? -1.414  40.987 5.987  1.00 26.43 ? 106 LYS A CA  1 
ATOM   853  C C   . LYS A 1 106 ? -0.457  40.341 6.978  1.00 27.35 ? 106 LYS A C   1 
ATOM   854  O O   . LYS A 1 106 ? 0.347   39.488 6.600  1.00 31.81 ? 106 LYS A O   1 
ATOM   855  C CB  . LYS A 1 106 ? -2.677  40.138 5.745  1.00 26.96 ? 106 LYS A CB  1 
ATOM   856  C CG  . LYS A 1 106 ? -3.565  40.019 6.972  1.00 33.14 ? 106 LYS A CG  1 
ATOM   857  C CD  . LYS A 1 106 ? -4.775  39.131 6.779  1.00 25.35 ? 106 LYS A CD  1 
ATOM   858  C CE  . LYS A 1 106 ? -4.622  37.865 7.609  1.00 32.86 ? 106 LYS A CE  1 
ATOM   859  N NZ  . LYS A 1 106 ? -4.625  38.170 9.071  1.00 26.53 ? 106 LYS A NZ  1 
ATOM   860  N N   . THR A 1 107 ? -0.553  40.718 8.235  1.00 23.45 ? 107 THR A N   1 
ATOM   861  C CA  . THR A 1 107 ? 0.296   40.125 9.248  1.00 26.97 ? 107 THR A CA  1 
ATOM   862  C C   . THR A 1 107 ? -0.556  39.185 10.083 1.00 31.68 ? 107 THR A C   1 
ATOM   863  O O   . THR A 1 107 ? -1.756  39.024 9.848  1.00 31.41 ? 107 THR A O   1 
ATOM   864  C CB  . THR A 1 107 ? 0.974   41.203 10.106 1.00 28.18 ? 107 THR A CB  1 
ATOM   865  O OG1 . THR A 1 107 ? -0.014  42.082 10.657 1.00 27.71 ? 107 THR A OG1 1 
ATOM   866  C CG2 . THR A 1 107 ? 1.959   42.025 9.276  1.00 24.00 ? 107 THR A CG2 1 
ATOM   867  N N   . ASP A 1 108 ? 0.065   38.566 11.076 1.00 27.59 ? 108 ASP A N   1 
ATOM   868  C CA  . ASP A 1 108 ? -0.605  37.538 11.851 1.00 28.36 ? 108 ASP A CA  1 
ATOM   869  C C   . ASP A 1 108 ? -0.837  37.948 13.288 1.00 28.18 ? 108 ASP A C   1 
ATOM   870  O O   . ASP A 1 108 ? -1.500  37.215 14.031 1.00 38.56 ? 108 ASP A O   1 
ATOM   871  C CB  . ASP A 1 108 ? 0.198   36.235 11.787 1.00 35.35 ? 108 ASP A CB  1 
ATOM   872  C CG  . ASP A 1 108 ? 0.304   35.698 10.361 1.00 42.09 ? 108 ASP A CG  1 
ATOM   873  O OD1 . ASP A 1 108 ? -0.752  35.471 9.734  1.00 37.62 ? 108 ASP A OD1 1 
ATOM   874  O OD2 . ASP A 1 108 ? 1.437   35.525 9.857  1.00 41.51 ? 108 ASP A OD2 1 
ATOM   875  N N   . GLY A 1 109 ? -0.331  39.101 13.702 1.00 25.21 ? 109 GLY A N   1 
ATOM   876  C CA  . GLY A 1 109 ? -0.608  39.543 15.049 1.00 24.94 ? 109 GLY A CA  1 
ATOM   877  C C   . GLY A 1 109 ? 0.280   40.707 15.432 1.00 24.06 ? 109 GLY A C   1 
ATOM   878  O O   . GLY A 1 109 ? 1.008   41.260 14.607 1.00 25.88 ? 109 GLY A O   1 
ATOM   879  N N   . VAL A 1 110 ? 0.254   41.010 16.724 1.00 17.32 ? 110 VAL A N   1 
ATOM   880  C CA  . VAL A 1 110 ? 0.979   42.134 17.291 1.00 18.76 ? 110 VAL A CA  1 
ATOM   881  C C   . VAL A 1 110 ? 1.506   41.682 18.630 1.00 16.76 ? 110 VAL A C   1 
ATOM   882  O O   . VAL A 1 110 ? 0.764   41.101 19.429 1.00 20.52 ? 110 VAL A O   1 
ATOM   883  C CB  . VAL A 1 110 ? 0.086   43.373 17.506 1.00 17.29 ? 110 VAL A CB  1 
ATOM   884  C CG1 . VAL A 1 110 ? 0.933   44.574 17.961 1.00 12.67 ? 110 VAL A CG1 1 
ATOM   885  C CG2 . VAL A 1 110 ? -0.711  43.690 16.278 1.00 23.94 ? 110 VAL A CG2 1 
ATOM   886  N N   . ARG A 1 111 ? 2.787   41.911 18.868 1.00 20.79 ? 111 ARG A N   1 
ATOM   887  C CA  . ARG A 1 111 ? 3.358   41.627 20.172 1.00 27.45 ? 111 ARG A CA  1 
ATOM   888  C C   . ARG A 1 111 ? 3.957   42.902 20.733 1.00 20.50 ? 111 ARG A C   1 
ATOM   889  O O   . ARG A 1 111 ? 4.393   43.793 19.992 1.00 24.80 ? 111 ARG A O   1 
ATOM   890  C CB  . ARG A 1 111 ? 4.404   40.516 20.111 1.00 24.84 ? 111 ARG A CB  1 
ATOM   891  C CG  . ARG A 1 111 ? 3.800   39.171 19.769 1.00 25.85 ? 111 ARG A CG  1 
ATOM   892  C CD  . ARG A 1 111 ? 4.828   38.050 19.799 1.00 48.61 ? 111 ARG A CD  1 
ATOM   893  N NE  . ARG A 1 111 ? 4.749   37.234 21.008 1.00 58.24 ? 111 ARG A NE  1 
ATOM   894  C CZ  . ARG A 1 111 ? 5.668   37.213 21.967 1.00 68.16 ? 111 ARG A CZ  1 
ATOM   895  N NH1 . ARG A 1 111 ? 6.752   37.971 21.901 1.00 59.71 ? 111 ARG A NH1 1 
ATOM   896  N NH2 . ARG A 1 111 ? 5.498   36.405 23.014 1.00 43.33 ? 111 ARG A NH2 1 
ATOM   897  N N   . GLN A 1 112 ? 3.920   42.999 22.047 1.00 23.05 ? 112 GLN A N   1 
ATOM   898  C CA  . GLN A 1 112 ? 4.453   44.148 22.743 1.00 17.83 ? 112 GLN A CA  1 
ATOM   899  C C   . GLN A 1 112 ? 5.786   43.766 23.342 1.00 19.54 ? 112 GLN A C   1 
ATOM   900  O O   . GLN A 1 112 ? 5.930   42.689 23.927 1.00 29.25 ? 112 GLN A O   1 
ATOM   901  C CB  . GLN A 1 112 ? 3.511   44.630 23.843 1.00 16.73 ? 112 GLN A CB  1 
ATOM   902  C CG  . GLN A 1 112 ? 3.993   45.925 24.466 1.00 25.82 ? 112 GLN A CG  1 
ATOM   903  C CD  . GLN A 1 112 ? 3.036   46.468 25.489 1.00 24.39 ? 112 GLN A CD  1 
ATOM   904  O OE1 . GLN A 1 112 ? 1.973   45.896 25.719 1.00 25.13 ? 112 GLN A OE1 1 
ATOM   905  N NE2 . GLN A 1 112 ? 3.409   47.582 26.121 1.00 24.83 ? 112 GLN A NE2 1 
ATOM   906  N N   . VAL A 1 113 ? 6.760   44.655 23.204 1.00 22.69 ? 113 VAL A N   1 
ATOM   907  C CA  . VAL A 1 113 ? 7.985   44.480 23.955 1.00 19.41 ? 113 VAL A CA  1 
ATOM   908  C C   . VAL A 1 113 ? 7.685   44.771 25.416 1.00 25.35 ? 113 VAL A C   1 
ATOM   909  O O   . VAL A 1 113 ? 6.913   45.686 25.740 1.00 21.97 ? 113 VAL A O   1 
ATOM   910  C CB  . VAL A 1 113 ? 9.084   45.401 23.409 1.00 18.18 ? 113 VAL A CB  1 
ATOM   911  C CG1 . VAL A 1 113 ? 10.383  45.136 24.143 1.00 18.49 ? 113 VAL A CG1 1 
ATOM   912  C CG2 . VAL A 1 113 ? 9.211   45.234 21.899 1.00 15.55 ? 113 VAL A CG2 1 
ATOM   913  N N   . GLN A 1 114 ? 8.242   43.961 26.300 1.00 21.18 ? 114 GLN A N   1 
ATOM   914  C CA  . GLN A 1 114 ? 8.167   44.238 27.720 1.00 23.25 ? 114 GLN A CA  1 
ATOM   915  C C   . GLN A 1 114 ? 8.654   45.665 27.984 1.00 22.91 ? 114 GLN A C   1 
ATOM   916  O O   . GLN A 1 114 ? 9.824   45.970 27.715 1.00 23.87 ? 114 GLN A O   1 
ATOM   917  C CB  . GLN A 1 114 ? 9.017   43.227 28.478 1.00 28.36 ? 114 GLN A CB  1 
ATOM   918  C CG  . GLN A 1 114 ? 9.413   43.698 29.846 1.00 43.00 ? 114 GLN A CG  1 
ATOM   919  C CD  . GLN A 1 114 ? 8.443   43.247 30.899 1.00 50.44 ? 114 GLN A CD  1 
ATOM   920  O OE1 . GLN A 1 114 ? 7.297   43.703 30.959 1.00 43.76 ? 114 GLN A OE1 1 
ATOM   921  N NE2 . GLN A 1 114 ? 8.896   42.336 31.746 1.00 61.04 ? 114 GLN A NE2 1 
ATOM   922  N N   . PRO A 1 115 ? 7.794   46.565 28.455 1.00 27.59 ? 115 PRO A N   1 
ATOM   923  C CA  . PRO A 1 115 ? 8.196   47.970 28.565 1.00 27.60 ? 115 PRO A CA  1 
ATOM   924  C C   . PRO A 1 115 ? 9.275   48.177 29.612 1.00 26.17 ? 115 PRO A C   1 
ATOM   925  O O   . PRO A 1 115 ? 9.478   47.363 30.516 1.00 27.53 ? 115 PRO A O   1 
ATOM   926  C CB  . PRO A 1 115 ? 6.898   48.687 28.956 1.00 26.15 ? 115 PRO A CB  1 
ATOM   927  C CG  . PRO A 1 115 ? 6.047   47.633 29.552 1.00 28.08 ? 115 PRO A CG  1 
ATOM   928  C CD  . PRO A 1 115 ? 6.403   46.344 28.886 1.00 24.69 ? 115 PRO A CD  1 
ATOM   929  N N   . TYR A 1 116 ? 9.973   49.302 29.467 1.00 23.73 ? 116 TYR A N   1 
ATOM   930  C CA  . TYR A 1 116 ? 10.956  49.754 30.449 1.00 27.26 ? 116 TYR A CA  1 
ATOM   931  C C   . TYR A 1 116 ? 12.065  48.728 30.612 1.00 20.17 ? 116 TYR A C   1 
ATOM   932  O O   . TYR A 1 116 ? 12.557  48.479 31.713 1.00 29.35 ? 116 TYR A O   1 
ATOM   933  C CB  . TYR A 1 116 ? 10.300  50.085 31.787 1.00 22.17 ? 116 TYR A CB  1 
ATOM   934  C CG  . TYR A 1 116 ? 9.134   51.002 31.610 1.00 28.60 ? 116 TYR A CG  1 
ATOM   935  C CD1 . TYR A 1 116 ? 9.324   52.265 31.077 1.00 22.76 ? 116 TYR A CD1 1 
ATOM   936  C CD2 . TYR A 1 116 ? 7.854   50.640 32.018 1.00 33.28 ? 116 TYR A CD2 1 
ATOM   937  C CE1 . TYR A 1 116 ? 8.268   53.142 30.910 1.00 30.76 ? 116 TYR A CE1 1 
ATOM   938  C CE2 . TYR A 1 116 ? 6.779   51.524 31.863 1.00 27.71 ? 116 TYR A CE2 1 
ATOM   939  C CZ  . TYR A 1 116 ? 7.001   52.773 31.304 1.00 22.55 ? 116 TYR A CZ  1 
ATOM   940  O OH  . TYR A 1 116 ? 5.971   53.672 31.127 1.00 31.78 ? 116 TYR A OH  1 
ATOM   941  N N   . ASN A 1 117 ? 12.467  48.143 29.494 1.00 18.79 ? 117 ASN A N   1 
ATOM   942  C CA  . ASN A 1 117 ? 13.420  47.045 29.491 1.00 20.06 ? 117 ASN A CA  1 
ATOM   943  C C   . ASN A 1 117 ? 14.229  47.198 28.212 1.00 21.11 ? 117 ASN A C   1 
ATOM   944  O O   . ASN A 1 117 ? 13.759  46.816 27.136 1.00 23.64 ? 117 ASN A O   1 
ATOM   945  C CB  . ASN A 1 117 ? 12.688  45.713 29.543 1.00 22.02 ? 117 ASN A CB  1 
ATOM   946  C CG  . ASN A 1 117 ? 13.614  44.533 29.660 1.00 21.70 ? 117 ASN A CG  1 
ATOM   947  O OD1 . ASN A 1 117 ? 14.716  44.527 29.115 1.00 22.58 ? 117 ASN A OD1 1 
ATOM   948  N ND2 . ASN A 1 117 ? 13.156  43.502 30.355 1.00 23.88 ? 117 ASN A ND2 1 
ATOM   949  N N   . GLU A 1 118 ? 15.448  47.719 28.341 1.00 17.39 ? 118 GLU A N   1 
ATOM   950  C CA  . GLU A 1 118 ? 16.245  48.007 27.155 1.00 20.45 ? 118 GLU A CA  1 
ATOM   951  C C   . GLU A 1 118 ? 16.552  46.733 26.377 1.00 17.04 ? 118 GLU A C   1 
ATOM   952  O O   . GLU A 1 118 ? 16.330  46.660 25.162 1.00 21.11 ? 118 GLU A O   1 
ATOM   953  C CB  . GLU A 1 118 ? 17.532  48.721 27.555 1.00 20.61 ? 118 GLU A CB  1 
ATOM   954  C CG  . GLU A 1 118 ? 18.462  49.003 26.394 1.00 26.58 ? 118 GLU A CG  1 
ATOM   955  C CD  . GLU A 1 118 ? 19.620  49.913 26.785 1.00 29.99 ? 118 GLU A CD  1 
ATOM   956  O OE1 . GLU A 1 118 ? 19.356  51.027 27.297 1.00 25.26 ? 118 GLU A OE1 1 
ATOM   957  O OE2 . GLU A 1 118 ? 20.793  49.504 26.587 1.00 18.16 ? 118 GLU A OE2 1 
ATOM   958  N N   . GLY A 1 119 ? 17.005  45.694 27.073 1.00 23.39 ? 119 GLY A N   1 
ATOM   959  C CA  . GLY A 1 119 ? 17.378  44.472 26.383 1.00 18.53 ? 119 GLY A CA  1 
ATOM   960  C C   . GLY A 1 119 ? 16.218  43.834 25.649 1.00 16.48 ? 119 GLY A C   1 
ATOM   961  O O   . GLY A 1 119 ? 16.385  43.309 24.546 1.00 17.97 ? 119 GLY A O   1 
ATOM   962  N N   . ALA A 1 120 ? 15.017  43.918 26.219 1.00 20.48 ? 120 ALA A N   1 
ATOM   963  C CA  . ALA A 1 120 ? 13.865  43.347 25.534 1.00 18.39 ? 120 ALA A CA  1 
ATOM   964  C C   . ALA A 1 120 ? 13.636  44.072 24.219 1.00 19.85 ? 120 ALA A C   1 
ATOM   965  O O   . ALA A 1 120 ? 13.313  43.452 23.199 1.00 22.13 ? 120 ALA A O   1 
ATOM   966  C CB  . ALA A 1 120 ? 12.626  43.428 26.428 1.00 24.70 ? 120 ALA A CB  1 
ATOM   967  N N   . LEU A 1 121 ? 13.810  45.390 24.225 1.00 17.81 ? 121 LEU A N   1 
ATOM   968  C CA  . LEU A 1 121 ? 13.646  46.155 23.003 1.00 17.82 ? 121 LEU A CA  1 
ATOM   969  C C   . LEU A 1 121 ? 14.763  45.853 22.017 1.00 22.39 ? 121 LEU A C   1 
ATOM   970  O O   . LEU A 1 121 ? 14.505  45.693 20.817 1.00 23.11 ? 121 LEU A O   1 
ATOM   971  C CB  . LEU A 1 121 ? 13.600  47.648 23.330 1.00 18.89 ? 121 LEU A CB  1 
ATOM   972  C CG  . LEU A 1 121 ? 13.530  48.571 22.121 1.00 17.86 ? 121 LEU A CG  1 
ATOM   973  C CD1 . LEU A 1 121 ? 12.280  48.268 21.317 1.00 14.71 ? 121 LEU A CD1 1 
ATOM   974  C CD2 . LEU A 1 121 ? 13.566  50.016 22.572 1.00 14.51 ? 121 LEU A CD2 1 
ATOM   975  N N   . LEU A 1 122 ? 16.012  45.765 22.498 1.00 18.34 ? 122 LEU A N   1 
ATOM   976  C CA  . LEU A 1 122 ? 17.114  45.411 21.603 1.00 15.84 ? 122 LEU A CA  1 
ATOM   977  C C   . LEU A 1 122 ? 16.898  44.044 20.978 1.00 19.52 ? 122 LEU A C   1 
ATOM   978  O O   . LEU A 1 122 ? 17.221  43.832 19.801 1.00 19.87 ? 122 LEU A O   1 
ATOM   979  C CB  . LEU A 1 122 ? 18.457  45.441 22.329 1.00 15.95 ? 122 LEU A CB  1 
ATOM   980  C CG  . LEU A 1 122 ? 18.887  46.769 22.935 1.00 21.46 ? 122 LEU A CG  1 
ATOM   981  C CD1 . LEU A 1 122 ? 20.211  46.599 23.670 1.00 18.19 ? 122 LEU A CD1 1 
ATOM   982  C CD2 . LEU A 1 122 ? 18.935  47.865 21.886 1.00 20.79 ? 122 LEU A CD2 1 
ATOM   983  N N   . TYR A 1 123 ? 16.419  43.083 21.772 1.00 16.81 ? 123 TYR A N   1 
ATOM   984  C CA  . TYR A 1 123 ? 16.146  41.755 21.240 1.00 16.88 ? 123 TYR A CA  1 
ATOM   985  C C   . TYR A 1 123 ? 15.114  41.822 20.115 1.00 16.95 ? 123 TYR A C   1 
ATOM   986  O O   . TYR A 1 123 ? 15.236  41.116 19.107 1.00 21.69 ? 123 TYR A O   1 
ATOM   987  C CB  . TYR A 1 123 ? 15.677  40.827 22.367 1.00 18.17 ? 123 TYR A CB  1 
ATOM   988  C CG  . TYR A 1 123 ? 15.413  39.408 21.918 1.00 26.67 ? 123 TYR A CG  1 
ATOM   989  C CD1 . TYR A 1 123 ? 16.476  38.547 21.642 1.00 31.32 ? 123 TYR A CD1 1 
ATOM   990  C CD2 . TYR A 1 123 ? 14.117  38.921 21.762 1.00 27.34 ? 123 TYR A CD2 1 
ATOM   991  C CE1 . TYR A 1 123 ? 16.259  37.242 21.229 1.00 26.69 ? 123 TYR A CE1 1 
ATOM   992  C CE2 . TYR A 1 123 ? 13.891  37.604 21.344 1.00 25.89 ? 123 TYR A CE2 1 
ATOM   993  C CZ  . TYR A 1 123 ? 14.970  36.777 21.081 1.00 32.47 ? 123 TYR A CZ  1 
ATOM   994  O OH  . TYR A 1 123 ? 14.767  35.479 20.668 1.00 40.65 ? 123 TYR A OH  1 
ATOM   995  N N   . SER A 1 124 ? 14.080  42.656 20.277 1.00 13.16 ? 124 SER A N   1 
ATOM   996  C CA  . SER A 1 124 ? 13.067  42.784 19.231 1.00 15.38 ? 124 SER A CA  1 
ATOM   997  C C   . SER A 1 124 ? 13.629  43.486 18.005 1.00 17.85 ? 124 SER A C   1 
ATOM   998  O O   . SER A 1 124 ? 13.264  43.150 16.874 1.00 23.56 ? 124 SER A O   1 
ATOM   999  C CB  . SER A 1 124 ? 11.840  43.531 19.754 1.00 16.50 ? 124 SER A CB  1 
ATOM   1000 O OG  . SER A 1 124 ? 11.139  42.751 20.719 1.00 27.04 ? 124 SER A OG  1 
ATOM   1001 N N   . ILE A 1 125 ? 14.518  44.464 18.205 1.00 18.74 ? 125 ILE A N   1 
ATOM   1002 C CA  . ILE A 1 125 ? 15.147  45.120 17.061 1.00 25.10 ? 125 ILE A CA  1 
ATOM   1003 C C   . ILE A 1 125 ? 16.078  44.166 16.328 1.00 21.32 ? 125 ILE A C   1 
ATOM   1004 O O   . ILE A 1 125 ? 16.203  44.229 15.098 1.00 29.57 ? 125 ILE A O   1 
ATOM   1005 C CB  . ILE A 1 125 ? 15.902  46.396 17.488 1.00 17.18 ? 125 ILE A CB  1 
ATOM   1006 C CG1 . ILE A 1 125 ? 14.955  47.422 18.105 1.00 16.73 ? 125 ILE A CG1 1 
ATOM   1007 C CG2 . ILE A 1 125 ? 16.664  46.981 16.320 1.00 14.75 ? 125 ILE A CG2 1 
ATOM   1008 C CD1 . ILE A 1 125 ? 15.686  48.538 18.811 1.00 18.90 ? 125 ILE A CD1 1 
ATOM   1009 N N   . ALA A 1 126 ? 16.742  43.270 17.049 1.00 17.71 ? 126 ALA A N   1 
ATOM   1010 C CA  . ALA A 1 126 ? 17.575  42.298 16.363 1.00 19.35 ? 126 ALA A CA  1 
ATOM   1011 C C   . ALA A 1 126 ? 16.752  41.436 15.417 1.00 22.64 ? 126 ALA A C   1 
ATOM   1012 O O   . ALA A 1 126 ? 17.262  40.992 14.382 1.00 25.92 ? 126 ALA A O   1 
ATOM   1013 C CB  . ALA A 1 126 ? 18.328  41.449 17.388 1.00 14.16 ? 126 ALA A CB  1 
ATOM   1014 N N   . ASN A 1 127 ? 15.475  41.223 15.722 1.00 17.04 ? 127 ASN A N   1 
ATOM   1015 C CA  . ASN A 1 127 ? 14.650  40.369 14.882 1.00 19.89 ? 127 ASN A CA  1 
ATOM   1016 C C   . ASN A 1 127 ? 13.888  41.139 13.808 1.00 28.58 ? 127 ASN A C   1 
ATOM   1017 O O   . ASN A 1 127 ? 13.547  40.555 12.770 1.00 27.63 ? 127 ASN A O   1 
ATOM   1018 C CB  . ASN A 1 127 ? 13.651  39.581 15.739 1.00 24.70 ? 127 ASN A CB  1 
ATOM   1019 C CG  . ASN A 1 127 ? 14.327  38.725 16.814 1.00 39.24 ? 127 ASN A CG  1 
ATOM   1020 O OD1 . ASN A 1 127 ? 15.471  38.969 17.217 1.00 34.61 ? 127 ASN A OD1 1 
ATOM   1021 N ND2 . ASN A 1 127 ? 13.608  37.713 17.283 1.00 40.55 ? 127 ASN A ND2 1 
ATOM   1022 N N   . GLN A 1 128 ? 13.635  42.439 14.012 1.00 25.55 ? 128 GLN A N   1 
ATOM   1023 C CA  . GLN A 1 128 ? 12.783  43.193 13.094 1.00 21.32 ? 128 GLN A CA  1 
ATOM   1024 C C   . GLN A 1 128 ? 12.661  44.640 13.547 1.00 21.76 ? 128 GLN A C   1 
ATOM   1025 O O   . GLN A 1 128 ? 13.013  44.970 14.681 1.00 20.69 ? 128 GLN A O   1 
ATOM   1026 C CB  . GLN A 1 128 ? 11.384  42.606 13.012 1.00 16.14 ? 128 GLN A CB  1 
ATOM   1027 C CG  . GLN A 1 128 ? 10.641  42.800 14.297 1.00 23.44 ? 128 GLN A CG  1 
ATOM   1028 C CD  . GLN A 1 128 ? 9.460   41.902 14.400 1.00 16.41 ? 128 GLN A CD  1 
ATOM   1029 O OE1 . GLN A 1 128 ? 9.503   40.908 15.117 1.00 19.61 ? 128 GLN A OE1 1 
ATOM   1030 N NE2 . GLN A 1 128 ? 8.397   42.224 13.673 1.00 20.28 ? 128 GLN A NE2 1 
ATOM   1031 N N   . PRO A 1 129 ? 12.245  45.535 12.659 1.00 24.53 ? 129 PRO A N   1 
ATOM   1032 C CA  . PRO A 1 129 ? 11.911  46.897 13.068 1.00 19.19 ? 129 PRO A CA  1 
ATOM   1033 C C   . PRO A 1 129 ? 10.776  46.884 14.080 1.00 16.48 ? 129 PRO A C   1 
ATOM   1034 O O   . PRO A 1 129 ? 9.873   46.044 14.016 1.00 18.10 ? 129 PRO A O   1 
ATOM   1035 C CB  . PRO A 1 129 ? 11.419  47.512 11.745 1.00 19.48 ? 129 PRO A CB  1 
ATOM   1036 C CG  . PRO A 1 129 ? 11.916  46.404 10.653 1.00 26.86 ? 129 PRO A CG  1 
ATOM   1037 C CD  . PRO A 1 129 ? 12.958  45.708 11.379 1.00 25.80 ? 129 PRO A CD  1 
ATOM   1038 N N   . VAL A 1 130 ? 10.820  47.815 15.026 1.00 13.65 ? 130 VAL A N   1 
ATOM   1039 C CA  . VAL A 1 130 ? 9.884   47.814 16.142 1.00 17.76 ? 130 VAL A CA  1 
ATOM   1040 C C   . VAL A 1 130 ? 9.216   49.182 16.201 1.00 12.86 ? 130 VAL A C   1 
ATOM   1041 O O   . VAL A 1 130 ? 9.873   50.213 16.039 1.00 12.55 ? 130 VAL A O   1 
ATOM   1042 C CB  . VAL A 1 130 ? 10.617  47.496 17.463 1.00 17.09 ? 130 VAL A CB  1 
ATOM   1043 C CG1 . VAL A 1 130 ? 9.684   47.575 18.668 1.00 20.43 ? 130 VAL A CG1 1 
ATOM   1044 C CG2 . VAL A 1 130 ? 11.291  46.123 17.364 1.00 18.13 ? 130 VAL A CG2 1 
ATOM   1045 N N   . SER A 1 131 ? 7.924   49.209 16.478 1.00 15.42 ? 131 SER A N   1 
ATOM   1046 C CA  . SER A 1 131 ? 7.269   50.493 16.691 1.00 16.73 ? 131 SER A CA  1 
ATOM   1047 C C   . SER A 1 131 ? 7.538   50.920 18.116 1.00 16.53 ? 131 SER A C   1 
ATOM   1048 O O   . SER A 1 131 ? 7.339   50.128 19.039 1.00 17.57 ? 131 SER A O   1 
ATOM   1049 C CB  . SER A 1 131 ? 5.771   50.409 16.422 1.00 14.48 ? 131 SER A CB  1 
ATOM   1050 O OG  . SER A 1 131 ? 5.113   51.557 16.904 1.00 12.50 ? 131 SER A OG  1 
ATOM   1051 N N   . VAL A 1 132 ? 8.055   52.136 18.299 1.00 16.08 ? 132 VAL A N   1 
ATOM   1052 C CA  . VAL A 1 132 ? 8.363   52.624 19.635 1.00 18.19 ? 132 VAL A CA  1 
ATOM   1053 C C   . VAL A 1 132 ? 7.796   54.028 19.741 1.00 16.19 ? 132 VAL A C   1 
ATOM   1054 O O   . VAL A 1 132 ? 7.443   54.660 18.746 1.00 19.71 ? 132 VAL A O   1 
ATOM   1055 C CB  . VAL A 1 132 ? 9.877   52.616 19.979 1.00 13.37 ? 132 VAL A CB  1 
ATOM   1056 C CG1 . VAL A 1 132 ? 10.441  51.192 19.910 1.00 13.23 ? 132 VAL A CG1 1 
ATOM   1057 C CG2 . VAL A 1 132 ? 10.665  53.569 19.091 1.00 12.71 ? 132 VAL A CG2 1 
ATOM   1058 N N   . VAL A 1 133 ? 7.692   54.509 20.968 1.00 17.08 ? 133 VAL A N   1 
ATOM   1059 C CA  . VAL A 1 133 ? 7.217   55.860 21.199 1.00 20.06 ? 133 VAL A CA  1 
ATOM   1060 C C   . VAL A 1 133 ? 8.297   56.580 21.991 1.00 21.99 ? 133 VAL A C   1 
ATOM   1061 O O   . VAL A 1 133 ? 9.156   55.962 22.624 1.00 16.56 ? 133 VAL A O   1 
ATOM   1062 C CB  . VAL A 1 133 ? 5.862   55.886 21.943 1.00 17.67 ? 133 VAL A CB  1 
ATOM   1063 C CG1 . VAL A 1 133 ? 4.774   55.204 21.110 1.00 23.50 ? 133 VAL A CG1 1 
ATOM   1064 C CG2 . VAL A 1 133 ? 5.986   55.194 23.276 1.00 20.45 ? 133 VAL A CG2 1 
ATOM   1065 N N   . LEU A 1 134 ? 8.265   57.902 21.923 1.00 14.91 ? 134 LEU A N   1 
ATOM   1066 C CA  . LEU A 1 134 ? 9.234   58.715 22.635 1.00 20.15 ? 134 LEU A CA  1 
ATOM   1067 C C   . LEU A 1 134 ? 8.654   60.110 22.805 1.00 23.71 ? 134 LEU A C   1 
ATOM   1068 O O   . LEU A 1 134 ? 7.630   60.464 22.209 1.00 24.25 ? 134 LEU A O   1 
ATOM   1069 C CB  . LEU A 1 134 ? 10.587  58.749 21.917 1.00 16.74 ? 134 LEU A CB  1 
ATOM   1070 C CG  . LEU A 1 134 ? 10.644  59.101 20.433 1.00 20.72 ? 134 LEU A CG  1 
ATOM   1071 C CD1 . LEU A 1 134 ? 10.359  60.570 20.199 1.00 21.13 ? 134 LEU A CD1 1 
ATOM   1072 C CD2 . LEU A 1 134 ? 12.030  58.752 19.912 1.00 23.21 ? 134 LEU A CD2 1 
ATOM   1073 N N   . GLU A 1 135 ? 9.325   60.891 23.646 1.00 17.88 ? 135 GLU A N   1 
ATOM   1074 C CA  . GLU A 1 135 ? 9.009   62.297 23.835 1.00 21.41 ? 135 GLU A CA  1 
ATOM   1075 C C   . GLU A 1 135 ? 9.773   63.094 22.794 1.00 23.13 ? 135 GLU A C   1 
ATOM   1076 O O   . GLU A 1 135 ? 11.004  63.183 22.850 1.00 26.67 ? 135 GLU A O   1 
ATOM   1077 C CB  . GLU A 1 135 ? 9.362   62.759 25.241 1.00 24.95 ? 135 GLU A CB  1 
ATOM   1078 C CG  . GLU A 1 135 ? 8.956   64.194 25.482 1.00 34.69 ? 135 GLU A CG  1 
ATOM   1079 C CD  . GLU A 1 135 ? 9.601   64.777 26.702 1.00 35.69 ? 135 GLU A CD  1 
ATOM   1080 O OE1 . GLU A 1 135 ? 9.050   64.539 27.797 1.00 33.19 ? 135 GLU A OE1 1 
ATOM   1081 O OE2 . GLU A 1 135 ? 10.609  65.507 26.562 1.00 41.42 ? 135 GLU A OE2 1 
ATOM   1082 N N   . ALA A 1 136 ? 9.042   63.657 21.838 1.00 22.17 ? 136 ALA A N   1 
ATOM   1083 C CA  . ALA A 1 136 ? 9.610   64.462 20.770 1.00 21.43 ? 136 ALA A CA  1 
ATOM   1084 C C   . ALA A 1 136 ? 9.320   65.943 20.933 1.00 21.38 ? 136 ALA A C   1 
ATOM   1085 O O   . ALA A 1 136 ? 9.719   66.735 20.073 1.00 30.66 ? 136 ALA A O   1 
ATOM   1086 C CB  . ALA A 1 136 ? 9.077   63.988 19.415 1.00 22.34 ? 136 ALA A CB  1 
ATOM   1087 N N   . ALA A 1 137 ? 8.624   66.341 22.000 1.00 29.08 ? 137 ALA A N   1 
ATOM   1088 C CA  . ALA A 1 137 ? 8.186   67.729 22.119 1.00 29.06 ? 137 ALA A CA  1 
ATOM   1089 C C   . ALA A 1 137 ? 9.335   68.682 22.432 1.00 26.46 ? 137 ALA A C   1 
ATOM   1090 O O   . ALA A 1 137 ? 9.264   69.864 22.074 1.00 32.31 ? 137 ALA A O   1 
ATOM   1091 C CB  . ALA A 1 137 ? 7.109   67.844 23.198 1.00 19.61 ? 137 ALA A CB  1 
ATOM   1092 N N   . GLY A 1 138 ? 10.405  68.193 23.053 1.00 22.29 ? 138 GLY A N   1 
ATOM   1093 C CA  . GLY A 1 138 ? 11.502  69.069 23.432 1.00 21.88 ? 138 GLY A CA  1 
ATOM   1094 C C   . GLY A 1 138 ? 12.232  69.631 22.223 1.00 26.82 ? 138 GLY A C   1 
ATOM   1095 O O   . GLY A 1 138 ? 12.400  68.960 21.205 1.00 27.33 ? 138 GLY A O   1 
ATOM   1096 N N   . LYS A 1 139 ? 12.680  70.888 22.347 1.00 25.59 ? 139 LYS A N   1 
ATOM   1097 C CA  . LYS A 1 139 ? 13.407  71.517 21.247 1.00 31.06 ? 139 LYS A CA  1 
ATOM   1098 C C   . LYS A 1 139 ? 14.700  70.785 20.945 1.00 22.52 ? 139 LYS A C   1 
ATOM   1099 O O   . LYS A 1 139 ? 15.146  70.770 19.792 1.00 27.55 ? 139 LYS A O   1 
ATOM   1100 C CB  . LYS A 1 139 ? 13.705  72.993 21.542 1.00 23.30 ? 139 LYS A CB  1 
ATOM   1101 C CG  . LYS A 1 139 ? 12.726  73.974 20.887 1.00 40.88 ? 139 LYS A CG  1 
ATOM   1102 C CD  . LYS A 1 139 ? 11.271  73.506 21.031 1.00 49.98 ? 139 LYS A CD  1 
ATOM   1103 C CE  . LYS A 1 139 ? 10.636  74.022 22.330 1.00 59.71 ? 139 LYS A CE  1 
ATOM   1104 N NZ  . LYS A 1 139 ? 9.257   73.490 22.576 1.00 36.87 ? 139 LYS A NZ  1 
ATOM   1105 N N   . ASP A 1 140 ? 15.319  70.174 21.956 1.00 20.54 ? 140 ASP A N   1 
ATOM   1106 C CA  . ASP A 1 140 ? 16.560  69.461 21.696 1.00 20.28 ? 140 ASP A CA  1 
ATOM   1107 C C   . ASP A 1 140 ? 16.318  68.343 20.693 1.00 29.43 ? 140 ASP A C   1 
ATOM   1108 O O   . ASP A 1 140 ? 17.141  68.107 19.799 1.00 22.87 ? 140 ASP A O   1 
ATOM   1109 C CB  . ASP A 1 140 ? 17.101  68.899 22.998 1.00 25.83 ? 140 ASP A CB  1 
ATOM   1110 C CG  . ASP A 1 140 ? 17.549  69.989 23.941 1.00 40.51 ? 140 ASP A CG  1 
ATOM   1111 O OD1 . ASP A 1 140 ? 18.686  70.484 23.795 1.00 32.94 ? 140 ASP A OD1 1 
ATOM   1112 O OD2 . ASP A 1 140 ? 16.750  70.337 24.844 1.00 35.32 ? 140 ASP A OD2 1 
ATOM   1113 N N   . PHE A 1 141 ? 15.209  67.613 20.862 1.00 26.82 ? 141 PHE A N   1 
ATOM   1114 C CA  . PHE A 1 141 ? 14.820  66.598 19.890 1.00 24.21 ? 141 PHE A CA  1 
ATOM   1115 C C   . PHE A 1 141 ? 14.356  67.229 18.582 1.00 19.23 ? 141 PHE A C   1 
ATOM   1116 O O   . PHE A 1 141 ? 14.724  66.764 17.498 1.00 22.88 ? 141 PHE A O   1 
ATOM   1117 C CB  . PHE A 1 141 ? 13.722  65.702 20.474 1.00 20.13 ? 141 PHE A CB  1 
ATOM   1118 C CG  . PHE A 1 141 ? 13.369  64.523 19.599 1.00 25.22 ? 141 PHE A CG  1 
ATOM   1119 C CD1 . PHE A 1 141 ? 12.461  64.653 18.556 1.00 18.08 ? 141 PHE A CD1 1 
ATOM   1120 C CD2 . PHE A 1 141 ? 13.972  63.288 19.805 1.00 22.79 ? 141 PHE A CD2 1 
ATOM   1121 C CE1 . PHE A 1 141 ? 12.147  63.560 17.736 1.00 28.80 ? 141 PHE A CE1 1 
ATOM   1122 C CE2 . PHE A 1 141 ? 13.660  62.187 18.990 1.00 28.02 ? 141 PHE A CE2 1 
ATOM   1123 C CZ  . PHE A 1 141 ? 12.745  62.327 17.958 1.00 22.53 ? 141 PHE A CZ  1 
ATOM   1124 N N   . GLN A 1 142 ? 13.549  68.294 18.664 1.00 19.66 ? 142 GLN A N   1 
ATOM   1125 C CA  . GLN A 1 142 ? 13.038  68.922 17.449 1.00 23.38 ? 142 GLN A CA  1 
ATOM   1126 C C   . GLN A 1 142 ? 14.172  69.418 16.566 1.00 25.56 ? 142 GLN A C   1 
ATOM   1127 O O   . GLN A 1 142 ? 14.118  69.287 15.338 1.00 28.56 ? 142 GLN A O   1 
ATOM   1128 C CB  . GLN A 1 142 ? 12.123  70.094 17.807 1.00 30.63 ? 142 GLN A CB  1 
ATOM   1129 C CG  . GLN A 1 142 ? 10.882  69.765 18.618 1.00 27.91 ? 142 GLN A CG  1 
ATOM   1130 C CD  . GLN A 1 142 ? 9.653   69.614 17.750 1.00 37.15 ? 142 GLN A CD  1 
ATOM   1131 O OE1 . GLN A 1 142 ? 9.490   70.326 16.754 1.00 35.00 ? 142 GLN A OE1 1 
ATOM   1132 N NE2 . GLN A 1 142 ? 8.782   68.678 18.112 1.00 35.60 ? 142 GLN A NE2 1 
ATOM   1133 N N   . LEU A 1 143 ? 15.223  69.956 17.177 1.00 23.75 ? 143 LEU A N   1 
ATOM   1134 C CA  . LEU A 1 143 ? 16.321  70.584 16.458 1.00 26.11 ? 143 LEU A CA  1 
ATOM   1135 C C   . LEU A 1 143 ? 17.473  69.622 16.235 1.00 23.47 ? 143 LEU A C   1 
ATOM   1136 O O   . LEU A 1 143 ? 18.536  70.038 15.762 1.00 28.98 ? 143 LEU A O   1 
ATOM   1137 C CB  . LEU A 1 143 ? 16.795  71.841 17.201 1.00 28.05 ? 143 LEU A CB  1 
ATOM   1138 C CG  . LEU A 1 143 ? 15.800  73.021 17.222 1.00 31.43 ? 143 LEU A CG  1 
ATOM   1139 C CD1 . LEU A 1 143 ? 16.512  74.366 17.224 1.00 43.42 ? 143 LEU A CD1 1 
ATOM   1140 C CD2 . LEU A 1 143 ? 14.822  72.958 16.041 1.00 30.07 ? 143 LEU A CD2 1 
ATOM   1141 N N   . TYR A 1 144 ? 17.297  68.355 16.603 1.00 21.96 ? 144 TYR A N   1 
ATOM   1142 C CA  . TYR A 1 144 ? 18.373  67.389 16.484 1.00 21.43 ? 144 TYR A CA  1 
ATOM   1143 C C   . TYR A 1 144 ? 18.877  67.369 15.052 1.00 22.92 ? 144 TYR A C   1 
ATOM   1144 O O   . TYR A 1 144 ? 18.094  67.262 14.105 1.00 24.74 ? 144 TYR A O   1 
ATOM   1145 C CB  . TYR A 1 144 ? 17.864  66.008 16.881 1.00 23.51 ? 144 TYR A CB  1 
ATOM   1146 C CG  . TYR A 1 144 ? 18.784  64.858 16.517 1.00 26.24 ? 144 TYR A CG  1 
ATOM   1147 C CD1 . TYR A 1 144 ? 19.862  64.516 17.326 1.00 21.91 ? 144 TYR A CD1 1 
ATOM   1148 C CD2 . TYR A 1 144 ? 18.578  64.119 15.351 1.00 18.20 ? 144 TYR A CD2 1 
ATOM   1149 C CE1 . TYR A 1 144 ? 20.701  63.466 16.987 1.00 24.64 ? 144 TYR A CE1 1 
ATOM   1150 C CE2 . TYR A 1 144 ? 19.415  63.071 15.000 1.00 13.75 ? 144 TYR A CE2 1 
ATOM   1151 C CZ  . TYR A 1 144 ? 20.468  62.742 15.824 1.00 21.04 ? 144 TYR A CZ  1 
ATOM   1152 O OH  . TYR A 1 144 ? 21.299  61.694 15.492 1.00 18.67 ? 144 TYR A OH  1 
ATOM   1153 N N   . ARG A 1 145 ? 20.191  67.451 14.891 1.00 22.16 ? 145 ARG A N   1 
ATOM   1154 C CA  . ARG A 1 145 ? 20.778  67.384 13.564 1.00 30.64 ? 145 ARG A CA  1 
ATOM   1155 C C   . ARG A 1 145 ? 21.607  66.138 13.332 1.00 25.40 ? 145 ARG A C   1 
ATOM   1156 O O   . ARG A 1 145 ? 21.757  65.722 12.183 1.00 26.92 ? 145 ARG A O   1 
ATOM   1157 C CB  . ARG A 1 145 ? 21.609  68.634 13.235 1.00 35.42 ? 145 ARG A CB  1 
ATOM   1158 C CG  . ARG A 1 145 ? 20.828  69.943 13.327 1.00 45.32 ? 145 ARG A CG  1 
ATOM   1159 C CD  . ARG A 1 145 ? 21.727  71.148 13.108 1.00 52.24 ? 145 ARG A CD  1 
ATOM   1160 N NE  . ARG A 1 145 ? 22.173  71.132 11.716 1.00 60.84 ? 145 ARG A NE  1 
ATOM   1161 C CZ  . ARG A 1 145 ? 21.799  72.001 10.784 1.00 67.46 ? 145 ARG A CZ  1 
ATOM   1162 N NH1 . ARG A 1 145 ? 20.959  72.990 11.054 1.00 59.06 ? 145 ARG A NH1 1 
ATOM   1163 N NH2 . ARG A 1 145 ? 22.253  71.855 9.540  1.00 47.44 ? 145 ARG A NH2 1 
ATOM   1164 N N   . GLY A 1 146 ? 22.143  65.537 14.378 1.00 22.24 ? 146 GLY A N   1 
ATOM   1165 C CA  . GLY A 1 146 ? 22.962  64.360 14.190 1.00 24.44 ? 146 GLY A CA  1 
ATOM   1166 C C   . GLY A 1 146 ? 23.743  64.053 15.440 1.00 23.09 ? 146 GLY A C   1 
ATOM   1167 O O   . GLY A 1 146 ? 23.796  64.837 16.392 1.00 17.43 ? 146 GLY A O   1 
ATOM   1168 N N   . GLY A 1 147 ? 24.352  62.879 15.419 1.00 30.39 ? 147 GLY A N   1 
ATOM   1169 C CA  . GLY A 1 147 ? 25.078  62.372 16.563 1.00 18.65 ? 147 GLY A CA  1 
ATOM   1170 C C   . GLY A 1 147 ? 24.182  61.457 17.374 1.00 24.12 ? 147 GLY A C   1 
ATOM   1171 O O   . GLY A 1 147 ? 23.013  61.217 17.056 1.00 22.87 ? 147 GLY A O   1 
ATOM   1172 N N   . ILE A 1 148 ? 24.753  60.935 18.451 1.00 27.58 ? 148 ILE A N   1 
ATOM   1173 C CA  . ILE A 1 148 ? 24.005  60.087 19.368 1.00 24.00 ? 148 ILE A CA  1 
ATOM   1174 C C   . ILE A 1 148 ? 23.268  61.001 20.342 1.00 19.64 ? 148 ILE A C   1 
ATOM   1175 O O   . ILE A 1 148 ? 23.882  61.699 21.149 1.00 25.14 ? 148 ILE A O   1 
ATOM   1176 C CB  . ILE A 1 148 ? 24.921  59.095 20.091 1.00 24.72 ? 148 ILE A CB  1 
ATOM   1177 C CG1 . ILE A 1 148 ? 25.485  58.083 19.087 1.00 22.28 ? 148 ILE A CG1 1 
ATOM   1178 C CG2 . ILE A 1 148 ? 24.178  58.389 21.187 1.00 29.02 ? 148 ILE A CG2 1 
ATOM   1179 C CD1 . ILE A 1 148 ? 26.586  57.222 19.655 1.00 35.69 ? 148 ILE A CD1 1 
ATOM   1180 N N   . PHE A 1 149 ? 21.949  61.027 20.232 1.00 22.38 ? 149 PHE A N   1 
ATOM   1181 C CA  . PHE A 1 149 ? 21.127  61.949 20.997 1.00 26.79 ? 149 PHE A CA  1 
ATOM   1182 C C   . PHE A 1 149 ? 20.985  61.458 22.429 1.00 20.61 ? 149 PHE A C   1 
ATOM   1183 O O   . PHE A 1 149 ? 20.567  60.321 22.669 1.00 24.69 ? 149 PHE A O   1 
ATOM   1184 C CB  . PHE A 1 149 ? 19.755  62.086 20.343 1.00 21.28 ? 149 PHE A CB  1 
ATOM   1185 C CG  . PHE A 1 149 ? 18.886  63.115 20.983 1.00 22.92 ? 149 PHE A CG  1 
ATOM   1186 C CD1 . PHE A 1 149 ? 19.164  64.460 20.845 1.00 19.44 ? 149 PHE A CD1 1 
ATOM   1187 C CD2 . PHE A 1 149 ? 17.775  62.735 21.715 1.00 22.34 ? 149 PHE A CD2 1 
ATOM   1188 C CE1 . PHE A 1 149 ? 18.365  65.400 21.438 1.00 20.48 ? 149 PHE A CE1 1 
ATOM   1189 C CE2 . PHE A 1 149 ? 16.970  63.676 22.302 1.00 26.44 ? 149 PHE A CE2 1 
ATOM   1190 C CZ  . PHE A 1 149 ? 17.263  65.008 22.164 1.00 22.58 ? 149 PHE A CZ  1 
ATOM   1191 N N   . VAL A 1 150 ? 21.304  62.330 23.382 1.00 24.53 ? 150 VAL A N   1 
ATOM   1192 C CA  . VAL A 1 150 ? 21.224  62.002 24.802 1.00 29.64 ? 150 VAL A CA  1 
ATOM   1193 C C   . VAL A 1 150 ? 20.139  62.786 25.520 1.00 21.51 ? 150 VAL A C   1 
ATOM   1194 O O   . VAL A 1 150 ? 19.979  62.632 26.740 1.00 22.92 ? 150 VAL A O   1 
ATOM   1195 C CB  . VAL A 1 150 ? 22.589  62.217 25.486 1.00 24.32 ? 150 VAL A CB  1 
ATOM   1196 C CG1 . VAL A 1 150 ? 23.675  61.467 24.735 1.00 27.34 ? 150 VAL A CG1 1 
ATOM   1197 C CG2 . VAL A 1 150 ? 22.932  63.698 25.547 1.00 20.22 ? 150 VAL A CG2 1 
ATOM   1198 N N   . GLY A 1 151 ? 19.373  63.603 24.802 1.00 25.37 ? 151 GLY A N   1 
ATOM   1199 C CA  . GLY A 1 151 ? 18.481  64.557 25.417 1.00 17.37 ? 151 GLY A CA  1 
ATOM   1200 C C   . GLY A 1 151 ? 19.094  65.944 25.358 1.00 23.50 ? 151 GLY A C   1 
ATOM   1201 O O   . GLY A 1 151 ? 19.973  66.214 24.532 1.00 19.20 ? 151 GLY A O   1 
ATOM   1202 N N   . PRO A 1 152 ? 18.666  66.854 26.243 1.00 19.43 ? 152 PRO A N   1 
ATOM   1203 C CA  . PRO A 1 152 ? 17.696  66.660 27.329 1.00 25.39 ? 152 PRO A CA  1 
ATOM   1204 C C   . PRO A 1 152 ? 16.322  66.249 26.815 1.00 23.91 ? 152 PRO A C   1 
ATOM   1205 O O   . PRO A 1 152 ? 15.906  66.662 25.735 1.00 26.35 ? 152 PRO A O   1 
ATOM   1206 C CB  . PRO A 1 152 ? 17.668  68.026 28.043 1.00 20.20 ? 152 PRO A CB  1 
ATOM   1207 C CG  . PRO A 1 152 ? 18.578  68.939 27.284 1.00 28.51 ? 152 PRO A CG  1 
ATOM   1208 C CD  . PRO A 1 152 ? 19.451  68.082 26.426 1.00 19.98 ? 152 PRO A CD  1 
ATOM   1209 N N   . CYS A 1 153 ? 15.610  65.416 27.562 1.00 24.65 ? 153 CYS A N   1 
ATOM   1210 C CA  . CYS A 1 153 ? 14.226  65.083 27.256 1.00 32.72 ? 153 CYS A CA  1 
ATOM   1211 C C   . CYS A 1 153 ? 13.655  64.402 28.485 1.00 26.51 ? 153 CYS A C   1 
ATOM   1212 O O   . CYS A 1 153 ? 14.393  63.799 29.267 1.00 39.64 ? 153 CYS A O   1 
ATOM   1213 C CB  . CYS A 1 153 ? 14.091  64.185 26.006 1.00 32.21 ? 153 CYS A CB  1 
ATOM   1214 S SG  . CYS A 1 153 ? 15.121  62.665 25.958 1.00 38.53 ? 153 CYS A SG  1 
ATOM   1215 N N   . GLY A 1 154 ? 12.341  64.502 28.649 1.00 29.61 ? 154 GLY A N   1 
ATOM   1216 C CA  . GLY A 1 154 ? 11.646  63.757 29.674 1.00 31.53 ? 154 GLY A CA  1 
ATOM   1217 C C   . GLY A 1 154 ? 11.118  62.461 29.105 1.00 31.56 ? 154 GLY A C   1 
ATOM   1218 O O   . GLY A 1 154 ? 11.430  62.069 27.979 1.00 36.78 ? 154 GLY A O   1 
ATOM   1219 N N   . ASN A 1 155 ? 10.308  61.773 29.903 1.00 31.21 ? 155 ASN A N   1 
ATOM   1220 C CA  . ASN A 1 155 ? 9.684   60.541 29.447 1.00 24.49 ? 155 ASN A CA  1 
ATOM   1221 C C   . ASN A 1 155 ? 8.213   60.731 29.091 1.00 26.29 ? 155 ASN A C   1 
ATOM   1222 O O   . ASN A 1 155 ? 7.472   59.748 28.983 1.00 38.50 ? 155 ASN A O   1 
ATOM   1223 C CB  . ASN A 1 155 ? 9.864   59.439 30.491 1.00 31.84 ? 155 ASN A CB  1 
ATOM   1224 C CG  . ASN A 1 155 ? 9.258   59.792 31.839 1.00 35.81 ? 155 ASN A CG  1 
ATOM   1225 O OD1 . ASN A 1 155 ? 8.187   60.391 31.921 1.00 41.27 ? 155 ASN A OD1 1 
ATOM   1226 N ND2 . ASN A 1 155 ? 9.940   59.396 32.911 1.00 44.21 ? 155 ASN A ND2 1 
ATOM   1227 N N   . LYS A 1 156 ? 7.783   61.975 28.894 1.00 24.44 ? 156 LYS A N   1 
ATOM   1228 C CA  . LYS A 1 156 ? 6.396   62.283 28.549 1.00 34.26 ? 156 LYS A CA  1 
ATOM   1229 C C   . LYS A 1 156 ? 6.192   61.939 27.076 1.00 30.38 ? 156 LYS A C   1 
ATOM   1230 O O   . LYS A 1 156 ? 6.255   62.797 26.191 1.00 34.74 ? 156 LYS A O   1 
ATOM   1231 C CB  . LYS A 1 156 ? 6.095   63.751 28.846 1.00 32.81 ? 156 LYS A CB  1 
ATOM   1232 C CG  . LYS A 1 156 ? 4.660   64.205 28.547 1.00 36.96 ? 156 LYS A CG  1 
ATOM   1233 C CD  . LYS A 1 156 ? 3.624   63.387 29.316 1.00 52.23 ? 156 LYS A CD  1 
ATOM   1234 C CE  . LYS A 1 156 ? 2.234   64.028 29.250 1.00 46.89 ? 156 LYS A CE  1 
ATOM   1235 N NZ  . LYS A 1 156 ? 1.513   63.695 27.986 1.00 50.05 ? 156 LYS A NZ  1 
ATOM   1236 N N   . VAL A 1 157 ? 5.942   60.654 26.800 1.00 28.95 ? 157 VAL A N   1 
ATOM   1237 C CA  . VAL A 1 157 ? 5.986   60.206 25.412 1.00 24.36 ? 157 VAL A CA  1 
ATOM   1238 C C   . VAL A 1 157 ? 4.767   60.721 24.666 1.00 24.58 ? 157 VAL A C   1 
ATOM   1239 O O   . VAL A 1 157 ? 3.648   60.777 25.200 1.00 22.54 ? 157 VAL A O   1 
ATOM   1240 C CB  . VAL A 1 157 ? 6.085   58.673 25.299 1.00 24.96 ? 157 VAL A CB  1 
ATOM   1241 C CG1 . VAL A 1 157 ? 7.365   58.180 25.939 1.00 20.37 ? 157 VAL A CG1 1 
ATOM   1242 C CG2 . VAL A 1 157 ? 4.835   57.956 25.814 1.00 17.23 ? 157 VAL A CG2 1 
ATOM   1243 N N   . ASP A 1 158 ? 4.990   61.092 23.414 1.00 21.53 ? 158 ASP A N   1 
ATOM   1244 C CA  . ASP A 1 158 ? 3.962   61.760 22.630 1.00 22.08 ? 158 ASP A CA  1 
ATOM   1245 C C   . ASP A 1 158 ? 4.127   61.523 21.137 1.00 19.62 ? 158 ASP A C   1 
ATOM   1246 O O   . ASP A 1 158 ? 3.371   62.110 20.354 1.00 22.90 ? 158 ASP A O   1 
ATOM   1247 C CB  . ASP A 1 158 ? 3.965   63.267 22.937 1.00 16.38 ? 158 ASP A CB  1 
ATOM   1248 C CG  . ASP A 1 158 ? 5.321   63.911 22.707 1.00 28.43 ? 158 ASP A CG  1 
ATOM   1249 O OD1 . ASP A 1 158 ? 6.088   63.437 21.839 1.00 25.84 ? 158 ASP A OD1 1 
ATOM   1250 O OD2 . ASP A 1 158 ? 5.638   64.890 23.420 1.00 41.10 ? 158 ASP A OD2 1 
ATOM   1251 N N   . HIS A 1 159 ? 5.039   60.654 20.718 1.00 17.49 ? 159 HIS A N   1 
ATOM   1252 C CA  . HIS A 1 159 ? 5.424   60.573 19.320 1.00 20.50 ? 159 HIS A CA  1 
ATOM   1253 C C   . HIS A 1 159 ? 5.842   59.155 19.006 1.00 20.67 ? 159 HIS A C   1 
ATOM   1254 O O   . HIS A 1 159 ? 6.716   58.609 19.674 1.00 25.03 ? 159 HIS A O   1 
ATOM   1255 C CB  . HIS A 1 159 ? 6.577   61.524 19.007 1.00 19.09 ? 159 HIS A CB  1 
ATOM   1256 C CG  . HIS A 1 159 ? 6.919   61.596 17.556 1.00 22.22 ? 159 HIS A CG  1 
ATOM   1257 N ND1 . HIS A 1 159 ? 5.982   61.851 16.579 1.00 21.27 ? 159 HIS A ND1 1 
ATOM   1258 C CD2 . HIS A 1 159 ? 8.097   61.410 16.913 1.00 22.25 ? 159 HIS A CD2 1 
ATOM   1259 C CE1 . HIS A 1 159 ? 6.572   61.830 15.395 1.00 22.27 ? 159 HIS A CE1 1 
ATOM   1260 N NE2 . HIS A 1 159 ? 7.855   61.563 15.570 1.00 19.53 ? 159 HIS A NE2 1 
ATOM   1261 N N   . ALA A 1 160 ? 5.218   58.562 17.995 1.00 21.30 ? 160 ALA A N   1 
ATOM   1262 C CA  . ALA A 1 160 ? 5.533   57.200 17.598 1.00 15.86 ? 160 ALA A CA  1 
ATOM   1263 C C   . ALA A 1 160 ? 6.505   57.231 16.430 1.00 18.12 ? 160 ALA A C   1 
ATOM   1264 O O   . ALA A 1 160 ? 6.311   57.982 15.466 1.00 22.70 ? 160 ALA A O   1 
ATOM   1265 C CB  . ALA A 1 160 ? 4.260   56.447 17.202 1.00 14.67 ? 160 ALA A CB  1 
ATOM   1266 N N   . VAL A 1 161 ? 7.541   56.406 16.520 1.00 14.40 ? 161 VAL A N   1 
ATOM   1267 C CA  . VAL A 1 161 ? 8.612   56.328 15.535 1.00 11.75 ? 161 VAL A CA  1 
ATOM   1268 C C   . VAL A 1 161 ? 8.967   54.864 15.415 1.00 14.74 ? 161 VAL A C   1 
ATOM   1269 O O   . VAL A 1 161 ? 8.317   54.005 16.029 1.00 16.78 ? 161 VAL A O   1 
ATOM   1270 C CB  . VAL A 1 161 ? 9.840   57.161 15.928 1.00 20.66 ? 161 VAL A CB  1 
ATOM   1271 C CG1 . VAL A 1 161 ? 9.521   58.637 15.893 1.00 18.99 ? 161 VAL A CG1 1 
ATOM   1272 C CG2 . VAL A 1 161 ? 10.276  56.760 17.318 1.00 17.55 ? 161 VAL A CG2 1 
ATOM   1273 N N   . ALA A 1 162 ? 10.046  54.551 14.715 1.00 15.25 ? 162 ALA A N   1 
ATOM   1274 C CA  . ALA A 1 162 ? 10.369  53.144 14.558 1.00 12.55 ? 162 ALA A CA  1 
ATOM   1275 C C   . ALA A 1 162 ? 11.826  52.880 14.843 1.00 11.47 ? 162 ALA A C   1 
ATOM   1276 O O   . ALA A 1 162 ? 12.689  53.621 14.380 1.00 18.24 ? 162 ALA A O   1 
ATOM   1277 C CB  . ALA A 1 162 ? 10.026  52.677 13.152 1.00 12.42 ? 162 ALA A CB  1 
ATOM   1278 N N   . ALA A 1 163 ? 12.106  51.849 15.630 1.00 15.88 ? 163 ALA A N   1 
ATOM   1279 C CA  . ALA A 1 163 ? 13.480  51.439 15.876 1.00 14.65 ? 163 ALA A CA  1 
ATOM   1280 C C   . ALA A 1 163 ? 13.866  50.429 14.805 1.00 13.17 ? 163 ALA A C   1 
ATOM   1281 O O   . ALA A 1 163 ? 13.239  49.373 14.688 1.00 19.13 ? 163 ALA A O   1 
ATOM   1282 C CB  . ALA A 1 163 ? 13.606  50.824 17.267 1.00 13.62 ? 163 ALA A CB  1 
ATOM   1283 N N   . VAL A 1 164 ? 14.910  50.744 14.037 1.00 16.26 ? 164 VAL A N   1 
ATOM   1284 C CA  . VAL A 1 164 ? 15.346  49.917 12.921 1.00 10.33 ? 164 VAL A CA  1 
ATOM   1285 C C   . VAL A 1 164 ? 16.775  49.433 13.089 1.00 13.02 ? 164 VAL A C   1 
ATOM   1286 O O   . VAL A 1 164 ? 17.319  48.804 12.182 1.00 17.30 ? 164 VAL A O   1 
ATOM   1287 C CB  . VAL A 1 164 ? 15.180  50.644 11.576 1.00 15.50 ? 164 VAL A CB  1 
ATOM   1288 C CG1 . VAL A 1 164 ? 13.711  50.953 11.325 1.00 21.86 ? 164 VAL A CG1 1 
ATOM   1289 C CG2 . VAL A 1 164 ? 16.041  51.897 11.549 1.00 15.60 ? 164 VAL A CG2 1 
ATOM   1290 N N   . GLY A 1 165 ? 17.383  49.678 14.242 1.00 18.62 ? 165 GLY A N   1 
ATOM   1291 C CA  . GLY A 1 165 ? 18.719  49.175 14.495 1.00 13.22 ? 165 GLY A CA  1 
ATOM   1292 C C   . GLY A 1 165 ? 19.205  49.660 15.835 1.00 13.28 ? 165 GLY A C   1 
ATOM   1293 O O   . GLY A 1 165 ? 18.475  50.308 16.589 1.00 14.79 ? 165 GLY A O   1 
ATOM   1294 N N   . TYR A 1 166 ? 20.459  49.341 16.130 1.00 17.80 ? 166 TYR A N   1 
ATOM   1295 C CA  . TYR A 1 166 ? 21.049  49.787 17.386 1.00 15.08 ? 166 TYR A CA  1 
ATOM   1296 C C   . TYR A 1 166 ? 22.548  49.574 17.311 1.00 12.06 ? 166 TYR A C   1 
ATOM   1297 O O   . TYR A 1 166 ? 23.056  48.878 16.429 1.00 18.61 ? 166 TYR A O   1 
ATOM   1298 C CB  . TYR A 1 166 ? 20.457  49.060 18.599 1.00 13.46 ? 166 TYR A CB  1 
ATOM   1299 C CG  . TYR A 1 166 ? 20.718  47.579 18.654 1.00 16.54 ? 166 TYR A CG  1 
ATOM   1300 C CD1 . TYR A 1 166 ? 21.953  47.090 19.063 1.00 17.11 ? 166 TYR A CD1 1 
ATOM   1301 C CD2 . TYR A 1 166 ? 19.730  46.663 18.319 1.00 19.95 ? 166 TYR A CD2 1 
ATOM   1302 C CE1 . TYR A 1 166 ? 22.206  45.734 19.122 1.00 25.61 ? 166 TYR A CE1 1 
ATOM   1303 C CE2 . TYR A 1 166 ? 19.972  45.293 18.380 1.00 17.16 ? 166 TYR A CE2 1 
ATOM   1304 C CZ  . TYR A 1 166 ? 21.219  44.839 18.776 1.00 23.01 ? 166 TYR A CZ  1 
ATOM   1305 O OH  . TYR A 1 166 ? 21.490  43.488 18.846 1.00 22.85 ? 166 TYR A OH  1 
ATOM   1306 N N   . GLY A 1 167 ? 23.246  50.162 18.268 1.00 17.21 ? 167 GLY A N   1 
ATOM   1307 C CA  . GLY A 1 167 ? 24.653  49.911 18.462 1.00 19.98 ? 167 GLY A CA  1 
ATOM   1308 C C   . GLY A 1 167 ? 24.976  49.875 19.938 1.00 20.51 ? 167 GLY A C   1 
ATOM   1309 O O   . GLY A 1 167 ? 24.079  49.839 20.786 1.00 17.78 ? 167 GLY A O   1 
ATOM   1310 N N   . PRO A 1 168 ? 26.266  49.787 20.271 1.00 22.21 ? 168 PRO A N   1 
ATOM   1311 C CA  . PRO A 1 168 ? 26.644  49.699 21.688 1.00 18.71 ? 168 PRO A CA  1 
ATOM   1312 C C   . PRO A 1 168 ? 26.092  50.833 22.525 1.00 22.51 ? 168 PRO A C   1 
ATOM   1313 O O   . PRO A 1 168 ? 25.693  50.602 23.671 1.00 20.59 ? 168 PRO A O   1 
ATOM   1314 C CB  . PRO A 1 168 ? 28.173  49.722 21.631 1.00 23.73 ? 168 PRO A CB  1 
ATOM   1315 C CG  . PRO A 1 168 ? 28.490  49.072 20.327 1.00 25.03 ? 168 PRO A CG  1 
ATOM   1316 C CD  . PRO A 1 168 ? 27.396  49.489 19.383 1.00 22.44 ? 168 PRO A CD  1 
ATOM   1317 N N   . ASN A 1 169 ? 26.037  52.055 21.987 1.00 29.76 ? 169 ASN A N   1 
ATOM   1318 C CA  . ASN A 1 169 ? 25.541  53.191 22.752 1.00 31.11 ? 169 ASN A CA  1 
ATOM   1319 C C   . ASN A 1 169 ? 24.175  53.673 22.301 1.00 23.36 ? 169 ASN A C   1 
ATOM   1320 O O   . ASN A 1 169 ? 23.659  54.631 22.879 1.00 28.09 ? 169 ASN A O   1 
ATOM   1321 C CB  . ASN A 1 169 ? 26.477  54.407 22.671 1.00 31.43 ? 169 ASN A CB  1 
ATOM   1322 C CG  . ASN A 1 169 ? 27.911  54.049 22.458 1.00 41.78 ? 169 ASN A CG  1 
ATOM   1323 O OD1 . ASN A 1 169 ? 28.511  53.292 23.230 1.00 37.78 ? 169 ASN A OD1 1 
ATOM   1324 N ND2 . ASN A 1 169 ? 28.502  54.646 21.420 1.00 24.48 ? 169 ASN A ND2 1 
ATOM   1325 N N   . TYR A 1 170 ? 23.589  53.102 21.263 1.00 21.30 ? 170 TYR A N   1 
ATOM   1326 C CA  . TYR A 1 170 ? 22.451  53.810 20.708 1.00 19.19 ? 170 TYR A CA  1 
ATOM   1327 C C   . TYR A 1 170 ? 21.414  52.825 20.199 1.00 22.71 ? 170 TYR A C   1 
ATOM   1328 O O   . TYR A 1 170 ? 21.672  51.628 20.036 1.00 17.77 ? 170 TYR A O   1 
ATOM   1329 C CB  . TYR A 1 170 ? 22.876  54.766 19.575 1.00 16.70 ? 170 TYR A CB  1 
ATOM   1330 C CG  . TYR A 1 170 ? 23.423  54.064 18.351 1.00 21.87 ? 170 TYR A CG  1 
ATOM   1331 C CD1 . TYR A 1 170 ? 22.568  53.672 17.319 1.00 17.68 ? 170 TYR A CD1 1 
ATOM   1332 C CD2 . TYR A 1 170 ? 24.778  53.779 18.223 1.00 23.16 ? 170 TYR A CD2 1 
ATOM   1333 C CE1 . TYR A 1 170 ? 23.043  53.021 16.200 1.00 17.64 ? 170 TYR A CE1 1 
ATOM   1334 C CE2 . TYR A 1 170 ? 25.271  53.121 17.081 1.00 25.82 ? 170 TYR A CE2 1 
ATOM   1335 C CZ  . TYR A 1 170 ? 24.388  52.748 16.079 1.00 19.50 ? 170 TYR A CZ  1 
ATOM   1336 O OH  . TYR A 1 170 ? 24.836  52.100 14.952 1.00 23.56 ? 170 TYR A OH  1 
ATOM   1337 N N   . ILE A 1 171 ? 20.228  53.371 19.965 1.00 19.83 ? 171 ILE A N   1 
ATOM   1338 C CA  . ILE A 1 171 ? 19.151  52.737 19.230 1.00 18.12 ? 171 ILE A CA  1 
ATOM   1339 C C   . ILE A 1 171 ? 18.882  53.614 18.016 1.00 21.40 ? 171 ILE A C   1 
ATOM   1340 O O   . ILE A 1 171 ? 18.826  54.844 18.127 1.00 21.67 ? 171 ILE A O   1 
ATOM   1341 C CB  . ILE A 1 171 ? 17.892  52.570 20.112 1.00 15.66 ? 171 ILE A CB  1 
ATOM   1342 C CG1 . ILE A 1 171 ? 18.161  51.493 21.176 1.00 22.08 ? 171 ILE A CG1 1 
ATOM   1343 C CG2 . ILE A 1 171 ? 16.661  52.237 19.267 1.00 14.11 ? 171 ILE A CG2 1 
ATOM   1344 C CD1 . ILE A 1 171 ? 17.123  51.412 22.280 1.00 25.06 ? 171 ILE A CD1 1 
ATOM   1345 N N   . LEU A 1 172 ? 18.725  52.982 16.862 1.00 13.64 ? 172 LEU A N   1 
ATOM   1346 C CA  . LEU A 1 172 ? 18.589  53.692 15.602 1.00 17.83 ? 172 LEU A CA  1 
ATOM   1347 C C   . LEU A 1 172 ? 17.113  53.870 15.294 1.00 14.93 ? 172 LEU A C   1 
ATOM   1348 O O   . LEU A 1 172 ? 16.374  52.883 15.244 1.00 16.58 ? 172 LEU A O   1 
ATOM   1349 C CB  . LEU A 1 172 ? 19.269  52.927 14.472 1.00 22.75 ? 172 LEU A CB  1 
ATOM   1350 C CG  . LEU A 1 172 ? 19.050  53.560 13.099 1.00 20.32 ? 172 LEU A CG  1 
ATOM   1351 C CD1 . LEU A 1 172 ? 19.710  54.916 13.067 1.00 16.01 ? 172 LEU A CD1 1 
ATOM   1352 C CD2 . LEU A 1 172 ? 19.585  52.660 11.992 1.00 22.69 ? 172 LEU A CD2 1 
ATOM   1353 N N   . ILE A 1 173 ? 16.682  55.113 15.100 1.00 11.41 ? 173 ILE A N   1 
ATOM   1354 C CA  . ILE A 1 173 ? 15.274  55.466 15.013 1.00 13.95 ? 173 ILE A CA  1 
ATOM   1355 C C   . ILE A 1 173 ? 15.007  56.109 13.658 1.00 18.30 ? 173 ILE A C   1 
ATOM   1356 O O   . ILE A 1 173 ? 15.718  57.033 13.246 1.00 18.76 ? 173 ILE A O   1 
ATOM   1357 C CB  . ILE A 1 173 ? 14.843  56.418 16.147 1.00 18.89 ? 173 ILE A CB  1 
ATOM   1358 C CG1 . ILE A 1 173 ? 15.010  55.767 17.521 1.00 27.75 ? 173 ILE A CG1 1 
ATOM   1359 C CG2 . ILE A 1 173 ? 13.433  56.904 15.926 1.00 14.77 ? 173 ILE A CG2 1 
ATOM   1360 C CD1 . ILE A 1 173 ? 14.127  54.542 17.713 1.00 28.97 ? 173 ILE A CD1 1 
ATOM   1361 N N   . LYS A 1 174 ? 14.005  55.586 12.961 1.00 20.71 ? 174 LYS A N   1 
ATOM   1362 C CA  . LYS A 1 174 ? 13.426  56.185 11.767 1.00 12.53 ? 174 LYS A CA  1 
ATOM   1363 C C   . LYS A 1 174 ? 12.284  57.088 12.207 1.00 15.31 ? 174 LYS A C   1 
ATOM   1364 O O   . LYS A 1 174 ? 11.294  56.616 12.794 1.00 18.03 ? 174 LYS A O   1 
ATOM   1365 C CB  . LYS A 1 174 ? 12.919  55.109 10.807 1.00 17.83 ? 174 LYS A CB  1 
ATOM   1366 C CG  . LYS A 1 174 ? 12.391  55.654 9.472  1.00 14.88 ? 174 LYS A CG  1 
ATOM   1367 C CD  . LYS A 1 174 ? 11.856  54.529 8.564  1.00 14.82 ? 174 LYS A CD  1 
ATOM   1368 C CE  . LYS A 1 174 ? 11.554  55.034 7.156  1.00 12.34 ? 174 LYS A CE  1 
ATOM   1369 N NZ  . LYS A 1 174 ? 10.744  54.089 6.361  1.00 16.23 ? 174 LYS A NZ  1 
ATOM   1370 N N   . ASN A 1 175 ? 12.457  58.385 11.998 1.00 14.78 ? 175 ASN A N   1 
ATOM   1371 C CA  . ASN A 1 175 ? 11.407  59.343 12.277 1.00 13.28 ? 175 ASN A CA  1 
ATOM   1372 C C   . ASN A 1 175 ? 10.608  59.584 10.991 1.00 16.37 ? 175 ASN A C   1 
ATOM   1373 O O   . ASN A 1 175 ? 11.025  59.217 9.890  1.00 11.19 ? 175 ASN A O   1 
ATOM   1374 C CB  . ASN A 1 175 ? 12.010  60.632 12.826 1.00 11.40 ? 175 ASN A CB  1 
ATOM   1375 C CG  . ASN A 1 175 ? 11.011  61.459 13.593 1.00 15.25 ? 175 ASN A CG  1 
ATOM   1376 O OD1 . ASN A 1 175 ? 9.856   61.068 13.756 1.00 15.97 ? 175 ASN A OD1 1 
ATOM   1377 N ND2 . ASN A 1 175 ? 11.456  62.607 14.090 1.00 17.97 ? 175 ASN A ND2 1 
ATOM   1378 N N   . SER A 1 176 ? 9.467   60.241 11.130 1.00 19.51 ? 176 SER A N   1 
ATOM   1379 C CA  . SER A 1 176 ? 8.580   60.514 10.009 1.00 15.15 ? 176 SER A CA  1 
ATOM   1380 C C   . SER A 1 176 ? 8.467   62.009 9.809  1.00 18.74 ? 176 SER A C   1 
ATOM   1381 O O   . SER A 1 176 ? 7.402   62.541 9.483  1.00 19.45 ? 176 SER A O   1 
ATOM   1382 C CB  . SER A 1 176 ? 7.197   59.901 10.221 1.00 12.12 ? 176 SER A CB  1 
ATOM   1383 O OG  . SER A 1 176 ? 6.671   60.251 11.490 1.00 15.52 ? 176 SER A OG  1 
ATOM   1384 N N   . TRP A 1 177 ? 9.602   62.691 9.909  1.00 18.95 ? 177 TRP A N   1 
ATOM   1385 C CA  . TRP A 1 177 ? 9.641   64.135 9.762  1.00 20.37 ? 177 TRP A CA  1 
ATOM   1386 C C   . TRP A 1 177 ? 10.395  64.553 8.510  1.00 21.49 ? 177 TRP A C   1 
ATOM   1387 O O   . TRP A 1 177 ? 10.903  65.675 8.440  1.00 17.58 ? 177 TRP A O   1 
ATOM   1388 C CB  . TRP A 1 177 ? 10.281  64.775 10.992 1.00 24.57 ? 177 TRP A CB  1 
ATOM   1389 C CG  . TRP A 1 177 ? 9.422   64.746 12.226 1.00 18.67 ? 177 TRP A CG  1 
ATOM   1390 C CD1 . TRP A 1 177 ? 8.116   64.355 12.316 1.00 15.27 ? 177 TRP A CD1 1 
ATOM   1391 C CD2 . TRP A 1 177 ? 9.808   65.164 13.536 1.00 20.15 ? 177 TRP A CD2 1 
ATOM   1392 N NE1 . TRP A 1 177 ? 7.675   64.479 13.606 1.00 19.95 ? 177 TRP A NE1 1 
ATOM   1393 C CE2 . TRP A 1 177 ? 8.692   64.982 14.376 1.00 21.18 ? 177 TRP A CE2 1 
ATOM   1394 C CE3 . TRP A 1 177 ? 10.989  65.689 14.080 1.00 22.19 ? 177 TRP A CE3 1 
ATOM   1395 C CZ2 . TRP A 1 177 ? 8.721   65.292 15.732 1.00 25.58 ? 177 TRP A CZ2 1 
ATOM   1396 C CZ3 . TRP A 1 177 ? 11.016  66.000 15.431 1.00 23.64 ? 177 TRP A CZ3 1 
ATOM   1397 C CH2 . TRP A 1 177 ? 9.891   65.797 16.241 1.00 32.03 ? 177 TRP A CH2 1 
ATOM   1398 N N   . GLY A 1 178 ? 10.502  63.661 7.532  1.00 16.63 ? 178 GLY A N   1 
ATOM   1399 C CA  . GLY A 1 178 ? 11.182  63.976 6.297  1.00 25.75 ? 178 GLY A CA  1 
ATOM   1400 C C   . GLY A 1 178 ? 12.667  63.703 6.368  1.00 15.84 ? 178 GLY A C   1 
ATOM   1401 O O   . GLY A 1 178 ? 13.244  63.457 7.427  1.00 21.14 ? 178 GLY A O   1 
ATOM   1402 N N   . THR A 1 179 ? 13.298  63.751 5.198  1.00 14.82 ? 179 THR A N   1 
ATOM   1403 C CA  . THR A 1 179 ? 14.714  63.440 5.096  1.00 17.58 ? 179 THR A CA  1 
ATOM   1404 C C   . THR A 1 179 ? 15.638  64.564 5.554  1.00 23.62 ? 179 THR A C   1 
ATOM   1405 O O   . THR A 1 179 ? 16.840  64.313 5.714  1.00 21.22 ? 179 THR A O   1 
ATOM   1406 C CB  . THR A 1 179 ? 15.049  63.050 3.658  1.00 20.98 ? 179 THR A CB  1 
ATOM   1407 O OG1 . THR A 1 179 ? 14.702  64.124 2.766  1.00 23.02 ? 179 THR A OG1 1 
ATOM   1408 C CG2 . THR A 1 179 ? 14.288  61.783 3.267  1.00 18.11 ? 179 THR A CG2 1 
ATOM   1409 N N   . GLY A 1 180 ? 15.124  65.775 5.799  1.00 19.68 ? 180 GLY A N   1 
ATOM   1410 C CA  . GLY A 1 180 ? 15.964  66.871 6.252  1.00 14.01 ? 180 GLY A CA  1 
ATOM   1411 C C   . GLY A 1 180 ? 16.177  66.973 7.745  1.00 22.06 ? 180 GLY A C   1 
ATOM   1412 O O   . GLY A 1 180 ? 17.015  67.755 8.202  1.00 27.54 ? 180 GLY A O   1 
ATOM   1413 N N   . TRP A 1 181 ? 15.459  66.183 8.523  1.00 19.87 ? 181 TRP A N   1 
ATOM   1414 C CA  . TRP A 1 181 ? 15.601  66.172 9.970  1.00 20.58 ? 181 TRP A CA  1 
ATOM   1415 C C   . TRP A 1 181 ? 16.609  65.120 10.395 1.00 20.64 ? 181 TRP A C   1 
ATOM   1416 O O   . TRP A 1 181 ? 16.673  64.036 9.807  1.00 22.10 ? 181 TRP A O   1 
ATOM   1417 C CB  . TRP A 1 181 ? 14.259  65.889 10.651 1.00 23.37 ? 181 TRP A CB  1 
ATOM   1418 C CG  . TRP A 1 181 ? 14.345  65.853 12.153 1.00 27.80 ? 181 TRP A CG  1 
ATOM   1419 C CD1 . TRP A 1 181 ? 14.252  66.911 13.020 1.00 21.02 ? 181 TRP A CD1 1 
ATOM   1420 C CD2 . TRP A 1 181 ? 14.548  64.687 12.963 1.00 24.81 ? 181 TRP A CD2 1 
ATOM   1421 N NE1 . TRP A 1 181 ? 14.384  66.467 14.316 1.00 24.20 ? 181 TRP A NE1 1 
ATOM   1422 C CE2 . TRP A 1 181 ? 14.569  65.109 14.307 1.00 23.87 ? 181 TRP A CE2 1 
ATOM   1423 C CE3 . TRP A 1 181 ? 14.719  63.326 12.679 1.00 24.23 ? 181 TRP A CE3 1 
ATOM   1424 C CZ2 . TRP A 1 181 ? 14.746  64.217 15.365 1.00 22.52 ? 181 TRP A CZ2 1 
ATOM   1425 C CZ3 . TRP A 1 181 ? 14.905  62.444 13.737 1.00 21.28 ? 181 TRP A CZ3 1 
ATOM   1426 C CH2 . TRP A 1 181 ? 14.905  62.891 15.057 1.00 15.48 ? 181 TRP A CH2 1 
ATOM   1427 N N   . GLY A 1 182 ? 17.451  65.479 11.360 1.00 16.83 ? 182 GLY A N   1 
ATOM   1428 C CA  . GLY A 1 182 ? 18.332  64.491 11.956 1.00 16.43 ? 182 GLY A CA  1 
ATOM   1429 C C   . GLY A 1 182 ? 19.349  63.970 10.964 1.00 16.87 ? 182 GLY A C   1 
ATOM   1430 O O   . GLY A 1 182 ? 19.829  64.695 10.089 1.00 21.94 ? 182 GLY A O   1 
ATOM   1431 N N   . GLU A 1 183 ? 19.660  62.681 11.084 1.00 18.13 ? 183 GLU A N   1 
ATOM   1432 C CA  . GLU A 1 183 ? 20.656  62.034 10.232 1.00 18.72 ? 183 GLU A CA  1 
ATOM   1433 C C   . GLU A 1 183 ? 19.908  61.429 9.050  1.00 17.38 ? 183 GLU A C   1 
ATOM   1434 O O   . GLU A 1 183 ? 19.615  60.233 9.005  1.00 16.32 ? 183 GLU A O   1 
ATOM   1435 C CB  . GLU A 1 183 ? 21.445  60.994 11.016 1.00 19.79 ? 183 GLU A CB  1 
ATOM   1436 C CG  . GLU A 1 183 ? 22.173  61.592 12.229 1.00 25.44 ? 183 GLU A CG  1 
ATOM   1437 C CD  . GLU A 1 183 ? 23.051  60.594 12.974 1.00 31.57 ? 183 GLU A CD  1 
ATOM   1438 O OE1 . GLU A 1 183 ? 22.679  59.401 13.061 1.00 23.09 ? 183 GLU A OE1 1 
ATOM   1439 O OE2 . GLU A 1 183 ? 24.112  61.015 13.494 1.00 30.04 ? 183 GLU A OE2 1 
ATOM   1440 N N   . ASN A 1 184 ? 19.606  62.297 8.074  1.00 23.15 ? 184 ASN A N   1 
ATOM   1441 C CA  . ASN A 1 184 ? 18.815  61.957 6.884  1.00 16.61 ? 184 ASN A CA  1 
ATOM   1442 C C   . ASN A 1 184 ? 17.466  61.358 7.267  1.00 17.79 ? 184 ASN A C   1 
ATOM   1443 O O   . ASN A 1 184 ? 16.946  60.461 6.599  1.00 21.11 ? 184 ASN A O   1 
ATOM   1444 C CB  . ASN A 1 184 ? 19.577  60.981 5.984  1.00 19.82 ? 184 ASN A CB  1 
ATOM   1445 C CG  . ASN A 1 184 ? 20.814  61.582 5.372  1.00 30.66 ? 184 ASN A CG  1 
ATOM   1446 O OD1 . ASN A 1 184 ? 20.975  62.805 5.319  1.00 31.34 ? 184 ASN A OD1 1 
ATOM   1447 N ND2 . ASN A 1 184 ? 21.709  60.720 4.908  1.00 26.73 ? 184 ASN A ND2 1 
ATOM   1448 N N   . GLY A 1 185 ? 16.887  61.859 8.347  1.00 14.77 ? 185 GLY A N   1 
ATOM   1449 C CA  . GLY A 1 185 ? 15.583  61.418 8.773  1.00 19.40 ? 185 GLY A CA  1 
ATOM   1450 C C   . GLY A 1 185 ? 15.637  60.466 9.935  1.00 12.19 ? 185 GLY A C   1 
ATOM   1451 O O   . GLY A 1 185 ? 14.588  60.074 10.453 1.00 15.85 ? 185 GLY A O   1 
ATOM   1452 N N   . TYR A 1 186 ? 16.836  60.079 10.342 1.00 14.72 ? 186 TYR A N   1 
ATOM   1453 C CA  . TYR A 1 186 ? 17.053  59.140 11.423 1.00 19.11 ? 186 TYR A CA  1 
ATOM   1454 C C   . TYR A 1 186 ? 17.624  59.879 12.621 1.00 18.91 ? 186 TYR A C   1 
ATOM   1455 O O   . TYR A 1 186 ? 18.192  60.967 12.505 1.00 18.83 ? 186 TYR A O   1 
ATOM   1456 C CB  . TYR A 1 186 ? 17.987  58.009 10.987 1.00 14.65 ? 186 TYR A CB  1 
ATOM   1457 C CG  . TYR A 1 186 ? 17.340  57.083 9.971  1.00 22.32 ? 186 TYR A CG  1 
ATOM   1458 C CD1 . TYR A 1 186 ? 17.307  57.429 8.631  1.00 18.76 ? 186 TYR A CD1 1 
ATOM   1459 C CD2 . TYR A 1 186 ? 16.776  55.860 10.350 1.00 19.34 ? 186 TYR A CD2 1 
ATOM   1460 C CE1 . TYR A 1 186 ? 16.737  56.596 7.690  1.00 21.99 ? 186 TYR A CE1 1 
ATOM   1461 C CE2 . TYR A 1 186 ? 16.190  55.018 9.400  1.00 20.03 ? 186 TYR A CE2 1 
ATOM   1462 C CZ  . TYR A 1 186 ? 16.167  55.408 8.075  1.00 16.10 ? 186 TYR A CZ  1 
ATOM   1463 O OH  . TYR A 1 186 ? 15.607  54.616 7.110  1.00 20.75 ? 186 TYR A OH  1 
ATOM   1464 N N   . ILE A 1 187 ? 17.487  59.249 13.770 1.00 13.89 ? 187 ILE A N   1 
ATOM   1465 C CA  . ILE A 1 187 ? 18.149  59.694 14.979 1.00 15.04 ? 187 ILE A CA  1 
ATOM   1466 C C   . ILE A 1 187 ? 18.749  58.490 15.671 1.00 16.76 ? 187 ILE A C   1 
ATOM   1467 O O   . ILE A 1 187 ? 18.133  57.426 15.753 1.00 16.27 ? 187 ILE A O   1 
ATOM   1468 C CB  . ILE A 1 187 ? 17.169  60.445 15.910 1.00 20.18 ? 187 ILE A CB  1 
ATOM   1469 C CG1 . ILE A 1 187 ? 17.862  60.891 17.208 1.00 20.00 ? 187 ILE A CG1 1 
ATOM   1470 C CG2 . ILE A 1 187 ? 15.932  59.621 16.177 1.00 17.84 ? 187 ILE A CG2 1 
ATOM   1471 C CD1 . ILE A 1 187 ? 17.063  61.908 18.015 1.00 21.12 ? 187 ILE A CD1 1 
ATOM   1472 N N   . ARG A 1 188 ? 19.943  58.659 16.188 1.00 14.97 ? 188 ARG A N   1 
ATOM   1473 C CA  . ARG A 1 188 ? 20.534  57.661 17.056 1.00 14.86 ? 188 ARG A CA  1 
ATOM   1474 C C   . ARG A 1 188 ? 20.370  58.157 18.483 1.00 18.96 ? 188 ARG A C   1 
ATOM   1475 O O   . ARG A 1 188 ? 20.839  59.248 18.821 1.00 24.87 ? 188 ARG A O   1 
ATOM   1476 C CB  . ARG A 1 188 ? 21.995  57.443 16.680 1.00 20.34 ? 188 ARG A CB  1 
ATOM   1477 C CG  . ARG A 1 188 ? 22.138  56.714 15.358 1.00 21.16 ? 188 ARG A CG  1 
ATOM   1478 C CD  . ARG A 1 188 ? 23.575  56.611 14.964 1.00 19.37 ? 188 ARG A CD  1 
ATOM   1479 N NE  . ARG A 1 188 ? 24.107  57.935 14.686 1.00 14.71 ? 188 ARG A NE  1 
ATOM   1480 C CZ  . ARG A 1 188 ? 25.335  58.329 14.997 1.00 23.09 ? 188 ARG A CZ  1 
ATOM   1481 N NH1 . ARG A 1 188 ? 26.211  57.500 15.545 1.00 22.34 ? 188 ARG A NH1 1 
ATOM   1482 N NH2 . ARG A 1 188 ? 25.703  59.577 14.723 1.00 19.03 ? 188 ARG A NH2 1 
ATOM   1483 N N   . ILE A 1 189 ? 19.671  57.382 19.307 1.00 22.44 ? 189 ILE A N   1 
ATOM   1484 C CA  . ILE A 1 189 ? 19.340  57.781 20.668 1.00 22.96 ? 189 ILE A CA  1 
ATOM   1485 C C   . ILE A 1 189 ? 20.181  56.956 21.624 1.00 23.99 ? 189 ILE A C   1 
ATOM   1486 O O   . ILE A 1 189 ? 20.215  55.727 21.519 1.00 22.38 ? 189 ILE A O   1 
ATOM   1487 C CB  . ILE A 1 189 ? 17.837  57.611 20.954 1.00 23.26 ? 189 ILE A CB  1 
ATOM   1488 C CG1 . ILE A 1 189 ? 17.015  58.496 20.015 1.00 18.34 ? 189 ILE A CG1 1 
ATOM   1489 C CG2 . ILE A 1 189 ? 17.520  57.865 22.417 1.00 26.61 ? 189 ILE A CG2 1 
ATOM   1490 C CD1 . ILE A 1 189 ? 15.549  58.497 20.333 1.00 20.36 ? 189 ILE A CD1 1 
ATOM   1491 N N   . LYS A 1 190 ? 20.840  57.632 22.566 1.00 19.95 ? 190 LYS A N   1 
ATOM   1492 C CA  . LYS A 1 190 ? 21.720  56.972 23.523 1.00 15.27 ? 190 LYS A CA  1 
ATOM   1493 C C   . LYS A 1 190 ? 20.983  55.853 24.246 1.00 19.11 ? 190 LYS A C   1 
ATOM   1494 O O   . LYS A 1 190 ? 19.815  55.997 24.613 1.00 18.89 ? 190 LYS A O   1 
ATOM   1495 C CB  . LYS A 1 190 ? 22.226  58.010 24.541 1.00 22.62 ? 190 LYS A CB  1 
ATOM   1496 C CG  . LYS A 1 190 ? 23.157  57.520 25.674 1.00 22.55 ? 190 LYS A CG  1 
ATOM   1497 C CD  . LYS A 1 190 ? 24.544  57.101 25.157 1.00 26.24 ? 190 LYS A CD  1 
ATOM   1498 C CE  . LYS A 1 190 ? 25.567  56.934 26.307 1.00 25.25 ? 190 LYS A CE  1 
ATOM   1499 N NZ  . LYS A 1 190 ? 25.910  58.221 26.976 1.00 26.99 ? 190 LYS A NZ  1 
ATOM   1500 N N   . ARG A 1 191 ? 21.665  54.730 24.453 1.00 24.14 ? 191 ARG A N   1 
ATOM   1501 C CA  . ARG A 1 191 ? 21.145  53.667 25.304 1.00 25.85 ? 191 ARG A CA  1 
ATOM   1502 C C   . ARG A 1 191 ? 22.212  53.317 26.334 1.00 21.22 ? 191 ARG A C   1 
ATOM   1503 O O   . ARG A 1 191 ? 23.353  53.777 26.256 1.00 25.59 ? 191 ARG A O   1 
ATOM   1504 C CB  . ARG A 1 191 ? 20.717  52.435 24.484 1.00 22.70 ? 191 ARG A CB  1 
ATOM   1505 C CG  . ARG A 1 191 ? 21.861  51.599 23.966 1.00 19.40 ? 191 ARG A CG  1 
ATOM   1506 C CD  . ARG A 1 191 ? 21.350  50.363 23.247 1.00 21.44 ? 191 ARG A CD  1 
ATOM   1507 N NE  . ARG A 1 191 ? 22.450  49.476 22.879 1.00 24.28 ? 191 ARG A NE  1 
ATOM   1508 C CZ  . ARG A 1 191 ? 22.986  48.580 23.699 1.00 20.37 ? 191 ARG A CZ  1 
ATOM   1509 N NH1 . ARG A 1 191 ? 22.598  48.476 24.960 1.00 12.94 ? 191 ARG A NH1 1 
ATOM   1510 N NH2 . ARG A 1 191 ? 23.962  47.798 23.254 1.00 24.54 ? 191 ARG A NH2 1 
ATOM   1511 N N   . GLY A 1 192 ? 21.850  52.463 27.285 1.00 20.30 ? 192 GLY A N   1 
ATOM   1512 C CA  . GLY A 1 192 ? 22.815  52.038 28.278 1.00 25.91 ? 192 GLY A CA  1 
ATOM   1513 C C   . GLY A 1 192 ? 23.000  53.015 29.420 1.00 21.29 ? 192 GLY A C   1 
ATOM   1514 O O   . GLY A 1 192 ? 24.010  52.940 30.129 1.00 19.71 ? 192 GLY A O   1 
ATOM   1515 N N   . THR A 1 193 ? 22.050  53.933 29.620 1.00 19.99 ? 193 THR A N   1 
ATOM   1516 C CA  . THR A 1 193 ? 22.133  54.933 30.679 1.00 23.64 ? 193 THR A CA  1 
ATOM   1517 C C   . THR A 1 193 ? 21.638  54.416 32.017 1.00 23.56 ? 193 THR A C   1 
ATOM   1518 O O   . THR A 1 193 ? 21.809  55.104 33.029 1.00 25.89 ? 193 THR A O   1 
ATOM   1519 C CB  . THR A 1 193 ? 21.320  56.188 30.323 1.00 28.13 ? 193 THR A CB  1 
ATOM   1520 O OG1 . THR A 1 193 ? 19.920  55.903 30.443 1.00 27.83 ? 193 THR A OG1 1 
ATOM   1521 C CG2 . THR A 1 193 ? 21.634  56.703 28.915 1.00 21.65 ? 193 THR A CG2 1 
ATOM   1522 N N   . GLY A 1 194 ? 21.001  53.248 32.046 1.00 31.30 ? 194 GLY A N   1 
ATOM   1523 C CA  . GLY A 1 194 ? 20.484  52.708 33.284 1.00 36.57 ? 194 GLY A CA  1 
ATOM   1524 C C   . GLY A 1 194 ? 19.149  53.276 33.681 1.00 32.46 ? 194 GLY A C   1 
ATOM   1525 O O   . GLY A 1 194 ? 18.610  52.894 34.729 1.00 40.23 ? 194 GLY A O   1 
ATOM   1526 N N   . ASN A 1 195 ? 18.605  54.178 32.877 1.00 33.10 ? 195 ASN A N   1 
ATOM   1527 C CA  . ASN A 1 195 ? 17.281  54.729 33.101 1.00 38.89 ? 195 ASN A CA  1 
ATOM   1528 C C   . ASN A 1 195 ? 16.269  53.769 32.495 1.00 34.83 ? 195 ASN A C   1 
ATOM   1529 O O   . ASN A 1 195 ? 16.289  53.520 31.284 1.00 32.50 ? 195 ASN A O   1 
ATOM   1530 C CB  . ASN A 1 195 ? 17.187  56.110 32.455 1.00 33.10 ? 195 ASN A CB  1 
ATOM   1531 C CG  . ASN A 1 195 ? 15.770  56.596 32.320 1.00 41.41 ? 195 ASN A CG  1 
ATOM   1532 O OD1 . ASN A 1 195 ? 14.876  56.186 33.068 1.00 38.13 ? 195 ASN A OD1 1 
ATOM   1533 N ND2 . ASN A 1 195 ? 15.542  57.446 31.328 1.00 30.31 ? 195 ASN A ND2 1 
ATOM   1534 N N   . SER A 1 196 ? 15.403  53.207 33.338 1.00 41.22 ? 196 SER A N   1 
ATOM   1535 C CA  . SER A 1 196 ? 14.463  52.206 32.846 1.00 39.85 ? 196 SER A CA  1 
ATOM   1536 C C   . SER A 1 196 ? 13.568  52.777 31.757 1.00 26.58 ? 196 SER A C   1 
ATOM   1537 O O   . SER A 1 196 ? 13.144  52.046 30.854 1.00 24.40 ? 196 SER A O   1 
ATOM   1538 C CB  . SER A 1 196 ? 13.628  51.656 34.007 1.00 33.46 ? 196 SER A CB  1 
ATOM   1539 O OG  . SER A 1 196 ? 13.029  52.708 34.751 1.00 36.81 ? 196 SER A OG  1 
ATOM   1540 N N   . TYR A 1 197 ? 13.290  54.079 31.813 1.00 21.89 ? 197 TYR A N   1 
ATOM   1541 C CA  . TYR A 1 197 ? 12.428  54.695 30.820 1.00 25.08 ? 197 TYR A CA  1 
ATOM   1542 C C   . TYR A 1 197 ? 13.082  54.736 29.448 1.00 20.60 ? 197 TYR A C   1 
ATOM   1543 O O   . TYR A 1 197 ? 12.373  54.825 28.440 1.00 18.50 ? 197 TYR A O   1 
ATOM   1544 C CB  . TYR A 1 197 ? 12.095  56.130 31.223 1.00 27.06 ? 197 TYR A CB  1 
ATOM   1545 C CG  . TYR A 1 197 ? 11.164  56.243 32.390 1.00 32.82 ? 197 TYR A CG  1 
ATOM   1546 C CD1 . TYR A 1 197 ? 9.796   56.078 32.238 1.00 40.29 ? 197 TYR A CD1 1 
ATOM   1547 C CD2 . TYR A 1 197 ? 11.658  56.549 33.655 1.00 38.49 ? 197 TYR A CD2 1 
ATOM   1548 C CE1 . TYR A 1 197 ? 8.938   56.187 33.329 1.00 44.40 ? 197 TYR A CE1 1 
ATOM   1549 C CE2 . TYR A 1 197 ? 10.818  56.662 34.745 1.00 41.43 ? 197 TYR A CE2 1 
ATOM   1550 C CZ  . TYR A 1 197 ? 9.458   56.483 34.579 1.00 44.34 ? 197 TYR A CZ  1 
ATOM   1551 O OH  . TYR A 1 197 ? 8.622   56.600 35.667 1.00 48.28 ? 197 TYR A OH  1 
ATOM   1552 N N   . GLY A 1 198 ? 14.411  54.705 29.387 1.00 22.51 ? 198 GLY A N   1 
ATOM   1553 C CA  . GLY A 1 198 ? 15.087  55.025 28.144 1.00 23.39 ? 198 GLY A CA  1 
ATOM   1554 C C   . GLY A 1 198 ? 15.254  56.515 27.948 1.00 17.24 ? 198 GLY A C   1 
ATOM   1555 O O   . GLY A 1 198 ? 14.465  57.306 28.470 1.00 18.54 ? 198 GLY A O   1 
ATOM   1556 N N   . VAL A 1 199 ? 16.266  56.918 27.188 1.00 20.91 ? 199 VAL A N   1 
ATOM   1557 C CA  . VAL A 1 199 ? 16.361  58.318 26.808 1.00 22.82 ? 199 VAL A CA  1 
ATOM   1558 C C   . VAL A 1 199 ? 15.082  58.698 26.076 1.00 22.85 ? 199 VAL A C   1 
ATOM   1559 O O   . VAL A 1 199 ? 14.634  57.983 25.170 1.00 24.48 ? 199 VAL A O   1 
ATOM   1560 C CB  . VAL A 1 199 ? 17.606  58.552 25.935 1.00 24.57 ? 199 VAL A CB  1 
ATOM   1561 C CG1 . VAL A 1 199 ? 17.633  59.969 25.405 1.00 28.26 ? 199 VAL A CG1 1 
ATOM   1562 C CG2 . VAL A 1 199 ? 18.887  58.245 26.701 1.00 21.31 ? 199 VAL A CG2 1 
ATOM   1563 N N   . CYS A 1 200 ? 14.478  59.820 26.482 1.00 20.64 ? 200 CYS A N   1 
ATOM   1564 C CA  . CYS A 1 200 ? 13.196  60.301 25.959 1.00 18.56 ? 200 CYS A CA  1 
ATOM   1565 C C   . CYS A 1 200 ? 12.056  59.300 26.119 1.00 21.70 ? 200 CYS A C   1 
ATOM   1566 O O   . CYS A 1 200 ? 11.114  59.298 25.323 1.00 19.51 ? 200 CYS A O   1 
ATOM   1567 C CB  . CYS A 1 200 ? 13.322  60.690 24.479 1.00 24.27 ? 200 CYS A CB  1 
ATOM   1568 S SG  . CYS A 1 200 ? 14.701  61.798 24.127 1.00 35.09 ? 200 CYS A SG  1 
ATOM   1569 N N   . GLY A 1 201 ? 12.103  58.452 27.145 1.00 25.95 ? 201 GLY A N   1 
ATOM   1570 C CA  . GLY A 1 201 ? 11.019  57.500 27.333 1.00 18.57 ? 201 GLY A CA  1 
ATOM   1571 C C   . GLY A 1 201 ? 10.971  56.418 26.280 1.00 23.52 ? 201 GLY A C   1 
ATOM   1572 O O   . GLY A 1 201 ? 9.915   55.812 26.064 1.00 17.92 ? 201 GLY A O   1 
ATOM   1573 N N   . LEU A 1 202 ? 12.101  56.158 25.619 1.00 21.26 ? 202 LEU A N   1 
ATOM   1574 C CA  . LEU A 1 202 ? 12.133  55.282 24.456 1.00 19.80 ? 202 LEU A CA  1 
ATOM   1575 C C   . LEU A 1 202 ? 11.641  53.866 24.761 1.00 18.50 ? 202 LEU A C   1 
ATOM   1576 O O   . LEU A 1 202 ? 11.278  53.132 23.838 1.00 23.62 ? 202 LEU A O   1 
ATOM   1577 C CB  . LEU A 1 202 ? 13.554  55.258 23.889 1.00 19.00 ? 202 LEU A CB  1 
ATOM   1578 C CG  . LEU A 1 202 ? 13.668  54.520 22.556 1.00 25.57 ? 202 LEU A CG  1 
ATOM   1579 C CD1 . LEU A 1 202 ? 12.729  55.207 21.555 1.00 22.38 ? 202 LEU A CD1 1 
ATOM   1580 C CD2 . LEU A 1 202 ? 15.085  54.480 22.038 1.00 22.40 ? 202 LEU A CD2 1 
ATOM   1581 N N   . TYR A 1 203 ? 11.615  53.450 26.021 1.00 16.61 ? 203 TYR A N   1 
ATOM   1582 C CA  . TYR A 1 203 ? 11.204  52.090 26.328 1.00 17.82 ? 203 TYR A CA  1 
ATOM   1583 C C   . TYR A 1 203 ? 9.767   52.020 26.829 1.00 19.32 ? 203 TYR A C   1 
ATOM   1584 O O   . TYR A 1 203 ? 9.355   50.978 27.342 1.00 28.11 ? 203 TYR A O   1 
ATOM   1585 C CB  . TYR A 1 203 ? 12.136  51.488 27.387 1.00 24.38 ? 203 TYR A CB  1 
ATOM   1586 C CG  . TYR A 1 203 ? 13.607  51.634 27.073 1.00 21.52 ? 203 TYR A CG  1 
ATOM   1587 C CD1 . TYR A 1 203 ? 14.058  51.733 25.757 1.00 19.85 ? 203 TYR A CD1 1 
ATOM   1588 C CD2 . TYR A 1 203 ? 14.540  51.709 28.094 1.00 19.24 ? 203 TYR A CD2 1 
ATOM   1589 C CE1 . TYR A 1 203 ? 15.389  51.889 25.477 1.00 17.45 ? 203 TYR A CE1 1 
ATOM   1590 C CE2 . TYR A 1 203 ? 15.881  51.869 27.820 1.00 23.19 ? 203 TYR A CE2 1 
ATOM   1591 C CZ  . TYR A 1 203 ? 16.300  51.963 26.511 1.00 21.41 ? 203 TYR A CZ  1 
ATOM   1592 O OH  . TYR A 1 203 ? 17.636  52.128 26.233 1.00 20.00 ? 203 TYR A OH  1 
ATOM   1593 N N   . THR A 1 204 ? 8.982   53.085 26.648 1.00 19.55 ? 204 THR A N   1 
ATOM   1594 C CA  . THR A 1 204 ? 7.665   53.143 27.276 1.00 17.20 ? 204 THR A CA  1 
ATOM   1595 C C   . THR A 1 204 ? 6.664   52.185 26.639 1.00 22.37 ? 204 THR A C   1 
ATOM   1596 O O   . THR A 1 204 ? 5.936   51.483 27.350 1.00 21.99 ? 204 THR A O   1 
ATOM   1597 C CB  . THR A 1 204 ? 7.147   54.581 27.195 1.00 20.18 ? 204 THR A CB  1 
ATOM   1598 O OG1 . THR A 1 204 ? 8.026   55.450 27.919 1.00 20.03 ? 204 THR A OG1 1 
ATOM   1599 C CG2 . THR A 1 204 ? 5.727   54.702 27.723 1.00 24.87 ? 204 THR A CG2 1 
ATOM   1600 N N   . SER A 1 205 ? 6.629   52.098 25.313 1.00 15.81 ? 205 SER A N   1 
ATOM   1601 C CA  . SER A 1 205 ? 5.521   51.395 24.666 1.00 25.48 ? 205 SER A CA  1 
ATOM   1602 C C   . SER A 1 205 ? 5.997   51.019 23.264 1.00 19.36 ? 205 SER A C   1 
ATOM   1603 O O   . SER A 1 205 ? 5.961   51.849 22.352 1.00 23.90 ? 205 SER A O   1 
ATOM   1604 C CB  . SER A 1 205 ? 4.268   52.261 24.623 1.00 22.02 ? 205 SER A CB  1 
ATOM   1605 O OG  . SER A 1 205 ? 3.164   51.550 24.087 1.00 26.99 ? 205 SER A OG  1 
ATOM   1606 N N   . SER A 1 206 ? 6.388   49.768 23.099 1.00 16.35 ? 206 SER A N   1 
ATOM   1607 C CA  . SER A 1 206 ? 7.017   49.320 21.873 1.00 15.43 ? 206 SER A CA  1 
ATOM   1608 C C   . SER A 1 206 ? 6.320   48.065 21.396 1.00 21.00 ? 206 SER A C   1 
ATOM   1609 O O   . SER A 1 206 ? 6.138   47.118 22.168 1.00 27.51 ? 206 SER A O   1 
ATOM   1610 C CB  . SER A 1 206 ? 8.510   49.099 22.069 1.00 11.84 ? 206 SER A CB  1 
ATOM   1611 O OG  . SER A 1 206 ? 8.741   48.482 23.317 1.00 33.35 ? 206 SER A OG  1 
ATOM   1612 N N   . PHE A 1 207 ? 5.988   48.042 20.110 1.00 23.25 ? 207 PHE A N   1 
ATOM   1613 C CA  . PHE A 1 207 ? 5.208   46.974 19.509 1.00 22.38 ? 207 PHE A CA  1 
ATOM   1614 C C   . PHE A 1 207 ? 5.844   46.593 18.189 1.00 21.98 ? 207 PHE A C   1 
ATOM   1615 O O   . PHE A 1 207 ? 6.534   47.398 17.552 1.00 16.04 ? 207 PHE A O   1 
ATOM   1616 C CB  . PHE A 1 207 ? 3.757   47.394 19.199 1.00 13.94 ? 207 PHE A CB  1 
ATOM   1617 C CG  . PHE A 1 207 ? 2.912   47.640 20.409 1.00 24.55 ? 207 PHE A CG  1 
ATOM   1618 C CD1 . PHE A 1 207 ? 2.221   46.601 21.016 1.00 19.81 ? 207 PHE A CD1 1 
ATOM   1619 C CD2 . PHE A 1 207 ? 2.807   48.919 20.942 1.00 20.27 ? 207 PHE A CD2 1 
ATOM   1620 C CE1 . PHE A 1 207 ? 1.441   46.832 22.129 1.00 21.34 ? 207 PHE A CE1 1 
ATOM   1621 C CE2 . PHE A 1 207 ? 2.021   49.161 22.060 1.00 20.20 ? 207 PHE A CE2 1 
ATOM   1622 C CZ  . PHE A 1 207 ? 1.342   48.116 22.654 1.00 27.17 ? 207 PHE A CZ  1 
ATOM   1623 N N   . TYR A 1 208 ? 5.613   45.349 17.795 1.00 23.22 ? 208 TYR A N   1 
ATOM   1624 C CA  . TYR A 1 208 ? 6.072   44.905 16.495 1.00 17.22 ? 208 TYR A CA  1 
ATOM   1625 C C   . TYR A 1 208 ? 5.043   43.932 15.962 1.00 17.91 ? 208 TYR A C   1 
ATOM   1626 O O   . TYR A 1 208 ? 4.381   43.235 16.744 1.00 25.08 ? 208 TYR A O   1 
ATOM   1627 C CB  . TYR A 1 208 ? 7.466   44.276 16.586 1.00 19.19 ? 208 TYR A CB  1 
ATOM   1628 C CG  . TYR A 1 208 ? 7.558   43.172 17.612 1.00 21.71 ? 208 TYR A CG  1 
ATOM   1629 C CD1 . TYR A 1 208 ? 7.904   43.479 18.920 1.00 18.05 ? 208 TYR A CD1 1 
ATOM   1630 C CD2 . TYR A 1 208 ? 7.406   41.828 17.265 1.00 18.50 ? 208 TYR A CD2 1 
ATOM   1631 C CE1 . TYR A 1 208 ? 8.034   42.508 19.876 1.00 19.76 ? 208 TYR A CE1 1 
ATOM   1632 C CE2 . TYR A 1 208 ? 7.535   40.825 18.234 1.00 27.56 ? 208 TYR A CE2 1 
ATOM   1633 C CZ  . TYR A 1 208 ? 7.855   41.181 19.538 1.00 23.62 ? 208 TYR A CZ  1 
ATOM   1634 O OH  . TYR A 1 208 ? 7.977   40.230 20.528 1.00 33.19 ? 208 TYR A OH  1 
ATOM   1635 N N   . PRO A 1 209 ? 4.893   43.847 14.648 1.00 17.74 ? 209 PRO A N   1 
ATOM   1636 C CA  . PRO A 1 209 ? 3.970   42.873 14.076 1.00 18.93 ? 209 PRO A CA  1 
ATOM   1637 C C   . PRO A 1 209 ? 4.596   41.500 14.032 1.00 24.35 ? 209 PRO A C   1 
ATOM   1638 O O   . PRO A 1 209 ? 5.815   41.341 13.918 1.00 20.97 ? 209 PRO A O   1 
ATOM   1639 C CB  . PRO A 1 209 ? 3.765   43.396 12.650 1.00 20.73 ? 209 PRO A CB  1 
ATOM   1640 C CG  . PRO A 1 209 ? 5.106   43.971 12.326 1.00 15.44 ? 209 PRO A CG  1 
ATOM   1641 C CD  . PRO A 1 209 ? 5.520   44.674 13.604 1.00 15.42 ? 209 PRO A CD  1 
ATOM   1642 N N   . VAL A 1 210 ? 3.746   40.497 14.117 1.00 28.40 ? 210 VAL A N   1 
ATOM   1643 C CA  . VAL A 1 210 ? 4.182   39.123 13.972 1.00 28.35 ? 210 VAL A CA  1 
ATOM   1644 C C   . VAL A 1 210 ? 3.575   38.607 12.680 1.00 33.31 ? 210 VAL A C   1 
ATOM   1645 O O   . VAL A 1 210 ? 2.390   38.845 12.391 1.00 32.51 ? 210 VAL A O   1 
ATOM   1646 C CB  . VAL A 1 210 ? 3.832   38.227 15.178 1.00 32.09 ? 210 VAL A CB  1 
ATOM   1647 C CG1 . VAL A 1 210 ? 2.361   37.972 15.264 1.00 35.27 ? 210 VAL A CG1 1 
ATOM   1648 C CG2 . VAL A 1 210 ? 4.567   36.907 15.053 1.00 50.16 ? 210 VAL A CG2 1 
ATOM   1649 N N   . LYS A 1 211 ? 4.398   37.921 11.897 1.00 36.85 ? 211 LYS A N   1 
ATOM   1650 C CA  . LYS A 1 211 ? 3.995   37.375 10.612 1.00 32.44 ? 211 LYS A CA  1 
ATOM   1651 C C   . LYS A 1 211 ? 4.670   36.030 10.446 1.00 38.07 ? 211 LYS A C   1 
ATOM   1652 O O   . LYS A 1 211 ? 5.902   35.946 10.389 1.00 33.86 ? 211 LYS A O   1 
ATOM   1653 C CB  . LYS A 1 211 ? 4.344   38.276 9.433  1.00 32.24 ? 211 LYS A CB  1 
ATOM   1654 C CG  . LYS A 1 211 ? 3.302   38.070 8.355  1.00 47.12 ? 211 LYS A CG  1 
ATOM   1655 C CD  . LYS A 1 211 ? 3.901   37.743 6.995  1.00 42.79 ? 211 LYS A CD  1 
ATOM   1656 C CE  . LYS A 1 211 ? 2.794   37.698 5.945  1.00 34.53 ? 211 LYS A CE  1 
ATOM   1657 N NZ  . LYS A 1 211 ? 1.624   36.897 6.444  1.00 38.02 ? 211 LYS A NZ  1 
ATOM   1658 N N   . ASN A 1 212 ? 3.851   34.994 10.347 1.00 40.27 ? 212 ASN A N   1 
ATOM   1659 C CA  . ASN A 1 212 ? 4.322   33.634 10.183 1.00 50.83 ? 212 ASN A CA  1 
ATOM   1660 C C   . ASN A 1 212 ? 4.764   33.424 8.736  1.00 57.19 ? 212 ASN A C   1 
ATOM   1661 O O   . ASN A 1 212 ? 5.652   32.616 8.452  1.00 58.90 ? 212 ASN A O   1 
ATOM   1662 C CB  . ASN A 1 212 ? 3.203   32.659 10.553 1.00 40.08 ? 212 ASN A CB  1 
ATOM   1663 C CG  . ASN A 1 212 ? 2.643   32.919 11.945 1.00 54.67 ? 212 ASN A CG  1 
ATOM   1664 O OD1 . ASN A 1 212 ? 3.347   33.399 12.838 1.00 43.92 ? 212 ASN A OD1 1 
ATOM   1665 N ND2 . ASN A 1 212 ? 1.357   32.636 12.122 1.00 51.60 ? 212 ASN A ND2 1 
ATOM   1666 O OXT . ASN A 1 212 ? 4.256   34.075 7.816  1.00 49.84 ? 212 ASN A OXT 1 
HETATM 1667 C C1  . E64 B 2 .   ? 2.552   62.451 16.011 0.75 29.43 ? 301 E64 A C1  1 
HETATM 1668 O O1  . E64 B 2 .   ? 2.038   62.667 14.917 0.75 29.59 ? 301 E64 A O1  1 
HETATM 1669 O O2  . E64 B 2 .   ? 3.586   63.043 16.459 0.75 33.01 ? 301 E64 A O2  1 
HETATM 1670 C C2  . E64 B 2 .   ? 1.944   61.375 16.914 0.75 32.37 ? 301 E64 A C2  1 
HETATM 1671 C C3  . E64 B 2 .   ? 0.546   61.667 17.471 0.75 30.70 ? 301 E64 A C3  1 
HETATM 1672 O O3  . E64 B 2 .   ? 0.508   62.903 18.147 0.75 27.97 ? 301 E64 A O3  1 
HETATM 1673 C C4  . E64 B 2 .   ? 0.094   60.473 18.328 0.75 24.10 ? 301 E64 A C4  1 
HETATM 1674 O O4  . E64 B 2 .   ? -0.371  59.470 17.803 0.75 23.76 ? 301 E64 A O4  1 
HETATM 1675 N N1  . E64 B 2 .   ? 0.256   60.578 19.656 0.75 28.84 ? 301 E64 A N1  1 
HETATM 1676 C C6  . E64 B 2 .   ? -0.107  59.510 20.570 0.75 29.21 ? 301 E64 A C6  1 
HETATM 1677 C C7  . E64 B 2 .   ? 0.967   59.367 21.634 0.75 27.13 ? 301 E64 A C7  1 
HETATM 1678 C C8  . E64 B 2 .   ? 2.146   58.474 21.265 0.75 27.30 ? 301 E64 A C8  1 
HETATM 1679 C C9  . E64 B 2 .   ? 1.760   57.559 20.105 0.75 20.46 ? 301 E64 A C9  1 
HETATM 1680 C C10 . E64 B 2 .   ? 2.563   57.661 22.488 0.75 23.66 ? 301 E64 A C10 1 
HETATM 1681 C C11 . E64 B 2 .   ? -1.428  59.816 21.271 0.75 31.78 ? 301 E64 A C11 1 
HETATM 1682 O O5  . E64 B 2 .   ? -1.659  60.943 21.694 0.75 31.82 ? 301 E64 A O5  1 
HETATM 1683 N N2  . E64 B 2 .   ? -2.254  58.764 21.389 0.75 30.61 ? 301 E64 A N2  1 
HETATM 1684 C C12 . E64 B 2 .   ? -3.556  58.805 22.023 0.75 28.74 ? 301 E64 A C12 1 
HETATM 1685 C C13 . E64 B 2 .   ? -4.675  59.212 21.070 0.75 30.40 ? 301 E64 A C13 1 
HETATM 1686 C C14 . E64 B 2 .   ? -4.663  60.696 20.727 0.75 34.55 ? 301 E64 A C14 1 
HETATM 1687 C C15 . E64 B 2 .   ? -5.269  61.530 21.850 0.75 43.29 ? 301 E64 A C15 1 
HETATM 1688 N N3  . E64 B 2 .   ? -6.706  61.342 21.939 0.75 43.03 ? 301 E64 A N3  1 
HETATM 1689 C C16 . E64 B 2 .   ? -7.586  61.843 21.067 0.75 42.24 ? 301 E64 A C16 1 
HETATM 1690 N N4  . E64 B 2 .   ? -7.229  62.577 20.028 0.75 39.36 ? 301 E64 A N4  1 
HETATM 1691 N N5  . E64 B 2 .   ? -8.886  61.601 21.248 0.75 41.23 ? 301 E64 A N5  1 
HETATM 1692 O O   . HOH C 3 .   ? 11.016  48.929 7.427  1.00 11.18 ? 401 HOH A O   1 
HETATM 1693 O O   . HOH C 3 .   ? 2.865   42.941 -0.398 1.00 21.74 ? 402 HOH A O   1 
HETATM 1694 O O   . HOH C 3 .   ? 11.425  47.723 26.687 1.00 17.42 ? 403 HOH A O   1 
HETATM 1695 O O   . HOH C 3 .   ? 7.085   48.220 25.476 1.00 17.35 ? 404 HOH A O   1 
HETATM 1696 O O   . HOH C 3 .   ? 17.845  54.709 25.972 1.00 13.89 ? 405 HOH A O   1 
HETATM 1697 O O   . HOH C 3 .   ? 20.945  57.951 8.877  1.00 14.25 ? 406 HOH A O   1 
HETATM 1698 O O   . HOH C 3 .   ? 15.590  63.551 0.329  1.00 16.15 ? 407 HOH A O   1 
HETATM 1699 O O   . HOH C 3 .   ? -11.954 59.833 13.269 1.00 14.27 ? 408 HOH A O   1 
HETATM 1700 O O   . HOH C 3 .   ? 5.145   64.731 14.987 1.00 22.77 ? 409 HOH A O   1 
HETATM 1701 O O   . HOH C 3 .   ? 19.662  67.601 9.122  1.00 22.65 ? 410 HOH A O   1 
HETATM 1702 O O   . HOH C 3 .   ? 26.446  54.333 14.338 1.00 21.08 ? 411 HOH A O   1 
HETATM 1703 O O   . HOH C 3 .   ? 10.376  51.255 6.551  1.00 19.71 ? 412 HOH A O   1 
HETATM 1704 O O   . HOH C 3 .   ? 7.915   54.115 5.786  1.00 21.62 ? 413 HOH A O   1 
HETATM 1705 O O   . HOH C 3 .   ? 19.221  54.049 28.322 1.00 21.96 ? 414 HOH A O   1 
HETATM 1706 O O   . HOH C 3 .   ? 9.378   66.182 3.386  1.00 17.23 ? 415 HOH A O   1 
HETATM 1707 O O   . HOH C 3 .   ? 16.749  48.733 30.805 1.00 16.17 ? 416 HOH A O   1 
HETATM 1708 O O   . HOH C 3 .   ? -1.651  62.501 -2.050 1.00 17.34 ? 417 HOH A O   1 
# 
