data_9QFU
# 
_entry.id   9QFU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9QFU         pdb_00009qfu 10.2210/pdb9qfu/pdb 
WWPDB D_1292146294 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-26 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9QFU 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              marco.gobbi@marionegri.it 
_pdbx_contact_author.name_first         Marco 
_pdbx_contact_author.name_last          Gobbi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1014-6225 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Porta, A.'     1 ? 
'Manelfi, C.'   2 ? 
'Talarico, C.'  3 ? 
'Beccari, A.R.' 4 ? 
'Brindisi, M.'  5 ? 
'Summa, V.'     6 ? 
'Iaconis, D.'   7 ? 
'Gobbi, M.'     8 ? 
'Beeg, M.'      9 ? 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Molecules 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1420-3049 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            30 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Integrating Surface Plasmon Resonance and Docking Analysis for Mechanistic Insights of Tryptase Inhibitors.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/molecules30061338 
_citation.pdbx_database_id_PubMed   40142113 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Porta, A.'     1 ? 
primary 'Manelfi, C.'   2 ? 
primary 'Talarico, C.'  3 ? 
primary 'Beccari, A.R.' 4 ? 
primary 'Brindisi, M.'  5 ? 
primary 'Summa, V.'     6 ? 
primary 'Iaconis, D.'   7 ? 
primary 'Gobbi, M.'     8 ? 
primary 'Beeg, M.'      9 ? 
# 
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 'Tryptase beta-2' 27265.131 4   3.4.21.59 ? ? ? 
2 non-polymer syn 
;~{N}-[(1~{S},2~{S})-6-azanyl-1-[5-[[4-[2-(3,4-dichlorophenyl)ethoxy]phenyl]methyl]-1,2,4-oxadiazol-3-yl]-1-oxidanyl-hexan-2-yl]-4-fluoranyl-benzamide
;
601.496   4   ?         ? ? ? 
3 non-polymer syn 'SULFATE ION' 96.063    16  ?         ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120   2   ?         ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL 62.068    15  ?         ? ? ? 
6 non-polymer syn 'ACETATE ION' 59.044    3   ?         ? ? ? 
7 non-polymer syn GLYCEROL 92.094    1   ?         ? ? ? 
8 water       nat water 18.015    524 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Tryptase-2,Tryptase II' 
# 
_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       
;IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVH
PQFYTAQIGADIALLELEEPVKVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDA
KYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY
VPK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVH
PQFYTAQIGADIALLELEEPVKVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDA
KYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY
VPK
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;~{N}-[(1~{S},2~{S})-6-azanyl-1-[5-[[4-[2-(3,4-dichlorophenyl)ethoxy]phenyl]methyl]-1,2,4-oxadiazol-3-yl]-1-oxidanyl-hexan-2-yl]-4-fluoranyl-benzamide
;
A1I52 
3 'SULFATE ION' SO4   
4 'DI(HYDROXYETHYL)ETHER' PEG   
5 1,2-ETHANEDIOL EDO   
6 'ACETATE ION' ACT   
7 GLYCEROL GOL   
8 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   VAL n 
1 3   GLY n 
1 4   GLY n 
1 5   GLN n 
1 6   GLU n 
1 7   ALA n 
1 8   PRO n 
1 9   ARG n 
1 10  SER n 
1 11  LYS n 
1 12  TRP n 
1 13  PRO n 
1 14  TRP n 
1 15  GLN n 
1 16  VAL n 
1 17  SER n 
1 18  LEU n 
1 19  ARG n 
1 20  VAL n 
1 21  HIS n 
1 22  GLY n 
1 23  PRO n 
1 24  TYR n 
1 25  TRP n 
1 26  MET n 
1 27  HIS n 
1 28  PHE n 
1 29  CYS n 
1 30  GLY n 
1 31  GLY n 
1 32  SER n 
1 33  LEU n 
1 34  ILE n 
1 35  HIS n 
1 36  PRO n 
1 37  GLN n 
1 38  TRP n 
1 39  VAL n 
1 40  LEU n 
1 41  THR n 
1 42  ALA n 
1 43  ALA n 
1 44  HIS n 
1 45  CYS n 
1 46  VAL n 
1 47  GLY n 
1 48  PRO n 
1 49  ASP n 
1 50  VAL n 
1 51  LYS n 
1 52  ASP n 
1 53  LEU n 
1 54  ALA n 
1 55  ALA n 
1 56  LEU n 
1 57  ARG n 
1 58  VAL n 
1 59  GLN n 
1 60  LEU n 
1 61  ARG n 
1 62  GLU n 
1 63  GLN n 
1 64  HIS n 
1 65  LEU n 
1 66  TYR n 
1 67  TYR n 
1 68  GLN n 
1 69  ASP n 
1 70  GLN n 
1 71  LEU n 
1 72  LEU n 
1 73  PRO n 
1 74  VAL n 
1 75  SER n 
1 76  ARG n 
1 77  ILE n 
1 78  ILE n 
1 79  VAL n 
1 80  HIS n 
1 81  PRO n 
1 82  GLN n 
1 83  PHE n 
1 84  TYR n 
1 85  THR n 
1 86  ALA n 
1 87  GLN n 
1 88  ILE n 
1 89  GLY n 
1 90  ALA n 
1 91  ASP n 
1 92  ILE n 
1 93  ALA n 
1 94  LEU n 
1 95  LEU n 
1 96  GLU n 
1 97  LEU n 
1 98  GLU n 
1 99  GLU n 
1 100 PRO n 
1 101 VAL n 
1 102 LYS n 
1 103 VAL n 
1 104 SER n 
1 105 SER n 
1 106 HIS n 
1 107 VAL n 
1 108 HIS n 
1 109 THR n 
1 110 VAL n 
1 111 THR n 
1 112 LEU n 
1 113 PRO n 
1 114 PRO n 
1 115 ALA n 
1 116 SER n 
1 117 GLU n 
1 118 THR n 
1 119 PHE n 
1 120 PRO n 
1 121 PRO n 
1 122 GLY n 
1 123 MET n 
1 124 PRO n 
1 125 CYS n 
1 126 TRP n 
1 127 VAL n 
1 128 THR n 
1 129 GLY n 
1 130 TRP n 
1 131 GLY n 
1 132 ASP n 
1 133 VAL n 
1 134 ASP n 
1 135 ASN n 
1 136 ASP n 
1 137 GLU n 
1 138 ARG n 
1 139 LEU n 
1 140 PRO n 
1 141 PRO n 
1 142 PRO n 
1 143 PHE n 
1 144 PRO n 
1 145 LEU n 
1 146 LYS n 
1 147 GLN n 
1 148 VAL n 
1 149 LYS n 
1 150 VAL n 
1 151 PRO n 
1 152 ILE n 
1 153 MET n 
1 154 GLU n 
1 155 ASN n 
1 156 HIS n 
1 157 ILE n 
1 158 CYS n 
1 159 ASP n 
1 160 ALA n 
1 161 LYS n 
1 162 TYR n 
1 163 HIS n 
1 164 LEU n 
1 165 GLY n 
1 166 ALA n 
1 167 TYR n 
1 168 THR n 
1 169 GLY n 
1 170 ASP n 
1 171 ASP n 
1 172 VAL n 
1 173 ARG n 
1 174 ILE n 
1 175 VAL n 
1 176 ARG n 
1 177 ASP n 
1 178 ASP n 
1 179 MET n 
1 180 LEU n 
1 181 CYS n 
1 182 ALA n 
1 183 GLY n 
1 184 ASN n 
1 185 THR n 
1 186 ARG n 
1 187 ARG n 
1 188 ASP n 
1 189 SER n 
1 190 CYS n 
1 191 GLN n 
1 192 GLY n 
1 193 ASP n 
1 194 SER n 
1 195 GLY n 
1 196 GLY n 
1 197 PRO n 
1 198 LEU n 
1 199 VAL n 
1 200 CYS n 
1 201 LYS n 
1 202 VAL n 
1 203 ASN n 
1 204 GLY n 
1 205 THR n 
1 206 TRP n 
1 207 LEU n 
1 208 GLN n 
1 209 ALA n 
1 210 GLY n 
1 211 VAL n 
1 212 VAL n 
1 213 SER n 
1 214 TRP n 
1 215 GLY n 
1 216 GLU n 
1 217 GLY n 
1 218 CYS n 
1 219 ALA n 
1 220 GLN n 
1 221 PRO n 
1 222 ASN n 
1 223 ARG n 
1 224 PRO n 
1 225 GLY n 
1 226 ILE n 
1 227 TYR n 
1 228 THR n 
1 229 ARG n 
1 230 VAL n 
1 231 THR n 
1 232 TYR n 
1 233 TYR n 
1 234 LEU n 
1 235 ASP n 
1 236 TRP n 
1 237 ILE n 
1 238 HIS n 
1 239 HIS n 
1 240 TYR n 
1 241 VAL n 
1 242 PRO n 
1 243 LYS n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           243 
_entity_src_nat.common_name                human 
_entity_src_nat.pdbx_organism_scientific   'Homo sapiens' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9606 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     Lung 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1I52 non-polymer         . 
;~{N}-[(1~{S},2~{S})-6-azanyl-1-[5-[[4-[2-(3,4-dichlorophenyl)ethoxy]phenyl]methyl]-1,2,4-oxadiazol-3-yl]-1-oxidanyl-hexan-2-yl]-4-fluoranyl-benzamide
;
?                               'C30 H31 Cl2 F N4 O4' 601.496 
ACT   non-polymer         . 'ACETATE ION' ?                               'C2 H3 O2 -1'         59.044  
ALA   'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'          89.093  
ARG   'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'      175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'         132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'          133.103 
CYS   'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'        121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL'               'C2 H6 O2'            62.068  
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 
PEG   non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                               'C4 H10 O3'           106.120 
PHE   'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'         165.189 
PRO   'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'          115.130 
SER   'L-peptide linking' y SERINE ?                               'C3 H7 N O3'          105.093 
SO4   non-polymer         . 'SULFATE ION' ?                               'O4 S -2'             96.063  
THR   'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'          119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'       204.225 
TYR   'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'         181.189 
VAL   'L-peptide linking' y VALINE ?                               'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ILE 1   16  16  ILE ILE A . n 
A 1 2   VAL 2   17  17  VAL VAL A . n 
A 1 3   GLY 3   18  18  GLY GLY A . n 
A 1 4   GLY 4   19  19  GLY GLY A . n 
A 1 5   GLN 5   20  20  GLN GLN A . n 
A 1 6   GLU 6   21  21  GLU GLU A . n 
A 1 7   ALA 7   22  22  ALA ALA A . n 
A 1 8   PRO 8   23  23  PRO PRO A . n 
A 1 9   ARG 9   24  24  ARG ARG A . n 
A 1 10  SER 10  25  25  SER SER A . n 
A 1 11  LYS 11  26  26  LYS LYS A . n 
A 1 12  TRP 12  27  27  TRP TRP A . n 
A 1 13  PRO 13  28  28  PRO PRO A . n 
A 1 14  TRP 14  29  29  TRP TRP A . n 
A 1 15  GLN 15  30  30  GLN GLN A . n 
A 1 16  VAL 16  31  31  VAL VAL A . n 
A 1 17  SER 17  32  32  SER SER A . n 
A 1 18  LEU 18  33  33  LEU LEU A . n 
A 1 19  ARG 19  34  34  ARG ARG A . n 
A 1 20  VAL 20  35  35  VAL VAL A . n 
A 1 21  HIS 21  36  36  HIS HIS A . n 
A 1 22  GLY 22  37  37  GLY GLY A . n 
A 1 23  PRO 23  38  38  PRO PRO A . n 
A 1 24  TYR 24  39  39  TYR TYR A . n 
A 1 25  TRP 25  40  40  TRP TRP A . n 
A 1 26  MET 26  41  41  MET MET A . n 
A 1 27  HIS 27  42  42  HIS HIS A . n 
A 1 28  PHE 28  43  43  PHE PHE A . n 
A 1 29  CYS 29  44  44  CYS CYS A . n 
A 1 30  GLY 30  45  45  GLY GLY A . n 
A 1 31  GLY 31  46  46  GLY GLY A . n 
A 1 32  SER 32  47  47  SER SER A . n 
A 1 33  LEU 33  48  48  LEU LEU A . n 
A 1 34  ILE 34  49  49  ILE ILE A . n 
A 1 35  HIS 35  50  50  HIS HIS A . n 
A 1 36  PRO 36  51  51  PRO PRO A . n 
A 1 37  GLN 37  52  52  GLN GLN A . n 
A 1 38  TRP 38  53  53  TRP TRP A . n 
A 1 39  VAL 39  54  54  VAL VAL A . n 
A 1 40  LEU 40  55  55  LEU LEU A . n 
A 1 41  THR 41  56  56  THR THR A . n 
A 1 42  ALA 42  57  57  ALA ALA A . n 
A 1 43  ALA 43  58  58  ALA ALA A . n 
A 1 44  HIS 44  59  59  HIS HIS A . n 
A 1 45  CYS 45  60  60  CYS CYS A . n 
A 1 46  VAL 46  61  61  VAL VAL A . n 
A 1 47  GLY 47  62  62  GLY GLY A . n 
A 1 48  PRO 48  63  63  PRO PRO A . n 
A 1 49  ASP 49  64  64  ASP ASP A . n 
A 1 50  VAL 50  65  65  VAL VAL A . n 
A 1 51  LYS 51  66  66  LYS LYS A . n 
A 1 52  ASP 52  67  67  ASP ASP A . n 
A 1 53  LEU 53  68  68  LEU LEU A . n 
A 1 54  ALA 54  69  69  ALA ALA A . n 
A 1 55  ALA 55  70  70  ALA ALA A . n 
A 1 56  LEU 56  71  71  LEU LEU A . n 
A 1 57  ARG 57  72  72  ARG ARG A . n 
A 1 58  VAL 58  73  73  VAL VAL A . n 
A 1 59  GLN 59  74  74  GLN GLN A . n 
A 1 60  LEU 60  75  75  LEU LEU A . n 
A 1 61  ARG 61  76  76  ARG ARG A . n 
A 1 62  GLU 62  77  77  GLU GLU A . n 
A 1 63  GLN 63  78  78  GLN GLN A . n 
A 1 64  HIS 64  79  79  HIS HIS A . n 
A 1 65  LEU 65  80  80  LEU LEU A . n 
A 1 66  TYR 66  81  81  TYR TYR A . n 
A 1 67  TYR 67  82  82  TYR TYR A . n 
A 1 68  GLN 68  83  83  GLN GLN A . n 
A 1 69  ASP 69  84  84  ASP ASP A . n 
A 1 70  GLN 70  85  85  GLN GLN A . n 
A 1 71  LEU 71  86  86  LEU LEU A . n 
A 1 72  LEU 72  87  87  LEU LEU A . n 
A 1 73  PRO 73  88  88  PRO PRO A . n 
A 1 74  VAL 74  89  89  VAL VAL A . n 
A 1 75  SER 75  90  90  SER SER A . n 
A 1 76  ARG 76  91  91  ARG ARG A . n 
A 1 77  ILE 77  92  92  ILE ILE A . n 
A 1 78  ILE 78  93  93  ILE ILE A . n 
A 1 79  VAL 79  94  94  VAL VAL A . n 
A 1 80  HIS 80  95  95  HIS HIS A . n 
A 1 81  PRO 81  96  96  PRO PRO A . n 
A 1 82  GLN 82  97  97  GLN GLN A . n 
A 1 83  PHE 83  98  98  PHE PHE A . n 
A 1 84  TYR 84  99  99  TYR TYR A . n 
A 1 85  THR 85  100 100 THR THR A . n 
A 1 86  ALA 86  101 101 ALA ALA A . n 
A 1 87  GLN 87  102 102 GLN GLN A . n 
A 1 88  ILE 88  103 103 ILE ILE A . n 
A 1 89  GLY 89  104 104 GLY GLY A . n 
A 1 90  ALA 90  105 105 ALA ALA A . n 
A 1 91  ASP 91  106 106 ASP ASP A . n 
A 1 92  ILE 92  107 107 ILE ILE A . n 
A 1 93  ALA 93  108 108 ALA ALA A . n 
A 1 94  LEU 94  109 109 LEU LEU A . n 
A 1 95  LEU 95  110 110 LEU LEU A . n 
A 1 96  GLU 96  111 111 GLU GLU A . n 
A 1 97  LEU 97  112 112 LEU LEU A . n 
A 1 98  GLU 98  113 113 GLU GLU A . n 
A 1 99  GLU 99  114 114 GLU GLU A . n 
A 1 100 PRO 100 115 115 PRO PRO A . n 
A 1 101 VAL 101 116 116 VAL VAL A . n 
A 1 102 LYS 102 117 117 LYS LYS A . n 
A 1 103 VAL 103 118 118 VAL VAL A . n 
A 1 104 SER 104 119 119 SER SER A . n 
A 1 105 SER 105 120 120 SER SER A . n 
A 1 106 HIS 106 121 121 HIS HIS A . n 
A 1 107 VAL 107 122 122 VAL VAL A . n 
A 1 108 HIS 108 123 123 HIS HIS A . n 
A 1 109 THR 109 124 124 THR THR A . n 
A 1 110 VAL 110 125 125 VAL VAL A . n 
A 1 111 THR 111 126 126 THR THR A . n 
A 1 112 LEU 112 127 127 LEU LEU A . n 
A 1 113 PRO 113 128 128 PRO PRO A . n 
A 1 114 PRO 114 129 129 PRO PRO A . n 
A 1 115 ALA 115 130 130 ALA ALA A . n 
A 1 116 SER 116 131 131 SER SER A . n 
A 1 117 GLU 117 132 132 GLU GLU A . n 
A 1 118 THR 118 133 133 THR THR A . n 
A 1 119 PHE 119 134 134 PHE PHE A . n 
A 1 120 PRO 120 135 135 PRO PRO A . n 
A 1 121 PRO 121 136 136 PRO PRO A . n 
A 1 122 GLY 122 137 137 GLY GLY A . n 
A 1 123 MET 123 138 138 MET MET A . n 
A 1 124 PRO 124 139 139 PRO PRO A . n 
A 1 125 CYS 125 140 140 CYS CYS A . n 
A 1 126 TRP 126 141 141 TRP TRP A . n 
A 1 127 VAL 127 142 142 VAL VAL A . n 
A 1 128 THR 128 143 143 THR THR A . n 
A 1 129 GLY 129 144 144 GLY GLY A . n 
A 1 130 TRP 130 145 145 TRP TRP A . n 
A 1 131 GLY 131 146 146 GLY GLY A . n 
A 1 132 ASP 132 147 147 ASP ASP A . n 
A 1 133 VAL 133 148 148 VAL VAL A . n 
A 1 134 ASP 134 149 149 ASP ASP A . n 
A 1 135 ASN 135 150 150 ASN ASN A . n 
A 1 136 ASP 136 151 151 ASP ASP A . n 
A 1 137 GLU 137 152 152 GLU GLU A . n 
A 1 138 ARG 138 153 153 ARG ARG A . n 
A 1 139 LEU 139 154 154 LEU LEU A . n 
A 1 140 PRO 140 155 155 PRO PRO A . n 
A 1 141 PRO 141 156 156 PRO PRO A . n 
A 1 142 PRO 142 157 157 PRO PRO A . n 
A 1 143 PHE 143 158 158 PHE PHE A . n 
A 1 144 PRO 144 159 159 PRO PRO A . n 
A 1 145 LEU 145 160 160 LEU LEU A . n 
A 1 146 LYS 146 161 161 LYS LYS A . n 
A 1 147 GLN 147 162 162 GLN GLN A . n 
A 1 148 VAL 148 163 163 VAL VAL A . n 
A 1 149 LYS 149 164 164 LYS LYS A . n 
A 1 150 VAL 150 165 165 VAL VAL A . n 
A 1 151 PRO 151 166 166 PRO PRO A . n 
A 1 152 ILE 152 167 167 ILE ILE A . n 
A 1 153 MET 153 168 168 MET MET A . n 
A 1 154 GLU 154 169 169 GLU GLU A . n 
A 1 155 ASN 155 170 170 ASN ASN A . n 
A 1 156 HIS 156 171 171 HIS HIS A . n 
A 1 157 ILE 157 172 172 ILE ILE A . n 
A 1 158 CYS 158 173 173 CYS CYS A . n 
A 1 159 ASP 159 174 174 ASP ASP A . n 
A 1 160 ALA 160 175 175 ALA ALA A . n 
A 1 161 LYS 161 176 176 LYS LYS A . n 
A 1 162 TYR 162 177 177 TYR TYR A . n 
A 1 163 HIS 163 178 178 HIS HIS A . n 
A 1 164 LEU 164 179 179 LEU LEU A . n 
A 1 165 GLY 165 180 180 GLY GLY A . n 
A 1 166 ALA 166 181 181 ALA ALA A . n 
A 1 167 TYR 167 182 182 TYR TYR A . n 
A 1 168 THR 168 183 183 THR THR A . n 
A 1 169 GLY 169 184 184 GLY GLY A . n 
A 1 170 ASP 170 185 185 ASP ASP A . n 
A 1 171 ASP 171 186 186 ASP ASP A . n 
A 1 172 VAL 172 187 187 VAL VAL A . n 
A 1 173 ARG 173 188 188 ARG ARG A . n 
A 1 174 ILE 174 189 189 ILE ILE A . n 
A 1 175 VAL 175 190 190 VAL VAL A . n 
A 1 176 ARG 176 191 191 ARG ARG A . n 
A 1 177 ASP 177 192 192 ASP ASP A . n 
A 1 178 ASP 178 193 193 ASP ASP A . n 
A 1 179 MET 179 194 194 MET MET A . n 
A 1 180 LEU 180 195 195 LEU LEU A . n 
A 1 181 CYS 181 196 196 CYS CYS A . n 
A 1 182 ALA 182 197 197 ALA ALA A . n 
A 1 183 GLY 183 198 198 GLY GLY A . n 
A 1 184 ASN 184 199 199 ASN ASN A . n 
A 1 185 THR 185 200 200 THR THR A . n 
A 1 186 ARG 186 201 201 ARG ARG A . n 
A 1 187 ARG 187 202 202 ARG ARG A . n 
A 1 188 ASP 188 203 203 ASP ASP A . n 
A 1 189 SER 189 204 204 SER SER A . n 
A 1 190 CYS 190 205 205 CYS CYS A . n 
A 1 191 GLN 191 206 206 GLN GLN A . n 
A 1 192 GLY 192 207 207 GLY GLY A . n 
A 1 193 ASP 193 208 208 ASP ASP A . n 
A 1 194 SER 194 209 209 SER SER A . n 
A 1 195 GLY 195 210 210 GLY GLY A . n 
A 1 196 GLY 196 211 211 GLY GLY A . n 
A 1 197 PRO 197 212 212 PRO PRO A . n 
A 1 198 LEU 198 213 213 LEU LEU A . n 
A 1 199 VAL 199 214 214 VAL VAL A . n 
A 1 200 CYS 200 215 215 CYS CYS A . n 
A 1 201 LYS 201 216 216 LYS LYS A . n 
A 1 202 VAL 202 217 217 VAL VAL A . n 
A 1 203 ASN 203 218 218 ASN ASN A . n 
A 1 204 GLY 204 219 219 GLY GLY A . n 
A 1 205 THR 205 220 220 THR THR A . n 
A 1 206 TRP 206 221 221 TRP TRP A . n 
A 1 207 LEU 207 222 222 LEU LEU A . n 
A 1 208 GLN 208 223 223 GLN GLN A . n 
A 1 209 ALA 209 224 224 ALA ALA A . n 
A 1 210 GLY 210 225 225 GLY GLY A . n 
A 1 211 VAL 211 226 226 VAL VAL A . n 
A 1 212 VAL 212 227 227 VAL VAL A . n 
A 1 213 SER 213 228 228 SER SER A . n 
A 1 214 TRP 214 229 229 TRP TRP A . n 
A 1 215 GLY 215 230 230 GLY GLY A . n 
A 1 216 GLU 216 231 231 GLU GLU A . n 
A 1 217 GLY 217 232 232 GLY GLY A . n 
A 1 218 CYS 218 233 233 CYS CYS A . n 
A 1 219 ALA 219 234 234 ALA ALA A . n 
A 1 220 GLN 220 235 235 GLN GLN A . n 
A 1 221 PRO 221 236 236 PRO PRO A . n 
A 1 222 ASN 222 237 237 ASN ASN A . n 
A 1 223 ARG 223 238 238 ARG ARG A . n 
A 1 224 PRO 224 239 239 PRO PRO A . n 
A 1 225 GLY 225 240 240 GLY GLY A . n 
A 1 226 ILE 226 241 241 ILE ILE A . n 
A 1 227 TYR 227 242 242 TYR TYR A . n 
A 1 228 THR 228 243 243 THR THR A . n 
A 1 229 ARG 229 244 244 ARG ARG A . n 
A 1 230 VAL 230 245 245 VAL VAL A . n 
A 1 231 THR 231 246 246 THR THR A . n 
A 1 232 TYR 232 247 247 TYR TYR A . n 
A 1 233 TYR 233 248 248 TYR TYR A . n 
A 1 234 LEU 234 249 249 LEU LEU A . n 
A 1 235 ASP 235 250 250 ASP ASP A . n 
A 1 236 TRP 236 251 251 TRP TRP A . n 
A 1 237 ILE 237 252 252 ILE ILE A . n 
A 1 238 HIS 238 253 253 HIS HIS A . n 
A 1 239 HIS 239 254 254 HIS HIS A . n 
A 1 240 TYR 240 255 255 TYR TYR A . n 
A 1 241 VAL 241 256 256 VAL VAL A . n 
A 1 242 PRO 242 257 257 PRO PRO A . n 
A 1 243 LYS 243 258 258 LYS LYS A . n 
B 1 1   ILE 1   16  16  ILE ILE B . n 
B 1 2   VAL 2   17  17  VAL VAL B . n 
B 1 3   GLY 3   18  18  GLY GLY B . n 
B 1 4   GLY 4   19  19  GLY GLY B . n 
B 1 5   GLN 5   20  20  GLN GLN B . n 
B 1 6   GLU 6   21  21  GLU GLU B . n 
B 1 7   ALA 7   22  22  ALA ALA B . n 
B 1 8   PRO 8   23  23  PRO PRO B . n 
B 1 9   ARG 9   24  24  ARG ARG B . n 
B 1 10  SER 10  25  25  SER SER B . n 
B 1 11  LYS 11  26  26  LYS LYS B . n 
B 1 12  TRP 12  27  27  TRP TRP B . n 
B 1 13  PRO 13  28  28  PRO PRO B . n 
B 1 14  TRP 14  29  29  TRP TRP B . n 
B 1 15  GLN 15  30  30  GLN GLN B . n 
B 1 16  VAL 16  31  31  VAL VAL B . n 
B 1 17  SER 17  32  32  SER SER B . n 
B 1 18  LEU 18  33  33  LEU LEU B . n 
B 1 19  ARG 19  34  34  ARG ARG B . n 
B 1 20  VAL 20  35  35  VAL VAL B . n 
B 1 21  HIS 21  36  36  HIS HIS B . n 
B 1 22  GLY 22  37  37  GLY GLY B . n 
B 1 23  PRO 23  38  38  PRO PRO B . n 
B 1 24  TYR 24  39  39  TYR TYR B . n 
B 1 25  TRP 25  40  40  TRP TRP B . n 
B 1 26  MET 26  41  41  MET MET B . n 
B 1 27  HIS 27  42  42  HIS HIS B . n 
B 1 28  PHE 28  43  43  PHE PHE B . n 
B 1 29  CYS 29  44  44  CYS CYS B . n 
B 1 30  GLY 30  45  45  GLY GLY B . n 
B 1 31  GLY 31  46  46  GLY GLY B . n 
B 1 32  SER 32  47  47  SER SER B . n 
B 1 33  LEU 33  48  48  LEU LEU B . n 
B 1 34  ILE 34  49  49  ILE ILE B . n 
B 1 35  HIS 35  50  50  HIS HIS B . n 
B 1 36  PRO 36  51  51  PRO PRO B . n 
B 1 37  GLN 37  52  52  GLN GLN B . n 
B 1 38  TRP 38  53  53  TRP TRP B . n 
B 1 39  VAL 39  54  54  VAL VAL B . n 
B 1 40  LEU 40  55  55  LEU LEU B . n 
B 1 41  THR 41  56  56  THR THR B . n 
B 1 42  ALA 42  57  57  ALA ALA B . n 
B 1 43  ALA 43  58  58  ALA ALA B . n 
B 1 44  HIS 44  59  59  HIS HIS B . n 
B 1 45  CYS 45  60  60  CYS CYS B . n 
B 1 46  VAL 46  61  61  VAL VAL B . n 
B 1 47  GLY 47  62  62  GLY GLY B . n 
B 1 48  PRO 48  63  63  PRO PRO B . n 
B 1 49  ASP 49  64  64  ASP ASP B . n 
B 1 50  VAL 50  65  65  VAL VAL B . n 
B 1 51  LYS 51  66  66  LYS LYS B . n 
B 1 52  ASP 52  67  67  ASP ASP B . n 
B 1 53  LEU 53  68  68  LEU LEU B . n 
B 1 54  ALA 54  69  69  ALA ALA B . n 
B 1 55  ALA 55  70  70  ALA ALA B . n 
B 1 56  LEU 56  71  71  LEU LEU B . n 
B 1 57  ARG 57  72  72  ARG ARG B . n 
B 1 58  VAL 58  73  73  VAL VAL B . n 
B 1 59  GLN 59  74  74  GLN GLN B . n 
B 1 60  LEU 60  75  75  LEU LEU B . n 
B 1 61  ARG 61  76  76  ARG ARG B . n 
B 1 62  GLU 62  77  77  GLU GLU B . n 
B 1 63  GLN 63  78  78  GLN GLN B . n 
B 1 64  HIS 64  79  79  HIS HIS B . n 
B 1 65  LEU 65  80  80  LEU LEU B . n 
B 1 66  TYR 66  81  81  TYR TYR B . n 
B 1 67  TYR 67  82  82  TYR TYR B . n 
B 1 68  GLN 68  83  83  GLN GLN B . n 
B 1 69  ASP 69  84  84  ASP ASP B . n 
B 1 70  GLN 70  85  85  GLN GLN B . n 
B 1 71  LEU 71  86  86  LEU LEU B . n 
B 1 72  LEU 72  87  87  LEU LEU B . n 
B 1 73  PRO 73  88  88  PRO PRO B . n 
B 1 74  VAL 74  89  89  VAL VAL B . n 
B 1 75  SER 75  90  90  SER SER B . n 
B 1 76  ARG 76  91  91  ARG ARG B . n 
B 1 77  ILE 77  92  92  ILE ILE B . n 
B 1 78  ILE 78  93  93  ILE ILE B . n 
B 1 79  VAL 79  94  94  VAL VAL B . n 
B 1 80  HIS 80  95  95  HIS HIS B . n 
B 1 81  PRO 81  96  96  PRO PRO B . n 
B 1 82  GLN 82  97  97  GLN GLN B . n 
B 1 83  PHE 83  98  98  PHE PHE B . n 
B 1 84  TYR 84  99  99  TYR TYR B . n 
B 1 85  THR 85  100 100 THR THR B . n 
B 1 86  ALA 86  101 101 ALA ALA B . n 
B 1 87  GLN 87  102 102 GLN GLN B . n 
B 1 88  ILE 88  103 103 ILE ILE B . n 
B 1 89  GLY 89  104 104 GLY GLY B . n 
B 1 90  ALA 90  105 105 ALA ALA B . n 
B 1 91  ASP 91  106 106 ASP ASP B . n 
B 1 92  ILE 92  107 107 ILE ILE B . n 
B 1 93  ALA 93  108 108 ALA ALA B . n 
B 1 94  LEU 94  109 109 LEU LEU B . n 
B 1 95  LEU 95  110 110 LEU LEU B . n 
B 1 96  GLU 96  111 111 GLU GLU B . n 
B 1 97  LEU 97  112 112 LEU LEU B . n 
B 1 98  GLU 98  113 113 GLU GLU B . n 
B 1 99  GLU 99  114 114 GLU GLU B . n 
B 1 100 PRO 100 115 115 PRO PRO B . n 
B 1 101 VAL 101 116 116 VAL VAL B . n 
B 1 102 LYS 102 117 117 LYS LYS B . n 
B 1 103 VAL 103 118 118 VAL VAL B . n 
B 1 104 SER 104 119 119 SER SER B . n 
B 1 105 SER 105 120 120 SER SER B . n 
B 1 106 HIS 106 121 121 HIS HIS B . n 
B 1 107 VAL 107 122 122 VAL VAL B . n 
B 1 108 HIS 108 123 123 HIS HIS B . n 
B 1 109 THR 109 124 124 THR THR B . n 
B 1 110 VAL 110 125 125 VAL VAL B . n 
B 1 111 THR 111 126 126 THR THR B . n 
B 1 112 LEU 112 127 127 LEU LEU B . n 
B 1 113 PRO 113 128 128 PRO PRO B . n 
B 1 114 PRO 114 129 129 PRO PRO B . n 
B 1 115 ALA 115 130 130 ALA ALA B . n 
B 1 116 SER 116 131 131 SER SER B . n 
B 1 117 GLU 117 132 132 GLU GLU B . n 
B 1 118 THR 118 133 133 THR THR B . n 
B 1 119 PHE 119 134 134 PHE PHE B . n 
B 1 120 PRO 120 135 135 PRO PRO B . n 
B 1 121 PRO 121 136 136 PRO PRO B . n 
B 1 122 GLY 122 137 137 GLY GLY B . n 
B 1 123 MET 123 138 138 MET MET B . n 
B 1 124 PRO 124 139 139 PRO PRO B . n 
B 1 125 CYS 125 140 140 CYS CYS B . n 
B 1 126 TRP 126 141 141 TRP TRP B . n 
B 1 127 VAL 127 142 142 VAL VAL B . n 
B 1 128 THR 128 143 143 THR THR B . n 
B 1 129 GLY 129 144 144 GLY GLY B . n 
B 1 130 TRP 130 145 145 TRP TRP B . n 
B 1 131 GLY 131 146 146 GLY GLY B . n 
B 1 132 ASP 132 147 147 ASP ASP B . n 
B 1 133 VAL 133 148 148 VAL VAL B . n 
B 1 134 ASP 134 149 149 ASP ASP B . n 
B 1 135 ASN 135 150 150 ASN ASN B . n 
B 1 136 ASP 136 151 151 ASP ASP B . n 
B 1 137 GLU 137 152 152 GLU GLU B . n 
B 1 138 ARG 138 153 153 ARG ARG B . n 
B 1 139 LEU 139 154 154 LEU LEU B . n 
B 1 140 PRO 140 155 155 PRO PRO B . n 
B 1 141 PRO 141 156 156 PRO PRO B . n 
B 1 142 PRO 142 157 157 PRO PRO B . n 
B 1 143 PHE 143 158 158 PHE PHE B . n 
B 1 144 PRO 144 159 159 PRO PRO B . n 
B 1 145 LEU 145 160 160 LEU LEU B . n 
B 1 146 LYS 146 161 161 LYS LYS B . n 
B 1 147 GLN 147 162 162 GLN GLN B . n 
B 1 148 VAL 148 163 163 VAL VAL B . n 
B 1 149 LYS 149 164 164 LYS LYS B . n 
B 1 150 VAL 150 165 165 VAL VAL B . n 
B 1 151 PRO 151 166 166 PRO PRO B . n 
B 1 152 ILE 152 167 167 ILE ILE B . n 
B 1 153 MET 153 168 168 MET MET B . n 
B 1 154 GLU 154 169 169 GLU GLU B . n 
B 1 155 ASN 155 170 170 ASN ASN B . n 
B 1 156 HIS 156 171 171 HIS HIS B . n 
B 1 157 ILE 157 172 172 ILE ILE B . n 
B 1 158 CYS 158 173 173 CYS CYS B . n 
B 1 159 ASP 159 174 174 ASP ASP B . n 
B 1 160 ALA 160 175 175 ALA ALA B . n 
B 1 161 LYS 161 176 176 LYS LYS B . n 
B 1 162 TYR 162 177 177 TYR TYR B . n 
B 1 163 HIS 163 178 178 HIS HIS B . n 
B 1 164 LEU 164 179 179 LEU LEU B . n 
B 1 165 GLY 165 180 180 GLY GLY B . n 
B 1 166 ALA 166 181 181 ALA ALA B . n 
B 1 167 TYR 167 182 182 TYR TYR B . n 
B 1 168 THR 168 183 183 THR THR B . n 
B 1 169 GLY 169 184 184 GLY GLY B . n 
B 1 170 ASP 170 185 185 ASP ASP B . n 
B 1 171 ASP 171 186 186 ASP ASP B . n 
B 1 172 VAL 172 187 187 VAL VAL B . n 
B 1 173 ARG 173 188 188 ARG ARG B . n 
B 1 174 ILE 174 189 189 ILE ILE B . n 
B 1 175 VAL 175 190 190 VAL VAL B . n 
B 1 176 ARG 176 191 191 ARG ARG B . n 
B 1 177 ASP 177 192 192 ASP ASP B . n 
B 1 178 ASP 178 193 193 ASP ASP B . n 
B 1 179 MET 179 194 194 MET MET B . n 
B 1 180 LEU 180 195 195 LEU LEU B . n 
B 1 181 CYS 181 196 196 CYS CYS B . n 
B 1 182 ALA 182 197 197 ALA ALA B . n 
B 1 183 GLY 183 198 198 GLY GLY B . n 
B 1 184 ASN 184 199 199 ASN ASN B . n 
B 1 185 THR 185 200 200 THR THR B . n 
B 1 186 ARG 186 201 201 ARG ARG B . n 
B 1 187 ARG 187 202 202 ARG ARG B . n 
B 1 188 ASP 188 203 203 ASP ASP B . n 
B 1 189 SER 189 204 204 SER SER B . n 
B 1 190 CYS 190 205 205 CYS CYS B . n 
B 1 191 GLN 191 206 206 GLN GLN B . n 
B 1 192 GLY 192 207 207 GLY GLY B . n 
B 1 193 ASP 193 208 208 ASP ASP B . n 
B 1 194 SER 194 209 209 SER SER B . n 
B 1 195 GLY 195 210 210 GLY GLY B . n 
B 1 196 GLY 196 211 211 GLY GLY B . n 
B 1 197 PRO 197 212 212 PRO PRO B . n 
B 1 198 LEU 198 213 213 LEU LEU B . n 
B 1 199 VAL 199 214 214 VAL VAL B . n 
B 1 200 CYS 200 215 215 CYS CYS B . n 
B 1 201 LYS 201 216 216 LYS LYS B . n 
B 1 202 VAL 202 217 217 VAL VAL B . n 
B 1 203 ASN 203 218 218 ASN ASN B . n 
B 1 204 GLY 204 219 219 GLY GLY B . n 
B 1 205 THR 205 220 220 THR THR B . n 
B 1 206 TRP 206 221 221 TRP TRP B . n 
B 1 207 LEU 207 222 222 LEU LEU B . n 
B 1 208 GLN 208 223 223 GLN GLN B . n 
B 1 209 ALA 209 224 224 ALA ALA B . n 
B 1 210 GLY 210 225 225 GLY GLY B . n 
B 1 211 VAL 211 226 226 VAL VAL B . n 
B 1 212 VAL 212 227 227 VAL VAL B . n 
B 1 213 SER 213 228 228 SER SER B . n 
B 1 214 TRP 214 229 229 TRP TRP B . n 
B 1 215 GLY 215 230 230 GLY GLY B . n 
B 1 216 GLU 216 231 231 GLU GLU B . n 
B 1 217 GLY 217 232 232 GLY GLY B . n 
B 1 218 CYS 218 233 233 CYS CYS B . n 
B 1 219 ALA 219 234 234 ALA ALA B . n 
B 1 220 GLN 220 235 235 GLN GLN B . n 
B 1 221 PRO 221 236 236 PRO PRO B . n 
B 1 222 ASN 222 237 237 ASN ASN B . n 
B 1 223 ARG 223 238 238 ARG ARG B . n 
B 1 224 PRO 224 239 239 PRO PRO B . n 
B 1 225 GLY 225 240 240 GLY GLY B . n 
B 1 226 ILE 226 241 241 ILE ILE B . n 
B 1 227 TYR 227 242 242 TYR TYR B . n 
B 1 228 THR 228 243 243 THR THR B . n 
B 1 229 ARG 229 244 244 ARG ARG B . n 
B 1 230 VAL 230 245 245 VAL VAL B . n 
B 1 231 THR 231 246 246 THR THR B . n 
B 1 232 TYR 232 247 247 TYR TYR B . n 
B 1 233 TYR 233 248 248 TYR TYR B . n 
B 1 234 LEU 234 249 249 LEU LEU B . n 
B 1 235 ASP 235 250 250 ASP ASP B . n 
B 1 236 TRP 236 251 251 TRP TRP B . n 
B 1 237 ILE 237 252 252 ILE ILE B . n 
B 1 238 HIS 238 253 253 HIS HIS B . n 
B 1 239 HIS 239 254 254 HIS HIS B . n 
B 1 240 TYR 240 255 255 TYR TYR B . n 
B 1 241 VAL 241 256 256 VAL VAL B . n 
B 1 242 PRO 242 257 257 PRO PRO B . n 
B 1 243 LYS 243 258 258 LYS LYS B . n 
C 1 1   ILE 1   16  16  ILE ILE C . n 
C 1 2   VAL 2   17  17  VAL VAL C . n 
C 1 3   GLY 3   18  18  GLY GLY C . n 
C 1 4   GLY 4   19  19  GLY GLY C . n 
C 1 5   GLN 5   20  20  GLN GLN C . n 
C 1 6   GLU 6   21  21  GLU GLU C . n 
C 1 7   ALA 7   22  22  ALA ALA C . n 
C 1 8   PRO 8   23  23  PRO PRO C . n 
C 1 9   ARG 9   24  24  ARG ARG C . n 
C 1 10  SER 10  25  25  SER SER C . n 
C 1 11  LYS 11  26  26  LYS LYS C . n 
C 1 12  TRP 12  27  27  TRP TRP C . n 
C 1 13  PRO 13  28  28  PRO PRO C . n 
C 1 14  TRP 14  29  29  TRP TRP C . n 
C 1 15  GLN 15  30  30  GLN GLN C . n 
C 1 16  VAL 16  31  31  VAL VAL C . n 
C 1 17  SER 17  32  32  SER SER C . n 
C 1 18  LEU 18  33  33  LEU LEU C . n 
C 1 19  ARG 19  34  34  ARG ARG C . n 
C 1 20  VAL 20  35  35  VAL VAL C . n 
C 1 21  HIS 21  36  36  HIS HIS C . n 
C 1 22  GLY 22  37  37  GLY GLY C . n 
C 1 23  PRO 23  38  38  PRO PRO C . n 
C 1 24  TYR 24  39  39  TYR TYR C . n 
C 1 25  TRP 25  40  40  TRP TRP C . n 
C 1 26  MET 26  41  41  MET MET C . n 
C 1 27  HIS 27  42  42  HIS HIS C . n 
C 1 28  PHE 28  43  43  PHE PHE C . n 
C 1 29  CYS 29  44  44  CYS CYS C . n 
C 1 30  GLY 30  45  45  GLY GLY C . n 
C 1 31  GLY 31  46  46  GLY GLY C . n 
C 1 32  SER 32  47  47  SER SER C . n 
C 1 33  LEU 33  48  48  LEU LEU C . n 
C 1 34  ILE 34  49  49  ILE ILE C . n 
C 1 35  HIS 35  50  50  HIS HIS C . n 
C 1 36  PRO 36  51  51  PRO PRO C . n 
C 1 37  GLN 37  52  52  GLN GLN C . n 
C 1 38  TRP 38  53  53  TRP TRP C . n 
C 1 39  VAL 39  54  54  VAL VAL C . n 
C 1 40  LEU 40  55  55  LEU LEU C . n 
C 1 41  THR 41  56  56  THR THR C . n 
C 1 42  ALA 42  57  57  ALA ALA C . n 
C 1 43  ALA 43  58  58  ALA ALA C . n 
C 1 44  HIS 44  59  59  HIS HIS C . n 
C 1 45  CYS 45  60  60  CYS CYS C . n 
C 1 46  VAL 46  61  61  VAL VAL C . n 
C 1 47  GLY 47  62  62  GLY GLY C . n 
C 1 48  PRO 48  63  63  PRO PRO C . n 
C 1 49  ASP 49  64  64  ASP ASP C . n 
C 1 50  VAL 50  65  65  VAL VAL C . n 
C 1 51  LYS 51  66  66  LYS LYS C . n 
C 1 52  ASP 52  67  67  ASP ASP C . n 
C 1 53  LEU 53  68  68  LEU LEU C . n 
C 1 54  ALA 54  69  69  ALA ALA C . n 
C 1 55  ALA 55  70  70  ALA ALA C . n 
C 1 56  LEU 56  71  71  LEU LEU C . n 
C 1 57  ARG 57  72  72  ARG ARG C . n 
C 1 58  VAL 58  73  73  VAL VAL C . n 
C 1 59  GLN 59  74  74  GLN GLN C . n 
C 1 60  LEU 60  75  75  LEU LEU C . n 
C 1 61  ARG 61  76  76  ARG ARG C . n 
C 1 62  GLU 62  77  77  GLU GLU C . n 
C 1 63  GLN 63  78  78  GLN GLN C . n 
C 1 64  HIS 64  79  79  HIS HIS C . n 
C 1 65  LEU 65  80  80  LEU LEU C . n 
C 1 66  TYR 66  81  81  TYR TYR C . n 
C 1 67  TYR 67  82  82  TYR TYR C . n 
C 1 68  GLN 68  83  83  GLN GLN C . n 
C 1 69  ASP 69  84  84  ASP ASP C . n 
C 1 70  GLN 70  85  85  GLN GLN C . n 
C 1 71  LEU 71  86  86  LEU LEU C . n 
C 1 72  LEU 72  87  87  LEU LEU C . n 
C 1 73  PRO 73  88  88  PRO PRO C . n 
C 1 74  VAL 74  89  89  VAL VAL C . n 
C 1 75  SER 75  90  90  SER SER C . n 
C 1 76  ARG 76  91  91  ARG ARG C . n 
C 1 77  ILE 77  92  92  ILE ILE C . n 
C 1 78  ILE 78  93  93  ILE ILE C . n 
C 1 79  VAL 79  94  94  VAL VAL C . n 
C 1 80  HIS 80  95  95  HIS HIS C . n 
C 1 81  PRO 81  96  96  PRO PRO C . n 
C 1 82  GLN 82  97  97  GLN GLN C . n 
C 1 83  PHE 83  98  98  PHE PHE C . n 
C 1 84  TYR 84  99  99  TYR TYR C . n 
C 1 85  THR 85  100 100 THR THR C . n 
C 1 86  ALA 86  101 101 ALA ALA C . n 
C 1 87  GLN 87  102 102 GLN GLN C . n 
C 1 88  ILE 88  103 103 ILE ILE C . n 
C 1 89  GLY 89  104 104 GLY GLY C . n 
C 1 90  ALA 90  105 105 ALA ALA C . n 
C 1 91  ASP 91  106 106 ASP ASP C . n 
C 1 92  ILE 92  107 107 ILE ILE C . n 
C 1 93  ALA 93  108 108 ALA ALA C . n 
C 1 94  LEU 94  109 109 LEU LEU C . n 
C 1 95  LEU 95  110 110 LEU LEU C . n 
C 1 96  GLU 96  111 111 GLU GLU C . n 
C 1 97  LEU 97  112 112 LEU LEU C . n 
C 1 98  GLU 98  113 113 GLU GLU C . n 
C 1 99  GLU 99  114 114 GLU GLU C . n 
C 1 100 PRO 100 115 115 PRO PRO C . n 
C 1 101 VAL 101 116 116 VAL VAL C . n 
C 1 102 LYS 102 117 117 LYS LYS C . n 
C 1 103 VAL 103 118 118 VAL VAL C . n 
C 1 104 SER 104 119 119 SER SER C . n 
C 1 105 SER 105 120 120 SER SER C . n 
C 1 106 HIS 106 121 121 HIS HIS C . n 
C 1 107 VAL 107 122 122 VAL VAL C . n 
C 1 108 HIS 108 123 123 HIS HIS C . n 
C 1 109 THR 109 124 124 THR THR C . n 
C 1 110 VAL 110 125 125 VAL VAL C . n 
C 1 111 THR 111 126 126 THR THR C . n 
C 1 112 LEU 112 127 127 LEU LEU C . n 
C 1 113 PRO 113 128 128 PRO PRO C . n 
C 1 114 PRO 114 129 129 PRO PRO C . n 
C 1 115 ALA 115 130 130 ALA ALA C . n 
C 1 116 SER 116 131 131 SER SER C . n 
C 1 117 GLU 117 132 132 GLU GLU C . n 
C 1 118 THR 118 133 133 THR THR C . n 
C 1 119 PHE 119 134 134 PHE PHE C . n 
C 1 120 PRO 120 135 135 PRO PRO C . n 
C 1 121 PRO 121 136 136 PRO PRO C . n 
C 1 122 GLY 122 137 137 GLY GLY C . n 
C 1 123 MET 123 138 138 MET MET C . n 
C 1 124 PRO 124 139 139 PRO PRO C . n 
C 1 125 CYS 125 140 140 CYS CYS C . n 
C 1 126 TRP 126 141 141 TRP TRP C . n 
C 1 127 VAL 127 142 142 VAL VAL C . n 
C 1 128 THR 128 143 143 THR THR C . n 
C 1 129 GLY 129 144 144 GLY GLY C . n 
C 1 130 TRP 130 145 145 TRP TRP C . n 
C 1 131 GLY 131 146 146 GLY GLY C . n 
C 1 132 ASP 132 147 147 ASP ASP C . n 
C 1 133 VAL 133 148 148 VAL VAL C . n 
C 1 134 ASP 134 149 149 ASP ASP C . n 
C 1 135 ASN 135 150 150 ASN ASN C . n 
C 1 136 ASP 136 151 151 ASP ASP C . n 
C 1 137 GLU 137 152 152 GLU GLU C . n 
C 1 138 ARG 138 153 153 ARG ARG C . n 
C 1 139 LEU 139 154 154 LEU LEU C . n 
C 1 140 PRO 140 155 155 PRO PRO C . n 
C 1 141 PRO 141 156 156 PRO PRO C . n 
C 1 142 PRO 142 157 157 PRO PRO C . n 
C 1 143 PHE 143 158 158 PHE PHE C . n 
C 1 144 PRO 144 159 159 PRO PRO C . n 
C 1 145 LEU 145 160 160 LEU LEU C . n 
C 1 146 LYS 146 161 161 LYS LYS C . n 
C 1 147 GLN 147 162 162 GLN GLN C . n 
C 1 148 VAL 148 163 163 VAL VAL C . n 
C 1 149 LYS 149 164 164 LYS LYS C . n 
C 1 150 VAL 150 165 165 VAL VAL C . n 
C 1 151 PRO 151 166 166 PRO PRO C . n 
C 1 152 ILE 152 167 167 ILE ILE C . n 
C 1 153 MET 153 168 168 MET MET C . n 
C 1 154 GLU 154 169 169 GLU GLU C . n 
C 1 155 ASN 155 170 170 ASN ASN C . n 
C 1 156 HIS 156 171 171 HIS HIS C . n 
C 1 157 ILE 157 172 172 ILE ILE C . n 
C 1 158 CYS 158 173 173 CYS CYS C . n 
C 1 159 ASP 159 174 174 ASP ASP C . n 
C 1 160 ALA 160 175 175 ALA ALA C . n 
C 1 161 LYS 161 176 176 LYS LYS C . n 
C 1 162 TYR 162 177 177 TYR TYR C . n 
C 1 163 HIS 163 178 178 HIS HIS C . n 
C 1 164 LEU 164 179 179 LEU LEU C . n 
C 1 165 GLY 165 180 180 GLY GLY C . n 
C 1 166 ALA 166 181 181 ALA ALA C . n 
C 1 167 TYR 167 182 182 TYR TYR C . n 
C 1 168 THR 168 183 183 THR THR C . n 
C 1 169 GLY 169 184 184 GLY GLY C . n 
C 1 170 ASP 170 185 185 ASP ASP C . n 
C 1 171 ASP 171 186 186 ASP ASP C . n 
C 1 172 VAL 172 187 187 VAL VAL C . n 
C 1 173 ARG 173 188 188 ARG ARG C . n 
C 1 174 ILE 174 189 189 ILE ILE C . n 
C 1 175 VAL 175 190 190 VAL VAL C . n 
C 1 176 ARG 176 191 191 ARG ARG C . n 
C 1 177 ASP 177 192 192 ASP ASP C . n 
C 1 178 ASP 178 193 193 ASP ASP C . n 
C 1 179 MET 179 194 194 MET MET C . n 
C 1 180 LEU 180 195 195 LEU LEU C . n 
C 1 181 CYS 181 196 196 CYS CYS C . n 
C 1 182 ALA 182 197 197 ALA ALA C . n 
C 1 183 GLY 183 198 198 GLY GLY C . n 
C 1 184 ASN 184 199 199 ASN ASN C . n 
C 1 185 THR 185 200 200 THR THR C . n 
C 1 186 ARG 186 201 201 ARG ARG C . n 
C 1 187 ARG 187 202 202 ARG ARG C . n 
C 1 188 ASP 188 203 203 ASP ASP C . n 
C 1 189 SER 189 204 204 SER SER C . n 
C 1 190 CYS 190 205 205 CYS CYS C . n 
C 1 191 GLN 191 206 206 GLN GLN C . n 
C 1 192 GLY 192 207 207 GLY GLY C . n 
C 1 193 ASP 193 208 208 ASP ASP C . n 
C 1 194 SER 194 209 209 SER SER C . n 
C 1 195 GLY 195 210 210 GLY GLY C . n 
C 1 196 GLY 196 211 211 GLY GLY C . n 
C 1 197 PRO 197 212 212 PRO PRO C . n 
C 1 198 LEU 198 213 213 LEU LEU C . n 
C 1 199 VAL 199 214 214 VAL VAL C . n 
C 1 200 CYS 200 215 215 CYS CYS C . n 
C 1 201 LYS 201 216 216 LYS LYS C . n 
C 1 202 VAL 202 217 217 VAL VAL C . n 
C 1 203 ASN 203 218 218 ASN ASN C . n 
C 1 204 GLY 204 219 219 GLY GLY C . n 
C 1 205 THR 205 220 220 THR THR C . n 
C 1 206 TRP 206 221 221 TRP TRP C . n 
C 1 207 LEU 207 222 222 LEU LEU C . n 
C 1 208 GLN 208 223 223 GLN GLN C . n 
C 1 209 ALA 209 224 224 ALA ALA C . n 
C 1 210 GLY 210 225 225 GLY GLY C . n 
C 1 211 VAL 211 226 226 VAL VAL C . n 
C 1 212 VAL 212 227 227 VAL VAL C . n 
C 1 213 SER 213 228 228 SER SER C . n 
C 1 214 TRP 214 229 229 TRP TRP C . n 
C 1 215 GLY 215 230 230 GLY GLY C . n 
C 1 216 GLU 216 231 231 GLU GLU C . n 
C 1 217 GLY 217 232 232 GLY GLY C . n 
C 1 218 CYS 218 233 233 CYS CYS C . n 
C 1 219 ALA 219 234 234 ALA ALA C . n 
C 1 220 GLN 220 235 235 GLN GLN C . n 
C 1 221 PRO 221 236 236 PRO PRO C . n 
C 1 222 ASN 222 237 237 ASN ASN C . n 
C 1 223 ARG 223 238 238 ARG ARG C . n 
C 1 224 PRO 224 239 239 PRO PRO C . n 
C 1 225 GLY 225 240 240 GLY GLY C . n 
C 1 226 ILE 226 241 241 ILE ILE C . n 
C 1 227 TYR 227 242 242 TYR TYR C . n 
C 1 228 THR 228 243 243 THR THR C . n 
C 1 229 ARG 229 244 244 ARG ARG C . n 
C 1 230 VAL 230 245 245 VAL VAL C . n 
C 1 231 THR 231 246 246 THR THR C . n 
C 1 232 TYR 232 247 247 TYR TYR C . n 
C 1 233 TYR 233 248 248 TYR TYR C . n 
C 1 234 LEU 234 249 249 LEU LEU C . n 
C 1 235 ASP 235 250 250 ASP ASP C . n 
C 1 236 TRP 236 251 251 TRP TRP C . n 
C 1 237 ILE 237 252 252 ILE ILE C . n 
C 1 238 HIS 238 253 253 HIS HIS C . n 
C 1 239 HIS 239 254 254 HIS HIS C . n 
C 1 240 TYR 240 255 255 TYR TYR C . n 
C 1 241 VAL 241 256 256 VAL VAL C . n 
C 1 242 PRO 242 257 257 PRO PRO C . n 
C 1 243 LYS 243 258 258 LYS LYS C . n 
D 1 1   ILE 1   16  16  ILE ILE D . n 
D 1 2   VAL 2   17  17  VAL VAL D . n 
D 1 3   GLY 3   18  18  GLY GLY D . n 
D 1 4   GLY 4   19  19  GLY GLY D . n 
D 1 5   GLN 5   20  20  GLN GLN D . n 
D 1 6   GLU 6   21  21  GLU GLU D . n 
D 1 7   ALA 7   22  22  ALA ALA D . n 
D 1 8   PRO 8   23  23  PRO PRO D . n 
D 1 9   ARG 9   24  24  ARG ARG D . n 
D 1 10  SER 10  25  25  SER SER D . n 
D 1 11  LYS 11  26  26  LYS LYS D . n 
D 1 12  TRP 12  27  27  TRP TRP D . n 
D 1 13  PRO 13  28  28  PRO PRO D . n 
D 1 14  TRP 14  29  29  TRP TRP D . n 
D 1 15  GLN 15  30  30  GLN GLN D . n 
D 1 16  VAL 16  31  31  VAL VAL D . n 
D 1 17  SER 17  32  32  SER SER D . n 
D 1 18  LEU 18  33  33  LEU LEU D . n 
D 1 19  ARG 19  34  34  ARG ARG D . n 
D 1 20  VAL 20  35  35  VAL VAL D . n 
D 1 21  HIS 21  36  36  HIS HIS D . n 
D 1 22  GLY 22  37  37  GLY GLY D . n 
D 1 23  PRO 23  38  38  PRO PRO D . n 
D 1 24  TYR 24  39  39  TYR TYR D . n 
D 1 25  TRP 25  40  40  TRP TRP D . n 
D 1 26  MET 26  41  41  MET MET D . n 
D 1 27  HIS 27  42  42  HIS HIS D . n 
D 1 28  PHE 28  43  43  PHE PHE D . n 
D 1 29  CYS 29  44  44  CYS CYS D . n 
D 1 30  GLY 30  45  45  GLY GLY D . n 
D 1 31  GLY 31  46  46  GLY GLY D . n 
D 1 32  SER 32  47  47  SER SER D . n 
D 1 33  LEU 33  48  48  LEU LEU D . n 
D 1 34  ILE 34  49  49  ILE ILE D . n 
D 1 35  HIS 35  50  50  HIS HIS D . n 
D 1 36  PRO 36  51  51  PRO PRO D . n 
D 1 37  GLN 37  52  52  GLN GLN D . n 
D 1 38  TRP 38  53  53  TRP TRP D . n 
D 1 39  VAL 39  54  54  VAL VAL D . n 
D 1 40  LEU 40  55  55  LEU LEU D . n 
D 1 41  THR 41  56  56  THR THR D . n 
D 1 42  ALA 42  57  57  ALA ALA D . n 
D 1 43  ALA 43  58  58  ALA ALA D . n 
D 1 44  HIS 44  59  59  HIS HIS D . n 
D 1 45  CYS 45  60  60  CYS CYS D . n 
D 1 46  VAL 46  61  61  VAL VAL D . n 
D 1 47  GLY 47  62  62  GLY GLY D . n 
D 1 48  PRO 48  63  63  PRO PRO D . n 
D 1 49  ASP 49  64  64  ASP ASP D . n 
D 1 50  VAL 50  65  65  VAL VAL D . n 
D 1 51  LYS 51  66  66  LYS LYS D . n 
D 1 52  ASP 52  67  67  ASP ASP D . n 
D 1 53  LEU 53  68  68  LEU LEU D . n 
D 1 54  ALA 54  69  69  ALA ALA D . n 
D 1 55  ALA 55  70  70  ALA ALA D . n 
D 1 56  LEU 56  71  71  LEU LEU D . n 
D 1 57  ARG 57  72  72  ARG ARG D . n 
D 1 58  VAL 58  73  73  VAL VAL D . n 
D 1 59  GLN 59  74  74  GLN GLN D . n 
D 1 60  LEU 60  75  75  LEU LEU D . n 
D 1 61  ARG 61  76  76  ARG ARG D . n 
D 1 62  GLU 62  77  77  GLU GLU D . n 
D 1 63  GLN 63  78  78  GLN GLN D . n 
D 1 64  HIS 64  79  79  HIS HIS D . n 
D 1 65  LEU 65  80  80  LEU LEU D . n 
D 1 66  TYR 66  81  81  TYR TYR D . n 
D 1 67  TYR 67  82  82  TYR TYR D . n 
D 1 68  GLN 68  83  83  GLN GLN D . n 
D 1 69  ASP 69  84  84  ASP ASP D . n 
D 1 70  GLN 70  85  85  GLN GLN D . n 
D 1 71  LEU 71  86  86  LEU LEU D . n 
D 1 72  LEU 72  87  87  LEU LEU D . n 
D 1 73  PRO 73  88  88  PRO PRO D . n 
D 1 74  VAL 74  89  89  VAL VAL D . n 
D 1 75  SER 75  90  90  SER SER D . n 
D 1 76  ARG 76  91  91  ARG ARG D . n 
D 1 77  ILE 77  92  92  ILE ILE D . n 
D 1 78  ILE 78  93  93  ILE ILE D . n 
D 1 79  VAL 79  94  94  VAL VAL D . n 
D 1 80  HIS 80  95  95  HIS HIS D . n 
D 1 81  PRO 81  96  96  PRO PRO D . n 
D 1 82  GLN 82  97  97  GLN GLN D . n 
D 1 83  PHE 83  98  98  PHE PHE D . n 
D 1 84  TYR 84  99  99  TYR TYR D . n 
D 1 85  THR 85  100 100 THR THR D . n 
D 1 86  ALA 86  101 101 ALA ALA D . n 
D 1 87  GLN 87  102 102 GLN GLN D . n 
D 1 88  ILE 88  103 103 ILE ILE D . n 
D 1 89  GLY 89  104 104 GLY GLY D . n 
D 1 90  ALA 90  105 105 ALA ALA D . n 
D 1 91  ASP 91  106 106 ASP ASP D . n 
D 1 92  ILE 92  107 107 ILE ILE D . n 
D 1 93  ALA 93  108 108 ALA ALA D . n 
D 1 94  LEU 94  109 109 LEU LEU D . n 
D 1 95  LEU 95  110 110 LEU LEU D . n 
D 1 96  GLU 96  111 111 GLU GLU D . n 
D 1 97  LEU 97  112 112 LEU LEU D . n 
D 1 98  GLU 98  113 113 GLU GLU D . n 
D 1 99  GLU 99  114 114 GLU GLU D . n 
D 1 100 PRO 100 115 115 PRO PRO D . n 
D 1 101 VAL 101 116 116 VAL VAL D . n 
D 1 102 LYS 102 117 117 LYS LYS D . n 
D 1 103 VAL 103 118 118 VAL VAL D . n 
D 1 104 SER 104 119 119 SER SER D . n 
D 1 105 SER 105 120 120 SER SER D . n 
D 1 106 HIS 106 121 121 HIS HIS D . n 
D 1 107 VAL 107 122 122 VAL VAL D . n 
D 1 108 HIS 108 123 123 HIS HIS D . n 
D 1 109 THR 109 124 124 THR THR D . n 
D 1 110 VAL 110 125 125 VAL VAL D . n 
D 1 111 THR 111 126 126 THR THR D . n 
D 1 112 LEU 112 127 127 LEU LEU D . n 
D 1 113 PRO 113 128 128 PRO PRO D . n 
D 1 114 PRO 114 129 129 PRO PRO D . n 
D 1 115 ALA 115 130 130 ALA ALA D . n 
D 1 116 SER 116 131 131 SER SER D . n 
D 1 117 GLU 117 132 132 GLU GLU D . n 
D 1 118 THR 118 133 133 THR THR D . n 
D 1 119 PHE 119 134 134 PHE PHE D . n 
D 1 120 PRO 120 135 135 PRO PRO D . n 
D 1 121 PRO 121 136 136 PRO PRO D . n 
D 1 122 GLY 122 137 137 GLY GLY D . n 
D 1 123 MET 123 138 138 MET MET D . n 
D 1 124 PRO 124 139 139 PRO PRO D . n 
D 1 125 CYS 125 140 140 CYS CYS D . n 
D 1 126 TRP 126 141 141 TRP TRP D . n 
D 1 127 VAL 127 142 142 VAL VAL D . n 
D 1 128 THR 128 143 143 THR THR D . n 
D 1 129 GLY 129 144 144 GLY GLY D . n 
D 1 130 TRP 130 145 145 TRP TRP D . n 
D 1 131 GLY 131 146 146 GLY GLY D . n 
D 1 132 ASP 132 147 147 ASP ASP D . n 
D 1 133 VAL 133 148 148 VAL VAL D . n 
D 1 134 ASP 134 149 149 ASP ASP D . n 
D 1 135 ASN 135 150 150 ASN ASN D . n 
D 1 136 ASP 136 151 151 ASP ASP D . n 
D 1 137 GLU 137 152 152 GLU GLU D . n 
D 1 138 ARG 138 153 153 ARG ARG D . n 
D 1 139 LEU 139 154 154 LEU LEU D . n 
D 1 140 PRO 140 155 155 PRO PRO D . n 
D 1 141 PRO 141 156 156 PRO PRO D . n 
D 1 142 PRO 142 157 157 PRO PRO D . n 
D 1 143 PHE 143 158 158 PHE PHE D . n 
D 1 144 PRO 144 159 159 PRO PRO D . n 
D 1 145 LEU 145 160 160 LEU LEU D . n 
D 1 146 LYS 146 161 161 LYS LYS D . n 
D 1 147 GLN 147 162 162 GLN GLN D . n 
D 1 148 VAL 148 163 163 VAL VAL D . n 
D 1 149 LYS 149 164 164 LYS LYS D . n 
D 1 150 VAL 150 165 165 VAL VAL D . n 
D 1 151 PRO 151 166 166 PRO PRO D . n 
D 1 152 ILE 152 167 167 ILE ILE D . n 
D 1 153 MET 153 168 168 MET MET D . n 
D 1 154 GLU 154 169 169 GLU GLU D . n 
D 1 155 ASN 155 170 170 ASN ASN D . n 
D 1 156 HIS 156 171 171 HIS HIS D . n 
D 1 157 ILE 157 172 172 ILE ILE D . n 
D 1 158 CYS 158 173 173 CYS CYS D . n 
D 1 159 ASP 159 174 174 ASP ASP D . n 
D 1 160 ALA 160 175 175 ALA ALA D . n 
D 1 161 LYS 161 176 176 LYS LYS D . n 
D 1 162 TYR 162 177 177 TYR TYR D . n 
D 1 163 HIS 163 178 178 HIS HIS D . n 
D 1 164 LEU 164 179 179 LEU LEU D . n 
D 1 165 GLY 165 180 180 GLY GLY D . n 
D 1 166 ALA 166 181 181 ALA ALA D . n 
D 1 167 TYR 167 182 182 TYR TYR D . n 
D 1 168 THR 168 183 183 THR THR D . n 
D 1 169 GLY 169 184 184 GLY GLY D . n 
D 1 170 ASP 170 185 185 ASP ASP D . n 
D 1 171 ASP 171 186 186 ASP ASP D . n 
D 1 172 VAL 172 187 187 VAL VAL D . n 
D 1 173 ARG 173 188 188 ARG ARG D . n 
D 1 174 ILE 174 189 189 ILE ILE D . n 
D 1 175 VAL 175 190 190 VAL VAL D . n 
D 1 176 ARG 176 191 191 ARG ARG D . n 
D 1 177 ASP 177 192 192 ASP ASP D . n 
D 1 178 ASP 178 193 193 ASP ASP D . n 
D 1 179 MET 179 194 194 MET MET D . n 
D 1 180 LEU 180 195 195 LEU LEU D . n 
D 1 181 CYS 181 196 196 CYS CYS D . n 
D 1 182 ALA 182 197 197 ALA ALA D . n 
D 1 183 GLY 183 198 198 GLY GLY D . n 
D 1 184 ASN 184 199 199 ASN ASN D . n 
D 1 185 THR 185 200 200 THR THR D . n 
D 1 186 ARG 186 201 201 ARG ARG D . n 
D 1 187 ARG 187 202 202 ARG ARG D . n 
D 1 188 ASP 188 203 203 ASP ASP D . n 
D 1 189 SER 189 204 204 SER SER D . n 
D 1 190 CYS 190 205 205 CYS CYS D . n 
D 1 191 GLN 191 206 206 GLN GLN D . n 
D 1 192 GLY 192 207 207 GLY GLY D . n 
D 1 193 ASP 193 208 208 ASP ASP D . n 
D 1 194 SER 194 209 209 SER SER D . n 
D 1 195 GLY 195 210 210 GLY GLY D . n 
D 1 196 GLY 196 211 211 GLY GLY D . n 
D 1 197 PRO 197 212 212 PRO PRO D . n 
D 1 198 LEU 198 213 213 LEU LEU D . n 
D 1 199 VAL 199 214 214 VAL VAL D . n 
D 1 200 CYS 200 215 215 CYS CYS D . n 
D 1 201 LYS 201 216 216 LYS LYS D . n 
D 1 202 VAL 202 217 217 VAL VAL D . n 
D 1 203 ASN 203 218 218 ASN ASN D . n 
D 1 204 GLY 204 219 219 GLY GLY D . n 
D 1 205 THR 205 220 220 THR THR D . n 
D 1 206 TRP 206 221 221 TRP TRP D . n 
D 1 207 LEU 207 222 222 LEU LEU D . n 
D 1 208 GLN 208 223 223 GLN GLN D . n 
D 1 209 ALA 209 224 224 ALA ALA D . n 
D 1 210 GLY 210 225 225 GLY GLY D . n 
D 1 211 VAL 211 226 226 VAL VAL D . n 
D 1 212 VAL 212 227 227 VAL VAL D . n 
D 1 213 SER 213 228 228 SER SER D . n 
D 1 214 TRP 214 229 229 TRP TRP D . n 
D 1 215 GLY 215 230 230 GLY GLY D . n 
D 1 216 GLU 216 231 231 GLU GLU D . n 
D 1 217 GLY 217 232 232 GLY GLY D . n 
D 1 218 CYS 218 233 233 CYS CYS D . n 
D 1 219 ALA 219 234 234 ALA ALA D . n 
D 1 220 GLN 220 235 235 GLN GLN D . n 
D 1 221 PRO 221 236 236 PRO PRO D . n 
D 1 222 ASN 222 237 237 ASN ASN D . n 
D 1 223 ARG 223 238 238 ARG ARG D . n 
D 1 224 PRO 224 239 239 PRO PRO D . n 
D 1 225 GLY 225 240 240 GLY GLY D . n 
D 1 226 ILE 226 241 241 ILE ILE D . n 
D 1 227 TYR 227 242 242 TYR TYR D . n 
D 1 228 THR 228 243 243 THR THR D . n 
D 1 229 ARG 229 244 244 ARG ARG D . n 
D 1 230 VAL 230 245 245 VAL VAL D . n 
D 1 231 THR 231 246 246 THR THR D . n 
D 1 232 TYR 232 247 247 TYR TYR D . n 
D 1 233 TYR 233 248 248 TYR TYR D . n 
D 1 234 LEU 234 249 249 LEU LEU D . n 
D 1 235 ASP 235 250 250 ASP ASP D . n 
D 1 236 TRP 236 251 251 TRP TRP D . n 
D 1 237 ILE 237 252 252 ILE ILE D . n 
D 1 238 HIS 238 253 253 HIS HIS D . n 
D 1 239 HIS 239 254 254 HIS HIS D . n 
D 1 240 TYR 240 255 255 TYR TYR D . n 
D 1 241 VAL 241 256 256 VAL VAL D . n 
D 1 242 PRO 242 257 257 PRO PRO D . n 
D 1 243 LYS 243 258 258 LYS LYS D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ACT   ? ? ACT   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 EDO   ? ? EDO   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 GOL   ? ? GOL   ? ? 'SUBJECT OF INVESTIGATION' ? 
4 A1I52 ? ? A1I52 ? ? 'SUBJECT OF INVESTIGATION' ? 
5 PEG   ? ? PEG   ? ? 'SUBJECT OF INVESTIGATION' ? 
6 SO4   ? ? SO4   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
E  2 A1I52 1   301 1   A1I52 INX A . 
F  3 SO4   1   302 3   SO4   SO4 A . 
G  3 SO4   1   303 12  SO4   SO4 A . 
H  3 SO4   1   304 23  SO4   SO4 A . 
I  3 SO4   1   305 26  SO4   SO4 A . 
J  4 PEG   1   306 28  PEG   PEG A . 
K  5 EDO   1   307 32  EDO   EDO A . 
L  5 EDO   1   308 33  EDO   EDO A . 
M  5 EDO   1   309 34  EDO   EDO A . 
N  6 ACT   1   310 41  ACT   ACT A . 
O  2 A1I52 1   301 2   A1I52 INX B . 
P  3 SO4   1   302 5   SO4   SO4 B . 
Q  3 SO4   1   303 8   SO4   SO4 B . 
R  6 ACT   1   304 10  ACT   ACT B . 
S  7 GOL   1   305 11  GOL   GOL B . 
T  5 EDO   1   306 16  EDO   EDO B . 
U  3 SO4   1   307 27  SO4   SO4 B . 
V  5 EDO   1   308 37  EDO   EDO B . 
W  5 EDO   1   309 38  EDO   EDO B . 
X  2 A1I52 1   301 3   A1I52 INX C . 
Y  3 SO4   1   302 6   SO4   SO4 C . 
Z  3 SO4   1   303 9   SO4   SO4 C . 
AA 3 SO4   1   304 17  SO4   SO4 C . 
BA 3 SO4   1   305 20  SO4   SO4 C . 
CA 5 EDO   1   306 21  EDO   EDO C . 
DA 6 ACT   1   307 22  ACT   ACT C . 
EA 3 SO4   1   308 25  SO4   SO4 C . 
FA 5 EDO   1   309 29  EDO   EDO C . 
GA 5 EDO   1   310 30  EDO   EDO C . 
HA 5 EDO   1   311 40  EDO   EDO C . 
IA 5 EDO   1   312 42  EDO   EDO C . 
JA 2 A1I52 1   301 4   A1I52 INX D . 
KA 3 SO4   1   302 7   SO4   SO4 D . 
LA 3 SO4   1   303 13  SO4   SO4 D . 
MA 5 EDO   1   304 14  EDO   EDO D . 
NA 3 SO4   1   305 18  SO4   SO4 D . 
OA 3 SO4   1   306 19  SO4   SO4 D . 
PA 5 EDO   1   307 24  EDO   EDO D . 
QA 4 PEG   1   308 31  PEG   PEG D . 
RA 5 EDO   1   309 35  EDO   EDO D . 
SA 5 EDO   1   310 36  EDO   EDO D . 
TA 8 HOH   1   401 247 HOH   HOH A . 
TA 8 HOH   2   402 584 HOH   HOH A . 
TA 8 HOH   3   403 626 HOH   HOH A . 
TA 8 HOH   4   404 614 HOH   HOH A . 
TA 8 HOH   5   405 613 HOH   HOH A . 
TA 8 HOH   6   406 493 HOH   HOH A . 
TA 8 HOH   7   407 41  HOH   HOH A . 
TA 8 HOH   8   408 228 HOH   HOH A . 
TA 8 HOH   9   409 132 HOH   HOH A . 
TA 8 HOH   10  410 110 HOH   HOH A . 
TA 8 HOH   11  411 127 HOH   HOH A . 
TA 8 HOH   12  412 603 HOH   HOH A . 
TA 8 HOH   13  413 336 HOH   HOH A . 
TA 8 HOH   14  414 409 HOH   HOH A . 
TA 8 HOH   15  415 269 HOH   HOH A . 
TA 8 HOH   16  416 371 HOH   HOH A . 
TA 8 HOH   17  417 425 HOH   HOH A . 
TA 8 HOH   18  418 212 HOH   HOH A . 
TA 8 HOH   19  419 126 HOH   HOH A . 
TA 8 HOH   20  420 600 HOH   HOH A . 
TA 8 HOH   21  421 181 HOH   HOH A . 
TA 8 HOH   22  422 103 HOH   HOH A . 
TA 8 HOH   23  423 299 HOH   HOH A . 
TA 8 HOH   24  424 467 HOH   HOH A . 
TA 8 HOH   25  425 32  HOH   HOH A . 
TA 8 HOH   26  426 473 HOH   HOH A . 
TA 8 HOH   27  427 323 HOH   HOH A . 
TA 8 HOH   28  428 302 HOH   HOH A . 
TA 8 HOH   29  429 253 HOH   HOH A . 
TA 8 HOH   30  430 89  HOH   HOH A . 
TA 8 HOH   31  431 569 HOH   HOH A . 
TA 8 HOH   32  432 1   HOH   HOH A . 
TA 8 HOH   33  433 174 HOH   HOH A . 
TA 8 HOH   34  434 328 HOH   HOH A . 
TA 8 HOH   35  435 327 HOH   HOH A . 
TA 8 HOH   36  436 4   HOH   HOH A . 
TA 8 HOH   37  437 332 HOH   HOH A . 
TA 8 HOH   38  438 64  HOH   HOH A . 
TA 8 HOH   39  439 121 HOH   HOH A . 
TA 8 HOH   40  440 227 HOH   HOH A . 
TA 8 HOH   41  441 561 HOH   HOH A . 
TA 8 HOH   42  442 72  HOH   HOH A . 
TA 8 HOH   43  443 67  HOH   HOH A . 
TA 8 HOH   44  444 39  HOH   HOH A . 
TA 8 HOH   45  445 285 HOH   HOH A . 
TA 8 HOH   46  446 502 HOH   HOH A . 
TA 8 HOH   47  447 266 HOH   HOH A . 
TA 8 HOH   48  448 334 HOH   HOH A . 
TA 8 HOH   49  449 61  HOH   HOH A . 
TA 8 HOH   50  450 66  HOH   HOH A . 
TA 8 HOH   51  451 143 HOH   HOH A . 
TA 8 HOH   52  452 262 HOH   HOH A . 
TA 8 HOH   53  453 162 HOH   HOH A . 
TA 8 HOH   54  454 593 HOH   HOH A . 
TA 8 HOH   55  455 259 HOH   HOH A . 
TA 8 HOH   56  456 381 HOH   HOH A . 
TA 8 HOH   57  457 136 HOH   HOH A . 
TA 8 HOH   58  458 205 HOH   HOH A . 
TA 8 HOH   59  459 200 HOH   HOH A . 
TA 8 HOH   60  460 387 HOH   HOH A . 
TA 8 HOH   61  461 115 HOH   HOH A . 
TA 8 HOH   62  462 77  HOH   HOH A . 
TA 8 HOH   63  463 73  HOH   HOH A . 
TA 8 HOH   64  464 117 HOH   HOH A . 
TA 8 HOH   65  465 362 HOH   HOH A . 
TA 8 HOH   66  466 62  HOH   HOH A . 
TA 8 HOH   67  467 611 HOH   HOH A . 
TA 8 HOH   68  468 116 HOH   HOH A . 
TA 8 HOH   69  469 6   HOH   HOH A . 
TA 8 HOH   70  470 69  HOH   HOH A . 
TA 8 HOH   71  471 153 HOH   HOH A . 
TA 8 HOH   72  472 214 HOH   HOH A . 
TA 8 HOH   73  473 24  HOH   HOH A . 
TA 8 HOH   74  474 8   HOH   HOH A . 
TA 8 HOH   75  475 125 HOH   HOH A . 
TA 8 HOH   76  476 13  HOH   HOH A . 
TA 8 HOH   77  477 260 HOH   HOH A . 
TA 8 HOH   78  478 30  HOH   HOH A . 
TA 8 HOH   79  479 356 HOH   HOH A . 
TA 8 HOH   80  480 199 HOH   HOH A . 
TA 8 HOH   81  481 261 HOH   HOH A . 
TA 8 HOH   82  482 58  HOH   HOH A . 
TA 8 HOH   83  483 374 HOH   HOH A . 
TA 8 HOH   84  484 68  HOH   HOH A . 
TA 8 HOH   85  485 540 HOH   HOH A . 
TA 8 HOH   86  486 324 HOH   HOH A . 
TA 8 HOH   87  487 101 HOH   HOH A . 
TA 8 HOH   88  488 480 HOH   HOH A . 
TA 8 HOH   89  489 75  HOH   HOH A . 
TA 8 HOH   90  490 369 HOH   HOH A . 
TA 8 HOH   91  491 120 HOH   HOH A . 
TA 8 HOH   92  492 279 HOH   HOH A . 
TA 8 HOH   93  493 404 HOH   HOH A . 
TA 8 HOH   94  494 601 HOH   HOH A . 
TA 8 HOH   95  495 408 HOH   HOH A . 
TA 8 HOH   96  496 274 HOH   HOH A . 
TA 8 HOH   97  497 498 HOH   HOH A . 
TA 8 HOH   98  498 406 HOH   HOH A . 
TA 8 HOH   99  499 248 HOH   HOH A . 
TA 8 HOH   100 500 128 HOH   HOH A . 
TA 8 HOH   101 501 410 HOH   HOH A . 
TA 8 HOH   102 502 187 HOH   HOH A . 
TA 8 HOH   103 503 35  HOH   HOH A . 
TA 8 HOH   104 504 380 HOH   HOH A . 
TA 8 HOH   105 505 553 HOH   HOH A . 
TA 8 HOH   106 506 322 HOH   HOH A . 
TA 8 HOH   107 507 257 HOH   HOH A . 
TA 8 HOH   108 508 504 HOH   HOH A . 
TA 8 HOH   109 509 300 HOH   HOH A . 
TA 8 HOH   110 510 93  HOH   HOH A . 
TA 8 HOH   111 511 592 HOH   HOH A . 
TA 8 HOH   112 512 620 HOH   HOH A . 
TA 8 HOH   113 513 570 HOH   HOH A . 
TA 8 HOH   114 514 588 HOH   HOH A . 
TA 8 HOH   115 515 211 HOH   HOH A . 
TA 8 HOH   116 516 206 HOH   HOH A . 
TA 8 HOH   117 517 141 HOH   HOH A . 
TA 8 HOH   118 518 74  HOH   HOH A . 
TA 8 HOH   119 519 183 HOH   HOH A . 
TA 8 HOH   120 520 166 HOH   HOH A . 
TA 8 HOH   121 521 131 HOH   HOH A . 
TA 8 HOH   122 522 629 HOH   HOH A . 
TA 8 HOH   123 523 526 HOH   HOH A . 
TA 8 HOH   124 524 304 HOH   HOH A . 
TA 8 HOH   125 525 513 HOH   HOH A . 
TA 8 HOH   126 526 621 HOH   HOH A . 
TA 8 HOH   127 527 358 HOH   HOH A . 
TA 8 HOH   128 528 533 HOH   HOH A . 
TA 8 HOH   129 529 599 HOH   HOH A . 
TA 8 HOH   130 530 312 HOH   HOH A . 
TA 8 HOH   131 531 497 HOH   HOH A . 
TA 8 HOH   132 532 150 HOH   HOH A . 
TA 8 HOH   133 533 417 HOH   HOH A . 
TA 8 HOH   134 534 403 HOH   HOH A . 
TA 8 HOH   135 535 305 HOH   HOH A . 
TA 8 HOH   136 536 151 HOH   HOH A . 
TA 8 HOH   137 537 190 HOH   HOH A . 
TA 8 HOH   138 538 405 HOH   HOH A . 
TA 8 HOH   139 539 292 HOH   HOH A . 
TA 8 HOH   140 540 589 HOH   HOH A . 
TA 8 HOH   141 541 462 HOH   HOH A . 
TA 8 HOH   142 542 579 HOH   HOH A . 
TA 8 HOH   143 543 368 HOH   HOH A . 
TA 8 HOH   144 544 463 HOH   HOH A . 
TA 8 HOH   145 545 213 HOH   HOH A . 
TA 8 HOH   146 546 407 HOH   HOH A . 
TA 8 HOH   147 547 612 HOH   HOH A . 
TA 8 HOH   148 548 191 HOH   HOH A . 
TA 8 HOH   149 549 503 HOH   HOH A . 
UA 8 HOH   1   401 597 HOH   HOH B . 
UA 8 HOH   2   402 119 HOH   HOH B . 
UA 8 HOH   3   403 542 HOH   HOH B . 
UA 8 HOH   4   404 250 HOH   HOH B . 
UA 8 HOH   5   405 441 HOH   HOH B . 
UA 8 HOH   6   406 238 HOH   HOH B . 
UA 8 HOH   7   407 318 HOH   HOH B . 
UA 8 HOH   8   408 470 HOH   HOH B . 
UA 8 HOH   9   409 268 HOH   HOH B . 
UA 8 HOH   10  410 571 HOH   HOH B . 
UA 8 HOH   11  411 429 HOH   HOH B . 
UA 8 HOH   12  412 21  HOH   HOH B . 
UA 8 HOH   13  413 210 HOH   HOH B . 
UA 8 HOH   14  414 218 HOH   HOH B . 
UA 8 HOH   15  415 564 HOH   HOH B . 
UA 8 HOH   16  416 95  HOH   HOH B . 
UA 8 HOH   17  417 252 HOH   HOH B . 
UA 8 HOH   18  418 148 HOH   HOH B . 
UA 8 HOH   19  419 460 HOH   HOH B . 
UA 8 HOH   20  420 283 HOH   HOH B . 
UA 8 HOH   21  421 137 HOH   HOH B . 
UA 8 HOH   22  422 237 HOH   HOH B . 
UA 8 HOH   23  423 245 HOH   HOH B . 
UA 8 HOH   24  424 81  HOH   HOH B . 
UA 8 HOH   25  425 51  HOH   HOH B . 
UA 8 HOH   26  426 105 HOH   HOH B . 
UA 8 HOH   27  427 59  HOH   HOH B . 
UA 8 HOH   28  428 596 HOH   HOH B . 
UA 8 HOH   29  429 84  HOH   HOH B . 
UA 8 HOH   30  430 457 HOH   HOH B . 
UA 8 HOH   31  431 572 HOH   HOH B . 
UA 8 HOH   32  432 507 HOH   HOH B . 
UA 8 HOH   33  433 544 HOH   HOH B . 
UA 8 HOH   34  434 496 HOH   HOH B . 
UA 8 HOH   35  435 9   HOH   HOH B . 
UA 8 HOH   36  436 138 HOH   HOH B . 
UA 8 HOH   37  437 382 HOH   HOH B . 
UA 8 HOH   38  438 438 HOH   HOH B . 
UA 8 HOH   39  439 610 HOH   HOH B . 
UA 8 HOH   40  440 350 HOH   HOH B . 
UA 8 HOH   41  441 348 HOH   HOH B . 
UA 8 HOH   42  442 454 HOH   HOH B . 
UA 8 HOH   43  443 87  HOH   HOH B . 
UA 8 HOH   44  444 185 HOH   HOH B . 
UA 8 HOH   45  445 426 HOH   HOH B . 
UA 8 HOH   46  446 15  HOH   HOH B . 
UA 8 HOH   47  447 364 HOH   HOH B . 
UA 8 HOH   48  448 152 HOH   HOH B . 
UA 8 HOH   49  449 37  HOH   HOH B . 
UA 8 HOH   50  450 177 HOH   HOH B . 
UA 8 HOH   51  451 97  HOH   HOH B . 
UA 8 HOH   52  452 449 HOH   HOH B . 
UA 8 HOH   53  453 239 HOH   HOH B . 
UA 8 HOH   54  454 202 HOH   HOH B . 
UA 8 HOH   55  455 372 HOH   HOH B . 
UA 8 HOH   56  456 159 HOH   HOH B . 
UA 8 HOH   57  457 244 HOH   HOH B . 
UA 8 HOH   58  458 196 HOH   HOH B . 
UA 8 HOH   59  459 427 HOH   HOH B . 
UA 8 HOH   60  460 106 HOH   HOH B . 
UA 8 HOH   61  461 289 HOH   HOH B . 
UA 8 HOH   62  462 45  HOH   HOH B . 
UA 8 HOH   63  463 11  HOH   HOH B . 
UA 8 HOH   64  464 236 HOH   HOH B . 
UA 8 HOH   65  465 147 HOH   HOH B . 
UA 8 HOH   66  466 492 HOH   HOH B . 
UA 8 HOH   67  467 437 HOH   HOH B . 
UA 8 HOH   68  468 354 HOH   HOH B . 
UA 8 HOH   69  469 618 HOH   HOH B . 
UA 8 HOH   70  470 217 HOH   HOH B . 
UA 8 HOH   71  471 226 HOH   HOH B . 
UA 8 HOH   72  472 193 HOH   HOH B . 
UA 8 HOH   73  473 229 HOH   HOH B . 
UA 8 HOH   74  474 423 HOH   HOH B . 
UA 8 HOH   75  475 363 HOH   HOH B . 
UA 8 HOH   76  476 479 HOH   HOH B . 
UA 8 HOH   77  477 298 HOH   HOH B . 
UA 8 HOH   78  478 123 HOH   HOH B . 
UA 8 HOH   79  479 416 HOH   HOH B . 
UA 8 HOH   80  480 201 HOH   HOH B . 
UA 8 HOH   81  481 508 HOH   HOH B . 
UA 8 HOH   82  482 432 HOH   HOH B . 
UA 8 HOH   83  483 514 HOH   HOH B . 
UA 8 HOH   84  484 586 HOH   HOH B . 
UA 8 HOH   85  485 602 HOH   HOH B . 
UA 8 HOH   86  486 461 HOH   HOH B . 
UA 8 HOH   87  487 235 HOH   HOH B . 
UA 8 HOH   88  488 189 HOH   HOH B . 
UA 8 HOH   89  489 474 HOH   HOH B . 
UA 8 HOH   90  490 184 HOH   HOH B . 
UA 8 HOH   91  491 314 HOH   HOH B . 
UA 8 HOH   92  492 60  HOH   HOH B . 
UA 8 HOH   93  493 484 HOH   HOH B . 
UA 8 HOH   94  494 490 HOH   HOH B . 
UA 8 HOH   95  495 251 HOH   HOH B . 
UA 8 HOH   96  496 263 HOH   HOH B . 
UA 8 HOH   97  497 559 HOH   HOH B . 
UA 8 HOH   98  498 450 HOH   HOH B . 
UA 8 HOH   99  499 488 HOH   HOH B . 
UA 8 HOH   100 500 133 HOH   HOH B . 
UA 8 HOH   101 501 168 HOH   HOH B . 
UA 8 HOH   102 502 477 HOH   HOH B . 
UA 8 HOH   103 503 225 HOH   HOH B . 
UA 8 HOH   104 504 234 HOH   HOH B . 
UA 8 HOH   105 505 616 HOH   HOH B . 
UA 8 HOH   106 506 231 HOH   HOH B . 
UA 8 HOH   107 507 34  HOH   HOH B . 
UA 8 HOH   108 508 280 HOH   HOH B . 
UA 8 HOH   109 509 617 HOH   HOH B . 
UA 8 HOH   110 510 583 HOH   HOH B . 
UA 8 HOH   111 511 443 HOH   HOH B . 
UA 8 HOH   112 512 483 HOH   HOH B . 
UA 8 HOH   113 513 276 HOH   HOH B . 
UA 8 HOH   114 514 415 HOH   HOH B . 
UA 8 HOH   115 515 622 HOH   HOH B . 
UA 8 HOH   116 516 481 HOH   HOH B . 
UA 8 HOH   117 517 398 HOH   HOH B . 
UA 8 HOH   118 518 455 HOH   HOH B . 
UA 8 HOH   119 519 444 HOH   HOH B . 
UA 8 HOH   120 520 482 HOH   HOH B . 
VA 8 HOH   1   401 578 HOH   HOH C . 
VA 8 HOH   2   402 249 HOH   HOH C . 
VA 8 HOH   3   403 164 HOH   HOH C . 
VA 8 HOH   4   404 434 HOH   HOH C . 
VA 8 HOH   5   405 489 HOH   HOH C . 
VA 8 HOH   6   406 439 HOH   HOH C . 
VA 8 HOH   7   407 433 HOH   HOH C . 
VA 8 HOH   8   408 10  HOH   HOH C . 
VA 8 HOH   9   409 573 HOH   HOH C . 
VA 8 HOH   10  410 264 HOH   HOH C . 
VA 8 HOH   11  411 606 HOH   HOH C . 
VA 8 HOH   12  412 442 HOH   HOH C . 
VA 8 HOH   13  413 256 HOH   HOH C . 
VA 8 HOH   14  414 224 HOH   HOH C . 
VA 8 HOH   15  415 172 HOH   HOH C . 
VA 8 HOH   16  416 186 HOH   HOH C . 
VA 8 HOH   17  417 108 HOH   HOH C . 
VA 8 HOH   18  418 509 HOH   HOH C . 
VA 8 HOH   19  419 297 HOH   HOH C . 
VA 8 HOH   20  420 265 HOH   HOH C . 
VA 8 HOH   21  421 146 HOH   HOH C . 
VA 8 HOH   22  422 271 HOH   HOH C . 
VA 8 HOH   23  423 501 HOH   HOH C . 
VA 8 HOH   24  424 47  HOH   HOH C . 
VA 8 HOH   25  425 379 HOH   HOH C . 
VA 8 HOH   26  426 288 HOH   HOH C . 
VA 8 HOH   27  427 113 HOH   HOH C . 
VA 8 HOH   28  428 57  HOH   HOH C . 
VA 8 HOH   29  429 122 HOH   HOH C . 
VA 8 HOH   30  430 555 HOH   HOH C . 
VA 8 HOH   31  431 232 HOH   HOH C . 
VA 8 HOH   32  432 286 HOH   HOH C . 
VA 8 HOH   33  433 26  HOH   HOH C . 
VA 8 HOH   34  434 5   HOH   HOH C . 
VA 8 HOH   35  435 349 HOH   HOH C . 
VA 8 HOH   36  436 576 HOH   HOH C . 
VA 8 HOH   37  437 173 HOH   HOH C . 
VA 8 HOH   38  438 42  HOH   HOH C . 
VA 8 HOH   39  439 469 HOH   HOH C . 
VA 8 HOH   40  440 472 HOH   HOH C . 
VA 8 HOH   41  441 165 HOH   HOH C . 
VA 8 HOH   42  442 54  HOH   HOH C . 
VA 8 HOH   43  443 20  HOH   HOH C . 
VA 8 HOH   44  444 155 HOH   HOH C . 
VA 8 HOH   45  445 287 HOH   HOH C . 
VA 8 HOH   46  446 94  HOH   HOH C . 
VA 8 HOH   47  447 631 HOH   HOH C . 
VA 8 HOH   48  448 158 HOH   HOH C . 
VA 8 HOH   49  449 222 HOH   HOH C . 
VA 8 HOH   50  450 511 HOH   HOH C . 
VA 8 HOH   51  451 605 HOH   HOH C . 
VA 8 HOH   52  452 419 HOH   HOH C . 
VA 8 HOH   53  453 339 HOH   HOH C . 
VA 8 HOH   54  454 149 HOH   HOH C . 
VA 8 HOH   55  455 195 HOH   HOH C . 
VA 8 HOH   56  456 63  HOH   HOH C . 
VA 8 HOH   57  457 18  HOH   HOH C . 
VA 8 HOH   58  458 203 HOH   HOH C . 
VA 8 HOH   59  459 515 HOH   HOH C . 
VA 8 HOH   60  460 604 HOH   HOH C . 
VA 8 HOH   61  461 270 HOH   HOH C . 
VA 8 HOH   62  462 19  HOH   HOH C . 
VA 8 HOH   63  463 360 HOH   HOH C . 
VA 8 HOH   64  464 466 HOH   HOH C . 
VA 8 HOH   65  465 163 HOH   HOH C . 
VA 8 HOH   66  466 456 HOH   HOH C . 
VA 8 HOH   67  467 90  HOH   HOH C . 
VA 8 HOH   68  468 591 HOH   HOH C . 
VA 8 HOH   69  469 50  HOH   HOH C . 
VA 8 HOH   70  470 22  HOH   HOH C . 
VA 8 HOH   71  471 340 HOH   HOH C . 
VA 8 HOH   72  472 528 HOH   HOH C . 
VA 8 HOH   73  473 160 HOH   HOH C . 
VA 8 HOH   74  474 194 HOH   HOH C . 
VA 8 HOH   75  475 558 HOH   HOH C . 
VA 8 HOH   76  476 365 HOH   HOH C . 
VA 8 HOH   77  477 464 HOH   HOH C . 
VA 8 HOH   78  478 170 HOH   HOH C . 
VA 8 HOH   79  479 204 HOH   HOH C . 
VA 8 HOH   80  480 333 HOH   HOH C . 
VA 8 HOH   81  481 376 HOH   HOH C . 
VA 8 HOH   82  482 485 HOH   HOH C . 
VA 8 HOH   83  483 487 HOH   HOH C . 
VA 8 HOH   84  484 118 HOH   HOH C . 
VA 8 HOH   85  485 351 HOH   HOH C . 
VA 8 HOH   86  486 223 HOH   HOH C . 
VA 8 HOH   87  487 104 HOH   HOH C . 
VA 8 HOH   88  488 361 HOH   HOH C . 
VA 8 HOH   89  489 500 HOH   HOH C . 
VA 8 HOH   90  490 48  HOH   HOH C . 
VA 8 HOH   91  491 353 HOH   HOH C . 
VA 8 HOH   92  492 567 HOH   HOH C . 
VA 8 HOH   93  493 556 HOH   HOH C . 
VA 8 HOH   94  494 595 HOH   HOH C . 
VA 8 HOH   95  495 506 HOH   HOH C . 
VA 8 HOH   96  496 468 HOH   HOH C . 
VA 8 HOH   97  497 574 HOH   HOH C . 
VA 8 HOH   98  498 412 HOH   HOH C . 
VA 8 HOH   99  499 315 HOH   HOH C . 
VA 8 HOH   100 500 385 HOH   HOH C . 
VA 8 HOH   101 501 169 HOH   HOH C . 
VA 8 HOH   102 502 44  HOH   HOH C . 
VA 8 HOH   103 503 543 HOH   HOH C . 
VA 8 HOH   104 504 448 HOH   HOH C . 
VA 8 HOH   105 505 453 HOH   HOH C . 
VA 8 HOH   106 506 594 HOH   HOH C . 
VA 8 HOH   107 507 335 HOH   HOH C . 
VA 8 HOH   108 508 130 HOH   HOH C . 
VA 8 HOH   109 509 440 HOH   HOH C . 
VA 8 HOH   110 510 451 HOH   HOH C . 
VA 8 HOH   111 511 411 HOH   HOH C . 
VA 8 HOH   112 512 418 HOH   HOH C . 
VA 8 HOH   113 513 471 HOH   HOH C . 
VA 8 HOH   114 514 476 HOH   HOH C . 
VA 8 HOH   115 515 452 HOH   HOH C . 
WA 8 HOH   1   401 625 HOH   HOH D . 
WA 8 HOH   2   402 577 HOH   HOH D . 
WA 8 HOH   3   403 607 HOH   HOH D . 
WA 8 HOH   4   404 157 HOH   HOH D . 
WA 8 HOH   5   405 331 HOH   HOH D . 
WA 8 HOH   6   406 38  HOH   HOH D . 
WA 8 HOH   7   407 445 HOH   HOH D . 
WA 8 HOH   8   408 215 HOH   HOH D . 
WA 8 HOH   9   409 140 HOH   HOH D . 
WA 8 HOH   10  410 258 HOH   HOH D . 
WA 8 HOH   11  411 486 HOH   HOH D . 
WA 8 HOH   12  412 145 HOH   HOH D . 
WA 8 HOH   13  413 391 HOH   HOH D . 
WA 8 HOH   14  414 272 HOH   HOH D . 
WA 8 HOH   15  415 240 HOH   HOH D . 
WA 8 HOH   16  416 420 HOH   HOH D . 
WA 8 HOH   17  417 220 HOH   HOH D . 
WA 8 HOH   18  418 29  HOH   HOH D . 
WA 8 HOH   19  419 630 HOH   HOH D . 
WA 8 HOH   20  420 527 HOH   HOH D . 
WA 8 HOH   21  421 388 HOH   HOH D . 
WA 8 HOH   22  422 86  HOH   HOH D . 
WA 8 HOH   23  423 241 HOH   HOH D . 
WA 8 HOH   24  424 178 HOH   HOH D . 
WA 8 HOH   25  425 325 HOH   HOH D . 
WA 8 HOH   26  426 100 HOH   HOH D . 
WA 8 HOH   27  427 107 HOH   HOH D . 
WA 8 HOH   28  428 568 HOH   HOH D . 
WA 8 HOH   29  429 96  HOH   HOH D . 
WA 8 HOH   30  430 510 HOH   HOH D . 
WA 8 HOH   31  431 12  HOH   HOH D . 
WA 8 HOH   32  432 14  HOH   HOH D . 
WA 8 HOH   33  433 367 HOH   HOH D . 
WA 8 HOH   34  434 494 HOH   HOH D . 
WA 8 HOH   35  435 378 HOH   HOH D . 
WA 8 HOH   36  436 337 HOH   HOH D . 
WA 8 HOH   37  437 295 HOH   HOH D . 
WA 8 HOH   38  438 587 HOH   HOH D . 
WA 8 HOH   39  439 43  HOH   HOH D . 
WA 8 HOH   40  440 319 HOH   HOH D . 
WA 8 HOH   41  441 142 HOH   HOH D . 
WA 8 HOH   42  442 307 HOH   HOH D . 
WA 8 HOH   43  443 175 HOH   HOH D . 
WA 8 HOH   44  444 80  HOH   HOH D . 
WA 8 HOH   45  445 422 HOH   HOH D . 
WA 8 HOH   46  446 282 HOH   HOH D . 
WA 8 HOH   47  447 91  HOH   HOH D . 
WA 8 HOH   48  448 25  HOH   HOH D . 
WA 8 HOH   49  449 40  HOH   HOH D . 
WA 8 HOH   50  450 560 HOH   HOH D . 
WA 8 HOH   51  451 3   HOH   HOH D . 
WA 8 HOH   52  452 197 HOH   HOH D . 
WA 8 HOH   53  453 49  HOH   HOH D . 
WA 8 HOH   54  454 208 HOH   HOH D . 
WA 8 HOH   55  455 109 HOH   HOH D . 
WA 8 HOH   56  456 355 HOH   HOH D . 
WA 8 HOH   57  457 179 HOH   HOH D . 
WA 8 HOH   58  458 114 HOH   HOH D . 
WA 8 HOH   59  459 134 HOH   HOH D . 
WA 8 HOH   60  460 246 HOH   HOH D . 
WA 8 HOH   61  461 293 HOH   HOH D . 
WA 8 HOH   62  462 495 HOH   HOH D . 
WA 8 HOH   63  463 85  HOH   HOH D . 
WA 8 HOH   64  464 55  HOH   HOH D . 
WA 8 HOH   65  465 198 HOH   HOH D . 
WA 8 HOH   66  466 46  HOH   HOH D . 
WA 8 HOH   67  467 619 HOH   HOH D . 
WA 8 HOH   68  468 16  HOH   HOH D . 
WA 8 HOH   69  469 76  HOH   HOH D . 
WA 8 HOH   70  470 7   HOH   HOH D . 
WA 8 HOH   71  471 65  HOH   HOH D . 
WA 8 HOH   72  472 505 HOH   HOH D . 
WA 8 HOH   73  473 71  HOH   HOH D . 
WA 8 HOH   74  474 221 HOH   HOH D . 
WA 8 HOH   75  475 446 HOH   HOH D . 
WA 8 HOH   76  476 557 HOH   HOH D . 
WA 8 HOH   77  477 17  HOH   HOH D . 
WA 8 HOH   78  478 219 HOH   HOH D . 
WA 8 HOH   79  479 156 HOH   HOH D . 
WA 8 HOH   80  480 284 HOH   HOH D . 
WA 8 HOH   81  481 27  HOH   HOH D . 
WA 8 HOH   82  482 478 HOH   HOH D . 
WA 8 HOH   83  483 28  HOH   HOH D . 
WA 8 HOH   84  484 139 HOH   HOH D . 
WA 8 HOH   85  485 79  HOH   HOH D . 
WA 8 HOH   86  486 180 HOH   HOH D . 
WA 8 HOH   87  487 243 HOH   HOH D . 
WA 8 HOH   88  488 395 HOH   HOH D . 
WA 8 HOH   89  489 392 HOH   HOH D . 
WA 8 HOH   90  490 341 HOH   HOH D . 
WA 8 HOH   91  491 370 HOH   HOH D . 
WA 8 HOH   92  492 70  HOH   HOH D . 
WA 8 HOH   93  493 111 HOH   HOH D . 
WA 8 HOH   94  494 384 HOH   HOH D . 
WA 8 HOH   95  495 294 HOH   HOH D . 
WA 8 HOH   96  496 608 HOH   HOH D . 
WA 8 HOH   97  497 275 HOH   HOH D . 
WA 8 HOH   98  498 242 HOH   HOH D . 
WA 8 HOH   99  499 342 HOH   HOH D . 
WA 8 HOH   100 500 192 HOH   HOH D . 
WA 8 HOH   101 501 83  HOH   HOH D . 
WA 8 HOH   102 502 98  HOH   HOH D . 
WA 8 HOH   103 503 554 HOH   HOH D . 
WA 8 HOH   104 504 273 HOH   HOH D . 
WA 8 HOH   105 505 538 HOH   HOH D . 
WA 8 HOH   106 506 209 HOH   HOH D . 
WA 8 HOH   107 507 414 HOH   HOH D . 
WA 8 HOH   108 508 609 HOH   HOH D . 
WA 8 HOH   109 509 359 HOH   HOH D . 
WA 8 HOH   110 510 519 HOH   HOH D . 
WA 8 HOH   111 511 56  HOH   HOH D . 
WA 8 HOH   112 512 396 HOH   HOH D . 
WA 8 HOH   113 513 537 HOH   HOH D . 
WA 8 HOH   114 514 188 HOH   HOH D . 
WA 8 HOH   115 515 598 HOH   HOH D . 
WA 8 HOH   116 516 535 HOH   HOH D . 
WA 8 HOH   117 517 499 HOH   HOH D . 
WA 8 HOH   118 518 628 HOH   HOH D . 
WA 8 HOH   119 519 129 HOH   HOH D . 
WA 8 HOH   120 520 566 HOH   HOH D . 
WA 8 HOH   121 521 291 HOH   HOH D . 
WA 8 HOH   122 522 82  HOH   HOH D . 
WA 8 HOH   123 523 582 HOH   HOH D . 
WA 8 HOH   124 524 397 HOH   HOH D . 
WA 8 HOH   125 525 182 HOH   HOH D . 
WA 8 HOH   126 526 281 HOH   HOH D . 
WA 8 HOH   127 527 615 HOH   HOH D . 
WA 8 HOH   128 528 590 HOH   HOH D . 
WA 8 HOH   129 529 580 HOH   HOH D . 
WA 8 HOH   130 530 565 HOH   HOH D . 
WA 8 HOH   131 531 421 HOH   HOH D . 
WA 8 HOH   132 532 413 HOH   HOH D . 
WA 8 HOH   133 533 401 HOH   HOH D . 
WA 8 HOH   134 534 400 HOH   HOH D . 
WA 8 HOH   135 535 447 HOH   HOH D . 
WA 8 HOH   136 536 475 HOH   HOH D . 
WA 8 HOH   137 537 88  HOH   HOH D . 
WA 8 HOH   138 538 102 HOH   HOH D . 
WA 8 HOH   139 539 399 HOH   HOH D . 
WA 8 HOH   140 540 465 HOH   HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A LYS 26  ? NZ  ? A LYS 11  NZ  
2  1 Y 0 A ASP 151 ? CG  B A ASP 136 CG  
3  1 Y 0 A ASP 151 ? OD1 B A ASP 136 OD1 
4  1 Y 0 A ASP 151 ? OD2 B A ASP 136 OD2 
5  1 Y 0 A ASN 218 ? CG  ? A ASN 203 CG  
6  1 Y 0 A ASN 218 ? OD1 ? A ASN 203 OD1 
7  1 Y 0 A ASN 218 ? ND2 ? A ASN 203 ND2 
8  1 Y 0 A LYS 258 ? CD  ? A LYS 243 CD  
9  1 Y 0 A LYS 258 ? CE  ? A LYS 243 CE  
10 1 Y 0 A LYS 258 ? NZ  ? A LYS 243 NZ  
11 1 Y 0 B LYS 26  ? NZ  ? B LYS 11  NZ  
12 1 Y 0 B LYS 117 ? CD  ? B LYS 102 CD  
13 1 Y 0 B LYS 117 ? CE  ? B LYS 102 CE  
14 1 Y 0 B LYS 117 ? NZ  ? B LYS 102 NZ  
15 1 Y 0 B ASP 151 ? CG  B B ASP 136 CG  
16 1 Y 0 B ASP 151 ? OD1 B B ASP 136 OD1 
17 1 Y 0 B ASP 151 ? OD2 B B ASP 136 OD2 
18 1 Y 0 B LYS 164 ? NZ  ? B LYS 149 NZ  
19 1 Y 0 B ARG 201 ? NE  ? B ARG 186 NE  
20 1 Y 0 B ARG 201 ? CZ  ? B ARG 186 CZ  
21 1 Y 0 B ARG 201 ? NH1 ? B ARG 186 NH1 
22 1 Y 0 B ARG 201 ? NH2 ? B ARG 186 NH2 
23 1 Y 0 B ASN 218 ? CG  ? B ASN 203 CG  
24 1 Y 0 B ASN 218 ? OD1 ? B ASN 203 OD1 
25 1 Y 0 B ASN 218 ? ND2 ? B ASN 203 ND2 
26 1 Y 0 C THR 133 ? OG1 ? C THR 118 OG1 
27 1 Y 0 C THR 133 ? CG2 ? C THR 118 CG2 
28 1 Y 0 C ARG 201 ? NE  ? C ARG 186 NE  
29 1 Y 0 C ARG 201 ? CZ  ? C ARG 186 CZ  
30 1 Y 0 C ARG 201 ? NH1 ? C ARG 186 NH1 
31 1 Y 0 C ARG 201 ? NH2 ? C ARG 186 NH2 
32 1 Y 0 C ASN 218 ? CG  ? C ASN 203 CG  
33 1 Y 0 C ASN 218 ? OD1 ? C ASN 203 OD1 
34 1 Y 0 C ASN 218 ? ND2 ? C ASN 203 ND2 
35 1 Y 0 C LYS 258 ? CG  ? C LYS 243 CG  
36 1 Y 0 C LYS 258 ? CD  ? C LYS 243 CD  
37 1 Y 0 C LYS 258 ? CE  ? C LYS 243 CE  
38 1 Y 0 C LYS 258 ? NZ  ? C LYS 243 NZ  
39 1 Y 0 D LYS 26  ? CE  ? D LYS 11  CE  
40 1 Y 0 D LYS 26  ? NZ  ? D LYS 11  NZ  
41 1 Y 0 D ASP 151 ? CG  A D ASP 136 CG  
42 1 Y 0 D ASP 151 ? OD1 A D ASP 136 OD1 
43 1 Y 0 D ASP 151 ? OD2 A D ASP 136 OD2 
44 1 Y 0 D LYS 164 ? NZ  ? D LYS 149 NZ  
45 1 Y 0 D LYS 216 ? CE  ? D LYS 201 CE  
46 1 Y 0 D LYS 216 ? NZ  ? D LYS 201 NZ  
47 1 Y 0 D ASN 218 ? CG  ? D ASN 203 CG  
48 1 Y 0 D ASN 218 ? OD1 ? D ASN 203 OD1 
49 1 Y 0 D ASN 218 ? ND2 ? D ASN 203 ND2 
50 1 Y 0 D LYS 258 ? CD  ? D LYS 243 CD  
51 1 Y 0 D LYS 258 ? CE  ? D LYS 243 CE  
52 1 Y 0 D LYS 258 ? NZ  ? D LYS 243 NZ  
# 
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   ? ? ? v.5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .          2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .          3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? v.5.8.0267 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9QFU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.552 
_cell.length_a_esd                 ? 
_cell.length_b                     78.552 
_cell.length_b_esd                 ? 
_cell.length_c                     165.688 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9QFU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                144 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31' 
_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                   9QFU 
_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             2.71 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.55 
_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' 
_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    
;The protein was formulated as a 2 mg/mL solution in 10 mM MES (pH 6.1) and 2M NaCl, and was crystallized from a solution of 0.1 M NaoAc (pH 4.6), 0.2 M ammonium sulfate and 30% PEG 1500
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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         2023-07-23 
_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   0.999 
_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                        'SRS BEAMLINE PX10.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   PX10.1 
_diffrn_source.pdbx_synchrotron_site       SRS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9QFU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.983 
_reflns.d_resolution_low                               62.930 
_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                                     74832 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.64 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.983 
_reflns_shell.d_res_low                                     2.017 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             74832 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.995 
_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                                  ? 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9QFU 
_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                            1.983 
_refine.ls_d_res_low                             62.930 
_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                     74832 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.64 
_refine.ls_percent_reflns_R_free                 5.4 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17907 
_refine.ls_R_factor_R_free                       0.22074 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17677 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_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       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                             ? 
_refine.overall_SU_ML                            ? 
_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                         LAST 
_refine_hist.pdbx_number_atoms_protein        7680 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         336 
_refine_hist.number_atoms_solvent             524 
_refine_hist.number_atoms_total               8540 
_refine_hist.d_res_high                       1.983 
_refine_hist.d_res_low                        62.930 
# 
_struct.entry_id                     9QFU 
_struct.title                        'Human Tryptase beta-2 (hTPSB2) complexed with covalent inhibitor Compound #1' 
_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        9QFU 
_struct_keywords.text            'BETA-TRYPTASE, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 3 ? 
J  N N 4 ? 
K  N N 5 ? 
L  N N 5 ? 
M  N N 5 ? 
N  N N 6 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 6 ? 
S  N N 7 ? 
T  N N 5 ? 
U  N N 3 ? 
V  N N 5 ? 
W  N N 5 ? 
X  N N 2 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 3 ? 
BA N N 3 ? 
CA N N 5 ? 
DA N N 6 ? 
EA N N 3 ? 
FA N N 5 ? 
GA N N 5 ? 
HA N N 5 ? 
IA N N 5 ? 
JA N N 2 ? 
KA N N 3 ? 
LA N N 3 ? 
MA N N 5 ? 
NA N N 3 ? 
OA N N 3 ? 
PA N N 5 ? 
QA N N 4 ? 
RA N N 5 ? 
SA N N 5 ? 
TA N N 8 ? 
UA N N 8 ? 
VA N N 8 ? 
WA N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TRYB2_HUMAN 
_struct_ref.pdbx_db_accession          P20231 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVH
PQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDA
KYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY
VPK
;
_struct_ref.pdbx_align_begin           31 
# 
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 9QFU A 1 ? 243 ? P20231 31 ? 273 ? 16 258 
2 1 9QFU B 1 ? 243 ? P20231 31 ? 273 ? 16 258 
3 1 9QFU C 1 ? 243 ? P20231 31 ? 273 ? 16 258 
4 1 9QFU D 1 ? 243 ? P20231 31 ? 273 ? 16 258 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9QFU HIS A 21  ? UNP P20231 ARG 51  variant  36  1  
1 9QFU GLY A 22  ? UNP P20231 ASP 52  variant  37  2  
1 9QFU PRO A 23  ? UNP P20231 ARG 53  variant  38  3  
1 9QFU LYS A 102 ? UNP P20231 ASN 132 conflict 117 4  
2 9QFU HIS B 21  ? UNP P20231 ARG 51  variant  36  5  
2 9QFU GLY B 22  ? UNP P20231 ASP 52  variant  37  6  
2 9QFU PRO B 23  ? UNP P20231 ARG 53  variant  38  7  
2 9QFU LYS B 102 ? UNP P20231 ASN 132 conflict 117 8  
3 9QFU HIS C 21  ? UNP P20231 ARG 51  variant  36  9  
3 9QFU GLY C 22  ? UNP P20231 ASP 52  variant  37  10 
3 9QFU PRO C 23  ? UNP P20231 ARG 53  variant  38  11 
3 9QFU LYS C 102 ? UNP P20231 ASN 132 conflict 117 12 
4 9QFU HIS D 21  ? UNP P20231 ARG 51  variant  36  13 
4 9QFU GLY D 22  ? UNP P20231 ASP 52  variant  37  14 
4 9QFU PRO D 23  ? UNP P20231 ARG 53  variant  38  15 
4 9QFU LYS D 102 ? UNP P20231 ASN 132 conflict 117 16 
# 
_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 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      
A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         0.9999999999999999 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ALA A 42  ? VAL A 46  ? ALA A 57  VAL A 61  5 ? 5  
HELX_P HELX_P2  AA2 ASP A 52  ? ALA A 54  ? ASP A 67  ALA A 69  5 ? 3  
HELX_P HELX_P3  AA3 GLU A 154 ? LEU A 164 ? GLU A 169 LEU A 179 1 ? 11 
HELX_P HELX_P4  AA4 TYR A 233 ? VAL A 241 ? TYR A 248 VAL A 256 1 ? 9  
HELX_P HELX_P5  AA5 ALA B 42  ? VAL B 46  ? ALA B 57  VAL B 61  5 ? 5  
HELX_P HELX_P6  AA6 ASP B 52  ? ALA B 54  ? ASP B 67  ALA B 69  5 ? 3  
HELX_P HELX_P7  AA7 GLU B 154 ? LEU B 164 ? GLU B 169 LEU B 179 1 ? 11 
HELX_P HELX_P8  AA8 TYR B 233 ? HIS B 239 ? TYR B 248 HIS B 254 1 ? 7  
HELX_P HELX_P9  AA9 ALA C 42  ? VAL C 46  ? ALA C 57  VAL C 61  5 ? 5  
HELX_P HELX_P10 AB1 ASP C 52  ? ALA C 54  ? ASP C 67  ALA C 69  5 ? 3  
HELX_P HELX_P11 AB2 GLU C 154 ? LEU C 164 ? GLU C 169 LEU C 179 1 ? 11 
HELX_P HELX_P12 AB3 TYR C 233 ? HIS C 239 ? TYR C 248 HIS C 254 1 ? 7  
HELX_P HELX_P13 AB4 ALA D 42  ? VAL D 46  ? ALA D 57  VAL D 61  5 ? 5  
HELX_P HELX_P14 AB5 ASP D 52  ? ALA D 54  ? ASP D 67  ALA D 69  5 ? 3  
HELX_P HELX_P15 AB6 GLU D 154 ? LEU D 164 ? GLU D 169 LEU D 179 1 ? 11 
HELX_P HELX_P16 AB7 TYR D 233 ? VAL D 241 ? TYR D 248 VAL D 256 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 29  SG ? ? ? 1_555 A  CYS   45  SG  ? ? A CYS 44  A CYS   60  1_555 ? ? ? ? ? ? ? 2.141 ? ? 
disulf2  disulf ?    ? A CYS 125 SG ? ? ? 1_555 A  CYS   200 SG  ? ? A CYS 140 A CYS   215 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
disulf3  disulf ?    ? A CYS 158 SG A ? ? 1_555 A  CYS   181 SG  A ? A CYS 173 A CYS   196 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
disulf4  disulf ?    ? A CYS 158 SG B ? ? 1_555 A  CYS   181 SG  B ? A CYS 173 A CYS   196 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf5  disulf ?    ? A CYS 190 SG ? ? ? 1_555 A  CYS   218 SG  ? ? A CYS 205 A CYS   233 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
disulf6  disulf ?    ? B CYS 29  SG ? ? ? 1_555 B  CYS   45  SG  ? ? B CYS 44  B CYS   60  1_555 ? ? ? ? ? ? ? 2.157 ? ? 
disulf7  disulf ?    ? B CYS 125 SG ? ? ? 1_555 B  CYS   200 SG  ? ? B CYS 140 B CYS   215 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
disulf8  disulf ?    ? B CYS 158 SG A ? ? 1_555 B  CYS   181 SG  A ? B CYS 173 B CYS   196 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf9  disulf ?    ? B CYS 158 SG B ? ? 1_555 B  CYS   181 SG  B ? B CYS 173 B CYS   196 1_555 ? ? ? ? ? ? ? 1.970 ? ? 
disulf10 disulf ?    ? B CYS 190 SG ? ? ? 1_555 B  CYS   218 SG  ? ? B CYS 205 B CYS   233 1_555 ? ? ? ? ? ? ? 2.145 ? ? 
disulf11 disulf ?    ? C CYS 29  SG ? ? ? 1_555 C  CYS   45  SG  ? ? C CYS 44  C CYS   60  1_555 ? ? ? ? ? ? ? 2.163 ? ? 
disulf12 disulf ?    ? C CYS 125 SG ? ? ? 1_555 C  CYS   200 SG  ? ? C CYS 140 C CYS   215 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf13 disulf ?    ? C CYS 158 SG A ? ? 1_555 C  CYS   181 SG  A ? C CYS 173 C CYS   196 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
disulf14 disulf ?    ? C CYS 190 SG ? ? ? 1_555 C  CYS   218 SG  A ? C CYS 205 C CYS   233 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
disulf15 disulf ?    ? C CYS 190 SG ? ? ? 1_555 C  CYS   218 SG  B ? C CYS 205 C CYS   233 1_555 ? ? ? ? ? ? ? 2.719 ? ? 
disulf16 disulf ?    ? D CYS 29  SG ? ? ? 1_555 D  CYS   45  SG  ? ? D CYS 44  D CYS   60  1_555 ? ? ? ? ? ? ? 2.129 ? ? 
disulf17 disulf ?    ? D CYS 125 SG ? ? ? 1_555 D  CYS   200 SG  ? ? D CYS 140 D CYS   215 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
disulf18 disulf ?    ? D CYS 158 SG A ? ? 1_555 D  CYS   181 SG  A ? D CYS 173 D CYS   196 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
disulf19 disulf ?    ? D CYS 158 SG B ? ? 1_555 D  CYS   181 SG  B ? D CYS 173 D CYS   196 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf20 disulf ?    ? D CYS 190 SG ? ? ? 1_555 D  CYS   218 SG  ? ? D CYS 205 D CYS   233 1_555 ? ? ? ? ? ? ? 2.166 ? ? 
covale1  covale none ? A SER 194 OG ? ? ? 1_555 E  A1I52 .   C12 ? ? A SER 209 A A1I52 301 1_555 ? ? ? ? ? ? ? 1.416 ? ? 
covale2  covale none ? B SER 194 OG ? ? ? 1_555 O  A1I52 .   C12 ? ? B SER 209 B A1I52 301 1_555 ? ? ? ? ? ? ? 1.420 ? ? 
covale3  covale none ? C SER 194 OG ? ? ? 1_555 X  A1I52 .   C12 ? ? C SER 209 C A1I52 301 1_555 ? ? ? ? ? ? ? 1.421 ? ? 
covale4  covale none ? D SER 194 OG ? ? ? 1_555 JA A1I52 .   C12 ? ? D SER 209 D A1I52 301 1_555 ? ? ? ? ? ? ? 1.417 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  A1I52 E  .   ? SER A 194 ? A1I52 A 301 ? 1_555 SER A 209 ? 1_555 C12 OG SER 1 A1I52 None 'Covalent chemical modification' 
2  A1I52 JA .   ? SER D 194 ? A1I52 D 301 ? 1_555 SER D 209 ? 1_555 C12 OG SER 1 A1I52 None 'Covalent chemical modification' 
3  A1I52 O  .   ? SER B 194 ? A1I52 B 301 ? 1_555 SER B 209 ? 1_555 C12 OG SER 1 A1I52 None 'Covalent chemical modification' 
4  A1I52 X  .   ? SER C 194 ? A1I52 C 301 ? 1_555 SER C 209 ? 1_555 C12 OG SER 1 A1I52 None 'Covalent chemical modification' 
5  CYS   A  29  ? CYS A 45  ? CYS   A 44  ? 1_555 CYS A 60  ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
6  CYS   A  125 ? CYS A 200 ? CYS   A 140 ? 1_555 CYS A 215 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
7  CYS   A  158 A CYS A 181 A CYS   A 173 ? 1_555 CYS A 196 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
8  CYS   A  158 B CYS A 181 B CYS   A 173 ? 1_555 CYS A 196 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
9  CYS   A  190 ? CYS A 218 ? CYS   A 205 ? 1_555 CYS A 233 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
10 CYS   B  29  ? CYS B 45  ? CYS   B 44  ? 1_555 CYS B 60  ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
11 CYS   B  125 ? CYS B 200 ? CYS   B 140 ? 1_555 CYS B 215 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
12 CYS   B  158 A CYS B 181 A CYS   B 173 ? 1_555 CYS B 196 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
13 CYS   B  158 B CYS B 181 B CYS   B 173 ? 1_555 CYS B 196 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
14 CYS   B  190 ? CYS B 218 ? CYS   B 205 ? 1_555 CYS B 233 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
15 CYS   C  29  ? CYS C 45  ? CYS   C 44  ? 1_555 CYS C 60  ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
16 CYS   C  125 ? CYS C 200 ? CYS   C 140 ? 1_555 CYS C 215 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
17 CYS   C  158 A CYS C 181 A CYS   C 173 ? 1_555 CYS C 196 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
18 CYS   C  190 ? CYS C 218 A CYS   C 205 ? 1_555 CYS C 233 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
19 CYS   C  190 ? CYS C 218 B CYS   C 205 ? 1_555 CYS C 233 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
20 CYS   D  29  ? CYS D 45  ? CYS   D 44  ? 1_555 CYS D 60  ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
21 CYS   D  125 ? CYS D 200 ? CYS   D 140 ? 1_555 CYS D 215 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
22 CYS   D  158 A CYS D 181 A CYS   D 173 ? 1_555 CYS D 196 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
23 CYS   D  158 B CYS D 181 B CYS   D 173 ? 1_555 CYS D 196 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
24 CYS   D  190 ? CYS D 218 ? CYS   D 205 ? 1_555 CYS D 233 ? 1_555 SG  SG .   . .     None 'Disulfide bridge'               
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 47  A . ? GLY 62  A PRO 48  A ? PRO 63  A 1 11.35 
2 PRO 141 A . ? PRO 156 A PRO 142 A ? PRO 157 A 1 3.01  
3 GLY 47  B . ? GLY 62  B PRO 48  B ? PRO 63  B 1 5.57  
4 PRO 141 B . ? PRO 156 B PRO 142 B ? PRO 157 B 1 1.53  
5 GLY 47  C . ? GLY 62  C PRO 48  C ? PRO 63  C 1 7.07  
6 PRO 141 C . ? PRO 156 C PRO 142 C ? PRO 157 C 1 2.88  
7 GLY 47  D . ? GLY 62  D PRO 48  D ? PRO 63  D 1 9.23  
8 PRO 141 D . ? PRO 156 D PRO 142 D ? PRO 157 D 1 3.46  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 7 ? 
AA3 ? 8 ? 
AA4 ? 7 ? 
AA5 ? 8 ? 
AA6 ? 7 ? 
AA7 ? 8 ? 
AA8 ? 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 
AA1 7 8 ? 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 
AA2 6 7 ? 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 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? 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 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA5 7 8 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA7 6 7 ? anti-parallel 
AA7 7 8 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 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 GLN A 5   ? GLU A 6   ? GLN A 20  GLU A 21  
AA1 2 LYS A 146 ? LYS A 149 ? LYS A 161 LYS A 164 
AA1 3 CYS A 125 ? GLY A 129 ? CYS A 140 GLY A 144 
AA1 4 PRO A 197 ? VAL A 202 ? PRO A 212 VAL A 217 
AA1 5 THR A 205 ? TRP A 214 ? THR A 220 TRP A 229 
AA1 6 GLY A 225 ? ARG A 229 ? GLY A 240 ARG A 244 
AA1 7 MET A 179 ? ALA A 182 ? MET A 194 ALA A 197 
AA1 8 ILE A 152 ? MET A 153 ? ILE A 167 MET A 168 
AA2 1 GLN A 15  ? VAL A 20  ? GLN A 30  VAL A 35  
AA2 2 MET A 26  ? HIS A 35  ? MET A 41  HIS A 50  
AA2 3 TRP A 38  ? THR A 41  ? TRP A 53  THR A 56  
AA2 4 ALA A 93  ? LEU A 97  ? ALA A 108 LEU A 112 
AA2 5 LEU A 72  ? VAL A 79  ? LEU A 87  VAL A 94  
AA2 6 LEU A 56  ? GLN A 59  ? LEU A 71  GLN A 74  
AA2 7 GLN A 15  ? VAL A 20  ? GLN A 30  VAL A 35  
AA3 1 GLN B 5   ? GLU B 6   ? GLN B 20  GLU B 21  
AA3 2 LYS B 146 ? MET B 153 ? LYS B 161 MET B 168 
AA3 3 MET B 179 ? ALA B 182 ? MET B 194 ALA B 197 
AA3 4 GLY B 225 ? ARG B 229 ? GLY B 240 ARG B 244 
AA3 5 THR B 205 ? TRP B 214 ? THR B 220 TRP B 229 
AA3 6 PRO B 197 ? VAL B 202 ? PRO B 212 VAL B 217 
AA3 7 PRO B 124 ? GLY B 129 ? PRO B 139 GLY B 144 
AA3 8 LYS B 146 ? MET B 153 ? LYS B 161 MET B 168 
AA4 1 GLN B 15  ? VAL B 20  ? GLN B 30  VAL B 35  
AA4 2 MET B 26  ? HIS B 35  ? MET B 41  HIS B 50  
AA4 3 TRP B 38  ? THR B 41  ? TRP B 53  THR B 56  
AA4 4 ALA B 93  ? LEU B 97  ? ALA B 108 LEU B 112 
AA4 5 LEU B 72  ? VAL B 79  ? LEU B 87  VAL B 94  
AA4 6 LEU B 56  ? GLN B 59  ? LEU B 71  GLN B 74  
AA4 7 GLN B 15  ? VAL B 20  ? GLN B 30  VAL B 35  
AA5 1 GLN C 5   ? GLU C 6   ? GLN C 20  GLU C 21  
AA5 2 LYS C 146 ? MET C 153 ? LYS C 161 MET C 168 
AA5 3 MET C 179 ? ALA C 182 ? MET C 194 ALA C 197 
AA5 4 GLY C 225 ? ARG C 229 ? GLY C 240 ARG C 244 
AA5 5 THR C 205 ? TRP C 214 ? THR C 220 TRP C 229 
AA5 6 PRO C 197 ? VAL C 202 ? PRO C 212 VAL C 217 
AA5 7 PRO C 124 ? GLY C 129 ? PRO C 139 GLY C 144 
AA5 8 LYS C 146 ? MET C 153 ? LYS C 161 MET C 168 
AA6 1 GLN C 15  ? VAL C 20  ? GLN C 30  VAL C 35  
AA6 2 MET C 26  ? HIS C 35  ? MET C 41  HIS C 50  
AA6 3 TRP C 38  ? THR C 41  ? TRP C 53  THR C 56  
AA6 4 ALA C 93  ? LEU C 97  ? ALA C 108 LEU C 112 
AA6 5 LEU C 72  ? VAL C 79  ? LEU C 87  VAL C 94  
AA6 6 LEU C 56  ? GLN C 59  ? LEU C 71  GLN C 74  
AA6 7 GLN C 15  ? VAL C 20  ? GLN C 30  VAL C 35  
AA7 1 GLN D 5   ? GLU D 6   ? GLN D 20  GLU D 21  
AA7 2 LYS D 146 ? MET D 153 ? LYS D 161 MET D 168 
AA7 3 MET D 179 ? ALA D 182 ? MET D 194 ALA D 197 
AA7 4 GLY D 225 ? ARG D 229 ? GLY D 240 ARG D 244 
AA7 5 THR D 205 ? TRP D 214 ? THR D 220 TRP D 229 
AA7 6 PRO D 197 ? VAL D 202 ? PRO D 212 VAL D 217 
AA7 7 PRO D 124 ? GLY D 129 ? PRO D 139 GLY D 144 
AA7 8 LYS D 146 ? MET D 153 ? LYS D 161 MET D 168 
AA8 1 GLN D 15  ? VAL D 20  ? GLN D 30  VAL D 35  
AA8 2 MET D 26  ? HIS D 35  ? MET D 41  HIS D 50  
AA8 3 TRP D 38  ? THR D 41  ? TRP D 53  THR D 56  
AA8 4 ALA D 93  ? LEU D 97  ? ALA D 108 LEU D 112 
AA8 5 LEU D 72  ? VAL D 79  ? LEU D 87  VAL D 94  
AA8 6 LEU D 56  ? GLN D 59  ? LEU D 71  GLN D 74  
AA8 7 GLN D 15  ? VAL D 20  ? GLN D 30  VAL D 35  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 5   ? N GLN A 20  O GLN A 147 ? O GLN A 162 
AA1 2 3 O LYS A 146 ? O LYS A 161 N GLY A 129 ? N GLY A 144 
AA1 3 4 N TRP A 126 ? N TRP A 141 O VAL A 199 ? O VAL A 214 
AA1 4 5 N VAL A 202 ? N VAL A 217 O THR A 205 ? O THR A 220 
AA1 5 6 N TRP A 214 ? N TRP A 229 O ILE A 226 ? O ILE A 241 
AA1 6 7 O TYR A 227 ? O TYR A 242 N LEU A 180 ? N LEU A 195 
AA1 7 8 O CYS A 181 ? O CYS A 196 N MET A 153 ? N MET A 168 
AA2 1 2 N LEU A 18  ? N LEU A 33  O CYS A 29  ? O CYS A 44  
AA2 2 3 N SER A 32  ? N SER A 47  O LEU A 40  ? O LEU A 55  
AA2 3 4 N VAL A 39  ? N VAL A 54  O LEU A 95  ? O LEU A 110 
AA2 4 5 O LEU A 94  ? O LEU A 109 N ILE A 78  ? N ILE A 93  
AA2 5 6 O LEU A 72  ? O LEU A 87  N VAL A 58  ? N VAL A 73  
AA2 6 7 O ARG A 57  ? O ARG A 72  N ARG A 19  ? N ARG A 34  
AA3 1 2 N GLN B 5   ? N GLN B 20  O GLN B 147 ? O GLN B 162 
AA3 2 3 N MET B 153 ? N MET B 168 O CYS B 181 ? O CYS B 196 
AA3 3 4 N LEU B 180 ? N LEU B 195 O TYR B 227 ? O TYR B 242 
AA3 4 5 O ILE B 226 ? O ILE B 241 N TRP B 214 ? N TRP B 229 
AA3 5 6 O THR B 205 ? O THR B 220 N VAL B 202 ? N VAL B 217 
AA3 6 7 O VAL B 199 ? O VAL B 214 N TRP B 126 ? N TRP B 141 
AA3 7 8 N CYS B 125 ? N CYS B 140 O VAL B 150 ? O VAL B 165 
AA4 1 2 N LEU B 18  ? N LEU B 33  O CYS B 29  ? O CYS B 44  
AA4 2 3 N SER B 32  ? N SER B 47  O LEU B 40  ? O LEU B 55  
AA4 3 4 N VAL B 39  ? N VAL B 54  O LEU B 95  ? O LEU B 110 
AA4 4 5 O LEU B 94  ? O LEU B 109 N ILE B 78  ? N ILE B 93  
AA4 5 6 O LEU B 72  ? O LEU B 87  N VAL B 58  ? N VAL B 73  
AA4 6 7 O ARG B 57  ? O ARG B 72  N ARG B 19  ? N ARG B 34  
AA5 1 2 N GLN C 5   ? N GLN C 20  O GLN C 147 ? O GLN C 162 
AA5 2 3 N MET C 153 ? N MET C 168 O CYS C 181 ? O CYS C 196 
AA5 3 4 N LEU C 180 ? N LEU C 195 O TYR C 227 ? O TYR C 242 
AA5 4 5 O ILE C 226 ? O ILE C 241 N TRP C 214 ? N TRP C 229 
AA5 5 6 O THR C 205 ? O THR C 220 N VAL C 202 ? N VAL C 217 
AA5 6 7 O VAL C 199 ? O VAL C 214 N TRP C 126 ? N TRP C 141 
AA5 7 8 N CYS C 125 ? N CYS C 140 O VAL C 150 ? O VAL C 165 
AA6 1 2 N LEU C 18  ? N LEU C 33  O CYS C 29  ? O CYS C 44  
AA6 2 3 N SER C 32  ? N SER C 47  O LEU C 40  ? O LEU C 55  
AA6 3 4 N VAL C 39  ? N VAL C 54  O LEU C 95  ? O LEU C 110 
AA6 4 5 O LEU C 94  ? O LEU C 109 N ILE C 78  ? N ILE C 93  
AA6 5 6 O LEU C 72  ? O LEU C 87  N VAL C 58  ? N VAL C 73  
AA6 6 7 O ARG C 57  ? O ARG C 72  N ARG C 19  ? N ARG C 34  
AA7 1 2 N GLN D 5   ? N GLN D 20  O GLN D 147 ? O GLN D 162 
AA7 2 3 N MET D 153 ? N MET D 168 O CYS D 181 ? O CYS D 196 
AA7 3 4 N LEU D 180 ? N LEU D 195 O TYR D 227 ? O TYR D 242 
AA7 4 5 O ILE D 226 ? O ILE D 241 N TRP D 214 ? N TRP D 229 
AA7 5 6 O THR D 205 ? O THR D 220 N VAL D 202 ? N VAL D 217 
AA7 6 7 O VAL D 199 ? O VAL D 214 N TRP D 126 ? N TRP D 141 
AA7 7 8 N CYS D 125 ? N CYS D 140 O VAL D 150 ? O VAL D 165 
AA8 1 2 N LEU D 18  ? N LEU D 33  O CYS D 29  ? O CYS D 44  
AA8 2 3 N SER D 32  ? N SER D 47  O LEU D 40  ? O LEU D 55  
AA8 3 4 N VAL D 39  ? N VAL D 54  O LEU D 95  ? O LEU D 110 
AA8 4 5 O GLU D 96  ? O GLU D 111 N SER D 75  ? N SER D 90  
AA8 5 6 O LEU D 72  ? O LEU D 87  N VAL D 58  ? N VAL D 73  
AA8 6 7 O ARG D 57  ? O ARG D 72  N ARG D 19  ? N ARG D 34  
# 
_pdbx_entry_details.entry_id                   9QFU 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O1 B SO4 307 ? ? O B HOH 401 ? ? 1.87 
2 1 O2 A SO4 305 ? ? O A HOH 402 ? ? 2.15 
3 1 O2 C SO4 308 ? ? O C HOH 401 ? ? 2.17 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              72 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              72 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              72 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.07 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.23 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 TYR A 81  ? ? 85.03   -24.97 
2  1 TYR A 81  ? ? 85.03   -25.15 
3  1 TYR A 99  ? ? -135.14 -48.14 
4  1 TYR B 81  ? ? 85.14   -21.21 
5  1 TYR B 81  ? ? 85.14   -21.17 
6  1 TYR B 99  ? ? -134.38 -47.01 
7  1 SER B 228 ? ? -115.20 -71.13 
8  1 TYR C 81  ? ? 86.31   -23.72 
9  1 TYR C 81  ? ? 86.31   -22.43 
10 1 TYR C 99  ? ? -133.42 -48.24 
11 1 TYR D 81  ? ? 84.74   -23.24 
12 1 TYR D 81  ? ? 84.74   -25.22 
13 1 TYR D 99  ? ? -133.76 -48.76 
14 1 PHE D 134 ? ? 54.77   70.16  
15 1 SER D 228 ? ? -118.11 -70.63 
# 
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 
A1I52 C1   C  N N 1   
A1I52 C2   C  N N 2   
A1I52 C3   C  N N 3   
A1I52 C4   C  N S 4   
A1I52 C5   C  N N 5   
A1I52 C6   C  Y N 6   
A1I52 C7   C  Y N 7   
A1I52 C8   C  Y N 8   
A1I52 C11  C  Y N 9   
A1I52 C12  C  N S 10  
A1I52 C15  C  N N 11  
A1I52 C16  C  Y N 12  
A1I52 C17  C  Y N 13  
A1I52 C18  C  Y N 14  
A1I52 C19  C  Y N 15  
A1I52 C21  C  N N 16  
A1I52 C23  C  Y N 17  
A1I52 C24  C  Y N 18  
A1I52 C27  C  Y N 19  
A1I52 N    N  N N 20  
A1I52 C    C  N N 21  
A1I52 O    O  N N 22  
A1I52 CL   CL N N 23  
A1I52 CL1  CL N N 24  
A1I52 N1   N  N N 25  
A1I52 O1   O  N N 26  
A1I52 N2   N  Y N 27  
A1I52 O2   O  Y N 28  
A1I52 N3   N  Y N 29  
A1I52 O3   O  N N 30  
A1I52 C9   C  Y N 31  
A1I52 C10  C  Y N 32  
A1I52 C13  C  Y N 33  
A1I52 C14  C  Y N 34  
A1I52 C20  C  N N 35  
A1I52 C22  C  Y N 36  
A1I52 C25  C  Y N 37  
A1I52 C26  C  Y N 38  
A1I52 C28  C  Y N 39  
A1I52 C29  C  Y N 40  
A1I52 F    F  N N 41  
A1I52 H1   H  N N 42  
A1I52 H2   H  N N 43  
A1I52 H3   H  N N 44  
A1I52 H4   H  N N 45  
A1I52 H5   H  N N 46  
A1I52 H6   H  N N 47  
A1I52 H7   H  N N 48  
A1I52 H8   H  N N 49  
A1I52 H9   H  N N 50  
A1I52 H10  H  N N 51  
A1I52 H11  H  N N 52  
A1I52 H12  H  N N 53  
A1I52 H13  H  N N 54  
A1I52 H14  H  N N 55  
A1I52 H15  H  N N 56  
A1I52 H16  H  N N 57  
A1I52 H17  H  N N 58  
A1I52 H18  H  N N 59  
A1I52 H19  H  N N 60  
A1I52 H20  H  N N 61  
A1I52 H21  H  N N 62  
A1I52 H22  H  N N 63  
A1I52 H24  H  N N 64  
A1I52 H25  H  N N 65  
A1I52 H26  H  N N 66  
A1I52 H27  H  N N 67  
A1I52 H28  H  N N 68  
A1I52 H29  H  N N 69  
A1I52 H30  H  N N 70  
A1I52 H31  H  N N 71  
A1I52 H32  H  N N 72  
ACT   C    C  N N 73  
ACT   O    O  N N 74  
ACT   OXT  O  N N 75  
ACT   CH3  C  N N 76  
ACT   H1   H  N N 77  
ACT   H2   H  N N 78  
ACT   H3   H  N N 79  
ALA   N    N  N N 80  
ALA   CA   C  N S 81  
ALA   C    C  N N 82  
ALA   O    O  N N 83  
ALA   CB   C  N N 84  
ALA   OXT  O  N N 85  
ALA   H    H  N N 86  
ALA   H2   H  N N 87  
ALA   HA   H  N N 88  
ALA   HB1  H  N N 89  
ALA   HB2  H  N N 90  
ALA   HB3  H  N N 91  
ALA   HXT  H  N N 92  
ARG   N    N  N N 93  
ARG   CA   C  N S 94  
ARG   C    C  N N 95  
ARG   O    O  N N 96  
ARG   CB   C  N N 97  
ARG   CG   C  N N 98  
ARG   CD   C  N N 99  
ARG   NE   N  N N 100 
ARG   CZ   C  N N 101 
ARG   NH1  N  N N 102 
ARG   NH2  N  N N 103 
ARG   OXT  O  N N 104 
ARG   H    H  N N 105 
ARG   H2   H  N N 106 
ARG   HA   H  N N 107 
ARG   HB2  H  N N 108 
ARG   HB3  H  N N 109 
ARG   HG2  H  N N 110 
ARG   HG3  H  N N 111 
ARG   HD2  H  N N 112 
ARG   HD3  H  N N 113 
ARG   HE   H  N N 114 
ARG   HH11 H  N N 115 
ARG   HH12 H  N N 116 
ARG   HH21 H  N N 117 
ARG   HH22 H  N N 118 
ARG   HXT  H  N N 119 
ASN   N    N  N N 120 
ASN   CA   C  N S 121 
ASN   C    C  N N 122 
ASN   O    O  N N 123 
ASN   CB   C  N N 124 
ASN   CG   C  N N 125 
ASN   OD1  O  N N 126 
ASN   ND2  N  N N 127 
ASN   OXT  O  N N 128 
ASN   H    H  N N 129 
ASN   H2   H  N N 130 
ASN   HA   H  N N 131 
ASN   HB2  H  N N 132 
ASN   HB3  H  N N 133 
ASN   HD21 H  N N 134 
ASN   HD22 H  N N 135 
ASN   HXT  H  N N 136 
ASP   N    N  N N 137 
ASP   CA   C  N S 138 
ASP   C    C  N N 139 
ASP   O    O  N N 140 
ASP   CB   C  N N 141 
ASP   CG   C  N N 142 
ASP   OD1  O  N N 143 
ASP   OD2  O  N N 144 
ASP   OXT  O  N N 145 
ASP   H    H  N N 146 
ASP   H2   H  N N 147 
ASP   HA   H  N N 148 
ASP   HB2  H  N N 149 
ASP   HB3  H  N N 150 
ASP   HD2  H  N N 151 
ASP   HXT  H  N N 152 
CYS   N    N  N N 153 
CYS   CA   C  N R 154 
CYS   C    C  N N 155 
CYS   O    O  N N 156 
CYS   CB   C  N N 157 
CYS   SG   S  N N 158 
CYS   OXT  O  N N 159 
CYS   H    H  N N 160 
CYS   H2   H  N N 161 
CYS   HA   H  N N 162 
CYS   HB2  H  N N 163 
CYS   HB3  H  N N 164 
CYS   HG   H  N N 165 
CYS   HXT  H  N N 166 
EDO   C1   C  N N 167 
EDO   O1   O  N N 168 
EDO   C2   C  N N 169 
EDO   O2   O  N N 170 
EDO   H11  H  N N 171 
EDO   H12  H  N N 172 
EDO   HO1  H  N N 173 
EDO   H21  H  N N 174 
EDO   H22  H  N N 175 
EDO   HO2  H  N N 176 
GLN   N    N  N N 177 
GLN   CA   C  N S 178 
GLN   C    C  N N 179 
GLN   O    O  N N 180 
GLN   CB   C  N N 181 
GLN   CG   C  N N 182 
GLN   CD   C  N N 183 
GLN   OE1  O  N N 184 
GLN   NE2  N  N N 185 
GLN   OXT  O  N N 186 
GLN   H    H  N N 187 
GLN   H2   H  N N 188 
GLN   HA   H  N N 189 
GLN   HB2  H  N N 190 
GLN   HB3  H  N N 191 
GLN   HG2  H  N N 192 
GLN   HG3  H  N N 193 
GLN   HE21 H  N N 194 
GLN   HE22 H  N N 195 
GLN   HXT  H  N N 196 
GLU   N    N  N N 197 
GLU   CA   C  N S 198 
GLU   C    C  N N 199 
GLU   O    O  N N 200 
GLU   CB   C  N N 201 
GLU   CG   C  N N 202 
GLU   CD   C  N N 203 
GLU   OE1  O  N N 204 
GLU   OE2  O  N N 205 
GLU   OXT  O  N N 206 
GLU   H    H  N N 207 
GLU   H2   H  N N 208 
GLU   HA   H  N N 209 
GLU   HB2  H  N N 210 
GLU   HB3  H  N N 211 
GLU   HG2  H  N N 212 
GLU   HG3  H  N N 213 
GLU   HE2  H  N N 214 
GLU   HXT  H  N N 215 
GLY   N    N  N N 216 
GLY   CA   C  N N 217 
GLY   C    C  N N 218 
GLY   O    O  N N 219 
GLY   OXT  O  N N 220 
GLY   H    H  N N 221 
GLY   H2   H  N N 222 
GLY   HA2  H  N N 223 
GLY   HA3  H  N N 224 
GLY   HXT  H  N N 225 
GOL   C1   C  N N 226 
GOL   O1   O  N N 227 
GOL   C2   C  N N 228 
GOL   O2   O  N N 229 
GOL   C3   C  N N 230 
GOL   O3   O  N N 231 
GOL   H11  H  N N 232 
GOL   H12  H  N N 233 
GOL   HO1  H  N N 234 
GOL   H2   H  N N 235 
GOL   HO2  H  N N 236 
GOL   H31  H  N N 237 
GOL   H32  H  N N 238 
GOL   HO3  H  N N 239 
HIS   N    N  N N 240 
HIS   CA   C  N S 241 
HIS   C    C  N N 242 
HIS   O    O  N N 243 
HIS   CB   C  N N 244 
HIS   CG   C  Y N 245 
HIS   ND1  N  Y N 246 
HIS   CD2  C  Y N 247 
HIS   CE1  C  Y N 248 
HIS   NE2  N  Y N 249 
HIS   OXT  O  N N 250 
HIS   H    H  N N 251 
HIS   H2   H  N N 252 
HIS   HA   H  N N 253 
HIS   HB2  H  N N 254 
HIS   HB3  H  N N 255 
HIS   HD1  H  N N 256 
HIS   HD2  H  N N 257 
HIS   HE1  H  N N 258 
HIS   HE2  H  N N 259 
HIS   HXT  H  N N 260 
HOH   O    O  N N 261 
HOH   H1   H  N N 262 
HOH   H2   H  N N 263 
ILE   N    N  N N 264 
ILE   CA   C  N S 265 
ILE   C    C  N N 266 
ILE   O    O  N N 267 
ILE   CB   C  N S 268 
ILE   CG1  C  N N 269 
ILE   CG2  C  N N 270 
ILE   CD1  C  N N 271 
ILE   OXT  O  N N 272 
ILE   H    H  N N 273 
ILE   H2   H  N N 274 
ILE   HA   H  N N 275 
ILE   HB   H  N N 276 
ILE   HG12 H  N N 277 
ILE   HG13 H  N N 278 
ILE   HG21 H  N N 279 
ILE   HG22 H  N N 280 
ILE   HG23 H  N N 281 
ILE   HD11 H  N N 282 
ILE   HD12 H  N N 283 
ILE   HD13 H  N N 284 
ILE   HXT  H  N N 285 
LEU   N    N  N N 286 
LEU   CA   C  N S 287 
LEU   C    C  N N 288 
LEU   O    O  N N 289 
LEU   CB   C  N N 290 
LEU   CG   C  N N 291 
LEU   CD1  C  N N 292 
LEU   CD2  C  N N 293 
LEU   OXT  O  N N 294 
LEU   H    H  N N 295 
LEU   H2   H  N N 296 
LEU   HA   H  N N 297 
LEU   HB2  H  N N 298 
LEU   HB3  H  N N 299 
LEU   HG   H  N N 300 
LEU   HD11 H  N N 301 
LEU   HD12 H  N N 302 
LEU   HD13 H  N N 303 
LEU   HD21 H  N N 304 
LEU   HD22 H  N N 305 
LEU   HD23 H  N N 306 
LEU   HXT  H  N N 307 
LYS   N    N  N N 308 
LYS   CA   C  N S 309 
LYS   C    C  N N 310 
LYS   O    O  N N 311 
LYS   CB   C  N N 312 
LYS   CG   C  N N 313 
LYS   CD   C  N N 314 
LYS   CE   C  N N 315 
LYS   NZ   N  N N 316 
LYS   OXT  O  N N 317 
LYS   H    H  N N 318 
LYS   H2   H  N N 319 
LYS   HA   H  N N 320 
LYS   HB2  H  N N 321 
LYS   HB3  H  N N 322 
LYS   HG2  H  N N 323 
LYS   HG3  H  N N 324 
LYS   HD2  H  N N 325 
LYS   HD3  H  N N 326 
LYS   HE2  H  N N 327 
LYS   HE3  H  N N 328 
LYS   HZ1  H  N N 329 
LYS   HZ2  H  N N 330 
LYS   HZ3  H  N N 331 
LYS   HXT  H  N N 332 
MET   N    N  N N 333 
MET   CA   C  N S 334 
MET   C    C  N N 335 
MET   O    O  N N 336 
MET   CB   C  N N 337 
MET   CG   C  N N 338 
MET   SD   S  N N 339 
MET   CE   C  N N 340 
MET   OXT  O  N N 341 
MET   H    H  N N 342 
MET   H2   H  N N 343 
MET   HA   H  N N 344 
MET   HB2  H  N N 345 
MET   HB3  H  N N 346 
MET   HG2  H  N N 347 
MET   HG3  H  N N 348 
MET   HE1  H  N N 349 
MET   HE2  H  N N 350 
MET   HE3  H  N N 351 
MET   HXT  H  N N 352 
PEG   C1   C  N N 353 
PEG   O1   O  N N 354 
PEG   C2   C  N N 355 
PEG   O2   O  N N 356 
PEG   C3   C  N N 357 
PEG   C4   C  N N 358 
PEG   O4   O  N N 359 
PEG   H11  H  N N 360 
PEG   H12  H  N N 361 
PEG   HO1  H  N N 362 
PEG   H21  H  N N 363 
PEG   H22  H  N N 364 
PEG   H31  H  N N 365 
PEG   H32  H  N N 366 
PEG   H41  H  N N 367 
PEG   H42  H  N N 368 
PEG   HO4  H  N N 369 
PHE   N    N  N N 370 
PHE   CA   C  N S 371 
PHE   C    C  N N 372 
PHE   O    O  N N 373 
PHE   CB   C  N N 374 
PHE   CG   C  Y N 375 
PHE   CD1  C  Y N 376 
PHE   CD2  C  Y N 377 
PHE   CE1  C  Y N 378 
PHE   CE2  C  Y N 379 
PHE   CZ   C  Y N 380 
PHE   OXT  O  N N 381 
PHE   H    H  N N 382 
PHE   H2   H  N N 383 
PHE   HA   H  N N 384 
PHE   HB2  H  N N 385 
PHE   HB3  H  N N 386 
PHE   HD1  H  N N 387 
PHE   HD2  H  N N 388 
PHE   HE1  H  N N 389 
PHE   HE2  H  N N 390 
PHE   HZ   H  N N 391 
PHE   HXT  H  N N 392 
PRO   N    N  N N 393 
PRO   CA   C  N S 394 
PRO   C    C  N N 395 
PRO   O    O  N N 396 
PRO   CB   C  N N 397 
PRO   CG   C  N N 398 
PRO   CD   C  N N 399 
PRO   OXT  O  N N 400 
PRO   H    H  N N 401 
PRO   HA   H  N N 402 
PRO   HB2  H  N N 403 
PRO   HB3  H  N N 404 
PRO   HG2  H  N N 405 
PRO   HG3  H  N N 406 
PRO   HD2  H  N N 407 
PRO   HD3  H  N N 408 
PRO   HXT  H  N N 409 
SER   N    N  N N 410 
SER   CA   C  N S 411 
SER   C    C  N N 412 
SER   O    O  N N 413 
SER   CB   C  N N 414 
SER   OG   O  N N 415 
SER   OXT  O  N N 416 
SER   H    H  N N 417 
SER   H2   H  N N 418 
SER   HA   H  N N 419 
SER   HB2  H  N N 420 
SER   HB3  H  N N 421 
SER   HG   H  N N 422 
SER   HXT  H  N N 423 
SO4   S    S  N N 424 
SO4   O1   O  N N 425 
SO4   O2   O  N N 426 
SO4   O3   O  N N 427 
SO4   O4   O  N N 428 
THR   N    N  N N 429 
THR   CA   C  N S 430 
THR   C    C  N N 431 
THR   O    O  N N 432 
THR   CB   C  N R 433 
THR   OG1  O  N N 434 
THR   CG2  C  N N 435 
THR   OXT  O  N N 436 
THR   H    H  N N 437 
THR   H2   H  N N 438 
THR   HA   H  N N 439 
THR   HB   H  N N 440 
THR   HG1  H  N N 441 
THR   HG21 H  N N 442 
THR   HG22 H  N N 443 
THR   HG23 H  N N 444 
THR   HXT  H  N N 445 
TRP   N    N  N N 446 
TRP   CA   C  N S 447 
TRP   C    C  N N 448 
TRP   O    O  N N 449 
TRP   CB   C  N N 450 
TRP   CG   C  Y N 451 
TRP   CD1  C  Y N 452 
TRP   CD2  C  Y N 453 
TRP   NE1  N  Y N 454 
TRP   CE2  C  Y N 455 
TRP   CE3  C  Y N 456 
TRP   CZ2  C  Y N 457 
TRP   CZ3  C  Y N 458 
TRP   CH2  C  Y N 459 
TRP   OXT  O  N N 460 
TRP   H    H  N N 461 
TRP   H2   H  N N 462 
TRP   HA   H  N N 463 
TRP   HB2  H  N N 464 
TRP   HB3  H  N N 465 
TRP   HD1  H  N N 466 
TRP   HE1  H  N N 467 
TRP   HE3  H  N N 468 
TRP   HZ2  H  N N 469 
TRP   HZ3  H  N N 470 
TRP   HH2  H  N N 471 
TRP   HXT  H  N N 472 
TYR   N    N  N N 473 
TYR   CA   C  N S 474 
TYR   C    C  N N 475 
TYR   O    O  N N 476 
TYR   CB   C  N N 477 
TYR   CG   C  Y N 478 
TYR   CD1  C  Y N 479 
TYR   CD2  C  Y N 480 
TYR   CE1  C  Y N 481 
TYR   CE2  C  Y N 482 
TYR   CZ   C  Y N 483 
TYR   OH   O  N N 484 
TYR   OXT  O  N N 485 
TYR   H    H  N N 486 
TYR   H2   H  N N 487 
TYR   HA   H  N N 488 
TYR   HB2  H  N N 489 
TYR   HB3  H  N N 490 
TYR   HD1  H  N N 491 
TYR   HD2  H  N N 492 
TYR   HE1  H  N N 493 
TYR   HE2  H  N N 494 
TYR   HH   H  N N 495 
TYR   HXT  H  N N 496 
VAL   N    N  N N 497 
VAL   CA   C  N S 498 
VAL   C    C  N N 499 
VAL   O    O  N N 500 
VAL   CB   C  N N 501 
VAL   CG1  C  N N 502 
VAL   CG2  C  N N 503 
VAL   OXT  O  N N 504 
VAL   H    H  N N 505 
VAL   H2   H  N N 506 
VAL   HA   H  N N 507 
VAL   HB   H  N N 508 
VAL   HG11 H  N N 509 
VAL   HG12 H  N N 510 
VAL   HG13 H  N N 511 
VAL   HG21 H  N N 512 
VAL   HG22 H  N N 513 
VAL   HG23 H  N N 514 
VAL   HXT  H  N N 515 
# 
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 
A1I52 CL1 C26  sing N N 1   
A1I52 N   C    sing N N 2   
A1I52 CL  C25  sing N N 3   
A1I52 C1  C    sing N N 4   
A1I52 C1  C2   sing N N 5   
A1I52 C26 C25  doub Y N 6   
A1I52 C26 C27  sing Y N 7   
A1I52 C3  C2   sing N N 8   
A1I52 C3  C4   sing N N 9   
A1I52 O1  C12  sing N N 10  
A1I52 C12 C4   sing N N 11  
A1I52 C12 C13  sing N N 12  
A1I52 C25 C24  sing Y N 13  
A1I52 C27 C22  doub Y N 14  
A1I52 C4  N1   sing N N 15  
A1I52 N1  C5   sing N N 16  
A1I52 C13 N3   sing Y N 17  
A1I52 C13 N2   doub Y N 18  
A1I52 N3  C14  doub Y N 19  
A1I52 C24 C23  doub Y N 20  
A1I52 C22 C23  sing Y N 21  
A1I52 C22 C21  sing N N 22  
A1I52 C28 C29  doub Y N 23  
A1I52 C28 C19  sing Y N 24  
A1I52 C11 C10  doub Y N 25  
A1I52 C11 C6   sing Y N 26  
A1I52 C29 C16  sing Y N 27  
A1I52 N2  O2   sing Y N 28  
A1I52 C20 C21  sing N N 29  
A1I52 C20 O3   sing N N 30  
A1I52 C5  C6   sing N N 31  
A1I52 C5  O    doub N N 32  
A1I52 C10 C9   sing Y N 33  
A1I52 C14 O2   sing Y N 34  
A1I52 C14 C15  sing N N 35  
A1I52 C6  C7   doub Y N 36  
A1I52 C19 O3   sing N N 37  
A1I52 C19 C18  doub Y N 38  
A1I52 C16 C15  sing N N 39  
A1I52 C16 C17  doub Y N 40  
A1I52 C9  F    sing N N 41  
A1I52 C9  C8   doub Y N 42  
A1I52 C7  C8   sing Y N 43  
A1I52 C18 C17  sing Y N 44  
A1I52 C1  H1   sing N N 45  
A1I52 C1  H2   sing N N 46  
A1I52 C2  H3   sing N N 47  
A1I52 C2  H4   sing N N 48  
A1I52 C3  H5   sing N N 49  
A1I52 C3  H6   sing N N 50  
A1I52 C4  H7   sing N N 51  
A1I52 C7  H8   sing N N 52  
A1I52 C8  H9   sing N N 53  
A1I52 C11 H10  sing N N 54  
A1I52 C12 H11  sing N N 55  
A1I52 C15 H12  sing N N 56  
A1I52 C15 H13  sing N N 57  
A1I52 C17 H14  sing N N 58  
A1I52 C18 H15  sing N N 59  
A1I52 C21 H16  sing N N 60  
A1I52 C21 H17  sing N N 61  
A1I52 C23 H18  sing N N 62  
A1I52 C24 H19  sing N N 63  
A1I52 C27 H20  sing N N 64  
A1I52 N   H21  sing N N 65  
A1I52 N   H22  sing N N 66  
A1I52 C   H24  sing N N 67  
A1I52 C   H25  sing N N 68  
A1I52 N1  H26  sing N N 69  
A1I52 O1  H27  sing N N 70  
A1I52 C10 H28  sing N N 71  
A1I52 C20 H29  sing N N 72  
A1I52 C20 H30  sing N N 73  
A1I52 C28 H31  sing N N 74  
A1I52 C29 H32  sing N N 75  
ACT   C   O    doub N N 76  
ACT   C   OXT  sing N N 77  
ACT   C   CH3  sing N N 78  
ACT   CH3 H1   sing N N 79  
ACT   CH3 H2   sing N N 80  
ACT   CH3 H3   sing N N 81  
ALA   N   CA   sing N N 82  
ALA   N   H    sing N N 83  
ALA   N   H2   sing N N 84  
ALA   CA  C    sing N N 85  
ALA   CA  CB   sing N N 86  
ALA   CA  HA   sing N N 87  
ALA   C   O    doub N N 88  
ALA   C   OXT  sing N N 89  
ALA   CB  HB1  sing N N 90  
ALA   CB  HB2  sing N N 91  
ALA   CB  HB3  sing N N 92  
ALA   OXT HXT  sing N N 93  
ARG   N   CA   sing N N 94  
ARG   N   H    sing N N 95  
ARG   N   H2   sing N N 96  
ARG   CA  C    sing N N 97  
ARG   CA  CB   sing N N 98  
ARG   CA  HA   sing N N 99  
ARG   C   O    doub N N 100 
ARG   C   OXT  sing N N 101 
ARG   CB  CG   sing N N 102 
ARG   CB  HB2  sing N N 103 
ARG   CB  HB3  sing N N 104 
ARG   CG  CD   sing N N 105 
ARG   CG  HG2  sing N N 106 
ARG   CG  HG3  sing N N 107 
ARG   CD  NE   sing N N 108 
ARG   CD  HD2  sing N N 109 
ARG   CD  HD3  sing N N 110 
ARG   NE  CZ   sing N N 111 
ARG   NE  HE   sing N N 112 
ARG   CZ  NH1  sing N N 113 
ARG   CZ  NH2  doub N N 114 
ARG   NH1 HH11 sing N N 115 
ARG   NH1 HH12 sing N N 116 
ARG   NH2 HH21 sing N N 117 
ARG   NH2 HH22 sing N N 118 
ARG   OXT HXT  sing N N 119 
ASN   N   CA   sing N N 120 
ASN   N   H    sing N N 121 
ASN   N   H2   sing N N 122 
ASN   CA  C    sing N N 123 
ASN   CA  CB   sing N N 124 
ASN   CA  HA   sing N N 125 
ASN   C   O    doub N N 126 
ASN   C   OXT  sing N N 127 
ASN   CB  CG   sing N N 128 
ASN   CB  HB2  sing N N 129 
ASN   CB  HB3  sing N N 130 
ASN   CG  OD1  doub N N 131 
ASN   CG  ND2  sing N N 132 
ASN   ND2 HD21 sing N N 133 
ASN   ND2 HD22 sing N N 134 
ASN   OXT HXT  sing N N 135 
ASP   N   CA   sing N N 136 
ASP   N   H    sing N N 137 
ASP   N   H2   sing N N 138 
ASP   CA  C    sing N N 139 
ASP   CA  CB   sing N N 140 
ASP   CA  HA   sing N N 141 
ASP   C   O    doub N N 142 
ASP   C   OXT  sing N N 143 
ASP   CB  CG   sing N N 144 
ASP   CB  HB2  sing N N 145 
ASP   CB  HB3  sing N N 146 
ASP   CG  OD1  doub N N 147 
ASP   CG  OD2  sing N N 148 
ASP   OD2 HD2  sing N N 149 
ASP   OXT HXT  sing N N 150 
CYS   N   CA   sing N N 151 
CYS   N   H    sing N N 152 
CYS   N   H2   sing N N 153 
CYS   CA  C    sing N N 154 
CYS   CA  CB   sing N N 155 
CYS   CA  HA   sing N N 156 
CYS   C   O    doub N N 157 
CYS   C   OXT  sing N N 158 
CYS   CB  SG   sing N N 159 
CYS   CB  HB2  sing N N 160 
CYS   CB  HB3  sing N N 161 
CYS   SG  HG   sing N N 162 
CYS   OXT HXT  sing N N 163 
EDO   C1  O1   sing N N 164 
EDO   C1  C2   sing N N 165 
EDO   C1  H11  sing N N 166 
EDO   C1  H12  sing N N 167 
EDO   O1  HO1  sing N N 168 
EDO   C2  O2   sing N N 169 
EDO   C2  H21  sing N N 170 
EDO   C2  H22  sing N N 171 
EDO   O2  HO2  sing N N 172 
GLN   N   CA   sing N N 173 
GLN   N   H    sing N N 174 
GLN   N   H2   sing N N 175 
GLN   CA  C    sing N N 176 
GLN   CA  CB   sing N N 177 
GLN   CA  HA   sing N N 178 
GLN   C   O    doub N N 179 
GLN   C   OXT  sing N N 180 
GLN   CB  CG   sing N N 181 
GLN   CB  HB2  sing N N 182 
GLN   CB  HB3  sing N N 183 
GLN   CG  CD   sing N N 184 
GLN   CG  HG2  sing N N 185 
GLN   CG  HG3  sing N N 186 
GLN   CD  OE1  doub N N 187 
GLN   CD  NE2  sing N N 188 
GLN   NE2 HE21 sing N N 189 
GLN   NE2 HE22 sing N N 190 
GLN   OXT HXT  sing N N 191 
GLU   N   CA   sing N N 192 
GLU   N   H    sing N N 193 
GLU   N   H2   sing N N 194 
GLU   CA  C    sing N N 195 
GLU   CA  CB   sing N N 196 
GLU   CA  HA   sing N N 197 
GLU   C   O    doub N N 198 
GLU   C   OXT  sing N N 199 
GLU   CB  CG   sing N N 200 
GLU   CB  HB2  sing N N 201 
GLU   CB  HB3  sing N N 202 
GLU   CG  CD   sing N N 203 
GLU   CG  HG2  sing N N 204 
GLU   CG  HG3  sing N N 205 
GLU   CD  OE1  doub N N 206 
GLU   CD  OE2  sing N N 207 
GLU   OE2 HE2  sing N N 208 
GLU   OXT HXT  sing N N 209 
GLY   N   CA   sing N N 210 
GLY   N   H    sing N N 211 
GLY   N   H2   sing N N 212 
GLY   CA  C    sing N N 213 
GLY   CA  HA2  sing N N 214 
GLY   CA  HA3  sing N N 215 
GLY   C   O    doub N N 216 
GLY   C   OXT  sing N N 217 
GLY   OXT HXT  sing N N 218 
GOL   C1  O1   sing N N 219 
GOL   C1  C2   sing N N 220 
GOL   C1  H11  sing N N 221 
GOL   C1  H12  sing N N 222 
GOL   O1  HO1  sing N N 223 
GOL   C2  O2   sing N N 224 
GOL   C2  C3   sing N N 225 
GOL   C2  H2   sing N N 226 
GOL   O2  HO2  sing N N 227 
GOL   C3  O3   sing N N 228 
GOL   C3  H31  sing N N 229 
GOL   C3  H32  sing N N 230 
GOL   O3  HO3  sing N N 231 
HIS   N   CA   sing N N 232 
HIS   N   H    sing N N 233 
HIS   N   H2   sing N N 234 
HIS   CA  C    sing N N 235 
HIS   CA  CB   sing N N 236 
HIS   CA  HA   sing N N 237 
HIS   C   O    doub N N 238 
HIS   C   OXT  sing N N 239 
HIS   CB  CG   sing N N 240 
HIS   CB  HB2  sing N N 241 
HIS   CB  HB3  sing N N 242 
HIS   CG  ND1  sing Y N 243 
HIS   CG  CD2  doub Y N 244 
HIS   ND1 CE1  doub Y N 245 
HIS   ND1 HD1  sing N N 246 
HIS   CD2 NE2  sing Y N 247 
HIS   CD2 HD2  sing N N 248 
HIS   CE1 NE2  sing Y N 249 
HIS   CE1 HE1  sing N N 250 
HIS   NE2 HE2  sing N N 251 
HIS   OXT HXT  sing N N 252 
HOH   O   H1   sing N N 253 
HOH   O   H2   sing N N 254 
ILE   N   CA   sing N N 255 
ILE   N   H    sing N N 256 
ILE   N   H2   sing N N 257 
ILE   CA  C    sing N N 258 
ILE   CA  CB   sing N N 259 
ILE   CA  HA   sing N N 260 
ILE   C   O    doub N N 261 
ILE   C   OXT  sing N N 262 
ILE   CB  CG1  sing N N 263 
ILE   CB  CG2  sing N N 264 
ILE   CB  HB   sing N N 265 
ILE   CG1 CD1  sing N N 266 
ILE   CG1 HG12 sing N N 267 
ILE   CG1 HG13 sing N N 268 
ILE   CG2 HG21 sing N N 269 
ILE   CG2 HG22 sing N N 270 
ILE   CG2 HG23 sing N N 271 
ILE   CD1 HD11 sing N N 272 
ILE   CD1 HD12 sing N N 273 
ILE   CD1 HD13 sing N N 274 
ILE   OXT HXT  sing N N 275 
LEU   N   CA   sing N N 276 
LEU   N   H    sing N N 277 
LEU   N   H2   sing N N 278 
LEU   CA  C    sing N N 279 
LEU   CA  CB   sing N N 280 
LEU   CA  HA   sing N N 281 
LEU   C   O    doub N N 282 
LEU   C   OXT  sing N N 283 
LEU   CB  CG   sing N N 284 
LEU   CB  HB2  sing N N 285 
LEU   CB  HB3  sing N N 286 
LEU   CG  CD1  sing N N 287 
LEU   CG  CD2  sing N N 288 
LEU   CG  HG   sing N N 289 
LEU   CD1 HD11 sing N N 290 
LEU   CD1 HD12 sing N N 291 
LEU   CD1 HD13 sing N N 292 
LEU   CD2 HD21 sing N N 293 
LEU   CD2 HD22 sing N N 294 
LEU   CD2 HD23 sing N N 295 
LEU   OXT HXT  sing N N 296 
LYS   N   CA   sing N N 297 
LYS   N   H    sing N N 298 
LYS   N   H2   sing N N 299 
LYS   CA  C    sing N N 300 
LYS   CA  CB   sing N N 301 
LYS   CA  HA   sing N N 302 
LYS   C   O    doub N N 303 
LYS   C   OXT  sing N N 304 
LYS   CB  CG   sing N N 305 
LYS   CB  HB2  sing N N 306 
LYS   CB  HB3  sing N N 307 
LYS   CG  CD   sing N N 308 
LYS   CG  HG2  sing N N 309 
LYS   CG  HG3  sing N N 310 
LYS   CD  CE   sing N N 311 
LYS   CD  HD2  sing N N 312 
LYS   CD  HD3  sing N N 313 
LYS   CE  NZ   sing N N 314 
LYS   CE  HE2  sing N N 315 
LYS   CE  HE3  sing N N 316 
LYS   NZ  HZ1  sing N N 317 
LYS   NZ  HZ2  sing N N 318 
LYS   NZ  HZ3  sing N N 319 
LYS   OXT HXT  sing N N 320 
MET   N   CA   sing N N 321 
MET   N   H    sing N N 322 
MET   N   H2   sing N N 323 
MET   CA  C    sing N N 324 
MET   CA  CB   sing N N 325 
MET   CA  HA   sing N N 326 
MET   C   O    doub N N 327 
MET   C   OXT  sing N N 328 
MET   CB  CG   sing N N 329 
MET   CB  HB2  sing N N 330 
MET   CB  HB3  sing N N 331 
MET   CG  SD   sing N N 332 
MET   CG  HG2  sing N N 333 
MET   CG  HG3  sing N N 334 
MET   SD  CE   sing N N 335 
MET   CE  HE1  sing N N 336 
MET   CE  HE2  sing N N 337 
MET   CE  HE3  sing N N 338 
MET   OXT HXT  sing N N 339 
PEG   C1  O1   sing N N 340 
PEG   C1  C2   sing N N 341 
PEG   C1  H11  sing N N 342 
PEG   C1  H12  sing N N 343 
PEG   O1  HO1  sing N N 344 
PEG   C2  O2   sing N N 345 
PEG   C2  H21  sing N N 346 
PEG   C2  H22  sing N N 347 
PEG   O2  C3   sing N N 348 
PEG   C3  C4   sing N N 349 
PEG   C3  H31  sing N N 350 
PEG   C3  H32  sing N N 351 
PEG   C4  O4   sing N N 352 
PEG   C4  H41  sing N N 353 
PEG   C4  H42  sing N N 354 
PEG   O4  HO4  sing N N 355 
PHE   N   CA   sing N N 356 
PHE   N   H    sing N N 357 
PHE   N   H2   sing N N 358 
PHE   CA  C    sing N N 359 
PHE   CA  CB   sing N N 360 
PHE   CA  HA   sing N N 361 
PHE   C   O    doub N N 362 
PHE   C   OXT  sing N N 363 
PHE   CB  CG   sing N N 364 
PHE   CB  HB2  sing N N 365 
PHE   CB  HB3  sing N N 366 
PHE   CG  CD1  doub Y N 367 
PHE   CG  CD2  sing Y N 368 
PHE   CD1 CE1  sing Y N 369 
PHE   CD1 HD1  sing N N 370 
PHE   CD2 CE2  doub Y N 371 
PHE   CD2 HD2  sing N N 372 
PHE   CE1 CZ   doub Y N 373 
PHE   CE1 HE1  sing N N 374 
PHE   CE2 CZ   sing Y N 375 
PHE   CE2 HE2  sing N N 376 
PHE   CZ  HZ   sing N N 377 
PHE   OXT HXT  sing N N 378 
PRO   N   CA   sing N N 379 
PRO   N   CD   sing N N 380 
PRO   N   H    sing N N 381 
PRO   CA  C    sing N N 382 
PRO   CA  CB   sing N N 383 
PRO   CA  HA   sing N N 384 
PRO   C   O    doub N N 385 
PRO   C   OXT  sing N N 386 
PRO   CB  CG   sing N N 387 
PRO   CB  HB2  sing N N 388 
PRO   CB  HB3  sing N N 389 
PRO   CG  CD   sing N N 390 
PRO   CG  HG2  sing N N 391 
PRO   CG  HG3  sing N N 392 
PRO   CD  HD2  sing N N 393 
PRO   CD  HD3  sing N N 394 
PRO   OXT HXT  sing N N 395 
SER   N   CA   sing N N 396 
SER   N   H    sing N N 397 
SER   N   H2   sing N N 398 
SER   CA  C    sing N N 399 
SER   CA  CB   sing N N 400 
SER   CA  HA   sing N N 401 
SER   C   O    doub N N 402 
SER   C   OXT  sing N N 403 
SER   CB  OG   sing N N 404 
SER   CB  HB2  sing N N 405 
SER   CB  HB3  sing N N 406 
SER   OG  HG   sing N N 407 
SER   OXT HXT  sing N N 408 
SO4   S   O1   doub N N 409 
SO4   S   O2   doub N N 410 
SO4   S   O3   sing N N 411 
SO4   S   O4   sing N N 412 
THR   N   CA   sing N N 413 
THR   N   H    sing N N 414 
THR   N   H2   sing N N 415 
THR   CA  C    sing N N 416 
THR   CA  CB   sing N N 417 
THR   CA  HA   sing N N 418 
THR   C   O    doub N N 419 
THR   C   OXT  sing N N 420 
THR   CB  OG1  sing N N 421 
THR   CB  CG2  sing N N 422 
THR   CB  HB   sing N N 423 
THR   OG1 HG1  sing N N 424 
THR   CG2 HG21 sing N N 425 
THR   CG2 HG22 sing N N 426 
THR   CG2 HG23 sing N N 427 
THR   OXT HXT  sing N N 428 
TRP   N   CA   sing N N 429 
TRP   N   H    sing N N 430 
TRP   N   H2   sing N N 431 
TRP   CA  C    sing N N 432 
TRP   CA  CB   sing N N 433 
TRP   CA  HA   sing N N 434 
TRP   C   O    doub N N 435 
TRP   C   OXT  sing N N 436 
TRP   CB  CG   sing N N 437 
TRP   CB  HB2  sing N N 438 
TRP   CB  HB3  sing N N 439 
TRP   CG  CD1  doub Y N 440 
TRP   CG  CD2  sing Y N 441 
TRP   CD1 NE1  sing Y N 442 
TRP   CD1 HD1  sing N N 443 
TRP   CD2 CE2  doub Y N 444 
TRP   CD2 CE3  sing Y N 445 
TRP   NE1 CE2  sing Y N 446 
TRP   NE1 HE1  sing N N 447 
TRP   CE2 CZ2  sing Y N 448 
TRP   CE3 CZ3  doub Y N 449 
TRP   CE3 HE3  sing N N 450 
TRP   CZ2 CH2  doub Y N 451 
TRP   CZ2 HZ2  sing N N 452 
TRP   CZ3 CH2  sing Y N 453 
TRP   CZ3 HZ3  sing N N 454 
TRP   CH2 HH2  sing N N 455 
TRP   OXT HXT  sing N N 456 
TYR   N   CA   sing N N 457 
TYR   N   H    sing N N 458 
TYR   N   H2   sing N N 459 
TYR   CA  C    sing N N 460 
TYR   CA  CB   sing N N 461 
TYR   CA  HA   sing N N 462 
TYR   C   O    doub N N 463 
TYR   C   OXT  sing N N 464 
TYR   CB  CG   sing N N 465 
TYR   CB  HB2  sing N N 466 
TYR   CB  HB3  sing N N 467 
TYR   CG  CD1  doub Y N 468 
TYR   CG  CD2  sing Y N 469 
TYR   CD1 CE1  sing Y N 470 
TYR   CD1 HD1  sing N N 471 
TYR   CD2 CE2  doub Y N 472 
TYR   CD2 HD2  sing N N 473 
TYR   CE1 CZ   doub Y N 474 
TYR   CE1 HE1  sing N N 475 
TYR   CE2 CZ   sing Y N 476 
TYR   CE2 HE2  sing N N 477 
TYR   CZ  OH   sing N N 478 
TYR   OH  HH   sing N N 479 
TYR   OXT HXT  sing N N 480 
VAL   N   CA   sing N N 481 
VAL   N   H    sing N N 482 
VAL   N   H2   sing N N 483 
VAL   CA  C    sing N N 484 
VAL   CA  CB   sing N N 485 
VAL   CA  HA   sing N N 486 
VAL   C   O    doub N N 487 
VAL   C   OXT  sing N N 488 
VAL   CB  CG1  sing N N 489 
VAL   CB  CG2  sing N N 490 
VAL   CB  HB   sing N N 491 
VAL   CG1 HG11 sing N N 492 
VAL   CG1 HG12 sing N N 493 
VAL   CG1 HG13 sing N N 494 
VAL   CG2 HG21 sing N N 495 
VAL   CG2 HG22 sing N N 496 
VAL   CG2 HG23 sing N N 497 
VAL   OXT HXT  sing N N 498 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2GDD 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9QFU 
_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]   0.012730 
_atom_sites.fract_transf_matrix[1][2]   0.007350 
_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]   0.014700 
_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]   0.006035 
_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  
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ILE   A  1 1   ? 24.409  -25.112 -20.428 1.00 25.18  0  16  ILE   A N   1 
ATOM   2    C  CA  . ILE   A  1 1   ? 25.644  -25.491 -21.178 1.00 26.13  0  16  ILE   A CA  1 
ATOM   3    C  C   . ILE   A  1 1   ? 26.882  -25.188 -20.311 1.00 27.23  0  16  ILE   A C   1 
ATOM   4    O  O   . ILE   A  1 1   ? 27.038  -24.019 -19.841 1.00 25.85  0  16  ILE   A O   1 
ATOM   5    C  CB  . ILE   A  1 1   ? 25.667  -24.773 -22.548 1.00 26.33  0  16  ILE   A CB  1 
ATOM   6    C  CG1 . ILE   A  1 1   ? 24.505  -25.194 -23.457 1.00 26.23  0  16  ILE   A CG1 1 
ATOM   7    C  CG2 . ILE   A  1 1   ? 27.011  -24.907 -23.240 1.00 27.74  0  16  ILE   A CG2 1 
ATOM   8    C  CD1 . ILE   A  1 1   ? 24.634  -26.569 -24.090 1.00 25.66  0  16  ILE   A CD1 1 
ATOM   9    N  N   . VAL   A  1 2   ? 27.771  -26.175 -20.156 1.00 27.65  0  17  VAL   A N   1 
ATOM   10   C  CA  . VAL   A  1 2   ? 29.074  -26.008 -19.450 1.00 29.09  0  17  VAL   A CA  1 
ATOM   11   C  C   . VAL   A  1 2   ? 30.168  -25.770 -20.485 1.00 27.25  0  17  VAL   A C   1 
ATOM   12   O  O   . VAL   A  1 2   ? 30.276  -26.563 -21.428 1.00 29.15  0  17  VAL   A O   1 
ATOM   13   C  CB  . VAL   A  1 2   ? 29.419  -27.218 -18.572 1.00 32.15  0  17  VAL   A CB  1 
ATOM   14   C  CG1 . VAL   A  1 2   ? 30.663  -26.941 -17.758 1.00 32.65  0  17  VAL   A CG1 1 
ATOM   15   C  CG2 . VAL   A  1 2   ? 28.253  -27.668 -17.679 1.00 32.72  0  17  VAL   A CG2 1 
ATOM   16   N  N   . GLY   A  1 3   ? 31.029  -24.771 -20.264 1.00 32.42  0  18  GLY   A N   1 
ATOM   17   C  CA  . GLY   A  1 3   ? 32.050  -24.337 -21.250 1.00 29.61  0  18  GLY   A CA  1 
ATOM   18   C  C   . GLY   A  1 3   ? 31.391  -23.630 -22.429 1.00 32.98  0  18  GLY   A C   1 
ATOM   19   O  O   . GLY   A  1 3   ? 30.212  -23.233 -22.335 1.00 35.92  0  18  GLY   A O   1 
ATOM   20   N  N   . GLY   A  1 4   ? 32.089  -23.459 -23.542 1.00 36.48  0  19  GLY   A N   1 
ATOM   21   C  CA  . GLY   A  1 4   ? 31.488  -22.873 -24.768 1.00 39.44  0  19  GLY   A CA  1 
ATOM   22   C  C   . GLY   A  1 4   ? 31.216  -21.382 -24.620 1.00 38.54  0  19  GLY   A C   1 
ATOM   23   O  O   . GLY   A  1 4   ? 31.915  -20.759 -23.826 1.00 42.95  0  19  GLY   A O   1 
ATOM   24   N  N   . GLN   A  1 5   ? 30.204  -20.855 -25.307 1.00 32.37  0  20  GLN   A N   1 
ATOM   25   C  CA  . GLN   A  1 5   ? 30.005  -19.398 -25.465 1.00 36.14  0  20  GLN   A CA  1 
ATOM   26   C  C   . GLN   A  1 5   ? 28.560  -19.123 -25.870 1.00 34.46  0  20  GLN   A C   1 
ATOM   27   O  O   . GLN   A  1 5   ? 27.835  -20.068 -26.262 1.00 29.39  0  20  GLN   A O   1 
ATOM   28   C  CB  . GLN   A  1 5   ? 30.953  -18.884 -26.548 1.00 44.00  0  20  GLN   A CB  1 
ATOM   29   C  CG  . GLN   A  1 5   ? 30.885  -19.732 -27.816 1.00 51.07  0  20  GLN   A CG  1 
ATOM   30   C  CD  . GLN   A  1 5   ? 31.956  -19.409 -28.826 1.00 58.22  0  20  GLN   A CD  1 
ATOM   31   O  OE1 . GLN   A  1 5   ? 32.271  -18.247 -29.066 1.00 63.32  0  20  GLN   A OE1 1 
ATOM   32   N  NE2 . GLN   A  1 5   ? 32.502  -20.437 -29.453 1.00 62.23  0  20  GLN   A NE2 1 
ATOM   33   N  N   . GLU   A  1 6   ? 28.195  -17.851 -25.835 1.00 28.67  0  21  GLU   A N   1 
ATOM   34   C  CA  . GLU   A  1 6   ? 26.926  -17.349 -26.378 1.00 32.77  0  21  GLU   A CA  1 
ATOM   35   C  C   . GLU   A  1 6   ? 26.926  -17.676 -27.869 1.00 29.42  0  21  GLU   A C   1 
ATOM   36   O  O   . GLU   A  1 6   ? 27.938  -17.469 -28.491 1.00 33.12  0  21  GLU   A O   1 
ATOM   37   C  CB  . GLU   A  1 6   ? 26.809  -15.850 -26.108 1.00 34.92  0  21  GLU   A CB  1 
ATOM   38   C  CG  . GLU   A  1 6   ? 25.726  -15.167 -26.936 1.00 41.63  0  21  GLU   A CG  1 
ATOM   39   C  CD  . GLU   A  1 6   ? 25.147  -13.892 -26.310 1.00 47.07  0  21  GLU   A CD  1 
ATOM   40   O  OE1 . GLU   A  1 6   ? 25.783  -13.394 -25.304 1.00 42.94  0  21  GLU   A OE1 1 
ATOM   41   O  OE2 . GLU   A  1 6   ? 24.052  -13.394 -26.819 1.00 36.97  -1 21  GLU   A OE2 1 
ATOM   42   N  N   . ALA   A  1 7   ? 25.811  -18.148 -28.395 1.00 29.86  0  22  ALA   A N   1 
ATOM   43   C  CA  . ALA   A  1 7   ? 25.648  -18.513 -29.823 1.00 32.72  0  22  ALA   A CA  1 
ATOM   44   C  C   . ALA   A  1 7   ? 25.515  -17.241 -30.644 1.00 31.99  0  22  ALA   A C   1 
ATOM   45   O  O   . ALA   A  1 7   ? 24.806  -16.352 -30.217 1.00 32.27  0  22  ALA   A O   1 
ATOM   46   C  CB  . ALA   A  1 7   ? 24.415  -19.357 -30.031 1.00 31.14  0  22  ALA   A CB  1 
ATOM   47   N  N   . PRO   A  1 8   ? 26.159  -17.131 -31.821 1.00 35.07  0  23  PRO   A N   1 
ATOM   48   C  CA  . PRO   A  1 8   ? 25.781  -16.108 -32.798 1.00 36.27  0  23  PRO   A CA  1 
ATOM   49   C  C   . PRO   A  1 8   ? 24.287  -16.235 -33.147 1.00 34.31  0  23  PRO   A C   1 
ATOM   50   O  O   . PRO   A  1 8   ? 23.776  -17.348 -33.185 1.00 30.50  0  23  PRO   A O   1 
ATOM   51   C  CB  . PRO   A  1 8   ? 26.657  -16.398 -34.028 1.00 37.27  0  23  PRO   A CB  1 
ATOM   52   C  CG  . PRO   A  1 8   ? 27.811  -17.262 -33.506 1.00 37.56  0  23  PRO   A CG  1 
ATOM   53   C  CD  . PRO   A  1 8   ? 27.262  -17.990 -32.293 1.00 38.40  0  23  PRO   A CD  1 
ATOM   54   N  N   . ARG   A  1 9   ? 23.639  -15.098 -33.419 1.00 34.88  0  24  ARG   A N   1 
ATOM   55   C  CA  . ARG   A  1 9   ? 22.201  -14.970 -33.790 1.00 37.58  0  24  ARG   A CA  1 
ATOM   56   C  C   . ARG   A  1 9   ? 21.851  -15.841 -34.997 1.00 31.62  0  24  ARG   A C   1 
ATOM   57   O  O   . ARG   A  1 9   ? 20.735  -16.340 -35.024 1.00 32.08  0  24  ARG   A O   1 
ATOM   58   C  CB  . ARG   A  1 9   ? 21.836  -13.511 -34.085 1.00 39.88  0  24  ARG   A CB  1 
ATOM   59   C  CG  . ARG   A  1 9   ? 21.956  -12.630 -32.854 1.00 48.76  0  24  ARG   A CG  1 
ATOM   60   C  CD  . ARG   A  1 9   ? 21.617  -11.158 -33.047 1.00 53.13  0  24  ARG   A CD  1 
ATOM   61   N  NE  . ARG   A  1 9   ? 21.287  -10.579 -31.747 1.00 53.68  0  24  ARG   A NE  1 
ATOM   62   C  CZ  . ARG   A  1 9   ? 20.075  -10.604 -31.163 1.00 50.64  0  24  ARG   A CZ  1 
ATOM   63   N  NH1 . ARG   A  1 9   ? 19.025  -11.169 -31.750 1.00 44.03  1  24  ARG   A NH1 1 
ATOM   64   N  NH2 . ARG   A  1 9   ? 19.927  -10.068 -29.961 1.00 57.05  0  24  ARG   A NH2 1 
ATOM   65   N  N   . SER   A  1 10  ? 22.772  -16.001 -35.946 1.00 31.65  0  25  SER   A N   1 
ATOM   66   C  CA  . SER   A  1 10  ? 22.581  -16.769 -37.205 1.00 36.00  0  25  SER   A CA  1 
ATOM   67   C  C   . SER   A  1 10  ? 22.704  -18.290 -37.004 1.00 34.33  0  25  SER   A C   1 
ATOM   68   O  O   . SER   A  1 10  ? 22.419  -19.011 -37.993 1.00 36.58  0  25  SER   A O   1 
ATOM   69   C  CB  . SER   A  1 10  ? 23.562  -16.297 -38.250 1.00 36.52  0  25  SER   A CB  1 
ATOM   70   O  OG  . SER   A  1 10  ? 24.890  -16.543 -37.803 1.00 38.01  0  25  SER   A OG  1 
ATOM   71   N  N   . LYS   A  1 11  ? 23.099  -18.783 -35.819 1.00 34.38  0  26  LYS   A N   1 
ATOM   72   C  CA  . LYS   A  1 11  ? 23.300  -20.244 -35.591 1.00 31.97  0  26  LYS   A CA  1 
ATOM   73   C  C   . LYS   A  1 11  ? 22.101  -20.843 -34.847 1.00 29.74  0  26  LYS   A C   1 
ATOM   74   O  O   . LYS   A  1 11  ? 21.463  -20.152 -34.029 1.00 28.34  0  26  LYS   A O   1 
ATOM   75   C  CB  . LYS   A  1 11  ? 24.622  -20.514 -34.876 1.00 34.26  0  26  LYS   A CB  1 
ATOM   76   C  CG  . LYS   A  1 11  ? 25.869  -20.046 -35.613 1.00 39.94  0  26  LYS   A CG  1 
ATOM   77   C  CD  . LYS   A  1 11  ? 26.326  -20.932 -36.742 1.00 47.30  0  26  LYS   A CD  1 
ATOM   78   C  CE  . LYS   A  1 11  ? 27.677  -20.497 -37.300 1.00 49.11  0  26  LYS   A CE  1 
ATOM   79   N  NZ  . LYS   A  1 11  ? 27.564  -19.236 -38.107 0.00 47.48  1  26  LYS   A NZ  1 
ATOM   80   N  N   . TRP   A  1 12  ? 21.844  -22.125 -35.104 1.00 28.60  0  27  TRP   A N   1 
ATOM   81   C  CA  . TRP   A  1 12  ? 20.864  -22.985 -34.391 1.00 26.81  0  27  TRP   A CA  1 
ATOM   82   C  C   . TRP   A  1 12  ? 19.444  -22.463 -34.577 1.00 25.56  0  27  TRP   A C   1 
ATOM   83   O  O   . TRP   A  1 12  ? 18.748  -22.197 -33.597 1.00 27.94  0  27  TRP   A O   1 
ATOM   84   C  CB  . TRP   A  1 12  ? 21.252  -23.110 -32.915 1.00 25.27  0  27  TRP   A CB  1 
ATOM   85   C  CG  . TRP   A  1 12  ? 22.725  -23.066 -32.659 1.00 23.69  0  27  TRP   A CG  1 
ATOM   86   C  CD1 . TRP   A  1 12  ? 23.380  -22.181 -31.863 1.00 24.20  0  27  TRP   A CD1 1 
ATOM   87   C  CD2 . TRP   A  1 12  ? 23.739  -23.905 -33.241 1.00 25.68  0  27  TRP   A CD2 1 
ATOM   88   N  NE1 . TRP   A  1 12  ? 24.730  -22.404 -31.913 1.00 26.78  0  27  TRP   A NE1 1 
ATOM   89   C  CE2 . TRP   A  1 12  ? 24.982  -23.458 -32.741 1.00 24.92  0  27  TRP   A CE2 1 
ATOM   90   C  CE3 . TRP   A  1 12  ? 23.721  -24.989 -34.133 1.00 25.68  0  27  TRP   A CE3 1 
ATOM   91   C  CZ2 . TRP   A  1 12  ? 26.191  -24.059 -33.099 1.00 25.33  0  27  TRP   A CZ2 1 
ATOM   92   C  CZ3 . TRP   A  1 12  ? 24.922  -25.573 -34.501 1.00 27.06  0  27  TRP   A CZ3 1 
ATOM   93   C  CH2 . TRP   A  1 12  ? 26.131  -25.130 -33.966 1.00 25.03  0  27  TRP   A CH2 1 
ATOM   94   N  N   . PRO   A  1 13  ? 18.962  -22.280 -35.823 1.00 25.74  0  28  PRO   A N   1 
ATOM   95   C  CA  . PRO   A  1 13  ? 17.620  -21.716 -36.050 1.00 27.03  0  28  PRO   A CA  1 
ATOM   96   C  C   . PRO   A  1 13  ? 16.471  -22.659 -35.672 1.00 23.34  0  28  PRO   A C   1 
ATOM   97   O  O   . PRO   A  1 13  ? 15.328  -22.256 -35.670 1.00 22.32  0  28  PRO   A O   1 
ATOM   98   C  CB  . PRO   A  1 13  ? 17.644  -21.420 -37.557 1.00 28.53  0  28  PRO   A CB  1 
ATOM   99   C  CG  . PRO   A  1 13  ? 18.644  -22.411 -38.144 1.00 28.68  0  28  PRO   A CG  1 
ATOM   100  C  CD  . PRO   A  1 13  ? 19.697  -22.498 -37.079 1.00 28.62  0  28  PRO   A CD  1 
ATOM   101  N  N   . TRP   A  1 14  ? 16.810  -23.892 -35.349 1.00 23.95  0  29  TRP   A N   1 
ATOM   102  C  CA  . TRP   A  1 14  ? 15.865  -24.943 -34.892 1.00 23.74  0  29  TRP   A CA  1 
ATOM   103  C  C   . TRP   A  1 14  ? 15.717  -24.988 -33.364 1.00 22.83  0  29  TRP   A C   1 
ATOM   104  O  O   . TRP   A  1 14  ? 14.792  -25.685 -32.904 1.00 24.30  0  29  TRP   A O   1 
ATOM   105  C  CB  . TRP   A  1 14  ? 16.318  -26.289 -35.442 1.00 24.04  0  29  TRP   A CB  1 
ATOM   106  C  CG  . TRP   A  1 14  ? 17.761  -26.540 -35.186 1.00 21.54  0  29  TRP   A CG  1 
ATOM   107  C  CD1 . TRP   A  1 14  ? 18.360  -26.837 -33.997 1.00 21.31  0  29  TRP   A CD1 1 
ATOM   108  C  CD2 . TRP   A  1 14  ? 18.792  -26.512 -36.172 1.00 23.85  0  29  TRP   A CD2 1 
ATOM   109  N  NE1 . TRP   A  1 14  ? 19.703  -27.016 -34.182 1.00 22.69  0  29  TRP   A NE1 1 
ATOM   110  C  CE2 . TRP   A  1 14  ? 19.998  -26.828 -35.504 1.00 22.88  0  29  TRP   A CE2 1 
ATOM   111  C  CE3 . TRP   A  1 14  ? 18.826  -26.227 -37.539 1.00 23.39  0  29  TRP   A CE3 1 
ATOM   112  C  CZ2 . TRP   A  1 14  ? 21.217  -26.863 -36.163 1.00 26.27  0  29  TRP   A CZ2 1 
ATOM   113  C  CZ3 . TRP   A  1 14  ? 20.040  -26.304 -38.191 1.00 25.92  0  29  TRP   A CZ3 1 
ATOM   114  C  CH2 . TRP   A  1 14  ? 21.218  -26.578 -37.501 1.00 23.72  0  29  TRP   A CH2 1 
ATOM   115  N  N   . GLN   A  1 15  ? 16.543  -24.276 -32.590 1.00 24.18  0  30  GLN   A N   1 
ATOM   116  C  CA  . GLN   A  1 15  ? 16.508  -24.383 -31.111 1.00 24.52  0  30  GLN   A CA  1 
ATOM   117  C  C   . GLN   A  1 15  ? 15.149  -23.870 -30.640 1.00 26.64  0  30  GLN   A C   1 
ATOM   118  O  O   . GLN   A  1 15  ? 14.703  -22.811 -31.156 1.00 25.45  0  30  GLN   A O   1 
ATOM   119  C  CB  . GLN   A  1 15  ? 17.652  -23.626 -30.449 1.00 27.82  0  30  GLN   A CB  1 
ATOM   120  C  CG  . GLN   A  1 15  ? 17.603  -23.670 -28.921 1.00 27.82  0  30  GLN   A CG  1 
ATOM   121  C  CD  . GLN   A  1 15  ? 18.111  -24.961 -28.319 1.00 26.54  0  30  GLN   A CD  1 
ATOM   122  O  OE1 . GLN   A  1 15  ? 19.183  -25.448 -28.673 1.00 26.72  0  30  GLN   A OE1 1 
ATOM   123  N  NE2 . GLN   A  1 15  ? 17.387  -25.489 -27.341 1.00 27.39  0  30  GLN   A NE2 1 
ATOM   124  N  N   . VAL   A  1 16  ? 14.483  -24.605 -29.745 1.00 24.70  0  31  VAL   A N   1 
ATOM   125  C  CA  . VAL   A  1 16  ? 13.242  -24.124 -29.081 1.00 25.43  0  31  VAL   A CA  1 
ATOM   126  C  C   . VAL   A  1 16  ? 13.384  -24.247 -27.555 1.00 24.85  0  31  VAL   A C   1 
ATOM   127  O  O   . VAL   A  1 16  ? 14.218  -25.026 -27.055 1.00 21.62  0  31  VAL   A O   1 
ATOM   128  C  CB  . VAL   A  1 16  ? 11.966  -24.781 -29.631 1.00 30.40  0  31  VAL   A CB  1 
ATOM   129  C  CG1 . VAL   A  1 16  ? 12.009  -24.997 -31.134 1.00 34.62  0  31  VAL   A CG1 1 
ATOM   130  C  CG2 . VAL   A  1 16  ? 11.583  -26.059 -28.945 1.00 30.47  0  31  VAL   A CG2 1 
ATOM   131  N  N   . SER   A  1 17  ? 12.579  -23.455 -26.857 1.00 24.49  0  32  SER   A N   1 
ATOM   132  C  CA  . SER   A  1 17  ? 12.434  -23.437 -25.381 1.00 24.88  0  32  SER   A CA  1 
ATOM   133  C  C   . SER   A  1 17  ? 11.037  -23.945 -25.048 1.00 23.14  0  32  SER   A C   1 
ATOM   134  O  O   . SER   A  1 17  ? 10.060  -23.441 -25.648 1.00 25.21  0  32  SER   A O   1 
ATOM   135  C  CB  . SER   A  1 17  ? 12.672  -22.025 -24.847 1.00 24.50  0  32  SER   A CB  1 
ATOM   136  O  OG  . SER   A  1 17  ? 12.340  -21.969 -23.480 1.00 27.37  0  32  SER   A OG  1 
ATOM   137  N  N   . LEU   A  1 18  ? 10.924  -24.889 -24.116 1.00 21.93  0  33  LEU   A N   1 
ATOM   138  C  CA  . LEU   A  1 18  ? 9.626   -25.379 -23.602 1.00 21.43  0  33  LEU   A CA  1 
ATOM   139  C  C   . LEU   A  1 18  ? 9.319   -24.583 -22.346 1.00 22.96  0  33  LEU   A C   1 
ATOM   140  O  O   . LEU   A  1 18  ? 10.274  -24.434 -21.492 1.00 21.27  0  33  LEU   A O   1 
ATOM   141  C  CB  . LEU   A  1 18  ? 9.682   -26.877 -23.281 1.00 24.56  0  33  LEU   A CB  1 
ATOM   142  C  CG  . LEU   A  1 18  ? 10.053  -27.816 -24.427 1.00 27.87  0  33  LEU   A CG  1 
ATOM   143  C  CD1 . LEU   A  1 18  ? 9.744   -29.263 -24.055 1.00 27.61  0  33  LEU   A CD1 1 
ATOM   144  C  CD2 . LEU   A  1 18  ? 9.338   -27.429 -25.702 1.00 29.56  0  33  LEU   A CD2 1 
ATOM   145  N  N   . ARG   A  1 19  ? 8.071   -24.126 -22.220 1.00 23.06  0  34  ARG   A N   1 
ATOM   146  C  CA  . ARG   A  1 19  ? 7.651   -23.239 -21.104 1.00 24.84  0  34  ARG   A CA  1 
ATOM   147  C  C   . ARG   A  1 19  ? 6.500   -23.877 -20.327 1.00 24.75  0  34  ARG   A C   1 
ATOM   148  O  O   . ARG   A  1 19  ? 5.543   -24.392 -20.971 1.00 23.15  0  34  ARG   A O   1 
ATOM   149  C  CB  . ARG   A  1 19  ? 7.214   -21.876 -21.637 1.00 22.94  0  34  ARG   A CB  1 
ATOM   150  C  CG  . ARG   A  1 19  ? 8.290   -21.139 -22.433 1.00 23.42  0  34  ARG   A CG  1 
ATOM   151  C  CD  . ARG   A  1 19  ? 9.586   -20.885 -21.697 1.00 25.03  0  34  ARG   A CD  1 
ATOM   152  N  NE  . ARG   A  1 19  ? 10.472  -20.019 -22.504 1.00 23.41  0  34  ARG   A NE  1 
ATOM   153  C  CZ  . ARG   A  1 19  ? 10.261  -18.705 -22.681 1.00 24.52  0  34  ARG   A CZ  1 
ATOM   154  N  NH1 . ARG   A  1 19  ? 9.297   -18.092 -22.028 1.00 21.69  1  34  ARG   A NH1 1 
ATOM   155  N  NH2 . ARG   A  1 19  ? 11.041  -17.996 -23.477 1.00 25.79  0  34  ARG   A NH2 1 
ATOM   156  N  N   . VAL   A  1 20  ? 6.573   -23.787 -18.986 1.00 25.71  0  35  VAL   A N   1 
ATOM   157  C  CA  . VAL   A  1 20  ? 5.502   -24.258 -18.064 1.00 25.81  0  35  VAL   A CA  1 
ATOM   158  C  C   . VAL   A  1 20  ? 4.825   -23.040 -17.439 1.00 26.57  0  35  VAL   A C   1 
ATOM   159  O  O   . VAL   A  1 20  ? 5.539   -22.087 -17.034 1.00 23.29  0  35  VAL   A O   1 
ATOM   160  C  CB  . VAL   A  1 20  ? 6.067   -25.211 -16.994 1.00 27.69  0  35  VAL   A CB  1 
ATOM   161  C  CG1 . VAL   A  1 20  ? 7.117   -24.604 -16.076 1.00 26.21  0  35  VAL   A CG1 1 
ATOM   162  C  CG2 . VAL   A  1 20  ? 4.936   -25.794 -16.180 1.00 29.04  0  35  VAL   A CG2 1 
ATOM   163  N  N   . HIS   A  1 21  ? 3.505   -23.088 -17.315 1.00 29.46  0  36  HIS   A N   1 
ATOM   164  C  CA  . HIS   A  1 21  ? 2.676   -22.009 -16.718 1.00 32.43  0  36  HIS   A CA  1 
ATOM   165  C  C   . HIS   A  1 21  ? 3.014   -21.895 -15.225 1.00 35.27  0  36  HIS   A C   1 
ATOM   166  O  O   . HIS   A  1 21  ? 3.119   -22.891 -14.564 1.00 37.21  0  36  HIS   A O   1 
ATOM   167  C  CB  . HIS   A  1 21  ? 1.180   -22.277 -16.921 1.00 40.73  0  36  HIS   A CB  1 
ATOM   168  C  CG  . HIS   A  1 21  ? 0.354   -21.116 -16.480 1.00 54.64  0  36  HIS   A CG  1 
ATOM   169  N  ND1 . HIS   A  1 21  ? 0.136   -20.024 -17.300 1.00 61.89  0  36  HIS   A ND1 1 
ATOM   170  C  CD2 . HIS   A  1 21  ? -0.276  -20.842 -15.314 1.00 61.13  0  36  HIS   A CD2 1 
ATOM   171  C  CE1 . HIS   A  1 21  ? -0.596  -19.130 -16.674 1.00 63.47  0  36  HIS   A CE1 1 
ATOM   172  N  NE2 . HIS   A  1 21  ? -0.847  -19.603 -15.448 1.00 70.41  0  36  HIS   A NE2 1 
ATOM   173  N  N   . GLY   A  1 22  ? 3.251   -20.695 -14.732 1.00 35.46  0  37  GLY   A N   1 
ATOM   174  C  CA  . GLY   A  1 22  ? 3.418   -20.424 -13.297 1.00 36.02  0  37  GLY   A CA  1 
ATOM   175  C  C   . GLY   A  1 22  ? 3.308   -18.929 -13.093 1.00 36.28  0  37  GLY   A C   1 
ATOM   176  O  O   . GLY   A  1 22  ? 2.551   -18.284 -13.819 1.00 34.83  0  37  GLY   A O   1 
ATOM   177  N  N   . PRO   A  1 23  ? 4.060   -18.338 -12.143 1.00 39.53  0  38  PRO   A N   1 
ATOM   178  C  CA  . PRO   A  1 23  ? 4.099   -16.880 -12.005 1.00 38.18  0  38  PRO   A CA  1 
ATOM   179  C  C   . PRO   A  1 23  ? 4.503   -16.223 -13.332 1.00 35.73  0  38  PRO   A C   1 
ATOM   180  O  O   . PRO   A  1 23  ? 4.058   -15.138 -13.629 1.00 40.08  0  38  PRO   A O   1 
ATOM   181  C  CB  . PRO   A  1 23  ? 5.174   -16.612 -10.936 1.00 41.87  0  38  PRO   A CB  1 
ATOM   182  C  CG  . PRO   A  1 23  ? 5.389   -17.938 -10.229 1.00 44.45  0  38  PRO   A CG  1 
ATOM   183  C  CD  . PRO   A  1 23  ? 4.921   -19.029 -11.173 1.00 41.52  0  38  PRO   A CD  1 
ATOM   184  N  N   . TYR   A  1 24  ? 5.326   -16.923 -14.111 1.00 32.62  0  39  TYR   A N   1 
ATOM   185  C  CA  . TYR   A  1 24  ? 5.626   -16.594 -15.527 1.00 30.48  0  39  TYR   A CA  1 
ATOM   186  C  C   . TYR   A  1 24  ? 5.779   -17.897 -16.312 1.00 30.73  0  39  TYR   A C   1 
ATOM   187  O  O   . TYR   A  1 24  ? 5.820   -18.984 -15.681 1.00 25.47  0  39  TYR   A O   1 
ATOM   188  C  CB  . TYR   A  1 24  ? 6.878   -15.715 -15.612 1.00 28.09  0  39  TYR   A CB  1 
ATOM   189  C  CG  . TYR   A  1 24  ? 8.150   -16.365 -15.127 1.00 28.56  0  39  TYR   A CG  1 
ATOM   190  C  CD1 . TYR   A  1 24  ? 8.402   -16.569 -13.770 1.00 30.25  0  39  TYR   A CD1 1 
ATOM   191  C  CD2 . TYR   A  1 24  ? 9.152   -16.690 -16.022 1.00 28.65  0  39  TYR   A CD2 1 
ATOM   192  C  CE1 . TYR   A  1 24  ? 9.621   -17.071 -13.329 1.00 30.52  0  39  TYR   A CE1 1 
ATOM   193  C  CE2 . TYR   A  1 24  ? 10.355  -17.254 -15.607 1.00 28.36  0  39  TYR   A CE2 1 
ATOM   194  C  CZ  . TYR   A  1 24  ? 10.586  -17.451 -14.260 1.00 31.04  0  39  TYR   A CZ  1 
ATOM   195  O  OH  . TYR   A  1 24  ? 11.768  -18.015 -13.883 1.00 31.81  0  39  TYR   A OH  1 
ATOM   196  N  N   . TRP   A  1 25  ? 5.893   -17.771 -17.634 1.00 29.05  0  40  TRP   A N   1 
ATOM   197  C  CA  . TRP   A  1 25  ? 6.111   -18.917 -18.542 1.00 28.26  0  40  TRP   A CA  1 
ATOM   198  C  C   . TRP   A  1 25  ? 7.582   -19.307 -18.488 1.00 27.22  0  40  TRP   A C   1 
ATOM   199  O  O   . TRP   A  1 25  ? 8.370   -18.768 -19.262 1.00 26.57  0  40  TRP   A O   1 
ATOM   200  C  CB  . TRP   A  1 25  ? 5.623   -18.570 -19.946 1.00 29.26  0  40  TRP   A CB  1 
ATOM   201  C  CG  . TRP   A  1 25  ? 4.135   -18.591 -20.028 1.00 28.02  0  40  TRP   A CG  1 
ATOM   202  C  CD1 . TRP   A  1 25  ? 3.308   -17.513 -19.924 1.00 31.36  0  40  TRP   A CD1 1 
ATOM   203  C  CD2 . TRP   A  1 25  ? 3.291   -19.749 -20.149 1.00 28.55  0  40  TRP   A CD2 1 
ATOM   204  N  NE1 . TRP   A  1 25  ? 2.010   -17.919 -20.048 1.00 30.90  0  40  TRP   A NE1 1 
ATOM   205  C  CE2 . TRP   A  1 25  ? 1.959   -19.279 -20.162 1.00 30.09  0  40  TRP   A CE2 1 
ATOM   206  C  CE3 . TRP   A  1 25  ? 3.523   -21.123 -20.321 1.00 28.74  0  40  TRP   A CE3 1 
ATOM   207  C  CZ2 . TRP   A  1 25  ? 0.871   -20.122 -20.350 1.00 30.27  0  40  TRP   A CZ2 1 
ATOM   208  C  CZ3 . TRP   A  1 25  ? 2.444   -21.971 -20.446 1.00 30.50  0  40  TRP   A CZ3 1 
ATOM   209  C  CH2 . TRP   A  1 25  ? 1.136   -21.472 -20.481 1.00 36.58  0  40  TRP   A CH2 1 
ATOM   210  N  N   . MET   A  1 26  ? 7.926   -20.192 -17.569 1.00 27.21  0  41  MET   A N   1 
ATOM   211  C  CA  . MET   A  1 26  ? 9.339   -20.522 -17.231 1.00 29.33  0  41  MET   A CA  1 
ATOM   212  C  C   . MET   A  1 26  ? 9.884   -21.620 -18.175 1.00 26.24  0  41  MET   A C   1 
ATOM   213  O  O   . MET   A  1 26  ? 9.233   -22.625 -18.389 1.00 24.53  0  41  MET   A O   1 
ATOM   214  C  CB  . MET   A  1 26  ? 9.420   -20.974 -15.767 1.00 30.60  0  41  MET   A CB  1 
ATOM   215  C  CG  . MET   A  1 26  ? 10.837  -21.139 -15.240 1.00 35.62  0  41  MET   A CG  1 
ATOM   216  S  SD  . MET   A  1 26  ? 10.937  -21.489 -13.459 1.00 40.11  0  41  MET   A SD  1 
ATOM   217  C  CE  . MET   A  1 26  ? 9.478   -22.491 -13.189 1.00 41.36  0  41  MET   A CE  1 
ATOM   218  N  N   . HIS   A  1 27  ? 11.091  -21.432 -18.682 1.00 26.57  0  42  HIS   A N   1 
ATOM   219  C  CA  . HIS   A  1 27  ? 11.917  -22.448 -19.387 1.00 25.89  0  42  HIS   A CA  1 
ATOM   220  C  C   . HIS   A  1 27  ? 12.209  -23.631 -18.453 1.00 26.66  0  42  HIS   A C   1 
ATOM   221  O  O   . HIS   A  1 27  ? 12.650  -23.408 -17.343 1.00 24.74  0  42  HIS   A O   1 
ATOM   222  C  CB  . HIS   A  1 27  ? 13.212  -21.822 -19.876 1.00 24.45  0  42  HIS   A CB  1 
ATOM   223  C  CG  . HIS   A  1 27  ? 14.122  -22.820 -20.474 1.00 24.76  0  42  HIS   A CG  1 
ATOM   224  N  ND1 . HIS   A  1 27  ? 14.089  -23.135 -21.818 1.00 23.30  0  42  HIS   A ND1 1 
ATOM   225  C  CD2 . HIS   A  1 27  ? 15.038  -23.635 -19.894 1.00 24.49  0  42  HIS   A CD2 1 
ATOM   226  C  CE1 . HIS   A  1 27  ? 15.000  -24.057 -22.043 1.00 25.43  0  42  HIS   A CE1 1 
ATOM   227  N  NE2 . HIS   A  1 27  ? 15.574  -24.397 -20.871 1.00 20.85  0  42  HIS   A NE2 1 
ATOM   228  N  N   . PHE   A  1 28  ? 11.876  -24.847 -18.867 1.00 27.35  0  43  PHE   A N   1 
ATOM   229  C  CA  . PHE   A  1 28  ? 12.220  -26.089 -18.126 1.00 27.56  0  43  PHE   A CA  1 
ATOM   230  C  C   . PHE   A  1 28  ? 12.992  -27.070 -19.024 1.00 28.47  0  43  PHE   A C   1 
ATOM   231  O  O   . PHE   A  1 28  ? 13.694  -27.890 -18.505 1.00 28.31  0  43  PHE   A O   1 
ATOM   232  C  CB  . PHE   A  1 28  ? 10.951  -26.681 -17.509 1.00 25.54  0  43  PHE   A CB  1 
ATOM   233  C  CG  . PHE   A  1 28  ? 9.978   -27.244 -18.508 1.00 26.50  0  43  PHE   A CG  1 
ATOM   234  C  CD1 . PHE   A  1 28  ? 10.063  -28.575 -18.873 1.00 24.83  0  43  PHE   A CD1 1 
ATOM   235  C  CD2 . PHE   A  1 28  ? 8.945   -26.480 -19.025 1.00 25.13  0  43  PHE   A CD2 1 
ATOM   236  C  CE1 . PHE   A  1 28  ? 9.188   -29.102 -19.798 1.00 28.75  0  43  PHE   A CE1 1 
ATOM   237  C  CE2 . PHE   A  1 28  ? 8.052   -27.017 -19.921 1.00 25.86  0  43  PHE   A CE2 1 
ATOM   238  C  CZ  . PHE   A  1 28  ? 8.167   -28.337 -20.306 1.00 29.94  0  43  PHE   A CZ  1 
ATOM   239  N  N   . CYS   A  1 29  ? 12.880  -26.988 -20.345 1.00 30.86  0  44  CYS   A N   1 
ATOM   240  C  CA  . CYS   A  1 29  ? 13.603  -27.887 -21.272 1.00 29.08  0  44  CYS   A CA  1 
ATOM   241  C  C   . CYS   A  1 29  ? 13.769  -27.214 -22.642 1.00 28.10  0  44  CYS   A C   1 
ATOM   242  O  O   . CYS   A  1 29  ? 13.016  -26.270 -22.962 1.00 25.09  0  44  CYS   A O   1 
ATOM   243  C  CB  . CYS   A  1 29  ? 12.843  -29.202 -21.453 1.00 28.61  0  44  CYS   A CB  1 
ATOM   244  S  SG  . CYS   A  1 29  ? 13.121  -30.463 -20.168 1.00 28.15  0  44  CYS   A SG  1 
ATOM   245  N  N   . GLY   A  1 30  ? 14.717  -27.733 -23.405 1.00 20.77  0  45  GLY   A N   1 
ATOM   246  C  CA  . GLY   A  1 30  ? 14.901  -27.492 -24.836 1.00 22.25  0  45  GLY   A CA  1 
ATOM   247  C  C   . GLY   A  1 30  ? 14.122  -28.461 -25.701 1.00 20.60  0  45  GLY   A C   1 
ATOM   248  O  O   . GLY   A  1 30  ? 13.426  -29.365 -25.180 1.00 21.04  0  45  GLY   A O   1 
ATOM   249  N  N   . GLY   A  1 31  ? 14.220  -28.208 -26.988 1.00 21.29  0  46  GLY   A N   1 
ATOM   250  C  CA  . GLY   A  1 31  ? 13.619  -28.956 -28.088 1.00 21.88  0  46  GLY   A CA  1 
ATOM   251  C  C   . GLY   A  1 31  ? 14.224  -28.491 -29.410 1.00 22.41  0  46  GLY   A C   1 
ATOM   252  O  O   . GLY   A  1 31  ? 15.091  -27.553 -29.408 1.00 21.86  0  46  GLY   A O   1 
ATOM   253  N  N   . SER   A  1 32  ? 13.793  -29.098 -30.510 1.00 21.94  0  47  SER   A N   1 
ATOM   254  C  CA  . SER   A  1 32  ? 14.233  -28.741 -31.873 1.00 23.02  0  47  SER   A CA  1 
ATOM   255  C  C   . SER   A  1 32  ? 13.028  -28.791 -32.811 1.00 22.27  0  47  SER   A C   1 
ATOM   256  O  O   . SER   A  1 32  ? 12.124  -29.641 -32.636 1.00 22.09  0  47  SER   A O   1 
ATOM   257  C  CB  . SER   A  1 32  ? 15.399  -29.579 -32.341 1.00 22.85  0  47  SER   A CB  1 
ATOM   258  O  OG  . SER   A  1 32  ? 15.045  -30.945 -32.354 1.00 22.71  0  47  SER   A OG  1 
ATOM   259  N  N   . LEU   A  1 33  ? 12.962  -27.835 -33.717 1.00 22.44  0  48  LEU   A N   1 
ATOM   260  C  CA  . LEU   A  1 33  ? 11.922  -27.813 -34.774 1.00 23.81  0  48  LEU   A CA  1 
ATOM   261  C  C   . LEU   A  1 33  ? 12.358  -28.767 -35.896 1.00 21.13  0  48  LEU   A C   1 
ATOM   262  O  O   . LEU   A  1 33  ? 13.412  -28.574 -36.469 1.00 21.24  0  48  LEU   A O   1 
ATOM   263  C  CB  . LEU   A  1 33  ? 11.755  -26.369 -35.253 1.00 23.86  0  48  LEU   A CB  1 
ATOM   264  C  CG  . LEU   A  1 33  ? 10.560  -26.132 -36.166 1.00 25.85  0  48  LEU   A CG  1 
ATOM   265  C  CD1 . LEU   A  1 33  ? 9.241   -26.200 -35.413 1.00 23.33  0  48  LEU   A CD1 1 
ATOM   266  C  CD2 . LEU   A  1 33  ? 10.716  -24.802 -36.907 1.00 28.10  0  48  LEU   A CD2 1 
ATOM   267  N  N   . ILE   A  1 34  ? 11.649  -29.875 -36.061 1.00 25.62  0  49  ILE   A N   1 
ATOM   268  C  CA  . ILE   A  1 34  ? 12.004  -30.914 -37.088 1.00 25.55  0  49  ILE   A CA  1 
ATOM   269  C  C   . ILE   A  1 34  ? 11.006  -30.842 -38.259 1.00 25.31  0  49  ILE   A C   1 
ATOM   270  O  O   . ILE   A  1 34  ? 11.165  -31.567 -39.208 1.00 23.93  0  49  ILE   A O   1 
ATOM   271  C  CB  . ILE   A  1 34  ? 12.058  -32.307 -36.435 1.00 24.26  0  49  ILE   A CB  1 
ATOM   272  C  CG1 . ILE   A  1 34  ? 10.752  -32.685 -35.751 1.00 25.37  0  49  ILE   A CG1 1 
ATOM   273  C  CG2 . ILE   A  1 34  ? 13.222  -32.414 -35.473 1.00 25.05  0  49  ILE   A CG2 1 
ATOM   274  C  CD1 . ILE   A  1 34  ? 10.540  -34.192 -35.696 1.00 26.45  0  49  ILE   A CD1 1 
ATOM   275  N  N   . HIS   A  1 35  ? 9.946   -30.053 -38.124 1.00 28.30  0  50  HIS   A N   1 
ATOM   276  C  CA  . HIS   A  1 35  ? 8.857   -29.894 -39.111 1.00 27.69  0  50  HIS   A CA  1 
ATOM   277  C  C   . HIS   A  1 35  ? 8.125   -28.634 -38.694 1.00 26.72  0  50  HIS   A C   1 
ATOM   278  O  O   . HIS   A  1 35  ? 8.111   -28.333 -37.517 1.00 25.75  0  50  HIS   A O   1 
ATOM   279  C  CB  . HIS   A  1 35  ? 7.953   -31.133 -39.169 1.00 29.85  0  50  HIS   A CB  1 
ATOM   280  C  CG  . HIS   A  1 35  ? 6.874   -31.049 -40.196 1.00 32.17  0  50  HIS   A CG  1 
ATOM   281  N  ND1 . HIS   A  1 35  ? 5.681   -30.338 -39.976 1.00 27.09  0  50  HIS   A ND1 1 
ATOM   282  C  CD2 . HIS   A  1 35  ? 6.791   -31.601 -41.431 1.00 30.74  0  50  HIS   A CD2 1 
ATOM   283  C  CE1 . HIS   A  1 35  ? 4.907   -30.469 -41.042 1.00 31.98  0  50  HIS   A CE1 1 
ATOM   284  N  NE2 . HIS   A  1 35  ? 5.576   -31.249 -41.957 1.00 29.77  0  50  HIS   A NE2 1 
ATOM   285  N  N   . PRO   A  1 36  ? 7.559   -27.834 -39.615 1.00 26.17  0  51  PRO   A N   1 
ATOM   286  C  CA  . PRO   A  1 36  ? 6.809   -26.642 -39.226 1.00 26.55  0  51  PRO   A CA  1 
ATOM   287  C  C   . PRO   A  1 36  ? 5.738   -26.809 -38.145 1.00 27.36  0  51  PRO   A C   1 
ATOM   288  O  O   . PRO   A  1 36  ? 5.396   -25.809 -37.513 1.00 30.33  0  51  PRO   A O   1 
ATOM   289  C  CB  . PRO   A  1 36  ? 6.183   -26.223 -40.562 1.00 27.74  0  51  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A  1 36  ? 7.268   -26.571 -41.541 1.00 29.01  0  51  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A  1 36  ? 7.686   -27.956 -41.083 1.00 29.16  0  51  PRO   A CD  1 
ATOM   292  N  N   A GLN   A  1 37  ? 5.216   -28.026 -37.967 0.50 27.60  0  52  GLN   A N   1 
ATOM   293  N  N   B GLN   A  1 37  ? 5.206   -28.016 -37.945 0.50 26.52  0  52  GLN   A N   1 
ATOM   294  C  CA  A GLN   A  1 37  ? 4.170   -28.363 -36.977 0.50 28.23  0  52  GLN   A CA  1 
ATOM   295  C  CA  B GLN   A  1 37  ? 4.198   -28.250 -36.881 0.50 26.38  0  52  GLN   A CA  1 
ATOM   296  C  C   A GLN   A  1 37  ? 4.734   -29.188 -35.807 0.50 27.81  0  52  GLN   A C   1 
ATOM   297  C  C   B GLN   A  1 37  ? 4.730   -29.197 -35.798 0.50 26.79  0  52  GLN   A C   1 
ATOM   298  O  O   A GLN   A  1 37  ? 3.933   -29.512 -34.891 0.50 28.65  0  52  GLN   A O   1 
ATOM   299  O  O   B GLN   A  1 37  ? 3.908   -29.586 -34.919 0.50 27.37  0  52  GLN   A O   1 
ATOM   300  C  CB  A GLN   A  1 37  ? 3.065   -29.176 -37.661 0.50 29.88  0  52  GLN   A CB  1 
ATOM   301  C  CB  B GLN   A  1 37  ? 2.886   -28.750 -37.486 0.50 26.94  0  52  GLN   A CB  1 
ATOM   302  C  CG  A GLN   A  1 37  ? 2.174   -28.345 -38.581 0.50 31.87  0  52  GLN   A CG  1 
ATOM   303  C  CG  B GLN   A  1 37  ? 1.677   -28.379 -36.637 0.50 26.18  0  52  GLN   A CG  1 
ATOM   304  C  CD  A GLN   A  1 37  ? 1.194   -29.175 -39.381 0.50 31.66  0  52  GLN   A CD  1 
ATOM   305  C  CD  B GLN   A  1 37  ? 0.401   -28.257 -37.434 0.50 25.13  0  52  GLN   A CD  1 
ATOM   306  O  OE1 A GLN   A  1 37  ? 0.125   -29.544 -38.914 0.50 37.33  0  52  GLN   A OE1 1 
ATOM   307  O  OE1 B GLN   A  1 37  ? 0.370   -28.503 -38.642 0.50 29.20  0  52  GLN   A OE1 1 
ATOM   308  N  NE2 A GLN   A  1 37  ? 1.539   -29.457 -40.618 0.50 31.90  0  52  GLN   A NE2 1 
ATOM   309  N  NE2 B GLN   A  1 37  ? -0.659  -27.850 -36.762 0.50 21.63  0  52  GLN   A NE2 1 
ATOM   310  N  N   . TRP   A  1 38  ? 6.013   -29.568 -35.821 1.00 25.45  0  53  TRP   A N   1 
ATOM   311  C  CA  . TRP   A  1 38  ? 6.531   -30.587 -34.860 1.00 23.95  0  53  TRP   A CA  1 
ATOM   312  C  C   . TRP   A  1 38  ? 7.826   -30.191 -34.189 1.00 23.19  0  53  TRP   A C   1 
ATOM   313  O  O   . TRP   A  1 38  ? 8.797   -29.787 -34.878 1.00 24.59  0  53  TRP   A O   1 
ATOM   314  C  CB  . TRP   A  1 38  ? 6.666   -31.961 -35.524 1.00 24.00  0  53  TRP   A CB  1 
ATOM   315  C  CG  . TRP   A  1 38  ? 5.362   -32.558 -35.935 1.00 24.05  0  53  TRP   A CG  1 
ATOM   316  C  CD1 . TRP   A  1 38  ? 4.744   -32.386 -37.145 1.00 26.82  0  53  TRP   A CD1 1 
ATOM   317  C  CD2 . TRP   A  1 38  ? 4.511   -33.437 -35.172 1.00 23.60  0  53  TRP   A CD2 1 
ATOM   318  N  NE1 . TRP   A  1 38  ? 3.587   -33.112 -37.184 1.00 25.39  0  53  TRP   A NE1 1 
ATOM   319  C  CE2 . TRP   A  1 38  ? 3.405   -33.754 -35.989 1.00 25.50  0  53  TRP   A CE2 1 
ATOM   320  C  CE3 . TRP   A  1 38  ? 4.575   -34.001 -33.891 1.00 24.99  0  53  TRP   A CE3 1 
ATOM   321  C  CZ2 . TRP   A  1 38  ? 2.387   -34.620 -35.583 1.00 24.96  0  53  TRP   A CZ2 1 
ATOM   322  C  CZ3 . TRP   A  1 38  ? 3.549   -34.822 -33.466 1.00 25.80  0  53  TRP   A CZ3 1 
ATOM   323  C  CH2 . TRP   A  1 38  ? 2.472   -35.123 -34.309 1.00 24.97  0  53  TRP   A CH2 1 
ATOM   324  N  N   . VAL   A  1 39  ? 7.841   -30.388 -32.870 1.00 23.24  0  54  VAL   A N   1 
ATOM   325  C  CA  . VAL   A  1 39  ? 9.040   -30.189 -32.015 1.00 22.48  0  54  VAL   A CA  1 
ATOM   326  C  C   . VAL   A  1 39  ? 9.491   -31.557 -31.479 1.00 21.33  0  54  VAL   A C   1 
ATOM   327  O  O   . VAL   A  1 39  ? 8.668   -32.332 -30.938 1.00 20.97  0  54  VAL   A O   1 
ATOM   328  C  CB  . VAL   A  1 39  ? 8.722   -29.209 -30.877 1.00 24.20  0  54  VAL   A CB  1 
ATOM   329  C  CG1 . VAL   A  1 39  ? 9.791   -29.170 -29.793 1.00 24.95  0  54  VAL   A CG1 1 
ATOM   330  C  CG2 . VAL   A  1 39  ? 8.480   -27.811 -31.415 1.00 25.30  0  54  VAL   A CG2 1 
ATOM   331  N  N   . LEU   A  1 40  ? 10.784  -31.817 -31.570 1.00 22.19  0  55  LEU   A N   1 
ATOM   332  C  CA  . LEU   A  1 40  ? 11.449  -33.022 -31.000 1.00 22.07  0  55  LEU   A CA  1 
ATOM   333  C  C   . LEU   A  1 40  ? 12.058  -32.626 -29.644 1.00 22.18  0  55  LEU   A C   1 
ATOM   334  O  O   . LEU   A  1 40  ? 12.786  -31.602 -29.589 1.00 23.09  0  55  LEU   A O   1 
ATOM   335  C  CB  . LEU   A  1 40  ? 12.492  -33.537 -31.998 1.00 21.67  0  55  LEU   A CB  1 
ATOM   336  C  CG  . LEU   A  1 40  ? 13.312  -34.739 -31.546 1.00 24.75  0  55  LEU   A CG  1 
ATOM   337  C  CD1 . LEU   A  1 40  ? 12.451  -35.984 -31.421 1.00 25.60  0  55  LEU   A CD1 1 
ATOM   338  C  CD2 . LEU   A  1 40  ? 14.498  -34.965 -32.468 1.00 24.27  0  55  LEU   A CD2 1 
ATOM   339  N  N   . THR   A  1 41  ? 11.776  -33.413 -28.604 1.00 21.46  0  56  THR   A N   1 
ATOM   340  C  CA  . THR   A  1 41  ? 12.301  -33.207 -27.235 1.00 22.34  0  56  THR   A CA  1 
ATOM   341  C  C   . THR   A  1 41  ? 12.587  -34.550 -26.553 1.00 23.29  0  56  THR   A C   1 
ATOM   342  O  O   . THR   A  1 41  ? 12.476  -35.614 -27.200 1.00 24.81  0  56  THR   A O   1 
ATOM   343  C  CB  . THR   A  1 41  ? 11.349  -32.249 -26.484 1.00 21.85  0  56  THR   A CB  1 
ATOM   344  O  OG1 . THR   A  1 41  ? 12.014  -31.739 -25.328 1.00 21.50  0  56  THR   A OG1 1 
ATOM   345  C  CG2 . THR   A  1 41  ? 10.023  -32.867 -26.099 1.00 24.28  0  56  THR   A CG2 1 
ATOM   346  N  N   . ALA   A  1 42  ? 12.946  -34.508 -25.265 1.00 24.59  0  57  ALA   A N   1 
ATOM   347  C  CA  . ALA   A  1 42  ? 13.126  -35.695 -24.398 1.00 21.24  0  57  ALA   A CA  1 
ATOM   348  C  C   . ALA   A  1 42  ? 11.774  -36.014 -23.770 1.00 20.80  0  57  ALA   A C   1 
ATOM   349  O  O   . ALA   A  1 42  ? 11.053  -35.092 -23.343 1.00 22.05  0  57  ALA   A O   1 
ATOM   350  C  CB  . ALA   A  1 42  ? 14.193  -35.419 -23.361 1.00 24.01  0  57  ALA   A CB  1 
ATOM   351  N  N   . ALA   A  1 43  ? 11.427  -37.290 -23.685 1.00 20.79  0  58  ALA   A N   1 
ATOM   352  C  CA  . ALA   A  1 43  ? 10.231  -37.763 -22.962 1.00 23.05  0  58  ALA   A CA  1 
ATOM   353  C  C   . ALA   A  1 43  ? 10.247  -37.325 -21.486 1.00 21.81  0  58  ALA   A C   1 
ATOM   354  O  O   . ALA   A  1 43  ? 9.170   -37.046 -20.966 1.00 24.22  0  58  ALA   A O   1 
ATOM   355  C  CB  . ALA   A  1 43  ? 10.138  -39.257 -23.078 1.00 21.68  0  58  ALA   A CB  1 
ATOM   356  N  N   . HIS   A  1 44  ? 11.398  -37.317 -20.818 1.00 20.23  0  59  HIS   A N   1 
ATOM   357  C  CA  . HIS   A  1 44  ? 11.484  -37.024 -19.366 1.00 23.37  0  59  HIS   A CA  1 
ATOM   358  C  C   . HIS   A  1 44  ? 11.113  -35.539 -19.122 1.00 22.71  0  59  HIS   A C   1 
ATOM   359  O  O   . HIS   A  1 44  ? 10.794  -35.195 -17.970 1.00 23.73  0  59  HIS   A O   1 
ATOM   360  C  CB  . HIS   A  1 44  ? 12.871  -37.425 -18.793 1.00 21.10  0  59  HIS   A CB  1 
ATOM   361  C  CG  . HIS   A  1 44  ? 13.927  -36.380 -18.907 1.00 21.99  0  59  HIS   A CG  1 
ATOM   362  N  ND1 . HIS   A  1 44  ? 14.944  -36.431 -19.853 1.00 23.03  0  59  HIS   A ND1 1 
ATOM   363  C  CD2 . HIS   A  1 44  ? 14.119  -35.235 -18.224 1.00 24.93  0  59  HIS   A CD2 1 
ATOM   364  C  CE1 . HIS   A  1 44  ? 15.717  -35.390 -19.717 1.00 27.06  0  59  HIS   A CE1 1 
ATOM   365  N  NE2 . HIS   A  1 44  ? 15.234  -34.622 -18.728 1.00 23.68  0  59  HIS   A NE2 1 
ATOM   366  N  N   . CYS   A  1 45  ? 11.132  -34.685 -20.142 1.00 21.45  0  60  CYS   A N   1 
ATOM   367  C  CA  . CYS   A  1 45  ? 10.669  -33.272 -20.007 1.00 24.99  0  60  CYS   A CA  1 
ATOM   368  C  C   . CYS   A  1 45  ? 9.152   -33.217 -19.857 1.00 24.08  0  60  CYS   A C   1 
ATOM   369  O  O   . CYS   A  1 45  ? 8.673   -32.274 -19.215 1.00 25.40  0  60  CYS   A O   1 
ATOM   370  C  CB  . CYS   A  1 45  ? 11.066  -32.443 -21.209 1.00 26.28  0  60  CYS   A CB  1 
ATOM   371  S  SG  . CYS   A  1 45  ? 12.851  -32.249 -21.317 1.00 27.29  0  60  CYS   A SG  1 
ATOM   372  N  N   . VAL   A  1 46  ? 8.424   -34.178 -20.431 1.00 23.46  0  61  VAL   A N   1 
ATOM   373  C  CA  . VAL   A  1 46  ? 6.929   -34.090 -20.551 1.00 28.51  0  61  VAL   A CA  1 
ATOM   374  C  C   . VAL   A  1 46  ? 6.232   -35.339 -20.007 1.00 27.45  0  61  VAL   A C   1 
ATOM   375  O  O   . VAL   A  1 46  ? 5.018   -35.393 -20.099 1.00 32.96  0  61  VAL   A O   1 
ATOM   376  C  CB  . VAL   A  1 46  ? 6.529   -33.800 -22.010 1.00 29.24  0  61  VAL   A CB  1 
ATOM   377  C  CG1 . VAL   A  1 46  ? 7.014   -32.424 -22.426 1.00 28.12  0  61  VAL   A CG1 1 
ATOM   378  C  CG2 . VAL   A  1 46  ? 7.051   -34.849 -22.988 1.00 29.40  0  61  VAL   A CG2 1 
ATOM   379  N  N   . GLY   A  1 47  ? 6.975   -36.299 -19.448 1.00 26.99  0  62  GLY   A N   1 
ATOM   380  C  CA  . GLY   A  1 47  ? 6.414   -37.581 -18.999 1.00 28.09  0  62  GLY   A CA  1 
ATOM   381  C  C   . GLY   A  1 47  ? 7.291   -38.222 -17.937 1.00 27.79  0  62  GLY   A C   1 
ATOM   382  O  O   . GLY   A  1 47  ? 8.278   -37.627 -17.530 1.00 29.87  0  62  GLY   A O   1 
ATOM   383  N  N   . PRO   A  1 48  ? 6.983   -39.439 -17.459 1.00 29.64  0  63  PRO   A N   1 
ATOM   384  C  CA  . PRO   A  1 48  ? 5.972   -40.294 -18.083 1.00 29.28  0  63  PRO   A CA  1 
ATOM   385  C  C   . PRO   A  1 48  ? 4.507   -39.966 -17.748 1.00 26.20  0  63  PRO   A C   1 
ATOM   386  O  O   . PRO   A  1 48  ? 3.650   -40.564 -18.297 1.00 28.24  0  63  PRO   A O   1 
ATOM   387  C  CB  . PRO   A  1 48  ? 6.370   -41.660 -17.487 1.00 29.52  0  63  PRO   A CB  1 
ATOM   388  C  CG  . PRO   A  1 48  ? 6.848   -41.353 -16.112 1.00 29.35  0  63  PRO   A CG  1 
ATOM   389  C  CD  . PRO   A  1 48  ? 7.611   -40.048 -16.264 1.00 29.30  0  63  PRO   A CD  1 
ATOM   390  N  N   . ASP   A  1 49  ? 4.250   -39.120 -16.765 1.00 29.16  0  64  ASP   A N   1 
ATOM   391  C  CA  . ASP   A  1 49  ? 2.861   -38.844 -16.301 1.00 30.54  0  64  ASP   A CA  1 
ATOM   392  C  C   . ASP   A  1 49  ? 2.197   -37.845 -17.246 1.00 31.41  0  64  ASP   A C   1 
ATOM   393  O  O   . ASP   A  1 49  ? 2.876   -36.916 -17.691 1.00 32.21  0  64  ASP   A O   1 
ATOM   394  C  CB  . ASP   A  1 49  ? 2.826   -38.302 -14.877 1.00 32.74  0  64  ASP   A CB  1 
ATOM   395  C  CG  . ASP   A  1 49  ? 3.210   -39.334 -13.829 1.00 36.33  0  64  ASP   A CG  1 
ATOM   396  O  OD1 . ASP   A  1 49  ? 3.006   -40.570 -14.059 1.00 35.16  0  64  ASP   A OD1 1 
ATOM   397  O  OD2 . ASP   A  1 49  ? 3.778   -38.890 -12.842 1.00 44.59  -1 64  ASP   A OD2 1 
ATOM   398  N  N   . VAL   A  1 50  ? 0.909   -38.016 -17.502 1.00 30.10  0  65  VAL   A N   1 
ATOM   399  C  CA  . VAL   A  1 50  ? 0.142   -37.180 -18.470 1.00 31.91  0  65  VAL   A CA  1 
ATOM   400  C  C   . VAL   A  1 50  ? -0.070  -35.812 -17.829 1.00 37.77  0  65  VAL   A C   1 
ATOM   401  O  O   . VAL   A  1 50  ? -0.555  -35.779 -16.707 1.00 37.26  0  65  VAL   A O   1 
ATOM   402  C  CB  . VAL   A  1 50  ? -1.183  -37.855 -18.847 1.00 31.45  0  65  VAL   A CB  1 
ATOM   403  C  CG1 . VAL   A  1 50  ? -2.109  -36.928 -19.619 1.00 32.52  0  65  VAL   A CG1 1 
ATOM   404  C  CG2 . VAL   A  1 50  ? -0.894  -39.116 -19.633 1.00 31.38  0  65  VAL   A CG2 1 
ATOM   405  N  N   . LYS   A  1 51  ? 0.257   -34.736 -18.541 1.00 41.72  0  66  LYS   A N   1 
ATOM   406  C  CA  . LYS   A  1 51  ? 0.070   -33.350 -18.044 1.00 49.79  0  66  LYS   A CA  1 
ATOM   407  C  C   . LYS   A  1 51  ? -1.027  -32.613 -18.830 1.00 45.93  0  66  LYS   A C   1 
ATOM   408  O  O   . LYS   A  1 51  ? -1.398  -33.046 -19.937 1.00 40.98  0  66  LYS   A O   1 
ATOM   409  C  CB  . LYS   A  1 51  ? 1.422   -32.642 -18.098 1.00 63.80  0  66  LYS   A CB  1 
ATOM   410  C  CG  . LYS   A  1 51  ? 2.360   -32.964 -16.938 1.00 75.49  0  66  LYS   A CG  1 
ATOM   411  C  CD  . LYS   A  1 51  ? 3.640   -33.664 -17.350 1.00 81.18  0  66  LYS   A CD  1 
ATOM   412  C  CE  . LYS   A  1 51  ? 4.396   -34.211 -16.159 1.00 77.24  0  66  LYS   A CE  1 
ATOM   413  N  NZ  . LYS   A  1 51  ? 5.558   -35.008 -16.589 1.00 72.18  1  66  LYS   A NZ  1 
ATOM   414  N  N   . ASP   A  1 52  ? -1.525  -31.506 -18.264 1.00 43.52  0  67  ASP   A N   1 
ATOM   415  C  CA  . ASP   A  1 52  ? -2.477  -30.581 -18.932 1.00 41.28  0  67  ASP   A CA  1 
ATOM   416  C  C   . ASP   A  1 52  ? -1.736  -29.837 -20.050 1.00 35.35  0  67  ASP   A C   1 
ATOM   417  O  O   . ASP   A  1 52  ? -0.865  -29.060 -19.727 1.00 32.79  0  67  ASP   A O   1 
ATOM   418  C  CB  . ASP   A  1 52  ? -3.090  -29.597 -17.932 1.00 42.47  0  67  ASP   A CB  1 
ATOM   419  C  CG  . ASP   A  1 52  ? -4.267  -28.801 -18.496 1.00 49.84  0  67  ASP   A CG  1 
ATOM   420  O  OD1 . ASP   A  1 52  ? -4.467  -28.792 -19.746 1.00 48.26  0  67  ASP   A OD1 1 
ATOM   421  O  OD2 . ASP   A  1 52  ? -4.977  -28.181 -17.679 1.00 60.38  -1 67  ASP   A OD2 1 
ATOM   422  N  N   . LEU   A  1 53  ? -2.094  -30.058 -21.309 1.00 33.16  0  68  LEU   A N   1 
ATOM   423  C  CA  . LEU   A  1 53  ? -1.479  -29.347 -22.471 1.00 40.95  0  68  LEU   A CA  1 
ATOM   424  C  C   . LEU   A  1 53  ? -1.574  -27.816 -22.323 1.00 36.01  0  68  LEU   A C   1 
ATOM   425  O  O   . LEU   A  1 53  ? -0.699  -27.141 -22.870 1.00 34.91  0  68  LEU   A O   1 
ATOM   426  C  CB  . LEU   A  1 53  ? -2.212  -29.739 -23.750 1.00 43.36  0  68  LEU   A CB  1 
ATOM   427  C  CG  . LEU   A  1 53  ? -2.035  -31.166 -24.229 1.00 50.90  0  68  LEU   A CG  1 
ATOM   428  C  CD1 . LEU   A  1 53  ? -3.015  -31.486 -25.340 1.00 52.51  0  68  LEU   A CD1 1 
ATOM   429  C  CD2 . LEU   A  1 53  ? -0.648  -31.358 -24.733 1.00 55.59  0  68  LEU   A CD2 1 
ATOM   430  N  N   . ALA   A  1 54  ? -2.615  -27.295 -21.657 1.00 34.25  0  69  ALA   A N   1 
ATOM   431  C  CA  . ALA   A  1 54  ? -2.852  -25.836 -21.499 1.00 36.06  0  69  ALA   A CA  1 
ATOM   432  C  C   . ALA   A  1 54  ? -1.707  -25.201 -20.712 1.00 31.27  0  69  ALA   A C   1 
ATOM   433  O  O   . ALA   A  1 54  ? -1.438  -24.019 -20.939 1.00 36.50  0  69  ALA   A O   1 
ATOM   434  C  CB  . ALA   A  1 54  ? -4.174  -25.576 -20.809 1.00 38.63  0  69  ALA   A CB  1 
ATOM   435  N  N   . ALA   A  1 55  ? -1.040  -25.971 -19.851 1.00 29.58  0  70  ALA   A N   1 
ATOM   436  C  CA  . ALA   A  1 55  ? 0.083   -25.536 -18.995 1.00 30.03  0  70  ALA   A CA  1 
ATOM   437  C  C   . ALA   A  1 55  ? 1.409   -25.511 -19.753 1.00 28.34  0  70  ALA   A C   1 
ATOM   438  O  O   . ALA   A  1 55  ? 2.411   -25.117 -19.127 1.00 26.98  0  70  ALA   A O   1 
ATOM   439  C  CB  . ALA   A  1 55  ? 0.174   -26.415 -17.762 1.00 33.41  0  70  ALA   A CB  1 
ATOM   440  N  N   . LEU   A  1 56  ? 1.440   -25.873 -21.042 1.00 28.58  0  71  LEU   A N   1 
ATOM   441  C  CA  . LEU   A  1 56  ? 2.684   -25.935 -21.854 1.00 27.30  0  71  LEU   A CA  1 
ATOM   442  C  C   . LEU   A  1 56  ? 2.588   -24.953 -23.021 1.00 25.39  0  71  LEU   A C   1 
ATOM   443  O  O   . LEU   A  1 56  ? 1.562   -24.934 -23.699 1.00 31.49  0  71  LEU   A O   1 
ATOM   444  C  CB  . LEU   A  1 56  ? 2.859   -27.367 -22.351 1.00 27.47  0  71  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A  1 56  ? 4.037   -27.641 -23.273 1.00 30.58  0  71  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A  1 56  ? 5.341   -27.483 -22.524 1.00 28.79  0  71  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A  1 56  ? 3.918   -29.054 -23.847 1.00 33.19  0  71  LEU   A CD2 1 
ATOM   448  N  N   . ARG   A  1 57  ? 3.675   -24.249 -23.291 1.00 25.77  0  72  ARG   A N   1 
ATOM   449  C  CA  . ARG   A  1 57  ? 3.873   -23.539 -24.564 1.00 28.58  0  72  ARG   A CA  1 
ATOM   450  C  C   . ARG   A  1 57  ? 5.283   -23.768 -25.098 1.00 27.08  0  72  ARG   A C   1 
ATOM   451  O  O   . ARG   A  1 57  ? 6.198   -24.139 -24.334 1.00 26.16  0  72  ARG   A O   1 
ATOM   452  C  CB  . ARG   A  1 57  ? 3.692   -22.038 -24.343 1.00 31.34  0  72  ARG   A CB  1 
ATOM   453  C  CG  . ARG   A  1 57  ? 2.328   -21.652 -23.798 1.00 36.07  0  72  ARG   A CG  1 
ATOM   454  C  CD  . ARG   A  1 57  ? 1.335   -21.444 -24.890 1.00 36.30  0  72  ARG   A CD  1 
ATOM   455  N  NE  . ARG   A  1 57  ? 0.258   -20.699 -24.280 1.00 35.62  0  72  ARG   A NE  1 
ATOM   456  C  CZ  . ARG   A  1 57  ? -0.800  -21.224 -23.672 1.00 42.56  0  72  ARG   A CZ  1 
ATOM   457  N  NH1 . ARG   A  1 57  ? -0.980  -22.548 -23.561 1.00 41.71  1  72  ARG   A NH1 1 
ATOM   458  N  NH2 . ARG   A  1 57  ? -1.679  -20.381 -23.160 1.00 41.54  0  72  ARG   A NH2 1 
ATOM   459  N  N   . VAL   A  1 58  ? 5.445   -23.414 -26.367 1.00 24.87  0  73  VAL   A N   1 
ATOM   460  C  CA  . VAL   A  1 58  ? 6.731   -23.487 -27.107 1.00 26.22  0  73  VAL   A CA  1 
ATOM   461  C  C   . VAL   A  1 58  ? 7.139   -22.064 -27.470 1.00 24.92  0  73  VAL   A C   1 
ATOM   462  O  O   . VAL   A  1 58  ? 6.280   -21.281 -27.922 1.00 25.86  0  73  VAL   A O   1 
ATOM   463  C  CB  . VAL   A  1 58  ? 6.587   -24.373 -28.357 1.00 26.96  0  73  VAL   A CB  1 
ATOM   464  C  CG1 . VAL   A  1 58  ? 7.786   -24.273 -29.263 1.00 29.35  0  73  VAL   A CG1 1 
ATOM   465  C  CG2 . VAL   A  1 58  ? 6.307   -25.834 -27.982 1.00 27.42  0  73  VAL   A CG2 1 
ATOM   466  N  N   . GLN   A  1 59  ? 8.417   -21.767 -27.339 1.00 24.53  0  74  GLN   A N   1 
ATOM   467  C  CA  . GLN   A  1 59  ? 9.040   -20.503 -27.815 1.00 25.91  0  74  GLN   A CA  1 
ATOM   468  C  C   . GLN   A  1 59  ? 10.074  -20.899 -28.863 1.00 26.06  0  74  GLN   A C   1 
ATOM   469  O  O   . GLN   A  1 59  ? 10.988  -21.653 -28.497 1.00 24.45  0  74  GLN   A O   1 
ATOM   470  C  CB  . GLN   A  1 59  ? 9.674   -19.748 -26.648 1.00 25.24  0  74  GLN   A CB  1 
ATOM   471  C  CG  . GLN   A  1 59  ? 10.553  -18.553 -27.016 1.00 26.74  0  74  GLN   A CG  1 
ATOM   472  C  CD  . GLN   A  1 59  ? 9.780   -17.491 -27.781 1.00 29.19  0  74  GLN   A CD  1 
ATOM   473  O  OE1 . GLN   A  1 59  ? 8.668   -17.069 -27.420 1.00 30.02  0  74  GLN   A OE1 1 
ATOM   474  N  NE2 . GLN   A  1 59  ? 10.351  -17.044 -28.874 1.00 28.00  0  74  GLN   A NE2 1 
ATOM   475  N  N   . LEU   A  1 60  ? 9.993   -20.331 -30.073 1.00 26.10  0  75  LEU   A N   1 
ATOM   476  C  CA  . LEU   A  1 60  ? 10.986  -20.590 -31.133 1.00 28.71  0  75  LEU   A CA  1 
ATOM   477  C  C   . LEU   A  1 60  ? 12.267  -19.811 -30.817 1.00 30.66  0  75  LEU   A C   1 
ATOM   478  O  O   . LEU   A  1 60  ? 12.311  -19.115 -29.800 1.00 31.25  0  75  LEU   A O   1 
ATOM   479  C  CB  . LEU   A  1 60  ? 10.409  -20.200 -32.492 1.00 31.60  0  75  LEU   A CB  1 
ATOM   480  C  CG  . LEU   A  1 60  ? 9.105   -20.876 -32.884 1.00 32.91  0  75  LEU   A CG  1 
ATOM   481  C  CD1 . LEU   A  1 60  ? 8.647   -20.351 -34.241 1.00 33.69  0  75  LEU   A CD1 1 
ATOM   482  C  CD2 . LEU   A  1 60  ? 9.227   -22.389 -32.921 1.00 32.12  0  75  LEU   A CD2 1 
ATOM   483  N  N   . ARG   A  1 61  ? 13.279  -19.926 -31.669 1.00 31.55  0  76  ARG   A N   1 
ATOM   484  C  CA  . ARG   A  1 61  ? 14.653  -19.410 -31.423 1.00 36.51  0  76  ARG   A CA  1 
ATOM   485  C  C   . ARG   A  1 61  ? 14.586  -17.978 -30.865 1.00 36.56  0  76  ARG   A C   1 
ATOM   486  O  O   . ARG   A  1 61  ? 13.981  -17.134 -31.516 1.00 33.88  0  76  ARG   A O   1 
ATOM   487  C  CB  . ARG   A  1 61  ? 15.424  -19.533 -32.738 1.00 37.06  0  76  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A  1 61  ? 16.793  -18.870 -32.846 1.00 38.32  0  76  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A  1 61  ? 17.798  -19.494 -31.938 1.00 40.96  0  76  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A  1 61  ? 19.213  -19.236 -32.272 1.00 41.70  0  76  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A  1 61  ? 19.855  -18.104 -32.026 1.00 37.17  0  76  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A  1 61  ? 19.208  -17.051 -31.535 1.00 43.28  1  76  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A  1 61  ? 21.157  -18.028 -32.209 1.00 34.36  0  76  ARG   A NH2 1 
ATOM   494  N  N   . GLU   A  1 62  ? 15.178  -17.764 -29.691 1.00 29.85  0  77  GLU   A N   1 
ATOM   495  C  CA  . GLU   A  1 62  ? 15.382  -16.450 -29.031 1.00 33.78  0  77  GLU   A CA  1 
ATOM   496  C  C   . GLU   A  1 62  ? 16.862  -16.342 -28.687 1.00 33.59  0  77  GLU   A C   1 
ATOM   497  O  O   . GLU   A  1 62  ? 17.373  -17.347 -28.121 1.00 36.92  0  77  GLU   A O   1 
ATOM   498  C  CB  . GLU   A  1 62  ? 14.712  -16.382 -27.659 1.00 33.10  0  77  GLU   A CB  1 
ATOM   499  C  CG  . GLU   A  1 62  ? 13.273  -16.077 -27.703 1.00 34.96  0  77  GLU   A CG  1 
ATOM   500  C  CD  . GLU   A  1 62  ? 12.630  -15.843 -26.354 1.00 31.44  0  77  GLU   A CD  1 
ATOM   501  O  OE1 . GLU   A  1 62  ? 11.767  -14.992 -26.291 1.00 37.54  0  77  GLU   A OE1 1 
ATOM   502  O  OE2 . GLU   A  1 62  ? 12.899  -16.586 -25.409 1.00 28.74  -1 77  GLU   A OE2 1 
ATOM   503  N  N   . GLN   A  1 63  ? 17.513  -15.202 -28.941 1.00 27.03  0  78  GLN   A N   1 
ATOM   504  C  CA  . GLN   A  1 63  ? 18.915  -14.979 -28.484 1.00 27.09  0  78  GLN   A CA  1 
ATOM   505  C  C   . GLN   A  1 63  ? 18.945  -14.904 -26.947 1.00 28.20  0  78  GLN   A C   1 
ATOM   506  O  O   . GLN   A  1 63  ? 19.867  -15.474 -26.354 1.00 28.39  0  78  GLN   A O   1 
ATOM   507  C  CB  . GLN   A  1 63  ? 19.498  -13.734 -29.155 1.00 29.53  0  78  GLN   A CB  1 
ATOM   508  C  CG  . GLN   A  1 63  ? 21.008  -13.603 -29.024 1.00 29.40  0  78  GLN   A CG  1 
ATOM   509  C  CD  . GLN   A  1 63  ? 21.761  -14.773 -29.602 1.00 33.21  0  78  GLN   A CD  1 
ATOM   510  O  OE1 . GLN   A  1 63  ? 21.292  -15.502 -30.492 1.00 31.43  0  78  GLN   A OE1 1 
ATOM   511  N  NE2 . GLN   A  1 63  ? 22.946  -14.988 -29.049 1.00 40.31  0  78  GLN   A NE2 1 
ATOM   512  N  N   . HIS   A  1 64  ? 17.960  -14.249 -26.334 1.00 28.39  0  79  HIS   A N   1 
ATOM   513  C  CA  . HIS   A  1 64  ? 17.837  -14.072 -24.859 1.00 28.31  0  79  HIS   A CA  1 
ATOM   514  C  C   . HIS   A  1 64  ? 16.458  -14.525 -24.418 1.00 30.03  0  79  HIS   A C   1 
ATOM   515  O  O   . HIS   A  1 64  ? 15.467  -13.973 -24.952 1.00 35.03  0  79  HIS   A O   1 
ATOM   516  C  CB  . HIS   A  1 64  ? 18.126  -12.614 -24.492 1.00 31.10  0  79  HIS   A CB  1 
ATOM   517  C  CG  . HIS   A  1 64  ? 19.494  -12.171 -24.866 1.00 28.44  0  79  HIS   A CG  1 
ATOM   518  N  ND1 . HIS   A  1 64  ? 19.742  -11.457 -26.038 1.00 31.55  0  79  HIS   A ND1 1 
ATOM   519  C  CD2 . HIS   A  1 64  ? 20.684  -12.352 -24.265 1.00 28.85  0  79  HIS   A CD2 1 
ATOM   520  C  CE1 . HIS   A  1 64  ? 21.054  -11.236 -26.141 1.00 30.53  0  79  HIS   A CE1 1 
ATOM   521  N  NE2 . HIS   A  1 64  ? 21.656  -11.778 -25.077 1.00 30.54  0  79  HIS   A NE2 1 
ATOM   522  N  N   . LEU   A  1 65  ? 16.385  -15.511 -23.512 1.00 27.99  0  80  LEU   A N   1 
ATOM   523  C  CA  . LEU   A  1 65  ? 15.087  -16.007 -22.987 1.00 29.11  0  80  LEU   A CA  1 
ATOM   524  C  C   . LEU   A  1 65  ? 14.253  -14.866 -22.416 1.00 27.13  0  80  LEU   A C   1 
ATOM   525  O  O   . LEU   A  1 65  ? 14.839  -14.025 -21.714 1.00 30.22  0  80  LEU   A O   1 
ATOM   526  C  CB  . LEU   A  1 65  ? 15.273  -17.014 -21.857 1.00 29.76  0  80  LEU   A CB  1 
ATOM   527  C  CG  . LEU   A  1 65  ? 15.472  -18.472 -22.210 1.00 32.51  0  80  LEU   A CG  1 
ATOM   528  C  CD1 . LEU   A  1 65  ? 15.470  -19.268 -20.906 1.00 30.91  0  80  LEU   A CD1 1 
ATOM   529  C  CD2 . LEU   A  1 65  ? 14.445  -19.028 -23.182 1.00 30.60  0  80  LEU   A CD2 1 
ATOM   530  N  N   . TYR   A  1 66  ? 12.949  -14.885 -22.679 1.00 25.81  0  81  TYR   A N   1 
ATOM   531  C  CA  . TYR   A  1 66  ? 11.909  -14.060 -22.004 1.00 28.54  0  81  TYR   A CA  1 
ATOM   532  C  C   . TYR   A  1 66  ? 11.746  -12.666 -22.612 1.00 29.61  0  81  TYR   A C   1 
ATOM   533  O  O   . TYR   A  1 66  ? 10.637  -12.112 -22.502 1.00 31.78  0  81  TYR   A O   1 
ATOM   534  C  CB  . TYR   A  1 66  ? 12.153  -13.957 -20.493 1.00 28.04  0  81  TYR   A CB  1 
ATOM   535  C  CG  . TYR   A  1 66  ? 12.309  -15.282 -19.806 1.00 26.27  0  81  TYR   A CG  1 
ATOM   536  C  CD1 . TYR   A  1 66  ? 11.278  -16.205 -19.822 1.00 25.12  0  81  TYR   A CD1 1 
ATOM   537  C  CD2 . TYR   A  1 66  ? 13.500  -15.640 -19.198 1.00 23.68  0  81  TYR   A CD2 1 
ATOM   538  C  CE1 . TYR   A  1 66  ? 11.408  -17.447 -19.209 1.00 25.50  0  81  TYR   A CE1 1 
ATOM   539  C  CE2 . TYR   A  1 66  ? 13.637  -16.883 -18.586 1.00 26.43  0  81  TYR   A CE2 1 
ATOM   540  C  CZ  . TYR   A  1 66  ? 12.600  -17.798 -18.610 1.00 24.35  0  81  TYR   A CZ  1 
ATOM   541  O  OH  . TYR   A  1 66  ? 12.706  -19.005 -17.964 1.00 25.25  0  81  TYR   A OH  1 
ATOM   542  N  N   A TYR   A  1 67  ? 12.774  -12.125 -23.263 0.50 30.62  0  82  TYR   A N   1 
ATOM   543  N  N   B TYR   A  1 67  ? 12.784  -12.128 -23.261 0.50 34.49  0  82  TYR   A N   1 
ATOM   544  C  CA  A TYR   A  1 67  ? 12.795  -10.693 -23.672 0.50 34.38  0  82  TYR   A CA  1 
ATOM   545  C  CA  B TYR   A  1 67  ? 12.845  -10.725 -23.755 0.50 41.53  0  82  TYR   A CA  1 
ATOM   546  C  C   A TYR   A  1 67  ? 11.784  -10.432 -24.806 0.50 36.38  0  82  TYR   A C   1 
ATOM   547  C  C   B TYR   A  1 67  ? 11.757  -10.447 -24.799 0.50 40.41  0  82  TYR   A C   1 
ATOM   548  O  O   A TYR   A  1 67  ? 11.077  -9.408  -24.689 0.50 39.83  0  82  TYR   A O   1 
ATOM   549  O  O   B TYR   A  1 67  ? 11.025  -9.442  -24.658 0.50 43.07  0  82  TYR   A O   1 
ATOM   550  C  CB  A TYR   A  1 67  ? 14.250  -10.266 -23.870 0.50 32.62  0  82  TYR   A CB  1 
ATOM   551  C  CB  B TYR   A  1 67  ? 14.225  -10.448 -24.352 0.50 44.88  0  82  TYR   A CB  1 
ATOM   552  C  CG  A TYR   A  1 67  ? 14.951  -10.103 -22.541 0.50 29.64  0  82  TYR   A CG  1 
ATOM   553  C  CG  B TYR   A  1 67  ? 14.490  -9.003  -24.685 0.50 50.32  0  82  TYR   A CG  1 
ATOM   554  C  CD1 A TYR   A  1 67  ? 14.673  -9.027  -21.704 0.50 29.37  0  82  TYR   A CD1 1 
ATOM   555  C  CD1 B TYR   A  1 67  ? 13.869  -7.977  -23.995 0.50 51.25  0  82  TYR   A CD1 1 
ATOM   556  C  CD2 A TYR   A  1 67  ? 15.779  -11.095 -22.048 0.50 28.42  0  82  TYR   A CD2 1 
ATOM   557  C  CD2 B TYR   A  1 67  ? 15.401  -8.661  -25.667 0.50 53.53  0  82  TYR   A CD2 1 
ATOM   558  C  CE1 A TYR   A  1 67  ? 15.288  -8.894  -20.470 0.50 26.71  0  82  TYR   A CE1 1 
ATOM   559  C  CE1 B TYR   A  1 67  ? 14.135  -6.652  -24.288 0.50 49.45  0  82  TYR   A CE1 1 
ATOM   560  C  CE2 A TYR   A  1 67  ? 16.382  -10.988 -20.807 0.50 26.17  0  82  TYR   A CE2 1 
ATOM   561  C  CE2 B TYR   A  1 67  ? 15.678  -7.344  -25.978 0.50 53.51  0  82  TYR   A CE2 1 
ATOM   562  C  CZ  A TYR   A  1 67  ? 16.159  -9.868  -20.027 0.50 25.65  0  82  TYR   A CZ  1 
ATOM   563  C  CZ  B TYR   A  1 67  ? 15.036  -6.335  -25.287 0.50 52.32  0  82  TYR   A CZ  1 
ATOM   564  O  OH  A TYR   A  1 67  ? 16.769  -9.766  -18.814 0.50 24.58  0  82  TYR   A OH  1 
ATOM   565  O  OH  B TYR   A  1 67  ? 15.317  -5.037  -25.588 0.50 58.11  0  82  TYR   A OH  1 
ATOM   566  N  N   . GLN   A  1 68  ? 11.610  -11.355 -25.760 1.00 37.87  0  83  GLN   A N   1 
ATOM   567  C  CA  . GLN   A  1 68  ? 10.712  -11.146 -26.932 1.00 41.66  0  83  GLN   A CA  1 
ATOM   568  C  C   . GLN   A  1 68  ? 9.787   -12.342 -27.102 1.00 33.37  0  83  GLN   A C   1 
ATOM   569  O  O   . GLN   A  1 68  ? 9.612   -12.755 -28.224 1.00 34.67  0  83  GLN   A O   1 
ATOM   570  C  CB  . GLN   A  1 68  ? 11.536  -11.020 -28.228 1.00 47.00  0  83  GLN   A CB  1 
ATOM   571  C  CG  . GLN   A  1 68  ? 12.638  -9.971  -28.226 1.00 54.57  0  83  GLN   A CG  1 
ATOM   572  C  CD  . GLN   A  1 68  ? 12.118  -8.603  -28.551 1.00 53.54  0  83  GLN   A CD  1 
ATOM   573  O  OE1 . GLN   A  1 68  ? 12.369  -8.088  -29.627 1.00 50.40  0  83  GLN   A OE1 1 
ATOM   574  N  NE2 . GLN   A  1 68  ? 11.396  -8.011  -27.617 1.00 62.70  0  83  GLN   A NE2 1 
ATOM   575  N  N   . ASP   A  1 69  ? 9.184   -12.847 -26.042 1.00 28.34  0  84  ASP   A N   1 
ATOM   576  C  CA  . ASP   A  1 69  ? 8.390   -14.097 -26.124 1.00 27.57  0  84  ASP   A CA  1 
ATOM   577  C  C   . ASP   A  1 69  ? 7.221   -13.917 -27.100 1.00 28.45  0  84  ASP   A C   1 
ATOM   578  O  O   . ASP   A  1 69  ? 6.536   -12.911 -27.028 1.00 26.44  0  84  ASP   A O   1 
ATOM   579  C  CB  . ASP   A  1 69  ? 7.901   -14.537 -24.754 1.00 25.69  0  84  ASP   A CB  1 
ATOM   580  C  CG  . ASP   A  1 69  ? 8.971   -15.220 -23.901 1.00 30.52  0  84  ASP   A CG  1 
ATOM   581  O  OD1 . ASP   A  1 69  ? 10.127  -15.368 -24.391 1.00 25.57  0  84  ASP   A OD1 1 
ATOM   582  O  OD2 . ASP   A  1 69  ? 8.636   -15.547 -22.714 1.00 31.98  -1 84  ASP   A OD2 1 
ATOM   583  N  N   . GLN   A  1 70  ? 7.006   -14.892 -27.967 1.00 29.36  0  85  GLN   A N   1 
ATOM   584  C  CA  . GLN   A  1 70  ? 5.740   -15.119 -28.693 1.00 29.61  0  85  GLN   A CA  1 
ATOM   585  C  C   . GLN   A  1 70  ? 5.424   -16.604 -28.564 1.00 30.33  0  85  GLN   A C   1 
ATOM   586  O  O   . GLN   A  1 70  ? 5.930   -17.400 -29.369 1.00 33.99  0  85  GLN   A O   1 
ATOM   587  C  CB  . GLN   A  1 70  ? 5.889   -14.661 -30.142 1.00 32.74  0  85  GLN   A CB  1 
ATOM   588  C  CG  . GLN   A  1 70  ? 6.532   -13.294 -30.265 1.00 36.56  0  85  GLN   A CG  1 
ATOM   589  C  CD  . GLN   A  1 70  ? 6.626   -12.824 -31.693 1.00 45.61  0  85  GLN   A CD  1 
ATOM   590  O  OE1 . GLN   A  1 70  ? 7.470   -13.280 -32.483 1.00 50.84  0  85  GLN   A OE1 1 
ATOM   591  N  NE2 . GLN   A  1 70  ? 5.776   -11.864 -32.004 1.00 48.19  0  85  GLN   A NE2 1 
ATOM   592  N  N   . LEU   A  1 71  ? 4.663   -16.959 -27.534 1.00 28.01  0  86  LEU   A N   1 
ATOM   593  C  CA  . LEU   A  1 71  ? 4.495   -18.356 -27.091 1.00 29.61  0  86  LEU   A CA  1 
ATOM   594  C  C   . LEU   A  1 71  ? 3.499   -19.063 -28.017 1.00 30.50  0  86  LEU   A C   1 
ATOM   595  O  O   . LEU   A  1 71  ? 2.503   -18.444 -28.355 1.00 30.73  0  86  LEU   A O   1 
ATOM   596  C  CB  . LEU   A  1 71  ? 4.056   -18.368 -25.619 1.00 27.23  0  86  LEU   A CB  1 
ATOM   597  C  CG  . LEU   A  1 71  ? 5.089   -17.791 -24.652 1.00 28.82  0  86  LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A  1 71  ? 4.591   -17.853 -23.242 1.00 30.16  0  86  LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A  1 71  ? 6.437   -18.483 -24.777 1.00 32.25  0  86  LEU   A CD2 1 
ATOM   600  N  N   . LEU   A  1 72  ? 3.749   -20.331 -28.367 1.00 30.62  0  87  LEU   A N   1 
ATOM   601  C  CA  . LEU   A  1 72  ? 2.850   -21.134 -29.239 1.00 26.27  0  87  LEU   A CA  1 
ATOM   602  C  C   . LEU   A  1 72  ? 2.206   -22.256 -28.427 1.00 27.21  0  87  LEU   A C   1 
ATOM   603  O  O   . LEU   A  1 72  ? 2.888   -23.000 -27.709 1.00 31.06  0  87  LEU   A O   1 
ATOM   604  C  CB  . LEU   A  1 72  ? 3.665   -21.643 -30.422 1.00 28.25  0  87  LEU   A CB  1 
ATOM   605  C  CG  . LEU   A  1 72  ? 4.435   -20.573 -31.203 1.00 28.48  0  87  LEU   A CG  1 
ATOM   606  C  CD1 . LEU   A  1 72  ? 5.267   -21.220 -32.275 1.00 31.65  0  87  LEU   A CD1 1 
ATOM   607  C  CD2 . LEU   A  1 72  ? 3.489   -19.540 -31.822 1.00 27.88  0  87  LEU   A CD2 1 
ATOM   608  N  N   . PRO   A  1 73  ? 0.868   -22.418 -28.498 1.00 25.95  0  88  PRO   A N   1 
ATOM   609  C  CA  . PRO   A  1 73  ? 0.220   -23.543 -27.842 1.00 27.04  0  88  PRO   A CA  1 
ATOM   610  C  C   . PRO   A  1 73  ? 0.460   -24.854 -28.606 1.00 26.20  0  88  PRO   A C   1 
ATOM   611  O  O   . PRO   A  1 73  ? 0.793   -24.825 -29.775 1.00 25.46  0  88  PRO   A O   1 
ATOM   612  C  CB  . PRO   A  1 73  ? -1.231  -23.053 -27.778 1.00 27.43  0  88  PRO   A CB  1 
ATOM   613  C  CG  . PRO   A  1 73  ? -1.389  -22.310 -29.093 1.00 27.55  0  88  PRO   A CG  1 
ATOM   614  C  CD  . PRO   A  1 73  ? -0.093  -21.538 -29.193 1.00 25.91  0  88  PRO   A CD  1 
ATOM   615  N  N   . VAL   A  1 74  ? 0.308   -25.967 -27.880 1.00 28.10  0  89  VAL   A N   1 
ATOM   616  C  CA  . VAL   A  1 74  ? 0.572   -27.361 -28.339 1.00 26.86  0  89  VAL   A CA  1 
ATOM   617  C  C   . VAL   A  1 74  ? -0.769  -28.070 -28.437 1.00 24.30  0  89  VAL   A C   1 
ATOM   618  O  O   . VAL   A  1 74  ? -1.520  -27.982 -27.452 1.00 25.89  0  89  VAL   A O   1 
ATOM   619  C  CB  . VAL   A  1 74  ? 1.506   -28.043 -27.316 1.00 28.98  0  89  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A  1 74  ? 1.561   -29.545 -27.478 1.00 28.95  0  89  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A  1 74  ? 2.904   -27.462 -27.426 1.00 27.62  0  89  VAL   A CG2 1 
ATOM   622  N  N   . SER   A  1 75  ? -1.027  -28.832 -29.501 1.00 24.70  0  90  SER   A N   1 
ATOM   623  C  CA  . SER   A  1 75  ? -2.276  -29.656 -29.627 1.00 24.84  0  90  SER   A CA  1 
ATOM   624  C  C   . SER   A  1 75  ? -2.093  -31.072 -29.088 1.00 27.20  0  90  SER   A C   1 
ATOM   625  O  O   . SER   A  1 75  ? -3.104  -31.681 -28.688 1.00 25.98  0  90  SER   A O   1 
ATOM   626  C  CB  . SER   A  1 75  ? -2.785  -29.719 -31.042 1.00 23.49  0  90  SER   A CB  1 
ATOM   627  O  OG  . SER   A  1 75  ? -1.744  -30.125 -31.903 1.00 29.40  0  90  SER   A OG  1 
ATOM   628  N  N   . ARG   A  1 76  ? -0.878  -31.614 -29.147 1.00 26.46  0  91  ARG   A N   1 
ATOM   629  C  CA  . ARG   A  1 76  ? -0.644  -33.040 -28.811 1.00 30.57  0  91  ARG   A CA  1 
ATOM   630  C  C   . ARG   A  1 76  ? 0.759   -33.196 -28.212 1.00 27.46  0  91  ARG   A C   1 
ATOM   631  O  O   . ARG   A  1 76  ? 1.694   -32.598 -28.740 1.00 22.68  0  91  ARG   A O   1 
ATOM   632  C  CB  . ARG   A  1 76  ? -0.692  -33.933 -30.058 1.00 33.52  0  91  ARG   A CB  1 
ATOM   633  C  CG  . ARG   A  1 76  ? -2.024  -34.039 -30.786 1.00 42.54  0  91  ARG   A CG  1 
ATOM   634  C  CD  . ARG   A  1 76  ? -1.960  -35.082 -31.897 1.00 48.30  0  91  ARG   A CD  1 
ATOM   635  N  NE  . ARG   A  1 76  ? -2.017  -36.439 -31.364 1.00 51.48  0  91  ARG   A NE  1 
ATOM   636  C  CZ  . ARG   A  1 76  ? -1.703  -37.565 -32.030 1.00 59.64  0  91  ARG   A CZ  1 
ATOM   637  N  NH1 . ARG   A  1 76  ? -1.266  -37.521 -33.283 1.00 51.89  1  91  ARG   A NH1 1 
ATOM   638  N  NH2 . ARG   A  1 76  ? -1.811  -38.739 -31.414 1.00 57.67  0  91  ARG   A NH2 1 
ATOM   639  N  N   . ILE   A  1 77  ? 0.878   -34.009 -27.176 1.00 28.30  0  92  ILE   A N   1 
ATOM   640  C  CA  . ILE   A  1 77  ? 2.190   -34.500 -26.653 1.00 28.54  0  92  ILE   A CA  1 
ATOM   641  C  C   . ILE   A  1 77  ? 2.246   -35.990 -26.952 1.00 26.24  0  92  ILE   A C   1 
ATOM   642  O  O   . ILE   A  1 77  ? 1.351   -36.701 -26.493 1.00 25.93  0  92  ILE   A O   1 
ATOM   643  C  CB  . ILE   A  1 77  ? 2.342   -34.204 -25.155 1.00 27.69  0  92  ILE   A CB  1 
ATOM   644  C  CG1 . ILE   A  1 77  ? 2.355   -32.702 -24.857 1.00 31.20  0  92  ILE   A CG1 1 
ATOM   645  C  CG2 . ILE   A  1 77  ? 3.604   -34.869 -24.619 1.00 29.03  0  92  ILE   A CG2 1 
ATOM   646  C  CD1 . ILE   A  1 77  ? 2.102   -32.364 -23.372 1.00 33.08  0  92  ILE   A CD1 1 
ATOM   647  N  N   . ILE   A  1 78  ? 3.218   -36.426 -27.741 1.00 26.89  0  93  ILE   A N   1 
ATOM   648  C  CA  . ILE   A  1 78  ? 3.411   -37.868 -28.073 1.00 30.64  0  93  ILE   A CA  1 
ATOM   649  C  C   . ILE   A  1 78  ? 4.726   -38.321 -27.434 1.00 26.89  0  93  ILE   A C   1 
ATOM   650  O  O   . ILE   A  1 78  ? 5.800   -37.794 -27.778 1.00 26.96  0  93  ILE   A O   1 
ATOM   651  C  CB  . ILE   A  1 78  ? 3.437   -38.129 -29.584 1.00 30.88  0  93  ILE   A CB  1 
ATOM   652  C  CG1 . ILE   A  1 78  ? 2.333   -37.388 -30.329 1.00 35.99  0  93  ILE   A CG1 1 
ATOM   653  C  CG2 . ILE   A  1 78  ? 3.425   -39.614 -29.869 1.00 32.76  0  93  ILE   A CG2 1 
ATOM   654  C  CD1 . ILE   A  1 78  ? 0.977   -37.838 -29.992 1.00 40.68  0  93  ILE   A CD1 1 
ATOM   655  N  N   . VAL   A  1 79  ? 4.623   -39.246 -26.516 1.00 26.78  0  94  VAL   A N   1 
ATOM   656  C  CA  . VAL   A  1 79  ? 5.784   -39.737 -25.733 1.00 27.88  0  94  VAL   A CA  1 
ATOM   657  C  C   . VAL   A  1 79  ? 6.009   -41.183 -26.133 1.00 25.92  0  94  VAL   A C   1 
ATOM   658  O  O   . VAL   A  1 79  ? 5.028   -41.966 -26.149 1.00 25.93  0  94  VAL   A O   1 
ATOM   659  C  CB  . VAL   A  1 79  ? 5.529   -39.582 -24.228 1.00 29.59  0  94  VAL   A CB  1 
ATOM   660  C  CG1 . VAL   A  1 79  ? 6.689   -40.144 -23.409 1.00 29.44  0  94  VAL   A CG1 1 
ATOM   661  C  CG2 . VAL   A  1 79  ? 5.277   -38.123 -23.885 1.00 31.17  0  94  VAL   A CG2 1 
ATOM   662  N  N   . HIS   A  1 80  ? 7.252   -41.542 -26.402 1.00 26.04  0  95  HIS   A N   1 
ATOM   663  C  CA  . HIS   A  1 80  ? 7.579   -42.942 -26.776 1.00 26.81  0  95  HIS   A CA  1 
ATOM   664  C  C   . HIS   A  1 80  ? 6.958   -43.871 -25.754 1.00 24.58  0  95  HIS   A C   1 
ATOM   665  O  O   . HIS   A  1 80  ? 7.217   -43.724 -24.563 1.00 26.43  0  95  HIS   A O   1 
ATOM   666  C  CB  . HIS   A  1 80  ? 9.080   -43.142 -26.906 1.00 25.95  0  95  HIS   A CB  1 
ATOM   667  C  CG  . HIS   A  1 80  ? 9.399   -44.323 -27.746 1.00 28.20  0  95  HIS   A CG  1 
ATOM   668  N  ND1 . HIS   A  1 80  ? 9.164   -45.602 -27.303 1.00 28.63  0  95  HIS   A ND1 1 
ATOM   669  C  CD2 . HIS   A  1 80  ? 9.881   -44.426 -29.006 1.00 28.45  0  95  HIS   A CD2 1 
ATOM   670  C  CE1 . HIS   A  1 80  ? 9.507   -46.456 -28.257 1.00 31.94  0  95  HIS   A CE1 1 
ATOM   671  N  NE2 . HIS   A  1 80  ? 9.920   -45.747 -29.327 1.00 29.54  0  95  HIS   A NE2 1 
ATOM   672  N  N   . PRO   A  1 81  ? 6.151   -44.872 -26.157 1.00 24.21  0  96  PRO   A N   1 
ATOM   673  C  CA  . PRO   A  1 81  ? 5.503   -45.745 -25.182 1.00 25.26  0  96  PRO   A CA  1 
ATOM   674  C  C   . PRO   A  1 81  ? 6.462   -46.689 -24.399 1.00 25.99  0  96  PRO   A C   1 
ATOM   675  O  O   . PRO   A  1 81  ? 6.054   -47.251 -23.419 1.00 26.08  0  96  PRO   A O   1 
ATOM   676  C  CB  . PRO   A  1 81  ? 4.510   -46.536 -26.044 1.00 25.82  0  96  PRO   A CB  1 
ATOM   677  C  CG  . PRO   A  1 81  ? 5.131   -46.579 -27.417 1.00 26.06  0  96  PRO   A CG  1 
ATOM   678  C  CD  . PRO   A  1 81  ? 5.846   -45.247 -27.550 1.00 27.16  0  96  PRO   A CD  1 
ATOM   679  N  N   . GLN   A  1 82  ? 7.715   -46.819 -24.793 1.00 27.30  0  97  GLN   A N   1 
ATOM   680  C  CA  . GLN   A  1 82  ? 8.714   -47.593 -24.014 1.00 30.74  0  97  GLN   A CA  1 
ATOM   681  C  C   . GLN   A  1 82  ? 9.349   -46.732 -22.923 1.00 31.38  0  97  GLN   A C   1 
ATOM   682  O  O   . GLN   A  1 82  ? 10.096  -47.317 -22.137 1.00 27.79  0  97  GLN   A O   1 
ATOM   683  C  CB  . GLN   A  1 82  ? 9.751   -48.199 -24.939 1.00 31.47  0  97  GLN   A CB  1 
ATOM   684  C  CG  . GLN   A  1 82  ? 9.194   -49.401 -25.673 1.00 34.23  0  97  GLN   A CG  1 
ATOM   685  C  CD  . GLN   A  1 82  ? 10.241  -49.892 -26.635 1.00 41.36  0  97  GLN   A CD  1 
ATOM   686  O  OE1 . GLN   A  1 82  ? 10.058  -49.862 -27.845 1.00 51.51  0  97  GLN   A OE1 1 
ATOM   687  N  NE2 . GLN   A  1 82  ? 11.385  -50.291 -26.112 1.00 50.30  0  97  GLN   A NE2 1 
ATOM   688  N  N   . PHE   A  1 83  ? 9.050   -45.425 -22.857 1.00 28.12  0  98  PHE   A N   1 
ATOM   689  C  CA  . PHE   A  1 83  ? 9.701   -44.517 -21.892 1.00 26.21  0  98  PHE   A CA  1 
ATOM   690  C  C   . PHE   A  1 83  ? 9.101   -44.638 -20.491 1.00 25.10  0  98  PHE   A C   1 
ATOM   691  O  O   . PHE   A  1 83  ? 7.882   -44.519 -20.339 1.00 25.79  0  98  PHE   A O   1 
ATOM   692  C  CB  . PHE   A  1 83  ? 9.603   -43.054 -22.300 1.00 26.69  0  98  PHE   A CB  1 
ATOM   693  C  CG  . PHE   A  1 83  ? 10.217  -42.154 -21.265 1.00 25.35  0  98  PHE   A CG  1 
ATOM   694  C  CD1 . PHE   A  1 83  ? 11.592  -42.166 -21.060 1.00 25.12  0  98  PHE   A CD1 1 
ATOM   695  C  CD2 . PHE   A  1 83  ? 9.412   -41.406 -20.404 1.00 25.70  0  98  PHE   A CD2 1 
ATOM   696  C  CE1 . PHE   A  1 83  ? 12.172  -41.358 -20.089 1.00 25.51  0  98  PHE   A CE1 1 
ATOM   697  C  CE2 . PHE   A  1 83  ? 9.999   -40.615 -19.427 1.00 24.92  0  98  PHE   A CE2 1 
ATOM   698  C  CZ  . PHE   A  1 83  ? 11.368  -40.600 -19.266 1.00 25.86  0  98  PHE   A CZ  1 
ATOM   699  N  N   . TYR   A  1 84  ? 9.971   -44.772 -19.482 1.00 23.01  0  99  TYR   A N   1 
ATOM   700  C  CA  . TYR   A  1 84  ? 9.614   -44.589 -18.059 1.00 26.17  0  99  TYR   A CA  1 
ATOM   701  C  C   . TYR   A  1 84  ? 10.681  -43.748 -17.364 1.00 23.62  0  99  TYR   A C   1 
ATOM   702  O  O   . TYR   A  1 84  ? 10.283  -42.799 -16.671 1.00 26.26  0  99  TYR   A O   1 
ATOM   703  C  CB  . TYR   A  1 84  ? 9.274   -45.928 -17.376 1.00 26.74  0  99  TYR   A CB  1 
ATOM   704  C  CG  . TYR   A  1 84  ? 8.740   -45.678 -15.996 1.00 28.08  0  99  TYR   A CG  1 
ATOM   705  C  CD1 . TYR   A  1 84  ? 7.526   -45.020 -15.827 1.00 27.51  0  99  TYR   A CD1 1 
ATOM   706  C  CD2 . TYR   A  1 84  ? 9.503   -45.924 -14.862 1.00 28.71  0  99  TYR   A CD2 1 
ATOM   707  C  CE1 . TYR   A  1 84  ? 7.057   -44.685 -14.575 1.00 26.32  0  99  TYR   A CE1 1 
ATOM   708  C  CE2 . TYR   A  1 84  ? 9.030   -45.617 -13.591 1.00 28.67  0  99  TYR   A CE2 1 
ATOM   709  C  CZ  . TYR   A  1 84  ? 7.813   -44.974 -13.449 1.00 26.17  0  99  TYR   A CZ  1 
ATOM   710  O  OH  . TYR   A  1 84  ? 7.352   -44.596 -12.225 1.00 27.26  0  99  TYR   A OH  1 
ATOM   711  N  N   . THR   A  1 85  ? 11.975  -44.052 -17.527 1.00 25.24  0  100 THR   A N   1 
ATOM   712  C  CA  . THR   A  1 85  ? 13.086  -43.206 -17.013 1.00 24.73  0  100 THR   A CA  1 
ATOM   713  C  C   . THR   A  1 85  ? 14.182  -43.055 -18.082 1.00 24.96  0  100 THR   A C   1 
ATOM   714  O  O   . THR   A  1 85  ? 14.263  -43.905 -18.985 1.00 24.57  0  100 THR   A O   1 
ATOM   715  C  CB  . THR   A  1 85  ? 13.705  -43.735 -15.713 1.00 25.59  0  100 THR   A CB  1 
ATOM   716  O  OG1 . THR   A  1 85  ? 14.527  -44.851 -16.042 1.00 24.05  0  100 THR   A OG1 1 
ATOM   717  C  CG2 . THR   A  1 85  ? 12.695  -44.163 -14.675 1.00 25.07  0  100 THR   A CG2 1 
ATOM   718  N  N   . ALA   A  1 86  ? 14.985  -41.987 -17.988 1.00 23.77  0  101 ALA   A N   1 
ATOM   719  C  CA  . ALA   A  1 86  ? 16.056  -41.675 -18.964 1.00 22.89  0  101 ALA   A CA  1 
ATOM   720  C  C   . ALA   A  1 86  ? 17.092  -42.783 -18.945 1.00 23.42  0  101 ALA   A C   1 
ATOM   721  O  O   . ALA   A  1 86  ? 17.590  -43.099 -20.037 1.00 24.72  0  101 ALA   A O   1 
ATOM   722  C  CB  . ALA   A  1 86  ? 16.731  -40.362 -18.678 1.00 26.95  0  101 ALA   A CB  1 
ATOM   723  N  N   . GLN   A  1 87  ? 17.426  -43.330 -17.774 1.00 23.41  0  102 GLN   A N   1 
ATOM   724  C  CA  . GLN   A  1 87  ? 18.484  -44.379 -17.668 1.00 25.58  0  102 GLN   A CA  1 
ATOM   725  C  C   . GLN   A  1 87  ? 18.012  -45.710 -18.260 1.00 25.47  0  102 GLN   A C   1 
ATOM   726  O  O   . GLN   A  1 87  ? 18.899  -46.507 -18.725 1.00 28.23  0  102 GLN   A O   1 
ATOM   727  C  CB  . GLN   A  1 87  ? 18.977  -44.614 -16.248 1.00 24.79  0  102 GLN   A CB  1 
ATOM   728  C  CG  . GLN   A  1 87  ? 19.512  -43.349 -15.617 1.00 30.58  0  102 GLN   A CG  1 
ATOM   729  C  CD  . GLN   A  1 87  ? 18.493  -42.615 -14.785 1.00 35.39  0  102 GLN   A CD  1 
ATOM   730  O  OE1 . GLN   A  1 87  ? 17.277  -42.862 -14.816 1.00 29.46  0  102 GLN   A OE1 1 
ATOM   731  N  NE2 . GLN   A  1 87  ? 19.010  -41.707 -13.987 1.00 46.46  0  102 GLN   A NE2 1 
ATOM   732  N  N   . ILE   A  1 88  ? 16.716  -45.974 -18.270 1.00 24.31  0  103 ILE   A N   1 
ATOM   733  C  CA  . ILE   A  1 88  ? 16.177  -47.188 -18.955 1.00 25.50  0  103 ILE   A CA  1 
ATOM   734  C  C   . ILE   A  1 88  ? 16.196  -46.970 -20.471 1.00 26.83  0  103 ILE   A C   1 
ATOM   735  O  O   . ILE   A  1 88  ? 16.603  -47.918 -21.213 1.00 27.16  0  103 ILE   A O   1 
ATOM   736  C  CB  . ILE   A  1 88  ? 14.800  -47.606 -18.421 1.00 26.66  0  103 ILE   A CB  1 
ATOM   737  C  CG1 . ILE   A  1 88  ? 14.874  -47.981 -16.946 1.00 26.47  0  103 ILE   A CG1 1 
ATOM   738  C  CG2 . ILE   A  1 88  ? 14.240  -48.759 -19.253 1.00 28.83  0  103 ILE   A CG2 1 
ATOM   739  C  CD1 . ILE   A  1 88  ? 13.527  -48.156 -16.221 1.00 28.02  0  103 ILE   A CD1 1 
ATOM   740  N  N   . GLY   A  1 89  ? 15.812  -45.775 -20.932 1.00 27.97  0  104 GLY   A N   1 
ATOM   741  C  CA  . GLY   A  1 89  ? 15.938  -45.343 -22.343 1.00 27.18  0  104 GLY   A CA  1 
ATOM   742  C  C   . GLY   A  1 89  ? 14.623  -44.930 -22.966 1.00 25.23  0  104 GLY   A C   1 
ATOM   743  O  O   . GLY   A  1 89  ? 13.643  -44.744 -22.248 1.00 25.47  0  104 GLY   A O   1 
ATOM   744  N  N   . ALA   A  1 90  ? 14.592  -44.854 -24.296 1.00 28.71  0  105 ALA   A N   1 
ATOM   745  C  CA  . ALA   A  1 90  ? 13.454  -44.359 -25.100 1.00 23.67  0  105 ALA   A CA  1 
ATOM   746  C  C   . ALA   A  1 90  ? 13.110  -42.934 -24.630 1.00 22.27  0  105 ALA   A C   1 
ATOM   747  O  O   . ALA   A  1 90  ? 11.926  -42.580 -24.629 1.00 22.93  0  105 ALA   A O   1 
ATOM   748  C  CB  . ALA   A  1 90  ? 12.279  -45.312 -25.026 1.00 25.59  0  105 ALA   A CB  1 
ATOM   749  N  N   . ASP   A  1 91  ? 14.134  -42.135 -24.351 1.00 21.60  0  106 ASP   A N   1 
ATOM   750  C  CA  . ASP   A  1 91  ? 13.967  -40.763 -23.823 1.00 22.03  0  106 ASP   A CA  1 
ATOM   751  C  C   . ASP   A  1 91  ? 13.723  -39.794 -25.004 1.00 21.48  0  106 ASP   A C   1 
ATOM   752  O  O   . ASP   A  1 91  ? 14.612  -39.008 -25.362 1.00 20.92  0  106 ASP   A O   1 
ATOM   753  C  CB  . ASP   A  1 91  ? 15.110  -40.391 -22.888 1.00 21.12  0  106 ASP   A CB  1 
ATOM   754  C  CG  . ASP   A  1 91  ? 14.781  -39.116 -22.124 1.00 21.54  0  106 ASP   A CG  1 
ATOM   755  O  OD1 . ASP   A  1 91  ? 13.587  -38.719 -22.150 1.00 22.30  0  106 ASP   A OD1 1 
ATOM   756  O  OD2 . ASP   A  1 91  ? 15.702  -38.531 -21.534 1.00 20.64  -1 106 ASP   A OD2 1 
ATOM   757  N  N   . ILE   A  1 92  ? 12.538  -39.856 -25.588 1.00 18.96  0  107 ILE   A N   1 
ATOM   758  C  CA  . ILE   A  1 92  ? 12.202  -39.126 -26.839 1.00 21.90  0  107 ILE   A CA  1 
ATOM   759  C  C   . ILE   A  1 92  ? 10.709  -38.861 -26.880 1.00 22.12  0  107 ILE   A C   1 
ATOM   760  O  O   . ILE   A  1 92  ? 9.939   -39.753 -26.445 1.00 21.87  0  107 ILE   A O   1 
ATOM   761  C  CB  . ILE   A  1 92  ? 12.733  -39.858 -28.076 1.00 23.04  0  107 ILE   A CB  1 
ATOM   762  C  CG1 . ILE   A  1 92  ? 12.807  -38.911 -29.266 1.00 25.45  0  107 ILE   A CG1 1 
ATOM   763  C  CG2 . ILE   A  1 92  ? 11.962  -41.124 -28.380 1.00 25.11  0  107 ILE   A CG2 1 
ATOM   764  C  CD1 . ILE   A  1 92  ? 13.625  -39.440 -30.407 1.00 27.02  0  107 ILE   A CD1 1 
ATOM   765  N  N   . ALA   A  1 93  ? 10.341  -37.648 -27.300 1.00 22.91  0  108 ALA   A N   1 
ATOM   766  C  CA  . ALA   A  1 93  ? 8.927   -37.198 -27.427 1.00 22.37  0  108 ALA   A CA  1 
ATOM   767  C  C   . ALA   A  1 93  ? 8.780   -36.172 -28.560 1.00 20.63  0  108 ALA   A C   1 
ATOM   768  O  O   . ALA   A  1 93  ? 9.762   -35.582 -29.002 1.00 21.76  0  108 ALA   A O   1 
ATOM   769  C  CB  . ALA   A  1 93  ? 8.458   -36.637 -26.100 1.00 22.44  0  108 ALA   A CB  1 
ATOM   770  N  N   . LEU   A  1 94  ? 7.548   -35.971 -28.973 1.00 23.72  0  109 LEU   A N   1 
ATOM   771  C  CA  . LEU   A  1 94  ? 7.123   -35.058 -30.043 1.00 25.15  0  109 LEU   A CA  1 
ATOM   772  C  C   . LEU   A  1 94  ? 6.045   -34.139 -29.492 1.00 24.61  0  109 LEU   A C   1 
ATOM   773  O  O   . LEU   A  1 94  ? 5.147   -34.636 -28.757 1.00 20.49  0  109 LEU   A O   1 
ATOM   774  C  CB  . LEU   A  1 94  ? 6.581   -35.886 -31.204 1.00 25.68  0  109 LEU   A CB  1 
ATOM   775  C  CG  . LEU   A  1 94  ? 7.593   -36.693 -31.993 1.00 23.89  0  109 LEU   A CG  1 
ATOM   776  C  CD1 . LEU   A  1 94  ? 6.827   -37.640 -32.927 1.00 25.29  0  109 LEU   A CD1 1 
ATOM   777  C  CD2 . LEU   A  1 94  ? 8.540   -35.775 -32.761 1.00 23.66  0  109 LEU   A CD2 1 
ATOM   778  N  N   . LEU   A  1 95  ? 6.171   -32.844 -29.801 1.00 26.39  0  110 LEU   A N   1 
ATOM   779  C  CA  . LEU   A  1 95  ? 5.091   -31.858 -29.556 1.00 25.16  0  110 LEU   A CA  1 
ATOM   780  C  C   . LEU   A  1 95  ? 4.518   -31.454 -30.903 1.00 23.97  0  110 LEU   A C   1 
ATOM   781  O  O   . LEU   A  1 95  ? 5.319   -31.025 -31.757 1.00 22.69  0  110 LEU   A O   1 
ATOM   782  C  CB  . LEU   A  1 95  ? 5.646   -30.649 -28.798 1.00 24.92  0  110 LEU   A CB  1 
ATOM   783  C  CG  . LEU   A  1 95  ? 6.513   -30.952 -27.585 1.00 26.91  0  110 LEU   A CG  1 
ATOM   784  C  CD1 . LEU   A  1 95  ? 7.084   -29.650 -27.005 1.00 27.94  0  110 LEU   A CD1 1 
ATOM   785  C  CD2 . LEU   A  1 95  ? 5.697   -31.714 -26.548 1.00 27.83  0  110 LEU   A CD2 1 
ATOM   786  N  N   . GLU   A  1 96  ? 3.213   -31.613 -31.078 1.00 25.43  0  111 GLU   A N   1 
ATOM   787  C  CA  . GLU   A  1 96  ? 2.473   -31.081 -32.261 1.00 28.24  0  111 GLU   A CA  1 
ATOM   788  C  C   . GLU   A  1 96  ? 1.941   -29.679 -31.921 1.00 25.82  0  111 GLU   A C   1 
ATOM   789  O  O   . GLU   A  1 96  ? 1.162   -29.538 -30.955 1.00 28.70  0  111 GLU   A O   1 
ATOM   790  C  CB  . GLU   A  1 96  ? 1.309   -31.958 -32.764 1.00 29.64  0  111 GLU   A CB  1 
ATOM   791  C  CG  . GLU   A  1 96  ? 0.939   -31.564 -34.201 1.00 31.86  0  111 GLU   A CG  1 
ATOM   792  C  CD  . GLU   A  1 96  ? -0.141  -32.330 -34.932 1.00 37.19  0  111 GLU   A CD  1 
ATOM   793  O  OE1 . GLU   A  1 96  ? -0.867  -33.126 -34.293 1.00 37.26  0  111 GLU   A OE1 1 
ATOM   794  O  OE2 . GLU   A  1 96  ? -0.264  -32.081 -36.157 1.00 44.80  -1 111 GLU   A OE2 1 
ATOM   795  N  N   . LEU   A  1 97  ? 2.315   -28.690 -32.709 1.00 27.64  0  112 LEU   A N   1 
ATOM   796  C  CA  . LEU   A  1 97  ? 1.818   -27.300 -32.527 1.00 29.10  0  112 LEU   A CA  1 
ATOM   797  C  C   . LEU   A  1 97  ? 0.387   -27.236 -33.072 1.00 26.97  0  112 LEU   A C   1 
ATOM   798  O  O   . LEU   A  1 97  ? 0.070   -28.001 -33.946 1.00 27.10  0  112 LEU   A O   1 
ATOM   799  C  CB  . LEU   A  1 97  ? 2.756   -26.332 -33.249 1.00 28.74  0  112 LEU   A CB  1 
ATOM   800  C  CG  . LEU   A  1 97  ? 4.218   -26.391 -32.830 1.00 27.81  0  112 LEU   A CG  1 
ATOM   801  C  CD1 . LEU   A  1 97  ? 5.072   -25.481 -33.693 1.00 27.96  0  112 LEU   A CD1 1 
ATOM   802  C  CD2 . LEU   A  1 97  ? 4.376   -26.027 -31.364 1.00 29.80  0  112 LEU   A CD2 1 
ATOM   803  N  N   . GLU   A  1 98  ? -0.416  -26.291 -32.600 1.00 31.99  0  113 GLU   A N   1 
ATOM   804  C  CA  . GLU   A  1 98  ? -1.824  -26.059 -33.051 1.00 30.64  0  113 GLU   A CA  1 
ATOM   805  C  C   . GLU   A  1 98  ? -1.827  -25.511 -34.474 1.00 25.93  0  113 GLU   A C   1 
ATOM   806  O  O   . GLU   A  1 98  ? -2.836  -25.707 -35.164 1.00 29.52  0  113 GLU   A O   1 
ATOM   807  C  CB  . GLU   A  1 98  ? -2.527  -25.086 -32.113 1.00 30.01  0  113 GLU   A CB  1 
ATOM   808  C  CG  . GLU   A  1 98  ? -2.836  -25.663 -30.761 1.00 30.71  0  113 GLU   A CG  1 
ATOM   809  C  CD  . GLU   A  1 98  ? -3.667  -24.741 -29.885 1.00 31.77  0  113 GLU   A CD  1 
ATOM   810  O  OE1 . GLU   A  1 98  ? -3.840  -25.071 -28.708 1.00 31.47  0  113 GLU   A OE1 1 
ATOM   811  O  OE2 . GLU   A  1 98  ? -4.123  -23.682 -30.371 1.00 28.08  -1 113 GLU   A OE2 1 
ATOM   812  N  N   . GLU   A  1 99  ? -0.732  -24.878 -34.898 1.00 28.89  0  114 GLU   A N   1 
ATOM   813  C  CA  . GLU   A  1 99  ? -0.582  -24.273 -36.242 1.00 30.95  0  114 GLU   A CA  1 
ATOM   814  C  C   . GLU   A  1 99  ? 0.834   -24.485 -36.731 1.00 29.69  0  114 GLU   A C   1 
ATOM   815  O  O   . GLU   A  1 99  ? 1.791   -24.467 -35.942 1.00 28.59  0  114 GLU   A O   1 
ATOM   816  C  CB  . GLU   A  1 99  ? -0.767  -22.741 -36.260 1.00 33.37  0  114 GLU   A CB  1 
ATOM   817  C  CG  . GLU   A  1 99  ? -2.039  -22.239 -35.601 1.00 34.25  0  114 GLU   A CG  1 
ATOM   818  C  CD  . GLU   A  1 99  ? -3.343  -22.596 -36.283 1.00 32.54  0  114 GLU   A CD  1 
ATOM   819  O  OE1 . GLU   A  1 99  ? -3.306  -22.964 -37.484 1.00 33.08  0  114 GLU   A OE1 1 
ATOM   820  O  OE2 . GLU   A  1 99  ? -4.388  -22.496 -35.590 1.00 28.93  -1 114 GLU   A OE2 1 
ATOM   821  N  N   . PRO   A  1 100 ? 1.008   -24.623 -38.054 1.00 31.19  0  115 PRO   A N   1 
ATOM   822  C  CA  . PRO   A  1 100 ? 2.340   -24.709 -38.644 1.00 34.16  0  115 PRO   A CA  1 
ATOM   823  C  C   . PRO   A  1 100 ? 3.005   -23.343 -38.464 1.00 33.77  0  115 PRO   A C   1 
ATOM   824  O  O   . PRO   A  1 100 ? 2.317   -22.367 -38.433 1.00 37.95  0  115 PRO   A O   1 
ATOM   825  C  CB  . PRO   A  1 100 ? 2.079   -25.084 -40.102 1.00 35.41  0  115 PRO   A CB  1 
ATOM   826  C  CG  . PRO   A  1 100 ? 0.690   -24.599 -40.379 1.00 34.16  0  115 PRO   A CG  1 
ATOM   827  C  CD  . PRO   A  1 100 ? -0.051  -24.664 -39.062 1.00 35.23  0  115 PRO   A CD  1 
ATOM   828  N  N   . VAL   A  1 101 ? 4.302   -23.323 -38.218 1.00 31.23  0  116 VAL   A N   1 
ATOM   829  C  CA  . VAL   A  1 101 ? 5.065   -22.054 -38.125 1.00 29.55  0  116 VAL   A CA  1 
ATOM   830  C  C   . VAL   A  1 101 ? 5.480   -21.675 -39.544 1.00 27.49  0  116 VAL   A C   1 
ATOM   831  O  O   . VAL   A  1 101 ? 5.672   -22.579 -40.397 1.00 26.78  0  116 VAL   A O   1 
ATOM   832  C  CB  . VAL   A  1 101 ? 6.273   -22.133 -37.166 1.00 31.21  0  116 VAL   A CB  1 
ATOM   833  C  CG1 . VAL   A  1 101 ? 5.871   -22.648 -35.803 1.00 34.87  0  116 VAL   A CG1 1 
ATOM   834  C  CG2 . VAL   A  1 101 ? 7.439   -22.918 -37.704 1.00 33.94  0  116 VAL   A CG2 1 
ATOM   835  N  N   . LYS   A  1 102 ? 5.722   -20.396 -39.737 1.00 27.09  0  117 LYS   A N   1 
ATOM   836  C  CA  . LYS   A  1 102 ? 6.354   -19.811 -40.930 1.00 32.44  0  117 LYS   A CA  1 
ATOM   837  C  C   . LYS   A  1 102 ? 7.867   -19.892 -40.757 1.00 32.01  0  117 LYS   A C   1 
ATOM   838  O  O   . LYS   A  1 102 ? 8.378   -19.311 -39.818 1.00 36.77  0  117 LYS   A O   1 
ATOM   839  C  CB  . LYS   A  1 102 ? 5.926   -18.349 -41.104 1.00 35.95  0  117 LYS   A CB  1 
ATOM   840  C  CG  . LYS   A  1 102 ? 4.425   -18.108 -41.291 1.00 35.49  0  117 LYS   A CG  1 
ATOM   841  C  CD  . LYS   A  1 102 ? 3.688   -19.099 -42.164 1.00 40.02  0  117 LYS   A CD  1 
ATOM   842  C  CE  . LYS   A  1 102 ? 2.210   -18.765 -42.272 1.00 41.42  0  117 LYS   A CE  1 
ATOM   843  N  NZ  . LYS   A  1 102 ? 1.502   -19.668 -43.207 1.00 45.24  1  117 LYS   A NZ  1 
ATOM   844  N  N   . VAL   A  1 103 ? 8.552   -20.519 -41.689 1.00 29.48  0  118 VAL   A N   1 
ATOM   845  C  CA  . VAL   A  1 103 ? 10.018  -20.715 -41.588 1.00 30.08  0  118 VAL   A CA  1 
ATOM   846  C  C   . VAL   A  1 103 ? 10.713  -19.595 -42.348 1.00 33.07  0  118 VAL   A C   1 
ATOM   847  O  O   . VAL   A  1 103 ? 10.096  -18.930 -43.211 1.00 31.84  0  118 VAL   A O   1 
ATOM   848  C  CB  . VAL   A  1 103 ? 10.455  -22.127 -42.007 1.00 31.94  0  118 VAL   A CB  1 
ATOM   849  C  CG1 . VAL   A  1 103 ? 9.976   -23.160 -41.000 1.00 32.39  0  118 VAL   A CG1 1 
ATOM   850  C  CG2 . VAL   A  1 103 ? 10.022  -22.524 -43.413 1.00 34.26  0  118 VAL   A CG2 1 
ATOM   851  N  N   . SER   A  1 104 ? 11.964  -19.355 -41.981 1.00 29.73  0  119 SER   A N   1 
ATOM   852  C  CA  . SER   A  1 104 ? 12.815  -18.251 -42.473 1.00 34.61  0  119 SER   A CA  1 
ATOM   853  C  C   . SER   A  1 104 ? 14.281  -18.652 -42.263 1.00 36.67  0  119 SER   A C   1 
ATOM   854  O  O   . SER   A  1 104 ? 14.510  -19.742 -41.742 1.00 33.36  0  119 SER   A O   1 
ATOM   855  C  CB  . SER   A  1 104 ? 12.479  -16.976 -41.741 1.00 35.34  0  119 SER   A CB  1 
ATOM   856  O  OG  . SER   A  1 104 ? 12.752  -17.081 -40.352 1.00 34.01  0  119 SER   A OG  1 
ATOM   857  N  N   . SER   A  1 105 ? 15.242  -17.817 -42.640 1.00 37.68  0  120 SER   A N   1 
ATOM   858  C  CA  . SER   A  1 105 ? 16.674  -18.153 -42.407 1.00 46.57  0  120 SER   A CA  1 
ATOM   859  C  C   . SER   A  1 105 ? 16.977  -18.109 -40.894 1.00 40.17  0  120 SER   A C   1 
ATOM   860  O  O   . SER   A  1 105 ? 17.851  -18.856 -40.461 1.00 46.91  0  120 SER   A O   1 
ATOM   861  C  CB  . SER   A  1 105 ? 17.605  -17.301 -43.238 1.00 43.53  0  120 SER   A CB  1 
ATOM   862  O  OG  . SER   A  1 105 ? 17.668  -16.005 -42.700 1.00 50.01  0  120 SER   A OG  1 
ATOM   863  N  N   . HIS   A  1 106 ? 16.245  -17.313 -40.113 1.00 41.50  0  121 HIS   A N   1 
ATOM   864  C  CA  . HIS   A  1 106 ? 16.453  -17.164 -38.650 1.00 42.17  0  121 HIS   A CA  1 
ATOM   865  C  C   . HIS   A  1 106 ? 15.749  -18.284 -37.860 1.00 39.11  0  121 HIS   A C   1 
ATOM   866  O  O   . HIS   A  1 106 ? 16.252  -18.627 -36.782 1.00 39.82  0  121 HIS   A O   1 
ATOM   867  C  CB  . HIS   A  1 106 ? 16.030  -15.766 -38.182 1.00 51.24  0  121 HIS   A CB  1 
ATOM   868  C  CG  . HIS   A  1 106 ? 16.430  -15.488 -36.764 1.00 73.70  0  121 HIS   A CG  1 
ATOM   869  N  ND1 . HIS   A  1 106 ? 17.756  -15.303 -36.380 1.00 71.64  0  121 HIS   A ND1 1 
ATOM   870  C  CD2 . HIS   A  1 106 ? 15.698  -15.439 -35.619 1.00 79.84  0  121 HIS   A CD2 1 
ATOM   871  C  CE1 . HIS   A  1 106 ? 17.814  -15.126 -35.068 1.00 76.99  0  121 HIS   A CE1 1 
ATOM   872  N  NE2 . HIS   A  1 106 ? 16.566  -15.204 -34.581 1.00 79.85  0  121 HIS   A NE2 1 
ATOM   873  N  N   . VAL   A  1 107 ? 14.630  -18.822 -38.355 1.00 32.85  0  122 VAL   A N   1 
ATOM   874  C  CA  . VAL   A  1 107 ? 13.825  -19.869 -37.669 1.00 31.92  0  122 VAL   A CA  1 
ATOM   875  C  C   . VAL   A  1 107 ? 13.438  -20.926 -38.702 1.00 31.93  0  122 VAL   A C   1 
ATOM   876  O  O   . VAL   A  1 107 ? 12.569  -20.637 -39.532 1.00 28.28  0  122 VAL   A O   1 
ATOM   877  C  CB  . VAL   A  1 107 ? 12.575  -19.273 -36.995 1.00 37.37  0  122 VAL   A CB  1 
ATOM   878  C  CG1 . VAL   A  1 107 ? 11.664  -20.343 -36.423 1.00 40.64  0  122 VAL   A CG1 1 
ATOM   879  C  CG2 . VAL   A  1 107 ? 12.923  -18.233 -35.940 1.00 39.31  0  122 VAL   A CG2 1 
ATOM   880  N  N   . HIS   A  1 108 ? 14.018  -22.125 -38.624 1.00 26.69  0  123 HIS   A N   1 
ATOM   881  C  CA  . HIS   A  1 108 ? 13.702  -23.235 -39.563 1.00 27.78  0  123 HIS   A CA  1 
ATOM   882  C  C   . HIS   A  1 108 ? 14.159  -24.583 -38.980 1.00 26.99  0  123 HIS   A C   1 
ATOM   883  O  O   . HIS   A  1 108 ? 14.716  -24.602 -37.861 1.00 25.13  0  123 HIS   A O   1 
ATOM   884  C  CB  . HIS   A  1 108 ? 14.249  -22.947 -40.967 1.00 30.87  0  123 HIS   A CB  1 
ATOM   885  C  CG  . HIS   A  1 108 ? 15.732  -23.013 -41.113 1.00 29.40  0  123 HIS   A CG  1 
ATOM   886  N  ND1 . HIS   A  1 108 ? 16.503  -21.877 -41.299 1.00 32.00  0  123 HIS   A ND1 1 
ATOM   887  C  CD2 . HIS   A  1 108 ? 16.571  -24.064 -41.199 1.00 26.79  0  123 HIS   A CD2 1 
ATOM   888  C  CE1 . HIS   A  1 108 ? 17.770  -22.230 -41.487 1.00 30.40  0  123 HIS   A CE1 1 
ATOM   889  N  NE2 . HIS   A  1 108 ? 17.831  -23.569 -41.429 1.00 30.53  0  123 HIS   A NE2 1 
ATOM   890  N  N   . THR   A  1 109 ? 13.811  -25.658 -39.675 1.00 24.46  0  124 THR   A N   1 
ATOM   891  C  CA  . THR   A  1 109 ? 13.850  -27.034 -39.147 1.00 26.75  0  124 THR   A CA  1 
ATOM   892  C  C   . THR   A  1 109 ? 15.279  -27.553 -39.216 1.00 27.88  0  124 THR   A C   1 
ATOM   893  O  O   . THR   A  1 109 ? 16.080  -27.033 -40.023 1.00 28.01  0  124 THR   A O   1 
ATOM   894  C  CB  . THR   A  1 109 ? 12.940  -28.004 -39.896 1.00 22.55  0  124 THR   A CB  1 
ATOM   895  O  OG1 . THR   A  1 109 ? 13.416  -27.976 -41.236 1.00 27.37  0  124 THR   A OG1 1 
ATOM   896  C  CG2 . THR   A  1 109 ? 11.482  -27.659 -39.840 1.00 26.98  0  124 THR   A CG2 1 
ATOM   897  N  N   . VAL   A  1 110 ? 15.574  -28.535 -38.369 1.00 30.38  0  125 VAL   A N   1 
ATOM   898  C  CA  . VAL   A  1 110 ? 16.855  -29.296 -38.407 1.00 28.79  0  125 VAL   A CA  1 
ATOM   899  C  C   . VAL   A  1 110 ? 16.564  -30.570 -39.207 1.00 26.71  0  125 VAL   A C   1 
ATOM   900  O  O   . VAL   A  1 110 ? 15.429  -31.073 -39.153 1.00 27.13  0  125 VAL   A O   1 
ATOM   901  C  CB  . VAL   A  1 110 ? 17.418  -29.580 -36.996 1.00 24.74  0  125 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A  1 110 ? 16.531  -30.533 -36.213 1.00 25.39  0  125 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A  1 110 ? 18.841  -30.108 -37.028 1.00 24.90  0  125 VAL   A CG2 1 
ATOM   904  N  N   . THR   A  1 111 ? 17.563  -31.049 -39.927 1.00 25.34  0  126 THR   A N   1 
ATOM   905  C  CA  . THR   A  1 111 ? 17.514  -32.317 -40.709 1.00 26.13  0  126 THR   A CA  1 
ATOM   906  C  C   . THR   A  1 111 ? 17.802  -33.499 -39.770 1.00 28.92  0  126 THR   A C   1 
ATOM   907  O  O   . THR   A  1 111 ? 18.796  -33.446 -39.006 1.00 27.60  0  126 THR   A O   1 
ATOM   908  C  CB  . THR   A  1 111 ? 18.521  -32.250 -41.859 1.00 28.83  0  126 THR   A CB  1 
ATOM   909  O  OG1 . THR   A  1 111 ? 18.313  -31.021 -42.549 1.00 31.93  0  126 THR   A OG1 1 
ATOM   910  C  CG2 . THR   A  1 111 ? 18.447  -33.416 -42.815 1.00 30.40  0  126 THR   A CG2 1 
ATOM   911  N  N   . LEU   A  1 112 ? 16.958  -34.515 -39.827 1.00 28.88  0  127 LEU   A N   1 
ATOM   912  C  CA  . LEU   A  1 112 ? 17.176  -35.808 -39.140 1.00 31.76  0  127 LEU   A CA  1 
ATOM   913  C  C   . LEU   A  1 112 ? 18.206  -36.619 -39.914 1.00 30.91  0  127 LEU   A C   1 
ATOM   914  O  O   . LEU   A  1 112 ? 18.250  -36.579 -41.135 1.00 29.32  0  127 LEU   A O   1 
ATOM   915  C  CB  . LEU   A  1 112 ? 15.836  -36.530 -39.034 1.00 29.71  0  127 LEU   A CB  1 
ATOM   916  C  CG  . LEU   A  1 112 ? 14.786  -35.813 -38.192 1.00 31.91  0  127 LEU   A CG  1 
ATOM   917  C  CD1 . LEU   A  1 112 ? 13.521  -36.637 -38.086 1.00 34.94  0  127 LEU   A CD1 1 
ATOM   918  C  CD2 . LEU   A  1 112 ? 15.307  -35.553 -36.798 1.00 36.56  0  127 LEU   A CD2 1 
ATOM   919  N  N   . PRO   A  1 113 ? 19.055  -37.393 -39.225 1.00 33.05  0  128 PRO   A N   1 
ATOM   920  C  CA  . PRO   A  1 113 ? 20.071  -38.188 -39.902 1.00 33.73  0  128 PRO   A CA  1 
ATOM   921  C  C   . PRO   A  1 113 ? 19.444  -39.389 -40.606 1.00 33.25  0  128 PRO   A C   1 
ATOM   922  O  O   . PRO   A  1 113 ? 18.387  -39.860 -40.200 1.00 28.57  0  128 PRO   A O   1 
ATOM   923  C  CB  . PRO   A  1 113 ? 20.987  -38.659 -38.762 1.00 33.38  0  128 PRO   A CB  1 
ATOM   924  C  CG  . PRO   A  1 113 ? 20.106  -38.657 -37.537 1.00 36.63  0  128 PRO   A CG  1 
ATOM   925  C  CD  . PRO   A  1 113 ? 19.075  -37.576 -37.770 1.00 35.92  0  128 PRO   A CD  1 
ATOM   926  N  N   . PRO   A  1 114 ? 20.094  -39.924 -41.661 1.00 33.46  0  129 PRO   A N   1 
ATOM   927  C  CA  . PRO   A  1 114 ? 19.701  -41.209 -42.225 1.00 35.69  0  129 PRO   A CA  1 
ATOM   928  C  C   . PRO   A  1 114 ? 20.040  -42.321 -41.227 1.00 33.42  0  129 PRO   A C   1 
ATOM   929  O  O   . PRO   A  1 114 ? 21.000  -42.158 -40.450 1.00 35.91  0  129 PRO   A O   1 
ATOM   930  C  CB  . PRO   A  1 114 ? 20.564  -41.295 -43.503 1.00 38.03  0  129 PRO   A CB  1 
ATOM   931  C  CG  . PRO   A  1 114 ? 21.798  -40.503 -43.170 1.00 38.19  0  129 PRO   A CG  1 
ATOM   932  C  CD  . PRO   A  1 114 ? 21.274  -39.350 -42.335 1.00 38.18  0  129 PRO   A CD  1 
ATOM   933  N  N   . ALA   A  1 115 ? 19.295  -43.417 -41.290 1.00 36.60  0  130 ALA   A N   1 
ATOM   934  C  CA  . ALA   A  1 115 ? 19.372  -44.583 -40.374 1.00 38.47  0  130 ALA   A CA  1 
ATOM   935  C  C   . ALA   A  1 115 ? 20.815  -45.099 -40.229 1.00 39.13  0  130 ALA   A C   1 
ATOM   936  O  O   . ALA   A  1 115 ? 21.191  -45.517 -39.121 1.00 41.53  0  130 ALA   A O   1 
ATOM   937  C  CB  . ALA   A  1 115 ? 18.439  -45.654 -40.865 1.00 43.69  0  130 ALA   A CB  1 
ATOM   938  N  N   . SER   A  1 116 ? 21.620  -45.031 -41.278 1.00 39.55  0  131 SER   A N   1 
ATOM   939  C  CA  . SER   A  1 116 ? 22.989  -45.623 -41.299 1.00 44.19  0  131 SER   A CA  1 
ATOM   940  C  C   . SER   A  1 116 ? 24.018  -44.760 -40.541 1.00 39.37  0  131 SER   A C   1 
ATOM   941  O  O   . SER   A  1 116 ? 25.119  -45.285 -40.281 1.00 36.31  0  131 SER   A O   1 
ATOM   942  C  CB  . SER   A  1 116 ? 23.427  -45.878 -42.724 1.00 40.80  0  131 SER   A CB  1 
ATOM   943  O  OG  . SER   A  1 116 ? 23.389  -44.683 -43.463 1.00 44.32  0  131 SER   A OG  1 
ATOM   944  N  N   . GLU   A  1 117 ? 23.733  -43.488 -40.234 1.00 36.15  0  132 GLU   A N   1 
ATOM   945  C  CA  . GLU   A  1 117 ? 24.779  -42.596 -39.649 1.00 40.17  0  132 GLU   A CA  1 
ATOM   946  C  C   . GLU   A  1 117 ? 25.038  -43.004 -38.189 1.00 41.74  0  132 GLU   A C   1 
ATOM   947  O  O   . GLU   A  1 117 ? 24.077  -42.984 -37.396 1.00 41.30  0  132 GLU   A O   1 
ATOM   948  C  CB  . GLU   A  1 117 ? 24.373  -41.126 -39.772 1.00 40.92  0  132 GLU   A CB  1 
ATOM   949  C  CG  . GLU   A  1 117 ? 25.385  -40.160 -39.188 1.00 43.63  0  132 GLU   A CG  1 
ATOM   950  C  CD  . GLU   A  1 117 ? 26.788  -40.237 -39.772 1.00 50.00  0  132 GLU   A CD  1 
ATOM   951  O  OE1 . GLU   A  1 117 ? 26.913  -40.008 -40.987 1.00 47.92  0  132 GLU   A OE1 1 
ATOM   952  O  OE2 . GLU   A  1 117 ? 27.740  -40.552 -39.009 1.00 49.44  -1 132 GLU   A OE2 1 
ATOM   953  N  N   . THR   A  1 118 ? 26.287  -43.327 -37.828 1.00 40.19  0  133 THR   A N   1 
ATOM   954  C  CA  . THR   A  1 118 ? 26.671  -43.831 -36.475 1.00 40.36  0  133 THR   A CA  1 
ATOM   955  C  C   . THR   A  1 118 ? 27.229  -42.713 -35.580 1.00 39.45  0  133 THR   A C   1 
ATOM   956  O  O   . THR   A  1 118 ? 27.309  -42.927 -34.348 1.00 42.11  0  133 THR   A O   1 
ATOM   957  C  CB  . THR   A  1 118 ? 27.715  -44.959 -36.549 1.00 40.97  0  133 THR   A CB  1 
ATOM   958  O  OG1 . THR   A  1 118 ? 28.906  -44.446 -37.147 1.00 40.61  0  133 THR   A OG1 1 
ATOM   959  C  CG2 . THR   A  1 118 ? 27.219  -46.168 -37.308 1.00 40.02  0  133 THR   A CG2 1 
ATOM   960  N  N   . PHE   A  1 119 ? 27.652  -41.603 -36.180 1.00 35.70  0  134 PHE   A N   1 
ATOM   961  C  CA  . PHE   A  1 119 ? 28.310  -40.443 -35.530 1.00 36.14  0  134 PHE   A CA  1 
ATOM   962  C  C   . PHE   A  1 119 ? 29.538  -40.892 -34.743 1.00 39.33  0  134 PHE   A C   1 
ATOM   963  O  O   . PHE   A  1 119 ? 29.549  -40.839 -33.508 1.00 37.39  0  134 PHE   A O   1 
ATOM   964  C  CB  . PHE   A  1 119 ? 27.294  -39.665 -34.690 1.00 33.93  0  134 PHE   A CB  1 
ATOM   965  C  CG  . PHE   A  1 119 ? 26.170  -39.079 -35.494 1.00 28.11  0  134 PHE   A CG  1 
ATOM   966  C  CD1 . PHE   A  1 119 ? 26.338  -37.902 -36.207 1.00 26.92  0  134 PHE   A CD1 1 
ATOM   967  C  CD2 . PHE   A  1 119 ? 24.940  -39.694 -35.502 1.00 26.66  0  134 PHE   A CD2 1 
ATOM   968  C  CE1 . PHE   A  1 119 ? 25.292  -37.369 -36.942 1.00 28.01  0  134 PHE   A CE1 1 
ATOM   969  C  CE2 . PHE   A  1 119 ? 23.881  -39.127 -36.194 1.00 28.41  0  134 PHE   A CE2 1 
ATOM   970  C  CZ  . PHE   A  1 119 ? 24.058  -37.974 -36.921 1.00 26.47  0  134 PHE   A CZ  1 
ATOM   971  N  N   . PRO   A  1 120 ? 30.625  -41.327 -35.422 1.00 42.17  0  135 PRO   A N   1 
ATOM   972  C  CA  . PRO   A  1 120 ? 31.798  -41.830 -34.710 1.00 41.16  0  135 PRO   A CA  1 
ATOM   973  C  C   . PRO   A  1 120 ? 32.606  -40.709 -34.069 1.00 37.96  0  135 PRO   A C   1 
ATOM   974  O  O   . PRO   A  1 120 ? 32.457  -39.537 -34.416 1.00 42.75  0  135 PRO   A O   1 
ATOM   975  C  CB  . PRO   A  1 120 ? 32.614  -42.500 -35.821 1.00 40.15  0  135 PRO   A CB  1 
ATOM   976  C  CG  . PRO   A  1 120 ? 32.265  -41.686 -37.061 1.00 43.73  0  135 PRO   A CG  1 
ATOM   977  C  CD  . PRO   A  1 120 ? 30.801  -41.347 -36.890 1.00 42.60  0  135 PRO   A CD  1 
ATOM   978  N  N   . PRO   A  1 121 ? 33.509  -41.041 -33.129 1.00 35.02  0  136 PRO   A N   1 
ATOM   979  C  CA  . PRO   A  1 121 ? 34.435  -40.065 -32.565 1.00 36.87  0  136 PRO   A CA  1 
ATOM   980  C  C   . PRO   A  1 121 ? 35.191  -39.258 -33.626 1.00 39.11  0  136 PRO   A C   1 
ATOM   981  O  O   . PRO   A  1 121 ? 35.526  -39.796 -34.657 1.00 39.58  0  136 PRO   A O   1 
ATOM   982  C  CB  . PRO   A  1 121 ? 35.432  -40.925 -31.758 1.00 38.48  0  136 PRO   A CB  1 
ATOM   983  C  CG  . PRO   A  1 121 ? 34.650  -42.196 -31.418 1.00 38.16  0  136 PRO   A CG  1 
ATOM   984  C  CD  . PRO   A  1 121 ? 33.681  -42.389 -32.562 1.00 38.67  0  136 PRO   A CD  1 
ATOM   985  N  N   . GLY   A  1 122 ? 35.450  -37.976 -33.336 1.00 40.76  0  137 GLY   A N   1 
ATOM   986  C  CA  . GLY   A  1 122 ? 36.117  -37.020 -34.229 1.00 42.59  0  137 GLY   A CA  1 
ATOM   987  C  C   . GLY   A  1 122 ? 35.142  -36.318 -35.151 1.00 43.17  0  137 GLY   A C   1 
ATOM   988  O  O   . GLY   A  1 122 ? 35.575  -35.411 -35.847 1.00 47.76  0  137 GLY   A O   1 
ATOM   989  N  N   . MET   A  1 123 ? 33.869  -36.703 -35.155 1.00 47.38  0  138 MET   A N   1 
ATOM   990  C  CA  . MET   A  1 123 ? 32.805  -35.879 -35.785 1.00 56.88  0  138 MET   A CA  1 
ATOM   991  C  C   . MET   A  1 123 ? 32.761  -34.538 -35.039 1.00 51.79  0  138 MET   A C   1 
ATOM   992  O  O   . MET   A  1 123 ? 32.789  -34.515 -33.808 1.00 44.60  0  138 MET   A O   1 
ATOM   993  C  CB  . MET   A  1 123 ? 31.446  -36.590 -35.710 1.00 64.55  0  138 MET   A CB  1 
ATOM   994  C  CG  . MET   A  1 123 ? 30.516  -36.266 -36.861 1.00 70.11  0  138 MET   A CG  1 
ATOM   995  S  SD  . MET   A  1 123 ? 31.071  -37.035 -38.398 1.00 79.93  0  138 MET   A SD  1 
ATOM   996  C  CE  . MET   A  1 123 ? 29.719  -38.160 -38.729 1.00 80.72  0  138 MET   A CE  1 
ATOM   997  N  N   . PRO   A  1 124 ? 32.698  -33.378 -35.739 1.00 46.89  0  139 PRO   A N   1 
ATOM   998  C  CA  . PRO   A  1 124 ? 32.426  -32.094 -35.092 1.00 44.58  0  139 PRO   A CA  1 
ATOM   999  C  C   . PRO   A  1 124 ? 30.943  -31.991 -34.701 1.00 36.20  0  139 PRO   A C   1 
ATOM   1000 O  O   . PRO   A  1 124 ? 30.113  -32.010 -35.585 1.00 39.35  0  139 PRO   A O   1 
ATOM   1001 C  CB  . PRO   A  1 124 ? 32.852  -31.068 -36.162 1.00 46.86  0  139 PRO   A CB  1 
ATOM   1002 C  CG  . PRO   A  1 124 ? 32.599  -31.767 -37.468 1.00 44.45  0  139 PRO   A CG  1 
ATOM   1003 C  CD  . PRO   A  1 124 ? 32.898  -33.226 -37.191 1.00 50.02  0  139 PRO   A CD  1 
ATOM   1004 N  N   . CYS   A  1 125 ? 30.645  -31.929 -33.391 1.00 32.69  0  140 CYS   A N   1 
ATOM   1005 C  CA  . CYS   A  1 125 ? 29.261  -31.849 -32.858 1.00 33.18  0  140 CYS   A CA  1 
ATOM   1006 C  C   . CYS   A  1 125 ? 29.149  -30.739 -31.824 1.00 32.90  0  140 CYS   A C   1 
ATOM   1007 O  O   . CYS   A  1 125 ? 30.108  -30.511 -31.050 1.00 29.18  0  140 CYS   A O   1 
ATOM   1008 C  CB  . CYS   A  1 125 ? 28.762  -33.156 -32.252 1.00 34.85  0  140 CYS   A CB  1 
ATOM   1009 S  SG  . CYS   A  1 125 ? 29.012  -34.560 -33.369 1.00 41.06  0  140 CYS   A SG  1 
ATOM   1010 N  N   . TRP   A  1 126 ? 27.974  -30.119 -31.795 1.00 29.13  0  141 TRP   A N   1 
ATOM   1011 C  CA  A TRP   A  1 126 ? 27.638  -28.981 -30.891 0.50 29.41  0  141 TRP   A CA  1 
ATOM   1012 C  CA  B TRP   A  1 126 ? 27.646  -28.990 -30.877 0.50 27.96  0  141 TRP   A CA  1 
ATOM   1013 C  C   . TRP   A  1 126 ? 26.340  -29.298 -30.141 1.00 27.10  0  141 TRP   A C   1 
ATOM   1014 O  O   . TRP   A  1 126 ? 25.455  -29.905 -30.753 1.00 26.28  0  141 TRP   A O   1 
ATOM   1015 C  CB  A TRP   A  1 126 ? 27.478  -27.688 -31.689 0.50 29.43  0  141 TRP   A CB  1 
ATOM   1016 C  CB  B TRP   A  1 126 ? 27.521  -27.674 -31.640 0.50 26.10  0  141 TRP   A CB  1 
ATOM   1017 C  CG  A TRP   A  1 126 ? 28.711  -27.271 -32.422 0.50 32.22  0  141 TRP   A CG  1 
ATOM   1018 C  CG  B TRP   A  1 126 ? 28.813  -26.946 -31.821 0.50 26.62  0  141 TRP   A CG  1 
ATOM   1019 C  CD1 A TRP   A  1 126 ? 29.244  -27.836 -33.545 0.50 32.95  0  141 TRP   A CD1 1 
ATOM   1020 C  CD1 B TRP   A  1 126 ? 29.303  -25.933 -31.050 0.50 25.98  0  141 TRP   A CD1 1 
ATOM   1021 C  CD2 A TRP   A  1 126 ? 29.592  -26.204 -32.056 0.50 34.84  0  141 TRP   A CD2 1 
ATOM   1022 C  CD2 B TRP   A  1 126 ? 29.773  -27.149 -32.879 0.50 27.72  0  141 TRP   A CD2 1 
ATOM   1023 N  NE1 A TRP   A  1 126 ? 30.393  -27.189 -33.908 0.50 32.73  0  141 TRP   A NE1 1 
ATOM   1024 N  NE1 B TRP   A  1 126 ? 30.510  -25.502 -31.546 0.50 27.30  0  141 TRP   A NE1 1 
ATOM   1025 C  CE2 A TRP   A  1 126 ? 30.634  -26.191 -33.010 0.50 33.64  0  141 TRP   A CE2 1 
ATOM   1026 C  CE2 B TRP   A  1 126 ? 30.825  -26.235 -32.665 0.50 27.96  0  141 TRP   A CE2 1 
ATOM   1027 C  CE3 A TRP   A  1 126 ? 29.600  -25.265 -31.023 0.50 35.45  0  141 TRP   A CE3 1 
ATOM   1028 C  CE3 B TRP   A  1 126 ? 29.859  -28.027 -33.964 0.50 30.30  0  141 TRP   A CE3 1 
ATOM   1029 C  CZ2 A TRP   A  1 126 ? 31.663  -25.258 -32.965 0.50 36.06  0  141 TRP   A CZ2 1 
ATOM   1030 C  CZ2 B TRP   A  1 126 ? 31.929  -26.165 -33.516 0.50 30.94  0  141 TRP   A CZ2 1 
ATOM   1031 C  CZ3 A TRP   A  1 126 ? 30.623  -24.344 -30.981 0.50 36.48  0  141 TRP   A CZ3 1 
ATOM   1032 C  CZ3 B TRP   A  1 126 ? 30.949  -27.953 -34.805 0.50 31.32  0  141 TRP   A CZ3 1 
ATOM   1033 C  CH2 A TRP   A  1 126 ? 31.627  -24.339 -31.946 0.50 36.66  0  141 TRP   A CH2 1 
ATOM   1034 C  CH2 B TRP   A  1 126 ? 31.970  -27.033 -34.585 0.50 30.53  0  141 TRP   A CH2 1 
ATOM   1035 N  N   . VAL   A  1 127 ? 26.243  -28.863 -28.890 1.00 26.43  0  142 VAL   A N   1 
ATOM   1036 C  CA  . VAL   A  1 127 ? 24.975  -28.942 -28.119 1.00 25.35  0  142 VAL   A CA  1 
ATOM   1037 C  C   . VAL   A  1 127 ? 24.672  -27.516 -27.659 1.00 24.71  0  142 VAL   A C   1 
ATOM   1038 O  O   . VAL   A  1 127 ? 25.621  -26.732 -27.396 1.00 26.88  0  142 VAL   A O   1 
ATOM   1039 C  CB  . VAL   A  1 127 ? 25.069  -29.961 -26.978 1.00 24.99  0  142 VAL   A CB  1 
ATOM   1040 C  CG1 . VAL   A  1 127 ? 26.161  -29.606 -25.988 1.00 27.78  0  142 VAL   A CG1 1 
ATOM   1041 C  CG2 . VAL   A  1 127 ? 23.737  -30.143 -26.278 1.00 25.95  0  142 VAL   A CG2 1 
ATOM   1042 N  N   . THR   A  1 128 ? 23.391  -27.172 -27.631 1.00 26.91  0  143 THR   A N   1 
ATOM   1043 C  CA  . THR   A  1 128 ? 22.910  -25.788 -27.432 1.00 27.06  0  143 THR   A CA  1 
ATOM   1044 C  C   . THR   A  1 128 ? 21.798  -25.787 -26.381 1.00 25.97  0  143 THR   A C   1 
ATOM   1045 O  O   . THR   A  1 128 ? 21.064  -26.779 -26.276 1.00 24.38  0  143 THR   A O   1 
ATOM   1046 C  CB  . THR   A  1 128 ? 22.474  -25.185 -28.774 1.00 25.64  0  143 THR   A CB  1 
ATOM   1047 O  OG1 . THR   A  1 128 ? 21.497  -26.011 -29.398 1.00 26.81  0  143 THR   A OG1 1 
ATOM   1048 C  CG2 . THR   A  1 128 ? 23.608  -25.021 -29.736 1.00 24.34  0  143 THR   A CG2 1 
ATOM   1049 N  N   . GLY   A  1 129 ? 21.688  -24.695 -25.631 1.00 25.36  0  144 GLY   A N   1 
ATOM   1050 C  CA  . GLY   A  1 129 ? 20.544  -24.491 -24.730 1.00 23.79  0  144 GLY   A CA  1 
ATOM   1051 C  C   . GLY   A  1 129 ? 20.776  -23.386 -23.742 1.00 24.62  0  144 GLY   A C   1 
ATOM   1052 O  O   . GLY   A  1 129 ? 21.827  -22.697 -23.823 1.00 23.73  0  144 GLY   A O   1 
ATOM   1053 N  N   . TRP   A  1 130 ? 19.774  -23.191 -22.890 1.00 25.78  0  145 TRP   A N   1 
ATOM   1054 C  CA  . TRP   A  1 130 ? 19.686  -22.131 -21.857 1.00 25.55  0  145 TRP   A CA  1 
ATOM   1055 C  C   . TRP   A  1 130 ? 19.813  -22.739 -20.463 1.00 28.76  0  145 TRP   A C   1 
ATOM   1056 O  O   . TRP   A  1 130 ? 19.295  -22.117 -19.488 1.00 30.82  0  145 TRP   A O   1 
ATOM   1057 C  CB  . TRP   A  1 130 ? 18.354  -21.395 -21.990 1.00 27.09  0  145 TRP   A CB  1 
ATOM   1058 C  CG  . TRP   A  1 130 ? 18.194  -20.619 -23.255 1.00 25.19  0  145 TRP   A CG  1 
ATOM   1059 C  CD1 . TRP   A  1 130 ? 18.642  -19.361 -23.515 1.00 26.10  0  145 TRP   A CD1 1 
ATOM   1060 C  CD2 . TRP   A  1 130 ? 17.457  -21.035 -24.407 1.00 26.28  0  145 TRP   A CD2 1 
ATOM   1061 N  NE1 . TRP   A  1 130 ? 18.266  -18.982 -24.762 1.00 26.88  0  145 TRP   A NE1 1 
ATOM   1062 C  CE2 . TRP   A  1 130 ? 17.525  -19.978 -25.331 1.00 26.38  0  145 TRP   A CE2 1 
ATOM   1063 C  CE3 . TRP   A  1 130 ? 16.733  -22.181 -24.734 1.00 24.70  0  145 TRP   A CE3 1 
ATOM   1064 C  CZ2 . TRP   A  1 130 ? 16.919  -20.050 -26.581 1.00 26.87  0  145 TRP   A CZ2 1 
ATOM   1065 C  CZ3 . TRP   A  1 130 ? 16.124  -22.247 -25.963 1.00 29.19  0  145 TRP   A CZ3 1 
ATOM   1066 C  CH2 . TRP   A  1 130 ? 16.219  -21.195 -26.880 1.00 29.30  0  145 TRP   A CH2 1 
ATOM   1067 N  N   . GLY   A  1 131 ? 20.495  -23.889 -20.350 1.00 28.69  0  146 GLY   A N   1 
ATOM   1068 C  CA  . GLY   A  1 131 ? 20.602  -24.594 -19.067 1.00 27.37  0  146 GLY   A CA  1 
ATOM   1069 C  C   . GLY   A  1 131 ? 21.730  -24.050 -18.223 1.00 27.37  0  146 GLY   A C   1 
ATOM   1070 O  O   . GLY   A  1 131 ? 22.485  -23.113 -18.665 1.00 24.73  0  146 GLY   A O   1 
ATOM   1071 N  N   . ASP   A  1 132 ? 21.896  -24.683 -17.068 1.00 27.22  0  147 ASP   A N   1 
ATOM   1072 C  CA  . ASP   A  1 132 ? 22.938  -24.357 -16.066 1.00 27.46  0  147 ASP   A CA  1 
ATOM   1073 C  C   . ASP   A  1 132 ? 24.321  -24.334 -16.719 1.00 27.45  0  147 ASP   A C   1 
ATOM   1074 O  O   . ASP   A  1 132 ? 24.617  -25.154 -17.641 1.00 26.49  0  147 ASP   A O   1 
ATOM   1075 C  CB  . ASP   A  1 132 ? 22.845  -25.320 -14.881 1.00 27.44  0  147 ASP   A CB  1 
ATOM   1076 C  CG  . ASP   A  1 132 ? 21.615  -25.153 -13.991 1.00 29.62  0  147 ASP   A CG  1 
ATOM   1077 O  OD1 . ASP   A  1 132 ? 20.789  -24.238 -14.238 1.00 27.79  0  147 ASP   A OD1 1 
ATOM   1078 O  OD2 . ASP   A  1 132 ? 21.507  -25.915 -13.000 1.00 32.78  -1 147 ASP   A OD2 1 
ATOM   1079 N  N   . VAL   A  1 133 ? 25.161  -23.413 -16.258 1.00 26.30  0  148 VAL   A N   1 
ATOM   1080 C  CA  . VAL   A  1 133 ? 26.549  -23.217 -16.756 1.00 28.12  0  148 VAL   A CA  1 
ATOM   1081 C  C   . VAL   A  1 133 ? 27.540  -24.034 -15.930 1.00 28.85  0  148 VAL   A C   1 
ATOM   1082 O  O   . VAL   A  1 133 ? 28.725  -24.098 -16.329 1.00 33.14  0  148 VAL   A O   1 
ATOM   1083 C  CB  . VAL   A  1 133 ? 26.935  -21.728 -16.823 1.00 31.42  0  148 VAL   A CB  1 
ATOM   1084 C  CG1 . VAL   A  1 133 ? 25.993  -20.995 -17.764 1.00 32.86  0  148 VAL   A CG1 1 
ATOM   1085 C  CG2 . VAL   A  1 133 ? 26.942  -21.057 -15.459 1.00 32.69  0  148 VAL   A CG2 1 
ATOM   1086 N  N   . ASP   A  1 134 ? 27.064  -24.748 -14.912 1.00 32.94  0  149 ASP   A N   1 
ATOM   1087 C  CA  . ASP   A  1 134 ? 27.843  -25.749 -14.125 1.00 31.85  0  149 ASP   A CA  1 
ATOM   1088 C  C   . ASP   A  1 134 ? 26.861  -26.406 -13.148 1.00 31.79  0  149 ASP   A C   1 
ATOM   1089 O  O   . ASP   A  1 134 ? 25.702  -25.917 -13.060 1.00 30.47  0  149 ASP   A O   1 
ATOM   1090 C  CB  . ASP   A  1 134 ? 29.027  -25.102 -13.382 1.00 34.43  0  149 ASP   A CB  1 
ATOM   1091 C  CG  . ASP   A  1 134 ? 30.189  -26.041 -13.122 1.00 38.30  0  149 ASP   A CG  1 
ATOM   1092 O  OD1 . ASP   A  1 134 ? 29.972  -27.246 -12.954 1.00 40.64  0  149 ASP   A OD1 1 
ATOM   1093 O  OD2 . ASP   A  1 134 ? 31.303  -25.569 -13.151 1.00 44.74  -1 149 ASP   A OD2 1 
ATOM   1094 N  N   . ASN   A  1 135 ? 27.287  -27.440 -12.421 1.00 33.56  0  150 ASN   A N   1 
ATOM   1095 C  CA  . ASN   A  1 135 ? 26.429  -28.114 -11.403 1.00 34.85  0  150 ASN   A CA  1 
ATOM   1096 C  C   . ASN   A  1 135 ? 25.854  -27.047 -10.444 1.00 35.63  0  150 ASN   A C   1 
ATOM   1097 O  O   . ASN   A  1 135 ? 26.651  -26.278 -9.861  1.00 31.58  0  150 ASN   A O   1 
ATOM   1098 C  CB  . ASN   A  1 135 ? 27.180  -29.205 -10.645 1.00 32.40  0  150 ASN   A CB  1 
ATOM   1099 C  CG  . ASN   A  1 135 ? 27.709  -30.292 -11.569 1.00 35.11  0  150 ASN   A CG  1 
ATOM   1100 O  OD1 . ASN   A  1 135 ? 26.952  -31.064 -12.167 1.00 31.86  0  150 ASN   A OD1 1 
ATOM   1101 N  ND2 . ASN   A  1 135 ? 29.015  -30.332 -11.719 1.00 31.83  0  150 ASN   A ND2 1 
ATOM   1102 N  N   . ASP   A  1 136 ? 24.523  -26.974 -10.348 1.00 34.73  0  151 ASP   A N   1 
ATOM   1103 C  CA  A ASP   A  1 136 ? 23.779  -26.077 -9.415  0.70 40.30  0  151 ASP   A CA  1 
ATOM   1104 C  CA  B ASP   A  1 136 ? 23.773  -26.078 -9.424  0.30 36.83  0  151 ASP   A CA  1 
ATOM   1105 C  C   . ASP   A  1 136 ? 24.154  -24.607 -9.651  1.00 36.97  0  151 ASP   A C   1 
ATOM   1106 O  O   . ASP   A  1 136 ? 24.057  -23.847 -8.707  1.00 38.16  0  151 ASP   A O   1 
ATOM   1107 C  CB  A ASP   A  1 136 ? 24.003  -26.446 -7.942  0.70 43.36  0  151 ASP   A CB  1 
ATOM   1108 C  CB  B ASP   A  1 136 ? 23.967  -26.498 -7.960  0.30 36.48  0  151 ASP   A CB  1 
ATOM   1109 C  CG  A ASP   A  1 136 ? 23.706  -27.894 -7.636  0.70 47.53  0  151 ASP   A CG  1 
ATOM   1110 C  CG  B ASP   A  1 136 ? 22.800  -26.126 -7.057  0.00 36.09  0  151 ASP   A CG  1 
ATOM   1111 O  OD1 A ASP   A  1 136 ? 22.530  -28.256 -7.673  0.70 54.70  0  151 ASP   A OD1 1 
ATOM   1112 O  OD1 B ASP   A  1 136 ? 21.788  -25.624 -7.584  0.00 35.72  0  151 ASP   A OD1 1 
ATOM   1113 O  OD2 A ASP   A  1 136 ? 24.653  -28.631 -7.347  0.70 56.47  -1 151 ASP   A OD2 1 
ATOM   1114 O  OD2 B ASP   A  1 136 ? 22.918  -26.336 -5.834  0.00 35.72  -1 151 ASP   A OD2 1 
ATOM   1115 N  N   . GLU   A  1 137 ? 24.544  -24.208 -10.869 1.00 35.45  0  152 GLU   A N   1 
ATOM   1116 C  CA  . GLU   A  1 137 ? 24.812  -22.785 -11.222 1.00 36.61  0  152 GLU   A CA  1 
ATOM   1117 C  C   . GLU   A  1 137 ? 23.908  -22.411 -12.404 1.00 35.22  0  152 GLU   A C   1 
ATOM   1118 O  O   . GLU   A  1 137 ? 24.173  -22.882 -13.561 1.00 29.92  0  152 GLU   A O   1 
ATOM   1119 C  CB  . GLU   A  1 137 ? 26.270  -22.528 -11.600 1.00 42.35  0  152 GLU   A CB  1 
ATOM   1120 C  CG  . GLU   A  1 137 ? 27.198  -22.334 -10.435 1.00 51.02  0  152 GLU   A CG  1 
ATOM   1121 C  CD  . GLU   A  1 137 ? 28.655  -22.187 -10.856 1.00 56.01  0  152 GLU   A CD  1 
ATOM   1122 O  OE1 . GLU   A  1 137 ? 28.918  -21.517 -11.895 1.00 51.52  0  152 GLU   A OE1 1 
ATOM   1123 O  OE2 . GLU   A  1 137 ? 29.532  -22.768 -10.158 1.00 61.73  -1 152 GLU   A OE2 1 
ATOM   1124 N  N   . ARG   A  1 138 ? 22.927  -21.559 -12.131 1.00 30.48  0  153 ARG   A N   1 
ATOM   1125 C  CA  . ARG   A  1 138 ? 21.959  -21.053 -13.134 1.00 32.84  0  153 ARG   A CA  1 
ATOM   1126 C  C   . ARG   A  1 138 ? 22.685  -20.257 -14.227 1.00 31.35  0  153 ARG   A C   1 
ATOM   1127 O  O   . ARG   A  1 138 ? 23.691  -19.571 -13.933 1.00 29.84  0  153 ARG   A O   1 
ATOM   1128 C  CB  . ARG   A  1 138 ? 20.909  -20.124 -12.515 1.00 35.93  0  153 ARG   A CB  1 
ATOM   1129 C  CG  . ARG   A  1 138 ? 20.028  -20.736 -11.431 1.00 41.78  0  153 ARG   A CG  1 
ATOM   1130 C  CD  . ARG   A  1 138 ? 19.139  -21.856 -11.915 1.00 42.59  0  153 ARG   A CD  1 
ATOM   1131 N  NE  . ARG   A  1 138 ? 19.788  -23.167 -11.792 1.00 45.90  0  153 ARG   A NE  1 
ATOM   1132 C  CZ  . ARG   A  1 138 ? 19.957  -23.870 -10.658 1.00 49.14  0  153 ARG   A CZ  1 
ATOM   1133 N  NH1 . ARG   A  1 138 ? 19.561  -23.379 -9.493  1.00 55.61  1  153 ARG   A NH1 1 
ATOM   1134 N  NH2 . ARG   A  1 138 ? 20.537  -25.064 -10.680 1.00 43.58  0  153 ARG   A NH2 1 
ATOM   1135 N  N   . LEU   A  1 139 ? 22.169  -20.323 -15.456 1.00 30.30  0  154 LEU   A N   1 
ATOM   1136 C  CA  . LEU   A  1 139 ? 22.489  -19.320 -16.494 1.00 28.65  0  154 LEU   A CA  1 
ATOM   1137 C  C   . LEU   A  1 139 ? 22.044  -17.973 -15.927 1.00 26.26  0  154 LEU   A C   1 
ATOM   1138 O  O   . LEU   A  1 139 ? 20.877  -17.835 -15.577 1.00 29.61  0  154 LEU   A O   1 
ATOM   1139 C  CB  . LEU   A  1 139 ? 21.734  -19.655 -17.783 1.00 29.37  0  154 LEU   A CB  1 
ATOM   1140 C  CG  . LEU   A  1 139 ? 22.066  -18.748 -18.967 1.00 27.43  0  154 LEU   A CG  1 
ATOM   1141 C  CD1 . LEU   A  1 139 ? 23.501  -18.940 -19.424 1.00 25.02  0  154 LEU   A CD1 1 
ATOM   1142 C  CD2 . LEU   A  1 139 ? 21.087  -18.993 -20.103 1.00 26.69  0  154 LEU   A CD2 1 
ATOM   1143 N  N   . PRO   A  1 140 ? 22.922  -16.970 -15.785 1.00 25.61  0  155 PRO   A N   1 
ATOM   1144 C  CA  . PRO   A  1 140 ? 22.489  -15.637 -15.339 1.00 28.83  0  155 PRO   A CA  1 
ATOM   1145 C  C   . PRO   A  1 140 ? 21.676  -14.847 -16.369 1.00 28.87  0  155 PRO   A C   1 
ATOM   1146 O  O   . PRO   A  1 140 ? 21.810  -15.056 -17.572 1.00 30.47  0  155 PRO   A O   1 
ATOM   1147 C  CB  . PRO   A  1 140 ? 23.802  -14.869 -15.123 1.00 30.97  0  155 PRO   A CB  1 
ATOM   1148 C  CG  . PRO   A  1 140 ? 24.912  -15.911 -15.161 1.00 30.52  0  155 PRO   A CG  1 
ATOM   1149 C  CD  . PRO   A  1 140 ? 24.376  -17.029 -16.034 1.00 29.81  0  155 PRO   A CD  1 
ATOM   1150 N  N   . PRO   A  1 141 ? 20.840  -13.876 -15.944 1.00 30.39  0  156 PRO   A N   1 
ATOM   1151 C  CA  . PRO   A  1 141 ? 20.250  -12.919 -16.872 1.00 31.38  0  156 PRO   A CA  1 
ATOM   1152 C  C   . PRO   A  1 141 ? 21.391  -12.235 -17.605 1.00 30.08  0  156 PRO   A C   1 
ATOM   1153 O  O   . PRO   A  1 141 ? 22.469  -12.065 -17.020 1.00 28.80  0  156 PRO   A O   1 
ATOM   1154 C  CB  . PRO   A  1 141 ? 19.483  -11.913 -16.003 1.00 34.69  0  156 PRO   A CB  1 
ATOM   1155 C  CG  . PRO   A  1 141 ? 19.368  -12.565 -14.635 1.00 34.45  0  156 PRO   A CG  1 
ATOM   1156 C  CD  . PRO   A  1 141 ? 20.448  -13.618 -14.547 1.00 33.71  0  156 PRO   A CD  1 
ATOM   1157 N  N   . PRO   A  1 142 ? 21.235  -11.833 -18.888 1.00 28.76  0  157 PRO   A N   1 
ATOM   1158 C  CA  . PRO   A  1 142 ? 19.984  -11.953 -19.643 1.00 26.74  0  157 PRO   A CA  1 
ATOM   1159 C  C   . PRO   A  1 142 ? 19.690  -13.271 -20.397 1.00 30.13  0  157 PRO   A C   1 
ATOM   1160 O  O   . PRO   A  1 142 ? 18.931  -13.242 -21.374 1.00 25.45  0  157 PRO   A O   1 
ATOM   1161 C  CB  . PRO   A  1 142 ? 20.187  -10.820 -20.637 1.00 27.79  0  157 PRO   A CB  1 
ATOM   1162 C  CG  . PRO   A  1 142 ? 21.641  -10.889 -20.973 1.00 27.44  0  157 PRO   A CG  1 
ATOM   1163 C  CD  . PRO   A  1 142 ? 22.316  -11.225 -19.667 1.00 27.63  0  157 PRO   A CD  1 
ATOM   1164 N  N   . PHE   A  1 143 ? 20.267  -14.394 -19.968 1.00 28.92  0  158 PHE   A N   1 
ATOM   1165 C  CA  . PHE   A  1 143 ? 19.880  -15.757 -20.434 1.00 25.92  0  158 PHE   A CA  1 
ATOM   1166 C  C   . PHE   A  1 143 ? 20.163  -15.933 -21.931 1.00 25.84  0  158 PHE   A C   1 
ATOM   1167 O  O   . PHE   A  1 143 ? 19.267  -16.229 -22.725 1.00 24.90  0  158 PHE   A O   1 
ATOM   1168 C  CB  . PHE   A  1 143 ? 18.406  -16.022 -20.122 1.00 27.11  0  158 PHE   A CB  1 
ATOM   1169 C  CG  . PHE   A  1 143 ? 17.923  -15.652 -18.733 1.00 30.44  0  158 PHE   A CG  1 
ATOM   1170 C  CD1 . PHE   A  1 143 ? 18.373  -16.326 -17.599 1.00 30.61  0  158 PHE   A CD1 1 
ATOM   1171 C  CD2 . PHE   A  1 143 ? 16.952  -14.669 -18.555 1.00 32.91  0  158 PHE   A CD2 1 
ATOM   1172 C  CE1 . PHE   A  1 143 ? 17.887  -16.009 -16.337 1.00 31.63  0  158 PHE   A CE1 1 
ATOM   1173 C  CE2 . PHE   A  1 143 ? 16.495  -14.329 -17.284 1.00 30.79  0  158 PHE   A CE2 1 
ATOM   1174 C  CZ  . PHE   A  1 143 ? 16.948  -15.013 -16.181 1.00 29.28  0  158 PHE   A CZ  1 
ATOM   1175 N  N   . PRO   A  1 144 ? 21.425  -15.768 -22.368 1.00 26.02  0  159 PRO   A N   1 
ATOM   1176 C  CA  . PRO   A  1 144 ? 21.787  -15.940 -23.771 1.00 27.88  0  159 PRO   A CA  1 
ATOM   1177 C  C   . PRO   A  1 144 ? 21.776  -17.439 -24.101 1.00 25.98  0  159 PRO   A C   1 
ATOM   1178 O  O   . PRO   A  1 144 ? 22.161  -18.255 -23.272 1.00 25.85  0  159 PRO   A O   1 
ATOM   1179 C  CB  . PRO   A  1 144 ? 23.208  -15.380 -23.847 1.00 27.71  0  159 PRO   A CB  1 
ATOM   1180 C  CG  . PRO   A  1 144 ? 23.768  -15.690 -22.448 1.00 29.69  0  159 PRO   A CG  1 
ATOM   1181 C  CD  . PRO   A  1 144 ? 22.599  -15.455 -21.523 1.00 28.03  0  159 PRO   A CD  1 
ATOM   1182 N  N   . LEU   A  1 145 ? 21.291  -17.777 -25.284 1.00 26.36  0  160 LEU   A N   1 
ATOM   1183 C  CA  . LEU   A  1 145 ? 21.465  -19.136 -25.841 1.00 25.51  0  160 LEU   A CA  1 
ATOM   1184 C  C   . LEU   A  1 145 ? 22.961  -19.455 -25.909 1.00 24.34  0  160 LEU   A C   1 
ATOM   1185 O  O   . LEU   A  1 145 ? 23.732  -18.693 -26.526 1.00 24.48  0  160 LEU   A O   1 
ATOM   1186 C  CB  . LEU   A  1 145 ? 20.790  -19.228 -27.201 1.00 26.28  0  160 LEU   A CB  1 
ATOM   1187 C  CG  . LEU   A  1 145 ? 20.975  -20.569 -27.888 1.00 26.35  0  160 LEU   A CG  1 
ATOM   1188 C  CD1 . LEU   A  1 145 ? 20.319  -21.688 -27.076 1.00 26.86  0  160 LEU   A CD1 1 
ATOM   1189 C  CD2 . LEU   A  1 145 ? 20.424  -20.472 -29.280 1.00 27.79  0  160 LEU   A CD2 1 
ATOM   1190 N  N   . LYS   A  1 146 ? 23.387  -20.550 -25.274 1.00 27.25  0  161 LYS   A N   1 
ATOM   1191 C  CA  . LYS   A  1 146 ? 24.801  -21.024 -25.322 1.00 28.91  0  161 LYS   A CA  1 
ATOM   1192 C  C   . LYS   A  1 146 ? 24.933  -22.215 -26.294 1.00 26.76  0  161 LYS   A C   1 
ATOM   1193 O  O   . LYS   A  1 146 ? 23.946  -22.905 -26.585 1.00 23.28  0  161 LYS   A O   1 
ATOM   1194 C  CB  . LYS   A  1 146 ? 25.319  -21.343 -23.909 1.00 27.52  0  161 LYS   A CB  1 
ATOM   1195 C  CG  . LYS   A  1 146 ? 25.573  -20.112 -23.033 1.00 32.16  0  161 LYS   A CG  1 
ATOM   1196 C  CD  . LYS   A  1 146 ? 26.362  -20.393 -21.722 1.00 33.48  0  161 LYS   A CD  1 
ATOM   1197 C  CE  . LYS   A  1 146 ? 27.821  -20.851 -21.870 1.00 36.15  0  161 LYS   A CE  1 
ATOM   1198 N  NZ  . LYS   A  1 146 ? 28.347  -21.733 -20.761 1.00 29.37  1  161 LYS   A NZ  1 
ATOM   1199 N  N   . GLN   A  1 147 ? 26.162  -22.419 -26.731 1.00 24.71  0  162 GLN   A N   1 
ATOM   1200 C  CA  . GLN   A  1 147 ? 26.609  -23.522 -27.608 1.00 26.54  0  162 GLN   A CA  1 
ATOM   1201 C  C   . GLN   A  1 147 ? 27.906  -24.045 -26.988 1.00 25.96  0  162 GLN   A C   1 
ATOM   1202 O  O   . GLN   A  1 147 ? 28.587  -23.253 -26.332 1.00 27.39  0  162 GLN   A O   1 
ATOM   1203 C  CB  . GLN   A  1 147 ? 26.856  -23.008 -29.025 1.00 27.63  0  162 GLN   A CB  1 
ATOM   1204 C  CG  . GLN   A  1 147 ? 27.904  -21.903 -29.101 1.00 29.16  0  162 GLN   A CG  1 
ATOM   1205 C  CD  . GLN   A  1 147 ? 28.189  -21.449 -30.510 1.00 32.88  0  162 GLN   A CD  1 
ATOM   1206 O  OE1 . GLN   A  1 147 ? 27.291  -21.258 -31.331 1.00 32.51  0  162 GLN   A OE1 1 
ATOM   1207 N  NE2 . GLN   A  1 147 ? 29.461  -21.317 -30.811 1.00 35.85  0  162 GLN   A NE2 1 
ATOM   1208 N  N   . VAL   A  1 148 ? 28.221  -25.319 -27.140 1.00 25.45  0  163 VAL   A N   1 
ATOM   1209 C  CA  . VAL   A  1 148 ? 29.584  -25.834 -26.822 1.00 25.42  0  163 VAL   A CA  1 
ATOM   1210 C  C   . VAL   A  1 148 ? 29.842  -27.016 -27.759 1.00 29.14  0  163 VAL   A C   1 
ATOM   1211 O  O   . VAL   A  1 148 ? 28.916  -27.826 -28.002 1.00 25.87  0  163 VAL   A O   1 
ATOM   1212 C  CB  . VAL   A  1 148 ? 29.727  -26.201 -25.330 1.00 26.79  0  163 VAL   A CB  1 
ATOM   1213 C  CG1 . VAL   A  1 148 ? 28.805  -27.330 -24.906 1.00 24.58  0  163 VAL   A CG1 1 
ATOM   1214 C  CG2 . VAL   A  1 148 ? 31.159  -26.525 -24.936 1.00 26.87  0  163 VAL   A CG2 1 
ATOM   1215 N  N   . LYS   A  1 149 ? 31.056  -27.068 -28.297 1.00 30.04  0  164 LYS   A N   1 
ATOM   1216 C  CA  . LYS   A  1 149 ? 31.531  -28.197 -29.127 1.00 33.87  0  164 LYS   A CA  1 
ATOM   1217 C  C   . LYS   A  1 149 ? 31.893  -29.352 -28.195 1.00 30.02  0  164 LYS   A C   1 
ATOM   1218 O  O   . LYS   A  1 149 ? 32.620  -29.103 -27.215 1.00 31.26  0  164 LYS   A O   1 
ATOM   1219 C  CB  . LYS   A  1 149 ? 32.715  -27.769 -29.990 1.00 37.70  0  164 LYS   A CB  1 
ATOM   1220 C  CG  . LYS   A  1 149 ? 33.117  -28.788 -31.054 1.00 42.23  0  164 LYS   A CG  1 
ATOM   1221 C  CD  . LYS   A  1 149 ? 34.324  -28.320 -31.835 1.00 43.01  0  164 LYS   A CD  1 
ATOM   1222 C  CE  . LYS   A  1 149 ? 34.737  -29.252 -32.941 1.00 46.26  0  164 LYS   A CE  1 
ATOM   1223 N  NZ  . LYS   A  1 149 ? 35.856  -30.111 -32.490 1.00 57.21  1  164 LYS   A NZ  1 
ATOM   1224 N  N   . VAL   A  1 150 ? 31.274  -30.517 -28.389 1.00 30.65  0  165 VAL   A N   1 
ATOM   1225 C  CA  . VAL   A  1 150 ? 31.495  -31.693 -27.490 1.00 33.22  0  165 VAL   A CA  1 
ATOM   1226 C  C   . VAL   A  1 150 ? 32.083  -32.804 -28.332 1.00 31.33  0  165 VAL   A C   1 
ATOM   1227 O  O   . VAL   A  1 150 ? 31.558  -33.091 -29.420 1.00 31.11  0  165 VAL   A O   1 
ATOM   1228 C  CB  . VAL   A  1 150 ? 30.230  -32.164 -26.742 1.00 29.41  0  165 VAL   A CB  1 
ATOM   1229 C  CG1 . VAL   A  1 150 ? 29.868  -31.174 -25.670 1.00 30.42  0  165 VAL   A CG1 1 
ATOM   1230 C  CG2 . VAL   A  1 150 ? 29.065  -32.439 -27.670 1.00 30.59  0  165 VAL   A CG2 1 
ATOM   1231 N  N   . PRO   A  1 151 ? 33.166  -33.447 -27.842 1.00 31.46  0  166 PRO   A N   1 
ATOM   1232 C  CA  . PRO   A  1 151 ? 33.716  -34.613 -28.517 1.00 36.06  0  166 PRO   A CA  1 
ATOM   1233 C  C   . PRO   A  1 151 ? 32.792  -35.826 -28.290 1.00 35.70  0  166 PRO   A C   1 
ATOM   1234 O  O   . PRO   A  1 151 ? 32.432  -36.090 -27.141 1.00 33.03  0  166 PRO   A O   1 
ATOM   1235 C  CB  . PRO   A  1 151 ? 35.101  -34.775 -27.860 1.00 35.20  0  166 PRO   A CB  1 
ATOM   1236 C  CG  . PRO   A  1 151 ? 34.906  -34.223 -26.467 1.00 37.12  0  166 PRO   A CG  1 
ATOM   1237 C  CD  . PRO   A  1 151 ? 33.905  -33.103 -26.617 1.00 35.09  0  166 PRO   A CD  1 
ATOM   1238 N  N   . ILE   A  1 152 ? 32.428  -36.512 -29.372 1.00 33.09  0  167 ILE   A N   1 
ATOM   1239 C  CA  . ILE   A  1 152 ? 31.718  -37.824 -29.317 1.00 37.90  0  167 ILE   A CA  1 
ATOM   1240 C  C   . ILE   A  1 152 ? 32.699  -38.880 -28.803 1.00 39.22  0  167 ILE   A C   1 
ATOM   1241 O  O   . ILE   A  1 152 ? 33.850  -38.879 -29.226 1.00 40.49  0  167 ILE   A O   1 
ATOM   1242 C  CB  . ILE   A  1 152 ? 31.198  -38.235 -30.697 1.00 42.12  0  167 ILE   A CB  1 
ATOM   1243 C  CG1 . ILE   A  1 152 ? 30.203  -37.219 -31.263 1.00 48.03  0  167 ILE   A CG1 1 
ATOM   1244 C  CG2 . ILE   A  1 152 ? 30.636  -39.655 -30.662 1.00 43.62  0  167 ILE   A CG2 1 
ATOM   1245 C  CD1 . ILE   A  1 152 ? 28.837  -37.318 -30.674 1.00 51.85  0  167 ILE   A CD1 1 
ATOM   1246 N  N   A MET   A  1 153 ? 32.233  -39.793 -27.951 0.50 41.11  0  168 MET   A N   1 
ATOM   1247 N  N   B MET   A  1 153 ? 32.224  -39.795 -27.960 0.50 41.64  0  168 MET   A N   1 
ATOM   1248 C  CA  A MET   A  1 153 ? 32.968  -41.037 -27.590 0.50 42.80  0  168 MET   A CA  1 
ATOM   1249 C  CA  B MET   A  1 153 ? 32.958  -41.033 -27.597 0.50 43.67  0  168 MET   A CA  1 
ATOM   1250 C  C   A MET   A  1 153 ? 32.072  -42.237 -27.917 0.50 41.42  0  168 MET   A C   1 
ATOM   1251 C  C   B MET   A  1 153 ? 32.068  -42.238 -27.917 0.50 41.93  0  168 MET   A C   1 
ATOM   1252 O  O   A MET   A  1 153 ? 30.840  -42.094 -27.796 0.50 41.84  0  168 MET   A O   1 
ATOM   1253 O  O   B MET   A  1 153 ? 30.835  -42.097 -27.797 0.50 42.38  0  168 MET   A O   1 
ATOM   1254 C  CB  A MET   A  1 153 ? 33.380  -41.044 -26.113 0.50 45.28  0  168 MET   A CB  1 
ATOM   1255 C  CB  B MET   A  1 153 ? 33.362  -41.001 -26.123 0.50 46.88  0  168 MET   A CB  1 
ATOM   1256 C  CG  A MET   A  1 153 ? 34.635  -40.214 -25.812 0.50 48.41  0  168 MET   A CG  1 
ATOM   1257 C  CG  B MET   A  1 153 ? 34.470  -39.985 -25.820 0.50 50.66  0  168 MET   A CG  1 
ATOM   1258 S  SD  A MET   A  1 153 ? 35.111  -40.316 -24.057 0.50 52.04  0  168 MET   A SD  1 
ATOM   1259 S  SD  B MET   A  1 153 ? 33.875  -38.391 -25.164 0.50 55.20  0  168 MET   A SD  1 
ATOM   1260 C  CE  A MET   A  1 153 ? 33.663  -41.140 -23.398 0.50 46.59  0  168 MET   A CE  1 
ATOM   1261 C  CE  B MET   A  1 153 ? 35.444  -37.549 -24.944 0.50 46.01  0  168 MET   A CE  1 
ATOM   1262 N  N   . GLU   A  1 154 ? 32.674  -43.351 -28.354 1.00 36.87  0  169 GLU   A N   1 
ATOM   1263 C  CA  . GLU   A  1 154 ? 31.986  -44.637 -28.612 1.00 35.13  0  169 GLU   A CA  1 
ATOM   1264 C  C   . GLU   A  1 154 ? 31.220  -45.078 -27.350 1.00 29.12  0  169 GLU   A C   1 
ATOM   1265 O  O   . GLU   A  1 154 ? 31.732  -44.883 -26.210 1.00 28.49  0  169 GLU   A O   1 
ATOM   1266 C  CB  . GLU   A  1 154 ? 33.011  -45.705 -29.015 1.00 44.26  0  169 GLU   A CB  1 
ATOM   1267 C  CG  . GLU   A  1 154 ? 33.228  -45.840 -30.509 1.00 54.86  0  169 GLU   A CG  1 
ATOM   1268 C  CD  . GLU   A  1 154 ? 34.128  -47.023 -30.842 1.00 62.22  0  169 GLU   A CD  1 
ATOM   1269 O  OE1 . GLU   A  1 154 ? 33.587  -48.145 -31.048 1.00 64.38  0  169 GLU   A OE1 1 
ATOM   1270 O  OE2 . GLU   A  1 154 ? 35.372  -46.833 -30.846 1.00 64.79  -1 169 GLU   A OE2 1 
ATOM   1271 N  N   . ASN   A  1 155 ? 30.057  -45.706 -27.537 1.00 26.25  0  170 ASN   A N   1 
ATOM   1272 C  CA  . ASN   A  1 155 ? 29.191  -46.183 -26.440 1.00 25.77  0  170 ASN   A CA  1 
ATOM   1273 C  C   . ASN   A  1 155 ? 29.999  -47.088 -25.504 1.00 30.86  0  170 ASN   A C   1 
ATOM   1274 O  O   . ASN   A  1 155 ? 29.790  -46.974 -24.293 1.00 30.82  0  170 ASN   A O   1 
ATOM   1275 C  CB  . ASN   A  1 155 ? 27.955  -46.904 -26.956 1.00 27.28  0  170 ASN   A CB  1 
ATOM   1276 C  CG  . ASN   A  1 155 ? 26.822  -45.976 -27.341 1.00 29.98  0  170 ASN   A CG  1 
ATOM   1277 O  OD1 . ASN   A  1 155 ? 27.071  -44.871 -27.790 1.00 28.81  0  170 ASN   A OD1 1 
ATOM   1278 N  ND2 . ASN   A  1 155 ? 25.589  -46.412 -27.121 1.00 28.67  0  170 ASN   A ND2 1 
ATOM   1279 N  N   . HIS   A  1 156 ? 30.848  -47.989 -26.021 1.00 29.71  0  171 HIS   A N   1 
ATOM   1280 C  CA  . HIS   A  1 156 ? 31.522  -49.005 -25.167 1.00 32.86  0  171 HIS   A CA  1 
ATOM   1281 C  C   . HIS   A  1 156 ? 32.507  -48.293 -24.221 1.00 31.11  0  171 HIS   A C   1 
ATOM   1282 O  O   . HIS   A  1 156 ? 32.720  -48.749 -23.065 1.00 31.30  0  171 HIS   A O   1 
ATOM   1283 C  CB  . HIS   A  1 156 ? 32.113  -50.169 -25.997 1.00 34.56  0  171 HIS   A CB  1 
ATOM   1284 C  CG  . HIS   A  1 156 ? 33.440  -49.897 -26.616 1.00 39.89  0  171 HIS   A CG  1 
ATOM   1285 N  ND1 . HIS   A  1 156 ? 33.562  -49.473 -27.949 1.00 47.44  0  171 HIS   A ND1 1 
ATOM   1286 C  CD2 . HIS   A  1 156 ? 34.707  -50.017 -26.131 1.00 43.42  0  171 HIS   A CD2 1 
ATOM   1287 C  CE1 . HIS   A  1 156 ? 34.855  -49.319 -28.247 1.00 43.85  0  171 HIS   A CE1 1 
ATOM   1288 N  NE2 . HIS   A  1 156 ? 35.586  -49.641 -27.147 1.00 42.36  0  171 HIS   A NE2 1 
ATOM   1289 N  N   . ILE   A  1 157 ? 33.178  -47.271 -24.715 1.00 29.51  0  172 ILE   A N   1 
ATOM   1290 C  CA  . ILE   A  1 157 ? 34.158  -46.466 -23.938 1.00 32.22  0  172 ILE   A CA  1 
ATOM   1291 C  C   . ILE   A  1 157 ? 33.423  -45.735 -22.821 1.00 32.51  0  172 ILE   A C   1 
ATOM   1292 O  O   . ILE   A  1 157 ? 33.908  -45.730 -21.678 1.00 32.31  0  172 ILE   A O   1 
ATOM   1293 C  CB  . ILE   A  1 157 ? 34.873  -45.474 -24.866 1.00 33.47  0  172 ILE   A CB  1 
ATOM   1294 C  CG1 . ILE   A  1 157 ? 35.725  -46.174 -25.930 1.00 38.94  0  172 ILE   A CG1 1 
ATOM   1295 C  CG2 . ILE   A  1 157 ? 35.664  -44.476 -24.050 1.00 36.05  0  172 ILE   A CG2 1 
ATOM   1296 C  CD1 . ILE   A  1 157 ? 36.703  -47.178 -25.371 1.00 39.51  0  172 ILE   A CD1 1 
ATOM   1297 N  N   A CYS   A  1 158 ? 32.307  -45.100 -23.168 0.50 29.60  0  173 CYS   A N   1 
ATOM   1298 N  N   B CYS   A  1 158 ? 32.297  -45.092 -23.151 0.50 30.57  0  173 CYS   A N   1 
ATOM   1299 C  CA  A CYS   A  1 158 ? 31.459  -44.327 -22.251 0.50 30.48  0  173 CYS   A CA  1 
ATOM   1300 C  CA  B CYS   A  1 158 ? 31.516  -44.308 -22.170 0.50 32.16  0  173 CYS   A CA  1 
ATOM   1301 C  C   A CYS   A  1 158 ? 30.890  -45.262 -21.175 0.50 29.29  0  173 CYS   A C   1 
ATOM   1302 C  C   B CYS   A  1 158 ? 30.889  -45.262 -21.151 0.50 30.25  0  173 CYS   A C   1 
ATOM   1303 O  O   A CYS   A  1 158 ? 30.921  -44.880 -19.989 0.50 26.72  0  173 CYS   A O   1 
ATOM   1304 O  O   B CYS   A  1 158 ? 30.887  -44.886 -19.966 0.50 27.67  0  173 CYS   A O   1 
ATOM   1305 C  CB  A CYS   A  1 158 ? 30.375  -43.667 -23.087 0.50 31.22  0  173 CYS   A CB  1 
ATOM   1306 C  CB  B CYS   A  1 158 ? 30.479  -43.430 -22.851 0.50 34.02  0  173 CYS   A CB  1 
ATOM   1307 S  SG  A CYS   A  1 158 ? 29.227  -42.665 -22.134 0.50 31.21  0  173 CYS   A SG  1 
ATOM   1308 S  SG  B CYS   A  1 158 ? 31.255  -42.071 -23.769 0.50 36.40  0  173 CYS   A SG  1 
ATOM   1309 N  N   . ASP   A  1 159 ? 30.408  -46.441 -21.587 1.00 28.37  0  174 ASP   A N   1 
ATOM   1310 C  CA  . ASP   A  1 159 ? 29.886  -47.506 -20.687 1.00 29.33  0  174 ASP   A CA  1 
ATOM   1311 C  C   . ASP   A  1 159 ? 30.970  -47.880 -19.683 1.00 27.04  0  174 ASP   A C   1 
ATOM   1312 O  O   . ASP   A  1 159 ? 30.673  -47.858 -18.455 1.00 22.63  0  174 ASP   A O   1 
ATOM   1313 C  CB  . ASP   A  1 159 ? 29.426  -48.769 -21.413 1.00 29.85  0  174 ASP   A CB  1 
ATOM   1314 C  CG  . ASP   A  1 159 ? 28.622  -49.729 -20.534 1.00 33.46  0  174 ASP   A CG  1 
ATOM   1315 O  OD1 . ASP   A  1 159 ? 27.645  -49.275 -19.878 1.00 30.30  0  174 ASP   A OD1 1 
ATOM   1316 O  OD2 . ASP   A  1 159 ? 28.922  -50.954 -20.551 1.00 28.88  -1 174 ASP   A OD2 1 
ATOM   1317 N  N   . ALA   A  1 160 ? 32.199  -48.105 -20.159 1.00 28.25  0  175 ALA   A N   1 
ATOM   1318 C  CA  . ALA   A  1 160 ? 33.324  -48.449 -19.262 1.00 28.73  0  175 ALA   A CA  1 
ATOM   1319 C  C   . ALA   A  1 160 ? 33.559  -47.280 -18.293 1.00 29.42  0  175 ALA   A C   1 
ATOM   1320 O  O   . ALA   A  1 160 ? 33.730  -47.555 -17.087 1.00 29.77  0  175 ALA   A O   1 
ATOM   1321 C  CB  . ALA   A  1 160 ? 34.578  -48.820 -20.042 1.00 30.50  0  175 ALA   A CB  1 
ATOM   1322 N  N   . LYS   A  1 161 ? 33.529  -46.020 -18.749 1.00 28.74  0  176 LYS   A N   1 
ATOM   1323 C  CA  . LYS   A  1 161 ? 33.759  -44.894 -17.811 1.00 30.44  0  176 LYS   A CA  1 
ATOM   1324 C  C   . LYS   A  1 161 ? 32.688  -44.864 -16.704 1.00 28.14  0  176 LYS   A C   1 
ATOM   1325 O  O   . LYS   A  1 161 ? 33.035  -44.699 -15.516 1.00 25.86  0  176 LYS   A O   1 
ATOM   1326 C  CB  . LYS   A  1 161 ? 33.843  -43.566 -18.539 1.00 34.73  0  176 LYS   A CB  1 
ATOM   1327 C  CG  . LYS   A  1 161 ? 35.130  -43.355 -19.327 1.00 37.57  0  176 LYS   A CG  1 
ATOM   1328 C  CD  . LYS   A  1 161 ? 35.045  -42.031 -20.084 1.00 45.02  0  176 LYS   A CD  1 
ATOM   1329 C  CE  . LYS   A  1 161 ? 36.381  -41.403 -20.409 1.00 52.69  0  176 LYS   A CE  1 
ATOM   1330 N  NZ  . LYS   A  1 161 ? 37.290  -42.397 -21.026 1.00 59.56  1  176 LYS   A NZ  1 
ATOM   1331 N  N   . TYR   A  1 162 ? 31.432  -45.082 -17.052 1.00 26.98  0  177 TYR   A N   1 
ATOM   1332 C  CA  . TYR   A  1 162 ? 30.323  -44.997 -16.090 1.00 27.40  0  177 TYR   A CA  1 
ATOM   1333 C  C   . TYR   A  1 162 ? 30.516  -46.068 -14.998 1.00 28.58  0  177 TYR   A C   1 
ATOM   1334 O  O   . TYR   A  1 162 ? 29.977  -45.835 -13.899 1.00 28.31  0  177 TYR   A O   1 
ATOM   1335 C  CB  . TYR   A  1 162 ? 28.973  -45.016 -16.810 1.00 28.03  0  177 TYR   A CB  1 
ATOM   1336 C  CG  . TYR   A  1 162 ? 28.420  -43.622 -16.988 1.00 27.76  0  177 TYR   A CG  1 
ATOM   1337 C  CD1 . TYR   A  1 162 ? 28.879  -42.787 -18.001 1.00 27.15  0  177 TYR   A CD1 1 
ATOM   1338 C  CD2 . TYR   A  1 162 ? 27.472  -43.108 -16.117 1.00 29.73  0  177 TYR   A CD2 1 
ATOM   1339 C  CE1 . TYR   A  1 162 ? 28.412  -41.498 -18.160 1.00 25.97  0  177 TYR   A CE1 1 
ATOM   1340 C  CE2 . TYR   A  1 162 ? 27.025  -41.796 -16.241 1.00 31.13  0  177 TYR   A CE2 1 
ATOM   1341 C  CZ  . TYR   A  1 162 ? 27.474  -40.999 -17.279 1.00 29.64  0  177 TYR   A CZ  1 
ATOM   1342 O  OH  . TYR   A  1 162 ? 27.009  -39.716 -17.413 1.00 30.96  0  177 TYR   A OH  1 
ATOM   1343 N  N   . HIS   A  1 163 ? 31.268  -47.147 -15.277 1.00 29.44  0  178 HIS   A N   1 
ATOM   1344 C  CA  . HIS   A  1 163 ? 31.544  -48.259 -14.330 1.00 27.56  0  178 HIS   A CA  1 
ATOM   1345 C  C   . HIS   A  1 163 ? 32.698  -47.933 -13.375 1.00 25.94  0  178 HIS   A C   1 
ATOM   1346 O  O   . HIS   A  1 163 ? 32.764  -48.588 -12.334 1.00 26.35  0  178 HIS   A O   1 
ATOM   1347 C  CB  . HIS   A  1 163 ? 31.777  -49.570 -15.102 1.00 25.79  0  178 HIS   A CB  1 
ATOM   1348 C  CG  . HIS   A  1 163 ? 30.521  -50.206 -15.579 1.00 25.12  0  178 HIS   A CG  1 
ATOM   1349 N  ND1 . HIS   A  1 163 ? 29.983  -49.920 -16.810 1.00 25.97  0  178 HIS   A ND1 1 
ATOM   1350 C  CD2 . HIS   A  1 163 ? 29.707  -51.130 -15.025 1.00 29.52  0  178 HIS   A CD2 1 
ATOM   1351 C  CE1 . HIS   A  1 163 ? 28.878  -50.624 -16.987 1.00 28.05  0  178 HIS   A CE1 1 
ATOM   1352 N  NE2 . HIS   A  1 163 ? 28.665  -51.346 -15.905 1.00 28.49  0  178 HIS   A NE2 1 
ATOM   1353 N  N   . LEU   A  1 164 ? 33.593  -47.018 -13.727 1.00 26.82  0  179 LEU   A N   1 
ATOM   1354 C  CA  . LEU   A  1 164 ? 34.709  -46.610 -12.838 1.00 28.51  0  179 LEU   A CA  1 
ATOM   1355 C  C   . LEU   A  1 164 ? 34.131  -45.865 -11.619 1.00 31.17  0  179 LEU   A C   1 
ATOM   1356 O  O   . LEU   A  1 164 ? 33.285  -44.976 -11.823 1.00 25.70  0  179 LEU   A O   1 
ATOM   1357 C  CB  . LEU   A  1 164 ? 35.680  -45.729 -13.624 1.00 31.14  0  179 LEU   A CB  1 
ATOM   1358 C  CG  . LEU   A  1 164 ? 36.458  -46.421 -14.752 1.00 34.72  0  179 LEU   A CG  1 
ATOM   1359 C  CD1 . LEU   A  1 164 ? 37.245  -45.413 -15.582 1.00 37.75  0  179 LEU   A CD1 1 
ATOM   1360 C  CD2 . LEU   A  1 164 ? 37.382  -47.512 -14.211 1.00 33.34  0  179 LEU   A CD2 1 
ATOM   1361 N  N   . GLY   A  1 165 ? 34.547  -46.221 -10.395 1.00 30.31  0  180 GLY   A N   1 
ATOM   1362 C  CA  . GLY   A  1 165 ? 34.023  -45.625 -9.149  1.00 30.51  0  180 GLY   A CA  1 
ATOM   1363 C  C   . GLY   A  1 165 ? 32.599  -46.046 -8.888  1.00 29.44  0  180 GLY   A C   1 
ATOM   1364 O  O   . GLY   A  1 165 ? 31.907  -45.334 -8.114  1.00 30.34  0  180 GLY   A O   1 
ATOM   1365 N  N   . ALA   A  1 166 ? 32.167  -47.185 -9.446  1.00 26.38  0  181 ALA   A N   1 
ATOM   1366 C  CA  . ALA   A  1 166 ? 30.797  -47.700 -9.236  1.00 29.68  0  181 ALA   A CA  1 
ATOM   1367 C  C   . ALA   A  1 166 ? 30.833  -49.148 -8.773  1.00 29.16  0  181 ALA   A C   1 
ATOM   1368 O  O   . ALA   A  1 166 ? 31.754  -49.868 -9.143  1.00 30.87  0  181 ALA   A O   1 
ATOM   1369 C  CB  . ALA   A  1 166 ? 29.943  -47.566 -10.472 1.00 30.14  0  181 ALA   A CB  1 
ATOM   1370 N  N   . TYR   A  1 167 ? 29.798  -49.554 -8.038  1.00 29.07  0  182 TYR   A N   1 
ATOM   1371 C  CA  . TYR   A  1 167 ? 29.585  -50.956 -7.604  1.00 31.36  0  182 TYR   A CA  1 
ATOM   1372 C  C   . TYR   A  1 167 ? 29.010  -51.788 -8.766  1.00 28.86  0  182 TYR   A C   1 
ATOM   1373 O  O   . TYR   A  1 167 ? 28.957  -53.031 -8.675  1.00 24.87  0  182 TYR   A O   1 
ATOM   1374 C  CB  . TYR   A  1 167 ? 28.680  -50.979 -6.360  1.00 31.81  0  182 TYR   A CB  1 
ATOM   1375 C  CG  . TYR   A  1 167 ? 29.221  -50.316 -5.107  1.00 34.05  0  182 TYR   A CG  1 
ATOM   1376 C  CD1 . TYR   A  1 167 ? 30.303  -50.837 -4.419  1.00 34.87  0  182 TYR   A CD1 1 
ATOM   1377 C  CD2 . TYR   A  1 167 ? 28.608  -49.184 -4.574  1.00 35.66  0  182 TYR   A CD2 1 
ATOM   1378 C  CE1 . TYR   A  1 167 ? 30.765  -50.263 -3.241  1.00 35.83  0  182 TYR   A CE1 1 
ATOM   1379 C  CE2 . TYR   A  1 167 ? 29.051  -48.600 -3.395  1.00 35.14  0  182 TYR   A CE2 1 
ATOM   1380 C  CZ  . TYR   A  1 167 ? 30.139  -49.135 -2.726  1.00 37.18  0  182 TYR   A CZ  1 
ATOM   1381 O  OH  . TYR   A  1 167 ? 30.586  -48.528 -1.580  1.00 34.71  0  182 TYR   A OH  1 
ATOM   1382 N  N   . THR   A  1 168 ? 28.425  -51.140 -9.773  1.00 24.97  0  183 THR   A N   1 
ATOM   1383 C  CA  . THR   A  1 168 ? 27.670  -51.847 -10.835 1.00 27.47  0  183 THR   A CA  1 
ATOM   1384 C  C   . THR   A  1 168 ? 28.638  -52.798 -11.533 1.00 27.00  0  183 THR   A C   1 
ATOM   1385 O  O   . THR   A  1 168 ? 29.742  -52.344 -11.861 1.00 27.63  0  183 THR   A O   1 
ATOM   1386 C  CB  . THR   A  1 168 ? 27.013  -50.862 -11.810 1.00 27.23  0  183 THR   A CB  1 
ATOM   1387 O  OG1 . THR   A  1 168 ? 26.219  -49.958 -11.039 1.00 25.99  0  183 THR   A OG1 1 
ATOM   1388 C  CG2 . THR   A  1 168 ? 26.140  -51.560 -12.822 1.00 26.35  0  183 THR   A CG2 1 
ATOM   1389 N  N   . GLY   A  1 169 ? 28.235  -54.055 -11.737 1.00 29.95  0  184 GLY   A N   1 
ATOM   1390 C  CA  . GLY   A  1 169 ? 29.070  -55.049 -12.433 1.00 31.00  0  184 GLY   A CA  1 
ATOM   1391 C  C   . GLY   A  1 169 ? 29.402  -54.601 -13.852 1.00 30.18  0  184 GLY   A C   1 
ATOM   1392 O  O   . GLY   A  1 169 ? 28.522  -54.018 -14.542 1.00 30.48  0  184 GLY   A O   1 
ATOM   1393 N  N   . ASP   A  1 170 ? 30.627  -54.882 -14.280 1.00 31.06  0  185 ASP   A N   1 
ATOM   1394 C  CA  . ASP   A  1 170 ? 31.196  -54.476 -15.588 1.00 32.87  0  185 ASP   A CA  1 
ATOM   1395 C  C   . ASP   A  1 170 ? 30.378  -54.990 -16.782 1.00 32.45  0  185 ASP   A C   1 
ATOM   1396 O  O   . ASP   A  1 170 ? 30.411  -54.297 -17.837 1.00 31.43  0  185 ASP   A O   1 
ATOM   1397 C  CB  . ASP   A  1 170 ? 32.660  -54.902 -15.692 1.00 35.38  0  185 ASP   A CB  1 
ATOM   1398 C  CG  . ASP   A  1 170 ? 33.614  -54.052 -14.864 1.00 41.03  0  185 ASP   A CG  1 
ATOM   1399 O  OD1 . ASP   A  1 170 ? 33.265  -52.911 -14.464 1.00 46.24  0  185 ASP   A OD1 1 
ATOM   1400 O  OD2 . ASP   A  1 170 ? 34.726  -54.518 -14.650 1.00 51.31  -1 185 ASP   A OD2 1 
ATOM   1401 N  N   A ASP   A  1 171 ? 29.687  -56.121 -16.601 0.50 29.63  0  186 ASP   A N   1 
ATOM   1402 N  N   B ASP   A  1 171 ? 29.673  -56.114 -16.646 0.50 29.14  0  186 ASP   A N   1 
ATOM   1403 C  CA  A ASP   A  1 171 ? 28.842  -56.846 -17.581 0.50 31.05  0  186 ASP   A CA  1 
ATOM   1404 C  CA  B ASP   A  1 171 ? 28.846  -56.708 -17.738 0.50 30.02  0  186 ASP   A CA  1 
ATOM   1405 C  C   A ASP   A  1 171 ? 27.417  -56.274 -17.600 0.50 29.41  0  186 ASP   A C   1 
ATOM   1406 C  C   B ASP   A  1 171 ? 27.377  -56.325 -17.551 0.50 28.60  0  186 ASP   A C   1 
ATOM   1407 O  O   A ASP   A  1 171 ? 26.634  -56.711 -18.447 0.50 28.32  0  186 ASP   A O   1 
ATOM   1408 O  O   B ASP   A  1 171 ? 26.525  -56.984 -18.169 0.50 26.03  0  186 ASP   A O   1 
ATOM   1409 C  CB  A ASP   A  1 171 ? 28.787  -58.334 -17.183 0.50 32.89  0  186 ASP   A CB  1 
ATOM   1410 C  CB  B ASP   A  1 171 ? 28.945  -58.235 -17.774 0.50 32.00  0  186 ASP   A CB  1 
ATOM   1411 C  CG  A ASP   A  1 171 ? 28.281  -58.585 -15.757 0.50 34.94  0  186 ASP   A CG  1 
ATOM   1412 C  CG  B ASP   A  1 171 ? 30.288  -58.759 -18.242 0.50 35.04  0  186 ASP   A CG  1 
ATOM   1413 O  OD1 A ASP   A  1 171 ? 28.929  -58.104 -14.776 0.50 32.96  0  186 ASP   A OD1 1 
ATOM   1414 O  OD1 B ASP   A  1 171 ? 31.212  -57.952 -18.354 0.50 37.99  0  186 ASP   A OD1 1 
ATOM   1415 O  OD2 A ASP   A  1 171 ? 27.226  -59.235 -15.622 0.50 37.77  -1 186 ASP   A OD2 1 
ATOM   1416 O  OD2 B ASP   A  1 171 ? 30.389  -59.974 -18.500 0.50 39.15  -1 186 ASP   A OD2 1 
ATOM   1417 N  N   . VAL   A  1 172 ? 27.070  -55.367 -16.679 1.00 27.14  0  187 VAL   A N   1 
ATOM   1418 C  CA  . VAL   A  1 172 ? 25.706  -54.787 -16.573 1.00 25.95  0  187 VAL   A CA  1 
ATOM   1419 C  C   . VAL   A  1 172 ? 25.755  -53.431 -17.278 1.00 27.21  0  187 VAL   A C   1 
ATOM   1420 O  O   . VAL   A  1 172 ? 26.403  -52.509 -16.750 1.00 33.13  0  187 VAL   A O   1 
ATOM   1421 C  CB  . VAL   A  1 172 ? 25.220  -54.715 -15.125 1.00 27.56  0  187 VAL   A CB  1 
ATOM   1422 C  CG1 . VAL   A  1 172 ? 23.835  -54.086 -15.042 1.00 28.40  0  187 VAL   A CG1 1 
ATOM   1423 C  CG2 . VAL   A  1 172 ? 25.204  -56.117 -14.511 1.00 31.95  0  187 VAL   A CG2 1 
ATOM   1424 N  N   . ARG   A  1 173 ? 25.122  -53.332 -18.449 1.00 27.29  0  188 ARG   A N   1 
ATOM   1425 C  CA  . ARG   A  1 173 ? 25.318  -52.184 -19.363 1.00 26.00  0  188 ARG   A CA  1 
ATOM   1426 C  C   . ARG   A  1 173 ? 24.591  -50.970 -18.764 1.00 25.80  0  188 ARG   A C   1 
ATOM   1427 O  O   . ARG   A  1 173 ? 23.432  -51.107 -18.342 1.00 25.85  0  188 ARG   A O   1 
ATOM   1428 C  CB  . ARG   A  1 173 ? 24.857  -52.500 -20.784 1.00 27.44  0  188 ARG   A CB  1 
ATOM   1429 C  CG  . ARG   A  1 173 ? 25.463  -51.543 -21.812 1.00 30.19  0  188 ARG   A CG  1 
ATOM   1430 C  CD  . ARG   A  1 173 ? 25.291  -51.944 -23.248 1.00 31.94  0  188 ARG   A CD  1 
ATOM   1431 N  NE  . ARG   A  1 173 ? 26.169  -53.084 -23.521 1.00 32.43  0  188 ARG   A NE  1 
ATOM   1432 C  CZ  . ARG   A  1 173 ? 26.632  -53.414 -24.724 1.00 33.14  0  188 ARG   A CZ  1 
ATOM   1433 N  NH1 . ARG   A  1 173 ? 26.230  -52.764 -25.815 1.00 31.67  1  188 ARG   A NH1 1 
ATOM   1434 N  NH2 . ARG   A  1 173 ? 27.466  -54.435 -24.823 1.00 31.69  0  188 ARG   A NH2 1 
ATOM   1435 N  N   . ILE   A  1 174 ? 25.284  -49.850 -18.685 1.00 26.05  0  189 ILE   A N   1 
ATOM   1436 C  CA  . ILE   A  1 174 ? 24.731  -48.576 -18.166 1.00 26.62  0  189 ILE   A CA  1 
ATOM   1437 C  C   . ILE   A  1 174 ? 24.345  -47.698 -19.367 1.00 27.02  0  189 ILE   A C   1 
ATOM   1438 O  O   . ILE   A  1 174 ? 23.185  -47.233 -19.419 1.00 27.76  0  189 ILE   A O   1 
ATOM   1439 C  CB  . ILE   A  1 174 ? 25.731  -47.897 -17.219 1.00 27.59  0  189 ILE   A CB  1 
ATOM   1440 C  CG1 . ILE   A  1 174 ? 25.917  -48.700 -15.924 1.00 31.43  0  189 ILE   A CG1 1 
ATOM   1441 C  CG2 . ILE   A  1 174 ? 25.240  -46.478 -16.927 1.00 27.66  0  189 ILE   A CG2 1 
ATOM   1442 C  CD1 . ILE   A  1 174 ? 27.062  -48.247 -15.037 1.00 27.91  0  189 ILE   A CD1 1 
ATOM   1443 N  N   . VAL   A  1 175 ? 25.292  -47.480 -20.272 1.00 24.54  0  190 VAL   A N   1 
ATOM   1444 C  CA  . VAL   A  1 175 ? 25.085  -46.705 -21.524 1.00 25.93  0  190 VAL   A CA  1 
ATOM   1445 C  C   . VAL   A  1 175 ? 24.503  -47.650 -22.578 1.00 26.28  0  190 VAL   A C   1 
ATOM   1446 O  O   . VAL   A  1 175 ? 25.238  -48.496 -23.091 1.00 25.68  0  190 VAL   A O   1 
ATOM   1447 C  CB  . VAL   A  1 175 ? 26.379  -46.018 -21.990 1.00 25.17  0  190 VAL   A CB  1 
ATOM   1448 C  CG1 . VAL   A  1 175 ? 26.155  -45.254 -23.310 1.00 27.67  0  190 VAL   A CG1 1 
ATOM   1449 C  CG2 . VAL   A  1 175 ? 26.896  -45.103 -20.898 1.00 24.06  0  190 VAL   A CG2 1 
ATOM   1450 N  N   . ARG   A  1 176 ? 23.226  -47.469 -22.901 1.00 23.66  0  191 ARG   A N   1 
ATOM   1451 C  CA  . ARG   A  1 176 ? 22.453  -48.443 -23.699 1.00 27.99  0  191 ARG   A CA  1 
ATOM   1452 C  C   . ARG   A  1 176 ? 22.576  -48.085 -25.184 1.00 28.61  0  191 ARG   A C   1 
ATOM   1453 O  O   . ARG   A  1 176 ? 23.145  -47.006 -25.514 1.00 27.80  0  191 ARG   A O   1 
ATOM   1454 C  CB  . ARG   A  1 176 ? 21.048  -48.510 -23.101 1.00 29.38  0  191 ARG   A CB  1 
ATOM   1455 C  CG  . ARG   A  1 176 ? 21.087  -48.952 -21.643 1.00 33.30  0  191 ARG   A CG  1 
ATOM   1456 C  CD  . ARG   A  1 176 ? 19.799  -49.549 -21.196 1.00 38.92  0  191 ARG   A CD  1 
ATOM   1457 N  NE  . ARG   A  1 176 ? 19.777  -49.951 -19.795 1.00 38.69  0  191 ARG   A NE  1 
ATOM   1458 C  CZ  . ARG   A  1 176 ? 18.820  -50.687 -19.265 1.00 41.59  0  191 ARG   A CZ  1 
ATOM   1459 N  NH1 . ARG   A  1 176 ? 17.850  -51.176 -20.026 1.00 49.34  1  191 ARG   A NH1 1 
ATOM   1460 N  NH2 . ARG   A  1 176 ? 18.857  -50.994 -17.981 1.00 43.15  0  191 ARG   A NH2 1 
ATOM   1461 N  N   . ASP   A  1 177 ? 22.128  -48.995 -26.051 1.00 27.43  0  192 ASP   A N   1 
ATOM   1462 C  CA  . ASP   A  1 177 ? 22.417  -48.943 -27.510 1.00 27.86  0  192 ASP   A CA  1 
ATOM   1463 C  C   . ASP   A  1 177 ? 21.558  -47.850 -28.179 1.00 28.44  0  192 ASP   A C   1 
ATOM   1464 O  O   . ASP   A  1 177 ? 21.977  -47.329 -29.228 1.00 27.19  0  192 ASP   A O   1 
ATOM   1465 C  CB  . ASP   A  1 177 ? 22.225  -50.310 -28.174 1.00 28.94  0  192 ASP   A CB  1 
ATOM   1466 C  CG  . ASP   A  1 177 ? 23.023  -51.450 -27.535 1.00 30.63  0  192 ASP   A CG  1 
ATOM   1467 O  OD1 . ASP   A  1 177 ? 24.005  -51.167 -26.777 1.00 30.79  0  192 ASP   A OD1 1 
ATOM   1468 O  OD2 . ASP   A  1 177 ? 22.654  -52.612 -27.782 1.00 30.19  -1 192 ASP   A OD2 1 
ATOM   1469 N  N   . ASP   A  1 178 ? 20.448  -47.453 -27.566 1.00 25.84  0  193 ASP   A N   1 
ATOM   1470 C  CA  . ASP   A  1 178 ? 19.609  -46.322 -28.040 1.00 27.04  0  193 ASP   A CA  1 
ATOM   1471 C  C   . ASP   A  1 178 ? 20.143  -44.983 -27.501 1.00 26.75  0  193 ASP   A C   1 
ATOM   1472 O  O   . ASP   A  1 178 ? 19.384  -44.011 -27.542 1.00 28.99  0  193 ASP   A O   1 
ATOM   1473 C  CB  . ASP   A  1 178 ? 18.153  -46.580 -27.655 1.00 27.30  0  193 ASP   A CB  1 
ATOM   1474 C  CG  . ASP   A  1 178 ? 17.874  -46.443 -26.167 1.00 27.90  0  193 ASP   A CG  1 
ATOM   1475 O  OD1 . ASP   A  1 178 ? 18.797  -46.703 -25.372 1.00 26.78  0  193 ASP   A OD1 1 
ATOM   1476 O  OD2 . ASP   A  1 178 ? 16.763  -46.049 -25.823 1.00 28.24  -1 193 ASP   A OD2 1 
ATOM   1477 N  N   . MET   A  1 179 ? 21.356  -44.939 -26.955 1.00 25.49  0  194 MET   A N   1 
ATOM   1478 C  CA  . MET   A  1 179 ? 21.962  -43.728 -26.363 1.00 24.78  0  194 MET   A CA  1 
ATOM   1479 C  C   . MET   A  1 179 ? 23.265  -43.445 -27.072 1.00 26.72  0  194 MET   A C   1 
ATOM   1480 O  O   . MET   A  1 179 ? 23.750  -44.307 -27.839 1.00 26.53  0  194 MET   A O   1 
ATOM   1481 C  CB  . MET   A  1 179 ? 22.204  -43.853 -24.857 1.00 24.72  0  194 MET   A CB  1 
ATOM   1482 C  CG  . MET   A  1 179 ? 20.960  -44.212 -24.078 1.00 24.39  0  194 MET   A CG  1 
ATOM   1483 S  SD  . MET   A  1 179 ? 21.292  -44.596 -22.354 1.00 25.60  0  194 MET   A SD  1 
ATOM   1484 C  CE  . MET   A  1 179 ? 19.667  -45.109 -21.829 1.00 24.08  0  194 MET   A CE  1 
ATOM   1485 N  N   . LEU   A  1 180 ? 23.732  -42.223 -26.898 1.00 26.08  0  195 LEU   A N   1 
ATOM   1486 C  CA  . LEU   A  1 180 ? 24.925  -41.652 -27.553 1.00 26.47  0  195 LEU   A CA  1 
ATOM   1487 C  C   . LEU   A  1 180 ? 25.600  -40.811 -26.479 1.00 28.40  0  195 LEU   A C   1 
ATOM   1488 O  O   . LEU   A  1 180 ? 24.904  -40.175 -25.681 1.00 29.84  0  195 LEU   A O   1 
ATOM   1489 C  CB  . LEU   A  1 180 ? 24.478  -40.804 -28.750 1.00 25.95  0  195 LEU   A CB  1 
ATOM   1490 C  CG  . LEU   A  1 180 ? 25.592  -40.125 -29.533 1.00 27.80  0  195 LEU   A CG  1 
ATOM   1491 C  CD1 . LEU   A  1 180 ? 25.180  -39.978 -30.966 1.00 28.28  0  195 LEU   A CD1 1 
ATOM   1492 C  CD2 . LEU   A  1 180 ? 25.966  -38.758 -28.962 1.00 31.09  0  195 LEU   A CD2 1 
ATOM   1493 N  N   A CYS   A  1 181 ? 26.930  -40.809 -26.472 0.50 28.10  0  196 CYS   A N   1 
ATOM   1494 N  N   B CYS   A  1 181 ? 26.922  -40.788 -26.498 0.50 29.83  0  196 CYS   A N   1 
ATOM   1495 C  CA  A CYS   A  1 181 ? 27.764  -40.149 -25.437 0.50 28.10  0  196 CYS   A CA  1 
ATOM   1496 C  CA  B CYS   A  1 181 ? 27.760  -40.155 -25.469 0.50 30.85  0  196 CYS   A CA  1 
ATOM   1497 C  C   A CYS   A  1 181 ? 28.611  -39.037 -26.063 0.50 27.12  0  196 CYS   A C   1 
ATOM   1498 C  C   B CYS   A  1 181 ? 28.613  -39.036 -26.070 0.50 28.57  0  196 CYS   A C   1 
ATOM   1499 O  O   A CYS   A  1 181 ? 29.267  -39.295 -27.092 0.50 25.29  0  196 CYS   A O   1 
ATOM   1500 O  O   B CYS   A  1 181 ? 29.279  -39.290 -27.095 0.50 26.43  0  196 CYS   A O   1 
ATOM   1501 C  CB  A CYS   A  1 181 ? 28.682  -41.160 -24.757 0.50 29.63  0  196 CYS   A CB  1 
ATOM   1502 C  CB  B CYS   A  1 181 ? 28.646  -41.251 -24.915 0.50 34.69  0  196 CYS   A CB  1 
ATOM   1503 S  SG  A CYS   A  1 181 ? 27.814  -42.230 -23.582 0.50 32.34  0  196 CYS   A SG  1 
ATOM   1504 S  SG  B CYS   A  1 181 ? 29.800  -40.638 -23.684 0.50 42.05  0  196 CYS   A SG  1 
ATOM   1505 N  N   . ALA   A  1 182 ? 28.665  -37.883 -25.402 1.00 28.28  0  197 ALA   A N   1 
ATOM   1506 C  CA  . ALA   A  1 182 ? 29.572  -36.772 -25.763 1.00 28.20  0  197 ALA   A CA  1 
ATOM   1507 C  C   . ALA   A  1 182 ? 29.884  -35.914 -24.549 1.00 28.41  0  197 ALA   A C   1 
ATOM   1508 O  O   . ALA   A  1 182 ? 29.058  -35.841 -23.633 1.00 26.95  0  197 ALA   A O   1 
ATOM   1509 C  CB  . ALA   A  1 182 ? 29.001  -35.945 -26.893 1.00 30.33  0  197 ALA   A CB  1 
ATOM   1510 N  N   . GLY   A  1 183 ? 31.058  -35.286 -24.575 1.00 25.89  0  198 GLY   A N   1 
ATOM   1511 C  CA  . GLY   A  1 183 ? 31.455  -34.264 -23.601 1.00 26.34  0  198 GLY   A CA  1 
ATOM   1512 C  C   . GLY   A  1 183 ? 32.623  -34.731 -22.785 1.00 28.74  0  198 GLY   A C   1 
ATOM   1513 O  O   . GLY   A  1 183 ? 33.008  -35.917 -22.909 1.00 28.09  0  198 GLY   A O   1 
ATOM   1514 N  N   . ASN   A  1 184 ? 33.202  -33.810 -22.021 1.00 30.85  0  199 ASN   A N   1 
ATOM   1515 C  CA  . ASN   A  1 184 ? 34.347  -34.081 -21.115 1.00 31.49  0  199 ASN   A CA  1 
ATOM   1516 C  C   . ASN   A  1 184 ? 34.176  -33.180 -19.893 1.00 30.52  0  199 ASN   A C   1 
ATOM   1517 O  O   . ASN   A  1 184 ? 33.076  -32.672 -19.713 1.00 31.17  0  199 ASN   A O   1 
ATOM   1518 C  CB  . ASN   A  1 184 ? 35.652  -33.913 -21.886 1.00 30.32  0  199 ASN   A CB  1 
ATOM   1519 C  CG  . ASN   A  1 184 ? 35.855  -32.520 -22.454 1.00 34.24  0  199 ASN   A CG  1 
ATOM   1520 O  OD1 . ASN   A  1 184 ? 35.358  -31.498 -21.941 1.00 31.70  0  199 ASN   A OD1 1 
ATOM   1521 N  ND2 . ASN   A  1 184 ? 36.624  -32.475 -23.534 1.00 35.36  0  199 ASN   A ND2 1 
ATOM   1522 N  N   . THR   A  1 185 ? 35.226  -32.982 -19.113 1.00 31.30  0  200 THR   A N   1 
ATOM   1523 C  CA  . THR   A  1 185 ? 35.194  -32.227 -17.834 1.00 35.62  0  200 THR   A CA  1 
ATOM   1524 C  C   . THR   A  1 185 ? 35.254  -30.722 -18.117 1.00 31.80  0  200 THR   A C   1 
ATOM   1525 O  O   . THR   A  1 185 ? 35.206  -29.995 -17.139 1.00 33.12  0  200 THR   A O   1 
ATOM   1526 C  CB  . THR   A  1 185 ? 36.312  -32.690 -16.880 1.00 32.98  0  200 THR   A CB  1 
ATOM   1527 O  OG1 . THR   A  1 185 ? 37.547  -32.529 -17.569 1.00 32.83  0  200 THR   A OG1 1 
ATOM   1528 C  CG2 . THR   A  1 185 ? 36.199  -34.150 -16.499 1.00 35.39  0  200 THR   A CG2 1 
ATOM   1529 N  N   . ARG   A  1 186 ? 35.275  -30.256 -19.370 1.00 33.44  0  201 ARG   A N   1 
ATOM   1530 C  CA  . ARG   A  1 186 ? 35.205  -28.795 -19.673 1.00 35.99  0  201 ARG   A CA  1 
ATOM   1531 C  C   . ARG   A  1 186 ? 33.981  -28.438 -20.541 1.00 34.16  0  201 ARG   A C   1 
ATOM   1532 O  O   . ARG   A  1 186 ? 33.696  -27.235 -20.715 1.00 35.37  0  201 ARG   A O   1 
ATOM   1533 C  CB  . ARG   A  1 186 ? 36.495  -28.371 -20.381 1.00 41.26  0  201 ARG   A CB  1 
ATOM   1534 C  CG  . ARG   A  1 186 ? 37.778  -28.565 -19.579 1.00 47.89  0  201 ARG   A CG  1 
ATOM   1535 C  CD  . ARG   A  1 186 ? 38.979  -28.576 -20.517 1.00 54.13  0  201 ARG   A CD  1 
ATOM   1536 N  NE  . ARG   A  1 186 ? 39.877  -29.711 -20.284 1.00 68.10  0  201 ARG   A NE  1 
ATOM   1537 C  CZ  . ARG   A  1 186 ? 39.760  -30.959 -20.758 1.00 67.58  0  201 ARG   A CZ  1 
ATOM   1538 N  NH1 . ARG   A  1 186 ? 38.751  -31.316 -21.532 1.00 70.74  1  201 ARG   A NH1 1 
ATOM   1539 N  NH2 . ARG   A  1 186 ? 40.678  -31.861 -20.451 1.00 76.67  0  201 ARG   A NH2 1 
ATOM   1540 N  N   . ARG   A  1 187 ? 33.336  -29.418 -21.168 1.00 29.00  0  202 ARG   A N   1 
ATOM   1541 C  CA  . ARG   A  1 187 ? 32.329  -29.195 -22.242 1.00 28.78  0  202 ARG   A CA  1 
ATOM   1542 C  C   . ARG   A  1 187 ? 31.183  -30.197 -22.052 1.00 29.09  0  202 ARG   A C   1 
ATOM   1543 O  O   . ARG   A  1 187 ? 31.429  -31.423 -22.155 1.00 29.31  0  202 ARG   A O   1 
ATOM   1544 C  CB  . ARG   A  1 187 ? 32.982  -29.412 -23.601 1.00 28.40  0  202 ARG   A CB  1 
ATOM   1545 C  CG  . ARG   A  1 187 ? 34.141  -28.492 -23.922 1.00 33.29  0  202 ARG   A CG  1 
ATOM   1546 C  CD  . ARG   A  1 187 ? 35.002  -29.092 -25.039 1.00 36.03  0  202 ARG   A CD  1 
ATOM   1547 N  NE  . ARG   A  1 187 ? 36.029  -28.128 -25.451 1.00 39.75  0  202 ARG   A NE  1 
ATOM   1548 C  CZ  . ARG   A  1 187 ? 35.826  -27.032 -26.188 1.00 45.31  0  202 ARG   A CZ  1 
ATOM   1549 N  NH1 . ARG   A  1 187 ? 34.631  -26.744 -26.683 1.00 47.55  1  202 ARG   A NH1 1 
ATOM   1550 N  NH2 . ARG   A  1 187 ? 36.836  -26.213 -26.432 1.00 49.48  0  202 ARG   A NH2 1 
ATOM   1551 N  N   . ASP   A  1 188 ? 29.989  -29.733 -21.707 1.00 27.95  0  203 ASP   A N   1 
ATOM   1552 C  CA  . ASP   A  1 188 ? 28.847  -30.651 -21.459 1.00 26.35  0  203 ASP   A CA  1 
ATOM   1553 C  C   . ASP   A  1 188 ? 27.561  -29.829 -21.550 1.00 28.20  0  203 ASP   A C   1 
ATOM   1554 O  O   . ASP   A  1 188 ? 27.619  -28.572 -21.561 1.00 24.09  0  203 ASP   A O   1 
ATOM   1555 C  CB  . ASP   A  1 188 ? 29.013  -31.383 -20.117 1.00 26.81  0  203 ASP   A CB  1 
ATOM   1556 C  CG  . ASP   A  1 188 ? 28.257  -32.704 -19.939 1.00 32.17  0  203 ASP   A CG  1 
ATOM   1557 O  OD1 . ASP   A  1 188 ? 27.420  -33.086 -20.863 1.00 31.48  0  203 ASP   A OD1 1 
ATOM   1558 O  OD2 . ASP   A  1 188 ? 28.466  -33.350 -18.865 1.00 30.13  -1 203 ASP   A OD2 1 
ATOM   1559 N  N   . SER   A  1 189 ? 26.442  -30.533 -21.609 1.00 25.62  0  204 SER   A N   1 
ATOM   1560 C  CA  . SER   A  1 189 ? 25.104  -29.977 -21.358 1.00 28.96  0  204 SER   A CA  1 
ATOM   1561 C  C   . SER   A  1 189 ? 24.819  -30.153 -19.870 1.00 30.40  0  204 SER   A C   1 
ATOM   1562 O  O   . SER   A  1 189 ? 25.512  -30.967 -19.198 1.00 25.27  0  204 SER   A O   1 
ATOM   1563 C  CB  . SER   A  1 189 ? 24.095  -30.665 -22.226 1.00 29.25  0  204 SER   A CB  1 
ATOM   1564 O  OG  . SER   A  1 189 ? 24.203  -32.066 -22.037 1.00 29.88  0  204 SER   A OG  1 
ATOM   1565 N  N   . CYS   A  1 190 ? 23.841  -29.411 -19.360 1.00 28.72  0  205 CYS   A N   1 
ATOM   1566 C  CA  . CYS   A  1 190 ? 23.516  -29.431 -17.922 1.00 30.02  0  205 CYS   A CA  1 
ATOM   1567 C  C   . CYS   A  1 190 ? 22.018  -29.228 -17.725 1.00 28.10  0  205 CYS   A C   1 
ATOM   1568 O  O   . CYS   A  1 190 ? 21.269  -29.248 -18.725 1.00 27.22  0  205 CYS   A O   1 
ATOM   1569 C  CB  . CYS   A  1 190 ? 24.409  -28.433 -17.203 1.00 33.86  0  205 CYS   A CB  1 
ATOM   1570 S  SG  . CYS   A  1 190 ? 24.595  -28.799 -15.435 1.00 38.85  0  205 CYS   A SG  1 
ATOM   1571 N  N   . GLN   A  1 191 ? 21.573  -29.129 -16.473 1.00 29.82  0  206 GLN   A N   1 
ATOM   1572 C  CA  . GLN   A  1 191 ? 20.132  -29.075 -16.113 1.00 27.03  0  206 GLN   A CA  1 
ATOM   1573 C  C   . GLN   A  1 191 ? 19.530  -27.869 -16.843 1.00 25.10  0  206 GLN   A C   1 
ATOM   1574 O  O   . GLN   A  1 191 ? 20.110  -26.789 -16.724 1.00 24.69  0  206 GLN   A O   1 
ATOM   1575 C  CB  . GLN   A  1 191 ? 19.935  -28.962 -14.603 1.00 31.03  0  206 GLN   A CB  1 
ATOM   1576 C  CG  . GLN   A  1 191 ? 20.055  -30.289 -13.850 1.00 34.68  0  206 GLN   A CG  1 
ATOM   1577 C  CD  . GLN   A  1 191 ? 21.415  -30.941 -13.935 1.00 33.28  0  206 GLN   A CD  1 
ATOM   1578 O  OE1 . GLN   A  1 191 ? 22.452  -30.327 -13.679 1.00 33.57  0  206 GLN   A OE1 1 
ATOM   1579 N  NE2 . GLN   A  1 191 ? 21.436  -32.211 -14.311 1.00 36.96  0  206 GLN   A NE2 1 
ATOM   1580 N  N   . GLY   A  1 192 ? 18.400  -28.040 -17.525 1.00 24.79  0  207 GLY   A N   1 
ATOM   1581 C  CA  . GLY   A  1 192 ? 17.764  -27.002 -18.378 1.00 25.13  0  207 GLY   A CA  1 
ATOM   1582 C  C   . GLY   A  1 192 ? 18.117  -27.159 -19.860 1.00 25.50  0  207 GLY   A C   1 
ATOM   1583 O  O   . GLY   A  1 192 ? 17.400  -26.573 -20.677 1.00 25.81  0  207 GLY   A O   1 
ATOM   1584 N  N   . ASP   A  1 193 ? 19.141  -27.961 -20.222 1.00 24.20  0  208 ASP   A N   1 
ATOM   1585 C  CA  . ASP   A  1 193 ? 19.468  -28.269 -21.641 1.00 23.36  0  208 ASP   A CA  1 
ATOM   1586 C  C   . ASP   A  1 193 ? 18.707  -29.501 -22.133 1.00 23.00  0  208 ASP   A C   1 
ATOM   1587 O  O   . ASP   A  1 193 ? 18.658  -29.705 -23.350 1.00 22.79  0  208 ASP   A O   1 
ATOM   1588 C  CB  . ASP   A  1 193 ? 20.972  -28.452 -21.814 1.00 26.55  0  208 ASP   A CB  1 
ATOM   1589 C  CG  . ASP   A  1 193 ? 21.737  -27.177 -21.578 1.00 25.60  0  208 ASP   A CG  1 
ATOM   1590 O  OD1 . ASP   A  1 193 ? 21.257  -26.123 -22.022 1.00 23.97  0  208 ASP   A OD1 1 
ATOM   1591 O  OD2 . ASP   A  1 193 ? 22.821  -27.253 -20.961 1.00 26.69  -1 208 ASP   A OD2 1 
ATOM   1592 N  N   . SER   A  1 194 ? 18.115  -30.274 -21.228 1.00 22.13  0  209 SER   A N   1 
ATOM   1593 C  CA  . SER   A  1 194 ? 17.291  -31.478 -21.495 1.00 22.68  0  209 SER   A CA  1 
ATOM   1594 C  C   . SER   A  1 194 ? 16.375  -31.229 -22.659 1.00 23.85  0  209 SER   A C   1 
ATOM   1595 O  O   . SER   A  1 194 ? 15.688  -30.169 -22.659 1.00 24.82  0  209 SER   A O   1 
ATOM   1596 C  CB  . SER   A  1 194 ? 16.484  -31.920 -20.306 1.00 26.50  0  209 SER   A CB  1 
ATOM   1597 O  OG  . SER   A  1 194 ? 17.329  -32.581 -19.379 1.00 30.42  0  209 SER   A OG  1 
ATOM   1598 N  N   . GLY   A  1 195 ? 16.311  -32.199 -23.567 1.00 22.64  0  210 GLY   A N   1 
ATOM   1599 C  CA  . GLY   A  1 195 ? 15.359  -32.174 -24.692 1.00 25.69  0  210 GLY   A CA  1 
ATOM   1600 C  C   . GLY   A  1 195 ? 15.910  -31.410 -25.893 1.00 22.54  0  210 GLY   A C   1 
ATOM   1601 O  O   . GLY   A  1 195 ? 15.360  -31.577 -26.967 1.00 25.80  0  210 GLY   A O   1 
ATOM   1602 N  N   . GLY   A  1 196 ? 16.957  -30.600 -25.699 1.00 24.80  0  211 GLY   A N   1 
ATOM   1603 C  CA  . GLY   A  1 196 ? 17.600  -29.825 -26.763 1.00 22.75  0  211 GLY   A CA  1 
ATOM   1604 C  C   . GLY   A  1 196 ? 18.442  -30.704 -27.671 1.00 25.88  0  211 GLY   A C   1 
ATOM   1605 O  O   . GLY   A  1 196 ? 18.658  -31.892 -27.406 1.00 27.78  0  211 GLY   A O   1 
ATOM   1606 N  N   . PRO   A  1 197 ? 18.932  -30.136 -28.790 1.00 25.67  0  212 PRO   A N   1 
ATOM   1607 C  CA  . PRO   A  1 197 ? 19.631  -30.923 -29.796 1.00 26.34  0  212 PRO   A CA  1 
ATOM   1608 C  C   . PRO   A  1 197 ? 21.149  -31.031 -29.607 1.00 26.14  0  212 PRO   A C   1 
ATOM   1609 O  O   . PRO   A  1 197 ? 21.791  -30.066 -29.182 1.00 26.54  0  212 PRO   A O   1 
ATOM   1610 C  CB  . PRO   A  1 197 ? 19.263  -30.148 -31.068 1.00 26.13  0  212 PRO   A CB  1 
ATOM   1611 C  CG  . PRO   A  1 197 ? 19.264  -28.661 -30.612 1.00 25.08  0  212 PRO   A CG  1 
ATOM   1612 C  CD  . PRO   A  1 197 ? 18.788  -28.714 -29.173 1.00 27.66  0  212 PRO   A CD  1 
ATOM   1613 N  N   . LEU   A  1 198 ? 21.673  -32.212 -29.932 1.00 25.46  0  213 LEU   A N   1 
ATOM   1614 C  CA  . LEU   A  1 198 ? 23.097  -32.410 -30.291 1.00 26.98  0  213 LEU   A CA  1 
ATOM   1615 C  C   . LEU   A  1 198 ? 23.146  -32.539 -31.823 1.00 26.56  0  213 LEU   A C   1 
ATOM   1616 O  O   . LEU   A  1 198 ? 22.492  -33.459 -32.372 1.00 24.00  0  213 LEU   A O   1 
ATOM   1617 C  CB  . LEU   A  1 198 ? 23.637  -33.661 -29.586 1.00 25.28  0  213 LEU   A CB  1 
ATOM   1618 C  CG  . LEU   A  1 198 ? 25.062  -34.070 -29.976 1.00 28.56  0  213 LEU   A CG  1 
ATOM   1619 C  CD1 . LEU   A  1 198 ? 26.070  -33.069 -29.466 1.00 30.25  0  213 LEU   A CD1 1 
ATOM   1620 C  CD2 . LEU   A  1 198 ? 25.403  -35.438 -29.444 1.00 33.02  0  213 LEU   A CD2 1 
ATOM   1621 N  N   . VAL   A  1 199 ? 23.891  -31.658 -32.476 1.00 25.27  0  214 VAL   A N   1 
ATOM   1622 C  CA  . VAL   A  1 199 ? 23.906  -31.546 -33.959 1.00 26.40  0  214 VAL   A CA  1 
ATOM   1623 C  C   . VAL   A  1 199 ? 25.347  -31.723 -34.455 1.00 29.78  0  214 VAL   A C   1 
ATOM   1624 O  O   . VAL   A  1 199 ? 26.273  -31.248 -33.824 1.00 30.21  0  214 VAL   A O   1 
ATOM   1625 C  CB  . VAL   A  1 199 ? 23.260  -30.237 -34.446 1.00 27.28  0  214 VAL   A CB  1 
ATOM   1626 C  CG1 . VAL   A  1 199 ? 21.785  -30.242 -34.158 1.00 28.26  0  214 VAL   A CG1 1 
ATOM   1627 C  CG2 . VAL   A  1 199 ? 23.912  -28.990 -33.849 1.00 28.82  0  214 VAL   A CG2 1 
ATOM   1628 N  N   . CYS   A  1 200 ? 25.526  -32.471 -35.537 1.00 33.93  0  215 CYS   A N   1 
ATOM   1629 C  CA  . CYS   A  1 200 ? 26.865  -32.712 -36.159 1.00 36.14  0  215 CYS   A CA  1 
ATOM   1630 C  C   . CYS   A  1 200 ? 26.760  -32.368 -37.642 1.00 33.86  0  215 CYS   A C   1 
ATOM   1631 O  O   . CYS   A  1 200 ? 25.712  -32.685 -38.280 1.00 30.20  0  215 CYS   A O   1 
ATOM   1632 C  CB  . CYS   A  1 200 ? 27.356  -34.154 -36.002 1.00 36.29  0  215 CYS   A CB  1 
ATOM   1633 S  SG  . CYS   A  1 200 ? 27.183  -34.791 -34.317 1.00 37.40  0  215 CYS   A SG  1 
ATOM   1634 N  N   . LYS   A  1 201 ? 27.771  -31.673 -38.141 1.00 38.57  0  216 LYS   A N   1 
ATOM   1635 C  CA  . LYS   A  1 201 ? 27.840  -31.229 -39.550 1.00 43.54  0  216 LYS   A CA  1 
ATOM   1636 C  C   . LYS   A  1 201 ? 28.433  -32.374 -40.368 1.00 40.11  0  216 LYS   A C   1 
ATOM   1637 O  O   . LYS   A  1 201 ? 29.587  -32.733 -40.112 1.00 38.32  0  216 LYS   A O   1 
ATOM   1638 C  CB  . LYS   A  1 201 ? 28.671  -29.949 -39.663 1.00 47.07  0  216 LYS   A CB  1 
ATOM   1639 C  CG  . LYS   A  1 201 ? 28.338  -29.121 -40.899 1.00 52.04  0  216 LYS   A CG  1 
ATOM   1640 C  CD  . LYS   A  1 201 ? 29.183  -27.865 -40.971 1.00 57.69  0  216 LYS   A CD  1 
ATOM   1641 C  CE  . LYS   A  1 201 ? 28.851  -26.986 -42.157 1.00 65.15  0  216 LYS   A CE  1 
ATOM   1642 N  NZ  . LYS   A  1 201 ? 29.290  -25.593 -41.928 1.00 63.91  1  216 LYS   A NZ  1 
ATOM   1643 N  N   . VAL   A  1 202 ? 27.634  -32.977 -41.237 1.00 39.01  0  217 VAL   A N   1 
ATOM   1644 C  CA  . VAL   A  1 202 ? 28.043  -34.155 -42.060 1.00 39.48  0  217 VAL   A CA  1 
ATOM   1645 C  C   . VAL   A  1 202 ? 27.834  -33.786 -43.536 1.00 41.18  0  217 VAL   A C   1 
ATOM   1646 O  O   . VAL   A  1 202 ? 26.686  -33.459 -43.891 1.00 42.76  0  217 VAL   A O   1 
ATOM   1647 C  CB  . VAL   A  1 202 ? 27.246  -35.406 -41.674 1.00 41.51  0  217 VAL   A CB  1 
ATOM   1648 C  CG1 . VAL   A  1 202 ? 27.746  -36.619 -42.446 1.00 43.37  0  217 VAL   A CG1 1 
ATOM   1649 C  CG2 . VAL   A  1 202 ? 27.259  -35.662 -40.172 1.00 39.16  0  217 VAL   A CG2 1 
ATOM   1650 N  N   . ASN   A  1 203 ? 28.902  -33.799 -44.346 1.00 46.25  0  218 ASN   A N   1 
ATOM   1651 C  CA  . ASN   A  1 203 ? 28.888  -33.493 -45.813 1.00 44.59  0  218 ASN   A CA  1 
ATOM   1652 C  C   . ASN   A  1 203 ? 28.104  -32.188 -46.043 1.00 44.84  0  218 ASN   A C   1 
ATOM   1653 O  O   . ASN   A  1 203 ? 27.140  -32.195 -46.859 1.00 43.73  0  218 ASN   A O   1 
ATOM   1654 C  CB  . ASN   A  1 203 ? 28.367  -34.678 -46.636 1.00 47.63  0  218 ASN   A CB  1 
ATOM   1655 C  CG  . ASN   A  1 203 ? 29.113  -35.977 -46.392 0.00 47.62  0  218 ASN   A CG  1 
ATOM   1656 O  OD1 . ASN   A  1 203 ? 30.234  -35.974 -45.887 0.00 47.59  0  218 ASN   A OD1 1 
ATOM   1657 N  ND2 . ASN   A  1 203 ? 28.491  -37.094 -46.733 0.00 47.69  0  218 ASN   A ND2 1 
ATOM   1658 N  N   . GLY   A  1 204 ? 28.469  -31.140 -45.283 1.00 47.02  0  219 GLY   A N   1 
ATOM   1659 C  CA  . GLY   A  1 204 ? 27.917  -29.770 -45.345 1.00 46.41  0  219 GLY   A CA  1 
ATOM   1660 C  C   . GLY   A  1 204 ? 26.494  -29.619 -44.816 1.00 51.81  0  219 GLY   A C   1 
ATOM   1661 O  O   . GLY   A  1 204 ? 25.966  -28.484 -44.923 1.00 47.81  0  219 GLY   A O   1 
ATOM   1662 N  N   . THR   A  1 205 ? 25.873  -30.657 -44.239 1.00 49.31  0  220 THR   A N   1 
ATOM   1663 C  CA  . THR   A  1 205 ? 24.496  -30.555 -43.680 1.00 44.25  0  220 THR   A CA  1 
ATOM   1664 C  C   . THR   A  1 205 ? 24.547  -30.747 -42.163 1.00 40.32  0  220 THR   A C   1 
ATOM   1665 O  O   . THR   A  1 205 ? 25.301  -31.632 -41.678 1.00 35.89  0  220 THR   A O   1 
ATOM   1666 C  CB  . THR   A  1 205 ? 23.547  -31.547 -44.347 1.00 47.03  0  220 THR   A CB  1 
ATOM   1667 O  OG1 . THR   A  1 205 ? 23.634  -31.267 -45.740 1.00 49.66  0  220 THR   A OG1 1 
ATOM   1668 C  CG2 . THR   A  1 205 ? 22.106  -31.410 -43.894 1.00 48.75  0  220 THR   A CG2 1 
ATOM   1669 N  N   . TRP   A  1 206 ? 23.778  -29.944 -41.434 1.00 37.41  0  221 TRP   A N   1 
ATOM   1670 C  CA  . TRP   A  1 206 ? 23.623  -30.126 -39.966 1.00 32.61  0  221 TRP   A CA  1 
ATOM   1671 C  C   . TRP   A  1 206 ? 22.610  -31.245 -39.742 1.00 27.98  0  221 TRP   A C   1 
ATOM   1672 O  O   . TRP   A  1 206 ? 21.470  -31.099 -40.259 1.00 26.47  0  221 TRP   A O   1 
ATOM   1673 C  CB  . TRP   A  1 206 ? 23.190  -28.832 -39.280 1.00 37.49  0  221 TRP   A CB  1 
ATOM   1674 C  CG  . TRP   A  1 206 ? 24.314  -27.862 -39.127 1.00 34.72  0  221 TRP   A CG  1 
ATOM   1675 C  CD1 . TRP   A  1 206 ? 24.447  -26.692 -39.806 1.00 38.16  0  221 TRP   A CD1 1 
ATOM   1676 C  CD2 . TRP   A  1 206 ? 25.413  -27.932 -38.199 1.00 35.79  0  221 TRP   A CD2 1 
ATOM   1677 N  NE1 . TRP   A  1 206 ? 25.588  -26.054 -39.413 1.00 38.85  0  221 TRP   A NE1 1 
ATOM   1678 C  CE2 . TRP   A  1 206 ? 26.199  -26.781 -38.424 1.00 37.85  0  221 TRP   A CE2 1 
ATOM   1679 C  CE3 . TRP   A  1 206 ? 25.843  -28.866 -37.246 1.00 35.30  0  221 TRP   A CE3 1 
ATOM   1680 C  CZ2 . TRP   A  1 206 ? 27.386  -26.544 -37.734 1.00 36.95  0  221 TRP   A CZ2 1 
ATOM   1681 C  CZ3 . TRP   A  1 206 ? 26.998  -28.618 -36.547 1.00 38.42  0  221 TRP   A CZ3 1 
ATOM   1682 C  CH2 . TRP   A  1 206 ? 27.767  -27.480 -36.800 1.00 38.89  0  221 TRP   A CH2 1 
ATOM   1683 N  N   . LEU   A  1 207 ? 23.007  -32.310 -39.036 1.00 26.48  0  222 LEU   A N   1 
ATOM   1684 C  CA  . LEU   A  1 207 ? 22.109  -33.456 -38.699 1.00 28.62  0  222 LEU   A CA  1 
ATOM   1685 C  C   . LEU   A  1 207 ? 21.905  -33.516 -37.180 1.00 25.77  0  222 LEU   A C   1 
ATOM   1686 O  O   . LEU   A  1 207 ? 22.935  -33.432 -36.414 1.00 26.65  0  222 LEU   A O   1 
ATOM   1687 C  CB  . LEU   A  1 207 ? 22.772  -34.740 -39.217 1.00 30.42  0  222 LEU   A CB  1 
ATOM   1688 C  CG  . LEU   A  1 207 ? 22.996  -34.852 -40.721 1.00 30.62  0  222 LEU   A CG  1 
ATOM   1689 C  CD1 . LEU   A  1 207 ? 23.505  -36.253 -41.063 1.00 30.62  0  222 LEU   A CD1 1 
ATOM   1690 C  CD2 . LEU   A  1 207 ? 21.729  -34.567 -41.503 1.00 31.62  0  222 LEU   A CD2 1 
ATOM   1691 N  N   . GLN   A  1 208 ? 20.690  -33.775 -36.726 1.00 24.48  0  223 GLN   A N   1 
ATOM   1692 C  CA  . GLN   A  1 208 ? 20.486  -33.997 -35.269 1.00 24.92  0  223 GLN   A CA  1 
ATOM   1693 C  C   . GLN   A  1 208 ? 20.837  -35.445 -34.915 1.00 24.57  0  223 GLN   A C   1 
ATOM   1694 O  O   . GLN   A  1 208 ? 19.999  -36.344 -35.090 1.00 25.81  0  223 GLN   A O   1 
ATOM   1695 C  CB  . GLN   A  1 208 ? 19.083  -33.644 -34.792 1.00 25.14  0  223 GLN   A CB  1 
ATOM   1696 C  CG  . GLN   A  1 208 ? 19.042  -33.556 -33.269 1.00 25.76  0  223 GLN   A CG  1 
ATOM   1697 C  CD  . GLN   A  1 208 ? 17.779  -32.996 -32.670 1.00 25.07  0  223 GLN   A CD  1 
ATOM   1698 O  OE1 . GLN   A  1 208 ? 16.980  -32.301 -33.328 1.00 25.28  0  223 GLN   A OE1 1 
ATOM   1699 N  NE2 . GLN   A  1 208 ? 17.612  -33.289 -31.393 1.00 22.89  0  223 GLN   A NE2 1 
ATOM   1700 N  N   . ALA   A  1 209 ? 21.987  -35.640 -34.291 1.00 27.59  0  224 ALA   A N   1 
ATOM   1701 C  CA  . ALA   A  1 209 ? 22.471  -36.932 -33.769 1.00 27.27  0  224 ALA   A CA  1 
ATOM   1702 C  C   . ALA   A  1 209 ? 21.776  -37.331 -32.455 1.00 27.77  0  224 ALA   A C   1 
ATOM   1703 O  O   . ALA   A  1 209 ? 21.553  -38.541 -32.239 1.00 26.61  0  224 ALA   A O   1 
ATOM   1704 C  CB  . ALA   A  1 209 ? 23.965  -36.815 -33.582 1.00 27.79  0  224 ALA   A CB  1 
ATOM   1705 N  N   . GLY   A  1 210 ? 21.501  -36.367 -31.573 1.00 25.86  0  225 GLY   A N   1 
ATOM   1706 C  CA  . GLY   A  1 210 ? 21.106  -36.642 -30.178 1.00 26.46  0  225 GLY   A CA  1 
ATOM   1707 C  C   . GLY   A  1 210 ? 20.022  -35.707 -29.639 1.00 24.91  0  225 GLY   A C   1 
ATOM   1708 O  O   . GLY   A  1 210 ? 19.895  -34.560 -30.107 1.00 24.23  0  225 GLY   A O   1 
ATOM   1709 N  N   . VAL   A  1 211 ? 19.345  -36.164 -28.602 1.00 24.04  0  226 VAL   A N   1 
ATOM   1710 C  CA  . VAL   A  1 211 ? 18.506  -35.337 -27.700 1.00 23.86  0  226 VAL   A CA  1 
ATOM   1711 C  C   . VAL   A  1 211 ? 19.161  -35.361 -26.314 1.00 24.26  0  226 VAL   A C   1 
ATOM   1712 O  O   . VAL   A  1 211 ? 19.436  -36.459 -25.830 1.00 24.11  0  226 VAL   A O   1 
ATOM   1713 C  CB  . VAL   A  1 211 ? 17.067  -35.857 -27.664 1.00 25.74  0  226 VAL   A CB  1 
ATOM   1714 C  CG1 . VAL   A  1 211 ? 16.218  -34.992 -26.749 1.00 27.20  0  226 VAL   A CG1 1 
ATOM   1715 C  CG2 . VAL   A  1 211 ? 16.436  -35.940 -29.054 1.00 27.64  0  226 VAL   A CG2 1 
ATOM   1716 N  N   . VAL   A  1 212 ? 19.423  -34.197 -25.705 1.00 23.11  0  227 VAL   A N   1 
ATOM   1717 C  CA  . VAL   A  1 212 ? 19.979  -34.085 -24.321 1.00 22.49  0  227 VAL   A CA  1 
ATOM   1718 C  C   . VAL   A  1 212 ? 19.099  -34.897 -23.372 1.00 22.44  0  227 VAL   A C   1 
ATOM   1719 O  O   . VAL   A  1 212 ? 17.899  -34.636 -23.299 1.00 23.07  0  227 VAL   A O   1 
ATOM   1720 C  CB  . VAL   A  1 212 ? 20.138  -32.636 -23.845 1.00 25.59  0  227 VAL   A CB  1 
ATOM   1721 C  CG1 . VAL   A  1 212 ? 20.673  -32.576 -22.413 1.00 29.68  0  227 VAL   A CG1 1 
ATOM   1722 C  CG2 . VAL   A  1 212 ? 21.069  -31.851 -24.762 1.00 27.11  0  227 VAL   A CG2 1 
ATOM   1723 N  N   . SER   A  1 213 ? 19.664  -35.922 -22.733 1.00 22.13  0  228 SER   A N   1 
ATOM   1724 C  CA  . SER   A  1 213 ? 18.881  -36.890 -21.928 1.00 21.40  0  228 SER   A CA  1 
ATOM   1725 C  C   . SER   A  1 213 ? 19.341  -36.829 -20.469 1.00 22.26  0  228 SER   A C   1 
ATOM   1726 O  O   . SER   A  1 213 ? 18.564  -36.321 -19.597 1.00 21.78  0  228 SER   A O   1 
ATOM   1727 C  CB  . SER   A  1 213 ? 18.983  -38.284 -22.515 1.00 21.14  0  228 SER   A CB  1 
ATOM   1728 O  OG  . SER   A  1 213 ? 18.072  -39.122 -21.822 1.00 22.90  0  228 SER   A OG  1 
ATOM   1729 N  N   . TRP   A  1 214 ? 20.552  -37.301 -20.176 1.00 19.29  0  229 TRP   A N   1 
ATOM   1730 C  CA  . TRP   A  1 214 ? 20.952  -37.494 -18.758 1.00 21.80  0  229 TRP   A CA  1 
ATOM   1731 C  C   . TRP   A  1 214 ? 22.469  -37.571 -18.619 1.00 21.98  0  229 TRP   A C   1 
ATOM   1732 O  O   . TRP   A  1 214 ? 23.189  -37.508 -19.618 1.00 21.59  0  229 TRP   A O   1 
ATOM   1733 C  CB  . TRP   A  1 214 ? 20.254  -38.705 -18.122 1.00 23.90  0  229 TRP   A CB  1 
ATOM   1734 C  CG  . TRP   A  1 214 ? 20.683  -40.037 -18.652 1.00 25.36  0  229 TRP   A CG  1 
ATOM   1735 C  CD1 . TRP   A  1 214 ? 20.268  -40.625 -19.809 1.00 26.16  0  229 TRP   A CD1 1 
ATOM   1736 C  CD2 . TRP   A  1 214 ? 21.532  -40.995 -18.003 1.00 24.65  0  229 TRP   A CD2 1 
ATOM   1737 N  NE1 . TRP   A  1 214 ? 20.837  -41.854 -19.950 1.00 26.95  0  229 TRP   A NE1 1 
ATOM   1738 C  CE2 . TRP   A  1 214 ? 21.642  -42.102 -18.875 1.00 25.16  0  229 TRP   A CE2 1 
ATOM   1739 C  CE3 . TRP   A  1 214 ? 22.262  -40.999 -16.815 1.00 25.60  0  229 TRP   A CE3 1 
ATOM   1740 C  CZ2 . TRP   A  1 214 ? 22.409  -43.223 -18.572 1.00 26.73  0  229 TRP   A CZ2 1 
ATOM   1741 C  CZ3 . TRP   A  1 214 ? 23.056  -42.090 -16.531 1.00 26.64  0  229 TRP   A CZ3 1 
ATOM   1742 C  CH2 . TRP   A  1 214 ? 23.105  -43.196 -17.383 1.00 25.75  0  229 TRP   A CH2 1 
ATOM   1743 N  N   . GLY   A  1 215 ? 22.904  -37.622 -17.361 1.00 24.15  0  230 GLY   A N   1 
ATOM   1744 C  CA  . GLY   A  1 215 ? 24.305  -37.810 -16.972 1.00 25.39  0  230 GLY   A CA  1 
ATOM   1745 C  C   . GLY   A  1 215 ? 24.354  -37.861 -15.464 1.00 27.84  0  230 GLY   A C   1 
ATOM   1746 O  O   . GLY   A  1 215 ? 23.312  -37.627 -14.821 1.00 23.56  0  230 GLY   A O   1 
ATOM   1747 N  N   A GLU   A  1 216 ? 25.517  -38.193 -14.911 0.50 28.15  0  231 GLU   A N   1 
ATOM   1748 N  N   B GLU   A  1 216 ? 25.513  -38.213 -14.901 0.50 27.01  0  231 GLU   A N   1 
ATOM   1749 C  CA  A GLU   A  1 216 ? 25.792  -38.050 -13.458 0.50 28.65  0  231 GLU   A CA  1 
ATOM   1750 C  CA  B GLU   A  1 216 ? 25.785  -38.031 -13.449 0.50 26.72  0  231 GLU   A CA  1 
ATOM   1751 C  C   A GLU   A  1 216 ? 26.432  -36.673 -13.292 0.50 28.38  0  231 GLU   A C   1 
ATOM   1752 C  C   B GLU   A  1 216 ? 26.429  -36.663 -13.299 0.50 27.29  0  231 GLU   A C   1 
ATOM   1753 O  O   A GLU   A  1 216 ? 27.616  -36.508 -13.693 0.50 30.29  0  231 GLU   A O   1 
ATOM   1754 O  O   B GLU   A  1 216 ? 27.616  -36.506 -13.701 0.50 29.21  0  231 GLU   A O   1 
ATOM   1755 C  CB  A GLU   A  1 216 ? 26.625  -39.236 -12.964 0.50 31.18  0  231 GLU   A CB  1 
ATOM   1756 C  CB  B GLU   A  1 216 ? 26.705  -39.089 -12.848 0.50 27.53  0  231 GLU   A CB  1 
ATOM   1757 C  CG  A GLU   A  1 216 ? 25.830  -40.540 -12.889 0.50 33.97  0  231 GLU   A CG  1 
ATOM   1758 C  CG  B GLU   A  1 216 ? 26.940  -38.862 -11.359 0.50 29.28  0  231 GLU   A CG  1 
ATOM   1759 C  CD  A GLU   A  1 216 ? 26.567  -41.718 -12.258 0.50 38.10  0  231 GLU   A CD  1 
ATOM   1760 C  CD  B GLU   A  1 216 ? 28.018  -39.751 -10.765 0.50 28.58  0  231 GLU   A CD  1 
ATOM   1761 O  OE1 A GLU   A  1 216 ? 27.527  -41.457 -11.490 0.50 39.37  0  231 GLU   A OE1 1 
ATOM   1762 O  OE1 B GLU   A  1 216 ? 28.021  -40.940 -11.081 0.50 29.20  0  231 GLU   A OE1 1 
ATOM   1763 O  OE2 A GLU   A  1 216 ? 26.185  -42.896 -12.539 0.50 35.55  -1 231 GLU   A OE2 1 
ATOM   1764 O  OE2 B GLU   A  1 216 ? 28.845  -39.252 -10.022 0.50 27.28  -1 231 GLU   A OE2 1 
ATOM   1765 N  N   . GLY   A  1 217 ? 25.634  -35.692 -12.855 1.00 26.78  0  232 GLY   A N   1 
ATOM   1766 C  CA  . GLY   A  1 217 ? 26.019  -34.273 -12.861 1.00 28.80  0  232 GLY   A CA  1 
ATOM   1767 C  C   . GLY   A  1 217 ? 26.337  -33.814 -14.271 1.00 28.74  0  232 GLY   A C   1 
ATOM   1768 O  O   . GLY   A  1 217 ? 25.824  -34.412 -15.246 1.00 29.50  0  232 GLY   A O   1 
ATOM   1769 N  N   . CYS   A  1 218 ? 27.183  -32.797 -14.363 1.00 28.28  0  233 CYS   A N   1 
ATOM   1770 C  CA  . CYS   A  1 218 ? 27.595  -32.135 -15.616 1.00 28.57  0  233 CYS   A CA  1 
ATOM   1771 C  C   . CYS   A  1 218 ? 29.113  -31.945 -15.563 1.00 31.54  0  233 CYS   A C   1 
ATOM   1772 O  O   . CYS   A  1 218 ? 29.622  -31.503 -14.506 1.00 31.61  0  233 CYS   A O   1 
ATOM   1773 C  CB  . CYS   A  1 218 ? 26.898  -30.782 -15.746 1.00 31.35  0  233 CYS   A CB  1 
ATOM   1774 S  SG  . CYS   A  1 218 ? 25.124  -30.889 -15.407 1.00 40.43  0  233 CYS   A SG  1 
ATOM   1775 N  N   . ALA   A  1 219 ? 29.810  -32.322 -16.634 1.00 30.12  0  234 ALA   A N   1 
ATOM   1776 C  CA  . ALA   A  1 219 ? 31.253  -32.171 -16.810 1.00 31.18  0  234 ALA   A CA  1 
ATOM   1777 C  C   . ALA   A  1 219 ? 32.022  -32.829 -15.648 1.00 31.97  0  234 ALA   A C   1 
ATOM   1778 O  O   . ALA   A  1 219 ? 33.077  -32.332 -15.374 1.00 31.36  0  234 ALA   A O   1 
ATOM   1779 C  CB  . ALA   A  1 219 ? 31.560  -30.698 -16.951 1.00 31.40  0  234 ALA   A CB  1 
ATOM   1780 N  N   . GLN   A  1 220 ? 31.529  -33.939 -15.073 1.00 30.91  0  235 GLN   A N   1 
ATOM   1781 C  CA  . GLN   A  1 220 ? 32.174  -34.690 -13.966 1.00 34.00  0  235 GLN   A CA  1 
ATOM   1782 C  C   . GLN   A  1 220 ? 33.164  -35.717 -14.533 1.00 32.11  0  235 GLN   A C   1 
ATOM   1783 O  O   . GLN   A  1 220 ? 32.929  -36.285 -15.592 1.00 30.28  0  235 GLN   A O   1 
ATOM   1784 C  CB  . GLN   A  1 220 ? 31.139  -35.402 -13.096 1.00 38.38  0  235 GLN   A CB  1 
ATOM   1785 C  CG  . GLN   A  1 220 ? 30.226  -34.505 -12.272 1.00 41.42  0  235 GLN   A CG  1 
ATOM   1786 C  CD  . GLN   A  1 220 ? 31.012  -33.753 -11.228 1.00 46.11  0  235 GLN   A CD  1 
ATOM   1787 O  OE1 . GLN   A  1 220 ? 31.184  -34.210 -10.104 1.00 48.55  0  235 GLN   A OE1 1 
ATOM   1788 N  NE2 . GLN   A  1 220 ? 31.568  -32.621 -11.619 1.00 47.31  0  235 GLN   A NE2 1 
ATOM   1789 N  N   . PRO   A  1 221 ? 34.296  -35.989 -13.833 1.00 32.12  0  236 PRO   A N   1 
ATOM   1790 C  CA  . PRO   A  1 221 ? 35.276  -36.994 -14.253 1.00 31.73  0  236 PRO   A CA  1 
ATOM   1791 C  C   . PRO   A  1 221 ? 34.629  -38.361 -14.500 1.00 29.51  0  236 PRO   A C   1 
ATOM   1792 O  O   . PRO   A  1 221 ? 33.855  -38.784 -13.649 1.00 28.46  0  236 PRO   A O   1 
ATOM   1793 C  CB  . PRO   A  1 221 ? 36.297  -37.077 -13.092 1.00 33.18  0  236 PRO   A CB  1 
ATOM   1794 C  CG  . PRO   A  1 221 ? 36.128  -35.790 -12.318 1.00 33.76  0  236 PRO   A CG  1 
ATOM   1795 C  CD  . PRO   A  1 221 ? 34.707  -35.323 -12.581 1.00 36.33  0  236 PRO   A CD  1 
ATOM   1796 N  N   . ASN   A  1 222 ? 34.933  -38.979 -15.658 1.00 31.60  0  237 ASN   A N   1 
ATOM   1797 C  CA  . ASN   A  1 222 ? 34.447  -40.332 -16.063 1.00 33.26  0  237 ASN   A CA  1 
ATOM   1798 C  C   . ASN   A  1 222 ? 32.915  -40.382 -16.179 1.00 30.44  0  237 ASN   A C   1 
ATOM   1799 O  O   . ASN   A  1 222 ? 32.337  -41.505 -16.060 1.00 27.24  0  237 ASN   A O   1 
ATOM   1800 C  CB  . ASN   A  1 222 ? 34.932  -41.418 -15.083 1.00 32.14  0  237 ASN   A CB  1 
ATOM   1801 C  CG  . ASN   A  1 222 ? 36.421  -41.634 -15.221 1.00 36.11  0  237 ASN   A CG  1 
ATOM   1802 O  OD1 . ASN   A  1 222 ? 36.958  -41.651 -16.323 1.00 34.31  0  237 ASN   A OD1 1 
ATOM   1803 N  ND2 . ASN   A  1 222 ? 37.100  -41.828 -14.105 1.00 38.53  0  237 ASN   A ND2 1 
ATOM   1804 N  N   . ARG   A  1 223 ? 32.260  -39.252 -16.454 1.00 32.20  0  238 ARG   A N   1 
ATOM   1805 C  CA  . ARG   A  1 223 ? 30.777  -39.193 -16.528 1.00 29.99  0  238 ARG   A CA  1 
ATOM   1806 C  C   . ARG   A  1 223 ? 30.383  -38.290 -17.694 1.00 30.90  0  238 ARG   A C   1 
ATOM   1807 O  O   . ARG   A  1 223 ? 29.831  -37.210 -17.515 1.00 30.08  0  238 ARG   A O   1 
ATOM   1808 C  CB  . ARG   A  1 223 ? 30.213  -38.728 -15.185 1.00 29.51  0  238 ARG   A CB  1 
ATOM   1809 C  CG  . ARG   A  1 223 ? 30.504  -39.648 -14.008 1.00 29.91  0  238 ARG   A CG  1 
ATOM   1810 C  CD  . ARG   A  1 223 ? 29.801  -41.004 -14.093 1.00 29.84  0  238 ARG   A CD  1 
ATOM   1811 N  NE  . ARG   A  1 223 ? 29.981  -41.815 -12.918 1.00 32.18  0  238 ARG   A NE  1 
ATOM   1812 C  CZ  . ARG   A  1 223 ? 30.972  -42.679 -12.677 1.00 33.33  0  238 ARG   A CZ  1 
ATOM   1813 N  NH1 . ARG   A  1 223 ? 31.970  -42.872 -13.535 1.00 29.85  1  238 ARG   A NH1 1 
ATOM   1814 N  NH2 . ARG   A  1 223 ? 30.944  -43.345 -11.527 1.00 35.47  0  238 ARG   A NH2 1 
ATOM   1815 N  N   . PRO   A  1 224 ? 30.668  -38.697 -18.944 1.00 31.73  0  239 PRO   A N   1 
ATOM   1816 C  CA  . PRO   A  1 224 ? 30.246  -37.895 -20.088 1.00 27.88  0  239 PRO   A CA  1 
ATOM   1817 C  C   . PRO   A  1 224 ? 28.726  -37.759 -20.194 1.00 24.58  0  239 PRO   A C   1 
ATOM   1818 O  O   . PRO   A  1 224 ? 27.998  -38.548 -19.628 1.00 27.44  0  239 PRO   A O   1 
ATOM   1819 C  CB  . PRO   A  1 224 ? 30.810  -38.580 -21.322 1.00 29.00  0  239 PRO   A CB  1 
ATOM   1820 C  CG  . PRO   A  1 224 ? 31.453  -39.878 -20.845 1.00 30.06  0  239 PRO   A CG  1 
ATOM   1821 C  CD  . PRO   A  1 224 ? 31.422  -39.897 -19.328 1.00 30.13  0  239 PRO   A CD  1 
ATOM   1822 N  N   . GLY   A  1 225 ? 28.279  -36.746 -20.926 1.00 24.79  0  240 GLY   A N   1 
ATOM   1823 C  CA  . GLY   A  1 225 ? 26.839  -36.518 -21.177 1.00 26.00  0  240 GLY   A CA  1 
ATOM   1824 C  C   . GLY   A  1 225 ? 26.249  -37.650 -22.005 1.00 22.54  0  240 GLY   A C   1 
ATOM   1825 O  O   . GLY   A  1 225 ? 26.907  -38.127 -22.936 1.00 24.25  0  240 GLY   A O   1 
ATOM   1826 N  N   . ILE   A  1 226 ? 25.034  -38.043 -21.698 1.00 24.04  0  241 ILE   A N   1 
ATOM   1827 C  CA  . ILE   A  1 226 ? 24.283  -39.086 -22.449 1.00 27.29  0  241 ILE   A CA  1 
ATOM   1828 C  C   . ILE   A  1 226 ? 23.094  -38.432 -23.170 1.00 26.87  0  241 ILE   A C   1 
ATOM   1829 O  O   . ILE   A  1 226 ? 22.428  -37.579 -22.594 1.00 30.44  0  241 ILE   A O   1 
ATOM   1830 C  CB  . ILE   A  1 226 ? 23.812  -40.197 -21.515 1.00 27.08  0  241 ILE   A CB  1 
ATOM   1831 C  CG1 . ILE   A  1 226 ? 24.890  -40.631 -20.514 1.00 29.70  0  241 ILE   A CG1 1 
ATOM   1832 C  CG2 . ILE   A  1 226 ? 23.290  -41.365 -22.328 1.00 29.20  0  241 ILE   A CG2 1 
ATOM   1833 C  CD1 . ILE   A  1 226 ? 26.140  -41.108 -21.135 1.00 32.22  0  241 ILE   A CD1 1 
ATOM   1834 N  N   . TYR   A  1 227 ? 22.849  -38.884 -24.390 1.00 23.40  0  242 TYR   A N   1 
ATOM   1835 C  CA  . TYR   A  1 227 ? 21.869  -38.354 -25.365 1.00 26.84  0  242 TYR   A CA  1 
ATOM   1836 C  C   . TYR   A  1 227 ? 21.022  -39.510 -25.883 1.00 26.51  0  242 TYR   A C   1 
ATOM   1837 O  O   . TYR   A  1 227 ? 21.563  -40.618 -26.022 1.00 25.57  0  242 TYR   A O   1 
ATOM   1838 C  CB  . TYR   A  1 227 ? 22.631  -37.658 -26.494 1.00 23.37  0  242 TYR   A CB  1 
ATOM   1839 C  CG  . TYR   A  1 227 ? 23.438  -36.479 -26.028 1.00 23.71  0  242 TYR   A CG  1 
ATOM   1840 C  CD1 . TYR   A  1 227 ? 24.663  -36.616 -25.377 1.00 23.49  0  242 TYR   A CD1 1 
ATOM   1841 C  CD2 . TYR   A  1 227 ? 22.976  -35.194 -26.262 1.00 25.44  0  242 TYR   A CD2 1 
ATOM   1842 C  CE1 . TYR   A  1 227 ? 25.382  -35.510 -24.962 1.00 23.57  0  242 TYR   A CE1 1 
ATOM   1843 C  CE2 . TYR   A  1 227 ? 23.688  -34.081 -25.853 1.00 23.96  0  242 TYR   A CE2 1 
ATOM   1844 C  CZ  . TYR   A  1 227 ? 24.895  -34.232 -25.205 1.00 25.79  0  242 TYR   A CZ  1 
ATOM   1845 O  OH  . TYR   A  1 227 ? 25.516  -33.093 -24.792 1.00 23.63  0  242 TYR   A OH  1 
ATOM   1846 N  N   . THR   A  1 228 ? 19.739  -39.284 -26.139 1.00 25.42  0  243 THR   A N   1 
ATOM   1847 C  CA  . THR   A  1 228 ? 18.931  -40.218 -26.939 1.00 25.42  0  243 THR   A CA  1 
ATOM   1848 C  C   . THR   A  1 228 ? 19.502  -40.236 -28.355 1.00 24.88  0  243 THR   A C   1 
ATOM   1849 O  O   . THR   A  1 228 ? 19.715  -39.136 -28.909 1.00 25.36  0  243 THR   A O   1 
ATOM   1850 C  CB  . THR   A  1 228 ? 17.442  -39.871 -26.923 1.00 24.76  0  243 THR   A CB  1 
ATOM   1851 O  OG1 . THR   A  1 228 ? 17.095  -39.604 -25.566 1.00 25.68  0  243 THR   A OG1 1 
ATOM   1852 C  CG2 . THR   A  1 228 ? 16.622  -41.027 -27.438 1.00 26.42  0  243 THR   A CG2 1 
ATOM   1853 N  N   . ARG   A  1 229 ? 19.798  -41.425 -28.882 1.00 23.42  0  244 ARG   A N   1 
ATOM   1854 C  CA  . ARG   A  1 229 ? 20.357  -41.619 -30.243 1.00 26.37  0  244 ARG   A CA  1 
ATOM   1855 C  C   . ARG   A  1 229 ? 19.200  -41.511 -31.259 1.00 22.58  0  244 ARG   A C   1 
ATOM   1856 O  O   . ARG   A  1 229 ? 18.350  -42.406 -31.300 1.00 20.92  0  244 ARG   A O   1 
ATOM   1857 C  CB  . ARG   A  1 229 ? 21.122  -42.944 -30.298 1.00 26.45  0  244 ARG   A CB  1 
ATOM   1858 C  CG  . ARG   A  1 229 ? 21.770  -43.238 -31.648 1.00 29.16  0  244 ARG   A CG  1 
ATOM   1859 C  CD  . ARG   A  1 229 ? 22.534  -44.548 -31.686 1.00 30.12  0  244 ARG   A CD  1 
ATOM   1860 N  NE  . ARG   A  1 229 ? 23.744  -44.428 -30.896 1.00 30.05  0  244 ARG   A NE  1 
ATOM   1861 C  CZ  . ARG   A  1 229 ? 24.913  -43.930 -31.296 1.00 29.62  0  244 ARG   A CZ  1 
ATOM   1862 N  NH1 . ARG   A  1 229 ? 25.097  -43.514 -32.536 1.00 29.72  1  244 ARG   A NH1 1 
ATOM   1863 N  NH2 . ARG   A  1 229 ? 25.940  -43.924 -30.457 1.00 30.52  0  244 ARG   A NH2 1 
ATOM   1864 N  N   . VAL   A  1 230 ? 19.163  -40.432 -32.035 1.00 23.99  0  245 VAL   A N   1 
ATOM   1865 C  CA  . VAL   A  1 230 ? 17.985  -40.125 -32.900 1.00 25.11  0  245 VAL   A CA  1 
ATOM   1866 C  C   . VAL   A  1 230 ? 17.814  -41.248 -33.941 1.00 25.21  0  245 VAL   A C   1 
ATOM   1867 O  O   . VAL   A  1 230 ? 16.631  -41.642 -34.177 1.00 26.61  0  245 VAL   A O   1 
ATOM   1868 C  CB  . VAL   A  1 230 ? 18.074  -38.731 -33.537 1.00 24.76  0  245 VAL   A CB  1 
ATOM   1869 C  CG1 . VAL   A  1 230 ? 16.998  -38.508 -34.601 1.00 27.04  0  245 VAL   A CG1 1 
ATOM   1870 C  CG2 . VAL   A  1 230 ? 17.964  -37.638 -32.463 1.00 28.65  0  245 VAL   A CG2 1 
ATOM   1871 N  N   . THR   A  1 231 ? 18.893  -41.779 -34.508 1.00 24.45  0  246 THR   A N   1 
ATOM   1872 C  CA  . THR   A  1 231 ? 18.779  -42.827 -35.560 1.00 25.56  0  246 THR   A CA  1 
ATOM   1873 C  C   . THR   A  1 231 ? 17.957  -43.984 -35.059 1.00 26.59  0  246 THR   A C   1 
ATOM   1874 O  O   . THR   A  1 231 ? 17.240  -44.555 -35.864 1.00 31.50  0  246 THR   A O   1 
ATOM   1875 C  CB  . THR   A  1 231 ? 20.123  -43.342 -36.070 1.00 29.21  0  246 THR   A CB  1 
ATOM   1876 O  OG1 . THR   A  1 231 ? 20.921  -43.736 -34.949 1.00 31.63  0  246 THR   A OG1 1 
ATOM   1877 C  CG2 . THR   A  1 231 ? 20.796  -42.298 -36.935 1.00 29.93  0  246 THR   A CG2 1 
ATOM   1878 N  N   . TYR   A  1 232 ? 18.013  -44.288 -33.763 1.00 25.37  0  247 TYR   A N   1 
ATOM   1879 C  CA  . TYR   A  1 232 ? 17.314  -45.455 -33.176 1.00 26.67  0  247 TYR   A CA  1 
ATOM   1880 C  C   . TYR   A  1 232 ? 15.794  -45.315 -33.297 1.00 26.53  0  247 TYR   A C   1 
ATOM   1881 O  O   . TYR   A  1 232 ? 15.119  -46.320 -33.360 1.00 25.15  0  247 TYR   A O   1 
ATOM   1882 C  CB  . TYR   A  1 232 ? 17.730  -45.662 -31.717 1.00 29.50  0  247 TYR   A CB  1 
ATOM   1883 C  CG  . TYR   A  1 232 ? 17.456  -47.049 -31.201 1.00 33.44  0  247 TYR   A CG  1 
ATOM   1884 C  CD1 . TYR   A  1 232 ? 16.196  -47.386 -30.710 1.00 34.36  0  247 TYR   A CD1 1 
ATOM   1885 C  CD2 . TYR   A  1 232 ? 18.454  -48.023 -31.186 1.00 31.60  0  247 TYR   A CD2 1 
ATOM   1886 C  CE1 . TYR   A  1 232 ? 15.926  -48.651 -30.204 1.00 32.91  0  247 TYR   A CE1 1 
ATOM   1887 C  CE2 . TYR   A  1 232 ? 18.200  -49.286 -30.678 1.00 32.16  0  247 TYR   A CE2 1 
ATOM   1888 C  CZ  . TYR   A  1 232 ? 16.935  -49.602 -30.194 1.00 38.05  0  247 TYR   A CZ  1 
ATOM   1889 O  OH  . TYR   A  1 232 ? 16.679  -50.850 -29.684 1.00 40.26  0  247 TYR   A OH  1 
ATOM   1890 N  N   . TYR   A  1 233 ? 15.266  -44.093 -33.286 1.00 25.40  0  248 TYR   A N   1 
ATOM   1891 C  CA  . TYR   A  1 233 ? 13.817  -43.792 -33.142 1.00 26.35  0  248 TYR   A CA  1 
ATOM   1892 C  C   . TYR   A  1 233 ? 13.246  -43.155 -34.436 1.00 26.75  0  248 TYR   A C   1 
ATOM   1893 O  O   . TYR   A  1 233 ? 12.091  -42.695 -34.391 1.00 26.40  0  248 TYR   A O   1 
ATOM   1894 C  CB  . TYR   A  1 233 ? 13.629  -42.964 -31.861 1.00 26.46  0  248 TYR   A CB  1 
ATOM   1895 C  CG  . TYR   A  1 233 ? 13.961  -43.739 -30.603 1.00 25.03  0  248 TYR   A CG  1 
ATOM   1896 C  CD1 . TYR   A  1 233 ? 13.118  -44.760 -30.216 1.00 25.03  0  248 TYR   A CD1 1 
ATOM   1897 C  CD2 . TYR   A  1 233 ? 15.153  -43.583 -29.899 1.00 23.69  0  248 TYR   A CD2 1 
ATOM   1898 C  CE1 . TYR   A  1 233 ? 13.369  -45.534 -29.103 1.00 24.86  0  248 TYR   A CE1 1 
ATOM   1899 C  CE2 . TYR   A  1 233 ? 15.438  -44.362 -28.779 1.00 24.34  0  248 TYR   A CE2 1 
ATOM   1900 C  CZ  . TYR   A  1 233 ? 14.547  -45.357 -28.403 1.00 24.63  0  248 TYR   A CZ  1 
ATOM   1901 O  OH  . TYR   A  1 233 ? 14.730  -46.179 -27.347 1.00 24.44  0  248 TYR   A OH  1 
ATOM   1902 N  N   . LEU   A  1 234 ? 13.967  -43.191 -35.570 1.00 28.63  0  249 LEU   A N   1 
ATOM   1903 C  CA  . LEU   A  1 234 ? 13.506  -42.608 -36.871 1.00 32.82  0  249 LEU   A CA  1 
ATOM   1904 C  C   . LEU   A  1 234 ? 12.152  -43.196 -37.269 1.00 31.08  0  249 LEU   A C   1 
ATOM   1905 O  O   . LEU   A  1 234 ? 11.265  -42.401 -37.616 1.00 28.40  0  249 LEU   A O   1 
ATOM   1906 C  CB  . LEU   A  1 234 ? 14.527  -42.813 -38.002 1.00 33.07  0  249 LEU   A CB  1 
ATOM   1907 C  CG  . LEU   A  1 234 ? 15.783  -41.953 -37.921 1.00 35.14  0  249 LEU   A CG  1 
ATOM   1908 C  CD1 . LEU   A  1 234 ? 16.861  -42.463 -38.866 1.00 34.74  0  249 LEU   A CD1 1 
ATOM   1909 C  CD2 . LEU   A  1 234 ? 15.475  -40.489 -38.199 1.00 35.01  0  249 LEU   A CD2 1 
ATOM   1910 N  N   . ASP   A  1 235 ? 11.979  -44.518 -37.196 1.00 35.18  0  250 ASP   A N   1 
ATOM   1911 C  CA  . ASP   A  1 235 ? 10.705  -45.166 -37.622 1.00 35.17  0  250 ASP   A CA  1 
ATOM   1912 C  C   . ASP   A  1 235 ? 9.556   -44.670 -36.758 1.00 34.20  0  250 ASP   A C   1 
ATOM   1913 O  O   . ASP   A  1 235 ? 8.478   -44.387 -37.324 1.00 32.21  0  250 ASP   A O   1 
ATOM   1914 C  CB  . ASP   A  1 235 ? 10.736  -46.698 -37.558 1.00 41.59  0  250 ASP   A CB  1 
ATOM   1915 C  CG  . ASP   A  1 235 ? 11.770  -47.314 -38.482 1.00 47.04  0  250 ASP   A CG  1 
ATOM   1916 O  OD1 . ASP   A  1 235 ? 12.196  -46.606 -39.414 1.00 46.05  0  250 ASP   A OD1 1 
ATOM   1917 O  OD2 . ASP   A  1 235 ? 12.134  -48.513 -38.267 1.00 53.87  -1 250 ASP   A OD2 1 
ATOM   1918 N  N   . TRP   A  1 236 ? 9.772   -44.556 -35.446 1.00 30.53  0  251 TRP   A N   1 
ATOM   1919 C  CA  . TRP   A  1 236 ? 8.752   -44.001 -34.522 1.00 28.15  0  251 TRP   A CA  1 
ATOM   1920 C  C   . TRP   A  1 236 ? 8.452   -42.524 -34.871 1.00 25.19  0  251 TRP   A C   1 
ATOM   1921 O  O   . TRP   A  1 236 ? 7.282   -42.164 -34.985 1.00 24.46  0  251 TRP   A O   1 
ATOM   1922 C  CB  . TRP   A  1 236 ? 9.216   -44.180 -33.073 1.00 27.02  0  251 TRP   A CB  1 
ATOM   1923 C  CG  . TRP   A  1 236 ? 8.241   -43.617 -32.090 1.00 25.99  0  251 TRP   A CG  1 
ATOM   1924 C  CD1 . TRP   A  1 236 ? 7.105   -44.201 -31.629 1.00 25.46  0  251 TRP   A CD1 1 
ATOM   1925 C  CD2 . TRP   A  1 236 ? 8.311   -42.322 -31.471 1.00 24.96  0  251 TRP   A CD2 1 
ATOM   1926 N  NE1 . TRP   A  1 236 ? 6.458   -43.358 -30.760 1.00 26.23  0  251 TRP   A NE1 1 
ATOM   1927 C  CE2 . TRP   A  1 236 ? 7.187   -42.207 -30.626 1.00 27.11  0  251 TRP   A CE2 1 
ATOM   1928 C  CE3 . TRP   A  1 236 ? 9.212   -41.258 -31.556 1.00 26.65  0  251 TRP   A CE3 1 
ATOM   1929 C  CZ2 . TRP   A  1 236 ? 6.957   -41.080 -29.835 1.00 24.64  0  251 TRP   A CZ2 1 
ATOM   1930 C  CZ3 . TRP   A  1 236 ? 8.994   -40.141 -30.769 1.00 28.03  0  251 TRP   A CZ3 1 
ATOM   1931 C  CH2 . TRP   A  1 236 ? 7.856   -40.043 -29.958 1.00 27.97  0  251 TRP   A CH2 1 
ATOM   1932 N  N   . ILE   A  1 237 ? 9.475   -41.691 -35.054 1.00 28.44  0  252 ILE   A N   1 
ATOM   1933 C  CA  . ILE   A  1 237 ? 9.280   -40.265 -35.449 1.00 28.30  0  252 ILE   A CA  1 
ATOM   1934 C  C   . ILE   A  1 237 ? 8.424   -40.231 -36.738 1.00 32.38  0  252 ILE   A C   1 
ATOM   1935 O  O   . ILE   A  1 237 ? 7.359   -39.557 -36.750 1.00 31.08  0  252 ILE   A O   1 
ATOM   1936 C  CB  . ILE   A  1 237 ? 10.629  -39.517 -35.593 1.00 29.33  0  252 ILE   A CB  1 
ATOM   1937 C  CG1 . ILE   A  1 237 ? 11.401  -39.387 -34.270 1.00 24.99  0  252 ILE   A CG1 1 
ATOM   1938 C  CG2 . ILE   A  1 237 ? 10.374  -38.136 -36.192 1.00 31.64  0  252 ILE   A CG2 1 
ATOM   1939 C  CD1 . ILE   A  1 237 ? 12.837  -38.867 -34.398 1.00 26.19  0  252 ILE   A CD1 1 
ATOM   1940 N  N   . HIS   A  1 238 ? 8.820   -40.994 -37.760 1.00 32.36  0  253 HIS   A N   1 
ATOM   1941 C  CA  . HIS   A  1 238 ? 8.186   -40.994 -39.106 1.00 31.47  0  253 HIS   A CA  1 
ATOM   1942 C  C   . HIS   A  1 238 ? 6.777   -41.589 -39.069 1.00 32.71  0  253 HIS   A C   1 
ATOM   1943 O  O   . HIS   A  1 238 ? 6.034   -41.347 -40.011 1.00 35.78  0  253 HIS   A O   1 
ATOM   1944 C  CB  . HIS   A  1 238 ? 9.134   -41.612 -40.150 1.00 32.88  0  253 HIS   A CB  1 
ATOM   1945 C  CG  . HIS   A  1 238 ? 10.334  -40.749 -40.432 1.00 37.06  0  253 HIS   A CG  1 
ATOM   1946 N  ND1 . HIS   A  1 238 ? 11.567  -41.274 -40.775 1.00 43.42  0  253 HIS   A ND1 1 
ATOM   1947 C  CD2 . HIS   A  1 238 ? 10.499  -39.404 -40.415 1.00 45.92  0  253 HIS   A CD2 1 
ATOM   1948 C  CE1 . HIS   A  1 238 ? 12.433  -40.294 -40.965 1.00 43.49  0  253 HIS   A CE1 1 
ATOM   1949 N  NE2 . HIS   A  1 238 ? 11.813  -39.142 -40.713 1.00 43.39  0  253 HIS   A NE2 1 
ATOM   1950 N  N   . HIS   A  1 239 ? 6.361   -42.267 -38.016 1.00 30.86  0  254 HIS   A N   1 
ATOM   1951 C  CA  . HIS   A  1 239 ? 4.926   -42.575 -37.811 1.00 30.56  0  254 HIS   A CA  1 
ATOM   1952 C  C   . HIS   A  1 239 ? 4.082   -41.295 -37.668 1.00 34.28  0  254 HIS   A C   1 
ATOM   1953 O  O   . HIS   A  1 239 ? 2.883   -41.337 -37.998 1.00 33.83  0  254 HIS   A O   1 
ATOM   1954 C  CB  . HIS   A  1 239 ? 4.759   -43.480 -36.612 1.00 36.53  0  254 HIS   A CB  1 
ATOM   1955 C  CG  . HIS   A  1 239 ? 3.372   -43.982 -36.430 1.00 43.48  0  254 HIS   A CG  1 
ATOM   1956 N  ND1 . HIS   A  1 239 ? 2.995   -45.246 -36.869 1.00 51.63  0  254 HIS   A ND1 1 
ATOM   1957 C  CD2 . HIS   A  1 239 ? 2.300   -43.444 -35.802 1.00 50.91  0  254 HIS   A CD2 1 
ATOM   1958 C  CE1 . HIS   A  1 239 ? 1.730   -45.455 -36.534 1.00 57.21  0  254 HIS   A CE1 1 
ATOM   1959 N  NE2 . HIS   A  1 239 ? 1.274   -44.353 -35.885 1.00 58.76  0  254 HIS   A NE2 1 
ATOM   1960 N  N   . TYR   A  1 240 ? 4.635   -40.218 -37.116 1.00 33.40  0  255 TYR   A N   1 
ATOM   1961 C  CA  . TYR   A  1 240 ? 3.858   -39.011 -36.731 1.00 32.39  0  255 TYR   A CA  1 
ATOM   1962 C  C   . TYR   A  1 240 ? 4.185   -37.832 -37.640 1.00 31.03  0  255 TYR   A C   1 
ATOM   1963 O  O   . TYR   A  1 240 ? 3.284   -37.044 -37.869 1.00 32.86  0  255 TYR   A O   1 
ATOM   1964 C  CB  . TYR   A  1 240 ? 4.090   -38.669 -35.262 1.00 29.51  0  255 TYR   A CB  1 
ATOM   1965 C  CG  . TYR   A  1 240 ? 3.590   -39.736 -34.325 1.00 33.06  0  255 TYR   A CG  1 
ATOM   1966 C  CD1 . TYR   A  1 240 ? 2.240   -39.854 -34.023 1.00 33.24  0  255 TYR   A CD1 1 
ATOM   1967 C  CD2 . TYR   A  1 240 ? 4.467   -40.647 -33.762 1.00 33.30  0  255 TYR   A CD2 1 
ATOM   1968 C  CE1 . TYR   A  1 240 ? 1.779   -40.852 -33.184 1.00 32.69  0  255 TYR   A CE1 1 
ATOM   1969 C  CE2 . TYR   A  1 240 ? 4.019   -41.639 -32.908 1.00 31.81  0  255 TYR   A CE2 1 
ATOM   1970 C  CZ  . TYR   A  1 240 ? 2.679   -41.744 -32.621 1.00 32.42  0  255 TYR   A CZ  1 
ATOM   1971 O  OH  . TYR   A  1 240 ? 2.275   -42.727 -31.764 1.00 34.91  0  255 TYR   A OH  1 
ATOM   1972 N  N   . VAL   A  1 241 ? 5.441   -37.677 -38.051 1.00 32.02  0  256 VAL   A N   1 
ATOM   1973 C  CA  . VAL   A  1 241 ? 5.963   -36.430 -38.672 1.00 34.96  0  256 VAL   A CA  1 
ATOM   1974 C  C   . VAL   A  1 241 ? 6.154   -36.715 -40.159 1.00 35.06  0  256 VAL   A C   1 
ATOM   1975 O  O   . VAL   A  1 241 ? 6.972   -37.561 -40.512 1.00 37.34  0  256 VAL   A O   1 
ATOM   1976 C  CB  . VAL   A  1 241 ? 7.288   -35.967 -38.022 1.00 35.42  0  256 VAL   A CB  1 
ATOM   1977 C  CG1 . VAL   A  1 241 ? 7.830   -34.693 -38.661 1.00 34.27  0  256 VAL   A CG1 1 
ATOM   1978 C  CG2 . VAL   A  1 241 ? 7.159   -35.783 -36.514 1.00 34.75  0  256 VAL   A CG2 1 
ATOM   1979 N  N   . PRO   A  1 242 ? 5.441   -36.004 -41.058 1.00 38.72  0  257 PRO   A N   1 
ATOM   1980 C  CA  . PRO   A  1 242 ? 5.651   -36.147 -42.508 1.00 40.20  0  257 PRO   A CA  1 
ATOM   1981 C  C   . PRO   A  1 242 ? 7.119   -35.973 -42.931 1.00 45.05  0  257 PRO   A C   1 
ATOM   1982 O  O   . PRO   A  1 242 ? 7.803   -35.142 -42.331 1.00 42.72  0  257 PRO   A O   1 
ATOM   1983 C  CB  . PRO   A  1 242 ? 4.825   -34.996 -43.097 1.00 38.82  0  257 PRO   A CB  1 
ATOM   1984 C  CG  . PRO   A  1 242 ? 3.713   -34.800 -42.071 1.00 41.08  0  257 PRO   A CG  1 
ATOM   1985 C  CD  . PRO   A  1 242 ? 4.413   -34.996 -40.731 1.00 39.22  0  257 PRO   A CD  1 
ATOM   1986 N  N   . LYS   A  1 243 ? 7.569   -36.748 -43.930 1.00 55.62  0  258 LYS   A N   1 
ATOM   1987 C  CA  . LYS   A  1 243 ? 8.854   -36.535 -44.676 1.00 65.40  0  258 LYS   A CA  1 
ATOM   1988 C  C   . LYS   A  1 243 ? 8.594   -35.668 -45.915 1.00 61.39  0  258 LYS   A C   1 
ATOM   1989 O  O   . LYS   A  1 243 ? 8.313   -34.481 -45.795 1.00 63.09  0  258 LYS   A O   1 
ATOM   1990 C  CB  . LYS   A  1 243 ? 9.495   -37.851 -45.141 1.00 67.13  0  258 LYS   A CB  1 
ATOM   1991 C  CG  . LYS   A  1 243 ? 10.014  -38.768 -44.039 1.00 67.61  0  258 LYS   A CG  1 
ATOM   1992 C  CD  . LYS   A  1 243 ? 11.080  -39.720 -44.475 0.00 72.21  0  258 LYS   A CD  1 
ATOM   1993 C  CE  . LYS   A  1 243 ? 12.417  -39.018 -44.580 0.00 71.96  0  258 LYS   A CE  1 
ATOM   1994 N  NZ  . LYS   A  1 243 ? 13.533  -39.985 -44.702 0.00 71.75  1  258 LYS   A NZ  1 
ATOM   1995 N  N   . ILE   B  1 1   ? 7.424   -3.467  -7.033  1.00 25.12  0  16  ILE   B N   1 
ATOM   1996 C  CA  . ILE   B  1 1   ? 6.172   -2.642  -7.058  1.00 24.54  0  16  ILE   B CA  1 
ATOM   1997 C  C   . ILE   B  1 1   ? 4.928   -3.547  -6.950  1.00 28.44  0  16  ILE   B C   1 
ATOM   1998 O  O   . ILE   B  1 1   ? 4.804   -4.509  -7.765  1.00 30.92  0  16  ILE   B O   1 
ATOM   1999 C  CB  . ILE   B  1 1   ? 6.148   -1.747  -8.320  1.00 26.02  0  16  ILE   B CB  1 
ATOM   2000 C  CG1 . ILE   B  1 1   ? 7.291   -0.729  -8.314  1.00 24.04  0  16  ILE   B CG1 1 
ATOM   2001 C  CG2 . ILE   B  1 1   ? 4.787   -1.069  -8.509  1.00 30.18  0  16  ILE   B CG2 1 
ATOM   2002 C  CD1 . ILE   B  1 1   ? 7.140   0.439   -7.328  1.00 23.89  0  16  ILE   B CD1 1 
ATOM   2003 N  N   . VAL   B  1 2   ? 4.041   -3.273  -5.973  1.00 25.86  0  17  VAL   B N   1 
ATOM   2004 C  CA  . VAL   B  1 2   ? 2.805   -4.070  -5.753  1.00 28.77  0  17  VAL   B CA  1 
ATOM   2005 C  C   . VAL   B  1 2   ? 1.639   -3.324  -6.398  1.00 30.01  0  17  VAL   B C   1 
ATOM   2006 O  O   . VAL   B  1 2   ? 1.458   -2.144  -6.064  1.00 27.60  0  17  VAL   B O   1 
ATOM   2007 C  CB  . VAL   B  1 2   ? 2.511   -4.344  -4.261  1.00 27.54  0  17  VAL   B CB  1 
ATOM   2008 C  CG1 . VAL   B  1 2   ? 1.303   -5.217  -4.103  1.00 27.70  0  17  VAL   B CG1 1 
ATOM   2009 C  CG2 . VAL   B  1 2   ? 3.702   -4.971  -3.568  1.00 30.67  0  17  VAL   B CG2 1 
ATOM   2010 N  N   . GLY   B  1 3   ? 0.812   -4.052  -7.165  1.00 30.74  0  18  GLY   B N   1 
ATOM   2011 C  CA  . GLY   B  1 3   ? -0.405  -3.512  -7.804  1.00 32.11  0  18  GLY   B CA  1 
ATOM   2012 C  C   . GLY   B  1 3   ? -0.081  -2.549  -8.921  1.00 35.46  0  18  GLY   B C   1 
ATOM   2013 O  O   . GLY   B  1 3   ? -0.947  -1.738  -9.263  1.00 38.55  0  18  GLY   B O   1 
ATOM   2014 N  N   . GLY   B  1 4   ? 1.118   -2.624  -9.475  1.00 30.77  0  19  GLY   B N   1 
ATOM   2015 C  CA  . GLY   B  1 4   ? 1.520   -1.666  -10.507 1.00 37.83  0  19  GLY   B CA  1 
ATOM   2016 C  C   . GLY   B  1 4   ? 1.173   -2.161  -11.904 1.00 41.86  0  19  GLY   B C   1 
ATOM   2017 O  O   . GLY   B  1 4   ? 0.464   -3.178  -12.054 1.00 42.49  0  19  GLY   B O   1 
ATOM   2018 N  N   . GLN   B  1 5   ? 1.728   -1.468  -12.892 1.00 33.36  0  20  GLN   B N   1 
ATOM   2019 C  CA  . GLN   B  1 5   ? 1.823   -1.903  -14.295 1.00 36.22  0  20  GLN   B CA  1 
ATOM   2020 C  C   . GLN   B  1 5   ? 3.213   -1.561  -14.809 1.00 34.10  0  20  GLN   B C   1 
ATOM   2021 O  O   . GLN   B  1 5   ? 3.902   -0.672  -14.213 1.00 27.56  0  20  GLN   B O   1 
ATOM   2022 C  CB  . GLN   B  1 5   ? 0.807   -1.156  -15.147 1.00 37.67  0  20  GLN   B CB  1 
ATOM   2023 C  CG  . GLN   B  1 5   ? -0.557  -1.134  -14.499 1.00 47.45  0  20  GLN   B CG  1 
ATOM   2024 C  CD  . GLN   B  1 5   ? -1.510  -0.240  -15.242 1.00 51.63  0  20  GLN   B CD  1 
ATOM   2025 O  OE1 . GLN   B  1 5   ? -1.163  0.879   -15.630 1.00 64.09  0  20  GLN   B OE1 1 
ATOM   2026 N  NE2 . GLN   B  1 5   ? -2.736  -0.717  -15.384 1.00 48.75  0  20  GLN   B NE2 1 
ATOM   2027 N  N   . GLU   B  1 6   ? 3.564   -2.177  -15.927 1.00 29.14  0  21  GLU   B N   1 
ATOM   2028 C  CA  . GLU   B  1 6   ? 4.808   -1.874  -16.673 1.00 31.20  0  21  GLU   B CA  1 
ATOM   2029 C  C   . GLU   B  1 6   ? 4.749   -0.402  -17.097 1.00 29.75  0  21  GLU   B C   1 
ATOM   2030 O  O   . GLU   B  1 6   ? 3.668   0.053   -17.491 1.00 29.40  0  21  GLU   B O   1 
ATOM   2031 C  CB  . GLU   B  1 6   ? 4.939   -2.800  -17.889 1.00 31.25  0  21  GLU   B CB  1 
ATOM   2032 C  CG  . GLU   B  1 6   ? 6.113   -2.437  -18.779 1.00 34.28  0  21  GLU   B CG  1 
ATOM   2033 C  CD  . GLU   B  1 6   ? 6.572   -3.473  -19.810 1.00 36.46  0  21  GLU   B CD  1 
ATOM   2034 O  OE1 . GLU   B  1 6   ? 7.519   -3.152  -20.579 1.00 32.47  0  21  GLU   B OE1 1 
ATOM   2035 O  OE2 . GLU   B  1 6   ? 6.013   -4.610  -19.816 1.00 35.40  -1 21  GLU   B OE2 1 
ATOM   2036 N  N   . ALA   B  1 7   ? 5.858   0.309   -16.996 1.00 28.37  0  22  ALA   B N   1 
ATOM   2037 C  CA  . ALA   B  1 7   ? 5.965   1.748   -17.309 1.00 31.41  0  22  ALA   B CA  1 
ATOM   2038 C  C   . ALA   B  1 7   ? 6.040   1.901   -18.823 1.00 36.17  0  22  ALA   B C   1 
ATOM   2039 O  O   . ALA   B  1 7   ? 6.762   1.132   -19.458 1.00 31.38  0  22  ALA   B O   1 
ATOM   2040 C  CB  . ALA   B  1 7   ? 7.239   2.293   -16.715 1.00 30.69  0  22  ALA   B CB  1 
ATOM   2041 N  N   . PRO   B  1 8   ? 5.374   2.916   -19.424 1.00 35.17  0  23  PRO   B N   1 
ATOM   2042 C  CA  . PRO   B  1 8   ? 5.685   3.342   -20.783 1.00 35.98  0  23  PRO   B CA  1 
ATOM   2043 C  C   . PRO   B  1 8   ? 7.166   3.719   -20.868 1.00 35.70  0  23  PRO   B C   1 
ATOM   2044 O  O   . PRO   B  1 8   ? 7.707   4.248   -19.887 1.00 35.65  0  23  PRO   B O   1 
ATOM   2045 C  CB  . PRO   B  1 8   ? 4.806   4.584   -21.030 1.00 36.08  0  23  PRO   B CB  1 
ATOM   2046 C  CG  . PRO   B  1 8   ? 3.698   4.476   -20.009 1.00 35.35  0  23  PRO   B CG  1 
ATOM   2047 C  CD  . PRO   B  1 8   ? 4.297   3.725   -18.832 1.00 38.54  0  23  PRO   B CD  1 
ATOM   2048 N  N   . ARG   B  1 9   ? 7.774   3.466   -22.026 1.00 33.15  0  24  ARG   B N   1 
ATOM   2049 C  CA  . ARG   B  1 9   ? 9.214   3.730   -22.314 1.00 34.18  0  24  ARG   B CA  1 
ATOM   2050 C  C   . ARG   B  1 9   ? 9.566   5.212   -22.105 1.00 32.63  0  24  ARG   B C   1 
ATOM   2051 O  O   . ARG   B  1 9   ? 10.725  5.484   -21.763 1.00 30.89  0  24  ARG   B O   1 
ATOM   2052 C  CB  . ARG   B  1 9   ? 9.566   3.292   -23.740 1.00 41.29  0  24  ARG   B CB  1 
ATOM   2053 C  CG  . ARG   B  1 9   ? 9.211   1.840   -24.083 1.00 48.78  0  24  ARG   B CG  1 
ATOM   2054 C  CD  . ARG   B  1 9   ? 9.719   1.334   -25.432 1.00 53.07  0  24  ARG   B CD  1 
ATOM   2055 N  NE  . ARG   B  1 9   ? 11.159  1.174   -25.322 1.00 55.59  0  24  ARG   B NE  1 
ATOM   2056 C  CZ  . ARG   B  1 9   ? 11.798  0.043   -25.007 1.00 52.62  0  24  ARG   B CZ  1 
ATOM   2057 N  NH1 . ARG   B  1 9   ? 11.160  -1.116  -24.877 1.00 51.52  1  24  ARG   B NH1 1 
ATOM   2058 N  NH2 . ARG   B  1 9   ? 13.114  0.072   -24.872 1.00 50.40  0  24  ARG   B NH2 1 
ATOM   2059 N  N   . SER   B  1 10  ? 8.627   6.135   -22.324 1.00 34.61  0  25  SER   B N   1 
ATOM   2060 C  CA  . SER   B  1 10  ? 8.848   7.612   -22.230 1.00 39.23  0  25  SER   B CA  1 
ATOM   2061 C  C   . SER   B  1 10  ? 8.786   8.101   -20.777 1.00 39.45  0  25  SER   B C   1 
ATOM   2062 O  O   . SER   B  1 10  ? 9.225   9.225   -20.565 1.00 48.46  0  25  SER   B O   1 
ATOM   2063 C  CB  . SER   B  1 10  ? 7.847   8.400   -23.051 1.00 38.70  0  25  SER   B CB  1 
ATOM   2064 O  OG  . SER   B  1 10  ? 6.507   8.076   -22.631 1.00 39.91  0  25  SER   B OG  1 
ATOM   2065 N  N   . LYS   B  1 11  ? 8.332   7.290   -19.808 1.00 38.33  0  26  LYS   B N   1 
ATOM   2066 C  CA  . LYS   B  1 11  ? 8.095   7.767   -18.411 1.00 36.34  0  26  LYS   B CA  1 
ATOM   2067 C  C   . LYS   B  1 11  ? 9.301   7.412   -17.535 1.00 35.68  0  26  LYS   B C   1 
ATOM   2068 O  O   . LYS   B  1 11  ? 9.992   6.393   -17.815 1.00 32.23  0  26  LYS   B O   1 
ATOM   2069 C  CB  . LYS   B  1 11  ? 6.784   7.204   -17.862 1.00 40.19  0  26  LYS   B CB  1 
ATOM   2070 C  CG  . LYS   B  1 11  ? 5.522   7.542   -18.665 1.00 43.17  0  26  LYS   B CG  1 
ATOM   2071 C  CD  . LYS   B  1 11  ? 5.061   9.012   -18.620 1.00 55.04  0  26  LYS   B CD  1 
ATOM   2072 C  CE  . LYS   B  1 11  ? 3.881   9.362   -19.521 1.00 55.46  0  26  LYS   B CE  1 
ATOM   2073 N  NZ  . LYS   B  1 11  ? 3.460   10.748  -19.431 0.00 54.25  1  26  LYS   B NZ  1 
ATOM   2074 N  N   . TRP   B  1 12  ? 9.556   8.234   -16.524 1.00 28.91  0  27  TRP   B N   1 
ATOM   2075 C  CA  . TRP   B  1 12  ? 10.548  8.011   -15.446 1.00 27.68  0  27  TRP   B CA  1 
ATOM   2076 C  C   . TRP   B  1 12  ? 11.963  7.966   -15.994 1.00 28.35  0  27  TRP   B C   1 
ATOM   2077 O  O   . TRP   B  1 12  ? 12.694  7.004   -15.737 1.00 29.55  0  27  TRP   B O   1 
ATOM   2078 C  CB  . TRP   B  1 12  ? 10.206  6.739   -14.674 1.00 27.92  0  27  TRP   B CB  1 
ATOM   2079 C  CG  . TRP   B  1 12  ? 8.748   6.468   -14.571 1.00 26.90  0  27  TRP   B CG  1 
ATOM   2080 C  CD1 . TRP   B  1 12  ? 8.120   5.322   -14.950 1.00 27.74  0  27  TRP   B CD1 1 
ATOM   2081 C  CD2 . TRP   B  1 12  ? 7.728   7.342   -14.061 1.00 27.04  0  27  TRP   B CD2 1 
ATOM   2082 N  NE1 . TRP   B  1 12  ? 6.784   5.419   -14.722 1.00 27.08  0  27  TRP   B NE1 1 
ATOM   2083 C  CE2 . TRP   B  1 12  ? 6.512   6.634   -14.143 1.00 25.97  0  27  TRP   B CE2 1 
ATOM   2084 C  CE3 . TRP   B  1 12  ? 7.727   8.643   -13.534 1.00 27.15  0  27  TRP   B CE3 1 
ATOM   2085 C  CZ2 . TRP   B  1 12  ? 5.301   7.189   -13.730 1.00 27.72  0  27  TRP   B CZ2 1 
ATOM   2086 C  CZ3 . TRP   B  1 12  ? 6.530   9.188   -13.117 1.00 25.70  0  27  TRP   B CZ3 1 
ATOM   2087 C  CH2 . TRP   B  1 12  ? 5.336   8.464   -13.208 1.00 27.91  0  27  TRP   B CH2 1 
ATOM   2088 N  N   . PRO   B  1 13  ? 12.409  8.998   -16.751 1.00 29.26  0  28  PRO   B N   1 
ATOM   2089 C  CA  . PRO   B  1 13  ? 13.757  9.009   -17.332 1.00 28.99  0  28  PRO   B CA  1 
ATOM   2090 C  C   . PRO   B  1 13  ? 14.898  9.117   -16.310 1.00 29.17  0  28  PRO   B C   1 
ATOM   2091 O  O   . PRO   B  1 13  ? 16.045  8.950   -16.666 1.00 31.31  0  28  PRO   B O   1 
ATOM   2092 C  CB  . PRO   B  1 13  ? 13.752  10.266  -18.242 1.00 31.67  0  28  PRO   B CB  1 
ATOM   2093 C  CG  . PRO   B  1 13  ? 12.686  11.171  -17.649 1.00 32.17  0  28  PRO   B CG  1 
ATOM   2094 C  CD  . PRO   B  1 13  ? 11.649  10.221  -17.076 1.00 31.14  0  28  PRO   B CD  1 
ATOM   2095 N  N   . TRP   B  1 14  ? 14.558  9.385   -15.052 1.00 29.72  0  29  TRP   B N   1 
ATOM   2096 C  CA  . TRP   B  1 14  ? 15.532  9.521   -13.934 1.00 29.46  0  29  TRP   B CA  1 
ATOM   2097 C  C   . TRP   B  1 14  ? 15.730  8.184   -13.192 1.00 29.71  0  29  TRP   B C   1 
ATOM   2098 O  O   . TRP   B  1 14  ? 16.634  8.125   -12.368 1.00 29.47  0  29  TRP   B O   1 
ATOM   2099 C  CB  . TRP   B  1 14  ? 15.062  10.625  -12.968 1.00 29.01  0  29  TRP   B CB  1 
ATOM   2100 C  CG  . TRP   B  1 14  ? 13.622  10.480  -12.647 1.00 26.03  0  29  TRP   B CG  1 
ATOM   2101 C  CD1 . TRP   B  1 14  ? 13.060  9.558   -11.833 1.00 29.66  0  29  TRP   B CD1 1 
ATOM   2102 C  CD2 . TRP   B  1 14  ? 12.549  11.288  -13.155 1.00 28.09  0  29  TRP   B CD2 1 
ATOM   2103 N  NE1 . TRP   B  1 14  ? 11.704  9.713   -11.822 1.00 30.23  0  29  TRP   B NE1 1 
ATOM   2104 C  CE2 . TRP   B  1 14  ? 11.357  10.755  -12.640 1.00 26.09  0  29  TRP   B CE2 1 
ATOM   2105 C  CE3 . TRP   B  1 14  ? 12.489  12.379  -14.028 1.00 26.73  0  29  TRP   B CE3 1 
ATOM   2106 C  CZ2 . TRP   B  1 14  ? 10.109  11.284  -12.942 1.00 29.21  0  29  TRP   B CZ2 1 
ATOM   2107 C  CZ3 . TRP   B  1 14  ? 11.249  12.877  -14.353 1.00 29.21  0  29  TRP   B CZ3 1 
ATOM   2108 C  CH2 . TRP   B  1 14  ? 10.081  12.346  -13.818 1.00 27.40  0  29  TRP   B CH2 1 
ATOM   2109 N  N   . GLN   B  1 15  ? 14.916  7.158   -13.430 1.00 29.93  0  30  GLN   B N   1 
ATOM   2110 C  CA  . GLN   B  1 15  ? 15.001  5.875   -12.670 1.00 29.52  0  30  GLN   B CA  1 
ATOM   2111 C  C   . GLN   B  1 15  ? 16.372  5.257   -12.922 1.00 28.46  0  30  GLN   B C   1 
ATOM   2112 O  O   . GLN   B  1 15  ? 16.785  5.227   -14.098 1.00 30.19  0  30  GLN   B O   1 
ATOM   2113 C  CB  . GLN   B  1 15  ? 13.889  4.902   -13.050 1.00 28.88  0  30  GLN   B CB  1 
ATOM   2114 C  CG  . GLN   B  1 15  ? 13.958  3.574   -12.307 1.00 29.49  0  30  GLN   B CG  1 
ATOM   2115 C  CD  . GLN   B  1 15  ? 13.487  3.636   -10.872 1.00 27.94  0  30  GLN   B CD  1 
ATOM   2116 O  OE1 . GLN   B  1 15  ? 12.442  4.193   -10.550 1.00 31.73  0  30  GLN   B OE1 1 
ATOM   2117 N  NE2 . GLN   B  1 15  ? 14.256  3.032   -9.985  1.00 31.56  0  30  GLN   B NE2 1 
ATOM   2118 N  N   . VAL   B  1 16  ? 17.059  4.819   -11.864 1.00 25.14  0  31  VAL   B N   1 
ATOM   2119 C  CA  . VAL   B  1 16  ? 18.316  4.035   -12.007 1.00 27.58  0  31  VAL   B CA  1 
ATOM   2120 C  C   . VAL   B  1 16  ? 18.228  2.730   -11.212 1.00 26.17  0  31  VAL   B C   1 
ATOM   2121 O  O   . VAL   B  1 16  ? 17.424  2.624   -10.271 1.00 24.59  0  31  VAL   B O   1 
ATOM   2122 C  CB  . VAL   B  1 16  ? 19.598  4.838   -11.723 1.00 31.77  0  31  VAL   B CB  1 
ATOM   2123 C  CG1 . VAL   B  1 16  ? 19.486  6.284   -12.200 1.00 32.95  0  31  VAL   B CG1 1 
ATOM   2124 C  CG2 . VAL   B  1 16  ? 20.044  4.777   -10.291 1.00 33.94  0  31  VAL   B CG2 1 
ATOM   2125 N  N   . SER   B  1 17  ? 19.002  1.743   -11.656 1.00 26.27  0  32  SER   B N   1 
ATOM   2126 C  CA  . SER   B  1 17  ? 19.201  0.429   -11.010 1.00 24.85  0  32  SER   B CA  1 
ATOM   2127 C  C   . SER   B  1 17  ? 20.606  0.376   -10.416 1.00 25.49  0  32  SER   B C   1 
ATOM   2128 O  O   . SER   B  1 17  ? 21.553  0.674   -11.132 1.00 25.58  0  32  SER   B O   1 
ATOM   2129 C  CB  . SER   B  1 17  ? 18.978  -0.676  -12.020 1.00 28.11  0  32  SER   B CB  1 
ATOM   2130 O  OG  . SER   B  1 17  ? 19.338  -1.933  -11.477 1.00 23.35  0  32  SER   B OG  1 
ATOM   2131 N  N   . LEU   B  1 18  ? 20.724  0.018   -9.136  1.00 27.59  0  33  LEU   B N   1 
ATOM   2132 C  CA  . LEU   B  1 18  ? 22.037  -0.209  -8.464  1.00 27.77  0  33  LEU   B CA  1 
ATOM   2133 C  C   . LEU   B  1 18  ? 22.371  -1.692  -8.590  1.00 25.05  0  33  LEU   B C   1 
ATOM   2134 O  O   . LEU   B  1 18  ? 21.474  -2.497  -8.334  1.00 25.12  0  33  LEU   B O   1 
ATOM   2135 C  CB  . LEU   B  1 18  ? 22.008  0.204   -6.981  1.00 26.39  0  33  LEU   B CB  1 
ATOM   2136 C  CG  . LEU   B  1 18  ? 21.562  1.632   -6.658  1.00 32.00  0  33  LEU   B CG  1 
ATOM   2137 C  CD1 . LEU   B  1 18  ? 22.034  2.066   -5.254  1.00 32.50  0  33  LEU   B CD1 1 
ATOM   2138 C  CD2 . LEU   B  1 18  ? 22.073  2.617   -7.689  1.00 32.54  0  33  LEU   B CD2 1 
ATOM   2139 N  N   . ARG   B  1 19  ? 23.631  -1.997  -8.891  1.00 25.37  0  34  ARG   B N   1 
ATOM   2140 C  CA  . ARG   B  1 19  ? 24.110  -3.360  -9.216  1.00 27.03  0  34  ARG   B CA  1 
ATOM   2141 C  C   . ARG   B  1 19  ? 25.313  -3.725  -8.355  1.00 28.43  0  34  ARG   B C   1 
ATOM   2142 O  O   . ARG   B  1 19  ? 26.194  -2.874  -8.175  1.00 26.86  0  34  ARG   B O   1 
ATOM   2143 C  CB  . ARG   B  1 19  ? 24.520  -3.499  -10.681 1.00 27.85  0  34  ARG   B CB  1 
ATOM   2144 C  CG  . ARG   B  1 19  ? 23.448  -3.084  -11.668 1.00 26.64  0  34  ARG   B CG  1 
ATOM   2145 C  CD  . ARG   B  1 19  ? 22.168  -3.915  -11.554 1.00 25.57  0  34  ARG   B CD  1 
ATOM   2146 N  NE  . ARG   B  1 19  ? 21.295  -3.613  -12.676 1.00 27.93  0  34  ARG   B NE  1 
ATOM   2147 C  CZ  . ARG   B  1 19  ? 21.518  -4.022  -13.937 1.00 28.48  0  34  ARG   B CZ  1 
ATOM   2148 N  NH1 . ARG   B  1 19  ? 22.551  -4.814  -14.213 1.00 21.97  1  34  ARG   B NH1 1 
ATOM   2149 N  NH2 . ARG   B  1 19  ? 20.661  -3.667  -14.893 1.00 26.71  0  34  ARG   B NH2 1 
ATOM   2150 N  N   . VAL   B  1 20  ? 25.307  -4.961  -7.832  1.00 28.70  0  35  VAL   B N   1 
ATOM   2151 C  CA  . VAL   B  1 20  ? 26.382  -5.526  -6.977  1.00 28.56  0  35  VAL   B CA  1 
ATOM   2152 C  C   . VAL   B  1 20  ? 27.088  -6.625  -7.767  1.00 31.44  0  35  VAL   B C   1 
ATOM   2153 O  O   . VAL   B  1 20  ? 26.374  -7.456  -8.395  1.00 29.10  0  35  VAL   B O   1 
ATOM   2154 C  CB  . VAL   B  1 20  ? 25.841  -6.055  -5.628  1.00 31.61  0  35  VAL   B CB  1 
ATOM   2155 C  CG1 . VAL   B  1 20  ? 24.738  -7.092  -5.756  1.00 31.13  0  35  VAL   B CG1 1 
ATOM   2156 C  CG2 . VAL   B  1 20  ? 26.952  -6.641  -4.770  1.00 31.68  0  35  VAL   B CG2 1 
ATOM   2157 N  N   . HIS   B  1 21  ? 28.424  -6.682  -7.675  1.00 34.00  0  36  HIS   B N   1 
ATOM   2158 C  CA  . HIS   B  1 21  ? 29.251  -7.727  -8.334  1.00 40.01  0  36  HIS   B CA  1 
ATOM   2159 C  C   . HIS   B  1 21  ? 28.925  -9.104  -7.745  1.00 38.77  0  36  HIS   B C   1 
ATOM   2160 O  O   . HIS   B  1 21  ? 28.875  -9.216  -6.562  1.00 38.92  0  36  HIS   B O   1 
ATOM   2161 C  CB  . HIS   B  1 21  ? 30.751  -7.432  -8.254  1.00 44.34  0  36  HIS   B CB  1 
ATOM   2162 C  CG  . HIS   B  1 21  ? 31.557  -8.401  -9.053  1.00 53.19  0  36  HIS   B CG  1 
ATOM   2163 N  ND1 . HIS   B  1 21  ? 31.660  -8.317  -10.438 1.00 55.29  0  36  HIS   B ND1 1 
ATOM   2164 C  CD2 . HIS   B  1 21  ? 32.225  -9.516  -8.685  1.00 56.61  0  36  HIS   B CD2 1 
ATOM   2165 C  CE1 . HIS   B  1 21  ? 32.391  -9.317  -10.881 1.00 58.56  0  36  HIS   B CE1 1 
ATOM   2166 N  NE2 . HIS   B  1 21  ? 32.736  -10.074 -9.826  1.00 59.91  0  36  HIS   B NE2 1 
ATOM   2167 N  N   . GLY   B  1 22  ? 28.659  -10.091 -8.594  1.00 42.94  0  37  GLY   B N   1 
ATOM   2168 C  CA  . GLY   B  1 22  ? 28.597  -11.516 -8.249  1.00 43.76  0  37  GLY   B CA  1 
ATOM   2169 C  C   . GLY   B  1 22  ? 28.630  -12.342 -9.540  1.00 45.05  0  37  GLY   B C   1 
ATOM   2170 O  O   . GLY   B  1 22  ? 29.268  -11.927 -10.498 1.00 41.96  0  37  GLY   B O   1 
ATOM   2171 N  N   . PRO   B  1 23  ? 27.927  -13.494 -9.626  1.00 43.36  0  38  PRO   B N   1 
ATOM   2172 C  CA  . PRO   B  1 23  ? 27.902  -14.299 -10.852 1.00 37.43  0  38  PRO   B CA  1 
ATOM   2173 C  C   . PRO   B  1 23  ? 27.372  -13.472 -12.030 1.00 38.50  0  38  PRO   B C   1 
ATOM   2174 O  O   . PRO   B  1 23  ? 27.680  -13.771 -13.169 1.00 42.22  0  38  PRO   B O   1 
ATOM   2175 C  CB  . PRO   B  1 23  ? 26.898  -15.419 -10.532 1.00 38.35  0  38  PRO   B CB  1 
ATOM   2176 C  CG  . PRO   B  1 23  ? 26.821  -15.460 -9.041  1.00 40.74  0  38  PRO   B CG  1 
ATOM   2177 C  CD  . PRO   B  1 23  ? 27.072  -14.047 -8.563  1.00 42.96  0  38  PRO   B CD  1 
ATOM   2178 N  N   . TYR   B  1 24  ? 26.542  -12.458 -11.741 1.00 33.14  0  39  TYR   B N   1 
ATOM   2179 C  CA  . TYR   B  1 24  ? 26.238  -11.330 -12.661 1.00 30.92  0  39  TYR   B CA  1 
ATOM   2180 C  C   . TYR   B  1 24  ? 26.081  -10.027 -11.841 1.00 33.79  0  39  TYR   B C   1 
ATOM   2181 O  O   . TYR   B  1 24  ? 26.067  -10.081 -10.570 1.00 31.92  0  39  TYR   B O   1 
ATOM   2182 C  CB  . TYR   B  1 24  ? 24.982  -11.661 -13.460 1.00 27.65  0  39  TYR   B CB  1 
ATOM   2183 C  CG  . TYR   B  1 24  ? 23.737  -11.853 -12.633 1.00 30.69  0  39  TYR   B CG  1 
ATOM   2184 C  CD1 . TYR   B  1 24  ? 23.512  -13.008 -11.890 1.00 30.63  0  39  TYR   B CD1 1 
ATOM   2185 C  CD2 . TYR   B  1 24  ? 22.748  -10.884 -12.628 1.00 27.26  0  39  TYR   B CD2 1 
ATOM   2186 C  CE1 . TYR   B  1 24  ? 22.355  -13.172 -11.148 1.00 30.10  0  39  TYR   B CE1 1 
ATOM   2187 C  CE2 . TYR   B  1 24  ? 21.588  -11.035 -11.902 1.00 30.68  0  39  TYR   B CE2 1 
ATOM   2188 C  CZ  . TYR   B  1 24  ? 21.402  -12.169 -11.134 1.00 30.02  0  39  TYR   B CZ  1 
ATOM   2189 O  OH  . TYR   B  1 24  ? 20.229  -12.265 -10.454 1.00 28.10  0  39  TYR   B OH  1 
ATOM   2190 N  N   . TRP   B  1 25  ? 25.949  -8.899  -12.531 1.00 27.85  0  40  TRP   B N   1 
ATOM   2191 C  CA  . TRP   B  1 25  ? 25.734  -7.559  -11.908 1.00 28.20  0  40  TRP   B CA  1 
ATOM   2192 C  C   . TRP   B  1 25  ? 24.265  -7.447  -11.541 1.00 26.30  0  40  TRP   B C   1 
ATOM   2193 O  O   . TRP   B  1 25  ? 23.460  -7.029  -12.382 1.00 28.91  0  40  TRP   B O   1 
ATOM   2194 C  CB  . TRP   B  1 25  ? 26.177  -6.429  -12.831 1.00 28.32  0  40  TRP   B CB  1 
ATOM   2195 C  CG  . TRP   B  1 25  ? 27.661  -6.344  -12.893 1.00 31.66  0  40  TRP   B CG  1 
ATOM   2196 C  CD1 . TRP   B  1 25  ? 28.461  -6.847  -13.860 1.00 33.71  0  40  TRP   B CD1 1 
ATOM   2197 C  CD2 . TRP   B  1 25  ? 28.527  -5.665  -11.963 1.00 36.52  0  40  TRP   B CD2 1 
ATOM   2198 N  NE1 . TRP   B  1 25  ? 29.768  -6.548  -13.592 1.00 34.99  0  40  TRP   B NE1 1 
ATOM   2199 C  CE2 . TRP   B  1 25  ? 29.846  -5.834  -12.431 1.00 34.71  0  40  TRP   B CE2 1 
ATOM   2200 C  CE3 . TRP   B  1 25  ? 28.323  -4.930  -10.784 1.00 34.43  0  40  TRP   B CE3 1 
ATOM   2201 C  CZ2 . TRP   B  1 25  ? 30.962  -5.321  -11.754 1.00 35.70  0  40  TRP   B CZ2 1 
ATOM   2202 C  CZ3 . TRP   B  1 25  ? 29.418  -4.392  -10.137 1.00 35.02  0  40  TRP   B CZ3 1 
ATOM   2203 C  CH2 . TRP   B  1 25  ? 30.719  -4.581  -10.617 1.00 36.61  0  40  TRP   B CH2 1 
ATOM   2204 N  N   . MET   B  1 26  ? 23.940  -7.888  -10.324 1.00 27.11  0  41  MET   B N   1 
ATOM   2205 C  CA  . MET   B  1 26  ? 22.548  -8.086  -9.880  1.00 28.43  0  41  MET   B CA  1 
ATOM   2206 C  C   . MET   B  1 26  ? 21.960  -6.749  -9.362  1.00 25.82  0  41  MET   B C   1 
ATOM   2207 O  O   . MET   B  1 26  ? 22.614  -6.068  -8.583  1.00 26.46  0  41  MET   B O   1 
ATOM   2208 C  CB  . MET   B  1 26  ? 22.530  -9.166  -8.785  1.00 29.31  0  41  MET   B CB  1 
ATOM   2209 C  CG  . MET   B  1 26  ? 21.140  -9.601  -8.395  1.00 35.59  0  41  MET   B CG  1 
ATOM   2210 S  SD  . MET   B  1 26  ? 21.137  -11.072 -7.338  1.00 41.92  0  41  MET   B SD  1 
ATOM   2211 C  CE  . MET   B  1 26  ? 22.420  -10.668 -6.162  1.00 44.12  0  41  MET   B CE  1 
ATOM   2212 N  N   . HIS   B  1 27  ? 20.737  -6.435  -9.759  1.00 26.05  0  42  HIS   B N   1 
ATOM   2213 C  CA  . HIS   B  1 27  ? 19.909  -5.364  -9.160  1.00 27.83  0  42  HIS   B CA  1 
ATOM   2214 C  C   . HIS   B  1 27  ? 19.650  -5.667  -7.675  1.00 32.90  0  42  HIS   B C   1 
ATOM   2215 O  O   . HIS   B  1 27  ? 19.198  -6.778  -7.373  1.00 28.96  0  42  HIS   B O   1 
ATOM   2216 C  CB  . HIS   B  1 27  ? 18.595  -5.247  -9.912  1.00 26.83  0  42  HIS   B CB  1 
ATOM   2217 C  CG  . HIS   B  1 27  ? 17.674  -4.273  -9.275  1.00 31.45  0  42  HIS   B CG  1 
ATOM   2218 N  ND1 . HIS   B  1 27  ? 17.696  -2.921  -9.569  1.00 27.60  0  42  HIS   B ND1 1 
ATOM   2219 C  CD2 . HIS   B  1 27  ? 16.729  -4.464  -8.332  1.00 27.12  0  42  HIS   B CD2 1 
ATOM   2220 C  CE1 . HIS   B  1 27  ? 16.765  -2.326  -8.865  1.00 27.03  0  42  HIS   B CE1 1 
ATOM   2221 N  NE2 . HIS   B  1 27  ? 16.156  -3.254  -8.080  1.00 24.14  0  42  HIS   B NE2 1 
ATOM   2222 N  N   . PHE   B  1 28  ? 19.984  -4.727  -6.788  1.00 32.45  0  43  PHE   B N   1 
ATOM   2223 C  CA  . PHE   B  1 28  ? 19.636  -4.803  -5.347  1.00 31.81  0  43  PHE   B CA  1 
ATOM   2224 C  C   . PHE   B  1 28  ? 18.813  -3.577  -4.882  1.00 30.64  0  43  PHE   B C   1 
ATOM   2225 O  O   . PHE   B  1 28  ? 18.193  -3.651  -3.814  1.00 28.69  0  43  PHE   B O   1 
ATOM   2226 C  CB  . PHE   B  1 28  ? 20.911  -4.998  -4.540  1.00 26.40  0  43  PHE   B CB  1 
ATOM   2227 C  CG  . PHE   B  1 28  ? 21.852  -3.823  -4.531  1.00 26.59  0  43  PHE   B CG  1 
ATOM   2228 C  CD1 . PHE   B  1 28  ? 21.735  -2.835  -3.575  1.00 25.95  0  43  PHE   B CD1 1 
ATOM   2229 C  CD2 . PHE   B  1 28  ? 22.909  -3.759  -5.417  1.00 24.69  0  43  PHE   B CD2 1 
ATOM   2230 C  CE1 . PHE   B  1 28  ? 22.630  -1.775  -3.522  1.00 27.93  0  43  PHE   B CE1 1 
ATOM   2231 C  CE2 . PHE   B  1 28  ? 23.821  -2.717  -5.363  1.00 26.83  0  43  PHE   B CE2 1 
ATOM   2232 C  CZ  . PHE   B  1 28  ? 23.662  -1.706  -4.436  1.00 28.61  0  43  PHE   B CZ  1 
ATOM   2233 N  N   . CYS   B  1 29  ? 18.855  -2.443  -5.581  1.00 28.06  0  44  CYS   B N   1 
ATOM   2234 C  CA  . CYS   B  1 29  ? 18.126  -1.218  -5.143  1.00 28.22  0  44  CYS   B CA  1 
ATOM   2235 C  C   . CYS   B  1 29  ? 17.917  -0.285  -6.333  1.00 27.46  0  44  CYS   B C   1 
ATOM   2236 O  O   . CYS   B  1 29  ? 18.664  -0.402  -7.312  1.00 31.06  0  44  CYS   B O   1 
ATOM   2237 C  CB  . CYS   B  1 29  ? 18.878  -0.464  -4.037  1.00 25.58  0  44  CYS   B CB  1 
ATOM   2238 S  SG  . CYS   B  1 29  ? 18.617  -1.090  -2.350  1.00 29.63  0  44  CYS   B SG  1 
ATOM   2239 N  N   . GLY   B  1 30  ? 16.952  0.619   -6.182  1.00 26.27  0  45  GLY   B N   1 
ATOM   2240 C  CA  . GLY   B  1 30  ? 16.704  1.777   -7.047  1.00 27.52  0  45  GLY   B CA  1 
ATOM   2241 C  C   . GLY   B  1 30  ? 17.472  3.007   -6.599  1.00 24.85  0  45  GLY   B C   1 
ATOM   2242 O  O   . GLY   B  1 30  ? 18.189  2.983   -5.580  1.00 25.15  0  45  GLY   B O   1 
ATOM   2243 N  N   . GLY   B  1 31  ? 17.413  4.011   -7.449  1.00 24.98  0  46  GLY   B N   1 
ATOM   2244 C  CA  . GLY   B  1 31  ? 17.958  5.356   -7.259  1.00 26.76  0  46  GLY   B CA  1 
ATOM   2245 C  C   . GLY   B  1 31  ? 17.283  6.311   -8.232  1.00 27.71  0  46  GLY   B C   1 
ATOM   2246 O  O   . GLY   B  1 31  ? 16.421  5.855   -9.039  1.00 26.83  0  46  GLY   B O   1 
ATOM   2247 N  N   . SER   B  1 32  ? 17.654  7.587   -8.172  1.00 26.09  0  47  SER   B N   1 
ATOM   2248 C  CA  . SER   B  1 32  ? 17.152  8.627   -9.100  1.00 26.27  0  47  SER   B CA  1 
ATOM   2249 C  C   . SER   B  1 32  ? 18.324  9.492   -9.532  1.00 26.85  0  47  SER   B C   1 
ATOM   2250 O  O   . SER   B  1 32  ? 19.253  9.723   -8.718  1.00 26.78  0  47  SER   B O   1 
ATOM   2251 C  CB  . SER   B  1 32  ? 16.014  9.411   -8.502  1.00 25.19  0  47  SER   B CB  1 
ATOM   2252 O  OG  . SER   B  1 32  ? 16.423  10.079  -7.329  1.00 26.01  0  47  SER   B OG  1 
ATOM   2253 N  N   . LEU   B  1 33  ? 18.333  9.878   -10.810 1.00 28.19  0  48  LEU   B N   1 
ATOM   2254 C  CA  . LEU   B  1 33  ? 19.337  10.836  -11.316 1.00 32.80  0  48  LEU   B CA  1 
ATOM   2255 C  C   . LEU   B  1 33  ? 18.852  12.255  -10.964 1.00 31.55  0  48  LEU   B C   1 
ATOM   2256 O  O   . LEU   B  1 33  ? 17.807  12.669  -11.483 1.00 32.56  0  48  LEU   B O   1 
ATOM   2257 C  CB  . LEU   B  1 33  ? 19.507  10.605  -12.812 1.00 33.79  0  48  LEU   B CB  1 
ATOM   2258 C  CG  . LEU   B  1 33  ? 20.660  11.368  -13.432 1.00 33.04  0  48  LEU   B CG  1 
ATOM   2259 C  CD1 . LEU   B  1 33  ? 21.974  10.696  -13.079 1.00 32.31  0  48  LEU   B CD1 1 
ATOM   2260 C  CD2 . LEU   B  1 33  ? 20.466  11.487  -14.939 1.00 36.52  0  48  LEU   B CD2 1 
ATOM   2261 N  N   . ILE   B  1 34  ? 19.518  12.930  -10.030 1.00 30.95  0  49  ILE   B N   1 
ATOM   2262 C  CA  . ILE   B  1 34  ? 19.117  14.307  -9.576  1.00 31.59  0  49  ILE   B CA  1 
ATOM   2263 C  C   . ILE   B  1 34  ? 20.070  15.357  -10.187 1.00 30.45  0  49  ILE   B C   1 
ATOM   2264 O  O   . ILE   B  1 34  ? 19.845  16.550  -10.016 1.00 32.49  0  49  ILE   B O   1 
ATOM   2265 C  CB  . ILE   B  1 34  ? 19.068  14.391  -8.036  1.00 28.33  0  49  ILE   B CB  1 
ATOM   2266 C  CG1 . ILE   B  1 34  ? 20.408  14.018  -7.398  1.00 28.40  0  49  ILE   B CG1 1 
ATOM   2267 C  CG2 . ILE   B  1 34  ? 17.917  13.541  -7.497  1.00 29.54  0  49  ILE   B CG2 1 
ATOM   2268 C  CD1 . ILE   B  1 34  ? 20.576  14.553  -6.000  1.00 30.58  0  49  ILE   B CD1 1 
ATOM   2269 N  N   . HIS   B  1 35  ? 21.157  14.917  -10.790 1.00 31.66  0  50  HIS   B N   1 
ATOM   2270 C  CA  . HIS   B  1 35  ? 22.166  15.768  -11.447 1.00 36.11  0  50  HIS   B CA  1 
ATOM   2271 C  C   . HIS   B  1 35  ? 22.868  14.840  -12.417 1.00 38.74  0  50  HIS   B C   1 
ATOM   2272 O  O   . HIS   B  1 35  ? 22.923  13.627  -12.148 1.00 33.88  0  50  HIS   B O   1 
ATOM   2273 C  CB  . HIS   B  1 35  ? 23.080  16.405  -10.392 1.00 34.58  0  50  HIS   B CB  1 
ATOM   2274 C  CG  . HIS   B  1 35  ? 24.176  17.260  -10.938 1.00 36.29  0  50  HIS   B CG  1 
ATOM   2275 N  ND1 . HIS   B  1 35  ? 25.355  16.737  -11.472 1.00 40.70  0  50  HIS   B ND1 1 
ATOM   2276 C  CD2 . HIS   B  1 35  ? 24.285  18.601  -11.061 1.00 35.66  0  50  HIS   B CD2 1 
ATOM   2277 C  CE1 . HIS   B  1 35  ? 26.162  17.715  -11.873 1.00 33.56  0  50  HIS   B CE1 1 
ATOM   2278 N  NE2 . HIS   B  1 35  ? 25.513  18.876  -11.624 1.00 33.75  0  50  HIS   B NE2 1 
ATOM   2279 N  N   . PRO   B  1 36  ? 23.403  15.344  -13.558 1.00 37.23  0  51  PRO   B N   1 
ATOM   2280 C  CA  . PRO   B  1 36  ? 24.163  14.484  -14.471 1.00 35.12  0  51  PRO   B CA  1 
ATOM   2281 C  C   . PRO   B  1 36  ? 25.247  13.600  -13.846 1.00 32.47  0  51  PRO   B C   1 
ATOM   2282 O  O   . PRO   B  1 36  ? 25.548  12.563  -14.432 1.00 32.21  0  51  PRO   B O   1 
ATOM   2283 C  CB  . PRO   B  1 36  ? 24.790  15.500  -15.448 1.00 38.27  0  51  PRO   B CB  1 
ATOM   2284 C  CG  . PRO   B  1 36  ? 23.719  16.601  -15.515 1.00 34.47  0  51  PRO   B CG  1 
ATOM   2285 C  CD  . PRO   B  1 36  ? 23.274  16.733  -14.069 1.00 36.86  0  51  PRO   B CD  1 
ATOM   2286 N  N   . GLN   B  1 37  ? 25.800  13.973  -12.692 1.00 36.66  0  52  GLN   B N   1 
ATOM   2287 C  CA  . GLN   B  1 37  ? 26.896  13.198  -12.031 1.00 33.12  0  52  GLN   B CA  1 
ATOM   2288 C  C   . GLN   B  1 37  ? 26.451  12.650  -10.664 1.00 28.72  0  52  GLN   B C   1 
ATOM   2289 O  O   . GLN   B  1 37  ? 27.311  12.081  -9.932  1.00 28.15  0  52  GLN   B O   1 
ATOM   2290 C  CB  . GLN   B  1 37  ? 28.140  14.065  -11.969 1.00 33.03  0  52  GLN   B CB  1 
ATOM   2291 C  CG  . GLN   B  1 37  ? 29.411  13.252  -11.735 1.00 36.45  0  52  GLN   B CG  1 
ATOM   2292 C  CD  . GLN   B  1 37  ? 30.640  13.866  -12.357 1.00 35.36  0  52  GLN   B CD  1 
ATOM   2293 O  OE1 . GLN   B  1 37  ? 30.586  14.983  -12.853 1.00 39.42  0  52  GLN   B OE1 1 
ATOM   2294 N  NE2 . GLN   B  1 37  ? 31.754  13.141  -12.307 1.00 33.39  0  52  GLN   B NE2 1 
ATOM   2295 N  N   . TRP   B  1 38  ? 25.158  12.740  -10.321 1.00 31.63  0  53  TRP   B N   1 
ATOM   2296 C  CA  . TRP   B  1 38  ? 24.699  12.351  -8.955  1.00 31.72  0  53  TRP   B CA  1 
ATOM   2297 C  C   . TRP   B  1 38  ? 23.440  11.501  -8.995  1.00 28.93  0  53  TRP   B C   1 
ATOM   2298 O  O   . TRP   B  1 38  ? 22.396  11.916  -9.595  1.00 28.49  0  53  TRP   B O   1 
ATOM   2299 C  CB  . TRP   B  1 38  ? 24.511  13.571  -8.043  1.00 31.76  0  53  TRP   B CB  1 
ATOM   2300 C  CG  . TRP   B  1 38  ? 25.802  14.251  -7.717  1.00 33.69  0  53  TRP   B CG  1 
ATOM   2301 C  CD1 . TRP   B  1 38  ? 26.371  15.261  -8.430  1.00 34.40  0  53  TRP   B CD1 1 
ATOM   2302 C  CD2 . TRP   B  1 38  ? 26.696  13.995  -6.615  1.00 34.82  0  53  TRP   B CD2 1 
ATOM   2303 N  NE1 . TRP   B  1 38  ? 27.568  15.622  -7.872  1.00 32.55  0  53  TRP   B NE1 1 
ATOM   2304 C  CE2 . TRP   B  1 38  ? 27.769  14.924  -6.723  1.00 34.71  0  53  TRP   B CE2 1 
ATOM   2305 C  CE3 . TRP   B  1 38  ? 26.675  13.147  -5.504  1.00 33.47  0  53  TRP   B CE3 1 
ATOM   2306 C  CZ2 . TRP   B  1 38  ? 28.819  14.983  -5.804  1.00 35.72  0  53  TRP   B CZ2 1 
ATOM   2307 C  CZ3 . TRP   B  1 38  ? 27.721  13.191  -4.601  1.00 32.24  0  53  TRP   B CZ3 1 
ATOM   2308 C  CH2 . TRP   B  1 38  ? 28.778  14.099  -4.743  1.00 33.66  0  53  TRP   B CH2 1 
ATOM   2309 N  N   . VAL   B  1 39  ? 23.496  10.427  -8.219  1.00 28.86  0  54  VAL   B N   1 
ATOM   2310 C  CA  . VAL   B  1 39  ? 22.319  9.552   -7.951  1.00 27.84  0  54  VAL   B CA  1 
ATOM   2311 C  C   . VAL   B  1 39  ? 21.935  9.683   -6.481  1.00 25.09  0  54  VAL   B C   1 
ATOM   2312 O  O   . VAL   B  1 39  ? 22.808  9.523   -5.606  1.00 24.57  0  54  VAL   B O   1 
ATOM   2313 C  CB  . VAL   B  1 39  ? 22.607  8.103   -8.367  1.00 27.73  0  54  VAL   B CB  1 
ATOM   2314 C  CG1 . VAL   B  1 39  ? 21.534  7.133   -7.878  1.00 25.48  0  54  VAL   B CG1 1 
ATOM   2315 C  CG2 . VAL   B  1 39  ? 22.767  8.022   -9.880  1.00 28.40  0  54  VAL   B CG2 1 
ATOM   2316 N  N   . LEU   B  1 40  ? 20.642  9.866   -6.248  1.00 26.40  0  55  LEU   B N   1 
ATOM   2317 C  CA  . LEU   B  1 40  ? 20.019  9.851   -4.913  1.00 25.91  0  55  LEU   B CA  1 
ATOM   2318 C  C   . LEU   B  1 40  ? 19.467  8.437   -4.654  1.00 27.61  0  55  LEU   B C   1 
ATOM   2319 O  O   . LEU   B  1 40  ? 18.728  7.901   -5.528  1.00 23.11  0  55  LEU   B O   1 
ATOM   2320 C  CB  . LEU   B  1 40  ? 18.909  10.906  -4.896  1.00 27.22  0  55  LEU   B CB  1 
ATOM   2321 C  CG  . LEU   B  1 40  ? 18.233  11.093  -3.537  1.00 27.48  0  55  LEU   B CG  1 
ATOM   2322 C  CD1 . LEU   B  1 40  ? 19.171  11.709  -2.535  1.00 28.44  0  55  LEU   B CD1 1 
ATOM   2323 C  CD2 . LEU   B  1 40  ? 16.982  11.912  -3.670  1.00 29.49  0  55  LEU   B CD2 1 
ATOM   2324 N  N   . THR   B  1 41  ? 19.801  7.855   -3.500  1.00 25.92  0  56  THR   B N   1 
ATOM   2325 C  CA  . THR   B  1 41  ? 19.280  6.536   -3.059  1.00 25.77  0  56  THR   B CA  1 
ATOM   2326 C  C   . THR   B  1 41  ? 19.035  6.514   -1.531  1.00 26.22  0  56  THR   B C   1 
ATOM   2327 O  O   . THR   B  1 41  ? 19.118  7.573   -0.845  1.00 22.04  0  56  THR   B O   1 
ATOM   2328 C  CB  . THR   B  1 41  ? 20.231  5.458   -3.611  1.00 23.66  0  56  THR   B CB  1 
ATOM   2329 O  OG1 . THR   B  1 41  ? 19.571  4.196   -3.514  1.00 26.76  0  56  THR   B OG1 1 
ATOM   2330 C  CG2 . THR   B  1 41  ? 21.573  5.404   -2.925  1.00 25.14  0  56  THR   B CG2 1 
ATOM   2331 N  N   . ALA   B  1 42  ? 18.692  5.338   -1.006  1.00 25.84  0  57  ALA   B N   1 
ATOM   2332 C  CA  . ALA   B  1 42  ? 18.549  5.063   0.448   1.00 27.14  0  57  ALA   B CA  1 
ATOM   2333 C  C   . ALA   B  1 42  ? 19.920  4.706   1.006   1.00 26.09  0  57  ALA   B C   1 
ATOM   2334 O  O   . ALA   B  1 42  ? 20.592  3.902   0.378   1.00 26.88  0  57  ALA   B O   1 
ATOM   2335 C  CB  . ALA   B  1 42  ? 17.581  3.932   0.679   1.00 29.11  0  57  ALA   B CB  1 
ATOM   2336 N  N   . ALA   B  1 43  ? 20.291  5.250   2.158   1.00 24.25  0  58  ALA   B N   1 
ATOM   2337 C  CA  . ALA   B  1 43  ? 21.474  4.828   2.947   1.00 24.65  0  58  ALA   B CA  1 
ATOM   2338 C  C   . ALA   B  1 43  ? 21.469  3.317   3.222   1.00 23.43  0  58  ALA   B C   1 
ATOM   2339 O  O   . ALA   B  1 43  ? 22.550  2.735   3.189   1.00 22.26  0  58  ALA   B O   1 
ATOM   2340 C  CB  . ALA   B  1 43  ? 21.552  5.578   4.256   1.00 28.15  0  58  ALA   B CB  1 
ATOM   2341 N  N   . HIS   B  1 44  ? 20.326  2.707   3.530   1.00 25.10  0  59  HIS   B N   1 
ATOM   2342 C  CA  . HIS   B  1 44  ? 20.279  1.260   3.902   1.00 25.40  0  59  HIS   B CA  1 
ATOM   2343 C  C   . HIS   B  1 44  ? 20.693  0.383   2.700   1.00 26.55  0  59  HIS   B C   1 
ATOM   2344 O  O   . HIS   B  1 44  ? 21.090  -0.774  2.941   1.00 29.83  0  59  HIS   B O   1 
ATOM   2345 C  CB  . HIS   B  1 44  ? 18.929  0.867   4.536   1.00 24.60  0  59  HIS   B CB  1 
ATOM   2346 C  CG  . HIS   B  1 44  ? 17.885  0.519   3.550   1.00 26.62  0  59  HIS   B CG  1 
ATOM   2347 N  ND1 . HIS   B  1 44  ? 16.884  1.417   3.188   1.00 24.96  0  59  HIS   B ND1 1 
ATOM   2348 C  CD2 . HIS   B  1 44  ? 17.708  -0.605  2.815   1.00 26.86  0  59  HIS   B CD2 1 
ATOM   2349 C  CE1 . HIS   B  1 44  ? 16.115  0.836   2.296   1.00 25.98  0  59  HIS   B CE1 1 
ATOM   2350 N  NE2 . HIS   B  1 44  ? 16.584  -0.410  2.057   1.00 24.09  0  59  HIS   B NE2 1 
ATOM   2351 N  N   . CYS   B  1 45  ? 20.641  0.885   1.461   1.00 25.73  0  60  CYS   B N   1 
ATOM   2352 C  CA  . CYS   B  1 45  ? 21.112  0.134   0.264   1.00 25.73  0  60  CYS   B CA  1 
ATOM   2353 C  C   . CYS   B  1 45  ? 22.622  -0.037  0.289   1.00 25.69  0  60  CYS   B C   1 
ATOM   2354 O  O   . CYS   B  1 45  ? 23.115  -1.060  -0.276  1.00 25.14  0  60  CYS   B O   1 
ATOM   2355 C  CB  . CYS   B  1 45  ? 20.717  0.809   -1.037  1.00 23.98  0  60  CYS   B CB  1 
ATOM   2356 S  SG  . CYS   B  1 45  ? 18.940  0.759   -1.288  1.00 27.99  0  60  CYS   B SG  1 
ATOM   2357 N  N   . VAL   B  1 46  ? 23.336  0.942   0.850   1.00 24.03  0  61  VAL   B N   1 
ATOM   2358 C  CA  . VAL   B  1 46  ? 24.820  1.027   0.708   1.00 27.09  0  61  VAL   B CA  1 
ATOM   2359 C  C   . VAL   B  1 46  ? 25.486  1.233   2.083   1.00 28.47  0  61  VAL   B C   1 
ATOM   2360 O  O   . VAL   B  1 46  ? 26.675  1.546   2.097   1.00 39.02  0  61  VAL   B O   1 
ATOM   2361 C  CB  . VAL   B  1 46  ? 25.203  2.127   -0.312  1.00 27.52  0  61  VAL   B CB  1 
ATOM   2362 C  CG1 . VAL   B  1 46  ? 24.716  1.805   -1.713  1.00 31.13  0  61  VAL   B CG1 1 
ATOM   2363 C  CG2 . VAL   B  1 46  ? 24.647  3.486   0.077   1.00 28.70  0  61  VAL   B CG2 1 
ATOM   2364 N  N   . GLY   B  1 47  ? 24.768  1.062   3.202   1.00 28.79  0  62  GLY   B N   1 
ATOM   2365 C  CA  . GLY   B  1 47  ? 25.325  1.238   4.557   1.00 26.74  0  62  GLY   B CA  1 
ATOM   2366 C  C   . GLY   B  1 47  ? 24.461  0.558   5.616   1.00 28.96  0  62  GLY   B C   1 
ATOM   2367 O  O   . GLY   B  1 47  ? 23.516  -0.115  5.259   1.00 27.51  0  62  GLY   B O   1 
ATOM   2368 N  N   . PRO   B  1 48  ? 24.717  0.734   6.940   1.00 27.58  0  63  PRO   B N   1 
ATOM   2369 C  CA  . PRO   B  1 48  ? 25.736  1.660   7.419   1.00 27.00  0  63  PRO   B CA  1 
ATOM   2370 C  C   . PRO   B  1 48  ? 27.187  1.215   7.304   1.00 27.62  0  63  PRO   B C   1 
ATOM   2371 O  O   . PRO   B  1 48  ? 28.039  2.049   7.481   1.00 31.93  0  63  PRO   B O   1 
ATOM   2372 C  CB  . PRO   B  1 48  ? 25.374  1.814   8.914   1.00 27.56  0  63  PRO   B CB  1 
ATOM   2373 C  CG  . PRO   B  1 48  ? 24.751  0.500   9.276   1.00 27.80  0  63  PRO   B CG  1 
ATOM   2374 C  CD  . PRO   B  1 48  ? 23.993  0.072   8.042   1.00 29.16  0  63  PRO   B CD  1 
ATOM   2375 N  N   . ASP   B  1 49  ? 27.468  -0.055  7.038   1.00 29.12  0  64  ASP   B N   1 
ATOM   2376 C  CA  . ASP   B  1 49  ? 28.874  -0.547  6.953   1.00 31.96  0  64  ASP   B CA  1 
ATOM   2377 C  C   . ASP   B  1 49  ? 29.497  -0.147  5.607   1.00 30.22  0  64  ASP   B C   1 
ATOM   2378 O  O   . ASP   B  1 49  ? 28.805  -0.156  4.601   1.00 29.85  0  64  ASP   B O   1 
ATOM   2379 C  CB  . ASP   B  1 49  ? 28.979  -2.055  7.146   1.00 33.96  0  64  ASP   B CB  1 
ATOM   2380 C  CG  . ASP   B  1 49  ? 28.572  -2.517  8.555   1.00 43.07  0  64  ASP   B CG  1 
ATOM   2381 O  OD1 . ASP   B  1 49  ? 28.748  -1.744  9.571   1.00 36.81  0  64  ASP   B OD1 1 
ATOM   2382 O  OD2 . ASP   B  1 49  ? 28.033  -3.625  8.630   1.00 53.61  -1 64  ASP   B OD2 1 
ATOM   2383 N  N   . VAL   B  1 50  ? 30.777  0.200   5.622   1.00 33.48  0  65  VAL   B N   1 
ATOM   2384 C  CA  . VAL   B  1 50  ? 31.533  0.712   4.446   1.00 36.06  0  65  VAL   B CA  1 
ATOM   2385 C  C   . VAL   B  1 50  ? 31.703  -0.434  3.443   1.00 41.21  0  65  VAL   B C   1 
ATOM   2386 O  O   . VAL   B  1 50  ? 32.144  -1.510  3.865   1.00 41.24  0  65  VAL   B O   1 
ATOM   2387 C  CB  . VAL   B  1 50  ? 32.898  1.277   4.872   1.00 40.77  0  65  VAL   B CB  1 
ATOM   2388 C  CG1 . VAL   B  1 50  ? 33.750  1.655   3.653   1.00 41.13  0  65  VAL   B CG1 1 
ATOM   2389 C  CG2 . VAL   B  1 50  ? 32.718  2.476   5.800   1.00 38.72  0  65  VAL   B CG2 1 
ATOM   2390 N  N   . LYS   B  1 51  ? 31.362  -0.209  2.176   1.00 40.40  0  66  LYS   B N   1 
ATOM   2391 C  CA  . LYS   B  1 51  ? 31.475  -1.233  1.099   1.00 47.21  0  66  LYS   B CA  1 
ATOM   2392 C  C   . LYS   B  1 51  ? 32.519  -0.817  0.047   1.00 44.56  0  66  LYS   B C   1 
ATOM   2393 O  O   . LYS   B  1 51  ? 32.896  0.357   -0.025  1.00 44.88  0  66  LYS   B O   1 
ATOM   2394 C  CB  . LYS   B  1 51  ? 30.070  -1.465  0.533   1.00 56.36  0  66  LYS   B CB  1 
ATOM   2395 C  CG  . LYS   B  1 51  ? 29.182  -2.378  1.393   1.00 60.22  0  66  LYS   B CG  1 
ATOM   2396 C  CD  . LYS   B  1 51  ? 27.835  -1.798  1.816   1.00 64.96  0  66  LYS   B CD  1 
ATOM   2397 C  CE  . LYS   B  1 51  ? 27.097  -2.678  2.810   1.00 61.89  0  66  LYS   B CE  1 
ATOM   2398 N  NZ  . LYS   B  1 51  ? 25.675  -2.278  2.926   1.00 64.86  1  66  LYS   B NZ  1 
ATOM   2399 N  N   . ASP   B  1 52  ? 32.993  -1.792  -0.718  1.00 46.86  0  67  ASP   B N   1 
ATOM   2400 C  CA  . ASP   B  1 52  ? 34.016  -1.618  -1.775  1.00 43.22  0  67  ASP   B CA  1 
ATOM   2401 C  C   . ASP   B  1 52  ? 33.347  -0.969  -2.985  1.00 38.83  0  67  ASP   B C   1 
ATOM   2402 O  O   . ASP   B  1 52  ? 32.450  -1.615  -3.562  1.00 43.62  0  67  ASP   B O   1 
ATOM   2403 C  CB  . ASP   B  1 52  ? 34.603  -2.975  -2.167  1.00 46.95  0  67  ASP   B CB  1 
ATOM   2404 C  CG  . ASP   B  1 52  ? 35.881  -2.860  -2.972  1.00 45.16  0  67  ASP   B CG  1 
ATOM   2405 O  OD1 . ASP   B  1 52  ? 36.064  -1.861  -3.680  1.00 43.23  0  67  ASP   B OD1 1 
ATOM   2406 O  OD2 . ASP   B  1 52  ? 36.721  -3.741  -2.820  1.00 60.71  -1 67  ASP   B OD2 1 
ATOM   2407 N  N   . LEU   B  1 53  ? 33.792  0.204   -3.421  1.00 36.64  0  68  LEU   B N   1 
ATOM   2408 C  CA  . LEU   B  1 53  ? 33.207  0.872   -4.618  1.00 39.83  0  68  LEU   B CA  1 
ATOM   2409 C  C   . LEU   B  1 53  ? 33.340  0.019   -5.884  1.00 37.35  0  68  LEU   B C   1 
ATOM   2410 O  O   . LEU   B  1 53  ? 32.477  0.170   -6.760  1.00 39.16  0  68  LEU   B O   1 
ATOM   2411 C  CB  . LEU   B  1 53  ? 33.886  2.214   -4.842  1.00 48.06  0  68  LEU   B CB  1 
ATOM   2412 C  CG  . LEU   B  1 53  ? 33.532  3.286   -3.822  1.00 54.78  0  68  LEU   B CG  1 
ATOM   2413 C  CD1 . LEU   B  1 53  ? 34.413  4.492   -4.045  1.00 61.93  0  68  LEU   B CD1 1 
ATOM   2414 C  CD2 . LEU   B  1 53  ? 32.063  3.679   -3.902  1.00 55.59  0  68  LEU   B CD2 1 
ATOM   2415 N  N   . ALA   B  1 54  ? 34.356  -0.842  -5.970  1.00 35.05  0  69  ALA   B N   1 
ATOM   2416 C  CA  . ALA   B  1 54  ? 34.622  -1.690  -7.161  1.00 36.72  0  69  ALA   B CA  1 
ATOM   2417 C  C   . ALA   B  1 54  ? 33.448  -2.658  -7.379  1.00 37.37  0  69  ALA   B C   1 
ATOM   2418 O  O   . ALA   B  1 54  ? 33.204  -3.002  -8.524  1.00 38.02  0  69  ALA   B O   1 
ATOM   2419 C  CB  . ALA   B  1 54  ? 35.916  -2.453  -7.008  1.00 34.84  0  69  ALA   B CB  1 
ATOM   2420 N  N   . ALA   B  1 55  ? 32.755  -3.044  -6.302  1.00 32.66  0  70  ALA   B N   1 
ATOM   2421 C  CA  . ALA   B  1 55  ? 31.644  -4.015  -6.325  1.00 33.11  0  70  ALA   B CA  1 
ATOM   2422 C  C   . ALA   B  1 55  ? 30.321  -3.332  -6.689  1.00 28.37  0  70  ALA   B C   1 
ATOM   2423 O  O   . ALA   B  1 55  ? 29.338  -4.046  -6.745  1.00 30.79  0  70  ALA   B O   1 
ATOM   2424 C  CB  . ALA   B  1 55  ? 31.574  -4.745  -4.998  1.00 31.33  0  70  ALA   B CB  1 
ATOM   2425 N  N   . LEU   B  1 56  ? 30.283  -2.019  -6.930  1.00 29.29  0  71  LEU   B N   1 
ATOM   2426 C  CA  . LEU   B  1 56  ? 29.026  -1.281  -7.216  1.00 30.47  0  71  LEU   B CA  1 
ATOM   2427 C  C   . LEU   B  1 56  ? 29.060  -0.696  -8.640  1.00 31.76  0  71  LEU   B C   1 
ATOM   2428 O  O   . LEU   B  1 56  ? 30.090  -0.130  -9.010  1.00 31.31  0  71  LEU   B O   1 
ATOM   2429 C  CB  . LEU   B  1 56  ? 28.860  -0.178  -6.177  1.00 29.43  0  71  LEU   B CB  1 
ATOM   2430 C  CG  . LEU   B  1 56  ? 27.639  0.719   -6.325  1.00 29.37  0  71  LEU   B CG  1 
ATOM   2431 C  CD1 . LEU   B  1 56  ? 26.353  -0.070  -6.144  1.00 31.79  0  71  LEU   B CD1 1 
ATOM   2432 C  CD2 . LEU   B  1 56  ? 27.674  1.853   -5.307  1.00 34.73  0  71  LEU   B CD2 1 
ATOM   2433 N  N   . ARG   B  1 57  ? 27.947  -0.794  -9.360  1.00 29.20  0  72  ARG   B N   1 
ATOM   2434 C  CA  . ARG   B  1 57  ? 27.725  -0.025  -10.598 1.00 31.91  0  72  ARG   B CA  1 
ATOM   2435 C  C   . ARG   B  1 57  ? 26.301  0.499   -10.631 1.00 28.22  0  72  ARG   B C   1 
ATOM   2436 O  O   . ARG   B  1 57  ? 25.389  -0.057  -9.950  1.00 25.72  0  72  ARG   B O   1 
ATOM   2437 C  CB  . ARG   B  1 57  ? 27.922  -0.890  -11.844 1.00 34.18  0  72  ARG   B CB  1 
ATOM   2438 C  CG  . ARG   B  1 57  ? 29.290  -1.523  -11.961 1.00 35.89  0  72  ARG   B CG  1 
ATOM   2439 C  CD  . ARG   B  1 57  ? 30.285  -0.616  -12.600 1.00 39.81  0  72  ARG   B CD  1 
ATOM   2440 N  NE  . ARG   B  1 57  ? 31.421  -1.436  -12.972 1.00 38.22  0  72  ARG   B NE  1 
ATOM   2441 C  CZ  . ARG   B  1 57  ? 32.459  -1.740  -12.200 1.00 45.93  0  72  ARG   B CZ  1 
ATOM   2442 N  NH1 . ARG   B  1 57  ? 32.548  -1.313  -10.949 1.00 49.90  1  72  ARG   B NH1 1 
ATOM   2443 N  NH2 . ARG   B  1 57  ? 33.419  -2.500  -12.700 1.00 45.79  0  72  ARG   B NH2 1 
ATOM   2444 N  N   . VAL   B  1 58  ? 26.126  1.500   -11.480 1.00 27.28  0  73  VAL   B N   1 
ATOM   2445 C  CA  . VAL   B  1 58  ? 24.833  2.163   -11.740 1.00 27.73  0  73  VAL   B CA  1 
ATOM   2446 C  C   . VAL   B  1 58  ? 24.430  1.847   -13.183 1.00 27.36  0  73  VAL   B C   1 
ATOM   2447 O  O   . VAL   B  1 58  ? 25.275  1.968   -14.090 1.00 26.37  0  73  VAL   B O   1 
ATOM   2448 C  CB  . VAL   B  1 58  ? 24.955  3.674   -11.481 1.00 28.55  0  73  VAL   B CB  1 
ATOM   2449 C  CG1 . VAL   B  1 58  ? 23.783  4.450   -12.043 1.00 29.07  0  73  VAL   B CG1 1 
ATOM   2450 C  CG2 . VAL   B  1 58  ? 25.111  3.950   -9.993  1.00 31.32  0  73  VAL   B CG2 1 
ATOM   2451 N  N   . GLN   B  1 59  ? 23.148  1.579   -13.374 1.00 26.00  0  74  GLN   B N   1 
ATOM   2452 C  CA  . GLN   B  1 59  ? 22.534  1.359   -14.701 1.00 30.59  0  74  GLN   B CA  1 
ATOM   2453 C  C   . GLN   B  1 59  ? 21.440  2.411   -14.828 1.00 30.54  0  74  GLN   B C   1 
ATOM   2454 O  O   . GLN   B  1 59  ? 20.515  2.368   -13.988 1.00 27.90  0  74  GLN   B O   1 
ATOM   2455 C  CB  . GLN   B  1 59  ? 21.980  -0.073  -14.798 1.00 29.05  0  74  GLN   B CB  1 
ATOM   2456 C  CG  . GLN   B  1 59  ? 21.090  -0.326  -16.008 1.00 30.28  0  74  GLN   B CG  1 
ATOM   2457 C  CD  . GLN   B  1 59  ? 21.817  -0.117  -17.316 1.00 30.95  0  74  GLN   B CD  1 
ATOM   2458 O  OE1 . GLN   B  1 59  ? 22.912  -0.630  -17.525 1.00 28.59  0  74  GLN   B OE1 1 
ATOM   2459 N  NE2 . GLN   B  1 59  ? 21.231  0.684   -18.187 1.00 33.22  0  74  GLN   B NE2 1 
ATOM   2460 N  N   . LEU   B  1 60  ? 21.499  3.262   -15.860 1.00 27.98  0  75  LEU   B N   1 
ATOM   2461 C  CA  . LEU   B  1 60  ? 20.466  4.314   -16.086 1.00 30.03  0  75  LEU   B CA  1 
ATOM   2462 C  C   . LEU   B  1 60  ? 19.203  3.687   -16.649 1.00 29.54  0  75  LEU   B C   1 
ATOM   2463 O  O   . LEU   B  1 60  ? 19.202  2.446   -16.834 1.00 34.89  0  75  LEU   B O   1 
ATOM   2464 C  CB  . LEU   B  1 60  ? 21.017  5.406   -17.004 1.00 35.23  0  75  LEU   B CB  1 
ATOM   2465 C  CG  . LEU   B  1 60  ? 22.333  6.029   -16.530 1.00 38.18  0  75  LEU   B CG  1 
ATOM   2466 C  CD1 . LEU   B  1 60  ? 22.852  7.031   -17.560 1.00 40.87  0  75  LEU   B CD1 1 
ATOM   2467 C  CD2 . LEU   B  1 60  ? 22.178  6.667   -15.150 1.00 38.36  0  75  LEU   B CD2 1 
ATOM   2468 N  N   . ARG   B  1 61  ? 18.177  4.501   -16.939 1.00 31.05  0  76  ARG   B N   1 
ATOM   2469 C  CA  . ARG   B  1 61  ? 16.850  3.938   -17.257 1.00 34.12  0  76  ARG   B CA  1 
ATOM   2470 C  C   . ARG   B  1 61  ? 16.945  2.861   -18.347 1.00 34.78  0  76  ARG   B C   1 
ATOM   2471 O  O   . ARG   B  1 61  ? 17.528  3.118   -19.384 1.00 40.53  0  76  ARG   B O   1 
ATOM   2472 C  CB  . ARG   B  1 61  ? 15.823  4.955   -17.711 1.00 34.52  0  76  ARG   B CB  1 
ATOM   2473 C  CG  . ARG   B  1 61  ? 14.415  4.425   -17.441 1.00 34.65  0  76  ARG   B CG  1 
ATOM   2474 C  CD  . ARG   B  1 61  ? 13.514  5.082   -18.418 1.00 36.26  0  76  ARG   B CD  1 
ATOM   2475 N  NE  . ARG   B  1 61  ? 12.123  4.759   -18.276 1.00 34.15  0  76  ARG   B NE  1 
ATOM   2476 C  CZ  . ARG   B  1 61  ? 11.542  3.686   -18.764 1.00 33.36  0  76  ARG   B CZ  1 
ATOM   2477 N  NH1 . ARG   B  1 61  ? 12.258  2.736   -19.346 1.00 37.62  1  76  ARG   B NH1 1 
ATOM   2478 N  NH2 . ARG   B  1 61  ? 10.228  3.568   -18.666 1.00 30.05  0  76  ARG   B NH2 1 
ATOM   2479 N  N   . GLU   B  1 62  ? 16.428  1.677   -18.054 1.00 36.71  0  77  GLU   B N   1 
ATOM   2480 C  CA  . GLU   B  1 62  ? 16.233  0.592   -19.048 1.00 37.97  0  77  GLU   B CA  1 
ATOM   2481 C  C   . GLU   B  1 62  ? 14.845  0.001   -18.785 1.00 35.29  0  77  GLU   B C   1 
ATOM   2482 O  O   . GLU   B  1 62  ? 14.389  -0.056  -17.610 1.00 36.29  0  77  GLU   B O   1 
ATOM   2483 C  CB  . GLU   B  1 62  ? 17.436  -0.370  -19.099 1.00 39.02  0  77  GLU   B CB  1 
ATOM   2484 C  CG  . GLU   B  1 62  ? 17.728  -1.094  -17.835 1.00 38.50  0  77  GLU   B CG  1 
ATOM   2485 C  CD  . GLU   B  1 62  ? 18.819  -2.145  -17.891 1.00 35.93  0  77  GLU   B CD  1 
ATOM   2486 O  OE1 . GLU   B  1 62  ? 19.492  -2.313  -18.898 1.00 39.62  0  77  GLU   B OE1 1 
ATOM   2487 O  OE2 . GLU   B  1 62  ? 18.931  -2.818  -16.893 1.00 40.35  -1 77  GLU   B OE2 1 
ATOM   2488 N  N   . GLN   B  1 63  ? 14.161  -0.336  -19.861 1.00 28.09  0  78  GLN   B N   1 
ATOM   2489 C  CA  . GLN   B  1 63  ? 12.769  -0.854  -19.814 1.00 31.64  0  78  GLN   B CA  1 
ATOM   2490 C  C   . GLN   B  1 63  ? 12.767  -2.245  -19.157 1.00 32.34  0  78  GLN   B C   1 
ATOM   2491 O  O   . GLN   B  1 63  ? 11.844  -2.520  -18.386 1.00 34.15  0  78  GLN   B O   1 
ATOM   2492 C  CB  . GLN   B  1 63  ? 12.178  -0.894  -21.233 1.00 28.76  0  78  GLN   B CB  1 
ATOM   2493 C  CG  . GLN   B  1 63  ? 10.673  -1.112  -21.312 1.00 31.54  0  78  GLN   B CG  1 
ATOM   2494 C  CD  . GLN   B  1 63  ? 9.895   -0.105  -20.510 1.00 35.24  0  78  GLN   B CD  1 
ATOM   2495 O  OE1 . GLN   B  1 63  ? 10.306  1.058   -20.385 1.00 29.52  0  78  GLN   B OE1 1 
ATOM   2496 N  NE2 . GLN   B  1 63  ? 8.784   -0.557  -19.925 1.00 38.33  0  78  GLN   B NE2 1 
ATOM   2497 N  N   . HIS   B  1 64  ? 13.760  -3.086  -19.457 1.00 30.87  0  79  HIS   B N   1 
ATOM   2498 C  CA  . HIS   B  1 64  ? 13.889  -4.470  -18.940 1.00 30.21  0  79  HIS   B CA  1 
ATOM   2499 C  C   . HIS   B  1 64  ? 15.291  -4.636  -18.358 1.00 31.00  0  79  HIS   B C   1 
ATOM   2500 O  O   . HIS   B  1 64  ? 16.279  -4.362  -19.102 1.00 31.55  0  79  HIS   B O   1 
ATOM   2501 C  CB  . HIS   B  1 64  ? 13.602  -5.462  -20.064 1.00 30.97  0  79  HIS   B CB  1 
ATOM   2502 C  CG  . HIS   B  1 64  ? 12.227  -5.367  -20.621 1.00 28.90  0  79  HIS   B CG  1 
ATOM   2503 N  ND1 . HIS   B  1 64  ? 11.969  -4.711  -21.808 1.00 30.04  0  79  HIS   B ND1 1 
ATOM   2504 C  CD2 . HIS   B  1 64  ? 11.047  -5.870  -20.198 1.00 28.68  0  79  HIS   B CD2 1 
ATOM   2505 C  CE1 . HIS   B  1 64  ? 10.683  -4.781  -22.087 1.00 27.28  0  79  HIS   B CE1 1 
ATOM   2506 N  NE2 . HIS   B  1 64  ? 10.097  -5.521  -21.134 1.00 29.80  0  79  HIS   B NE2 1 
ATOM   2507 N  N   . LEU   B  1 65  ? 15.390  -5.025  -17.086 1.00 28.34  0  80  LEU   B N   1 
ATOM   2508 C  CA  . LEU   B  1 65  ? 16.709  -5.229  -16.428 1.00 28.05  0  80  LEU   B CA  1 
ATOM   2509 C  C   . LEU   B  1 65  ? 17.542  -6.236  -17.213 1.00 28.39  0  80  LEU   B C   1 
ATOM   2510 O  O   . LEU   B  1 65  ? 16.982  -7.238  -17.641 1.00 25.60  0  80  LEU   B O   1 
ATOM   2511 C  CB  . LEU   B  1 65  ? 16.591  -5.774  -15.004 1.00 28.75  0  80  LEU   B CB  1 
ATOM   2512 C  CG  . LEU   B  1 65  ? 16.251  -4.811  -13.882 1.00 31.27  0  80  LEU   B CG  1 
ATOM   2513 C  CD1 . LEU   B  1 65  ? 16.215  -5.601  -12.589 1.00 32.15  0  80  LEU   B CD1 1 
ATOM   2514 C  CD2 . LEU   B  1 65  ? 17.250  -3.669  -13.776 1.00 30.44  0  80  LEU   B CD2 1 
ATOM   2515 N  N   . TYR   B  1 66  ? 18.843  -5.973  -17.335 1.00 26.24  0  81  TYR   B N   1 
ATOM   2516 C  CA  . TYR   B  1 66  ? 19.903  -6.929  -17.764 1.00 32.33  0  81  TYR   B CA  1 
ATOM   2517 C  C   . TYR   B  1 66  ? 20.041  -7.018  -19.300 1.00 33.10  0  81  TYR   B C   1 
ATOM   2518 O  O   . TYR   B  1 66  ? 21.109  -7.410  -19.763 1.00 34.24  0  81  TYR   B O   1 
ATOM   2519 C  CB  . TYR   B  1 66  ? 19.680  -8.322  -17.151 1.00 29.49  0  81  TYR   B CB  1 
ATOM   2520 C  CG  . TYR   B  1 66  ? 19.520  -8.329  -15.649 1.00 26.66  0  81  TYR   B CG  1 
ATOM   2521 C  CD1 . TYR   B  1 66  ? 20.535  -7.887  -14.820 1.00 26.93  0  81  TYR   B CD1 1 
ATOM   2522 C  CD2 . TYR   B  1 66  ? 18.350  -8.755  -15.054 1.00 25.31  0  81  TYR   B CD2 1 
ATOM   2523 C  CE1 . TYR   B  1 66  ? 20.389  -7.851  -13.442 1.00 28.36  0  81  TYR   B CE1 1 
ATOM   2524 C  CE2 . TYR   B  1 66  ? 18.184  -8.731  -13.675 1.00 26.85  0  81  TYR   B CE2 1 
ATOM   2525 C  CZ  . TYR   B  1 66  ? 19.207  -8.272  -12.861 1.00 27.05  0  81  TYR   B CZ  1 
ATOM   2526 O  OH  . TYR   B  1 66  ? 19.064  -8.256  -11.499 1.00 23.62  0  81  TYR   B OH  1 
ATOM   2527 N  N   A TYR   B  1 67  ? 19.004  -6.632  -20.057 0.50 36.83  0  82  TYR   B N   1 
ATOM   2528 N  N   B TYR   B  1 67  ? 19.016  -6.636  -20.068 0.50 35.18  0  82  TYR   B N   1 
ATOM   2529 C  CA  A TYR   B  1 67  ? 18.881  -6.885  -21.518 0.50 40.20  0  82  TYR   B CA  1 
ATOM   2530 C  CA  B TYR   B  1 67  ? 18.936  -6.973  -21.516 0.50 37.48  0  82  TYR   B CA  1 
ATOM   2531 C  C   A TYR   B  1 67  ? 19.944  -6.096  -22.284 0.50 39.04  0  82  TYR   B C   1 
ATOM   2532 C  C   B TYR   B  1 67  ? 19.913  -6.092  -22.313 0.50 37.57  0  82  TYR   B C   1 
ATOM   2533 O  O   A TYR   B  1 67  ? 20.666  -6.707  -23.092 0.50 40.63  0  82  TYR   B O   1 
ATOM   2534 O  O   B TYR   B  1 67  ? 20.604  -6.674  -23.162 0.50 39.89  0  82  TYR   B O   1 
ATOM   2535 C  CB  A TYR   B  1 67  ? 17.491  -6.523  -22.046 0.50 42.88  0  82  TYR   B CB  1 
ATOM   2536 C  CB  B TYR   B  1 67  ? 17.472  -7.045  -21.956 0.50 37.55  0  82  TYR   B CB  1 
ATOM   2537 C  CG  A TYR   B  1 67  ? 17.350  -6.712  -23.536 0.50 43.14  0  82  TYR   B CG  1 
ATOM   2538 C  CG  B TYR   B  1 67  ? 16.798  -8.301  -21.456 0.50 34.22  0  82  TYR   B CG  1 
ATOM   2539 C  CD1 A TYR   B  1 67  ? 17.542  -7.955  -24.112 0.50 41.57  0  82  TYR   B CD1 1 
ATOM   2540 C  CD1 B TYR   B  1 67  ? 16.993  -9.520  -22.080 0.50 35.25  0  82  TYR   B CD1 1 
ATOM   2541 C  CD2 A TYR   B  1 67  ? 17.037  -5.653  -24.374 0.50 44.04  0  82  TYR   B CD2 1 
ATOM   2542 C  CD2 B TYR   B  1 67  ? 16.009  -8.286  -20.325 0.50 34.07  0  82  TYR   B CD2 1 
ATOM   2543 C  CE1 A TYR   B  1 67  ? 17.439  -8.146  -25.479 0.50 40.26  0  82  TYR   B CE1 1 
ATOM   2544 C  CE1 B TYR   B  1 67  ? 16.388  -10.679 -21.612 0.50 33.38  0  82  TYR   B CE1 1 
ATOM   2545 C  CE2 A TYR   B  1 67  ? 16.920  -5.830  -25.746 0.50 43.68  0  82  TYR   B CE2 1 
ATOM   2546 C  CE2 B TYR   B  1 67  ? 15.403  -9.430  -19.836 0.50 30.77  0  82  TYR   B CE2 1 
ATOM   2547 C  CZ  A TYR   B  1 67  ? 17.122  -7.083  -26.299 0.50 41.06  0  82  TYR   B CZ  1 
ATOM   2548 C  CZ  B TYR   B  1 67  ? 15.596  -10.634 -20.482 0.50 31.28  0  82  TYR   B CZ  1 
ATOM   2549 O  OH  A TYR   B  1 67  ? 16.995  -7.291  -27.638 0.50 42.42  0  82  TYR   B OH  1 
ATOM   2550 O  OH  B TYR   B  1 67  ? 14.994  -11.757 -20.002 0.50 29.35  0  82  TYR   B OH  1 
ATOM   2551 N  N   . GLN   B  1 68  ? 20.035  -4.787  -22.033 1.00 37.47  0  83  GLN   B N   1 
ATOM   2552 C  CA  . GLN   B  1 68  ? 21.024  -3.911  -22.733 1.00 44.65  0  83  GLN   B CA  1 
ATOM   2553 C  C   . GLN   B  1 68  ? 21.763  -3.058  -21.732 1.00 41.55  0  83  GLN   B C   1 
ATOM   2554 O  O   . GLN   B  1 68  ? 21.837  -1.850  -21.943 1.00 43.35  0  83  GLN   B O   1 
ATOM   2555 C  CB  . GLN   B  1 68  ? 20.395  -3.046  -23.824 1.00 47.78  0  83  GLN   B CB  1 
ATOM   2556 C  CG  . GLN   B  1 68  ? 19.928  -3.924  -24.975 1.00 55.58  0  83  GLN   B CG  1 
ATOM   2557 C  CD  . GLN   B  1 68  ? 19.442  -3.094  -26.131 1.00 61.29  0  83  GLN   B CD  1 
ATOM   2558 O  OE1 . GLN   B  1 68  ? 18.240  -2.879  -26.310 1.00 68.98  0  83  GLN   B OE1 1 
ATOM   2559 N  NE2 . GLN   B  1 68  ? 20.397  -2.580  -26.887 1.00 60.93  0  83  GLN   B NE2 1 
ATOM   2560 N  N   . ASP   B  1 69  ? 22.407  -3.708  -20.776 1.00 38.54  0  84  ASP   B N   1 
ATOM   2561 C  CA  . ASP   B  1 69  ? 23.135  -2.988  -19.705 1.00 37.65  0  84  ASP   B CA  1 
ATOM   2562 C  C   . ASP   B  1 69  ? 24.265  -2.147  -20.315 1.00 36.03  0  84  ASP   B C   1 
ATOM   2563 O  O   . ASP   B  1 69  ? 24.946  -2.622  -21.197 1.00 33.32  0  84  ASP   B O   1 
ATOM   2564 C  CB  . ASP   B  1 69  ? 23.678  -3.947  -18.644 1.00 35.27  0  84  ASP   B CB  1 
ATOM   2565 C  CG  . ASP   B  1 69  ? 22.644  -4.496  -17.681 1.00 33.89  0  84  ASP   B CG  1 
ATOM   2566 O  OD1 . ASP   B  1 69  ? 21.469  -4.045  -17.731 1.00 32.58  0  84  ASP   B OD1 1 
ATOM   2567 O  OD2 . ASP   B  1 69  ? 23.030  -5.389  -16.901 1.00 30.96  -1 84  ASP   B OD2 1 
ATOM   2568 N  N   . GLN   B  1 70  ? 24.460  -0.931  -19.803 1.00 34.75  0  85  GLN   B N   1 
ATOM   2569 C  CA  . GLN   B  1 70  ? 25.690  -0.101  -19.958 1.00 38.28  0  85  GLN   B CA  1 
ATOM   2570 C  C   . GLN   B  1 70  ? 26.078  0.395   -18.552 1.00 37.08  0  85  GLN   B C   1 
ATOM   2571 O  O   . GLN   B  1 70  ? 25.525  1.435   -18.104 1.00 34.78  0  85  GLN   B O   1 
ATOM   2572 C  CB  . GLN   B  1 70  ? 25.391  1.038   -20.933 1.00 41.88  0  85  GLN   B CB  1 
ATOM   2573 C  CG  . GLN   B  1 70  ? 24.686  0.550   -22.189 1.00 54.74  0  85  GLN   B CG  1 
ATOM   2574 C  CD  . GLN   B  1 70  ? 24.384  1.673   -23.151 1.00 60.25  0  85  GLN   B CD  1 
ATOM   2575 O  OE1 . GLN   B  1 70  ? 23.348  2.339   -23.061 1.00 54.36  0  85  GLN   B OE1 1 
ATOM   2576 N  NE2 . GLN   B  1 70  ? 25.282  1.858   -24.105 1.00 60.02  0  85  GLN   B NE2 1 
ATOM   2577 N  N   . LEU   B  1 71  ? 26.898  -0.382  -17.847 1.00 33.42  0  86  LEU   B N   1 
ATOM   2578 C  CA  . LEU   B  1 71  ? 27.099  -0.230  -16.394 1.00 36.70  0  86  LEU   B CA  1 
ATOM   2579 C  C   . LEU   B  1 71  ? 28.078  0.912   -16.152 1.00 40.61  0  86  LEU   B C   1 
ATOM   2580 O  O   . LEU   B  1 71  ? 29.099  0.963   -16.843 1.00 38.16  0  86  LEU   B O   1 
ATOM   2581 C  CB  . LEU   B  1 71  ? 27.583  -1.554  -15.798 1.00 36.49  0  86  LEU   B CB  1 
ATOM   2582 C  CG  . LEU   B  1 71  ? 26.581  -2.706  -15.863 1.00 37.12  0  86  LEU   B CG  1 
ATOM   2583 C  CD1 . LEU   B  1 71  ? 27.105  -3.872  -15.044 1.00 37.62  0  86  LEU   B CD1 1 
ATOM   2584 C  CD2 . LEU   B  1 71  ? 25.181  -2.314  -15.385 1.00 36.17  0  86  LEU   B CD2 1 
ATOM   2585 N  N   . LEU   B  1 72  ? 27.756  1.792   -15.200 1.00 36.98  0  87  LEU   B N   1 
ATOM   2586 C  CA  . LEU   B  1 72  ? 28.538  3.024   -14.914 1.00 36.11  0  87  LEU   B CA  1 
ATOM   2587 C  C   . LEU   B  1 72  ? 29.229  2.883   -13.562 1.00 34.64  0  87  LEU   B C   1 
ATOM   2588 O  O   . LEU   B  1 72  ? 28.600  2.535   -12.554 1.00 34.62  0  87  LEU   B O   1 
ATOM   2589 C  CB  . LEU   B  1 72  ? 27.613  4.239   -14.960 1.00 32.58  0  87  LEU   B CB  1 
ATOM   2590 C  CG  . LEU   B  1 72  ? 26.797  4.416   -16.239 1.00 34.65  0  87  LEU   B CG  1 
ATOM   2591 C  CD1 . LEU   B  1 72  ? 25.913  5.650   -16.132 1.00 37.93  0  87  LEU   B CD1 1 
ATOM   2592 C  CD2 . LEU   B  1 72  ? 27.677  4.531   -17.480 1.00 35.83  0  87  LEU   B CD2 1 
ATOM   2593 N  N   . PRO   B  1 73  ? 30.555  3.137   -13.491 1.00 37.78  0  88  PRO   B N   1 
ATOM   2594 C  CA  . PRO   B  1 73  ? 31.254  3.074   -12.212 1.00 37.49  0  88  PRO   B CA  1 
ATOM   2595 C  C   . PRO   B  1 73  ? 30.909  4.307   -11.346 1.00 34.29  0  88  PRO   B C   1 
ATOM   2596 O  O   . PRO   B  1 73  ? 30.470  5.336   -11.862 1.00 35.65  0  88  PRO   B O   1 
ATOM   2597 C  CB  . PRO   B  1 73  ? 32.724  2.942   -12.634 1.00 39.41  0  88  PRO   B CB  1 
ATOM   2598 C  CG  . PRO   B  1 73  ? 32.793  3.723   -13.946 1.00 41.04  0  88  PRO   B CG  1 
ATOM   2599 C  CD  . PRO   B  1 73  ? 31.448  3.512   -14.611 1.00 40.01  0  88  PRO   B CD  1 
ATOM   2600 N  N   . VAL   B  1 74  ? 31.018  4.131   -10.027 1.00 33.94  0  89  VAL   B N   1 
ATOM   2601 C  CA  . VAL   B  1 74  ? 30.711  5.150   -8.976  1.00 33.27  0  89  VAL   B CA  1 
ATOM   2602 C  C   . VAL   B  1 74  ? 32.052  5.618   -8.394  1.00 32.32  0  89  VAL   B C   1 
ATOM   2603 O  O   . VAL   B  1 74  ? 32.869  4.754   -8.077  1.00 32.06  0  89  VAL   B O   1 
ATOM   2604 C  CB  . VAL   B  1 74  ? 29.817  4.545   -7.885  1.00 30.92  0  89  VAL   B CB  1 
ATOM   2605 C  CG1 . VAL   B  1 74  ? 29.704  5.450   -6.661  1.00 32.42  0  89  VAL   B CG1 1 
ATOM   2606 C  CG2 . VAL   B  1 74  ? 28.435  4.225   -8.445  1.00 33.90  0  89  VAL   B CG2 1 
ATOM   2607 N  N   . SER   B  1 75  ? 32.269  6.915   -8.241  1.00 33.73  0  90  SER   B N   1 
ATOM   2608 C  CA  . SER   B  1 75  ? 33.531  7.477   -7.682  1.00 37.71  0  90  SER   B CA  1 
ATOM   2609 C  C   . SER   B  1 75  ? 33.430  7.612   -6.160  1.00 38.91  0  90  SER   B C   1 
ATOM   2610 O  O   . SER   B  1 75  ? 34.437  7.492   -5.520  1.00 40.96  0  90  SER   B O   1 
ATOM   2611 C  CB  . SER   B  1 75  ? 33.872  8.791   -8.289  1.00 41.93  0  90  SER   B CB  1 
ATOM   2612 O  OG  . SER   B  1 75  ? 32.782  9.698   -8.187  1.00 52.60  0  90  SER   B OG  1 
ATOM   2613 N  N   . ARG   B  1 76  ? 32.230  7.808   -5.612  1.00 36.07  0  91  ARG   B N   1 
ATOM   2614 C  CA  . ARG   B  1 76  ? 32.051  8.066   -4.170  1.00 37.17  0  91  ARG   B CA  1 
ATOM   2615 C  C   . ARG   B  1 76  ? 30.647  7.678   -3.722  1.00 30.69  0  91  ARG   B C   1 
ATOM   2616 O  O   . ARG   B  1 76  ? 29.693  8.013   -4.437  1.00 29.65  0  91  ARG   B O   1 
ATOM   2617 C  CB  . ARG   B  1 76  ? 32.261  9.554   -3.876  1.00 38.47  0  91  ARG   B CB  1 
ATOM   2618 C  CG  . ARG   B  1 76  ? 32.366  9.861   -2.400  1.00 41.83  0  91  ARG   B CG  1 
ATOM   2619 C  CD  . ARG   B  1 76  ? 32.674  11.333  -2.188  1.00 45.74  0  91  ARG   B CD  1 
ATOM   2620 N  NE  . ARG   B  1 76  ? 32.671  11.627  -0.756  1.00 51.29  0  91  ARG   B NE  1 
ATOM   2621 C  CZ  . ARG   B  1 76  ? 32.752  12.835  -0.222  1.00 51.92  0  91  ARG   B CZ  1 
ATOM   2622 N  NH1 . ARG   B  1 76  ? 32.843  13.911  -0.990  1.00 56.34  1  91  ARG   B NH1 1 
ATOM   2623 N  NH2 . ARG   B  1 76  ? 32.744  12.954  1.090   1.00 50.37  0  91  ARG   B NH2 1 
ATOM   2624 N  N   . ILE   B  1 77  ? 30.558  7.080   -2.537  1.00 28.96  0  92  ILE   B N   1 
ATOM   2625 C  CA  . ILE   B  1 77  ? 29.288  6.855   -1.793  1.00 31.35  0  92  ILE   B CA  1 
ATOM   2626 C  C   . ILE   B  1 77  ? 29.260  7.845   -0.627  1.00 28.77  0  92  ILE   B C   1 
ATOM   2627 O  O   . ILE   B  1 77  ? 30.179  7.805   0.203   1.00 28.25  0  92  ILE   B O   1 
ATOM   2628 C  CB  . ILE   B  1 77  ? 29.209  5.407   -1.286  1.00 29.72  0  92  ILE   B CB  1 
ATOM   2629 C  CG1 . ILE   B  1 77  ? 29.146  4.404   -2.439  1.00 34.11  0  92  ILE   B CG1 1 
ATOM   2630 C  CG2 . ILE   B  1 77  ? 28.002  5.243   -0.378  1.00 32.41  0  92  ILE   B CG2 1 
ATOM   2631 C  CD1 . ILE   B  1 77  ? 29.466  2.980   -2.035  1.00 35.79  0  92  ILE   B CD1 1 
ATOM   2632 N  N   . ILE   B  1 78  ? 28.226  8.676   -0.550  1.00 29.28  0  93  ILE   B N   1 
ATOM   2633 C  CA  . ILE   B  1 78  ? 28.027  9.596   0.613   1.00 30.95  0  93  ILE   B CA  1 
ATOM   2634 C  C   . ILE   B  1 78  ? 26.780  9.143   1.354   1.00 27.69  0  93  ILE   B C   1 
ATOM   2635 O  O   . ILE   B  1 78  ? 25.670  9.364   0.863   1.00 28.26  0  93  ILE   B O   1 
ATOM   2636 C  CB  . ILE   B  1 78  ? 27.941  11.083  0.227   1.00 32.22  0  93  ILE   B CB  1 
ATOM   2637 C  CG1 . ILE   B  1 78  ? 28.985  11.435  -0.843  1.00 37.14  0  93  ILE   B CG1 1 
ATOM   2638 C  CG2 . ILE   B  1 78  ? 28.059  11.920  1.496   1.00 29.28  0  93  ILE   B CG2 1 
ATOM   2639 C  CD1 . ILE   B  1 78  ? 29.019  12.917  -1.205  1.00 39.91  0  93  ILE   B CD1 1 
ATOM   2640 N  N   . VAL   B  1 79  ? 26.976  8.503   2.504   1.00 30.71  0  94  VAL   B N   1 
ATOM   2641 C  CA  . VAL   B  1 79  ? 25.839  8.076   3.359   1.00 28.78  0  94  VAL   B CA  1 
ATOM   2642 C  C   . VAL   B  1 79  ? 25.667  9.128   4.431   1.00 27.22  0  94  VAL   B C   1 
ATOM   2643 O  O   . VAL   B  1 79  ? 26.649  9.480   5.078   1.00 33.27  0  94  VAL   B O   1 
ATOM   2644 C  CB  . VAL   B  1 79  ? 26.087  6.661   3.907   1.00 29.63  0  94  VAL   B CB  1 
ATOM   2645 C  CG1 . VAL   B  1 79  ? 25.082  6.281   4.982   1.00 27.63  0  94  VAL   B CG1 1 
ATOM   2646 C  CG2 . VAL   B  1 79  ? 26.113  5.656   2.770   1.00 29.93  0  94  VAL   B CG2 1 
ATOM   2647 N  N   . HIS   B  1 80  ? 24.455  9.596   4.604   1.00 29.03  0  95  HIS   B N   1 
ATOM   2648 C  CA  . HIS   B  1 80  ? 24.146  10.570  5.672   1.00 28.92  0  95  HIS   B CA  1 
ATOM   2649 C  C   . HIS   B  1 80  ? 24.769  10.079  6.980   1.00 28.83  0  95  HIS   B C   1 
ATOM   2650 O  O   . HIS   B  1 80  ? 24.516  8.955   7.411   1.00 28.74  0  95  HIS   B O   1 
ATOM   2651 C  CB  . HIS   B  1 80  ? 22.639  10.759  5.832   1.00 26.36  0  95  HIS   B CB  1 
ATOM   2652 C  CG  . HIS   B  1 80  ? 22.334  12.057  6.493   1.00 31.94  0  95  HIS   B CG  1 
ATOM   2653 N  ND1 . HIS   B  1 80  ? 22.646  12.298  7.815   1.00 28.42  0  95  HIS   B ND1 1 
ATOM   2654 C  CD2 . HIS   B  1 80  ? 21.774  13.195  6.010   1.00 32.37  0  95  HIS   B CD2 1 
ATOM   2655 C  CE1 . HIS   B  1 80  ? 22.304  13.524  8.120   1.00 28.98  0  95  HIS   B CE1 1 
ATOM   2656 N  NE2 . HIS   B  1 80  ? 21.745  14.088  7.048   1.00 30.80  0  95  HIS   B NE2 1 
ATOM   2657 N  N   . PRO   B  1 81  ? 25.595  10.889  7.659   1.00 31.35  0  96  PRO   B N   1 
ATOM   2658 C  CA  . PRO   B  1 81  ? 26.242  10.446  8.893   1.00 31.46  0  96  PRO   B CA  1 
ATOM   2659 C  C   . PRO   B  1 81  ? 25.327  10.148  10.095  1.00 26.70  0  96  PRO   B C   1 
ATOM   2660 O  O   . PRO   B  1 81  ? 25.764  9.491   10.993  1.00 25.77  0  96  PRO   B O   1 
ATOM   2661 C  CB  . PRO   B  1 81  ? 27.213  11.602  9.207   1.00 35.40  0  96  PRO   B CB  1 
ATOM   2662 C  CG  . PRO   B  1 81  ? 26.566  12.809  8.571   1.00 38.24  0  96  PRO   B CG  1 
ATOM   2663 C  CD  . PRO   B  1 81  ? 25.967  12.269  7.285   1.00 36.90  0  96  PRO   B CD  1 
ATOM   2664 N  N   . GLN   B  1 82  ? 24.077  10.584  10.084  1.00 26.65  0  97  GLN   B N   1 
ATOM   2665 C  CA  . GLN   B  1 82  ? 23.106  10.271  11.160  1.00 28.35  0  97  GLN   B CA  1 
ATOM   2666 C  C   . GLN   B  1 82  ? 22.427  8.933   10.873  1.00 30.83  0  97  GLN   B C   1 
ATOM   2667 O  O   . GLN   B  1 82  ? 21.650  8.526   11.731  1.00 31.84  0  97  GLN   B O   1 
ATOM   2668 C  CB  . GLN   B  1 82  ? 22.086  11.411  11.346  1.00 30.91  0  97  GLN   B CB  1 
ATOM   2669 C  CG  . GLN   B  1 82  ? 22.791  12.732  11.706  1.00 33.11  0  97  GLN   B CG  1 
ATOM   2670 C  CD  . GLN   B  1 82  ? 21.979  14.005  11.722  1.00 34.67  0  97  GLN   B CD  1 
ATOM   2671 O  OE1 . GLN   B  1 82  ? 22.511  15.059  12.047  1.00 41.59  0  97  GLN   B OE1 1 
ATOM   2672 N  NE2 . GLN   B  1 82  ? 20.702  13.928  11.407  1.00 38.04  0  97  GLN   B NE2 1 
ATOM   2673 N  N   . PHE   B  1 83  ? 22.707  8.253   9.750   1.00 27.13  0  98  PHE   B N   1 
ATOM   2674 C  CA  . PHE   B  1 83  ? 22.074  6.947   9.423   1.00 25.19  0  98  PHE   B CA  1 
ATOM   2675 C  C   . PHE   B  1 83  ? 22.717  5.789   10.198  1.00 24.07  0  98  PHE   B C   1 
ATOM   2676 O  O   . PHE   B  1 83  ? 23.962  5.578   10.158  1.00 21.61  0  98  PHE   B O   1 
ATOM   2677 C  CB  . PHE   B  1 83  ? 22.191  6.587   7.944   1.00 25.59  0  98  PHE   B CB  1 
ATOM   2678 C  CG  . PHE   B  1 83  ? 21.565  5.256   7.653   1.00 24.39  0  98  PHE   B CG  1 
ATOM   2679 C  CD1 . PHE   B  1 83  ? 20.176  5.108   7.710   1.00 23.66  0  98  PHE   B CD1 1 
ATOM   2680 C  CD2 . PHE   B  1 83  ? 22.353  4.146   7.395   1.00 25.29  0  98  PHE   B CD2 1 
ATOM   2681 C  CE1 . PHE   B  1 83  ? 19.586  3.889   7.421   1.00 24.62  0  98  PHE   B CE1 1 
ATOM   2682 C  CE2 . PHE   B  1 83  ? 21.761  2.923   7.092   1.00 22.24  0  98  PHE   B CE2 1 
ATOM   2683 C  CZ  . PHE   B  1 83  ? 20.387  2.790   7.142   1.00 23.02  0  98  PHE   B CZ  1 
ATOM   2684 N  N   . TYR   B  1 84  ? 21.869  4.956   10.795  1.00 25.13  0  99  TYR   B N   1 
ATOM   2685 C  CA  . TYR   B  1 84  ? 22.260  3.622   11.305  1.00 25.03  0  99  TYR   B CA  1 
ATOM   2686 C  C   . TYR   B  1 84  ? 21.197  2.579   10.871  1.00 26.31  0  99  TYR   B C   1 
ATOM   2687 O  O   . TYR   B  1 84  ? 21.610  1.519   10.402  1.00 24.25  0  99  TYR   B O   1 
ATOM   2688 C  CB  . TYR   B  1 84  ? 22.566  3.661   12.820  1.00 24.34  0  99  TYR   B CB  1 
ATOM   2689 C  CG  . TYR   B  1 84  ? 23.119  2.331   13.259  1.00 23.98  0  99  TYR   B CG  1 
ATOM   2690 C  CD1 . TYR   B  1 84  ? 24.322  1.855   12.760  1.00 24.37  0  99  TYR   B CD1 1 
ATOM   2691 C  CD2 . TYR   B  1 84  ? 22.354  1.470   14.037  1.00 27.44  0  99  TYR   B CD2 1 
ATOM   2692 C  CE1 . TYR   B  1 84  ? 24.774  0.576   13.055  1.00 23.78  0  99  TYR   B CE1 1 
ATOM   2693 C  CE2 . TYR   B  1 84  ? 22.782  0.188   14.327  1.00 25.73  0  99  TYR   B CE2 1 
ATOM   2694 C  CZ  . TYR   B  1 84  ? 24.000  -0.261  13.852  1.00 26.91  0  99  TYR   B CZ  1 
ATOM   2695 O  OH  . TYR   B  1 84  ? 24.400  -1.540  14.135  1.00 27.69  0  99  TYR   B OH  1 
ATOM   2696 N  N   . THR   B  1 85  ? 19.899  2.850   11.035  1.00 22.65  0  100 THR   B N   1 
ATOM   2697 C  CA  . THR   B  1 85  ? 18.802  1.988   10.538  1.00 25.24  0  100 THR   B CA  1 
ATOM   2698 C  C   . THR   B  1 85  ? 17.705  2.884   9.953   1.00 24.25  0  100 THR   B C   1 
ATOM   2699 O  O   . THR   B  1 85  ? 17.571  4.072   10.344  1.00 21.63  0  100 THR   B O   1 
ATOM   2700 C  CB  . THR   B  1 85  ? 18.194  1.082   11.639  1.00 25.42  0  100 THR   B CB  1 
ATOM   2701 O  OG1 . THR   B  1 85  ? 17.348  1.858   12.491  1.00 26.06  0  100 THR   B OG1 1 
ATOM   2702 C  CG2 . THR   B  1 85  ? 19.208  0.404   12.527  1.00 26.04  0  100 THR   B CG2 1 
ATOM   2703 N  N   . ALA   B  1 86  ? 16.905  2.311   9.072   1.00 24.47  0  101 ALA   B N   1 
ATOM   2704 C  CA  . ALA   B  1 86  ? 15.786  2.998   8.401   1.00 24.50  0  101 ALA   B CA  1 
ATOM   2705 C  C   . ALA   B  1 86  ? 14.764  3.451   9.433   1.00 28.41  0  101 ALA   B C   1 
ATOM   2706 O  O   . ALA   B  1 86  ? 14.194  4.550   9.219   1.00 27.65  0  101 ALA   B O   1 
ATOM   2707 C  CB  . ALA   B  1 86  ? 15.174  2.090   7.377   1.00 26.93  0  101 ALA   B CB  1 
ATOM   2708 N  N   . GLN   B  1 87  ? 14.500  2.657   10.493  1.00 27.41  0  102 GLN   B N   1 
ATOM   2709 C  CA  . GLN   B  1 87  ? 13.420  3.033   11.450  1.00 26.83  0  102 GLN   B CA  1 
ATOM   2710 C  C   . GLN   B  1 87  ? 13.842  4.224   12.327  1.00 25.07  0  102 GLN   B C   1 
ATOM   2711 O  O   . GLN   B  1 87  ? 12.937  4.921   12.831  1.00 24.03  0  102 GLN   B O   1 
ATOM   2712 C  CB  . GLN   B  1 87  ? 13.012  1.845   12.309  1.00 28.86  0  102 GLN   B CB  1 
ATOM   2713 C  CG  . GLN   B  1 87  ? 12.382  0.726   11.504  1.00 30.79  0  102 GLN   B CG  1 
ATOM   2714 C  CD  . GLN   B  1 87  ? 13.329  -0.308  10.938  1.00 35.23  0  102 GLN   B CD  1 
ATOM   2715 O  OE1 . GLN   B  1 87  ? 14.528  -0.367  11.241  1.00 33.10  0  102 GLN   B OE1 1 
ATOM   2716 N  NE2 . GLN   B  1 87  ? 12.797  -1.053  9.991   1.00 48.87  0  102 GLN   B NE2 1 
ATOM   2717 N  N   . ILE   B  1 88  ? 15.143  4.404   12.546  1.00 24.43  0  103 ILE   B N   1 
ATOM   2718 C  CA  . ILE   B  1 88  ? 15.694  5.586   13.261  1.00 26.59  0  103 ILE   B CA  1 
ATOM   2719 C  C   . ILE   B  1 88  ? 15.619  6.797   12.319  1.00 27.17  0  103 ILE   B C   1 
ATOM   2720 O  O   . ILE   B  1 88  ? 15.244  7.881   12.791  1.00 26.63  0  103 ILE   B O   1 
ATOM   2721 C  CB  . ILE   B  1 88  ? 17.119  5.299   13.767  1.00 28.78  0  103 ILE   B CB  1 
ATOM   2722 C  CG1 . ILE   B  1 88  ? 17.134  4.169   14.808  1.00 27.07  0  103 ILE   B CG1 1 
ATOM   2723 C  CG2 . ILE   B  1 88  ? 17.708  6.588   14.335  1.00 28.52  0  103 ILE   B CG2 1 
ATOM   2724 C  CD1 . ILE   B  1 88  ? 18.506  3.665   15.191  1.00 29.17  0  103 ILE   B CD1 1 
ATOM   2725 N  N   . GLY   B  1 89  ? 16.018  6.639   11.044  1.00 25.77  0  104 GLY   B N   1 
ATOM   2726 C  CA  . GLY   B  1 89  ? 15.864  7.667   9.990   1.00 24.84  0  104 GLY   B CA  1 
ATOM   2727 C  C   . GLY   B  1 89  ? 17.176  8.080   9.375   1.00 21.92  0  104 GLY   B C   1 
ATOM   2728 O  O   . GLY   B  1 89  ? 18.191  7.350   9.506   1.00 24.62  0  104 GLY   B O   1 
ATOM   2729 N  N   . ALA   B  1 90  ? 17.180  9.241   8.723   1.00 26.43  0  105 ALA   B N   1 
ATOM   2730 C  CA  . ALA   B  1 90  ? 18.292  9.729   7.879   1.00 25.31  0  105 ALA   B CA  1 
ATOM   2731 C  C   . ALA   B  1 90  ? 18.647  8.657   6.819   1.00 24.50  0  105 ALA   B C   1 
ATOM   2732 O  O   . ALA   B  1 90  ? 19.859  8.490   6.505   1.00 24.96  0  105 ALA   B O   1 
ATOM   2733 C  CB  . ALA   B  1 90  ? 19.454  10.080  8.764   1.00 25.80  0  105 ALA   B CB  1 
ATOM   2734 N  N   . ASP   B  1 91  ? 17.631  7.967   6.280   1.00 23.07  0  106 ASP   B N   1 
ATOM   2735 C  CA  . ASP   B  1 91  ? 17.821  6.882   5.285   1.00 22.20  0  106 ASP   B CA  1 
ATOM   2736 C  C   . ASP   B  1 91  ? 18.006  7.512   3.878   1.00 22.53  0  106 ASP   B C   1 
ATOM   2737 O  O   . ASP   B  1 91  ? 17.058  7.488   3.032   1.00 24.21  0  106 ASP   B O   1 
ATOM   2738 C  CB  . ASP   B  1 91  ? 16.654  5.889   5.340   1.00 22.52  0  106 ASP   B CB  1 
ATOM   2739 C  CG  . ASP   B  1 91  ? 16.965  4.639   4.519   1.00 24.04  0  106 ASP   B CG  1 
ATOM   2740 O  OD1 . ASP   B  1 91  ? 18.134  4.502   4.090   1.00 21.21  0  106 ASP   B OD1 1 
ATOM   2741 O  OD2 . ASP   B  1 91  ? 16.039  3.845   4.291   1.00 25.97  -1 106 ASP   B OD2 1 
ATOM   2742 N  N   . ILE   B  1 92  ? 19.185  8.055   3.623   1.00 22.27  0  107 ILE   B N   1 
ATOM   2743 C  CA  . ILE   B  1 92  ? 19.445  8.845   2.388   1.00 24.97  0  107 ILE   B CA  1 
ATOM   2744 C  C   . ILE   B  1 92  ? 20.937  8.826   2.124   1.00 24.45  0  107 ILE   B C   1 
ATOM   2745 O  O   . ILE   B  1 92  ? 21.707  8.833   3.093   1.00 24.82  0  107 ILE   B O   1 
ATOM   2746 C  CB  . ILE   B  1 92  ? 18.877  10.271  2.481   1.00 26.16  0  107 ILE   B CB  1 
ATOM   2747 C  CG1 . ILE   B  1 92  ? 18.810  10.931  1.106   1.00 28.00  0  107 ILE   B CG1 1 
ATOM   2748 C  CG2 . ILE   B  1 92  ? 19.633  11.118  3.507   1.00 26.68  0  107 ILE   B CG2 1 
ATOM   2749 C  CD1 . ILE   B  1 92  ? 17.956  12.176  1.107   1.00 31.30  0  107 ILE   B CD1 1 
ATOM   2750 N  N   . ALA   B  1 93  ? 21.293  8.712   0.841   1.00 27.02  0  108 ALA   B N   1 
ATOM   2751 C  CA  . ALA   B  1 93  ? 22.671  8.597   0.351   1.00 27.51  0  108 ALA   B CA  1 
ATOM   2752 C  C   . ALA   B  1 93  ? 22.771  9.161   -1.062  1.00 26.92  0  108 ALA   B C   1 
ATOM   2753 O  O   . ALA   B  1 93  ? 21.739  9.246   -1.766  1.00 25.56  0  108 ALA   B O   1 
ATOM   2754 C  CB  . ALA   B  1 93  ? 23.154  7.159   0.400   1.00 29.13  0  108 ALA   B CB  1 
ATOM   2755 N  N   . LEU   B  1 94  ? 24.002  9.484   -1.432  1.00 26.77  0  109 LEU   B N   1 
ATOM   2756 C  CA  . LEU   B  1 94  ? 24.364  10.056  -2.753  1.00 28.59  0  109 LEU   B CA  1 
ATOM   2757 C  C   . LEU   B  1 94  ? 25.453  9.185   -3.353  1.00 26.73  0  109 LEU   B C   1 
ATOM   2758 O  O   . LEU   B  1 94  ? 26.386  8.817   -2.617  1.00 27.53  0  109 LEU   B O   1 
ATOM   2759 C  CB  . LEU   B  1 94  ? 24.843  11.502  -2.578  1.00 28.23  0  109 LEU   B CB  1 
ATOM   2760 C  CG  . LEU   B  1 94  ? 23.736  12.487  -2.201  1.00 29.25  0  109 LEU   B CG  1 
ATOM   2761 C  CD1 . LEU   B  1 94  ? 24.308  13.816  -1.700  1.00 32.73  0  109 LEU   B CD1 1 
ATOM   2762 C  CD2 . LEU   B  1 94  ? 22.782  12.705  -3.375  1.00 31.37  0  109 LEU   B CD2 1 
ATOM   2763 N  N   . LEU   B  1 95  ? 25.293  8.844   -4.634  1.00 26.64  0  110 LEU   B N   1 
ATOM   2764 C  CA  . LEU   B  1 95  ? 26.368  8.231   -5.437  1.00 27.28  0  110 LEU   B CA  1 
ATOM   2765 C  C   . LEU   B  1 95  ? 26.854  9.274   -6.446  1.00 27.92  0  110 LEU   B C   1 
ATOM   2766 O  O   . LEU   B  1 95  ? 26.033  9.804   -7.233  1.00 26.75  0  110 LEU   B O   1 
ATOM   2767 C  CB  . LEU   B  1 95  ? 25.828  6.996   -6.163  1.00 28.77  0  110 LEU   B CB  1 
ATOM   2768 C  CG  . LEU   B  1 95  ? 25.035  5.984   -5.345  1.00 29.43  0  110 LEU   B CG  1 
ATOM   2769 C  CD1 . LEU   B  1 95  ? 24.621  4.815   -6.269  1.00 31.21  0  110 LEU   B CD1 1 
ATOM   2770 C  CD2 . LEU   B  1 95  ? 25.873  5.482   -4.160  1.00 30.51  0  110 LEU   B CD2 1 
ATOM   2771 N  N   . GLU   B  1 96  ? 28.141  9.547   -6.405  1.00 27.40  0  111 GLU   B N   1 
ATOM   2772 C  CA  . GLU   B  1 96  ? 28.844  10.385  -7.395  1.00 29.53  0  111 GLU   B CA  1 
ATOM   2773 C  C   . GLU   B  1 96  ? 29.366  9.489   -8.514  1.00 29.65  0  111 GLU   B C   1 
ATOM   2774 O  O   . GLU   B  1 96  ? 30.189  8.577   -8.232  1.00 29.35  0  111 GLU   B O   1 
ATOM   2775 C  CB  . GLU   B  1 96  ? 29.975  11.143  -6.702  1.00 31.36  0  111 GLU   B CB  1 
ATOM   2776 C  CG  . GLU   B  1 96  ? 30.522  12.269  -7.558  1.00 34.92  0  111 GLU   B CG  1 
ATOM   2777 C  CD  . GLU   B  1 96  ? 31.650  13.088  -6.945  1.00 38.79  0  111 GLU   B CD  1 
ATOM   2778 O  OE1 . GLU   B  1 96  ? 32.347  12.603  -6.044  1.00 39.44  0  111 GLU   B OE1 1 
ATOM   2779 O  OE2 . GLU   B  1 96  ? 31.852  14.197  -7.411  1.00 47.84  -1 111 GLU   B OE2 1 
ATOM   2780 N  N   . LEU   B  1 97  ? 28.888  9.715   -9.735  1.00 31.72  0  112 LEU   B N   1 
ATOM   2781 C  CA  . LEU   B  1 97  ? 29.353  8.965   -10.925 1.00 30.52  0  112 LEU   B CA  1 
ATOM   2782 C  C   . LEU   B  1 97  ? 30.746  9.467   -11.290 1.00 34.05  0  112 LEU   B C   1 
ATOM   2783 O  O   . LEU   B  1 97  ? 31.038  10.629  -11.025 1.00 31.90  0  112 LEU   B O   1 
ATOM   2784 C  CB  . LEU   B  1 97  ? 28.349  9.154   -12.064 1.00 30.08  0  112 LEU   B CB  1 
ATOM   2785 C  CG  . LEU   B  1 97  ? 26.911  8.719   -11.727 1.00 33.73  0  112 LEU   B CG  1 
ATOM   2786 C  CD1 . LEU   B  1 97  ? 25.933  9.054   -12.850 1.00 35.12  0  112 LEU   B CD1 1 
ATOM   2787 C  CD2 . LEU   B  1 97  ? 26.854  7.242   -11.391 1.00 31.90  0  112 LEU   B CD2 1 
ATOM   2788 N  N   . GLU   B  1 98  ? 31.520  8.613   -11.956 1.00 38.25  0  113 GLU   B N   1 
ATOM   2789 C  CA  A GLU   B  1 98  ? 32.895  8.913   -12.438 0.50 42.13  0  113 GLU   B CA  1 
ATOM   2790 C  CA  B GLU   B  1 98  ? 32.893  8.913   -12.441 0.50 41.82  0  113 GLU   B CA  1 
ATOM   2791 C  C   . GLU   B  1 98  ? 32.828  9.933   -13.582 1.00 39.17  0  113 GLU   B C   1 
ATOM   2792 O  O   . GLU   B  1 98  ? 33.816  10.572  -13.806 1.00 39.28  0  113 GLU   B O   1 
ATOM   2793 C  CB  A GLU   B  1 98  ? 33.605  7.631   -12.897 0.50 44.27  0  113 GLU   B CB  1 
ATOM   2794 C  CB  B GLU   B  1 98  ? 33.582  7.629   -12.914 0.50 43.44  0  113 GLU   B CB  1 
ATOM   2795 C  CG  A GLU   B  1 98  ? 35.104  7.794   -13.069 0.50 47.88  0  113 GLU   B CG  1 
ATOM   2796 C  CG  B GLU   B  1 98  ? 33.731  6.600   -11.809 0.50 47.25  0  113 GLU   B CG  1 
ATOM   2797 C  CD  A GLU   B  1 98  ? 35.949  6.532   -12.946 0.50 53.29  0  113 GLU   B CD  1 
ATOM   2798 C  CD  B GLU   B  1 98  ? 35.161  6.375   -11.382 0.50 48.39  0  113 GLU   B CD  1 
ATOM   2799 O  OE1 A GLU   B  1 98  ? 35.522  5.486   -13.481 0.50 53.91  0  113 GLU   B OE1 1 
ATOM   2800 O  OE1 B GLU   B  1 98  ? 36.012  7.148   -11.839 0.50 54.29  0  113 GLU   B OE1 1 
ATOM   2801 O  OE2 A GLU   B  1 98  ? 37.051  6.594   -12.318 0.50 52.33  -1 113 GLU   B OE2 1 
ATOM   2802 O  OE2 B GLU   B  1 98  ? 35.409  5.428   -10.610 0.50 50.57  -1 113 GLU   B OE2 1 
ATOM   2803 N  N   . GLU   B  1 99  ? 31.695  10.016  -14.277 1.00 36.99  0  114 GLU   B N   1 
ATOM   2804 C  CA  . GLU   B  1 99  ? 31.468  10.926  -15.424 1.00 45.57  0  114 GLU   B CA  1 
ATOM   2805 C  C   . GLU   B  1 99  ? 30.061  11.485  -15.381 1.00 41.12  0  114 GLU   B C   1 
ATOM   2806 O  O   . GLU   B  1 99  ? 29.127  10.805  -14.977 1.00 35.01  0  114 GLU   B O   1 
ATOM   2807 C  CB  . GLU   B  1 99  ? 31.559  10.203  -16.778 1.00 48.63  0  114 GLU   B CB  1 
ATOM   2808 C  CG  . GLU   B  1 99  ? 32.917  9.576   -17.045 1.00 51.69  0  114 GLU   B CG  1 
ATOM   2809 C  CD  . GLU   B  1 99  ? 34.042  10.564  -17.330 1.00 54.81  0  114 GLU   B CD  1 
ATOM   2810 O  OE1 . GLU   B  1 99  ? 33.756  11.756  -17.577 1.00 52.04  0  114 GLU   B OE1 1 
ATOM   2811 O  OE2 . GLU   B  1 99  ? 35.207  10.133  -17.327 1.00 66.90  -1 114 GLU   B OE2 1 
ATOM   2812 N  N   . PRO   B  1 100 ? 29.879  12.730  -15.854 1.00 40.13  0  115 PRO   B N   1 
ATOM   2813 C  CA  . PRO   B  1 100 ? 28.542  13.297  -15.998 1.00 43.73  0  115 PRO   B CA  1 
ATOM   2814 C  C   . PRO   B  1 100 ? 27.869  12.510  -17.130 1.00 42.79  0  115 PRO   B C   1 
ATOM   2815 O  O   . PRO   B  1 100 ? 28.527  12.052  -18.008 1.00 50.47  0  115 PRO   B O   1 
ATOM   2816 C  CB  . PRO   B  1 100 ? 28.776  14.773  -16.348 1.00 43.56  0  115 PRO   B CB  1 
ATOM   2817 C  CG  . PRO   B  1 100 ? 30.180  14.797  -16.940 1.00 43.33  0  115 PRO   B CG  1 
ATOM   2818 C  CD  . PRO   B  1 100 ? 30.941  13.638  -16.314 1.00 43.74  0  115 PRO   B CD  1 
ATOM   2819 N  N   . VAL   B  1 101 ? 26.580  12.280  -17.008 1.00 41.04  0  116 VAL   B N   1 
ATOM   2820 C  CA  . VAL   B  1 101 ? 25.749  11.613  -18.040 1.00 41.66  0  116 VAL   B CA  1 
ATOM   2821 C  C   . VAL   B  1 101 ? 25.400  12.719  -19.054 1.00 44.41  0  116 VAL   B C   1 
ATOM   2822 O  O   . VAL   B  1 101 ? 25.169  13.914  -18.620 1.00 41.64  0  116 VAL   B O   1 
ATOM   2823 C  CB  . VAL   B  1 101 ? 24.504  10.964  -17.389 1.00 39.98  0  116 VAL   B CB  1 
ATOM   2824 C  CG1 . VAL   B  1 101 ? 23.470  10.494  -18.402 1.00 43.05  0  116 VAL   B CG1 1 
ATOM   2825 C  CG2 . VAL   B  1 101 ? 24.874  9.836   -16.432 1.00 42.22  0  116 VAL   B CG2 1 
ATOM   2826 N  N   . LYS   B  1 102 ? 25.427  12.372  -20.343 1.00 45.53  0  117 LYS   B N   1 
ATOM   2827 C  CA  . LYS   B  1 102 ? 24.889  13.211  -21.453 1.00 48.31  0  117 LYS   B CA  1 
ATOM   2828 C  C   . LYS   B  1 102 ? 23.368  13.037  -21.463 1.00 47.07  0  117 LYS   B C   1 
ATOM   2829 O  O   . LYS   B  1 102 ? 22.930  11.955  -21.831 1.00 52.87  0  117 LYS   B O   1 
ATOM   2830 C  CB  . LYS   B  1 102 ? 25.523  12.800  -22.794 1.00 48.59  0  117 LYS   B CB  1 
ATOM   2831 C  CG  . LYS   B  1 102 ? 25.164  13.660  -24.002 1.00 49.17  0  117 LYS   B CG  1 
ATOM   2832 C  CD  . LYS   B  1 102 ? 25.783  13.162  -25.296 0.00 51.21  0  117 LYS   B CD  1 
ATOM   2833 C  CE  . LYS   B  1 102 ? 25.362  13.985  -26.496 0.00 51.12  0  117 LYS   B CE  1 
ATOM   2834 N  NZ  . LYS   B  1 102 ? 25.946  13.460  -27.752 0.00 51.11  1  117 LYS   B NZ  1 
ATOM   2835 N  N   . VAL   B  1 103 ? 22.586  14.034  -21.016 1.00 46.00  0  118 VAL   B N   1 
ATOM   2836 C  CA  . VAL   B  1 103 ? 21.113  13.867  -20.819 1.00 46.64  0  118 VAL   B CA  1 
ATOM   2837 C  C   . VAL   B  1 103 ? 20.397  13.896  -22.185 1.00 52.15  0  118 VAL   B C   1 
ATOM   2838 O  O   . VAL   B  1 103 ? 20.974  14.395  -23.173 1.00 50.95  0  118 VAL   B O   1 
ATOM   2839 C  CB  . VAL   B  1 103 ? 20.540  14.887  -19.813 1.00 47.49  0  118 VAL   B CB  1 
ATOM   2840 C  CG1 . VAL   B  1 103 ? 21.130  14.700  -18.411 1.00 45.32  0  118 VAL   B CG1 1 
ATOM   2841 C  CG2 . VAL   B  1 103 ? 20.672  16.336  -20.260 1.00 49.02  0  118 VAL   B CG2 1 
ATOM   2842 N  N   . SER   B  1 104 ? 19.207  13.316  -22.230 1.00 46.78  0  119 SER   B N   1 
ATOM   2843 C  CA  . SER   B  1 104 ? 18.375  13.171  -23.444 1.00 50.90  0  119 SER   B CA  1 
ATOM   2844 C  C   . SER   B  1 104 ? 16.913  13.152  -23.015 1.00 53.91  0  119 SER   B C   1 
ATOM   2845 O  O   . SER   B  1 104 ? 16.662  13.207  -21.791 1.00 56.61  0  119 SER   B O   1 
ATOM   2846 C  CB  . SER   B  1 104 ? 18.777  11.932  -24.198 1.00 47.97  0  119 SER   B CB  1 
ATOM   2847 O  OG  . SER   B  1 104 ? 18.521  10.758  -23.442 1.00 43.45  0  119 SER   B OG  1 
ATOM   2848 N  N   . SER   B  1 105 ? 15.980  13.069  -23.959 1.00 50.92  0  120 SER   B N   1 
ATOM   2849 C  CA  . SER   B  1 105 ? 14.541  12.982  -23.608 1.00 56.32  0  120 SER   B CA  1 
ATOM   2850 C  C   . SER   B  1 105 ? 14.261  11.631  -22.920 1.00 48.54  0  120 SER   B C   1 
ATOM   2851 O  O   . SER   B  1 105 ? 13.381  11.607  -22.049 1.00 56.35  0  120 SER   B O   1 
ATOM   2852 C  CB  . SER   B  1 105 ? 13.652  13.245  -24.806 1.00 54.58  0  120 SER   B CB  1 
ATOM   2853 O  OG  . SER   B  1 105 ? 13.641  12.128  -25.673 1.00 58.87  0  120 SER   B OG  1 
ATOM   2854 N  N   . HIS   B  1 106 ? 15.039  10.581  -23.221 1.00 47.56  0  121 HIS   B N   1 
ATOM   2855 C  CA  . HIS   B  1 106 ? 14.857  9.220   -22.656 1.00 51.89  0  121 HIS   B CA  1 
ATOM   2856 C  C   . HIS   B  1 106 ? 15.525  9.077   -21.267 1.00 52.25  0  121 HIS   B C   1 
ATOM   2857 O  O   . HIS   B  1 106 ? 15.013  8.289   -20.452 1.00 47.95  0  121 HIS   B O   1 
ATOM   2858 C  CB  . HIS   B  1 106 ? 15.353  8.156   -23.651 1.00 59.34  0  121 HIS   B CB  1 
ATOM   2859 C  CG  . HIS   B  1 106 ? 15.015  6.767   -23.229 1.00 66.97  0  121 HIS   B CG  1 
ATOM   2860 N  ND1 . HIS   B  1 106 ? 13.711  6.279   -23.265 1.00 66.11  0  121 HIS   B ND1 1 
ATOM   2861 C  CD2 . HIS   B  1 106 ? 15.783  5.790   -22.693 1.00 71.10  0  121 HIS   B CD2 1 
ATOM   2862 C  CE1 . HIS   B  1 106 ? 13.695  5.051   -22.790 1.00 67.57  0  121 HIS   B CE1 1 
ATOM   2863 N  NE2 . HIS   B  1 106 ? 14.960  4.729   -22.436 1.00 77.98  0  121 HIS   B NE2 1 
ATOM   2864 N  N   . VAL   B  1 107 ? 16.672  9.720   -21.033 1.00 45.14  0  122 VAL   B N   1 
ATOM   2865 C  CA  . VAL   B  1 107 ? 17.432  9.633   -19.754 1.00 48.64  0  122 VAL   B CA  1 
ATOM   2866 C  C   . VAL   B  1 107 ? 17.788  11.061  -19.320 1.00 47.84  0  122 VAL   B C   1 
ATOM   2867 O  O   . VAL   B  1 107 ? 18.667  11.695  -19.966 1.00 46.33  0  122 VAL   B O   1 
ATOM   2868 C  CB  . VAL   B  1 107 ? 18.636  8.670   -19.833 1.00 51.22  0  122 VAL   B CB  1 
ATOM   2869 C  CG1 . VAL   B  1 107 ? 19.436  8.783   -21.120 1.00 62.14  0  122 VAL   B CG1 1 
ATOM   2870 C  CG2 . VAL   B  1 107 ? 19.556  8.774   -18.623 1.00 52.34  0  122 VAL   B CG2 1 
ATOM   2871 N  N   . HIS   B  1 108 ? 17.153  11.544  -18.244 1.00 37.68  0  123 HIS   B N   1 
ATOM   2872 C  CA  . HIS   B  1 108 ? 17.471  12.878  -17.669 1.00 40.62  0  123 HIS   B CA  1 
ATOM   2873 C  C   . HIS   B  1 108 ? 17.036  12.993  -16.198 1.00 35.80  0  123 HIS   B C   1 
ATOM   2874 O  O   . HIS   B  1 108 ? 16.436  12.045  -15.686 1.00 31.15  0  123 HIS   B O   1 
ATOM   2875 C  CB  . HIS   B  1 108 ? 16.923  13.986  -18.581 1.00 38.07  0  123 HIS   B CB  1 
ATOM   2876 C  CG  . HIS   B  1 108 ? 15.453  14.139  -18.585 1.00 36.48  0  123 HIS   B CG  1 
ATOM   2877 N  ND1 . HIS   B  1 108 ? 14.681  13.754  -19.678 1.00 45.78  0  123 HIS   B ND1 1 
ATOM   2878 C  CD2 . HIS   B  1 108 ? 14.623  14.722  -17.694 1.00 39.88  0  123 HIS   B CD2 1 
ATOM   2879 C  CE1 . HIS   B  1 108 ? 13.415  14.053  -19.433 1.00 46.47  0  123 HIS   B CE1 1 
ATOM   2880 N  NE2 . HIS   B  1 108 ? 13.344  14.654  -18.217 1.00 46.03  0  123 HIS   B NE2 1 
ATOM   2881 N  N   . THR   B  1 109 ? 17.335  14.134  -15.564 1.00 31.62  0  124 THR   B N   1 
ATOM   2882 C  CA  . THR   B  1 109 ? 17.304  14.296  -14.090 1.00 30.33  0  124 THR   B CA  1 
ATOM   2883 C  C   . THR   B  1 109 ? 15.880  14.558  -13.652 1.00 30.03  0  124 THR   B C   1 
ATOM   2884 O  O   . THR   B  1 109 ? 15.062  14.959  -14.479 1.00 30.70  0  124 THR   B O   1 
ATOM   2885 C  CB  . THR   B  1 109 ? 18.218  15.409  -13.585 1.00 33.36  0  124 THR   B CB  1 
ATOM   2886 O  OG1 . THR   B  1 109 ? 17.644  16.614  -14.069 1.00 34.50  0  124 THR   B OG1 1 
ATOM   2887 C  CG2 . THR   B  1 109 ? 19.660  15.292  -14.032 1.00 30.05  0  124 THR   B CG2 1 
ATOM   2888 N  N   . VAL   B  1 110 ? 15.584  14.230  -12.401 1.00 27.44  0  125 VAL   B N   1 
ATOM   2889 C  CA  . VAL   B  1 110 ? 14.304  14.608  -11.736 1.00 30.36  0  125 VAL   B CA  1 
ATOM   2890 C  C   . VAL   B  1 110 ? 14.584  15.919  -10.996 1.00 28.82  0  125 VAL   B C   1 
ATOM   2891 O  O   . VAL   B  1 110 ? 15.751  16.131  -10.606 1.00 30.66  0  125 VAL   B O   1 
ATOM   2892 C  CB  . VAL   B  1 110 ? 13.787  13.492  -10.800 1.00 26.05  0  125 VAL   B CB  1 
ATOM   2893 C  CG1 . VAL   B  1 110 ? 14.652  13.355  -9.557  1.00 26.41  0  125 VAL   B CG1 1 
ATOM   2894 C  CG2 . VAL   B  1 110 ? 12.329  13.700  -10.459 1.00 26.14  0  125 VAL   B CG2 1 
ATOM   2895 N  N   . THR   B  1 111 ? 13.564  16.742  -10.822 1.00 30.43  0  126 THR   B N   1 
ATOM   2896 C  CA  . THR   B  1 111 ? 13.663  18.023  -10.069 1.00 35.70  0  126 THR   B CA  1 
ATOM   2897 C  C   . THR   B  1 111 ? 13.454  17.742  -8.562  1.00 32.13  0  126 THR   B C   1 
ATOM   2898 O  O   . THR   B  1 111 ? 12.471  17.051  -8.202  1.00 32.28  0  126 THR   B O   1 
ATOM   2899 C  CB  . THR   B  1 111 ? 12.682  19.045  -10.658 1.00 36.10  0  126 THR   B CB  1 
ATOM   2900 O  OG1 . THR   B  1 111 ? 12.979  19.112  -12.062 1.00 38.35  0  126 THR   B OG1 1 
ATOM   2901 C  CG2 . THR   B  1 111 ? 12.781  20.407  -10.001 1.00 39.33  0  126 THR   B CG2 1 
ATOM   2902 N  N   . LEU   B  1 112 ? 14.323  18.292  -7.724  1.00 32.32  0  127 LEU   B N   1 
ATOM   2903 C  CA  . LEU   B  1 112 ? 14.151  18.300  -6.248  1.00 38.46  0  127 LEU   B CA  1 
ATOM   2904 C  C   . LEU   B  1 112 ? 13.102  19.336  -5.877  1.00 39.57  0  127 LEU   B C   1 
ATOM   2905 O  O   . LEU   B  1 112 ? 12.980  20.377  -6.509  1.00 35.27  0  127 LEU   B O   1 
ATOM   2906 C  CB  . LEU   B  1 112 ? 15.481  18.577  -5.554  1.00 36.36  0  127 LEU   B CB  1 
ATOM   2907 C  CG  . LEU   B  1 112 ? 16.526  17.508  -5.821  1.00 40.33  0  127 LEU   B CG  1 
ATOM   2908 C  CD1 . LEU   B  1 112 ? 17.884  17.894  -5.270  1.00 38.88  0  127 LEU   B CD1 1 
ATOM   2909 C  CD2 . LEU   B  1 112 ? 16.065  16.181  -5.276  1.00 40.72  0  127 LEU   B CD2 1 
ATOM   2910 N  N   . PRO   B  1 113 ? 12.293  19.081  -4.834  1.00 39.38  0  128 PRO   B N   1 
ATOM   2911 C  CA  . PRO   B  1 113 ? 11.292  20.054  -4.407  1.00 39.75  0  128 PRO   B CA  1 
ATOM   2912 C  C   . PRO   B  1 113 ? 11.970  21.238  -3.718  1.00 37.91  0  128 PRO   B C   1 
ATOM   2913 O  O   . PRO   B  1 113 ? 13.087  21.121  -3.229  1.00 35.06  0  128 PRO   B O   1 
ATOM   2914 C  CB  . PRO   B  1 113 ? 10.409  19.264  -3.453  1.00 36.42  0  128 PRO   B CB  1 
ATOM   2915 C  CG  . PRO   B  1 113 ? 11.293  18.158  -2.934  1.00 37.45  0  128 PRO   B CG  1 
ATOM   2916 C  CD  . PRO   B  1 113 ? 12.311  17.871  -4.009  1.00 41.41  0  128 PRO   B CD  1 
ATOM   2917 N  N   . PRO   B  1 114 ? 11.326  22.422  -3.671  1.00 47.05  0  129 PRO   B N   1 
ATOM   2918 C  CA  . PRO   B  1 114 ? 11.789  23.505  -2.803  1.00 47.60  0  129 PRO   B CA  1 
ATOM   2919 C  C   . PRO   B  1 114 ? 11.549  23.103  -1.334  1.00 50.07  0  129 PRO   B C   1 
ATOM   2920 O  O   . PRO   B  1 114 ? 10.609  22.355  -1.073  1.00 46.31  0  129 PRO   B O   1 
ATOM   2921 C  CB  . PRO   B  1 114 ? 10.940  24.722  -3.203  1.00 51.45  0  129 PRO   B CB  1 
ATOM   2922 C  CG  . PRO   B  1 114 ? 10.116  24.279  -4.410  1.00 55.90  0  129 PRO   B CG  1 
ATOM   2923 C  CD  . PRO   B  1 114 ? 10.107  22.769  -4.416  1.00 49.00  0  129 PRO   B CD  1 
ATOM   2924 N  N   . ALA   B  1 115 ? 12.364  23.632  -0.407  1.00 51.87  0  130 ALA   B N   1 
ATOM   2925 C  CA  . ALA   B  1 115 ? 12.305  23.389  1.058   1.00 49.99  0  130 ALA   B CA  1 
ATOM   2926 C  C   . ALA   B  1 115 ? 10.891  23.605  1.584   1.00 48.36  0  130 ALA   B C   1 
ATOM   2927 O  O   . ALA   B  1 115 ? 10.463  22.830  2.426   1.00 53.42  0  130 ALA   B O   1 
ATOM   2928 C  CB  . ALA   B  1 115 ? 13.311  24.252  1.781   1.00 47.89  0  130 ALA   B CB  1 
ATOM   2929 N  N   . SER   B  1 116 ? 10.159  24.568  1.036   1.00 53.83  0  131 SER   B N   1 
ATOM   2930 C  CA  . SER   B  1 116 ? 8.801   24.950  1.502   1.00 56.86  0  131 SER   B CA  1 
ATOM   2931 C  C   . SER   B  1 116 ? 7.721   23.942  1.063   1.00 55.60  0  131 SER   B C   1 
ATOM   2932 O  O   . SER   B  1 116 ? 6.612   24.007  1.617   1.00 58.68  0  131 SER   B O   1 
ATOM   2933 C  CB  . SER   B  1 116 ? 8.472   26.353  1.017   1.00 56.33  0  131 SER   B CB  1 
ATOM   2934 O  OG  . SER   B  1 116 ? 8.648   26.452  -0.392  1.00 57.83  0  131 SER   B OG  1 
ATOM   2935 N  N   . GLU   B  1 117 ? 7.973   23.083  0.070   1.00 52.56  0  132 GLU   B N   1 
ATOM   2936 C  CA  . GLU   B  1 117 ? 6.932   22.247  -0.583  1.00 49.27  0  132 GLU   B CA  1 
ATOM   2937 C  C   . GLU   B  1 117 ? 6.407   21.221  0.425   1.00 51.41  0  132 GLU   B C   1 
ATOM   2938 O  O   . GLU   B  1 117 ? 7.215   20.458  0.991   1.00 46.57  0  132 GLU   B O   1 
ATOM   2939 C  CB  . GLU   B  1 117 ? 7.502   21.550  -1.820  1.00 50.74  0  132 GLU   B CB  1 
ATOM   2940 C  CG  . GLU   B  1 117 ? 6.508   20.638  -2.520  1.00 54.65  0  132 GLU   B CG  1 
ATOM   2941 C  CD  . GLU   B  1 117 ? 5.363   21.346  -3.227  1.00 63.46  0  132 GLU   B CD  1 
ATOM   2942 O  OE1 . GLU   B  1 117 ? 4.203   20.840  -3.147  1.00 68.98  0  132 GLU   B OE1 1 
ATOM   2943 O  OE2 . GLU   B  1 117 ? 5.638   22.373  -3.900  1.00 58.72  -1 132 GLU   B OE2 1 
ATOM   2944 N  N   . THR   B  1 118 ? 5.097   21.226  0.627   1.00 57.94  0  133 THR   B N   1 
ATOM   2945 C  CA  . THR   B  1 118 ? 4.365   20.297  1.515   1.00 61.66  0  133 THR   B CA  1 
ATOM   2946 C  C   . THR   B  1 118 ? 3.443   19.520  0.577   1.00 64.30  0  133 THR   B C   1 
ATOM   2947 O  O   . THR   B  1 118 ? 2.454   20.102  0.093   1.00 79.24  0  133 THR   B O   1 
ATOM   2948 C  CB  . THR   B  1 118 ? 3.659   21.031  2.672   1.00 67.76  0  133 THR   B CB  1 
ATOM   2949 O  OG1 . THR   B  1 118 ? 2.825   20.072  3.323   1.00 71.80  0  133 THR   B OG1 1 
ATOM   2950 C  CG2 . THR   B  1 118 ? 2.791   22.210  2.272   1.00 67.80  0  133 THR   B CG2 1 
ATOM   2951 N  N   . PHE   B  1 119 ? 3.823   18.288  0.268   1.00 51.58  0  134 PHE   B N   1 
ATOM   2952 C  CA  . PHE   B  1 119 ? 3.058   17.359  -0.593  1.00 45.77  0  134 PHE   B CA  1 
ATOM   2953 C  C   . PHE   B  1 119 ? 1.820   16.945  0.188   1.00 44.44  0  134 PHE   B C   1 
ATOM   2954 O  O   . PHE   B  1 119 ? 1.913   16.062  1.019   1.00 52.19  0  134 PHE   B O   1 
ATOM   2955 C  CB  . PHE   B  1 119 ? 3.943   16.174  -0.980  1.00 40.28  0  134 PHE   B CB  1 
ATOM   2956 C  CG  . PHE   B  1 119 ? 5.165   16.552  -1.782  1.00 36.60  0  134 PHE   B CG  1 
ATOM   2957 C  CD1 . PHE   B  1 119 ? 5.080   16.752  -3.146  1.00 40.32  0  134 PHE   B CD1 1 
ATOM   2958 C  CD2 . PHE   B  1 119 ? 6.392   16.721  -1.178  1.00 32.41  0  134 PHE   B CD2 1 
ATOM   2959 C  CE1 . PHE   B  1 119 ? 6.189   17.097  -3.900  1.00 40.41  0  134 PHE   B CE1 1 
ATOM   2960 C  CE2 . PHE   B  1 119 ? 7.491   17.101  -1.921  1.00 36.48  0  134 PHE   B CE2 1 
ATOM   2961 C  CZ  . PHE   B  1 119 ? 7.394   17.261  -3.284  1.00 36.90  0  134 PHE   B CZ  1 
ATOM   2962 N  N   . PRO   B  1 120 ? 0.639   17.540  -0.044  1.00 45.36  0  135 PRO   B N   1 
ATOM   2963 C  CA  . PRO   B  1 120 ? -0.468  17.378  0.883   1.00 44.32  0  135 PRO   B CA  1 
ATOM   2964 C  C   . PRO   B  1 120 ? -1.122  16.004  0.788   1.00 40.45  0  135 PRO   B C   1 
ATOM   2965 O  O   . PRO   B  1 120 ? -1.051  15.319  -0.219  1.00 36.39  0  135 PRO   B O   1 
ATOM   2966 C  CB  . PRO   B  1 120 ? -1.470  18.465  0.461   1.00 48.13  0  135 PRO   B CB  1 
ATOM   2967 C  CG  . PRO   B  1 120 ? -1.212  18.627  -1.040  1.00 49.68  0  135 PRO   B CG  1 
ATOM   2968 C  CD  . PRO   B  1 120 ? 0.278   18.375  -1.206  1.00 50.53  0  135 PRO   B CD  1 
ATOM   2969 N  N   . PRO   B  1 121 ? -1.783  15.556  1.863   1.00 42.56  0  136 PRO   B N   1 
ATOM   2970 C  CA  . PRO   B  1 121 ? -2.472  14.269  1.847   1.00 43.54  0  136 PRO   B CA  1 
ATOM   2971 C  C   . PRO   B  1 121 ? -3.449  14.153  0.675   1.00 45.01  0  136 PRO   B C   1 
ATOM   2972 O  O   . PRO   B  1 121 ? -4.122  15.115  0.382   1.00 38.19  0  136 PRO   B O   1 
ATOM   2973 C  CB  . PRO   B  1 121 ? -3.205  14.257  3.188   1.00 47.00  0  136 PRO   B CB  1 
ATOM   2974 C  CG  . PRO   B  1 121 ? -2.324  15.135  4.067   1.00 45.89  0  136 PRO   B CG  1 
ATOM   2975 C  CD  . PRO   B  1 121 ? -1.887  16.255  3.158   1.00 42.62  0  136 PRO   B CD  1 
ATOM   2976 N  N   . GLY   B  1 122 ? -3.454  12.987  0.036   1.00 47.37  0  137 GLY   B N   1 
ATOM   2977 C  CA  . GLY   B  1 122 ? -4.368  12.658  -1.071  1.00 50.41  0  137 GLY   B CA  1 
ATOM   2978 C  C   . GLY   B  1 122 ? -3.772  12.944  -2.435  1.00 48.79  0  137 GLY   B C   1 
ATOM   2979 O  O   . GLY   B  1 122 ? -4.296  12.392  -3.424  1.00 54.96  0  137 GLY   B O   1 
ATOM   2980 N  N   . MET   B  1 123 ? -2.701  13.734  -2.506  1.00 48.20  0  138 MET   B N   1 
ATOM   2981 C  CA  . MET   B  1 123 ? -2.029  14.088  -3.787  1.00 53.88  0  138 MET   B CA  1 
ATOM   2982 C  C   . MET   B  1 123 ? -1.646  12.808  -4.547  1.00 59.25  0  138 MET   B C   1 
ATOM   2983 O  O   . MET   B  1 123 ? -1.115  11.869  -3.935  1.00 51.32  0  138 MET   B O   1 
ATOM   2984 C  CB  . MET   B  1 123 ? -0.770  14.929  -3.541  1.00 52.38  0  138 MET   B CB  1 
ATOM   2985 C  CG  . MET   B  1 123 ? 0.067   15.108  -4.790  1.00 61.95  0  138 MET   B CG  1 
ATOM   2986 S  SD  . MET   B  1 123 ? 0.649   16.761  -4.992  1.00 78.37  0  138 MET   B SD  1 
ATOM   2987 C  CE  . MET   B  1 123 ? 2.071   16.664  -3.928  1.00 66.85  0  138 MET   B CE  1 
ATOM   2988 N  N   . PRO   B  1 124 ? -1.907  12.727  -5.882  1.00 61.81  0  139 PRO   B N   1 
ATOM   2989 C  CA  . PRO   B  1 124 ? -1.459  11.593  -6.692  1.00 60.99  0  139 PRO   B CA  1 
ATOM   2990 C  C   . PRO   B  1 124 ? 0.057   11.651  -6.953  1.00 46.29  0  139 PRO   B C   1 
ATOM   2991 O  O   . PRO   B  1 124 ? 0.530   12.599  -7.534  1.00 48.52  0  139 PRO   B O   1 
ATOM   2992 C  CB  . PRO   B  1 124 ? -2.264  11.756  -7.998  1.00 63.41  0  139 PRO   B CB  1 
ATOM   2993 C  CG  . PRO   B  1 124 ? -2.479  13.250  -8.128  1.00 66.15  0  139 PRO   B CG  1 
ATOM   2994 C  CD  . PRO   B  1 124 ? -2.633  13.724  -6.695  1.00 66.97  0  139 PRO   B CD  1 
ATOM   2995 N  N   . CYS   B  1 125 ? 0.787   10.667  -6.437  1.00 38.58  0  140 CYS   B N   1 
ATOM   2996 C  CA  . CYS   B  1 125 ? 2.243   10.487  -6.638  1.00 34.96  0  140 CYS   B CA  1 
ATOM   2997 C  C   . CYS   B  1 125 ? 2.488   9.081   -7.193  1.00 32.63  0  140 CYS   B C   1 
ATOM   2998 O  O   . CYS   B  1 125 ? 1.573   8.254   -7.128  1.00 31.92  0  140 CYS   B O   1 
ATOM   2999 C  CB  . CYS   B  1 125 ? 2.966   10.698  -5.316  1.00 37.98  0  140 CYS   B CB  1 
ATOM   3000 S  SG  . CYS   B  1 125 ? 2.636   12.336  -4.598  1.00 38.26  0  140 CYS   B SG  1 
ATOM   3001 N  N   . TRP   B  1 126 ? 3.684   8.832   -7.728  1.00 32.78  0  141 TRP   B N   1 
ATOM   3002 C  CA  . TRP   B  1 126 ? 4.068   7.575   -8.414  1.00 33.20  0  141 TRP   B CA  1 
ATOM   3003 C  C   . TRP   B  1 126 ? 5.368   7.077   -7.808  1.00 29.21  0  141 TRP   B C   1 
ATOM   3004 O  O   . TRP   B  1 126 ? 6.312   7.873   -7.641  1.00 27.54  0  141 TRP   B O   1 
ATOM   3005 C  CB  . TRP   B  1 126 ? 4.196   7.758   -9.934  1.00 33.05  0  141 TRP   B CB  1 
ATOM   3006 C  CG  . TRP   B  1 126 ? 2.878   8.083   -10.565 1.00 34.94  0  141 TRP   B CG  1 
ATOM   3007 C  CD1 . TRP   B  1 126 ? 2.233   9.287   -10.533 1.00 37.12  0  141 TRP   B CD1 1 
ATOM   3008 C  CD2 . TRP   B  1 126 ? 2.020   7.187   -11.283 1.00 34.61  0  141 TRP   B CD2 1 
ATOM   3009 N  NE1 . TRP   B  1 126 ? 1.036   9.197   -11.185 1.00 36.76  0  141 TRP   B NE1 1 
ATOM   3010 C  CE2 . TRP   B  1 126 ? 0.871   7.922   -11.651 1.00 38.17  0  141 TRP   B CE2 1 
ATOM   3011 C  CE3 . TRP   B  1 126 ? 2.096   5.840   -11.645 1.00 38.93  0  141 TRP   B CE3 1 
ATOM   3012 C  CZ2 . TRP   B  1 126 ? -0.181  7.357   -12.375 1.00 38.39  0  141 TRP   B CZ2 1 
ATOM   3013 C  CZ3 . TRP   B  1 126 ? 1.050   5.273   -12.345 1.00 44.20  0  141 TRP   B CZ3 1 
ATOM   3014 C  CH2 . TRP   B  1 126 ? -0.064  6.032   -12.725 1.00 44.51  0  141 TRP   B CH2 1 
ATOM   3015 N  N   . VAL   B  1 127 ? 5.424   5.775   -7.601  1.00 27.02  0  142 VAL   B N   1 
ATOM   3016 C  CA  . VAL   B  1 127 ? 6.684   5.110   -7.205  1.00 27.63  0  142 VAL   B CA  1 
ATOM   3017 C  C   . VAL   B  1 127 ? 6.961   4.045   -8.268  1.00 28.70  0  142 VAL   B C   1 
ATOM   3018 O  O   . VAL   B  1 127 ? 5.985   3.467   -8.831  1.00 26.90  0  142 VAL   B O   1 
ATOM   3019 C  CB  . VAL   B  1 127 ? 6.615   4.571   -5.767  1.00 25.74  0  142 VAL   B CB  1 
ATOM   3020 C  CG1 . VAL   B  1 127 ? 5.496   3.564   -5.590  1.00 27.20  0  142 VAL   B CG1 1 
ATOM   3021 C  CG2 . VAL   B  1 127 ? 7.969   3.994   -5.320  1.00 26.88  0  142 VAL   B CG2 1 
ATOM   3022 N  N   . THR   B  1 128 ? 8.237   3.889   -8.597  1.00 24.12  0  143 THR   B N   1 
ATOM   3023 C  CA  . THR   B  1 128 ? 8.692   3.098   -9.745  1.00 24.27  0  143 THR   B CA  1 
ATOM   3024 C  C   . THR   B  1 128 ? 9.806   2.174   -9.272  1.00 23.08  0  143 THR   B C   1 
ATOM   3025 O  O   . THR   B  1 128 ? 10.514  2.544   -8.302  1.00 21.74  0  143 THR   B O   1 
ATOM   3026 C  CB  . THR   B  1 128 ? 9.125   4.030   -10.889 1.00 25.85  0  143 THR   B CB  1 
ATOM   3027 O  OG1 . THR   B  1 128 ? 10.125  4.958   -10.451 1.00 25.26  0  143 THR   B OG1 1 
ATOM   3028 C  CG2 . THR   B  1 128 ? 7.976   4.839   -11.434 1.00 27.40  0  143 THR   B CG2 1 
ATOM   3029 N  N   . GLY   B  1 129 ? 9.984   1.030   -9.945  1.00 21.01  0  144 GLY   B N   1 
ATOM   3030 C  CA  . GLY   B  1 129 ? 11.170  0.193   -9.709  1.00 23.92  0  144 GLY   B CA  1 
ATOM   3031 C  C   . GLY   B  1 129 ? 10.992  -1.226  -10.183 1.00 22.99  0  144 GLY   B C   1 
ATOM   3032 O  O   . GLY   B  1 129 ? 9.914   -1.558  -10.762 1.00 25.14  0  144 GLY   B O   1 
ATOM   3033 N  N   . TRP   B  1 130 ? 12.027  -2.024  -9.944  1.00 26.88  0  145 TRP   B N   1 
ATOM   3034 C  CA  . TRP   B  1 130 ? 12.120  -3.444  -10.379 1.00 28.86  0  145 TRP   B CA  1 
ATOM   3035 C  C   . TRP   B  1 130 ? 12.036  -4.385  -9.178  1.00 32.86  0  145 TRP   B C   1 
ATOM   3036 O  O   . TRP   B  1 130 ? 12.607  -5.532  -9.266  1.00 31.47  0  145 TRP   B O   1 
ATOM   3037 C  CB  . TRP   B  1 130 ? 13.421  -3.645  -11.137 1.00 28.31  0  145 TRP   B CB  1 
ATOM   3038 C  CG  . TRP   B  1 130 ? 13.542  -2.882  -12.427 1.00 29.36  0  145 TRP   B CG  1 
ATOM   3039 C  CD1 . TRP   B  1 130 ? 13.062  -3.235  -13.653 1.00 28.17  0  145 TRP   B CD1 1 
ATOM   3040 C  CD2 . TRP   B  1 130 ? 14.220  -1.630  -12.606 1.00 27.69  0  145 TRP   B CD2 1 
ATOM   3041 N  NE1 . TRP   B  1 130 ? 13.450  -2.323  -14.590 1.00 30.56  0  145 TRP   B NE1 1 
ATOM   3042 C  CE2 . TRP   B  1 130 ? 14.125  -1.303  -13.975 1.00 28.98  0  145 TRP   B CE2 1 
ATOM   3043 C  CE3 . TRP   B  1 130 ? 14.871  -0.752  -11.733 1.00 26.09  0  145 TRP   B CE3 1 
ATOM   3044 C  CZ2 . TRP   B  1 130 ? 14.717  -0.161  -14.500 1.00 26.03  0  145 TRP   B CZ2 1 
ATOM   3045 C  CZ3 . TRP   B  1 130 ? 15.436  0.392   -12.247 1.00 26.92  0  145 TRP   B CZ3 1 
ATOM   3046 C  CH2 . TRP   B  1 130 ? 15.393  0.660   -13.620 1.00 27.98  0  145 TRP   B CH2 1 
ATOM   3047 N  N   . GLY   B  1 131 ? 11.377  -3.950  -8.094  1.00 28.34  0  146 GLY   B N   1 
ATOM   3048 C  CA  . GLY   B  1 131 ? 11.273  -4.782  -6.884  1.00 27.69  0  146 GLY   B CA  1 
ATOM   3049 C  C   . GLY   B  1 131 ? 10.161  -5.836  -6.982  1.00 29.54  0  146 GLY   B C   1 
ATOM   3050 O  O   . GLY   B  1 131 ? 9.424   -5.908  -8.022  1.00 30.67  0  146 GLY   B O   1 
ATOM   3051 N  N   . ASP   B  1 132 ? 9.994   -6.578  -5.893  1.00 25.87  0  147 ASP   B N   1 
ATOM   3052 C  CA  . ASP   B  1 132 ? 8.975   -7.636  -5.719  1.00 26.31  0  147 ASP   B CA  1 
ATOM   3053 C  C   . ASP   B  1 132 ? 7.567   -7.103  -6.024  1.00 25.60  0  147 ASP   B C   1 
ATOM   3054 O  O   . ASP   B  1 132 ? 7.259   -5.945  -5.740  1.00 24.31  0  147 ASP   B O   1 
ATOM   3055 C  CB  . ASP   B  1 132 ? 9.113   -8.233  -4.317  1.00 26.34  0  147 ASP   B CB  1 
ATOM   3056 C  CG  . ASP   B  1 132 ? 10.354  -9.100  -4.121  1.00 26.35  0  147 ASP   B CG  1 
ATOM   3057 O  OD1 . ASP   B  1 132 ? 11.124  -9.301  -5.075  1.00 27.98  0  147 ASP   B OD1 1 
ATOM   3058 O  OD2 . ASP   B  1 132 ? 10.522  -9.583  -3.001  1.00 34.40  -1 147 ASP   B OD2 1 
ATOM   3059 N  N   . VAL   B  1 133 ? 6.735   -7.957  -6.593  1.00 27.42  0  148 VAL   B N   1 
ATOM   3060 C  CA  . VAL   B  1 133 ? 5.336   -7.649  -7.004  1.00 28.87  0  148 VAL   B CA  1 
ATOM   3061 C  C   . VAL   B  1 133 ? 4.378   -8.053  -5.878  1.00 29.75  0  148 VAL   B C   1 
ATOM   3062 O  O   . VAL   B  1 133 ? 3.184   -7.798  -6.015  1.00 30.22  0  148 VAL   B O   1 
ATOM   3063 C  CB  . VAL   B  1 133 ? 5.008   -8.326  -8.347  1.00 33.12  0  148 VAL   B CB  1 
ATOM   3064 C  CG1 . VAL   B  1 133 ? 5.940   -7.835  -9.451  1.00 37.44  0  148 VAL   B CG1 1 
ATOM   3065 C  CG2 . VAL   B  1 133 ? 5.028   -9.851  -8.266  1.00 33.33  0  148 VAL   B CG2 1 
ATOM   3066 N  N   . ASP   B  1 134 ? 4.883   -8.666  -4.801  1.00 31.63  0  149 ASP   B N   1 
ATOM   3067 C  CA  . ASP   B  1 134 ? 4.136   -8.929  -3.546  1.00 31.08  0  149 ASP   B CA  1 
ATOM   3068 C  C   . ASP   B  1 134 ? 5.132   -9.457  -2.509  1.00 31.46  0  149 ASP   B C   1 
ATOM   3069 O  O   . ASP   B  1 134 ? 6.316   -9.657  -2.885  1.00 29.96  0  149 ASP   B O   1 
ATOM   3070 C  CB  . ASP   B  1 134 ? 2.996   -9.919  -3.770  1.00 36.82  0  149 ASP   B CB  1 
ATOM   3071 C  CG  . ASP   B  1 134 ? 1.810   -9.679  -2.855  1.00 41.11  0  149 ASP   B CG  1 
ATOM   3072 O  OD1 . ASP   B  1 134 ? 2.014   -9.350  -1.663  1.00 41.66  0  149 ASP   B OD1 1 
ATOM   3073 O  OD2 . ASP   B  1 134 ? 0.695   -9.842  -3.333  1.00 55.72  -1 149 ASP   B OD2 1 
ATOM   3074 N  N   . ASN   B  1 135 ? 4.705   -9.663  -1.258  1.00 31.02  0  150 ASN   B N   1 
ATOM   3075 C  CA  . ASN   B  1 135 ? 5.601   -10.209 -0.197  1.00 35.46  0  150 ASN   B CA  1 
ATOM   3076 C  C   . ASN   B  1 135 ? 6.249   -11.513 -0.700  1.00 35.29  0  150 ASN   B C   1 
ATOM   3077 O  O   . ASN   B  1 135 ? 5.515   -12.399 -1.120  1.00 35.73  0  150 ASN   B O   1 
ATOM   3078 C  CB  . ASN   B  1 135 ? 4.862   -10.374 1.131   1.00 33.29  0  150 ASN   B CB  1 
ATOM   3079 C  CG  . ASN   B  1 135 ? 4.387   -9.036  1.668   1.00 40.23  0  150 ASN   B CG  1 
ATOM   3080 O  OD1 . ASN   B  1 135 ? 5.181   -8.149  2.010   1.00 36.86  0  150 ASN   B OD1 1 
ATOM   3081 N  ND2 . ASN   B  1 135 ? 3.085   -8.854  1.702   1.00 41.64  0  150 ASN   B ND2 1 
ATOM   3082 N  N   . ASP   B  1 136 ? 7.577   -11.570 -0.715  1.00 33.97  0  151 ASP   B N   1 
ATOM   3083 C  CA  A ASP   B  1 136 ? 8.399   -12.745 -1.133  0.70 40.55  0  151 ASP   B CA  1 
ATOM   3084 C  CA  B ASP   B  1 136 ? 8.379   -12.762 -1.120  0.30 37.65  0  151 ASP   B CA  1 
ATOM   3085 C  C   . ASP   B  1 136 ? 7.977   -13.243 -2.530  1.00 41.18  0  151 ASP   B C   1 
ATOM   3086 O  O   . ASP   B  1 136 ? 8.047   -14.446 -2.774  1.00 40.20  0  151 ASP   B O   1 
ATOM   3087 C  CB  A ASP   B  1 136 ? 8.330   -13.850 -0.081  0.70 44.45  0  151 ASP   B CB  1 
ATOM   3088 C  CB  B ASP   B  1 136 ? 8.245   -13.876 -0.074  0.30 38.10  0  151 ASP   B CB  1 
ATOM   3089 C  CG  A ASP   B  1 136 ? 9.561   -14.760 -0.104  0.70 48.48  0  151 ASP   B CG  1 
ATOM   3090 C  CG  B ASP   B  1 136 ? 8.626   -13.451 1.337   0.00 38.01  0  151 ASP   B CG  1 
ATOM   3091 O  OD1 A ASP   B  1 136 ? 10.684  -14.282 0.187   0.70 45.26  0  151 ASP   B OD1 1 
ATOM   3092 O  OD1 B ASP   B  1 136 ? 9.330   -12.431 1.467   0.00 38.12  0  151 ASP   B OD1 1 
ATOM   3093 O  OD2 A ASP   B  1 136 ? 9.399   -15.931 -0.466  0.70 53.17  -1 151 ASP   B OD2 1 
ATOM   3094 O  OD2 B ASP   B  1 136 ? 8.217   -14.142 2.290   0.00 38.02  -1 151 ASP   B OD2 1 
ATOM   3095 N  N   . GLU   B  1 137 ? 7.576   -12.339 -3.426  1.00 35.72  0  152 GLU   B N   1 
ATOM   3096 C  CA  . GLU   B  1 137 ? 7.209   -12.658 -4.831  1.00 37.42  0  152 GLU   B CA  1 
ATOM   3097 C  C   . GLU   B  1 137 ? 8.074   -11.784 -5.750  1.00 34.02  0  152 GLU   B C   1 
ATOM   3098 O  O   . GLU   B  1 137 ? 7.792   -10.565 -5.867  1.00 29.20  0  152 GLU   B O   1 
ATOM   3099 C  CB  . GLU   B  1 137 ? 5.711   -12.442 -5.013  1.00 42.96  0  152 GLU   B CB  1 
ATOM   3100 C  CG  . GLU   B  1 137 ? 5.160   -12.937 -6.338  1.00 51.62  0  152 GLU   B CG  1 
ATOM   3101 C  CD  . GLU   B  1 137 ? 3.639   -13.065 -6.371  1.00 58.80  0  152 GLU   B CD  1 
ATOM   3102 O  OE1 . GLU   B  1 137 ? 3.074   -12.850 -7.460  1.00 64.83  0  152 GLU   B OE1 1 
ATOM   3103 O  OE2 . GLU   B  1 137 ? 3.019   -13.415 -5.317  1.00 54.36  -1 152 GLU   B OE2 1 
ATOM   3104 N  N   . ARG   B  1 138 ? 9.094   -12.384 -6.357  1.00 31.33  0  153 ARG   B N   1 
ATOM   3105 C  CA  . ARG   B  1 138 ? 10.071  -11.733 -7.269  1.00 36.00  0  153 ARG   B CA  1 
ATOM   3106 C  C   . ARG   B  1 138 ? 9.357   -11.143 -8.487  1.00 33.57  0  153 ARG   B C   1 
ATOM   3107 O  O   . ARG   B  1 138 ? 8.346   -11.711 -8.943  1.00 28.38  0  153 ARG   B O   1 
ATOM   3108 C  CB  . ARG   B  1 138 ? 11.117  -12.719 -7.807  1.00 38.93  0  153 ARG   B CB  1 
ATOM   3109 C  CG  . ARG   B  1 138 ? 12.001  -13.390 -6.761  1.00 44.45  0  153 ARG   B CG  1 
ATOM   3110 C  CD  . ARG   B  1 138 ? 12.916  -12.440 -6.022  1.00 48.48  0  153 ARG   B CD  1 
ATOM   3111 N  NE  . ARG   B  1 138 ? 12.325  -11.890 -4.802  1.00 53.53  0  153 ARG   B NE  1 
ATOM   3112 C  CZ  . ARG   B  1 138 ? 12.132  -12.561 -3.637  1.00 58.99  0  153 ARG   B CZ  1 
ATOM   3113 N  NH1 . ARG   B  1 138 ? 12.412  -13.854 -3.526  1.00 50.42  1  153 ARG   B NH1 1 
ATOM   3114 N  NH2 . ARG   B  1 138 ? 11.630  -11.938 -2.574  1.00 47.51  0  153 ARG   B NH2 1 
ATOM   3115 N  N   . LEU   B  1 139 ? 9.881   -10.034 -9.004  1.00 29.52  0  154 LEU   B N   1 
ATOM   3116 C  CA  . LEU   B  1 139 ? 9.514   -9.559  -10.352 1.00 29.82  0  154 LEU   B CA  1 
ATOM   3117 C  C   . LEU   B  1 139 ? 9.943   -10.666 -11.316 1.00 27.77  0  154 LEU   B C   1 
ATOM   3118 O  O   . LEU   B  1 139 ? 11.110  -11.038 -11.321 1.00 28.61  0  154 LEU   B O   1 
ATOM   3119 C  CB  . LEU   B  1 139 ? 10.234  -8.241  -10.666 1.00 29.38  0  154 LEU   B CB  1 
ATOM   3120 C  CG  . LEU   B  1 139 ? 9.852   -7.590  -11.998 1.00 31.70  0  154 LEU   B CG  1 
ATOM   3121 C  CD1 . LEU   B  1 139 ? 8.379   -7.212  -12.061 1.00 31.17  0  154 LEU   B CD1 1 
ATOM   3122 C  CD2 . LEU   B  1 139 ? 10.706  -6.362  -12.266 1.00 29.91  0  154 LEU   B CD2 1 
ATOM   3123 N  N   . PRO   B  1 140 ? 9.035   -11.237 -12.133 1.00 29.90  0  155 PRO   B N   1 
ATOM   3124 C  CA  . PRO   B  1 140 ? 9.440   -12.239 -13.126 1.00 30.91  0  155 PRO   B CA  1 
ATOM   3125 C  C   . PRO   B  1 140 ? 10.238  -11.668 -14.298 1.00 31.79  0  155 PRO   B C   1 
ATOM   3126 O  O   . PRO   B  1 140 ? 10.085  -10.496 -14.672 1.00 28.65  0  155 PRO   B O   1 
ATOM   3127 C  CB  . PRO   B  1 140 ? 8.135   -12.803 -13.697 1.00 32.53  0  155 PRO   B CB  1 
ATOM   3128 C  CG  . PRO   B  1 140 ? 6.971   -12.063 -12.979 1.00 34.83  0  155 PRO   B CG  1 
ATOM   3129 C  CD  . PRO   B  1 140 ? 7.589   -10.951 -12.157 1.00 31.67  0  155 PRO   B CD  1 
ATOM   3130 N  N   . PRO   B  1 141 ? 11.093  -12.485 -14.952 1.00 34.46  0  156 PRO   B N   1 
ATOM   3131 C  CA  . PRO   B  1 141 ? 11.612  -12.140 -16.281 1.00 31.96  0  156 PRO   B CA  1 
ATOM   3132 C  C   . PRO   B  1 141 ? 10.437  -11.784 -17.189 1.00 28.07  0  156 PRO   B C   1 
ATOM   3133 O  O   . PRO   B  1 141 ? 9.345   -12.340 -17.030 1.00 26.35  0  156 PRO   B O   1 
ATOM   3134 C  CB  . PRO   B  1 141 ? 12.285  -13.431 -16.786 1.00 35.26  0  156 PRO   B CB  1 
ATOM   3135 C  CG  . PRO   B  1 141 ? 12.526  -14.291 -15.543 1.00 33.19  0  156 PRO   B CG  1 
ATOM   3136 C  CD  . PRO   B  1 141 ? 11.566  -13.799 -14.478 1.00 36.75  0  156 PRO   B CD  1 
ATOM   3137 N  N   . PRO   B  1 142 ? 10.573  -10.842 -18.147 1.00 27.01  0  157 PRO   B N   1 
ATOM   3138 C  CA  . PRO   B  1 142 ? 11.822  -10.113 -18.429 1.00 26.67  0  157 PRO   B CA  1 
ATOM   3139 C  C   . PRO   B  1 142 ? 12.094  -8.821  -17.618 1.00 30.13  0  157 PRO   B C   1 
ATOM   3140 O  O   . PRO   B  1 142 ? 12.837  -7.956  -18.089 1.00 27.73  0  157 PRO   B O   1 
ATOM   3141 C  CB  . PRO   B  1 142 ? 11.620  -9.750  -19.909 1.00 27.52  0  157 PRO   B CB  1 
ATOM   3142 C  CG  . PRO   B  1 142 ? 10.112  -9.511  -20.040 1.00 27.79  0  157 PRO   B CG  1 
ATOM   3143 C  CD  . PRO   B  1 142 ? 9.456   -10.435 -19.028 1.00 28.54  0  157 PRO   B CD  1 
ATOM   3144 N  N   . PHE   B  1 143 ? 11.579  -8.720  -16.393 1.00 30.58  0  158 PHE   B N   1 
ATOM   3145 C  CA  . PHE   B  1 143 ? 11.963  -7.669  -15.398 1.00 29.22  0  158 PHE   B CA  1 
ATOM   3146 C  C   . PHE   B  1 143 ? 11.655  -6.265  -15.939 1.00 26.75  0  158 PHE   B C   1 
ATOM   3147 O  O   . PHE   B  1 143 ? 12.538  -5.409  -16.047 1.00 25.71  0  158 PHE   B O   1 
ATOM   3148 C  CB  . PHE   B  1 143 ? 13.449  -7.796  -15.062 1.00 27.35  0  158 PHE   B CB  1 
ATOM   3149 C  CG  . PHE   B  1 143 ? 13.989  -9.184  -14.824 1.00 31.70  0  158 PHE   B CG  1 
ATOM   3150 C  CD1 . PHE   B  1 143 ? 13.673  -9.869  -13.662 1.00 30.23  0  158 PHE   B CD1 1 
ATOM   3151 C  CD2 . PHE   B  1 143 ? 14.909  -9.760  -15.708 1.00 31.76  0  158 PHE   B CD2 1 
ATOM   3152 C  CE1 . PHE   B  1 143 ? 14.226  -11.118 -13.400 1.00 32.07  0  158 PHE   B CE1 1 
ATOM   3153 C  CE2 . PHE   B  1 143 ? 15.421  -11.026 -15.463 1.00 34.16  0  158 PHE   B CE2 1 
ATOM   3154 C  CZ  . PHE   B  1 143 ? 15.082  -11.701 -14.307 1.00 32.33  0  158 PHE   B CZ  1 
ATOM   3155 N  N   . PRO   B  1 144 ? 10.392  -5.977  -16.310 1.00 26.44  0  159 PRO   B N   1 
ATOM   3156 C  CA  . PRO   B  1 144 ? 10.024  -4.665  -16.837 1.00 27.27  0  159 PRO   B CA  1 
ATOM   3157 C  C   . PRO   B  1 144 ? 10.009  -3.650  -15.675 1.00 24.67  0  159 PRO   B C   1 
ATOM   3158 O  O   . PRO   B  1 144 ? 9.643   -4.010  -14.564 1.00 26.92  0  159 PRO   B O   1 
ATOM   3159 C  CB  . PRO   B  1 144 ? 8.588   -4.888  -17.360 1.00 30.85  0  159 PRO   B CB  1 
ATOM   3160 C  CG  . PRO   B  1 144 ? 8.039   -5.970  -16.429 1.00 30.31  0  159 PRO   B CG  1 
ATOM   3161 C  CD  . PRO   B  1 144 ? 9.234   -6.872  -16.180 1.00 28.14  0  159 PRO   B CD  1 
ATOM   3162 N  N   . LEU   B  1 145 ? 10.443  -2.414  -15.917 1.00 27.01  0  160 LEU   B N   1 
ATOM   3163 C  CA  . LEU   B  1 145 ? 10.271  -1.320  -14.925 1.00 25.28  0  160 LEU   B CA  1 
ATOM   3164 C  C   . LEU   B  1 145 ? 8.779   -1.149  -14.629 1.00 28.32  0  160 LEU   B C   1 
ATOM   3165 O  O   . LEU   B  1 145 ? 7.979   -0.978  -15.605 1.00 29.99  0  160 LEU   B O   1 
ATOM   3166 C  CB  . LEU   B  1 145 ? 10.900  -0.035  -15.450 1.00 26.17  0  160 LEU   B CB  1 
ATOM   3167 C  CG  . LEU   B  1 145 ? 10.652  1.201   -14.569 1.00 27.55  0  160 LEU   B CG  1 
ATOM   3168 C  CD1 . LEU   B  1 145 ? 11.218  0.989   -13.175 1.00 29.87  0  160 LEU   B CD1 1 
ATOM   3169 C  CD2 . LEU   B  1 145 ? 11.281  2.419   -15.207 1.00 28.29  0  160 LEU   B CD2 1 
ATOM   3170 N  N   . LYS   B  1 146 ? 8.383   -1.179  -13.350 1.00 28.51  0  161 LYS   B N   1 
ATOM   3171 C  CA  . LYS   B  1 146 ? 6.948   -1.032  -12.959 1.00 27.12  0  161 LYS   B CA  1 
ATOM   3172 C  C   . LYS   B  1 146 ? 6.699   0.333   -12.293 1.00 27.97  0  161 LYS   B C   1 
ATOM   3173 O  O   . LYS   B  1 146 ? 7.642   0.989   -11.850 1.00 27.93  0  161 LYS   B O   1 
ATOM   3174 C  CB  . LYS   B  1 146 ? 6.446   -2.199  -12.107 1.00 28.60  0  161 LYS   B CB  1 
ATOM   3175 C  CG  . LYS   B  1 146 ? 6.548   -3.576  -12.766 1.00 34.55  0  161 LYS   B CG  1 
ATOM   3176 C  CD  . LYS   B  1 146 ? 5.583   -4.605  -12.229 1.00 38.57  0  161 LYS   B CD  1 
ATOM   3177 C  CE  . LYS   B  1 146 ? 4.298   -4.590  -13.013 1.00 43.54  0  161 LYS   B CE  1 
ATOM   3178 N  NZ  . LYS   B  1 146 ? 3.455   -5.762  -12.683 1.00 49.31  1  161 LYS   B NZ  1 
ATOM   3179 N  N   . GLN   B  1 147 ? 5.439   0.742   -12.247 1.00 24.79  0  162 GLN   B N   1 
ATOM   3180 C  CA  . GLN   B  1 147 ? 4.978   2.053   -11.722 1.00 27.46  0  162 GLN   B CA  1 
ATOM   3181 C  C   . GLN   B  1 147 ? 3.682   1.777   -10.970 1.00 28.58  0  162 GLN   B C   1 
ATOM   3182 O  O   . GLN   B  1 147 ? 2.966   0.851   -11.368 1.00 28.97  0  162 GLN   B O   1 
ATOM   3183 C  CB  . GLN   B  1 147 ? 4.773   3.044   -12.870 1.00 29.26  0  162 GLN   B CB  1 
ATOM   3184 C  CG  . GLN   B  1 147 ? 3.692   2.614   -13.871 1.00 31.84  0  162 GLN   B CG  1 
ATOM   3185 C  CD  . GLN   B  1 147 ? 3.442   3.584   -15.005 1.00 33.66  0  162 GLN   B CD  1 
ATOM   3186 O  OE1 . GLN   B  1 147 ? 4.329   4.271   -15.487 1.00 28.58  0  162 GLN   B OE1 1 
ATOM   3187 N  NE2 . GLN   B  1 147 ? 2.211   3.641   -15.461 1.00 32.16  0  162 GLN   B NE2 1 
ATOM   3188 N  N   . VAL   B  1 148 ? 3.419   2.506   -9.891  1.00 28.26  0  163 VAL   B N   1 
ATOM   3189 C  CA  . VAL   B  1 148 ? 2.087   2.483   -9.245  1.00 28.26  0  163 VAL   B CA  1 
ATOM   3190 C  C   . VAL   B  1 148 ? 1.785   3.866   -8.672  1.00 30.08  0  163 VAL   B C   1 
ATOM   3191 O  O   . VAL   B  1 148 ? 2.703   4.518   -8.168  1.00 29.04  0  163 VAL   B O   1 
ATOM   3192 C  CB  . VAL   B  1 148 ? 2.010   1.341   -8.218  1.00 29.03  0  163 VAL   B CB  1 
ATOM   3193 C  CG1 . VAL   B  1 148 ? 2.935   1.572   -7.011  1.00 28.20  0  163 VAL   B CG1 1 
ATOM   3194 C  CG2 . VAL   B  1 148 ? 0.561   1.061   -7.827  1.00 28.23  0  163 VAL   B CG2 1 
ATOM   3195 N  N   . LYS   B  1 149 ? 0.530   4.304   -8.826  1.00 35.02  0  164 LYS   B N   1 
ATOM   3196 C  CA  . LYS   B  1 149 ? 0.002   5.552   -8.224  1.00 36.73  0  164 LYS   B CA  1 
ATOM   3197 C  C   . LYS   B  1 149 ? -0.322  5.235   -6.761  1.00 33.11  0  164 LYS   B C   1 
ATOM   3198 O  O   . LYS   B  1 149 ? -1.066  4.298   -6.510  1.00 32.25  0  164 LYS   B O   1 
ATOM   3199 C  CB  . LYS   B  1 149 ? -1.219  6.086   -8.997  1.00 41.54  0  164 LYS   B CB  1 
ATOM   3200 C  CG  . LYS   B  1 149 ? -1.822  7.390   -8.464  1.00 42.15  0  164 LYS   B CG  1 
ATOM   3201 C  CD  . LYS   B  1 149 ? -2.892  8.025   -9.359  1.00 44.77  0  164 LYS   B CD  1 
ATOM   3202 C  CE  . LYS   B  1 149 ? -4.083  7.130   -9.644  1.00 44.70  0  164 LYS   B CE  1 
ATOM   3203 N  NZ  . LYS   B  1 149 ? -5.060  7.805   -10.536 0.00 44.49  1  164 LYS   B NZ  1 
ATOM   3204 N  N   . VAL   B  1 150 ? 0.215   6.020   -5.836  1.00 32.38  0  165 VAL   B N   1 
ATOM   3205 C  CA  . VAL   B  1 150 ? 0.050   5.855   -4.365  1.00 30.83  0  165 VAL   B CA  1 
ATOM   3206 C  C   . VAL   B  1 150 ? -0.302  7.234   -3.811  1.00 36.76  0  165 VAL   B C   1 
ATOM   3207 O  O   . VAL   B  1 150 ? 0.356   8.245   -4.092  1.00 37.01  0  165 VAL   B O   1 
ATOM   3208 C  CB  . VAL   B  1 150 ? 1.319   5.298   -3.694  1.00 30.79  0  165 VAL   B CB  1 
ATOM   3209 C  CG1 . VAL   B  1 150 ? 1.550   3.830   -4.027  1.00 32.26  0  165 VAL   B CG1 1 
ATOM   3210 C  CG2 . VAL   B  1 150 ? 2.580   6.081   -4.034  1.00 31.86  0  165 VAL   B CG2 1 
ATOM   3211 N  N   . PRO   B  1 151 ? -1.374  7.333   -3.013  1.00 39.82  0  166 PRO   B N   1 
ATOM   3212 C  CA  . PRO   B  1 151 ? -1.719  8.606   -2.381  1.00 44.12  0  166 PRO   B CA  1 
ATOM   3213 C  C   . PRO   B  1 151 ? -0.764  8.882   -1.204  1.00 42.27  0  166 PRO   B C   1 
ATOM   3214 O  O   . PRO   B  1 151 ? -0.505  7.986   -0.397  1.00 38.11  0  166 PRO   B O   1 
ATOM   3215 C  CB  . PRO   B  1 151 ? -3.167  8.380   -1.955  1.00 43.83  0  166 PRO   B CB  1 
ATOM   3216 C  CG  . PRO   B  1 151 ? -3.230  6.890   -1.670  1.00 48.18  0  166 PRO   B CG  1 
ATOM   3217 C  CD  . PRO   B  1 151 ? -2.294  6.239   -2.664  1.00 43.09  0  166 PRO   B CD  1 
ATOM   3218 N  N   . ILE   B  1 152 ? -0.294  10.125  -1.120  1.00 44.42  0  167 ILE   B N   1 
ATOM   3219 C  CA  . ILE   B  1 152 ? 0.391   10.685  0.084   1.00 41.29  0  167 ILE   B CA  1 
ATOM   3220 C  C   . ILE   B  1 152 ? -0.572  10.663  1.269   1.00 37.64  0  167 ILE   B C   1 
ATOM   3221 O  O   . ILE   B  1 152 ? -1.765  10.938  1.101   1.00 35.12  0  167 ILE   B O   1 
ATOM   3222 C  CB  . ILE   B  1 152 ? 0.895   12.108  -0.171  1.00 41.51  0  167 ILE   B CB  1 
ATOM   3223 C  CG1 . ILE   B  1 152 ? 1.977   12.118  -1.237  1.00 40.47  0  167 ILE   B CG1 1 
ATOM   3224 C  CG2 . ILE   B  1 152 ? 1.386   12.789  1.110   1.00 49.01  0  167 ILE   B CG2 1 
ATOM   3225 C  CD1 . ILE   B  1 152 ? 3.305   11.585  -0.798  1.00 41.05  0  167 ILE   B CD1 1 
ATOM   3226 N  N   A MET   B  1 153 ? -0.043  10.314  2.438   0.50 37.70  0  168 MET   B N   1 
ATOM   3227 N  N   B MET   B  1 153 ? -0.052  10.292  2.436   0.50 36.84  0  168 MET   B N   1 
ATOM   3228 C  CA  A MET   B  1 153 ? -0.786  10.254  3.714   0.50 39.93  0  168 MET   B CA  1 
ATOM   3229 C  CA  B MET   B  1 153 ? -0.814  10.281  3.705   0.50 38.48  0  168 MET   B CA  1 
ATOM   3230 C  C   A MET   B  1 153 ? -0.019  11.092  4.737   0.50 38.82  0  168 MET   B C   1 
ATOM   3231 C  C   B MET   B  1 153 ? -0.025  11.094  4.735   0.50 38.00  0  168 MET   B C   1 
ATOM   3232 O  O   A MET   B  1 153 ? 1.248   11.047  4.721   0.50 40.10  0  168 MET   B O   1 
ATOM   3233 O  O   B MET   B  1 153 ? 1.239   11.049  4.718   0.50 39.50  0  168 MET   B O   1 
ATOM   3234 C  CB  A MET   B  1 153 ? -0.875  8.801   4.177   0.50 42.98  0  168 MET   B CB  1 
ATOM   3235 C  CB  B MET   B  1 153 ? -1.038  8.851   4.198   0.50 40.21  0  168 MET   B CB  1 
ATOM   3236 C  CG  A MET   B  1 153 ? -1.427  8.582   5.567   0.50 45.85  0  168 MET   B CG  1 
ATOM   3237 C  CG  B MET   B  1 153 ? -1.502  7.898   3.113   0.50 41.59  0  168 MET   B CG  1 
ATOM   3238 S  SD  A MET   B  1 153 ? -1.126  6.859   6.071   0.50 44.81  0  168 MET   B SD  1 
ATOM   3239 S  SD  B MET   B  1 153 ? -3.120  7.186   3.430   0.50 39.64  0  168 MET   B SD  1 
ATOM   3240 C  CE  A MET   B  1 153 ? -2.299  5.980   5.035   0.50 48.25  0  168 MET   B CE  1 
ATOM   3241 C  CE  B MET   B  1 153 ? -2.824  6.263   4.931   0.50 42.55  0  168 MET   B CE  1 
ATOM   3242 N  N   . GLU   B  1 154 ? -0.747  11.850  5.559   1.00 36.61  0  169 GLU   B N   1 
ATOM   3243 C  CA  . GLU   B  1 154 ? -0.156  12.700  6.618   1.00 40.80  0  169 GLU   B CA  1 
ATOM   3244 C  C   . GLU   B  1 154 ? 0.642   11.802  7.581   1.00 34.49  0  169 GLU   B C   1 
ATOM   3245 O  O   . GLU   B  1 154 ? 0.198   10.704  7.884   1.00 29.53  0  169 GLU   B O   1 
ATOM   3246 C  CB  . GLU   B  1 154 ? -1.267  13.483  7.310   1.00 48.25  0  169 GLU   B CB  1 
ATOM   3247 C  CG  . GLU   B  1 154 ? -0.788  14.634  8.162   1.00 54.49  0  169 GLU   B CG  1 
ATOM   3248 C  CD  . GLU   B  1 154 ? -1.941  15.177  8.980   1.00 59.66  0  169 GLU   B CD  1 
ATOM   3249 O  OE1 . GLU   B  1 154 ? -2.482  14.405  9.769   1.00 62.29  0  169 GLU   B OE1 1 
ATOM   3250 O  OE2 . GLU   B  1 154 ? -2.352  16.316  8.753   1.00 60.52  -1 169 GLU   B OE2 1 
ATOM   3251 N  N   . ASN   B  1 155 ? 1.793   12.266  8.025   1.00 31.31  0  170 ASN   B N   1 
ATOM   3252 C  CA  . ASN   B  1 155 ? 2.638   11.549  9.010   1.00 32.49  0  170 ASN   B CA  1 
ATOM   3253 C  C   . ASN   B  1 155 ? 1.832   11.142  10.234  1.00 36.89  0  170 ASN   B C   1 
ATOM   3254 O  O   . ASN   B  1 155 ? 2.035   10.031  10.683  1.00 40.50  0  170 ASN   B O   1 
ATOM   3255 C  CB  . ASN   B  1 155 ? 3.865   12.348  9.429   1.00 32.77  0  170 ASN   B CB  1 
ATOM   3256 C  CG  . ASN   B  1 155 ? 5.007   12.107  8.482   1.00 30.80  0  170 ASN   B CG  1 
ATOM   3257 O  OD1 . ASN   B  1 155 ? 4.785   11.832  7.313   1.00 36.66  0  170 ASN   B OD1 1 
ATOM   3258 N  ND2 . ASN   B  1 155 ? 6.229   12.268  8.946   1.00 29.42  0  170 ASN   B ND2 1 
ATOM   3259 N  N   . HIS   B  1 156 ? 0.957   11.995  10.753  1.00 36.88  0  171 HIS   B N   1 
ATOM   3260 C  CA  . HIS   B  1 156 ? 0.213   11.703  11.992  1.00 36.03  0  171 HIS   B CA  1 
ATOM   3261 C  C   . HIS   B  1 156 ? -0.714  10.498  11.751  1.00 36.30  0  171 HIS   B C   1 
ATOM   3262 O  O   . HIS   B  1 156 ? -0.716  9.594   12.604  1.00 31.69  0  171 HIS   B O   1 
ATOM   3263 C  CB  . HIS   B  1 156 ? -0.472  12.963  12.514  1.00 40.65  0  171 HIS   B CB  1 
ATOM   3264 C  CG  . HIS   B  1 156 ? -1.186  12.735  13.798  1.00 43.22  0  171 HIS   B CG  1 
ATOM   3265 N  ND1 . HIS   B  1 156 ? -0.554  12.785  15.027  1.00 44.84  0  171 HIS   B ND1 1 
ATOM   3266 C  CD2 . HIS   B  1 156 ? -2.458  12.376  14.035  1.00 43.80  0  171 HIS   B CD2 1 
ATOM   3267 C  CE1 . HIS   B  1 156 ? -1.424  12.501  15.967  1.00 49.03  0  171 HIS   B CE1 1 
ATOM   3268 N  NE2 . HIS   B  1 156 ? -2.609  12.273  15.385  1.00 46.85  0  171 HIS   B NE2 1 
ATOM   3269 N  N   . ILE   B  1 157 ? -1.372  10.419  10.598  1.00 33.31  0  172 ILE   B N   1 
ATOM   3270 C  CA  . ILE   B  1 157 ? -2.274  9.287   10.244  1.00 31.93  0  172 ILE   B CA  1 
ATOM   3271 C  C   . ILE   B  1 157 ? -1.474  7.985   10.072  1.00 33.51  0  172 ILE   B C   1 
ATOM   3272 O  O   . ILE   B  1 157 ? -1.937  6.898   10.508  1.00 35.82  0  172 ILE   B O   1 
ATOM   3273 C  CB  . ILE   B  1 157 ? -3.068  9.607   8.970   1.00 35.11  0  172 ILE   B CB  1 
ATOM   3274 C  CG1 . ILE   B  1 157 ? -4.003  10.799  9.183   1.00 38.43  0  172 ILE   B CG1 1 
ATOM   3275 C  CG2 . ILE   B  1 157 ? -3.838  8.395   8.481   1.00 31.26  0  172 ILE   B CG2 1 
ATOM   3276 C  CD1 . ILE   B  1 157 ? -4.952  10.672  10.361  1.00 37.71  0  172 ILE   B CD1 1 
ATOM   3277 N  N   A CYS   B  1 158 ? -0.341  8.077   9.406   0.50 30.49  0  173 CYS   B N   1 
ATOM   3278 N  N   B CYS   B  1 158 ? -0.327  8.062   9.397   0.50 31.36  0  173 CYS   B N   1 
ATOM   3279 C  CA  A CYS   B  1 158 ? 0.522   6.921   9.090   0.50 32.52  0  173 CYS   B CA  1 
ATOM   3280 C  CA  B CYS   B  1 158 ? 0.513   6.874   9.090   0.50 34.14  0  173 CYS   B CA  1 
ATOM   3281 C  C   A CYS   B  1 158 ? 1.106   6.360   10.391  0.50 31.58  0  173 CYS   B C   1 
ATOM   3282 C  C   B CYS   B  1 158 ? 1.111   6.349   10.396  0.50 32.42  0  173 CYS   B C   1 
ATOM   3283 O  O   A CYS   B  1 158 ? 1.050   5.115   10.583  0.50 29.36  0  173 CYS   B O   1 
ATOM   3284 O  O   B CYS   B  1 158 ? 1.075   5.109   10.586  0.50 30.11  0  173 CYS   B O   1 
ATOM   3285 C  CB  A CYS   B  1 158 ? 1.587   7.363   8.110   0.50 33.58  0  173 CYS   B CB  1 
ATOM   3286 C  CB  B CYS   B  1 158 ? 1.598   7.163   8.061   0.50 35.97  0  173 CYS   B CB  1 
ATOM   3287 S  SG  A CYS   B  1 158 ? 2.769   6.067   7.709   0.50 34.57  0  173 CYS   B SG  1 
ATOM   3288 S  SG  B CYS   B  1 158 ? 0.924   7.437   6.398   0.50 40.80  0  173 CYS   B SG  1 
ATOM   3289 N  N   . ASP   B  1 159 ? 1.572   7.255   11.271  1.00 31.45  0  174 ASP   B N   1 
ATOM   3290 C  CA  . ASP   B  1 159 ? 2.062   6.918   12.635  1.00 32.30  0  174 ASP   B CA  1 
ATOM   3291 C  C   . ASP   B  1 159 ? 0.944   6.198   13.395  1.00 31.87  0  174 ASP   B C   1 
ATOM   3292 O  O   . ASP   B  1 159 ? 1.203   5.107   13.931  1.00 26.18  0  174 ASP   B O   1 
ATOM   3293 C  CB  . ASP   B  1 159 ? 2.534   8.138   13.414  1.00 32.18  0  174 ASP   B CB  1 
ATOM   3294 C  CG  . ASP   B  1 159 ? 3.253   7.772   14.705  1.00 32.07  0  174 ASP   B CG  1 
ATOM   3295 O  OD1 . ASP   B  1 159 ? 4.306   7.098   14.638  1.00 31.88  0  174 ASP   B OD1 1 
ATOM   3296 O  OD2 . ASP   B  1 159 ? 2.696   8.067   15.771  1.00 35.23  -1 174 ASP   B OD2 1 
ATOM   3297 N  N   . ALA   B  1 160 ? -0.273  6.744   13.359  1.00 29.42  0  175 ALA   B N   1 
ATOM   3298 C  CA  . ALA   B  1 160 ? -1.443  6.138   14.028  1.00 32.96  0  175 ALA   B CA  1 
ATOM   3299 C  C   . ALA   B  1 160 ? -1.677  4.730   13.460  1.00 33.26  0  175 ALA   B C   1 
ATOM   3300 O  O   . ALA   B  1 160 ? -1.895  3.796   14.268  1.00 35.47  0  175 ALA   B O   1 
ATOM   3301 C  CB  . ALA   B  1 160 ? -2.661  7.035   13.928  1.00 31.30  0  175 ALA   B CB  1 
ATOM   3302 N  N   . LYS   B  1 161 ? -1.598  4.538   12.139  1.00 31.43  0  176 LYS   B N   1 
ATOM   3303 C  CA  . LYS   B  1 161 ? -1.835  3.207   11.538  1.00 30.36  0  176 LYS   B CA  1 
ATOM   3304 C  C   . LYS   B  1 161 ? -0.796  2.205   12.057  1.00 26.69  0  176 LYS   B C   1 
ATOM   3305 O  O   . LYS   B  1 161 ? -1.180  1.099   12.440  1.00 30.01  0  176 LYS   B O   1 
ATOM   3306 C  CB  . LYS   B  1 161 ? -1.817  3.290   10.016  1.00 32.87  0  176 LYS   B CB  1 
ATOM   3307 C  CG  . LYS   B  1 161 ? -3.048  3.939   9.416   1.00 37.16  0  176 LYS   B CG  1 
ATOM   3308 C  CD  . LYS   B  1 161 ? -3.090  3.684   7.933   1.00 40.92  0  176 LYS   B CD  1 
ATOM   3309 C  CE  . LYS   B  1 161 ? -4.240  4.363   7.242   1.00 44.26  0  176 LYS   B CE  1 
ATOM   3310 N  NZ  . LYS   B  1 161 ? -5.533  4.026   7.873   1.00 50.44  1  176 LYS   B NZ  1 
ATOM   3311 N  N   . TYR   B  1 162 ? 0.468   2.583   12.117  1.00 26.59  0  177 TYR   B N   1 
ATOM   3312 C  CA  . TYR   B  1 162 ? 1.550   1.655   12.558  1.00 28.18  0  177 TYR   B CA  1 
ATOM   3313 C  C   . TYR   B  1 162 ? 1.327   1.200   14.009  1.00 30.05  0  177 TYR   B C   1 
ATOM   3314 O  O   . TYR   B  1 162 ? 1.865   0.142   14.366  1.00 30.41  0  177 TYR   B O   1 
ATOM   3315 C  CB  . TYR   B  1 162 ? 2.935   2.242   12.288  1.00 25.92  0  177 TYR   B CB  1 
ATOM   3316 C  CG  . TYR   B  1 162 ? 3.496   1.771   10.969  1.00 25.46  0  177 TYR   B CG  1 
ATOM   3317 C  CD1 . TYR   B  1 162 ? 3.069   2.331   9.771   1.00 26.16  0  177 TYR   B CD1 1 
ATOM   3318 C  CD2 . TYR   B  1 162 ? 4.395   0.723   10.904  1.00 27.76  0  177 TYR   B CD2 1 
ATOM   3319 C  CE1 . TYR   B  1 162 ? 3.601   1.929   8.552   1.00 26.31  0  177 TYR   B CE1 1 
ATOM   3320 C  CE2 . TYR   B  1 162 ? 4.902   0.281   9.684   1.00 27.99  0  177 TYR   B CE2 1 
ATOM   3321 C  CZ  . TYR   B  1 162 ? 4.499   0.878   8.506   1.00 27.26  0  177 TYR   B CZ  1 
ATOM   3322 O  OH  . TYR   B  1 162 ? 4.946   0.422   7.306   1.00 27.64  0  177 TYR   B OH  1 
ATOM   3323 N  N   . HIS   B  1 163 ? 0.550   1.950   14.800  1.00 33.14  0  178 HIS   B N   1 
ATOM   3324 C  CA  . HIS   B  1 163 ? 0.233   1.646   16.223  1.00 29.76  0  178 HIS   B CA  1 
ATOM   3325 C  C   . HIS   B  1 163 ? -0.961  0.695   16.328  1.00 31.73  0  178 HIS   B C   1 
ATOM   3326 O  O   . HIS   B  1 163 ? -1.078  0.062   17.393  1.00 32.92  0  178 HIS   B O   1 
ATOM   3327 C  CB  . HIS   B  1 163 ? -0.011  2.938   17.010  1.00 29.29  0  178 HIS   B CB  1 
ATOM   3328 C  CG  . HIS   B  1 163 ? 1.235   3.680   17.345  1.00 29.35  0  178 HIS   B CG  1 
ATOM   3329 N  ND1 . HIS   B  1 163 ? 1.850   4.562   16.486  1.00 29.66  0  178 HIS   B ND1 1 
ATOM   3330 C  CD2 . HIS   B  1 163 ? 1.981   3.692   18.463  1.00 32.42  0  178 HIS   B CD2 1 
ATOM   3331 C  CE1 . HIS   B  1 163 ? 2.912   5.078   17.057  1.00 28.19  0  178 HIS   B CE1 1 
ATOM   3332 N  NE2 . HIS   B  1 163 ? 3.005   4.575   18.265  1.00 26.87  0  178 HIS   B NE2 1 
ATOM   3333 N  N   . LEU   B  1 164 ? -1.814  0.590   15.303  1.00 29.62  0  179 LEU   B N   1 
ATOM   3334 C  CA  . LEU   B  1 164 ? -2.970  -0.341  15.336  1.00 30.95  0  179 LEU   B CA  1 
ATOM   3335 C  C   . LEU   B  1 164 ? -2.410  -1.770  15.271  1.00 29.33  0  179 LEU   B C   1 
ATOM   3336 O  O   . LEU   B  1 164 ? -1.620  -2.008  14.376  1.00 26.48  0  179 LEU   B O   1 
ATOM   3337 C  CB  . LEU   B  1 164 ? -3.914  -0.050  14.167  1.00 33.05  0  179 LEU   B CB  1 
ATOM   3338 C  CG  . LEU   B  1 164 ? -4.666  1.282   14.243  1.00 40.83  0  179 LEU   B CG  1 
ATOM   3339 C  CD1 . LEU   B  1 164 ? -5.450  1.541   12.959  1.00 40.19  0  179 LEU   B CD1 1 
ATOM   3340 C  CD2 . LEU   B  1 164 ? -5.619  1.308   15.440  1.00 41.82  0  179 LEU   B CD2 1 
ATOM   3341 N  N   . GLY   B  1 165 ? -2.786  -2.647  16.207  1.00 27.99  0  180 GLY   B N   1 
ATOM   3342 C  CA  . GLY   B  1 165 ? -2.316  -4.045  16.239  1.00 28.79  0  180 GLY   B CA  1 
ATOM   3343 C  C   . GLY   B  1 165 ? -0.854  -4.112  16.659  1.00 30.75  0  180 GLY   B C   1 
ATOM   3344 O  O   . GLY   B  1 165 ? -0.170  -5.094  16.298  1.00 28.06  0  180 GLY   B O   1 
ATOM   3345 N  N   . ALA   B  1 166 ? -0.393  -3.105  17.412  1.00 28.35  0  181 ALA   B N   1 
ATOM   3346 C  CA  . ALA   B  1 166 ? 0.977   -3.040  17.960  1.00 31.89  0  181 ALA   B CA  1 
ATOM   3347 C  C   . ALA   B  1 166 ? 0.939   -2.777  19.464  1.00 27.96  0  181 ALA   B C   1 
ATOM   3348 O  O   . ALA   B  1 166 ? 0.007   -2.148  19.947  1.00 29.92  0  181 ALA   B O   1 
ATOM   3349 C  CB  . ALA   B  1 166 ? 1.797   -1.982  17.262  1.00 27.47  0  181 ALA   B CB  1 
ATOM   3350 N  N   . TYR   B  1 167 ? 1.978   -3.217  20.169  1.00 29.78  0  182 TYR   B N   1 
ATOM   3351 C  CA  . TYR   B  1 167 ? 2.151   -2.998  21.634  1.00 28.77  0  182 TYR   B CA  1 
ATOM   3352 C  C   . TYR   B  1 167 ? 2.722   -1.590  21.864  1.00 29.49  0  182 TYR   B C   1 
ATOM   3353 O  O   . TYR   B  1 167 ? 2.661   -1.112  22.991  1.00 29.72  0  182 TYR   B O   1 
ATOM   3354 C  CB  . TYR   B  1 167 ? 3.068   -4.072  22.221  1.00 29.22  0  182 TYR   B CB  1 
ATOM   3355 C  CG  . TYR   B  1 167 ? 2.505   -5.472  22.190  1.00 33.63  0  182 TYR   B CG  1 
ATOM   3356 C  CD1 . TYR   B  1 167 ? 1.521   -5.858  23.093  1.00 33.47  0  182 TYR   B CD1 1 
ATOM   3357 C  CD2 . TYR   B  1 167 ? 3.021   -6.446  21.335  1.00 33.35  0  182 TYR   B CD2 1 
ATOM   3358 C  CE1 . TYR   B  1 167 ? 1.043   -7.160  23.133  1.00 33.70  0  182 TYR   B CE1 1 
ATOM   3359 C  CE2 . TYR   B  1 167 ? 2.528   -7.742  21.340  1.00 31.75  0  182 TYR   B CE2 1 
ATOM   3360 C  CZ  . TYR   B  1 167 ? 1.523   -8.095  22.225  1.00 36.04  0  182 TYR   B CZ  1 
ATOM   3361 O  OH  . TYR   B  1 167 ? 0.995   -9.360  22.228  1.00 36.36  0  182 TYR   B OH  1 
ATOM   3362 N  N   . THR   B  1 168 ? 3.293   -0.943  20.840  1.00 25.75  0  183 THR   B N   1 
ATOM   3363 C  CA  . THR   B  1 168 ? 4.004   0.338   21.004  1.00 24.52  0  183 THR   B CA  1 
ATOM   3364 C  C   . THR   B  1 168 ? 2.999   1.350   21.546  1.00 26.31  0  183 THR   B C   1 
ATOM   3365 O  O   . THR   B  1 168 ? 1.888   1.418   20.975  1.00 23.50  0  183 THR   B O   1 
ATOM   3366 C  CB  . THR   B  1 168 ? 4.597   0.820   19.676  1.00 25.04  0  183 THR   B CB  1 
ATOM   3367 O  OG1 . THR   B  1 168 ? 5.379   -0.211  19.065  1.00 27.71  0  183 THR   B OG1 1 
ATOM   3368 C  CG2 . THR   B  1 168 ? 5.463   2.048   19.842  1.00 24.56  0  183 THR   B CG2 1 
ATOM   3369 N  N   . GLY   B  1 169 ? 3.394   2.118   22.556  1.00 26.66  0  184 GLY   B N   1 
ATOM   3370 C  CA  . GLY   B  1 169 ? 2.563   3.191   23.122  1.00 30.95  0  184 GLY   B CA  1 
ATOM   3371 C  C   . GLY   B  1 169 ? 2.228   4.248   22.089  1.00 28.89  0  184 GLY   B C   1 
ATOM   3372 O  O   . GLY   B  1 169 ? 3.096   4.581   21.264  1.00 28.66  0  184 GLY   B O   1 
ATOM   3373 N  N   . ASP   B  1 170 ? 1.004   4.759   22.129  1.00 32.90  0  185 ASP   B N   1 
ATOM   3374 C  CA  . ASP   B  1 170 ? 0.451   5.720   21.130  1.00 36.65  0  185 ASP   B CA  1 
ATOM   3375 C  C   . ASP   B  1 170 ? 1.258   7.024   21.071  1.00 36.22  0  185 ASP   B C   1 
ATOM   3376 O  O   . ASP   B  1 170 ? 1.292   7.656   19.988  1.00 45.49  0  185 ASP   B O   1 
ATOM   3377 C  CB  . ASP   B  1 170 ? -1.017  6.015   21.419  1.00 37.90  0  185 ASP   B CB  1 
ATOM   3378 C  CG  . ASP   B  1 170 ? -1.932  4.840   21.154  1.00 40.09  0  185 ASP   B CG  1 
ATOM   3379 O  OD1 . ASP   B  1 170 ? -1.602  3.985   20.288  1.00 36.28  0  185 ASP   B OD1 1 
ATOM   3380 O  OD2 . ASP   B  1 170 ? -2.944  4.768   21.854  1.00 53.69  -1 185 ASP   B OD2 1 
ATOM   3381 N  N   . ASP   B  1 171 ? 1.923   7.401   22.160  1.00 37.37  0  186 ASP   B N   1 
ATOM   3382 C  CA  . ASP   B  1 171 ? 2.761   8.628   22.307  1.00 41.66  0  186 ASP   B CA  1 
ATOM   3383 C  C   . ASP   B  1 171 ? 4.203   8.356   21.868  1.00 38.23  0  186 ASP   B C   1 
ATOM   3384 O  O   . ASP   B  1 171 ? 5.012   9.290   21.947  1.00 39.77  0  186 ASP   B O   1 
ATOM   3385 C  CB  . ASP   B  1 171 ? 2.792   9.103   23.769  1.00 49.98  0  186 ASP   B CB  1 
ATOM   3386 C  CG  . ASP   B  1 171 ? 3.423   8.058   24.695  1.00 58.40  0  186 ASP   B CG  1 
ATOM   3387 O  OD1 . ASP   B  1 171 ? 2.878   6.919   24.757  1.00 60.75  0  186 ASP   B OD1 1 
ATOM   3388 O  OD2 . ASP   B  1 171 ? 4.496   8.343   25.269  1.00 69.89  -1 186 ASP   B OD2 1 
ATOM   3389 N  N   . VAL   B  1 172 ? 4.547   7.124   21.481  1.00 34.63  0  187 VAL   B N   1 
ATOM   3390 C  CA  . VAL   B  1 172 ? 5.929   6.755   21.047  1.00 33.88  0  187 VAL   B CA  1 
ATOM   3391 C  C   . VAL   B  1 172 ? 5.923   6.744   19.524  1.00 33.06  0  187 VAL   B C   1 
ATOM   3392 O  O   . VAL   B  1 172 ? 5.217   5.925   18.932  1.00 32.83  0  187 VAL   B O   1 
ATOM   3393 C  CB  . VAL   B  1 172 ? 6.363   5.404   21.629  1.00 34.33  0  187 VAL   B CB  1 
ATOM   3394 C  CG1 . VAL   B  1 172 ? 7.737   4.999   21.147  1.00 35.39  0  187 VAL   B CG1 1 
ATOM   3395 C  CG2 . VAL   B  1 172 ? 6.306   5.434   23.142  1.00 33.90  0  187 VAL   B CG2 1 
ATOM   3396 N  N   . ARG   B  1 173 ? 6.698   7.633   18.938  1.00 30.80  0  188 ARG   B N   1 
ATOM   3397 C  CA  . ARG   B  1 173 ? 6.674   7.914   17.487  1.00 34.14  0  188 ARG   B CA  1 
ATOM   3398 C  C   . ARG   B  1 173 ? 7.297   6.729   16.734  1.00 31.92  0  188 ARG   B C   1 
ATOM   3399 O  O   . ARG   B  1 173 ? 8.394   6.268   17.141  1.00 26.51  0  188 ARG   B O   1 
ATOM   3400 C  CB  . ARG   B  1 173 ? 7.444   9.205   17.187  1.00 34.24  0  188 ARG   B CB  1 
ATOM   3401 C  CG  . ARG   B  1 173 ? 6.856   9.942   16.008  1.00 40.31  0  188 ARG   B CG  1 
ATOM   3402 C  CD  . ARG   B  1 173 ? 5.628   10.794  16.325  1.00 42.95  0  188 ARG   B CD  1 
ATOM   3403 N  NE  . ARG   B  1 173 ? 5.179   11.295  15.022  1.00 51.45  0  188 ARG   B NE  1 
ATOM   3404 C  CZ  . ARG   B  1 173 ? 3.949   11.731  14.697  1.00 58.73  0  188 ARG   B CZ  1 
ATOM   3405 N  NH1 . ARG   B  1 173 ? 2.974   11.740  15.598  1.00 54.08  1  188 ARG   B NH1 1 
ATOM   3406 N  NH2 . ARG   B  1 173 ? 3.702   12.127  13.445  1.00 48.22  0  188 ARG   B NH2 1 
ATOM   3407 N  N   . ILE   B  1 174 ? 6.593   6.184   15.740  1.00 27.83  0  189 ILE   B N   1 
ATOM   3408 C  CA  . ILE   B  1 174 ? 7.158   5.156   14.815  1.00 28.59  0  189 ILE   B CA  1 
ATOM   3409 C  C   . ILE   B  1 174 ? 7.565   5.845   13.501  1.00 28.31  0  189 ILE   B C   1 
ATOM   3410 O  O   . ILE   B  1 174 ? 8.722   5.656   13.054  1.00 26.45  0  189 ILE   B O   1 
ATOM   3411 C  CB  . ILE   B  1 174 ? 6.155   4.013   14.608  1.00 27.85  0  189 ILE   B CB  1 
ATOM   3412 C  CG1 . ILE   B  1 174 ? 6.036   3.168   15.877  1.00 30.86  0  189 ILE   B CG1 1 
ATOM   3413 C  CG2 . ILE   B  1 174 ? 6.556   3.162   13.424  1.00 30.52  0  189 ILE   B CG2 1 
ATOM   3414 C  CD1 . ILE   B  1 174 ? 4.804   2.274   15.911  1.00 31.59  0  189 ILE   B CD1 1 
ATOM   3415 N  N   . VAL   B  1 175 ? 6.648   6.609   12.920  1.00 26.62  0  190 VAL   B N   1 
ATOM   3416 C  CA  . VAL   B  1 175 ? 6.900   7.402   11.685  1.00 29.74  0  190 VAL   B CA  1 
ATOM   3417 C  C   . VAL   B  1 175 ? 7.376   8.794   12.098  1.00 29.45  0  190 VAL   B C   1 
ATOM   3418 O  O   . VAL   B  1 175 ? 6.599   9.546   12.683  1.00 28.56  0  190 VAL   B O   1 
ATOM   3419 C  CB  . VAL   B  1 175 ? 5.691   7.509   10.744  1.00 29.03  0  190 VAL   B CB  1 
ATOM   3420 C  CG1 . VAL   B  1 175 ? 6.148   8.113   9.420   1.00 26.99  0  190 VAL   B CG1 1 
ATOM   3421 C  CG2 . VAL   B  1 175 ? 5.001   6.173   10.507  1.00 29.84  0  190 VAL   B CG2 1 
ATOM   3422 N  N   . ARG   B  1 176 ? 8.623   9.099   11.793  1.00 28.37  0  191 ARG   B N   1 
ATOM   3423 C  CA  . ARG   B  1 176 ? 9.325   10.286  12.309  1.00 31.38  0  191 ARG   B CA  1 
ATOM   3424 C  C   . ARG   B  1 176 ? 9.168   11.434  11.299  1.00 34.29  0  191 ARG   B C   1 
ATOM   3425 O  O   . ARG   B  1 176 ? 8.663   11.194  10.185  1.00 29.05  0  191 ARG   B O   1 
ATOM   3426 C  CB  . ARG   B  1 176 ? 10.770  9.881   12.605  1.00 32.99  0  191 ARG   B CB  1 
ATOM   3427 C  CG  . ARG   B  1 176 ? 10.896  8.755   13.621  1.00 36.92  0  191 ARG   B CG  1 
ATOM   3428 C  CD  . ARG   B  1 176 ? 12.294  8.751   14.199  1.00 43.47  0  191 ARG   B CD  1 
ATOM   3429 N  NE  . ARG   B  1 176 ? 12.628  7.502   14.851  1.00 52.75  0  191 ARG   B NE  1 
ATOM   3430 C  CZ  . ARG   B  1 176 ? 12.210  7.125   16.056  1.00 56.15  0  191 ARG   B CZ  1 
ATOM   3431 N  NH1 . ARG   B  1 176 ? 11.422  7.909   16.779  1.00 62.17  1  191 ARG   B NH1 1 
ATOM   3432 N  NH2 . ARG   B  1 176 ? 12.583  5.948   16.525  1.00 61.06  0  191 ARG   B NH2 1 
ATOM   3433 N  N   . ASP   B  1 177 ? 9.591   12.645  11.681  1.00 32.71  0  192 ASP   B N   1 
ATOM   3434 C  CA  . ASP   B  1 177 ? 9.334   13.890  10.915  1.00 35.87  0  192 ASP   B CA  1 
ATOM   3435 C  C   . ASP   B  1 177 ? 10.215  13.939  9.654   1.00 30.24  0  192 ASP   B C   1 
ATOM   3436 O  O   . ASP   B  1 177 ? 9.825   14.628  8.719   1.00 34.76  0  192 ASP   B O   1 
ATOM   3437 C  CB  . ASP   B  1 177 ? 9.533   15.098  11.833  1.00 39.58  0  192 ASP   B CB  1 
ATOM   3438 C  CG  . ASP   B  1 177 ? 8.485   15.194  12.944  1.00 42.35  0  192 ASP   B CG  1 
ATOM   3439 O  OD1 . ASP   B  1 177 ? 7.322   14.832  12.681  1.00 42.50  0  192 ASP   B OD1 1 
ATOM   3440 O  OD2 . ASP   B  1 177 ? 8.818   15.675  14.042  1.00 44.42  -1 192 ASP   B OD2 1 
ATOM   3441 N  N   . ASP   B  1 178 ? 11.341  13.217  9.608   1.00 26.42  0  193 ASP   B N   1 
ATOM   3442 C  CA  . ASP   B  1 178 ? 12.174  13.125  8.377   1.00 24.77  0  193 ASP   B CA  1 
ATOM   3443 C  C   . ASP   B  1 178 ? 11.639  12.019  7.437   1.00 27.48  0  193 ASP   B C   1 
ATOM   3444 O  O   . ASP   B  1 178 ? 12.322  11.741  6.462   1.00 28.80  0  193 ASP   B O   1 
ATOM   3445 C  CB  . ASP   B  1 178 ? 13.652  12.900  8.687   1.00 28.04  0  193 ASP   B CB  1 
ATOM   3446 C  CG  . ASP   B  1 178 ? 13.965  11.577  9.375   1.00 26.89  0  193 ASP   B CG  1 
ATOM   3447 O  OD1 . ASP   B  1 178 ? 13.024  10.987  9.975   1.00 24.90  0  193 ASP   B OD1 1 
ATOM   3448 O  OD2 . ASP   B  1 178 ? 15.164  11.200  9.427   1.00 27.52  -1 193 ASP   B OD2 1 
ATOM   3449 N  N   . MET   B  1 179 ? 10.450  11.450  7.675   1.00 27.27  0  194 MET   B N   1 
ATOM   3450 C  CA  . MET   B  1 179 ? 9.843   10.365  6.859   1.00 25.32  0  194 MET   B CA  1 
ATOM   3451 C  C   . MET   B  1 179 ? 8.552   10.908  6.258   1.00 27.58  0  194 MET   B C   1 
ATOM   3452 O  O   . MET   B  1 179 ? 8.059   11.965  6.702   1.00 28.52  0  194 MET   B O   1 
ATOM   3453 C  CB  . MET   B  1 179 ? 9.533   9.117   7.691   1.00 23.87  0  194 MET   B CB  1 
ATOM   3454 C  CG  . MET   B  1 179 ? 10.795  8.521   8.314   1.00 27.63  0  194 MET   B CG  1 
ATOM   3455 S  SD  . MET   B  1 179 ? 10.502  7.200   9.540   1.00 27.55  0  194 MET   B SD  1 
ATOM   3456 C  CE  . MET   B  1 179 ? 12.182  7.133   10.162  1.00 29.23  0  194 MET   B CE  1 
ATOM   3457 N  N   . LEU   B  1 180 ? 8.071   10.215  5.245   1.00 28.13  0  195 LEU   B N   1 
ATOM   3458 C  CA  . LEU   B  1 180 ? 6.847   10.507  4.476   1.00 30.52  0  195 LEU   B CA  1 
ATOM   3459 C  C   . LEU   B  1 180 ? 6.210   9.144   4.217   1.00 31.25  0  195 LEU   B C   1 
ATOM   3460 O  O   . LEU   B  1 180 ? 6.939   8.172   4.074   1.00 32.31  0  195 LEU   B O   1 
ATOM   3461 C  CB  . LEU   B  1 180 ? 7.305   11.202  3.187   1.00 32.20  0  195 LEU   B CB  1 
ATOM   3462 C  CG  . LEU   B  1 180 ? 6.214   11.504  2.164   1.00 37.23  0  195 LEU   B CG  1 
ATOM   3463 C  CD1 . LEU   B  1 180 ? 6.533   12.749  1.368   1.00 38.04  0  195 LEU   B CD1 1 
ATOM   3464 C  CD2 . LEU   B  1 180 ? 6.025   10.349  1.214   1.00 40.11  0  195 LEU   B CD2 1 
ATOM   3465 N  N   A CYS   B  1 181 ? 4.884   9.084   4.107   0.50 31.64  0  196 CYS   B N   1 
ATOM   3466 N  N   B CYS   B  1 181 ? 4.899   9.091   4.055   0.50 32.47  0  196 CYS   B N   1 
ATOM   3467 C  CA  A CYS   B  1 181 ? 4.081   7.839   4.005   0.50 31.52  0  196 CYS   B CA  1 
ATOM   3468 C  CA  B CYS   B  1 181 ? 4.190   7.815   3.916   0.50 32.58  0  196 CYS   B CA  1 
ATOM   3469 C  C   A CYS   B  1 181 ? 3.183   7.855   2.756   0.50 31.30  0  196 CYS   B C   1 
ATOM   3470 C  C   B CYS   B  1 181 ? 3.163   7.839   2.774   0.50 31.96  0  196 CYS   B C   1 
ATOM   3471 O  O   A CYS   B  1 181 ? 2.594   8.913   2.472   0.50 30.30  0  196 CYS   B O   1 
ATOM   3472 O  O   B CYS   B  1 181 ? 2.513   8.872   2.551   0.50 30.81  0  196 CYS   B O   1 
ATOM   3473 C  CB  A CYS   B  1 181 ? 3.214   7.698   5.251   0.50 36.12  0  196 CYS   B CB  1 
ATOM   3474 C  CB  B CYS   B  1 181 ? 3.636   7.507   5.287   0.50 38.66  0  196 CYS   B CB  1 
ATOM   3475 S  SG  A CYS   B  1 181 ? 4.141   7.205   6.728   0.50 37.97  0  196 CYS   B SG  1 
ATOM   3476 S  SG  B CYS   B  1 181 ? 2.158   6.506   5.177   0.50 40.93  0  196 CYS   B SG  1 
ATOM   3477 N  N   . ALA   B  1 182 ? 3.048   6.714   2.059   1.00 29.36  0  197 ALA   B N   1 
ATOM   3478 C  CA  . ALA   B  1 182 ? 2.137   6.544   0.903   1.00 30.33  0  197 ALA   B CA  1 
ATOM   3479 C  C   . ALA   B  1 182 ? 1.783   5.063   0.721   1.00 32.57  0  197 ALA   B C   1 
ATOM   3480 O  O   . ALA   B  1 182 ? 2.617   4.187   1.052   1.00 28.25  0  197 ALA   B O   1 
ATOM   3481 C  CB  . ALA   B  1 182 ? 2.794   7.097   -0.345  1.00 27.86  0  197 ALA   B CB  1 
ATOM   3482 N  N   . GLY   B  1 183 ? 0.599   4.799   0.172   1.00 32.52  0  198 GLY   B N   1 
ATOM   3483 C  CA  . GLY   B  1 183 ? 0.201   3.454   -0.291  1.00 31.53  0  198 GLY   B CA  1 
ATOM   3484 C  C   . GLY   B  1 183 ? -0.931  2.877   0.542   1.00 35.35  0  198 GLY   B C   1 
ATOM   3485 O  O   . GLY   B  1 183 ? -1.324  3.505   1.542   1.00 36.00  0  198 GLY   B O   1 
ATOM   3486 N  N   . ASN   B  1 184 ? -1.419  1.705   0.146   1.00 32.50  0  199 ASN   B N   1 
ATOM   3487 C  CA  . ASN   B  1 184 ? -2.600  1.026   0.741   1.00 36.61  0  199 ASN   B CA  1 
ATOM   3488 C  C   . ASN   B  1 184 ? -2.403  -0.467  0.488   1.00 32.78  0  199 ASN   B C   1 
ATOM   3489 O  O   . ASN   B  1 184 ? -1.274  -0.861  0.069   1.00 34.84  0  199 ASN   B O   1 
ATOM   3490 C  CB  . ASN   B  1 184 ? -3.917  1.608   0.195   1.00 34.19  0  199 ASN   B CB  1 
ATOM   3491 C  CG  . ASN   B  1 184 ? -3.977  1.552   -1.322  1.00 38.85  0  199 ASN   B CG  1 
ATOM   3492 O  OD1 . ASN   B  1 184 ? -3.642  0.529   -1.911  1.00 38.00  0  199 ASN   B OD1 1 
ATOM   3493 N  ND2 . ASN   B  1 184 ? -4.377  2.640   -1.971  1.00 41.74  0  199 ASN   B ND2 1 
ATOM   3494 N  N   . THR   B  1 185 ? -3.434  -1.276  0.718   1.00 33.71  0  200 THR   B N   1 
ATOM   3495 C  CA  . THR   B  1 185 ? -3.326  -2.755  0.633   1.00 34.82  0  200 THR   B CA  1 
ATOM   3496 C  C   . THR   B  1 185 ? -3.375  -3.229  -0.815  1.00 34.78  0  200 THR   B C   1 
ATOM   3497 O  O   . THR   B  1 185 ? -3.219  -4.445  -1.004  1.00 38.79  0  200 THR   B O   1 
ATOM   3498 C  CB  . THR   B  1 185 ? -4.385  -3.444  1.495   1.00 41.18  0  200 THR   B CB  1 
ATOM   3499 O  OG1 . THR   B  1 185 ? -5.685  -3.078  1.033   1.00 33.72  0  200 THR   B OG1 1 
ATOM   3500 C  CG2 . THR   B  1 185 ? -4.245  -3.076  2.958   1.00 48.10  0  200 THR   B CG2 1 
ATOM   3501 N  N   . ARG   B  1 186 ? -3.554  -2.327  -1.791  1.00 37.83  0  201 ARG   B N   1 
ATOM   3502 C  CA  . ARG   B  1 186 ? -3.488  -2.691  -3.231  1.00 39.68  0  201 ARG   B CA  1 
ATOM   3503 C  C   . ARG   B  1 186 ? -2.247  -2.078  -3.898  1.00 38.52  0  201 ARG   B C   1 
ATOM   3504 O  O   . ARG   B  1 186 ? -1.868  -2.594  -4.938  1.00 41.00  0  201 ARG   B O   1 
ATOM   3505 C  CB  . ARG   B  1 186 ? -4.770  -2.274  -3.955  1.00 43.18  0  201 ARG   B CB  1 
ATOM   3506 C  CG  . ARG   B  1 186 ? -6.044  -2.923  -3.417  1.00 48.28  0  201 ARG   B CG  1 
ATOM   3507 C  CD  . ARG   B  1 186 ? -7.296  -2.604  -4.220  1.00 53.20  0  201 ARG   B CD  1 
ATOM   3508 N  NE  . ARG   B  1 186 ? -8.534  -3.123  -3.696  0.00 52.35  0  201 ARG   B NE  1 
ATOM   3509 C  CZ  . ARG   B  1 186 ? -9.758  -2.894  -4.184  0.00 52.46  0  201 ARG   B CZ  1 
ATOM   3510 N  NH1 . ARG   B  1 186 ? -9.953  -2.121  -5.242  0.00 52.44  1  201 ARG   B NH1 1 
ATOM   3511 N  NH2 . ARG   B  1 186 ? -10.802 -3.450  -3.597  0.00 52.31  0  201 ARG   B NH2 1 
ATOM   3512 N  N   . ARG   B  1 187 ? -1.636  -1.020  -3.365  1.00 31.36  0  202 ARG   B N   1 
ATOM   3513 C  CA  . ARG   B  1 187 ? -0.587  -0.235  -4.075  1.00 34.26  0  202 ARG   B CA  1 
ATOM   3514 C  C   . ARG   B  1 187 ? 0.557   0.100   -3.115  1.00 35.15  0  202 ARG   B C   1 
ATOM   3515 O  O   . ARG   B  1 187 ? 0.319   0.796   -2.089  1.00 31.98  0  202 ARG   B O   1 
ATOM   3516 C  CB  . ARG   B  1 187 ? -1.209  1.037   -4.634  1.00 39.81  0  202 ARG   B CB  1 
ATOM   3517 C  CG  . ARG   B  1 187 ? -2.313  0.777   -5.653  1.00 48.37  0  202 ARG   B CG  1 
ATOM   3518 C  CD  . ARG   B  1 187 ? -3.218  1.971   -5.745  1.00 60.46  0  202 ARG   B CD  1 
ATOM   3519 N  NE  . ARG   B  1 187 ? -3.969  1.921   -6.988  1.00 73.01  0  202 ARG   B NE  1 
ATOM   3520 C  CZ  . ARG   B  1 187 ? -4.401  2.978   -7.674  1.00 80.28  0  202 ARG   B CZ  1 
ATOM   3521 N  NH1 . ARG   B  1 187 ? -4.146  4.214   -7.263  1.00 90.45  1  202 ARG   B NH1 1 
ATOM   3522 N  NH2 . ARG   B  1 187 ? -5.085  2.786   -8.790  1.00 76.33  0  202 ARG   B NH2 1 
ATOM   3523 N  N   . ASP   B  1 188 ? 1.765   -0.353  -3.427  1.00 28.78  0  203 ASP   B N   1 
ATOM   3524 C  CA  . ASP   B  1 188 ? 2.927   -0.154  -2.528  1.00 30.27  0  203 ASP   B CA  1 
ATOM   3525 C  C   . ASP   B  1 188 ? 4.208   -0.389  -3.320  1.00 27.56  0  203 ASP   B C   1 
ATOM   3526 O  O   . ASP   B  1 188 ? 4.165   -0.965  -4.429  1.00 30.74  0  203 ASP   B O   1 
ATOM   3527 C  CB  . ASP   B  1 188 ? 2.811   -1.013  -1.255  1.00 30.71  0  203 ASP   B CB  1 
ATOM   3528 C  CG  . ASP   B  1 188 ? 3.556   -0.535  -0.002  1.00 32.01  0  203 ASP   B CG  1 
ATOM   3529 O  OD1 . ASP   B  1 188 ? 4.336   0.442   -0.085  1.00 30.48  0  203 ASP   B OD1 1 
ATOM   3530 O  OD2 . ASP   B  1 188 ? 3.332   -1.153  1.089   1.00 29.06  -1 203 ASP   B OD2 1 
ATOM   3531 N  N   . SER   B  1 189 ? 5.310   0.056   -2.745  1.00 27.52  0  204 SER   B N   1 
ATOM   3532 C  CA  . SER   B  1 189 ? 6.684   -0.364  -3.098  1.00 27.33  0  204 SER   B CA  1 
ATOM   3533 C  C   . SER   B  1 189 ? 7.034   -1.601  -2.272  1.00 25.09  0  204 SER   B C   1 
ATOM   3534 O  O   . SER   B  1 189 ? 6.327   -1.885  -1.301  1.00 27.92  0  204 SER   B O   1 
ATOM   3535 C  CB  . SER   B  1 189 ? 7.613   0.773   -2.825  1.00 30.35  0  204 SER   B CB  1 
ATOM   3536 O  OG  . SER   B  1 189 ? 7.450   1.191   -1.458  1.00 31.18  0  204 SER   B OG  1 
ATOM   3537 N  N   . CYS   B  1 190 ? 8.096   -2.314  -2.608  1.00 26.57  0  205 CYS   B N   1 
ATOM   3538 C  CA  . CYS   B  1 190 ? 8.413   -3.619  -1.993  1.00 26.39  0  205 CYS   B CA  1 
ATOM   3539 C  C   . CYS   B  1 190 ? 9.917   -3.853  -2.075  1.00 27.62  0  205 CYS   B C   1 
ATOM   3540 O  O   . CYS   B  1 190 ? 10.636  -2.946  -2.578  1.00 25.52  0  205 CYS   B O   1 
ATOM   3541 C  CB  . CYS   B  1 190 ? 7.593   -4.739  -2.645  1.00 33.07  0  205 CYS   B CB  1 
ATOM   3542 S  SG  . CYS   B  1 190 ? 7.400   -6.208  -1.581  1.00 36.05  0  205 CYS   B SG  1 
ATOM   3543 N  N   . GLN   B  1 191 ? 10.389  -5.001  -1.589  1.00 27.72  0  206 GLN   B N   1 
ATOM   3544 C  CA  . GLN   B  1 191 ? 11.831  -5.335  -1.523  1.00 26.61  0  206 GLN   B CA  1 
ATOM   3545 C  C   . GLN   B  1 191 ? 12.398  -5.243  -2.940  1.00 26.63  0  206 GLN   B C   1 
ATOM   3546 O  O   . GLN   B  1 191 ? 11.812  -5.842  -3.844  1.00 28.76  0  206 GLN   B O   1 
ATOM   3547 C  CB  . GLN   B  1 191 ? 12.103  -6.724  -0.913  1.00 29.55  0  206 GLN   B CB  1 
ATOM   3548 C  CG  . GLN   B  1 191 ? 12.011  -6.758  0.612   1.00 34.90  0  206 GLN   B CG  1 
ATOM   3549 C  CD  . GLN   B  1 191 ? 10.646  -6.419  1.188   1.00 40.41  0  206 GLN   B CD  1 
ATOM   3550 O  OE1 . GLN   B  1 191 ? 10.482  -5.503  2.009   1.00 43.53  0  206 GLN   B OE1 1 
ATOM   3551 N  NE2 . GLN   B  1 191 ? 9.632   -7.169  0.781   1.00 36.68  0  206 GLN   B NE2 1 
ATOM   3552 N  N   . GLY   B  1 192 ? 13.500  -4.517  -3.105  1.00 25.92  0  207 GLY   B N   1 
ATOM   3553 C  CA  . GLY   B  1 192 ? 14.140  -4.219  -4.399  1.00 26.41  0  207 GLY   B CA  1 
ATOM   3554 C  C   . GLY   B  1 192 ? 13.737  -2.868  -4.977  1.00 25.17  0  207 GLY   B C   1 
ATOM   3555 O  O   . GLY   B  1 192 ? 14.431  -2.405  -5.917  1.00 24.78  0  207 GLY   B O   1 
ATOM   3556 N  N   . ASP   B  1 193 ? 12.685  -2.216  -4.466  1.00 25.43  0  208 ASP   B N   1 
ATOM   3557 C  CA  . ASP   B  1 193 ? 12.347  -0.819  -4.842  1.00 23.08  0  208 ASP   B CA  1 
ATOM   3558 C  C   . ASP   B  1 193 ? 13.096  0.205   -3.993  1.00 26.04  0  208 ASP   B C   1 
ATOM   3559 O  O   . ASP   B  1 193 ? 13.101  1.398   -4.375  1.00 25.81  0  208 ASP   B O   1 
ATOM   3560 C  CB  . ASP   B  1 193 ? 10.847  -0.586  -4.751  1.00 24.25  0  208 ASP   B CB  1 
ATOM   3561 C  CG  . ASP   B  1 193 ? 10.059  -1.394  -5.745  1.00 24.41  0  208 ASP   B CG  1 
ATOM   3562 O  OD1 . ASP   B  1 193 ? 10.507  -1.446  -6.924  1.00 25.08  0  208 ASP   B OD1 1 
ATOM   3563 O  OD2 . ASP   B  1 193 ? 8.969   -1.898  -5.338  1.00 25.56  -1 208 ASP   B OD2 1 
ATOM   3564 N  N   . SER   B  1 194 ? 13.685  -0.230  -2.884  1.00 25.90  0  209 SER   B N   1 
ATOM   3565 C  CA  . SER   B  1 194 ? 14.465  0.579   -1.938  1.00 28.20  0  209 SER   B CA  1 
ATOM   3566 C  C   . SER   B  1 194 ? 15.376  1.523   -2.700  1.00 27.37  0  209 SER   B C   1 
ATOM   3567 O  O   . SER   B  1 194 ? 16.076  1.054   -3.628  1.00 26.92  0  209 SER   B O   1 
ATOM   3568 C  CB  . SER   B  1 194 ? 15.284  -0.279  -0.996  1.00 27.29  0  209 SER   B CB  1 
ATOM   3569 O  OG  . SER   B  1 194 ? 14.421  -0.741  0.023   1.00 29.48  0  209 SER   B OG  1 
ATOM   3570 N  N   . GLY   B  1 195 ? 15.390  2.778   -2.256  1.00 26.86  0  210 GLY   B N   1 
ATOM   3571 C  CA  . GLY   B  1 195 ? 16.276  3.813   -2.802  1.00 29.41  0  210 GLY   B CA  1 
ATOM   3572 C  C   . GLY   B  1 195 ? 15.695  4.496   -4.026  1.00 27.13  0  210 GLY   B C   1 
ATOM   3573 O  O   . GLY   B  1 195 ? 16.215  5.553   -4.396  1.00 28.51  0  210 GLY   B O   1 
ATOM   3574 N  N   . GLY   B  1 196 ? 14.667  3.910   -4.633  1.00 27.11  0  211 GLY   B N   1 
ATOM   3575 C  CA  . GLY   B  1 196 ? 13.945  4.453   -5.780  1.00 31.37  0  211 GLY   B CA  1 
ATOM   3576 C  C   . GLY   B  1 196 ? 13.122  5.688   -5.427  1.00 30.31  0  211 GLY   B C   1 
ATOM   3577 O  O   . GLY   B  1 196 ? 12.911  6.001   -4.265  1.00 30.58  0  211 GLY   B O   1 
ATOM   3578 N  N   . PRO   B  1 197 ? 12.657  6.434   -6.444  1.00 31.49  0  212 PRO   B N   1 
ATOM   3579 C  CA  . PRO   B  1 197 ? 11.935  7.686   -6.221  1.00 29.08  0  212 PRO   B CA  1 
ATOM   3580 C  C   . PRO   B  1 197 ? 10.415  7.558   -6.071  1.00 30.47  0  212 PRO   B C   1 
ATOM   3581 O  O   . PRO   B  1 197 ? 9.809   6.740   -6.733  1.00 26.78  0  212 PRO   B O   1 
ATOM   3582 C  CB  . PRO   B  1 197 ? 12.298  8.481   -7.482  1.00 30.07  0  212 PRO   B CB  1 
ATOM   3583 C  CG  . PRO   B  1 197 ? 12.362  7.386   -8.566  1.00 32.14  0  212 PRO   B CG  1 
ATOM   3584 C  CD  . PRO   B  1 197 ? 12.863  6.133   -7.868  1.00 28.73  0  212 PRO   B CD  1 
ATOM   3585 N  N   . LEU   B  1 198 ? 9.861   8.382   -5.168  1.00 26.40  0  213 LEU   B N   1 
ATOM   3586 C  CA  . LEU   B  1 198 ? 8.432   8.727   -5.113  1.00 28.18  0  213 LEU   B CA  1 
ATOM   3587 C  C   . LEU   B  1 198 ? 8.326   10.148  -5.690  1.00 29.62  0  213 LEU   B C   1 
ATOM   3588 O  O   . LEU   B  1 198 ? 8.924   11.066  -5.106  1.00 27.48  0  213 LEU   B O   1 
ATOM   3589 C  CB  . LEU   B  1 198 ? 7.948   8.632   -3.661  1.00 29.49  0  213 LEU   B CB  1 
ATOM   3590 C  CG  . LEU   B  1 198 ? 6.482   8.997   -3.428  1.00 30.72  0  213 LEU   B CG  1 
ATOM   3591 C  CD1 . LEU   B  1 198 ? 5.542   7.966   -3.984  1.00 32.11  0  213 LEU   B CD1 1 
ATOM   3592 C  CD2 . LEU   B  1 198 ? 6.206   9.210   -1.959  1.00 31.62  0  213 LEU   B CD2 1 
ATOM   3593 N  N   . VAL   B  1 199 ? 7.653   10.305  -6.828  1.00 28.27  0  214 VAL   B N   1 
ATOM   3594 C  CA  . VAL   B  1 199 ? 7.603   11.572  -7.605  1.00 29.31  0  214 VAL   B CA  1 
ATOM   3595 C  C   . VAL   B  1 199 ? 6.148   12.053  -7.626  1.00 30.72  0  214 VAL   B C   1 
ATOM   3596 O  O   . VAL   B  1 199 ? 5.222   11.229  -7.680  1.00 32.63  0  214 VAL   B O   1 
ATOM   3597 C  CB  . VAL   B  1 199 ? 8.200   11.387  -9.015  1.00 31.00  0  214 VAL   B CB  1 
ATOM   3598 C  CG1 . VAL   B  1 199 ? 9.680   11.066  -8.949  1.00 29.36  0  214 VAL   B CG1 1 
ATOM   3599 C  CG2 . VAL   B  1 199 ? 7.485   10.311  -9.834  1.00 28.87  0  214 VAL   B CG2 1 
ATOM   3600 N  N   . CYS   B  1 200 ? 5.947   13.359  -7.535  1.00 31.79  0  215 CYS   B N   1 
ATOM   3601 C  CA  . CYS   B  1 200 ? 4.611   13.989  -7.577  1.00 33.07  0  215 CYS   B CA  1 
ATOM   3602 C  C   . CYS   B  1 200 ? 4.658   15.123  -8.626  1.00 34.41  0  215 CYS   B C   1 
ATOM   3603 O  O   . CYS   B  1 200 ? 5.687   15.834  -8.726  1.00 31.34  0  215 CYS   B O   1 
ATOM   3604 C  CB  . CYS   B  1 200 ? 4.226   14.503  -6.192  1.00 36.59  0  215 CYS   B CB  1 
ATOM   3605 S  SG  . CYS   B  1 200 ? 4.424   13.344  -4.793  1.00 35.66  0  215 CYS   B SG  1 
ATOM   3606 N  N   . LYS   B  1 201 ? 3.601   15.264  -9.413  1.00 35.56  0  216 LYS   B N   1 
ATOM   3607 C  CA  . LYS   B  1 201 ? 3.529   16.317  -10.465 1.00 41.63  0  216 LYS   B CA  1 
ATOM   3608 C  C   . LYS   B  1 201 ? 2.921   17.564  -9.810  1.00 37.90  0  216 LYS   B C   1 
ATOM   3609 O  O   . LYS   B  1 201 ? 1.768   17.486  -9.408  1.00 37.78  0  216 LYS   B O   1 
ATOM   3610 C  CB  . LYS   B  1 201 ? 2.743   15.854  -11.695 1.00 44.66  0  216 LYS   B CB  1 
ATOM   3611 C  CG  . LYS   B  1 201 ? 3.034   16.681  -12.947 1.00 49.84  0  216 LYS   B CG  1 
ATOM   3612 C  CD  . LYS   B  1 201 ? 2.510   16.097  -14.250 1.00 52.44  0  216 LYS   B CD  1 
ATOM   3613 C  CE  . LYS   B  1 201 ? 3.411   16.497  -15.402 1.00 53.01  0  216 LYS   B CE  1 
ATOM   3614 N  NZ  . LYS   B  1 201 ? 2.765   16.332  -16.726 1.00 52.45  1  216 LYS   B NZ  1 
ATOM   3615 N  N   . VAL   B  1 202 ? 3.706   18.629  -9.672  1.00 38.59  0  217 VAL   B N   1 
ATOM   3616 C  CA  . VAL   B  1 202 ? 3.318   19.904  -8.998  1.00 49.18  0  217 VAL   B CA  1 
ATOM   3617 C  C   . VAL   B  1 202 ? 3.515   21.045  -10.004 1.00 48.73  0  217 VAL   B C   1 
ATOM   3618 O  O   . VAL   B  1 202 ? 4.659   21.206  -10.457 1.00 48.55  0  217 VAL   B O   1 
ATOM   3619 C  CB  . VAL   B  1 202 ? 4.174   20.149  -7.729  1.00 50.62  0  217 VAL   B CB  1 
ATOM   3620 C  CG1 . VAL   B  1 202 ? 3.789   21.447  -7.021  1.00 49.05  0  217 VAL   B CG1 1 
ATOM   3621 C  CG2 . VAL   B  1 202 ? 4.107   18.979  -6.748  1.00 50.48  0  217 VAL   B CG2 1 
ATOM   3622 N  N   . ASN   B  1 203 ? 2.465   21.824  -10.304 1.00 60.74  0  218 ASN   B N   1 
ATOM   3623 C  CA  . ASN   B  1 203 ? 2.511   23.014  -11.215 1.00 59.18  0  218 ASN   B CA  1 
ATOM   3624 C  C   . ASN   B  1 203 ? 3.215   22.598  -12.518 1.00 61.34  0  218 ASN   B C   1 
ATOM   3625 O  O   . ASN   B  1 203 ? 4.217   23.284  -12.914 1.00 52.32  0  218 ASN   B O   1 
ATOM   3626 C  CB  . ASN   B  1 203 ? 3.138   24.257  -10.551 1.00 55.49  0  218 ASN   B CB  1 
ATOM   3627 C  CG  . ASN   B  1 203 ? 2.298   24.701  -9.357  0.00 59.29  0  218 ASN   B CG  1 
ATOM   3628 O  OD1 . ASN   B  1 203 ? 2.291   24.032  -8.328  0.00 59.08  0  218 ASN   B OD1 1 
ATOM   3629 N  ND2 . ASN   B  1 203 ? 1.608   25.823  -9.484  0.00 59.33  0  218 ASN   B ND2 1 
ATOM   3630 N  N   . GLY   B  1 204 ? 2.765   21.462  -13.095 1.00 61.63  0  219 GLY   B N   1 
ATOM   3631 C  CA  . GLY   B  1 204 ? 3.256   20.861  -14.354 1.00 55.54  0  219 GLY   B CA  1 
ATOM   3632 C  C   . GLY   B  1 204 ? 4.668   20.284  -14.287 1.00 59.28  0  219 GLY   B C   1 
ATOM   3633 O  O   . GLY   B  1 204 ? 5.150   19.883  -15.360 1.00 59.53  0  219 GLY   B O   1 
ATOM   3634 N  N   . THR   B  1 205 ? 5.326   20.208  -13.117 1.00 52.14  0  220 THR   B N   1 
ATOM   3635 C  CA  . THR   B  1 205 ? 6.721   19.690  -12.975 1.00 52.98  0  220 THR   B CA  1 
ATOM   3636 C  C   . THR   B  1 205 ? 6.736   18.441  -12.073 1.00 47.66  0  220 THR   B C   1 
ATOM   3637 O  O   . THR   B  1 205 ? 6.028   18.434  -11.039 1.00 38.88  0  220 THR   B O   1 
ATOM   3638 C  CB  . THR   B  1 205 ? 7.678   20.753  -12.429 1.00 55.51  0  220 THR   B CB  1 
ATOM   3639 O  OG1 . THR   B  1 205 ? 7.496   21.896  -13.261 1.00 67.76  0  220 THR   B OG1 1 
ATOM   3640 C  CG2 . THR   B  1 205 ? 9.128   20.311  -12.408 1.00 55.97  0  220 THR   B CG2 1 
ATOM   3641 N  N   . TRP   B  1 206 ? 7.507   17.414  -12.457 1.00 42.87  0  221 TRP   B N   1 
ATOM   3642 C  CA  . TRP   B  1 206 ? 7.745   16.216  -11.606 1.00 38.39  0  221 TRP   B CA  1 
ATOM   3643 C  C   . TRP   B  1 206 ? 8.751   16.603  -10.512 1.00 32.71  0  221 TRP   B C   1 
ATOM   3644 O  O   . TRP   B  1 206 ? 9.849   16.997  -10.873 1.00 36.68  0  221 TRP   B O   1 
ATOM   3645 C  CB  . TRP   B  1 206 ? 8.213   15.001  -12.431 1.00 36.39  0  221 TRP   B CB  1 
ATOM   3646 C  CG  . TRP   B  1 206 ? 7.098   14.368  -13.200 1.00 33.63  0  221 TRP   B CG  1 
ATOM   3647 C  CD1 . TRP   B  1 206 ? 6.882   14.500  -14.537 1.00 36.45  0  221 TRP   B CD1 1 
ATOM   3648 C  CD2 . TRP   B  1 206 ? 6.008   13.561  -12.697 1.00 33.25  0  221 TRP   B CD2 1 
ATOM   3649 N  NE1 . TRP   B  1 206 ? 5.751   13.821  -14.903 1.00 37.52  0  221 TRP   B NE1 1 
ATOM   3650 C  CE2 . TRP   B  1 206 ? 5.198   13.227  -13.807 1.00 35.84  0  221 TRP   B CE2 1 
ATOM   3651 C  CE3 . TRP   B  1 206 ? 5.642   13.067  -11.443 1.00 29.71  0  221 TRP   B CE3 1 
ATOM   3652 C  CZ2 . TRP   B  1 206 ? 4.051   12.437  -13.698 1.00 38.14  0  221 TRP   B CZ2 1 
ATOM   3653 C  CZ3 . TRP   B  1 206 ? 4.499   12.298  -11.329 1.00 33.15  0  221 TRP   B CZ3 1 
ATOM   3654 C  CH2 . TRP   B  1 206 ? 3.711   11.990  -12.438 1.00 33.52  0  221 TRP   B CH2 1 
ATOM   3655 N  N   . LEU   B  1 207 ? 8.351   16.509  -9.233  1.00 32.43  0  222 LEU   B N   1 
ATOM   3656 C  CA  . LEU   B  1 207 ? 9.211   16.727  -8.039  1.00 33.59  0  222 LEU   B CA  1 
ATOM   3657 C  C   . LEU   B  1 207 ? 9.403   15.401  -7.280  1.00 31.58  0  222 LEU   B C   1 
ATOM   3658 O  O   . LEU   B  1 207 ? 8.410   14.680  -7.041  1.00 31.71  0  222 LEU   B O   1 
ATOM   3659 C  CB  . LEU   B  1 207 ? 8.546   17.777  -7.137  1.00 36.54  0  222 LEU   B CB  1 
ATOM   3660 C  CG  . LEU   B  1 207 ? 8.314   19.168  -7.746  1.00 34.52  0  222 LEU   B CG  1 
ATOM   3661 C  CD1 . LEU   B  1 207 ? 7.755   20.127  -6.703  1.00 37.10  0  222 LEU   B CD1 1 
ATOM   3662 C  CD2 . LEU   B  1 207 ? 9.608   19.736  -8.326  1.00 35.04  0  222 LEU   B CD2 1 
ATOM   3663 N  N   . GLN   B  1 208 ? 10.630  15.097  -6.873  1.00 28.87  0  223 GLN   B N   1 
ATOM   3664 C  CA  . GLN   B  1 208 ? 10.873  13.919  -6.014  1.00 27.65  0  223 GLN   B CA  1 
ATOM   3665 C  C   . GLN   B  1 208 ? 10.512  14.246  -4.554  1.00 26.77  0  223 GLN   B C   1 
ATOM   3666 O  O   . GLN   B  1 208 ? 11.318  14.870  -3.860  1.00 28.19  0  223 GLN   B O   1 
ATOM   3667 C  CB  . GLN   B  1 208 ? 12.304  13.405  -6.137  1.00 26.46  0  223 GLN   B CB  1 
ATOM   3668 C  CG  . GLN   B  1 208 ? 12.413  12.020  -5.499  1.00 27.50  0  223 GLN   B CG  1 
ATOM   3669 C  CD  . GLN   B  1 208 ? 13.731  11.323  -5.699  1.00 29.25  0  223 GLN   B CD  1 
ATOM   3670 O  OE1 . GLN   B  1 208 ? 14.541  11.643  -6.592  1.00 27.10  0  223 GLN   B OE1 1 
ATOM   3671 N  NE2 . GLN   B  1 208 ? 13.936  10.319  -4.855  1.00 30.20  0  223 GLN   B NE2 1 
ATOM   3672 N  N   . ALA   B  1 209 ? 9.381   13.731  -4.074  1.00 30.09  0  224 ALA   B N   1 
ATOM   3673 C  CA  . ALA   B  1 209 ? 8.918   13.855  -2.663  1.00 31.46  0  224 ALA   B CA  1 
ATOM   3674 C  C   . ALA   B  1 209 ? 9.678   12.901  -1.722  1.00 30.82  0  224 ALA   B C   1 
ATOM   3675 O  O   . ALA   B  1 209 ? 9.930   13.284  -0.580  1.00 25.86  0  224 ALA   B O   1 
ATOM   3676 C  CB  . ALA   B  1 209 ? 7.432   13.598  -2.594  1.00 28.89  0  224 ALA   B CB  1 
ATOM   3677 N  N   . GLY   B  1 210 ? 9.994   11.678  -2.172  1.00 29.56  0  225 GLY   B N   1 
ATOM   3678 C  CA  . GLY   B  1 210 ? 10.417  10.578  -1.294  1.00 25.93  0  225 GLY   B CA  1 
ATOM   3679 C  C   . GLY   B  1 210 ? 11.485  9.674   -1.886  1.00 27.12  0  225 GLY   B C   1 
ATOM   3680 O  O   . GLY   B  1 210 ? 11.669  9.614   -3.131  1.00 29.39  0  225 GLY   B O   1 
ATOM   3681 N  N   . VAL   B  1 211 ? 12.183  8.991   -0.992  1.00 25.08  0  226 VAL   B N   1 
ATOM   3682 C  CA  . VAL   B  1 211 ? 13.071  7.854   -1.327  1.00 25.99  0  226 VAL   B CA  1 
ATOM   3683 C  C   . VAL   B  1 211 ? 12.487  6.614   -0.645  1.00 26.07  0  226 VAL   B C   1 
ATOM   3684 O  O   . VAL   B  1 211 ? 12.295  6.656   0.579   1.00 24.32  0  226 VAL   B O   1 
ATOM   3685 C  CB  . VAL   B  1 211 ? 14.511  8.144   -0.897  1.00 25.72  0  226 VAL   B CB  1 
ATOM   3686 C  CG1 . VAL   B  1 211 ? 15.413  6.957   -1.178  1.00 25.34  0  226 VAL   B CG1 1 
ATOM   3687 C  CG2 . VAL   B  1 211 ? 15.041  9.422   -1.545  1.00 25.80  0  226 VAL   B CG2 1 
ATOM   3688 N  N   . VAL   B  1 212 ? 12.268  5.535   -1.403  1.00 27.17  0  227 VAL   B N   1 
ATOM   3689 C  CA  . VAL   B  1 212 ? 11.731  4.245   -0.860  1.00 26.46  0  227 VAL   B CA  1 
ATOM   3690 C  C   . VAL   B  1 212 ? 12.641  3.807   0.311   1.00 24.01  0  227 VAL   B C   1 
ATOM   3691 O  O   . VAL   B  1 212 ? 13.857  3.665   0.079   1.00 25.94  0  227 VAL   B O   1 
ATOM   3692 C  CB  . VAL   B  1 212 ? 11.645  3.162   -1.947  1.00 22.95  0  227 VAL   B CB  1 
ATOM   3693 C  CG1 . VAL   B  1 212 ? 11.142  1.853   -1.349  1.00 24.91  0  227 VAL   B CG1 1 
ATOM   3694 C  CG2 . VAL   B  1 212 ? 10.740  3.584   -3.103  1.00 25.92  0  227 VAL   B CG2 1 
ATOM   3695 N  N   . SER   B  1 213 ? 12.105  3.702   1.524   1.00 23.29  0  228 SER   B N   1 
ATOM   3696 C  CA  . SER   B  1 213 ? 12.886  3.416   2.761   1.00 25.27  0  228 SER   B CA  1 
ATOM   3697 C  C   . SER   B  1 213 ? 12.490  2.054   3.366   1.00 24.90  0  228 SER   B C   1 
ATOM   3698 O  O   . SER   B  1 213 ? 13.288  1.117   3.310   1.00 27.04  0  228 SER   B O   1 
ATOM   3699 C  CB  . SER   B  1 213 ? 12.744  4.517   3.774   1.00 25.59  0  228 SER   B CB  1 
ATOM   3700 O  OG  . SER   B  1 213 ? 13.681  4.342   4.834   1.00 25.38  0  228 SER   B OG  1 
ATOM   3701 N  N   . TRP   B  1 214 ? 11.304  1.936   3.941   1.00 25.98  0  229 TRP   B N   1 
ATOM   3702 C  CA  . TRP   B  1 214 ? 10.944  0.743   4.751   1.00 23.65  0  229 TRP   B CA  1 
ATOM   3703 C  C   . TRP   B  1 214 ? 9.442   0.632   4.878   1.00 24.46  0  229 TRP   B C   1 
ATOM   3704 O  O   . TRP   B  1 214 ? 8.687   1.524   4.406   1.00 25.39  0  229 TRP   B O   1 
ATOM   3705 C  CB  . TRP   B  1 214 ? 11.639  0.739   6.121   1.00 23.82  0  229 TRP   B CB  1 
ATOM   3706 C  CG  . TRP   B  1 214 ? 11.202  1.801   7.082   1.00 24.96  0  229 TRP   B CG  1 
ATOM   3707 C  CD1 . TRP   B  1 214 ? 11.554  3.119   7.082   1.00 27.53  0  229 TRP   B CD1 1 
ATOM   3708 C  CD2 . TRP   B  1 214 ? 10.322  1.637   8.199   1.00 26.27  0  229 TRP   B CD2 1 
ATOM   3709 N  NE1 . TRP   B  1 214 ? 10.951  3.788   8.113   1.00 27.99  0  229 TRP   B NE1 1 
ATOM   3710 C  CE2 . TRP   B  1 214 ? 10.220  2.893   8.842   1.00 27.14  0  229 TRP   B CE2 1 
ATOM   3711 C  CE3 . TRP   B  1 214 ? 9.631   0.537   8.739   1.00 28.19  0  229 TRP   B CE3 1 
ATOM   3712 C  CZ2 . TRP   B  1 214 ? 9.471   3.075   10.004  1.00 29.67  0  229 TRP   B CZ2 1 
ATOM   3713 C  CZ3 . TRP   B  1 214 ? 8.900   0.721   9.886   1.00 29.23  0  229 TRP   B CZ3 1 
ATOM   3714 C  CH2 . TRP   B  1 214 ? 8.784   1.979   10.481  1.00 29.05  0  229 TRP   B CH2 1 
ATOM   3715 N  N   . GLY   B  1 215 ? 9.044   -0.487  5.452   1.00 25.88  0  230 GLY   B N   1 
ATOM   3716 C  CA  . GLY   B  1 215 ? 7.672   -0.747  5.882   1.00 26.91  0  230 GLY   B CA  1 
ATOM   3717 C  C   . GLY   B  1 215 ? 7.644   -2.090  6.548   1.00 26.61  0  230 GLY   B C   1 
ATOM   3718 O  O   . GLY   B  1 215 ? 8.678   -2.788  6.544   1.00 34.07  0  230 GLY   B O   1 
ATOM   3719 N  N   A GLU   B  1 216 ? 6.509   -2.447  7.128   0.50 28.44  0  231 GLU   B N   1 
ATOM   3720 N  N   B GLU   B  1 216 ? 6.515   -2.447  7.147   0.50 28.22  0  231 GLU   B N   1 
ATOM   3721 C  CA  A GLU   B  1 216 ? 6.224   -3.816  7.627   0.50 31.20  0  231 GLU   B CA  1 
ATOM   3722 C  CA  B GLU   B  1 216 ? 6.257   -3.837  7.605   0.50 30.71  0  231 GLU   B CA  1 
ATOM   3723 C  C   A GLU   B  1 216 ? 5.628   -4.605  6.444   0.50 30.35  0  231 GLU   B C   1 
ATOM   3724 C  C   B GLU   B  1 216 ? 5.635   -4.605  6.434   0.50 30.06  0  231 GLU   B C   1 
ATOM   3725 O  O   A GLU   B  1 216 ? 4.438   -4.424  6.174   0.50 31.52  0  231 GLU   B O   1 
ATOM   3726 O  O   B GLU   B  1 216 ? 4.444   -4.424  6.175   0.50 31.15  0  231 GLU   B O   1 
ATOM   3727 C  CB  A GLU   B  1 216 ? 5.317   -3.726  8.860   0.50 32.03  0  231 GLU   B CB  1 
ATOM   3728 C  CB  B GLU   B  1 216 ? 5.343   -3.909  8.820   0.50 31.30  0  231 GLU   B CB  1 
ATOM   3729 C  CG  A GLU   B  1 216 ? 6.050   -3.369  10.150  0.50 33.69  0  231 GLU   B CG  1 
ATOM   3730 C  CG  B GLU   B  1 216 ? 5.043   -5.353  9.183   0.50 32.21  0  231 GLU   B CG  1 
ATOM   3731 C  CD  A GLU   B  1 216 ? 5.189   -3.374  11.408  0.50 34.24  0  231 GLU   B CD  1 
ATOM   3732 C  CD  B GLU   B  1 216 ? 3.915   -5.478  10.177  0.50 30.43  0  231 GLU   B CD  1 
ATOM   3733 O  OE1 A GLU   B  1 216 ? 4.262   -4.207  11.463  0.50 34.62  0  231 GLU   B OE1 1 
ATOM   3734 O  OE1 B GLU   B  1 216 ? 3.869   -4.637  11.070  0.50 30.30  0  231 GLU   B OE1 1 
ATOM   3735 O  OE2 A GLU   B  1 216 ? 5.417   -2.528  12.321  0.50 32.89  -1 231 GLU   B OE2 1 
ATOM   3736 O  OE2 B GLU   B  1 216 ? 3.089   -6.389  10.039  0.50 31.09  -1 231 GLU   B OE2 1 
ATOM   3737 N  N   . GLY   B  1 217 ? 6.455   -5.372  5.722   1.00 32.60  0  232 GLY   B N   1 
ATOM   3738 C  CA  . GLY   B  1 217 ? 6.059   -6.041  4.474   1.00 31.23  0  232 GLY   B CA  1 
ATOM   3739 C  C   . GLY   B  1 217 ? 5.630   -5.008  3.449   1.00 34.12  0  232 GLY   B C   1 
ATOM   3740 O  O   . GLY   B  1 217 ? 6.087   -3.828  3.529   1.00 32.61  0  232 GLY   B O   1 
ATOM   3741 N  N   . CYS   B  1 218 ? 4.787   -5.431  2.515   1.00 31.64  0  233 CYS   B N   1 
ATOM   3742 C  CA  . CYS   B  1 218 ? 4.337   -4.626  1.352   1.00 36.15  0  233 CYS   B CA  1 
ATOM   3743 C  C   . CYS   B  1 218 ? 2.823   -4.775  1.268   1.00 34.72  0  233 CYS   B C   1 
ATOM   3744 O  O   . CYS   B  1 218 ? 2.351   -5.889  1.414   1.00 35.14  0  233 CYS   B O   1 
ATOM   3745 C  CB  . CYS   B  1 218 ? 5.031   -5.094  0.080   1.00 35.40  0  233 CYS   B CB  1 
ATOM   3746 S  SG  . CYS   B  1 218 ? 6.813   -5.398  0.317   1.00 40.44  0  233 CYS   B SG  1 
ATOM   3747 N  N   . ALA   B  1 219 ? 2.107   -3.665  1.174   1.00 34.10  0  234 ALA   B N   1 
ATOM   3748 C  CA  . ALA   B  1 219 ? 0.648   -3.614  0.938   1.00 34.03  0  234 ALA   B CA  1 
ATOM   3749 C  C   . ALA   B  1 219 ? -0.113  -4.344  2.051   1.00 33.82  0  234 ALA   B C   1 
ATOM   3750 O  O   . ALA   B  1 219 ? -1.173  -4.845  1.745   1.00 33.47  0  234 ALA   B O   1 
ATOM   3751 C  CB  . ALA   B  1 219 ? 0.345   -4.178  -0.438  1.00 33.53  0  234 ALA   B CB  1 
ATOM   3752 N  N   . GLN   B  1 220 ? 0.399   -4.357  3.293   1.00 32.99  0  235 GLN   B N   1 
ATOM   3753 C  CA  . GLN   B  1 220 ? -0.239  -4.990  4.481   1.00 33.72  0  235 GLN   B CA  1 
ATOM   3754 C  C   . GLN   B  1 220 ? -1.226  -4.007  5.119   1.00 32.54  0  235 GLN   B C   1 
ATOM   3755 O  O   . GLN   B  1 220 ? -0.996  -2.786  5.085   1.00 31.78  0  235 GLN   B O   1 
ATOM   3756 C  CB  . GLN   B  1 220 ? 0.801   -5.407  5.533   1.00 36.31  0  235 GLN   B CB  1 
ATOM   3757 C  CG  . GLN   B  1 220 ? 1.751   -6.523  5.125   1.00 39.67  0  235 GLN   B CG  1 
ATOM   3758 C  CD  . GLN   B  1 220 ? 1.010   -7.818  4.894   1.00 48.83  0  235 GLN   B CD  1 
ATOM   3759 O  OE1 . GLN   B  1 220 ? 0.900   -8.670  5.770   1.00 59.30  0  235 GLN   B OE1 1 
ATOM   3760 N  NE2 . GLN   B  1 220 ? 0.442   -7.958  3.709   1.00 52.24  0  235 GLN   B NE2 1 
ATOM   3761 N  N   . PRO   B  1 221 ? -2.350  -4.507  5.691   1.00 33.69  0  236 PRO   B N   1 
ATOM   3762 C  CA  . PRO   B  1 221 ? -3.308  -3.667  6.413   1.00 35.95  0  236 PRO   B CA  1 
ATOM   3763 C  C   . PRO   B  1 221 ? -2.638  -2.781  7.472   1.00 34.58  0  236 PRO   B C   1 
ATOM   3764 O  O   . PRO   B  1 221 ? -1.868  -3.311  8.255   1.00 30.96  0  236 PRO   B O   1 
ATOM   3765 C  CB  . PRO   B  1 221 ? -4.288  -4.662  7.071   1.00 35.11  0  236 PRO   B CB  1 
ATOM   3766 C  CG  . PRO   B  1 221 ? -4.175  -5.934  6.245   1.00 34.85  0  236 PRO   B CG  1 
ATOM   3767 C  CD  . PRO   B  1 221 ? -2.795  -5.918  5.619   1.00 35.45  0  236 PRO   B CD  1 
ATOM   3768 N  N   . ASN   B  1 222 ? -2.924  -1.472  7.439   1.00 33.44  0  237 ASN   B N   1 
ATOM   3769 C  CA  . ASN   B  1 222 ? -2.441  -0.463  8.422   1.00 33.29  0  237 ASN   B CA  1 
ATOM   3770 C  C   . ASN   B  1 222 ? -0.906  -0.378  8.427   1.00 30.09  0  237 ASN   B C   1 
ATOM   3771 O  O   . ASN   B  1 222 ? -0.354  0.018   9.456   1.00 26.79  0  237 ASN   B O   1 
ATOM   3772 C  CB  . ASN   B  1 222 ? -2.969  -0.771  9.833   1.00 33.50  0  237 ASN   B CB  1 
ATOM   3773 C  CG  . ASN   B  1 222 ? -4.480  -0.666  9.883   1.00 37.48  0  237 ASN   B CG  1 
ATOM   3774 O  OD1 . ASN   B  1 222 ? -5.019  0.251   9.304   1.00 33.62  0  237 ASN   B OD1 1 
ATOM   3775 N  ND2 . ASN   B  1 222 ? -5.159  -1.604  10.515  1.00 36.73  0  237 ASN   B ND2 1 
ATOM   3776 N  N   . ARG   B  1 223 ? -0.247  -0.667  7.314   1.00 26.80  0  238 ARG   B N   1 
ATOM   3777 C  CA  . ARG   B  1 223 ? 1.241   -0.599  7.248   1.00 30.23  0  238 ARG   B CA  1 
ATOM   3778 C  C   . ARG   B  1 223 ? 1.633   0.034   5.924   1.00 29.27  0  238 ARG   B C   1 
ATOM   3779 O  O   . ARG   B  1 223 ? 2.201   -0.613  5.051   1.00 31.23  0  238 ARG   B O   1 
ATOM   3780 C  CB  . ARG   B  1 223 ? 1.849   -1.982  7.473   1.00 30.48  0  238 ARG   B CB  1 
ATOM   3781 C  CG  . ARG   B  1 223 ? 1.483   -2.642  8.798   1.00 31.16  0  238 ARG   B CG  1 
ATOM   3782 C  CD  . ARG   B  1 223 ? 2.108   -1.958  9.989   1.00 32.75  0  238 ARG   B CD  1 
ATOM   3783 N  NE  . ARG   B  1 223 ? 1.809   -2.701  11.208  1.00 34.04  0  238 ARG   B NE  1 
ATOM   3784 C  CZ  . ARG   B  1 223 ? 0.770   -2.492  12.044  1.00 29.83  0  238 ARG   B CZ  1 
ATOM   3785 N  NH1 . ARG   B  1 223 ? -0.123  -1.531  11.832  1.00 28.81  1  238 ARG   B NH1 1 
ATOM   3786 N  NH2 . ARG   B  1 223 ? 0.627   -3.284  13.101  1.00 29.09  0  238 ARG   B NH2 1 
ATOM   3787 N  N   . PRO   B  1 224 ? 1.328   1.333   5.738   1.00 30.32  0  239 PRO   B N   1 
ATOM   3788 C  CA  . PRO   B  1 224 ? 1.690   2.011   4.508   1.00 30.34  0  239 PRO   B CA  1 
ATOM   3789 C  C   . PRO   B  1 224 ? 3.203   2.041   4.292   1.00 27.40  0  239 PRO   B C   1 
ATOM   3790 O  O   . PRO   B  1 224 ? 3.981   1.914   5.258   1.00 30.12  0  239 PRO   B O   1 
ATOM   3791 C  CB  . PRO   B  1 224 ? 1.191   3.458   4.652   1.00 30.78  0  239 PRO   B CB  1 
ATOM   3792 C  CG  . PRO   B  1 224 ? 0.341   3.486   5.903   1.00 33.51  0  239 PRO   B CG  1 
ATOM   3793 C  CD  . PRO   B  1 224 ? 0.611   2.215   6.676   1.00 30.27  0  239 PRO   B CD  1 
ATOM   3794 N  N   . GLY   B  1 225 ? 3.599   2.232   3.034   1.00 24.46  0  240 GLY   B N   1 
ATOM   3795 C  CA  . GLY   B  1 225 ? 5.014   2.425   2.678   1.00 28.01  0  240 GLY   B CA  1 
ATOM   3796 C  C   . GLY   B  1 225 ? 5.597   3.666   3.319   1.00 26.06  0  240 GLY   B C   1 
ATOM   3797 O  O   . GLY   B  1 225 ? 4.938   4.697   3.265   1.00 25.16  0  240 GLY   B O   1 
ATOM   3798 N  N   . ILE   B  1 226 ? 6.802   3.577   3.878   1.00 25.31  0  241 ILE   B N   1 
ATOM   3799 C  CA  . ILE   B  1 226 ? 7.519   4.734   4.478   1.00 25.78  0  241 ILE   B CA  1 
ATOM   3800 C  C   . ILE   B  1 226 ? 8.706   5.094   3.596   1.00 24.30  0  241 ILE   B C   1 
ATOM   3801 O  O   . ILE   B  1 226 ? 9.370   4.188   3.052   1.00 24.56  0  241 ILE   B O   1 
ATOM   3802 C  CB  . ILE   B  1 226 ? 8.000   4.435   5.908   1.00 29.36  0  241 ILE   B CB  1 
ATOM   3803 C  CG1 . ILE   B  1 226 ? 6.956   3.708   6.759   1.00 30.63  0  241 ILE   B CG1 1 
ATOM   3804 C  CG2 . ILE   B  1 226 ? 8.484   5.721   6.581   1.00 28.88  0  241 ILE   B CG2 1 
ATOM   3805 C  CD1 . ILE   B  1 226 ? 5.664   4.417   6.848   1.00 30.91  0  241 ILE   B CD1 1 
ATOM   3806 N  N   . TYR   B  1 227 ? 8.929   6.396   3.429   1.00 24.20  0  242 TYR   B N   1 
ATOM   3807 C  CA  . TYR   B  1 227 ? 9.908   7.011   2.499   1.00 26.12  0  242 TYR   B CA  1 
ATOM   3808 C  C   . TYR   B  1 227 ? 10.738  8.056   3.267   1.00 25.86  0  242 TYR   B C   1 
ATOM   3809 O  O   . TYR   B  1 227 ? 10.200  8.647   4.194   1.00 27.50  0  242 TYR   B O   1 
ATOM   3810 C  CB  . TYR   B  1 227 ? 9.120   7.660   1.353   1.00 26.64  0  242 TYR   B CB  1 
ATOM   3811 C  CG  . TYR   B  1 227 ? 8.297   6.716   0.525   1.00 25.81  0  242 TYR   B CG  1 
ATOM   3812 C  CD1 . TYR   B  1 227 ? 7.072   6.213   0.965   1.00 30.94  0  242 TYR   B CD1 1 
ATOM   3813 C  CD2 . TYR   B  1 227 ? 8.764   6.286   -0.695  1.00 26.42  0  242 TYR   B CD2 1 
ATOM   3814 C  CE1 . TYR   B  1 227 ? 6.331   5.345   0.165   1.00 28.85  0  242 TYR   B CE1 1 
ATOM   3815 C  CE2 . TYR   B  1 227 ? 8.029   5.447   -1.515  1.00 25.39  0  242 TYR   B CE2 1 
ATOM   3816 C  CZ  . TYR   B  1 227 ? 6.821   4.961   -1.081  1.00 27.32  0  242 TYR   B CZ  1 
ATOM   3817 O  OH  . TYR   B  1 227 ? 6.157   4.125   -1.930  1.00 29.07  0  242 TYR   B OH  1 
ATOM   3818 N  N   . THR   B  1 228 ? 12.006  8.257   2.925   1.00 26.23  0  243 THR   B N   1 
ATOM   3819 C  CA  . THR   B  1 228 ? 12.766  9.437   3.399   1.00 29.25  0  243 THR   B CA  1 
ATOM   3820 C  C   . THR   B  1 228 ? 12.125  10.676  2.762   1.00 30.86  0  243 THR   B C   1 
ATOM   3821 O  O   . THR   B  1 228 ? 11.872  10.643  1.542   1.00 29.09  0  243 THR   B O   1 
ATOM   3822 C  CB  . THR   B  1 228 ? 14.254  9.321   3.103   1.00 31.29  0  243 THR   B CB  1 
ATOM   3823 O  OG1 . THR   B  1 228 ? 14.639  8.038   3.576   1.00 27.91  0  243 THR   B OG1 1 
ATOM   3824 C  CG2 . THR   B  1 228 ? 15.064  10.418  3.765   1.00 31.29  0  243 THR   B CG2 1 
ATOM   3825 N  N   . ARG   B  1 229 ? 11.770  11.672  3.573   1.00 28.79  0  244 ARG   B N   1 
ATOM   3826 C  CA  . ARG   B  1 229 ? 11.170  12.967  3.132   1.00 31.31  0  244 ARG   B CA  1 
ATOM   3827 C  C   . ARG   B  1 229 ? 12.279  13.836  2.524   1.00 32.49  0  244 ARG   B C   1 
ATOM   3828 O  O   . ARG   B  1 229 ? 13.228  14.243  3.256   1.00 30.19  0  244 ARG   B O   1 
ATOM   3829 C  CB  . ARG   B  1 229 ? 10.480  13.663  4.312   1.00 31.95  0  244 ARG   B CB  1 
ATOM   3830 C  CG  . ARG   B  1 229 ? 9.752   14.945  3.932   1.00 37.32  0  244 ARG   B CG  1 
ATOM   3831 C  CD  . ARG   B  1 229 ? 9.119   15.605  5.150   1.00 38.79  0  244 ARG   B CD  1 
ATOM   3832 N  NE  . ARG   B  1 229 ? 7.954   14.877  5.603   1.00 39.18  0  244 ARG   B NE  1 
ATOM   3833 C  CZ  . ARG   B  1 229 ? 6.739   14.921  5.045   1.00 47.76  0  244 ARG   B CZ  1 
ATOM   3834 N  NH1 . ARG   B  1 229 ? 6.488   15.668  3.977   1.00 48.97  1  244 ARG   B NH1 1 
ATOM   3835 N  NH2 . ARG   B  1 229 ? 5.763   14.192  5.561   1.00 51.10  0  244 ARG   B NH2 1 
ATOM   3836 N  N   . VAL   B  1 230 ? 12.238  14.048  1.207   1.00 30.33  0  245 VAL   B N   1 
ATOM   3837 C  CA  . VAL   B  1 230 ? 13.406  14.667  0.512   1.00 31.54  0  245 VAL   B CA  1 
ATOM   3838 C  C   . VAL   B  1 230 ? 13.555  16.111  1.018   1.00 28.27  0  245 VAL   B C   1 
ATOM   3839 O  O   . VAL   B  1 230 ? 14.702  16.540  1.204   1.00 26.74  0  245 VAL   B O   1 
ATOM   3840 C  CB  . VAL   B  1 230 ? 13.282  14.567  -1.024  1.00 30.21  0  245 VAL   B CB  1 
ATOM   3841 C  CG1 . VAL   B  1 230 ? 14.301  15.455  -1.730  1.00 28.21  0  245 VAL   B CG1 1 
ATOM   3842 C  CG2 . VAL   B  1 230 ? 13.433  13.114  -1.481  1.00 31.09  0  245 VAL   B CG2 1 
ATOM   3843 N  N   . THR   B  1 231 ? 12.459  16.835  1.223   1.00 28.81  0  246 THR   B N   1 
ATOM   3844 C  CA  . THR   B  1 231 ? 12.524  18.267  1.633   1.00 33.61  0  246 THR   B CA  1 
ATOM   3845 C  C   . THR   B  1 231 ? 13.338  18.368  2.918   1.00 36.12  0  246 THR   B C   1 
ATOM   3846 O  O   . THR   B  1 231 ? 14.075  19.356  3.077   1.00 34.05  0  246 THR   B O   1 
ATOM   3847 C  CB  . THR   B  1 231 ? 11.145  18.903  1.858   1.00 34.42  0  246 THR   B CB  1 
ATOM   3848 O  OG1 . THR   B  1 231 ? 10.379  18.123  2.779   1.00 30.43  0  246 THR   B OG1 1 
ATOM   3849 C  CG2 . THR   B  1 231 ? 10.349  19.056  0.576   1.00 32.15  0  246 THR   B CG2 1 
ATOM   3850 N  N   . TYR   B  1 232 ? 13.242  17.356  3.795   1.00 37.29  0  247 TYR   B N   1 
ATOM   3851 C  CA  . TYR   B  1 232 ? 13.938  17.350  5.098   1.00 32.31  0  247 TYR   B CA  1 
ATOM   3852 C  C   . TYR   B  1 232 ? 15.443  17.405  4.902   1.00 29.32  0  247 TYR   B C   1 
ATOM   3853 O  O   . TYR   B  1 232 ? 16.096  18.015  5.746   1.00 29.84  0  247 TYR   B O   1 
ATOM   3854 C  CB  . TYR   B  1 232 ? 13.533  16.151  5.960   1.00 31.54  0  247 TYR   B CB  1 
ATOM   3855 C  CG  . TYR   B  1 232 ? 13.915  16.287  7.415   1.00 29.51  0  247 TYR   B CG  1 
ATOM   3856 C  CD1 . TYR   B  1 232 ? 15.211  15.988  7.835   1.00 29.44  0  247 TYR   B CD1 1 
ATOM   3857 C  CD2 . TYR   B  1 232 ? 12.985  16.679  8.365   1.00 30.31  0  247 TYR   B CD2 1 
ATOM   3858 C  CE1 . TYR   B  1 232 ? 15.591  16.116  9.157   1.00 31.15  0  247 TYR   B CE1 1 
ATOM   3859 C  CE2 . TYR   B  1 232 ? 13.340  16.769  9.707   1.00 32.48  0  247 TYR   B CE2 1 
ATOM   3860 C  CZ  . TYR   B  1 232 ? 14.646  16.493  10.096  1.00 32.56  0  247 TYR   B CZ  1 
ATOM   3861 O  OH  . TYR   B  1 232 ? 15.083  16.594  11.377  1.00 35.14  0  247 TYR   B OH  1 
ATOM   3862 N  N   . TYR   B  1 233 ? 15.984  16.806  3.844   1.00 31.87  0  248 TYR   B N   1 
ATOM   3863 C  CA  . TYR   B  1 233 ? 17.443  16.653  3.652   1.00 28.39  0  248 TYR   B CA  1 
ATOM   3864 C  C   . TYR   B  1 233 ? 17.966  17.526  2.497   1.00 26.98  0  248 TYR   B C   1 
ATOM   3865 O  O   . TYR   B  1 233 ? 19.149  17.295  2.091   1.00 28.20  0  248 TYR   B O   1 
ATOM   3866 C  CB  . TYR   B  1 233 ? 17.741  15.148  3.528   1.00 30.25  0  248 TYR   B CB  1 
ATOM   3867 C  CG  . TYR   B  1 233 ? 17.603  14.429  4.852   1.00 28.83  0  248 TYR   B CG  1 
ATOM   3868 C  CD1 . TYR   B  1 233 ? 18.490  14.682  5.903   1.00 28.08  0  248 TYR   B CD1 1 
ATOM   3869 C  CD2 . TYR   B  1 233 ? 16.517  13.604  5.096   1.00 26.08  0  248 TYR   B CD2 1 
ATOM   3870 C  CE1 . TYR   B  1 233 ? 18.319  14.107  7.145   1.00 27.56  0  248 TYR   B CE1 1 
ATOM   3871 C  CE2 . TYR   B  1 233 ? 16.370  12.965  6.317   1.00 29.17  0  248 TYR   B CE2 1 
ATOM   3872 C  CZ  . TYR   B  1 233 ? 17.268  13.225  7.346   1.00 26.29  0  248 TYR   B CZ  1 
ATOM   3873 O  OH  . TYR   B  1 233 ? 17.096  12.639  8.557   1.00 26.49  0  248 TYR   B OH  1 
ATOM   3874 N  N   . LEU   B  1 234 ? 17.226  18.544  2.033   1.00 31.52  0  249 LEU   B N   1 
ATOM   3875 C  CA  . LEU   B  1 234 ? 17.690  19.427  0.903   1.00 31.65  0  249 LEU   B CA  1 
ATOM   3876 C  C   . LEU   B  1 234 ? 19.029  20.065  1.224   1.00 33.31  0  249 LEU   B C   1 
ATOM   3877 O  O   . LEU   B  1 234 ? 19.909  20.010  0.357   1.00 39.64  0  249 LEU   B O   1 
ATOM   3878 C  CB  . LEU   B  1 234 ? 16.665  20.509  0.577   1.00 35.49  0  249 LEU   B CB  1 
ATOM   3879 C  CG  . LEU   B  1 234 ? 15.497  20.032  -0.269  1.00 41.13  0  249 LEU   B CG  1 
ATOM   3880 C  CD1 . LEU   B  1 234 ? 14.379  21.049  -0.220  1.00 42.89  0  249 LEU   B CD1 1 
ATOM   3881 C  CD2 . LEU   B  1 234 ? 15.919  19.738  -1.714  1.00 42.01  0  249 LEU   B CD2 1 
ATOM   3882 N  N   . ASP   B  1 235 ? 19.218  20.594  2.432   1.00 38.40  0  250 ASP   B N   1 
ATOM   3883 C  CA  . ASP   B  1 235 ? 20.479  21.293  2.779   1.00 40.02  0  250 ASP   B CA  1 
ATOM   3884 C  C   . ASP   B  1 235 ? 21.650  20.315  2.711   1.00 40.36  0  250 ASP   B C   1 
ATOM   3885 O  O   . ASP   B  1 235 ? 22.712  20.715  2.238   1.00 36.55  0  250 ASP   B O   1 
ATOM   3886 C  CB  . ASP   B  1 235 ? 20.404  21.944  4.151   1.00 42.49  0  250 ASP   B CB  1 
ATOM   3887 C  CG  . ASP   B  1 235 ? 19.420  23.097  4.206   1.00 46.42  0  250 ASP   B CG  1 
ATOM   3888 O  OD1 . ASP   B  1 235 ? 18.953  23.544  3.130   1.00 51.32  0  250 ASP   B OD1 1 
ATOM   3889 O  OD2 . ASP   B  1 235 ? 19.101  23.527  5.340   1.00 60.43  -1 250 ASP   B OD2 1 
ATOM   3890 N  N   . TRP   B  1 236 ? 21.468  19.084  3.195   1.00 37.43  0  251 TRP   B N   1 
ATOM   3891 C  CA  . TRP   B  1 236 ? 22.513  18.019  3.105   1.00 32.76  0  251 TRP   B CA  1 
ATOM   3892 C  C   . TRP   B  1 236 ? 22.770  17.666  1.631   1.00 27.77  0  251 TRP   B C   1 
ATOM   3893 O  O   . TRP   B  1 236 ? 23.916  17.619  1.219   1.00 29.53  0  251 TRP   B O   1 
ATOM   3894 C  CB  . TRP   B  1 236 ? 22.114  16.792  3.958   1.00 29.80  0  251 TRP   B CB  1 
ATOM   3895 C  CG  . TRP   B  1 236 ? 23.132  15.705  3.894   1.00 27.59  0  251 TRP   B CG  1 
ATOM   3896 C  CD1 . TRP   B  1 236 ? 24.281  15.623  4.599   1.00 27.72  0  251 TRP   B CD1 1 
ATOM   3897 C  CD2 . TRP   B  1 236 ? 23.129  14.578  3.001   1.00 28.69  0  251 TRP   B CD2 1 
ATOM   3898 N  NE1 . TRP   B  1 236 ? 24.993  14.518  4.214   1.00 29.83  0  251 TRP   B NE1 1 
ATOM   3899 C  CE2 . TRP   B  1 236 ? 24.305  13.847  3.249   1.00 27.98  0  251 TRP   B CE2 1 
ATOM   3900 C  CE3 . TRP   B  1 236 ? 22.243  14.118  2.024   1.00 28.59  0  251 TRP   B CE3 1 
ATOM   3901 C  CZ2 . TRP   B  1 236 ? 24.619  12.666  2.571   1.00 31.81  0  251 TRP   B CZ2 1 
ATOM   3902 C  CZ3 . TRP   B  1 236 ? 22.550  12.954  1.351   1.00 31.97  0  251 TRP   B CZ3 1 
ATOM   3903 C  CH2 . TRP   B  1 236 ? 23.719  12.230  1.631   1.00 30.04  0  251 TRP   B CH2 1 
ATOM   3904 N  N   . ILE   B  1 237 ? 21.731  17.419  0.848   1.00 30.74  0  252 ILE   B N   1 
ATOM   3905 C  CA  . ILE   B  1 237 ? 21.900  17.083  -0.603  1.00 34.13  0  252 ILE   B CA  1 
ATOM   3906 C  C   . ILE   B  1 237 ? 22.680  18.230  -1.279  1.00 34.58  0  252 ILE   B C   1 
ATOM   3907 O  O   . ILE   B  1 237 ? 23.733  17.962  -1.910  1.00 33.70  0  252 ILE   B O   1 
ATOM   3908 C  CB  . ILE   B  1 237 ? 20.551  16.807  -1.296  1.00 31.17  0  252 ILE   B CB  1 
ATOM   3909 C  CG1 . ILE   B  1 237 ? 19.869  15.553  -0.749  1.00 28.80  0  252 ILE   B CG1 1 
ATOM   3910 C  CG2 . ILE   B  1 237 ? 20.721  16.733  -2.813  1.00 30.72  0  252 ILE   B CG2 1 
ATOM   3911 C  CD1 . ILE   B  1 237 ? 18.397  15.488  -1.104  1.00 28.06  0  252 ILE   B CD1 1 
ATOM   3912 N  N   . HIS   B  1 238 ? 22.233  19.475  -1.096  1.00 39.74  0  253 HIS   B N   1 
ATOM   3913 C  CA  . HIS   B  1 238 ? 22.800  20.693  -1.765  1.00 41.52  0  253 HIS   B CA  1 
ATOM   3914 C  C   . HIS   B  1 238 ? 24.203  21.010  -1.263  1.00 40.30  0  253 HIS   B C   1 
ATOM   3915 O  O   . HIS   B  1 238 ? 24.919  21.736  -1.955  1.00 46.67  0  253 HIS   B O   1 
ATOM   3916 C  CB  . HIS   B  1 238 ? 21.851  21.885  -1.648  1.00 38.80  0  253 HIS   B CB  1 
ATOM   3917 C  CG  . HIS   B  1 238 ? 20.653  21.734  -2.513  1.00 39.42  0  253 HIS   B CG  1 
ATOM   3918 N  ND1 . HIS   B  1 238 ? 20.737  21.189  -3.797  1.00 42.04  0  253 HIS   B ND1 1 
ATOM   3919 C  CD2 . HIS   B  1 238 ? 19.363  22.097  -2.329  1.00 41.81  0  253 HIS   B CD2 1 
ATOM   3920 C  CE1 . HIS   B  1 238 ? 19.544  21.221  -4.361  1.00 41.90  0  253 HIS   B CE1 1 
ATOM   3921 N  NE2 . HIS   B  1 238 ? 18.671  21.756  -3.470  1.00 42.30  0  253 HIS   B NE2 1 
ATOM   3922 N  N   . HIS   B  1 239 ? 24.642  20.432  -0.150  1.00 41.26  0  254 HIS   B N   1 
ATOM   3923 C  CA  . HIS   B  1 239 ? 26.064  20.505  0.279   1.00 39.43  0  254 HIS   B CA  1 
ATOM   3924 C  C   . HIS   B  1 239 ? 26.994  19.843  -0.739  1.00 42.57  0  254 HIS   B C   1 
ATOM   3925 O  O   . HIS   B  1 239 ? 28.207  20.190  -0.758  1.00 41.28  0  254 HIS   B O   1 
ATOM   3926 C  CB  . HIS   B  1 239 ? 26.219  19.869  1.667   1.00 45.76  0  254 HIS   B CB  1 
ATOM   3927 C  CG  . HIS   B  1 239 ? 27.570  20.025  2.262   1.00 46.29  0  254 HIS   B CG  1 
ATOM   3928 N  ND1 . HIS   B  1 239 ? 27.864  21.058  3.123   1.00 47.12  0  254 HIS   B ND1 1 
ATOM   3929 C  CD2 . HIS   B  1 239 ? 28.697  19.300  2.118   1.00 49.98  0  254 HIS   B CD2 1 
ATOM   3930 C  CE1 . HIS   B  1 239 ? 29.115  20.964  3.498   1.00 48.00  0  254 HIS   B CE1 1 
ATOM   3931 N  NE2 . HIS   B  1 239 ? 29.662  19.896  2.882   1.00 50.91  0  254 HIS   B NE2 1 
ATOM   3932 N  N   . TYR   B  1 240 ? 26.500  18.844  -1.486  1.00 42.68  0  255 TYR   B N   1 
ATOM   3933 C  CA  . TYR   B  1 240 ? 27.310  18.038  -2.436  1.00 39.46  0  255 TYR   B CA  1 
ATOM   3934 C  C   . TYR   B  1 240 ? 26.869  18.270  -3.885  1.00 35.95  0  255 TYR   B C   1 
ATOM   3935 O  O   . TYR   B  1 240 ? 27.730  18.186  -4.747  1.00 41.49  0  255 TYR   B O   1 
ATOM   3936 C  CB  . TYR   B  1 240 ? 27.206  16.550  -2.086  1.00 42.50  0  255 TYR   B CB  1 
ATOM   3937 C  CG  . TYR   B  1 240 ? 27.683  16.223  -0.696  1.00 38.60  0  255 TYR   B CG  1 
ATOM   3938 C  CD1 . TYR   B  1 240 ? 29.034  16.166  -0.414  1.00 37.06  0  255 TYR   B CD1 1 
ATOM   3939 C  CD2 . TYR   B  1 240 ? 26.782  16.038  0.341   1.00 37.32  0  255 TYR   B CD2 1 
ATOM   3940 C  CE1 . TYR   B  1 240 ? 29.483  15.927  0.868   1.00 37.51  0  255 TYR   B CE1 1 
ATOM   3941 C  CE2 . TYR   B  1 240 ? 27.214  15.777  1.631   1.00 37.87  0  255 TYR   B CE2 1 
ATOM   3942 C  CZ  . TYR   B  1 240 ? 28.572  15.718  1.889   1.00 36.13  0  255 TYR   B CZ  1 
ATOM   3943 O  OH  . TYR   B  1 240 ? 29.025  15.488  3.148   1.00 36.64  0  255 TYR   B OH  1 
ATOM   3944 N  N   . VAL   B  1 241 ? 25.594  18.544  -4.144  1.00 37.45  0  256 VAL   B N   1 
ATOM   3945 C  CA  . VAL   B  1 241 ? 24.995  18.532  -5.506  1.00 40.99  0  256 VAL   B CA  1 
ATOM   3946 C  C   . VAL   B  1 241 ? 24.687  19.969  -5.900  1.00 45.47  0  256 VAL   B C   1 
ATOM   3947 O  O   . VAL   B  1 241 ? 23.814  20.587  -5.285  1.00 41.99  0  256 VAL   B O   1 
ATOM   3948 C  CB  . VAL   B  1 241 ? 23.744  17.637  -5.569  1.00 40.91  0  256 VAL   B CB  1 
ATOM   3949 C  CG1 . VAL   B  1 241 ? 23.084  17.633  -6.948  1.00 39.73  0  256 VAL   B CG1 1 
ATOM   3950 C  CG2 . VAL   B  1 241 ? 24.096  16.213  -5.158  1.00 40.80  0  256 VAL   B CG2 1 
ATOM   3951 N  N   . PRO   B  1 242 ? 25.370  20.519  -6.939  1.00 51.36  0  257 PRO   B N   1 
ATOM   3952 C  CA  . PRO   B  1 242 ? 25.041  21.842  -7.487  1.00 52.98  0  257 PRO   B CA  1 
ATOM   3953 C  C   . PRO   B  1 242 ? 23.552  22.073  -7.789  1.00 57.56  0  257 PRO   B C   1 
ATOM   3954 O  O   . PRO   B  1 242 ? 22.918  21.137  -8.237  1.00 59.11  0  257 PRO   B O   1 
ATOM   3955 C  CB  . PRO   B  1 242 ? 25.839  21.852  -8.795  1.00 49.73  0  257 PRO   B CB  1 
ATOM   3956 C  CG  . PRO   B  1 242 ? 27.071  21.052  -8.448  1.00 51.76  0  257 PRO   B CG  1 
ATOM   3957 C  CD  . PRO   B  1 242 ? 26.513  19.902  -7.637  1.00 53.26  0  257 PRO   B CD  1 
ATOM   3958 N  N   . LYS   B  1 243 ? 23.069  23.311  -7.605  1.00 67.93  0  258 LYS   B N   1 
ATOM   3959 C  CA  . LYS   B  1 243 ? 21.635  23.715  -7.655  1.00 73.43  0  258 LYS   B CA  1 
ATOM   3960 C  C   . LYS   B  1 243 ? 21.291  24.225  -9.064  1.00 73.25  0  258 LYS   B C   1 
ATOM   3961 O  O   . LYS   B  1 243 ? 21.253  23.496  -10.067 1.00 72.47  0  258 LYS   B O   1 
ATOM   3962 C  CB  . LYS   B  1 243 ? 21.379  24.793  -6.595  1.00 76.47  0  258 LYS   B CB  1 
ATOM   3963 C  CG  . LYS   B  1 243 ? 20.026  24.738  -5.885  1.00 83.84  0  258 LYS   B CG  1 
ATOM   3964 C  CD  . LYS   B  1 243 ? 19.903  25.663  -4.650  1.00 83.47  0  258 LYS   B CD  1 
ATOM   3965 C  CE  . LYS   B  1 243 ? 20.944  25.418  -3.563  1.00 81.55  0  258 LYS   B CE  1 
ATOM   3966 N  NZ  . LYS   B  1 243 ? 20.655  26.142  -2.298  1.00 77.77  1  258 LYS   B NZ  1 
ATOM   3967 N  N   . ILE   C  1 1   ? 7.410   -41.868 7.133   1.00 26.33  0  16  ILE   C N   1 
ATOM   3968 C  CA  . ILE   C  1 1   ? 6.159   -42.717 7.140   1.00 24.95  0  16  ILE   C CA  1 
ATOM   3969 C  C   . ILE   C  1 1   ? 4.917   -41.802 7.031   1.00 28.62  0  16  ILE   C C   1 
ATOM   3970 O  O   . ILE   C  1 1   ? 4.777   -40.852 7.847   1.00 29.94  0  16  ILE   C O   1 
ATOM   3971 C  CB  . ILE   C  1 1   ? 6.116   -43.617 8.398   1.00 26.11  0  16  ILE   C CB  1 
ATOM   3972 C  CG1 . ILE   C  1 1   ? 7.269   -44.625 8.402   1.00 25.87  0  16  ILE   C CG1 1 
ATOM   3973 C  CG2 . ILE   C  1 1   ? 4.748   -44.288 8.587   1.00 29.69  0  16  ILE   C CG2 1 
ATOM   3974 C  CD1 . ILE   C  1 1   ? 7.103   -45.810 7.462   1.00 24.67  0  16  ILE   C CD1 1 
ATOM   3975 N  N   . VAL   C  1 2   ? 4.031   -42.076 6.058   1.00 25.95  0  17  VAL   C N   1 
ATOM   3976 C  CA  . VAL   C  1 2   ? 2.782   -41.306 5.840   1.00 30.51  0  17  VAL   C CA  1 
ATOM   3977 C  C   . VAL   C  1 2   ? 1.634   -42.066 6.489   1.00 30.34  0  17  VAL   C C   1 
ATOM   3978 O  O   . VAL   C  1 2   ? 1.456   -43.248 6.176   1.00 28.26  0  17  VAL   C O   1 
ATOM   3979 C  CB  . VAL   C  1 2   ? 2.503   -41.017 4.353   1.00 28.02  0  17  VAL   C CB  1 
ATOM   3980 C  CG1 . VAL   C  1 2   ? 1.260   -40.191 4.161   1.00 29.27  0  17  VAL   C CG1 1 
ATOM   3981 C  CG2 . VAL   C  1 2   ? 3.676   -40.301 3.735   1.00 33.12  0  17  VAL   C CG2 1 
ATOM   3982 N  N   . GLY   C  1 3   ? 0.819   -41.341 7.259   1.00 33.85  0  18  GLY   C N   1 
ATOM   3983 C  CA  . GLY   C  1 3   ? -0.402  -41.867 7.903   1.00 32.93  0  18  GLY   C CA  1 
ATOM   3984 C  C   . GLY   C  1 3   ? -0.086  -42.819 9.028   1.00 34.35  0  18  GLY   C C   1 
ATOM   3985 O  O   . GLY   C  1 3   ? -0.962  -43.640 9.386   1.00 37.62  0  18  GLY   C O   1 
ATOM   3986 N  N   . GLY   C  1 4   ? 1.114   -42.743 9.571   1.00 28.85  0  19  GLY   C N   1 
ATOM   3987 C  CA  . GLY   C  1 4   ? 1.519   -43.692 10.604  1.00 38.09  0  19  GLY   C CA  1 
ATOM   3988 C  C   . GLY   C  1 4   ? 1.191   -43.186 12.001  1.00 42.17  0  19  GLY   C C   1 
ATOM   3989 O  O   . GLY   C  1 4   ? 0.465   -42.191 12.147  1.00 44.73  0  19  GLY   C O   1 
ATOM   3990 N  N   . GLN   C  1 5   ? 1.744   -43.873 12.997  1.00 38.19  0  20  GLN   C N   1 
ATOM   3991 C  CA  . GLN   C  1 5   ? 1.835   -43.414 14.399  1.00 37.62  0  20  GLN   C CA  1 
ATOM   3992 C  C   . GLN   C  1 5   ? 3.215   -43.772 14.935  1.00 34.18  0  20  GLN   C C   1 
ATOM   3993 O  O   . GLN   C  1 5   ? 3.909   -44.639 14.339  1.00 29.19  0  20  GLN   C O   1 
ATOM   3994 C  CB  . GLN   C  1 5   ? 0.790   -44.125 15.253  1.00 41.25  0  20  GLN   C CB  1 
ATOM   3995 C  CG  . GLN   C  1 5   ? -0.560  -44.188 14.582  1.00 50.91  0  20  GLN   C CG  1 
ATOM   3996 C  CD  . GLN   C  1 5   ? -1.491  -45.090 15.338  1.00 54.16  0  20  GLN   C CD  1 
ATOM   3997 O  OE1 . GLN   C  1 5   ? -1.137  -46.226 15.666  1.00 65.38  0  20  GLN   C OE1 1 
ATOM   3998 N  NE2 . GLN   C  1 5   ? -2.693  -44.588 15.581  1.00 46.38  0  20  GLN   C NE2 1 
ATOM   3999 N  N   . GLU   C  1 6   ? 3.559   -43.178 16.063  1.00 31.64  0  21  GLU   C N   1 
ATOM   4000 C  CA  . GLU   C  1 6   ? 4.793   -43.490 16.816  1.00 33.00  0  21  GLU   C CA  1 
ATOM   4001 C  C   . GLU   C  1 6   ? 4.719   -44.956 17.230  1.00 30.91  0  21  GLU   C C   1 
ATOM   4002 O  O   . GLU   C  1 6   ? 3.627   -45.399 17.639  1.00 29.50  0  21  GLU   C O   1 
ATOM   4003 C  CB  . GLU   C  1 6   ? 4.923   -42.581 18.037  1.00 34.57  0  21  GLU   C CB  1 
ATOM   4004 C  CG  . GLU   C  1 6   ? 6.131   -42.931 18.892  1.00 39.40  0  21  GLU   C CG  1 
ATOM   4005 C  CD  . GLU   C  1 6   ? 6.589   -41.874 19.898  1.00 38.49  0  21  GLU   C CD  1 
ATOM   4006 O  OE1 . GLU   C  1 6   ? 7.605   -42.139 20.603  1.00 33.04  0  21  GLU   C OE1 1 
ATOM   4007 O  OE2 . GLU   C  1 6   ? 5.949   -40.780 19.957  1.00 33.47  -1 21  GLU   C OE2 1 
ATOM   4008 N  N   . ALA   C  1 7   ? 5.824   -45.669 17.114  1.00 29.03  0  22  ALA   C N   1 
ATOM   4009 C  CA  . ALA   C  1 7   ? 5.930   -47.102 17.435  1.00 33.63  0  22  ALA   C CA  1 
ATOM   4010 C  C   . ALA   C  1 7   ? 6.014   -47.253 18.945  1.00 38.33  0  22  ALA   C C   1 
ATOM   4011 O  O   . ALA   C  1 7   ? 6.734   -46.485 19.574  1.00 35.74  0  22  ALA   C O   1 
ATOM   4012 C  CB  . ALA   C  1 7   ? 7.201   -47.657 16.832  1.00 35.07  0  22  ALA   C CB  1 
ATOM   4013 N  N   . PRO   C  1 8   ? 5.348   -48.267 19.553  1.00 36.77  0  23  PRO   C N   1 
ATOM   4014 C  CA  . PRO   C  1 8   ? 5.686   -48.704 20.901  1.00 37.23  0  23  PRO   C CA  1 
ATOM   4015 C  C   . PRO   C  1 8   ? 7.174   -49.073 20.960  1.00 37.48  0  23  PRO   C C   1 
ATOM   4016 O  O   . PRO   C  1 8   ? 7.690   -49.621 19.972  1.00 39.27  0  23  PRO   C O   1 
ATOM   4017 C  CB  . PRO   C  1 8   ? 4.816   -49.951 21.157  1.00 36.22  0  23  PRO   C CB  1 
ATOM   4018 C  CG  . PRO   C  1 8   ? 3.696   -49.854 20.147  1.00 37.75  0  23  PRO   C CG  1 
ATOM   4019 C  CD  . PRO   C  1 8   ? 4.252   -49.055 18.975  1.00 39.29  0  23  PRO   C CD  1 
ATOM   4020 N  N   . ARG   C  1 9   ? 7.807   -48.824 22.107  1.00 34.46  0  24  ARG   C N   1 
ATOM   4021 C  CA  . ARG   C  1 9   ? 9.247   -49.139 22.373  1.00 35.18  0  24  ARG   C CA  1 
ATOM   4022 C  C   . ARG   C  1 9   ? 9.554   -50.629 22.178  1.00 33.21  0  24  ARG   C C   1 
ATOM   4023 O  O   . ARG   C  1 9   ? 10.708  -50.953 21.836  1.00 32.18  0  24  ARG   C O   1 
ATOM   4024 C  CB  . ARG   C  1 9   ? 9.627   -48.731 23.796  1.00 40.77  0  24  ARG   C CB  1 
ATOM   4025 C  CG  . ARG   C  1 9   ? 9.444   -47.247 24.077  1.00 45.27  0  24  ARG   C CG  1 
ATOM   4026 C  CD  . ARG   C  1 9   ? 9.894   -46.810 25.466  1.00 52.19  0  24  ARG   C CD  1 
ATOM   4027 N  NE  . ARG   C  1 9   ? 10.238  -45.398 25.383  1.00 53.17  0  24  ARG   C NE  1 
ATOM   4028 C  CZ  . ARG   C  1 9   ? 11.443  -44.899 25.074  1.00 52.58  0  24  ARG   C CZ  1 
ATOM   4029 N  NH1 . ARG   C  1 9   ? 12.474  -45.699 24.826  1.00 50.62  1  24  ARG   C NH1 1 
ATOM   4030 N  NH2 . ARG   C  1 9   ? 11.604  -43.582 25.006  1.00 51.56  0  24  ARG   C NH2 1 
ATOM   4031 N  N   . SER   C  1 10  ? 8.589   -51.511 22.423  1.00 36.67  0  25  SER   C N   1 
ATOM   4032 C  CA  . SER   C  1 10  ? 8.747   -52.994 22.349  1.00 41.61  0  25  SER   C CA  1 
ATOM   4033 C  C   . SER   C  1 10  ? 8.647   -53.514 20.901  1.00 40.92  0  25  SER   C C   1 
ATOM   4034 O  O   . SER   C  1 10  ? 8.881   -54.700 20.727  1.00 47.05  0  25  SER   C O   1 
ATOM   4035 C  CB  . SER   C  1 10  ? 7.710   -53.676 23.218  1.00 38.96  0  25  SER   C CB  1 
ATOM   4036 O  OG  . SER   C  1 10  ? 6.388   -53.338 22.771  1.00 36.65  0  25  SER   C OG  1 
ATOM   4037 N  N   . LYS   C  1 11  ? 8.280   -52.691 19.912  1.00 40.07  0  26  LYS   C N   1 
ATOM   4038 C  CA  . LYS   C  1 11  ? 8.071   -53.150 18.507  1.00 37.10  0  26  LYS   C CA  1 
ATOM   4039 C  C   . LYS   C  1 11  ? 9.292   -52.803 17.651  1.00 36.37  0  26  LYS   C C   1 
ATOM   4040 O  O   . LYS   C  1 11  ? 9.987   -51.772 17.930  1.00 31.50  0  26  LYS   C O   1 
ATOM   4041 C  CB  . LYS   C  1 11  ? 6.791   -52.539 17.940  1.00 40.49  0  26  LYS   C CB  1 
ATOM   4042 C  CG  . LYS   C  1 11  ? 5.513   -52.990 18.632  1.00 45.65  0  26  LYS   C CG  1 
ATOM   4043 C  CD  . LYS   C  1 11  ? 5.009   -54.339 18.122  1.00 59.81  0  26  LYS   C CD  1 
ATOM   4044 C  CE  . LYS   C  1 11  ? 3.618   -54.721 18.613  1.00 63.10  0  26  LYS   C CE  1 
ATOM   4045 N  NZ  . LYS   C  1 11  ? 3.597   -55.053 20.057  1.00 61.71  1  26  LYS   C NZ  1 
ATOM   4046 N  N   . TRP   C  1 12  ? 9.537   -53.621 16.624  1.00 30.57  0  27  TRP   C N   1 
ATOM   4047 C  CA  . TRP   C  1 12  ? 10.530  -53.392 15.543  1.00 27.93  0  27  TRP   C CA  1 
ATOM   4048 C  C   . TRP   C  1 12  ? 11.948  -53.349 16.096  1.00 28.42  0  27  TRP   C C   1 
ATOM   4049 O  O   . TRP   C  1 12  ? 12.684  -52.378 15.860  1.00 29.57  0  27  TRP   C O   1 
ATOM   4050 C  CB  . TRP   C  1 12  ? 10.189  -52.113 14.789  1.00 28.18  0  27  TRP   C CB  1 
ATOM   4051 C  CG  . TRP   C  1 12  ? 8.729   -51.828 14.706  1.00 28.72  0  27  TRP   C CG  1 
ATOM   4052 C  CD1 . TRP   C  1 12  ? 8.113   -50.687 15.098  1.00 30.42  0  27  TRP   C CD1 1 
ATOM   4053 C  CD2 . TRP   C  1 12  ? 7.697   -52.688 14.187  1.00 30.14  0  27  TRP   C CD2 1 
ATOM   4054 N  NE1 . TRP   C  1 12  ? 6.776   -50.769 14.856  1.00 30.96  0  27  TRP   C NE1 1 
ATOM   4055 C  CE2 . TRP   C  1 12  ? 6.488   -51.981 14.287  1.00 26.91  0  27  TRP   C CE2 1 
ATOM   4056 C  CE3 . TRP   C  1 12  ? 7.685   -53.978 13.633  1.00 30.27  0  27  TRP   C CE3 1 
ATOM   4057 C  CZ2 . TRP   C  1 12  ? 5.272   -52.519 13.863  1.00 29.31  0  27  TRP   C CZ2 1 
ATOM   4058 C  CZ3 . TRP   C  1 12  ? 6.477   -54.523 13.241  1.00 28.56  0  27  TRP   C CZ3 1 
ATOM   4059 C  CH2 . TRP   C  1 12  ? 5.293   -53.784 13.318  1.00 29.41  0  27  TRP   C CH2 1 
ATOM   4060 N  N   . PRO   C  1 13  ? 12.389  -54.377 16.855  1.00 28.11  0  28  PRO   C N   1 
ATOM   4061 C  CA  . PRO   C  1 13  ? 13.737  -54.389 17.442  1.00 28.44  0  28  PRO   C CA  1 
ATOM   4062 C  C   . PRO   C  1 13  ? 14.890  -54.479 16.435  1.00 26.69  0  28  PRO   C C   1 
ATOM   4063 O  O   . PRO   C  1 13  ? 16.057  -54.320 16.802  1.00 30.86  0  28  PRO   C O   1 
ATOM   4064 C  CB  . PRO   C  1 13  ? 13.744  -55.655 18.334  1.00 29.21  0  28  PRO   C CB  1 
ATOM   4065 C  CG  . PRO   C  1 13  ? 12.670  -56.556 17.733  1.00 29.79  0  28  PRO   C CG  1 
ATOM   4066 C  CD  . PRO   C  1 13  ? 11.623  -55.594 17.194  1.00 30.85  0  28  PRO   C CD  1 
ATOM   4067 N  N   . TRP   C  1 14  ? 14.556  -54.745 15.177  1.00 26.51  0  29  TRP   C N   1 
ATOM   4068 C  CA  . TRP   C  1 14  ? 15.524  -54.872 14.060  1.00 27.85  0  29  TRP   C CA  1 
ATOM   4069 C  C   . TRP   C  1 14  ? 15.731  -53.538 13.327  1.00 31.61  0  29  TRP   C C   1 
ATOM   4070 O  O   . TRP   C  1 14  ? 16.669  -53.484 12.505  1.00 26.45  0  29  TRP   C O   1 
ATOM   4071 C  CB  . TRP   C  1 14  ? 15.050  -55.967 13.091  1.00 30.83  0  29  TRP   C CB  1 
ATOM   4072 C  CG  . TRP   C  1 14  ? 13.613  -55.814 12.755  1.00 28.61  0  29  TRP   C CG  1 
ATOM   4073 C  CD1 . TRP   C  1 14  ? 13.061  -54.880 11.939  1.00 30.14  0  29  TRP   C CD1 1 
ATOM   4074 C  CD2 . TRP   C  1 14  ? 12.532  -56.617 13.253  1.00 30.91  0  29  TRP   C CD2 1 
ATOM   4075 N  NE1 . TRP   C  1 14  ? 11.704  -55.025 11.922  1.00 30.18  0  29  TRP   C NE1 1 
ATOM   4076 C  CE2 . TRP   C  1 14  ? 11.349  -56.085 12.719  1.00 29.02  0  29  TRP   C CE2 1 
ATOM   4077 C  CE3 . TRP   C  1 14  ? 12.458  -57.696 14.139  1.00 30.39  0  29  TRP   C CE3 1 
ATOM   4078 C  CZ2 . TRP   C  1 14  ? 10.098  -56.615 13.010  1.00 32.03  0  29  TRP   C CZ2 1 
ATOM   4079 C  CZ3 . TRP   C  1 14  ? 11.217  -58.199 14.447  1.00 30.49  0  29  TRP   C CZ3 1 
ATOM   4080 C  CH2 . TRP   C  1 14  ? 10.062  -57.692 13.865  1.00 30.39  0  29  TRP   C CH2 1 
ATOM   4081 N  N   . GLN   C  1 15  ? 14.902  -52.507 13.568  1.00 27.48  0  30  GLN   C N   1 
ATOM   4082 C  CA  . GLN   C  1 15  ? 14.993  -51.228 12.809  1.00 28.96  0  30  GLN   C CA  1 
ATOM   4083 C  C   . GLN   C  1 15  ? 16.372  -50.613 13.041  1.00 26.05  0  30  GLN   C C   1 
ATOM   4084 O  O   . GLN   C  1 15  ? 16.811  -50.590 14.224  1.00 29.61  0  30  GLN   C O   1 
ATOM   4085 C  CB  . GLN   C  1 15  ? 13.896  -50.230 13.190  1.00 30.40  0  30  GLN   C CB  1 
ATOM   4086 C  CG  . GLN   C  1 15  ? 13.967  -48.922 12.409  1.00 28.96  0  30  GLN   C CG  1 
ATOM   4087 C  CD  . GLN   C  1 15  ? 13.485  -48.999 10.977  1.00 28.74  0  30  GLN   C CD  1 
ATOM   4088 O  OE1 . GLN   C  1 15  ? 12.436  -49.558 10.679  1.00 29.00  0  30  GLN   C OE1 1 
ATOM   4089 N  NE2 . GLN   C  1 15  ? 14.242  -48.390 10.074  1.00 29.70  0  30  GLN   C NE2 1 
ATOM   4090 N  N   . VAL   C  1 16  ? 17.048  -50.180 11.970  1.00 24.52  0  31  VAL   C N   1 
ATOM   4091 C  CA  . VAL   C  1 16  ? 18.310  -49.394 12.106  1.00 27.56  0  31  VAL   C CA  1 
ATOM   4092 C  C   . VAL   C  1 16  ? 18.222  -48.085 11.315  1.00 25.36  0  31  VAL   C C   1 
ATOM   4093 O  O   . VAL   C  1 16  ? 17.415  -47.983 10.373  1.00 25.86  0  31  VAL   C O   1 
ATOM   4094 C  CB  . VAL   C  1 16  ? 19.590  -50.191 11.806  1.00 32.90  0  31  VAL   C CB  1 
ATOM   4095 C  CG1 . VAL   C  1 16  ? 19.500  -51.627 12.290  1.00 34.93  0  31  VAL   C CG1 1 
ATOM   4096 C  CG2 . VAL   C  1 16  ? 20.021  -50.132 10.358  1.00 34.43  0  31  VAL   C CG2 1 
ATOM   4097 N  N   . SER   C  1 17  ? 19.015  -47.107 11.743  1.00 24.83  0  32  SER   C N   1 
ATOM   4098 C  CA  . SER   C  1 17  ? 19.213  -45.789 11.098  1.00 24.64  0  32  SER   C CA  1 
ATOM   4099 C  C   . SER   C  1 17  ? 20.623  -45.728 10.524  1.00 24.21  0  32  SER   C C   1 
ATOM   4100 O  O   . SER   C  1 17  ? 21.565  -46.017 11.252  1.00 26.82  0  32  SER   C O   1 
ATOM   4101 C  CB  . SER   C  1 17  ? 18.981  -44.681 12.102  1.00 26.71  0  32  SER   C CB  1 
ATOM   4102 O  OG  . SER   C  1 17  ? 19.354  -43.428 11.569  1.00 23.30  0  32  SER   C OG  1 
ATOM   4103 N  N   . LEU   C  1 18  ? 20.740  -45.373 9.248   1.00 25.53  0  33  LEU   C N   1 
ATOM   4104 C  CA  . LEU   C  1 18  ? 22.034  -45.144 8.561   1.00 28.46  0  33  LEU   C CA  1 
ATOM   4105 C  C   . LEU   C  1 18  ? 22.361  -43.666 8.690   1.00 24.21  0  33  LEU   C C   1 
ATOM   4106 O  O   . LEU   C  1 18  ? 21.476  -42.861 8.408   1.00 23.78  0  33  LEU   C O   1 
ATOM   4107 C  CB  . LEU   C  1 18  ? 21.965  -45.553 7.078   1.00 27.07  0  33  LEU   C CB  1 
ATOM   4108 C  CG  . LEU   C  1 18  ? 21.528  -46.991 6.775   1.00 33.32  0  33  LEU   C CG  1 
ATOM   4109 C  CD1 . LEU   C  1 18  ? 21.971  -47.424 5.373   1.00 35.10  0  33  LEU   C CD1 1 
ATOM   4110 C  CD2 . LEU   C  1 18  ? 22.065  -47.974 7.795   1.00 34.60  0  33  LEU   C CD2 1 
ATOM   4111 N  N   . ARG   C  1 19  ? 23.612  -43.369 9.029   1.00 24.07  0  34  ARG   C N   1 
ATOM   4112 C  CA  . ARG   C  1 19  ? 24.112  -42.019 9.373   1.00 26.26  0  34  ARG   C CA  1 
ATOM   4113 C  C   . ARG   C  1 19  ? 25.296  -41.642 8.493   1.00 25.16  0  34  ARG   C C   1 
ATOM   4114 O  O   . ARG   C  1 19  ? 26.162  -42.489 8.313   1.00 25.89  0  34  ARG   C O   1 
ATOM   4115 C  CB  . ARG   C  1 19  ? 24.541  -41.931 10.842  1.00 27.41  0  34  ARG   C CB  1 
ATOM   4116 C  CG  . ARG   C  1 19  ? 23.432  -42.281 11.815  1.00 29.02  0  34  ARG   C CG  1 
ATOM   4117 C  CD  . ARG   C  1 19  ? 22.171  -41.444 11.689  1.00 27.76  0  34  ARG   C CD  1 
ATOM   4118 N  NE  . ARG   C  1 19  ? 21.294  -41.737 12.805  1.00 30.59  0  34  ARG   C NE  1 
ATOM   4119 C  CZ  . ARG   C  1 19  ? 21.497  -41.330 14.068  1.00 28.58  0  34  ARG   C CZ  1 
ATOM   4120 N  NH1 . ARG   C  1 19  ? 22.509  -40.532 14.359  1.00 23.93  1  34  ARG   C NH1 1 
ATOM   4121 N  NH2 . ARG   C  1 19  ? 20.624  -41.672 15.005  1.00 31.04  0  34  ARG   C NH2 1 
ATOM   4122 N  N   . VAL   C  1 20  ? 25.290  -40.406 7.966   1.00 27.87  0  35  VAL   C N   1 
ATOM   4123 C  CA  . VAL   C  1 20  ? 26.359  -39.835 7.095   1.00 28.64  0  35  VAL   C CA  1 
ATOM   4124 C  C   . VAL   C  1 20  ? 27.067  -38.726 7.878   1.00 31.44  0  35  VAL   C C   1 
ATOM   4125 O  O   . VAL   C  1 20  ? 26.360  -37.922 8.510   1.00 28.46  0  35  VAL   C O   1 
ATOM   4126 C  CB  . VAL   C  1 20  ? 25.830  -39.316 5.741   1.00 29.05  0  35  VAL   C CB  1 
ATOM   4127 C  CG1 . VAL   C  1 20  ? 24.743  -38.263 5.859   1.00 30.62  0  35  VAL   C CG1 1 
ATOM   4128 C  CG2 . VAL   C  1 20  ? 26.946  -38.750 4.891   1.00 31.24  0  35  VAL   C CG2 1 
ATOM   4129 N  N   . HIS   C  1 21  ? 28.402  -38.669 7.805   1.00 36.16  0  36  HIS   C N   1 
ATOM   4130 C  CA  . HIS   C  1 21  ? 29.234  -37.638 8.487   1.00 43.53  0  36  HIS   C CA  1 
ATOM   4131 C  C   . HIS   C  1 21  ? 28.922  -36.249 7.903   1.00 39.56  0  36  HIS   C C   1 
ATOM   4132 O  O   . HIS   C  1 21  ? 28.894  -36.125 6.714   1.00 41.14  0  36  HIS   C O   1 
ATOM   4133 C  CB  . HIS   C  1 21  ? 30.741  -37.945 8.388   1.00 45.83  0  36  HIS   C CB  1 
ATOM   4134 C  CG  . HIS   C  1 21  ? 31.577  -36.971 9.152   1.00 52.53  0  36  HIS   C CG  1 
ATOM   4135 N  ND1 . HIS   C  1 21  ? 31.687  -37.009 10.541  1.00 55.07  0  36  HIS   C ND1 1 
ATOM   4136 C  CD2 . HIS   C  1 21  ? 32.273  -35.884 8.743   1.00 58.52  0  36  HIS   C CD2 1 
ATOM   4137 C  CE1 . HIS   C  1 21  ? 32.446  -36.011 10.947  1.00 57.50  0  36  HIS   C CE1 1 
ATOM   4138 N  NE2 . HIS   C  1 21  ? 32.809  -35.301 9.862   1.00 59.58  0  36  HIS   C NE2 1 
ATOM   4139 N  N   . GLY   C  1 22  ? 28.686  -35.248 8.745   1.00 44.99  0  37  GLY   C N   1 
ATOM   4140 C  CA  . GLY   C  1 22  ? 28.516  -33.829 8.373   1.00 43.19  0  37  GLY   C CA  1 
ATOM   4141 C  C   . GLY   C  1 22  ? 28.637  -32.961 9.630   1.00 46.47  0  37  GLY   C C   1 
ATOM   4142 O  O   . GLY   C  1 22  ? 29.343  -33.343 10.556  1.00 51.08  0  37  GLY   C O   1 
ATOM   4143 N  N   . PRO   C  1 23  ? 27.936  -31.807 9.733   1.00 41.81  0  38  PRO   C N   1 
ATOM   4144 C  CA  . PRO   C  1 23  ? 27.886  -31.039 10.977  1.00 40.35  0  38  PRO   C CA  1 
ATOM   4145 C  C   . PRO   C  1 23  ? 27.397  -31.910 12.143  1.00 39.77  0  38  PRO   C C   1 
ATOM   4146 O  O   . PRO   C  1 23  ? 27.744  -31.647 13.287  1.00 42.82  0  38  PRO   C O   1 
ATOM   4147 C  CB  . PRO   C  1 23  ? 26.852  -29.933 10.690  1.00 40.66  0  38  PRO   C CB  1 
ATOM   4148 C  CG  . PRO   C  1 23  ? 26.817  -29.822 9.194   1.00 41.71  0  38  PRO   C CG  1 
ATOM   4149 C  CD  . PRO   C  1 23  ? 27.118  -31.211 8.667   1.00 43.48  0  38  PRO   C CD  1 
ATOM   4150 N  N   . TYR   C  1 24  ? 26.570  -32.914 11.841  1.00 34.86  0  39  TYR   C N   1 
ATOM   4151 C  CA  . TYR   C  1 24  ? 26.233  -34.041 12.758  1.00 30.97  0  39  TYR   C CA  1 
ATOM   4152 C  C   . TYR   C  1 24  ? 26.040  -35.344 11.940  1.00 33.16  0  39  TYR   C C   1 
ATOM   4153 O  O   . TYR   C  1 24  ? 26.037  -35.300 10.683  1.00 35.28  0  39  TYR   C O   1 
ATOM   4154 C  CB  . TYR   C  1 24  ? 24.989  -33.692 13.568  1.00 26.96  0  39  TYR   C CB  1 
ATOM   4155 C  CG  . TYR   C  1 24  ? 23.737  -33.485 12.749  1.00 28.11  0  39  TYR   C CG  1 
ATOM   4156 C  CD1 . TYR   C  1 24  ? 23.520  -32.337 11.993  1.00 30.08  0  39  TYR   C CD1 1 
ATOM   4157 C  CD2 . TYR   C  1 24  ? 22.735  -34.441 12.760  1.00 27.83  0  39  TYR   C CD2 1 
ATOM   4158 C  CE1 . TYR   C  1 24  ? 22.343  -32.160 11.265  1.00 27.80  0  39  TYR   C CE1 1 
ATOM   4159 C  CE2 . TYR   C  1 24  ? 21.559  -34.274 12.059  1.00 28.59  0  39  TYR   C CE2 1 
ATOM   4160 C  CZ  . TYR   C  1 24  ? 21.378  -33.157 11.266  1.00 29.10  0  39  TYR   C CZ  1 
ATOM   4161 O  OH  . TYR   C  1 24  ? 20.174  -33.066 10.611  1.00 30.74  0  39  TYR   C OH  1 
ATOM   4162 N  N   . TRP   C  1 25  ? 25.917  -36.474 12.635  1.00 28.39  0  40  TRP   C N   1 
ATOM   4163 C  CA  . TRP   C  1 25  ? 25.705  -37.818 12.031  1.00 27.62  0  40  TRP   C CA  1 
ATOM   4164 C  C   . TRP   C  1 25  ? 24.236  -37.939 11.667  1.00 25.79  0  40  TRP   C C   1 
ATOM   4165 O  O   . TRP   C  1 25  ? 23.442  -38.336 12.495  1.00 27.36  0  40  TRP   C O   1 
ATOM   4166 C  CB  . TRP   C  1 25  ? 26.175  -38.931 12.960  1.00 27.74  0  40  TRP   C CB  1 
ATOM   4167 C  CG  . TRP   C  1 25  ? 27.664  -38.998 12.997  1.00 31.36  0  40  TRP   C CG  1 
ATOM   4168 C  CD1 . TRP   C  1 25  ? 28.475  -38.473 13.946  1.00 34.19  0  40  TRP   C CD1 1 
ATOM   4169 C  CD2 . TRP   C  1 25  ? 28.522  -39.664 12.056  1.00 36.03  0  40  TRP   C CD2 1 
ATOM   4170 N  NE1 . TRP   C  1 25  ? 29.780  -38.744 13.651  1.00 36.45  0  40  TRP   C NE1 1 
ATOM   4171 C  CE2 . TRP   C  1 25  ? 29.844  -39.493 12.511  1.00 37.26  0  40  TRP   C CE2 1 
ATOM   4172 C  CE3 . TRP   C  1 25  ? 28.306  -40.432 10.903  1.00 34.04  0  40  TRP   C CE3 1 
ATOM   4173 C  CZ2 . TRP   C  1 25  ? 30.952  -39.997 11.822  1.00 34.16  0  40  TRP   C CZ2 1 
ATOM   4174 C  CZ3 . TRP   C  1 25  ? 29.392  -40.957 10.240  1.00 33.01  0  40  TRP   C CZ3 1 
ATOM   4175 C  CH2 . TRP   C  1 25  ? 30.697  -40.737 10.692  1.00 38.23  0  40  TRP   C CH2 1 
ATOM   4176 N  N   . MET   C  1 26  ? 23.922  -37.524 10.451  1.00 28.12  0  41  MET   C N   1 
ATOM   4177 C  CA  . MET   C  1 26  ? 22.542  -37.316 9.986   1.00 28.13  0  41  MET   C CA  1 
ATOM   4178 C  C   . MET   C  1 26  ? 21.952  -38.634 9.445   1.00 26.29  0  41  MET   C C   1 
ATOM   4179 O  O   . MET   C  1 26  ? 22.610  -39.310 8.667   1.00 31.04  0  41  MET   C O   1 
ATOM   4180 C  CB  . MET   C  1 26  ? 22.572  -36.232 8.906   1.00 29.58  0  41  MET   C CB  1 
ATOM   4181 C  CG  . MET   C  1 26  ? 21.190  -35.706 8.593   1.00 36.14  0  41  MET   C CG  1 
ATOM   4182 S  SD  . MET   C  1 26  ? 21.139  -34.367 7.356   1.00 41.29  0  41  MET   C SD  1 
ATOM   4183 C  CE  . MET   C  1 26  ? 22.750  -33.593 7.519   1.00 48.36  0  41  MET   C CE  1 
ATOM   4184 N  N   . HIS   C  1 27  ? 20.731  -38.947 9.830   1.00 26.75  0  42  HIS   C N   1 
ATOM   4185 C  CA  . HIS   C  1 27  ? 19.896  -40.018 9.240   1.00 27.81  0  42  HIS   C CA  1 
ATOM   4186 C  C   . HIS   C  1 27  ? 19.642  -39.712 7.759   1.00 31.29  0  42  HIS   C C   1 
ATOM   4187 O  O   . HIS   C  1 27  ? 19.178  -38.624 7.457   1.00 28.88  0  42  HIS   C O   1 
ATOM   4188 C  CB  . HIS   C  1 27  ? 18.590  -40.150 9.994   1.00 27.30  0  42  HIS   C CB  1 
ATOM   4189 C  CG  . HIS   C  1 27  ? 17.660  -41.113 9.349   1.00 29.50  0  42  HIS   C CG  1 
ATOM   4190 N  ND1 . HIS   C  1 27  ? 17.647  -42.446 9.689   1.00 26.31  0  42  HIS   C ND1 1 
ATOM   4191 C  CD2 . HIS   C  1 27  ? 16.757  -40.942 8.348   1.00 25.52  0  42  HIS   C CD2 1 
ATOM   4192 C  CE1 . HIS   C  1 27  ? 16.712  -43.040 8.978   1.00 25.58  0  42  HIS   C CE1 1 
ATOM   4193 N  NE2 . HIS   C  1 27  ? 16.167  -42.144 8.138   1.00 23.50  0  42  HIS   C NE2 1 
ATOM   4194 N  N   . PHE   C  1 28  ? 19.972  -40.641 6.873   1.00 30.21  0  43  PHE   C N   1 
ATOM   4195 C  CA  . PHE   C  1 28  ? 19.615  -40.553 5.431   1.00 32.02  0  43  PHE   C CA  1 
ATOM   4196 C  C   . PHE   C  1 28  ? 18.786  -41.774 4.984   1.00 29.66  0  43  PHE   C C   1 
ATOM   4197 O  O   . PHE   C  1 28  ? 18.114  -41.700 3.944   1.00 30.27  0  43  PHE   C O   1 
ATOM   4198 C  CB  . PHE   C  1 28  ? 20.885  -40.347 4.615   1.00 27.39  0  43  PHE   C CB  1 
ATOM   4199 C  CG  . PHE   C  1 28  ? 21.834  -41.517 4.616   1.00 28.17  0  43  PHE   C CG  1 
ATOM   4200 C  CD1 . PHE   C  1 28  ? 21.708  -42.539 3.692   1.00 29.47  0  43  PHE   C CD1 1 
ATOM   4201 C  CD2 . PHE   C  1 28  ? 22.900  -41.558 5.493   1.00 30.19  0  43  PHE   C CD2 1 
ATOM   4202 C  CE1 . PHE   C  1 28  ? 22.595  -43.606 3.669   1.00 31.76  0  43  PHE   C CE1 1 
ATOM   4203 C  CE2 . PHE   C  1 28  ? 23.822  -42.596 5.451   1.00 29.66  0  43  PHE   C CE2 1 
ATOM   4204 C  CZ  . PHE   C  1 28  ? 23.647  -43.641 4.562   1.00 32.14  0  43  PHE   C CZ  1 
ATOM   4205 N  N   . CYS   C  1 29  ? 18.851  -42.905 5.683   1.00 26.68  0  44  CYS   C N   1 
ATOM   4206 C  CA  . CYS   C  1 29  ? 18.132  -44.135 5.261   1.00 26.97  0  44  CYS   C CA  1 
ATOM   4207 C  C   . CYS   C  1 29  ? 17.920  -45.051 6.455   1.00 25.36  0  44  CYS   C C   1 
ATOM   4208 O  O   . CYS   C  1 29  ? 18.643  -44.901 7.451   1.00 28.24  0  44  CYS   C O   1 
ATOM   4209 C  CB  . CYS   C  1 29  ? 18.885  -44.888 4.156   1.00 25.26  0  44  CYS   C CB  1 
ATOM   4210 S  SG  . CYS   C  1 29  ? 18.558  -44.305 2.461   1.00 29.58  0  44  CYS   C SG  1 
ATOM   4211 N  N   . GLY   C  1 30  ? 16.976  -45.974 6.294   1.00 24.26  0  45  GLY   C N   1 
ATOM   4212 C  CA  . GLY   C  1 30  ? 16.744  -47.107 7.188   1.00 26.13  0  45  GLY   C CA  1 
ATOM   4213 C  C   . GLY   C  1 30  ? 17.495  -48.345 6.733   1.00 26.38  0  45  GLY   C C   1 
ATOM   4214 O  O   . GLY   C  1 30  ? 18.197  -48.327 5.698   1.00 25.30  0  45  GLY   C O   1 
ATOM   4215 N  N   . GLY   C  1 31  ? 17.361  -49.379 7.541   1.00 26.71  0  46  GLY   C N   1 
ATOM   4216 C  CA  . GLY   C  1 31  ? 17.932  -50.721 7.354   1.00 29.10  0  46  GLY   C CA  1 
ATOM   4217 C  C   . GLY   C  1 31  ? 17.271  -51.674 8.338   1.00 26.05  0  46  GLY   C C   1 
ATOM   4218 O  O   . GLY   C  1 31  ? 16.421  -51.228 9.148   1.00 27.39  0  46  GLY   C O   1 
ATOM   4219 N  N   . SER   C  1 32  ? 17.635  -52.944 8.289   1.00 25.59  0  47  SER   C N   1 
ATOM   4220 C  CA  . SER   C  1 32  ? 17.144  -53.979 9.228   1.00 26.61  0  47  SER   C CA  1 
ATOM   4221 C  C   . SER   C  1 32  ? 18.320  -54.846 9.649   1.00 25.91  0  47  SER   C C   1 
ATOM   4222 O  O   . SER   C  1 32  ? 19.244  -55.077 8.828   1.00 29.14  0  47  SER   C O   1 
ATOM   4223 C  CB  . SER   C  1 32  ? 16.006  -54.753 8.624   1.00 26.55  0  47  SER   C CB  1 
ATOM   4224 O  OG  . SER   C  1 32  ? 16.425  -55.416 7.442   1.00 26.21  0  47  SER   C OG  1 
ATOM   4225 N  N   . LEU   C  1 33  ? 18.335  -55.242 10.916  1.00 27.03  0  48  LEU   C N   1 
ATOM   4226 C  CA  . LEU   C  1 33  ? 19.353  -56.188 11.427  1.00 29.86  0  48  LEU   C CA  1 
ATOM   4227 C  C   . LEU   C  1 33  ? 18.876  -57.608 11.081  1.00 29.59  0  48  LEU   C C   1 
ATOM   4228 O  O   . LEU   C  1 33  ? 17.841  -58.023 11.598  1.00 30.35  0  48  LEU   C O   1 
ATOM   4229 C  CB  . LEU   C  1 33  ? 19.508  -55.964 12.929  1.00 34.15  0  48  LEU   C CB  1 
ATOM   4230 C  CG  . LEU   C  1 33  ? 20.654  -56.723 13.583  1.00 34.39  0  48  LEU   C CG  1 
ATOM   4231 C  CD1 . LEU   C  1 33  ? 21.974  -56.073 13.217  1.00 32.81  0  48  LEU   C CD1 1 
ATOM   4232 C  CD2 . LEU   C  1 33  ? 20.452  -56.782 15.096  1.00 36.79  0  48  LEU   C CD2 1 
ATOM   4233 N  N   . ILE   C  1 34  ? 19.533  -58.283 10.136  1.00 31.69  0  49  ILE   C N   1 
ATOM   4234 C  CA  . ILE   C  1 34  ? 19.143  -59.663 9.681   1.00 32.51  0  49  ILE   C CA  1 
ATOM   4235 C  C   . ILE   C  1 34  ? 20.076  -60.709 10.317  1.00 31.94  0  49  ILE   C C   1 
ATOM   4236 O  O   . ILE   C  1 34  ? 19.839  -61.881 10.181  1.00 32.84  0  49  ILE   C O   1 
ATOM   4237 C  CB  . ILE   C  1 34  ? 19.135  -59.767 8.141   1.00 27.76  0  49  ILE   C CB  1 
ATOM   4238 C  CG1 . ILE   C  1 34  ? 20.473  -59.363 7.526   1.00 28.32  0  49  ILE   C CG1 1 
ATOM   4239 C  CG2 . ILE   C  1 34  ? 17.970  -58.958 7.582   1.00 29.33  0  49  ILE   C CG2 1 
ATOM   4240 C  CD1 . ILE   C  1 34  ? 20.677  -59.888 6.121   1.00 31.64  0  49  ILE   C CD1 1 
ATOM   4241 N  N   . HIS   C  1 35  ? 21.151  -60.271 10.941  1.00 34.46  0  50  HIS   C N   1 
ATOM   4242 C  CA  . HIS   C  1 35  ? 22.164  -61.117 11.588  1.00 35.41  0  50  HIS   C CA  1 
ATOM   4243 C  C   . HIS   C  1 35  ? 22.870  -60.191 12.559  1.00 37.57  0  50  HIS   C C   1 
ATOM   4244 O  O   . HIS   C  1 35  ? 22.922  -58.981 12.296  1.00 32.15  0  50  HIS   C O   1 
ATOM   4245 C  CB  . HIS   C  1 35  ? 23.080  -61.721 10.519  1.00 35.35  0  50  HIS   C CB  1 
ATOM   4246 C  CG  . HIS   C  1 35  ? 24.168  -62.590 11.041  1.00 35.47  0  50  HIS   C CG  1 
ATOM   4247 N  ND1 . HIS   C  1 35  ? 25.352  -62.078 11.561  1.00 41.55  0  50  HIS   C ND1 1 
ATOM   4248 C  CD2 . HIS   C  1 35  ? 24.247  -63.936 11.158  1.00 33.99  0  50  HIS   C CD2 1 
ATOM   4249 C  CE1 . HIS   C  1 35  ? 26.146  -63.078 11.936  1.00 34.01  0  50  HIS   C CE1 1 
ATOM   4250 N  NE2 . HIS   C  1 35  ? 25.475  -64.233 11.688  1.00 32.78  0  50  HIS   C NE2 1 
ATOM   4251 N  N   . PRO   C  1 36  ? 23.417  -60.695 13.691  1.00 36.82  0  51  PRO   C N   1 
ATOM   4252 C  CA  . PRO   C  1 36  ? 24.171  -59.837 14.610  1.00 34.88  0  51  PRO   C CA  1 
ATOM   4253 C  C   . PRO   C  1 36  ? 25.241  -58.941 13.980  1.00 30.69  0  51  PRO   C C   1 
ATOM   4254 O  O   . PRO   C  1 36  ? 25.517  -57.913 14.569  1.00 33.86  0  51  PRO   C O   1 
ATOM   4255 C  CB  . PRO   C  1 36  ? 24.824  -60.867 15.561  1.00 37.21  0  51  PRO   C CB  1 
ATOM   4256 C  CG  . PRO   C  1 36  ? 23.769  -61.955 15.626  1.00 36.68  0  51  PRO   C CG  1 
ATOM   4257 C  CD  . PRO   C  1 36  ? 23.303  -62.085 14.187  1.00 37.59  0  51  PRO   C CD  1 
ATOM   4258 N  N   . GLN   C  1 37  ? 25.800  -59.315 12.825  1.00 32.19  0  52  GLN   C N   1 
ATOM   4259 C  CA  . GLN   C  1 37  ? 26.893  -58.539 12.172  1.00 32.78  0  52  GLN   C CA  1 
ATOM   4260 C  C   . GLN   C  1 37  ? 26.455  -58.025 10.789  1.00 27.52  0  52  GLN   C C   1 
ATOM   4261 O  O   . GLN   C  1 37  ? 27.307  -57.441 10.074  1.00 26.90  0  52  GLN   C O   1 
ATOM   4262 C  CB  . GLN   C  1 37  ? 28.157  -59.388 12.136  1.00 32.91  0  52  GLN   C CB  1 
ATOM   4263 C  CG  . GLN   C  1 37  ? 29.426  -58.569 11.884  1.00 35.28  0  52  GLN   C CG  1 
ATOM   4264 C  CD  . GLN   C  1 37  ? 30.680  -59.143 12.501  1.00 33.74  0  52  GLN   C CD  1 
ATOM   4265 O  OE1 . GLN   C  1 37  ? 30.649  -60.239 13.029  1.00 37.19  0  52  GLN   C OE1 1 
ATOM   4266 N  NE2 . GLN   C  1 37  ? 31.797  -58.418 12.411  1.00 31.80  0  52  GLN   C NE2 1 
ATOM   4267 N  N   . TRP   C  1 38  ? 25.169  -58.147 10.425  1.00 32.58  0  53  TRP   C N   1 
ATOM   4268 C  CA  . TRP   C  1 38  ? 24.718  -57.729 9.062   1.00 31.02  0  53  TRP   C CA  1 
ATOM   4269 C  C   . TRP   C  1 38  ? 23.450  -56.877 9.111   1.00 26.94  0  53  TRP   C C   1 
ATOM   4270 O  O   . TRP   C  1 38  ? 22.422  -57.296 9.711   1.00 27.44  0  53  TRP   C O   1 
ATOM   4271 C  CB  . TRP   C  1 38  ? 24.541  -58.945 8.154   1.00 30.94  0  53  TRP   C CB  1 
ATOM   4272 C  CG  . TRP   C  1 38  ? 25.836  -59.629 7.830   1.00 33.34  0  53  TRP   C CG  1 
ATOM   4273 C  CD1 . TRP   C  1 38  ? 26.403  -60.643 8.536   1.00 34.06  0  53  TRP   C CD1 1 
ATOM   4274 C  CD2 . TRP   C  1 38  ? 26.744  -59.359 6.744   1.00 36.10  0  53  TRP   C CD2 1 
ATOM   4275 N  NE1 . TRP   C  1 38  ? 27.576  -61.036 7.954   1.00 32.94  0  53  TRP   C NE1 1 
ATOM   4276 C  CE2 . TRP   C  1 38  ? 27.809  -60.289 6.844   1.00 34.91  0  53  TRP   C CE2 1 
ATOM   4277 C  CE3 . TRP   C  1 38  ? 26.744  -58.471 5.661   1.00 34.66  0  53  TRP   C CE3 1 
ATOM   4278 C  CZ2 . TRP   C  1 38  ? 28.860  -60.345 5.927   1.00 35.54  0  53  TRP   C CZ2 1 
ATOM   4279 C  CZ3 . TRP   C  1 38  ? 27.799  -58.499 4.767   1.00 34.57  0  53  TRP   C CZ3 1 
ATOM   4280 C  CH2 . TRP   C  1 38  ? 28.837  -59.436 4.887   1.00 35.33  0  53  TRP   C CH2 1 
ATOM   4281 N  N   . VAL   C  1 39  ? 23.499  -55.783 8.356   1.00 28.71  0  54  VAL   C N   1 
ATOM   4282 C  CA  . VAL   C  1 39  ? 22.320  -54.911 8.085   1.00 26.07  0  54  VAL   C CA  1 
ATOM   4283 C  C   . VAL   C  1 39  ? 21.961  -55.026 6.604   1.00 26.15  0  54  VAL   C C   1 
ATOM   4284 O  O   . VAL   C  1 39  ? 22.862  -54.847 5.737   1.00 26.05  0  54  VAL   C O   1 
ATOM   4285 C  CB  . VAL   C  1 39  ? 22.609  -53.449 8.489   1.00 26.46  0  54  VAL   C CB  1 
ATOM   4286 C  CG1 . VAL   C  1 39  ? 21.511  -52.492 8.038   1.00 24.03  0  54  VAL   C CG1 1 
ATOM   4287 C  CG2 . VAL   C  1 39  ? 22.825  -53.331 9.992   1.00 26.45  0  54  VAL   C CG2 1 
ATOM   4288 N  N   . LEU   C  1 40  ? 20.673  -55.226 6.353   1.00 26.64  0  55  LEU   C N   1 
ATOM   4289 C  CA  . LEU   C  1 40  ? 20.052  -55.201 5.015   1.00 27.89  0  55  LEU   C CA  1 
ATOM   4290 C  C   . LEU   C  1 40  ? 19.473  -53.793 4.767   1.00 29.60  0  55  LEU   C C   1 
ATOM   4291 O  O   . LEU   C  1 40  ? 18.688  -53.291 5.630   1.00 26.01  0  55  LEU   C O   1 
ATOM   4292 C  CB  . LEU   C  1 40  ? 18.948  -56.257 5.001   1.00 27.86  0  55  LEU   C CB  1 
ATOM   4293 C  CG  . LEU   C  1 40  ? 18.237  -56.455 3.667   1.00 27.51  0  55  LEU   C CG  1 
ATOM   4294 C  CD1 . LEU   C  1 40  ? 19.163  -57.070 2.643   1.00 29.26  0  55  LEU   C CD1 1 
ATOM   4295 C  CD2 . LEU   C  1 40  ? 17.018  -57.305 3.860   1.00 29.31  0  55  LEU   C CD2 1 
ATOM   4296 N  N   . THR   C  1 41  ? 19.825  -53.191 3.628   1.00 29.24  0  56  THR   C N   1 
ATOM   4297 C  CA  . THR   C  1 41  ? 19.288  -51.885 3.179   1.00 28.56  0  56  THR   C CA  1 
ATOM   4298 C  C   . THR   C  1 41  ? 19.061  -51.870 1.651   1.00 28.26  0  56  THR   C C   1 
ATOM   4299 O  O   . THR   C  1 41  ? 19.136  -52.915 0.983   1.00 23.98  0  56  THR   C O   1 
ATOM   4300 C  CB  . THR   C  1 41  ? 20.214  -50.807 3.745   1.00 24.36  0  56  THR   C CB  1 
ATOM   4301 O  OG1 . THR   C  1 41  ? 19.541  -49.568 3.622   1.00 27.26  0  56  THR   C OG1 1 
ATOM   4302 C  CG2 . THR   C  1 41  ? 21.562  -50.694 3.084   1.00 25.48  0  56  THR   C CG2 1 
ATOM   4303 N  N   . ALA   C  1 42  ? 18.698  -50.703 1.125   1.00 27.10  0  57  ALA   C N   1 
ATOM   4304 C  CA  . ALA   C  1 42  ? 18.529  -50.432 -0.325  1.00 26.40  0  57  ALA   C CA  1 
ATOM   4305 C  C   . ALA   C  1 42  ? 19.893  -50.052 -0.897  1.00 23.64  0  57  ALA   C C   1 
ATOM   4306 O  O   . ALA   C  1 42  ? 20.560  -49.251 -0.269  1.00 25.82  0  57  ALA   C O   1 
ATOM   4307 C  CB  . ALA   C  1 42  ? 17.535  -49.313 -0.547  1.00 28.11  0  57  ALA   C CB  1 
ATOM   4308 N  N   . ALA   C  1 43  ? 20.264  -50.578 -2.053  1.00 21.20  0  58  ALA   C N   1 
ATOM   4309 C  CA  . ALA   C  1 43  ? 21.463  -50.162 -2.821  1.00 21.41  0  58  ALA   C CA  1 
ATOM   4310 C  C   . ALA   C  1 43  ? 21.481  -48.652 -3.090  1.00 22.78  0  58  ALA   C C   1 
ATOM   4311 O  O   . ALA   C  1 43  ? 22.578  -48.057 -3.085  1.00 21.80  0  58  ALA   C O   1 
ATOM   4312 C  CB  . ALA   C  1 43  ? 21.504  -50.898 -4.140  1.00 24.00  0  58  ALA   C CB  1 
ATOM   4313 N  N   . HIS   C  1 44  ? 20.338  -48.040 -3.417  1.00 22.85  0  59  HIS   C N   1 
ATOM   4314 C  CA  . HIS   C  1 44  ? 20.286  -46.603 -3.808  1.00 24.13  0  59  HIS   C CA  1 
ATOM   4315 C  C   . HIS   C  1 44  ? 20.684  -45.715 -2.608  1.00 24.50  0  59  HIS   C C   1 
ATOM   4316 O  O   . HIS   C  1 44  ? 21.055  -44.573 -2.844  1.00 27.10  0  59  HIS   C O   1 
ATOM   4317 C  CB  . HIS   C  1 44  ? 18.921  -46.265 -4.428  1.00 22.50  0  59  HIS   C CB  1 
ATOM   4318 C  CG  . HIS   C  1 44  ? 17.872  -45.882 -3.457  1.00 25.80  0  59  HIS   C CG  1 
ATOM   4319 N  ND1 . HIS   C  1 44  ? 16.869  -46.766 -3.081  1.00 25.52  0  59  HIS   C ND1 1 
ATOM   4320 C  CD2 . HIS   C  1 44  ? 17.695  -44.743 -2.740  1.00 24.43  0  59  HIS   C CD2 1 
ATOM   4321 C  CE1 . HIS   C  1 44  ? 16.104  -46.175 -2.200  1.00 25.21  0  59  HIS   C CE1 1 
ATOM   4322 N  NE2 . HIS   C  1 44  ? 16.584  -44.920 -1.978  1.00 23.38  0  59  HIS   C NE2 1 
ATOM   4323 N  N   . CYS   C  1 45  ? 20.618  -46.212 -1.363  1.00 25.56  0  60  CYS   C N   1 
ATOM   4324 C  CA  . CYS   C  1 45  ? 21.095  -45.470 -0.161  1.00 25.17  0  60  CYS   C CA  1 
ATOM   4325 C  C   . CYS   C  1 45  ? 22.606  -45.306 -0.183  1.00 27.60  0  60  CYS   C C   1 
ATOM   4326 O  O   . CYS   C  1 45  ? 23.111  -44.320 0.426   1.00 27.55  0  60  CYS   C O   1 
ATOM   4327 C  CB  . CYS   C  1 45  ? 20.697  -46.159 1.134   1.00 24.78  0  60  CYS   C CB  1 
ATOM   4328 S  SG  . CYS   C  1 45  ? 18.915  -46.131 1.357   1.00 28.06  0  60  CYS   C SG  1 
ATOM   4329 N  N   . VAL   C  1 46  ? 23.325  -46.277 -0.753  1.00 27.07  0  61  VAL   C N   1 
ATOM   4330 C  CA  . VAL   C  1 46  ? 24.813  -46.356 -0.611  1.00 28.54  0  61  VAL   C CA  1 
ATOM   4331 C  C   . VAL   C  1 46  ? 25.490  -46.556 -1.973  1.00 30.88  0  61  VAL   C C   1 
ATOM   4332 O  O   . VAL   C  1 46  ? 26.698  -46.848 -1.975  1.00 44.89  0  61  VAL   C O   1 
ATOM   4333 C  CB  . VAL   C  1 46  ? 25.203  -47.453 0.409   1.00 28.86  0  61  VAL   C CB  1 
ATOM   4334 C  CG1 . VAL   C  1 46  ? 24.741  -47.119 1.799   1.00 33.58  0  61  VAL   C CG1 1 
ATOM   4335 C  CG2 . VAL   C  1 46  ? 24.638  -48.811 0.048   1.00 30.40  0  61  VAL   C CG2 1 
ATOM   4336 N  N   . GLY   C  1 47  ? 24.783  -46.362 -3.094  1.00 30.51  0  62  GLY   C N   1 
ATOM   4337 C  CA  . GLY   C  1 47  ? 25.341  -46.554 -4.446  1.00 31.94  0  62  GLY   C CA  1 
ATOM   4338 C  C   . GLY   C  1 47  ? 24.459  -45.907 -5.512  1.00 32.12  0  62  GLY   C C   1 
ATOM   4339 O  O   . GLY   C  1 47  ? 23.501  -45.236 -5.164  1.00 29.52  0  62  GLY   C O   1 
ATOM   4340 N  N   . PRO   C  1 48  ? 24.722  -46.102 -6.829  1.00 32.21  0  63  PRO   C N   1 
ATOM   4341 C  CA  . PRO   C  1 48  ? 25.738  -47.037 -7.302  1.00 30.05  0  63  PRO   C CA  1 
ATOM   4342 C  C   . PRO   C  1 48  ? 27.186  -46.578 -7.189  1.00 29.73  0  63  PRO   C C   1 
ATOM   4343 O  O   . PRO   C  1 48  ? 28.016  -47.421 -7.332  1.00 35.05  0  63  PRO   C O   1 
ATOM   4344 C  CB  . PRO   C  1 48  ? 25.352  -47.202 -8.786  1.00 30.70  0  63  PRO   C CB  1 
ATOM   4345 C  CG  . PRO   C  1 48  ? 24.811  -45.847 -9.163  1.00 30.08  0  63  PRO   C CG  1 
ATOM   4346 C  CD  . PRO   C  1 48  ? 24.003  -45.447 -7.945  1.00 30.50  0  63  PRO   C CD  1 
ATOM   4347 N  N   . ASP   C  1 49  ? 27.454  -45.297 -6.940  1.00 30.44  0  64  ASP   C N   1 
ATOM   4348 C  CA  . ASP   C  1 49  ? 28.848  -44.793 -6.840  1.00 33.11  0  64  ASP   C CA  1 
ATOM   4349 C  C   . ASP   C  1 49  ? 29.450  -45.165 -5.479  1.00 31.90  0  64  ASP   C C   1 
ATOM   4350 O  O   . ASP   C  1 49  ? 28.751  -45.097 -4.470  1.00 28.84  0  64  ASP   C O   1 
ATOM   4351 C  CB  . ASP   C  1 49  ? 28.932  -43.285 -7.065  1.00 34.92  0  64  ASP   C CB  1 
ATOM   4352 C  CG  . ASP   C  1 49  ? 28.676  -42.861 -8.522  1.00 44.59  0  64  ASP   C CG  1 
ATOM   4353 O  OD1 . ASP   C  1 49  ? 28.722  -43.711 -9.500  1.00 36.75  0  64  ASP   C OD1 1 
ATOM   4354 O  OD2 . ASP   C  1 49  ? 28.427  -41.669 -8.693  1.00 47.08  -1 64  ASP   C OD2 1 
ATOM   4355 N  N   . VAL   C  1 50  ? 30.726  -45.512 -5.483  1.00 32.36  0  65  VAL   C N   1 
ATOM   4356 C  CA  . VAL   C  1 50  ? 31.490  -46.011 -4.312  1.00 37.14  0  65  VAL   C CA  1 
ATOM   4357 C  C   . VAL   C  1 50  ? 31.641  -44.877 -3.289  1.00 41.36  0  65  VAL   C C   1 
ATOM   4358 O  O   . VAL   C  1 50  ? 32.093  -43.805 -3.688  1.00 40.57  0  65  VAL   C O   1 
ATOM   4359 C  CB  . VAL   C  1 50  ? 32.864  -46.536 -4.778  1.00 40.01  0  65  VAL   C CB  1 
ATOM   4360 C  CG1 . VAL   C  1 50  ? 33.779  -46.858 -3.596  1.00 42.61  0  65  VAL   C CG1 1 
ATOM   4361 C  CG2 . VAL   C  1 50  ? 32.698  -47.764 -5.686  1.00 38.36  0  65  VAL   C CG2 1 
ATOM   4362 N  N   . LYS   C  1 51  ? 31.330  -45.135 -2.020  1.00 39.99  0  66  LYS   C N   1 
ATOM   4363 C  CA  . LYS   C  1 51  ? 31.460  -44.157 -0.910  1.00 47.47  0  66  LYS   C CA  1 
ATOM   4364 C  C   . LYS   C  1 51  ? 32.563  -44.560 0.085   1.00 43.71  0  66  LYS   C C   1 
ATOM   4365 O  O   . LYS   C  1 51  ? 32.975  -45.720 0.131   1.00 41.86  0  66  LYS   C O   1 
ATOM   4366 C  CB  . LYS   C  1 51  ? 30.091  -44.011 -0.233  1.00 59.67  0  66  LYS   C CB  1 
ATOM   4367 C  CG  . LYS   C  1 51  ? 29.166  -43.023 -0.935  1.00 62.96  0  66  LYS   C CG  1 
ATOM   4368 C  CD  . LYS   C  1 51  ? 27.938  -43.608 -1.585  1.00 71.73  0  66  LYS   C CD  1 
ATOM   4369 C  CE  . LYS   C  1 51  ? 27.317  -42.628 -2.564  1.00 67.78  0  66  LYS   C CE  1 
ATOM   4370 N  NZ  . LYS   C  1 51  ? 26.034  -43.139 -3.087  1.00 68.78  1  66  LYS   C NZ  1 
ATOM   4371 N  N   . ASP   C  1 52  ? 33.051  -43.579 0.836   1.00 45.17  0  67  ASP   C N   1 
ATOM   4372 C  CA  . ASP   C  1 52  ? 34.044  -43.753 1.922   1.00 42.52  0  67  ASP   C CA  1 
ATOM   4373 C  C   . ASP   C  1 52  ? 33.342  -44.409 3.113   1.00 41.56  0  67  ASP   C C   1 
ATOM   4374 O  O   . ASP   C  1 52  ? 32.414  -43.780 3.664   1.00 42.68  0  67  ASP   C O   1 
ATOM   4375 C  CB  . ASP   C  1 52  ? 34.608  -42.403 2.344   1.00 46.13  0  67  ASP   C CB  1 
ATOM   4376 C  CG  . ASP   C  1 52  ? 35.851  -42.508 3.201   1.00 47.47  0  67  ASP   C CG  1 
ATOM   4377 O  OD1 . ASP   C  1 52  ? 36.094  -43.572 3.809   1.00 48.42  0  67  ASP   C OD1 1 
ATOM   4378 O  OD2 . ASP   C  1 52  ? 36.589  -41.537 3.213   1.00 63.66  -1 67  ASP   C OD2 1 
ATOM   4379 N  N   . LEU   C  1 53  ? 33.774  -45.588 3.548   1.00 36.77  0  68  LEU   C N   1 
ATOM   4380 C  CA  . LEU   C  1 53  ? 33.188  -46.247 4.746   1.00 42.46  0  68  LEU   C CA  1 
ATOM   4381 C  C   . LEU   C  1 53  ? 33.300  -45.376 6.003   1.00 37.33  0  68  LEU   C C   1 
ATOM   4382 O  O   . LEU   C  1 53  ? 32.430  -45.517 6.862   1.00 36.39  0  68  LEU   C O   1 
ATOM   4383 C  CB  . LEU   C  1 53  ? 33.890  -47.577 4.969   1.00 50.79  0  68  LEU   C CB  1 
ATOM   4384 C  CG  . LEU   C  1 53  ? 33.356  -48.664 4.053   1.00 56.90  0  68  LEU   C CG  1 
ATOM   4385 C  CD1 . LEU   C  1 53  ? 34.357  -49.797 3.933   1.00 65.05  0  68  LEU   C CD1 1 
ATOM   4386 C  CD2 . LEU   C  1 53  ? 32.024  -49.170 4.567   1.00 60.18  0  68  LEU   C CD2 1 
ATOM   4387 N  N   . ALA   C  1 54  ? 34.327  -44.533 6.094   1.00 35.10  0  69  ALA   C N   1 
ATOM   4388 C  CA  . ALA   C  1 54  ? 34.601  -43.676 7.272   1.00 35.68  0  69  ALA   C CA  1 
ATOM   4389 C  C   . ALA   C  1 54  ? 33.450  -42.680 7.466   1.00 34.06  0  69  ALA   C C   1 
ATOM   4390 O  O   . ALA   C  1 54  ? 33.230  -42.291 8.595   1.00 36.79  0  69  ALA   C O   1 
ATOM   4391 C  CB  . ALA   C  1 54  ? 35.917  -42.945 7.123   1.00 31.70  0  69  ALA   C CB  1 
ATOM   4392 N  N   . ALA   C  1 55  ? 32.760  -42.295 6.397   1.00 32.29  0  70  ALA   C N   1 
ATOM   4393 C  CA  . ALA   C  1 55  ? 31.646  -41.311 6.445   1.00 33.31  0  70  ALA   C CA  1 
ATOM   4394 C  C   . ALA   C  1 55  ? 30.315  -41.991 6.806   1.00 29.28  0  70  ALA   C C   1 
ATOM   4395 O  O   . ALA   C  1 55  ? 29.308  -41.281 6.838   1.00 33.30  0  70  ALA   C O   1 
ATOM   4396 C  CB  . ALA   C  1 55  ? 31.571  -40.561 5.134   1.00 31.27  0  70  ALA   C CB  1 
ATOM   4397 N  N   . LEU   C  1 56  ? 30.279  -43.302 7.052   1.00 29.66  0  71  LEU   C N   1 
ATOM   4398 C  CA  . LEU   C  1 56  ? 29.028  -44.048 7.345   1.00 28.95  0  71  LEU   C CA  1 
ATOM   4399 C  C   . LEU   C  1 56  ? 29.064  -44.635 8.765   1.00 31.55  0  71  LEU   C C   1 
ATOM   4400 O  O   . LEU   C  1 56  ? 30.088  -45.203 9.144   1.00 29.81  0  71  LEU   C O   1 
ATOM   4401 C  CB  . LEU   C  1 56  ? 28.888  -45.159 6.304   1.00 29.76  0  71  LEU   C CB  1 
ATOM   4402 C  CG  . LEU   C  1 56  ? 27.686  -46.086 6.431   1.00 28.80  0  71  LEU   C CG  1 
ATOM   4403 C  CD1 . LEU   C  1 56  ? 26.366  -45.338 6.345   1.00 30.67  0  71  LEU   C CD1 1 
ATOM   4404 C  CD2 . LEU   C  1 56  ? 27.719  -47.143 5.334   1.00 33.47  0  71  LEU   C CD2 1 
ATOM   4405 N  N   . ARG   C  1 57  ? 27.941  -44.560 9.476   1.00 28.81  0  72  ARG   C N   1 
ATOM   4406 C  CA  . ARG   C  1 57  ? 27.717  -45.337 10.710  1.00 29.09  0  72  ARG   C CA  1 
ATOM   4407 C  C   . ARG   C  1 57  ? 26.297  -45.883 10.742  1.00 28.26  0  72  ARG   C C   1 
ATOM   4408 O  O   . ARG   C  1 57  ? 25.390  -45.336 10.061  1.00 27.50  0  72  ARG   C O   1 
ATOM   4409 C  CB  . ARG   C  1 57  ? 27.898  -44.467 11.957  1.00 32.73  0  72  ARG   C CB  1 
ATOM   4410 C  CG  . ARG   C  1 57  ? 29.261  -43.815 12.086  1.00 35.06  0  72  ARG   C CG  1 
ATOM   4411 C  CD  . ARG   C  1 57  ? 30.283  -44.743 12.653  1.00 36.01  0  72  ARG   C CD  1 
ATOM   4412 N  NE  . ARG   C  1 57  ? 31.399  -43.926 13.084  1.00 35.47  0  72  ARG   C NE  1 
ATOM   4413 C  CZ  . ARG   C  1 57  ? 32.423  -43.543 12.334  1.00 42.75  0  72  ARG   C CZ  1 
ATOM   4414 N  NH1 . ARG   C  1 57  ? 32.510  -43.876 11.052  1.00 47.73  1  72  ARG   C NH1 1 
ATOM   4415 N  NH2 . ARG   C  1 57  ? 33.363  -42.790 12.881  1.00 40.28  0  72  ARG   C NH2 1 
ATOM   4416 N  N   . VAL   C  1 58  ? 26.119  -46.874 11.601  1.00 26.78  0  73  VAL   C N   1 
ATOM   4417 C  CA  . VAL   C  1 58  ? 24.823  -47.536 11.871  1.00 27.62  0  73  VAL   C CA  1 
ATOM   4418 C  C   . VAL   C  1 58  ? 24.432  -47.221 13.313  1.00 26.67  0  73  VAL   C C   1 
ATOM   4419 O  O   . VAL   C  1 58  ? 25.285  -47.346 14.204  1.00 28.60  0  73  VAL   C O   1 
ATOM   4420 C  CB  . VAL   C  1 58  ? 24.917  -49.050 11.618  1.00 29.27  0  73  VAL   C CB  1 
ATOM   4421 C  CG1 . VAL   C  1 58  ? 23.716  -49.798 12.166  1.00 30.67  0  73  VAL   C CG1 1 
ATOM   4422 C  CG2 . VAL   C  1 58  ? 25.117  -49.363 10.147  1.00 30.78  0  73  VAL   C CG2 1 
ATOM   4423 N  N   . GLN   C  1 59  ? 23.153  -46.926 13.508  1.00 27.51  0  74  GLN   C N   1 
ATOM   4424 C  CA  . GLN   C  1 59  ? 22.524  -46.723 14.824  1.00 30.13  0  74  GLN   C CA  1 
ATOM   4425 C  C   . GLN   C  1 59  ? 21.424  -47.770 14.942  1.00 30.97  0  74  GLN   C C   1 
ATOM   4426 O  O   . GLN   C  1 59  ? 20.511  -47.736 14.089  1.00 30.62  0  74  GLN   C O   1 
ATOM   4427 C  CB  . GLN   C  1 59  ? 21.970  -45.285 14.902  1.00 28.14  0  74  GLN   C CB  1 
ATOM   4428 C  CG  . GLN   C  1 59  ? 21.073  -45.007 16.110  1.00 28.82  0  74  GLN   C CG  1 
ATOM   4429 C  CD  . GLN   C  1 59  ? 21.830  -45.208 17.407  1.00 30.30  0  74  GLN   C CD  1 
ATOM   4430 O  OE1 . GLN   C  1 59  ? 22.939  -44.691 17.593  1.00 28.87  0  74  GLN   C OE1 1 
ATOM   4431 N  NE2 . GLN   C  1 59  ? 21.253  -46.008 18.295  1.00 31.61  0  74  GLN   C NE2 1 
ATOM   4432 N  N   . LEU   C  1 60  ? 21.471  -48.632 15.962  1.00 29.06  0  75  LEU   C N   1 
ATOM   4433 C  CA  . LEU   C  1 60  ? 20.424  -49.663 16.200  1.00 32.80  0  75  LEU   C CA  1 
ATOM   4434 C  C   . LEU   C  1 60  ? 19.178  -49.013 16.772  1.00 30.57  0  75  LEU   C C   1 
ATOM   4435 O  O   . LEU   C  1 60  ? 19.184  -47.761 16.943  1.00 35.61  0  75  LEU   C O   1 
ATOM   4436 C  CB  . LEU   C  1 60  ? 20.980  -50.733 17.136  1.00 38.85  0  75  LEU   C CB  1 
ATOM   4437 C  CG  . LEU   C  1 60  ? 22.241  -51.430 16.631  1.00 41.45  0  75  LEU   C CG  1 
ATOM   4438 C  CD1 . LEU   C  1 60  ? 22.737  -52.423 17.677  1.00 45.23  0  75  LEU   C CD1 1 
ATOM   4439 C  CD2 . LEU   C  1 60  ? 22.009  -52.102 15.278  1.00 38.28  0  75  LEU   C CD2 1 
ATOM   4440 N  N   . ARG   C  1 61  ? 18.163  -49.814 17.086  1.00 33.54  0  76  ARG   C N   1 
ATOM   4441 C  CA  . ARG   C  1 61  ? 16.825  -49.269 17.386  1.00 34.56  0  76  ARG   C CA  1 
ATOM   4442 C  C   . ARG   C  1 61  ? 16.903  -48.132 18.417  1.00 34.50  0  76  ARG   C C   1 
ATOM   4443 O  O   . ARG   C  1 61  ? 17.459  -48.330 19.468  1.00 39.78  0  76  ARG   C O   1 
ATOM   4444 C  CB  . ARG   C  1 61  ? 15.828  -50.297 17.889  1.00 34.49  0  76  ARG   C CB  1 
ATOM   4445 C  CG  . ARG   C  1 61  ? 14.414  -49.811 17.578  1.00 35.06  0  76  ARG   C CG  1 
ATOM   4446 C  CD  . ARG   C  1 61  ? 13.493  -50.465 18.538  1.00 35.99  0  76  ARG   C CD  1 
ATOM   4447 N  NE  . ARG   C  1 61  ? 12.103  -50.120 18.369  1.00 34.61  0  76  ARG   C NE  1 
ATOM   4448 C  CZ  . ARG   C  1 61  ? 11.528  -49.055 18.876  1.00 34.16  0  76  ARG   C CZ  1 
ATOM   4449 N  NH1 . ARG   C  1 61  ? 12.248  -48.134 19.504  1.00 39.84  1  76  ARG   C NH1 1 
ATOM   4450 N  NH2 . ARG   C  1 61  ? 10.221  -48.929 18.776  1.00 31.27  0  76  ARG   C NH2 1 
ATOM   4451 N  N   . GLU   C  1 62  ? 16.370  -46.979 18.045  1.00 35.94  0  77  GLU   C N   1 
ATOM   4452 C  CA  . GLU   C  1 62  ? 16.209  -45.759 18.860  1.00 35.34  0  77  GLU   C CA  1 
ATOM   4453 C  C   . GLU   C  1 62  ? 14.740  -45.375 18.799  1.00 31.74  0  77  GLU   C C   1 
ATOM   4454 O  O   . GLU   C  1 62  ? 14.225  -45.364 17.689  1.00 33.93  0  77  GLU   C O   1 
ATOM   4455 C  CB  . GLU   C  1 62  ? 16.972  -44.603 18.218  1.00 34.26  0  77  GLU   C CB  1 
ATOM   4456 C  CG  . GLU   C  1 62  ? 18.356  -44.473 18.734  1.00 30.93  0  77  GLU   C CG  1 
ATOM   4457 C  CD  . GLU   C  1 62  ? 19.057  -43.201 18.314  1.00 31.21  0  77  GLU   C CD  1 
ATOM   4458 O  OE1 . GLU   C  1 62  ? 19.867  -42.741 19.071  1.00 36.85  0  77  GLU   C OE1 1 
ATOM   4459 O  OE2 . GLU   C  1 62  ? 18.807  -42.670 17.223  1.00 35.66  -1 77  GLU   C OE2 1 
ATOM   4460 N  N   . GLN   C  1 63  ? 14.121  -45.040 19.921  1.00 26.60  0  78  GLN   C N   1 
ATOM   4461 C  CA  . GLN   C  1 63  ? 12.743  -44.491 19.928  1.00 31.94  0  78  GLN   C CA  1 
ATOM   4462 C  C   . GLN   C  1 63  ? 12.751  -43.097 19.265  1.00 33.13  0  78  GLN   C C   1 
ATOM   4463 O  O   . GLN   C  1 63  ? 11.831  -42.806 18.501  1.00 32.57  0  78  GLN   C O   1 
ATOM   4464 C  CB  . GLN   C  1 63  ? 12.182  -44.460 21.356  1.00 29.92  0  78  GLN   C CB  1 
ATOM   4465 C  CG  . GLN   C  1 63  ? 10.671  -44.258 21.424  1.00 32.61  0  78  GLN   C CG  1 
ATOM   4466 C  CD  . GLN   C  1 63  ? 9.891   -45.273 20.626  1.00 36.15  0  78  GLN   C CD  1 
ATOM   4467 O  OE1 . GLN   C  1 63  ? 10.309  -46.420 20.504  1.00 31.22  0  78  GLN   C OE1 1 
ATOM   4468 N  NE2 . GLN   C  1 63  ? 8.777   -44.846 20.033  1.00 40.24  0  78  GLN   C NE2 1 
ATOM   4469 N  N   . HIS   C  1 64  ? 13.762  -42.278 19.565  1.00 30.89  0  79  HIS   C N   1 
ATOM   4470 C  CA  . HIS   C  1 64  ? 13.905  -40.884 19.063  1.00 31.58  0  79  HIS   C CA  1 
ATOM   4471 C  C   . HIS   C  1 64  ? 15.300  -40.729 18.473  1.00 28.92  0  79  HIS   C C   1 
ATOM   4472 O  O   . HIS   C  1 64  ? 16.279  -40.995 19.218  1.00 32.83  0  79  HIS   C O   1 
ATOM   4473 C  CB  . HIS   C  1 64  ? 13.615  -39.888 20.188  1.00 32.40  0  79  HIS   C CB  1 
ATOM   4474 C  CG  . HIS   C  1 64  ? 12.241  -40.004 20.760  1.00 29.91  0  79  HIS   C CG  1 
ATOM   4475 N  ND1 . HIS   C  1 64  ? 11.999  -40.674 21.942  1.00 34.13  0  79  HIS   C ND1 1 
ATOM   4476 C  CD2 . HIS   C  1 64  ? 11.053  -39.506 20.347  1.00 30.81  0  79  HIS   C CD2 1 
ATOM   4477 C  CE1 . HIS   C  1 64  ? 10.712  -40.634 22.226  1.00 30.73  0  79  HIS   C CE1 1 
ATOM   4478 N  NE2 . HIS   C  1 64  ? 10.100  -39.881 21.270  1.00 33.15  0  79  HIS   C NE2 1 
ATOM   4479 N  N   . LEU   C  1 65  ? 15.402  -40.353 17.195  1.00 27.07  0  80  LEU   C N   1 
ATOM   4480 C  CA  . LEU   C  1 65  ? 16.733  -40.160 16.536  1.00 28.20  0  80  LEU   C CA  1 
ATOM   4481 C  C   . LEU   C  1 65  ? 17.552  -39.146 17.315  1.00 26.70  0  80  LEU   C C   1 
ATOM   4482 O  O   . LEU   C  1 65  ? 16.974  -38.139 17.731  1.00 23.41  0  80  LEU   C O   1 
ATOM   4483 C  CB  . LEU   C  1 65  ? 16.638  -39.618 15.102  1.00 28.38  0  80  LEU   C CB  1 
ATOM   4484 C  CG  . LEU   C  1 65  ? 16.193  -40.557 13.992  1.00 31.85  0  80  LEU   C CG  1 
ATOM   4485 C  CD1 . LEU   C  1 65  ? 16.199  -39.797 12.674  1.00 33.69  0  80  LEU   C CD1 1 
ATOM   4486 C  CD2 . LEU   C  1 65  ? 17.063  -41.793 13.913  1.00 29.66  0  80  LEU   C CD2 1 
ATOM   4487 N  N   . TYR   C  1 66  ? 18.849  -39.410 17.455  1.00 26.47  0  81  TYR   C N   1 
ATOM   4488 C  CA  . TYR   C  1 66  ? 19.899  -38.440 17.885  1.00 30.71  0  81  TYR   C CA  1 
ATOM   4489 C  C   . TYR   C  1 66  ? 20.029  -38.355 19.424  1.00 31.10  0  81  TYR   C C   1 
ATOM   4490 O  O   . TYR   C  1 66  ? 21.107  -37.980 19.895  1.00 34.09  0  81  TYR   C O   1 
ATOM   4491 C  CB  . TYR   C  1 66  ? 19.676  -37.053 17.271  1.00 26.55  0  81  TYR   C CB  1 
ATOM   4492 C  CG  . TYR   C  1 66  ? 19.522  -37.044 15.765  1.00 26.81  0  81  TYR   C CG  1 
ATOM   4493 C  CD1 . TYR   C  1 66  ? 20.532  -37.503 14.935  1.00 26.18  0  81  TYR   C CD1 1 
ATOM   4494 C  CD2 . TYR   C  1 66  ? 18.360  -36.614 15.168  1.00 27.08  0  81  TYR   C CD2 1 
ATOM   4495 C  CE1 . TYR   C  1 66  ? 20.389  -37.533 13.559  1.00 29.93  0  81  TYR   C CE1 1 
ATOM   4496 C  CE2 . TYR   C  1 66  ? 18.192  -36.645 13.787  1.00 28.59  0  81  TYR   C CE2 1 
ATOM   4497 C  CZ  . TYR   C  1 66  ? 19.222  -37.081 12.972  1.00 30.40  0  81  TYR   C CZ  1 
ATOM   4498 O  OH  . TYR   C  1 66  ? 19.080  -37.135 11.606  1.00 25.92  0  81  TYR   C OH  1 
ATOM   4499 N  N   A TYR   C  1 67  ? 18.974  -38.708 20.177  0.50 33.86  0  82  TYR   C N   1 
ATOM   4500 N  N   B TYR   C  1 67  ? 18.996  -38.728 20.179  0.50 33.31  0  82  TYR   C N   1 
ATOM   4501 C  CA  A TYR   C  1 67  ? 18.870  -38.513 21.651  0.50 36.98  0  82  TYR   C CA  1 
ATOM   4502 C  CA  B TYR   C  1 67  ? 18.917  -38.428 21.632  0.50 36.08  0  82  TYR   C CA  1 
ATOM   4503 C  C   A TYR   C  1 67  ? 19.921  -39.349 22.385  0.50 37.70  0  82  TYR   C C   1 
ATOM   4504 C  C   B TYR   C  1 67  ? 19.871  -39.351 22.411  0.50 37.30  0  82  TYR   C C   1 
ATOM   4505 O  O   A TYR   C  1 67  ? 20.660  -38.786 23.216  0.50 41.57  0  82  TYR   C O   1 
ATOM   4506 O  O   B TYR   C  1 67  ? 20.558  -38.805 23.287  0.50 41.66  0  82  TYR   C O   1 
ATOM   4507 C  CB  A TYR   C  1 67  ? 17.482  -38.887 22.184  0.50 38.60  0  82  TYR   C CB  1 
ATOM   4508 C  CB  B TYR   C  1 67  ? 17.443  -38.346 22.031  0.50 37.37  0  82  TYR   C CB  1 
ATOM   4509 C  CG  A TYR   C  1 67  ? 17.329  -38.647 23.669  0.50 39.67  0  82  TYR   C CG  1 
ATOM   4510 C  CG  B TYR   C  1 67  ? 16.786  -37.079 21.532  0.50 34.68  0  82  TYR   C CG  1 
ATOM   4511 C  CD1 A TYR   C  1 67  ? 17.699  -37.432 24.224  0.50 39.29  0  82  TYR   C CD1 1 
ATOM   4512 C  CD1 B TYR   C  1 67  ? 17.038  -35.857 22.132  0.50 36.99  0  82  TYR   C CD1 1 
ATOM   4513 C  CD2 A TYR   C  1 67  ? 16.828  -39.618 24.524  0.50 40.26  0  82  TYR   C CD2 1 
ATOM   4514 C  CD2 B TYR   C  1 67  ? 15.953  -37.090 20.433  0.50 35.45  0  82  TYR   C CD2 1 
ATOM   4515 C  CE1 A TYR   C  1 67  ? 17.594  -37.185 25.582  0.50 36.37  0  82  TYR   C CE1 1 
ATOM   4516 C  CE1 B TYR   C  1 67  ? 16.445  -34.689 21.676  0.50 37.64  0  82  TYR   C CE1 1 
ATOM   4517 C  CE2 A TYR   C  1 67  ? 16.719  -39.388 25.889  0.50 40.86  0  82  TYR   C CE2 1 
ATOM   4518 C  CE2 B TYR   C  1 67  ? 15.349  -35.939 19.962  0.50 33.84  0  82  TYR   C CE2 1 
ATOM   4519 C  CZ  A TYR   C  1 67  ? 17.092  -38.160 26.415  0.50 36.80  0  82  TYR   C CZ  1 
ATOM   4520 C  CZ  B TYR   C  1 67  ? 15.598  -34.731 20.583  0.50 35.92  0  82  TYR   C CZ  1 
ATOM   4521 O  OH  A TYR   C  1 67  ? 16.977  -37.883 27.739  0.50 35.99  0  82  TYR   C OH  1 
ATOM   4522 O  OH  B TYR   C  1 67  ? 15.006  -33.595 20.116  0.50 37.66  0  82  TYR   C OH  1 
ATOM   4523 N  N   . GLN   C  1 68  ? 20.004  -40.636 22.054  1.00 37.14  0  83  GLN   C N   1 
ATOM   4524 C  CA  . GLN   C  1 68  ? 20.882  -41.586 22.786  1.00 45.01  0  83  GLN   C CA  1 
ATOM   4525 C  C   . GLN   C  1 68  ? 21.771  -42.331 21.811  1.00 41.62  0  83  GLN   C C   1 
ATOM   4526 O  O   . GLN   C  1 68  ? 21.850  -43.551 21.951  1.00 41.70  0  83  GLN   C O   1 
ATOM   4527 C  CB  . GLN   C  1 68  ? 20.060  -42.606 23.577  1.00 51.33  0  83  GLN   C CB  1 
ATOM   4528 C  CG  . GLN   C  1 68  ? 19.193  -42.024 24.676  1.00 60.49  0  83  GLN   C CG  1 
ATOM   4529 C  CD  . GLN   C  1 68  ? 19.981  -41.770 25.936  1.00 63.69  0  83  GLN   C CD  1 
ATOM   4530 O  OE1 . GLN   C  1 68  ? 19.973  -42.561 26.878  1.00 60.97  0  83  GLN   C OE1 1 
ATOM   4531 N  NE2 . GLN   C  1 68  ? 20.707  -40.668 25.926  1.00 64.48  0  83  GLN   C NE2 1 
ATOM   4532 N  N   . ASP   C  1 69  ? 22.445  -41.632 20.889  1.00 38.50  0  84  ASP   C N   1 
ATOM   4533 C  CA  . ASP   C  1 69  ? 23.166  -42.340 19.800  1.00 37.59  0  84  ASP   C CA  1 
ATOM   4534 C  C   . ASP   C  1 69  ? 24.284  -43.203 20.406  1.00 37.75  0  84  ASP   C C   1 
ATOM   4535 O  O   . ASP   C  1 69  ? 24.969  -42.736 21.318  1.00 33.37  0  84  ASP   C O   1 
ATOM   4536 C  CB  . ASP   C  1 69  ? 23.719  -41.372 18.761  1.00 37.17  0  84  ASP   C CB  1 
ATOM   4537 C  CG  . ASP   C  1 69  ? 22.694  -40.833 17.781  1.00 34.06  0  84  ASP   C CG  1 
ATOM   4538 O  OD1 . ASP   C  1 69  ? 21.548  -41.285 17.788  1.00 31.89  0  84  ASP   C OD1 1 
ATOM   4539 O  OD2 . ASP   C  1 69  ? 23.058  -39.935 17.025  1.00 33.36  -1 84  ASP   C OD2 1 
ATOM   4540 N  N   . GLN   C  1 70  ? 24.437  -44.426 19.910  1.00 37.19  0  85  GLN   C N   1 
ATOM   4541 C  CA  . GLN   C  1 70  ? 25.696  -45.216 20.040  1.00 39.62  0  85  GLN   C CA  1 
ATOM   4542 C  C   . GLN   C  1 70  ? 26.065  -45.733 18.644  1.00 38.01  0  85  GLN   C C   1 
ATOM   4543 O  O   . GLN   C  1 70  ? 25.508  -46.780 18.209  1.00 29.61  0  85  GLN   C O   1 
ATOM   4544 C  CB  . GLN   C  1 70  ? 25.507  -46.343 21.043  1.00 40.97  0  85  GLN   C CB  1 
ATOM   4545 C  CG  . GLN   C  1 70  ? 24.801  -45.889 22.310  1.00 51.43  0  85  GLN   C CG  1 
ATOM   4546 C  CD  . GLN   C  1 70  ? 24.709  -47.014 23.318  1.00 56.40  0  85  GLN   C CD  1 
ATOM   4547 O  OE1 . GLN   C  1 70  ? 25.614  -47.213 24.124  1.00 61.83  0  85  GLN   C OE1 1 
ATOM   4548 N  NE2 . GLN   C  1 70  ? 23.613  -47.764 23.283  1.00 55.23  0  85  GLN   C NE2 1 
ATOM   4549 N  N   . LEU   C  1 71  ? 26.897  -44.968 17.947  1.00 33.18  0  86  LEU   C N   1 
ATOM   4550 C  CA  . LEU   C  1 71  ? 27.119  -45.146 16.505  1.00 35.71  0  86  LEU   C CA  1 
ATOM   4551 C  C   . LEU   C  1 71  ? 28.080  -46.312 16.293  1.00 39.64  0  86  LEU   C C   1 
ATOM   4552 O  O   . LEU   C  1 71  ? 29.066  -46.392 17.011  1.00 40.58  0  86  LEU   C O   1 
ATOM   4553 C  CB  . LEU   C  1 71  ? 27.612  -43.829 15.913  1.00 32.62  0  86  LEU   C CB  1 
ATOM   4554 C  CG  . LEU   C  1 71  ? 26.598  -42.674 15.964  1.00 36.42  0  86  LEU   C CG  1 
ATOM   4555 C  CD1 . LEU   C  1 71  ? 27.095  -41.491 15.150  1.00 35.41  0  86  LEU   C CD1 1 
ATOM   4556 C  CD2 . LEU   C  1 71  ? 25.201  -43.077 15.495  1.00 35.72  0  86  LEU   C CD2 1 
ATOM   4557 N  N   . LEU   C  1 72  ? 27.759  -47.188 15.339  1.00 39.08  0  87  LEU   C N   1 
ATOM   4558 C  CA  . LEU   C  1 72  ? 28.557  -48.404 15.010  1.00 33.40  0  87  LEU   C CA  1 
ATOM   4559 C  C   . LEU   C  1 72  ? 29.249  -48.209 13.671  1.00 31.39  0  87  LEU   C C   1 
ATOM   4560 O  O   . LEU   C  1 72  ? 28.618  -47.850 12.668  1.00 30.23  0  87  LEU   C O   1 
ATOM   4561 C  CB  . LEU   C  1 72  ? 27.650  -49.637 15.012  1.00 29.90  0  87  LEU   C CB  1 
ATOM   4562 C  CG  . LEU   C  1 72  ? 26.835  -49.855 16.287  1.00 31.30  0  87  LEU   C CG  1 
ATOM   4563 C  CD1 . LEU   C  1 72  ? 25.912  -51.065 16.147  1.00 34.49  0  87  LEU   C CD1 1 
ATOM   4564 C  CD2 . LEU   C  1 72  ? 27.726  -50.035 17.505  1.00 31.94  0  87  LEU   C CD2 1 
ATOM   4565 N  N   . PRO   C  1 73  ? 30.579  -48.443 13.593  1.00 32.73  0  88  PRO   C N   1 
ATOM   4566 C  CA  . PRO   C  1 73  ? 31.274  -48.384 12.309  1.00 33.42  0  88  PRO   C CA  1 
ATOM   4567 C  C   . PRO   C  1 73  ? 30.914  -49.623 11.460  1.00 33.85  0  88  PRO   C C   1 
ATOM   4568 O  O   . PRO   C  1 73  ? 30.439  -50.648 11.983  1.00 31.86  0  88  PRO   C O   1 
ATOM   4569 C  CB  . PRO   C  1 73  ? 32.755  -48.275 12.695  1.00 36.33  0  88  PRO   C CB  1 
ATOM   4570 C  CG  . PRO   C  1 73  ? 32.833  -48.947 14.066  1.00 37.57  0  88  PRO   C CG  1 
ATOM   4571 C  CD  . PRO   C  1 73  ? 31.473  -48.789 14.711  1.00 36.83  0  88  PRO   C CD  1 
ATOM   4572 N  N   . VAL   C  1 74  ? 31.013  -49.460 10.142  1.00 34.45  0  89  VAL   C N   1 
ATOM   4573 C  CA  . VAL   C  1 74  ? 30.719  -50.499 9.106   1.00 34.00  0  89  VAL   C CA  1 
ATOM   4574 C  C   . VAL   C  1 74  ? 32.062  -50.935 8.520   1.00 31.55  0  89  VAL   C C   1 
ATOM   4575 O  O   . VAL   C  1 74  ? 32.840  -50.047 8.206   1.00 29.77  0  89  VAL   C O   1 
ATOM   4576 C  CB  . VAL   C  1 74  ? 29.793  -49.930 8.014   1.00 35.01  0  89  VAL   C CB  1 
ATOM   4577 C  CG1 . VAL   C  1 74  ? 29.650  -50.886 6.830   1.00 36.32  0  89  VAL   C CG1 1 
ATOM   4578 C  CG2 . VAL   C  1 74  ? 28.426  -49.566 8.583   1.00 34.39  0  89  VAL   C CG2 1 
ATOM   4579 N  N   . SER   C  1 75  ? 32.303  -52.229 8.344   1.00 33.97  0  90  SER   C N   1 
ATOM   4580 C  CA  . SER   C  1 75  ? 33.565  -52.757 7.761   1.00 37.04  0  90  SER   C CA  1 
ATOM   4581 C  C   . SER   C  1 75  ? 33.423  -52.922 6.250   1.00 37.35  0  90  SER   C C   1 
ATOM   4582 O  O   . SER   C  1 75  ? 34.390  -52.709 5.591   1.00 40.83  0  90  SER   C O   1 
ATOM   4583 C  CB  . SER   C  1 75  ? 33.971  -54.055 8.383   1.00 42.40  0  90  SER   C CB  1 
ATOM   4584 O  OG  . SER   C  1 75  ? 32.901  -54.978 8.371   1.00 51.69  0  90  SER   C OG  1 
ATOM   4585 N  N   . ARG   C  1 76  ? 32.237  -53.229 5.723   1.00 36.97  0  91  ARG   C N   1 
ATOM   4586 C  CA  . ARG   C  1 76  ? 32.058  -53.426 4.270   1.00 37.12  0  91  ARG   C CA  1 
ATOM   4587 C  C   . ARG   C  1 76  ? 30.661  -53.014 3.828   1.00 30.20  0  91  ARG   C C   1 
ATOM   4588 O  O   . ARG   C  1 76  ? 29.702  -53.376 4.505   1.00 29.98  0  91  ARG   C O   1 
ATOM   4589 C  CB  . ARG   C  1 76  ? 32.292  -54.899 3.942   1.00 40.95  0  91  ARG   C CB  1 
ATOM   4590 C  CG  . ARG   C  1 76  ? 32.273  -55.228 2.466   1.00 43.54  0  91  ARG   C CG  1 
ATOM   4591 C  CD  . ARG   C  1 76  ? 32.641  -56.684 2.266   1.00 46.74  0  91  ARG   C CD  1 
ATOM   4592 N  NE  . ARG   C  1 76  ? 32.598  -57.008 0.839   1.00 56.03  0  91  ARG   C NE  1 
ATOM   4593 C  CZ  . ARG   C  1 76  ? 32.691  -58.227 0.316   1.00 55.41  0  91  ARG   C CZ  1 
ATOM   4594 N  NH1 . ARG   C  1 76  ? 32.813  -59.289 1.098   1.00 52.88  1  91  ARG   C NH1 1 
ATOM   4595 N  NH2 . ARG   C  1 76  ? 32.646  -58.371 -0.997  1.00 57.66  0  91  ARG   C NH2 1 
ATOM   4596 N  N   . ILE   C  1 77  ? 30.585  -52.393 2.659   1.00 29.31  0  92  ILE   C N   1 
ATOM   4597 C  CA  . ILE   C  1 77  ? 29.322  -52.143 1.904   1.00 30.11  0  92  ILE   C CA  1 
ATOM   4598 C  C   . ILE   C  1 77  ? 29.296  -53.117 0.718   1.00 29.60  0  92  ILE   C C   1 
ATOM   4599 O  O   . ILE   C  1 77  ? 30.227  -53.044 -0.120  1.00 28.79  0  92  ILE   C O   1 
ATOM   4600 C  CB  . ILE   C  1 77  ? 29.277  -50.681 1.435   1.00 28.11  0  92  ILE   C CB  1 
ATOM   4601 C  CG1 . ILE   C  1 77  ? 29.259  -49.686 2.601   1.00 31.12  0  92  ILE   C CG1 1 
ATOM   4602 C  CG2 . ILE   C  1 77  ? 28.085  -50.484 0.513   1.00 32.66  0  92  ILE   C CG2 1 
ATOM   4603 C  CD1 . ILE   C  1 77  ? 29.612  -48.274 2.200   1.00 33.31  0  92  ILE   C CD1 1 
ATOM   4604 N  N   . ILE   C  1 78  ? 28.277  -53.970 0.634   1.00 28.29  0  93  ILE   C N   1 
ATOM   4605 C  CA  . ILE   C  1 78  ? 28.093  -54.904 -0.518  1.00 29.31  0  93  ILE   C CA  1 
ATOM   4606 C  C   . ILE   C  1 78  ? 26.823  -54.495 -1.244  1.00 26.64  0  93  ILE   C C   1 
ATOM   4607 O  O   . ILE   C  1 78  ? 25.709  -54.751 -0.742  1.00 28.47  0  93  ILE   C O   1 
ATOM   4608 C  CB  . ILE   C  1 78  ? 28.042  -56.395 -0.123  1.00 32.94  0  93  ILE   C CB  1 
ATOM   4609 C  CG1 . ILE   C  1 78  ? 29.062  -56.743 0.971   1.00 37.61  0  93  ILE   C CG1 1 
ATOM   4610 C  CG2 . ILE   C  1 78  ? 28.190  -57.229 -1.392  1.00 32.01  0  93  ILE   C CG2 1 
ATOM   4611 C  CD1 . ILE   C  1 78  ? 29.152  -58.229 1.307   1.00 40.98  0  93  ILE   C CD1 1 
ATOM   4612 N  N   . VAL   C  1 79  ? 26.981  -53.850 -2.397  1.00 28.80  0  94  VAL   C N   1 
ATOM   4613 C  CA  . VAL   C  1 79  ? 25.831  -53.429 -3.237  1.00 27.80  0  94  VAL   C CA  1 
ATOM   4614 C  C   . VAL   C  1 79  ? 25.644  -54.488 -4.307  1.00 26.63  0  94  VAL   C C   1 
ATOM   4615 O  O   . VAL   C  1 79  ? 26.614  -54.830 -4.967  1.00 31.66  0  94  VAL   C O   1 
ATOM   4616 C  CB  . VAL   C  1 79  ? 26.085  -52.026 -3.823  1.00 29.60  0  94  VAL   C CB  1 
ATOM   4617 C  CG1 . VAL   C  1 79  ? 25.051  -51.646 -4.857  1.00 28.28  0  94  VAL   C CG1 1 
ATOM   4618 C  CG2 . VAL   C  1 79  ? 26.187  -50.995 -2.720  1.00 28.39  0  94  VAL   C CG2 1 
ATOM   4619 N  N   . HIS   C  1 80  ? 24.426  -54.955 -4.485  1.00 28.52  0  95  HIS   C N   1 
ATOM   4620 C  CA  . HIS   C  1 80  ? 24.120  -55.926 -5.562  1.00 29.70  0  95  HIS   C CA  1 
ATOM   4621 C  C   . HIS   C  1 80  ? 24.749  -55.432 -6.871  1.00 29.73  0  95  HIS   C C   1 
ATOM   4622 O  O   . HIS   C  1 80  ? 24.505  -54.302 -7.299  1.00 27.04  0  95  HIS   C O   1 
ATOM   4623 C  CB  . HIS   C  1 80  ? 22.623  -56.113 -5.725  1.00 29.17  0  95  HIS   C CB  1 
ATOM   4624 C  CG  . HIS   C  1 80  ? 22.306  -57.408 -6.386  1.00 31.96  0  95  HIS   C CG  1 
ATOM   4625 N  ND1 . HIS   C  1 80  ? 22.636  -57.657 -7.706  1.00 29.29  0  95  HIS   C ND1 1 
ATOM   4626 C  CD2 . HIS   C  1 80  ? 21.725  -58.533 -5.901  1.00 32.25  0  95  HIS   C CD2 1 
ATOM   4627 C  CE1 . HIS   C  1 80  ? 22.246  -58.869 -8.017  1.00 30.42  0  95  HIS   C CE1 1 
ATOM   4628 N  NE2 . HIS   C  1 80  ? 21.706  -59.442 -6.940  1.00 32.41  0  95  HIS   C NE2 1 
ATOM   4629 N  N   . PRO   C  1 81  ? 25.594  -56.234 -7.543  1.00 29.83  0  96  PRO   C N   1 
ATOM   4630 C  CA  . PRO   C  1 81  ? 26.249  -55.788 -8.771  1.00 30.85  0  96  PRO   C CA  1 
ATOM   4631 C  C   . PRO   C  1 81  ? 25.352  -55.493 -9.984  1.00 25.92  0  96  PRO   C C   1 
ATOM   4632 O  O   . PRO   C  1 81  ? 25.790  -54.808 -10.838 1.00 27.87  0  96  PRO   C O   1 
ATOM   4633 C  CB  . PRO   C  1 81  ? 27.241  -56.924 -9.079  1.00 32.42  0  96  PRO   C CB  1 
ATOM   4634 C  CG  . PRO   C  1 81  ? 26.610  -58.132 -8.434  1.00 33.62  0  96  PRO   C CG  1 
ATOM   4635 C  CD  . PRO   C  1 81  ? 26.009  -57.587 -7.149  1.00 33.29  0  96  PRO   C CD  1 
ATOM   4636 N  N   . GLN   C  1 82  ? 24.101  -55.922 -9.985  1.00 26.71  0  97  GLN   C N   1 
ATOM   4637 C  CA  . GLN   C  1 82  ? 23.150  -55.599 -11.071 1.00 29.19  0  97  GLN   C CA  1 
ATOM   4638 C  C   . GLN   C  1 82  ? 22.478  -54.253 -10.799 1.00 30.39  0  97  GLN   C C   1 
ATOM   4639 O  O   . GLN   C  1 82  ? 21.740  -53.837 -11.671 1.00 31.02  0  97  GLN   C O   1 
ATOM   4640 C  CB  . GLN   C  1 82  ? 22.111  -56.712 -11.241 1.00 29.89  0  97  GLN   C CB  1 
ATOM   4641 C  CG  . GLN   C  1 82  ? 22.763  -58.065 -11.568 1.00 33.31  0  97  GLN   C CG  1 
ATOM   4642 C  CD  . GLN   C  1 82  ? 21.846  -59.269 -11.587 1.00 36.39  0  97  GLN   C CD  1 
ATOM   4643 O  OE1 . GLN   C  1 82  ? 22.303  -60.377 -11.815 1.00 42.44  0  97  GLN   C OE1 1 
ATOM   4644 N  NE2 . GLN   C  1 82  ? 20.553  -59.070 -11.418 1.00 40.09  0  97  GLN   C NE2 1 
ATOM   4645 N  N   . PHE   C  1 83  ? 22.732  -53.589 -9.664  1.00 27.24  0  98  PHE   C N   1 
ATOM   4646 C  CA  . PHE   C  1 83  ? 22.066  -52.297 -9.329  1.00 24.81  0  98  PHE   C CA  1 
ATOM   4647 C  C   . PHE   C  1 83  ? 22.703  -51.122 -10.084 1.00 24.01  0  98  PHE   C C   1 
ATOM   4648 O  O   . PHE   C  1 83  ? 23.945  -50.915 -10.021 1.00 20.62  0  98  PHE   C O   1 
ATOM   4649 C  CB  . PHE   C  1 83  ? 22.153  -51.968 -7.848  1.00 24.20  0  98  PHE   C CB  1 
ATOM   4650 C  CG  . PHE   C  1 83  ? 21.550  -50.627 -7.546  1.00 22.27  0  98  PHE   C CG  1 
ATOM   4651 C  CD1 . PHE   C  1 83  ? 20.166  -50.455 -7.609  1.00 21.65  0  98  PHE   C CD1 1 
ATOM   4652 C  CD2 . PHE   C  1 83  ? 22.361  -49.537 -7.252  1.00 21.36  0  98  PHE   C CD2 1 
ATOM   4653 C  CE1 . PHE   C  1 83  ? 19.593  -49.221 -7.312  1.00 21.99  0  98  PHE   C CE1 1 
ATOM   4654 C  CE2 . PHE   C  1 83  ? 21.786  -48.314 -6.929  1.00 20.35  0  98  PHE   C CE2 1 
ATOM   4655 C  CZ  . PHE   C  1 83  ? 20.409  -48.149 -7.005  1.00 21.64  0  98  PHE   C CZ  1 
ATOM   4656 N  N   . TYR   C  1 84  ? 21.851  -50.298 -10.693 1.00 24.68  0  99  TYR   C N   1 
ATOM   4657 C  CA  . TYR   C  1 84  ? 22.226  -48.965 -11.216 1.00 25.41  0  99  TYR   C CA  1 
ATOM   4658 C  C   . TYR   C  1 84  ? 21.173  -47.905 -10.785 1.00 26.24  0  99  TYR   C C   1 
ATOM   4659 O  O   . TYR   C  1 84  ? 21.574  -46.865 -10.308 1.00 22.68  0  99  TYR   C O   1 
ATOM   4660 C  CB  . TYR   C  1 84  ? 22.515  -49.009 -12.735 1.00 24.67  0  99  TYR   C CB  1 
ATOM   4661 C  CG  . TYR   C  1 84  ? 23.077  -47.680 -13.161 1.00 25.89  0  99  TYR   C CG  1 
ATOM   4662 C  CD1 . TYR   C  1 84  ? 24.303  -47.249 -12.684 1.00 25.76  0  99  TYR   C CD1 1 
ATOM   4663 C  CD2 . TYR   C  1 84  ? 22.324  -46.789 -13.919 1.00 28.73  0  99  TYR   C CD2 1 
ATOM   4664 C  CE1 . TYR   C  1 84  ? 24.775  -45.973 -12.945 1.00 27.11  0  99  TYR   C CE1 1 
ATOM   4665 C  CE2 . TYR   C  1 84  ? 22.788  -45.512 -14.184 1.00 26.26  0  99  TYR   C CE2 1 
ATOM   4666 C  CZ  . TYR   C  1 84  ? 24.020  -45.107 -13.715 1.00 27.98  0  99  TYR   C CZ  1 
ATOM   4667 O  OH  . TYR   C  1 84  ? 24.481  -43.839 -13.978 1.00 30.55  0  99  TYR   C OH  1 
ATOM   4668 N  N   . THR   C  1 85  ? 19.882  -48.155 -10.952 1.00 23.97  0  100 THR   C N   1 
ATOM   4669 C  CA  . THR   C  1 85  ? 18.784  -47.299 -10.435 1.00 24.72  0  100 THR   C CA  1 
ATOM   4670 C  C   . THR   C  1 85  ? 17.694  -48.202 -9.850  1.00 24.06  0  100 THR   C C   1 
ATOM   4671 O  O   . THR   C  1 85  ? 17.570  -49.397 -10.254 1.00 22.77  0  100 THR   C O   1 
ATOM   4672 C  CB  . THR   C  1 85  ? 18.168  -46.402 -11.534 1.00 24.72  0  100 THR   C CB  1 
ATOM   4673 O  OG1 . THR   C  1 85  ? 17.349  -47.204 -12.385 1.00 26.26  0  100 THR   C OG1 1 
ATOM   4674 C  CG2 . THR   C  1 85  ? 19.172  -45.703 -12.412 1.00 25.60  0  100 THR   C CG2 1 
ATOM   4675 N  N   . ALA   C  1 86  ? 16.884  -47.645 -8.966  1.00 23.70  0  101 ALA   C N   1 
ATOM   4676 C  CA  . ALA   C  1 86  ? 15.780  -48.369 -8.289  1.00 25.19  0  101 ALA   C CA  1 
ATOM   4677 C  C   . ALA   C  1 86  ? 14.747  -48.823 -9.315  1.00 27.89  0  101 ALA   C C   1 
ATOM   4678 O  O   . ALA   C  1 86  ? 14.167  -49.923 -9.125  1.00 27.77  0  101 ALA   C O   1 
ATOM   4679 C  CB  . ALA   C  1 86  ? 15.150  -47.476 -7.254  1.00 27.97  0  101 ALA   C CB  1 
ATOM   4680 N  N   . GLN   C  1 87  ? 14.485  -48.016 -10.358 1.00 25.58  0  102 GLN   C N   1 
ATOM   4681 C  CA  . GLN   C  1 87  ? 13.441  -48.368 -11.353 1.00 26.03  0  102 GLN   C CA  1 
ATOM   4682 C  C   . GLN   C  1 87  ? 13.869  -49.555 -12.223 1.00 23.76  0  102 GLN   C C   1 
ATOM   4683 O  O   . GLN   C  1 87  ? 12.965  -50.288 -12.669 1.00 24.03  0  102 GLN   C O   1 
ATOM   4684 C  CB  . GLN   C  1 87  ? 13.050  -47.179 -12.210 1.00 25.84  0  102 GLN   C CB  1 
ATOM   4685 C  CG  . GLN   C  1 87  ? 12.504  -46.031 -11.385 1.00 27.27  0  102 GLN   C CG  1 
ATOM   4686 C  CD  . GLN   C  1 87  ? 13.511  -44.968 -11.009 1.00 32.58  0  102 GLN   C CD  1 
ATOM   4687 O  OE1 . GLN   C  1 87  ? 14.743  -45.092 -11.125 1.00 33.61  0  102 GLN   C OE1 1 
ATOM   4688 N  NE2 . GLN   C  1 87  ? 12.964  -43.855 -10.573 1.00 45.33  0  102 GLN   C NE2 1 
ATOM   4689 N  N   . ILE   C  1 88  ? 15.164  -49.734 -12.442 1.00 23.95  0  103 ILE   C N   1 
ATOM   4690 C  CA  . ILE   C  1 88  ? 15.720  -50.908 -13.172 1.00 26.82  0  103 ILE   C CA  1 
ATOM   4691 C  C   . ILE   C  1 88  ? 15.649  -52.133 -12.248 1.00 28.73  0  103 ILE   C C   1 
ATOM   4692 O  O   . ILE   C  1 88  ? 15.257  -53.194 -12.723 1.00 26.57  0  103 ILE   C O   1 
ATOM   4693 C  CB  . ILE   C  1 88  ? 17.140  -50.630 -13.694 1.00 28.20  0  103 ILE   C CB  1 
ATOM   4694 C  CG1 . ILE   C  1 88  ? 17.144  -49.489 -14.724 1.00 26.69  0  103 ILE   C CG1 1 
ATOM   4695 C  CG2 . ILE   C  1 88  ? 17.721  -51.917 -14.268 1.00 27.32  0  103 ILE   C CG2 1 
ATOM   4696 C  CD1 . ILE   C  1 88  ? 18.516  -48.999 -15.098 1.00 27.79  0  103 ILE   C CD1 1 
ATOM   4697 N  N   . GLY   C  1 89  ? 16.042  -51.984 -10.976 1.00 29.04  0  104 GLY   C N   1 
ATOM   4698 C  CA  . GLY   C  1 89  ? 15.866  -53.000 -9.917  1.00 28.17  0  104 GLY   C CA  1 
ATOM   4699 C  C   . GLY   C  1 89  ? 17.181  -53.419 -9.293  1.00 24.15  0  104 GLY   C C   1 
ATOM   4700 O  O   . GLY   C  1 89  ? 18.157  -52.685 -9.408  1.00 25.56  0  104 GLY   C O   1 
ATOM   4701 N  N   . ALA   C  1 90  ? 17.199  -54.589 -8.662  1.00 28.70  0  105 ALA   C N   1 
ATOM   4702 C  CA  . ALA   C  1 90  ? 18.303  -55.072 -7.807  1.00 27.93  0  105 ALA   C CA  1 
ATOM   4703 C  C   . ALA   C  1 90  ? 18.635  -54.018 -6.718  1.00 26.53  0  105 ALA   C C   1 
ATOM   4704 O  O   . ALA   C  1 90  ? 19.824  -53.892 -6.366  1.00 24.92  0  105 ALA   C O   1 
ATOM   4705 C  CB  . ALA   C  1 90  ? 19.477  -55.412 -8.681  1.00 28.86  0  105 ALA   C CB  1 
ATOM   4706 N  N   . ASP   C  1 91  ? 17.622  -53.324 -6.174  1.00 23.69  0  106 ASP   C N   1 
ATOM   4707 C  CA  . ASP   C  1 91  ? 17.829  -52.242 -5.175  1.00 23.33  0  106 ASP   C CA  1 
ATOM   4708 C  C   . ASP   C  1 91  ? 17.993  -52.862 -3.758  1.00 23.98  0  106 ASP   C C   1 
ATOM   4709 O  O   . ASP   C  1 91  ? 17.043  -52.845 -2.932  1.00 23.34  0  106 ASP   C O   1 
ATOM   4710 C  CB  . ASP   C  1 91  ? 16.688  -51.213 -5.250  1.00 23.19  0  106 ASP   C CB  1 
ATOM   4711 C  CG  . ASP   C  1 91  ? 16.984  -49.983 -4.413  1.00 23.47  0  106 ASP   C CG  1 
ATOM   4712 O  OD1 . ASP   C  1 91  ? 18.145  -49.839 -3.988  1.00 23.16  0  106 ASP   C OD1 1 
ATOM   4713 O  OD2 . ASP   C  1 91  ? 16.042  -49.200 -4.151  1.00 27.06  -1 106 ASP   C OD2 1 
ATOM   4714 N  N   . ILE   C  1 92  ? 19.171  -53.400 -3.481  1.00 23.49  0  107 ILE   C N   1 
ATOM   4715 C  CA  . ILE   C  1 92  ? 19.431  -54.194 -2.246  1.00 24.96  0  107 ILE   C CA  1 
ATOM   4716 C  C   . ILE   C  1 92  ? 20.930  -54.179 -1.975  1.00 24.80  0  107 ILE   C C   1 
ATOM   4717 O  O   . ILE   C  1 92  ? 21.700  -54.206 -2.934  1.00 25.39  0  107 ILE   C O   1 
ATOM   4718 C  CB  . ILE   C  1 92  ? 18.869  -55.622 -2.353  1.00 26.62  0  107 ILE   C CB  1 
ATOM   4719 C  CG1 . ILE   C  1 92  ? 18.837  -56.307 -0.987  1.00 29.72  0  107 ILE   C CG1 1 
ATOM   4720 C  CG2 . ILE   C  1 92  ? 19.616  -56.459 -3.396  1.00 27.64  0  107 ILE   C CG2 1 
ATOM   4721 C  CD1 . ILE   C  1 92  ? 17.938  -57.530 -0.992  1.00 31.67  0  107 ILE   C CD1 1 
ATOM   4722 N  N   . ALA   C  1 93  ? 21.299  -54.034 -0.701  1.00 25.08  0  108 ALA   C N   1 
ATOM   4723 C  CA  . ALA   C  1 93  ? 22.693  -53.958 -0.224  1.00 26.04  0  108 ALA   C CA  1 
ATOM   4724 C  C   . ALA   C  1 93  ? 22.787  -54.521 1.189   1.00 24.93  0  108 ALA   C C   1 
ATOM   4725 O  O   . ALA   C  1 93  ? 21.766  -54.602 1.887   1.00 24.29  0  108 ALA   C O   1 
ATOM   4726 C  CB  . ALA   C  1 93  ? 23.225  -52.536 -0.301  1.00 25.66  0  108 ALA   C CB  1 
ATOM   4727 N  N   . LEU   C  1 94  ? 24.019  -54.836 1.561   1.00 27.06  0  109 LEU   C N   1 
ATOM   4728 C  CA  . LEU   C  1 94  ? 24.393  -55.401 2.870   1.00 28.17  0  109 LEU   C CA  1 
ATOM   4729 C  C   . LEU   C  1 94  ? 25.482  -54.508 3.442   1.00 28.69  0  109 LEU   C C   1 
ATOM   4730 O  O   . LEU   C  1 94  ? 26.419  -54.144 2.701   1.00 26.10  0  109 LEU   C O   1 
ATOM   4731 C  CB  . LEU   C  1 94  ? 24.860  -56.845 2.687   1.00 29.18  0  109 LEU   C CB  1 
ATOM   4732 C  CG  . LEU   C  1 94  ? 23.730  -57.828 2.342   1.00 32.09  0  109 LEU   C CG  1 
ATOM   4733 C  CD1 . LEU   C  1 94  ? 24.279  -59.176 1.861   1.00 33.72  0  109 LEU   C CD1 1 
ATOM   4734 C  CD2 . LEU   C  1 94  ? 22.766  -58.008 3.517   1.00 31.76  0  109 LEU   C CD2 1 
ATOM   4735 N  N   . LEU   C  1 95  ? 25.327  -54.161 4.714   1.00 27.83  0  110 LEU   C N   1 
ATOM   4736 C  CA  . LEU   C  1 95  ? 26.400  -53.557 5.529   1.00 26.96  0  110 LEU   C CA  1 
ATOM   4737 C  C   . LEU   C  1 95  ? 26.871  -54.618 6.530   1.00 26.78  0  110 LEU   C C   1 
ATOM   4738 O  O   . LEU   C  1 95  ? 26.040  -55.138 7.305   1.00 26.02  0  110 LEU   C O   1 
ATOM   4739 C  CB  . LEU   C  1 95  ? 25.860  -52.324 6.270   1.00 28.54  0  110 LEU   C CB  1 
ATOM   4740 C  CG  . LEU   C  1 95  ? 25.020  -51.336 5.468   1.00 28.83  0  110 LEU   C CG  1 
ATOM   4741 C  CD1 . LEU   C  1 95  ? 24.514  -50.209 6.391   1.00 28.64  0  110 LEU   C CD1 1 
ATOM   4742 C  CD2 . LEU   C  1 95  ? 25.853  -50.800 4.298   1.00 28.91  0  110 LEU   C CD2 1 
ATOM   4743 N  N   . GLU   C  1 96  ? 28.164  -54.891 6.510   1.00 28.40  0  111 GLU   C N   1 
ATOM   4744 C  CA  . GLU   C  1 96  ? 28.837  -55.753 7.508   1.00 29.06  0  111 GLU   C CA  1 
ATOM   4745 C  C   . GLU   C  1 96  ? 29.352  -54.853 8.626   1.00 28.85  0  111 GLU   C C   1 
ATOM   4746 O  O   . GLU   C  1 96  ? 30.220  -53.965 8.350   1.00 31.44  0  111 GLU   C O   1 
ATOM   4747 C  CB  . GLU   C  1 96  ? 29.981  -56.514 6.824   1.00 31.70  0  111 GLU   C CB  1 
ATOM   4748 C  CG  . GLU   C  1 96  ? 30.617  -57.583 7.702   1.00 37.38  0  111 GLU   C CG  1 
ATOM   4749 C  CD  . GLU   C  1 96  ? 31.710  -58.418 7.037   1.00 39.71  0  111 GLU   C CD  1 
ATOM   4750 O  OE1 . GLU   C  1 96  ? 32.379  -57.928 6.127   1.00 41.65  0  111 GLU   C OE1 1 
ATOM   4751 O  OE2 . GLU   C  1 96  ? 31.889  -59.558 7.449   1.00 45.39  -1 111 GLU   C OE2 1 
ATOM   4752 N  N   . LEU   C  1 97  ? 28.858  -55.057 9.847   1.00 30.13  0  112 LEU   C N   1 
ATOM   4753 C  CA  . LEU   C  1 97  ? 29.311  -54.278 11.034  1.00 33.54  0  112 LEU   C CA  1 
ATOM   4754 C  C   . LEU   C  1 97  ? 30.708  -54.768 11.416  1.00 36.22  0  112 LEU   C C   1 
ATOM   4755 O  O   . LEU   C  1 97  ? 31.007  -55.934 11.128  1.00 31.14  0  112 LEU   C O   1 
ATOM   4756 C  CB  . LEU   C  1 97  ? 28.315  -54.488 12.178  1.00 34.83  0  112 LEU   C CB  1 
ATOM   4757 C  CG  . LEU   C  1 97  ? 26.869  -54.096 11.845  1.00 38.72  0  112 LEU   C CG  1 
ATOM   4758 C  CD1 . LEU   C  1 97  ? 25.920  -54.438 12.983  1.00 41.81  0  112 LEU   C CD1 1 
ATOM   4759 C  CD2 . LEU   C  1 97  ? 26.768  -52.625 11.489  1.00 37.72  0  112 LEU   C CD2 1 
ATOM   4760 N  N   . GLU   C  1 98  ? 31.491  -53.900 12.062  1.00 39.28  0  113 GLU   C N   1 
ATOM   4761 C  CA  A GLU   C  1 98  ? 32.877  -54.211 12.505  0.50 42.02  0  113 GLU   C CA  1 
ATOM   4762 C  CA  B GLU   C  1 98  ? 32.872  -54.163 12.560  0.50 41.63  0  113 GLU   C CA  1 
ATOM   4763 C  C   . GLU   C  1 98  ? 32.840  -55.241 13.641  1.00 40.85  0  113 GLU   C C   1 
ATOM   4764 O  O   . GLU   C  1 98  ? 33.824  -55.889 13.812  1.00 39.04  0  113 GLU   C O   1 
ATOM   4765 C  CB  A GLU   C  1 98  ? 33.592  -52.930 12.943  0.50 43.60  0  113 GLU   C CB  1 
ATOM   4766 C  CB  B GLU   C  1 98  ? 33.487  -52.916 13.210  0.50 42.85  0  113 GLU   C CB  1 
ATOM   4767 C  CG  A GLU   C  1 98  ? 35.087  -53.089 13.117  0.50 44.81  0  113 GLU   C CG  1 
ATOM   4768 C  CG  B GLU   C  1 98  ? 33.780  -51.809 12.239  0.50 42.38  0  113 GLU   C CG  1 
ATOM   4769 C  CD  A GLU   C  1 98  ? 35.889  -51.806 13.011  0.50 46.88  0  113 GLU   C CD  1 
ATOM   4770 C  CD  B GLU   C  1 98  ? 34.992  -52.147 11.425  0.50 42.96  0  113 GLU   C CD  1 
ATOM   4771 O  OE1 A GLU   C  1 98  ? 35.486  -50.828 13.655  0.50 51.68  0  113 GLU   C OE1 1 
ATOM   4772 O  OE1 B GLU   C  1 98  ? 35.319  -53.345 11.392  0.50 41.88  0  113 GLU   C OE1 1 
ATOM   4773 O  OE2 A GLU   C  1 98  ? 36.922  -51.791 12.290  0.50 45.60  -1 113 GLU   C OE2 1 
ATOM   4774 O  OE2 B GLU   C  1 98  ? 35.612  -51.216 10.876  0.50 42.94  -1 113 GLU   C OE2 1 
ATOM   4775 N  N   . GLU   C  1 99  ? 31.727  -55.333 14.366  1.00 39.82  0  114 GLU   C N   1 
ATOM   4776 C  CA  . GLU   C  1 99  ? 31.517  -56.274 15.489  1.00 46.57  0  114 GLU   C CA  1 
ATOM   4777 C  C   . GLU   C  1 99  ? 30.102  -56.802 15.462  1.00 39.64  0  114 GLU   C C   1 
ATOM   4778 O  O   . GLU   C  1 99  ? 29.168  -56.094 15.083  1.00 39.02  0  114 GLU   C O   1 
ATOM   4779 C  CB  . GLU   C  1 99  ? 31.649  -55.581 16.854  1.00 51.78  0  114 GLU   C CB  1 
ATOM   4780 C  CG  . GLU   C  1 99  ? 33.036  -55.042 17.117  1.00 52.73  0  114 GLU   C CG  1 
ATOM   4781 C  CD  . GLU   C  1 99  ? 34.090  -56.089 17.448  1.00 57.40  0  114 GLU   C CD  1 
ATOM   4782 O  OE1 . GLU   C  1 99  ? 33.754  -57.271 17.619  1.00 56.39  0  114 GLU   C OE1 1 
ATOM   4783 O  OE2 . GLU   C  1 99  ? 35.254  -55.706 17.570  1.00 74.75  -1 114 GLU   C OE2 1 
ATOM   4784 N  N   . PRO   C  1 100 ? 29.903  -58.049 15.927  1.00 42.71  0  115 PRO   C N   1 
ATOM   4785 C  CA  . PRO   C  1 100 ? 28.552  -58.587 16.069  1.00 43.58  0  115 PRO   C CA  1 
ATOM   4786 C  C   . PRO   C  1 100 ? 27.891  -57.810 17.217  1.00 43.68  0  115 PRO   C C   1 
ATOM   4787 O  O   . PRO   C  1 100 ? 28.599  -57.364 18.103  1.00 51.27  0  115 PRO   C O   1 
ATOM   4788 C  CB  . PRO   C  1 100 ? 28.765  -60.071 16.388  1.00 42.33  0  115 PRO   C CB  1 
ATOM   4789 C  CG  . PRO   C  1 100 ? 30.160  -60.129 16.989  1.00 44.20  0  115 PRO   C CG  1 
ATOM   4790 C  CD  . PRO   C  1 100 ? 30.953  -58.983 16.376  1.00 43.41  0  115 PRO   C CD  1 
ATOM   4791 N  N   . VAL   C  1 101 ? 26.591  -57.577 17.149  1.00 40.69  0  116 VAL   C N   1 
ATOM   4792 C  CA  . VAL   C  1 101 ? 25.886  -56.896 18.269  1.00 44.82  0  116 VAL   C CA  1 
ATOM   4793 C  C   . VAL   C  1 101 ? 25.468  -58.014 19.239  1.00 45.44  0  116 VAL   C C   1 
ATOM   4794 O  O   . VAL   C  1 101 ? 25.187  -59.165 18.758  1.00 46.67  0  116 VAL   C O   1 
ATOM   4795 C  CB  . VAL   C  1 101 ? 24.730  -55.998 17.789  1.00 43.23  0  116 VAL   C CB  1 
ATOM   4796 C  CG1 . VAL   C  1 101 ? 25.100  -55.172 16.556  1.00 44.98  0  116 VAL   C CG1 1 
ATOM   4797 C  CG2 . VAL   C  1 101 ? 23.456  -56.756 17.523  1.00 46.91  0  116 VAL   C CG2 1 
ATOM   4798 N  N   . LYS   C  1 102 ? 25.446  -57.705 20.539  1.00 47.76  0  117 LYS   C N   1 
ATOM   4799 C  CA  . LYS   C  1 102 ? 24.884  -58.584 21.602  1.00 53.45  0  117 LYS   C CA  1 
ATOM   4800 C  C   . LYS   C  1 102 ? 23.367  -58.390 21.605  1.00 48.50  0  117 LYS   C C   1 
ATOM   4801 O  O   . LYS   C  1 102 ? 22.945  -57.316 22.007  1.00 52.93  0  117 LYS   C O   1 
ATOM   4802 C  CB  . LYS   C  1 102 ? 25.505  -58.247 22.968  1.00 58.33  0  117 LYS   C CB  1 
ATOM   4803 C  CG  . LYS   C  1 102 ? 25.102  -59.186 24.100  1.00 65.02  0  117 LYS   C CG  1 
ATOM   4804 C  CD  . LYS   C  1 102 ? 25.859  -58.986 25.405  1.00 69.00  0  117 LYS   C CD  1 
ATOM   4805 C  CE  . LYS   C  1 102 ? 25.285  -59.806 26.546  1.00 71.85  0  117 LYS   C CE  1 
ATOM   4806 N  NZ  . LYS   C  1 102 ? 25.398  -59.111 27.854  1.00 74.69  1  117 LYS   C NZ  1 
ATOM   4807 N  N   . VAL   C  1 103 ? 22.577  -59.370 21.147  1.00 49.75  0  118 VAL   C N   1 
ATOM   4808 C  CA  . VAL   C  1 103 ? 21.103  -59.182 20.944  1.00 49.32  0  118 VAL   C CA  1 
ATOM   4809 C  C   . VAL   C  1 103 ? 20.365  -59.233 22.301  1.00 51.76  0  118 VAL   C C   1 
ATOM   4810 O  O   . VAL   C  1 103 ? 20.928  -59.733 23.289  1.00 47.58  0  118 VAL   C O   1 
ATOM   4811 C  CB  . VAL   C  1 103 ? 20.519  -60.171 19.910  1.00 50.68  0  118 VAL   C CB  1 
ATOM   4812 C  CG1 . VAL   C  1 103 ? 21.118  -59.957 18.521  1.00 50.97  0  118 VAL   C CG1 1 
ATOM   4813 C  CG2 . VAL   C  1 103 ? 20.648  -61.630 20.316  1.00 50.17  0  118 VAL   C CG2 1 
ATOM   4814 N  N   . SER   C  1 104 ? 19.164  -58.675 22.341  1.00 45.09  0  119 SER   C N   1 
ATOM   4815 C  CA  . SER   C  1 104 ? 18.321  -58.536 23.548  1.00 49.33  0  119 SER   C CA  1 
ATOM   4816 C  C   . SER   C  1 104 ? 16.867  -58.527 23.101  1.00 52.70  0  119 SER   C C   1 
ATOM   4817 O  O   . SER   C  1 104 ? 16.625  -58.561 21.874  1.00 58.29  0  119 SER   C O   1 
ATOM   4818 C  CB  . SER   C  1 104 ? 18.703  -57.293 24.301  1.00 50.06  0  119 SER   C CB  1 
ATOM   4819 O  OG  . SER   C  1 104 ? 18.467  -56.126 23.530  1.00 41.88  0  119 SER   C OG  1 
ATOM   4820 N  N   . SER   C  1 105 ? 15.924  -58.480 24.031  1.00 48.46  0  120 SER   C N   1 
ATOM   4821 C  CA  . SER   C  1 105 ? 14.489  -58.373 23.661  1.00 55.34  0  120 SER   C CA  1 
ATOM   4822 C  C   . SER   C  1 105 ? 14.221  -56.991 23.027  1.00 49.12  0  120 SER   C C   1 
ATOM   4823 O  O   . SER   C  1 105 ? 13.276  -56.891 22.214  1.00 54.89  0  120 SER   C O   1 
ATOM   4824 C  CB  . SER   C  1 105 ? 13.588  -58.678 24.842  1.00 54.78  0  120 SER   C CB  1 
ATOM   4825 O  OG  . SER   C  1 105 ? 13.596  -57.596 25.754  1.00 57.90  0  120 SER   C OG  1 
ATOM   4826 N  N   . HIS   C  1 106 ? 15.018  -55.961 23.354  1.00 49.93  0  121 HIS   C N   1 
ATOM   4827 C  CA  . HIS   C  1 106 ? 14.867  -54.593 22.786  1.00 53.25  0  121 HIS   C CA  1 
ATOM   4828 C  C   . HIS   C  1 106 ? 15.511  -54.462 21.386  1.00 49.60  0  121 HIS   C C   1 
ATOM   4829 O  O   . HIS   C  1 106 ? 14.990  -53.679 20.563  1.00 43.10  0  121 HIS   C O   1 
ATOM   4830 C  CB  . HIS   C  1 106 ? 15.393  -53.523 23.752  1.00 59.27  0  121 HIS   C CB  1 
ATOM   4831 C  CG  . HIS   C  1 106 ? 15.007  -52.134 23.347  1.00 72.68  0  121 HIS   C CG  1 
ATOM   4832 N  ND1 . HIS   C  1 106 ? 13.690  -51.679 23.385  1.00 72.19  0  121 HIS   C ND1 1 
ATOM   4833 C  CD2 . HIS   C  1 106 ? 15.753  -51.100 22.888  1.00 78.88  0  121 HIS   C CD2 1 
ATOM   4834 C  CE1 . HIS   C  1 106 ? 13.643  -50.433 22.956  1.00 78.94  0  121 HIS   C CE1 1 
ATOM   4835 N  NE2 . HIS   C  1 106 ? 14.901  -50.054 22.652  1.00 85.93  0  121 HIS   C NE2 1 
ATOM   4836 N  N   . VAL   C  1 107 ? 16.629  -55.143 21.141  1.00 40.69  0  122 VAL   C N   1 
ATOM   4837 C  CA  . VAL   C  1 107 ? 17.438  -55.038 19.897  1.00 42.13  0  122 VAL   C CA  1 
ATOM   4838 C  C   . VAL   C  1 107 ? 17.780  -56.458 19.436  1.00 42.20  0  122 VAL   C C   1 
ATOM   4839 O  O   . VAL   C  1 107 ? 18.676  -57.079 20.063  1.00 35.75  0  122 VAL   C O   1 
ATOM   4840 C  CB  . VAL   C  1 107 ? 18.702  -54.192 20.114  1.00 41.57  0  122 VAL   C CB  1 
ATOM   4841 C  CG1 . VAL   C  1 107 ? 19.591  -54.196 18.886  1.00 42.95  0  122 VAL   C CG1 1 
ATOM   4842 C  CG2 . VAL   C  1 107 ? 18.358  -52.766 20.516  1.00 47.60  0  122 VAL   C CG2 1 
ATOM   4843 N  N   . HIS   C  1 108 ? 17.141  -56.940 18.366  1.00 35.35  0  123 HIS   C N   1 
ATOM   4844 C  CA  . HIS   C  1 108 ? 17.462  -58.268 17.785  1.00 39.67  0  123 HIS   C CA  1 
ATOM   4845 C  C   . HIS   C  1 108 ? 17.021  -58.354 16.318  1.00 37.49  0  123 HIS   C C   1 
ATOM   4846 O  O   . HIS   C  1 108 ? 16.434  -57.390 15.811  1.00 33.14  0  123 HIS   C O   1 
ATOM   4847 C  CB  . HIS   C  1 108 ? 16.928  -59.389 18.692  1.00 38.42  0  123 HIS   C CB  1 
ATOM   4848 C  CG  . HIS   C  1 108 ? 15.461  -59.562 18.691  1.00 38.76  0  123 HIS   C CG  1 
ATOM   4849 N  ND1 . HIS   C  1 108 ? 14.671  -59.130 19.745  1.00 43.55  0  123 HIS   C ND1 1 
ATOM   4850 C  CD2 . HIS   C  1 108 ? 14.645  -60.165 17.801  1.00 40.15  0  123 HIS   C CD2 1 
ATOM   4851 C  CE1 . HIS   C  1 108 ? 13.415  -59.441 19.495  1.00 45.84  0  123 HIS   C CE1 1 
ATOM   4852 N  NE2 . HIS   C  1 108 ? 13.367  -60.084 18.306  1.00 44.59  0  123 HIS   C NE2 1 
ATOM   4853 N  N   . THR   C  1 109 ? 17.346  -59.472 15.667  1.00 31.55  0  124 THR   C N   1 
ATOM   4854 C  CA  . THR   C  1 109 ? 17.319  -59.629 14.200  1.00 30.34  0  124 THR   C CA  1 
ATOM   4855 C  C   . THR   C  1 109 ? 15.887  -59.879 13.752  1.00 29.86  0  124 THR   C C   1 
ATOM   4856 O  O   . THR   C  1 109 ? 15.057  -60.302 14.576  1.00 32.20  0  124 THR   C O   1 
ATOM   4857 C  CB  . THR   C  1 109 ? 18.205  -60.774 13.702  1.00 33.04  0  124 THR   C CB  1 
ATOM   4858 O  OG1 . THR   C  1 109 ? 17.606  -61.971 14.186  1.00 34.95  0  124 THR   C OG1 1 
ATOM   4859 C  CG2 . THR   C  1 109 ? 19.649  -60.696 14.129  1.00 28.99  0  124 THR   C CG2 1 
ATOM   4860 N  N   . VAL   C  1 110 ? 15.611  -59.576 12.491  1.00 26.67  0  125 VAL   C N   1 
ATOM   4861 C  CA  . VAL   C  1 110 ? 14.338  -59.966 11.825  1.00 29.20  0  125 VAL   C CA  1 
ATOM   4862 C  C   . VAL   C  1 110 ? 14.625  -61.287 11.095  1.00 29.29  0  125 VAL   C C   1 
ATOM   4863 O  O   . VAL   C  1 110 ? 15.790  -61.494 10.688  1.00 31.95  0  125 VAL   C O   1 
ATOM   4864 C  CB  . VAL   C  1 110 ? 13.816  -58.856 10.887  1.00 26.87  0  125 VAL   C CB  1 
ATOM   4865 C  CG1 . VAL   C  1 110 ? 14.694  -58.687 9.661   1.00 26.05  0  125 VAL   C CG1 1 
ATOM   4866 C  CG2 . VAL   C  1 110 ? 12.364  -59.082 10.516  1.00 28.28  0  125 VAL   C CG2 1 
ATOM   4867 N  N   . THR   C  1 111 ? 13.611  -62.115 10.929  1.00 31.57  0  126 THR   C N   1 
ATOM   4868 C  CA  . THR   C  1 111 ? 13.696  -63.396 10.176  1.00 34.73  0  126 THR   C CA  1 
ATOM   4869 C  C   . THR   C  1 111 ? 13.482  -63.120 8.672   1.00 32.53  0  126 THR   C C   1 
ATOM   4870 O  O   . THR   C  1 111 ? 12.494  -62.414 8.311   1.00 29.95  0  126 THR   C O   1 
ATOM   4871 C  CB  . THR   C  1 111 ? 12.685  -64.390 10.770  1.00 39.92  0  126 THR   C CB  1 
ATOM   4872 O  OG1 . THR   C  1 111 ? 13.054  -64.491 12.156  1.00 40.90  0  126 THR   C OG1 1 
ATOM   4873 C  CG2 . THR   C  1 111 ? 12.665  -65.746 10.096  1.00 41.52  0  126 THR   C CG2 1 
ATOM   4874 N  N   . LEU   C  1 112 ? 14.361  -63.663 7.826   1.00 30.00  0  127 LEU   C N   1 
ATOM   4875 C  CA  . LEU   C  1 112 ? 14.155  -63.665 6.351   1.00 33.91  0  127 LEU   C CA  1 
ATOM   4876 C  C   . LEU   C  1 112 ? 13.110  -64.708 5.986   1.00 39.93  0  127 LEU   C C   1 
ATOM   4877 O  O   . LEU   C  1 112 ? 13.014  -65.750 6.614   1.00 37.93  0  127 LEU   C O   1 
ATOM   4878 C  CB  . LEU   C  1 112 ? 15.469  -63.901 5.608   1.00 33.19  0  127 LEU   C CB  1 
ATOM   4879 C  CG  . LEU   C  1 112 ? 16.512  -62.829 5.892   1.00 35.91  0  127 LEU   C CG  1 
ATOM   4880 C  CD1 . LEU   C  1 112 ? 17.827  -63.120 5.206   1.00 38.30  0  127 LEU   C CD1 1 
ATOM   4881 C  CD2 . LEU   C  1 112 ? 15.983  -61.459 5.514   1.00 36.91  0  127 LEU   C CD2 1 
ATOM   4882 N  N   . PRO   C  1 113 ? 12.283  -64.450 4.956   1.00 37.65  0  128 PRO   C N   1 
ATOM   4883 C  CA  . PRO   C  1 113 ? 11.278  -65.419 4.538   1.00 38.20  0  128 PRO   C CA  1 
ATOM   4884 C  C   . PRO   C  1 113 ? 11.945  -66.591 3.819   1.00 35.81  0  128 PRO   C C   1 
ATOM   4885 O  O   . PRO   C  1 113 ? 13.065  -66.469 3.322   1.00 30.99  0  128 PRO   C O   1 
ATOM   4886 C  CB  . PRO   C  1 113 ? 10.374  -64.605 3.622   1.00 37.98  0  128 PRO   C CB  1 
ATOM   4887 C  CG  . PRO   C  1 113 ? 11.268  -63.514 3.071   1.00 36.64  0  128 PRO   C CG  1 
ATOM   4888 C  CD  . PRO   C  1 113 ? 12.297  -63.231 4.135   1.00 41.04  0  128 PRO   C CD  1 
ATOM   4889 N  N   . PRO   C  1 114 ? 11.294  -67.771 3.759   1.00 42.32  0  129 PRO   C N   1 
ATOM   4890 C  CA  . PRO   C  1 114 ? 11.766  -68.852 2.884   1.00 44.27  0  129 PRO   C CA  1 
ATOM   4891 C  C   . PRO   C  1 114 ? 11.531  -68.446 1.417   1.00 42.18  0  129 PRO   C C   1 
ATOM   4892 O  O   . PRO   C  1 114 ? 10.595  -67.700 1.153   1.00 38.84  0  129 PRO   C O   1 
ATOM   4893 C  CB  . PRO   C  1 114 ? 10.907  -70.049 3.306   1.00 45.80  0  129 PRO   C CB  1 
ATOM   4894 C  CG  . PRO   C  1 114 ? 9.618   -69.407 3.797   1.00 48.70  0  129 PRO   C CG  1 
ATOM   4895 C  CD  . PRO   C  1 114 ? 10.067  -68.130 4.489   1.00 46.12  0  129 PRO   C CD  1 
ATOM   4896 N  N   . ALA   C  1 115 ? 12.340  -68.980 0.491   1.00 47.87  0  130 ALA   C N   1 
ATOM   4897 C  CA  . ALA   C  1 115 ? 12.276  -68.743 -0.976  1.00 47.54  0  130 ALA   C CA  1 
ATOM   4898 C  C   . ALA   C  1 115 ? 10.865  -68.968 -1.510  1.00 46.83  0  130 ALA   C C   1 
ATOM   4899 O  O   . ALA   C  1 115 ? 10.437  -68.219 -2.379  1.00 57.79  0  130 ALA   C O   1 
ATOM   4900 C  CB  . ALA   C  1 115 ? 13.289  -69.607 -1.685  1.00 52.04  0  130 ALA   C CB  1 
ATOM   4901 N  N   . SER   C  1 116 ? 10.130  -69.913 -0.947  1.00 50.61  0  131 SER   C N   1 
ATOM   4902 C  CA  . SER   C  1 116 ? 8.772   -70.301 -1.391  1.00 56.36  0  131 SER   C CA  1 
ATOM   4903 C  C   . SER   C  1 116 ? 7.708   -69.271 -0.982  1.00 53.47  0  131 SER   C C   1 
ATOM   4904 O  O   . SER   C  1 116 ? 6.663   -69.300 -1.596  1.00 55.30  0  131 SER   C O   1 
ATOM   4905 C  CB  . SER   C  1 116 ? 8.436   -71.684 -0.866  1.00 58.38  0  131 SER   C CB  1 
ATOM   4906 O  OG  . SER   C  1 116 ? 8.618   -71.748 0.544   1.00 59.27  0  131 SER   C OG  1 
ATOM   4907 N  N   . GLU   C  1 117 ? 7.951   -68.393 -0.003  1.00 54.13  0  132 GLU   C N   1 
ATOM   4908 C  CA  . GLU   C  1 117 ? 6.894   -67.553 0.623   1.00 50.30  0  132 GLU   C CA  1 
ATOM   4909 C  C   . GLU   C  1 117 ? 6.395   -66.520 -0.396  1.00 51.83  0  132 GLU   C C   1 
ATOM   4910 O  O   . GLU   C  1 117 ? 7.214   -65.753 -0.924  1.00 49.21  0  132 GLU   C O   1 
ATOM   4911 C  CB  . GLU   C  1 117 ? 7.435   -66.844 1.863   1.00 51.27  0  132 GLU   C CB  1 
ATOM   4912 C  CG  . GLU   C  1 117 ? 6.345   -66.107 2.613   1.00 53.23  0  132 GLU   C CG  1 
ATOM   4913 C  CD  . GLU   C  1 117 ? 5.527   -66.982 3.548   1.00 59.74  0  132 GLU   C CD  1 
ATOM   4914 O  OE1 . GLU   C  1 117 ? 6.132   -67.879 4.181   1.00 58.64  0  132 GLU   C OE1 1 
ATOM   4915 O  OE2 . GLU   C  1 117 ? 4.289   -66.738 3.677   1.00 62.90  -1 132 GLU   C OE2 1 
ATOM   4916 N  N   . THR   C  1 118 ? 5.100   -66.542 -0.703  1.00 59.45  0  133 THR   C N   1 
ATOM   4917 C  CA  . THR   C  1 118 ? 4.414   -65.586 -1.605  1.00 57.47  0  133 THR   C CA  1 
ATOM   4918 C  C   . THR   C  1 118 ? 3.422   -64.868 -0.693  1.00 63.08  0  133 THR   C C   1 
ATOM   4919 O  O   . THR   C  1 118 ? 2.408   -65.479 -0.316  1.00 82.74  0  133 THR   C O   1 
ATOM   4920 C  CB  . THR   C  1 118 ? 3.811   -66.289 -2.831  1.00 56.75  0  133 THR   C CB  1 
ATOM   4921 O  OG1 . THR   C  1 118 ? 4.818   -66.987 -3.519  0.00 60.30  0  133 THR   C OG1 1 
ATOM   4922 C  CG2 . THR   C  1 118 ? 3.188   -65.263 -3.815  0.00 60.47  0  133 THR   C CG2 1 
ATOM   4923 N  N   . PHE   C  1 119 ? 3.794   -63.671 -0.256  1.00 51.78  0  134 PHE   C N   1 
ATOM   4924 C  CA  . PHE   C  1 119 ? 3.005   -62.779 0.622   1.00 44.89  0  134 PHE   C CA  1 
ATOM   4925 C  C   . PHE   C  1 119 ? 1.764   -62.353 -0.149  1.00 43.75  0  134 PHE   C C   1 
ATOM   4926 O  O   . PHE   C  1 119 ? 1.854   -61.467 -0.984  1.00 52.22  0  134 PHE   C O   1 
ATOM   4927 C  CB  . PHE   C  1 119 ? 3.868   -61.582 1.012   1.00 41.33  0  134 PHE   C CB  1 
ATOM   4928 C  CG  . PHE   C  1 119 ? 5.084   -61.930 1.831   1.00 38.72  0  134 PHE   C CG  1 
ATOM   4929 C  CD1 . PHE   C  1 119 ? 4.977   -62.085 3.200   1.00 38.06  0  134 PHE   C CD1 1 
ATOM   4930 C  CD2 . PHE   C  1 119 ? 6.325   -62.074 1.245   1.00 35.72  0  134 PHE   C CD2 1 
ATOM   4931 C  CE1 . PHE   C  1 119 ? 6.092   -62.368 3.973   1.00 39.78  0  134 PHE   C CE1 1 
ATOM   4932 C  CE2 . PHE   C  1 119 ? 7.429   -62.401 2.008   1.00 36.09  0  134 PHE   C CE2 1 
ATOM   4933 C  CZ  . PHE   C  1 119 ? 7.317   -62.535 3.376   1.00 36.79  0  134 PHE   C CZ  1 
ATOM   4934 N  N   . PRO   C  1 120 ? 0.582   -62.956 0.084   1.00 43.15  0  135 PRO   C N   1 
ATOM   4935 C  CA  . PRO   C  1 120 ? -0.557  -62.752 -0.797  1.00 42.54  0  135 PRO   C CA  1 
ATOM   4936 C  C   . PRO   C  1 120 ? -1.149  -61.356 -0.688  1.00 39.94  0  135 PRO   C C   1 
ATOM   4937 O  O   . PRO   C  1 120 ? -1.047  -60.672 0.328   1.00 34.38  0  135 PRO   C O   1 
ATOM   4938 C  CB  . PRO   C  1 120 ? -1.615  -63.774 -0.330  1.00 42.33  0  135 PRO   C CB  1 
ATOM   4939 C  CG  . PRO   C  1 120 ? -1.272  -63.962 1.153   1.00 47.52  0  135 PRO   C CG  1 
ATOM   4940 C  CD  . PRO   C  1 120 ? 0.250   -63.861 1.198   1.00 43.94  0  135 PRO   C CD  1 
ATOM   4941 N  N   . PRO   C  1 121 ? -1.795  -60.886 -1.764  1.00 41.94  0  136 PRO   C N   1 
ATOM   4942 C  CA  . PRO   C  1 121 ? -2.462  -59.589 -1.736  1.00 43.43  0  136 PRO   C CA  1 
ATOM   4943 C  C   . PRO   C  1 121 ? -3.449  -59.483 -0.574  1.00 43.48  0  136 PRO   C C   1 
ATOM   4944 O  O   . PRO   C  1 121 ? -4.121  -60.442 -0.293  1.00 43.08  0  136 PRO   C O   1 
ATOM   4945 C  CB  . PRO   C  1 121 ? -3.169  -59.542 -3.091  1.00 44.37  0  136 PRO   C CB  1 
ATOM   4946 C  CG  . PRO   C  1 121 ? -2.262  -60.393 -3.968  1.00 46.34  0  136 PRO   C CG  1 
ATOM   4947 C  CD  . PRO   C  1 121 ? -1.913  -61.558 -3.073  1.00 46.05  0  136 PRO   C CD  1 
ATOM   4948 N  N   . GLY   C  1 122 ? -3.449  -58.330 0.079   1.00 48.88  0  137 GLY   C N   1 
ATOM   4949 C  CA  . GLY   C  1 122 ? -4.371  -58.011 1.181   1.00 48.38  0  137 GLY   C CA  1 
ATOM   4950 C  C   . GLY   C  1 122 ? -3.751  -58.261 2.536   1.00 47.54  0  137 GLY   C C   1 
ATOM   4951 O  O   . GLY   C  1 122 ? -4.236  -57.648 3.502   1.00 53.35  0  137 GLY   C O   1 
ATOM   4952 N  N   . MET   C  1 123 ? -2.714  -59.100 2.616   1.00 44.88  0  138 MET   C N   1 
ATOM   4953 C  CA  . MET   C  1 123 ? -2.048  -59.464 3.898   1.00 49.98  0  138 MET   C CA  1 
ATOM   4954 C  C   . MET   C  1 123 ? -1.604  -58.186 4.626   1.00 56.24  0  138 MET   C C   1 
ATOM   4955 O  O   . MET   C  1 123 ? -1.024  -57.288 3.992   1.00 50.78  0  138 MET   C O   1 
ATOM   4956 C  CB  . MET   C  1 123 ? -0.827  -60.363 3.666   1.00 46.35  0  138 MET   C CB  1 
ATOM   4957 C  CG  . MET   C  1 123 ? -0.005  -60.572 4.918   1.00 57.19  0  138 MET   C CG  1 
ATOM   4958 S  SD  . MET   C  1 123 ? 1.373   -61.683 4.636   1.00 70.94  0  138 MET   C SD  1 
ATOM   4959 C  CE  . MET   C  1 123 ? 0.504   -63.245 4.791   1.00 70.64  0  138 MET   C CE  1 
ATOM   4960 N  N   . PRO   C  1 124 ? -1.883  -58.058 5.951   1.00 58.27  0  139 PRO   C N   1 
ATOM   4961 C  CA  . PRO   C  1 124 ? -1.445  -56.892 6.719   1.00 58.52  0  139 PRO   C CA  1 
ATOM   4962 C  C   . PRO   C  1 124 ? 0.057   -56.969 7.046   1.00 44.76  0  139 PRO   C C   1 
ATOM   4963 O  O   . PRO   C  1 124 ? 0.470   -57.868 7.708   1.00 47.16  0  139 PRO   C O   1 
ATOM   4964 C  CB  . PRO   C  1 124 ? -2.326  -56.955 7.983   1.00 60.26  0  139 PRO   C CB  1 
ATOM   4965 C  CG  . PRO   C  1 124 ? -2.577  -58.436 8.187   1.00 62.63  0  139 PRO   C CG  1 
ATOM   4966 C  CD  . PRO   C  1 124 ? -2.646  -59.008 6.782   1.00 64.11  0  139 PRO   C CD  1 
ATOM   4967 N  N   . CYS   C  1 125 ? 0.831   -56.040 6.498   1.00 40.76  0  140 CYS   C N   1 
ATOM   4968 C  CA  . CYS   C  1 125 ? 2.274   -55.866 6.730   1.00 32.89  0  140 CYS   C CA  1 
ATOM   4969 C  C   . CYS   C  1 125 ? 2.504   -54.462 7.301   1.00 32.27  0  140 CYS   C C   1 
ATOM   4970 O  O   . CYS   C  1 125 ? 1.579   -53.637 7.239   1.00 27.81  0  140 CYS   C O   1 
ATOM   4971 C  CB  . CYS   C  1 125 ? 3.000   -56.067 5.410   1.00 39.34  0  140 CYS   C CB  1 
ATOM   4972 S  SG  . CYS   C  1 125 ? 2.676   -57.695 4.666   1.00 39.91  0  140 CYS   C SG  1 
ATOM   4973 N  N   . TRP   C  1 126 ? 3.700   -54.205 7.837   1.00 31.02  0  141 TRP   C N   1 
ATOM   4974 C  CA  . TRP   C  1 126 ? 4.070   -52.941 8.519   1.00 30.88  0  141 TRP   C CA  1 
ATOM   4975 C  C   . TRP   C  1 126 ? 5.365   -52.436 7.913   1.00 26.72  0  141 TRP   C C   1 
ATOM   4976 O  O   . TRP   C  1 126 ? 6.294   -53.230 7.724   1.00 26.54  0  141 TRP   C O   1 
ATOM   4977 C  CB  . TRP   C  1 126 ? 4.201   -53.130 10.038  1.00 29.99  0  141 TRP   C CB  1 
ATOM   4978 C  CG  . TRP   C  1 126 ? 2.885   -53.459 10.666  1.00 31.90  0  141 TRP   C CG  1 
ATOM   4979 C  CD1 . TRP   C  1 126 ? 2.252   -54.666 10.649  1.00 34.58  0  141 TRP   C CD1 1 
ATOM   4980 C  CD2 . TRP   C  1 126 ? 2.006   -52.547 11.344  1.00 34.74  0  141 TRP   C CD2 1 
ATOM   4981 N  NE1 . TRP   C  1 126 ? 1.043   -54.570 11.291  1.00 39.44  0  141 TRP   C NE1 1 
ATOM   4982 C  CE2 . TRP   C  1 126 ? 0.858   -53.281 11.718  1.00 36.03  0  141 TRP   C CE2 1 
ATOM   4983 C  CE3 . TRP   C  1 126 ? 2.080   -51.189 11.684  1.00 36.61  0  141 TRP   C CE3 1 
ATOM   4984 C  CZ2 . TRP   C  1 126 ? -0.194  -52.710 12.435  1.00 39.19  0  141 TRP   C CZ2 1 
ATOM   4985 C  CZ3 . TRP   C  1 126 ? 1.031   -50.614 12.372  1.00 42.96  0  141 TRP   C CZ3 1 
ATOM   4986 C  CH2 . TRP   C  1 126 ? -0.083  -51.374 12.764  1.00 44.15  0  141 TRP   C CH2 1 
ATOM   4987 N  N   . VAL   C  1 127 ? 5.431   -51.135 7.713   1.00 26.79  0  142 VAL   C N   1 
ATOM   4988 C  CA  . VAL   C  1 127 ? 6.700   -50.468 7.319   1.00 26.93  0  142 VAL   C CA  1 
ATOM   4989 C  C   . VAL   C  1 127 ? 6.971   -49.405 8.379   1.00 26.36  0  142 VAL   C C   1 
ATOM   4990 O  O   . VAL   C  1 127 ? 5.997   -48.839 8.942   1.00 27.17  0  142 VAL   C O   1 
ATOM   4991 C  CB  . VAL   C  1 127 ? 6.643   -49.924 5.878   1.00 24.80  0  142 VAL   C CB  1 
ATOM   4992 C  CG1 . VAL   C  1 127 ? 5.569   -48.876 5.694   1.00 26.60  0  142 VAL   C CG1 1 
ATOM   4993 C  CG2 . VAL   C  1 127 ? 7.996   -49.382 5.431   1.00 25.54  0  142 VAL   C CG2 1 
ATOM   4994 N  N   . THR   C  1 128 ? 8.247   -49.216 8.692   1.00 25.57  0  143 THR   C N   1 
ATOM   4995 C  CA  . THR   C  1 128 ? 8.711   -48.418 9.840   1.00 25.45  0  143 THR   C CA  1 
ATOM   4996 C  C   . THR   C  1 128 ? 9.837   -47.507 9.382   1.00 24.07  0  143 THR   C C   1 
ATOM   4997 O  O   . THR   C  1 128 ? 10.583  -47.888 8.407   1.00 24.10  0  143 THR   C O   1 
ATOM   4998 C  CB  . THR   C  1 128 ? 9.139   -49.364 10.980  1.00 27.57  0  143 THR   C CB  1 
ATOM   4999 O  OG1 . THR   C  1 128 ? 10.097  -50.312 10.523  1.00 25.19  0  143 THR   C OG1 1 
ATOM   5000 C  CG2 . THR   C  1 128 ? 8.011   -50.209 11.523  1.00 28.30  0  143 THR   C CG2 1 
ATOM   5001 N  N   . GLY   C  1 129 ? 9.996   -46.357 10.047  1.00 23.34  0  144 GLY   C N   1 
ATOM   5002 C  CA  . GLY   C  1 129 ? 11.162  -45.504 9.794   1.00 25.74  0  144 GLY   C CA  1 
ATOM   5003 C  C   . GLY   C  1 129 ? 10.990  -44.092 10.291  1.00 25.04  0  144 GLY   C C   1 
ATOM   5004 O  O   . GLY   C  1 129 ? 9.920   -43.774 10.878  1.00 25.83  0  144 GLY   C O   1 
ATOM   5005 N  N   . TRP   C  1 130 ? 12.035  -43.296 10.055  1.00 25.76  0  145 TRP   C N   1 
ATOM   5006 C  CA  . TRP   C  1 130 ? 12.131  -41.879 10.493  1.00 27.93  0  145 TRP   C CA  1 
ATOM   5007 C  C   . TRP   C  1 130 ? 12.065  -40.940 9.286   1.00 30.39  0  145 TRP   C C   1 
ATOM   5008 O  O   . TRP   C  1 130 ? 12.603  -39.801 9.383   1.00 30.18  0  145 TRP   C O   1 
ATOM   5009 C  CB  . TRP   C  1 130 ? 13.415  -41.668 11.274  1.00 25.56  0  145 TRP   C CB  1 
ATOM   5010 C  CG  . TRP   C  1 130 ? 13.538  -42.448 12.547  1.00 28.04  0  145 TRP   C CG  1 
ATOM   5011 C  CD1 . TRP   C  1 130 ? 13.088  -42.103 13.780  1.00 29.91  0  145 TRP   C CD1 1 
ATOM   5012 C  CD2 . TRP   C  1 130 ? 14.226  -43.699 12.711  1.00 27.75  0  145 TRP   C CD2 1 
ATOM   5013 N  NE1 . TRP   C  1 130 ? 13.456  -43.043 14.707  1.00 32.53  0  145 TRP   C NE1 1 
ATOM   5014 C  CE2 . TRP   C  1 130 ? 14.165  -44.031 14.084  1.00 30.28  0  145 TRP   C CE2 1 
ATOM   5015 C  CE3 . TRP   C  1 130 ? 14.851  -44.579 11.821  1.00 24.74  0  145 TRP   C CE3 1 
ATOM   5016 C  CZ2 . TRP   C  1 130 ? 14.748  -45.190 14.591  1.00 27.73  0  145 TRP   C CZ2 1 
ATOM   5017 C  CZ3 . TRP   C  1 130 ? 15.435  -45.721 12.324  1.00 27.75  0  145 TRP   C CZ3 1 
ATOM   5018 C  CH2 . TRP   C  1 130 ? 15.398  -46.009 13.696  1.00 27.02  0  145 TRP   C CH2 1 
ATOM   5019 N  N   . GLY   C  1 131 ? 11.422  -41.373 8.199   1.00 28.70  0  146 GLY   C N   1 
ATOM   5020 C  CA  . GLY   C  1 131 ? 11.297  -40.545 6.983   1.00 28.53  0  146 GLY   C CA  1 
ATOM   5021 C  C   . GLY   C  1 131 ? 10.180  -39.508 7.084   1.00 27.93  0  146 GLY   C C   1 
ATOM   5022 O  O   . GLY   C  1 131 ? 9.455   -39.454 8.105   1.00 31.17  0  146 GLY   C O   1 
ATOM   5023 N  N   . ASP   C  1 132 ? 10.021  -38.745 6.008   1.00 27.63  0  147 ASP   C N   1 
ATOM   5024 C  CA  . ASP   C  1 132 ? 9.012   -37.685 5.842   1.00 27.78  0  147 ASP   C CA  1 
ATOM   5025 C  C   . ASP   C  1 132 ? 7.601   -38.223 6.146   1.00 27.77  0  147 ASP   C C   1 
ATOM   5026 O  O   . ASP   C  1 132 ? 7.280   -39.381 5.827   1.00 24.83  0  147 ASP   C O   1 
ATOM   5027 C  CB  . ASP   C  1 132 ? 9.139   -37.082 4.445   1.00 26.76  0  147 ASP   C CB  1 
ATOM   5028 C  CG  . ASP   C  1 132 ? 10.385  -36.221 4.240   1.00 26.20  0  147 ASP   C CG  1 
ATOM   5029 O  OD1 . ASP   C  1 132 ? 11.183  -36.057 5.160   1.00 29.06  0  147 ASP   C OD1 1 
ATOM   5030 O  OD2 . ASP   C  1 132 ? 10.549  -35.740 3.142   1.00 30.14  -1 147 ASP   C OD2 1 
ATOM   5031 N  N   . VAL   C  1 133 ? 6.768   -37.371 6.726   1.00 28.23  0  148 VAL   C N   1 
ATOM   5032 C  CA  . VAL   C  1 133 ? 5.374   -37.710 7.136   1.00 30.84  0  148 VAL   C CA  1 
ATOM   5033 C  C   . VAL   C  1 133 ? 4.408   -37.331 6.009   1.00 29.52  0  148 VAL   C C   1 
ATOM   5034 O  O   . VAL   C  1 133 ? 3.238   -37.667 6.119   1.00 29.86  0  148 VAL   C O   1 
ATOM   5035 C  CB  . VAL   C  1 133 ? 5.020   -37.039 8.477   1.00 35.44  0  148 VAL   C CB  1 
ATOM   5036 C  CG1 . VAL   C  1 133 ? 5.957   -37.512 9.578   1.00 36.91  0  148 VAL   C CG1 1 
ATOM   5037 C  CG2 . VAL   C  1 133 ? 5.029   -35.515 8.410   1.00 34.88  0  148 VAL   C CG2 1 
ATOM   5038 N  N   . ASP   C  1 134 ? 4.899   -36.710 4.929   1.00 32.20  0  149 ASP   C N   1 
ATOM   5039 C  CA  . ASP   C  1 134 ? 4.156   -36.472 3.664   1.00 30.67  0  149 ASP   C CA  1 
ATOM   5040 C  C   . ASP   C  1 134 ? 5.146   -35.934 2.628   1.00 32.08  0  149 ASP   C C   1 
ATOM   5041 O  O   . ASP   C  1 134 ? 6.328   -35.718 3.003   1.00 30.14  0  149 ASP   C O   1 
ATOM   5042 C  CB  . ASP   C  1 134 ? 2.967   -35.536 3.876   1.00 36.13  0  149 ASP   C CB  1 
ATOM   5043 C  CG  . ASP   C  1 134 ? 1.824   -35.723 2.880   1.00 43.93  0  149 ASP   C CG  1 
ATOM   5044 O  OD1 . ASP   C  1 134 ? 2.033   -36.367 1.803   1.00 44.65  0  149 ASP   C OD1 1 
ATOM   5045 O  OD2 . ASP   C  1 134 ? 0.754   -35.186 3.157   1.00 55.38  -1 149 ASP   C OD2 1 
ATOM   5046 N  N   . ASN   C  1 135 ? 4.715   -35.737 1.377   1.00 31.91  0  150 ASN   C N   1 
ATOM   5047 C  CA  . ASN   C  1 135 ? 5.590   -35.172 0.313   1.00 36.11  0  150 ASN   C CA  1 
ATOM   5048 C  C   . ASN   C  1 135 ? 6.222   -33.865 0.812   1.00 35.71  0  150 ASN   C C   1 
ATOM   5049 O  O   . ASN   C  1 135 ? 5.489   -32.991 1.238   1.00 35.80  0  150 ASN   C O   1 
ATOM   5050 C  CB  . ASN   C  1 135 ? 4.835   -34.996 -1.008  1.00 37.08  0  150 ASN   C CB  1 
ATOM   5051 C  CG  . ASN   C  1 135 ? 4.338   -36.325 -1.544  1.00 40.67  0  150 ASN   C CG  1 
ATOM   5052 O  OD1 . ASN   C  1 135 ? 5.124   -37.193 -1.931  1.00 38.84  0  150 ASN   C OD1 1 
ATOM   5053 N  ND2 . ASN   C  1 135 ? 3.032   -36.504 -1.556  1.00 41.76  0  150 ASN   C ND2 1 
ATOM   5054 N  N   . ASP   C  1 136 ? 7.549   -33.793 0.823   1.00 35.77  0  151 ASP   C N   1 
ATOM   5055 C  CA  . ASP   C  1 136 ? 8.362   -32.626 1.258   1.00 44.05  0  151 ASP   C CA  1 
ATOM   5056 C  C   . ASP   C  1 136 ? 7.935   -32.115 2.650   1.00 45.33  0  151 ASP   C C   1 
ATOM   5057 O  O   . ASP   C  1 136 ? 7.957   -30.903 2.869   1.00 41.56  0  151 ASP   C O   1 
ATOM   5058 C  CB  . ASP   C  1 136 ? 8.283   -31.533 0.194   1.00 51.74  0  151 ASP   C CB  1 
ATOM   5059 C  CG  . ASP   C  1 136 ? 9.528   -30.658 0.205   1.00 57.65  0  151 ASP   C CG  1 
ATOM   5060 O  OD1 . ASP   C  1 136 ? 10.626  -31.166 -0.118  1.00 62.11  0  151 ASP   C OD1 1 
ATOM   5061 O  OD2 . ASP   C  1 136 ? 9.402   -29.487 0.577   1.00 63.78  -1 151 ASP   C OD2 1 
ATOM   5062 N  N   . GLU   C  1 137 ? 7.536   -33.008 3.546   1.00 40.52  0  152 GLU   C N   1 
ATOM   5063 C  CA  . GLU   C  1 137 ? 7.213   -32.678 4.953   1.00 42.72  0  152 GLU   C CA  1 
ATOM   5064 C  C   . GLU   C  1 137 ? 8.109   -33.542 5.853   1.00 35.75  0  152 GLU   C C   1 
ATOM   5065 O  O   . GLU   C  1 137 ? 7.829   -34.761 5.984   1.00 28.28  0  152 GLU   C O   1 
ATOM   5066 C  CB  . GLU   C  1 137 ? 5.735   -32.947 5.219   1.00 49.14  0  152 GLU   C CB  1 
ATOM   5067 C  CG  . GLU   C  1 137 ? 4.811   -31.787 4.918   1.00 59.20  0  152 GLU   C CG  1 
ATOM   5068 C  CD  . GLU   C  1 137 ? 3.412   -31.948 5.512   1.00 64.19  0  152 GLU   C CD  1 
ATOM   5069 O  OE1 . GLU   C  1 137 ? 2.468   -31.377 4.932   1.00 65.34  0  152 GLU   C OE1 1 
ATOM   5070 O  OE2 . GLU   C  1 137 ? 3.262   -32.632 6.564   1.00 59.30  -1 152 GLU   C OE2 1 
ATOM   5071 N  N   . ARG   C  1 138 ? 9.120   -32.930 6.460   1.00 32.02  0  153 ARG   C N   1 
ATOM   5072 C  CA  . ARG   C  1 138 ? 10.077  -33.580 7.398   1.00 37.22  0  153 ARG   C CA  1 
ATOM   5073 C  C   . ARG   C  1 138 ? 9.343   -34.171 8.615   1.00 31.16  0  153 ARG   C C   1 
ATOM   5074 O  O   . ARG   C  1 138 ? 8.341   -33.602 9.064   1.00 28.04  0  153 ARG   C O   1 
ATOM   5075 C  CB  . ARG   C  1 138 ? 11.116  -32.595 7.940   1.00 38.67  0  153 ARG   C CB  1 
ATOM   5076 C  CG  . ARG   C  1 138 ? 12.050  -31.978 6.910   1.00 42.41  0  153 ARG   C CG  1 
ATOM   5077 C  CD  . ARG   C  1 138 ? 12.970  -32.961 6.222   1.00 46.04  0  153 ARG   C CD  1 
ATOM   5078 N  NE  . ARG   C  1 138 ? 12.406  -33.493 4.978   1.00 46.95  0  153 ARG   C NE  1 
ATOM   5079 C  CZ  . ARG   C  1 138 ? 12.270  -32.820 3.807   1.00 57.12  0  153 ARG   C CZ  1 
ATOM   5080 N  NH1 . ARG   C  1 138 ? 12.632  -31.545 3.708   1.00 56.33  1  153 ARG   C NH1 1 
ATOM   5081 N  NH2 . ARG   C  1 138 ? 11.760  -33.417 2.732   1.00 43.46  0  153 ARG   C NH2 1 
ATOM   5082 N  N   . LEU   C  1 139 ? 9.842   -35.296 9.118   1.00 29.32  0  154 LEU   C N   1 
ATOM   5083 C  CA  . LEU   C  1 139 ? 9.491   -35.796 10.464  1.00 28.78  0  154 LEU   C CA  1 
ATOM   5084 C  C   . LEU   C  1 139 ? 9.940   -34.700 11.429  1.00 28.43  0  154 LEU   C C   1 
ATOM   5085 O  O   . LEU   C  1 139 ? 11.124  -34.341 11.420  1.00 31.14  0  154 LEU   C O   1 
ATOM   5086 C  CB  . LEU   C  1 139 ? 10.241  -37.107 10.763  1.00 26.77  0  154 LEU   C CB  1 
ATOM   5087 C  CG  . LEU   C  1 139 ? 9.896   -37.781 12.096  1.00 26.66  0  154 LEU   C CG  1 
ATOM   5088 C  CD1 . LEU   C  1 139 ? 8.424   -38.188 12.165  1.00 29.78  0  154 LEU   C CD1 1 
ATOM   5089 C  CD2 . LEU   C  1 139 ? 10.750  -39.006 12.341  1.00 28.63  0  154 LEU   C CD2 1 
ATOM   5090 N  N   . PRO   C  1 140 ? 9.044   -34.123 12.255  1.00 30.96  0  155 PRO   C N   1 
ATOM   5091 C  CA  . PRO   C  1 140 ? 9.465   -33.136 13.246  1.00 30.69  0  155 PRO   C CA  1 
ATOM   5092 C  C   . PRO   C  1 140 ? 10.272  -33.698 14.409  1.00 31.28  0  155 PRO   C C   1 
ATOM   5093 O  O   . PRO   C  1 140 ? 10.132  -34.861 14.779  1.00 29.12  0  155 PRO   C O   1 
ATOM   5094 C  CB  . PRO   C  1 140 ? 8.174   -32.532 13.811  1.00 32.83  0  155 PRO   C CB  1 
ATOM   5095 C  CG  . PRO   C  1 140 ? 7.013   -33.334 13.212  1.00 36.93  0  155 PRO   C CG  1 
ATOM   5096 C  CD  . PRO   C  1 140 ? 7.591   -34.363 12.264  1.00 32.77  0  155 PRO   C CD  1 
ATOM   5097 N  N   . PRO   C  1 141 ? 11.119  -32.877 15.068  1.00 35.83  0  156 PRO   C N   1 
ATOM   5098 C  CA  . PRO   C  1 141 ? 11.666  -33.236 16.375  1.00 31.08  0  156 PRO   C CA  1 
ATOM   5099 C  C   . PRO   C  1 141 ? 10.481  -33.551 17.286  1.00 29.34  0  156 PRO   C C   1 
ATOM   5100 O  O   . PRO   C  1 141 ? 9.404   -32.954 17.138  1.00 27.90  0  156 PRO   C O   1 
ATOM   5101 C  CB  . PRO   C  1 141 ? 12.400  -31.991 16.885  1.00 35.32  0  156 PRO   C CB  1 
ATOM   5102 C  CG  . PRO   C  1 141 ? 12.491  -31.036 15.709  1.00 33.57  0  156 PRO   C CG  1 
ATOM   5103 C  CD  . PRO   C  1 141 ? 11.559  -31.541 14.629  1.00 37.20  0  156 PRO   C CD  1 
ATOM   5104 N  N   . PRO   C  1 142 ? 10.599  -34.495 18.234  1.00 27.65  0  157 PRO   C N   1 
ATOM   5105 C  CA  . PRO   C  1 142 ? 11.839  -35.234 18.513  1.00 26.39  0  157 PRO   C CA  1 
ATOM   5106 C  C   . PRO   C  1 142 ? 12.100  -36.532 17.716  1.00 28.59  0  157 PRO   C C   1 
ATOM   5107 O  O   . PRO   C  1 142 ? 12.810  -37.392 18.203  1.00 27.32  0  157 PRO   C O   1 
ATOM   5108 C  CB  . PRO   C  1 142 ? 11.650  -35.549 19.997  1.00 28.33  0  157 PRO   C CB  1 
ATOM   5109 C  CG  . PRO   C  1 142 ? 10.159  -35.781 20.138  1.00 29.92  0  157 PRO   C CG  1 
ATOM   5110 C  CD  . PRO   C  1 142 ? 9.481   -34.884 19.111  1.00 29.85  0  157 PRO   C CD  1 
ATOM   5111 N  N   . PHE   C  1 143 ? 11.593  -36.639 16.494  1.00 29.64  0  158 PHE   C N   1 
ATOM   5112 C  CA  . PHE   C  1 143 ? 11.968  -37.700 15.510  1.00 28.32  0  158 PHE   C CA  1 
ATOM   5113 C  C   . PHE   C  1 143 ? 11.647  -39.099 16.050  1.00 26.99  0  158 PHE   C C   1 
ATOM   5114 O  O   . PHE   C  1 143 ? 12.528  -39.956 16.189  1.00 25.09  0  158 PHE   C O   1 
ATOM   5115 C  CB  . PHE   C  1 143 ? 13.458  -37.601 15.180  1.00 27.32  0  158 PHE   C CB  1 
ATOM   5116 C  CG  . PHE   C  1 143 ? 13.996  -36.226 14.917  1.00 30.28  0  158 PHE   C CG  1 
ATOM   5117 C  CD1 . PHE   C  1 143 ? 13.685  -35.556 13.739  1.00 30.44  0  158 PHE   C CD1 1 
ATOM   5118 C  CD2 . PHE   C  1 143 ? 14.907  -35.641 15.799  1.00 32.76  0  158 PHE   C CD2 1 
ATOM   5119 C  CE1 . PHE   C  1 143 ? 14.227  -34.301 13.478  1.00 32.55  0  158 PHE   C CE1 1 
ATOM   5120 C  CE2 . PHE   C  1 143 ? 15.437  -34.393 15.535  1.00 31.91  0  158 PHE   C CE2 1 
ATOM   5121 C  CZ  . PHE   C  1 143 ? 15.098  -33.726 14.376  1.00 33.07  0  158 PHE   C CZ  1 
ATOM   5122 N  N   . PRO   C  1 144 ? 10.372  -39.380 16.389  1.00 25.71  0  159 PRO   C N   1 
ATOM   5123 C  CA  . PRO   C  1 144 ? 10.002  -40.690 16.914  1.00 27.54  0  159 PRO   C CA  1 
ATOM   5124 C  C   . PRO   C  1 144 ? 10.010  -41.708 15.759  1.00 25.93  0  159 PRO   C C   1 
ATOM   5125 O  O   . PRO   C  1 144 ? 9.631   -41.354 14.638  1.00 26.97  0  159 PRO   C O   1 
ATOM   5126 C  CB  . PRO   C  1 144 ? 8.581   -40.460 17.447  1.00 29.55  0  159 PRO   C CB  1 
ATOM   5127 C  CG  . PRO   C  1 144 ? 8.033   -39.379 16.515  1.00 30.96  0  159 PRO   C CG  1 
ATOM   5128 C  CD  . PRO   C  1 144 ? 9.220   -38.482 16.244  1.00 27.27  0  159 PRO   C CD  1 
ATOM   5129 N  N   . LEU   C  1 145 ? 10.448  -42.944 16.019  1.00 28.83  0  160 LEU   C N   1 
ATOM   5130 C  CA  . LEU   C  1 145 ? 10.253  -44.051 15.045  1.00 25.84  0  160 LEU   C CA  1 
ATOM   5131 C  C   . LEU   C  1 145 ? 8.754   -44.198 14.747  1.00 27.48  0  160 LEU   C C   1 
ATOM   5132 O  O   . LEU   C  1 145 ? 7.952   -44.351 15.711  1.00 30.20  0  160 LEU   C O   1 
ATOM   5133 C  CB  . LEU   C  1 145 ? 10.857  -45.353 15.550  1.00 25.97  0  160 LEU   C CB  1 
ATOM   5134 C  CG  . LEU   C  1 145 ? 10.627  -46.535 14.600  1.00 27.62  0  160 LEU   C CG  1 
ATOM   5135 C  CD1 . LEU   C  1 145 ? 11.318  -46.290 13.261  1.00 29.49  0  160 LEU   C CD1 1 
ATOM   5136 C  CD2 . LEU   C  1 145 ? 11.127  -47.823 15.225  1.00 31.49  0  160 LEU   C CD2 1 
ATOM   5137 N  N   . LYS   C  1 146 ? 8.365   -44.171 13.465  1.00 26.70  0  161 LYS   C N   1 
ATOM   5138 C  CA  . LYS   C  1 146 ? 6.932   -44.303 13.060  1.00 27.88  0  161 LYS   C CA  1 
ATOM   5139 C  C   . LYS   C  1 146 ? 6.687   -45.677 12.402  1.00 29.04  0  161 LYS   C C   1 
ATOM   5140 O  O   . LYS   C  1 146 ? 7.644   -46.337 11.948  1.00 27.96  0  161 LYS   C O   1 
ATOM   5141 C  CB  . LYS   C  1 146 ? 6.475   -43.175 12.140  1.00 28.79  0  161 LYS   C CB  1 
ATOM   5142 C  CG  . LYS   C  1 146 ? 6.671   -41.744 12.647  1.00 35.72  0  161 LYS   C CG  1 
ATOM   5143 C  CD  . LYS   C  1 146 ? 5.455   -41.068 13.183  1.00 41.13  0  161 LYS   C CD  1 
ATOM   5144 C  CE  . LYS   C  1 146 ? 4.509   -40.573 12.125  1.00 45.41  0  161 LYS   C CE  1 
ATOM   5145 N  NZ  . LYS   C  1 146 ? 3.434   -39.771 12.772  1.00 51.44  1  161 LYS   C NZ  1 
ATOM   5146 N  N   . GLN   C  1 147 ? 5.431   -46.094 12.367  1.00 26.07  0  162 GLN   C N   1 
ATOM   5147 C  CA  . GLN   C  1 147 ? 4.980   -47.398 11.831  1.00 27.34  0  162 GLN   C CA  1 
ATOM   5148 C  C   . GLN   C  1 147 ? 3.679   -47.121 11.086  1.00 29.44  0  162 GLN   C C   1 
ATOM   5149 O  O   . GLN   C  1 147 ? 2.956   -46.200 11.489  1.00 28.25  0  162 GLN   C O   1 
ATOM   5150 C  CB  . GLN   C  1 147 ? 4.772   -48.384 12.984  1.00 29.98  0  162 GLN   C CB  1 
ATOM   5151 C  CG  . GLN   C  1 147 ? 3.666   -47.961 13.976  1.00 32.46  0  162 GLN   C CG  1 
ATOM   5152 C  CD  . GLN   C  1 147 ? 3.416   -48.955 15.094  1.00 31.46  0  162 GLN   C CD  1 
ATOM   5153 O  OE1 . GLN   C  1 147 ? 4.327   -49.571 15.620  1.00 28.51  0  162 GLN   C OE1 1 
ATOM   5154 N  NE2 . GLN   C  1 147 ? 2.177   -49.106 15.496  1.00 31.23  0  162 GLN   C NE2 1 
ATOM   5155 N  N   . VAL   C  1 148 ? 3.415   -47.852 10.022  1.00 29.95  0  163 VAL   C N   1 
ATOM   5156 C  CA  . VAL   C  1 148 ? 2.087   -47.832 9.367   1.00 30.19  0  163 VAL   C CA  1 
ATOM   5157 C  C   . VAL   C  1 148 ? 1.804   -49.222 8.800   1.00 29.31  0  163 VAL   C C   1 
ATOM   5158 O  O   . VAL   C  1 148 ? 2.729   -49.870 8.303   1.00 29.41  0  163 VAL   C O   1 
ATOM   5159 C  CB  . VAL   C  1 148 ? 2.013   -46.695 8.331   1.00 27.23  0  163 VAL   C CB  1 
ATOM   5160 C  CG1 . VAL   C  1 148 ? 2.898   -46.941 7.118   1.00 27.69  0  163 VAL   C CG1 1 
ATOM   5161 C  CG2 . VAL   C  1 148 ? 0.579   -46.408 7.946   1.00 26.77  0  163 VAL   C CG2 1 
ATOM   5162 N  N   . LYS   C  1 149 ? 0.560   -49.660 8.936   1.00 36.41  0  164 LYS   C N   1 
ATOM   5163 C  CA  . LYS   C  1 149 ? 0.047   -50.915 8.334   1.00 34.90  0  164 LYS   C CA  1 
ATOM   5164 C  C   . LYS   C  1 149 ? -0.289  -50.604 6.875   1.00 32.80  0  164 LYS   C C   1 
ATOM   5165 O  O   . LYS   C  1 149 ? -1.028  -49.655 6.631   1.00 31.83  0  164 LYS   C O   1 
ATOM   5166 C  CB  . LYS   C  1 149 ? -1.157  -51.442 9.129   1.00 37.92  0  164 LYS   C CB  1 
ATOM   5167 C  CG  . LYS   C  1 149 ? -1.805  -52.719 8.592   1.00 39.41  0  164 LYS   C CG  1 
ATOM   5168 C  CD  . LYS   C  1 149 ? -2.699  -53.468 9.582   1.00 45.19  0  164 LYS   C CD  1 
ATOM   5169 C  CE  . LYS   C  1 149 ? -3.832  -52.639 10.144  1.00 50.67  0  164 LYS   C CE  1 
ATOM   5170 N  NZ  . LYS   C  1 149 ? -4.707  -52.106 9.071   1.00 54.27  1  164 LYS   C NZ  1 
ATOM   5171 N  N   . VAL   C  1 150 ? 0.263   -51.382 5.943   1.00 33.25  0  165 VAL   C N   1 
ATOM   5172 C  CA  . VAL   C  1 150 ? 0.089   -51.212 4.474   1.00 31.51  0  165 VAL   C CA  1 
ATOM   5173 C  C   . VAL   C  1 150 ? -0.276  -52.576 3.902   1.00 35.26  0  165 VAL   C C   1 
ATOM   5174 O  O   . VAL   C  1 150 ? 0.389   -53.590 4.162   1.00 32.72  0  165 VAL   C O   1 
ATOM   5175 C  CB  . VAL   C  1 150 ? 1.343   -50.638 3.785   1.00 30.57  0  165 VAL   C CB  1 
ATOM   5176 C  CG1 . VAL   C  1 150 ? 1.557   -49.176 4.138   1.00 31.90  0  165 VAL   C CG1 1 
ATOM   5177 C  CG2 . VAL   C  1 150 ? 2.610   -51.428 4.076   1.00 29.54  0  165 VAL   C CG2 1 
ATOM   5178 N  N   . PRO   C  1 151 ? -1.357  -52.646 3.110   1.00 37.77  0  166 PRO   C N   1 
ATOM   5179 C  CA  . PRO   C  1 151 ? -1.736  -53.899 2.468   1.00 43.01  0  166 PRO   C CA  1 
ATOM   5180 C  C   . PRO   C  1 151 ? -0.780  -54.207 1.299   1.00 39.23  0  166 PRO   C C   1 
ATOM   5181 O  O   . PRO   C  1 151 ? -0.488  -53.318 0.500   1.00 35.89  0  166 PRO   C O   1 
ATOM   5182 C  CB  . PRO   C  1 151 ? -3.170  -53.597 2.009   1.00 42.76  0  166 PRO   C CB  1 
ATOM   5183 C  CG  . PRO   C  1 151 ? -3.154  -52.105 1.707   1.00 45.83  0  166 PRO   C CG  1 
ATOM   5184 C  CD  . PRO   C  1 151 ? -2.255  -51.529 2.769   1.00 41.89  0  166 PRO   C CD  1 
ATOM   5185 N  N   . ILE   C  1 152 ? -0.334  -55.461 1.213   1.00 40.86  0  167 ILE   C N   1 
ATOM   5186 C  CA  . ILE   C  1 152 ? 0.362   -56.023 0.014   1.00 39.36  0  167 ILE   C CA  1 
ATOM   5187 C  C   . ILE   C  1 152 ? -0.592  -55.989 -1.175  1.00 35.15  0  167 ILE   C C   1 
ATOM   5188 O  O   . ILE   C  1 152 ? -1.803  -56.249 -1.017  1.00 36.39  0  167 ILE   C O   1 
ATOM   5189 C  CB  . ILE   C  1 152 ? 0.843   -57.455 0.268   1.00 43.68  0  167 ILE   C CB  1 
ATOM   5190 C  CG1 . ILE   C  1 152 ? 1.931   -57.480 1.330   1.00 44.76  0  167 ILE   C CG1 1 
ATOM   5191 C  CG2 . ILE   C  1 152 ? 1.304   -58.162 -1.013  1.00 51.48  0  167 ILE   C CG2 1 
ATOM   5192 C  CD1 . ILE   C  1 152 ? 3.271   -56.999 0.869   1.00 46.11  0  167 ILE   C CD1 1 
ATOM   5193 N  N   . MET   C  1 153 ? -0.056  -55.630 -2.329  1.00 35.25  0  168 MET   C N   1 
ATOM   5194 C  CA  . MET   C  1 153 ? -0.789  -55.649 -3.609  1.00 39.01  0  168 MET   C CA  1 
ATOM   5195 C  C   . MET   C  1 153 ? 0.014   -56.469 -4.612  1.00 35.92  0  168 MET   C C   1 
ATOM   5196 O  O   . MET   C  1 153 ? 1.284   -56.407 -4.617  1.00 39.36  0  168 MET   C O   1 
ATOM   5197 C  CB  . MET   C  1 153 ? -1.074  -54.226 -4.079  1.00 45.89  0  168 MET   C CB  1 
ATOM   5198 C  CG  . MET   C  1 153 ? -2.136  -53.587 -3.167  1.00 55.61  0  168 MET   C CG  1 
ATOM   5199 S  SD  . MET   C  1 153 ? -2.505  -51.848 -3.480  1.00 67.31  0  168 MET   C SD  1 
ATOM   5200 C  CE  . MET   C  1 153 ? -3.490  -51.953 -4.971  1.00 61.29  0  168 MET   C CE  1 
ATOM   5201 N  N   . GLU   C  1 154 ? -0.710  -57.261 -5.396  1.00 34.36  0  169 GLU   C N   1 
ATOM   5202 C  CA  . GLU   C  1 154 ? -0.146  -58.085 -6.491  1.00 38.50  0  169 GLU   C CA  1 
ATOM   5203 C  C   . GLU   C  1 154 ? 0.614   -57.166 -7.459  1.00 32.95  0  169 GLU   C C   1 
ATOM   5204 O  O   . GLU   C  1 154 ? 0.139   -56.061 -7.756  1.00 27.79  0  169 GLU   C O   1 
ATOM   5205 C  CB  . GLU   C  1 154 ? -1.281  -58.847 -7.175  1.00 45.86  0  169 GLU   C CB  1 
ATOM   5206 C  CG  . GLU   C  1 154 ? -0.856  -59.944 -8.126  1.00 52.81  0  169 GLU   C CG  1 
ATOM   5207 C  CD  . GLU   C  1 154 ? -2.066  -60.481 -8.874  1.00 60.75  0  169 GLU   C CD  1 
ATOM   5208 O  OE1 . GLU   C  1 154 ? -2.538  -61.568 -8.527  1.00 62.28  0  169 GLU   C OE1 1 
ATOM   5209 O  OE2 . GLU   C  1 154 ? -2.580  -59.764 -9.744  1.00 66.03  -1 169 GLU   C OE2 1 
ATOM   5210 N  N   . ASN   C  1 155 ? 1.774   -57.609 -7.902  1.00 32.67  0  170 ASN   C N   1 
ATOM   5211 C  CA  . ASN   C  1 155 ? 2.613   -56.872 -8.876  1.00 33.60  0  170 ASN   C CA  1 
ATOM   5212 C  C   . ASN   C  1 155 ? 1.805   -56.480 -10.106 1.00 35.04  0  170 ASN   C C   1 
ATOM   5213 O  O   . ASN   C  1 155 ? 2.010   -55.374 -10.560 1.00 35.63  0  170 ASN   C O   1 
ATOM   5214 C  CB  . ASN   C  1 155 ? 3.853   -57.658 -9.285  1.00 37.18  0  170 ASN   C CB  1 
ATOM   5215 C  CG  . ASN   C  1 155 ? 4.995   -57.395 -8.341  1.00 37.93  0  170 ASN   C CG  1 
ATOM   5216 O  OD1 . ASN   C  1 155 ? 4.763   -57.087 -7.176  1.00 44.02  0  170 ASN   C OD1 1 
ATOM   5217 N  ND2 . ASN   C  1 155 ? 6.219   -57.536 -8.820  1.00 32.12  0  170 ASN   C ND2 1 
ATOM   5218 N  N   . HIS   C  1 156 ? 0.928   -57.338 -10.618 1.00 34.18  0  171 HIS   C N   1 
ATOM   5219 C  CA  . HIS   C  1 156 ? 0.190   -57.058 -11.861 1.00 34.34  0  171 HIS   C CA  1 
ATOM   5220 C  C   . HIS   C  1 156 ? -0.736  -55.852 -11.634 1.00 35.30  0  171 HIS   C C   1 
ATOM   5221 O  O   . HIS   C  1 156 ? -0.707  -54.936 -12.484 1.00 34.87  0  171 HIS   C O   1 
ATOM   5222 C  CB  . HIS   C  1 156 ? -0.496  -58.316 -12.391 1.00 37.53  0  171 HIS   C CB  1 
ATOM   5223 C  CG  . HIS   C  1 156 ? -1.186  -58.087 -13.685 1.00 42.76  0  171 HIS   C CG  1 
ATOM   5224 N  ND1 . HIS   C  1 156 ? -0.540  -58.183 -14.895 1.00 46.93  0  171 HIS   C ND1 1 
ATOM   5225 C  CD2 . HIS   C  1 156 ? -2.443  -57.697 -13.953 1.00 47.70  0  171 HIS   C CD2 1 
ATOM   5226 C  CE1 . HIS   C  1 156 ? -1.375  -57.873 -15.859 1.00 52.33  0  171 HIS   C CE1 1 
ATOM   5227 N  NE2 . HIS   C  1 156 ? -2.558  -57.593 -15.307 1.00 51.34  0  171 HIS   C NE2 1 
ATOM   5228 N  N   . ILE   C  1 157 ? -1.402  -55.772 -10.486 1.00 32.69  0  172 ILE   C N   1 
ATOM   5229 C  CA  . ILE   C  1 157 ? -2.306  -54.642 -10.135 1.00 32.87  0  172 ILE   C CA  1 
ATOM   5230 C  C   . ILE   C  1 157 ? -1.503  -53.340 -9.968  1.00 32.49  0  172 ILE   C C   1 
ATOM   5231 O  O   . ILE   C  1 157 ? -1.957  -52.272 -10.433 1.00 38.07  0  172 ILE   C O   1 
ATOM   5232 C  CB  . ILE   C  1 157 ? -3.101  -54.949 -8.857  1.00 36.01  0  172 ILE   C CB  1 
ATOM   5233 C  CG1 . ILE   C  1 157 ? -4.038  -56.141 -9.052  1.00 39.15  0  172 ILE   C CG1 1 
ATOM   5234 C  CG2 . ILE   C  1 157 ? -3.874  -53.722 -8.373  1.00 30.92  0  172 ILE   C CG2 1 
ATOM   5235 C  CD1 . ILE   C  1 157 ? -5.001  -56.029 -10.215 1.00 40.40  0  172 ILE   C CD1 1 
ATOM   5236 N  N   A CYS   C  1 158 ? -0.371  -53.422 -9.295  0.50 30.69  0  173 CYS   C N   1 
ATOM   5237 N  N   B CYS   C  1 158 ? -0.361  -53.409 -9.290  0.50 32.09  0  173 CYS   C N   1 
ATOM   5238 C  CA  A CYS   C  1 158 ? 0.497   -52.264 -8.995  0.50 31.03  0  173 CYS   C CA  1 
ATOM   5239 C  CA  B CYS   C  1 158 ? 0.484   -52.225 -8.993  0.50 33.48  0  173 CYS   C CA  1 
ATOM   5240 C  C   A CYS   C  1 158 ? 1.085   -51.718 -10.302 0.50 30.45  0  173 CYS   C C   1 
ATOM   5241 C  C   B CYS   C  1 158 ? 1.098   -51.709 -10.298 0.50 31.69  0  173 CYS   C C   1 
ATOM   5242 O  O   A CYS   C  1 158 ? 1.057   -50.470 -10.498 0.50 26.91  0  173 CYS   C O   1 
ATOM   5243 O  O   B CYS   C  1 158 ? 1.097   -50.461 -10.487 0.50 27.82  0  173 CYS   C O   1 
ATOM   5244 C  CB  A CYS   C  1 158 ? 1.567   -52.690 -8.011  0.50 33.16  0  173 CYS   C CB  1 
ATOM   5245 C  CB  B CYS   C  1 158 ? 1.533   -52.530 -7.934  0.50 37.08  0  173 CYS   C CB  1 
ATOM   5246 S  SG  A CYS   C  1 158 ? 2.660   -51.355 -7.488  0.50 34.00  0  173 CYS   C SG  1 
ATOM   5247 S  SG  B CYS   C  1 158 ? 0.816   -52.672 -6.270  0.50 44.76  0  173 CYS   C SG  1 
ATOM   5248 N  N   . ASP   C  1 159 ? 1.549   -52.619 -11.173 1.00 30.25  0  174 ASP   C N   1 
ATOM   5249 C  CA  . ASP   C  1 159 ? 2.067   -52.284 -12.528 1.00 31.12  0  174 ASP   C CA  1 
ATOM   5250 C  C   . ASP   C  1 159 ? 0.956   -51.568 -13.308 1.00 30.61  0  174 ASP   C C   1 
ATOM   5251 O  O   . ASP   C  1 159 ? 1.218   -50.489 -13.853 1.00 28.15  0  174 ASP   C O   1 
ATOM   5252 C  CB  . ASP   C  1 159 ? 2.567   -53.507 -13.295 1.00 31.69  0  174 ASP   C CB  1 
ATOM   5253 C  CG  . ASP   C  1 159 ? 3.306   -53.140 -14.578 1.00 31.82  0  174 ASP   C CG  1 
ATOM   5254 O  OD1 . ASP   C  1 159 ? 4.337   -52.503 -14.494 1.00 33.12  0  174 ASP   C OD1 1 
ATOM   5255 O  OD2 . ASP   C  1 159 ? 2.789   -53.422 -15.651 1.00 36.70  -1 174 ASP   C OD2 1 
ATOM   5256 N  N   . ALA   C  1 160 ? -0.262  -52.110 -13.284 1.00 28.98  0  175 ALA   C N   1 
ATOM   5257 C  CA  . ALA   C  1 160 ? -1.438  -51.507 -13.948 1.00 30.48  0  175 ALA   C CA  1 
ATOM   5258 C  C   . ALA   C  1 160 ? -1.664  -50.096 -13.373 1.00 32.87  0  175 ALA   C C   1 
ATOM   5259 O  O   . ALA   C  1 160 ? -1.882  -49.167 -14.174 1.00 33.48  0  175 ALA   C O   1 
ATOM   5260 C  CB  . ALA   C  1 160 ? -2.649  -52.398 -13.829 1.00 28.48  0  175 ALA   C CB  1 
ATOM   5261 N  N   . LYS   C  1 161 ? -1.586  -49.895 -12.051 1.00 29.36  0  176 LYS   C N   1 
ATOM   5262 C  CA  . LYS   C  1 161 ? -1.835  -48.554 -11.452 1.00 29.34  0  176 LYS   C CA  1 
ATOM   5263 C  C   . LYS   C  1 161 ? -0.791  -47.557 -11.968 1.00 28.68  0  176 LYS   C C   1 
ATOM   5264 O  O   . LYS   C  1 161 ? -1.166  -46.438 -12.334 1.00 27.80  0  176 LYS   C O   1 
ATOM   5265 C  CB  . LYS   C  1 161 ? -1.854  -48.617 -9.926  1.00 31.15  0  176 LYS   C CB  1 
ATOM   5266 C  CG  . LYS   C  1 161 ? -3.114  -49.299 -9.398  1.00 34.55  0  176 LYS   C CG  1 
ATOM   5267 C  CD  . LYS   C  1 161 ? -3.297  -49.251 -7.906  1.00 36.00  0  176 LYS   C CD  1 
ATOM   5268 C  CE  . LYS   C  1 161 ? -4.733  -49.599 -7.566  1.00 42.64  0  176 LYS   C CE  1 
ATOM   5269 N  NZ  . LYS   C  1 161 ? -5.126  -49.134 -6.218  1.00 52.03  1  176 LYS   C NZ  1 
ATOM   5270 N  N   . TYR   C  1 162 ? 0.476   -47.951 -12.031 1.00 26.57  0  177 TYR   C N   1 
ATOM   5271 C  CA  . TYR   C  1 162 ? 1.555   -47.026 -12.463 1.00 28.66  0  177 TYR   C CA  1 
ATOM   5272 C  C   . TYR   C  1 162 ? 1.323   -46.572 -13.913 1.00 29.17  0  177 TYR   C C   1 
ATOM   5273 O  O   . TYR   C  1 162 ? 1.879   -45.506 -14.293 1.00 31.28  0  177 TYR   C O   1 
ATOM   5274 C  CB  . TYR   C  1 162 ? 2.945   -47.619 -12.209 1.00 24.90  0  177 TYR   C CB  1 
ATOM   5275 C  CG  . TYR   C  1 162 ? 3.521   -47.157 -10.895 1.00 25.56  0  177 TYR   C CG  1 
ATOM   5276 C  CD1 . TYR   C  1 162 ? 3.088   -47.714 -9.701  1.00 24.67  0  177 TYR   C CD1 1 
ATOM   5277 C  CD2 . TYR   C  1 162 ? 4.392   -46.075 -10.825 1.00 25.98  0  177 TYR   C CD2 1 
ATOM   5278 C  CE1 . TYR   C  1 162 ? 3.601   -47.301 -8.480  1.00 26.84  0  177 TYR   C CE1 1 
ATOM   5279 C  CE2 . TYR   C  1 162 ? 4.912   -45.649 -9.603  1.00 26.14  0  177 TYR   C CE2 1 
ATOM   5280 C  CZ  . TYR   C  1 162 ? 4.493   -46.243 -8.427  1.00 26.85  0  177 TYR   C CZ  1 
ATOM   5281 O  OH  . TYR   C  1 162 ? 4.900   -45.775 -7.214  1.00 26.38  0  177 TYR   C OH  1 
ATOM   5282 N  N   . HIS   C  1 163 ? 0.556   -47.339 -14.701 1.00 29.68  0  178 HIS   C N   1 
ATOM   5283 C  CA  . HIS   C  1 163 ? 0.214   -47.041 -16.116 1.00 29.00  0  178 HIS   C CA  1 
ATOM   5284 C  C   . HIS   C  1 163 ? -0.969  -46.073 -16.219 1.00 33.18  0  178 HIS   C C   1 
ATOM   5285 O  O   . HIS   C  1 163 ? -1.118  -45.459 -17.316 1.00 32.58  0  178 HIS   C O   1 
ATOM   5286 C  CB  . HIS   C  1 163 ? -0.041  -48.327 -16.921 1.00 30.04  0  178 HIS   C CB  1 
ATOM   5287 C  CG  . HIS   C  1 163 ? 1.204   -49.071 -17.268 1.00 30.38  0  178 HIS   C CG  1 
ATOM   5288 N  ND1 . HIS   C  1 163 ? 1.803   -49.962 -16.426 1.00 30.39  0  178 HIS   C ND1 1 
ATOM   5289 C  CD2 . HIS   C  1 163 ? 1.992   -49.031 -18.360 1.00 32.15  0  178 HIS   C CD2 1 
ATOM   5290 C  CE1 . HIS   C  1 163 ? 2.892   -50.439 -16.981 1.00 28.63  0  178 HIS   C CE1 1 
ATOM   5291 N  NE2 . HIS   C  1 163 ? 3.026   -49.895 -18.157 1.00 28.72  0  178 HIS   C NE2 1 
ATOM   5292 N  N   . LEU   C  1 164 ? -1.804  -45.957 -15.179 1.00 29.92  0  179 LEU   C N   1 
ATOM   5293 C  CA  . LEU   C  1 164 ? -2.966  -45.027 -15.196 1.00 36.44  0  179 LEU   C CA  1 
ATOM   5294 C  C   . LEU   C  1 164 ? -2.395  -43.607 -15.147 1.00 32.36  0  179 LEU   C C   1 
ATOM   5295 O  O   . LEU   C  1 164 ? -1.570  -43.369 -14.279 1.00 26.97  0  179 LEU   C O   1 
ATOM   5296 C  CB  . LEU   C  1 164 ? -3.923  -45.283 -14.020 1.00 35.91  0  179 LEU   C CB  1 
ATOM   5297 C  CG  . LEU   C  1 164 ? -4.947  -46.404 -14.170 1.00 41.58  0  179 LEU   C CG  1 
ATOM   5298 C  CD1 . LEU   C  1 164 ? -5.903  -46.182 -15.334 1.00 39.92  0  179 LEU   C CD1 1 
ATOM   5299 C  CD2 . LEU   C  1 164 ? -4.269  -47.732 -14.322 1.00 49.08  0  179 LEU   C CD2 1 
ATOM   5300 N  N   . GLY   C  1 165 ? -2.806  -42.723 -16.059 1.00 31.11  0  180 GLY   C N   1 
ATOM   5301 C  CA  . GLY   C  1 165 ? -2.328  -41.330 -16.102 1.00 31.88  0  180 GLY   C CA  1 
ATOM   5302 C  C   . GLY   C  1 165 ? -0.888  -41.268 -16.595 1.00 31.84  0  180 GLY   C C   1 
ATOM   5303 O  O   . GLY   C  1 165 ? -0.193  -40.282 -16.274 1.00 29.50  0  180 GLY   C O   1 
ATOM   5304 N  N   . ALA   C  1 166 ? -0.432  -42.296 -17.333 1.00 30.55  0  181 ALA   C N   1 
ATOM   5305 C  CA  . ALA   C  1 166 ? 0.936   -42.353 -17.887 1.00 31.18  0  181 ALA   C CA  1 
ATOM   5306 C  C   . ALA   C  1 166 ? 0.910   -42.630 -19.389 1.00 29.39  0  181 ALA   C C   1 
ATOM   5307 O  O   . ALA   C  1 166 ? -0.014  -43.267 -19.874 1.00 32.09  0  181 ALA   C O   1 
ATOM   5308 C  CB  . ALA   C  1 166 ? 1.769   -43.375 -17.165 1.00 29.99  0  181 ALA   C CB  1 
ATOM   5309 N  N   . TYR   C  1 167 ? 1.936   -42.158 -20.086 1.00 32.80  0  182 TYR   C N   1 
ATOM   5310 C  CA  . TYR   C  1 167 ? 2.148   -42.367 -21.545 1.00 29.88  0  182 TYR   C CA  1 
ATOM   5311 C  C   . TYR   C  1 167 ? 2.735   -43.768 -21.773 1.00 28.66  0  182 TYR   C C   1 
ATOM   5312 O  O   . TYR   C  1 167 ? 2.677   -44.256 -22.889 1.00 28.12  0  182 TYR   C O   1 
ATOM   5313 C  CB  . TYR   C  1 167 ? 3.089   -41.293 -22.106 1.00 29.64  0  182 TYR   C CB  1 
ATOM   5314 C  CG  . TYR   C  1 167 ? 2.547   -39.888 -22.069 1.00 31.40  0  182 TYR   C CG  1 
ATOM   5315 C  CD1 . TYR   C  1 167 ? 1.583   -39.486 -22.980 1.00 32.64  0  182 TYR   C CD1 1 
ATOM   5316 C  CD2 . TYR   C  1 167 ? 3.018   -38.941 -21.163 1.00 32.16  0  182 TYR   C CD2 1 
ATOM   5317 C  CE1 . TYR   C  1 167 ? 1.102   -38.183 -23.000 1.00 34.34  0  182 TYR   C CE1 1 
ATOM   5318 C  CE2 . TYR   C  1 167 ? 2.541   -37.640 -21.162 1.00 29.31  0  182 TYR   C CE2 1 
ATOM   5319 C  CZ  . TYR   C  1 167 ? 1.564   -37.262 -22.070 1.00 35.21  0  182 TYR   C CZ  1 
ATOM   5320 O  OH  . TYR   C  1 167 ? 1.024   -35.996 -22.075 1.00 32.70  0  182 TYR   C OH  1 
ATOM   5321 N  N   . THR   C  1 168 ? 3.331   -44.392 -20.753 1.00 26.81  0  183 THR   C N   1 
ATOM   5322 C  CA  . THR   C  1 168 ? 4.046   -45.679 -20.892 1.00 25.74  0  183 THR   C CA  1 
ATOM   5323 C  C   . THR   C  1 168 ? 3.050   -46.698 -21.428 1.00 26.68  0  183 THR   C C   1 
ATOM   5324 O  O   . THR   C  1 168 ? 1.937   -46.760 -20.869 1.00 24.38  0  183 THR   C O   1 
ATOM   5325 C  CB  . THR   C  1 168 ? 4.659   -46.125 -19.563 1.00 27.30  0  183 THR   C CB  1 
ATOM   5326 O  OG1 . THR   C  1 168 ? 5.458   -45.062 -19.015 1.00 27.42  0  183 THR   C OG1 1 
ATOM   5327 C  CG2 . THR   C  1 168 ? 5.505   -47.373 -19.719 1.00 24.95  0  183 THR   C CG2 1 
ATOM   5328 N  N   . GLY   C  1 169 ? 3.450   -47.467 -22.444 1.00 28.52  0  184 GLY   C N   1 
ATOM   5329 C  CA  . GLY   C  1 169 ? 2.592   -48.527 -23.001 1.00 31.42  0  184 GLY   C CA  1 
ATOM   5330 C  C   . GLY   C  1 169 ? 2.240   -49.580 -21.959 1.00 29.71  0  184 GLY   C C   1 
ATOM   5331 O  O   . GLY   C  1 169 ? 3.106   -49.920 -21.153 1.00 27.84  0  184 GLY   C O   1 
ATOM   5332 N  N   . ASP   C  1 170 ? 1.012   -50.084 -21.989 1.00 33.30  0  185 ASP   C N   1 
ATOM   5333 C  CA  . ASP   C  1 170 ? 0.458   -51.048 -20.994 1.00 38.71  0  185 ASP   C CA  1 
ATOM   5334 C  C   . ASP   C  1 170 ? 1.274   -52.352 -20.940 1.00 38.49  0  185 ASP   C C   1 
ATOM   5335 O  O   . ASP   C  1 170 ? 1.344   -52.950 -19.862 1.00 42.77  0  185 ASP   C O   1 
ATOM   5336 C  CB  . ASP   C  1 170 ? -1.010  -51.340 -21.286 1.00 41.24  0  185 ASP   C CB  1 
ATOM   5337 C  CG  . ASP   C  1 170 ? -1.930  -50.168 -21.041 1.00 44.57  0  185 ASP   C CG  1 
ATOM   5338 O  OD1 . ASP   C  1 170 ? -1.622  -49.318 -20.153 1.00 42.69  0  185 ASP   C OD1 1 
ATOM   5339 O  OD2 . ASP   C  1 170 ? -2.924  -50.100 -21.777 1.00 56.01  -1 185 ASP   C OD2 1 
ATOM   5340 N  N   . ASP   C  1 171 ? 1.911   -52.741 -22.038 1.00 36.60  0  186 ASP   C N   1 
ATOM   5341 C  CA  . ASP   C  1 171 ? 2.753   -53.964 -22.214 1.00 40.07  0  186 ASP   C CA  1 
ATOM   5342 C  C   . ASP   C  1 171 ? 4.204   -53.693 -21.796 1.00 37.65  0  186 ASP   C C   1 
ATOM   5343 O  O   . ASP   C  1 171 ? 5.015   -54.627 -21.858 1.00 36.33  0  186 ASP   C O   1 
ATOM   5344 C  CB  . ASP   C  1 171 ? 2.765   -54.425 -23.681 1.00 45.13  0  186 ASP   C CB  1 
ATOM   5345 C  CG  . ASP   C  1 171 ? 3.288   -53.331 -24.624 1.00 50.81  0  186 ASP   C CG  1 
ATOM   5346 O  OD1 . ASP   C  1 171 ? 2.644   -52.227 -24.682 1.00 44.47  0  186 ASP   C OD1 1 
ATOM   5347 O  OD2 . ASP   C  1 171 ? 4.391   -53.516 -25.197 1.00 59.43  -1 186 ASP   C OD2 1 
ATOM   5348 N  N   . VAL   C  1 172 ? 4.551   -52.463 -21.414 1.00 33.59  0  187 VAL   C N   1 
ATOM   5349 C  CA  . VAL   C  1 172 ? 5.924   -52.083 -20.965 1.00 34.22  0  187 VAL   C CA  1 
ATOM   5350 C  C   . VAL   C  1 172 ? 5.904   -52.086 -19.442 1.00 35.49  0  187 VAL   C C   1 
ATOM   5351 O  O   . VAL   C  1 172 ? 5.215   -51.257 -18.844 1.00 32.66  0  187 VAL   C O   1 
ATOM   5352 C  CB  . VAL   C  1 172 ? 6.357   -50.727 -21.532 1.00 32.61  0  187 VAL   C CB  1 
ATOM   5353 C  CG1 . VAL   C  1 172 ? 7.707   -50.269 -21.014 1.00 36.13  0  187 VAL   C CG1 1 
ATOM   5354 C  CG2 . VAL   C  1 172 ? 6.337   -50.771 -23.042 1.00 34.12  0  187 VAL   C CG2 1 
ATOM   5355 N  N   . ARG   C  1 173 ? 6.652   -53.004 -18.849 1.00 34.87  0  188 ARG   C N   1 
ATOM   5356 C  CA  . ARG   C  1 173 ? 6.616   -53.269 -17.394 1.00 35.90  0  188 ARG   C CA  1 
ATOM   5357 C  C   . ARG   C  1 173 ? 7.263   -52.094 -16.639 1.00 33.56  0  188 ARG   C C   1 
ATOM   5358 O  O   . ARG   C  1 173 ? 8.343   -51.651 -17.063 1.00 29.15  0  188 ARG   C O   1 
ATOM   5359 C  CB  . ARG   C  1 173 ? 7.325   -54.595 -17.103 1.00 38.60  0  188 ARG   C CB  1 
ATOM   5360 C  CG  . ARG   C  1 173 ? 6.914   -55.219 -15.786 1.00 44.77  0  188 ARG   C CG  1 
ATOM   5361 C  CD  . ARG   C  1 173 ? 5.521   -55.834 -15.729 1.00 52.14  0  188 ARG   C CD  1 
ATOM   5362 N  NE  . ARG   C  1 173 ? 5.450   -57.088 -16.458 1.00 62.87  0  188 ARG   C NE  1 
ATOM   5363 C  CZ  . ARG   C  1 173 ? 5.939   -58.268 -16.041 1.00 75.21  0  188 ARG   C CZ  1 
ATOM   5364 N  NH1 . ARG   C  1 173 ? 6.586   -58.379 -14.890 1.00 79.71  1  188 ARG   C NH1 1 
ATOM   5365 N  NH2 . ARG   C  1 173 ? 5.799   -59.347 -16.797 1.00 80.12  0  188 ARG   C NH2 1 
ATOM   5366 N  N   . ILE   C  1 174 ? 6.595   -51.560 -15.610 1.00 31.72  0  189 ILE   C N   1 
ATOM   5367 C  CA  . ILE   C  1 174 ? 7.161   -50.522 -14.702 1.00 30.50  0  189 ILE   C CA  1 
ATOM   5368 C  C   . ILE   C  1 174 ? 7.567   -51.204 -13.383 1.00 29.47  0  189 ILE   C C   1 
ATOM   5369 O  O   . ILE   C  1 174 ? 8.721   -51.015 -12.937 1.00 30.02  0  189 ILE   C O   1 
ATOM   5370 C  CB  . ILE   C  1 174 ? 6.173   -49.371 -14.492 1.00 28.10  0  189 ILE   C CB  1 
ATOM   5371 C  CG1 . ILE   C  1 174 ? 6.008   -48.542 -15.766 1.00 28.43  0  189 ILE   C CG1 1 
ATOM   5372 C  CG2 . ILE   C  1 174 ? 6.605   -48.498 -13.319 1.00 28.74  0  189 ILE   C CG2 1 
ATOM   5373 C  CD1 . ILE   C  1 174 ? 4.783   -47.643 -15.749 1.00 26.19  0  189 ILE   C CD1 1 
ATOM   5374 N  N   . VAL   C  1 175 ? 6.646   -51.935 -12.774 1.00 30.35  0  190 VAL   C N   1 
ATOM   5375 C  CA  . VAL   C  1 175 ? 6.886   -52.730 -11.536 1.00 32.00  0  190 VAL   C CA  1 
ATOM   5376 C  C   . VAL   C  1 175 ? 7.388   -54.109 -11.950 1.00 30.40  0  190 VAL   C C   1 
ATOM   5377 O  O   . VAL   C  1 175 ? 6.601   -54.877 -12.515 1.00 30.40  0  190 VAL   C O   1 
ATOM   5378 C  CB  . VAL   C  1 175 ? 5.642   -52.849 -10.645 1.00 32.10  0  190 VAL   C CB  1 
ATOM   5379 C  CG1 . VAL   C  1 175 ? 6.008   -53.567 -9.354  1.00 30.74  0  190 VAL   C CG1 1 
ATOM   5380 C  CG2 . VAL   C  1 175 ? 5.014   -51.497 -10.352 1.00 33.87  0  190 VAL   C CG2 1 
ATOM   5381 N  N   . ARG   C  1 176 ? 8.642   -54.408 -11.661 1.00 27.63  0  191 ARG   C N   1 
ATOM   5382 C  CA  . ARG   C  1 176 ? 9.311   -55.621 -12.192 1.00 30.54  0  191 ARG   C CA  1 
ATOM   5383 C  C   . ARG   C  1 176 ? 9.178   -56.763 -11.178 1.00 32.47  0  191 ARG   C C   1 
ATOM   5384 O  O   . ARG   C  1 176 ? 8.686   -56.518 -10.059 1.00 29.35  0  191 ARG   C O   1 
ATOM   5385 C  CB  . ARG   C  1 176 ? 10.734  -55.229 -12.562 1.00 33.68  0  191 ARG   C CB  1 
ATOM   5386 C  CG  . ARG   C  1 176 ? 10.784  -54.244 -13.720 1.00 38.04  0  191 ARG   C CG  1 
ATOM   5387 C  CD  . ARG   C  1 176 ? 12.082  -53.503 -13.656 1.00 43.01  0  191 ARG   C CD  1 
ATOM   5388 N  NE  . ARG   C  1 176 ? 12.763  -53.262 -14.907 1.00 51.68  0  191 ARG   C NE  1 
ATOM   5389 C  CZ  . ARG   C  1 176 ? 12.470  -52.306 -15.778 1.00 58.00  0  191 ARG   C CZ  1 
ATOM   5390 N  NH1 . ARG   C  1 176 ? 11.441  -51.498 -15.590 1.00 63.34  1  191 ARG   C NH1 1 
ATOM   5391 N  NH2 . ARG   C  1 176 ? 13.220  -52.162 -16.856 1.00 64.50  0  191 ARG   C NH2 1 
ATOM   5392 N  N   . ASP   C  1 177 ? 9.599   -57.974 -11.565 1.00 33.17  0  192 ASP   C N   1 
ATOM   5393 C  CA  . ASP   C  1 177 ? 9.339   -59.222 -10.802 1.00 33.74  0  192 ASP   C CA  1 
ATOM   5394 C  C   . ASP   C  1 177 ? 10.213  -59.275 -9.543  1.00 31.13  0  192 ASP   C C   1 
ATOM   5395 O  O   . ASP   C  1 177 ? 9.783   -59.914 -8.588  1.00 34.21  0  192 ASP   C O   1 
ATOM   5396 C  CB  . ASP   C  1 177 ? 9.546   -60.441 -11.703 1.00 36.06  0  192 ASP   C CB  1 
ATOM   5397 C  CG  . ASP   C  1 177 ? 8.553   -60.512 -12.861 1.00 38.81  0  192 ASP   C CG  1 
ATOM   5398 O  OD1 . ASP   C  1 177 ? 7.403   -60.055 -12.682 1.00 41.21  0  192 ASP   C OD1 1 
ATOM   5399 O  OD2 . ASP   C  1 177 ? 8.924   -61.034 -13.929 1.00 41.48  -1 192 ASP   C OD2 1 
ATOM   5400 N  N   . ASP   C  1 178 ? 11.339  -58.557 -9.504  1.00 27.61  0  193 ASP   C N   1 
ATOM   5401 C  CA  . ASP   C  1 178 ? 12.163  -58.454 -8.267  1.00 25.95  0  193 ASP   C CA  1 
ATOM   5402 C  C   . ASP   C  1 178 ? 11.644  -57.347 -7.326  1.00 26.24  0  193 ASP   C C   1 
ATOM   5403 O  O   . ASP   C  1 178 ? 12.335  -57.082 -6.345  1.00 28.67  0  193 ASP   C O   1 
ATOM   5404 C  CB  . ASP   C  1 178 ? 13.633  -58.252 -8.589  1.00 25.35  0  193 ASP   C CB  1 
ATOM   5405 C  CG  . ASP   C  1 178 ? 13.961  -56.934 -9.269  1.00 25.58  0  193 ASP   C CG  1 
ATOM   5406 O  OD1 . ASP   C  1 178 ? 13.041  -56.317 -9.871  1.00 24.32  0  193 ASP   C OD1 1 
ATOM   5407 O  OD2 . ASP   C  1 178 ? 15.165  -56.569 -9.275  1.00 26.11  -1 193 ASP   C OD2 1 
ATOM   5408 N  N   . MET   C  1 179 ? 10.451  -56.792 -7.550  1.00 27.04  0  194 MET   C N   1 
ATOM   5409 C  CA  . MET   C  1 179 ? 9.845   -55.715 -6.729  1.00 26.37  0  194 MET   C CA  1 
ATOM   5410 C  C   . MET   C  1 179 ? 8.529   -56.239 -6.161  1.00 28.80  0  194 MET   C C   1 
ATOM   5411 O  O   . MET   C  1 179 ? 8.042   -57.288 -6.603  1.00 28.65  0  194 MET   C O   1 
ATOM   5412 C  CB  . MET   C  1 179 ? 9.573   -54.448 -7.536  1.00 25.92  0  194 MET   C CB  1 
ATOM   5413 C  CG  . MET   C  1 179 ? 10.830  -53.874 -8.189  1.00 29.51  0  194 MET   C CG  1 
ATOM   5414 S  SD  . MET   C  1 179 ? 10.566  -52.562 -9.433  1.00 27.70  0  194 MET   C SD  1 
ATOM   5415 C  CE  . MET   C  1 179 ? 12.223  -52.555 -10.087 1.00 28.02  0  194 MET   C CE  1 
ATOM   5416 N  N   . LEU   C  1 180 ? 8.044   -55.564 -5.129  1.00 27.08  0  195 LEU   C N   1 
ATOM   5417 C  CA  . LEU   C  1 180 ? 6.816   -55.866 -4.374  1.00 29.60  0  195 LEU   C CA  1 
ATOM   5418 C  C   . LEU   C  1 180 ? 6.178   -54.503 -4.080  1.00 30.35  0  195 LEU   C C   1 
ATOM   5419 O  O   . LEU   C  1 180 ? 6.903   -53.520 -3.919  1.00 29.89  0  195 LEU   C O   1 
ATOM   5420 C  CB  . LEU   C  1 180 ? 7.273   -56.599 -3.109  1.00 34.30  0  195 LEU   C CB  1 
ATOM   5421 C  CG  . LEU   C  1 180 ? 6.205   -56.904 -2.066  1.00 40.23  0  195 LEU   C CG  1 
ATOM   5422 C  CD1 . LEU   C  1 180 ? 6.560   -58.151 -1.279  1.00 42.22  0  195 LEU   C CD1 1 
ATOM   5423 C  CD2 . LEU   C  1 180 ? 6.027   -55.755 -1.105  1.00 42.78  0  195 LEU   C CD2 1 
ATOM   5424 N  N   A CYS   C  1 181 ? 4.858   -54.457 -3.964  0.50 31.43  0  196 CYS   C N   1 
ATOM   5425 N  N   B CYS   C  1 181 ? 4.870   -54.454 -3.914  0.50 32.09  0  196 CYS   C N   1 
ATOM   5426 C  CA  A CYS   C  1 181 ? 4.054   -53.213 -3.863  0.50 31.28  0  196 CYS   C CA  1 
ATOM   5427 C  CA  B CYS   C  1 181 ? 4.131   -53.183 -3.819  0.50 32.10  0  196 CYS   C CA  1 
ATOM   5428 C  C   A CYS   C  1 181 ? 3.178   -53.229 -2.603  0.50 31.89  0  196 CYS   C C   1 
ATOM   5429 C  C   B CYS   C  1 181 ? 3.148   -53.205 -2.640  0.50 32.39  0  196 CYS   C C   1 
ATOM   5430 O  O   A CYS   C  1 181 ? 2.587   -54.292 -2.304  0.50 31.49  0  196 CYS   C O   1 
ATOM   5431 O  O   B CYS   C  1 181 ? 2.505   -54.250 -2.397  0.50 31.60  0  196 CYS   C O   1 
ATOM   5432 C  CB  A CYS   C  1 181 ? 3.165   -53.079 -5.096  0.50 35.95  0  196 CYS   C CB  1 
ATOM   5433 C  CB  B CYS   C  1 181 ? 3.508   -52.950 -5.184  0.50 38.06  0  196 CYS   C CB  1 
ATOM   5434 S  SG  A CYS   C  1 181 ? 4.051   -52.504 -6.563  0.50 37.12  0  196 CYS   C SG  1 
ATOM   5435 S  SG  B CYS   C  1 181 ? 1.959   -52.043 -5.121  0.50 40.64  0  196 CYS   C SG  1 
ATOM   5436 N  N   . ALA   C  1 182 ? 3.058   -52.082 -1.918  1.00 30.66  0  197 ALA   C N   1 
ATOM   5437 C  CA  . ALA   C  1 182 ? 2.155   -51.889 -0.769  1.00 31.01  0  197 ALA   C CA  1 
ATOM   5438 C  C   . ALA   C  1 182 ? 1.811   -50.399 -0.620  1.00 31.53  0  197 ALA   C C   1 
ATOM   5439 O  O   . ALA   C  1 182 ? 2.641   -49.532 -0.975  1.00 28.63  0  197 ALA   C O   1 
ATOM   5440 C  CB  . ALA   C  1 182 ? 2.807   -52.422 0.493   1.00 29.08  0  197 ALA   C CB  1 
ATOM   5441 N  N   . GLY   C  1 183 ? 0.628   -50.122 -0.079  1.00 31.69  0  198 GLY   C N   1 
ATOM   5442 C  CA  . GLY   C  1 183 ? 0.230   -48.772 0.366   1.00 32.61  0  198 GLY   C CA  1 
ATOM   5443 C  C   . GLY   C  1 183 ? -0.914  -48.202 -0.449  1.00 34.25  0  198 GLY   C C   1 
ATOM   5444 O  O   . GLY   C  1 183 ? -1.261  -48.786 -1.463  1.00 31.81  0  198 GLY   C O   1 
ATOM   5445 N  N   . ASN   C  1 184 ? -1.453  -47.077 0.006   1.00 35.33  0  199 ASN   C N   1 
ATOM   5446 C  CA  . ASN   C  1 184 ? -2.610  -46.389 -0.609  1.00 38.38  0  199 ASN   C CA  1 
ATOM   5447 C  C   . ASN   C  1 184 ? -2.385  -44.894 -0.384  1.00 33.94  0  199 ASN   C C   1 
ATOM   5448 O  O   . ASN   C  1 184 ? -1.267  -44.520 0.020   1.00 32.92  0  199 ASN   C O   1 
ATOM   5449 C  CB  . ASN   C  1 184 ? -3.925  -46.951 -0.064  1.00 38.03  0  199 ASN   C CB  1 
ATOM   5450 C  CG  . ASN   C  1 184 ? -4.008  -46.864 1.451   1.00 42.03  0  199 ASN   C CG  1 
ATOM   5451 O  OD1 . ASN   C  1 184 ? -3.654  -45.847 2.037   1.00 41.26  0  199 ASN   C OD1 1 
ATOM   5452 N  ND2 . ASN   C  1 184 ? -4.405  -47.944 2.104   1.00 39.84  0  199 ASN   C ND2 1 
ATOM   5453 N  N   . THR   C  1 185 ? -3.395  -44.074 -0.624  1.00 33.07  0  200 THR   C N   1 
ATOM   5454 C  CA  . THR   C  1 185 ? -3.291  -42.595 -0.542  1.00 36.02  0  200 THR   C CA  1 
ATOM   5455 C  C   . THR   C  1 185 ? -3.349  -42.127 0.908   1.00 35.72  0  200 THR   C C   1 
ATOM   5456 O  O   . THR   C  1 185 ? -3.250  -40.902 1.105   1.00 39.69  0  200 THR   C O   1 
ATOM   5457 C  CB  . THR   C  1 185 ? -4.378  -41.918 -1.383  1.00 40.17  0  200 THR   C CB  1 
ATOM   5458 O  OG1 . THR   C  1 185 ? -5.663  -42.346 -0.925  1.00 34.52  0  200 THR   C OG1 1 
ATOM   5459 C  CG2 . THR   C  1 185 ? -4.227  -42.237 -2.854  1.00 45.13  0  200 THR   C CG2 1 
ATOM   5460 N  N   . ARG   C  1 186 ? -3.509  -43.032 1.887   1.00 38.23  0  201 ARG   C N   1 
ATOM   5461 C  CA  . ARG   C  1 186 ? -3.443  -42.659 3.323   1.00 38.29  0  201 ARG   C CA  1 
ATOM   5462 C  C   . ARG   C  1 186 ? -2.216  -43.290 4.007   1.00 34.38  0  201 ARG   C C   1 
ATOM   5463 O  O   . ARG   C  1 186 ? -1.838  -42.766 5.027   1.00 38.06  0  201 ARG   C O   1 
ATOM   5464 C  CB  . ARG   C  1 186 ? -4.742  -43.053 4.034   1.00 40.12  0  201 ARG   C CB  1 
ATOM   5465 C  CG  . ARG   C  1 186 ? -6.004  -42.386 3.494   1.00 44.11  0  201 ARG   C CG  1 
ATOM   5466 C  CD  . ARG   C  1 186 ? -7.295  -42.798 4.190   1.00 48.44  0  201 ARG   C CD  1 
ATOM   5467 N  NE  . ARG   C  1 186 ? -8.475  -42.094 3.663   0.00 47.88  0  201 ARG   C NE  1 
ATOM   5468 C  CZ  . ARG   C  1 186 ? -8.897  -40.878 4.016   0.00 47.98  0  201 ARG   C CZ  1 
ATOM   5469 N  NH1 . ARG   C  1 186 ? -8.251  -40.147 4.913   0.00 47.92  1  201 ARG   C NH1 1 
ATOM   5470 N  NH2 . ARG   C  1 186 ? -9.986  -40.386 3.453   0.00 47.87  0  201 ARG   C NH2 1 
ATOM   5471 N  N   . ARG   C  1 187 ? -1.611  -44.348 3.486   1.00 30.12  0  202 ARG   C N   1 
ATOM   5472 C  CA  . ARG   C  1 187 ? -0.607  -45.171 4.215   1.00 32.62  0  202 ARG   C CA  1 
ATOM   5473 C  C   . ARG   C  1 187 ? 0.547   -45.477 3.246   1.00 34.48  0  202 ARG   C C   1 
ATOM   5474 O  O   . ARG   C  1 187 ? 0.311   -46.148 2.203   1.00 30.93  0  202 ARG   C O   1 
ATOM   5475 C  CB  . ARG   C  1 187 ? -1.248  -46.464 4.732   1.00 41.04  0  202 ARG   C CB  1 
ATOM   5476 C  CG  . ARG   C  1 187 ? -2.617  -46.340 5.416   1.00 50.06  0  202 ARG   C CG  1 
ATOM   5477 C  CD  . ARG   C  1 187 ? -2.700  -46.532 6.922   1.00 59.48  0  202 ARG   C CD  1 
ATOM   5478 N  NE  . ARG   C  1 187 ? -3.935  -45.968 7.470   1.00 69.73  0  202 ARG   C NE  1 
ATOM   5479 C  CZ  . ARG   C  1 187 ? -4.170  -44.657 7.682   1.00 72.75  0  202 ARG   C CZ  1 
ATOM   5480 N  NH1 . ARG   C  1 187 ? -3.247  -43.750 7.406   1.00 80.67  1  202 ARG   C NH1 1 
ATOM   5481 N  NH2 . ARG   C  1 187 ? -5.336  -44.245 8.159   1.00 63.36  0  202 ARG   C NH2 1 
ATOM   5482 N  N   . ASP   C  1 188 ? 1.768   -45.051 3.564   1.00 29.04  0  203 ASP   C N   1 
ATOM   5483 C  CA  . ASP   C  1 188 ? 2.926   -45.241 2.656   1.00 28.53  0  203 ASP   C CA  1 
ATOM   5484 C  C   . ASP   C  1 188 ? 4.205   -44.977 3.445   1.00 27.09  0  203 ASP   C C   1 
ATOM   5485 O  O   . ASP   C  1 188 ? 4.166   -44.370 4.529   1.00 28.33  0  203 ASP   C O   1 
ATOM   5486 C  CB  . ASP   C  1 188 ? 2.798   -44.375 1.380   1.00 29.63  0  203 ASP   C CB  1 
ATOM   5487 C  CG  . ASP   C  1 188 ? 3.551   -44.841 0.131   1.00 31.30  0  203 ASP   C CG  1 
ATOM   5488 O  OD1 . ASP   C  1 188 ? 4.342   -45.802 0.215   1.00 31.83  0  203 ASP   C OD1 1 
ATOM   5489 O  OD2 . ASP   C  1 188 ? 3.295   -44.254 -0.963  1.00 33.74  -1 203 ASP   C OD2 1 
ATOM   5490 N  N   . SER   C  1 189 ? 5.309   -45.427 2.882   1.00 25.79  0  204 SER   C N   1 
ATOM   5491 C  CA  . SER   C  1 189 ? 6.687   -45.012 3.231   1.00 28.39  0  204 SER   C CA  1 
ATOM   5492 C  C   . SER   C  1 189 ? 7.042   -43.769 2.399   1.00 26.50  0  204 SER   C C   1 
ATOM   5493 O  O   . SER   C  1 189 ? 6.324   -43.478 1.448   1.00 30.98  0  204 SER   C O   1 
ATOM   5494 C  CB  . SER   C  1 189 ? 7.604   -46.157 2.959   1.00 31.09  0  204 SER   C CB  1 
ATOM   5495 O  OG  . SER   C  1 189 ? 7.420   -46.580 1.603   1.00 32.16  0  204 SER   C OG  1 
ATOM   5496 N  N   . CYS   C  1 190 ? 8.093   -43.048 2.739   1.00 27.30  0  205 CYS   C N   1 
ATOM   5497 C  CA  . CYS   C  1 190 ? 8.416   -41.745 2.103   1.00 28.39  0  205 CYS   C CA  1 
ATOM   5498 C  C   . CYS   C  1 190 ? 9.924   -41.506 2.198   1.00 30.73  0  205 CYS   C C   1 
ATOM   5499 O  O   . CYS   C  1 190 ? 10.639  -42.409 2.715   1.00 26.22  0  205 CYS   C O   1 
ATOM   5500 C  CB  . CYS   C  1 190 ? 7.596   -40.609 2.725   1.00 33.76  0  205 CYS   C CB  1 
ATOM   5501 S  SG  . CYS   C  1 190 ? 7.425   -39.173 1.603   1.00 33.97  0  205 CYS   C SG  1 
ATOM   5502 N  N   . GLN   C  1 191 ? 10.397  -40.353 1.718   1.00 28.33  0  206 GLN   C N   1 
ATOM   5503 C  CA  . GLN   C  1 191 ? 11.839  -40.026 1.656   1.00 28.06  0  206 GLN   C CA  1 
ATOM   5504 C  C   . GLN   C  1 191 ? 12.383  -40.113 3.082   1.00 27.39  0  206 GLN   C C   1 
ATOM   5505 O  O   . GLN   C  1 191 ? 11.801  -39.488 3.956   1.00 29.34  0  206 GLN   C O   1 
ATOM   5506 C  CB  . GLN   C  1 191 ? 12.134  -38.649 1.022   1.00 31.60  0  206 GLN   C CB  1 
ATOM   5507 C  CG  . GLN   C  1 191 ? 12.011  -38.624 -0.504  1.00 36.04  0  206 GLN   C CG  1 
ATOM   5508 C  CD  . GLN   C  1 191 ? 10.616  -38.915 -1.030  1.00 40.17  0  206 GLN   C CD  1 
ATOM   5509 O  OE1 . GLN   C  1 191 ? 9.616   -38.327 -0.594  1.00 39.04  0  206 GLN   C OE1 1 
ATOM   5510 N  NE2 . GLN   C  1 191 ? 10.515  -39.823 -1.997  1.00 40.77  0  206 GLN   C NE2 1 
ATOM   5511 N  N   . GLY   C  1 192 ? 13.490  -40.826 3.266   1.00 23.13  0  207 GLY   C N   1 
ATOM   5512 C  CA  . GLY   C  1 192 ? 14.109  -41.144 4.555   1.00 24.08  0  207 GLY   C CA  1 
ATOM   5513 C  C   . GLY   C  1 192 ? 13.716  -42.510 5.104   1.00 22.32  0  207 GLY   C C   1 
ATOM   5514 O  O   . GLY   C  1 192 ? 14.413  -42.985 6.030   1.00 23.49  0  207 GLY   C O   1 
ATOM   5515 N  N   . ASP   C  1 193 ? 12.666  -43.157 4.583   1.00 22.85  0  208 ASP   C N   1 
ATOM   5516 C  CA  . ASP   C  1 193 ? 12.324  -44.558 4.953   1.00 22.72  0  208 ASP   C CA  1 
ATOM   5517 C  C   . ASP   C  1 193 ? 13.067  -45.577 4.088   1.00 24.41  0  208 ASP   C C   1 
ATOM   5518 O  O   . ASP   C  1 193 ? 13.070  -46.796 4.460   1.00 24.22  0  208 ASP   C O   1 
ATOM   5519 C  CB  . ASP   C  1 193 ? 10.819  -44.795 4.879   1.00 23.33  0  208 ASP   C CB  1 
ATOM   5520 C  CG  . ASP   C  1 193 ? 10.049  -43.956 5.863   1.00 24.14  0  208 ASP   C CG  1 
ATOM   5521 O  OD1 . ASP   C  1 193 ? 10.533  -43.846 7.039   1.00 23.42  0  208 ASP   C OD1 1 
ATOM   5522 O  OD2 . ASP   C  1 193 ? 8.968   -43.466 5.462   1.00 24.07  -1 208 ASP   C OD2 1 
ATOM   5523 N  N   . SER   C  1 194 ? 13.654  -45.131 2.982   1.00 24.40  0  209 SER   C N   1 
ATOM   5524 C  CA  . SER   C  1 194 ? 14.438  -45.938 2.030   1.00 25.70  0  209 SER   C CA  1 
ATOM   5525 C  C   . SER   C  1 194 ? 15.354  -46.871 2.796   1.00 28.15  0  209 SER   C C   1 
ATOM   5526 O  O   . SER   C  1 194 ? 16.056  -46.382 3.740   1.00 27.03  0  209 SER   C O   1 
ATOM   5527 C  CB  . SER   C  1 194 ? 15.256  -45.079 1.085   1.00 26.92  0  209 SER   C CB  1 
ATOM   5528 O  OG  . SER   C  1 194 ? 14.392  -44.594 0.058   1.00 30.10  0  209 SER   C OG  1 
ATOM   5529 N  N   . GLY   C  1 195 ? 15.387  -48.131 2.349   1.00 27.67  0  210 GLY   C N   1 
ATOM   5530 C  CA  . GLY   C  1 195 ? 16.298  -49.140 2.897   1.00 29.26  0  210 GLY   C CA  1 
ATOM   5531 C  C   . GLY   C  1 195 ? 15.709  -49.850 4.107   1.00 27.80  0  210 GLY   C C   1 
ATOM   5532 O  O   . GLY   C  1 195 ? 16.222  -50.893 4.467   1.00 27.58  0  210 GLY   C O   1 
ATOM   5533 N  N   . GLY   C  1 196 ? 14.675  -49.282 4.709   1.00 27.04  0  211 GLY   C N   1 
ATOM   5534 C  CA  . GLY   C  1 196 ? 13.979  -49.838 5.873   1.00 30.44  0  211 GLY   C CA  1 
ATOM   5535 C  C   . GLY   C  1 196 ? 13.125  -51.047 5.519   1.00 27.41  0  211 GLY   C C   1 
ATOM   5536 O  O   . GLY   C  1 196 ? 12.891  -51.342 4.358   1.00 27.74  0  211 GLY   C O   1 
ATOM   5537 N  N   . PRO   C  1 197 ? 12.645  -51.781 6.539   1.00 30.93  0  212 PRO   C N   1 
ATOM   5538 C  CA  . PRO   C  1 197 ? 11.920  -53.031 6.320   1.00 29.53  0  212 PRO   C CA  1 
ATOM   5539 C  C   . PRO   C  1 197 ? 10.398  -52.900 6.144   1.00 30.56  0  212 PRO   C C   1 
ATOM   5540 O  O   . PRO   C  1 197 ? 9.777   -52.044 6.776   1.00 27.41  0  212 PRO   C O   1 
ATOM   5541 C  CB  . PRO   C  1 197 ? 12.262  -53.798 7.599   1.00 29.71  0  212 PRO   C CB  1 
ATOM   5542 C  CG  . PRO   C  1 197 ? 12.288  -52.697 8.673   1.00 31.91  0  212 PRO   C CG  1 
ATOM   5543 C  CD  . PRO   C  1 197 ? 12.826  -51.469 7.966   1.00 29.65  0  212 PRO   C CD  1 
ATOM   5544 N  N   . LEU   C  1 198 ? 9.855   -53.737 5.250   1.00 26.19  0  213 LEU   C N   1 
ATOM   5545 C  CA  . LEU   C  1 198 ? 8.426   -54.107 5.204   1.00 30.86  0  213 LEU   C CA  1 
ATOM   5546 C  C   . LEU   C  1 198 ? 8.341   -55.522 5.785   1.00 31.96  0  213 LEU   C C   1 
ATOM   5547 O  O   . LEU   C  1 198 ? 8.987   -56.441 5.220   1.00 31.21  0  213 LEU   C O   1 
ATOM   5548 C  CB  . LEU   C  1 198 ? 7.927   -54.043 3.756   1.00 30.43  0  213 LEU   C CB  1 
ATOM   5549 C  CG  . LEU   C  1 198 ? 6.461   -54.400 3.528   1.00 33.20  0  213 LEU   C CG  1 
ATOM   5550 C  CD1 . LEU   C  1 198 ? 5.530   -53.337 4.066   1.00 33.49  0  213 LEU   C CD1 1 
ATOM   5551 C  CD2 . LEU   C  1 198 ? 6.195   -54.606 2.053   1.00 32.89  0  213 LEU   C CD2 1 
ATOM   5552 N  N   . VAL   C  1 199 ? 7.631   -55.678 6.899   1.00 29.40  0  214 VAL   C N   1 
ATOM   5553 C  CA  . VAL   C  1 199 ? 7.603   -56.940 7.687   1.00 29.58  0  214 VAL   C CA  1 
ATOM   5554 C  C   . VAL   C  1 199 ? 6.157   -57.439 7.730   1.00 30.13  0  214 VAL   C C   1 
ATOM   5555 O  O   . VAL   C  1 199 ? 5.230   -56.627 7.797   1.00 32.99  0  214 VAL   C O   1 
ATOM   5556 C  CB  . VAL   C  1 199 ? 8.220   -56.761 9.090   1.00 31.08  0  214 VAL   C CB  1 
ATOM   5557 C  CG1 . VAL   C  1 199 ? 9.699   -56.458 9.001   1.00 29.62  0  214 VAL   C CG1 1 
ATOM   5558 C  CG2 . VAL   C  1 199 ? 7.530   -55.680 9.905   1.00 30.49  0  214 VAL   C CG2 1 
ATOM   5559 N  N   . CYS   C  1 200 ? 5.969   -58.750 7.615   1.00 33.37  0  215 CYS   C N   1 
ATOM   5560 C  CA  . CYS   C  1 200 ? 4.632   -59.386 7.648   1.00 34.02  0  215 CYS   C CA  1 
ATOM   5561 C  C   . CYS   C  1 200 ? 4.669   -60.505 8.703   1.00 33.08  0  215 CYS   C C   1 
ATOM   5562 O  O   . CYS   C  1 200 ? 5.698   -61.211 8.825   1.00 31.55  0  215 CYS   C O   1 
ATOM   5563 C  CB  . CYS   C  1 200 ? 4.246   -59.903 6.268   1.00 37.54  0  215 CYS   C CB  1 
ATOM   5564 S  SG  . CYS   C  1 200 ? 4.450   -58.724 4.887   1.00 37.73  0  215 CYS   C SG  1 
ATOM   5565 N  N   . LYS   C  1 201 ? 3.619   -60.614 9.495   1.00 34.00  0  216 LYS   C N   1 
ATOM   5566 C  CA  . LYS   C  1 201 ? 3.560   -61.642 10.567  1.00 42.90  0  216 LYS   C CA  1 
ATOM   5567 C  C   . LYS   C  1 201 ? 2.906   -62.885 9.943   1.00 39.03  0  216 LYS   C C   1 
ATOM   5568 O  O   . LYS   C  1 201 ? 1.729   -62.800 9.589   1.00 40.85  0  216 LYS   C O   1 
ATOM   5569 C  CB  . LYS   C  1 201 ? 2.819   -61.134 11.805  1.00 44.06  0  216 LYS   C CB  1 
ATOM   5570 C  CG  . LYS   C  1 201 ? 3.104   -61.951 13.061  1.00 49.64  0  216 LYS   C CG  1 
ATOM   5571 C  CD  . LYS   C  1 201 ? 2.553   -61.382 14.354  1.00 50.87  0  216 LYS   C CD  1 
ATOM   5572 C  CE  . LYS   C  1 201 ? 3.397   -61.861 15.515  1.00 55.39  0  216 LYS   C CE  1 
ATOM   5573 N  NZ  . LYS   C  1 201 ? 2.817   -61.542 16.841  1.00 55.12  1  216 LYS   C NZ  1 
ATOM   5574 N  N   . VAL   C  1 202 ? 3.655   -63.973 9.824   1.00 43.72  0  217 VAL   C N   1 
ATOM   5575 C  CA  . VAL   C  1 202 ? 3.234   -65.244 9.150   1.00 49.44  0  217 VAL   C CA  1 
ATOM   5576 C  C   . VAL   C  1 202 ? 3.472   -66.412 10.120  1.00 50.24  0  217 VAL   C C   1 
ATOM   5577 O  O   . VAL   C  1 202 ? 4.625   -66.550 10.566  1.00 46.70  0  217 VAL   C O   1 
ATOM   5578 C  CB  . VAL   C  1 202 ? 4.043   -65.453 7.848   1.00 50.46  0  217 VAL   C CB  1 
ATOM   5579 C  CG1 . VAL   C  1 202 ? 3.683   -66.753 7.132   1.00 50.08  0  217 VAL   C CG1 1 
ATOM   5580 C  CG2 . VAL   C  1 202 ? 3.890   -64.277 6.890   1.00 50.89  0  217 VAL   C CG2 1 
ATOM   5581 N  N   . ASN   C  1 203 ? 2.452   -67.242 10.403  1.00 60.95  0  218 ASN   C N   1 
ATOM   5582 C  CA  . ASN   C  1 203 ? 2.519   -68.409 11.342  1.00 60.53  0  218 ASN   C CA  1 
ATOM   5583 C  C   . ASN   C  1 203 ? 3.208   -67.960 12.644  1.00 60.50  0  218 ASN   C C   1 
ATOM   5584 O  O   . ASN   C  1 203 ? 4.217   -68.629 13.048  1.00 51.21  0  218 ASN   C O   1 
ATOM   5585 C  CB  . ASN   C  1 203 ? 3.178   -69.640 10.693  1.00 58.41  0  218 ASN   C CB  1 
ATOM   5586 C  CG  . ASN   C  1 203 ? 2.491   -70.074 9.400   0.00 61.34  0  218 ASN   C CG  1 
ATOM   5587 O  OD1 . ASN   C  1 203 ? 1.355   -69.693 9.121   0.00 61.07  0  218 ASN   C OD1 1 
ATOM   5588 N  ND2 . ASN   C  1 203 ? 3.183   -70.876 8.606   0.00 61.13  0  218 ASN   C ND2 1 
ATOM   5589 N  N   . GLY   C  1 204 ? 2.745   -66.820 13.204  1.00 58.22  0  219 GLY   C N   1 
ATOM   5590 C  CA  . GLY   C  1 204 ? 3.233   -66.182 14.448  1.00 57.35  0  219 GLY   C CA  1 
ATOM   5591 C  C   . GLY   C  1 204 ? 4.660   -65.630 14.396  1.00 61.61  0  219 GLY   C C   1 
ATOM   5592 O  O   . GLY   C  1 204 ? 5.165   -65.247 15.479  1.00 56.10  0  219 GLY   C O   1 
ATOM   5593 N  N   . THR   C  1 205 ? 5.318   -65.566 13.227  1.00 51.87  0  220 THR   C N   1 
ATOM   5594 C  CA  . THR   C  1 205 ? 6.711   -65.056 13.086  1.00 52.66  0  220 THR   C CA  1 
ATOM   5595 C  C   . THR   C  1 205 ? 6.726   -63.817 12.176  1.00 47.83  0  220 THR   C C   1 
ATOM   5596 O  O   . THR   C  1 205 ? 6.023   -63.813 11.140  1.00 42.77  0  220 THR   C O   1 
ATOM   5597 C  CB  . THR   C  1 205 ? 7.660   -66.134 12.553  1.00 55.18  0  220 THR   C CB  1 
ATOM   5598 O  OG1 . THR   C  1 205 ? 7.469   -67.278 13.383  1.00 65.32  0  220 THR   C OG1 1 
ATOM   5599 C  CG2 . THR   C  1 205 ? 9.110   -65.701 12.536  1.00 51.15  0  220 THR   C CG2 1 
ATOM   5600 N  N   . TRP   C  1 206 ? 7.494   -62.793 12.559  1.00 44.76  0  221 TRP   C N   1 
ATOM   5601 C  CA  . TRP   C  1 206 ? 7.733   -61.591 11.716  1.00 39.71  0  221 TRP   C CA  1 
ATOM   5602 C  C   . TRP   C  1 206 ? 8.749   -61.972 10.634  1.00 35.04  0  221 TRP   C C   1 
ATOM   5603 O  O   . TRP   C  1 206 ? 9.850   -62.392 11.001  1.00 35.26  0  221 TRP   C O   1 
ATOM   5604 C  CB  . TRP   C  1 206 ? 8.204   -60.388 12.550  1.00 38.20  0  221 TRP   C CB  1 
ATOM   5605 C  CG  . TRP   C  1 206 ? 7.092   -59.742 13.311  1.00 38.77  0  221 TRP   C CG  1 
ATOM   5606 C  CD1 . TRP   C  1 206 ? 6.891   -59.830 14.655  1.00 36.71  0  221 TRP   C CD1 1 
ATOM   5607 C  CD2 . TRP   C  1 206 ? 6.013   -58.921 12.797  1.00 35.84  0  221 TRP   C CD2 1 
ATOM   5608 N  NE1 . TRP   C  1 206 ? 5.772   -59.127 15.007  1.00 40.48  0  221 TRP   C NE1 1 
ATOM   5609 C  CE2 . TRP   C  1 206 ? 5.224   -58.541 13.902  1.00 37.09  0  221 TRP   C CE2 1 
ATOM   5610 C  CE3 . TRP   C  1 206 ? 5.653   -58.441 11.536  1.00 34.48  0  221 TRP   C CE3 1 
ATOM   5611 C  CZ2 . TRP   C  1 206 ? 4.092   -57.738 13.780  1.00 36.99  0  221 TRP   C CZ2 1 
ATOM   5612 C  CZ3 . TRP   C  1 206 ? 4.516   -57.668 11.404  1.00 34.46  0  221 TRP   C CZ3 1 
ATOM   5613 C  CH2 . TRP   C  1 206 ? 3.759   -57.301 12.513  1.00 34.74  0  221 TRP   C CH2 1 
ATOM   5614 N  N   . LEU   C  1 207 ? 8.364   -61.833 9.354   1.00 35.18  0  222 LEU   C N   1 
ATOM   5615 C  CA  . LEU   C  1 207 ? 9.247   -62.051 8.177   1.00 35.24  0  222 LEU   C CA  1 
ATOM   5616 C  C   . LEU   C  1 207 ? 9.435   -60.729 7.411   1.00 31.49  0  222 LEU   C C   1 
ATOM   5617 O  O   . LEU   C  1 207 ? 8.434   -60.037 7.157   1.00 33.18  0  222 LEU   C O   1 
ATOM   5618 C  CB  . LEU   C  1 207 ? 8.612   -63.136 7.290   1.00 36.87  0  222 LEU   C CB  1 
ATOM   5619 C  CG  . LEU   C  1 207 ? 8.436   -64.517 7.934   1.00 35.40  0  222 LEU   C CG  1 
ATOM   5620 C  CD1 . LEU   C  1 207 ? 7.866   -65.503 6.930   1.00 39.43  0  222 LEU   C CD1 1 
ATOM   5621 C  CD2 . LEU   C  1 207 ? 9.761   -65.045 8.492   1.00 35.47  0  222 LEU   C CD2 1 
ATOM   5622 N  N   . GLN   C  1 208 ? 10.657  -60.421 6.996   1.00 27.75  0  223 GLN   C N   1 
ATOM   5623 C  CA  . GLN   C  1 208 ? 10.890  -59.258 6.115   1.00 27.36  0  223 GLN   C CA  1 
ATOM   5624 C  C   . GLN   C  1 208 ? 10.529  -59.595 4.662   1.00 26.71  0  223 GLN   C C   1 
ATOM   5625 O  O   . GLN   C  1 208 ? 11.336  -60.206 3.966   1.00 28.48  0  223 GLN   C O   1 
ATOM   5626 C  CB  . GLN   C  1 208 ? 12.314  -58.732 6.245   1.00 29.11  0  223 GLN   C CB  1 
ATOM   5627 C  CG  . GLN   C  1 208 ? 12.410  -57.342 5.621   1.00 28.46  0  223 GLN   C CG  1 
ATOM   5628 C  CD  . GLN   C  1 208 ? 13.726  -56.638 5.828   1.00 29.49  0  223 GLN   C CD  1 
ATOM   5629 O  OE1 . GLN   C  1 208 ? 14.550  -56.972 6.708   1.00 29.74  0  223 GLN   C OE1 1 
ATOM   5630 N  NE2 . GLN   C  1 208 ? 13.939  -55.633 4.987   1.00 30.84  0  223 GLN   C NE2 1 
ATOM   5631 N  N   . ALA   C  1 209 ? 9.386   -59.106 4.184   1.00 28.34  0  224 ALA   C N   1 
ATOM   5632 C  CA  . ALA   C  1 209 ? 8.914   -59.240 2.782   1.00 29.54  0  224 ALA   C CA  1 
ATOM   5633 C  C   . ALA   C  1 209 ? 9.652   -58.278 1.831   1.00 32.56  0  224 ALA   C C   1 
ATOM   5634 O  O   . ALA   C  1 209 ? 9.926   -58.691 0.690   1.00 28.43  0  224 ALA   C O   1 
ATOM   5635 C  CB  . ALA   C  1 209 ? 7.434   -59.001 2.743   1.00 29.67  0  224 ALA   C CB  1 
ATOM   5636 N  N   . GLY   C  1 210 ? 9.968   -57.043 2.272   1.00 29.70  0  225 GLY   C N   1 
ATOM   5637 C  CA  . GLY   C  1 210 ? 10.418  -55.952 1.387   1.00 26.91  0  225 GLY   C CA  1 
ATOM   5638 C  C   . GLY   C  1 210 ? 11.487  -55.035 1.985   1.00 28.01  0  225 GLY   C C   1 
ATOM   5639 O  O   . GLY   C  1 210 ? 11.674  -54.976 3.233   1.00 25.72  0  225 GLY   C O   1 
ATOM   5640 N  N   . VAL   C  1 211 ? 12.211  -54.365 1.098   1.00 25.91  0  226 VAL   C N   1 
ATOM   5641 C  CA  . VAL   C  1 211 ? 13.098  -53.225 1.429   1.00 26.98  0  226 VAL   C CA  1 
ATOM   5642 C  C   . VAL   C  1 211 ? 12.510  -51.981 0.749   1.00 27.65  0  226 VAL   C C   1 
ATOM   5643 O  O   . VAL   C  1 211 ? 12.331  -52.023 -0.476  1.00 26.03  0  226 VAL   C O   1 
ATOM   5644 C  CB  . VAL   C  1 211 ? 14.526  -53.520 0.982   1.00 28.89  0  226 VAL   C CB  1 
ATOM   5645 C  CG1 . VAL   C  1 211 ? 15.433  -52.315 1.194   1.00 27.97  0  226 VAL   C CG1 1 
ATOM   5646 C  CG2 . VAL   C  1 211 ? 15.059  -54.769 1.668   1.00 27.71  0  226 VAL   C CG2 1 
ATOM   5647 N  N   . VAL   C  1 212 ? 12.282  -50.896 1.498   1.00 27.90  0  227 VAL   C N   1 
ATOM   5648 C  CA  . VAL   C  1 212 ? 11.746  -49.611 0.937   1.00 26.82  0  227 VAL   C CA  1 
ATOM   5649 C  C   . VAL   C  1 212 ? 12.659  -49.174 -0.223  1.00 23.15  0  227 VAL   C C   1 
ATOM   5650 O  O   . VAL   C  1 212 ? 13.861  -48.989 0.012   1.00 27.46  0  227 VAL   C O   1 
ATOM   5651 C  CB  . VAL   C  1 212 ? 11.627  -48.496 1.991   1.00 23.20  0  227 VAL   C CB  1 
ATOM   5652 C  CG1 . VAL   C  1 212 ? 11.151  -47.191 1.348   1.00 24.23  0  227 VAL   C CG1 1 
ATOM   5653 C  CG2 . VAL   C  1 212 ? 10.720  -48.907 3.137   1.00 25.34  0  227 VAL   C CG2 1 
ATOM   5654 N  N   . SER   C  1 213 ? 12.118  -49.064 -1.433  1.00 22.35  0  228 SER   C N   1 
ATOM   5655 C  CA  . SER   C  1 213 ? 12.903  -48.790 -2.669  1.00 23.52  0  228 SER   C CA  1 
ATOM   5656 C  C   . SER   C  1 213 ? 12.502  -47.436 -3.289  1.00 23.59  0  228 SER   C C   1 
ATOM   5657 O  O   . SER   C  1 213 ? 13.296  -46.486 -3.226  1.00 26.67  0  228 SER   C O   1 
ATOM   5658 C  CB  . SER   C  1 213 ? 12.778  -49.899 -3.631  1.00 23.29  0  228 SER   C CB  1 
ATOM   5659 O  OG  . SER   C  1 213 ? 13.694  -49.727 -4.710  1.00 24.04  0  228 SER   C OG  1 
ATOM   5660 N  N   . TRP   C  1 214 ? 11.305  -47.317 -3.847  1.00 25.84  0  229 TRP   C N   1 
ATOM   5661 C  CA  . TRP   C  1 214 ? 10.936  -46.123 -4.648  1.00 22.86  0  229 TRP   C CA  1 
ATOM   5662 C  C   . TRP   C  1 214 ? 9.435   -46.001 -4.776  1.00 25.48  0  229 TRP   C C   1 
ATOM   5663 O  O   . TRP   C  1 214 ? 8.677   -46.868 -4.295  1.00 25.49  0  229 TRP   C O   1 
ATOM   5664 C  CB  . TRP   C  1 214 ? 11.638  -46.113 -6.014  1.00 25.65  0  229 TRP   C CB  1 
ATOM   5665 C  CG  . TRP   C  1 214 ? 11.213  -47.187 -6.970  1.00 27.57  0  229 TRP   C CG  1 
ATOM   5666 C  CD1 . TRP   C  1 214 ? 11.589  -48.496 -6.975  1.00 29.44  0  229 TRP   C CD1 1 
ATOM   5667 C  CD2 . TRP   C  1 214 ? 10.341  -47.028 -8.101  1.00 29.14  0  229 TRP   C CD2 1 
ATOM   5668 N  NE1 . TRP   C  1 214 ? 10.994  -49.174 -8.007  1.00 28.88  0  229 TRP   C NE1 1 
ATOM   5669 C  CE2 . TRP   C  1 214 ? 10.244  -48.288 -8.736  1.00 29.16  0  229 TRP   C CE2 1 
ATOM   5670 C  CE3 . TRP   C  1 214 ? 9.611   -45.948 -8.623  1.00 32.71  0  229 TRP   C CE3 1 
ATOM   5671 C  CZ2 . TRP   C  1 214 ? 9.507   -48.469 -9.907  1.00 30.02  0  229 TRP   C CZ2 1 
ATOM   5672 C  CZ3 . TRP   C  1 214 ? 8.861   -46.137 -9.757  1.00 31.00  0  229 TRP   C CZ3 1 
ATOM   5673 C  CH2 . TRP   C  1 214 ? 8.794   -47.385 -10.374 1.00 31.94  0  229 TRP   C CH2 1 
ATOM   5674 N  N   . GLY   C  1 215 ? 9.032   -44.893 -5.377  1.00 26.33  0  230 GLY   C N   1 
ATOM   5675 C  CA  . GLY   C  1 215 ? 7.661   -44.634 -5.817  1.00 27.20  0  230 GLY   C CA  1 
ATOM   5676 C  C   . GLY   C  1 215 ? 7.613   -43.279 -6.460  1.00 28.65  0  230 GLY   C C   1 
ATOM   5677 O  O   . GLY   C  1 215 ? 8.622   -42.597 -6.439  1.00 29.50  0  230 GLY   C O   1 
ATOM   5678 N  N   A GLU   C  1 216 ? 6.475   -42.919 -7.045  0.50 29.63  0  231 GLU   C N   1 
ATOM   5679 N  N   B GLU   C  1 216 ? 6.466   -42.892 -7.015  0.50 28.87  0  231 GLU   C N   1 
ATOM   5680 C  CA  A GLU   C  1 216 ? 6.190   -41.549 -7.531  0.50 31.69  0  231 GLU   C CA  1 
ATOM   5681 C  CA  B GLU   C  1 216 ? 6.215   -41.491 -7.443  0.50 30.54  0  231 GLU   C CA  1 
ATOM   5682 C  C   A GLU   C  1 216 ? 5.584   -40.762 -6.362  0.50 30.67  0  231 GLU   C C   1 
ATOM   5683 C  C   B GLU   C  1 216 ? 5.605   -40.731 -6.259  0.50 30.41  0  231 GLU   C C   1 
ATOM   5684 O  O   A GLU   C  1 216 ? 4.384   -40.929 -6.083  0.50 32.06  0  231 GLU   C O   1 
ATOM   5685 O  O   B GLU   C  1 216 ? 4.411   -40.911 -5.974  0.50 31.32  0  231 GLU   C O   1 
ATOM   5686 C  CB  A GLU   C  1 216 ? 5.284   -41.617 -8.759  0.50 34.57  0  231 GLU   C CB  1 
ATOM   5687 C  CB  B GLU   C  1 216 ? 5.320   -41.431 -8.674  0.50 32.08  0  231 GLU   C CB  1 
ATOM   5688 C  CG  A GLU   C  1 216 ? 6.029   -41.948 -10.040 0.50 35.95  0  231 GLU   C CG  1 
ATOM   5689 C  CG  B GLU   C  1 216 ? 5.023   -40.006 -9.110  0.50 31.52  0  231 GLU   C CG  1 
ATOM   5690 C  CD  A GLU   C  1 216 ? 5.170   -41.882 -11.290 0.50 36.64  0  231 GLU   C CD  1 
ATOM   5691 C  CD  B GLU   C  1 216 ? 3.892   -39.963 -10.111 0.50 30.82  0  231 GLU   C CD  1 
ATOM   5692 O  OE1 A GLU   C  1 216 ? 4.197   -41.101 -11.276 0.50 38.36  0  231 GLU   C OE1 1 
ATOM   5693 O  OE1 B GLU   C  1 216 ? 3.907   -40.809 -11.007 0.50 31.35  0  231 GLU   C OE1 1 
ATOM   5694 O  OE2 A GLU   C  1 216 ? 5.438   -42.643 -12.248 0.50 36.01  -1 231 GLU   C OE2 1 
ATOM   5695 O  OE2 B GLU   C  1 216 ? 2.983   -39.130 -9.965  0.50 33.81  -1 231 GLU   C OE2 1 
ATOM   5696 N  N   A GLY   C  1 217 ? 6.407   -39.982 -5.669  0.50 30.72  0  232 GLY   C N   1 
ATOM   5697 N  N   B GLY   C  1 217 ? 6.416   -39.934 -5.576  0.50 32.40  0  232 GLY   C N   1 
ATOM   5698 C  CA  A GLY   C  1 217 ? 6.037   -39.313 -4.411  0.50 30.03  0  232 GLY   C CA  1 
ATOM   5699 C  CA  B GLY   C  1 217 ? 6.029   -39.297 -4.310  0.50 33.14  0  232 GLY   C CA  1 
ATOM   5700 C  C   A GLY   C  1 217 ? 5.612   -40.336 -3.375  0.50 31.31  0  232 GLY   C C   1 
ATOM   5701 C  C   B GLY   C  1 217 ? 5.568   -40.348 -3.317  0.50 36.13  0  232 GLY   C C   1 
ATOM   5702 O  O   A GLY   C  1 217 ? 6.070   -41.507 -3.453  0.50 31.08  0  232 GLY   C O   1 
ATOM   5703 O  O   B GLY   C  1 217 ? 5.929   -41.537 -3.486  0.50 35.87  0  232 GLY   C O   1 
ATOM   5704 N  N   A CYS   C  1 218 ? 4.772   -39.913 -2.434  0.50 27.67  0  233 CYS   C N   1 
ATOM   5705 N  N   B CYS   C  1 218 ? 4.810   -39.937 -2.305  0.50 34.63  0  233 CYS   C N   1 
ATOM   5706 C  CA  A CYS   C  1 218 ? 4.344   -40.724 -1.275  0.50 28.73  0  233 CYS   C CA  1 
ATOM   5707 C  CA  B CYS   C  1 218 ? 4.291   -40.851 -1.264  0.50 37.55  0  233 CYS   C CA  1 
ATOM   5708 C  C   A CYS   C  1 218 ? 2.828   -40.586 -1.147  0.50 29.55  0  233 CYS   C C   1 
ATOM   5709 C  C   B CYS   C  1 218 ? 2.789   -40.640 -1.138  0.50 36.01  0  233 CYS   C C   1 
ATOM   5710 O  O   A CYS   C  1 218 ? 2.337   -39.470 -1.232  0.50 30.80  0  233 CYS   C O   1 
ATOM   5711 O  O   B CYS   C  1 218 ? 2.333   -39.493 -1.201  0.50 36.82  0  233 CYS   C O   1 
ATOM   5712 C  CB  A CYS   C  1 218 ? 5.093   -40.302 -0.017  0.50 27.97  0  233 CYS   C CB  1 
ATOM   5713 C  CB  B CYS   C  1 218 ? 4.988   -40.651 0.074   0.50 39.62  0  233 CYS   C CB  1 
ATOM   5714 S  SG  A CYS   C  1 218 ? 6.868   -39.975 -0.266  0.50 26.10  0  233 CYS   C SG  1 
ATOM   5715 S  SG  B CYS   C  1 218 ? 4.869   -38.957 0.701   0.50 48.16  0  233 CYS   C SG  1 
ATOM   5716 N  N   A ALA   C  1 219 ? 2.129   -41.709 -1.077  0.50 30.90  0  234 ALA   C N   1 
ATOM   5717 N  N   B ALA   C  1 219 ? 2.062   -41.744 -1.065  0.50 35.83  0  234 ALA   C N   1 
ATOM   5718 C  CA  A ALA   C  1 219 ? 0.663   -41.791 -0.890  0.50 32.17  0  234 ALA   C CA  1 
ATOM   5719 C  CA  B ALA   C  1 219 ? 0.599   -41.784 -0.879  0.50 35.79  0  234 ALA   C CA  1 
ATOM   5720 C  C   A ALA   C  1 219 ? -0.085  -41.013 -1.984  0.50 33.32  0  234 ALA   C C   1 
ATOM   5721 C  C   B ALA   C  1 219 ? -0.113  -41.004 -1.993  0.50 35.30  0  234 ALA   C C   1 
ATOM   5722 O  O   A ALA   C  1 219 ? -1.151  -40.456 -1.673  0.50 33.87  0  234 ALA   C O   1 
ATOM   5723 O  O   B ALA   C  1 219 ? -1.178  -40.429 -1.700  0.50 35.56  0  234 ALA   C O   1 
ATOM   5724 C  CB  A ALA   C  1 219 ? 0.319   -41.295 0.492   0.50 32.50  0  234 ALA   C CB  1 
ATOM   5725 C  CB  B ALA   C  1 219 ? 0.272   -41.257 0.497   0.50 36.16  0  234 ALA   C CB  1 
ATOM   5726 N  N   . GLN   C  1 220 ? 0.434   -41.008 -3.218  1.00 33.33  0  235 GLN   C N   1 
ATOM   5727 C  CA  . GLN   C  1 220 ? -0.194  -40.370 -4.414  1.00 36.16  0  235 GLN   C CA  1 
ATOM   5728 C  C   . GLN   C  1 220 ? -1.185  -41.350 -5.045  1.00 35.21  0  235 GLN   C C   1 
ATOM   5729 O  O   . GLN   C  1 220 ? -0.962  -42.562 -4.999  1.00 34.65  0  235 GLN   C O   1 
ATOM   5730 C  CB  . GLN   C  1 220 ? 0.837   -39.914 -5.457  1.00 37.46  0  235 GLN   C CB  1 
ATOM   5731 C  CG  . GLN   C  1 220 ? 1.815   -38.839 -4.983  1.00 41.01  0  235 GLN   C CG  1 
ATOM   5732 C  CD  . GLN   C  1 220 ? 1.108   -37.526 -4.726  1.00 50.94  0  235 GLN   C CD  1 
ATOM   5733 O  OE1 . GLN   C  1 220 ? 1.152   -36.613 -5.539  1.00 55.65  0  235 GLN   C OE1 1 
ATOM   5734 N  NE2 . GLN   C  1 220 ? 0.426   -37.406 -3.599  1.00 55.95  0  235 GLN   C NE2 1 
ATOM   5735 N  N   . PRO   C  1 221 ? -2.307  -40.849 -5.619  1.00 38.06  0  236 PRO   C N   1 
ATOM   5736 C  CA  . PRO   C  1 221 ? -3.289  -41.701 -6.294  1.00 38.57  0  236 PRO   C CA  1 
ATOM   5737 C  C   . PRO   C  1 221 ? -2.647  -42.601 -7.364  1.00 36.70  0  236 PRO   C C   1 
ATOM   5738 O  O   . PRO   C  1 221 ? -1.891  -42.077 -8.163  1.00 33.30  0  236 PRO   C O   1 
ATOM   5739 C  CB  . PRO   C  1 221 ? -4.304  -40.729 -6.938  1.00 36.42  0  236 PRO   C CB  1 
ATOM   5740 C  CG  . PRO   C  1 221 ? -4.106  -39.406 -6.206  1.00 39.50  0  236 PRO   C CG  1 
ATOM   5741 C  CD  . PRO   C  1 221 ? -2.713  -39.427 -5.610  1.00 39.48  0  236 PRO   C CD  1 
ATOM   5742 N  N   . ASN   C  1 222 ? -2.930  -43.910 -7.312  1.00 32.93  0  237 ASN   C N   1 
ATOM   5743 C  CA  . ASN   C  1 222 ? -2.449  -44.936 -8.276  1.00 34.93  0  237 ASN   C CA  1 
ATOM   5744 C  C   . ASN   C  1 222 ? -0.915  -45.018 -8.300  1.00 29.53  0  237 ASN   C C   1 
ATOM   5745 O  O   . ASN   C  1 222 ? -0.362  -45.431 -9.330  1.00 27.56  0  237 ASN   C O   1 
ATOM   5746 C  CB  . ASN   C  1 222 ? -2.988  -44.654 -9.689  1.00 37.22  0  237 ASN   C CB  1 
ATOM   5747 C  CG  . ASN   C  1 222 ? -4.497  -44.754 -9.730  1.00 37.49  0  237 ASN   C CG  1 
ATOM   5748 O  OD1 . ASN   C  1 222 ? -5.039  -45.659 -9.120  1.00 38.47  0  237 ASN   C OD1 1 
ATOM   5749 N  ND2 . ASN   C  1 222 ? -5.165  -43.813 -10.382 1.00 37.32  0  237 ASN   C ND2 1 
ATOM   5750 N  N   . ARG   C  1 223 ? -0.246  -44.702 -7.201  1.00 28.30  0  238 ARG   C N   1 
ATOM   5751 C  CA  . ARG   C  1 223 ? 1.230   -44.800 -7.123  1.00 29.28  0  238 ARG   C CA  1 
ATOM   5752 C  C   . ARG   C  1 223 ? 1.594   -45.432 -5.792  1.00 28.51  0  238 ARG   C C   1 
ATOM   5753 O  O   . ARG   C  1 223 ? 2.156   -44.799 -4.902  1.00 30.27  0  238 ARG   C O   1 
ATOM   5754 C  CB  . ARG   C  1 223 ? 1.849   -43.427 -7.346  1.00 31.72  0  238 ARG   C CB  1 
ATOM   5755 C  CG  . ARG   C  1 223 ? 1.512   -42.785 -8.690  1.00 33.34  0  238 ARG   C CG  1 
ATOM   5756 C  CD  . ARG   C  1 223 ? 2.120   -43.474 -9.893  1.00 34.80  0  238 ARG   C CD  1 
ATOM   5757 N  NE  . ARG   C  1 223 ? 1.834   -42.721 -11.108 1.00 34.29  0  238 ARG   C NE  1 
ATOM   5758 C  CZ  . ARG   C  1 223 ? 0.795   -42.898 -11.934 1.00 31.07  0  238 ARG   C CZ  1 
ATOM   5759 N  NH1 . ARG   C  1 223 ? -0.135  -43.816 -11.713 1.00 27.58  1  238 ARG   C NH1 1 
ATOM   5760 N  NH2 . ARG   C  1 223 ? 0.668   -42.088 -12.977 1.00 34.22  0  238 ARG   C NH2 1 
ATOM   5761 N  N   . PRO   C  1 224 ? 1.286   -46.726 -5.603  1.00 30.39  0  239 PRO   C N   1 
ATOM   5762 C  CA  . PRO   C  1 224 ? 1.674   -47.400 -4.376  1.00 29.86  0  239 PRO   C CA  1 
ATOM   5763 C  C   . PRO   C  1 224 ? 3.195   -47.442 -4.216  1.00 29.03  0  239 PRO   C C   1 
ATOM   5764 O  O   . PRO   C  1 224 ? 3.943   -47.326 -5.195  1.00 27.61  0  239 PRO   C O   1 
ATOM   5765 C  CB  . PRO   C  1 224 ? 1.133   -48.823 -4.468  1.00 31.99  0  239 PRO   C CB  1 
ATOM   5766 C  CG  . PRO   C  1 224 ? 0.330   -48.887 -5.763  1.00 31.15  0  239 PRO   C CG  1 
ATOM   5767 C  CD  . PRO   C  1 224 ? 0.547   -47.603 -6.521  1.00 29.10  0  239 PRO   C CD  1 
ATOM   5768 N  N   . GLY   C  1 225 ? 3.620   -47.581 -2.966  1.00 25.31  0  240 GLY   C N   1 
ATOM   5769 C  CA  . GLY   C  1 225 ? 5.031   -47.774 -2.631  1.00 27.52  0  240 GLY   C CA  1 
ATOM   5770 C  C   . GLY   C  1 225 ? 5.596   -49.031 -3.250  1.00 24.80  0  240 GLY   C C   1 
ATOM   5771 O  O   . GLY   C  1 225 ? 4.939   -50.078 -3.168  1.00 24.37  0  240 GLY   C O   1 
ATOM   5772 N  N   . ILE   C  1 226 ? 6.807   -48.939 -3.776  1.00 24.54  0  241 ILE   C N   1 
ATOM   5773 C  CA  . ILE   C  1 226 ? 7.538   -50.092 -4.354  1.00 26.75  0  241 ILE   C CA  1 
ATOM   5774 C  C   . ILE   C  1 226 ? 8.705   -50.452 -3.444  1.00 26.35  0  241 ILE   C C   1 
ATOM   5775 O  O   . ILE   C  1 226 ? 9.385   -49.541 -2.942  1.00 24.84  0  241 ILE   C O   1 
ATOM   5776 C  CB  . ILE   C  1 226 ? 8.029   -49.796 -5.780  1.00 29.92  0  241 ILE   C CB  1 
ATOM   5777 C  CG1 . ILE   C  1 226 ? 6.986   -49.094 -6.656  1.00 31.21  0  241 ILE   C CG1 1 
ATOM   5778 C  CG2 . ILE   C  1 226 ? 8.540   -51.083 -6.433  1.00 31.55  0  241 ILE   C CG2 1 
ATOM   5779 C  CD1 . ILE   C  1 226 ? 5.698   -49.809 -6.735  1.00 31.74  0  241 ILE   C CD1 1 
ATOM   5780 N  N   . TYR   C  1 227 ? 8.931   -51.755 -3.279  1.00 26.04  0  242 TYR   C N   1 
ATOM   5781 C  CA  . TYR   C  1 227 ? 9.909   -52.366 -2.351  1.00 25.13  0  242 TYR   C CA  1 
ATOM   5782 C  C   . TYR   C  1 227 ? 10.724  -53.413 -3.128  1.00 26.62  0  242 TYR   C C   1 
ATOM   5783 O  O   . TYR   C  1 227 ? 10.168  -54.011 -4.060  1.00 28.85  0  242 TYR   C O   1 
ATOM   5784 C  CB  . TYR   C  1 227 ? 9.135   -53.013 -1.195  1.00 25.71  0  242 TYR   C CB  1 
ATOM   5785 C  CG  . TYR   C  1 227 ? 8.312   -52.063 -0.373  1.00 23.18  0  242 TYR   C CG  1 
ATOM   5786 C  CD1 . TYR   C  1 227 ? 7.078   -51.590 -0.812  1.00 27.06  0  242 TYR   C CD1 1 
ATOM   5787 C  CD2 . TYR   C  1 227 ? 8.762   -51.635 0.857   1.00 24.85  0  242 TYR   C CD2 1 
ATOM   5788 C  CE1 . TYR   C  1 227 ? 6.332   -50.709 -0.031  1.00 28.94  0  242 TYR   C CE1 1 
ATOM   5789 C  CE2 . TYR   C  1 227 ? 8.007   -50.787 1.667   1.00 25.98  0  242 TYR   C CE2 1 
ATOM   5790 C  CZ  . TYR   C  1 227 ? 6.804   -50.306 1.219   1.00 25.50  0  242 TYR   C CZ  1 
ATOM   5791 O  OH  . TYR   C  1 227 ? 6.085   -49.480 2.045   1.00 26.83  0  242 TYR   C OH  1 
ATOM   5792 N  N   . THR   C  1 228 ? 11.989  -53.618 -2.781  1.00 26.07  0  243 THR   C N   1 
ATOM   5793 C  CA  . THR   C  1 228 ? 12.760  -54.775 -3.277  1.00 28.47  0  243 THR   C CA  1 
ATOM   5794 C  C   . THR   C  1 228 ? 12.147  -56.020 -2.639  1.00 30.11  0  243 THR   C C   1 
ATOM   5795 O  O   . THR   C  1 228 ? 11.968  -56.005 -1.410  1.00 29.19  0  243 THR   C O   1 
ATOM   5796 C  CB  . THR   C  1 228 ? 14.250  -54.623 -2.989  1.00 29.20  0  243 THR   C CB  1 
ATOM   5797 O  OG1 . THR   C  1 228 ? 14.618  -53.336 -3.481  1.00 26.64  0  243 THR   C OG1 1 
ATOM   5798 C  CG2 . THR   C  1 228 ? 15.086  -55.725 -3.616  1.00 27.66  0  243 THR   C CG2 1 
ATOM   5799 N  N   . ARG   C  1 229 ? 11.774  -57.012 -3.453  1.00 29.23  0  244 ARG   C N   1 
ATOM   5800 C  CA  . ARG   C  1 229 ? 11.175  -58.299 -3.005  1.00 30.16  0  244 ARG   C CA  1 
ATOM   5801 C  C   . ARG   C  1 229 ? 12.280  -59.181 -2.404  1.00 31.26  0  244 ARG   C C   1 
ATOM   5802 O  O   . ARG   C  1 229 ? 13.183  -59.608 -3.143  1.00 30.83  0  244 ARG   C O   1 
ATOM   5803 C  CB  . ARG   C  1 229 ? 10.449  -58.979 -4.174  1.00 31.72  0  244 ARG   C CB  1 
ATOM   5804 C  CG  . ARG   C  1 229 ? 9.707   -60.246 -3.782  1.00 33.90  0  244 ARG   C CG  1 
ATOM   5805 C  CD  . ARG   C  1 229 ? 9.064   -60.880 -5.002  1.00 37.42  0  244 ARG   C CD  1 
ATOM   5806 N  NE  . ARG   C  1 229 ? 7.899   -60.133 -5.456  1.00 39.04  0  244 ARG   C NE  1 
ATOM   5807 C  CZ  . ARG   C  1 229 ? 6.680   -60.178 -4.901  1.00 46.30  0  244 ARG   C CZ  1 
ATOM   5808 N  NH1 . ARG   C  1 229 ? 6.433   -60.937 -3.844  1.00 47.88  1  244 ARG   C NH1 1 
ATOM   5809 N  NH2 . ARG   C  1 229 ? 5.699   -59.441 -5.399  1.00 51.93  0  244 ARG   C NH2 1 
ATOM   5810 N  N   . VAL   C  1 230 ? 12.273  -59.382 -1.081  1.00 30.33  0  245 VAL   C N   1 
ATOM   5811 C  CA  . VAL   C  1 230 ? 13.431  -60.030 -0.400  1.00 30.20  0  245 VAL   C CA  1 
ATOM   5812 C  C   . VAL   C  1 230 ? 13.550  -61.478 -0.910  1.00 25.18  0  245 VAL   C C   1 
ATOM   5813 O  O   . VAL   C  1 230 ? 14.672  -61.913 -1.110  1.00 24.98  0  245 VAL   C O   1 
ATOM   5814 C  CB  . VAL   C  1 230 ? 13.338  -59.921 1.134   1.00 32.93  0  245 VAL   C CB  1 
ATOM   5815 C  CG1 . VAL   C  1 230 ? 14.318  -60.858 1.844   1.00 31.68  0  245 VAL   C CG1 1 
ATOM   5816 C  CG2 . VAL   C  1 230 ? 13.580  -58.468 1.558   1.00 33.06  0  245 VAL   C CG2 1 
ATOM   5817 N  N   . THR   C  1 231 ? 12.448  -62.188 -1.112  1.00 26.24  0  246 THR   C N   1 
ATOM   5818 C  CA  . THR   C  1 231 ? 12.496  -63.612 -1.551  1.00 30.79  0  246 THR   C CA  1 
ATOM   5819 C  C   . THR   C  1 231 ? 13.305  -63.704 -2.844  1.00 34.18  0  246 THR   C C   1 
ATOM   5820 O  O   . THR   C  1 231 ? 14.049  -64.682 -2.999  1.00 33.90  0  246 THR   C O   1 
ATOM   5821 C  CB  . THR   C  1 231 ? 11.114  -64.239 -1.754  1.00 33.46  0  246 THR   C CB  1 
ATOM   5822 O  OG1 . THR   C  1 231 ? 10.345  -63.451 -2.666  1.00 28.93  0  246 THR   C OG1 1 
ATOM   5823 C  CG2 . THR   C  1 231 ? 10.345  -64.412 -0.451  1.00 31.01  0  246 THR   C CG2 1 
ATOM   5824 N  N   . TYR   C  1 232 ? 13.216  -62.691 -3.717  1.00 35.92  0  247 TYR   C N   1 
ATOM   5825 C  CA  . TYR   C  1 232 ? 13.932  -62.675 -5.014  1.00 31.78  0  247 TYR   C CA  1 
ATOM   5826 C  C   . TYR   C  1 232 ? 15.438  -62.747 -4.795  1.00 28.51  0  247 TYR   C C   1 
ATOM   5827 O  O   . TYR   C  1 232 ? 16.093  -63.364 -5.626  1.00 28.55  0  247 TYR   C O   1 
ATOM   5828 C  CB  . TYR   C  1 232 ? 13.569  -61.465 -5.877  1.00 31.04  0  247 TYR   C CB  1 
ATOM   5829 C  CG  . TYR   C  1 232 ? 13.960  -61.606 -7.331  1.00 27.66  0  247 TYR   C CG  1 
ATOM   5830 C  CD1 . TYR   C  1 232 ? 15.260  -61.339 -7.747  1.00 30.12  0  247 TYR   C CD1 1 
ATOM   5831 C  CD2 . TYR   C  1 232 ? 13.034  -61.970 -8.291  1.00 31.85  0  247 TYR   C CD2 1 
ATOM   5832 C  CE1 . TYR   C  1 232 ? 15.643  -61.457 -9.072  1.00 28.71  0  247 TYR   C CE1 1 
ATOM   5833 C  CE2 . TYR   C  1 232 ? 13.394  -62.066 -9.633  1.00 32.34  0  247 TYR   C CE2 1 
ATOM   5834 C  CZ  . TYR   C  1 232 ? 14.703  -61.822 -10.018 1.00 33.32  0  247 TYR   C CZ  1 
ATOM   5835 O  OH  . TYR   C  1 232 ? 15.120  -61.928 -11.318 1.00 33.95  0  247 TYR   C OH  1 
ATOM   5836 N  N   . TYR   C  1 233 ? 15.978  -62.120 -3.751  1.00 33.20  0  248 TYR   C N   1 
ATOM   5837 C  CA  . TYR   C  1 233 ? 17.448  -61.981 -3.550  1.00 30.51  0  248 TYR   C CA  1 
ATOM   5838 C  C   . TYR   C  1 233 ? 17.957  -62.859 -2.391  1.00 29.46  0  248 TYR   C C   1 
ATOM   5839 O  O   . TYR   C  1 233 ? 19.135  -62.639 -1.964  1.00 29.31  0  248 TYR   C O   1 
ATOM   5840 C  CB  . TYR   C  1 233 ? 17.795  -60.485 -3.421  1.00 30.79  0  248 TYR   C CB  1 
ATOM   5841 C  CG  . TYR   C  1 233 ? 17.630  -59.754 -4.728  1.00 29.74  0  248 TYR   C CG  1 
ATOM   5842 C  CD1 . TYR   C  1 233 ? 18.476  -60.015 -5.799  1.00 30.26  0  248 TYR   C CD1 1 
ATOM   5843 C  CD2 . TYR   C  1 233 ? 16.549  -58.900 -4.943  1.00 30.26  0  248 TYR   C CD2 1 
ATOM   5844 C  CE1 . TYR   C  1 233 ? 18.293  -59.411 -7.028  1.00 28.32  0  248 TYR   C CE1 1 
ATOM   5845 C  CE2 . TYR   C  1 233 ? 16.370  -58.262 -6.166  1.00 29.68  0  248 TYR   C CE2 1 
ATOM   5846 C  CZ  . TYR   C  1 233 ? 17.228  -58.540 -7.217  1.00 29.20  0  248 TYR   C CZ  1 
ATOM   5847 O  OH  . TYR   C  1 233 ? 17.060  -57.968 -8.442  1.00 28.07  0  248 TYR   C OH  1 
ATOM   5848 N  N   . LEU   C  1 234 ? 17.214  -63.885 -1.956  1.00 32.08  0  249 LEU   C N   1 
ATOM   5849 C  CA  . LEU   C  1 234 ? 17.669  -64.777 -0.834  1.00 33.17  0  249 LEU   C CA  1 
ATOM   5850 C  C   . LEU   C  1 234 ? 19.003  -65.425 -1.152  1.00 33.44  0  249 LEU   C C   1 
ATOM   5851 O  O   . LEU   C  1 234 ? 19.878  -65.389 -0.271  1.00 38.39  0  249 LEU   C O   1 
ATOM   5852 C  CB  . LEU   C  1 234 ? 16.625  -65.842 -0.520  1.00 35.19  0  249 LEU   C CB  1 
ATOM   5853 C  CG  . LEU   C  1 234 ? 15.461  -65.356 0.331   1.00 40.39  0  249 LEU   C CG  1 
ATOM   5854 C  CD1 . LEU   C  1 234 ? 14.316  -66.368 0.284   1.00 40.32  0  249 LEU   C CD1 1 
ATOM   5855 C  CD2 . LEU   C  1 234 ? 15.885  -65.065 1.775   1.00 40.49  0  249 LEU   C CD2 1 
ATOM   5856 N  N   . ASP   C  1 235 ? 19.207  -65.933 -2.374  1.00 38.43  0  250 ASP   C N   1 
ATOM   5857 C  CA  . ASP   C  1 235 ? 20.478  -66.629 -2.717  1.00 40.08  0  250 ASP   C CA  1 
ATOM   5858 C  C   . ASP   C  1 235 ? 21.646  -65.657 -2.612  1.00 39.57  0  250 ASP   C C   1 
ATOM   5859 O  O   . ASP   C  1 235 ? 22.705  -66.072 -2.128  1.00 38.11  0  250 ASP   C O   1 
ATOM   5860 C  CB  . ASP   C  1 235 ? 20.459  -67.282 -4.097  1.00 43.77  0  250 ASP   C CB  1 
ATOM   5861 C  CG  . ASP   C  1 235 ? 19.421  -68.377 -4.207  1.00 49.15  0  250 ASP   C CG  1 
ATOM   5862 O  OD1 . ASP   C  1 235 ? 18.993  -68.886 -3.154  1.00 52.40  0  250 ASP   C OD1 1 
ATOM   5863 O  OD2 . ASP   C  1 235 ? 19.010  -68.674 -5.348  1.00 62.84  -1 250 ASP   C OD2 1 
ATOM   5864 N  N   . TRP   C  1 236 ? 21.473  -64.423 -3.082  1.00 35.60  0  251 TRP   C N   1 
ATOM   5865 C  CA  . TRP   C  1 236 ? 22.516  -63.363 -2.978  1.00 32.64  0  251 TRP   C CA  1 
ATOM   5866 C  C   . TRP   C  1 236 ? 22.755  -63.004 -1.500  1.00 29.56  0  251 TRP   C C   1 
ATOM   5867 O  O   . TRP   C  1 236 ? 23.899  -62.931 -1.066  1.00 27.89  0  251 TRP   C O   1 
ATOM   5868 C  CB  . TRP   C  1 236 ? 22.112  -62.137 -3.826  1.00 31.03  0  251 TRP   C CB  1 
ATOM   5869 C  CG  . TRP   C  1 236 ? 23.129  -61.054 -3.783  1.00 27.64  0  251 TRP   C CG  1 
ATOM   5870 C  CD1 . TRP   C  1 236 ? 24.272  -60.996 -4.498  1.00 29.54  0  251 TRP   C CD1 1 
ATOM   5871 C  CD2 . TRP   C  1 236 ? 23.142  -59.918 -2.902  1.00 30.09  0  251 TRP   C CD2 1 
ATOM   5872 N  NE1 . TRP   C  1 236 ? 24.993  -59.890 -4.134  1.00 32.60  0  251 TRP   C NE1 1 
ATOM   5873 C  CE2 . TRP   C  1 236 ? 24.317  -59.198 -3.176  1.00 28.75  0  251 TRP   C CE2 1 
ATOM   5874 C  CE3 . TRP   C  1 236 ? 22.276  -59.438 -1.911  1.00 29.78  0  251 TRP   C CE3 1 
ATOM   5875 C  CZ2 . TRP   C  1 236 ? 24.651  -58.011 -2.519  1.00 33.29  0  251 TRP   C CZ2 1 
ATOM   5876 C  CZ3 . TRP   C  1 236 ? 22.605  -58.266 -1.254  1.00 30.67  0  251 TRP   C CZ3 1 
ATOM   5877 C  CH2 . TRP   C  1 236 ? 23.778  -57.560 -1.558  1.00 29.64  0  251 TRP   C CH2 1 
ATOM   5878 N  N   . ILE   C  1 237 ? 21.709  -62.772 -0.725  1.00 32.21  0  252 ILE   C N   1 
ATOM   5879 C  CA  . ILE   C  1 237 ? 21.867  -62.439 0.730   1.00 35.64  0  252 ILE   C CA  1 
ATOM   5880 C  C   . ILE   C  1 237 ? 22.652  -63.586 1.404   1.00 36.28  0  252 ILE   C C   1 
ATOM   5881 O  O   . ILE   C  1 237 ? 23.694  -63.316 2.042   1.00 33.62  0  252 ILE   C O   1 
ATOM   5882 C  CB  . ILE   C  1 237 ? 20.493  -62.206 1.397   1.00 33.27  0  252 ILE   C CB  1 
ATOM   5883 C  CG1 . ILE   C  1 237 ? 19.830  -60.932 0.880   1.00 30.75  0  252 ILE   C CG1 1 
ATOM   5884 C  CG2 . ILE   C  1 237 ? 20.609  -62.202 2.927   1.00 35.02  0  252 ILE   C CG2 1 
ATOM   5885 C  CD1 . ILE   C  1 237 ? 18.352  -60.900 1.139   1.00 32.97  0  252 ILE   C CD1 1 
ATOM   5886 N  N   . HIS   C  1 238 ? 22.207  -64.834 1.212   1.00 38.94  0  253 HIS   C N   1 
ATOM   5887 C  CA  . HIS   C  1 238 ? 22.781  -66.056 1.869   1.00 41.24  0  253 HIS   C CA  1 
ATOM   5888 C  C   . HIS   C  1 238 ? 24.184  -66.361 1.359   1.00 38.81  0  253 HIS   C C   1 
ATOM   5889 O  O   . HIS   C  1 238 ? 24.909  -67.092 2.031   1.00 45.38  0  253 HIS   C O   1 
ATOM   5890 C  CB  . HIS   C  1 238 ? 21.830  -67.250 1.743   1.00 37.02  0  253 HIS   C CB  1 
ATOM   5891 C  CG  . HIS   C  1 238 ? 20.635  -67.107 2.613   1.00 37.89  0  253 HIS   C CG  1 
ATOM   5892 N  ND1 . HIS   C  1 238 ? 20.724  -66.560 3.903   1.00 44.08  0  253 HIS   C ND1 1 
ATOM   5893 C  CD2 . HIS   C  1 238 ? 19.338  -67.439 2.425   1.00 37.74  0  253 HIS   C CD2 1 
ATOM   5894 C  CE1 . HIS   C  1 238 ? 19.527  -66.584 4.471   1.00 39.82  0  253 HIS   C CE1 1 
ATOM   5895 N  NE2 . HIS   C  1 238 ? 18.649  -67.074 3.565   1.00 41.50  0  253 HIS   C NE2 1 
ATOM   5896 N  N   . HIS   C  1 239 ? 24.608  -65.775 0.253   1.00 40.59  0  254 HIS   C N   1 
ATOM   5897 C  CA  . HIS   C  1 239 ? 26.017  -65.857 -0.206  1.00 38.15  0  254 HIS   C CA  1 
ATOM   5898 C  C   . HIS   C  1 239 ? 26.968  -65.188 0.783   1.00 43.50  0  254 HIS   C C   1 
ATOM   5899 O  O   . HIS   C  1 239 ? 28.177  -65.544 0.776   1.00 41.92  0  254 HIS   C O   1 
ATOM   5900 C  CB  . HIS   C  1 239 ? 26.142  -65.238 -1.597  1.00 41.74  0  254 HIS   C CB  1 
ATOM   5901 C  CG  . HIS   C  1 239 ? 27.464  -65.433 -2.231  1.00 43.44  0  254 HIS   C CG  1 
ATOM   5902 N  ND1 . HIS   C  1 239 ? 27.727  -66.513 -3.063  1.00 46.64  0  254 HIS   C ND1 1 
ATOM   5903 C  CD2 . HIS   C  1 239 ? 28.597  -64.710 -2.139  1.00 47.21  0  254 HIS   C CD2 1 
ATOM   5904 C  CE1 . HIS   C  1 239 ? 28.972  -66.429 -3.481  1.00 47.06  0  254 HIS   C CE1 1 
ATOM   5905 N  NE2 . HIS   C  1 239 ? 29.538  -65.337 -2.911  1.00 51.90  0  254 HIS   C NE2 1 
ATOM   5906 N  N   . TYR   C  1 240 ? 26.488  -64.194 1.552   1.00 40.38  0  255 TYR   C N   1 
ATOM   5907 C  CA  . TYR   C  1 240 ? 27.327  -63.406 2.490   1.00 39.23  0  255 TYR   C CA  1 
ATOM   5908 C  C   . TYR   C  1 240 ? 26.912  -63.643 3.948   1.00 37.71  0  255 TYR   C C   1 
ATOM   5909 O  O   . TYR   C  1 240 ? 27.788  -63.503 4.824   1.00 39.63  0  255 TYR   C O   1 
ATOM   5910 C  CB  . TYR   C  1 240 ? 27.234  -61.916 2.145   1.00 41.98  0  255 TYR   C CB  1 
ATOM   5911 C  CG  . TYR   C  1 240 ? 27.706  -61.588 0.753   1.00 38.16  0  255 TYR   C CG  1 
ATOM   5912 C  CD1 . TYR   C  1 240 ? 29.057  -61.521 0.466   1.00 38.98  0  255 TYR   C CD1 1 
ATOM   5913 C  CD2 . TYR   C  1 240 ? 26.806  -61.397 -0.278  1.00 35.93  0  255 TYR   C CD2 1 
ATOM   5914 C  CE1 . TYR   C  1 240 ? 29.503  -61.273 -0.818  1.00 40.28  0  255 TYR   C CE1 1 
ATOM   5915 C  CE2 . TYR   C  1 240 ? 27.230  -61.149 -1.568  1.00 39.05  0  255 TYR   C CE2 1 
ATOM   5916 C  CZ  . TYR   C  1 240 ? 28.585  -61.077 -1.835  1.00 39.07  0  255 TYR   C CZ  1 
ATOM   5917 O  OH  . TYR   C  1 240 ? 29.033  -60.831 -3.093  1.00 42.01  0  255 TYR   C OH  1 
ATOM   5918 N  N   . VAL   C  1 241 ? 25.635  -63.919 4.213   1.00 35.54  0  256 VAL   C N   1 
ATOM   5919 C  CA  . VAL   C  1 241 ? 25.047  -63.891 5.578   1.00 42.36  0  256 VAL   C CA  1 
ATOM   5920 C  C   . VAL   C  1 241 ? 24.746  -65.326 5.981   1.00 47.59  0  256 VAL   C C   1 
ATOM   5921 O  O   . VAL   C  1 241 ? 23.875  -65.944 5.374   1.00 41.87  0  256 VAL   C O   1 
ATOM   5922 C  CB  . VAL   C  1 241 ? 23.790  -63.004 5.667   1.00 41.30  0  256 VAL   C CB  1 
ATOM   5923 C  CG1 . VAL   C  1 241 ? 23.205  -62.969 7.081   1.00 40.23  0  256 VAL   C CG1 1 
ATOM   5924 C  CG2 . VAL   C  1 241 ? 24.094  -61.591 5.202   1.00 40.57  0  256 VAL   C CG2 1 
ATOM   5925 N  N   . PRO   C  1 242 ? 25.446  -65.869 7.012   1.00 55.82  0  257 PRO   C N   1 
ATOM   5926 C  CA  . PRO   C  1 242 ? 25.145  -67.196 7.554   1.00 59.86  0  257 PRO   C CA  1 
ATOM   5927 C  C   . PRO   C  1 242 ? 23.665  -67.465 7.851   1.00 61.43  0  257 PRO   C C   1 
ATOM   5928 O  O   . PRO   C  1 242 ? 23.002  -66.555 8.318   1.00 65.33  0  257 PRO   C O   1 
ATOM   5929 C  CB  . PRO   C  1 242 ? 25.941  -67.206 8.863   1.00 56.53  0  257 PRO   C CB  1 
ATOM   5930 C  CG  . PRO   C  1 242 ? 27.164  -66.377 8.530   1.00 58.33  0  257 PRO   C CG  1 
ATOM   5931 C  CD  . PRO   C  1 242 ? 26.594  -65.243 7.699   1.00 59.19  0  257 PRO   C CD  1 
ATOM   5932 N  N   . LYS   C  1 243 ? 23.211  -68.695 7.569   1.00 67.70  0  258 LYS   C N   1 
ATOM   5933 C  CA  . LYS   C  1 243 ? 21.812  -69.170 7.759   1.00 73.98  0  258 LYS   C CA  1 
ATOM   5934 C  C   . LYS   C  1 243 ? 21.691  -69.840 9.138   1.00 74.28  0  258 LYS   C C   1 
ATOM   5935 O  O   . LYS   C  1 243 ? 21.647  -69.118 10.146  1.00 79.86  0  258 LYS   C O   1 
ATOM   5936 C  CB  . LYS   C  1 243 ? 21.419  -70.114 6.616   1.00 69.26  0  258 LYS   C CB  1 
ATOM   5937 C  CG  . LYS   C  1 243 ? 22.118  -71.503 6.637   0.00 76.75  0  258 LYS   C CG  1 
ATOM   5938 C  CD  . LYS   C  1 243 ? 21.699  -72.399 5.493   0.00 76.54  0  258 LYS   C CD  1 
ATOM   5939 C  CE  . LYS   C  1 243 ? 22.325  -73.776 5.569   0.00 76.29  0  258 LYS   C CE  1 
ATOM   5940 N  NZ  . LYS   C  1 243 ? 21.897  -74.636 4.441   0.00 76.18  1  258 LYS   C NZ  1 
ATOM   5941 N  N   . ILE   D  1 1   ? 24.411  -20.258 20.554  1.00 24.95  0  16  ILE   D N   1 
ATOM   5942 C  CA  . ILE   D  1 1   ? 25.643  -19.874 21.315  1.00 26.60  0  16  ILE   D CA  1 
ATOM   5943 C  C   . ILE   D  1 1   ? 26.891  -20.173 20.458  1.00 26.20  0  16  ILE   D C   1 
ATOM   5944 O  O   . ILE   D  1 1   ? 27.033  -21.320 19.973  1.00 26.10  0  16  ILE   D O   1 
ATOM   5945 C  CB  . ILE   D  1 1   ? 25.671  -20.572 22.687  1.00 25.53  0  16  ILE   D CB  1 
ATOM   5946 C  CG1 . ILE   D  1 1   ? 24.508  -20.129 23.590  1.00 27.42  0  16  ILE   D CG1 1 
ATOM   5947 C  CG2 . ILE   D  1 1   ? 27.020  -20.425 23.386  1.00 25.11  0  16  ILE   D CG2 1 
ATOM   5948 C  CD1 . ILE   D  1 1   ? 24.654  -18.740 24.201  1.00 25.27  0  16  ILE   D CD1 1 
ATOM   5949 N  N   . VAL   D  1 2   ? 27.762  -19.176 20.286  1.00 27.17  0  17  VAL   D N   1 
ATOM   5950 C  CA  . VAL   D  1 2   ? 29.071  -19.326 19.579  1.00 28.25  0  17  VAL   D CA  1 
ATOM   5951 C  C   . VAL   D  1 2   ? 30.162  -19.558 20.620  1.00 25.99  0  17  VAL   D C   1 
ATOM   5952 O  O   . VAL   D  1 2   ? 30.236  -18.779 21.560  1.00 27.79  0  17  VAL   D O   1 
ATOM   5953 C  CB  . VAL   D  1 2   ? 29.423  -18.116 18.700  1.00 29.21  0  17  VAL   D CB  1 
ATOM   5954 C  CG1 . VAL   D  1 2   ? 30.721  -18.350 17.935  1.00 31.24  0  17  VAL   D CG1 1 
ATOM   5955 C  CG2 . VAL   D  1 2   ? 28.289  -17.768 17.748  1.00 30.02  0  17  VAL   D CG2 1 
ATOM   5956 N  N   . GLY   D  1 3   ? 31.022  -20.557 20.415  1.00 28.74  0  18  GLY   D N   1 
ATOM   5957 C  CA  . GLY   D  1 3   ? 32.035  -20.964 21.411  1.00 28.88  0  18  GLY   D CA  1 
ATOM   5958 C  C   . GLY   D  1 3   ? 31.376  -21.692 22.577  1.00 33.69  0  18  GLY   D C   1 
ATOM   5959 O  O   . GLY   D  1 3   ? 30.195  -22.115 22.478  1.00 36.85  0  18  GLY   D O   1 
ATOM   5960 N  N   . GLY   D  1 4   ? 32.091  -21.882 23.678  1.00 38.13  0  19  GLY   D N   1 
ATOM   5961 C  CA  . GLY   D  1 4   ? 31.497  -22.483 24.897  1.00 39.10  0  19  GLY   D CA  1 
ATOM   5962 C  C   . GLY   D  1 4   ? 31.202  -23.965 24.720  1.00 39.26  0  19  GLY   D C   1 
ATOM   5963 O  O   . GLY   D  1 4   ? 31.901  -24.593 23.894  1.00 42.34  0  19  GLY   D O   1 
ATOM   5964 N  N   . GLN   D  1 5   ? 30.200  -24.496 25.423  1.00 34.09  0  20  GLN   D N   1 
ATOM   5965 C  CA  . GLN   D  1 5   ? 29.976  -25.959 25.512  1.00 37.14  0  20  GLN   D CA  1 
ATOM   5966 C  C   . GLN   D  1 5   ? 28.552  -26.254 25.971  1.00 34.59  0  20  GLN   D C   1 
ATOM   5967 O  O   . GLN   D  1 5   ? 27.832  -25.300 26.367  1.00 30.65  0  20  GLN   D O   1 
ATOM   5968 C  CB  . GLN   D  1 5   ? 30.964  -26.545 26.512  1.00 45.32  0  20  GLN   D CB  1 
ATOM   5969 C  CG  . GLN   D  1 5   ? 30.890  -25.868 27.872  1.00 54.17  0  20  GLN   D CG  1 
ATOM   5970 C  CD  . GLN   D  1 5   ? 32.252  -25.432 28.352  1.00 62.99  0  20  GLN   D CD  1 
ATOM   5971 O  OE1 . GLN   D  1 5   ? 33.008  -24.816 27.598  1.00 78.09  0  20  GLN   D OE1 1 
ATOM   5972 N  NE2 . GLN   D  1 5   ? 32.577  -25.738 29.601  1.00 60.76  0  20  GLN   D NE2 1 
ATOM   5973 N  N   . GLU   D  1 6   ? 28.191  -27.529 25.938  1.00 29.21  0  21  GLU   D N   1 
ATOM   5974 C  CA  . GLU   D  1 6   ? 26.908  -28.010 26.469  1.00 32.79  0  21  GLU   D CA  1 
ATOM   5975 C  C   . GLU   D  1 6   ? 26.909  -27.693 27.959  1.00 31.30  0  21  GLU   D C   1 
ATOM   5976 O  O   . GLU   D  1 6   ? 27.915  -27.936 28.595  1.00 35.37  0  21  GLU   D O   1 
ATOM   5977 C  CB  . GLU   D  1 6   ? 26.751  -29.498 26.185  1.00 34.29  0  21  GLU   D CB  1 
ATOM   5978 C  CG  . GLU   D  1 6   ? 25.598  -30.129 26.947  1.00 42.38  0  21  GLU   D CG  1 
ATOM   5979 C  CD  . GLU   D  1 6   ? 25.105  -31.465 26.394  1.00 45.44  0  21  GLU   D CD  1 
ATOM   5980 O  OE1 . GLU   D  1 6   ? 25.770  -31.977 25.417  1.00 45.75  0  21  GLU   D OE1 1 
ATOM   5981 O  OE2 . GLU   D  1 6   ? 24.037  -31.979 26.916  1.00 35.33  -1 21  GLU   D OE2 1 
ATOM   5982 N  N   . ALA   D  1 7   ? 25.802  -27.190 28.475  1.00 31.08  0  22  ALA   D N   1 
ATOM   5983 C  CA  . ALA   D  1 7   ? 25.642  -26.812 29.900  1.00 32.78  0  22  ALA   D CA  1 
ATOM   5984 C  C   . ALA   D  1 7   ? 25.472  -28.083 30.718  1.00 31.32  0  22  ALA   D C   1 
ATOM   5985 O  O   . ALA   D  1 7   ? 24.737  -28.953 30.281  1.00 29.00  0  22  ALA   D O   1 
ATOM   5986 C  CB  . ALA   D  1 7   ? 24.421  -25.942 30.081  1.00 30.72  0  22  ALA   D CB  1 
ATOM   5987 N  N   . PRO   D  1 8   ? 26.117  -28.217 31.889  1.00 31.54  0  23  PRO   D N   1 
ATOM   5988 C  CA  . PRO   D  1 8   ? 25.767  -29.275 32.837  1.00 33.43  0  23  PRO   D CA  1 
ATOM   5989 C  C   . PRO   D  1 8   ? 24.281  -29.148 33.224  1.00 33.27  0  23  PRO   D C   1 
ATOM   5990 O  O   . PRO   D  1 8   ? 23.774  -28.017 33.286  1.00 31.28  0  23  PRO   D O   1 
ATOM   5991 C  CB  . PRO   D  1 8   ? 26.654  -29.014 34.073  1.00 35.67  0  23  PRO   D CB  1 
ATOM   5992 C  CG  . PRO   D  1 8   ? 27.744  -28.064 33.620  1.00 35.92  0  23  PRO   D CG  1 
ATOM   5993 C  CD  . PRO   D  1 8   ? 27.203  -27.353 32.389  1.00 37.82  0  23  PRO   D CD  1 
ATOM   5994 N  N   . ARG   D  1 9   ? 23.627  -30.282 33.506  1.00 33.89  0  24  ARG   D N   1 
ATOM   5995 C  CA  . ARG   D  1 9   ? 22.198  -30.399 33.908  1.00 36.72  0  24  ARG   D CA  1 
ATOM   5996 C  C   . ARG   D  1 9   ? 21.871  -29.527 35.122  1.00 31.09  0  24  ARG   D C   1 
ATOM   5997 O  O   . ARG   D  1 9   ? 20.739  -29.078 35.203  1.00 33.12  0  24  ARG   D O   1 
ATOM   5998 C  CB  . ARG   D  1 9   ? 21.831  -31.852 34.228  1.00 41.11  0  24  ARG   D CB  1 
ATOM   5999 C  CG  . ARG   D  1 9   ? 21.966  -32.775 33.033  1.00 53.31  0  24  ARG   D CG  1 
ATOM   6000 C  CD  . ARG   D  1 9   ? 21.481  -34.184 33.303  1.00 55.97  0  24  ARG   D CD  1 
ATOM   6001 N  NE  . ARG   D  1 9   ? 21.165  -34.831 32.033  1.00 60.77  0  24  ARG   D NE  1 
ATOM   6002 C  CZ  . ARG   D  1 9   ? 19.998  -34.752 31.379  1.00 54.08  0  24  ARG   D CZ  1 
ATOM   6003 N  NH1 . ARG   D  1 9   ? 18.981  -34.043 31.855  1.00 47.97  1  24  ARG   D NH1 1 
ATOM   6004 N  NH2 . ARG   D  1 9   ? 19.867  -35.375 30.217  1.00 61.67  0  24  ARG   D NH2 1 
ATOM   6005 N  N   . SER   D  1 10  ? 22.819  -29.336 36.043  1.00 33.14  0  25  SER   D N   1 
ATOM   6006 C  CA  . SER   D  1 10  ? 22.637  -28.587 37.317  1.00 37.32  0  25  SER   D CA  1 
ATOM   6007 C  C   . SER   D  1 10  ? 22.729  -27.067 37.116  1.00 35.09  0  25  SER   D C   1 
ATOM   6008 O  O   . SER   D  1 10  ? 22.459  -26.348 38.110  1.00 38.58  0  25  SER   D O   1 
ATOM   6009 C  CB  . SER   D  1 10  ? 23.647  -29.030 38.357  1.00 35.35  0  25  SER   D CB  1 
ATOM   6010 O  OG  . SER   D  1 10  ? 24.968  -28.782 37.894  1.00 36.89  0  25  SER   D OG  1 
ATOM   6011 N  N   . LYS   D  1 11  ? 23.117  -26.572 35.932  1.00 35.78  0  26  LYS   D N   1 
ATOM   6012 C  CA  . LYS   D  1 11  ? 23.327  -25.108 35.721  1.00 30.51  0  26  LYS   D CA  1 
ATOM   6013 C  C   . LYS   D  1 11  ? 22.122  -24.503 34.995  1.00 28.06  0  26  LYS   D C   1 
ATOM   6014 O  O   . LYS   D  1 11  ? 21.476  -25.194 34.205  1.00 28.02  0  26  LYS   D O   1 
ATOM   6015 C  CB  . LYS   D  1 11  ? 24.651  -24.825 35.024  1.00 31.38  0  26  LYS   D CB  1 
ATOM   6016 C  CG  . LYS   D  1 11  ? 25.890  -25.324 35.754  1.00 36.94  0  26  LYS   D CG  1 
ATOM   6017 C  CD  . LYS   D  1 11  ? 26.359  -24.450 36.885  1.00 39.54  0  26  LYS   D CD  1 
ATOM   6018 C  CE  . LYS   D  1 11  ? 27.738  -24.974 37.377  0.00 39.43  0  26  LYS   D CE  1 
ATOM   6019 N  NZ  . LYS   D  1 11  ? 27.631  -26.215 38.180  0.00 39.55  1  26  LYS   D NZ  1 
ATOM   6020 N  N   . TRP   D  1 12  ? 21.844  -23.229 35.281  1.00 29.35  0  27  TRP   D N   1 
ATOM   6021 C  CA  . TRP   D  1 12  ? 20.862  -22.361 34.576  1.00 26.44  0  27  TRP   D CA  1 
ATOM   6022 C  C   . TRP   D  1 12  ? 19.442  -22.905 34.730  1.00 26.28  0  27  TRP   D C   1 
ATOM   6023 O  O   . TRP   D  1 12  ? 18.754  -23.180 33.734  1.00 26.22  0  27  TRP   D O   1 
ATOM   6024 C  CB  . TRP   D  1 12  ? 21.241  -22.214 33.111  1.00 24.98  0  27  TRP   D CB  1 
ATOM   6025 C  CG  . TRP   D  1 12  ? 22.710  -22.270 32.834  1.00 23.89  0  27  TRP   D CG  1 
ATOM   6026 C  CD1 . TRP   D  1 12  ? 23.338  -23.136 32.005  1.00 25.94  0  27  TRP   D CD1 1 
ATOM   6027 C  CD2 . TRP   D  1 12  ? 23.733  -21.433 33.383  1.00 26.73  0  27  TRP   D CD2 1 
ATOM   6028 N  NE1 . TRP   D  1 12  ? 24.682  -22.902 31.991  1.00 25.21  0  27  TRP   D NE1 1 
ATOM   6029 C  CE2 . TRP   D  1 12  ? 24.955  -21.867 32.831  1.00 24.71  0  27  TRP   D CE2 1 
ATOM   6030 C  CE3 . TRP   D  1 12  ? 23.743  -20.361 34.293  1.00 25.76  0  27  TRP   D CE3 1 
ATOM   6031 C  CZ2 . TRP   D  1 12  ? 26.177  -21.268 33.159  1.00 27.57  0  27  TRP   D CZ2 1 
ATOM   6032 C  CZ3 . TRP   D  1 12  ? 24.950  -19.775 34.617  1.00 27.94  0  27  TRP   D CZ3 1 
ATOM   6033 C  CH2 . TRP   D  1 12  ? 26.143  -20.210 34.046  1.00 26.02  0  27  TRP   D CH2 1 
ATOM   6034 N  N   . PRO   D  1 13  ? 18.946  -23.081 35.974  1.00 26.82  0  28  PRO   D N   1 
ATOM   6035 C  CA  . PRO   D  1 13  ? 17.597  -23.630 36.195  1.00 28.09  0  28  PRO   D CA  1 
ATOM   6036 C  C   . PRO   D  1 13  ? 16.461  -22.690 35.758  1.00 24.47  0  28  PRO   D C   1 
ATOM   6037 O  O   . PRO   D  1 13  ? 15.303  -23.076 35.745  1.00 25.96  0  28  PRO   D O   1 
ATOM   6038 C  CB  . PRO   D  1 13  ? 17.550  -23.857 37.718  1.00 28.12  0  28  PRO   D CB  1 
ATOM   6039 C  CG  . PRO   D  1 13  ? 18.566  -22.867 38.292  1.00 27.29  0  28  PRO   D CG  1 
ATOM   6040 C  CD  . PRO   D  1 13  ? 19.648  -22.809 37.239  1.00 28.24  0  28  PRO   D CD  1 
ATOM   6041 N  N   . TRP   D  1 14  ? 16.816  -21.456 35.446  1.00 23.38  0  29  TRP   D N   1 
ATOM   6042 C  CA  . TRP   D  1 14  ? 15.883  -20.396 34.999  1.00 24.06  0  29  TRP   D CA  1 
ATOM   6043 C  C   . TRP   D  1 14  ? 15.743  -20.339 33.472  1.00 23.70  0  29  TRP   D C   1 
ATOM   6044 O  O   . TRP   D  1 14  ? 14.804  -19.663 33.031  1.00 25.63  0  29  TRP   D O   1 
ATOM   6045 C  CB  . TRP   D  1 14  ? 16.338  -19.067 35.574  1.00 23.05  0  29  TRP   D CB  1 
ATOM   6046 C  CG  . TRP   D  1 14  ? 17.777  -18.809 35.321  1.00 22.43  0  29  TRP   D CG  1 
ATOM   6047 C  CD1 . TRP   D  1 14  ? 18.371  -18.502 34.133  1.00 23.39  0  29  TRP   D CD1 1 
ATOM   6048 C  CD2 . TRP   D  1 14  ? 18.808  -18.824 36.304  1.00 25.05  0  29  TRP   D CD2 1 
ATOM   6049 N  NE1 . TRP   D  1 14  ? 19.710  -18.313 34.317  1.00 25.16  0  29  TRP   D NE1 1 
ATOM   6050 C  CE2 . TRP   D  1 14  ? 20.016  -18.537 35.626  1.00 24.36  0  29  TRP   D CE2 1 
ATOM   6051 C  CE3 . TRP   D  1 14  ? 18.846  -19.098 37.674  1.00 24.54  0  29  TRP   D CE3 1 
ATOM   6052 C  CZ2 . TRP   D  1 14  ? 21.237  -18.481 36.280  1.00 27.28  0  29  TRP   D CZ2 1 
ATOM   6053 C  CZ3 . TRP   D  1 14  ? 20.063  -19.048 38.318  1.00 28.67  0  29  TRP   D CZ3 1 
ATOM   6054 C  CH2 . TRP   D  1 14  ? 21.233  -18.730 37.631  1.00 26.65  0  29  TRP   D CH2 1 
ATOM   6055 N  N   . GLN   D  1 15  ? 16.583  -21.032 32.701  1.00 27.05  0  30  GLN   D N   1 
ATOM   6056 C  CA  . GLN   D  1 15  ? 16.524  -20.970 31.222  1.00 26.93  0  30  GLN   D CA  1 
ATOM   6057 C  C   . GLN   D  1 15  ? 15.158  -21.498 30.777  1.00 26.74  0  30  GLN   D C   1 
ATOM   6058 O  O   . GLN   D  1 15  ? 14.722  -22.545 31.294  1.00 26.02  0  30  GLN   D O   1 
ATOM   6059 C  CB  . GLN   D  1 15  ? 17.652  -21.756 30.559  1.00 27.60  0  30  GLN   D CB  1 
ATOM   6060 C  CG  . GLN   D  1 15  ? 17.587  -21.709 29.028  1.00 26.86  0  30  GLN   D CG  1 
ATOM   6061 C  CD  . GLN   D  1 15  ? 18.101  -20.411 28.436  1.00 25.50  0  30  GLN   D CD  1 
ATOM   6062 O  OE1 . GLN   D  1 15  ? 19.181  -19.945 28.780  1.00 27.65  0  30  GLN   D OE1 1 
ATOM   6063 N  NE2 . GLN   D  1 15  ? 17.370  -19.849 27.481  1.00 27.34  0  30  GLN   D NE2 1 
ATOM   6064 N  N   . VAL   D  1 16  ? 14.514  -20.776 29.861  1.00 25.48  0  31  VAL   D N   1 
ATOM   6065 C  CA  . VAL   D  1 16  ? 13.195  -21.098 29.258  1.00 26.13  0  31  VAL   D CA  1 
ATOM   6066 C  C   . VAL   D  1 16  ? 13.345  -21.080 27.715  1.00 24.42  0  31  VAL   D C   1 
ATOM   6067 O  O   . VAL   D  1 16  ? 14.219  -20.347 27.178  1.00 22.06  0  31  VAL   D O   1 
ATOM   6068 C  CB  . VAL   D  1 16  ? 12.200  -20.050 29.804  1.00 30.43  0  31  VAL   D CB  1 
ATOM   6069 C  CG1 . VAL   D  1 16  ? 11.148  -19.640 28.819  1.00 32.14  0  31  VAL   D CG1 1 
ATOM   6070 C  CG2 . VAL   D  1 16  ? 11.595  -20.453 31.136  1.00 35.07  0  31  VAL   D CG2 1 
ATOM   6071 N  N   . SER   D  1 17  ? 12.512  -21.857 27.025  1.00 22.99  0  32  SER   D N   1 
ATOM   6072 C  CA  . SER   D  1 17  ? 12.389  -21.915 25.540  1.00 23.82  0  32  SER   D CA  1 
ATOM   6073 C  C   . SER   D  1 17  ? 11.000  -21.414 25.163  1.00 24.62  0  32  SER   D C   1 
ATOM   6074 O  O   . SER   D  1 17  ? 10.007  -21.920 25.746  1.00 25.93  0  32  SER   D O   1 
ATOM   6075 C  CB  . SER   D  1 17  ? 12.630  -23.335 25.012  1.00 22.30  0  32  SER   D CB  1 
ATOM   6076 O  OG  . SER   D  1 17  ? 12.347  -23.388 23.619  1.00 24.12  0  32  SER   D OG  1 
ATOM   6077 N  N   . LEU   D  1 18  ? 10.911  -20.482 24.215  1.00 21.79  0  33  LEU   D N   1 
ATOM   6078 C  CA  A LEU   D  1 18  ? 9.612   -20.000 23.692  0.50 21.70  0  33  LEU   D CA  1 
ATOM   6079 C  CA  B LEU   D  1 18  ? 9.625   -19.983 23.687  0.50 21.38  0  33  LEU   D CA  1 
ATOM   6080 C  C   . LEU   D  1 18  ? 9.303   -20.774 22.418  1.00 22.54  0  33  LEU   D C   1 
ATOM   6081 O  O   . LEU   D  1 18  ? 10.217  -20.903 21.580  1.00 23.27  0  33  LEU   D O   1 
ATOM   6082 C  CB  A LEU   D  1 18  ? 9.667   -18.500 23.409  0.50 22.63  0  33  LEU   D CB  1 
ATOM   6083 C  CB  B LEU   D  1 18  ? 9.761   -18.482 23.413  0.50 21.77  0  33  LEU   D CB  1 
ATOM   6084 C  CG  A LEU   D  1 18  ? 9.484   -17.595 24.620  0.50 23.11  0  33  LEU   D CG  1 
ATOM   6085 C  CG  B LEU   D  1 18  ? 10.080  -17.625 24.637  0.50 21.94  0  33  LEU   D CG  1 
ATOM   6086 C  CD1 A LEU   D  1 18  ? 10.601  -17.804 25.629  0.50 23.36  0  33  LEU   D CD1 1 
ATOM   6087 C  CD1 B LEU   D  1 18  ? 10.096  -16.138 24.279  0.50 21.96  0  33  LEU   D CD1 1 
ATOM   6088 C  CD2 A LEU   D  1 18  ? 9.434   -16.137 24.179  0.50 23.12  0  33  LEU   D CD2 1 
ATOM   6089 C  CD2 B LEU   D  1 18  ? 9.079   -17.912 25.753  0.50 21.02  0  33  LEU   D CD2 1 
ATOM   6090 N  N   . ARG   D  1 19  ? 8.060   -21.232 22.296  1.00 21.94  0  34  ARG   D N   1 
ATOM   6091 C  CA  . ARG   D  1 19  ? 7.623   -22.114 21.204  1.00 22.68  0  34  ARG   D CA  1 
ATOM   6092 C  C   . ARG   D  1 19  ? 6.470   -21.477 20.438  1.00 25.12  0  34  ARG   D C   1 
ATOM   6093 O  O   . ARG   D  1 19  ? 5.544   -20.939 21.075  1.00 24.92  0  34  ARG   D O   1 
ATOM   6094 C  CB  . ARG   D  1 19  ? 7.208   -23.469 21.762  1.00 22.36  0  34  ARG   D CB  1 
ATOM   6095 C  CG  . ARG   D  1 19  ? 8.294   -24.185 22.555  1.00 22.74  0  34  ARG   D CG  1 
ATOM   6096 C  CD  . ARG   D  1 19  ? 9.574   -24.442 21.808  1.00 24.19  0  34  ARG   D CD  1 
ATOM   6097 N  NE  . ARG   D  1 19  ? 10.440  -25.316 22.599  1.00 25.77  0  34  ARG   D NE  1 
ATOM   6098 C  CZ  . ARG   D  1 19  ? 10.229  -26.634 22.755  1.00 24.90  0  34  ARG   D CZ  1 
ATOM   6099 N  NH1 . ARG   D  1 19  ? 9.250   -27.245 22.133  1.00 23.18  1  34  ARG   D NH1 1 
ATOM   6100 N  NH2 . ARG   D  1 19  ? 11.018  -27.350 23.509  1.00 25.49  0  34  ARG   D NH2 1 
ATOM   6101 N  N   . VAL   D  1 20  ? 6.520   -21.604 19.108  1.00 27.46  0  35  VAL   D N   1 
ATOM   6102 C  CA  . VAL   D  1 20  ? 5.483   -21.106 18.168  1.00 28.22  0  35  VAL   D CA  1 
ATOM   6103 C  C   . VAL   D  1 20  ? 4.793   -22.321 17.545  1.00 28.68  0  35  VAL   D C   1 
ATOM   6104 O  O   . VAL   D  1 20  ? 5.498   -23.272 17.149  1.00 25.91  0  35  VAL   D O   1 
ATOM   6105 C  CB  . VAL   D  1 20  ? 6.081   -20.175 17.088  1.00 28.95  0  35  VAL   D CB  1 
ATOM   6106 C  CG1 . VAL   D  1 20  ? 7.158   -20.804 16.228  1.00 27.10  0  35  VAL   D CG1 1 
ATOM   6107 C  CG2 . VAL   D  1 20  ? 4.995   -19.624 16.210  1.00 31.71  0  35  VAL   D CG2 1 
ATOM   6108 N  N   . HIS   D  1 21  ? 3.475   -22.255 17.398  1.00 31.55  0  36  HIS   D N   1 
ATOM   6109 C  CA  . HIS   D  1 21  ? 2.651   -23.342 16.808  1.00 35.45  0  36  HIS   D CA  1 
ATOM   6110 C  C   . HIS   D  1 21  ? 2.985   -23.455 15.315  1.00 37.08  0  36  HIS   D C   1 
ATOM   6111 O  O   . HIS   D  1 21  ? 3.083   -22.453 14.660  1.00 35.27  0  36  HIS   D O   1 
ATOM   6112 C  CB  . HIS   D  1 21  ? 1.167   -23.083 17.034  1.00 42.70  0  36  HIS   D CB  1 
ATOM   6113 C  CG  . HIS   D  1 21  ? 0.336   -24.231 16.586  1.00 56.71  0  36  HIS   D CG  1 
ATOM   6114 N  ND1 . HIS   D  1 21  ? 0.161   -25.371 17.363  1.00 61.41  0  36  HIS   D ND1 1 
ATOM   6115 C  CD2 . HIS   D  1 21  ? -0.354  -24.438 15.444  1.00 66.01  0  36  HIS   D CD2 1 
ATOM   6116 C  CE1 . HIS   D  1 21  ? -0.613  -26.225 16.730  1.00 62.85  0  36  HIS   D CE1 1 
ATOM   6117 N  NE2 . HIS   D  1 21  ? -0.936  -25.680 15.544  1.00 68.36  0  36  HIS   D NE2 1 
ATOM   6118 N  N   . GLY   D  1 22  ? 3.225   -24.657 14.818  1.00 36.14  0  37  GLY   D N   1 
ATOM   6119 C  CA  . GLY   D  1 22  ? 3.432   -24.938 13.384  1.00 37.31  0  37  GLY   D CA  1 
ATOM   6120 C  C   . GLY   D  1 22  ? 3.300   -26.433 13.177  1.00 35.34  0  37  GLY   D C   1 
ATOM   6121 O  O   . GLY   D  1 22  ? 2.556   -27.070 13.920  1.00 34.10  0  37  GLY   D O   1 
ATOM   6122 N  N   . PRO   D  1 23  ? 4.032   -27.048 12.223  1.00 40.43  0  38  PRO   D N   1 
ATOM   6123 C  CA  . PRO   D  1 23  ? 4.079   -28.510 12.124  1.00 37.19  0  38  PRO   D CA  1 
ATOM   6124 C  C   . PRO   D  1 23  ? 4.484   -29.141 13.465  1.00 36.78  0  38  PRO   D C   1 
ATOM   6125 O  O   . PRO   D  1 23  ? 4.043   -30.242 13.784  1.00 38.25  0  38  PRO   D O   1 
ATOM   6126 C  CB  . PRO   D  1 23  ? 5.164   -28.809 11.073  1.00 44.83  0  38  PRO   D CB  1 
ATOM   6127 C  CG  . PRO   D  1 23  ? 5.376   -27.490 10.324  1.00 44.61  0  38  PRO   D CG  1 
ATOM   6128 C  CD  . PRO   D  1 23  ? 4.872   -26.376 11.222  1.00 42.92  0  38  PRO   D CD  1 
ATOM   6129 N  N   . TYR   D  1 24  ? 5.304   -28.417 14.241  1.00 32.14  0  39  TYR   D N   1 
ATOM   6130 C  CA  . TYR   D  1 24  ? 5.606   -28.749 15.655  1.00 29.53  0  39  TYR   D CA  1 
ATOM   6131 C  C   . TYR   D  1 24  ? 5.790   -27.443 16.428  1.00 31.26  0  39  TYR   D C   1 
ATOM   6132 O  O   . TYR   D  1 24  ? 5.832   -26.337 15.790  1.00 27.77  0  39  TYR   D O   1 
ATOM   6133 C  CB  . TYR   D  1 24  ? 6.846   -29.648 15.749  1.00 27.04  0  39  TYR   D CB  1 
ATOM   6134 C  CG  . TYR   D  1 24  ? 8.123   -29.027 15.253  1.00 28.28  0  39  TYR   D CG  1 
ATOM   6135 C  CD1 . TYR   D  1 24  ? 8.370   -28.811 13.895  1.00 29.04  0  39  TYR   D CD1 1 
ATOM   6136 C  CD2 . TYR   D  1 24  ? 9.122   -28.689 16.152  1.00 27.91  0  39  TYR   D CD2 1 
ATOM   6137 C  CE1 . TYR   D  1 24  ? 9.590   -28.301 13.459  1.00 29.89  0  39  TYR   D CE1 1 
ATOM   6138 C  CE2 . TYR   D  1 24  ? 10.305  -28.101 15.738  1.00 28.44  0  39  TYR   D CE2 1 
ATOM   6139 C  CZ  . TYR   D  1 24  ? 10.556  -27.930 14.387  1.00 30.71  0  39  TYR   D CZ  1 
ATOM   6140 O  OH  . TYR   D  1 24  ? 11.760  -27.391 14.022  1.00 30.96  0  39  TYR   D OH  1 
ATOM   6141 N  N   . TRP   D  1 25  ? 5.915   -27.578 17.747  1.00 27.78  0  40  TRP   D N   1 
ATOM   6142 C  CA  . TRP   D  1 25  ? 6.102   -26.441 18.667  1.00 26.36  0  40  TRP   D CA  1 
ATOM   6143 C  C   . TRP   D  1 25  ? 7.569   -26.042 18.608  1.00 25.57  0  40  TRP   D C   1 
ATOM   6144 O  O   . TRP   D  1 25  ? 8.377   -26.580 19.362  1.00 23.74  0  40  TRP   D O   1 
ATOM   6145 C  CB  . TRP   D  1 25  ? 5.615   -26.843 20.057  1.00 27.43  0  40  TRP   D CB  1 
ATOM   6146 C  CG  . TRP   D  1 25  ? 4.127   -26.812 20.126  1.00 26.70  0  40  TRP   D CG  1 
ATOM   6147 C  CD1 . TRP   D  1 25  ? 3.284   -27.875 19.985  1.00 29.27  0  40  TRP   D CD1 1 
ATOM   6148 C  CD2 . TRP   D  1 25  ? 3.288   -25.653 20.274  1.00 29.87  0  40  TRP   D CD2 1 
ATOM   6149 N  NE1 . TRP   D  1 25  ? 1.988   -27.455 20.088  1.00 29.86  0  40  TRP   D NE1 1 
ATOM   6150 C  CE2 . TRP   D  1 25  ? 1.950   -26.105 20.260  1.00 31.15  0  40  TRP   D CE2 1 
ATOM   6151 C  CE3 . TRP   D  1 25  ? 3.528   -24.287 20.480  1.00 30.11  0  40  TRP   D CE3 1 
ATOM   6152 C  CZ2 . TRP   D  1 25  ? 0.867   -25.247 20.454  1.00 32.86  0  40  TRP   D CZ2 1 
ATOM   6153 C  CZ3 . TRP   D  1 25  ? 2.459   -23.429 20.628  1.00 31.24  0  40  TRP   D CZ3 1 
ATOM   6154 C  CH2 . TRP   D  1 25  ? 1.147   -23.909 20.644  1.00 33.04  0  40  TRP   D CH2 1 
ATOM   6155 N  N   A MET   D  1 26  ? 7.898   -25.139 17.696  0.50 26.46  0  41  MET   D N   1 
ATOM   6156 N  N   B MET   D  1 26  ? 7.902   -25.173 17.654  0.50 26.68  0  41  MET   D N   1 
ATOM   6157 C  CA  A MET   D  1 26  ? 9.294   -24.815 17.322  0.50 28.37  0  41  MET   D CA  1 
ATOM   6158 C  CA  B MET   D  1 26  ? 9.309   -24.830 17.308  0.50 28.83  0  41  MET   D CA  1 
ATOM   6159 C  C   A MET   D  1 26  ? 9.854   -23.718 18.248  0.50 27.72  0  41  MET   D C   1 
ATOM   6160 C  C   B MET   D  1 26  ? 9.847   -23.729 18.248  0.50 28.02  0  41  MET   D C   1 
ATOM   6161 O  O   A MET   D  1 26  ? 9.184   -22.716 18.486  0.50 26.88  0  41  MET   D O   1 
ATOM   6162 O  O   B MET   D  1 26  ? 9.147   -22.739 18.485  0.50 27.24  0  41  MET   D O   1 
ATOM   6163 C  CB  A MET   D  1 26  ? 9.329   -24.360 15.864  0.50 30.12  0  41  MET   D CB  1 
ATOM   6164 C  CB  B MET   D  1 26  ? 9.417   -24.373 15.848  0.50 31.00  0  41  MET   D CB  1 
ATOM   6165 C  CG  A MET   D  1 26  ? 10.711  -24.320 15.270  0.50 32.54  0  41  MET   D CG  1 
ATOM   6166 C  CG  B MET   D  1 26  ? 10.854  -24.194 15.373  0.50 33.83  0  41  MET   D CG  1 
ATOM   6167 S  SD  A MET   D  1 26  ? 10.641  -24.212 13.451  0.50 33.94  0  41  MET   D SD  1 
ATOM   6168 S  SD  B MET   D  1 26  ? 11.005  -23.476 13.699  0.50 36.73  0  41  MET   D SD  1 
ATOM   6169 C  CE  A MET   D  1 26  ? 9.422   -22.911 13.258  0.50 28.83  0  41  MET   D CE  1 
ATOM   6170 C  CE  B MET   D  1 26  ? 12.766  -23.637 13.442  0.50 29.16  0  41  MET   D CE  1 
ATOM   6171 N  N   . HIS   D  1 27  ? 11.066  -23.917 18.759  1.00 27.01  0  42  HIS   D N   1 
ATOM   6172 C  CA  . HIS   D  1 27  ? 11.861  -22.897 19.488  1.00 26.27  0  42  HIS   D CA  1 
ATOM   6173 C  C   . HIS   D  1 27  ? 12.161  -21.708 18.558  1.00 26.67  0  42  HIS   D C   1 
ATOM   6174 O  O   . HIS   D  1 27  ? 12.625  -21.934 17.434  1.00 24.01  0  42  HIS   D O   1 
ATOM   6175 C  CB  . HIS   D  1 27  ? 13.140  -23.540 20.014  1.00 25.53  0  42  HIS   D CB  1 
ATOM   6176 C  CG  . HIS   D  1 27  ? 14.078  -22.555 20.574  1.00 25.03  0  42  HIS   D CG  1 
ATOM   6177 N  ND1 . HIS   D  1 27  ? 14.070  -22.233 21.908  1.00 25.62  0  42  HIS   D ND1 1 
ATOM   6178 C  CD2 . HIS   D  1 27  ? 14.981  -21.748 19.982  1.00 26.00  0  42  HIS   D CD2 1 
ATOM   6179 C  CE1 . HIS   D  1 27  ? 14.949  -21.279 22.116  1.00 24.97  0  42  HIS   D CE1 1 
ATOM   6180 N  NE2 . HIS   D  1 27  ? 15.507  -20.952 20.954  1.00 23.83  0  42  HIS   D NE2 1 
ATOM   6181 N  N   . PHE   D  1 28  ? 11.855  -20.487 18.985  1.00 27.04  0  43  PHE   D N   1 
ATOM   6182 C  CA  . PHE   D  1 28  ? 12.210  -19.246 18.244  1.00 26.91  0  43  PHE   D CA  1 
ATOM   6183 C  C   . PHE   D  1 28  ? 13.003  -18.280 19.139  1.00 26.80  0  43  PHE   D C   1 
ATOM   6184 O  O   . PHE   D  1 28  ? 13.759  -17.512 18.629  1.00 28.80  0  43  PHE   D O   1 
ATOM   6185 C  CB  . PHE   D  1 28  ? 10.960  -18.604 17.643  1.00 25.75  0  43  PHE   D CB  1 
ATOM   6186 C  CG  . PHE   D  1 28  ? 9.976   -18.072 18.654  1.00 25.68  0  43  PHE   D CG  1 
ATOM   6187 C  CD1 . PHE   D  1 28  ? 8.980   -18.884 19.181  1.00 24.54  0  43  PHE   D CD1 1 
ATOM   6188 C  CD2 . PHE   D  1 28  ? 10.021  -16.745 19.043  1.00 23.99  0  43  PHE   D CD2 1 
ATOM   6189 C  CE1 . PHE   D  1 28  ? 8.066   -18.385 20.083  1.00 25.80  0  43  PHE   D CE1 1 
ATOM   6190 C  CE2 . PHE   D  1 28  ? 9.138   -16.257 19.982  1.00 28.27  0  43  PHE   D CE2 1 
ATOM   6191 C  CZ  . PHE   D  1 28  ? 8.142   -17.064 20.485  1.00 28.78  0  43  PHE   D CZ  1 
ATOM   6192 N  N   . CYS   D  1 29  ? 12.889  -18.353 20.457  1.00 28.15  0  44  CYS   D N   1 
ATOM   6193 C  CA  . CYS   D  1 29  ? 13.606  -17.448 21.380  1.00 26.07  0  44  CYS   D CA  1 
ATOM   6194 C  C   . CYS   D  1 29  ? 13.774  -18.113 22.745  1.00 27.01  0  44  CYS   D C   1 
ATOM   6195 O  O   . CYS   D  1 29  ? 13.001  -19.061 23.060  1.00 24.38  0  44  CYS   D O   1 
ATOM   6196 C  CB  . CYS   D  1 29  ? 12.833  -16.147 21.557  1.00 26.02  0  44  CYS   D CB  1 
ATOM   6197 S  SG  . CYS   D  1 29  ? 13.158  -14.894 20.287  1.00 28.08  0  44  CYS   D SG  1 
ATOM   6198 N  N   . GLY   D  1 30  ? 14.727  -17.592 23.500  1.00 21.71  0  45  GLY   D N   1 
ATOM   6199 C  CA  . GLY   D  1 30  ? 14.890  -17.869 24.932  1.00 26.39  0  45  GLY   D CA  1 
ATOM   6200 C  C   . GLY   D  1 30  ? 14.128  -16.885 25.811  1.00 23.38  0  45  GLY   D C   1 
ATOM   6201 O  O   . GLY   D  1 30  ? 13.401  -15.966 25.291  1.00 21.50  0  45  GLY   D O   1 
ATOM   6202 N  N   . GLY   D  1 31  ? 14.234  -17.158 27.093  1.00 22.36  0  46  GLY   D N   1 
ATOM   6203 C  CA  . GLY   D  1 31  ? 13.622  -16.417 28.198  1.00 22.81  0  46  GLY   D CA  1 
ATOM   6204 C  C   . GLY   D  1 31  ? 14.242  -16.859 29.512  1.00 23.17  0  46  GLY   D C   1 
ATOM   6205 O  O   . GLY   D  1 31  ? 15.074  -17.791 29.508  1.00 25.25  0  46  GLY   D O   1 
ATOM   6206 N  N   . SER   D  1 32  ? 13.818  -16.248 30.614  1.00 22.94  0  47  SER   D N   1 
ATOM   6207 C  CA  . SER   D  1 32  ? 14.243  -16.606 31.975  1.00 23.93  0  47  SER   D CA  1 
ATOM   6208 C  C   . SER   D  1 32  ? 13.020  -16.560 32.904  1.00 24.13  0  47  SER   D C   1 
ATOM   6209 O  O   . SER   D  1 32  ? 12.114  -15.716 32.727  1.00 22.58  0  47  SER   D O   1 
ATOM   6210 C  CB  . SER   D  1 32  ? 15.393  -15.754 32.446  1.00 25.75  0  47  SER   D CB  1 
ATOM   6211 O  OG  . SER   D  1 32  ? 15.033  -14.382 32.453  1.00 23.70  0  47  SER   D OG  1 
ATOM   6212 N  N   . LEU   D  1 33  ? 12.946  -17.517 33.810  1.00 23.34  0  48  LEU   D N   1 
ATOM   6213 C  CA  . LEU   D  1 33  ? 11.916  -17.530 34.869  1.00 24.98  0  48  LEU   D CA  1 
ATOM   6214 C  C   . LEU   D  1 33  ? 12.357  -16.576 35.982  1.00 21.46  0  48  LEU   D C   1 
ATOM   6215 O  O   . LEU   D  1 33  ? 13.424  -16.779 36.562  1.00 20.79  0  48  LEU   D O   1 
ATOM   6216 C  CB  . LEU   D  1 33  ? 11.747  -18.970 35.360  1.00 23.98  0  48  LEU   D CB  1 
ATOM   6217 C  CG  . LEU   D  1 33  ? 10.521  -19.182 36.251  1.00 25.79  0  48  LEU   D CG  1 
ATOM   6218 C  CD1 . LEU   D  1 33  ? 9.225   -19.121 35.465  1.00 24.28  0  48  LEU   D CD1 1 
ATOM   6219 C  CD2 . LEU   D  1 33  ? 10.650  -20.521 36.975  1.00 28.15  0  48  LEU   D CD2 1 
ATOM   6220 N  N   . ILE   D  1 34  ? 11.639  -15.473 36.150  1.00 24.30  0  49  ILE   D N   1 
ATOM   6221 C  CA  . ILE   D  1 34  ? 12.000  -14.457 37.191  1.00 25.63  0  49  ILE   D CA  1 
ATOM   6222 C  C   . ILE   D  1 34  ? 11.023  -14.534 38.373  1.00 25.27  0  49  ILE   D C   1 
ATOM   6223 O  O   . ILE   D  1 34  ? 11.211  -13.823 39.336  1.00 25.64  0  49  ILE   D O   1 
ATOM   6224 C  CB  . ILE   D  1 34  ? 12.093  -13.054 36.571  1.00 26.27  0  49  ILE   D CB  1 
ATOM   6225 C  CG1 . ILE   D  1 34  ? 10.787  -12.633 35.913  1.00 25.39  0  49  ILE   D CG1 1 
ATOM   6226 C  CG2 . ILE   D  1 34  ? 13.267  -12.992 35.604  1.00 26.73  0  49  ILE   D CG2 1 
ATOM   6227 C  CD1 . ILE   D  1 34  ? 10.676  -11.097 35.742  1.00 26.92  0  49  ILE   D CD1 1 
ATOM   6228 N  N   . HIS   D  1 35  ? 9.957   -15.310 38.236  1.00 26.85  0  50  HIS   D N   1 
ATOM   6229 C  CA  . HIS   D  1 35  ? 8.876   -15.478 39.233  1.00 28.04  0  50  HIS   D CA  1 
ATOM   6230 C  C   . HIS   D  1 35  ? 8.144   -16.746 38.819  1.00 26.05  0  50  HIS   D C   1 
ATOM   6231 O  O   . HIS   D  1 35  ? 8.120   -17.052 37.633  1.00 25.23  0  50  HIS   D O   1 
ATOM   6232 C  CB  . HIS   D  1 35  ? 7.973   -14.245 39.269  1.00 29.67  0  50  HIS   D CB  1 
ATOM   6233 C  CG  . HIS   D  1 35  ? 6.891   -14.308 40.286  1.00 32.35  0  50  HIS   D CG  1 
ATOM   6234 N  ND1 . HIS   D  1 35  ? 5.693   -15.002 40.057  1.00 27.24  0  50  HIS   D ND1 1 
ATOM   6235 C  CD2 . HIS   D  1 35  ? 6.807   -13.757 41.523  1.00 30.71  0  50  HIS   D CD2 1 
ATOM   6236 C  CE1 . HIS   D  1 35  ? 4.912   -14.865 41.118  1.00 33.68  0  50  HIS   D CE1 1 
ATOM   6237 N  NE2 . HIS   D  1 35  ? 5.580   -14.085 42.035  1.00 29.26  0  50  HIS   D NE2 1 
ATOM   6238 N  N   . PRO   D  1 36  ? 7.569   -17.539 39.741  1.00 25.58  0  51  PRO   D N   1 
ATOM   6239 C  CA  . PRO   D  1 36  ? 6.825   -18.740 39.347  1.00 25.28  0  51  PRO   D CA  1 
ATOM   6240 C  C   . PRO   D  1 36  ? 5.750   -18.560 38.266  1.00 27.78  0  51  PRO   D C   1 
ATOM   6241 O  O   . PRO   D  1 36  ? 5.402   -19.555 37.634  1.00 30.94  0  51  PRO   D O   1 
ATOM   6242 C  CB  . PRO   D  1 36  ? 6.193   -19.164 40.686  1.00 27.97  0  51  PRO   D CB  1 
ATOM   6243 C  CG  . PRO   D  1 36  ? 7.225   -18.751 41.707  1.00 26.58  0  51  PRO   D CG  1 
ATOM   6244 C  CD  . PRO   D  1 36  ? 7.669   -17.394 41.205  1.00 28.59  0  51  PRO   D CD  1 
ATOM   6245 N  N   A GLN   D  1 37  ? 5.224   -17.338 38.091  0.50 27.32  0  52  GLN   D N   1 
ATOM   6246 N  N   B GLN   D  1 37  ? 5.207   -17.353 38.069  0.50 26.16  0  52  GLN   D N   1 
ATOM   6247 C  CA  A GLN   D  1 37  ? 4.152   -17.009 37.122  0.50 28.06  0  52  GLN   D CA  1 
ATOM   6248 C  CA  B GLN   D  1 37  ? 4.190   -17.119 37.016  0.50 26.32  0  52  GLN   D CA  1 
ATOM   6249 C  C   A GLN   D  1 37  ? 4.688   -16.164 35.943  0.50 27.30  0  52  GLN   D C   1 
ATOM   6250 C  C   B GLN   D  1 37  ? 4.671   -16.109 35.960  0.50 26.17  0  52  GLN   D C   1 
ATOM   6251 O  O   A GLN   D  1 37  ? 3.883   -15.847 35.043  0.50 28.86  0  52  GLN   D O   1 
ATOM   6252 O  O   B GLN   D  1 37  ? 3.796   -15.632 35.165  0.50 27.08  0  52  GLN   D O   1 
ATOM   6253 C  CB  A GLN   D  1 37  ? 3.027   -16.233 37.812  0.50 29.80  0  52  GLN   D CB  1 
ATOM   6254 C  CB  B GLN   D  1 37  ? 2.874   -16.650 37.618  0.50 26.03  0  52  GLN   D CB  1 
ATOM   6255 C  CG  A GLN   D  1 37  ? 2.274   -17.032 38.867  0.50 31.28  0  52  GLN   D CG  1 
ATOM   6256 C  CG  B GLN   D  1 37  ? 1.686   -17.022 36.752  0.50 25.04  0  52  GLN   D CG  1 
ATOM   6257 C  CD  A GLN   D  1 37  ? 1.247   -16.202 39.589  0.50 30.67  0  52  GLN   D CD  1 
ATOM   6258 C  CD  B GLN   D  1 37  ? 0.422   -17.044 37.565  0.50 24.80  0  52  GLN   D CD  1 
ATOM   6259 O  OE1 A GLN   D  1 37  ? 0.216   -15.841 39.041  0.50 35.80  0  52  GLN   D OE1 1 
ATOM   6260 O  OE1 B GLN   D  1 37  ? 0.463   -16.813 38.775  0.50 29.16  0  52  GLN   D OE1 1 
ATOM   6261 N  NE2 A GLN   D  1 37  ? 1.506   -15.917 40.847  0.50 31.99  0  52  GLN   D NE2 1 
ATOM   6262 N  NE2 B GLN   D  1 37  ? -0.697  -17.342 36.914  0.50 19.94  0  52  GLN   D NE2 1 
ATOM   6263 N  N   . TRP   D  1 38  ? 5.966   -15.790 35.921  1.00 24.83  0  53  TRP   D N   1 
ATOM   6264 C  CA  . TRP   D  1 38  ? 6.489   -14.770 34.960  1.00 23.07  0  53  TRP   D CA  1 
ATOM   6265 C  C   . TRP   D  1 38  ? 7.804   -15.153 34.300  1.00 23.82  0  53  TRP   D C   1 
ATOM   6266 O  O   . TRP   D  1 38  ? 8.760   -15.571 35.007  1.00 24.00  0  53  TRP   D O   1 
ATOM   6267 C  CB  . TRP   D  1 38  ? 6.613   -13.396 35.610  1.00 24.41  0  53  TRP   D CB  1 
ATOM   6268 C  CG  . TRP   D  1 38  ? 5.310   -12.795 36.028  1.00 23.96  0  53  TRP   D CG  1 
ATOM   6269 C  CD1 . TRP   D  1 38  ? 4.705   -12.961 37.243  1.00 25.52  0  53  TRP   D CD1 1 
ATOM   6270 C  CD2 . TRP   D  1 38  ? 4.450   -11.913 35.269  1.00 24.99  0  53  TRP   D CD2 1 
ATOM   6271 N  NE1 . TRP   D  1 38  ? 3.553   -12.218 37.292  1.00 24.94  0  53  TRP   D NE1 1 
ATOM   6272 C  CE2 . TRP   D  1 38  ? 3.362   -11.576 36.105  1.00 24.74  0  53  TRP   D CE2 1 
ATOM   6273 C  CE3 . TRP   D  1 38  ? 4.498   -11.353 33.985  1.00 24.85  0  53  TRP   D CE3 1 
ATOM   6274 C  CZ2 . TRP   D  1 38  ? 2.334   -10.720 35.706  1.00 24.65  0  53  TRP   D CZ2 1 
ATOM   6275 C  CZ3 . TRP   D  1 38  ? 3.470   -10.534 33.574  1.00 26.67  0  53  TRP   D CZ3 1 
ATOM   6276 C  CH2 . TRP   D  1 38  ? 2.412   -10.213 34.433  1.00 25.17  0  53  TRP   D CH2 1 
ATOM   6277 N  N   . VAL   D  1 39  ? 7.844   -14.927 32.987  1.00 22.72  0  54  VAL   D N   1 
ATOM   6278 C  CA  . VAL   D  1 39  ? 9.043   -15.142 32.145  1.00 22.84  0  54  VAL   D CA  1 
ATOM   6279 C  C   . VAL   D  1 39  ? 9.477   -13.782 31.575  1.00 22.18  0  54  VAL   D C   1 
ATOM   6280 O  O   . VAL   D  1 39  ? 8.638   -13.020 31.034  1.00 20.50  0  54  VAL   D O   1 
ATOM   6281 C  CB  . VAL   D  1 39  ? 8.745   -16.147 31.031  1.00 24.23  0  54  VAL   D CB  1 
ATOM   6282 C  CG1 . VAL   D  1 39  ? 9.850   -16.230 29.990  1.00 23.96  0  54  VAL   D CG1 1 
ATOM   6283 C  CG2 . VAL   D  1 39  ? 8.422   -17.520 31.575  1.00 25.07  0  54  VAL   D CG2 1 
ATOM   6284 N  N   . LEU   D  1 40  ? 10.765  -13.508 31.669  1.00 21.75  0  55  LEU   D N   1 
ATOM   6285 C  CA  . LEU   D  1 40  ? 11.436  -12.313 31.077  1.00 22.06  0  55  LEU   D CA  1 
ATOM   6286 C  C   . LEU   D  1 40  ? 12.033  -12.726 29.725  1.00 21.69  0  55  LEU   D C   1 
ATOM   6287 O  O   . LEU   D  1 40  ? 12.705  -13.795 29.655  1.00 22.98  0  55  LEU   D O   1 
ATOM   6288 C  CB  . LEU   D  1 40  ? 12.513  -11.817 32.051  1.00 21.44  0  55  LEU   D CB  1 
ATOM   6289 C  CG  . LEU   D  1 40  ? 13.298  -10.579 31.616  1.00 23.58  0  55  LEU   D CG  1 
ATOM   6290 C  CD1 . LEU   D  1 40  ? 12.422  -9.344  31.473  1.00 23.89  0  55  LEU   D CD1 1 
ATOM   6291 C  CD2 . LEU   D  1 40  ? 14.422  -10.297 32.600  1.00 24.29  0  55  LEU   D CD2 1 
ATOM   6292 N  N   . THR   D  1 41  ? 11.784  -11.919 28.687  1.00 21.54  0  56  THR   D N   1 
ATOM   6293 C  CA  . THR   D  1 41  ? 12.290  -12.134 27.318  1.00 21.10  0  56  THR   D CA  1 
ATOM   6294 C  C   . THR   D  1 41  ? 12.574  -10.788 26.630  1.00 23.45  0  56  THR   D C   1 
ATOM   6295 O  O   . THR   D  1 41  ? 12.437  -9.711  27.258  1.00 22.40  0  56  THR   D O   1 
ATOM   6296 C  CB  . THR   D  1 41  ? 11.309  -13.065 26.578  1.00 21.63  0  56  THR   D CB  1 
ATOM   6297 O  OG1 . THR   D  1 41  ? 11.989  -13.605 25.435  1.00 21.40  0  56  THR   D OG1 1 
ATOM   6298 C  CG2 . THR   D  1 41  ? 9.983   -12.409 26.230  1.00 22.40  0  56  THR   D CG2 1 
ATOM   6299 N  N   . ALA   D  1 42  ? 12.951  -10.843 25.347  1.00 25.60  0  57  ALA   D N   1 
ATOM   6300 C  CA  . ALA   D  1 42  ? 13.130  -9.669  24.467  1.00 21.50  0  57  ALA   D CA  1 
ATOM   6301 C  C   . ALA   D  1 42  ? 11.774  -9.348  23.845  1.00 20.51  0  57  ALA   D C   1 
ATOM   6302 O  O   . ALA   D  1 42  ? 11.041  -10.268 23.449  1.00 21.00  0  57  ALA   D O   1 
ATOM   6303 C  CB  . ALA   D  1 42  ? 14.175  -9.966  23.403  1.00 24.09  0  57  ALA   D CB  1 
ATOM   6304 N  N   . ALA   D  1 43  ? 11.422  -8.081  23.773  1.00 19.62  0  58  ALA   D N   1 
ATOM   6305 C  CA  . ALA   D  1 43  ? 10.232  -7.585  23.048  1.00 21.33  0  58  ALA   D CA  1 
ATOM   6306 C  C   . ALA   D  1 43  ? 10.263  -8.014  21.571  1.00 21.12  0  58  ALA   D C   1 
ATOM   6307 O  O   . ALA   D  1 43  ? 9.197   -8.258  21.024  1.00 22.98  0  58  ALA   D O   1 
ATOM   6308 C  CB  . ALA   D  1 43  ? 10.186  -6.090  23.152  1.00 20.49  0  58  ALA   D CB  1 
ATOM   6309 N  N   . HIS   D  1 44  ? 11.426  -8.058  20.917  1.00 21.91  0  59  HIS   D N   1 
ATOM   6310 C  CA  . HIS   D  1 44  ? 11.504  -8.347  19.457  1.00 24.68  0  59  HIS   D CA  1 
ATOM   6311 C  C   . HIS   D  1 44  ? 11.120  -9.828  19.226  1.00 23.46  0  59  HIS   D C   1 
ATOM   6312 O  O   . HIS   D  1 44  ? 10.737  -10.155 18.103  1.00 23.70  0  59  HIS   D O   1 
ATOM   6313 C  CB  . HIS   D  1 44  ? 12.862  -7.940  18.860  1.00 21.52  0  59  HIS   D CB  1 
ATOM   6314 C  CG  . HIS   D  1 44  ? 13.929  -8.961  18.977  1.00 21.60  0  59  HIS   D CG  1 
ATOM   6315 N  ND1 . HIS   D  1 44  ? 14.918  -8.903  19.958  1.00 22.50  0  59  HIS   D ND1 1 
ATOM   6316 C  CD2 . HIS   D  1 44  ? 14.127  -10.106 18.293  1.00 23.92  0  59  HIS   D CD2 1 
ATOM   6317 C  CE1 . HIS   D  1 44  ? 15.688  -9.950  19.850  1.00 25.54  0  59  HIS   D CE1 1 
ATOM   6318 N  NE2 . HIS   D  1 44  ? 15.245  -10.703 18.819  1.00 23.77  0  59  HIS   D NE2 1 
ATOM   6319 N  N   . CYS   D  1 45  ? 11.147  -10.670 20.255  1.00 21.70  0  60  CYS   D N   1 
ATOM   6320 C  CA  . CYS   D  1 45  ? 10.687  -12.078 20.145  1.00 23.84  0  60  CYS   D CA  1 
ATOM   6321 C  C   . CYS   D  1 45  ? 9.163   -12.131 20.008  1.00 23.71  0  60  CYS   D C   1 
ATOM   6322 O  O   . CYS   D  1 45  ? 8.698   -13.058 19.356  1.00 25.54  0  60  CYS   D O   1 
ATOM   6323 C  CB  . CYS   D  1 45  ? 11.100  -12.903 21.333  1.00 23.68  0  60  CYS   D CB  1 
ATOM   6324 S  SG  . CYS   D  1 45  ? 12.880  -13.111 21.416  1.00 26.51  0  60  CYS   D SG  1 
ATOM   6325 N  N   . VAL   D  1 46  ? 8.436   -11.171 20.577  1.00 24.33  0  61  VAL   D N   1 
ATOM   6326 C  CA  . VAL   D  1 46  ? 6.946   -11.252 20.697  1.00 29.43  0  61  VAL   D CA  1 
ATOM   6327 C  C   . VAL   D  1 46  ? 6.254   -9.997  20.165  1.00 29.41  0  61  VAL   D C   1 
ATOM   6328 O  O   . VAL   D  1 46  ? 5.037   -9.955  20.229  1.00 34.77  0  61  VAL   D O   1 
ATOM   6329 C  CB  . VAL   D  1 46  ? 6.532   -11.564 22.147  1.00 29.33  0  61  VAL   D CB  1 
ATOM   6330 C  CG1 . VAL   D  1 46  ? 6.977   -12.964 22.533  1.00 30.56  0  61  VAL   D CG1 1 
ATOM   6331 C  CG2 . VAL   D  1 46  ? 7.100   -10.557 23.143  1.00 31.05  0  61  VAL   D CG2 1 
ATOM   6332 N  N   . GLY   D  1 47  ? 6.980   -9.043  19.589  1.00 28.45  0  62  GLY   D N   1 
ATOM   6333 C  CA  . GLY   D  1 47  ? 6.402   -7.769  19.121  1.00 29.39  0  62  GLY   D CA  1 
ATOM   6334 C  C   . GLY   D  1 47  ? 7.282   -7.147  18.052  1.00 26.45  0  62  GLY   D C   1 
ATOM   6335 O  O   . GLY   D  1 47  ? 8.240   -7.769  17.640  1.00 27.67  0  62  GLY   D O   1 
ATOM   6336 N  N   . PRO   D  1 48  ? 7.008   -5.921  17.581  1.00 27.89  0  63  PRO   D N   1 
ATOM   6337 C  CA  . PRO   D  1 48  ? 6.002   -5.056  18.189  1.00 26.99  0  63  PRO   D CA  1 
ATOM   6338 C  C   . PRO   D  1 48  ? 4.540   -5.350  17.831  1.00 27.31  0  63  PRO   D C   1 
ATOM   6339 O  O   . PRO   D  1 48  ? 3.676   -4.772  18.420  1.00 28.12  0  63  PRO   D O   1 
ATOM   6340 C  CB  . PRO   D  1 48  ? 6.396   -3.680  17.628  1.00 26.46  0  63  PRO   D CB  1 
ATOM   6341 C  CG  . PRO   D  1 48  ? 6.981   -3.954  16.291  1.00 27.66  0  63  PRO   D CG  1 
ATOM   6342 C  CD  . PRO   D  1 48  ? 7.674   -5.303  16.409  1.00 27.78  0  63  PRO   D CD  1 
ATOM   6343 N  N   . ASP   D  1 49  ? 4.276   -6.199  16.851  1.00 27.93  0  64  ASP   D N   1 
ATOM   6344 C  CA  . ASP   D  1 49  ? 2.876   -6.476  16.427  1.00 30.80  0  64  ASP   D CA  1 
ATOM   6345 C  C   . ASP   D  1 49  ? 2.219   -7.476  17.382  1.00 32.59  0  64  ASP   D C   1 
ATOM   6346 O  O   . ASP   D  1 49  ? 2.903   -8.385  17.834  1.00 31.46  0  64  ASP   D O   1 
ATOM   6347 C  CB  . ASP   D  1 49  ? 2.815   -7.023  15.005  1.00 31.51  0  64  ASP   D CB  1 
ATOM   6348 C  CG  . ASP   D  1 49  ? 3.185   -6.013  13.934  1.00 34.89  0  64  ASP   D CG  1 
ATOM   6349 O  OD1 . ASP   D  1 49  ? 3.075   -4.756  14.166  1.00 34.30  0  64  ASP   D OD1 1 
ATOM   6350 O  OD2 . ASP   D  1 49  ? 3.607   -6.499  12.898  1.00 41.66  -1 64  ASP   D OD2 1 
ATOM   6351 N  N   . VAL   D  1 50  ? 0.925   -7.323  17.642  1.00 31.56  0  65  VAL   D N   1 
ATOM   6352 C  CA  . VAL   D  1 50  ? 0.176   -8.166  18.611  1.00 31.96  0  65  VAL   D CA  1 
ATOM   6353 C  C   . VAL   D  1 50  ? -0.049  -9.532  17.957  1.00 36.61  0  65  VAL   D C   1 
ATOM   6354 O  O   . VAL   D  1 50  ? -0.606  -9.559  16.872  1.00 38.98  0  65  VAL   D O   1 
ATOM   6355 C  CB  . VAL   D  1 50  ? -1.144  -7.494  19.016  1.00 31.43  0  65  VAL   D CB  1 
ATOM   6356 C  CG1 . VAL   D  1 50  ? -1.999  -8.430  19.857  1.00 34.49  0  65  VAL   D CG1 1 
ATOM   6357 C  CG2 . VAL   D  1 50  ? -0.866  -6.195  19.757  1.00 30.05  0  65  VAL   D CG2 1 
ATOM   6358 N  N   . LYS   D  1 51  ? 0.285   -10.625 18.630  1.00 40.76  0  66  LYS   D N   1 
ATOM   6359 C  CA  . LYS   D  1 51  ? 0.050   -11.999 18.100  1.00 49.37  0  66  LYS   D CA  1 
ATOM   6360 C  C   . LYS   D  1 51  ? -1.026  -12.742 18.907  1.00 43.17  0  66  LYS   D C   1 
ATOM   6361 O  O   . LYS   D  1 51  ? -1.382  -12.305 20.002  1.00 37.47  0  66  LYS   D O   1 
ATOM   6362 C  CB  . LYS   D  1 51  ? 1.384   -12.737 18.047  1.00 61.43  0  66  LYS   D CB  1 
ATOM   6363 C  CG  . LYS   D  1 51  ? 2.299   -12.340 16.892  1.00 68.58  0  66  LYS   D CG  1 
ATOM   6364 C  CD  . LYS   D  1 51  ? 3.555   -11.642 17.362  1.00 73.60  0  66  LYS   D CD  1 
ATOM   6365 C  CE  . LYS   D  1 51  ? 4.369   -11.056 16.231  1.00 69.17  0  66  LYS   D CE  1 
ATOM   6366 N  NZ  . LYS   D  1 51  ? 5.585   -10.403 16.753  1.00 65.26  1  66  LYS   D NZ  1 
ATOM   6367 N  N   . ASP   D  1 52  ? -1.546  -13.843 18.354  1.00 46.59  0  67  ASP   D N   1 
ATOM   6368 C  CA  . ASP   D  1 52  ? -2.500  -14.755 19.045  1.00 42.89  0  67  ASP   D CA  1 
ATOM   6369 C  C   . ASP   D  1 52  ? -1.740  -15.519 20.130  1.00 34.30  0  67  ASP   D C   1 
ATOM   6370 O  O   . ASP   D  1 52  ? -0.886  -16.300 19.780  1.00 35.82  0  67  ASP   D O   1 
ATOM   6371 C  CB  . ASP   D  1 52  ? -3.167  -15.733 18.072  1.00 45.13  0  67  ASP   D CB  1 
ATOM   6372 C  CG  . ASP   D  1 52  ? -4.355  -16.477 18.672  1.00 48.40  0  67  ASP   D CG  1 
ATOM   6373 O  OD1 . ASP   D  1 52  ? -4.487  -16.521 19.919  1.00 48.53  0  67  ASP   D OD1 1 
ATOM   6374 O  OD2 . ASP   D  1 52  ? -5.145  -17.018 17.884  1.00 63.15  -1 67  ASP   D OD2 1 
ATOM   6375 N  N   . LEU   D  1 53  ? -2.057  -15.298 21.397  1.00 31.78  0  68  LEU   D N   1 
ATOM   6376 C  CA  . LEU   D  1 53  ? -1.440  -16.012 22.554  1.00 38.35  0  68  LEU   D CA  1 
ATOM   6377 C  C   . LEU   D  1 53  ? -1.539  -17.542 22.405  1.00 34.27  0  68  LEU   D C   1 
ATOM   6378 O  O   . LEU   D  1 53  ? -0.685  -18.223 22.968  1.00 35.07  0  68  LEU   D O   1 
ATOM   6379 C  CB  . LEU   D  1 53  ? -2.174  -15.615 23.836  1.00 38.79  0  68  LEU   D CB  1 
ATOM   6380 C  CG  . LEU   D  1 53  ? -2.026  -14.180 24.310  1.00 46.86  0  68  LEU   D CG  1 
ATOM   6381 C  CD1 . LEU   D  1 53  ? -2.984  -13.886 25.450  1.00 48.38  0  68  LEU   D CD1 1 
ATOM   6382 C  CD2 . LEU   D  1 53  ? -0.630  -13.946 24.774  1.00 51.33  0  68  LEU   D CD2 1 
ATOM   6383 N  N   . ALA   D  1 54  ? -2.583  -18.062 21.749  1.00 31.14  0  69  ALA   D N   1 
ATOM   6384 C  CA  . ALA   D  1 54  ? -2.828  -19.519 21.583  1.00 35.74  0  69  ALA   D CA  1 
ATOM   6385 C  C   . ALA   D  1 54  ? -1.687  -20.152 20.784  1.00 34.21  0  69  ALA   D C   1 
ATOM   6386 O  O   . ALA   D  1 54  ? -1.448  -21.335 20.979  1.00 37.27  0  69  ALA   D O   1 
ATOM   6387 C  CB  . ALA   D  1 54  ? -4.158  -19.764 20.898  1.00 36.31  0  69  ALA   D CB  1 
ATOM   6388 N  N   . ALA   D  1 55  ? -1.010  -19.373 19.933  1.00 30.54  0  70  ALA   D N   1 
ATOM   6389 C  CA  . ALA   D  1 55  ? 0.126   -19.798 19.091  1.00 30.04  0  70  ALA   D CA  1 
ATOM   6390 C  C   . ALA   D  1 55  ? 1.438   -19.849 19.873  1.00 29.40  0  70  ALA   D C   1 
ATOM   6391 O  O   . ALA   D  1 55  ? 2.434   -20.279 19.264  1.00 26.47  0  70  ALA   D O   1 
ATOM   6392 C  CB  . ALA   D  1 55  ? 0.256   -18.915 17.872  1.00 32.60  0  70  ALA   D CB  1 
ATOM   6393 N  N   . LEU   D  1 56  ? 1.459   -19.458 21.151  1.00 27.65  0  71  LEU   D N   1 
ATOM   6394 C  CA  . LEU   D  1 56  ? 2.695   -19.404 21.964  1.00 26.47  0  71  LEU   D CA  1 
ATOM   6395 C  C   . LEU   D  1 56  ? 2.588   -20.374 23.140  1.00 25.18  0  71  LEU   D C   1 
ATOM   6396 O  O   . LEU   D  1 56  ? 1.581   -20.351 23.836  1.00 31.74  0  71  LEU   D O   1 
ATOM   6397 C  CB  . LEU   D  1 56  ? 2.886   -17.967 22.445  1.00 29.30  0  71  LEU   D CB  1 
ATOM   6398 C  CG  . LEU   D  1 56  ? 4.061   -17.714 23.380  1.00 30.37  0  71  LEU   D CG  1 
ATOM   6399 C  CD1 . LEU   D  1 56  ? 5.359   -17.888 22.649  1.00 30.66  0  71  LEU   D CD1 1 
ATOM   6400 C  CD2 . LEU   D  1 56  ? 3.970   -16.292 23.945  1.00 32.93  0  71  LEU   D CD2 1 
ATOM   6401 N  N   . ARG   D  1 57  ? 3.651   -21.126 23.403  1.00 25.48  0  72  ARG   D N   1 
ATOM   6402 C  CA  . ARG   D  1 57  ? 3.853   -21.813 24.692  1.00 25.49  0  72  ARG   D CA  1 
ATOM   6403 C  C   . ARG   D  1 57  ? 5.275   -21.633 25.197  1.00 25.69  0  72  ARG   D C   1 
ATOM   6404 O  O   . ARG   D  1 57  ? 6.178   -21.257 24.430  1.00 24.50  0  72  ARG   D O   1 
ATOM   6405 C  CB  . ARG   D  1 57  ? 3.460   -23.287 24.566  1.00 30.87  0  72  ARG   D CB  1 
ATOM   6406 C  CG  . ARG   D  1 57  ? 1.950   -23.415 24.341  1.00 35.90  0  72  ARG   D CG  1 
ATOM   6407 C  CD  . ARG   D  1 57  ? 1.229   -24.658 24.744  1.00 39.75  0  72  ARG   D CD  1 
ATOM   6408 N  NE  . ARG   D  1 57  ? -0.101  -24.600 24.158  1.00 43.15  0  72  ARG   D NE  1 
ATOM   6409 C  CZ  . ARG   D  1 57  ? -0.858  -25.655 23.834  1.00 52.91  0  72  ARG   D CZ  1 
ATOM   6410 N  NH1 . ARG   D  1 57  ? -0.455  -26.910 24.026  1.00 49.07  1  72  ARG   D NH1 1 
ATOM   6411 N  NH2 . ARG   D  1 57  ? -2.043  -25.437 23.300  1.00 55.97  0  72  ARG   D NH2 1 
ATOM   6412 N  N   . VAL   D  1 58  ? 5.434   -21.953 26.476  1.00 25.13  0  73  VAL   D N   1 
ATOM   6413 C  CA  . VAL   D  1 58  ? 6.726   -21.878 27.209  1.00 27.68  0  73  VAL   D CA  1 
ATOM   6414 C  C   . VAL   D  1 58  ? 7.136   -23.298 27.584  1.00 24.40  0  73  VAL   D C   1 
ATOM   6415 O  O   . VAL   D  1 58  ? 6.282   -24.064 28.064  1.00 24.50  0  73  VAL   D O   1 
ATOM   6416 C  CB  . VAL   D  1 58  ? 6.610   -20.975 28.451  1.00 28.16  0  73  VAL   D CB  1 
ATOM   6417 C  CG1 . VAL   D  1 58  ? 7.838   -21.034 29.308  1.00 31.39  0  73  VAL   D CG1 1 
ATOM   6418 C  CG2 . VAL   D  1 58  ? 6.296   -19.529 28.085  1.00 28.76  0  73  VAL   D CG2 1 
ATOM   6419 N  N   . GLN   D  1 59  ? 8.426   -23.591 27.479  1.00 25.12  0  74  GLN   D N   1 
ATOM   6420 C  CA  . GLN   D  1 59  ? 9.045   -24.839 27.966  1.00 25.79  0  74  GLN   D CA  1 
ATOM   6421 C  C   . GLN   D  1 59  ? 10.081  -24.433 29.004  1.00 26.82  0  74  GLN   D C   1 
ATOM   6422 O  O   . GLN   D  1 59  ? 11.043  -23.722 28.615  1.00 26.30  0  74  GLN   D O   1 
ATOM   6423 C  CB  . GLN   D  1 59  ? 9.646   -25.598 26.787  1.00 23.67  0  74  GLN   D CB  1 
ATOM   6424 C  CG  . GLN   D  1 59  ? 10.522  -26.785 27.170  1.00 24.86  0  74  GLN   D CG  1 
ATOM   6425 C  CD  . GLN   D  1 59  ? 9.771   -27.868 27.917  1.00 26.82  0  74  GLN   D CD  1 
ATOM   6426 O  OE1 . GLN   D  1 59  ? 8.668   -28.278 27.544  1.00 27.21  0  74  GLN   D OE1 1 
ATOM   6427 N  NE2 . GLN   D  1 59  ? 10.341  -28.321 29.014  1.00 28.28  0  74  GLN   D NE2 1 
ATOM   6428 N  N   . LEU   D  1 60  ? 9.979   -24.986 30.222  1.00 26.41  0  75  LEU   D N   1 
ATOM   6429 C  CA  . LEU   D  1 60  ? 10.977  -24.753 31.286  1.00 28.32  0  75  LEU   D CA  1 
ATOM   6430 C  C   . LEU   D  1 60  ? 12.242  -25.555 30.972  1.00 29.63  0  75  LEU   D C   1 
ATOM   6431 O  O   . LEU   D  1 60  ? 12.271  -26.261 29.951  1.00 32.44  0  75  LEU   D O   1 
ATOM   6432 C  CB  . LEU   D  1 60  ? 10.403  -25.131 32.649  1.00 32.87  0  75  LEU   D CB  1 
ATOM   6433 C  CG  . LEU   D  1 60  ? 9.096   -24.447 33.028  1.00 34.52  0  75  LEU   D CG  1 
ATOM   6434 C  CD1 . LEU   D  1 60  ? 8.559   -25.054 34.309  1.00 35.64  0  75  LEU   D CD1 1 
ATOM   6435 C  CD2 . LEU   D  1 60  ? 9.274   -22.945 33.162  1.00 32.51  0  75  LEU   D CD2 1 
ATOM   6436 N  N   . ARG   D  1 61  ? 13.265  -25.450 31.809  1.00 31.53  0  76  ARG   D N   1 
ATOM   6437 C  CA  . ARG   D  1 61  ? 14.613  -25.948 31.448  1.00 34.13  0  76  ARG   D CA  1 
ATOM   6438 C  C   . ARG   D  1 61  ? 14.553  -27.403 30.968  1.00 35.89  0  76  ARG   D C   1 
ATOM   6439 O  O   . ARG   D  1 61  ? 13.957  -28.234 31.679  1.00 36.50  0  76  ARG   D O   1 
ATOM   6440 C  CB  . ARG   D  1 61  ? 15.599  -25.864 32.600  1.00 35.20  0  76  ARG   D CB  1 
ATOM   6441 C  CG  . ARG   D  1 61  ? 17.034  -25.871 32.096  1.00 36.31  0  76  ARG   D CG  1 
ATOM   6442 C  CD  . ARG   D  1 61  ? 17.885  -26.371 33.222  1.00 39.17  0  76  ARG   D CD  1 
ATOM   6443 N  NE  . ARG   D  1 61  ? 19.317  -26.366 32.937  1.00 38.53  0  76  ARG   D NE  1 
ATOM   6444 C  CZ  . ARG   D  1 61  ? 19.949  -27.295 32.237  1.00 36.83  0  76  ARG   D CZ  1 
ATOM   6445 N  NH1 . ARG   D  1 61  ? 19.271  -28.272 31.655  1.00 40.40  1  76  ARG   D NH1 1 
ATOM   6446 N  NH2 . ARG   D  1 61  ? 21.266  -27.243 32.122  1.00 32.83  0  76  ARG   D NH2 1 
ATOM   6447 N  N   . GLU   D  1 62  ? 15.130  -27.640 29.786  1.00 30.74  0  77  GLU   D N   1 
ATOM   6448 C  CA  A GLU   D  1 62  ? 15.405  -29.012 29.296  0.50 32.96  0  77  GLU   D CA  1 
ATOM   6449 C  CA  B GLU   D  1 62  ? 15.362  -28.953 29.122  0.50 31.46  0  77  GLU   D CA  1 
ATOM   6450 C  C   . GLU   D  1 62  ? 16.851  -29.040 28.782  1.00 33.77  0  77  GLU   D C   1 
ATOM   6451 O  O   . GLU   D  1 62  ? 17.372  -28.011 28.280  1.00 38.14  0  77  GLU   D O   1 
ATOM   6452 C  CB  A GLU   D  1 62  ? 14.301  -29.535 28.362  0.50 32.04  0  77  GLU   D CB  1 
ATOM   6453 C  CB  B GLU   D  1 62  ? 14.638  -29.047 27.775  0.50 28.40  0  77  GLU   D CB  1 
ATOM   6454 C  CG  A GLU   D  1 62  ? 14.192  -28.863 27.015  0.50 32.51  0  77  GLU   D CG  1 
ATOM   6455 C  CG  B GLU   D  1 62  ? 13.197  -29.494 27.849  0.50 27.54  0  77  GLU   D CG  1 
ATOM   6456 C  CD  A GLU   D  1 62  ? 12.965  -29.223 26.189  0.50 31.35  0  77  GLU   D CD  1 
ATOM   6457 C  CD  B GLU   D  1 62  ? 12.511  -29.628 26.498  0.50 27.08  0  77  GLU   D CD  1 
ATOM   6458 O  OE1 A GLU   D  1 62  ? 12.268  -30.190 26.513  0.50 33.24  0  77  GLU   D OE1 1 
ATOM   6459 O  OE1 B GLU   D  1 62  ? 12.947  -28.972 25.559  0.50 25.62  0  77  GLU   D OE1 1 
ATOM   6460 O  OE2 A GLU   D  1 62  ? 12.723  -28.513 25.224  0.50 30.29  -1 77  GLU   D OE2 1 
ATOM   6461 O  OE2 B GLU   D  1 62  ? 11.535  -30.387 26.384  0.50 27.66  -1 77  GLU   D OE2 1 
ATOM   6462 N  N   . GLN   D  1 63  ? 17.502  -30.172 29.000  1.00 28.93  0  78  GLN   D N   1 
ATOM   6463 C  CA  . GLN   D  1 63  ? 18.914  -30.372 28.573  1.00 28.95  0  78  GLN   D CA  1 
ATOM   6464 C  C   . GLN   D  1 63  ? 18.958  -30.454 27.040  1.00 29.41  0  78  GLN   D C   1 
ATOM   6465 O  O   . GLN   D  1 63  ? 19.911  -29.915 26.453  1.00 28.54  0  78  GLN   D O   1 
ATOM   6466 C  CB  . GLN   D  1 63  ? 19.473  -31.625 29.251  1.00 28.53  0  78  GLN   D CB  1 
ATOM   6467 C  CG  . GLN   D  1 63  ? 20.976  -31.773 29.165  1.00 28.81  0  78  GLN   D CG  1 
ATOM   6468 C  CD  . GLN   D  1 63  ? 21.732  -30.598 29.716  1.00 32.96  0  78  GLN   D CD  1 
ATOM   6469 O  OE1 . GLN   D  1 63  ? 21.268  -29.880 30.611  1.00 29.56  0  78  GLN   D OE1 1 
ATOM   6470 N  NE2 . GLN   D  1 63  ? 22.898  -30.363 29.136  1.00 36.68  0  78  GLN   D NE2 1 
ATOM   6471 N  N   . HIS   D  1 64  ? 17.968  -31.103 26.418  1.00 29.14  0  79  HIS   D N   1 
ATOM   6472 C  CA  . HIS   D  1 64  ? 17.853  -31.290 24.947  1.00 28.09  0  79  HIS   D CA  1 
ATOM   6473 C  C   . HIS   D  1 64  ? 16.474  -30.830 24.496  1.00 28.58  0  79  HIS   D C   1 
ATOM   6474 O  O   . HIS   D  1 64  ? 15.491  -31.383 25.000  1.00 35.62  0  79  HIS   D O   1 
ATOM   6475 C  CB  . HIS   D  1 64  ? 18.165  -32.751 24.593  1.00 30.57  0  79  HIS   D CB  1 
ATOM   6476 C  CG  . HIS   D  1 64  ? 19.532  -33.191 24.986  1.00 28.11  0  79  HIS   D CG  1 
ATOM   6477 N  ND1 . HIS   D  1 64  ? 19.763  -33.917 26.157  1.00 29.34  0  79  HIS   D ND1 1 
ATOM   6478 C  CD2 . HIS   D  1 64  ? 20.736  -32.986 24.422  1.00 27.83  0  79  HIS   D CD2 1 
ATOM   6479 C  CE1 . HIS   D  1 64  ? 21.059  -34.156 26.278  1.00 28.64  0  79  HIS   D CE1 1 
ATOM   6480 N  NE2 . HIS   D  1 64  ? 21.679  -33.607 25.217  1.00 30.13  0  79  HIS   D NE2 1 
ATOM   6481 N  N   . LEU   D  1 65  ? 16.398  -29.826 23.608  1.00 28.15  0  80  LEU   D N   1 
ATOM   6482 C  CA  . LEU   D  1 65  ? 15.113  -29.327 23.050  1.00 27.11  0  80  LEU   D CA  1 
ATOM   6483 C  C   . LEU   D  1 65  ? 14.297  -30.469 22.461  1.00 27.17  0  80  LEU   D C   1 
ATOM   6484 O  O   . LEU   D  1 65  ? 14.888  -31.308 21.765  1.00 26.32  0  80  LEU   D O   1 
ATOM   6485 C  CB  . LEU   D  1 65  ? 15.326  -28.335 21.910  1.00 29.33  0  80  LEU   D CB  1 
ATOM   6486 C  CG  . LEU   D  1 65  ? 15.539  -26.880 22.260  1.00 29.81  0  80  LEU   D CG  1 
ATOM   6487 C  CD1 . LEU   D  1 65  ? 15.589  -26.099 20.958  1.00 27.55  0  80  LEU   D CD1 1 
ATOM   6488 C  CD2 . LEU   D  1 65  ? 14.481  -26.298 23.190  1.00 30.84  0  80  LEU   D CD2 1 
ATOM   6489 N  N   . TYR   D  1 66  ? 12.990  -30.459 22.714  1.00 24.82  0  81  TYR   D N   1 
ATOM   6490 C  CA  . TYR   D  1 66  ? 11.957  -31.292 22.050  1.00 28.44  0  81  TYR   D CA  1 
ATOM   6491 C  C   . TYR   D  1 66  ? 11.812  -32.684 22.682  1.00 28.63  0  81  TYR   D C   1 
ATOM   6492 O  O   . TYR   D  1 66  ? 10.733  -33.250 22.566  1.00 30.37  0  81  TYR   D O   1 
ATOM   6493 C  CB  . TYR   D  1 66  ? 12.195  -31.404 20.542  1.00 26.92  0  81  TYR   D CB  1 
ATOM   6494 C  CG  . TYR   D  1 66  ? 12.341  -30.082 19.853  1.00 26.06  0  81  TYR   D CG  1 
ATOM   6495 C  CD1 . TYR   D  1 66  ? 11.298  -29.166 19.874  1.00 25.05  0  81  TYR   D CD1 1 
ATOM   6496 C  CD2 . TYR   D  1 66  ? 13.529  -29.708 19.252  1.00 23.87  0  81  TYR   D CD2 1 
ATOM   6497 C  CE1 . TYR   D  1 66  ? 11.417  -27.923 19.279  1.00 24.32  0  81  TYR   D CE1 1 
ATOM   6498 C  CE2 . TYR   D  1 66  ? 13.666  -28.450 18.683  1.00 27.23  0  81  TYR   D CE2 1 
ATOM   6499 C  CZ  . TYR   D  1 66  ? 12.608  -27.551 18.692  1.00 25.94  0  81  TYR   D CZ  1 
ATOM   6500 O  OH  . TYR   D  1 66  ? 12.697  -26.343 18.062  1.00 25.70  0  81  TYR   D OH  1 
ATOM   6501 N  N   A TYR   D  1 67  ? 12.833  -33.192 23.365  0.50 28.67  0  82  TYR   D N   1 
ATOM   6502 N  N   B TYR   D  1 67  ? 12.855  -33.204 23.332  0.50 32.44  0  82  TYR   D N   1 
ATOM   6503 C  CA  A TYR   D  1 67  ? 12.886  -34.616 23.790  0.50 31.77  0  82  TYR   D CA  1 
ATOM   6504 C  CA  B TYR   D  1 67  ? 12.885  -34.597 23.855  0.50 38.71  0  82  TYR   D CA  1 
ATOM   6505 C  C   A TYR   D  1 67  ? 11.888  -34.895 24.926  0.50 34.10  0  82  TYR   D C   1 
ATOM   6506 C  C   B TYR   D  1 67  ? 11.727  -34.822 24.832  0.50 38.20  0  82  TYR   D C   1 
ATOM   6507 O  O   A TYR   D  1 67  ? 11.336  -36.005 24.907  0.50 37.46  0  82  TYR   D O   1 
ATOM   6508 O  O   B TYR   D  1 67  ? 10.898  -35.740 24.586  0.50 39.72  0  82  TYR   D O   1 
ATOM   6509 C  CB  A TYR   D  1 67  ? 14.348  -35.005 23.986  0.50 29.46  0  82  TYR   D CB  1 
ATOM   6510 C  CB  B TYR   D  1 67  ? 14.226  -34.911 24.518  0.50 41.93  0  82  TYR   D CB  1 
ATOM   6511 C  CG  A TYR   D  1 67  ? 15.039  -35.186 22.652  0.50 27.09  0  82  TYR   D CG  1 
ATOM   6512 C  CG  B TYR   D  1 67  ? 14.444  -36.382 24.773  0.50 46.10  0  82  TYR   D CG  1 
ATOM   6513 C  CD1 A TYR   D  1 67  ? 14.820  -36.313 21.870  0.50 27.92  0  82  TYR   D CD1 1 
ATOM   6514 C  CD1 B TYR   D  1 67  ? 13.562  -37.336 24.290  0.50 48.44  0  82  TYR   D CD1 1 
ATOM   6515 C  CD2 A TYR   D  1 67  ? 15.827  -34.188 22.108  0.50 27.13  0  82  TYR   D CD2 1 
ATOM   6516 C  CD2 B TYR   D  1 67  ? 15.562  -36.827 25.459  0.50 51.96  0  82  TYR   D CD2 1 
ATOM   6517 C  CE1 A TYR   D  1 67  ? 15.429  -36.481 20.637  0.50 26.29  0  82  TYR   D CE1 1 
ATOM   6518 C  CE1 B TYR   D  1 67  ? 13.767  -38.689 24.511  0.50 47.36  0  82  TYR   D CE1 1 
ATOM   6519 C  CE2 A TYR   D  1 67  ? 16.417  -34.325 20.864  0.50 26.99  0  82  TYR   D CE2 1 
ATOM   6520 C  CE2 B TYR   D  1 67  ? 15.782  -38.173 25.689  0.50 51.70  0  82  TYR   D CE2 1 
ATOM   6521 C  CZ  A TYR   D  1 67  ? 16.246  -35.490 20.135  0.50 26.97  0  82  TYR   D CZ  1 
ATOM   6522 C  CZ  B TYR   D  1 67  ? 14.877  -39.104 25.218  0.50 47.42  0  82  TYR   D CZ  1 
ATOM   6523 O  OH  A TYR   D  1 67  ? 16.853  -35.630 18.921  0.50 25.92  0  82  TYR   D OH  1 
ATOM   6524 O  OH  B TYR   D  1 67  ? 15.103  -40.428 25.437  0.50 54.55  0  82  TYR   D OH  1 
ATOM   6525 N  N   . GLN   D  1 68  ? 11.636  -33.957 25.847  1.00 36.12  0  83  GLN   D N   1 
ATOM   6526 C  CA  . GLN   D  1 68  ? 10.757  -34.177 27.036  1.00 39.54  0  83  GLN   D CA  1 
ATOM   6527 C  C   . GLN   D  1 68  ? 9.782   -33.018 27.224  1.00 32.47  0  83  GLN   D C   1 
ATOM   6528 O  O   . GLN   D  1 68  ? 9.555   -32.661 28.360  1.00 36.51  0  83  GLN   D O   1 
ATOM   6529 C  CB  . GLN   D  1 68  ? 11.598  -34.268 28.326  1.00 45.60  0  83  GLN   D CB  1 
ATOM   6530 C  CG  . GLN   D  1 68  ? 12.680  -35.336 28.318  1.00 52.82  0  83  GLN   D CG  1 
ATOM   6531 C  CD  . GLN   D  1 68  ? 12.158  -36.680 28.736  1.00 53.92  0  83  GLN   D CD  1 
ATOM   6532 O  OE1 . GLN   D  1 68  ? 12.482  -37.159 29.803  1.00 49.44  0  83  GLN   D OE1 1 
ATOM   6533 N  NE2 . GLN   D  1 68  ? 11.343  -37.297 27.904  1.00 67.79  0  83  GLN   D NE2 1 
ATOM   6534 N  N   . ASP   D  1 69  ? 9.189   -32.490 26.162  1.00 29.96  0  84  ASP   D N   1 
ATOM   6535 C  CA  . ASP   D  1 69  ? 8.413   -31.233 26.239  1.00 29.20  0  84  ASP   D CA  1 
ATOM   6536 C  C   . ASP   D  1 69  ? 7.225   -31.412 27.210  1.00 30.79  0  84  ASP   D C   1 
ATOM   6537 O  O   . ASP   D  1 69  ? 6.534   -32.404 27.127  1.00 28.25  0  84  ASP   D O   1 
ATOM   6538 C  CB  . ASP   D  1 69  ? 7.939   -30.811 24.854  1.00 29.03  0  84  ASP   D CB  1 
ATOM   6539 C  CG  . ASP   D  1 69  ? 9.001   -30.171 23.957  1.00 31.37  0  84  ASP   D CG  1 
ATOM   6540 O  OD1 . ASP   D  1 69  ? 10.166  -30.013 24.425  1.00 27.33  0  84  ASP   D OD1 1 
ATOM   6541 O  OD2 . ASP   D  1 69  ? 8.621   -29.817 22.780  1.00 29.65  -1 84  ASP   D OD2 1 
ATOM   6542 N  N   . GLN   D  1 70  ? 7.005   -30.452 28.096  1.00 30.52  0  85  GLN   D N   1 
ATOM   6543 C  CA  . GLN   D  1 70  ? 5.733   -30.229 28.821  1.00 30.73  0  85  GLN   D CA  1 
ATOM   6544 C  C   . GLN   D  1 70  ? 5.429   -28.740 28.696  1.00 31.77  0  85  GLN   D C   1 
ATOM   6545 O  O   . GLN   D  1 70  ? 5.933   -27.963 29.504  1.00 32.99  0  85  GLN   D O   1 
ATOM   6546 C  CB  . GLN   D  1 70  ? 5.861   -30.712 30.269  1.00 35.87  0  85  GLN   D CB  1 
ATOM   6547 C  CG  . GLN   D  1 70  ? 6.470   -32.111 30.371  1.00 38.07  0  85  GLN   D CG  1 
ATOM   6548 C  CD  . GLN   D  1 70  ? 6.583   -32.717 31.754  1.00 48.26  0  85  GLN   D CD  1 
ATOM   6549 O  OE1 . GLN   D  1 70  ? 5.922   -33.718 32.046  1.00 47.28  0  85  GLN   D OE1 1 
ATOM   6550 N  NE2 . GLN   D  1 70  ? 7.487   -32.184 32.582  1.00 52.16  0  85  GLN   D NE2 1 
ATOM   6551 N  N   . LEU   D  1 71  ? 4.687   -28.368 27.657  1.00 28.64  0  86  LEU   D N   1 
ATOM   6552 C  CA  . LEU   D  1 71  ? 4.557   -26.967 27.210  1.00 31.36  0  86  LEU   D CA  1 
ATOM   6553 C  C   . LEU   D  1 71  ? 3.539   -26.266 28.123  1.00 31.91  0  86  LEU   D C   1 
ATOM   6554 O  O   . LEU   D  1 71  ? 2.532   -26.881 28.442  1.00 28.65  0  86  LEU   D O   1 
ATOM   6555 C  CB  . LEU   D  1 71  ? 4.141   -26.949 25.723  1.00 28.82  0  86  LEU   D CB  1 
ATOM   6556 C  CG  . LEU   D  1 71  ? 5.163   -27.578 24.781  1.00 29.99  0  86  LEU   D CG  1 
ATOM   6557 C  CD1 . LEU   D  1 71  ? 4.686   -27.572 23.346  1.00 31.24  0  86  LEU   D CD1 1 
ATOM   6558 C  CD2 . LEU   D  1 71  ? 6.530   -26.920 24.922  1.00 30.66  0  86  LEU   D CD2 1 
ATOM   6559 N  N   . LEU   D  1 72  ? 3.778   -25.009 28.498  1.00 31.08  0  87  LEU   D N   1 
ATOM   6560 C  CA  . LEU   D  1 72  ? 2.869   -24.205 29.365  1.00 26.96  0  87  LEU   D CA  1 
ATOM   6561 C  C   . LEU   D  1 72  ? 2.215   -23.092 28.551  1.00 27.62  0  87  LEU   D C   1 
ATOM   6562 O  O   . LEU   D  1 72  ? 2.906   -22.350 27.835  1.00 30.70  0  87  LEU   D O   1 
ATOM   6563 C  CB  . LEU   D  1 72  ? 3.717   -23.674 30.519  1.00 27.31  0  87  LEU   D CB  1 
ATOM   6564 C  CG  . LEU   D  1 72  ? 4.451   -24.752 31.327  1.00 30.42  0  87  LEU   D CG  1 
ATOM   6565 C  CD1 . LEU   D  1 72  ? 5.391   -24.110 32.318  1.00 30.67  0  87  LEU   D CD1 1 
ATOM   6566 C  CD2 . LEU   D  1 72  ? 3.464   -25.686 32.020  1.00 28.98  0  87  LEU   D CD2 1 
ATOM   6567 N  N   . PRO   D  1 73  ? 0.871   -22.930 28.602  1.00 24.07  0  88  PRO   D N   1 
ATOM   6568 C  CA  . PRO   D  1 73  ? 0.233   -21.820 27.910  1.00 27.90  0  88  PRO   D CA  1 
ATOM   6569 C  C   . PRO   D  1 73  ? 0.466   -20.493 28.664  1.00 28.05  0  88  PRO   D C   1 
ATOM   6570 O  O   . PRO   D  1 73  ? 0.789   -20.510 29.842  1.00 24.62  0  88  PRO   D O   1 
ATOM   6571 C  CB  . PRO   D  1 73  ? -1.228  -22.293 27.831  1.00 29.43  0  88  PRO   D CB  1 
ATOM   6572 C  CG  . PRO   D  1 73  ? -1.400  -23.056 29.130  1.00 29.95  0  88  PRO   D CG  1 
ATOM   6573 C  CD  . PRO   D  1 73  ? -0.093  -23.805 29.274  1.00 25.57  0  88  PRO   D CD  1 
ATOM   6574 N  N   . VAL   D  1 74  ? 0.304   -19.382 27.935  1.00 29.04  0  89  VAL   D N   1 
ATOM   6575 C  CA  . VAL   D  1 74  ? 0.574   -17.985 28.402  1.00 26.20  0  89  VAL   D CA  1 
ATOM   6576 C  C   . VAL   D  1 74  ? -0.761  -17.270 28.535  1.00 23.81  0  89  VAL   D C   1 
ATOM   6577 O  O   . VAL   D  1 74  ? -1.549  -17.383 27.578  1.00 25.06  0  89  VAL   D O   1 
ATOM   6578 C  CB  . VAL   D  1 74  ? 1.500   -17.299 27.381  1.00 27.51  0  89  VAL   D CB  1 
ATOM   6579 C  CG1 . VAL   D  1 74  ? 1.579   -15.797 27.584  1.00 27.20  0  89  VAL   D CG1 1 
ATOM   6580 C  CG2 . VAL   D  1 74  ? 2.888   -17.881 27.500  1.00 27.27  0  89  VAL   D CG2 1 
ATOM   6581 N  N   . SER   D  1 75  ? -1.006  -16.515 29.612  1.00 24.64  0  90  SER   D N   1 
ATOM   6582 C  CA  . SER   D  1 75  ? -2.252  -15.686 29.759  1.00 26.52  0  90  SER   D CA  1 
ATOM   6583 C  C   . SER   D  1 75  ? -2.085  -14.269 29.200  1.00 26.42  0  90  SER   D C   1 
ATOM   6584 O  O   . SER   D  1 75  ? -3.100  -13.679 28.793  1.00 25.07  0  90  SER   D O   1 
ATOM   6585 C  CB  . SER   D  1 75  ? -2.752  -15.599 31.175  1.00 23.34  0  90  SER   D CB  1 
ATOM   6586 O  OG  . SER   D  1 75  ? -1.716  -15.171 32.015  1.00 29.75  0  90  SER   D OG  1 
ATOM   6587 N  N   . ARG   D  1 76  ? -0.876  -13.728 29.244  1.00 26.62  0  91  ARG   D N   1 
ATOM   6588 C  CA  . ARG   D  1 76  ? -0.619  -12.315 28.889  1.00 30.03  0  91  ARG   D CA  1 
ATOM   6589 C  C   . ARG   D  1 76  ? 0.774   -12.187 28.281  1.00 27.60  0  91  ARG   D C   1 
ATOM   6590 O  O   . ARG   D  1 76  ? 1.725   -12.780 28.826  1.00 22.92  0  91  ARG   D O   1 
ATOM   6591 C  CB  . ARG   D  1 76  ? -0.650  -11.409 30.133  1.00 32.82  0  91  ARG   D CB  1 
ATOM   6592 C  CG  . ARG   D  1 76  ? -2.024  -11.185 30.743  1.00 42.55  0  91  ARG   D CG  1 
ATOM   6593 C  CD  . ARG   D  1 76  ? -2.327  -9.708  30.983  1.00 50.05  0  91  ARG   D CD  1 
ATOM   6594 N  NE  . ARG   D  1 76  ? -1.623  -9.133  32.107  1.00 55.14  0  91  ARG   D NE  1 
ATOM   6595 C  CZ  . ARG   D  1 76  ? -1.542  -7.820  32.387  1.00 56.81  0  91  ARG   D CZ  1 
ATOM   6596 N  NH1 . ARG   D  1 76  ? -2.043  -6.899  31.576  1.00 53.23  1  91  ARG   D NH1 1 
ATOM   6597 N  NH2 . ARG   D  1 76  ? -0.922  -7.434  33.489  1.00 53.83  0  91  ARG   D NH2 1 
ATOM   6598 N  N   . ILE   D  1 77  ? 0.889   -11.360 27.249  1.00 29.67  0  92  ILE   D N   1 
ATOM   6599 C  CA  . ILE   D  1 77  ? 2.206   -10.864 26.748  1.00 28.97  0  92  ILE   D CA  1 
ATOM   6600 C  C   . ILE   D  1 77  ? 2.236   -9.371  27.052  1.00 26.09  0  92  ILE   D C   1 
ATOM   6601 O  O   . ILE   D  1 77  ? 1.330   -8.656  26.569  1.00 30.83  0  92  ILE   D O   1 
ATOM   6602 C  CB  . ILE   D  1 77  ? 2.367   -11.171 25.251  1.00 28.33  0  92  ILE   D CB  1 
ATOM   6603 C  CG1 . ILE   D  1 77  ? 2.404   -12.678 24.967  1.00 33.60  0  92  ILE   D CG1 1 
ATOM   6604 C  CG2 . ILE   D  1 77  ? 3.592   -10.480 24.698  1.00 30.96  0  92  ILE   D CG2 1 
ATOM   6605 C  CD1 . ILE   D  1 77  ? 2.190   -13.039 23.492  1.00 33.82  0  92  ILE   D CD1 1 
ATOM   6606 N  N   . ILE   D  1 78  ? 3.202   -8.931  27.832  1.00 28.30  0  93  ILE   D N   1 
ATOM   6607 C  CA  . ILE   D  1 78  ? 3.384   -7.487  28.150  1.00 31.24  0  93  ILE   D CA  1 
ATOM   6608 C  C   . ILE   D  1 78  ? 4.711   -7.019  27.534  1.00 27.44  0  93  ILE   D C   1 
ATOM   6609 O  O   . ILE   D  1 78  ? 5.784   -7.550  27.875  1.00 25.32  0  93  ILE   D O   1 
ATOM   6610 C  CB  . ILE   D  1 78  ? 3.292   -7.268  29.662  1.00 32.44  0  93  ILE   D CB  1 
ATOM   6611 C  CG1 . ILE   D  1 78  ? 1.963   -7.831  30.171  1.00 36.87  0  93  ILE   D CG1 1 
ATOM   6612 C  CG2 . ILE   D  1 78  ? 3.457   -5.800  30.009  1.00 34.11  0  93  ILE   D CG2 1 
ATOM   6613 C  CD1 . ILE   D  1 78  ? 1.774   -7.716  31.625  1.00 44.58  0  93  ILE   D CD1 1 
ATOM   6614 N  N   . VAL   D  1 79  ? 4.611   -6.105  26.593  1.00 26.80  0  94  VAL   D N   1 
ATOM   6615 C  CA  . VAL   D  1 79  ? 5.796   -5.610  25.836  1.00 26.10  0  94  VAL   D CA  1 
ATOM   6616 C  C   . VAL   D  1 79  ? 6.025   -4.163  26.245  1.00 25.41  0  94  VAL   D C   1 
ATOM   6617 O  O   . VAL   D  1 79  ? 5.044   -3.382  26.275  1.00 23.13  0  94  VAL   D O   1 
ATOM   6618 C  CB  . VAL   D  1 79  ? 5.567   -5.757  24.330  1.00 28.42  0  94  VAL   D CB  1 
ATOM   6619 C  CG1 . VAL   D  1 79  ? 6.742   -5.213  23.529  1.00 29.64  0  94  VAL   D CG1 1 
ATOM   6620 C  CG2 . VAL   D  1 79  ? 5.302   -7.206  23.964  1.00 31.26  0  94  VAL   D CG2 1 
ATOM   6621 N  N   . HIS   D  1 80  ? 7.260   -3.798  26.530  1.00 24.76  0  95  HIS   D N   1 
ATOM   6622 C  CA  . HIS   D  1 80  ? 7.596   -2.393  26.869  1.00 25.40  0  95  HIS   D CA  1 
ATOM   6623 C  C   . HIS   D  1 80  ? 6.956   -1.482  25.837  1.00 25.28  0  95  HIS   D C   1 
ATOM   6624 O  O   . HIS   D  1 80  ? 7.205   -1.641  24.640  1.00 26.48  0  95  HIS   D O   1 
ATOM   6625 C  CB  . HIS   D  1 80  ? 9.097   -2.182  26.959  1.00 24.52  0  95  HIS   D CB  1 
ATOM   6626 C  CG  . HIS   D  1 80  ? 9.411   -1.006  27.813  1.00 28.03  0  95  HIS   D CG  1 
ATOM   6627 N  ND1 . HIS   D  1 80  ? 9.138   0.276   27.411  1.00 28.45  0  95  HIS   D ND1 1 
ATOM   6628 C  CD2 . HIS   D  1 80  ? 9.871   -0.928  29.080  1.00 28.91  0  95  HIS   D CD2 1 
ATOM   6629 C  CE1 . HIS   D  1 80  ? 9.433   1.110   28.387  1.00 30.15  0  95  HIS   D CE1 1 
ATOM   6630 N  NE2 . HIS   D  1 80  ? 9.877   0.390   29.426  1.00 31.52  0  95  HIS   D NE2 1 
ATOM   6631 N  N   . PRO   D  1 81  ? 6.138   -0.486  26.232  1.00 24.20  0  96  PRO   D N   1 
ATOM   6632 C  CA  . PRO   D  1 81  ? 5.474   0.378   25.254  1.00 24.99  0  96  PRO   D CA  1 
ATOM   6633 C  C   . PRO   D  1 81  ? 6.437   1.301   24.449  1.00 26.90  0  96  PRO   D C   1 
ATOM   6634 O  O   . PRO   D  1 81  ? 6.047   1.837   23.449  1.00 27.84  0  96  PRO   D O   1 
ATOM   6635 C  CB  . PRO   D  1 81  ? 4.518   1.217   26.116  1.00 25.16  0  96  PRO   D CB  1 
ATOM   6636 C  CG  . PRO   D  1 81  ? 5.121   1.221   27.483  1.00 26.41  0  96  PRO   D CG  1 
ATOM   6637 C  CD  . PRO   D  1 81  ? 5.847   -0.104  27.625  1.00 28.40  0  96  PRO   D CD  1 
ATOM   6638 N  N   . GLN   D  1 82  ? 7.681   1.470   24.876  1.00 28.39  0  97  GLN   D N   1 
ATOM   6639 C  CA  . GLN   D  1 82  ? 8.692   2.260   24.121  1.00 30.35  0  97  GLN   D CA  1 
ATOM   6640 C  C   . GLN   D  1 82  ? 9.365   1.396   23.053  1.00 29.95  0  97  GLN   D C   1 
ATOM   6641 O  O   . GLN   D  1 82  ? 10.131  1.976   22.284  1.00 27.79  0  97  GLN   D O   1 
ATOM   6642 C  CB  . GLN   D  1 82  ? 9.722   2.873   25.059  1.00 30.70  0  97  GLN   D CB  1 
ATOM   6643 C  CG  . GLN   D  1 82  ? 9.157   4.067   25.821  1.00 34.31  0  97  GLN   D CG  1 
ATOM   6644 C  CD  . GLN   D  1 82  ? 10.243  4.630   26.697  1.00 40.17  0  97  GLN   D CD  1 
ATOM   6645 O  OE1 . GLN   D  1 82  ? 10.228  4.509   27.910  1.00 48.73  0  97  GLN   D OE1 1 
ATOM   6646 N  NE2 . GLN   D  1 82  ? 11.272  5.161   26.074  1.00 50.77  0  97  GLN   D NE2 1 
ATOM   6647 N  N   . PHE   D  1 83  ? 9.070   0.089   22.979  1.00 26.26  0  98  PHE   D N   1 
ATOM   6648 C  CA  . PHE   D  1 83  ? 9.718   -0.815  22.010  1.00 24.64  0  98  PHE   D CA  1 
ATOM   6649 C  C   . PHE   D  1 83  ? 9.102   -0.684  20.620  1.00 24.47  0  98  PHE   D C   1 
ATOM   6650 O  O   . PHE   D  1 83  ? 7.881   -0.773  20.464  1.00 23.50  0  98  PHE   D O   1 
ATOM   6651 C  CB  . PHE   D  1 83  ? 9.617   -2.274  22.413  1.00 26.87  0  98  PHE   D CB  1 
ATOM   6652 C  CG  . PHE   D  1 83  ? 10.209  -3.182  21.371  1.00 23.94  0  98  PHE   D CG  1 
ATOM   6653 C  CD1 . PHE   D  1 83  ? 11.582  -3.209  21.173  1.00 22.00  0  98  PHE   D CD1 1 
ATOM   6654 C  CD2 . PHE   D  1 83  ? 9.383   -3.926  20.525  1.00 26.36  0  98  PHE   D CD2 1 
ATOM   6655 C  CE1 . PHE   D  1 83  ? 12.135  -4.001  20.173  1.00 23.24  0  98  PHE   D CE1 1 
ATOM   6656 C  CE2 . PHE   D  1 83  ? 9.948   -4.732  19.546  1.00 24.72  0  98  PHE   D CE2 1 
ATOM   6657 C  CZ  . PHE   D  1 83  ? 11.314  -4.752  19.362  1.00 23.99  0  98  PHE   D CZ  1 
ATOM   6658 N  N   . TYR   D  1 84  ? 9.966   -0.539  19.617  1.00 24.44  0  99  TYR   D N   1 
ATOM   6659 C  CA  . TYR   D  1 84  ? 9.602   -0.710  18.191  1.00 25.25  0  99  TYR   D CA  1 
ATOM   6660 C  C   . TYR   D  1 84  ? 10.658  -1.571  17.512  1.00 24.18  0  99  TYR   D C   1 
ATOM   6661 O  O   . TYR   D  1 84  ? 10.237  -2.523  16.846  1.00 24.02  0  99  TYR   D O   1 
ATOM   6662 C  CB  . TYR   D  1 84  ? 9.268   0.617   17.500  1.00 26.66  0  99  TYR   D CB  1 
ATOM   6663 C  CG  . TYR   D  1 84  ? 8.730   0.365   16.121  1.00 26.37  0  99  TYR   D CG  1 
ATOM   6664 C  CD1 . TYR   D  1 84  ? 7.532   -0.315  15.948  1.00 28.88  0  99  TYR   D CD1 1 
ATOM   6665 C  CD2 . TYR   D  1 84  ? 9.474   0.651   14.989  1.00 27.90  0  99  TYR   D CD2 1 
ATOM   6666 C  CE1 . TYR   D  1 84  ? 7.071   -0.657  14.692  1.00 24.94  0  99  TYR   D CE1 1 
ATOM   6667 C  CE2 . TYR   D  1 84  ? 9.036   0.289   13.722  1.00 29.34  0  99  TYR   D CE2 1 
ATOM   6668 C  CZ  . TYR   D  1 84  ? 7.826   -0.371  13.570  1.00 27.76  0  99  TYR   D CZ  1 
ATOM   6669 O  OH  . TYR   D  1 84  ? 7.375   -0.747  12.329  1.00 26.94  0  99  TYR   D OH  1 
ATOM   6670 N  N   . THR   D  1 85  ? 11.966  -1.287  17.673  1.00 26.13  0  100 THR   D N   1 
ATOM   6671 C  CA  . THR   D  1 85  ? 13.057  -2.158  17.155  1.00 25.00  0  100 THR   D CA  1 
ATOM   6672 C  C   . THR   D  1 85  ? 14.179  -2.308  18.193  1.00 26.16  0  100 THR   D C   1 
ATOM   6673 O  O   . THR   D  1 85  ? 14.291  -1.436  19.091  1.00 23.24  0  100 THR   D O   1 
ATOM   6674 C  CB  . THR   D  1 85  ? 13.677  -1.636  15.847  1.00 25.83  0  100 THR   D CB  1 
ATOM   6675 O  OG1 . THR   D  1 85  ? 14.520  -0.524  16.135  1.00 27.14  0  100 THR   D OG1 1 
ATOM   6676 C  CG2 . THR   D  1 85  ? 12.655  -1.267  14.799  1.00 26.08  0  100 THR   D CG2 1 
ATOM   6677 N  N   . ALA   D  1 86  ? 14.983  -3.370  18.076  1.00 23.15  0  101 ALA   D N   1 
ATOM   6678 C  CA  . ALA   D  1 86  ? 16.054  -3.679  19.047  1.00 23.40  0  101 ALA   D CA  1 
ATOM   6679 C  C   . ALA   D  1 86  ? 17.096  -2.568  19.046  1.00 23.06  0  101 ALA   D C   1 
ATOM   6680 O  O   . ALA   D  1 86  ? 17.594  -2.270  20.132  1.00 24.54  0  101 ALA   D O   1 
ATOM   6681 C  CB  . ALA   D  1 86  ? 16.708  -4.979  18.707  1.00 28.22  0  101 ALA   D CB  1 
ATOM   6682 N  N   . GLN   D  1 87  ? 17.428  -2.014  17.880  1.00 22.58  0  102 GLN   D N   1 
ATOM   6683 C  CA  . GLN   D  1 87  ? 18.492  -0.977  17.758  1.00 24.73  0  102 GLN   D CA  1 
ATOM   6684 C  C   . GLN   D  1 87  ? 18.020  0.350   18.354  1.00 26.45  0  102 GLN   D C   1 
ATOM   6685 O  O   . GLN   D  1 87  ? 18.895  1.106   18.834  1.00 29.58  0  102 GLN   D O   1 
ATOM   6686 C  CB  . GLN   D  1 87  ? 18.953  -0.754  16.327  1.00 24.23  0  102 GLN   D CB  1 
ATOM   6687 C  CG  . GLN   D  1 87  ? 19.433  -2.043  15.696  1.00 29.15  0  102 GLN   D CG  1 
ATOM   6688 C  CD  . GLN   D  1 87  ? 18.398  -2.662  14.797  1.00 31.24  0  102 GLN   D CD  1 
ATOM   6689 O  OE1 . GLN   D  1 87  ? 17.181  -2.493  14.929  1.00 28.27  0  102 GLN   D OE1 1 
ATOM   6690 N  NE2 . GLN   D  1 87  ? 18.895  -3.325  13.771  1.00 40.46  0  102 GLN   D NE2 1 
ATOM   6691 N  N   . ILE   D  1 88  ? 16.714  0.630   18.353  1.00 24.29  0  103 ILE   D N   1 
ATOM   6692 C  CA  . ILE   D  1 88  ? 16.170  1.828   19.047  1.00 26.92  0  103 ILE   D CA  1 
ATOM   6693 C  C   . ILE   D  1 88  ? 16.210  1.604   20.568  1.00 26.62  0  103 ILE   D C   1 
ATOM   6694 O  O   . ILE   D  1 88  ? 16.615  2.558   21.295  1.00 27.43  0  103 ILE   D O   1 
ATOM   6695 C  CB  . ILE   D  1 88  ? 14.782  2.225   18.524  1.00 25.87  0  103 ILE   D CB  1 
ATOM   6696 C  CG1 . ILE   D  1 88  ? 14.833  2.616   17.051  1.00 27.28  0  103 ILE   D CG1 1 
ATOM   6697 C  CG2 . ILE   D  1 88  ? 14.212  3.343   19.374  1.00 29.00  0  103 ILE   D CG2 1 
ATOM   6698 C  CD1 . ILE   D  1 88  ? 13.487  2.734   16.340  1.00 28.51  0  103 ILE   D CD1 1 
ATOM   6699 N  N   . GLY   D  1 89  ? 15.834  0.410   21.043  1.00 27.34  0  104 GLY   D N   1 
ATOM   6700 C  CA  . GLY   D  1 89  ? 15.949  0.007   22.469  1.00 26.58  0  104 GLY   D CA  1 
ATOM   6701 C  C   . GLY   D  1 89  ? 14.619  -0.409  23.094  1.00 26.18  0  104 GLY   D C   1 
ATOM   6702 O  O   . GLY   D  1 89  ? 13.629  -0.587  22.372  1.00 26.56  0  104 GLY   D O   1 
ATOM   6703 N  N   . ALA   D  1 90  ? 14.593  -0.508  24.422  1.00 28.61  0  105 ALA   D N   1 
ATOM   6704 C  CA  . ALA   D  1 90  ? 13.461  -1.022  25.230  1.00 23.52  0  105 ALA   D CA  1 
ATOM   6705 C  C   . ALA   D  1 90  ? 13.120  -2.432  24.740  1.00 21.40  0  105 ALA   D C   1 
ATOM   6706 O  O   . ALA   D  1 90  ? 11.926  -2.800  24.732  1.00 21.17  0  105 ALA   D O   1 
ATOM   6707 C  CB  . ALA   D  1 90  ? 12.282  -0.076  25.170  1.00 24.07  0  105 ALA   D CB  1 
ATOM   6708 N  N   . ASP   D  1 91  ? 14.140  -3.222  24.440  1.00 20.71  0  106 ASP   D N   1 
ATOM   6709 C  CA  . ASP   D  1 91  ? 13.974  -4.601  23.925  1.00 21.46  0  106 ASP   D CA  1 
ATOM   6710 C  C   . ASP   D  1 91  ? 13.741  -5.567  25.106  1.00 21.43  0  106 ASP   D C   1 
ATOM   6711 O  O   . ASP   D  1 91  ? 14.631  -6.356  25.457  1.00 22.70  0  106 ASP   D O   1 
ATOM   6712 C  CB  . ASP   D  1 91  ? 15.085  -4.971  22.954  1.00 22.09  0  106 ASP   D CB  1 
ATOM   6713 C  CG  . ASP   D  1 91  ? 14.769  -6.248  22.206  1.00 23.17  0  106 ASP   D CG  1 
ATOM   6714 O  OD1 . ASP   D  1 91  ? 13.584  -6.643  22.248  1.00 23.94  0  106 ASP   D OD1 1 
ATOM   6715 O  OD2 . ASP   D  1 91  ? 15.729  -6.864  21.629  1.00 22.06  -1 106 ASP   D OD2 1 
ATOM   6716 N  N   . ILE   D  1 92  ? 12.545  -5.518  25.681  1.00 20.82  0  107 ILE   D N   1 
ATOM   6717 C  CA  . ILE   D  1 92  ? 12.202  -6.241  26.939  1.00 22.87  0  107 ILE   D CA  1 
ATOM   6718 C  C   . ILE   D  1 92  ? 10.708  -6.467  26.983  1.00 23.62  0  107 ILE   D C   1 
ATOM   6719 O  O   . ILE   D  1 92  ? 9.951   -5.573  26.513  1.00 23.66  0  107 ILE   D O   1 
ATOM   6720 C  CB  . ILE   D  1 92  ? 12.741  -5.503  28.174  1.00 24.61  0  107 ILE   D CB  1 
ATOM   6721 C  CG1 . ILE   D  1 92  ? 12.791  -6.433  29.382  1.00 25.35  0  107 ILE   D CG1 1 
ATOM   6722 C  CG2 . ILE   D  1 92  ? 11.979  -4.213  28.457  1.00 26.10  0  107 ILE   D CG2 1 
ATOM   6723 C  CD1 . ILE   D  1 92  ? 13.605  -5.896  30.520  1.00 26.72  0  107 ILE   D CD1 1 
ATOM   6724 N  N   . ALA   D  1 93  ? 10.324  -7.666  27.431  1.00 22.96  0  108 ALA   D N   1 
ATOM   6725 C  CA  . ALA   D  1 93  ? 8.921   -8.122  27.522  1.00 23.30  0  108 ALA   D CA  1 
ATOM   6726 C  C   . ALA   D  1 93  ? 8.779   -9.164  28.644  1.00 21.41  0  108 ALA   D C   1 
ATOM   6727 O  O   . ALA   D  1 93  ? 9.778   -9.726  29.116  1.00 22.27  0  108 ALA   D O   1 
ATOM   6728 C  CB  . ALA   D  1 93  ? 8.463   -8.682  26.197  1.00 23.55  0  108 ALA   D CB  1 
ATOM   6729 N  N   . LEU   D  1 94  ? 7.540   -9.392  29.035  1.00 22.45  0  109 LEU   D N   1 
ATOM   6730 C  CA  . LEU   D  1 94  ? 7.106   -10.273 30.132  1.00 24.93  0  109 LEU   D CA  1 
ATOM   6731 C  C   . LEU   D  1 94  ? 6.021   -11.200 29.603  1.00 23.69  0  109 LEU   D C   1 
ATOM   6732 O  O   . LEU   D  1 94  ? 5.186   -10.751 28.804  1.00 21.15  0  109 LEU   D O   1 
ATOM   6733 C  CB  . LEU   D  1 94  ? 6.574   -9.412  31.273  1.00 27.63  0  109 LEU   D CB  1 
ATOM   6734 C  CG  . LEU   D  1 94  ? 7.625   -8.657  32.060  1.00 24.98  0  109 LEU   D CG  1 
ATOM   6735 C  CD1 . LEU   D  1 94  ? 6.941   -7.609  32.939  1.00 25.26  0  109 LEU   D CD1 1 
ATOM   6736 C  CD2 . LEU   D  1 94  ? 8.469   -9.603  32.886  1.00 25.98  0  109 LEU   D CD2 1 
ATOM   6737 N  N   . LEU   D  1 95  ? 6.156   -12.486 29.927  1.00 25.18  0  110 LEU   D N   1 
ATOM   6738 C  CA  . LEU   D  1 95  ? 5.102   -13.497 29.676  1.00 24.87  0  110 LEU   D CA  1 
ATOM   6739 C  C   . LEU   D  1 95  ? 4.532   -13.903 31.029  1.00 22.59  0  110 LEU   D C   1 
ATOM   6740 O  O   . LEU   D  1 95  ? 5.316   -14.332 31.881  1.00 23.67  0  110 LEU   D O   1 
ATOM   6741 C  CB  . LEU   D  1 95  ? 5.689   -14.688 28.926  1.00 25.27  0  110 LEU   D CB  1 
ATOM   6742 C  CG  . LEU   D  1 95  ? 6.564   -14.385 27.715  1.00 26.06  0  110 LEU   D CG  1 
ATOM   6743 C  CD1 . LEU   D  1 95  ? 7.054   -15.710 27.108  1.00 27.79  0  110 LEU   D CD1 1 
ATOM   6744 C  CD2 . LEU   D  1 95  ? 5.784   -13.581 26.683  1.00 26.27  0  110 LEU   D CD2 1 
ATOM   6745 N  N   . GLU   D  1 96  ? 3.230   -13.761 31.200  1.00 23.87  0  111 GLU   D N   1 
ATOM   6746 C  CA  . GLU   D  1 96  ? 2.497   -14.319 32.371  1.00 27.31  0  111 GLU   D CA  1 
ATOM   6747 C  C   . GLU   D  1 96  ? 1.986   -15.718 32.008  1.00 25.12  0  111 GLU   D C   1 
ATOM   6748 O  O   . GLU   D  1 96  ? 1.187   -15.852 31.061  1.00 26.59  0  111 GLU   D O   1 
ATOM   6749 C  CB  . GLU   D  1 96  ? 1.362   -13.429 32.882  1.00 28.00  0  111 GLU   D CB  1 
ATOM   6750 C  CG  . GLU   D  1 96  ? 0.909   -13.888 34.281  1.00 29.02  0  111 GLU   D CG  1 
ATOM   6751 C  CD  . GLU   D  1 96  ? -0.129  -13.039 34.993  1.00 35.02  0  111 GLU   D CD  1 
ATOM   6752 O  OE1 . GLU   D  1 96  ? -0.854  -12.278 34.329  1.00 34.19  0  111 GLU   D OE1 1 
ATOM   6753 O  OE2 . GLU   D  1 96  ? -0.193  -13.148 36.229  1.00 43.41  -1 111 GLU   D OE2 1 
ATOM   6754 N  N   . LEU   D  1 97  ? 2.379   -16.704 32.798  1.00 25.15  0  112 LEU   D N   1 
ATOM   6755 C  CA  . LEU   D  1 97  ? 1.874   -18.090 32.637  1.00 27.88  0  112 LEU   D CA  1 
ATOM   6756 C  C   . LEU   D  1 97  ? 0.454   -18.143 33.193  1.00 28.30  0  112 LEU   D C   1 
ATOM   6757 O  O   . LEU   D  1 97  ? 0.146   -17.355 34.058  1.00 28.00  0  112 LEU   D O   1 
ATOM   6758 C  CB  . LEU   D  1 97  ? 2.812   -19.060 33.349  1.00 26.02  0  112 LEU   D CB  1 
ATOM   6759 C  CG  . LEU   D  1 97  ? 4.263   -18.979 32.924  1.00 23.48  0  112 LEU   D CG  1 
ATOM   6760 C  CD1 . LEU   D  1 97  ? 5.106   -19.883 33.766  1.00 25.59  0  112 LEU   D CD1 1 
ATOM   6761 C  CD2 . LEU   D  1 97  ? 4.426   -19.282 31.447  1.00 28.02  0  112 LEU   D CD2 1 
ATOM   6762 N  N   . GLU   D  1 98  ? -0.364  -19.062 32.699  1.00 31.41  0  113 GLU   D N   1 
ATOM   6763 C  CA  . GLU   D  1 98  ? -1.775  -19.282 33.143  1.00 29.74  0  113 GLU   D CA  1 
ATOM   6764 C  C   . GLU   D  1 98  ? -1.787  -19.852 34.556  1.00 26.49  0  113 GLU   D C   1 
ATOM   6765 O  O   . GLU   D  1 98  ? -2.811  -19.679 35.242  1.00 28.04  0  113 GLU   D O   1 
ATOM   6766 C  CB  . GLU   D  1 98  ? -2.492  -20.252 32.212  1.00 27.74  0  113 GLU   D CB  1 
ATOM   6767 C  CG  . GLU   D  1 98  ? -2.787  -19.692 30.853  1.00 28.00  0  113 GLU   D CG  1 
ATOM   6768 C  CD  . GLU   D  1 98  ? -3.644  -20.624 30.011  1.00 31.77  0  113 GLU   D CD  1 
ATOM   6769 O  OE1 . GLU   D  1 98  ? -4.079  -21.683 30.538  1.00 28.76  0  113 GLU   D OE1 1 
ATOM   6770 O  OE2 . GLU   D  1 98  ? -3.861  -20.304 28.826  1.00 31.96  -1 113 GLU   D OE2 1 
ATOM   6771 N  N   . GLU   D  1 99  ? -0.693  -20.507 34.971  1.00 29.00  0  114 GLU   D N   1 
ATOM   6772 C  CA  . GLU   D  1 99  ? -0.550  -21.110 36.308  1.00 28.36  0  114 GLU   D CA  1 
ATOM   6773 C  C   . GLU   D  1 99  ? 0.865   -20.893 36.806  1.00 30.93  0  114 GLU   D C   1 
ATOM   6774 O  O   . GLU   D  1 99  ? 1.838   -20.916 36.027  1.00 27.37  0  114 GLU   D O   1 
ATOM   6775 C  CB  . GLU   D  1 99  ? -0.757  -22.639 36.310  1.00 32.76  0  114 GLU   D CB  1 
ATOM   6776 C  CG  . GLU   D  1 99  ? -2.062  -23.115 35.648  1.00 30.78  0  114 GLU   D CG  1 
ATOM   6777 C  CD  . GLU   D  1 99  ? -3.352  -22.742 36.351  1.00 27.61  0  114 GLU   D CD  1 
ATOM   6778 O  OE1 . GLU   D  1 99  ? -3.272  -22.394 37.564  1.00 26.72  0  114 GLU   D OE1 1 
ATOM   6779 O  OE2 . GLU   D  1 99  ? -4.445  -22.827 35.678  1.00 24.57  -1 114 GLU   D OE2 1 
ATOM   6780 N  N   . PRO   D  1 100 ? 1.019   -20.751 38.130  1.00 30.85  0  115 PRO   D N   1 
ATOM   6781 C  CA  . PRO   D  1 100 ? 2.336   -20.664 38.746  1.00 33.51  0  115 PRO   D CA  1 
ATOM   6782 C  C   . PRO   D  1 100 ? 3.007   -22.026 38.571  1.00 35.26  0  115 PRO   D C   1 
ATOM   6783 O  O   . PRO   D  1 100 ? 2.305   -23.021 38.527  1.00 41.34  0  115 PRO   D O   1 
ATOM   6784 C  CB  . PRO   D  1 100 ? 2.050   -20.307 40.212  1.00 33.47  0  115 PRO   D CB  1 
ATOM   6785 C  CG  . PRO   D  1 100 ? 0.670   -20.800 40.458  1.00 33.70  0  115 PRO   D CG  1 
ATOM   6786 C  CD  . PRO   D  1 100 ? -0.057  -20.702 39.127  1.00 35.50  0  115 PRO   D CD  1 
ATOM   6787 N  N   . VAL   D  1 101 ? 4.307   -22.038 38.331  1.00 32.14  0  116 VAL   D N   1 
ATOM   6788 C  CA  . VAL   D  1 101 ? 5.055   -23.322 38.214  1.00 31.68  0  116 VAL   D CA  1 
ATOM   6789 C  C   . VAL   D  1 101 ? 5.469   -23.725 39.631  1.00 27.63  0  116 VAL   D C   1 
ATOM   6790 O  O   . VAL   D  1 101 ? 5.634   -22.848 40.488  1.00 29.21  0  116 VAL   D O   1 
ATOM   6791 C  CB  . VAL   D  1 101 ? 6.259   -23.249 37.243  1.00 32.61  0  116 VAL   D CB  1 
ATOM   6792 C  CG1 . VAL   D  1 101 ? 5.883   -22.619 35.912  1.00 39.30  0  116 VAL   D CG1 1 
ATOM   6793 C  CG2 . VAL   D  1 101 ? 7.454   -22.531 37.814  1.00 33.95  0  116 VAL   D CG2 1 
ATOM   6794 N  N   . LYS   D  1 102 ? 5.790   -24.991 39.795  1.00 29.30  0  117 LYS   D N   1 
ATOM   6795 C  CA  . LYS   D  1 102 ? 6.372   -25.593 41.005  1.00 32.08  0  117 LYS   D CA  1 
ATOM   6796 C  C   . LYS   D  1 102 ? 7.885   -25.487 40.876  1.00 35.09  0  117 LYS   D C   1 
ATOM   6797 O  O   . LYS   D  1 102 ? 8.421   -26.060 39.923  1.00 37.13  0  117 LYS   D O   1 
ATOM   6798 C  CB  . LYS   D  1 102 ? 5.920   -27.056 41.100  1.00 36.48  0  117 LYS   D CB  1 
ATOM   6799 C  CG  . LYS   D  1 102 ? 4.632   -27.338 41.878  1.00 35.93  0  117 LYS   D CG  1 
ATOM   6800 C  CD  . LYS   D  1 102 ? 3.598   -26.234 41.972  1.00 40.03  0  117 LYS   D CD  1 
ATOM   6801 C  CE  . LYS   D  1 102 ? 2.246   -26.728 42.426  1.00 42.23  0  117 LYS   D CE  1 
ATOM   6802 N  NZ  . LYS   D  1 102 ? 1.479   -25.672 43.121  1.00 46.23  1  117 LYS   D NZ  1 
ATOM   6803 N  N   . VAL   D  1 103 ? 8.554   -24.846 41.821  1.00 29.62  0  118 VAL   D N   1 
ATOM   6804 C  CA  . VAL   D  1 103 ? 10.024  -24.648 41.711  1.00 30.16  0  118 VAL   D CA  1 
ATOM   6805 C  C   . VAL   D  1 103 ? 10.738  -25.755 42.474  1.00 34.01  0  118 VAL   D C   1 
ATOM   6806 O  O   . VAL   D  1 103 ? 10.118  -26.431 43.314  1.00 34.40  0  118 VAL   D O   1 
ATOM   6807 C  CB  . VAL   D  1 103 ? 10.483  -23.234 42.088  1.00 30.48  0  118 VAL   D CB  1 
ATOM   6808 C  CG1 . VAL   D  1 103 ? 9.995   -22.233 41.058  1.00 30.87  0  118 VAL   D CG1 1 
ATOM   6809 C  CG2 . VAL   D  1 103 ? 10.089  -22.804 43.485  1.00 32.42  0  118 VAL   D CG2 1 
ATOM   6810 N  N   . SER   D  1 104 ? 11.977  -26.008 42.081  1.00 28.48  0  119 SER   D N   1 
ATOM   6811 C  CA  . SER   D  1 104 ? 12.825  -27.110 42.585  1.00 35.33  0  119 SER   D CA  1 
ATOM   6812 C  C   . SER   D  1 104 ? 14.288  -26.700 42.400  1.00 36.82  0  119 SER   D C   1 
ATOM   6813 O  O   . SER   D  1 104 ? 14.523  -25.597 41.859  1.00 33.45  0  119 SER   D O   1 
ATOM   6814 C  CB  . SER   D  1 104 ? 12.499  -28.387 41.854  1.00 35.35  0  119 SER   D CB  1 
ATOM   6815 O  OG  . SER   D  1 104 ? 12.783  -28.281 40.472  1.00 36.47  0  119 SER   D OG  1 
ATOM   6816 N  N   . SER   D  1 105 ? 15.242  -27.538 42.782  1.00 38.31  0  120 SER   D N   1 
ATOM   6817 C  CA  . SER   D  1 105 ? 16.675  -27.223 42.541  1.00 44.87  0  120 SER   D CA  1 
ATOM   6818 C  C   . SER   D  1 105 ? 16.972  -27.265 41.027  1.00 39.79  0  120 SER   D C   1 
ATOM   6819 O  O   . SER   D  1 105 ? 17.838  -26.507 40.596  1.00 40.33  0  120 SER   D O   1 
ATOM   6820 C  CB  . SER   D  1 105 ? 17.599  -28.089 43.365  1.00 43.97  0  120 SER   D CB  1 
ATOM   6821 O  OG  . SER   D  1 105 ? 17.635  -29.391 42.834  1.00 50.68  0  120 SER   D OG  1 
ATOM   6822 N  N   . HIS   D  1 106 ? 16.229  -28.044 40.244  1.00 40.80  0  121 HIS   D N   1 
ATOM   6823 C  CA  . HIS   D  1 106 ? 16.442  -28.189 38.782  1.00 41.15  0  121 HIS   D CA  1 
ATOM   6824 C  C   . HIS   D  1 106 ? 15.747  -27.066 37.986  1.00 41.38  0  121 HIS   D C   1 
ATOM   6825 O  O   . HIS   D  1 106 ? 16.272  -26.716 36.931  1.00 41.90  0  121 HIS   D O   1 
ATOM   6826 C  CB  . HIS   D  1 106 ? 16.007  -29.579 38.318  1.00 52.64  0  121 HIS   D CB  1 
ATOM   6827 C  CG  . HIS   D  1 106 ? 16.451  -29.881 36.921  1.00 71.00  0  121 HIS   D CG  1 
ATOM   6828 N  ND1 . HIS   D  1 106 ? 17.776  -30.162 36.600  1.00 69.18  0  121 HIS   D ND1 1 
ATOM   6829 C  CD2 . HIS   D  1 106 ? 15.761  -29.913 35.750  1.00 77.13  0  121 HIS   D CD2 1 
ATOM   6830 C  CE1 . HIS   D  1 106 ? 17.871  -30.379 35.294  1.00 73.63  0  121 HIS   D CE1 1 
ATOM   6831 N  NE2 . HIS   D  1 106 ? 16.652  -30.223 34.753  1.00 76.07  0  121 HIS   D NE2 1 
ATOM   6832 N  N   . VAL   D  1 107 ? 14.620  -26.528 38.461  1.00 33.37  0  122 VAL   D N   1 
ATOM   6833 C  CA  . VAL   D  1 107 ? 13.838  -25.466 37.772  1.00 30.56  0  122 VAL   D CA  1 
ATOM   6834 C  C   . VAL   D  1 107 ? 13.451  -24.418 38.814  1.00 30.79  0  122 VAL   D C   1 
ATOM   6835 O  O   . VAL   D  1 107 ? 12.568  -24.691 39.632  1.00 26.52  0  122 VAL   D O   1 
ATOM   6836 C  CB  . VAL   D  1 107 ? 12.591  -26.054 37.083  1.00 36.30  0  122 VAL   D CB  1 
ATOM   6837 C  CG1 . VAL   D  1 107 ? 11.667  -24.983 36.527  1.00 40.59  0  122 VAL   D CG1 1 
ATOM   6838 C  CG2 . VAL   D  1 107 ? 12.945  -27.082 36.017  1.00 39.74  0  122 VAL   D CG2 1 
ATOM   6839 N  N   . HIS   D  1 108 ? 14.046  -23.231 38.753  1.00 28.60  0  123 HIS   D N   1 
ATOM   6840 C  CA  . HIS   D  1 108 ? 13.720  -22.126 39.686  1.00 26.95  0  123 HIS   D CA  1 
ATOM   6841 C  C   . HIS   D  1 108 ? 14.139  -20.783 39.078  1.00 27.41  0  123 HIS   D C   1 
ATOM   6842 O  O   . HIS   D  1 108 ? 14.670  -20.756 37.939  1.00 25.39  0  123 HIS   D O   1 
ATOM   6843 C  CB  . HIS   D  1 108 ? 14.303  -22.407 41.081  1.00 30.67  0  123 HIS   D CB  1 
ATOM   6844 C  CG  . HIS   D  1 108 ? 15.789  -22.348 41.205  1.00 28.42  0  123 HIS   D CG  1 
ATOM   6845 N  ND1 . HIS   D  1 108 ? 16.551  -23.467 41.498  1.00 32.74  0  123 HIS   D ND1 1 
ATOM   6846 C  CD2 . HIS   D  1 108 ? 16.647  -21.306 41.206  1.00 27.94  0  123 HIS   D CD2 1 
ATOM   6847 C  CE1 . HIS   D  1 108 ? 17.824  -23.118 41.659  1.00 31.87  0  123 HIS   D CE1 1 
ATOM   6848 N  NE2 . HIS   D  1 108 ? 17.912  -21.795 41.486  1.00 32.18  0  123 HIS   D NE2 1 
ATOM   6849 N  N   . THR   D  1 109 ? 13.784  -19.712 39.770  1.00 25.71  0  124 THR   D N   1 
ATOM   6850 C  CA  . THR   D  1 109 ? 13.813  -18.331 39.247  1.00 27.56  0  124 THR   D CA  1 
ATOM   6851 C  C   . THR   D  1 109 ? 15.239  -17.804 39.330  1.00 28.52  0  124 THR   D C   1 
ATOM   6852 O  O   . THR   D  1 109 ? 16.043  -18.345 40.108  1.00 27.04  0  124 THR   D O   1 
ATOM   6853 C  CB  . THR   D  1 109 ? 12.893  -17.372 39.999  1.00 25.15  0  124 THR   D CB  1 
ATOM   6854 O  OG1 . THR   D  1 109 ? 13.386  -17.367 41.332  1.00 28.92  0  124 THR   D OG1 1 
ATOM   6855 C  CG2 . THR   D  1 109 ? 11.434  -17.736 39.985  1.00 29.77  0  124 THR   D CG2 1 
ATOM   6856 N  N   . VAL   D  1 110 ? 15.529  -16.798 38.511  1.00 30.13  0  125 VAL   D N   1 
ATOM   6857 C  CA  . VAL   D  1 110 ? 16.814  -16.061 38.543  1.00 27.91  0  125 VAL   D CA  1 
ATOM   6858 C  C   . VAL   D  1 110 ? 16.541  -14.777 39.334  1.00 28.43  0  125 VAL   D C   1 
ATOM   6859 O  O   . VAL   D  1 110 ? 15.406  -14.263 39.282  1.00 26.00  0  125 VAL   D O   1 
ATOM   6860 C  CB  . VAL   D  1 110 ? 17.351  -15.799 37.113  1.00 25.71  0  125 VAL   D CB  1 
ATOM   6861 C  CG1 . VAL   D  1 110 ? 16.479  -14.814 36.336  1.00 25.26  0  125 VAL   D CG1 1 
ATOM   6862 C  CG2 . VAL   D  1 110 ? 18.798  -15.329 37.141  1.00 24.61  0  125 VAL   D CG2 1 
ATOM   6863 N  N   . THR   D  1 111 ? 17.562  -14.280 40.023  1.00 26.51  0  126 THR   D N   1 
ATOM   6864 C  CA  . THR   D  1 111 ? 17.522  -13.036 40.832  1.00 27.44  0  126 THR   D CA  1 
ATOM   6865 C  C   . THR   D  1 111 ? 17.813  -11.858 39.897  1.00 28.58  0  126 THR   D C   1 
ATOM   6866 O  O   . THR   D  1 111 ? 18.847  -11.894 39.152  1.00 29.42  0  126 THR   D O   1 
ATOM   6867 C  CB  . THR   D  1 111 ? 18.559  -13.115 41.961  1.00 30.59  0  126 THR   D CB  1 
ATOM   6868 O  OG1 . THR   D  1 111 ? 18.344  -14.338 42.654  1.00 31.09  0  126 THR   D OG1 1 
ATOM   6869 C  CG2 . THR   D  1 111 ? 18.532  -11.950 42.923  1.00 30.94  0  126 THR   D CG2 1 
ATOM   6870 N  N   . LEU   D  1 112 ? 16.958  -10.847 39.948  1.00 29.18  0  127 LEU   D N   1 
ATOM   6871 C  CA  . LEU   D  1 112 ? 17.174  -9.561  39.254  1.00 30.75  0  127 LEU   D CA  1 
ATOM   6872 C  C   . LEU   D  1 112 ? 18.220  -8.744  39.994  1.00 29.69  0  127 LEU   D C   1 
ATOM   6873 O  O   . LEU   D  1 112 ? 18.314  -8.802  41.214  1.00 28.22  0  127 LEU   D O   1 
ATOM   6874 C  CB  . LEU   D  1 112 ? 15.842  -8.826  39.130  1.00 28.61  0  127 LEU   D CB  1 
ATOM   6875 C  CG  . LEU   D  1 112 ? 14.806  -9.554  38.277  1.00 31.74  0  127 LEU   D CG  1 
ATOM   6876 C  CD1 . LEU   D  1 112 ? 13.532  -8.740  38.133  1.00 35.09  0  127 LEU   D CD1 1 
ATOM   6877 C  CD2 . LEU   D  1 112 ? 15.360  -9.879  36.906  1.00 36.24  0  127 LEU   D CD2 1 
ATOM   6878 N  N   . PRO   D  1 113 ? 19.040  -7.956  39.271  1.00 32.20  0  128 PRO   D N   1 
ATOM   6879 C  CA  . PRO   D  1 113 ? 20.082  -7.172  39.925  1.00 31.83  0  128 PRO   D CA  1 
ATOM   6880 C  C   . PRO   D  1 113 ? 19.465  -5.980  40.658  1.00 30.87  0  128 PRO   D C   1 
ATOM   6881 O  O   . PRO   D  1 113 ? 18.392  -5.515  40.284  1.00 27.08  0  128 PRO   D O   1 
ATOM   6882 C  CB  . PRO   D  1 113 ? 20.962  -6.720  38.762  1.00 32.12  0  128 PRO   D CB  1 
ATOM   6883 C  CG  . PRO   D  1 113 ? 20.012  -6.655  37.567  1.00 35.79  0  128 PRO   D CG  1 
ATOM   6884 C  CD  . PRO   D  1 113 ? 18.975  -7.739  37.816  1.00 34.09  0  128 PRO   D CD  1 
ATOM   6885 N  N   . PRO   D  1 114 ? 20.128  -5.446  41.705  1.00 33.55  0  129 PRO   D N   1 
ATOM   6886 C  CA  . PRO   D  1 114 ? 19.719  -4.170  42.282  1.00 35.30  0  129 PRO   D CA  1 
ATOM   6887 C  C   . PRO   D  1 114 ? 20.036  -3.039  41.296  1.00 35.84  0  129 PRO   D C   1 
ATOM   6888 O  O   . PRO   D  1 114 ? 20.996  -3.186  40.513  1.00 33.11  0  129 PRO   D O   1 
ATOM   6889 C  CB  . PRO   D  1 114 ? 20.569  -4.092  43.565  1.00 37.56  0  129 PRO   D CB  1 
ATOM   6890 C  CG  . PRO   D  1 114 ? 21.806  -4.870  43.229  1.00 39.14  0  129 PRO   D CG  1 
ATOM   6891 C  CD  . PRO   D  1 114 ? 21.317  -6.008  42.361  1.00 35.73  0  129 PRO   D CD  1 
ATOM   6892 N  N   . ALA   D  1 115 ? 19.296  -1.928  41.399  1.00 39.11  0  130 ALA   D N   1 
ATOM   6893 C  CA  . ALA   D  1 115 ? 19.377  -0.753  40.496  1.00 42.26  0  130 ALA   D CA  1 
ATOM   6894 C  C   . ALA   D  1 115 ? 20.826  -0.249  40.351  1.00 42.60  0  130 ALA   D C   1 
ATOM   6895 O  O   . ALA   D  1 115 ? 21.206  0.160   39.244  1.00 40.17  0  130 ALA   D O   1 
ATOM   6896 C  CB  . ALA   D  1 115 ? 18.460  0.329   40.999  1.00 44.21  0  130 ALA   D CB  1 
ATOM   6897 N  N   . SER   D  1 116 ? 21.633  -0.330  41.402  1.00 42.29  0  131 SER   D N   1 
ATOM   6898 C  CA  . SER   D  1 116 ? 23.002  0.265   41.428  1.00 42.01  0  131 SER   D CA  1 
ATOM   6899 C  C   . SER   D  1 116 ? 24.028  -0.598  40.684  1.00 37.92  0  131 SER   D C   1 
ATOM   6900 O  O   . SER   D  1 116 ? 25.118  -0.073  40.425  1.00 37.91  0  131 SER   D O   1 
ATOM   6901 C  CB  . SER   D  1 116 ? 23.431  0.527   42.852  1.00 38.70  0  131 SER   D CB  1 
ATOM   6902 O  OG  . SER   D  1 116 ? 23.381  -0.667  43.603  1.00 41.54  0  131 SER   D OG  1 
ATOM   6903 N  N   . GLU   D  1 117 ? 23.749  -1.873  40.379  1.00 34.44  0  132 GLU   D N   1 
ATOM   6904 C  CA  . GLU   D  1 117 ? 24.818  -2.752  39.810  1.00 38.29  0  132 GLU   D CA  1 
ATOM   6905 C  C   . GLU   D  1 117 ? 25.079  -2.346  38.347  1.00 39.22  0  132 GLU   D C   1 
ATOM   6906 O  O   . GLU   D  1 117 ? 24.107  -2.372  37.554  1.00 38.81  0  132 GLU   D O   1 
ATOM   6907 C  CB  . GLU   D  1 117 ? 24.434  -4.229  39.936  1.00 39.02  0  132 GLU   D CB  1 
ATOM   6908 C  CG  . GLU   D  1 117 ? 25.439  -5.187  39.339  1.00 42.51  0  132 GLU   D CG  1 
ATOM   6909 C  CD  . GLU   D  1 117 ? 26.841  -5.111  39.931  1.00 48.22  0  132 GLU   D CD  1 
ATOM   6910 O  OE1 . GLU   D  1 117 ? 27.795  -4.798  39.168  1.00 49.35  0  132 GLU   D OE1 1 
ATOM   6911 O  OE2 . GLU   D  1 117 ? 26.961  -5.342  41.159  1.00 46.89  -1 132 GLU   D OE2 1 
ATOM   6912 N  N   . THR   D  1 118 ? 26.327  -2.015  37.981  1.00 35.68  0  133 THR   D N   1 
ATOM   6913 C  CA  . THR   D  1 118 ? 26.715  -1.527  36.627  1.00 37.70  0  133 THR   D CA  1 
ATOM   6914 C  C   . THR   D  1 118 ? 27.259  -2.648  35.728  1.00 38.00  0  133 THR   D C   1 
ATOM   6915 O  O   . THR   D  1 118 ? 27.316  -2.423  34.483  1.00 39.13  0  133 THR   D O   1 
ATOM   6916 C  CB  . THR   D  1 118 ? 27.774  -0.414  36.673  1.00 41.66  0  133 THR   D CB  1 
ATOM   6917 O  OG1 . THR   D  1 118 ? 28.932  -0.934  37.327  1.00 43.24  0  133 THR   D OG1 1 
ATOM   6918 C  CG2 . THR   D  1 118 ? 27.270  0.830   37.371  1.00 39.95  0  133 THR   D CG2 1 
ATOM   6919 N  N   . PHE   D  1 119 ? 27.697  -3.761  36.318  1.00 36.70  0  134 PHE   D N   1 
ATOM   6920 C  CA  . PHE   D  1 119 ? 28.358  -4.907  35.648  1.00 36.51  0  134 PHE   D CA  1 
ATOM   6921 C  C   . PHE   D  1 119 ? 29.572  -4.436  34.851  1.00 38.53  0  134 PHE   D C   1 
ATOM   6922 O  O   . PHE   D  1 119 ? 29.566  -4.467  33.620  1.00 33.99  0  134 PHE   D O   1 
ATOM   6923 C  CB  . PHE   D  1 119 ? 27.344  -5.678  34.797  1.00 34.53  0  134 PHE   D CB  1 
ATOM   6924 C  CG  . PHE   D  1 119 ? 26.229  -6.281  35.597  1.00 31.95  0  134 PHE   D CG  1 
ATOM   6925 C  CD1 . PHE   D  1 119 ? 26.422  -7.447  36.330  1.00 30.41  0  134 PHE   D CD1 1 
ATOM   6926 C  CD2 . PHE   D  1 119 ? 24.996  -5.680  35.614  1.00 29.00  0  134 PHE   D CD2 1 
ATOM   6927 C  CE1 . PHE   D  1 119 ? 25.382  -7.993  37.066  1.00 31.93  0  134 PHE   D CE1 1 
ATOM   6928 C  CE2 . PHE   D  1 119 ? 23.951  -6.251  36.320  1.00 32.15  0  134 PHE   D CE2 1 
ATOM   6929 C  CZ  . PHE   D  1 119 ? 24.147  -7.398  37.053  1.00 29.22  0  134 PHE   D CZ  1 
ATOM   6930 N  N   . PRO   D  1 120 ? 30.665  -4.007  35.522  1.00 40.70  0  135 PRO   D N   1 
ATOM   6931 C  CA  . PRO   D  1 120 ? 31.827  -3.498  34.796  1.00 40.27  0  135 PRO   D CA  1 
ATOM   6932 C  C   . PRO   D  1 120 ? 32.625  -4.625  34.159  1.00 38.80  0  135 PRO   D C   1 
ATOM   6933 O  O   . PRO   D  1 120 ? 32.471  -5.792  34.512  1.00 40.41  0  135 PRO   D O   1 
ATOM   6934 C  CB  . PRO   D  1 120 ? 32.646  -2.805  35.889  1.00 39.21  0  135 PRO   D CB  1 
ATOM   6935 C  CG  . PRO   D  1 120 ? 32.311  -3.617  37.142  1.00 42.67  0  135 PRO   D CG  1 
ATOM   6936 C  CD  . PRO   D  1 120 ? 30.850  -3.981  36.989  1.00 39.57  0  135 PRO   D CD  1 
ATOM   6937 N  N   . PRO   D  1 121 ? 33.529  -4.305  33.221  1.00 37.12  0  136 PRO   D N   1 
ATOM   6938 C  CA  . PRO   D  1 121 ? 34.483  -5.277  32.701  1.00 38.28  0  136 PRO   D CA  1 
ATOM   6939 C  C   . PRO   D  1 121 ? 35.219  -6.058  33.792  1.00 43.07  0  136 PRO   D C   1 
ATOM   6940 O  O   . PRO   D  1 121 ? 35.542  -5.489  34.814  1.00 41.18  0  136 PRO   D O   1 
ATOM   6941 C  CB  . PRO   D  1 121 ? 35.462  -4.397  31.910  1.00 40.21  0  136 PRO   D CB  1 
ATOM   6942 C  CG  . PRO   D  1 121 ? 34.576  -3.273  31.420  1.00 41.25  0  136 PRO   D CG  1 
ATOM   6943 C  CD  . PRO   D  1 121 ? 33.668  -2.982  32.597  1.00 42.40  0  136 PRO   D CD  1 
ATOM   6944 N  N   . GLY   D  1 122 ? 35.465  -7.343  33.523  1.00 42.48  0  137 GLY   D N   1 
ATOM   6945 C  CA  . GLY   D  1 122 ? 36.116  -8.282  34.443  1.00 42.32  0  137 GLY   D CA  1 
ATOM   6946 C  C   . GLY   D  1 122 ? 35.107  -9.046  35.264  1.00 43.73  0  137 GLY   D C   1 
ATOM   6947 O  O   . GLY   D  1 122 ? 35.505  -10.030 35.873  1.00 50.48  0  137 GLY   D O   1 
ATOM   6948 N  N   . MET   D  1 123 ? 33.839  -8.640  35.273  1.00 45.74  0  138 MET   D N   1 
ATOM   6949 C  CA  . MET   D  1 123 ? 32.761  -9.461  35.887  1.00 53.60  0  138 MET   D CA  1 
ATOM   6950 C  C   . MET   D  1 123 ? 32.704  -10.793 35.128  1.00 50.86  0  138 MET   D C   1 
ATOM   6951 O  O   . MET   D  1 123 ? 32.727  -10.800 33.898  1.00 45.75  0  138 MET   D O   1 
ATOM   6952 C  CB  . MET   D  1 123 ? 31.418  -8.727  35.821  1.00 60.47  0  138 MET   D CB  1 
ATOM   6953 C  CG  . MET   D  1 123 ? 30.467  -9.076  36.949  1.00 68.01  0  138 MET   D CG  1 
ATOM   6954 S  SD  . MET   D  1 123 ? 31.001  -8.420  38.539  1.00 75.84  0  138 MET   D SD  1 
ATOM   6955 C  CE  . MET   D  1 123 ? 29.825  -7.094  38.781  1.00 78.45  0  138 MET   D CE  1 
ATOM   6956 N  N   . PRO   D  1 124 ? 32.660  -11.963 35.817  1.00 48.12  0  139 PRO   D N   1 
ATOM   6957 C  CA  . PRO   D  1 124 ? 32.419  -13.250 35.153  1.00 43.18  0  139 PRO   D CA  1 
ATOM   6958 C  C   . PRO   D  1 124 ? 30.936  -13.377 34.766  1.00 37.68  0  139 PRO   D C   1 
ATOM   6959 O  O   . PRO   D  1 124 ? 30.105  -13.372 35.656  1.00 32.54  0  139 PRO   D O   1 
ATOM   6960 C  CB  . PRO   D  1 124 ? 32.855  -14.284 36.209  1.00 46.44  0  139 PRO   D CB  1 
ATOM   6961 C  CG  . PRO   D  1 124 ? 32.595  -13.598 37.535  1.00 45.96  0  139 PRO   D CG  1 
ATOM   6962 C  CD  . PRO   D  1 124 ? 32.863  -12.127 37.271  1.00 48.45  0  139 PRO   D CD  1 
ATOM   6963 N  N   . CYS   D  1 125 ? 30.630  -13.409 33.457  1.00 35.40  0  140 CYS   D N   1 
ATOM   6964 C  CA  . CYS   D  1 125 ? 29.235  -13.499 32.942  1.00 33.62  0  140 CYS   D CA  1 
ATOM   6965 C  C   . CYS   D  1 125 ? 29.128  -14.611 31.910  1.00 32.28  0  140 CYS   D C   1 
ATOM   6966 O  O   . CYS   D  1 125 ? 30.084  -14.819 31.132  1.00 30.96  0  140 CYS   D O   1 
ATOM   6967 C  CB  . CYS   D  1 125 ? 28.719  -12.190 32.358  1.00 33.79  0  140 CYS   D CB  1 
ATOM   6968 S  SG  . CYS   D  1 125 ? 28.991  -10.794 33.483  1.00 42.98  0  140 CYS   D SG  1 
ATOM   6969 N  N   . TRP   D  1 126 ? 27.962  -15.242 31.894  1.00 29.10  0  141 TRP   D N   1 
ATOM   6970 C  CA  A TRP   D  1 126 ? 27.626  -16.394 31.016  0.50 28.70  0  141 TRP   D CA  1 
ATOM   6971 C  CA  B TRP   D  1 126 ? 27.643  -16.385 30.993  0.50 27.58  0  141 TRP   D CA  1 
ATOM   6972 C  C   . TRP   D  1 126 ? 26.336  -16.069 30.255  1.00 26.09  0  141 TRP   D C   1 
ATOM   6973 O  O   . TRP   D  1 126 ? 25.467  -15.451 30.843  1.00 25.54  0  141 TRP   D O   1 
ATOM   6974 C  CB  A TRP   D  1 126 ? 27.458  -17.682 31.824  0.50 28.84  0  141 TRP   D CB  1 
ATOM   6975 C  CB  B TRP   D  1 126 ? 27.553  -17.710 31.759  0.50 26.19  0  141 TRP   D CB  1 
ATOM   6976 C  CG  A TRP   D  1 126 ? 28.685  -18.081 32.579  0.50 32.18  0  141 TRP   D CG  1 
ATOM   6977 C  CG  B TRP   D  1 126 ? 28.863  -18.409 31.964  0.50 27.80  0  141 TRP   D CG  1 
ATOM   6978 C  CD1 A TRP   D  1 126 ? 29.198  -17.480 33.691  0.50 33.27  0  141 TRP   D CD1 1 
ATOM   6979 C  CD1 B TRP   D  1 126 ? 29.389  -19.399 31.185  0.50 27.74  0  141 TRP   D CD1 1 
ATOM   6980 C  CD2 A TRP   D  1 126 ? 29.595  -19.140 32.248  0.50 34.31  0  141 TRP   D CD2 1 
ATOM   6981 C  CD2 B TRP   D  1 126 ? 29.818  -18.189 33.027  0.50 28.56  0  141 TRP   D CD2 1 
ATOM   6982 N  NE1 A TRP   D  1 126 ? 30.361  -18.088 34.074  0.50 34.35  0  141 TRP   D NE1 1 
ATOM   6983 N  NE1 B TRP   D  1 126 ? 30.610  -19.786 31.671  0.50 29.16  0  141 TRP   D NE1 1 
ATOM   6984 C  CE2 A TRP   D  1 126 ? 30.634  -19.105 33.205  0.50 34.91  0  141 TRP   D CE2 1 
ATOM   6985 C  CE2 B TRP   D  1 126 ? 30.901  -19.062 32.802  0.50 28.65  0  141 TRP   D CE2 1 
ATOM   6986 C  CE3 A TRP   D  1 126 ? 29.640  -20.104 31.238  0.50 34.94  0  141 TRP   D CE3 1 
ATOM   6987 C  CE3 B TRP   D  1 126 ? 29.882  -17.327 34.127  0.50 30.79  0  141 TRP   D CE3 1 
ATOM   6988 C  CZ2 A TRP   D  1 126 ? 31.692  -20.011 33.192  0.50 36.74  0  141 TRP   D CZ2 1 
ATOM   6989 C  CZ2 B TRP   D  1 126 ? 32.014  -19.111 33.648  0.50 29.07  0  141 TRP   D CZ2 1 
ATOM   6990 C  CZ3 A TRP   D  1 126 ? 30.685  -21.000 31.228  0.50 37.44  0  141 TRP   D CZ3 1 
ATOM   6991 C  CZ3 B TRP   D  1 126 ? 30.971  -17.385 34.973  0.50 30.99  0  141 TRP   D CZ3 1 
ATOM   6992 C  CH2 A TRP   D  1 126 ? 31.699  -20.949 32.187  0.50 37.37  0  141 TRP   D CH2 1 
ATOM   6993 C  CH2 B TRP   D  1 126 ? 32.026  -18.269 34.739  0.50 30.11  0  141 TRP   D CH2 1 
ATOM   6994 N  N   . VAL   D  1 127 ? 26.243  -16.493 29.008  1.00 26.88  0  142 VAL   D N   1 
ATOM   6995 C  CA  . VAL   D  1 127 ? 24.989  -16.402 28.209  1.00 26.26  0  142 VAL   D CA  1 
ATOM   6996 C  C   . VAL   D  1 127 ? 24.683  -17.829 27.745  1.00 24.80  0  142 VAL   D C   1 
ATOM   6997 O  O   . VAL   D  1 127 ? 25.625  -18.605 27.487  1.00 25.59  0  142 VAL   D O   1 
ATOM   6998 C  CB  . VAL   D  1 127 ? 25.109  -15.387 27.069  1.00 26.08  0  142 VAL   D CB  1 
ATOM   6999 C  CG1 . VAL   D  1 127 ? 26.238  -15.736 26.116  1.00 29.40  0  142 VAL   D CG1 1 
ATOM   7000 C  CG2 . VAL   D  1 127 ? 23.795  -15.224 26.339  1.00 27.99  0  142 VAL   D CG2 1 
ATOM   7001 N  N   . THR   D  1 128 ? 23.412  -18.177 27.740  1.00 25.05  0  143 THR   D N   1 
ATOM   7002 C  CA  . THR   D  1 128 ? 22.937  -19.565 27.525  1.00 25.97  0  143 THR   D CA  1 
ATOM   7003 C  C   . THR   D  1 128 ? 21.830  -19.553 26.473  1.00 23.71  0  143 THR   D C   1 
ATOM   7004 O  O   . THR   D  1 128 ? 21.078  -18.566 26.387  1.00 22.59  0  143 THR   D O   1 
ATOM   7005 C  CB  . THR   D  1 128 ? 22.500  -20.193 28.862  1.00 24.11  0  143 THR   D CB  1 
ATOM   7006 O  OG1 . THR   D  1 128 ? 21.500  -19.386 29.483  1.00 26.16  0  143 THR   D OG1 1 
ATOM   7007 C  CG2 . THR   D  1 128 ? 23.657  -20.364 29.811  1.00 23.51  0  143 THR   D CG2 1 
ATOM   7008 N  N   . GLY   D  1 129 ? 21.717  -20.655 25.738  1.00 24.06  0  144 GLY   D N   1 
ATOM   7009 C  CA  . GLY   D  1 129 ? 20.583  -20.867 24.839  1.00 24.62  0  144 GLY   D CA  1 
ATOM   7010 C  C   . GLY   D  1 129 ? 20.823  -21.981 23.855  1.00 23.15  0  144 GLY   D C   1 
ATOM   7011 O  O   . GLY   D  1 129 ? 21.890  -22.618 23.898  1.00 24.35  0  144 GLY   D O   1 
ATOM   7012 N  N   . TRP   D  1 130 ? 19.813  -22.191 23.028  1.00 24.26  0  145 TRP   D N   1 
ATOM   7013 C  CA  . TRP   D  1 130 ? 19.694  -23.227 21.973  1.00 24.65  0  145 TRP   D CA  1 
ATOM   7014 C  C   . TRP   D  1 130 ? 19.783  -22.585 20.581  1.00 27.53  0  145 TRP   D C   1 
ATOM   7015 O  O   . TRP   D  1 130 ? 19.247  -23.180 19.591  1.00 28.06  0  145 TRP   D O   1 
ATOM   7016 C  CB  . TRP   D  1 130 ? 18.343  -23.937 22.121  1.00 26.16  0  145 TRP   D CB  1 
ATOM   7017 C  CG  . TRP   D  1 130 ? 18.184  -24.734 23.379  1.00 25.31  0  145 TRP   D CG  1 
ATOM   7018 C  CD1 . TRP   D  1 130 ? 18.645  -25.990 23.632  1.00 26.24  0  145 TRP   D CD1 1 
ATOM   7019 C  CD2 . TRP   D  1 130 ? 17.460  -24.330 24.548  1.00 26.85  0  145 TRP   D CD2 1 
ATOM   7020 N  NE1 . TRP   D  1 130 ? 18.257  -26.386 24.876  1.00 27.99  0  145 TRP   D NE1 1 
ATOM   7021 C  CE2 . TRP   D  1 130 ? 17.527  -25.397 25.458  1.00 28.15  0  145 TRP   D CE2 1 
ATOM   7022 C  CE3 . TRP   D  1 130 ? 16.759  -23.178 24.906  1.00 26.70  0  145 TRP   D CE3 1 
ATOM   7023 C  CZ2 . TRP   D  1 130 ? 16.937  -25.331 26.716  1.00 30.16  0  145 TRP   D CZ2 1 
ATOM   7024 C  CZ3 . TRP   D  1 130 ? 16.139  -23.133 26.127  1.00 29.93  0  145 TRP   D CZ3 1 
ATOM   7025 C  CH2 . TRP   D  1 130 ? 16.217  -24.203 27.017  1.00 30.30  0  145 TRP   D CH2 1 
ATOM   7026 N  N   . GLY   D  1 131 ? 20.438  -21.426 20.475  1.00 26.72  0  146 GLY   D N   1 
ATOM   7027 C  CA  . GLY   D  1 131 ? 20.595  -20.729 19.190  1.00 25.75  0  146 GLY   D CA  1 
ATOM   7028 C  C   . GLY   D  1 131 ? 21.732  -21.293 18.351  1.00 25.68  0  146 GLY   D C   1 
ATOM   7029 O  O   . GLY   D  1 131 ? 22.465  -22.210 18.798  1.00 25.82  0  146 GLY   D O   1 
ATOM   7030 N  N   . ASP   D  1 132 ? 21.883  -20.730 17.164  1.00 26.64  0  147 ASP   D N   1 
ATOM   7031 C  CA  . ASP   D  1 132 ? 22.934  -21.058 16.165  1.00 27.33  0  147 ASP   D CA  1 
ATOM   7032 C  C   . ASP   D  1 132 ? 24.321  -21.045 16.825  1.00 25.56  0  147 ASP   D C   1 
ATOM   7033 O  O   . ASP   D  1 132 ? 24.612  -20.208 17.724  1.00 22.34  0  147 ASP   D O   1 
ATOM   7034 C  CB  . ASP   D  1 132 ? 22.850  -20.084 14.980  1.00 29.63  0  147 ASP   D CB  1 
ATOM   7035 C  CG  . ASP   D  1 132 ? 21.613  -20.203 14.110  1.00 30.74  0  147 ASP   D CG  1 
ATOM   7036 O  OD1 . ASP   D  1 132 ? 20.760  -21.106 14.363  1.00 29.93  0  147 ASP   D OD1 1 
ATOM   7037 O  OD2 . ASP   D  1 132 ? 21.526  -19.433 13.127  1.00 35.54  -1 147 ASP   D OD2 1 
ATOM   7038 N  N   . VAL   D  1 133 ? 25.180  -21.956 16.385  1.00 24.90  0  148 VAL   D N   1 
ATOM   7039 C  CA  . VAL   D  1 133 ? 26.573  -22.126 16.879  1.00 26.00  0  148 VAL   D CA  1 
ATOM   7040 C  C   . VAL   D  1 133 ? 27.544  -21.272 16.065  1.00 28.42  0  148 VAL   D C   1 
ATOM   7041 O  O   . VAL   D  1 133 ? 28.737  -21.215 16.446  1.00 31.24  0  148 VAL   D O   1 
ATOM   7042 C  CB  . VAL   D  1 133 ? 26.992  -23.611 16.915  1.00 28.51  0  148 VAL   D CB  1 
ATOM   7043 C  CG1 . VAL   D  1 133 ? 26.062  -24.410 17.819  1.00 29.66  0  148 VAL   D CG1 1 
ATOM   7044 C  CG2 . VAL   D  1 133 ? 27.048  -24.246 15.539  1.00 30.99  0  148 VAL   D CG2 1 
ATOM   7045 N  N   . ASP   D  1 134 ? 27.060  -20.617 15.010  1.00 32.50  0  149 ASP   D N   1 
ATOM   7046 C  CA  . ASP   D  1 134 ? 27.822  -19.601 14.231  1.00 33.58  0  149 ASP   D CA  1 
ATOM   7047 C  C   . ASP   D  1 134 ? 26.841  -18.921 13.271  1.00 31.81  0  149 ASP   D C   1 
ATOM   7048 O  O   . ASP   D  1 134 ? 25.693  -19.401 13.188  1.00 30.55  0  149 ASP   D O   1 
ATOM   7049 C  CB  . ASP   D  1 134 ? 29.019  -20.223 13.484  1.00 36.76  0  149 ASP   D CB  1 
ATOM   7050 C  CG  . ASP   D  1 134 ? 30.179  -19.243 13.291  1.00 39.23  0  149 ASP   D CG  1 
ATOM   7051 O  OD1 . ASP   D  1 134 ? 29.946  -18.045 13.176  1.00 40.06  0  149 ASP   D OD1 1 
ATOM   7052 O  OD2 . ASP   D  1 134 ? 31.299  -19.670 13.304  1.00 42.10  -1 149 ASP   D OD2 1 
ATOM   7053 N  N   . ASN   D  1 135 ? 27.265  -17.878 12.552  1.00 33.16  0  150 ASN   D N   1 
ATOM   7054 C  CA  . ASN   D  1 135 ? 26.411  -17.204 11.523  1.00 32.86  0  150 ASN   D CA  1 
ATOM   7055 C  C   . ASN   D  1 135 ? 25.842  -18.279 10.566  1.00 33.04  0  150 ASN   D C   1 
ATOM   7056 O  O   . ASN   D  1 135 ? 26.647  -19.054 9.983   1.00 32.31  0  150 ASN   D O   1 
ATOM   7057 C  CB  . ASN   D  1 135 ? 27.177  -16.120 10.762  1.00 31.12  0  150 ASN   D CB  1 
ATOM   7058 C  CG  . ASN   D  1 135 ? 27.697  -15.028 11.684  1.00 34.32  0  150 ASN   D CG  1 
ATOM   7059 O  OD1 . ASN   D  1 135 ? 26.932  -14.262 12.273  1.00 35.64  0  150 ASN   D OD1 1 
ATOM   7060 N  ND2 . ASN   D  1 135 ? 28.998  -14.971 11.861  1.00 34.06  0  150 ASN   D ND2 1 
ATOM   7061 N  N   A ASP   D  1 136 ? 24.516  -18.352 10.456  0.50 32.67  0  151 ASP   D N   1 
ATOM   7062 N  N   B ASP   D  1 136 ? 24.505  -18.326 10.440  0.50 33.04  0  151 ASP   D N   1 
ATOM   7063 C  CA  A ASP   D  1 136 ? 23.783  -19.249 9.522   0.50 36.07  0  151 ASP   D CA  1 
ATOM   7064 C  CA  B ASP   D  1 136 ? 23.686  -19.249 9.592   0.50 36.29  0  151 ASP   D CA  1 
ATOM   7065 C  C   A ASP   D  1 136 ? 24.167  -20.721 9.763   0.50 33.96  0  151 ASP   D C   1 
ATOM   7066 C  C   B ASP   D  1 136 ? 24.134  -20.709 9.778   0.50 34.19  0  151 ASP   D C   1 
ATOM   7067 O  O   A ASP   D  1 136 ? 24.116  -21.481 8.804   0.50 33.04  0  151 ASP   D O   1 
ATOM   7068 O  O   B ASP   D  1 136 ? 24.115  -21.429 8.787   0.50 33.15  0  151 ASP   D O   1 
ATOM   7069 C  CB  A ASP   D  1 136 ? 24.008  -18.838 8.054   0.50 36.68  0  151 ASP   D CB  1 
ATOM   7070 C  CB  B ASP   D  1 136 ? 23.713  -18.845 8.105   0.50 37.83  0  151 ASP   D CB  1 
ATOM   7071 C  CG  A ASP   D  1 136 ? 23.663  -17.381 7.772   0.00 36.27  0  151 ASP   D CG  1 
ATOM   7072 C  CG  B ASP   D  1 136 ? 22.541  -19.346 7.254   0.50 36.57  0  151 ASP   D CG  1 
ATOM   7073 O  OD1 A ASP   D  1 136 ? 22.466  -17.040 7.838   0.00 36.10  0  151 ASP   D OD1 1 
ATOM   7074 O  OD1 B ASP   D  1 136 ? 21.455  -19.644 7.798   0.50 34.47  0  151 ASP   D OD1 1 
ATOM   7075 O  OD2 A ASP   D  1 136 ? 24.596  -16.604 7.512   0.00 36.15  -1 151 ASP   D OD2 1 
ATOM   7076 O  OD2 B ASP   D  1 136 ? 22.709  -19.408 6.028   0.50 38.26  -1 151 ASP   D OD2 1 
ATOM   7077 N  N   . GLU   D  1 137 ? 24.523  -21.118 10.994  1.00 34.39  0  152 GLU   D N   1 
ATOM   7078 C  CA  . GLU   D  1 137 ? 24.890  -22.517 11.338  1.00 36.39  0  152 GLU   D CA  1 
ATOM   7079 C  C   . GLU   D  1 137 ? 24.018  -22.968 12.525  1.00 37.81  0  152 GLU   D C   1 
ATOM   7080 O  O   . GLU   D  1 137 ? 24.286  -22.511 13.684  1.00 33.01  0  152 GLU   D O   1 
ATOM   7081 C  CB  . GLU   D  1 137 ? 26.386  -22.624 11.623  1.00 42.45  0  152 GLU   D CB  1 
ATOM   7082 C  CG  . GLU   D  1 137 ? 26.885  -24.055 11.523  1.00 50.81  0  152 GLU   D CG  1 
ATOM   7083 C  CD  . GLU   D  1 137 ? 28.336  -24.300 11.930  1.00 60.23  0  152 GLU   D CD  1 
ATOM   7084 O  OE1 . GLU   D  1 137 ? 29.126  -23.340 11.948  1.00 55.37  0  152 GLU   D OE1 1 
ATOM   7085 O  OE2 . GLU   D  1 137 ? 28.677  -25.472 12.235  1.00 63.32  -1 152 GLU   D OE2 1 
ATOM   7086 N  N   . ARG   D  1 138 ? 23.006  -23.800 12.248  1.00 30.95  0  153 ARG   D N   1 
ATOM   7087 C  CA  . ARG   D  1 138 ? 22.023  -24.302 13.238  1.00 32.20  0  153 ARG   D CA  1 
ATOM   7088 C  C   . ARG   D  1 138 ? 22.724  -25.104 14.339  1.00 33.98  0  153 ARG   D C   1 
ATOM   7089 O  O   . ARG   D  1 138 ? 23.737  -25.806 14.057  1.00 30.50  0  153 ARG   D O   1 
ATOM   7090 C  CB  . ARG   D  1 138 ? 20.991  -25.237 12.605  1.00 36.19  0  153 ARG   D CB  1 
ATOM   7091 C  CG  . ARG   D  1 138 ? 20.075  -24.620 11.558  1.00 39.20  0  153 ARG   D CG  1 
ATOM   7092 C  CD  . ARG   D  1 138 ? 19.170  -23.528 12.084  1.00 41.22  0  153 ARG   D CD  1 
ATOM   7093 N  NE  . ARG   D  1 138 ? 19.802  -22.214 11.932  1.00 47.33  0  153 ARG   D NE  1 
ATOM   7094 C  CZ  . ARG   D  1 138 ? 19.901  -21.499 10.802  1.00 50.04  0  153 ARG   D CZ  1 
ATOM   7095 N  NH1 . ARG   D  1 138 ? 19.420  -21.966 9.660   1.00 57.81  1  153 ARG   D NH1 1 
ATOM   7096 N  NH2 . ARG   D  1 138 ? 20.500  -20.318 10.816  1.00 50.46  0  153 ARG   D NH2 1 
ATOM   7097 N  N   . LEU   D  1 139 ? 22.191  -25.032 15.559  1.00 35.17  0  154 LEU   D N   1 
ATOM   7098 C  CA  . LEU   D  1 139 ? 22.495  -26.039 16.606  1.00 29.67  0  154 LEU   D CA  1 
ATOM   7099 C  C   . LEU   D  1 139 ? 22.052  -27.383 16.035  1.00 27.92  0  154 LEU   D C   1 
ATOM   7100 O  O   . LEU   D  1 139 ? 20.883  -27.523 15.678  1.00 29.40  0  154 LEU   D O   1 
ATOM   7101 C  CB  . LEU   D  1 139 ? 21.729  -25.715 17.889  1.00 28.89  0  154 LEU   D CB  1 
ATOM   7102 C  CG  . LEU   D  1 139 ? 22.020  -26.639 19.071  1.00 25.41  0  154 LEU   D CG  1 
ATOM   7103 C  CD1 . LEU   D  1 139 ? 23.464  -26.518 19.541  1.00 24.22  0  154 LEU   D CD1 1 
ATOM   7104 C  CD2 . LEU   D  1 139 ? 21.055  -26.362 20.208  1.00 24.95  0  154 LEU   D CD2 1 
ATOM   7105 N  N   . PRO   D  1 140 ? 22.942  -28.385 15.915  1.00 26.62  0  155 PRO   D N   1 
ATOM   7106 C  CA  . PRO   D  1 140 ? 22.526  -29.714 15.473  1.00 28.16  0  155 PRO   D CA  1 
ATOM   7107 C  C   . PRO   D  1 140 ? 21.688  -30.493 16.489  1.00 28.99  0  155 PRO   D C   1 
ATOM   7108 O  O   . PRO   D  1 140 ? 21.809  -30.286 17.691  1.00 31.83  0  155 PRO   D O   1 
ATOM   7109 C  CB  . PRO   D  1 140 ? 23.854  -30.469 15.306  1.00 30.00  0  155 PRO   D CB  1 
ATOM   7110 C  CG  . PRO   D  1 140 ? 24.943  -29.382 15.252  1.00 31.55  0  155 PRO   D CG  1 
ATOM   7111 C  CD  . PRO   D  1 140 ? 24.400  -28.318 16.180  1.00 31.39  0  155 PRO   D CD  1 
ATOM   7112 N  N   . PRO   D  1 141 ? 20.867  -31.465 16.050  1.00 30.56  0  156 PRO   D N   1 
ATOM   7113 C  CA  . PRO   D  1 141 ? 20.279  -32.433 16.974  1.00 32.01  0  156 PRO   D CA  1 
ATOM   7114 C  C   . PRO   D  1 141 ? 21.414  -33.114 17.729  1.00 28.21  0  156 PRO   D C   1 
ATOM   7115 O  O   . PRO   D  1 141 ? 22.489  -33.291 17.163  1.00 28.93  0  156 PRO   D O   1 
ATOM   7116 C  CB  . PRO   D  1 141 ? 19.545  -33.451 16.086  1.00 33.12  0  156 PRO   D CB  1 
ATOM   7117 C  CG  . PRO   D  1 141 ? 19.400  -32.747 14.744  1.00 35.11  0  156 PRO   D CG  1 
ATOM   7118 C  CD  . PRO   D  1 141 ? 20.528  -31.746 14.649  1.00 31.52  0  156 PRO   D CD  1 
ATOM   7119 N  N   . PRO   D  1 142 ? 21.246  -33.521 19.010  1.00 30.38  0  157 PRO   D N   1 
ATOM   7120 C  CA  . PRO   D  1 142 ? 19.975  -33.418 19.747  1.00 28.58  0  157 PRO   D CA  1 
ATOM   7121 C  C   . PRO   D  1 142 ? 19.674  -32.093 20.483  1.00 31.07  0  157 PRO   D C   1 
ATOM   7122 O  O   . PRO   D  1 142 ? 18.959  -32.124 21.467  1.00 26.92  0  157 PRO   D O   1 
ATOM   7123 C  CB  . PRO   D  1 142 ? 20.177  -34.560 20.739  1.00 29.41  0  157 PRO   D CB  1 
ATOM   7124 C  CG  . PRO   D  1 142 ? 21.627  -34.476 21.097  1.00 29.71  0  157 PRO   D CG  1 
ATOM   7125 C  CD  . PRO   D  1 142 ? 22.322  -34.115 19.809  1.00 29.47  0  157 PRO   D CD  1 
ATOM   7126 N  N   . PHE   D  1 143 ? 20.272  -30.963 20.062  1.00 30.98  0  158 PHE   D N   1 
ATOM   7127 C  CA  . PHE   D  1 143 ? 19.887  -29.601 20.529  1.00 28.08  0  158 PHE   D CA  1 
ATOM   7128 C  C   . PHE   D  1 143 ? 20.161  -29.424 22.022  1.00 26.13  0  158 PHE   D C   1 
ATOM   7129 O  O   . PHE   D  1 143 ? 19.263  -29.133 22.815  1.00 23.36  0  158 PHE   D O   1 
ATOM   7130 C  CB  . PHE   D  1 143 ? 18.422  -29.317 20.223  1.00 27.55  0  158 PHE   D CB  1 
ATOM   7131 C  CG  . PHE   D  1 143 ? 17.946  -29.676 18.835  1.00 30.13  0  158 PHE   D CG  1 
ATOM   7132 C  CD1 . PHE   D  1 143 ? 18.390  -28.988 17.713  1.00 29.64  0  158 PHE   D CD1 1 
ATOM   7133 C  CD2 . PHE   D  1 143 ? 17.008  -30.690 18.652  1.00 34.43  0  158 PHE   D CD2 1 
ATOM   7134 C  CE1 . PHE   D  1 143 ? 17.925  -29.310 16.449  1.00 28.67  0  158 PHE   D CE1 1 
ATOM   7135 C  CE2 . PHE   D  1 143 ? 16.556  -31.021 17.379  1.00 33.05  0  158 PHE   D CE2 1 
ATOM   7136 C  CZ  . PHE   D  1 143 ? 16.998  -30.314 16.285  1.00 29.63  0  158 PHE   D CZ  1 
ATOM   7137 N  N   . PRO   D  1 144 ? 21.428  -29.569 22.451  1.00 25.65  0  159 PRO   D N   1 
ATOM   7138 C  CA  . PRO   D  1 144 ? 21.768  -29.403 23.856  1.00 26.40  0  159 PRO   D CA  1 
ATOM   7139 C  C   . PRO   D  1 144 ? 21.767  -27.902 24.186  1.00 25.01  0  159 PRO   D C   1 
ATOM   7140 O  O   . PRO   D  1 144 ? 22.203  -27.092 23.368  1.00 26.99  0  159 PRO   D O   1 
ATOM   7141 C  CB  . PRO   D  1 144 ? 23.169  -29.996 23.947  1.00 26.88  0  159 PRO   D CB  1 
ATOM   7142 C  CG  . PRO   D  1 144 ? 23.765  -29.689 22.563  1.00 28.97  0  159 PRO   D CG  1 
ATOM   7143 C  CD  . PRO   D  1 144 ? 22.605  -29.857 21.610  1.00 29.02  0  159 PRO   D CD  1 
ATOM   7144 N  N   . LEU   D  1 145 ? 21.283  -27.561 25.369  1.00 26.69  0  160 LEU   D N   1 
ATOM   7145 C  CA  . LEU   D  1 145 ? 21.458  -26.207 25.927  1.00 24.78  0  160 LEU   D CA  1 
ATOM   7146 C  C   . LEU   D  1 145 ? 22.964  -25.897 26.009  1.00 24.45  0  160 LEU   D C   1 
ATOM   7147 O  O   . LEU   D  1 145 ? 23.718  -26.657 26.625  1.00 26.78  0  160 LEU   D O   1 
ATOM   7148 C  CB  . LEU   D  1 145 ? 20.758  -26.122 27.282  1.00 25.45  0  160 LEU   D CB  1 
ATOM   7149 C  CG  . LEU   D  1 145 ? 20.990  -24.796 27.988  1.00 24.55  0  160 LEU   D CG  1 
ATOM   7150 C  CD1 . LEU   D  1 145 ? 20.315  -23.679 27.196  1.00 24.26  0  160 LEU   D CD1 1 
ATOM   7151 C  CD2 . LEU   D  1 145 ? 20.499  -24.888 29.413  1.00 25.84  0  160 LEU   D CD2 1 
ATOM   7152 N  N   . LYS   D  1 146 ? 23.405  -24.804 25.377  1.00 27.88  0  161 LYS   D N   1 
ATOM   7153 C  CA  . LYS   D  1 146 ? 24.817  -24.337 25.409  1.00 27.31  0  161 LYS   D CA  1 
ATOM   7154 C  C   . LYS   D  1 146 ? 24.957  -23.134 26.359  1.00 26.26  0  161 LYS   D C   1 
ATOM   7155 O  O   . LYS   D  1 146 ? 23.967  -22.466 26.671  1.00 22.98  0  161 LYS   D O   1 
ATOM   7156 C  CB  . LYS   D  1 146 ? 25.306  -24.022 23.991  1.00 27.20  0  161 LYS   D CB  1 
ATOM   7157 C  CG  . LYS   D  1 146 ? 25.517  -25.241 23.091  1.00 29.37  0  161 LYS   D CG  1 
ATOM   7158 C  CD  . LYS   D  1 146 ? 26.319  -24.948 21.784  1.00 29.81  0  161 LYS   D CD  1 
ATOM   7159 C  CE  . LYS   D  1 146 ? 27.798  -24.565 21.949  1.00 34.27  0  161 LYS   D CE  1 
ATOM   7160 N  NZ  . LYS   D  1 146 ? 28.359  -23.639 20.894  1.00 30.09  1  161 LYS   D NZ  1 
ATOM   7161 N  N   . GLN   D  1 147 ? 26.187  -22.915 26.793  1.00 25.13  0  162 GLN   D N   1 
ATOM   7162 C  CA  . GLN   D  1 147 ? 26.616  -21.811 27.680  1.00 26.28  0  162 GLN   D CA  1 
ATOM   7163 C  C   . GLN   D  1 147 ? 27.915  -21.281 27.088  1.00 27.39  0  162 GLN   D C   1 
ATOM   7164 O  O   . GLN   D  1 147 ? 28.613  -22.076 26.427  1.00 27.27  0  162 GLN   D O   1 
ATOM   7165 C  CB  . GLN   D  1 147 ? 26.869  -22.314 29.101  1.00 29.19  0  162 GLN   D CB  1 
ATOM   7166 C  CG  . GLN   D  1 147 ? 27.897  -23.448 29.184  1.00 31.54  0  162 GLN   D CG  1 
ATOM   7167 C  CD  . GLN   D  1 147 ? 28.131  -23.901 30.598  1.00 32.64  0  162 GLN   D CD  1 
ATOM   7168 O  OE1 . GLN   D  1 147 ? 27.203  -24.096 31.378  1.00 34.86  0  162 GLN   D OE1 1 
ATOM   7169 N  NE2 . GLN   D  1 147 ? 29.387  -23.988 30.975  1.00 35.34  0  162 GLN   D NE2 1 
ATOM   7170 N  N   . VAL   D  1 148 ? 28.219  -19.998 27.256  1.00 25.04  0  163 VAL   D N   1 
ATOM   7171 C  CA  . VAL   D  1 148 ? 29.589  -19.495 26.977  1.00 26.06  0  163 VAL   D CA  1 
ATOM   7172 C  C   . VAL   D  1 148 ? 29.838  -18.314 27.913  1.00 27.50  0  163 VAL   D C   1 
ATOM   7173 O  O   . VAL   D  1 148 ? 28.919  -17.494 28.142  1.00 25.65  0  163 VAL   D O   1 
ATOM   7174 C  CB  . VAL   D  1 148 ? 29.760  -19.142 25.484  1.00 26.73  0  163 VAL   D CB  1 
ATOM   7175 C  CG1 . VAL   D  1 148 ? 28.840  -17.990 25.037  1.00 26.27  0  163 VAL   D CG1 1 
ATOM   7176 C  CG2 . VAL   D  1 148 ? 31.201  -18.870 25.119  1.00 26.97  0  163 VAL   D CG2 1 
ATOM   7177 N  N   . LYS   D  1 149 ? 31.034  -18.277 28.477  1.00 28.97  0  164 LYS   D N   1 
ATOM   7178 C  CA  . LYS   D  1 149 ? 31.558  -17.131 29.264  1.00 34.31  0  164 LYS   D CA  1 
ATOM   7179 C  C   . LYS   D  1 149 ? 31.902  -16.000 28.292  1.00 29.26  0  164 LYS   D C   1 
ATOM   7180 O  O   . LYS   D  1 149 ? 32.558  -16.274 27.272  1.00 30.27  0  164 LYS   D O   1 
ATOM   7181 C  CB  . LYS   D  1 149 ? 32.781  -17.553 30.094  1.00 35.67  0  164 LYS   D CB  1 
ATOM   7182 C  CG  . LYS   D  1 149 ? 33.283  -16.500 31.092  1.00 39.56  0  164 LYS   D CG  1 
ATOM   7183 C  CD  . LYS   D  1 149 ? 34.609  -16.850 31.770  1.00 40.07  0  164 LYS   D CD  1 
ATOM   7184 C  CE  . LYS   D  1 149 ? 34.858  -16.120 33.072  1.00 40.32  0  164 LYS   D CE  1 
ATOM   7185 N  NZ  . LYS   D  1 149 ? 36.205  -16.414 33.620  0.00 39.56  1  164 LYS   D NZ  1 
ATOM   7186 N  N   . VAL   D  1 150 ? 31.314  -14.830 28.502  1.00 29.76  0  165 VAL   D N   1 
ATOM   7187 C  CA  . VAL   D  1 150 ? 31.511  -13.667 27.599  1.00 30.88  0  165 VAL   D CA  1 
ATOM   7188 C  C   . VAL   D  1 150 ? 32.088  -12.540 28.432  1.00 31.62  0  165 VAL   D C   1 
ATOM   7189 O  O   . VAL   D  1 150 ? 31.585  -12.260 29.531  1.00 29.06  0  165 VAL   D O   1 
ATOM   7190 C  CB  . VAL   D  1 150 ? 30.232  -13.231 26.857  1.00 29.86  0  165 VAL   D CB  1 
ATOM   7191 C  CG1 . VAL   D  1 150 ? 29.884  -14.238 25.783  1.00 30.93  0  165 VAL   D CG1 1 
ATOM   7192 C  CG2 . VAL   D  1 150 ? 29.071  -12.973 27.783  1.00 30.10  0  165 VAL   D CG2 1 
ATOM   7193 N  N   . PRO   D  1 151 ? 33.143  -11.873 27.910  1.00 32.77  0  166 PRO   D N   1 
ATOM   7194 C  CA  . PRO   D  1 151 ? 33.698  -10.713 28.589  1.00 35.07  0  166 PRO   D CA  1 
ATOM   7195 C  C   . PRO   D  1 151 ? 32.757  -9.509  28.386  1.00 35.37  0  166 PRO   D C   1 
ATOM   7196 O  O   . PRO   D  1 151 ? 32.366  -9.245  27.256  1.00 33.89  0  166 PRO   D O   1 
ATOM   7197 C  CB  . PRO   D  1 151 ? 35.069  -10.569 27.900  1.00 37.29  0  166 PRO   D CB  1 
ATOM   7198 C  CG  . PRO   D  1 151 ? 34.835  -11.073 26.483  1.00 37.04  0  166 PRO   D CG  1 
ATOM   7199 C  CD  . PRO   D  1 151 ? 33.839  -12.196 26.648  1.00 35.12  0  166 PRO   D CD  1 
ATOM   7200 N  N   . ILE   D  1 152 ? 32.397  -8.838  29.474  1.00 33.22  0  167 ILE   D N   1 
ATOM   7201 C  CA  . ILE   D  1 152 ? 31.679  -7.535  29.434  1.00 36.13  0  167 ILE   D CA  1 
ATOM   7202 C  C   . ILE   D  1 152 ? 32.649  -6.471  28.928  1.00 39.65  0  167 ILE   D C   1 
ATOM   7203 O  O   . ILE   D  1 152 ? 33.803  -6.453  29.383  1.00 40.79  0  167 ILE   D O   1 
ATOM   7204 C  CB  . ILE   D  1 152 ? 31.139  -7.148  30.813  1.00 41.26  0  167 ILE   D CB  1 
ATOM   7205 C  CG1 . ILE   D  1 152 ? 30.166  -8.191  31.371  1.00 46.36  0  167 ILE   D CG1 1 
ATOM   7206 C  CG2 . ILE   D  1 152 ? 30.541  -5.743  30.772  1.00 42.78  0  167 ILE   D CG2 1 
ATOM   7207 C  CD1 . ILE   D  1 152 ? 28.811  -8.131  30.768  1.00 49.37  0  167 ILE   D CD1 1 
ATOM   7208 N  N   . MET   D  1 153 ? 32.174  -5.555  28.090  1.00 40.87  0  168 MET   D N   1 
ATOM   7209 C  CA  A MET   D  1 153 ? 32.928  -4.334  27.699  0.50 42.59  0  168 MET   D CA  1 
ATOM   7210 C  CA  B MET   D  1 153 ? 32.943  -4.335  27.729  0.50 43.23  0  168 MET   D CA  1 
ATOM   7211 C  C   . MET   D  1 153 ? 32.070  -3.105  28.003  1.00 39.62  0  168 MET   D C   1 
ATOM   7212 O  O   . MET   D  1 153 ? 30.835  -3.217  27.880  1.00 44.49  0  168 MET   D O   1 
ATOM   7213 C  CB  A MET   D  1 153 ? 33.300  -4.379  26.217  0.50 45.16  0  168 MET   D CB  1 
ATOM   7214 C  CB  B MET   D  1 153 ? 33.425  -4.383  26.275  0.50 46.70  0  168 MET   D CB  1 
ATOM   7215 C  CG  A MET   D  1 153 ? 34.379  -5.390  25.906  0.50 48.98  0  168 MET   D CG  1 
ATOM   7216 C  CG  B MET   D  1 153 ? 34.682  -5.256  26.080  0.50 50.78  0  168 MET   D CG  1 
ATOM   7217 S  SD  A MET   D  1 153 ? 34.379  -5.789  24.145  0.50 50.83  0  168 MET   D SD  1 
ATOM   7218 S  SD  B MET   D  1 153 ? 34.356  -6.978  25.555  0.50 56.11  0  168 MET   D SD  1 
ATOM   7219 C  CE  A MET   D  1 153 ? 34.454  -4.148  23.440  0.50 45.15  0  168 MET   D CE  1 
ATOM   7220 C  CE  B MET   D  1 153 ? 32.661  -6.829  24.984  0.50 49.69  0  168 MET   D CE  1 
ATOM   7221 N  N   . GLU   D  1 154 ? 32.704  -2.004  28.433  1.00 37.27  0  169 GLU   D N   1 
ATOM   7222 C  CA  . GLU   D  1 154 ? 32.025  -0.712  28.730  1.00 34.14  0  169 GLU   D CA  1 
ATOM   7223 C  C   . GLU   D  1 154 ? 31.256  -0.239  27.484  1.00 29.87  0  169 GLU   D C   1 
ATOM   7224 O  O   . GLU   D  1 154 ? 31.765  -0.432  26.336  1.00 25.80  0  169 GLU   D O   1 
ATOM   7225 C  CB  . GLU   D  1 154 ? 33.032  0.360   29.158  1.00 43.45  0  169 GLU   D CB  1 
ATOM   7226 C  CG  . GLU   D  1 154 ? 33.272  0.443   30.652  1.00 52.89  0  169 GLU   D CG  1 
ATOM   7227 C  CD  . GLU   D  1 154 ? 34.069  1.690   30.995  1.00 61.47  0  169 GLU   D CD  1 
ATOM   7228 O  OE1 . GLU   D  1 154 ? 35.326  1.597   31.070  1.00 63.49  0  169 GLU   D OE1 1 
ATOM   7229 O  OE2 . GLU   D  1 154 ? 33.434  2.764   31.125  1.00 62.27  -1 169 GLU   D OE2 1 
ATOM   7230 N  N   . ASN   D  1 155 ? 30.097  0.411   27.690  1.00 28.11  0  170 ASN   D N   1 
ATOM   7231 C  CA  . ASN   D  1 155 ? 29.228  0.868   26.592  1.00 27.48  0  170 ASN   D CA  1 
ATOM   7232 C  C   . ASN   D  1 155 ? 30.031  1.763   25.637  1.00 29.81  0  170 ASN   D C   1 
ATOM   7233 O  O   . ASN   D  1 155 ? 29.813  1.638   24.416  1.00 27.68  0  170 ASN   D O   1 
ATOM   7234 C  CB  . ASN   D  1 155 ? 27.985  1.585   27.105  1.00 29.87  0  170 ASN   D CB  1 
ATOM   7235 C  CG  . ASN   D  1 155 ? 26.857  0.638   27.480  1.00 31.61  0  170 ASN   D CG  1 
ATOM   7236 O  OD1 . ASN   D  1 155 ? 27.103  -0.488  27.898  1.00 32.18  0  170 ASN   D OD1 1 
ATOM   7237 N  ND2 . ASN   D  1 155 ? 25.621  1.063   27.262  1.00 31.65  0  170 ASN   D ND2 1 
ATOM   7238 N  N   . HIS   D  1 156 ? 30.887  2.662   26.140  1.00 29.65  0  171 HIS   D N   1 
ATOM   7239 C  CA  . HIS   D  1 156 ? 31.555  3.672   25.273  1.00 33.00  0  171 HIS   D CA  1 
ATOM   7240 C  C   . HIS   D  1 156 ? 32.522  2.945   24.319  1.00 33.64  0  171 HIS   D C   1 
ATOM   7241 O  O   . HIS   D  1 156 ? 32.699  3.374   23.171  1.00 32.18  0  171 HIS   D O   1 
ATOM   7242 C  CB  . HIS   D  1 156 ? 32.165  4.826   26.094  1.00 36.19  0  171 HIS   D CB  1 
ATOM   7243 C  CG  . HIS   D  1 156 ? 33.513  4.558   26.669  1.00 43.14  0  171 HIS   D CG  1 
ATOM   7244 N  ND1 . HIS   D  1 156 ? 33.681  4.082   27.974  1.00 52.30  0  171 HIS   D ND1 1 
ATOM   7245 C  CD2 . HIS   D  1 156 ? 34.760  4.710   26.151  1.00 48.82  0  171 HIS   D CD2 1 
ATOM   7246 C  CE1 . HIS   D  1 156 ? 34.982  3.939   28.230  1.00 44.69  0  171 HIS   D CE1 1 
ATOM   7247 N  NE2 . HIS   D  1 156 ? 35.670  4.317   27.125  1.00 46.98  0  171 HIS   D NE2 1 
ATOM   7248 N  N   . ILE   D  1 157 ? 33.207  1.921   24.815  1.00 32.64  0  172 ILE   D N   1 
ATOM   7249 C  CA  . ILE   D  1 157 ? 34.177  1.102   24.037  1.00 32.97  0  172 ILE   D CA  1 
ATOM   7250 C  C   . ILE   D  1 157 ? 33.434  0.366   22.919  1.00 32.68  0  172 ILE   D C   1 
ATOM   7251 O  O   . ILE   D  1 157 ? 33.915  0.345   21.770  1.00 30.05  0  172 ILE   D O   1 
ATOM   7252 C  CB  . ILE   D  1 157 ? 34.892  0.114   24.971  1.00 34.35  0  172 ILE   D CB  1 
ATOM   7253 C  CG1 . ILE   D  1 157 ? 35.757  0.819   26.021  1.00 37.23  0  172 ILE   D CG1 1 
ATOM   7254 C  CG2 . ILE   D  1 157 ? 35.666  -0.916  24.169  1.00 38.26  0  172 ILE   D CG2 1 
ATOM   7255 C  CD1 . ILE   D  1 157 ? 36.767  1.779   25.442  1.00 38.44  0  172 ILE   D CD1 1 
ATOM   7256 N  N   A CYS   D  1 158 ? 32.308  -0.251  23.268  0.50 29.40  0  173 CYS   D N   1 
ATOM   7257 N  N   B CYS   D  1 158 ? 32.302  -0.266  23.233  0.50 30.17  0  173 CYS   D N   1 
ATOM   7258 C  CA  A CYS   D  1 158 ? 31.449  -1.021  22.356  0.50 30.48  0  173 CYS   D CA  1 
ATOM   7259 C  CA  B CYS   D  1 158 ? 31.512  -1.042  22.237  0.50 31.71  0  173 CYS   D CA  1 
ATOM   7260 C  C   A CYS   D  1 158 ? 30.883  -0.084  21.283  0.50 28.83  0  173 CYS   D C   1 
ATOM   7261 C  C   B CYS   D  1 158 ? 30.865  -0.079  21.238  0.50 29.71  0  173 CYS   D C   1 
ATOM   7262 O  O   A CYS   D  1 158 ? 30.922  -0.473  20.102  0.50 27.03  0  173 CYS   D O   1 
ATOM   7263 O  O   B CYS   D  1 158 ? 30.805  -0.460  20.043  0.50 28.32  0  173 CYS   D O   1 
ATOM   7264 C  CB  A CYS   D  1 158 ? 30.367  -1.677  23.207  0.50 31.25  0  173 CYS   D CB  1 
ATOM   7265 C  CB  B CYS   D  1 158 ? 30.466  -1.941  22.891  0.50 33.28  0  173 CYS   D CB  1 
ATOM   7266 S  SG  A CYS   D  1 158 ? 29.198  -2.683  22.286  0.50 32.61  0  173 CYS   D SG  1 
ATOM   7267 S  SG  B CYS   D  1 158 ? 31.224  -3.255  23.882  0.50 37.33  0  173 CYS   D SG  1 
ATOM   7268 N  N   . ASP   D  1 159 ? 30.418  1.112   21.691  1.00 27.50  0  174 ASP   D N   1 
ATOM   7269 C  CA  . ASP   D  1 159 ? 29.870  2.145   20.784  1.00 28.41  0  174 ASP   D CA  1 
ATOM   7270 C  C   . ASP   D  1 159 ? 30.962  2.527   19.786  1.00 27.85  0  174 ASP   D C   1 
ATOM   7271 O  O   . ASP   D  1 159 ? 30.674  2.521   18.571  1.00 24.04  0  174 ASP   D O   1 
ATOM   7272 C  CB  . ASP   D  1 159 ? 29.384  3.394   21.516  1.00 29.67  0  174 ASP   D CB  1 
ATOM   7273 C  CG  . ASP   D  1 159 ? 28.609  4.365   20.632  1.00 30.51  0  174 ASP   D CG  1 
ATOM   7274 O  OD1 . ASP   D  1 159 ? 27.677  3.913   19.927  1.00 30.51  0  174 ASP   D OD1 1 
ATOM   7275 O  OD2 . ASP   D  1 159 ? 28.910  5.594   20.688  1.00 30.77  -1 174 ASP   D OD2 1 
ATOM   7276 N  N   . ALA   D  1 160 ? 32.184  2.767   20.264  1.00 29.61  0  175 ALA   D N   1 
ATOM   7277 C  CA  . ALA   D  1 160 ? 33.302  3.138   19.364  1.00 29.34  0  175 ALA   D CA  1 
ATOM   7278 C  C   . ALA   D  1 160 ? 33.564  1.967   18.394  1.00 31.58  0  175 ALA   D C   1 
ATOM   7279 O  O   . ALA   D  1 160 ? 33.737  2.234   17.194  1.00 29.41  0  175 ALA   D O   1 
ATOM   7280 C  CB  . ALA   D  1 160 ? 34.531  3.524   20.149  1.00 32.10  0  175 ALA   D CB  1 
ATOM   7281 N  N   . LYS   D  1 161 ? 33.538  0.707   18.849  1.00 27.71  0  176 LYS   D N   1 
ATOM   7282 C  CA  . LYS   D  1 161 ? 33.782  -0.419  17.907  1.00 28.51  0  176 LYS   D CA  1 
ATOM   7283 C  C   . LYS   D  1 161 ? 32.695  -0.474  16.821  1.00 27.60  0  176 LYS   D C   1 
ATOM   7284 O  O   . LYS   D  1 161 ? 33.029  -0.642  15.630  1.00 26.64  0  176 LYS   D O   1 
ATOM   7285 C  CB  . LYS   D  1 161 ? 33.909  -1.740  18.638  1.00 32.31  0  176 LYS   D CB  1 
ATOM   7286 C  CG  . LYS   D  1 161 ? 35.197  -1.859  19.429  1.00 37.55  0  176 LYS   D CG  1 
ATOM   7287 C  CD  . LYS   D  1 161 ? 35.280  -3.175  20.132  1.00 43.18  0  176 LYS   D CD  1 
ATOM   7288 C  CE  . LYS   D  1 161 ? 36.546  -3.251  20.955  1.00 51.52  0  176 LYS   D CE  1 
ATOM   7289 N  NZ  . LYS   D  1 161 ? 36.999  -4.647  21.095  1.00 58.14  1  176 LYS   D NZ  1 
ATOM   7290 N  N   . TYR   D  1 162 ? 31.440  -0.254  17.177  1.00 27.10  0  177 TYR   D N   1 
ATOM   7291 C  CA  . TYR   D  1 162 ? 30.323  -0.312  16.214  1.00 26.74  0  177 TYR   D CA  1 
ATOM   7292 C  C   . TYR   D  1 162 ? 30.522  0.761   15.125  1.00 27.32  0  177 TYR   D C   1 
ATOM   7293 O  O   . TYR   D  1 162 ? 29.967  0.554   14.030  1.00 24.88  0  177 TYR   D O   1 
ATOM   7294 C  CB  . TYR   D  1 162 ? 28.973  -0.290  16.924  1.00 26.18  0  177 TYR   D CB  1 
ATOM   7295 C  CG  . TYR   D  1 162 ? 28.409  -1.683  17.102  1.00 27.98  0  177 TYR   D CG  1 
ATOM   7296 C  CD1 . TYR   D  1 162 ? 28.887  -2.537  18.092  1.00 28.47  0  177 TYR   D CD1 1 
ATOM   7297 C  CD2 . TYR   D  1 162 ? 27.454  -2.190  16.230  1.00 27.99  0  177 TYR   D CD2 1 
ATOM   7298 C  CE1 . TYR   D  1 162 ? 28.403  -3.827  18.250  1.00 27.16  0  177 TYR   D CE1 1 
ATOM   7299 C  CE2 . TYR   D  1 162 ? 26.995  -3.498  16.351  1.00 30.64  0  177 TYR   D CE2 1 
ATOM   7300 C  CZ  . TYR   D  1 162 ? 27.449  -4.313  17.377  1.00 29.56  0  177 TYR   D CZ  1 
ATOM   7301 O  OH  . TYR   D  1 162 ? 26.967  -5.592  17.516  1.00 30.04  0  177 TYR   D OH  1 
ATOM   7302 N  N   . HIS   D  1 163 ? 31.277  1.834   15.409  1.00 27.35  0  178 HIS   D N   1 
ATOM   7303 C  CA  . HIS   D  1 163 ? 31.568  2.942   14.453  1.00 26.32  0  178 HIS   D CA  1 
ATOM   7304 C  C   . HIS   D  1 163 ? 32.719  2.596   13.497  1.00 27.26  0  178 HIS   D C   1 
ATOM   7305 O  O   . HIS   D  1 163 ? 32.810  3.263   12.464  1.00 27.33  0  178 HIS   D O   1 
ATOM   7306 C  CB  . HIS   D  1 163 ? 31.797  4.259   15.217  1.00 26.02  0  178 HIS   D CB  1 
ATOM   7307 C  CG  . HIS   D  1 163 ? 30.530  4.891   15.688  1.00 25.18  0  178 HIS   D CG  1 
ATOM   7308 N  ND1 . HIS   D  1 163 ? 29.970  4.591   16.908  1.00 26.21  0  178 HIS   D ND1 1 
ATOM   7309 C  CD2 . HIS   D  1 163 ? 29.692  5.786   15.116  1.00 30.03  0  178 HIS   D CD2 1 
ATOM   7310 C  CE1 . HIS   D  1 163 ? 28.864  5.300   17.073  1.00 26.53  0  178 HIS   D CE1 1 
ATOM   7311 N  NE2 . HIS   D  1 163 ? 28.660  6.017   15.991  1.00 30.26  0  178 HIS   D NE2 1 
ATOM   7312 N  N   . LEU   D  1 164 ? 33.605  1.669   13.859  1.00 27.31  0  179 LEU   D N   1 
ATOM   7313 C  CA  . LEU   D  1 164 ? 34.724  1.258   12.982  1.00 28.17  0  179 LEU   D CA  1 
ATOM   7314 C  C   . LEU   D  1 164 ? 34.157  0.528   11.761  1.00 28.45  0  179 LEU   D C   1 
ATOM   7315 O  O   . LEU   D  1 164 ? 33.304  -0.380  11.957  1.00 26.29  0  179 LEU   D O   1 
ATOM   7316 C  CB  . LEU   D  1 164 ? 35.685  0.375   13.781  1.00 29.49  0  179 LEU   D CB  1 
ATOM   7317 C  CG  . LEU   D  1 164 ? 36.474  1.077   14.894  1.00 33.03  0  179 LEU   D CG  1 
ATOM   7318 C  CD1 . LEU   D  1 164 ? 37.291  0.088   15.718  1.00 37.22  0  179 LEU   D CD1 1 
ATOM   7319 C  CD2 . LEU   D  1 164 ? 37.391  2.168   14.326  1.00 32.95  0  179 LEU   D CD2 1 
ATOM   7320 N  N   . GLY   D  1 165 ? 34.572  0.909   10.546  1.00 26.85  0  180 GLY   D N   1 
ATOM   7321 C  CA  . GLY   D  1 165 ? 34.062  0.326   9.289   1.00 28.29  0  180 GLY   D CA  1 
ATOM   7322 C  C   . GLY   D  1 165 ? 32.619  0.717   9.034   1.00 30.01  0  180 GLY   D C   1 
ATOM   7323 O  O   . GLY   D  1 165 ? 31.937  0.003   8.238   1.00 26.07  0  180 GLY   D O   1 
ATOM   7324 N  N   . ALA   D  1 166 ? 32.169  1.845   9.603   1.00 25.77  0  181 ALA   D N   1 
ATOM   7325 C  CA  . ALA   D  1 166 ? 30.806  2.366   9.366   1.00 28.02  0  181 ALA   D CA  1 
ATOM   7326 C  C   . ALA   D  1 166 ? 30.845  3.814   8.895   1.00 27.31  0  181 ALA   D C   1 
ATOM   7327 O  O   . ALA   D  1 166 ? 31.737  4.517   9.272   1.00 29.11  0  181 ALA   D O   1 
ATOM   7328 C  CB  . ALA   D  1 166 ? 29.939  2.228   10.594  1.00 29.92  0  181 ALA   D CB  1 
ATOM   7329 N  N   . TYR   D  1 167 ? 29.823  4.233   8.159   1.00 29.58  0  182 TYR   D N   1 
ATOM   7330 C  CA  . TYR   D  1 167 ? 29.617  5.635   7.710   1.00 32.19  0  182 TYR   D CA  1 
ATOM   7331 C  C   . TYR   D  1 167 ? 29.044  6.461   8.871   1.00 30.40  0  182 TYR   D C   1 
ATOM   7332 O  O   . TYR   D  1 167 ? 29.069  7.674   8.796   1.00 25.63  0  182 TYR   D O   1 
ATOM   7333 C  CB  . TYR   D  1 167 ? 28.692  5.656   6.476   1.00 34.14  0  182 TYR   D CB  1 
ATOM   7334 C  CG  . TYR   D  1 167 ? 29.225  5.003   5.221   1.00 33.49  0  182 TYR   D CG  1 
ATOM   7335 C  CD1 . TYR   D  1 167 ? 30.257  5.574   4.500   1.00 36.06  0  182 TYR   D CD1 1 
ATOM   7336 C  CD2 . TYR   D  1 167 ? 28.664  3.835   4.716   1.00 37.41  0  182 TYR   D CD2 1 
ATOM   7337 C  CE1 . TYR   D  1 167 ? 30.737  4.998   3.330   1.00 36.07  0  182 TYR   D CE1 1 
ATOM   7338 C  CE2 . TYR   D  1 167 ? 29.118  3.254   3.536   1.00 36.15  0  182 TYR   D CE2 1 
ATOM   7339 C  CZ  . TYR   D  1 167 ? 30.157  3.840   2.835   1.00 36.90  0  182 TYR   D CZ  1 
ATOM   7340 O  OH  . TYR   D  1 167 ? 30.640  3.257   1.688   1.00 34.73  0  182 TYR   D OH  1 
ATOM   7341 N  N   . THR   D  1 168 ? 28.423  5.815   9.868   1.00 26.50  0  183 THR   D N   1 
ATOM   7342 C  CA  . THR   D  1 168 ? 27.684  6.524   10.935  1.00 28.02  0  183 THR   D CA  1 
ATOM   7343 C  C   . THR   D  1 168 ? 28.659  7.469   11.631  1.00 28.81  0  183 THR   D C   1 
ATOM   7344 O  O   . THR   D  1 168 ? 29.760  7.013   11.970  1.00 28.44  0  183 THR   D O   1 
ATOM   7345 C  CB  . THR   D  1 168 ? 27.035  5.546   11.925  1.00 29.79  0  183 THR   D CB  1 
ATOM   7346 O  OG1 . THR   D  1 168 ? 26.273  4.601   11.175  1.00 25.47  0  183 THR   D OG1 1 
ATOM   7347 C  CG2 . THR   D  1 168 ? 26.131  6.256   12.908  1.00 29.07  0  183 THR   D CG2 1 
ATOM   7348 N  N   . GLY   D  1 169 ? 28.254  8.731   11.833  1.00 29.04  0  184 GLY   D N   1 
ATOM   7349 C  CA  . GLY   D  1 169 ? 29.068  9.732   12.539  1.00 29.40  0  184 GLY   D CA  1 
ATOM   7350 C  C   . GLY   D  1 169 ? 29.385  9.290   13.956  1.00 27.33  0  184 GLY   D C   1 
ATOM   7351 O  O   . GLY   D  1 169 ? 28.502  8.684   14.627  1.00 26.66  0  184 GLY   D O   1 
ATOM   7352 N  N   . ASP   D  1 170 ? 30.616  9.557   14.388  1.00 29.72  0  185 ASP   D N   1 
ATOM   7353 C  CA  . ASP   D  1 170 ? 31.173  9.113   15.693  1.00 32.24  0  185 ASP   D CA  1 
ATOM   7354 C  C   . ASP   D  1 170 ? 30.335  9.601   16.881  1.00 31.13  0  185 ASP   D C   1 
ATOM   7355 O  O   . ASP   D  1 170 ? 30.317  8.865   17.923  1.00 31.91  0  185 ASP   D O   1 
ATOM   7356 C  CB  . ASP   D  1 170 ? 32.642  9.512   15.817  1.00 33.05  0  185 ASP   D CB  1 
ATOM   7357 C  CG  . ASP   D  1 170 ? 33.582  8.628   14.998  1.00 41.35  0  185 ASP   D CG  1 
ATOM   7358 O  OD1 . ASP   D  1 170 ? 33.192  7.501   14.580  1.00 47.43  0  185 ASP   D OD1 1 
ATOM   7359 O  OD2 . ASP   D  1 170 ? 34.723  9.041   14.807  1.00 49.08  -1 185 ASP   D OD2 1 
ATOM   7360 N  N   A ASP   D  1 171 ? 29.666  10.748  16.767  0.50 28.13  0  186 ASP   D N   1 
ATOM   7361 N  N   B ASP   D  1 171 ? 29.661  10.740  16.677  0.50 27.90  0  186 ASP   D N   1 
ATOM   7362 C  CA  A ASP   D  1 171 ? 28.847  11.340  17.868  0.50 29.74  0  186 ASP   D CA  1 
ATOM   7363 C  CA  B ASP   D  1 171 ? 28.824  11.499  17.643  0.50 30.19  0  186 ASP   D CA  1 
ATOM   7364 C  C   A ASP   D  1 171 ? 27.370  10.973  17.681  0.50 27.35  0  186 ASP   D C   1 
ATOM   7365 C  C   B ASP   D  1 171 ? 27.450  10.840  17.772  0.50 27.74  0  186 ASP   D C   1 
ATOM   7366 O  O   A ASP   D  1 171 ? 26.516  11.621  18.326  0.50 25.66  0  186 ASP   D O   1 
ATOM   7367 O  O   B ASP   D  1 171 ? 26.778  11.108  18.765  0.50 28.10  0  186 ASP   D O   1 
ATOM   7368 C  CB  A ASP   D  1 171 ? 29.033  12.859  17.927  0.50 31.20  0  186 ASP   D CB  1 
ATOM   7369 C  CB  B ASP   D  1 171 ? 28.679  12.966  17.191  0.50 30.27  0  186 ASP   D CB  1 
ATOM   7370 C  CG  A ASP   D  1 171 ? 30.438  13.321  18.271  0.50 33.43  0  186 ASP   D CG  1 
ATOM   7371 C  CG  B ASP   D  1 171 ? 28.343  13.197  15.714  0.50 31.55  0  186 ASP   D CG  1 
ATOM   7372 O  OD1 A ASP   D  1 171 ? 31.407  12.635  17.922  0.50 36.71  0  186 ASP   D OD1 1 
ATOM   7373 O  OD1 B ASP   D  1 171 ? 28.964  12.556  14.831  0.50 28.25  0  186 ASP   D OD1 1 
ATOM   7374 O  OD2 A ASP   D  1 171 ? 30.551  14.384  18.904  0.50 39.50  -1 186 ASP   D OD2 1 
ATOM   7375 O  OD2 B ASP   D  1 171 ? 27.465  14.046  15.444  0.50 34.65  -1 186 ASP   D OD2 1 
ATOM   7376 N  N   . VAL   D  1 172 ? 27.048  10.033  16.790  1.00 26.44  0  187 VAL   D N   1 
ATOM   7377 C  CA  . VAL   D  1 172 ? 25.678  9.451   16.696  1.00 23.23  0  187 VAL   D CA  1 
ATOM   7378 C  C   . VAL   D  1 172 ? 25.734  8.089   17.397  1.00 25.93  0  187 VAL   D C   1 
ATOM   7379 O  O   . VAL   D  1 172 ? 26.387  7.161   16.854  1.00 28.12  0  187 VAL   D O   1 
ATOM   7380 C  CB  . VAL   D  1 172 ? 25.204  9.334   15.240  1.00 25.31  0  187 VAL   D CB  1 
ATOM   7381 C  CG1 . VAL   D  1 172 ? 23.794  8.718   15.186  1.00 24.36  0  187 VAL   D CG1 1 
ATOM   7382 C  CG2 . VAL   D  1 172 ? 25.259  10.696  14.550  1.00 28.45  0  187 VAL   D CG2 1 
ATOM   7383 N  N   . ARG   D  1 173 ? 25.144  7.991   18.590  1.00 26.16  0  188 ARG   D N   1 
ATOM   7384 C  CA  . ARG   D  1 173 ? 25.344  6.829   19.483  1.00 24.68  0  188 ARG   D CA  1 
ATOM   7385 C  C   . ARG   D  1 173 ? 24.605  5.618   18.875  1.00 24.65  0  188 ARG   D C   1 
ATOM   7386 O  O   . ARG   D  1 173 ? 23.427  5.752   18.509  1.00 23.99  0  188 ARG   D O   1 
ATOM   7387 C  CB  . ARG   D  1 173 ? 24.858  7.161   20.890  1.00 25.20  0  188 ARG   D CB  1 
ATOM   7388 C  CG  . ARG   D  1 173 ? 25.422  6.200   21.925  1.00 26.42  0  188 ARG   D CG  1 
ATOM   7389 C  CD  . ARG   D  1 173 ? 25.316  6.653   23.331  1.00 30.60  0  188 ARG   D CD  1 
ATOM   7390 N  NE  . ARG   D  1 173 ? 26.225  7.758   23.592  1.00 31.56  0  188 ARG   D NE  1 
ATOM   7391 C  CZ  . ARG   D  1 173 ? 26.602  8.135   24.816  1.00 33.25  0  188 ARG   D CZ  1 
ATOM   7392 N  NH1 . ARG   D  1 173 ? 26.115  7.537   25.907  1.00 31.79  1  188 ARG   D NH1 1 
ATOM   7393 N  NH2 . ARG   D  1 173 ? 27.413  9.166   24.938  1.00 31.95  0  188 ARG   D NH2 1 
ATOM   7394 N  N   . ILE   D  1 174 ? 25.288  4.499   18.765  1.00 25.53  0  189 ILE   D N   1 
ATOM   7395 C  CA  . ILE   D  1 174 ? 24.704  3.223   18.270  1.00 25.53  0  189 ILE   D CA  1 
ATOM   7396 C  C   . ILE   D  1 174 ? 24.334  2.352   19.477  1.00 26.02  0  189 ILE   D C   1 
ATOM   7397 O  O   . ILE   D  1 174 ? 23.143  1.906   19.564  1.00 27.97  0  189 ILE   D O   1 
ATOM   7398 C  CB  . ILE   D  1 174 ? 25.653  2.507   17.296  1.00 26.20  0  189 ILE   D CB  1 
ATOM   7399 C  CG1 . ILE   D  1 174 ? 25.870  3.316   16.012  1.00 28.64  0  189 ILE   D CG1 1 
ATOM   7400 C  CG2 . ILE   D  1 174 ? 25.084  1.115   16.994  1.00 26.01  0  189 ILE   D CG2 1 
ATOM   7401 C  CD1 . ILE   D  1 174 ? 27.012  2.834   15.144  1.00 27.65  0  189 ILE   D CD1 1 
ATOM   7402 N  N   . VAL   D  1 175 ? 25.296  2.150   20.377  1.00 23.09  0  190 VAL   D N   1 
ATOM   7403 C  CA  . VAL   D  1 175 ? 25.081  1.362   21.620  1.00 26.04  0  190 VAL   D CA  1 
ATOM   7404 C  C   . VAL   D  1 175 ? 24.496  2.293   22.691  1.00 26.12  0  190 VAL   D C   1 
ATOM   7405 O  O   . VAL   D  1 175 ? 25.229  3.136   23.187  1.00 26.40  0  190 VAL   D O   1 
ATOM   7406 C  CB  . VAL   D  1 175 ? 26.385  0.680   22.063  1.00 25.19  0  190 VAL   D CB  1 
ATOM   7407 C  CG1 . VAL   D  1 175 ? 26.175  -0.083  23.381  1.00 26.74  0  190 VAL   D CG1 1 
ATOM   7408 C  CG2 . VAL   D  1 175 ? 26.875  -0.234  20.958  1.00 26.13  0  190 VAL   D CG2 1 
ATOM   7409 N  N   . ARG   D  1 176 ? 23.217  2.127   23.025  1.00 24.64  0  191 ARG   D N   1 
ATOM   7410 C  CA  . ARG   D  1 176 ? 22.466  3.103   23.850  1.00 27.23  0  191 ARG   D CA  1 
ATOM   7411 C  C   . ARG   D  1 176 ? 22.609  2.740   25.326  1.00 26.89  0  191 ARG   D C   1 
ATOM   7412 O  O   . ARG   D  1 176 ? 23.184  1.658   25.658  1.00 27.12  0  191 ARG   D O   1 
ATOM   7413 C  CB  . ARG   D  1 176 ? 21.042  3.208   23.288  1.00 30.83  0  191 ARG   D CB  1 
ATOM   7414 C  CG  . ARG   D  1 176 ? 21.063  3.662   21.838  1.00 33.73  0  191 ARG   D CG  1 
ATOM   7415 C  CD  . ARG   D  1 176 ? 19.773  4.256   21.402  1.00 41.78  0  191 ARG   D CD  1 
ATOM   7416 N  NE  . ARG   D  1 176 ? 19.788  4.612   19.993  1.00 41.43  0  191 ARG   D NE  1 
ATOM   7417 C  CZ  . ARG   D  1 176 ? 18.889  5.388   19.419  1.00 45.17  0  191 ARG   D CZ  1 
ATOM   7418 N  NH1 . ARG   D  1 176 ? 17.924  5.943   20.139  1.00 49.02  1  191 ARG   D NH1 1 
ATOM   7419 N  NH2 . ARG   D  1 176 ? 18.984  5.662   18.129  1.00 46.52  0  191 ARG   D NH2 1 
ATOM   7420 N  N   . ASP   D  1 177 ? 22.157  3.642   26.195  1.00 26.98  0  192 ASP   D N   1 
ATOM   7421 C  CA  . ASP   D  1 177 ? 22.466  3.590   27.645  1.00 27.42  0  192 ASP   D CA  1 
ATOM   7422 C  C   . ASP   D  1 177 ? 21.595  2.497   28.311  1.00 26.44  0  192 ASP   D C   1 
ATOM   7423 O  O   . ASP   D  1 177 ? 22.006  1.984   29.340  1.00 25.08  0  192 ASP   D O   1 
ATOM   7424 C  CB  . ASP   D  1 177 ? 22.283  4.964   28.304  1.00 30.00  0  192 ASP   D CB  1 
ATOM   7425 C  CG  . ASP   D  1 177 ? 23.050  6.111   27.655  1.00 32.12  0  192 ASP   D CG  1 
ATOM   7426 O  OD1 . ASP   D  1 177 ? 24.001  5.845   26.872  1.00 30.02  0  192 ASP   D OD1 1 
ATOM   7427 O  OD2 . ASP   D  1 177 ? 22.656  7.255   27.898  1.00 31.67  -1 192 ASP   D OD2 1 
ATOM   7428 N  N   . ASP   D  1 178 ? 20.469  2.117   27.712  1.00 23.60  0  193 ASP   D N   1 
ATOM   7429 C  CA  . ASP   D  1 178 ? 19.627  0.986   28.168  1.00 25.05  0  193 ASP   D CA  1 
ATOM   7430 C  C   . ASP   D  1 178 ? 20.156  -0.356  27.620  1.00 24.26  0  193 ASP   D C   1 
ATOM   7431 O  O   . ASP   D  1 178 ? 19.415  -1.340  27.714  1.00 27.80  0  193 ASP   D O   1 
ATOM   7432 C  CB  . ASP   D  1 178 ? 18.158  1.234   27.793  1.00 25.23  0  193 ASP   D CB  1 
ATOM   7433 C  CG  . ASP   D  1 178 ? 17.875  1.119   26.305  1.00 28.19  0  193 ASP   D CG  1 
ATOM   7434 O  OD1 . ASP   D  1 178 ? 18.786  1.420   25.526  1.00 25.32  0  193 ASP   D OD1 1 
ATOM   7435 O  OD2 . ASP   D  1 178 ? 16.770  0.655   25.948  1.00 28.01  -1 193 ASP   D OD2 1 
ATOM   7436 N  N   . MET   D  1 179 ? 21.352  -0.407  27.044  1.00 25.74  0  194 MET   D N   1 
ATOM   7437 C  CA  . MET   D  1 179 ? 21.949  -1.630  26.456  1.00 25.28  0  194 MET   D CA  1 
ATOM   7438 C  C   . MET   D  1 179 ? 23.260  -1.914  27.164  1.00 27.01  0  194 MET   D C   1 
ATOM   7439 O  O   . MET   D  1 179 ? 23.764  -1.054  27.917  1.00 26.30  0  194 MET   D O   1 
ATOM   7440 C  CB  . MET   D  1 179 ? 22.205  -1.483  24.954  1.00 25.68  0  194 MET   D CB  1 
ATOM   7441 C  CG  . MET   D  1 179 ? 20.957  -1.165  24.158  1.00 26.16  0  194 MET   D CG  1 
ATOM   7442 S  SD  . MET   D  1 179 ? 21.294  -0.749  22.443  1.00 26.75  0  194 MET   D SD  1 
ATOM   7443 C  CE  . MET   D  1 179 ? 19.650  -0.236  21.960  1.00 25.31  0  194 MET   D CE  1 
ATOM   7444 N  N   . LEU   D  1 180 ? 23.742  -3.128  26.972  1.00 26.05  0  195 LEU   D N   1 
ATOM   7445 C  CA  . LEU   D  1 180 ? 24.913  -3.706  27.655  1.00 27.78  0  195 LEU   D CA  1 
ATOM   7446 C  C   . LEU   D  1 180 ? 25.609  -4.548  26.601  1.00 28.95  0  195 LEU   D C   1 
ATOM   7447 O  O   . LEU   D  1 180 ? 24.930  -5.191  25.805  1.00 28.69  0  195 LEU   D O   1 
ATOM   7448 C  CB  . LEU   D  1 180 ? 24.455  -4.559  28.850  1.00 27.08  0  195 LEU   D CB  1 
ATOM   7449 C  CG  . LEU   D  1 180 ? 25.567  -5.219  29.650  1.00 30.39  0  195 LEU   D CG  1 
ATOM   7450 C  CD1 . LEU   D  1 180 ? 25.141  -5.348  31.091  1.00 33.10  0  195 LEU   D CD1 1 
ATOM   7451 C  CD2 . LEU   D  1 180 ? 25.938  -6.591  29.093  1.00 35.11  0  195 LEU   D CD2 1 
ATOM   7452 N  N   A CYS   D  1 181 ? 26.939  -4.578  26.621  0.50 27.02  0  196 CYS   D N   1 
ATOM   7453 N  N   B CYS   D  1 181 ? 26.924  -4.619  26.681  0.50 28.66  0  196 CYS   D N   1 
ATOM   7454 C  CA  A CYS   D  1 181 ? 27.765  -5.223  25.569  0.50 27.80  0  196 CYS   D CA  1 
ATOM   7455 C  CA  B CYS   D  1 181 ? 27.752  -5.205  25.620  0.50 30.41  0  196 CYS   D CA  1 
ATOM   7456 C  C   A CYS   D  1 181 ? 28.618  -6.338  26.171  0.50 27.28  0  196 CYS   D C   1 
ATOM   7457 C  C   B CYS   D  1 181 ? 28.611  -6.340  26.184  0.50 28.66  0  196 CYS   D C   1 
ATOM   7458 O  O   A CYS   D  1 181 ? 29.308  -6.086  27.200  0.50 27.06  0  196 CYS   D O   1 
ATOM   7459 O  O   B CYS   D  1 181 ? 29.261  -6.117  27.232  0.50 28.24  0  196 CYS   D O   1 
ATOM   7460 C  CB  A CYS   D  1 181 ? 28.677  -4.192  24.906  0.50 31.16  0  196 CYS   D CB  1 
ATOM   7461 C  CB  B CYS   D  1 181 ? 28.584  -4.072  25.043  0.50 36.21  0  196 CYS   D CB  1 
ATOM   7462 S  SG  A CYS   D  1 181 ? 27.802  -3.111  23.752  0.50 32.52  0  196 CYS   D SG  1 
ATOM   7463 S  SG  B CYS   D  1 181 ? 29.794  -4.696  23.868  0.50 42.27  0  196 CYS   D SG  1 
ATOM   7464 N  N   . ALA   D  1 182 ? 28.645  -7.493  25.503  1.00 28.13  0  197 ALA   D N   1 
ATOM   7465 C  CA  . ALA   D  1 182 ? 29.542  -8.610  25.855  1.00 25.91  0  197 ALA   D CA  1 
ATOM   7466 C  C   . ALA   D  1 182 ? 29.863  -9.451  24.625  1.00 27.07  0  197 ALA   D C   1 
ATOM   7467 O  O   . ALA   D  1 182 ? 29.009  -9.567  23.729  1.00 26.59  0  197 ALA   D O   1 
ATOM   7468 C  CB  . ALA   D  1 182 ? 28.959  -9.444  26.969  1.00 26.11  0  197 ALA   D CB  1 
ATOM   7469 N  N   . GLY   D  1 183 ? 31.052  -10.061 24.645  1.00 24.11  0  198 GLY   D N   1 
ATOM   7470 C  CA  . GLY   D  1 183 ? 31.454  -11.074 23.668  1.00 25.95  0  198 GLY   D CA  1 
ATOM   7471 C  C   . GLY   D  1 183 ? 32.638  -10.598 22.878  1.00 29.52  0  198 GLY   D C   1 
ATOM   7472 O  O   . GLY   D  1 183 ? 33.018  -9.417  23.004  1.00 32.44  0  198 GLY   D O   1 
ATOM   7473 N  N   . ASN   D  1 184 ? 33.222  -11.519 22.124  1.00 29.29  0  199 ASN   D N   1 
ATOM   7474 C  CA  . ASN   D  1 184 ? 34.349  -11.246 21.207  1.00 28.92  0  199 ASN   D CA  1 
ATOM   7475 C  C   . ASN   D  1 184 ? 34.161  -12.150 19.987  1.00 29.31  0  199 ASN   D C   1 
ATOM   7476 O  O   . ASN   D  1 184 ? 33.067  -12.660 19.825  1.00 29.48  0  199 ASN   D O   1 
ATOM   7477 C  CB  . ASN   D  1 184 ? 35.668  -11.418 21.960  1.00 30.15  0  199 ASN   D CB  1 
ATOM   7478 C  CG  . ASN   D  1 184 ? 35.856  -12.814 22.529  1.00 30.69  0  199 ASN   D CG  1 
ATOM   7479 O  OD1 . ASN   D  1 184 ? 35.335  -13.832 22.030  1.00 29.25  0  199 ASN   D OD1 1 
ATOM   7480 N  ND2 . ASN   D  1 184 ? 36.620  -12.869 23.605  1.00 33.00  0  199 ASN   D ND2 1 
ATOM   7481 N  N   . THR   D  1 185 ? 35.200  -12.360 19.197  1.00 29.72  0  200 THR   D N   1 
ATOM   7482 C  CA  . THR   D  1 185 ? 35.158  -13.141 17.936  1.00 34.22  0  200 THR   D CA  1 
ATOM   7483 C  C   . THR   D  1 185 ? 35.213  -14.644 18.241  1.00 32.00  0  200 THR   D C   1 
ATOM   7484 O  O   . THR   D  1 185 ? 35.123  -15.390 17.284  1.00 30.58  0  200 THR   D O   1 
ATOM   7485 C  CB  . THR   D  1 185 ? 36.282  -12.699 16.988  1.00 31.86  0  200 THR   D CB  1 
ATOM   7486 O  OG1 . THR   D  1 185 ? 37.512  -12.844 17.686  1.00 32.62  0  200 THR   D OG1 1 
ATOM   7487 C  CG2 . THR   D  1 185 ? 36.166  -11.245 16.574  1.00 34.78  0  200 THR   D CG2 1 
ATOM   7488 N  N   . ARG   D  1 186 ? 35.278  -15.084 19.497  1.00 32.13  0  201 ARG   D N   1 
ATOM   7489 C  CA  . ARG   D  1 186 ? 35.220  -16.534 19.825  1.00 33.88  0  201 ARG   D CA  1 
ATOM   7490 C  C   . ARG   D  1 186 ? 33.993  -16.904 20.667  1.00 33.07  0  201 ARG   D C   1 
ATOM   7491 O  O   . ARG   D  1 186 ? 33.716  -18.095 20.808  1.00 38.03  0  201 ARG   D O   1 
ATOM   7492 C  CB  . ARG   D  1 186 ? 36.523  -16.919 20.518  1.00 38.65  0  201 ARG   D CB  1 
ATOM   7493 C  CG  . ARG   D  1 186 ? 37.718  -16.901 19.570  1.00 47.20  0  201 ARG   D CG  1 
ATOM   7494 C  CD  . ARG   D  1 186 ? 39.050  -16.988 20.290  1.00 48.92  0  201 ARG   D CD  1 
ATOM   7495 N  NE  . ARG   D  1 186 ? 39.235  -15.928 21.287  1.00 58.04  0  201 ARG   D NE  1 
ATOM   7496 C  CZ  . ARG   D  1 186 ? 39.690  -14.682 21.064  1.00 59.36  0  201 ARG   D CZ  1 
ATOM   7497 N  NH1 . ARG   D  1 186 ? 40.022  -14.271 19.849  1.00 62.77  1  201 ARG   D NH1 1 
ATOM   7498 N  NH2 . ARG   D  1 186 ? 39.815  -13.842 22.079  1.00 60.99  0  201 ARG   D NH2 1 
ATOM   7499 N  N   . ARG   D  1 187 ? 33.337  -15.935 21.296  1.00 29.44  0  202 ARG   D N   1 
ATOM   7500 C  CA  . ARG   D  1 187 ? 32.303  -16.164 22.343  1.00 27.10  0  202 ARG   D CA  1 
ATOM   7501 C  C   . ARG   D  1 187 ? 31.166  -15.157 22.129  1.00 28.04  0  202 ARG   D C   1 
ATOM   7502 O  O   . ARG   D  1 187 ? 31.434  -13.930 22.209  1.00 25.95  0  202 ARG   D O   1 
ATOM   7503 C  CB  . ARG   D  1 187 ? 32.930  -15.948 23.714  1.00 29.01  0  202 ARG   D CB  1 
ATOM   7504 C  CG  . ARG   D  1 187 ? 34.072  -16.891 24.045  1.00 32.05  0  202 ARG   D CG  1 
ATOM   7505 C  CD  . ARG   D  1 187 ? 34.961  -16.249 25.093  1.00 36.21  0  202 ARG   D CD  1 
ATOM   7506 N  NE  . ARG   D  1 187 ? 36.025  -17.179 25.459  1.00 42.79  0  202 ARG   D NE  1 
ATOM   7507 C  CZ  . ARG   D  1 187 ? 35.899  -18.232 26.263  1.00 45.05  0  202 ARG   D CZ  1 
ATOM   7508 N  NH1 . ARG   D  1 187 ? 34.736  -18.532 26.831  1.00 48.55  1  202 ARG   D NH1 1 
ATOM   7509 N  NH2 . ARG   D  1 187 ? 36.954  -18.999 26.484  1.00 45.77  0  202 ARG   D NH2 1 
ATOM   7510 N  N   . ASP   D  1 188 ? 29.957  -15.620 21.810  1.00 26.86  0  203 ASP   D N   1 
ATOM   7511 C  CA  . ASP   D  1 188 ? 28.817  -14.697 21.560  1.00 26.33  0  203 ASP   D CA  1 
ATOM   7512 C  C   . ASP   D  1 188 ? 27.527  -15.509 21.649  1.00 28.46  0  203 ASP   D C   1 
ATOM   7513 O  O   . ASP   D  1 188 ? 27.580  -16.766 21.692  1.00 26.37  0  203 ASP   D O   1 
ATOM   7514 C  CB  . ASP   D  1 188 ? 28.980  -13.966 20.217  1.00 27.54  0  203 ASP   D CB  1 
ATOM   7515 C  CG  . ASP   D  1 188 ? 28.237  -12.633 20.044  1.00 30.87  0  203 ASP   D CG  1 
ATOM   7516 O  OD1 . ASP   D  1 188 ? 27.403  -12.251 20.958  1.00 28.44  0  203 ASP   D OD1 1 
ATOM   7517 O  OD2 . ASP   D  1 188 ? 28.456  -11.976 18.985  1.00 28.32  -1 203 ASP   D OD2 1 
ATOM   7518 N  N   . SER   D  1 189 ? 26.406  -14.799 21.716  1.00 28.50  0  204 SER   D N   1 
ATOM   7519 C  CA  . SER   D  1 189 ? 25.061  -15.342 21.465  1.00 30.33  0  204 SER   D CA  1 
ATOM   7520 C  C   . SER   D  1 189 ? 24.782  -15.145 19.979  1.00 31.81  0  204 SER   D C   1 
ATOM   7521 O  O   . SER   D  1 189 ? 25.491  -14.327 19.296  1.00 24.62  0  204 SER   D O   1 
ATOM   7522 C  CB  . SER   D  1 189 ? 24.053  -14.636 22.325  1.00 32.42  0  204 SER   D CB  1 
ATOM   7523 O  OG  . SER   D  1 189 ? 24.170  -13.231 22.140  1.00 33.74  0  204 SER   D OG  1 
ATOM   7524 N  N   . CYS   D  1 190 ? 23.825  -15.891 19.465  1.00 26.53  0  205 CYS   D N   1 
ATOM   7525 C  CA  . CYS   D  1 190 ? 23.513  -15.873 18.030  1.00 29.09  0  205 CYS   D CA  1 
ATOM   7526 C  C   . CYS   D  1 190 ? 22.007  -16.078 17.843  1.00 26.96  0  205 CYS   D C   1 
ATOM   7527 O  O   . CYS   D  1 190 ? 21.272  -16.101 18.845  1.00 25.29  0  205 CYS   D O   1 
ATOM   7528 C  CB  . CYS   D  1 190 ? 24.400  -16.904 17.337  1.00 31.47  0  205 CYS   D CB  1 
ATOM   7529 S  SG  . CYS   D  1 190 ? 24.575  -16.600 15.554  1.00 38.55  0  205 CYS   D SG  1 
ATOM   7530 N  N   . GLN   D  1 191 ? 21.557  -16.178 16.597  1.00 28.04  0  206 GLN   D N   1 
ATOM   7531 C  CA  . GLN   D  1 191 ? 20.116  -16.264 16.230  1.00 26.78  0  206 GLN   D CA  1 
ATOM   7532 C  C   . GLN   D  1 191 ? 19.536  -17.487 16.939  1.00 24.80  0  206 GLN   D C   1 
ATOM   7533 O  O   . GLN   D  1 191 ? 20.156  -18.560 16.831  1.00 23.18  0  206 GLN   D O   1 
ATOM   7534 C  CB  . GLN   D  1 191 ? 19.912  -16.352 14.715  1.00 29.89  0  206 GLN   D CB  1 
ATOM   7535 C  CG  . GLN   D  1 191 ? 20.032  -14.994 14.001  1.00 35.14  0  206 GLN   D CG  1 
ATOM   7536 C  CD  . GLN   D  1 191 ? 21.408  -14.359 14.088  1.00 34.76  0  206 GLN   D CD  1 
ATOM   7537 O  OE1 . GLN   D  1 191 ? 22.435  -14.988 13.806  1.00 35.77  0  206 GLN   D OE1 1 
ATOM   7538 N  NE2 . GLN   D  1 191 ? 21.463  -13.105 14.521  1.00 35.73  0  206 GLN   D NE2 1 
ATOM   7539 N  N   . GLY   D  1 192 ? 18.407  -17.328 17.627  1.00 26.73  0  207 GLY   D N   1 
ATOM   7540 C  CA  . GLY   D  1 192 ? 17.779  -18.362 18.491  1.00 26.05  0  207 GLY   D CA  1 
ATOM   7541 C  C   . GLY   D  1 192 ? 18.134  -18.195 19.972  1.00 26.11  0  207 GLY   D C   1 
ATOM   7542 O  O   . GLY   D  1 192 ? 17.452  -18.837 20.826  1.00 27.11  0  207 GLY   D O   1 
ATOM   7543 N  N   . ASP   D  1 193 ? 19.157  -17.388 20.324  1.00 24.49  0  208 ASP   D N   1 
ATOM   7544 C  CA  . ASP   D  1 193 ? 19.473  -17.077 21.743  1.00 23.24  0  208 ASP   D CA  1 
ATOM   7545 C  C   . ASP   D  1 193 ? 18.697  -15.846 22.224  1.00 23.88  0  208 ASP   D C   1 
ATOM   7546 O  O   . ASP   D  1 193 ? 18.627  -15.654 23.462  1.00 21.03  0  208 ASP   D O   1 
ATOM   7547 C  CB  . ASP   D  1 193 ? 20.970  -16.901 21.933  1.00 25.76  0  208 ASP   D CB  1 
ATOM   7548 C  CG  . ASP   D  1 193 ? 21.752  -18.174 21.684  1.00 24.27  0  208 ASP   D CG  1 
ATOM   7549 O  OD1 . ASP   D  1 193 ? 21.298  -19.225 22.148  1.00 25.70  0  208 ASP   D OD1 1 
ATOM   7550 O  OD2 . ASP   D  1 193 ? 22.830  -18.106 21.055  1.00 25.31  -1 208 ASP   D OD2 1 
ATOM   7551 N  N   . SER   D  1 194 ? 18.129  -15.059 21.306  1.00 21.61  0  209 SER   D N   1 
ATOM   7552 C  CA  . SER   D  1 194 ? 17.306  -13.848 21.585  1.00 21.15  0  209 SER   D CA  1 
ATOM   7553 C  C   . SER   D  1 194 ? 16.374  -14.097 22.749  1.00 21.04  0  209 SER   D C   1 
ATOM   7554 O  O   . SER   D  1 194 ? 15.674  -15.128 22.732  1.00 23.14  0  209 SER   D O   1 
ATOM   7555 C  CB  . SER   D  1 194 ? 16.511  -13.377 20.397  1.00 23.32  0  209 SER   D CB  1 
ATOM   7556 O  OG  . SER   D  1 194 ? 17.363  -12.717 19.467  1.00 29.80  0  209 SER   D OG  1 
ATOM   7557 N  N   . GLY   D  1 195 ? 16.301  -13.142 23.668  1.00 20.37  0  210 GLY   D N   1 
ATOM   7558 C  CA  . GLY   D  1 195 ? 15.369  -13.159 24.808  1.00 21.47  0  210 GLY   D CA  1 
ATOM   7559 C  C   . GLY   D  1 195 ? 15.923  -13.930 25.998  1.00 19.61  0  210 GLY   D C   1 
ATOM   7560 O  O   . GLY   D  1 195 ? 15.359  -13.793 27.080  1.00 21.49  0  210 GLY   D O   1 
ATOM   7561 N  N   . GLY   D  1 196 ? 16.969  -14.737 25.793  1.00 22.32  0  211 GLY   D N   1 
ATOM   7562 C  CA  . GLY   D  1 196 ? 17.611  -15.518 26.847  1.00 20.91  0  211 GLY   D CA  1 
ATOM   7563 C  C   . GLY   D  1 196 ? 18.453  -14.655 27.773  1.00 26.55  0  211 GLY   D C   1 
ATOM   7564 O  O   . GLY   D  1 196 ? 18.653  -13.458 27.544  1.00 26.60  0  211 GLY   D O   1 
ATOM   7565 N  N   . PRO   D  1 197 ? 18.959  -15.258 28.869  1.00 25.97  0  212 PRO   D N   1 
ATOM   7566 C  CA  . PRO   D  1 197 ? 19.653  -14.501 29.889  1.00 27.39  0  212 PRO   D CA  1 
ATOM   7567 C  C   . PRO   D  1 197 ? 21.172  -14.394 29.714  1.00 28.11  0  212 PRO   D C   1 
ATOM   7568 O  O   . PRO   D  1 197 ? 21.817  -15.352 29.309  1.00 27.95  0  212 PRO   D O   1 
ATOM   7569 C  CB  . PRO   D  1 197 ? 19.251  -15.286 31.134  1.00 26.61  0  212 PRO   D CB  1 
ATOM   7570 C  CG  . PRO   D  1 197 ? 19.228  -16.746 30.681  1.00 26.20  0  212 PRO   D CG  1 
ATOM   7571 C  CD  . PRO   D  1 197 ? 18.802  -16.685 29.229  1.00 28.89  0  212 PRO   D CD  1 
ATOM   7572 N  N   . LEU   D  1 198 ? 21.678  -13.199 30.024  1.00 27.07  0  213 LEU   D N   1 
ATOM   7573 C  CA  . LEU   D  1 198 ? 23.099  -12.972 30.388  1.00 28.33  0  213 LEU   D CA  1 
ATOM   7574 C  C   . LEU   D  1 198 ? 23.136  -12.846 31.924  1.00 25.48  0  213 LEU   D C   1 
ATOM   7575 O  O   . LEU   D  1 198 ? 22.472  -11.921 32.457  1.00 25.22  0  213 LEU   D O   1 
ATOM   7576 C  CB  . LEU   D  1 198 ? 23.615  -11.708 29.675  1.00 25.97  0  213 LEU   D CB  1 
ATOM   7577 C  CG  . LEU   D  1 198 ? 25.036  -11.284 30.063  1.00 27.49  0  213 LEU   D CG  1 
ATOM   7578 C  CD1 . LEU   D  1 198 ? 26.067  -12.272 29.549  1.00 29.75  0  213 LEU   D CD1 1 
ATOM   7579 C  CD2 . LEU   D  1 198 ? 25.356  -9.913  29.532  1.00 32.80  0  213 LEU   D CD2 1 
ATOM   7580 N  N   . VAL   D  1 199 ? 23.852  -13.748 32.594  1.00 26.00  0  214 VAL   D N   1 
ATOM   7581 C  CA  . VAL   D  1 199 ? 23.888  -13.838 34.081  1.00 25.85  0  214 VAL   D CA  1 
ATOM   7582 C  C   . VAL   D  1 199 ? 25.328  -13.650 34.564  1.00 28.90  0  214 VAL   D C   1 
ATOM   7583 O  O   . VAL   D  1 199 ? 26.262  -14.167 33.944  1.00 28.31  0  214 VAL   D O   1 
ATOM   7584 C  CB  . VAL   D  1 199 ? 23.261  -15.150 34.594  1.00 27.86  0  214 VAL   D CB  1 
ATOM   7585 C  CG1 . VAL   D  1 199 ? 21.782  -15.177 34.315  1.00 27.95  0  214 VAL   D CG1 1 
ATOM   7586 C  CG2 . VAL   D  1 199 ? 23.924  -16.413 34.014  1.00 28.72  0  214 VAL   D CG2 1 
ATOM   7587 N  N   . CYS   D  1 200 ? 25.514  -12.866 35.621  1.00 32.41  0  215 CYS   D N   1 
ATOM   7588 C  CA  . CYS   D  1 200 ? 26.857  -12.651 36.251  1.00 35.38  0  215 CYS   D CA  1 
ATOM   7589 C  C   . CYS   D  1 200 ? 26.745  -13.009 37.735  1.00 32.66  0  215 CYS   D C   1 
ATOM   7590 O  O   . CYS   D  1 200 ? 25.709  -12.673 38.366  1.00 29.45  0  215 CYS   D O   1 
ATOM   7591 C  CB  . CYS   D  1 200 ? 27.366  -11.213 36.108  1.00 35.22  0  215 CYS   D CB  1 
ATOM   7592 S  SG  . CYS   D  1 200 ? 27.172  -10.532 34.440  1.00 37.97  0  215 CYS   D SG  1 
ATOM   7593 N  N   . LYS   D  1 201 ? 27.743  -13.717 38.248  1.00 40.31  0  216 LYS   D N   1 
ATOM   7594 C  CA  . LYS   D  1 201 ? 27.802  -14.161 39.668  1.00 44.83  0  216 LYS   D CA  1 
ATOM   7595 C  C   . LYS   D  1 201 ? 28.417  -13.014 40.474  1.00 39.51  0  216 LYS   D C   1 
ATOM   7596 O  O   . LYS   D  1 201 ? 29.583  -12.687 40.209  1.00 40.25  0  216 LYS   D O   1 
ATOM   7597 C  CB  . LYS   D  1 201 ? 28.594  -15.474 39.818  1.00 44.84  0  216 LYS   D CB  1 
ATOM   7598 C  CG  . LYS   D  1 201 ? 28.298  -16.246 41.110  1.00 48.62  0  216 LYS   D CG  1 
ATOM   7599 C  CD  . LYS   D  1 201 ? 28.968  -17.627 41.221  1.00 54.58  0  216 LYS   D CD  1 
ATOM   7600 C  CE  . LYS   D  1 201 ? 28.852  -18.335 42.524  0.00 54.04  0  216 LYS   D CE  1 
ATOM   7601 N  NZ  . LYS   D  1 201 ? 27.513  -18.954 42.657  0.00 54.15  1  216 LYS   D NZ  1 
ATOM   7602 N  N   . VAL   D  1 202 ? 27.636  -12.378 41.346  1.00 38.70  0  217 VAL   D N   1 
ATOM   7603 C  CA  . VAL   D  1 202 ? 28.072  -11.210 42.170  1.00 38.94  0  217 VAL   D CA  1 
ATOM   7604 C  C   . VAL   D  1 202 ? 27.859  -11.576 43.646  1.00 38.12  0  217 VAL   D C   1 
ATOM   7605 O  O   . VAL   D  1 202 ? 26.700  -11.871 44.012  1.00 38.39  0  217 VAL   D O   1 
ATOM   7606 C  CB  . VAL   D  1 202 ? 27.294  -9.937  41.803  1.00 40.59  0  217 VAL   D CB  1 
ATOM   7607 C  CG1 . VAL   D  1 202 ? 27.731  -8.740  42.641  1.00 42.52  0  217 VAL   D CG1 1 
ATOM   7608 C  CG2 . VAL   D  1 202 ? 27.386  -9.621  40.319  1.00 41.64  0  217 VAL   D CG2 1 
ATOM   7609 N  N   . ASN   D  1 203 ? 28.931  -11.576 44.454  1.00 43.74  0  218 ASN   D N   1 
ATOM   7610 C  CA  . ASN   D  1 203 ? 28.913  -11.904 45.919  1.00 42.68  0  218 ASN   D CA  1 
ATOM   7611 C  C   . ASN   D  1 203 ? 28.134  -13.216 46.123  1.00 42.90  0  218 ASN   D C   1 
ATOM   7612 O  O   . ASN   D  1 203 ? 27.197  -13.230 46.953  1.00 42.92  0  218 ASN   D O   1 
ATOM   7613 C  CB  . ASN   D  1 203 ? 28.376  -10.746 46.777  1.00 45.15  0  218 ASN   D CB  1 
ATOM   7614 C  CG  . ASN   D  1 203 ? 28.678  -10.881 48.269  0.00 45.14  0  218 ASN   D CG  1 
ATOM   7615 O  OD1 . ASN   D  1 203 ? 29.391  -11.783 48.706  0.00 45.27  0  218 ASN   D OD1 1 
ATOM   7616 N  ND2 . ASN   D  1 203 ? 28.115  -9.982  49.060  0.00 45.11  0  218 ASN   D ND2 1 
ATOM   7617 N  N   . GLY   D  1 204 ? 28.484  -14.243 45.328  1.00 46.21  0  219 GLY   D N   1 
ATOM   7618 C  CA  . GLY   D  1 204 ? 27.943  -15.616 45.346  1.00 45.60  0  219 GLY   D CA  1 
ATOM   7619 C  C   . GLY   D  1 204 ? 26.497  -15.740 44.882  1.00 49.52  0  219 GLY   D C   1 
ATOM   7620 O  O   . GLY   D  1 204 ? 25.958  -16.845 45.052  1.00 46.15  0  219 GLY   D O   1 
ATOM   7621 N  N   . THR   D  1 205 ? 25.856  -14.687 44.342  1.00 46.16  0  220 THR   D N   1 
ATOM   7622 C  CA  . THR   D  1 205 ? 24.489  -14.805 43.771  1.00 43.46  0  220 THR   D CA  1 
ATOM   7623 C  C   . THR   D  1 205 ? 24.548  -14.594 42.261  1.00 39.56  0  220 THR   D C   1 
ATOM   7624 O  O   . THR   D  1 205 ? 25.277  -13.683 41.798  1.00 33.27  0  220 THR   D O   1 
ATOM   7625 C  CB  . THR   D  1 205 ? 23.521  -13.858 44.473  1.00 46.63  0  220 THR   D CB  1 
ATOM   7626 O  OG1 . THR   D  1 205 ? 23.544  -14.308 45.825  1.00 46.51  0  220 THR   D OG1 1 
ATOM   7627 C  CG2 . THR   D  1 205 ? 22.100  -13.901 43.948  1.00 46.41  0  220 THR   D CG2 1 
ATOM   7628 N  N   . TRP   D  1 206 ? 23.792  -15.398 41.519  1.00 36.44  0  221 TRP   D N   1 
ATOM   7629 C  CA  . TRP   D  1 206 ? 23.633  -15.196 40.053  1.00 32.44  0  221 TRP   D CA  1 
ATOM   7630 C  C   . TRP   D  1 206 ? 22.623  -14.077 39.836  1.00 28.98  0  221 TRP   D C   1 
ATOM   7631 O  O   . TRP   D  1 206 ? 21.490  -14.221 40.360  1.00 30.52  0  221 TRP   D O   1 
ATOM   7632 C  CB  . TRP   D  1 206 ? 23.203  -16.479 39.350  1.00 36.26  0  221 TRP   D CB  1 
ATOM   7633 C  CG  . TRP   D  1 206 ? 24.308  -17.476 39.208  1.00 34.62  0  221 TRP   D CG  1 
ATOM   7634 C  CD1 . TRP   D  1 206 ? 24.425  -18.643 39.902  1.00 37.29  0  221 TRP   D CD1 1 
ATOM   7635 C  CD2 . TRP   D  1 206 ? 25.426  -17.416 38.304  1.00 33.58  0  221 TRP   D CD2 1 
ATOM   7636 N  NE1 . TRP   D  1 206 ? 25.556  -19.305 39.513  1.00 37.31  0  221 TRP   D NE1 1 
ATOM   7637 C  CE2 . TRP   D  1 206 ? 26.183  -18.589 38.522  1.00 36.52  0  221 TRP   D CE2 1 
ATOM   7638 C  CE3 . TRP   D  1 206 ? 25.871  -16.497 37.344  1.00 32.92  0  221 TRP   D CE3 1 
ATOM   7639 C  CZ2 . TRP   D  1 206 ? 27.370  -18.847 37.842  1.00 35.20  0  221 TRP   D CZ2 1 
ATOM   7640 C  CZ3 . TRP   D  1 206 ? 27.020  -16.771 36.642  1.00 33.74  0  221 TRP   D CZ3 1 
ATOM   7641 C  CH2 . TRP   D  1 206 ? 27.784  -17.907 36.923  1.00 37.67  0  221 TRP   D CH2 1 
ATOM   7642 N  N   . LEU   D  1 207 ? 23.031  -13.000 39.147  1.00 28.19  0  222 LEU   D N   1 
ATOM   7643 C  CA  . LEU   D  1 207 ? 22.143  -11.850 38.785  1.00 30.02  0  222 LEU   D CA  1 
ATOM   7644 C  C   . LEU   D  1 207 ? 21.936  -11.816 37.272  1.00 26.34  0  222 LEU   D C   1 
ATOM   7645 O  O   . LEU   D  1 207 ? 22.940  -11.931 36.515  1.00 26.79  0  222 LEU   D O   1 
ATOM   7646 C  CB  . LEU   D  1 207 ? 22.774  -10.535 39.287  1.00 33.17  0  222 LEU   D CB  1 
ATOM   7647 C  CG  . LEU   D  1 207 ? 23.063  -10.457 40.788  1.00 32.92  0  222 LEU   D CG  1 
ATOM   7648 C  CD1 . LEU   D  1 207 ? 23.586  -9.070  41.174  1.00 31.04  0  222 LEU   D CD1 1 
ATOM   7649 C  CD2 . LEU   D  1 207 ? 21.820  -10.794 41.603  1.00 33.43  0  222 LEU   D CD2 1 
ATOM   7650 N  N   . GLN   D  1 208 ? 20.709  -11.595 36.815  1.00 24.48  0  223 GLN   D N   1 
ATOM   7651 C  CA  . GLN   D  1 208 ? 20.513  -11.360 35.363  1.00 24.59  0  223 GLN   D CA  1 
ATOM   7652 C  C   . GLN   D  1 208 ? 20.867  -9.913  35.005  1.00 24.45  0  223 GLN   D C   1 
ATOM   7653 O  O   . GLN   D  1 208 ? 20.032  -9.025  35.185  1.00 27.22  0  223 GLN   D O   1 
ATOM   7654 C  CB  . GLN   D  1 208 ? 19.108  -11.715 34.899  1.00 25.14  0  223 GLN   D CB  1 
ATOM   7655 C  CG  . GLN   D  1 208 ? 19.045  -11.772 33.373  1.00 24.46  0  223 GLN   D CG  1 
ATOM   7656 C  CD  . GLN   D  1 208 ? 17.791  -12.369 32.788  1.00 24.02  0  223 GLN   D CD  1 
ATOM   7657 O  OE1 . GLN   D  1 208 ? 16.995  -13.055 33.459  1.00 23.87  0  223 GLN   D OE1 1 
ATOM   7658 N  NE2 . GLN   D  1 208 ? 17.635  -12.102 31.508  1.00 21.07  0  223 GLN   D NE2 1 
ATOM   7659 N  N   . ALA   D  1 209 ? 22.024  -9.717  34.383  1.00 25.99  0  224 ALA   D N   1 
ATOM   7660 C  CA  . ALA   D  1 209 ? 22.497  -8.420  33.855  1.00 26.66  0  224 ALA   D CA  1 
ATOM   7661 C  C   . ALA   D  1 209 ? 21.776  -8.011  32.554  1.00 25.99  0  224 ALA   D C   1 
ATOM   7662 O  O   . ALA   D  1 209 ? 21.574  -6.803  32.321  1.00 25.91  0  224 ALA   D O   1 
ATOM   7663 C  CB  . ALA   D  1 209 ? 23.991  -8.538  33.638  1.00 27.53  0  224 ALA   D CB  1 
ATOM   7664 N  N   . GLY   D  1 210 ? 21.466  -8.972  31.694  1.00 26.04  0  225 GLY   D N   1 
ATOM   7665 C  CA  . GLY   D  1 210 ? 21.100  -8.717  30.287  1.00 25.64  0  225 GLY   D CA  1 
ATOM   7666 C  C   . GLY   D  1 210 ? 20.027  -9.651  29.749  1.00 26.13  0  225 GLY   D C   1 
ATOM   7667 O  O   . GLY   D  1 210 ? 19.917  -10.807 30.216  1.00 24.47  0  225 GLY   D O   1 
ATOM   7668 N  N   . VAL   D  1 211 ? 19.308  -9.186  28.742  1.00 25.98  0  226 VAL   D N   1 
ATOM   7669 C  CA  . VAL   D  1 211 ? 18.478  -10.013 27.822  1.00 23.36  0  226 VAL   D CA  1 
ATOM   7670 C  C   . VAL   D  1 211 ? 19.154  -10.007 26.438  1.00 24.06  0  226 VAL   D C   1 
ATOM   7671 O  O   . VAL   D  1 211 ? 19.491  -8.925  25.964  1.00 21.84  0  226 VAL   D O   1 
ATOM   7672 C  CB  . VAL   D  1 211 ? 17.062  -9.428  27.768  1.00 24.56  0  226 VAL   D CB  1 
ATOM   7673 C  CG1 . VAL   D  1 211 ? 16.194  -10.157 26.768  1.00 25.25  0  226 VAL   D CG1 1 
ATOM   7674 C  CG2 . VAL   D  1 211 ? 16.378  -9.400  29.136  1.00 25.19  0  226 VAL   D CG2 1 
ATOM   7675 N  N   . VAL   D  1 212 ? 19.380  -11.167 25.820  1.00 23.93  0  227 VAL   D N   1 
ATOM   7676 C  CA  . VAL   D  1 212 ? 19.978  -11.289 24.455  1.00 22.66  0  227 VAL   D CA  1 
ATOM   7677 C  C   . VAL   D  1 212 ? 19.120  -10.481 23.492  1.00 22.09  0  227 VAL   D C   1 
ATOM   7678 O  O   . VAL   D  1 212 ? 17.903  -10.747 23.405  1.00 20.62  0  227 VAL   D O   1 
ATOM   7679 C  CB  . VAL   D  1 212 ? 20.125  -12.749 23.987  1.00 24.58  0  227 VAL   D CB  1 
ATOM   7680 C  CG1 . VAL   D  1 212 ? 20.653  -12.832 22.557  1.00 27.95  0  227 VAL   D CG1 1 
ATOM   7681 C  CG2 . VAL   D  1 212 ? 21.075  -13.509 24.897  1.00 25.48  0  227 VAL   D CG2 1 
ATOM   7682 N  N   . SER   D  1 213 ? 19.698  -9.463  22.856  1.00 22.35  0  228 SER   D N   1 
ATOM   7683 C  CA  . SER   D  1 213 ? 18.916  -8.480  22.066  1.00 22.51  0  228 SER   D CA  1 
ATOM   7684 C  C   . SER   D  1 213 ? 19.346  -8.526  20.600  1.00 23.35  0  228 SER   D C   1 
ATOM   7685 O  O   . SER   D  1 213 ? 18.538  -9.003  19.774  1.00 23.13  0  228 SER   D O   1 
ATOM   7686 C  CB  . SER   D  1 213 ? 19.001  -7.081  22.645  1.00 22.75  0  228 SER   D CB  1 
ATOM   7687 O  OG  . SER   D  1 213 ? 18.075  -6.238  21.962  1.00 24.69  0  228 SER   D OG  1 
ATOM   7688 N  N   . TRP   D  1 214 ? 20.554  -8.050  20.278  1.00 21.86  0  229 TRP   D N   1 
ATOM   7689 C  CA  . TRP   D  1 214 ? 20.938  -7.868  18.856  1.00 23.31  0  229 TRP   D CA  1 
ATOM   7690 C  C   . TRP   D  1 214 ? 22.455  -7.785  18.705  1.00 23.87  0  229 TRP   D C   1 
ATOM   7691 O  O   . TRP   D  1 214 ? 23.204  -7.832  19.711  1.00 23.36  0  229 TRP   D O   1 
ATOM   7692 C  CB  . TRP   D  1 214 ? 20.233  -6.676  18.203  1.00 25.46  0  229 TRP   D CB  1 
ATOM   7693 C  CG  . TRP   D  1 214 ? 20.650  -5.331  18.717  1.00 27.06  0  229 TRP   D CG  1 
ATOM   7694 C  CD1 . TRP   D  1 214 ? 20.226  -4.727  19.868  1.00 26.55  0  229 TRP   D CD1 1 
ATOM   7695 C  CD2 . TRP   D  1 214 ? 21.535  -4.396  18.081  1.00 25.51  0  229 TRP   D CD2 1 
ATOM   7696 N  NE1 . TRP   D  1 214 ? 20.821  -3.505  20.013  1.00 27.61  0  229 TRP   D NE1 1 
ATOM   7697 C  CE2 . TRP   D  1 214 ? 21.624  -3.268  18.933  1.00 28.05  0  229 TRP   D CE2 1 
ATOM   7698 C  CE3 . TRP   D  1 214 ? 22.262  -4.393  16.890  1.00 30.62  0  229 TRP   D CE3 1 
ATOM   7699 C  CZ2 . TRP   D  1 214 ? 22.406  -2.152  18.624  1.00 28.60  0  229 TRP   D CZ2 1 
ATOM   7700 C  CZ3 . TRP   D  1 214 ? 23.057  -3.301  16.597  1.00 31.03  0  229 TRP   D CZ3 1 
ATOM   7701 C  CH2 . TRP   D  1 214 ? 23.114  -2.195  17.444  1.00 26.40  0  229 TRP   D CH2 1 
ATOM   7702 N  N   . GLY   D  1 215 ? 22.869  -7.735  17.449  1.00 22.98  0  230 GLY   D N   1 
ATOM   7703 C  CA  . GLY   D  1 215 ? 24.248  -7.449  17.049  1.00 24.64  0  230 GLY   D CA  1 
ATOM   7704 C  C   . GLY   D  1 215 ? 24.324  -7.440  15.549  1.00 26.25  0  230 GLY   D C   1 
ATOM   7705 O  O   . GLY   D  1 215 ? 23.301  -7.740  14.908  1.00 24.02  0  230 GLY   D O   1 
ATOM   7706 N  N   A GLU   D  1 216 ? 25.495  -7.121  15.001  0.50 27.62  0  231 GLU   D N   1 
ATOM   7707 N  N   B GLU   D  1 216 ? 25.486  -7.082  14.992  0.50 27.47  0  231 GLU   D N   1 
ATOM   7708 C  CA  A GLU   D  1 216 ? 25.773  -7.297  13.551  0.50 28.11  0  231 GLU   D CA  1 
ATOM   7709 C  CA  B GLU   D  1 216 ? 25.790  -7.317  13.553  0.50 27.88  0  231 GLU   D CA  1 
ATOM   7710 C  C   A GLU   D  1 216 ? 26.400  -8.687  13.393  0.50 28.71  0  231 GLU   D C   1 
ATOM   7711 C  C   B GLU   D  1 216 ? 26.399  -8.710  13.424  0.50 28.53  0  231 GLU   D C   1 
ATOM   7712 O  O   A GLU   D  1 216 ? 27.605  -8.871  13.756  0.50 28.68  0  231 GLU   D O   1 
ATOM   7713 O  O   B GLU   D  1 216 ? 27.606  -8.899  13.791  0.50 28.33  0  231 GLU   D O   1 
ATOM   7714 C  CB  A GLU   D  1 216 ? 26.595  -6.108  13.049  0.50 29.01  0  231 GLU   D CB  1 
ATOM   7715 C  CB  B GLU   D  1 216 ? 26.766  -6.306  12.958  0.50 28.52  0  231 GLU   D CB  1 
ATOM   7716 C  CG  A GLU   D  1 216 ? 25.776  -4.819  12.998  0.50 30.14  0  231 GLU   D CG  1 
ATOM   7717 C  CG  B GLU   D  1 216 ? 27.008  -6.568  11.477  0.50 30.60  0  231 GLU   D CG  1 
ATOM   7718 C  CD  A GLU   D  1 216 ? 26.485  -3.587  12.442  0.50 33.00  0  231 GLU   D CD  1 
ATOM   7719 C  CD  B GLU   D  1 216 ? 27.999  -5.631  10.814  0.50 28.69  0  231 GLU   D CD  1 
ATOM   7720 O  OE1 A GLU   D  1 216 ? 27.483  -3.767  11.720  0.50 33.99  0  231 GLU   D OE1 1 
ATOM   7721 O  OE1 B GLU   D  1 216 ? 27.945  -4.442  11.086  0.50 29.67  0  231 GLU   D OE1 1 
ATOM   7722 O  OE2 A GLU   D  1 216 ? 26.038  -2.449  12.737  0.50 31.16  -1 231 GLU   D OE2 1 
ATOM   7723 O  OE2 B GLU   D  1 216 ? 28.822  -6.101  10.060  0.50 31.50  -1 231 GLU   D OE2 1 
ATOM   7724 N  N   . GLY   D  1 217 ? 25.589  -9.656  12.956  1.00 28.14  0  232 GLY   D N   1 
ATOM   7725 C  CA  . GLY   D  1 217 ? 25.971  -11.081 12.949  1.00 29.55  0  232 GLY   D CA  1 
ATOM   7726 C  C   . GLY   D  1 217 ? 26.308  -11.545 14.358  1.00 28.88  0  232 GLY   D C   1 
ATOM   7727 O  O   . GLY   D  1 217 ? 25.784  -10.949 15.326  1.00 26.51  0  232 GLY   D O   1 
ATOM   7728 N  N   . CYS   D  1 218 ? 27.178  -12.552 14.462  1.00 27.69  0  233 CYS   D N   1 
ATOM   7729 C  CA  . CYS   D  1 218 ? 27.596  -13.203 15.722  1.00 27.99  0  233 CYS   D CA  1 
ATOM   7730 C  C   . CYS   D  1 218 ? 29.114  -13.374 15.679  1.00 30.17  0  233 CYS   D C   1 
ATOM   7731 O  O   . CYS   D  1 218 ? 29.620  -13.821 14.644  1.00 28.66  0  233 CYS   D O   1 
ATOM   7732 C  CB  . CYS   D  1 218 ? 26.913  -14.563 15.869  1.00 33.71  0  233 CYS   D CB  1 
ATOM   7733 S  SG  . CYS   D  1 218 ? 25.147  -14.513 15.463  1.00 39.47  0  233 CYS   D SG  1 
ATOM   7734 N  N   . ALA   D  1 219 ? 29.809  -12.983 16.748  1.00 29.65  0  234 ALA   D N   1 
ATOM   7735 C  CA  . ALA   D  1 219 ? 31.260  -13.150 16.927  1.00 31.06  0  234 ALA   D CA  1 
ATOM   7736 C  C   . ALA   D  1 219 ? 32.039  -12.514 15.764  1.00 32.45  0  234 ALA   D C   1 
ATOM   7737 O  O   . ALA   D  1 219 ? 33.076  -13.057 15.455  1.00 33.70  0  234 ALA   D O   1 
ATOM   7738 C  CB  . ALA   D  1 219 ? 31.553  -14.623 17.080  1.00 32.57  0  234 ALA   D CB  1 
ATOM   7739 N  N   . GLN   D  1 220 ? 31.558  -11.402 15.194  1.00 30.83  0  235 GLN   D N   1 
ATOM   7740 C  CA  . GLN   D  1 220 ? 32.219  -10.658 14.086  1.00 34.37  0  235 GLN   D CA  1 
ATOM   7741 C  C   . GLN   D  1 220 ? 33.200  -9.631  14.648  1.00 29.92  0  235 GLN   D C   1 
ATOM   7742 O  O   . GLN   D  1 220 ? 32.953  -9.056  15.697  1.00 29.80  0  235 GLN   D O   1 
ATOM   7743 C  CB  . GLN   D  1 220 ? 31.210  -9.946  13.181  1.00 37.77  0  235 GLN   D CB  1 
ATOM   7744 C  CG  . GLN   D  1 220 ? 30.272  -10.875 12.416  1.00 41.33  0  235 GLN   D CG  1 
ATOM   7745 C  CD  . GLN   D  1 220 ? 31.038  -11.697 11.413  1.00 44.27  0  235 GLN   D CD  1 
ATOM   7746 O  OE1 . GLN   D  1 220 ? 31.480  -12.806 11.697  1.00 48.58  0  235 GLN   D OE1 1 
ATOM   7747 N  NE2 . GLN   D  1 220 ? 31.281  -11.115 10.254  1.00 44.35  0  235 GLN   D NE2 1 
ATOM   7748 N  N   . PRO   D  1 221 ? 34.336  -9.366  13.957  1.00 34.19  0  236 PRO   D N   1 
ATOM   7749 C  CA  . PRO   D  1 221 ? 35.290  -8.331  14.359  1.00 31.71  0  236 PRO   D CA  1 
ATOM   7750 C  C   . PRO   D  1 221 ? 34.619  -6.971  14.582  1.00 30.03  0  236 PRO   D C   1 
ATOM   7751 O  O   . PRO   D  1 221 ? 33.831  -6.575  13.741  1.00 28.12  0  236 PRO   D O   1 
ATOM   7752 C  CB  . PRO   D  1 221 ? 36.341  -8.262  13.234  1.00 34.14  0  236 PRO   D CB  1 
ATOM   7753 C  CG  . PRO   D  1 221 ? 35.930  -9.253  12.183  1.00 37.71  0  236 PRO   D CG  1 
ATOM   7754 C  CD  . PRO   D  1 221 ? 34.783  -10.069 12.741  1.00 38.93  0  236 PRO   D CD  1 
ATOM   7755 N  N   . ASN   D  1 222 ? 34.901  -6.345  15.738  1.00 31.40  0  237 ASN   D N   1 
ATOM   7756 C  CA  . ASN   D  1 222 ? 34.423  -4.987  16.121  1.00 33.57  0  237 ASN   D CA  1 
ATOM   7757 C  C   . ASN   D  1 222 ? 32.898  -4.946  16.260  1.00 31.53  0  237 ASN   D C   1 
ATOM   7758 O  O   . ASN   D  1 222 ? 32.338  -3.833  16.141  1.00 28.07  0  237 ASN   D O   1 
ATOM   7759 C  CB  . ASN   D  1 222 ? 34.885  -3.917  15.115  1.00 33.42  0  237 ASN   D CB  1 
ATOM   7760 C  CG  . ASN   D  1 222 ? 36.379  -3.729  15.155  1.00 35.38  0  237 ASN   D CG  1 
ATOM   7761 O  OD1 . ASN   D  1 222 ? 37.015  -3.530  14.119  1.00 40.98  0  237 ASN   D OD1 1 
ATOM   7762 N  ND2 . ASN   D  1 222 ? 36.933  -3.704  16.345  1.00 32.81  0  237 ASN   D ND2 1 
ATOM   7763 N  N   . ARG   D  1 223 ? 32.236  -6.074  16.541  1.00 31.89  0  238 ARG   D N   1 
ATOM   7764 C  CA  . ARG   D  1 223 ? 30.757  -6.118  16.648  1.00 28.33  0  238 ARG   D CA  1 
ATOM   7765 C  C   . ARG   D  1 223 ? 30.373  -7.030  17.809  1.00 31.29  0  238 ARG   D C   1 
ATOM   7766 O  O   . ARG   D  1 223 ? 29.800  -8.113  17.628  1.00 30.10  0  238 ARG   D O   1 
ATOM   7767 C  CB  . ARG   D  1 223 ? 30.161  -6.562  15.312  1.00 27.59  0  238 ARG   D CB  1 
ATOM   7768 C  CG  . ARG   D  1 223 ? 30.482  -5.682  14.108  1.00 28.75  0  238 ARG   D CG  1 
ATOM   7769 C  CD  . ARG   D  1 223 ? 29.806  -4.312  14.219  1.00 28.14  0  238 ARG   D CD  1 
ATOM   7770 N  NE  . ARG   D  1 223 ? 29.985  -3.538  13.027  1.00 29.99  0  238 ARG   D NE  1 
ATOM   7771 C  CZ  . ARG   D  1 223 ? 30.957  -2.653  12.773  1.00 31.76  0  238 ARG   D CZ  1 
ATOM   7772 N  NH1 . ARG   D  1 223 ? 31.939  -2.429  13.639  1.00 28.12  1  238 ARG   D NH1 1 
ATOM   7773 N  NH2 . ARG   D  1 223 ? 30.942  -2.029  11.596  1.00 27.69  0  238 ARG   D NH2 1 
ATOM   7774 N  N   . PRO   D  1 224 ? 30.679  -6.634  19.057  1.00 31.13  0  239 PRO   D N   1 
ATOM   7775 C  CA  . PRO   D  1 224 ? 30.253  -7.434  20.201  1.00 27.96  0  239 PRO   D CA  1 
ATOM   7776 C  C   . PRO   D  1 224 ? 28.730  -7.560  20.302  1.00 25.53  0  239 PRO   D C   1 
ATOM   7777 O  O   . PRO   D  1 224 ? 28.012  -6.744  19.752  1.00 26.99  0  239 PRO   D O   1 
ATOM   7778 C  CB  . PRO   D  1 224 ? 30.792  -6.734  21.439  1.00 29.48  0  239 PRO   D CB  1 
ATOM   7779 C  CG  . PRO   D  1 224 ? 31.650  -5.583  20.944  1.00 29.61  0  239 PRO   D CG  1 
ATOM   7780 C  CD  . PRO   D  1 224 ? 31.454  -5.449  19.446  1.00 30.47  0  239 PRO   D CD  1 
ATOM   7781 N  N   . GLY   D  1 225 ? 28.279  -8.592  21.015  1.00 26.21  0  240 GLY   D N   1 
ATOM   7782 C  CA  . GLY   D  1 225 ? 26.840  -8.816  21.259  1.00 26.24  0  240 GLY   D CA  1 
ATOM   7783 C  C   . GLY   D  1 225 ? 26.253  -7.690  22.096  1.00 22.41  0  240 GLY   D C   1 
ATOM   7784 O  O   . GLY   D  1 225 ? 26.898  -7.233  23.049  1.00 24.27  0  240 GLY   D O   1 
ATOM   7785 N  N   . ILE   D  1 226 ? 25.038  -7.291  21.783  1.00 24.40  0  241 ILE   D N   1 
ATOM   7786 C  CA  . ILE   D  1 226 ? 24.281  -6.257  22.529  1.00 26.30  0  241 ILE   D CA  1 
ATOM   7787 C  C   . ILE   D  1 226 ? 23.112  -6.923  23.270  1.00 25.42  0  241 ILE   D C   1 
ATOM   7788 O  O   . ILE   D  1 226 ? 22.436  -7.774  22.695  1.00 25.95  0  241 ILE   D O   1 
ATOM   7789 C  CB  . ILE   D  1 226 ? 23.801  -5.150  21.599  1.00 26.39  0  241 ILE   D CB  1 
ATOM   7790 C  CG1 . ILE   D  1 226 ? 24.882  -4.681  20.610  1.00 26.60  0  241 ILE   D CG1 1 
ATOM   7791 C  CG2 . ILE   D  1 226 ? 23.272  -4.005  22.421  1.00 26.50  0  241 ILE   D CG2 1 
ATOM   7792 C  CD1 . ILE   D  1 226 ? 26.169  -4.255  21.270  1.00 28.49  0  241 ILE   D CD1 1 
ATOM   7793 N  N   . TYR   D  1 227 ? 22.896  -6.478  24.498  1.00 23.25  0  242 TYR   D N   1 
ATOM   7794 C  CA  . TYR   D  1 227 ? 21.891  -7.017  25.448  1.00 28.97  0  242 TYR   D CA  1 
ATOM   7795 C  C   . TYR   D  1 227 ? 21.038  -5.865  25.943  1.00 26.31  0  242 TYR   D C   1 
ATOM   7796 O  O   . TYR   D  1 227 ? 21.601  -4.765  26.112  1.00 26.39  0  242 TYR   D O   1 
ATOM   7797 C  CB  . TYR   D  1 227 ? 22.633  -7.721  26.590  1.00 24.92  0  242 TYR   D CB  1 
ATOM   7798 C  CG  . TYR   D  1 227 ? 23.409  -8.922  26.139  1.00 24.52  0  242 TYR   D CG  1 
ATOM   7799 C  CD1 . TYR   D  1 227 ? 24.635  -8.800  25.495  1.00 23.92  0  242 TYR   D CD1 1 
ATOM   7800 C  CD2 . TYR   D  1 227 ? 22.936  -10.195 26.397  1.00 24.38  0  242 TYR   D CD2 1 
ATOM   7801 C  CE1 . TYR   D  1 227 ? 25.360  -9.913  25.109  1.00 26.30  0  242 TYR   D CE1 1 
ATOM   7802 C  CE2 . TYR   D  1 227 ? 23.643  -11.317 25.986  1.00 26.65  0  242 TYR   D CE2 1 
ATOM   7803 C  CZ  . TYR   D  1 227 ? 24.857  -11.183 25.343  1.00 26.43  0  242 TYR   D CZ  1 
ATOM   7804 O  OH  . TYR   D  1 227 ? 25.534  -12.290 24.930  1.00 29.21  0  242 TYR   D OH  1 
ATOM   7805 N  N   . THR   D  1 228 ? 19.767  -6.106  26.240  1.00 26.38  0  243 THR   D N   1 
ATOM   7806 C  CA  . THR   D  1 228 ? 18.971  -5.151  27.024  1.00 26.08  0  243 THR   D CA  1 
ATOM   7807 C  C   . THR   D  1 228 ? 19.538  -5.132  28.442  1.00 24.89  0  243 THR   D C   1 
ATOM   7808 O  O   . THR   D  1 228 ? 19.735  -6.216  28.988  1.00 26.50  0  243 THR   D O   1 
ATOM   7809 C  CB  . THR   D  1 228 ? 17.484  -5.485  26.974  1.00 26.75  0  243 THR   D CB  1 
ATOM   7810 O  OG1 . THR   D  1 228 ? 17.125  -5.740  25.614  1.00 25.54  0  243 THR   D OG1 1 
ATOM   7811 C  CG2 . THR   D  1 228 ? 16.652  -4.365  27.545  1.00 25.82  0  243 THR   D CG2 1 
ATOM   7812 N  N   . ARG   D  1 229 ? 19.840  -3.952  28.985  1.00 23.39  0  244 ARG   D N   1 
ATOM   7813 C  CA  . ARG   D  1 229 ? 20.387  -3.769  30.356  1.00 24.92  0  244 ARG   D CA  1 
ATOM   7814 C  C   . ARG   D  1 229 ? 19.231  -3.859  31.370  1.00 24.63  0  244 ARG   D C   1 
ATOM   7815 O  O   . ARG   D  1 229 ? 18.345  -2.973  31.394  1.00 22.37  0  244 ARG   D O   1 
ATOM   7816 C  CB  . ARG   D  1 229 ? 21.169  -2.459  30.423  1.00 27.60  0  244 ARG   D CB  1 
ATOM   7817 C  CG  . ARG   D  1 229 ? 21.833  -2.181  31.764  1.00 28.72  0  244 ARG   D CG  1 
ATOM   7818 C  CD  . ARG   D  1 229 ? 22.552  -0.828  31.787  1.00 28.68  0  244 ARG   D CD  1 
ATOM   7819 N  NE  . ARG   D  1 229 ? 23.775  -0.919  31.017  1.00 28.63  0  244 ARG   D NE  1 
ATOM   7820 C  CZ  . ARG   D  1 229 ? 24.939  -1.428  31.433  1.00 27.52  0  244 ARG   D CZ  1 
ATOM   7821 N  NH1 . ARG   D  1 229 ? 25.090  -1.888  32.667  1.00 27.70  1  244 ARG   D NH1 1 
ATOM   7822 N  NH2 . ARG   D  1 229 ? 25.975  -1.438  30.602  1.00 28.02  0  244 ARG   D NH2 1 
ATOM   7823 N  N   . VAL   D  1 230 ? 19.194  -4.933  32.153  1.00 27.31  0  245 VAL   D N   1 
ATOM   7824 C  CA  . VAL   D  1 230 ? 18.024  -5.232  33.021  1.00 26.27  0  245 VAL   D CA  1 
ATOM   7825 C  C   . VAL   D  1 230 ? 17.852  -4.101  34.047  1.00 27.17  0  245 VAL   D C   1 
ATOM   7826 O  O   . VAL   D  1 230 ? 16.680  -3.704  34.288  1.00 25.78  0  245 VAL   D O   1 
ATOM   7827 C  CB  . VAL   D  1 230 ? 18.103  -6.626  33.659  1.00 27.40  0  245 VAL   D CB  1 
ATOM   7828 C  CG1 . VAL   D  1 230 ? 17.018  -6.827  34.725  1.00 28.57  0  245 VAL   D CG1 1 
ATOM   7829 C  CG2 . VAL   D  1 230 ? 17.977  -7.725  32.585  1.00 30.96  0  245 VAL   D CG2 1 
ATOM   7830 N  N   . THR   D  1 231 ? 18.934  -3.578  34.617  1.00 25.80  0  246 THR   D N   1 
ATOM   7831 C  CA  . THR   D  1 231 ? 18.818  -2.530  35.674  1.00 26.36  0  246 THR   D CA  1 
ATOM   7832 C  C   . THR   D  1 231 ? 18.001  -1.365  35.165  1.00 27.94  0  246 THR   D C   1 
ATOM   7833 O  O   . THR   D  1 231 ? 17.292  -0.780  35.971  1.00 32.65  0  246 THR   D O   1 
ATOM   7834 C  CB  . THR   D  1 231 ? 20.168  -2.027  36.179  1.00 29.79  0  246 THR   D CB  1 
ATOM   7835 O  OG1 . THR   D  1 231 ? 20.941  -1.638  35.033  1.00 26.21  0  246 THR   D OG1 1 
ATOM   7836 C  CG2 . THR   D  1 231 ? 20.841  -3.094  37.029  1.00 30.34  0  246 THR   D CG2 1 
ATOM   7837 N  N   . TYR   D  1 232 ? 18.063  -1.063  33.866  1.00 26.41  0  247 TYR   D N   1 
ATOM   7838 C  CA  . TYR   D  1 232 ? 17.352  0.104   33.279  1.00 27.56  0  247 TYR   D CA  1 
ATOM   7839 C  C   . TYR   D  1 232 ? 15.834  -0.035  33.415  1.00 26.75  0  247 TYR   D C   1 
ATOM   7840 O  O   . TYR   D  1 232 ? 15.154  0.977   33.466  1.00 25.77  0  247 TYR   D O   1 
ATOM   7841 C  CB  . TYR   D  1 232 ? 17.755  0.306   31.815  1.00 29.32  0  247 TYR   D CB  1 
ATOM   7842 C  CG  . TYR   D  1 232 ? 17.484  1.691   31.296  1.00 32.81  0  247 TYR   D CG  1 
ATOM   7843 C  CD1 . TYR   D  1 232 ? 16.215  2.033   30.829  1.00 32.71  0  247 TYR   D CD1 1 
ATOM   7844 C  CD2 . TYR   D  1 232 ? 18.483  2.663   31.257  1.00 30.75  0  247 TYR   D CD2 1 
ATOM   7845 C  CE1 . TYR   D  1 232 ? 15.933  3.296   30.332  1.00 30.90  0  247 TYR   D CE1 1 
ATOM   7846 C  CE2 . TYR   D  1 232 ? 18.220  3.926   30.754  1.00 29.69  0  247 TYR   D CE2 1 
ATOM   7847 C  CZ  . TYR   D  1 232 ? 16.941  4.245   30.306  1.00 36.06  0  247 TYR   D CZ  1 
ATOM   7848 O  OH  . TYR   D  1 232 ? 16.638  5.473   29.784  1.00 40.70  0  247 TYR   D OH  1 
ATOM   7849 N  N   . TYR   D  1 233 ? 15.299  -1.259  33.410  1.00 27.59  0  248 TYR   D N   1 
ATOM   7850 C  CA  . TYR   D  1 233 ? 13.840  -1.539  33.280  1.00 28.18  0  248 TYR   D CA  1 
ATOM   7851 C  C   . TYR   D  1 233 ? 13.240  -2.154  34.577  1.00 27.90  0  248 TYR   D C   1 
ATOM   7852 O  O   . TYR   D  1 233 ? 12.089  -2.644  34.541  1.00 27.81  0  248 TYR   D O   1 
ATOM   7853 C  CB  . TYR   D  1 233 ? 13.625  -2.375  32.006  1.00 27.62  0  248 TYR   D CB  1 
ATOM   7854 C  CG  . TYR   D  1 233 ? 13.922  -1.600  30.737  1.00 25.73  0  248 TYR   D CG  1 
ATOM   7855 C  CD1 . TYR   D  1 233 ? 13.091  -0.559  30.374  1.00 26.47  0  248 TYR   D CD1 1 
ATOM   7856 C  CD2 . TYR   D  1 233 ? 15.093  -1.776  30.011  1.00 25.58  0  248 TYR   D CD2 1 
ATOM   7857 C  CE1 . TYR   D  1 233 ? 13.346  0.229   29.268  1.00 27.38  0  248 TYR   D CE1 1 
ATOM   7858 C  CE2 . TYR   D  1 233 ? 15.380  -0.987  28.901  1.00 27.18  0  248 TYR   D CE2 1 
ATOM   7859 C  CZ  . TYR   D  1 233 ? 14.511  0.033   28.545  1.00 27.93  0  248 TYR   D CZ  1 
ATOM   7860 O  OH  . TYR   D  1 233 ? 14.723  0.834   27.478  1.00 25.82  0  248 TYR   D OH  1 
ATOM   7861 N  N   . LEU   D  1 234 ? 13.946  -2.086  35.709  1.00 28.96  0  249 LEU   D N   1 
ATOM   7862 C  CA  . LEU   D  1 234 ? 13.483  -2.670  37.008  1.00 30.60  0  249 LEU   D CA  1 
ATOM   7863 C  C   . LEU   D  1 234 ? 12.124  -2.112  37.404  1.00 30.94  0  249 LEU   D C   1 
ATOM   7864 O  O   . LEU   D  1 234 ? 11.242  -2.917  37.737  1.00 28.78  0  249 LEU   D O   1 
ATOM   7865 C  CB  . LEU   D  1 234 ? 14.517  -2.479  38.124  1.00 34.03  0  249 LEU   D CB  1 
ATOM   7866 C  CG  . LEU   D  1 234 ? 15.762  -3.360  38.021  1.00 33.10  0  249 LEU   D CG  1 
ATOM   7867 C  CD1 . LEU   D  1 234 ? 16.853  -2.890  38.968  1.00 35.93  0  249 LEU   D CD1 1 
ATOM   7868 C  CD2 . LEU   D  1 234 ? 15.437  -4.830  38.280  1.00 34.26  0  249 LEU   D CD2 1 
ATOM   7869 N  N   . ASP   D  1 235 ? 11.928  -0.802  37.324  1.00 33.81  0  250 ASP   D N   1 
ATOM   7870 C  CA  . ASP   D  1 235 ? 10.653  -0.171  37.757  1.00 33.91  0  250 ASP   D CA  1 
ATOM   7871 C  C   . ASP   D  1 235 ? 9.506   -0.674  36.881  1.00 31.34  0  250 ASP   D C   1 
ATOM   7872 O  O   . ASP   D  1 235 ? 8.431   -0.946  37.425  1.00 31.28  0  250 ASP   D O   1 
ATOM   7873 C  CB  . ASP   D  1 235 ? 10.694  1.361   37.692  1.00 41.06  0  250 ASP   D CB  1 
ATOM   7874 C  CG  . ASP   D  1 235 ? 11.758  1.972   38.593  1.00 46.66  0  250 ASP   D CG  1 
ATOM   7875 O  OD1 . ASP   D  1 235 ? 12.188  1.265   39.522  1.00 49.97  0  250 ASP   D OD1 1 
ATOM   7876 O  OD2 . ASP   D  1 235 ? 12.173  3.139   38.341  1.00 49.99  -1 250 ASP   D OD2 1 
ATOM   7877 N  N   . TRP   D  1 236 ? 9.725   -0.790  35.570  1.00 28.35  0  251 TRP   D N   1 
ATOM   7878 C  CA  . TRP   D  1 236 ? 8.731   -1.361  34.626  1.00 26.40  0  251 TRP   D CA  1 
ATOM   7879 C  C   . TRP   D  1 236 ? 8.445   -2.838  34.987  1.00 24.26  0  251 TRP   D C   1 
ATOM   7880 O  O   . TRP   D  1 236 ? 7.261   -3.213  35.095  1.00 23.21  0  251 TRP   D O   1 
ATOM   7881 C  CB  . TRP   D  1 236 ? 9.204   -1.196  33.172  1.00 28.07  0  251 TRP   D CB  1 
ATOM   7882 C  CG  . TRP   D  1 236 ? 8.237   -1.772  32.190  1.00 27.94  0  251 TRP   D CG  1 
ATOM   7883 C  CD1 . TRP   D  1 236 ? 7.096   -1.197  31.727  1.00 25.81  0  251 TRP   D CD1 1 
ATOM   7884 C  CD2 . TRP   D  1 236 ? 8.313   -3.073  31.583  1.00 27.90  0  251 TRP   D CD2 1 
ATOM   7885 N  NE1 . TRP   D  1 236 ? 6.451   -2.050  30.868  1.00 26.60  0  251 TRP   D NE1 1 
ATOM   7886 C  CE2 . TRP   D  1 236 ? 7.184   -3.199  30.743  1.00 29.17  0  251 TRP   D CE2 1 
ATOM   7887 C  CE3 . TRP   D  1 236 ? 9.219   -4.131  31.668  1.00 29.38  0  251 TRP   D CE3 1 
ATOM   7888 C  CZ2 . TRP   D  1 236 ? 6.949   -4.342  29.971  1.00 29.00  0  251 TRP   D CZ2 1 
ATOM   7889 C  CZ3 . TRP   D  1 236 ? 9.007   -5.252  30.881  1.00 30.41  0  251 TRP   D CZ3 1 
ATOM   7890 C  CH2 . TRP   D  1 236 ? 7.861   -5.371  30.081  1.00 30.95  0  251 TRP   D CH2 1 
ATOM   7891 N  N   . ILE   D  1 237 ? 9.469   -3.656  35.181  1.00 25.18  0  252 ILE   D N   1 
ATOM   7892 C  CA  . ILE   D  1 237 ? 9.274   -5.086  35.577  1.00 27.58  0  252 ILE   D CA  1 
ATOM   7893 C  C   . ILE   D  1 237 ? 8.424   -5.123  36.874  1.00 31.41  0  252 ILE   D C   1 
ATOM   7894 O  O   . ILE   D  1 237 ? 7.387   -5.822  36.892  1.00 31.43  0  252 ILE   D O   1 
ATOM   7895 C  CB  . ILE   D  1 237 ? 10.629  -5.817  35.717  1.00 26.95  0  252 ILE   D CB  1 
ATOM   7896 C  CG1 . ILE   D  1 237 ? 11.363  -5.971  34.382  1.00 26.22  0  252 ILE   D CG1 1 
ATOM   7897 C  CG2 . ILE   D  1 237 ? 10.455  -7.175  36.394  1.00 28.14  0  252 ILE   D CG2 1 
ATOM   7898 C  CD1 . ILE   D  1 237 ? 12.836  -6.347  34.523  1.00 24.41  0  252 ILE   D CD1 1 
ATOM   7899 N  N   . HIS   D  1 238 ? 8.796   -4.336  37.892  1.00 33.28  0  253 HIS   D N   1 
ATOM   7900 C  CA  . HIS   D  1 238 ? 8.148   -4.333  39.237  1.00 32.92  0  253 HIS   D CA  1 
ATOM   7901 C  C   . HIS   D  1 238 ? 6.723   -3.780  39.174  1.00 31.78  0  253 HIS   D C   1 
ATOM   7902 O  O   . HIS   D  1 238 ? 5.952   -4.051  40.109  1.00 31.57  0  253 HIS   D O   1 
ATOM   7903 C  CB  . HIS   D  1 238 ? 9.040   -3.644  40.275  1.00 33.69  0  253 HIS   D CB  1 
ATOM   7904 C  CG  . HIS   D  1 238 ? 10.283  -4.425  40.596  1.00 41.42  0  253 HIS   D CG  1 
ATOM   7905 N  ND1 . HIS   D  1 238 ? 10.325  -5.822  40.549  1.00 47.13  0  253 HIS   D ND1 1 
ATOM   7906 C  CD2 . HIS   D  1 238 ? 11.532  -4.019  40.942  1.00 42.83  0  253 HIS   D CD2 1 
ATOM   7907 C  CE1 . HIS   D  1 238 ? 11.547  -6.233  40.846  1.00 43.99  0  253 HIS   D CE1 1 
ATOM   7908 N  NE2 . HIS   D  1 238 ? 12.312  -5.145  41.074  1.00 43.75  0  253 HIS   D NE2 1 
ATOM   7909 N  N   . HIS   D  1 239 ? 6.319   -3.100  38.111  1.00 30.33  0  254 HIS   D N   1 
ATOM   7910 C  CA  . HIS   D  1 239 ? 4.885   -2.786  37.887  1.00 31.32  0  254 HIS   D CA  1 
ATOM   7911 C  C   . HIS   D  1 239 ? 4.039   -4.069  37.758  1.00 35.73  0  254 HIS   D C   1 
ATOM   7912 O  O   . HIS   D  1 239 ? 2.864   -4.018  38.122  1.00 31.62  0  254 HIS   D O   1 
ATOM   7913 C  CB  . HIS   D  1 239 ? 4.709   -1.896  36.680  1.00 35.42  0  254 HIS   D CB  1 
ATOM   7914 C  CG  . HIS   D  1 239 ? 3.325   -1.400  36.489  1.00 41.68  0  254 HIS   D CG  1 
ATOM   7915 N  ND1 . HIS   D  1 239 ? 2.939   -0.128  36.912  1.00 51.22  0  254 HIS   D ND1 1 
ATOM   7916 C  CD2 . HIS   D  1 239 ? 2.255   -1.955  35.861  1.00 48.53  0  254 HIS   D CD2 1 
ATOM   7917 C  CE1 . HIS   D  1 239 ? 1.675   0.078   36.555  1.00 52.72  0  254 HIS   D CE1 1 
ATOM   7918 N  NE2 . HIS   D  1 239 ? 1.221   -1.049  35.917  1.00 50.26  0  254 HIS   D NE2 1 
ATOM   7919 N  N   . TYR   D  1 240 ? 4.597   -5.158  37.228  1.00 33.16  0  255 TYR   D N   1 
ATOM   7920 C  CA  . TYR   D  1 240 ? 3.827   -6.368  36.838  1.00 32.31  0  255 TYR   D CA  1 
ATOM   7921 C  C   . TYR   D  1 240 ? 4.172   -7.558  37.722  1.00 29.06  0  255 TYR   D C   1 
ATOM   7922 O  O   . TYR   D  1 240 ? 3.274   -8.333  37.984  1.00 29.69  0  255 TYR   D O   1 
ATOM   7923 C  CB  . TYR   D  1 240 ? 4.094   -6.694  35.369  1.00 29.79  0  255 TYR   D CB  1 
ATOM   7924 C  CG  . TYR   D  1 240 ? 3.566   -5.632  34.438  1.00 29.86  0  255 TYR   D CG  1 
ATOM   7925 C  CD1 . TYR   D  1 240 ? 2.218   -5.552  34.134  1.00 30.02  0  255 TYR   D CD1 1 
ATOM   7926 C  CD2 . TYR   D  1 240 ? 4.411   -4.687  33.892  1.00 30.15  0  255 TYR   D CD2 1 
ATOM   7927 C  CE1 . TYR   D  1 240 ? 1.724   -4.568  33.298  1.00 29.70  0  255 TYR   D CE1 1 
ATOM   7928 C  CE2 . TYR   D  1 240 ? 3.940   -3.708  33.039  1.00 28.37  0  255 TYR   D CE2 1 
ATOM   7929 C  CZ  . TYR   D  1 240 ? 2.602   -3.656  32.736  1.00 31.44  0  255 TYR   D CZ  1 
ATOM   7930 O  OH  . TYR   D  1 240 ? 2.188   -2.681  31.879  1.00 30.92  0  255 TYR   D OH  1 
ATOM   7931 N  N   . VAL   D  1 241 ? 5.419   -7.687  38.155  1.00 28.40  0  256 VAL   D N   1 
ATOM   7932 C  CA  . VAL   D  1 241 ? 5.964   -8.919  38.774  1.00 34.34  0  256 VAL   D CA  1 
ATOM   7933 C  C   . VAL   D  1 241 ? 6.152   -8.635  40.258  1.00 34.81  0  256 VAL   D C   1 
ATOM   7934 O  O   . VAL   D  1 241 ? 6.938   -7.764  40.603  1.00 38.79  0  256 VAL   D O   1 
ATOM   7935 C  CB  . VAL   D  1 241 ? 7.300   -9.326  38.117  1.00 33.30  0  256 VAL   D CB  1 
ATOM   7936 C  CG1 . VAL   D  1 241 ? 7.876   -10.594 38.743  1.00 35.09  0  256 VAL   D CG1 1 
ATOM   7937 C  CG2 . VAL   D  1 241 ? 7.179   -9.487  36.607  1.00 31.36  0  256 VAL   D CG2 1 
ATOM   7938 N  N   . PRO   D  1 242 ? 5.466   -9.359  41.168  1.00 41.22  0  257 PRO   D N   1 
ATOM   7939 C  CA  . PRO   D  1 242 ? 5.696   -9.218  42.619  1.00 40.11  0  257 PRO   D CA  1 
ATOM   7940 C  C   . PRO   D  1 242 ? 7.168   -9.361  43.032  1.00 42.33  0  257 PRO   D C   1 
ATOM   7941 O  O   . PRO   D  1 242 ? 7.854   -10.162 42.410  1.00 43.03  0  257 PRO   D O   1 
ATOM   7942 C  CB  . PRO   D  1 242 ? 4.904   -10.397 43.212  1.00 39.49  0  257 PRO   D CB  1 
ATOM   7943 C  CG  . PRO   D  1 242 ? 3.778   -10.597 42.208  1.00 41.64  0  257 PRO   D CG  1 
ATOM   7944 C  CD  . PRO   D  1 242 ? 4.425   -10.356 40.848  1.00 40.58  0  257 PRO   D CD  1 
ATOM   7945 N  N   . LYS   D  1 243 ? 7.618   -8.599  44.032  1.00 54.59  0  258 LYS   D N   1 
ATOM   7946 C  CA  . LYS   D  1 243 ? 8.893   -8.851  44.773  1.00 70.49  0  258 LYS   D CA  1 
ATOM   7947 C  C   . LYS   D  1 243 ? 8.514   -9.441  46.136  1.00 67.82  0  258 LYS   D C   1 
ATOM   7948 O  O   . LYS   D  1 243 ? 8.270   -10.648 46.186  1.00 69.46  0  258 LYS   D O   1 
ATOM   7949 C  CB  . LYS   D  1 243 ? 9.775   -7.598  44.862  1.00 74.62  0  258 LYS   D CB  1 
ATOM   7950 C  CG  . LYS   D  1 243 ? 11.186  -7.833  45.402  1.00 74.90  0  258 LYS   D CG  1 
ATOM   7951 C  CD  . LYS   D  1 243 ? 12.143  -8.500  44.646  0.00 77.67  0  258 LYS   D CD  1 
ATOM   7952 C  CE  . LYS   D  1 243 ? 12.785  -7.521  43.693  0.00 77.44  0  258 LYS   D CE  1 
ATOM   7953 N  NZ  . LYS   D  1 243 ? 13.568  -8.216  42.645  0.00 77.19  1  258 LYS   D NZ  1 
HETATM 7954 C  C1  . A1I52 E  2 .   ? 22.576  -33.404 -19.056 1.00 25.97  0  301 A1I52 A C1  1 
HETATM 7955 C  C2  . A1I52 E  2 .   ? 21.466  -33.362 -18.081 1.00 25.71  0  301 A1I52 A C2  1 
HETATM 7956 C  C3  . A1I52 E  2 .   ? 20.226  -32.755 -18.696 1.00 27.47  0  301 A1I52 A C3  1 
HETATM 7957 C  C4  . A1I52 E  2 .   ? 19.067  -32.641 -17.737 1.00 30.28  0  301 A1I52 A C4  1 
HETATM 7958 C  C5  . A1I52 E  2 .   ? 18.745  -34.359 -16.022 1.00 46.57  0  301 A1I52 A C5  1 
HETATM 7959 C  C6  . A1I52 E  2 .   ? 18.427  -35.789 -15.743 1.00 45.87  0  301 A1I52 A C6  1 
HETATM 7960 C  C7  . A1I52 E  2 .   ? 19.248  -36.588 -14.936 1.00 50.78  0  301 A1I52 A C7  1 
HETATM 7961 C  C8  . A1I52 E  2 .   ? 18.894  -37.900 -14.650 1.00 48.80  0  301 A1I52 A C8  1 
HETATM 7962 C  C11 . A1I52 E  2 .   ? 17.267  -36.338 -16.293 1.00 38.27  0  301 A1I52 A C11 1 
HETATM 7963 C  C12 . A1I52 E  2 .   ? 17.806  -31.857 -18.260 1.00 33.25  0  301 A1I52 A C12 1 
HETATM 7964 C  C15 . A1I52 E  2 .   ? 14.003  -32.716 -15.227 1.00 37.35  0  301 A1I52 A C15 1 
HETATM 7965 C  C16 . A1I52 E  2 .   ? 12.768  -31.855 -15.356 1.00 42.99  0  301 A1I52 A C16 1 
HETATM 7966 C  C17 . A1I52 E  2 .   ? 12.562  -30.782 -14.485 1.00 49.05  0  301 A1I52 A C17 1 
HETATM 7967 C  C18 . A1I52 E  2 .   ? 11.417  -30.007 -14.560 1.00 46.09  0  301 A1I52 A C18 1 
HETATM 7968 C  C19 . A1I52 E  2 .   ? 10.417  -30.345 -15.464 1.00 48.08  0  301 A1I52 A C19 1 
HETATM 7969 C  C21 . A1I52 E  2 .   ? 6.977   -29.210 -15.783 1.00 35.14  0  301 A1I52 A C21 1 
HETATM 7970 C  C23 . A1I52 E  2 .   ? 4.539   -28.916 -16.212 1.00 58.30  0  301 A1I52 A C23 1 
HETATM 7971 C  C24 . A1I52 E  2 .   ? 3.403   -28.979 -16.996 1.00 61.77  0  301 A1I52 A C24 1 
HETATM 7972 C  C27 . A1I52 E  2 .   ? 5.822   -29.957 -17.945 1.00 41.85  0  301 A1I52 A C27 1 
HETATM 7973 N  N   . A1I52 E  2 .   ? 24.967  -33.806 -19.442 1.00 27.38  0  301 A1I52 A N   1 
HETATM 7974 C  C   . A1I52 E  2 .   ? 23.879  -33.906 -18.455 1.00 25.49  0  301 A1I52 A C   1 
HETATM 7975 O  O   . A1I52 E  2 .   ? 18.919  -33.563 -15.102 1.00 45.09  0  301 A1I52 A O   1 
HETATM 7976 CL CL  . A1I52 E  2 .   ? 2.031   -29.613 -19.202 1.00 91.66  0  301 A1I52 A CL  1 
HETATM 7977 CL CL1 . A1I52 E  2 .   ? 4.744   -30.828 -20.258 1.00 78.98  0  301 A1I52 A CL1 1 
HETATM 7978 N  N1  . A1I52 E  2 .   ? 18.765  -33.998 -17.314 1.00 37.28  0  301 A1I52 A N1  1 
HETATM 7979 O  O1  . A1I52 E  2 .   ? 18.294  -30.581 -18.536 1.00 34.10  0  301 A1I52 A O1  1 
HETATM 7980 N  N2  . A1I52 E  2 .   ? 17.005  -30.886 -16.136 1.00 42.53  0  301 A1I52 A N2  1 
HETATM 7981 O  O2  . A1I52 E  2 .   ? 15.875  -31.177 -15.300 1.00 47.63  0  301 A1I52 A O2  1 
HETATM 7982 N  N3  . A1I52 E  2 .   ? 15.761  -32.558 -17.010 1.00 36.65  0  301 A1I52 A N3  1 
HETATM 7983 O  O3  . A1I52 E  2 .   ? 9.288   -29.546 -15.416 1.00 44.01  0  301 A1I52 A O3  1 
HETATM 7984 C  C9  . A1I52 E  2 .   ? 17.727  -38.395 -15.201 1.00 44.54  0  301 A1I52 A C9  1 
HETATM 7985 C  C10 . A1I52 E  2 .   ? 16.894  -37.640 -16.007 1.00 43.09  0  301 A1I52 A C10 1 
HETATM 7986 C  C13 . A1I52 E  2 .   ? 16.866  -31.745 -17.107 1.00 38.39  0  301 A1I52 A C13 1 
HETATM 7987 C  C14 . A1I52 E  2 .   ? 15.208  -32.164 -15.911 1.00 37.73  0  301 A1I52 A C14 1 
HETATM 7988 C  C20 . A1I52 E  2 .   ? 8.125   -30.042 -16.084 1.00 35.93  0  301 A1I52 A C20 1 
HETATM 7989 C  C22 . A1I52 E  2 .   ? 5.769   -29.375 -16.680 1.00 43.53  0  301 A1I52 A C22 1 
HETATM 7990 C  C25 . A1I52 E  2 .   ? 3.470   -29.536 -18.246 1.00 63.50  0  301 A1I52 A C25 1 
HETATM 7991 C  C26 . A1I52 E  2 .   ? 4.677   -30.044 -18.718 1.00 57.57  0  301 A1I52 A C26 1 
HETATM 7992 C  C28 . A1I52 E  2 .   ? 10.590  -31.436 -16.319 1.00 40.52  0  301 A1I52 A C28 1 
HETATM 7993 C  C29 . A1I52 E  2 .   ? 11.755  -32.187 -16.249 1.00 42.36  0  301 A1I52 A C29 1 
HETATM 7994 F  F   . A1I52 E  2 .   ? 17.402  -39.685 -14.973 1.00 48.97  0  301 A1I52 A F   1 
HETATM 7995 S  S   . SO4   F  3 .   ? 39.249  -29.334 -24.502 1.00 76.61  0  302 SO4   A S   1 
HETATM 7996 O  O1  . SO4   F  3 .   ? 40.201  -29.551 -25.553 1.00 72.37  0  302 SO4   A O1  1 
HETATM 7997 O  O2  . SO4   F  3 .   ? 37.993  -29.892 -24.906 1.00 72.18  0  302 SO4   A O2  1 
HETATM 7998 O  O3  . SO4   F  3 .   ? 39.694  -30.012 -23.320 1.00 77.78  -1 302 SO4   A O3  1 
HETATM 7999 O  O4  . SO4   F  3 .   ? 39.130  -27.910 -24.242 1.00 67.90  0  302 SO4   A O4  1 
HETATM 8000 S  S   . SO4   G  3 .   ? 3.780   -48.764 -38.212 1.00 80.03  0  303 SO4   A S   1 
HETATM 8001 O  O1  . SO4   G  3 .   ? 3.771   -49.327 -39.546 1.00 75.57  0  303 SO4   A O1  1 
HETATM 8002 O  O2  . SO4   G  3 .   ? 2.431   -48.583 -37.757 1.00 67.43  0  303 SO4   A O2  1 
HETATM 8003 O  O3  . SO4   G  3 .   ? 4.467   -49.690 -37.343 1.00 89.04  -1 303 SO4   A O3  1 
HETATM 8004 O  O4  . SO4   G  3 .   ? 4.454   -47.469 -38.185 1.00 67.15  0  303 SO4   A O4  1 
HETATM 8005 S  S   . SO4   H  3 .   ? 27.036  -22.816 -40.222 1.00 105.28 0  304 SO4   A S   1 
HETATM 8006 O  O1  . SO4   H  3 .   ? 26.576  -23.435 -41.443 1.00 85.26  0  304 SO4   A O1  1 
HETATM 8007 O  O2  . SO4   H  3 .   ? 26.013  -22.914 -39.205 1.00 118.00 0  304 SO4   A O2  1 
HETATM 8008 O  O3  . SO4   H  3 .   ? 28.238  -23.472 -39.766 1.00 94.18  -1 304 SO4   A O3  1 
HETATM 8009 O  O4  . SO4   H  3 .   ? 27.311  -21.424 -40.460 1.00 112.53 0  304 SO4   A O4  1 
HETATM 8010 S  S   . SO4   I  3 .   ? 16.686  -11.028 -28.400 1.00 77.12  0  305 SO4   A S   1 
HETATM 8011 O  O1  . SO4   I  3 .   ? 17.939  -10.417 -28.019 1.00 55.56  0  305 SO4   A O1  1 
HETATM 8012 O  O2  . SO4   I  3 .   ? 16.651  -11.210 -29.831 1.00 69.00  0  305 SO4   A O2  1 
HETATM 8013 O  O3  . SO4   I  3 .   ? 16.479  -12.313 -27.739 1.00 53.58  -1 305 SO4   A O3  1 
HETATM 8014 O  O4  . SO4   I  3 .   ? 15.624  -10.132 -28.039 1.00 83.17  0  305 SO4   A O4  1 
HETATM 8015 C  C1  . PEG   J  4 .   ? 11.341  -50.951 -22.384 1.00 58.59  0  306 PEG   A C1  1 
HETATM 8016 O  O1  . PEG   J  4 .   ? 10.979  -52.108 -23.107 1.00 58.08  0  306 PEG   A O1  1 
HETATM 8017 C  C2  . PEG   J  4 .   ? 12.754  -50.526 -22.666 1.00 63.01  0  306 PEG   A C2  1 
HETATM 8018 O  O2  . PEG   J  4 .   ? 12.802  -49.671 -23.812 1.00 66.36  0  306 PEG   A O2  1 
HETATM 8019 C  C3  . PEG   J  4 .   ? 14.074  -49.078 -24.075 1.00 56.63  0  306 PEG   A C3  1 
HETATM 8020 C  C4  . PEG   J  4 .   ? 15.005  -50.113 -24.637 1.00 58.08  0  306 PEG   A C4  1 
HETATM 8021 O  O4  . PEG   J  4 .   ? 15.786  -49.666 -25.721 1.00 60.56  0  306 PEG   A O4  1 
HETATM 8022 C  C1  . EDO   K  5 .   ? 29.279  -23.634 -36.150 1.00 65.64  0  307 EDO   A C1  1 
HETATM 8023 O  O1  . EDO   K  5 .   ? 30.408  -24.261 -36.697 1.00 69.47  0  307 EDO   A O1  1 
HETATM 8024 C  C2  . EDO   K  5 .   ? 29.495  -23.169 -34.768 1.00 63.51  0  307 EDO   A C2  1 
HETATM 8025 O  O2  . EDO   K  5 .   ? 30.772  -22.608 -34.558 1.00 69.56  0  307 EDO   A O2  1 
HETATM 8026 C  C1  . EDO   L  5 .   ? 33.300  -56.146 -19.449 1.00 52.88  0  308 EDO   A C1  1 
HETATM 8027 O  O1  . EDO   L  5 .   ? 34.673  -56.258 -19.138 1.00 55.03  0  308 EDO   A O1  1 
HETATM 8028 C  C2  . EDO   L  5 .   ? 32.994  -55.004 -20.350 1.00 50.69  0  308 EDO   A C2  1 
HETATM 8029 O  O2  . EDO   L  5 .   ? 31.838  -55.223 -21.134 1.00 54.36  0  308 EDO   A O2  1 
HETATM 8030 C  C1  . EDO   M  5 .   ? 26.965  -48.258 -30.656 1.00 59.16  0  309 EDO   A C1  1 
HETATM 8031 O  O1  . EDO   M  5 .   ? 25.887  -47.646 -31.336 1.00 63.31  0  309 EDO   A O1  1 
HETATM 8032 C  C2  . EDO   M  5 .   ? 26.555  -49.122 -29.531 1.00 59.03  0  309 EDO   A C2  1 
HETATM 8033 O  O2  . EDO   M  5 .   ? 25.913  -50.318 -29.893 1.00 58.69  0  309 EDO   A O2  1 
HETATM 8034 C  C   . ACT   N  6 .   ? 32.888  -23.819 -28.730 1.00 51.32  0  310 ACT   A C   1 
HETATM 8035 O  O   . ACT   N  6 .   ? 32.114  -22.878 -28.525 1.00 56.08  0  310 ACT   A O   1 
HETATM 8036 O  OXT . ACT   N  6 .   ? 32.919  -24.887 -28.041 1.00 40.79  0  310 ACT   A OXT 1 
HETATM 8037 C  CH3 . ACT   N  6 .   ? 33.887  -23.630 -29.857 1.00 54.94  0  310 ACT   A CH3 1 
HETATM 8038 C  C1  . A1I52 O  2 .   ? 9.237   -0.777  0.865   1.00 26.80  0  301 A1I52 B C1  1 
HETATM 8039 C  C2  . A1I52 O  2 .   ? 10.401  -1.551  1.348   1.00 27.43  0  301 A1I52 B C2  1 
HETATM 8040 C  C3  . A1I52 O  2 .   ? 11.627  -1.229  0.553   1.00 29.99  0  301 A1I52 B C3  1 
HETATM 8041 C  C4  . A1I52 O  2 .   ? 12.770  -2.203  0.869   1.00 33.06  0  301 A1I52 B C4  1 
HETATM 8042 C  C5  . A1I52 O  2 .   ? 13.256  -3.019  3.133   1.00 47.31  0  301 A1I52 B C5  1 
HETATM 8043 C  C6  . A1I52 O  2 .   ? 13.613  -2.626  4.529   1.00 48.59  0  301 A1I52 B C6  1 
HETATM 8044 C  C7  . A1I52 O  2 .   ? 12.863  -3.032  5.638   1.00 51.22  0  301 A1I52 B C7  1 
HETATM 8045 C  C8  . A1I52 O  2 .   ? 13.260  -2.687  6.923   1.00 49.02  0  301 A1I52 B C8  1 
HETATM 8046 C  C11 . A1I52 O  2 .   ? 14.744  -1.830  4.726   1.00 48.63  0  301 A1I52 B C11 1 
HETATM 8047 C  C12 . A1I52 O  2 .   ? 14.035  -2.104  -0.070  1.00 38.06  0  301 A1I52 B C12 1 
HETATM 8048 C  C15 . A1I52 O  2 .   ? 17.813  -4.474  2.063   1.00 44.71  0  301 A1I52 B C15 1 
HETATM 8049 C  C16 . A1I52 O  2 .   ? 19.083  -4.666  1.266   1.00 50.75  0  301 A1I52 B C16 1 
HETATM 8050 C  C17 . A1I52 O  2 .   ? 19.474  -5.941  0.852   1.00 62.12  0  301 A1I52 B C17 1 
HETATM 8051 C  C18 . A1I52 O  2 .   ? 20.644  -6.133  0.137   1.00 59.19  0  301 A1I52 B C18 1 
HETATM 8052 C  C19 . A1I52 O  2 .   ? 21.464  -5.044  -0.142  1.00 62.65  0  301 A1I52 B C19 1 
HETATM 8053 C  C21 . A1I52 O  2 .   ? 24.947  -5.101  -1.117  1.00 43.08  0  301 A1I52 B C21 1 
HETATM 8054 C  C23 . A1I52 O  2 .   ? 27.305  -4.961  -1.938  1.00 60.01  0  301 A1I52 B C23 1 
HETATM 8055 C  C24 . A1I52 O  2 .   ? 28.420  -4.266  -2.371  1.00 69.03  0  301 A1I52 B C24 1 
HETATM 8056 C  C27 . A1I52 O  2 .   ? 26.144  -2.895  -1.575  1.00 60.62  0  301 A1I52 B C27 1 
HETATM 8057 N  N   . A1I52 O  2 .   ? 6.858   -0.322  1.182   1.00 26.58  0  301 A1I52 B N   1 
HETATM 8058 C  C   . A1I52 O  2 .   ? 7.953   -1.223  1.507   1.00 26.59  0  301 A1I52 B C   1 
HETATM 8059 O  O   . A1I52 O  2 .   ? 13.175  -4.204  2.804   1.00 52.14  0  301 A1I52 B O   1 
HETATM 8060 CL CL  . A1I52 O  2 .   ? 29.806  -2.045  -2.944  1.00 108.46 0  301 A1I52 B CL  1 
HETATM 8061 CL CL1 . A1I52 O  2 .   ? 27.252  -0.467  -1.983  1.00 95.45  0  301 A1I52 B CL1 1 
HETATM 8062 N  N1  . A1I52 O  2 .   ? 13.101  -2.011  2.267   1.00 33.80  0  301 A1I52 B N1  1 
HETATM 8063 O  O1  . A1I52 O  2 .   ? 13.529  -2.440  -1.321  1.00 39.37  0  301 A1I52 B O1  1 
HETATM 8064 N  N2  . A1I52 O  2 .   ? 15.026  -4.391  -0.234  1.00 50.10  0  301 A1I52 B N2  1 
HETATM 8065 O  O2  . A1I52 O  2 .   ? 16.118  -5.016  0.423   1.00 46.05  0  301 A1I52 B O2  1 
HETATM 8066 N  N3  . A1I52 O  2 .   ? 16.030  -2.950  1.176   1.00 44.74  0  301 A1I52 B N3  1 
HETATM 8067 O  O3  . A1I52 O  2 .   ? 22.637  -5.325  -0.803  1.00 52.88  0  301 A1I52 B O3  1 
HETATM 8068 C  C9  . A1I52 O  2 .   ? 14.389  -1.896  7.070   1.00 48.91  0  301 A1I52 B C9  1 
HETATM 8069 C  C10 . A1I52 O  2 .   ? 15.145  -1.460  6.001   1.00 47.73  0  301 A1I52 B C10 1 
HETATM 8070 C  C13 . A1I52 O  2 .   ? 15.034  -3.187  0.276   1.00 43.01  0  301 A1I52 B C13 1 
HETATM 8071 C  C14 . A1I52 O  2 .   ? 16.650  -4.083  1.219   1.00 44.46  0  301 A1I52 B C14 1 
HETATM 8072 C  C20 . A1I52 O  2 .   ? 23.721  -4.367  -0.679  1.00 47.00  0  301 A1I52 B C20 1 
HETATM 8073 C  C22 . A1I52 O  2 .   ? 26.147  -4.292  -1.549  1.00 50.07  0  301 A1I52 B C22 1 
HETATM 8074 C  C25 . A1I52 O  2 .   ? 28.398  -2.890  -2.408  1.00 73.42  0  301 A1I52 B C25 1 
HETATM 8075 C  C26 . A1I52 O  2 .   ? 27.264  -2.201  -2.000  1.00 72.64  0  301 A1I52 B C26 1 
HETATM 8076 C  C28 . A1I52 O  2 .   ? 21.101  -3.768  0.292   1.00 53.16  0  301 A1I52 B C28 1 
HETATM 8077 C  C29 . A1I52 O  2 .   ? 19.908  -3.587  0.970   1.00 52.38  0  301 A1I52 B C29 1 
HETATM 8078 F  F   . A1I52 O  2 .   ? 14.760  -1.520  8.321   1.00 45.90  0  301 A1I52 B F   1 
HETATM 8079 S  S   . SO4   P  3 .   ? -7.282  1.090   -5.623  1.00 90.39  0  302 SO4   B S   1 
HETATM 8080 O  O1  . SO4   P  3 .   ? -6.216  0.385   -6.283  1.00 99.88  0  302 SO4   B O1  1 
HETATM 8081 O  O2  . SO4   P  3 .   ? -7.383  2.419   -6.163  1.00 90.49  0  302 SO4   B O2  1 
HETATM 8082 O  O3  . SO4   P  3 .   ? -8.508  0.372   -5.844  1.00 89.92  -1 302 SO4   B O3  1 
HETATM 8083 O  O4  . SO4   P  3 .   ? -7.013  1.166   -4.210  1.00 83.63  0  302 SO4   B O4  1 
HETATM 8084 S  S   . SO4   Q  3 .   ? 4.548   13.397  -18.256 1.00 101.32 0  303 SO4   B S   1 
HETATM 8085 O  O1  . SO4   Q  3 .   ? 4.977   12.082  -17.860 1.00 113.53 0  303 SO4   B O1  1 
HETATM 8086 O  O2  . SO4   Q  3 .   ? 4.033   13.332  -19.598 1.00 105.21 0  303 SO4   B O2  1 
HETATM 8087 O  O3  . SO4   Q  3 .   ? 3.492   13.813  -17.366 1.00 95.38  -1 303 SO4   B O3  1 
HETATM 8088 O  O4  . SO4   Q  3 .   ? 5.664   14.327  -18.194 1.00 69.28  0  303 SO4   B O4  1 
HETATM 8089 C  C   . ACT   R  6 .   ? 10.018  16.891  -16.156 1.00 61.58  0  304 ACT   B C   1 
HETATM 8090 O  O   . ACT   R  6 .   ? 9.242   17.441  -15.312 1.00 53.78  0  304 ACT   B O   1 
HETATM 8091 O  OXT . ACT   R  6 .   ? 11.257  16.901  -16.059 1.00 62.66  0  304 ACT   B OXT 1 
HETATM 8092 C  CH3 . ACT   R  6 .   ? 9.421   16.184  -17.388 1.00 56.94  0  304 ACT   B CH3 1 
HETATM 8093 C  C1  . GOL   S  7 .   ? 16.062  -0.801  -23.459 1.00 57.42  0  305 GOL   B C1  1 
HETATM 8094 O  O1  . GOL   S  7 .   ? 15.552  0.119   -22.490 1.00 49.22  0  305 GOL   B O1  1 
HETATM 8095 C  C2  . GOL   S  7 .   ? 15.794  -2.246  -23.094 1.00 55.72  0  305 GOL   B C2  1 
HETATM 8096 O  O2  . GOL   S  7 .   ? 16.377  -2.523  -21.821 1.00 58.89  0  305 GOL   B O2  1 
HETATM 8097 C  C3  . GOL   S  7 .   ? 14.327  -2.615  -23.022 1.00 54.37  0  305 GOL   B C3  1 
HETATM 8098 O  O3  . GOL   S  7 .   ? 13.881  -3.542  -24.003 1.00 48.31  0  305 GOL   B O3  1 
HETATM 8099 C  C1  . EDO   T  5 .   ? 2.222   7.834   -16.096 1.00 61.98  0  306 EDO   B C1  1 
HETATM 8100 O  O1  . EDO   T  5 .   ? 0.893   7.381   -16.007 1.00 64.00  0  306 EDO   B O1  1 
HETATM 8101 C  C2  . EDO   T  5 .   ? 2.384   9.203   -15.566 1.00 65.30  0  306 EDO   B C2  1 
HETATM 8102 O  O2  . EDO   T  5 .   ? 1.179   9.800   -15.117 1.00 63.88  0  306 EDO   B O2  1 
HETATM 8103 S  S   . SO4   U  3 .   ? 32.567  16.353  3.040   1.00 97.21  0  307 SO4   B S   1 
HETATM 8104 O  O1  . SO4   U  3 .   ? 32.838  16.421  1.623   1.00 88.18  0  307 SO4   B O1  1 
HETATM 8105 O  O2  . SO4   U  3 .   ? 31.498  15.425  3.312   1.00 70.01  0  307 SO4   B O2  1 
HETATM 8106 O  O3  . SO4   U  3 .   ? 33.734  15.890  3.737   1.00 99.17  -1 307 SO4   B O3  1 
HETATM 8107 O  O4  . SO4   U  3 .   ? 32.209  17.670  3.505   1.00 95.04  0  307 SO4   B O4  1 
HETATM 8108 C  C1  . EDO   V  5 .   ? -2.650  -4.190  11.447  1.00 63.61  0  308 EDO   B C1  1 
HETATM 8109 O  O1  . EDO   V  5 .   ? -3.809  -3.815  12.142  1.00 59.77  0  308 EDO   B O1  1 
HETATM 8110 C  C2  . EDO   V  5 .   ? -2.037  -5.433  11.932  1.00 64.34  0  308 EDO   B C2  1 
HETATM 8111 O  O2  . EDO   V  5 .   ? -2.887  -6.183  12.771  1.00 73.21  0  308 EDO   B O2  1 
HETATM 8112 C  C1  . EDO   W  5 .   ? 14.673  20.148  8.077   1.00 54.32  0  309 EDO   B C1  1 
HETATM 8113 O  O1  . EDO   W  5 .   ? 16.072  20.312  8.227   1.00 59.24  0  309 EDO   B O1  1 
HETATM 8114 C  C2  . EDO   W  5 .   ? 13.936  21.431  8.214   1.00 56.24  0  309 EDO   B C2  1 
HETATM 8115 O  O2  . EDO   W  5 .   ? 12.525  21.284  8.325   1.00 58.49  0  309 EDO   B O2  1 
HETATM 8116 C  C1  . A1I52 X  2 .   ? 9.219   -44.552 -0.808  1.00 25.47  0  301 A1I52 C C1  1 
HETATM 8117 C  C2  . A1I52 X  2 .   ? 10.354  -43.684 -1.228  1.00 27.04  0  301 A1I52 C C2  1 
HETATM 8118 C  C3  . A1I52 X  2 .   ? 11.584  -44.050 -0.486  1.00 27.04  0  301 A1I52 C C3  1 
HETATM 8119 C  C4  . A1I52 X  2 .   ? 12.754  -43.120 -0.803  1.00 34.54  0  301 A1I52 C C4  1 
HETATM 8120 C  C5  . A1I52 X  2 .   ? 13.266  -42.363 -3.075  1.00 46.06  0  301 A1I52 C C5  1 
HETATM 8121 C  C6  . A1I52 X  2 .   ? 13.646  -42.772 -4.465  1.00 47.48  0  301 A1I52 C C6  1 
HETATM 8122 C  C7  . A1I52 X  2 .   ? 12.890  -42.413 -5.587  1.00 49.54  0  301 A1I52 C C7  1 
HETATM 8123 C  C8  . A1I52 X  2 .   ? 13.298  -42.780 -6.862  1.00 46.99  0  301 A1I52 C C8  1 
HETATM 8124 C  C11 . A1I52 X  2 .   ? 14.815  -43.514 -4.645  1.00 45.29  0  301 A1I52 C C11 1 
HETATM 8125 C  C12 . A1I52 X  2 .   ? 13.991  -43.237 0.184   1.00 38.73  0  301 A1I52 C C12 1 
HETATM 8126 C  C15 . A1I52 X  2 .   ? 17.780  -40.988 -2.012  1.00 45.56  0  301 A1I52 C C15 1 
HETATM 8127 C  C16 . A1I52 X  2 .   ? 19.042  -40.741 -1.219  1.00 49.34  0  301 A1I52 C C16 1 
HETATM 8128 C  C17 . A1I52 X  2 .   ? 19.421  -39.442 -0.870  1.00 60.48  0  301 A1I52 C C17 1 
HETATM 8129 C  C18 . A1I52 X  2 .   ? 20.577  -39.204 -0.143  1.00 57.69  0  301 A1I52 C C18 1 
HETATM 8130 C  C19 . A1I52 X  2 .   ? 21.401  -40.272 0.201   1.00 61.69  0  301 A1I52 C C19 1 
HETATM 8131 C  C21 . A1I52 X  2 .   ? 24.862  -40.146 0.915   1.00 49.80  0  301 A1I52 C C21 1 
HETATM 8132 C  C23 . A1I52 X  2 .   ? 27.168  -40.159 1.885   1.00 64.02  0  301 A1I52 C C23 1 
HETATM 8133 C  C24 . A1I52 X  2 .   ? 28.270  -40.801 2.420   1.00 71.66  0  301 A1I52 C C24 1 
HETATM 8134 C  C27 . A1I52 X  2 .   ? 26.046  -42.268 1.637   1.00 64.19  0  301 A1I52 C C27 1 
HETATM 8135 N  N   . A1I52 X  2 .   ? 6.888   -45.018 -1.085  1.00 28.15  0  301 A1I52 C N   1 
HETATM 8136 C  C   . A1I52 X  2 .   ? 7.989   -44.250 -1.594  1.00 26.81  0  301 A1I52 C C   1 
HETATM 8137 O  O   . A1I52 X  2 .   ? 13.192  -41.177 -2.757  1.00 55.25  0  301 A1I52 C O   1 
HETATM 8138 CL CL  . A1I52 X  2 .   ? 29.637  -42.948 3.258   1.00 93.62  0  301 A1I52 C CL  1 
HETATM 8139 CL CL1 . A1I52 X  2 .   ? 27.145  -44.642 2.291   1.00 96.87  0  301 A1I52 C CL1 1 
HETATM 8140 N  N1  . A1I52 X  2 .   ? 13.103  -43.353 -2.192  1.00 33.94  0  301 A1I52 C N1  1 
HETATM 8141 O  O1  . A1I52 X  2 .   ? 13.456  -42.878 1.437   1.00 44.70  0  301 A1I52 C O1  1 
HETATM 8142 N  N2  . A1I52 X  2 .   ? 14.953  -40.920 0.251   1.00 50.50  0  301 A1I52 C N2  1 
HETATM 8143 O  O2  . A1I52 X  2 .   ? 16.059  -40.334 -0.431  1.00 48.17  0  301 A1I52 C O2  1 
HETATM 8144 N  N3  . A1I52 X  2 .   ? 15.984  -42.447 -1.046  1.00 42.33  0  301 A1I52 C N3  1 
HETATM 8145 O  O3  . A1I52 X  2 .   ? 22.528  -39.883 0.886   1.00 52.50  0  301 A1I52 C O3  1 
HETATM 8146 C  C9  . A1I52 X  2 .   ? 14.460  -43.512 -6.992  1.00 47.25  0  301 A1I52 C C9  1 
HETATM 8147 C  C10 . A1I52 X  2 .   ? 15.235  -43.891 -5.910  1.00 45.42  0  301 A1I52 C C10 1 
HETATM 8148 C  C13 . A1I52 X  2 .   ? 14.979  -42.158 -0.173  1.00 41.08  0  301 A1I52 C C13 1 
HETATM 8149 C  C14 . A1I52 X  2 .   ? 16.603  -41.318 -1.159  1.00 44.50  0  301 A1I52 C C14 1 
HETATM 8150 C  C20 . A1I52 X  2 .   ? 23.570  -40.862 1.074   1.00 50.46  0  301 A1I52 C C20 1 
HETATM 8151 C  C22 . A1I52 X  2 .   ? 26.037  -40.875 1.504   1.00 56.36  0  301 A1I52 C C22 1 
HETATM 8152 C  C25 . A1I52 X  2 .   ? 28.256  -42.173 2.576   1.00 70.41  0  301 A1I52 C C25 1 
HETATM 8153 C  C26 . A1I52 X  2 .   ? 27.147  -42.910 2.174   1.00 74.16  0  301 A1I52 C C26 1 
HETATM 8154 C  C28 . A1I52 X  2 .   ? 21.054  -41.573 -0.172  1.00 51.00  0  301 A1I52 C C28 1 
HETATM 8155 C  C29 . A1I52 X  2 .   ? 19.874  -41.797 -0.861  1.00 53.46  0  301 A1I52 C C29 1 
HETATM 8156 F  F   . A1I52 X  2 .   ? 14.855  -43.883 -8.235  1.00 50.26  0  301 A1I52 C F   1 
HETATM 8157 S  S   . SO4   Y  3 .   ? -7.176  -46.674 5.337   1.00 98.44  0  302 SO4   C S   1 
HETATM 8158 O  O1  . SO4   Y  3 .   ? -5.849  -46.914 5.835   1.00 100.95 0  302 SO4   C O1  1 
HETATM 8159 O  O2  . SO4   Y  3 .   ? -7.116  -46.192 3.981   1.00 97.73  0  302 SO4   C O2  1 
HETATM 8160 O  O3  . SO4   Y  3 .   ? -7.902  -47.913 5.377   1.00 103.54 -1 302 SO4   C O3  1 
HETATM 8161 O  O4  . SO4   Y  3 .   ? -7.836  -45.687 6.153   1.00 88.07  0  302 SO4   C O4  1 
HETATM 8162 S  S   . SO4   Z  3 .   ? 4.948   -59.017 18.504  1.00 91.36  0  303 SO4   C S   1 
HETATM 8163 O  O1  . SO4   Z  3 .   ? 6.233   -58.457 18.180  1.00 86.98  0  303 SO4   C O1  1 
HETATM 8164 O  O2  . SO4   Z  3 .   ? 4.966   -60.400 18.129  1.00 80.24  0  303 SO4   C O2  1 
HETATM 8165 O  O3  . SO4   Z  3 .   ? 4.713   -58.916 19.915  1.00 95.71  -1 303 SO4   C O3  1 
HETATM 8166 O  O4  . SO4   Z  3 .   ? 3.888   -58.305 17.810  1.00 84.34  0  303 SO4   C O4  1 
HETATM 8167 S  S   . SO4   AA 3 .   ? -6.124  -45.629 -2.802  1.00 88.01  0  304 SO4   C S   1 
HETATM 8168 O  O1  . SO4   AA 3 .   ? -4.700  -45.663 -3.016  1.00 92.75  0  304 SO4   C O1  1 
HETATM 8169 O  O2  . SO4   AA 3 .   ? -6.748  -44.844 -3.851  1.00 75.68  0  304 SO4   C O2  1 
HETATM 8170 O  O3  . SO4   AA 3 .   ? -6.621  -46.984 -2.817  1.00 79.96  -1 304 SO4   C O3  1 
HETATM 8171 O  O4  . SO4   AA 3 .   ? -6.409  -45.036 -1.515  1.00 80.61  0  304 SO4   C O4  1 
HETATM 8172 S  S   . SO4   BA 3 .   ? 17.980  -59.371 27.698  1.00 74.36  0  305 SO4   C S   1 
HETATM 8173 O  O1  . SO4   BA 3 .   ? 19.171  -60.175 27.828  1.00 76.44  0  305 SO4   C O1  1 
HETATM 8174 O  O2  . SO4   BA 3 .   ? 17.304  -59.715 26.475  1.00 84.58  0  305 SO4   C O2  1 
HETATM 8175 O  O3  . SO4   BA 3 .   ? 17.094  -59.614 28.810  1.00 89.14  -1 305 SO4   C O3  1 
HETATM 8176 O  O4  . SO4   BA 3 .   ? 18.339  -57.986 27.671  1.00 84.70  0  305 SO4   C O4  1 
HETATM 8177 C  C1  . EDO   CA 5 .   ? 1.805   -52.423 16.077  1.00 64.56  0  306 EDO   C C1  1 
HETATM 8178 O  O1  . EDO   CA 5 .   ? 1.553   -52.305 17.472  1.00 67.83  0  306 EDO   C O1  1 
HETATM 8179 C  C2  . EDO   CA 5 .   ? 2.113   -53.790 15.583  1.00 61.22  0  306 EDO   C C2  1 
HETATM 8180 O  O2  . EDO   CA 5 .   ? 0.980   -54.601 15.384  1.00 62.65  0  306 EDO   C O2  1 
HETATM 8181 C  C   . ACT   DA 6 .   ? 2.432   -61.026 -14.074 1.00 55.94  0  307 ACT   C C   1 
HETATM 8182 O  O   . ACT   DA 6 .   ? 2.186   -60.558 -12.955 1.00 61.91  0  307 ACT   C O   1 
HETATM 8183 O  OXT . ACT   DA 6 .   ? 1.773   -60.731 -15.071 1.00 56.67  0  307 ACT   C OXT 1 
HETATM 8184 C  CH3 . ACT   DA 6 .   ? 3.642   -61.984 -14.217 1.00 54.95  0  307 ACT   C CH3 1 
HETATM 8185 S  S   . SO4   EA 3 .   ? 15.881  -43.839 22.874  1.00 94.18  0  308 SO4   C S   1 
HETATM 8186 O  O1  . SO4   EA 3 .   ? 15.496  -42.764 21.964  1.00 66.62  0  308 SO4   C O1  1 
HETATM 8187 O  O2  . SO4   EA 3 .   ? 15.376  -43.517 24.185  1.00 68.02  0  308 SO4   C O2  1 
HETATM 8188 O  O3  . SO4   EA 3 .   ? 15.350  -45.142 22.466  1.00 62.81  -1 308 SO4   C O3  1 
HETATM 8189 O  O4  . SO4   EA 3 .   ? 17.324  -43.939 22.890  1.00 73.45  0  308 SO4   C O4  1 
HETATM 8190 C  C1  . EDO   FA 5 .   ? 11.433  -53.555 24.825  1.00 72.73  0  309 EDO   C C1  1 
HETATM 8191 O  O1  . EDO   FA 5 .   ? 12.702  -53.404 25.394  1.00 85.03  0  309 EDO   C O1  1 
HETATM 8192 C  C2  . EDO   FA 5 .   ? 11.185  -54.958 24.436  1.00 70.85  0  309 EDO   C C2  1 
HETATM 8193 O  O2  . EDO   FA 5 .   ? 10.812  -55.797 25.497  1.00 72.96  0  309 EDO   C O2  1 
HETATM 8194 C  C1  . EDO   GA 5 .   ? -2.757  -39.822 -11.333 1.00 67.51  0  310 EDO   C C1  1 
HETATM 8195 O  O1  . EDO   GA 5 .   ? -1.541  -40.525 -11.483 1.00 66.61  0  310 EDO   C O1  1 
HETATM 8196 C  C2  . EDO   GA 5 .   ? -3.884  -40.481 -12.028 1.00 65.38  0  310 EDO   C C2  1 
HETATM 8197 O  O2  . EDO   GA 5 .   ? -3.695  -41.865 -12.251 1.00 59.44  0  310 EDO   C O2  1 
HETATM 8198 C  C1  . EDO   HA 5 .   ? 10.144  -41.297 -12.164 1.00 57.27  0  311 EDO   C C1  1 
HETATM 8199 O  O1  . EDO   HA 5 .   ? 10.575  -42.508 -11.572 1.00 55.39  0  311 EDO   C O1  1 
HETATM 8200 C  C2  . EDO   HA 5 .   ? 8.708   -41.359 -12.531 1.00 61.06  0  311 EDO   C C2  1 
HETATM 8201 O  O2  . EDO   HA 5 .   ? 8.015   -40.121 -12.507 1.00 60.39  0  311 EDO   C O2  1 
HETATM 8202 C  C1  . EDO   IA 5 .   ? 33.238  -63.253 1.273   1.00 74.01  0  312 EDO   C C1  1 
HETATM 8203 O  O1  . EDO   IA 5 .   ? 34.465  -62.539 1.224   1.00 84.17  0  312 EDO   C O1  1 
HETATM 8204 C  C2  . EDO   IA 5 .   ? 32.427  -63.157 0.043   1.00 62.36  0  312 EDO   C C2  1 
HETATM 8205 O  O2  . EDO   IA 5 .   ? 32.998  -62.372 -0.969  1.00 61.08  0  312 EDO   C O2  1 
HETATM 8206 C  C1  . A1I52 JA 2 .   ? 22.660  -12.021 19.102  1.00 27.13  0  301 A1I52 D C1  1 
HETATM 8207 C  C2  . A1I52 JA 2 .   ? 21.475  -11.917 18.183  1.00 25.65  0  301 A1I52 D C2  1 
HETATM 8208 C  C3  . A1I52 JA 2 .   ? 20.239  -12.491 18.826  1.00 26.53  0  301 A1I52 D C3  1 
HETATM 8209 C  C4  . A1I52 JA 2 .   ? 19.099  -12.685 17.843  1.00 28.84  0  301 A1I52 D C4  1 
HETATM 8210 C  C5  . A1I52 JA 2 .   ? 18.705  -11.008 16.104  1.00 40.77  0  301 A1I52 D C5  1 
HETATM 8211 C  C6  . A1I52 JA 2 .   ? 18.391  -9.575  15.830  1.00 40.45  0  301 A1I52 D C6  1 
HETATM 8212 C  C7  . A1I52 JA 2 .   ? 19.248  -8.841  14.995  1.00 43.37  0  301 A1I52 D C7  1 
HETATM 8213 C  C8  . A1I52 JA 2 .   ? 18.975  -7.513  14.691  1.00 44.17  0  301 A1I52 D C8  1 
HETATM 8214 C  C11 . A1I52 JA 2 .   ? 17.305  -8.933  16.430  1.00 33.16  0  301 A1I52 D C11 1 
HETATM 8215 C  C12 . A1I52 JA 2 .   ? 17.855  -13.471 18.373  1.00 32.32  0  301 A1I52 D C12 1 
HETATM 8216 C  C15 . A1I52 JA 2 .   ? 14.036  -12.663 15.365  1.00 38.12  0  301 A1I52 D C15 1 
HETATM 8217 C  C16 . A1I52 JA 2 .   ? 12.782  -13.500 15.530  1.00 44.20  0  301 A1I52 D C16 1 
HETATM 8218 C  C17 . A1I52 JA 2 .   ? 12.593  -14.671 14.790  1.00 47.47  0  301 A1I52 D C17 1 
HETATM 8219 C  C18 . A1I52 JA 2 .   ? 11.427  -15.416 14.911  1.00 47.64  0  301 A1I52 D C18 1 
HETATM 8220 C  C19 . A1I52 JA 2 .   ? 10.394  -14.960 15.732  1.00 48.02  0  301 A1I52 D C19 1 
HETATM 8221 C  C21 . A1I52 JA 2 .   ? 6.963   -16.153 16.221  1.00 36.45  0  301 A1I52 D C21 1 
HETATM 8222 C  C23 A A1I52 JA 2 .   ? 4.513   -16.510 16.657  0.70 53.55  0  301 A1I52 D C23 1 
HETATM 8223 C  C23 B A1I52 JA 2 .   ? 5.796   -15.779 18.434  0.30 45.96  0  301 A1I52 D C23 1 
HETATM 8224 C  C24 A A1I52 JA 2 .   ? 3.367   -16.387 17.426  0.70 53.52  0  301 A1I52 D C24 1 
HETATM 8225 C  C24 B A1I52 JA 2 .   ? 4.652   -15.638 19.201  0.30 52.40  0  301 A1I52 D C24 1 
HETATM 8226 C  C27 A A1I52 JA 2 .   ? 5.745   -15.227 18.254  0.70 43.82  0  301 A1I52 D C27 1 
HETATM 8227 C  C27 B A1I52 JA 2 .   ? 4.460   -15.998 16.464  0.30 50.05  0  301 A1I52 D C27 1 
HETATM 8228 N  N   . A1I52 JA 2 .   ? 25.048  -11.562 19.486  1.00 28.45  0  301 A1I52 D N   1 
HETATM 8229 C  C   . A1I52 JA 2 .   ? 23.938  -11.467 18.494  1.00 25.23  0  301 A1I52 D C   1 
HETATM 8230 O  O   . A1I52 JA 2 .   ? 18.875  -11.807 15.190  1.00 40.86  0  301 A1I52 D O   1 
HETATM 8231 CL CL  . A1I52 JA 2 .   ? 1.977   -15.514 19.562  1.00 86.73  0  301 A1I52 D CL  1 
HETATM 8232 CL CL1 A A1I52 JA 2 .   ? 4.614   -14.160 20.461  0.70 59.76  0  301 A1I52 D CL1 1 
HETATM 8233 CL CL1 B A1I52 JA 2 .   ? 1.765   -15.912 16.436  0.30 61.40  0  301 A1I52 D CL1 1 
HETATM 8234 N  N1  . A1I52 JA 2 .   ? 18.761  -11.353 17.393  1.00 33.37  0  301 A1I52 D N1  1 
HETATM 8235 O  O1  . A1I52 JA 2 .   ? 18.367  -14.741 18.712  1.00 29.67  0  301 A1I52 D O1  1 
HETATM 8236 N  N2  . A1I52 JA 2 .   ? 17.055  -14.488 16.253  1.00 40.57  0  301 A1I52 D N2  1 
HETATM 8237 O  O2  . A1I52 JA 2 .   ? 15.911  -14.201 15.421  1.00 47.21  0  301 A1I52 D O2  1 
HETATM 8238 N  N3  . A1I52 JA 2 .   ? 15.830  -12.801 17.116  1.00 37.99  0  301 A1I52 D N3  1 
HETATM 8239 O  O3  . A1I52 JA 2 .   ? 9.230   -15.717 15.810  1.00 43.23  0  301 A1I52 D O3  1 
HETATM 8240 C  C9  . A1I52 JA 2 .   ? 17.853  -6.931  15.257  1.00 42.04  0  301 A1I52 D C9  1 
HETATM 8241 C  C10 . A1I52 JA 2 .   ? 16.993  -7.618  16.105  1.00 40.18  0  301 A1I52 D C10 1 
HETATM 8242 C  C13 . A1I52 JA 2 .   ? 16.923  -13.625 17.220  1.00 35.15  0  301 A1I52 D C13 1 
HETATM 8243 C  C14 . A1I52 JA 2 .   ? 15.248  -13.214 16.036  1.00 36.73  0  301 A1I52 D C14 1 
HETATM 8244 C  C20 . A1I52 JA 2 .   ? 7.922   -15.043 15.913  1.00 39.66  0  301 A1I52 D C20 1 
HETATM 8245 C  C22 . A1I52 JA 2 .   ? 5.721   -15.942 17.060  1.00 42.98  0  301 A1I52 D C22 1 
HETATM 8246 C  C25 . A1I52 JA 2 .   ? 3.407   -15.675 18.598  1.00 56.93  0  301 A1I52 D C25 1 
HETATM 8247 C  C26 A A1I52 JA 2 .   ? 4.591   -15.089 19.008  0.70 51.55  0  301 A1I52 D C26 1 
HETATM 8248 C  C26 B A1I52 JA 2 .   ? 3.314   -15.861 17.226  0.30 54.45  0  301 A1I52 D C26 1 
HETATM 8249 C  C28 . A1I52 JA 2 .   ? 10.564  -13.790 16.465  1.00 40.37  0  301 A1I52 D C28 1 
HETATM 8250 C  C29 . A1I52 JA 2 .   ? 11.735  -13.055 16.334  1.00 44.30  0  301 A1I52 D C29 1 
HETATM 8251 F  F   . A1I52 JA 2 .   ? 17.604  -5.625  15.002  1.00 50.65  0  301 A1I52 D F   1 
HETATM 8252 S  S   . SO4   KA 3 .   ? 39.194  -16.181 24.654  1.00 75.00  0  302 SO4   D S   1 
HETATM 8253 O  O1  . SO4   KA 3 .   ? 40.206  -15.306 24.128  1.00 83.15  0  302 SO4   D O1  1 
HETATM 8254 O  O2  . SO4   KA 3 .   ? 37.957  -15.453 24.701  1.00 71.74  0  302 SO4   D O2  1 
HETATM 8255 O  O3  . SO4   KA 3 .   ? 39.061  -17.358 23.823  1.00 76.25  -1 302 SO4   D O3  1 
HETATM 8256 O  O4  . SO4   KA 3 .   ? 39.558  -16.600 25.977  1.00 81.36  0  302 SO4   D O4  1 
HETATM 8257 S  S   . SO4   LA 3 .   ? 3.697   3.431   38.336  1.00 78.56  0  303 SO4   D S   1 
HETATM 8258 O  O1  . SO4   LA 3 .   ? 4.397   4.315   37.439  1.00 93.27  0  303 SO4   D O1  1 
HETATM 8259 O  O2  . SO4   LA 3 .   ? 2.387   3.135   37.816  1.00 70.95  0  303 SO4   D O2  1 
HETATM 8260 O  O3  . SO4   LA 3 .   ? 4.433   2.180   38.445  1.00 75.11  -1 303 SO4   D O3  1 
HETATM 8261 O  O4  . SO4   LA 3 .   ? 3.585   4.099   39.616  1.00 76.13  0  303 SO4   D O4  1 
HETATM 8262 C  C1  . EDO   MA 5 .   ? 33.525  -20.899 29.253  1.00 64.41  0  304 EDO   D C1  1 
HETATM 8263 O  O1  . EDO   MA 5 .   ? 32.922  -20.403 28.070  1.00 47.30  0  304 EDO   D O1  1 
HETATM 8264 C  C2  . EDO   MA 5 .   ? 33.126  -22.286 29.472  1.00 65.13  0  304 EDO   D C2  1 
HETATM 8265 O  O2  . EDO   MA 5 .   ? 31.828  -22.522 28.972  1.00 70.20  0  304 EDO   D O2  1 
HETATM 8266 S  S   . SO4   NA 3 .   ? 26.836  -22.615 40.242  1.00 110.43 0  305 SO4   D S   1 
HETATM 8267 O  O1  . SO4   NA 3 .   ? 27.102  -22.191 38.888  1.00 117.94 0  305 SO4   D O1  1 
HETATM 8268 O  O2  . SO4   NA 3 .   ? 25.435  -22.425 40.557  1.00 102.26 0  305 SO4   D O2  1 
HETATM 8269 O  O3  . SO4   NA 3 .   ? 27.160  -24.009 40.352  1.00 119.27 -1 305 SO4   D O3  1 
HETATM 8270 O  O4  . SO4   NA 3 .   ? 27.643  -21.851 41.159  1.00 95.85  0  305 SO4   D O4  1 
HETATM 8271 S  S   . SO4   OA 3 .   ? 16.680  -34.379 28.525  1.00 76.82  0  306 SO4   D S   1 
HETATM 8272 O  O1  . SO4   OA 3 .   ? 17.972  -34.908 28.134  1.00 55.78  0  306 SO4   D O1  1 
HETATM 8273 O  O2  . SO4   OA 3 .   ? 16.469  -33.035 28.010  1.00 56.19  0  306 SO4   D O2  1 
HETATM 8274 O  O3  . SO4   OA 3 .   ? 15.663  -35.249 28.004  1.00 80.89  -1 306 SO4   D O3  1 
HETATM 8275 O  O4  . SO4   OA 3 .   ? 16.585  -34.353 29.963  1.00 68.19  0  306 SO4   D O4  1 
HETATM 8276 C  C1  . EDO   PA 5 .   ? 29.666  -22.745 34.440  1.00 63.24  0  307 EDO   D C1  1 
HETATM 8277 O  O1  . EDO   PA 5 .   ? 30.551  -23.824 34.682  1.00 66.16  0  307 EDO   D O1  1 
HETATM 8278 C  C2  . EDO   PA 5 .   ? 29.222  -21.981 35.638  1.00 59.38  0  307 EDO   D C2  1 
HETATM 8279 O  O2  . EDO   PA 5 .   ? 30.237  -21.534 36.510  1.00 61.33  0  307 EDO   D O2  1 
HETATM 8280 C  C1  . PEG   QA 4 .   ? 14.014  3.524   24.686  1.00 48.12  0  308 PEG   D C1  1 
HETATM 8281 O  O1  . PEG   QA 4 .   ? 15.109  4.278   25.184  1.00 50.62  0  308 PEG   D O1  1 
HETATM 8282 C  C2  . PEG   QA 4 .   ? 13.524  4.009   23.360  1.00 52.57  0  308 PEG   D C2  1 
HETATM 8283 O  O2  . PEG   QA 4 .   ? 12.602  5.080   23.561  1.00 58.30  0  308 PEG   D O2  1 
HETATM 8284 C  C3  . PEG   QA 4 .   ? 11.824  5.419   22.416  1.00 55.45  0  308 PEG   D C3  1 
HETATM 8285 C  C4  . PEG   QA 4 .   ? 11.290  6.823   22.555  1.00 57.83  0  308 PEG   D C4  1 
HETATM 8286 O  O4  . PEG   QA 4 .   ? 10.775  7.099   23.856  1.00 55.84  0  308 PEG   D O4  1 
HETATM 8287 C  C1  . EDO   RA 5 .   ? 32.478  10.482  20.095  1.00 48.51  0  309 EDO   D C1  1 
HETATM 8288 O  O1  . EDO   RA 5 .   ? 31.974  9.842   21.229  1.00 50.63  0  309 EDO   D O1  1 
HETATM 8289 C  C2  . EDO   RA 5 .   ? 33.860  10.041  19.799  1.00 52.07  0  309 EDO   D C2  1 
HETATM 8290 O  O2  . EDO   RA 5 .   ? 34.637  11.025  19.115  1.00 51.15  0  309 EDO   D O2  1 
HETATM 8291 C  C1  . EDO   SA 5 .   ? 38.872  -9.689  20.150  1.00 62.90  0  310 EDO   D C1  1 
HETATM 8292 O  O1  . EDO   SA 5 .   ? 37.948  -10.368 19.342  1.00 51.94  0  310 EDO   D O1  1 
HETATM 8293 C  C2  . EDO   SA 5 .   ? 39.924  -10.626 20.620  1.00 65.41  0  310 EDO   D C2  1 
HETATM 8294 O  O2  . EDO   SA 5 .   ? 40.429  -10.376 21.919  1.00 70.14  0  310 EDO   D O2  1 
HETATM 8295 O  O   . HOH   TA 8 .   ? 26.317  -42.792 -12.647 0.50 32.46  0  401 HOH   A O   1 
HETATM 8296 O  O   . HOH   TA 8 .   ? 15.780  -13.123 -30.301 1.00 36.96  0  402 HOH   A O   1 
HETATM 8297 O  O   . HOH   TA 8 .   ? 7.565   -34.534 -15.732 1.00 59.72  0  403 HOH   A O   1 
HETATM 8298 O  O   . HOH   TA 8 .   ? 25.356  -51.995 -31.333 1.00 49.49  0  404 HOH   A O   1 
HETATM 8299 O  O   . HOH   TA 8 .   ? 31.404  -56.252 -23.280 1.00 50.48  0  405 HOH   A O   1 
HETATM 8300 O  O   . HOH   TA 8 .   ? -0.065  -38.736 -26.504 1.00 41.69  0  406 HOH   A O   1 
HETATM 8301 O  O   . HOH   TA 8 .   ? 23.248  -42.796 -34.637 1.00 28.58  0  407 HOH   A O   1 
HETATM 8302 O  O   . HOH   TA 8 .   ? 22.716  -28.003 -12.182 1.00 30.70  0  408 HOH   A O   1 
HETATM 8303 O  O   . HOH   TA 8 .   ? 13.915  -12.669 -26.518 1.00 50.55  0  409 HOH   A O   1 
HETATM 8304 O  O   . HOH   TA 8 .   ? 3.628   -43.915 -29.936 1.00 31.13  0  410 HOH   A O   1 
HETATM 8305 O  O   . HOH   TA 8 .   ? 13.375  -32.637 -39.977 1.00 28.47  0  411 HOH   A O   1 
HETATM 8306 O  O   . HOH   TA 8 .   ? 29.154  -54.392 -6.492  1.00 37.69  0  412 HOH   A O   1 
HETATM 8307 O  O   . HOH   TA 8 .   ? 6.349   -14.900 -21.701 1.00 29.41  0  413 HOH   A O   1 
HETATM 8308 O  O   . HOH   TA 8 .   ? 19.781  -29.283 -40.999 1.00 35.25  0  414 HOH   A O   1 
HETATM 8309 O  O   . HOH   TA 8 .   ? -0.516  -25.637 -25.076 1.00 27.79  0  415 HOH   A O   1 
HETATM 8310 O  O   . HOH   TA 8 .   ? -2.955  -29.799 -34.173 1.00 37.73  0  416 HOH   A O   1 
HETATM 8311 O  O   . HOH   TA 8 .   ? 21.193  -47.862 -17.878 1.00 37.23  0  417 HOH   A O   1 
HETATM 8312 O  O   . HOH   TA 8 .   ? 15.121  -19.646 -17.258 1.00 45.36  0  418 HOH   A O   1 
HETATM 8313 O  O   . HOH   TA 8 .   ? 2.818   -43.169 -25.472 1.00 30.04  0  419 HOH   A O   1 
HETATM 8314 O  O   . HOH   TA 8 .   ? 33.671  -36.049 -31.890 1.00 46.24  0  420 HOH   A O   1 
HETATM 8315 O  O   . HOH   TA 8 .   ? 28.337  -42.526 -28.435 1.00 33.41  0  421 HOH   A O   1 
HETATM 8316 O  O   . HOH   TA 8 .   ? 2.471   -22.747 -34.084 1.00 24.94  0  422 HOH   A O   1 
HETATM 8317 O  O   . HOH   TA 8 .   ? 23.213  -34.665 -15.297 1.00 34.97  0  423 HOH   A O   1 
HETATM 8318 O  O   . HOH   TA 8 .   ? 16.731  -15.608 -31.978 1.00 47.61  0  424 HOH   A O   1 
HETATM 8319 O  O   . HOH   TA 8 .   ? 27.814  -33.198 -23.473 1.00 28.22  0  425 HOH   A O   1 
HETATM 8320 O  O   . HOH   TA 8 .   ? -0.641  -18.044 -23.825 1.00 42.06  0  426 HOH   A O   1 
HETATM 8321 O  O   . HOH   TA 8 .   ? 31.759  -52.039 -18.098 1.00 41.26  0  427 HOH   A O   1 
HETATM 8322 O  O   . HOH   TA 8 .   ? 32.919  -38.403 -11.194 1.00 40.29  0  428 HOH   A O   1 
HETATM 8323 O  O   B HOH   TA 8 .   ? 5.322   -42.898 -11.984 0.50 27.17  0  429 HOH   A O   1 
HETATM 8324 O  O   . HOH   TA 8 .   ? 28.514  -53.411 -19.610 1.00 27.49  0  430 HOH   A O   1 
HETATM 8325 O  O   . HOH   TA 8 .   ? 25.174  -18.419 -12.040 1.00 39.79  0  431 HOH   A O   1 
HETATM 8326 O  O   . HOH   TA 8 .   ? 23.418  -22.587 -21.108 1.00 26.25  0  432 HOH   A O   1 
HETATM 8327 O  O   . HOH   TA 8 .   ? 11.691  -43.902 -41.217 1.00 48.97  0  433 HOH   A O   1 
HETATM 8328 O  O   . HOH   TA 8 .   ? 24.039  -12.064 -23.770 1.00 41.04  0  434 HOH   A O   1 
HETATM 8329 O  O   . HOH   TA 8 .   ? 35.251  -49.652 -16.410 1.00 30.72  0  435 HOH   A O   1 
HETATM 8330 O  O   . HOH   TA 8 .   ? 21.630  -40.528 -34.034 1.00 24.97  0  436 HOH   A O   1 
HETATM 8331 O  O   . HOH   TA 8 .   ? 22.563  -27.894 -42.659 1.00 41.56  0  437 HOH   A O   1 
HETATM 8332 O  O   . HOH   TA 8 .   ? 18.802  -19.527 -15.691 1.00 29.01  0  438 HOH   A O   1 
HETATM 8333 O  O   . HOH   TA 8 .   ? -5.206  -21.247 -30.036 1.00 28.32  0  439 HOH   A O   1 
HETATM 8334 O  O   . HOH   TA 8 .   ? 24.292  -31.220 -11.807 1.00 33.79  0  440 HOH   A O   1 
HETATM 8335 O  O   . HOH   TA 8 .   ? 12.154  -18.225 -11.224 1.00 44.49  0  441 HOH   A O   1 
HETATM 8336 O  O   . HOH   TA 8 .   ? 5.987   -37.289 -15.219 1.00 31.56  0  442 HOH   A O   1 
HETATM 8337 O  O   . HOH   TA 8 .   ? 7.868   -18.554 -30.849 1.00 26.62  0  443 HOH   A O   1 
HETATM 8338 O  O   . HOH   TA 8 .   ? -1.458  -34.960 -26.189 1.00 30.35  0  444 HOH   A O   1 
HETATM 8339 O  O   . HOH   TA 8 .   ? 32.917  -49.486 -0.586  1.00 35.60  0  445 HOH   A O   1 
HETATM 8340 O  O   . HOH   TA 8 .   ? 32.264  -51.455 -11.421 1.00 34.37  0  446 HOH   A O   1 
HETATM 8341 O  O   . HOH   TA 8 .   ? 10.465  -37.916 -15.949 1.00 33.73  0  447 HOH   A O   1 
HETATM 8342 O  O   . HOH   TA 8 .   ? 32.834  -32.523 -31.762 1.00 34.51  0  448 HOH   A O   1 
HETATM 8343 O  O   . HOH   TA 8 .   ? 12.379  -45.922 -20.060 1.00 23.78  0  449 HOH   A O   1 
HETATM 8344 O  O   . HOH   TA 8 .   ? 29.124  -35.315 -15.671 1.00 29.54  0  450 HOH   A O   1 
HETATM 8345 O  O   . HOH   TA 8 .   ? 30.248  -22.896 -18.263 1.00 32.26  0  451 HOH   A O   1 
HETATM 8346 O  O   . HOH   TA 8 .   ? 42.973  -32.016 -18.960 1.00 53.29  0  452 HOH   A O   1 
HETATM 8347 O  O   . HOH   TA 8 .   ? 28.093  -44.849 -12.167 1.00 35.97  0  453 HOH   A O   1 
HETATM 8348 O  O   . HOH   TA 8 .   ? 10.769  -17.481 -45.442 1.00 48.71  0  454 HOH   A O   1 
HETATM 8349 O  O   . HOH   TA 8 .   ? 32.786  -35.620 -18.254 1.00 36.55  0  455 HOH   A O   1 
HETATM 8350 O  O   . HOH   TA 8 .   ? 4.533   -31.628 -44.471 1.00 44.72  0  456 HOH   A O   1 
HETATM 8351 O  O   . HOH   TA 8 .   ? 38.555  -43.327 -17.806 1.00 49.79  0  457 HOH   A O   1 
HETATM 8352 O  O   . HOH   TA 8 .   ? 18.301  -41.864 -22.394 1.00 25.82  0  458 HOH   A O   1 
HETATM 8353 O  O   . HOH   TA 8 .   ? 18.668  -27.341 -25.039 1.00 19.87  0  459 HOH   A O   1 
HETATM 8354 O  O   . HOH   TA 8 .   ? 19.495  -16.988 -13.350 1.00 45.15  0  460 HOH   A O   1 
HETATM 8355 O  O   . HOH   TA 8 .   ? 26.869  -35.396 -17.937 1.00 31.70  0  461 HOH   A O   1 
HETATM 8356 O  O   . HOH   TA 8 .   ? 16.063  -45.063 -13.681 1.00 26.84  0  462 HOH   A O   1 
HETATM 8357 O  O   . HOH   TA 8 .   ? 0.590   -23.253 -32.033 1.00 26.15  0  463 HOH   A O   1 
HETATM 8358 O  O   . HOH   TA 8 .   ? 17.606  -48.574 -23.723 1.00 31.79  0  464 HOH   A O   1 
HETATM 8359 O  O   . HOH   TA 8 .   ? 27.303  -54.739 -21.606 1.00 33.25  0  465 HOH   A O   1 
HETATM 8360 O  O   . HOH   TA 8 .   ? 25.607  -49.106 -25.780 1.00 27.21  0  466 HOH   A O   1 
HETATM 8361 O  O   . HOH   TA 8 .   ? 36.637  -46.329 -21.431 1.00 47.17  0  467 HOH   A O   1 
HETATM 8362 O  O   . HOH   TA 8 .   ? 12.642  -25.531 -42.374 1.00 30.43  0  468 HOH   A O   1 
HETATM 8363 O  O   . HOH   TA 8 .   ? 15.728  -31.741 -29.745 1.00 26.20  0  469 HOH   A O   1 
HETATM 8364 O  O   . HOH   TA 8 .   ? 14.063  -40.040 -16.167 1.00 22.75  0  470 HOH   A O   1 
HETATM 8365 O  O   . HOH   TA 8 .   ? 11.658  -46.293 -34.260 1.00 39.81  0  471 HOH   A O   1 
HETATM 8366 O  O   . HOH   TA 8 .   ? 17.722  -23.166 -17.385 1.00 36.96  0  472 HOH   A O   1 
HETATM 8367 O  O   . HOH   TA 8 .   ? 23.563  -35.084 -21.895 1.00 31.92  0  473 HOH   A O   1 
HETATM 8368 O  O   . HOH   TA 8 .   ? 13.381  -22.189 -33.604 1.00 25.34  0  474 HOH   A O   1 
HETATM 8369 O  O   . HOH   TA 8 .   ? 2.073   -40.477 -26.290 1.00 43.62  0  475 HOH   A O   1 
HETATM 8370 O  O   . HOH   TA 8 .   ? 21.776  -26.720 -32.138 1.00 30.01  0  476 HOH   A O   1 
HETATM 8371 O  O   . HOH   TA 8 .   ? 36.773  -37.944 -17.572 1.00 40.45  0  477 HOH   A O   1 
HETATM 8372 O  O   . HOH   TA 8 .   ? 5.927   -43.221 -21.956 1.00 30.94  0  478 HOH   A O   1 
HETATM 8373 O  O   . HOH   TA 8 .   ? 34.868  -37.787 -21.826 1.00 47.62  0  479 HOH   A O   1 
HETATM 8374 O  O   . HOH   TA 8 .   ? 17.769  -25.411 -23.256 1.00 22.15  0  480 HOH   A O   1 
HETATM 8375 O  O   . HOH   TA 8 .   ? 40.128  -34.643 -20.786 1.00 59.90  0  481 HOH   A O   1 
HETATM 8376 O  O   . HOH   TA 8 .   ? 30.897  -34.565 -19.769 1.00 34.09  0  482 HOH   A O   1 
HETATM 8377 O  O   . HOH   TA 8 .   ? 17.512  -34.470 -12.775 1.00 52.96  0  483 HOH   A O   1 
HETATM 8378 O  O   . HOH   TA 8 .   ? 29.248  -51.552 -23.342 1.00 33.99  0  484 HOH   A O   1 
HETATM 8379 O  O   . HOH   TA 8 .   ? 5.426   -18.422 -37.653 1.00 38.93  0  485 HOH   A O   1 
HETATM 8380 O  O   . HOH   TA 8 .   ? -3.945  -33.910 -27.045 1.00 37.86  0  486 HOH   A O   1 
HETATM 8381 O  O   . HOH   TA 8 .   ? 10.660  -47.268 -31.680 1.00 28.99  0  487 HOH   A O   1 
HETATM 8382 O  O   . HOH   TA 8 .   ? 10.278  -50.116 -36.721 1.00 58.99  0  488 HOH   A O   1 
HETATM 8383 O  O   . HOH   TA 8 .   ? 32.335  -56.347 -12.446 1.00 39.45  0  489 HOH   A O   1 
HETATM 8384 O  O   . HOH   TA 8 .   ? 28.839  -55.656 -27.075 1.00 35.70  0  490 HOH   A O   1 
HETATM 8385 O  O   . HOH   TA 8 .   ? 29.238  -45.887 -30.321 1.00 38.07  0  491 HOH   A O   1 
HETATM 8386 O  O   . HOH   TA 8 .   ? 19.860  -22.123 -16.008 1.00 36.37  0  492 HOH   A O   1 
HETATM 8387 O  O   . HOH   TA 8 .   ? -0.605  -43.208 -31.792 1.00 55.56  0  493 HOH   A O   1 
HETATM 8388 O  O   . HOH   TA 8 .   ? 24.385  -14.601 -18.872 1.00 38.62  0  494 HOH   A O   1 
HETATM 8389 O  O   . HOH   TA 8 .   ? 20.649  -24.326 -41.570 1.00 45.83  0  495 HOH   A O   1 
HETATM 8390 O  O   . HOH   TA 8 .   ? -1.939  -21.479 -39.599 1.00 41.93  0  496 HOH   A O   1 
HETATM 8391 O  O   . HOH   TA 8 .   ? 17.161  -53.378 -17.854 1.00 45.75  0  497 HOH   A O   1 
HETATM 8392 O  O   . HOH   TA 8 .   ? 35.268  -50.874 -13.789 1.00 41.02  0  498 HOH   A O   1 
HETATM 8393 O  O   . HOH   TA 8 .   ? 11.384  -40.343 -15.491 1.00 31.15  0  499 HOH   A O   1 
HETATM 8394 O  O   . HOH   TA 8 .   ? 35.592  -43.034 -28.072 1.00 34.40  0  500 HOH   A O   1 
HETATM 8395 O  O   . HOH   TA 8 .   ? 35.269  -32.374 -30.686 1.00 41.91  0  501 HOH   A O   1 
HETATM 8396 O  O   . HOH   TA 8 .   ? 3.509   -14.753 -25.941 1.00 32.43  0  502 HOH   A O   1 
HETATM 8397 O  O   . HOH   TA 8 .   ? 5.804   -15.146 -18.999 1.00 26.34  0  503 HOH   A O   1 
HETATM 8398 O  O   . HOH   TA 8 .   ? 21.437  -50.024 -16.438 1.00 36.36  0  504 HOH   A O   1 
HETATM 8399 O  O   . HOH   TA 8 .   ? 22.683  -20.343 -9.440  1.00 36.35  0  505 HOH   A O   1 
HETATM 8400 O  O   . HOH   TA 8 .   ? 14.600  -34.575 -41.622 1.00 32.12  0  506 HOH   A O   1 
HETATM 8401 O  O   . HOH   TA 8 .   ? 10.782  -48.588 -19.545 1.00 33.88  0  507 HOH   A O   1 
HETATM 8402 O  O   . HOH   TA 8 .   ? 25.121  -13.916 -36.435 1.00 45.99  0  508 HOH   A O   1 
HETATM 8403 O  O   . HOH   TA 8 .   ? 22.722  -35.687 -12.255 1.00 36.14  0  509 HOH   A O   1 
HETATM 8404 O  O   . HOH   TA 8 .   ? 38.005  -34.892 -19.326 1.00 39.95  0  510 HOH   A O   1 
HETATM 8405 O  O   . HOH   TA 8 .   ? -4.659  -31.508 -21.767 1.00 39.33  0  511 HOH   A O   1 
HETATM 8406 O  O   . HOH   TA 8 .   ? 7.774   -12.275 -21.679 1.00 48.52  0  512 HOH   A O   1 
HETATM 8407 O  O   . HOH   TA 8 .   ? 28.445  -42.521 -31.282 1.00 35.09  0  513 HOH   A O   1 
HETATM 8408 O  O   . HOH   TA 8 .   ? 14.197  -46.332 -36.306 1.00 42.83  0  514 HOH   A O   1 
HETATM 8409 O  O   . HOH   TA 8 .   ? 17.664  -20.006 -18.112 1.00 32.20  0  515 HOH   A O   1 
HETATM 8410 O  O   . HOH   TA 8 .   ? 17.035  -42.903 -24.504 1.00 25.04  0  516 HOH   A O   1 
HETATM 8411 O  O   . HOH   TA 8 .   ? 23.357  -23.368 -37.397 1.00 30.10  0  517 HOH   A O   1 
HETATM 8412 O  O   . HOH   TA 8 .   ? 30.619  -49.044 -28.872 1.00 34.16  0  518 HOH   A O   1 
HETATM 8413 O  O   . HOH   TA 8 .   ? 12.271  -35.914 -15.323 1.00 37.07  0  519 HOH   A O   1 
HETATM 8414 O  O   . HOH   TA 8 .   ? 14.848  -17.703 -14.334 1.00 52.73  0  520 HOH   A O   1 
HETATM 8415 O  O   . HOH   TA 8 .   ? 30.303  -15.686 -24.949 1.00 38.29  0  521 HOH   A O   1 
HETATM 8416 O  O   . HOH   TA 8 .   ? 25.340  -12.432 -33.411 1.00 49.76  0  522 HOH   A O   1 
HETATM 8417 O  O   . HOH   TA 8 .   ? 11.979  -5.786  -25.401 1.00 56.78  0  523 HOH   A O   1 
HETATM 8418 O  O   . HOH   TA 8 .   ? 33.203  -27.006 -15.339 1.00 55.12  0  524 HOH   A O   1 
HETATM 8419 O  O   . HOH   TA 8 .   ? 36.132  -25.440 -29.514 1.00 53.05  0  525 HOH   A O   1 
HETATM 8420 O  O   . HOH   TA 8 .   ? 9.181   -15.977 -31.762 1.00 39.59  0  526 HOH   A O   1 
HETATM 8421 O  O   . HOH   TA 8 .   ? -0.944  -16.486 -20.124 1.00 49.76  0  527 HOH   A O   1 
HETATM 8422 O  O   . HOH   TA 8 .   ? 36.773  -48.627 -10.023 1.00 51.83  0  528 HOH   A O   1 
HETATM 8423 O  O   . HOH   TA 8 .   ? 14.350  -15.577 -44.892 1.00 48.21  0  529 HOH   A O   1 
HETATM 8424 O  O   . HOH   TA 8 .   ? -1.701  -40.492 -34.690 1.00 45.27  0  530 HOH   A O   1 
HETATM 8425 O  O   . HOH   TA 8 .   ? 26.791  -58.578 -12.256 1.00 48.67  0  531 HOH   A O   1 
HETATM 8426 O  O   . HOH   TA 8 .   ? 28.260  -50.111 -25.433 1.00 38.08  0  532 HOH   A O   1 
HETATM 8427 O  O   . HOH   TA 8 .   ? 37.902  -35.407 -24.654 1.00 47.78  0  533 HOH   A O   1 
HETATM 8428 O  O   . HOH   TA 8 .   ? -1.304  -42.903 -34.229 1.00 52.52  0  534 HOH   A O   1 
HETATM 8429 O  O   . HOH   TA 8 .   ? 36.069  -25.501 -23.034 1.00 51.82  0  535 HOH   A O   1 
HETATM 8430 O  O   . HOH   TA 8 .   ? 2.202   -20.506 -35.339 1.00 29.96  0  536 HOH   A O   1 
HETATM 8431 O  O   . HOH   TA 8 .   ? 22.545  -23.558 -40.009 1.00 37.57  0  537 HOH   A O   1 
HETATM 8432 O  O   . HOH   TA 8 .   ? 34.413  -51.952 -17.813 1.00 44.96  0  538 HOH   A O   1 
HETATM 8433 O  O   . HOH   TA 8 .   ? 20.960  -8.027  -26.779 1.00 50.41  0  539 HOH   A O   1 
HETATM 8434 O  O   . HOH   TA 8 .   ? 29.016  -51.325 -27.989 1.00 51.01  0  540 HOH   A O   1 
HETATM 8435 O  O   . HOH   TA 8 .   ? 1.628   -14.262 -21.394 1.00 52.40  0  541 HOH   A O   1 
HETATM 8436 O  O   . HOH   TA 8 .   ? 37.122  -34.947 -31.208 1.00 48.98  0  542 HOH   A O   1 
HETATM 8437 O  O   . HOH   TA 8 .   ? 37.524  -49.031 -17.695 1.00 41.89  0  543 HOH   A O   1 
HETATM 8438 O  O   . HOH   TA 8 .   ? 2.945   -14.036 -18.959 1.00 52.69  0  544 HOH   A O   1 
HETATM 8439 O  O   . HOH   TA 8 .   ? 15.038  -15.582 -12.972 1.00 49.93  0  545 HOH   A O   1 
HETATM 8440 O  O   . HOH   TA 8 .   ? 20.544  -26.623 -42.507 1.00 49.40  0  546 HOH   A O   1 
HETATM 8441 O  O   . HOH   TA 8 .   ? 37.516  -48.769 -22.080 1.00 48.59  0  547 HOH   A O   1 
HETATM 8442 O  O   . HOH   TA 8 .   ? 4.009   -14.121 -23.146 1.00 34.67  0  548 HOH   A O   1 
HETATM 8443 O  O   . HOH   TA 8 .   ? 16.450  -19.814 -13.319 1.00 52.53  0  549 HOH   A O   1 
HETATM 8444 O  O   . HOH   UA 8 .   ? 32.974  17.640  0.218   1.00 39.98  0  401 HOH   B O   1 
HETATM 8445 O  O   . HOH   UA 8 .   ? 23.699  -3.231  3.108   1.00 51.14  0  402 HOH   B O   1 
HETATM 8446 O  O   . HOH   UA 8 .   ? 26.445  22.832  3.244   1.00 56.08  0  403 HOH   B O   1 
HETATM 8447 O  O   . HOH   UA 8 .   ? 3.542   11.416  5.034   1.00 41.75  0  404 HOH   B O   1 
HETATM 8448 O  O   . HOH   UA 8 .   ? 0.895   5.734   -17.804 1.00 49.13  0  405 HOH   B O   1 
HETATM 8449 O  O   . HOH   UA 8 .   ? 7.789   -8.145  2.171   1.00 36.81  0  406 HOH   B O   1 
HETATM 8450 O  O   . HOH   UA 8 .   ? 17.363  15.994  12.283  1.00 32.03  0  407 HOH   B O   1 
HETATM 8451 O  O   . HOH   UA 8 .   ? 15.242  22.275  -3.899  1.00 49.48  0  408 HOH   B O   1 
HETATM 8452 O  O   B HOH   UA 8 .   ? 26.239  -2.582  12.721  0.50 44.18  0  409 HOH   B O   1 
HETATM 8453 O  O   . HOH   UA 8 .   ? 18.209  13.474  11.171  1.00 38.33  0  410 HOH   B O   1 
HETATM 8454 O  O   . HOH   UA 8 .   ? 23.543  3.063   -17.962 1.00 30.09  0  411 HOH   B O   1 
HETATM 8455 O  O   . HOH   UA 8 .   ? 4.059   2.951   -1.010  1.00 30.07  0  412 HOH   B O   1 
HETATM 8456 O  O   . HOH   UA 8 .   ? -5.957  3.769   -4.484  1.00 51.99  0  413 HOH   B O   1 
HETATM 8457 O  O   . HOH   UA 8 .   ? 16.680  -8.659  -10.580 1.00 36.37  0  414 HOH   B O   1 
HETATM 8458 O  O   . HOH   UA 8 .   ? -3.281  4.295   16.399  1.00 44.51  0  415 HOH   B O   1 
HETATM 8459 O  O   . HOH   UA 8 .   ? 1.504   -6.838  -7.741  1.00 29.47  0  416 HOH   B O   1 
HETATM 8460 O  O   . HOH   UA 8 .   ? 7.953   17.378  2.147   1.00 38.14  0  417 HOH   B O   1 
HETATM 8461 O  O   . HOH   UA 8 .   ? 3.188   8.540   18.412  1.00 35.73  0  418 HOH   B O   1 
HETATM 8462 O  O   . HOH   UA 8 .   ? 9.232   -9.425  -0.490  1.00 28.51  0  419 HOH   B O   1 
HETATM 8463 O  O   . HOH   UA 8 .   ? 0.719   -6.457  11.163  1.00 45.54  0  420 HOH   B O   1 
HETATM 8464 O  O   . HOH   UA 8 .   ? -1.201  -9.800  23.597  1.00 33.05  0  421 HOH   B O   1 
HETATM 8465 O  O   . HOH   UA 8 .   ? 12.029  -8.681  -7.464  1.00 33.59  0  422 HOH   B O   1 
HETATM 8466 O  O   . HOH   UA 8 .   ? 10.651  4.216   14.115  1.00 27.71  0  423 HOH   B O   1 
HETATM 8467 O  O   . HOH   UA 8 .   ? 7.702   -6.520  -20.468 1.00 38.94  0  424 HOH   B O   1 
HETATM 8468 O  O   . HOH   UA 8 .   ? -1.070  -0.755  3.401   1.00 33.53  0  425 HOH   B O   1 
HETATM 8469 O  O   . HOH   UA 8 .   ? 10.629  18.874  5.300   1.00 37.62  0  426 HOH   B O   1 
HETATM 8470 O  O   . HOH   UA 8 .   ? 19.438  6.129   11.505  1.00 24.87  0  427 HOH   B O   1 
HETATM 8471 O  O   . HOH   UA 8 .   ? 0.450   7.467   17.051  1.00 49.69  0  428 HOH   B O   1 
HETATM 8472 O  O   . HOH   UA 8 .   ? 7.019   -12.831 -18.219 1.00 39.14  0  429 HOH   B O   1 
HETATM 8473 O  O   . HOH   UA 8 .   ? 34.296  13.485  -4.461  1.00 45.91  0  430 HOH   B O   1 
HETATM 8474 O  O   . HOH   UA 8 .   ? 11.694  16.927  -12.883 1.00 38.89  0  431 HOH   B O   1 
HETATM 8475 O  O   . HOH   UA 8 .   ? 14.662  2.580   -20.885 1.00 48.24  0  432 HOH   B O   1 
HETATM 8476 O  O   . HOH   UA 8 .   ? 28.933  9.146   6.416   1.00 37.30  0  433 HOH   B O   1 
HETATM 8477 O  O   . HOH   UA 8 .   ? 19.369  -14.671 -9.681  1.00 45.81  0  434 HOH   B O   1 
HETATM 8478 O  O   . HOH   UA 8 .   ? 3.560   -1.956  14.153  1.00 27.50  0  435 HOH   B O   1 
HETATM 8479 O  O   . HOH   UA 8 .   ? 23.435  23.204  1.577   1.00 39.65  0  436 HOH   B O   1 
HETATM 8480 O  O   . HOH   UA 8 .   ? 32.818  6.226   -1.374  1.00 40.21  0  437 HOH   B O   1 
HETATM 8481 O  O   . HOH   UA 8 .   ? 28.517  8.275   -15.653 1.00 38.22  0  438 HOH   B O   1 
HETATM 8482 O  O   . HOH   UA 8 .   ? 23.734  -7.857  -19.346 1.00 46.94  0  439 HOH   B O   1 
HETATM 8483 O  O   . HOH   UA 8 .   ? 31.869  9.949   1.200   1.00 41.25  0  440 HOH   B O   1 
HETATM 8484 O  O   . HOH   UA 8 .   ? 27.660  14.281  5.145   1.00 33.87  0  441 HOH   B O   1 
HETATM 8485 O  O   . HOH   UA 8 .   ? 32.082  1.772   -9.226  1.00 36.44  0  442 HOH   B O   1 
HETATM 8486 O  O   . HOH   UA 8 .   ? 3.013   -3.166  4.229   1.00 30.83  0  443 HOH   B O   1 
HETATM 8487 O  O   . HOH   UA 8 .   ? -0.627  -5.644  8.898   1.00 38.55  0  444 HOH   B O   1 
HETATM 8488 O  O   . HOH   UA 8 .   ? 15.687  8.040   -5.370  1.00 26.59  0  445 HOH   B O   1 
HETATM 8489 O  O   . HOH   UA 8 .   ? 8.526   -3.836  -9.548  1.00 29.46  0  446 HOH   B O   1 
HETATM 8490 O  O   . HOH   UA 8 .   ? 3.252   -4.685  -10.000 1.00 34.63  0  447 HOH   B O   1 
HETATM 8491 O  O   . HOH   UA 8 .   ? -0.611  0.754   20.109  1.00 36.54  0  448 HOH   B O   1 
HETATM 8492 O  O   . HOH   UA 8 .   ? 25.775  6.284   8.238   1.00 40.64  0  449 HOH   B O   1 
HETATM 8493 O  O   . HOH   UA 8 .   ? 13.177  -9.993  -9.854  1.00 38.27  0  450 HOH   B O   1 
HETATM 8494 O  O   . HOH   UA 8 .   ? 5.131   -1.029  3.191   1.00 34.94  0  451 HOH   B O   1 
HETATM 8495 O  O   . HOH   UA 8 .   ? 6.098   12.188  12.041  1.00 35.63  0  452 HOH   B O   1 
HETATM 8496 O  O   . HOH   UA 8 .   ? 8.858   -3.753  3.543   1.00 36.68  0  453 HOH   B O   1 
HETATM 8497 O  O   . HOH   UA 8 .   ? 13.468  6.091   6.977   1.00 26.45  0  454 HOH   B O   1 
HETATM 8498 O  O   . HOH   UA 8 .   ? 20.565  -0.604  8.944   1.00 35.35  0  455 HOH   B O   1 
HETATM 8499 O  O   . HOH   UA 8 .   ? 9.594   15.824  0.506   1.00 27.32  0  456 HOH   B O   1 
HETATM 8500 O  O   . HOH   UA 8 .   ? 15.998  -0.243  13.755  1.00 26.63  0  457 HOH   B O   1 
HETATM 8501 O  O   . HOH   UA 8 .   ? 12.989  1.759   -7.251  1.00 22.90  0  458 HOH   B O   1 
HETATM 8502 O  O   . HOH   UA 8 .   ? 18.118  7.137   -15.661 1.00 30.60  0  459 HOH   B O   1 
HETATM 8503 O  O   . HOH   UA 8 .   ? 25.591  -6.548  -16.934 1.00 37.65  0  460 HOH   B O   1 
HETATM 8504 O  O   . HOH   UA 8 .   ? 9.567   7.702   -10.817 1.00 32.67  0  461 HOH   B O   1 
HETATM 8505 O  O   . HOH   UA 8 .   ? 0.875   0.120   1.723   1.00 27.96  0  462 HOH   B O   1 
HETATM 8506 O  O   . HOH   UA 8 .   ? 8.321   2.449   1.053   1.00 29.12  0  463 HOH   B O   1 
HETATM 8507 O  O   . HOH   UA 8 .   ? 9.310   -15.222 -6.175  1.00 44.50  0  464 HOH   B O   1 
HETATM 8508 O  O   . HOH   UA 8 .   ? 25.916  -2.315  6.246   1.00 34.27  0  465 HOH   B O   1 
HETATM 8509 O  O   . HOH   UA 8 .   ? 29.614  8.590   3.591   1.00 42.50  0  466 HOH   B O   1 
HETATM 8510 O  O   . HOH   UA 8 .   ? 30.417  6.900   -14.263 1.00 31.65  0  467 HOH   B O   1 
HETATM 8511 O  O   . HOH   UA 8 .   ? 28.041  -2.789  -18.943 1.00 38.59  0  468 HOH   B O   1 
HETATM 8512 O  O   . HOH   UA 8 .   ? -7.429  -0.260  -1.730  1.00 49.14  0  469 HOH   B O   1 
HETATM 8513 O  O   . HOH   UA 8 .   ? 14.158  -7.613  -10.594 1.00 34.82  0  470 HOH   B O   1 
HETATM 8514 O  O   . HOH   UA 8 .   ? 7.994   10.695  -16.336 1.00 30.76  0  471 HOH   B O   1 
HETATM 8515 O  O   . HOH   UA 8 .   ? 14.093  -0.604  -8.192  1.00 20.37  0  472 HOH   B O   1 
HETATM 8516 O  O   . HOH   UA 8 .   ? -1.179  2.932   -10.761 1.00 40.23  0  473 HOH   B O   1 
HETATM 8517 O  O   . HOH   UA 8 .   ? 21.120  -1.403  6.351   1.00 49.07  0  474 HOH   B O   1 
HETATM 8518 O  O   . HOH   UA 8 .   ? 8.398   9.474   20.481  1.00 35.57  0  475 HOH   B O   1 
HETATM 8519 O  O   . HOH   UA 8 .   ? 7.573   -9.499  -15.847 1.00 48.83  0  476 HOH   B O   1 
HETATM 8520 O  O   . HOH   UA 8 .   ? 16.507  -2.366  10.312  1.00 37.94  0  477 HOH   B O   1 
HETATM 8521 O  O   . HOH   UA 8 .   ? 25.969  -8.732  -15.502 1.00 27.39  0  478 HOH   B O   1 
HETATM 8522 O  O   . HOH   UA 8 .   ? 31.891  -3.252  -15.297 1.00 53.38  0  479 HOH   B O   1 
HETATM 8523 O  O   . HOH   UA 8 .   ? 14.736  8.517   6.782   1.00 24.79  0  480 HOH   B O   1 
HETATM 8524 O  O   . HOH   UA 8 .   ? -0.629  3.602   24.354  1.00 46.03  0  481 HOH   B O   1 
HETATM 8525 O  O   . HOH   UA 8 .   ? 18.203  16.700  -17.015 1.00 35.19  0  482 HOH   B O   1 
HETATM 8526 O  O   . HOH   UA 8 .   ? -3.725  11.403  5.601   1.00 46.69  0  483 HOH   B O   1 
HETATM 8527 O  O   . HOH   UA 8 .   ? 12.012  7.714   -20.194 1.00 40.13  0  484 HOH   B O   1 
HETATM 8528 O  O   . HOH   UA 8 .   ? 14.375  -7.126  -7.407  1.00 43.58  0  485 HOH   B O   1 
HETATM 8529 O  O   . HOH   UA 8 .   ? 26.226  21.753  -12.213 1.00 49.06  0  486 HOH   B O   1 
HETATM 8530 O  O   . HOH   UA 8 .   ? 9.442   -5.715  6.080   1.00 44.39  0  487 HOH   B O   1 
HETATM 8531 O  O   . HOH   UA 8 .   ? 1.722   14.931  10.345  1.00 44.85  0  488 HOH   B O   1 
HETATM 8532 O  O   . HOH   UA 8 .   ? 16.867  19.723  -8.711  1.00 48.11  0  489 HOH   B O   1 
HETATM 8533 O  O   . HOH   UA 8 .   ? 17.797  -0.489  8.121   1.00 33.50  0  490 HOH   B O   1 
HETATM 8534 O  O   . HOH   UA 8 .   ? -4.857  -1.498  18.190  1.00 45.52  0  491 HOH   B O   1 
HETATM 8535 O  O   . HOH   UA 8 .   ? 9.621   12.709  14.778  1.00 34.20  0  492 HOH   B O   1 
HETATM 8536 O  O   . HOH   UA 8 .   ? 6.178   5.514   -24.364 1.00 46.74  0  493 HOH   B O   1 
HETATM 8537 O  O   . HOH   UA 8 .   ? 29.441  17.842  -9.001  1.00 44.45  0  494 HOH   B O   1 
HETATM 8538 O  O   . HOH   UA 8 .   ? 2.552   15.184  7.116   1.00 41.76  0  495 HOH   B O   1 
HETATM 8539 O  O   . HOH   UA 8 .   ? 36.290  1.535   -2.003  1.00 38.69  0  496 HOH   B O   1 
HETATM 8540 O  O   . HOH   UA 8 .   ? -3.898  -1.418  -8.145  1.00 54.78  0  497 HOH   B O   1 
HETATM 8541 O  O   . HOH   UA 8 .   ? 10.917  11.049  16.667  1.00 43.13  0  498 HOH   B O   1 
HETATM 8542 O  O   . HOH   UA 8 .   ? 5.801   2.717   -24.437 1.00 55.23  0  499 HOH   B O   1 
HETATM 8543 O  O   . HOH   UA 8 .   ? 32.094  -12.738 -8.125  1.00 58.19  0  500 HOH   B O   1 
HETATM 8544 O  O   . HOH   UA 8 .   ? -3.688  2.257   18.483  1.00 39.82  0  501 HOH   B O   1 
HETATM 8545 O  O   . HOH   UA 8 .   ? 19.229  18.950  5.562   1.00 50.61  0  502 HOH   B O   1 
HETATM 8546 O  O   . HOH   UA 8 .   ? 8.697   13.218  -17.643 1.00 42.27  0  503 HOH   B O   1 
HETATM 8547 O  O   . HOH   UA 8 .   ? 10.037  -4.775  8.770   1.00 51.64  0  504 HOH   B O   1 
HETATM 8548 O  O   . HOH   UA 8 .   ? -5.514  -0.740  5.384   1.00 52.07  0  505 HOH   B O   1 
HETATM 8549 O  O   . HOH   UA 8 .   ? 16.159  0.935   -26.210 1.00 51.33  0  506 HOH   B O   1 
HETATM 8550 O  O   . HOH   UA 8 .   ? 1.820   15.203  14.429  1.00 44.47  0  507 HOH   B O   1 
HETATM 8551 O  O   . HOH   UA 8 .   ? 7.795   -4.998  12.718  1.00 53.56  0  508 HOH   B O   1 
HETATM 8552 O  O   . HOH   UA 8 .   ? -3.137  0.908   4.936   1.00 43.63  0  509 HOH   B O   1 
HETATM 8553 O  O   . HOH   UA 8 .   ? 10.518  12.480  -20.119 1.00 44.69  0  510 HOH   B O   1 
HETATM 8554 O  O   . HOH   UA 8 .   ? 32.862  -6.271  -15.337 1.00 44.72  0  511 HOH   B O   1 
HETATM 8555 O  O   . HOH   UA 8 .   ? 28.359  8.490   -18.345 1.00 39.16  0  512 HOH   B O   1 
HETATM 8556 O  O   . HOH   UA 8 .   ? 14.430  7.440   19.486  1.00 42.26  0  513 HOH   B O   1 
HETATM 8557 O  O   . HOH   UA 8 .   ? 30.356  -6.232  -17.535 1.00 52.56  0  514 HOH   B O   1 
HETATM 8558 O  O   . HOH   UA 8 .   ? -6.801  0.458   2.560   1.00 47.32  0  515 HOH   B O   1 
HETATM 8559 O  O   . HOH   UA 8 .   ? 31.825  6.258   -16.580 1.00 43.91  0  516 HOH   B O   1 
HETATM 8560 O  O   . HOH   UA 8 .   ? 27.452  -5.274  -18.297 1.00 41.69  0  517 HOH   B O   1 
HETATM 8561 O  O   . HOH   UA 8 .   ? -2.677  -6.698  24.128  1.00 47.59  0  518 HOH   B O   1 
HETATM 8562 O  O   . HOH   UA 8 .   ? 33.534  -9.591  -15.026 1.00 61.39  0  519 HOH   B O   1 
HETATM 8563 O  O   . HOH   UA 8 .   ? 30.337  7.015   -19.004 1.00 44.94  0  520 HOH   B O   1 
HETATM 8564 O  O   . HOH   VA 8 .   ? 13.898  -41.967 23.809  1.00 40.17  0  401 HOH   C O   1 
HETATM 8565 O  O   . HOH   VA 8 .   ? 23.873  -42.362 -3.130  1.00 53.45  0  402 HOH   C O   1 
HETATM 8566 O  O   . HOH   VA 8 .   ? 13.841  -47.586 24.422  1.00 51.26  0  403 HOH   C O   1 
HETATM 8567 O  O   . HOH   VA 8 .   ? 18.143  -58.998 -11.003 1.00 34.89  0  404 HOH   C O   1 
HETATM 8568 O  O   . HOH   VA 8 .   ? 15.079  -67.649 4.099   1.00 51.19  0  405 HOH   C O   1 
HETATM 8569 O  O   . HOH   VA 8 .   ? 23.622  -48.395 18.094  1.00 29.72  0  406 HOH   C O   1 
HETATM 8570 O  O   . HOH   VA 8 .   ? 17.392  -61.332 -12.154 1.00 31.27  0  407 HOH   C O   1 
HETATM 8571 O  O   . HOH   VA 8 .   ? 4.027   -48.430 1.092   1.00 27.82  0  408 HOH   C O   1 
HETATM 8572 O  O   . HOH   VA 8 .   ? 20.827  -45.813 21.518  1.00 47.07  0  409 HOH   C O   1 
HETATM 8573 O  O   . HOH   VA 8 .   ? 9.057   -36.156 0.587   1.00 32.38  0  410 HOH   C O   1 
HETATM 8574 O  O   . HOH   VA 8 .   ? 3.755   -57.150 -4.835  1.00 43.27  0  411 HOH   C O   1 
HETATM 8575 O  O   . HOH   VA 8 .   ? 7.993   -62.695 -2.011  1.00 41.83  0  412 HOH   C O   1 
HETATM 8576 O  O   . HOH   VA 8 .   ? 10.774  -49.561 -14.026 1.00 32.22  0  413 HOH   C O   1 
HETATM 8577 O  O   . HOH   VA 8 .   ? 16.732  -36.731 10.618  1.00 32.96  0  414 HOH   C O   1 
HETATM 8578 O  O   . HOH   VA 8 .   ? 7.133   -32.467 18.279  1.00 43.92  0  415 HOH   C O   1 
HETATM 8579 O  O   . HOH   VA 8 .   ? 3.148   -53.841 -18.184 1.00 30.91  0  416 HOH   C O   1 
HETATM 8580 O  O   . HOH   VA 8 .   ? 3.040   -40.537 9.748   1.00 32.05  0  417 HOH   C O   1 
HETATM 8581 O  O   . HOH   VA 8 .   ? 11.769  -62.379 12.978  1.00 38.16  0  418 HOH   C O   1 
HETATM 8582 O  O   . HOH   VA 8 .   ? 0.630   -39.032 -11.105 1.00 45.48  0  419 HOH   C O   1 
HETATM 8583 O  O   . HOH   VA 8 .   ? 7.735   -37.186 -2.127  1.00 38.84  0  420 HOH   C O   1 
HETATM 8584 O  O   . HOH   VA 8 .   ? 31.997  -46.983 9.415   1.00 35.15  0  421 HOH   C O   1 
HETATM 8585 O  O   . HOH   VA 8 .   ? 12.085  -36.493 7.606   1.00 33.13  0  422 HOH   C O   1 
HETATM 8586 O  O   . HOH   VA 8 .   ? 33.262  -61.366 6.095   1.00 45.04  0  423 HOH   C O   1 
HETATM 8587 O  O   . HOH   VA 8 .   ? 19.534  -51.479 -11.324 1.00 28.18  0  424 HOH   C O   1 
HETATM 8588 O  O   . HOH   VA 8 .   ? 21.445  -44.014 -6.307  1.00 40.99  0  425 HOH   C O   1 
HETATM 8589 O  O   . HOH   VA 8 .   ? 27.676  -59.571 -4.991  1.00 37.76  0  426 HOH   C O   1 
HETATM 8590 O  O   . HOH   VA 8 .   ? 23.266  -68.628 -1.605  1.00 33.43  0  427 HOH   C O   1 
HETATM 8591 O  O   . HOH   VA 8 .   ? -1.036  -44.704 -3.408  1.00 30.87  0  428 HOH   C O   1 
HETATM 8592 O  O   . HOH   VA 8 .   ? 25.475  -38.802 17.066  1.00 40.17  0  429 HOH   C O   1 
HETATM 8593 O  O   . HOH   VA 8 .   ? 20.021  -30.758 9.272   1.00 43.16  0  430 HOH   C O   1 
HETATM 8594 O  O   . HOH   VA 8 .   ? 8.749   -41.605 -3.515  1.00 32.30  0  431 HOH   C O   1 
HETATM 8595 O  O   . HOH   VA 8 .   ? 32.711  -51.842 1.109   1.00 42.65  0  432 HOH   C O   1 
HETATM 8596 O  O   . HOH   VA 8 .   ? 15.663  -53.317 5.491   1.00 28.84  0  433 HOH   C O   1 
HETATM 8597 O  O   . HOH   VA 8 .   ? 3.572   -43.421 -14.023 1.00 29.30  0  434 HOH   C O   1 
HETATM 8598 O  O   . HOH   VA 8 .   ? 34.431  -58.655 4.546   1.00 43.74  0  435 HOH   C O   1 
HETATM 8599 O  O   . HOH   VA 8 .   ? 8.878   -58.607 17.698  1.00 44.55  0  436 HOH   C O   1 
HETATM 8600 O  O   . HOH   VA 8 .   ? -1.287  -35.598 -23.399 1.00 35.00  0  437 HOH   C O   1 
HETATM 8601 O  O   . HOH   VA 8 .   ? 7.718   -38.812 20.506  1.00 35.78  0  438 HOH   C O   1 
HETATM 8602 O  O   . HOH   VA 8 .   ? 30.306  -62.815 4.100   1.00 41.63  0  439 HOH   C O   1 
HETATM 8603 O  O   . HOH   VA 8 .   ? 9.833   -52.952 -18.923 1.00 41.14  0  440 HOH   C O   1 
HETATM 8604 O  O   . HOH   VA 8 .   ? 1.523   -38.609 8.007   1.00 31.35  0  441 HOH   C O   1 
HETATM 8605 O  O   . HOH   VA 8 .   ? 3.009   -42.288 -4.091  1.00 30.88  0  442 HOH   C O   1 
HETATM 8606 O  O   . HOH   VA 8 .   ? 8.532   -41.487 9.671   1.00 25.03  0  443 HOH   C O   1 
HETATM 8607 O  O   . HOH   VA 8 .   ? -0.754  -39.685 -8.824  1.00 42.97  0  444 HOH   C O   1 
HETATM 8608 O  O   . HOH   VA 8 .   ? 31.874  -55.299 -1.164  1.00 42.53  0  445 HOH   C O   1 
HETATM 8609 O  O   . HOH   VA 8 .   ? 9.704   -61.186 -0.401  1.00 29.67  0  446 HOH   C O   1 
HETATM 8610 O  O   . HOH   VA 8 .   ? 32.386  -61.037 -3.275  1.00 42.36  0  447 HOH   C O   1 
HETATM 8611 O  O   . HOH   VA 8 .   ? 4.999   -44.364 -3.106  1.00 32.43  0  448 HOH   C O   1 
HETATM 8612 O  O   . HOH   VA 8 .   ? 13.216  -35.168 9.854   1.00 34.28  0  449 HOH   C O   1 
HETATM 8613 O  O   . HOH   VA 8 .   ? 1.651   -60.360 -10.268 1.00 46.33  0  450 HOH   C O   1 
HETATM 8614 O  O   . HOH   VA 8 .   ? 6.681   -31.418 9.272   1.00 42.34  0  451 HOH   C O   1 
HETATM 8615 O  O   . HOH   VA 8 .   ? -3.304  -49.670 -16.492 1.00 43.88  0  452 HOH   C O   1 
HETATM 8616 O  O   . HOH   VA 8 .   ? 28.391  -53.526 15.765  1.00 39.55  0  453 HOH   C O   1 
HETATM 8617 O  O   . HOH   VA 8 .   ? 10.845  -64.202 -5.284  1.00 34.69  0  454 HOH   C O   1 
HETATM 8618 O  O   . HOH   VA 8 .   ? 13.024  -47.082 7.365   1.00 20.98  0  455 HOH   C O   1 
HETATM 8619 O  O   . HOH   VA 8 .   ? 0.777   -45.457 -1.613  1.00 31.58  0  456 HOH   C O   1 
HETATM 8620 O  O   . HOH   VA 8 .   ? 18.005  -52.556 15.793  1.00 30.34  0  457 HOH   C O   1 
HETATM 8621 O  O   . HOH   VA 8 .   ? 13.407  -51.446 -6.907  1.00 26.35  0  458 HOH   C O   1 
HETATM 8622 O  O   . HOH   VA 8 .   ? 14.839  -48.014 20.738  1.00 51.15  0  459 HOH   C O   1 
HETATM 8623 O  O   . HOH   VA 8 .   ? 26.363  -55.204 21.401  1.00 46.46  0  460 HOH   C O   1 
HETATM 8624 O  O   . HOH   VA 8 .   ? 25.904  -43.133 -6.044  1.00 36.47  0  461 HOH   C O   1 
HETATM 8625 O  O   . HOH   VA 8 .   ? 8.301   -47.787 -1.030  1.00 32.66  0  462 HOH   C O   1 
HETATM 8626 O  O   . HOH   VA 8 .   ? 9.320   -30.116 6.246   1.00 39.26  0  463 HOH   C O   1 
HETATM 8627 O  O   . HOH   VA 8 .   ? 6.132   -57.658 -11.863 1.00 38.71  0  464 HOH   C O   1 
HETATM 8628 O  O   . HOH   VA 8 .   ? -0.710  -46.035 -20.111 1.00 40.11  0  465 HOH   C O   1 
HETATM 8629 O  O   . HOH   VA 8 .   ? -3.533  -56.922 -5.576  1.00 44.32  0  466 HOH   C O   1 
HETATM 8630 O  O   . HOH   VA 8 .   ? -1.311  -48.327 10.637  1.00 38.21  0  467 HOH   C O   1 
HETATM 8631 O  O   . HOH   VA 8 .   ? 11.996  -53.067 20.406  1.00 38.93  0  468 HOH   C O   1 
HETATM 8632 O  O   . HOH   VA 8 .   ? 18.157  -62.086 16.990  1.00 35.82  0  469 HOH   C O   1 
HETATM 8633 O  O   . HOH   VA 8 .   ? 9.523   -53.094 10.925  1.00 27.39  0  470 HOH   C O   1 
HETATM 8634 O  O   . HOH   VA 8 .   ? 21.276  -62.262 -7.331  1.00 39.23  0  471 HOH   C O   1 
HETATM 8635 O  O   . HOH   VA 8 .   ? 18.995  -68.265 9.395   1.00 53.55  0  472 HOH   C O   1 
HETATM 8636 O  O   . HOH   VA 8 .   ? 7.920   -56.014 16.390  1.00 32.38  0  473 HOH   C O   1 
HETATM 8637 O  O   . HOH   VA 8 .   ? 14.080  -44.750 8.305   1.00 23.17  0  474 HOH   C O   1 
HETATM 8638 O  O   . HOH   VA 8 .   ? -0.018  -37.820 0.359   1.00 41.84  0  475 HOH   C O   1 
HETATM 8639 O  O   . HOH   VA 8 .   ? 26.633  -66.826 12.301  1.00 48.10  0  476 HOH   C O   1 
HETATM 8640 O  O   . HOH   VA 8 .   ? 8.316   -54.818 -20.445 1.00 34.65  0  477 HOH   C O   1 
HETATM 8641 O  O   . HOH   VA 8 .   ? 30.314  -52.294 14.418  1.00 33.72  0  478 HOH   C O   1 
HETATM 8642 O  O   . HOH   VA 8 .   ? 14.768  -53.850 -6.689  1.00 23.36  0  479 HOH   C O   1 
HETATM 8643 O  O   . HOH   VA 8 .   ? 8.062   -41.508 23.449  1.00 53.69  0  480 HOH   C O   1 
HETATM 8644 O  O   . HOH   VA 8 .   ? 6.438   -50.953 24.509  1.00 45.26  0  481 HOH   C O   1 
HETATM 8645 O  O   . HOH   VA 8 .   ? 27.906  -42.528 19.269  1.00 40.43  0  482 HOH   C O   1 
HETATM 8646 O  O   . HOH   VA 8 .   ? 7.495   -35.699 15.858  1.00 53.90  0  483 HOH   C O   1 
HETATM 8647 O  O   . HOH   VA 8 .   ? 26.025  -36.511 15.603  1.00 28.19  0  484 HOH   C O   1 
HETATM 8648 O  O   . HOH   VA 8 .   ? 23.978  -37.337 19.464  1.00 45.72  0  485 HOH   C O   1 
HETATM 8649 O  O   . HOH   VA 8 .   ? 14.135  -37.634 10.749  1.00 36.99  0  486 HOH   C O   1 
HETATM 8650 O  O   . HOH   VA 8 .   ? 17.833  -44.999 -7.946  1.00 26.03  0  487 HOH   C O   1 
HETATM 8651 O  O   . HOH   VA 8 .   ? -3.595  -47.703 -18.460 1.00 41.97  0  488 HOH   C O   1 
HETATM 8652 O  O   . HOH   VA 8 .   ? 16.821  -65.210 8.811   1.00 42.47  0  489 HOH   C O   1 
HETATM 8653 O  O   . HOH   VA 8 .   ? 9.913   -58.121 -14.624 1.00 32.85  0  490 HOH   C O   1 
HETATM 8654 O  O   . HOH   VA 8 .   ? 2.632   -60.437 -6.986  1.00 39.73  0  491 HOH   C O   1 
HETATM 8655 O  O   . HOH   VA 8 .   ? -0.842  -48.818 -24.136 1.00 50.18  0  492 HOH   C O   1 
HETATM 8656 O  O   . HOH   VA 8 .   ? 9.004   -62.865 15.300  1.00 49.69  0  493 HOH   C O   1 
HETATM 8657 O  O   . HOH   VA 8 .   ? 11.630  -31.250 11.138  1.00 46.22  0  494 HOH   C O   1 
HETATM 8658 O  O   . HOH   VA 8 .   ? 36.319  -46.885 2.174   1.00 39.45  0  495 HOH   C O   1 
HETATM 8659 O  O   . HOH   VA 8 .   ? 6.070   -47.827 24.568  1.00 57.80  0  496 HOH   C O   1 
HETATM 8660 O  O   . HOH   VA 8 .   ? -3.071  -43.838 -19.228 1.00 54.23  0  497 HOH   C O   1 
HETATM 8661 O  O   . HOH   VA 8 .   ? 19.322  -64.314 -5.446  1.00 45.15  0  498 HOH   C O   1 
HETATM 8662 O  O   . HOH   VA 8 .   ? -5.262  -43.836 -17.862 1.00 49.47  0  499 HOH   C O   1 
HETATM 8663 O  O   . HOH   VA 8 .   ? 4.968   -45.145 22.003  1.00 46.17  0  500 HOH   C O   1 
HETATM 8664 O  O   . HOH   VA 8 .   ? -5.003  -45.938 13.649  1.00 55.94  0  501 HOH   C O   1 
HETATM 8665 O  O   . HOH   VA 8 .   ? 32.651  -38.931 15.568  1.00 43.05  0  502 HOH   C O   1 
HETATM 8666 O  O   . HOH   VA 8 .   ? 13.324  -71.678 2.420   1.00 57.53  0  503 HOH   C O   1 
HETATM 8667 O  O   . HOH   VA 8 .   ? -0.263  -45.822 -23.967 1.00 43.38  0  504 HOH   C O   1 
HETATM 8668 O  O   . HOH   VA 8 .   ? 28.511  -53.858 18.419  1.00 44.57  0  505 HOH   C O   1 
HETATM 8669 O  O   . HOH   VA 8 .   ? 34.301  -38.660 8.739   1.00 54.21  0  506 HOH   C O   1 
HETATM 8670 O  O   . HOH   VA 8 .   ? 10.488  -58.022 20.187  1.00 39.13  0  507 HOH   C O   1 
HETATM 8671 O  O   . HOH   VA 8 .   ? 10.884  -56.470 -16.362 1.00 40.20  0  508 HOH   C O   1 
HETATM 8672 O  O   . HOH   VA 8 .   ? 24.850  -50.540 20.438  1.00 46.60  0  509 HOH   C O   1 
HETATM 8673 O  O   . HOH   VA 8 .   ? 32.055  -51.594 16.492  1.00 42.59  0  510 HOH   C O   1 
HETATM 8674 O  O   . HOH   VA 8 .   ? 23.234  -63.718 -7.584  1.00 49.64  0  511 HOH   C O   1 
HETATM 8675 O  O   . HOH   VA 8 .   ? 11.702  -28.593 7.104   1.00 55.12  0  512 HOH   C O   1 
HETATM 8676 O  O   . HOH   VA 8 .   ? 27.461  -40.072 18.419  1.00 42.06  0  513 HOH   C O   1 
HETATM 8677 O  O   . HOH   VA 8 .   ? -2.615  -38.656 -24.014 1.00 48.49  0  514 HOH   C O   1 
HETATM 8678 O  O   . HOH   VA 8 .   ? 30.373  -52.075 19.303  1.00 49.09  0  515 HOH   C O   1 
HETATM 8679 O  O   . HOH   WA 8 .   ? 7.635   -10.913 15.958  1.00 43.53  0  401 HOH   D O   1 
HETATM 8680 O  O   . HOH   WA 8 .   ? 15.873  -32.241 30.605  1.00 38.39  0  402 HOH   D O   1 
HETATM 8681 O  O   . HOH   WA 8 .   ? -1.098  -22.514 23.758  1.00 43.23  0  403 HOH   D O   1 
HETATM 8682 O  O   . HOH   WA 8 .   ? 6.431   -30.403 21.807  1.00 29.21  0  404 HOH   D O   1 
HETATM 8683 O  O   . HOH   WA 8 .   ? 2.371   -22.543 34.161  1.00 30.39  0  405 HOH   D O   1 
HETATM 8684 O  O   . HOH   WA 8 .   ? 23.287  -2.595  34.782  1.00 27.78  0  406 HOH   D O   1 
HETATM 8685 O  O   . HOH   WA 8 .   ? 31.691  6.729   18.125  1.00 41.10  0  407 HOH   D O   1 
HETATM 8686 O  O   . HOH   WA 8 .   ? 23.230  -10.716 15.344  1.00 32.25  0  408 HOH   D O   1 
HETATM 8687 O  O   . HOH   WA 8 .   ? 13.417  -12.748 40.084  1.00 31.56  0  409 HOH   D O   1 
HETATM 8688 O  O   . HOH   WA 8 .   ? -0.491  -19.656 25.211  1.00 27.87  0  410 HOH   D O   1 
HETATM 8689 O  O   . HOH   WA 8 .   ? 16.648  -29.786 32.206  1.00 45.62  0  411 HOH   D O   1 
HETATM 8690 O  O   . HOH   WA 8 .   ? 28.344  -2.830  28.470  1.00 28.51  0  412 HOH   D O   1 
HETATM 8691 O  O   . HOH   WA 8 .   ? 32.884  4.204   0.782   1.00 34.94  0  413 HOH   D O   1 
HETATM 8692 O  O   . HOH   WA 8 .   ? 21.154  2.271   17.930  1.00 37.42  0  414 HOH   D O   1 
HETATM 8693 O  O   . HOH   WA 8 .   ? 24.354  -14.122 11.945  1.00 37.14  0  415 HOH   D O   1 
HETATM 8694 O  O   . HOH   WA 8 .   ? 24.215  -34.472 27.642  1.00 51.97  0  416 HOH   D O   1 
HETATM 8695 O  O   . HOH   WA 8 .   ? 15.079  -25.733 17.206  1.00 43.23  0  417 HOH   D O   1 
HETATM 8696 O  O   . HOH   WA 8 .   ? 27.756  -12.101 23.584  1.00 30.04  0  418 HOH   D O   1 
HETATM 8697 O  O   . HOH   WA 8 .   ? 33.670  -9.127  32.126  1.00 41.90  0  419 HOH   D O   1 
HETATM 8698 O  O   . HOH   WA 8 .   ? 29.914  13.231  21.167  1.00 53.86  0  420 HOH   D O   1 
HETATM 8699 O  O   . HOH   WA 8 .   ? 19.792  -16.066 41.126  1.00 35.85  0  421 HOH   D O   1 
HETATM 8700 O  O   . HOH   WA 8 .   ? 2.769   -2.247  25.591  1.00 27.87  0  422 HOH   D O   1 
HETATM 8701 O  O   . HOH   WA 8 .   ? 22.804  -17.286 12.291  1.00 31.28  0  423 HOH   D O   1 
HETATM 8702 O  O   . HOH   WA 8 .   ? 35.289  4.262   16.509  1.00 33.85  0  424 HOH   D O   1 
HETATM 8703 O  O   . HOH   WA 8 .   ? 32.862  -12.701 31.807  1.00 37.65  0  425 HOH   D O   1 
HETATM 8704 O  O   . HOH   WA 8 .   ? 7.831   -26.761 30.915  1.00 27.03  0  426 HOH   D O   1 
HETATM 8705 O  O   . HOH   WA 8 .   ? 28.513  8.055   19.693  1.00 26.48  0  427 HOH   D O   1 
HETATM 8706 O  O   . HOH   WA 8 .   ? 31.442  11.326  23.379  1.00 52.16  0  428 HOH   D O   1 
HETATM 8707 O  O   . HOH   WA 8 .   ? 3.630   -1.284  30.122  1.00 35.66  0  429 HOH   D O   1 
HETATM 8708 O  O   . HOH   WA 8 .   ? 0.755   -7.871  37.232  1.00 42.54  0  430 HOH   D O   1 
HETATM 8709 O  O   . HOH   WA 8 .   ? 21.629  -4.843  34.139  1.00 23.77  0  431 HOH   D O   1 
HETATM 8710 O  O   . HOH   WA 8 .   ? 23.550  -22.762 21.184  1.00 26.48  0  432 HOH   D O   1 
HETATM 8711 O  O   . HOH   WA 8 .   ? 24.165  -33.367 23.777  1.00 37.34  0  433 HOH   D O   1 
HETATM 8712 O  O   . HOH   WA 8 .   ? 32.299  6.153   11.714  1.00 38.13  0  434 HOH   D O   1 
HETATM 8713 O  O   . HOH   WA 8 .   ? 27.347  9.415   21.781  1.00 34.05  0  435 HOH   D O   1 
HETATM 8714 O  O   . HOH   WA 8 .   ? 30.284  -22.261 18.405  1.00 36.22  0  436 HOH   D O   1 
HETATM 8715 O  O   . HOH   WA 8 .   ? 24.963  -26.789 11.853  1.00 45.86  0  437 HOH   D O   1 
HETATM 8716 O  O   . HOH   WA 8 .   ? 10.716  -27.912 45.502  1.00 46.02  0  438 HOH   D O   1 
HETATM 8717 O  O   . HOH   WA 8 .   ? 25.582  3.658   25.823  1.00 27.53  0  439 HOH   D O   1 
HETATM 8718 O  O   . HOH   WA 8 .   ? -3.958  -11.645 27.216  1.00 42.97  0  440 HOH   D O   1 
HETATM 8719 O  O   . HOH   WA 8 .   ? -5.314  -24.083 30.211  1.00 26.68  0  441 HOH   D O   1 
HETATM 8720 O  O   . HOH   WA 8 .   ? 32.714  -7.082  11.313  1.00 46.07  0  442 HOH   D O   1 
HETATM 8721 O  O   . HOH   WA 8 .   ? 10.309  -7.353  15.922  1.00 35.41  0  443 HOH   D O   1 
HETATM 8722 O  O   . HOH   WA 8 .   ? 29.132  -9.999  15.782  1.00 31.03  0  444 HOH   D O   1 
HETATM 8723 O  O   . HOH   WA 8 .   ? 22.449  -17.416 42.771  1.00 46.23  0  445 HOH   D O   1 
HETATM 8724 O  O   B HOH   WA 8 .   ? 5.339   -2.555  12.154  0.50 29.96  0  446 HOH   D O   1 
HETATM 8725 O  O   . HOH   WA 8 .   ? 18.737  -25.837 15.716  1.00 26.46  0  447 HOH   D O   1 
HETATM 8726 O  O   . HOH   WA 8 .   ? 28.090  -0.424  12.299  1.00 34.46  0  448 HOH   D O   1 
HETATM 8727 O  O   . HOH   WA 8 .   ? 12.475  0.552   20.169  1.00 22.14  0  449 HOH   D O   1 
HETATM 8728 O  O   . HOH   WA 8 .   ? 34.804  -13.106 13.335  1.00 44.58  0  450 HOH   D O   1 
HETATM 8729 O  O   . HOH   WA 8 .   ? 15.734  -13.676 29.904  1.00 24.41  0  451 HOH   D O   1 
HETATM 8730 O  O   . HOH   WA 8 .   ? 17.721  -19.900 23.350  1.00 24.40  0  452 HOH   D O   1 
HETATM 8731 O  O   . HOH   WA 8 .   ? 5.917   -8.070  15.321  1.00 32.33  0  453 HOH   D O   1 
HETATM 8732 O  O   . HOH   WA 8 .   ? 18.406  -3.519  22.463  1.00 23.62  0  454 HOH   D O   1 
HETATM 8733 O  O   . HOH   WA 8 .   ? 17.609  3.286   23.855  1.00 36.14  0  455 HOH   D O   1 
HETATM 8734 O  O   . HOH   WA 8 .   ? 20.247  0.946   34.280  1.00 44.68  0  456 HOH   D O   1 
HETATM 8735 O  O   . HOH   WA 8 .   ? 36.630  0.922   21.602  1.00 41.33  0  457 HOH   D O   1 
HETATM 8736 O  O   . HOH   WA 8 .   ? -1.542  -10.404 26.281  1.00 31.78  0  458 HOH   D O   1 
HETATM 8737 O  O   . HOH   WA 8 .   ? 26.898  -9.885  18.000  1.00 31.24  0  459 HOH   D O   1 
HETATM 8738 O  O   . HOH   WA 8 .   ? 32.851  -9.671  18.419  1.00 36.58  0  460 HOH   D O   1 
HETATM 8739 O  O   . HOH   WA 8 .   ? 12.275  -27.138 11.288  1.00 45.72  0  461 HOH   D O   1 
HETATM 8740 O  O   . HOH   WA 8 .   ? -2.133  -23.706 39.752  1.00 37.53  0  462 HOH   D O   1 
HETATM 8741 O  O   . HOH   WA 8 .   ? 12.575  -19.785 42.478  1.00 30.95  0  463 HOH   D O   1 
HETATM 8742 O  O   . HOH   WA 8 .   ? 14.008  -5.339  16.338  1.00 23.18  0  464 HOH   D O   1 
HETATM 8743 O  O   . HOH   WA 8 .   ? 18.612  -18.008 25.161  1.00 20.26  0  465 HOH   D O   1 
HETATM 8744 O  O   . HOH   WA 8 .   ? 0.573   -22.079 32.164  1.00 24.81  0  466 HOH   D O   1 
HETATM 8745 O  O   . HOH   WA 8 .   ? 24.296  -30.748 18.923  1.00 39.73  0  467 HOH   D O   1 
HETATM 8746 O  O   . HOH   WA 8 .   ? 23.468  -10.317 22.047  1.00 27.86  0  468 HOH   D O   1 
HETATM 8747 O  O   . HOH   WA 8 .   ? 30.932  -10.815 19.948  1.00 33.08  0  469 HOH   D O   1 
HETATM 8748 O  O   . HOH   WA 8 .   ? 13.342  -23.215 33.673  1.00 25.37  0  470 HOH   D O   1 
HETATM 8749 O  O   . HOH   WA 8 .   ? 11.619  0.873   34.241  1.00 32.61  0  471 HOH   D O   1 
HETATM 8750 O  O   . HOH   WA 8 .   ? 28.854  10.343  27.103  1.00 37.12  0  472 HOH   D O   1 
HETATM 8751 O  O   . HOH   WA 8 .   ? 29.201  6.282   23.468  1.00 29.68  0  473 HOH   D O   1 
HETATM 8752 O  O   . HOH   WA 8 .   ? 19.790  -23.264 16.003  1.00 37.21  0  474 HOH   D O   1 
HETATM 8753 O  O   . HOH   WA 8 .   ? 35.237  5.613   13.832  1.00 45.04  0  475 HOH   D O   1 
HETATM 8754 O  O   . HOH   WA 8 .   ? -0.678  -2.375  31.825  1.00 51.67  0  476 HOH   D O   1 
HETATM 8755 O  O   . HOH   WA 8 .   ? 21.740  -18.669 32.265  1.00 25.80  0  477 HOH   D O   1 
HETATM 8756 O  O   . HOH   WA 8 .   ? 17.698  -25.231 18.281  1.00 41.48  0  478 HOH   D O   1 
HETATM 8757 O  O   . HOH   WA 8 .   ? 35.583  -2.219  28.313  1.00 36.47  0  479 HOH   D O   1 
HETATM 8758 O  O   . HOH   WA 8 .   ? 17.653  -22.124 17.394  1.00 37.15  0  480 HOH   D O   1 
HETATM 8759 O  O   . HOH   WA 8 .   ? 5.839   -2.176  21.996  1.00 29.75  0  481 HOH   D O   1 
HETATM 8760 O  O   . HOH   WA 8 .   ? 4.120   -13.706 44.527  1.00 45.65  0  482 HOH   D O   1 
HETATM 8761 O  O   . HOH   WA 8 .   ? 5.769   -30.162 19.088  1.00 26.24  0  483 HOH   D O   1 
HETATM 8762 O  O   . HOH   WA 8 .   ? 23.369  -22.021 37.453  1.00 29.55  0  484 HOH   D O   1 
HETATM 8763 O  O   . HOH   WA 8 .   ? 10.658  1.942   31.790  1.00 29.68  0  485 HOH   D O   1 
HETATM 8764 O  O   . HOH   WA 8 .   ? 14.717  -10.846 41.878  1.00 35.16  0  486 HOH   D O   1 
HETATM 8765 O  O   . HOH   WA 8 .   ? 11.404  -4.977  15.657  1.00 32.15  0  487 HOH   D O   1 
HETATM 8766 O  O   . HOH   WA 8 .   ? 1.927   -4.846  26.453  1.00 43.81  0  488 HOH   D O   1 
HETATM 8767 O  O   . HOH   WA 8 .   ? 19.411  -8.318  43.937  1.00 43.63  0  489 HOH   D O   1 
HETATM 8768 O  O   . HOH   WA 8 .   ? 25.266  -31.341 36.398  1.00 43.62  0  490 HOH   D O   1 
HETATM 8769 O  O   . HOH   WA 8 .   ? 20.756  -20.914 41.597  1.00 48.74  0  491 HOH   D O   1 
HETATM 8770 O  O   . HOH   WA 8 .   ? 29.214  0.717   30.520  1.00 34.51  0  492 HOH   D O   1 
HETATM 8771 O  O   . HOH   WA 8 .   ? 30.606  3.616   28.952  1.00 35.52  0  493 HOH   D O   1 
HETATM 8772 O  O   . HOH   WA 8 .   ? 36.683  -6.705  18.116  1.00 52.81  0  494 HOH   D O   1 
HETATM 8773 O  O   . HOH   WA 8 .   ? 19.235  -28.396 13.335  1.00 50.60  0  495 HOH   D O   1 
HETATM 8774 O  O   . HOH   WA 8 .   ? 19.253  -26.684 36.621  1.00 43.71  0  496 HOH   D O   1 
HETATM 8775 O  O   . HOH   WA 8 .   ? 16.702  7.811   18.130  1.00 44.33  0  497 HOH   D O   1 
HETATM 8776 O  O   . HOH   WA 8 .   ? 22.662  -9.623  12.261  1.00 36.60  0  498 HOH   D O   1 
HETATM 8777 O  O   . HOH   WA 8 .   ? 3.442   -30.592 26.055  1.00 34.50  0  499 HOH   D O   1 
HETATM 8778 O  O   . HOH   WA 8 .   ? 22.492  -22.068 40.024  1.00 41.83  0  500 HOH   D O   1 
HETATM 8779 O  O   . HOH   WA 8 .   ? -1.755  -4.808  34.722  1.00 40.77  0  501 HOH   D O   1 
HETATM 8780 O  O   . HOH   WA 8 .   ? 32.231  11.164  12.359  1.00 42.76  0  502 HOH   D O   1 
HETATM 8781 O  O   . HOH   WA 8 .   ? 5.271   -26.900 37.464  1.00 41.07  0  503 HOH   D O   1 
HETATM 8782 O  O   . HOH   WA 8 .   ? 21.495  4.391   16.566  1.00 37.80  0  504 HOH   D O   1 
HETATM 8783 O  O   . HOH   WA 8 .   ? 36.533  3.257   10.219  1.00 46.00  0  505 HOH   D O   1 
HETATM 8784 O  O   . HOH   WA 8 .   ? 17.120  -2.473  24.626  1.00 25.14  0  506 HOH   D O   1 
HETATM 8785 O  O   . HOH   WA 8 .   ? 25.477  -32.744 33.676  1.00 46.11  0  507 HOH   D O   1 
HETATM 8786 O  O   . HOH   WA 8 .   ? 29.141  -2.187  40.156  1.00 49.07  0  508 HOH   D O   1 
HETATM 8787 O  O   . HOH   WA 8 .   ? 38.501  -1.665  18.089  1.00 54.20  0  509 HOH   D O   1 
HETATM 8788 O  O   . HOH   WA 8 .   ? -3.191  -27.525 14.412  1.00 56.47  0  510 HOH   D O   1 
HETATM 8789 O  O   . HOH   WA 8 .   ? 30.272  -29.691 24.997  1.00 39.00  0  511 HOH   D O   1 
HETATM 8790 O  O   . HOH   WA 8 .   ? 14.529  -29.909 44.775  1.00 46.39  0  512 HOH   D O   1 
HETATM 8791 O  O   . HOH   WA 8 .   ? 35.364  -22.222 27.131  1.00 51.64  0  513 HOH   D O   1 
HETATM 8792 O  O   . HOH   WA 8 .   ? 35.320  -15.012 28.267  1.00 50.06  0  514 HOH   D O   1 
HETATM 8793 O  O   . HOH   WA 8 .   ? 27.079  13.487  12.308  1.00 54.44  0  515 HOH   D O   1 
HETATM 8794 O  O   . HOH   WA 8 .   ? 14.874  -27.441 14.821  1.00 53.91  0  516 HOH   D O   1 
HETATM 8795 O  O   . HOH   WA 8 .   ? 17.352  -2.055  43.961  1.00 51.16  0  517 HOH   D O   1 
HETATM 8796 O  O   . HOH   WA 8 .   ? 9.150   -29.301 31.903  1.00 36.21  0  518 HOH   D O   1 
HETATM 8797 O  O   . HOH   WA 8 .   ? 11.281  -39.796 25.777  1.00 54.98  0  519 HOH   D O   1 
HETATM 8798 O  O   . HOH   WA 8 .   ? -1.379  -2.391  34.239  1.00 51.61  0  520 HOH   D O   1 
HETATM 8799 O  O   . HOH   WA 8 .   ? 3.946   -9.727  11.854  1.00 49.19  0  521 HOH   D O   1 
HETATM 8800 O  O   . HOH   WA 8 .   ? -1.129  -28.929 20.185  1.00 43.53  0  522 HOH   D O   1 
HETATM 8801 O  O   . HOH   WA 8 .   ? -4.601  -26.893 21.438  1.00 48.72  0  523 HOH   D O   1 
HETATM 8802 O  O   . HOH   WA 8 .   ? 2.256   -24.981 35.620  1.00 33.07  0  524 HOH   D O   1 
HETATM 8803 O  O   . HOH   WA 8 .   ? 28.141  4.702   25.337  1.00 36.56  0  525 HOH   D O   1 
HETATM 8804 O  O   . HOH   WA 8 .   ? 9.790   -3.394  11.901  1.00 53.68  0  526 HOH   D O   1 
HETATM 8805 O  O   . HOH   WA 8 .   ? 34.399  6.578   18.025  1.00 43.18  0  527 HOH   D O   1 
HETATM 8806 O  O   . HOH   WA 8 .   ? 15.102  -29.291 13.142  1.00 49.84  0  528 HOH   D O   1 
HETATM 8807 O  O   . HOH   WA 8 .   ? 29.789  13.526  11.025  1.00 42.99  0  529 HOH   D O   1 
HETATM 8808 O  O   . HOH   WA 8 .   ? -4.700  -9.006  29.337  1.00 55.60  0  530 HOH   D O   1 
HETATM 8809 O  O   . HOH   WA 8 .   ? 20.265  -18.545 42.335  1.00 44.84  0  531 HOH   D O   1 
HETATM 8810 O  O   . HOH   WA 8 .   ? 23.762  -33.001 37.739  1.00 50.28  0  532 HOH   D O   1 
HETATM 8811 O  O   . HOH   WA 8 .   ? 3.257   -31.087 18.427  1.00 44.43  0  533 HOH   D O   1 
HETATM 8812 O  O   . HOH   WA 8 .   ? 1.869   -31.484 21.322  1.00 54.33  0  534 HOH   D O   1 
HETATM 8813 O  O   . HOH   WA 8 .   ? 37.659  3.665   17.860  1.00 39.10  0  535 HOH   D O   1 
HETATM 8814 O  O   . HOH   WA 8 .   ? 1.951   -0.631  27.987  1.00 43.21  0  536 HOH   D O   1 
HETATM 8815 O  O   . HOH   WA 8 .   ? 18.609  9.570   22.715  1.00 25.30  0  537 HOH   D O   1 
HETATM 8816 O  O   . HOH   WA 8 .   ? -1.042  -24.397 32.636  1.00 27.72  0  538 HOH   D O   1 
HETATM 8817 O  O   . HOH   WA 8 .   ? 4.231   -31.269 23.268  1.00 36.84  0  539 HOH   D O   1 
HETATM 8818 O  O   . HOH   WA 8 .   ? 37.527  3.308   22.815  1.00 44.65  0  540 HOH   D O   1 
# 
