data_9J1A
# 
_entry.id   9J1A 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9J1A         pdb_00009j1a 10.2210/pdb9j1a/pdb 
WWPDB D_1300050148 ?            ?                   
# 
_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       2024-12-04 
# 
_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                        9J1A 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-04 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              guosong@fudan.edu.cn 
_pdbx_contact_author.name_first         Guosong 
_pdbx_contact_author.name_last          Chen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7089-911X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, L.'   1 ? 
'Chen, G.' 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                     'Structure of ConA without ligand' 
_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 'Li, L.'   1 ? 
primary 'Chen, G.' 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-A       25622.385 1   ? ? ? ? 
2 non-polymer syn GLYCEROL             92.094    1   ? ? ? ? 
3 non-polymer syn 'MANGANESE (II) ION' 54.938    1   ? ? ? ? 
4 non-polymer syn 'CALCIUM ION'        40.078    1   ? ? ? ? 
5 water       nat water                18.015    122 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Con A' 
# 
_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 GLYCEROL             GOL 
3 'MANGANESE (II) ION' MN  
4 'CALCIUM ION'        CA  
5 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 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_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 
1 1 sample 1   118 'jack bean' 'Canavalia ensiformis' 3823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 119 237 'jack bean' 'Canavalia ensiformis' 3823 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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  
GOL non-polymer         . GLYCEROL             'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
THR 'L-peptide linking' y THREONINE            ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE             ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE               ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   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 
# 
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 GOL 1   401 401 GOL GOL A . 
C 3 MN  1   402 1   MN  MN  A . 
D 4 CA  1   403 1   CA  CA  A . 
E 5 HOH 1   501 66  HOH HOH A . 
E 5 HOH 2   502 86  HOH HOH A . 
E 5 HOH 3   503 54  HOH HOH A . 
E 5 HOH 4   504 41  HOH HOH A . 
E 5 HOH 5   505 71  HOH HOH A . 
E 5 HOH 6   506 52  HOH HOH A . 
E 5 HOH 7   507 97  HOH HOH A . 
E 5 HOH 8   508 105 HOH HOH A . 
E 5 HOH 9   509 72  HOH HOH A . 
E 5 HOH 10  510 25  HOH HOH A . 
E 5 HOH 11  511 108 HOH HOH A . 
E 5 HOH 12  512 79  HOH HOH A . 
E 5 HOH 13  513 18  HOH HOH A . 
E 5 HOH 14  514 85  HOH HOH A . 
E 5 HOH 15  515 60  HOH HOH A . 
E 5 HOH 16  516 119 HOH HOH A . 
E 5 HOH 17  517 9   HOH HOH A . 
E 5 HOH 18  518 124 HOH HOH A . 
E 5 HOH 19  519 42  HOH HOH A . 
E 5 HOH 20  520 34  HOH HOH A . 
E 5 HOH 21  521 103 HOH HOH A . 
E 5 HOH 22  522 67  HOH HOH A . 
E 5 HOH 23  523 12  HOH HOH A . 
E 5 HOH 24  524 100 HOH HOH A . 
E 5 HOH 25  525 99  HOH HOH A . 
E 5 HOH 26  526 121 HOH HOH A . 
E 5 HOH 27  527 47  HOH HOH A . 
E 5 HOH 28  528 63  HOH HOH A . 
E 5 HOH 29  529 29  HOH HOH A . 
E 5 HOH 30  530 13  HOH HOH A . 
E 5 HOH 31  531 122 HOH HOH A . 
E 5 HOH 32  532 39  HOH HOH A . 
E 5 HOH 33  533 61  HOH HOH A . 
E 5 HOH 34  534 75  HOH HOH A . 
E 5 HOH 35  535 93  HOH HOH A . 
E 5 HOH 36  536 74  HOH HOH A . 
E 5 HOH 37  537 44  HOH HOH A . 
E 5 HOH 38  538 20  HOH HOH A . 
E 5 HOH 39  539 46  HOH HOH A . 
E 5 HOH 40  540 4   HOH HOH A . 
E 5 HOH 41  541 15  HOH HOH A . 
E 5 HOH 42  542 55  HOH HOH A . 
E 5 HOH 43  543 82  HOH HOH A . 
E 5 HOH 44  544 84  HOH HOH A . 
E 5 HOH 45  545 65  HOH HOH A . 
E 5 HOH 46  546 62  HOH HOH A . 
E 5 HOH 47  547 6   HOH HOH A . 
E 5 HOH 48  548 73  HOH HOH A . 
E 5 HOH 49  549 104 HOH HOH A . 
E 5 HOH 50  550 1   HOH HOH A . 
E 5 HOH 51  551 83  HOH HOH A . 
E 5 HOH 52  552 64  HOH HOH A . 
E 5 HOH 53  553 89  HOH HOH A . 
E 5 HOH 54  554 23  HOH HOH A . 
E 5 HOH 55  555 16  HOH HOH A . 
E 5 HOH 56  556 92  HOH HOH A . 
E 5 HOH 57  557 125 HOH HOH A . 
E 5 HOH 58  558 5   HOH HOH A . 
E 5 HOH 59  559 117 HOH HOH A . 
E 5 HOH 60  560 78  HOH HOH A . 
E 5 HOH 61  561 101 HOH HOH A . 
E 5 HOH 62  562 22  HOH HOH A . 
E 5 HOH 63  563 53  HOH HOH A . 
E 5 HOH 64  564 69  HOH HOH A . 
E 5 HOH 65  565 45  HOH HOH A . 
E 5 HOH 66  566 81  HOH HOH A . 
E 5 HOH 67  567 76  HOH HOH A . 
E 5 HOH 68  568 80  HOH HOH A . 
E 5 HOH 69  569 110 HOH HOH A . 
E 5 HOH 70  570 87  HOH HOH A . 
E 5 HOH 71  571 10  HOH HOH A . 
E 5 HOH 72  572 90  HOH HOH A . 
E 5 HOH 73  573 109 HOH HOH A . 
E 5 HOH 74  574 88  HOH HOH A . 
E 5 HOH 75  575 59  HOH HOH A . 
E 5 HOH 76  576 2   HOH HOH A . 
E 5 HOH 77  577 56  HOH HOH A . 
E 5 HOH 78  578 3   HOH HOH A . 
E 5 HOH 79  579 96  HOH HOH A . 
E 5 HOH 80  580 49  HOH HOH A . 
E 5 HOH 81  581 37  HOH HOH A . 
E 5 HOH 82  582 115 HOH HOH A . 
E 5 HOH 83  583 24  HOH HOH A . 
E 5 HOH 84  584 33  HOH HOH A . 
E 5 HOH 85  585 98  HOH HOH A . 
E 5 HOH 86  586 11  HOH HOH A . 
E 5 HOH 87  587 91  HOH HOH A . 
E 5 HOH 88  588 26  HOH HOH A . 
E 5 HOH 89  589 43  HOH HOH A . 
E 5 HOH 90  590 94  HOH HOH A . 
E 5 HOH 91  591 19  HOH HOH A . 
E 5 HOH 92  592 68  HOH HOH A . 
E 5 HOH 93  593 57  HOH HOH A . 
E 5 HOH 94  594 111 HOH HOH A . 
E 5 HOH 95  595 8   HOH HOH A . 
E 5 HOH 96  596 102 HOH HOH A . 
E 5 HOH 97  597 35  HOH HOH A . 
E 5 HOH 98  598 40  HOH HOH A . 
E 5 HOH 99  599 51  HOH HOH A . 
E 5 HOH 100 600 70  HOH HOH A . 
E 5 HOH 101 601 32  HOH HOH A . 
E 5 HOH 102 602 7   HOH HOH A . 
E 5 HOH 103 603 118 HOH HOH A . 
E 5 HOH 104 604 106 HOH HOH A . 
E 5 HOH 105 605 120 HOH HOH A . 
E 5 HOH 106 606 50  HOH HOH A . 
E 5 HOH 107 607 31  HOH HOH A . 
E 5 HOH 108 608 95  HOH HOH A . 
E 5 HOH 109 609 14  HOH HOH A . 
E 5 HOH 110 610 114 HOH HOH A . 
E 5 HOH 111 611 77  HOH HOH A . 
E 5 HOH 112 612 30  HOH HOH A . 
E 5 HOH 113 613 38  HOH HOH A . 
E 5 HOH 114 614 113 HOH HOH A . 
E 5 HOH 115 615 48  HOH HOH A . 
E 5 HOH 116 616 17  HOH HOH A . 
E 5 HOH 117 617 21  HOH HOH A . 
E 5 HOH 118 618 116 HOH HOH A . 
E 5 HOH 119 619 28  HOH HOH A . 
E 5 HOH 120 620 112 HOH HOH A . 
E 5 HOH 121 621 58  HOH HOH A . 
E 5 HOH 122 622 107 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  ? ? ? 5.8.0238 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J1A 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.239 
_cell.length_a_esd                 ? 
_cell.length_b                     87.413 
_cell.length_b_esd                 ? 
_cell.length_c                     88.959 
_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                         9J1A 
_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                   9J1A 
_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             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.91 
_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              ? 
_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    '1.8M Ammonium Sulfate, 0.1M MES pH 6.5, 0.01M Cobalt Chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-06-08 
_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   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9J1A 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.48 
_reflns.d_resolution_low                               31.19 
_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                                     40754 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.76 
_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                                0.113 
_reflns.pdbx_Rpim_I_all                                0.033 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.108 
_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                                    1.48 
_reflns_shell.d_res_low                                     1.52 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           21079 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2977 
_reflns_shell.percent_possible_obs                          100.0 
_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                               7.1 
_reflns_shell.pdbx_chi_squared                              0.69 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.548 
_reflns_shell.pdbx_Rpim_I_all                               0.575 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.741 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.434 
_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]                            0.01 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.931 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_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                                 9J1A 
_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                            1.48 
_refine.ls_d_res_low                             31.19 
_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                     38671 
_refine.ls_number_reflns_R_free                  2010 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.80 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18537 
_refine.ls_R_factor_R_free                       0.21318 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18386 
_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                       0.069 
_refine.pdbx_overall_ESU_R_Free                  0.072 
_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                             1.685 
_refine.overall_SU_ML                            0.059 
_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                       1.48 
_refine_hist.d_res_low                        31.19 
_refine_hist.number_atoms_solvent             122 
_refine_hist.number_atoms_total               1939 
_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         8 
_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' ? 0.013  0.013  1856 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  1660 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.730  1.632  2529 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.514  1.574  3867 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.663  5.000  236  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.387 23.810 84   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.909 15.000 289  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 20.741 15.000 6    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.081  0.200  255  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  2092 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  374  ? 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' ? 1.795  1.608  947  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.784  1.606  946  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.857  2.407  1182 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.858  2.409  1183 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.026  1.947  908  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.024  1.948  909  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.526  2.775  1348 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.865  19.887 1941 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.851  19.749 1926 ? 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                       1.480 
_refine_ls_shell.d_res_low                        1.518 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             133 
_refine_ls_shell.number_reflns_R_work             2831 
_refine_ls_shell.percent_reflns_obs               99.63 
_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                  0.333 
_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                  0.367 
# 
_struct.entry_id                     9J1A 
_struct.title                        'Structure of ConA without ligand' 
_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        9J1A 
_struct_keywords.text            'Mannose, Lectin, 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 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CONA_CANEN P02866 ? 1 
;ADTIVAVELDTYPNTDIGDPSYPHIGIDIKSVRSKKTAKWNMQNGKVGTAHIIYNSVDKRLSAVVSYPNADSATVSYDVD
LDNVLPEWVRVGLSASTGLYKETNTILSWSFTSKLKSN
;
164 
2 UNP CONA_CANEN P02866 ? 1 
;STHETNALHFMFNQFSKDQKDLILQGDATTGTDGNLELTRVSSNGSPQGSSVGRALFYAPVHIWESSAVVASFEATFTFL
IKSPDSHPADGIAFFISNIDSSIPSGSTGRLLGLFPDAN
;
30  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9J1A A 1   ? 118 ? P02866 164 ? 281 ? 1   118 
2 2 9J1A A 119 ? 237 ? P02866 30  ? 148 ? 119 237 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 11490 ? 
1 MORE         -109  ? 
1 'SSA (A^2)'  32990 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_665 -x+1,-y+1,z -1.0000000000 0.0000000000 0.0000000000 62.2390000000 0.0000000000 -1.0000000000 
0.0000000000 87.4130000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_655 -x+1,y,-z   -1.0000000000 0.0000000000 0.0000000000 62.2390000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000  0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_565 x,-y+1,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 87.4130000000 0.0000000000 0.0000000000 -1.0000000000 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 C MN  . MN ? ? A GLU 8   A MN  402 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
metalc2  metalc ? ? A ASP 10 OD2 ? ? ? 1_555 C MN  . MN ? ? A ASP 10  A MN  402 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc3  metalc ? ? A ASP 10 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 10  A CA  403 1_555 ? ? ? ? ? ? ? 2.448 ? ? 
metalc4  metalc ? ? A ASP 10 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 10  A CA  403 1_555 ? ? ? ? ? ? ? 2.503 ? ? 
metalc5  metalc ? ? A TYR 12 O   ? ? ? 1_555 D CA  . CA ? ? A TYR 12  A CA  403 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc6  metalc ? ? A ASN 14 OD1 ? ? ? 1_555 D CA  . CA ? ? A ASN 14  A CA  403 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc7  metalc ? ? A ASP 19 OD1 ? ? ? 1_555 C MN  . MN ? ? A ASP 19  A MN  402 1_555 ? ? ? ? ? ? ? 2.177 ? ? 
metalc8  metalc ? ? A ASP 19 OD2 ? ? ? 1_555 D CA  . CA ? ? A ASP 19  A CA  403 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc9  metalc ? ? A HIS 24 NE2 ? ? ? 1_555 C MN  . MN ? ? A HIS 24  A MN  402 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc10 metalc ? ? C MN  .  MN  ? ? ? 1_555 E HOH . O  ? ? A MN  402 A HOH 517 1_555 ? ? ? ? ? ? ? 2.139 ? ? 
metalc11 metalc ? ? C MN  .  MN  ? ? ? 1_555 E HOH . O  ? ? A MN  402 A HOH 546 1_555 ? ? ? ? ? ? ? 2.159 ? ? 
metalc12 metalc ? ? D CA  .  CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 540 1_555 ? ? ? ? ? ? ? 2.431 ? ? 
metalc13 metalc ? ? D CA  .  CA  ? ? ? 1_555 E HOH . O  ? ? A CA  403 A HOH 576 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
# 
_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 ? C MN . ? A MN 402 ? 1_555 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 97.2  ? 
2  OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 OD1 ? A ASP 19 ? A ASP 19  ? 1_555 167.8 ? 
3  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 OD1 ? A ASP 19 ? A ASP 19  ? 1_555 94.6  ? 
4  OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 91.7  ? 
5  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 88.9  ? 
6  OD1 ? A ASP 19 ? A ASP 19  ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 91.2  ? 
7  OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 O   ? E HOH .  ? A HOH 517 ? 1_555 86.8  ? 
8  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 O   ? E HOH .  ? A HOH 517 ? 1_555 175.8 ? 
9  OD1 ? A ASP 19 ? A ASP 19  ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 O   ? E HOH .  ? A HOH 517 ? 1_555 81.4  ? 
10 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 O   ? E HOH .  ? A HOH 517 ? 1_555 90.1  ? 
11 OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 O   ? E HOH .  ? A HOH 546 ? 1_555 90.2  ? 
12 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 O   ? E HOH .  ? A HOH 546 ? 1_555 90.1  ? 
13 OD1 ? A ASP 19 ? A ASP 19  ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 O   ? E HOH .  ? A HOH 546 ? 1_555 87.0  ? 
14 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 O   ? E HOH .  ? A HOH 546 ? 1_555 178.0 ? 
15 O   ? E HOH .  ? A HOH 517 ? 1_555 MN ? C MN . ? A MN 402 ? 1_555 O   ? E HOH .  ? A HOH 546 ? 1_555 90.8  ? 
16 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 53.4  ? 
17 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? A TYR 12 ? A TYR 12  ? 1_555 76.6  ? 
18 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? A TYR 12 ? A TYR 12  ? 1_555 111.5 ? 
19 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 149.2 ? 
20 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 157.4 ? 
21 O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 81.9  ? 
22 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 109.9 ? 
23 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 77.2  ? 
24 O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 80.5  ? 
25 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 87.8  ? 
26 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 540 ? 1_555 73.3  ? 
27 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 540 ? 1_555 111.8 ? 
28 O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 540 ? 1_555 90.8  ? 
29 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 540 ? 1_555 85.2  ? 
30 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 540 ? 1_555 169.5 ? 
31 OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 576 ? 1_555 111.0 ? 
32 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 576 ? 1_555 74.0  ? 
33 O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 576 ? 1_555 172.3 ? 
34 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 576 ? 1_555 91.1  ? 
35 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 576 ? 1_555 95.9  ? 
36 O   ? E HOH .  ? A HOH 540 ? 1_555 CA ? D CA . ? A CA 403 ? 1_555 O   ? E HOH .  ? A HOH 576 ? 1_555 92.0  ? 
# 
_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       1.81 
# 
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 ? PHE A 130 ? THR A 123 PHE A 130 
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 LEU A 154 ? GLU A 155 ? LEU A 154 GLU A 155 
AA4 7 THR A 147 ? THR A 148 ? THR A 147 THR A 148 
# 
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 LEU A 9   ? N LEU A 9   O ILE A 210 ? O ILE A 210 
AA1 4 5 O PHE A 213 ? O PHE A 213 N GLY A 92  ? N GLY A 92  
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 LEU A 9   ? N LEU A 9   O ILE A 210 ? O ILE A 210 
AA2 4 5 O PHE A 213 ? O PHE A 213 N GLY A 92  ? N GLY A 92  
AA2 5 6 N VAL A 89  ? N VAL A 89  O VAL A 179 ? O VAL A 179 
AA3 1 2 O TYR A 77  ? O TYR A 77  N LEU A 61  ? N LEU A 61  
AA3 2 3 O VAL A 64  ? O VAL A 64  N HIS A 51  ? N HIS A 51  
AA3 3 4 N ALA A 50  ? N ALA A 50  O PHE A 195 ? O PHE A 195 
AA3 4 5 O VAL A 187 ? O VAL A 187 N LYS A 116 ? N LYS A 116 
AA3 5 6 N TRP A 109 ? N TRP A 109 O PHE A 130 ? O PHE A 130 
AA4 1 2 O TYR A 77  ? O TYR A 77  N LEU A 61  ? N LEU A 61  
AA4 2 3 O VAL A 64  ? O VAL A 64  N HIS A 51  ? N HIS A 51  
AA4 3 4 N ALA A 50  ? N ALA A 50  O PHE A 195 ? O PHE A 195 
AA4 4 5 O VAL A 187 ? O VAL A 187 N LYS A 116 ? N LYS A 116 
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                   9J1A 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     21 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -75.90 
_pdbx_validate_torsion.psi             24.10 
# 
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 
GOL C1   C  N N 124 
GOL O1   O  N N 125 
GOL C2   C  N N 126 
GOL O2   O  N N 127 
GOL C3   C  N N 128 
GOL O3   O  N N 129 
GOL H11  H  N N 130 
GOL H12  H  N N 131 
GOL HO1  H  N N 132 
GOL H2   H  N N 133 
GOL HO2  H  N N 134 
GOL H31  H  N N 135 
GOL H32  H  N N 136 
GOL HO3  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MN  MN   MN N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SER N    N  N N 292 
SER CA   C  N S 293 
SER C    C  N N 294 
SER O    O  N N 295 
SER CB   C  N N 296 
SER OG   O  N N 297 
SER OXT  O  N N 298 
SER H    H  N N 299 
SER H2   H  N N 300 
SER HA   H  N N 301 
SER HB2  H  N N 302 
SER HB3  H  N N 303 
SER HG   H  N N 304 
SER HXT  H  N N 305 
THR N    N  N N 306 
THR CA   C  N S 307 
THR C    C  N N 308 
THR O    O  N N 309 
THR CB   C  N R 310 
THR OG1  O  N N 311 
THR CG2  C  N N 312 
THR OXT  O  N N 313 
THR H    H  N N 314 
THR H2   H  N N 315 
THR HA   H  N N 316 
THR HB   H  N N 317 
THR HG1  H  N N 318 
THR HG21 H  N N 319 
THR HG22 H  N N 320 
THR HG23 H  N N 321 
THR HXT  H  N N 322 
TRP N    N  N N 323 
TRP CA   C  N S 324 
TRP C    C  N N 325 
TRP O    O  N N 326 
TRP CB   C  N N 327 
TRP CG   C  Y N 328 
TRP CD1  C  Y N 329 
TRP CD2  C  Y N 330 
TRP NE1  N  Y N 331 
TRP CE2  C  Y N 332 
TRP CE3  C  Y N 333 
TRP CZ2  C  Y N 334 
TRP CZ3  C  Y N 335 
TRP CH2  C  Y N 336 
TRP OXT  O  N N 337 
TRP H    H  N N 338 
TRP H2   H  N N 339 
TRP HA   H  N N 340 
TRP HB2  H  N N 341 
TRP HB3  H  N N 342 
TRP HD1  H  N N 343 
TRP HE1  H  N N 344 
TRP HE3  H  N N 345 
TRP HZ2  H  N N 346 
TRP HZ3  H  N N 347 
TRP HH2  H  N N 348 
TRP HXT  H  N N 349 
TYR N    N  N N 350 
TYR CA   C  N S 351 
TYR C    C  N N 352 
TYR O    O  N N 353 
TYR CB   C  N N 354 
TYR CG   C  Y N 355 
TYR CD1  C  Y N 356 
TYR CD2  C  Y N 357 
TYR CE1  C  Y N 358 
TYR CE2  C  Y N 359 
TYR CZ   C  Y N 360 
TYR OH   O  N N 361 
TYR OXT  O  N N 362 
TYR H    H  N N 363 
TYR H2   H  N N 364 
TYR HA   H  N N 365 
TYR HB2  H  N N 366 
TYR HB3  H  N N 367 
TYR HD1  H  N N 368 
TYR HD2  H  N N 369 
TYR HE1  H  N N 370 
TYR HE2  H  N N 371 
TYR HH   H  N N 372 
TYR HXT  H  N N 373 
VAL N    N  N N 374 
VAL CA   C  N S 375 
VAL C    C  N N 376 
VAL O    O  N N 377 
VAL CB   C  N N 378 
VAL CG1  C  N N 379 
VAL CG2  C  N N 380 
VAL OXT  O  N N 381 
VAL H    H  N N 382 
VAL H2   H  N N 383 
VAL HA   H  N N 384 
VAL HB   H  N N 385 
VAL HG11 H  N N 386 
VAL HG12 H  N N 387 
VAL HG13 H  N N 388 
VAL HG21 H  N N 389 
VAL HG22 H  N N 390 
VAL HG23 H  N N 391 
VAL HXT  H  N N 392 
# 
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 
GOL C1  O1   sing N N 116 
GOL C1  C2   sing N N 117 
GOL C1  H11  sing N N 118 
GOL C1  H12  sing N N 119 
GOL O1  HO1  sing N N 120 
GOL C2  O2   sing N N 121 
GOL C2  C3   sing N N 122 
GOL C2  H2   sing N N 123 
GOL O2  HO2  sing N N 124 
GOL C3  O3   sing N N 125 
GOL C3  H31  sing N N 126 
GOL C3  H32  sing N N 127 
GOL O3  HO3  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_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   4P9W 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9J1A 
_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]   0.016067 
_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]   0.011440 
_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]   0.011241 
_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 
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   ? 1.086  22.461 2.765   1.00 29.39 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 1.864  23.188 3.809   1.00 28.38 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 3.030  23.958 3.163   1.00 26.62 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 3.343  23.736 2.003   1.00 27.08 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 2.390  22.189 4.818   1.00 30.17 ? 1   ALA A CB  1 
ATOM   6    N  N   . ASP A 1 2   ? 3.707  24.792 3.930   1.00 23.27 ? 2   ASP A N   1 
ATOM   7    C  CA  . ASP A 1 2   ? 4.907  25.509 3.429   1.00 22.14 ? 2   ASP A CA  1 
ATOM   8    C  C   . ASP A 1 2   ? 6.003  24.488 3.110   1.00 20.66 ? 2   ASP A C   1 
ATOM   9    O  O   . ASP A 1 2   ? 5.958  23.318 3.580   1.00 20.11 ? 2   ASP A O   1 
ATOM   10   C  CB  . ASP A 1 2   ? 5.390  26.502 4.490   1.00 21.97 ? 2   ASP A CB  1 
ATOM   11   C  CG  . ASP A 1 2   ? 4.440  27.662 4.703   1.00 24.82 ? 2   ASP A CG  1 
ATOM   12   O  OD1 . ASP A 1 2   ? 3.666  28.005 3.749   1.00 22.25 ? 2   ASP A OD1 1 
ATOM   13   O  OD2 . ASP A 1 2   ? 4.509  28.256 5.828   1.00 23.66 ? 2   ASP A OD2 1 
ATOM   14   N  N   . THR A 1 3   ? 7.023  24.936 2.389   1.00 17.51 ? 3   THR A N   1 
ATOM   15   C  CA  . THR A 1 3   ? 8.272  24.177 2.203   1.00 16.66 ? 3   THR A CA  1 
ATOM   16   C  C   . THR A 1 3   ? 9.324  24.856 3.069   1.00 15.26 ? 3   THR A C   1 
ATOM   17   O  O   . THR A 1 3   ? 9.548  26.083 2.879   1.00 16.93 ? 3   THR A O   1 
ATOM   18   C  CB  . THR A 1 3   ? 8.723  24.170 0.743   1.00 18.45 ? 3   THR A CB  1 
ATOM   19   O  OG1 . THR A 1 3   ? 7.612  23.667 -0.002  1.00 22.18 ? 3   THR A OG1 1 
ATOM   20   C  CG2 . THR A 1 3   ? 9.961  23.347 0.529   1.00 19.17 ? 3   THR A CG2 1 
ATOM   21   N  N   . ILE A 1 4   ? 9.973  24.092 3.935   1.00 15.21 ? 4   ILE A N   1 
ATOM   22   C  CA  . ILE A 1 4   ? 10.980 24.652 4.877   1.00 15.23 ? 4   ILE A CA  1 
ATOM   23   C  C   . ILE A 1 4   ? 12.287 23.903 4.797   1.00 13.23 ? 4   ILE A C   1 
ATOM   24   O  O   . ILE A 1 4   ? 12.314 22.662 4.835   1.00 13.59 ? 4   ILE A O   1 
ATOM   25   C  CB  . ILE A 1 4   ? 10.443 24.572 6.309   1.00 16.37 ? 4   ILE A CB  1 
ATOM   26   C  CG1 . ILE A 1 4   ? 9.158  25.392 6.451   1.00 18.48 ? 4   ILE A CG1 1 
ATOM   27   C  CG2 . ILE A 1 4   ? 11.541 24.984 7.287   1.00 17.43 ? 4   ILE A CG2 1 
ATOM   28   C  CD1 . ILE A 1 4   ? 9.348  26.891 6.385   1.00 20.24 ? 4   ILE A CD1 1 
ATOM   29   N  N   . VAL A 1 5   ? 13.373 24.641 4.682   1.00 11.61 ? 5   VAL A N   1 
ATOM   30   C  CA  . VAL A 1 5   ? 14.765 24.202 4.913   1.00 11.53 ? 5   VAL A CA  1 
ATOM   31   C  C   . VAL A 1 5   ? 15.266 25.005 6.103   1.00 12.10 ? 5   VAL A C   1 
ATOM   32   O  O   . VAL A 1 5   ? 15.172 26.242 6.082   1.00 11.35 ? 5   VAL A O   1 
ATOM   33   C  CB  . VAL A 1 5   ? 15.640 24.436 3.683   1.00 11.96 ? 5   VAL A CB  1 
ATOM   34   C  CG1 . VAL A 1 5   ? 17.110 24.251 3.981   1.00 12.53 ? 5   VAL A CG1 1 
ATOM   35   C  CG2 . VAL A 1 5   ? 15.216 23.476 2.571   1.00 12.11 ? 5   VAL A CG2 1 
ATOM   36   N  N   . ALA A 1 6   ? 15.833 24.386 7.120   1.00 10.87 ? 6   ALA A N   1 
ATOM   37   C  CA  . ALA A 1 6   ? 16.235 25.159 8.315   1.00 10.78 ? 6   ALA A CA  1 
ATOM   38   C  C   . ALA A 1 6   ? 17.510 24.591 8.930   1.00 10.88 ? 6   ALA A C   1 
ATOM   39   O  O   . ALA A 1 6   ? 17.774 23.393 8.802   1.00 11.03 ? 6   ALA A O   1 
ATOM   40   C  CB  . ALA A 1 6   ? 15.136 25.184 9.324   1.00 11.33 ? 6   ALA A CB  1 
ATOM   41   N  N   . VAL A 1 7   ? 18.247 25.457 9.596   1.00 9.72  ? 7   VAL A N   1 
ATOM   42   C  CA  . VAL A 1 7   ? 19.299 25.027 10.540  1.00 10.03 ? 7   VAL A CA  1 
ATOM   43   C  C   . VAL A 1 7   ? 18.743 25.314 11.933  1.00 10.40 ? 7   VAL A C   1 
ATOM   44   O  O   . VAL A 1 7   ? 18.409 26.482 12.224  1.00 11.67 ? 7   VAL A O   1 
ATOM   45   C  CB  . VAL A 1 7   ? 20.632 25.741 10.281  1.00 10.71 ? 7   VAL A CB  1 
ATOM   46   C  CG1 . VAL A 1 7   ? 21.643 25.444 11.362  1.00 11.89 ? 7   VAL A CG1 1 
ATOM   47   C  CG2 . VAL A 1 7   ? 21.187 25.371 8.926   1.00 11.83 ? 7   VAL A CG2 1 
ATOM   48   N  N   . GLU A 1 8   ? 18.584 24.266 12.728  1.00 10.66 ? 8   GLU A N   1 
ATOM   49   C  CA  . GLU A 1 8   ? 18.017 24.439 14.088  1.00 11.16 ? 8   GLU A CA  1 
ATOM   50   C  C   . GLU A 1 8   ? 19.143 24.479 15.116  1.00 11.60 ? 8   GLU A C   1 
ATOM   51   O  O   . GLU A 1 8   ? 20.100 23.635 15.082  1.00 12.01 ? 8   GLU A O   1 
ATOM   52   C  CB  . GLU A 1 8   ? 16.964 23.368 14.386  1.00 11.30 ? 8   GLU A CB  1 
ATOM   53   C  CG  . GLU A 1 8   ? 17.465 21.927 14.303  1.00 12.45 ? 8   GLU A CG  1 
ATOM   54   C  CD  . GLU A 1 8   ? 16.522 20.917 14.916  1.00 11.90 ? 8   GLU A CD  1 
ATOM   55   O  OE1 . GLU A 1 8   ? 15.376 20.789 14.431  1.00 12.92 ? 8   GLU A OE1 1 
ATOM   56   O  OE2 . GLU A 1 8   ? 16.998 20.205 15.858  1.00 11.35 ? 8   GLU A OE2 1 
ATOM   57   N  N   . LEU A 1 9   ? 18.962 25.400 16.068  1.00 10.19 ? 9   LEU A N   1 
ATOM   58   C  CA  . LEU A 1 9   ? 19.722 25.425 17.337  1.00 11.17 ? 9   LEU A CA  1 
ATOM   59   C  C   . LEU A 1 9   ? 18.714 24.931 18.381  1.00 10.52 ? 9   LEU A C   1 
ATOM   60   O  O   . LEU A 1 9   ? 17.892 25.732 18.887  1.00 10.38 ? 9   LEU A O   1 
ATOM   61   C  CB  . LEU A 1 9   ? 20.278 26.819 17.645  1.00 11.59 ? 9   LEU A CB  1 
ATOM   62   C  CG  . LEU A 1 9   ? 21.503 27.293 16.860  1.00 13.94 ? 9   LEU A CG  1 
ATOM   63   C  CD1 . LEU A 1 9   ? 21.398 27.088 15.361  1.00 16.23 ? 9   LEU A CD1 1 
ATOM   64   C  CD2 . LEU A 1 9   ? 21.776 28.740 17.171  1.00 13.56 ? 9   LEU A CD2 1 
ATOM   65   N  N   . ASP A 1 10  ? 18.708 23.634 18.625  1.00 10.46 ? 10  ASP A N   1 
ATOM   66   C  CA  . ASP A 1 10  ? 17.619 22.941 19.366  1.00 10.31 ? 10  ASP A CA  1 
ATOM   67   C  C   . ASP A 1 10  ? 18.055 22.736 20.820  1.00 10.27 ? 10  ASP A C   1 
ATOM   68   O  O   . ASP A 1 10  ? 19.007 21.985 21.087  1.00 10.30 ? 10  ASP A O   1 
ATOM   69   C  CB  . ASP A 1 10  ? 17.281 21.625 18.684  1.00 11.48 ? 10  ASP A CB  1 
ATOM   70   C  CG  . ASP A 1 10  ? 16.066 20.914 19.265  1.00 12.04 ? 10  ASP A CG  1 
ATOM   71   O  OD1 . ASP A 1 10  ? 15.700 21.265 20.410  1.00 12.96 ? 10  ASP A OD1 1 
ATOM   72   O  OD2 . ASP A 1 10  ? 15.538 19.972 18.607  1.00 10.90 ? 10  ASP A OD2 1 
ATOM   73   N  N   . THR A 1 11  ? 17.448 23.481 21.726  1.00 10.72 ? 11  THR A N   1 
ATOM   74   C  CA  . THR A 1 11  ? 17.896 23.550 23.125  1.00 11.03 ? 11  THR A CA  1 
ATOM   75   C  C   . THR A 1 11  ? 17.290 22.444 23.972  1.00 11.63 ? 11  THR A C   1 
ATOM   76   O  O   . THR A 1 11  ? 17.795 22.254 25.101  1.00 13.05 ? 11  THR A O   1 
ATOM   77   C  CB  . THR A 1 11  ? 17.616 24.908 23.776  1.00 11.20 ? 11  THR A CB  1 
ATOM   78   O  OG1 . THR A 1 11  ? 16.209 25.135 23.621  1.00 11.26 ? 11  THR A OG1 1 
ATOM   79   C  CG2 . THR A 1 11  ? 18.389 26.039 23.135  1.00 11.89 ? 11  THR A CG2 1 
ATOM   80   N  N   . TYR A 1 12  ? 16.211 21.805 23.515  1.00 11.45 ? 12  TYR A N   1 
ATOM   81   C  CA  . TYR A 1 12  ? 15.505 20.793 24.337  1.00 11.67 ? 12  TYR A CA  1 
ATOM   82   C  C   . TYR A 1 12  ? 15.404 19.458 23.609  1.00 12.33 ? 12  TYR A C   1 
ATOM   83   O  O   . TYR A 1 12  ? 14.843 19.336 22.528  1.00 11.74 ? 12  TYR A O   1 
ATOM   84   C  CB  . TYR A 1 12  ? 14.123 21.315 24.699  1.00 11.93 ? 12  TYR A CB  1 
ATOM   85   C  CG  . TYR A 1 12  ? 13.447 20.425 25.720  1.00 11.64 ? 12  TYR A CG  1 
ATOM   86   C  CD1 . TYR A 1 12  ? 12.867 19.232 25.353  1.00 12.30 ? 12  TYR A CD1 1 
ATOM   87   C  CD2 . TYR A 1 12  ? 13.433 20.792 27.044  1.00 13.25 ? 12  TYR A CD2 1 
ATOM   88   C  CE1 . TYR A 1 12  ? 12.266 18.405 26.300  1.00 13.23 ? 12  TYR A CE1 1 
ATOM   89   C  CE2 . TYR A 1 12  ? 12.859 19.958 28.000  1.00 12.12 ? 12  TYR A CE2 1 
ATOM   90   C  CZ  . TYR A 1 12  ? 12.270 18.769 27.618  1.00 12.58 ? 12  TYR A CZ  1 
ATOM   91   O  OH  . TYR A 1 12  ? 11.673 17.942 28.550  1.00 15.00 ? 12  TYR A OH  1 
ATOM   92   N  N   . PRO A 1 13  ? 15.896 18.360 24.206  1.00 13.25 ? 13  PRO A N   1 
ATOM   93   C  CA  . PRO A 1 13  ? 15.879 17.052 23.549  1.00 15.08 ? 13  PRO A CA  1 
ATOM   94   C  C   . PRO A 1 13  ? 14.504 16.389 23.631  1.00 16.50 ? 13  PRO A C   1 
ATOM   95   O  O   . PRO A 1 13  ? 14.042 16.004 24.713  1.00 18.12 ? 13  PRO A O   1 
ATOM   96   C  CB  . PRO A 1 13  ? 16.948 16.251 24.314  1.00 15.39 ? 13  PRO A CB  1 
ATOM   97   C  CG  . PRO A 1 13  ? 16.950 16.842 25.709  1.00 16.91 ? 13  PRO A CG  1 
ATOM   98   C  CD  . PRO A 1 13  ? 16.514 18.294 25.536  1.00 16.11 ? 13  PRO A CD  1 
ATOM   99   N  N   . ASN A 1 14  ? 13.815 16.347 22.518  1.00 13.19 ? 14  ASN A N   1 
ATOM   100  C  CA  . ASN A 1 14  ? 12.558 15.577 22.324  1.00 13.32 ? 14  ASN A CA  1 
ATOM   101  C  C   . ASN A 1 14  ? 12.929 14.225 21.671  1.00 15.45 ? 14  ASN A C   1 
ATOM   102  O  O   . ASN A 1 14  ? 12.844 14.105 20.443  1.00 15.19 ? 14  ASN A O   1 
ATOM   103  C  CB  . ASN A 1 14  ? 11.550 16.373 21.503  1.00 14.53 ? 14  ASN A CB  1 
ATOM   104  C  CG  . ASN A 1 14  ? 11.372 17.781 22.026  1.00 14.77 ? 14  ASN A CG  1 
ATOM   105  O  OD1 . ASN A 1 14  ? 11.965 18.756 21.522  1.00 14.90 ? 14  ASN A OD1 1 
ATOM   106  N  ND2 . ASN A 1 14  ? 10.526 17.945 23.022  1.00 14.10 ? 14  ASN A ND2 1 
ATOM   107  N  N   . THR A 1 15  ? 13.302 13.236 22.472  1.00 17.86 ? 15  THR A N   1 
ATOM   108  C  CA  . THR A 1 15  ? 13.864 11.962 21.968  1.00 19.65 ? 15  THR A CA  1 
ATOM   109  C  C   . THR A 1 15  ? 12.772 11.146 21.269  1.00 22.41 ? 15  THR A C   1 
ATOM   110  O  O   . THR A 1 15  ? 13.127 10.384 20.322  1.00 25.85 ? 15  THR A O   1 
ATOM   111  C  CB  . THR A 1 15  ? 14.570 11.214 23.095  1.00 21.74 ? 15  THR A CB  1 
ATOM   112  O  OG1 . THR A 1 15  ? 13.592 10.954 24.101  1.00 23.79 ? 15  THR A OG1 1 
ATOM   113  C  CG2 . THR A 1 15  ? 15.760 11.978 23.616  1.00 20.90 ? 15  THR A CG2 1 
ATOM   114  N  N   . ASP A 1 16  ? 11.499 11.402 21.585  1.00 22.38 ? 16  ASP A N   1 
ATOM   115  C  CA  . ASP A 1 16  ? 10.326 10.755 20.927  1.00 27.40 ? 16  ASP A CA  1 
ATOM   116  C  C   . ASP A 1 16  ? 10.198 11.178 19.463  1.00 27.82 ? 16  ASP A C   1 
ATOM   117  O  O   . ASP A 1 16  ? 9.617  10.386 18.707  1.00 31.27 ? 16  ASP A O   1 
ATOM   118  C  CB  . ASP A 1 16  ? 9.017  11.014 21.692  1.00 30.57 ? 16  ASP A CB  1 
ATOM   119  C  CG  . ASP A 1 16  ? 8.788  12.462 22.123  1.00 32.61 ? 16  ASP A CG  1 
ATOM   120  O  OD1 . ASP A 1 16  ? 9.785  13.215 22.306  1.00 31.88 ? 16  ASP A OD1 1 
ATOM   121  O  OD2 . ASP A 1 16  ? 7.624  12.825 22.334  1.00 32.74 ? 16  ASP A OD2 1 
ATOM   122  N  N   . ILE A 1 17  ? 10.688 12.362 19.037  1.00 22.03 ? 17  ILE A N   1 
ATOM   123  C  CA  . ILE A 1 17  ? 10.664 12.757 17.596  1.00 21.38 ? 17  ILE A CA  1 
ATOM   124  C  C   . ILE A 1 17  ? 12.098 12.744 17.034  1.00 18.69 ? 17  ILE A C   1 
ATOM   125  O  O   . ILE A 1 17  ? 12.335 13.496 16.146  1.00 20.80 ? 17  ILE A O   1 
ATOM   126  C  CB  . ILE A 1 17  ? 9.958  14.098 17.381  1.00 20.87 ? 17  ILE A CB  1 
ATOM   127  C  CG1 . ILE A 1 17  ? 10.653 15.259 18.101  1.00 19.87 ? 17  ILE A CG1 1 
ATOM   128  C  CG2 . ILE A 1 17  ? 8.496  13.973 17.793  1.00 21.92 ? 17  ILE A CG2 1 
ATOM   129  C  CD1 . ILE A 1 17  ? 10.263 16.612 17.612  1.00 20.40 ? 17  ILE A CD1 1 
ATOM   130  N  N   . GLY A 1 18  ? 12.995 11.912 17.567  1.00 20.47 ? 18  GLY A N   1 
ATOM   131  C  CA  . GLY A 1 18  ? 14.320 11.659 16.945  1.00 19.89 ? 18  GLY A CA  1 
ATOM   132  C  C   . GLY A 1 18  ? 15.422 12.633 17.351  1.00 20.41 ? 18  GLY A C   1 
ATOM   133  O  O   . GLY A 1 18  ? 16.555 12.471 16.875  1.00 19.60 ? 18  GLY A O   1 
ATOM   134  N  N   . ASP A 1 19  ? 15.166 13.601 18.234  1.00 17.55 ? 19  ASP A N   1 
ATOM   135  C  CA  . ASP A 1 19  ? 16.297 14.414 18.758  1.00 14.79 ? 19  ASP A CA  1 
ATOM   136  C  C   . ASP A 1 19  ? 17.280 13.501 19.462  1.00 15.06 ? 19  ASP A C   1 
ATOM   137  O  O   . ASP A 1 19  ? 16.843 12.599 20.172  1.00 17.07 ? 19  ASP A O   1 
ATOM   138  C  CB  . ASP A 1 19  ? 15.872 15.434 19.814  1.00 13.80 ? 19  ASP A CB  1 
ATOM   139  C  CG  . ASP A 1 19  ? 15.242 16.710 19.271  1.00 14.56 ? 19  ASP A CG  1 
ATOM   140  O  OD1 . ASP A 1 19  ? 15.327 16.930 18.020  1.00 12.80 ? 19  ASP A OD1 1 
ATOM   141  O  OD2 . ASP A 1 19  ? 14.647 17.430 20.089  1.00 13.66 ? 19  ASP A OD2 1 
ATOM   142  N  N   . PRO A 1 20  ? 18.593 13.793 19.451  1.00 15.25 ? 20  PRO A N   1 
ATOM   143  C  CA  . PRO A 1 20  ? 19.506 13.123 20.376  1.00 17.55 ? 20  PRO A CA  1 
ATOM   144  C  C   . PRO A 1 20  ? 19.245 13.603 21.810  1.00 19.24 ? 20  PRO A C   1 
ATOM   145  O  O   . PRO A 1 20  ? 18.476 14.546 22.005  1.00 17.71 ? 20  PRO A O   1 
ATOM   146  C  CB  . PRO A 1 20  ? 20.860 13.517 19.778  1.00 18.34 ? 20  PRO A CB  1 
ATOM   147  C  CG  . PRO A 1 20  ? 20.632 14.921 19.262  1.00 16.86 ? 20  PRO A CG  1 
ATOM   148  C  CD  . PRO A 1 20  ? 19.242 14.888 18.675  1.00 15.70 ? 20  PRO A CD  1 
ATOM   149  N  N   . SER A 1 21  ? 19.858 12.948 22.801  1.00 19.15 ? 21  SER A N   1 
ATOM   150  C  CA  . SER A 1 21  ? 19.592 13.143 24.245  1.00 20.51 ? 21  SER A CA  1 
ATOM   151  C  C   . SER A 1 21  ? 20.212 14.434 24.803  1.00 19.48 ? 21  SER A C   1 
ATOM   152  O  O   . SER A 1 21  ? 20.532 14.479 25.986  1.00 24.30 ? 21  SER A O   1 
ATOM   153  C  CB  . SER A 1 21  ? 20.150 11.951 24.979  1.00 24.15 ? 21  SER A CB  1 
ATOM   154  O  OG  . SER A 1 21  ? 19.440 10.825 24.573  1.00 30.98 ? 21  SER A OG  1 
ATOM   155  N  N   . TYR A 1 22  ? 20.460 15.434 23.964  1.00 16.45 ? 22  TYR A N   1 
ATOM   156  C  CA  . TYR A 1 22  ? 21.267 16.614 24.349  1.00 15.52 ? 22  TYR A CA  1 
ATOM   157  C  C   . TYR A 1 22  ? 20.870 17.757 23.413  1.00 14.07 ? 22  TYR A C   1 
ATOM   158  O  O   . TYR A 1 22  ? 20.388 17.509 22.300  1.00 14.62 ? 22  TYR A O   1 
ATOM   159  C  CB  . TYR A 1 22  ? 22.786 16.343 24.335  1.00 16.68 ? 22  TYR A CB  1 
ATOM   160  C  CG  . TYR A 1 22  ? 23.294 15.496 23.191  1.00 20.19 ? 22  TYR A CG  1 
ATOM   161  C  CD1 . TYR A 1 22  ? 23.413 16.028 21.915  1.00 18.77 ? 22  TYR A CD1 1 
ATOM   162  C  CD2 . TYR A 1 22  ? 23.671 14.155 23.372  1.00 21.69 ? 22  TYR A CD2 1 
ATOM   163  C  CE1 . TYR A 1 22  ? 23.834 15.274 20.828  1.00 18.74 ? 22  TYR A CE1 1 
ATOM   164  C  CE2 . TYR A 1 22  ? 24.086 13.383 22.281  1.00 23.70 ? 22  TYR A CE2 1 
ATOM   165  C  CZ  . TYR A 1 22  ? 24.192 13.941 21.011  1.00 23.91 ? 22  TYR A CZ  1 
ATOM   166  O  OH  . TYR A 1 22  ? 24.580 13.252 19.890  1.00 27.74 ? 22  TYR A OH  1 
ATOM   167  N  N   . PRO A 1 23  ? 21.130 19.003 23.847  1.00 13.38 ? 23  PRO A N   1 
ATOM   168  C  CA  . PRO A 1 23  ? 21.038 20.158 22.944  1.00 12.87 ? 23  PRO A CA  1 
ATOM   169  C  C   . PRO A 1 23  ? 21.928 19.881 21.727  1.00 11.52 ? 23  PRO A C   1 
ATOM   170  O  O   . PRO A 1 23  ? 23.002 19.245 21.826  1.00 11.78 ? 23  PRO A O   1 
ATOM   171  C  CB  . PRO A 1 23  ? 21.497 21.344 23.795  1.00 14.49 ? 23  PRO A CB  1 
ATOM   172  C  CG  . PRO A 1 23  ? 21.191 20.885 25.229  1.00 14.77 ? 23  PRO A CG  1 
ATOM   173  C  CD  . PRO A 1 23  ? 21.469 19.408 25.230  1.00 15.32 ? 23  PRO A CD  1 
ATOM   174  N  N   . HIS A 1 24  ? 21.500 20.341 20.567  1.00 10.93 ? 24  HIS A N   1 
ATOM   175  C  CA  . HIS A 1 24  ? 22.126 19.944 19.289  1.00 11.59 ? 24  HIS A CA  1 
ATOM   176  C  C   . HIS A 1 24  ? 21.822 20.996 18.234  1.00 12.85 ? 24  HIS A C   1 
ATOM   177  O  O   . HIS A 1 24  ? 20.893 21.765 18.390  1.00 11.58 ? 24  HIS A O   1 
ATOM   178  C  CB  . HIS A 1 24  ? 21.614 18.576 18.833  1.00 11.58 ? 24  HIS A CB  1 
ATOM   179  C  CG  . HIS A 1 24  ? 20.134 18.481 18.749  1.00 10.93 ? 24  HIS A CG  1 
ATOM   180  N  ND1 . HIS A 1 24  ? 19.330 18.292 19.878  1.00 11.36 ? 24  HIS A ND1 1 
ATOM   181  C  CD2 . HIS A 1 24  ? 19.314 18.535 17.705  1.00 11.63 ? 24  HIS A CD2 1 
ATOM   182  C  CE1 . HIS A 1 24  ? 18.078 18.279 19.462  1.00 10.39 ? 24  HIS A CE1 1 
ATOM   183  N  NE2 . HIS A 1 24  ? 18.012 18.455 18.151  1.00 11.98 ? 24  HIS A NE2 1 
ATOM   184  N  N   . ILE A 1 25  ? 22.680 21.026 17.230  1.00 12.05 ? 25  ILE A N   1 
ATOM   185  C  CA  . ILE A 1 25  ? 22.420 21.751 15.983  1.00 12.52 ? 25  ILE A CA  1 
ATOM   186  C  C   . ILE A 1 25  ? 22.026 20.718 14.926  1.00 13.79 ? 25  ILE A C   1 
ATOM   187  O  O   . ILE A 1 25  ? 22.525 19.565 14.976  1.00 14.36 ? 25  ILE A O   1 
ATOM   188  C  CB  . ILE A 1 25  ? 23.628 22.576 15.618  1.00 13.23 ? 25  ILE A CB  1 
ATOM   189  C  CG1 . ILE A 1 25  ? 24.875 21.757 15.351  1.00 14.86 ? 25  ILE A CG1 1 
ATOM   190  C  CG2 . ILE A 1 25  ? 23.829 23.568 16.710  1.00 16.69 ? 25  ILE A CG2 1 
ATOM   191  C  CD1 . ILE A 1 25  ? 25.924 22.621 14.745  1.00 18.19 ? 25  ILE A CD1 1 
ATOM   192  N  N   . GLY A 1 26  ? 21.094 21.073 14.069  1.00 11.98 ? 26  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 26  ? 20.576 20.135 13.085  1.00 12.70 ? 26  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 26  ? 20.252 20.797 11.782  1.00 11.96 ? 26  GLY A C   1 
ATOM   195  O  O   . GLY A 1 26  ? 20.026 22.002 11.726  1.00 12.59 ? 26  GLY A O   1 
ATOM   196  N  N   . ILE A 1 27  ? 20.183 19.978 10.759  1.00 12.66 ? 27  ILE A N   1 
ATOM   197  C  CA  . ILE A 1 27  ? 19.752 20.416 9.406   1.00 12.88 ? 27  ILE A CA  1 
ATOM   198  C  C   . ILE A 1 27  ? 18.437 19.748 9.149   1.00 12.55 ? 27  ILE A C   1 
ATOM   199  O  O   . ILE A 1 27  ? 18.365 18.505 9.239   1.00 13.62 ? 27  ILE A O   1 
ATOM   200  C  CB  . ILE A 1 27  ? 20.820 20.118 8.362   1.00 14.40 ? 27  ILE A CB  1 
ATOM   201  C  CG1 . ILE A 1 27  ? 22.033 21.024 8.612   1.00 16.53 ? 27  ILE A CG1 1 
ATOM   202  C  CG2 . ILE A 1 27  ? 20.247 20.285 6.963   1.00 14.58 ? 27  ILE A CG2 1 
ATOM   203  C  CD1 . ILE A 1 27  ? 23.227 20.623 7.910   1.00 18.57 ? 27  ILE A CD1 1 
ATOM   204  N  N   . ASP A 1 28  ? 17.424 20.554 8.923   1.00 11.84 ? 28  ASP A N   1 
ATOM   205  C  CA  . ASP A 1 28  ? 16.011 20.158 8.748   1.00 11.86 ? 28  ASP A CA  1 
ATOM   206  C  C   . ASP A 1 28  ? 15.618 20.386 7.291   1.00 13.14 ? 28  ASP A C   1 
ATOM   207  O  O   . ASP A 1 28  ? 15.603 21.537 6.848   1.00 12.12 ? 28  ASP A O   1 
ATOM   208  C  CB  . ASP A 1 28  ? 15.109 20.915 9.725   1.00 12.85 ? 28  ASP A CB  1 
ATOM   209  C  CG  . ASP A 1 28  ? 15.414 20.622 11.183  1.00 14.05 ? 28  ASP A CG  1 
ATOM   210  O  OD1 . ASP A 1 28  ? 16.355 19.821 11.459  1.00 15.03 ? 28  ASP A OD1 1 
ATOM   211  O  OD2 . ASP A 1 28  ? 14.840 21.371 12.031  1.00 12.95 ? 28  ASP A OD2 1 
ATOM   212  N  N   . ILE A 1 29  ? 15.303 19.306 6.581   1.00 12.81 ? 29  ILE A N   1 
ATOM   213  C  CA  . ILE A 1 29  ? 14.812 19.410 5.173   1.00 13.51 ? 29  ILE A CA  1 
ATOM   214  C  C   . ILE A 1 29  ? 13.365 18.880 5.149   1.00 14.99 ? 29  ILE A C   1 
ATOM   215  O  O   . ILE A 1 29  ? 13.151 17.602 5.215   1.00 15.64 ? 29  ILE A O   1 
ATOM   216  C  CB  . ILE A 1 29  ? 15.739 18.630 4.225   1.00 12.25 ? 29  ILE A CB  1 
ATOM   217  C  CG1 . ILE A 1 29  ? 17.223 18.959 4.417   1.00 14.11 ? 29  ILE A CG1 1 
ATOM   218  C  CG2 . ILE A 1 29  ? 15.343 18.824 2.784   1.00 11.56 ? 29  ILE A CG2 1 
ATOM   219  C  CD1 . ILE A 1 29  ? 17.611 20.359 4.023   1.00 14.44 ? 29  ILE A CD1 1 
ATOM   220  N  N   . LYS A 1 30  ? 12.409 19.807 5.232   1.00 14.90 ? 30  LYS A N   1 
ATOM   221  C  CA  . LYS A 1 30  ? 10.956 19.553 5.096   1.00 16.10 ? 30  LYS A CA  1 
ATOM   222  C  C   . LYS A 1 30  ? 10.483 18.683 6.266   1.00 17.55 ? 30  LYS A C   1 
ATOM   223  O  O   . LYS A 1 30  ? 9.385  18.161 6.178   1.00 19.48 ? 30  LYS A O   1 
ATOM   224  C  CB  . LYS A 1 30  ? 10.648 18.920 3.737   1.00 18.50 ? 30  LYS A CB  1 
ATOM   225  C  CG  . LYS A 1 30  ? 10.900 19.832 2.554   1.00 20.46 ? 30  LYS A CG  1 
ATOM   226  C  CD  . LYS A 1 30  ? 10.891 19.143 1.194   1.00 23.55 ? 30  LYS A CD  1 
ATOM   227  C  CE  . LYS A 1 30  ? 9.538  18.702 0.713   1.00 31.04 ? 30  LYS A CE  1 
ATOM   228  N  NZ  . LYS A 1 30  ? 9.717  17.807 -0.461  1.00 33.25 ? 30  LYS A NZ  1 
ATOM   229  N  N   . SER A 1 31  ? 11.229 18.626 7.369   1.00 15.86 ? 31  SER A N   1 
ATOM   230  C  CA  . SER A 1 31  ? 10.816 17.860 8.567   1.00 15.82 ? 31  SER A CA  1 
ATOM   231  C  C   . SER A 1 31  ? 11.547 18.392 9.794   1.00 15.12 ? 31  SER A C   1 
ATOM   232  O  O   . SER A 1 31  ? 12.743 18.652 9.682   1.00 14.11 ? 31  SER A O   1 
ATOM   233  C  CB  . SER A 1 31  ? 11.089 16.411 8.373   1.00 16.75 ? 31  SER A CB  1 
ATOM   234  O  OG  . SER A 1 31  ? 10.938 15.710 9.587   1.00 17.71 ? 31  SER A OG  1 
ATOM   235  N  N   . VAL A 1 32  ? 10.887 18.437 10.947  1.00 14.69 ? 32  VAL A N   1 
ATOM   236  C  CA  . VAL A 1 32  ? 11.563 18.722 12.248  1.00 15.61 ? 32  VAL A CA  1 
ATOM   237  C  C   . VAL A 1 32  ? 12.566 17.611 12.638  1.00 14.42 ? 32  VAL A C   1 
ATOM   238  O  O   . VAL A 1 32  ? 13.463 17.864 13.481  1.00 14.83 ? 32  VAL A O   1 
ATOM   239  C  CB  . VAL A 1 32  ? 10.492 18.998 13.331  1.00 16.18 ? 32  VAL A CB  1 
ATOM   240  C  CG1 . VAL A 1 32  ? 9.907  17.689 13.868  1.00 16.67 ? 32  VAL A CG1 1 
ATOM   241  C  CG2 . VAL A 1 32  ? 11.041 19.863 14.449  1.00 16.05 ? 32  VAL A CG2 1 
ATOM   242  N  N   . ARG A 1 33  ? 12.425 16.401 12.062  1.00 15.84 ? 33  ARG A N   1 
ATOM   243  C  CA  . ARG A 1 33  ? 13.313 15.251 12.326  1.00 17.06 ? 33  ARG A CA  1 
ATOM   244  C  C   . ARG A 1 33  ? 14.566 15.480 11.489  1.00 15.13 ? 33  ARG A C   1 
ATOM   245  O  O   . ARG A 1 33  ? 14.556 15.124 10.301  1.00 16.40 ? 33  ARG A O   1 
ATOM   246  C  CB  . ARG A 1 33  ? 12.612 13.928 12.019  1.00 18.29 ? 33  ARG A CB  1 
ATOM   247  C  CG  . ARG A 1 33  ? 11.416 13.674 12.920  1.00 21.79 ? 33  ARG A CG  1 
ATOM   248  C  CD  . ARG A 1 33  ? 10.661 12.393 12.592  1.00 23.94 ? 33  ARG A CD  1 
ATOM   249  N  NE  . ARG A 1 33  ? 9.413  12.314 13.356  1.00 24.93 ? 33  ARG A NE  1 
ATOM   250  C  CZ  . ARG A 1 33  ? 9.155  11.435 14.331  1.00 27.92 ? 33  ARG A CZ  1 
ATOM   251  N  NH1 . ARG A 1 33  ? 10.086 10.610 14.760  1.00 29.36 ? 33  ARG A NH1 1 
ATOM   252  N  NH2 . ARG A 1 33  ? 7.979  11.447 14.931  1.00 26.74 ? 33  ARG A NH2 1 
ATOM   253  N  N   . SER A 1 34  ? 15.554 16.126 12.068  1.00 15.25 ? 34  SER A N   1 
ATOM   254  C  CA  . SER A 1 34  ? 16.783 16.589 11.377  1.00 14.23 ? 34  SER A CA  1 
ATOM   255  C  C   . SER A 1 34  ? 17.406 15.437 10.590  1.00 14.79 ? 34  SER A C   1 
ATOM   256  O  O   . SER A 1 34  ? 17.460 14.297 11.116  1.00 14.91 ? 34  SER A O   1 
ATOM   257  C  CB  . SER A 1 34  ? 17.807 17.118 12.342  1.00 14.54 ? 34  SER A CB  1 
ATOM   258  O  OG  . SER A 1 34  ? 17.253 18.123 13.199  1.00 13.61 ? 34  SER A OG  1 
ATOM   259  N  N   . LYS A 1 35  ? 17.877 15.731 9.383   1.00 14.45 ? 35  LYS A N   1 
ATOM   260  C  CA  . LYS A 1 35  ? 18.605 14.759 8.539   1.00 14.92 ? 35  LYS A CA  1 
ATOM   261  C  C   . LYS A 1 35  ? 20.000 14.530 9.097   1.00 15.64 ? 35  LYS A C   1 
ATOM   262  O  O   . LYS A 1 35  ? 20.523 13.441 8.887   1.00 16.73 ? 35  LYS A O   1 
ATOM   263  C  CB  . LYS A 1 35  ? 18.708 15.210 7.089   1.00 14.57 ? 35  LYS A CB  1 
ATOM   264  C  CG  . LYS A 1 35  ? 17.370 15.575 6.468   1.00 15.66 ? 35  LYS A CG  1 
ATOM   265  C  CD  . LYS A 1 35  ? 16.407 14.467 6.487   1.00 18.33 ? 35  LYS A CD  1 
ATOM   266  C  CE  . LYS A 1 35  ? 15.154 14.756 5.706   1.00 19.58 ? 35  LYS A CE  1 
ATOM   267  N  NZ  . LYS A 1 35  ? 14.167 13.671 5.874   1.00 21.53 ? 35  LYS A NZ  1 
ATOM   268  N  N   . LYS A 1 36  ? 20.574 15.486 9.833   1.00 14.63 ? 36  LYS A N   1 
ATOM   269  C  CA  . LYS A 1 36  ? 21.898 15.348 10.457  1.00 14.80 ? 36  LYS A CA  1 
ATOM   270  C  C   . LYS A 1 36  ? 21.895 16.229 11.703  1.00 14.03 ? 36  LYS A C   1 
ATOM   271  O  O   . LYS A 1 36  ? 21.317 17.316 11.649  1.00 14.13 ? 36  LYS A O   1 
ATOM   272  C  CB  . LYS A 1 36  ? 23.001 15.816 9.501   1.00 17.38 ? 36  LYS A CB  1 
ATOM   273  C  CG  . LYS A 1 36  ? 24.376 15.276 9.801   1.00 22.80 ? 36  LYS A CG  1 
ATOM   274  C  CD  . LYS A 1 36  ? 24.572 13.846 9.249   1.00 24.84 ? 36  LYS A CD  1 
ATOM   275  C  CE  . LYS A 1 36  ? 26.039 13.485 9.094   1.00 31.79 ? 36  LYS A CE  1 
ATOM   276  N  NZ  . LYS A 1 36  ? 26.760 14.439 8.214   1.00 34.00 ? 36  LYS A NZ  1 
ATOM   277  N  N   . THR A 1 37  ? 22.508 15.781 12.782  1.00 13.79 ? 37  THR A N   1 
ATOM   278  C  CA  . THR A 1 37  ? 22.637 16.576 14.022  1.00 14.34 ? 37  THR A CA  1 
ATOM   279  C  C   . THR A 1 37  ? 24.063 16.473 14.540  1.00 14.73 ? 37  THR A C   1 
ATOM   280  O  O   . THR A 1 37  ? 24.818 15.554 14.140  1.00 16.36 ? 37  THR A O   1 
ATOM   281  C  CB  . THR A 1 37  ? 21.647 16.174 15.120  1.00 17.77 ? 37  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 37  ? 22.011 14.861 15.525  1.00 19.27 ? 37  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 37  ? 20.207 16.256 14.707  1.00 19.03 ? 37  THR A CG2 1 
ATOM   284  N  N   . ALA A 1 38  ? 24.442 17.441 15.356  1.00 13.54 ? 38  ALA A N   1 
ATOM   285  C  CA  . ALA A 1 38  ? 25.702 17.446 16.109  1.00 13.41 ? 38  ALA A CA  1 
ATOM   286  C  C   . ALA A 1 38  ? 25.403 17.932 17.516  1.00 14.14 ? 38  ALA A C   1 
ATOM   287  O  O   . ALA A 1 38  ? 24.607 18.841 17.697  1.00 14.31 ? 38  ALA A O   1 
ATOM   288  C  CB  . ALA A 1 38  ? 26.777 18.284 15.465  1.00 15.13 ? 38  ALA A CB  1 
ATOM   289  N  N   . LYS A 1 39  ? 26.132 17.377 18.471  1.00 14.33 ? 39  LYS A N   1 
ATOM   290  C  CA  . LYS A 1 39  ? 26.047 17.835 19.873  1.00 14.22 ? 39  LYS A CA  1 
ATOM   291  C  C   . LYS A 1 39  ? 26.417 19.314 19.974  1.00 13.94 ? 39  LYS A C   1 
ATOM   292  O  O   . LYS A 1 39  ? 27.465 19.762 19.413  1.00 14.91 ? 39  LYS A O   1 
ATOM   293  C  CB  . LYS A 1 39  ? 26.955 17.005 20.770  1.00 16.17 ? 39  LYS A CB  1 
ATOM   294  C  CG  . LYS A 1 39  ? 26.863 17.323 22.258  1.00 18.35 ? 39  LYS A CG  1 
ATOM   295  C  CD  . LYS A 1 39  ? 27.570 16.250 23.104  1.00 22.06 ? 39  LYS A CD  1 
ATOM   296  C  CE  . LYS A 1 39  ? 26.996 16.194 24.503  1.00 28.22 ? 39  LYS A CE  1 
ATOM   297  N  NZ  . LYS A 1 39  ? 27.464 17.357 25.267  1.00 34.26 ? 39  LYS A NZ  1 
ATOM   298  N  N   . TRP A 1 40  ? 25.632 20.063 20.736  1.00 13.35 ? 40  TRP A N   1 
ATOM   299  C  CA  . TRP A 1 40  ? 25.847 21.499 20.957  1.00 13.54 ? 40  TRP A CA  1 
ATOM   300  C  C   . TRP A 1 40  ? 25.912 21.777 22.445  1.00 13.22 ? 40  TRP A C   1 
ATOM   301  O  O   . TRP A 1 40  ? 24.892 21.573 23.118  1.00 15.30 ? 40  TRP A O   1 
ATOM   302  C  CB  . TRP A 1 40  ? 24.695 22.256 20.316  1.00 13.28 ? 40  TRP A CB  1 
ATOM   303  C  CG  . TRP A 1 40  ? 24.710 23.733 20.525  1.00 12.89 ? 40  TRP A CG  1 
ATOM   304  C  CD1 . TRP A 1 40  ? 25.807 24.543 20.526  1.00 14.05 ? 40  TRP A CD1 1 
ATOM   305  C  CD2 . TRP A 1 40  ? 23.564 24.587 20.682  1.00 12.74 ? 40  TRP A CD2 1 
ATOM   306  N  NE1 . TRP A 1 40  ? 25.441 25.830 20.773  1.00 14.86 ? 40  TRP A NE1 1 
ATOM   307  C  CE2 . TRP A 1 40  ? 24.070 25.900 20.825  1.00 13.60 ? 40  TRP A CE2 1 
ATOM   308  C  CE3 . TRP A 1 40  ? 22.182 24.375 20.730  1.00 12.76 ? 40  TRP A CE3 1 
ATOM   309  C  CZ2 . TRP A 1 40  ? 23.231 26.994 20.995  1.00 14.57 ? 40  TRP A CZ2 1 
ATOM   310  C  CZ3 . TRP A 1 40  ? 21.349 25.463 20.910  1.00 12.89 ? 40  TRP A CZ3 1 
ATOM   311  C  CH2 . TRP A 1 40  ? 21.893 26.744 21.073  1.00 13.53 ? 40  TRP A CH2 1 
ATOM   312  N  N   . ASN A 1 41  ? 27.029 22.305 22.908  1.00 13.70 ? 41  ASN A N   1 
ATOM   313  C  CA  . ASN A 1 41  ? 27.232 22.633 24.345  1.00 16.47 ? 41  ASN A CA  1 
ATOM   314  C  C   . ASN A 1 41  ? 26.679 24.053 24.555  1.00 16.59 ? 41  ASN A C   1 
ATOM   315  O  O   . ASN A 1 41  ? 27.437 25.032 24.622  1.00 17.33 ? 41  ASN A O   1 
ATOM   316  C  CB  . ASN A 1 41  ? 28.687 22.337 24.743  1.00 15.33 ? 41  ASN A CB  1 
ATOM   317  C  CG  . ASN A 1 41  ? 29.025 20.846 24.806  1.00 18.27 ? 41  ASN A CG  1 
ATOM   318  O  OD1 . ASN A 1 41  ? 28.263 20.064 25.388  1.00 21.43 ? 41  ASN A OD1 1 
ATOM   319  N  ND2 . ASN A 1 41  ? 30.125 20.432 24.177  1.00 20.20 ? 41  ASN A ND2 1 
ATOM   320  N  N   . MET A 1 42  ? 25.364 24.175 24.555  1.00 18.37 ? 42  MET A N   1 
ATOM   321  C  CA  . MET A 1 42  ? 24.672 25.469 24.663  1.00 20.54 ? 42  MET A CA  1 
ATOM   322  C  C   . MET A 1 42  ? 25.057 26.127 25.999  1.00 19.28 ? 42  MET A C   1 
ATOM   323  O  O   . MET A 1 42  ? 25.169 25.426 27.022  1.00 19.86 ? 42  MET A O   1 
ATOM   324  C  CB  . MET A 1 42  ? 23.154 25.262 24.589  1.00 24.08 ? 42  MET A CB  1 
ATOM   325  C  CG  . MET A 1 42  ? 22.397 26.542 24.333  1.00 31.11 ? 42  MET A CG  1 
ATOM   326  S  SD  . MET A 1 42  ? 22.065 27.556 25.829  1.00 49.98 ? 42  MET A SD  1 
ATOM   327  C  CE  . MET A 1 42  ? 21.112 26.402 26.798  1.00 36.56 ? 42  MET A CE  1 
ATOM   328  N  N   . GLN A 1 43  ? 25.262 27.432 25.986  1.00 17.99 ? 43  GLN A N   1 
ATOM   329  C  CA  . GLN A 1 43  ? 25.604 28.218 27.200  1.00 17.44 ? 43  GLN A CA  1 
ATOM   330  C  C   . GLN A 1 43  ? 24.467 29.176 27.557  1.00 17.23 ? 43  GLN A C   1 
ATOM   331  O  O   . GLN A 1 43  ? 24.295 30.237 26.907  1.00 16.49 ? 43  GLN A O   1 
ATOM   332  C  CB  . GLN A 1 43  ? 26.940 28.919 26.999  1.00 19.49 ? 43  GLN A CB  1 
ATOM   333  C  CG  . GLN A 1 43  ? 28.108 27.945 26.904  1.00 21.67 ? 43  GLN A CG  1 
ATOM   334  C  CD  . GLN A 1 43  ? 29.415 28.678 26.778  1.00 23.90 ? 43  GLN A CD  1 
ATOM   335  O  OE1 . GLN A 1 43  ? 30.349 28.261 26.087  1.00 23.06 ? 43  GLN A OE1 1 
ATOM   336  N  NE2 . GLN A 1 43  ? 29.542 29.767 27.518  1.00 23.43 ? 43  GLN A NE2 1 
ATOM   337  N  N   . ASN A 1 44  ? 23.790 28.874 28.653  1.00 16.21 ? 44  ASN A N   1 
ATOM   338  C  CA  . ASN A 1 44  ? 22.672 29.690 29.157  1.00 17.31 ? 44  ASN A CA  1 
ATOM   339  C  C   . ASN A 1 44  ? 23.187 31.091 29.501  1.00 18.77 ? 44  ASN A C   1 
ATOM   340  O  O   . ASN A 1 44  ? 24.097 31.242 30.346  1.00 20.46 ? 44  ASN A O   1 
ATOM   341  C  CB  . ASN A 1 44  ? 22.005 28.978 30.335  1.00 19.15 ? 44  ASN A CB  1 
ATOM   342  C  CG  . ASN A 1 44  ? 20.673 29.574 30.732  1.00 21.01 ? 44  ASN A CG  1 
ATOM   343  O  OD1 . ASN A 1 44  ? 20.427 30.734 30.546  1.00 21.24 ? 44  ASN A OD1 1 
ATOM   344  N  ND2 . ASN A 1 44  ? 19.848 28.785 31.385  1.00 27.04 ? 44  ASN A ND2 1 
ATOM   345  N  N   . GLY A 1 45  ? 22.689 32.113 28.811  1.00 15.99 ? 45  GLY A N   1 
ATOM   346  C  CA  . GLY A 1 45  ? 22.951 33.524 29.140  1.00 17.26 ? 45  GLY A CA  1 
ATOM   347  C  C   . GLY A 1 45  ? 24.143 34.092 28.412  1.00 16.72 ? 45  GLY A C   1 
ATOM   348  O  O   . GLY A 1 45  ? 24.494 35.252 28.665  1.00 17.05 ? 45  GLY A O   1 
ATOM   349  N  N   . LYS A 1 46  ? 24.774 33.325 27.522  1.00 16.16 ? 46  LYS A N   1 
ATOM   350  C  CA  . LYS A 1 46  ? 25.946 33.842 26.798  1.00 16.36 ? 46  LYS A CA  1 
ATOM   351  C  C   . LYS A 1 46  ? 25.546 34.155 25.368  1.00 15.04 ? 46  LYS A C   1 
ATOM   352  O  O   . LYS A 1 46  ? 24.590 33.547 24.871  1.00 14.80 ? 46  LYS A O   1 
ATOM   353  C  CB  . LYS A 1 46  ? 27.102 32.861 26.859  1.00 19.89 ? 46  LYS A CB  1 
ATOM   354  C  CG  . LYS A 1 46  ? 27.519 32.587 28.294  1.00 24.35 ? 46  LYS A CG  1 
ATOM   355  C  CD  . LYS A 1 46  ? 28.085 33.844 28.940  1.00 28.04 ? 46  LYS A CD  1 
ATOM   356  C  CE  . LYS A 1 46  ? 29.295 33.527 29.806  1.00 36.08 ? 46  LYS A CE  1 
ATOM   357  N  NZ  . LYS A 1 46  ? 28.872 33.110 31.156  1.00 40.47 ? 46  LYS A NZ  1 
ATOM   358  N  N   . VAL A 1 47  ? 26.234 35.106 24.780  1.00 15.05 ? 47  VAL A N   1 
ATOM   359  C  CA  . VAL A 1 47  ? 25.991 35.424 23.352  1.00 14.70 ? 47  VAL A CA  1 
ATOM   360  C  C   . VAL A 1 47  ? 26.741 34.434 22.482  1.00 13.90 ? 47  VAL A C   1 
ATOM   361  O  O   . VAL A 1 47  ? 27.994 34.361 22.604  1.00 16.24 ? 47  VAL A O   1 
ATOM   362  C  CB  . VAL A 1 47  ? 26.400 36.867 23.020  1.00 15.87 ? 47  VAL A CB  1 
ATOM   363  C  CG1 . VAL A 1 47  ? 26.144 37.190 21.558  1.00 15.76 ? 47  VAL A CG1 1 
ATOM   364  C  CG2 . VAL A 1 47  ? 25.664 37.834 23.945  1.00 17.64 ? 47  VAL A CG2 1 
ATOM   365  N  N   . GLY A 1 48  ? 26.009 33.771 21.579  1.00 12.48 ? 48  GLY A N   1 
ATOM   366  C  CA  . GLY A 1 48  ? 26.547 32.833 20.587  1.00 12.08 ? 48  GLY A CA  1 
ATOM   367  C  C   . GLY A 1 48  ? 26.447 33.380 19.177  1.00 11.61 ? 48  GLY A C   1 
ATOM   368  O  O   . GLY A 1 48  ? 25.706 34.332 18.929  1.00 11.30 ? 48  GLY A O   1 
ATOM   369  N  N   . THR A 1 49  ? 27.167 32.760 18.282  1.00 9.93  ? 49  THR A N   1 
ATOM   370  C  CA  . THR A 1 49  ? 27.136 33.106 16.846  1.00 10.67 ? 49  THR A CA  1 
ATOM   371  C  C   . THR A 1 49  ? 27.003 31.847 16.006  1.00 11.95 ? 49  THR A C   1 
ATOM   372  O  O   . THR A 1 49  ? 27.754 30.888 16.202  1.00 11.90 ? 49  THR A O   1 
ATOM   373  C  CB  . THR A 1 49  ? 28.428 33.834 16.453  1.00 12.43 ? 49  THR A CB  1 
ATOM   374  O  OG1 . THR A 1 49  ? 28.682 34.994 17.250  1.00 15.60 ? 49  THR A OG1 1 
ATOM   375  C  CG2 . THR A 1 49  ? 28.450 34.202 14.993  1.00 13.24 ? 49  THR A CG2 1 
ATOM   376  N  N   . ALA A 1 50  ? 26.099 31.890 15.048  1.00 11.19 ? 50  ALA A N   1 
ATOM   377  C  CA  . ALA A 1 50  ? 25.848 30.815 14.091  1.00 10.18 ? 50  ALA A CA  1 
ATOM   378  C  C   . ALA A 1 50  ? 26.168 31.306 12.688  1.00 11.41 ? 50  ALA A C   1 
ATOM   379  O  O   . ALA A 1 50  ? 25.841 32.462 12.335  1.00 11.16 ? 50  ALA A O   1 
ATOM   380  C  CB  . ALA A 1 50  ? 24.434 30.390 14.176  1.00 11.85 ? 50  ALA A CB  1 
ATOM   381  N  N   . HIS A 1 51  ? 26.797 30.421 11.923  1.00 10.77 ? 51  HIS A N   1 
ATOM   382  C  CA  . HIS A 1 51  ? 27.147 30.661 10.505  1.00 11.77 ? 51  HIS A CA  1 
ATOM   383  C  C   . HIS A 1 51  ? 26.542 29.533 9.684   1.00 11.85 ? 51  HIS A C   1 
ATOM   384  O  O   . HIS A 1 51  ? 26.616 28.368 10.082  1.00 12.50 ? 51  HIS A O   1 
ATOM   385  C  CB  . HIS A 1 51  ? 28.671 30.683 10.292  1.00 13.26 ? 51  HIS A CB  1 
ATOM   386  C  CG  . HIS A 1 51  ? 29.399 31.781 10.964  1.00 17.62 ? 51  HIS A CG  1 
ATOM   387  N  ND1 . HIS A 1 51  ? 30.213 31.583 12.073  1.00 19.99 ? 51  HIS A ND1 1 
ATOM   388  C  CD2 . HIS A 1 51  ? 29.441 33.099 10.674  1.00 18.83 ? 51  HIS A CD2 1 
ATOM   389  C  CE1 . HIS A 1 51  ? 30.712 32.747 12.447  1.00 19.55 ? 51  HIS A CE1 1 
ATOM   390  N  NE2 . HIS A 1 51  ? 30.254 33.691 11.594  1.00 21.97 ? 51  HIS A NE2 1 
ATOM   391  N  N   . ILE A 1 52  ? 25.901 29.874 8.574   1.00 11.26 ? 52  ILE A N   1 
ATOM   392  C  CA  . ILE A 1 52  ? 25.252 28.917 7.663   1.00 10.87 ? 52  ILE A CA  1 
ATOM   393  C  C   . ILE A 1 52  ? 25.794 29.211 6.271   1.00 11.19 ? 52  ILE A C   1 
ATOM   394  O  O   . ILE A 1 52  ? 25.850 30.383 5.880   1.00 12.63 ? 52  ILE A O   1 
ATOM   395  C  CB  . ILE A 1 52  ? 23.715 29.046 7.737   1.00 11.38 ? 52  ILE A CB  1 
ATOM   396  C  CG1 . ILE A 1 52  ? 23.114 28.809 9.149   1.00 12.99 ? 52  ILE A CG1 1 
ATOM   397  C  CG2 . ILE A 1 52  ? 23.098 28.108 6.748   1.00 12.73 ? 52  ILE A CG2 1 
ATOM   398  C  CD1 . ILE A 1 52  ? 22.704 30.020 9.830   1.00 15.51 ? 52  ILE A CD1 1 
ATOM   399  N  N   . ILE A 1 53  ? 26.214 28.191 5.538   1.00 10.72 ? 53  ILE A N   1 
ATOM   400  C  CA  . ILE A 1 53  ? 26.764 28.351 4.171   1.00 11.04 ? 53  ILE A CA  1 
ATOM   401  C  C   . ILE A 1 53  ? 26.195 27.269 3.245   1.00 11.23 ? 53  ILE A C   1 
ATOM   402  O  O   . ILE A 1 53  ? 25.938 26.131 3.667   1.00 11.45 ? 53  ILE A O   1 
ATOM   403  C  CB  . ILE A 1 53  ? 28.298 28.336 4.183   1.00 13.70 ? 53  ILE A CB  1 
ATOM   404  C  CG1 . ILE A 1 53  ? 28.890 27.087 4.823   1.00 16.42 ? 53  ILE A CG1 1 
ATOM   405  C  CG2 . ILE A 1 53  ? 28.840 29.582 4.868   1.00 15.32 ? 53  ILE A CG2 1 
ATOM   406  C  CD1 . ILE A 1 53  ? 30.399 27.037 4.779   1.00 19.17 ? 53  ILE A CD1 1 
ATOM   407  N  N   . TYR A 1 54  ? 26.095 27.602 1.982   1.00 10.23 ? 54  TYR A N   1 
ATOM   408  C  CA  . TYR A 1 54  ? 25.608 26.673 0.950   1.00 10.89 ? 54  TYR A CA  1 
ATOM   409  C  C   . TYR A 1 54  ? 26.119 27.159 -0.401  1.00 10.71 ? 54  TYR A C   1 
ATOM   410  O  O   . TYR A 1 54  ? 26.052 28.367 -0.670  1.00 11.33 ? 54  TYR A O   1 
ATOM   411  C  CB  . TYR A 1 54  ? 24.082 26.576 0.948   1.00 10.48 ? 54  TYR A CB  1 
ATOM   412  C  CG  . TYR A 1 54  ? 23.533 25.736 -0.191  1.00 11.37 ? 54  TYR A CG  1 
ATOM   413  C  CD1 . TYR A 1 54  ? 23.392 24.364 -0.038  1.00 11.36 ? 54  TYR A CD1 1 
ATOM   414  C  CD2 . TYR A 1 54  ? 23.157 26.292 -1.401  1.00 11.84 ? 54  TYR A CD2 1 
ATOM   415  C  CE1 . TYR A 1 54  ? 22.955 23.564 -1.080  1.00 13.17 ? 54  TYR A CE1 1 
ATOM   416  C  CE2 . TYR A 1 54  ? 22.689 25.502 -2.443  1.00 12.14 ? 54  TYR A CE2 1 
ATOM   417  C  CZ  . TYR A 1 54  ? 22.559 24.140 -2.266  1.00 12.90 ? 54  TYR A CZ  1 
ATOM   418  O  OH  . TYR A 1 54  ? 22.062 23.314 -3.263  1.00 14.18 ? 54  TYR A OH  1 
ATOM   419  N  N   . ASN A 1 55  ? 26.403 26.234 -1.308  1.00 10.90 ? 55  ASN A N   1 
ATOM   420  C  CA  . ASN A 1 55  ? 26.485 26.617 -2.732  1.00 11.09 ? 55  ASN A CA  1 
ATOM   421  C  C   . ASN A 1 55  ? 25.983 25.484 -3.600  1.00 10.94 ? 55  ASN A C   1 
ATOM   422  O  O   . ASN A 1 55  ? 26.006 24.307 -3.200  1.00 10.35 ? 55  ASN A O   1 
ATOM   423  C  CB  . ASN A 1 55  ? 27.902 27.076 -3.099  1.00 12.95 ? 55  ASN A CB  1 
ATOM   424  C  CG  . ASN A 1 55  ? 28.875 25.933 -3.221  1.00 12.41 ? 55  ASN A CG  1 
ATOM   425  O  OD1 . ASN A 1 55  ? 28.844 25.226 -4.246  1.00 13.60 ? 55  ASN A OD1 1 
ATOM   426  N  ND2 . ASN A 1 55  ? 29.704 25.736 -2.203  1.00 14.58 ? 55  ASN A ND2 1 
ATOM   427  N  N   . SER A 1 56  ? 25.563 25.864 -4.801  1.00 12.24 ? 56  SER A N   1 
ATOM   428  C  CA  . SER A 1 56  ? 24.882 24.967 -5.770  1.00 13.17 ? 56  SER A CA  1 
ATOM   429  C  C   . SER A 1 56  ? 25.856 24.040 -6.478  1.00 14.16 ? 56  SER A C   1 
ATOM   430  O  O   . SER A 1 56  ? 25.387 23.079 -7.167  1.00 16.23 ? 56  SER A O   1 
ATOM   431  C  CB  . SER A 1 56  ? 24.085 25.791 -6.779  1.00 13.22 ? 56  SER A CB  1 
ATOM   432  O  OG  . SER A 1 56  ? 24.961 26.486 -7.633  1.00 14.12 ? 56  SER A OG  1 
ATOM   433  N  N   . VAL A 1 57  ? 27.157 24.285 -6.380  1.00 14.16 ? 57  VAL A N   1 
ATOM   434  C  CA  . VAL A 1 57  ? 28.138 23.375 -7.013  1.00 14.93 ? 57  VAL A CA  1 
ATOM   435  C  C   . VAL A 1 57  ? 28.355 22.180 -6.081  1.00 15.64 ? 57  VAL A C   1 
ATOM   436  O  O   . VAL A 1 57  ? 28.260 21.010 -6.523  1.00 17.28 ? 57  VAL A O   1 
ATOM   437  C  CB  . VAL A 1 57  ? 29.419 24.135 -7.359  1.00 16.76 ? 57  VAL A CB  1 
ATOM   438  C  CG1 . VAL A 1 57  ? 30.511 23.208 -7.856  1.00 17.25 ? 57  VAL A CG1 1 
ATOM   439  C  CG2 . VAL A 1 57  ? 29.097 25.205 -8.402  1.00 18.65 ? 57  VAL A CG2 1 
ATOM   440  N  N   . ASP A 1 58  ? 28.622 22.450 -4.818  1.00 15.06 ? 58  ASP A N   1 
ATOM   441  C  CA  . ASP A 1 58  ? 28.905 21.353 -3.854  1.00 16.32 ? 58  ASP A CA  1 
ATOM   442  C  C   . ASP A 1 58  ? 27.604 20.759 -3.308  1.00 15.63 ? 58  ASP A C   1 
ATOM   443  O  O   . ASP A 1 58  ? 27.646 19.588 -2.838  1.00 15.05 ? 58  ASP A O   1 
ATOM   444  C  CB  . ASP A 1 58  ? 29.755 21.866 -2.706  1.00 17.77 ? 58  ASP A CB  1 
ATOM   445  C  CG  . ASP A 1 58  ? 31.114 22.343 -3.167  1.00 21.56 ? 58  ASP A CG  1 
ATOM   446  O  OD1 . ASP A 1 58  ? 31.619 21.819 -4.187  1.00 23.21 ? 58  ASP A OD1 1 
ATOM   447  O  OD2 . ASP A 1 58  ? 31.592 23.268 -2.570  1.00 22.42 ? 58  ASP A OD2 1 
ATOM   448  N  N   . LYS A 1 59  ? 26.493 21.505 -3.311  1.00 13.85 ? 59  LYS A N   1 
ATOM   449  C  CA  . LYS A 1 59  ? 25.178 21.021 -2.843  1.00 14.12 ? 59  LYS A CA  1 
ATOM   450  C  C   . LYS A 1 59  ? 25.343 20.455 -1.434  1.00 14.13 ? 59  LYS A C   1 
ATOM   451  O  O   . LYS A 1 59  ? 24.965 19.273 -1.158  1.00 14.23 ? 59  LYS A O   1 
ATOM   452  C  CB  . LYS A 1 59  ? 24.592 19.986 -3.809  1.00 17.37 ? 59  LYS A CB  1 
ATOM   453  C  CG  . LYS A 1 59  ? 24.291 20.507 -5.213  1.00 20.46 ? 59  LYS A CG  1 
ATOM   454  C  CD  . LYS A 1 59  ? 24.090 19.397 -6.231  1.00 24.55 ? 59  LYS A CD  1 
ATOM   455  C  CE  . LYS A 1 59  ? 24.667 19.717 -7.591  1.00 32.48 ? 59  LYS A CE  1 
ATOM   456  N  NZ  . LYS A 1 59  ? 24.079 20.960 -8.135  1.00 35.88 ? 59  LYS A NZ  1 
ATOM   457  N  N   . ARG A 1 60  ? 25.903 21.277 -0.555  1.00 14.98 ? 60  ARG A N   1 
ATOM   458  C  CA  . ARG A 1 60  ? 26.128 20.864 0.844   1.00 15.35 ? 60  ARG A CA  1 
ATOM   459  C  C   . ARG A 1 60  ? 25.756 22.043 1.739   1.00 14.88 ? 60  ARG A C   1 
ATOM   460  O  O   . ARG A 1 60  ? 26.265 23.154 1.512   1.00 16.15 ? 60  ARG A O   1 
ATOM   461  C  CB  . ARG A 1 60  ? 27.585 20.499 1.100   1.00 18.21 ? 60  ARG A CB  1 
ATOM   462  C  CG  . ARG A 1 60  ? 27.844 19.892 2.472   1.00 23.37 ? 60  ARG A CG  1 
ATOM   463  C  CD  . ARG A 1 60  ? 29.111 19.086 2.297   1.00 29.67 ? 60  ARG A CD  1 
ATOM   464  N  NE  . ARG A 1 60  ? 29.662 18.575 3.530   1.00 31.27 ? 60  ARG A NE  1 
ATOM   465  C  CZ  . ARG A 1 60  ? 29.730 17.291 3.860   1.00 38.62 ? 60  ARG A CZ  1 
ATOM   466  N  NH1 . ARG A 1 60  ? 30.258 16.935 5.025   1.00 38.81 ? 60  ARG A NH1 1 
ATOM   467  N  NH2 . ARG A 1 60  ? 29.297 16.360 3.026   1.00 43.47 ? 60  ARG A NH2 1 
ATOM   468  N  N   . LEU A 1 61  ? 24.788 21.847 2.606   1.00 13.74 ? 61  LEU A N   1 
ATOM   469  C  CA  . LEU A 1 61  ? 24.362 22.890 3.556   1.00 12.19 ? 61  LEU A CA  1 
ATOM   470  C  C   . LEU A 1 61  ? 25.138 22.630 4.842   1.00 13.35 ? 61  LEU A C   1 
ATOM   471  O  O   . LEU A 1 61  ? 25.055 21.507 5.393   1.00 13.59 ? 61  LEU A O   1 
ATOM   472  C  CB  . LEU A 1 61  ? 22.845 22.795 3.734   1.00 12.18 ? 61  LEU A CB  1 
ATOM   473  C  CG  . LEU A 1 61  ? 22.227 23.777 4.746   1.00 12.63 ? 61  LEU A CG  1 
ATOM   474  C  CD1 . LEU A 1 61  ? 22.459 25.229 4.326   1.00 13.98 ? 61  LEU A CD1 1 
ATOM   475  C  CD2 . LEU A 1 61  ? 20.750 23.488 4.825   1.00 14.09 ? 61  LEU A CD2 1 
ATOM   476  N  N   . SER A 1 62  ? 25.902 23.596 5.320   1.00 11.48 ? 62  SER A N   1 
ATOM   477  C  CA  . SER A 1 62  ? 26.743 23.440 6.523   1.00 11.76 ? 62  SER A CA  1 
ATOM   478  C  C   . SER A 1 62  ? 26.465 24.585 7.498   1.00 11.88 ? 62  SER A C   1 
ATOM   479  O  O   . SER A 1 62  ? 26.059 25.702 7.084   1.00 12.61 ? 62  SER A O   1 
ATOM   480  C  CB  . SER A 1 62  ? 28.213 23.398 6.177   1.00 13.69 ? 62  SER A CB  1 
ATOM   481  O  OG  . SER A 1 62  ? 28.578 22.258 5.379   1.00 14.43 ? 62  SER A OG  1 
ATOM   482  N  N   . ALA A 1 63  ? 26.683 24.315 8.778   1.00 11.98 ? 63  ALA A N   1 
ATOM   483  C  CA  . ALA A 1 63  ? 26.496 25.326 9.825   1.00 11.68 ? 63  ALA A CA  1 
ATOM   484  C  C   . ALA A 1 63  ? 27.506 25.115 10.927  1.00 11.84 ? 63  ALA A C   1 
ATOM   485  O  O   . ALA A 1 63  ? 27.900 23.953 11.176  1.00 11.37 ? 63  ALA A O   1 
ATOM   486  C  CB  . ALA A 1 63  ? 25.098 25.250 10.378  1.00 12.92 ? 63  ALA A CB  1 
ATOM   487  N  N   . VAL A 1 64  ? 27.921 26.215 11.552  1.00 11.80 ? 64  VAL A N   1 
ATOM   488  C  CA  . VAL A 1 64  ? 28.868 26.207 12.687  1.00 13.24 ? 64  VAL A CA  1 
ATOM   489  C  C   . VAL A 1 64  ? 28.293 27.122 13.751  1.00 13.32 ? 64  VAL A C   1 
ATOM   490  O  O   . VAL A 1 64  ? 27.847 28.238 13.403  1.00 13.80 ? 64  VAL A O   1 
ATOM   491  C  CB  . VAL A 1 64  ? 30.262 26.701 12.280  1.00 16.68 ? 64  VAL A CB  1 
ATOM   492  C  CG1 . VAL A 1 64  ? 31.189 26.669 13.489  1.00 19.11 ? 64  VAL A CG1 1 
ATOM   493  C  CG2 . VAL A 1 64  ? 30.844 25.888 11.136  1.00 19.34 ? 64  VAL A CG2 1 
ATOM   494  N  N   . VAL A 1 65  ? 28.313 26.695 15.005  1.00 11.56 ? 65  VAL A N   1 
ATOM   495  C  CA  . VAL A 1 65  ? 27.832 27.561 16.110  1.00 12.18 ? 65  VAL A CA  1 
ATOM   496  C  C   . VAL A 1 65  ? 28.938 27.614 17.143  1.00 13.76 ? 65  VAL A C   1 
ATOM   497  O  O   . VAL A 1 65  ? 29.499 26.560 17.447  1.00 13.71 ? 65  VAL A O   1 
ATOM   498  C  CB  . VAL A 1 65  ? 26.489 27.064 16.681  1.00 14.74 ? 65  VAL A CB  1 
ATOM   499  C  CG1 . VAL A 1 65  ? 25.966 28.016 17.753  1.00 16.16 ? 65  VAL A CG1 1 
ATOM   500  C  CG2 . VAL A 1 65  ? 25.443 26.930 15.597  1.00 18.39 ? 65  VAL A CG2 1 
ATOM   501  N  N   . SER A 1 66  ? 29.204 28.782 17.693  1.00 13.28 ? 66  SER A N   1 
ATOM   502  C  CA  . SER A 1 66  ? 30.261 28.925 18.703  1.00 15.92 ? 66  SER A CA  1 
ATOM   503  C  C   . SER A 1 66  ? 29.885 29.971 19.722  1.00 15.30 ? 66  SER A C   1 
ATOM   504  O  O   . SER A 1 66  ? 29.013 30.816 19.475  1.00 13.27 ? 66  SER A O   1 
ATOM   505  C  CB  . SER A 1 66  ? 31.593 29.257 18.146  1.00 18.64 ? 66  SER A CB  1 
ATOM   506  O  OG  . SER A 1 66  ? 31.571 30.487 17.536  1.00 20.85 ? 66  SER A OG  1 
ATOM   507  N  N   . TYR A 1 67  ? 30.600 29.908 20.829  1.00 14.79 ? 67  TYR A N   1 
ATOM   508  C  CA  . TYR A 1 67  ? 30.625 30.950 21.852  1.00 13.88 ? 67  TYR A CA  1 
ATOM   509  C  C   . TYR A 1 67  ? 32.068 31.356 22.044  1.00 15.09 ? 67  TYR A C   1 
ATOM   510  O  O   . TYR A 1 67  ? 32.969 30.550 21.808  1.00 15.29 ? 67  TYR A O   1 
ATOM   511  C  CB  . TYR A 1 67  ? 30.075 30.412 23.161  1.00 14.71 ? 67  TYR A CB  1 
ATOM   512  C  CG  . TYR A 1 67  ? 28.611 30.068 23.181  1.00 14.18 ? 67  TYR A CG  1 
ATOM   513  C  CD1 . TYR A 1 67  ? 27.697 31.046 23.438  1.00 13.19 ? 67  TYR A CD1 1 
ATOM   514  C  CD2 . TYR A 1 67  ? 28.142 28.775 23.004  1.00 17.08 ? 67  TYR A CD2 1 
ATOM   515  C  CE1 . TYR A 1 67  ? 26.340 30.778 23.541  1.00 14.92 ? 67  TYR A CE1 1 
ATOM   516  C  CE2 . TYR A 1 67  ? 26.784 28.485 23.107  1.00 16.89 ? 67  TYR A CE2 1 
ATOM   517  C  CZ  . TYR A 1 67  ? 25.876 29.498 23.365  1.00 18.13 ? 67  TYR A CZ  1 
ATOM   518  O  OH  . TYR A 1 67  ? 24.515 29.314 23.508  1.00 22.74 ? 67  TYR A OH  1 
ATOM   519  N  N   . PRO A 1 68  ? 32.297 32.581 22.534  1.00 15.91 ? 68  PRO A N   1 
ATOM   520  C  CA  . PRO A 1 68  ? 33.664 32.989 22.859  1.00 18.25 ? 68  PRO A CA  1 
ATOM   521  C  C   . PRO A 1 68  ? 34.273 32.014 23.890  1.00 16.26 ? 68  PRO A C   1 
ATOM   522  O  O   . PRO A 1 68  ? 33.565 31.575 24.773  1.00 16.94 ? 68  PRO A O   1 
ATOM   523  C  CB  . PRO A 1 68  ? 33.495 34.396 23.472  1.00 20.30 ? 68  PRO A CB  1 
ATOM   524  C  CG  . PRO A 1 68  ? 32.130 34.885 22.946  1.00 21.13 ? 68  PRO A CG  1 
ATOM   525  C  CD  . PRO A 1 68  ? 31.286 33.627 22.805  1.00 18.49 ? 68  PRO A CD  1 
ATOM   526  N  N   . ASN A 1 69  ? 35.544 31.683 23.709  1.00 19.04 ? 69  ASN A N   1 
ATOM   527  C  CA  . ASN A 1 69  ? 36.359 30.919 24.695  1.00 19.01 ? 69  ASN A CA  1 
ATOM   528  C  C   . ASN A 1 69  ? 35.940 29.441 24.681  1.00 17.58 ? 69  ASN A C   1 
ATOM   529  O  O   . ASN A 1 69  ? 36.328 28.697 25.578  1.00 18.77 ? 69  ASN A O   1 
ATOM   530  C  CB  . ASN A 1 69  ? 36.254 31.471 26.127  1.00 20.82 ? 69  ASN A CB  1 
ATOM   531  C  CG  . ASN A 1 69  ? 36.692 32.918 26.275  1.00 24.67 ? 69  ASN A CG  1 
ATOM   532  O  OD1 . ASN A 1 69  ? 36.136 33.639 27.089  1.00 39.54 ? 69  ASN A OD1 1 
ATOM   533  N  ND2 . ASN A 1 69  ? 37.651 33.364 25.489  1.00 25.80 ? 69  ASN A ND2 1 
ATOM   534  N  N   . ALA A 1 70  ? 35.171 28.982 23.690  1.00 15.54 ? 70  ALA A N   1 
ATOM   535  C  CA  . ALA A 1 70  ? 34.676 27.608 23.586  1.00 14.50 ? 70  ALA A CA  1 
ATOM   536  C  C   . ALA A 1 70  ? 34.888 27.049 22.183  1.00 14.61 ? 70  ALA A C   1 
ATOM   537  O  O   . ALA A 1 70  ? 34.975 27.777 21.183  1.00 14.94 ? 70  ALA A O   1 
ATOM   538  C  CB  . ALA A 1 70  ? 33.223 27.537 23.930  1.00 16.19 ? 70  ALA A CB  1 
ATOM   539  N  N   . ASP A 1 71  ? 34.899 25.726 22.149  1.00 14.57 ? 71  ASP A N   1 
ATOM   540  C  CA  . ASP A 1 71  ? 34.972 24.928 20.918  1.00 15.25 ? 71  ASP A CA  1 
ATOM   541  C  C   . ASP A 1 71  ? 33.653 25.093 20.178  1.00 15.75 ? 71  ASP A C   1 
ATOM   542  O  O   . ASP A 1 71  ? 32.625 25.326 20.849  1.00 18.37 ? 71  ASP A O   1 
ATOM   543  C  CB  . ASP A 1 71  ? 35.317 23.474 21.224  1.00 16.31 ? 71  ASP A CB  1 
ATOM   544  C  CG  . ASP A 1 71  ? 36.700 23.278 21.846  1.00 19.60 ? 71  ASP A CG  1 
ATOM   545  O  OD1 . ASP A 1 71  ? 37.646 23.972 21.453  1.00 22.28 ? 71  ASP A OD1 1 
ATOM   546  O  OD2 . ASP A 1 71  ? 36.826 22.422 22.714  1.00 23.76 ? 71  ASP A OD2 1 
ATOM   547  N  N   . SER A 1 72  ? 33.697 25.004 18.870  1.00 16.92 ? 72  SER A N   1 
ATOM   548  C  CA  . SER A 1 72  ? 32.500 25.101 17.992  1.00 16.93 ? 72  SER A CA  1 
ATOM   549  C  C   . SER A 1 72  ? 31.795 23.757 17.872  1.00 15.90 ? 72  SER A C   1 
ATOM   550  O  O   . SER A 1 72  ? 32.415 22.712 18.147  1.00 15.86 ? 72  SER A O   1 
ATOM   551  C  CB  . SER A 1 72  ? 32.894 25.534 16.616  1.00 20.73 ? 72  SER A CB  1 
ATOM   552  O  OG  . SER A 1 72  ? 33.469 26.793 16.670  1.00 27.82 ? 72  SER A OG  1 
ATOM   553  N  N   . ALA A 1 73  ? 30.533 23.786 17.436  1.00 13.58 ? 73  ALA A N   1 
ATOM   554  C  CA  . ALA A 1 73  ? 29.781 22.622 16.919  1.00 12.68 ? 73  ALA A CA  1 
ATOM   555  C  C   . ALA A 1 73  ? 29.500 22.857 15.444  1.00 13.56 ? 73  ALA A C   1 
ATOM   556  O  O   . ALA A 1 73  ? 29.274 23.990 15.054  1.00 14.24 ? 73  ALA A O   1 
ATOM   557  C  CB  . ALA A 1 73  ? 28.527 22.371 17.682  1.00 14.96 ? 73  ALA A CB  1 
ATOM   558  N  N   . THR A 1 74  ? 29.560 21.809 14.651  1.00 13.33 ? 74  THR A N   1 
ATOM   559  C  CA  . THR A 1 74  ? 29.357 21.923 13.194  1.00 13.84 ? 74  THR A CA  1 
ATOM   560  C  C   . THR A 1 74  ? 28.520 20.752 12.728  1.00 14.31 ? 74  THR A C   1 
ATOM   561  O  O   . THR A 1 74  ? 28.654 19.610 13.253  1.00 14.15 ? 74  THR A O   1 
ATOM   562  C  CB  . THR A 1 74  ? 30.704 22.062 12.452  1.00 17.25 ? 74  THR A CB  1 
ATOM   563  O  OG1 . THR A 1 74  ? 30.440 22.360 11.079  1.00 18.65 ? 74  THR A OG1 1 
ATOM   564  C  CG2 . THR A 1 74  ? 31.596 20.840 12.484  1.00 20.46 ? 74  THR A CG2 1 
ATOM   565  N  N   . VAL A 1 75  ? 27.739 21.001 11.689  1.00 13.10 ? 75  VAL A N   1 
ATOM   566  C  CA  . VAL A 1 75  ? 26.905 19.966 11.075  1.00 12.95 ? 75  VAL A CA  1 
ATOM   567  C  C   . VAL A 1 75  ? 26.866 20.284 9.587   1.00 12.78 ? 75  VAL A C   1 
ATOM   568  O  O   . VAL A 1 75  ? 26.781 21.477 9.209   1.00 13.10 ? 75  VAL A O   1 
ATOM   569  C  CB  . VAL A 1 75  ? 25.520 19.899 11.740  1.00 13.07 ? 75  VAL A CB  1 
ATOM   570  C  CG1 . VAL A 1 75  ? 24.659 21.128 11.480  1.00 14.15 ? 75  VAL A CG1 1 
ATOM   571  C  CG2 . VAL A 1 75  ? 24.773 18.640 11.404  1.00 14.52 ? 75  VAL A CG2 1 
ATOM   572  N  N   . SER A 1 76  ? 26.844 19.231 8.778   1.00 13.14 ? 76  SER A N   1 
ATOM   573  C  CA  . SER A 1 76  ? 26.720 19.367 7.301   1.00 13.55 ? 76  SER A CA  1 
ATOM   574  C  C   . SER A 1 76  ? 25.754 18.327 6.753   1.00 16.06 ? 76  SER A C   1 
ATOM   575  O  O   . SER A 1 76  ? 25.733 17.180 7.271   1.00 13.94 ? 76  SER A O   1 
ATOM   576  C  CB  . SER A 1 76  ? 28.040 19.200 6.664   1.00 15.44 ? 76  SER A CB  1 
ATOM   577  O  OG  . SER A 1 76  ? 28.923 20.209 7.059   1.00 17.35 ? 76  SER A OG  1 
ATOM   578  N  N   . TYR A 1 77  ? 25.132 18.642 5.634   1.00 13.21 ? 77  TYR A N   1 
ATOM   579  C  CA  . TYR A 1 77  ? 24.257 17.666 4.963   1.00 13.23 ? 77  TYR A CA  1 
ATOM   580  C  C   . TYR A 1 77  ? 24.315 17.891 3.454   1.00 13.91 ? 77  TYR A C   1 
ATOM   581  O  O   . TYR A 1 77  ? 24.113 19.027 2.994   1.00 14.25 ? 77  TYR A O   1 
ATOM   582  C  CB  . TYR A 1 77  ? 22.826 17.734 5.483   1.00 13.42 ? 77  TYR A CB  1 
ATOM   583  C  CG  . TYR A 1 77  ? 21.884 16.711 4.896   1.00 14.22 ? 77  TYR A CG  1 
ATOM   584  C  CD1 . TYR A 1 77  ? 22.116 15.345 5.084   1.00 16.31 ? 77  TYR A CD1 1 
ATOM   585  C  CD2 . TYR A 1 77  ? 20.739 17.080 4.213   1.00 15.36 ? 77  TYR A CD2 1 
ATOM   586  C  CE1 . TYR A 1 77  ? 21.246 14.379 4.573   1.00 17.01 ? 77  TYR A CE1 1 
ATOM   587  C  CE2 . TYR A 1 77  ? 19.853 16.130 3.720   1.00 16.10 ? 77  TYR A CE2 1 
ATOM   588  C  CZ  . TYR A 1 77  ? 20.105 14.783 3.904   1.00 17.27 ? 77  TYR A CZ  1 
ATOM   589  O  OH  . TYR A 1 77  ? 19.239 13.877 3.375   1.00 22.78 ? 77  TYR A OH  1 
ATOM   590  N  N   . ASP A 1 78  ? 24.523 16.810 2.705   1.00 13.76 ? 78  ASP A N   1 
ATOM   591  C  CA  . ASP A 1 78  ? 24.446 16.869 1.220   1.00 14.73 ? 78  ASP A CA  1 
ATOM   592  C  C   . ASP A 1 78  ? 22.989 16.957 0.802   1.00 14.36 ? 78  ASP A C   1 
ATOM   593  O  O   . ASP A 1 78  ? 22.169 15.987 1.062   1.00 15.45 ? 78  ASP A O   1 
ATOM   594  C  CB  . ASP A 1 78  ? 25.137 15.675 0.585   1.00 15.66 ? 78  ASP A CB  1 
ATOM   595  C  CG  . ASP A 1 78  ? 26.640 15.685 0.667   1.00 19.82 ? 78  ASP A CG  1 
ATOM   596  O  OD1 . ASP A 1 78  ? 27.239 16.731 0.932   1.00 21.55 ? 78  ASP A OD1 1 
ATOM   597  O  OD2 . ASP A 1 78  ? 27.203 14.613 0.450   1.00 25.62 ? 78  ASP A OD2 1 
ATOM   598  N  N   . VAL A 1 79  ? 22.655 18.058 0.142   1.00 14.17 ? 79  VAL A N   1 
ATOM   599  C  CA  . VAL A 1 79  ? 21.268 18.311 -0.344  1.00 14.78 ? 79  VAL A CA  1 
ATOM   600  C  C   . VAL A 1 79  ? 21.328 19.322 -1.487  1.00 16.07 ? 79  VAL A C   1 
ATOM   601  O  O   . VAL A 1 79  ? 22.051 20.297 -1.406  1.00 16.12 ? 79  VAL A O   1 
ATOM   602  C  CB  . VAL A 1 79  ? 20.322 18.793 0.760   1.00 16.85 ? 79  VAL A CB  1 
ATOM   603  C  CG1 . VAL A 1 79  ? 20.857 20.020 1.484   1.00 16.87 ? 79  VAL A CG1 1 
ATOM   604  C  CG2 . VAL A 1 79  ? 18.926 19.070 0.214   1.00 19.40 ? 79  VAL A CG2 1 
ATOM   605  N  N   . ASP A 1 80  ? 20.638 18.993 -2.563  1.00 15.17 ? 80  ASP A N   1 
ATOM   606  C  CA  . ASP A 1 80  ? 20.428 19.912 -3.698  1.00 15.13 ? 80  ASP A CA  1 
ATOM   607  C  C   . ASP A 1 80  ? 19.212 20.790 -3.419  1.00 14.91 ? 80  ASP A C   1 
ATOM   608  O  O   . ASP A 1 80  ? 18.094 20.308 -3.541  1.00 15.03 ? 80  ASP A O   1 
ATOM   609  C  CB  . ASP A 1 80  ? 20.272 19.126 -4.990  1.00 15.41 ? 80  ASP A CB  1 
ATOM   610  C  CG  . ASP A 1 80  ? 20.293 20.048 -6.185  1.00 18.67 ? 80  ASP A CG  1 
ATOM   611  O  OD1 . ASP A 1 80  ? 20.251 21.257 -5.982  1.00 17.85 ? 80  ASP A OD1 1 
ATOM   612  O  OD2 . ASP A 1 80  ? 20.349 19.509 -7.325  1.00 21.06 ? 80  ASP A OD2 1 
ATOM   613  N  N   . LEU A 1 81  ? 19.432 22.022 -2.955  1.00 14.10 ? 81  LEU A N   1 
ATOM   614  C  CA  . LEU A 1 81  ? 18.290 22.893 -2.602  1.00 14.44 ? 81  LEU A CA  1 
ATOM   615  C  C   . LEU A 1 81  ? 17.450 23.206 -3.834  1.00 15.90 ? 81  LEU A C   1 
ATOM   616  O  O   . LEU A 1 81  ? 16.273 23.496 -3.604  1.00 15.65 ? 81  LEU A O   1 
ATOM   617  C  CB  . LEU A 1 81  ? 18.755 24.132 -1.840  1.00 14.88 ? 81  LEU A CB  1 
ATOM   618  C  CG  . LEU A 1 81  ? 19.360 23.793 -0.487  1.00 15.42 ? 81  LEU A CG  1 
ATOM   619  C  CD1 . LEU A 1 81  ? 19.801 25.055 0.216   1.00 15.80 ? 81  LEU A CD1 1 
ATOM   620  C  CD2 . LEU A 1 81  ? 18.425 22.995 0.391   1.00 17.30 ? 81  LEU A CD2 1 
ATOM   621  N  N   . ASP A 1 82  ? 17.967 23.070 -5.067  1.00 15.73 ? 82  ASP A N   1 
ATOM   622  C  CA  . ASP A 1 82  ? 17.123 23.292 -6.274  1.00 18.52 ? 82  ASP A CA  1 
ATOM   623  C  C   . ASP A 1 82  ? 16.050 22.183 -6.381  1.00 18.25 ? 82  ASP A C   1 
ATOM   624  O  O   . ASP A 1 82  ? 15.048 22.422 -7.099  1.00 17.10 ? 82  ASP A O   1 
ATOM   625  C  CB  . ASP A 1 82  ? 17.851 23.300 -7.625  1.00 22.88 ? 82  ASP A CB  1 
ATOM   626  C  CG  . ASP A 1 82  ? 19.178 24.026 -7.876  1.00 31.59 ? 82  ASP A CG  1 
ATOM   627  O  OD1 . ASP A 1 82  ? 19.407 25.078 -7.277  1.00 28.08 ? 82  ASP A OD1 1 
ATOM   628  O  OD2 . ASP A 1 82  ? 19.964 23.524 -8.777  1.00 33.23 ? 82  ASP A OD2 1 
ATOM   629  N  N   . ASN A 1 83  ? 16.170 21.062 -5.643  1.00 15.40 ? 83  ASN A N   1 
ATOM   630  C  CA  . ASN A 1 83  ? 15.183 19.958 -5.662  1.00 17.02 ? 83  ASN A CA  1 
ATOM   631  C  C   . ASN A 1 83  ? 14.234 20.068 -4.470  1.00 17.35 ? 83  ASN A C   1 
ATOM   632  O  O   . ASN A 1 83  ? 13.339 19.202 -4.348  1.00 18.44 ? 83  ASN A O   1 
ATOM   633  C  CB  . ASN A 1 83  ? 15.916 18.618 -5.613  1.00 16.65 ? 83  ASN A CB  1 
ATOM   634  C  CG  . ASN A 1 83  ? 16.567 18.289 -6.931  1.00 17.31 ? 83  ASN A CG  1 
ATOM   635  O  OD1 . ASN A 1 83  ? 16.267 18.918 -7.961  1.00 16.56 ? 83  ASN A OD1 1 
ATOM   636  N  ND2 . ASN A 1 83  ? 17.469 17.332 -6.896  1.00 19.96 ? 83  ASN A ND2 1 
ATOM   637  N  N   . VAL A 1 84  ? 14.501 20.989 -3.548  1.00 14.75 ? 84  VAL A N   1 
ATOM   638  C  CA  . VAL A 1 84  ? 13.675 21.142 -2.322  1.00 15.31 ? 84  VAL A CA  1 
ATOM   639  C  C   . VAL A 1 84  ? 12.882 22.437 -2.393  1.00 15.10 ? 84  VAL A C   1 
ATOM   640  O  O   . VAL A 1 84  ? 11.658 22.377 -2.170  1.00 19.00 ? 84  VAL A O   1 
ATOM   641  C  CB  . VAL A 1 84  ? 14.563 21.064 -1.071  1.00 17.09 ? 84  VAL A CB  1 
ATOM   642  C  CG1 . VAL A 1 84  ? 13.704 21.232 0.174   1.00 17.33 ? 84  VAL A CG1 1 
ATOM   643  C  CG2 . VAL A 1 84  ? 15.314 19.752 -1.050  1.00 18.81 ? 84  VAL A CG2 1 
ATOM   644  N  N   . LEU A 1 85  ? 13.525 23.560 -2.718  1.00 14.28 ? 85  LEU A N   1 
ATOM   645  C  CA  . LEU A 1 85  ? 12.932 24.901 -2.594  1.00 14.27 ? 85  LEU A CA  1 
ATOM   646  C  C   . LEU A 1 85  ? 12.525 25.438 -3.956  1.00 14.54 ? 85  LEU A C   1 
ATOM   647  O  O   . LEU A 1 85  ? 13.103 25.033 -4.966  1.00 14.47 ? 85  LEU A O   1 
ATOM   648  C  CB  . LEU A 1 85  ? 13.974 25.832 -1.974  1.00 14.35 ? 85  LEU A CB  1 
ATOM   649  C  CG  . LEU A 1 85  ? 14.244 25.599 -0.496  1.00 14.62 ? 85  LEU A CG  1 
ATOM   650  C  CD1 . LEU A 1 85  ? 15.501 26.334 -0.088  1.00 15.25 ? 85  LEU A CD1 1 
ATOM   651  C  CD2 . LEU A 1 85  ? 13.074 26.039 0.327   1.00 16.95 ? 85  LEU A CD2 1 
ATOM   652  N  N   . PRO A 1 86  ? 11.535 26.346 -3.984  1.00 15.18 ? 86  PRO A N   1 
ATOM   653  C  CA  . PRO A 1 86  ? 11.183 27.071 -5.208  1.00 16.08 ? 86  PRO A CA  1 
ATOM   654  C  C   . PRO A 1 86  ? 12.352 28.010 -5.600  1.00 15.74 ? 86  PRO A C   1 
ATOM   655  O  O   . PRO A 1 86  ? 13.264 28.256 -4.761  1.00 14.88 ? 86  PRO A O   1 
ATOM   656  C  CB  . PRO A 1 86  ? 9.909  27.795 -4.804  1.00 15.55 ? 86  PRO A CB  1 
ATOM   657  C  CG  . PRO A 1 86  ? 9.964  27.949 -3.311  1.00 15.63 ? 86  PRO A CG  1 
ATOM   658  C  CD  . PRO A 1 86  ? 10.777 26.794 -2.806  1.00 15.01 ? 86  PRO A CD  1 
ATOM   659  N  N   . GLU A 1 87  ? 12.307 28.583 -6.806  1.00 13.44 ? 87  GLU A N   1 
ATOM   660  C  CA  . GLU A 1 87  ? 13.397 29.457 -7.309  1.00 15.42 ? 87  GLU A CA  1 
ATOM   661  C  C   . GLU A 1 87  ? 13.443 30.802 -6.565  1.00 13.30 ? 87  GLU A C   1 
ATOM   662  O  O   . GLU A 1 87  ? 14.520 31.386 -6.464  1.00 13.39 ? 87  GLU A O   1 
ATOM   663  C  CB  . GLU A 1 87  ? 13.323 29.583 -8.833  1.00 17.66 ? 87  GLU A CB  1 
ATOM   664  C  CG  . GLU A 1 87  ? 12.533 30.720 -9.406  1.00 22.72 ? 87  GLU A CG  1 
ATOM   665  C  CD  . GLU A 1 87  ? 12.714 30.867 -10.932 1.00 25.80 ? 87  GLU A CD  1 
ATOM   666  O  OE1 . GLU A 1 87  ? 12.221 30.000 -11.642 1.00 23.09 ? 87  GLU A OE1 1 
ATOM   667  O  OE2 . GLU A 1 87  ? 13.438 31.815 -11.400 1.00 23.88 ? 87  GLU A OE2 1 
ATOM   668  N  N   . TRP A 1 88  ? 12.317 31.276 -6.052  1.00 11.77 ? 88  TRP A N   1 
ATOM   669  C  CA  . TRP A 1 88  ? 12.214 32.479 -5.199  1.00 11.62 ? 88  TRP A CA  1 
ATOM   670  C  C   . TRP A 1 88  ? 11.803 32.062 -3.797  1.00 12.33 ? 88  TRP A C   1 
ATOM   671  O  O   . TRP A 1 88  ? 10.856 31.258 -3.655  1.00 12.30 ? 88  TRP A O   1 
ATOM   672  C  CB  . TRP A 1 88  ? 11.207 33.501 -5.762  1.00 12.38 ? 88  TRP A CB  1 
ATOM   673  C  CG  . TRP A 1 88  ? 11.658 34.201 -7.004  1.00 12.63 ? 88  TRP A CG  1 
ATOM   674  C  CD1 . TRP A 1 88  ? 11.453 33.845 -8.318  1.00 13.42 ? 88  TRP A CD1 1 
ATOM   675  C  CD2 . TRP A 1 88  ? 12.506 35.354 -7.054  1.00 13.03 ? 88  TRP A CD2 1 
ATOM   676  N  NE1 . TRP A 1 88  ? 12.037 34.749 -9.152  1.00 13.04 ? 88  TRP A NE1 1 
ATOM   677  C  CE2 . TRP A 1 88  ? 12.698 35.684 -8.420  1.00 13.18 ? 88  TRP A CE2 1 
ATOM   678  C  CE3 . TRP A 1 88  ? 13.038 36.197 -6.082  1.00 13.34 ? 88  TRP A CE3 1 
ATOM   679  C  CZ2 . TRP A 1 88  ? 13.433 36.800 -8.819  1.00 14.23 ? 88  TRP A CZ2 1 
ATOM   680  C  CZ3 . TRP A 1 88  ? 13.742 37.309 -6.486  1.00 14.63 ? 88  TRP A CZ3 1 
ATOM   681  C  CH2 . TRP A 1 88  ? 13.940 37.600 -7.835  1.00 14.96 ? 88  TRP A CH2 1 
ATOM   682  N  N   . VAL A 1 89  ? 12.504 32.560 -2.805  1.00 11.69 ? 89  VAL A N   1 
ATOM   683  C  CA  . VAL A 1 89  ? 12.260 32.182 -1.397  1.00 11.37 ? 89  VAL A CA  1 
ATOM   684  C  C   . VAL A 1 89  ? 12.244 33.432 -0.538  1.00 11.98 ? 89  VAL A C   1 
ATOM   685  O  O   . VAL A 1 89  ? 12.702 34.500 -0.992  1.00 12.74 ? 89  VAL A O   1 
ATOM   686  C  CB  . VAL A 1 89  ? 13.330 31.199 -0.911  1.00 11.15 ? 89  VAL A CB  1 
ATOM   687  C  CG1 . VAL A 1 89  ? 13.215 29.859 -1.636  1.00 12.13 ? 89  VAL A CG1 1 
ATOM   688  C  CG2 . VAL A 1 89  ? 14.728 31.788 -1.028  1.00 12.07 ? 89  VAL A CG2 1 
ATOM   689  N  N   . ARG A 1 90  ? 11.833 33.271 0.720   1.00 11.15 ? 90  ARG A N   1 
ATOM   690  C  CA  . ARG A 1 90  ? 12.188 34.253 1.766   1.00 11.23 ? 90  ARG A CA  1 
ATOM   691  C  C   . ARG A 1 90  ? 13.087 33.564 2.782   1.00 10.62 ? 90  ARG A C   1 
ATOM   692  O  O   . ARG A 1 90  ? 13.049 32.336 2.900   1.00 10.79 ? 90  ARG A O   1 
ATOM   693  C  CB  . ARG A 1 90  ? 10.966 34.897 2.413   1.00 12.58 ? 90  ARG A CB  1 
ATOM   694  C  CG  . ARG A 1 90  ? 10.408 36.055 1.585   1.00 13.71 ? 90  ARG A CG  1 
ATOM   695  C  CD  . ARG A 1 90  ? 9.424  36.856 2.414   1.00 14.78 ? 90  ARG A CD  1 
ATOM   696  N  NE  . ARG A 1 90  ? 9.084  38.122 1.753   1.00 16.18 ? 90  ARG A NE  1 
ATOM   697  C  CZ  . ARG A 1 90  ? 7.911  38.396 1.164   1.00 18.35 ? 90  ARG A CZ  1 
ATOM   698  N  NH1 . ARG A 1 90  ? 7.005  37.453 1.020   1.00 21.63 ? 90  ARG A NH1 1 
ATOM   699  N  NH2 . ARG A 1 90  ? 7.695  39.580 0.611   1.00 19.00 ? 90  ARG A NH2 1 
ATOM   700  N  N   . VAL A 1 91  ? 13.914 34.368 3.437   1.00 10.39 ? 91  VAL A N   1 
ATOM   701  C  CA  . VAL A 1 91  ? 14.809 33.868 4.504   1.00 10.24 ? 91  VAL A CA  1 
ATOM   702  C  C   . VAL A 1 91  ? 14.409 34.510 5.816   1.00 10.79 ? 91  VAL A C   1 
ATOM   703  O  O   . VAL A 1 91  ? 13.865 35.641 5.840   1.00 10.23 ? 91  VAL A O   1 
ATOM   704  C  CB  . VAL A 1 91  ? 16.294 34.114 4.200   1.00 11.59 ? 91  VAL A CB  1 
ATOM   705  C  CG1 . VAL A 1 91  ? 16.678 33.304 2.965   1.00 12.35 ? 91  VAL A CG1 1 
ATOM   706  C  CG2 . VAL A 1 91  ? 16.597 35.582 4.036   1.00 11.79 ? 91  VAL A CG2 1 
ATOM   707  N  N   . GLY A 1 92  ? 14.613 33.779 6.888   1.00 9.49  ? 92  GLY A N   1 
ATOM   708  C  CA  . GLY A 1 92  ? 14.213 34.309 8.186   1.00 10.52 ? 92  GLY A CA  1 
ATOM   709  C  C   . GLY A 1 92  ? 14.754 33.535 9.363   1.00 9.76  ? 92  GLY A C   1 
ATOM   710  O  O   . GLY A 1 92  ? 15.544 32.581 9.219   1.00 10.03 ? 92  GLY A O   1 
ATOM   711  N  N   . LEU A 1 93  ? 14.374 34.030 10.532  1.00 9.89  ? 93  LEU A N   1 
ATOM   712  C  CA  . LEU A 1 93  ? 14.694 33.411 11.833  1.00 9.83  ? 93  LEU A CA  1 
ATOM   713  C  C   . LEU A 1 93  ? 13.365 33.026 12.480  1.00 10.48 ? 93  LEU A C   1 
ATOM   714  O  O   . LEU A 1 93  ? 12.388 33.797 12.428  1.00 10.96 ? 93  LEU A O   1 
ATOM   715  C  CB  . LEU A 1 93  ? 15.500 34.412 12.660  1.00 10.12 ? 93  LEU A CB  1 
ATOM   716  C  CG  . LEU A 1 93  ? 16.821 34.884 12.046  1.00 11.95 ? 93  LEU A CG  1 
ATOM   717  C  CD1 . LEU A 1 93  ? 17.433 35.982 12.890  1.00 11.84 ? 93  LEU A CD1 1 
ATOM   718  C  CD2 . LEU A 1 93  ? 17.795 33.748 11.976  1.00 14.23 ? 93  LEU A CD2 1 
ATOM   719  N  N   . SER A 1 94  ? 13.345 31.907 13.179  1.00 10.36 ? 94  SER A N   1 
ATOM   720  C  CA  . SER A 1 94  ? 12.176 31.446 13.941  1.00 10.56 ? 94  SER A CA  1 
ATOM   721  C  C   . SER A 1 94  ? 12.594 30.979 15.324  1.00 10.66 ? 94  SER A C   1 
ATOM   722  O  O   . SER A 1 94  ? 13.748 30.581 15.501  1.00 10.51 ? 94  SER A O   1 
ATOM   723  C  CB  . SER A 1 94  ? 11.558 30.320 13.196  1.00 11.11 ? 94  SER A CB  1 
ATOM   724  O  OG  . SER A 1 94  ? 10.308 29.943 13.752  1.00 13.40 ? 94  SER A OG  1 
ATOM   725  N  N   . ALA A 1 95  ? 11.680 31.050 16.285  1.00 11.26 ? 95  ALA A N   1 
ATOM   726  C  CA  . ALA A 1 95  ? 11.971 30.530 17.641  1.00 11.13 ? 95  ALA A CA  1 
ATOM   727  C  C   . ALA A 1 95  ? 10.665 30.171 18.318  1.00 11.72 ? 95  ALA A C   1 
ATOM   728  O  O   . ALA A 1 95  ? 9.619  30.650 17.915  1.00 10.04 ? 95  ALA A O   1 
ATOM   729  C  CB  . ALA A 1 95  ? 12.784 31.475 18.463  1.00 11.36 ? 95  ALA A CB  1 
ATOM   730  N  N   . SER A 1 96  ? 10.758 29.335 19.338  1.00 11.26 ? 96  SER A N   1 
ATOM   731  C  CA  . SER A 1 96  ? 9.566  28.938 20.085  1.00 12.43 ? 96  SER A CA  1 
ATOM   732  C  C   . SER A 1 96  ? 9.944  28.621 21.522  1.00 12.32 ? 96  SER A C   1 
ATOM   733  O  O   . SER A 1 96  ? 11.105 28.374 21.826  1.00 11.29 ? 96  SER A O   1 
ATOM   734  C  CB  . SER A 1 96  ? 8.928  27.756 19.448  1.00 13.07 ? 96  SER A CB  1 
ATOM   735  O  OG  . SER A 1 96  ? 9.831  26.645 19.477  1.00 12.98 ? 96  SER A OG  1 
ATOM   736  N  N   . THR A 1 97  ? 8.911  28.650 22.331  1.00 12.02 ? 97  THR A N   1 
ATOM   737  C  CA  . THR A 1 97  ? 8.921  28.101 23.693  1.00 12.20 ? 97  THR A CA  1 
ATOM   738  C  C   . THR A 1 97  ? 7.684  27.214 23.841  1.00 11.86 ? 97  THR A C   1 
ATOM   739  O  O   . THR A 1 97  ? 6.773  27.277 23.014  1.00 11.97 ? 97  THR A O   1 
ATOM   740  C  CB  . THR A 1 97  ? 8.985  29.220 24.745  1.00 12.26 ? 97  THR A CB  1 
ATOM   741  O  OG1 . THR A 1 97  ? 7.787  29.959 24.696  1.00 12.60 ? 97  THR A OG1 1 
ATOM   742  C  CG2 . THR A 1 97  ? 10.196 30.114 24.591  1.00 11.33 ? 97  THR A CG2 1 
ATOM   743  N  N   . GLY A 1 98  ? 7.642  26.417 24.912  1.00 12.61 ? 98  GLY A N   1 
ATOM   744  C  CA  . GLY A 1 98  ? 6.473  25.563 25.198  1.00 14.89 ? 98  GLY A CA  1 
ATOM   745  C  C   . GLY A 1 98  ? 6.177  25.595 26.681  1.00 14.34 ? 98  GLY A C   1 
ATOM   746  O  O   . GLY A 1 98  ? 6.104  26.696 27.241  1.00 15.36 ? 98  GLY A O   1 
ATOM   747  N  N   . LEU A 1 99  ? 6.100  24.407 27.318  1.00 15.88 ? 99  LEU A N   1 
ATOM   748  C  CA  . LEU A 1 99  ? 5.988  24.421 28.789  1.00 18.96 ? 99  LEU A CA  1 
ATOM   749  C  C   . LEU A 1 99  ? 7.349  24.825 29.382  1.00 17.09 ? 99  LEU A C   1 
ATOM   750  O  O   . LEU A 1 99  ? 7.385  25.430 30.461  1.00 21.12 ? 99  LEU A O   1 
ATOM   751  C  CB  . LEU A 1 99  ? 5.487  23.051 29.232  1.00 21.37 ? 99  LEU A CB  1 
ATOM   752  C  CG  . LEU A 1 99  ? 4.043  22.728 28.817  1.00 28.29 ? 99  LEU A CG  1 
ATOM   753  C  CD1 . LEU A 1 99  ? 3.578  21.444 29.501  1.00 31.46 ? 99  LEU A CD1 1 
ATOM   754  C  CD2 . LEU A 1 99  ? 3.053  23.880 29.091  1.00 30.31 ? 99  LEU A CD2 1 
ATOM   755  N  N   . TYR A 1 100 ? 8.441  24.467 28.722  1.00 13.78 ? 100 TYR A N   1 
ATOM   756  C  CA  . TYR A 1 100 ? 9.799  24.946 29.058  1.00 14.12 ? 100 TYR A CA  1 
ATOM   757  C  C   . TYR A 1 100 ? 10.086 26.177 28.175  1.00 13.27 ? 100 TYR A C   1 
ATOM   758  O  O   . TYR A 1 100 ? 9.533  26.299 27.082  1.00 13.10 ? 100 TYR A O   1 
ATOM   759  C  CB  . TYR A 1 100 ? 10.815 23.830 28.864  1.00 13.56 ? 100 TYR A CB  1 
ATOM   760  C  CG  . TYR A 1 100 ? 10.643 22.609 29.748  1.00 14.95 ? 100 TYR A CG  1 
ATOM   761  C  CD1 . TYR A 1 100 ? 9.857  21.538 29.359  1.00 17.00 ? 100 TYR A CD1 1 
ATOM   762  C  CD2 . TYR A 1 100 ? 11.326 22.510 30.941  1.00 16.09 ? 100 TYR A CD2 1 
ATOM   763  C  CE1 . TYR A 1 100 ? 9.734  20.400 30.133  1.00 18.13 ? 100 TYR A CE1 1 
ATOM   764  C  CE2 . TYR A 1 100 ? 11.233 21.347 31.711  1.00 18.35 ? 100 TYR A CE2 1 
ATOM   765  C  CZ  . TYR A 1 100 ? 10.436 20.302 31.308  1.00 18.00 ? 100 TYR A CZ  1 
ATOM   766  O  OH  . TYR A 1 100 ? 10.280 19.170 32.066  1.00 21.24 ? 100 TYR A OH  1 
ATOM   767  N  N   . LYS A 1 101 ? 10.942 27.068 28.652  1.00 13.19 ? 101 LYS A N   1 
ATOM   768  C  CA  . LYS A 1 101 ? 11.048 28.403 28.018  1.00 14.24 ? 101 LYS A CA  1 
ATOM   769  C  C   . LYS A 1 101 ? 12.480 28.954 28.111  1.00 12.94 ? 101 LYS A C   1 
ATOM   770  O  O   . LYS A 1 101 ? 13.337 28.435 28.835  1.00 14.20 ? 101 LYS A O   1 
ATOM   771  C  CB  . LYS A 1 101 ? 10.023 29.332 28.650  1.00 17.29 ? 101 LYS A CB  1 
ATOM   772  C  CG  . LYS A 1 101 ? 10.259 29.551 30.131  1.00 21.97 ? 101 LYS A CG  1 
ATOM   773  C  CD  . LYS A 1 101 ? 9.112  30.171 30.879  1.00 28.30 ? 101 LYS A CD  1 
ATOM   774  C  CE  . LYS A 1 101 ? 9.454  30.465 32.327  1.00 31.97 ? 101 LYS A CE  1 
ATOM   775  N  NZ  . LYS A 1 101 ? 9.862  29.249 33.063  1.00 34.13 ? 101 LYS A NZ  1 
ATOM   776  N  N   . GLU A 1 102 ? 12.709 29.996 27.325  1.00 11.85 ? 102 GLU A N   1 
ATOM   777  C  CA  . GLU A 1 102 ? 13.979 30.726 27.258  1.00 11.71 ? 102 GLU A CA  1 
ATOM   778  C  C   . GLU A 1 102 ? 13.718 32.016 26.470  1.00 11.14 ? 102 GLU A C   1 
ATOM   779  O  O   . GLU A 1 102 ? 12.663 32.071 25.757  1.00 12.37 ? 102 GLU A O   1 
ATOM   780  C  CB  . GLU A 1 102 ? 15.019 29.878 26.518  1.00 12.07 ? 102 GLU A CB  1 
ATOM   781  C  CG  . GLU A 1 102 ? 14.756 29.744 25.012  1.00 12.93 ? 102 GLU A CG  1 
ATOM   782  C  CD  . GLU A 1 102 ? 15.386 28.591 24.248  1.00 12.73 ? 102 GLU A CD  1 
ATOM   783  O  OE1 . GLU A 1 102 ? 15.803 27.657 24.875  1.00 12.20 ? 102 GLU A OE1 1 
ATOM   784  O  OE2 . GLU A 1 102 ? 15.475 28.675 22.940  1.00 12.34 ? 102 GLU A OE2 1 
ATOM   785  N  N   . THR A 1 103 ? 14.611 32.989 26.618  1.00 11.48 ? 103 THR A N   1 
ATOM   786  C  CA  . THR A 1 103 ? 14.668 34.131 25.663  1.00 11.85 ? 103 THR A CA  1 
ATOM   787  C  C   . THR A 1 103 ? 15.185 33.624 24.326  1.00 12.72 ? 103 THR A C   1 
ATOM   788  O  O   . THR A 1 103 ? 16.093 32.755 24.289  1.00 13.44 ? 103 THR A O   1 
ATOM   789  C  CB  . THR A 1 103 ? 15.520 35.282 26.169  1.00 13.27 ? 103 THR A CB  1 
ATOM   790  O  OG1 . THR A 1 103 ? 16.885 34.865 26.208  1.00 16.56 ? 103 THR A OG1 1 
ATOM   791  C  CG2 . THR A 1 103 ? 15.108 35.717 27.545  1.00 14.10 ? 103 THR A CG2 1 
ATOM   792  N  N   . ASN A 1 104 ? 14.692 34.186 23.245  1.00 11.66 ? 104 ASN A N   1 
ATOM   793  C  CA  . ASN A 1 104 ? 15.203 33.857 21.892  1.00 10.85 ? 104 ASN A CA  1 
ATOM   794  C  C   . ASN A 1 104 ? 15.598 35.180 21.235  1.00 11.74 ? 104 ASN A C   1 
ATOM   795  O  O   . ASN A 1 104 ? 14.942 35.606 20.293  1.00 13.17 ? 104 ASN A O   1 
ATOM   796  C  CB  . ASN A 1 104 ? 14.163 33.060 21.124  1.00 10.90 ? 104 ASN A CB  1 
ATOM   797  C  CG  . ASN A 1 104 ? 13.964 31.693 21.735  1.00 11.60 ? 104 ASN A CG  1 
ATOM   798  O  OD1 . ASN A 1 104 ? 12.823 31.362 22.140  1.00 15.95 ? 104 ASN A OD1 1 
ATOM   799  N  ND2 . ASN A 1 104 ? 15.034 30.918 21.770  1.00 9.14  ? 104 ASN A ND2 1 
ATOM   800  N  N   . THR A 1 105 ? 16.607 35.811 21.791  1.00 11.14 ? 105 THR A N   1 
ATOM   801  C  CA  . THR A 1 105 ? 17.003 37.189 21.452  1.00 12.13 ? 105 THR A CA  1 
ATOM   802  C  C   . THR A 1 105 ? 18.019 37.165 20.338  1.00 11.27 ? 105 THR A C   1 
ATOM   803  O  O   . THR A 1 105 ? 19.025 36.462 20.444  1.00 11.31 ? 105 THR A O   1 
ATOM   804  C  CB  . THR A 1 105 ? 17.603 37.903 22.659  1.00 14.43 ? 105 THR A CB  1 
ATOM   805  O  OG1 . THR A 1 105 ? 16.694 37.716 23.749  1.00 15.79 ? 105 THR A OG1 1 
ATOM   806  C  CG2 . THR A 1 105 ? 17.823 39.365 22.382  1.00 15.15 ? 105 THR A CG2 1 
ATOM   807  N  N   . ILE A 1 106 ? 17.774 37.921 19.274  1.00 10.99 ? 106 ILE A N   1 
ATOM   808  C  CA  . ILE A 1 106 ? 18.701 38.058 18.141  1.00 10.90 ? 106 ILE A CA  1 
ATOM   809  C  C   . ILE A 1 106 ? 19.332 39.443 18.236  1.00 10.36 ? 106 ILE A C   1 
ATOM   810  O  O   . ILE A 1 106 ? 18.604 40.472 18.261  1.00 10.07 ? 106 ILE A O   1 
ATOM   811  C  CB  . ILE A 1 106 ? 17.955 37.852 16.807  1.00 11.38 ? 106 ILE A CB  1 
ATOM   812  C  CG1 . ILE A 1 106 ? 17.218 36.515 16.715  1.00 11.52 ? 106 ILE A CG1 1 
ATOM   813  C  CG2 . ILE A 1 106 ? 18.929 38.107 15.629  1.00 11.32 ? 106 ILE A CG2 1 
ATOM   814  C  CD1 . ILE A 1 106 ? 18.115 35.321 16.834  1.00 12.65 ? 106 ILE A CD1 1 
ATOM   815  N  N   . LEU A 1 107 ? 20.673 39.507 18.314  1.00 11.00 ? 107 LEU A N   1 
ATOM   816  C  CA  . LEU A 1 107 ? 21.421 40.757 18.444  1.00 12.74 ? 107 LEU A CA  1 
ATOM   817  C  C   . LEU A 1 107 ? 21.901 41.254 17.081  1.00 11.62 ? 107 LEU A C   1 
ATOM   818  O  O   . LEU A 1 107 ? 22.049 42.471 16.923  1.00 13.05 ? 107 LEU A O   1 
ATOM   819  C  CB  . LEU A 1 107 ? 22.628 40.559 19.353  1.00 13.69 ? 107 LEU A CB  1 
ATOM   820  C  CG  . LEU A 1 107 ? 22.336 40.461 20.842  1.00 17.96 ? 107 LEU A CG  1 
ATOM   821  C  CD1 . LEU A 1 107 ? 21.691 39.160 21.189  1.00 20.32 ? 107 LEU A CD1 1 
ATOM   822  C  CD2 . LEU A 1 107 ? 23.642 40.567 21.629  1.00 21.76 ? 107 LEU A CD2 1 
ATOM   823  N  N   . SER A 1 108 ? 22.117 40.361 16.126  1.00 10.22 ? 108 SER A N   1 
ATOM   824  C  CA  . SER A 1 108 ? 22.519 40.785 14.766  1.00 11.83 ? 108 SER A CA  1 
ATOM   825  C  C   . SER A 1 108 ? 22.185 39.673 13.793  1.00 11.24 ? 108 SER A C   1 
ATOM   826  O  O   . SER A 1 108 ? 22.085 38.495 14.199  1.00 11.72 ? 108 SER A O   1 
ATOM   827  C  CB  . SER A 1 108 ? 24.002 41.117 14.707  1.00 13.42 ? 108 SER A CB  1 
ATOM   828  O  OG  . SER A 1 108 ? 24.752 39.951 14.957  1.00 16.30 ? 108 SER A OG  1 
ATOM   829  N  N   . TRP A 1 109 ? 22.025 40.040 12.527  1.00 10.63 ? 109 TRP A N   1 
ATOM   830  C  CA  . TRP A 1 109 ? 21.670 39.053 11.479  1.00 10.90 ? 109 TRP A CA  1 
ATOM   831  C  C   . TRP A 1 109 ? 22.154 39.608 10.158  1.00 11.13 ? 109 TRP A C   1 
ATOM   832  O  O   . TRP A 1 109 ? 21.838 40.753 9.836   1.00 12.19 ? 109 TRP A O   1 
ATOM   833  C  CB  . TRP A 1 109 ? 20.170 38.793 11.460  1.00 10.21 ? 109 TRP A CB  1 
ATOM   834  C  CG  . TRP A 1 109 ? 19.659 37.831 10.422  1.00 11.05 ? 109 TRP A CG  1 
ATOM   835  C  CD1 . TRP A 1 109 ? 20.322 36.777 9.856   1.00 11.98 ? 109 TRP A CD1 1 
ATOM   836  C  CD2 . TRP A 1 109 ? 18.338 37.821 9.838   1.00 11.90 ? 109 TRP A CD2 1 
ATOM   837  N  NE1 . TRP A 1 109 ? 19.517 36.112 8.972   1.00 12.60 ? 109 TRP A NE1 1 
ATOM   838  C  CE2 . TRP A 1 109 ? 18.311 36.751 8.918   1.00 12.45 ? 109 TRP A CE2 1 
ATOM   839  C  CE3 . TRP A 1 109 ? 17.202 38.622 9.990   1.00 14.25 ? 109 TRP A CE3 1 
ATOM   840  C  CZ2 . TRP A 1 109 ? 17.186 36.430 8.178   1.00 13.41 ? 109 TRP A CZ2 1 
ATOM   841  C  CZ3 . TRP A 1 109 ? 16.088 38.311 9.231   1.00 15.10 ? 109 TRP A CZ3 1 
ATOM   842  C  CH2 . TRP A 1 109 ? 16.096 37.255 8.325   1.00 14.14 ? 109 TRP A CH2 1 
ATOM   843  N  N   . SER A 1 110 ? 22.951 38.826 9.446   1.00 11.31 ? 110 SER A N   1 
ATOM   844  C  CA  . SER A 1 110 ? 23.398 39.212 8.091   1.00 12.03 ? 110 SER A CA  1 
ATOM   845  C  C   . SER A 1 110 ? 23.190 38.049 7.136   1.00 11.76 ? 110 SER A C   1 
ATOM   846  O  O   . SER A 1 110 ? 23.113 36.869 7.550   1.00 11.39 ? 110 SER A O   1 
ATOM   847  C  CB  . SER A 1 110 ? 24.800 39.693 8.126   1.00 14.86 ? 110 SER A CB  1 
ATOM   848  O  OG  . SER A 1 110 ? 25.654 38.637 8.412   1.00 19.90 ? 110 SER A OG  1 
ATOM   849  N  N   . PHE A 1 111 ? 23.068 38.382 5.852   1.00 10.31 ? 111 PHE A N   1 
ATOM   850  C  CA  . PHE A 1 111 ? 22.735 37.407 4.820   1.00 10.03 ? 111 PHE A CA  1 
ATOM   851  C  C   . PHE A 1 111 ? 23.288 37.912 3.509   1.00 10.14 ? 111 PHE A C   1 
ATOM   852  O  O   . PHE A 1 111 ? 23.190 39.102 3.266   1.00 10.95 ? 111 PHE A O   1 
ATOM   853  C  CB  . PHE A 1 111 ? 21.217 37.207 4.703   1.00 10.38 ? 111 PHE A CB  1 
ATOM   854  C  CG  . PHE A 1 111 ? 20.821 36.264 3.592   1.00 10.80 ? 111 PHE A CG  1 
ATOM   855  C  CD1 . PHE A 1 111 ? 20.847 34.882 3.765   1.00 11.87 ? 111 PHE A CD1 1 
ATOM   856  C  CD2 . PHE A 1 111 ? 20.419 36.726 2.364   1.00 11.82 ? 111 PHE A CD2 1 
ATOM   857  C  CE1 . PHE A 1 111 ? 20.517 34.008 2.742   1.00 11.13 ? 111 PHE A CE1 1 
ATOM   858  C  CE2 . PHE A 1 111 ? 20.072 35.847 1.349   1.00 12.58 ? 111 PHE A CE2 1 
ATOM   859  C  CZ  . PHE A 1 111 ? 20.139 34.499 1.523   1.00 11.69 ? 111 PHE A CZ  1 
ATOM   860  N  N   . THR A 1 112 ? 23.876 37.024 2.720   1.00 10.26 ? 112 THR A N   1 
ATOM   861  C  CA  . THR A 1 112 ? 24.315 37.342 1.356   1.00 11.47 ? 112 THR A CA  1 
ATOM   862  C  C   . THR A 1 112 ? 23.877 36.193 0.461   1.00 12.78 ? 112 THR A C   1 
ATOM   863  O  O   . THR A 1 112 ? 24.142 35.028 0.798   1.00 12.74 ? 112 THR A O   1 
ATOM   864  C  CB  . THR A 1 112 ? 25.841 37.547 1.271   1.00 13.14 ? 112 THR A CB  1 
ATOM   865  O  OG1 . THR A 1 112 ? 26.274 38.557 2.194   1.00 17.12 ? 112 THR A OG1 1 
ATOM   866  C  CG2 . THR A 1 112 ? 26.208 37.943 -0.139  1.00 14.11 ? 112 THR A CG2 1 
ATOM   867  N  N   . SER A 1 113 ? 23.303 36.489 -0.688  1.00 12.27 ? 113 SER A N   1 
ATOM   868  C  CA  . SER A 1 113 ? 22.972 35.522 -1.741  1.00 13.01 ? 113 SER A CA  1 
ATOM   869  C  C   . SER A 1 113 ? 23.594 36.033 -3.035  1.00 14.21 ? 113 SER A C   1 
ATOM   870  O  O   . SER A 1 113 ? 23.516 37.240 -3.298  1.00 14.15 ? 113 SER A O   1 
ATOM   871  C  CB  . SER A 1 113 ? 21.489 35.440 -1.928  1.00 16.68 ? 113 SER A CB  1 
ATOM   872  O  OG  . SER A 1 113 ? 21.197 34.463 -2.895  1.00 24.86 ? 113 SER A OG  1 
ATOM   873  N  N   . LYS A 1 114 ? 24.148 35.138 -3.826  1.00 14.10 ? 114 LYS A N   1 
ATOM   874  C  CA  . LYS A 1 114 ? 24.741 35.482 -5.133  1.00 13.93 ? 114 LYS A CA  1 
ATOM   875  C  C   . LYS A 1 114 ? 24.278 34.456 -6.161  1.00 14.05 ? 114 LYS A C   1 
ATOM   876  O  O   . LYS A 1 114 ? 24.164 33.241 -5.853  1.00 15.68 ? 114 LYS A O   1 
ATOM   877  C  CB  . LYS A 1 114 ? 26.264 35.466 -5.059  1.00 17.42 ? 114 LYS A CB  1 
ATOM   878  C  CG  . LYS A 1 114 ? 26.851 36.540 -4.167  1.00 21.28 ? 114 LYS A CG  1 
ATOM   879  C  CD  . LYS A 1 114 ? 28.351 36.466 -4.067  1.00 28.47 ? 114 LYS A CD  1 
ATOM   880  C  CE  . LYS A 1 114 ? 28.865 37.265 -2.881  1.00 33.88 ? 114 LYS A CE  1 
ATOM   881  N  NZ  . LYS A 1 114 ? 30.325 37.509 -2.952  1.00 39.86 ? 114 LYS A NZ  1 
ATOM   882  N  N   . LEU A 1 115 ? 23.988 34.918 -7.361  1.00 13.35 ? 115 LEU A N   1 
ATOM   883  C  CA  . LEU A 1 115 ? 23.609 34.059 -8.499  1.00 15.89 ? 115 LEU A CA  1 
ATOM   884  C  C   . LEU A 1 115 ? 24.504 34.517 -9.630  1.00 17.00 ? 115 LEU A C   1 
ATOM   885  O  O   . LEU A 1 115 ? 24.319 35.689 -10.055 1.00 17.00 ? 115 LEU A O   1 
ATOM   886  C  CB  . LEU A 1 115 ? 22.166 34.322 -8.927  1.00 20.25 ? 115 LEU A CB  1 
ATOM   887  C  CG  . LEU A 1 115 ? 21.024 33.504 -8.385  1.00 24.27 ? 115 LEU A CG  1 
ATOM   888  C  CD1 . LEU A 1 115 ? 19.757 33.907 -9.148  1.00 21.05 ? 115 LEU A CD1 1 
ATOM   889  C  CD2 . LEU A 1 115 ? 21.284 32.023 -8.544  1.00 22.37 ? 115 LEU A CD2 1 
ATOM   890  N  N   . LYS A 1 116 ? 25.441 33.698 -10.053 1.00 16.04 ? 116 LYS A N   1 
ATOM   891  C  CA  . LYS A 1 116 ? 26.370 34.065 -11.131 1.00 18.79 ? 116 LYS A CA  1 
ATOM   892  C  C   . LYS A 1 116 ? 25.953 33.320 -12.395 1.00 20.34 ? 116 LYS A C   1 
ATOM   893  O  O   . LYS A 1 116 ? 25.826 32.110 -12.328 1.00 20.14 ? 116 LYS A O   1 
ATOM   894  C  CB  . LYS A 1 116 ? 27.771 33.754 -10.647 1.00 19.19 ? 116 LYS A CB  1 
ATOM   895  C  CG  . LYS A 1 116 ? 28.037 34.432 -9.315  1.00 24.76 ? 116 LYS A CG  1 
ATOM   896  C  CD  . LYS A 1 116 ? 29.483 34.551 -8.941  1.00 29.15 ? 116 LYS A CD  1 
ATOM   897  C  CE  . LYS A 1 116 ? 29.700 35.371 -7.682  1.00 32.26 ? 116 LYS A CE  1 
ATOM   898  N  NZ  . LYS A 1 116 ? 30.925 34.927 -6.980  1.00 36.07 ? 116 LYS A NZ  1 
ATOM   899  N  N   . SER A 1 117 ? 25.718 34.054 -13.474 1.00 21.35 ? 117 SER A N   1 
ATOM   900  C  CA  . SER A 1 117 ? 25.353 33.430 -14.768 1.00 22.40 ? 117 SER A CA  1 
ATOM   901  C  C   . SER A 1 117 ? 26.620 33.268 -15.619 1.00 23.10 ? 117 SER A C   1 
ATOM   902  O  O   . SER A 1 117 ? 27.734 33.565 -15.128 1.00 26.12 ? 117 SER A O   1 
ATOM   903  C  CB  . SER A 1 117 ? 24.336 34.238 -15.454 1.00 24.65 ? 117 SER A CB  1 
ATOM   904  O  OG  . SER A 1 117 ? 24.971 35.422 -15.865 1.00 25.67 ? 117 SER A OG  1 
ATOM   905  N  N   . ASN A 1 118 ? 26.449 32.753 -16.834 1.00 23.20 ? 118 ASN A N   1 
ATOM   906  C  CA  . ASN A 1 118 ? 27.523 32.509 -17.832 1.00 25.30 ? 118 ASN A CA  1 
ATOM   907  C  C   . ASN A 1 118 ? 27.696 33.758 -18.694 1.00 28.13 ? 118 ASN A C   1 
ATOM   908  O  O   . ASN A 1 118 ? 28.595 33.765 -19.509 1.00 27.15 ? 118 ASN A O   1 
ATOM   909  C  CB  . ASN A 1 118 ? 27.269 31.263 -18.697 1.00 24.90 ? 118 ASN A CB  1 
ATOM   910  C  CG  . ASN A 1 118 ? 25.981 31.299 -19.496 1.00 30.01 ? 118 ASN A CG  1 
ATOM   911  O  OD1 . ASN A 1 118 ? 24.975 31.842 -19.044 1.00 30.48 ? 118 ASN A OD1 1 
ATOM   912  N  ND2 . ASN A 1 118 ? 25.999 30.690 -20.679 1.00 28.77 ? 118 ASN A ND2 1 
ATOM   913  N  N   . SER A 1 119 ? 26.863 34.785 -18.526 1.00 35.06 ? 119 SER A N   1 
ATOM   914  C  CA  . SER A 1 119 ? 27.151 36.125 -19.105 1.00 41.75 ? 119 SER A CA  1 
ATOM   915  C  C   . SER A 1 119 ? 28.435 36.685 -18.471 1.00 45.01 ? 119 SER A C   1 
ATOM   916  O  O   . SER A 1 119 ? 28.595 36.542 -17.246 1.00 47.45 ? 119 SER A O   1 
ATOM   917  C  CB  . SER A 1 119 ? 25.987 37.043 -18.920 1.00 41.26 ? 119 SER A CB  1 
ATOM   918  O  OG  . SER A 1 119 ? 24.907 36.595 -19.708 1.00 46.03 ? 119 SER A OG  1 
ATOM   919  N  N   . THR A 1 120 ? 29.335 37.273 -19.268 1.00 54.09 ? 120 THR A N   1 
ATOM   920  C  CA  . THR A 1 120 ? 30.565 37.951 -18.763 1.00 56.06 ? 120 THR A CA  1 
ATOM   921  C  C   . THR A 1 120 ? 30.138 39.024 -17.747 1.00 58.82 ? 120 THR A C   1 
ATOM   922  O  O   . THR A 1 120 ? 29.157 39.744 -18.025 1.00 52.95 ? 120 THR A O   1 
ATOM   923  C  CB  . THR A 1 120 ? 31.442 38.469 -19.918 1.00 54.50 ? 120 THR A CB  1 
ATOM   924  O  OG1 . THR A 1 120 ? 31.731 37.327 -20.726 1.00 40.17 ? 120 THR A OG1 1 
ATOM   925  C  CG2 . THR A 1 120 ? 32.740 39.118 -19.468 1.00 51.22 ? 120 THR A CG2 1 
ATOM   926  N  N   . HIS A 1 121 ? 30.803 39.054 -16.584 1.00 67.14 ? 121 HIS A N   1 
ATOM   927  C  CA  . HIS A 1 121 ? 30.531 39.960 -15.429 1.00 73.13 ? 121 HIS A CA  1 
ATOM   928  C  C   . HIS A 1 121 ? 29.021 40.054 -15.140 1.00 67.56 ? 121 HIS A C   1 
ATOM   929  O  O   . HIS A 1 121 ? 28.472 41.170 -15.231 1.00 72.33 ? 121 HIS A O   1 
ATOM   930  C  CB  . HIS A 1 121 ? 31.191 41.324 -15.690 1.00 79.08 ? 121 HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 121 ? 32.668 41.308 -15.473 1.00 87.00 ? 121 HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 121 ? 33.564 40.972 -16.480 1.00 84.27 ? 121 HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 121 ? 33.406 41.566 -14.369 1.00 87.45 ? 121 HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 121 ? 34.790 41.037 -16.004 1.00 83.77 ? 121 HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 121 ? 34.719 41.398 -14.708 1.00 84.37 ? 121 HIS A NE2 1 
ATOM   936  N  N   . GLU A 1 122 ? 28.380 38.930 -14.791 1.00 54.37 ? 122 GLU A N   1 
ATOM   937  C  CA  . GLU A 1 122 ? 26.910 38.847 -14.583 1.00 51.96 ? 122 GLU A CA  1 
ATOM   938  C  C   . GLU A 1 122 ? 26.617 38.117 -13.257 1.00 40.59 ? 122 GLU A C   1 
ATOM   939  O  O   . GLU A 1 122 ? 26.091 36.963 -13.240 1.00 39.98 ? 122 GLU A O   1 
ATOM   940  C  CB  . GLU A 1 122 ? 26.254 38.208 -15.808 1.00 58.33 ? 122 GLU A CB  1 
ATOM   941  C  CG  . GLU A 1 122 ? 24.815 38.646 -16.060 1.00 62.65 ? 122 GLU A CG  1 
ATOM   942  C  CD  . GLU A 1 122 ? 24.607 39.495 -17.311 1.00 69.04 ? 122 GLU A CD  1 
ATOM   943  O  OE1 . GLU A 1 122 ? 25.523 40.285 -17.657 1.00 66.65 ? 122 GLU A OE1 1 
ATOM   944  O  OE2 . GLU A 1 122 ? 23.535 39.354 -17.957 1.00 65.78 ? 122 GLU A OE2 1 
ATOM   945  N  N   . THR A 1 123 ? 26.860 38.801 -12.148 1.00 30.33 ? 123 THR A N   1 
ATOM   946  C  CA  . THR A 1 123 ? 26.343 38.361 -10.829 1.00 27.41 ? 123 THR A CA  1 
ATOM   947  C  C   . THR A 1 123 ? 25.116 39.184 -10.455 1.00 23.34 ? 123 THR A C   1 
ATOM   948  O  O   . THR A 1 123 ? 25.094 40.418 -10.701 1.00 21.54 ? 123 THR A O   1 
ATOM   949  C  CB  . THR A 1 123 ? 27.404 38.397 -9.727  1.00 33.97 ? 123 THR A CB  1 
ATOM   950  O  OG1 . THR A 1 123 ? 27.229 39.634 -9.049  1.00 46.97 ? 123 THR A OG1 1 
ATOM   951  C  CG2 . THR A 1 123 ? 28.814 38.248 -10.239 1.00 34.63 ? 123 THR A CG2 1 
ATOM   952  N  N   . ASN A 1 124 ? 24.116 38.509 -9.912  1.00 16.89 ? 124 ASN A N   1 
ATOM   953  C  CA  . ASN A 1 124 ? 22.989 39.107 -9.185  1.00 15.72 ? 124 ASN A CA  1 
ATOM   954  C  C   . ASN A 1 124 ? 23.310 38.871 -7.706  1.00 14.39 ? 124 ASN A C   1 
ATOM   955  O  O   . ASN A 1 124 ? 23.863 37.798 -7.367  1.00 15.49 ? 124 ASN A O   1 
ATOM   956  C  CB  . ASN A 1 124 ? 21.640 38.518 -9.574  1.00 16.73 ? 124 ASN A CB  1 
ATOM   957  C  CG  . ASN A 1 124 ? 21.094 39.085 -10.871 1.00 20.73 ? 124 ASN A CG  1 
ATOM   958  O  OD1 . ASN A 1 124 ? 19.890 38.958 -11.151 1.00 28.69 ? 124 ASN A OD1 1 
ATOM   959  N  ND2 . ASN A 1 124 ? 21.963 39.668 -11.664 1.00 15.08 ? 124 ASN A ND2 1 
ATOM   960  N  N   . ALA A 1 125 ? 23.085 39.855 -6.861  1.00 13.26 ? 125 ALA A N   1 
ATOM   961  C  CA  . ALA A 1 125 ? 23.405 39.673 -5.426  1.00 12.82 ? 125 ALA A CA  1 
ATOM   962  C  C   . ALA A 1 125 ? 22.400 40.418 -4.557  1.00 12.23 ? 125 ALA A C   1 
ATOM   963  O  O   . ALA A 1 125 ? 21.859 41.491 -4.967  1.00 11.71 ? 125 ALA A O   1 
ATOM   964  C  CB  . ALA A 1 125 ? 24.792 40.159 -5.086  1.00 13.52 ? 125 ALA A CB  1 
ATOM   965  N  N   . LEU A 1 126 ? 22.216 39.909 -3.336  1.00 11.65 ? 126 LEU A N   1 
ATOM   966  C  CA  . LEU A 1 126 ? 21.463 40.552 -2.251  1.00 12.04 ? 126 LEU A CA  1 
ATOM   967  C  C   . LEU A 1 126 ? 22.321 40.394 -0.993  1.00 12.47 ? 126 LEU A C   1 
ATOM   968  O  O   . LEU A 1 126 ? 22.768 39.271 -0.677  1.00 12.29 ? 126 LEU A O   1 
ATOM   969  C  CB  . LEU A 1 126 ? 20.080 39.951 -2.020  1.00 13.64 ? 126 LEU A CB  1 
ATOM   970  C  CG  . LEU A 1 126 ? 19.367 40.508 -0.793  1.00 16.27 ? 126 LEU A CG  1 
ATOM   971  C  CD1 . LEU A 1 126 ? 18.926 41.949 -1.024  1.00 16.37 ? 126 LEU A CD1 1 
ATOM   972  C  CD2 . LEU A 1 126 ? 18.196 39.652 -0.401  1.00 17.95 ? 126 LEU A CD2 1 
ATOM   973  N  N   . HIS A 1 127 ? 22.505 41.477 -0.272  1.00 12.18 ? 127 HIS A N   1 
ATOM   974  C  CA  . HIS A 1 127 ? 23.140 41.429 1.059   1.00 12.01 ? 127 HIS A CA  1 
ATOM   975  C  C   . HIS A 1 127 ? 22.374 42.333 2.015   1.00 12.25 ? 127 HIS A C   1 
ATOM   976  O  O   . HIS A 1 127 ? 21.962 43.462 1.620   1.00 11.59 ? 127 HIS A O   1 
ATOM   977  C  CB  . HIS A 1 127 ? 24.614 41.833 0.939   1.00 13.38 ? 127 HIS A CB  1 
ATOM   978  C  CG  . HIS A 1 127 ? 25.235 42.099 2.270   1.00 14.72 ? 127 HIS A CG  1 
ATOM   979  N  ND1 . HIS A 1 127 ? 25.498 41.097 3.191   1.00 14.43 ? 127 HIS A ND1 1 
ATOM   980  C  CD2 . HIS A 1 127 ? 25.553 43.273 2.867   1.00 15.63 ? 127 HIS A CD2 1 
ATOM   981  C  CE1 . HIS A 1 127 ? 26.011 41.666 4.295   1.00 15.68 ? 127 HIS A CE1 1 
ATOM   982  N  NE2 . HIS A 1 127 ? 26.037 43.009 4.109   1.00 17.35 ? 127 HIS A NE2 1 
ATOM   983  N  N   . PHE A 1 128 ? 22.108 41.876 3.217   1.00 10.05 ? 128 PHE A N   1 
ATOM   984  C  CA  . PHE A 1 128 ? 21.600 42.764 4.268   1.00 10.39 ? 128 PHE A CA  1 
ATOM   985  C  C   . PHE A 1 128 ? 22.374 42.465 5.526   1.00 11.54 ? 128 PHE A C   1 
ATOM   986  O  O   . PHE A 1 128 ? 22.854 41.332 5.725   1.00 10.89 ? 128 PHE A O   1 
ATOM   987  C  CB  . PHE A 1 128 ? 20.075 42.643 4.444   1.00 12.03 ? 128 PHE A CB  1 
ATOM   988  C  CG  . PHE A 1 128 ? 19.560 41.270 4.846   1.00 11.94 ? 128 PHE A CG  1 
ATOM   989  C  CD1 . PHE A 1 128 ? 19.601 40.860 6.175   1.00 12.80 ? 128 PHE A CD1 1 
ATOM   990  C  CD2 . PHE A 1 128 ? 18.969 40.425 3.925   1.00 13.02 ? 128 PHE A CD2 1 
ATOM   991  C  CE1 . PHE A 1 128 ? 19.074 39.644 6.566   1.00 14.27 ? 128 PHE A CE1 1 
ATOM   992  C  CE2 . PHE A 1 128 ? 18.450 39.201 4.334   1.00 12.87 ? 128 PHE A CE2 1 
ATOM   993  C  CZ  . PHE A 1 128 ? 18.474 38.829 5.648   1.00 12.41 ? 128 PHE A CZ  1 
ATOM   994  N  N   . MET A 1 129 ? 22.432 43.460 6.386   1.00 11.65 ? 129 MET A N   1 
ATOM   995  C  CA  . MET A 1 129 ? 23.065 43.295 7.717   1.00 12.72 ? 129 MET A CA  1 
ATOM   996  C  C   . MET A 1 129 ? 22.292 44.151 8.716   1.00 12.29 ? 129 MET A C   1 
ATOM   997  O  O   . MET A 1 129 ? 22.080 45.376 8.474   1.00 11.59 ? 129 MET A O   1 
ATOM   998  C  CB  . MET A 1 129 ? 24.526 43.734 7.652   1.00 16.73 ? 129 MET A CB  1 
ATOM   999  C  CG  . MET A 1 129 ? 25.153 43.849 9.016   1.00 17.65 ? 129 MET A CG  1 
ATOM   1000 S  SD  . MET A 1 129 ? 26.917 44.222 8.845   1.00 27.32 ? 129 MET A SD  1 
ATOM   1001 C  CE  . MET A 1 129 ? 27.523 42.569 8.550   1.00 29.57 ? 129 MET A CE  1 
ATOM   1002 N  N   . PHE A 1 130 ? 21.808 43.527 9.781   1.00 12.10 ? 130 PHE A N   1 
ATOM   1003 C  CA  . PHE A 1 130 ? 21.173 44.231 10.911  1.00 13.33 ? 130 PHE A CA  1 
ATOM   1004 C  C   . PHE A 1 130 ? 22.085 44.047 12.109  1.00 13.71 ? 130 PHE A C   1 
ATOM   1005 O  O   . PHE A 1 130 ? 22.307 42.900 12.515  1.00 13.60 ? 130 PHE A O   1 
ATOM   1006 C  CB  . PHE A 1 130 ? 19.801 43.630 11.228  1.00 14.61 ? 130 PHE A CB  1 
ATOM   1007 C  CG  . PHE A 1 130 ? 18.819 43.667 10.100  1.00 16.59 ? 130 PHE A CG  1 
ATOM   1008 C  CD1 . PHE A 1 130 ? 18.207 44.845 9.721   1.00 20.90 ? 130 PHE A CD1 1 
ATOM   1009 C  CD2 . PHE A 1 130 ? 18.505 42.526 9.410   1.00 16.98 ? 130 PHE A CD2 1 
ATOM   1010 C  CE1 . PHE A 1 130 ? 17.313 44.867 8.667   1.00 22.13 ? 130 PHE A CE1 1 
ATOM   1011 C  CE2 . PHE A 1 130 ? 17.566 42.528 8.398   1.00 17.28 ? 130 PHE A CE2 1 
ATOM   1012 C  CZ  . PHE A 1 130 ? 16.999 43.708 7.992   1.00 19.54 ? 130 PHE A CZ  1 
ATOM   1013 N  N   . ASN A 1 131 ? 22.603 45.137 12.642  1.00 16.13 ? 131 ASN A N   1 
ATOM   1014 C  CA  . ASN A 1 131 ? 23.305 45.111 13.948  1.00 18.25 ? 131 ASN A CA  1 
ATOM   1015 C  C   . ASN A 1 131 ? 22.440 45.777 14.982  1.00 19.39 ? 131 ASN A C   1 
ATOM   1016 O  O   . ASN A 1 131 ? 22.732 45.605 16.186  1.00 19.34 ? 131 ASN A O   1 
ATOM   1017 C  CB  . ASN A 1 131 ? 24.702 45.707 13.863  1.00 20.76 ? 131 ASN A CB  1 
ATOM   1018 C  CG  . ASN A 1 131 ? 25.678 44.690 13.355  1.00 24.22 ? 131 ASN A CG  1 
ATOM   1019 O  OD1 . ASN A 1 131 ? 25.851 43.656 13.993  1.00 29.99 ? 131 ASN A OD1 1 
ATOM   1020 N  ND2 . ASN A 1 131 ? 26.312 44.972 12.248  1.00 26.19 ? 131 ASN A ND2 1 
ATOM   1021 N  N   . GLN A 1 132 ? 21.446 46.555 14.570  1.00 19.91 ? 132 GLN A N   1 
ATOM   1022 C  CA  . GLN A 1 132 ? 20.476 47.121 15.513  1.00 25.91 ? 132 GLN A CA  1 
ATOM   1023 C  C   . GLN A 1 132 ? 19.126 47.066 14.829  1.00 23.53 ? 132 GLN A C   1 
ATOM   1024 O  O   . GLN A 1 132 ? 18.992 47.437 13.640  1.00 24.69 ? 132 GLN A O   1 
ATOM   1025 C  CB  . GLN A 1 132 ? 20.936 48.472 16.069  1.00 32.22 ? 132 GLN A CB  1 
ATOM   1026 C  CG  . GLN A 1 132 ? 20.693 49.679 15.199  1.00 37.34 ? 132 GLN A CG  1 
ATOM   1027 C  CD  . GLN A 1 132 ? 21.074 50.948 15.938  1.00 45.41 ? 132 GLN A CD  1 
ATOM   1028 O  OE1 . GLN A 1 132 ? 20.577 52.025 15.632  1.00 51.92 ? 132 GLN A OE1 1 
ATOM   1029 N  NE2 . GLN A 1 132 ? 21.943 50.834 16.939  1.00 49.63 ? 132 GLN A NE2 1 
ATOM   1030 N  N   . PHE A 1 133 ? 18.164 46.581 15.579  1.00 17.38 ? 133 PHE A N   1 
ATOM   1031 C  CA  . PHE A 1 133 ? 16.760 46.453 15.139  1.00 16.73 ? 133 PHE A CA  1 
ATOM   1032 C  C   . PHE A 1 133 ? 16.001 47.662 15.707  1.00 20.12 ? 133 PHE A C   1 
ATOM   1033 O  O   . PHE A 1 133 ? 16.199 48.022 16.870  1.00 23.12 ? 133 PHE A O   1 
ATOM   1034 C  CB  . PHE A 1 133 ? 16.196 45.107 15.592  1.00 14.00 ? 133 PHE A CB  1 
ATOM   1035 C  CG  . PHE A 1 133 ? 16.890 43.910 14.986  1.00 13.11 ? 133 PHE A CG  1 
ATOM   1036 C  CD1 . PHE A 1 133 ? 16.498 43.394 13.765  1.00 12.65 ? 133 PHE A CD1 1 
ATOM   1037 C  CD2 . PHE A 1 133 ? 17.982 43.325 15.613  1.00 13.80 ? 133 PHE A CD2 1 
ATOM   1038 C  CE1 . PHE A 1 133 ? 17.131 42.293 13.201  1.00 14.63 ? 133 PHE A CE1 1 
ATOM   1039 C  CE2 . PHE A 1 133 ? 18.605 42.222 15.065  1.00 14.01 ? 133 PHE A CE2 1 
ATOM   1040 C  CZ  . PHE A 1 133 ? 18.186 41.725 13.851  1.00 13.17 ? 133 PHE A CZ  1 
ATOM   1041 N  N   . SER A 1 134 ? 15.126 48.251 14.913  1.00 21.13 ? 134 SER A N   1 
ATOM   1042 C  CA  . SER A 1 134 ? 14.367 49.452 15.333  1.00 23.28 ? 134 SER A CA  1 
ATOM   1043 C  C   . SER A 1 134 ? 12.934 49.043 15.611  1.00 23.10 ? 134 SER A C   1 
ATOM   1044 O  O   . SER A 1 134 ? 12.491 48.004 15.095  1.00 20.19 ? 134 SER A O   1 
ATOM   1045 C  CB  . SER A 1 134 ? 14.449 50.548 14.310  1.00 26.24 ? 134 SER A CB  1 
ATOM   1046 O  OG  . SER A 1 134 ? 14.083 50.060 13.036  1.00 32.32 ? 134 SER A OG  1 
ATOM   1047 N  N   . LYS A 1 135 ? 12.235 49.865 16.393  1.00 26.51 ? 135 LYS A N   1 
ATOM   1048 C  CA  . LYS A 1 135 ? 10.851 49.608 16.828  1.00 32.42 ? 135 LYS A CA  1 
ATOM   1049 C  C   . LYS A 1 135 ? 9.964  49.366 15.609  1.00 32.44 ? 135 LYS A C   1 
ATOM   1050 O  O   . LYS A 1 135 ? 9.028  48.570 15.741  1.00 39.03 ? 135 LYS A O   1 
ATOM   1051 C  CB  . LYS A 1 135 ? 10.307 50.752 17.691  1.00 37.96 ? 135 LYS A CB  1 
ATOM   1052 C  CG  . LYS A 1 135 ? 9.013  50.411 18.420  1.00 47.90 ? 135 LYS A CG  1 
ATOM   1053 C  CD  . LYS A 1 135 ? 8.198  51.614 18.909  1.00 52.69 ? 135 LYS A CD  1 
ATOM   1054 C  CE  . LYS A 1 135 ? 8.889  52.377 20.020  1.00 60.48 ? 135 LYS A CE  1 
ATOM   1055 N  NZ  . LYS A 1 135 ? 7.952  53.272 20.744  1.00 63.00 ? 135 LYS A NZ  1 
ATOM   1056 N  N   . ASP A 1 136 ? 10.196 50.048 14.487  1.00 28.83 ? 136 ASP A N   1 
ATOM   1057 C  CA  . ASP A 1 136 ? 9.337  49.860 13.293  1.00 30.95 ? 136 ASP A CA  1 
ATOM   1058 C  C   . ASP A 1 136 ? 10.247 49.537 12.100  1.00 27.19 ? 136 ASP A C   1 
ATOM   1059 O  O   . ASP A 1 136 ? 10.539 50.421 11.279  1.00 29.50 ? 136 ASP A O   1 
ATOM   1060 C  CB  . ASP A 1 136 ? 8.449  51.077 13.050  1.00 33.78 ? 136 ASP A CB  1 
ATOM   1061 C  CG  . ASP A 1 136 ? 7.668  51.013 11.747  1.00 39.69 ? 136 ASP A CG  1 
ATOM   1062 O  OD1 . ASP A 1 136 ? 7.202  49.924 11.400  1.00 43.53 ? 136 ASP A OD1 1 
ATOM   1063 O  OD2 . ASP A 1 136 ? 7.545  52.059 11.078  1.00 42.56 ? 136 ASP A OD2 1 
ATOM   1064 N  N   . GLN A 1 137 ? 10.672 48.285 12.011  1.00 21.73 ? 137 GLN A N   1 
ATOM   1065 C  CA  . GLN A 1 137 ? 11.687 47.830 11.036  1.00 21.21 ? 137 GLN A CA  1 
ATOM   1066 C  C   . GLN A 1 137 ? 10.952 47.392 9.762   1.00 20.14 ? 137 GLN A C   1 
ATOM   1067 O  O   . GLN A 1 137 ? 10.593 46.210 9.634   1.00 19.82 ? 137 GLN A O   1 
ATOM   1068 C  CB  . GLN A 1 137 ? 12.453 46.681 11.684  1.00 23.51 ? 137 GLN A CB  1 
ATOM   1069 C  CG  . GLN A 1 137 ? 13.641 46.223 10.879  1.00 26.35 ? 137 GLN A CG  1 
ATOM   1070 C  CD  . GLN A 1 137 ? 14.836 47.034 11.234  1.00 30.97 ? 137 GLN A CD  1 
ATOM   1071 O  OE1 . GLN A 1 137 ? 15.111 47.197 12.413  1.00 34.14 ? 137 GLN A OE1 1 
ATOM   1072 N  NE2 . GLN A 1 137 ? 15.499 47.583 10.225  1.00 28.95 ? 137 GLN A NE2 1 
ATOM   1073 N  N   . LYS A 1 138 ? 10.790 48.294 8.800   1.00 17.10 ? 138 LYS A N   1 
ATOM   1074 C  CA  . LYS A 1 138 ? 9.951  48.056 7.612   1.00 17.45 ? 138 LYS A CA  1 
ATOM   1075 C  C   . LYS A 1 138 ? 10.550 47.026 6.641   1.00 16.62 ? 138 LYS A C   1 
ATOM   1076 O  O   . LYS A 1 138 ? 9.850  46.601 5.696   1.00 20.13 ? 138 LYS A O   1 
ATOM   1077 C  CB  . LYS A 1 138 ? 9.737  49.410 6.958   1.00 18.99 ? 138 LYS A CB  1 
ATOM   1078 C  CG  . LYS A 1 138 ? 9.017  50.416 7.847   1.00 20.68 ? 138 LYS A CG  1 
ATOM   1079 C  CD  . LYS A 1 138 ? 8.503  51.522 6.972   1.00 24.21 ? 138 LYS A CD  1 
ATOM   1080 C  CE  . LYS A 1 138 ? 7.932  52.700 7.716   1.00 26.46 ? 138 LYS A CE  1 
ATOM   1081 N  NZ  . LYS A 1 138 ? 6.616  52.282 8.236   1.00 27.93 ? 138 LYS A NZ  1 
ATOM   1082 N  N   . ASP A 1 139 ? 11.838 46.723 6.732   1.00 15.00 ? 139 ASP A N   1 
ATOM   1083 C  CA  . ASP A 1 139 ? 12.421 45.703 5.833   1.00 13.99 ? 139 ASP A CA  1 
ATOM   1084 C  C   . ASP A 1 139 ? 12.349 44.312 6.495   1.00 13.81 ? 139 ASP A C   1 
ATOM   1085 O  O   . ASP A 1 139 ? 12.950 43.392 5.961   1.00 13.18 ? 139 ASP A O   1 
ATOM   1086 C  CB  . ASP A 1 139 ? 13.831 46.119 5.426   1.00 14.43 ? 139 ASP A CB  1 
ATOM   1087 C  CG  . ASP A 1 139 ? 14.763 46.490 6.558   1.00 15.67 ? 139 ASP A CG  1 
ATOM   1088 O  OD1 . ASP A 1 139 ? 14.378 46.330 7.774   1.00 17.18 ? 139 ASP A OD1 1 
ATOM   1089 O  OD2 . ASP A 1 139 ? 15.927 46.878 6.251   1.00 17.79 ? 139 ASP A OD2 1 
ATOM   1090 N  N   . LEU A 1 140 ? 11.616 44.135 7.598   1.00 13.75 ? 140 LEU A N   1 
ATOM   1091 C  CA  . LEU A 1 140 ? 11.359 42.801 8.198   1.00 15.00 ? 140 LEU A CA  1 
ATOM   1092 C  C   . LEU A 1 140 ? 9.861  42.545 8.222   1.00 15.79 ? 140 LEU A C   1 
ATOM   1093 O  O   . LEU A 1 140 ? 9.105  43.501 8.566   1.00 17.06 ? 140 LEU A O   1 
ATOM   1094 C  CB  . LEU A 1 140 ? 11.882 42.733 9.627   1.00 15.38 ? 140 LEU A CB  1 
ATOM   1095 C  CG  . LEU A 1 140 ? 13.397 42.661 9.797   1.00 18.18 ? 140 LEU A CG  1 
ATOM   1096 C  CD1 . LEU A 1 140 ? 13.772 42.590 11.282  1.00 19.27 ? 140 LEU A CD1 1 
ATOM   1097 C  CD2 . LEU A 1 140 ? 13.994 41.499 9.026   1.00 18.39 ? 140 LEU A CD2 1 
ATOM   1098 N  N   . ILE A 1 141 ? 9.472  41.306 7.997   1.00 13.56 ? 141 ILE A N   1 
ATOM   1099 C  CA  . ILE A 1 141 ? 8.095  40.807 8.212   1.00 13.75 ? 141 ILE A CA  1 
ATOM   1100 C  C   . ILE A 1 141 ? 8.122  40.059 9.555   1.00 14.45 ? 141 ILE A C   1 
ATOM   1101 O  O   . ILE A 1 141 ? 8.872  39.068 9.674   1.00 13.60 ? 141 ILE A O   1 
ATOM   1102 C  CB  . ILE A 1 141 ? 7.667  39.886 7.083   1.00 14.68 ? 141 ILE A CB  1 
ATOM   1103 C  CG1 . ILE A 1 141 ? 7.687  40.572 5.718   1.00 15.89 ? 141 ILE A CG1 1 
ATOM   1104 C  CG2 . ILE A 1 141 ? 6.282  39.289 7.411   1.00 16.15 ? 141 ILE A CG2 1 
ATOM   1105 C  CD1 . ILE A 1 141 ? 7.583  39.611 4.561   1.00 18.02 ? 141 ILE A CD1 1 
ATOM   1106 N  N   . LEU A 1 142 ? 7.459  40.590 10.563  1.00 13.14 ? 142 LEU A N   1 
ATOM   1107 C  CA  . LEU A 1 142 ? 7.391  39.931 11.888  1.00 12.66 ? 142 LEU A CA  1 
ATOM   1108 C  C   . LEU A 1 142 ? 6.123  39.104 11.939  1.00 14.81 ? 142 LEU A C   1 
ATOM   1109 O  O   . LEU A 1 142 ? 5.056  39.633 11.581  1.00 15.20 ? 142 LEU A O   1 
ATOM   1110 C  CB  . LEU A 1 142 ? 7.415  40.968 13.007  1.00 13.49 ? 142 LEU A CB  1 
ATOM   1111 C  CG  . LEU A 1 142 ? 8.613  41.913 13.042  1.00 14.60 ? 142 LEU A CG  1 
ATOM   1112 C  CD1 . LEU A 1 142 ? 8.553  42.778 14.295  1.00 15.37 ? 142 LEU A CD1 1 
ATOM   1113 C  CD2 . LEU A 1 142 ? 9.919  41.158 13.010  1.00 16.03 ? 142 LEU A CD2 1 
ATOM   1114 N  N   . GLN A 1 143 ? 6.247  37.881 12.445  1.00 13.20 ? 143 GLN A N   1 
ATOM   1115 C  CA  . GLN A 1 143 ? 5.107  36.934 12.560  1.00 13.16 ? 143 GLN A CA  1 
ATOM   1116 C  C   . GLN A 1 143 ? 4.989  36.464 13.993  1.00 12.50 ? 143 GLN A C   1 
ATOM   1117 O  O   . GLN A 1 143 ? 6.019  36.333 14.702  1.00 12.66 ? 143 GLN A O   1 
ATOM   1118 C  CB  . GLN A 1 143 ? 5.263  35.754 11.600  1.00 13.29 ? 143 GLN A CB  1 
ATOM   1119 C  CG  . GLN A 1 143 ? 5.325  36.221 10.151  1.00 14.40 ? 143 GLN A CG  1 
ATOM   1120 C  CD  . GLN A 1 143 ? 5.479  35.090 9.175   1.00 14.55 ? 143 GLN A CD  1 
ATOM   1121 O  OE1 . GLN A 1 143 ? 6.081  34.030 9.459   1.00 14.03 ? 143 GLN A OE1 1 
ATOM   1122 N  NE2 . GLN A 1 143 ? 4.990  35.331 7.962   1.00 15.71 ? 143 GLN A NE2 1 
ATOM   1123 N  N   . GLY A 1 144 ? 3.748  36.211 14.422  1.00 13.49 ? 144 GLY A N   1 
ATOM   1124 C  CA  . GLY A 1 144 ? 3.498  35.718 15.788  1.00 13.17 ? 144 GLY A CA  1 
ATOM   1125 C  C   . GLY A 1 144 ? 3.953  36.697 16.845  1.00 13.97 ? 144 GLY A C   1 
ATOM   1126 O  O   . GLY A 1 144 ? 3.576  37.876 16.782  1.00 14.67 ? 144 GLY A O   1 
ATOM   1127 N  N   . ASP A 1 145 ? 4.746  36.257 17.813  1.00 13.97 ? 145 ASP A N   1 
ATOM   1128 C  CA  . ASP A 1 145 ? 5.111  37.041 19.002  1.00 14.00 ? 145 ASP A CA  1 
ATOM   1129 C  C   . ASP A 1 145 ? 6.390  37.883 18.775  1.00 14.13 ? 145 ASP A C   1 
ATOM   1130 O  O   . ASP A 1 145 ? 6.755  38.619 19.688  1.00 14.85 ? 145 ASP A O   1 
ATOM   1131 C  CB  . ASP A 1 145 ? 5.299  36.112 20.213  1.00 14.83 ? 145 ASP A CB  1 
ATOM   1132 C  CG  . ASP A 1 145 ? 4.017  35.398 20.643  1.00 18.00 ? 145 ASP A CG  1 
ATOM   1133 O  OD1 . ASP A 1 145 ? 2.946  35.933 20.316  1.00 19.46 ? 145 ASP A OD1 1 
ATOM   1134 O  OD2 . ASP A 1 145 ? 4.097  34.329 21.334  1.00 19.87 ? 145 ASP A OD2 1 
ATOM   1135 N  N   . ALA A 1 146 ? 7.001  37.853 17.585  1.00 12.99 ? 146 ALA A N   1 
ATOM   1136 C  CA  . ALA A 1 146 ? 8.295  38.517 17.343  1.00 13.55 ? 146 ALA A CA  1 
ATOM   1137 C  C   . ALA A 1 146 ? 8.115  40.029 17.477  1.00 14.30 ? 146 ALA A C   1 
ATOM   1138 O  O   . ALA A 1 146 ? 7.113  40.591 16.924  1.00 14.27 ? 146 ALA A O   1 
ATOM   1139 C  CB  . ALA A 1 146 ? 8.849  38.106 15.986  1.00 14.92 ? 146 ALA A CB  1 
ATOM   1140 N  N   . THR A 1 147 ? 9.044  40.692 18.151  1.00 13.87 ? 147 THR A N   1 
ATOM   1141 C  CA  . THR A 1 147 ? 9.064  42.182 18.250  1.00 15.19 ? 147 THR A CA  1 
ATOM   1142 C  C   . THR A 1 147 ? 10.470 42.716 18.053  1.00 16.80 ? 147 THR A C   1 
ATOM   1143 O  O   . THR A 1 147 ? 11.433 41.949 18.259  1.00 16.75 ? 147 THR A O   1 
ATOM   1144 C  CB  . THR A 1 147 ? 8.535  42.663 19.608  1.00 18.07 ? 147 THR A CB  1 
ATOM   1145 O  OG1 . THR A 1 147 ? 9.382  42.073 20.594  1.00 20.69 ? 147 THR A OG1 1 
ATOM   1146 C  CG2 . THR A 1 147 ? 7.104  42.263 19.854  1.00 19.20 ? 147 THR A CG2 1 
ATOM   1147 N  N   . THR A 1 148 ? 10.600 43.980 17.632  1.00 17.41 ? 148 THR A N   1 
ATOM   1148 C  CA  . THR A 1 148 ? 11.905 44.641 17.466  1.00 19.56 ? 148 THR A CA  1 
ATOM   1149 C  C   . THR A 1 148 ? 11.940 45.927 18.295  1.00 22.62 ? 148 THR A C   1 
ATOM   1150 O  O   . THR A 1 148 ? 10.858 46.495 18.534  1.00 23.98 ? 148 THR A O   1 
ATOM   1151 C  CB  . THR A 1 148 ? 12.209 45.008 16.009  1.00 20.79 ? 148 THR A CB  1 
ATOM   1152 O  OG1 . THR A 1 148 ? 11.106 45.779 15.509  1.00 23.26 ? 148 THR A OG1 1 
ATOM   1153 C  CG2 . THR A 1 148 ? 12.452 43.808 15.119  1.00 21.90 ? 148 THR A CG2 1 
ATOM   1154 N  N   . GLY A 1 149 ? 13.164 46.355 18.630  1.00 24.95 ? 149 GLY A N   1 
ATOM   1155 C  CA  . GLY A 1 149 ? 13.517 47.697 19.133  1.00 28.10 ? 149 GLY A CA  1 
ATOM   1156 C  C   . GLY A 1 149 ? 13.773 47.716 20.631  1.00 34.88 ? 149 GLY A C   1 
ATOM   1157 O  O   . GLY A 1 149 ? 14.255 48.767 21.116  1.00 40.18 ? 149 GLY A O   1 
ATOM   1158 N  N   . THR A 1 150 ? 13.430 46.643 21.369  1.00 34.55 ? 150 THR A N   1 
ATOM   1159 C  CA  . THR A 1 150 ? 13.763 46.532 22.812  1.00 32.47 ? 150 THR A CA  1 
ATOM   1160 C  C   . THR A 1 150 ? 15.282 46.329 22.906  1.00 30.59 ? 150 THR A C   1 
ATOM   1161 O  O   . THR A 1 150 ? 15.735 45.328 22.407  1.00 23.07 ? 150 THR A O   1 
ATOM   1162 C  CB  . THR A 1 150 ? 13.020 45.407 23.548  1.00 37.06 ? 150 THR A CB  1 
ATOM   1163 O  OG1 . THR A 1 150 ? 11.634 45.432 23.214  1.00 41.44 ? 150 THR A OG1 1 
ATOM   1164 C  CG2 . THR A 1 150 ? 13.171 45.535 25.049  1.00 40.68 ? 150 THR A CG2 1 
ATOM   1165 N  N   . ASP A 1 151 ? 16.013 47.323 23.435  1.00 26.61 ? 151 ASP A N   1 
ATOM   1166 C  CA  . ASP A 1 151 ? 17.493 47.406 23.465  1.00 29.59 ? 151 ASP A CA  1 
ATOM   1167 C  C   . ASP A 1 151 ? 18.122 47.227 22.067  1.00 24.82 ? 151 ASP A C   1 
ATOM   1168 O  O   . ASP A 1 151 ? 19.192 46.655 22.038  1.00 27.77 ? 151 ASP A O   1 
ATOM   1169 C  CB  . ASP A 1 151 ? 18.072 46.319 24.380  1.00 38.05 ? 151 ASP A CB  1 
ATOM   1170 C  CG  . ASP A 1 151 ? 17.564 46.351 25.811  1.00 43.59 ? 151 ASP A CG  1 
ATOM   1171 O  OD1 . ASP A 1 151 ? 17.383 47.458 26.343  1.00 51.21 ? 151 ASP A OD1 1 
ATOM   1172 O  OD2 . ASP A 1 151 ? 17.379 45.267 26.388  1.00 51.53 ? 151 ASP A OD2 1 
ATOM   1173 N  N   . GLY A 1 152 ? 17.448 47.583 20.961  1.00 22.72 ? 152 GLY A N   1 
ATOM   1174 C  CA  . GLY A 1 152 ? 17.962 47.376 19.593  1.00 19.06 ? 152 GLY A CA  1 
ATOM   1175 C  C   . GLY A 1 152 ? 18.020 45.907 19.171  1.00 17.29 ? 152 GLY A C   1 
ATOM   1176 O  O   . GLY A 1 152 ? 18.736 45.572 18.225  1.00 18.02 ? 152 GLY A O   1 
ATOM   1177 N  N   . ASN A 1 153 ? 17.273 45.041 19.847  1.00 16.03 ? 153 ASN A N   1 
ATOM   1178 C  CA  . ASN A 1 153 ? 17.304 43.590 19.525  1.00 14.78 ? 153 ASN A CA  1 
ATOM   1179 C  C   . ASN A 1 153 ? 15.974 43.126 18.933  1.00 12.74 ? 153 ASN A C   1 
ATOM   1180 O  O   . ASN A 1 153 ? 14.938 43.796 18.997  1.00 15.91 ? 153 ASN A O   1 
ATOM   1181 C  CB  . ASN A 1 153 ? 17.606 42.773 20.785  1.00 15.42 ? 153 ASN A CB  1 
ATOM   1182 C  CG  . ASN A 1 153 ? 18.960 43.066 21.379  1.00 16.04 ? 153 ASN A CG  1 
ATOM   1183 O  OD1 . ASN A 1 153 ? 19.907 43.378 20.671  1.00 17.36 ? 153 ASN A OD1 1 
ATOM   1184 N  ND2 . ASN A 1 153 ? 19.089 42.939 22.692  1.00 16.72 ? 153 ASN A ND2 1 
ATOM   1185 N  N   . LEU A 1 154 ? 16.017 41.975 18.301  1.00 12.29 ? 154 LEU A N   1 
ATOM   1186 C  CA  . LEU A 1 154 ? 14.851 41.240 17.797  1.00 11.98 ? 154 LEU A CA  1 
ATOM   1187 C  C   . LEU A 1 154 ? 14.540 40.165 18.836  1.00 13.15 ? 154 LEU A C   1 
ATOM   1188 O  O   . LEU A 1 154 ? 15.380 39.319 19.090  1.00 15.25 ? 154 LEU A O   1 
ATOM   1189 C  CB  . LEU A 1 154 ? 15.210 40.685 16.430  1.00 12.38 ? 154 LEU A CB  1 
ATOM   1190 C  CG  . LEU A 1 154 ? 14.363 39.568 15.844  1.00 13.17 ? 154 LEU A CG  1 
ATOM   1191 C  CD1 . LEU A 1 154 ? 12.916 40.010 15.661  1.00 15.08 ? 154 LEU A CD1 1 
ATOM   1192 C  CD2 . LEU A 1 154 ? 14.971 39.098 14.545  1.00 14.69 ? 154 LEU A CD2 1 
ATOM   1193 N  N   . GLU A 1 155 ? 13.399 40.261 19.465  1.00 11.35 ? 155 GLU A N   1 
ATOM   1194 C  CA  . GLU A 1 155 ? 12.923 39.261 20.443  1.00 13.77 ? 155 GLU A CA  1 
ATOM   1195 C  C   . GLU A 1 155 ? 11.969 38.334 19.702  1.00 12.92 ? 155 GLU A C   1 
ATOM   1196 O  O   . GLU A 1 155 ? 10.812 38.715 19.469  1.00 14.77 ? 155 GLU A O   1 
ATOM   1197 C  CB  . GLU A 1 155 ? 12.258 39.954 21.627  1.00 15.23 ? 155 GLU A CB  1 
ATOM   1198 C  CG  . GLU A 1 155 ? 13.225 40.714 22.482  1.00 16.40 ? 155 GLU A CG  1 
ATOM   1199 C  CD  . GLU A 1 155 ? 14.153 39.915 23.372  1.00 18.61 ? 155 GLU A CD  1 
ATOM   1200 O  OE1 . GLU A 1 155 ? 14.337 38.672 23.147  1.00 17.55 ? 155 GLU A OE1 1 
ATOM   1201 O  OE2 . GLU A 1 155 ? 14.733 40.541 24.302  1.00 21.62 ? 155 GLU A OE2 1 
ATOM   1202 N  N   . LEU A 1 156 ? 12.408 37.140 19.337  1.00 11.99 ? 156 LEU A N   1 
ATOM   1203 C  CA  . LEU A 1 156 ? 11.562 36.247 18.514  1.00 12.11 ? 156 LEU A CA  1 
ATOM   1204 C  C   . LEU A 1 156 ? 10.377 35.723 19.322  1.00 13.53 ? 156 LEU A C   1 
ATOM   1205 O  O   . LEU A 1 156 ? 9.298  35.547 18.726  1.00 13.89 ? 156 LEU A O   1 
ATOM   1206 C  CB  . LEU A 1 156 ? 12.418 35.120 17.960  1.00 13.04 ? 156 LEU A CB  1 
ATOM   1207 C  CG  . LEU A 1 156 ? 13.371 35.540 16.844  1.00 12.84 ? 156 LEU A CG  1 
ATOM   1208 C  CD1 . LEU A 1 156 ? 14.332 34.405 16.555  1.00 12.95 ? 156 LEU A CD1 1 
ATOM   1209 C  CD2 . LEU A 1 156 ? 12.595 35.894 15.586  1.00 13.42 ? 156 LEU A CD2 1 
ATOM   1210 N  N   . THR A 1 157 ? 10.567 35.483 20.616  1.00 12.72 ? 157 THR A N   1 
ATOM   1211 C  CA  . THR A 1 157 ? 9.455  35.021 21.484  1.00 13.00 ? 157 THR A CA  1 
ATOM   1212 C  C   . THR A 1 157 ? 9.208  36.034 22.607  1.00 14.26 ? 157 THR A C   1 
ATOM   1213 O  O   . THR A 1 157 ? 10.044 36.895 22.880  1.00 14.84 ? 157 THR A O   1 
ATOM   1214 C  CB  . THR A 1 157 ? 9.683  33.581 21.963  1.00 13.82 ? 157 THR A CB  1 
ATOM   1215 O  OG1 . THR A 1 157 ? 10.991 33.566 22.542  1.00 13.16 ? 157 THR A OG1 1 
ATOM   1216 C  CG2 . THR A 1 157 ? 9.537  32.562 20.854  1.00 14.45 ? 157 THR A CG2 1 
ATOM   1217 N  N   . ARG A 1 158 ? 8.063  35.869 23.269  1.00 15.44 ? 158 ARG A N   1 
ATOM   1218 C  CA  . ARG A 1 158 ? 7.579  36.832 24.275  1.00 18.03 ? 158 ARG A CA  1 
ATOM   1219 C  C   . ARG A 1 158 ? 8.472  36.867 25.516  1.00 16.70 ? 158 ARG A C   1 
ATOM   1220 O  O   . ARG A 1 158 ? 8.857  35.814 26.098  1.00 15.57 ? 158 ARG A O   1 
ATOM   1221 C  CB  . ARG A 1 158 ? 6.129  36.523 24.650  1.00 23.18 ? 158 ARG A CB  1 
ATOM   1222 C  CG  . ARG A 1 158 ? 5.496  37.612 25.507  1.00 33.68 ? 158 ARG A CG  1 
ATOM   1223 C  CD  . ARG A 1 158 ? 3.981  37.562 25.412  1.00 43.10 ? 158 ARG A CD  1 
ATOM   1224 N  NE  . ARG A 1 158 ? 3.581  38.177 24.151  1.00 51.76 ? 158 ARG A NE  1 
ATOM   1225 C  CZ  . ARG A 1 158 ? 2.480  37.879 23.463  1.00 57.02 ? 158 ARG A CZ  1 
ATOM   1226 N  NH1 . ARG A 1 158 ? 1.628  36.966 23.907  1.00 55.59 ? 158 ARG A NH1 1 
ATOM   1227 N  NH2 . ARG A 1 158 ? 2.243  38.506 22.322  1.00 56.36 ? 158 ARG A NH2 1 
ATOM   1228 N  N   . VAL A 1 159 ? 8.828  38.089 25.904  1.00 17.72 ? 159 VAL A N   1 
ATOM   1229 C  CA  . VAL A 1 159 ? 9.586  38.369 27.142  1.00 19.65 ? 159 VAL A CA  1 
ATOM   1230 C  C   . VAL A 1 159 ? 8.799  39.455 27.885  1.00 20.89 ? 159 VAL A C   1 
ATOM   1231 O  O   . VAL A 1 159 ? 8.458  40.422 27.262  1.00 23.72 ? 159 VAL A O   1 
ATOM   1232 C  CB  . VAL A 1 159 ? 11.041 38.782 26.834  1.00 21.59 ? 159 VAL A CB  1 
ATOM   1233 C  CG1 . VAL A 1 159 ? 11.862 38.897 28.102  1.00 27.43 ? 159 VAL A CG1 1 
ATOM   1234 C  CG2 . VAL A 1 159 ? 11.735 37.797 25.918  1.00 24.46 ? 159 VAL A CG2 1 
ATOM   1235 N  N   . SER A 1 160 ? 8.585  39.316 29.189  1.00 24.62 ? 160 SER A N   1 
ATOM   1236 C  CA  . SER A 1 160 ? 7.936  40.352 30.049  1.00 29.39 ? 160 SER A CA  1 
ATOM   1237 C  C   . SER A 1 160 ? 8.775  41.641 30.101  1.00 31.87 ? 160 SER A C   1 
ATOM   1238 O  O   . SER A 1 160 ? 9.929  41.628 29.650  1.00 31.12 ? 160 SER A O   1 
ATOM   1239 C  CB  . SER A 1 160 ? 7.742  39.816 31.432  1.00 30.05 ? 160 SER A CB  1 
ATOM   1240 O  OG  . SER A 1 160 ? 9.018  39.720 32.061  1.00 35.22 ? 160 SER A OG  1 
ATOM   1241 N  N   . SER A 1 161 ? 8.256  42.727 30.702  1.00 38.17 ? 161 SER A N   1 
ATOM   1242 C  CA  . SER A 1 161 ? 9.034  43.987 30.888  1.00 39.59 ? 161 SER A CA  1 
ATOM   1243 C  C   . SER A 1 161 ? 10.259 43.719 31.783  1.00 42.72 ? 161 SER A C   1 
ATOM   1244 O  O   . SER A 1 161 ? 11.376 44.167 31.416  1.00 43.38 ? 161 SER A O   1 
ATOM   1245 C  CB  . SER A 1 161 ? 8.163  45.116 31.411  1.00 42.94 ? 161 SER A CB  1 
ATOM   1246 O  OG  . SER A 1 161 ? 7.057  44.625 32.157  1.00 42.26 ? 161 SER A OG  1 
ATOM   1247 N  N   . ASN A 1 162 ? 10.103 42.910 32.838  1.00 42.49 ? 162 ASN A N   1 
ATOM   1248 C  CA  . ASN A 1 162 ? 11.210 42.539 33.766  1.00 44.88 ? 162 ASN A CA  1 
ATOM   1249 C  C   . ASN A 1 162 ? 12.214 41.592 33.081  1.00 46.37 ? 162 ASN A C   1 
ATOM   1250 O  O   . ASN A 1 162 ? 13.211 41.246 33.742  1.00 50.19 ? 162 ASN A O   1 
ATOM   1251 C  CB  . ASN A 1 162 ? 10.689 41.957 35.084  1.00 49.21 ? 162 ASN A CB  1 
ATOM   1252 C  CG  . ASN A 1 162 ? 10.068 40.575 34.969  1.00 59.41 ? 162 ASN A CG  1 
ATOM   1253 O  OD1 . ASN A 1 162 ? 10.185 39.902 33.948  1.00 62.92 ? 162 ASN A OD1 1 
ATOM   1254 N  ND2 . ASN A 1 162 ? 9.406  40.127 36.024  1.00 56.22 ? 162 ASN A ND2 1 
ATOM   1255 N  N   . GLY A 1 163 ? 11.978 41.166 31.828  1.00 40.83 ? 163 GLY A N   1 
ATOM   1256 C  CA  . GLY A 1 163 ? 12.937 40.347 31.053  1.00 38.60 ? 163 GLY A CA  1 
ATOM   1257 C  C   . GLY A 1 163 ? 12.725 38.838 31.188  1.00 32.08 ? 163 GLY A C   1 
ATOM   1258 O  O   . GLY A 1 163 ? 13.552 38.096 30.668  1.00 35.50 ? 163 GLY A O   1 
ATOM   1259 N  N   . SER A 1 164 ? 11.657 38.382 31.853  1.00 30.63 ? 164 SER A N   1 
ATOM   1260 C  CA  . SER A 1 164 ? 11.317 36.943 32.018  1.00 25.91 ? 164 SER A CA  1 
ATOM   1261 C  C   . SER A 1 164 ? 10.773 36.398 30.704  1.00 20.47 ? 164 SER A C   1 
ATOM   1262 O  O   . SER A 1 164 ? 9.731  36.849 30.242  1.00 20.74 ? 164 SER A O   1 
ATOM   1263 C  CB  . SER A 1 164 ? 10.306 36.671 33.111  1.00 29.17 ? 164 SER A CB  1 
ATOM   1264 O  OG  . SER A 1 164 ? 10.900 36.815 34.387  1.00 34.07 ? 164 SER A OG  1 
ATOM   1265 N  N   . PRO A 1 165 ? 11.354 35.312 30.148  1.00 18.99 ? 165 PRO A N   1 
ATOM   1266 C  CA  . PRO A 1 165 ? 10.753 34.661 28.980  1.00 18.85 ? 165 PRO A CA  1 
ATOM   1267 C  C   . PRO A 1 165 ? 9.452  33.943 29.366  1.00 20.60 ? 165 PRO A C   1 
ATOM   1268 O  O   . PRO A 1 165 ? 9.285  33.512 30.500  1.00 21.45 ? 165 PRO A O   1 
ATOM   1269 C  CB  . PRO A 1 165 ? 11.861 33.695 28.537  1.00 18.34 ? 165 PRO A CB  1 
ATOM   1270 C  CG  . PRO A 1 165 ? 12.540 33.316 29.842  1.00 18.32 ? 165 PRO A CG  1 
ATOM   1271 C  CD  . PRO A 1 165 ? 12.563 34.616 30.619  1.00 19.52 ? 165 PRO A CD  1 
ATOM   1272 N  N   . GLN A 1 166 ? 8.521  33.933 28.431  1.00 19.11 ? 166 GLN A N   1 
ATOM   1273 C  CA  . GLN A 1 166 ? 7.180  33.358 28.576  1.00 18.62 ? 166 GLN A CA  1 
ATOM   1274 C  C   . GLN A 1 166 ? 7.142  32.032 27.832  1.00 19.05 ? 166 GLN A C   1 
ATOM   1275 O  O   . GLN A 1 166 ? 7.777  31.901 26.763  1.00 17.04 ? 166 GLN A O   1 
ATOM   1276 C  CB  . GLN A 1 166 ? 6.131  34.323 28.028  1.00 22.11 ? 166 GLN A CB  1 
ATOM   1277 C  CG  . GLN A 1 166 ? 6.137  35.700 28.698  1.00 25.06 ? 166 GLN A CG  1 
ATOM   1278 C  CD  . GLN A 1 166 ? 6.075  35.610 30.199  1.00 30.13 ? 166 GLN A CD  1 
ATOM   1279 O  OE1 . GLN A 1 166 ? 5.125  35.045 30.746  1.00 35.77 ? 166 GLN A OE1 1 
ATOM   1280 N  NE2 . GLN A 1 166 ? 7.076  36.171 30.865  1.00 31.57 ? 166 GLN A NE2 1 
ATOM   1281 N  N   . GLY A 1 167 ? 6.344  31.094 28.335  1.00 17.60 ? 167 GLY A N   1 
ATOM   1282 C  CA  . GLY A 1 167 ? 6.047  29.816 27.681  1.00 16.94 ? 167 GLY A CA  1 
ATOM   1283 C  C   . GLY A 1 167 ? 5.038  29.948 26.561  1.00 15.36 ? 167 GLY A C   1 
ATOM   1284 O  O   . GLY A 1 167 ? 4.420  30.994 26.393  1.00 17.20 ? 167 GLY A O   1 
ATOM   1285 N  N   . SER A 1 168 ? 4.922  28.916 25.753  1.00 15.45 ? 168 SER A N   1 
ATOM   1286 C  CA  . SER A 1 168 ? 3.886  28.732 24.720  1.00 16.61 ? 168 SER A CA  1 
ATOM   1287 C  C   . SER A 1 168 ? 3.908  29.884 23.720  1.00 16.68 ? 168 SER A C   1 
ATOM   1288 O  O   . SER A 1 168 ? 2.851  30.381 23.349  1.00 17.20 ? 168 SER A O   1 
ATOM   1289 C  CB  . SER A 1 168 ? 2.526  28.554 25.414  1.00 20.82 ? 168 SER A CB  1 
ATOM   1290 O  OG  . SER A 1 168 ? 2.576  27.381 26.233  1.00 23.52 ? 168 SER A OG  1 
ATOM   1291 N  N   . SER A 1 169 ? 5.118  30.314 23.339  1.00 13.54 ? 169 SER A N   1 
ATOM   1292 C  CA  . SER A 1 169 ? 5.336  31.488 22.465  1.00 13.34 ? 169 SER A CA  1 
ATOM   1293 C  C   . SER A 1 169 ? 5.987  31.029 21.163  1.00 12.79 ? 169 SER A C   1 
ATOM   1294 O  O   . SER A 1 169 ? 6.701  30.034 21.122  1.00 12.56 ? 169 SER A O   1 
ATOM   1295 C  CB  . SER A 1 169 ? 6.179  32.509 23.164  1.00 13.70 ? 169 SER A CB  1 
ATOM   1296 O  OG  . SER A 1 169 ? 6.377  33.670 22.374  1.00 14.80 ? 169 SER A OG  1 
ATOM   1297 N  N   . VAL A 1 170 ? 5.654  31.701 20.085  1.00 12.81 ? 170 VAL A N   1 
ATOM   1298 C  CA  . VAL A 1 170 ? 6.300  31.403 18.786  1.00 13.25 ? 170 VAL A CA  1 
ATOM   1299 C  C   . VAL A 1 170 ? 6.401  32.714 18.008  1.00 12.71 ? 170 VAL A C   1 
ATOM   1300 O  O   . VAL A 1 170 ? 5.472  33.551 18.047  1.00 12.67 ? 170 VAL A O   1 
ATOM   1301 C  CB  . VAL A 1 170 ? 5.534  30.300 18.039  1.00 14.81 ? 170 VAL A CB  1 
ATOM   1302 C  CG1 . VAL A 1 170 ? 4.105  30.676 17.710  1.00 15.23 ? 170 VAL A CG1 1 
ATOM   1303 C  CG2 . VAL A 1 170 ? 6.280  29.855 16.791  1.00 15.40 ? 170 VAL A CG2 1 
ATOM   1304 N  N   . GLY A 1 171 ? 7.509  32.914 17.334  1.00 12.40 ? 171 GLY A N   1 
ATOM   1305 C  CA  . GLY A 1 171 ? 7.683  34.136 16.551  1.00 12.13 ? 171 GLY A CA  1 
ATOM   1306 C  C   . GLY A 1 171 ? 8.739  33.989 15.476  1.00 11.45 ? 171 GLY A C   1 
ATOM   1307 O  O   . GLY A 1 171 ? 9.618  33.152 15.628  1.00 12.38 ? 171 GLY A O   1 
ATOM   1308 N  N   . ARG A 1 172 ? 8.596  34.763 14.406  1.00 11.21 ? 172 ARG A N   1 
ATOM   1309 C  CA  . ARG A 1 172 ? 9.460  34.696 13.219  1.00 11.20 ? 172 ARG A CA  1 
ATOM   1310 C  C   . ARG A 1 172 ? 9.711  36.094 12.696  1.00 11.12 ? 172 ARG A C   1 
ATOM   1311 O  O   . ARG A 1 172 ? 8.891  36.966 12.869  1.00 10.63 ? 172 ARG A O   1 
ATOM   1312 C  CB  . ARG A 1 172 ? 8.888  33.807 12.117  1.00 12.15 ? 172 ARG A CB  1 
ATOM   1313 C  CG  . ARG A 1 172 ? 8.413  32.487 12.684  1.00 12.56 ? 172 ARG A CG  1 
ATOM   1314 C  CD  . ARG A 1 172 ? 8.296  31.405 11.687  1.00 13.20 ? 172 ARG A CD  1 
ATOM   1315 N  NE  . ARG A 1 172 ? 7.655  31.787 10.447  1.00 13.81 ? 172 ARG A NE  1 
ATOM   1316 C  CZ  . ARG A 1 172 ? 7.290  30.916 9.499   1.00 14.46 ? 172 ARG A CZ  1 
ATOM   1317 N  NH1 . ARG A 1 172 ? 7.495  29.613 9.655   1.00 14.16 ? 172 ARG A NH1 1 
ATOM   1318 N  NH2 . ARG A 1 172 ? 6.797  31.376 8.362   1.00 16.02 ? 172 ARG A NH2 1 
ATOM   1319 N  N   . ALA A 1 173 ? 10.891 36.273 12.099  1.00 10.39 ? 173 ALA A N   1 
ATOM   1320 C  CA  . ALA A 1 173 ? 11.238 37.466 11.331  1.00 10.99 ? 173 ALA A CA  1 
ATOM   1321 C  C   . ALA A 1 173 ? 11.697 37.007 9.963   1.00 11.09 ? 173 ALA A C   1 
ATOM   1322 O  O   . ALA A 1 173 ? 12.662 36.233 9.891   1.00 12.44 ? 173 ALA A O   1 
ATOM   1323 C  CB  . ALA A 1 173 ? 12.299 38.275 12.051  1.00 11.65 ? 173 ALA A CB  1 
ATOM   1324 N  N   . LEU A 1 174 ? 11.147 37.601 8.915   1.00 11.16 ? 174 LEU A N   1 
ATOM   1325 C  CA  . LEU A 1 174 ? 11.613 37.300 7.527   1.00 10.88 ? 174 LEU A CA  1 
ATOM   1326 C  C   . LEU A 1 174 ? 12.093 38.585 6.847   1.00 11.51 ? 174 LEU A C   1 
ATOM   1327 O  O   . LEU A 1 174 ? 11.469 39.641 7.008   1.00 11.35 ? 174 LEU A O   1 
ATOM   1328 C  CB  . LEU A 1 174 ? 10.510 36.677 6.657   1.00 12.52 ? 174 LEU A CB  1 
ATOM   1329 C  CG  . LEU A 1 174 ? 10.007 35.332 7.130   1.00 15.77 ? 174 LEU A CG  1 
ATOM   1330 C  CD1 . LEU A 1 174 ? 9.028  35.526 8.260   1.00 16.87 ? 174 LEU A CD1 1 
ATOM   1331 C  CD2 . LEU A 1 174 ? 9.320  34.567 6.010   1.00 17.77 ? 174 LEU A CD2 1 
ATOM   1332 N  N   . PHE A 1 175 ? 13.141 38.497 6.036   1.00 10.35 ? 175 PHE A N   1 
ATOM   1333 C  CA  . PHE A 1 175 ? 13.525 39.678 5.263   1.00 10.64 ? 175 PHE A CA  1 
ATOM   1334 C  C   . PHE A 1 175 ? 12.437 39.981 4.214   1.00 11.74 ? 175 PHE A C   1 
ATOM   1335 O  O   . PHE A 1 175 ? 11.894 39.089 3.581   1.00 11.57 ? 175 PHE A O   1 
ATOM   1336 C  CB  . PHE A 1 175 ? 14.936 39.531 4.696   1.00 11.92 ? 175 PHE A CB  1 
ATOM   1337 C  CG  . PHE A 1 175 ? 15.429 40.787 4.033   1.00 12.87 ? 175 PHE A CG  1 
ATOM   1338 C  CD1 . PHE A 1 175 ? 15.821 41.884 4.790   1.00 12.53 ? 175 PHE A CD1 1 
ATOM   1339 C  CD2 . PHE A 1 175 ? 15.504 40.864 2.656   1.00 13.21 ? 175 PHE A CD2 1 
ATOM   1340 C  CE1 . PHE A 1 175 ? 16.251 43.059 4.200   1.00 14.27 ? 175 PHE A CE1 1 
ATOM   1341 C  CE2 . PHE A 1 175 ? 15.972 42.038 2.074   1.00 13.89 ? 175 PHE A CE2 1 
ATOM   1342 C  CZ  . PHE A 1 175 ? 16.315 43.126 2.840   1.00 13.98 ? 175 PHE A CZ  1 
ATOM   1343 N  N   . TYR A 1 176 ? 12.148 41.266 4.027   1.00 12.48 ? 176 TYR A N   1 
ATOM   1344 C  CA  . TYR A 1 176 ? 10.980 41.728 3.235   1.00 14.07 ? 176 TYR A CA  1 
ATOM   1345 C  C   . TYR A 1 176 ? 11.158 41.310 1.760   1.00 13.21 ? 176 TYR A C   1 
ATOM   1346 O  O   . TYR A 1 176 ? 10.216 40.813 1.211   1.00 14.93 ? 176 TYR A O   1 
ATOM   1347 C  CB  . TYR A 1 176 ? 10.831 43.244 3.389   1.00 16.02 ? 176 TYR A CB  1 
ATOM   1348 C  CG  . TYR A 1 176 ? 9.545  43.806 2.854   1.00 19.60 ? 176 TYR A CG  1 
ATOM   1349 C  CD1 . TYR A 1 176 ? 9.444  44.203 1.538   1.00 22.28 ? 176 TYR A CD1 1 
ATOM   1350 C  CD2 . TYR A 1 176 ? 8.454  43.988 3.671   1.00 28.80 ? 176 TYR A CD2 1 
ATOM   1351 C  CE1 . TYR A 1 176 ? 8.263  44.726 1.030   1.00 27.23 ? 176 TYR A CE1 1 
ATOM   1352 C  CE2 . TYR A 1 176 ? 7.268  44.509 3.183   1.00 30.79 ? 176 TYR A CE2 1 
ATOM   1353 C  CZ  . TYR A 1 176 ? 7.177  44.895 1.861   1.00 26.44 ? 176 TYR A CZ  1 
ATOM   1354 O  OH  . TYR A 1 176 ? 5.981  45.324 1.359   1.00 30.42 ? 176 TYR A OH  1 
ATOM   1355 N  N   . ALA A 1 177 ? 12.348 41.415 1.202   1.00 13.24 ? 177 ALA A N   1 
ATOM   1356 C  CA  . ALA A 1 177 ? 12.567 41.156 -0.250  1.00 14.68 ? 177 ALA A CA  1 
ATOM   1357 C  C   . ALA A 1 177 ? 12.671 39.651 -0.443  1.00 13.89 ? 177 ALA A C   1 
ATOM   1358 O  O   . ALA A 1 177 ? 13.444 39.000 0.257   1.00 14.44 ? 177 ALA A O   1 
ATOM   1359 C  CB  . ALA A 1 177 ? 13.809 41.799 -0.781  1.00 15.35 ? 177 ALA A CB  1 
ATOM   1360 N  N   . PRO A 1 178 ? 11.975 39.087 -1.450  1.00 15.00 ? 178 PRO A N   1 
ATOM   1361 C  CA  . PRO A 1 178 ? 12.303 37.735 -1.912  1.00 15.75 ? 178 PRO A CA  1 
ATOM   1362 C  C   . PRO A 1 178 ? 13.741 37.644 -2.423  1.00 13.83 ? 178 PRO A C   1 
ATOM   1363 O  O   . PRO A 1 178 ? 14.281 38.666 -2.893  1.00 13.86 ? 178 PRO A O   1 
ATOM   1364 C  CB  . PRO A 1 178 ? 11.321 37.511 -3.071  1.00 16.62 ? 178 PRO A CB  1 
ATOM   1365 C  CG  . PRO A 1 178 ? 10.162 38.415 -2.723  1.00 19.01 ? 178 PRO A CG  1 
ATOM   1366 C  CD  . PRO A 1 178 ? 10.801 39.647 -2.118  1.00 17.08 ? 178 PRO A CD  1 
ATOM   1367 N  N   . VAL A 1 179 ? 14.286 36.426 -2.358  1.00 12.32 ? 179 VAL A N   1 
ATOM   1368 C  CA  . VAL A 1 179 ? 15.673 36.052 -2.685  1.00 12.05 ? 179 VAL A CA  1 
ATOM   1369 C  C   . VAL A 1 179 ? 15.595 35.051 -3.841  1.00 12.42 ? 179 VAL A C   1 
ATOM   1370 O  O   . VAL A 1 179 ? 14.818 34.069 -3.777  1.00 11.43 ? 179 VAL A O   1 
ATOM   1371 C  CB  . VAL A 1 179 ? 16.387 35.440 -1.477  1.00 12.40 ? 179 VAL A CB  1 
ATOM   1372 C  CG1 . VAL A 1 179 ? 17.819 35.071 -1.792  1.00 13.99 ? 179 VAL A CG1 1 
ATOM   1373 C  CG2 . VAL A 1 179 ? 16.316 36.396 -0.277  1.00 12.32 ? 179 VAL A CG2 1 
ATOM   1374 N  N   . HIS A 1 180 ? 16.403 35.284 -4.858  1.00 11.85 ? 180 HIS A N   1 
ATOM   1375 C  CA  . HIS A 1 180 ? 16.481 34.419 -6.055  1.00 12.44 ? 180 HIS A CA  1 
ATOM   1376 C  C   . HIS A 1 180 ? 17.617 33.400 -5.891  1.00 13.26 ? 180 HIS A C   1 
ATOM   1377 O  O   . HIS A 1 180 ? 18.750 33.789 -5.757  1.00 14.18 ? 180 HIS A O   1 
ATOM   1378 C  CB  . HIS A 1 180 ? 16.633 35.329 -7.269  1.00 12.79 ? 180 HIS A CB  1 
ATOM   1379 C  CG  . HIS A 1 180 ? 16.192 34.689 -8.530  1.00 13.24 ? 180 HIS A CG  1 
ATOM   1380 N  ND1 . HIS A 1 180 ? 16.446 35.263 -9.757  1.00 15.41 ? 180 HIS A ND1 1 
ATOM   1381 C  CD2 . HIS A 1 180 ? 15.390 33.649 -8.760  1.00 13.76 ? 180 HIS A CD2 1 
ATOM   1382 C  CE1 . HIS A 1 180 ? 15.852 34.527 -10.703 1.00 15.01 ? 180 HIS A CE1 1 
ATOM   1383 N  NE2 . HIS A 1 180 ? 15.224 33.540 -10.134 1.00 15.55 ? 180 HIS A NE2 1 
ATOM   1384 N  N   . ILE A 1 181 ? 17.311 32.100 -5.813  1.00 13.80 ? 181 ILE A N   1 
ATOM   1385 C  CA  . ILE A 1 181 ? 18.345 31.075 -5.472  1.00 15.11 ? 181 ILE A CA  1 
ATOM   1386 C  C   . ILE A 1 181 ? 18.539 30.117 -6.643  1.00 15.06 ? 181 ILE A C   1 
ATOM   1387 O  O   . ILE A 1 181 ? 19.503 29.281 -6.577  1.00 16.11 ? 181 ILE A O   1 
ATOM   1388 C  CB  . ILE A 1 181 ? 18.003 30.332 -4.177  1.00 16.20 ? 181 ILE A CB  1 
ATOM   1389 C  CG1 . ILE A 1 181 ? 16.688 29.565 -4.274  1.00 15.94 ? 181 ILE A CG1 1 
ATOM   1390 C  CG2 . ILE A 1 181 ? 18.020 31.271 -2.965  1.00 16.87 ? 181 ILE A CG2 1 
ATOM   1391 C  CD1 . ILE A 1 181 ? 16.555 28.511 -3.205  1.00 18.19 ? 181 ILE A CD1 1 
ATOM   1392 N  N   . TRP A 1 182 ? 17.854 30.338 -7.749  1.00 14.58 ? 182 TRP A N   1 
ATOM   1393 C  CA  . TRP A 1 182 ? 18.064 29.548 -8.982  1.00 14.58 ? 182 TRP A CA  1 
ATOM   1394 C  C   . TRP A 1 182 ? 17.664 30.411 -10.168 1.00 15.93 ? 182 TRP A C   1 
ATOM   1395 O  O   . TRP A 1 182 ? 16.660 31.112 -10.104 1.00 15.51 ? 182 TRP A O   1 
ATOM   1396 C  CB  . TRP A 1 182 ? 17.292 28.206 -8.952  1.00 16.63 ? 182 TRP A CB  1 
ATOM   1397 C  CG  . TRP A 1 182 ? 17.476 27.425 -10.228 1.00 17.00 ? 182 TRP A CG  1 
ATOM   1398 C  CD1 . TRP A 1 182 ? 18.478 26.531 -10.506 1.00 18.65 ? 182 TRP A CD1 1 
ATOM   1399 C  CD2 . TRP A 1 182 ? 16.696 27.544 -11.434 1.00 16.35 ? 182 TRP A CD2 1 
ATOM   1400 N  NE1 . TRP A 1 182 ? 18.369 26.083 -11.799 1.00 18.25 ? 182 TRP A NE1 1 
ATOM   1401 C  CE2 . TRP A 1 182 ? 17.272 26.662 -12.387 1.00 19.21 ? 182 TRP A CE2 1 
ATOM   1402 C  CE3 . TRP A 1 182 ? 15.528 28.245 -11.775 1.00 17.18 ? 182 TRP A CE3 1 
ATOM   1403 C  CZ2 . TRP A 1 182 ? 16.738 26.514 -13.672 1.00 18.35 ? 182 TRP A CZ2 1 
ATOM   1404 C  CZ3 . TRP A 1 182 ? 14.985 28.065 -13.031 1.00 19.20 ? 182 TRP A CZ3 1 
ATOM   1405 C  CH2 . TRP A 1 182 ? 15.599 27.231 -13.972 1.00 17.92 ? 182 TRP A CH2 1 
ATOM   1406 N  N   . GLU A 1 183 ? 18.380 30.310 -11.256 1.00 15.16 ? 183 GLU A N   1 
ATOM   1407 C  CA  . GLU A 1 183 ? 17.985 30.926 -12.535 1.00 18.02 ? 183 GLU A CA  1 
ATOM   1408 C  C   . GLU A 1 183 ? 18.558 29.984 -13.606 1.00 17.76 ? 183 GLU A C   1 
ATOM   1409 O  O   . GLU A 1 183 ? 19.584 29.319 -13.355 1.00 17.04 ? 183 GLU A O   1 
ATOM   1410 C  CB  . GLU A 1 183 ? 18.489 32.378 -12.536 1.00 21.49 ? 183 GLU A CB  1 
ATOM   1411 C  CG  . GLU A 1 183 ? 18.082 33.196 -13.729 1.00 28.29 ? 183 GLU A CG  1 
ATOM   1412 C  CD  . GLU A 1 183 ? 19.019 33.015 -14.913 1.00 36.21 ? 183 GLU A CD  1 
ATOM   1413 O  OE1 . GLU A 1 183 ? 20.224 32.685 -14.676 1.00 45.86 ? 183 GLU A OE1 1 
ATOM   1414 O  OE2 . GLU A 1 183 ? 18.556 33.160 -16.067 1.00 36.76 ? 183 GLU A OE2 1 
ATOM   1415 N  N   . SER A 1 184 ? 17.915 29.910 -14.746 1.00 16.94 ? 184 SER A N   1 
ATOM   1416 C  CA  . SER A 1 184 ? 18.288 28.902 -15.756 1.00 17.97 ? 184 SER A CA  1 
ATOM   1417 C  C   . SER A 1 184 ? 19.717 29.133 -16.287 1.00 17.67 ? 184 SER A C   1 
ATOM   1418 O  O   . SER A 1 184 ? 20.341 28.157 -16.682 1.00 16.84 ? 184 SER A O   1 
ATOM   1419 C  CB  . SER A 1 184 ? 17.253 28.867 -16.827 1.00 17.18 ? 184 SER A CB  1 
ATOM   1420 O  OG  . SER A 1 184 ? 17.158 30.108 -17.492 1.00 18.73 ? 184 SER A OG  1 
ATOM   1421 N  N   . SER A 1 185 ? 20.258 30.354 -16.266 1.00 17.80 ? 185 SER A N   1 
ATOM   1422 C  CA  . SER A 1 185 ? 21.636 30.646 -16.752 1.00 19.70 ? 185 SER A CA  1 
ATOM   1423 C  C   . SER A 1 185 ? 22.661 30.587 -15.632 1.00 18.26 ? 185 SER A C   1 
ATOM   1424 O  O   . SER A 1 185 ? 23.793 30.914 -15.900 1.00 16.49 ? 185 SER A O   1 
ATOM   1425 C  CB  . SER A 1 185 ? 21.703 32.009 -17.439 1.00 24.44 ? 185 SER A CB  1 
ATOM   1426 O  OG  . SER A 1 185 ? 20.882 31.997 -18.590 1.00 33.84 ? 185 SER A OG  1 
ATOM   1427 N  N   . ALA A 1 186 ? 22.269 30.267 -14.406 1.00 17.78 ? 186 ALA A N   1 
ATOM   1428 C  CA  . ALA A 1 186 ? 23.175 30.322 -13.245 1.00 19.08 ? 186 ALA A CA  1 
ATOM   1429 C  C   . ALA A 1 186 ? 24.247 29.251 -13.411 1.00 17.83 ? 186 ALA A C   1 
ATOM   1430 O  O   . ALA A 1 186 ? 23.877 28.124 -13.717 1.00 17.87 ? 186 ALA A O   1 
ATOM   1431 C  CB  . ALA A 1 186 ? 22.432 30.128 -11.945 1.00 19.74 ? 186 ALA A CB  1 
ATOM   1432 N  N   . VAL A 1 187 ? 25.530 29.593 -13.254 1.00 16.09 ? 187 VAL A N   1 
ATOM   1433 C  CA  . VAL A 1 187 ? 26.585 28.561 -13.156 1.00 16.57 ? 187 VAL A CA  1 
ATOM   1434 C  C   . VAL A 1 187 ? 26.941 28.296 -11.689 1.00 15.00 ? 187 VAL A C   1 
ATOM   1435 O  O   . VAL A 1 187 ? 27.469 27.241 -11.414 1.00 15.00 ? 187 VAL A O   1 
ATOM   1436 C  CB  . VAL A 1 187 ? 27.826 28.924 -13.982 1.00 19.31 ? 187 VAL A CB  1 
ATOM   1437 C  CG1 . VAL A 1 187 ? 27.453 29.231 -15.428 1.00 20.31 ? 187 VAL A CG1 1 
ATOM   1438 C  CG2 . VAL A 1 187 ? 28.591 30.066 -13.391 1.00 20.57 ? 187 VAL A CG2 1 
ATOM   1439 N  N   . VAL A 1 188 ? 26.717 29.243 -10.785 1.00 14.87 ? 188 VAL A N   1 
ATOM   1440 C  CA  . VAL A 1 188 ? 26.924 28.996 -9.335  1.00 15.86 ? 188 VAL A CA  1 
ATOM   1441 C  C   . VAL A 1 188 ? 25.982 29.909 -8.565  1.00 15.30 ? 188 VAL A C   1 
ATOM   1442 O  O   . VAL A 1 188 ? 25.790 31.084 -8.937  1.00 15.39 ? 188 VAL A O   1 
ATOM   1443 C  CB  . VAL A 1 188 ? 28.387 29.157 -8.875  1.00 19.33 ? 188 VAL A CB  1 
ATOM   1444 C  CG1 . VAL A 1 188 ? 28.984 30.454 -9.294  1.00 21.96 ? 188 VAL A CG1 1 
ATOM   1445 C  CG2 . VAL A 1 188 ? 28.556 28.953 -7.374  1.00 20.93 ? 188 VAL A CG2 1 
ATOM   1446 N  N   . ALA A 1 189 ? 25.328 29.344 -7.565  1.00 14.29 ? 189 ALA A N   1 
ATOM   1447 C  CA  . ALA A 1 189 ? 24.413 30.069 -6.668  1.00 13.56 ? 189 ALA A CA  1 
ATOM   1448 C  C   . ALA A 1 189 ? 24.915 29.800 -5.267  1.00 13.27 ? 189 ALA A C   1 
ATOM   1449 O  O   . ALA A 1 189 ? 25.303 28.660 -5.004  1.00 15.11 ? 189 ALA A O   1 
ATOM   1450 C  CB  . ALA A 1 189 ? 22.986 29.585 -6.830  1.00 15.25 ? 189 ALA A CB  1 
ATOM   1451 N  N   . SER A 1 190 ? 24.970 30.796 -4.408  1.00 12.77 ? 190 SER A N   1 
ATOM   1452 C  CA  . SER A 1 190 ? 25.489 30.557 -3.044  1.00 13.12 ? 190 SER A CA  1 
ATOM   1453 C  C   . SER A 1 190 ? 24.718 31.440 -2.083  1.00 13.55 ? 190 SER A C   1 
ATOM   1454 O  O   . SER A 1 190 ? 24.222 32.500 -2.483  1.00 12.98 ? 190 SER A O   1 
ATOM   1455 C  CB  . SER A 1 190 ? 27.000 30.791 -2.960  1.00 14.91 ? 190 SER A CB  1 
ATOM   1456 O  OG  . SER A 1 190 ? 27.343 32.141 -3.292  1.00 19.78 ? 190 SER A OG  1 
ATOM   1457 N  N   . PHE A 1 191 ? 24.767 31.077 -0.823  1.00 12.93 ? 191 PHE A N   1 
ATOM   1458 C  CA  . PHE A 1 191 ? 24.345 32.016 0.218   1.00 13.54 ? 191 PHE A CA  1 
ATOM   1459 C  C   . PHE A 1 191 ? 25.126 31.737 1.475   1.00 13.64 ? 191 PHE A C   1 
ATOM   1460 O  O   . PHE A 1 191 ? 25.692 30.648 1.673   1.00 13.08 ? 191 PHE A O   1 
ATOM   1461 C  CB  . PHE A 1 191 ? 22.827 31.978 0.409   1.00 14.69 ? 191 PHE A CB  1 
ATOM   1462 C  CG  . PHE A 1 191 ? 22.252 30.713 0.984   1.00 17.82 ? 191 PHE A CG  1 
ATOM   1463 C  CD1 . PHE A 1 191 ? 22.310 30.445 2.339   1.00 20.43 ? 191 PHE A CD1 1 
ATOM   1464 C  CD2 . PHE A 1 191 ? 21.596 29.833 0.156   1.00 18.99 ? 191 PHE A CD2 1 
ATOM   1465 C  CE1 . PHE A 1 191 ? 21.785 29.252 2.839   1.00 21.06 ? 191 PHE A CE1 1 
ATOM   1466 C  CE2 . PHE A 1 191 ? 20.995 28.692 0.662   1.00 22.19 ? 191 PHE A CE2 1 
ATOM   1467 C  CZ  . PHE A 1 191 ? 21.143 28.380 2.002   1.00 21.61 ? 191 PHE A CZ  1 
ATOM   1468 N  N   . GLU A 1 192 ? 25.146 32.755 2.314   1.00 13.84 ? 192 GLU A N   1 
ATOM   1469 C  CA  . GLU A 1 192 ? 25.721 32.665 3.660   1.00 15.32 ? 192 GLU A CA  1 
ATOM   1470 C  C   . GLU A 1 192 ? 24.817 33.474 4.583   1.00 13.23 ? 192 GLU A C   1 
ATOM   1471 O  O   . GLU A 1 192 ? 24.272 34.494 4.170   1.00 12.47 ? 192 GLU A O   1 
ATOM   1472 C  CB  . GLU A 1 192 ? 27.198 33.042 3.665   1.00 19.93 ? 192 GLU A CB  1 
ATOM   1473 C  CG  . GLU A 1 192 ? 27.546 34.459 3.313   1.00 26.04 ? 192 GLU A CG  1 
ATOM   1474 C  CD  . GLU A 1 192 ? 28.957 34.742 3.825   1.00 37.93 ? 192 GLU A CD  1 
ATOM   1475 O  OE1 . GLU A 1 192 ? 29.099 35.602 4.721   1.00 46.70 ? 192 GLU A OE1 1 
ATOM   1476 O  OE2 . GLU A 1 192 ? 29.895 34.005 3.418   1.00 43.50 ? 192 GLU A OE2 1 
ATOM   1477 N  N   . ALA A 1 193 ? 24.617 32.974 5.790   1.00 10.93 ? 193 ALA A N   1 
ATOM   1478 C  CA  . ALA A 1 193 ? 23.942 33.759 6.835   1.00 11.73 ? 193 ALA A CA  1 
ATOM   1479 C  C   . ALA A 1 193 ? 24.737 33.693 8.123   1.00 11.54 ? 193 ALA A C   1 
ATOM   1480 O  O   . ALA A 1 193 ? 25.400 32.707 8.371   1.00 11.48 ? 193 ALA A O   1 
ATOM   1481 C  CB  . ALA A 1 193 ? 22.553 33.234 7.051   1.00 11.54 ? 193 ALA A CB  1 
ATOM   1482 N  N   . THR A 1 194 ? 24.681 34.756 8.904   1.00 11.65 ? 194 THR A N   1 
ATOM   1483 C  CA  . THR A 1 194 ? 25.281 34.804 10.245  1.00 12.22 ? 194 THR A CA  1 
ATOM   1484 C  C   . THR A 1 194 ? 24.248 35.417 11.173  1.00 11.98 ? 194 THR A C   1 
ATOM   1485 O  O   . THR A 1 194 ? 23.671 36.413 10.790  1.00 12.27 ? 194 THR A O   1 
ATOM   1486 C  CB  . THR A 1 194 ? 26.580 35.602 10.263  1.00 15.34 ? 194 THR A CB  1 
ATOM   1487 O  OG1 . THR A 1 194 ? 27.506 35.019 9.347   1.00 18.29 ? 194 THR A OG1 1 
ATOM   1488 C  CG2 . THR A 1 194 ? 27.256 35.601 11.622  1.00 16.40 ? 194 THR A CG2 1 
ATOM   1489 N  N   . PHE A 1 195 ? 24.111 34.936 12.391  1.00 10.88 ? 195 PHE A N   1 
ATOM   1490 C  CA  . PHE A 1 195 ? 23.297 35.645 13.393  1.00 10.32 ? 195 PHE A CA  1 
ATOM   1491 C  C   . PHE A 1 195 ? 23.926 35.454 14.746  1.00 10.13 ? 195 PHE A C   1 
ATOM   1492 O  O   . PHE A 1 195 ? 24.648 34.447 14.979  1.00 11.83 ? 195 PHE A O   1 
ATOM   1493 C  CB  . PHE A 1 195 ? 21.825 35.264 13.370  1.00 10.75 ? 195 PHE A CB  1 
ATOM   1494 C  CG  . PHE A 1 195 ? 21.475 33.851 13.713  1.00 11.12 ? 195 PHE A CG  1 
ATOM   1495 C  CD1 . PHE A 1 195 ? 21.402 32.876 12.745  1.00 11.79 ? 195 PHE A CD1 1 
ATOM   1496 C  CD2 . PHE A 1 195 ? 21.160 33.518 15.030  1.00 12.26 ? 195 PHE A CD2 1 
ATOM   1497 C  CE1 . PHE A 1 195 ? 21.029 31.584 13.064  1.00 11.71 ? 195 PHE A CE1 1 
ATOM   1498 C  CE2 . PHE A 1 195 ? 20.781 32.224 15.342  1.00 13.65 ? 195 PHE A CE2 1 
ATOM   1499 C  CZ  . PHE A 1 195 ? 20.744 31.252 14.365  1.00 11.92 ? 195 PHE A CZ  1 
ATOM   1500 N  N   . THR A 1 196 ? 23.751 36.447 15.593  1.00 10.05 ? 196 THR A N   1 
ATOM   1501 C  CA  . THR A 1 196 ? 24.187 36.357 16.995  1.00 11.42 ? 196 THR A CA  1 
ATOM   1502 C  C   . THR A 1 196 ? 22.937 36.347 17.864  1.00 10.85 ? 196 THR A C   1 
ATOM   1503 O  O   . THR A 1 196 ? 21.965 37.032 17.547  1.00 11.96 ? 196 THR A O   1 
ATOM   1504 C  CB  . THR A 1 196 ? 25.173 37.453 17.364  1.00 14.87 ? 196 THR A CB  1 
ATOM   1505 O  OG1 . THR A 1 196 ? 24.558 38.731 17.284  1.00 16.91 ? 196 THR A OG1 1 
ATOM   1506 C  CG2 . THR A 1 196 ? 26.418 37.404 16.498  1.00 14.18 ? 196 THR A CG2 1 
ATOM   1507 N  N   . PHE A 1 197 ? 23.001 35.564 18.924  1.00 10.11 ? 197 PHE A N   1 
ATOM   1508 C  CA  . PHE A 1 197 ? 21.810 35.212 19.690  1.00 10.54 ? 197 PHE A CA  1 
ATOM   1509 C  C   . PHE A 1 197 ? 22.155 35.127 21.171  1.00 11.67 ? 197 PHE A C   1 
ATOM   1510 O  O   . PHE A 1 197 ? 23.356 34.868 21.521  1.00 11.93 ? 197 PHE A O   1 
ATOM   1511 C  CB  . PHE A 1 197 ? 21.198 33.893 19.189  1.00 11.57 ? 197 PHE A CB  1 
ATOM   1512 C  CG  . PHE A 1 197 ? 22.130 32.720 19.337  1.00 11.59 ? 197 PHE A CG  1 
ATOM   1513 C  CD1 . PHE A 1 197 ? 22.167 31.968 20.498  1.00 12.37 ? 197 PHE A CD1 1 
ATOM   1514 C  CD2 . PHE A 1 197 ? 22.998 32.388 18.306  1.00 12.37 ? 197 PHE A CD2 1 
ATOM   1515 C  CE1 . PHE A 1 197 ? 23.082 30.941 20.635  1.00 14.08 ? 197 PHE A CE1 1 
ATOM   1516 C  CE2 . PHE A 1 197 ? 23.887 31.342 18.436  1.00 12.41 ? 197 PHE A CE2 1 
ATOM   1517 C  CZ  . PHE A 1 197 ? 23.936 30.625 19.602  1.00 14.41 ? 197 PHE A CZ  1 
ATOM   1518 N  N   . LEU A 1 198 ? 21.156 35.367 21.978  1.00 12.12 ? 198 LEU A N   1 
ATOM   1519 C  CA  . LEU A 1 198 ? 21.284 35.218 23.443  1.00 12.79 ? 198 LEU A CA  1 
ATOM   1520 C  C   . LEU A 1 198 ? 20.083 34.418 23.925  1.00 11.83 ? 198 LEU A C   1 
ATOM   1521 O  O   . LEU A 1 198 ? 18.960 34.941 23.877  1.00 13.86 ? 198 LEU A O   1 
ATOM   1522 C  CB  . LEU A 1 198 ? 21.388 36.624 24.051  1.00 15.69 ? 198 LEU A CB  1 
ATOM   1523 C  CG  . LEU A 1 198 ? 22.096 36.723 25.406  1.00 21.83 ? 198 LEU A CG  1 
ATOM   1524 C  CD1 . LEU A 1 198 ? 21.949 38.135 25.983  1.00 23.59 ? 198 LEU A CD1 1 
ATOM   1525 C  CD2 . LEU A 1 198 ? 21.605 35.704 26.388  1.00 22.90 ? 198 LEU A CD2 1 
ATOM   1526 N  N   . ILE A 1 199 ? 20.334 33.165 24.314  1.00 13.02 ? 199 ILE A N   1 
ATOM   1527 C  CA  . ILE A 1 199 ? 19.315 32.257 24.882  1.00 12.87 ? 199 ILE A CA  1 
ATOM   1528 C  C   . ILE A 1 199 ? 19.581 32.181 26.386  1.00 13.91 ? 199 ILE A C   1 
ATOM   1529 O  O   . ILE A 1 199 ? 20.660 31.798 26.765  1.00 14.51 ? 199 ILE A O   1 
ATOM   1530 C  CB  . ILE A 1 199 ? 19.367 30.884 24.222  1.00 13.84 ? 199 ILE A CB  1 
ATOM   1531 C  CG1 . ILE A 1 199 ? 19.029 30.981 22.740  1.00 14.00 ? 199 ILE A CG1 1 
ATOM   1532 C  CG2 . ILE A 1 199 ? 18.449 29.910 24.943  1.00 14.36 ? 199 ILE A CG2 1 
ATOM   1533 C  CD1 . ILE A 1 199 ? 19.304 29.679 22.006  1.00 14.78 ? 199 ILE A CD1 1 
ATOM   1534 N  N   . LYS A 1 200 ? 18.621 32.683 27.153  1.00 14.92 ? 200 LYS A N   1 
ATOM   1535 C  CA  . LYS A 1 200 ? 18.731 32.753 28.634  1.00 15.71 ? 200 LYS A CA  1 
ATOM   1536 C  C   . LYS A 1 200 ? 17.437 32.162 29.202  1.00 15.68 ? 200 LYS A C   1 
ATOM   1537 O  O   . LYS A 1 200 ? 16.308 32.441 28.752  1.00 14.28 ? 200 LYS A O   1 
ATOM   1538 C  CB  . LYS A 1 200 ? 18.971 34.199 29.084  1.00 20.92 ? 200 LYS A CB  1 
ATOM   1539 C  CG  . LYS A 1 200 ? 18.956 34.445 30.588  1.00 28.17 ? 200 LYS A CG  1 
ATOM   1540 C  CD  . LYS A 1 200 ? 20.254 34.920 31.205  1.00 39.10 ? 200 LYS A CD  1 
ATOM   1541 C  CE  . LYS A 1 200 ? 20.329 34.725 32.716  1.00 45.61 ? 200 LYS A CE  1 
ATOM   1542 N  NZ  . LYS A 1 200 ? 20.396 33.281 33.111  1.00 52.31 ? 200 LYS A NZ  1 
ATOM   1543 N  N   . SER A 1 201 ? 17.578 31.348 30.231  1.00 15.97 ? 201 SER A N   1 
ATOM   1544 C  CA  . SER A 1 201 ? 16.399 30.753 30.890  1.00 15.33 ? 201 SER A CA  1 
ATOM   1545 C  C   . SER A 1 201 ? 16.665 30.784 32.382  1.00 16.66 ? 201 SER A C   1 
ATOM   1546 O  O   . SER A 1 201 ? 17.814 30.585 32.789  1.00 18.09 ? 201 SER A O   1 
ATOM   1547 C  CB  . SER A 1 201 ? 16.123 29.363 30.438  1.00 14.94 ? 201 SER A CB  1 
ATOM   1548 O  OG  . SER A 1 201 ? 14.875 28.941 30.982  1.00 19.51 ? 201 SER A OG  1 
ATOM   1549 N  N   . PRO A 1 202 ? 15.646 31.072 33.201  1.00 18.64 ? 202 PRO A N   1 
ATOM   1550 C  CA  . PRO A 1 202 ? 15.804 30.913 34.653  1.00 19.61 ? 202 PRO A CA  1 
ATOM   1551 C  C   . PRO A 1 202 ? 15.830 29.427 35.035  1.00 21.91 ? 202 PRO A C   1 
ATOM   1552 O  O   . PRO A 1 202 ? 16.088 29.100 36.185  1.00 22.42 ? 202 PRO A O   1 
ATOM   1553 C  CB  . PRO A 1 202 ? 14.540 31.588 35.198  1.00 20.79 ? 202 PRO A CB  1 
ATOM   1554 C  CG  . PRO A 1 202 ? 13.512 31.359 34.133  1.00 21.26 ? 202 PRO A CG  1 
ATOM   1555 C  CD  . PRO A 1 202 ? 14.297 31.536 32.837  1.00 19.39 ? 202 PRO A CD  1 
ATOM   1556 N  N   . ASP A 1 203 ? 15.570 28.543 34.074  1.00 20.68 ? 203 ASP A N   1 
ATOM   1557 C  CA  . ASP A 1 203 ? 15.371 27.090 34.333  1.00 21.17 ? 203 ASP A CA  1 
ATOM   1558 C  C   . ASP A 1 203 ? 16.584 26.262 33.899  1.00 23.05 ? 203 ASP A C   1 
ATOM   1559 O  O   . ASP A 1 203 ? 17.312 26.654 32.951  1.00 22.57 ? 203 ASP A O   1 
ATOM   1560 C  CB  . ASP A 1 203 ? 14.103 26.618 33.646  1.00 20.17 ? 203 ASP A CB  1 
ATOM   1561 C  CG  . ASP A 1 203 ? 12.866 27.373 34.091  1.00 23.48 ? 203 ASP A CG  1 
ATOM   1562 O  OD1 . ASP A 1 203 ? 12.699 27.609 35.328  1.00 22.41 ? 203 ASP A OD1 1 
ATOM   1563 O  OD2 . ASP A 1 203 ? 12.084 27.772 33.203  1.00 25.21 ? 203 ASP A OD2 1 
ATOM   1564 N  N   . SER A 1 204 ? 16.786 25.103 34.539  1.00 18.49 ? 204 SER A N   1 
ATOM   1565 C  CA  . SER A 1 204 ? 17.848 24.139 34.152  1.00 17.33 ? 204 SER A CA  1 
ATOM   1566 C  C   . SER A 1 204 ? 17.605 23.541 32.767  1.00 18.67 ? 204 SER A C   1 
ATOM   1567 O  O   . SER A 1 204 ? 18.553 23.021 32.181  1.00 18.59 ? 204 SER A O   1 
ATOM   1568 C  CB  . SER A 1 204 ? 17.929 23.025 35.166  1.00 18.39 ? 204 SER A CB  1 
ATOM   1569 O  OG  . SER A 1 204 ? 18.395 23.568 36.398  1.00 19.49 ? 204 SER A OG  1 
ATOM   1570 N  N   . HIS A 1 205 ? 16.347 23.500 32.343  1.00 17.10 ? 205 HIS A N   1 
ATOM   1571 C  CA  . HIS A 1 205 ? 15.931 22.939 31.044  1.00 16.64 ? 205 HIS A CA  1 
ATOM   1572 C  C   . HIS A 1 205 ? 15.307 24.030 30.190  1.00 17.76 ? 205 HIS A C   1 
ATOM   1573 O  O   . HIS A 1 205 ? 14.085 24.202 30.158  1.00 18.75 ? 205 HIS A O   1 
ATOM   1574 C  CB  . HIS A 1 205 ? 14.949 21.796 31.286  1.00 17.30 ? 205 HIS A CB  1 
ATOM   1575 C  CG  . HIS A 1 205 ? 15.590 20.677 32.025  1.00 16.28 ? 205 HIS A CG  1 
ATOM   1576 N  ND1 . HIS A 1 205 ? 15.347 20.427 33.364  1.00 22.00 ? 205 HIS A ND1 1 
ATOM   1577 C  CD2 . HIS A 1 205 ? 16.479 19.766 31.609  1.00 17.36 ? 205 HIS A CD2 1 
ATOM   1578 C  CE1 . HIS A 1 205 ? 16.085 19.383 33.746  1.00 17.40 ? 205 HIS A CE1 1 
ATOM   1579 N  NE2 . HIS A 1 205 ? 16.790 18.964 32.690  1.00 21.33 ? 205 HIS A NE2 1 
ATOM   1580 N  N   . PRO A 1 206 ? 16.123 24.780 29.451  1.00 13.75 ? 206 PRO A N   1 
ATOM   1581 C  CA  . PRO A 1 206 ? 15.568 25.718 28.476  1.00 14.63 ? 206 PRO A CA  1 
ATOM   1582 C  C   . PRO A 1 206 ? 14.863 25.004 27.322  1.00 12.88 ? 206 PRO A C   1 
ATOM   1583 O  O   . PRO A 1 206 ? 15.170 23.858 27.017  1.00 14.59 ? 206 PRO A O   1 
ATOM   1584 C  CB  . PRO A 1 206 ? 16.776 26.529 28.023  1.00 14.91 ? 206 PRO A CB  1 
ATOM   1585 C  CG  . PRO A 1 206 ? 17.940 25.624 28.269  1.00 16.95 ? 206 PRO A CG  1 
ATOM   1586 C  CD  . PRO A 1 206 ? 17.601 24.760 29.468  1.00 14.77 ? 206 PRO A CD  1 
ATOM   1587 N  N   . ALA A 1 207 ? 13.917 25.716 26.698  1.00 11.82 ? 207 ALA A N   1 
ATOM   1588 C  CA  . ALA A 1 207 ? 13.349 25.257 25.419  1.00 11.25 ? 207 ALA A CA  1 
ATOM   1589 C  C   . ALA A 1 207 ? 12.814 26.447 24.654  1.00 10.64 ? 207 ALA A C   1 
ATOM   1590 O  O   . ALA A 1 207 ? 12.472 27.443 25.278  1.00 11.48 ? 207 ALA A O   1 
ATOM   1591 C  CB  . ALA A 1 207 ? 12.237 24.296 25.716  1.00 11.53 ? 207 ALA A CB  1 
ATOM   1592 N  N   . ASP A 1 208 ? 12.590 26.306 23.333  1.00 10.82 ? 208 ASP A N   1 
ATOM   1593 C  CA  . ASP A 1 208 ? 12.771 25.107 22.537  1.00 10.97 ? 208 ASP A CA  1 
ATOM   1594 C  C   . ASP A 1 208 ? 13.921 25.311 21.535  1.00 11.84 ? 208 ASP A C   1 
ATOM   1595 O  O   . ASP A 1 208 ? 14.484 24.317 21.068  1.00 10.81 ? 208 ASP A O   1 
ATOM   1596 C  CB  . ASP A 1 208 ? 11.468 24.733 21.818  1.00 12.11 ? 208 ASP A CB  1 
ATOM   1597 C  CG  . ASP A 1 208 ? 10.618 23.846 22.722  1.00 15.40 ? 208 ASP A CG  1 
ATOM   1598 O  OD1 . ASP A 1 208 ? 10.886 22.587 22.747  1.00 15.81 ? 208 ASP A OD1 1 
ATOM   1599 O  OD2 . ASP A 1 208 ? 9.755  24.425 23.472  1.00 17.14 ? 208 ASP A OD2 1 
ATOM   1600 N  N   . GLY A 1 209 ? 14.219 26.561 21.163  1.00 12.20 ? 209 GLY A N   1 
ATOM   1601 C  CA  . GLY A 1 209 ? 15.357 26.835 20.270  1.00 12.28 ? 209 GLY A CA  1 
ATOM   1602 C  C   . GLY A 1 209 ? 15.063 27.899 19.227  1.00 11.38 ? 209 GLY A C   1 
ATOM   1603 O  O   . GLY A 1 209 ? 14.013 28.524 19.249  1.00 11.57 ? 209 GLY A O   1 
ATOM   1604 N  N   . ILE A 1 210 ? 16.065 28.142 18.403  1.00 10.91 ? 210 ILE A N   1 
ATOM   1605 C  CA  . ILE A 1 210 ? 16.070 29.146 17.313  1.00 10.90 ? 210 ILE A CA  1 
ATOM   1606 C  C   . ILE A 1 210 ? 16.458 28.428 16.029  1.00 11.63 ? 210 ILE A C   1 
ATOM   1607 O  O   . ILE A 1 210 ? 17.291 27.496 16.059  1.00 11.16 ? 210 ILE A O   1 
ATOM   1608 C  CB  . ILE A 1 210 ? 17.075 30.272 17.632  1.00 11.20 ? 210 ILE A CB  1 
ATOM   1609 C  CG1 . ILE A 1 210 ? 16.783 30.954 18.967  1.00 11.81 ? 210 ILE A CG1 1 
ATOM   1610 C  CG2 . ILE A 1 210 ? 17.202 31.244 16.456  1.00 12.37 ? 210 ILE A CG2 1 
ATOM   1611 C  CD1 . ILE A 1 210 ? 17.709 32.112 19.389  1.00 12.61 ? 210 ILE A CD1 1 
ATOM   1612 N  N   . ALA A 1 211 ? 15.902 28.855 14.903  1.00 11.95 ? 211 ALA A N   1 
ATOM   1613 C  CA  . ALA A 1 211 ? 16.261 28.294 13.601  1.00 11.02 ? 211 ALA A CA  1 
ATOM   1614 C  C   . ALA A 1 211 ? 16.475 29.438 12.617  1.00 12.09 ? 211 ALA A C   1 
ATOM   1615 O  O   . ALA A 1 211 ? 15.709 30.423 12.652  1.00 11.64 ? 211 ALA A O   1 
ATOM   1616 C  CB  . ALA A 1 211 ? 15.195 27.374 13.103  1.00 11.78 ? 211 ALA A CB  1 
ATOM   1617 N  N   . PHE A 1 212 ? 17.427 29.262 11.715  1.00 9.85  ? 212 PHE A N   1 
ATOM   1618 C  CA  . PHE A 1 212 ? 17.503 30.061 10.459  1.00 9.55  ? 212 PHE A CA  1 
ATOM   1619 C  C   . PHE A 1 212 ? 16.777 29.217 9.425   1.00 10.47 ? 212 PHE A C   1 
ATOM   1620 O  O   . PHE A 1 212 ? 17.022 28.005 9.348   1.00 10.57 ? 212 PHE A O   1 
ATOM   1621 C  CB  . PHE A 1 212 ? 18.945 30.303 10.027  1.00 10.21 ? 212 PHE A CB  1 
ATOM   1622 C  CG  . PHE A 1 212 ? 19.095 30.859 8.638   1.00 10.92 ? 212 PHE A CG  1 
ATOM   1623 C  CD1 . PHE A 1 212 ? 18.822 32.180 8.385   1.00 11.48 ? 212 PHE A CD1 1 
ATOM   1624 C  CD2 . PHE A 1 212 ? 19.396 30.021 7.569   1.00 11.46 ? 212 PHE A CD2 1 
ATOM   1625 C  CE1 . PHE A 1 212 ? 18.856 32.687 7.096   1.00 12.75 ? 212 PHE A CE1 1 
ATOM   1626 C  CE2 . PHE A 1 212 ? 19.457 30.538 6.283   1.00 12.27 ? 212 PHE A CE2 1 
ATOM   1627 C  CZ  . PHE A 1 212 ? 19.215 31.875 6.053   1.00 13.56 ? 212 PHE A CZ  1 
ATOM   1628 N  N   . PHE A 1 213 ? 15.907 29.832 8.634   1.00 10.37 ? 213 PHE A N   1 
ATOM   1629 C  CA  . PHE A 1 213 ? 15.134 29.020 7.662   1.00 10.84 ? 213 PHE A CA  1 
ATOM   1630 C  C   . PHE A 1 213 ? 14.994 29.757 6.334   1.00 11.48 ? 213 PHE A C   1 
ATOM   1631 O  O   . PHE A 1 213 ? 15.154 30.968 6.247   1.00 11.51 ? 213 PHE A O   1 
ATOM   1632 C  CB  . PHE A 1 213 ? 13.766 28.634 8.210   1.00 11.45 ? 213 PHE A CB  1 
ATOM   1633 C  CG  . PHE A 1 213 ? 12.758 29.751 8.322   1.00 12.46 ? 213 PHE A CG  1 
ATOM   1634 C  CD1 . PHE A 1 213 ? 12.743 30.604 9.417   1.00 12.17 ? 213 PHE A CD1 1 
ATOM   1635 C  CD2 . PHE A 1 213 ? 11.809 29.946 7.329   1.00 13.92 ? 213 PHE A CD2 1 
ATOM   1636 C  CE1 . PHE A 1 213 ? 11.807 31.619 9.523   1.00 12.35 ? 213 PHE A CE1 1 
ATOM   1637 C  CE2 . PHE A 1 213 ? 10.850 30.944 7.438   1.00 14.67 ? 213 PHE A CE2 1 
ATOM   1638 C  CZ  . PHE A 1 213 ? 10.863 31.802 8.522   1.00 14.40 ? 213 PHE A CZ  1 
ATOM   1639 N  N   . ILE A 1 214 ? 14.731 28.929 5.340   1.00 11.24 ? 214 ILE A N   1 
ATOM   1640 C  CA  . ILE A 1 214 ? 14.427 29.354 3.962   1.00 11.31 ? 214 ILE A CA  1 
ATOM   1641 C  C   . ILE A 1 214 ? 13.105 28.697 3.589   1.00 12.02 ? 214 ILE A C   1 
ATOM   1642 O  O   . ILE A 1 214 ? 12.932 27.505 3.843   1.00 11.28 ? 214 ILE A O   1 
ATOM   1643 C  CB  . ILE A 1 214 ? 15.544 28.942 3.018   1.00 12.62 ? 214 ILE A CB  1 
ATOM   1644 C  CG1 . ILE A 1 214 ? 16.908 29.285 3.570   1.00 14.92 ? 214 ILE A CG1 1 
ATOM   1645 C  CG2 . ILE A 1 214 ? 15.304 29.545 1.643   1.00 13.95 ? 214 ILE A CG2 1 
ATOM   1646 C  CD1 . ILE A 1 214 ? 18.030 28.769 2.709   1.00 18.76 ? 214 ILE A CD1 1 
ATOM   1647 N  N   . SER A 1 215 ? 12.222 29.475 3.000   1.00 11.32 ? 215 SER A N   1 
ATOM   1648 C  CA  . SER A 1 215 ? 10.831 29.049 2.789   1.00 12.48 ? 215 SER A CA  1 
ATOM   1649 C  C   . SER A 1 215 ? 10.290 29.575 1.475   1.00 12.87 ? 215 SER A C   1 
ATOM   1650 O  O   . SER A 1 215 ? 10.814 30.527 0.919   1.00 12.30 ? 215 SER A O   1 
ATOM   1651 C  CB  . SER A 1 215 ? 9.977  29.484 3.950   1.00 14.02 ? 215 SER A CB  1 
ATOM   1652 O  OG  . SER A 1 215 ? 9.716  30.905 3.885   1.00 17.64 ? 215 SER A OG  1 
ATOM   1653 N  N   . ASN A 1 216 ? 9.162  28.998 1.053   1.00 14.43 ? 216 ASN A N   1 
ATOM   1654 C  CA  . ASN A 1 216 ? 8.324  29.694 0.050   1.00 15.05 ? 216 ASN A CA  1 
ATOM   1655 C  C   . ASN A 1 216 ? 8.060  31.136 0.520   1.00 14.59 ? 216 ASN A C   1 
ATOM   1656 O  O   . ASN A 1 216 ? 7.978  31.405 1.725   1.00 15.43 ? 216 ASN A O   1 
ATOM   1657 C  CB  . ASN A 1 216 ? 7.066  28.886 -0.202  1.00 16.31 ? 216 ASN A CB  1 
ATOM   1658 C  CG  . ASN A 1 216 ? 6.361  28.459 1.055   1.00 18.85 ? 216 ASN A CG  1 
ATOM   1659 O  OD1 . ASN A 1 216 ? 6.899  27.669 1.828   1.00 19.12 ? 216 ASN A OD1 1 
ATOM   1660 N  ND2 . ASN A 1 216 ? 5.153  28.985 1.254   1.00 18.58 ? 216 ASN A ND2 1 
ATOM   1661 N  N   . ILE A 1 217 ? 7.865  32.096 -0.405  1.00 13.42 ? 217 ILE A N   1 
ATOM   1662 C  CA  . ILE A 1 217 ? 7.872  33.544 -0.068  1.00 14.78 ? 217 ILE A CA  1 
ATOM   1663 C  C   . ILE A 1 217 ? 6.681  33.866 0.836   1.00 14.27 ? 217 ILE A C   1 
ATOM   1664 O  O   . ILE A 1 217 ? 6.826  34.795 1.664   1.00 16.03 ? 217 ILE A O   1 
ATOM   1665 C  CB  . ILE A 1 217 ? 7.889  34.398 -1.354  1.00 16.38 ? 217 ILE A CB  1 
ATOM   1666 C  CG1 . ILE A 1 217 ? 6.686  34.087 -2.244  1.00 18.43 ? 217 ILE A CG1 1 
ATOM   1667 C  CG2 . ILE A 1 217 ? 9.196  34.223 -2.088  1.00 16.90 ? 217 ILE A CG2 1 
ATOM   1668 C  CD1 . ILE A 1 217 ? 6.530  35.060 -3.421  1.00 21.12 ? 217 ILE A CD1 1 
ATOM   1669 N  N   . ASP A 1 218 ? 5.593  33.090 0.736   1.00 16.05 ? 218 ASP A N   1 
ATOM   1670 C  CA  . ASP A 1 218 ? 4.330  33.375 1.461   1.00 18.28 ? 218 ASP A CA  1 
ATOM   1671 C  C   . ASP A 1 218 ? 4.242  32.571 2.768   1.00 18.67 ? 218 ASP A C   1 
ATOM   1672 O  O   . ASP A 1 218 ? 3.155  32.527 3.365   1.00 19.79 ? 218 ASP A O   1 
ATOM   1673 C  CB  . ASP A 1 218 ? 3.134  33.127 0.541   1.00 22.03 ? 218 ASP A CB  1 
ATOM   1674 C  CG  . ASP A 1 218 ? 3.092  31.738 -0.082  1.00 26.41 ? 218 ASP A CG  1 
ATOM   1675 O  OD1 . ASP A 1 218 ? 4.155  31.151 -0.412  1.00 26.43 ? 218 ASP A OD1 1 
ATOM   1676 O  OD2 . ASP A 1 218 ? 1.981  31.262 -0.313  1.00 35.53 ? 218 ASP A OD2 1 
ATOM   1677 N  N   . SER A 1 219 ? 5.344  32.009 3.261   1.00 17.08 ? 219 SER A N   1 
ATOM   1678 C  CA  . SER A 1 219 ? 5.368  31.196 4.500   1.00 16.20 ? 219 SER A CA  1 
ATOM   1679 C  C   . SER A 1 219 ? 4.767  31.967 5.688   1.00 18.08 ? 219 SER A C   1 
ATOM   1680 O  O   . SER A 1 219 ? 5.071  33.158 5.887   1.00 17.28 ? 219 SER A O   1 
ATOM   1681 C  CB  . SER A 1 219 ? 6.792  30.784 4.772   1.00 17.39 ? 219 SER A CB  1 
ATOM   1682 O  OG  . SER A 1 219 ? 6.900  29.955 5.937   1.00 19.96 ? 219 SER A OG  1 
ATOM   1683 N  N   . SER A 1 220 ? 3.964  31.275 6.494   1.00 16.80 ? 220 SER A N   1 
ATOM   1684 C  CA  . SER A 1 220 ? 3.432  31.778 7.772   1.00 16.41 ? 220 SER A CA  1 
ATOM   1685 C  C   . SER A 1 220 ? 3.607  30.704 8.850   1.00 14.46 ? 220 SER A C   1 
ATOM   1686 O  O   . SER A 1 220 ? 3.888  29.539 8.532   1.00 14.66 ? 220 SER A O   1 
ATOM   1687 C  CB  . SER A 1 220 ? 1.971  32.155 7.650   1.00 18.51 ? 220 SER A CB  1 
ATOM   1688 O  OG  . SER A 1 220 ? 1.250  31.059 7.142   1.00 22.33 ? 220 SER A OG  1 
ATOM   1689 N  N   . ILE A 1 221 ? 3.513  31.120 10.100  1.00 14.32 ? 221 ILE A N   1 
ATOM   1690 C  CA  . ILE A 1 221 ? 3.680  30.193 11.249  1.00 14.81 ? 221 ILE A CA  1 
ATOM   1691 C  C   . ILE A 1 221 ? 2.585  29.140 11.156  1.00 15.03 ? 221 ILE A C   1 
ATOM   1692 O  O   . ILE A 1 221 ? 1.392  29.497 11.130  1.00 17.14 ? 221 ILE A O   1 
ATOM   1693 C  CB  . ILE A 1 221 ? 3.624  30.955 12.578  1.00 15.16 ? 221 ILE A CB  1 
ATOM   1694 C  CG1 . ILE A 1 221 ? 4.800  31.928 12.714  1.00 14.63 ? 221 ILE A CG1 1 
ATOM   1695 C  CG2 . ILE A 1 221 ? 3.589  29.970 13.756  1.00 14.42 ? 221 ILE A CG2 1 
ATOM   1696 C  CD1 . ILE A 1 221 ? 4.713  32.857 13.877  1.00 14.71 ? 221 ILE A CD1 1 
ATOM   1697 N  N   . PRO A 1 222 ? 2.917  27.836 11.112  1.00 15.56 ? 222 PRO A N   1 
ATOM   1698 C  CA  . PRO A 1 222 ? 1.892  26.789 11.144  1.00 16.61 ? 222 PRO A CA  1 
ATOM   1699 C  C   . PRO A 1 222 ? 1.140  26.768 12.481  1.00 19.00 ? 222 PRO A C   1 
ATOM   1700 O  O   . PRO A 1 222 ? 1.696  26.943 13.526  1.00 17.12 ? 222 PRO A O   1 
ATOM   1701 C  CB  . PRO A 1 222 ? 2.629  25.468 10.922  1.00 17.31 ? 222 PRO A CB  1 
ATOM   1702 C  CG  . PRO A 1 222 ? 4.007  25.887 10.396  1.00 17.88 ? 222 PRO A CG  1 
ATOM   1703 C  CD  . PRO A 1 222 ? 4.256  27.262 10.934  1.00 15.61 ? 222 PRO A CD  1 
ATOM   1704 N  N   . SER A 1 223 ? -0.143 26.481 12.391  1.00 20.32 ? 223 SER A N   1 
ATOM   1705 C  CA  . SER A 1 223 ? -1.008 26.295 13.566  1.00 22.19 ? 223 SER A CA  1 
ATOM   1706 C  C   . SER A 1 223 ? -0.381 25.249 14.495  1.00 19.48 ? 223 SER A C   1 
ATOM   1707 O  O   . SER A 1 223 ? 0.055  24.229 14.007  1.00 20.66 ? 223 SER A O   1 
ATOM   1708 C  CB  . SER A 1 223 ? -2.407 25.906 13.066  1.00 26.51 ? 223 SER A CB  1 
ATOM   1709 O  OG  . SER A 1 223 ? -3.219 25.576 14.161  1.00 34.90 ? 223 SER A OG  1 
ATOM   1710 N  N   . GLY A 1 224 ? -0.263 25.546 15.787  1.00 19.65 ? 224 GLY A N   1 
ATOM   1711 C  CA  . GLY A 1 224 ? 0.184  24.576 16.804  1.00 18.82 ? 224 GLY A CA  1 
ATOM   1712 C  C   . GLY A 1 224 ? 1.679  24.305 16.779  1.00 17.82 ? 224 GLY A C   1 
ATOM   1713 O  O   . GLY A 1 224 ? 2.076  23.239 17.309  1.00 20.58 ? 224 GLY A O   1 
ATOM   1714 N  N   . SER A 1 225 ? 2.505  25.228 16.268  1.00 16.63 ? 225 SER A N   1 
ATOM   1715 C  CA  . SER A 1 225 ? 3.957  25.003 16.061  1.00 14.71 ? 225 SER A CA  1 
ATOM   1716 C  C   . SER A 1 225 ? 4.750  25.684 17.171  1.00 15.14 ? 225 SER A C   1 
ATOM   1717 O  O   . SER A 1 225 ? 5.983  25.878 17.011  1.00 14.79 ? 225 SER A O   1 
ATOM   1718 C  CB  . SER A 1 225 ? 4.407  25.510 14.711  1.00 14.57 ? 225 SER A CB  1 
ATOM   1719 O  OG  . SER A 1 225 ? 4.173  26.897 14.612  1.00 15.42 ? 225 SER A OG  1 
ATOM   1720 N  N   . THR A 1 226 ? 4.142  25.892 18.325  1.00 14.67 ? 226 THR A N   1 
ATOM   1721 C  CA  . THR A 1 226 ? 4.855  26.203 19.560  1.00 14.52 ? 226 THR A CA  1 
ATOM   1722 C  C   . THR A 1 226 ? 5.737  25.011 19.947  1.00 13.14 ? 226 THR A C   1 
ATOM   1723 O  O   . THR A 1 226 ? 5.653  23.931 19.337  1.00 15.08 ? 226 THR A O   1 
ATOM   1724 C  CB  . THR A 1 226 ? 3.916  26.569 20.715  1.00 17.08 ? 226 THR A CB  1 
ATOM   1725 O  OG1 . THR A 1 226 ? 2.892  25.578 20.766  1.00 16.30 ? 226 THR A OG1 1 
ATOM   1726 C  CG2 . THR A 1 226 ? 3.330  27.951 20.539  1.00 17.35 ? 226 THR A CG2 1 
ATOM   1727 N  N   . GLY A 1 227 ? 6.624  25.221 20.932  1.00 13.93 ? 227 GLY A N   1 
ATOM   1728 C  CA  . GLY A 1 227 ? 7.369  24.129 21.546  1.00 13.35 ? 227 GLY A CA  1 
ATOM   1729 C  C   . GLY A 1 227 ? 8.289  23.409 20.554  1.00 12.24 ? 227 GLY A C   1 
ATOM   1730 O  O   . GLY A 1 227 ? 9.066  24.073 19.895  1.00 12.04 ? 227 GLY A O   1 
ATOM   1731 N  N   . ARG A 1 228 ? 8.231  22.094 20.493  1.00 12.34 ? 228 ARG A N   1 
ATOM   1732 C  CA  . ARG A 1 228 ? 9.253  21.295 19.792  1.00 12.17 ? 228 ARG A CA  1 
ATOM   1733 C  C   . ARG A 1 228 ? 9.241  21.584 18.273  1.00 12.14 ? 228 ARG A C   1 
ATOM   1734 O  O   . ARG A 1 228 ? 10.181 21.172 17.597  1.00 13.63 ? 228 ARG A O   1 
ATOM   1735 C  CB  . ARG A 1 228 ? 9.039  19.813 20.091  1.00 13.29 ? 228 ARG A CB  1 
ATOM   1736 C  CG  . ARG A 1 228 ? 7.730  19.284 19.506  1.00 14.14 ? 228 ARG A CG  1 
ATOM   1737 C  CD  . ARG A 1 228 ? 7.446  17.831 19.841  1.00 14.90 ? 228 ARG A CD  1 
ATOM   1738 N  NE  . ARG A 1 228 ? 7.237  17.699 21.286  1.00 15.22 ? 228 ARG A NE  1 
ATOM   1739 C  CZ  . ARG A 1 228 ? 7.332  16.550 21.933  1.00 16.92 ? 228 ARG A CZ  1 
ATOM   1740 N  NH1 . ARG A 1 228 ? 7.192  16.527 23.246  1.00 20.47 ? 228 ARG A NH1 1 
ATOM   1741 N  NH2 . ARG A 1 228 ? 7.582  15.438 21.276  1.00 18.54 ? 228 ARG A NH2 1 
ATOM   1742 N  N   . LEU A 1 229 ? 8.194  22.200 17.745  1.00 10.31 ? 229 LEU A N   1 
ATOM   1743 C  CA  . LEU A 1 229 ? 8.057  22.383 16.264  1.00 11.55 ? 229 LEU A CA  1 
ATOM   1744 C  C   . LEU A 1 229 ? 8.681  23.697 15.811  1.00 11.45 ? 229 LEU A C   1 
ATOM   1745 O  O   . LEU A 1 229 ? 8.732  23.880 14.577  1.00 13.47 ? 229 LEU A O   1 
ATOM   1746 C  CB  . LEU A 1 229 ? 6.581  22.263 15.891  1.00 13.04 ? 229 LEU A CB  1 
ATOM   1747 C  CG  . LEU A 1 229 ? 5.990  20.878 16.211  1.00 13.72 ? 229 LEU A CG  1 
ATOM   1748 C  CD1 . LEU A 1 229 ? 4.531  20.872 15.808  1.00 14.54 ? 229 LEU A CD1 1 
ATOM   1749 C  CD2 . LEU A 1 229 ? 6.780  19.732 15.542  1.00 13.96 ? 229 LEU A CD2 1 
ATOM   1750 N  N   . LEU A 1 230 ? 9.185  24.531 16.737  1.00 11.23 ? 230 LEU A N   1 
ATOM   1751 C  CA  . LEU A 1 230 ? 10.134 25.649 16.472  1.00 12.27 ? 230 LEU A CA  1 
ATOM   1752 C  C   . LEU A 1 230 ? 9.525  26.727 15.573  1.00 12.73 ? 230 LEU A C   1 
ATOM   1753 O  O   . LEU A 1 230 ? 10.290 27.536 14.997  1.00 13.07 ? 230 LEU A O   1 
ATOM   1754 C  CB  . LEU A 1 230 ? 11.414 25.097 15.840  1.00 13.69 ? 230 LEU A CB  1 
ATOM   1755 C  CG  . LEU A 1 230 ? 12.250 24.168 16.715  1.00 17.27 ? 230 LEU A CG  1 
ATOM   1756 C  CD1 . LEU A 1 230 ? 13.443 23.645 15.914  1.00 17.59 ? 230 LEU A CD1 1 
ATOM   1757 C  CD2 . LEU A 1 230 ? 12.755 24.885 17.962  1.00 18.56 ? 230 LEU A CD2 1 
ATOM   1758 N  N   . GLY A 1 231 ? 8.202  26.808 15.464  1.00 11.98 ? 231 GLY A N   1 
ATOM   1759 C  CA  . GLY A 1 231 ? 7.567  27.781 14.574  1.00 12.64 ? 231 GLY A CA  1 
ATOM   1760 C  C   . GLY A 1 231 ? 7.676  27.435 13.112  1.00 12.57 ? 231 GLY A C   1 
ATOM   1761 O  O   . GLY A 1 231 ? 7.289  28.314 12.320  1.00 13.40 ? 231 GLY A O   1 
ATOM   1762 N  N   . LEU A 1 232 ? 8.163  26.249 12.751  1.00 13.26 ? 232 LEU A N   1 
ATOM   1763 C  CA  . LEU A 1 232 ? 8.509  25.884 11.350  1.00 13.77 ? 232 LEU A CA  1 
ATOM   1764 C  C   . LEU A 1 232 ? 7.576  24.822 10.788  1.00 14.18 ? 232 LEU A C   1 
ATOM   1765 O  O   . LEU A 1 232 ? 7.309  24.871 9.573   1.00 15.13 ? 232 LEU A O   1 
ATOM   1766 C  CB  . LEU A 1 232 ? 9.929  25.330 11.290  1.00 14.41 ? 232 LEU A CB  1 
ATOM   1767 C  CG  . LEU A 1 232 ? 11.049 26.295 11.686  1.00 16.31 ? 232 LEU A CG  1 
ATOM   1768 C  CD1 . LEU A 1 232 ? 12.365 25.570 11.622  1.00 18.04 ? 232 LEU A CD1 1 
ATOM   1769 C  CD2 . LEU A 1 232 ? 11.065 27.491 10.798  1.00 17.56 ? 232 LEU A CD2 1 
ATOM   1770 N  N   . PHE A 1 233 ? 7.112  23.863 11.602  1.00 14.07 ? 233 PHE A N   1 
ATOM   1771 C  CA  . PHE A 1 233 ? 6.448  22.654 11.043  1.00 15.47 ? 233 PHE A CA  1 
ATOM   1772 C  C   . PHE A 1 233 ? 5.074  22.503 11.669  1.00 14.39 ? 233 PHE A C   1 
ATOM   1773 O  O   . PHE A 1 233 ? 4.931  22.846 12.820  1.00 14.00 ? 233 PHE A O   1 
ATOM   1774 C  CB  . PHE A 1 233 ? 7.347  21.441 11.291  1.00 16.49 ? 233 PHE A CB  1 
ATOM   1775 C  CG  . PHE A 1 233 ? 8.664  21.530 10.567  1.00 17.17 ? 233 PHE A CG  1 
ATOM   1776 C  CD1 . PHE A 1 233 ? 8.685  21.414 9.182   1.00 20.15 ? 233 PHE A CD1 1 
ATOM   1777 C  CD2 . PHE A 1 233 ? 9.835  21.821 11.238  1.00 18.75 ? 233 PHE A CD2 1 
ATOM   1778 C  CE1 . PHE A 1 233 ? 9.878  21.466 8.480   1.00 18.05 ? 233 PHE A CE1 1 
ATOM   1779 C  CE2 . PHE A 1 233 ? 11.024 21.910 10.526  1.00 18.86 ? 233 PHE A CE2 1 
ATOM   1780 C  CZ  . PHE A 1 233 ? 11.029 21.763 9.152   1.00 18.55 ? 233 PHE A CZ  1 
ATOM   1781 N  N   . PRO A 1 234 ? 4.058  22.020 10.924  1.00 18.45 ? 234 PRO A N   1 
ATOM   1782 C  CA  . PRO A 1 234 ? 2.712  21.788 11.473  1.00 18.71 ? 234 PRO A CA  1 
ATOM   1783 C  C   . PRO A 1 234 ? 2.614  20.499 12.303  1.00 19.06 ? 234 PRO A C   1 
ATOM   1784 O  O   . PRO A 1 234 ? 1.647  20.320 13.011  1.00 21.48 ? 234 PRO A O   1 
ATOM   1785 C  CB  . PRO A 1 234 ? 1.857  21.646 10.210  1.00 19.21 ? 234 PRO A CB  1 
ATOM   1786 C  CG  . PRO A 1 234 ? 2.785  21.077 9.168   1.00 19.62 ? 234 PRO A CG  1 
ATOM   1787 C  CD  . PRO A 1 234 ? 4.166  21.641 9.507   1.00 20.29 ? 234 PRO A CD  1 
ATOM   1788 N  N   . ASP A 1 235 ? 3.583  19.605 12.163  1.00 19.30 ? 235 ASP A N   1 
ATOM   1789 C  CA  . ASP A 1 235 ? 3.584  18.323 12.892  1.00 20.97 ? 235 ASP A CA  1 
ATOM   1790 C  C   . ASP A 1 235 ? 5.006  17.758 12.913  1.00 22.04 ? 235 ASP A C   1 
ATOM   1791 O  O   . ASP A 1 235 ? 5.920  18.404 12.360  1.00 19.01 ? 235 ASP A O   1 
ATOM   1792 C  CB  . ASP A 1 235 ? 2.561  17.369 12.271  1.00 21.17 ? 235 ASP A CB  1 
ATOM   1793 C  CG  . ASP A 1 235 ? 2.888  17.073 10.828  1.00 24.44 ? 235 ASP A CG  1 
ATOM   1794 O  OD1 . ASP A 1 235 ? 4.081  16.770 10.546  1.00 27.51 ? 235 ASP A OD1 1 
ATOM   1795 O  OD2 . ASP A 1 235 ? 1.993  17.249 9.988   1.00 27.47 ? 235 ASP A OD2 1 
ATOM   1796 N  N   . ALA A 1 236 ? 5.194  16.609 13.568  1.00 19.06 ? 236 ALA A N   1 
ATOM   1797 C  CA  . ALA A 1 236 ? 6.525  16.003 13.816  1.00 21.55 ? 236 ALA A CA  1 
ATOM   1798 C  C   . ALA A 1 236 ? 6.804  14.875 12.815  1.00 23.12 ? 236 ALA A C   1 
ATOM   1799 O  O   . ALA A 1 236 ? 7.648  14.032 13.134  1.00 30.03 ? 236 ALA A O   1 
ATOM   1800 C  CB  . ALA A 1 236 ? 6.617  15.527 15.250  1.00 21.89 ? 236 ALA A CB  1 
ATOM   1801 N  N   . ASN A 1 237 ? 6.150  14.856 11.651  1.00 26.42 ? 237 ASN A N   1 
ATOM   1802 C  CA  . ASN A 1 237 ? 6.397  13.817 10.608  1.00 29.92 ? 237 ASN A CA  1 
ATOM   1803 C  C   . ASN A 1 237 ? 7.816  14.009 10.037  1.00 33.15 ? 237 ASN A C   1 
ATOM   1804 O  O   . ASN A 1 237 ? 8.342  15.131 9.900   1.00 27.57 ? 237 ASN A O   1 
ATOM   1805 C  CB  . ASN A 1 237 ? 5.345  13.822 9.503   1.00 32.17 ? 237 ASN A CB  1 
ATOM   1806 C  CG  . ASN A 1 237 ? 3.953  13.510 10.006  1.00 36.15 ? 237 ASN A CG  1 
ATOM   1807 O  OD1 . ASN A 1 237 ? 2.981  13.753 9.306   1.00 44.88 ? 237 ASN A OD1 1 
ATOM   1808 N  ND2 . ASN A 1 237 ? 3.845  13.012 11.225  1.00 35.66 ? 237 ASN A ND2 1 
ATOM   1809 O  OXT . ASN A 1 237 ? 8.495  13.011 9.729   1.00 34.76 ? 237 ASN A OXT 1 
HETATM 1810 C  C1  . GOL B 2 .   ? 20.109 50.411 5.995   1.00 23.19 ? 401 GOL A C1  1 
HETATM 1811 O  O1  . GOL B 2 .   ? 20.447 51.487 5.110   1.00 21.22 ? 401 GOL A O1  1 
HETATM 1812 C  C2  . GOL B 2 .   ? 19.289 49.298 5.352   1.00 23.30 ? 401 GOL A C2  1 
HETATM 1813 O  O2  . GOL B 2 .   ? 18.017 49.771 4.886   1.00 17.74 ? 401 GOL A O2  1 
HETATM 1814 C  C3  . GOL B 2 .   ? 19.099 48.101 6.277   1.00 25.10 ? 401 GOL A C3  1 
HETATM 1815 O  O3  . GOL B 2 .   ? 18.045 48.267 7.244   1.00 25.33 ? 401 GOL A O3  1 
HETATM 1816 MN MN  . MN  C 3 .   ? 16.155 18.724 17.107  1.00 10.45 ? 402 MN  A MN  1 
HETATM 1817 CA CA  . CA  D 4 .   ? 13.827 19.689 20.412  1.00 11.01 ? 403 CA  A CA  1 
HETATM 1818 O  O   . HOH E 5 .   ? 30.797 32.973 -19.145 1.00 25.64 ? 501 HOH A O   1 
HETATM 1819 O  O   . HOH E 5 .   ? 11.877 30.415 -14.078 1.00 28.99 ? 502 HOH A O   1 
HETATM 1820 O  O   . HOH E 5 .   ? 20.934 17.156 -7.938  1.00 26.98 ? 503 HOH A O   1 
HETATM 1821 O  O   . HOH E 5 .   ? 33.587 24.750 -2.220  1.00 25.04 ? 504 HOH A O   1 
HETATM 1822 O  O   . HOH E 5 .   ? 29.536 18.721 18.342  1.00 25.87 ? 505 HOH A O   1 
HETATM 1823 O  O   . HOH E 5 .   ? 27.736 23.758 -0.496  1.00 20.67 ? 506 HOH A O   1 
HETATM 1824 O  O   . HOH E 5 .   ? 30.425 26.307 21.733  1.00 31.08 ? 507 HOH A O   1 
HETATM 1825 O  O   . HOH E 5 .   ? 27.465 44.816 5.292   1.00 29.35 ? 508 HOH A O   1 
HETATM 1826 O  O   . HOH E 5 .   ? 30.298 33.199 -15.117 1.00 25.92 ? 509 HOH A O   1 
HETATM 1827 O  O   . HOH E 5 .   ? 11.040 34.278 25.035  1.00 20.71 ? 510 HOH A O   1 
HETATM 1828 O  O   . HOH E 5 .   ? 3.375  39.787 9.608   1.00 30.20 ? 511 HOH A O   1 
HETATM 1829 O  O   . HOH E 5 .   ? 5.748  24.325 7.569   1.00 22.85 ? 512 HOH A O   1 
HETATM 1830 O  O   . HOH E 5 .   ? 12.118 26.226 31.114  1.00 18.78 ? 513 HOH A O   1 
HETATM 1831 O  O   . HOH E 5 .   ? 10.828 12.618 8.652   1.00 27.41 ? 514 HOH A O   1 
HETATM 1832 O  O   . HOH E 5 .   ? 35.422 27.836 18.613  1.00 26.39 ? 515 HOH A O   1 
HETATM 1833 O  O   . HOH E 5 .   ? 30.426 30.629 15.189  1.00 36.59 ? 516 HOH A O   1 
HETATM 1834 O  O   . HOH E 5 .   ? 16.773 17.300 15.635  1.00 13.39 ? 517 HOH A O   1 
HETATM 1835 O  O   . HOH E 5 .   ? 9.554  20.588 23.785  1.00 20.61 ? 518 HOH A O   1 
HETATM 1836 O  O   . HOH E 5 .   ? 21.213 24.666 -5.339  1.00 22.61 ? 519 HOH A O   1 
HETATM 1837 O  O   . HOH E 5 .   ? 19.022 30.015 -19.343 1.00 23.61 ? 520 HOH A O   1 
HETATM 1838 O  O   . HOH E 5 .   ? 2.278  27.027 1.715   1.00 31.45 ? 521 HOH A O   1 
HETATM 1839 O  O   . HOH E 5 .   ? 30.206 20.104 9.382   1.00 20.88 ? 522 HOH A O   1 
HETATM 1840 O  O   . HOH E 5 .   ? 8.007  17.796 10.830  1.00 17.91 ? 523 HOH A O   1 
HETATM 1841 O  O   . HOH E 5 .   ? 27.537 25.081 -12.963 1.00 28.88 ? 524 HOH A O   1 
HETATM 1842 O  O   . HOH E 5 .   ? 6.119  22.206 5.993   1.00 27.95 ? 525 HOH A O   1 
HETATM 1843 O  O   . HOH E 5 .   ? 16.274 42.699 24.044  1.00 30.63 ? 526 HOH A O   1 
HETATM 1844 O  O   . HOH E 5 .   ? 3.895  21.930 19.207  1.00 21.91 ? 527 HOH A O   1 
HETATM 1845 O  O   . HOH E 5 .   ? 16.619 47.681 3.802   1.00 17.01 ? 528 HOH A O   1 
HETATM 1846 O  O   . HOH E 5 .   ? 9.913  20.344 -2.108  1.00 21.35 ? 529 HOH A O   1 
HETATM 1847 O  O   . HOH E 5 .   ? 8.740  39.396 21.315  1.00 17.91 ? 530 HOH A O   1 
HETATM 1848 O  O   . HOH E 5 .   ? 14.563 30.576 -17.982 1.00 29.75 ? 531 HOH A O   1 
HETATM 1849 O  O   . HOH E 5 .   ? 9.681  54.306 22.516  1.00 25.64 ? 532 HOH A O   1 
HETATM 1850 O  O   . HOH E 5 .   ? 32.954 29.611 26.509  1.00 26.27 ? 533 HOH A O   1 
HETATM 1851 O  O   . HOH E 5 .   ? 9.458  46.084 13.394  1.00 24.34 ? 534 HOH A O   1 
HETATM 1852 O  O   . HOH E 5 .   ? 25.350 38.624 12.684  1.00 33.81 ? 535 HOH A O   1 
HETATM 1853 O  O   . HOH E 5 .   ? 19.827 20.879 -9.594  1.00 24.07 ? 536 HOH A O   1 
HETATM 1854 O  O   . HOH E 5 .   ? 20.780 27.272 -8.067  1.00 20.61 ? 537 HOH A O   1 
HETATM 1855 O  O   . HOH E 5 .   ? 17.029 21.904 27.673  1.00 17.95 ? 538 HOH A O   1 
HETATM 1856 O  O   . HOH E 5 .   ? 24.729 16.959 -2.542  1.00 28.93 ? 539 HOH A O   1 
HETATM 1857 O  O   . HOH E 5 .   ? 12.940 21.826 21.157  1.00 11.97 ? 540 HOH A O   1 
HETATM 1858 O  O   . HOH E 5 .   ? 5.989  35.213 4.381   1.00 18.89 ? 541 HOH A O   1 
HETATM 1859 O  O   . HOH E 5 .   ? 31.351 21.648 20.403  1.00 26.26 ? 542 HOH A O   1 
HETATM 1860 O  O   . HOH E 5 .   ? 12.031 15.251 4.457   1.00 27.22 ? 543 HOH A O   1 
HETATM 1861 O  O   . HOH E 5 .   ? 22.400 13.309 1.484   1.00 23.83 ? 544 HOH A O   1 
HETATM 1862 O  O   . HOH E 5 .   ? 17.802 49.620 9.593   1.00 20.87 ? 545 HOH A O   1 
HETATM 1863 O  O   . HOH E 5 .   ? 14.251 18.964 16.117  1.00 12.89 ? 546 HOH A O   1 
HETATM 1864 O  O   . HOH E 5 .   ? 8.184  31.015 -3.142  1.00 15.64 ? 547 HOH A O   1 
HETATM 1865 O  O   . HOH E 5 .   ? 13.375 13.434 8.507   1.00 21.55 ? 548 HOH A O   1 
HETATM 1866 O  O   . HOH E 5 .   ? 21.381 27.020 -13.522 1.00 27.88 ? 549 HOH A O   1 
HETATM 1867 O  O   . HOH E 5 .   ? 14.703 17.107 8.420   1.00 13.85 ? 550 HOH A O   1 
HETATM 1868 O  O   . HOH E 5 .   ? 3.715  23.339 22.110  1.00 24.29 ? 551 HOH A O   1 
HETATM 1869 O  O   . HOH E 5 .   ? 29.438 34.786 19.882  1.00 18.80 ? 552 HOH A O   1 
HETATM 1870 O  O   . HOH E 5 .   ? 23.326 27.175 -9.730  1.00 33.20 ? 553 HOH A O   1 
HETATM 1871 O  O   . HOH E 5 .   ? 35.738 26.284 26.755  1.00 17.87 ? 554 HOH A O   1 
HETATM 1872 O  O   . HOH E 5 .   ? 30.045 25.864 24.347  1.00 15.78 ? 555 HOH A O   1 
HETATM 1873 O  O   . HOH E 5 .   ? 5.015  39.877 15.289  1.00 24.68 ? 556 HOH A O   1 
HETATM 1874 O  O   . HOH E 5 .   ? 8.857  23.262 25.805  1.00 19.73 ? 557 HOH A O   1 
HETATM 1875 O  O   . HOH E 5 .   ? 12.911 36.338 22.774  1.00 15.09 ? 558 HOH A O   1 
HETATM 1876 O  O   . HOH E 5 .   ? 5.994  22.095 25.786  1.00 31.91 ? 559 HOH A O   1 
HETATM 1877 O  O   . HOH E 5 .   ? 12.770 43.798 20.743  1.00 31.01 ? 560 HOH A O   1 
HETATM 1878 O  O   . HOH E 5 .   ? 15.342 11.409 4.755   1.00 34.96 ? 561 HOH A O   1 
HETATM 1879 O  O   . HOH E 5 .   ? 17.222 20.464 -10.073 1.00 19.74 ? 562 HOH A O   1 
HETATM 1880 O  O   . HOH E 5 .   ? 19.671 15.252 0.070   1.00 27.13 ? 563 HOH A O   1 
HETATM 1881 O  O   . HOH E 5 .   ? 25.192 19.323 24.738  1.00 22.69 ? 564 HOH A O   1 
HETATM 1882 O  O   . HOH E 5 .   ? 21.546 44.561 18.731  1.00 19.80 ? 565 HOH A O   1 
HETATM 1883 O  O   . HOH E 5 .   ? 24.171 14.410 17.253  1.00 25.11 ? 566 HOH A O   1 
HETATM 1884 O  O   . HOH E 5 .   ? 0.155  26.103 20.450  1.00 28.13 ? 567 HOH A O   1 
HETATM 1885 O  O   . HOH E 5 .   ? 29.682 26.916 0.362   1.00 25.58 ? 568 HOH A O   1 
HETATM 1886 O  O   . HOH E 5 .   ? 36.122 24.022 17.791  1.00 27.91 ? 569 HOH A O   1 
HETATM 1887 O  O   . HOH E 5 .   ? 16.033 13.255 13.333  1.00 27.86 ? 570 HOH A O   1 
HETATM 1888 O  O   . HOH E 5 .   ? 25.321 14.405 3.979   1.00 20.00 ? 571 HOH A O   1 
HETATM 1889 O  O   . HOH E 5 .   ? 5.614  18.573 8.982   1.00 27.81 ? 572 HOH A O   1 
HETATM 1890 O  O   . HOH E 5 .   ? 19.926 26.001 31.931  1.00 29.19 ? 573 HOH A O   1 
HETATM 1891 O  O   . HOH E 5 .   ? 1.071  18.886 15.393  1.00 30.63 ? 574 HOH A O   1 
HETATM 1892 O  O   . HOH E 5 .   ? 4.867  39.535 21.607  1.00 33.02 ? 575 HOH A O   1 
HETATM 1893 O  O   . HOH E 5 .   ? 12.581 19.807 18.319  1.00 12.73 ? 576 HOH A O   1 
HETATM 1894 O  O   . HOH E 5 .   ? 0.349  20.967 17.222  1.00 26.18 ? 577 HOH A O   1 
HETATM 1895 O  O   . HOH E 5 .   ? 29.209 23.072 21.229  1.00 16.38 ? 578 HOH A O   1 
HETATM 1896 O  O   . HOH E 5 .   ? 5.008  31.699 30.794  1.00 28.58 ? 579 HOH A O   1 
HETATM 1897 O  O   . HOH E 5 .   ? 6.384  27.546 8.011   1.00 21.65 ? 580 HOH A O   1 
HETATM 1898 O  O   . HOH E 5 .   ? 10.316 27.472 -8.548  1.00 24.45 ? 581 HOH A O   1 
HETATM 1899 O  O   . HOH E 5 .   ? 22.928 36.375 -12.482 1.00 29.31 ? 582 HOH A O   1 
HETATM 1900 O  O   . HOH E 5 .   ? 2.532  33.790 10.573  1.00 17.71 ? 583 HOH A O   1 
HETATM 1901 O  O   . HOH E 5 .   ? 8.207  45.064 10.821  1.00 23.06 ? 584 HOH A O   1 
HETATM 1902 O  O   . HOH E 5 .   ? 23.987 26.196 29.770  1.00 27.61 ? 585 HOH A O   1 
HETATM 1903 O  O   . HOH E 5 .   ? 8.540  21.698 4.762   1.00 19.69 ? 586 HOH A O   1 
HETATM 1904 O  O   . HOH E 5 .   ? 28.669 25.990 20.179  1.00 27.92 ? 587 HOH A O   1 
HETATM 1905 O  O   . HOH E 5 .   ? 23.423 13.019 12.577  1.00 23.35 ? 588 HOH A O   1 
HETATM 1906 O  O   . HOH E 5 .   ? 6.230  43.230 10.374  1.00 23.86 ? 589 HOH A O   1 
HETATM 1907 O  O   . HOH E 5 .   ? 32.253 22.091 23.046  1.00 28.82 ? 590 HOH A O   1 
HETATM 1908 O  O   . HOH E 5 .   ? 27.635 16.708 10.040  1.00 19.63 ? 591 HOH A O   1 
HETATM 1909 O  O   . HOH E 5 .   ? 2.078  27.531 7.399   1.00 21.25 ? 592 HOH A O   1 
HETATM 1910 O  O   . HOH E 5 .   ? 3.055  25.046 6.792   1.00 22.13 ? 593 HOH A O   1 
HETATM 1911 O  O   . HOH E 5 .   ? 28.038 32.348 7.105   1.00 29.67 ? 594 HOH A O   1 
HETATM 1912 O  O   . HOH E 5 .   ? 30.658 19.426 15.996  1.00 16.75 ? 595 HOH A O   1 
HETATM 1913 O  O   . HOH E 5 .   ? 15.380 31.423 -14.741 1.00 27.73 ? 596 HOH A O   1 
HETATM 1914 O  O   . HOH E 5 .   ? 3.212  37.657 7.515   1.00 20.73 ? 597 HOH A O   1 
HETATM 1915 O  O   . HOH E 5 .   ? 7.919  45.176 17.163  1.00 22.86 ? 598 HOH A O   1 
HETATM 1916 O  O   . HOH E 5 .   ? 19.303 16.330 -2.478  1.00 27.31 ? 599 HOH A O   1 
HETATM 1917 O  O   . HOH E 5 .   ? 14.421 25.132 -8.195  1.00 25.14 ? 600 HOH A O   1 
HETATM 1918 O  O   . HOH E 5 .   ? 8.542  40.260 23.866  1.00 20.30 ? 601 HOH A O   1 
HETATM 1919 O  O   . HOH E 5 .   ? 34.861 24.504 24.895  1.00 16.85 ? 602 HOH A O   1 
HETATM 1920 O  O   . HOH E 5 .   ? 30.971 32.142 26.354  1.00 30.43 ? 603 HOH A O   1 
HETATM 1921 O  O   . HOH E 5 .   ? 17.669 15.675 -4.393  1.00 29.12 ? 604 HOH A O   1 
HETATM 1922 O  O   . HOH E 5 .   ? 26.218 36.560 6.309   1.00 33.01 ? 605 HOH A O   1 
HETATM 1923 O  O   . HOH E 5 .   ? 28.317 15.390 17.874  1.00 26.32 ? 606 HOH A O   1 
HETATM 1924 O  O   . HOH E 5 .   ? 10.015 15.442 24.638  1.00 21.30 ? 607 HOH A O   1 
HETATM 1925 O  O   . HOH E 5 .   ? 1.406  36.712 12.544  1.00 31.93 ? 608 HOH A O   1 
HETATM 1926 O  O   . HOH E 5 .   ? 15.443 26.576 -6.233  1.00 19.13 ? 609 HOH A O   1 
HETATM 1927 O  O   . HOH E 5 .   ? 21.884 43.299 24.157  1.00 35.70 ? 610 HOH A O   1 
HETATM 1928 O  O   . HOH E 5 .   ? -1.113 25.125 9.585   1.00 30.77 ? 611 HOH A O   1 
HETATM 1929 O  O   . HOH E 5 .   ? 9.324  30.609 -7.235  1.00 21.79 ? 612 HOH A O   1 
HETATM 1930 O  O   . HOH E 5 .   ? 2.651  16.767 15.864  1.00 25.97 ? 613 HOH A O   1 
HETATM 1931 O  O   . HOH E 5 .   ? 10.407 42.315 24.602  1.00 29.96 ? 614 HOH A O   1 
HETATM 1932 O  O   . HOH E 5 .   ? 1.389  35.546 8.920   1.00 31.15 ? 615 HOH A O   1 
HETATM 1933 O  O   . HOH E 5 .   ? 20.666 24.647 25.354  1.00 27.14 ? 616 HOH A O   1 
HETATM 1934 O  O   . HOH E 5 .   ? 16.565 19.441 28.827  1.00 21.46 ? 617 HOH A O   1 
HETATM 1935 O  O   . HOH E 5 .   ? 8.919  31.308 -9.765  1.00 33.66 ? 618 HOH A O   1 
HETATM 1936 O  O   . HOH E 5 .   ? 32.084 23.976 24.680  1.00 24.23 ? 619 HOH A O   1 
HETATM 1937 O  O   . HOH E 5 .   ? 19.214 40.817 26.223  1.00 34.24 ? 620 HOH A O   1 
HETATM 1938 O  O   . HOH E 5 .   ? 6.492  28.928 -3.716  1.00 24.12 ? 621 HOH A O   1 
HETATM 1939 O  O   . HOH E 5 .   ? 0.822  23.987 7.469   1.00 30.97 ? 622 HOH A O   1 
# 
