data_8YYA
# 
_entry.id   8YYA 
# 
_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   8YYA         pdb_00008yya 10.2210/pdb8yya/pdb 
WWPDB D_1300046600 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-09 
_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                        8YYA 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              saimarasheed1@hotmail.com 
_pdbx_contact_author.name_first         Saima 
_pdbx_contact_author.name_last          Rasheed 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6742-3003 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rasheed, S.' 1 0000-0002-6742-3003 
'Arif, R.'    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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal Structure of Concanavalin A Complexed with 5-Fluorouracil' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rasheed, S.' 1 0000-0002-6742-3003 
primary 'Arif, R.'    2 ?                   
# 
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 Concanavalin-Br      25622.385 1  ? ? ? ? 
2 non-polymer syn 5-FLUOROURACIL       130.077   1  ? ? ? ? 
3 non-polymer syn 'CALCIUM ION'        40.078    1  ? ? ? ? 
4 non-polymer syn 'MANGANESE (II) ION' 54.938    1  ? ? ? ? 
5 non-polymer syn 'SULFATE ION'        96.063    1  ? ? ? ? 
6 water       nat water                18.015    13 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Con Br' 
# 
_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       
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVS
SNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVS
SNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
_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 5-FLUOROURACIL       URF 
3 'CALCIUM ION'        CA  
4 'MANGANESE (II) ION' MN  
5 'SULFATE ION'        SO4 
6 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ASP n 
1 3   THR n 
1 4   ILE n 
1 5   VAL n 
1 6   ALA n 
1 7   VAL n 
1 8   GLU n 
1 9   LEU n 
1 10  ASP n 
1 11  THR n 
1 12  TYR n 
1 13  PRO n 
1 14  ASN n 
1 15  THR n 
1 16  ASP n 
1 17  ILE n 
1 18  GLY n 
1 19  ASP n 
1 20  PRO n 
1 21  SER n 
1 22  TYR n 
1 23  PRO n 
1 24  HIS n 
1 25  ILE n 
1 26  GLY n 
1 27  ILE n 
1 28  ASP n 
1 29  ILE n 
1 30  LYS n 
1 31  SER n 
1 32  VAL n 
1 33  ARG n 
1 34  SER n 
1 35  LYS n 
1 36  LYS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TRP n 
1 41  ASN n 
1 42  MET n 
1 43  GLN n 
1 44  ASN n 
1 45  GLY n 
1 46  LYS n 
1 47  VAL n 
1 48  GLY n 
1 49  THR n 
1 50  ALA n 
1 51  HIS n 
1 52  ILE n 
1 53  ILE n 
1 54  TYR n 
1 55  ASN n 
1 56  SER n 
1 57  VAL n 
1 58  ASP n 
1 59  LYS n 
1 60  ARG n 
1 61  LEU n 
1 62  SER n 
1 63  ALA n 
1 64  VAL n 
1 65  VAL n 
1 66  SER n 
1 67  TYR n 
1 68  PRO n 
1 69  ASN n 
1 70  ALA n 
1 71  ASP n 
1 72  SER n 
1 73  ALA n 
1 74  THR n 
1 75  VAL n 
1 76  SER n 
1 77  TYR n 
1 78  ASP n 
1 79  VAL n 
1 80  ASP n 
1 81  LEU n 
1 82  ASP n 
1 83  ASN n 
1 84  VAL n 
1 85  LEU n 
1 86  PRO n 
1 87  GLU n 
1 88  TRP n 
1 89  VAL n 
1 90  ARG n 
1 91  VAL n 
1 92  GLY n 
1 93  LEU n 
1 94  SER n 
1 95  ALA n 
1 96  SER n 
1 97  THR n 
1 98  GLY n 
1 99  LEU n 
1 100 TYR n 
1 101 LYS n 
1 102 GLU n 
1 103 THR n 
1 104 ASN n 
1 105 THR n 
1 106 ILE n 
1 107 LEU n 
1 108 SER n 
1 109 TRP n 
1 110 SER n 
1 111 PHE n 
1 112 THR n 
1 113 SER n 
1 114 LYS n 
1 115 LEU n 
1 116 LYS n 
1 117 SER n 
1 118 ASN n 
1 119 SER n 
1 120 THR n 
1 121 HIS n 
1 122 GLU n 
1 123 THR n 
1 124 ASN n 
1 125 ALA n 
1 126 LEU n 
1 127 HIS n 
1 128 PHE n 
1 129 MET n 
1 130 PHE n 
1 131 ASN n 
1 132 GLN n 
1 133 PHE n 
1 134 SER n 
1 135 LYS n 
1 136 ASP n 
1 137 GLN n 
1 138 LYS n 
1 139 ASP n 
1 140 LEU n 
1 141 ILE n 
1 142 LEU n 
1 143 GLN n 
1 144 GLY n 
1 145 ASP n 
1 146 ALA n 
1 147 THR n 
1 148 THR n 
1 149 GLY n 
1 150 THR n 
1 151 ASP n 
1 152 GLY n 
1 153 ASN n 
1 154 LEU n 
1 155 GLU n 
1 156 LEU n 
1 157 THR n 
1 158 ARG n 
1 159 VAL n 
1 160 SER n 
1 161 SER n 
1 162 ASN n 
1 163 GLY n 
1 164 SER n 
1 165 PRO n 
1 166 GLN n 
1 167 GLY n 
1 168 SER n 
1 169 SER n 
1 170 VAL n 
1 171 GLY n 
1 172 ARG n 
1 173 ALA n 
1 174 LEU n 
1 175 PHE n 
1 176 TYR n 
1 177 ALA n 
1 178 PRO n 
1 179 VAL n 
1 180 HIS n 
1 181 ILE n 
1 182 TRP n 
1 183 GLU n 
1 184 SER n 
1 185 SER n 
1 186 ALA n 
1 187 VAL n 
1 188 VAL n 
1 189 ALA n 
1 190 SER n 
1 191 PHE n 
1 192 GLU n 
1 193 ALA n 
1 194 THR n 
1 195 PHE n 
1 196 THR n 
1 197 PHE n 
1 198 LEU n 
1 199 ILE n 
1 200 LYS n 
1 201 SER n 
1 202 PRO n 
1 203 ASP n 
1 204 SER n 
1 205 HIS n 
1 206 PRO n 
1 207 ALA n 
1 208 ASP n 
1 209 GLY n 
1 210 ILE n 
1 211 ALA n 
1 212 PHE n 
1 213 PHE n 
1 214 ILE n 
1 215 SER n 
1 216 ASN n 
1 217 ILE n 
1 218 ASP n 
1 219 SER n 
1 220 SER n 
1 221 ILE n 
1 222 PRO n 
1 223 SER n 
1 224 GLY n 
1 225 SER n 
1 226 THR n 
1 227 GLY n 
1 228 ARG n 
1 229 LEU n 
1 230 LEU n 
1 231 GLY n 
1 232 LEU n 
1 233 PHE n 
1 234 PRO n 
1 235 ASP n 
1 236 ALA n 
1 237 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           237 
_entity_src_nat.common_name                'jack bean' 
_entity_src_nat.pdbx_organism_scientific   'Canavalia ensiformis' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      3823 
_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 
CA  non-polymer         . 'CALCIUM ION'        ? 'Ca 2'           40.078  
GLN 'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE            ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'  149.211 
MN  non-polymer         . 'MANGANESE (II) ION' ? 'Mn 2'           54.938  
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'        ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE             ? 'C9 H11 N O3'    181.189 
URF non-polymer         . 5-FLUOROURACIL       ? 'C4 H3 F N2 O2'  130.077 
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   ALA 1   1   1   ALA ALA A . n 
A 1 2   ASP 2   2   2   ASP ASP A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  TYR 12  12  12  TYR TYR A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  HIS 24  24  24  HIS HIS A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ILE 27  27  27  ILE ILE A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TRP 40  40  40  TRP TRP A . n 
A 1 41  ASN 41  41  41  ASN ASN A . n 
A 1 42  MET 42  42  42  MET MET A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  SER 66  66  66  SER SER 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  ASN 69  69  69  ASN ASN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  TRP 88  88  88  TRP TRP A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 TRP 109 109 109 TRP TRP A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 PHE 111 111 111 PHE PHE A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 MET 129 129 129 MET MET A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLN 132 132 132 GLN GLN A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ILE 141 141 141 ILE ILE A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 GLN 143 143 143 GLN GLN A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 ASN 153 153 153 ASN ASN A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 GLN 166 166 166 GLN GLN A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 VAL 170 170 170 VAL VAL A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 TYR 176 176 176 TYR TYR A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 TRP 182 182 182 TRP TRP A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 GLU 192 192 192 GLU GLU A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 LYS 200 200 200 LYS LYS A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 PHE 213 213 213 PHE PHE A . n 
A 1 214 ILE 214 214 214 ILE ILE A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 PHE 233 233 233 PHE PHE A . n 
A 1 234 PRO 234 234 234 PRO PRO A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ALA 236 236 236 ALA ALA A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        URF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   URF 
_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 URF 1  301 301 URF URF A . 
C 3 CA  1  302 1   CA  CA  A . 
D 4 MN  1  303 1   MN  MN  A . 
E 5 SO4 1  304 1   SO4 SO4 A . 
F 6 HOH 1  401 9   HOH HOH A . 
F 6 HOH 2  402 13  HOH HOH A . 
F 6 HOH 3  403 4   HOH HOH A . 
F 6 HOH 4  404 18  HOH HOH A . 
F 6 HOH 5  405 7   HOH HOH A . 
F 6 HOH 6  406 3   HOH HOH A . 
F 6 HOH 7  407 5   HOH HOH A . 
F 6 HOH 8  408 15  HOH HOH A . 
F 6 HOH 9  409 2   HOH HOH A . 
F 6 HOH 10 410 12  HOH HOH A . 
F 6 HOH 11 411 10  HOH HOH A . 
F 6 HOH 12 412 1   HOH HOH A . 
F 6 HOH 13 413 16  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC         ? ? ? 5.8.0411 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless        ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP         ? ? ? .        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                     8YYA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.781 
_cell.length_a_esd                 ? 
_cell.length_b                     86.546 
_cell.length_b_esd                 ? 
_cell.length_c                     88.637 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8YYA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YYA 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.80 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0. 1M Sodium Accetate buffer pH 5.0 , 5% PEG 6000, 2 M Ammonium Sulphate.' 
_exptl_crystal_grow.pdbx_pH_range   4.5-5.0 
_exptl_crystal_grow.temp            293.5 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'Bruker PHOTON II' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5406 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'SEALED TUBE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'BRUKER D8 QUEST' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5406 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YYA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.94 
_reflns.d_resolution_low                               20.74 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     5189 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.910 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.175 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.94 
_reflns_shell.d_res_low                                     3.14 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           5.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             829 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.722 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.296 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            3.04 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -1.99 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.05 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               5.397 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.907 
_refine.correlation_coeff_Fo_to_Fc_free          0.797 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8YYA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.96 
_refine.ls_d_res_low                             20.74 
_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                     4905 
_refine.ls_number_reflns_R_free                  283 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.58 
_refine.ls_percent_reflns_R_free                 5.5 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19918 
_refine.ls_R_factor_R_free                       0.27389 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19477 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.507 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             21.426 
_refine.overall_SU_ML                            0.383 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.96 
_refine_hist.d_res_low                        20.74 
_refine_hist.number_atoms_solvent             13 
_refine_hist.number_atoms_total               1838 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1809 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         16 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  0.012  1868 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1695 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.422  1.636  2548 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.484  1.572  3916 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 9.339  5.000  236  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.783 5.000  6    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.140 10.000 289  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.062  0.200  292  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  2165 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  415  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 0.776  0.548  947  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.776  0.548  947  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.457  0.984  1182 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.456  0.984  1183 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 0.581  0.608  921  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 0.554  0.578  914  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.089  1.044  1355 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.677  5.80   2054 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 2.676  5.81   2055 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.960 
_refine_ls_shell.d_res_low                        3.035 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             24 
_refine_ls_shell.number_reflns_R_work             344 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.274 
_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   20 
_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                  0.306 
# 
_struct.entry_id                     8YYA 
_struct.title                        'Crystal Structure of Concanavalin A Complexed with 5-Fluorouracil' 
_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        8YYA 
_struct_keywords.text            'Plant Lectin, Canavalia ensiformis, jack beans, SUGAR BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'SUGAR BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CONA_CANBR 
_struct_ref.pdbx_db_accession          P55915 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVGKRLSAVVSYPNGDSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSNSTHETNALHFMFNQFSKDQKDLILQGDATTGTEGNLRLTRVS
SNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFLIKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YYA 
_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                 237 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P55915 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  237 
_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       237 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8YYA ASP A 58  ? UNP P55915 GLY 58  conflict 58  1 
1 8YYA ALA A 70  ? UNP P55915 GLY 70  conflict 70  2 
1 8YYA ASP A 151 ? UNP P55915 GLU 151 conflict 151 3 
1 8YYA GLU A 155 ? UNP P55915 ARG 155 conflict 155 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 90    ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  10430 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASN A 14  ? GLY A 18  ? ASN A 14  GLY A 18  5 ? 5 
HELX_P HELX_P2 AA2 ASP A 80  ? VAL A 84  ? ASP A 80  VAL A 84  5 ? 5 
HELX_P HELX_P3 AA3 THR A 226 ? LEU A 230 ? THR A 226 LEU A 230 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 
metalc1 metalc ? ? A GLU 8  OE2 ? ? ? 1_555 D MN . MN ? ? A GLU 8  A MN 303 1_555 ? ? ? ? ? ? ? 1.988 ? ? 
metalc2 metalc ? ? A ASP 10 OD1 ? ? ? 1_555 C CA . CA ? ? A ASP 10 A CA 302 1_555 ? ? ? ? ? ? ? 2.204 ? ? 
metalc3 metalc ? ? A ASP 10 OD2 ? ? ? 1_555 C CA . CA ? ? A ASP 10 A CA 302 1_555 ? ? ? ? ? ? ? 2.594 ? ? 
metalc4 metalc ? ? A TYR 12 O   ? ? ? 1_555 C CA . CA ? ? A TYR 12 A CA 302 1_555 ? ? ? ? ? ? ? 2.461 ? ? 
metalc5 metalc ? ? A ASN 14 OD1 ? ? ? 1_555 C CA . CA ? ? A ASN 14 A CA 302 1_555 ? ? ? ? ? ? ? 2.539 ? ? 
metalc6 metalc ? ? A ASP 19 OD2 ? ? ? 1_555 C CA . CA ? ? A ASP 19 A CA 302 1_555 ? ? ? ? ? ? ? 2.460 ? ? 
metalc7 metalc ? ? A ASP 19 OD1 ? ? ? 1_555 D MN . MN ? ? A ASP 19 A MN 303 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc8 metalc ? ? A HIS 24 NE2 ? ? ? 1_555 D MN . MN ? ? A HIS 24 A MN 303 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE2 ? A GLU 8  ? A GLU 8  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 OD1 ? A ASP 19 ? A ASP 19 ? 1_555 119.4 ? 
2  OE2 ? A GLU 8  ? A GLU 8  ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 NE2 ? A HIS 24 ? A HIS 24 ? 1_555 85.3  ? 
3  OD1 ? A ASP 19 ? A ASP 19 ? 1_555 MN ? D MN . ? A MN 303 ? 1_555 NE2 ? A HIS 24 ? A HIS 24 ? 1_555 82.1  ? 
4  OD1 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD2 ? A ASP 10 ? A ASP 10 ? 1_555 54.9  ? 
5  OD1 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? A TYR 12 ? A TYR 12 ? 1_555 71.5  ? 
6  OD2 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 O   ? A TYR 12 ? A TYR 12 ? 1_555 96.3  ? 
7  OD1 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14 ? 1_555 156.2 ? 
8  OD2 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14 ? 1_555 145.3 ? 
9  O   ? A TYR 12 ? A TYR 12 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14 ? 1_555 90.1  ? 
10 OD1 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19 ? 1_555 99.0  ? 
11 OD2 ? A ASP 10 ? A ASP 10 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19 ? 1_555 61.1  ? 
12 O   ? A TYR 12 ? A TYR 12 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19 ? 1_555 71.9  ? 
13 OD1 ? A ASN 14 ? A ASN 14 ? 1_555 CA ? C CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19 ? 1_555 89.1  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ALA 
_struct_mon_prot_cis.label_seq_id           207 
_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           ALA 
_struct_mon_prot_cis.auth_seq_id            207 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   ASP 
_struct_mon_prot_cis.pdbx_label_seq_id_2    208 
_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    ASP 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     208 
_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       5.65 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? 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 LYS A 36  ? LYS A 39  ? LYS A 36  LYS A 39  
AA1 2 HIS A 24  ? ILE A 29  ? HIS A 24  ILE A 29  
AA1 3 ILE A 4   ? ASP A 10  ? ILE A 4   ASP A 10  
AA1 4 GLY A 209 ? SER A 215 ? GLY A 209 SER A 215 
AA1 5 TRP A 88  ? SER A 96  ? TRP A 88  SER A 96  
AA1 6 VAL A 170 ? PHE A 175 ? VAL A 170 PHE A 175 
AA1 7 LEU A 140 ? GLY A 144 ? LEU A 140 GLY A 144 
AA2 1 LYS A 36  ? LYS A 39  ? LYS A 36  LYS A 39  
AA2 2 HIS A 24  ? ILE A 29  ? HIS A 24  ILE A 29  
AA2 3 ILE A 4   ? ASP A 10  ? ILE A 4   ASP A 10  
AA2 4 GLY A 209 ? SER A 215 ? GLY A 209 SER A 215 
AA2 5 TRP A 88  ? SER A 96  ? TRP A 88  SER A 96  
AA2 6 VAL A 179 ? HIS A 180 ? VAL A 179 HIS A 180 
AA3 1 ALA A 73  ? ASP A 78  ? ALA A 73  ASP A 78  
AA3 2 ARG A 60  ? SER A 66  ? ARG A 60  SER A 66  
AA3 3 VAL A 47  ? ASN A 55  ? VAL A 47  ASN A 55  
AA3 4 ALA A 186 ? LEU A 198 ? ALA A 186 LEU A 198 
AA3 5 THR A 105 ? SER A 117 ? THR A 105 SER A 117 
AA3 6 THR A 123 ? HIS A 127 ? THR A 123 HIS A 127 
AA4 1 ALA A 73  ? ASP A 78  ? ALA A 73  ASP A 78  
AA4 2 ARG A 60  ? SER A 66  ? ARG A 60  SER A 66  
AA4 3 VAL A 47  ? ASN A 55  ? VAL A 47  ASN A 55  
AA4 4 ALA A 186 ? LEU A 198 ? ALA A 186 LEU A 198 
AA4 5 THR A 105 ? SER A 117 ? THR A 105 SER A 117 
AA4 6 ASN A 153 ? GLU A 155 ? ASN A 153 GLU A 155 
AA4 7 THR A 147 ? THR A 150 ? THR A 147 THR A 150 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 38  ? O ALA A 38  N ILE A 25  ? N ILE A 25  
AA1 2 3 O ASP A 28  ? O ASP A 28  N ALA A 6   ? N ALA A 6   
AA1 3 4 N VAL A 5   ? N VAL A 5   O ILE A 214 ? O ILE A 214 
AA1 4 5 O ALA A 211 ? O ALA A 211 N SER A 94  ? N SER A 94  
AA1 5 6 N LEU A 93  ? N LEU A 93  O ALA A 173 ? O ALA A 173 
AA1 6 7 O LEU A 174 ? O LEU A 174 N ILE A 141 ? N ILE A 141 
AA2 1 2 O ALA A 38  ? O ALA A 38  N ILE A 25  ? N ILE A 25  
AA2 2 3 O ASP A 28  ? O ASP A 28  N ALA A 6   ? N ALA A 6   
AA2 3 4 N VAL A 5   ? N VAL A 5   O ILE A 214 ? O ILE A 214 
AA2 4 5 O ALA A 211 ? O ALA A 211 N SER A 94  ? N SER A 94  
AA2 5 6 N VAL A 89  ? N VAL A 89  O VAL A 179 ? O VAL A 179 
AA3 1 2 O VAL A 75  ? O VAL A 75  N ALA A 63  ? N ALA A 63  
AA3 2 3 O VAL A 64  ? O VAL A 64  N HIS A 51  ? N HIS A 51  
AA3 3 4 N ILE A 52  ? N ILE A 52  O ALA A 193 ? O ALA A 193 
AA3 4 5 O THR A 194 ? O THR A 194 N SER A 110 ? N SER A 110 
AA3 5 6 N LEU A 115 ? N LEU A 115 O ASN A 124 ? O ASN A 124 
AA4 1 2 O VAL A 75  ? O VAL A 75  N ALA A 63  ? N ALA A 63  
AA4 2 3 O VAL A 64  ? O VAL A 64  N HIS A 51  ? N HIS A 51  
AA4 3 4 N ILE A 52  ? N ILE A 52  O ALA A 193 ? O ALA A 193 
AA4 4 5 O THR A 194 ? O THR A 194 N SER A 110 ? N SER A 110 
AA4 5 6 N ILE A 106 ? N ILE A 106 O LEU A 154 ? O LEU A 154 
AA4 6 7 O GLU A 155 ? O GLU A 155 N THR A 147 ? N THR A 147 
# 
_pdbx_entry_details.entry_id                   8YYA 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 20 ? ? -62.04  -177.06 
2 1 SER A 21 ? ? -90.51  31.20   
3 1 LYS A 30 ? ? 47.06   18.37   
4 1 VAL A 84 ? ? -130.08 -51.35  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 33  ? ? 0.156 'SIDE CHAIN' 
2 1 ARG A 158 ? ? 0.162 'SIDE CHAIN' 
# 
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  
CA  CA   CA N N 74  
GLN N    N  N N 75  
GLN CA   C  N S 76  
GLN C    C  N N 77  
GLN O    O  N N 78  
GLN CB   C  N N 79  
GLN CG   C  N N 80  
GLN CD   C  N N 81  
GLN OE1  O  N N 82  
GLN NE2  N  N N 83  
GLN OXT  O  N N 84  
GLN H    H  N N 85  
GLN H2   H  N N 86  
GLN HA   H  N N 87  
GLN HB2  H  N N 88  
GLN HB3  H  N N 89  
GLN HG2  H  N N 90  
GLN HG3  H  N N 91  
GLN HE21 H  N N 92  
GLN HE22 H  N N 93  
GLN HXT  H  N N 94  
GLU N    N  N N 95  
GLU CA   C  N S 96  
GLU C    C  N N 97  
GLU O    O  N N 98  
GLU CB   C  N N 99  
GLU CG   C  N N 100 
GLU CD   C  N N 101 
GLU OE1  O  N N 102 
GLU OE2  O  N N 103 
GLU OXT  O  N N 104 
GLU H    H  N N 105 
GLU H2   H  N N 106 
GLU HA   H  N N 107 
GLU HB2  H  N N 108 
GLU HB3  H  N N 109 
GLU HG2  H  N N 110 
GLU HG3  H  N N 111 
GLU HE2  H  N N 112 
GLU HXT  H  N N 113 
GLY N    N  N N 114 
GLY CA   C  N N 115 
GLY C    C  N N 116 
GLY O    O  N N 117 
GLY OXT  O  N N 118 
GLY H    H  N N 119 
GLY H2   H  N N 120 
GLY HA2  H  N N 121 
GLY HA3  H  N N 122 
GLY HXT  H  N N 123 
HIS N    N  N N 124 
HIS CA   C  N S 125 
HIS C    C  N N 126 
HIS O    O  N N 127 
HIS CB   C  N N 128 
HIS CG   C  Y N 129 
HIS ND1  N  Y N 130 
HIS CD2  C  Y N 131 
HIS CE1  C  Y N 132 
HIS NE2  N  Y N 133 
HIS OXT  O  N N 134 
HIS H    H  N N 135 
HIS H2   H  N N 136 
HIS HA   H  N N 137 
HIS HB2  H  N N 138 
HIS HB3  H  N N 139 
HIS HD1  H  N N 140 
HIS HD2  H  N N 141 
HIS HE1  H  N N 142 
HIS HE2  H  N N 143 
HIS HXT  H  N N 144 
HOH O    O  N N 145 
HOH H1   H  N N 146 
HOH H2   H  N N 147 
ILE N    N  N N 148 
ILE CA   C  N S 149 
ILE C    C  N N 150 
ILE O    O  N N 151 
ILE CB   C  N S 152 
ILE CG1  C  N N 153 
ILE CG2  C  N N 154 
ILE CD1  C  N N 155 
ILE OXT  O  N N 156 
ILE H    H  N N 157 
ILE H2   H  N N 158 
ILE HA   H  N N 159 
ILE HB   H  N N 160 
ILE HG12 H  N N 161 
ILE HG13 H  N N 162 
ILE HG21 H  N N 163 
ILE HG22 H  N N 164 
ILE HG23 H  N N 165 
ILE HD11 H  N N 166 
ILE HD12 H  N N 167 
ILE HD13 H  N N 168 
ILE HXT  H  N N 169 
LEU N    N  N N 170 
LEU CA   C  N S 171 
LEU C    C  N N 172 
LEU O    O  N N 173 
LEU CB   C  N N 174 
LEU CG   C  N N 175 
LEU CD1  C  N N 176 
LEU CD2  C  N N 177 
LEU OXT  O  N N 178 
LEU H    H  N N 179 
LEU H2   H  N N 180 
LEU HA   H  N N 181 
LEU HB2  H  N N 182 
LEU HB3  H  N N 183 
LEU HG   H  N N 184 
LEU HD11 H  N N 185 
LEU HD12 H  N N 186 
LEU HD13 H  N N 187 
LEU HD21 H  N N 188 
LEU HD22 H  N N 189 
LEU HD23 H  N N 190 
LEU HXT  H  N N 191 
LYS N    N  N N 192 
LYS CA   C  N S 193 
LYS C    C  N N 194 
LYS O    O  N N 195 
LYS CB   C  N N 196 
LYS CG   C  N N 197 
LYS CD   C  N N 198 
LYS CE   C  N N 199 
LYS NZ   N  N N 200 
LYS OXT  O  N N 201 
LYS H    H  N N 202 
LYS H2   H  N N 203 
LYS HA   H  N N 204 
LYS HB2  H  N N 205 
LYS HB3  H  N N 206 
LYS HG2  H  N N 207 
LYS HG3  H  N N 208 
LYS HD2  H  N N 209 
LYS HD3  H  N N 210 
LYS HE2  H  N N 211 
LYS HE3  H  N N 212 
LYS HZ1  H  N N 213 
LYS HZ2  H  N N 214 
LYS HZ3  H  N N 215 
LYS HXT  H  N N 216 
MET N    N  N N 217 
MET CA   C  N S 218 
MET C    C  N N 219 
MET O    O  N N 220 
MET CB   C  N N 221 
MET CG   C  N N 222 
MET SD   S  N N 223 
MET CE   C  N N 224 
MET OXT  O  N N 225 
MET H    H  N N 226 
MET H2   H  N N 227 
MET HA   H  N N 228 
MET HB2  H  N N 229 
MET HB3  H  N N 230 
MET HG2  H  N N 231 
MET HG3  H  N N 232 
MET HE1  H  N N 233 
MET HE2  H  N N 234 
MET HE3  H  N N 235 
MET HXT  H  N N 236 
MN  MN   MN N N 237 
PHE N    N  N N 238 
PHE CA   C  N S 239 
PHE C    C  N N 240 
PHE O    O  N N 241 
PHE CB   C  N N 242 
PHE CG   C  Y N 243 
PHE CD1  C  Y N 244 
PHE CD2  C  Y N 245 
PHE CE1  C  Y N 246 
PHE CE2  C  Y N 247 
PHE CZ   C  Y N 248 
PHE OXT  O  N N 249 
PHE H    H  N N 250 
PHE H2   H  N N 251 
PHE HA   H  N N 252 
PHE HB2  H  N N 253 
PHE HB3  H  N N 254 
PHE HD1  H  N N 255 
PHE HD2  H  N N 256 
PHE HE1  H  N N 257 
PHE HE2  H  N N 258 
PHE HZ   H  N N 259 
PHE HXT  H  N N 260 
PRO N    N  N N 261 
PRO CA   C  N S 262 
PRO C    C  N N 263 
PRO O    O  N N 264 
PRO CB   C  N N 265 
PRO CG   C  N N 266 
PRO CD   C  N N 267 
PRO OXT  O  N N 268 
PRO H    H  N N 269 
PRO HA   H  N N 270 
PRO HB2  H  N N 271 
PRO HB3  H  N N 272 
PRO HG2  H  N N 273 
PRO HG3  H  N N 274 
PRO HD2  H  N N 275 
PRO HD3  H  N N 276 
PRO HXT  H  N N 277 
SER N    N  N N 278 
SER CA   C  N S 279 
SER C    C  N N 280 
SER O    O  N N 281 
SER CB   C  N N 282 
SER OG   O  N N 283 
SER OXT  O  N N 284 
SER H    H  N N 285 
SER H2   H  N N 286 
SER HA   H  N N 287 
SER HB2  H  N N 288 
SER HB3  H  N N 289 
SER HG   H  N N 290 
SER HXT  H  N N 291 
SO4 S    S  N N 292 
SO4 O1   O  N N 293 
SO4 O2   O  N N 294 
SO4 O3   O  N N 295 
SO4 O4   O  N N 296 
THR N    N  N N 297 
THR CA   C  N S 298 
THR C    C  N N 299 
THR O    O  N N 300 
THR CB   C  N R 301 
THR OG1  O  N N 302 
THR CG2  C  N N 303 
THR OXT  O  N N 304 
THR H    H  N N 305 
THR H2   H  N N 306 
THR HA   H  N N 307 
THR HB   H  N N 308 
THR HG1  H  N N 309 
THR HG21 H  N N 310 
THR HG22 H  N N 311 
THR HG23 H  N N 312 
THR HXT  H  N N 313 
TRP N    N  N N 314 
TRP CA   C  N S 315 
TRP C    C  N N 316 
TRP O    O  N N 317 
TRP CB   C  N N 318 
TRP CG   C  Y N 319 
TRP CD1  C  Y N 320 
TRP CD2  C  Y N 321 
TRP NE1  N  Y N 322 
TRP CE2  C  Y N 323 
TRP CE3  C  Y N 324 
TRP CZ2  C  Y N 325 
TRP CZ3  C  Y N 326 
TRP CH2  C  Y N 327 
TRP OXT  O  N N 328 
TRP H    H  N N 329 
TRP H2   H  N N 330 
TRP HA   H  N N 331 
TRP HB2  H  N N 332 
TRP HB3  H  N N 333 
TRP HD1  H  N N 334 
TRP HE1  H  N N 335 
TRP HE3  H  N N 336 
TRP HZ2  H  N N 337 
TRP HZ3  H  N N 338 
TRP HH2  H  N N 339 
TRP HXT  H  N N 340 
TYR N    N  N N 341 
TYR CA   C  N S 342 
TYR C    C  N N 343 
TYR O    O  N N 344 
TYR CB   C  N N 345 
TYR CG   C  Y N 346 
TYR CD1  C  Y N 347 
TYR CD2  C  Y N 348 
TYR CE1  C  Y N 349 
TYR CE2  C  Y N 350 
TYR CZ   C  Y N 351 
TYR OH   O  N N 352 
TYR OXT  O  N N 353 
TYR H    H  N N 354 
TYR H2   H  N N 355 
TYR HA   H  N N 356 
TYR HB2  H  N N 357 
TYR HB3  H  N N 358 
TYR HD1  H  N N 359 
TYR HD2  H  N N 360 
TYR HE1  H  N N 361 
TYR HE2  H  N N 362 
TYR HH   H  N N 363 
TYR HXT  H  N N 364 
URF N1   N  N N 365 
URF C2   C  N N 366 
URF N3   N  N N 367 
URF C4   C  N N 368 
URF C5   C  N N 369 
URF C6   C  N N 370 
URF O2   O  N N 371 
URF O4   O  N N 372 
URF F5   F  N N 373 
URF HN1  H  N N 374 
URF HN3  H  N N 375 
URF H6   H  N N 376 
VAL N    N  N N 377 
VAL CA   C  N S 378 
VAL C    C  N N 379 
VAL O    O  N N 380 
VAL CB   C  N N 381 
VAL CG1  C  N N 382 
VAL CG2  C  N N 383 
VAL OXT  O  N N 384 
VAL H    H  N N 385 
VAL H2   H  N N 386 
VAL HA   H  N N 387 
VAL HB   H  N N 388 
VAL HG11 H  N N 389 
VAL HG12 H  N N 390 
VAL HG13 H  N N 391 
VAL HG21 H  N N 392 
VAL HG22 H  N N 393 
VAL HG23 H  N N 394 
VAL HXT  H  N N 395 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
SO4 S   O1   doub N N 277 
SO4 S   O2   doub N N 278 
SO4 S   O3   sing N N 279 
SO4 S   O4   sing N N 280 
THR N   CA   sing N N 281 
THR N   H    sing N N 282 
THR N   H2   sing N N 283 
THR CA  C    sing N N 284 
THR CA  CB   sing N N 285 
THR CA  HA   sing N N 286 
THR C   O    doub N N 287 
THR C   OXT  sing N N 288 
THR CB  OG1  sing N N 289 
THR CB  CG2  sing N N 290 
THR CB  HB   sing N N 291 
THR OG1 HG1  sing N N 292 
THR CG2 HG21 sing N N 293 
THR CG2 HG22 sing N N 294 
THR CG2 HG23 sing N N 295 
THR OXT HXT  sing N N 296 
TRP N   CA   sing N N 297 
TRP N   H    sing N N 298 
TRP N   H2   sing N N 299 
TRP CA  C    sing N N 300 
TRP CA  CB   sing N N 301 
TRP CA  HA   sing N N 302 
TRP C   O    doub N N 303 
TRP C   OXT  sing N N 304 
TRP CB  CG   sing N N 305 
TRP CB  HB2  sing N N 306 
TRP CB  HB3  sing N N 307 
TRP CG  CD1  doub Y N 308 
TRP CG  CD2  sing Y N 309 
TRP CD1 NE1  sing Y N 310 
TRP CD1 HD1  sing N N 311 
TRP CD2 CE2  doub Y N 312 
TRP CD2 CE3  sing Y N 313 
TRP NE1 CE2  sing Y N 314 
TRP NE1 HE1  sing N N 315 
TRP CE2 CZ2  sing Y N 316 
TRP CE3 CZ3  doub Y N 317 
TRP CE3 HE3  sing N N 318 
TRP CZ2 CH2  doub Y N 319 
TRP CZ2 HZ2  sing N N 320 
TRP CZ3 CH2  sing Y N 321 
TRP CZ3 HZ3  sing N N 322 
TRP CH2 HH2  sing N N 323 
TRP OXT HXT  sing N N 324 
TYR N   CA   sing N N 325 
TYR N   H    sing N N 326 
TYR N   H2   sing N N 327 
TYR CA  C    sing N N 328 
TYR CA  CB   sing N N 329 
TYR CA  HA   sing N N 330 
TYR C   O    doub N N 331 
TYR C   OXT  sing N N 332 
TYR CB  CG   sing N N 333 
TYR CB  HB2  sing N N 334 
TYR CB  HB3  sing N N 335 
TYR CG  CD1  doub Y N 336 
TYR CG  CD2  sing Y N 337 
TYR CD1 CE1  sing Y N 338 
TYR CD1 HD1  sing N N 339 
TYR CD2 CE2  doub Y N 340 
TYR CD2 HD2  sing N N 341 
TYR CE1 CZ   doub Y N 342 
TYR CE1 HE1  sing N N 343 
TYR CE2 CZ   sing Y N 344 
TYR CE2 HE2  sing N N 345 
TYR CZ  OH   sing N N 346 
TYR OH  HH   sing N N 347 
TYR OXT HXT  sing N N 348 
URF N1  C2   sing N N 349 
URF N1  C6   sing N N 350 
URF N1  HN1  sing N N 351 
URF C2  N3   sing N N 352 
URF C2  O2   doub N N 353 
URF N3  C4   sing N N 354 
URF N3  HN3  sing N N 355 
URF C4  C5   sing N N 356 
URF C4  O4   doub N N 357 
URF C5  C6   doub N N 358 
URF C5  F5   sing N N 359 
URF C6  H6   sing N N 360 
VAL N   CA   sing N N 361 
VAL N   H    sing N N 362 
VAL N   H2   sing N N 363 
VAL CA  C    sing N N 364 
VAL CA  CB   sing N N 365 
VAL CA  HA   sing N N 366 
VAL C   O    doub N N 367 
VAL C   OXT  sing N N 368 
VAL CB  CG1  sing N N 369 
VAL CB  CG2  sing N N 370 
VAL CB  HB   sing N N 371 
VAL CG1 HG11 sing N N 372 
VAL CG1 HG12 sing N N 373 
VAL CG1 HG13 sing N N 374 
VAL CG2 HG21 sing N N 375 
VAL CG2 HG22 sing N N 376 
VAL CG2 HG23 sing N N 377 
VAL OXT HXT  sing N N 378 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1DQ0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8YYA 
_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]   0.016186 
_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]   0.011555 
_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]   0.011282 
_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  
CA 
F  
MN 
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   . ALA A 1 1   ? 29.891 21.312 3.109   1.00 2.49  ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 29.667 20.218 2.119   1.00 2.49  ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 28.212 19.754 2.214   1.00 2.43  ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 27.445 20.024 1.280   1.00 2.43  ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 30.645 19.054 2.290   1.00 2.49  ? 1   ALA A CB  1 
ATOM   6    N  N   . ASP A 1 2   ? 27.858 19.100 3.342   1.00 2.34  ? 2   ASP A N   1 
ATOM   7    C  CA  . ASP A 1 2   ? 26.631 18.319 3.425   1.00 2.28  ? 2   ASP A CA  1 
ATOM   8    C  C   . ASP A 1 2   ? 25.448 19.261 3.294   1.00 2.19  ? 2   ASP A C   1 
ATOM   9    O  O   . ASP A 1 2   ? 25.578 20.440 3.617   1.00 2.19  ? 2   ASP A O   1 
ATOM   10   C  CB  . ASP A 1 2   ? 26.513 17.492 4.713   1.00 2.30  ? 2   ASP A CB  1 
ATOM   11   C  CG  . ASP A 1 2   ? 27.059 16.071 4.630   1.00 2.33  ? 2   ASP A CG  1 
ATOM   12   O  OD1 . ASP A 1 2   ? 27.428 15.648 3.507   1.00 2.34  ? 2   ASP A OD1 1 
ATOM   13   O  OD2 . ASP A 1 2   ? 27.129 15.393 5.697   1.00 2.33  ? 2   ASP A OD2 1 
ATOM   14   N  N   . THR A 1 3   ? 24.323 18.687 2.851   1.00 2.08  ? 3   THR A N   1 
ATOM   15   C  CA  . THR A 1 3   ? 23.114 19.412 2.513   1.00 2.01  ? 3   THR A CA  1 
ATOM   16   C  C   . THR A 1 3   ? 21.899 18.797 3.191   1.00 1.95  ? 3   THR A C   1 
ATOM   17   O  O   . THR A 1 3   ? 21.602 17.632 2.973   1.00 1.95  ? 3   THR A O   1 
ATOM   18   C  CB  . THR A 1 3   ? 22.849 19.281 1.023   1.00 2.01  ? 3   THR A CB  1 
ATOM   19   O  OG1 . THR A 1 3   ? 24.116 19.522 0.419   1.00 2.02  ? 3   THR A OG1 1 
ATOM   20   C  CG2 . THR A 1 3   ? 21.766 20.211 0.532   1.00 2.02  ? 3   THR A CG2 1 
ATOM   21   N  N   . ILE A 1 4   ? 21.156 19.603 3.949   1.00 1.90  ? 4   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 4   ? 20.197 19.071 4.904   1.00 1.84  ? 4   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 4   ? 18.860 19.756 4.719   1.00 1.81  ? 4   ILE A C   1 
ATOM   24   O  O   . ILE A 1 4   ? 18.803 20.961 4.613   1.00 1.80  ? 4   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 4   ? 20.692 19.282 6.344   1.00 1.82  ? 4   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 4   ? 22.055 18.629 6.574   1.00 1.81  ? 4   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 4   ? 19.647 18.828 7.347   1.00 1.82  ? 4   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 4   ? 22.083 17.164 6.308   1.00 1.81  ? 4   ILE A CD1 1 
ATOM   29   N  N   . VAL A 1 5   ? 17.809 18.957 4.680   1.00 1.80  ? 5   VAL A N   1 
ATOM   30   C  CA  . VAL A 1 5   ? 16.467 19.431 4.938   1.00 1.82  ? 5   VAL A CA  1 
ATOM   31   C  C   . VAL A 1 5   ? 15.947 18.585 6.084   1.00 1.83  ? 5   VAL A C   1 
ATOM   32   O  O   . VAL A 1 5   ? 16.154 17.372 6.094   1.00 1.85  ? 5   VAL A O   1 
ATOM   33   C  CB  . VAL A 1 5   ? 15.566 19.327 3.689   1.00 1.82  ? 5   VAL A CB  1 
ATOM   34   C  CG1 . VAL A 1 5   ? 14.093 19.583 4.003   1.00 1.82  ? 5   VAL A CG1 1 
ATOM   35   C  CG2 . VAL A 1 5   ? 16.043 20.264 2.586   1.00 1.83  ? 5   VAL A CG2 1 
ATOM   36   N  N   . ALA A 1 6   ? 15.280 19.206 7.050   1.00 1.84  ? 6   ALA A N   1 
ATOM   37   C  CA  . ALA A 1 6   ? 14.866 18.434 8.203   1.00 1.87  ? 6   ALA A CA  1 
ATOM   38   C  C   . ALA A 1 6   ? 13.669 19.077 8.883   1.00 1.89  ? 6   ALA A C   1 
ATOM   39   O  O   . ALA A 1 6   ? 13.378 20.242 8.657   1.00 1.88  ? 6   ALA A O   1 
ATOM   40   C  CB  . ALA A 1 6   ? 16.036 18.287 9.139   1.00 1.87  ? 6   ALA A CB  1 
ATOM   41   N  N   . VAL A 1 7   ? 12.970 18.279 9.685   1.00 1.95  ? 7   VAL A N   1 
ATOM   42   C  CA  . VAL A 1 7   ? 11.865 18.768 10.487  1.00 2.03  ? 7   VAL A CA  1 
ATOM   43   C  C   . VAL A 1 7   ? 12.254 18.501 11.937  1.00 2.15  ? 7   VAL A C   1 
ATOM   44   O  O   . VAL A 1 7   ? 12.382 17.344 12.322  1.00 2.17  ? 7   VAL A O   1 
ATOM   45   C  CB  . VAL A 1 7   ? 10.517 18.113 10.110  1.00 1.98  ? 7   VAL A CB  1 
ATOM   46   C  CG1 . VAL A 1 7   ? 9.428  18.413 11.126  1.00 1.96  ? 7   VAL A CG1 1 
ATOM   47   C  CG2 . VAL A 1 7   ? 10.046 18.497 8.718   1.00 1.97  ? 7   VAL A CG2 1 
ATOM   48   N  N   . GLU A 1 8   ? 12.501 19.572 12.706  1.00 2.31  ? 8   GLU A N   1 
ATOM   49   C  CA  . GLU A 1 8   ? 13.116 19.439 14.017  1.00 2.46  ? 8   GLU A CA  1 
ATOM   50   C  C   . GLU A 1 8   ? 12.006 19.395 15.071  1.00 2.60  ? 8   GLU A C   1 
ATOM   51   O  O   . GLU A 1 8   ? 10.938 20.017 14.925  1.00 2.61  ? 8   GLU A O   1 
ATOM   52   C  CB  . GLU A 1 8   ? 14.247 20.457 14.281  1.00 2.48  ? 8   GLU A CB  1 
ATOM   53   C  CG  . GLU A 1 8   ? 13.862 21.941 14.369  1.00 2.52  ? 8   GLU A CG  1 
ATOM   54   C  CD  . GLU A 1 8   ? 14.917 22.865 14.986  1.00 2.56  ? 8   GLU A CD  1 
ATOM   55   O  OE1 . GLU A 1 8   ? 16.090 22.833 14.519  1.00 2.60  ? 8   GLU A OE1 1 
ATOM   56   O  OE2 . GLU A 1 8   ? 14.581 23.647 15.941  1.00 2.59  ? 8   GLU A OE2 1 
ATOM   57   N  N   . LEU A 1 9   ? 12.259 18.498 16.041  1.00 2.74  ? 9   LEU A N   1 
ATOM   58   C  CA  . LEU A 1 9   ? 11.601 18.426 17.331  1.00 2.82  ? 9   LEU A CA  1 
ATOM   59   C  C   . LEU A 1 9   ? 12.643 18.862 18.363  1.00 2.91  ? 9   LEU A C   1 
ATOM   60   O  O   . LEU A 1 9   ? 13.378 18.031 18.916  1.00 2.89  ? 9   LEU A O   1 
ATOM   61   C  CB  . LEU A 1 9   ? 11.095 16.992 17.556  1.00 2.83  ? 9   LEU A CB  1 
ATOM   62   C  CG  . LEU A 1 9   ? 9.738  16.632 16.931  1.00 2.82  ? 9   LEU A CG  1 
ATOM   63   C  CD1 . LEU A 1 9   ? 9.764  16.676 15.412  1.00 2.82  ? 9   LEU A CD1 1 
ATOM   64   C  CD2 . LEU A 1 9   ? 9.292  15.250 17.387  1.00 2.82  ? 9   LEU A CD2 1 
ATOM   65   N  N   . ASP A 1 10  ? 12.723 20.197 18.538  1.00 2.99  ? 10  ASP A N   1 
ATOM   66   C  CA  . ASP A 1 10  ? 13.714 20.861 19.366  1.00 3.04  ? 10  ASP A CA  1 
ATOM   67   C  C   . ASP A 1 10  ? 13.158 20.980 20.777  1.00 3.13  ? 10  ASP A C   1 
ATOM   68   O  O   . ASP A 1 10  ? 12.287 21.809 21.028  1.00 3.09  ? 10  ASP A O   1 
ATOM   69   C  CB  . ASP A 1 10  ? 14.036 22.236 18.786  1.00 3.06  ? 10  ASP A CB  1 
ATOM   70   C  CG  . ASP A 1 10  ? 15.345 22.860 19.249  1.00 3.09  ? 10  ASP A CG  1 
ATOM   71   O  OD1 . ASP A 1 10  ? 15.942 22.355 20.248  1.00 3.08  ? 10  ASP A OD1 1 
ATOM   72   O  OD2 . ASP A 1 10  ? 15.787 23.839 18.580  1.00 3.11  ? 10  ASP A OD2 1 
ATOM   73   N  N   . THR A 1 11  ? 13.687 20.138 21.682  1.00 3.27  ? 11  THR A N   1 
ATOM   74   C  CA  . THR A 1 11  ? 13.222 20.036 23.061  1.00 3.35  ? 11  THR A CA  1 
ATOM   75   C  C   . THR A 1 11  ? 13.861 21.092 23.958  1.00 3.42  ? 11  THR A C   1 
ATOM   76   O  O   . THR A 1 11  ? 13.476 21.211 25.125  1.00 3.48  ? 11  THR A O   1 
ATOM   77   C  CB  . THR A 1 11  ? 13.497 18.647 23.654  1.00 3.36  ? 11  THR A CB  1 
ATOM   78   O  OG1 . THR A 1 11  ? 14.894 18.342 23.622  1.00 3.30  ? 11  THR A OG1 1 
ATOM   79   C  CG2 . THR A 1 11  ? 12.713 17.569 22.937  1.00 3.39  ? 11  THR A CG2 1 
ATOM   80   N  N   . TYR A 1 12  ? 14.822 21.849 23.417  1.00 3.48  ? 12  TYR A N   1 
ATOM   81   C  CA  . TYR A 1 12  ? 15.503 22.851 24.207  1.00 3.58  ? 12  TYR A CA  1 
ATOM   82   C  C   . TYR A 1 12  ? 15.688 24.135 23.398  1.00 3.83  ? 12  TYR A C   1 
ATOM   83   O  O   . TYR A 1 12  ? 16.266 24.124 22.306  1.00 3.89  ? 12  TYR A O   1 
ATOM   84   C  CB  . TYR A 1 12  ? 16.812 22.270 24.739  1.00 3.49  ? 12  TYR A CB  1 
ATOM   85   C  CG  . TYR A 1 12  ? 17.519 23.174 25.709  1.00 3.39  ? 12  TYR A CG  1 
ATOM   86   C  CD1 . TYR A 1 12  ? 18.076 24.367 25.283  1.00 3.36  ? 12  TYR A CD1 1 
ATOM   87   C  CD2 . TYR A 1 12  ? 17.592 22.854 27.049  1.00 3.35  ? 12  TYR A CD2 1 
ATOM   88   C  CE1 . TYR A 1 12  ? 18.710 25.213 26.166  1.00 3.33  ? 12  TYR A CE1 1 
ATOM   89   C  CE2 . TYR A 1 12  ? 18.212 23.693 27.952  1.00 3.33  ? 12  TYR A CE2 1 
ATOM   90   C  CZ  . TYR A 1 12  ? 18.774 24.872 27.502  1.00 3.32  ? 12  TYR A CZ  1 
ATOM   91   O  OH  . TYR A 1 12  ? 19.388 25.725 28.366  1.00 3.34  ? 12  TYR A OH  1 
ATOM   92   N  N   . PRO A 1 13  ? 15.219 25.288 23.935  1.00 4.12  ? 13  PRO A N   1 
ATOM   93   C  CA  . PRO A 1 13  ? 15.322 26.576 23.255  1.00 4.30  ? 13  PRO A CA  1 
ATOM   94   C  C   . PRO A 1 13  ? 16.675 27.249 23.456  1.00 4.55  ? 13  PRO A C   1 
ATOM   95   O  O   . PRO A 1 13  ? 17.012 27.653 24.570  1.00 4.69  ? 13  PRO A O   1 
ATOM   96   C  CB  . PRO A 1 13  ? 14.218 27.410 23.924  1.00 4.28  ? 13  PRO A CB  1 
ATOM   97   C  CG  . PRO A 1 13  ? 14.148 26.875 25.337  1.00 4.24  ? 13  PRO A CG  1 
ATOM   98   C  CD  . PRO A 1 13  ? 14.532 25.414 25.230  1.00 4.19  ? 13  PRO A CD  1 
ATOM   99   N  N   . ASN A 1 14  ? 17.443 27.334 22.360  1.00 4.74  ? 14  ASN A N   1 
ATOM   100  C  CA  . ASN A 1 14  ? 18.671 28.118 22.295  1.00 4.79  ? 14  ASN A CA  1 
ATOM   101  C  C   . ASN A 1 14  ? 18.311 29.465 21.664  1.00 4.90  ? 14  ASN A C   1 
ATOM   102  O  O   . ASN A 1 14  ? 18.534 29.684 20.470  1.00 5.02  ? 14  ASN A O   1 
ATOM   103  C  CB  . ASN A 1 14  ? 19.758 27.341 21.535  1.00 4.71  ? 14  ASN A CB  1 
ATOM   104  C  CG  . ASN A 1 14  ? 19.960 25.940 22.071  1.00 4.61  ? 14  ASN A CG  1 
ATOM   105  O  OD1 . ASN A 1 14  ? 19.602 24.944 21.448  1.00 4.51  ? 14  ASN A OD1 1 
ATOM   106  N  ND2 . ASN A 1 14  ? 20.497 25.864 23.269  1.00 4.61  ? 14  ASN A ND2 1 
ATOM   107  N  N   . THR A 1 15  ? 17.710 30.362 22.455  1.00 4.90  ? 15  THR A N   1 
ATOM   108  C  CA  . THR A 1 15  ? 17.030 31.513 21.880  1.00 4.91  ? 15  THR A CA  1 
ATOM   109  C  C   . THR A 1 15  ? 18.032 32.470 21.242  1.00 4.90  ? 15  THR A C   1 
ATOM   110  O  O   . THR A 1 15  ? 17.644 33.333 20.463  1.00 4.80  ? 15  THR A O   1 
ATOM   111  C  CB  . THR A 1 15  ? 16.158 32.229 22.915  1.00 4.91  ? 15  THR A CB  1 
ATOM   112  O  OG1 . THR A 1 15  ? 17.038 32.700 23.934  1.00 4.92  ? 15  THR A OG1 1 
ATOM   113  C  CG2 . THR A 1 15  ? 15.089 31.337 23.512  1.00 4.92  ? 15  THR A CG2 1 
ATOM   114  N  N   . ASP A 1 16  ? 19.318 32.296 21.563  1.00 5.01  ? 16  ASP A N   1 
ATOM   115  C  CA  . ASP A 1 16  ? 20.366 33.104 20.962  1.00 5.14  ? 16  ASP A CA  1 
ATOM   116  C  C   . ASP A 1 16  ? 20.631 32.680 19.513  1.00 5.16  ? 16  ASP A C   1 
ATOM   117  O  O   . ASP A 1 16  ? 21.340 33.396 18.808  1.00 5.27  ? 16  ASP A O   1 
ATOM   118  C  CB  . ASP A 1 16  ? 21.651 33.049 21.790  1.00 5.19  ? 16  ASP A CB  1 
ATOM   119  C  CG  . ASP A 1 16  ? 22.327 31.686 21.761  1.00 5.29  ? 16  ASP A CG  1 
ATOM   120  O  OD1 . ASP A 1 16  ? 21.832 30.737 22.448  1.00 5.30  ? 16  ASP A OD1 1 
ATOM   121  O  OD2 . ASP A 1 16  ? 23.326 31.577 21.033  1.00 5.27  ? 16  ASP A OD2 1 
ATOM   122  N  N   . ILE A 1 17  ? 20.084 31.533 19.059  1.00 5.10  ? 17  ILE A N   1 
ATOM   123  C  CA  . ILE A 1 17  ? 20.156 31.155 17.646  1.00 5.03  ? 17  ILE A CA  1 
ATOM   124  C  C   . ILE A 1 17  ? 18.760 30.930 17.049  1.00 4.92  ? 17  ILE A C   1 
ATOM   125  O  O   . ILE A 1 17  ? 18.594 30.099 16.146  1.00 4.72  ? 17  ILE A O   1 
ATOM   126  C  CB  . ILE A 1 17  ? 21.072 29.935 17.432  1.00 5.06  ? 17  ILE A CB  1 
ATOM   127  C  CG1 . ILE A 1 17  ? 20.516 28.676 18.104  1.00 5.07  ? 17  ILE A CG1 1 
ATOM   128  C  CG2 . ILE A 1 17  ? 22.477 30.254 17.901  1.00 5.07  ? 17  ILE A CG2 1 
ATOM   129  C  CD1 . ILE A 1 17  ? 21.047 27.384 17.529  1.00 5.09  ? 17  ILE A CD1 1 
ATOM   130  N  N   . GLY A 1 18  ? 17.781 31.687 17.583  1.00 4.93  ? 18  GLY A N   1 
ATOM   131  C  CA  . GLY A 1 18  ? 16.485 31.922 16.963  1.00 4.92  ? 18  GLY A CA  1 
ATOM   132  C  C   . GLY A 1 18  ? 15.418 30.916 17.387  1.00 4.90  ? 18  GLY A C   1 
ATOM   133  O  O   . GLY A 1 18  ? 14.260 31.011 16.971  1.00 4.90  ? 18  GLY A O   1 
ATOM   134  N  N   . ASP A 1 19  ? 15.840 29.907 18.156  1.00 4.89  ? 19  ASP A N   1 
ATOM   135  C  CA  . ASP A 1 19  ? 14.899 29.016 18.810  1.00 4.82  ? 19  ASP A CA  1 
ATOM   136  C  C   . ASP A 1 19  ? 13.949 29.936 19.556  1.00 4.81  ? 19  ASP A C   1 
ATOM   137  O  O   . ASP A 1 19  ? 14.440 30.875 20.170  1.00 4.85  ? 19  ASP A O   1 
ATOM   138  C  CB  . ASP A 1 19  ? 15.593 28.031 19.762  1.00 4.75  ? 19  ASP A CB  1 
ATOM   139  C  CG  . ASP A 1 19  ? 15.973 26.657 19.209  1.00 4.66  ? 19  ASP A CG  1 
ATOM   140  O  OD1 . ASP A 1 19  ? 15.668 26.366 18.023  1.00 4.58  ? 19  ASP A OD1 1 
ATOM   141  O  OD2 . ASP A 1 19  ? 16.536 25.847 20.003  1.00 4.61  ? 19  ASP A OD2 1 
ATOM   142  N  N   . PRO A 1 20  ? 12.618 29.638 19.497  1.00 4.82  ? 20  PRO A N   1 
ATOM   143  C  CA  . PRO A 1 20  ? 11.644 30.311 20.344  1.00 4.84  ? 20  PRO A CA  1 
ATOM   144  C  C   . PRO A 1 20  ? 11.928 30.042 21.830  1.00 4.87  ? 20  PRO A C   1 
ATOM   145  O  O   . PRO A 1 20  ? 12.851 29.364 22.125  1.00 4.85  ? 20  PRO A O   1 
ATOM   146  C  CB  . PRO A 1 20  ? 10.310 29.738 19.861  1.00 4.83  ? 20  PRO A CB  1 
ATOM   147  C  CG  . PRO A 1 20  ? 10.642 28.465 19.194  1.00 4.85  ? 20  PRO A CG  1 
ATOM   148  C  CD  . PRO A 1 20  ? 11.921 28.812 18.488  1.00 4.83  ? 20  PRO A CD  1 
ATOM   149  N  N   . SER A 1 21  ? 11.097 30.535 22.733  1.00 4.95  ? 21  SER A N   1 
ATOM   150  C  CA  . SER A 1 21  ? 11.422 30.493 24.154  1.00 4.99  ? 21  SER A CA  1 
ATOM   151  C  C   . SER A 1 21  ? 10.905 29.216 24.825  1.00 4.81  ? 21  SER A C   1 
ATOM   152  O  O   . SER A 1 21  ? 10.614 29.228 26.023  1.00 4.81  ? 21  SER A O   1 
ATOM   153  C  CB  . SER A 1 21  ? 10.890 31.734 24.852  1.00 5.09  ? 21  SER A CB  1 
ATOM   154  O  OG  . SER A 1 21  ? 11.119 32.899 24.060  1.00 5.25  ? 21  SER A OG  1 
ATOM   155  N  N   . TYR A 1 22  ? 10.845 28.105 24.073  1.00 4.57  ? 22  TYR A N   1 
ATOM   156  C  CA  . TYR A 1 22  ? 10.204 26.891 24.556  1.00 4.39  ? 22  TYR A CA  1 
ATOM   157  C  C   . TYR A 1 22  ? 10.447 25.736 23.587  1.00 4.16  ? 22  TYR A C   1 
ATOM   158  O  O   . TYR A 1 22  ? 11.091 25.913 22.553  1.00 4.19  ? 22  TYR A O   1 
ATOM   159  C  CB  . TYR A 1 22  ? 8.709  27.160 24.722  1.00 4.47  ? 22  TYR A CB  1 
ATOM   160  C  CG  . TYR A 1 22  ? 8.102  27.924 23.575  1.00 4.50  ? 22  TYR A CG  1 
ATOM   161  C  CD1 . TYR A 1 22  ? 7.872  27.314 22.353  1.00 4.51  ? 22  TYR A CD1 1 
ATOM   162  C  CD2 . TYR A 1 22  ? 7.811  29.269 23.697  1.00 4.51  ? 22  TYR A CD2 1 
ATOM   163  C  CE1 . TYR A 1 22  ? 7.340  28.017 21.287  1.00 4.52  ? 22  TYR A CE1 1 
ATOM   164  C  CE2 . TYR A 1 22  ? 7.273  29.984 22.644  1.00 4.56  ? 22  TYR A CE2 1 
ATOM   165  C  CZ  . TYR A 1 22  ? 7.033  29.357 21.434  1.00 4.57  ? 22  TYR A CZ  1 
ATOM   166  O  OH  . TYR A 1 22  ? 6.501  30.065 20.382  1.00 4.63  ? 22  TYR A OH  1 
ATOM   167  N  N   . PRO A 1 23  ? 9.968  24.509 23.891  1.00 3.86  ? 23  PRO A N   1 
ATOM   168  C  CA  . PRO A 1 23  ? 9.975  23.415 22.915  1.00 3.68  ? 23  PRO A CA  1 
ATOM   169  C  C   . PRO A 1 23  ? 9.019  23.643 21.740  1.00 3.45  ? 23  PRO A C   1 
ATOM   170  O  O   . PRO A 1 23  ? 7.877  24.083 21.919  1.00 3.42  ? 23  PRO A O   1 
ATOM   171  C  CB  . PRO A 1 23  ? 9.568  22.180 23.733  1.00 3.73  ? 23  PRO A CB  1 
ATOM   172  C  CG  . PRO A 1 23  ? 9.815  22.583 25.170  1.00 3.77  ? 23  PRO A CG  1 
ATOM   173  C  CD  . PRO A 1 23  ? 9.502  24.064 25.209  1.00 3.81  ? 23  PRO A CD  1 
ATOM   174  N  N   . HIS A 1 24  ? 9.527  23.321 20.541  1.00 3.18  ? 24  HIS A N   1 
ATOM   175  C  CA  . HIS A 1 24  ? 8.952  23.746 19.280  1.00 2.95  ? 24  HIS A CA  1 
ATOM   176  C  C   . HIS A 1 24  ? 9.256  22.709 18.209  1.00 2.75  ? 24  HIS A C   1 
ATOM   177  O  O   . HIS A 1 24  ? 10.221 21.961 18.344  1.00 2.71  ? 24  HIS A O   1 
ATOM   178  C  CB  . HIS A 1 24  ? 9.523  25.098 18.844  1.00 2.95  ? 24  HIS A CB  1 
ATOM   179  C  CG  . HIS A 1 24  ? 10.998 25.110 18.646  1.00 2.97  ? 24  HIS A CG  1 
ATOM   180  N  ND1 . HIS A 1 24  ? 11.862 25.358 19.688  1.00 2.98  ? 24  HIS A ND1 1 
ATOM   181  C  CD2 . HIS A 1 24  ? 11.762 24.949 17.549  1.00 2.98  ? 24  HIS A CD2 1 
ATOM   182  C  CE1 . HIS A 1 24  ? 13.104 25.321 19.231  1.00 2.99  ? 24  HIS A CE1 1 
ATOM   183  N  NE2 . HIS A 1 24  ? 13.074 25.066 17.937  1.00 2.97  ? 24  HIS A NE2 1 
ATOM   184  N  N   . ILE A 1 25  ? 8.397  22.668 17.174  1.00 2.55  ? 25  ILE A N   1 
ATOM   185  C  CA  . ILE A 1 25  ? 8.707  21.990 15.918  1.00 2.38  ? 25  ILE A CA  1 
ATOM   186  C  C   . ILE A 1 25  ? 9.147  23.020 14.900  1.00 2.23  ? 25  ILE A C   1 
ATOM   187  O  O   . ILE A 1 25  ? 8.784  24.184 15.003  1.00 2.23  ? 25  ILE A O   1 
ATOM   188  C  CB  . ILE A 1 25  ? 7.548  21.178 15.310  1.00 2.34  ? 25  ILE A CB  1 
ATOM   189  C  CG1 . ILE A 1 25  ? 6.180  21.776 15.650  1.00 2.30  ? 25  ILE A CG1 1 
ATOM   190  C  CG2 . ILE A 1 25  ? 7.683  19.712 15.698  1.00 2.35  ? 25  ILE A CG2 1 
ATOM   191  C  CD1 . ILE A 1 25  ? 5.070  21.314 14.738  1.00 2.26  ? 25  ILE A CD1 1 
ATOM   192  N  N   . GLY A 1 26  ? 9.871  22.548 13.888  1.00 2.07  ? 26  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 26  ? 10.428 23.476 12.926  1.00 1.97  ? 26  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 26  ? 10.994 22.760 11.718  1.00 1.84  ? 26  GLY A C   1 
ATOM   195  O  O   . GLY A 1 26  ? 11.207 21.563 11.775  1.00 1.82  ? 26  GLY A O   1 
ATOM   196  N  N   . ILE A 1 27  ? 11.246 23.544 10.670  1.00 1.72  ? 27  ILE A N   1 
ATOM   197  C  CA  . ILE A 1 27  ? 11.571 23.038 9.355   1.00 1.63  ? 27  ILE A CA  1 
ATOM   198  C  C   . ILE A 1 27  ? 12.858 23.712 8.904   1.00 1.61  ? 27  ILE A C   1 
ATOM   199  O  O   . ILE A 1 27  ? 12.884 24.918 8.699   1.00 1.58  ? 27  ILE A O   1 
ATOM   200  C  CB  . ILE A 1 27  ? 10.384 23.313 8.418   1.00 1.58  ? 27  ILE A CB  1 
ATOM   201  C  CG1 . ILE A 1 27  ? 9.231  22.349 8.700   1.00 1.55  ? 27  ILE A CG1 1 
ATOM   202  C  CG2 . ILE A 1 27  ? 10.819 23.263 6.971   1.00 1.57  ? 27  ILE A CG2 1 
ATOM   203  C  CD1 . ILE A 1 27  ? 7.873  22.946 8.488   1.00 1.53  ? 27  ILE A CD1 1 
ATOM   204  N  N   . ASP A 1 28  ? 13.922 22.915 8.777   1.00 1.59  ? 28  ASP A N   1 
ATOM   205  C  CA  . ASP A 1 28  ? 15.268 23.433 8.570   1.00 1.58  ? 28  ASP A CA  1 
ATOM   206  C  C   . ASP A 1 28  ? 15.716 23.148 7.146   1.00 1.59  ? 28  ASP A C   1 
ATOM   207  O  O   . ASP A 1 28  ? 15.973 22.007 6.804   1.00 1.59  ? 28  ASP A O   1 
ATOM   208  C  CB  . ASP A 1 28  ? 16.266 22.824 9.555   1.00 1.56  ? 28  ASP A CB  1 
ATOM   209  C  CG  . ASP A 1 28  ? 15.836 23.003 10.997  1.00 1.55  ? 28  ASP A CG  1 
ATOM   210  O  OD1 . ASP A 1 28  ? 14.974 23.858 11.243  1.00 1.54  ? 28  ASP A OD1 1 
ATOM   211  O  OD2 . ASP A 1 28  ? 16.339 22.258 11.847  1.00 1.54  ? 28  ASP A OD2 1 
ATOM   212  N  N   . ILE A 1 29  ? 15.766 24.200 6.328   1.00 1.61  ? 29  ILE A N   1 
ATOM   213  C  CA  . ILE A 1 29  ? 16.471 24.165 5.058   1.00 1.63  ? 29  ILE A CA  1 
ATOM   214  C  C   . ILE A 1 29  ? 17.900 24.612 5.331   1.00 1.66  ? 29  ILE A C   1 
ATOM   215  O  O   . ILE A 1 29  ? 18.130 25.735 5.764   1.00 1.66  ? 29  ILE A O   1 
ATOM   216  C  CB  . ILE A 1 29  ? 15.809 25.061 3.985   1.00 1.62  ? 29  ILE A CB  1 
ATOM   217  C  CG1 . ILE A 1 29  ? 14.288 24.892 3.901   1.00 1.62  ? 29  ILE A CG1 1 
ATOM   218  C  CG2 . ILE A 1 29  ? 16.481 24.847 2.640   1.00 1.62  ? 29  ILE A CG2 1 
ATOM   219  C  CD1 . ILE A 1 29  ? 13.831 23.454 3.712   1.00 1.63  ? 29  ILE A CD1 1 
ATOM   220  N  N   . LYS A 1 30  ? 18.839 23.696 5.133   1.00 1.70  ? 30  LYS A N   1 
ATOM   221  C  CA  . LYS A 1 30  ? 20.249 24.013 5.143   1.00 1.75  ? 30  LYS A CA  1 
ATOM   222  C  C   . LYS A 1 30  ? 20.652 24.880 6.337   1.00 1.77  ? 30  LYS A C   1 
ATOM   223  O  O   . LYS A 1 30  ? 21.717 25.487 6.309   1.00 1.79  ? 30  LYS A O   1 
ATOM   224  C  CB  . LYS A 1 30  ? 20.579 24.729 3.837   1.00 1.77  ? 30  LYS A CB  1 
ATOM   225  C  CG  . LYS A 1 30  ? 20.745 23.817 2.639   1.00 1.80  ? 30  LYS A CG  1 
ATOM   226  C  CD  . LYS A 1 30  ? 21.023 24.590 1.378   1.00 1.83  ? 30  LYS A CD  1 
ATOM   227  C  CE  . LYS A 1 30  ? 19.775 25.256 0.831   1.00 1.86  ? 30  LYS A CE  1 
ATOM   228  N  NZ  . LYS A 1 30  ? 20.012 25.952 -0.467  1.00 1.88  ? 30  LYS A NZ  1 
ATOM   229  N  N   . SER A 1 31  ? 19.834 24.939 7.392   1.00 1.78  ? 31  SER A N   1 
ATOM   230  C  CA  . SER A 1 31  ? 20.172 25.753 8.545   1.00 1.78  ? 31  SER A CA  1 
ATOM   231  C  C   . SER A 1 31  ? 19.247 25.469 9.719   1.00 1.80  ? 31  SER A C   1 
ATOM   232  O  O   . SER A 1 31  ? 18.020 25.556 9.596   1.00 1.79  ? 31  SER A O   1 
ATOM   233  C  CB  . SER A 1 31  ? 20.143 27.202 8.233   1.00 1.78  ? 31  SER A CB  1 
ATOM   234  O  OG  . SER A 1 31  ? 20.191 27.933 9.444   1.00 1.78  ? 31  SER A OG  1 
ATOM   235  N  N   . VAL A 1 32  ? 19.906 25.228 10.863  1.00 1.83  ? 32  VAL A N   1 
ATOM   236  C  CA  . VAL A 1 32  ? 19.301 24.839 12.129  1.00 1.85  ? 32  VAL A CA  1 
ATOM   237  C  C   . VAL A 1 32  ? 18.453 26.007 12.637  1.00 1.87  ? 32  VAL A C   1 
ATOM   238  O  O   . VAL A 1 32  ? 17.596 25.801 13.504  1.00 1.85  ? 32  VAL A O   1 
ATOM   239  C  CB  . VAL A 1 32  ? 20.386 24.413 13.143  1.00 1.85  ? 32  VAL A CB  1 
ATOM   240  C  CG1 . VAL A 1 32  ? 21.220 25.589 13.640  1.00 1.85  ? 32  VAL A CG1 1 
ATOM   241  C  CG2 . VAL A 1 32  ? 19.789 23.676 14.331  1.00 1.86  ? 32  VAL A CG2 1 
ATOM   242  N  N   . ARG A 1 33  ? 18.699 27.167 12.046  1.00 1.91  ? 33  ARG A N   1 
ATOM   243  C  CA  . ARG A 1 33  ? 17.856 28.347 12.264  1.00 1.96  ? 33  ARG A CA  1 
ATOM   244  C  C   . ARG A 1 33  ? 16.621 28.032 11.422  1.00 1.93  ? 33  ARG A C   1 
ATOM   245  O  O   . ARG A 1 33  ? 16.649 28.248 10.216  1.00 1.93  ? 33  ARG A O   1 
ATOM   246  C  CB  . ARG A 1 33  ? 18.729 29.541 11.897  1.00 2.02  ? 33  ARG A CB  1 
ATOM   247  C  CG  . ARG A 1 33  ? 19.943 29.722 12.791  1.00 2.09  ? 33  ARG A CG  1 
ATOM   248  C  CD  . ARG A 1 33  ? 20.116 31.169 13.207  1.00 2.16  ? 33  ARG A CD  1 
ATOM   249  N  NE  . ARG A 1 33  ? 21.504 31.592 13.141  1.00 2.24  ? 33  ARG A NE  1 
ATOM   250  C  CZ  . ARG A 1 33  ? 22.185 32.127 14.147  1.00 2.32  ? 33  ARG A CZ  1 
ATOM   251  N  NH1 . ARG A 1 33  ? 21.581 32.909 15.019  1.00 2.37  ? 33  ARG A NH1 1 
ATOM   252  N  NH2 . ARG A 1 33  ? 23.479 31.895 14.265  1.00 2.34  ? 33  ARG A NH2 1 
ATOM   253  N  N   . SER A 1 34  ? 15.583 27.509 12.045  1.00 1.92  ? 34  SER A N   1 
ATOM   254  C  CA  . SER A 1 34  ? 14.398 26.993 11.396  1.00 1.91  ? 34  SER A CA  1 
ATOM   255  C  C   . SER A 1 34  ? 13.758 28.171 10.677  1.00 1.90  ? 34  SER A C   1 
ATOM   256  O  O   . SER A 1 34  ? 13.604 29.218 11.290  1.00 1.88  ? 34  SER A O   1 
ATOM   257  C  CB  . SER A 1 34  ? 13.410 26.330 12.356  1.00 1.91  ? 34  SER A CB  1 
ATOM   258  O  OG  . SER A 1 34  ? 14.025 25.794 13.540  1.00 1.90  ? 34  SER A OG  1 
ATOM   259  N  N   . LYS A 1 35  ? 13.428 27.987 9.386   1.00 1.91  ? 35  LYS A N   1 
ATOM   260  C  CA  . LYS A 1 35  ? 12.798 29.008 8.558   1.00 1.90  ? 35  LYS A CA  1 
ATOM   261  C  C   . LYS A 1 35  ? 11.379 29.229 9.044   1.00 1.95  ? 35  LYS A C   1 
ATOM   262  O  O   . LYS A 1 35  ? 10.816 30.302 8.872   1.00 1.95  ? 35  LYS A O   1 
ATOM   263  C  CB  . LYS A 1 35  ? 12.711 28.591 7.091   1.00 1.87  ? 35  LYS A CB  1 
ATOM   264  C  CG  . LYS A 1 35  ? 14.021 28.155 6.457   1.00 1.85  ? 35  LYS A CG  1 
ATOM   265  C  CD  . LYS A 1 35  ? 14.922 29.265 6.037   1.00 1.83  ? 35  LYS A CD  1 
ATOM   266  C  CE  . LYS A 1 35  ? 16.346 28.788 5.864   1.00 1.82  ? 35  LYS A CE  1 
ATOM   267  N  NZ  . LYS A 1 35  ? 17.186 29.848 5.277   1.00 1.81  ? 35  LYS A NZ  1 
ATOM   268  N  N   . LYS A 1 36  ? 10.815 28.175 9.618   1.00 2.02  ? 36  LYS A N   1 
ATOM   269  C  CA  . LYS A 1 36  ? 9.542  28.254 10.296  1.00 2.10  ? 36  LYS A CA  1 
ATOM   270  C  C   . LYS A 1 36  ? 9.624  27.360 11.534  1.00 2.17  ? 36  LYS A C   1 
ATOM   271  O  O   . LYS A 1 36  ? 10.390 26.393 11.552  1.00 2.14  ? 36  LYS A O   1 
ATOM   272  C  CB  . LYS A 1 36  ? 8.427  27.869 9.310   1.00 2.11  ? 36  LYS A CB  1 
ATOM   273  C  CG  . LYS A 1 36  ? 7.000  28.185 9.746   1.00 2.12  ? 36  LYS A CG  1 
ATOM   274  C  CD  . LYS A 1 36  ? 6.557  29.615 9.424   1.00 2.14  ? 36  LYS A CD  1 
ATOM   275  C  CE  . LYS A 1 36  ? 5.130  29.929 9.850   1.00 2.16  ? 36  LYS A CE  1 
ATOM   276  N  NZ  . LYS A 1 36  ? 4.121  29.286 8.955   1.00 2.17  ? 36  LYS A NZ  1 
ATOM   277  N  N   . THR A 1 37  ? 8.850  27.733 12.570  1.00 2.29  ? 37  THR A N   1 
ATOM   278  C  CA  . THR A 1 37  ? 8.637  26.918 13.757  1.00 2.38  ? 37  THR A CA  1 
ATOM   279  C  C   . THR A 1 37  ? 7.213  27.095 14.259  1.00 2.53  ? 37  THR A C   1 
ATOM   280  O  O   . THR A 1 37  ? 6.459  27.869 13.697  1.00 2.56  ? 37  THR A O   1 
ATOM   281  C  CB  . THR A 1 37  ? 9.504  27.331 14.945  1.00 2.35  ? 37  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 37  ? 8.879  28.508 15.442  1.00 2.33  ? 37  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 37  ? 10.954 27.569 14.599  1.00 2.35  ? 37  THR A CG2 1 
ATOM   284  N  N   . ALA A 1 38  ? 6.875  26.371 15.327  1.00 2.73  ? 38  ALA A N   1 
ATOM   285  C  CA  . ALA A 1 38  ? 5.636  26.539 16.068  1.00 2.90  ? 38  ALA A CA  1 
ATOM   286  C  C   . ALA A 1 38  ? 5.813  25.832 17.407  1.00 3.12  ? 38  ALA A C   1 
ATOM   287  O  O   . ALA A 1 38  ? 6.669  24.954 17.502  1.00 3.12  ? 38  ALA A O   1 
ATOM   288  C  CB  . ALA A 1 38  ? 4.471  25.968 15.293  1.00 2.89  ? 38  ALA A CB  1 
ATOM   289  N  N   . LYS A 1 39  ? 4.977  26.183 18.399  1.00 3.39  ? 39  LYS A N   1 
ATOM   290  C  CA  . LYS A 1 39  ? 5.105  25.692 19.764  1.00 3.62  ? 39  LYS A CA  1 
ATOM   291  C  C   . LYS A 1 39  ? 4.823  24.198 19.847  1.00 3.90  ? 39  LYS A C   1 
ATOM   292  O  O   . LYS A 1 39  ? 3.911  23.690 19.205  1.00 3.89  ? 39  LYS A O   1 
ATOM   293  C  CB  . LYS A 1 39  ? 4.129  26.429 20.684  1.00 3.64  ? 39  LYS A CB  1 
ATOM   294  C  CG  . LYS A 1 39  ? 4.274  26.159 22.181  1.00 3.65  ? 39  LYS A CG  1 
ATOM   295  C  CD  . LYS A 1 39  ? 3.712  27.283 23.024  1.00 3.65  ? 39  LYS A CD  1 
ATOM   296  C  CE  . LYS A 1 39  ? 4.109  27.209 24.480  1.00 3.67  ? 39  LYS A CE  1 
ATOM   297  N  NZ  . LYS A 1 39  ? 3.312  26.178 25.179  1.00 3.70  ? 39  LYS A NZ  1 
ATOM   298  N  N   . TRP A 1 40  ? 5.607  23.517 20.683  1.00 4.33  ? 40  TRP A N   1 
ATOM   299  C  CA  . TRP A 1 40  ? 5.445  22.091 20.920  1.00 4.81  ? 40  TRP A CA  1 
ATOM   300  C  C   . TRP A 1 40  ? 5.335  21.846 22.429  1.00 5.38  ? 40  TRP A C   1 
ATOM   301  O  O   . TRP A 1 40  ? 6.168  22.333 23.195  1.00 5.36  ? 40  TRP A O   1 
ATOM   302  C  CB  . TRP A 1 40  ? 6.613  21.324 20.275  1.00 4.79  ? 40  TRP A CB  1 
ATOM   303  C  CG  . TRP A 1 40  ? 6.560  19.831 20.413  1.00 4.74  ? 40  TRP A CG  1 
ATOM   304  C  CD1 . TRP A 1 40  ? 5.451  19.047 20.345  1.00 4.70  ? 40  TRP A CD1 1 
ATOM   305  C  CD2 . TRP A 1 40  ? 7.680  18.931 20.572  1.00 4.72  ? 40  TRP A CD2 1 
ATOM   306  N  NE1 . TRP A 1 40  ? 5.797  17.732 20.475  1.00 4.71  ? 40  TRP A NE1 1 
ATOM   307  C  CE2 . TRP A 1 40  ? 7.152  17.626 20.624  1.00 4.66  ? 40  TRP A CE2 1 
ATOM   308  C  CE3 . TRP A 1 40  ? 9.072  19.097 20.683  1.00 4.67  ? 40  TRP A CE3 1 
ATOM   309  C  CZ2 . TRP A 1 40  ? 7.957  16.505 20.800  1.00 4.60  ? 40  TRP A CZ2 1 
ATOM   310  C  CZ3 . TRP A 1 40  ? 9.868  17.991 20.861  1.00 4.57  ? 40  TRP A CZ3 1 
ATOM   311  C  CH2 . TRP A 1 40  ? 9.313  16.715 20.913  1.00 4.60  ? 40  TRP A CH2 1 
ATOM   312  N  N   . ASN A 1 41  ? 4.271  21.144 22.853  1.00 5.98  ? 41  ASN A N   1 
ATOM   313  C  CA  . ASN A 1 41  ? 4.109  20.806 24.255  1.00 6.52  ? 41  ASN A CA  1 
ATOM   314  C  C   . ASN A 1 41  ? 4.629  19.386 24.437  1.00 7.18  ? 41  ASN A C   1 
ATOM   315  O  O   . ASN A 1 41  ? 3.850  18.443 24.500  1.00 7.32  ? 41  ASN A O   1 
ATOM   316  C  CB  . ASN A 1 41  ? 2.669  20.985 24.748  1.00 6.53  ? 41  ASN A CB  1 
ATOM   317  C  CG  . ASN A 1 41  ? 2.165  22.419 24.725  1.00 6.59  ? 41  ASN A CG  1 
ATOM   318  O  OD1 . ASN A 1 41  ? 2.724  23.330 25.334  1.00 6.59  ? 41  ASN A OD1 1 
ATOM   319  N  ND2 . ASN A 1 41  ? 1.058  22.635 24.046  1.00 6.71  ? 41  ASN A ND2 1 
ATOM   320  N  N   . MET A 1 42  ? 5.963  19.251 24.495  1.00 7.97  ? 42  MET A N   1 
ATOM   321  C  CA  . MET A 1 42  ? 6.612  17.955 24.660  1.00 8.39  ? 42  MET A CA  1 
ATOM   322  C  C   . MET A 1 42  ? 6.122  17.323 25.959  1.00 7.76  ? 42  MET A C   1 
ATOM   323  O  O   . MET A 1 42  ? 5.773  18.035 26.898  1.00 7.68  ? 42  MET A O   1 
ATOM   324  C  CB  . MET A 1 42  ? 8.143  18.067 24.717  1.00 9.25  ? 42  MET A CB  1 
ATOM   325  C  CG  . MET A 1 42  ? 8.826  16.698 24.780  1.00 10.14 ? 42  MET A CG  1 
ATOM   326  S  SD  . MET A 1 42  ? 10.262 16.580 25.888  1.00 11.79 ? 42  MET A SD  1 
ATOM   327  C  CE  . MET A 1 42  ? 9.535  17.128 27.437  1.00 11.88 ? 42  MET A CE  1 
ATOM   328  N  N   . GLN A 1 43  ? 6.077  15.986 25.988  1.00 7.21  ? 43  GLN A N   1 
ATOM   329  C  CA  . GLN A 1 43  ? 5.695  15.269 27.193  1.00 6.88  ? 43  GLN A CA  1 
ATOM   330  C  C   . GLN A 1 43  ? 6.770  14.255 27.558  1.00 6.56  ? 43  GLN A C   1 
ATOM   331  O  O   . GLN A 1 43  ? 6.864  13.178 26.962  1.00 6.62  ? 43  GLN A O   1 
ATOM   332  C  CB  . GLN A 1 43  ? 4.320  14.616 27.038  1.00 6.87  ? 43  GLN A CB  1 
ATOM   333  C  CG  . GLN A 1 43  ? 3.178  15.601 27.244  1.00 6.80  ? 43  GLN A CG  1 
ATOM   334  C  CD  . GLN A 1 43  ? 1.916  15.059 26.638  1.00 6.72  ? 43  GLN A CD  1 
ATOM   335  O  OE1 . GLN A 1 43  ? 1.503  15.477 25.560  1.00 6.54  ? 43  GLN A OE1 1 
ATOM   336  N  NE2 . GLN A 1 43  ? 1.338  14.081 27.313  1.00 6.72  ? 43  GLN A NE2 1 
ATOM   337  N  N   . ASN A 1 44  ? 7.544  14.635 28.579  1.00 6.15  ? 44  ASN A N   1 
ATOM   338  C  CA  . ASN A 1 44  ? 8.565  13.794 29.164  1.00 5.73  ? 44  ASN A CA  1 
ATOM   339  C  C   . ASN A 1 44  ? 7.973  12.422 29.451  1.00 5.39  ? 44  ASN A C   1 
ATOM   340  O  O   . ASN A 1 44  ? 7.071  12.294 30.276  1.00 5.30  ? 44  ASN A O   1 
ATOM   341  C  CB  . ASN A 1 44  ? 9.105  14.431 30.436  1.00 5.74  ? 44  ASN A CB  1 
ATOM   342  C  CG  . ASN A 1 44  ? 10.264 13.655 31.000  1.00 5.90  ? 44  ASN A CG  1 
ATOM   343  O  OD1 . ASN A 1 44  ? 10.133 12.474 31.320  1.00 5.94  ? 44  ASN A OD1 1 
ATOM   344  N  ND2 . ASN A 1 44  ? 11.408 14.311 31.104  1.00 6.07  ? 44  ASN A ND2 1 
ATOM   345  N  N   . GLY A 1 45  ? 8.448  11.417 28.713  1.00 5.10  ? 45  GLY A N   1 
ATOM   346  C  CA  . GLY A 1 45  ? 8.153  10.029 29.026  1.00 4.93  ? 45  GLY A CA  1 
ATOM   347  C  C   . GLY A 1 45  ? 6.971  9.423  28.255  1.00 4.68  ? 45  GLY A C   1 
ATOM   348  O  O   . GLY A 1 45  ? 6.721  8.219  28.377  1.00 4.54  ? 45  GLY A O   1 
ATOM   349  N  N   . LYS A 1 46  ? 6.235  10.224 27.469  1.00 4.43  ? 46  LYS A N   1 
ATOM   350  C  CA  . LYS A 1 46  ? 5.138  9.658  26.697  1.00 4.27  ? 46  LYS A CA  1 
ATOM   351  C  C   . LYS A 1 46  ? 5.611  9.366  25.271  1.00 4.00  ? 46  LYS A C   1 
ATOM   352  O  O   . LYS A 1 46  ? 6.668  9.823  24.816  1.00 3.98  ? 46  LYS A O   1 
ATOM   353  C  CB  . LYS A 1 46  ? 3.887  10.540 26.757  1.00 4.34  ? 46  LYS A CB  1 
ATOM   354  C  CG  . LYS A 1 46  ? 3.426  10.878 28.167  1.00 4.44  ? 46  LYS A CG  1 
ATOM   355  C  CD  . LYS A 1 46  ? 3.730  9.786  29.174  1.00 4.56  ? 46  LYS A CD  1 
ATOM   356  C  CE  . LYS A 1 46  ? 3.103  9.975  30.537  1.00 4.65  ? 46  LYS A CE  1 
ATOM   357  N  NZ  . LYS A 1 46  ? 1.688  9.521  30.538  1.00 4.74  ? 46  LYS A NZ  1 
ATOM   358  N  N   . VAL A 1 47  ? 4.824  8.532  24.593  1.00 3.69  ? 47  VAL A N   1 
ATOM   359  C  CA  . VAL A 1 47  ? 5.162  8.104  23.252  1.00 3.45  ? 47  VAL A CA  1 
ATOM   360  C  C   . VAL A 1 47  ? 4.462  9.061  22.301  1.00 3.16  ? 47  VAL A C   1 
ATOM   361  O  O   . VAL A 1 47  ? 3.234  9.079  22.247  1.00 3.09  ? 47  VAL A O   1 
ATOM   362  C  CB  . VAL A 1 47  ? 4.788  6.625  23.011  1.00 3.46  ? 47  VAL A CB  1 
ATOM   363  C  CG1 . VAL A 1 47  ? 4.820  6.247  21.532  1.00 3.43  ? 47  VAL A CG1 1 
ATOM   364  C  CG2 . VAL A 1 47  ? 5.682  5.691  23.828  1.00 3.45  ? 47  VAL A CG2 1 
ATOM   365  N  N   . GLY A 1 48  ? 5.280  9.856  21.596  1.00 2.90  ? 48  GLY A N   1 
ATOM   366  C  CA  . GLY A 1 48  ? 4.789  10.835 20.641  1.00 2.72  ? 48  GLY A CA  1 
ATOM   367  C  C   . GLY A 1 48  ? 4.954  10.336 19.209  1.00 2.51  ? 48  GLY A C   1 
ATOM   368  O  O   . GLY A 1 48  ? 5.741  9.420  18.978  1.00 2.48  ? 48  GLY A O   1 
ATOM   369  N  N   . THR A 1 49  ? 4.224  10.971 18.278  1.00 2.28  ? 49  THR A N   1 
ATOM   370  C  CA  . THR A 1 49  ? 4.141  10.531 16.894  1.00 2.12  ? 49  THR A CA  1 
ATOM   371  C  C   . THR A 1 49  ? 4.279  11.740 15.966  1.00 1.99  ? 49  THR A C   1 
ATOM   372  O  O   . THR A 1 49  ? 3.751  12.805 16.279  1.00 1.97  ? 49  THR A O   1 
ATOM   373  C  CB  . THR A 1 49  ? 2.830  9.767  16.675  1.00 2.11  ? 49  THR A CB  1 
ATOM   374  O  OG1 . THR A 1 49  ? 2.800  8.674  17.601  1.00 2.09  ? 49  THR A OG1 1 
ATOM   375  C  CG2 . THR A 1 49  ? 2.650  9.287  15.248  1.00 2.11  ? 49  THR A CG2 1 
ATOM   376  N  N   . ALA A 1 50  ? 4.986  11.557 14.831  1.00 1.84  ? 50  ALA A N   1 
ATOM   377  C  CA  . ALA A 1 50  ? 5.414  12.638 13.946  1.00 1.72  ? 50  ALA A CA  1 
ATOM   378  C  C   . ALA A 1 50  ? 5.102  12.300 12.484  1.00 1.62  ? 50  ALA A C   1 
ATOM   379  O  O   . ALA A 1 50  ? 5.517  11.254 12.011  1.00 1.61  ? 50  ALA A O   1 
ATOM   380  C  CB  . ALA A 1 50  ? 6.888  12.867 14.145  1.00 1.72  ? 50  ALA A CB  1 
ATOM   381  N  N   . HIS A 1 51  ? 4.376  13.193 11.781  1.00 1.51  ? 51  HIS A N   1 
ATOM   382  C  CA  . HIS A 1 51  ? 3.935  13.003 10.396  1.00 1.43  ? 51  HIS A CA  1 
ATOM   383  C  C   . HIS A 1 51  ? 4.511  14.104 9.491   1.00 1.33  ? 51  HIS A C   1 
ATOM   384  O  O   . HIS A 1 51  ? 4.208  15.276 9.678   1.00 1.31  ? 51  HIS A O   1 
ATOM   385  C  CB  . HIS A 1 51  ? 2.400  13.027 10.300  1.00 1.44  ? 51  HIS A CB  1 
ATOM   386  C  CG  . HIS A 1 51  ? 1.671  11.943 11.041  1.00 1.45  ? 51  HIS A CG  1 
ATOM   387  N  ND1 . HIS A 1 51  ? 1.404  10.694 10.510  1.00 1.46  ? 51  HIS A ND1 1 
ATOM   388  C  CD2 . HIS A 1 51  ? 1.102  11.955 12.269  1.00 1.45  ? 51  HIS A CD2 1 
ATOM   389  C  CE1 . HIS A 1 51  ? 0.738  9.969  11.406  1.00 1.45  ? 51  HIS A CE1 1 
ATOM   390  N  NE2 . HIS A 1 51  ? 0.548  10.714 12.484  1.00 1.45  ? 51  HIS A NE2 1 
ATOM   391  N  N   . ILE A 1 52  ? 5.349  13.724 8.512   1.00 1.25  ? 52  ILE A N   1 
ATOM   392  C  CA  . ILE A 1 52  ? 6.019  14.644 7.604   1.00 1.18  ? 52  ILE A CA  1 
ATOM   393  C  C   . ILE A 1 52  ? 5.401  14.446 6.223   1.00 1.11  ? 52  ILE A C   1 
ATOM   394  O  O   . ILE A 1 52  ? 5.148  13.307 5.863   1.00 1.12  ? 52  ILE A O   1 
ATOM   395  C  CB  . ILE A 1 52  ? 7.537  14.355 7.598   1.00 1.18  ? 52  ILE A CB  1 
ATOM   396  C  CG1 . ILE A 1 52  ? 8.188  14.793 8.906   1.00 1.18  ? 52  ILE A CG1 1 
ATOM   397  C  CG2 . ILE A 1 52  ? 8.254  14.984 6.412   1.00 1.19  ? 52  ILE A CG2 1 
ATOM   398  C  CD1 . ILE A 1 52  ? 7.865  13.899 10.054  1.00 1.18  ? 52  ILE A CD1 1 
ATOM   399  N  N   . ILE A 1 53  ? 5.169  15.528 5.458   1.00 1.02  ? 53  ILE A N   1 
ATOM   400  C  CA  . ILE A 1 53  ? 4.607  15.435 4.110   1.00 0.96  ? 53  ILE A CA  1 
ATOM   401  C  C   . ILE A 1 53  ? 5.173  16.531 3.194   1.00 0.90  ? 53  ILE A C   1 
ATOM   402  O  O   . ILE A 1 53  ? 5.522  17.623 3.640   1.00 0.89  ? 53  ILE A O   1 
ATOM   403  C  CB  . ILE A 1 53  ? 3.061  15.476 4.141   1.00 0.95  ? 53  ILE A CB  1 
ATOM   404  C  CG1 . ILE A 1 53  ? 2.537  16.572 5.072   1.00 0.95  ? 53  ILE A CG1 1 
ATOM   405  C  CG2 . ILE A 1 53  ? 2.474  14.126 4.510   1.00 0.95  ? 53  ILE A CG2 1 
ATOM   406  C  CD1 . ILE A 1 53  ? 1.095  16.984 4.806   1.00 0.95  ? 53  ILE A CD1 1 
ATOM   407  N  N   . TYR A 1 54  ? 5.242  16.215 1.890   1.00 0.83  ? 54  TYR A N   1 
ATOM   408  C  CA  . TYR A 1 54  ? 5.581  17.136 0.811   1.00 0.78  ? 54  TYR A CA  1 
ATOM   409  C  C   . TYR A 1 54  ? 4.982  16.614 -0.490  1.00 0.74  ? 54  TYR A C   1 
ATOM   410  O  O   . TYR A 1 54  ? 4.756  15.418 -0.613  1.00 0.74  ? 54  TYR A O   1 
ATOM   411  C  CB  . TYR A 1 54  ? 7.097  17.232 0.654   1.00 0.78  ? 54  TYR A CB  1 
ATOM   412  C  CG  . TYR A 1 54  ? 7.617  18.102 -0.468  1.00 0.77  ? 54  TYR A CG  1 
ATOM   413  C  CD1 . TYR A 1 54  ? 7.742  19.477 -0.329  1.00 0.77  ? 54  TYR A CD1 1 
ATOM   414  C  CD2 . TYR A 1 54  ? 8.054  17.538 -1.653  1.00 0.77  ? 54  TYR A CD2 1 
ATOM   415  C  CE1 . TYR A 1 54  ? 8.262  20.269 -1.341  1.00 0.77  ? 54  TYR A CE1 1 
ATOM   416  C  CE2 . TYR A 1 54  ? 8.588  18.312 -2.669  1.00 0.77  ? 54  TYR A CE2 1 
ATOM   417  C  CZ  . TYR A 1 54  ? 8.694  19.684 -2.520  1.00 0.77  ? 54  TYR A CZ  1 
ATOM   418  O  OH  . TYR A 1 54  ? 9.229  20.420 -3.562  1.00 0.77  ? 54  TYR A OH  1 
ATOM   419  N  N   . ASN A 1 55  ? 4.709  17.508 -1.447  1.00 0.70  ? 55  ASN A N   1 
ATOM   420  C  CA  . ASN A 1 55  ? 4.503  17.104 -2.831  1.00 0.67  ? 55  ASN A CA  1 
ATOM   421  C  C   . ASN A 1 55  ? 4.982  18.216 -3.755  1.00 0.64  ? 55  ASN A C   1 
ATOM   422  O  O   . ASN A 1 55  ? 4.873  19.388 -3.436  1.00 0.63  ? 55  ASN A O   1 
ATOM   423  C  CB  . ASN A 1 55  ? 3.060  16.690 -3.153  1.00 0.67  ? 55  ASN A CB  1 
ATOM   424  C  CG  . ASN A 1 55  ? 2.020  17.799 -3.096  1.00 0.67  ? 55  ASN A CG  1 
ATOM   425  O  OD1 . ASN A 1 55  ? 2.089  18.802 -3.805  1.00 0.67  ? 55  ASN A OD1 1 
ATOM   426  N  ND2 . ASN A 1 55  ? 0.999  17.603 -2.283  1.00 0.67  ? 55  ASN A ND2 1 
ATOM   427  N  N   . SER A 1 56  ? 5.457  17.833 -4.934  1.00 0.60  ? 56  SER A N   1 
ATOM   428  C  CA  . SER A 1 56  ? 6.107  18.758 -5.843  1.00 0.57  ? 56  SER A CA  1 
ATOM   429  C  C   . SER A 1 56  ? 5.103  19.610 -6.607  1.00 0.54  ? 56  SER A C   1 
ATOM   430  O  O   . SER A 1 56  ? 5.513  20.423 -7.425  1.00 0.54  ? 56  SER A O   1 
ATOM   431  C  CB  . SER A 1 56  ? 6.995  18.016 -6.798  1.00 0.57  ? 56  SER A CB  1 
ATOM   432  O  OG  . SER A 1 56  ? 6.223  17.240 -7.696  1.00 0.57  ? 56  SER A OG  1 
ATOM   433  N  N   . VAL A 1 57  ? 3.811  19.416 -6.358  1.00 0.52  ? 57  VAL A N   1 
ATOM   434  C  CA  . VAL A 1 57  ? 2.802  20.315 -6.893  1.00 0.51  ? 57  VAL A CA  1 
ATOM   435  C  C   . VAL A 1 57  ? 2.663  21.533 -5.982  1.00 0.50  ? 57  VAL A C   1 
ATOM   436  O  O   . VAL A 1 57  ? 2.691  22.674 -6.433  1.00 0.50  ? 57  VAL A O   1 
ATOM   437  C  CB  . VAL A 1 57  ? 1.452  19.595 -7.034  1.00 0.50  ? 57  VAL A CB  1 
ATOM   438  C  CG1 . VAL A 1 57  ? 0.338  20.557 -7.417  1.00 0.50  ? 57  VAL A CG1 1 
ATOM   439  C  CG2 . VAL A 1 57  ? 1.556  18.438 -8.015  1.00 0.50  ? 57  VAL A CG2 1 
ATOM   440  N  N   . ASP A 1 58  ? 2.482  21.244 -4.692  1.00 0.50  ? 58  ASP A N   1 
ATOM   441  C  CA  . ASP A 1 58  ? 2.283  22.240 -3.654  1.00 0.50  ? 58  ASP A CA  1 
ATOM   442  C  C   . ASP A 1 58  ? 3.626  22.760 -3.140  1.00 0.50  ? 58  ASP A C   1 
ATOM   443  O  O   . ASP A 1 58  ? 3.662  23.797 -2.501  1.00 0.50  ? 58  ASP A O   1 
ATOM   444  C  CB  . ASP A 1 58  ? 1.438  21.629 -2.531  1.00 0.50  ? 58  ASP A CB  1 
ATOM   445  C  CG  . ASP A 1 58  ? 0.097  21.137 -3.045  1.00 0.50  ? 58  ASP A CG  1 
ATOM   446  O  OD1 . ASP A 1 58  ? -0.321 21.590 -4.140  1.00 0.50  ? 58  ASP A OD1 1 
ATOM   447  O  OD2 . ASP A 1 58  ? -0.503 20.290 -2.373  1.00 0.50  ? 58  ASP A OD2 1 
ATOM   448  N  N   . LYS A 1 59  ? 4.711  22.020 -3.386  1.00 0.50  ? 59  LYS A N   1 
ATOM   449  C  CA  . LYS A 1 59  ? 6.046  22.403 -2.957  1.00 0.50  ? 59  LYS A CA  1 
ATOM   450  C  C   . LYS A 1 59  ? 5.996  22.994 -1.551  1.00 0.50  ? 59  LYS A C   1 
ATOM   451  O  O   . LYS A 1 59  ? 6.448  24.109 -1.324  1.00 0.50  ? 59  LYS A O   1 
ATOM   452  C  CB  . LYS A 1 59  ? 6.645  23.388 -3.962  1.00 0.50  ? 59  LYS A CB  1 
ATOM   453  C  CG  . LYS A 1 59  ? 6.558  22.955 -5.417  1.00 0.50  ? 59  LYS A CG  1 
ATOM   454  C  CD  . LYS A 1 59  ? 7.180  23.958 -6.373  1.00 0.50  ? 59  LYS A CD  1 
ATOM   455  C  CE  . LYS A 1 59  ? 7.156  23.562 -7.838  1.00 0.50  ? 59  LYS A CE  1 
ATOM   456  N  NZ  . LYS A 1 59  ? 7.720  22.207 -8.050  1.00 0.50  ? 59  LYS A NZ  1 
ATOM   457  N  N   . ARG A 1 60  ? 5.415  22.234 -0.619  1.00 0.50  ? 60  ARG A N   1 
ATOM   458  C  CA  . ARG A 1 60  ? 5.222  22.671 0.758   1.00 0.51  ? 60  ARG A CA  1 
ATOM   459  C  C   . ARG A 1 60  ? 5.527  21.493 1.675   1.00 0.51  ? 60  ARG A C   1 
ATOM   460  O  O   . ARG A 1 60  ? 5.078  20.380 1.405   1.00 0.51  ? 60  ARG A O   1 
ATOM   461  C  CB  . ARG A 1 60  ? 3.787  23.162 0.989   1.00 0.50  ? 60  ARG A CB  1 
ATOM   462  C  CG  . ARG A 1 60  ? 3.559  23.909 2.298   1.00 0.51  ? 60  ARG A CG  1 
ATOM   463  C  CD  . ARG A 1 60  ? 2.108  24.361 2.343   1.00 0.51  ? 60  ARG A CD  1 
ATOM   464  N  NE  . ARG A 1 60  ? 1.719  25.179 3.493   1.00 0.51  ? 60  ARG A NE  1 
ATOM   465  C  CZ  . ARG A 1 60  ? 1.391  26.468 3.451   1.00 0.51  ? 60  ARG A CZ  1 
ATOM   466  N  NH1 . ARG A 1 60  ? 1.583  27.186 2.361   1.00 0.51  ? 60  ARG A NH1 1 
ATOM   467  N  NH2 . ARG A 1 60  ? 0.928  27.067 4.530   1.00 0.51  ? 60  ARG A NH2 1 
ATOM   468  N  N   . LEU A 1 61  ? 6.297  21.761 2.736   1.00 0.52  ? 61  LEU A N   1 
ATOM   469  C  CA  . LEU A 1 61  ? 6.770  20.742 3.652   1.00 0.52  ? 61  LEU A CA  1 
ATOM   470  C  C   . LEU A 1 61  ? 6.059  20.969 4.978   1.00 0.54  ? 61  LEU A C   1 
ATOM   471  O  O   . LEU A 1 61  ? 6.182  22.034 5.564   1.00 0.54  ? 61  LEU A O   1 
ATOM   472  C  CB  . LEU A 1 61  ? 8.292  20.881 3.759   1.00 0.52  ? 61  LEU A CB  1 
ATOM   473  C  CG  . LEU A 1 61  ? 8.983  19.927 4.728   1.00 0.51  ? 61  LEU A CG  1 
ATOM   474  C  CD1 . LEU A 1 61  ? 8.649  18.482 4.405   1.00 0.51  ? 61  LEU A CD1 1 
ATOM   475  C  CD2 . LEU A 1 61  ? 10.489 20.132 4.714   1.00 0.51  ? 61  LEU A CD2 1 
ATOM   476  N  N   . SER A 1 62  ? 5.232  20.016 5.405   1.00 0.56  ? 62  SER A N   1 
ATOM   477  C  CA  . SER A 1 62  ? 4.343  20.240 6.544   1.00 0.57  ? 62  SER A CA  1 
ATOM   478  C  C   . SER A 1 62  ? 4.488  19.076 7.531   1.00 0.59  ? 62  SER A C   1 
ATOM   479  O  O   . SER A 1 62  ? 4.646  17.924 7.103   1.00 0.60  ? 62  SER A O   1 
ATOM   480  C  CB  . SER A 1 62  ? 2.893  20.424 6.096   1.00 0.57  ? 62  SER A CB  1 
ATOM   481  O  OG  . SER A 1 62  ? 2.768  21.412 5.083   1.00 0.56  ? 62  SER A OG  1 
ATOM   482  N  N   . ALA A 1 63  ? 4.455  19.364 8.844   1.00 0.61  ? 63  ALA A N   1 
ATOM   483  C  CA  . ALA A 1 63  ? 4.589  18.309 9.836   1.00 0.64  ? 63  ALA A CA  1 
ATOM   484  C  C   . ALA A 1 63  ? 3.619  18.527 10.988  1.00 0.65  ? 63  ALA A C   1 
ATOM   485  O  O   . ALA A 1 63  ? 3.214  19.639 11.258  1.00 0.65  ? 63  ALA A O   1 
ATOM   486  C  CB  . ALA A 1 63  ? 6.015  18.213 10.314  1.00 0.64  ? 63  ALA A CB  1 
ATOM   487  N  N   . VAL A 1 64  ? 3.263  17.439 11.662  1.00 0.68  ? 64  VAL A N   1 
ATOM   488  C  CA  . VAL A 1 64  ? 2.257  17.422 12.712  1.00 0.70  ? 64  VAL A CA  1 
ATOM   489  C  C   . VAL A 1 64  ? 2.776  16.466 13.786  1.00 0.73  ? 64  VAL A C   1 
ATOM   490  O  O   . VAL A 1 64  ? 3.182  15.343 13.451  1.00 0.74  ? 64  VAL A O   1 
ATOM   491  C  CB  . VAL A 1 64  ? 0.894  16.923 12.177  1.00 0.69  ? 64  VAL A CB  1 
ATOM   492  C  CG1 . VAL A 1 64  ? -0.242 17.161 13.166  1.00 0.69  ? 64  VAL A CG1 1 
ATOM   493  C  CG2 . VAL A 1 64  ? 0.571  17.521 10.813  1.00 0.69  ? 64  VAL A CG2 1 
ATOM   494  N  N   . VAL A 1 65  ? 2.781  16.887 15.062  1.00 0.76  ? 65  VAL A N   1 
ATOM   495  C  CA  . VAL A 1 65  ? 3.302  16.024 16.112  1.00 0.78  ? 65  VAL A CA  1 
ATOM   496  C  C   . VAL A 1 65  ? 2.233  15.925 17.184  1.00 0.80  ? 65  VAL A C   1 
ATOM   497  O  O   . VAL A 1 65  ? 1.617  16.922 17.523  1.00 0.79  ? 65  VAL A O   1 
ATOM   498  C  CB  . VAL A 1 65  ? 4.653  16.511 16.670  1.00 0.79  ? 65  VAL A CB  1 
ATOM   499  C  CG1 . VAL A 1 65  ? 5.163  15.579 17.744  1.00 0.79  ? 65  VAL A CG1 1 
ATOM   500  C  CG2 . VAL A 1 65  ? 5.703  16.661 15.581  1.00 0.79  ? 65  VAL A CG2 1 
ATOM   501  N  N   . SER A 1 66  ? 2.051  14.716 17.712  1.00 0.83  ? 66  SER A N   1 
ATOM   502  C  CA  . SER A 1 66  ? 0.809  14.341 18.359  1.00 0.85  ? 66  SER A CA  1 
ATOM   503  C  C   . SER A 1 66  ? 1.062  13.276 19.408  1.00 0.87  ? 66  SER A C   1 
ATOM   504  O  O   . SER A 1 66  ? 1.492  12.171 19.070  1.00 0.88  ? 66  SER A O   1 
ATOM   505  C  CB  . SER A 1 66  ? -0.207 13.847 17.352  1.00 0.86  ? 66  SER A CB  1 
ATOM   506  O  OG  . SER A 1 66  ? 0.425  13.207 16.242  1.00 0.86  ? 66  SER A OG  1 
ATOM   507  N  N   . TYR A 1 67  ? 0.777  13.636 20.666  1.00 0.89  ? 67  TYR A N   1 
ATOM   508  C  CA  . TYR A 1 67  ? 0.700  12.685 21.764  1.00 0.91  ? 67  TYR A CA  1 
ATOM   509  C  C   . TYR A 1 67  ? -0.757 12.279 21.912  1.00 0.87  ? 67  TYR A C   1 
ATOM   510  O  O   . TYR A 1 67  ? -1.632 13.028 21.504  1.00 0.87  ? 67  TYR A O   1 
ATOM   511  C  CB  . TYR A 1 67  ? 1.236  13.315 23.050  1.00 0.95  ? 67  TYR A CB  1 
ATOM   512  C  CG  . TYR A 1 67  ? 2.737  13.422 23.151  1.00 1.01  ? 67  TYR A CG  1 
ATOM   513  C  CD1 . TYR A 1 67  ? 3.495  12.325 23.508  1.00 1.05  ? 67  TYR A CD1 1 
ATOM   514  C  CD2 . TYR A 1 67  ? 3.400  14.614 22.904  1.00 1.04  ? 67  TYR A CD2 1 
ATOM   515  C  CE1 . TYR A 1 67  ? 4.872  12.411 23.636  1.00 1.08  ? 67  TYR A CE1 1 
ATOM   516  C  CE2 . TYR A 1 67  ? 4.775  14.720 23.025  1.00 1.07  ? 67  TYR A CE2 1 
ATOM   517  C  CZ  . TYR A 1 67  ? 5.516  13.612 23.399  1.00 1.09  ? 67  TYR A CZ  1 
ATOM   518  O  OH  . TYR A 1 67  ? 6.879  13.639 23.547  1.00 1.10  ? 67  TYR A OH  1 
ATOM   519  N  N   . PRO A 1 68  ? -1.091 11.094 22.456  1.00 0.83  ? 68  PRO A N   1 
ATOM   520  C  CA  . PRO A 1 68  ? -2.492 10.762 22.712  1.00 0.81  ? 68  PRO A CA  1 
ATOM   521  C  C   . PRO A 1 68  ? -3.047 11.683 23.791  1.00 0.77  ? 68  PRO A C   1 
ATOM   522  O  O   . PRO A 1 68  ? -2.279 12.223 24.589  1.00 0.78  ? 68  PRO A O   1 
ATOM   523  C  CB  . PRO A 1 68  ? -2.479 9.297  23.186  1.00 0.81  ? 68  PRO A CB  1 
ATOM   524  C  CG  . PRO A 1 68  ? -1.074 8.783  22.859  1.00 0.82  ? 68  PRO A CG  1 
ATOM   525  C  CD  . PRO A 1 68  ? -0.176 10.008 22.836  1.00 0.82  ? 68  PRO A CD  1 
ATOM   526  N  N   . ASN A 1 69  ? -4.377 11.861 23.784  1.00 0.74  ? 69  ASN A N   1 
ATOM   527  C  CA  . ASN A 1 69  ? -5.122 12.649 24.773  1.00 0.71  ? 69  ASN A CA  1 
ATOM   528  C  C   . ASN A 1 69  ? -4.862 14.142 24.608  1.00 0.68  ? 69  ASN A C   1 
ATOM   529  O  O   . ASN A 1 69  ? -5.309 14.928 25.445  1.00 0.68  ? 69  ASN A O   1 
ATOM   530  C  CB  . ASN A 1 69  ? -4.847 12.224 26.226  1.00 0.71  ? 69  ASN A CB  1 
ATOM   531  C  CG  . ASN A 1 69  ? -5.356 10.833 26.563  1.00 0.72  ? 69  ASN A CG  1 
ATOM   532  O  OD1 . ASN A 1 69  ? -4.921 10.256 27.555  1.00 0.72  ? 69  ASN A OD1 1 
ATOM   533  N  ND2 . ASN A 1 69  ? -6.253 10.274 25.759  1.00 0.71  ? 69  ASN A ND2 1 
ATOM   534  N  N   . ALA A 1 70  ? -4.220 14.512 23.490  1.00 0.65  ? 70  ALA A N   1 
ATOM   535  C  CA  . ALA A 1 70  ? -3.554 15.796 23.386  1.00 0.63  ? 70  ALA A CA  1 
ATOM   536  C  C   . ALA A 1 70  ? -3.762 16.427 22.012  1.00 0.60  ? 70  ALA A C   1 
ATOM   537  O  O   . ALA A 1 70  ? -4.002 15.747 21.014  1.00 0.60  ? 70  ALA A O   1 
ATOM   538  C  CB  . ALA A 1 70  ? -2.094 15.617 23.694  1.00 0.62  ? 70  ALA A CB  1 
ATOM   539  N  N   . ASP A 1 71  ? -3.672 17.757 21.997  1.00 0.58  ? 71  ASP A N   1 
ATOM   540  C  CA  . ASP A 1 71  ? -3.664 18.502 20.758  1.00 0.57  ? 71  ASP A CA  1 
ATOM   541  C  C   . ASP A 1 71  ? -2.323 18.277 20.084  1.00 0.56  ? 71  ASP A C   1 
ATOM   542  O  O   . ASP A 1 71  ? -1.326 17.989 20.742  1.00 0.55  ? 71  ASP A O   1 
ATOM   543  C  CB  . ASP A 1 71  ? -3.914 19.991 20.982  1.00 0.57  ? 71  ASP A CB  1 
ATOM   544  C  CG  . ASP A 1 71  ? -5.252 20.242 21.653  1.00 0.57  ? 71  ASP A CG  1 
ATOM   545  O  OD1 . ASP A 1 71  ? -6.273 19.720 21.147  1.00 0.57  ? 71  ASP A OD1 1 
ATOM   546  O  OD2 . ASP A 1 71  ? -5.262 20.937 22.688  1.00 0.57  ? 71  ASP A OD2 1 
ATOM   547  N  N   . SER A 1 72  ? -2.362 18.383 18.756  1.00 0.54  ? 72  SER A N   1 
ATOM   548  C  CA  . SER A 1 72  ? -1.201 18.262 17.900  1.00 0.53  ? 72  SER A CA  1 
ATOM   549  C  C   . SER A 1 72  ? -0.585 19.646 17.736  1.00 0.52  ? 72  SER A C   1 
ATOM   550  O  O   . SER A 1 72  ? -1.173 20.632 18.129  1.00 0.52  ? 72  SER A O   1 
ATOM   551  C  CB  . SER A 1 72  ? -1.592 17.607 16.575  1.00 0.53  ? 72  SER A CB  1 
ATOM   552  O  OG  . SER A 1 72  ? -2.748 18.213 16.000  1.00 0.53  ? 72  SER A OG  1 
ATOM   553  N  N   . ALA A 1 73  ? 0.644  19.698 17.249  1.00 0.52  ? 73  ALA A N   1 
ATOM   554  C  CA  . ALA A 1 73  ? 1.266  20.940 16.820  1.00 0.52  ? 73  ALA A CA  1 
ATOM   555  C  C   . ALA A 1 73  ? 1.563  20.774 15.342  1.00 0.53  ? 73  ALA A C   1 
ATOM   556  O  O   . ALA A 1 73  ? 1.917  19.675 14.922  1.00 0.53  ? 73  ALA A O   1 
ATOM   557  C  CB  . ALA A 1 73  ? 2.542  21.212 17.588  1.00 0.52  ? 73  ALA A CB  1 
ATOM   558  N  N   . THR A 1 74  ? 1.413  21.835 14.556  1.00 0.53  ? 74  THR A N   1 
ATOM   559  C  CA  . THR A 1 74  ? 1.706  21.724 13.140  1.00 0.53  ? 74  THR A CA  1 
ATOM   560  C  C   . THR A 1 74  ? 2.548  22.924 12.726  1.00 0.54  ? 74  THR A C   1 
ATOM   561  O  O   . THR A 1 74  ? 2.471  23.994 13.334  1.00 0.54  ? 74  THR A O   1 
ATOM   562  C  CB  . THR A 1 74  ? 0.421  21.507 12.328  1.00 0.52  ? 74  THR A CB  1 
ATOM   563  O  OG1 . THR A 1 74  ? 0.745  21.440 10.939  1.00 0.52  ? 74  THR A OG1 1 
ATOM   564  C  CG2 . THR A 1 74  ? -0.607 22.594 12.552  1.00 0.52  ? 74  THR A CG2 1 
ATOM   565  N  N   . VAL A 1 75  ? 3.390  22.690 11.719  1.00 0.56  ? 75  VAL A N   1 
ATOM   566  C  CA  . VAL A 1 75  ? 4.212  23.725 11.125  1.00 0.58  ? 75  VAL A CA  1 
ATOM   567  C  C   . VAL A 1 75  ? 4.272  23.383 9.638   1.00 0.60  ? 75  VAL A C   1 
ATOM   568  O  O   . VAL A 1 75  ? 4.103  22.222 9.298   1.00 0.60  ? 75  VAL A O   1 
ATOM   569  C  CB  . VAL A 1 75  ? 5.579  23.814 11.848  1.00 0.59  ? 75  VAL A CB  1 
ATOM   570  C  CG1 . VAL A 1 75  ? 6.427  22.560 11.703  1.00 0.60  ? 75  VAL A CG1 1 
ATOM   571  C  CG2 . VAL A 1 75  ? 6.371  25.041 11.436  1.00 0.59  ? 75  VAL A CG2 1 
ATOM   572  N  N   . SER A 1 76  ? 4.377  24.383 8.755   1.00 0.62  ? 76  SER A N   1 
ATOM   573  C  CA  . SER A 1 76  ? 4.557  24.163 7.322   1.00 0.64  ? 76  SER A CA  1 
ATOM   574  C  C   . SER A 1 76  ? 5.491  25.239 6.781   1.00 0.67  ? 76  SER A C   1 
ATOM   575  O  O   . SER A 1 76  ? 5.652  26.300 7.376   1.00 0.68  ? 76  SER A O   1 
ATOM   576  C  CB  . SER A 1 76  ? 3.256  24.199 6.531   1.00 0.63  ? 76  SER A CB  1 
ATOM   577  O  OG  . SER A 1 76  ? 2.265  23.336 7.072   1.00 0.63  ? 76  SER A OG  1 
ATOM   578  N  N   . TYR A 1 77  ? 6.059  24.993 5.608   1.00 0.70  ? 77  TYR A N   1 
ATOM   579  C  CA  . TYR A 1 77  ? 6.872  26.004 4.968   1.00 0.73  ? 77  TYR A CA  1 
ATOM   580  C  C   . TYR A 1 77  ? 6.940  25.687 3.483   1.00 0.77  ? 77  TYR A C   1 
ATOM   581  O  O   . TYR A 1 77  ? 7.228  24.551 3.121   1.00 0.78  ? 77  TYR A O   1 
ATOM   582  C  CB  . TYR A 1 77  ? 8.244  26.030 5.629   1.00 0.72  ? 77  TYR A CB  1 
ATOM   583  C  CG  . TYR A 1 77  ? 9.233  26.971 4.997   1.00 0.71  ? 77  TYR A CG  1 
ATOM   584  C  CD1 . TYR A 1 77  ? 9.037  28.348 4.993   1.00 0.70  ? 77  TYR A CD1 1 
ATOM   585  C  CD2 . TYR A 1 77  ? 10.377 26.468 4.401   1.00 0.71  ? 77  TYR A CD2 1 
ATOM   586  C  CE1 . TYR A 1 77  ? 9.962  29.203 4.413   1.00 0.70  ? 77  TYR A CE1 1 
ATOM   587  C  CE2 . TYR A 1 77  ? 11.311 27.309 3.824   1.00 0.70  ? 77  TYR A CE2 1 
ATOM   588  C  CZ  . TYR A 1 77  ? 11.105 28.676 3.834   1.00 0.70  ? 77  TYR A CZ  1 
ATOM   589  O  OH  . TYR A 1 77  ? 12.083 29.416 3.239   1.00 0.70  ? 77  TYR A OH  1 
ATOM   590  N  N   . ASP A 1 78  ? 6.640  26.693 2.649   1.00 0.82  ? 78  ASP A N   1 
ATOM   591  C  CA  . ASP A 1 78  ? 6.652  26.531 1.202   1.00 0.87  ? 78  ASP A CA  1 
ATOM   592  C  C   . ASP A 1 78  ? 8.087  26.533 0.721   1.00 0.92  ? 78  ASP A C   1 
ATOM   593  O  O   . ASP A 1 78  ? 8.783  27.528 0.891   1.00 0.92  ? 78  ASP A O   1 
ATOM   594  C  CB  . ASP A 1 78  ? 5.913  27.642 0.453   1.00 0.86  ? 78  ASP A CB  1 
ATOM   595  C  CG  . ASP A 1 78  ? 4.449  27.715 0.828   1.00 0.85  ? 78  ASP A CG  1 
ATOM   596  O  OD1 . ASP A 1 78  ? 3.991  26.843 1.602   1.00 0.84  ? 78  ASP A OD1 1 
ATOM   597  O  OD2 . ASP A 1 78  ? 3.800  28.655 0.379   1.00 0.85  ? 78  ASP A OD2 1 
ATOM   598  N  N   . VAL A 1 79  ? 8.461  25.411 0.098   1.00 0.99  ? 79  VAL A N   1 
ATOM   599  C  CA  . VAL A 1 79  ? 9.769  25.228 -0.502  1.00 1.05  ? 79  VAL A CA  1 
ATOM   600  C  C   . VAL A 1 79  ? 9.694  24.189 -1.633  1.00 1.10  ? 79  VAL A C   1 
ATOM   601  O  O   . VAL A 1 79  ? 9.037  23.146 -1.532  1.00 1.08  ? 79  VAL A O   1 
ATOM   602  C  CB  . VAL A 1 79  ? 10.771 24.865 0.616   1.00 1.06  ? 79  VAL A CB  1 
ATOM   603  C  CG1 . VAL A 1 79  ? 10.421 23.539 1.296   1.00 1.06  ? 79  VAL A CG1 1 
ATOM   604  C  CG2 . VAL A 1 79  ? 12.227 24.878 0.144   1.00 1.06  ? 79  VAL A CG2 1 
ATOM   605  N  N   . ASP A 1 80  ? 10.343 24.535 -2.748  1.00 1.18  ? 80  ASP A N   1 
ATOM   606  C  CA  . ASP A 1 80  ? 10.620 23.589 -3.810  1.00 1.25  ? 80  ASP A CA  1 
ATOM   607  C  C   . ASP A 1 80  ? 11.894 22.840 -3.444  1.00 1.35  ? 80  ASP A C   1 
ATOM   608  O  O   . ASP A 1 80  ? 12.994 23.385 -3.545  1.00 1.35  ? 80  ASP A O   1 
ATOM   609  C  CB  . ASP A 1 80  ? 10.784 24.246 -5.181  1.00 1.24  ? 80  ASP A CB  1 
ATOM   610  C  CG  . ASP A 1 80  ? 10.649 23.228 -6.296  1.00 1.24  ? 80  ASP A CG  1 
ATOM   611  O  OD1 . ASP A 1 80  ? 10.217 22.098 -5.996  1.00 1.25  ? 80  ASP A OD1 1 
ATOM   612  O  OD2 . ASP A 1 80  ? 10.961 23.561 -7.449  1.00 1.25  ? 80  ASP A OD2 1 
ATOM   613  N  N   . LEU A 1 81  ? 11.712 21.581 -3.028  1.00 1.46  ? 81  LEU A N   1 
ATOM   614  C  CA  . LEU A 1 81  ? 12.808 20.746 -2.557  1.00 1.57  ? 81  LEU A CA  1 
ATOM   615  C  C   . LEU A 1 81  ? 13.753 20.385 -3.719  1.00 1.69  ? 81  LEU A C   1 
ATOM   616  O  O   . LEU A 1 81  ? 14.930 20.095 -3.491  1.00 1.70  ? 81  LEU A O   1 
ATOM   617  C  CB  . LEU A 1 81  ? 12.227 19.510 -1.842  1.00 1.55  ? 81  LEU A CB  1 
ATOM   618  C  CG  . LEU A 1 81  ? 11.600 19.716 -0.451  1.00 1.55  ? 81  LEU A CG  1 
ATOM   619  C  CD1 . LEU A 1 81  ? 11.261 18.387 0.209   1.00 1.55  ? 81  LEU A CD1 1 
ATOM   620  C  CD2 . LEU A 1 81  ? 12.481 20.526 0.493   1.00 1.55  ? 81  LEU A CD2 1 
ATOM   621  N  N   . ASP A 1 82  ? 13.260 20.442 -4.967  1.00 1.83  ? 82  ASP A N   1 
ATOM   622  C  CA  . ASP A 1 82  ? 14.084 20.160 -6.135  1.00 1.95  ? 82  ASP A CA  1 
ATOM   623  C  C   . ASP A 1 82  ? 15.141 21.256 -6.324  1.00 2.05  ? 82  ASP A C   1 
ATOM   624  O  O   . ASP A 1 82  ? 16.176 21.024 -6.961  1.00 2.07  ? 82  ASP A O   1 
ATOM   625  C  CB  . ASP A 1 82  ? 13.252 20.032 -7.421  1.00 1.98  ? 82  ASP A CB  1 
ATOM   626  C  CG  . ASP A 1 82  ? 12.225 18.904 -7.455  1.00 2.00  ? 82  ASP A CG  1 
ATOM   627  O  OD1 . ASP A 1 82  ? 12.544 17.794 -6.965  1.00 2.03  ? 82  ASP A OD1 1 
ATOM   628  O  OD2 . ASP A 1 82  ? 11.124 19.143 -8.014  1.00 2.00  ? 82  ASP A OD2 1 
ATOM   629  N  N   . ASN A 1 83  ? 14.882 22.455 -5.775  1.00 2.16  ? 83  ASN A N   1 
ATOM   630  C  CA  . ASN A 1 83  ? 15.816 23.572 -5.876  1.00 2.24  ? 83  ASN A CA  1 
ATOM   631  C  C   . ASN A 1 83  ? 16.697 23.653 -4.633  1.00 2.33  ? 83  ASN A C   1 
ATOM   632  O  O   . ASN A 1 83  ? 17.327 24.679 -4.413  1.00 2.35  ? 83  ASN A O   1 
ATOM   633  C  CB  . ASN A 1 83  ? 15.089 24.900 -6.104  1.00 2.25  ? 83  ASN A CB  1 
ATOM   634  C  CG  . ASN A 1 83  ? 14.241 24.853 -7.359  1.00 2.27  ? 83  ASN A CG  1 
ATOM   635  O  OD1 . ASN A 1 83  ? 14.332 23.898 -8.138  1.00 2.31  ? 83  ASN A OD1 1 
ATOM   636  N  ND2 . ASN A 1 83  ? 13.402 25.857 -7.565  1.00 2.26  ? 83  ASN A ND2 1 
ATOM   637  N  N   . VAL A 1 84  ? 16.762 22.567 -3.849  1.00 2.42  ? 84  VAL A N   1 
ATOM   638  C  CA  . VAL A 1 84  ? 17.479 22.552 -2.583  1.00 2.49  ? 84  VAL A CA  1 
ATOM   639  C  C   . VAL A 1 84  ? 18.405 21.343 -2.529  1.00 2.59  ? 84  VAL A C   1 
ATOM   640  O  O   . VAL A 1 84  ? 19.586 21.470 -2.207  1.00 2.58  ? 84  VAL A O   1 
ATOM   641  C  CB  . VAL A 1 84  ? 16.482 22.485 -1.415  1.00 2.46  ? 84  VAL A CB  1 
ATOM   642  C  CG1 . VAL A 1 84  ? 17.195 22.380 -0.076  1.00 2.45  ? 84  VAL A CG1 1 
ATOM   643  C  CG2 . VAL A 1 84  ? 15.523 23.660 -1.440  1.00 2.45  ? 84  VAL A CG2 1 
ATOM   644  N  N   . LEU A 1 85  ? 17.791 20.185 -2.818  1.00 2.74  ? 85  LEU A N   1 
ATOM   645  C  CA  . LEU A 1 85  ? 18.329 18.857 -2.585  1.00 2.86  ? 85  LEU A CA  1 
ATOM   646  C  C   . LEU A 1 85  ? 18.781 18.255 -3.908  1.00 2.97  ? 85  LEU A C   1 
ATOM   647  O  O   . LEU A 1 85  ? 18.192 18.540 -4.952  1.00 2.99  ? 85  LEU A O   1 
ATOM   648  C  CB  . LEU A 1 85  ? 17.220 17.983 -1.995  1.00 2.87  ? 85  LEU A CB  1 
ATOM   649  C  CG  . LEU A 1 85  ? 16.868 18.282 -0.539  1.00 2.91  ? 85  LEU A CG  1 
ATOM   650  C  CD1 . LEU A 1 85  ? 15.419 17.905 -0.209  1.00 2.90  ? 85  LEU A CD1 1 
ATOM   651  C  CD2 . LEU A 1 85  ? 17.837 17.556 0.386   1.00 2.93  ? 85  LEU A CD2 1 
ATOM   652  N  N   . PRO A 1 86  ? 19.787 17.351 -3.886  1.00 3.06  ? 86  PRO A N   1 
ATOM   653  C  CA  . PRO A 1 86  ? 20.210 16.663 -5.097  1.00 3.13  ? 86  PRO A CA  1 
ATOM   654  C  C   . PRO A 1 86  ? 19.085 15.746 -5.568  1.00 3.29  ? 86  PRO A C   1 
ATOM   655  O  O   . PRO A 1 86  ? 18.094 15.550 -4.863  1.00 3.37  ? 86  PRO A O   1 
ATOM   656  C  CB  . PRO A 1 86  ? 21.473 15.928 -4.646  1.00 3.09  ? 86  PRO A CB  1 
ATOM   657  C  CG  . PRO A 1 86  ? 21.293 15.716 -3.172  1.00 3.06  ? 86  PRO A CG  1 
ATOM   658  C  CD  . PRO A 1 86  ? 20.525 16.922 -2.691  1.00 3.05  ? 86  PRO A CD  1 
ATOM   659  N  N   . GLU A 1 87  ? 19.234 15.197 -6.775  1.00 3.42  ? 87  GLU A N   1 
ATOM   660  C  CA  . GLU A 1 87  ? 18.162 14.430 -7.389  1.00 3.48  ? 87  GLU A CA  1 
ATOM   661  C  C   . GLU A 1 87  ? 18.040 13.071 -6.690  1.00 3.38  ? 87  GLU A C   1 
ATOM   662  O  O   . GLU A 1 87  ? 16.936 12.542 -6.594  1.00 3.42  ? 87  GLU A O   1 
ATOM   663  C  CB  . GLU A 1 87  ? 18.422 14.423 -8.901  1.00 3.65  ? 87  GLU A CB  1 
ATOM   664  C  CG  . GLU A 1 87  ? 17.882 13.221 -9.664  1.00 3.77  ? 87  GLU A CG  1 
ATOM   665  C  CD  . GLU A 1 87  ? 18.366 13.164 -11.107 1.00 3.84  ? 87  GLU A CD  1 
ATOM   666  O  OE1 . GLU A 1 87  ? 18.744 14.228 -11.649 1.00 3.83  ? 87  GLU A OE1 1 
ATOM   667  O  OE2 . GLU A 1 87  ? 18.414 12.045 -11.662 1.00 3.86  ? 87  GLU A OE2 1 
ATOM   668  N  N   . TRP A 1 88  ? 19.156 12.543 -6.155  1.00 3.28  ? 88  TRP A N   1 
ATOM   669  C  CA  . TRP A 1 88  ? 19.167 11.329 -5.334  1.00 3.19  ? 88  TRP A CA  1 
ATOM   670  C  C   . TRP A 1 88  ? 19.651 11.627 -3.914  1.00 3.12  ? 88  TRP A C   1 
ATOM   671  O  O   . TRP A 1 88  ? 20.641 12.331 -3.716  1.00 3.10  ? 88  TRP A O   1 
ATOM   672  C  CB  . TRP A 1 88  ? 20.079 10.255 -5.929  1.00 3.20  ? 88  TRP A CB  1 
ATOM   673  C  CG  . TRP A 1 88  ? 19.576 9.489  -7.110  1.00 3.20  ? 88  TRP A CG  1 
ATOM   674  C  CD1 . TRP A 1 88  ? 19.897 9.681  -8.423  1.00 3.21  ? 88  TRP A CD1 1 
ATOM   675  C  CD2 . TRP A 1 88  ? 18.767 8.306  -7.062  1.00 3.18  ? 88  TRP A CD2 1 
ATOM   676  N  NE1 . TRP A 1 88  ? 19.289 8.731  -9.200  1.00 3.21  ? 88  TRP A NE1 1 
ATOM   677  C  CE2 . TRP A 1 88  ? 18.596 7.872  -8.389  1.00 3.18  ? 88  TRP A CE2 1 
ATOM   678  C  CE3 . TRP A 1 88  ? 18.155 7.600  -6.028  1.00 3.16  ? 88  TRP A CE3 1 
ATOM   679  C  CZ2 . TRP A 1 88  ? 17.842 6.752  -8.708  1.00 3.19  ? 88  TRP A CZ2 1 
ATOM   680  C  CZ3 . TRP A 1 88  ? 17.409 6.496  -6.346  1.00 3.18  ? 88  TRP A CZ3 1 
ATOM   681  C  CH2 . TRP A 1 88  ? 17.265 6.073  -7.666  1.00 3.20  ? 88  TRP A CH2 1 
ATOM   682  N  N   . VAL A 1 89  ? 19.002 10.993 -2.933  1.00 3.08  ? 89  VAL A N   1 
ATOM   683  C  CA  . VAL A 1 89  ? 19.060 11.427 -1.546  1.00 3.04  ? 89  VAL A CA  1 
ATOM   684  C  C   . VAL A 1 89  ? 18.907 10.199 -0.649  1.00 2.92  ? 89  VAL A C   1 
ATOM   685  O  O   . VAL A 1 89  ? 18.333 9.201  -1.076  1.00 2.91  ? 89  VAL A O   1 
ATOM   686  C  CB  . VAL A 1 89  ? 17.957 12.469 -1.236  1.00 3.11  ? 89  VAL A CB  1 
ATOM   687  C  CG1 . VAL A 1 89  ? 18.140 13.785 -1.973  1.00 3.13  ? 89  VAL A CG1 1 
ATOM   688  C  CG2 . VAL A 1 89  ? 16.559 11.937 -1.516  1.00 3.16  ? 89  VAL A CG2 1 
ATOM   689  N  N   . ARG A 1 90  ? 19.416 10.303 0.590   1.00 2.80  ? 90  ARG A N   1 
ATOM   690  C  CA  . ARG A 1 90  ? 19.088 9.379  1.664   1.00 2.69  ? 90  ARG A CA  1 
ATOM   691  C  C   . ARG A 1 90  ? 18.267 10.105 2.722   1.00 2.57  ? 90  ARG A C   1 
ATOM   692  O  O   . ARG A 1 90  ? 18.454 11.297 2.934   1.00 2.54  ? 90  ARG A O   1 
ATOM   693  C  CB  . ARG A 1 90  ? 20.352 8.789  2.289   1.00 2.73  ? 90  ARG A CB  1 
ATOM   694  C  CG  . ARG A 1 90  ? 20.990 7.678  1.464   1.00 2.76  ? 90  ARG A CG  1 
ATOM   695  C  CD  . ARG A 1 90  ? 21.852 6.735  2.286   1.00 2.80  ? 90  ARG A CD  1 
ATOM   696  N  NE  . ARG A 1 90  ? 22.092 5.484  1.572   1.00 2.84  ? 90  ARG A NE  1 
ATOM   697  C  CZ  . ARG A 1 90  ? 23.245 5.112  1.008   1.00 2.87  ? 90  ARG A CZ  1 
ATOM   698  N  NH1 . ARG A 1 90  ? 24.345 5.826  1.172   1.00 2.86  ? 90  ARG A NH1 1 
ATOM   699  N  NH2 . ARG A 1 90  ? 23.293 4.009  0.276   1.00 2.87  ? 90  ARG A NH2 1 
ATOM   700  N  N   . VAL A 1 91  ? 17.352 9.363  3.360   1.00 2.49  ? 91  VAL A N   1 
ATOM   701  C  CA  . VAL A 1 91  ? 16.474 9.875  4.405   1.00 2.42  ? 91  VAL A CA  1 
ATOM   702  C  C   . VAL A 1 91  ? 16.916 9.267  5.734   1.00 2.42  ? 91  VAL A C   1 
ATOM   703  O  O   . VAL A 1 91  ? 17.512 8.191  5.755   1.00 2.44  ? 91  VAL A O   1 
ATOM   704  C  CB  . VAL A 1 91  ? 14.994 9.572  4.110   1.00 2.37  ? 91  VAL A CB  1 
ATOM   705  C  CG1 . VAL A 1 91  ? 14.524 10.258 2.841   1.00 2.36  ? 91  VAL A CG1 1 
ATOM   706  C  CG2 . VAL A 1 91  ? 14.704 8.080  4.050   1.00 2.36  ? 91  VAL A CG2 1 
ATOM   707  N  N   . GLY A 1 92  ? 16.640 9.958  6.846   1.00 2.42  ? 92  GLY A N   1 
ATOM   708  C  CA  . GLY A 1 92  ? 17.206 9.539  8.121   1.00 2.41  ? 92  GLY A CA  1 
ATOM   709  C  C   . GLY A 1 92  ? 16.499 10.156 9.325   1.00 2.41  ? 92  GLY A C   1 
ATOM   710  O  O   . GLY A 1 92  ? 15.667 11.040 9.158   1.00 2.41  ? 92  GLY A O   1 
ATOM   711  N  N   . LEU A 1 93  ? 16.848 9.645  10.521  1.00 2.42  ? 93  LEU A N   1 
ATOM   712  C  CA  . LEU A 1 93  ? 16.474 10.209 11.811  1.00 2.42  ? 93  LEU A CA  1 
ATOM   713  C  C   . LEU A 1 93  ? 17.753 10.533 12.582  1.00 2.47  ? 93  LEU A C   1 
ATOM   714  O  O   . LEU A 1 93  ? 18.667 9.715  12.668  1.00 2.45  ? 93  LEU A O   1 
ATOM   715  C  CB  . LEU A 1 93  ? 15.604 9.217  12.593  1.00 2.38  ? 93  LEU A CB  1 
ATOM   716  C  CG  . LEU A 1 93  ? 14.301 8.775  11.927  1.00 2.35  ? 93  LEU A CG  1 
ATOM   717  C  CD1 . LEU A 1 93  ? 13.576 7.762  12.789  1.00 2.35  ? 93  LEU A CD1 1 
ATOM   718  C  CD2 . LEU A 1 93  ? 13.395 9.956  11.653  1.00 2.34  ? 93  LEU A CD2 1 
ATOM   719  N  N   . SER A 1 94  ? 17.787 11.756 13.121  1.00 2.57  ? 94  SER A N   1 
ATOM   720  C  CA  . SER A 1 94  ? 18.895 12.287 13.893  1.00 2.65  ? 94  SER A CA  1 
ATOM   721  C  C   . SER A 1 94  ? 18.345 12.813 15.205  1.00 2.77  ? 94  SER A C   1 
ATOM   722  O  O   . SER A 1 94  ? 17.184 13.206 15.266  1.00 2.74  ? 94  SER A O   1 
ATOM   723  C  CB  . SER A 1 94  ? 19.601 13.396 13.155  1.00 2.65  ? 94  SER A CB  1 
ATOM   724  O  OG  . SER A 1 94  ? 20.606 13.998 13.960  1.00 2.64  ? 94  SER A OG  1 
ATOM   725  N  N   . ALA A 1 95  ? 19.214 12.842 16.222  1.00 2.94  ? 95  ALA A N   1 
ATOM   726  C  CA  . ALA A 1 95  ? 18.886 13.367 17.540  1.00 3.07  ? 95  ALA A CA  1 
ATOM   727  C  C   . ALA A 1 95  ? 20.180 13.582 18.309  1.00 3.24  ? 95  ALA A C   1 
ATOM   728  O  O   . ALA A 1 95  ? 21.231 13.110 17.876  1.00 3.21  ? 95  ALA A O   1 
ATOM   729  C  CB  . ALA A 1 95  ? 17.976 12.417 18.274  1.00 3.06  ? 95  ALA A CB  1 
ATOM   730  N  N   . SER A 1 96  ? 20.094 14.289 19.445  1.00 3.49  ? 96  SER A N   1 
ATOM   731  C  CA  . SER A 1 96  ? 21.289 14.584 20.219  1.00 3.69  ? 96  SER A CA  1 
ATOM   732  C  C   . SER A 1 96  ? 21.000 15.122 21.620  1.00 3.89  ? 96  SER A C   1 
ATOM   733  O  O   . SER A 1 96  ? 19.874 15.465 21.968  1.00 3.77  ? 96  SER A O   1 
ATOM   734  C  CB  . SER A 1 96  ? 22.163 15.547 19.473  1.00 3.70  ? 96  SER A CB  1 
ATOM   735  O  OG  . SER A 1 96  ? 21.526 16.804 19.432  1.00 3.73  ? 96  SER A OG  1 
ATOM   736  N  N   . THR A 1 97  ? 22.107 15.183 22.383  1.00 4.26  ? 97  THR A N   1 
ATOM   737  C  CA  . THR A 1 97  ? 22.228 15.743 23.721  1.00 4.51  ? 97  THR A CA  1 
ATOM   738  C  C   . THR A 1 97  ? 23.479 16.628 23.804  1.00 4.78  ? 97  THR A C   1 
ATOM   739  O  O   . THR A 1 97  ? 24.422 16.457 23.024  1.00 4.78  ? 97  THR A O   1 
ATOM   740  C  CB  . THR A 1 97  ? 22.361 14.616 24.753  1.00 4.53  ? 97  THR A CB  1 
ATOM   741  O  OG1 . THR A 1 97  ? 23.523 13.876 24.385  1.00 4.50  ? 97  THR A OG1 1 
ATOM   742  C  CG2 . THR A 1 97  ? 21.174 13.680 24.818  1.00 4.56  ? 97  THR A CG2 1 
ATOM   743  N  N   . GLY A 1 98  ? 23.463 17.589 24.744  1.00 5.14  ? 98  GLY A N   1 
ATOM   744  C  CA  . GLY A 1 98  ? 24.652 18.308 25.191  1.00 5.39  ? 98  GLY A CA  1 
ATOM   745  C  C   . GLY A 1 98  ? 24.826 18.195 26.709  1.00 5.71  ? 98  GLY A C   1 
ATOM   746  O  O   . GLY A 1 98  ? 24.784 17.102 27.276  1.00 5.77  ? 98  GLY A O   1 
ATOM   747  N  N   . LEU A 1 99  ? 24.982 19.323 27.402  1.00 6.02  ? 99  LEU A N   1 
ATOM   748  C  CA  . LEU A 1 99  ? 25.062 19.256 28.855  1.00 6.29  ? 99  LEU A CA  1 
ATOM   749  C  C   . LEU A 1 99  ? 23.660 19.158 29.478  1.00 6.46  ? 99  LEU A C   1 
ATOM   750  O  O   . LEU A 1 99  ? 23.540 18.988 30.689  1.00 6.54  ? 99  LEU A O   1 
ATOM   751  C  CB  . LEU A 1 99  ? 25.882 20.452 29.354  1.00 6.33  ? 99  LEU A CB  1 
ATOM   752  C  CG  . LEU A 1 99  ? 27.350 20.458 28.905  1.00 6.37  ? 99  LEU A CG  1 
ATOM   753  C  CD1 . LEU A 1 99  ? 28.044 21.767 29.269  1.00 6.41  ? 99  LEU A CD1 1 
ATOM   754  C  CD2 . LEU A 1 99  ? 28.122 19.290 29.501  1.00 6.36  ? 99  LEU A CD2 1 
ATOM   755  N  N   . TYR A 1 100 ? 22.606 19.268 28.652  1.00 6.57  ? 100 TYR A N   1 
ATOM   756  C  CA  . TYR A 1 100 ? 21.286 18.761 28.990  1.00 6.72  ? 100 TYR A CA  1 
ATOM   757  C  C   . TYR A 1 100 ? 21.015 17.524 28.134  1.00 6.84  ? 100 TYR A C   1 
ATOM   758  O  O   . TYR A 1 100 ? 21.712 17.323 27.145  1.00 7.01  ? 100 TYR A O   1 
ATOM   759  C  CB  . TYR A 1 100 ? 20.249 19.858 28.790  1.00 6.83  ? 100 TYR A CB  1 
ATOM   760  C  CG  . TYR A 1 100 ? 20.433 21.078 29.658  1.00 7.10  ? 100 TYR A CG  1 
ATOM   761  C  CD1 . TYR A 1 100 ? 21.306 22.096 29.288  1.00 7.17  ? 100 TYR A CD1 1 
ATOM   762  C  CD2 . TYR A 1 100 ? 19.731 21.231 30.854  1.00 7.21  ? 100 TYR A CD2 1 
ATOM   763  C  CE1 . TYR A 1 100 ? 21.466 23.234 30.069  1.00 7.17  ? 100 TYR A CE1 1 
ATOM   764  C  CE2 . TYR A 1 100 ? 19.895 22.356 31.654  1.00 7.21  ? 100 TYR A CE2 1 
ATOM   765  C  CZ  . TYR A 1 100 ? 20.763 23.366 31.259  1.00 7.18  ? 100 TYR A CZ  1 
ATOM   766  O  OH  . TYR A 1 100 ? 20.920 24.503 32.024  1.00 7.08  ? 100 TYR A OH  1 
ATOM   767  N  N   . LYS A 1 101 ? 20.039 16.672 28.489  1.00 6.81  ? 101 LYS A N   1 
ATOM   768  C  CA  . LYS A 1 101 ? 19.927 15.397 27.782  1.00 6.85  ? 101 LYS A CA  1 
ATOM   769  C  C   . LYS A 1 101 ? 18.552 14.744 27.913  1.00 6.65  ? 101 LYS A C   1 
ATOM   770  O  O   . LYS A 1 101 ? 17.731 15.128 28.748  1.00 6.70  ? 101 LYS A O   1 
ATOM   771  C  CB  . LYS A 1 101 ? 20.964 14.415 28.327  1.00 7.13  ? 101 LYS A CB  1 
ATOM   772  C  CG  . LYS A 1 101 ? 20.753 14.043 29.785  1.00 7.38  ? 101 LYS A CG  1 
ATOM   773  C  CD  . LYS A 1 101 ? 22.036 13.917 30.575  1.00 7.64  ? 101 LYS A CD  1 
ATOM   774  C  CE  . LYS A 1 101 ? 21.787 13.726 32.061  1.00 7.79  ? 101 LYS A CE  1 
ATOM   775  N  NZ  . LYS A 1 101 ? 20.921 14.793 32.625  1.00 7.81  ? 101 LYS A NZ  1 
ATOM   776  N  N   . GLU A 1 102 ? 18.331 13.713 27.087  1.00 6.33  ? 102 GLU A N   1 
ATOM   777  C  CA  . GLU A 1 102 ? 17.095 12.945 27.119  1.00 6.14  ? 102 GLU A CA  1 
ATOM   778  C  C   . GLU A 1 102 ? 17.331 11.604 26.426  1.00 6.03  ? 102 GLU A C   1 
ATOM   779  O  O   . GLU A 1 102 ? 18.358 11.407 25.777  1.00 6.04  ? 102 GLU A O   1 
ATOM   780  C  CB  . GLU A 1 102 ? 15.980 13.730 26.425  1.00 6.06  ? 102 GLU A CB  1 
ATOM   781  C  CG  . GLU A 1 102 ? 16.267 13.936 24.950  1.00 6.06  ? 102 GLU A CG  1 
ATOM   782  C  CD  . GLU A 1 102 ? 15.512 15.021 24.199  1.00 6.03  ? 102 GLU A CD  1 
ATOM   783  O  OE1 . GLU A 1 102 ? 15.613 16.226 24.566  1.00 5.86  ? 102 GLU A OE1 1 
ATOM   784  O  OE2 . GLU A 1 102 ? 14.873 14.651 23.191  1.00 6.07  ? 102 GLU A OE2 1 
ATOM   785  N  N   . THR A 1 103 ? 16.384 10.671 26.578  1.00 5.88  ? 103 THR A N   1 
ATOM   786  C  CA  . THR A 1 103 ? 16.307 9.544  25.661  1.00 5.78  ? 103 THR A CA  1 
ATOM   787  C  C   . THR A 1 103 ? 15.742 10.027 24.323  1.00 5.62  ? 103 THR A C   1 
ATOM   788  O  O   . THR A 1 103 ? 14.842 10.865 24.285  1.00 5.44  ? 103 THR A O   1 
ATOM   789  C  CB  . THR A 1 103 ? 15.442 8.396  26.194  1.00 5.79  ? 103 THR A CB  1 
ATOM   790  O  OG1 . THR A 1 103 ? 14.225 9.010  26.612  1.00 5.88  ? 103 THR A OG1 1 
ATOM   791  C  CG2 . THR A 1 103 ? 16.083 7.604  27.312  1.00 5.77  ? 103 THR A CG2 1 
ATOM   792  N  N   . ASN A 1 104 ? 16.303 9.484  23.234  1.00 5.54  ? 104 ASN A N   1 
ATOM   793  C  CA  . ASN A 1 104 ? 15.862 9.766  21.881  1.00 5.43  ? 104 ASN A CA  1 
ATOM   794  C  C   . ASN A 1 104 ? 15.607 8.426  21.210  1.00 5.22  ? 104 ASN A C   1 
ATOM   795  O  O   . ASN A 1 104 ? 16.520 7.790  20.680  1.00 5.25  ? 104 ASN A O   1 
ATOM   796  C  CB  . ASN A 1 104 ? 16.883 10.591 21.098  1.00 5.56  ? 104 ASN A CB  1 
ATOM   797  C  CG  . ASN A 1 104 ? 17.285 11.872 21.799  1.00 5.67  ? 104 ASN A CG  1 
ATOM   798  O  OD1 . ASN A 1 104 ? 18.369 11.931 22.375  1.00 5.89  ? 104 ASN A OD1 1 
ATOM   799  N  ND2 . ASN A 1 104 ? 16.438 12.896 21.754  1.00 5.68  ? 104 ASN A ND2 1 
ATOM   800  N  N   . THR A 1 105 ? 14.347 8.005  21.272  1.00 4.95  ? 105 THR A N   1 
ATOM   801  C  CA  . THR A 1 105 ? 14.028 6.610  21.078  1.00 4.73  ? 105 THR A CA  1 
ATOM   802  C  C   . THR A 1 105 ? 12.963 6.461  19.999  1.00 4.44  ? 105 THR A C   1 
ATOM   803  O  O   . THR A 1 105 ? 11.826 6.881  20.147  1.00 4.38  ? 105 THR A O   1 
ATOM   804  C  CB  . THR A 1 105 ? 13.628 6.001  22.419  1.00 4.77  ? 105 THR A CB  1 
ATOM   805  O  OG1 . THR A 1 105 ? 14.699 6.265  23.321  1.00 4.81  ? 105 THR A OG1 1 
ATOM   806  C  CG2 . THR A 1 105 ? 13.397 4.514  22.324  1.00 4.80  ? 105 THR A CG2 1 
ATOM   807  N  N   . ILE A 1 106 ? 13.351 5.826  18.905  1.00 4.14  ? 106 ILE A N   1 
ATOM   808  C  CA  . ILE A 1 106 ? 12.428 5.561  17.829  1.00 3.91  ? 106 ILE A CA  1 
ATOM   809  C  C   . ILE A 1 106 ? 11.833 4.172  18.037  1.00 3.63  ? 106 ILE A C   1 
ATOM   810  O  O   . ILE A 1 106 ? 12.532 3.161  18.019  1.00 3.58  ? 106 ILE A O   1 
ATOM   811  C  CB  . ILE A 1 106 ? 13.189 5.723  16.505  1.00 3.97  ? 106 ILE A CB  1 
ATOM   812  C  CG1 . ILE A 1 106 ? 13.872 7.091  16.453  1.00 4.04  ? 106 ILE A CG1 1 
ATOM   813  C  CG2 . ILE A 1 106 ? 12.288 5.481  15.311  1.00 3.96  ? 106 ILE A CG2 1 
ATOM   814  C  CD1 . ILE A 1 106 ? 12.974 8.257  16.851  1.00 4.04  ? 106 ILE A CD1 1 
ATOM   815  N  N   . LEU A 1 107 ? 10.518 4.143  18.258  1.00 3.38  ? 107 LEU A N   1 
ATOM   816  C  CA  . LEU A 1 107 ? 9.776  2.896  18.345  1.00 3.17  ? 107 LEU A CA  1 
ATOM   817  C  C   . LEU A 1 107 ? 9.342  2.432  16.950  1.00 2.99  ? 107 LEU A C   1 
ATOM   818  O  O   . LEU A 1 107 ? 9.140  1.238  16.743  1.00 2.97  ? 107 LEU A O   1 
ATOM   819  C  CB  . LEU A 1 107 ? 8.573  3.084  19.279  1.00 3.12  ? 107 LEU A CB  1 
ATOM   820  C  CG  . LEU A 1 107 ? 8.895  3.115  20.768  1.00 3.09  ? 107 LEU A CG  1 
ATOM   821  C  CD1 . LEU A 1 107 ? 9.444  4.469  21.167  1.00 3.11  ? 107 LEU A CD1 1 
ATOM   822  C  CD2 . LEU A 1 107 ? 7.674  2.786  21.597  1.00 3.08  ? 107 LEU A CD2 1 
ATOM   823  N  N   . SER A 1 108 ? 9.183  3.363  16.001  1.00 2.80  ? 108 SER A N   1 
ATOM   824  C  CA  . SER A 1 108 ? 8.799  3.001  14.646  1.00 2.69  ? 108 SER A CA  1 
ATOM   825  C  C   . SER A 1 108 ? 9.218  4.115  13.697  1.00 2.61  ? 108 SER A C   1 
ATOM   826  O  O   . SER A 1 108 ? 9.404  5.234  14.149  1.00 2.63  ? 108 SER A O   1 
ATOM   827  C  CB  . SER A 1 108 ? 7.318  2.701  14.532  1.00 2.66  ? 108 SER A CB  1 
ATOM   828  O  OG  . SER A 1 108 ? 6.553  3.889  14.518  1.00 2.63  ? 108 SER A OG  1 
ATOM   829  N  N   . TRP A 1 109 ? 9.376  3.790  12.403  1.00 2.51  ? 109 TRP A N   1 
ATOM   830  C  CA  . TRP A 1 109 ? 9.743  4.749  11.367  1.00 2.43  ? 109 TRP A CA  1 
ATOM   831  C  C   . TRP A 1 109 ? 9.223  4.255  10.017  1.00 2.43  ? 109 TRP A C   1 
ATOM   832  O  O   . TRP A 1 109 ? 9.487  3.119  9.661   1.00 2.42  ? 109 TRP A O   1 
ATOM   833  C  CB  . TRP A 1 109 ? 11.263 4.939  11.358  1.00 2.37  ? 109 TRP A CB  1 
ATOM   834  C  CG  . TRP A 1 109 ? 11.768 5.905  10.332  1.00 2.32  ? 109 TRP A CG  1 
ATOM   835  C  CD1 . TRP A 1 109 ? 11.070 6.908  9.728   1.00 2.30  ? 109 TRP A CD1 1 
ATOM   836  C  CD2 . TRP A 1 109 ? 13.084 5.925  9.754   1.00 2.28  ? 109 TRP A CD2 1 
ATOM   837  N  NE1 . TRP A 1 109 ? 11.868 7.564  8.834   1.00 2.29  ? 109 TRP A NE1 1 
ATOM   838  C  CE2 . TRP A 1 109 ? 13.112 6.987  8.833   1.00 2.28  ? 109 TRP A CE2 1 
ATOM   839  C  CE3 . TRP A 1 109 ? 14.243 5.171  9.936   1.00 2.26  ? 109 TRP A CE3 1 
ATOM   840  C  CZ2 . TRP A 1 109 ? 14.253 7.296  8.093   1.00 2.27  ? 109 TRP A CZ2 1 
ATOM   841  C  CZ3 . TRP A 1 109 ? 15.373 5.484  9.216   1.00 2.26  ? 109 TRP A CZ3 1 
ATOM   842  C  CH2 . TRP A 1 109 ? 15.376 6.530  8.303   1.00 2.26  ? 109 TRP A CH2 1 
ATOM   843  N  N   . SER A 1 110 ? 8.486  5.076  9.256   1.00 2.45  ? 110 SER A N   1 
ATOM   844  C  CA  . SER A 1 110 ? 7.835  4.558  8.059   1.00 2.49  ? 110 SER A CA  1 
ATOM   845  C  C   . SER A 1 110 ? 7.755  5.593  6.939   1.00 2.50  ? 110 SER A C   1 
ATOM   846  O  O   . SER A 1 110 ? 6.782  6.328  6.842   1.00 2.50  ? 110 SER A O   1 
ATOM   847  C  CB  . SER A 1 110 ? 6.472  3.967  8.375   1.00 2.50  ? 110 SER A CB  1 
ATOM   848  O  OG  . SER A 1 110 ? 5.495  4.970  8.583   1.00 2.52  ? 110 SER A OG  1 
ATOM   849  N  N   . PHE A 1 111 ? 8.757  5.537  6.047   1.00 2.55  ? 111 PHE A N   1 
ATOM   850  C  CA  . PHE A 1 111 ? 8.878  6.366  4.858   1.00 2.56  ? 111 PHE A CA  1 
ATOM   851  C  C   . PHE A 1 111 ? 8.076  5.818  3.687   1.00 2.66  ? 111 PHE A C   1 
ATOM   852  O  O   . PHE A 1 111 ? 7.885  4.616  3.545   1.00 2.63  ? 111 PHE A O   1 
ATOM   853  C  CB  . PHE A 1 111 ? 10.332 6.399  4.401   1.00 2.50  ? 111 PHE A CB  1 
ATOM   854  C  CG  . PHE A 1 111 ? 10.642 7.367  3.293   1.00 2.46  ? 111 PHE A CG  1 
ATOM   855  C  CD1 . PHE A 1 111 ? 10.454 8.724  3.465   1.00 2.44  ? 111 PHE A CD1 1 
ATOM   856  C  CD2 . PHE A 1 111 ? 11.184 6.923  2.098   1.00 2.46  ? 111 PHE A CD2 1 
ATOM   857  C  CE1 . PHE A 1 111 ? 10.788 9.612  2.459   1.00 2.45  ? 111 PHE A CE1 1 
ATOM   858  C  CE2 . PHE A 1 111 ? 11.499 7.808  1.082   1.00 2.47  ? 111 PHE A CE2 1 
ATOM   859  C  CZ  . PHE A 1 111 ? 11.301 9.151  1.268   1.00 2.47  ? 111 PHE A CZ  1 
ATOM   860  N  N   . THR A 1 112 ? 7.650  6.746  2.834   1.00 2.83  ? 112 THR A N   1 
ATOM   861  C  CA  . THR A 1 112 ? 7.088  6.450  1.528   1.00 3.02  ? 112 THR A CA  1 
ATOM   862  C  C   . THR A 1 112 ? 7.543  7.565  0.597   1.00 3.21  ? 112 THR A C   1 
ATOM   863  O  O   . THR A 1 112 ? 7.713  8.682  1.040   1.00 3.18  ? 112 THR A O   1 
ATOM   864  C  CB  . THR A 1 112 ? 5.552  6.305  1.561   1.00 3.01  ? 112 THR A CB  1 
ATOM   865  O  OG1 . THR A 1 112 ? 5.205  5.050  2.154   1.00 3.00  ? 112 THR A OG1 1 
ATOM   866  C  CG2 . THR A 1 112 ? 4.899  6.391  0.195   1.00 2.99  ? 112 THR A CG2 1 
ATOM   867  N  N   . SER A 1 113 ? 7.859  7.211  -0.650  1.00 3.57  ? 113 SER A N   1 
ATOM   868  C  CA  . SER A 1 113 ? 8.255  8.153  -1.730  1.00 3.86  ? 113 SER A CA  1 
ATOM   869  C  C   . SER A 1 113 ? 7.631  7.687  -3.053  1.00 4.21  ? 113 SER A C   1 
ATOM   870  O  O   . SER A 1 113 ? 7.584  6.484  -3.250  1.00 4.25  ? 113 SER A O   1 
ATOM   871  C  CB  . SER A 1 113 ? 9.729  8.198  -1.867  1.00 3.86  ? 113 SER A CB  1 
ATOM   872  O  OG  . SER A 1 113 ? 10.106 9.051  -2.927  1.00 3.95  ? 113 SER A OG  1 
ATOM   873  N  N   . LYS A 1 114 ? 7.150  8.596  -3.915  1.00 4.65  ? 114 LYS A N   1 
ATOM   874  C  CA  . LYS A 1 114 ? 6.595  8.243  -5.220  1.00 4.99  ? 114 LYS A CA  1 
ATOM   875  C  C   . LYS A 1 114 ? 7.058  9.250  -6.269  1.00 5.33  ? 114 LYS A C   1 
ATOM   876  O  O   . LYS A 1 114 ? 7.075  10.446 -6.000  1.00 5.37  ? 114 LYS A O   1 
ATOM   877  C  CB  . LYS A 1 114 ? 5.063  8.220  -5.190  1.00 5.09  ? 114 LYS A CB  1 
ATOM   878  C  CG  . LYS A 1 114 ? 4.466  6.983  -4.546  1.00 5.26  ? 114 LYS A CG  1 
ATOM   879  C  CD  . LYS A 1 114 ? 3.087  7.177  -3.979  1.00 5.48  ? 114 LYS A CD  1 
ATOM   880  C  CE  . LYS A 1 114 ? 2.458  5.875  -3.506  1.00 5.66  ? 114 LYS A CE  1 
ATOM   881  N  NZ  . LYS A 1 114 ? 1.437  6.107  -2.442  1.00 5.76  ? 114 LYS A NZ  1 
ATOM   882  N  N   . LEU A 1 115 ? 7.432  8.756  -7.454  1.00 5.74  ? 115 LEU A N   1 
ATOM   883  C  CA  . LEU A 1 115 ? 7.564  9.572  -8.647  1.00 6.15  ? 115 LEU A CA  1 
ATOM   884  C  C   . LEU A 1 115 ? 6.552  9.078  -9.669  1.00 6.78  ? 115 LEU A C   1 
ATOM   885  O  O   . LEU A 1 115 ? 6.588  7.916  -10.030 1.00 6.99  ? 115 LEU A O   1 
ATOM   886  C  CB  . LEU A 1 115 ? 8.976  9.421  -9.215  1.00 6.11  ? 115 LEU A CB  1 
ATOM   887  C  CG  . LEU A 1 115 ? 10.107 9.897  -8.319  1.00 6.12  ? 115 LEU A CG  1 
ATOM   888  C  CD1 . LEU A 1 115 ? 11.445 9.748  -9.024  1.00 6.12  ? 115 LEU A CD1 1 
ATOM   889  C  CD2 . LEU A 1 115 ? 9.881  11.341 -7.894  1.00 6.19  ? 115 LEU A CD2 1 
ATOM   890  N  N   . LYS A 1 116 ? 5.673  9.949  -10.155 1.00 7.67  ? 116 LYS A N   1 
ATOM   891  C  CA  . LYS A 1 116 ? 4.690  9.556  -11.148 1.00 8.67  ? 116 LYS A CA  1 
ATOM   892  C  C   . LYS A 1 116 ? 4.933  10.350 -12.428 1.00 10.28 ? 116 LYS A C   1 
ATOM   893  O  O   . LYS A 1 116 ? 5.072  11.565 -12.356 1.00 10.71 ? 116 LYS A O   1 
ATOM   894  C  CB  . LYS A 1 116 ? 3.291  9.800  -10.586 1.00 8.35  ? 116 LYS A CB  1 
ATOM   895  C  CG  . LYS A 1 116 ? 2.963  8.999  -9.337  1.00 8.17  ? 116 LYS A CG  1 
ATOM   896  C  CD  . LYS A 1 116 ? 1.710  9.493  -8.663  1.00 8.22  ? 116 LYS A CD  1 
ATOM   897  C  CE  . LYS A 1 116 ? 1.181  8.561  -7.596  1.00 8.26  ? 116 LYS A CE  1 
ATOM   898  N  NZ  . LYS A 1 116 ? 0.149  9.248  -6.787  1.00 8.31  ? 116 LYS A NZ  1 
ATOM   899  N  N   . SER A 1 117 ? 4.995  9.670  -13.584 1.00 12.21 ? 117 SER A N   1 
ATOM   900  C  CA  . SER A 1 117 ? 5.416  10.309 -14.823 1.00 14.45 ? 117 SER A CA  1 
ATOM   901  C  C   . SER A 1 117 ? 4.315  10.486 -15.867 1.00 17.23 ? 117 SER A C   1 
ATOM   902  O  O   . SER A 1 117 ? 3.194  10.046 -15.660 1.00 17.85 ? 117 SER A O   1 
ATOM   903  C  CB  . SER A 1 117 ? 6.586  9.594  -15.439 1.00 14.78 ? 117 SER A CB  1 
ATOM   904  O  OG  . SER A 1 117 ? 6.246  8.272  -15.816 1.00 15.24 ? 117 SER A OG  1 
ATOM   905  N  N   . ASN A 1 118 ? 4.647  11.175 -16.970 1.00 21.34 ? 118 ASN A N   1 
ATOM   906  C  CA  . ASN A 1 118 ? 3.673  11.584 -17.975 1.00 24.99 ? 118 ASN A CA  1 
ATOM   907  C  C   . ASN A 1 118 ? 3.035  10.332 -18.585 1.00 28.00 ? 118 ASN A C   1 
ATOM   908  O  O   . ASN A 1 118 ? 1.876  10.351 -19.011 1.00 29.87 ? 118 ASN A O   1 
ATOM   909  C  CB  . ASN A 1 118 ? 4.218  12.557 -19.041 1.00 27.11 ? 118 ASN A CB  1 
ATOM   910  C  CG  . ASN A 1 118 ? 5.302  12.030 -19.974 1.00 28.30 ? 118 ASN A CG  1 
ATOM   911  O  OD1 . ASN A 1 118 ? 5.289  10.851 -20.321 1.00 29.67 ? 118 ASN A OD1 1 
ATOM   912  N  ND2 . ASN A 1 118 ? 6.273  12.850 -20.356 1.00 28.24 ? 118 ASN A ND2 1 
ATOM   913  N  N   . SER A 1 119 ? 3.847  9.265  -18.573 1.00 30.77 ? 119 SER A N   1 
ATOM   914  C  CA  . SER A 1 119 ? 3.497  7.972  -19.134 1.00 34.29 ? 119 SER A CA  1 
ATOM   915  C  C   . SER A 1 119 ? 2.266  7.315  -18.519 1.00 38.84 ? 119 SER A C   1 
ATOM   916  O  O   . SER A 1 119 ? 1.764  7.769  -17.490 1.00 38.67 ? 119 SER A O   1 
ATOM   917  C  CB  . SER A 1 119 ? 4.704  7.070  -19.021 1.00 32.90 ? 119 SER A CB  1 
ATOM   918  O  OG  . SER A 1 119 ? 5.903  7.828  -19.022 1.00 32.10 ? 119 SER A OG  1 
ATOM   919  N  N   . THR A 1 120 ? 1.797  6.241  -19.166 1.00 43.03 ? 120 THR A N   1 
ATOM   920  C  CA  . THR A 1 120 ? 0.673  5.470  -18.663 1.00 45.68 ? 120 THR A CA  1 
ATOM   921  C  C   . THR A 1 120 ? 1.212  4.525  -17.579 1.00 45.17 ? 120 THR A C   1 
ATOM   922  O  O   . THR A 1 120 ? 2.283  3.942  -17.747 1.00 43.03 ? 120 THR A O   1 
ATOM   923  C  CB  . THR A 1 120 ? -0.094 4.872  -19.858 1.00 45.93 ? 120 THR A CB  1 
ATOM   924  O  OG1 . THR A 1 120 ? -1.458 4.676  -19.472 1.00 43.42 ? 120 THR A OG1 1 
ATOM   925  C  CG2 . THR A 1 120 ? 0.519  3.593  -20.395 1.00 44.99 ? 120 THR A CG2 1 
ATOM   926  N  N   . HIS A 1 121 ? 0.501  4.462  -16.437 1.00 47.22 ? 121 HIS A N   1 
ATOM   927  C  CA  . HIS A 1 121 ? 0.780  3.552  -15.329 1.00 48.70 ? 121 HIS A CA  1 
ATOM   928  C  C   . HIS A 1 121 ? 2.257  3.581  -14.940 1.00 41.29 ? 121 HIS A C   1 
ATOM   929  O  O   . HIS A 1 121 ? 2.935  2.548  -14.971 1.00 41.36 ? 121 HIS A O   1 
ATOM   930  C  CB  . HIS A 1 121 ? 0.352  2.117  -15.677 1.00 57.11 ? 121 HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 121 ? -1.102 1.949  -15.976 1.00 64.20 ? 121 HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 121 ? -1.605 0.803  -16.557 1.00 68.32 ? 121 HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 121 ? -2.151 2.772  -15.798 1.00 64.85 ? 121 HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 121 ? -2.917 0.933  -16.706 1.00 70.50 ? 121 HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 121 ? -3.270 2.123  -16.250 1.00 67.61 ? 121 HIS A NE2 1 
ATOM   936  N  N   . GLU A 1 122 ? 2.762  4.759  -14.558 1.00 33.01 ? 122 GLU A N   1 
ATOM   937  C  CA  . GLU A 1 122 ? 4.200  4.874  -14.373 1.00 28.39 ? 122 GLU A CA  1 
ATOM   938  C  C   . GLU A 1 122 ? 4.528  5.598  -13.069 1.00 20.71 ? 122 GLU A C   1 
ATOM   939  O  O   . GLU A 1 122 ? 5.160  6.642  -13.048 1.00 20.45 ? 122 GLU A O   1 
ATOM   940  C  CB  . GLU A 1 122 ? 4.826  5.489  -15.624 1.00 30.04 ? 122 GLU A CB  1 
ATOM   941  C  CG  . GLU A 1 122 ? 6.285  5.101  -15.814 1.00 31.18 ? 122 GLU A CG  1 
ATOM   942  C  CD  . GLU A 1 122 ? 6.547  4.406  -17.140 1.00 32.57 ? 122 GLU A CD  1 
ATOM   943  O  OE1 . GLU A 1 122 ? 5.709  3.554  -17.530 1.00 32.64 ? 122 GLU A OE1 1 
ATOM   944  O  OE2 . GLU A 1 122 ? 7.593  4.695  -17.769 1.00 32.01 ? 122 GLU A OE2 1 
ATOM   945  N  N   . THR A 1 123 ? 4.145  4.966  -11.969 1.00 15.10 ? 123 THR A N   1 
ATOM   946  C  CA  . THR A 1 123 ? 4.638  5.328  -10.664 1.00 11.97 ? 123 THR A CA  1 
ATOM   947  C  C   . THR A 1 123 ? 5.998  4.666  -10.446 1.00 9.98  ? 123 THR A C   1 
ATOM   948  O  O   . THR A 1 123 ? 6.274  3.609  -10.994 1.00 9.61  ? 123 THR A O   1 
ATOM   949  C  CB  . THR A 1 123 ? 3.610  4.906  -9.615  1.00 11.54 ? 123 THR A CB  1 
ATOM   950  O  OG1 . THR A 1 123 ? 2.355  5.460  -9.995  1.00 11.18 ? 123 THR A OG1 1 
ATOM   951  C  CG2 . THR A 1 123 ? 3.972  5.371  -8.226  1.00 11.62 ? 123 THR A CG2 1 
ATOM   952  N  N   . ASN A 1 124 ? 6.852  5.323  -9.660  1.00 8.32  ? 124 ASN A N   1 
ATOM   953  C  CA  . ASN A 1 124 ? 8.030  4.715  -9.066  1.00 7.30  ? 124 ASN A CA  1 
ATOM   954  C  C   . ASN A 1 124 ? 7.988  4.975  -7.565  1.00 6.68  ? 124 ASN A C   1 
ATOM   955  O  O   . ASN A 1 124 ? 7.699  6.090  -7.152  1.00 6.75  ? 124 ASN A O   1 
ATOM   956  C  CB  . ASN A 1 124 ? 9.328  5.274  -9.639  1.00 7.03  ? 124 ASN A CB  1 
ATOM   957  C  CG  . ASN A 1 124 ? 9.609  4.754  -11.022 1.00 6.75  ? 124 ASN A CG  1 
ATOM   958  O  OD1 . ASN A 1 124 ? 8.775  4.874  -11.909 1.00 6.61  ? 124 ASN A OD1 1 
ATOM   959  N  ND2 . ASN A 1 124 ? 10.772 4.162  -11.200 1.00 6.64  ? 124 ASN A ND2 1 
ATOM   960  N  N   . ALA A 1 125 ? 8.289  3.956  -6.755  1.00 6.00  ? 125 ALA A N   1 
ATOM   961  C  CA  . ALA A 1 125 ? 7.982  4.002  -5.332  1.00 5.51  ? 125 ALA A CA  1 
ATOM   962  C  C   . ALA A 1 125 ? 9.084  3.353  -4.492  1.00 5.01  ? 125 ALA A C   1 
ATOM   963  O  O   . ALA A 1 125 ? 9.849  2.523  -4.963  1.00 5.05  ? 125 ALA A O   1 
ATOM   964  C  CB  . ALA A 1 125 ? 6.636  3.350  -5.075  1.00 5.50  ? 125 ALA A CB  1 
ATOM   965  N  N   . LEU A 1 126 ? 9.188  3.806  -3.248  1.00 4.52  ? 126 LEU A N   1 
ATOM   966  C  CA  . LEU A 1 126 ? 9.881  3.089  -2.204  1.00 4.20  ? 126 LEU A CA  1 
ATOM   967  C  C   . LEU A 1 126 ? 9.111  3.340  -0.918  1.00 3.96  ? 126 LEU A C   1 
ATOM   968  O  O   . LEU A 1 126 ? 8.871  4.489  -0.560  1.00 3.93  ? 126 LEU A O   1 
ATOM   969  C  CB  . LEU A 1 126 ? 11.317 3.594  -2.055  1.00 4.16  ? 126 LEU A CB  1 
ATOM   970  C  CG  . LEU A 1 126 ? 11.936 3.297  -0.692  1.00 4.12  ? 126 LEU A CG  1 
ATOM   971  C  CD1 . LEU A 1 126 ? 12.204 1.812  -0.550  1.00 4.12  ? 126 LEU A CD1 1 
ATOM   972  C  CD2 . LEU A 1 126 ? 13.200 4.093  -0.469  1.00 4.11  ? 126 LEU A CD2 1 
ATOM   973  N  N   . HIS A 1 127 ? 8.740  2.259  -0.239  1.00 3.69  ? 127 HIS A N   1 
ATOM   974  C  CA  . HIS A 1 127 ? 8.169  2.332  1.090   1.00 3.47  ? 127 HIS A CA  1 
ATOM   975  C  C   . HIS A 1 127 ? 9.185  1.659  1.998   1.00 3.40  ? 127 HIS A C   1 
ATOM   976  O  O   . HIS A 1 127 ? 9.918  0.815  1.522   1.00 3.41  ? 127 HIS A O   1 
ATOM   977  C  CB  . HIS A 1 127 ? 6.796  1.642  1.084   1.00 3.34  ? 127 HIS A CB  1 
ATOM   978  C  CG  . HIS A 1 127 ? 6.172  1.508  2.427   1.00 3.23  ? 127 HIS A CG  1 
ATOM   979  N  ND1 . HIS A 1 127 ? 5.666  2.570  3.139   1.00 3.16  ? 127 HIS A ND1 1 
ATOM   980  C  CD2 . HIS A 1 127 ? 5.979  0.429  3.188   1.00 3.18  ? 127 HIS A CD2 1 
ATOM   981  C  CE1 . HIS A 1 127 ? 5.179  2.130  4.288   1.00 3.15  ? 127 HIS A CE1 1 
ATOM   982  N  NE2 . HIS A 1 127 ? 5.367  0.833  4.343   1.00 3.15  ? 127 HIS A NE2 1 
ATOM   983  N  N   . PHE A 1 128 ? 9.262  2.044  3.270   1.00 3.36  ? 128 PHE A N   1 
ATOM   984  C  CA  . PHE A 1 128 ? 9.681  1.093  4.286   1.00 3.35  ? 128 PHE A CA  1 
ATOM   985  C  C   . PHE A 1 128 ? 8.921  1.387  5.571   1.00 3.38  ? 128 PHE A C   1 
ATOM   986  O  O   . PHE A 1 128 ? 8.507  2.508  5.806   1.00 3.27  ? 128 PHE A O   1 
ATOM   987  C  CB  . PHE A 1 128 ? 11.206 1.049  4.460   1.00 3.31  ? 128 PHE A CB  1 
ATOM   988  C  CG  . PHE A 1 128 ? 11.863 2.331  4.894   1.00 3.29  ? 128 PHE A CG  1 
ATOM   989  C  CD1 . PHE A 1 128 ? 11.834 2.736  6.218   1.00 3.28  ? 128 PHE A CD1 1 
ATOM   990  C  CD2 . PHE A 1 128 ? 12.500 3.147  3.972   1.00 3.30  ? 128 PHE A CD2 1 
ATOM   991  C  CE1 . PHE A 1 128 ? 12.432 3.926  6.610   1.00 3.27  ? 128 PHE A CE1 1 
ATOM   992  C  CE2 . PHE A 1 128 ? 13.113 4.329  4.369   1.00 3.29  ? 128 PHE A CE2 1 
ATOM   993  C  CZ  . PHE A 1 128 ? 13.080 4.714  5.687   1.00 3.28  ? 128 PHE A CZ  1 
ATOM   994  N  N   . MET A 1 129 ? 8.713  0.338  6.360   1.00 3.55  ? 129 MET A N   1 
ATOM   995  C  CA  . MET A 1 129 ? 8.127  0.445  7.682   1.00 3.74  ? 129 MET A CA  1 
ATOM   996  C  C   . MET A 1 129 ? 8.912  -0.436 8.659   1.00 3.81  ? 129 MET A C   1 
ATOM   997  O  O   . MET A 1 129 ? 9.066  -1.629 8.424   1.00 3.83  ? 129 MET A O   1 
ATOM   998  C  CB  . MET A 1 129 ? 6.673  -0.010 7.630   1.00 3.86  ? 129 MET A CB  1 
ATOM   999  C  CG  . MET A 1 129 ? 6.057  -0.188 8.985   1.00 4.01  ? 129 MET A CG  1 
ATOM   1000 S  SD  . MET A 1 129 ? 4.264  -0.174 8.795   1.00 4.30  ? 129 MET A SD  1 
ATOM   1001 C  CE  . MET A 1 129 ? 3.889  1.322  9.721   1.00 4.31  ? 129 MET A CE  1 
ATOM   1002 N  N   . PHE A 1 130 ? 9.453  0.171  9.724   1.00 3.85  ? 130 PHE A N   1 
ATOM   1003 C  CA  . PHE A 1 130 ? 10.088 -0.542 10.820  1.00 3.89  ? 130 PHE A CA  1 
ATOM   1004 C  C   . PHE A 1 130 ? 9.215  -0.375 12.063  1.00 4.04  ? 130 PHE A C   1 
ATOM   1005 O  O   . PHE A 1 130 ? 8.992  0.743  12.513  1.00 3.96  ? 130 PHE A O   1 
ATOM   1006 C  CB  . PHE A 1 130 ? 11.471 0.034  11.138  1.00 3.85  ? 130 PHE A CB  1 
ATOM   1007 C  CG  . PHE A 1 130 ? 12.492 0.040  10.028  1.00 3.84  ? 130 PHE A CG  1 
ATOM   1008 C  CD1 . PHE A 1 130 ? 13.144 -1.117 9.644   1.00 3.86  ? 130 PHE A CD1 1 
ATOM   1009 C  CD2 . PHE A 1 130 ? 12.864 1.217  9.410   1.00 3.82  ? 130 PHE A CD2 1 
ATOM   1010 C  CE1 . PHE A 1 130 ? 14.123 -1.096 8.662   1.00 3.86  ? 130 PHE A CE1 1 
ATOM   1011 C  CE2 . PHE A 1 130 ? 13.840 1.234  8.426   1.00 3.82  ? 130 PHE A CE2 1 
ATOM   1012 C  CZ  . PHE A 1 130 ? 14.468 0.079  8.051   1.00 3.83  ? 130 PHE A CZ  1 
ATOM   1013 N  N   . ASN A 1 131 ? 8.678  -1.477 12.598  1.00 4.28  ? 131 ASN A N   1 
ATOM   1014 C  CA  . ASN A 1 131 ? 8.025  -1.433 13.894  1.00 4.43  ? 131 ASN A CA  1 
ATOM   1015 C  C   . ASN A 1 131 ? 8.935  -2.092 14.915  1.00 4.61  ? 131 ASN A C   1 
ATOM   1016 O  O   . ASN A 1 131 ? 8.729  -1.916 16.108  1.00 4.64  ? 131 ASN A O   1 
ATOM   1017 C  CB  . ASN A 1 131 ? 6.617  -2.034 13.885  1.00 4.44  ? 131 ASN A CB  1 
ATOM   1018 C  CG  . ASN A 1 131 ? 5.608  -1.056 13.325  1.00 4.51  ? 131 ASN A CG  1 
ATOM   1019 O  OD1 . ASN A 1 131 ? 5.457  0.045  13.851  1.00 4.57  ? 131 ASN A OD1 1 
ATOM   1020 N  ND2 . ASN A 1 131 ? 4.960  -1.412 12.229  1.00 4.53  ? 131 ASN A ND2 1 
ATOM   1021 N  N   . GLN A 1 132 ? 9.975  -2.787 14.449  1.00 4.86  ? 132 GLN A N   1 
ATOM   1022 C  CA  . GLN A 1 132 ? 10.827 -3.514 15.367  1.00 5.14  ? 132 GLN A CA  1 
ATOM   1023 C  C   . GLN A 1 132 ? 12.260 -3.515 14.867  1.00 5.14  ? 132 GLN A C   1 
ATOM   1024 O  O   . GLN A 1 132 ? 12.554 -4.057 13.818  1.00 5.10  ? 132 GLN A O   1 
ATOM   1025 C  CB  . GLN A 1 132 ? 10.298 -4.936 15.526  1.00 5.39  ? 132 GLN A CB  1 
ATOM   1026 C  CG  . GLN A 1 132 ? 11.036 -5.745 16.584  1.00 5.62  ? 132 GLN A CG  1 
ATOM   1027 C  CD  . GLN A 1 132 ? 10.276 -7.015 16.866  1.00 5.85  ? 132 GLN A CD  1 
ATOM   1028 O  OE1 . GLN A 1 132 ? 10.726 -8.112 16.539  1.00 5.94  ? 132 GLN A OE1 1 
ATOM   1029 N  NE2 . GLN A 1 132 ? 9.085  -6.860 17.428  1.00 6.00  ? 132 GLN A NE2 1 
ATOM   1030 N  N   . PHE A 1 133 ? 13.153 -2.961 15.668  1.00 5.26  ? 133 PHE A N   1 
ATOM   1031 C  CA  . PHE A 1 133 ? 14.522 -2.835 15.237  1.00 5.53  ? 133 PHE A CA  1 
ATOM   1032 C  C   . PHE A 1 133 ? 15.327 -4.041 15.706  1.00 6.07  ? 133 PHE A C   1 
ATOM   1033 O  O   . PHE A 1 133 ? 15.241 -4.477 16.855  1.00 6.18  ? 133 PHE A O   1 
ATOM   1034 C  CB  . PHE A 1 133 ? 15.080 -1.498 15.709  1.00 5.40  ? 133 PHE A CB  1 
ATOM   1035 C  CG  . PHE A 1 133 ? 14.400 -0.300 15.087  1.00 5.26  ? 133 PHE A CG  1 
ATOM   1036 C  CD1 . PHE A 1 133 ? 13.225 0.208  15.618  1.00 5.19  ? 133 PHE A CD1 1 
ATOM   1037 C  CD2 . PHE A 1 133 ? 14.934 0.317  13.968  1.00 5.14  ? 133 PHE A CD2 1 
ATOM   1038 C  CE1 . PHE A 1 133 ? 12.615 1.322  15.071  1.00 5.08  ? 133 PHE A CE1 1 
ATOM   1039 C  CE2 . PHE A 1 133 ? 14.314 1.419  13.415  1.00 5.09  ? 133 PHE A CE2 1 
ATOM   1040 C  CZ  . PHE A 1 133 ? 13.157 1.915  13.966  1.00 5.08  ? 133 PHE A CZ  1 
ATOM   1041 N  N   . SER A 1 134 ? 16.113 -4.571 14.770  1.00 6.67  ? 134 SER A N   1 
ATOM   1042 C  CA  . SER A 1 134 ? 16.972 -5.714 15.014  1.00 7.25  ? 134 SER A CA  1 
ATOM   1043 C  C   . SER A 1 134 ? 18.263 -5.233 15.655  1.00 7.35  ? 134 SER A C   1 
ATOM   1044 O  O   . SER A 1 134 ? 18.512 -4.037 15.608  1.00 7.50  ? 134 SER A O   1 
ATOM   1045 C  CB  . SER A 1 134 ? 17.225 -6.440 13.710  1.00 7.69  ? 134 SER A CB  1 
ATOM   1046 O  OG  . SER A 1 134 ? 18.564 -6.926 13.632  1.00 8.16  ? 134 SER A OG  1 
ATOM   1047 N  N   . LYS A 1 135 ? 19.066 -6.151 16.225  1.00 7.57  ? 135 LYS A N   1 
ATOM   1048 C  CA  . LYS A 1 135 ? 20.450 -5.844 16.585  1.00 7.85  ? 135 LYS A CA  1 
ATOM   1049 C  C   . LYS A 1 135 ? 21.226 -5.526 15.312  1.00 7.63  ? 135 LYS A C   1 
ATOM   1050 O  O   . LYS A 1 135 ? 21.638 -4.393 15.109  1.00 8.01  ? 135 LYS A O   1 
ATOM   1051 C  CB  . LYS A 1 135 ? 21.174 -6.967 17.344  1.00 8.23  ? 135 LYS A CB  1 
ATOM   1052 C  CG  . LYS A 1 135 ? 21.323 -6.769 18.848  1.00 8.75  ? 135 LYS A CG  1 
ATOM   1053 C  CD  . LYS A 1 135 ? 20.010 -6.914 19.642  1.00 9.19  ? 135 LYS A CD  1 
ATOM   1054 C  CE  . LYS A 1 135 ? 20.139 -6.754 21.151  1.00 9.28  ? 135 LYS A CE  1 
ATOM   1055 N  NZ  . LYS A 1 135 ? 19.168 -7.626 21.860  1.00 9.20  ? 135 LYS A NZ  1 
ATOM   1056 N  N   . ASP A 1 136 ? 21.411 -6.518 14.447  1.00 7.27  ? 136 ASP A N   1 
ATOM   1057 C  CA  . ASP A 1 136 ? 22.147 -6.300 13.220  1.00 7.25  ? 136 ASP A CA  1 
ATOM   1058 C  C   . ASP A 1 136 ? 21.152 -5.966 12.110  1.00 7.10  ? 136 ASP A C   1 
ATOM   1059 O  O   . ASP A 1 136 ? 20.644 -6.866 11.441  1.00 7.38  ? 136 ASP A O   1 
ATOM   1060 C  CB  . ASP A 1 136 ? 22.997 -7.520 12.887  1.00 7.46  ? 136 ASP A CB  1 
ATOM   1061 C  CG  . ASP A 1 136 ? 23.758 -7.372 11.587  1.00 7.63  ? 136 ASP A CG  1 
ATOM   1062 O  OD1 . ASP A 1 136 ? 24.840 -6.748 11.624  1.00 8.04  ? 136 ASP A OD1 1 
ATOM   1063 O  OD2 . ASP A 1 136 ? 23.249 -7.860 10.551  1.00 7.39  ? 136 ASP A OD2 1 
ATOM   1064 N  N   . GLN A 1 137 ? 20.877 -4.663 11.949  1.00 6.68  ? 137 GLN A N   1 
ATOM   1065 C  CA  . GLN A 1 137 ? 19.878 -4.130 11.034  1.00 6.21  ? 137 GLN A CA  1 
ATOM   1066 C  C   . GLN A 1 137 ? 20.574 -3.669 9.752   1.00 5.85  ? 137 GLN A C   1 
ATOM   1067 O  O   . GLN A 1 137 ? 21.047 -2.535 9.652   1.00 5.84  ? 137 GLN A O   1 
ATOM   1068 C  CB  . GLN A 1 137 ? 19.166 -2.981 11.753  1.00 6.21  ? 137 GLN A CB  1 
ATOM   1069 C  CG  . GLN A 1 137 ? 18.045 -2.311 10.969  1.00 6.19  ? 137 GLN A CG  1 
ATOM   1070 C  CD  . GLN A 1 137 ? 16.780 -3.129 11.003  1.00 6.18  ? 137 GLN A CD  1 
ATOM   1071 O  OE1 . GLN A 1 137 ? 16.295 -3.512 12.068  1.00 6.13  ? 137 GLN A OE1 1 
ATOM   1072 N  NE2 . GLN A 1 137 ? 16.251 -3.425 9.826   1.00 6.17  ? 137 GLN A NE2 1 
ATOM   1073 N  N   . LYS A 1 138 ? 20.623 -4.549 8.753   1.00 5.46  ? 138 LYS A N   1 
ATOM   1074 C  CA  . LYS A 1 138 ? 21.453 -4.318 7.581   1.00 5.18  ? 138 LYS A CA  1 
ATOM   1075 C  C   . LYS A 1 138 ? 20.829 -3.347 6.576   1.00 4.76  ? 138 LYS A C   1 
ATOM   1076 O  O   . LYS A 1 138 ? 21.485 -3.009 5.594   1.00 4.73  ? 138 LYS A O   1 
ATOM   1077 C  CB  . LYS A 1 138 ? 21.728 -5.654 6.892   1.00 5.27  ? 138 LYS A CB  1 
ATOM   1078 C  CG  . LYS A 1 138 ? 22.480 -6.655 7.747   1.00 5.35  ? 138 LYS A CG  1 
ATOM   1079 C  CD  . LYS A 1 138 ? 22.899 -7.870 6.969   1.00 5.42  ? 138 LYS A CD  1 
ATOM   1080 C  CE  . LYS A 1 138 ? 23.448 -8.963 7.859   1.00 5.48  ? 138 LYS A CE  1 
ATOM   1081 N  NZ  . LYS A 1 138 ? 24.674 -8.516 8.566   1.00 5.49  ? 138 LYS A NZ  1 
ATOM   1082 N  N   . ASP A 1 139 ? 19.573 -2.928 6.781   1.00 4.37  ? 139 ASP A N   1 
ATOM   1083 C  CA  . ASP A 1 139 ? 18.932 -1.964 5.894   1.00 4.11  ? 139 ASP A CA  1 
ATOM   1084 C  C   . ASP A 1 139 ? 18.988 -0.552 6.487   1.00 3.89  ? 139 ASP A C   1 
ATOM   1085 O  O   . ASP A 1 139 ? 18.430 0.372  5.905   1.00 3.74  ? 139 ASP A O   1 
ATOM   1086 C  CB  . ASP A 1 139 ? 17.510 -2.402 5.534   1.00 4.10  ? 139 ASP A CB  1 
ATOM   1087 C  CG  . ASP A 1 139 ? 16.630 -2.810 6.703   1.00 4.12  ? 139 ASP A CG  1 
ATOM   1088 O  OD1 . ASP A 1 139 ? 17.046 -2.668 7.857   1.00 4.16  ? 139 ASP A OD1 1 
ATOM   1089 O  OD2 . ASP A 1 139 ? 15.541 -3.298 6.450   1.00 4.13  ? 139 ASP A OD2 1 
ATOM   1090 N  N   . LEU A 1 140 ? 19.698 -0.396 7.623   1.00 3.78  ? 140 LEU A N   1 
ATOM   1091 C  CA  . LEU A 1 140 ? 19.955 0.896  8.252   1.00 3.67  ? 140 LEU A CA  1 
ATOM   1092 C  C   . LEU A 1 140 ? 21.461 1.139  8.381   1.00 3.58  ? 140 LEU A C   1 
ATOM   1093 O  O   . LEU A 1 140 ? 22.200 0.262  8.825   1.00 3.50  ? 140 LEU A O   1 
ATOM   1094 C  CB  . LEU A 1 140 ? 19.294 0.969  9.639   1.00 3.63  ? 140 LEU A CB  1 
ATOM   1095 C  CG  . LEU A 1 140 ? 17.774 1.154  9.675   1.00 3.63  ? 140 LEU A CG  1 
ATOM   1096 C  CD1 . LEU A 1 140 ? 17.336 1.626  11.049  1.00 3.64  ? 140 LEU A CD1 1 
ATOM   1097 C  CD2 . LEU A 1 140 ? 17.257 2.129  8.622   1.00 3.62  ? 140 LEU A CD2 1 
ATOM   1098 N  N   . ILE A 1 141 ? 21.878 2.358  8.004   1.00 3.54  ? 141 ILE A N   1 
ATOM   1099 C  CA  . ILE A 1 141 ? 23.221 2.864  8.244   1.00 3.56  ? 141 ILE A CA  1 
ATOM   1100 C  C   . ILE A 1 141 ? 23.225 3.652  9.552   1.00 3.59  ? 141 ILE A C   1 
ATOM   1101 O  O   . ILE A 1 141 ? 22.874 4.827  9.577   1.00 3.57  ? 141 ILE A O   1 
ATOM   1102 C  CB  . ILE A 1 141 ? 23.736 3.735  7.076   1.00 3.51  ? 141 ILE A CB  1 
ATOM   1103 C  CG1 . ILE A 1 141 ? 23.603 3.021  5.729   1.00 3.52  ? 141 ILE A CG1 1 
ATOM   1104 C  CG2 . ILE A 1 141 ? 25.169 4.172  7.336   1.00 3.48  ? 141 ILE A CG2 1 
ATOM   1105 C  CD1 . ILE A 1 141 ? 23.818 3.907  4.512   1.00 3.51  ? 141 ILE A CD1 1 
ATOM   1106 N  N   . LEU A 1 142 ? 23.653 2.988  10.630  1.00 3.64  ? 142 LEU A N   1 
ATOM   1107 C  CA  . LEU A 1 142 ? 23.759 3.616  11.936  1.00 3.65  ? 142 LEU A CA  1 
ATOM   1108 C  C   . LEU A 1 142 ? 25.041 4.436  11.979  1.00 3.67  ? 142 LEU A C   1 
ATOM   1109 O  O   . LEU A 1 142 ? 26.060 3.995  11.458  1.00 3.68  ? 142 LEU A O   1 
ATOM   1110 C  CB  . LEU A 1 142 ? 23.739 2.523  13.013  1.00 3.66  ? 142 LEU A CB  1 
ATOM   1111 C  CG  . LEU A 1 142 ? 22.417 1.756  13.150  1.00 3.69  ? 142 LEU A CG  1 
ATOM   1112 C  CD1 . LEU A 1 142 ? 22.386 0.906  14.407  1.00 3.71  ? 142 LEU A CD1 1 
ATOM   1113 C  CD2 . LEU A 1 142 ? 21.219 2.696  13.154  1.00 3.71  ? 142 LEU A CD2 1 
ATOM   1114 N  N   . GLN A 1 143 ? 24.963 5.630  12.581  1.00 3.70  ? 143 GLN A N   1 
ATOM   1115 C  CA  . GLN A 1 143 ? 26.098 6.534  12.649  1.00 3.76  ? 143 GLN A CA  1 
ATOM   1116 C  C   . GLN A 1 143 ? 26.228 7.151  14.035  1.00 3.95  ? 143 GLN A C   1 
ATOM   1117 O  O   . GLN A 1 143 ? 25.228 7.391  14.718  1.00 3.90  ? 143 GLN A O   1 
ATOM   1118 C  CB  . GLN A 1 143 ? 25.958 7.688  11.666  1.00 3.69  ? 143 GLN A CB  1 
ATOM   1119 C  CG  . GLN A 1 143 ? 25.837 7.243  10.222  1.00 3.61  ? 143 GLN A CG  1 
ATOM   1120 C  CD  . GLN A 1 143 ? 25.676 8.461  9.359   1.00 3.53  ? 143 GLN A CD  1 
ATOM   1121 O  OE1 . GLN A 1 143 ? 24.923 9.374  9.686   1.00 3.50  ? 143 GLN A OE1 1 
ATOM   1122 N  NE2 . GLN A 1 143 ? 26.404 8.496  8.262   1.00 3.51  ? 143 GLN A NE2 1 
ATOM   1123 N  N   . GLY A 1 144 ? 27.493 7.424  14.397  1.00 4.20  ? 144 GLY A N   1 
ATOM   1124 C  CA  . GLY A 1 144 ? 27.840 7.956  15.701  1.00 4.39  ? 144 GLY A CA  1 
ATOM   1125 C  C   . GLY A 1 144 ? 27.490 6.980  16.822  1.00 4.59  ? 144 GLY A C   1 
ATOM   1126 O  O   . GLY A 1 144 ? 28.127 5.940  16.945  1.00 4.72  ? 144 GLY A O   1 
ATOM   1127 N  N   . ASP A 1 145 ? 26.473 7.327  17.626  1.00 4.79  ? 145 ASP A N   1 
ATOM   1128 C  CA  . ASP A 1 145 ? 26.165 6.636  18.871  1.00 4.94  ? 145 ASP A CA  1 
ATOM   1129 C  C   . ASP A 1 145 ? 24.860 5.851  18.746  1.00 5.28  ? 145 ASP A C   1 
ATOM   1130 O  O   . ASP A 1 145 ? 24.357 5.334  19.742  1.00 5.23  ? 145 ASP A O   1 
ATOM   1131 C  CB  . ASP A 1 145 ? 26.035 7.631  20.031  1.00 4.82  ? 145 ASP A CB  1 
ATOM   1132 C  CG  . ASP A 1 145 ? 27.340 8.168  20.595  1.00 4.71  ? 145 ASP A CG  1 
ATOM   1133 O  OD1 . ASP A 1 145 ? 28.421 7.932  19.987  1.00 4.60  ? 145 ASP A OD1 1 
ATOM   1134 O  OD2 . ASP A 1 145 ? 27.262 8.797  21.652  1.00 4.58  ? 145 ASP A OD2 1 
ATOM   1135 N  N   . ALA A 1 146 ? 24.300 5.794  17.530  1.00 5.74  ? 146 ALA A N   1 
ATOM   1136 C  CA  . ALA A 1 146 ? 22.994 5.197  17.323  1.00 6.13  ? 146 ALA A CA  1 
ATOM   1137 C  C   . ALA A 1 146 ? 23.140 3.687  17.412  1.00 6.60  ? 146 ALA A C   1 
ATOM   1138 O  O   . ALA A 1 146 ? 24.102 3.149  16.867  1.00 6.59  ? 146 ALA A O   1 
ATOM   1139 C  CB  . ALA A 1 146 ? 22.437 5.622  15.988  1.00 6.14  ? 146 ALA A CB  1 
ATOM   1140 N  N   . THR A 1 147 ? 22.215 3.027  18.131  1.00 7.31  ? 147 THR A N   1 
ATOM   1141 C  CA  . THR A 1 147 ? 22.196 1.569  18.213  1.00 7.83  ? 147 THR A CA  1 
ATOM   1142 C  C   . THR A 1 147 ? 20.767 1.066  18.080  1.00 8.84  ? 147 THR A C   1 
ATOM   1143 O  O   . THR A 1 147 ? 19.830 1.831  18.260  1.00 9.00  ? 147 THR A O   1 
ATOM   1144 C  CB  . THR A 1 147 ? 22.746 1.029  19.537  1.00 7.43  ? 147 THR A CB  1 
ATOM   1145 O  OG1 . THR A 1 147 ? 21.856 1.520  20.530  1.00 7.19  ? 147 THR A OG1 1 
ATOM   1146 C  CG2 . THR A 1 147 ? 24.173 1.433  19.830  1.00 7.28  ? 147 THR A CG2 1 
ATOM   1147 N  N   . THR A 1 148 ? 20.624 -0.235 17.818  1.00 10.39 ? 148 THR A N   1 
ATOM   1148 C  CA  . THR A 1 148 ? 19.322 -0.854 17.612  1.00 11.93 ? 148 THR A CA  1 
ATOM   1149 C  C   . THR A 1 148 ? 19.123 -2.034 18.575  1.00 13.31 ? 148 THR A C   1 
ATOM   1150 O  O   . THR A 1 148 ? 19.995 -2.346 19.383  1.00 13.47 ? 148 THR A O   1 
ATOM   1151 C  CB  . THR A 1 148 ? 19.143 -1.221 16.126  1.00 12.05 ? 148 THR A CB  1 
ATOM   1152 O  OG1 . THR A 1 148 ? 20.330 -1.814 15.594  1.00 12.27 ? 148 THR A OG1 1 
ATOM   1153 C  CG2 . THR A 1 148 ? 18.813 -0.026 15.258  1.00 11.91 ? 148 THR A CG2 1 
ATOM   1154 N  N   . GLY A 1 149 ? 17.926 -2.644 18.523  1.00 15.20 ? 149 GLY A N   1 
ATOM   1155 C  CA  . GLY A 1 149 ? 17.641 -3.913 19.185  1.00 16.68 ? 149 GLY A CA  1 
ATOM   1156 C  C   . GLY A 1 149 ? 17.361 -3.815 20.692  1.00 18.42 ? 149 GLY A C   1 
ATOM   1157 O  O   . GLY A 1 149 ? 17.044 -4.826 21.329  1.00 18.68 ? 149 GLY A O   1 
ATOM   1158 N  N   . THR A 1 150 ? 17.460 -2.604 21.270  1.00 19.24 ? 150 THR A N   1 
ATOM   1159 C  CA  . THR A 1 150 ? 17.376 -2.457 22.715  1.00 19.31 ? 150 THR A CA  1 
ATOM   1160 C  C   . THR A 1 150 ? 15.893 -2.311 23.045  1.00 18.77 ? 150 THR A C   1 
ATOM   1161 O  O   . THR A 1 150 ? 15.312 -1.252 22.840  1.00 20.01 ? 150 THR A O   1 
ATOM   1162 C  CB  . THR A 1 150 ? 18.273 -1.307 23.216  1.00 19.72 ? 150 THR A CB  1 
ATOM   1163 O  OG1 . THR A 1 150 ? 19.653 -1.557 22.902  1.00 20.11 ? 150 THR A OG1 1 
ATOM   1164 C  CG2 . THR A 1 150 ? 18.099 -1.062 24.701  1.00 18.85 ? 150 THR A CG2 1 
ATOM   1165 N  N   . ASP A 1 151 ? 15.276 -3.401 23.509  1.00 18.03 ? 151 ASP A N   1 
ATOM   1166 C  CA  . ASP A 1 151 ? 13.821 -3.530 23.547  1.00 17.53 ? 151 ASP A CA  1 
ATOM   1167 C  C   . ASP A 1 151 ? 13.272 -3.425 22.120  1.00 15.36 ? 151 ASP A C   1 
ATOM   1168 O  O   . ASP A 1 151 ? 12.146 -2.979 21.896  1.00 14.67 ? 151 ASP A O   1 
ATOM   1169 C  CB  . ASP A 1 151 ? 13.155 -2.540 24.514  1.00 18.54 ? 151 ASP A CB  1 
ATOM   1170 C  CG  . ASP A 1 151 ? 13.986 -2.151 25.732  1.00 19.97 ? 151 ASP A CG  1 
ATOM   1171 O  OD1 . ASP A 1 151 ? 14.686 -3.027 26.301  1.00 20.86 ? 151 ASP A OD1 1 
ATOM   1172 O  OD2 . ASP A 1 151 ? 13.902 -0.972 26.135  1.00 21.41 ? 151 ASP A OD2 1 
ATOM   1173 N  N   . GLY A 1 152 ? 14.095 -3.873 21.163  1.00 13.72 ? 152 GLY A N   1 
ATOM   1174 C  CA  . GLY A 1 152 ? 13.760 -3.873 19.749  1.00 12.55 ? 152 GLY A CA  1 
ATOM   1175 C  C   . GLY A 1 152 ? 13.598 -2.468 19.174  1.00 11.14 ? 152 GLY A C   1 
ATOM   1176 O  O   . GLY A 1 152 ? 12.840 -2.279 18.220  1.00 11.10 ? 152 GLY A O   1 
ATOM   1177 N  N   . ASN A 1 153 ? 14.346 -1.508 19.726  1.00 9.60  ? 153 ASN A N   1 
ATOM   1178 C  CA  . ASN A 1 153 ? 14.166 -0.115 19.382  1.00 8.66  ? 153 ASN A CA  1 
ATOM   1179 C  C   . ASN A 1 153 ? 15.446 0.473  18.807  1.00 8.30  ? 153 ASN A C   1 
ATOM   1180 O  O   . ASN A 1 153 ? 16.538 -0.054 19.022  1.00 8.34  ? 153 ASN A O   1 
ATOM   1181 C  CB  . ASN A 1 153 ? 13.769 0.700  20.605  1.00 8.29  ? 153 ASN A CB  1 
ATOM   1182 C  CG  . ASN A 1 153 ? 12.335 0.489  21.010  1.00 7.93  ? 153 ASN A CG  1 
ATOM   1183 O  OD1 . ASN A 1 153 ? 11.437 0.562  20.183  1.00 7.96  ? 153 ASN A OD1 1 
ATOM   1184 N  ND2 . ASN A 1 153 ? 12.107 0.254  22.282  1.00 7.77  ? 153 ASN A ND2 1 
ATOM   1185 N  N   . LEU A 1 154 ? 15.272 1.615  18.133  1.00 7.89  ? 154 LEU A N   1 
ATOM   1186 C  CA  . LEU A 1 154 ? 16.373 2.436  17.671  1.00 7.72  ? 154 LEU A CA  1 
ATOM   1187 C  C   . LEU A 1 154 ? 16.705 3.503  18.718  1.00 7.98  ? 154 LEU A C   1 
ATOM   1188 O  O   . LEU A 1 154 ? 15.853 4.322  19.079  1.00 7.91  ? 154 LEU A O   1 
ATOM   1189 C  CB  . LEU A 1 154 ? 15.996 3.066  16.329  1.00 7.41  ? 154 LEU A CB  1 
ATOM   1190 C  CG  . LEU A 1 154 ? 16.978 4.103  15.791  1.00 7.25  ? 154 LEU A CG  1 
ATOM   1191 C  CD1 . LEU A 1 154 ? 18.383 3.535  15.653  1.00 7.23  ? 154 LEU A CD1 1 
ATOM   1192 C  CD2 . LEU A 1 154 ? 16.504 4.626  14.454  1.00 7.21  ? 154 LEU A CD2 1 
ATOM   1193 N  N   . GLU A 1 155 ? 17.969 3.472  19.185  1.00 8.12  ? 155 GLU A N   1 
ATOM   1194 C  CA  . GLU A 1 155 ? 18.490 4.413  20.159  1.00 8.20  ? 155 GLU A CA  1 
ATOM   1195 C  C   . GLU A 1 155 ? 19.467 5.359  19.480  1.00 8.52  ? 155 GLU A C   1 
ATOM   1196 O  O   . GLU A 1 155 ? 20.656 5.050  19.348  1.00 8.22  ? 155 GLU A O   1 
ATOM   1197 C  CB  . GLU A 1 155 ? 19.207 3.716  21.312  1.00 8.08  ? 155 GLU A CB  1 
ATOM   1198 C  CG  . GLU A 1 155 ? 18.274 3.090  22.326  1.00 8.02  ? 155 GLU A CG  1 
ATOM   1199 C  CD  . GLU A 1 155 ? 17.387 4.035  23.116  1.00 8.05  ? 155 GLU A CD  1 
ATOM   1200 O  OE1 . GLU A 1 155 ? 17.317 5.263  22.786  1.00 8.01  ? 155 GLU A OE1 1 
ATOM   1201 O  OE2 . GLU A 1 155 ? 16.757 3.527  24.066  1.00 8.01  ? 155 GLU A OE2 1 
ATOM   1202 N  N   . LEU A 1 156 ? 18.923 6.530  19.123  1.00 9.01  ? 156 LEU A N   1 
ATOM   1203 C  CA  . LEU A 1 156 ? 19.660 7.552  18.416  1.00 9.39  ? 156 LEU A CA  1 
ATOM   1204 C  C   . LEU A 1 156 ? 20.762 8.054  19.333  1.00 10.56 ? 156 LEU A C   1 
ATOM   1205 O  O   . LEU A 1 156 ? 21.925 8.037  18.940  1.00 10.68 ? 156 LEU A O   1 
ATOM   1206 C  CB  . LEU A 1 156 ? 18.686 8.635  17.945  1.00 8.94  ? 156 LEU A CB  1 
ATOM   1207 C  CG  . LEU A 1 156 ? 17.752 8.184  16.814  1.00 8.80  ? 156 LEU A CG  1 
ATOM   1208 C  CD1 . LEU A 1 156 ? 16.599 9.150  16.602  1.00 8.73  ? 156 LEU A CD1 1 
ATOM   1209 C  CD2 . LEU A 1 156 ? 18.506 8.007  15.502  1.00 8.70  ? 156 LEU A CD2 1 
ATOM   1210 N  N   . THR A 1 157 ? 20.407 8.416  20.570  1.00 12.03 ? 157 THR A N   1 
ATOM   1211 C  CA  . THR A 1 157 ? 21.411 8.824  21.537  1.00 13.21 ? 157 THR A CA  1 
ATOM   1212 C  C   . THR A 1 157 ? 21.776 7.692  22.483  1.00 15.77 ? 157 THR A C   1 
ATOM   1213 O  O   . THR A 1 157 ? 21.049 6.704  22.581  1.00 15.87 ? 157 THR A O   1 
ATOM   1214 C  CB  . THR A 1 157 ? 20.963 10.008 22.392  1.00 12.66 ? 157 THR A CB  1 
ATOM   1215 O  OG1 . THR A 1 157 ? 19.742 9.676  23.062  1.00 12.23 ? 157 THR A OG1 1 
ATOM   1216 C  CG2 . THR A 1 157 ? 20.855 11.249 21.543  1.00 12.44 ? 157 THR A CG2 1 
ATOM   1217 N  N   . ARG A 1 158 ? 22.895 7.918  23.185  1.00 18.45 ? 158 ARG A N   1 
ATOM   1218 C  CA  . ARG A 1 158 ? 23.459 6.915  24.110  1.00 20.17 ? 158 ARG A CA  1 
ATOM   1219 C  C   . ARG A 1 158 ? 22.655 6.771  25.392  1.00 19.50 ? 158 ARG A C   1 
ATOM   1220 O  O   . ARG A 1 158 ? 22.215 7.770  25.927  1.00 18.71 ? 158 ARG A O   1 
ATOM   1221 C  CB  . ARG A 1 158 ? 24.927 7.250  24.379  1.00 23.01 ? 158 ARG A CB  1 
ATOM   1222 C  CG  . ARG A 1 158 ? 25.670 6.276  25.279  1.00 26.66 ? 158 ARG A CG  1 
ATOM   1223 C  CD  . ARG A 1 158 ? 25.612 4.873  24.718  1.00 29.36 ? 158 ARG A CD  1 
ATOM   1224 N  NE  . ARG A 1 158 ? 26.152 4.817  23.366  1.00 33.97 ? 158 ARG A NE  1 
ATOM   1225 C  CZ  . ARG A 1 158 ? 27.439 4.679  23.072  1.00 34.60 ? 158 ARG A CZ  1 
ATOM   1226 N  NH1 . ARG A 1 158 ? 27.803 3.993  22.005  1.00 34.44 ? 158 ARG A NH1 1 
ATOM   1227 N  NH2 . ARG A 1 158 ? 28.356 5.227  23.849  1.00 33.00 ? 158 ARG A NH2 1 
ATOM   1228 N  N   . VAL A 1 159 ? 22.528 5.535  25.840  1.00 20.84 ? 159 VAL A N   1 
ATOM   1229 C  CA  . VAL A 1 159 ? 21.798 5.153  27.046  1.00 22.01 ? 159 VAL A CA  1 
ATOM   1230 C  C   . VAL A 1 159 ? 22.661 4.165  27.835  1.00 23.94 ? 159 VAL A C   1 
ATOM   1231 O  O   . VAL A 1 159 ? 23.460 3.430  27.256  1.00 23.73 ? 159 VAL A O   1 
ATOM   1232 C  CB  . VAL A 1 159 ? 20.409 4.537  26.764  1.00 21.87 ? 159 VAL A CB  1 
ATOM   1233 C  CG1 . VAL A 1 159 ? 19.570 4.432  28.027  1.00 22.53 ? 159 VAL A CG1 1 
ATOM   1234 C  CG2 . VAL A 1 159 ? 19.625 5.293  25.701  1.00 21.66 ? 159 VAL A CG2 1 
ATOM   1235 N  N   . SER A 1 160 ? 22.524 4.136  29.165  1.00 26.69 ? 160 SER A N   1 
ATOM   1236 C  CA  . SER A 1 160 ? 23.247 3.140  29.941  1.00 29.18 ? 160 SER A CA  1 
ATOM   1237 C  C   . SER A 1 160 ? 22.311 1.969  30.232  1.00 30.26 ? 160 SER A C   1 
ATOM   1238 O  O   . SER A 1 160 ? 21.091 2.112  30.156  1.00 28.60 ? 160 SER A O   1 
ATOM   1239 C  CB  . SER A 1 160 ? 23.854 3.716  31.203  1.00 29.47 ? 160 SER A CB  1 
ATOM   1240 O  OG  . SER A 1 160 ? 22.888 3.807  32.239  1.00 30.18 ? 160 SER A OG  1 
ATOM   1241 N  N   . SER A 1 161 ? 22.898 0.824  30.549  1.00 31.95 ? 161 SER A N   1 
ATOM   1242 C  CA  . SER A 1 161 ? 22.118 -0.388 30.883  1.00 31.85 ? 161 SER A CA  1 
ATOM   1243 C  C   . SER A 1 161 ? 20.893 -0.048 31.713  1.00 31.01 ? 161 SER A C   1 
ATOM   1244 O  O   . SER A 1 161 ? 19.771 -0.365 31.291  1.00 28.85 ? 161 SER A O   1 
ATOM   1245 C  CB  . SER A 1 161 ? 22.996 -1.276 31.678  1.00 32.01 ? 161 SER A CB  1 
ATOM   1246 O  OG  . SER A 1 161 ? 24.029 -0.538 32.312  1.00 31.41 ? 161 SER A OG  1 
ATOM   1247 N  N   . ASN A 1 162 ? 21.123 0.551  32.868  1.00 30.44 ? 162 ASN A N   1 
ATOM   1248 C  CA  . ASN A 1 162 ? 20.040 0.833  33.804  1.00 28.92 ? 162 ASN A CA  1 
ATOM   1249 C  C   . ASN A 1 162 ? 18.869 1.479  33.049  1.00 26.60 ? 162 ASN A C   1 
ATOM   1250 O  O   . ASN A 1 162 ? 17.720 1.170  33.344  1.00 25.85 ? 162 ASN A O   1 
ATOM   1251 C  CB  . ASN A 1 162 ? 20.547 1.586  35.050  1.00 29.02 ? 162 ASN A CB  1 
ATOM   1252 C  CG  . ASN A 1 162 ? 20.610 3.102  34.936  1.00 29.65 ? 162 ASN A CG  1 
ATOM   1253 O  OD1 . ASN A 1 162 ? 19.609 3.789  35.119  1.00 29.72 ? 162 ASN A OD1 1 
ATOM   1254 N  ND2 . ASN A 1 162 ? 21.793 3.654  34.720  1.00 29.91 ? 162 ASN A ND2 1 
ATOM   1255 N  N   . GLY A 1 163 ? 19.156 2.345  32.061  1.00 25.35 ? 163 GLY A N   1 
ATOM   1256 C  CA  . GLY A 1 163 ? 18.158 2.812  31.096  1.00 23.38 ? 163 GLY A CA  1 
ATOM   1257 C  C   . GLY A 1 163 ? 17.983 4.337  31.026  1.00 20.91 ? 163 GLY A C   1 
ATOM   1258 O  O   . GLY A 1 163 ? 16.909 4.816  30.669  1.00 19.42 ? 163 GLY A O   1 
ATOM   1259 N  N   . SER A 1 164 ? 19.041 5.107  31.327  1.00 19.04 ? 164 SER A N   1 
ATOM   1260 C  CA  . SER A 1 164 ? 18.913 6.555  31.378  1.00 17.32 ? 164 SER A CA  1 
ATOM   1261 C  C   . SER A 1 164 ? 19.976 7.255  30.524  1.00 15.37 ? 164 SER A C   1 
ATOM   1262 O  O   . SER A 1 164 ? 21.113 6.806  30.353  1.00 14.35 ? 164 SER A O   1 
ATOM   1263 C  CB  . SER A 1 164 ? 18.928 7.059  32.796  1.00 17.47 ? 164 SER A CB  1 
ATOM   1264 O  OG  . SER A 1 164 ? 20.214 7.544  33.153  1.00 17.85 ? 164 SER A OG  1 
ATOM   1265 N  N   . PRO A 1 165 ? 19.623 8.445  30.004  1.00 13.40 ? 165 PRO A N   1 
ATOM   1266 C  CA  . PRO A 1 165 ? 20.351 9.037  28.885  1.00 12.59 ? 165 PRO A CA  1 
ATOM   1267 C  C   . PRO A 1 165 ? 21.657 9.744  29.232  1.00 11.75 ? 165 PRO A C   1 
ATOM   1268 O  O   . PRO A 1 165 ? 21.765 10.397 30.263  1.00 11.94 ? 165 PRO A O   1 
ATOM   1269 C  CB  . PRO A 1 165 ? 19.313 10.033 28.353  1.00 12.71 ? 165 PRO A CB  1 
ATOM   1270 C  CG  . PRO A 1 165 ? 18.542 10.475 29.581  1.00 12.90 ? 165 PRO A CG  1 
ATOM   1271 C  CD  . PRO A 1 165 ? 18.493 9.262  30.476  1.00 12.98 ? 165 PRO A CD  1 
ATOM   1272 N  N   . GLN A 1 166 ? 22.641 9.629  28.339  1.00 10.91 ? 166 GLN A N   1 
ATOM   1273 C  CA  . GLN A 1 166 ? 23.918 10.286 28.540  1.00 10.63 ? 166 GLN A CA  1 
ATOM   1274 C  C   . GLN A 1 166 ? 23.947 11.582 27.729  1.00 9.38  ? 166 GLN A C   1 
ATOM   1275 O  O   . GLN A 1 166 ? 23.417 11.641 26.629  1.00 9.31  ? 166 GLN A O   1 
ATOM   1276 C  CB  . GLN A 1 166 ? 25.063 9.334  28.179  1.00 11.54 ? 166 GLN A CB  1 
ATOM   1277 C  CG  . GLN A 1 166 ? 25.041 7.997  28.923  1.00 12.46 ? 166 GLN A CG  1 
ATOM   1278 C  CD  . GLN A 1 166 ? 24.774 8.124  30.410  1.00 13.67 ? 166 GLN A CD  1 
ATOM   1279 O  OE1 . GLN A 1 166 ? 25.565 8.705  31.164  1.00 14.51 ? 166 GLN A OE1 1 
ATOM   1280 N  NE2 . GLN A 1 166 ? 23.639 7.585  30.847  1.00 13.84 ? 166 GLN A NE2 1 
ATOM   1281 N  N   . GLY A 1 167 ? 24.565 12.626 28.288  1.00 8.21  ? 167 GLY A N   1 
ATOM   1282 C  CA  . GLY A 1 167 ? 24.756 13.882 27.587  1.00 7.40  ? 167 GLY A CA  1 
ATOM   1283 C  C   . GLY A 1 167 ? 25.878 13.795 26.556  1.00 6.63  ? 167 GLY A C   1 
ATOM   1284 O  O   . GLY A 1 167 ? 26.455 12.736 26.369  1.00 6.57  ? 167 GLY A O   1 
ATOM   1285 N  N   . SER A 1 168 ? 26.154 14.916 25.884  1.00 5.98  ? 168 SER A N   1 
ATOM   1286 C  CA  . SER A 1 168 ? 27.232 15.028 24.921  1.00 5.65  ? 168 SER A CA  1 
ATOM   1287 C  C   . SER A 1 168 ? 27.222 13.844 23.968  1.00 5.38  ? 168 SER A C   1 
ATOM   1288 O  O   . SER A 1 168 ? 28.274 13.246 23.770  1.00 5.51  ? 168 SER A O   1 
ATOM   1289 C  CB  . SER A 1 168 ? 28.553 15.115 25.611  1.00 5.61  ? 168 SER A CB  1 
ATOM   1290 O  OG  . SER A 1 168 ? 28.438 15.902 26.780  1.00 5.72  ? 168 SER A OG  1 
ATOM   1291 N  N   . SER A 1 169 ? 26.050 13.525 23.393  1.00 4.99  ? 169 SER A N   1 
ATOM   1292 C  CA  . SER A 1 169 ? 25.878 12.382 22.505  1.00 4.71  ? 169 SER A CA  1 
ATOM   1293 C  C   . SER A 1 169 ? 25.130 12.797 21.242  1.00 4.65  ? 169 SER A C   1 
ATOM   1294 O  O   . SER A 1 169 ? 24.203 13.608 21.305  1.00 4.71  ? 169 SER A O   1 
ATOM   1295 C  CB  . SER A 1 169 ? 25.129 11.273 23.175  1.00 4.61  ? 169 SER A CB  1 
ATOM   1296 O  OG  . SER A 1 169 ? 24.980 10.164 22.310  1.00 4.53  ? 169 SER A OG  1 
ATOM   1297 N  N   . VAL A 1 170 ? 25.521 12.196 20.104  1.00 4.43  ? 170 VAL A N   1 
ATOM   1298 C  CA  . VAL A 1 170 ? 24.839 12.396 18.836  1.00 4.15  ? 170 VAL A CA  1 
ATOM   1299 C  C   . VAL A 1 170 ? 24.872 11.084 18.057  1.00 3.92  ? 170 VAL A C   1 
ATOM   1300 O  O   . VAL A 1 170 ? 25.863 10.369 18.106  1.00 3.81  ? 170 VAL A O   1 
ATOM   1301 C  CB  . VAL A 1 170 ? 25.499 13.554 18.063  1.00 4.16  ? 170 VAL A CB  1 
ATOM   1302 C  CG1 . VAL A 1 170 ? 26.997 13.319 17.864  1.00 4.13  ? 170 VAL A CG1 1 
ATOM   1303 C  CG2 . VAL A 1 170 ? 24.782 13.852 16.744  1.00 4.15  ? 170 VAL A CG2 1 
ATOM   1304 N  N   . GLY A 1 171 ? 23.769 10.780 17.363  1.00 3.77  ? 171 GLY A N   1 
ATOM   1305 C  CA  . GLY A 1 171 ? 23.640 9.576  16.552  1.00 3.66  ? 171 GLY A CA  1 
ATOM   1306 C  C   . GLY A 1 171 ? 22.543 9.731  15.500  1.00 3.55  ? 171 GLY A C   1 
ATOM   1307 O  O   . GLY A 1 171 ? 21.623 10.525 15.687  1.00 3.57  ? 171 GLY A O   1 
ATOM   1308 N  N   . ARG A 1 172 ? 22.662 9.002  14.380  1.00 3.41  ? 172 ARG A N   1 
ATOM   1309 C  CA  . ARG A 1 172 ? 21.674 9.060  13.311  1.00 3.28  ? 172 ARG A CA  1 
ATOM   1310 C  C   . ARG A 1 172 ? 21.445 7.656  12.750  1.00 3.26  ? 172 ARG A C   1 
ATOM   1311 O  O   . ARG A 1 172 ? 22.265 6.761  12.953  1.00 3.26  ? 172 ARG A O   1 
ATOM   1312 C  CB  . ARG A 1 172 ? 22.138 10.025 12.216  1.00 3.22  ? 172 ARG A CB  1 
ATOM   1313 C  CG  . ARG A 1 172 ? 22.636 11.370 12.730  1.00 3.18  ? 172 ARG A CG  1 
ATOM   1314 C  CD  . ARG A 1 172 ? 22.975 12.403 11.663  1.00 3.17  ? 172 ARG A CD  1 
ATOM   1315 N  NE  . ARG A 1 172 ? 23.703 11.924 10.474  1.00 3.16  ? 172 ARG A NE  1 
ATOM   1316 C  CZ  . ARG A 1 172 ? 23.983 12.672 9.403   1.00 3.12  ? 172 ARG A CZ  1 
ATOM   1317 N  NH1 . ARG A 1 172 ? 23.817 13.980 9.441   1.00 3.13  ? 172 ARG A NH1 1 
ATOM   1318 N  NH2 . ARG A 1 172 ? 24.446 12.123 8.296   1.00 3.11  ? 172 ARG A NH2 1 
ATOM   1319 N  N   . ALA A 1 173 ? 20.308 7.454  12.069  1.00 3.23  ? 173 ALA A N   1 
ATOM   1320 C  CA  . ALA A 1 173 ? 20.037 6.209  11.361  1.00 3.20  ? 173 ALA A CA  1 
ATOM   1321 C  C   . ALA A 1 173 ? 19.496 6.554  9.981   1.00 3.22  ? 173 ALA A C   1 
ATOM   1322 O  O   . ALA A 1 173 ? 18.542 7.327  9.883   1.00 3.20  ? 173 ALA A O   1 
ATOM   1323 C  CB  . ALA A 1 173 ? 19.053 5.369  12.121  1.00 3.19  ? 173 ALA A CB  1 
ATOM   1324 N  N   . LEU A 1 174 ? 20.137 6.007  8.929   1.00 3.24  ? 174 LEU A N   1 
ATOM   1325 C  CA  . LEU A 1 174 ? 19.789 6.313  7.547   1.00 3.21  ? 174 LEU A CA  1 
ATOM   1326 C  C   . LEU A 1 174 ? 19.400 5.032  6.833   1.00 3.29  ? 174 LEU A C   1 
ATOM   1327 O  O   . LEU A 1 174 ? 20.064 4.016  6.977   1.00 3.26  ? 174 LEU A O   1 
ATOM   1328 C  CB  . LEU A 1 174 ? 20.964 6.979  6.834   1.00 3.12  ? 174 LEU A CB  1 
ATOM   1329 C  CG  . LEU A 1 174 ? 21.257 8.396  7.303   1.00 3.08  ? 174 LEU A CG  1 
ATOM   1330 C  CD1 . LEU A 1 174 ? 22.426 8.394  8.264   1.00 3.07  ? 174 LEU A CD1 1 
ATOM   1331 C  CD2 . LEU A 1 174 ? 21.510 9.327  6.128   1.00 3.07  ? 174 LEU A CD2 1 
ATOM   1332 N  N   . PHE A 1 175 ? 18.324 5.109  6.056   1.00 3.42  ? 175 PHE A N   1 
ATOM   1333 C  CA  . PHE A 1 175 ? 17.870 3.966  5.301   1.00 3.57  ? 175 PHE A CA  1 
ATOM   1334 C  C   . PHE A 1 175 ? 18.877 3.671  4.194   1.00 3.82  ? 175 PHE A C   1 
ATOM   1335 O  O   . PHE A 1 175 ? 19.262 4.586  3.467   1.00 3.86  ? 175 PHE A O   1 
ATOM   1336 C  CB  . PHE A 1 175 ? 16.481 4.237  4.743   1.00 3.52  ? 175 PHE A CB  1 
ATOM   1337 C  CG  . PHE A 1 175 ? 15.933 3.016  4.076   1.00 3.51  ? 175 PHE A CG  1 
ATOM   1338 C  CD1 . PHE A 1 175 ? 15.628 1.895  4.830   1.00 3.51  ? 175 PHE A CD1 1 
ATOM   1339 C  CD2 . PHE A 1 175 ? 15.818 2.954  2.699   1.00 3.50  ? 175 PHE A CD2 1 
ATOM   1340 C  CE1 . PHE A 1 175 ? 15.157 0.745  4.221   1.00 3.51  ? 175 PHE A CE1 1 
ATOM   1341 C  CE2 . PHE A 1 175 ? 15.342 1.808  2.088   1.00 3.50  ? 175 PHE A CE2 1 
ATOM   1342 C  CZ  . PHE A 1 175 ? 15.016 0.706  2.849   1.00 3.52  ? 175 PHE A CZ  1 
ATOM   1343 N  N   . TYR A 1 176 ? 19.268 2.392  4.056   1.00 4.10  ? 176 TYR A N   1 
ATOM   1344 C  CA  . TYR A 1 176 ? 20.466 2.008  3.305   1.00 4.38  ? 176 TYR A CA  1 
ATOM   1345 C  C   . TYR A 1 176 ? 20.365 2.419  1.839   1.00 4.35  ? 176 TYR A C   1 
ATOM   1346 O  O   . TYR A 1 176 ? 21.370 2.755  1.224   1.00 4.26  ? 176 TYR A O   1 
ATOM   1347 C  CB  . TYR A 1 176 ? 20.746 0.494  3.385   1.00 4.63  ? 176 TYR A CB  1 
ATOM   1348 C  CG  . TYR A 1 176 ? 22.105 0.054  2.875   1.00 4.88  ? 176 TYR A CG  1 
ATOM   1349 C  CD1 . TYR A 1 176 ? 23.281 0.408  3.531   1.00 5.02  ? 176 TYR A CD1 1 
ATOM   1350 C  CD2 . TYR A 1 176 ? 22.235 -0.696 1.712   1.00 5.03  ? 176 TYR A CD2 1 
ATOM   1351 C  CE1 . TYR A 1 176 ? 24.534 0.023  3.059   1.00 5.09  ? 176 TYR A CE1 1 
ATOM   1352 C  CE2 . TYR A 1 176 ? 23.479 -1.085 1.222   1.00 5.06  ? 176 TYR A CE2 1 
ATOM   1353 C  CZ  . TYR A 1 176 ? 24.634 -0.735 1.901   1.00 5.09  ? 176 TYR A CZ  1 
ATOM   1354 O  OH  . TYR A 1 176 ? 25.854 -1.125 1.401   1.00 5.12  ? 176 TYR A OH  1 
ATOM   1355 N  N   . ALA A 1 177 ? 19.149 2.352  1.291   1.00 4.45  ? 177 ALA A N   1 
ATOM   1356 C  CA  . ALA A 1 177 ? 18.912 2.583  -0.122  1.00 4.55  ? 177 ALA A CA  1 
ATOM   1357 C  C   . ALA A 1 177 ? 18.607 4.053  -0.370  1.00 4.67  ? 177 ALA A C   1 
ATOM   1358 O  O   . ALA A 1 177 ? 17.764 4.665  0.299   1.00 4.72  ? 177 ALA A O   1 
ATOM   1359 C  CB  . ALA A 1 177 ? 17.766 1.734  -0.609  1.00 4.57  ? 177 ALA A CB  1 
ATOM   1360 N  N   . PRO A 1 178 ? 19.286 4.663  -1.361  1.00 4.77  ? 178 PRO A N   1 
ATOM   1361 C  CA  . PRO A 1 178 ? 18.858 5.965  -1.880  1.00 4.90  ? 178 PRO A CA  1 
ATOM   1362 C  C   . PRO A 1 178 ? 17.380 6.082  -2.304  1.00 5.07  ? 178 PRO A C   1 
ATOM   1363 O  O   . PRO A 1 178 ? 16.702 5.084  -2.590  1.00 5.05  ? 178 PRO A O   1 
ATOM   1364 C  CB  . PRO A 1 178 ? 19.837 6.157  -3.052  1.00 4.82  ? 178 PRO A CB  1 
ATOM   1365 C  CG  . PRO A 1 178 ? 21.083 5.410  -2.624  1.00 4.76  ? 178 PRO A CG  1 
ATOM   1366 C  CD  . PRO A 1 178 ? 20.546 4.179  -1.941  1.00 4.73  ? 178 PRO A CD  1 
ATOM   1367 N  N   . VAL A 1 179 ? 16.896 7.335  -2.332  1.00 5.24  ? 179 VAL A N   1 
ATOM   1368 C  CA  . VAL A 1 179 ? 15.526 7.665  -2.690  1.00 5.44  ? 179 VAL A CA  1 
ATOM   1369 C  C   . VAL A 1 179 ? 15.555 8.673  -3.828  1.00 5.73  ? 179 VAL A C   1 
ATOM   1370 O  O   . VAL A 1 179 ? 16.132 9.741  -3.696  1.00 5.66  ? 179 VAL A O   1 
ATOM   1371 C  CB  . VAL A 1 179 ? 14.752 8.262  -1.500  1.00 5.38  ? 179 VAL A CB  1 
ATOM   1372 C  CG1 . VAL A 1 179 ? 13.309 8.594  -1.862  1.00 5.30  ? 179 VAL A CG1 1 
ATOM   1373 C  CG2 . VAL A 1 179 ? 14.823 7.361  -0.277  1.00 5.37  ? 179 VAL A CG2 1 
ATOM   1374 N  N   . HIS A 1 180 ? 14.887 8.345  -4.929  1.00 6.20  ? 180 HIS A N   1 
ATOM   1375 C  CA  . HIS A 1 180 ? 14.802 9.262  -6.050  1.00 6.61  ? 180 HIS A CA  1 
ATOM   1376 C  C   . HIS A 1 180 ? 13.625 10.189 -5.741  1.00 7.36  ? 180 HIS A C   1 
ATOM   1377 O  O   . HIS A 1 180 ? 12.513 9.712  -5.499  1.00 7.26  ? 180 HIS A O   1 
ATOM   1378 C  CB  . HIS A 1 180 ? 14.709 8.445  -7.348  1.00 6.39  ? 180 HIS A CB  1 
ATOM   1379 C  CG  . HIS A 1 180 ? 15.315 9.063  -8.570  1.00 6.10  ? 180 HIS A CG  1 
ATOM   1380 N  ND1 . HIS A 1 180 ? 14.962 8.640  -9.832  1.00 5.90  ? 180 HIS A ND1 1 
ATOM   1381 C  CD2 . HIS A 1 180 ? 16.186 10.052 -8.748  1.00 6.01  ? 180 HIS A CD2 1 
ATOM   1382 C  CE1 . HIS A 1 180 ? 15.602 9.362  -10.736 1.00 5.93  ? 180 HIS A CE1 1 
ATOM   1383 N  NE2 . HIS A 1 180 ? 16.349 10.229 -10.101 1.00 5.97  ? 180 HIS A NE2 1 
ATOM   1384 N  N   . ILE A 1 181 ? 13.894 11.503 -5.664  1.00 8.28  ? 181 ILE A N   1 
ATOM   1385 C  CA  . ILE A 1 181 ? 12.862 12.478 -5.315  1.00 9.03  ? 181 ILE A CA  1 
ATOM   1386 C  C   . ILE A 1 181 ? 12.439 13.247 -6.566  1.00 10.10 ? 181 ILE A C   1 
ATOM   1387 O  O   . ILE A 1 181 ? 11.353 13.846 -6.591  1.00 10.32 ? 181 ILE A O   1 
ATOM   1388 C  CB  . ILE A 1 181 ? 13.297 13.422 -4.172  1.00 8.90  ? 181 ILE A CB  1 
ATOM   1389 C  CG1 . ILE A 1 181 ? 14.776 13.793 -4.278  1.00 9.09  ? 181 ILE A CG1 1 
ATOM   1390 C  CG2 . ILE A 1 181 ? 12.965 12.838 -2.801  1.00 8.69  ? 181 ILE A CG2 1 
ATOM   1391 C  CD1 . ILE A 1 181 ? 15.173 14.933 -3.374  1.00 9.21  ? 181 ILE A CD1 1 
ATOM   1392 N  N   . TRP A 1 182 ? 13.263 13.148 -7.621  1.00 11.23 ? 182 TRP A N   1 
ATOM   1393 C  CA  . TRP A 1 182 ? 13.013 13.846 -8.872  1.00 12.23 ? 182 TRP A CA  1 
ATOM   1394 C  C   . TRP A 1 182 ? 13.432 12.913 -10.015 1.00 13.08 ? 182 TRP A C   1 
ATOM   1395 O  O   . TRP A 1 182 ? 14.333 12.085 -9.872  1.00 12.86 ? 182 TRP A O   1 
ATOM   1396 C  CB  . TRP A 1 182 ? 13.846 15.132 -8.920  1.00 12.38 ? 182 TRP A CB  1 
ATOM   1397 C  CG  . TRP A 1 182 ? 13.639 15.868 -10.198 1.00 12.48 ? 182 TRP A CG  1 
ATOM   1398 C  CD1 . TRP A 1 182 ? 12.581 16.664 -10.522 1.00 12.94 ? 182 TRP A CD1 1 
ATOM   1399 C  CD2 . TRP A 1 182 ? 14.452 15.764 -11.375 1.00 12.42 ? 182 TRP A CD2 1 
ATOM   1400 N  NE1 . TRP A 1 182 ? 12.717 17.121 -11.804 1.00 13.02 ? 182 TRP A NE1 1 
ATOM   1401 C  CE2 . TRP A 1 182 ? 13.852 16.578 -12.355 1.00 12.80 ? 182 TRP A CE2 1 
ATOM   1402 C  CE3 . TRP A 1 182 ? 15.646 15.105 -11.682 1.00 12.25 ? 182 TRP A CE3 1 
ATOM   1403 C  CZ2 . TRP A 1 182 ? 14.413 16.738 -13.622 1.00 12.72 ? 182 TRP A CZ2 1 
ATOM   1404 C  CZ3 . TRP A 1 182 ? 16.192 15.256 -12.936 1.00 12.13 ? 182 TRP A CZ3 1 
ATOM   1405 C  CH2 . TRP A 1 182 ? 15.582 16.062 -13.892 1.00 12.42 ? 182 TRP A CH2 1 
ATOM   1406 N  N   . GLU A 1 183 ? 12.776 13.102 -11.171 1.00 14.18 ? 183 GLU A N   1 
ATOM   1407 C  CA  . GLU A 1 183 ? 13.032 12.440 -12.434 1.00 15.00 ? 183 GLU A CA  1 
ATOM   1408 C  C   . GLU A 1 183 ? 12.612 13.413 -13.526 1.00 13.63 ? 183 GLU A C   1 
ATOM   1409 O  O   . GLU A 1 183 ? 11.684 14.190 -13.299 1.00 13.33 ? 183 GLU A O   1 
ATOM   1410 C  CB  . GLU A 1 183 ? 12.316 11.074 -12.503 1.00 16.95 ? 183 GLU A CB  1 
ATOM   1411 C  CG  . GLU A 1 183 ? 10.782 11.097 -12.473 1.00 18.86 ? 183 GLU A CG  1 
ATOM   1412 C  CD  . GLU A 1 183 ? 10.020 9.763  -12.422 1.00 21.69 ? 183 GLU A CD  1 
ATOM   1413 O  OE1 . GLU A 1 183 ? 10.626 8.681  -12.751 1.00 22.10 ? 183 GLU A OE1 1 
ATOM   1414 O  OE2 . GLU A 1 183 ? 8.781  9.789  -12.087 1.00 22.34 ? 183 GLU A OE2 1 
ATOM   1415 N  N   . SER A 1 184 ? 13.305 13.424 -14.673 1.00 12.47 ? 184 SER A N   1 
ATOM   1416 C  CA  . SER A 1 184 ? 12.918 14.284 -15.780 1.00 11.74 ? 184 SER A CA  1 
ATOM   1417 C  C   . SER A 1 184 ? 11.422 14.358 -16.064 1.00 10.87 ? 184 SER A C   1 
ATOM   1418 O  O   . SER A 1 184 ? 10.859 15.437 -16.161 1.00 10.81 ? 184 SER A O   1 
ATOM   1419 C  CB  . SER A 1 184 ? 13.657 13.825 -17.025 1.00 11.75 ? 184 SER A CB  1 
ATOM   1420 O  OG  . SER A 1 184 ? 12.731 13.465 -18.054 1.00 11.59 ? 184 SER A OG  1 
ATOM   1421 N  N   . SER A 1 185 ? 10.782 13.197 -16.190 1.00 10.05 ? 185 SER A N   1 
ATOM   1422 C  CA  . SER A 1 185 ? 9.395  13.133 -16.618 1.00 9.43  ? 185 SER A CA  1 
ATOM   1423 C  C   . SER A 1 185 ? 8.436  13.132 -15.426 1.00 8.52  ? 185 SER A C   1 
ATOM   1424 O  O   . SER A 1 185 ? 7.283  12.733 -15.562 1.00 8.14  ? 185 SER A O   1 
ATOM   1425 C  CB  . SER A 1 185 ? 9.197  11.919 -17.458 1.00 9.64  ? 185 SER A CB  1 
ATOM   1426 O  OG  . SER A 1 185 ? 9.371  10.760 -16.659 1.00 10.00 ? 185 SER A OG  1 
ATOM   1427 N  N   . ALA A 1 186 ? 8.915  13.579 -14.260 1.00 7.76  ? 186 ALA A N   1 
ATOM   1428 C  CA  . ALA A 1 186 ? 8.075  13.724 -13.085 1.00 7.21  ? 186 ALA A CA  1 
ATOM   1429 C  C   . ALA A 1 186 ? 6.881  14.599 -13.437 1.00 6.59  ? 186 ALA A C   1 
ATOM   1430 O  O   . ALA A 1 186 ? 7.081  15.601 -14.108 1.00 6.57  ? 186 ALA A O   1 
ATOM   1431 C  CB  . ALA A 1 186 ? 8.888  14.366 -11.992 1.00 7.30  ? 186 ALA A CB  1 
ATOM   1432 N  N   . VAL A 1 187 ? 5.667  14.241 -12.996 1.00 5.99  ? 187 VAL A N   1 
ATOM   1433 C  CA  . VAL A 1 187 ? 4.540  15.171 -13.061 1.00 5.63  ? 187 VAL A CA  1 
ATOM   1434 C  C   . VAL A 1 187 ? 3.991  15.479 -11.670 1.00 5.14  ? 187 VAL A C   1 
ATOM   1435 O  O   . VAL A 1 187 ? 3.483  16.580 -11.459 1.00 5.07  ? 187 VAL A O   1 
ATOM   1436 C  CB  . VAL A 1 187 ? 3.401  14.707 -13.987 1.00 5.78  ? 187 VAL A CB  1 
ATOM   1437 C  CG1 . VAL A 1 187 ? 3.852  14.675 -15.436 1.00 5.85  ? 187 VAL A CG1 1 
ATOM   1438 C  CG2 . VAL A 1 187 ? 2.791  13.374 -13.571 1.00 5.84  ? 187 VAL A CG2 1 
ATOM   1439 N  N   . VAL A 1 188 ? 4.027  14.492 -10.764 1.00 4.65  ? 188 VAL A N   1 
ATOM   1440 C  CA  . VAL A 1 188 ? 3.968  14.747 -9.333  1.00 4.27  ? 188 VAL A CA  1 
ATOM   1441 C  C   . VAL A 1 188 ? 4.981  13.833 -8.654  1.00 3.97  ? 188 VAL A C   1 
ATOM   1442 O  O   . VAL A 1 188 ? 5.131  12.680 -9.013  1.00 3.93  ? 188 VAL A O   1 
ATOM   1443 C  CB  . VAL A 1 188 ? 2.547  14.589 -8.755  1.00 4.24  ? 188 VAL A CB  1 
ATOM   1444 C  CG1 . VAL A 1 188 ? 1.853  13.337 -9.249  1.00 4.24  ? 188 VAL A CG1 1 
ATOM   1445 C  CG2 . VAL A 1 188 ? 2.539  14.626 -7.236  1.00 4.23  ? 188 VAL A CG2 1 
ATOM   1446 N  N   . ALA A 1 189 ? 5.745  14.391 -7.725  1.00 3.72  ? 189 ALA A N   1 
ATOM   1447 C  CA  . ALA A 1 189 ? 6.562  13.603 -6.826  1.00 3.54  ? 189 ALA A CA  1 
ATOM   1448 C  C   . ALA A 1 189 ? 6.011  13.861 -5.427  1.00 3.33  ? 189 ALA A C   1 
ATOM   1449 O  O   . ALA A 1 189 ? 5.397  14.895 -5.203  1.00 3.27  ? 189 ALA A O   1 
ATOM   1450 C  CB  . ALA A 1 189 ? 8.033  13.968 -6.979  1.00 3.55  ? 189 ALA A CB  1 
ATOM   1451 N  N   . SER A 1 190 ? 6.174  12.902 -4.508  1.00 3.14  ? 190 SER A N   1 
ATOM   1452 C  CA  . SER A 1 190 ? 5.675  13.043 -3.148  1.00 2.99  ? 190 SER A CA  1 
ATOM   1453 C  C   . SER A 1 190 ? 6.581  12.281 -2.183  1.00 2.85  ? 190 SER A C   1 
ATOM   1454 O  O   . SER A 1 190 ? 7.390  11.460 -2.601  1.00 2.84  ? 190 SER A O   1 
ATOM   1455 C  CB  . SER A 1 190 ? 4.247  12.556 -3.049  1.00 2.99  ? 190 SER A CB  1 
ATOM   1456 O  OG  . SER A 1 190 ? 4.197  11.134 -3.081  1.00 2.99  ? 190 SER A OG  1 
ATOM   1457 N  N   . PHE A 1 191 ? 6.445  12.574 -0.890  1.00 2.70  ? 191 PHE A N   1 
ATOM   1458 C  CA  . PHE A 1 191 ? 6.977  11.700 0.133   1.00 2.60  ? 191 PHE A CA  1 
ATOM   1459 C  C   . PHE A 1 191 ? 6.248  11.988 1.432   1.00 2.58  ? 191 PHE A C   1 
ATOM   1460 O  O   . PHE A 1 191 ? 5.834  13.120 1.637   1.00 2.57  ? 191 PHE A O   1 
ATOM   1461 C  CB  . PHE A 1 191 ? 8.498  11.836 0.261   1.00 2.54  ? 191 PHE A CB  1 
ATOM   1462 C  CG  . PHE A 1 191 ? 9.043  13.066 0.940   1.00 2.47  ? 191 PHE A CG  1 
ATOM   1463 C  CD1 . PHE A 1 191 ? 8.910  13.260 2.300   1.00 2.43  ? 191 PHE A CD1 1 
ATOM   1464 C  CD2 . PHE A 1 191 ? 9.779  13.994 0.221   1.00 2.46  ? 191 PHE A CD2 1 
ATOM   1465 C  CE1 . PHE A 1 191 ? 9.450  14.375 2.915   1.00 2.40  ? 191 PHE A CE1 1 
ATOM   1466 C  CE2 . PHE A 1 191 ? 10.321 15.110 0.837   1.00 2.42  ? 191 PHE A CE2 1 
ATOM   1467 C  CZ  . PHE A 1 191 ? 10.139 15.302 2.180   1.00 2.40  ? 191 PHE A CZ  1 
ATOM   1468 N  N   . GLU A 1 192 ? 6.073  10.945 2.263   1.00 2.57  ? 192 GLU A N   1 
ATOM   1469 C  CA  . GLU A 1 192 ? 5.660  11.104 3.651   1.00 2.56  ? 192 GLU A CA  1 
ATOM   1470 C  C   . GLU A 1 192 ? 6.567  10.244 4.525   1.00 2.45  ? 192 GLU A C   1 
ATOM   1471 O  O   . GLU A 1 192 ? 7.090  9.247  4.054   1.00 2.42  ? 192 GLU A O   1 
ATOM   1472 C  CB  . GLU A 1 192 ? 4.160  10.841 3.848   1.00 2.64  ? 192 GLU A CB  1 
ATOM   1473 C  CG  . GLU A 1 192 ? 3.757  9.387  3.912   1.00 2.74  ? 192 GLU A CG  1 
ATOM   1474 C  CD  . GLU A 1 192 ? 2.251  9.191  4.061   1.00 2.88  ? 192 GLU A CD  1 
ATOM   1475 O  OE1 . GLU A 1 192 ? 1.531  10.237 4.264   1.00 2.95  ? 192 GLU A OE1 1 
ATOM   1476 O  OE2 . GLU A 1 192 ? 1.772  7.998  3.957   1.00 2.94  ? 192 GLU A OE2 1 
ATOM   1477 N  N   . ALA A 1 193 ? 6.822  10.723 5.752   1.00 2.37  ? 193 ALA A N   1 
ATOM   1478 C  CA  . ALA A 1 193 ? 7.563  10.006 6.785   1.00 2.31  ? 193 ALA A CA  1 
ATOM   1479 C  C   . ALA A 1 193 ? 6.731  10.040 8.062   1.00 2.26  ? 193 ALA A C   1 
ATOM   1480 O  O   . ALA A 1 193 ? 6.155  11.078 8.383   1.00 2.24  ? 193 ALA A O   1 
ATOM   1481 C  CB  . ALA A 1 193 ? 8.931  10.614 7.003   1.00 2.28  ? 193 ALA A CB  1 
ATOM   1482 N  N   . THR A 1 194 ? 6.607  8.890  8.731   1.00 2.22  ? 194 THR A N   1 
ATOM   1483 C  CA  . THR A 1 194 ? 6.032  8.855  10.065  1.00 2.21  ? 194 THR A CA  1 
ATOM   1484 C  C   . THR A 1 194 ? 7.045  8.185  10.986  1.00 2.23  ? 194 THR A C   1 
ATOM   1485 O  O   . THR A 1 194 ? 7.821  7.353  10.550  1.00 2.24  ? 194 THR A O   1 
ATOM   1486 C  CB  . THR A 1 194 ? 4.652  8.177  10.104  1.00 2.18  ? 194 THR A CB  1 
ATOM   1487 O  OG1 . THR A 1 194 ? 3.904  8.548  8.950   1.00 2.18  ? 194 THR A OG1 1 
ATOM   1488 C  CG2 . THR A 1 194 ? 3.852  8.545  11.336  1.00 2.16  ? 194 THR A CG2 1 
ATOM   1489 N  N   . PHE A 1 195 ? 7.066  8.580  12.254  1.00 2.27  ? 195 PHE A N   1 
ATOM   1490 C  CA  . PHE A 1 195 ? 7.891  7.891  13.223  1.00 2.31  ? 195 PHE A CA  1 
ATOM   1491 C  C   . PHE A 1 195 ? 7.371  8.220  14.613  1.00 2.42  ? 195 PHE A C   1 
ATOM   1492 O  O   . PHE A 1 195 ? 6.872  9.317  14.838  1.00 2.42  ? 195 PHE A O   1 
ATOM   1493 C  CB  . PHE A 1 195 ? 9.367  8.271  13.077  1.00 2.27  ? 195 PHE A CB  1 
ATOM   1494 C  CG  . PHE A 1 195 ? 9.699  9.697  13.436  1.00 2.23  ? 195 PHE A CG  1 
ATOM   1495 C  CD1 . PHE A 1 195 ? 9.575  10.715 12.502  1.00 2.20  ? 195 PHE A CD1 1 
ATOM   1496 C  CD2 . PHE A 1 195 ? 10.099 10.026 14.718  1.00 2.20  ? 195 PHE A CD2 1 
ATOM   1497 C  CE1 . PHE A 1 195 ? 9.868  12.025 12.837  1.00 2.18  ? 195 PHE A CE1 1 
ATOM   1498 C  CE2 . PHE A 1 195 ? 10.392 11.338 15.050  1.00 2.19  ? 195 PHE A CE2 1 
ATOM   1499 C  CZ  . PHE A 1 195 ? 10.272 12.337 14.109  1.00 2.18  ? 195 PHE A CZ  1 
ATOM   1500 N  N   . THR A 1 196 ? 7.496  7.250  15.521  1.00 2.55  ? 196 THR A N   1 
ATOM   1501 C  CA  . THR A 1 196 ? 7.110  7.425  16.908  1.00 2.67  ? 196 THR A CA  1 
ATOM   1502 C  C   . THR A 1 196 ? 8.359  7.365  17.774  1.00 2.82  ? 196 THR A C   1 
ATOM   1503 O  O   . THR A 1 196 ? 9.363  6.770  17.395  1.00 2.82  ? 196 THR A O   1 
ATOM   1504 C  CB  . THR A 1 196 ? 6.065  6.392  17.342  1.00 2.67  ? 196 THR A CB  1 
ATOM   1505 O  OG1 . THR A 1 196 ? 6.616  5.074  17.308  1.00 2.67  ? 196 THR A OG1 1 
ATOM   1506 C  CG2 . THR A 1 196 ? 4.832  6.431  16.469  1.00 2.67  ? 196 THR A CG2 1 
ATOM   1507 N  N   . PHE A 1 197 ? 8.273  8.010  18.939  1.00 3.03  ? 197 PHE A N   1 
ATOM   1508 C  CA  . PHE A 1 197 ? 9.436  8.218  19.777  1.00 3.19  ? 197 PHE A CA  1 
ATOM   1509 C  C   . PHE A 1 197 ? 9.029  8.382  21.236  1.00 3.43  ? 197 PHE A C   1 
ATOM   1510 O  O   . PHE A 1 197 ? 7.887  8.696  21.567  1.00 3.46  ? 197 PHE A O   1 
ATOM   1511 C  CB  . PHE A 1 197 ? 10.185 9.474  19.344  1.00 3.15  ? 197 PHE A CB  1 
ATOM   1512 C  CG  . PHE A 1 197 ? 9.295  10.676 19.410  1.00 3.10  ? 197 PHE A CG  1 
ATOM   1513 C  CD1 . PHE A 1 197 ? 8.432  10.965 18.375  1.00 3.10  ? 197 PHE A CD1 1 
ATOM   1514 C  CD2 . PHE A 1 197 ? 9.230  11.437 20.557  1.00 3.10  ? 197 PHE A CD2 1 
ATOM   1515 C  CE1 . PHE A 1 197 ? 7.571  12.047 18.451  1.00 3.10  ? 197 PHE A CE1 1 
ATOM   1516 C  CE2 . PHE A 1 197 ? 8.372  12.517 20.635  1.00 3.09  ? 197 PHE A CE2 1 
ATOM   1517 C  CZ  . PHE A 1 197 ? 7.540  12.818 19.583  1.00 3.10  ? 197 PHE A CZ  1 
ATOM   1518 N  N   . LEU A 1 198 ? 10.031 8.190  22.086  1.00 3.73  ? 198 LEU A N   1 
ATOM   1519 C  CA  . LEU A 1 198 ? 9.903  8.324  23.519  1.00 3.97  ? 198 LEU A CA  1 
ATOM   1520 C  C   . LEU A 1 198 ? 11.123 9.097  24.002  1.00 4.25  ? 198 LEU A C   1 
ATOM   1521 O  O   . LEU A 1 198 ? 12.190 8.526  24.263  1.00 4.20  ? 198 LEU A O   1 
ATOM   1522 C  CB  . LEU A 1 198 ? 9.812  6.931  24.143  1.00 3.95  ? 198 LEU A CB  1 
ATOM   1523 C  CG  . LEU A 1 198 ? 9.804  6.888  25.666  1.00 3.92  ? 198 LEU A CG  1 
ATOM   1524 C  CD1 . LEU A 1 198 ? 8.968  8.006  26.252  1.00 3.93  ? 198 LEU A CD1 1 
ATOM   1525 C  CD2 . LEU A 1 198 ? 9.275  5.554  26.143  1.00 3.92  ? 198 LEU A CD2 1 
ATOM   1526 N  N   . ILE A 1 199 ? 10.938 10.421 24.000  1.00 4.60  ? 199 ILE A N   1 
ATOM   1527 C  CA  . ILE A 1 199 ? 11.842 11.350 24.648  1.00 4.87  ? 199 ILE A CA  1 
ATOM   1528 C  C   . ILE A 1 199 ? 11.471 11.367 26.116  1.00 5.08  ? 199 ILE A C   1 
ATOM   1529 O  O   . ILE A 1 199 ? 10.302 11.549 26.444  1.00 5.04  ? 199 ILE A O   1 
ATOM   1530 C  CB  . ILE A 1 199 ? 11.764 12.757 24.023  1.00 4.89  ? 199 ILE A CB  1 
ATOM   1531 C  CG1 . ILE A 1 199 ? 12.339 12.760 22.608  1.00 4.86  ? 199 ILE A CG1 1 
ATOM   1532 C  CG2 . ILE A 1 199 ? 12.457 13.789 24.901  1.00 4.93  ? 199 ILE A CG2 1 
ATOM   1533 C  CD1 . ILE A 1 199 ? 11.903 13.950 21.796  1.00 4.87  ? 199 ILE A CD1 1 
ATOM   1534 N  N   . LYS A 1 200 ? 12.495 11.191 26.952  1.00 5.40  ? 200 LYS A N   1 
ATOM   1535 C  CA  . LYS A 1 200 ? 12.327 11.005 28.377  1.00 5.76  ? 200 LYS A CA  1 
ATOM   1536 C  C   . LYS A 1 200 ? 13.619 11.465 29.030  1.00 5.98  ? 200 LYS A C   1 
ATOM   1537 O  O   . LYS A 1 200 ? 14.698 11.297 28.469  1.00 5.76  ? 200 LYS A O   1 
ATOM   1538 C  CB  . LYS A 1 200 ? 11.991 9.536  28.654  1.00 5.93  ? 200 LYS A CB  1 
ATOM   1539 C  CG  . LYS A 1 200 ? 11.572 9.161  30.072  1.00 6.10  ? 200 LYS A CG  1 
ATOM   1540 C  CD  . LYS A 1 200 ? 11.191 7.668  30.249  1.00 6.23  ? 200 LYS A CD  1 
ATOM   1541 C  CE  . LYS A 1 200 ? 12.214 6.687  29.684  1.00 6.32  ? 200 LYS A CE  1 
ATOM   1542 N  NZ  . LYS A 1 200 ? 11.785 5.270  29.817  1.00 6.30  ? 200 LYS A NZ  1 
ATOM   1543 N  N   . SER A 1 201 ? 13.478 12.059 30.216  1.00 6.51  ? 201 SER A N   1 
ATOM   1544 C  CA  . SER A 1 201 ? 14.614 12.616 30.925  1.00 6.91  ? 201 SER A CA  1 
ATOM   1545 C  C   . SER A 1 201 ? 14.335 12.654 32.424  1.00 7.19  ? 201 SER A C   1 
ATOM   1546 O  O   . SER A 1 201 ? 13.184 12.759 32.840  1.00 7.05  ? 201 SER A O   1 
ATOM   1547 C  CB  . SER A 1 201 ? 14.938 13.986 30.398  1.00 7.01  ? 201 SER A CB  1 
ATOM   1548 O  OG  . SER A 1 201 ? 16.209 14.412 30.866  1.00 7.05  ? 201 SER A OG  1 
ATOM   1549 N  N   . PRO A 1 202 ? 15.385 12.534 33.269  1.00 7.72  ? 202 PRO A N   1 
ATOM   1550 C  CA  . PRO A 1 202 ? 15.294 12.878 34.692  1.00 7.98  ? 202 PRO A CA  1 
ATOM   1551 C  C   . PRO A 1 202 ? 15.254 14.359 35.072  1.00 8.29  ? 202 PRO A C   1 
ATOM   1552 O  O   . PRO A 1 202 ? 15.276 14.661 36.263  1.00 8.51  ? 202 PRO A O   1 
ATOM   1553 C  CB  . PRO A 1 202 ? 16.600 12.326 35.284  1.00 8.02  ? 202 PRO A CB  1 
ATOM   1554 C  CG  . PRO A 1 202 ? 17.556 12.336 34.116  1.00 8.08  ? 202 PRO A CG  1 
ATOM   1555 C  CD  . PRO A 1 202 ? 16.698 11.969 32.916  1.00 7.93  ? 202 PRO A CD  1 
ATOM   1556 N  N   . ASP A 1 203 ? 15.151 15.271 34.085  1.00 8.42  ? 203 ASP A N   1 
ATOM   1557 C  CA  . ASP A 1 203 ? 15.270 16.704 34.340  1.00 8.36  ? 203 ASP A CA  1 
ATOM   1558 C  C   . ASP A 1 203 ? 14.053 17.477 33.811  1.00 8.42  ? 203 ASP A C   1 
ATOM   1559 O  O   . ASP A 1 203 ? 13.363 17.029 32.884  1.00 8.73  ? 203 ASP A O   1 
ATOM   1560 C  CB  . ASP A 1 203 ? 16.565 17.247 33.720  1.00 8.28  ? 203 ASP A CB  1 
ATOM   1561 C  CG  . ASP A 1 203 ? 17.760 16.320 33.882  1.00 8.12  ? 203 ASP A CG  1 
ATOM   1562 O  OD1 . ASP A 1 203 ? 17.932 15.753 34.976  1.00 7.89  ? 203 ASP A OD1 1 
ATOM   1563 O  OD2 . ASP A 1 203 ? 18.511 16.181 32.914  1.00 8.14  ? 203 ASP A OD2 1 
ATOM   1564 N  N   . SER A 1 204 ? 13.825 18.669 34.395  1.00 8.14  ? 204 SER A N   1 
ATOM   1565 C  CA  . SER A 1 204 ? 12.766 19.583 33.982  1.00 7.81  ? 204 SER A CA  1 
ATOM   1566 C  C   . SER A 1 204 ? 13.084 20.180 32.618  1.00 7.42  ? 204 SER A C   1 
ATOM   1567 O  O   . SER A 1 204 ? 12.192 20.670 31.938  1.00 7.19  ? 204 SER A O   1 
ATOM   1568 C  CB  . SER A 1 204 ? 12.585 20.701 34.975  1.00 7.95  ? 204 SER A CB  1 
ATOM   1569 O  OG  . SER A 1 204 ? 12.269 20.212 36.269  1.00 8.16  ? 204 SER A OG  1 
ATOM   1570 N  N   . HIS A 1 205 ? 14.382 20.190 32.292  1.00 7.24  ? 205 HIS A N   1 
ATOM   1571 C  CA  . HIS A 1 205 ? 14.903 20.723 31.046  1.00 7.03  ? 205 HIS A CA  1 
ATOM   1572 C  C   . HIS A 1 205 ? 15.585 19.592 30.283  1.00 6.64  ? 205 HIS A C   1 
ATOM   1573 O  O   . HIS A 1 205 ? 16.719 19.201 30.578  1.00 6.95  ? 205 HIS A O   1 
ATOM   1574 C  CB  . HIS A 1 205 ? 15.888 21.862 31.335  1.00 7.19  ? 205 HIS A CB  1 
ATOM   1575 C  CG  . HIS A 1 205 ? 15.265 22.995 32.079  1.00 7.30  ? 205 HIS A CG  1 
ATOM   1576 N  ND1 . HIS A 1 205 ? 14.494 23.964 31.468  1.00 7.38  ? 205 HIS A ND1 1 
ATOM   1577 C  CD2 . HIS A 1 205 ? 15.315 23.311 33.378  1.00 7.28  ? 205 HIS A CD2 1 
ATOM   1578 C  CE1 . HIS A 1 205 ? 14.088 24.835 32.383  1.00 7.41  ? 205 HIS A CE1 1 
ATOM   1579 N  NE2 . HIS A 1 205 ? 14.574 24.452 33.551  1.00 7.41  ? 205 HIS A NE2 1 
ATOM   1580 N  N   . PRO A 1 206 ? 14.914 18.994 29.287  1.00 5.96  ? 206 PRO A N   1 
ATOM   1581 C  CA  . PRO A 1 206 ? 15.553 17.970 28.476  1.00 5.59  ? 206 PRO A CA  1 
ATOM   1582 C  C   . PRO A 1 206 ? 16.100 18.646 27.219  1.00 5.15  ? 206 PRO A C   1 
ATOM   1583 O  O   . PRO A 1 206 ? 15.568 19.670 26.794  1.00 5.11  ? 206 PRO A O   1 
ATOM   1584 C  CB  . PRO A 1 206 ? 14.357 17.016 28.306  1.00 5.67  ? 206 PRO A CB  1 
ATOM   1585 C  CG  . PRO A 1 206 ? 13.140 17.929 28.214  1.00 5.78  ? 206 PRO A CG  1 
ATOM   1586 C  CD  . PRO A 1 206 ? 13.517 19.229 28.901  1.00 5.85  ? 206 PRO A CD  1 
ATOM   1587 N  N   . ALA A 1 207 ? 17.185 18.099 26.659  1.00 4.73  ? 207 ALA A N   1 
ATOM   1588 C  CA  . ALA A 1 207 ? 17.714 18.540 25.376  1.00 4.44  ? 207 ALA A CA  1 
ATOM   1589 C  C   . ALA A 1 207 ? 18.222 17.323 24.601  1.00 4.22  ? 207 ALA A C   1 
ATOM   1590 O  O   . ALA A 1 207 ? 18.468 16.290 25.213  1.00 4.25  ? 207 ALA A O   1 
ATOM   1591 C  CB  . ALA A 1 207 ? 18.795 19.564 25.606  1.00 4.39  ? 207 ALA A CB  1 
ATOM   1592 N  N   . ASP A 1 208 ? 18.383 17.413 23.269  1.00 3.96  ? 208 ASP A N   1 
ATOM   1593 C  CA  . ASP A 1 208 ? 18.224 18.625 22.481  1.00 3.76  ? 208 ASP A CA  1 
ATOM   1594 C  C   . ASP A 1 208 ? 17.100 18.507 21.463  1.00 3.51  ? 208 ASP A C   1 
ATOM   1595 O  O   . ASP A 1 208 ? 16.517 19.526 21.100  1.00 3.50  ? 208 ASP A O   1 
ATOM   1596 C  CB  . ASP A 1 208 ? 19.514 18.961 21.748  1.00 3.79  ? 208 ASP A CB  1 
ATOM   1597 C  CG  . ASP A 1 208 ? 20.493 19.637 22.673  1.00 3.84  ? 208 ASP A CG  1 
ATOM   1598 O  OD1 . ASP A 1 208 ? 21.186 18.908 23.408  1.00 3.90  ? 208 ASP A OD1 1 
ATOM   1599 O  OD2 . ASP A 1 208 ? 20.473 20.885 22.714  1.00 3.86  ? 208 ASP A OD2 1 
ATOM   1600 N  N   . GLY A 1 209 ? 16.850 17.288 20.969  1.00 3.28  ? 209 GLY A N   1 
ATOM   1601 C  CA  . GLY A 1 209 ? 15.710 17.023 20.109  1.00 3.09  ? 209 GLY A CA  1 
ATOM   1602 C  C   . GLY A 1 209 ? 15.961 15.867 19.145  1.00 2.92  ? 209 GLY A C   1 
ATOM   1603 O  O   . GLY A 1 209 ? 17.010 15.236 19.173  1.00 2.86  ? 209 GLY A O   1 
ATOM   1604 N  N   . ILE A 1 210 ? 14.961 15.622 18.290  1.00 2.76  ? 210 ILE A N   1 
ATOM   1605 C  CA  . ILE A 1 210 ? 15.011 14.637 17.224  1.00 2.63  ? 210 ILE A CA  1 
ATOM   1606 C  C   . ILE A 1 210 ? 14.636 15.362 15.936  1.00 2.55  ? 210 ILE A C   1 
ATOM   1607 O  O   . ILE A 1 210 ? 13.670 16.123 15.933  1.00 2.55  ? 210 ILE A O   1 
ATOM   1608 C  CB  . ILE A 1 210 ? 14.033 13.474 17.494  1.00 2.63  ? 210 ILE A CB  1 
ATOM   1609 C  CG1 . ILE A 1 210 ? 14.265 12.797 18.851  1.00 2.63  ? 210 ILE A CG1 1 
ATOM   1610 C  CG2 . ILE A 1 210 ? 14.071 12.471 16.354  1.00 2.63  ? 210 ILE A CG2 1 
ATOM   1611 C  CD1 . ILE A 1 210 ? 13.233 11.741 19.238  1.00 2.62  ? 210 ILE A CD1 1 
ATOM   1612 N  N   . ALA A 1 211 ? 15.394 15.123 14.856  1.00 2.43  ? 211 ALA A N   1 
ATOM   1613 C  CA  . ALA A 1 211 ? 15.008 15.556 13.522  1.00 2.34  ? 211 ALA A CA  1 
ATOM   1614 C  C   . ALA A 1 211 ? 14.818 14.332 12.631  1.00 2.28  ? 211 ALA A C   1 
ATOM   1615 O  O   . ALA A 1 211 ? 15.549 13.359 12.793  1.00 2.30  ? 211 ALA A O   1 
ATOM   1616 C  CB  . ALA A 1 211 ? 16.061 16.468 12.957  1.00 2.32  ? 211 ALA A CB  1 
ATOM   1617 N  N   . PHE A 1 212 ? 13.811 14.369 11.734  1.00 2.19  ? 212 PHE A N   1 
ATOM   1618 C  CA  . PHE A 1 212 ? 13.784 13.535 10.533  1.00 2.09  ? 212 PHE A CA  1 
ATOM   1619 C  C   . PHE A 1 212 ? 14.452 14.319 9.403   1.00 2.03  ? 212 PHE A C   1 
ATOM   1620 O  O   . PHE A 1 212 ? 14.086 15.455 9.142   1.00 2.03  ? 212 PHE A O   1 
ATOM   1621 C  CB  . PHE A 1 212 ? 12.353 13.136 10.146  1.00 2.06  ? 212 PHE A CB  1 
ATOM   1622 C  CG  . PHE A 1 212 ? 12.232 12.705 8.708   1.00 2.03  ? 212 PHE A CG  1 
ATOM   1623 C  CD1 . PHE A 1 212 ? 12.466 11.396 8.337   1.00 2.00  ? 212 PHE A CD1 1 
ATOM   1624 C  CD2 . PHE A 1 212 ? 11.992 13.639 7.701   1.00 2.03  ? 212 PHE A CD2 1 
ATOM   1625 C  CE1 . PHE A 1 212 ? 12.412 11.024 7.002   1.00 2.00  ? 212 PHE A CE1 1 
ATOM   1626 C  CE2 . PHE A 1 212 ? 11.942 13.262 6.365   1.00 2.01  ? 212 PHE A CE2 1 
ATOM   1627 C  CZ  . PHE A 1 212 ? 12.156 11.953 6.018   1.00 1.99  ? 212 PHE A CZ  1 
ATOM   1628 N  N   . PHE A 1 213 ? 15.449 13.751 8.734   1.00 1.98  ? 213 PHE A N   1 
ATOM   1629 C  CA  . PHE A 1 213 ? 16.194 14.569 7.798   1.00 1.96  ? 213 PHE A CA  1 
ATOM   1630 C  C   . PHE A 1 213 ? 16.287 13.883 6.452   1.00 1.98  ? 213 PHE A C   1 
ATOM   1631 O  O   . PHE A 1 213 ? 16.157 12.670 6.350   1.00 1.95  ? 213 PHE A O   1 
ATOM   1632 C  CB  . PHE A 1 213 ? 17.592 14.919 8.315   1.00 1.94  ? 213 PHE A CB  1 
ATOM   1633 C  CG  . PHE A 1 213 ? 18.596 13.796 8.321   1.00 1.91  ? 213 PHE A CG  1 
ATOM   1634 C  CD1 . PHE A 1 213 ? 18.530 12.790 9.265   1.00 1.90  ? 213 PHE A CD1 1 
ATOM   1635 C  CD2 . PHE A 1 213 ? 19.625 13.764 7.403   1.00 1.90  ? 213 PHE A CD2 1 
ATOM   1636 C  CE1 . PHE A 1 213 ? 19.471 11.773 9.287   1.00 1.91  ? 213 PHE A CE1 1 
ATOM   1637 C  CE2 . PHE A 1 213 ? 20.558 12.742 7.419   1.00 1.91  ? 213 PHE A CE2 1 
ATOM   1638 C  CZ  . PHE A 1 213 ? 20.478 11.744 8.360   1.00 1.91  ? 213 PHE A CZ  1 
ATOM   1639 N  N   . ILE A 1 214 ? 16.494 14.722 5.442   1.00 2.02  ? 214 ILE A N   1 
ATOM   1640 C  CA  . ILE A 1 214 ? 16.723 14.282 4.084   1.00 2.08  ? 214 ILE A CA  1 
ATOM   1641 C  C   . ILE A 1 214 ? 18.000 14.960 3.618   1.00 2.17  ? 214 ILE A C   1 
ATOM   1642 O  O   . ILE A 1 214 ? 18.116 16.181 3.736   1.00 2.17  ? 214 ILE A O   1 
ATOM   1643 C  CB  . ILE A 1 214 ? 15.540 14.648 3.170   1.00 2.06  ? 214 ILE A CB  1 
ATOM   1644 C  CG1 . ILE A 1 214 ? 14.199 14.324 3.823   1.00 2.04  ? 214 ILE A CG1 1 
ATOM   1645 C  CG2 . ILE A 1 214 ? 15.700 13.973 1.816   1.00 2.05  ? 214 ILE A CG2 1 
ATOM   1646 C  CD1 . ILE A 1 214 ? 13.021 14.752 3.023   1.00 2.04  ? 214 ILE A CD1 1 
ATOM   1647 N  N   . SER A 1 215 ? 18.945 14.161 3.106   1.00 2.29  ? 215 SER A N   1 
ATOM   1648 C  CA  . SER A 1 215 ? 20.299 14.644 2.875   1.00 2.39  ? 215 SER A CA  1 
ATOM   1649 C  C   . SER A 1 215 ? 20.875 14.045 1.610   1.00 2.47  ? 215 SER A C   1 
ATOM   1650 O  O   . SER A 1 215 ? 20.307 13.132 1.022   1.00 2.44  ? 215 SER A O   1 
ATOM   1651 C  CB  . SER A 1 215 ? 21.214 14.326 4.033   1.00 2.41  ? 215 SER A CB  1 
ATOM   1652 O  OG  . SER A 1 215 ? 21.522 12.942 4.057   1.00 2.44  ? 215 SER A OG  1 
ATOM   1653 N  N   . ASN A 1 216 ? 22.046 14.548 1.238   1.00 2.60  ? 216 ASN A N   1 
ATOM   1654 C  CA  . ASN A 1 216 ? 22.785 13.871 0.193   1.00 2.74  ? 216 ASN A CA  1 
ATOM   1655 C  C   . ASN A 1 216 ? 23.146 12.489 0.725   1.00 2.91  ? 216 ASN A C   1 
ATOM   1656 O  O   . ASN A 1 216 ? 23.039 12.224 1.931   1.00 2.89  ? 216 ASN A O   1 
ATOM   1657 C  CB  . ASN A 1 216 ? 23.981 14.671 -0.297  1.00 2.69  ? 216 ASN A CB  1 
ATOM   1658 C  CG  . ASN A 1 216 ? 24.761 15.178 0.871   1.00 2.68  ? 216 ASN A CG  1 
ATOM   1659 O  OD1 . ASN A 1 216 ? 24.284 16.067 1.562   1.00 2.67  ? 216 ASN A OD1 1 
ATOM   1660 N  ND2 . ASN A 1 216 ? 25.909 14.569 1.119   1.00 2.70  ? 216 ASN A ND2 1 
ATOM   1661 N  N   . ILE A 1 217 ? 23.506 11.604 -0.212  1.00 3.08  ? 217 ILE A N   1 
ATOM   1662 C  CA  . ILE A 1 217 ? 23.539 10.184 0.086   1.00 3.23  ? 217 ILE A CA  1 
ATOM   1663 C  C   . ILE A 1 217 ? 24.825 9.844  0.825   1.00 3.32  ? 217 ILE A C   1 
ATOM   1664 O  O   . ILE A 1 217 ? 24.908 8.803  1.455   1.00 3.35  ? 217 ILE A O   1 
ATOM   1665 C  CB  . ILE A 1 217 ? 23.384 9.346  -1.195  1.00 3.27  ? 217 ILE A CB  1 
ATOM   1666 C  CG1 . ILE A 1 217 ? 24.651 9.437  -2.067  1.00 3.29  ? 217 ILE A CG1 1 
ATOM   1667 C  CG2 . ILE A 1 217 ? 22.082 9.731  -1.901  1.00 3.24  ? 217 ILE A CG2 1 
ATOM   1668 C  CD1 . ILE A 1 217 ? 24.516 8.858  -3.470  1.00 3.30  ? 217 ILE A CD1 1 
ATOM   1669 N  N   . ASP A 1 218 ? 25.813 10.731 0.747   1.00 3.43  ? 218 ASP A N   1 
ATOM   1670 C  CA  . ASP A 1 218 ? 27.081 10.503 1.408   1.00 3.53  ? 218 ASP A CA  1 
ATOM   1671 C  C   . ASP A 1 218 ? 27.087 11.249 2.749   1.00 3.53  ? 218 ASP A C   1 
ATOM   1672 O  O   . ASP A 1 218 ? 28.118 11.341 3.419   1.00 3.53  ? 218 ASP A O   1 
ATOM   1673 C  CB  . ASP A 1 218 ? 28.212 10.814 0.422   1.00 3.64  ? 218 ASP A CB  1 
ATOM   1674 C  CG  . ASP A 1 218 ? 28.047 12.093 -0.398  1.00 3.75  ? 218 ASP A CG  1 
ATOM   1675 O  OD1 . ASP A 1 218 ? 26.911 12.407 -0.825  1.00 3.75  ? 218 ASP A OD1 1 
ATOM   1676 O  OD2 . ASP A 1 218 ? 29.084 12.742 -0.664  1.00 3.93  ? 218 ASP A OD2 1 
ATOM   1677 N  N   . SER A 1 219 ? 25.910 11.720 3.188   1.00 3.52  ? 219 SER A N   1 
ATOM   1678 C  CA  . SER A 1 219 ? 25.820 12.575 4.361   1.00 3.50  ? 219 SER A CA  1 
ATOM   1679 C  C   . SER A 1 219 ? 26.366 11.853 5.592   1.00 3.59  ? 219 SER A C   1 
ATOM   1680 O  O   . SER A 1 219 ? 26.125 10.663 5.760   1.00 3.58  ? 219 SER A O   1 
ATOM   1681 C  CB  . SER A 1 219 ? 24.412 13.032 4.585   1.00 3.44  ? 219 SER A CB  1 
ATOM   1682 O  OG  . SER A 1 219 ? 24.314 13.798 5.775   1.00 3.42  ? 219 SER A OG  1 
ATOM   1683 N  N   . SER A 1 220 ? 27.088 12.584 6.454   1.00 3.67  ? 220 SER A N   1 
ATOM   1684 C  CA  . SER A 1 220 ? 27.565 12.032 7.713   1.00 3.73  ? 220 SER A CA  1 
ATOM   1685 C  C   . SER A 1 220 ? 27.501 13.097 8.810   1.00 3.74  ? 220 SER A C   1 
ATOM   1686 O  O   . SER A 1 220 ? 27.329 14.269 8.504   1.00 3.73  ? 220 SER A O   1 
ATOM   1687 C  CB  . SER A 1 220 ? 28.958 11.474 7.557   1.00 3.78  ? 220 SER A CB  1 
ATOM   1688 O  OG  . SER A 1 220 ? 29.942 12.499 7.735   1.00 3.85  ? 220 SER A OG  1 
ATOM   1689 N  N   . ILE A 1 221 ? 27.660 12.666 10.074  1.00 3.79  ? 221 ILE A N   1 
ATOM   1690 C  CA  . ILE A 1 221 ? 27.598 13.519 11.255  1.00 3.84  ? 221 ILE A CA  1 
ATOM   1691 C  C   . ILE A 1 221 ? 28.766 14.496 11.221  1.00 3.90  ? 221 ILE A C   1 
ATOM   1692 O  O   . ILE A 1 221 ? 29.914 14.066 11.358  1.00 3.86  ? 221 ILE A O   1 
ATOM   1693 C  CB  . ILE A 1 221 ? 27.631 12.687 12.556  1.00 3.85  ? 221 ILE A CB  1 
ATOM   1694 C  CG1 . ILE A 1 221 ? 26.302 11.976 12.827  1.00 3.90  ? 221 ILE A CG1 1 
ATOM   1695 C  CG2 . ILE A 1 221 ? 28.025 13.530 13.753  1.00 3.84  ? 221 ILE A CG2 1 
ATOM   1696 C  CD1 . ILE A 1 221 ? 26.409 10.745 13.734  1.00 3.91  ? 221 ILE A CD1 1 
ATOM   1697 N  N   . PRO A 1 222 ? 28.486 15.819 11.089  1.00 3.97  ? 222 PRO A N   1 
ATOM   1698 C  CA  . PRO A 1 222 ? 29.518 16.856 11.138  1.00 4.05  ? 222 PRO A CA  1 
ATOM   1699 C  C   . PRO A 1 222 ? 30.076 17.078 12.542  1.00 4.01  ? 222 PRO A C   1 
ATOM   1700 O  O   . PRO A 1 222 ? 29.349 16.915 13.509  1.00 4.03  ? 222 PRO A O   1 
ATOM   1701 C  CB  . PRO A 1 222 ? 28.801 18.144 10.699  1.00 4.03  ? 222 PRO A CB  1 
ATOM   1702 C  CG  . PRO A 1 222 ? 27.383 17.746 10.315  1.00 3.98  ? 222 PRO A CG  1 
ATOM   1703 C  CD  . PRO A 1 222 ? 27.141 16.382 10.913  1.00 3.96  ? 222 PRO A CD  1 
ATOM   1704 N  N   . SER A 1 223 ? 31.340 17.503 12.656  1.00 4.00  ? 223 SER A N   1 
ATOM   1705 C  CA  . SER A 1 223 ? 31.995 17.621 13.952  1.00 3.95  ? 223 SER A CA  1 
ATOM   1706 C  C   . SER A 1 223 ? 31.281 18.654 14.813  1.00 3.82  ? 223 SER A C   1 
ATOM   1707 O  O   . SER A 1 223 ? 30.783 19.659 14.306  1.00 3.71  ? 223 SER A O   1 
ATOM   1708 C  CB  . SER A 1 223 ? 33.451 17.982 13.849  1.00 4.05  ? 223 SER A CB  1 
ATOM   1709 O  OG  . SER A 1 223 ? 33.965 17.645 12.570  1.00 4.23  ? 223 SER A OG  1 
ATOM   1710 N  N   . GLY A 1 224 ? 31.274 18.359 16.121  1.00 3.78  ? 224 GLY A N   1 
ATOM   1711 C  CA  . GLY A 1 224 ? 30.592 19.135 17.148  1.00 3.74  ? 224 GLY A CA  1 
ATOM   1712 C  C   . GLY A 1 224 ? 29.098 19.355 16.887  1.00 3.67  ? 224 GLY A C   1 
ATOM   1713 O  O   . GLY A 1 224 ? 28.554 20.375 17.325  1.00 3.63  ? 224 GLY A O   1 
ATOM   1714 N  N   . SER A 1 225 ? 28.434 18.409 16.199  1.00 3.60  ? 225 SER A N   1 
ATOM   1715 C  CA  . SER A 1 225 ? 27.002 18.528 15.973  1.00 3.60  ? 225 SER A CA  1 
ATOM   1716 C  C   . SER A 1 225 ? 26.245 17.808 17.087  1.00 3.57  ? 225 SER A C   1 
ATOM   1717 O  O   . SER A 1 225 ? 25.129 17.341 16.897  1.00 3.53  ? 225 SER A O   1 
ATOM   1718 C  CB  . SER A 1 225 ? 26.587 18.058 14.603  1.00 3.60  ? 225 SER A CB  1 
ATOM   1719 O  OG  . SER A 1 225 ? 26.839 16.675 14.440  1.00 3.61  ? 225 SER A OG  1 
ATOM   1720 N  N   . THR A 1 226 ? 26.876 17.739 18.259  1.00 3.57  ? 226 THR A N   1 
ATOM   1721 C  CA  . THR A 1 226 ? 26.193 17.402 19.489  1.00 3.63  ? 226 THR A CA  1 
ATOM   1722 C  C   . THR A 1 226 ? 25.398 18.609 19.967  1.00 3.72  ? 226 THR A C   1 
ATOM   1723 O  O   . THR A 1 226 ? 25.641 19.740 19.535  1.00 3.78  ? 226 THR A O   1 
ATOM   1724 C  CB  . THR A 1 226 ? 27.221 16.985 20.536  1.00 3.62  ? 226 THR A CB  1 
ATOM   1725 O  OG1 . THR A 1 226 ? 28.309 17.850 20.219  1.00 3.62  ? 226 THR A OG1 1 
ATOM   1726 C  CG2 . THR A 1 226 ? 27.625 15.526 20.461  1.00 3.63  ? 226 THR A CG2 1 
ATOM   1727 N  N   . GLY A 1 227 ? 24.447 18.352 20.870  1.00 3.77  ? 227 GLY A N   1 
ATOM   1728 C  CA  . GLY A 1 227 ? 23.681 19.421 21.482  1.00 3.80  ? 227 GLY A CA  1 
ATOM   1729 C  C   . GLY A 1 227 ? 22.777 20.125 20.475  1.00 3.86  ? 227 GLY A C   1 
ATOM   1730 O  O   . GLY A 1 227 ? 21.969 19.481 19.821  1.00 3.86  ? 227 GLY A O   1 
ATOM   1731 N  N   . ARG A 1 228 ? 22.955 21.447 20.326  1.00 3.96  ? 228 ARG A N   1 
ATOM   1732 C  CA  . ARG A 1 228 ? 21.924 22.307 19.761  1.00 3.99  ? 228 ARG A CA  1 
ATOM   1733 C  C   . ARG A 1 228 ? 21.834 22.126 18.252  1.00 3.95  ? 228 ARG A C   1 
ATOM   1734 O  O   . ARG A 1 228 ? 20.804 22.477 17.669  1.00 4.03  ? 228 ARG A O   1 
ATOM   1735 C  CB  . ARG A 1 228 ? 22.154 23.778 20.118  1.00 4.05  ? 228 ARG A CB  1 
ATOM   1736 C  CG  . ARG A 1 228 ? 23.457 24.358 19.595  1.00 4.13  ? 228 ARG A CG  1 
ATOM   1737 C  CD  . ARG A 1 228 ? 23.583 25.832 19.935  1.00 4.20  ? 228 ARG A CD  1 
ATOM   1738 N  NE  . ARG A 1 228 ? 23.772 26.048 21.363  1.00 4.28  ? 228 ARG A NE  1 
ATOM   1739 C  CZ  . ARG A 1 228 ? 23.748 27.233 21.972  1.00 4.36  ? 228 ARG A CZ  1 
ATOM   1740 N  NH1 . ARG A 1 228 ? 23.388 28.330 21.323  1.00 4.41  ? 228 ARG A NH1 1 
ATOM   1741 N  NH2 . ARG A 1 228 ? 24.061 27.310 23.253  1.00 4.37  ? 228 ARG A NH2 1 
ATOM   1742 N  N   . LEU A 1 229 ? 22.888 21.542 17.657  1.00 3.87  ? 229 LEU A N   1 
ATOM   1743 C  CA  . LEU A 1 229 ? 22.987 21.360 16.212  1.00 3.80  ? 229 LEU A CA  1 
ATOM   1744 C  C   . LEU A 1 229 ? 22.359 20.034 15.744  1.00 3.71  ? 229 LEU A C   1 
ATOM   1745 O  O   . LEU A 1 229 ? 22.307 19.771 14.533  1.00 3.71  ? 229 LEU A O   1 
ATOM   1746 C  CB  . LEU A 1 229 ? 24.470 21.455 15.837  1.00 3.80  ? 229 LEU A CB  1 
ATOM   1747 C  CG  . LEU A 1 229 ? 25.137 22.789 16.193  1.00 3.82  ? 229 LEU A CG  1 
ATOM   1748 C  CD1 . LEU A 1 229 ? 26.657 22.748 15.984  1.00 3.84  ? 229 LEU A CD1 1 
ATOM   1749 C  CD2 . LEU A 1 229 ? 24.519 23.948 15.408  1.00 3.78  ? 229 LEU A CD2 1 
ATOM   1750 N  N   . LEU A 1 230 ? 21.923 19.187 16.700  1.00 3.55  ? 230 LEU A N   1 
ATOM   1751 C  CA  . LEU A 1 230 ? 21.006 18.081 16.450  1.00 3.43  ? 230 LEU A CA  1 
ATOM   1752 C  C   . LEU A 1 230 ? 21.605 16.998 15.547  1.00 3.38  ? 230 LEU A C   1 
ATOM   1753 O  O   . LEU A 1 230 ? 20.893 16.114 15.081  1.00 3.35  ? 230 LEU A O   1 
ATOM   1754 C  CB  . LEU A 1 230 ? 19.717 18.661 15.859  1.00 3.40  ? 230 LEU A CB  1 
ATOM   1755 C  CG  . LEU A 1 230 ? 18.896 19.506 16.831  1.00 3.36  ? 230 LEU A CG  1 
ATOM   1756 C  CD1 . LEU A 1 230 ? 17.700 20.130 16.136  1.00 3.35  ? 230 LEU A CD1 1 
ATOM   1757 C  CD2 . LEU A 1 230 ? 18.439 18.664 18.009  1.00 3.34  ? 230 LEU A CD2 1 
ATOM   1758 N  N   . GLY A 1 231 ? 22.923 17.042 15.330  1.00 3.36  ? 231 GLY A N   1 
ATOM   1759 C  CA  . GLY A 1 231 ? 23.610 16.072 14.496  1.00 3.32  ? 231 GLY A CA  1 
ATOM   1760 C  C   . GLY A 1 231 ? 23.477 16.367 13.006  1.00 3.28  ? 231 GLY A C   1 
ATOM   1761 O  O   . GLY A 1 231 ? 23.871 15.523 12.204  1.00 3.25  ? 231 GLY A O   1 
ATOM   1762 N  N   . LEU A 1 232 ? 22.941 17.557 12.657  1.00 3.25  ? 232 LEU A N   1 
ATOM   1763 C  CA  . LEU A 1 232 ? 22.548 17.901 11.292  1.00 3.22  ? 232 LEU A CA  1 
ATOM   1764 C  C   . LEU A 1 232 ? 23.546 18.867 10.660  1.00 3.32  ? 232 LEU A C   1 
ATOM   1765 O  O   . LEU A 1 232 ? 24.010 18.656 9.542   1.00 3.31  ? 232 LEU A O   1 
ATOM   1766 C  CB  . LEU A 1 232 ? 21.165 18.549 11.323  1.00 3.14  ? 232 LEU A CB  1 
ATOM   1767 C  CG  . LEU A 1 232 ? 20.017 17.668 11.805  1.00 3.09  ? 232 LEU A CG  1 
ATOM   1768 C  CD1 . LEU A 1 232 ? 18.684 18.255 11.393  1.00 3.08  ? 232 LEU A CD1 1 
ATOM   1769 C  CD2 . LEU A 1 232 ? 20.141 16.257 11.278  1.00 3.07  ? 232 LEU A CD2 1 
ATOM   1770 N  N   . PHE A 1 233 ? 23.857 19.933 11.402  1.00 3.44  ? 233 PHE A N   1 
ATOM   1771 C  CA  . PHE A 1 233 ? 24.689 21.027 10.930  1.00 3.51  ? 233 PHE A CA  1 
ATOM   1772 C  C   . PHE A 1 233 ? 26.018 21.040 11.685  1.00 3.57  ? 233 PHE A C   1 
ATOM   1773 O  O   . PHE A 1 233 ? 26.075 20.591 12.831  1.00 3.57  ? 233 PHE A O   1 
ATOM   1774 C  CB  . PHE A 1 233 ? 23.898 22.323 11.107  1.00 3.52  ? 233 PHE A CB  1 
ATOM   1775 C  CG  . PHE A 1 233 ? 22.561 22.283 10.408  1.00 3.54  ? 233 PHE A CG  1 
ATOM   1776 C  CD1 . PHE A 1 233 ? 22.463 22.548 9.042   1.00 3.51  ? 233 PHE A CD1 1 
ATOM   1777 C  CD2 . PHE A 1 233 ? 21.410 21.907 11.095  1.00 3.53  ? 233 PHE A CD2 1 
ATOM   1778 C  CE1 . PHE A 1 233 ? 21.238 22.490 8.391   1.00 3.47  ? 233 PHE A CE1 1 
ATOM   1779 C  CE2 . PHE A 1 233 ? 20.185 21.826 10.437  1.00 3.53  ? 233 PHE A CE2 1 
ATOM   1780 C  CZ  . PHE A 1 233 ? 20.101 22.124 9.088   1.00 3.52  ? 233 PHE A CZ  1 
ATOM   1781 N  N   . PRO A 1 234 ? 27.119 21.539 11.058  1.00 3.65  ? 234 PRO A N   1 
ATOM   1782 C  CA  . PRO A 1 234 ? 28.401 21.748 11.747  1.00 3.67  ? 234 PRO A CA  1 
ATOM   1783 C  C   . PRO A 1 234 ? 28.471 23.042 12.561  1.00 3.72  ? 234 PRO A C   1 
ATOM   1784 O  O   . PRO A 1 234 ? 29.193 23.097 13.551  1.00 3.73  ? 234 PRO A O   1 
ATOM   1785 C  CB  . PRO A 1 234 ? 29.380 21.817 10.577  1.00 3.64  ? 234 PRO A CB  1 
ATOM   1786 C  CG  . PRO A 1 234 ? 28.578 22.525 9.507   1.00 3.61  ? 234 PRO A CG  1 
ATOM   1787 C  CD  . PRO A 1 234 ? 27.181 21.964 9.648   1.00 3.61  ? 234 PRO A CD  1 
ATOM   1788 N  N   . ASP A 1 235 ? 27.690 24.055 12.151  1.00 3.74  ? 235 ASP A N   1 
ATOM   1789 C  CA  . ASP A 1 235 ? 27.587 25.321 12.856  1.00 3.78  ? 235 ASP A CA  1 
ATOM   1790 C  C   . ASP A 1 235 ? 26.120 25.774 12.879  1.00 3.86  ? 235 ASP A C   1 
ATOM   1791 O  O   . ASP A 1 235 ? 25.241 25.004 12.504  1.00 3.82  ? 235 ASP A O   1 
ATOM   1792 C  CB  . ASP A 1 235 ? 28.512 26.335 12.196  1.00 3.74  ? 235 ASP A CB  1 
ATOM   1793 C  CG  . ASP A 1 235 ? 28.161 26.570 10.743  1.00 3.73  ? 235 ASP A CG  1 
ATOM   1794 O  OD1 . ASP A 1 235 ? 27.074 27.114 10.463  1.00 3.69  ? 235 ASP A OD1 1 
ATOM   1795 O  OD2 . ASP A 1 235 ? 28.972 26.189 9.912   1.00 3.76  ? 235 ASP A OD2 1 
ATOM   1796 N  N   . ALA A 1 236 ? 25.863 27.022 13.324  1.00 3.96  ? 236 ALA A N   1 
ATOM   1797 C  CA  . ALA A 1 236 ? 24.510 27.523 13.563  1.00 4.03  ? 236 ALA A CA  1 
ATOM   1798 C  C   . ALA A 1 236 ? 24.102 28.606 12.552  1.00 4.10  ? 236 ALA A C   1 
ATOM   1799 O  O   . ALA A 1 236 ? 23.141 29.343 12.759  1.00 4.00  ? 236 ALA A O   1 
ATOM   1800 C  CB  . ALA A 1 236 ? 24.418 28.039 14.983  1.00 4.01  ? 236 ALA A CB  1 
ATOM   1801 N  N   . ASN A 1 237 ? 24.817 28.691 11.432  1.00 4.20  ? 237 ASN A N   1 
ATOM   1802 C  CA  . ASN A 1 237 ? 24.506 29.687 10.427  1.00 4.32  ? 237 ASN A CA  1 
ATOM   1803 C  C   . ASN A 1 237 ? 23.177 29.314 9.760   1.00 4.42  ? 237 ASN A C   1 
ATOM   1804 O  O   . ASN A 1 237 ? 22.984 28.090 9.535   1.00 4.43  ? 237 ASN A O   1 
ATOM   1805 C  CB  . ASN A 1 237 ? 25.631 29.795 9.395   1.00 4.37  ? 237 ASN A CB  1 
ATOM   1806 C  CG  . ASN A 1 237 ? 26.995 30.020 10.014  1.00 4.39  ? 237 ASN A CG  1 
ATOM   1807 O  OD1 . ASN A 1 237 ? 28.000 29.716 9.382   1.00 4.44  ? 237 ASN A OD1 1 
ATOM   1808 N  ND2 . ASN A 1 237 ? 27.057 30.511 11.244  1.00 4.40  ? 237 ASN A ND2 1 
ATOM   1809 O  OXT . ASN A 1 237 ? 22.382 30.257 9.485   1.00 4.47  ? 237 ASN A OXT 1 
HETATM 1810 N  N1  . URF B 2 .   ? 10.997 5.925  -6.164  1.00 16.14 ? 301 URF A N1  1 
HETATM 1811 C  C2  . URF B 2 .   ? 11.465 6.596  -5.072  1.00 15.73 ? 301 URF A C2  1 
HETATM 1812 N  N3  . URF B 2 .   ? 12.511 5.973  -4.425  1.00 16.45 ? 301 URF A N3  1 
HETATM 1813 C  C4  . URF B 2 .   ? 13.105 4.762  -4.748  1.00 16.69 ? 301 URF A C4  1 
HETATM 1814 C  C5  . URF B 2 .   ? 12.519 4.145  -5.926  1.00 16.52 ? 301 URF A C5  1 
HETATM 1815 C  C6  . URF B 2 .   ? 11.516 4.730  -6.589  1.00 16.06 ? 301 URF A C6  1 
HETATM 1816 O  O2  . URF B 2 .   ? 11.000 7.667  -4.695  1.00 14.31 ? 301 URF A O2  1 
HETATM 1817 O  O4  . URF B 2 .   ? 14.026 4.290  -4.068  1.00 16.40 ? 301 URF A O4  1 
HETATM 1818 F  F5  . URF B 2 .   ? 13.019 2.965  -6.334  1.00 17.42 ? 301 URF A F5  1 
HETATM 1819 CA CA  . CA  C 3 .   ? 17.686 23.699 20.341  1.00 2.55  ? 302 CA  A CA  1 
HETATM 1820 MN MN  . MN  D 4 .   ? 14.550 25.597 16.326  1.00 1.57  ? 303 MN  A MN  1 
HETATM 1821 S  S   . SO4 E 5 .   ? 32.478 17.834 8.996   1.00 39.72 ? 304 SO4 A S   1 
HETATM 1822 O  O1  . SO4 E 5 .   ? 33.650 17.169 8.455   1.00 37.01 ? 304 SO4 A O1  1 
HETATM 1823 O  O2  . SO4 E 5 .   ? 31.285 17.166 8.544   1.00 37.70 ? 304 SO4 A O2  1 
HETATM 1824 O  O3  . SO4 E 5 .   ? 32.534 17.778 10.431  1.00 38.20 ? 304 SO4 A O3  1 
HETATM 1825 O  O4  . SO4 E 5 .   ? 32.427 19.220 8.572   1.00 38.28 ? 304 SO4 A O4  1 
HETATM 1826 O  O   . HOH F 6 .   ? 22.693 26.072 10.838  1.00 1.64  ? 401 HOH A O   1 
HETATM 1827 O  O   . HOH F 6 .   ? 8.521  11.995 24.771  1.00 2.76  ? 402 HOH A O   1 
HETATM 1828 O  O   . HOH F 6 .   ? 1.652  9.310  19.775  1.00 0.75  ? 403 HOH A O   1 
HETATM 1829 O  O   . HOH F 6 .   ? 26.654 18.530 -0.782  1.00 0.80  ? 404 HOH A O   1 
HETATM 1830 O  O   . HOH F 6 .   ? 5.525  2.683  17.959  1.00 1.63  ? 405 HOH A O   1 
HETATM 1831 O  O   . HOH F 6 .   ? 2.240  20.625 20.923  1.00 1.05  ? 406 HOH A O   1 
HETATM 1832 O  O   . HOH F 6 .   ? 3.224  -0.808 5.483   1.00 0.50  ? 407 HOH A O   1 
HETATM 1833 O  O   . HOH F 6 .   ? 0.216  11.393 25.905  1.00 0.60  ? 408 HOH A O   1 
HETATM 1834 O  O   . HOH F 6 .   ? 4.242  6.450  5.131   1.00 1.32  ? 409 HOH A O   1 
HETATM 1835 O  O   . HOH F 6 .   ? 17.704 8.011  34.872  1.00 5.99  ? 410 HOH A O   1 
HETATM 1836 O  O   . HOH F 6 .   ? 15.643 16.943 -6.211  1.00 2.39  ? 411 HOH A O   1 
HETATM 1837 O  O   . HOH F 6 .   ? 13.736 -4.873 8.466   1.00 2.91  ? 412 HOH A O   1 
HETATM 1838 O  O   . HOH F 6 .   ? 25.684 0.619  10.199  1.00 0.50  ? 413 HOH A O   1 
# 
