data_9QFV
# 
_entry.id   9QFV 
# 
_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   9QFV         pdb_00009qfv 10.2210/pdb9qfv/pdb 
WWPDB D_1292146088 ?            ?                   
# 
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.journal_volume'          
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 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                        9QFV 
_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           Y 
# 
_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'                      27491.426 4   3.4.21.59 ? ? ? 
2 non-polymer syn 'ACETATE ION'                          59.044    4   ?         ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                         62.068    13  ?         ? ? ? 
4 non-polymer syn 'SULFATE ION'                          96.063    8   ?         ? ? ? 
5 non-polymer syn GLYCEROL                               92.094    4   ?         ? ? ? 
6 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   4   ?         ? ? ? 
7 non-polymer syn 'PENTAETHYLENE GLYCOL'                 238.278   2   ?         ? ? ? 
8 water       nat water                                  18.015    554 ?         ? ? ? 
# 
_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
VPKKP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVH
PQFYTAQIGADIALLELEEPVKVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDA
KYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY
VPKKP
;
_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 'ACETATE ION'                          ACT 
3 1,2-ETHANEDIOL                         EDO 
4 'SULFATE ION'                          SO4 
5 GLYCEROL                               GOL 
6 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
7 'PENTAETHYLENE GLYCOL'                 1PE 
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 
1 244 LYS n 
1 245 PRO 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           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_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 
1PE non-polymer         . 'PENTAETHYLENE GLYCOL'                 PEG400                          'C10 H22 O6'     238.278 
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 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' ?                               'C6 H13 N O4 S'  195.237 
MET 'L-peptide linking' y METHIONINE                             ?                               'C5 H11 N O2 S'  149.211 
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 
A 1 244 LYS 244 259 259 LYS LYS A . n 
A 1 245 PRO 245 260 ?   ?   ?   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 
B 1 244 LYS 244 259 259 LYS LYS B . n 
B 1 245 PRO 245 260 ?   ?   ?   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 
C 1 244 LYS 244 259 ?   ?   ?   C . n 
C 1 245 PRO 245 260 ?   ?   ?   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 
D 1 244 LYS 244 259 259 LYS LYS D . n 
D 1 245 PRO 245 260 260 PRO PRO 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 1PE ? ? 1PE ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ACT ? ? ACT ? ? 'SUBJECT OF INVESTIGATION' ? 
3 EDO ? ? EDO ? ? 'SUBJECT OF INVESTIGATION' ? 
4 GOL ? ? GOL ? ? 'SUBJECT OF INVESTIGATION' ? 
5 MES ? ? MES ? ? '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 ACT 1   301 1   ACT ACT A . 
F  3 EDO 1   302 4   EDO EDO A . 
G  4 SO4 1   303 5   SO4 SO4 A . 
H  3 EDO 1   304 6   EDO EDO A . 
I  5 GOL 1   305 8   GOL GOL A . 
J  6 MES 1   306 9   MES MES A . 
K  3 EDO 1   307 10  EDO EDO A . 
L  3 EDO 1   308 25  EDO EDO A . 
M  3 EDO 1   309 26  EDO EDO A . 
N  4 SO4 1   310 35  SO4 SO4 A . 
O  2 ACT 1   301 11  ACT ACT B . 
P  3 EDO 1   302 15  EDO EDO B . 
Q  7 1PE 1   303 16  1PE 1PE B . 
R  4 SO4 1   304 17  SO4 SO4 B . 
S  4 SO4 1   305 18  SO4 SO4 B . 
T  3 EDO 1   306 27  EDO EDO B . 
U  6 MES 1   307 30  MES MES B . 
V  3 EDO 1   308 33  EDO EDO B . 
W  5 GOL 1   309 37  GOL GOL B . 
X  6 MES 1   301 3   MES MES C . 
Y  2 ACT 1   302 12  ACT ACT C . 
Z  4 SO4 1   303 19  SO4 SO4 C . 
AA 5 GOL 1   304 20  GOL GOL C . 
BA 3 EDO 1   305 32  EDO EDO C . 
CA 4 SO4 1   306 36  SO4 SO4 C . 
DA 3 EDO 1   307 39  EDO EDO C . 
EA 2 ACT 1   301 13  ACT ACT D . 
FA 3 EDO 1   302 21  EDO EDO D . 
GA 4 SO4 1   303 22  SO4 SO4 D . 
HA 4 SO4 1   304 23  SO4 SO4 D . 
IA 3 EDO 1   305 24  EDO EDO D . 
JA 7 1PE 1   306 28  1PE 1PE D . 
KA 6 MES 1   307 31  MES MES D . 
LA 3 EDO 1   308 34  EDO EDO D . 
MA 5 GOL 1   309 38  GOL GOL D . 
NA 8 HOH 1   401 348 HOH HOH A . 
NA 8 HOH 2   402 336 HOH HOH A . 
NA 8 HOH 3   403 588 HOH HOH A . 
NA 8 HOH 4   404 104 HOH HOH A . 
NA 8 HOH 5   405 320 HOH HOH A . 
NA 8 HOH 6   406 361 HOH HOH A . 
NA 8 HOH 7   407 362 HOH HOH A . 
NA 8 HOH 8   408 135 HOH HOH A . 
NA 8 HOH 9   409 210 HOH HOH A . 
NA 8 HOH 10  410 298 HOH HOH A . 
NA 8 HOH 11  411 252 HOH HOH A . 
NA 8 HOH 12  412 102 HOH HOH A . 
NA 8 HOH 13  413 192 HOH HOH A . 
NA 8 HOH 14  414 133 HOH HOH A . 
NA 8 HOH 15  415 24  HOH HOH A . 
NA 8 HOH 16  416 181 HOH HOH A . 
NA 8 HOH 17  417 317 HOH HOH A . 
NA 8 HOH 18  418 355 HOH HOH A . 
NA 8 HOH 19  419 303 HOH HOH A . 
NA 8 HOH 20  420 305 HOH HOH A . 
NA 8 HOH 21  421 585 HOH HOH A . 
NA 8 HOH 22  422 337 HOH HOH A . 
NA 8 HOH 23  423 365 HOH HOH A . 
NA 8 HOH 24  424 186 HOH HOH A . 
NA 8 HOH 25  425 373 HOH HOH A . 
NA 8 HOH 26  426 308 HOH HOH A . 
NA 8 HOH 27  427 548 HOH HOH A . 
NA 8 HOH 28  428 363 HOH HOH A . 
NA 8 HOH 29  429 58  HOH HOH A . 
NA 8 HOH 30  430 220 HOH HOH A . 
NA 8 HOH 31  431 137 HOH HOH A . 
NA 8 HOH 32  432 250 HOH HOH A . 
NA 8 HOH 33  433 311 HOH HOH A . 
NA 8 HOH 34  434 549 HOH HOH A . 
NA 8 HOH 35  435 286 HOH HOH A . 
NA 8 HOH 36  436 55  HOH HOH A . 
NA 8 HOH 37  437 230 HOH HOH A . 
NA 8 HOH 38  438 263 HOH HOH A . 
NA 8 HOH 39  439 283 HOH HOH A . 
NA 8 HOH 40  440 96  HOH HOH A . 
NA 8 HOH 41  441 367 HOH HOH A . 
NA 8 HOH 42  442 290 HOH HOH A . 
NA 8 HOH 43  443 64  HOH HOH A . 
NA 8 HOH 44  444 356 HOH HOH A . 
NA 8 HOH 45  445 281 HOH HOH A . 
NA 8 HOH 46  446 282 HOH HOH A . 
NA 8 HOH 47  447 589 HOH HOH A . 
NA 8 HOH 48  448 255 HOH HOH A . 
NA 8 HOH 49  449 385 HOH HOH A . 
NA 8 HOH 50  450 322 HOH HOH A . 
NA 8 HOH 51  451 193 HOH HOH A . 
NA 8 HOH 52  452 312 HOH HOH A . 
NA 8 HOH 53  453 124 HOH HOH A . 
NA 8 HOH 54  454 351 HOH HOH A . 
NA 8 HOH 55  455 316 HOH HOH A . 
NA 8 HOH 56  456 99  HOH HOH A . 
NA 8 HOH 57  457 163 HOH HOH A . 
NA 8 HOH 58  458 323 HOH HOH A . 
NA 8 HOH 59  459 334 HOH HOH A . 
NA 8 HOH 60  460 297 HOH HOH A . 
NA 8 HOH 61  461 380 HOH HOH A . 
NA 8 HOH 62  462 347 HOH HOH A . 
NA 8 HOH 63  463 79  HOH HOH A . 
NA 8 HOH 64  464 204 HOH HOH A . 
NA 8 HOH 65  465 338 HOH HOH A . 
NA 8 HOH 66  466 141 HOH HOH A . 
NA 8 HOH 67  467 235 HOH HOH A . 
NA 8 HOH 68  468 293 HOH HOH A . 
NA 8 HOH 69  469 319 HOH HOH A . 
NA 8 HOH 70  470 205 HOH HOH A . 
NA 8 HOH 71  471 296 HOH HOH A . 
NA 8 HOH 72  472 67  HOH HOH A . 
NA 8 HOH 73  473 552 HOH HOH A . 
NA 8 HOH 74  474 335 HOH HOH A . 
NA 8 HOH 75  475 54  HOH HOH A . 
NA 8 HOH 76  476 383 HOH HOH A . 
NA 8 HOH 77  477 118 HOH HOH A . 
NA 8 HOH 78  478 307 HOH HOH A . 
NA 8 HOH 79  479 16  HOH HOH A . 
NA 8 HOH 80  480 326 HOH HOH A . 
NA 8 HOH 81  481 201 HOH HOH A . 
NA 8 HOH 82  482 51  HOH HOH A . 
NA 8 HOH 83  483 310 HOH HOH A . 
NA 8 HOH 84  484 366 HOH HOH A . 
NA 8 HOH 85  485 15  HOH HOH A . 
NA 8 HOH 86  486 309 HOH HOH A . 
NA 8 HOH 87  487 331 HOH HOH A . 
NA 8 HOH 88  488 379 HOH HOH A . 
NA 8 HOH 89  489 47  HOH HOH A . 
NA 8 HOH 90  490 349 HOH HOH A . 
NA 8 HOH 91  491 313 HOH HOH A . 
NA 8 HOH 92  492 285 HOH HOH A . 
NA 8 HOH 93  493 244 HOH HOH A . 
NA 8 HOH 94  494 234 HOH HOH A . 
NA 8 HOH 95  495 295 HOH HOH A . 
NA 8 HOH 96  496 254 HOH HOH A . 
NA 8 HOH 97  497 354 HOH HOH A . 
NA 8 HOH 98  498 82  HOH HOH A . 
NA 8 HOH 99  499 386 HOH HOH A . 
NA 8 HOH 100 500 358 HOH HOH A . 
NA 8 HOH 101 501 144 HOH HOH A . 
NA 8 HOH 102 502 360 HOH HOH A . 
NA 8 HOH 103 503 191 HOH HOH A . 
NA 8 HOH 104 504 23  HOH HOH A . 
NA 8 HOH 105 505 575 HOH HOH A . 
NA 8 HOH 106 506 372 HOH HOH A . 
NA 8 HOH 107 507 413 HOH HOH A . 
NA 8 HOH 108 508 330 HOH HOH A . 
NA 8 HOH 109 509 156 HOH HOH A . 
NA 8 HOH 110 510 357 HOH HOH A . 
NA 8 HOH 111 511 287 HOH HOH A . 
NA 8 HOH 112 512 161 HOH HOH A . 
NA 8 HOH 113 513 207 HOH HOH A . 
NA 8 HOH 114 514 182 HOH HOH A . 
NA 8 HOH 115 515 35  HOH HOH A . 
NA 8 HOH 116 516 152 HOH HOH A . 
NA 8 HOH 117 517 371 HOH HOH A . 
NA 8 HOH 118 518 188 HOH HOH A . 
NA 8 HOH 119 519 288 HOH HOH A . 
NA 8 HOH 120 520 32  HOH HOH A . 
NA 8 HOH 121 521 273 HOH HOH A . 
NA 8 HOH 122 522 364 HOH HOH A . 
NA 8 HOH 123 523 81  HOH HOH A . 
NA 8 HOH 124 524 107 HOH HOH A . 
NA 8 HOH 125 525 381 HOH HOH A . 
NA 8 HOH 126 526 318 HOH HOH A . 
NA 8 HOH 127 527 324 HOH HOH A . 
NA 8 HOH 128 528 352 HOH HOH A . 
NA 8 HOH 129 529 300 HOH HOH A . 
NA 8 HOH 130 530 327 HOH HOH A . 
NA 8 HOH 131 531 350 HOH HOH A . 
NA 8 HOH 132 532 377 HOH HOH A . 
NA 8 HOH 133 533 302 HOH HOH A . 
NA 8 HOH 134 534 368 HOH HOH A . 
NA 8 HOH 135 535 314 HOH HOH A . 
NA 8 HOH 136 536 617 HOH HOH A . 
NA 8 HOH 137 537 306 HOH HOH A . 
NA 8 HOH 138 538 590 HOH HOH A . 
NA 8 HOH 139 539 550 HOH HOH A . 
NA 8 HOH 140 540 292 HOH HOH A . 
NA 8 HOH 141 541 19  HOH HOH A . 
NA 8 HOH 142 542 574 HOH HOH A . 
NA 8 HOH 143 543 535 HOH HOH A . 
NA 8 HOH 144 544 586 HOH HOH A . 
NA 8 HOH 145 545 301 HOH HOH A . 
NA 8 HOH 146 546 619 HOH HOH A . 
NA 8 HOH 147 547 587 HOH HOH A . 
OA 8 HOH 1   401 472 HOH HOH B . 
OA 8 HOH 2   402 434 HOH HOH B . 
OA 8 HOH 3   403 395 HOH HOH B . 
OA 8 HOH 4   404 466 HOH HOH B . 
OA 8 HOH 5   405 206 HOH HOH B . 
OA 8 HOH 6   406 474 HOH HOH B . 
OA 8 HOH 7   407 369 HOH HOH B . 
OA 8 HOH 8   408 592 HOH HOH B . 
OA 8 HOH 9   409 456 HOH HOH B . 
OA 8 HOH 10  410 409 HOH HOH B . 
OA 8 HOH 11  411 38  HOH HOH B . 
OA 8 HOH 12  412 256 HOH HOH B . 
OA 8 HOH 13  413 577 HOH HOH B . 
OA 8 HOH 14  414 224 HOH HOH B . 
OA 8 HOH 15  415 112 HOH HOH B . 
OA 8 HOH 16  416 86  HOH HOH B . 
OA 8 HOH 17  417 169 HOH HOH B . 
OA 8 HOH 18  418 473 HOH HOH B . 
OA 8 HOH 19  419 471 HOH HOH B . 
OA 8 HOH 20  420 173 HOH HOH B . 
OA 8 HOH 21  421 159 HOH HOH B . 
OA 8 HOH 22  422 71  HOH HOH B . 
OA 8 HOH 23  423 146 HOH HOH B . 
OA 8 HOH 24  424 554 HOH HOH B . 
OA 8 HOH 25  425 44  HOH HOH B . 
OA 8 HOH 26  426 557 HOH HOH B . 
OA 8 HOH 27  427 179 HOH HOH B . 
OA 8 HOH 28  428 149 HOH HOH B . 
OA 8 HOH 29  429 439 HOH HOH B . 
OA 8 HOH 30  430 405 HOH HOH B . 
OA 8 HOH 31  431 45  HOH HOH B . 
OA 8 HOH 32  432 95  HOH HOH B . 
OA 8 HOH 33  433 74  HOH HOH B . 
OA 8 HOH 34  434 167 HOH HOH B . 
OA 8 HOH 35  435 202 HOH HOH B . 
OA 8 HOH 36  436 211 HOH HOH B . 
OA 8 HOH 37  437 128 HOH HOH B . 
OA 8 HOH 38  438 229 HOH HOH B . 
OA 8 HOH 39  439 174 HOH HOH B . 
OA 8 HOH 40  440 122 HOH HOH B . 
OA 8 HOH 41  441 18  HOH HOH B . 
OA 8 HOH 42  442 25  HOH HOH B . 
OA 8 HOH 43  443 597 HOH HOH B . 
OA 8 HOH 44  444 85  HOH HOH B . 
OA 8 HOH 45  445 28  HOH HOH B . 
OA 8 HOH 46  446 462 HOH HOH B . 
OA 8 HOH 47  447 440 HOH HOH B . 
OA 8 HOH 48  448 457 HOH HOH B . 
OA 8 HOH 49  449 451 HOH HOH B . 
OA 8 HOH 50  450 198 HOH HOH B . 
OA 8 HOH 51  451 41  HOH HOH B . 
OA 8 HOH 52  452 469 HOH HOH B . 
OA 8 HOH 53  453 136 HOH HOH B . 
OA 8 HOH 54  454 291 HOH HOH B . 
OA 8 HOH 55  455 408 HOH HOH B . 
OA 8 HOH 56  456 467 HOH HOH B . 
OA 8 HOH 57  457 458 HOH HOH B . 
OA 8 HOH 58  458 200 HOH HOH B . 
OA 8 HOH 59  459 407 HOH HOH B . 
OA 8 HOH 60  460 233 HOH HOH B . 
OA 8 HOH 61  461 251 HOH HOH B . 
OA 8 HOH 62  462 176 HOH HOH B . 
OA 8 HOH 63  463 31  HOH HOH B . 
OA 8 HOH 64  464 241 HOH HOH B . 
OA 8 HOH 65  465 162 HOH HOH B . 
OA 8 HOH 66  466 420 HOH HOH B . 
OA 8 HOH 67  467 247 HOH HOH B . 
OA 8 HOH 68  468 42  HOH HOH B . 
OA 8 HOH 69  469 68  HOH HOH B . 
OA 8 HOH 70  470 442 HOH HOH B . 
OA 8 HOH 71  471 168 HOH HOH B . 
OA 8 HOH 72  472 555 HOH HOH B . 
OA 8 HOH 73  473 547 HOH HOH B . 
OA 8 HOH 74  474 228 HOH HOH B . 
OA 8 HOH 75  475 449 HOH HOH B . 
OA 8 HOH 76  476 103 HOH HOH B . 
OA 8 HOH 77  477 121 HOH HOH B . 
OA 8 HOH 78  478 417 HOH HOH B . 
OA 8 HOH 79  479 69  HOH HOH B . 
OA 8 HOH 80  480 134 HOH HOH B . 
OA 8 HOH 81  481 593 HOH HOH B . 
OA 8 HOH 82  482 435 HOH HOH B . 
OA 8 HOH 83  483 151 HOH HOH B . 
OA 8 HOH 84  484 6   HOH HOH B . 
OA 8 HOH 85  485 274 HOH HOH B . 
OA 8 HOH 86  486 160 HOH HOH B . 
OA 8 HOH 87  487 470 HOH HOH B . 
OA 8 HOH 88  488 106 HOH HOH B . 
OA 8 HOH 89  489 468 HOH HOH B . 
OA 8 HOH 90  490 199 HOH HOH B . 
OA 8 HOH 91  491 257 HOH HOH B . 
OA 8 HOH 92  492 424 HOH HOH B . 
OA 8 HOH 93  493 410 HOH HOH B . 
OA 8 HOH 94  494 73  HOH HOH B . 
OA 8 HOH 95  495 422 HOH HOH B . 
OA 8 HOH 96  496 601 HOH HOH B . 
OA 8 HOH 97  497 183 HOH HOH B . 
OA 8 HOH 98  498 600 HOH HOH B . 
OA 8 HOH 99  499 108 HOH HOH B . 
OA 8 HOH 100 500 276 HOH HOH B . 
OA 8 HOH 101 501 427 HOH HOH B . 
OA 8 HOH 102 502 245 HOH HOH B . 
OA 8 HOH 103 503 433 HOH HOH B . 
OA 8 HOH 104 504 227 HOH HOH B . 
OA 8 HOH 105 505 460 HOH HOH B . 
OA 8 HOH 106 506 65  HOH HOH B . 
OA 8 HOH 107 507 437 HOH HOH B . 
OA 8 HOH 108 508 425 HOH HOH B . 
OA 8 HOH 109 509 203 HOH HOH B . 
OA 8 HOH 110 510 423 HOH HOH B . 
OA 8 HOH 111 511 110 HOH HOH B . 
OA 8 HOH 112 512 446 HOH HOH B . 
OA 8 HOH 113 513 542 HOH HOH B . 
OA 8 HOH 114 514 461 HOH HOH B . 
OA 8 HOH 115 515 139 HOH HOH B . 
OA 8 HOH 116 516 465 HOH HOH B . 
OA 8 HOH 117 517 447 HOH HOH B . 
OA 8 HOH 118 518 450 HOH HOH B . 
OA 8 HOH 119 519 426 HOH HOH B . 
OA 8 HOH 120 520 453 HOH HOH B . 
OA 8 HOH 121 521 246 HOH HOH B . 
OA 8 HOH 122 522 599 HOH HOH B . 
OA 8 HOH 123 523 332 HOH HOH B . 
OA 8 HOH 124 524 596 HOH HOH B . 
OA 8 HOH 125 525 271 HOH HOH B . 
OA 8 HOH 126 526 594 HOH HOH B . 
OA 8 HOH 127 527 443 HOH HOH B . 
OA 8 HOH 128 528 455 HOH HOH B . 
OA 8 HOH 129 529 444 HOH HOH B . 
OA 8 HOH 130 530 517 HOH HOH B . 
OA 8 HOH 131 531 595 HOH HOH B . 
OA 8 HOH 132 532 279 HOH HOH B . 
OA 8 HOH 133 533 120 HOH HOH B . 
OA 8 HOH 134 534 278 HOH HOH B . 
OA 8 HOH 135 535 448 HOH HOH B . 
PA 8 HOH 1   401 495 HOH HOH C . 
PA 8 HOH 2   402 503 HOH HOH C . 
PA 8 HOH 3   403 344 HOH HOH C . 
PA 8 HOH 4   404 518 HOH HOH C . 
PA 8 HOH 5   405 463 HOH HOH C . 
PA 8 HOH 6   406 476 HOH HOH C . 
PA 8 HOH 7   407 88  HOH HOH C . 
PA 8 HOH 8   408 505 HOH HOH C . 
PA 8 HOH 9   409 502 HOH HOH C . 
PA 8 HOH 10  410 506 HOH HOH C . 
PA 8 HOH 11  411 490 HOH HOH C . 
PA 8 HOH 12  412 155 HOH HOH C . 
PA 8 HOH 13  413 49  HOH HOH C . 
PA 8 HOH 14  414 602 HOH HOH C . 
PA 8 HOH 15  415 166 HOH HOH C . 
PA 8 HOH 16  416 382 HOH HOH C . 
PA 8 HOH 17  417 138 HOH HOH C . 
PA 8 HOH 18  418 484 HOH HOH C . 
PA 8 HOH 19  419 43  HOH HOH C . 
PA 8 HOH 20  420 17  HOH HOH C . 
PA 8 HOH 21  421 63  HOH HOH C . 
PA 8 HOH 22  422 345 HOH HOH C . 
PA 8 HOH 23  423 406 HOH HOH C . 
PA 8 HOH 24  424 501 HOH HOH C . 
PA 8 HOH 25  425 57  HOH HOH C . 
PA 8 HOH 26  426 114 HOH HOH C . 
PA 8 HOH 27  427 418 HOH HOH C . 
PA 8 HOH 28  428 339 HOH HOH C . 
PA 8 HOH 29  429 61  HOH HOH C . 
PA 8 HOH 30  430 346 HOH HOH C . 
PA 8 HOH 31  431 491 HOH HOH C . 
PA 8 HOH 32  432 261 HOH HOH C . 
PA 8 HOH 33  433 565 HOH HOH C . 
PA 8 HOH 34  434 416 HOH HOH C . 
PA 8 HOH 35  435 70  HOH HOH C . 
PA 8 HOH 36  436 113 HOH HOH C . 
PA 8 HOH 37  437 507 HOH HOH C . 
PA 8 HOH 38  438 145 HOH HOH C . 
PA 8 HOH 39  439 83  HOH HOH C . 
PA 8 HOH 40  440 111 HOH HOH C . 
PA 8 HOH 41  441 46  HOH HOH C . 
PA 8 HOH 42  442 53  HOH HOH C . 
PA 8 HOH 43  443 165 HOH HOH C . 
PA 8 HOH 44  444 500 HOH HOH C . 
PA 8 HOH 45  445 48  HOH HOH C . 
PA 8 HOH 46  446 239 HOH HOH C . 
PA 8 HOH 47  447 130 HOH HOH C . 
PA 8 HOH 48  448 341 HOH HOH C . 
PA 8 HOH 49  449 66  HOH HOH C . 
PA 8 HOH 50  450 232 HOH HOH C . 
PA 8 HOH 51  451 240 HOH HOH C . 
PA 8 HOH 52  452 221 HOH HOH C . 
PA 8 HOH 53  453 153 HOH HOH C . 
PA 8 HOH 54  454 563 HOH HOH C . 
PA 8 HOH 55  455 479 HOH HOH C . 
PA 8 HOH 56  456 243 HOH HOH C . 
PA 8 HOH 57  457 493 HOH HOH C . 
PA 8 HOH 58  458 117 HOH HOH C . 
PA 8 HOH 59  459 268 HOH HOH C . 
PA 8 HOH 60  460 90  HOH HOH C . 
PA 8 HOH 61  461 481 HOH HOH C . 
PA 8 HOH 62  462 397 HOH HOH C . 
PA 8 HOH 63  463 212 HOH HOH C . 
PA 8 HOH 64  464 511 HOH HOH C . 
PA 8 HOH 65  465 342 HOH HOH C . 
PA 8 HOH 66  466 214 HOH HOH C . 
PA 8 HOH 67  467 87  HOH HOH C . 
PA 8 HOH 68  468 180 HOH HOH C . 
PA 8 HOH 69  469 438 HOH HOH C . 
PA 8 HOH 70  470 578 HOH HOH C . 
PA 8 HOH 71  471 37  HOH HOH C . 
PA 8 HOH 72  472 514 HOH HOH C . 
PA 8 HOH 73  473 219 HOH HOH C . 
PA 8 HOH 74  474 325 HOH HOH C . 
PA 8 HOH 75  475 39  HOH HOH C . 
PA 8 HOH 76  476 12  HOH HOH C . 
PA 8 HOH 77  477 370 HOH HOH C . 
PA 8 HOH 78  478 22  HOH HOH C . 
PA 8 HOH 79  479 412 HOH HOH C . 
PA 8 HOH 80  480 431 HOH HOH C . 
PA 8 HOH 81  481 478 HOH HOH C . 
PA 8 HOH 82  482 197 HOH HOH C . 
PA 8 HOH 83  483 404 HOH HOH C . 
PA 8 HOH 84  484 508 HOH HOH C . 
PA 8 HOH 85  485 59  HOH HOH C . 
PA 8 HOH 86  486 494 HOH HOH C . 
PA 8 HOH 87  487 399 HOH HOH C . 
PA 8 HOH 88  488 504 HOH HOH C . 
PA 8 HOH 89  489 513 HOH HOH C . 
PA 8 HOH 90  490 237 HOH HOH C . 
PA 8 HOH 91  491 604 HOH HOH C . 
PA 8 HOH 92  492 499 HOH HOH C . 
PA 8 HOH 93  493 56  HOH HOH C . 
PA 8 HOH 94  494 569 HOH HOH C . 
PA 8 HOH 95  495 606 HOH HOH C . 
PA 8 HOH 96  496 14  HOH HOH C . 
PA 8 HOH 97  497 401 HOH HOH C . 
PA 8 HOH 98  498 258 HOH HOH C . 
PA 8 HOH 99  499 567 HOH HOH C . 
PA 8 HOH 100 500 515 HOH HOH C . 
PA 8 HOH 101 501 485 HOH HOH C . 
PA 8 HOH 102 502 275 HOH HOH C . 
PA 8 HOH 103 503 343 HOH HOH C . 
PA 8 HOH 104 504 394 HOH HOH C . 
PA 8 HOH 105 505 396 HOH HOH C . 
PA 8 HOH 106 506 143 HOH HOH C . 
PA 8 HOH 107 507 226 HOH HOH C . 
PA 8 HOH 108 508 610 HOH HOH C . 
PA 8 HOH 109 509 265 HOH HOH C . 
PA 8 HOH 110 510 187 HOH HOH C . 
PA 8 HOH 111 511 510 HOH HOH C . 
PA 8 HOH 112 512 272 HOH HOH C . 
PA 8 HOH 113 513 483 HOH HOH C . 
PA 8 HOH 114 514 512 HOH HOH C . 
PA 8 HOH 115 515 225 HOH HOH C . 
PA 8 HOH 116 516 477 HOH HOH C . 
PA 8 HOH 117 517 218 HOH HOH C . 
PA 8 HOH 118 518 27  HOH HOH C . 
PA 8 HOH 119 519 486 HOH HOH C . 
PA 8 HOH 120 520 562 HOH HOH C . 
PA 8 HOH 121 521 487 HOH HOH C . 
PA 8 HOH 122 522 609 HOH HOH C . 
PA 8 HOH 123 523 432 HOH HOH C . 
PA 8 HOH 124 524 568 HOH HOH C . 
PA 8 HOH 125 525 519 HOH HOH C . 
PA 8 HOH 126 526 492 HOH HOH C . 
PA 8 HOH 127 527 480 HOH HOH C . 
PA 8 HOH 128 528 566 HOH HOH C . 
PA 8 HOH 129 529 496 HOH HOH C . 
PA 8 HOH 130 530 260 HOH HOH C . 
PA 8 HOH 131 531 608 HOH HOH C . 
PA 8 HOH 132 532 419 HOH HOH C . 
PA 8 HOH 133 533 488 HOH HOH C . 
PA 8 HOH 134 534 498 HOH HOH C . 
PA 8 HOH 135 535 497 HOH HOH C . 
PA 8 HOH 136 536 509 HOH HOH C . 
PA 8 HOH 137 537 603 HOH HOH C . 
PA 8 HOH 138 538 441 HOH HOH C . 
PA 8 HOH 139 539 489 HOH HOH C . 
PA 8 HOH 140 540 607 HOH HOH C . 
PA 8 HOH 141 541 475 HOH HOH C . 
QA 8 HOH 1   401 129 HOH HOH D . 
QA 8 HOH 2   402 584 HOH HOH D . 
QA 8 HOH 3   403 415 HOH HOH D . 
QA 8 HOH 4   404 77  HOH HOH D . 
QA 8 HOH 5   405 521 HOH HOH D . 
QA 8 HOH 6   406 389 HOH HOH D . 
QA 8 HOH 7   407 613 HOH HOH D . 
QA 8 HOH 8   408 482 HOH HOH D . 
QA 8 HOH 9   409 249 HOH HOH D . 
QA 8 HOH 10  410 618 HOH HOH D . 
QA 8 HOH 11  411 40  HOH HOH D . 
QA 8 HOH 12  412 78  HOH HOH D . 
QA 8 HOH 13  413 36  HOH HOH D . 
QA 8 HOH 14  414 556 HOH HOH D . 
QA 8 HOH 15  415 222 HOH HOH D . 
QA 8 HOH 16  416 127 HOH HOH D . 
QA 8 HOH 17  417 170 HOH HOH D . 
QA 8 HOH 18  418 148 HOH HOH D . 
QA 8 HOH 19  419 402 HOH HOH D . 
QA 8 HOH 20  420 62  HOH HOH D . 
QA 8 HOH 21  421 93  HOH HOH D . 
QA 8 HOH 22  422 154 HOH HOH D . 
QA 8 HOH 23  423 116 HOH HOH D . 
QA 8 HOH 24  424 582 HOH HOH D . 
QA 8 HOH 25  425 190 HOH HOH D . 
QA 8 HOH 26  426 140 HOH HOH D . 
QA 8 HOH 27  427 581 HOH HOH D . 
QA 8 HOH 28  428 20  HOH HOH D . 
QA 8 HOH 29  429 259 HOH HOH D . 
QA 8 HOH 30  430 132 HOH HOH D . 
QA 8 HOH 31  431 264 HOH HOH D . 
QA 8 HOH 32  432 213 HOH HOH D . 
QA 8 HOH 33  433 178 HOH HOH D . 
QA 8 HOH 34  434 531 HOH HOH D . 
QA 8 HOH 35  435 76  HOH HOH D . 
QA 8 HOH 36  436 100 HOH HOH D . 
QA 8 HOH 37  437 236 HOH HOH D . 
QA 8 HOH 38  438 147 HOH HOH D . 
QA 8 HOH 39  439 157 HOH HOH D . 
QA 8 HOH 40  440 208 HOH HOH D . 
QA 8 HOH 41  441 123 HOH HOH D . 
QA 8 HOH 42  442 50  HOH HOH D . 
QA 8 HOH 43  443 561 HOH HOH D . 
QA 8 HOH 44  444 172 HOH HOH D . 
QA 8 HOH 45  445 534 HOH HOH D . 
QA 8 HOH 46  446 215 HOH HOH D . 
QA 8 HOH 47  447 177 HOH HOH D . 
QA 8 HOH 48  448 105 HOH HOH D . 
QA 8 HOH 49  449 520 HOH HOH D . 
QA 8 HOH 50  450 131 HOH HOH D . 
QA 8 HOH 51  451 411 HOH HOH D . 
QA 8 HOH 52  452 209 HOH HOH D . 
QA 8 HOH 53  453 101 HOH HOH D . 
QA 8 HOH 54  454 223 HOH HOH D . 
QA 8 HOH 55  455 611 HOH HOH D . 
QA 8 HOH 56  456 560 HOH HOH D . 
QA 8 HOH 57  457 189 HOH HOH D . 
QA 8 HOH 58  458 158 HOH HOH D . 
QA 8 HOH 59  459 536 HOH HOH D . 
QA 8 HOH 60  460 29  HOH HOH D . 
QA 8 HOH 61  461 89  HOH HOH D . 
QA 8 HOH 62  462 253 HOH HOH D . 
QA 8 HOH 63  463 194 HOH HOH D . 
QA 8 HOH 64  464 98  HOH HOH D . 
QA 8 HOH 65  465 528 HOH HOH D . 
QA 8 HOH 66  466 576 HOH HOH D . 
QA 8 HOH 67  467 262 HOH HOH D . 
QA 8 HOH 68  468 544 HOH HOH D . 
QA 8 HOH 69  469 119 HOH HOH D . 
QA 8 HOH 70  470 329 HOH HOH D . 
QA 8 HOH 71  471 142 HOH HOH D . 
QA 8 HOH 72  472 579 HOH HOH D . 
QA 8 HOH 73  473 52  HOH HOH D . 
QA 8 HOH 74  474 242 HOH HOH D . 
QA 8 HOH 75  475 238 HOH HOH D . 
QA 8 HOH 76  476 216 HOH HOH D . 
QA 8 HOH 77  477 195 HOH HOH D . 
QA 8 HOH 78  478 570 HOH HOH D . 
QA 8 HOH 79  479 84  HOH HOH D . 
QA 8 HOH 80  480 94  HOH HOH D . 
QA 8 HOH 81  481 125 HOH HOH D . 
QA 8 HOH 82  482 175 HOH HOH D . 
QA 8 HOH 83  483 109 HOH HOH D . 
QA 8 HOH 84  484 558 HOH HOH D . 
QA 8 HOH 85  485 398 HOH HOH D . 
QA 8 HOH 86  486 34  HOH HOH D . 
QA 8 HOH 87  487 80  HOH HOH D . 
QA 8 HOH 88  488 72  HOH HOH D . 
QA 8 HOH 89  489 171 HOH HOH D . 
QA 8 HOH 90  490 30  HOH HOH D . 
QA 8 HOH 91  491 583 HOH HOH D . 
QA 8 HOH 92  492 533 HOH HOH D . 
QA 8 HOH 93  493 248 HOH HOH D . 
QA 8 HOH 94  494 217 HOH HOH D . 
QA 8 HOH 95  495 184 HOH HOH D . 
QA 8 HOH 96  496 388 HOH HOH D . 
QA 8 HOH 97  497 92  HOH HOH D . 
QA 8 HOH 98  498 33  HOH HOH D . 
QA 8 HOH 99  499 414 HOH HOH D . 
QA 8 HOH 100 500 328 HOH HOH D . 
QA 8 HOH 101 501 572 HOH HOH D . 
QA 8 HOH 102 502 8   HOH HOH D . 
QA 8 HOH 103 503 598 HOH HOH D . 
QA 8 HOH 104 504 387 HOH HOH D . 
QA 8 HOH 105 505 390 HOH HOH D . 
QA 8 HOH 106 506 196 HOH HOH D . 
QA 8 HOH 107 507 164 HOH HOH D . 
QA 8 HOH 108 508 530 HOH HOH D . 
QA 8 HOH 109 509 546 HOH HOH D . 
QA 8 HOH 110 510 400 HOH HOH D . 
QA 8 HOH 111 511 580 HOH HOH D . 
QA 8 HOH 112 512 537 HOH HOH D . 
QA 8 HOH 113 513 538 HOH HOH D . 
QA 8 HOH 114 514 540 HOH HOH D . 
QA 8 HOH 115 515 376 HOH HOH D . 
QA 8 HOH 116 516 591 HOH HOH D . 
QA 8 HOH 117 517 527 HOH HOH D . 
QA 8 HOH 118 518 545 HOH HOH D . 
QA 8 HOH 119 519 543 HOH HOH D . 
QA 8 HOH 120 520 616 HOH HOH D . 
QA 8 HOH 121 521 270 HOH HOH D . 
QA 8 HOH 122 522 529 HOH HOH D . 
QA 8 HOH 123 523 526 HOH HOH D . 
QA 8 HOH 124 524 612 HOH HOH D . 
QA 8 HOH 125 525 553 HOH HOH D . 
QA 8 HOH 126 526 280 HOH HOH D . 
QA 8 HOH 127 527 277 HOH HOH D . 
QA 8 HOH 128 528 75  HOH HOH D . 
QA 8 HOH 129 529 615 HOH HOH D . 
QA 8 HOH 130 530 571 HOH HOH D . 
QA 8 HOH 131 531 620 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 117 ? CG  ? A LYS 102 CG  
2  1 Y 0 A LYS 117 ? CD  ? A LYS 102 CD  
3  1 Y 0 A LYS 117 ? CE  ? A LYS 102 CE  
4  1 Y 0 A LYS 117 ? NZ  ? A LYS 102 NZ  
5  1 Y 0 A SER 120 ? OG  ? A SER 105 OG  
6  1 Y 0 A THR 133 ? OG1 ? A THR 118 OG1 
7  1 Y 0 A THR 133 ? CG2 ? A THR 118 CG2 
8  1 Y 0 A ASP 151 ? CG  ? A ASP 136 CG  
9  1 Y 0 A ASP 151 ? OD1 ? A ASP 136 OD1 
10 1 Y 0 A ASP 151 ? OD2 ? A ASP 136 OD2 
11 1 Y 0 A LYS 164 ? NZ  ? A LYS 149 NZ  
12 1 Y 0 A GLN 206 ? CD  ? A GLN 191 CD  
13 1 Y 0 A GLN 206 ? OE1 ? A GLN 191 OE1 
14 1 Y 0 A GLN 206 ? NE2 ? A GLN 191 NE2 
15 1 Y 0 A LYS 258 ? CD  ? A LYS 243 CD  
16 1 Y 0 A LYS 258 ? CE  ? A LYS 243 CE  
17 1 Y 0 A LYS 258 ? NZ  ? A LYS 243 NZ  
18 1 Y 0 A LYS 259 ? CG  ? A LYS 244 CG  
19 1 Y 0 A LYS 259 ? CD  ? A LYS 244 CD  
20 1 Y 0 A LYS 259 ? CE  ? A LYS 244 CE  
21 1 Y 0 A LYS 259 ? NZ  ? A LYS 244 NZ  
22 1 Y 0 B HIS 121 ? CG  ? B HIS 106 CG  
23 1 Y 0 B HIS 121 ? ND1 ? B HIS 106 ND1 
24 1 Y 0 B HIS 121 ? CD2 ? B HIS 106 CD2 
25 1 Y 0 B HIS 121 ? CE1 ? B HIS 106 CE1 
26 1 Y 0 B HIS 121 ? NE2 ? B HIS 106 NE2 
27 1 Y 0 B ARG 153 ? NE  ? B ARG 138 NE  
28 1 Y 0 B ARG 153 ? CZ  ? B ARG 138 CZ  
29 1 Y 0 B ARG 153 ? NH1 ? B ARG 138 NH1 
30 1 Y 0 B ARG 153 ? NH2 ? B ARG 138 NH2 
31 1 Y 0 B ILE 167 ? CD1 ? B ILE 152 CD1 
32 1 Y 0 B LYS 176 ? NZ  ? B LYS 161 NZ  
33 1 Y 0 B LYS 258 ? CG  ? B LYS 243 CG  
34 1 Y 0 B LYS 258 ? CD  ? B LYS 243 CD  
35 1 Y 0 B LYS 258 ? CE  ? B LYS 243 CE  
36 1 Y 0 B LYS 258 ? NZ  ? B LYS 243 NZ  
37 1 Y 0 B LYS 259 ? CG  ? B LYS 244 CG  
38 1 Y 0 B LYS 259 ? CD  ? B LYS 244 CD  
39 1 Y 0 B LYS 259 ? CE  ? B LYS 244 CE  
40 1 Y 0 B LYS 259 ? NZ  ? B LYS 244 NZ  
41 1 Y 0 C LYS 117 ? CG  ? C LYS 102 CG  
42 1 Y 0 C LYS 117 ? CD  ? C LYS 102 CD  
43 1 Y 0 C LYS 117 ? CE  ? C LYS 102 CE  
44 1 Y 0 C LYS 117 ? NZ  ? C LYS 102 NZ  
45 1 Y 0 C HIS 121 ? CG  ? C HIS 106 CG  
46 1 Y 0 C HIS 121 ? ND1 ? C HIS 106 ND1 
47 1 Y 0 C HIS 121 ? CD2 ? C HIS 106 CD2 
48 1 Y 0 C HIS 121 ? CE1 ? C HIS 106 CE1 
49 1 Y 0 C HIS 121 ? NE2 ? C HIS 106 NE2 
50 1 Y 0 C ARG 153 ? NE  ? C ARG 138 NE  
51 1 Y 0 C ARG 153 ? CZ  ? C ARG 138 CZ  
52 1 Y 0 C ARG 153 ? NH1 ? C ARG 138 NH1 
53 1 Y 0 C ARG 153 ? NH2 ? C ARG 138 NH2 
54 1 Y 0 C LYS 164 ? NZ  ? C LYS 149 NZ  
55 1 Y 0 C ARG 188 ? CZ  ? C ARG 173 CZ  
56 1 Y 0 C ARG 188 ? NH1 ? C ARG 173 NH1 
57 1 Y 0 C ARG 188 ? NH2 ? C ARG 173 NH2 
58 1 Y 0 C ARG 201 ? NE  ? C ARG 186 NE  
59 1 Y 0 C ARG 201 ? CZ  ? C ARG 186 CZ  
60 1 Y 0 C ARG 201 ? NH1 ? C ARG 186 NH1 
61 1 Y 0 C ARG 201 ? NH2 ? C ARG 186 NH2 
62 1 Y 0 C GLN 206 ? CD  B C GLN 191 CD  
63 1 Y 0 C GLN 206 ? OE1 B C GLN 191 OE1 
64 1 Y 0 C GLN 206 ? NE2 B C GLN 191 NE2 
65 1 Y 0 C LYS 258 ? CG  ? C LYS 243 CG  
66 1 Y 0 C LYS 258 ? CD  ? C LYS 243 CD  
67 1 Y 0 C LYS 258 ? CE  ? C LYS 243 CE  
68 1 Y 0 C LYS 258 ? NZ  ? C LYS 243 NZ  
69 1 Y 0 D GLN 20  ? CD  ? D GLN 5   CD  
70 1 Y 0 D GLN 20  ? OE1 ? D GLN 5   OE1 
71 1 Y 0 D GLN 20  ? NE2 ? D GLN 5   NE2 
72 1 Y 0 D LYS 26  ? CE  ? D LYS 11  CE  
73 1 Y 0 D LYS 26  ? NZ  ? D LYS 11  NZ  
74 1 Y 0 D GLN 85  ? CD  ? D GLN 70  CD  
75 1 Y 0 D GLN 85  ? OE1 ? D GLN 70  OE1 
76 1 Y 0 D GLN 85  ? NE2 ? D GLN 70  NE2 
77 1 Y 0 D HIS 121 ? CG  ? D HIS 106 CG  
78 1 Y 0 D HIS 121 ? ND1 ? D HIS 106 ND1 
79 1 Y 0 D HIS 121 ? CD2 ? D HIS 106 CD2 
80 1 Y 0 D HIS 121 ? CE1 ? D HIS 106 CE1 
81 1 Y 0 D HIS 121 ? NE2 ? D HIS 106 NE2 
82 1 Y 0 D ASP 151 ? CG  ? D ASP 136 CG  
83 1 Y 0 D ASP 151 ? OD1 ? D ASP 136 OD1 
84 1 Y 0 D ASP 151 ? OD2 ? D ASP 136 OD2 
85 1 Y 0 D ARG 153 ? NE  ? D ARG 138 NE  
86 1 Y 0 D ARG 153 ? CZ  ? D ARG 138 CZ  
87 1 Y 0 D ARG 153 ? NH1 ? D ARG 138 NH1 
88 1 Y 0 D ARG 153 ? NH2 ? D ARG 138 NH2 
89 1 Y 0 D LYS 258 ? CE  ? D LYS 243 CE  
90 1 Y 0 D LYS 258 ? NZ  ? D LYS 243 NZ  
91 1 Y 0 D LYS 259 ? CD  ? D LYS 244 CD  
92 1 Y 0 D LYS 259 ? CE  ? D LYS 244 CE  
93 1 Y 0 D LYS 259 ? NZ  ? D LYS 244 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 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .   2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .   3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? .   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                     9QFV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     78.634 
_cell.length_a_esd                 ? 
_cell.length_b                     78.634 
_cell.length_b_esd                 ? 
_cell.length_c                     165.051 
_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                         9QFV 
_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                   9QFV 
_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             2.68 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          54.09 
_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              4.6 
_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         2023-06-30 
_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                                       9QFV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.06 
_reflns.d_resolution_low                               68.10 
_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                                     70311 
_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                           99.95 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.2 
_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                                   0.997 
_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                                    2.06 
_reflns_shell.d_res_low                                     2.094 
_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                             70696 
_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                                  0.997 
_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]                            1.20 
_refine.aniso_B[1][2]                            0.60 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            1.20 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -3.89 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               37.788 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9QFV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.06 
_refine.ls_d_res_low                             68.10 
_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                     70311 
_refine.ls_number_reflns_R_free                  365 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 21.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18842 
_refine.ls_R_factor_R_free                       0.21921 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18825 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.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       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.187 
_refine.pdbx_overall_ESU_R_Free                  0.157 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.890 
_refine.overall_SU_ML                            0.129 
_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.details                          ? 
_refine_hist.d_res_high                       2.06 
_refine_hist.d_res_low                        68.10 
_refine_hist.number_atoms_solvent             554 
_refine_hist.number_atoms_total               8481 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7715 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         212 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  0.013  8179  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.017  7462  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.359  1.643  11208 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.139  1.571  17204 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.895  5.000  1002  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 27.000 21.974 390   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.487 15.000 1148  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.063 15.000 43    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.061  0.200  994   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  10744 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  1814  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.743  3.853  3937  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.733  3.851  3932  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.595  5.779  4918  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.595  5.780  4919  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.177  4.190  4242  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.176  4.190  4243  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.359  6.161  6277  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.722  44.997 8676  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.692  44.827 8617  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.03 ? 0.05 1  'interatomic distance' ? A 2751 ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.03 ? 0.05 2  'interatomic distance' ? B 2751 ? ? 1 
'X-RAY DIFFRACTION' 1 ? ? 0.01 ? 0.05 3  'interatomic distance' ? A 2788 ? ? 2 
'X-RAY DIFFRACTION' 2 ? ? 0.01 ? 0.05 4  'interatomic distance' ? C 2788 ? ? 2 
'X-RAY DIFFRACTION' 1 ? ? 0.03 ? 0.05 5  'interatomic distance' ? A 2732 ? ? 3 
'X-RAY DIFFRACTION' 2 ? ? 0.03 ? 0.05 6  'interatomic distance' ? D 2732 ? ? 3 
'X-RAY DIFFRACTION' 1 ? ? 0.03 ? 0.05 7  'interatomic distance' ? B 2738 ? ? 4 
'X-RAY DIFFRACTION' 2 ? ? 0.03 ? 0.05 8  'interatomic distance' ? C 2738 ? ? 4 
'X-RAY DIFFRACTION' 1 ? ? 0.02 ? 0.05 9  'interatomic distance' ? B 2798 ? ? 5 
'X-RAY DIFFRACTION' 2 ? ? 0.02 ? 0.05 10 'interatomic distance' ? D 2798 ? ? 5 
'X-RAY DIFFRACTION' 1 ? ? 0.03 ? 0.05 11 'interatomic distance' ? C 2710 ? ? 6 
'X-RAY DIFFRACTION' 2 ? ? 0.03 ? 0.05 12 'interatomic distance' ? D 2710 ? ? 6 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          2.06 
_refine_ls_shell.d_res_low                           2.112 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                27 
_refine_ls_shell.number_reflns_R_work                5184 
_refine_ls_shell.percent_reflns_obs                  99.75 
_refine_ls_shell.percent_reflns_R_free               ? 
_refine_ls_shell.R_factor_all                        ? 
_refine_ls_shell.R_factor_obs                        ? 
_refine_ls_shell.R_factor_R_free_error               ? 
_refine_ls_shell.R_factor_R_work                     0.295 
_refine_ls_shell.redundancy_reflns_all               ? 
_refine_ls_shell.redundancy_reflns_obs               ? 
_refine_ls_shell.wR_factor_all                       ? 
_refine_ls_shell.wR_factor_obs                       ? 
_refine_ls_shell.wR_factor_R_free                    ? 
_refine_ls_shell.wR_factor_R_work                    ? 
_refine_ls_shell.pdbx_R_complete                     ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      ? 
_refine_ls_shell.pdbx_phase_error                    ? 
_refine_ls_shell.pdbx_fsc_work                       ? 
_refine_ls_shell.pdbx_fsc_free                       ? 
_refine_ls_shell.R_factor_R_free                     0.293 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 ? 1 
2 ? 2 
3 ? 3 
4 ? 4 
5 ? 5 
6 ? 6 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
3 ? 
4 ? 
5 ? 
6 ? 
# 
_struct.entry_id                     9QFV 
_struct.title                        'Human Tryptase beta-2 (hTPSB2)' 
_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        9QFV 
_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 4 ? 
H  N N 3 ? 
I  N N 5 ? 
J  N N 6 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 4 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 7 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 3 ? 
U  N N 6 ? 
V  N N 3 ? 
W  N N 5 ? 
X  N N 6 ? 
Y  N N 2 ? 
Z  N N 4 ? 
AA N N 5 ? 
BA N N 3 ? 
CA N N 4 ? 
DA N N 3 ? 
EA N N 2 ? 
FA N N 3 ? 
GA N N 4 ? 
HA N N 4 ? 
IA N N 3 ? 
JA N N 7 ? 
KA N N 6 ? 
LA N N 3 ? 
MA N N 5 ? 
NA N N 8 ? 
OA N N 8 ? 
PA N N 8 ? 
QA 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   
;IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQLREQHLYYQDQLLPVSRIIVH
PQFYTAQIGADIALLELEEPVNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDA
KYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY
VPKKP
;
_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 9QFV A 1 ? 245 ? P20231 31 ? 275 ? 16 260 
2 1 9QFV B 1 ? 245 ? P20231 31 ? 275 ? 16 260 
3 1 9QFV C 1 ? 245 ? P20231 31 ? 275 ? 16 260 
4 1 9QFV D 1 ? 245 ? P20231 31 ? 275 ? 16 260 
# 
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 9QFV LYS A 102 ? UNP P20231 ASN 132 conflict 117 1 
2 9QFV LYS B 102 ? UNP P20231 ASN 132 conflict 117 2 
3 9QFV LYS C 102 ? UNP P20231 ASN 132 conflict 117 3 
4 9QFV LYS D 102 ? UNP P20231 ASN 132 conflict 117 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   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 
# 
_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]         1.0 
_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 ? HIS A 239 ? TYR A 248 HIS A 254 1 ? 7  
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 ? VAL B 241 ? TYR B 248 VAL B 256 1 ? 9  
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 ? ? ? ? ? ? ? 2.085 ? ? 
disulf2  disulf ? ? A CYS 125 SG ? ? ? 1_555 A CYS 200 SG ? ? A CYS 140 A CYS 215 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
disulf3  disulf ? ? A CYS 158 SG A ? ? 1_555 A CYS 181 SG A ? A CYS 173 A CYS 196 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf4  disulf ? ? A CYS 158 SG B ? ? 1_555 A CYS 181 SG B ? A CYS 173 A CYS 196 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
disulf5  disulf ? ? A CYS 190 SG ? ? ? 1_555 A CYS 218 SG ? ? A CYS 205 A CYS 233 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf6  disulf ? ? B CYS 29  SG ? ? ? 1_555 B CYS 45  SG ? ? B CYS 44  B CYS 60  1_555 ? ? ? ? ? ? ? 2.075 ? ? 
disulf7  disulf ? ? B CYS 125 SG ? ? ? 1_555 B CYS 200 SG ? ? B CYS 140 B CYS 215 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf8  disulf ? ? B CYS 158 SG A ? ? 1_555 B CYS 181 SG A ? B CYS 173 B CYS 196 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
disulf9  disulf ? ? B CYS 158 SG B ? ? 1_555 B CYS 181 SG B ? B CYS 173 B CYS 196 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
disulf10 disulf ? ? B CYS 190 SG ? ? ? 1_555 B CYS 218 SG ? ? B CYS 205 B CYS 233 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
disulf11 disulf ? ? C CYS 29  SG ? ? ? 1_555 C CYS 45  SG ? ? C CYS 44  C CYS 60  1_555 ? ? ? ? ? ? ? 2.085 ? ? 
disulf12 disulf ? ? C CYS 125 SG ? ? ? 1_555 C CYS 200 SG ? ? C CYS 140 C CYS 215 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf13 disulf ? ? C CYS 158 SG A ? ? 1_555 C CYS 181 SG A ? C CYS 173 C CYS 196 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf14 disulf ? ? C CYS 158 SG B ? ? 1_555 C CYS 181 SG B ? C CYS 173 C CYS 196 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
disulf15 disulf ? ? C CYS 190 SG ? ? ? 1_555 C CYS 218 SG ? ? C CYS 205 C CYS 233 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf16 disulf ? ? D CYS 29  SG ? ? ? 1_555 D CYS 45  SG ? ? D CYS 44  D CYS 60  1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf17 disulf ? ? D CYS 125 SG ? ? ? 1_555 D CYS 200 SG ? ? D CYS 140 D CYS 215 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
disulf18 disulf ? ? D CYS 158 SG A ? ? 1_555 D CYS 181 SG A ? D CYS 173 D CYS 196 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
disulf19 disulf ? ? D CYS 158 SG B ? ? 1_555 D CYS 181 SG B ? D CYS 173 D CYS 196 1_555 ? ? ? ? ? ? ? 2.016 ? ? 
disulf20 disulf ? ? D CYS 190 SG ? ? ? 1_555 D CYS 218 SG ? ? D CYS 205 D CYS 233 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  CYS A 29  ? CYS A 45  ? CYS A 44  ? 1_555 CYS A 60  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 125 ? CYS A 200 ? CYS A 140 ? 1_555 CYS A 215 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 158 A CYS A 181 A CYS A 173 ? 1_555 CYS A 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 158 B CYS A 181 B CYS A 173 ? 1_555 CYS A 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS A 190 ? CYS A 218 ? CYS A 205 ? 1_555 CYS A 233 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS B 29  ? CYS B 45  ? CYS B 44  ? 1_555 CYS B 60  ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS B 125 ? CYS B 200 ? CYS B 140 ? 1_555 CYS B 215 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS B 158 A CYS B 181 A CYS B 173 ? 1_555 CYS B 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS B 158 B CYS B 181 B CYS B 173 ? 1_555 CYS B 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS B 190 ? CYS B 218 ? CYS B 205 ? 1_555 CYS B 233 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS C 29  ? CYS C 45  ? CYS C 44  ? 1_555 CYS C 60  ? 1_555 SG SG . . . None 'Disulfide bridge' 
12 CYS C 125 ? CYS C 200 ? CYS C 140 ? 1_555 CYS C 215 ? 1_555 SG SG . . . None 'Disulfide bridge' 
13 CYS C 158 A CYS C 181 A CYS C 173 ? 1_555 CYS C 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
14 CYS C 158 B CYS C 181 B CYS C 173 ? 1_555 CYS C 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
15 CYS C 190 ? CYS C 218 ? CYS C 205 ? 1_555 CYS C 233 ? 1_555 SG SG . . . None 'Disulfide bridge' 
16 CYS D 29  ? CYS D 45  ? CYS D 44  ? 1_555 CYS D 60  ? 1_555 SG SG . . . None 'Disulfide bridge' 
17 CYS D 125 ? CYS D 200 ? CYS D 140 ? 1_555 CYS D 215 ? 1_555 SG SG . . . None 'Disulfide bridge' 
18 CYS D 158 A CYS D 181 A CYS D 173 ? 1_555 CYS D 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
19 CYS D 158 B CYS D 181 B CYS D 173 ? 1_555 CYS D 196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
20 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 6.34 
2 PRO 141 A . ? PRO 156 A PRO 142 A ? PRO 157 A 1 5.58 
3 GLY 47  B . ? GLY 62  B PRO 48  B ? PRO 63  B 1 7.73 
4 PRO 141 B . ? PRO 156 B PRO 142 B ? PRO 157 B 1 5.82 
5 GLY 47  C . ? GLY 62  C PRO 48  C ? PRO 63  C 1 6.92 
6 PRO 141 C . ? PRO 156 C PRO 142 C ? PRO 157 C 1 6.40 
7 GLY 47  D . ? GLY 62  D PRO 48  D ? PRO 63  D 1 8.28 
8 PRO 141 D . ? PRO 156 D PRO 142 D ? PRO 157 D 1 4.57 
# 
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 ? MET A 153 ? LYS A 161 MET A 168 
AA1 3 MET A 179 ? ALA A 182 ? MET A 194 ALA A 197 
AA1 4 GLY A 225 ? ARG A 229 ? GLY A 240 ARG A 244 
AA1 5 THR A 205 ? TRP A 214 ? THR A 220 TRP A 229 
AA1 6 PRO A 197 ? VAL A 202 ? PRO A 212 VAL A 217 
AA1 7 PRO A 124 ? GLY A 129 ? PRO A 139 GLY A 144 
AA1 8 LYS A 146 ? MET A 153 ? LYS A 161 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 N MET A 153 ? N MET A 168 O CYS A 181 ? O CYS A 196 
AA1 3 4 N LEU A 180 ? N LEU A 195 O TYR A 227 ? O TYR A 242 
AA1 4 5 O ILE A 226 ? O ILE A 241 N TRP A 214 ? N TRP A 229 
AA1 5 6 O THR A 205 ? O THR A 220 N VAL A 202 ? N VAL A 217 
AA1 6 7 O VAL A 199 ? O VAL A 214 N TRP A 126 ? N TRP A 141 
AA1 7 8 N CYS A 125 ? N CYS A 140 O VAL A 150 ? O VAL A 165 
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 LEU D 94  ? O LEU D 109 N ILE D 78  ? N ILE D 93  
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                   9QFV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   C 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    457 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   C 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    477 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             0.90 
# 
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  ? ? 86.83   -18.01 
2  1 PHE A 158 ? ? 63.73   61.16  
3  1 SER A 228 ? ? -117.59 -70.53 
4  1 TYR B 81  ? ? 87.02   -17.34 
5  1 TYR B 99  ? ? -130.60 -47.21 
6  1 PHE B 134 ? ? 57.50   73.23  
7  1 PHE B 158 ? ? 63.94   60.58  
8  1 SER B 228 ? ? -118.78 -70.47 
9  1 TYR C 81  ? ? 86.93   -17.38 
10 1 TYR C 99  ? ? -131.10 -48.53 
11 1 PHE C 158 ? ? 64.27   60.85  
12 1 SER C 228 ? ? -118.79 -70.53 
13 1 TYR D 81  ? ? 85.48   -15.73 
14 1 TYR D 99  ? ? -130.27 -47.90 
15 1 PHE D 134 ? ? 56.50   71.34  
16 1 PHE D 158 ? ? 63.55   61.07  
17 1 SER D 228 ? ? -117.80 -70.55 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A PRO 260 ? A PRO 245 
2 1 Y 1 B PRO 260 ? B PRO 245 
3 1 Y 1 C LYS 259 ? C LYS 244 
4 1 Y 1 C PRO 260 ? C PRO 245 
# 
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 
1PE OH2  O N N 1   
1PE C12  C N N 2   
1PE C22  C N N 3   
1PE OH3  O N N 4   
1PE C13  C N N 5   
1PE C23  C N N 6   
1PE OH4  O N N 7   
1PE C14  C N N 8   
1PE C24  C N N 9   
1PE OH5  O N N 10  
1PE C15  C N N 11  
1PE C25  C N N 12  
1PE OH6  O N N 13  
1PE C16  C N N 14  
1PE C26  C N N 15  
1PE OH7  O N N 16  
1PE HO2  H N N 17  
1PE H121 H N N 18  
1PE H122 H N N 19  
1PE H221 H N N 20  
1PE H222 H N N 21  
1PE H131 H N N 22  
1PE H132 H N N 23  
1PE H231 H N N 24  
1PE H232 H N N 25  
1PE H141 H N N 26  
1PE H142 H N N 27  
1PE H241 H N N 28  
1PE H242 H N N 29  
1PE H151 H N N 30  
1PE H152 H N N 31  
1PE H251 H N N 32  
1PE H252 H N N 33  
1PE H161 H N N 34  
1PE H162 H N N 35  
1PE H261 H N N 36  
1PE H262 H N N 37  
1PE HO7  H N N 38  
ACT C    C N N 39  
ACT O    O N N 40  
ACT OXT  O N N 41  
ACT CH3  C N N 42  
ACT H1   H N N 43  
ACT H2   H N N 44  
ACT H3   H N N 45  
ALA N    N N N 46  
ALA CA   C N S 47  
ALA C    C N N 48  
ALA O    O N N 49  
ALA CB   C N N 50  
ALA OXT  O N N 51  
ALA H    H N N 52  
ALA H2   H N N 53  
ALA HA   H N N 54  
ALA HB1  H N N 55  
ALA HB2  H N N 56  
ALA HB3  H N N 57  
ALA HXT  H N N 58  
ARG N    N N N 59  
ARG CA   C N S 60  
ARG C    C N N 61  
ARG O    O N N 62  
ARG CB   C N N 63  
ARG CG   C N N 64  
ARG CD   C N N 65  
ARG NE   N N N 66  
ARG CZ   C N N 67  
ARG NH1  N N N 68  
ARG NH2  N N N 69  
ARG OXT  O N N 70  
ARG H    H N N 71  
ARG H2   H N N 72  
ARG HA   H N N 73  
ARG HB2  H N N 74  
ARG HB3  H N N 75  
ARG HG2  H N N 76  
ARG HG3  H N N 77  
ARG HD2  H N N 78  
ARG HD3  H N N 79  
ARG HE   H N N 80  
ARG HH11 H N N 81  
ARG HH12 H N N 82  
ARG HH21 H N N 83  
ARG HH22 H N N 84  
ARG HXT  H N N 85  
ASN N    N N N 86  
ASN CA   C N S 87  
ASN C    C N N 88  
ASN O    O N N 89  
ASN CB   C N N 90  
ASN CG   C N N 91  
ASN OD1  O N N 92  
ASN ND2  N N N 93  
ASN OXT  O N N 94  
ASN H    H N N 95  
ASN H2   H N N 96  
ASN HA   H N N 97  
ASN HB2  H N N 98  
ASN HB3  H N N 99  
ASN HD21 H N N 100 
ASN HD22 H N N 101 
ASN HXT  H N N 102 
ASP N    N N N 103 
ASP CA   C N S 104 
ASP C    C N N 105 
ASP O    O N N 106 
ASP CB   C N N 107 
ASP CG   C N N 108 
ASP OD1  O N N 109 
ASP OD2  O N N 110 
ASP OXT  O N N 111 
ASP H    H N N 112 
ASP H2   H N N 113 
ASP HA   H N N 114 
ASP HB2  H N N 115 
ASP HB3  H N N 116 
ASP HD2  H N N 117 
ASP HXT  H N N 118 
CYS N    N N N 119 
CYS CA   C N R 120 
CYS C    C N N 121 
CYS O    O N N 122 
CYS CB   C N N 123 
CYS SG   S N N 124 
CYS OXT  O N N 125 
CYS H    H N N 126 
CYS H2   H N N 127 
CYS HA   H N N 128 
CYS HB2  H N N 129 
CYS HB3  H N N 130 
CYS HG   H N N 131 
CYS HXT  H N N 132 
EDO C1   C N N 133 
EDO O1   O N N 134 
EDO C2   C N N 135 
EDO O2   O N N 136 
EDO H11  H N N 137 
EDO H12  H N N 138 
EDO HO1  H N N 139 
EDO H21  H N N 140 
EDO H22  H N N 141 
EDO HO2  H N N 142 
GLN N    N N N 143 
GLN CA   C N S 144 
GLN C    C N N 145 
GLN O    O N N 146 
GLN CB   C N N 147 
GLN CG   C N N 148 
GLN CD   C N N 149 
GLN OE1  O N N 150 
GLN NE2  N N N 151 
GLN OXT  O N N 152 
GLN H    H N N 153 
GLN H2   H N N 154 
GLN HA   H N N 155 
GLN HB2  H N N 156 
GLN HB3  H N N 157 
GLN HG2  H N N 158 
GLN HG3  H N N 159 
GLN HE21 H N N 160 
GLN HE22 H N N 161 
GLN HXT  H N N 162 
GLU N    N N N 163 
GLU CA   C N S 164 
GLU C    C N N 165 
GLU O    O N N 166 
GLU CB   C N N 167 
GLU CG   C N N 168 
GLU CD   C N N 169 
GLU OE1  O N N 170 
GLU OE2  O N N 171 
GLU OXT  O N N 172 
GLU H    H N N 173 
GLU H2   H N N 174 
GLU HA   H N N 175 
GLU HB2  H N N 176 
GLU HB3  H N N 177 
GLU HG2  H N N 178 
GLU HG3  H N N 179 
GLU HE2  H N N 180 
GLU HXT  H N N 181 
GLY N    N N N 182 
GLY CA   C N N 183 
GLY C    C N N 184 
GLY O    O N N 185 
GLY OXT  O N N 186 
GLY H    H N N 187 
GLY H2   H N N 188 
GLY HA2  H N N 189 
GLY HA3  H N N 190 
GLY HXT  H N N 191 
GOL C1   C N N 192 
GOL O1   O N N 193 
GOL C2   C N N 194 
GOL O2   O N N 195 
GOL C3   C N N 196 
GOL O3   O N N 197 
GOL H11  H N N 198 
GOL H12  H N N 199 
GOL HO1  H N N 200 
GOL H2   H N N 201 
GOL HO2  H N N 202 
GOL H31  H N N 203 
GOL H32  H N N 204 
GOL HO3  H N N 205 
HIS N    N N N 206 
HIS CA   C N S 207 
HIS C    C N N 208 
HIS O    O N N 209 
HIS CB   C N N 210 
HIS CG   C Y N 211 
HIS ND1  N Y N 212 
HIS CD2  C Y N 213 
HIS CE1  C Y N 214 
HIS NE2  N Y N 215 
HIS OXT  O N N 216 
HIS H    H N N 217 
HIS H2   H N N 218 
HIS HA   H N N 219 
HIS HB2  H N N 220 
HIS HB3  H N N 221 
HIS HD1  H N N 222 
HIS HD2  H N N 223 
HIS HE1  H N N 224 
HIS HE2  H N N 225 
HIS HXT  H N N 226 
HOH O    O N N 227 
HOH H1   H N N 228 
HOH H2   H N N 229 
ILE N    N N N 230 
ILE CA   C N S 231 
ILE C    C N N 232 
ILE O    O N N 233 
ILE CB   C N S 234 
ILE CG1  C N N 235 
ILE CG2  C N N 236 
ILE CD1  C N N 237 
ILE OXT  O N N 238 
ILE H    H N N 239 
ILE H2   H N N 240 
ILE HA   H N N 241 
ILE HB   H N N 242 
ILE HG12 H N N 243 
ILE HG13 H N N 244 
ILE HG21 H N N 245 
ILE HG22 H N N 246 
ILE HG23 H N N 247 
ILE HD11 H N N 248 
ILE HD12 H N N 249 
ILE HD13 H N N 250 
ILE HXT  H N N 251 
LEU N    N N N 252 
LEU CA   C N S 253 
LEU C    C N N 254 
LEU O    O N N 255 
LEU CB   C N N 256 
LEU CG   C N N 257 
LEU CD1  C N N 258 
LEU CD2  C N N 259 
LEU OXT  O N N 260 
LEU H    H N N 261 
LEU H2   H N N 262 
LEU HA   H N N 263 
LEU HB2  H N N 264 
LEU HB3  H N N 265 
LEU HG   H N N 266 
LEU HD11 H N N 267 
LEU HD12 H N N 268 
LEU HD13 H N N 269 
LEU HD21 H N N 270 
LEU HD22 H N N 271 
LEU HD23 H N N 272 
LEU HXT  H N N 273 
LYS N    N N N 274 
LYS CA   C N S 275 
LYS C    C N N 276 
LYS O    O N N 277 
LYS CB   C N N 278 
LYS CG   C N N 279 
LYS CD   C N N 280 
LYS CE   C N N 281 
LYS NZ   N N N 282 
LYS OXT  O N N 283 
LYS H    H N N 284 
LYS H2   H N N 285 
LYS HA   H N N 286 
LYS HB2  H N N 287 
LYS HB3  H N N 288 
LYS HG2  H N N 289 
LYS HG3  H N N 290 
LYS HD2  H N N 291 
LYS HD3  H N N 292 
LYS HE2  H N N 293 
LYS HE3  H N N 294 
LYS HZ1  H N N 295 
LYS HZ2  H N N 296 
LYS HZ3  H N N 297 
LYS HXT  H N N 298 
MES O1   O N N 299 
MES C2   C N N 300 
MES C3   C N N 301 
MES N4   N N N 302 
MES C5   C N N 303 
MES C6   C N N 304 
MES C7   C N N 305 
MES C8   C N N 306 
MES S    S N N 307 
MES O1S  O N N 308 
MES O2S  O N N 309 
MES O3S  O N N 310 
MES H21  H N N 311 
MES H22  H N N 312 
MES H31  H N N 313 
MES H32  H N N 314 
MES HN4  H N N 315 
MES H51  H N N 316 
MES H52  H N N 317 
MES H61  H N N 318 
MES H62  H N N 319 
MES H71  H N N 320 
MES H72  H N N 321 
MES H81  H N N 322 
MES H82  H N N 323 
MET N    N N N 324 
MET CA   C N S 325 
MET C    C N N 326 
MET O    O N N 327 
MET CB   C N N 328 
MET CG   C N N 329 
MET SD   S N N 330 
MET CE   C N N 331 
MET OXT  O N N 332 
MET H    H N N 333 
MET H2   H N N 334 
MET HA   H N N 335 
MET HB2  H N N 336 
MET HB3  H N N 337 
MET HG2  H N N 338 
MET HG3  H N N 339 
MET HE1  H N N 340 
MET HE2  H N N 341 
MET HE3  H N N 342 
MET HXT  H N N 343 
PHE N    N N N 344 
PHE CA   C N S 345 
PHE C    C N N 346 
PHE O    O N N 347 
PHE CB   C N N 348 
PHE CG   C Y N 349 
PHE CD1  C Y N 350 
PHE CD2  C Y N 351 
PHE CE1  C Y N 352 
PHE CE2  C Y N 353 
PHE CZ   C Y N 354 
PHE OXT  O N N 355 
PHE H    H N N 356 
PHE H2   H N N 357 
PHE HA   H N N 358 
PHE HB2  H N N 359 
PHE HB3  H N N 360 
PHE HD1  H N N 361 
PHE HD2  H N N 362 
PHE HE1  H N N 363 
PHE HE2  H N N 364 
PHE HZ   H N N 365 
PHE HXT  H N N 366 
PRO N    N N N 367 
PRO CA   C N S 368 
PRO C    C N N 369 
PRO O    O N N 370 
PRO CB   C N N 371 
PRO CG   C N N 372 
PRO CD   C N N 373 
PRO OXT  O N N 374 
PRO H    H N N 375 
PRO HA   H N N 376 
PRO HB2  H N N 377 
PRO HB3  H N N 378 
PRO HG2  H N N 379 
PRO HG3  H N N 380 
PRO HD2  H N N 381 
PRO HD3  H N N 382 
PRO HXT  H N N 383 
SER N    N N N 384 
SER CA   C N S 385 
SER C    C N N 386 
SER O    O N N 387 
SER CB   C N N 388 
SER OG   O N N 389 
SER OXT  O N N 390 
SER H    H N N 391 
SER H2   H N N 392 
SER HA   H N N 393 
SER HB2  H N N 394 
SER HB3  H N N 395 
SER HG   H N N 396 
SER HXT  H N N 397 
SO4 S    S N N 398 
SO4 O1   O N N 399 
SO4 O2   O N N 400 
SO4 O3   O N N 401 
SO4 O4   O N N 402 
THR N    N N N 403 
THR CA   C N S 404 
THR C    C N N 405 
THR O    O N N 406 
THR CB   C N R 407 
THR OG1  O N N 408 
THR CG2  C N N 409 
THR OXT  O N N 410 
THR H    H N N 411 
THR H2   H N N 412 
THR HA   H N N 413 
THR HB   H N N 414 
THR HG1  H N N 415 
THR HG21 H N N 416 
THR HG22 H N N 417 
THR HG23 H N N 418 
THR HXT  H N N 419 
TRP N    N N N 420 
TRP CA   C N S 421 
TRP C    C N N 422 
TRP O    O N N 423 
TRP CB   C N N 424 
TRP CG   C Y N 425 
TRP CD1  C Y N 426 
TRP CD2  C Y N 427 
TRP NE1  N Y N 428 
TRP CE2  C Y N 429 
TRP CE3  C Y N 430 
TRP CZ2  C Y N 431 
TRP CZ3  C Y N 432 
TRP CH2  C Y N 433 
TRP OXT  O N N 434 
TRP H    H N N 435 
TRP H2   H N N 436 
TRP HA   H N N 437 
TRP HB2  H N N 438 
TRP HB3  H N N 439 
TRP HD1  H N N 440 
TRP HE1  H N N 441 
TRP HE3  H N N 442 
TRP HZ2  H N N 443 
TRP HZ3  H N N 444 
TRP HH2  H N N 445 
TRP HXT  H N N 446 
TYR N    N N N 447 
TYR CA   C N S 448 
TYR C    C N N 449 
TYR O    O N N 450 
TYR CB   C N N 451 
TYR CG   C Y N 452 
TYR CD1  C Y N 453 
TYR CD2  C Y N 454 
TYR CE1  C Y N 455 
TYR CE2  C Y N 456 
TYR CZ   C Y N 457 
TYR OH   O N N 458 
TYR OXT  O N N 459 
TYR H    H N N 460 
TYR H2   H N N 461 
TYR HA   H N N 462 
TYR HB2  H N N 463 
TYR HB3  H N N 464 
TYR HD1  H N N 465 
TYR HD2  H N N 466 
TYR HE1  H N N 467 
TYR HE2  H N N 468 
TYR HH   H N N 469 
TYR HXT  H N N 470 
VAL N    N N N 471 
VAL CA   C N S 472 
VAL C    C N N 473 
VAL O    O N N 474 
VAL CB   C N N 475 
VAL CG1  C N N 476 
VAL CG2  C N N 477 
VAL OXT  O N N 478 
VAL H    H N N 479 
VAL H2   H N N 480 
VAL HA   H N N 481 
VAL HB   H N N 482 
VAL HG11 H N N 483 
VAL HG12 H N N 484 
VAL HG13 H N N 485 
VAL HG21 H N N 486 
VAL HG22 H N N 487 
VAL HG23 H N N 488 
VAL HXT  H N N 489 
# 
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 
1PE OH2 C12  sing N N 1   
1PE OH2 HO2  sing N N 2   
1PE C12 C22  sing N N 3   
1PE C12 H121 sing N N 4   
1PE C12 H122 sing N N 5   
1PE C22 OH3  sing N N 6   
1PE C22 H221 sing N N 7   
1PE C22 H222 sing N N 8   
1PE OH3 C23  sing N N 9   
1PE C13 C23  sing N N 10  
1PE C13 OH4  sing N N 11  
1PE C13 H131 sing N N 12  
1PE C13 H132 sing N N 13  
1PE C23 H231 sing N N 14  
1PE C23 H232 sing N N 15  
1PE OH4 C24  sing N N 16  
1PE C14 C24  sing N N 17  
1PE C14 OH5  sing N N 18  
1PE C14 H141 sing N N 19  
1PE C14 H142 sing N N 20  
1PE C24 H241 sing N N 21  
1PE C24 H242 sing N N 22  
1PE OH5 C25  sing N N 23  
1PE C15 C25  sing N N 24  
1PE C15 OH6  sing N N 25  
1PE C15 H151 sing N N 26  
1PE C15 H152 sing N N 27  
1PE C25 H251 sing N N 28  
1PE C25 H252 sing N N 29  
1PE OH6 C26  sing N N 30  
1PE C16 C26  sing N N 31  
1PE C16 OH7  sing N N 32  
1PE C16 H161 sing N N 33  
1PE C16 H162 sing N N 34  
1PE C26 H261 sing N N 35  
1PE C26 H262 sing N N 36  
1PE OH7 HO7  sing N N 37  
ACT C   O    doub N N 38  
ACT C   OXT  sing N N 39  
ACT C   CH3  sing N N 40  
ACT CH3 H1   sing N N 41  
ACT CH3 H2   sing N N 42  
ACT CH3 H3   sing N N 43  
ALA N   CA   sing N N 44  
ALA N   H    sing N N 45  
ALA N   H2   sing N N 46  
ALA CA  C    sing N N 47  
ALA CA  CB   sing N N 48  
ALA CA  HA   sing N N 49  
ALA C   O    doub N N 50  
ALA C   OXT  sing N N 51  
ALA CB  HB1  sing N N 52  
ALA CB  HB2  sing N N 53  
ALA CB  HB3  sing N N 54  
ALA OXT HXT  sing N N 55  
ARG N   CA   sing N N 56  
ARG N   H    sing N N 57  
ARG N   H2   sing N N 58  
ARG CA  C    sing N N 59  
ARG CA  CB   sing N N 60  
ARG CA  HA   sing N N 61  
ARG C   O    doub N N 62  
ARG C   OXT  sing N N 63  
ARG CB  CG   sing N N 64  
ARG CB  HB2  sing N N 65  
ARG CB  HB3  sing N N 66  
ARG CG  CD   sing N N 67  
ARG CG  HG2  sing N N 68  
ARG CG  HG3  sing N N 69  
ARG CD  NE   sing N N 70  
ARG CD  HD2  sing N N 71  
ARG CD  HD3  sing N N 72  
ARG NE  CZ   sing N N 73  
ARG NE  HE   sing N N 74  
ARG CZ  NH1  sing N N 75  
ARG CZ  NH2  doub N N 76  
ARG NH1 HH11 sing N N 77  
ARG NH1 HH12 sing N N 78  
ARG NH2 HH21 sing N N 79  
ARG NH2 HH22 sing N N 80  
ARG OXT HXT  sing N N 81  
ASN N   CA   sing N N 82  
ASN N   H    sing N N 83  
ASN N   H2   sing N N 84  
ASN CA  C    sing N N 85  
ASN CA  CB   sing N N 86  
ASN CA  HA   sing N N 87  
ASN C   O    doub N N 88  
ASN C   OXT  sing N N 89  
ASN CB  CG   sing N N 90  
ASN CB  HB2  sing N N 91  
ASN CB  HB3  sing N N 92  
ASN CG  OD1  doub N N 93  
ASN CG  ND2  sing N N 94  
ASN ND2 HD21 sing N N 95  
ASN ND2 HD22 sing N N 96  
ASN OXT HXT  sing N N 97  
ASP N   CA   sing N N 98  
ASP N   H    sing N N 99  
ASP N   H2   sing N N 100 
ASP CA  C    sing N N 101 
ASP CA  CB   sing N N 102 
ASP CA  HA   sing N N 103 
ASP C   O    doub N N 104 
ASP C   OXT  sing N N 105 
ASP CB  CG   sing N N 106 
ASP CB  HB2  sing N N 107 
ASP CB  HB3  sing N N 108 
ASP CG  OD1  doub N N 109 
ASP CG  OD2  sing N N 110 
ASP OD2 HD2  sing N N 111 
ASP OXT HXT  sing N N 112 
CYS N   CA   sing N N 113 
CYS N   H    sing N N 114 
CYS N   H2   sing N N 115 
CYS CA  C    sing N N 116 
CYS CA  CB   sing N N 117 
CYS CA  HA   sing N N 118 
CYS C   O    doub N N 119 
CYS C   OXT  sing N N 120 
CYS CB  SG   sing N N 121 
CYS CB  HB2  sing N N 122 
CYS CB  HB3  sing N N 123 
CYS SG  HG   sing N N 124 
CYS OXT HXT  sing N N 125 
EDO C1  O1   sing N N 126 
EDO C1  C2   sing N N 127 
EDO C1  H11  sing N N 128 
EDO C1  H12  sing N N 129 
EDO O1  HO1  sing N N 130 
EDO C2  O2   sing N N 131 
EDO C2  H21  sing N N 132 
EDO C2  H22  sing N N 133 
EDO O2  HO2  sing N N 134 
GLN N   CA   sing N N 135 
GLN N   H    sing N N 136 
GLN N   H2   sing N N 137 
GLN CA  C    sing N N 138 
GLN CA  CB   sing N N 139 
GLN CA  HA   sing N N 140 
GLN C   O    doub N N 141 
GLN C   OXT  sing N N 142 
GLN CB  CG   sing N N 143 
GLN CB  HB2  sing N N 144 
GLN CB  HB3  sing N N 145 
GLN CG  CD   sing N N 146 
GLN CG  HG2  sing N N 147 
GLN CG  HG3  sing N N 148 
GLN CD  OE1  doub N N 149 
GLN CD  NE2  sing N N 150 
GLN NE2 HE21 sing N N 151 
GLN NE2 HE22 sing N N 152 
GLN OXT HXT  sing N N 153 
GLU N   CA   sing N N 154 
GLU N   H    sing N N 155 
GLU N   H2   sing N N 156 
GLU CA  C    sing N N 157 
GLU CA  CB   sing N N 158 
GLU CA  HA   sing N N 159 
GLU C   O    doub N N 160 
GLU C   OXT  sing N N 161 
GLU CB  CG   sing N N 162 
GLU CB  HB2  sing N N 163 
GLU CB  HB3  sing N N 164 
GLU CG  CD   sing N N 165 
GLU CG  HG2  sing N N 166 
GLU CG  HG3  sing N N 167 
GLU CD  OE1  doub N N 168 
GLU CD  OE2  sing N N 169 
GLU OE2 HE2  sing N N 170 
GLU OXT HXT  sing N N 171 
GLY N   CA   sing N N 172 
GLY N   H    sing N N 173 
GLY N   H2   sing N N 174 
GLY CA  C    sing N N 175 
GLY CA  HA2  sing N N 176 
GLY CA  HA3  sing N N 177 
GLY C   O    doub N N 178 
GLY C   OXT  sing N N 179 
GLY OXT HXT  sing N N 180 
GOL C1  O1   sing N N 181 
GOL C1  C2   sing N N 182 
GOL C1  H11  sing N N 183 
GOL C1  H12  sing N N 184 
GOL O1  HO1  sing N N 185 
GOL C2  O2   sing N N 186 
GOL C2  C3   sing N N 187 
GOL C2  H2   sing N N 188 
GOL O2  HO2  sing N N 189 
GOL C3  O3   sing N N 190 
GOL C3  H31  sing N N 191 
GOL C3  H32  sing N N 192 
GOL O3  HO3  sing N N 193 
HIS N   CA   sing N N 194 
HIS N   H    sing N N 195 
HIS N   H2   sing N N 196 
HIS CA  C    sing N N 197 
HIS CA  CB   sing N N 198 
HIS CA  HA   sing N N 199 
HIS C   O    doub N N 200 
HIS C   OXT  sing N N 201 
HIS CB  CG   sing N N 202 
HIS CB  HB2  sing N N 203 
HIS CB  HB3  sing N N 204 
HIS CG  ND1  sing Y N 205 
HIS CG  CD2  doub Y N 206 
HIS ND1 CE1  doub Y N 207 
HIS ND1 HD1  sing N N 208 
HIS CD2 NE2  sing Y N 209 
HIS CD2 HD2  sing N N 210 
HIS CE1 NE2  sing Y N 211 
HIS CE1 HE1  sing N N 212 
HIS NE2 HE2  sing N N 213 
HIS OXT HXT  sing N N 214 
HOH O   H1   sing N N 215 
HOH O   H2   sing N N 216 
ILE N   CA   sing N N 217 
ILE N   H    sing N N 218 
ILE N   H2   sing N N 219 
ILE CA  C    sing N N 220 
ILE CA  CB   sing N N 221 
ILE CA  HA   sing N N 222 
ILE C   O    doub N N 223 
ILE C   OXT  sing N N 224 
ILE CB  CG1  sing N N 225 
ILE CB  CG2  sing N N 226 
ILE CB  HB   sing N N 227 
ILE CG1 CD1  sing N N 228 
ILE CG1 HG12 sing N N 229 
ILE CG1 HG13 sing N N 230 
ILE CG2 HG21 sing N N 231 
ILE CG2 HG22 sing N N 232 
ILE CG2 HG23 sing N N 233 
ILE CD1 HD11 sing N N 234 
ILE CD1 HD12 sing N N 235 
ILE CD1 HD13 sing N N 236 
ILE OXT HXT  sing N N 237 
LEU N   CA   sing N N 238 
LEU N   H    sing N N 239 
LEU N   H2   sing N N 240 
LEU CA  C    sing N N 241 
LEU CA  CB   sing N N 242 
LEU CA  HA   sing N N 243 
LEU C   O    doub N N 244 
LEU C   OXT  sing N N 245 
LEU CB  CG   sing N N 246 
LEU CB  HB2  sing N N 247 
LEU CB  HB3  sing N N 248 
LEU CG  CD1  sing N N 249 
LEU CG  CD2  sing N N 250 
LEU CG  HG   sing N N 251 
LEU CD1 HD11 sing N N 252 
LEU CD1 HD12 sing N N 253 
LEU CD1 HD13 sing N N 254 
LEU CD2 HD21 sing N N 255 
LEU CD2 HD22 sing N N 256 
LEU CD2 HD23 sing N N 257 
LEU OXT HXT  sing N N 258 
LYS N   CA   sing N N 259 
LYS N   H    sing N N 260 
LYS N   H2   sing N N 261 
LYS CA  C    sing N N 262 
LYS CA  CB   sing N N 263 
LYS CA  HA   sing N N 264 
LYS C   O    doub N N 265 
LYS C   OXT  sing N N 266 
LYS CB  CG   sing N N 267 
LYS CB  HB2  sing N N 268 
LYS CB  HB3  sing N N 269 
LYS CG  CD   sing N N 270 
LYS CG  HG2  sing N N 271 
LYS CG  HG3  sing N N 272 
LYS CD  CE   sing N N 273 
LYS CD  HD2  sing N N 274 
LYS CD  HD3  sing N N 275 
LYS CE  NZ   sing N N 276 
LYS CE  HE2  sing N N 277 
LYS CE  HE3  sing N N 278 
LYS NZ  HZ1  sing N N 279 
LYS NZ  HZ2  sing N N 280 
LYS NZ  HZ3  sing N N 281 
LYS OXT HXT  sing N N 282 
MES O1  C2   sing N N 283 
MES O1  C6   sing N N 284 
MES C2  C3   sing N N 285 
MES C2  H21  sing N N 286 
MES C2  H22  sing N N 287 
MES C3  N4   sing N N 288 
MES C3  H31  sing N N 289 
MES C3  H32  sing N N 290 
MES N4  C5   sing N N 291 
MES N4  C7   sing N N 292 
MES N4  HN4  sing N N 293 
MES C5  C6   sing N N 294 
MES C5  H51  sing N N 295 
MES C5  H52  sing N N 296 
MES C6  H61  sing N N 297 
MES C6  H62  sing N N 298 
MES C7  C8   sing N N 299 
MES C7  H71  sing N N 300 
MES C7  H72  sing N N 301 
MES C8  S    sing N N 302 
MES C8  H81  sing N N 303 
MES C8  H82  sing N N 304 
MES S   O1S  doub N N 305 
MES S   O2S  doub N N 306 
MES S   O3S  sing N N 307 
MET N   CA   sing N N 308 
MET N   H    sing N N 309 
MET N   H2   sing N N 310 
MET CA  C    sing N N 311 
MET CA  CB   sing N N 312 
MET CA  HA   sing N N 313 
MET C   O    doub N N 314 
MET C   OXT  sing N N 315 
MET CB  CG   sing N N 316 
MET CB  HB2  sing N N 317 
MET CB  HB3  sing N N 318 
MET CG  SD   sing N N 319 
MET CG  HG2  sing N N 320 
MET CG  HG3  sing N N 321 
MET SD  CE   sing N N 322 
MET CE  HE1  sing N N 323 
MET CE  HE2  sing N N 324 
MET CE  HE3  sing N N 325 
MET OXT HXT  sing N N 326 
PHE N   CA   sing N N 327 
PHE N   H    sing N N 328 
PHE N   H2   sing N N 329 
PHE CA  C    sing N N 330 
PHE CA  CB   sing N N 331 
PHE CA  HA   sing N N 332 
PHE C   O    doub N N 333 
PHE C   OXT  sing N N 334 
PHE CB  CG   sing N N 335 
PHE CB  HB2  sing N N 336 
PHE CB  HB3  sing N N 337 
PHE CG  CD1  doub Y N 338 
PHE CG  CD2  sing Y N 339 
PHE CD1 CE1  sing Y N 340 
PHE CD1 HD1  sing N N 341 
PHE CD2 CE2  doub Y N 342 
PHE CD2 HD2  sing N N 343 
PHE CE1 CZ   doub Y N 344 
PHE CE1 HE1  sing N N 345 
PHE CE2 CZ   sing Y N 346 
PHE CE2 HE2  sing N N 347 
PHE CZ  HZ   sing N N 348 
PHE OXT HXT  sing N N 349 
PRO N   CA   sing N N 350 
PRO N   CD   sing N N 351 
PRO N   H    sing N N 352 
PRO CA  C    sing N N 353 
PRO CA  CB   sing N N 354 
PRO CA  HA   sing N N 355 
PRO C   O    doub N N 356 
PRO C   OXT  sing N N 357 
PRO CB  CG   sing N N 358 
PRO CB  HB2  sing N N 359 
PRO CB  HB3  sing N N 360 
PRO CG  CD   sing N N 361 
PRO CG  HG2  sing N N 362 
PRO CG  HG3  sing N N 363 
PRO CD  HD2  sing N N 364 
PRO CD  HD3  sing N N 365 
PRO OXT HXT  sing N N 366 
SER N   CA   sing N N 367 
SER N   H    sing N N 368 
SER N   H2   sing N N 369 
SER CA  C    sing N N 370 
SER CA  CB   sing N N 371 
SER CA  HA   sing N N 372 
SER C   O    doub N N 373 
SER C   OXT  sing N N 374 
SER CB  OG   sing N N 375 
SER CB  HB2  sing N N 376 
SER CB  HB3  sing N N 377 
SER OG  HG   sing N N 378 
SER OXT HXT  sing N N 379 
SO4 S   O1   doub N N 380 
SO4 S   O2   doub N N 381 
SO4 S   O3   sing N N 382 
SO4 S   O4   sing N N 383 
THR N   CA   sing N N 384 
THR N   H    sing N N 385 
THR N   H2   sing N N 386 
THR CA  C    sing N N 387 
THR CA  CB   sing N N 388 
THR CA  HA   sing N N 389 
THR C   O    doub N N 390 
THR C   OXT  sing N N 391 
THR CB  OG1  sing N N 392 
THR CB  CG2  sing N N 393 
THR CB  HB   sing N N 394 
THR OG1 HG1  sing N N 395 
THR CG2 HG21 sing N N 396 
THR CG2 HG22 sing N N 397 
THR CG2 HG23 sing N N 398 
THR OXT HXT  sing N N 399 
TRP N   CA   sing N N 400 
TRP N   H    sing N N 401 
TRP N   H2   sing N N 402 
TRP CA  C    sing N N 403 
TRP CA  CB   sing N N 404 
TRP CA  HA   sing N N 405 
TRP C   O    doub N N 406 
TRP C   OXT  sing N N 407 
TRP CB  CG   sing N N 408 
TRP CB  HB2  sing N N 409 
TRP CB  HB3  sing N N 410 
TRP CG  CD1  doub Y N 411 
TRP CG  CD2  sing Y N 412 
TRP CD1 NE1  sing Y N 413 
TRP CD1 HD1  sing N N 414 
TRP CD2 CE2  doub Y N 415 
TRP CD2 CE3  sing Y N 416 
TRP NE1 CE2  sing Y N 417 
TRP NE1 HE1  sing N N 418 
TRP CE2 CZ2  sing Y N 419 
TRP CE3 CZ3  doub Y N 420 
TRP CE3 HE3  sing N N 421 
TRP CZ2 CH2  doub Y N 422 
TRP CZ2 HZ2  sing N N 423 
TRP CZ3 CH2  sing Y N 424 
TRP CZ3 HZ3  sing N N 425 
TRP CH2 HH2  sing N N 426 
TRP OXT HXT  sing N N 427 
TYR N   CA   sing N N 428 
TYR N   H    sing N N 429 
TYR N   H2   sing N N 430 
TYR CA  C    sing N N 431 
TYR CA  CB   sing N N 432 
TYR CA  HA   sing N N 433 
TYR C   O    doub N N 434 
TYR C   OXT  sing N N 435 
TYR CB  CG   sing N N 436 
TYR CB  HB2  sing N N 437 
TYR CB  HB3  sing N N 438 
TYR CG  CD1  doub Y N 439 
TYR CG  CD2  sing Y N 440 
TYR CD1 CE1  sing Y N 441 
TYR CD1 HD1  sing N N 442 
TYR CD2 CE2  doub Y N 443 
TYR CD2 HD2  sing N N 444 
TYR CE1 CZ   doub Y N 445 
TYR CE1 HE1  sing N N 446 
TYR CE2 CZ   sing Y N 447 
TYR CE2 HE2  sing N N 448 
TYR CZ  OH   sing N N 449 
TYR OH  HH   sing N N 450 
TYR OXT HXT  sing N N 451 
VAL N   CA   sing N N 452 
VAL N   H    sing N N 453 
VAL N   H2   sing N N 454 
VAL CA  C    sing N N 455 
VAL CA  CB   sing N N 456 
VAL CA  HA   sing N N 457 
VAL C   O    doub N N 458 
VAL C   OXT  sing N N 459 
VAL CB  CG1  sing N N 460 
VAL CB  CG2  sing N N 461 
VAL CB  HB   sing N N 462 
VAL CG1 HG11 sing N N 463 
VAL CG1 HG12 sing N N 464 
VAL CG1 HG13 sing N N 465 
VAL CG2 HG21 sing N N 466 
VAL CG2 HG22 sing N N 467 
VAL CG2 HG23 sing N N 468 
VAL OXT HXT  sing N N 469 
# 
_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                    9QFV 
_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]   0.012717 
_atom_sites.fract_transf_matrix[1][2]   0.007342 
_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]   0.014684 
_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]   0.006059 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ILE A  1 1   ? 31.935 19.242  93.065  1.00 37.47  ? 16  ILE A N   1 
ATOM   2    C CA  . ILE A  1 1   ? 33.182 20.082  93.065  1.00 35.79  ? 16  ILE A CA  1 
ATOM   3    C C   . ILE A  1 1   ? 34.396 19.148  92.981  1.00 36.03  ? 16  ILE A C   1 
ATOM   4    O O   . ILE A  1 1   ? 34.488 18.224  93.821  1.00 36.67  ? 16  ILE A O   1 
ATOM   5    C CB  . ILE A  1 1   ? 33.248 21.007  94.303  1.00 36.17  ? 16  ILE A CB  1 
ATOM   6    C CG1 . ILE A  1 1   ? 32.067 21.985  94.362  1.00 34.74  ? 16  ILE A CG1 1 
ATOM   7    C CG2 . ILE A  1 1   ? 34.590 21.737  94.386  1.00 35.53  ? 16  ILE A CG2 1 
ATOM   8    C CD1 . ILE A  1 1   ? 32.057 23.041  93.271  1.00 35.28  ? 16  ILE A CD1 1 
ATOM   9    N N   . VAL A  1 2   ? 35.284 19.383  92.006  1.00 35.53  ? 17  VAL A N   1 
ATOM   10   C CA  . VAL A  1 2   ? 36.534 18.593  91.786  1.00 38.43  ? 17  VAL A CA  1 
ATOM   11   C C   . VAL A  1 2   ? 37.705 19.344  92.431  1.00 40.01  ? 17  VAL A C   1 
ATOM   12   O O   . VAL A  1 2   ? 37.833 20.557  92.180  1.00 38.00  ? 17  VAL A O   1 
ATOM   13   C CB  . VAL A  1 2   ? 36.794 18.353  90.286  1.00 39.05  ? 17  VAL A CB  1 
ATOM   14   C CG1 . VAL A  1 2   ? 38.044 17.515  90.041  1.00 40.47  ? 17  VAL A CG1 1 
ATOM   15   C CG2 . VAL A  1 2   ? 35.596 17.716  89.604  1.00 39.47  ? 17  VAL A CG2 1 
ATOM   16   N N   . GLY A  1 3   ? 38.536 18.633  93.207  1.00 41.13  ? 18  GLY A N   1 
ATOM   17   C CA  . GLY A  1 3   ? 39.751 19.156  93.863  1.00 40.95  ? 18  GLY A CA  1 
ATOM   18   C C   . GLY A  1 3   ? 39.435 20.144  94.970  1.00 42.02  ? 18  GLY A C   1 
ATOM   19   O O   . GLY A  1 3   ? 40.321 20.945  95.324  1.00 43.44  ? 18  GLY A O   1 
ATOM   20   N N   . GLY A  1 4   ? 38.226 20.081  95.528  1.00 41.77  ? 19  GLY A N   1 
ATOM   21   C CA  . GLY A  1 4   ? 37.758 21.023  96.553  1.00 45.38  ? 19  GLY A CA  1 
ATOM   22   C C   . GLY A  1 4   ? 38.084 20.534  97.951  1.00 46.40  ? 19  GLY A C   1 
ATOM   23   O O   . GLY A  1 4   ? 38.801 19.522  98.098  1.00 45.76  ? 19  GLY A O   1 
ATOM   24   N N   . GLN A  1 5   ? 37.583 21.258  98.947  1.00 43.91  ? 20  GLN A N   1 
ATOM   25   C CA  . GLN A  1 5   ? 37.548 20.853  100.374 1.00 43.19  ? 20  GLN A CA  1 
ATOM   26   C C   . GLN A  1 5   ? 36.151 21.156  100.899 1.00 40.06  ? 20  GLN A C   1 
ATOM   27   O O   . GLN A  1 5   ? 35.440 21.951  100.245 1.00 37.57  ? 20  GLN A O   1 
ATOM   28   C CB  . GLN A  1 5   ? 38.613 21.610  101.170 1.00 43.50  ? 20  GLN A CB  1 
ATOM   29   C CG  . GLN A  1 5   ? 40.020 21.218  100.753 1.00 47.61  ? 20  GLN A CG  1 
ATOM   30   C CD  . GLN A  1 5   ? 41.096 22.141  101.263 1.00 46.81  ? 20  GLN A CD  1 
ATOM   31   O OE1 . GLN A  1 5   ? 40.841 23.270  101.674 1.00 50.44  ? 20  GLN A OE1 1 
ATOM   32   N NE2 . GLN A  1 5   ? 42.326 21.666  101.203 1.00 47.96  ? 20  GLN A NE2 1 
ATOM   33   N N   . GLU A  1 6   ? 35.794 20.571  102.041 1.00 37.54  ? 21  GLU A N   1 
ATOM   34   C CA  . GLU A  1 6   ? 34.547 20.904  102.778 1.00 39.24  ? 21  GLU A CA  1 
ATOM   35   C C   . GLU A  1 6   ? 34.601 22.389  103.139 1.00 38.73  ? 21  GLU A C   1 
ATOM   36   O O   . GLU A  1 6   ? 35.675 22.855  103.588 1.00 39.15  ? 21  GLU A O   1 
ATOM   37   C CB  . GLU A  1 6   ? 34.379 20.026  104.021 1.00 40.81  ? 21  GLU A CB  1 
ATOM   38   C CG  . GLU A  1 6   ? 33.124 20.346  104.830 1.00 43.41  ? 21  GLU A CG  1 
ATOM   39   C CD  . GLU A  1 6   ? 32.690 19.280  105.833 1.00 43.77  ? 21  GLU A CD  1 
ATOM   40   O OE1 . GLU A  1 6   ? 33.348 18.220  105.897 1.00 43.02  ? 21  GLU A OE1 1 
ATOM   41   O OE2 . GLU A  1 6   ? 31.691 19.508  106.552 1.00 43.59  ? 21  GLU A OE2 1 
ATOM   42   N N   . ALA A  1 7   ? 33.512 23.116  102.887 1.00 37.51  ? 22  ALA A N   1 
ATOM   43   C CA  . ALA A  1 7   ? 33.354 24.541  103.244 1.00 39.72  ? 22  ALA A CA  1 
ATOM   44   C C   . ALA A  1 7   ? 33.309 24.663  104.764 1.00 43.24  ? 22  ALA A C   1 
ATOM   45   O O   . ALA A  1 7   ? 32.662 23.850  105.421 1.00 42.96  ? 22  ALA A O   1 
ATOM   46   C CB  . ALA A  1 7   ? 32.090 25.096  102.628 1.00 40.17  ? 22  ALA A CB  1 
ATOM   47   N N   . PRO A  1 8   ? 33.973 25.670  105.380 1.00 41.73  ? 23  PRO A N   1 
ATOM   48   C CA  . PRO A  1 8   ? 33.674 26.030  106.763 1.00 42.35  ? 23  PRO A CA  1 
ATOM   49   C C   . PRO A  1 8   ? 32.201 26.453  106.890 1.00 41.52  ? 23  PRO A C   1 
ATOM   50   O O   . PRO A  1 8   ? 31.658 27.017  105.934 1.00 41.05  ? 23  PRO A O   1 
ATOM   51   C CB  . PRO A  1 8   ? 34.628 27.191  107.096 1.00 41.96  ? 23  PRO A CB  1 
ATOM   52   C CG  . PRO A  1 8   ? 35.671 27.187  105.993 1.00 42.25  ? 23  PRO A CG  1 
ATOM   53   C CD  . PRO A  1 8   ? 35.032 26.507  104.799 1.00 43.39  ? 23  PRO A CD  1 
ATOM   54   N N   . ARG A  1 9   ? 31.601 26.170  108.049 1.00 40.53  ? 24  ARG A N   1 
ATOM   55   C CA  . ARG A  1 9   ? 30.170 26.442  108.370 1.00 43.00  ? 24  ARG A CA  1 
ATOM   56   C C   . ARG A  1 9   ? 29.820 27.923  108.171 1.00 42.98  ? 24  ARG A C   1 
ATOM   57   O O   . ARG A  1 9   ? 28.663 28.189  107.813 1.00 43.14  ? 24  ARG A O   1 
ATOM   58   C CB  . ARG A  1 9   ? 29.858 26.029  109.811 1.00 47.14  ? 24  ARG A CB  1 
ATOM   59   C CG  . ARG A  1 9   ? 29.914 24.527  110.036 1.00 50.83  ? 24  ARG A CG  1 
ATOM   60   C CD  . ARG A  1 9   ? 29.427 24.102  111.409 1.00 51.98  ? 24  ARG A CD  1 
ATOM   61   N NE  . ARG A  1 9   ? 29.076 22.687  111.378 1.00 56.27  ? 24  ARG A NE  1 
ATOM   62   C CZ  . ARG A  1 9   ? 27.886 22.177  111.039 1.00 54.07  ? 24  ARG A CZ  1 
ATOM   63   N NH1 . ARG A  1 9   ? 26.874 22.962  110.701 1.00 52.30  ? 24  ARG A NH1 1 
ATOM   64   N NH2 . ARG A  1 9   ? 27.719 20.863  111.046 1.00 53.54  ? 24  ARG A NH2 1 
ATOM   65   N N   . SER A  1 10  ? 30.768 28.841  108.395 1.00 45.34  ? 25  SER A N   1 
ATOM   66   C CA  . SER A  1 10  ? 30.559 30.315  108.305 1.00 47.97  ? 25  SER A CA  1 
ATOM   67   C C   . SER A  1 10  ? 30.534 30.808  106.850 1.00 47.02  ? 25  SER A C   1 
ATOM   68   O O   . SER A  1 10  ? 30.037 31.926  106.644 1.00 51.44  ? 25  SER A O   1 
ATOM   69   C CB  . SER A  1 10  ? 31.600 31.065  109.099 1.00 48.44  ? 25  SER A CB  1 
ATOM   70   O OG  . SER A  1 10  ? 32.907 30.754  108.635 1.00 49.31  ? 25  SER A OG  1 
ATOM   71   N N   . LYS A  1 11  ? 31.009 30.015  105.877 1.00 44.27  ? 26  LYS A N   1 
ATOM   72   C CA  . LYS A  1 11  ? 31.220 30.468  104.474 1.00 42.72  ? 26  LYS A CA  1 
ATOM   73   C C   . LYS A  1 11  ? 30.007 30.129  103.599 1.00 41.53  ? 26  LYS A C   1 
ATOM   74   O O   . LYS A  1 11  ? 29.346 29.098  103.852 1.00 37.35  ? 26  LYS A O   1 
ATOM   75   C CB  . LYS A  1 11  ? 32.477 29.832  103.872 1.00 42.88  ? 26  LYS A CB  1 
ATOM   76   C CG  . LYS A  1 11  ? 33.760 30.010  104.674 1.00 45.16  ? 26  LYS A CG  1 
ATOM   77   C CD  . LYS A  1 11  ? 34.026 31.428  105.138 1.00 47.29  ? 26  LYS A CD  1 
ATOM   78   C CE  . LYS A  1 11  ? 35.410 31.616  105.723 1.00 48.03  ? 26  LYS A CE  1 
ATOM   79   N NZ  . LYS A  1 11  ? 35.567 32.972  106.297 1.00 48.80  ? 26  LYS A NZ  1 
ATOM   80   N N   . TRP A  1 12  ? 29.758 30.975  102.593 1.00 38.60  ? 27  TRP A N   1 
ATOM   81   C CA  . TRP A  1 12  ? 28.767 30.783  101.498 1.00 37.01  ? 27  TRP A CA  1 
ATOM   82   C C   . TRP A  1 12  ? 27.347 30.704  102.059 1.00 36.86  ? 27  TRP A C   1 
ATOM   83   O O   . TRP A  1 12  ? 26.639 29.729  101.823 1.00 36.34  ? 27  TRP A O   1 
ATOM   84   C CB  . TRP A  1 12  ? 29.122 29.547  100.661 1.00 35.81  ? 27  TRP A CB  1 
ATOM   85   C CG  . TRP A  1 12  ? 30.586 29.249  100.574 1.00 36.09  ? 27  TRP A CG  1 
ATOM   86   C CD1 . TRP A  1 12  ? 31.194 28.094  100.963 1.00 35.84  ? 27  TRP A CD1 1 
ATOM   87   C CD2 . TRP A  1 12  ? 31.631 30.111  100.084 1.00 35.93  ? 27  TRP A CD2 1 
ATOM   88   N NE1 . TRP A  1 12  ? 32.539 28.169  100.740 1.00 35.58  ? 27  TRP A NE1 1 
ATOM   89   C CE2 . TRP A  1 12  ? 32.839 29.389  100.195 1.00 34.80  ? 27  TRP A CE2 1 
ATOM   90   C CE3 . TRP A  1 12  ? 31.666 31.407  99.548  1.00 35.39  ? 27  TRP A CE3 1 
ATOM   91   C CZ2 . TRP A  1 12  ? 34.066 29.925  99.804  1.00 35.13  ? 27  TRP A CZ2 1 
ATOM   92   C CZ3 . TRP A  1 12  ? 32.878 31.937  99.162  1.00 34.29  ? 27  TRP A CZ3 1 
ATOM   93   C CH2 . TRP A  1 12  ? 34.062 31.209  99.298  1.00 35.49  ? 27  TRP A CH2 1 
ATOM   94   N N   . PRO A  1 13  ? 26.873 31.729  102.805 1.00 36.50  ? 28  PRO A N   1 
ATOM   95   C CA  . PRO A  1 13  ? 25.521 31.713  103.379 1.00 35.79  ? 28  PRO A CA  1 
ATOM   96   C C   . PRO A  1 13  ? 24.374 31.851  102.359 1.00 35.47  ? 28  PRO A C   1 
ATOM   97   O O   . PRO A  1 13  ? 23.217 31.713  102.753 1.00 35.14  ? 28  PRO A O   1 
ATOM   98   C CB  . PRO A  1 13  ? 25.560 32.909  104.346 1.00 36.96  ? 28  PRO A CB  1 
ATOM   99   C CG  . PRO A  1 13  ? 26.559 33.862  103.726 1.00 37.01  ? 28  PRO A CG  1 
ATOM   100  C CD  . PRO A  1 13  ? 27.614 32.958  103.135 1.00 37.12  ? 28  PRO A CD  1 
ATOM   101  N N   . TRP A  1 14  ? 24.711 32.085  101.085 1.00 33.72  ? 29  TRP A N   1 
ATOM   102  C CA  . TRP A  1 14  ? 23.765 32.268  99.948  1.00 34.28  ? 29  TRP A CA  1 
ATOM   103  C C   . TRP A  1 14  ? 23.562 30.961  99.163  1.00 34.31  ? 29  TRP A C   1 
ATOM   104  O O   . TRP A  1 14  ? 22.627 30.933  98.346  1.00 34.21  ? 29  TRP A O   1 
ATOM   105  C CB  . TRP A  1 14  ? 24.263 33.382  99.017  1.00 33.82  ? 29  TRP A CB  1 
ATOM   106  C CG  . TRP A  1 14  ? 25.714 33.262  98.681  1.00 32.86  ? 29  TRP A CG  1 
ATOM   107  C CD1 . TRP A  1 14  ? 26.290 32.364  97.836  1.00 33.72  ? 29  TRP A CD1 1 
ATOM   108  C CD2 . TRP A  1 14  ? 26.784 34.060  99.215  1.00 33.71  ? 29  TRP A CD2 1 
ATOM   109  N NE1 . TRP A  1 14  ? 27.645 32.556  97.797  1.00 36.10  ? 29  TRP A NE1 1 
ATOM   110  C CE2 . TRP A  1 14  ? 27.979 33.589  98.633  1.00 32.81  ? 29  TRP A CE2 1 
ATOM   111  C CE3 . TRP A  1 14  ? 26.849 35.119  100.127 1.00 33.47  ? 29  TRP A CE3 1 
ATOM   112  C CZ2 . TRP A  1 14  ? 29.221 34.146  98.930  1.00 33.92  ? 29  TRP A CZ2 1 
ATOM   113  C CZ3 . TRP A  1 14  ? 28.078 35.664  100.427 1.00 34.01  ? 29  TRP A CZ3 1 
ATOM   114  C CH2 . TRP A  1 14  ? 29.247 35.189  99.828  1.00 33.54  ? 29  TRP A CH2 1 
ATOM   115  N N   . GLN A  1 15  ? 24.405 29.938  99.367  1.00 34.74  ? 30  GLN A N   1 
ATOM   116  C CA  . GLN A  1 15  ? 24.321 28.637  98.643  1.00 35.78  ? 30  GLN A CA  1 
ATOM   117  C C   . GLN A  1 15  ? 22.966 27.993  98.957  1.00 34.78  ? 30  GLN A C   1 
ATOM   118  O O   . GLN A  1 15  ? 22.604 27.950  100.144 1.00 36.66  ? 30  GLN A O   1 
ATOM   119  C CB  . GLN A  1 15  ? 25.469 27.705  99.041  1.00 36.09  ? 30  GLN A CB  1 
ATOM   120  C CG  . GLN A  1 15  ? 25.444 26.351  98.340  1.00 37.20  ? 30  GLN A CG  1 
ATOM   121  C CD  . GLN A  1 15  ? 25.860 26.410  96.887  1.00 36.89  ? 30  GLN A CD  1 
ATOM   122  O OE1 . GLN A  1 15  ? 26.894 26.971  96.541  1.00 36.12  ? 30  GLN A OE1 1 
ATOM   123  N NE2 . GLN A  1 15  ? 25.077 25.783  96.020  1.00 36.50  ? 30  GLN A NE2 1 
ATOM   124  N N   . VAL A  1 16  ? 22.238 27.554  97.925  1.00 34.08  ? 31  VAL A N   1 
ATOM   125  C CA  . VAL A  1 16  ? 20.980 26.769  98.088  1.00 35.37  ? 31  VAL A CA  1 
ATOM   126  C C   . VAL A  1 16  ? 21.098 25.480  97.273  1.00 34.02  ? 31  VAL A C   1 
ATOM   127  O O   . VAL A  1 16  ? 21.925 25.423  96.340  1.00 36.20  ? 31  VAL A O   1 
ATOM   128  C CB  . VAL A  1 16  ? 19.714 27.583  97.739  1.00 37.64  ? 31  VAL A CB  1 
ATOM   129  C CG1 . VAL A  1 16  ? 19.781 29.005  98.286  1.00 37.50  ? 31  VAL A CG1 1 
ATOM   130  C CG2 . VAL A  1 16  ? 19.410 27.609  96.254  1.00 37.55  ? 31  VAL A CG2 1 
ATOM   131  N N   . SER A  1 17  ? 20.310 24.482  97.661  1.00 32.96  ? 32  SER A N   1 
ATOM   132  C CA  . SER A  1 17  ? 20.147 23.174  96.990  1.00 31.69  ? 32  SER A CA  1 
ATOM   133  C C   . SER A  1 17  ? 18.735 23.122  96.403  1.00 31.51  ? 32  SER A C   1 
ATOM   134  O O   . SER A  1 17  ? 17.788 23.436  97.134  1.00 30.65  ? 32  SER A O   1 
ATOM   135  C CB  . SER A  1 17  ? 20.424 22.048  97.974  1.00 32.83  ? 32  SER A CB  1 
ATOM   136  O OG  . SER A  1 17  ? 19.944 20.799  97.503  1.00 31.14  ? 32  SER A OG  1 
ATOM   137  N N   . LEU A  1 18  ? 18.605 22.781  95.118  1.00 32.11  ? 33  LEU A N   1 
ATOM   138  C CA  . LEU A  1 18  ? 17.294 22.557  94.449  1.00 34.16  ? 33  LEU A CA  1 
ATOM   139  C C   . LEU A  1 18  ? 16.951 21.074  94.575  1.00 31.44  ? 33  LEU A C   1 
ATOM   140  O O   . LEU A  1 18  ? 17.841 20.252  94.314  1.00 30.81  ? 33  LEU A O   1 
ATOM   141  C CB  . LEU A  1 18  ? 17.341 22.987  92.978  1.00 33.98  ? 33  LEU A CB  1 
ATOM   142  C CG  . LEU A  1 18  ? 17.828 24.406  92.680  1.00 37.22  ? 33  LEU A CG  1 
ATOM   143  C CD1 . LEU A  1 18  ? 17.441 24.812  91.258  1.00 37.80  ? 33  LEU A CD1 1 
ATOM   144  C CD2 . LEU A  1 18  ? 17.294 25.422  93.677  1.00 38.30  ? 33  LEU A CD2 1 
ATOM   145  N N   . ARG A  1 19  ? 15.709 20.763  94.958  1.00 31.96  ? 34  ARG A N   1 
ATOM   146  C CA  . ARG A  1 19  ? 15.246 19.381  95.250  1.00 32.84  ? 34  ARG A CA  1 
ATOM   147  C C   . ARG A  1 19  ? 14.072 19.030  94.337  1.00 32.52  ? 34  ARG A C   1 
ATOM   148  O O   . ARG A  1 19  ? 13.194 19.895  94.142  1.00 33.51  ? 34  ARG A O   1 
ATOM   149  C CB  . ARG A  1 19  ? 14.846 19.234  96.719  1.00 32.25  ? 34  ARG A CB  1 
ATOM   150  C CG  . ARG A  1 19  ? 15.919 19.659  97.709  1.00 32.35  ? 34  ARG A CG  1 
ATOM   151  C CD  . ARG A  1 19  ? 17.228 18.889  97.573  1.00 32.26  ? 34  ARG A CD  1 
ATOM   152  N NE  . ARG A  1 19  ? 18.088 19.141  98.717  1.00 32.82  ? 34  ARG A NE  1 
ATOM   153  C CZ  . ARG A  1 19  ? 17.894 18.673  99.958  1.00 32.18  ? 34  ARG A CZ  1 
ATOM   154  N NH1 . ARG A  1 19  ? 16.882 17.861  100.236 1.00 30.13  ? 34  ARG A NH1 1 
ATOM   155  N NH2 . ARG A  1 19  ? 18.725 19.027  100.925 1.00 29.64  ? 34  ARG A NH2 1 
ATOM   156  N N   . VAL A  1 20  ? 14.085 17.808  93.797  1.00 34.96  ? 35  VAL A N   1 
ATOM   157  C CA  . VAL A  1 20  ? 13.021 17.237  92.919  1.00 35.54  ? 35  VAL A CA  1 
ATOM   158  C C   . VAL A  1 20  ? 12.316 16.126  93.707  1.00 37.83  ? 35  VAL A C   1 
ATOM   159  O O   . VAL A  1 20  ? 13.017 15.365  94.407  1.00 34.52  ? 35  VAL A O   1 
ATOM   160  C CB  . VAL A  1 20  ? 13.580 16.738  91.566  1.00 35.77  ? 35  VAL A CB  1 
ATOM   161  C CG1 . VAL A  1 20  ? 14.646 15.656  91.702  1.00 36.30  ? 35  VAL A CG1 1 
ATOM   162  C CG2 . VAL A  1 20  ? 12.474 16.259  90.641  1.00 37.42  ? 35  VAL A CG2 1 
ATOM   163  N N   . HIS A  1 21  ? 10.985 16.043  93.599  1.00 42.50  ? 36  HIS A N   1 
ATOM   164  C CA  . HIS A  1 21  ? 10.162 15.021  94.301  1.00 47.12  ? 36  HIS A CA  1 
ATOM   165  C C   . HIS A  1 21  ? 10.440 13.647  93.684  1.00 45.86  ? 36  HIS A C   1 
ATOM   166  O O   . HIS A  1 21  ? 10.387 13.534  92.462  1.00 50.22  ? 36  HIS A O   1 
ATOM   167  C CB  . HIS A  1 21  ? 8.664  15.366  94.271  1.00 50.07  ? 36  HIS A CB  1 
ATOM   168  C CG  . HIS A  1 21  ? 7.816  14.372  94.995  1.00 52.62  ? 36  HIS A CG  1 
ATOM   169  N ND1 . HIS A  1 21  ? 7.720  14.345  96.374  1.00 55.16  ? 36  HIS A ND1 1 
ATOM   170  C CD2 . HIS A  1 21  ? 7.059  13.350  94.540  1.00 54.79  ? 36  HIS A CD2 1 
ATOM   171  C CE1 . HIS A  1 21  ? 6.920  13.365  96.738  1.00 56.55  ? 36  HIS A CE1 1 
ATOM   172  N NE2 . HIS A  1 21  ? 6.504  12.734  95.629  1.00 58.54  ? 36  HIS A NE2 1 
ATOM   173  N N   . GLY A  1 22  ? 10.738 12.658  94.521  1.00 47.87  ? 37  GLY A N   1 
ATOM   174  C CA  . GLY A  1 22  ? 10.849 11.239  94.142  1.00 48.63  ? 37  GLY A CA  1 
ATOM   175  C C   . GLY A  1 22  ? 10.678 10.357  95.374  1.00 48.73  ? 37  GLY A C   1 
ATOM   176  O O   . GLY A  1 22  ? 9.898  10.701  96.263  1.00 49.98  ? 37  GLY A O   1 
ATOM   177  N N   . PRO A  1 23  ? 11.394 9.211   95.471  1.00 46.50  ? 38  PRO A N   1 
ATOM   178  C CA  . PRO A  1 23  ? 11.474 8.450   96.721  1.00 44.82  ? 38  PRO A CA  1 
ATOM   179  C C   . PRO A  1 23  ? 11.873 9.334   97.916  1.00 45.06  ? 38  PRO A C   1 
ATOM   180  O O   . PRO A  1 23  ? 11.397 9.098   99.017  1.00 47.02  ? 38  PRO A O   1 
ATOM   181  C CB  . PRO A  1 23  ? 12.564 7.410   96.425  1.00 45.36  ? 38  PRO A CB  1 
ATOM   182  C CG  . PRO A  1 23  ? 12.494 7.215   94.930  1.00 44.66  ? 38  PRO A CG  1 
ATOM   183  C CD  . PRO A  1 23  ? 12.161 8.586   94.382  1.00 46.01  ? 38  PRO A CD  1 
ATOM   184  N N   . TYR A  1 24  ? 12.737 10.325  97.666  1.00 39.95  ? 39  TYR A N   1 
ATOM   185  C CA  . TYR A  1 24  ? 13.068 11.434  98.596  1.00 37.69  ? 39  TYR A CA  1 
ATOM   186  C C   . TYR A  1 24  ? 13.244 12.733  97.798  1.00 37.17  ? 39  TYR A C   1 
ATOM   187  O O   . TYR A  1 24  ? 13.247 12.690  96.558  1.00 38.66  ? 39  TYR A O   1 
ATOM   188  C CB  . TYR A  1 24  ? 14.311 11.087  99.415  1.00 35.99  ? 39  TYR A CB  1 
ATOM   189  C CG  . TYR A  1 24  ? 15.586 10.912  98.626  1.00 36.13  ? 39  TYR A CG  1 
ATOM   190  C CD1 . TYR A  1 24  ? 15.837 9.759   97.893  1.00 35.84  ? 39  TYR A CD1 1 
ATOM   191  C CD2 . TYR A  1 24  ? 16.571 11.889  98.646  1.00 36.71  ? 39  TYR A CD2 1 
ATOM   192  C CE1 . TYR A  1 24  ? 17.023 9.589   97.191  1.00 35.08  ? 39  TYR A CE1 1 
ATOM   193  C CE2 . TYR A  1 24  ? 17.756 11.739  97.942  1.00 35.86  ? 39  TYR A CE2 1 
ATOM   194  C CZ  . TYR A  1 24  ? 17.986 10.585  97.216  1.00 36.25  ? 39  TYR A CZ  1 
ATOM   195  O OH  . TYR A  1 24  ? 19.169 10.447  96.547  1.00 37.58  ? 39  TYR A OH  1 
ATOM   196  N N   . TRP A  1 25  ? 13.361 13.860  98.502  1.00 37.04  ? 40  TRP A N   1 
ATOM   197  C CA  . TRP A  1 25  ? 13.576 15.202  97.898  1.00 36.93  ? 40  TRP A CA  1 
ATOM   198  C C   . TRP A  1 25  ? 15.054 15.333  97.534  1.00 34.90  ? 40  TRP A C   1 
ATOM   199  O O   . TRP A  1 25  ? 15.831 15.816  98.362  1.00 37.13  ? 40  TRP A O   1 
ATOM   200  C CB  . TRP A  1 25  ? 13.089 16.312  98.832  1.00 37.21  ? 40  TRP A CB  1 
ATOM   201  C CG  . TRP A  1 25  ? 11.600 16.427  98.844  1.00 37.90  ? 40  TRP A CG  1 
ATOM   202  C CD1 . TRP A  1 25  ? 10.738 15.882  99.747  1.00 38.30  ? 40  TRP A CD1 1 
ATOM   203  C CD2 . TRP A  1 25  ? 10.790 17.135  97.890  1.00 39.39  ? 40  TRP A CD2 1 
ATOM   204  N NE1 . TRP A  1 25  ? 9.449  16.213  99.429  1.00 38.40  ? 40  TRP A NE1 1 
ATOM   205  C CE2 . TRP A  1 25  ? 9.445  16.980  98.296  1.00 39.19  ? 40  TRP A CE2 1 
ATOM   206  C CE3 . TRP A  1 25  ? 11.065 17.897  96.748  1.00 39.29  ? 40  TRP A CE3 1 
ATOM   207  C CZ2 . TRP A  1 25  ? 8.384  17.555  97.596  1.00 39.50  ? 40  TRP A CZ2 1 
ATOM   208  C CZ3 . TRP A  1 25  ? 10.017 18.458  96.051  1.00 39.03  ? 40  TRP A CZ3 1 
ATOM   209  C CH2 . TRP A  1 25  ? 8.697  18.296  96.476  1.00 41.05  ? 40  TRP A CH2 1 
ATOM   210  N N   . MET A  1 26  ? 15.409 14.882  96.331  1.00 36.32  ? 41  MET A N   1 
ATOM   211  C CA  . MET A  1 26  ? 16.806 14.665  95.885  1.00 35.85  ? 41  MET A CA  1 
ATOM   212  C C   . MET A  1 26  ? 17.382 15.972  95.325  1.00 32.71  ? 41  MET A C   1 
ATOM   213  O O   . MET A  1 26  ? 16.698 16.637  94.530  1.00 33.53  ? 41  MET A O   1 
ATOM   214  C CB  . MET A  1 26  ? 16.851 13.574  94.812  1.00 39.00  ? 41  MET A CB  1 
ATOM   215  C CG  . MET A  1 26  ? 18.253 13.122  94.460  1.00 42.31  ? 41  MET A CG  1 
ATOM   216  S SD  . MET A  1 26  ? 18.273 11.693  93.358  1.00 46.71  ? 41  MET A SD  1 
ATOM   217  C CE  . MET A  1 26  ? 17.505 12.387  91.896  1.00 46.48  ? 41  MET A CE  1 
ATOM   218  N N   . HIS A  1 27  ? 18.602 16.307  95.737  1.00 32.61  ? 42  HIS A N   1 
ATOM   219  C CA  . HIS A  1 27  ? 19.446 17.373  95.142  1.00 33.93  ? 42  HIS A CA  1 
ATOM   220  C C   . HIS A  1 27  ? 19.701 17.052  93.664  1.00 35.24  ? 42  HIS A C   1 
ATOM   221  O O   . HIS A  1 27  ? 20.145 15.927  93.381  1.00 35.17  ? 42  HIS A O   1 
ATOM   222  C CB  . HIS A  1 27  ? 20.763 17.517  95.912  1.00 33.79  ? 42  HIS A CB  1 
ATOM   223  C CG  . HIS A  1 27  ? 21.700 18.476  95.266  1.00 35.22  ? 42  HIS A CG  1 
ATOM   224  N ND1 . HIS A  1 27  ? 21.716 19.813  95.582  1.00 33.76  ? 42  HIS A ND1 1 
ATOM   225  C CD2 . HIS A  1 27  ? 22.607 18.305  94.282  1.00 34.16  ? 42  HIS A CD2 1 
ATOM   226  C CE1 . HIS A  1 27  ? 22.621 20.421  94.847  1.00 33.97  ? 42  HIS A CE1 1 
ATOM   227  N NE2 . HIS A  1 27  ? 23.174 19.520  94.039  1.00 32.01  ? 42  HIS A NE2 1 
ATOM   228  N N   . PHE A  1 28  ? 19.405 17.997  92.768  1.00 34.30  ? 43  PHE A N   1 
ATOM   229  C CA  . PHE A  1 28  ? 19.763 17.924  91.328  1.00 35.57  ? 43  PHE A CA  1 
ATOM   230  C C   . PHE A  1 28  ? 20.626 19.123  90.893  1.00 35.68  ? 43  PHE A C   1 
ATOM   231  O O   . PHE A  1 28  ? 21.378 18.960  89.920  1.00 41.12  ? 43  PHE A O   1 
ATOM   232  C CB  . PHE A  1 28  ? 18.508 17.767  90.468  1.00 32.48  ? 43  PHE A CB  1 
ATOM   233  C CG  . PHE A  1 28  ? 17.569 18.946  90.464  1.00 33.03  ? 43  PHE A CG  1 
ATOM   234  C CD1 . PHE A  1 28  ? 16.530 19.014  91.380  1.00 30.82  ? 43  PHE A CD1 1 
ATOM   235  C CD2 . PHE A  1 28  ? 17.680 19.951  89.513  1.00 31.40  ? 43  PHE A CD2 1 
ATOM   236  C CE1 . PHE A  1 28  ? 15.642 20.079  91.363  1.00 30.81  ? 43  PHE A CE1 1 
ATOM   237  C CE2 . PHE A  1 28  ? 16.799 21.022  89.508  1.00 31.75  ? 43  PHE A CE2 1 
ATOM   238  C CZ  . PHE A  1 28  ? 15.783 21.085  90.434  1.00 30.91  ? 43  PHE A CZ  1 
ATOM   239  N N   . CYS A  1 29  ? 20.520 20.289  91.542  1.00 36.57  ? 44  CYS A N   1 
ATOM   240  C CA  . CYS A  1 29  ? 21.216 21.537  91.109  1.00 37.16  ? 44  CYS A CA  1 
ATOM   241  C C   . CYS A  1 29  ? 21.432 22.473  92.301  1.00 33.90  ? 44  CYS A C   1 
ATOM   242  O O   . CYS A  1 29  ? 20.718 22.353  93.309  1.00 37.06  ? 44  CYS A O   1 
ATOM   243  C CB  . CYS A  1 29  ? 20.437 22.283  90.025  1.00 35.36  ? 44  CYS A CB  1 
ATOM   244  S SG  . CYS A  1 29  ? 20.849 21.786  88.332  1.00 44.00  ? 44  CYS A SG  1 
ATOM   245  N N   . GLY A  1 30  ? 22.389 23.382  92.154  1.00 33.16  ? 45  GLY A N   1 
ATOM   246  C CA  . GLY A  1 30  ? 22.638 24.488  93.086  1.00 32.16  ? 45  GLY A CA  1 
ATOM   247  C C   . GLY A  1 30  ? 21.901 25.744  92.668  1.00 30.75  ? 45  GLY A C   1 
ATOM   248  O O   . GLY A  1 30  ? 21.194 25.740  91.642  1.00 31.07  ? 45  GLY A O   1 
ATOM   249  N N   . GLY A  1 31  ? 22.074 26.782  93.470  1.00 31.15  ? 46  GLY A N   1 
ATOM   250  C CA  . GLY A  1 31  ? 21.492 28.120  93.298  1.00 31.10  ? 46  GLY A CA  1 
ATOM   251  C C   . GLY A  1 31  ? 22.148 29.081  94.266  1.00 31.32  ? 46  GLY A C   1 
ATOM   252  O O   . GLY A  1 31  ? 22.967 28.632  95.092  1.00 32.28  ? 46  GLY A O   1 
ATOM   253  N N   . SER A  1 32  ? 21.818 30.361  94.163  1.00 32.63  ? 47  SER A N   1 
ATOM   254  C CA  . SER A  1 32  ? 22.269 31.409  95.107  1.00 33.96  ? 47  SER A CA  1 
ATOM   255  C C   . SER A  1 32  ? 21.062 32.257  95.513  1.00 34.68  ? 47  SER A C   1 
ATOM   256  O O   . SER A  1 32  ? 20.208 32.529  94.651  1.00 37.28  ? 47  SER A O   1 
ATOM   257  C CB  . SER A  1 32  ? 23.374 32.229  94.509  1.00 33.09  ? 47  SER A CB  1 
ATOM   258  O OG  . SER A  1 32  ? 22.968 32.805  93.283  1.00 34.46  ? 47  SER A OG  1 
ATOM   259  N N   . LEU A  1 33  ? 20.992 32.627  96.788  1.00 34.61  ? 48  LEU A N   1 
ATOM   260  C CA  . LEU A  1 33  ? 19.996 33.597  97.297  1.00 37.42  ? 48  LEU A CA  1 
ATOM   261  C C   . LEU A  1 33  ? 20.519 35.002  96.967  1.00 36.30  ? 48  LEU A C   1 
ATOM   262  O O   . LEU A  1 33  ? 21.547 35.387  97.524  1.00 37.36  ? 48  LEU A O   1 
ATOM   263  C CB  . LEU A  1 33  ? 19.800 33.363  98.797  1.00 36.78  ? 48  LEU A CB  1 
ATOM   264  C CG  . LEU A  1 33  ? 18.635 34.122  99.421  1.00 38.14  ? 48  LEU A CG  1 
ATOM   265  C CD1 . LEU A  1 33  ? 17.311 33.473  99.052  1.00 37.77  ? 48  LEU A CD1 1 
ATOM   266  C CD2 . LEU A  1 33  ? 18.803 34.218  100.929 1.00 39.34  ? 48  LEU A CD2 1 
ATOM   267  N N   . ILE A  1 34  ? 19.862 35.709  96.046  1.00 36.68  ? 49  ILE A N   1 
ATOM   268  C CA  . ILE A  1 34  ? 20.249 37.080  95.587  1.00 36.65  ? 49  ILE A CA  1 
ATOM   269  C C   . ILE A  1 34  ? 19.313 38.135  96.206  1.00 36.64  ? 49  ILE A C   1 
ATOM   270  O O   . ILE A  1 34  ? 19.580 39.337  96.044  1.00 36.73  ? 49  ILE A O   1 
ATOM   271  C CB  . ILE A  1 34  ? 20.268 37.155  94.048  1.00 33.54  ? 49  ILE A CB  1 
ATOM   272  C CG1 . ILE A  1 34  ? 18.937 36.750  93.408  1.00 34.85  ? 49  ILE A CG1 1 
ATOM   273  C CG2 . ILE A  1 34  ? 21.418 36.329  93.498  1.00 34.80  ? 49  ILE A CG2 1 
ATOM   274  C CD1 . ILE A  1 34  ? 18.717 37.339  92.042  1.00 36.30  ? 49  ILE A CD1 1 
ATOM   275  N N   . HIS A  1 35  ? 18.263 37.693  96.893  1.00 37.99  ? 50  HIS A N   1 
ATOM   276  C CA  . HIS A  1 35  ? 17.214 38.533  97.526  1.00 39.71  ? 50  HIS A CA  1 
ATOM   277  C C   . HIS A  1 35  ? 16.474 37.611  98.487  1.00 39.65  ? 50  HIS A C   1 
ATOM   278  O O   . HIS A  1 35  ? 16.404 36.411  98.216  1.00 38.88  ? 50  HIS A O   1 
ATOM   279  C CB  . HIS A  1 35  ? 16.326 39.152  96.435  1.00 39.88  ? 50  HIS A CB  1 
ATOM   280  C CG  . HIS A  1 35  ? 15.220 40.035  96.908  1.00 41.95  ? 50  HIS A CG  1 
ATOM   281  N ND1 . HIS A  1 35  ? 14.015 39.538  97.381  1.00 43.87  ? 50  HIS A ND1 1 
ATOM   282  C CD2 . HIS A  1 35  ? 15.109 41.380  96.940  1.00 40.74  ? 50  HIS A CD2 1 
ATOM   283  C CE1 . HIS A  1 35  ? 13.222 40.539  97.705  1.00 40.39  ? 50  HIS A CE1 1 
ATOM   284  N NE2 . HIS A  1 35  ? 13.864 41.678  97.435  1.00 40.03  ? 50  HIS A NE2 1 
ATOM   285  N N   . PRO A  1 36  ? 15.917 38.105  99.619  1.00 40.09  ? 51  PRO A N   1 
ATOM   286  C CA  . PRO A  1 36  ? 15.136 37.257  100.525 1.00 39.47  ? 51  PRO A CA  1 
ATOM   287  C C   . PRO A  1 36  ? 14.096 36.325  99.883  1.00 38.57  ? 51  PRO A C   1 
ATOM   288  O O   . PRO A  1 36  ? 13.831 35.301  100.479 1.00 38.19  ? 51  PRO A O   1 
ATOM   289  C CB  . PRO A  1 36  ? 14.420 38.285  101.419 1.00 40.39  ? 51  PRO A CB  1 
ATOM   290  C CG  . PRO A  1 36  ? 15.413 39.426  101.503 1.00 40.56  ? 51  PRO A CG  1 
ATOM   291  C CD  . PRO A  1 36  ? 16.025 39.489  100.118 1.00 40.20  ? 51  PRO A CD  1 
ATOM   292  N N   . GLN A  1 37  ? 13.557 36.667  98.705  1.00 37.75  ? 52  GLN A N   1 
ATOM   293  C CA  . GLN A  1 37  ? 12.475 35.882  98.050  1.00 35.96  ? 52  GLN A CA  1 
ATOM   294  C C   . GLN A  1 37  ? 12.903 35.376  96.662  1.00 33.93  ? 52  GLN A C   1 
ATOM   295  O O   . GLN A  1 37  ? 12.035 34.836  95.950  1.00 34.82  ? 52  GLN A O   1 
ATOM   296  C CB  . GLN A  1 37  ? 11.206 36.732  97.997  1.00 35.95  ? 52  GLN A CB  1 
ATOM   297  C CG  . GLN A  1 37  ? 9.926  35.906  97.907  1.00 37.39  ? 52  GLN A CG  1 
ATOM   298  C CD  . GLN A  1 37  ? 8.697  36.636  98.392  1.00 36.99  ? 52  GLN A CD  1 
ATOM   299  O OE1 . GLN A  1 37  ? 8.757  37.788  98.814  1.00 38.64  ? 52  GLN A OE1 1 
ATOM   300  N NE2 . GLN A  1 37  ? 7.558  35.969  98.317  1.00 37.05  ? 52  GLN A NE2 1 
ATOM   301  N N   . TRP A  1 38  ? 14.182 35.486  96.285  1.00 34.58  ? 53  TRP A N   1 
ATOM   302  C CA  . TRP A  1 38  ? 14.637 35.099  94.922  1.00 35.02  ? 53  TRP A CA  1 
ATOM   303  C C   . TRP A  1 38  ? 15.932 34.284  94.974  1.00 33.09  ? 53  TRP A C   1 
ATOM   304  O O   . TRP A  1 38  ? 16.926 34.741  95.598  1.00 32.26  ? 53  TRP A O   1 
ATOM   305  C CB  . TRP A  1 38  ? 14.784 36.320  94.009  1.00 35.05  ? 53  TRP A CB  1 
ATOM   306  C CG  . TRP A  1 38  ? 13.490 37.003  93.701  1.00 35.29  ? 53  TRP A CG  1 
ATOM   307  C CD1 . TRP A  1 38  ? 12.899 37.995  94.423  1.00 36.78  ? 53  TRP A CD1 1 
ATOM   308  C CD2 . TRP A  1 38  ? 12.610 36.740  92.593  1.00 36.05  ? 53  TRP A CD2 1 
ATOM   309  N NE1 . TRP A  1 38  ? 11.724 38.378  93.834  1.00 37.61  ? 53  TRP A NE1 1 
ATOM   310  C CE2 . TRP A  1 38  ? 11.519 37.631  92.709  1.00 36.57  ? 53  TRP A CE2 1 
ATOM   311  C CE3 . TRP A  1 38  ? 12.644 35.861  91.506  1.00 36.43  ? 53  TRP A CE3 1 
ATOM   312  C CZ2 . TRP A  1 38  ? 10.468 37.652  91.790  1.00 37.99  ? 53  TRP A CZ2 1 
ATOM   313  C CZ3 . TRP A  1 38  ? 11.611 35.885  90.593  1.00 36.34  ? 53  TRP A CZ3 1 
ATOM   314  C CH2 . TRP A  1 38  ? 10.544 36.776  90.728  1.00 37.07  ? 53  TRP A CH2 1 
ATOM   315  N N   . VAL A  1 39  ? 15.914 33.149  94.270  1.00 35.18  ? 54  VAL A N   1 
ATOM   316  C CA  . VAL A  1 39  ? 17.088 32.269  94.003  1.00 33.73  ? 54  VAL A CA  1 
ATOM   317  C C   . VAL A  1 39  ? 17.483 32.412  92.525  1.00 34.68  ? 54  VAL A C   1 
ATOM   318  O O   . VAL A  1 39  ? 16.597 32.295  91.651  1.00 33.93  ? 54  VAL A O   1 
ATOM   319  C CB  . VAL A  1 39  ? 16.776 30.805  94.372  1.00 33.60  ? 54  VAL A CB  1 
ATOM   320  C CG1 . VAL A  1 39  ? 17.862 29.835  93.920  1.00 33.22  ? 54  VAL A CG1 1 
ATOM   321  C CG2 . VAL A  1 39  ? 16.506 30.653  95.858  1.00 33.39  ? 54  VAL A CG2 1 
ATOM   322  N N   . LEU A  1 40  ? 18.771 32.647  92.272  1.00 33.27  ? 55  LEU A N   1 
ATOM   323  C CA  . LEU A  1 40  ? 19.383 32.638  90.926  1.00 33.34  ? 55  LEU A CA  1 
ATOM   324  C C   . LEU A  1 40  ? 19.953 31.239  90.666  1.00 34.50  ? 55  LEU A C   1 
ATOM   325  O O   . LEU A  1 40  ? 20.692 30.725  91.542  1.00 34.92  ? 55  LEU A O   1 
ATOM   326  C CB  . LEU A  1 40  ? 20.478 33.709  90.877  1.00 33.10  ? 55  LEU A CB  1 
ATOM   327  C CG  . LEU A  1 40  ? 21.143 33.902  89.519  1.00 32.60  ? 55  LEU A CG  1 
ATOM   328  C CD1 . LEU A  1 40  ? 20.154 34.464  88.510  1.00 34.19  ? 55  LEU A CD1 1 
ATOM   329  C CD2 . LEU A  1 40  ? 22.351 34.805  89.646  1.00 33.40  ? 55  LEU A CD2 1 
ATOM   330  N N   . THR A  1 41  ? 19.642 30.660  89.502  1.00 35.53  ? 56  THR A N   1 
ATOM   331  C CA  . THR A  1 41  ? 20.089 29.304  89.086  1.00 34.79  ? 56  THR A CA  1 
ATOM   332  C C   . THR A  1 41  ? 20.332 29.273  87.567  1.00 33.40  ? 56  THR A C   1 
ATOM   333  O O   . THR A  1 41  ? 20.219 30.320  86.903  1.00 30.01  ? 56  THR A O   1 
ATOM   334  C CB  . THR A  1 41  ? 19.088 28.251  89.590  1.00 34.07  ? 56  THR A CB  1 
ATOM   335  O OG1 . THR A  1 41  ? 19.717 26.976  89.498  1.00 33.95  ? 56  THR A OG1 1 
ATOM   336  C CG2 . THR A  1 41  ? 17.777 28.223  88.834  1.00 33.53  ? 56  THR A CG2 1 
ATOM   337  N N   . ALA A  1 42  ? 20.672 28.096  87.046  1.00 33.15  ? 57  ALA A N   1 
ATOM   338  C CA  . ALA A  1 42  ? 20.854 27.824  85.605  1.00 31.76  ? 57  ALA A CA  1 
ATOM   339  C C   . ALA A  1 42  ? 19.497 27.398  85.049  1.00 29.98  ? 57  ALA A C   1 
ATOM   340  O O   . ALA A  1 42  ? 18.812 26.615  85.720  1.00 31.11  ? 57  ALA A O   1 
ATOM   341  C CB  . ALA A  1 42  ? 21.910 26.768  85.393  1.00 32.14  ? 57  ALA A CB  1 
ATOM   342  N N   . ALA A  1 43  ? 19.119 27.927  83.887  1.00 28.76  ? 58  ALA A N   1 
ATOM   343  C CA  . ALA A  1 43  ? 17.910 27.544  83.114  1.00 30.28  ? 58  ALA A CA  1 
ATOM   344  C C   . ALA A  1 43  ? 17.866 26.033  82.844  1.00 29.53  ? 58  ALA A C   1 
ATOM   345  O O   . ALA A  1 43  ? 16.753 25.464  82.916  1.00 29.50  ? 58  ALA A O   1 
ATOM   346  C CB  . ALA A  1 43  ? 17.850 28.318  81.816  1.00 31.49  ? 58  ALA A CB  1 
ATOM   347  N N   . HIS A  1 44  ? 19.003 25.398  82.530  1.00 29.60  ? 59  HIS A N   1 
ATOM   348  C CA  . HIS A  1 44  ? 19.062 23.958  82.142  1.00 30.85  ? 59  HIS A CA  1 
ATOM   349  C C   . HIS A  1 44  ? 18.650 23.060  83.323  1.00 31.47  ? 59  HIS A C   1 
ATOM   350  O O   . HIS A  1 44  ? 18.245 21.919  83.071  1.00 34.49  ? 59  HIS A O   1 
ATOM   351  C CB  . HIS A  1 44  ? 20.425 23.589  81.523  1.00 30.72  ? 59  HIS A CB  1 
ATOM   352  C CG  . HIS A  1 44  ? 21.485 23.232  82.504  1.00 32.74  ? 59  HIS A CG  1 
ATOM   353  N ND1 . HIS A  1 44  ? 22.449 24.137  82.899  1.00 32.88  ? 59  HIS A ND1 1 
ATOM   354  C CD2 . HIS A  1 44  ? 21.730 22.086  83.179  1.00 32.22  ? 59  HIS A CD2 1 
ATOM   355  C CE1 . HIS A  1 44  ? 23.241 23.562  83.776  1.00 32.44  ? 59  HIS A CE1 1 
ATOM   356  N NE2 . HIS A  1 44  ? 22.827 22.304  83.960  1.00 30.09  ? 59  HIS A NE2 1 
ATOM   357  N N   . CYS A  1 45  ? 18.734 23.553  84.560  1.00 33.85  ? 60  CYS A N   1 
ATOM   358  C CA  . CYS A  1 45  ? 18.279 22.844  85.788  1.00 34.08  ? 60  CYS A CA  1 
ATOM   359  C C   . CYS A  1 45  ? 16.753 22.691  85.805  1.00 33.30  ? 60  CYS A C   1 
ATOM   360  O O   . CYS A  1 45  ? 16.271 21.708  86.404  1.00 32.48  ? 60  CYS A O   1 
ATOM   361  C CB  . CYS A  1 45  ? 18.739 23.576  87.043  1.00 34.67  ? 60  CYS A CB  1 
ATOM   362  S SG  . CYS A  1 45  ? 20.535 23.544  87.256  1.00 38.83  ? 60  CYS A SG  1 
ATOM   363  N N   . VAL A  1 46  ? 16.018 23.645  85.224  1.00 34.38  ? 61  VAL A N   1 
ATOM   364  C CA  . VAL A  1 46  ? 14.528 23.741  85.341  1.00 36.82  ? 61  VAL A CA  1 
ATOM   365  C C   . VAL A  1 46  ? 13.861 23.887  83.963  1.00 38.05  ? 61  VAL A C   1 
ATOM   366  O O   . VAL A  1 46  ? 12.642 24.099  83.943  1.00 43.69  ? 61  VAL A O   1 
ATOM   367  C CB  . VAL A  1 46  ? 14.131 24.890  86.293  1.00 36.13  ? 61  VAL A CB  1 
ATOM   368  C CG1 . VAL A  1 46  ? 14.551 24.595  87.720  1.00 37.89  ? 61  VAL A CG1 1 
ATOM   369  C CG2 . VAL A  1 46  ? 14.676 26.242  85.850  1.00 37.15  ? 61  VAL A CG2 1 
ATOM   370  N N   . GLY A  1 47  ? 14.606 23.757  82.857  1.00 36.24  ? 62  GLY A N   1 
ATOM   371  C CA  . GLY A  1 47  ? 14.084 23.942  81.489  1.00 35.04  ? 62  GLY A CA  1 
ATOM   372  C C   . GLY A  1 47  ? 14.952 23.242  80.443  1.00 34.90  ? 62  GLY A C   1 
ATOM   373  O O   . GLY A  1 47  ? 15.879 22.529  80.804  1.00 33.57  ? 62  GLY A O   1 
ATOM   374  N N   . PRO A  1 48  ? 14.703 23.422  79.122  1.00 34.20  ? 63  PRO A N   1 
ATOM   375  C CA  . PRO A  1 48  ? 13.709 24.375  78.619  1.00 34.63  ? 63  PRO A CA  1 
ATOM   376  C C   . PRO A  1 48  ? 12.239 23.946  78.734  1.00 34.52  ? 63  PRO A C   1 
ATOM   377  O O   . PRO A  1 48  ? 11.407 24.796  78.566  1.00 35.17  ? 63  PRO A O   1 
ATOM   378  C CB  . PRO A  1 48  ? 14.076 24.490  77.127  1.00 35.04  ? 63  PRO A CB  1 
ATOM   379  C CG  . PRO A  1 48  ? 14.618 23.112  76.789  1.00 35.03  ? 63  PRO A CG  1 
ATOM   380  C CD  . PRO A  1 48  ? 15.386 22.702  78.032  1.00 34.38  ? 63  PRO A CD  1 
ATOM   381  N N   . ASP A  1 49  ? 11.951 22.663  78.989  1.00 35.80  ? 64  ASP A N   1 
ATOM   382  C CA  . ASP A  1 49  ? 10.557 22.147  79.099  1.00 38.57  ? 64  ASP A CA  1 
ATOM   383  C C   . ASP A  1 49  ? 9.964  22.552  80.451  1.00 36.42  ? 64  ASP A C   1 
ATOM   384  O O   . ASP A  1 49  ? 10.691 22.491  81.461  1.00 37.09  ? 64  ASP A O   1 
ATOM   385  C CB  . ASP A  1 49  ? 10.464 20.631  78.931  1.00 39.58  ? 64  ASP A CB  1 
ATOM   386  C CG  . ASP A  1 49  ? 10.955 20.147  77.580  1.00 44.28  ? 64  ASP A CG  1 
ATOM   387  O OD1 . ASP A  1 49  ? 10.624 20.793  76.562  1.00 43.54  ? 64  ASP A OD1 1 
ATOM   388  O OD2 . ASP A  1 49  ? 11.707 19.160  77.567  1.00 51.23  ? 64  ASP A OD2 1 
ATOM   389  N N   . VAL A  1 50  ? 8.691  22.944  80.449  1.00 37.74  ? 65  VAL A N   1 
ATOM   390  C CA  . VAL A  1 50  ? 7.961  23.471  81.640  1.00 39.83  ? 65  VAL A CA  1 
ATOM   391  C C   . VAL A  1 50  ? 7.806  22.333  82.657  1.00 41.86  ? 65  VAL A C   1 
ATOM   392  O O   . VAL A  1 50  ? 7.353  21.253  82.258  1.00 44.65  ? 65  VAL A O   1 
ATOM   393  C CB  . VAL A  1 50  ? 6.611  24.088  81.228  1.00 41.75  ? 65  VAL A CB  1 
ATOM   394  C CG1 . VAL A  1 50  ? 5.751  24.466  82.428  1.00 43.67  ? 65  VAL A CG1 1 
ATOM   395  C CG2 . VAL A  1 50  ? 6.806  25.295  80.314  1.00 39.19  ? 65  VAL A CG2 1 
ATOM   396  N N   . LYS A  1 51  ? 8.176  22.584  83.918  1.00 43.21  ? 66  LYS A N   1 
ATOM   397  C CA  . LYS A  1 51  ? 8.174  21.608  85.044  1.00 47.21  ? 66  LYS A CA  1 
ATOM   398  C C   . LYS A  1 51  ? 7.010  21.944  85.996  1.00 45.98  ? 66  LYS A C   1 
ATOM   399  O O   . LYS A  1 51  ? 6.573  23.109  86.028  1.00 43.51  ? 66  LYS A O   1 
ATOM   400  C CB  . LYS A  1 51  ? 9.502  21.631  85.828  1.00 51.88  ? 66  LYS A CB  1 
ATOM   401  C CG  . LYS A  1 51  ? 10.800 21.692  85.034  1.00 52.62  ? 66  LYS A CG  1 
ATOM   402  C CD  . LYS A  1 51  ? 11.139 20.433  84.282  1.00 54.57  ? 66  LYS A CD  1 
ATOM   403  C CE  . LYS A  1 51  ? 12.483 20.535  83.590  1.00 56.40  ? 66  LYS A CE  1 
ATOM   404  N NZ  . LYS A  1 51  ? 12.550 19.659  82.399  1.00 59.58  ? 66  LYS A NZ  1 
ATOM   405  N N   . ASP A  1 52  ? 6.531  20.948  86.744  1.00 47.03  ? 67  ASP A N   1 
ATOM   406  C CA  . ASP A  1 52  ? 5.495  21.093  87.797  1.00 46.43  ? 67  ASP A CA  1 
ATOM   407  C C   . ASP A  1 52  ? 6.140  21.759  89.021  1.00 45.35  ? 67  ASP A C   1 
ATOM   408  O O   . ASP A  1 52  ? 7.112  21.178  89.550  1.00 47.03  ? 67  ASP A O   1 
ATOM   409  C CB  . ASP A  1 52  ? 4.902  19.720  88.116  1.00 47.87  ? 67  ASP A CB  1 
ATOM   410  C CG  . ASP A  1 52  ? 3.820  19.712  89.178  1.00 50.03  ? 67  ASP A CG  1 
ATOM   411  O OD1 . ASP A  1 52  ? 3.186  20.764  89.407  1.00 51.88  ? 67  ASP A OD1 1 
ATOM   412  O OD2 . ASP A  1 52  ? 3.611  18.635  89.760  1.00 56.61  ? 67  ASP A OD2 1 
ATOM   413  N N   . LEU A  1 53  ? 5.626  22.912  89.469  1.00 44.07  ? 68  LEU A N   1 
ATOM   414  C CA  . LEU A  1 53  ? 6.136  23.644  90.672  1.00 45.90  ? 68  LEU A CA  1 
ATOM   415  C C   . LEU A  1 53  ? 6.005  22.789  91.938  1.00 41.89  ? 68  LEU A C   1 
ATOM   416  O O   . LEU A  1 53  ? 6.879  22.918  92.829  1.00 40.08  ? 68  LEU A O   1 
ATOM   417  C CB  . LEU A  1 53  ? 5.386  24.965  90.858  1.00 47.73  ? 68  LEU A CB  1 
ATOM   418  C CG  . LEU A  1 53  ? 5.832  26.100  89.942  1.00 51.78  ? 68  LEU A CG  1 
ATOM   419  C CD1 . LEU A  1 53  ? 4.788  27.200  89.924  1.00 55.15  ? 68  LEU A CD1 1 
ATOM   420  C CD2 . LEU A  1 53  ? 7.178  26.673  90.366  1.00 54.77  ? 68  LEU A CD2 1 
ATOM   421  N N   . ALA A  1 54  ? 4.962  21.958  92.021  1.00 41.07  ? 69  ALA A N   1 
ATOM   422  C CA  . ALA A  1 54  ? 4.670  21.076  93.181  1.00 41.51  ? 69  ALA A CA  1 
ATOM   423  C C   . ALA A  1 54  ? 5.809  20.068  93.407  1.00 41.04  ? 69  ALA A C   1 
ATOM   424  O O   . ALA A  1 54  ? 5.979  19.629  94.558  1.00 43.47  ? 69  ALA A O   1 
ATOM   425  C CB  . ALA A  1 54  ? 3.350  20.368  92.988  1.00 40.24  ? 69  ALA A CB  1 
ATOM   426  N N   . ALA A  1 55  ? 6.559  19.720  92.358  1.00 39.73  ? 70  ALA A N   1 
ATOM   427  C CA  . ALA A  1 55  ? 7.658  18.728  92.392  1.00 38.94  ? 70  ALA A CA  1 
ATOM   428  C C   . ALA A  1 55  ? 9.010  19.401  92.667  1.00 36.46  ? 70  ALA A C   1 
ATOM   429  O O   . ALA A  1 55  ? 10.013 18.674  92.644  1.00 38.68  ? 70  ALA A O   1 
ATOM   430  C CB  . ALA A  1 55  ? 7.674  17.962  91.090  1.00 38.42  ? 70  ALA A CB  1 
ATOM   431  N N   . LEU A  1 56  ? 9.050  20.713  92.934  1.00 37.25  ? 71  LEU A N   1 
ATOM   432  C CA  . LEU A  1 56  ? 10.312 21.468  93.178  1.00 37.17  ? 71  LEU A CA  1 
ATOM   433  C C   . LEU A  1 56  ? 10.294 22.067  94.588  1.00 39.53  ? 71  LEU A C   1 
ATOM   434  O O   . LEU A  1 56  ? 9.259  22.642  94.966  1.00 41.57  ? 71  LEU A O   1 
ATOM   435  C CB  . LEU A  1 56  ? 10.459 22.565  92.119  1.00 36.74  ? 71  LEU A CB  1 
ATOM   436  C CG  . LEU A  1 56  ? 11.708 23.443  92.238  1.00 37.44  ? 71  LEU A CG  1 
ATOM   437  C CD1 . LEU A  1 56  ? 12.968 22.633  92.010  1.00 38.44  ? 71  LEU A CD1 1 
ATOM   438  C CD2 . LEU A  1 56  ? 11.653 24.612  91.268  1.00 39.33  ? 71  LEU A CD2 1 
ATOM   439  N N   . ARG A  1 57  ? 11.410 21.960  95.318  1.00 38.87  ? 72  ARG A N   1 
ATOM   440  C CA  . ARG A  1 57  ? 11.630 22.684  96.598  1.00 38.01  ? 72  ARG A CA  1 
ATOM   441  C C   . ARG A  1 57  ? 13.041 23.274  96.619  1.00 34.37  ? 72  ARG A C   1 
ATOM   442  O O   . ARG A  1 57  ? 13.933 22.747  95.917  1.00 32.98  ? 72  ARG A O   1 
ATOM   443  C CB  . ARG A  1 57  ? 11.434 21.756  97.801  1.00 40.99  ? 72  ARG A CB  1 
ATOM   444  C CG  . ARG A  1 57  ? 10.026 21.203  97.956  1.00 41.69  ? 72  ARG A CG  1 
ATOM   445  C CD  . ARG A  1 57  ? 9.066  22.154  98.621  1.00 42.06  ? 72  ARG A CD  1 
ATOM   446  N NE  . ARG A  1 57  ? 7.877  21.406  98.997  1.00 43.94  ? 72  ARG A NE  1 
ATOM   447  C CZ  . ARG A  1 57  ? 6.870  21.077  98.186  1.00 46.48  ? 72  ARG A CZ  1 
ATOM   448  N NH1 . ARG A  1 57  ? 6.866  21.438  96.912  1.00 49.46  ? 72  ARG A NH1 1 
ATOM   449  N NH2 . ARG A  1 57  ? 5.854  20.372  98.662  1.00 46.99  ? 72  ARG A NH2 1 
ATOM   450  N N   . VAL A  1 58  ? 13.225 24.328  97.419  1.00 35.02  ? 73  VAL A N   1 
ATOM   451  C CA  . VAL A  1 58  ? 14.544 24.954  97.720  1.00 34.51  ? 73  VAL A CA  1 
ATOM   452  C C   . VAL A  1 58  ? 14.924 24.595  99.160  1.00 34.99  ? 73  VAL A C   1 
ATOM   453  O O   . VAL A  1 58  ? 14.053 24.654  100.053 1.00 35.02  ? 73  VAL A O   1 
ATOM   454  C CB  . VAL A  1 58  ? 14.521 26.477  97.487  1.00 35.93  ? 73  VAL A CB  1 
ATOM   455  C CG1 . VAL A  1 58  ? 15.785 27.166  97.977  1.00 36.00  ? 73  VAL A CG1 1 
ATOM   456  C CG2 . VAL A  1 58  ? 14.283 26.803  96.025  1.00 36.76  ? 73  VAL A CG2 1 
ATOM   457  N N   . GLN A  1 59  ? 16.193 24.242  99.356  1.00 34.31  ? 74  GLN A N   1 
ATOM   458  C CA  . GLN A  1 59  ? 16.830 24.056  100.677 1.00 34.94  ? 74  GLN A CA  1 
ATOM   459  C C   . GLN A  1 59  ? 17.926 25.113  100.808 1.00 34.70  ? 74  GLN A C   1 
ATOM   460  O O   . GLN A  1 59  ? 18.821 25.123  99.953  1.00 34.98  ? 74  GLN A O   1 
ATOM   461  C CB  . GLN A  1 59  ? 17.386 22.633  100.783 1.00 35.46  ? 74  GLN A CB  1 
ATOM   462  C CG  . GLN A  1 59  ? 18.210 22.372  102.037 1.00 37.07  ? 74  GLN A CG  1 
ATOM   463  C CD  . GLN A  1 59  ? 17.422 22.626  103.298 1.00 37.00  ? 74  GLN A CD  1 
ATOM   464  O OE1 . GLN A  1 59  ? 16.300 22.153  103.445 1.00 37.22  ? 74  GLN A OE1 1 
ATOM   465  N NE2 . GLN A  1 59  ? 17.991 23.398  104.212 1.00 37.85  ? 74  GLN A NE2 1 
ATOM   466  N N   . LEU A  1 60  ? 17.856 25.949  101.844 1.00 34.34  ? 75  LEU A N   1 
ATOM   467  C CA  . LEU A  1 60  ? 18.874 26.987  102.144 1.00 36.71  ? 75  LEU A CA  1 
ATOM   468  C C   . LEU A  1 60  ? 20.136 26.307  102.671 1.00 37.81  ? 75  LEU A C   1 
ATOM   469  O O   . LEU A  1 60  ? 20.105 25.073  102.900 1.00 39.53  ? 75  LEU A O   1 
ATOM   470  C CB  . LEU A  1 60  ? 18.304 27.986  103.156 1.00 38.59  ? 75  LEU A CB  1 
ATOM   471  C CG  . LEU A  1 60  ? 17.063 28.750  102.694 1.00 40.17  ? 75  LEU A CG  1 
ATOM   472  C CD1 . LEU A  1 60  ? 16.511 29.614  103.821 1.00 39.42  ? 75  LEU A CD1 1 
ATOM   473  C CD2 . LEU A  1 60  ? 17.359 29.590  101.455 1.00 40.07  ? 75  LEU A CD2 1 
ATOM   474  N N   . ARG A  1 61  ? 21.203 27.082  102.851 1.00 38.62  ? 76  ARG A N   1 
ATOM   475  C CA  . ARG A  1 61  ? 22.546 26.530  103.139 1.00 40.42  ? 76  ARG A CA  1 
ATOM   476  C C   . ARG A  1 61  ? 22.450 25.515  104.282 1.00 41.51  ? 76  ARG A C   1 
ATOM   477  O O   . ARG A  1 61  ? 21.897 25.861  105.340 1.00 41.90  ? 76  ARG A O   1 
ATOM   478  C CB  . ARG A  1 61  ? 23.541 27.621  103.516 1.00 40.21  ? 76  ARG A CB  1 
ATOM   479  C CG  . ARG A  1 61  ? 24.979 27.139  103.422 1.00 40.86  ? 76  ARG A CG  1 
ATOM   480  C CD  . ARG A  1 61  ? 25.830 27.814  104.463 1.00 40.31  ? 76  ARG A CD  1 
ATOM   481  N NE  . ARG A  1 61  ? 27.242 27.509  104.337 1.00 40.04  ? 76  ARG A NE  1 
ATOM   482  C CZ  . ARG A  1 61  ? 27.841 26.400  104.772 1.00 40.47  ? 76  ARG A CZ  1 
ATOM   483  N NH1 . ARG A  1 61  ? 27.140 25.429  105.335 1.00 41.84  ? 76  ARG A NH1 1 
ATOM   484  N NH2 . ARG A  1 61  ? 29.157 26.273  104.638 1.00 38.69  ? 76  ARG A NH2 1 
ATOM   485  N N   . GLU A  1 62  ? 22.912 24.290  104.042 1.00 42.11  ? 77  GLU A N   1 
ATOM   486  C CA  . GLU A  1 62  ? 23.138 23.271  105.099 1.00 43.56  ? 77  GLU A CA  1 
ATOM   487  C C   . GLU A  1 62  ? 24.530 22.684  104.862 1.00 42.69  ? 77  GLU A C   1 
ATOM   488  O O   . GLU A  1 62  ? 24.949 22.590  103.692 1.00 45.21  ? 77  GLU A O   1 
ATOM   489  C CB  . GLU A  1 62  ? 21.997 22.246  105.164 1.00 43.13  ? 77  GLU A CB  1 
ATOM   490  C CG  . GLU A  1 62  ? 21.536 21.707  103.831 1.00 42.50  ? 77  GLU A CG  1 
ATOM   491  C CD  . GLU A  1 62  ? 20.493 20.602  103.904 1.00 42.54  ? 77  GLU A CD  1 
ATOM   492  O OE1 . GLU A  1 62  ? 19.772 20.506  104.913 1.00 46.89  ? 77  GLU A OE1 1 
ATOM   493  O OE2 . GLU A  1 62  ? 20.395 19.845  102.938 1.00 42.28  ? 77  GLU A OE2 1 
ATOM   494  N N   . GLN A  1 63  ? 25.236 22.355  105.943 1.00 39.34  ? 78  GLN A N   1 
ATOM   495  C CA  . GLN A  1 63  ? 26.631 21.843  105.895 1.00 40.23  ? 78  GLN A CA  1 
ATOM   496  C C   . GLN A  1 63  ? 26.634 20.446  105.255 1.00 39.09  ? 78  GLN A C   1 
ATOM   497  O O   . GLN A  1 63  ? 27.562 20.158  104.493 1.00 38.79  ? 78  GLN A O   1 
ATOM   498  C CB  . GLN A  1 63  ? 27.252 21.833  107.298 1.00 39.76  ? 78  GLN A CB  1 
ATOM   499  C CG  . GLN A  1 63  ? 28.761 21.637  107.316 1.00 40.19  ? 78  GLN A CG  1 
ATOM   500  C CD  . GLN A  1 63  ? 29.522 22.737  106.619 1.00 43.93  ? 78  GLN A CD  1 
ATOM   501  O OE1 . GLN A  1 63  ? 29.024 23.844  106.422 1.00 40.44  ? 78  GLN A OE1 1 
ATOM   502  N NE2 . GLN A  1 63  ? 30.736 22.424  106.203 1.00 46.25  ? 78  GLN A NE2 1 
ATOM   503  N N   . HIS A  1 64  ? 25.609 19.637  105.533 1.00 38.02  ? 79  HIS A N   1 
ATOM   504  C CA  . HIS A  1 64  ? 25.454 18.240  105.049 1.00 37.41  ? 79  HIS A CA  1 
ATOM   505  C C   . HIS A  1 64  ? 24.063 18.078  104.446 1.00 37.28  ? 79  HIS A C   1 
ATOM   506  O O   . HIS A  1 64  ? 23.082 18.253  105.204 1.00 38.55  ? 79  HIS A O   1 
ATOM   507  C CB  . HIS A  1 64  ? 25.706 17.260  106.199 1.00 37.98  ? 79  HIS A CB  1 
ATOM   508  C CG  . HIS A  1 64  ? 27.091 17.336  106.739 1.00 37.79  ? 79  HIS A CG  1 
ATOM   509  N ND1 . HIS A  1 64  ? 27.385 17.968  107.933 1.00 39.90  ? 79  HIS A ND1 1 
ATOM   510  C CD2 . HIS A  1 64  ? 28.266 16.901  106.235 1.00 37.01  ? 79  HIS A CD2 1 
ATOM   511  C CE1 . HIS A  1 64  ? 28.682 17.901  108.152 1.00 39.06  ? 79  HIS A CE1 1 
ATOM   512  N NE2 . HIS A  1 64  ? 29.243 17.242  107.126 1.00 37.91  ? 79  HIS A NE2 1 
ATOM   513  N N   . LEU A  1 65  ? 23.981 17.766  103.147 1.00 37.06  ? 80  LEU A N   1 
ATOM   514  C CA  . LEU A  1 65  ? 22.682 17.568  102.444 1.00 36.51  ? 80  LEU A CA  1 
ATOM   515  C C   . LEU A  1 65  ? 21.839 16.545  103.201 1.00 35.18  ? 80  LEU A C   1 
ATOM   516  O O   . LEU A  1 65  ? 22.402 15.516  103.597 1.00 32.23  ? 80  LEU A O   1 
ATOM   517  C CB  . LEU A  1 65  ? 22.864 17.076  101.003 1.00 37.90  ? 80  LEU A CB  1 
ATOM   518  C CG  . LEU A  1 65  ? 23.051 18.120  99.906  1.00 39.30  ? 80  LEU A CG  1 
ATOM   519  C CD1 . LEU A  1 65  ? 23.165 17.423  98.562  1.00 40.34  ? 80  LEU A CD1 1 
ATOM   520  C CD2 . LEU A  1 65  ? 21.934 19.154  99.873  1.00 38.83  ? 80  LEU A CD2 1 
ATOM   521  N N   . TYR A  1 66  ? 20.541 16.836  103.347 1.00 35.04  ? 81  TYR A N   1 
ATOM   522  C CA  . TYR A  1 66  ? 19.447 15.904  103.726 1.00 37.54  ? 81  TYR A CA  1 
ATOM   523  C C   . TYR A  1 66  ? 19.289 15.776  105.247 1.00 38.20  ? 81  TYR A C   1 
ATOM   524  O O   . TYR A  1 66  ? 18.197 15.337  105.645 1.00 40.75  ? 81  TYR A O   1 
ATOM   525  C CB  . TYR A  1 66  ? 19.631 14.514  103.105 1.00 34.96  ? 81  TYR A CB  1 
ATOM   526  C CG  . TYR A  1 66  ? 19.797 14.513  101.605 1.00 34.92  ? 81  TYR A CG  1 
ATOM   527  C CD1 . TYR A  1 66  ? 18.800 15.013  100.779 1.00 32.74  ? 81  TYR A CD1 1 
ATOM   528  C CD2 . TYR A  1 66  ? 20.948 14.022  101.009 1.00 32.52  ? 81  TYR A CD2 1 
ATOM   529  C CE1 . TYR A  1 66  ? 18.945 15.033  99.403  1.00 33.55  ? 81  TYR A CE1 1 
ATOM   530  C CE2 . TYR A  1 66  ? 21.107 14.030  99.632  1.00 33.48  ? 81  TYR A CE2 1 
ATOM   531  C CZ  . TYR A  1 66  ? 20.100 14.536  98.827  1.00 32.86  ? 81  TYR A CZ  1 
ATOM   532  O OH  . TYR A  1 66  ? 20.234 14.547  97.475  1.00 30.73  ? 81  TYR A OH  1 
ATOM   533  N N   . TYR A  1 67  ? 20.279 16.155  106.067 1.00 41.31  ? 82  TYR A N   1 
ATOM   534  C CA  A TYR A  1 67  ? 20.289 15.801  107.512 0.50 42.85  ? 82  TYR A CA  1 
ATOM   535  C CA  B TYR A  1 67  ? 20.315 15.815  107.518 0.50 44.98  ? 82  TYR A CA  1 
ATOM   536  C C   . TYR A  1 67  ? 19.336 16.705  108.302 1.00 44.76  ? 82  TYR A C   1 
ATOM   537  O O   . TYR A  1 67  ? 18.658 16.170  109.198 1.00 47.60  ? 82  TYR A O   1 
ATOM   538  C CB  A TYR A  1 67  ? 21.721 15.754  108.047 0.50 42.36  ? 82  TYR A CB  1 
ATOM   539  C CB  B TYR A  1 67  ? 21.745 15.874  108.080 0.50 47.25  ? 82  TYR A CB  1 
ATOM   540  C CG  A TYR A  1 67  ? 22.452 14.517  107.585 0.50 40.20  ? 82  TYR A CG  1 
ATOM   541  C CG  B TYR A  1 67  ? 21.826 15.807  109.587 0.50 48.81  ? 82  TYR A CG  1 
ATOM   542  C CD1 A TYR A  1 67  ? 22.345 13.315  108.266 0.50 39.51  ? 82  TYR A CD1 1 
ATOM   543  C CD1 B TYR A  1 67  ? 21.228 14.773  110.291 0.50 48.99  ? 82  TYR A CD1 1 
ATOM   544  C CD2 A TYR A  1 67  ? 23.201 14.531  106.423 0.50 39.35  ? 82  TYR A CD2 1 
ATOM   545  C CD2 B TYR A  1 67  ? 22.467 16.795  110.314 0.50 49.27  ? 82  TYR A CD2 1 
ATOM   546  C CE1 A TYR A  1 67  ? 22.993 12.171  107.824 0.50 38.39  ? 82  TYR A CE1 1 
ATOM   547  C CE1 B TYR A  1 67  ? 21.271 14.718  111.673 0.50 47.87  ? 82  TYR A CE1 1 
ATOM   548  C CE2 A TYR A  1 67  ? 23.853 13.399  105.965 0.50 38.51  ? 82  TYR A CE2 1 
ATOM   549  C CE2 B TYR A  1 67  ? 22.521 16.755  111.698 0.50 49.77  ? 82  TYR A CE2 1 
ATOM   550  C CZ  A TYR A  1 67  ? 23.748 12.212  106.666 0.50 38.74  ? 82  TYR A CZ  1 
ATOM   551  C CZ  B TYR A  1 67  ? 21.922 15.712  112.379 0.50 48.65  ? 82  TYR A CZ  1 
ATOM   552  O OH  A TYR A  1 67  ? 24.395 11.098  106.212 0.50 36.32  ? 82  TYR A OH  1 
ATOM   553  O OH  B TYR A  1 67  ? 21.970 15.665  113.740 0.50 50.99  ? 82  TYR A OH  1 
ATOM   554  N N   . GLN A  1 68  ? 19.270 17.999  107.984 1.00 45.63  ? 83  GLN A N   1 
ATOM   555  C CA  . GLN A  1 68  ? 18.364 18.946  108.699 1.00 50.13  ? 83  GLN A CA  1 
ATOM   556  C C   . GLN A  1 68  ? 17.593 19.771  107.670 1.00 48.15  ? 83  GLN A C   1 
ATOM   557  O O   . GLN A  1 68  ? 17.687 21.008  107.698 1.00 48.80  ? 83  GLN A O   1 
ATOM   558  C CB  . GLN A  1 68  ? 19.142 19.817  109.692 1.00 53.68  ? 83  GLN A CB  1 
ATOM   559  C CG  . GLN A  1 68  ? 19.755 19.005  110.828 1.00 57.97  ? 83  GLN A CG  1 
ATOM   560  C CD  . GLN A  1 68  ? 20.009 19.811  112.076 1.00 60.07  ? 83  GLN A CD  1 
ATOM   561  O OE1 . GLN A  1 68  ? 21.129 20.250  112.326 1.00 62.82  ? 83  GLN A OE1 1 
ATOM   562  N NE2 . GLN A  1 68  ? 18.966 20.013  112.867 1.00 59.43  ? 83  GLN A NE2 1 
ATOM   563  N N   . ASP A  1 69  ? 16.823 19.091  106.821 1.00 44.95  ? 84  ASP A N   1 
ATOM   564  C CA  . ASP A  1 69  ? 16.089 19.727  105.696 1.00 43.46  ? 84  ASP A CA  1 
ATOM   565  C C   . ASP A  1 69  ? 14.938 20.578  106.243 1.00 43.78  ? 84  ASP A C   1 
ATOM   566  O O   . ASP A  1 69  ? 14.183 20.084  107.097 1.00 43.41  ? 84  ASP A O   1 
ATOM   567  C CB  . ASP A  1 69  ? 15.562 18.700  104.686 1.00 39.98  ? 84  ASP A CB  1 
ATOM   568  C CG  . ASP A  1 69  ? 16.591 18.166  103.704 1.00 37.94  ? 84  ASP A CG  1 
ATOM   569  O OD1 . ASP A  1 69  ? 17.749 18.629  103.741 1.00 36.27  ? 84  ASP A OD1 1 
ATOM   570  O OD2 . ASP A  1 69  ? 16.217 17.291  102.895 1.00 37.02  ? 84  ASP A OD2 1 
ATOM   571  N N   . GLN A  1 70  ? 14.823 21.814  105.751 1.00 46.25  ? 85  GLN A N   1 
ATOM   572  C CA  . GLN A  1 70  ? 13.632 22.693  105.898 1.00 49.64  ? 85  GLN A CA  1 
ATOM   573  C C   . GLN A  1 70  ? 13.254 23.180  104.498 1.00 45.42  ? 85  GLN A C   1 
ATOM   574  O O   . GLN A  1 70  ? 13.735 24.243  104.082 1.00 45.30  ? 85  GLN A O   1 
ATOM   575  C CB  . GLN A  1 70  ? 13.943 23.812  106.891 1.00 51.52  ? 85  GLN A CB  1 
ATOM   576  C CG  . GLN A  1 70  ? 14.133 23.286  108.307 1.00 56.90  ? 85  GLN A CG  1 
ATOM   577  C CD  . GLN A  1 70  ? 14.684 24.315  109.264 1.00 60.65  ? 85  GLN A CD  1 
ATOM   578  O OE1 . GLN A  1 70  ? 15.618 25.049  108.944 1.00 62.64  ? 85  GLN A OE1 1 
ATOM   579  N NE2 . GLN A  1 70  ? 14.128 24.358  110.465 1.00 63.30  ? 85  GLN A NE2 1 
ATOM   580  N N   . LEU A  1 71  ? 12.475 22.377  103.778 1.00 42.37  ? 86  LEU A N   1 
ATOM   581  C CA  . LEU A  1 71  ? 12.229 22.567  102.329 1.00 40.08  ? 86  LEU A CA  1 
ATOM   582  C C   . LEU A  1 71  ? 11.233 23.711  102.122 1.00 40.50  ? 86  LEU A C   1 
ATOM   583  O O   . LEU A  1 71  ? 10.202 23.734  102.814 1.00 39.76  ? 86  LEU A O   1 
ATOM   584  C CB  . LEU A  1 71  ? 11.733 21.251  101.729 1.00 38.08  ? 86  LEU A CB  1 
ATOM   585  C CG  . LEU A  1 71  ? 12.717 20.082  101.800 1.00 39.36  ? 86  LEU A CG  1 
ATOM   586  C CD1 . LEU A  1 71  ? 12.165 18.892  101.039 1.00 39.18  ? 86  LEU A CD1 1 
ATOM   587  C CD2 . LEU A  1 71  ? 14.098 20.446  101.263 1.00 38.82  ? 86  LEU A CD2 1 
ATOM   588  N N   . LEU A  1 72  ? 11.566 24.627  101.209 1.00 38.47  ? 87  LEU A N   1 
ATOM   589  C CA  . LEU A  1 72  ? 10.781 25.850  100.908 1.00 37.35  ? 87  LEU A CA  1 
ATOM   590  C C   . LEU A  1 72  ? 10.103 25.677  99.553  1.00 38.20  ? 87  LEU A C   1 
ATOM   591  O O   . LEU A  1 72  ? 10.757 25.319  98.574  1.00 38.87  ? 87  LEU A O   1 
ATOM   592  C CB  . LEU A  1 72  ? 11.718 27.062  100.915 1.00 35.53  ? 87  LEU A CB  1 
ATOM   593  C CG  . LEU A  1 72  ? 12.533 27.271  102.192 1.00 35.34  ? 87  LEU A CG  1 
ATOM   594  C CD1 . LEU A  1 72  ? 13.434 28.480  102.050 1.00 36.19  ? 87  LEU A CD1 1 
ATOM   595  C CD2 . LEU A  1 72  ? 11.640 27.430  103.418 1.00 36.82  ? 87  LEU A CD2 1 
ATOM   596  N N   . PRO A  1 73  ? 8.774  25.912  99.452  1.00 40.13  ? 88  PRO A N   1 
ATOM   597  C CA  . PRO A  1 73  ? 8.086  25.842  98.165  1.00 39.87  ? 88  PRO A CA  1 
ATOM   598  C C   . PRO A  1 73  ? 8.422  27.059  97.287  1.00 39.57  ? 88  PRO A C   1 
ATOM   599  O O   . PRO A  1 73  ? 8.822  28.089  97.805  1.00 40.07  ? 88  PRO A O   1 
ATOM   600  C CB  . PRO A  1 73  ? 6.604  25.775  98.565  1.00 40.92  ? 88  PRO A CB  1 
ATOM   601  C CG  . PRO A  1 73  ? 6.546  26.546  99.869  1.00 40.91  ? 88  PRO A CG  1 
ATOM   602  C CD  . PRO A  1 73  ? 7.863  26.258  100.559 1.00 39.81  ? 88  PRO A CD  1 
ATOM   603  N N   . VAL A  1 74  ? 8.312  26.876  95.968  1.00 40.56  ? 89  VAL A N   1 
ATOM   604  C CA  . VAL A  1 74  ? 8.585  27.899  94.916  1.00 40.27  ? 89  VAL A CA  1 
ATOM   605  C C   . VAL A  1 74  ? 7.235  28.352  94.356  1.00 39.54  ? 89  VAL A C   1 
ATOM   606  O O   . VAL A  1 74  ? 6.416  27.471  94.035  1.00 38.46  ? 89  VAL A O   1 
ATOM   607  C CB  . VAL A  1 74  ? 9.501  27.336  93.810  1.00 40.67  ? 89  VAL A CB  1 
ATOM   608  C CG1 . VAL A  1 74  ? 9.731  28.333  92.678  1.00 42.77  ? 89  VAL A CG1 1 
ATOM   609  C CG2 . VAL A  1 74  ? 10.831 26.865  94.376  1.00 42.44  ? 89  VAL A CG2 1 
ATOM   610  N N   . SER A  1 75  ? 7.009  29.666  94.263  1.00 40.84  ? 90  SER A N   1 
ATOM   611  C CA  . SER A  1 75  ? 5.783  30.263  93.675  1.00 42.36  ? 90  SER A CA  1 
ATOM   612  C C   . SER A  1 75  ? 5.927  30.388  92.155  1.00 43.64  ? 90  SER A C   1 
ATOM   613  O O   . SER A  1 75  ? 4.915  30.214  91.480  1.00 46.59  ? 90  SER A O   1 
ATOM   614  C CB  . SER A  1 75  ? 5.450  31.585  94.300  1.00 43.94  ? 90  SER A CB  1 
ATOM   615  O OG  . SER A  1 75  ? 6.484  32.523  94.082  1.00 48.17  ? 90  SER A OG  1 
ATOM   616  N N   . ARG A  1 76  ? 7.132  30.665  91.639  1.00 42.76  ? 91  ARG A N   1 
ATOM   617  C CA  . ARG A  1 76  ? 7.349  30.929  90.193  1.00 41.65  ? 91  ARG A CA  1 
ATOM   618  C C   . ARG A  1 76  ? 8.747  30.488  89.755  1.00 38.36  ? 91  ARG A C   1 
ATOM   619  O O   . ARG A  1 76  ? 9.720  30.831  90.440  1.00 36.12  ? 91  ARG A O   1 
ATOM   620  C CB  . ARG A  1 76  ? 7.154  32.418  89.894  1.00 43.85  ? 91  ARG A CB  1 
ATOM   621  C CG  . ARG A  1 76  ? 6.958  32.722  88.418  1.00 44.69  ? 91  ARG A CG  1 
ATOM   622  C CD  . ARG A  1 76  ? 6.583  34.170  88.200  1.00 47.22  ? 91  ARG A CD  1 
ATOM   623  N NE  . ARG A  1 76  ? 6.654  34.533  86.791  1.00 50.30  ? 91  ARG A NE  1 
ATOM   624  C CZ  . ARG A  1 76  ? 6.446  35.751  86.298  1.00 49.84  ? 91  ARG A CZ  1 
ATOM   625  N NH1 . ARG A  1 76  ? 6.147  36.762  87.099  1.00 51.57  ? 91  ARG A NH1 1 
ATOM   626  N NH2 . ARG A  1 76  ? 6.541  35.950  84.994  1.00 50.49  ? 91  ARG A NH2 1 
ATOM   627  N N   . ILE A  1 77  ? 8.818  29.796  88.614  1.00 36.09  ? 92  ILE A N   1 
ATOM   628  C CA  . ILE A  1 77  ? 10.059 29.576  87.814  1.00 37.54  ? 92  ILE A CA  1 
ATOM   629  C C   . ILE A  1 77  ? 10.039 30.570  86.645  1.00 36.89  ? 92  ILE A C   1 
ATOM   630  O O   . ILE A  1 77  ? 9.088  30.521  85.850  1.00 37.60  ? 92  ILE A O   1 
ATOM   631  C CB  . ILE A  1 77  ? 10.164 28.122  87.312  1.00 36.86  ? 92  ILE A CB  1 
ATOM   632  C CG1 . ILE A  1 77  ? 10.230 27.114  88.463  1.00 37.79  ? 92  ILE A CG1 1 
ATOM   633  C CG2 . ILE A  1 77  ? 11.357 27.974  86.373  1.00 38.31  ? 92  ILE A CG2 1 
ATOM   634  C CD1 . ILE A  1 77  ? 9.894  25.692  88.065  1.00 38.06  ? 92  ILE A CD1 1 
ATOM   635  N N   . ILE A  1 78  ? 11.056 31.430  86.552  1.00 37.12  ? 93  ILE A N   1 
ATOM   636  C CA  . ILE A  1 78  ? 11.267 32.349  85.395  1.00 36.80  ? 93  ILE A CA  1 
ATOM   637  C C   . ILE A  1 78  ? 12.566 31.920  84.700  1.00 35.74  ? 93  ILE A C   1 
ATOM   638  O O   . ILE A  1 78  ? 13.644 32.151  85.262  1.00 35.82  ? 93  ILE A O   1 
ATOM   639  C CB  . ILE A  1 78  ? 11.283 33.826  85.840  1.00 37.98  ? 93  ILE A CB  1 
ATOM   640  C CG1 . ILE A  1 78  ? 10.117 34.150  86.781  1.00 39.77  ? 93  ILE A CG1 1 
ATOM   641  C CG2 . ILE A  1 78  ? 11.308 34.732  84.618  1.00 40.02  ? 93  ILE A CG2 1 
ATOM   642  C CD1 . ILE A  1 78  ? 10.084 35.579  87.269  1.00 39.81  ? 93  ILE A CD1 1 
ATOM   643  N N   . VAL A  1 79  ? 12.451 31.273  83.534  1.00 35.76  ? 94  VAL A N   1 
ATOM   644  C CA  . VAL A  1 79  ? 13.598 30.863  82.673  1.00 36.57  ? 94  VAL A CA  1 
ATOM   645  C C   . VAL A  1 79  ? 13.772 31.938  81.603  1.00 35.80  ? 94  VAL A C   1 
ATOM   646  O O   . VAL A  1 79  ? 12.756 32.398  81.061  1.00 39.12  ? 94  VAL A O   1 
ATOM   647  C CB  . VAL A  1 79  ? 13.365 29.464  82.069  1.00 35.23  ? 94  VAL A CB  1 
ATOM   648  C CG1 . VAL A  1 79  ? 14.393 29.101  81.011  1.00 36.42  ? 94  VAL A CG1 1 
ATOM   649  C CG2 . VAL A  1 79  ? 13.340 28.417  83.161  1.00 35.31  ? 94  VAL A CG2 1 
ATOM   650  N N   . HIS A  1 80  ? 15.011 32.335  81.328  1.00 37.32  ? 95  HIS A N   1 
ATOM   651  C CA  . HIS A  1 80  ? 15.315 33.323  80.261  1.00 35.54  ? 95  HIS A CA  1 
ATOM   652  C C   . HIS A  1 80  ? 14.656 32.836  78.968  1.00 35.98  ? 95  HIS A C   1 
ATOM   653  O O   . HIS A  1 80  ? 14.883 31.699  78.551  1.00 36.16  ? 95  HIS A O   1 
ATOM   654  C CB  . HIS A  1 80  ? 16.822 33.548  80.104  1.00 34.19  ? 95  HIS A CB  1 
ATOM   655  C CG  . HIS A  1 80  ? 17.126 34.867  79.481  1.00 34.37  ? 95  HIS A CG  1 
ATOM   656  N ND1 . HIS A  1 80  ? 16.837 35.145  78.159  1.00 32.07  ? 95  HIS A ND1 1 
ATOM   657  C CD2 . HIS A  1 80  ? 17.642 36.001  80.007  1.00 34.57  ? 95  HIS A CD2 1 
ATOM   658  C CE1 . HIS A  1 80  ? 17.177 36.391  77.893  1.00 32.91  ? 95  HIS A CE1 1 
ATOM   659  N NE2 . HIS A  1 80  ? 17.687 36.935  79.004  1.00 33.88  ? 95  HIS A NE2 1 
ATOM   660  N N   . PRO A  1 81  ? 13.811 33.655  78.295  1.00 35.72  ? 96  PRO A N   1 
ATOM   661  C CA  . PRO A  1 81  ? 13.108 33.201  77.093  1.00 34.59  ? 96  PRO A CA  1 
ATOM   662  C C   . PRO A  1 81  ? 14.029 32.881  75.899  1.00 33.22  ? 96  PRO A C   1 
ATOM   663  O O   . PRO A  1 81  ? 13.580 32.203  75.003  1.00 34.71  ? 96  PRO A O   1 
ATOM   664  C CB  . PRO A  1 81  ? 12.136 34.347  76.772  1.00 34.81  ? 96  PRO A CB  1 
ATOM   665  C CG  . PRO A  1 81  ? 12.754 35.566  77.424  1.00 36.13  ? 96  PRO A CG  1 
ATOM   666  C CD  . PRO A  1 81  ? 13.484 35.046  78.646  1.00 36.47  ? 96  PRO A CD  1 
ATOM   667  N N   . GLN A  1 82  ? 15.289 33.311  75.929  1.00 33.62  ? 97  GLN A N   1 
ATOM   668  C CA  . GLN A  1 82  ? 16.293 33.010  74.873  1.00 36.10  ? 97  GLN A CA  1 
ATOM   669  C C   . GLN A  1 82  ? 16.913 31.622  75.097  1.00 35.49  ? 97  GLN A C   1 
ATOM   670  O O   . GLN A  1 82  ? 17.593 31.162  74.180  1.00 39.63  ? 97  GLN A O   1 
ATOM   671  C CB  . GLN A  1 82  ? 17.342 34.122  74.794  1.00 36.74  ? 97  GLN A CB  1 
ATOM   672  C CG  . GLN A  1 82  ? 16.742 35.455  74.351  1.00 38.32  ? 97  GLN A CG  1 
ATOM   673  C CD  . GLN A  1 82  ? 17.712 36.613  74.344  1.00 40.98  ? 97  GLN A CD  1 
ATOM   674  O OE1 . GLN A  1 82  ? 18.904 36.470  74.602  1.00 45.74  ? 97  GLN A OE1 1 
ATOM   675  N NE2 . GLN A  1 82  ? 17.197 37.786  74.032  1.00 44.75  ? 97  GLN A NE2 1 
ATOM   676  N N   . PHE A  1 83  ? 16.662 30.958  76.231  1.00 33.26  ? 98  PHE A N   1 
ATOM   677  C CA  . PHE A  1 83  ? 17.321 29.668  76.569  1.00 31.94  ? 98  PHE A CA  1 
ATOM   678  C C   . PHE A  1 83  ? 16.669 28.499  75.824  1.00 31.08  ? 98  PHE A C   1 
ATOM   679  O O   . PHE A  1 83  ? 15.433 28.319  75.897  1.00 28.94  ? 98  PHE A O   1 
ATOM   680  C CB  . PHE A  1 83  ? 17.258 29.355  78.062  1.00 30.96  ? 98  PHE A CB  1 
ATOM   681  C CG  . PHE A  1 83  ? 17.834 28.003  78.401  1.00 31.31  ? 98  PHE A CG  1 
ATOM   682  C CD1 . PHE A  1 83  ? 19.207 27.801  78.387  1.00 29.32  ? 98  PHE A CD1 1 
ATOM   683  C CD2 . PHE A  1 83  ? 17.009 26.924  78.691  1.00 30.50  ? 98  PHE A CD2 1 
ATOM   684  C CE1 . PHE A  1 83  ? 19.744 26.561  78.701  1.00 28.59  ? 98  PHE A CE1 1 
ATOM   685  C CE2 . PHE A  1 83  ? 17.550 25.680  78.987  1.00 29.79  ? 98  PHE A CE2 1 
ATOM   686  C CZ  . PHE A  1 83  ? 18.916 25.505  78.991  1.00 28.73  ? 98  PHE A CZ  1 
ATOM   687  N N   . TYR A  1 84  ? 17.500 27.670  75.196  1.00 29.72  ? 99  TYR A N   1 
ATOM   688  C CA  . TYR A  1 84  ? 17.125 26.300  74.768  1.00 29.95  ? 99  TYR A CA  1 
ATOM   689  C C   . TYR A  1 84  ? 18.185 25.290  75.252  1.00 29.72  ? 99  TYR A C   1 
ATOM   690  O O   . TYR A  1 84  ? 17.773 24.274  75.807  1.00 29.25  ? 99  TYR A O   1 
ATOM   691  C CB  . TYR A  1 84  ? 16.842 26.238  73.264  1.00 29.59  ? 99  TYR A CB  1 
ATOM   692  C CG  . TYR A  1 84  ? 16.277 24.897  72.886  1.00 30.85  ? 99  TYR A CG  1 
ATOM   693  C CD1 . TYR A  1 84  ? 15.020 24.515  73.331  1.00 30.69  ? 99  TYR A CD1 1 
ATOM   694  C CD2 . TYR A  1 84  ? 17.025 23.974  72.175  1.00 31.69  ? 99  TYR A CD2 1 
ATOM   695  C CE1 . TYR A  1 84  ? 14.506 23.259  73.051  1.00 30.80  ? 99  TYR A CE1 1 
ATOM   696  C CE2 . TYR A  1 84  ? 16.525 22.714  71.886  1.00 31.68  ? 99  TYR A CE2 1 
ATOM   697  C CZ  . TYR A  1 84  ? 15.264 22.355  72.328  1.00 32.01  ? 99  TYR A CZ  1 
ATOM   698  O OH  . TYR A  1 84  ? 14.772 21.110  72.061  1.00 35.96  ? 99  TYR A OH  1 
ATOM   699  N N   . THR A  1 85  ? 19.482 25.542  75.043  1.00 29.73  ? 100 THR A N   1 
ATOM   700  C CA  . THR A  1 85  ? 20.597 24.704  75.572  1.00 30.34  ? 100 THR A CA  1 
ATOM   701  C C   . THR A  1 85  ? 21.676 25.610  76.166  1.00 29.99  ? 100 THR A C   1 
ATOM   702  O O   . THR A  1 85  ? 21.775 26.781  75.748  1.00 29.92  ? 100 THR A O   1 
ATOM   703  C CB  . THR A  1 85  ? 21.220 23.786  74.505  1.00 31.51  ? 100 THR A CB  1 
ATOM   704  O OG1 . THR A  1 85  ? 22.056 24.562  73.643  1.00 32.34  ? 100 THR A OG1 1 
ATOM   705  C CG2 . THR A  1 85  ? 20.196 23.041  73.678  1.00 30.91  ? 100 THR A CG2 1 
ATOM   706  N N   . ALA A  1 86  ? 22.470 25.061  77.084  1.00 29.93  ? 101 ALA A N   1 
ATOM   707  C CA  . ALA A  1 86  ? 23.585 25.755  77.769  1.00 30.64  ? 101 ALA A CA  1 
ATOM   708  C C   . ALA A  1 86  ? 24.639 26.206  76.749  1.00 31.49  ? 101 ALA A C   1 
ATOM   709  O O   . ALA A  1 86  ? 25.214 27.296  76.949  1.00 32.89  ? 101 ALA A O   1 
ATOM   710  C CB  . ALA A  1 86  ? 24.183 24.853  78.820  1.00 31.32  ? 101 ALA A CB  1 
ATOM   711  N N   . GLN A  1 87  ? 24.875 25.421  75.691  1.00 31.36  ? 102 GLN A N   1 
ATOM   712  C CA  . GLN A  1 87  ? 25.940 25.693  74.682  1.00 31.04  ? 102 GLN A CA  1 
ATOM   713  C C   . GLN A  1 87  ? 25.526 26.876  73.795  1.00 31.30  ? 102 GLN A C   1 
ATOM   714  O O   . GLN A  1 87  ? 26.418 27.588  73.334  1.00 30.10  ? 102 GLN A O   1 
ATOM   715  C CB  . GLN A  1 87  ? 26.253 24.473  73.817  1.00 32.49  ? 102 GLN A CB  1 
ATOM   716  C CG  . GLN A  1 87  ? 26.936 23.334  74.565  1.00 33.60  ? 102 GLN A CG  1 
ATOM   717  C CD  . GLN A  1 87  ? 26.034 22.475  75.423  1.00 35.70  ? 102 GLN A CD  1 
ATOM   718  O OE1 . GLN A  1 87  ? 26.460 21.957  76.451  1.00 41.11  ? 102 GLN A OE1 1 
ATOM   719  N NE2 . GLN A  1 87  ? 24.797 22.265  75.009  1.00 35.67  ? 102 GLN A NE2 1 
ATOM   720  N N   . ILE A  1 88  ? 24.229 27.079  73.573  1.00 30.28  ? 103 ILE A N   1 
ATOM   721  C CA  . ILE A  1 88  ? 23.697 28.261  72.836  1.00 32.95  ? 103 ILE A CA  1 
ATOM   722  C C   . ILE A  1 88  ? 23.765 29.485  73.762  1.00 33.19  ? 103 ILE A C   1 
ATOM   723  O O   . ILE A  1 88  ? 24.157 30.558  73.283  1.00 33.43  ? 103 ILE A O   1 
ATOM   724  C CB  . ILE A  1 88  ? 22.285 27.976  72.283  1.00 33.27  ? 103 ILE A CB  1 
ATOM   725  C CG1 . ILE A  1 88  ? 22.323 26.851  71.242  1.00 33.58  ? 103 ILE A CG1 1 
ATOM   726  C CG2 . ILE A  1 88  ? 21.661 29.243  71.710  1.00 33.22  ? 103 ILE A CG2 1 
ATOM   727  C CD1 . ILE A  1 88  ? 20.989 26.213  70.943  1.00 35.10  ? 103 ILE A CD1 1 
ATOM   728  N N   . GLY A  1 89  ? 23.373 29.335  75.030  1.00 34.65  ? 104 GLY A N   1 
ATOM   729  C CA  . GLY A  1 89  ? 23.526 30.359  76.085  1.00 33.06  ? 104 GLY A CA  1 
ATOM   730  C C   . GLY A  1 89  ? 22.197 30.787  76.681  1.00 31.43  ? 104 GLY A C   1 
ATOM   731  O O   . GLY A  1 89  ? 21.200 30.063  76.490  1.00 32.84  ? 104 GLY A O   1 
ATOM   732  N N   . ALA A  1 90  ? 22.195 31.939  77.362  1.00 31.83  ? 105 ALA A N   1 
ATOM   733  C CA  . ALA A  1 90  ? 21.093 32.464  78.207  1.00 31.67  ? 105 ALA A CA  1 
ATOM   734  C C   . ALA A  1 90  ? 20.730 31.434  79.289  1.00 31.29  ? 105 ALA A C   1 
ATOM   735  O O   . ALA A  1 90  ? 19.531 31.300  79.625  1.00 32.53  ? 105 ALA A O   1 
ATOM   736  C CB  . ALA A  1 90  ? 19.915 32.846  77.339  1.00 31.48  ? 105 ALA A CB  1 
ATOM   737  N N   . ASP A  1 91  ? 21.739 30.749  79.837  1.00 30.92  ? 106 ASP A N   1 
ATOM   738  C CA  . ASP A  1 91  ? 21.559 29.648  80.814  1.00 30.60  ? 106 ASP A CA  1 
ATOM   739  C C   . ASP A  1 91  ? 21.419 30.281  82.202  1.00 31.62  ? 106 ASP A C   1 
ATOM   740  O O   . ASP A  1 91  ? 22.376 30.250  82.999  1.00 31.04  ? 106 ASP A O   1 
ATOM   741  C CB  . ASP A  1 91  ? 22.666 28.597  80.704  1.00 30.91  ? 106 ASP A CB  1 
ATOM   742  C CG  . ASP A  1 91  ? 22.368 27.337  81.499  1.00 30.51  ? 106 ASP A CG  1 
ATOM   743  O OD1 . ASP A  1 91  ? 21.205 27.153  81.902  1.00 29.21  ? 106 ASP A OD1 1 
ATOM   744  O OD2 . ASP A  1 91  ? 23.303 26.559  81.722  1.00 32.49  ? 106 ASP A OD2 1 
ATOM   745  N N   . ILE A  1 92  ? 20.246 30.858  82.456  1.00 31.15  ? 107 ILE A N   1 
ATOM   746  C CA  . ILE A  1 92  ? 19.948 31.627  83.696  1.00 32.09  ? 107 ILE A CA  1 
ATOM   747  C C   . ILE A  1 92  ? 18.442 31.544  83.955  1.00 31.08  ? 107 ILE A C   1 
ATOM   748  O O   . ILE A  1 92  ? 17.660 31.630  82.983  1.00 29.93  ? 107 ILE A O   1 
ATOM   749  C CB  . ILE A  1 92  ? 20.481 33.071  83.577  1.00 32.90  ? 107 ILE A CB  1 
ATOM   750  C CG1 . ILE A  1 92  ? 20.547 33.764  84.940  1.00 33.46  ? 107 ILE A CG1 1 
ATOM   751  C CG2 . ILE A  1 92  ? 19.703 33.886  82.542  1.00 33.41  ? 107 ILE A CG2 1 
ATOM   752  C CD1 . ILE A  1 92  ? 21.418 34.995  84.951  1.00 33.65  ? 107 ILE A CD1 1 
ATOM   753  N N   . ALA A  1 93  ? 18.070 31.330  85.216  1.00 32.35  ? 108 ALA A N   1 
ATOM   754  C CA  . ALA A  1 93  ? 16.674 31.245  85.683  1.00 31.36  ? 108 ALA A CA  1 
ATOM   755  C C   . ALA A  1 93  ? 16.559 31.849  87.081  1.00 31.43  ? 108 ALA A C   1 
ATOM   756  O O   . ALA A  1 93  ? 17.584 31.924  87.799  1.00 30.89  ? 108 ALA A O   1 
ATOM   757  C CB  . ALA A  1 93  ? 16.191 29.818  85.646  1.00 31.79  ? 108 ALA A CB  1 
ATOM   758  N N   . LEU A  1 94  ? 15.343 32.275  87.426  1.00 32.41  ? 109 LEU A N   1 
ATOM   759  C CA  . LEU A  1 94  ? 14.986 32.833  88.751  1.00 33.70  ? 109 LEU A CA  1 
ATOM   760  C C   . LEU A  1 94  ? 13.914 31.937  89.368  1.00 33.13  ? 109 LEU A C   1 
ATOM   761  O O   . LEU A  1 94  ? 12.960 31.584  88.664  1.00 35.22  ? 109 LEU A O   1 
ATOM   762  C CB  . LEU A  1 94  ? 14.490 34.272  88.575  1.00 33.92  ? 109 LEU A CB  1 
ATOM   763  C CG  . LEU A  1 94  ? 15.556 35.297  88.191  1.00 35.39  ? 109 LEU A CG  1 
ATOM   764  C CD1 . LEU A  1 94  ? 14.914 36.600  87.727  1.00 35.26  ? 109 LEU A CD1 1 
ATOM   765  C CD2 . LEU A  1 94  ? 16.513 35.556  89.347  1.00 36.56  ? 109 LEU A CD2 1 
ATOM   766  N N   . LEU A  1 95  ? 14.087 31.573  90.638  1.00 35.22  ? 110 LEU A N   1 
ATOM   767  C CA  . LEU A  1 95  ? 13.019 30.960  91.467  1.00 35.13  ? 110 LEU A CA  1 
ATOM   768  C C   . LEU A  1 95  ? 12.492 32.013  92.441  1.00 34.37  ? 110 LEU A C   1 
ATOM   769  O O   . LEU A  1 95  ? 13.292 32.546  93.220  1.00 35.17  ? 110 LEU A O   1 
ATOM   770  C CB  . LEU A  1 95  ? 13.566 29.733  92.201  1.00 35.23  ? 110 LEU A CB  1 
ATOM   771  C CG  . LEU A  1 95  ? 14.334 28.722  91.352  1.00 34.93  ? 110 LEU A CG  1 
ATOM   772  C CD1 . LEU A  1 95  ? 14.724 27.520  92.197  1.00 36.42  ? 110 LEU A CD1 1 
ATOM   773  C CD2 . LEU A  1 95  ? 13.531 28.274  90.137  1.00 35.49  ? 110 LEU A CD2 1 
ATOM   774  N N   . GLU A  1 96  ? 11.199 32.327  92.363  1.00 36.24  ? 111 GLU A N   1 
ATOM   775  C CA  . GLU A  1 96  ? 10.512 33.166  93.378  1.00 37.88  ? 111 GLU A CA  1 
ATOM   776  C C   . GLU A  1 96  ? 9.993  32.242  94.479  1.00 36.36  ? 111 GLU A C   1 
ATOM   777  O O   . GLU A  1 96  ? 9.212  31.333  94.172  1.00 36.26  ? 111 GLU A O   1 
ATOM   778  C CB  . GLU A  1 96  ? 9.369  33.962  92.758  1.00 38.49  ? 111 GLU A CB  1 
ATOM   779  C CG  . GLU A  1 96  ? 8.849  35.061  93.665  1.00 40.77  ? 111 GLU A CG  1 
ATOM   780  C CD  . GLU A  1 96  ? 7.741  35.918  93.071  1.00 44.04  ? 111 GLU A CD  1 
ATOM   781  O OE1 . GLU A  1 96  ? 7.018  35.435  92.176  1.00 45.76  ? 111 GLU A OE1 1 
ATOM   782  O OE2 . GLU A  1 96  ? 7.580  37.057  93.531  1.00 50.20  ? 111 GLU A OE2 1 
ATOM   783  N N   . LEU A  1 97  ? 10.443 32.446  95.713  1.00 37.34  ? 112 LEU A N   1 
ATOM   784  C CA  . LEU A  1 97  ? 9.978  31.653  96.883  1.00 40.25  ? 112 LEU A CA  1 
ATOM   785  C C   . LEU A  1 97  ? 8.575  32.146  97.257  1.00 41.59  ? 112 LEU A C   1 
ATOM   786  O O   . LEU A  1 97  ? 8.247  33.303  96.926  1.00 40.10  ? 112 LEU A O   1 
ATOM   787  C CB  . LEU A  1 97  ? 10.988 31.807  98.022  1.00 41.13  ? 112 LEU A CB  1 
ATOM   788  C CG  . LEU A  1 97  ? 12.405 31.333  97.689  1.00 42.00  ? 112 LEU A CG  1 
ATOM   789  C CD1 . LEU A  1 97  ? 13.389 31.694  98.788  1.00 42.57  ? 112 LEU A CD1 1 
ATOM   790  C CD2 . LEU A  1 97  ? 12.431 29.837  97.432  1.00 43.46  ? 112 LEU A CD2 1 
ATOM   791  N N   . GLU A  1 98  ? 7.756  31.285  97.865  1.00 44.37  ? 113 GLU A N   1 
ATOM   792  C CA  . GLU A  1 98  ? 6.387  31.644  98.334  1.00 49.51  ? 113 GLU A CA  1 
ATOM   793  C C   . GLU A  1 98  ? 6.472  32.649  99.482  1.00 46.67  ? 113 GLU A C   1 
ATOM   794  O O   . GLU A  1 98  ? 5.537  33.440  99.624  1.00 45.59  ? 113 GLU A O   1 
ATOM   795  C CB  . GLU A  1 98  ? 5.601  30.418  98.789  1.00 54.81  ? 113 GLU A CB  1 
ATOM   796  C CG  . GLU A  1 98  ? 5.166  29.550  97.628  1.00 61.79  ? 113 GLU A CG  1 
ATOM   797  C CD  . GLU A  1 98  ? 4.056  28.566  97.944  1.00 69.04  ? 113 GLU A CD  1 
ATOM   798  O OE1 . GLU A  1 98  ? 3.390  28.747  98.982  1.00 73.66  ? 113 GLU A OE1 1 
ATOM   799  O OE2 . GLU A  1 98  ? 3.859  27.626  97.146  1.00 76.10  ? 113 GLU A OE2 1 
ATOM   800  N N   . GLU A  1 99  ? 7.553  32.603  100.266 1.00 46.10  ? 114 GLU A N   1 
ATOM   801  C CA  . GLU A  1 99  ? 7.812  33.528  101.396 1.00 47.48  ? 114 GLU A CA  1 
ATOM   802  C C   . GLU A  1 99  ? 9.222  34.088  101.284 1.00 43.41  ? 114 GLU A C   1 
ATOM   803  O O   . GLU A  1 99  ? 10.114 33.420  100.777 1.00 41.31  ? 114 GLU A O   1 
ATOM   804  C CB  . GLU A  1 99  ? 7.669  32.807  102.736 1.00 49.25  ? 114 GLU A CB  1 
ATOM   805  C CG  . GLU A  1 99  ? 6.293  32.212  102.954 1.00 52.07  ? 114 GLU A CG  1 
ATOM   806  C CD  . GLU A  1 99  ? 5.195  33.205  103.296 1.00 55.63  ? 114 GLU A CD  1 
ATOM   807  O OE1 . GLU A  1 99  ? 5.417  34.428  103.196 1.00 55.57  ? 114 GLU A OE1 1 
ATOM   808  O OE2 . GLU A  1 99  ? 4.108  32.742  103.698 1.00 64.25  ? 114 GLU A OE2 1 
ATOM   809  N N   . PRO A  1 100 ? 9.462  35.327  101.764 1.00 43.23  ? 115 PRO A N   1 
ATOM   810  C CA  . PRO A  1 100 ? 10.824 35.830  101.924 1.00 45.25  ? 115 PRO A CA  1 
ATOM   811  C C   . PRO A  1 100 ? 11.472 35.083  103.099 1.00 47.00  ? 115 PRO A C   1 
ATOM   812  O O   . PRO A  1 100 ? 10.766 34.750  104.031 1.00 47.51  ? 115 PRO A O   1 
ATOM   813  C CB  . PRO A  1 100 ? 10.633 37.322  102.211 1.00 44.57  ? 115 PRO A CB  1 
ATOM   814  C CG  . PRO A  1 100 ? 9.270  37.396  102.853 1.00 44.94  ? 115 PRO A CG  1 
ATOM   815  C CD  . PRO A  1 100 ? 8.448  36.304  102.194 1.00 44.37  ? 115 PRO A CD  1 
ATOM   816  N N   . VAL A  1 101 ? 12.773 34.810  103.022 1.00 47.34  ? 116 VAL A N   1 
ATOM   817  C CA  . VAL A  1 101 ? 13.514 34.138  104.125 1.00 49.98  ? 116 VAL A CA  1 
ATOM   818  C C   . VAL A  1 101 ? 13.888 35.221  105.143 1.00 52.49  ? 116 VAL A C   1 
ATOM   819  O O   . VAL A  1 101 ? 14.109 36.387  104.724 1.00 53.14  ? 116 VAL A O   1 
ATOM   820  C CB  . VAL A  1 101 ? 14.737 33.344  103.621 1.00 48.98  ? 116 VAL A CB  1 
ATOM   821  C CG1 . VAL A  1 101 ? 14.377 32.420  102.464 1.00 49.78  ? 116 VAL A CG1 1 
ATOM   822  C CG2 . VAL A  1 101 ? 15.907 34.230  103.232 1.00 48.38  ? 116 VAL A CG2 1 
ATOM   823  N N   . LYS A  1 102 ? 13.909 34.856  106.426 1.00 55.94  ? 117 LYS A N   1 
ATOM   824  C CA  . LYS A  1 102 ? 14.468 35.692  107.523 1.00 58.42  ? 117 LYS A CA  1 
ATOM   825  C C   . LYS A  1 102 ? 15.989 35.516  107.490 1.00 59.07  ? 117 LYS A C   1 
ATOM   826  O O   . LYS A  1 102 ? 16.438 34.378  107.710 1.00 66.83  ? 117 LYS A O   1 
ATOM   827  C CB  . LYS A  1 102 ? 13.865 35.291  108.875 1.00 57.19  ? 117 LYS A CB  1 
ATOM   828  C CG  . LYS A  1 102 ? 12.366 35.442  109.006 0.00 58.54  ? 117 LYS A CG  1 
ATOM   829  C CD  . LYS A  1 102 ? 11.822 34.981  110.342 0.00 58.49  ? 117 LYS A CD  1 
ATOM   830  C CE  . LYS A  1 102 ? 10.310 34.991  110.403 0.00 58.44  ? 117 LYS A CE  1 
ATOM   831  N NZ  . LYS A  1 102 ? 9.811  34.520  111.716 0.00 58.44  ? 117 LYS A NZ  1 
ATOM   832  N N   . VAL A  1 103 ? 16.741 36.575  107.167 1.00 62.71  ? 118 VAL A N   1 
ATOM   833  C CA  . VAL A  1 103 ? 18.214 36.503  106.921 1.00 63.60  ? 118 VAL A CA  1 
ATOM   834  C C   . VAL A  1 103 ? 18.946 36.544  108.270 1.00 65.09  ? 118 VAL A C   1 
ATOM   835  O O   . VAL A  1 103 ? 18.373 37.054  109.260 1.00 65.37  ? 118 VAL A O   1 
ATOM   836  C CB  . VAL A  1 103 ? 18.711 37.599  105.950 1.00 61.82  ? 118 VAL A CB  1 
ATOM   837  C CG1 . VAL A  1 103 ? 18.026 37.497  104.595 1.00 62.66  ? 118 VAL A CG1 1 
ATOM   838  C CG2 . VAL A  1 103 ? 18.581 39.014  106.499 1.00 62.43  ? 118 VAL A CG2 1 
ATOM   839  N N   . SER A  1 104 ? 20.155 35.989  108.293 1.00 63.01  ? 119 SER A N   1 
ATOM   840  C CA  . SER A  1 104 ? 21.041 35.883  109.480 1.00 64.96  ? 119 SER A CA  1 
ATOM   841  C C   . SER A  1 104 ? 22.496 35.879  109.007 1.00 66.10  ? 119 SER A C   1 
ATOM   842  O O   . SER A  1 104 ? 22.715 35.958  107.783 1.00 69.70  ? 119 SER A O   1 
ATOM   843  C CB  . SER A  1 104 ? 20.705 34.657  110.291 1.00 62.40  ? 119 SER A CB  1 
ATOM   844  O OG  . SER A  1 104 ? 20.806 33.480  109.507 1.00 58.87  ? 119 SER A OG  1 
ATOM   845  N N   . SER A  1 105 ? 23.454 35.801  109.934 1.00 68.06  ? 120 SER A N   1 
ATOM   846  C CA  . SER A  1 105 ? 24.905 35.666  109.632 1.00 68.50  ? 120 SER A CA  1 
ATOM   847  C C   . SER A  1 105 ? 25.163 34.362  108.858 1.00 67.09  ? 120 SER A C   1 
ATOM   848  O O   . SER A  1 105 ? 26.043 34.376  107.976 1.00 70.81  ? 120 SER A O   1 
ATOM   849  C CB  . SER A  1 105 ? 25.741 35.737  110.893 1.00 66.73  ? 120 SER A CB  1 
ATOM   850  O OG  . SER A  1 105 ? 25.519 34.619  111.723 0.00 66.80  ? 120 SER A OG  1 
ATOM   851  N N   . HIS A  1 106 ? 24.396 33.304  109.158 1.00 64.33  ? 121 HIS A N   1 
ATOM   852  C CA  . HIS A  1 106 ? 24.554 31.929  108.613 1.00 65.94  ? 121 HIS A CA  1 
ATOM   853  C C   . HIS A  1 106 ? 23.796 31.750  107.285 1.00 61.89  ? 121 HIS A C   1 
ATOM   854  O O   . HIS A  1 106 ? 24.211 30.878  106.498 1.00 60.71  ? 121 HIS A O   1 
ATOM   855  C CB  . HIS A  1 106 ? 24.101 30.919  109.673 1.00 70.29  ? 121 HIS A CB  1 
ATOM   856  C CG  . HIS A  1 106 ? 24.452 29.502  109.373 1.00 77.50  ? 121 HIS A CG  1 
ATOM   857  N ND1 . HIS A  1 106 ? 25.737 29.007  109.518 1.00 78.78  ? 121 HIS A ND1 1 
ATOM   858  C CD2 . HIS A  1 106 ? 23.690 28.469  108.957 1.00 81.26  ? 121 HIS A CD2 1 
ATOM   859  C CE1 . HIS A  1 106 ? 25.750 27.730  109.193 1.00 83.11  ? 121 HIS A CE1 1 
ATOM   860  N NE2 . HIS A  1 106 ? 24.505 27.377  108.851 1.00 86.06  ? 121 HIS A NE2 1 
ATOM   861  N N   . VAL A  1 107 ? 22.715 32.506  107.055 1.00 56.86  ? 122 VAL A N   1 
ATOM   862  C CA  . VAL A  1 107 ? 21.891 32.462  105.810 1.00 55.96  ? 122 VAL A CA  1 
ATOM   863  C C   . VAL A  1 107 ? 21.568 33.898  105.382 1.00 52.40  ? 122 VAL A C   1 
ATOM   864  O O   . VAL A  1 107 ? 20.736 34.544  106.060 1.00 52.72  ? 122 VAL A O   1 
ATOM   865  C CB  . VAL A  1 107 ? 20.603 31.641  106.018 1.00 57.76  ? 122 VAL A CB  1 
ATOM   866  C CG1 . VAL A  1 107 ? 19.666 31.718  104.822 1.00 57.17  ? 122 VAL A CG1 1 
ATOM   867  C CG2 . VAL A  1 107 ? 20.909 30.189  106.353 1.00 59.27  ? 122 VAL A CG2 1 
ATOM   868  N N   . HIS A  1 108 ? 22.155 34.365  104.275 1.00 49.04  ? 123 HIS A N   1 
ATOM   869  C CA  . HIS A  1 108 ? 21.860 35.708  103.702 1.00 49.55  ? 123 HIS A CA  1 
ATOM   870  C C   . HIS A  1 108 ? 22.276 35.784  102.227 1.00 44.63  ? 123 HIS A C   1 
ATOM   871  O O   . HIS A  1 108 ? 22.875 34.814  101.713 1.00 42.87  ? 123 HIS A O   1 
ATOM   872  C CB  . HIS A  1 108 ? 22.437 36.832  104.583 1.00 52.72  ? 123 HIS A CB  1 
ATOM   873  C CG  . HIS A  1 108 ? 23.921 36.945  104.623 1.00 52.27  ? 123 HIS A CG  1 
ATOM   874  N ND1 . HIS A  1 108 ? 24.669 36.473  105.687 1.00 58.33  ? 123 HIS A ND1 1 
ATOM   875  C CD2 . HIS A  1 108 ? 24.789 37.523  103.768 1.00 55.89  ? 123 HIS A CD2 1 
ATOM   876  C CE1 . HIS A  1 108 ? 25.942 36.740  105.480 1.00 58.07  ? 123 HIS A CE1 1 
ATOM   877  N NE2 . HIS A  1 108 ? 26.043 37.389  104.305 1.00 57.72  ? 123 HIS A NE2 1 
ATOM   878  N N   . THR A  1 109 ? 21.920 36.888  101.565 1.00 39.68  ? 124 THR A N   1 
ATOM   879  C CA  . THR A  1 109 ? 21.998 37.048  100.089 1.00 37.60  ? 124 THR A CA  1 
ATOM   880  C C   . THR A  1 109 ? 23.449 37.281  99.666  1.00 36.11  ? 124 THR A C   1 
ATOM   881  O O   . THR A  1 109 ? 24.242 37.780  100.490 1.00 37.39  ? 124 THR A O   1 
ATOM   882  C CB  . THR A  1 109 ? 21.110 38.191  99.584  1.00 37.24  ? 124 THR A CB  1 
ATOM   883  O OG1 . THR A  1 109 ? 21.601 39.409  100.138 1.00 39.76  ? 124 THR A OG1 1 
ATOM   884  C CG2 . THR A  1 109 ? 19.655 38.030  99.954  1.00 35.61  ? 124 THR A CG2 1 
ATOM   885  N N   . VAL A  1 110 ? 23.778 36.907  98.428  1.00 34.05  ? 125 VAL A N   1 
ATOM   886  C CA  . VAL A  1 110 ? 25.026 37.325  97.723  1.00 34.29  ? 125 VAL A CA  1 
ATOM   887  C C   . VAL A  1 110 ? 24.734 38.652  97.009  1.00 35.04  ? 125 VAL A C   1 
ATOM   888  O O   . VAL A  1 110 ? 23.571 38.859  96.598  1.00 35.94  ? 125 VAL A O   1 
ATOM   889  C CB  . VAL A  1 110 ? 25.528 36.238  96.750  1.00 33.65  ? 125 VAL A CB  1 
ATOM   890  C CG1 . VAL A  1 110 ? 24.638 36.068  95.524  1.00 34.58  ? 125 VAL A CG1 1 
ATOM   891  C CG2 . VAL A  1 110 ? 26.972 36.473  96.341  1.00 34.57  ? 125 VAL A CG2 1 
ATOM   892  N N   . THR A  1 111 ? 25.748 39.502  96.861  1.00 36.49  ? 126 THR A N   1 
ATOM   893  C CA  . THR A  1 111 ? 25.661 40.787  96.116  1.00 39.47  ? 126 THR A CA  1 
ATOM   894  C C   . THR A  1 111 ? 25.910 40.506  94.630  1.00 39.17  ? 126 THR A C   1 
ATOM   895  O O   . THR A  1 111 ? 26.873 39.774  94.319  1.00 39.29  ? 126 THR A O   1 
ATOM   896  C CB  . THR A  1 111 ? 26.639 41.822  96.688  1.00 40.97  ? 126 THR A CB  1 
ATOM   897  O OG1 . THR A  1 111 ? 26.370 41.935  98.087  1.00 44.79  ? 126 THR A OG1 1 
ATOM   898  C CG2 . THR A  1 111 ? 26.517 43.189  96.048  1.00 41.58  ? 126 THR A CG2 1 
ATOM   899  N N   . LEU A  1 112 ? 25.076 41.060  93.747  1.00 39.12  ? 127 LEU A N   1 
ATOM   900  C CA  . LEU A  1 112 ? 25.311 41.028  92.281  1.00 41.23  ? 127 LEU A CA  1 
ATOM   901  C C   . LEU A  1 112 ? 26.285 42.140  91.917  1.00 42.26  ? 127 LEU A C   1 
ATOM   902  O O   . LEU A  1 112 ? 26.269 43.207  92.525  1.00 43.96  ? 127 LEU A O   1 
ATOM   903  C CB  . LEU A  1 112 ? 23.983 41.158  91.534  1.00 41.19  ? 127 LEU A CB  1 
ATOM   904  C CG  . LEU A  1 112 ? 22.979 40.045  91.823  1.00 42.11  ? 127 LEU A CG  1 
ATOM   905  C CD1 . LEU A  1 112 ? 21.730 40.215  90.974  1.00 43.12  ? 127 LEU A CD1 1 
ATOM   906  C CD2 . LEU A  1 112 ? 23.594 38.669  91.599  1.00 41.70  ? 127 LEU A CD2 1 
ATOM   907  N N   . PRO A  1 113 ? 27.168 41.922  90.918  1.00 41.42  ? 128 PRO A N   1 
ATOM   908  C CA  . PRO A  1 113 ? 28.116 42.950  90.497  1.00 43.24  ? 128 PRO A CA  1 
ATOM   909  C C   . PRO A  1 113 ? 27.403 44.076  89.752  1.00 42.89  ? 128 PRO A C   1 
ATOM   910  O O   . PRO A  1 113 ? 26.309 43.873  89.230  1.00 43.36  ? 128 PRO A O   1 
ATOM   911  C CB  . PRO A  1 113 ? 29.093 42.207  89.579  1.00 41.09  ? 128 PRO A CB  1 
ATOM   912  C CG  . PRO A  1 113 ? 28.301 41.026  89.057  1.00 41.44  ? 128 PRO A CG  1 
ATOM   913  C CD  . PRO A  1 113 ? 27.299 40.685  90.137  1.00 41.79  ? 128 PRO A CD  1 
ATOM   914  N N   . PRO A  1 114 ? 27.988 45.294  89.687  1.00 46.27  ? 129 PRO A N   1 
ATOM   915  C CA  . PRO A  1 114 ? 27.500 46.332  88.780  1.00 47.87  ? 129 PRO A CA  1 
ATOM   916  C C   . PRO A  1 114 ? 27.769 45.906  87.328  1.00 48.25  ? 129 PRO A C   1 
ATOM   917  O O   . PRO A  1 114 ? 28.667 45.110  87.114  1.00 47.10  ? 129 PRO A O   1 
ATOM   918  C CB  . PRO A  1 114 ? 28.297 47.598  89.152  1.00 49.23  ? 129 PRO A CB  1 
ATOM   919  C CG  . PRO A  1 114 ? 29.018 47.255  90.447  1.00 50.85  ? 129 PRO A CG  1 
ATOM   920  C CD  . PRO A  1 114 ? 29.144 45.746  90.473  1.00 48.27  ? 129 PRO A CD  1 
ATOM   921  N N   . ALA A  1 115 ? 27.004 46.452  86.373  1.00 50.55  ? 130 ALA A N   1 
ATOM   922  C CA  . ALA A  1 115 ? 27.144 46.218  84.912  1.00 52.42  ? 130 ALA A CA  1 
ATOM   923  C C   . ALA A  1 115 ? 28.578 46.511  84.448  1.00 53.93  ? 130 ALA A C   1 
ATOM   924  O O   . ALA A  1 115 ? 29.072 45.776  83.583  1.00 55.21  ? 130 ALA A O   1 
ATOM   925  C CB  . ALA A  1 115 ? 26.142 47.055  84.155  1.00 53.05  ? 130 ALA A CB  1 
ATOM   926  N N   . SER A  1 116 ? 29.235 47.516  85.037  1.00 56.30  ? 131 SER A N   1 
ATOM   927  C CA  . SER A  1 116 ? 30.598 47.982  84.660  1.00 60.96  ? 131 SER A CA  1 
ATOM   928  C C   . SER A  1 116 ? 31.692 46.996  85.107  1.00 62.16  ? 131 SER A C   1 
ATOM   929  O O   . SER A  1 116 ? 32.812 47.097  84.581  1.00 65.37  ? 131 SER A O   1 
ATOM   930  C CB  . SER A  1 116 ? 30.854 49.362  85.212  1.00 60.83  ? 131 SER A CB  1 
ATOM   931  O OG  . SER A  1 116 ? 30.673 49.381  86.619  1.00 61.38  ? 131 SER A OG  1 
ATOM   932  N N   . GLU A  1 117 ? 31.404 46.097  86.055  1.00 62.02  ? 132 GLU A N   1 
ATOM   933  C CA  . GLU A  1 117 ? 32.377 45.161  86.680  1.00 58.53  ? 132 GLU A CA  1 
ATOM   934  C C   . GLU A  1 117 ? 32.938 44.191  85.633  1.00 57.53  ? 132 GLU A C   1 
ATOM   935  O O   . GLU A  1 117 ? 32.140 43.488  84.983  1.00 57.75  ? 132 GLU A O   1 
ATOM   936  C CB  . GLU A  1 117 ? 31.706 44.378  87.810  1.00 58.55  ? 132 GLU A CB  1 
ATOM   937  C CG  . GLU A  1 117 ? 32.693 43.648  88.703  1.00 59.61  ? 132 GLU A CG  1 
ATOM   938  C CD  . GLU A  1 117 ? 33.552 44.547  89.580  1.00 59.00  ? 132 GLU A CD  1 
ATOM   939  O OE1 . GLU A  1 117 ? 34.739 44.226  89.762  1.00 56.87  ? 132 GLU A OE1 1 
ATOM   940  O OE2 . GLU A  1 117 ? 33.031 45.561  90.092  1.00 58.41  ? 132 GLU A OE2 1 
ATOM   941  N N   . THR A  1 118 ? 34.260 44.202  85.458  1.00 58.77  ? 133 THR A N   1 
ATOM   942  C CA  . THR A  1 118 ? 35.024 43.273  84.590  1.00 58.41  ? 133 THR A CA  1 
ATOM   943  C C   . THR A  1 118 ? 36.005 42.540  85.508  1.00 58.52  ? 133 THR A C   1 
ATOM   944  O O   . THR A  1 118 ? 37.064 43.113  85.849  1.00 66.18  ? 133 THR A O   1 
ATOM   945  C CB  . THR A  1 118 ? 35.669 44.015  83.408  1.00 58.86  ? 133 THR A CB  1 
ATOM   946  O OG1 . THR A  1 118 ? 36.584 44.961  83.933  0.00 59.74  ? 133 THR A OG1 1 
ATOM   947  C CG2 . THR A  1 118 ? 34.667 44.685  82.497  0.00 59.80  ? 133 THR A CG2 1 
ATOM   948  N N   . PHE A  1 119 ? 35.631 41.330  85.931  1.00 54.20  ? 134 PHE A N   1 
ATOM   949  C CA  . PHE A  1 119 ? 36.460 40.404  86.746  1.00 49.59  ? 134 PHE A CA  1 
ATOM   950  C C   . PHE A  1 119 ? 37.666 40.003  85.908  1.00 48.46  ? 134 PHE A C   1 
ATOM   951  O O   . PHE A  1 119 ? 37.507 39.213  84.984  1.00 50.43  ? 134 PHE A O   1 
ATOM   952  C CB  . PHE A  1 119 ? 35.651 39.171  87.149  1.00 46.87  ? 134 PHE A CB  1 
ATOM   953  C CG  . PHE A  1 119 ? 34.438 39.467  87.994  1.00 45.50  ? 134 PHE A CG  1 
ATOM   954  C CD1 . PHE A  1 119 ? 34.562 39.672  89.358  1.00 46.10  ? 134 PHE A CD1 1 
ATOM   955  C CD2 . PHE A  1 119 ? 33.175 39.540  87.425  1.00 44.31  ? 134 PHE A CD2 1 
ATOM   956  C CE1 . PHE A  1 119 ? 33.447 39.936  90.139  1.00 47.97  ? 134 PHE A CE1 1 
ATOM   957  C CE2 . PHE A  1 119 ? 32.063 39.812  88.206  1.00 43.63  ? 134 PHE A CE2 1 
ATOM   958  C CZ  . PHE A  1 119 ? 32.199 40.007  89.561  1.00 45.73  ? 134 PHE A CZ  1 
ATOM   959  N N   . PRO A  1 120 ? 38.885 40.520  86.180  1.00 47.25  ? 135 PRO A N   1 
ATOM   960  C CA  . PRO A  1 120 ? 40.003 40.336  85.257  1.00 47.56  ? 135 PRO A CA  1 
ATOM   961  C C   . PRO A  1 120 ? 40.515 38.898  85.266  1.00 48.07  ? 135 PRO A C   1 
ATOM   962  O O   . PRO A  1 120 ? 40.361 38.190  86.255  1.00 47.45  ? 135 PRO A O   1 
ATOM   963  C CB  . PRO A  1 120 ? 41.078 41.302  85.772  1.00 48.82  ? 135 PRO A CB  1 
ATOM   964  C CG  . PRO A  1 120 ? 40.776 41.419  87.256  1.00 49.01  ? 135 PRO A CG  1 
ATOM   965  C CD  . PRO A  1 120 ? 39.266 41.297  87.372  1.00 49.25  ? 135 PRO A CD  1 
ATOM   966  N N   . PRO A  1 121 ? 41.102 38.412  84.154  1.00 48.31  ? 136 PRO A N   1 
ATOM   967  C CA  . PRO A  1 121 ? 41.778 37.112  84.137  1.00 47.14  ? 136 PRO A CA  1 
ATOM   968  C C   . PRO A  1 121 ? 42.792 36.932  85.272  1.00 46.62  ? 136 PRO A C   1 
ATOM   969  O O   . PRO A  1 121 ? 43.480 37.877  85.586  1.00 44.74  ? 136 PRO A O   1 
ATOM   970  C CB  . PRO A  1 121 ? 42.488 37.113  82.782  1.00 47.95  ? 136 PRO A CB  1 
ATOM   971  C CG  . PRO A  1 121 ? 41.573 37.958  81.916  1.00 48.35  ? 136 PRO A CG  1 
ATOM   972  C CD  . PRO A  1 121 ? 41.113 39.066  82.836  1.00 48.24  ? 136 PRO A CD  1 
ATOM   973  N N   . GLY A  1 122 ? 42.809 35.743  85.878  1.00 47.19  ? 137 GLY A N   1 
ATOM   974  C CA  . GLY A  1 122 ? 43.713 35.388  86.987  1.00 49.94  ? 137 GLY A CA  1 
ATOM   975  C C   . GLY A  1 122 ? 43.143 35.694  88.365  1.00 50.54  ? 137 GLY A C   1 
ATOM   976  O O   . GLY A  1 122 ? 43.768 35.262  89.347  1.00 53.85  ? 137 GLY A O   1 
ATOM   977  N N   . MET A  1 123 ? 42.019 36.415  88.456  1.00 51.03  ? 138 MET A N   1 
ATOM   978  C CA  . MET A  1 123 ? 41.372 36.783  89.746  1.00 53.25  ? 138 MET A CA  1 
ATOM   979  C C   . MET A  1 123 ? 40.977 35.498  90.474  1.00 52.14  ? 138 MET A C   1 
ATOM   980  O O   . MET A  1 123 ? 40.350 34.632  89.866  1.00 47.67  ? 138 MET A O   1 
ATOM   981  C CB  . MET A  1 123 ? 40.128 37.664  89.545  1.00 57.79  ? 138 MET A CB  1 
ATOM   982  C CG  . MET A  1 123 ? 39.379 37.986  90.842  1.00 63.27  ? 138 MET A CG  1 
ATOM   983  S SD  . MET A  1 123 ? 38.413 39.495  90.795  1.00 75.42  ? 138 MET A SD  1 
ATOM   984  C CE  . MET A  1 123 ? 39.726 40.701  90.976  1.00 74.59  ? 138 MET A CE  1 
ATOM   985  N N   . PRO A  1 124 ? 41.332 35.328  91.773  1.00 51.29  ? 139 PRO A N   1 
ATOM   986  C CA  . PRO A  1 124 ? 40.887 34.174  92.550  1.00 50.61  ? 139 PRO A CA  1 
ATOM   987  C C   . PRO A  1 124 ? 39.387 34.278  92.867  1.00 46.87  ? 139 PRO A C   1 
ATOM   988  O O   . PRO A  1 124 ? 38.987 35.227  93.497  1.00 50.27  ? 139 PRO A O   1 
ATOM   989  C CB  . PRO A  1 124 ? 41.710 34.213  93.852  1.00 53.12  ? 139 PRO A CB  1 
ATOM   990  C CG  . PRO A  1 124 ? 42.721 35.330  93.665  1.00 53.33  ? 139 PRO A CG  1 
ATOM   991  C CD  . PRO A  1 124 ? 42.167 36.231  92.582  1.00 53.70  ? 139 PRO A CD  1 
ATOM   992  N N   . CYS A  1 125 ? 38.601 33.329  92.367  1.00 43.46  ? 140 CYS A N   1 
ATOM   993  C CA  . CYS A  1 125 ? 37.141 33.197  92.615  1.00 41.39  ? 140 CYS A CA  1 
ATOM   994  C C   . CYS A  1 125 ? 36.880 31.820  93.224  1.00 38.64  ? 140 CYS A C   1 
ATOM   995  O O   . CYS A  1 125 ? 37.784 30.983  93.174  1.00 37.35  ? 140 CYS A O   1 
ATOM   996  C CB  . CYS A  1 125 ? 36.367 33.409  91.320  1.00 43.71  ? 140 CYS A CB  1 
ATOM   997  S SG  . CYS A  1 125 ? 36.677 35.041  90.594  1.00 47.23  ? 140 CYS A SG  1 
ATOM   998  N N   . TRP A  1 126 ? 35.707 31.622  93.825  1.00 37.78  ? 141 TRP A N   1 
ATOM   999  C CA  . TRP A  1 126 ? 35.306 30.356  94.483  1.00 37.06  ? 141 TRP A CA  1 
ATOM   1000 C C   . TRP A  1 126 ? 34.013 29.850  93.851  1.00 35.22  ? 141 TRP A C   1 
ATOM   1001 O O   . TRP A  1 126 ? 33.095 30.660  93.625  1.00 34.36  ? 141 TRP A O   1 
ATOM   1002 C CB  . TRP A  1 126 ? 35.177 30.557  95.991  1.00 38.53  ? 141 TRP A CB  1 
ATOM   1003 C CG  . TRP A  1 126 ? 36.500 30.827  96.638  1.00 40.02  ? 141 TRP A CG  1 
ATOM   1004 C CD1 . TRP A  1 126 ? 37.188 32.007  96.655  1.00 41.31  ? 141 TRP A CD1 1 
ATOM   1005 C CD2 . TRP A  1 126 ? 37.317 29.876  97.338  1.00 40.99  ? 141 TRP A CD2 1 
ATOM   1006 N NE1 . TRP A  1 126 ? 38.374 31.856  97.320  1.00 43.43  ? 141 TRP A NE1 1 
ATOM   1007 C CE2 . TRP A  1 126 ? 38.480 30.560  97.754  1.00 42.84  ? 141 TRP A CE2 1 
ATOM   1008 C CE3 . TRP A  1 126 ? 37.178 28.520  97.654  1.00 40.93  ? 141 TRP A CE3 1 
ATOM   1009 C CZ2 . TRP A  1 126 ? 39.488 29.931  98.485  1.00 42.85  ? 141 TRP A CZ2 1 
ATOM   1010 C CZ3 . TRP A  1 126 ? 38.177 27.896  98.366  1.00 42.78  ? 141 TRP A CZ3 1 
ATOM   1011 C CH2 . TRP A  1 126 ? 39.315 28.595  98.778  1.00 44.38  ? 141 TRP A CH2 1 
ATOM   1012 N N   . VAL A  1 127 ? 33.970 28.548  93.586  1.00 34.74  ? 142 VAL A N   1 
ATOM   1013 C CA  . VAL A  1 127 ? 32.727 27.825  93.198  1.00 33.63  ? 142 VAL A CA  1 
ATOM   1014 C C   . VAL A  1 127 ? 32.431 26.816  94.308  1.00 33.06  ? 142 VAL A C   1 
ATOM   1015 O O   . VAL A  1 127 ? 33.389 26.239  94.877  1.00 33.95  ? 142 VAL A O   1 
ATOM   1016 C CB  . VAL A  1 127 ? 32.808 27.196  91.793  1.00 33.25  ? 142 VAL A CB  1 
ATOM   1017 C CG1 . VAL A  1 127 ? 33.873 26.118  91.682  1.00 35.12  ? 142 VAL A CG1 1 
ATOM   1018 C CG2 . VAL A  1 127 ? 31.453 26.656  91.344  1.00 32.93  ? 142 VAL A CG2 1 
ATOM   1019 N N   . THR A  1 128 ? 31.150 26.675  94.640  1.00 33.06  ? 143 THR A N   1 
ATOM   1020 C CA  . THR A  1 128 ? 30.652 25.872  95.784  1.00 32.46  ? 143 THR A CA  1 
ATOM   1021 C C   . THR A  1 128 ? 29.519 24.963  95.300  1.00 30.92  ? 143 THR A C   1 
ATOM   1022 O O   . THR A  1 128 ? 28.822 25.342  94.338  1.00 29.25  ? 143 THR A O   1 
ATOM   1023 C CB  . THR A  1 128 ? 30.241 26.799  96.937  1.00 33.11  ? 143 THR A CB  1 
ATOM   1024 O OG1 . THR A  1 128 ? 29.278 27.747  96.479  1.00 34.28  ? 143 THR A OG1 1 
ATOM   1025 C CG2 . THR A  1 128 ? 31.404 27.579  97.506  1.00 32.81  ? 143 THR A CG2 1 
ATOM   1026 N N   . GLY A  1 129 ? 29.335 23.808  95.947  1.00 30.48  ? 144 GLY A N   1 
ATOM   1027 C CA  . GLY A  1 129 ? 28.150 22.961  95.711  1.00 31.54  ? 144 GLY A CA  1 
ATOM   1028 C C   . GLY A  1 129 ? 28.310 21.548  96.225  1.00 32.10  ? 144 GLY A C   1 
ATOM   1029 O O   . GLY A  1 129 ? 29.368 21.235  96.808  1.00 32.44  ? 144 GLY A O   1 
ATOM   1030 N N   . TRP A  1 130 ? 27.281 20.728  95.996  1.00 34.21  ? 145 TRP A N   1 
ATOM   1031 C CA  . TRP A  1 130 ? 27.197 19.313  96.440  1.00 35.59  ? 145 TRP A CA  1 
ATOM   1032 C C   . TRP A  1 130 ? 27.308 18.378  95.230  1.00 37.71  ? 145 TRP A C   1 
ATOM   1033 O O   . TRP A  1 130 ? 26.820 17.230  95.322  1.00 38.94  ? 145 TRP A O   1 
ATOM   1034 C CB  . TRP A  1 130 ? 25.892 19.085  97.207  1.00 34.94  ? 145 TRP A CB  1 
ATOM   1035 C CG  . TRP A  1 130 ? 25.761 19.877  98.473  1.00 35.39  ? 145 TRP A CG  1 
ATOM   1036 C CD1 . TRP A  1 130 ? 26.210 19.533  99.713  1.00 35.21  ? 145 TRP A CD1 1 
ATOM   1037 C CD2 . TRP A  1 130 ? 25.079 21.134  98.628  1.00 34.83  ? 145 TRP A CD2 1 
ATOM   1038 N NE1 . TRP A  1 130 ? 25.851 20.486  100.629 1.00 36.64  ? 145 TRP A NE1 1 
ATOM   1039 C CE2 . TRP A  1 130 ? 25.159 21.483  99.993  1.00 34.43  ? 145 TRP A CE2 1 
ATOM   1040 C CE3 . TRP A  1 130 ? 24.412 21.994  97.746  1.00 33.19  ? 145 TRP A CE3 1 
ATOM   1041 C CZ2 . TRP A  1 130 ? 24.599 22.660  100.492 1.00 34.01  ? 145 TRP A CZ2 1 
ATOM   1042 C CZ3 . TRP A  1 130 ? 23.862 23.157  98.242  1.00 35.50  ? 145 TRP A CZ3 1 
ATOM   1043 C CH2 . TRP A  1 130 ? 23.948 23.480  99.598  1.00 34.80  ? 145 TRP A CH2 1 
ATOM   1044 N N   . GLY A  1 131 ? 27.946 18.834  94.148  1.00 35.04  ? 146 GLY A N   1 
ATOM   1045 C CA  . GLY A  1 131 ? 28.079 18.055  92.907  1.00 34.84  ? 146 GLY A CA  1 
ATOM   1046 C C   . GLY A  1 131 ? 29.158 16.991  93.006  1.00 35.03  ? 146 GLY A C   1 
ATOM   1047 O O   . GLY A  1 131 ? 29.809 16.873  94.072  1.00 35.52  ? 146 GLY A O   1 
ATOM   1048 N N   . ASP A  1 132 ? 29.353 16.263  91.906  1.00 34.25  ? 147 ASP A N   1 
ATOM   1049 C CA  . ASP A  1 132 ? 30.295 15.122  91.790  1.00 34.94  ? 147 ASP A CA  1 
ATOM   1050 C C   . ASP A  1 132 ? 31.716 15.597  92.118  1.00 34.87  ? 147 ASP A C   1 
ATOM   1051 O O   . ASP A  1 132 ? 32.044 16.762  91.817  1.00 34.88  ? 147 ASP A O   1 
ATOM   1052 C CB  . ASP A  1 132 ? 30.183 14.484  90.404  1.00 35.82  ? 147 ASP A CB  1 
ATOM   1053 C CG  . ASP A  1 132 ? 28.907 13.685  90.181  1.00 36.35  ? 147 ASP A CG  1 
ATOM   1054 O OD1 . ASP A  1 132 ? 27.999 13.728  91.041  1.00 37.16  ? 147 ASP A OD1 1 
ATOM   1055 O OD2 . ASP A  1 132 ? 28.829 13.024  89.142  1.00 41.68  ? 147 ASP A OD2 1 
ATOM   1056 N N   . VAL A  1 133 ? 32.517 14.734  92.746  1.00 36.20  ? 148 VAL A N   1 
ATOM   1057 C CA  . VAL A  1 133 ? 33.915 15.053  93.165  1.00 37.68  ? 148 VAL A CA  1 
ATOM   1058 C C   . VAL A  1 133 ? 34.881 14.675  92.037  1.00 38.64  ? 148 VAL A C   1 
ATOM   1059 O O   . VAL A  1 133 ? 36.068 15.030  92.149  1.00 39.15  ? 148 VAL A O   1 
ATOM   1060 C CB  . VAL A  1 133 ? 34.285 14.401  94.512  1.00 39.48  ? 148 VAL A CB  1 
ATOM   1061 C CG1 . VAL A  1 133 ? 33.392 14.927  95.629  1.00 40.60  ? 148 VAL A CG1 1 
ATOM   1062 C CG2 . VAL A  1 133 ? 34.261 12.879  94.471  1.00 38.16  ? 148 VAL A CG2 1 
ATOM   1063 N N   . ASP A  1 134 ? 34.391 13.988  90.997  1.00 40.55  ? 149 ASP A N   1 
ATOM   1064 C CA  . ASP A  1 134 ? 35.127 13.719  89.735  1.00 42.35  ? 149 ASP A CA  1 
ATOM   1065 C C   . ASP A  1 134 ? 34.129 13.225  88.681  1.00 43.07  ? 149 ASP A C   1 
ATOM   1066 O O   . ASP A  1 134 ? 32.926 13.119  89.008  1.00 42.01  ? 149 ASP A O   1 
ATOM   1067 C CB  . ASP A  1 134 ? 36.255 12.703  89.951  1.00 47.17  ? 149 ASP A CB  1 
ATOM   1068 C CG  . ASP A  1 134 ? 37.516 13.016  89.163  1.00 51.32  ? 149 ASP A CG  1 
ATOM   1069 O OD1 . ASP A  1 134 ? 37.396 13.525  88.020  1.00 54.19  ? 149 ASP A OD1 1 
ATOM   1070 O OD2 . ASP A  1 134 ? 38.610 12.754  89.697  1.00 58.10  ? 149 ASP A OD2 1 
ATOM   1071 N N   . ASN A  1 135 ? 34.602 12.938  87.469  1.00 41.45  ? 150 ASN A N   1 
ATOM   1072 C CA  . ASN A  1 135 ? 33.770 12.396  86.361  1.00 46.56  ? 150 ASN A CA  1 
ATOM   1073 C C   . ASN A  1 135 ? 33.115 11.089  86.836  1.00 45.14  ? 150 ASN A C   1 
ATOM   1074 O O   . ASN A  1 135 ? 33.858 10.180  87.251  1.00 45.56  ? 150 ASN A O   1 
ATOM   1075 C CB  . ASN A  1 135 ? 34.590 12.204  85.078  1.00 46.88  ? 150 ASN A CB  1 
ATOM   1076 C CG  . ASN A  1 135 ? 35.129 13.510  84.530  1.00 48.76  ? 150 ASN A CG  1 
ATOM   1077 O OD1 . ASN A  1 135 ? 34.371 14.328  84.015  1.00 48.53  ? 150 ASN A OD1 1 
ATOM   1078 N ND2 . ASN A  1 135 ? 36.426 13.735  84.659  1.00 50.66  ? 150 ASN A ND2 1 
ATOM   1079 N N   . ASP A  1 136 ? 31.779 11.035  86.842  1.00 47.31  ? 151 ASP A N   1 
ATOM   1080 C CA  . ASP A  1 136 ? 30.963 9.848   87.224  1.00 51.45  ? 151 ASP A CA  1 
ATOM   1081 C C   . ASP A  1 136 ? 31.309 9.379   88.650  1.00 52.02  ? 151 ASP A C   1 
ATOM   1082 O O   . ASP A  1 136 ? 31.238 8.164   88.894  1.00 56.12  ? 151 ASP A O   1 
ATOM   1083 C CB  . ASP A  1 136 ? 31.148 8.730   86.193  1.00 52.43  ? 151 ASP A CB  1 
ATOM   1084 C CG  . ASP A  1 136 ? 30.917 9.161   84.759  0.00 52.53  ? 151 ASP A CG  1 
ATOM   1085 O OD1 . ASP A  1 136 ? 29.804 9.642   84.465  0.00 52.56  ? 151 ASP A OD1 1 
ATOM   1086 O OD2 . ASP A  1 136 ? 31.853 9.025   83.948  0.00 52.62  ? 151 ASP A OD2 1 
ATOM   1087 N N   . GLU A  1 137 ? 31.673 10.302  89.551  1.00 50.15  ? 152 GLU A N   1 
ATOM   1088 C CA  . GLU A  1 137 ? 31.993 10.020  90.979  1.00 47.27  ? 152 GLU A CA  1 
ATOM   1089 C C   . GLU A  1 137 ? 31.153 10.950  91.862  1.00 43.25  ? 152 GLU A C   1 
ATOM   1090 O O   . GLU A  1 137 ? 31.529 12.133  92.032  1.00 37.37  ? 152 GLU A O   1 
ATOM   1091 C CB  . GLU A  1 137 ? 33.485 10.206  91.252  1.00 51.12  ? 152 GLU A CB  1 
ATOM   1092 C CG  . GLU A  1 137 ? 34.344 9.046   90.777  1.00 57.46  ? 152 GLU A CG  1 
ATOM   1093 C CD  . GLU A  1 137 ? 35.842 9.201   91.020  1.00 62.18  ? 152 GLU A CD  1 
ATOM   1094 O OE1 . GLU A  1 137 ? 36.237 9.999   91.907  1.00 61.30  ? 152 GLU A OE1 1 
ATOM   1095 O OE2 . GLU A  1 137 ? 36.620 8.527   90.313  1.00 65.71  ? 152 GLU A OE2 1 
ATOM   1096 N N   . ARG A  1 138 ? 30.062 10.425  92.419  1.00 42.04  ? 153 ARG A N   1 
ATOM   1097 C CA  . ARG A  1 138 ? 29.120 11.185  93.286  1.00 46.53  ? 153 ARG A CA  1 
ATOM   1098 C C   . ARG A  1 138 ? 29.846 11.653  94.556  1.00 42.06  ? 153 ARG A C   1 
ATOM   1099 O O   . ARG A  1 138 ? 30.831 11.000  94.974  1.00 39.44  ? 153 ARG A O   1 
ATOM   1100 C CB  . ARG A  1 138 ? 27.876 10.351  93.626  1.00 51.06  ? 153 ARG A CB  1 
ATOM   1101 C CG  . ARG A  1 138 ? 26.994 10.033  92.425  1.00 56.77  ? 153 ARG A CG  1 
ATOM   1102 C CD  . ARG A  1 138 ? 25.645 9.450   92.797  1.00 61.58  ? 153 ARG A CD  1 
ATOM   1103 N NE  . ARG A  1 138 ? 24.636 10.483  93.006  1.00 68.56  ? 153 ARG A NE  1 
ATOM   1104 C CZ  . ARG A  1 138 ? 23.316 10.285  93.075  1.00 71.02  ? 153 ARG A CZ  1 
ATOM   1105 N NH1 . ARG A  1 138 ? 22.796 9.072   92.955  1.00 72.78  ? 153 ARG A NH1 1 
ATOM   1106 N NH2 . ARG A  1 138 ? 22.511 11.317  93.267  1.00 71.70  ? 153 ARG A NH2 1 
ATOM   1107 N N   . LEU A  1 139 ? 29.413 12.792  95.102  1.00 37.94  ? 154 LEU A N   1 
ATOM   1108 C CA  . LEU A  1 139 ? 29.790 13.264  96.459  1.00 37.82  ? 154 LEU A CA  1 
ATOM   1109 C C   . LEU A  1 139 ? 29.367 12.182  97.453  1.00 37.09  ? 154 LEU A C   1 
ATOM   1110 O O   . LEU A  1 139 ? 28.186 11.846  97.517  1.00 37.83  ? 154 LEU A O   1 
ATOM   1111 C CB  . LEU A  1 139 ? 29.090 14.597  96.756  1.00 37.83  ? 154 LEU A CB  1 
ATOM   1112 C CG  . LEU A  1 139 ? 29.447 15.276  98.077  1.00 38.44  ? 154 LEU A CG  1 
ATOM   1113 C CD1 . LEU A  1 139 ? 30.895 15.750  98.089  1.00 38.64  ? 154 LEU A CD1 1 
ATOM   1114 C CD2 . LEU A  1 139 ? 28.513 16.440  98.346  1.00 38.22  ? 154 LEU A CD2 1 
ATOM   1115 N N   . PRO A  1 140 ? 30.298 11.585  98.235  1.00 36.82  ? 155 PRO A N   1 
ATOM   1116 C CA  . PRO A  1 140 ? 29.923 10.582  99.231  1.00 36.79  ? 155 PRO A CA  1 
ATOM   1117 C C   . PRO A  1 140 ? 29.112 11.147  100.395 1.00 36.15  ? 155 PRO A C   1 
ATOM   1118 O O   . PRO A  1 140 ? 29.241 12.328  100.725 1.00 35.90  ? 155 PRO A O   1 
ATOM   1119 C CB  . PRO A  1 140 ? 31.258 10.044  99.773  1.00 35.94  ? 155 PRO A CB  1 
ATOM   1120 C CG  . PRO A  1 140 ? 32.319 10.555  98.823  1.00 37.35  ? 155 PRO A CG  1 
ATOM   1121 C CD  . PRO A  1 140 ? 31.751 11.810  98.196  1.00 37.04  ? 155 PRO A CD  1 
ATOM   1122 N N   . PRO A  1 141 ? 28.266 10.325  101.065 1.00 37.83  ? 156 PRO A N   1 
ATOM   1123 C CA  . PRO A  1 141 ? 27.678 10.715  102.346 1.00 36.90  ? 156 PRO A CA  1 
ATOM   1124 C C   . PRO A  1 141 ? 28.794 11.032  103.344 1.00 35.58  ? 156 PRO A C   1 
ATOM   1125 O O   . PRO A  1 141 ? 29.864 10.429  103.267 1.00 37.60  ? 156 PRO A O   1 
ATOM   1126 C CB  . PRO A  1 141 ? 26.841 9.507   102.806 1.00 37.58  ? 156 PRO A CB  1 
ATOM   1127 C CG  . PRO A  1 141 ? 26.752 8.578   101.610 1.00 36.92  ? 156 PRO A CG  1 
ATOM   1128 C CD  . PRO A  1 141 ? 27.837 8.985   100.635 1.00 38.08  ? 156 PRO A CD  1 
ATOM   1129 N N   . PRO A  1 142 ? 28.618 11.976  104.302 1.00 34.93  ? 157 PRO A N   1 
ATOM   1130 C CA  . PRO A  1 142 ? 27.347 12.669  104.539 1.00 34.45  ? 157 PRO A CA  1 
ATOM   1131 C C   . PRO A  1 142 ? 27.111 13.955  103.718 1.00 34.22  ? 157 PRO A C   1 
ATOM   1132 O O   . PRO A  1 142 ? 26.408 14.826  104.185 1.00 34.34  ? 157 PRO A O   1 
ATOM   1133 C CB  . PRO A  1 142 ? 27.487 12.975  106.037 1.00 34.23  ? 157 PRO A CB  1 
ATOM   1134 C CG  . PRO A  1 142 ? 28.948 13.340  106.191 1.00 34.47  ? 157 PRO A CG  1 
ATOM   1135 C CD  . PRO A  1 142 ? 29.673 12.422  105.229 1.00 35.36  ? 157 PRO A CD  1 
ATOM   1136 N N   . PHE A  1 143 ? 27.694 14.052  102.521 1.00 35.17  ? 158 PHE A N   1 
ATOM   1137 C CA  . PHE A  1 143 ? 27.373 15.082  101.495 1.00 34.28  ? 158 PHE A CA  1 
ATOM   1138 C C   . PHE A  1 143 ? 27.718 16.479  102.012 1.00 32.49  ? 158 PHE A C   1 
ATOM   1139 O O   . PHE A  1 143 ? 26.843 17.340  102.122 1.00 30.37  ? 158 PHE A O   1 
ATOM   1140 C CB  . PHE A  1 143 ? 25.895 15.003  101.104 1.00 33.13  ? 158 PHE A CB  1 
ATOM   1141 C CG  . PHE A  1 143 ? 25.373 13.620  100.817 1.00 33.30  ? 158 PHE A CG  1 
ATOM   1142 C CD1 . PHE A  1 143 ? 25.764 12.940  99.674  1.00 33.90  ? 158 PHE A CD1 1 
ATOM   1143 C CD2 . PHE A  1 143 ? 24.474 13.008  101.684 1.00 33.23  ? 158 PHE A CD2 1 
ATOM   1144 C CE1 . PHE A  1 143 ? 25.270 11.672  99.401  1.00 34.11  ? 158 PHE A CE1 1 
ATOM   1145 C CE2 . PHE A  1 143 ? 23.979 11.741  101.407 1.00 33.43  ? 158 PHE A CE2 1 
ATOM   1146 C CZ  . PHE A  1 143 ? 24.373 11.079  100.266 1.00 33.43  ? 158 PHE A CZ  1 
ATOM   1147 N N   . PRO A  1 144 ? 29.001 16.757  102.334 1.00 31.04  ? 159 PRO A N   1 
ATOM   1148 C CA  . PRO A  1 144 ? 29.391 18.080  102.814 1.00 32.89  ? 159 PRO A CA  1 
ATOM   1149 C C   . PRO A  1 144 ? 29.378 19.096  101.660 1.00 32.67  ? 159 PRO A C   1 
ATOM   1150 O O   . PRO A  1 144 ? 29.738 18.724  100.546 1.00 34.02  ? 159 PRO A O   1 
ATOM   1151 C CB  . PRO A  1 144 ? 30.813 17.854  103.348 1.00 32.75  ? 159 PRO A CB  1 
ATOM   1152 C CG  . PRO A  1 144 ? 31.349 16.735  102.469 1.00 32.67  ? 159 PRO A CG  1 
ATOM   1153 C CD  . PRO A  1 144 ? 30.148 15.837  102.235 1.00 32.70  ? 159 PRO A CD  1 
ATOM   1154 N N   . LEU A  1 145 ? 28.972 20.339  101.928 1.00 34.41  ? 160 LEU A N   1 
ATOM   1155 C CA  . LEU A  1 145 ? 29.122 21.455  100.954 1.00 34.05  ? 160 LEU A CA  1 
ATOM   1156 C C   . LEU A  1 145 ? 30.621 21.628  100.689 1.00 34.31  ? 160 LEU A C   1 
ATOM   1157 O O   . LEU A  1 145 ? 31.381 21.764  101.669 1.00 36.85  ? 160 LEU A O   1 
ATOM   1158 C CB  . LEU A  1 145 ? 28.485 22.742  101.491 1.00 35.11  ? 160 LEU A CB  1 
ATOM   1159 C CG  . LEU A  1 145 ? 28.680 23.988  100.619 1.00 35.52  ? 160 LEU A CG  1 
ATOM   1160 C CD1 . LEU A  1 145 ? 28.025 23.812  99.258  1.00 35.93  ? 160 LEU A CD1 1 
ATOM   1161 C CD2 . LEU A  1 145 ? 28.145 25.231  101.309 1.00 35.75  ? 160 LEU A CD2 1 
ATOM   1162 N N   . LYS A  1 146 ? 31.024 21.578  99.421  1.00 35.84  ? 161 LYS A N   1 
ATOM   1163 C CA  . LYS A  1 146 ? 32.447 21.696  99.013  1.00 35.29  ? 161 LYS A CA  1 
ATOM   1164 C C   . LYS A  1 146 ? 32.667 23.053  98.337  1.00 36.86  ? 161 LYS A C   1 
ATOM   1165 O O   . LYS A  1 146 ? 31.697 23.661  97.856  1.00 34.75  ? 161 LYS A O   1 
ATOM   1166 C CB  . LYS A  1 146 ? 32.876 20.526  98.126  1.00 37.29  ? 161 LYS A CB  1 
ATOM   1167 C CG  . LYS A  1 146 ? 32.738 19.147  98.760  1.00 40.34  ? 161 LYS A CG  1 
ATOM   1168 C CD  . LYS A  1 146 ? 33.659 18.110  98.184  1.00 44.75  ? 161 LYS A CD  1 
ATOM   1169 C CE  . LYS A  1 146 ? 35.042 18.165  98.789  1.00 49.27  ? 161 LYS A CE  1 
ATOM   1170 N NZ  . LYS A  1 146 ? 35.808 16.933  98.490  1.00 52.39  ? 161 LYS A NZ  1 
ATOM   1171 N N   . GLN A  1 147 ? 33.918 23.508  98.359  1.00 35.58  ? 162 GLN A N   1 
ATOM   1172 C CA  . GLN A  1 147 ? 34.398 24.792  97.806  1.00 34.79  ? 162 GLN A CA  1 
ATOM   1173 C C   . GLN A  1 147 ? 35.684 24.491  97.039  1.00 35.56  ? 162 GLN A C   1 
ATOM   1174 O O   . GLN A  1 147 ? 36.394 23.544  97.429  1.00 33.69  ? 162 GLN A O   1 
ATOM   1175 C CB  . GLN A  1 147 ? 34.634 25.803  98.935  1.00 35.44  ? 162 GLN A CB  1 
ATOM   1176 C CG  . GLN A  1 147 ? 35.654 25.339  99.974  1.00 36.01  ? 162 GLN A CG  1 
ATOM   1177 C CD  . GLN A  1 147 ? 36.013 26.376  101.013 1.00 36.65  ? 162 GLN A CD  1 
ATOM   1178 O OE1 . GLN A  1 147 ? 35.167 27.107  101.506 1.00 35.56  ? 162 GLN A OE1 1 
ATOM   1179 N NE2 . GLN A  1 147 ? 37.283 26.435  101.378 1.00 37.98  ? 162 GLN A NE2 1 
ATOM   1180 N N   . VAL A  1 148 ? 35.979 25.270  96.000  1.00 34.96  ? 163 VAL A N   1 
ATOM   1181 C CA  . VAL A  1 148 ? 37.314 25.249  95.344  1.00 36.15  ? 163 VAL A CA  1 
ATOM   1182 C C   . VAL A  1 148 ? 37.606 26.645  94.784  1.00 35.38  ? 163 VAL A C   1 
ATOM   1183 O O   . VAL A  1 148 ? 36.673 27.299  94.269  1.00 35.83  ? 163 VAL A O   1 
ATOM   1184 C CB  . VAL A  1 148 ? 37.409 24.126  94.292  1.00 36.24  ? 163 VAL A CB  1 
ATOM   1185 C CG1 . VAL A  1 148 ? 36.482 24.339  93.107  1.00 37.60  ? 163 VAL A CG1 1 
ATOM   1186 C CG2 . VAL A  1 148 ? 38.840 23.903  93.827  1.00 36.31  ? 163 VAL A CG2 1 
ATOM   1187 N N   . LYS A  1 149 ? 38.848 27.098  94.958  1.00 38.05  ? 164 LYS A N   1 
ATOM   1188 C CA  . LYS A  1 149 ? 39.387 28.336  94.347  1.00 37.94  ? 164 LYS A CA  1 
ATOM   1189 C C   . LYS A  1 149 ? 39.694 28.030  92.879  1.00 36.08  ? 164 LYS A C   1 
ATOM   1190 O O   . LYS A  1 149 ? 40.419 27.073  92.630  1.00 34.31  ? 164 LYS A O   1 
ATOM   1191 C CB  . LYS A  1 149 ? 40.630 28.819  95.103  1.00 39.70  ? 164 LYS A CB  1 
ATOM   1192 C CG  . LYS A  1 149 ? 41.160 30.192  94.701  1.00 41.37  ? 164 LYS A CG  1 
ATOM   1193 C CD  . LYS A  1 149 ? 42.597 30.445  95.138  1.00 43.92  ? 164 LYS A CD  1 
ATOM   1194 C CE  . LYS A  1 149 ? 42.735 30.705  96.622  1.00 45.85  ? 164 LYS A CE  1 
ATOM   1195 N NZ  . LYS A  1 149 ? 44.117 30.988  97.022  0.00 45.08  ? 164 LYS A NZ  1 
ATOM   1196 N N   . VAL A  1 150 ? 39.153 28.818  91.951  1.00 36.52  ? 165 VAL A N   1 
ATOM   1197 C CA  . VAL A  1 150 ? 39.373 28.670  90.481  1.00 36.85  ? 165 VAL A CA  1 
ATOM   1198 C C   . VAL A  1 150 ? 39.748 30.038  89.915  1.00 38.88  ? 165 VAL A C   1 
ATOM   1199 O O   . VAL A  1 150 ? 39.094 31.037  90.211  1.00 39.40  ? 165 VAL A O   1 
ATOM   1200 C CB  . VAL A  1 150 ? 38.149 28.060  89.767  1.00 37.27  ? 165 VAL A CB  1 
ATOM   1201 C CG1 . VAL A  1 150 ? 38.009 26.575  90.073  1.00 38.11  ? 165 VAL A CG1 1 
ATOM   1202 C CG2 . VAL A  1 150 ? 36.842 28.783  90.074  1.00 37.10  ? 165 VAL A CG2 1 
ATOM   1203 N N   . PRO A  1 151 ? 40.818 30.138  89.098  1.00 43.53  ? 166 PRO A N   1 
ATOM   1204 C CA  . PRO A  1 151 ? 41.161 31.401  88.446  1.00 45.27  ? 166 PRO A CA  1 
ATOM   1205 C C   . PRO A  1 151 ? 40.201 31.673  87.278  1.00 44.26  ? 166 PRO A C   1 
ATOM   1206 O O   . PRO A  1 151 ? 39.987 30.779  86.473  1.00 43.23  ? 166 PRO A O   1 
ATOM   1207 C CB  . PRO A  1 151 ? 42.591 31.172  87.948  1.00 47.53  ? 166 PRO A CB  1 
ATOM   1208 C CG  . PRO A  1 151 ? 42.653 29.676  87.694  1.00 49.53  ? 166 PRO A CG  1 
ATOM   1209 C CD  . PRO A  1 151 ? 41.751 29.057  88.742  1.00 45.71  ? 166 PRO A CD  1 
ATOM   1210 N N   . ILE A  1 152 ? 39.662 32.892  87.204  1.00 44.65  ? 167 ILE A N   1 
ATOM   1211 C CA  . ILE A  1 152 ? 38.941 33.393  85.999  1.00 44.65  ? 167 ILE A CA  1 
ATOM   1212 C C   . ILE A  1 152 ? 39.940 33.455  84.840  1.00 44.02  ? 167 ILE A C   1 
ATOM   1213 O O   . ILE A  1 152 ? 41.105 33.815  85.054  1.00 43.83  ? 167 ILE A O   1 
ATOM   1214 C CB  . ILE A  1 152 ? 38.226 34.734  86.264  1.00 46.55  ? 167 ILE A CB  1 
ATOM   1215 C CG1 . ILE A  1 152 ? 36.881 34.471  86.946  1.00 47.02  ? 167 ILE A CG1 1 
ATOM   1216 C CG2 . ILE A  1 152 ? 38.057 35.548  84.983  1.00 48.25  ? 167 ILE A CG2 1 
ATOM   1217 C CD1 . ILE A  1 152 ? 36.083 35.710  87.263  1.00 49.48  ? 167 ILE A CD1 1 
ATOM   1218 N N   . MET A  1 153 ? 39.480 33.051  83.665  1.00 44.73  ? 168 MET A N   1 
ATOM   1219 C CA  A MET A  1 153 ? 40.289 33.030  82.422  0.50 46.36  ? 168 MET A CA  1 
ATOM   1220 C CA  B MET A  1 153 ? 40.272 32.989  82.409  0.50 46.72  ? 168 MET A CA  1 
ATOM   1221 C C   . MET A  1 153 ? 39.522 33.801  81.345  1.00 44.76  ? 168 MET A C   1 
ATOM   1222 O O   . MET A  1 153 ? 38.269 33.773  81.371  1.00 45.60  ? 168 MET A O   1 
ATOM   1223 C CB  A MET A  1 153 ? 40.579 31.591  81.987  0.50 47.10  ? 168 MET A CB  1 
ATOM   1224 C CB  B MET A  1 153 ? 40.430 31.521  81.991  0.50 47.91  ? 168 MET A CB  1 
ATOM   1225 C CG  A MET A  1 153 ? 41.476 30.852  82.982  0.50 47.11  ? 168 MET A CG  1 
ATOM   1226 C CG  B MET A  1 153 ? 40.857 31.269  80.553  0.50 49.28  ? 168 MET A CG  1 
ATOM   1227 S SD  A MET A  1 153 ? 42.381 29.457  82.283  0.50 49.07  ? 168 MET A SD  1 
ATOM   1228 S SD  B MET A  1 153 ? 40.844 29.492  80.182  0.50 49.18  ? 168 MET A SD  1 
ATOM   1229 C CE  A MET A  1 153 ? 41.019 28.454  81.689  0.50 50.73  ? 168 MET A CE  1 
ATOM   1230 C CE  B MET A  1 153 ? 41.751 28.870  81.598  0.50 52.40  ? 168 MET A CE  1 
ATOM   1231 N N   . GLU A  1 154 ? 40.260 34.500  80.481  1.00 44.75  ? 169 GLU A N   1 
ATOM   1232 C CA  . GLU A  1 154 ? 39.696 35.342  79.389  1.00 45.83  ? 169 GLU A CA  1 
ATOM   1233 C C   . GLU A  1 154 ? 38.852 34.454  78.465  1.00 41.67  ? 169 GLU A C   1 
ATOM   1234 O O   . GLU A  1 154 ? 39.264 33.312  78.209  1.00 39.43  ? 169 GLU A O   1 
ATOM   1235 C CB  . GLU A  1 154 ? 40.817 36.041  78.617  1.00 50.53  ? 169 GLU A CB  1 
ATOM   1236 C CG  . GLU A  1 154 ? 40.355 37.199  77.755  1.00 55.52  ? 169 GLU A CG  1 
ATOM   1237 C CD  . GLU A  1 154 ? 41.452 37.738  76.856  1.00 59.93  ? 169 GLU A CD  1 
ATOM   1238 O OE1 . GLU A  1 154 ? 41.954 36.963  76.022  1.00 64.55  ? 169 GLU A OE1 1 
ATOM   1239 O OE2 . GLU A  1 154 ? 41.826 38.916  77.014  1.00 65.55  ? 169 GLU A OE2 1 
ATOM   1240 N N   . ASN A  1 155 ? 37.707 34.960  78.002  1.00 41.43  ? 170 ASN A N   1 
ATOM   1241 C CA  . ASN A  1 155 ? 36.789 34.229  77.085  1.00 41.33  ? 170 ASN A CA  1 
ATOM   1242 C C   . ASN A  1 155 ? 37.532 33.768  75.834  1.00 41.14  ? 170 ASN A C   1 
ATOM   1243 O O   . ASN A  1 155 ? 37.310 32.624  75.423  1.00 41.00  ? 170 ASN A O   1 
ATOM   1244 C CB  . ASN A  1 155 ? 35.556 35.049  76.701  1.00 41.94  ? 170 ASN A CB  1 
ATOM   1245 C CG  . ASN A  1 155 ? 34.392 34.780  77.623  1.00 43.38  ? 170 ASN A CG  1 
ATOM   1246 O OD1 . ASN A  1 155 ? 34.584 34.386  78.777  1.00 49.66  ? 170 ASN A OD1 1 
ATOM   1247 N ND2 . ASN A  1 155 ? 33.184 34.992  77.133  1.00 39.36  ? 170 ASN A ND2 1 
ATOM   1248 N N   . HIS A  1 156 ? 38.390 34.614  75.266  1.00 41.76  ? 171 HIS A N   1 
ATOM   1249 C CA  . HIS A  1 156 ? 39.140 34.308  74.025  1.00 42.94  ? 171 HIS A CA  1 
ATOM   1250 C C   . HIS A  1 156 ? 40.089 33.121  74.266  1.00 41.19  ? 171 HIS A C   1 
ATOM   1251 O O   . HIS A  1 156 ? 40.125 32.241  73.397  1.00 40.31  ? 171 HIS A O   1 
ATOM   1252 C CB  . HIS A  1 156 ? 39.833 35.569  73.491  1.00 46.31  ? 171 HIS A CB  1 
ATOM   1253 C CG  . HIS A  1 156 ? 40.625 35.340  72.252  1.00 49.24  ? 171 HIS A CG  1 
ATOM   1254 N ND1 . HIS A  1 156 ? 40.118 35.598  70.996  1.00 52.55  ? 171 HIS A ND1 1 
ATOM   1255 C CD2 . HIS A  1 156 ? 41.887 34.897  72.066  1.00 51.63  ? 171 HIS A CD2 1 
ATOM   1256 C CE1 . HIS A  1 156 ? 41.028 35.314  70.090  1.00 51.98  ? 171 HIS A CE1 1 
ATOM   1257 N NE2 . HIS A  1 156 ? 42.121 34.878  70.720  1.00 51.58  ? 171 HIS A NE2 1 
ATOM   1258 N N   . ILE A  1 157 ? 40.759 33.060  75.423  1.00 38.95  ? 172 ILE A N   1 
ATOM   1259 C CA  . ILE A  1 157 ? 41.689 31.952  75.804  1.00 39.64  ? 172 ILE A CA  1 
ATOM   1260 C C   . ILE A  1 157 ? 40.898 30.650  75.984  1.00 38.78  ? 172 ILE A C   1 
ATOM   1261 O O   . ILE A  1 157 ? 41.386 29.592  75.555  1.00 40.46  ? 172 ILE A O   1 
ATOM   1262 C CB  . ILE A  1 157 ? 42.474 32.322  77.079  1.00 40.50  ? 172 ILE A CB  1 
ATOM   1263 C CG1 . ILE A  1 157 ? 43.410 33.513  76.842  1.00 42.91  ? 172 ILE A CG1 1 
ATOM   1264 C CG2 . ILE A  1 157 ? 43.225 31.125  77.651  1.00 39.83  ? 172 ILE A CG2 1 
ATOM   1265 C CD1 . ILE A  1 157 ? 44.445 33.310  75.744  1.00 44.34  ? 172 ILE A CD1 1 
ATOM   1266 N N   . CYS A  1 158 ? 39.750 30.728  76.642  1.00 38.78  ? 173 CYS A N   1 
ATOM   1267 C CA  A CYS A  1 158 ? 38.877 29.563  76.957  0.50 39.75  ? 173 CYS A CA  1 
ATOM   1268 C CA  B CYS A  1 158 ? 38.899 29.549  76.948  0.50 40.56  ? 173 CYS A CA  1 
ATOM   1269 C C   . CYS A  1 158 ? 38.260 29.015  75.663  1.00 37.90  ? 173 CYS A C   1 
ATOM   1270 O O   . CYS A  1 158 ? 38.221 27.774  75.508  1.00 35.94  ? 173 CYS A O   1 
ATOM   1271 C CB  A CYS A  1 158 ? 37.814 29.966  77.973  0.50 41.34  ? 173 CYS A CB  1 
ATOM   1272 C CB  B CYS A  1 158 ? 37.880 29.894  78.018  0.50 43.03  ? 173 CYS A CB  1 
ATOM   1273 S SG  A CYS A  1 158 ? 36.641 28.657  78.410  0.50 43.17  ? 173 CYS A SG  1 
ATOM   1274 S SG  B CYS A  1 158 ? 38.676 30.024  79.639  0.50 47.37  ? 173 CYS A SG  1 
ATOM   1275 N N   . ASP A  1 159 ? 37.813 29.912  74.779  1.00 35.23  ? 174 ASP A N   1 
ATOM   1276 C CA  . ASP A  1 159 ? 37.313 29.555  73.423  1.00 36.53  ? 174 ASP A CA  1 
ATOM   1277 C C   . ASP A  1 159 ? 38.408 28.790  72.668  1.00 36.24  ? 174 ASP A C   1 
ATOM   1278 O O   . ASP A  1 159 ? 38.101 27.721  72.132  1.00 38.20  ? 174 ASP A O   1 
ATOM   1279 C CB  . ASP A  1 159 ? 36.873 30.787  72.632  1.00 38.48  ? 174 ASP A CB  1 
ATOM   1280 C CG  . ASP A  1 159 ? 36.125 30.449  71.357  1.00 38.87  ? 174 ASP A CG  1 
ATOM   1281 O OD1 . ASP A  1 159 ? 35.136 29.702  71.439  1.00 40.06  ? 174 ASP A OD1 1 
ATOM   1282 O OD2 . ASP A  1 159 ? 36.554 30.916  70.293  1.00 44.38  ? 174 ASP A OD2 1 
ATOM   1283 N N   . ALA A  1 160 ? 39.645 29.299  72.681  1.00 35.21  ? 175 ALA A N   1 
ATOM   1284 C CA  . ALA A  1 160 ? 40.820 28.686  72.024  1.00 36.50  ? 175 ALA A CA  1 
ATOM   1285 C C   . ALA A  1 160 ? 41.077 27.284  72.592  1.00 37.10  ? 175 ALA A C   1 
ATOM   1286 O O   . ALA A  1 160 ? 41.345 26.378  71.787  1.00 39.68  ? 175 ALA A O   1 
ATOM   1287 C CB  . ALA A  1 160 ? 42.028 29.582  72.160  1.00 36.85  ? 175 ALA A CB  1 
ATOM   1288 N N   . LYS A  1 161 ? 40.988 27.096  73.916  1.00 37.74  ? 176 LYS A N   1 
ATOM   1289 C CA  . LYS A  1 161 ? 41.209 25.778  74.572  1.00 38.10  ? 176 LYS A CA  1 
ATOM   1290 C C   . LYS A  1 161 ? 40.167 24.762  74.072  1.00 37.43  ? 176 LYS A C   1 
ATOM   1291 O O   . LYS A  1 161 ? 40.568 23.625  73.763  1.00 36.96  ? 176 LYS A O   1 
ATOM   1292 C CB  . LYS A  1 161 ? 41.176 25.894  76.100  1.00 39.72  ? 176 LYS A CB  1 
ATOM   1293 C CG  . LYS A  1 161 ? 42.409 26.515  76.732  1.00 42.15  ? 176 LYS A CG  1 
ATOM   1294 C CD  . LYS A  1 161 ? 42.299 26.593  78.237  1.00 44.20  ? 176 LYS A CD  1 
ATOM   1295 C CE  . LYS A  1 161 ? 43.420 27.370  78.892  1.00 47.74  ? 176 LYS A CE  1 
ATOM   1296 N NZ  . LYS A  1 161 ? 44.747 26.767  78.629  1.00 51.45  ? 176 LYS A NZ  1 
ATOM   1297 N N   . TYR A  1 162 ? 38.891 25.150  73.963  1.00 33.42  ? 177 TYR A N   1 
ATOM   1298 C CA  . TYR A  1 162 ? 37.791 24.247  73.524  1.00 34.48  ? 177 TYR A CA  1 
ATOM   1299 C C   . TYR A  1 162 ? 37.979 23.813  72.062  1.00 34.29  ? 177 TYR A C   1 
ATOM   1300 O O   . TYR A  1 162 ? 37.386 22.781  71.687  1.00 34.62  ? 177 TYR A O   1 
ATOM   1301 C CB  . TYR A  1 162 ? 36.417 24.875  73.785  1.00 32.99  ? 177 TYR A CB  1 
ATOM   1302 C CG  . TYR A  1 162 ? 35.831 24.425  75.091  1.00 31.71  ? 177 TYR A CG  1 
ATOM   1303 C CD1 . TYR A  1 162 ? 36.237 25.005  76.282  1.00 32.23  ? 177 TYR A CD1 1 
ATOM   1304 C CD2 . TYR A  1 162 ? 34.932 23.373  75.151  1.00 32.98  ? 177 TYR A CD2 1 
ATOM   1305 C CE1 . TYR A  1 162 ? 35.728 24.583  77.497  1.00 32.74  ? 177 TYR A CE1 1 
ATOM   1306 C CE2 . TYR A  1 162 ? 34.408 22.939  76.361  1.00 32.77  ? 177 TYR A CE2 1 
ATOM   1307 C CZ  . TYR A  1 162 ? 34.810 23.547  77.539  1.00 34.12  ? 177 TYR A CZ  1 
ATOM   1308 O OH  . TYR A  1 162 ? 34.331 23.128  78.747  1.00 35.28  ? 177 TYR A OH  1 
ATOM   1309 N N   . HIS A  1 163 ? 38.763 24.560  71.273  1.00 36.14  ? 178 HIS A N   1 
ATOM   1310 C CA  . HIS A  1 163 ? 39.111 24.244  69.863  1.00 35.63  ? 178 HIS A CA  1 
ATOM   1311 C C   . HIS A  1 163 ? 40.290 23.264  69.769  1.00 37.38  ? 178 HIS A C   1 
ATOM   1312 O O   . HIS A  1 163 ? 40.375 22.583  68.737  1.00 38.56  ? 178 HIS A O   1 
ATOM   1313 C CB  . HIS A  1 163 ? 39.374 25.529  69.072  1.00 35.87  ? 178 HIS A CB  1 
ATOM   1314 C CG  . HIS A  1 163 ? 38.132 26.278  68.736  1.00 35.01  ? 178 HIS A CG  1 
ATOM   1315 N ND1 . HIS A  1 163 ? 37.564 27.195  69.588  1.00 35.65  ? 178 HIS A ND1 1 
ATOM   1316 C CD2 . HIS A  1 163 ? 37.336 26.234  67.656  1.00 34.39  ? 178 HIS A CD2 1 
ATOM   1317 C CE1 . HIS A  1 163 ? 36.490 27.700  69.035  1.00 35.24  ? 178 HIS A CE1 1 
ATOM   1318 N NE2 . HIS A  1 163 ? 36.332 27.129  67.851  1.00 35.83  ? 178 HIS A NE2 1 
ATOM   1319 N N   . LEU A  1 164 ? 41.159 23.182  70.780  1.00 37.94  ? 179 LEU A N   1 
ATOM   1320 C CA  . LEU A  1 164 ? 42.288 22.209  70.806  1.00 39.16  ? 179 LEU A CA  1 
ATOM   1321 C C   . LEU A  1 164 ? 41.721 20.788  70.929  1.00 37.10  ? 179 LEU A C   1 
ATOM   1322 O O   . LEU A  1 164 ? 40.931 20.556  71.845  1.00 35.14  ? 179 LEU A O   1 
ATOM   1323 C CB  . LEU A  1 164 ? 43.238 22.529  71.965  1.00 40.85  ? 179 LEU A CB  1 
ATOM   1324 C CG  . LEU A  1 164 ? 44.032 23.829  71.824  1.00 44.81  ? 179 LEU A CG  1 
ATOM   1325 C CD1 . LEU A  1 164 ? 44.711 24.196  73.134  1.00 45.91  ? 179 LEU A CD1 1 
ATOM   1326 C CD2 . LEU A  1 164 ? 45.070 23.719  70.714  1.00 44.15  ? 179 LEU A CD2 1 
ATOM   1327 N N   . GLY A  1 165 ? 42.102 19.889  70.016  1.00 37.11  ? 180 GLY A N   1 
ATOM   1328 C CA  . GLY A  1 165 ? 41.606 18.501  69.954  1.00 36.29  ? 180 GLY A CA  1 
ATOM   1329 C C   . GLY A  1 165 ? 40.156 18.426  69.507  1.00 36.18  ? 180 GLY A C   1 
ATOM   1330 O O   . GLY A  1 165 ? 39.496 17.429  69.844  1.00 38.30  ? 180 GLY A O   1 
ATOM   1331 N N   . ALA A  1 166 ? 39.681 19.433  68.767  1.00 35.74  ? 181 ALA A N   1 
ATOM   1332 C CA  . ALA A  1 166 ? 38.305 19.522  68.230  1.00 36.00  ? 181 ALA A CA  1 
ATOM   1333 C C   . ALA A  1 166 ? 38.351 19.787  66.722  1.00 35.60  ? 181 ALA A C   1 
ATOM   1334 O O   . ALA A  1 166 ? 39.321 20.399  66.245  1.00 36.03  ? 181 ALA A O   1 
ATOM   1335 C CB  . ALA A  1 166 ? 37.529 20.598  68.949  1.00 34.45  ? 181 ALA A CB  1 
ATOM   1336 N N   . TYR A  1 167 ? 37.314 19.355  66.006  1.00 35.41  ? 182 TYR A N   1 
ATOM   1337 C CA  . TYR A  1 167 ? 37.141 19.586  64.546  1.00 35.30  ? 182 TYR A CA  1 
ATOM   1338 C C   . TYR A  1 167 ? 36.608 21.003  64.290  1.00 35.31  ? 182 TYR A C   1 
ATOM   1339 O O   . TYR A  1 167 ? 36.766 21.480  63.166  1.00 35.67  ? 182 TYR A O   1 
ATOM   1340 C CB  . TYR A  1 167 ? 36.203 18.544  63.938  1.00 35.29  ? 182 TYR A CB  1 
ATOM   1341 C CG  . TYR A  1 167 ? 36.743 17.135  63.967  1.00 37.45  ? 182 TYR A CG  1 
ATOM   1342 C CD1 . TYR A  1 167 ? 37.773 16.745  63.118  1.00 38.11  ? 182 TYR A CD1 1 
ATOM   1343 C CD2 . TYR A  1 167 ? 36.226 16.186  64.836  1.00 36.10  ? 182 TYR A CD2 1 
ATOM   1344 C CE1 . TYR A  1 167 ? 38.265 15.448  63.126  1.00 37.91  ? 182 TYR A CE1 1 
ATOM   1345 C CE2 . TYR A  1 167 ? 36.708 14.886  64.856  1.00 35.73  ? 182 TYR A CE2 1 
ATOM   1346 C CZ  . TYR A  1 167 ? 37.732 14.515  64.001  1.00 37.79  ? 182 TYR A CZ  1 
ATOM   1347 O OH  . TYR A  1 167 ? 38.226 13.241  64.046  1.00 40.78  ? 182 TYR A OH  1 
ATOM   1348 N N   . THR A  1 168 ? 35.970 21.630  65.287  1.00 37.23  ? 183 THR A N   1 
ATOM   1349 C CA  . THR A  1 168 ? 35.313 22.957  65.175  1.00 35.69  ? 183 THR A CA  1 
ATOM   1350 C C   . THR A  1 168 ? 36.333 23.967  64.644  1.00 36.20  ? 183 THR A C   1 
ATOM   1351 O O   . THR A  1 168 ? 37.462 24.004  65.183  1.00 34.74  ? 183 THR A O   1 
ATOM   1352 C CB  . THR A  1 168 ? 34.711 23.409  66.512  1.00 35.06  ? 183 THR A CB  1 
ATOM   1353 O OG1 . THR A  1 168 ? 33.999 22.328  67.119  1.00 34.78  ? 183 THR A OG1 1 
ATOM   1354 C CG2 . THR A  1 168 ? 33.769 24.582  66.350  1.00 33.77  ? 183 THR A CG2 1 
ATOM   1355 N N   . GLY A  1 169 ? 35.951 24.727  63.611  1.00 37.41  ? 184 GLY A N   1 
ATOM   1356 C CA  . GLY A  1 169 ? 36.777 25.793  63.016  1.00 37.86  ? 184 GLY A CA  1 
ATOM   1357 C C   . GLY A  1 169 ? 37.143 26.828  64.058  1.00 37.12  ? 184 GLY A C   1 
ATOM   1358 O O   . GLY A  1 169 ? 36.264 27.178  64.858  1.00 40.19  ? 184 GLY A O   1 
ATOM   1359 N N   . ASP A  1 170 ? 38.393 27.293  64.060  1.00 38.90  ? 185 ASP A N   1 
ATOM   1360 C CA  . ASP A  1 170 ? 38.949 28.249  65.062  1.00 43.39  ? 185 ASP A CA  1 
ATOM   1361 C C   . ASP A  1 170 ? 38.132 29.553  65.099  1.00 43.32  ? 185 ASP A C   1 
ATOM   1362 O O   . ASP A  1 170 ? 38.058 30.155  66.178  1.00 46.94  ? 185 ASP A O   1 
ATOM   1363 C CB  . ASP A  1 170 ? 40.429 28.538  64.788  1.00 45.49  ? 185 ASP A CB  1 
ATOM   1364 C CG  . ASP A  1 170 ? 41.365 27.384  65.109  1.00 49.40  ? 185 ASP A CG  1 
ATOM   1365 O OD1 . ASP A  1 170 ? 40.969 26.488  65.891  1.00 50.36  ? 185 ASP A OD1 1 
ATOM   1366 O OD2 . ASP A  1 170 ? 42.493 27.391  64.575  1.00 57.12  ? 185 ASP A OD2 1 
ATOM   1367 N N   . ASP A  1 171 ? 37.530 29.961  63.975  1.00 43.38  ? 186 ASP A N   1 
ATOM   1368 C CA  . ASP A  1 171 ? 36.703 31.191  63.815  1.00 45.89  ? 186 ASP A CA  1 
ATOM   1369 C C   . ASP A  1 171 ? 35.244 30.962  64.247  1.00 42.59  ? 186 ASP A C   1 
ATOM   1370 O O   . ASP A  1 171 ? 34.474 31.926  64.195  1.00 42.17  ? 186 ASP A O   1 
ATOM   1371 C CB  . ASP A  1 171 ? 36.733 31.692  62.366  1.00 51.39  ? 186 ASP A CB  1 
ATOM   1372 C CG  . ASP A  1 171 ? 36.086 30.734  61.373  1.00 56.25  ? 186 ASP A CG  1 
ATOM   1373 O OD1 . ASP A  1 171 ? 36.307 29.509  61.508  1.00 56.36  ? 186 ASP A OD1 1 
ATOM   1374 O OD2 . ASP A  1 171 ? 35.343 31.211  60.493  1.00 66.98  ? 186 ASP A OD2 1 
ATOM   1375 N N   . VAL A  1 172 ? 34.864 29.738  64.620  1.00 42.56  ? 187 VAL A N   1 
ATOM   1376 C CA  . VAL A  1 172 ? 33.479 29.379  65.056  1.00 40.69  ? 187 VAL A CA  1 
ATOM   1377 C C   . VAL A  1 172 ? 33.467 29.409  66.581  1.00 40.51  ? 187 VAL A C   1 
ATOM   1378 O O   . VAL A  1 172 ? 34.145 28.571  67.192  1.00 41.26  ? 187 VAL A O   1 
ATOM   1379 C CB  . VAL A  1 172 ? 33.043 28.007  64.503  1.00 39.45  ? 187 VAL A CB  1 
ATOM   1380 C CG1 . VAL A  1 172 ? 31.642 27.605  64.951  1.00 39.75  ? 187 VAL A CG1 1 
ATOM   1381 C CG2 . VAL A  1 172 ? 33.155 27.978  62.992  1.00 39.32  ? 187 VAL A CG2 1 
ATOM   1382 N N   . ARG A  1 173 ? 32.704 30.330  67.162  1.00 40.74  ? 188 ARG A N   1 
ATOM   1383 C CA  . ARG A  1 173 ? 32.685 30.576  68.625  1.00 42.82  ? 188 ARG A CA  1 
ATOM   1384 C C   . ARG A  1 173 ? 32.048 29.377  69.335  1.00 39.53  ? 188 ARG A C   1 
ATOM   1385 O O   . ARG A  1 173 ? 30.976 28.921  68.885  1.00 35.60  ? 188 ARG A O   1 
ATOM   1386 C CB  . ARG A  1 173 ? 31.939 31.875  68.943  1.00 47.28  ? 188 ARG A CB  1 
ATOM   1387 C CG  . ARG A  1 173 ? 32.288 32.471  70.297  1.00 54.93  ? 188 ARG A CG  1 
ATOM   1388 C CD  . ARG A  1 173 ? 33.688 33.073  70.351  1.00 58.19  ? 188 ARG A CD  1 
ATOM   1389 N NE  . ARG A  1 173 ? 33.875 34.236  69.500  1.00 63.35  ? 188 ARG A NE  1 
ATOM   1390 C CZ  . ARG A  1 173 ? 33.455 35.475  69.770  1.00 68.64  ? 188 ARG A CZ  1 
ATOM   1391 N NH1 . ARG A  1 173 ? 32.768 35.742  70.871  1.00 69.14  ? 188 ARG A NH1 1 
ATOM   1392 N NH2 . ARG A  1 173 ? 33.714 36.453  68.914  1.00 70.92  ? 188 ARG A NH2 1 
ATOM   1393 N N   . ILE A  1 174 ? 32.725 28.845  70.357  1.00 37.99  ? 189 ILE A N   1 
ATOM   1394 C CA  . ILE A  1 174 ? 32.177 27.813  71.285  1.00 36.79  ? 189 ILE A CA  1 
ATOM   1395 C C   . ILE A  1 174 ? 31.770 28.524  72.579  1.00 35.83  ? 189 ILE A C   1 
ATOM   1396 O O   . ILE A  1 174 ? 30.600 28.408  72.984  1.00 35.94  ? 189 ILE A O   1 
ATOM   1397 C CB  . ILE A  1 174 ? 33.190 26.672  71.501  1.00 35.94  ? 189 ILE A CB  1 
ATOM   1398 C CG1 . ILE A  1 174 ? 33.397 25.877  70.209  1.00 35.52  ? 189 ILE A CG1 1 
ATOM   1399 C CG2 . ILE A  1 174 ? 32.761 25.769  72.651  1.00 36.62  ? 189 ILE A CG2 1 
ATOM   1400 C CD1 . ILE A  1 174 ? 34.637 25.009  70.201  1.00 35.38  ? 189 ILE A CD1 1 
ATOM   1401 N N   . VAL A  1 175 ? 32.713 29.229  73.202  1.00 36.44  ? 190 VAL A N   1 
ATOM   1402 C CA  . VAL A  1 175 ? 32.492 30.036  74.436  1.00 36.23  ? 190 VAL A CA  1 
ATOM   1403 C C   . VAL A  1 175 ? 32.024 31.424  73.994  1.00 36.27  ? 190 VAL A C   1 
ATOM   1404 O O   . VAL A  1 175 ? 32.832 32.152  73.410  1.00 38.55  ? 190 VAL A O   1 
ATOM   1405 C CB  . VAL A  1 175 ? 33.761 30.109  75.307  1.00 36.27  ? 190 VAL A CB  1 
ATOM   1406 C CG1 . VAL A  1 175 ? 33.496 30.880  76.590  1.00 35.35  ? 190 VAL A CG1 1 
ATOM   1407 C CG2 . VAL A  1 175 ? 34.322 28.727  75.610  1.00 36.12  ? 190 VAL A CG2 1 
ATOM   1408 N N   . ARG A  1 176 ? 30.776 31.777  74.292  1.00 35.71  ? 191 ARG A N   1 
ATOM   1409 C CA  . ARG A  1 176 ? 30.105 32.991  73.759  1.00 38.32  ? 191 ARG A CA  1 
ATOM   1410 C C   . ARG A  1 176 ? 30.255 34.143  74.761  1.00 37.63  ? 191 ARG A C   1 
ATOM   1411 O O   . ARG A  1 176 ? 30.763 33.899  75.869  1.00 34.62  ? 191 ARG A O   1 
ATOM   1412 C CB  . ARG A  1 176 ? 28.656 32.635  73.418  1.00 39.05  ? 191 ARG A CB  1 
ATOM   1413 C CG  . ARG A  1 176 ? 28.541 31.486  72.427  1.00 43.38  ? 191 ARG A CG  1 
ATOM   1414 C CD  . ARG A  1 176 ? 27.154 31.459  71.810  1.00 49.01  ? 191 ARG A CD  1 
ATOM   1415 N NE  . ARG A  1 176 ? 26.643 30.370  70.971  1.00 52.73  ? 191 ARG A NE  1 
ATOM   1416 C CZ  . ARG A  1 176 ? 27.330 29.495  70.233  1.00 57.69  ? 191 ARG A CZ  1 
ATOM   1417 N NH1 . ARG A  1 176 ? 28.651 29.484  70.189  1.00 63.02  ? 191 ARG A NH1 1 
ATOM   1418 N NH2 . ARG A  1 176 ? 26.665 28.606  69.515  1.00 62.57  ? 191 ARG A NH2 1 
ATOM   1419 N N   . ASP A  1 177 ? 29.836 35.354  74.371  1.00 37.48  ? 192 ASP A N   1 
ATOM   1420 C CA  . ASP A  1 177 ? 30.071 36.611  75.129  1.00 37.82  ? 192 ASP A CA  1 
ATOM   1421 C C   . ASP A  1 177 ? 29.218 36.662  76.402  1.00 35.90  ? 192 ASP A C   1 
ATOM   1422 O O   . ASP A  1 177 ? 29.624 37.372  77.334  1.00 36.97  ? 192 ASP A O   1 
ATOM   1423 C CB  . ASP A  1 177 ? 29.854 37.819  74.212  1.00 40.18  ? 192 ASP A CB  1 
ATOM   1424 C CG  . ASP A  1 177 ? 30.895 37.909  73.107  1.00 42.02  ? 192 ASP A CG  1 
ATOM   1425 O OD1 . ASP A  1 177 ? 31.997 37.365  73.289  1.00 43.21  ? 192 ASP A OD1 1 
ATOM   1426 O OD2 . ASP A  1 177 ? 30.598 38.515  72.067  1.00 46.15  ? 192 ASP A OD2 1 
ATOM   1427 N N   . ASP A  1 178 ? 28.106 35.926  76.462  1.00 34.28  ? 193 ASP A N   1 
ATOM   1428 C CA  . ASP A  1 178 ? 27.254 35.826  77.682  1.00 33.85  ? 193 ASP A CA  1 
ATOM   1429 C C   . ASP A  1 178 ? 27.769 34.720  78.621  1.00 33.32  ? 193 ASP A C   1 
ATOM   1430 O O   . ASP A  1 178 ? 27.051 34.390  79.578  1.00 32.76  ? 193 ASP A O   1 
ATOM   1431 C CB  . ASP A  1 178 ? 25.785 35.601  77.323  1.00 33.53  ? 193 ASP A CB  1 
ATOM   1432 C CG  . ASP A  1 178 ? 25.491 34.266  76.654  1.00 33.87  ? 193 ASP A CG  1 
ATOM   1433 O OD1 . ASP A  1 178 ? 26.398 33.711  75.999  1.00 32.17  ? 193 ASP A OD1 1 
ATOM   1434 O OD2 . ASP A  1 178 ? 24.335 33.819  76.735  1.00 34.52  ? 193 ASP A OD2 1 
ATOM   1435 N N   . MET A  1 179 ? 28.959 34.171  78.369  1.00 33.37  ? 194 MET A N   1 
ATOM   1436 C CA  . MET A  1 179 ? 29.568 33.092  79.185  1.00 33.09  ? 194 MET A CA  1 
ATOM   1437 C C   . MET A  1 179 ? 30.882 33.591  79.791  1.00 36.15  ? 194 MET A C   1 
ATOM   1438 O O   . MET A  1 179 ? 31.474 34.563  79.276  1.00 37.31  ? 194 MET A O   1 
ATOM   1439 C CB  . MET A  1 179 ? 29.830 31.836  78.353  1.00 32.15  ? 194 MET A CB  1 
ATOM   1440 C CG  . MET A  1 179 ? 28.560 31.243  77.784  1.00 33.23  ? 194 MET A CG  1 
ATOM   1441 S SD  . MET A  1 179 ? 28.846 29.966  76.550  1.00 33.70  ? 194 MET A SD  1 
ATOM   1442 C CE  . MET A  1 179 ? 27.198 29.873  75.856  1.00 34.63  ? 194 MET A CE  1 
ATOM   1443 N N   . LEU A  1 180 ? 31.277 32.950  80.884  1.00 38.28  ? 195 LEU A N   1 
ATOM   1444 C CA  . LEU A  1 180 ? 32.502 33.214  81.675  1.00 39.44  ? 195 LEU A CA  1 
ATOM   1445 C C   . LEU A  1 180 ? 33.173 31.857  81.906  1.00 41.03  ? 195 LEU A C   1 
ATOM   1446 O O   . LEU A  1 180 ? 32.442 30.846  81.955  1.00 39.35  ? 195 LEU A O   1 
ATOM   1447 C CB  . LEU A  1 180 ? 32.057 33.888  82.975  1.00 42.60  ? 195 LEU A CB  1 
ATOM   1448 C CG  . LEU A  1 180 ? 33.168 34.341  83.918  1.00 45.40  ? 195 LEU A CG  1 
ATOM   1449 C CD1 . LEU A  1 180 ? 32.767 35.601  84.668  1.00 46.80  ? 195 LEU A CD1 1 
ATOM   1450 C CD2 . LEU A  1 180 ? 33.525 33.241  84.897  1.00 46.26  ? 195 LEU A CD2 1 
ATOM   1451 N N   . CYS A  1 181 ? 34.499 31.826  82.042  1.00 40.46  ? 196 CYS A N   1 
ATOM   1452 C CA  A CYS A  1 181 ? 35.316 30.578  82.079  0.50 41.50  ? 196 CYS A CA  1 
ATOM   1453 C CA  B CYS A  1 181 ? 35.294 30.578  82.097  0.50 41.73  ? 196 CYS A CA  1 
ATOM   1454 C C   . CYS A  1 181 ? 36.243 30.570  83.301  1.00 41.37  ? 196 CYS A C   1 
ATOM   1455 O O   . CYS A  1 181 ? 36.851 31.610  83.567  1.00 41.19  ? 196 CYS A O   1 
ATOM   1456 C CB  A CYS A  1 181 ? 36.147 30.446  80.807  0.50 43.72  ? 196 CYS A CB  1 
ATOM   1457 C CB  B CYS A  1 181 ? 36.057 30.454  80.794  0.50 44.47  ? 196 CYS A CB  1 
ATOM   1458 S SG  A CYS A  1 181 ? 35.232 29.707  79.432  0.50 44.58  ? 196 CYS A SG  1 
ATOM   1459 S SG  B CYS A  1 181 ? 37.327 29.180  80.844  0.50 45.37  ? 196 CYS A SG  1 
ATOM   1460 N N   . ALA A  1 182 ? 36.366 29.415  83.971  1.00 40.82  ? 197 ALA A N   1 
ATOM   1461 C CA  . ALA A  1 182 ? 37.264 29.202  85.135  1.00 39.63  ? 197 ALA A CA  1 
ATOM   1462 C C   . ALA A  1 182 ? 37.550 27.706  85.334  1.00 38.78  ? 197 ALA A C   1 
ATOM   1463 O O   . ALA A  1 182 ? 36.683 26.872  84.980  1.00 37.80  ? 197 ALA A O   1 
ATOM   1464 C CB  . ALA A  1 182 ? 36.634 29.792  86.378  1.00 40.42  ? 197 ALA A CB  1 
ATOM   1465 N N   . GLY A  1 183 ? 38.703 27.388  85.928  1.00 37.85  ? 198 GLY A N   1 
ATOM   1466 C CA  . GLY A  1 183 ? 39.070 26.026  86.366  1.00 39.19  ? 198 GLY A CA  1 
ATOM   1467 C C   . GLY A  1 183 ? 40.189 25.435  85.531  1.00 40.30  ? 198 GLY A C   1 
ATOM   1468 O O   . GLY A  1 183 ? 40.545 26.029  84.495  1.00 42.27  ? 198 GLY A O   1 
ATOM   1469 N N   . ASN A  1 184 ? 40.700 24.282  85.966  1.00 42.76  ? 199 ASN A N   1 
ATOM   1470 C CA  . ASN A  1 184 ? 41.872 23.591  85.370  1.00 44.50  ? 199 ASN A CA  1 
ATOM   1471 C C   . ASN A  1 184 ? 41.685 22.086  85.598  1.00 43.71  ? 199 ASN A C   1 
ATOM   1472 O O   . ASN A  1 184 ? 40.569 21.690  86.005  1.00 41.70  ? 199 ASN A O   1 
ATOM   1473 C CB  . ASN A  1 184 ? 43.177 24.180  85.924  1.00 44.97  ? 199 ASN A CB  1 
ATOM   1474 C CG  . ASN A  1 184 ? 43.266 24.119  87.437  1.00 46.05  ? 199 ASN A CG  1 
ATOM   1475 O OD1 . ASN A  1 184 ? 42.906 23.112  88.042  1.00 47.48  ? 199 ASN A OD1 1 
ATOM   1476 N ND2 . ASN A  1 184 ? 43.700 25.200  88.063  1.00 46.18  ? 199 ASN A ND2 1 
ATOM   1477 N N   . THR A  1 185 ? 42.734 21.287  85.373  1.00 43.94  ? 200 THR A N   1 
ATOM   1478 C CA  . THR A  1 185 ? 42.699 19.803  85.448  1.00 45.00  ? 200 THR A CA  1 
ATOM   1479 C C   . THR A  1 185 ? 42.693 19.312  86.902  1.00 42.50  ? 200 THR A C   1 
ATOM   1480 O O   . THR A  1 185 ? 42.510 18.099  87.095  1.00 43.70  ? 200 THR A O   1 
ATOM   1481 C CB  . THR A  1 185 ? 43.859 19.186  84.652  1.00 45.82  ? 200 THR A CB  1 
ATOM   1482 O OG1 . THR A  1 185 ? 45.087 19.759  85.102  1.00 45.60  ? 200 THR A OG1 1 
ATOM   1483 C CG2 . THR A  1 185 ? 43.714 19.407  83.163  1.00 47.30  ? 200 THR A CG2 1 
ATOM   1484 N N   . ARG A  1 186 ? 42.875 20.199  87.887  1.00 45.36  ? 201 ARG A N   1 
ATOM   1485 C CA  . ARG A  1 186 ? 42.798 19.860  89.334  1.00 46.27  ? 201 ARG A CA  1 
ATOM   1486 C C   . ARG A  1 186 ? 41.526 20.448  89.965  1.00 43.57  ? 201 ARG A C   1 
ATOM   1487 O O   . ARG A  1 186 ? 41.078 19.882  90.966  1.00 42.36  ? 201 ARG A O   1 
ATOM   1488 C CB  . ARG A  1 186 ? 44.057 20.359  90.055  1.00 50.34  ? 201 ARG A CB  1 
ATOM   1489 C CG  . ARG A  1 186 ? 45.356 19.713  89.581  1.00 53.40  ? 201 ARG A CG  1 
ATOM   1490 C CD  . ARG A  1 186 ? 46.602 20.504  89.942  1.00 58.61  ? 201 ARG A CD  1 
ATOM   1491 N NE  . ARG A  1 186 ? 46.602 21.834  89.337  1.00 63.52  ? 201 ARG A NE  1 
ATOM   1492 C CZ  . ARG A  1 186 ? 46.881 22.119  88.060  1.00 65.48  ? 201 ARG A CZ  1 
ATOM   1493 N NH1 . ARG A  1 186 ? 47.221 21.168  87.202  1.00 65.80  ? 201 ARG A NH1 1 
ATOM   1494 N NH2 . ARG A  1 186 ? 46.826 23.375  87.645  1.00 66.96  ? 201 ARG A NH2 1 
ATOM   1495 N N   . ARG A  1 187 ? 40.983 21.556  89.435  1.00 42.36  ? 202 ARG A N   1 
ATOM   1496 C CA  . ARG A  1 187 ? 39.994 22.421  90.137  1.00 43.29  ? 202 ARG A CA  1 
ATOM   1497 C C   . ARG A  1 187 ? 38.857 22.786  89.180  1.00 42.14  ? 202 ARG A C   1 
ATOM   1498 O O   . ARG A  1 187 ? 39.125 23.465  88.177  1.00 40.97  ? 202 ARG A O   1 
ATOM   1499 C CB  . ARG A  1 187 ? 40.704 23.665  90.682  1.00 48.44  ? 202 ARG A CB  1 
ATOM   1500 C CG  . ARG A  1 187 ? 41.811 23.324  91.673  1.00 52.25  ? 202 ARG A CG  1 
ATOM   1501 C CD  . ARG A  1 187 ? 42.459 24.492  92.369  1.00 57.62  ? 202 ARG A CD  1 
ATOM   1502 N NE  . ARG A  1 187 ? 43.249 24.065  93.519  1.00 62.35  ? 202 ARG A NE  1 
ATOM   1503 C CZ  . ARG A  1 187 ? 43.958 24.875  94.310  1.00 67.06  ? 202 ARG A CZ  1 
ATOM   1504 N NH1 . ARG A  1 187 ? 43.999 26.181  94.088  1.00 68.98  ? 202 ARG A NH1 1 
ATOM   1505 N NH2 . ARG A  1 187 ? 44.638 24.366  95.324  1.00 67.88  ? 202 ARG A NH2 1 
ATOM   1506 N N   . ASP A  1 188 ? 37.630 22.354  89.476  1.00 38.57  ? 203 ASP A N   1 
ATOM   1507 C CA  . ASP A  1 188 ? 36.464 22.572  88.583  1.00 37.83  ? 203 ASP A CA  1 
ATOM   1508 C C   . ASP A  1 188 ? 35.155 22.329  89.342  1.00 35.96  ? 203 ASP A C   1 
ATOM   1509 O O   . ASP A  1 188 ? 35.171 21.715  90.428  1.00 34.44  ? 203 ASP A O   1 
ATOM   1510 C CB  . ASP A  1 188 ? 36.564 21.672  87.342  1.00 38.99  ? 203 ASP A CB  1 
ATOM   1511 C CG  . ASP A  1 188 ? 35.819 22.156  86.105  1.00 39.83  ? 203 ASP A CG  1 
ATOM   1512 O OD1 . ASP A  1 188 ? 35.137 23.204  86.179  1.00 40.04  ? 203 ASP A OD1 1 
ATOM   1513 O OD2 . ASP A  1 188 ? 35.948 21.482  85.052  1.00 41.82  ? 203 ASP A OD2 1 
ATOM   1514 N N   . SER A  1 189 ? 34.061 22.818  88.768  1.00 34.32  ? 204 SER A N   1 
ATOM   1515 C CA  . SER A  1 189 ? 32.671 22.430  89.105  1.00 35.36  ? 204 SER A CA  1 
ATOM   1516 C C   . SER A  1 189 ? 32.332 21.173  88.298  1.00 33.42  ? 204 SER A C   1 
ATOM   1517 O O   . SER A  1 189 ? 33.073 20.863  87.353  1.00 33.39  ? 204 SER A O   1 
ATOM   1518 C CB  . SER A  1 189 ? 31.726 23.563  88.821  1.00 36.00  ? 204 SER A CB  1 
ATOM   1519 O OG  . SER A  1 189 ? 31.786 23.930  87.448  1.00 36.44  ? 204 SER A OG  1 
ATOM   1520 N N   . CYS A  1 190 ? 31.256 20.473  88.648  1.00 34.03  ? 205 CYS A N   1 
ATOM   1521 C CA  . CYS A  1 190 ? 30.884 19.172  88.033  1.00 34.72  ? 205 CYS A CA  1 
ATOM   1522 C C   . CYS A  1 190 ? 29.364 18.985  88.078  1.00 34.06  ? 205 CYS A C   1 
ATOM   1523 O O   . CYS A  1 190 ? 28.663 19.925  88.494  1.00 33.33  ? 205 CYS A O   1 
ATOM   1524 C CB  . CYS A  1 190 ? 31.618 18.040  88.747  1.00 38.70  ? 205 CYS A CB  1 
ATOM   1525 S SG  . CYS A  1 190 ? 31.824 16.532  87.763  1.00 44.86  ? 205 CYS A SG  1 
ATOM   1526 N N   . GLN A  1 191 ? 28.875 17.841  87.595  1.00 34.39  ? 206 GLN A N   1 
ATOM   1527 C CA  . GLN A  1 191 ? 27.436 17.453  87.600  1.00 34.84  ? 206 GLN A CA  1 
ATOM   1528 C C   . GLN A  1 191 ? 26.899 17.573  89.029  1.00 32.89  ? 206 GLN A C   1 
ATOM   1529 O O   . GLN A  1 191 ? 27.533 17.031  89.942  1.00 36.29  ? 206 GLN A O   1 
ATOM   1530 C CB  . GLN A  1 191 ? 27.271 16.040  87.029  1.00 36.01  ? 206 GLN A CB  1 
ATOM   1531 C CG  . GLN A  1 191 ? 25.849 15.498  87.029  1.00 38.56  ? 206 GLN A CG  1 
ATOM   1532 C CD  . GLN A  1 191 ? 25.722 14.081  86.528  0.00 37.54  ? 206 GLN A CD  1 
ATOM   1533 O OE1 . GLN A  1 191 ? 26.685 13.316  86.498  0.00 37.78  ? 206 GLN A OE1 1 
ATOM   1534 N NE2 . GLN A  1 191 ? 24.517 13.710  86.127  0.00 37.58  ? 206 GLN A NE2 1 
ATOM   1535 N N   . GLY A  1 192 ? 25.790 18.295  89.204  1.00 31.64  ? 207 GLY A N   1 
ATOM   1536 C CA  . GLY A  1 192 ? 25.171 18.577  90.512  1.00 32.34  ? 207 GLY A CA  1 
ATOM   1537 C C   . GLY A  1 192 ? 25.546 19.944  91.069  1.00 31.52  ? 207 GLY A C   1 
ATOM   1538 O O   . GLY A  1 192 ? 24.848 20.399  91.988  1.00 33.96  ? 207 GLY A O   1 
ATOM   1539 N N   . ASP A  1 193 ? 26.601 20.581  90.553  1.00 31.47  ? 208 ASP A N   1 
ATOM   1540 C CA  . ASP A  1 193 ? 27.005 21.959  90.934  1.00 32.08  ? 208 ASP A CA  1 
ATOM   1541 C C   . ASP A  1 193 ? 26.281 22.988  90.068  1.00 33.09  ? 208 ASP A C   1 
ATOM   1542 O O   . ASP A  1 193 ? 26.305 24.170  90.459  1.00 33.15  ? 208 ASP A O   1 
ATOM   1543 C CB  . ASP A  1 193 ? 28.515 22.160  90.821  1.00 33.26  ? 208 ASP A CB  1 
ATOM   1544 C CG  . ASP A  1 193 ? 29.295 21.313  91.799  1.00 32.31  ? 208 ASP A CG  1 
ATOM   1545 O OD1 . ASP A  1 193 ? 28.860 21.229  92.966  1.00 31.16  ? 208 ASP A OD1 1 
ATOM   1546 O OD2 . ASP A  1 193 ? 30.322 20.752  91.385  1.00 33.32  ? 208 ASP A OD2 1 
ATOM   1547 N N   . SER A  1 194 ? 25.679 22.556  88.950  1.00 34.27  ? 209 SER A N   1 
ATOM   1548 C CA  . SER A  1 194 ? 24.940 23.401  87.978  1.00 35.28  ? 209 SER A CA  1 
ATOM   1549 C C   . SER A  1 194 ? 23.977 24.333  88.708  1.00 34.22  ? 209 SER A C   1 
ATOM   1550 O O   . SER A  1 194 ? 23.299 23.870  89.647  1.00 35.20  ? 209 SER A O   1 
ATOM   1551 C CB  . SER A  1 194 ? 24.199 22.572  86.966  1.00 36.39  ? 209 SER A CB  1 
ATOM   1552 O OG  . SER A  1 194 ? 25.085 22.127  85.956  1.00 38.24  ? 209 SER A OG  1 
ATOM   1553 N N   . GLY A  1 195 ? 23.935 25.594  88.273  1.00 33.58  ? 210 GLY A N   1 
ATOM   1554 C CA  . GLY A  1 195 ? 23.068 26.637  88.842  1.00 32.78  ? 210 GLY A CA  1 
ATOM   1555 C C   . GLY A  1 195 ? 23.676 27.315  90.050  1.00 33.01  ? 210 GLY A C   1 
ATOM   1556 O O   . GLY A  1 195 ? 23.178 28.389  90.412  1.00 33.51  ? 210 GLY A O   1 
ATOM   1557 N N   . GLY A  1 196 ? 24.733 26.738  90.627  1.00 32.67  ? 211 GLY A N   1 
ATOM   1558 C CA  . GLY A  1 196 ? 25.422 27.272  91.807  1.00 32.83  ? 211 GLY A CA  1 
ATOM   1559 C C   . GLY A  1 196 ? 26.268 28.487  91.456  1.00 34.03  ? 211 GLY A C   1 
ATOM   1560 O O   . GLY A  1 196 ? 26.510 28.767  90.288  1.00 34.28  ? 211 GLY A O   1 
ATOM   1561 N N   . PRO A  1 197 ? 26.731 29.245  92.470  1.00 36.21  ? 212 PRO A N   1 
ATOM   1562 C CA  . PRO A  1 197 ? 27.435 30.503  92.233  1.00 35.61  ? 212 PRO A CA  1 
ATOM   1563 C C   . PRO A  1 197 ? 28.954 30.359  92.059  1.00 35.23  ? 212 PRO A C   1 
ATOM   1564 O O   . PRO A  1 197 ? 29.552 29.519  92.725  1.00 35.82  ? 212 PRO A O   1 
ATOM   1565 C CB  . PRO A  1 197 ? 27.093 31.273  93.510  1.00 35.06  ? 212 PRO A CB  1 
ATOM   1566 C CG  . PRO A  1 197 ? 27.067 30.209  94.586  1.00 35.69  ? 212 PRO A CG  1 
ATOM   1567 C CD  . PRO A  1 197 ? 26.593 28.940  93.903  1.00 35.20  ? 212 PRO A CD  1 
ATOM   1568 N N   . LEU A  1 198 ? 29.513 31.139  91.125  1.00 34.99  ? 213 LEU A N   1 
ATOM   1569 C CA  . LEU A  1 198 ? 30.951 31.516  91.088  1.00 33.86  ? 213 LEU A CA  1 
ATOM   1570 C C   . LEU A  1 198 ? 31.054 32.924  91.686  1.00 34.70  ? 213 LEU A C   1 
ATOM   1571 O O   . LEU A  1 198 ? 30.442 33.847  91.113  1.00 32.49  ? 213 LEU A O   1 
ATOM   1572 C CB  . LEU A  1 198 ? 31.467 31.460  89.648  1.00 34.02  ? 213 LEU A CB  1 
ATOM   1573 C CG  . LEU A  1 198 ? 32.953 31.768  89.461  1.00 35.00  ? 213 LEU A CG  1 
ATOM   1574 C CD1 . LEU A  1 198 ? 33.834 30.687  90.066  1.00 34.75  ? 213 LEU A CD1 1 
ATOM   1575 C CD2 . LEU A  1 198 ? 33.278 31.939  87.991  1.00 36.16  ? 213 LEU A CD2 1 
ATOM   1576 N N   . VAL A  1 199 ? 31.723 33.054  92.836  1.00 34.60  ? 214 VAL A N   1 
ATOM   1577 C CA  . VAL A  1 199 ? 31.806 34.319  93.624  1.00 35.68  ? 214 VAL A CA  1 
ATOM   1578 C C   . VAL A  1 199 ? 33.271 34.768  93.671  1.00 39.04  ? 214 VAL A C   1 
ATOM   1579 O O   . VAL A  1 199 ? 34.157 33.902  93.788  1.00 38.35  ? 214 VAL A O   1 
ATOM   1580 C CB  . VAL A  1 199 ? 31.187 34.170  95.029  1.00 36.07  ? 214 VAL A CB  1 
ATOM   1581 C CG1 . VAL A  1 199 ? 29.687 33.950  94.944  1.00 35.89  ? 214 VAL A CG1 1 
ATOM   1582 C CG2 . VAL A  1 199 ? 31.838 33.078  95.867  1.00 37.47  ? 214 VAL A CG2 1 
ATOM   1583 N N   . CYS A  1 200 ? 33.506 36.077  93.550  1.00 42.65  ? 215 CYS A N   1 
ATOM   1584 C CA  . CYS A  1 200 ? 34.849 36.717  93.624  1.00 42.80  ? 215 CYS A CA  1 
ATOM   1585 C C   . CYS A  1 200 ? 34.782 37.853  94.654  1.00 41.68  ? 215 CYS A C   1 
ATOM   1586 O O   . CYS A  1 200 ? 33.762 38.576  94.661  1.00 37.83  ? 215 CYS A O   1 
ATOM   1587 C CB  . CYS A  1 200 ? 35.299 37.244  92.261  1.00 45.18  ? 215 CYS A CB  1 
ATOM   1588 S SG  . CYS A  1 200 ? 34.962 36.133  90.863  1.00 47.98  ? 215 CYS A SG  1 
ATOM   1589 N N   . LYS A  1 201 ? 35.798 37.986  95.511  1.00 42.63  ? 216 LYS A N   1 
ATOM   1590 C CA  . LYS A  1 201 ? 35.835 39.040  96.559  1.00 45.79  ? 216 LYS A CA  1 
ATOM   1591 C C   . LYS A  1 201 ? 36.487 40.284  95.950  1.00 44.33  ? 216 LYS A C   1 
ATOM   1592 O O   . LYS A  1 201 ? 37.680 40.215  95.637  1.00 45.03  ? 216 LYS A O   1 
ATOM   1593 C CB  . LYS A  1 201 ? 36.537 38.560  97.833  1.00 46.44  ? 216 LYS A CB  1 
ATOM   1594 C CG  . LYS A  1 201 ? 36.178 39.380  99.065  1.00 47.73  ? 216 LYS A CG  1 
ATOM   1595 C CD  . LYS A  1 201 ? 36.803 38.899  100.346 1.00 49.08  ? 216 LYS A CD  1 
ATOM   1596 C CE  . LYS A  1 201 ? 36.153 39.542  101.550 1.00 49.72  ? 216 LYS A CE  1 
ATOM   1597 N NZ  . LYS A  1 201 ? 36.730 39.027  102.810 1.00 53.13  ? 216 LYS A NZ  1 
ATOM   1598 N N   . VAL A  1 202 ? 35.720 41.367  95.815  1.00 47.08  ? 217 VAL A N   1 
ATOM   1599 C CA  . VAL A  1 202 ? 36.143 42.661  95.200  1.00 49.67  ? 217 VAL A CA  1 
ATOM   1600 C C   . VAL A  1 202 ? 35.867 43.781  96.213  1.00 51.03  ? 217 VAL A C   1 
ATOM   1601 O O   . VAL A  1 202 ? 34.682 44.032  96.497  1.00 50.99  ? 217 VAL A O   1 
ATOM   1602 C CB  . VAL A  1 202 ? 35.403 42.907  93.867  1.00 52.64  ? 217 VAL A CB  1 
ATOM   1603 C CG1 . VAL A  1 202 ? 35.878 44.177  93.171  1.00 54.95  ? 217 VAL A CG1 1 
ATOM   1604 C CG2 . VAL A  1 202 ? 35.512 41.720  92.919  1.00 53.12  ? 217 VAL A CG2 1 
ATOM   1605 N N   . ASN A  1 203 ? 36.921 44.429  96.722  1.00 56.87  ? 218 ASN A N   1 
ATOM   1606 C CA  . ASN A  1 203 ? 36.849 45.590  97.657  1.00 59.41  ? 218 ASN A CA  1 
ATOM   1607 C C   . ASN A  1 203 ? 36.043 45.187  98.895  1.00 59.99  ? 218 ASN A C   1 
ATOM   1608 O O   . ASN A  1 203 ? 35.096 45.920  99.268  1.00 57.78  ? 218 ASN A O   1 
ATOM   1609 C CB  . ASN A  1 203 ? 36.259 46.836  96.986  1.00 63.01  ? 218 ASN A CB  1 
ATOM   1610 C CG  . ASN A  1 203 ? 37.024 47.267  95.754  1.00 67.20  ? 218 ASN A CG  1 
ATOM   1611 O OD1 . ASN A  1 203 ? 38.179 46.885  95.566  1.00 70.53  ? 218 ASN A OD1 1 
ATOM   1612 N ND2 . ASN A  1 203 ? 36.392 48.072  94.914  1.00 69.72  ? 218 ASN A ND2 1 
ATOM   1613 N N   . GLY A  1 204 ? 36.377 44.026  99.470  1.00 61.22  ? 219 GLY A N   1 
ATOM   1614 C CA  . GLY A  1 204 ? 35.781 43.496  100.710 1.00 58.29  ? 219 GLY A CA  1 
ATOM   1615 C C   . GLY A  1 204 ? 34.393 42.897  100.522 1.00 57.73  ? 219 GLY A C   1 
ATOM   1616 O O   . GLY A  1 204 ? 33.834 42.439  101.538 1.00 53.93  ? 219 GLY A O   1 
ATOM   1617 N N   . THR A  1 205 ? 33.842 42.889  99.301  1.00 54.26  ? 220 THR A N   1 
ATOM   1618 C CA  . THR A  1 205 ? 32.478 42.378  99.004  1.00 53.46  ? 220 THR A CA  1 
ATOM   1619 C C   . THR A  1 205 ? 32.596 41.151  98.094  1.00 48.09  ? 220 THR A C   1 
ATOM   1620 O O   . THR A  1 205 ? 33.297 41.230  97.071  1.00 44.01  ? 220 THR A O   1 
ATOM   1621 C CB  . THR A  1 205 ? 31.587 43.476  98.413  1.00 55.23  ? 220 THR A CB  1 
ATOM   1622 O OG1 . THR A  1 205 ? 31.534 44.526  99.377  1.00 60.21  ? 220 THR A OG1 1 
ATOM   1623 C CG2 . THR A  1 205 ? 30.179 43.015  98.099  1.00 54.93  ? 220 THR A CG2 1 
ATOM   1624 N N   . TRP A  1 206 ? 31.924 40.060  98.467  1.00 46.63  ? 221 TRP A N   1 
ATOM   1625 C CA  . TRP A  1 206 ? 31.705 38.880  97.589  1.00 43.12  ? 221 TRP A CA  1 
ATOM   1626 C C   . TRP A  1 206 ? 30.677 39.259  96.520  1.00 39.96  ? 221 TRP A C   1 
ATOM   1627 O O   . TRP A  1 206 ? 29.560 39.648  96.896  1.00 41.73  ? 221 TRP A O   1 
ATOM   1628 C CB  . TRP A  1 206 ? 31.272 37.655  98.403  1.00 42.26  ? 221 TRP A CB  1 
ATOM   1629 C CG  . TRP A  1 206 ? 32.394 37.101  99.220  1.00 41.74  ? 221 TRP A CG  1 
ATOM   1630 C CD1 . TRP A  1 206 ? 32.624 37.310  100.548 1.00 41.93  ? 221 TRP A CD1 1 
ATOM   1631 C CD2 . TRP A  1 206 ? 33.474 36.275  98.749  1.00 41.14  ? 221 TRP A CD2 1 
ATOM   1632 N NE1 . TRP A  1 206 ? 33.764 36.664  100.937 1.00 43.39  ? 221 TRP A NE1 1 
ATOM   1633 C CE2 . TRP A  1 206 ? 34.304 36.014  99.862  1.00 41.58  ? 221 TRP A CE2 1 
ATOM   1634 C CE3 . TRP A  1 206 ? 33.808 35.708  97.513  1.00 39.41  ? 221 TRP A CE3 1 
ATOM   1635 C CZ2 . TRP A  1 206 ? 35.449 35.223  99.770  1.00 41.63  ? 221 TRP A CZ2 1 
ATOM   1636 C CZ3 . TRP A  1 206 ? 34.943 34.932  97.421  1.00 39.12  ? 221 TRP A CZ3 1 
ATOM   1637 C CH2 . TRP A  1 206 ? 35.749 34.691  98.537  1.00 40.54  ? 221 TRP A CH2 1 
ATOM   1638 N N   . LEU A  1 207 ? 31.069 39.194  95.243  1.00 39.39  ? 222 LEU A N   1 
ATOM   1639 C CA  . LEU A  1 207 ? 30.188 39.444  94.071  1.00 39.49  ? 222 LEU A CA  1 
ATOM   1640 C C   . LEU A  1 207 ? 30.024 38.135  93.292  1.00 36.81  ? 222 LEU A C   1 
ATOM   1641 O O   . LEU A  1 207 ? 31.038 37.444  93.067  1.00 37.37  ? 222 LEU A O   1 
ATOM   1642 C CB  . LEU A  1 207 ? 30.807 40.542  93.196  1.00 39.89  ? 222 LEU A CB  1 
ATOM   1643 C CG  . LEU A  1 207 ? 30.997 41.903  93.869  1.00 39.87  ? 222 LEU A CG  1 
ATOM   1644 C CD1 . LEU A  1 207 ? 31.721 42.869  92.941  1.00 40.44  ? 222 LEU A CD1 1 
ATOM   1645 C CD2 . LEU A  1 207 ? 29.665 42.492  94.316  1.00 40.62  ? 222 LEU A CD2 1 
ATOM   1646 N N   . GLN A  1 208 ? 28.798 37.807  92.890  1.00 35.98  ? 223 GLN A N   1 
ATOM   1647 C CA  . GLN A  1 208 ? 28.542 36.622  92.032  1.00 35.37  ? 223 GLN A CA  1 
ATOM   1648 C C   . GLN A  1 208 ? 28.887 36.977  90.578  1.00 33.99  ? 223 GLN A C   1 
ATOM   1649 O O   . GLN A  1 208 ? 28.104 37.684  89.926  1.00 34.99  ? 223 GLN A O   1 
ATOM   1650 C CB  . GLN A  1 208 ? 27.110 36.113  92.181  1.00 34.91  ? 223 GLN A CB  1 
ATOM   1651 C CG  . GLN A  1 208 ? 26.930 34.793  91.444  1.00 36.01  ? 223 GLN A CG  1 
ATOM   1652 C CD  . GLN A  1 208 ? 25.652 34.055  91.736  1.00 36.08  ? 223 GLN A CD  1 
ATOM   1653 O OE1 . GLN A  1 208 ? 24.897 34.376  92.657  1.00 35.84  ? 223 GLN A OE1 1 
ATOM   1654 N NE2 . GLN A  1 208 ? 25.416 33.027  90.936  1.00 38.01  ? 223 GLN A NE2 1 
ATOM   1655 N N   . ALA A  1 209 ? 30.026 36.481  90.097  1.00 32.84  ? 224 ALA A N   1 
ATOM   1656 C CA  . ALA A  1 209 ? 30.515 36.643  88.709  1.00 33.72  ? 224 ALA A CA  1 
ATOM   1657 C C   . ALA A  1 209 ? 29.758 35.705  87.753  1.00 35.06  ? 224 ALA A C   1 
ATOM   1658 O O   . ALA A  1 209 ? 29.544 36.109  86.582  1.00 33.27  ? 224 ALA A O   1 
ATOM   1659 C CB  . ALA A  1 209 ? 32.001 36.379  88.667  1.00 32.49  ? 224 ALA A CB  1 
ATOM   1660 N N   . GLY A  1 210 ? 29.396 34.494  88.209  1.00 33.82  ? 225 GLY A N   1 
ATOM   1661 C CA  . GLY A  1 210 ? 28.948 33.402  87.323  1.00 34.03  ? 225 GLY A CA  1 
ATOM   1662 C C   . GLY A  1 210 ? 27.899 32.479  87.928  1.00 32.35  ? 225 GLY A C   1 
ATOM   1663 O O   . GLY A  1 210 ? 27.756 32.431  89.158  1.00 34.17  ? 225 GLY A O   1 
ATOM   1664 N N   . VAL A  1 211 ? 27.179 31.779  87.052  1.00 32.45  ? 226 VAL A N   1 
ATOM   1665 C CA  . VAL A  1 211 ? 26.284 30.636  87.377  1.00 33.36  ? 226 VAL A CA  1 
ATOM   1666 C C   . VAL A  1 211 ? 26.875 29.409  86.679  1.00 32.28  ? 226 VAL A C   1 
ATOM   1667 O O   . VAL A  1 211 ? 27.072 29.487  85.467  1.00 32.26  ? 226 VAL A O   1 
ATOM   1668 C CB  . VAL A  1 211 ? 24.843 30.929  86.927  1.00 32.69  ? 226 VAL A CB  1 
ATOM   1669 C CG1 . VAL A  1 211 ? 23.914 29.752  87.163  1.00 33.67  ? 226 VAL A CG1 1 
ATOM   1670 C CG2 . VAL A  1 211 ? 24.296 32.185  87.589  1.00 32.31  ? 226 VAL A CG2 1 
ATOM   1671 N N   . VAL A  1 212 ? 27.112 28.315  87.412  1.00 32.36  ? 227 VAL A N   1 
ATOM   1672 C CA  . VAL A  1 212 ? 27.640 27.033  86.852  1.00 31.74  ? 227 VAL A CA  1 
ATOM   1673 C C   . VAL A  1 212 ? 26.701 26.608  85.718  1.00 30.90  ? 227 VAL A C   1 
ATOM   1674 O O   . VAL A  1 212 ? 25.498 26.464  85.991  1.00 34.76  ? 227 VAL A O   1 
ATOM   1675 C CB  . VAL A  1 212 ? 27.789 25.926  87.917  1.00 30.03  ? 227 VAL A CB  1 
ATOM   1676 C CG1 . VAL A  1 212 ? 28.271 24.612  87.303  1.00 29.77  ? 227 VAL A CG1 1 
ATOM   1677 C CG2 . VAL A  1 212 ? 28.728 26.329  89.034  1.00 30.49  ? 227 VAL A CG2 1 
ATOM   1678 N N   . SER A  1 213 ? 27.221 26.473  84.492  1.00 30.06  ? 228 SER A N   1 
ATOM   1679 C CA  . SER A  1 213 ? 26.425 26.241  83.257  1.00 31.43  ? 228 SER A CA  1 
ATOM   1680 C C   . SER A  1 213 ? 26.783 24.892  82.623  1.00 32.62  ? 228 SER A C   1 
ATOM   1681 O O   . SER A  1 213 ? 25.926 24.000  82.631  1.00 33.44  ? 228 SER A O   1 
ATOM   1682 C CB  . SER A  1 213 ? 26.580 27.370  82.273  1.00 30.35  ? 228 SER A CB  1 
ATOM   1683 O OG  . SER A  1 213 ? 25.701 27.191  81.167  1.00 31.08  ? 228 SER A OG  1 
ATOM   1684 N N   . TRP A  1 214 ? 27.976 24.751  82.044  1.00 33.52  ? 229 TRP A N   1 
ATOM   1685 C CA  . TRP A  1 214 ? 28.334 23.540  81.259  1.00 32.36  ? 229 TRP A CA  1 
ATOM   1686 C C   . TRP A  1 214 ? 29.844 23.378  81.141  1.00 31.25  ? 229 TRP A C   1 
ATOM   1687 O O   . TRP A  1 214 ? 30.603 24.265  81.580  1.00 30.36  ? 229 TRP A O   1 
ATOM   1688 C CB  . TRP A  1 214 ? 27.647 23.539  79.883  1.00 33.01  ? 229 TRP A CB  1 
ATOM   1689 C CG  . TRP A  1 214 ? 28.102 24.602  78.932  1.00 33.76  ? 229 TRP A CG  1 
ATOM   1690 C CD1 . TRP A  1 214 ? 27.721 25.912  78.911  1.00 33.67  ? 229 TRP A CD1 1 
ATOM   1691 C CD2 . TRP A  1 214 ? 29.011 24.433  77.833  1.00 33.11  ? 229 TRP A CD2 1 
ATOM   1692 N NE1 . TRP A  1 214 ? 28.339 26.576  77.891  1.00 33.28  ? 229 TRP A NE1 1 
ATOM   1693 C CE2 . TRP A  1 214 ? 29.125 25.690  77.198  1.00 33.73  ? 229 TRP A CE2 1 
ATOM   1694 C CE3 . TRP A  1 214 ? 29.739 23.347  77.326  1.00 34.51  ? 229 TRP A CE3 1 
ATOM   1695 C CZ2 . TRP A  1 214 ? 29.933 25.882  76.077  1.00 33.55  ? 229 TRP A CZ2 1 
ATOM   1696 C CZ3 . TRP A  1 214 ? 30.539 23.541  76.221  1.00 35.25  ? 229 TRP A CZ3 1 
ATOM   1697 C CH2 . TRP A  1 214 ? 30.632 24.792  75.606  1.00 33.99  ? 229 TRP A CH2 1 
ATOM   1698 N N   . GLY A  1 215 ? 30.237 22.239  80.588  1.00 31.38  ? 230 GLY A N   1 
ATOM   1699 C CA  . GLY A  1 215 ? 31.623 21.940  80.211  1.00 33.42  ? 230 GLY A CA  1 
ATOM   1700 C C   . GLY A  1 215 ? 31.702 20.554  79.636  1.00 35.03  ? 230 GLY A C   1 
ATOM   1701 O O   . GLY A  1 215 ? 30.694 19.828  79.727  1.00 40.31  ? 230 GLY A O   1 
ATOM   1702 N N   . GLU A  1 216 ? 32.836 20.205  79.043  1.00 37.60  ? 231 GLU A N   1 
ATOM   1703 C CA  . GLU A  1 216 ? 33.093 18.822  78.574  1.00 39.51  ? 231 GLU A CA  1 
ATOM   1704 C C   . GLU A  1 216 ? 33.697 18.051  79.746  1.00 39.02  ? 231 GLU A C   1 
ATOM   1705 O O   . GLU A  1 216 ? 34.891 18.227  80.020  1.00 40.13  ? 231 GLU A O   1 
ATOM   1706 C CB  . GLU A  1 216 ? 33.976 18.832  77.338  1.00 42.62  ? 231 GLU A CB  1 
ATOM   1707 C CG  . GLU A  1 216 ? 34.152 17.452  76.740  1.00 45.81  ? 231 GLU A CG  1 
ATOM   1708 C CD  . GLU A  1 216 ? 35.305 17.441  75.769  1.00 48.83  ? 231 GLU A CD  1 
ATOM   1709 O OE1 . GLU A  1 216 ? 36.263 16.663  75.982  1.00 53.97  ? 231 GLU A OE1 1 
ATOM   1710 O OE2 . GLU A  1 216 ? 35.262 18.266  74.831  1.00 48.74  ? 231 GLU A OE2 1 
ATOM   1711 N N   . GLY A  1 217 ? 32.869 17.272  80.442  1.00 39.57  ? 232 GLY A N   1 
ATOM   1712 C CA  . GLY A  1 217 ? 33.238 16.594  81.694  1.00 41.50  ? 232 GLY A CA  1 
ATOM   1713 C C   . GLY A  1 217 ? 33.683 17.597  82.745  1.00 43.41  ? 232 GLY A C   1 
ATOM   1714 O O   . GLY A  1 217 ? 33.256 18.778  82.687  1.00 39.43  ? 232 GLY A O   1 
ATOM   1715 N N   . CYS A  1 218 ? 34.509 17.136  83.681  1.00 43.07  ? 233 CYS A N   1 
ATOM   1716 C CA  . CYS A  1 218 ? 34.980 17.901  84.863  1.00 44.65  ? 233 CYS A CA  1 
ATOM   1717 C C   . CYS A  1 218 ? 36.502 17.769  84.923  1.00 42.70  ? 233 CYS A C   1 
ATOM   1718 O O   . CYS A  1 218 ? 36.992 16.627  84.844  1.00 45.04  ? 233 CYS A O   1 
ATOM   1719 C CB  . CYS A  1 218 ? 34.309 17.398  86.138  1.00 44.72  ? 233 CYS A CB  1 
ATOM   1720 S SG  . CYS A  1 218 ? 32.518 17.164  85.946  1.00 52.31  ? 233 CYS A SG  1 
ATOM   1721 N N   . ALA A  1 219 ? 37.203 18.903  84.974  1.00 42.75  ? 234 ALA A N   1 
ATOM   1722 C CA  . ALA A  1 219 ? 38.674 19.006  85.122  1.00 43.81  ? 234 ALA A CA  1 
ATOM   1723 C C   . ALA A  1 219 ? 39.396 18.199  84.031  1.00 43.61  ? 234 ALA A C   1 
ATOM   1724 O O   . ALA A  1 219 ? 40.445 17.607  84.332  1.00 43.26  ? 234 ALA A O   1 
ATOM   1725 C CB  . ALA A  1 219 ? 39.059 18.555  86.512  1.00 43.04  ? 234 ALA A CB  1 
ATOM   1726 N N   . GLN A  1 220 ? 38.872 18.202  82.799  1.00 44.49  ? 235 GLN A N   1 
ATOM   1727 C CA  . GLN A  1 220 ? 39.510 17.576  81.606  1.00 44.72  ? 235 GLN A CA  1 
ATOM   1728 C C   . GLN A  1 220 ? 40.491 18.571  80.984  1.00 41.62  ? 235 GLN A C   1 
ATOM   1729 O O   . GLN A  1 220 ? 40.246 19.775  81.039  1.00 39.69  ? 235 GLN A O   1 
ATOM   1730 C CB  . GLN A  1 220 ? 38.455 17.151  80.583  1.00 46.38  ? 235 GLN A CB  1 
ATOM   1731 C CG  . GLN A  1 220 ? 37.517 16.064  81.083  1.00 51.21  ? 235 GLN A CG  1 
ATOM   1732 C CD  . GLN A  1 220 ? 38.206 14.726  81.221  1.00 57.61  ? 235 GLN A CD  1 
ATOM   1733 O OE1 . GLN A  1 220 ? 38.970 14.491  82.155  1.00 62.23  ? 235 GLN A OE1 1 
ATOM   1734 N NE2 . GLN A  1 220 ? 37.931 13.822  80.295  1.00 64.01  ? 235 GLN A NE2 1 
ATOM   1735 N N   . PRO A  1 221 ? 41.620 18.110  80.391  1.00 41.05  ? 236 PRO A N   1 
ATOM   1736 C CA  . PRO A  1 221 ? 42.561 19.000  79.704  1.00 41.21  ? 236 PRO A CA  1 
ATOM   1737 C C   . PRO A  1 221 ? 41.903 19.898  78.645  1.00 38.71  ? 236 PRO A C   1 
ATOM   1738 O O   . PRO A  1 221 ? 41.149 19.390  77.841  1.00 38.73  ? 236 PRO A O   1 
ATOM   1739 C CB  . PRO A  1 221 ? 43.553 18.038  79.026  1.00 41.41  ? 236 PRO A CB  1 
ATOM   1740 C CG  . PRO A  1 221 ? 43.507 16.795  79.887  1.00 42.53  ? 236 PRO A CG  1 
ATOM   1741 C CD  . PRO A  1 221 ? 42.073 16.708  80.369  1.00 42.85  ? 236 PRO A CD  1 
ATOM   1742 N N   . ASN A  1 222 ? 42.173 21.204  78.707  1.00 36.03  ? 237 ASN A N   1 
ATOM   1743 C CA  . ASN A  1 222 ? 41.730 22.229  77.722  1.00 36.12  ? 237 ASN A CA  1 
ATOM   1744 C C   . ASN A  1 222 ? 40.197 22.342  77.708  1.00 34.52  ? 237 ASN A C   1 
ATOM   1745 O O   . ASN A  1 222 ? 39.660 22.778  76.677  1.00 33.14  ? 237 ASN A O   1 
ATOM   1746 C CB  . ASN A  1 222 ? 42.283 21.924  76.324  1.00 38.24  ? 237 ASN A CB  1 
ATOM   1747 C CG  . ASN A  1 222 ? 43.797 21.955  76.291  1.00 38.82  ? 237 ASN A CG  1 
ATOM   1748 O OD1 . ASN A  1 222 ? 44.394 22.898  76.793  1.00 43.42  ? 237 ASN A OD1 1 
ATOM   1749 N ND2 . ASN A  1 222 ? 44.421 20.929  75.739  1.00 39.48  ? 237 ASN A ND2 1 
ATOM   1750 N N   . ARG A  1 223 ? 39.524 21.983  78.805  1.00 33.04  ? 238 ARG A N   1 
ATOM   1751 C CA  . ARG A  1 223 ? 38.040 22.037  78.917  1.00 35.12  ? 238 ARG A CA  1 
ATOM   1752 C C   . ARG A  1 223 ? 37.674 22.633  80.272  1.00 33.10  ? 238 ARG A C   1 
ATOM   1753 O O   . ARG A  1 223 ? 37.106 21.961  81.129  1.00 36.22  ? 238 ARG A O   1 
ATOM   1754 C CB  . ARG A  1 223 ? 37.435 20.651  78.686  1.00 35.04  ? 238 ARG A CB  1 
ATOM   1755 C CG  . ARG A  1 223 ? 37.767 20.029  77.336  1.00 35.65  ? 238 ARG A CG  1 
ATOM   1756 C CD  . ARG A  1 223 ? 37.165 20.726  76.132  1.00 35.72  ? 238 ARG A CD  1 
ATOM   1757 N NE  . ARG A  1 223 ? 37.462 19.973  74.915  1.00 35.52  ? 238 ARG A NE  1 
ATOM   1758 C CZ  . ARG A  1 223 ? 38.518 20.134  74.108  1.00 36.32  ? 238 ARG A CZ  1 
ATOM   1759 N NH1 . ARG A  1 223 ? 39.430 21.066  74.335  1.00 35.45  ? 238 ARG A NH1 1 
ATOM   1760 N NH2 . ARG A  1 223 ? 38.653 19.348  73.050  1.00 36.26  ? 238 ARG A NH2 1 
ATOM   1761 N N   . PRO A  1 224 ? 37.988 23.926  80.517  1.00 34.36  ? 239 PRO A N   1 
ATOM   1762 C CA  . PRO A  1 224 ? 37.580 24.581  81.757  1.00 35.60  ? 239 PRO A CA  1 
ATOM   1763 C C   . PRO A  1 224 ? 36.054 24.716  81.874  1.00 34.60  ? 239 PRO A C   1 
ATOM   1764 O O   . PRO A  1 224 ? 35.363 24.654  80.867  1.00 37.23  ? 239 PRO A O   1 
ATOM   1765 C CB  . PRO A  1 224 ? 38.283 25.945  81.718  1.00 35.95  ? 239 PRO A CB  1 
ATOM   1766 C CG  . PRO A  1 224 ? 38.576 26.183  80.253  1.00 36.12  ? 239 PRO A CG  1 
ATOM   1767 C CD  . PRO A  1 224 ? 38.757 24.817  79.636  1.00 34.93  ? 239 PRO A CD  1 
ATOM   1768 N N   . GLY A  1 225 ? 35.572 24.848  83.109  1.00 32.00  ? 240 GLY A N   1 
ATOM   1769 C CA  . GLY A  1 225 ? 34.158 25.096  83.437  1.00 32.05  ? 240 GLY A CA  1 
ATOM   1770 C C   . GLY A  1 225 ? 33.652 26.348  82.743  1.00 31.94  ? 240 GLY A C   1 
ATOM   1771 O O   . GLY A  1 225 ? 34.389 27.344  82.736  1.00 30.14  ? 240 GLY A O   1 
ATOM   1772 N N   . ILE A  1 226 ? 32.474 26.270  82.123  1.00 31.04  ? 241 ILE A N   1 
ATOM   1773 C CA  . ILE A  1 226 ? 31.756 27.425  81.513  1.00 32.32  ? 241 ILE A CA  1 
ATOM   1774 C C   . ILE A  1 226 ? 30.623 27.821  82.460  1.00 32.33  ? 241 ILE A C   1 
ATOM   1775 O O   . ILE A  1 226 ? 29.921 26.927  82.969  1.00 32.88  ? 241 ILE A O   1 
ATOM   1776 C CB  . ILE A  1 226 ? 31.213 27.103  80.108  1.00 33.46  ? 241 ILE A CB  1 
ATOM   1777 C CG1 . ILE A  1 226 ? 32.205 26.302  79.263  1.00 33.58  ? 241 ILE A CG1 1 
ATOM   1778 C CG2 . ILE A  1 226 ? 30.760 28.382  79.405  1.00 32.93  ? 241 ILE A CG2 1 
ATOM   1779 C CD1 . ILE A  1 226 ? 33.524 26.979  79.070  1.00 34.26  ? 241 ILE A CD1 1 
ATOM   1780 N N   . TYR A  1 227 ? 30.477 29.123  82.674  1.00 31.44  ? 242 TYR A N   1 
ATOM   1781 C CA  . TYR A  1 227 ? 29.507 29.751  83.596  1.00 32.67  ? 242 TYR A CA  1 
ATOM   1782 C C   . TYR A  1 227 ? 28.713 30.780  82.796  1.00 32.85  ? 242 TYR A C   1 
ATOM   1783 O O   . TYR A  1 227 ? 29.284 31.374  81.871  1.00 32.59  ? 242 TYR A O   1 
ATOM   1784 C CB  . TYR A  1 227 ? 30.253 30.415  84.756  1.00 31.88  ? 242 TYR A CB  1 
ATOM   1785 C CG  . TYR A  1 227 ? 31.060 29.473  85.612  1.00 31.70  ? 242 TYR A CG  1 
ATOM   1786 C CD1 . TYR A  1 227 ? 32.276 28.963  85.175  1.00 32.69  ? 242 TYR A CD1 1 
ATOM   1787 C CD2 . TYR A  1 227 ? 30.613 29.093  86.866  1.00 32.66  ? 242 TYR A CD2 1 
ATOM   1788 C CE1 . TYR A  1 227 ? 33.020 28.097  85.962  1.00 32.83  ? 242 TYR A CE1 1 
ATOM   1789 C CE2 . TYR A  1 227 ? 31.360 28.252  87.677  1.00 33.45  ? 242 TYR A CE2 1 
ATOM   1790 C CZ  . TYR A  1 227 ? 32.560 27.742  87.220  1.00 33.54  ? 242 TYR A CZ  1 
ATOM   1791 O OH  . TYR A  1 227 ? 33.275 26.897  88.016  1.00 35.03  ? 242 TYR A OH  1 
ATOM   1792 N N   . THR A  1 228 ? 27.444 30.989  83.132  1.00 31.22  ? 243 THR A N   1 
ATOM   1793 C CA  . THR A  1 228 ? 26.674 32.151  82.623  1.00 33.44  ? 243 THR A CA  1 
ATOM   1794 C C   . THR A  1 228 ? 27.291 33.407  83.245  1.00 33.63  ? 243 THR A C   1 
ATOM   1795 O O   . THR A  1 228 ? 27.485 33.405  84.470  1.00 35.52  ? 243 THR A O   1 
ATOM   1796 C CB  . THR A  1 228 ? 25.182 32.012  82.918  1.00 33.38  ? 243 THR A CB  1 
ATOM   1797 O OG1 . THR A  1 228 ? 24.804 30.723  82.439  1.00 33.55  ? 243 THR A OG1 1 
ATOM   1798 C CG2 . THR A  1 228 ? 24.347 33.085  82.257  1.00 34.43  ? 243 THR A CG2 1 
ATOM   1799 N N   . ARG A  1 229 ? 27.633 34.401  82.425  1.00 34.46  ? 244 ARG A N   1 
ATOM   1800 C CA  . ARG A  1 229 ? 28.207 35.698  82.873  1.00 36.01  ? 244 ARG A CA  1 
ATOM   1801 C C   . ARG A  1 229 ? 27.078 36.545  83.477  1.00 35.01  ? 244 ARG A C   1 
ATOM   1802 O O   . ARG A  1 229 ? 26.175 36.934  82.724  1.00 36.14  ? 244 ARG A O   1 
ATOM   1803 C CB  . ARG A  1 229 ? 28.891 36.385  81.690  1.00 38.02  ? 244 ARG A CB  1 
ATOM   1804 C CG  . ARG A  1 229 ? 29.667 37.641  82.060  1.00 41.10  ? 244 ARG A CG  1 
ATOM   1805 C CD  . ARG A  1 229 ? 30.299 38.278  80.840  1.00 42.36  ? 244 ARG A CD  1 
ATOM   1806 N NE  . ARG A  1 229 ? 31.471 37.535  80.404  1.00 45.55  ? 244 ARG A NE  1 
ATOM   1807 C CZ  . ARG A  1 229 ? 32.688 37.602  80.956  1.00 50.06  ? 244 ARG A CZ  1 
ATOM   1808 N NH1 . ARG A  1 229 ? 32.927 38.387  81.997  1.00 51.34  ? 244 ARG A NH1 1 
ATOM   1809 N NH2 . ARG A  1 229 ? 33.670 36.867  80.463  1.00 50.46  ? 244 ARG A NH2 1 
ATOM   1810 N N   . VAL A  1 230 ? 27.096 36.780  84.794  1.00 36.03  ? 245 VAL A N   1 
ATOM   1811 C CA  . VAL A  1 230 ? 25.952 37.431  85.509  1.00 36.65  ? 245 VAL A CA  1 
ATOM   1812 C C   . VAL A  1 230 ? 25.790 38.874  85.006  1.00 36.70  ? 245 VAL A C   1 
ATOM   1813 O O   . VAL A  1 230 ? 24.634 39.285  84.805  1.00 36.30  ? 245 VAL A O   1 
ATOM   1814 C CB  . VAL A  1 230 ? 26.081 37.365  87.042  1.00 36.17  ? 245 VAL A CB  1 
ATOM   1815 C CG1 . VAL A  1 230 ? 25.012 38.201  87.739  1.00 35.52  ? 245 VAL A CG1 1 
ATOM   1816 C CG2 . VAL A  1 230 ? 26.037 35.928  87.540  1.00 37.42  ? 245 VAL A CG2 1 
ATOM   1817 N N   . THR A  1 231 ? 26.888 39.602  84.776  1.00 37.39  ? 246 THR A N   1 
ATOM   1818 C CA  . THR A  1 231 ? 26.853 41.023  84.324  1.00 38.22  ? 246 THR A CA  1 
ATOM   1819 C C   . THR A  1 231 ? 26.045 41.137  83.027  1.00 39.34  ? 246 THR A C   1 
ATOM   1820 O O   . THR A  1 231 ? 25.334 42.146  82.874  1.00 40.51  ? 246 THR A O   1 
ATOM   1821 C CB  . THR A  1 231 ? 28.250 41.629  84.146  1.00 38.38  ? 246 THR A CB  1 
ATOM   1822 O OG1 . THR A  1 231 ? 29.023 40.806  83.273  1.00 37.48  ? 246 THR A OG1 1 
ATOM   1823 C CG2 . THR A  1 231 ? 28.979 41.802  85.461  1.00 39.49  ? 246 THR A CG2 1 
ATOM   1824 N N   . TYR A  1 232 ? 26.115 40.121  82.155  1.00 38.43  ? 247 TYR A N   1 
ATOM   1825 C CA  . TYR A  1 232 ? 25.402 40.074  80.853  1.00 36.23  ? 247 TYR A CA  1 
ATOM   1826 C C   . TYR A  1 232 ? 23.883 40.155  81.058  1.00 35.20  ? 247 TYR A C   1 
ATOM   1827 O O   . TYR A  1 232 ? 23.224 40.779  80.199  1.00 34.84  ? 247 TYR A O   1 
ATOM   1828 C CB  . TYR A  1 232 ? 25.789 38.835  80.039  1.00 35.47  ? 247 TYR A CB  1 
ATOM   1829 C CG  . TYR A  1 232 ? 25.419 38.926  78.582  1.00 34.63  ? 247 TYR A CG  1 
ATOM   1830 C CD1 . TYR A  1 232 ? 24.130 38.644  78.154  1.00 35.79  ? 247 TYR A CD1 1 
ATOM   1831 C CD2 . TYR A  1 232 ? 26.347 39.323  77.630  1.00 34.71  ? 247 TYR A CD2 1 
ATOM   1832 C CE1 . TYR A  1 232 ? 23.766 38.762  76.825  1.00 35.46  ? 247 TYR A CE1 1 
ATOM   1833 C CE2 . TYR A  1 232 ? 26.002 39.429  76.292  1.00 36.44  ? 247 TYR A CE2 1 
ATOM   1834 C CZ  . TYR A  1 232 ? 24.708 39.141  75.889  1.00 37.34  ? 247 TYR A CZ  1 
ATOM   1835 O OH  . TYR A  1 232 ? 24.328 39.246  74.583  1.00 40.97  ? 247 TYR A OH  1 
ATOM   1836 N N   . TYR A  1 233 ? 23.350 39.575  82.137  1.00 36.74  ? 248 TYR A N   1 
ATOM   1837 C CA  . TYR A  1 233 ? 21.887 39.395  82.348  1.00 36.48  ? 248 TYR A CA  1 
ATOM   1838 C C   . TYR A  1 233 ? 21.371 40.216  83.542  1.00 36.56  ? 248 TYR A C   1 
ATOM   1839 O O   . TYR A  1 233 ? 20.224 39.955  83.947  1.00 37.77  ? 248 TYR A O   1 
ATOM   1840 C CB  . TYR A  1 233 ? 21.584 37.897  82.452  1.00 36.32  ? 248 TYR A CB  1 
ATOM   1841 C CG  . TYR A  1 233 ? 21.805 37.169  81.151  1.00 36.85  ? 248 TYR A CG  1 
ATOM   1842 C CD1 . TYR A  1 233 ? 20.971 37.393  80.064  1.00 39.02  ? 248 TYR A CD1 1 
ATOM   1843 C CD2 . TYR A  1 233 ? 22.859 36.281  80.987  1.00 38.06  ? 248 TYR A CD2 1 
ATOM   1844 C CE1 . TYR A  1 233 ? 21.170 36.750  78.853  1.00 38.09  ? 248 TYR A CE1 1 
ATOM   1845 C CE2 . TYR A  1 233 ? 23.065 35.621  79.785  1.00 37.68  ? 248 TYR A CE2 1 
ATOM   1846 C CZ  . TYR A  1 233 ? 22.222 35.862  78.712  1.00 37.46  ? 248 TYR A CZ  1 
ATOM   1847 O OH  . TYR A  1 233 ? 22.418 35.232  77.518  1.00 37.50  ? 248 TYR A OH  1 
ATOM   1848 N N   . LEU A  1 234 ? 22.113 41.224  84.026  1.00 39.82  ? 249 LEU A N   1 
ATOM   1849 C CA  . LEU A  1 234 ? 21.703 42.077  85.184  1.00 39.85  ? 249 LEU A CA  1 
ATOM   1850 C C   . LEU A  1 234 ? 20.352 42.743  84.910  1.00 41.85  ? 249 LEU A C   1 
ATOM   1851 O O   . LEU A  1 234 ? 19.503 42.710  85.814  1.00 44.49  ? 249 LEU A O   1 
ATOM   1852 C CB  . LEU A  1 234 ? 22.764 43.144  85.472  1.00 41.84  ? 249 LEU A CB  1 
ATOM   1853 C CG  . LEU A  1 234 ? 23.989 42.665  86.246  1.00 43.97  ? 249 LEU A CG  1 
ATOM   1854 C CD1 . LEU A  1 234 ? 25.094 43.707  86.174  1.00 44.75  ? 249 LEU A CD1 1 
ATOM   1855 C CD2 . LEU A  1 234 ? 23.650 42.351  87.698  1.00 43.15  ? 249 LEU A CD2 1 
ATOM   1856 N N   . ASP A  1 235 ? 20.162 43.329  83.722  1.00 43.42  ? 250 ASP A N   1 
ATOM   1857 C CA  . ASP A  1 235 ? 18.912 44.043  83.344  1.00 44.22  ? 250 ASP A CA  1 
ATOM   1858 C C   . ASP A  1 235 ? 17.731 43.071  83.391  1.00 43.82  ? 250 ASP A C   1 
ATOM   1859 O O   . ASP A  1 235 ? 16.652 43.485  83.852  1.00 43.23  ? 250 ASP A O   1 
ATOM   1860 C CB  . ASP A  1 235 ? 19.006 44.687  81.957  1.00 46.72  ? 250 ASP A CB  1 
ATOM   1861 C CG  . ASP A  1 235 ? 19.996 45.838  81.865  1.00 50.04  ? 250 ASP A CG  1 
ATOM   1862 O OD1 . ASP A  1 235 ? 20.422 46.335  82.919  1.00 54.56  ? 250 ASP A OD1 1 
ATOM   1863 O OD2 . ASP A  1 235 ? 20.343 46.215  80.732  1.00 59.38  ? 250 ASP A OD2 1 
ATOM   1864 N N   . TRP A  1 236 ? 17.913 41.840  82.902  1.00 41.61  ? 251 TRP A N   1 
ATOM   1865 C CA  . TRP A  1 236 ? 16.867 40.781  82.942  1.00 38.40  ? 251 TRP A CA  1 
ATOM   1866 C C   . TRP A  1 236 ? 16.571 40.400  84.400  1.00 36.64  ? 251 TRP A C   1 
ATOM   1867 O O   . TRP A  1 236 ? 15.395 40.308  84.747  1.00 34.76  ? 251 TRP A O   1 
ATOM   1868 C CB  . TRP A  1 236 ? 17.263 39.566  82.092  1.00 36.33  ? 251 TRP A CB  1 
ATOM   1869 C CG  . TRP A  1 236 ? 16.239 38.476  82.118  1.00 34.70  ? 251 TRP A CG  1 
ATOM   1870 C CD1 . TRP A  1 236 ? 15.122 38.379  81.347  1.00 34.65  ? 251 TRP A CD1 1 
ATOM   1871 C CD2 . TRP A  1 236 ? 16.228 37.326  82.983  1.00 35.55  ? 251 TRP A CD2 1 
ATOM   1872 N NE1 . TRP A  1 236 ? 14.416 37.251  81.673  1.00 35.60  ? 251 TRP A NE1 1 
ATOM   1873 C CE2 . TRP A  1 236 ? 15.069 36.586  82.672  1.00 34.21  ? 251 TRP A CE2 1 
ATOM   1874 C CE3 . TRP A  1 236 ? 17.076 36.857  83.994  1.00 34.42  ? 251 TRP A CE3 1 
ATOM   1875 C CZ2 . TRP A  1 236 ? 14.748 35.395  83.323  1.00 35.43  ? 251 TRP A CZ2 1 
ATOM   1876 C CZ3 . TRP A  1 236 ? 16.757 35.683  84.638  1.00 35.26  ? 251 TRP A CZ3 1 
ATOM   1877 C CH2 . TRP A  1 236 ? 15.610 34.959  84.302  1.00 34.76  ? 251 TRP A CH2 1 
ATOM   1878 N N   . ILE A  1 237 ? 17.601 40.197  85.221  1.00 39.43  ? 252 ILE A N   1 
ATOM   1879 C CA  . ILE A  1 237 ? 17.445 39.853  86.667  1.00 42.76  ? 252 ILE A CA  1 
ATOM   1880 C C   . ILE A  1 237 ? 16.663 40.982  87.358  1.00 44.64  ? 252 ILE A C   1 
ATOM   1881 O O   . ILE A  1 237 ? 15.658 40.679  88.040  1.00 44.91  ? 252 ILE A O   1 
ATOM   1882 C CB  . ILE A  1 237 ? 18.810 39.586  87.337  1.00 42.03  ? 252 ILE A CB  1 
ATOM   1883 C CG1 . ILE A  1 237 ? 19.463 38.312  86.799  1.00 39.96  ? 252 ILE A CG1 1 
ATOM   1884 C CG2 . ILE A  1 237 ? 18.677 39.541  88.857  1.00 42.75  ? 252 ILE A CG2 1 
ATOM   1885 C CD1 . ILE A  1 237 ? 20.932 38.201  87.118  1.00 40.07  ? 252 ILE A CD1 1 
ATOM   1886 N N   . HIS A  1 238 ? 17.093 42.233  87.167  1.00 44.61  ? 253 HIS A N   1 
ATOM   1887 C CA  . HIS A  1 238 ? 16.521 43.443  87.829  1.00 46.69  ? 253 HIS A CA  1 
ATOM   1888 C C   . HIS A  1 238 ? 15.126 43.767  87.286  1.00 44.65  ? 253 HIS A C   1 
ATOM   1889 O O   . HIS A  1 238 ? 14.428 44.571  87.927  1.00 49.07  ? 253 HIS A O   1 
ATOM   1890 C CB  . HIS A  1 238 ? 17.460 44.646  87.697  1.00 45.48  ? 253 HIS A CB  1 
ATOM   1891 C CG  . HIS A  1 238 ? 18.712 44.496  88.485  1.00 47.54  ? 253 HIS A CG  1 
ATOM   1892 N ND1 . HIS A  1 238 ? 19.920 45.019  88.067  1.00 50.13  ? 253 HIS A ND1 1 
ATOM   1893 C CD2 . HIS A  1 238 ? 18.939 43.915  89.684  1.00 49.70  ? 253 HIS A CD2 1 
ATOM   1894 C CE1 . HIS A  1 238 ? 20.846 44.751  88.967  1.00 49.56  ? 253 HIS A CE1 1 
ATOM   1895 N NE2 . HIS A  1 238 ? 20.269 44.076  89.973  1.00 49.67  ? 253 HIS A NE2 1 
ATOM   1896 N N   . HIS A  1 239 ? 14.714 43.168  86.170  1.00 46.38  ? 254 HIS A N   1 
ATOM   1897 C CA  . HIS A  1 239 ? 13.321 43.252  85.661  1.00 46.64  ? 254 HIS A CA  1 
ATOM   1898 C C   . HIS A  1 239 ? 12.350 42.570  86.633  1.00 47.08  ? 254 HIS A C   1 
ATOM   1899 O O   . HIS A  1 239 ? 11.167 42.966  86.660  1.00 49.78  ? 254 HIS A O   1 
ATOM   1900 C CB  . HIS A  1 239 ? 13.226 42.655  84.254  1.00 48.77  ? 254 HIS A CB  1 
ATOM   1901 C CG  . HIS A  1 239 ? 11.925 42.935  83.589  1.00 51.03  ? 254 HIS A CG  1 
ATOM   1902 N ND1 . HIS A  1 239 ? 10.874 42.042  83.626  1.00 52.11  ? 254 HIS A ND1 1 
ATOM   1903 C CD2 . HIS A  1 239 ? 11.499 44.000  82.874  1.00 51.73  ? 254 HIS A CD2 1 
ATOM   1904 C CE1 . HIS A  1 239 ? 9.853  42.540  82.957  1.00 54.16  ? 254 HIS A CE1 1 
ATOM   1905 N NE2 . HIS A  1 239 ? 10.211 43.742  82.482  1.00 53.02  ? 254 HIS A NE2 1 
ATOM   1906 N N   . TYR A  1 240 ? 12.815 41.568  87.394  1.00 46.66  ? 255 TYR A N   1 
ATOM   1907 C CA  . TYR A  1 240 ? 11.992 40.757  88.332  1.00 43.54  ? 255 TYR A CA  1 
ATOM   1908 C C   . TYR A  1 240 ? 12.393 40.997  89.795  1.00 42.38  ? 255 TYR A C   1 
ATOM   1909 O O   . TYR A  1 240 ? 11.488 41.037  90.643  1.00 44.49  ? 255 TYR A O   1 
ATOM   1910 C CB  . TYR A  1 240 ? 12.113 39.279  87.966  1.00 42.54  ? 255 TYR A CB  1 
ATOM   1911 C CG  . TYR A  1 240 ? 11.630 38.964  86.574  1.00 40.13  ? 255 TYR A CG  1 
ATOM   1912 C CD1 . TYR A  1 240 ? 10.277 38.955  86.282  1.00 38.96  ? 255 TYR A CD1 1 
ATOM   1913 C CD2 . TYR A  1 240 ? 12.522 38.732  85.538  1.00 40.67  ? 255 TYR A CD2 1 
ATOM   1914 C CE1 . TYR A  1 240 ? 9.817  38.686  85.007  1.00 40.79  ? 255 TYR A CE1 1 
ATOM   1915 C CE2 . TYR A  1 240 ? 12.080 38.464  84.251  1.00 39.23  ? 255 TYR A CE2 1 
ATOM   1916 C CZ  . TYR A  1 240 ? 10.721 38.437  83.988  1.00 39.80  ? 255 TYR A CZ  1 
ATOM   1917 O OH  . TYR A  1 240 ? 10.245 38.170  82.741  1.00 41.49  ? 255 TYR A OH  1 
ATOM   1918 N N   . VAL A  1 241 ? 13.688 41.110  90.087  1.00 43.17  ? 256 VAL A N   1 
ATOM   1919 C CA  . VAL A  1 241 ? 14.239 41.100  91.475  1.00 45.49  ? 256 VAL A CA  1 
ATOM   1920 C C   . VAL A  1 241 ? 14.458 42.544  91.914  1.00 48.31  ? 256 VAL A C   1 
ATOM   1921 O O   . VAL A  1 241 ? 15.246 43.253  91.291  1.00 46.07  ? 256 VAL A O   1 
ATOM   1922 C CB  . VAL A  1 241 ? 15.545 40.284  91.557  1.00 43.33  ? 256 VAL A CB  1 
ATOM   1923 C CG1 . VAL A  1 241 ? 16.109 40.235  92.971  1.00 42.67  ? 256 VAL A CG1 1 
ATOM   1924 C CG2 . VAL A  1 241 ? 15.347 38.876  91.018  1.00 43.41  ? 256 VAL A CG2 1 
ATOM   1925 N N   . PRO A  1 242 ? 13.791 43.023  92.993  1.00 54.79  ? 257 PRO A N   1 
ATOM   1926 C CA  . PRO A  1 242 ? 14.050 44.363  93.531  1.00 58.35  ? 257 PRO A CA  1 
ATOM   1927 C C   . PRO A  1 242 ? 15.514 44.569  93.946  1.00 62.37  ? 257 PRO A C   1 
ATOM   1928 O O   . PRO A  1 242 ? 16.113 43.642  94.477  1.00 58.38  ? 257 PRO A O   1 
ATOM   1929 C CB  . PRO A  1 242 ? 13.143 44.472  94.764  1.00 57.57  ? 257 PRO A CB  1 
ATOM   1930 C CG  . PRO A  1 242 ? 12.070 43.426  94.539  1.00 58.12  ? 257 PRO A CG  1 
ATOM   1931 C CD  . PRO A  1 242 ? 12.743 42.320  93.751  1.00 56.45  ? 257 PRO A CD  1 
ATOM   1932 N N   . LYS A  1 243 ? 16.063 45.745  93.633  1.00 68.71  ? 258 LYS A N   1 
ATOM   1933 C CA  . LYS A  1 243 ? 17.463 46.117  93.972  1.00 74.66  ? 258 LYS A CA  1 
ATOM   1934 C C   . LYS A  1 243 ? 17.561 46.300  95.491  1.00 78.41  ? 258 LYS A C   1 
ATOM   1935 O O   . LYS A  1 243 ? 16.516 46.569  96.125  1.00 78.95  ? 258 LYS A O   1 
ATOM   1936 C CB  . LYS A  1 243 ? 17.894 47.370  93.201  1.00 75.24  ? 258 LYS A CB  1 
ATOM   1937 C CG  . LYS A  1 243 ? 17.983 47.191  91.690  1.00 74.07  ? 258 LYS A CG  1 
ATOM   1938 C CD  . LYS A  1 243 ? 18.432 48.394  90.921  0.00 76.96  ? 258 LYS A CD  1 
ATOM   1939 C CE  . LYS A  1 243 ? 18.580 48.131  89.437  0.00 76.86  ? 258 LYS A CE  1 
ATOM   1940 N NZ  . LYS A  1 243 ? 18.999 49.347  88.701  0.00 76.82  ? 258 LYS A NZ  1 
ATOM   1941 N N   . LYS A  1 244 ? 18.766 46.136  96.051  1.00 79.26  ? 259 LYS A N   1 
ATOM   1942 C CA  . LYS A  1 244 ? 19.051 46.347  97.499  1.00 78.77  ? 259 LYS A CA  1 
ATOM   1943 C C   . LYS A  1 244 ? 18.946 47.845  97.809  1.00 77.94  ? 259 LYS A C   1 
ATOM   1944 O O   . LYS A  1 244 ? 18.108 48.280  98.598  1.00 76.24  ? 259 LYS A O   1 
ATOM   1945 C CB  . LYS A  1 244 ? 20.434 45.804  97.875  1.00 76.76  ? 259 LYS A CB  1 
ATOM   1946 C CG  . LYS A  1 244 ? 20.810 45.849  99.346  0.00 79.85  ? 259 LYS A CG  1 
ATOM   1947 C CD  . LYS A  1 244 ? 22.150 45.214  99.652  0.00 79.71  ? 259 LYS A CD  1 
ATOM   1948 C CE  . LYS A  1 244 ? 22.595 45.423  101.084 0.00 79.60  ? 259 LYS A CE  1 
ATOM   1949 N NZ  . LYS A  1 244 ? 23.922 44.815  101.339 0.00 79.54  ? 259 LYS A NZ  1 
ATOM   1950 N N   . ILE B  1 1   ? 14.943 -2.362  106.266 1.00 35.77  ? 16  ILE B N   1 
ATOM   1951 C CA  . ILE B  1 1   ? 13.723 -2.742  107.047 1.00 36.12  ? 16  ILE B CA  1 
ATOM   1952 C C   . ILE B  1 1   ? 12.475 -2.417  106.212 1.00 35.79  ? 16  ILE B C   1 
ATOM   1953 O O   . ILE B  1 1   ? 12.350 -1.268  105.752 1.00 33.71  ? 16  ILE B O   1 
ATOM   1954 C CB  . ILE B  1 1   ? 13.705 -2.047  108.427 1.00 37.41  ? 16  ILE B CB  1 
ATOM   1955 C CG1 . ILE B  1 1   ? 14.907 -2.440  109.300 1.00 37.46  ? 16  ILE B CG1 1 
ATOM   1956 C CG2 . ILE B  1 1   ? 12.392 -2.295  109.157 1.00 36.97  ? 16  ILE B CG2 1 
ATOM   1957 C CD1 . ILE B  1 1   ? 14.936 -3.892  109.738 1.00 36.87  ? 16  ILE B CD1 1 
ATOM   1958 N N   . VAL B  1 2   ? 11.588 -3.400  106.036 1.00 36.71  ? 17  VAL B N   1 
ATOM   1959 C CA  . VAL B  1 2   ? 10.301 -3.267  105.296 1.00 36.63  ? 17  VAL B CA  1 
ATOM   1960 C C   . VAL B  1 2   ? 9.179  -3.040  106.314 1.00 36.57  ? 17  VAL B C   1 
ATOM   1961 O O   . VAL B  1 2   ? 9.099  -3.816  107.284 1.00 36.17  ? 17  VAL B O   1 
ATOM   1962 C CB  . VAL B  1 2   ? 10.017 -4.499  104.417 1.00 36.50  ? 17  VAL B CB  1 
ATOM   1963 C CG1 . VAL B  1 2   ? 8.756  -4.310  103.589 1.00 36.63  ? 17  VAL B CG1 1 
ATOM   1964 C CG2 . VAL B  1 2   ? 11.194 -4.843  103.515 1.00 37.89  ? 17  VAL B CG2 1 
ATOM   1965 N N   . GLY B  1 3   ? 8.341  -2.030  106.072 1.00 37.75  ? 18  GLY B N   1 
ATOM   1966 C CA  . GLY B  1 3   ? 7.129  -1.717  106.852 1.00 38.20  ? 18  GLY B CA  1 
ATOM   1967 C C   . GLY B  1 3   ? 7.453  -1.189  108.232 1.00 40.81  ? 18  GLY B C   1 
ATOM   1968 O O   . GLY B  1 3   ? 6.595  -1.309  109.130 1.00 47.26  ? 18  GLY B O   1 
ATOM   1969 N N   . GLY B  1 4   ? 8.641  -0.618  108.405 1.00 41.00  ? 19  GLY B N   1 
ATOM   1970 C CA  . GLY B  1 4   ? 9.114  -0.140  109.711 1.00 47.76  ? 19  GLY B CA  1 
ATOM   1971 C C   . GLY B  1 4   ? 8.715  1.298   109.987 1.00 46.59  ? 19  GLY B C   1 
ATOM   1972 O O   . GLY B  1 4   ? 7.928  1.869   109.211 1.00 49.57  ? 19  GLY B O   1 
ATOM   1973 N N   . GLN B  1 5   ? 9.244  1.854   111.075 1.00 44.36  ? 20  GLN B N   1 
ATOM   1974 C CA  . GLN B  1 5   ? 9.338  3.320   111.300 1.00 46.20  ? 20  GLN B CA  1 
ATOM   1975 C C   . GLN B  1 5   ? 10.764 3.636   111.740 1.00 42.94  ? 20  GLN B C   1 
ATOM   1976 O O   . GLN B  1 5   ? 11.495 2.689   112.086 1.00 40.27  ? 20  GLN B O   1 
ATOM   1977 C CB  . GLN B  1 5   ? 8.308  3.783   112.327 1.00 51.38  ? 20  GLN B CB  1 
ATOM   1978 C CG  . GLN B  1 5   ? 8.480  3.174   113.709 1.00 56.59  ? 20  GLN B CG  1 
ATOM   1979 C CD  . GLN B  1 5   ? 7.310  3.505   114.604 1.00 61.90  ? 20  GLN B CD  1 
ATOM   1980 O OE1 . GLN B  1 5   ? 7.418  4.296   115.539 1.00 62.28  ? 20  GLN B OE1 1 
ATOM   1981 N NE2 . GLN B  1 5   ? 6.164  2.918   114.302 1.00 66.81  ? 20  GLN B NE2 1 
ATOM   1982 N N   . GLU B  1 6   ? 11.134 4.915   111.715 1.00 41.26  ? 21  GLU B N   1 
ATOM   1983 C CA  . GLU B  1 6   ? 12.409 5.411   112.284 1.00 41.45  ? 21  GLU B CA  1 
ATOM   1984 C C   . GLU B  1 6   ? 12.428 5.053   113.774 1.00 39.09  ? 21  GLU B C   1 
ATOM   1985 O O   . GLU B  1 6   ? 11.401 5.266   114.448 1.00 40.99  ? 21  GLU B O   1 
ATOM   1986 C CB  . GLU B  1 6   ? 12.549 6.916   112.050 1.00 42.53  ? 21  GLU B CB  1 
ATOM   1987 C CG  . GLU B  1 6   ? 13.804 7.502   112.678 1.00 45.80  ? 21  GLU B CG  1 
ATOM   1988 C CD  . GLU B  1 6   ? 14.210 8.887   112.207 1.00 45.89  ? 21  GLU B CD  1 
ATOM   1989 O OE1 . GLU B  1 6   ? 13.566 9.405   111.256 1.00 45.65  ? 21  GLU B OE1 1 
ATOM   1990 O OE2 . GLU B  1 6   ? 15.182 9.435   112.786 1.00 45.54  ? 21  GLU B OE2 1 
ATOM   1991 N N   . ALA B  1 7   ? 13.536 4.489   114.247 1.00 37.13  ? 22  ALA B N   1 
ATOM   1992 C CA  . ALA B  1 7   ? 13.754 4.141   115.669 1.00 38.68  ? 22  ALA B CA  1 
ATOM   1993 C C   . ALA B  1 7   ? 13.848 5.430   116.477 1.00 38.40  ? 22  ALA B C   1 
ATOM   1994 O O   . ALA B  1 7   ? 14.502 6.379   116.043 1.00 38.23  ? 22  ALA B O   1 
ATOM   1995 C CB  . ALA B  1 7   ? 15.001 3.310   115.830 1.00 39.24  ? 22  ALA B CB  1 
ATOM   1996 N N   . PRO B  1 8   ? 13.193 5.529   117.654 1.00 39.54  ? 23  PRO B N   1 
ATOM   1997 C CA  . PRO B  1 8   ? 13.524 6.587   118.607 1.00 38.99  ? 23  PRO B CA  1 
ATOM   1998 C C   . PRO B  1 8   ? 14.997 6.476   119.033 1.00 39.29  ? 23  PRO B C   1 
ATOM   1999 O O   . PRO B  1 8   ? 15.521 5.374   119.091 1.00 36.22  ? 23  PRO B O   1 
ATOM   2000 C CB  . PRO B  1 8   ? 12.557 6.379   119.783 1.00 39.54  ? 23  PRO B CB  1 
ATOM   2001 C CG  . PRO B  1 8   ? 11.446 5.499   119.226 1.00 40.11  ? 23  PRO B CG  1 
ATOM   2002 C CD  . PRO B  1 8   ? 12.090 4.674   118.125 1.00 40.13  ? 23  PRO B CD  1 
ATOM   2003 N N   . ARG B  1 9   ? 15.605 7.625   119.331 1.00 38.94  ? 24  ARG B N   1 
ATOM   2004 C CA  . ARG B  1 9   ? 17.045 7.800   119.682 1.00 40.98  ? 24  ARG B CA  1 
ATOM   2005 C C   . ARG B  1 9   ? 17.424 6.918   120.881 1.00 38.90  ? 24  ARG B C   1 
ATOM   2006 O O   . ARG B  1 9   ? 18.572 6.463   120.927 1.00 42.37  ? 24  ARG B O   1 
ATOM   2007 C CB  . ARG B  1 9   ? 17.382 9.263   120.002 1.00 44.01  ? 24  ARG B CB  1 
ATOM   2008 C CG  . ARG B  1 9   ? 16.854 10.297  119.014 1.00 50.64  ? 24  ARG B CG  1 
ATOM   2009 C CD  . ARG B  1 9   ? 17.416 11.683  119.261 1.00 55.17  ? 24  ARG B CD  1 
ATOM   2010 N NE  . ARG B  1 9   ? 18.745 11.799  118.673 1.00 58.81  ? 24  ARG B NE  1 
ATOM   2011 C CZ  . ARG B  1 9   ? 19.018 12.124  117.407 1.00 58.39  ? 24  ARG B CZ  1 
ATOM   2012 N NH1 . ARG B  1 9   ? 18.055 12.398  116.538 1.00 62.41  ? 24  ARG B NH1 1 
ATOM   2013 N NH2 . ARG B  1 9   ? 20.277 12.179  117.012 1.00 57.85  ? 24  ARG B NH2 1 
ATOM   2014 N N   . SER B  1 10  ? 16.499 6.699   121.816 1.00 37.52  ? 25  SER B N   1 
ATOM   2015 C CA  . SER B  1 10  ? 16.697 5.936   123.076 1.00 41.36  ? 25  SER B CA  1 
ATOM   2016 C C   . SER B  1 10  ? 16.685 4.416   122.844 1.00 41.73  ? 25  SER B C   1 
ATOM   2017 O O   . SER B  1 10  ? 17.085 3.692   123.781 1.00 44.38  ? 25  SER B O   1 
ATOM   2018 C CB  . SER B  1 10  ? 15.650 6.332   124.090 1.00 41.20  ? 25  SER B CB  1 
ATOM   2019 O OG  . SER B  1 10  ? 14.342 6.089   123.584 1.00 44.29  ? 25  SER B OG  1 
ATOM   2020 N N   . LYS B  1 11  ? 16.228 3.928   121.681 1.00 41.62  ? 26  LYS B N   1 
ATOM   2021 C CA  . LYS B  1 11  ? 16.033 2.475   121.411 1.00 39.64  ? 26  LYS B CA  1 
ATOM   2022 C C   . LYS B  1 11  ? 17.255 1.881   120.704 1.00 36.90  ? 26  LYS B C   1 
ATOM   2023 O O   . LYS B  1 11  ? 17.882 2.579   119.890 1.00 36.38  ? 26  LYS B O   1 
ATOM   2024 C CB  . LYS B  1 11  ? 14.781 2.202   120.575 1.00 41.25  ? 26  LYS B CB  1 
ATOM   2025 C CG  . LYS B  1 11  ? 13.498 2.842   121.075 1.00 46.28  ? 26  LYS B CG  1 
ATOM   2026 C CD  . LYS B  1 11  ? 13.204 2.583   122.518 1.00 49.35  ? 26  LYS B CD  1 
ATOM   2027 C CE  . LYS B  1 11  ? 11.757 2.849   122.872 1.00 52.43  ? 26  LYS B CE  1 
ATOM   2028 N NZ  . LYS B  1 11  ? 11.548 2.724   124.332 1.00 54.84  ? 26  LYS B NZ  1 
ATOM   2029 N N   . TRP B  1 12  ? 17.538 0.607   120.997 1.00 36.08  ? 27  TRP B N   1 
ATOM   2030 C CA  . TRP B  1 12  ? 18.518 -0.268  120.300 1.00 33.59  ? 27  TRP B CA  1 
ATOM   2031 C C   . TRP B  1 12  ? 19.933 0.289   120.435 1.00 33.20  ? 27  TRP B C   1 
ATOM   2032 O O   . TRP B  1 12  ? 20.605 0.556   119.435 1.00 33.90  ? 27  TRP B O   1 
ATOM   2033 C CB  . TRP B  1 12  ? 18.118 -0.469  118.834 1.00 34.35  ? 27  TRP B CB  1 
ATOM   2034 C CG  . TRP B  1 12  ? 16.646 -0.447  118.582 1.00 33.45  ? 27  TRP B CG  1 
ATOM   2035 C CD1 . TRP B  1 12  ? 15.996 0.415   117.756 1.00 33.51  ? 27  TRP B CD1 1 
ATOM   2036 C CD2 . TRP B  1 12  ? 15.633 -1.285  119.169 1.00 35.64  ? 27  TRP B CD2 1 
ATOM   2037 N NE1 . TRP B  1 12  ? 14.656 0.164   117.774 1.00 33.99  ? 27  TRP B NE1 1 
ATOM   2038 C CE2 . TRP B  1 12  ? 14.396 -0.875  118.624 1.00 34.32  ? 27  TRP B CE2 1 
ATOM   2039 C CE3 . TRP B  1 12  ? 15.644 -2.340  120.091 1.00 34.25  ? 27  TRP B CE3 1 
ATOM   2040 C CZ2 . TRP B  1 12  ? 13.186 -1.484  118.968 1.00 34.87  ? 27  TRP B CZ2 1 
ATOM   2041 C CZ3 . TRP B  1 12  ? 14.450 -2.942  120.435 1.00 35.69  ? 27  TRP B CZ3 1 
ATOM   2042 C CH2 . TRP B  1 12  ? 13.239 -2.523  119.873 1.00 35.21  ? 27  TRP B CH2 1 
ATOM   2043 N N   . PRO B  1 13  ? 20.442 0.467   121.677 1.00 33.66  ? 28  PRO B N   1 
ATOM   2044 C CA  . PRO B  1 13  ? 21.793 0.999   121.887 1.00 33.83  ? 28  PRO B CA  1 
ATOM   2045 C C   . PRO B  1 13  ? 22.935 0.043   121.494 1.00 33.02  ? 28  PRO B C   1 
ATOM   2046 O O   . PRO B  1 13  ? 24.073 0.469   121.479 1.00 32.28  ? 28  PRO B O   1 
ATOM   2047 C CB  . PRO B  1 13  ? 21.805 1.307   123.392 1.00 34.44  ? 28  PRO B CB  1 
ATOM   2048 C CG  . PRO B  1 13  ? 20.833 0.310   123.987 1.00 35.04  ? 28  PRO B CG  1 
ATOM   2049 C CD  . PRO B  1 13  ? 19.749 0.176   122.944 1.00 34.44  ? 28  PRO B CD  1 
ATOM   2050 N N   . TRP B  1 14  ? 22.593 -1.193  121.119 1.00 31.64  ? 29  TRP B N   1 
ATOM   2051 C CA  . TRP B  1 14  ? 23.524 -2.279  120.712 1.00 30.35  ? 29  TRP B CA  1 
ATOM   2052 C C   . TRP B  1 14  ? 23.680 -2.360  119.188 1.00 30.17  ? 29  TRP B C   1 
ATOM   2053 O O   . TRP B  1 14  ? 24.600 -3.072  118.761 1.00 29.69  ? 29  TRP B O   1 
ATOM   2054 C CB  . TRP B  1 14  ? 23.038 -3.613  121.283 1.00 29.34  ? 29  TRP B CB  1 
ATOM   2055 C CG  . TRP B  1 14  ? 21.585 -3.863  121.043 1.00 28.71  ? 29  TRP B CG  1 
ATOM   2056 C CD1 . TRP B  1 14  ? 20.992 -4.205  119.867 1.00 29.05  ? 29  TRP B CD1 1 
ATOM   2057 C CD2 . TRP B  1 14  ? 20.532 -3.762  122.013 1.00 29.50  ? 29  TRP B CD2 1 
ATOM   2058 N NE1 . TRP B  1 14  ? 19.642 -4.328  120.039 1.00 30.37  ? 29  TRP B NE1 1 
ATOM   2059 C CE2 . TRP B  1 14  ? 19.329 -4.075  121.345 1.00 30.04  ? 29  TRP B CE2 1 
ATOM   2060 C CE3 . TRP B  1 14  ? 20.486 -3.436  123.372 1.00 28.60  ? 29  TRP B CE3 1 
ATOM   2061 C CZ2 . TRP B  1 14  ? 18.098 -4.085  121.996 1.00 31.20  ? 29  TRP B CZ2 1 
ATOM   2062 C CZ3 . TRP B  1 14  ? 19.268 -3.447  124.015 1.00 30.70  ? 29  TRP B CZ3 1 
ATOM   2063 C CH2 . TRP B  1 14  ? 18.090 -3.756  123.331 1.00 30.45  ? 29  TRP B CH2 1 
ATOM   2064 N N   . GLN B  1 15  ? 22.818 -1.696  118.403 1.00 30.92  ? 30  GLN B N   1 
ATOM   2065 C CA  . GLN B  1 15  ? 22.871 -1.718  116.915 1.00 32.28  ? 30  GLN B CA  1 
ATOM   2066 C C   . GLN B  1 15  ? 24.216 -1.140  116.465 1.00 33.61  ? 30  GLN B C   1 
ATOM   2067 O O   . GLN B  1 15  ? 24.596 -0.077  116.979 1.00 37.80  ? 30  GLN B O   1 
ATOM   2068 C CB  . GLN B  1 15  ? 21.714 -0.931  116.291 1.00 33.26  ? 30  GLN B CB  1 
ATOM   2069 C CG  . GLN B  1 15  ? 21.695 -0.961  114.764 1.00 33.33  ? 30  GLN B CG  1 
ATOM   2070 C CD  . GLN B  1 15  ? 21.252 -2.294  114.201 1.00 32.96  ? 30  GLN B CD  1 
ATOM   2071 O OE1 . GLN B  1 15  ? 20.189 -2.800  114.541 1.00 33.53  ? 30  GLN B OE1 1 
ATOM   2072 N NE2 . GLN B  1 15  ? 22.057 -2.872  113.321 1.00 33.28  ? 30  GLN B NE2 1 
ATOM   2073 N N   . VAL B  1 16  ? 24.920 -1.842  115.580 1.00 32.89  ? 31  VAL B N   1 
ATOM   2074 C CA  . VAL B  1 16  ? 26.173 -1.361  114.936 1.00 33.44  ? 31  VAL B CA  1 
ATOM   2075 C C   . VAL B  1 16  ? 26.020 -1.490  113.420 1.00 32.35  ? 31  VAL B C   1 
ATOM   2076 O O   . VAL B  1 16  ? 25.169 -2.278  112.945 1.00 31.66  ? 31  VAL B O   1 
ATOM   2077 C CB  . VAL B  1 16  ? 27.434 -2.077  115.463 1.00 36.02  ? 31  VAL B CB  1 
ATOM   2078 C CG1 . VAL B  1 16  ? 27.403 -2.249  116.972 1.00 37.13  ? 31  VAL B CG1 1 
ATOM   2079 C CG2 . VAL B  1 16  ? 27.689 -3.417  114.802 1.00 36.14  ? 31  VAL B CG2 1 
ATOM   2080 N N   . SER B  1 17  ? 26.798 -0.680  112.705 1.00 31.25  ? 32  SER B N   1 
ATOM   2081 C CA  . SER B  1 17  ? 26.926 -0.669  111.232 1.00 30.06  ? 32  SER B CA  1 
ATOM   2082 C C   . SER B  1 17  ? 28.320 -1.196  110.888 1.00 31.22  ? 32  SER B C   1 
ATOM   2083 O O   . SER B  1 17  ? 29.296 -0.700  111.504 1.00 31.25  ? 32  SER B O   1 
ATOM   2084 C CB  . SER B  1 17  ? 26.677 0.731   110.707 1.00 29.56  ? 32  SER B CB  1 
ATOM   2085 O OG  . SER B  1 17  ? 27.068 0.846   109.351 1.00 29.47  ? 32  SER B OG  1 
ATOM   2086 N N   . LEU B  1 18  ? 28.415 -2.187  109.994 1.00 30.61  ? 33  LEU B N   1 
ATOM   2087 C CA  . LEU B  1 18  ? 29.710 -2.656  109.432 1.00 31.20  ? 33  LEU B CA  1 
ATOM   2088 C C   . LEU B  1 18  ? 30.010 -1.849  108.169 1.00 30.74  ? 33  LEU B C   1 
ATOM   2089 O O   . LEU B  1 18  ? 29.093 -1.691  107.361 1.00 30.87  ? 33  LEU B O   1 
ATOM   2090 C CB  . LEU B  1 18  ? 29.637 -4.156  109.125 1.00 33.28  ? 33  LEU B CB  1 
ATOM   2091 C CG  . LEU B  1 18  ? 29.276 -5.090  110.283 1.00 34.93  ? 33  LEU B CG  1 
ATOM   2092 C CD1 . LEU B  1 18  ? 29.693 -6.517  109.952 1.00 35.26  ? 33  LEU B CD1 1 
ATOM   2093 C CD2 . LEU B  1 18  ? 29.913 -4.660  111.598 1.00 36.45  ? 33  LEU B CD2 1 
ATOM   2094 N N   . ARG B  1 19  ? 31.242 -1.353  108.029 1.00 30.44  ? 34  ARG B N   1 
ATOM   2095 C CA  . ARG B  1 19  ? 31.671 -0.472  106.913 1.00 31.15  ? 34  ARG B CA  1 
ATOM   2096 C C   . ARG B  1 19  ? 32.816 -1.134  106.145 1.00 32.21  ? 34  ARG B C   1 
ATOM   2097 O O   . ARG B  1 19  ? 33.718 -1.697  106.793 1.00 32.22  ? 34  ARG B O   1 
ATOM   2098 C CB  . ARG B  1 19  ? 32.108 0.903   107.425 1.00 30.09  ? 34  ARG B CB  1 
ATOM   2099 C CG  . ARG B  1 19  ? 31.082 1.603   108.297 1.00 29.70  ? 34  ARG B CG  1 
ATOM   2100 C CD  . ARG B  1 19  ? 29.738 1.822   107.631 1.00 30.59  ? 34  ARG B CD  1 
ATOM   2101 N NE  . ARG B  1 19  ? 28.907 2.721   108.422 1.00 30.54  ? 34  ARG B NE  1 
ATOM   2102 C CZ  . ARG B  1 19  ? 29.096 4.039   108.545 1.00 29.71  ? 34  ARG B CZ  1 
ATOM   2103 N NH1 . ARG B  1 19  ? 30.071 4.651   107.894 1.00 29.23  ? 34  ARG B NH1 1 
ATOM   2104 N NH2 . ARG B  1 19  ? 28.299 4.748   109.327 1.00 30.23  ? 34  ARG B NH2 1 
ATOM   2105 N N   . VAL B  1 20  ? 32.763 -1.059  104.813 1.00 33.87  ? 35  VAL B N   1 
ATOM   2106 C CA  . VAL B  1 20  ? 33.808 -1.573  103.880 1.00 34.57  ? 35  VAL B CA  1 
ATOM   2107 C C   . VAL B  1 20  ? 34.489 -0.361  103.237 1.00 35.58  ? 35  VAL B C   1 
ATOM   2108 O O   . VAL B  1 20  ? 33.785 0.608   102.913 1.00 35.35  ? 35  VAL B O   1 
ATOM   2109 C CB  . VAL B  1 20  ? 33.226 -2.554  102.839 1.00 34.34  ? 35  VAL B CB  1 
ATOM   2110 C CG1 . VAL B  1 20  ? 32.159 -1.941  101.942 1.00 34.41  ? 35  VAL B CG1 1 
ATOM   2111 C CG2 . VAL B  1 20  ? 34.324 -3.177  101.995 1.00 35.44  ? 35  VAL B CG2 1 
ATOM   2112 N N   . HIS B  1 21  ? 35.811 -0.415  103.068 1.00 41.23  ? 36  HIS B N   1 
ATOM   2113 C CA  . HIS B  1 21  ? 36.621 0.665   102.445 1.00 43.81  ? 36  HIS B CA  1 
ATOM   2114 C C   . HIS B  1 21  ? 36.292 0.727   100.952 1.00 42.20  ? 36  HIS B C   1 
ATOM   2115 O O   . HIS B  1 21  ? 36.292 -0.323  100.304 1.00 46.21  ? 36  HIS B O   1 
ATOM   2116 C CB  . HIS B  1 21  ? 38.115 0.456   102.698 1.00 48.20  ? 36  HIS B CB  1 
ATOM   2117 C CG  . HIS B  1 21  ? 38.944 1.571   102.164 1.00 53.62  ? 36  HIS B CG  1 
ATOM   2118 N ND1 . HIS B  1 21  ? 39.387 1.578   100.860 1.00 57.84  ? 36  HIS B ND1 1 
ATOM   2119 C CD2 . HIS B  1 21  ? 39.366 2.728   102.721 1.00 57.37  ? 36  HIS B CD2 1 
ATOM   2120 C CE1 . HIS B  1 21  ? 40.073 2.683   100.637 1.00 59.64  ? 36  HIS B CE1 1 
ATOM   2121 N NE2 . HIS B  1 21  ? 40.073 3.408   101.768 1.00 60.74  ? 36  HIS B NE2 1 
ATOM   2122 N N   . GLY B  1 22  ? 36.002 1.919   100.445 1.00 43.75  ? 37  GLY B N   1 
ATOM   2123 C CA  . GLY B  1 22  ? 35.874 2.195   99.004  1.00 44.95  ? 37  GLY B CA  1 
ATOM   2124 C C   . GLY B  1 22  ? 36.017 3.688   98.756  1.00 45.34  ? 37  GLY B C   1 
ATOM   2125 O O   . GLY B  1 22  ? 36.833 4.329   99.415  1.00 47.84  ? 37  GLY B O   1 
ATOM   2126 N N   . PRO B  1 23  ? 35.232 4.277   97.824  1.00 44.56  ? 38  PRO B N   1 
ATOM   2127 C CA  . PRO B  1 23  ? 35.146 5.732   97.693  1.00 46.55  ? 38  PRO B CA  1 
ATOM   2128 C C   . PRO B  1 23  ? 34.828 6.410   99.036  1.00 45.86  ? 38  PRO B C   1 
ATOM   2129 O O   . PRO B  1 23  ? 35.323 7.495   99.278  1.00 49.94  ? 38  PRO B O   1 
ATOM   2130 C CB  . PRO B  1 23  ? 33.997 5.930   96.690  1.00 47.74  ? 38  PRO B CB  1 
ATOM   2131 C CG  . PRO B  1 23  ? 34.002 4.666   95.867  1.00 48.19  ? 38  PRO B CG  1 
ATOM   2132 C CD  . PRO B  1 23  ? 34.382 3.577   96.848  1.00 47.90  ? 38  PRO B CD  1 
ATOM   2133 N N   . TYR B  1 24  ? 34.006 5.749   99.863  1.00 42.23  ? 39  TYR B N   1 
ATOM   2134 C CA  . TYR B  1 24  ? 33.744 6.098   101.285 1.00 38.69  ? 39  TYR B CA  1 
ATOM   2135 C C   . TYR B  1 24  ? 33.558 4.813   102.103 1.00 38.62  ? 39  TYR B C   1 
ATOM   2136 O O   . TYR B  1 24  ? 33.517 3.715   101.509 1.00 36.68  ? 39  TYR B O   1 
ATOM   2137 C CB  . TYR B  1 24  ? 32.533 7.029   101.393 1.00 38.17  ? 39  TYR B CB  1 
ATOM   2138 C CG  . TYR B  1 24  ? 31.215 6.440   100.961 1.00 36.97  ? 39  TYR B CG  1 
ATOM   2139 C CD1 . TYR B  1 24  ? 30.898 6.269   99.619  1.00 36.91  ? 39  TYR B CD1 1 
ATOM   2140 C CD2 . TYR B  1 24  ? 30.260 6.084   101.902 1.00 36.87  ? 39  TYR B CD2 1 
ATOM   2141 C CE1 . TYR B  1 24  ? 29.676 5.740   99.225  1.00 37.49  ? 39  TYR B CE1 1 
ATOM   2142 C CE2 . TYR B  1 24  ? 29.036 5.551   101.525 1.00 37.02  ? 39  TYR B CE2 1 
ATOM   2143 C CZ  . TYR B  1 24  ? 28.743 5.378   100.184 1.00 36.81  ? 39  TYR B CZ  1 
ATOM   2144 O OH  . TYR B  1 24  ? 27.538 4.851   99.825  1.00 36.47  ? 39  TYR B OH  1 
ATOM   2145 N N   . TRP B  1 25  ? 33.471 4.952   103.428 1.00 36.49  ? 40  TRP B N   1 
ATOM   2146 C CA  . TRP B  1 25  ? 33.265 3.821   104.367 1.00 36.21  ? 40  TRP B CA  1 
ATOM   2147 C C   . TRP B  1 25  ? 31.782 3.442   104.358 1.00 35.03  ? 40  TRP B C   1 
ATOM   2148 O O   . TRP B  1 25  ? 31.015 3.995   105.165 1.00 33.10  ? 40  TRP B O   1 
ATOM   2149 C CB  . TRP B  1 25  ? 33.791 4.160   105.762 1.00 36.57  ? 40  TRP B CB  1 
ATOM   2150 C CG  . TRP B  1 25  ? 35.284 4.124   105.829 1.00 36.28  ? 40  TRP B CG  1 
ATOM   2151 C CD1 . TRP B  1 25  ? 36.138 5.183   105.730 1.00 34.92  ? 40  TRP B CD1 1 
ATOM   2152 C CD2 . TRP B  1 25  ? 36.106 2.952   105.961 1.00 36.10  ? 40  TRP B CD2 1 
ATOM   2153 N NE1 . TRP B  1 25  ? 37.434 4.754   105.822 1.00 33.40  ? 40  TRP B NE1 1 
ATOM   2154 C CE2 . TRP B  1 25  ? 37.447 3.392   105.966 1.00 36.11  ? 40  TRP B CE2 1 
ATOM   2155 C CE3 . TRP B  1 25  ? 35.842 1.584   106.094 1.00 37.17  ? 40  TRP B CE3 1 
ATOM   2156 C CZ2 . TRP B  1 25  ? 38.516 2.506   106.094 1.00 35.85  ? 40  TRP B CZ2 1 
ATOM   2157 C CZ3 . TRP B  1 25  ? 36.899 0.706   106.206 1.00 38.43  ? 40  TRP B CZ3 1 
ATOM   2158 C CH2 . TRP B  1 25  ? 38.218 1.167   106.219 1.00 38.11  ? 40  TRP B CH2 1 
ATOM   2159 N N   . MET B  1 26  ? 31.408 2.553   103.440 1.00 35.39  ? 41  MET B N   1 
ATOM   2160 C CA  . MET B  1 26  ? 29.991 2.267   103.095 1.00 37.32  ? 41  MET B CA  1 
ATOM   2161 C C   . MET B  1 26  ? 29.453 1.153   104.002 1.00 33.99  ? 41  MET B C   1 
ATOM   2162 O O   . MET B  1 26  ? 30.142 0.141   104.182 1.00 30.66  ? 41  MET B O   1 
ATOM   2163 C CB  . MET B  1 26  ? 29.863 1.859   101.625 1.00 41.18  ? 41  MET B CB  1 
ATOM   2164 C CG  . MET B  1 26  ? 28.429 1.776   101.130 1.00 45.96  ? 41  MET B CG  1 
ATOM   2165 S SD  . MET B  1 26  ? 28.307 1.386   99.365  1.00 49.95  ? 41  MET B SD  1 
ATOM   2166 C CE  . MET B  1 26  ? 29.031 -0.253  99.344  1.00 50.50  ? 41  MET B CE  1 
ATOM   2167 N N   . HIS B  1 27  ? 28.246 1.349   104.535 1.00 33.28  ? 42  HIS B N   1 
ATOM   2168 C CA  . HIS B  1 27  ? 27.427 0.324   105.227 1.00 32.41  ? 42  HIS B CA  1 
ATOM   2169 C C   . HIS B  1 27  ? 27.158 -0.853  104.281 1.00 31.86  ? 42  HIS B C   1 
ATOM   2170 O O   . HIS B  1 27  ? 26.702 -0.601  103.166 1.00 32.54  ? 42  HIS B O   1 
ATOM   2171 C CB  . HIS B  1 27  ? 26.124 0.942   105.746 1.00 31.40  ? 42  HIS B CB  1 
ATOM   2172 C CG  . HIS B  1 27  ? 25.202 -0.069  106.328 1.00 30.49  ? 42  HIS B CG  1 
ATOM   2173 N ND1 . HIS B  1 27  ? 25.199 -0.365  107.660 1.00 28.90  ? 42  HIS B ND1 1 
ATOM   2174 C CD2 . HIS B  1 27  ? 24.289 -0.884  105.754 1.00 31.08  ? 42  HIS B CD2 1 
ATOM   2175 C CE1 . HIS B  1 27  ? 24.303 -1.300  107.900 1.00 30.16  ? 42  HIS B CE1 1 
ATOM   2176 N NE2 . HIS B  1 27  ? 23.732 -1.638  106.750 1.00 28.88  ? 42  HIS B NE2 1 
ATOM   2177 N N   . PHE B  1 28  ? 27.454 -2.087  104.709 1.00 33.03  ? 43  PHE B N   1 
ATOM   2178 C CA  . PHE B  1 28  ? 27.096 -3.336  103.975 1.00 35.27  ? 43  PHE B CA  1 
ATOM   2179 C C   . PHE B  1 28  ? 26.302 -4.313  104.857 1.00 35.25  ? 43  PHE B C   1 
ATOM   2180 O O   . PHE B  1 28  ? 25.543 -5.098  104.290 1.00 39.15  ? 43  PHE B O   1 
ATOM   2181 C CB  . PHE B  1 28  ? 28.341 -3.980  103.359 1.00 34.31  ? 43  PHE B CB  1 
ATOM   2182 C CG  . PHE B  1 28  ? 29.332 -4.548  104.343 1.00 33.37  ? 43  PHE B CG  1 
ATOM   2183 C CD1 . PHE B  1 28  ? 30.342 -3.760  104.881 1.00 31.01  ? 43  PHE B CD1 1 
ATOM   2184 C CD2 . PHE B  1 28  ? 29.273 -5.886  104.701 1.00 31.52  ? 43  PHE B CD2 1 
ATOM   2185 C CE1 . PHE B  1 28  ? 31.268 -4.303  105.755 1.00 29.89  ? 43  PHE B CE1 1 
ATOM   2186 C CE2 . PHE B  1 28  ? 30.193 -6.418  105.590 1.00 31.81  ? 43  PHE B CE2 1 
ATOM   2187 C CZ  . PHE B  1 28  ? 31.189 -5.629  106.112 1.00 30.49  ? 43  PHE B CZ  1 
ATOM   2188 N N   . CYS B  1 29  ? 26.471 -4.293  106.179 1.00 36.78  ? 44  CYS B N   1 
ATOM   2189 C CA  . CYS B  1 29  ? 25.768 -5.213  107.110 1.00 36.54  ? 44  CYS B CA  1 
ATOM   2190 C C   . CYS B  1 29  ? 25.543 -4.542  108.467 1.00 34.88  ? 44  CYS B C   1 
ATOM   2191 O O   . CYS B  1 29  ? 26.249 -3.568  108.797 1.00 35.80  ? 44  CYS B O   1 
ATOM   2192 C CB  . CYS B  1 29  ? 26.551 -6.509  107.304 1.00 36.82  ? 44  CYS B CB  1 
ATOM   2193 S SG  . CYS B  1 29  ? 26.198 -7.798  106.079 1.00 40.29  ? 44  CYS B SG  1 
ATOM   2194 N N   . GLY B  1 30  ? 24.591 -5.079  109.226 1.00 32.72  ? 45  GLY B N   1 
ATOM   2195 C CA  . GLY B  1 30  ? 24.376 -4.753  110.643 1.00 32.47  ? 45  GLY B CA  1 
ATOM   2196 C C   . GLY B  1 30  ? 25.142 -5.700  111.553 1.00 31.46  ? 45  GLY B C   1 
ATOM   2197 O O   . GLY B  1 30  ? 25.841 -6.611  111.052 1.00 31.99  ? 45  GLY B O   1 
ATOM   2198 N N   . GLY B  1 31  ? 25.031 -5.449  112.851 1.00 32.79  ? 46  GLY B N   1 
ATOM   2199 C CA  . GLY B  1 31  ? 25.657 -6.222  113.936 1.00 32.23  ? 46  GLY B CA  1 
ATOM   2200 C C   . GLY B  1 31  ? 25.072 -5.803  115.265 1.00 32.24  ? 46  GLY B C   1 
ATOM   2201 O O   . GLY B  1 31  ? 24.257 -4.852  115.293 1.00 31.99  ? 46  GLY B O   1 
ATOM   2202 N N   . SER B  1 32  ? 25.471 -6.473  116.341 1.00 32.87  ? 47  SER B N   1 
ATOM   2203 C CA  . SER B  1 32  ? 25.075 -6.109  117.720 1.00 32.36  ? 47  SER B CA  1 
ATOM   2204 C C   . SER B  1 32  ? 26.311 -6.124  118.620 1.00 31.43  ? 47  SER B C   1 
ATOM   2205 O O   . SER B  1 32  ? 27.156 -7.024  118.460 1.00 28.45  ? 47  SER B O   1 
ATOM   2206 C CB  . SER B  1 32  ? 23.975 -6.988  118.222 1.00 31.95  ? 47  SER B CB  1 
ATOM   2207 O OG  . SER B  1 32  ? 24.350 -8.351  118.148 1.00 34.61  ? 47  SER B OG  1 
ATOM   2208 N N   . LEU B  1 33  ? 26.415 -5.139  119.511 1.00 30.69  ? 48  LEU B N   1 
ATOM   2209 C CA  . LEU B  1 33  ? 27.430 -5.125  120.591 1.00 31.76  ? 48  LEU B CA  1 
ATOM   2210 C C   . LEU B  1 33  ? 26.961 -6.075  121.700 1.00 31.44  ? 48  LEU B C   1 
ATOM   2211 O O   . LEU B  1 33  ? 25.892 -5.832  122.276 1.00 30.69  ? 48  LEU B O   1 
ATOM   2212 C CB  . LEU B  1 33  ? 27.604 -3.692  121.095 1.00 33.08  ? 48  LEU B CB  1 
ATOM   2213 C CG  . LEU B  1 33  ? 28.828 -3.455  121.978 1.00 33.66  ? 48  LEU B CG  1 
ATOM   2214 C CD1 . LEU B  1 33  ? 30.111 -3.472  121.158 1.00 34.12  ? 48  LEU B CD1 1 
ATOM   2215 C CD2 . LEU B  1 33  ? 28.688 -2.140  122.728 1.00 35.05  ? 48  LEU B CD2 1 
ATOM   2216 N N   . ILE B  1 34  ? 27.684 -7.172  121.912 1.00 32.76  ? 49  ILE B N   1 
ATOM   2217 C CA  . ILE B  1 34  ? 27.350 -8.192  122.956 1.00 32.69  ? 49  ILE B CA  1 
ATOM   2218 C C   . ILE B  1 34  ? 28.362 -8.117  124.110 1.00 32.05  ? 49  ILE B C   1 
ATOM   2219 O O   . ILE B  1 34  ? 28.161 -8.799  125.113 1.00 33.78  ? 49  ILE B O   1 
ATOM   2220 C CB  . ILE B  1 34  ? 27.259 -9.602  122.336 1.00 31.79  ? 49  ILE B CB  1 
ATOM   2221 C CG1 . ILE B  1 34  ? 28.542 -10.022 121.616 1.00 30.72  ? 49  ILE B CG1 1 
ATOM   2222 C CG2 . ILE B  1 34  ? 26.046 -9.699  121.425 1.00 31.75  ? 49  ILE B CG2 1 
ATOM   2223 C CD1 . ILE B  1 34  ? 28.704 -11.530 121.506 1.00 32.74  ? 49  ILE B CD1 1 
ATOM   2224 N N   . HIS B  1 35  ? 29.425 -7.336  123.949 1.00 33.30  ? 50  HIS B N   1 
ATOM   2225 C CA  . HIS B  1 35  ? 30.504 -7.117  124.942 1.00 34.44  ? 50  HIS B CA  1 
ATOM   2226 C C   . HIS B  1 35  ? 31.193 -5.826  124.529 1.00 34.58  ? 50  HIS B C   1 
ATOM   2227 O O   . HIS B  1 35  ? 31.197 -5.514  123.341 1.00 33.93  ? 50  HIS B O   1 
ATOM   2228 C CB  . HIS B  1 35  ? 31.422 -8.344  124.965 1.00 35.89  ? 50  HIS B CB  1 
ATOM   2229 C CG  . HIS B  1 35  ? 32.526 -8.299  125.968 1.00 36.53  ? 50  HIS B CG  1 
ATOM   2230 N ND1 . HIS B  1 35  ? 33.720 -7.624  125.741 1.00 37.25  ? 50  HIS B ND1 1 
ATOM   2231 C CD2 . HIS B  1 35  ? 32.655 -8.894  127.172 1.00 37.19  ? 50  HIS B CD2 1 
ATOM   2232 C CE1 . HIS B  1 35  ? 34.517 -7.777  126.779 1.00 37.01  ? 50  HIS B CE1 1 
ATOM   2233 N NE2 . HIS B  1 35  ? 33.886 -8.552  127.670 1.00 37.70  ? 50  HIS B NE2 1 
ATOM   2234 N N   . PRO B  1 36  ? 31.766 -5.024  125.456 1.00 34.74  ? 51  PRO B N   1 
ATOM   2235 C CA  . PRO B  1 36  ? 32.518 -3.826  125.069 1.00 34.16  ? 51  PRO B CA  1 
ATOM   2236 C C   . PRO B  1 36  ? 33.556 -3.991  123.946 1.00 34.00  ? 51  PRO B C   1 
ATOM   2237 O O   . PRO B  1 36  ? 33.871 -2.995  123.320 1.00 35.37  ? 51  PRO B O   1 
ATOM   2238 C CB  . PRO B  1 36  ? 33.216 -3.462  126.387 1.00 35.13  ? 51  PRO B CB  1 
ATOM   2239 C CG  . PRO B  1 36  ? 32.208 -3.860  127.425 1.00 34.20  ? 51  PRO B CG  1 
ATOM   2240 C CD  . PRO B  1 36  ? 31.691 -5.190  126.919 1.00 34.27  ? 51  PRO B CD  1 
ATOM   2241 N N   . GLN B  1 37  ? 34.069 -5.204  123.707 1.00 33.91  ? 52  GLN B N   1 
ATOM   2242 C CA  . GLN B  1 37  ? 35.112 -5.475  122.682 1.00 34.40  ? 52  GLN B CA  1 
ATOM   2243 C C   . GLN B  1 37  ? 34.611 -6.458  121.606 1.00 32.65  ? 52  GLN B C   1 
ATOM   2244 O O   . GLN B  1 37  ? 35.430 -6.819  120.743 1.00 32.25  ? 52  GLN B O   1 
ATOM   2245 C CB  . GLN B  1 37  ? 36.383 -5.986  123.366 1.00 36.49  ? 52  GLN B CB  1 
ATOM   2246 C CG  . GLN B  1 37  ? 37.650 -5.725  122.555 1.00 39.98  ? 52  GLN B CG  1 
ATOM   2247 C CD  . GLN B  1 37  ? 38.922 -5.793  123.365 1.00 42.16  ? 52  GLN B CD  1 
ATOM   2248 O OE1 . GLN B  1 37  ? 38.916 -6.167  124.538 1.00 44.44  ? 52  GLN B OE1 1 
ATOM   2249 N NE2 . GLN B  1 37  ? 40.029 -5.424  122.733 1.00 40.72  ? 52  GLN B NE2 1 
ATOM   2250 N N   . TRP B  1 38  ? 33.337 -6.863  121.600 1.00 31.21  ? 53  TRP B N   1 
ATOM   2251 C CA  . TRP B  1 38  ? 32.842 -7.912  120.662 1.00 31.48  ? 53  TRP B CA  1 
ATOM   2252 C C   . TRP B  1 38  ? 31.522 -7.523  119.996 1.00 31.12  ? 53  TRP B C   1 
ATOM   2253 O O   . TRP B  1 38  ? 30.573 -7.122  120.700 1.00 31.04  ? 53  TRP B O   1 
ATOM   2254 C CB  . TRP B  1 38  ? 32.733 -9.270  121.354 1.00 31.43  ? 53  TRP B CB  1 
ATOM   2255 C CG  . TRP B  1 38  ? 34.058 -9.841  121.754 1.00 32.55  ? 53  TRP B CG  1 
ATOM   2256 C CD1 . TRP B  1 38  ? 34.715 -9.640  122.932 1.00 34.40  ? 53  TRP B CD1 1 
ATOM   2257 C CD2 . TRP B  1 38  ? 34.890 -10.726 120.981 1.00 32.68  ? 53  TRP B CD2 1 
ATOM   2258 N NE1 . TRP B  1 38  ? 35.895 -10.336 122.944 1.00 33.21  ? 53  TRP B NE1 1 
ATOM   2259 C CE2 . TRP B  1 38  ? 36.026 -11.018 121.768 1.00 33.96  ? 53  TRP B CE2 1 
ATOM   2260 C CE3 . TRP B  1 38  ? 34.787 -11.304 119.711 1.00 33.48  ? 53  TRP B CE3 1 
ATOM   2261 C CZ2 . TRP B  1 38  ? 37.047 -11.861 121.325 1.00 33.17  ? 53  TRP B CZ2 1 
ATOM   2262 C CZ3 . TRP B  1 38  ? 35.800 -12.129 119.268 1.00 34.13  ? 53  TRP B CZ3 1 
ATOM   2263 C CH2 . TRP B  1 38  ? 36.915 -12.401 120.066 1.00 32.14  ? 53  TRP B CH2 1 
ATOM   2264 N N   . VAL B  1 39  ? 31.478 -7.686  118.671 1.00 31.95  ? 54  VAL B N   1 
ATOM   2265 C CA  . VAL B  1 39  ? 30.270 -7.489  117.821 1.00 30.34  ? 54  VAL B CA  1 
ATOM   2266 C C   . VAL B  1 39  ? 29.842 -8.853  117.279 1.00 29.67  ? 54  VAL B C   1 
ATOM   2267 O O   . VAL B  1 39  ? 30.694 -9.583  116.745 1.00 28.44  ? 54  VAL B O   1 
ATOM   2268 C CB  . VAL B  1 39  ? 30.556 -6.467  116.709 1.00 30.03  ? 54  VAL B CB  1 
ATOM   2269 C CG1 . VAL B  1 39  ? 29.452 -6.403  115.659 1.00 29.65  ? 54  VAL B CG1 1 
ATOM   2270 C CG2 . VAL B  1 39  ? 30.816 -5.094  117.311 1.00 29.91  ? 54  VAL B CG2 1 
ATOM   2271 N N   . LEU B  1 40  ? 28.558 -9.173  117.421 1.00 29.42  ? 55  LEU B N   1 
ATOM   2272 C CA  . LEU B  1 40  ? 27.916 -10.369 116.819 1.00 29.42  ? 55  LEU B CA  1 
ATOM   2273 C C   . LEU B  1 40  ? 27.326 -9.965  115.467 1.00 31.20  ? 55  LEU B C   1 
ATOM   2274 O O   . LEU B  1 40  ? 26.618 -8.930  115.417 1.00 30.79  ? 55  LEU B O   1 
ATOM   2275 C CB  . LEU B  1 40  ? 26.843 -10.888 117.780 1.00 29.63  ? 55  LEU B CB  1 
ATOM   2276 C CG  . LEU B  1 40  ? 26.099 -12.146 117.344 1.00 30.27  ? 55  LEU B CG  1 
ATOM   2277 C CD1 . LEU B  1 40  ? 27.043 -13.332 117.247 1.00 31.64  ? 55  LEU B CD1 1 
ATOM   2278 C CD2 . LEU B  1 40  ? 24.957 -12.447 118.302 1.00 30.33  ? 55  LEU B CD2 1 
ATOM   2279 N N   . THR B  1 41  ? 27.611 -10.746 114.416 1.00 30.41  ? 56  THR B N   1 
ATOM   2280 C CA  . THR B  1 41  ? 27.105 -10.504 113.041 1.00 31.16  ? 56  THR B CA  1 
ATOM   2281 C C   . THR B  1 41  ? 26.813 -11.840 112.343 1.00 31.05  ? 56  THR B C   1 
ATOM   2282 O O   . THR B  1 41  ? 26.930 -12.905 112.993 1.00 30.23  ? 56  THR B O   1 
ATOM   2283 C CB  . THR B  1 41  ? 28.071 -9.576  112.288 1.00 31.42  ? 56  THR B CB  1 
ATOM   2284 O OG1 . THR B  1 41  ? 27.353 -9.055  111.171 1.00 31.04  ? 56  THR B OG1 1 
ATOM   2285 C CG2 . THR B  1 41  ? 29.357 -10.247 111.852 1.00 32.24  ? 56  THR B CG2 1 
ATOM   2286 N N   . ALA B  1 42  ? 26.434 -11.777 111.063 1.00 31.43  ? 57  ALA B N   1 
ATOM   2287 C CA  . ALA B  1 42  ? 26.245 -12.952 110.185 1.00 29.33  ? 57  ALA B CA  1 
ATOM   2288 C C   . ALA B  1 42  ? 27.593 -13.265 109.532 1.00 29.16  ? 57  ALA B C   1 
ATOM   2289 O O   . ALA B  1 42  ? 28.278 -12.320 109.128 1.00 28.79  ? 57  ALA B O   1 
ATOM   2290 C CB  . ALA B  1 42  ? 25.174 -12.680 109.163 1.00 30.47  ? 57  ALA B CB  1 
ATOM   2291 N N   . ALA B  1 43  ? 27.962 -14.543 109.462 1.00 28.08  ? 58  ALA B N   1 
ATOM   2292 C CA  . ALA B  1 43  ? 29.149 -15.052 108.736 1.00 28.17  ? 58  ALA B CA  1 
ATOM   2293 C C   . ALA B  1 43  ? 29.148 -14.608 107.264 1.00 29.01  ? 58  ALA B C   1 
ATOM   2294 O O   . ALA B  1 43  ? 30.243 -14.287 106.763 1.00 30.46  ? 58  ALA B O   1 
ATOM   2295 C CB  . ALA B  1 43  ? 29.204 -16.550 108.852 1.00 27.24  ? 58  ALA B CB  1 
ATOM   2296 N N   . HIS B  1 44  ? 27.991 -14.587 106.585 1.00 29.80  ? 59  HIS B N   1 
ATOM   2297 C CA  . HIS B  1 44  ? 27.897 -14.283 105.127 1.00 31.00  ? 59  HIS B CA  1 
ATOM   2298 C C   . HIS B  1 44  ? 28.317 -12.827 104.858 1.00 31.59  ? 59  HIS B C   1 
ATOM   2299 O O   . HIS B  1 44  ? 28.720 -12.542 103.722 1.00 30.23  ? 59  HIS B O   1 
ATOM   2300 C CB  . HIS B  1 44  ? 26.514 -14.647 104.545 1.00 30.40  ? 59  HIS B CB  1 
ATOM   2301 C CG  . HIS B  1 44  ? 25.452 -13.611 104.710 1.00 29.88  ? 59  HIS B CG  1 
ATOM   2302 N ND1 . HIS B  1 44  ? 24.451 -13.724 105.644 1.00 29.35  ? 59  HIS B ND1 1 
ATOM   2303 C CD2 . HIS B  1 44  ? 25.214 -12.457 104.046 1.00 29.74  ? 59  HIS B CD2 1 
ATOM   2304 C CE1 . HIS B  1 44  ? 23.660 -12.676 105.564 1.00 29.20  ? 59  HIS B CE1 1 
ATOM   2305 N NE2 . HIS B  1 44  ? 24.102 -11.895 104.592 1.00 29.23  ? 59  HIS B NE2 1 
ATOM   2306 N N   . CYS B  1 45  ? 28.252 -11.952 105.865 1.00 32.49  ? 60  CYS B N   1 
ATOM   2307 C CA  . CYS B  1 45  ? 28.705 -10.539 105.784 1.00 34.15  ? 60  CYS B CA  1 
ATOM   2308 C C   . CYS B  1 45  ? 30.230 -10.457 105.631 1.00 33.41  ? 60  CYS B C   1 
ATOM   2309 O O   . CYS B  1 45  ? 30.687 -9.518  104.967 1.00 34.08  ? 60  CYS B O   1 
ATOM   2310 C CB  . CYS B  1 45  ? 28.276 -9.761  107.019 1.00 34.97  ? 60  CYS B CB  1 
ATOM   2311 S SG  . CYS B  1 45  ? 26.483 -9.559  107.139 1.00 37.00  ? 60  CYS B SG  1 
ATOM   2312 N N   . VAL B  1 46  ? 30.975 -11.399 106.213 1.00 33.36  ? 61  VAL B N   1 
ATOM   2313 C CA  . VAL B  1 46  ? 32.468 -11.334 106.314 1.00 37.42  ? 61  VAL B CA  1 
ATOM   2314 C C   . VAL B  1 46  ? 33.130 -12.615 105.785 1.00 37.76  ? 61  VAL B C   1 
ATOM   2315 O O   . VAL B  1 46  ? 34.362 -12.687 105.869 1.00 41.69  ? 61  VAL B O   1 
ATOM   2316 C CB  . VAL B  1 46  ? 32.899 -11.030 107.762 1.00 38.03  ? 61  VAL B CB  1 
ATOM   2317 C CG1 . VAL B  1 46  ? 32.479 -9.623  108.170 1.00 37.26  ? 61  VAL B CG1 1 
ATOM   2318 C CG2 . VAL B  1 46  ? 32.375 -12.055 108.765 1.00 38.11  ? 61  VAL B CG2 1 
ATOM   2319 N N   . GLY B  1 47  ? 32.372 -13.551 105.210 1.00 35.20  ? 62  GLY B N   1 
ATOM   2320 C CA  . GLY B  1 47  ? 32.891 -14.857 104.770 1.00 34.92  ? 62  GLY B CA  1 
ATOM   2321 C C   . GLY B  1 47  ? 32.018 -15.489 103.692 1.00 33.29  ? 62  GLY B C   1 
ATOM   2322 O O   . GLY B  1 47  ? 31.074 -14.862 103.230 1.00 34.81  ? 62  GLY B O   1 
ATOM   2323 N N   . PRO B  1 48  ? 32.294 -16.740 103.255 1.00 34.81  ? 63  PRO B N   1 
ATOM   2324 C CA  . PRO B  1 48  ? 33.303 -17.603 103.881 1.00 34.67  ? 63  PRO B CA  1 
ATOM   2325 C C   . PRO B  1 48  ? 34.777 -17.290 103.555 1.00 34.50  ? 63  PRO B C   1 
ATOM   2326 O O   . PRO B  1 48  ? 35.630 -17.870 104.190 1.00 34.75  ? 63  PRO B O   1 
ATOM   2327 C CB  . PRO B  1 48  ? 32.936 -18.980 103.314 1.00 32.66  ? 63  PRO B CB  1 
ATOM   2328 C CG  . PRO B  1 48  ? 32.410 -18.680 101.942 1.00 33.27  ? 63  PRO B CG  1 
ATOM   2329 C CD  . PRO B  1 48  ? 31.632 -17.390 102.113 1.00 34.08  ? 63  PRO B CD  1 
ATOM   2330 N N   . ASP B  1 49  ? 35.049 -16.448 102.560 1.00 36.56  ? 64  ASP B N   1 
ATOM   2331 C CA  . ASP B  1 49  ? 36.433 -16.131 102.115 1.00 39.36  ? 64  ASP B CA  1 
ATOM   2332 C C   . ASP B  1 49  ? 37.064 -15.127 103.077 1.00 39.12  ? 64  ASP B C   1 
ATOM   2333 O O   . ASP B  1 49  ? 36.364 -14.191 103.503 1.00 36.74  ? 64  ASP B O   1 
ATOM   2334 C CB  . ASP B  1 49  ? 36.474 -15.584 100.690 1.00 39.34  ? 64  ASP B CB  1 
ATOM   2335 C CG  . ASP B  1 49  ? 36.014 -16.588 99.655  1.00 43.14  ? 64  ASP B CG  1 
ATOM   2336 O OD1 . ASP B  1 49  ? 36.340 -17.804 99.798  1.00 42.59  ? 64  ASP B OD1 1 
ATOM   2337 O OD2 . ASP B  1 49  ? 35.312 -16.151 98.732  1.00 47.13  ? 64  ASP B OD2 1 
ATOM   2338 N N   . VAL B  1 50  ? 38.349 -15.320 103.373 1.00 38.81  ? 65  VAL B N   1 
ATOM   2339 C CA  . VAL B  1 50  ? 39.137 -14.466 104.304 1.00 40.06  ? 65  VAL B CA  1 
ATOM   2340 C C   . VAL B  1 50  ? 39.312 -13.100 103.638 1.00 41.73  ? 65  VAL B C   1 
ATOM   2341 O O   . VAL B  1 50  ? 39.755 -13.066 102.476 1.00 47.60  ? 65  VAL B O   1 
ATOM   2342 C CB  . VAL B  1 50  ? 40.474 -15.123 104.686 1.00 39.63  ? 65  VAL B CB  1 
ATOM   2343 C CG1 . VAL B  1 50  ? 41.387 -14.177 105.464 1.00 40.35  ? 65  VAL B CG1 1 
ATOM   2344 C CG2 . VAL B  1 50  ? 40.231 -16.397 105.480 1.00 40.22  ? 65  VAL B CG2 1 
ATOM   2345 N N   . LYS B  1 51  ? 38.951 -12.038 104.357 1.00 43.68  ? 66  LYS B N   1 
ATOM   2346 C CA  . LYS B  1 51  ? 39.009 -10.632 103.888 1.00 49.34  ? 66  LYS B CA  1 
ATOM   2347 C C   . LYS B  1 51  ? 40.014 -9.834  104.717 1.00 46.50  ? 66  LYS B C   1 
ATOM   2348 O O   . LYS B  1 51  ? 40.309 -10.249 105.850 1.00 43.92  ? 66  LYS B O   1 
ATOM   2349 C CB  . LYS B  1 51  ? 37.594 -10.070 103.930 1.00 55.33  ? 66  LYS B CB  1 
ATOM   2350 C CG  . LYS B  1 51  ? 36.741 -10.593 102.782 1.00 59.34  ? 66  LYS B CG  1 
ATOM   2351 C CD  . LYS B  1 51  ? 35.256 -10.669 103.053 1.00 60.58  ? 66  LYS B CD  1 
ATOM   2352 C CE  . LYS B  1 51  ? 34.560 -11.650 102.133 1.00 60.20  ? 66  LYS B CE  1 
ATOM   2353 N NZ  . LYS B  1 51  ? 33.086 -11.570 102.260 1.00 64.43  ? 66  LYS B NZ  1 
ATOM   2354 N N   . ASP B  1 52  ? 40.526 -8.741  104.141 1.00 46.88  ? 67  ASP B N   1 
ATOM   2355 C CA  . ASP B  1 52  ? 41.536 -7.844  104.770 1.00 45.52  ? 67  ASP B CA  1 
ATOM   2356 C C   . ASP B  1 52  ? 40.848 -7.051  105.886 1.00 42.35  ? 67  ASP B C   1 
ATOM   2357 O O   . ASP B  1 52  ? 39.896 -6.321  105.579 1.00 42.10  ? 67  ASP B O   1 
ATOM   2358 C CB  . ASP B  1 52  ? 42.186 -6.924  103.730 1.00 48.83  ? 67  ASP B CB  1 
ATOM   2359 C CG  . ASP B  1 52  ? 43.230 -5.958  104.276 1.00 51.46  ? 67  ASP B CG  1 
ATOM   2360 O OD1 . ASP B  1 52  ? 43.827 -6.250  105.332 1.00 52.23  ? 67  ASP B OD1 1 
ATOM   2361 O OD2 . ASP B  1 52  ? 43.443 -4.916  103.631 1.00 60.51  ? 67  ASP B OD2 1 
ATOM   2362 N N   . LEU B  1 53  ? 41.307 -7.219  107.131 1.00 41.84  ? 68  LEU B N   1 
ATOM   2363 C CA  . LEU B  1 53  ? 40.784 -6.530  108.348 1.00 44.00  ? 68  LEU B CA  1 
ATOM   2364 C C   . LEU B  1 53  ? 40.879 -5.006  108.179 1.00 43.32  ? 68  LEU B C   1 
ATOM   2365 O O   . LEU B  1 53  ? 39.982 -4.318  108.682 1.00 43.34  ? 68  LEU B O   1 
ATOM   2366 C CB  . LEU B  1 53  ? 41.596 -6.959  109.577 1.00 44.52  ? 68  LEU B CB  1 
ATOM   2367 C CG  . LEU B  1 53  ? 41.331 -8.358  110.127 1.00 47.67  ? 68  LEU B CG  1 
ATOM   2368 C CD1 . LEU B  1 53  ? 42.497 -8.835  110.983 1.00 47.69  ? 68  LEU B CD1 1 
ATOM   2369 C CD2 . LEU B  1 53  ? 40.053 -8.370  110.933 1.00 48.36  ? 68  LEU B CD2 1 
ATOM   2370 N N   . ALA B  1 54  ? 41.935 -4.511  107.517 1.00 40.52  ? 69  ALA B N   1 
ATOM   2371 C CA  . ALA B  1 54  ? 42.222 -3.072  107.320 1.00 43.03  ? 69  ALA B CA  1 
ATOM   2372 C C   . ALA B  1 54  ? 41.105 -2.398  106.512 1.00 40.27  ? 69  ALA B C   1 
ATOM   2373 O O   . ALA B  1 54  ? 40.946 -1.185  106.668 1.00 43.15  ? 69  ALA B O   1 
ATOM   2374 C CB  . ALA B  1 54  ? 43.569 -2.902  106.650 1.00 42.74  ? 69  ALA B CB  1 
ATOM   2375 N N   . ALA B  1 55  ? 40.370 -3.143  105.680 1.00 39.07  ? 70  ALA B N   1 
ATOM   2376 C CA  . ALA B  1 55  ? 39.266 -2.622  104.836 1.00 38.65  ? 70  ALA B CA  1 
ATOM   2377 C C   . ALA B  1 55  ? 37.903 -2.747  105.539 1.00 38.11  ? 70  ALA B C   1 
ATOM   2378 O O   . ALA B  1 55  ? 36.883 -2.461  104.893 1.00 37.22  ? 70  ALA B O   1 
ATOM   2379 C CB  . ALA B  1 55  ? 39.281 -3.320  103.499 1.00 39.96  ? 70  ALA B CB  1 
ATOM   2380 N N   . LEU B  1 56  ? 37.872 -3.115  106.821 1.00 38.27  ? 71  LEU B N   1 
ATOM   2381 C CA  . LEU B  1 56  ? 36.639 -3.238  107.645 1.00 37.80  ? 71  LEU B CA  1 
ATOM   2382 C C   . LEU B  1 56  ? 36.699 -2.246  108.811 1.00 35.57  ? 71  LEU B C   1 
ATOM   2383 O O   . LEU B  1 56  ? 37.753 -2.144  109.444 1.00 37.67  ? 71  LEU B O   1 
ATOM   2384 C CB  . LEU B  1 56  ? 36.530 -4.680  108.152 1.00 37.71  ? 71  LEU B CB  1 
ATOM   2385 C CG  . LEU B  1 56  ? 35.364 -4.997  109.089 1.00 38.21  ? 71  LEU B CG  1 
ATOM   2386 C CD1 . LEU B  1 56  ? 34.019 -4.740  108.426 1.00 39.24  ? 71  LEU B CD1 1 
ATOM   2387 C CD2 . LEU B  1 56  ? 35.446 -6.442  109.557 1.00 38.73  ? 71  LEU B CD2 1 
ATOM   2388 N N   . ARG B  1 57  ? 35.590 -1.562  109.085 1.00 34.68  ? 72  ARG B N   1 
ATOM   2389 C CA  . ARG B  1 57  ? 35.405 -0.717  110.290 1.00 36.06  ? 72  ARG B CA  1 
ATOM   2390 C C   . ARG B  1 57  ? 34.022 -0.970  110.886 1.00 32.81  ? 72  ARG B C   1 
ATOM   2391 O O   . ARG B  1 57  ? 33.116 -1.418  110.153 1.00 31.11  ? 72  ARG B O   1 
ATOM   2392 C CB  . ARG B  1 57  ? 35.561 0.767   109.954 1.00 38.93  ? 72  ARG B CB  1 
ATOM   2393 C CG  . ARG B  1 57  ? 36.963 1.161   109.519 1.00 41.80  ? 72  ARG B CG  1 
ATOM   2394 C CD  . ARG B  1 57  ? 37.914 1.414   110.660 1.00 41.52  ? 72  ARG B CD  1 
ATOM   2395 N NE  . ARG B  1 57  ? 39.087 2.101   110.138 1.00 43.68  ? 72  ARG B NE  1 
ATOM   2396 C CZ  . ARG B  1 57  ? 40.107 1.525   109.503 1.00 47.03  ? 72  ARG B CZ  1 
ATOM   2397 N NH1 . ARG B  1 57  ? 40.144 0.212   109.301 1.00 49.46  ? 72  ARG B NH1 1 
ATOM   2398 N NH2 . ARG B  1 57  ? 41.101 2.283   109.069 1.00 46.87  ? 72  ARG B NH2 1 
ATOM   2399 N N   . VAL B  1 58  ? 33.891 -0.706  112.185 1.00 34.05  ? 73  VAL B N   1 
ATOM   2400 C CA  . VAL B  1 58  ? 32.607 -0.786  112.933 1.00 33.99  ? 73  VAL B CA  1 
ATOM   2401 C C   . VAL B  1 58  ? 32.214 0.633   113.339 1.00 32.73  ? 73  VAL B C   1 
ATOM   2402 O O   . VAL B  1 58  ? 33.088 1.398   113.782 1.00 31.79  ? 73  VAL B O   1 
ATOM   2403 C CB  . VAL B  1 58  ? 32.708 -1.743  114.135 1.00 36.05  ? 73  VAL B CB  1 
ATOM   2404 C CG1 . VAL B  1 58  ? 31.463 -1.701  115.003 1.00 37.70  ? 73  VAL B CG1 1 
ATOM   2405 C CG2 . VAL B  1 58  ? 32.995 -3.171  113.685 1.00 36.33  ? 73  VAL B CG2 1 
ATOM   2406 N N   . GLN B  1 59  ? 30.931 0.953   113.182 1.00 32.47  ? 74  GLN B N   1 
ATOM   2407 C CA  . GLN B  1 59  ? 30.301 2.212   113.644 1.00 31.61  ? 74  GLN B CA  1 
ATOM   2408 C C   . GLN B  1 59  ? 29.249 1.835   114.685 1.00 32.66  ? 74  GLN B C   1 
ATOM   2409 O O   . GLN B  1 59  ? 28.347 1.040   114.339 1.00 33.18  ? 74  GLN B O   1 
ATOM   2410 C CB  . GLN B  1 59  ? 29.694 2.957   112.455 1.00 30.89  ? 74  GLN B CB  1 
ATOM   2411 C CG  . GLN B  1 59  ? 28.876 4.186   112.823 1.00 31.31  ? 74  GLN B CG  1 
ATOM   2412 C CD  . GLN B  1 59  ? 29.665 5.201   113.614 1.00 32.79  ? 74  GLN B CD  1 
ATOM   2413 O OE1 . GLN B  1 59  ? 30.777 5.559   113.238 1.00 34.42  ? 74  GLN B OE1 1 
ATOM   2414 N NE2 . GLN B  1 59  ? 29.110 5.676   114.722 1.00 33.32  ? 74  GLN B NE2 1 
ATOM   2415 N N   . LEU B  1 60  ? 29.353 2.399   115.895 1.00 32.96  ? 75  LEU B N   1 
ATOM   2416 C CA  . LEU B  1 60  ? 28.377 2.190   116.996 1.00 34.78  ? 75  LEU B CA  1 
ATOM   2417 C C   . LEU B  1 60  ? 27.079 2.926   116.650 1.00 35.51  ? 75  LEU B C   1 
ATOM   2418 O O   . LEU B  1 60  ? 27.070 3.688   115.651 1.00 35.66  ? 75  LEU B O   1 
ATOM   2419 C CB  . LEU B  1 60  ? 28.971 2.691   118.318 1.00 35.39  ? 75  LEU B CB  1 
ATOM   2420 C CG  . LEU B  1 60  ? 30.241 1.973   118.774 1.00 36.75  ? 75  LEU B CG  1 
ATOM   2421 C CD1 . LEU B  1 60  ? 30.880 2.681   119.961 1.00 36.50  ? 75  LEU B CD1 1 
ATOM   2422 C CD2 . LEU B  1 60  ? 29.955 0.518   119.104 1.00 36.30  ? 75  LEU B CD2 1 
ATOM   2423 N N   . ARG B  1 61  ? 26.025 2.721   117.441 1.00 36.61  ? 76  ARG B N   1 
ATOM   2424 C CA  . ARG B  1 61  ? 24.660 3.211   117.104 1.00 37.71  ? 76  ARG B CA  1 
ATOM   2425 C C   . ARG B  1 61  ? 24.731 4.686   116.694 1.00 37.41  ? 76  ARG B C   1 
ATOM   2426 O O   . ARG B  1 61  ? 25.293 5.485   117.457 1.00 36.49  ? 76  ARG B O   1 
ATOM   2427 C CB  . ARG B  1 61  ? 23.687 3.051   118.273 1.00 38.43  ? 76  ARG B CB  1 
ATOM   2428 C CG  . ARG B  1 61  ? 22.229 3.216   117.865 1.00 39.04  ? 76  ARG B CG  1 
ATOM   2429 C CD  . ARG B  1 61  ? 21.419 3.796   118.994 1.00 40.41  ? 76  ARG B CD  1 
ATOM   2430 N NE  . ARG B  1 61  ? 19.986 3.826   118.727 1.00 42.04  ? 76  ARG B NE  1 
ATOM   2431 C CZ  . ARG B  1 61  ? 19.353 4.738   117.992 1.00 40.19  ? 76  ARG B CZ  1 
ATOM   2432 N NH1 . ARG B  1 61  ? 20.016 5.707   117.384 1.00 43.79  ? 76  ARG B NH1 1 
ATOM   2433 N NH2 . ARG B  1 61  ? 18.039 4.668   117.865 1.00 39.49  ? 76  ARG B NH2 1 
ATOM   2434 N N   . GLU B  1 62  ? 24.211 5.018   115.514 1.00 38.26  ? 77  GLU B N   1 
ATOM   2435 C CA  . GLU B  1 62  ? 23.908 6.420   115.122 1.00 40.86  ? 77  GLU B CA  1 
ATOM   2436 C C   . GLU B  1 62  ? 22.472 6.464   114.597 1.00 39.59  ? 77  GLU B C   1 
ATOM   2437 O O   . GLU B  1 62  ? 22.006 5.454   114.052 1.00 43.01  ? 77  GLU B O   1 
ATOM   2438 C CB  . GLU B  1 62  ? 24.969 6.994   114.173 1.00 41.35  ? 77  GLU B CB  1 
ATOM   2439 C CG  . GLU B  1 62  ? 25.367 6.092   113.037 1.00 42.96  ? 77  GLU B CG  1 
ATOM   2440 C CD  . GLU B  1 62  ? 26.449 6.623   112.111 1.00 41.27  ? 77  GLU B CD  1 
ATOM   2441 O OE1 . GLU B  1 62  ? 27.158 7.576   112.469 1.00 43.77  ? 77  GLU B OE1 1 
ATOM   2442 O OE2 . GLU B  1 62  ? 26.588 6.050   111.034 1.00 38.21  ? 77  GLU B OE2 1 
ATOM   2443 N N   . GLN B  1 63  ? 21.783 7.578   114.830 1.00 36.94  ? 78  GLN B N   1 
ATOM   2444 C CA  . GLN B  1 63  ? 20.376 7.791   114.409 1.00 37.23  ? 78  GLN B CA  1 
ATOM   2445 C C   . GLN B  1 63  ? 20.316 7.876   112.879 1.00 36.21  ? 78  GLN B C   1 
ATOM   2446 O O   . GLN B  1 63  ? 19.342 7.358   112.307 1.00 36.25  ? 78  GLN B O   1 
ATOM   2447 C CB  . GLN B  1 63  ? 19.822 9.035   115.107 1.00 36.65  ? 78  GLN B CB  1 
ATOM   2448 C CG  . GLN B  1 63  ? 18.317 9.198   114.975 1.00 38.38  ? 78  GLN B CG  1 
ATOM   2449 C CD  . GLN B  1 63  ? 17.524 8.131   115.685 1.00 39.22  ? 78  GLN B CD  1 
ATOM   2450 O OE1 . GLN B  1 63  ? 18.045 7.301   116.431 1.00 37.41  ? 78  GLN B OE1 1 
ATOM   2451 N NE2 . GLN B  1 63  ? 16.220 8.157   115.461 1.00 44.70  ? 78  GLN B NE2 1 
ATOM   2452 N N   . HIS B  1 64  ? 21.316 8.509   112.258 1.00 36.00  ? 79  HIS B N   1 
ATOM   2453 C CA  . HIS B  1 64  ? 21.423 8.738   110.794 1.00 36.57  ? 79  HIS B CA  1 
ATOM   2454 C C   . HIS B  1 64  ? 22.804 8.278   110.313 1.00 36.29  ? 79  HIS B C   1 
ATOM   2455 O O   . HIS B  1 64  ? 23.780 8.885   110.765 1.00 38.25  ? 79  HIS B O   1 
ATOM   2456 C CB  . HIS B  1 64  ? 21.146 10.220  110.492 1.00 36.24  ? 79  HIS B CB  1 
ATOM   2457 C CG  . HIS B  1 64  ? 19.759 10.639  110.838 1.00 34.35  ? 79  HIS B CG  1 
ATOM   2458 N ND1 . HIS B  1 64  ? 19.472 11.375  111.970 1.00 36.82  ? 79  HIS B ND1 1 
ATOM   2459 C CD2 . HIS B  1 64  ? 18.577 10.389  110.236 1.00 35.06  ? 79  HIS B CD2 1 
ATOM   2460 C CE1 . HIS B  1 64  ? 18.171 11.576  112.043 1.00 35.69  ? 79  HIS B CE1 1 
ATOM   2461 N NE2 . HIS B  1 64  ? 17.599 10.984  110.989 1.00 35.36  ? 79  HIS B NE2 1 
ATOM   2462 N N   . LEU B  1 65  ? 22.880 7.237   109.465 1.00 35.94  ? 80  LEU B N   1 
ATOM   2463 C CA  . LEU B  1 65  ? 24.165 6.706   108.922 1.00 38.30  ? 80  LEU B CA  1 
ATOM   2464 C C   . LEU B  1 65  ? 24.985 7.847   108.327 1.00 37.19  ? 80  LEU B C   1 
ATOM   2465 O O   . LEU B  1 65  ? 24.394 8.669   107.595 1.00 37.91  ? 80  LEU B O   1 
ATOM   2466 C CB  . LEU B  1 65  ? 23.937 5.678   107.809 1.00 39.12  ? 80  LEU B CB  1 
ATOM   2467 C CG  . LEU B  1 65  ? 23.870 4.209   108.192 1.00 40.51  ? 80  LEU B CG  1 
ATOM   2468 C CD1 . LEU B  1 65  ? 23.678 3.389   106.929 1.00 40.61  ? 80  LEU B CD1 1 
ATOM   2469 C CD2 . LEU B  1 65  ? 25.101 3.727   108.935 1.00 39.90  ? 80  LEU B CD2 1 
ATOM   2470 N N   . TYR B  1 66  ? 26.289 7.852   108.617 1.00 34.93  ? 81  TYR B N   1 
ATOM   2471 C CA  . TYR B  1 66  ? 27.359 8.629   107.937 1.00 36.52  ? 81  TYR B CA  1 
ATOM   2472 C C   . TYR B  1 66  ? 27.521 10.035  108.530 1.00 38.05  ? 81  TYR B C   1 
ATOM   2473 O O   . TYR B  1 66  ? 28.586 10.614  108.291 1.00 38.71  ? 81  TYR B O   1 
ATOM   2474 C CB  . TYR B  1 66  ? 27.136 8.715   106.427 1.00 33.59  ? 81  TYR B CB  1 
ATOM   2475 C CG  . TYR B  1 66  ? 26.975 7.383   105.741 1.00 33.27  ? 81  TYR B CG  1 
ATOM   2476 C CD1 . TYR B  1 66  ? 27.998 6.448   105.764 1.00 32.63  ? 81  TYR B CD1 1 
ATOM   2477 C CD2 . TYR B  1 66  ? 25.814 7.060   105.057 1.00 31.21  ? 81  TYR B CD2 1 
ATOM   2478 C CE1 . TYR B  1 66  ? 27.866 5.218   105.140 1.00 32.40  ? 81  TYR B CE1 1 
ATOM   2479 C CE2 . TYR B  1 66  ? 25.667 5.834   104.425 1.00 32.39  ? 81  TYR B CE2 1 
ATOM   2480 C CZ  . TYR B  1 66  ? 26.701 4.913   104.461 1.00 32.87  ? 81  TYR B CZ  1 
ATOM   2481 O OH  . TYR B  1 66  ? 26.592 3.711   103.832 1.00 31.59  ? 81  TYR B OH  1 
ATOM   2482 N N   . TYR B  1 67  ? 26.550 10.559  109.283 1.00 41.22  ? 82  TYR B N   1 
ATOM   2483 C CA  A TYR B  1 67  ? 26.513 11.993  109.685 0.50 45.63  ? 82  TYR B CA  1 
ATOM   2484 C CA  B TYR B  1 67  ? 26.530 11.995  109.676 0.50 43.24  ? 82  TYR B CA  1 
ATOM   2485 C C   . TYR B  1 67  ? 27.500 12.261  110.834 1.00 47.01  ? 82  TYR B C   1 
ATOM   2486 O O   . TYR B  1 67  ? 28.144 13.333  110.817 1.00 52.25  ? 82  TYR B O   1 
ATOM   2487 C CB  A TYR B  1 67  ? 25.083 12.428  110.026 0.50 46.48  ? 82  TYR B CB  1 
ATOM   2488 C CB  B TYR B  1 67  ? 25.092 12.457  109.921 0.50 41.04  ? 82  TYR B CB  1 
ATOM   2489 C CG  A TYR B  1 67  ? 24.981 13.829  110.575 0.50 47.93  ? 82  TYR B CG  1 
ATOM   2490 C CG  B TYR B  1 67  ? 24.357 12.634  108.615 0.50 38.67  ? 82  TYR B CG  1 
ATOM   2491 C CD1 A TYR B  1 67  ? 25.600 14.900  109.952 0.50 46.77  ? 82  TYR B CD1 1 
ATOM   2492 C CD1 B TYR B  1 67  ? 24.507 13.786  107.860 0.50 37.97  ? 82  TYR B CD1 1 
ATOM   2493 C CD2 A TYR B  1 67  ? 24.250 14.085  111.721 0.50 50.40  ? 82  TYR B CD2 1 
ATOM   2494 C CD2 B TYR B  1 67  ? 23.600 11.609  108.079 0.50 37.42  ? 82  TYR B CD2 1 
ATOM   2495 C CE1 A TYR B  1 67  ? 25.511 16.183  110.462 0.50 46.71  ? 82  TYR B CE1 1 
ATOM   2496 C CE1 B TYR B  1 67  ? 23.875 13.937  106.636 0.50 36.04  ? 82  TYR B CE1 1 
ATOM   2497 C CE2 A TYR B  1 67  ? 24.144 15.363  112.245 0.50 49.82  ? 82  TYR B CE2 1 
ATOM   2498 C CE2 B TYR B  1 67  ? 22.967 11.738  106.855 0.50 36.80  ? 82  TYR B CE2 1 
ATOM   2499 C CZ  A TYR B  1 67  ? 24.776 16.417  111.611 0.50 48.64  ? 82  TYR B CZ  1 
ATOM   2500 C CZ  B TYR B  1 67  ? 23.102 12.908  106.131 0.50 36.76  ? 82  TYR B CZ  1 
ATOM   2501 O OH  A TYR B  1 67  ? 24.675 17.674  112.129 0.50 50.06  ? 82  TYR B OH  1 
ATOM   2502 O OH  B TYR B  1 67  ? 22.479 13.038  104.925 0.50 34.99  ? 82  TYR B OH  1 
ATOM   2503 N N   . GLN B  1 68  ? 27.629 11.333  111.786 1.00 49.26  ? 83  GLN B N   1 
ATOM   2504 C CA  . GLN B  1 68  ? 28.520 11.519  112.968 1.00 51.74  ? 83  GLN B CA  1 
ATOM   2505 C C   . GLN B  1 68  ? 29.404 10.283  113.136 1.00 45.47  ? 83  GLN B C   1 
ATOM   2506 O O   . GLN B  1 68  ? 29.389 9.688   114.217 1.00 48.33  ? 83  GLN B O   1 
ATOM   2507 C CB  . GLN B  1 68  ? 27.687 11.812  114.224 1.00 57.85  ? 83  GLN B CB  1 
ATOM   2508 C CG  . GLN B  1 68  ? 26.885 13.110  114.160 1.00 64.69  ? 83  GLN B CG  1 
ATOM   2509 C CD  . GLN B  1 68  ? 27.743 14.341  114.337 1.00 68.17  ? 83  GLN B CD  1 
ATOM   2510 O OE1 . GLN B  1 68  ? 28.144 14.985  113.369 1.00 77.19  ? 83  GLN B OE1 1 
ATOM   2511 N NE2 . GLN B  1 68  ? 28.045 14.673  115.581 1.00 69.35  ? 83  GLN B NE2 1 
ATOM   2512 N N   . ASP B  1 69  ? 30.158 9.924   112.099 1.00 42.05  ? 84  ASP B N   1 
ATOM   2513 C CA  . ASP B  1 69  ? 30.936 8.659   112.073 1.00 38.96  ? 84  ASP B CA  1 
ATOM   2514 C C   . ASP B  1 69  ? 32.136 8.771   113.020 1.00 38.52  ? 84  ASP B C   1 
ATOM   2515 O O   . ASP B  1 69  ? 32.855 9.776   112.956 1.00 35.58  ? 84  ASP B O   1 
ATOM   2516 C CB  . ASP B  1 69  ? 31.385 8.277   110.662 1.00 37.03  ? 84  ASP B CB  1 
ATOM   2517 C CG  . ASP B  1 69  ? 30.323 7.599   109.811 1.00 35.96  ? 84  ASP B CG  1 
ATOM   2518 O OD1 . ASP B  1 69  ? 29.175 7.446   110.276 1.00 34.39  ? 84  ASP B OD1 1 
ATOM   2519 O OD2 . ASP B  1 69  ? 30.658 7.239   108.671 1.00 38.17  ? 84  ASP B OD2 1 
ATOM   2520 N N   . GLN B  1 70  ? 32.315 7.764   113.875 1.00 39.02  ? 85  GLN B N   1 
ATOM   2521 C CA  . GLN B  1 70  ? 33.547 7.500   114.660 1.00 40.07  ? 85  GLN B CA  1 
ATOM   2522 C C   . GLN B  1 70  ? 33.903 6.027   114.440 1.00 37.86  ? 85  GLN B C   1 
ATOM   2523 O O   . GLN B  1 70  ? 33.454 5.169   115.220 1.00 40.15  ? 85  GLN B O   1 
ATOM   2524 C CB  . GLN B  1 70  ? 33.310 7.862   116.126 1.00 42.40  ? 85  GLN B CB  1 
ATOM   2525 C CG  . GLN B  1 70  ? 33.087 9.357   116.340 1.00 47.23  ? 85  GLN B CG  1 
ATOM   2526 C CD  . GLN B  1 70  ? 32.524 9.730   117.693 1.00 50.52  ? 85  GLN B CD  1 
ATOM   2527 O OE1 . GLN B  1 70  ? 31.772 8.980   118.319 1.00 52.15  ? 85  GLN B OE1 1 
ATOM   2528 N NE2 . GLN B  1 70  ? 32.859 10.930  118.145 1.00 53.95  ? 85  GLN B NE2 1 
ATOM   2529 N N   . LEU B  1 71  ? 34.636 5.746   113.370 1.00 35.99  ? 86  LEU B N   1 
ATOM   2530 C CA  . LEU B  1 71  ? 34.830 4.364   112.864 1.00 36.67  ? 86  LEU B CA  1 
ATOM   2531 C C   . LEU B  1 71  ? 35.877 3.654   113.726 1.00 37.14  ? 86  LEU B C   1 
ATOM   2532 O O   . LEU B  1 71  ? 36.927 4.261   113.997 1.00 37.18  ? 86  LEU B O   1 
ATOM   2533 C CB  . LEU B  1 71  ? 35.233 4.430   111.388 1.00 35.38  ? 86  LEU B CB  1 
ATOM   2534 C CG  . LEU B  1 71  ? 34.200 5.063   110.453 1.00 35.22  ? 86  LEU B CG  1 
ATOM   2535 C CD1 . LEU B  1 71  ? 34.684 5.010   109.015 1.00 35.04  ? 86  LEU B CD1 1 
ATOM   2536 C CD2 . LEU B  1 71  ? 32.838 4.388   110.580 1.00 34.95  ? 86  LEU B CD2 1 
ATOM   2537 N N   . LEU B  1 72  ? 35.597 2.408   114.116 1.00 35.38  ? 87  LEU B N   1 
ATOM   2538 C CA  . LEU B  1 72  ? 36.446 1.602   115.024 1.00 34.06  ? 87  LEU B CA  1 
ATOM   2539 C C   . LEU B  1 72  ? 37.104 0.486   114.224 1.00 34.80  ? 87  LEU B C   1 
ATOM   2540 O O   . LEU B  1 72  ? 36.425 -0.255  113.513 1.00 36.53  ? 87  LEU B O   1 
ATOM   2541 C CB  . LEU B  1 72  ? 35.587 1.059   116.165 1.00 33.16  ? 87  LEU B CB  1 
ATOM   2542 C CG  . LEU B  1 72  ? 34.868 2.112   117.007 1.00 33.24  ? 87  LEU B CG  1 
ATOM   2543 C CD1 . LEU B  1 72  ? 34.034 1.446   118.077 1.00 33.93  ? 87  LEU B CD1 1 
ATOM   2544 C CD2 . LEU B  1 72  ? 35.839 3.099   117.651 1.00 32.76  ? 87  LEU B CD2 1 
ATOM   2545 N N   . PRO B  1 73  ? 38.446 0.337   114.308 1.00 33.65  ? 88  PRO B N   1 
ATOM   2546 C CA  . PRO B  1 73  ? 39.126 -0.768  113.641 1.00 34.57  ? 88  PRO B CA  1 
ATOM   2547 C C   . PRO B  1 73  ? 38.889 -2.102  114.370 1.00 33.30  ? 88  PRO B C   1 
ATOM   2548 O O   . PRO B  1 73  ? 38.544 -2.098  115.537 1.00 33.22  ? 88  PRO B O   1 
ATOM   2549 C CB  . PRO B  1 73  ? 40.587 -0.301  113.651 1.00 34.19  ? 88  PRO B CB  1 
ATOM   2550 C CG  . PRO B  1 73  ? 40.706 0.495   114.922 1.00 34.28  ? 88  PRO B CG  1 
ATOM   2551 C CD  . PRO B  1 73  ? 39.380 1.214   115.034 1.00 32.55  ? 88  PRO B CD  1 
ATOM   2552 N N   . VAL B  1 74  ? 39.051 -3.199  113.631 1.00 34.34  ? 89  VAL B N   1 
ATOM   2553 C CA  . VAL B  1 74  ? 38.789 -4.595  114.078 1.00 35.32  ? 89  VAL B CA  1 
ATOM   2554 C C   . VAL B  1 74  ? 40.143 -5.300  114.185 1.00 34.40  ? 89  VAL B C   1 
ATOM   2555 O O   . VAL B  1 74  ? 40.931 -5.201  113.224 1.00 34.19  ? 89  VAL B O   1 
ATOM   2556 C CB  . VAL B  1 74  ? 37.834 -5.291  113.092 1.00 36.83  ? 89  VAL B CB  1 
ATOM   2557 C CG1 . VAL B  1 74  ? 37.661 -6.771  113.385 1.00 38.24  ? 89  VAL B CG1 1 
ATOM   2558 C CG2 . VAL B  1 74  ? 36.479 -4.604  113.076 1.00 37.80  ? 89  VAL B CG2 1 
ATOM   2559 N N   . SER B  1 75  ? 40.391 -5.993  115.298 1.00 34.49  ? 90  SER B N   1 
ATOM   2560 C CA  . SER B  1 75  ? 41.614 -6.814  115.521 1.00 36.47  ? 90  SER B CA  1 
ATOM   2561 C C   . SER B  1 75  ? 41.432 -8.225  114.953 1.00 35.78  ? 90  SER B C   1 
ATOM   2562 O O   . SER B  1 75  ? 42.437 -8.813  114.519 1.00 34.62  ? 90  SER B O   1 
ATOM   2563 C CB  . SER B  1 75  ? 41.988 -6.874  116.983 1.00 35.84  ? 90  SER B CB  1 
ATOM   2564 O OG  . SER B  1 75  ? 40.934 -7.441  117.740 1.00 39.61  ? 90  SER B OG  1 
ATOM   2565 N N   . ARG B  1 76  ? 40.210 -8.769  114.990 1.00 36.64  ? 91  ARG B N   1 
ATOM   2566 C CA  . ARG B  1 76  ? 39.956 -10.208 114.716 1.00 39.53  ? 91  ARG B CA  1 
ATOM   2567 C C   . ARG B  1 76  ? 38.565 -10.433 114.117 1.00 36.36  ? 91  ARG B C   1 
ATOM   2568 O O   . ARG B  1 76  ? 37.602 -9.848  114.632 1.00 33.17  ? 91  ARG B O   1 
ATOM   2569 C CB  . ARG B  1 76  ? 40.066 -10.986 116.028 1.00 43.30  ? 91  ARG B CB  1 
ATOM   2570 C CG  . ARG B  1 76  ? 40.502 -12.422 115.837 1.00 49.60  ? 91  ARG B CG  1 
ATOM   2571 C CD  . ARG B  1 76  ? 40.820 -13.072 117.163 1.00 51.33  ? 91  ARG B CD  1 
ATOM   2572 N NE  . ARG B  1 76  ? 40.939 -14.509 116.967 1.00 56.84  ? 91  ARG B NE  1 
ATOM   2573 C CZ  . ARG B  1 76  ? 40.860 -15.433 117.922 1.00 56.76  ? 91  ARG B CZ  1 
ATOM   2574 N NH1 . ARG B  1 76  ? 40.646 -15.089 119.183 1.00 56.88  ? 91  ARG B NH1 1 
ATOM   2575 N NH2 . ARG B  1 76  ? 40.975 -16.712 117.597 1.00 60.08  ? 91  ARG B NH2 1 
ATOM   2576 N N   . ILE B  1 77  ? 38.480 -11.237 113.054 1.00 37.78  ? 92  ILE B N   1 
ATOM   2577 C CA  . ILE B  1 77  ? 37.206 -11.785 112.495 1.00 37.71  ? 92  ILE B CA  1 
ATOM   2578 C C   . ILE B  1 77  ? 37.184 -13.280 112.816 1.00 36.82  ? 92  ILE B C   1 
ATOM   2579 O O   . ILE B  1 77  ? 38.105 -13.988 112.377 1.00 36.64  ? 92  ILE B O   1 
ATOM   2580 C CB  . ILE B  1 77  ? 37.077 -11.517 110.981 1.00 37.04  ? 92  ILE B CB  1 
ATOM   2581 C CG1 . ILE B  1 77  ? 36.996 -10.019 110.677 1.00 39.55  ? 92  ILE B CG1 1 
ATOM   2582 C CG2 . ILE B  1 77  ? 35.883 -12.261 110.392 1.00 38.45  ? 92  ILE B CG2 1 
ATOM   2583 C CD1 . ILE B  1 77  ? 37.320 -9.656  109.240 1.00 40.59  ? 92  ILE B CD1 1 
ATOM   2584 N N   . ILE B  1 78  ? 36.158 -13.733 113.528 1.00 37.14  ? 93  ILE B N   1 
ATOM   2585 C CA  . ILE B  1 78  ? 35.954 -15.168 113.871 1.00 38.31  ? 93  ILE B CA  1 
ATOM   2586 C C   . ILE B  1 78  ? 34.624 -15.608 113.257 1.00 36.29  ? 93  ILE B C   1 
ATOM   2587 O O   . ILE B  1 78  ? 33.567 -15.128 113.702 1.00 34.83  ? 93  ILE B O   1 
ATOM   2588 C CB  . ILE B  1 78  ? 36.028 -15.386 115.391 1.00 41.04  ? 93  ILE B CB  1 
ATOM   2589 C CG1 . ILE B  1 78  ? 37.304 -14.750 115.958 1.00 44.48  ? 93  ILE B CG1 1 
ATOM   2590 C CG2 . ILE B  1 78  ? 35.934 -16.867 115.728 1.00 39.30  ? 93  ILE B CG2 1 
ATOM   2591 C CD1 . ILE B  1 78  ? 37.474 -14.880 117.439 1.00 47.03  ? 93  ILE B CD1 1 
ATOM   2592 N N   . VAL B  1 79  ? 34.696 -16.479 112.262 1.00 33.34  ? 94  VAL B N   1 
ATOM   2593 C CA  . VAL B  1 79  ? 33.516 -16.991 111.508 1.00 34.03  ? 94  VAL B CA  1 
ATOM   2594 C C   . VAL B  1 79  ? 33.321 -18.448 111.923 1.00 34.25  ? 94  VAL B C   1 
ATOM   2595 O O   . VAL B  1 79  ? 34.331 -19.179 112.038 1.00 32.76  ? 94  VAL B O   1 
ATOM   2596 C CB  . VAL B  1 79  ? 33.730 -16.836 109.995 1.00 33.79  ? 94  VAL B CB  1 
ATOM   2597 C CG1 . VAL B  1 79  ? 32.607 -17.468 109.196 1.00 34.46  ? 94  VAL B CG1 1 
ATOM   2598 C CG2 . VAL B  1 79  ? 33.920 -15.379 109.592 1.00 34.64  ? 94  VAL B CG2 1 
ATOM   2599 N N   . HIS B  1 80  ? 32.074 -18.856 112.151 1.00 34.87  ? 95  HIS B N   1 
ATOM   2600 C CA  . HIS B  1 80  ? 31.749 -20.245 112.558 1.00 33.43  ? 95  HIS B CA  1 
ATOM   2601 C C   . HIS B  1 80  ? 32.371 -21.193 111.536 1.00 32.33  ? 95  HIS B C   1 
ATOM   2602 O O   . HIS B  1 80  ? 32.130 -21.046 110.341 1.00 31.91  ? 95  HIS B O   1 
ATOM   2603 C CB  . HIS B  1 80  ? 30.242 -20.462 112.731 1.00 33.48  ? 95  HIS B CB  1 
ATOM   2604 C CG  . HIS B  1 80  ? 29.958 -21.607 113.639 1.00 33.84  ? 95  HIS B CG  1 
ATOM   2605 N ND1 . HIS B  1 80  ? 30.151 -22.905 113.242 1.00 34.75  ? 95  HIS B ND1 1 
ATOM   2606 C CD2 . HIS B  1 80  ? 29.569 -21.658 114.930 1.00 33.89  ? 95  HIS B CD2 1 
ATOM   2607 C CE1 . HIS B  1 80  ? 29.867 -23.719 114.236 1.00 33.85  ? 95  HIS B CE1 1 
ATOM   2608 N NE2 . HIS B  1 80  ? 29.510 -22.979 115.286 1.00 34.90  ? 95  HIS B NE2 1 
ATOM   2609 N N   . PRO B  1 81  ? 33.195 -22.182 111.959 1.00 32.31  ? 96  PRO B N   1 
ATOM   2610 C CA  . PRO B  1 81  ? 33.875 -23.062 111.005 1.00 32.98  ? 96  PRO B CA  1 
ATOM   2611 C C   . PRO B  1 81  ? 32.926 -23.973 110.201 1.00 33.05  ? 96  PRO B C   1 
ATOM   2612 O O   . PRO B  1 81  ? 33.354 -24.523 109.204 1.00 33.78  ? 96  PRO B O   1 
ATOM   2613 C CB  . PRO B  1 81  ? 34.846 -23.876 111.884 1.00 33.25  ? 96  PRO B CB  1 
ATOM   2614 C CG  . PRO B  1 81  ? 34.227 -23.848 113.269 1.00 33.97  ? 96  PRO B CG  1 
ATOM   2615 C CD  . PRO B  1 81  ? 33.517 -22.511 113.357 1.00 32.94  ? 96  PRO B CD  1 
ATOM   2616 N N   . GLN B  1 82  ? 31.669 -24.114 110.626 1.00 34.74  ? 97  GLN B N   1 
ATOM   2617 C CA  . GLN B  1 82  ? 30.625 -24.885 109.901 1.00 36.58  ? 97  GLN B CA  1 
ATOM   2618 C C   . GLN B  1 82  ? 30.027 -24.046 108.764 1.00 35.76  ? 97  GLN B C   1 
ATOM   2619 O O   . GLN B  1 82  ? 29.329 -24.641 107.931 1.00 34.38  ? 97  GLN B O   1 
ATOM   2620 C CB  . GLN B  1 82  ? 29.531 -25.332 110.867 1.00 38.23  ? 97  GLN B CB  1 
ATOM   2621 C CG  . GLN B  1 82  ? 30.002 -26.364 111.877 1.00 41.50  ? 97  GLN B CG  1 
ATOM   2622 C CD  . GLN B  1 82  ? 30.107 -27.763 111.325 1.00 45.54  ? 97  GLN B CD  1 
ATOM   2623 O OE1 . GLN B  1 82  ? 31.057 -28.484 111.615 1.00 51.70  ? 97  GLN B OE1 1 
ATOM   2624 N NE2 . GLN B  1 82  ? 29.134 -28.176 110.527 1.00 47.75  ? 97  GLN B NE2 1 
ATOM   2625 N N   . PHE B  1 83  ? 30.277 -22.730 108.714 1.00 33.34  ? 98  PHE B N   1 
ATOM   2626 C CA  . PHE B  1 83  ? 29.635 -21.827 107.722 1.00 32.86  ? 98  PHE B CA  1 
ATOM   2627 C C   . PHE B  1 83  ? 30.279 -21.963 106.341 1.00 32.14  ? 98  PHE B C   1 
ATOM   2628 O O   . PHE B  1 83  ? 31.509 -21.849 106.217 1.00 32.82  ? 98  PHE B O   1 
ATOM   2629 C CB  . PHE B  1 83  ? 29.713 -20.350 108.105 1.00 32.35  ? 98  PHE B CB  1 
ATOM   2630 C CG  . PHE B  1 83  ? 29.114 -19.448 107.057 1.00 31.60  ? 98  PHE B CG  1 
ATOM   2631 C CD1 . PHE B  1 83  ? 27.738 -19.379 106.890 1.00 31.45  ? 98  PHE B CD1 1 
ATOM   2632 C CD2 . PHE B  1 83  ? 29.923 -18.705 106.206 1.00 31.47  ? 98  PHE B CD2 1 
ATOM   2633 C CE1 . PHE B  1 83  ? 27.180 -18.564 105.916 1.00 30.79  ? 98  PHE B CE1 1 
ATOM   2634 C CE2 . PHE B  1 83  ? 29.363 -17.896 105.230 1.00 31.17  ? 98  PHE B CE2 1 
ATOM   2635 C CZ  . PHE B  1 83  ? 27.994 -17.825 105.089 1.00 31.67  ? 98  PHE B CZ  1 
ATOM   2636 N N   . TYR B  1 84  ? 29.441 -22.154 105.322 1.00 32.85  ? 99  TYR B N   1 
ATOM   2637 C CA  . TYR B  1 84  ? 29.800 -21.907 103.905 1.00 33.99  ? 99  TYR B CA  1 
ATOM   2638 C C   . TYR B  1 84  ? 28.721 -21.051 103.227 1.00 32.92  ? 99  TYR B C   1 
ATOM   2639 O O   . TYR B  1 84  ? 29.111 -20.093 102.550 1.00 35.56  ? 99  TYR B O   1 
ATOM   2640 C CB  . TYR B  1 84  ? 30.118 -23.211 103.171 1.00 33.81  ? 99  TYR B CB  1 
ATOM   2641 C CG  . TYR B  1 84  ? 30.673 -22.934 101.804 1.00 35.22  ? 99  TYR B CG  1 
ATOM   2642 C CD1 . TYR B  1 84  ? 31.896 -22.292 101.655 1.00 34.94  ? 99  TYR B CD1 1 
ATOM   2643 C CD2 . TYR B  1 84  ? 29.928 -23.193 100.665 1.00 34.15  ? 99  TYR B CD2 1 
ATOM   2644 C CE1 . TYR B  1 84  ? 32.387 -21.966 100.404 1.00 33.78  ? 99  TYR B CE1 1 
ATOM   2645 C CE2 . TYR B  1 84  ? 30.408 -22.874 99.407  1.00 34.62  ? 99  TYR B CE2 1 
ATOM   2646 C CZ  . TYR B  1 84  ? 31.639 -22.257 99.276  1.00 34.05  ? 99  TYR B CZ  1 
ATOM   2647 O OH  . TYR B  1 84  ? 32.116 -21.943 98.040  1.00 34.96  ? 99  TYR B OH  1 
ATOM   2648 N N   . THR B  1 85  ? 27.431 -21.373 103.385 1.00 32.82  ? 100 THR B N   1 
ATOM   2649 C CA  . THR B  1 85  ? 26.298 -20.543 102.886 1.00 33.62  ? 100 THR B CA  1 
ATOM   2650 C C   . THR B  1 85  ? 25.232 -20.404 103.973 1.00 31.88  ? 100 THR B C   1 
ATOM   2651 O O   . THR B  1 85  ? 25.151 -21.293 104.849 1.00 31.12  ? 100 THR B O   1 
ATOM   2652 C CB  . THR B  1 85  ? 25.653 -21.106 101.610 1.00 34.62  ? 100 THR B CB  1 
ATOM   2653 O OG1 . THR B  1 85  ? 24.856 -22.241 101.947 1.00 35.05  ? 100 THR B OG1 1 
ATOM   2654 C CG2 . THR B  1 85  ? 26.662 -21.481 100.552 1.00 34.98  ? 100 THR B CG2 1 
ATOM   2655 N N   . ALA B  1 86  ? 24.436 -19.332 103.900 1.00 30.74  ? 101 ALA B N   1 
ATOM   2656 C CA  . ALA B  1 86  ? 23.331 -19.035 104.843 1.00 30.75  ? 101 ALA B CA  1 
ATOM   2657 C C   . ALA B  1 86  ? 22.283 -20.157 104.816 1.00 30.63  ? 101 ALA B C   1 
ATOM   2658 O O   . ALA B  1 86  ? 21.742 -20.467 105.895 1.00 32.73  ? 101 ALA B O   1 
ATOM   2659 C CB  . ALA B  1 86  ? 22.717 -17.700 104.522 1.00 30.87  ? 101 ALA B CB  1 
ATOM   2660 N N   . GLN B  1 87  ? 22.028 -20.761 103.651 1.00 32.26  ? 102 GLN B N   1 
ATOM   2661 C CA  . GLN B  1 87  ? 20.957 -21.783 103.474 1.00 33.50  ? 102 GLN B CA  1 
ATOM   2662 C C   . GLN B  1 87  ? 21.384 -23.109 104.114 1.00 34.10  ? 102 GLN B C   1 
ATOM   2663 O O   . GLN B  1 87  ? 20.492 -23.855 104.555 1.00 35.24  ? 102 GLN B O   1 
ATOM   2664 C CB  . GLN B  1 87  ? 20.598 -22.001 102.006 1.00 35.62  ? 102 GLN B CB  1 
ATOM   2665 C CG  . GLN B  1 87  ? 19.872 -20.825 101.364 1.00 35.87  ? 102 GLN B CG  1 
ATOM   2666 C CD  . GLN B  1 87  ? 20.754 -19.665 100.965 1.00 37.94  ? 102 GLN B CD  1 
ATOM   2667 O OE1 . GLN B  1 87  ? 20.342 -18.512 101.041 1.00 43.51  ? 102 GLN B OE1 1 
ATOM   2668 N NE2 . GLN B  1 87  ? 21.975 -19.939 100.529 1.00 36.78  ? 102 GLN B NE2 1 
ATOM   2669 N N   . ILE B  1 88  ? 22.684 -23.402 104.167 1.00 33.34  ? 103 ILE B N   1 
ATOM   2670 C CA  . ILE B  1 88  ? 23.210 -24.603 104.881 1.00 35.48  ? 103 ILE B CA  1 
ATOM   2671 C C   . ILE B  1 88  ? 23.172 -24.323 106.393 1.00 35.84  ? 103 ILE B C   1 
ATOM   2672 O O   . ILE B  1 88  ? 22.739 -25.221 107.143 1.00 36.77  ? 103 ILE B O   1 
ATOM   2673 C CB  . ILE B  1 88  ? 24.607 -24.998 104.366 1.00 37.07  ? 103 ILE B CB  1 
ATOM   2674 C CG1 . ILE B  1 88  ? 24.560 -25.403 102.889 1.00 38.12  ? 103 ILE B CG1 1 
ATOM   2675 C CG2 . ILE B  1 88  ? 25.209 -26.099 105.235 1.00 38.44  ? 103 ILE B CG2 1 
ATOM   2676 C CD1 . ILE B  1 88  ? 25.899 -25.411 102.184 1.00 37.08  ? 103 ILE B CD1 1 
ATOM   2677 N N   . GLY B  1 89  ? 23.601 -23.128 106.815 1.00 35.23  ? 104 GLY B N   1 
ATOM   2678 C CA  . GLY B  1 89  ? 23.469 -22.640 108.203 1.00 34.41  ? 104 GLY B CA  1 
ATOM   2679 C C   . GLY B  1 89  ? 24.800 -22.265 108.825 1.00 33.65  ? 104 GLY B C   1 
ATOM   2680 O O   . GLY B  1 89  ? 25.790 -22.126 108.084 1.00 33.22  ? 104 GLY B O   1 
ATOM   2681 N N   . ALA B  1 90  ? 24.809 -22.133 110.153 1.00 33.12  ? 105 ALA B N   1 
ATOM   2682 C CA  . ALA B  1 90  ? 25.927 -21.619 110.983 1.00 32.24  ? 105 ALA B CA  1 
ATOM   2683 C C   . ALA B  1 90  ? 26.287 -20.202 110.527 1.00 30.75  ? 105 ALA B C   1 
ATOM   2684 O O   . ALA B  1 90  ? 27.485 -19.849 110.564 1.00 30.81  ? 105 ALA B O   1 
ATOM   2685 C CB  . ALA B  1 90  ? 27.103 -22.575 110.940 1.00 33.94  ? 105 ALA B CB  1 
ATOM   2686 N N   . ASP B  1 91  ? 25.275 -19.401 110.176 1.00 28.38  ? 106 ASP B N   1 
ATOM   2687 C CA  . ASP B  1 91  ? 25.451 -18.023 109.657 1.00 30.01  ? 106 ASP B CA  1 
ATOM   2688 C C   . ASP B  1 91  ? 25.633 -17.083 110.854 1.00 29.26  ? 106 ASP B C   1 
ATOM   2689 O O   . ASP B  1 91  ? 24.696 -16.340 111.213 1.00 30.48  ? 106 ASP B O   1 
ATOM   2690 C CB  . ASP B  1 91  ? 24.329 -17.628 108.696 1.00 29.34  ? 106 ASP B CB  1 
ATOM   2691 C CG  . ASP B  1 91  ? 24.622 -16.346 107.939 1.00 30.29  ? 106 ASP B CG  1 
ATOM   2692 O OD1 . ASP B  1 91  ? 25.803 -15.916 107.927 1.00 30.07  ? 106 ASP B OD1 1 
ATOM   2693 O OD2 . ASP B  1 91  ? 23.671 -15.777 107.379 1.00 30.08  ? 106 ASP B OD2 1 
ATOM   2694 N N   . ILE B  1 92  ? 26.814 -17.145 111.460 1.00 29.17  ? 107 ILE B N   1 
ATOM   2695 C CA  . ILE B  1 92  ? 27.164 -16.396 112.695 1.00 30.49  ? 107 ILE B CA  1 
ATOM   2696 C C   . ILE B  1 92  ? 28.672 -16.150 112.693 1.00 29.36  ? 107 ILE B C   1 
ATOM   2697 O O   . ILE B  1 92  ? 29.431 -17.060 112.314 1.00 28.92  ? 107 ILE B O   1 
ATOM   2698 C CB  . ILE B  1 92  ? 26.649 -17.134 113.946 1.00 31.22  ? 107 ILE B CB  1 
ATOM   2699 C CG1 . ILE B  1 92  ? 26.606 -16.217 115.166 1.00 33.60  ? 107 ILE B CG1 1 
ATOM   2700 C CG2 . ILE B  1 92  ? 27.415 -18.421 114.216 1.00 31.19  ? 107 ILE B CG2 1 
ATOM   2701 C CD1 . ILE B  1 92  ? 25.694 -16.726 116.267 1.00 33.27  ? 107 ILE B CD1 1 
ATOM   2702 N N   . ALA B  1 93  ? 29.061 -14.926 113.040 1.00 29.98  ? 108 ALA B N   1 
ATOM   2703 C CA  . ALA B  1 93  ? 30.466 -14.482 113.149 1.00 29.44  ? 108 ALA B CA  1 
ATOM   2704 C C   . ALA B  1 93  ? 30.609 -13.486 114.305 1.00 28.02  ? 108 ALA B C   1 
ATOM   2705 O O   . ALA B  1 93  ? 29.595 -12.935 114.766 1.00 28.48  ? 108 ALA B O   1 
ATOM   2706 C CB  . ALA B  1 93  ? 30.911 -13.899 111.834 1.00 28.95  ? 108 ALA B CB  1 
ATOM   2707 N N   . LEU B  1 94  ? 31.849 -13.280 114.740 1.00 30.18  ? 109 LEU B N   1 
ATOM   2708 C CA  . LEU B  1 94  ? 32.254 -12.379 115.842 1.00 31.11  ? 109 LEU B CA  1 
ATOM   2709 C C   . LEU B  1 94  ? 33.337 -11.431 115.325 1.00 30.77  ? 109 LEU B C   1 
ATOM   2710 O O   . LEU B  1 94  ? 34.235 -11.905 114.609 1.00 30.69  ? 109 LEU B O   1 
ATOM   2711 C CB  . LEU B  1 94  ? 32.760 -13.222 117.015 1.00 32.32  ? 109 LEU B CB  1 
ATOM   2712 C CG  . LEU B  1 94  ? 31.704 -14.047 117.751 1.00 31.94  ? 109 LEU B CG  1 
ATOM   2713 C CD1 . LEU B  1 94  ? 32.358 -15.065 118.676 1.00 32.57  ? 109 LEU B CD1 1 
ATOM   2714 C CD2 . LEU B  1 94  ? 30.749 -13.153 118.530 1.00 31.77  ? 109 LEU B CD2 1 
ATOM   2715 N N   . LEU B  1 95  ? 33.219 -10.136 115.631 1.00 32.69  ? 110 LEU B N   1 
ATOM   2716 C CA  . LEU B  1 95  ? 34.278 -9.125  115.380 1.00 33.42  ? 110 LEU B CA  1 
ATOM   2717 C C   . LEU B  1 95  ? 34.869 -8.713  116.725 1.00 32.97  ? 110 LEU B C   1 
ATOM   2718 O O   . LEU B  1 95  ? 34.093 -8.252  117.588 1.00 33.07  ? 110 LEU B O   1 
ATOM   2719 C CB  . LEU B  1 95  ? 33.690 -7.911  114.649 1.00 34.61  ? 110 LEU B CB  1 
ATOM   2720 C CG  . LEU B  1 95  ? 32.800 -8.212  113.445 1.00 35.43  ? 110 LEU B CG  1 
ATOM   2721 C CD1 . LEU B  1 95  ? 32.315 -6.914  112.811 1.00 35.82  ? 110 LEU B CD1 1 
ATOM   2722 C CD2 . LEU B  1 95  ? 33.535 -9.072  112.423 1.00 34.27  ? 110 LEU B CD2 1 
ATOM   2723 N N   . GLU B  1 96  ? 36.183 -8.859  116.899 1.00 33.47  ? 111 GLU B N   1 
ATOM   2724 C CA  . GLU B  1 96  ? 36.887 -8.293  118.076 1.00 34.79  ? 111 GLU B CA  1 
ATOM   2725 C C   . GLU B  1 96  ? 37.381 -6.894  117.709 1.00 33.77  ? 111 GLU B C   1 
ATOM   2726 O O   . GLU B  1 96  ? 38.171 -6.782  116.764 1.00 36.70  ? 111 GLU B O   1 
ATOM   2727 C CB  . GLU B  1 96  ? 38.029 -9.164  118.600 1.00 34.81  ? 111 GLU B CB  1 
ATOM   2728 C CG  . GLU B  1 96  ? 38.455 -8.721  119.995 1.00 37.06  ? 111 GLU B CG  1 
ATOM   2729 C CD  . GLU B  1 96  ? 39.525 -9.535  120.684 1.00 38.70  ? 111 GLU B CD  1 
ATOM   2730 O OE1 . GLU B  1 96  ? 40.260 -10.270 119.991 1.00 40.53  ? 111 GLU B OE1 1 
ATOM   2731 O OE2 . GLU B  1 96  ? 39.594 -9.434  121.918 1.00 42.80  ? 111 GLU B OE2 1 
ATOM   2732 N N   . LEU B  1 97  ? 36.957 -5.884  118.469 1.00 34.00  ? 112 LEU B N   1 
ATOM   2733 C CA  . LEU B  1 97  ? 37.447 -4.491  118.313 1.00 36.13  ? 112 LEU B CA  1 
ATOM   2734 C C   . LEU B  1 97  ? 38.866 -4.418  118.886 1.00 35.20  ? 112 LEU B C   1 
ATOM   2735 O O   . LEU B  1 97  ? 39.210 -5.248  119.742 1.00 37.30  ? 112 LEU B O   1 
ATOM   2736 C CB  . LEU B  1 97  ? 36.490 -3.525  119.022 1.00 34.12  ? 112 LEU B CB  1 
ATOM   2737 C CG  . LEU B  1 97  ? 35.037 -3.570  118.563 1.00 34.68  ? 112 LEU B CG  1 
ATOM   2738 C CD1 . LEU B  1 97  ? 34.192 -2.618  119.390 1.00 34.31  ? 112 LEU B CD1 1 
ATOM   2739 C CD2 . LEU B  1 97  ? 34.906 -3.243  117.082 1.00 36.44  ? 112 LEU B CD2 1 
ATOM   2740 N N   . GLU B  1 98  ? 39.670 -3.487  118.387 1.00 37.73  ? 113 GLU B N   1 
ATOM   2741 C CA  . GLU B  1 98  ? 41.069 -3.256  118.839 1.00 38.12  ? 113 GLU B CA  1 
ATOM   2742 C C   . GLU B  1 98  ? 41.074 -2.720  120.272 1.00 35.22  ? 113 GLU B C   1 
ATOM   2743 O O   . GLU B  1 98  ? 42.075 -2.946  120.974 1.00 35.92  ? 113 GLU B O   1 
ATOM   2744 C CB  . GLU B  1 98  ? 41.776 -2.260  117.921 1.00 38.28  ? 113 GLU B CB  1 
ATOM   2745 C CG  . GLU B  1 98  ? 42.053 -2.803  116.536 1.00 39.16  ? 113 GLU B CG  1 
ATOM   2746 C CD  . GLU B  1 98  ? 43.008 -1.960  115.717 1.00 39.48  ? 113 GLU B CD  1 
ATOM   2747 O OE1 . GLU B  1 98  ? 43.308 -2.365  114.579 1.00 43.44  ? 113 GLU B OE1 1 
ATOM   2748 O OE2 . GLU B  1 98  ? 43.440 -0.903  116.213 1.00 39.47  ? 113 GLU B OE2 1 
ATOM   2749 N N   . GLU B  1 99  ? 40.019 -1.998  120.661 1.00 34.30  ? 114 GLU B N   1 
ATOM   2750 C CA  . GLU B  1 99  ? 39.839 -1.429  122.016 1.00 35.45  ? 114 GLU B CA  1 
ATOM   2751 C C   . GLU B  1 99  ? 38.430 -1.744  122.505 1.00 35.14  ? 114 GLU B C   1 
ATOM   2752 O O   . GLU B  1 99  ? 37.502 -1.862  121.703 1.00 33.49  ? 114 GLU B O   1 
ATOM   2753 C CB  . GLU B  1 99  ? 40.031 0.095   122.029 1.00 35.10  ? 114 GLU B CB  1 
ATOM   2754 C CG  . GLU B  1 99  ? 41.325 0.578   121.392 1.00 34.77  ? 114 GLU B CG  1 
ATOM   2755 C CD  . GLU B  1 99  ? 42.617 0.194   122.092 1.00 34.20  ? 114 GLU B CD  1 
ATOM   2756 O OE1 . GLU B  1 99  ? 42.554 -0.328  123.218 1.00 37.24  ? 114 GLU B OE1 1 
ATOM   2757 O OE2 . GLU B  1 99  ? 43.683 0.421   121.505 1.00 34.05  ? 114 GLU B OE2 1 
ATOM   2758 N N   . PRO B  1 100 ? 38.230 -1.871  123.832 1.00 36.61  ? 115 PRO B N   1 
ATOM   2759 C CA  . PRO B  1 100 ? 36.886 -1.948  124.395 1.00 39.63  ? 115 PRO B CA  1 
ATOM   2760 C C   . PRO B  1 100 ? 36.244 -0.559  124.283 1.00 40.62  ? 115 PRO B C   1 
ATOM   2761 O O   . PRO B  1 100 ? 36.943 0.419   124.404 1.00 43.96  ? 115 PRO B O   1 
ATOM   2762 C CB  . PRO B  1 100 ? 37.125 -2.380  125.840 1.00 39.05  ? 115 PRO B CB  1 
ATOM   2763 C CG  . PRO B  1 100 ? 38.501 -1.835  126.156 1.00 39.97  ? 115 PRO B CG  1 
ATOM   2764 C CD  . PRO B  1 100 ? 39.277 -1.935  124.863 1.00 39.21  ? 115 PRO B CD  1 
ATOM   2765 N N   . VAL B  1 101 ? 34.956 -0.508  123.976 1.00 38.07  ? 116 VAL B N   1 
ATOM   2766 C CA  . VAL B  1 101 ? 34.199 0.772   123.885 1.00 39.13  ? 116 VAL B CA  1 
ATOM   2767 C C   . VAL B  1 101 ? 33.762 1.139   125.307 1.00 37.50  ? 116 VAL B C   1 
ATOM   2768 O O   . VAL B  1 101 ? 33.550 0.209   126.124 1.00 36.44  ? 116 VAL B O   1 
ATOM   2769 C CB  . VAL B  1 101 ? 33.013 0.686   122.901 1.00 39.77  ? 116 VAL B CB  1 
ATOM   2770 C CG1 . VAL B  1 101 ? 33.453 0.161   121.544 1.00 41.55  ? 116 VAL B CG1 1 
ATOM   2771 C CG2 . VAL B  1 101 ? 31.845 -0.124  123.441 1.00 38.51  ? 116 VAL B CG2 1 
ATOM   2772 N N   . LYS B  1 102 ? 33.631 2.436   125.580 1.00 37.85  ? 117 LYS B N   1 
ATOM   2773 C CA  . LYS B  1 102 ? 33.006 2.977   126.812 1.00 39.88  ? 117 LYS B CA  1 
ATOM   2774 C C   . LYS B  1 102 ? 31.489 2.920   126.621 1.00 40.08  ? 117 LYS B C   1 
ATOM   2775 O O   . LYS B  1 102 ? 30.993 3.538   125.671 1.00 41.50  ? 117 LYS B O   1 
ATOM   2776 C CB  . LYS B  1 102 ? 33.456 4.413   127.101 1.00 42.19  ? 117 LYS B CB  1 
ATOM   2777 C CG  . LYS B  1 102 ? 34.959 4.641   127.198 1.00 43.40  ? 117 LYS B CG  1 
ATOM   2778 C CD  . LYS B  1 102 ? 35.707 3.694   128.117 1.00 45.77  ? 117 LYS B CD  1 
ATOM   2779 C CE  . LYS B  1 102 ? 37.182 4.033   128.207 1.00 47.45  ? 117 LYS B CE  1 
ATOM   2780 N NZ  . LYS B  1 102 ? 37.926 3.059   129.042 1.00 49.11  ? 117 LYS B NZ  1 
ATOM   2781 N N   . VAL B  1 103 ? 30.791 2.185   127.481 1.00 39.85  ? 118 VAL B N   1 
ATOM   2782 C CA  . VAL B  1 103 ? 29.314 2.002   127.392 1.00 40.58  ? 118 VAL B CA  1 
ATOM   2783 C C   . VAL B  1 103 ? 28.618 3.184   128.073 1.00 41.24  ? 118 VAL B C   1 
ATOM   2784 O O   . VAL B  1 103 ? 29.234 3.838   128.929 1.00 42.90  ? 118 VAL B O   1 
ATOM   2785 C CB  . VAL B  1 103 ? 28.839 0.637   127.931 1.00 40.40  ? 118 VAL B CB  1 
ATOM   2786 C CG1 . VAL B  1 103 ? 29.480 -0.509  127.159 1.00 41.53  ? 118 VAL B CG1 1 
ATOM   2787 C CG2 . VAL B  1 103 ? 29.052 0.470   129.426 1.00 42.10  ? 118 VAL B CG2 1 
ATOM   2788 N N   . SER B  1 104 ? 27.376 3.444   127.665 1.00 41.22  ? 119 SER B N   1 
ATOM   2789 C CA  . SER B  1 104 ? 26.487 4.519   128.174 1.00 43.68  ? 119 SER B CA  1 
ATOM   2790 C C   . SER B  1 104 ? 25.030 4.080   127.981 1.00 44.57  ? 119 SER B C   1 
ATOM   2791 O O   . SER B  1 104 ? 24.823 2.966   127.472 1.00 44.28  ? 119 SER B O   1 
ATOM   2792 C CB  . SER B  1 104 ? 26.777 5.824   127.477 1.00 41.83  ? 119 SER B CB  1 
ATOM   2793 O OG  . SER B  1 104 ? 26.581 5.706   126.076 1.00 42.52  ? 119 SER B OG  1 
ATOM   2794 N N   . SER B  1 105 ? 24.066 4.921   128.358 1.00 45.98  ? 120 SER B N   1 
ATOM   2795 C CA  . SER B  1 105 ? 22.616 4.671   128.144 1.00 49.24  ? 120 SER B CA  1 
ATOM   2796 C C   . SER B  1 105 ? 22.315 4.601   126.639 1.00 47.19  ? 120 SER B C   1 
ATOM   2797 O O   . SER B  1 105 ? 21.448 3.797   126.261 1.00 49.75  ? 120 SER B O   1 
ATOM   2798 C CB  . SER B  1 105 ? 21.767 5.713   128.839 1.00 50.66  ? 120 SER B CB  1 
ATOM   2799 O OG  . SER B  1 105 ? 21.920 6.981   128.221 1.00 51.79  ? 120 SER B OG  1 
ATOM   2800 N N   . HIS B  1 106 ? 23.035 5.382   125.822 1.00 45.12  ? 121 HIS B N   1 
ATOM   2801 C CA  . HIS B  1 106 ? 22.843 5.518   124.354 1.00 45.13  ? 121 HIS B CA  1 
ATOM   2802 C C   . HIS B  1 106 ? 23.599 4.426   123.578 1.00 45.99  ? 121 HIS B C   1 
ATOM   2803 O O   . HIS B  1 106 ? 23.167 4.119   122.452 1.00 48.89  ? 121 HIS B O   1 
ATOM   2804 C CB  . HIS B  1 106 ? 23.253 6.925   123.894 1.00 46.92  ? 121 HIS B CB  1 
ATOM   2805 C CG  . HIS B  1 106 ? 22.770 7.261   122.522 0.00 46.42  ? 121 HIS B CG  1 
ATOM   2806 N ND1 . HIS B  1 106 ? 23.465 6.873   121.395 0.00 46.44  ? 121 HIS B ND1 1 
ATOM   2807 C CD2 . HIS B  1 106 ? 21.682 7.933   122.086 0.00 46.49  ? 121 HIS B CD2 1 
ATOM   2808 C CE1 . HIS B  1 106 ? 22.829 7.298   120.322 0.00 46.43  ? 121 HIS B CE1 1 
ATOM   2809 N NE2 . HIS B  1 106 ? 21.731 7.951   120.719 0.00 46.44  ? 121 HIS B NE2 1 
ATOM   2810 N N   . VAL B  1 107 ? 24.697 3.889   124.121 1.00 43.30  ? 122 VAL B N   1 
ATOM   2811 C CA  . VAL B  1 107 ? 25.529 2.828   123.473 1.00 41.40  ? 122 VAL B CA  1 
ATOM   2812 C C   . VAL B  1 107 ? 25.899 1.777   124.526 1.00 39.24  ? 122 VAL B C   1 
ATOM   2813 O O   . VAL B  1 107 ? 26.741 2.082   125.381 1.00 36.96  ? 122 VAL B O   1 
ATOM   2814 C CB  . VAL B  1 107 ? 26.792 3.428   122.819 1.00 45.38  ? 122 VAL B CB  1 
ATOM   2815 C CG1 . VAL B  1 107 ? 27.725 2.351   122.279 1.00 46.37  ? 122 VAL B CG1 1 
ATOM   2816 C CG2 . VAL B  1 107 ? 26.457 4.432   121.730 1.00 46.85  ? 122 VAL B CG2 1 
ATOM   2817 N N   . HIS B  1 108 ? 25.320 0.576   124.456 1.00 36.72  ? 123 HIS B N   1 
ATOM   2818 C CA  . HIS B  1 108 ? 25.641 -0.543  125.384 1.00 37.03  ? 123 HIS B CA  1 
ATOM   2819 C C   . HIS B  1 108 ? 25.217 -1.890  124.788 1.00 35.95  ? 123 HIS B C   1 
ATOM   2820 O O   . HIS B  1 108 ? 24.570 -1.905  123.728 1.00 35.15  ? 123 HIS B O   1 
ATOM   2821 C CB  . HIS B  1 108 ? 25.082 -0.279  126.795 1.00 38.51  ? 123 HIS B CB  1 
ATOM   2822 C CG  . HIS B  1 108 ? 23.601 -0.300  126.950 1.00 39.07  ? 123 HIS B CG  1 
ATOM   2823 N ND1 . HIS B  1 108 ? 22.866 0.854   127.162 1.00 41.07  ? 123 HIS B ND1 1 
ATOM   2824 C CD2 . HIS B  1 108 ? 22.724 -1.323  127.037 1.00 38.38  ? 123 HIS B CD2 1 
ATOM   2825 C CE1 . HIS B  1 108 ? 21.595 0.544   127.321 1.00 40.71  ? 123 HIS B CE1 1 
ATOM   2826 N NE2 . HIS B  1 108 ? 21.481 -0.787  127.244 1.00 41.23  ? 123 HIS B NE2 1 
ATOM   2827 N N   . THR B  1 109 ? 25.602 -2.972  125.463 1.00 34.53  ? 124 THR B N   1 
ATOM   2828 C CA  . THR B  1 109 ? 25.515 -4.365  124.970 1.00 35.22  ? 124 THR B CA  1 
ATOM   2829 C C   . THR B  1 109 ? 24.068 -4.858  125.023 1.00 33.87  ? 124 THR B C   1 
ATOM   2830 O O   . THR B  1 109 ? 23.285 -4.349  125.845 1.00 34.20  ? 124 THR B O   1 
ATOM   2831 C CB  . THR B  1 109 ? 26.416 -5.313  125.769 1.00 34.03  ? 124 THR B CB  1 
ATOM   2832 O OG1 . THR B  1 109 ? 25.964 -5.293  127.123 1.00 37.83  ? 124 THR B OG1 1 
ATOM   2833 C CG2 . THR B  1 109 ? 27.878 -4.940  125.709 1.00 36.40  ? 124 THR B CG2 1 
ATOM   2834 N N   . VAL B  1 110 ? 23.739 -5.807  124.151 1.00 34.87  ? 125 VAL B N   1 
ATOM   2835 C CA  . VAL B  1 110 ? 22.480 -6.606  124.207 1.00 35.00  ? 125 VAL B CA  1 
ATOM   2836 C C   . VAL B  1 110 ? 22.782 -7.879  125.004 1.00 33.92  ? 125 VAL B C   1 
ATOM   2837 O O   . VAL B  1 110 ? 23.919 -8.377  124.930 1.00 33.94  ? 125 VAL B O   1 
ATOM   2838 C CB  . VAL B  1 110 ? 21.919 -6.911  122.804 1.00 33.31  ? 125 VAL B CB  1 
ATOM   2839 C CG1 . VAL B  1 110 ? 22.784 -7.880  122.015 1.00 33.78  ? 125 VAL B CG1 1 
ATOM   2840 C CG2 . VAL B  1 110 ? 20.477 -7.400  122.862 1.00 33.02  ? 125 VAL B CG2 1 
ATOM   2841 N N   . THR B  1 111 ? 21.783 -8.381  125.729 1.00 34.30  ? 126 THR B N   1 
ATOM   2842 C CA  . THR B  1 111 ? 21.850 -9.627  126.532 1.00 33.93  ? 126 THR B CA  1 
ATOM   2843 C C   . THR B  1 111 ? 21.544 -10.810 125.609 1.00 34.87  ? 126 THR B C   1 
ATOM   2844 O O   . THR B  1 111 ? 20.552 -10.729 124.846 1.00 33.97  ? 126 THR B O   1 
ATOM   2845 C CB  . THR B  1 111 ? 20.878 -9.567  127.718 1.00 35.15  ? 126 THR B CB  1 
ATOM   2846 O OG1 . THR B  1 111 ? 21.117 -8.358  128.439 1.00 35.60  ? 126 THR B OG1 1 
ATOM   2847 C CG2 . THR B  1 111 ? 20.994 -10.754 128.651 1.00 33.83  ? 126 THR B CG2 1 
ATOM   2848 N N   . LEU B  1 112 ? 22.367 -11.860 125.671 1.00 35.25  ? 127 LEU B N   1 
ATOM   2849 C CA  . LEU B  1 112 ? 22.127 -13.130 124.941 1.00 36.62  ? 127 LEU B CA  1 
ATOM   2850 C C   . LEU B  1 112 ? 21.148 -13.982 125.741 1.00 36.06  ? 127 LEU B C   1 
ATOM   2851 O O   . LEU B  1 112 ? 21.146 -13.936 126.968 1.00 35.44  ? 127 LEU B O   1 
ATOM   2852 C CB  . LEU B  1 112 ? 23.456 -13.858 124.718 1.00 36.84  ? 127 LEU B CB  1 
ATOM   2853 C CG  . LEU B  1 112 ? 24.494 -13.100 123.895 1.00 38.26  ? 127 LEU B CG  1 
ATOM   2854 C CD1 . LEU B  1 112 ? 25.676 -13.998 123.576 1.00 39.76  ? 127 LEU B CD1 1 
ATOM   2855 C CD2 . LEU B  1 112 ? 23.907 -12.549 122.607 1.00 40.03  ? 127 LEU B CD2 1 
ATOM   2856 N N   . PRO B  1 113 ? 20.285 -14.776 125.064 1.00 36.26  ? 128 PRO B N   1 
ATOM   2857 C CA  . PRO B  1 113 ? 19.280 -15.571 125.760 1.00 38.16  ? 128 PRO B CA  1 
ATOM   2858 C C   . PRO B  1 113 ? 19.913 -16.759 126.477 1.00 38.87  ? 128 PRO B C   1 
ATOM   2859 O O   . PRO B  1 113 ? 21.008 -17.185 126.120 1.00 40.45  ? 128 PRO B O   1 
ATOM   2860 C CB  . PRO B  1 113 ? 18.344 -16.030 124.633 1.00 37.90  ? 128 PRO B CB  1 
ATOM   2861 C CG  . PRO B  1 113 ? 19.212 -16.050 123.389 1.00 37.50  ? 128 PRO B CG  1 
ATOM   2862 C CD  . PRO B  1 113 ? 20.240 -14.959 123.605 1.00 36.50  ? 128 PRO B CD  1 
ATOM   2863 N N   . PRO B  1 114 ? 19.247 -17.332 127.504 1.00 40.50  ? 129 PRO B N   1 
ATOM   2864 C CA  . PRO B  1 114 ? 19.643 -18.642 128.022 1.00 40.75  ? 129 PRO B CA  1 
ATOM   2865 C C   . PRO B  1 114 ? 19.319 -19.714 126.971 1.00 40.52  ? 129 PRO B C   1 
ATOM   2866 O O   . PRO B  1 114 ? 18.453 -19.472 126.135 1.00 40.08  ? 129 PRO B O   1 
ATOM   2867 C CB  . PRO B  1 114 ? 18.805 -18.800 129.301 1.00 42.06  ? 129 PRO B CB  1 
ATOM   2868 C CG  . PRO B  1 114 ? 17.588 -17.924 129.064 1.00 41.24  ? 129 PRO B CG  1 
ATOM   2869 C CD  . PRO B  1 114 ? 18.080 -16.773 128.209 1.00 40.43  ? 129 PRO B CD  1 
ATOM   2870 N N   . ALA B  1 115 ? 20.009 -20.855 127.042 1.00 43.41  ? 130 ALA B N   1 
ATOM   2871 C CA  . ALA B  1 115 ? 19.913 -21.978 126.078 1.00 45.06  ? 130 ALA B CA  1 
ATOM   2872 C C   . ALA B  1 115 ? 18.463 -22.471 125.946 1.00 46.06  ? 130 ALA B C   1 
ATOM   2873 O O   . ALA B  1 115 ? 18.073 -22.853 124.825 1.00 47.33  ? 130 ALA B O   1 
ATOM   2874 C CB  . ALA B  1 115 ? 20.839 -23.089 126.499 1.00 46.50  ? 130 ALA B CB  1 
ATOM   2875 N N   . SER B  1 116 ? 17.688 -22.439 127.033 1.00 48.56  ? 131 SER B N   1 
ATOM   2876 C CA  . SER B  1 116 ? 16.313 -22.999 127.113 1.00 49.46  ? 131 SER B CA  1 
ATOM   2877 C C   . SER B  1 116 ? 15.292 -22.134 126.360 1.00 49.16  ? 131 SER B C   1 
ATOM   2878 O O   . SER B  1 116 ? 14.217 -22.686 126.043 1.00 48.95  ? 131 SER B O   1 
ATOM   2879 C CB  . SER B  1 116 ? 15.898 -23.194 128.547 1.00 50.49  ? 131 SER B CB  1 
ATOM   2880 O OG  . SER B  1 116 ? 15.982 -21.975 129.264 1.00 53.75  ? 131 SER B OG  1 
ATOM   2881 N N   . GLU B  1 117 ? 15.586 -20.854 126.075 1.00 47.12  ? 132 GLU B N   1 
ATOM   2882 C CA  . GLU B  1 117 ? 14.573 -19.929 125.478 1.00 47.37  ? 132 GLU B CA  1 
ATOM   2883 C C   . GLU B  1 117 ? 14.337 -20.326 124.011 1.00 47.57  ? 132 GLU B C   1 
ATOM   2884 O O   . GLU B  1 117 ? 15.307 -20.286 123.236 1.00 45.84  ? 132 GLU B O   1 
ATOM   2885 C CB  . GLU B  1 117 ? 14.996 -18.463 125.618 1.00 48.28  ? 132 GLU B CB  1 
ATOM   2886 C CG  . GLU B  1 117 ? 13.982 -17.446 125.096 1.00 49.89  ? 132 GLU B CG  1 
ATOM   2887 C CD  . GLU B  1 117 ? 12.590 -17.477 125.714 1.00 53.87  ? 132 GLU B CD  1 
ATOM   2888 O OE1 . GLU B  1 117 ? 12.473 -17.182 126.921 1.00 55.62  ? 132 GLU B OE1 1 
ATOM   2889 O OE2 . GLU B  1 117 ? 11.628 -17.811 124.988 1.00 56.23  ? 132 GLU B OE2 1 
ATOM   2890 N N   . THR B  1 118 ? 13.086 -20.634 123.639 1.00 46.40  ? 133 THR B N   1 
ATOM   2891 C CA  . THR B  1 118 ? 12.682 -21.105 122.281 1.00 48.33  ? 133 THR B CA  1 
ATOM   2892 C C   . THR B  1 118 ? 12.094 -19.979 121.419 1.00 48.42  ? 133 THR B C   1 
ATOM   2893 O O   . THR B  1 118 ? 12.067 -20.181 120.189 1.00 48.23  ? 133 THR B O   1 
ATOM   2894 C CB  . THR B  1 118 ? 11.656 -22.243 122.344 1.00 49.87  ? 133 THR B CB  1 
ATOM   2895 O OG1 . THR B  1 118 ? 10.504 -21.800 123.065 1.00 52.23  ? 133 THR B OG1 1 
ATOM   2896 C CG2 . THR B  1 118 ? 12.215 -23.487 123.002 1.00 51.74  ? 133 THR B CG2 1 
ATOM   2897 N N   . PHE B  1 119 ? 11.631 -18.885 122.038 1.00 46.53  ? 134 PHE B N   1 
ATOM   2898 C CA  . PHE B  1 119 ? 10.960 -17.725 121.394 1.00 45.03  ? 134 PHE B CA  1 
ATOM   2899 C C   . PHE B  1 119 ? 9.723  -18.199 120.627 1.00 47.31  ? 134 PHE B C   1 
ATOM   2900 O O   . PHE B  1 119 ? 9.721  -18.226 119.396 1.00 45.37  ? 134 PHE B O   1 
ATOM   2901 C CB  . PHE B  1 119 ? 11.955 -16.938 120.535 1.00 42.52  ? 134 PHE B CB  1 
ATOM   2902 C CG  . PHE B  1 119 ? 13.103 -16.346 121.310 1.00 40.48  ? 134 PHE B CG  1 
ATOM   2903 C CD1 . PHE B  1 119 ? 12.943 -15.170 122.032 1.00 40.26  ? 134 PHE B CD1 1 
ATOM   2904 C CD2 . PHE B  1 119 ? 14.342 -16.968 121.324 1.00 39.18  ? 134 PHE B CD2 1 
ATOM   2905 C CE1 . PHE B  1 119 ? 14.003 -14.628 122.744 1.00 40.80  ? 134 PHE B CE1 1 
ATOM   2906 C CE2 . PHE B  1 119 ? 15.404 -16.412 122.021 1.00 38.25  ? 134 PHE B CE2 1 
ATOM   2907 C CZ  . PHE B  1 119 ? 15.230 -15.249 122.737 1.00 37.84  ? 134 PHE B CZ  1 
ATOM   2908 N N   . PRO B  1 120 ? 8.620  -18.576 121.318 1.00 49.09  ? 135 PRO B N   1 
ATOM   2909 C CA  . PRO B  1 120 ? 7.438  -19.100 120.633 1.00 49.14  ? 135 PRO B CA  1 
ATOM   2910 C C   . PRO B  1 120 ? 6.684  -18.008 119.874 1.00 48.62  ? 135 PRO B C   1 
ATOM   2911 O O   . PRO B  1 120 ? 6.842  -16.823 120.175 1.00 49.96  ? 135 PRO B O   1 
ATOM   2912 C CB  . PRO B  1 120 ? 6.590  -19.658 121.786 1.00 50.21  ? 135 PRO B CB  1 
ATOM   2913 C CG  . PRO B  1 120 ? 6.959  -18.785 122.968 1.00 51.47  ? 135 PRO B CG  1 
ATOM   2914 C CD  . PRO B  1 120 ? 8.437  -18.510 122.779 1.00 49.61  ? 135 PRO B CD  1 
ATOM   2915 N N   . PRO B  1 121 ? 5.827  -18.373 118.889 1.00 46.98  ? 136 PRO B N   1 
ATOM   2916 C CA  . PRO B  1 121 ? 4.921  -17.419 118.248 1.00 48.56  ? 136 PRO B CA  1 
ATOM   2917 C C   . PRO B  1 121 ? 4.083  -16.605 119.248 1.00 51.10  ? 136 PRO B C   1 
ATOM   2918 O O   . PRO B  1 121 ? 3.683  -17.161 120.251 1.00 52.30  ? 136 PRO B O   1 
ATOM   2919 C CB  . PRO B  1 121 ? 3.991  -18.318 117.414 1.00 48.64  ? 136 PRO B CB  1 
ATOM   2920 C CG  . PRO B  1 121 ? 4.820  -19.543 117.118 1.00 48.72  ? 136 PRO B CG  1 
ATOM   2921 C CD  . PRO B  1 121 ? 5.678  -19.734 118.348 1.00 49.29  ? 136 PRO B CD  1 
ATOM   2922 N N   . GLY B  1 122 ? 3.823  -15.328 118.940 1.00 52.32  ? 137 GLY B N   1 
ATOM   2923 C CA  . GLY B  1 122 ? 3.087  -14.395 119.814 1.00 50.90  ? 137 GLY B CA  1 
ATOM   2924 C C   . GLY B  1 122 ? 4.015  -13.561 120.680 1.00 51.15  ? 137 GLY B C   1 
ATOM   2925 O O   . GLY B  1 122 ? 3.557  -12.526 121.194 1.00 52.80  ? 137 GLY B O   1 
ATOM   2926 N N   . MET B  1 123 ? 5.270  -13.977 120.855 1.00 53.21  ? 138 MET B N   1 
ATOM   2927 C CA  . MET B  1 123 ? 6.289  -13.169 121.570 1.00 57.03  ? 138 MET B CA  1 
ATOM   2928 C C   . MET B  1 123 ? 6.542  -11.882 120.788 1.00 55.43  ? 138 MET B C   1 
ATOM   2929 O O   . MET B  1 123 ? 6.718  -11.943 119.571 1.00 56.49  ? 138 MET B O   1 
ATOM   2930 C CB  . MET B  1 123 ? 7.594  -13.949 121.708 1.00 61.29  ? 138 MET B CB  1 
ATOM   2931 C CG  . MET B  1 123 ? 8.555  -13.269 122.634 1.00 66.28  ? 138 MET B CG  1 
ATOM   2932 S SD  . MET B  1 123 ? 9.530  -14.466 123.578 1.00 75.23  ? 138 MET B SD  1 
ATOM   2933 C CE  . MET B  1 123 ? 8.347  -14.989 124.819 1.00 74.99  ? 138 MET B CE  1 
ATOM   2934 N N   . PRO B  1 124 ? 6.560  -10.685 121.432 1.00 53.92  ? 139 PRO B N   1 
ATOM   2935 C CA  . PRO B  1 124 ? 6.862  -9.434  120.733 1.00 52.00  ? 139 PRO B CA  1 
ATOM   2936 C C   . PRO B  1 124 ? 8.357  -9.354  120.396 1.00 48.41  ? 139 PRO B C   1 
ATOM   2937 O O   . PRO B  1 124 ? 9.153  -9.336  121.322 1.00 49.05  ? 139 PRO B O   1 
ATOM   2938 C CB  . PRO B  1 124 ? 6.439  -8.337  121.725 1.00 52.97  ? 139 PRO B CB  1 
ATOM   2939 C CG  . PRO B  1 124 ? 6.592  -8.985  123.081 1.00 53.68  ? 139 PRO B CG  1 
ATOM   2940 C CD  . PRO B  1 124 ? 6.269  -10.451 122.858 1.00 57.11  ? 139 PRO B CD  1 
ATOM   2941 N N   . CYS B  1 125 ? 8.701  -9.335  119.101 1.00 45.29  ? 140 CYS B N   1 
ATOM   2942 C CA  . CYS B  1 125 ? 10.105 -9.270  118.619 1.00 43.07  ? 140 CYS B CA  1 
ATOM   2943 C C   . CYS B  1 125 ? 10.262 -8.159  117.581 1.00 40.42  ? 140 CYS B C   1 
ATOM   2944 O O   . CYS B  1 125 ? 9.327  -7.923  116.777 1.00 39.24  ? 140 CYS B O   1 
ATOM   2945 C CB  . CYS B  1 125 ? 10.597 -10.602 118.065 1.00 44.27  ? 140 CYS B CB  1 
ATOM   2946 S SG  . CYS B  1 125 ? 10.384 -11.976 119.228 1.00 51.78  ? 140 CYS B SG  1 
ATOM   2947 N N   . TRP B  1 126 ? 11.426 -7.511  117.613 1.00 38.00  ? 141 TRP B N   1 
ATOM   2948 C CA  . TRP B  1 126 ? 11.778 -6.350  116.756 1.00 36.43  ? 141 TRP B CA  1 
ATOM   2949 C C   . TRP B  1 126 ? 13.076 -6.635  115.994 1.00 34.76  ? 141 TRP B C   1 
ATOM   2950 O O   . TRP B  1 126 ? 13.997 -7.218  116.592 1.00 32.63  ? 141 TRP B O   1 
ATOM   2951 C CB  . TRP B  1 126 ? 11.908 -5.088  117.608 1.00 36.89  ? 141 TRP B CB  1 
ATOM   2952 C CG  . TRP B  1 126 ? 10.609 -4.660  118.211 1.00 39.51  ? 141 TRP B CG  1 
ATOM   2953 C CD1 . TRP B  1 126 ? 9.982  -5.189  119.303 1.00 40.64  ? 141 TRP B CD1 1 
ATOM   2954 C CD2 . TRP B  1 126 ? 9.767  -3.603  117.737 1.00 40.42  ? 141 TRP B CD2 1 
ATOM   2955 N NE1 . TRP B  1 126 ? 8.806  -4.531  119.541 1.00 42.00  ? 141 TRP B NE1 1 
ATOM   2956 C CE2 . TRP B  1 126 ? 8.647  -3.553  118.596 1.00 42.47  ? 141 TRP B CE2 1 
ATOM   2957 C CE3 . TRP B  1 126 ? 9.860  -2.690  116.685 1.00 40.25  ? 141 TRP B CE3 1 
ATOM   2958 C CZ2 . TRP B  1 126 ? 7.618  -2.630  118.415 1.00 44.54  ? 141 TRP B CZ2 1 
ATOM   2959 C CZ3 . TRP B  1 126 ? 8.838  -1.789  116.501 1.00 44.21  ? 141 TRP B CZ3 1 
ATOM   2960 C CH2 . TRP B  1 126 ? 7.740  -1.748  117.364 1.00 44.26  ? 141 TRP B CH2 1 
ATOM   2961 N N   . VAL B  1 127 ? 13.130 -6.243  114.722 1.00 33.94  ? 142 VAL B N   1 
ATOM   2962 C CA  . VAL B  1 127 ? 14.364 -6.266  113.886 1.00 34.42  ? 142 VAL B CA  1 
ATOM   2963 C C   . VAL B  1 127 ? 14.651 -4.820  113.474 1.00 33.95  ? 142 VAL B C   1 
ATOM   2964 O O   . VAL B  1 127 ? 13.688 -4.053  113.244 1.00 33.00  ? 142 VAL B O   1 
ATOM   2965 C CB  . VAL B  1 127 ? 14.251 -7.233  112.690 1.00 35.47  ? 142 VAL B CB  1 
ATOM   2966 C CG1 . VAL B  1 127 ? 13.168 -6.832  111.688 1.00 37.06  ? 142 VAL B CG1 1 
ATOM   2967 C CG2 . VAL B  1 127 ? 15.595 -7.413  111.997 1.00 35.93  ? 142 VAL B CG2 1 
ATOM   2968 N N   . THR B  1 128 ? 15.933 -4.456  113.439 1.00 33.11  ? 143 THR B N   1 
ATOM   2969 C CA  . THR B  1 128 ? 16.422 -3.068  113.266 1.00 33.00  ? 143 THR B CA  1 
ATOM   2970 C C   . THR B  1 128 ? 17.557 -3.053  112.239 1.00 31.61  ? 143 THR B C   1 
ATOM   2971 O O   . THR B  1 128 ? 18.285 -4.066  112.116 1.00 30.42  ? 143 THR B O   1 
ATOM   2972 C CB  . THR B  1 128 ? 16.840 -2.467  114.618 1.00 33.52  ? 143 THR B CB  1 
ATOM   2973 O OG1 . THR B  1 128 ? 17.802 -3.313  115.249 1.00 35.09  ? 143 THR B OG1 1 
ATOM   2974 C CG2 . THR B  1 128 ? 15.667 -2.281  115.546 1.00 33.59  ? 143 THR B CG2 1 
ATOM   2975 N N   . GLY B  1 129 ? 17.691 -1.946  111.514 1.00 30.60  ? 144 GLY B N   1 
ATOM   2976 C CA  . GLY B  1 129 ? 18.860 -1.719  110.649 1.00 32.74  ? 144 GLY B CA  1 
ATOM   2977 C C   . GLY B  1 129 ? 18.642 -0.606  109.656 1.00 31.64  ? 144 GLY B C   1 
ATOM   2978 O O   . GLY B  1 129 ? 17.574 0.052   109.694 1.00 29.64  ? 144 GLY B O   1 
ATOM   2979 N N   . TRP B  1 130 ? 19.645 -0.415  108.800 1.00 31.77  ? 145 TRP B N   1 
ATOM   2980 C CA  . TRP B  1 130 ? 19.693 0.632   107.753 1.00 32.75  ? 145 TRP B CA  1 
ATOM   2981 C C   . TRP B  1 130 ? 19.552 -0.011  106.371 1.00 33.45  ? 145 TRP B C   1 
ATOM   2982 O O   . TRP B  1 130 ? 20.010 0.598   105.395 1.00 33.82  ? 145 TRP B O   1 
ATOM   2983 C CB  . TRP B  1 130 ? 20.999 1.420   107.872 1.00 32.41  ? 145 TRP B CB  1 
ATOM   2984 C CG  . TRP B  1 130 ? 21.171 2.171   109.152 1.00 30.36  ? 145 TRP B CG  1 
ATOM   2985 C CD1 . TRP B  1 130 ? 20.729 3.431   109.436 1.00 29.80  ? 145 TRP B CD1 1 
ATOM   2986 C CD2 . TRP B  1 130 ? 21.904 1.730   110.304 1.00 31.40  ? 145 TRP B CD2 1 
ATOM   2987 N NE1 . TRP B  1 130 ? 21.126 3.804   110.690 1.00 29.29  ? 145 TRP B NE1 1 
ATOM   2988 C CE2 . TRP B  1 130 ? 21.853 2.780   111.247 1.00 31.00  ? 145 TRP B CE2 1 
ATOM   2989 C CE3 . TRP B  1 130 ? 22.593 0.553   110.630 1.00 31.48  ? 145 TRP B CE3 1 
ATOM   2990 C CZ2 . TRP B  1 130 ? 22.462 2.676   112.497 1.00 30.59  ? 145 TRP B CZ2 1 
ATOM   2991 C CZ3 . TRP B  1 130 ? 23.191 0.458   111.865 1.00 32.86  ? 145 TRP B CZ3 1 
ATOM   2992 C CH2 . TRP B  1 130 ? 23.131 1.509   112.784 1.00 32.08  ? 145 TRP B CH2 1 
ATOM   2993 N N   . GLY B  1 131 ? 18.921 -1.189  106.290 1.00 34.20  ? 146 GLY B N   1 
ATOM   2994 C CA  . GLY B  1 131 ? 18.770 -1.936  105.029 1.00 32.70  ? 146 GLY B CA  1 
ATOM   2995 C C   . GLY B  1 131 ? 17.657 -1.370  104.167 1.00 33.30  ? 146 GLY B C   1 
ATOM   2996 O O   . GLY B  1 131 ? 17.008 -0.371  104.566 1.00 33.96  ? 146 GLY B O   1 
ATOM   2997 N N   . ASP B  1 132 ? 17.437 -2.008  103.017 1.00 35.63  ? 147 ASP B N   1 
ATOM   2998 C CA  . ASP B  1 132 ? 16.469 -1.588  101.969 1.00 36.30  ? 147 ASP B CA  1 
ATOM   2999 C C   . ASP B  1 132 ? 15.065 -1.533  102.586 1.00 36.04  ? 147 ASP B C   1 
ATOM   3000 O O   . ASP B  1 132 ? 14.764 -2.345  103.486 1.00 34.28  ? 147 ASP B O   1 
ATOM   3001 C CB  . ASP B  1 132 ? 16.546 -2.522  100.759 1.00 38.16  ? 147 ASP B CB  1 
ATOM   3002 C CG  . ASP B  1 132 ? 17.828 -2.436  99.943  1.00 39.62  ? 147 ASP B CG  1 
ATOM   3003 O OD1 . ASP B  1 132 ? 18.719 -1.647  100.307 1.00 39.34  ? 147 ASP B OD1 1 
ATOM   3004 O OD2 . ASP B  1 132 ? 17.922 -3.170  98.946  1.00 44.96  ? 147 ASP B OD2 1 
ATOM   3005 N N   . VAL B  1 133 ? 14.245 -0.581  102.138 1.00 36.96  ? 148 VAL B N   1 
ATOM   3006 C CA  . VAL B  1 133 ? 12.855 -0.365  102.640 1.00 38.44  ? 148 VAL B CA  1 
ATOM   3007 C C   . VAL B  1 133 ? 11.873 -1.234  101.840 1.00 40.38  ? 148 VAL B C   1 
ATOM   3008 O O   . VAL B  1 133 ? 10.696 -1.317  102.250 1.00 38.65  ? 148 VAL B O   1 
ATOM   3009 C CB  . VAL B  1 133 ? 12.464 1.125   102.638 1.00 39.22  ? 148 VAL B CB  1 
ATOM   3010 C CG1 . VAL B  1 133 ? 13.383 1.930   103.549 1.00 40.15  ? 148 VAL B CG1 1 
ATOM   3011 C CG2 . VAL B  1 133 ? 12.428 1.740   101.246 1.00 39.38  ? 148 VAL B CG2 1 
ATOM   3012 N N   . ASP B  1 134 ? 12.337 -1.842  100.742 1.00 42.44  ? 149 ASP B N   1 
ATOM   3013 C CA  . ASP B  1 134 ? 11.585 -2.844  99.937  1.00 43.40  ? 149 ASP B CA  1 
ATOM   3014 C C   . ASP B  1 134 ? 12.574 -3.564  99.014  1.00 42.69  ? 149 ASP B C   1 
ATOM   3015 O O   . ASP B  1 134 ? 13.768 -3.198  99.034  1.00 42.70  ? 149 ASP B O   1 
ATOM   3016 C CB  . ASP B  1 134 ? 10.458 -2.177  99.142  1.00 44.78  ? 149 ASP B CB  1 
ATOM   3017 C CG  . ASP B  1 134 ? 9.194  -3.015  99.055  1.00 48.62  ? 149 ASP B CG  1 
ATOM   3018 O OD1 . ASP B  1 134 ? 9.307  -4.248  98.921  1.00 52.31  ? 149 ASP B OD1 1 
ATOM   3019 O OD2 . ASP B  1 134 ? 8.106  -2.431  99.149  1.00 56.40  ? 149 ASP B OD2 1 
ATOM   3020 N N   . ASN B  1 135 ? 12.104 -4.528  98.218  1.00 43.06  ? 150 ASN B N   1 
ATOM   3021 C CA  . ASN B  1 135 ? 12.949 -5.237  97.214  1.00 44.33  ? 150 ASN B CA  1 
ATOM   3022 C C   . ASN B  1 135 ? 13.549 -4.203  96.250  1.00 43.63  ? 150 ASN B C   1 
ATOM   3023 O O   . ASN B  1 135 ? 12.773 -3.427  95.658  1.00 41.71  ? 150 ASN B O   1 
ATOM   3024 C CB  . ASN B  1 135 ? 12.169 -6.318  96.466  1.00 43.11  ? 150 ASN B CB  1 
ATOM   3025 C CG  . ASN B  1 135 ? 11.725 -7.440  97.379  1.00 44.49  ? 150 ASN B CG  1 
ATOM   3026 O OD1 . ASN B  1 135 ? 12.539 -8.253  97.815  1.00 44.05  ? 150 ASN B OD1 1 
ATOM   3027 N ND2 . ASN B  1 135 ? 10.437 -7.502  97.669  1.00 45.23  ? 150 ASN B ND2 1 
ATOM   3028 N N   . ASP B  1 136 ? 14.883 -4.149  96.168  1.00 46.43  ? 151 ASP B N   1 
ATOM   3029 C CA  . ASP B  1 136 ? 15.659 -3.259  95.259  1.00 50.33  ? 151 ASP B CA  1 
ATOM   3030 C C   . ASP B  1 136 ? 15.317 -1.781  95.518  1.00 48.71  ? 151 ASP B C   1 
ATOM   3031 O O   . ASP B  1 136 ? 15.421 -0.998  94.569  1.00 50.26  ? 151 ASP B O   1 
ATOM   3032 C CB  . ASP B  1 136 ? 15.415 -3.636  93.792  1.00 53.07  ? 151 ASP B CB  1 
ATOM   3033 C CG  . ASP B  1 136 ? 15.623 -5.111  93.497  1.00 56.93  ? 151 ASP B CG  1 
ATOM   3034 O OD1 . ASP B  1 136 ? 16.748 -5.602  93.723  1.00 54.80  ? 151 ASP B OD1 1 
ATOM   3035 O OD2 . ASP B  1 136 ? 14.653 -5.762  93.054  1.00 64.90  ? 151 ASP B OD2 1 
ATOM   3036 N N   . GLU B  1 137 ? 14.954 -1.407  96.753  1.00 49.87  ? 152 GLU B N   1 
ATOM   3037 C CA  . GLU B  1 137 ? 14.582 -0.019  97.151  1.00 49.00  ? 152 GLU B CA  1 
ATOM   3038 C C   . GLU B  1 137 ? 15.443 0.399   98.350  1.00 45.06  ? 152 GLU B C   1 
ATOM   3039 O O   . GLU B  1 137 ? 15.111 0.011   99.487  1.00 44.84  ? 152 GLU B O   1 
ATOM   3040 C CB  . GLU B  1 137 ? 13.093 0.063   97.488  1.00 52.63  ? 152 GLU B CB  1 
ATOM   3041 C CG  . GLU B  1 137 ? 12.190 0.126   96.275  1.00 59.15  ? 152 GLU B CG  1 
ATOM   3042 C CD  . GLU B  1 137 ? 10.728 0.395   96.595  1.00 63.27  ? 152 GLU B CD  1 
ATOM   3043 O OE1 . GLU B  1 137 ? 10.453 1.121   97.585  1.00 62.75  ? 152 GLU B OE1 1 
ATOM   3044 O OE2 . GLU B  1 137 ? 9.862  -0.132  95.859  1.00 67.45  ? 152 GLU B OE2 1 
ATOM   3045 N N   . ARG B  1 138 ? 16.517 1.148   98.104  1.00 42.30  ? 153 ARG B N   1 
ATOM   3046 C CA  . ARG B  1 138 ? 17.480 1.560   99.155  1.00 42.08  ? 153 ARG B CA  1 
ATOM   3047 C C   . ARG B  1 138 ? 16.793 2.502   100.151 1.00 39.99  ? 153 ARG B C   1 
ATOM   3048 O O   . ARG B  1 138 ? 15.808 3.167   99.780  1.00 41.70  ? 153 ARG B O   1 
ATOM   3049 C CB  . ARG B  1 138 ? 18.734 2.169   98.524  1.00 45.71  ? 153 ARG B CB  1 
ATOM   3050 C CG  . ARG B  1 138 ? 19.616 1.140   97.825  1.00 47.60  ? 153 ARG B CG  1 
ATOM   3051 C CD  . ARG B  1 138 ? 21.094 1.486   97.841  1.00 48.97  ? 153 ARG B CD  1 
ATOM   3052 N NE  . ARG B  1 138 ? 21.930 0.450   97.257  0.00 48.86  ? 153 ARG B NE  1 
ATOM   3053 C CZ  . ARG B  1 138 ? 23.258 0.495   97.144  0.00 48.86  ? 153 ARG B CZ  1 
ATOM   3054 N NH1 . ARG B  1 138 ? 23.949 1.542   97.568  0.00 48.86  ? 153 ARG B NH1 1 
ATOM   3055 N NH2 . ARG B  1 138 ? 23.897 -0.523  96.598  0.00 48.84  ? 153 ARG B NH2 1 
ATOM   3056 N N   . LEU B  1 139 ? 17.262 2.492   101.398 1.00 38.75  ? 154 LEU B N   1 
ATOM   3057 C CA  . LEU B  1 139 ? 16.910 3.508   102.422 1.00 36.16  ? 154 LEU B CA  1 
ATOM   3058 C C   . LEU B  1 139 ? 17.350 4.871   101.886 1.00 35.81  ? 154 LEU B C   1 
ATOM   3059 O O   . LEU B  1 139 ? 18.528 5.055   101.591 1.00 36.85  ? 154 LEU B O   1 
ATOM   3060 C CB  . LEU B  1 139 ? 17.615 3.160   103.733 1.00 34.31  ? 154 LEU B CB  1 
ATOM   3061 C CG  . LEU B  1 139 ? 17.293 4.054   104.928 1.00 33.20  ? 154 LEU B CG  1 
ATOM   3062 C CD1 . LEU B  1 139 ? 15.858 3.876   105.396 1.00 32.87  ? 154 LEU B CD1 1 
ATOM   3063 C CD2 . LEU B  1 139 ? 18.268 3.776   106.054 1.00 35.43  ? 154 LEU B CD2 1 
ATOM   3064 N N   . PRO B  1 140 ? 16.440 5.857   101.719 1.00 33.81  ? 155 PRO B N   1 
ATOM   3065 C CA  . PRO B  1 140 ? 16.845 7.202   101.308 1.00 34.73  ? 155 PRO B CA  1 
ATOM   3066 C C   . PRO B  1 140 ? 17.667 7.954   102.354 1.00 34.01  ? 155 PRO B C   1 
ATOM   3067 O O   . PRO B  1 140 ? 17.555 7.682   103.551 1.00 35.26  ? 155 PRO B O   1 
ATOM   3068 C CB  . PRO B  1 140 ? 15.512 7.943   101.105 1.00 34.98  ? 155 PRO B CB  1 
ATOM   3069 C CG  . PRO B  1 140 ? 14.479 6.844   100.975 1.00 35.30  ? 155 PRO B CG  1 
ATOM   3070 C CD  . PRO B  1 140 ? 14.983 5.750   101.889 1.00 34.72  ? 155 PRO B CD  1 
ATOM   3071 N N   . PRO B  1 141 ? 18.511 8.934   101.951 1.00 34.54  ? 156 PRO B N   1 
ATOM   3072 C CA  . PRO B  1 141 ? 19.112 9.857   102.911 1.00 35.24  ? 156 PRO B CA  1 
ATOM   3073 C C   . PRO B  1 141 ? 18.006 10.609  103.649 1.00 36.31  ? 156 PRO B C   1 
ATOM   3074 O O   . PRO B  1 141 ? 16.944 10.832  103.075 1.00 37.81  ? 156 PRO B O   1 
ATOM   3075 C CB  . PRO B  1 141 ? 20.012 10.785  102.085 1.00 36.55  ? 156 PRO B CB  1 
ATOM   3076 C CG  . PRO B  1 141 ? 19.633 10.547  100.644 1.00 35.23  ? 156 PRO B CG  1 
ATOM   3077 C CD  . PRO B  1 141 ? 18.937 9.205   100.572 1.00 34.64  ? 156 PRO B CD  1 
ATOM   3078 N N   . PRO B  1 142 ? 18.185 11.022  104.930 1.00 35.72  ? 157 PRO B N   1 
ATOM   3079 C CA  . PRO B  1 142 ? 19.451 10.904  105.659 1.00 35.74  ? 157 PRO B CA  1 
ATOM   3080 C C   . PRO B  1 142 ? 19.687 9.579   106.411 1.00 36.49  ? 157 PRO B C   1 
ATOM   3081 O O   . PRO B  1 142 ? 20.402 9.582   107.405 1.00 35.60  ? 157 PRO B O   1 
ATOM   3082 C CB  . PRO B  1 142 ? 19.314 12.080  106.635 1.00 36.40  ? 157 PRO B CB  1 
ATOM   3083 C CG  . PRO B  1 142 ? 17.854 12.060  107.014 1.00 36.67  ? 157 PRO B CG  1 
ATOM   3084 C CD  . PRO B  1 142 ? 17.133 11.639  105.752 1.00 36.10  ? 157 PRO B CD  1 
ATOM   3085 N N   . PHE B  1 143 ? 19.093 8.477   105.944 1.00 36.71  ? 158 PHE B N   1 
ATOM   3086 C CA  . PHE B  1 143 ? 19.431 7.090   106.363 1.00 35.84  ? 158 PHE B CA  1 
ATOM   3087 C C   . PHE B  1 143 ? 19.121 6.882   107.843 1.00 34.66  ? 158 PHE B C   1 
ATOM   3088 O O   . PHE B  1 143 ? 20.009 6.571   108.637 1.00 33.44  ? 158 PHE B O   1 
ATOM   3089 C CB  . PHE B  1 143 ? 20.904 6.788   106.072 1.00 35.52  ? 158 PHE B CB  1 
ATOM   3090 C CG  . PHE B  1 143 ? 21.390 7.168   104.697 1.00 36.85  ? 158 PHE B CG  1 
ATOM   3091 C CD1 . PHE B  1 143 ? 20.938 6.501   103.566 1.00 38.21  ? 158 PHE B CD1 1 
ATOM   3092 C CD2 . PHE B  1 143 ? 22.334 8.174   104.536 1.00 38.91  ? 158 PHE B CD2 1 
ATOM   3093 C CE1 . PHE B  1 143 ? 21.409 6.840   102.307 1.00 37.06  ? 158 PHE B CE1 1 
ATOM   3094 C CE2 . PHE B  1 143 ? 22.799 8.516   103.275 1.00 38.75  ? 158 PHE B CE2 1 
ATOM   3095 C CZ  . PHE B  1 143 ? 22.335 7.848   102.162 1.00 38.90  ? 158 PHE B CZ  1 
ATOM   3096 N N   . PRO B  1 144 ? 17.849 7.036   108.275 1.00 36.28  ? 159 PRO B N   1 
ATOM   3097 C CA  . PRO B  1 144 ? 17.495 6.826   109.675 1.00 34.38  ? 159 PRO B CA  1 
ATOM   3098 C C   . PRO B  1 144 ? 17.525 5.329   110.008 1.00 33.79  ? 159 PRO B C   1 
ATOM   3099 O O   . PRO B  1 144 ? 17.149 4.526   109.166 1.00 33.79  ? 159 PRO B O   1 
ATOM   3100 C CB  . PRO B  1 144 ? 16.080 7.402   109.762 1.00 35.84  ? 159 PRO B CB  1 
ATOM   3101 C CG  . PRO B  1 144 ? 15.512 7.168   108.383 1.00 36.24  ? 159 PRO B CG  1 
ATOM   3102 C CD  . PRO B  1 144 ? 16.683 7.395   107.455 1.00 36.89  ? 159 PRO B CD  1 
ATOM   3103 N N   . LEU B  1 145 ? 17.985 4.984   111.208 1.00 33.34  ? 160 LEU B N   1 
ATOM   3104 C CA  . LEU B  1 145 ? 17.848 3.607   111.737 1.00 33.48  ? 160 LEU B CA  1 
ATOM   3105 C C   . LEU B  1 145 ? 16.348 3.295   111.827 1.00 31.80  ? 160 LEU B C   1 
ATOM   3106 O O   . LEU B  1 145 ? 15.612 4.092   112.430 1.00 31.51  ? 160 LEU B O   1 
ATOM   3107 C CB  . LEU B  1 145 ? 18.539 3.486   113.098 1.00 33.35  ? 160 LEU B CB  1 
ATOM   3108 C CG  . LEU B  1 145 ? 18.411 2.126   113.785 1.00 33.60  ? 160 LEU B CG  1 
ATOM   3109 C CD1 . LEU B  1 145 ? 19.041 1.024   112.951 1.00 33.30  ? 160 LEU B CD1 1 
ATOM   3110 C CD2 . LEU B  1 145 ? 19.029 2.164   115.173 1.00 34.20  ? 160 LEU B CD2 1 
ATOM   3111 N N   . LYS B  1 146 ? 15.911 2.208   111.195 1.00 33.74  ? 161 LYS B N   1 
ATOM   3112 C CA  . LYS B  1 146 ? 14.499 1.759   111.190 1.00 33.26  ? 161 LYS B CA  1 
ATOM   3113 C C   . LYS B  1 146 ? 14.352 0.537   112.107 1.00 34.95  ? 161 LYS B C   1 
ATOM   3114 O O   . LYS B  1 146 ? 15.352 -0.181  112.352 1.00 30.66  ? 161 LYS B O   1 
ATOM   3115 C CB  . LYS B  1 146 ? 14.054 1.451   109.759 1.00 34.11  ? 161 LYS B CB  1 
ATOM   3116 C CG  . LYS B  1 146 ? 13.850 2.662   108.864 1.00 36.02  ? 161 LYS B CG  1 
ATOM   3117 C CD  . LYS B  1 146 ? 13.155 2.311   107.551 1.00 37.35  ? 161 LYS B CD  1 
ATOM   3118 C CE  . LYS B  1 146 ? 11.654 2.096   107.658 1.00 40.67  ? 161 LYS B CE  1 
ATOM   3119 N NZ  . LYS B  1 146 ? 11.137 1.120   106.653 1.00 39.68  ? 161 LYS B NZ  1 
ATOM   3120 N N   . GLN B  1 147 ? 13.125 0.340   112.583 1.00 33.20  ? 162 GLN B N   1 
ATOM   3121 C CA  . GLN B  1 147 ? 12.687 -0.777  113.445 1.00 33.85  ? 162 GLN B CA  1 
ATOM   3122 C C   . GLN B  1 147 ? 11.389 -1.327  112.850 1.00 33.52  ? 162 GLN B C   1 
ATOM   3123 O O   . GLN B  1 147 ? 10.654 -0.540  112.223 1.00 33.86  ? 162 GLN B O   1 
ATOM   3124 C CB  . GLN B  1 147 ? 12.464 -0.279  114.873 1.00 35.48  ? 162 GLN B CB  1 
ATOM   3125 C CG  . GLN B  1 147 ? 11.441 0.853   114.987 1.00 37.33  ? 162 GLN B CG  1 
ATOM   3126 C CD  . GLN B  1 147 ? 11.194 1.283   116.411 1.00 38.27  ? 162 GLN B CD  1 
ATOM   3127 O OE1 . GLN B  1 147 ? 12.121 1.466   117.187 1.00 37.21  ? 162 GLN B OE1 1 
ATOM   3128 N NE2 . GLN B  1 147 ? 9.933  1.466   116.771 1.00 40.66  ? 162 GLN B NE2 1 
ATOM   3129 N N   . VAL B  1 148 ? 11.113 -2.613  113.026 1.00 32.15  ? 163 VAL B N   1 
ATOM   3130 C CA  . VAL B  1 148 ? 9.770  -3.183  112.716 1.00 34.15  ? 163 VAL B CA  1 
ATOM   3131 C C   . VAL B  1 148 ? 9.508  -4.352  113.669 1.00 34.41  ? 163 VAL B C   1 
ATOM   3132 O O   . VAL B  1 148 ? 10.443 -5.130  113.944 1.00 32.64  ? 163 VAL B O   1 
ATOM   3133 C CB  . VAL B  1 148 ? 9.642  -3.559  111.224 1.00 33.70  ? 163 VAL B CB  1 
ATOM   3134 C CG1 . VAL B  1 148 ? 10.561 -4.700  110.813 1.00 32.32  ? 163 VAL B CG1 1 
ATOM   3135 C CG2 . VAL B  1 148 ? 8.197  -3.855  110.847 1.00 35.08  ? 163 VAL B CG2 1 
ATOM   3136 N N   . LYS B  1 149 ? 8.283  -4.423  114.190 1.00 35.19  ? 164 LYS B N   1 
ATOM   3137 C CA  . LYS B  1 149 ? 7.788  -5.559  115.000 1.00 37.34  ? 164 LYS B CA  1 
ATOM   3138 C C   . LYS B  1 149 ? 7.453  -6.697  114.032 1.00 35.75  ? 164 LYS B C   1 
ATOM   3139 O O   . LYS B  1 149 ? 6.691  -6.446  113.082 1.00 35.72  ? 164 LYS B O   1 
ATOM   3140 C CB  . LYS B  1 149 ? 6.572  -5.132  115.824 1.00 41.46  ? 164 LYS B CB  1 
ATOM   3141 C CG  . LYS B  1 149 ? 6.145  -6.127  116.896 1.00 43.70  ? 164 LYS B CG  1 
ATOM   3142 C CD  . LYS B  1 149 ? 4.925  -5.677  117.667 1.00 47.79  ? 164 LYS B CD  1 
ATOM   3143 C CE  . LYS B  1 149 ? 4.556  -6.636  118.776 1.00 53.49  ? 164 LYS B CE  1 
ATOM   3144 N NZ  . LYS B  1 149 ? 3.267  -6.266  119.409 1.00 59.55  ? 164 LYS B NZ  1 
ATOM   3145 N N   . VAL B  1 150 ? 8.073  -7.865  114.207 1.00 36.18  ? 165 VAL B N   1 
ATOM   3146 C CA  . VAL B  1 150 ? 7.873  -9.034  113.298 1.00 37.69  ? 165 VAL B CA  1 
ATOM   3147 C C   . VAL B  1 150 ? 7.275  -10.166 114.121 1.00 39.44  ? 165 VAL B C   1 
ATOM   3148 O O   . VAL B  1 150 ? 7.765  -10.453 115.219 1.00 38.56  ? 165 VAL B O   1 
ATOM   3149 C CB  . VAL B  1 150 ? 9.159  -9.458  112.560 1.00 36.99  ? 165 VAL B CB  1 
ATOM   3150 C CG1 . VAL B  1 150 ? 9.485  -8.475  111.450 1.00 37.82  ? 165 VAL B CG1 1 
ATOM   3151 C CG2 . VAL B  1 150 ? 10.348 -9.655  113.484 1.00 37.39  ? 165 VAL B CG2 1 
ATOM   3152 N N   . PRO B  1 151 ? 6.205  -10.834 113.620 1.00 39.55  ? 166 PRO B N   1 
ATOM   3153 C CA  . PRO B  1 151 ? 5.654  -12.004 114.294 1.00 41.69  ? 166 PRO B CA  1 
ATOM   3154 C C   . PRO B  1 151 ? 6.591  -13.201 114.074 1.00 41.97  ? 166 PRO B C   1 
ATOM   3155 O O   . PRO B  1 151 ? 6.878  -13.515 112.936 1.00 42.44  ? 166 PRO B O   1 
ATOM   3156 C CB  . PRO B  1 151 ? 4.289  -12.200 113.616 1.00 40.26  ? 166 PRO B CB  1 
ATOM   3157 C CG  . PRO B  1 151 ? 4.495  -11.663 112.215 1.00 41.39  ? 166 PRO B CG  1 
ATOM   3158 C CD  . PRO B  1 151 ? 5.477  -10.519 112.379 1.00 41.71  ? 166 PRO B CD  1 
ATOM   3159 N N   . ILE B  1 152 ? 7.073  -13.800 115.160 1.00 42.97  ? 167 ILE B N   1 
ATOM   3160 C CA  . ILE B  1 152 ? 7.797  -15.103 115.113 1.00 46.29  ? 167 ILE B CA  1 
ATOM   3161 C C   . ILE B  1 152 ? 6.802  -16.168 114.640 1.00 48.06  ? 167 ILE B C   1 
ATOM   3162 O O   . ILE B  1 152 ? 5.616  -16.114 115.050 1.00 48.74  ? 167 ILE B O   1 
ATOM   3163 C CB  . ILE B  1 152 ? 8.447  -15.444 116.469 1.00 47.21  ? 167 ILE B CB  1 
ATOM   3164 C CG1 . ILE B  1 152 ? 9.749  -14.664 116.682 1.00 49.29  ? 167 ILE B CG1 1 
ATOM   3165 C CG2 . ILE B  1 152 ? 8.667  -16.943 116.614 1.00 48.00  ? 167 ILE B CG2 1 
ATOM   3166 C CD1 . ILE B  1 152 ? 10.654 -15.075 117.777 0.00 48.71  ? 167 ILE B CD1 1 
ATOM   3167 N N   . MET B  1 153 ? 7.262  -17.086 113.789 1.00 48.67  ? 168 MET B N   1 
ATOM   3168 C CA  . MET B  1 153 ? 6.482  -18.281 113.378 1.00 52.29  ? 168 MET B CA  1 
ATOM   3169 C C   . MET B  1 153 ? 7.303  -19.538 113.672 1.00 48.48  ? 168 MET B C   1 
ATOM   3170 O O   . MET B  1 153 ? 8.538  -19.454 113.599 1.00 50.64  ? 168 MET B O   1 
ATOM   3171 C CB  . MET B  1 153 ? 6.120  -18.185 111.898 1.00 58.11  ? 168 MET B CB  1 
ATOM   3172 C CG  . MET B  1 153 ? 5.056  -17.146 111.637 1.00 64.86  ? 168 MET B CG  1 
ATOM   3173 S SD  . MET B  1 153 ? 5.005  -16.652 109.902 1.00 80.93  ? 168 MET B SD  1 
ATOM   3174 C CE  . MET B  1 153 ? 4.714  -18.234 109.111 1.00 72.87  ? 168 MET B CE  1 
ATOM   3175 N N   . GLU B  1 154 ? 6.632  -20.639 114.031 1.00 46.89  ? 169 GLU B N   1 
ATOM   3176 C CA  . GLU B  1 154 ? 7.261  -21.948 114.362 1.00 45.02  ? 169 GLU B CA  1 
ATOM   3177 C C   . GLU B  1 154 ? 8.074  -22.440 113.154 1.00 38.96  ? 169 GLU B C   1 
ATOM   3178 O O   . GLU B  1 154 ? 7.628  -22.218 112.015 1.00 36.47  ? 169 GLU B O   1 
ATOM   3179 C CB  . GLU B  1 154 ? 6.187  -22.965 114.755 1.00 52.71  ? 169 GLU B CB  1 
ATOM   3180 C CG  . GLU B  1 154 ? 6.596  -23.871 115.903 1.00 59.42  ? 169 GLU B CG  1 
ATOM   3181 C CD  . GLU B  1 154 ? 5.472  -24.681 116.539 1.00 64.21  ? 169 GLU B CD  1 
ATOM   3182 O OE1 . GLU B  1 154 ? 4.376  -24.118 116.773 1.00 70.42  ? 169 GLU B OE1 1 
ATOM   3183 O OE2 . GLU B  1 154 ? 5.697  -25.880 116.814 1.00 69.35  ? 169 GLU B OE2 1 
ATOM   3184 N N   . ASN B  1 155 ? 9.231  -23.068 113.393 1.00 36.69  ? 170 ASN B N   1 
ATOM   3185 C CA  . ASN B  1 155 ? 10.162 -23.544 112.333 1.00 36.57  ? 170 ASN B CA  1 
ATOM   3186 C C   . ASN B  1 155 ? 9.416  -24.483 111.369 1.00 37.72  ? 170 ASN B C   1 
ATOM   3187 O O   . ASN B  1 155 ? 9.619  -24.340 110.152 1.00 36.07  ? 170 ASN B O   1 
ATOM   3188 C CB  . ASN B  1 155 ? 11.403 -24.238 112.902 1.00 36.50  ? 170 ASN B CB  1 
ATOM   3189 C CG  . ASN B  1 155 ? 12.558 -23.295 113.192 1.00 37.24  ? 170 ASN B CG  1 
ATOM   3190 O OD1 . ASN B  1 155 ? 12.354 -22.140 113.555 1.00 37.01  ? 170 ASN B OD1 1 
ATOM   3191 N ND2 . ASN B  1 155 ? 13.781 -23.773 113.030 1.00 38.95  ? 170 ASN B ND2 1 
ATOM   3192 N N   . HIS B  1 156 ? 8.577  -25.393 111.877 1.00 38.91  ? 171 HIS B N   1 
ATOM   3193 C CA  . HIS B  1 156 ? 7.845  -26.388 111.037 1.00 42.00  ? 171 HIS B CA  1 
ATOM   3194 C C   . HIS B  1 156 ? 6.860  -25.667 110.097 1.00 38.97  ? 171 HIS B C   1 
ATOM   3195 O O   . HIS B  1 156 ? 6.756  -26.083 108.934 1.00 39.06  ? 171 HIS B O   1 
ATOM   3196 C CB  . HIS B  1 156 ? 7.233  -27.519 111.882 1.00 44.17  ? 171 HIS B CB  1 
ATOM   3197 C CG  . HIS B  1 156 ? 5.919  -27.214 112.511 1.00 49.73  ? 171 HIS B CG  1 
ATOM   3198 N ND1 . HIS B  1 156 ? 4.712  -27.523 111.908 1.00 54.83  ? 171 HIS B ND1 1 
ATOM   3199 C CD2 . HIS B  1 156 ? 5.620  -26.646 113.695 1.00 52.72  ? 171 HIS B CD2 1 
ATOM   3200 C CE1 . HIS B  1 156 ? 3.722  -27.149 112.699 1.00 55.38  ? 171 HIS B CE1 1 
ATOM   3201 N NE2 . HIS B  1 156 ? 4.253  -26.608 113.804 1.00 54.46  ? 171 HIS B NE2 1 
ATOM   3202 N N   . ILE B  1 157 ? 6.178  -24.620 110.570 1.00 40.12  ? 172 ILE B N   1 
ATOM   3203 C CA  . ILE B  1 157 ? 5.214  -23.798 109.764 1.00 40.03  ? 172 ILE B CA  1 
ATOM   3204 C C   . ILE B  1 157 ? 5.974  -23.066 108.649 1.00 38.07  ? 172 ILE B C   1 
ATOM   3205 O O   . ILE B  1 157 ? 5.484  -23.024 107.504 1.00 36.70  ? 172 ILE B O   1 
ATOM   3206 C CB  . ILE B  1 157 ? 4.442  -22.797 110.654 1.00 40.25  ? 172 ILE B CB  1 
ATOM   3207 C CG1 . ILE B  1 157 ? 3.582  -23.496 111.715 1.00 42.57  ? 172 ILE B CG1 1 
ATOM   3208 C CG2 . ILE B  1 157 ? 3.624  -21.822 109.811 1.00 40.38  ? 172 ILE B CG2 1 
ATOM   3209 C CD1 . ILE B  1 157 ? 2.542  -24.446 111.161 1.00 43.68  ? 172 ILE B CD1 1 
ATOM   3210 N N   . CYS B  1 158 ? 7.113  -22.475 108.997 1.00 37.92  ? 173 CYS B N   1 
ATOM   3211 C CA  A CYS B  1 158 ? 7.971  -21.689 108.075 0.50 36.98  ? 173 CYS B CA  1 
ATOM   3212 C CA  B CYS B  1 158 ? 7.954  -21.687 108.056 0.50 39.10  ? 173 CYS B CA  1 
ATOM   3213 C C   . CYS B  1 158 ? 8.592  -22.617 107.020 1.00 36.15  ? 173 CYS B C   1 
ATOM   3214 O O   . CYS B  1 158 ? 8.630  -22.218 105.849 1.00 35.22  ? 173 CYS B O   1 
ATOM   3215 C CB  A CYS B  1 158 ? 9.023  -20.950 108.891 0.50 36.26  ? 173 CYS B CB  1 
ATOM   3216 C CB  B CYS B  1 158 ? 8.994  -20.856 108.794 0.50 40.94  ? 173 CYS B CB  1 
ATOM   3217 S SG  A CYS B  1 158 ? 10.190 -19.974 107.916 0.50 36.93  ? 173 CYS B SG  1 
ATOM   3218 S SG  B CYS B  1 158 ? 8.248  -19.357 109.479 0.50 46.97  ? 173 CYS B SG  1 
ATOM   3219 N N   . ASP B  1 159 ? 9.041  -23.805 107.438 1.00 36.25  ? 174 ASP B N   1 
ATOM   3220 C CA  . ASP B  1 159 ? 9.558  -24.861 106.527 1.00 35.36  ? 174 ASP B CA  1 
ATOM   3221 C C   . ASP B  1 159 ? 8.473  -25.214 105.503 1.00 35.27  ? 174 ASP B C   1 
ATOM   3222 O O   . ASP B  1 159 ? 8.794  -25.223 104.299 1.00 31.71  ? 174 ASP B O   1 
ATOM   3223 C CB  . ASP B  1 159 ? 10.016 -26.110 107.282 1.00 36.73  ? 174 ASP B CB  1 
ATOM   3224 C CG  . ASP B  1 159 ? 10.792 -27.084 106.411 1.00 37.36  ? 174 ASP B CG  1 
ATOM   3225 O OD1 . ASP B  1 159 ? 11.743 -26.639 105.728 1.00 37.29  ? 174 ASP B OD1 1 
ATOM   3226 O OD2 . ASP B  1 159 ? 10.424 -28.274 106.394 1.00 38.71  ? 174 ASP B OD2 1 
ATOM   3227 N N   . ALA B  1 160 ? 7.235  -25.448 105.957 1.00 34.96  ? 175 ALA B N   1 
ATOM   3228 C CA  . ALA B  1 160 ? 6.084  -25.787 105.080 1.00 35.27  ? 175 ALA B CA  1 
ATOM   3229 C C   . ALA B  1 160 ? 5.819  -24.642 104.083 1.00 35.49  ? 175 ALA B C   1 
ATOM   3230 O O   . ALA B  1 160 ? 5.591  -24.938 102.900 1.00 35.18  ? 175 ALA B O   1 
ATOM   3231 C CB  . ALA B  1 160 ? 4.857  -26.106 105.901 1.00 34.61  ? 175 ALA B CB  1 
ATOM   3232 N N   . LYS B  1 161 ? 5.876  -23.382 104.523 1.00 36.73  ? 176 LYS B N   1 
ATOM   3233 C CA  . LYS B  1 161 ? 5.635  -22.207 103.632 1.00 37.93  ? 176 LYS B CA  1 
ATOM   3234 C C   . LYS B  1 161 ? 6.714  -22.132 102.538 1.00 35.32  ? 176 LYS B C   1 
ATOM   3235 O O   . LYS B  1 161 ? 6.354  -21.886 101.388 1.00 34.67  ? 176 LYS B O   1 
ATOM   3236 C CB  . LYS B  1 161 ? 5.523  -20.911 104.437 1.00 39.51  ? 176 LYS B CB  1 
ATOM   3237 C CG  . LYS B  1 161 ? 4.211  -20.764 105.201 1.00 41.53  ? 176 LYS B CG  1 
ATOM   3238 C CD  . LYS B  1 161 ? 3.938  -19.363 105.691 1.00 46.16  ? 176 LYS B CD  1 
ATOM   3239 C CE  . LYS B  1 161 ? 2.677  -19.265 106.526 1.00 47.98  ? 176 LYS B CE  1 
ATOM   3240 N NZ  . LYS B  1 161 ? 2.187  -17.860 106.615 0.00 47.36  ? 176 LYS B NZ  1 
ATOM   3241 N N   . TYR B  1 162 ? 7.978  -22.405 102.861 1.00 34.52  ? 177 TYR B N   1 
ATOM   3242 C CA  . TYR B  1 162 ? 9.108  -22.370 101.892 1.00 34.55  ? 177 TYR B CA  1 
ATOM   3243 C C   . TYR B  1 162 ? 8.947  -23.463 100.824 1.00 34.72  ? 177 TYR B C   1 
ATOM   3244 O O   . TYR B  1 162 ? 9.520  -23.282 99.733  1.00 34.02  ? 177 TYR B O   1 
ATOM   3245 C CB  . TYR B  1 162 ? 10.464 -22.415 102.605 1.00 34.54  ? 177 TYR B CB  1 
ATOM   3246 C CG  . TYR B  1 162 ? 11.041 -21.036 102.784 1.00 33.51  ? 177 TYR B CG  1 
ATOM   3247 C CD1 . TYR B  1 162 ? 10.605 -20.201 103.803 1.00 33.53  ? 177 TYR B CD1 1 
ATOM   3248 C CD2 . TYR B  1 162 ? 11.954 -20.524 101.875 1.00 33.70  ? 177 TYR B CD2 1 
ATOM   3249 C CE1 . TYR B  1 162 ? 11.093 -18.909 103.943 1.00 33.04  ? 177 TYR B CE1 1 
ATOM   3250 C CE2 . TYR B  1 162 ? 12.443 -19.230 101.995 1.00 34.92  ? 177 TYR B CE2 1 
ATOM   3251 C CZ  . TYR B  1 162 ? 12.021 -18.420 103.038 1.00 33.65  ? 177 TYR B CZ  1 
ATOM   3252 O OH  . TYR B  1 162 ? 12.513 -17.146 103.156 1.00 33.70  ? 177 TYR B OH  1 
ATOM   3253 N N   . HIS B  1 163 ? 8.185  -24.527 101.110 1.00 34.06  ? 178 HIS B N   1 
ATOM   3254 C CA  . HIS B  1 163 ? 7.879  -25.638 100.167 1.00 34.23  ? 178 HIS B CA  1 
ATOM   3255 C C   . HIS B  1 163 ? 6.709  -25.288 99.230  1.00 33.07  ? 178 HIS B C   1 
ATOM   3256 O O   . HIS B  1 163 ? 6.627  -25.917 98.163  1.00 33.41  ? 178 HIS B O   1 
ATOM   3257 C CB  . HIS B  1 163 ? 7.631  -26.938 100.939 1.00 33.21  ? 178 HIS B CB  1 
ATOM   3258 C CG  . HIS B  1 163 ? 8.881  -27.574 101.440 1.00 33.45  ? 178 HIS B CG  1 
ATOM   3259 N ND1 . HIS B  1 163 ? 9.448  -27.240 102.651 1.00 34.12  ? 178 HIS B ND1 1 
ATOM   3260 C CD2 . HIS B  1 163 ? 9.669  -28.530 100.906 1.00 34.66  ? 178 HIS B CD2 1 
ATOM   3261 C CE1 . HIS B  1 163 ? 10.532 -27.972 102.841 1.00 33.37  ? 178 HIS B CE1 1 
ATOM   3262 N NE2 . HIS B  1 163 ? 10.687 -28.767 101.791 1.00 34.24  ? 178 HIS B NE2 1 
ATOM   3263 N N   . LEU B  1 164 ? 5.823  -24.361 99.608  1.00 34.28  ? 179 LEU B N   1 
ATOM   3264 C CA  . LEU B  1 164 ? 4.698  -23.902 98.748  1.00 35.07  ? 179 LEU B CA  1 
ATOM   3265 C C   . LEU B  1 164 ? 5.274  -23.151 97.539  1.00 36.04  ? 179 LEU B C   1 
ATOM   3266 O O   . LEU B  1 164 ? 6.073  -22.212 97.747  1.00 33.19  ? 179 LEU B O   1 
ATOM   3267 C CB  . LEU B  1 164 ? 3.749  -23.004 99.548  1.00 37.00  ? 179 LEU B CB  1 
ATOM   3268 C CG  . LEU B  1 164 ? 2.973  -23.669 100.686 1.00 40.89  ? 179 LEU B CG  1 
ATOM   3269 C CD1 . LEU B  1 164 ? 2.244  -22.623 101.519 1.00 42.38  ? 179 LEU B CD1 1 
ATOM   3270 C CD2 . LEU B  1 164 ? 1.981  -24.704 100.161 1.00 40.07  ? 179 LEU B CD2 1 
ATOM   3271 N N   . GLY B  1 165 ? 4.896  -23.564 96.325  1.00 35.83  ? 180 GLY B N   1 
ATOM   3272 C CA  . GLY B  1 165 ? 5.392  -22.990 95.060  1.00 36.05  ? 180 GLY B CA  1 
ATOM   3273 C C   . GLY B  1 165 ? 6.838  -23.370 94.789  1.00 35.01  ? 180 GLY B C   1 
ATOM   3274 O O   . GLY B  1 165 ? 7.503  -22.632 94.027  1.00 34.87  ? 180 GLY B O   1 
ATOM   3275 N N   . ALA B  1 166 ? 7.307  -24.488 95.355  1.00 32.67  ? 181 ALA B N   1 
ATOM   3276 C CA  . ALA B  1 166 ? 8.681  -25.010 95.175  1.00 33.96  ? 181 ALA B CA  1 
ATOM   3277 C C   . ALA B  1 166 ? 8.628  -26.468 94.721  1.00 34.43  ? 181 ALA B C   1 
ATOM   3278 O O   . ALA B  1 166 ? 7.675  -27.178 95.079  1.00 35.90  ? 181 ALA B O   1 
ATOM   3279 C CB  . ALA B  1 166 ? 9.474  -24.860 96.448  1.00 34.96  ? 181 ALA B CB  1 
ATOM   3280 N N   . TYR B  1 167 ? 9.648  -26.893 93.976  1.00 34.72  ? 182 TYR B N   1 
ATOM   3281 C CA  . TYR B  1 167 ? 9.844  -28.292 93.522  1.00 35.73  ? 182 TYR B CA  1 
ATOM   3282 C C   . TYR B  1 167 ? 10.415 -29.154 94.657  1.00 34.78  ? 182 TYR B C   1 
ATOM   3283 O O   . TYR B  1 167 ? 10.292 -30.382 94.568  1.00 34.17  ? 182 TYR B O   1 
ATOM   3284 C CB  . TYR B  1 167 ? 10.770 -28.333 92.302  1.00 35.87  ? 182 TYR B CB  1 
ATOM   3285 C CG  . TYR B  1 167 ? 10.234 -27.671 91.056  1.00 36.57  ? 182 TYR B CG  1 
ATOM   3286 C CD1 . TYR B  1 167 ? 9.162  -28.213 90.365  1.00 37.83  ? 182 TYR B CD1 1 
ATOM   3287 C CD2 . TYR B  1 167 ? 10.834 -26.537 90.527  1.00 35.76  ? 182 TYR B CD2 1 
ATOM   3288 C CE1 . TYR B  1 167 ? 8.683  -27.638 89.197  1.00 37.35  ? 182 TYR B CE1 1 
ATOM   3289 C CE2 . TYR B  1 167 ? 10.374 -25.954 89.357  1.00 36.40  ? 182 TYR B CE2 1 
ATOM   3290 C CZ  . TYR B  1 167 ? 9.292  -26.504 88.690  1.00 36.99  ? 182 TYR B CZ  1 
ATOM   3291 O OH  . TYR B  1 167 ? 8.809  -25.918 87.557  1.00 35.11  ? 182 TYR B OH  1 
ATOM   3292 N N   . THR B  1 168 ? 11.067 -28.543 95.653  1.00 34.16  ? 183 THR B N   1 
ATOM   3293 C CA  . THR B  1 168 ? 11.780 -29.247 96.754  1.00 32.80  ? 183 THR B CA  1 
ATOM   3294 C C   . THR B  1 168 ? 10.785 -30.179 97.455  1.00 34.54  ? 183 THR B C   1 
ATOM   3295 O O   . THR B  1 168 ? 9.659  -29.712 97.768  1.00 33.43  ? 183 THR B O   1 
ATOM   3296 C CB  . THR B  1 168 ? 12.421 -28.251 97.731  1.00 34.05  ? 183 THR B CB  1 
ATOM   3297 O OG1 . THR B  1 168 ? 13.156 -27.281 96.981  1.00 33.92  ? 183 THR B OG1 1 
ATOM   3298 C CG2 . THR B  1 168 ? 13.356 -28.900 98.730  1.00 32.61  ? 183 THR B CG2 1 
ATOM   3299 N N   . GLY B  1 169 ? 11.170 -31.444 97.653  1.00 34.67  ? 184 GLY B N   1 
ATOM   3300 C CA  . GLY B  1 169 ? 10.364 -32.465 98.348  1.00 35.20  ? 184 GLY B CA  1 
ATOM   3301 C C   . GLY B  1 169 ? 10.015 -32.018 99.757  1.00 34.91  ? 184 GLY B C   1 
ATOM   3302 O O   . GLY B  1 169 ? 10.892 -31.426 100.426 1.00 35.30  ? 184 GLY B O   1 
ATOM   3303 N N   . ASP B  1 170 ? 8.784  -32.297 100.195 1.00 35.87  ? 185 ASP B N   1 
ATOM   3304 C CA  . ASP B  1 170 ? 8.217  -31.852 101.496 1.00 38.58  ? 185 ASP B CA  1 
ATOM   3305 C C   . ASP B  1 170 ? 9.076  -32.325 102.678 1.00 38.14  ? 185 ASP B C   1 
ATOM   3306 O O   . ASP B  1 170 ? 9.103  -31.593 103.684 1.00 35.67  ? 185 ASP B O   1 
ATOM   3307 C CB  . ASP B  1 170 ? 6.760  -32.310 101.645 1.00 39.69  ? 185 ASP B CB  1 
ATOM   3308 C CG  . ASP B  1 170 ? 5.778  -31.513 100.805 1.00 44.00  ? 185 ASP B CG  1 
ATOM   3309 O OD1 . ASP B  1 170 ? 6.127  -30.394 100.364 1.00 46.95  ? 185 ASP B OD1 1 
ATOM   3310 O OD2 . ASP B  1 170 ? 4.654  -32.002 100.620 1.00 52.13  ? 185 ASP B OD2 1 
ATOM   3311 N N   . ASP B  1 171 ? 9.734  -33.484 102.560 1.00 37.75  ? 186 ASP B N   1 
ATOM   3312 C CA  . ASP B  1 171 ? 10.557 -34.116 103.629 1.00 39.16  ? 186 ASP B CA  1 
ATOM   3313 C C   . ASP B  1 171 ? 12.018 -33.660 103.531 1.00 36.42  ? 186 ASP B C   1 
ATOM   3314 O O   . ASP B  1 171 ? 12.832 -34.151 104.333 1.00 35.33  ? 186 ASP B O   1 
ATOM   3315 C CB  . ASP B  1 171 ? 10.474 -35.646 103.560 1.00 42.42  ? 186 ASP B CB  1 
ATOM   3316 C CG  . ASP B  1 171 ? 9.082  -36.231 103.749 1.00 48.71  ? 186 ASP B CG  1 
ATOM   3317 O OD1 . ASP B  1 171 ? 8.092  -35.452 103.757 1.00 53.16  ? 186 ASP B OD1 1 
ATOM   3318 O OD2 . ASP B  1 171 ? 8.995  -37.468 103.903 1.00 57.88  ? 186 ASP B OD2 1 
ATOM   3319 N N   . VAL B  1 172 ? 12.356 -32.771 102.592 1.00 34.31  ? 187 VAL B N   1 
ATOM   3320 C CA  . VAL B  1 172 ? 13.713 -32.162 102.490 1.00 33.32  ? 187 VAL B CA  1 
ATOM   3321 C C   . VAL B  1 172 ? 13.653 -30.805 103.193 1.00 33.73  ? 187 VAL B C   1 
ATOM   3322 O O   . VAL B  1 172 ? 12.992 -29.895 102.660 1.00 35.97  ? 187 VAL B O   1 
ATOM   3323 C CB  . VAL B  1 172 ? 14.172 -32.067 101.027 1.00 33.91  ? 187 VAL B CB  1 
ATOM   3324 C CG1 . VAL B  1 172 ? 15.561 -31.438 100.907 1.00 32.86  ? 187 VAL B CG1 1 
ATOM   3325 C CG2 . VAL B  1 172 ? 14.151 -33.448 100.370 1.00 35.35  ? 187 VAL B CG2 1 
ATOM   3326 N N   . ARG B  1 173 ? 14.268 -30.696 104.373 1.00 33.88  ? 188 ARG B N   1 
ATOM   3327 C CA  . ARG B  1 173 ? 14.108 -29.511 105.248 1.00 34.20  ? 188 ARG B CA  1 
ATOM   3328 C C   . ARG B  1 173 ? 14.848 -28.334 104.605 1.00 32.72  ? 188 ARG B C   1 
ATOM   3329 O O   . ARG B  1 173 ? 16.011 -28.513 104.201 1.00 32.01  ? 188 ARG B O   1 
ATOM   3330 C CB  . ARG B  1 173 ? 14.589 -29.788 106.673 1.00 36.58  ? 188 ARG B CB  1 
ATOM   3331 C CG  . ARG B  1 173 ? 14.031 -28.788 107.674 1.00 39.05  ? 188 ARG B CG  1 
ATOM   3332 C CD  . ARG B  1 173 ? 14.064 -29.240 109.110 1.00 40.63  ? 188 ARG B CD  1 
ATOM   3333 N NE  . ARG B  1 173 ? 13.142 -30.345 109.356 1.00 42.19  ? 188 ARG B NE  1 
ATOM   3334 C CZ  . ARG B  1 173 ? 12.760 -30.772 110.565 1.00 40.30  ? 188 ARG B CZ  1 
ATOM   3335 N NH1 . ARG B  1 173 ? 13.226 -30.204 111.667 1.00 40.55  ? 188 ARG B NH1 1 
ATOM   3336 N NH2 . ARG B  1 173 ? 11.905 -31.775 110.666 1.00 40.20  ? 188 ARG B NH2 1 
ATOM   3337 N N   . ILE B  1 174 ? 14.176 -27.189 104.505 1.00 31.07  ? 189 ILE B N   1 
ATOM   3338 C CA  . ILE B  1 174 ? 14.741 -25.908 104.001 1.00 31.31  ? 189 ILE B CA  1 
ATOM   3339 C C   . ILE B  1 174 ? 15.114 -25.053 105.216 1.00 32.17  ? 189 ILE B C   1 
ATOM   3340 O O   . ILE B  1 174 ? 16.283 -24.622 105.298 1.00 32.60  ? 189 ILE B O   1 
ATOM   3341 C CB  . ILE B  1 174 ? 13.741 -25.218 103.048 1.00 31.23  ? 189 ILE B CB  1 
ATOM   3342 C CG1 . ILE B  1 174 ? 13.539 -26.035 101.767 1.00 31.06  ? 189 ILE B CG1 1 
ATOM   3343 C CG2 . ILE B  1 174 ? 14.184 -23.790 102.741 1.00 30.75  ? 189 ILE B CG2 1 
ATOM   3344 C CD1 . ILE B  1 174 ? 12.314 -25.656 100.966 1.00 31.27  ? 189 ILE B CD1 1 
ATOM   3345 N N   . VAL B  1 175 ? 14.150 -24.817 106.115 1.00 32.34  ? 190 VAL B N   1 
ATOM   3346 C CA  . VAL B  1 175 ? 14.344 -24.041 107.376 1.00 33.74  ? 190 VAL B CA  1 
ATOM   3347 C C   . VAL B  1 175 ? 14.882 -25.003 108.438 1.00 34.63  ? 190 VAL B C   1 
ATOM   3348 O O   . VAL B  1 175 ? 14.129 -25.882 108.876 1.00 36.02  ? 190 VAL B O   1 
ATOM   3349 C CB  . VAL B  1 175 ? 13.043 -23.350 107.825 1.00 33.21  ? 190 VAL B CB  1 
ATOM   3350 C CG1 . VAL B  1 175 ? 13.226 -22.555 109.113 1.00 34.51  ? 190 VAL B CG1 1 
ATOM   3351 C CG2 . VAL B  1 175 ? 12.501 -22.459 106.723 1.00 34.07  ? 190 VAL B CG2 1 
ATOM   3352 N N   . ARG B  1 176 ? 16.147 -24.830 108.828 1.00 34.67  ? 191 ARG B N   1 
ATOM   3353 C CA  . ARG B  1 176 ? 16.897 -25.811 109.646 1.00 36.27  ? 191 ARG B CA  1 
ATOM   3354 C C   . ARG B  1 176 ? 16.772 -25.446 111.124 1.00 35.45  ? 191 ARG B C   1 
ATOM   3355 O O   . ARG B  1 176 ? 16.217 -24.367 111.436 1.00 33.48  ? 191 ARG B O   1 
ATOM   3356 C CB  . ARG B  1 176 ? 18.326 -25.891 109.112 1.00 38.11  ? 191 ARG B CB  1 
ATOM   3357 C CG  . ARG B  1 176 ? 18.356 -26.349 107.664 1.00 40.97  ? 191 ARG B CG  1 
ATOM   3358 C CD  . ARG B  1 176 ? 19.698 -26.893 107.246 1.00 45.71  ? 191 ARG B CD  1 
ATOM   3359 N NE  . ARG B  1 176 ? 19.680 -27.332 105.858 1.00 47.78  ? 191 ARG B NE  1 
ATOM   3360 C CZ  . ARG B  1 176 ? 20.675 -27.959 105.234 1.00 51.71  ? 191 ARG B CZ  1 
ATOM   3361 N NH1 . ARG B  1 176 ? 21.802 -28.256 105.868 1.00 53.03  ? 191 ARG B NH1 1 
ATOM   3362 N NH2 . ARG B  1 176 ? 20.533 -28.298 103.963 1.00 53.67  ? 191 ARG B NH2 1 
ATOM   3363 N N   . ASP B  1 177 ? 17.235 -26.341 111.997 1.00 34.61  ? 192 ASP B N   1 
ATOM   3364 C CA  . ASP B  1 177 ? 16.977 -26.289 113.464 1.00 35.85  ? 192 ASP B CA  1 
ATOM   3365 C C   . ASP B  1 177 ? 17.813 -25.166 114.104 1.00 35.18  ? 192 ASP B C   1 
ATOM   3366 O O   . ASP B  1 177 ? 17.390 -24.648 115.150 1.00 34.63  ? 192 ASP B O   1 
ATOM   3367 C CB  . ASP B  1 177 ? 17.229 -27.647 114.132 1.00 38.32  ? 192 ASP B CB  1 
ATOM   3368 C CG  . ASP B  1 177 ? 16.439 -28.806 113.532 1.00 39.78  ? 192 ASP B CG  1 
ATOM   3369 O OD1 . ASP B  1 177 ? 15.471 -28.544 112.789 1.00 39.65  ? 192 ASP B OD1 1 
ATOM   3370 O OD2 . ASP B  1 177 ? 16.815 -29.964 113.792 1.00 41.89  ? 192 ASP B OD2 1 
ATOM   3371 N N   . ASP B  1 178 ? 18.922 -24.766 113.474 1.00 35.30  ? 193 ASP B N   1 
ATOM   3372 C CA  . ASP B  1 178 ? 19.781 -23.634 113.914 1.00 35.52  ? 193 ASP B CA  1 
ATOM   3373 C C   . ASP B  1 178 ? 19.248 -22.303 113.354 1.00 34.48  ? 193 ASP B C   1 
ATOM   3374 O O   . ASP B  1 178 ? 19.990 -21.301 113.429 1.00 33.40  ? 193 ASP B O   1 
ATOM   3375 C CB  . ASP B  1 178 ? 21.236 -23.872 113.500 1.00 35.45  ? 193 ASP B CB  1 
ATOM   3376 C CG  . ASP B  1 178 ? 21.490 -23.825 112.001 1.00 37.49  ? 193 ASP B CG  1 
ATOM   3377 O OD1 . ASP B  1 178 ? 20.581 -24.205 111.240 1.00 36.62  ? 193 ASP B OD1 1 
ATOM   3378 O OD2 . ASP B  1 178 ? 22.581 -23.374 111.611 1.00 40.27  ? 193 ASP B OD2 1 
ATOM   3379 N N   . MET B  1 179 ? 18.035 -22.279 112.787 1.00 34.23  ? 194 MET B N   1 
ATOM   3380 C CA  . MET B  1 179 ? 17.424 -21.065 112.197 1.00 34.67  ? 194 MET B CA  1 
ATOM   3381 C C   . MET B  1 179 ? 16.100 -20.752 112.901 1.00 35.33  ? 194 MET B C   1 
ATOM   3382 O O   . MET B  1 179 ? 15.504 -21.655 113.539 1.00 34.45  ? 194 MET B O   1 
ATOM   3383 C CB  . MET B  1 179 ? 17.185 -21.233 110.695 1.00 33.18  ? 194 MET B CB  1 
ATOM   3384 C CG  . MET B  1 179 ? 18.453 -21.460 109.909 1.00 32.35  ? 194 MET B CG  1 
ATOM   3385 S SD  . MET B  1 179 ? 18.091 -21.916 108.206 1.00 32.74  ? 194 MET B SD  1 
ATOM   3386 C CE  . MET B  1 179 ? 19.687 -22.550 107.695 1.00 31.21  ? 194 MET B CE  1 
ATOM   3387 N N   . LEU B  1 180 ? 15.693 -19.491 112.788 1.00 36.17  ? 195 LEU B N   1 
ATOM   3388 C CA  . LEU B  1 180 ? 14.484 -18.907 113.410 1.00 37.49  ? 195 LEU B CA  1 
ATOM   3389 C C   . LEU B  1 180 ? 13.800 -18.099 112.310 1.00 37.12  ? 195 LEU B C   1 
ATOM   3390 O O   . LEU B  1 180 ? 14.514 -17.511 111.472 1.00 37.06  ? 195 LEU B O   1 
ATOM   3391 C CB  . LEU B  1 180 ? 14.905 -18.050 114.611 1.00 38.90  ? 195 LEU B CB  1 
ATOM   3392 C CG  . LEU B  1 180 ? 13.775 -17.423 115.427 1.00 40.50  ? 195 LEU B CG  1 
ATOM   3393 C CD1 . LEU B  1 180 ? 14.189 -17.264 116.878 1.00 42.34  ? 195 LEU B CD1 1 
ATOM   3394 C CD2 . LEU B  1 180 ? 13.343 -16.075 114.861 1.00 42.06  ? 195 LEU B CD2 1 
ATOM   3395 N N   . CYS B  1 181 ? 12.472 -18.076 112.331 1.00 36.98  ? 196 CYS B N   1 
ATOM   3396 C CA  A CYS B  1 181 ? 11.626 -17.492 111.255 0.50 36.57  ? 196 CYS B CA  1 
ATOM   3397 C CA  B CYS B  1 181 ? 11.645 -17.480 111.264 0.50 38.46  ? 196 CYS B CA  1 
ATOM   3398 C C   . CYS B  1 181 ? 10.752 -16.371 111.829 1.00 36.55  ? 196 CYS B C   1 
ATOM   3399 O O   . CYS B  1 181 ? 10.141 -16.585 112.890 1.00 36.86  ? 196 CYS B O   1 
ATOM   3400 C CB  A CYS B  1 181 ? 10.742 -18.551 110.599 0.50 37.74  ? 196 CYS B CB  1 
ATOM   3401 C CB  B CYS B  1 181 ? 10.827 -18.583 110.626 0.50 42.20  ? 196 CYS B CB  1 
ATOM   3402 S SG  A CYS B  1 181 ? 11.598 -19.530 109.340 0.50 37.40  ? 196 CYS B SG  1 
ATOM   3403 S SG  B CYS B  1 181 ? 9.710  -17.973 109.350 0.50 46.33  ? 196 CYS B SG  1 
ATOM   3404 N N   . ALA B  1 182 ? 10.689 -15.240 111.126 1.00 35.67  ? 197 ALA B N   1 
ATOM   3405 C CA  . ALA B  1 182 ? 9.908  -14.054 111.535 1.00 35.05  ? 197 ALA B CA  1 
ATOM   3406 C C   . ALA B  1 182 ? 9.571  -13.185 110.325 1.00 34.92  ? 197 ALA B C   1 
ATOM   3407 O O   . ALA B  1 182 ? 10.369 -13.133 109.366 1.00 35.23  ? 197 ALA B O   1 
ATOM   3408 C CB  . ALA B  1 182 ? 10.654 -13.268 112.584 1.00 36.15  ? 197 ALA B CB  1 
ATOM   3409 N N   . GLY B  1 183 ? 8.415  -12.523 110.395 1.00 34.68  ? 198 GLY B N   1 
ATOM   3410 C CA  . GLY B  1 183 ? 7.970  -11.520 109.415 1.00 34.29  ? 198 GLY B CA  1 
ATOM   3411 C C   . GLY B  1 183 ? 6.803  -12.009 108.586 1.00 34.83  ? 198 GLY B C   1 
ATOM   3412 O O   . GLY B  1 183 ? 6.426  -13.178 108.715 1.00 35.72  ? 198 GLY B O   1 
ATOM   3413 N N   . ASN B  1 184 ? 6.260  -11.117 107.759 1.00 36.30  ? 199 ASN B N   1 
ATOM   3414 C CA  . ASN B  1 184 ? 5.096  -11.362 106.869 1.00 37.64  ? 199 ASN B CA  1 
ATOM   3415 C C   . ASN B  1 184 ? 5.247  -10.452 105.642 1.00 38.31  ? 199 ASN B C   1 
ATOM   3416 O O   . ASN B  1 184 ? 6.351  -9.933  105.451 1.00 37.71  ? 199 ASN B O   1 
ATOM   3417 C CB  . ASN B  1 184 ? 3.791  -11.194 107.653 1.00 36.71  ? 199 ASN B CB  1 
ATOM   3418 C CG  . ASN B  1 184 ? 3.597  -9.819  108.263 1.00 36.52  ? 199 ASN B CG  1 
ATOM   3419 O OD1 . ASN B  1 184 ? 4.081  -8.802  107.763 1.00 37.54  ? 199 ASN B OD1 1 
ATOM   3420 N ND2 . ASN B  1 184 ? 2.819  -9.767  109.328 1.00 37.76  ? 199 ASN B ND2 1 
ATOM   3421 N N   . THR B  1 185 ? 4.182  -10.243 104.864 1.00 40.57  ? 200 THR B N   1 
ATOM   3422 C CA  . THR B  1 185 ? 4.198  -9.459  103.597 1.00 41.92  ? 200 THR B CA  1 
ATOM   3423 C C   . THR B  1 185 ? 4.203  -7.950  103.888 1.00 41.38  ? 200 THR B C   1 
ATOM   3424 O O   . THR B  1 185 ? 4.363  -7.191  102.926 1.00 42.88  ? 200 THR B O   1 
ATOM   3425 C CB  . THR B  1 185 ? 3.032  -9.872  102.688 1.00 41.84  ? 200 THR B CB  1 
ATOM   3426 O OG1 . THR B  1 185 ? 1.815  -9.746  103.425 1.00 43.85  ? 200 THR B OG1 1 
ATOM   3427 C CG2 . THR B  1 185 ? 3.158  -11.296 102.188 1.00 41.53  ? 200 THR B CG2 1 
ATOM   3428 N N   . ARG B  1 186 ? 4.041  -7.526  105.145 1.00 43.56  ? 201 ARG B N   1 
ATOM   3429 C CA  . ARG B  1 186 ? 4.087  -6.097  105.550 1.00 45.25  ? 201 ARG B CA  1 
ATOM   3430 C C   . ARG B  1 186 ? 5.349  -5.786  106.367 1.00 43.46  ? 201 ARG B C   1 
ATOM   3431 O O   . ARG B  1 186 ? 5.748  -4.620  106.369 1.00 41.95  ? 201 ARG B O   1 
ATOM   3432 C CB  . ARG B  1 186 ? 2.817  -5.753  106.330 1.00 47.42  ? 201 ARG B CB  1 
ATOM   3433 C CG  . ARG B  1 186 ? 1.568  -5.744  105.463 1.00 51.22  ? 201 ARG B CG  1 
ATOM   3434 C CD  . ARG B  1 186 ? 0.307  -5.531  106.280 1.00 54.47  ? 201 ARG B CD  1 
ATOM   3435 N NE  . ARG B  1 186 ? 0.035  -6.672  107.146 1.00 59.77  ? 201 ARG B NE  1 
ATOM   3436 C CZ  . ARG B  1 186 ? -0.508 -7.835  106.770 1.00 62.09  ? 201 ARG B CZ  1 
ATOM   3437 N NH1 . ARG B  1 186 ? -0.868 -8.051  105.513 1.00 64.19  ? 201 ARG B NH1 1 
ATOM   3438 N NH2 . ARG B  1 186 ? -0.696 -8.788  107.669 1.00 63.05  ? 201 ARG B NH2 1 
ATOM   3439 N N   . ARG B  1 187 ? 5.942  -6.773  107.044 1.00 41.64  ? 202 ARG B N   1 
ATOM   3440 C CA  . ARG B  1 187 ? 6.995  -6.564  108.075 1.00 39.98  ? 202 ARG B CA  1 
ATOM   3441 C C   . ARG B  1 187 ? 8.133  -7.561  107.844 1.00 38.63  ? 202 ARG B C   1 
ATOM   3442 O O   . ARG B  1 187 ? 7.878  -8.775  107.947 1.00 37.24  ? 202 ARG B O   1 
ATOM   3443 C CB  . ARG B  1 187 ? 6.382  -6.741  109.464 1.00 41.87  ? 202 ARG B CB  1 
ATOM   3444 C CG  . ARG B  1 187 ? 5.247  -5.777  109.765 1.00 43.73  ? 202 ARG B CG  1 
ATOM   3445 C CD  . ARG B  1 187 ? 4.298  -6.361  110.791 1.00 47.57  ? 202 ARG B CD  1 
ATOM   3446 N NE  . ARG B  1 187 ? 3.307  -5.368  111.188 1.00 51.35  ? 202 ARG B NE  1 
ATOM   3447 C CZ  . ARG B  1 187 ? 3.514  -4.358  112.033 1.00 51.96  ? 202 ARG B CZ  1 
ATOM   3448 N NH1 . ARG B  1 187 ? 4.693  -4.185  112.610 1.00 52.07  ? 202 ARG B NH1 1 
ATOM   3449 N NH2 . ARG B  1 187 ? 2.530  -3.515  112.299 1.00 55.18  ? 202 ARG B NH2 1 
ATOM   3450 N N   . ASP B  1 188 ? 9.332  -7.074  107.516 1.00 36.41  ? 203 ASP B N   1 
ATOM   3451 C CA  . ASP B  1 188 ? 10.497 -7.957  107.250 1.00 35.88  ? 203 ASP B CA  1 
ATOM   3452 C C   . ASP B  1 188 ? 11.793 -7.145  107.321 1.00 36.74  ? 203 ASP B C   1 
ATOM   3453 O O   . ASP B  1 188 ? 11.751 -5.903  107.277 1.00 35.96  ? 203 ASP B O   1 
ATOM   3454 C CB  . ASP B  1 188 ? 10.357 -8.677  105.899 1.00 36.91  ? 203 ASP B CB  1 
ATOM   3455 C CG  . ASP B  1 188 ? 11.136 -9.983  105.751 1.00 38.53  ? 203 ASP B CG  1 
ATOM   3456 O OD1 . ASP B  1 188 ? 11.850 -10.368 106.706 1.00 39.78  ? 203 ASP B OD1 1 
ATOM   3457 O OD2 . ASP B  1 188 ? 11.025 -10.619 104.668 1.00 38.84  ? 203 ASP B OD2 1 
ATOM   3458 N N   . SER B  1 189 ? 12.906 -7.855  107.464 1.00 36.40  ? 204 SER B N   1 
ATOM   3459 C CA  . SER B  1 189 ? 14.276 -7.349  107.226 1.00 36.74  ? 204 SER B CA  1 
ATOM   3460 C C   . SER B  1 189 ? 14.555 -7.490  105.731 1.00 37.53  ? 204 SER B C   1 
ATOM   3461 O O   . SER B  1 189 ? 13.822 -8.251  105.044 1.00 34.13  ? 204 SER B O   1 
ATOM   3462 C CB  . SER B  1 189 ? 15.286 -8.092  108.061 1.00 38.75  ? 204 SER B CB  1 
ATOM   3463 O OG  . SER B  1 189 ? 15.220 -9.485  107.795 1.00 37.98  ? 204 SER B OG  1 
ATOM   3464 N N   . CYS B  1 190 ? 15.562 -6.777  105.239 1.00 35.38  ? 205 CYS B N   1 
ATOM   3465 C CA  . CYS B  1 190 ? 15.910 -6.762  103.801 1.00 36.85  ? 205 CYS B CA  1 
ATOM   3466 C C   . CYS B  1 190 ? 17.426 -6.623  103.635 1.00 34.29  ? 205 CYS B C   1 
ATOM   3467 O O   . CYS B  1 190 ? 18.153 -6.701  104.652 1.00 33.68  ? 205 CYS B O   1 
ATOM   3468 C CB  . CYS B  1 190 ? 15.117 -5.658  103.111 1.00 39.20  ? 205 CYS B CB  1 
ATOM   3469 S SG  . CYS B  1 190 ? 14.848 -5.942  101.343 1.00 46.27  ? 205 CYS B SG  1 
ATOM   3470 N N   . GLN B  1 191 ? 17.877 -6.487  102.389 1.00 37.17  ? 206 GLN B N   1 
ATOM   3471 C CA  . GLN B  1 191 ? 19.317 -6.368  102.025 1.00 38.31  ? 206 GLN B CA  1 
ATOM   3472 C C   . GLN B  1 191 ? 19.893 -5.155  102.770 1.00 35.72  ? 206 GLN B C   1 
ATOM   3473 O O   . GLN B  1 191 ? 19.259 -4.084  102.726 1.00 34.36  ? 206 GLN B O   1 
ATOM   3474 C CB  . GLN B  1 191 ? 19.491 -6.246  100.509 1.00 42.31  ? 206 GLN B CB  1 
ATOM   3475 C CG  . GLN B  1 191 ? 19.370 -7.570  99.754  1.00 47.72  ? 206 GLN B CG  1 
ATOM   3476 C CD  . GLN B  1 191 ? 17.968 -8.130  99.646  1.00 50.55  ? 206 GLN B CD  1 
ATOM   3477 O OE1 . GLN B  1 191 ? 17.714 -9.289  99.958  1.00 54.52  ? 206 GLN B OE1 1 
ATOM   3478 N NE2 . GLN B  1 191 ? 17.028 -7.317  99.199  1.00 53.66  ? 206 GLN B NE2 1 
ATOM   3479 N N   . GLY B  1 192 ? 21.017 -5.332  103.467 1.00 33.85  ? 207 GLY B N   1 
ATOM   3480 C CA  . GLY B  1 192 ? 21.655 -4.298  104.307 1.00 34.16  ? 207 GLY B CA  1 
ATOM   3481 C C   . GLY B  1 192 ? 21.325 -4.455  105.786 1.00 33.45  ? 207 GLY B C   1 
ATOM   3482 O O   . GLY B  1 192 ? 22.060 -3.877  106.600 1.00 33.39  ? 207 GLY B O   1 
ATOM   3483 N N   . ASP B  1 193 ? 20.267 -5.200  106.137 1.00 32.54  ? 208 ASP B N   1 
ATOM   3484 C CA  . ASP B  1 193 ? 19.910 -5.516  107.545 1.00 32.32  ? 208 ASP B CA  1 
ATOM   3485 C C   . ASP B  1 193 ? 20.655 -6.769  108.018 1.00 31.09  ? 208 ASP B C   1 
ATOM   3486 O O   . ASP B  1 193 ? 20.683 -6.970  109.240 1.00 32.52  ? 208 ASP B O   1 
ATOM   3487 C CB  . ASP B  1 193 ? 18.405 -5.698  107.731 1.00 33.48  ? 208 ASP B CB  1 
ATOM   3488 C CG  . ASP B  1 193 ? 17.614 -4.434  107.451 1.00 33.54  ? 208 ASP B CG  1 
ATOM   3489 O OD1 . ASP B  1 193 ? 18.061 -3.354  107.886 1.00 32.68  ? 208 ASP B OD1 1 
ATOM   3490 O OD2 . ASP B  1 193 ? 16.574 -4.536  106.778 1.00 35.37  ? 208 ASP B OD2 1 
ATOM   3491 N N   . SER B  1 194 ? 21.232 -7.554  107.097 1.00 31.90  ? 209 SER B N   1 
ATOM   3492 C CA  . SER B  1 194 ? 22.002 -8.800  107.370 1.00 31.81  ? 209 SER B CA  1 
ATOM   3493 C C   . SER B  1 194 ? 22.997 -8.578  108.505 1.00 32.45  ? 209 SER B C   1 
ATOM   3494 O O   . SER B  1 194 ? 23.666 -7.522  108.510 1.00 30.51  ? 209 SER B O   1 
ATOM   3495 C CB  . SER B  1 194 ? 22.723 -9.305  106.155 1.00 33.73  ? 209 SER B CB  1 
ATOM   3496 O OG  . SER B  1 194 ? 21.846 -10.038 105.334 1.00 37.12  ? 209 SER B OG  1 
ATOM   3497 N N   . GLY B  1 195 ? 23.080 -9.548  109.422 1.00 31.07  ? 210 GLY B N   1 
ATOM   3498 C CA  . GLY B  1 195 ? 23.999 -9.529  110.570 1.00 32.82  ? 210 GLY B CA  1 
ATOM   3499 C C   . GLY B  1 195 ? 23.432 -8.770  111.757 1.00 33.08  ? 210 GLY B C   1 
ATOM   3500 O O   . GLY B  1 195 ? 23.983 -8.924  112.859 1.00 32.83  ? 210 GLY B O   1 
ATOM   3501 N N   . GLY B  1 196 ? 22.379 -7.972  111.547 1.00 32.51  ? 211 GLY B N   1 
ATOM   3502 C CA  . GLY B  1 196 ? 21.745 -7.163  112.592 1.00 31.51  ? 211 GLY B CA  1 
ATOM   3503 C C   . GLY B  1 196 ? 20.895 -8.027  113.513 1.00 31.72  ? 211 GLY B C   1 
ATOM   3504 O O   . GLY B  1 196 ? 20.641 -9.200  113.226 1.00 32.43  ? 211 GLY B O   1 
ATOM   3505 N N   . PRO B  1 197 ? 20.435 -7.457  114.647 1.00 31.35  ? 212 PRO B N   1 
ATOM   3506 C CA  . PRO B  1 197 ? 19.750 -8.224  115.676 1.00 31.84  ? 212 PRO B CA  1 
ATOM   3507 C C   . PRO B  1 197 ? 18.232 -8.335  115.485 1.00 33.64  ? 212 PRO B C   1 
ATOM   3508 O O   . PRO B  1 197 ? 17.610 -7.376  115.046 1.00 34.55  ? 212 PRO B O   1 
ATOM   3509 C CB  . PRO B  1 197 ? 20.095 -7.402  116.926 1.00 30.87  ? 212 PRO B CB  1 
ATOM   3510 C CG  . PRO B  1 197 ? 20.087 -5.964  116.440 1.00 30.47  ? 212 PRO B CG  1 
ATOM   3511 C CD  . PRO B  1 197 ? 20.569 -6.035  115.009 1.00 31.60  ? 212 PRO B CD  1 
ATOM   3512 N N   . LEU B  1 198 ? 17.698 -9.522  115.778 1.00 34.51  ? 213 LEU B N   1 
ATOM   3513 C CA  . LEU B  1 198 ? 16.270 -9.753  116.120 1.00 34.75  ? 213 LEU B CA  1 
ATOM   3514 C C   . LEU B  1 198 ? 16.208 -9.881  117.643 1.00 34.22  ? 213 LEU B C   1 
ATOM   3515 O O   . LEU B  1 198 ? 16.852 -10.819 118.183 1.00 33.73  ? 213 LEU B O   1 
ATOM   3516 C CB  . LEU B  1 198 ? 15.762 -11.013 115.411 1.00 33.96  ? 213 LEU B CB  1 
ATOM   3517 C CG  . LEU B  1 198 ? 14.307 -11.401 115.679 1.00 35.49  ? 213 LEU B CG  1 
ATOM   3518 C CD1 . LEU B  1 198 ? 13.352 -10.389 115.075 1.00 37.38  ? 213 LEU B CD1 1 
ATOM   3519 C CD2 . LEU B  1 198 ? 14.017 -12.782 115.128 1.00 37.05  ? 213 LEU B CD2 1 
ATOM   3520 N N   . VAL B  1 199 ? 15.487 -8.969  118.303 1.00 34.00  ? 214 VAL B N   1 
ATOM   3521 C CA  . VAL B  1 199 ? 15.445 -8.852  119.787 1.00 35.53  ? 214 VAL B CA  1 
ATOM   3522 C C   . VAL B  1 199 ? 13.997 -9.028  120.258 1.00 37.70  ? 214 VAL B C   1 
ATOM   3523 O O   . VAL B  1 199 ? 13.085 -8.469  119.617 1.00 36.82  ? 214 VAL B O   1 
ATOM   3524 C CB  . VAL B  1 199 ? 16.077 -7.541  120.296 1.00 36.22  ? 214 VAL B CB  1 
ATOM   3525 C CG1 . VAL B  1 199 ? 17.572 -7.523  120.032 1.00 37.08  ? 214 VAL B CG1 1 
ATOM   3526 C CG2 . VAL B  1 199 ? 15.424 -6.292  119.715 1.00 36.71  ? 214 VAL B CG2 1 
ATOM   3527 N N   . CYS B  1 200 ? 13.802 -9.829  121.309 1.00 40.44  ? 215 CYS B N   1 
ATOM   3528 C CA  . CYS B  1 200 ? 12.483 -10.067 121.953 1.00 43.55  ? 215 CYS B CA  1 
ATOM   3529 C C   . CYS B  1 200 ? 12.588 -9.674  123.429 1.00 42.50  ? 215 CYS B C   1 
ATOM   3530 O O   . CYS B  1 200 ? 13.600 -10.022 124.066 1.00 39.12  ? 215 CYS B O   1 
ATOM   3531 C CB  . CYS B  1 200 ? 12.029 -11.517 121.806 1.00 45.87  ? 215 CYS B CB  1 
ATOM   3532 S SG  . CYS B  1 200 ? 12.200 -12.179 120.127 1.00 50.35  ? 215 CYS B SG  1 
ATOM   3533 N N   . LYS B  1 201 ? 11.593 -8.941  123.932 1.00 45.17  ? 216 LYS B N   1 
ATOM   3534 C CA  . LYS B  1 201 ? 11.517 -8.497  125.346 1.00 48.46  ? 216 LYS B CA  1 
ATOM   3535 C C   . LYS B  1 201 ? 10.876 -9.622  126.165 1.00 47.11  ? 216 LYS B C   1 
ATOM   3536 O O   . LYS B  1 201 ? 9.701  -9.946  125.907 1.00 48.27  ? 216 LYS B O   1 
ATOM   3537 C CB  . LYS B  1 201 ? 10.732 -7.187  125.456 1.00 50.75  ? 216 LYS B CB  1 
ATOM   3538 C CG  . LYS B  1 201 ? 11.013 -6.400  126.729 1.00 53.34  ? 216 LYS B CG  1 
ATOM   3539 C CD  . LYS B  1 201 ? 10.340 -5.050  126.769 1.00 56.94  ? 216 LYS B CD  1 
ATOM   3540 C CE  . LYS B  1 201 ? 10.787 -4.215  127.949 1.00 59.27  ? 216 LYS B CE  1 
ATOM   3541 N NZ  . LYS B  1 201 ? 10.140 -2.883  127.950 1.00 59.88  ? 216 LYS B NZ  1 
ATOM   3542 N N   . VAL B  1 202 ? 11.651 -10.223 127.070 1.00 46.31  ? 217 VAL B N   1 
ATOM   3543 C CA  . VAL B  1 202 ? 11.264 -11.418 127.881 1.00 46.54  ? 217 VAL B CA  1 
ATOM   3544 C C   . VAL B  1 202 ? 11.486 -11.076 129.359 1.00 47.01  ? 217 VAL B C   1 
ATOM   3545 O O   . VAL B  1 202 ? 12.662 -10.881 129.744 1.00 44.26  ? 217 VAL B O   1 
ATOM   3546 C CB  . VAL B  1 202 ? 12.065 -12.667 127.464 1.00 46.02  ? 217 VAL B CB  1 
ATOM   3547 C CG1 . VAL B  1 202 ? 11.600 -13.910 128.212 1.00 48.15  ? 217 VAL B CG1 1 
ATOM   3548 C CG2 . VAL B  1 202 ? 12.014 -12.907 125.963 1.00 44.39  ? 217 VAL B CG2 1 
ATOM   3549 N N   . ASN B  1 203 ? 10.401 -10.978 130.141 1.00 51.77  ? 218 ASN B N   1 
ATOM   3550 C CA  . ASN B  1 203 ? 10.423 -10.642 131.594 1.00 54.02  ? 218 ASN B CA  1 
ATOM   3551 C C   . ASN B  1 203 ? 11.158 -9.309  131.793 1.00 51.86  ? 218 ASN B C   1 
ATOM   3552 O O   . ASN B  1 203 ? 12.059 -9.253  132.650 1.00 52.31  ? 218 ASN B O   1 
ATOM   3553 C CB  . ASN B  1 203 ? 11.045 -11.770 132.428 1.00 60.25  ? 218 ASN B CB  1 
ATOM   3554 C CG  . ASN B  1 203 ? 10.341 -13.100 132.251 1.00 66.71  ? 218 ASN B CG  1 
ATOM   3555 O OD1 . ASN B  1 203 ? 9.178  -13.137 131.855 1.00 70.24  ? 218 ASN B OD1 1 
ATOM   3556 N ND2 . ASN B  1 203 ? 11.032 -14.194 132.535 1.00 69.99  ? 218 ASN B ND2 1 
ATOM   3557 N N   . GLY B  1 204 ? 10.810 -8.297  130.986 1.00 52.95  ? 219 GLY B N   1 
ATOM   3558 C CA  . GLY B  1 204 ? 11.345 -6.925  131.069 1.00 51.92  ? 219 GLY B CA  1 
ATOM   3559 C C   . GLY B  1 204 ? 12.762 -6.772  130.528 1.00 53.05  ? 219 GLY B C   1 
ATOM   3560 O O   . GLY B  1 204 ? 13.276 -5.641  130.611 1.00 51.99  ? 219 GLY B O   1 
ATOM   3561 N N   . THR B  1 205 ? 13.384 -7.835  129.996 1.00 51.62  ? 220 THR B N   1 
ATOM   3562 C CA  . THR B  1 205 ? 14.776 -7.805  129.462 1.00 48.92  ? 220 THR B CA  1 
ATOM   3563 C C   . THR B  1 205 ? 14.751 -8.080  127.953 1.00 45.59  ? 220 THR B C   1 
ATOM   3564 O O   . THR B  1 205 ? 14.084 -9.053  127.533 1.00 43.13  ? 220 THR B O   1 
ATOM   3565 C CB  . THR B  1 205 ? 15.686 -8.778  130.224 1.00 50.38  ? 220 THR B CB  1 
ATOM   3566 O OG1 . THR B  1 205 ? 15.669 -8.372  131.591 1.00 53.32  ? 220 THR B OG1 1 
ATOM   3567 C CG2 . THR B  1 205 ? 17.122 -8.784  129.745 1.00 49.63  ? 220 THR B CG2 1 
ATOM   3568 N N   . TRP B  1 206 ? 15.440 -7.239  127.174 1.00 42.27  ? 221 TRP B N   1 
ATOM   3569 C CA  . TRP B  1 206 ? 15.677 -7.457  125.725 1.00 39.78  ? 221 TRP B CA  1 
ATOM   3570 C C   . TRP B  1 206 ? 16.700 -8.580  125.555 1.00 37.59  ? 221 TRP B C   1 
ATOM   3571 O O   . TRP B  1 206 ? 17.810 -8.452  126.113 1.00 37.20  ? 221 TRP B O   1 
ATOM   3572 C CB  . TRP B  1 206 ? 16.130 -6.172  125.030 1.00 39.24  ? 221 TRP B CB  1 
ATOM   3573 C CG  . TRP B  1 206 ? 15.028 -5.170  124.924 1.00 38.94  ? 221 TRP B CG  1 
ATOM   3574 C CD1 . TRP B  1 206 ? 14.854 -4.069  125.705 1.00 37.95  ? 221 TRP B CD1 1 
ATOM   3575 C CD2 . TRP B  1 206 ? 13.919 -5.202  124.010 1.00 37.65  ? 221 TRP B CD2 1 
ATOM   3576 N NE1 . TRP B  1 206 ? 13.722 -3.404  125.330 1.00 38.25  ? 221 TRP B NE1 1 
ATOM   3577 C CE2 . TRP B  1 206 ? 13.123 -4.073  124.295 1.00 38.02  ? 221 TRP B CE2 1 
ATOM   3578 C CE3 . TRP B  1 206 ? 13.520 -6.068  122.983 1.00 37.68  ? 221 TRP B CE3 1 
ATOM   3579 C CZ2 . TRP B  1 206 ? 11.958 -3.783  123.584 1.00 36.08  ? 221 TRP B CZ2 1 
ATOM   3580 C CZ3 . TRP B  1 206 ? 12.369 -5.783  122.281 1.00 37.71  ? 221 TRP B CZ3 1 
ATOM   3581 C CH2 . TRP B  1 206 ? 11.596 -4.659  122.585 1.00 36.65  ? 221 TRP B CH2 1 
ATOM   3582 N N   . LEU B  1 207 ? 16.323 -9.636  124.825 1.00 35.89  ? 222 LEU B N   1 
ATOM   3583 C CA  . LEU B  1 207 ? 17.221 -10.775 124.483 1.00 36.54  ? 222 LEU B CA  1 
ATOM   3584 C C   . LEU B  1 207 ? 17.373 -10.844 122.961 1.00 34.41  ? 222 LEU B C   1 
ATOM   3585 O O   . LEU B  1 207 ? 16.352 -10.733 122.262 1.00 35.71  ? 222 LEU B O   1 
ATOM   3586 C CB  . LEU B  1 207 ? 16.632 -12.076 125.046 1.00 35.35  ? 222 LEU B CB  1 
ATOM   3587 C CG  . LEU B  1 207 ? 16.392 -12.121 126.556 1.00 35.57  ? 222 LEU B CG  1 
ATOM   3588 C CD1 . LEU B  1 207 ? 15.790 -13.458 126.960 1.00 36.25  ? 222 LEU B CD1 1 
ATOM   3589 C CD2 . LEU B  1 207 ? 17.670 -11.868 127.345 1.00 36.17  ? 222 LEU B CD2 1 
ATOM   3590 N N   . GLN B  1 208 ? 18.592 -11.052 122.462 1.00 33.94  ? 223 GLN B N   1 
ATOM   3591 C CA  . GLN B  1 208 ? 18.823 -11.276 121.015 1.00 34.23  ? 223 GLN B CA  1 
ATOM   3592 C C   . GLN B  1 208 ? 18.473 -12.731 120.672 1.00 34.35  ? 223 GLN B C   1 
ATOM   3593 O O   . GLN B  1 208 ? 19.281 -13.625 120.963 1.00 36.03  ? 223 GLN B O   1 
ATOM   3594 C CB  . GLN B  1 208 ? 20.244 -10.909 120.588 1.00 33.36  ? 223 GLN B CB  1 
ATOM   3595 C CG  . GLN B  1 208 ? 20.367 -10.918 119.071 1.00 33.85  ? 223 GLN B CG  1 
ATOM   3596 C CD  . GLN B  1 208 ? 21.611 -10.276 118.511 1.00 34.61  ? 223 GLN B CD  1 
ATOM   3597 O OE1 . GLN B  1 208 ? 22.339 -9.560  119.193 1.00 32.36  ? 223 GLN B OE1 1 
ATOM   3598 N NE2 . GLN B  1 208 ? 21.853 -10.532 117.239 1.00 34.40  ? 223 GLN B NE2 1 
ATOM   3599 N N   . ALA B  1 209 ? 17.311 -12.948 120.052 1.00 35.97  ? 224 ALA B N   1 
ATOM   3600 C CA  . ALA B  1 209 ? 16.844 -14.260 119.544 1.00 34.03  ? 224 ALA B CA  1 
ATOM   3601 C C   . ALA B  1 209 ? 17.582 -14.643 118.250 1.00 33.38  ? 224 ALA B C   1 
ATOM   3602 O O   . ALA B  1 209 ? 17.863 -15.846 118.066 1.00 34.24  ? 224 ALA B O   1 
ATOM   3603 C CB  . ALA B  1 209 ? 15.355 -14.209 119.321 1.00 35.42  ? 224 ALA B CB  1 
ATOM   3604 N N   . GLY B  1 210 ? 17.880 -13.668 117.387 1.00 31.74  ? 225 GLY B N   1 
ATOM   3605 C CA  . GLY B  1 210 ? 18.242 -13.907 115.978 1.00 32.53  ? 225 GLY B CA  1 
ATOM   3606 C C   . GLY B  1 210 ? 19.314 -12.972 115.445 1.00 30.44  ? 225 GLY B C   1 
ATOM   3607 O O   . GLY B  1 210 ? 19.469 -11.856 115.947 1.00 28.57  ? 225 GLY B O   1 
ATOM   3608 N N   . VAL B  1 211 ? 20.035 -13.451 114.437 1.00 32.16  ? 226 VAL B N   1 
ATOM   3609 C CA  . VAL B  1 211 ? 20.895 -12.652 113.516 1.00 31.22  ? 226 VAL B CA  1 
ATOM   3610 C C   . VAL B  1 211 ? 20.225 -12.705 112.143 1.00 30.36  ? 226 VAL B C   1 
ATOM   3611 O O   . VAL B  1 211 ? 19.947 -13.831 111.686 1.00 31.79  ? 226 VAL B O   1 
ATOM   3612 C CB  . VAL B  1 211 ? 22.329 -13.209 113.469 1.00 31.67  ? 226 VAL B CB  1 
ATOM   3613 C CG1 . VAL B  1 211 ? 23.210 -12.425 112.511 1.00 32.17  ? 226 VAL B CG1 1 
ATOM   3614 C CG2 . VAL B  1 211 ? 22.960 -13.274 114.848 1.00 31.21  ? 226 VAL B CG2 1 
ATOM   3615 N N   . VAL B  1 212 ? 19.971 -11.548 111.521 1.00 30.50  ? 227 VAL B N   1 
ATOM   3616 C CA  . VAL B  1 212 ? 19.373 -11.462 110.158 1.00 30.21  ? 227 VAL B CA  1 
ATOM   3617 C C   . VAL B  1 212 ? 20.276 -12.271 109.220 1.00 31.01  ? 227 VAL B C   1 
ATOM   3618 O O   . VAL B  1 212 ? 21.483 -11.956 109.158 1.00 28.55  ? 227 VAL B O   1 
ATOM   3619 C CB  . VAL B  1 212 ? 19.192 -10.013 109.672 1.00 31.88  ? 227 VAL B CB  1 
ATOM   3620 C CG1 . VAL B  1 212 ? 18.638 -9.966  108.254 1.00 34.02  ? 227 VAL B CG1 1 
ATOM   3621 C CG2 . VAL B  1 212 ? 18.286 -9.202  110.589 1.00 33.30  ? 227 VAL B CG2 1 
ATOM   3622 N N   . SER B  1 213 ? 19.724 -13.294 108.557 1.00 29.33  ? 228 SER B N   1 
ATOM   3623 C CA  . SER B  1 213 ? 20.512 -14.287 107.782 1.00 30.42  ? 228 SER B CA  1 
ATOM   3624 C C   . SER B  1 213 ? 20.121 -14.263 106.304 1.00 29.78  ? 228 SER B C   1 
ATOM   3625 O O   . SER B  1 213 ? 20.961 -13.861 105.492 1.00 31.60  ? 228 SER B O   1 
ATOM   3626 C CB  . SER B  1 213 ? 20.397 -15.668 108.374 1.00 28.64  ? 228 SER B CB  1 
ATOM   3627 O OG  . SER B  1 213 ? 21.280 -16.544 107.700 1.00 30.09  ? 228 SER B OG  1 
ATOM   3628 N N   . TRP B  1 214 ? 18.924 -14.734 105.953 1.00 31.22  ? 229 TRP B N   1 
ATOM   3629 C CA  . TRP B  1 214 ? 18.528 -14.926 104.533 1.00 31.38  ? 229 TRP B CA  1 
ATOM   3630 C C   . TRP B  1 214 ? 17.008 -14.977 104.374 1.00 32.45  ? 229 TRP B C   1 
ATOM   3631 O O   . TRP B  1 214 ? 16.278 -14.978 105.380 1.00 33.10  ? 229 TRP B O   1 
ATOM   3632 C CB  . TRP B  1 214 ? 19.212 -16.159 103.932 1.00 30.87  ? 229 TRP B CB  1 
ATOM   3633 C CG  . TRP B  1 214 ? 18.781 -17.480 104.494 1.00 30.46  ? 229 TRP B CG  1 
ATOM   3634 C CD1 . TRP B  1 214 ? 19.217 -18.068 105.643 1.00 30.49  ? 229 TRP B CD1 1 
ATOM   3635 C CD2 . TRP B  1 214 ? 17.907 -18.434 103.866 1.00 29.67  ? 229 TRP B CD2 1 
ATOM   3636 N NE1 . TRP B  1 214 ? 18.628 -19.293 105.803 1.00 30.59  ? 229 TRP B NE1 1 
ATOM   3637 C CE2 . TRP B  1 214 ? 17.830 -19.554 104.722 1.00 30.37  ? 229 TRP B CE2 1 
ATOM   3638 C CE3 . TRP B  1 214 ? 17.165 -18.441 102.678 1.00 30.97  ? 229 TRP B CE3 1 
ATOM   3639 C CZ2 . TRP B  1 214 ? 17.037 -20.665 104.428 1.00 30.85  ? 229 TRP B CZ2 1 
ATOM   3640 C CZ3 . TRP B  1 214 ? 16.377 -19.537 102.390 1.00 31.06  ? 229 TRP B CZ3 1 
ATOM   3641 C CH2 . TRP B  1 214 ? 16.323 -20.635 103.250 1.00 30.56  ? 229 TRP B CH2 1 
ATOM   3642 N N   . GLY B  1 215 ? 16.571 -14.996 103.120 1.00 34.53  ? 230 GLY B N   1 
ATOM   3643 C CA  . GLY B  1 215 ? 15.168 -15.199 102.720 1.00 37.00  ? 230 GLY B CA  1 
ATOM   3644 C C   . GLY B  1 215 ? 15.053 -15.110 101.215 1.00 37.69  ? 230 GLY B C   1 
ATOM   3645 O O   . GLY B  1 215 ? 16.048 -14.729 100.581 1.00 40.50  ? 230 GLY B O   1 
ATOM   3646 N N   . GLU B  1 216 ? 13.902 -15.477 100.656 1.00 38.45  ? 231 GLU B N   1 
ATOM   3647 C CA  . GLU B  1 216 ? 13.599 -15.254 99.221  1.00 38.65  ? 231 GLU B CA  1 
ATOM   3648 C C   . GLU B  1 216 ? 13.009 -13.847 99.107  1.00 38.98  ? 231 GLU B C   1 
ATOM   3649 O O   . GLU B  1 216 ? 11.821 -13.664 99.464  1.00 40.39  ? 231 GLU B O   1 
ATOM   3650 C CB  . GLU B  1 216 ? 12.664 -16.331 98.676  1.00 42.47  ? 231 GLU B CB  1 
ATOM   3651 C CG  . GLU B  1 216 ? 12.387 -16.185 97.185  1.00 46.60  ? 231 GLU B CG  1 
ATOM   3652 C CD  . GLU B  1 216 ? 11.369 -17.166 96.633  1.00 47.50  ? 231 GLU B CD  1 
ATOM   3653 O OE1 . GLU B  1 216 ? 11.404 -18.337 97.042  1.00 48.92  ? 231 GLU B OE1 1 
ATOM   3654 O OE2 . GLU B  1 216 ? 10.542 -16.752 95.801  1.00 52.02  ? 231 GLU B OE2 1 
ATOM   3655 N N   . GLY B  1 217 ? 13.832 -12.888 98.685  1.00 39.38  ? 232 GLY B N   1 
ATOM   3656 C CA  . GLY B  1 217 ? 13.465 -11.461 98.649  1.00 40.62  ? 232 GLY B CA  1 
ATOM   3657 C C   . GLY B  1 217 ? 13.101 -10.956 100.034 1.00 38.65  ? 232 GLY B C   1 
ATOM   3658 O O   . GLY B  1 217 ? 13.589 -11.532 101.029 1.00 37.37  ? 232 GLY B O   1 
ATOM   3659 N N   . CYS B  1 218 ? 12.253 -9.928  100.090 1.00 38.79  ? 233 CYS B N   1 
ATOM   3660 C CA  . CYS B  1 218 ? 11.809 -9.243  101.328 1.00 39.24  ? 233 CYS B CA  1 
ATOM   3661 C C   . CYS B  1 218 ? 10.281 -9.152  101.298 1.00 38.64  ? 233 CYS B C   1 
ATOM   3662 O O   . CYS B  1 218 ? 9.746  -8.724  100.263 1.00 37.64  ? 233 CYS B O   1 
ATOM   3663 C CB  . CYS B  1 218 ? 12.450 -7.862  101.432 1.00 42.08  ? 233 CYS B CB  1 
ATOM   3664 S SG  . CYS B  1 218 ? 14.242 -7.904  101.159 1.00 48.75  ? 233 CYS B SG  1 
ATOM   3665 N N   . ALA B  1 219 ? 9.624  -9.598  102.370 1.00 38.56  ? 234 ALA B N   1 
ATOM   3666 C CA  . ALA B  1 219 ? 8.167  -9.486  102.605 1.00 39.26  ? 234 ALA B CA  1 
ATOM   3667 C C   . ALA B  1 219 ? 7.380  -10.097 101.433 1.00 39.25  ? 234 ALA B C   1 
ATOM   3668 O O   . ALA B  1 219 ? 6.372  -9.512  101.042 1.00 38.23  ? 234 ALA B O   1 
ATOM   3669 C CB  . ALA B  1 219 ? 7.820  -8.034  102.842 1.00 39.23  ? 234 ALA B CB  1 
ATOM   3670 N N   . GLN B  1 220 ? 7.850  -11.226 100.897 1.00 40.14  ? 235 GLN B N   1 
ATOM   3671 C CA  . GLN B  1 220 ? 7.202  -11.975 99.789  1.00 43.36  ? 235 GLN B CA  1 
ATOM   3672 C C   . GLN B  1 220 ? 6.243  -13.005 100.382 1.00 40.29  ? 235 GLN B C   1 
ATOM   3673 O O   . GLN B  1 220 ? 6.517  -13.554 101.449 1.00 37.96  ? 235 GLN B O   1 
ATOM   3674 C CB  . GLN B  1 220 ? 8.246  -12.668 98.907  1.00 45.72  ? 235 GLN B CB  1 
ATOM   3675 C CG  . GLN B  1 220 ? 9.214  -11.719 98.215  1.00 51.01  ? 235 GLN B CG  1 
ATOM   3676 C CD  . GLN B  1 220 ? 8.541  -10.882 97.152  1.00 52.82  ? 235 GLN B CD  1 
ATOM   3677 O OE1 . GLN B  1 220 ? 7.839  -9.918  97.451  1.00 54.23  ? 235 GLN B OE1 1 
ATOM   3678 N NE2 . GLN B  1 220 ? 8.749  -11.240 95.896  1.00 55.06  ? 235 GLN B NE2 1 
ATOM   3679 N N   . PRO B  1 221 ? 5.100  -13.305 99.715  1.00 41.85  ? 236 PRO B N   1 
ATOM   3680 C CA  . PRO B  1 221 ? 4.173  -14.339 100.186 1.00 40.28  ? 236 PRO B CA  1 
ATOM   3681 C C   . PRO B  1 221 ? 4.840  -15.705 100.418 1.00 38.61  ? 236 PRO B C   1 
ATOM   3682 O O   . PRO B  1 221 ? 5.582  -16.136 99.559  1.00 36.03  ? 236 PRO B O   1 
ATOM   3683 C CB  . PRO B  1 221 ? 3.133  -14.449 99.059  1.00 41.55  ? 236 PRO B CB  1 
ATOM   3684 C CG  . PRO B  1 221 ? 3.182  -13.102 98.365  1.00 42.52  ? 236 PRO B CG  1 
ATOM   3685 C CD  . PRO B  1 221 ? 4.628  -12.665 98.471  1.00 42.34  ? 236 PRO B CD  1 
ATOM   3686 N N   . ASN B  1 222 ? 4.587  -16.318 101.584 1.00 38.11  ? 237 ASN B N   1 
ATOM   3687 C CA  . ASN B  1 222 ? 5.063  -17.674 101.974 1.00 39.02  ? 237 ASN B CA  1 
ATOM   3688 C C   . ASN B  1 222 ? 6.595  -17.727 102.064 1.00 38.16  ? 237 ASN B C   1 
ATOM   3689 O O   . ASN B  1 222 ? 7.143  -18.853 101.965 1.00 36.76  ? 237 ASN B O   1 
ATOM   3690 C CB  . ASN B  1 222 ? 4.544  -18.745 101.005 1.00 39.58  ? 237 ASN B CB  1 
ATOM   3691 C CG  . ASN B  1 222 ? 3.043  -18.911 101.070 1.00 40.47  ? 237 ASN B CG  1 
ATOM   3692 O OD1 . ASN B  1 222 ? 2.458  -18.889 102.148 1.00 40.67  ? 237 ASN B OD1 1 
ATOM   3693 N ND2 . ASN B  1 222 ? 2.414  -19.136 99.927  1.00 40.92  ? 237 ASN B ND2 1 
ATOM   3694 N N   . ARG B  1 223 ? 7.261  -16.578 102.253 1.00 37.79  ? 238 ARG B N   1 
ATOM   3695 C CA  . ARG B  1 223 ? 8.741  -16.469 102.305 1.00 37.57  ? 238 ARG B CA  1 
ATOM   3696 C C   . ARG B  1 223 ? 9.139  -15.526 103.440 1.00 37.94  ? 238 ARG B C   1 
ATOM   3697 O O   . ARG B  1 223 ? 9.716  -14.465 103.214 1.00 36.38  ? 238 ARG B O   1 
ATOM   3698 C CB  . ARG B  1 223 ? 9.271  -16.018 100.939 1.00 36.41  ? 238 ARG B CB  1 
ATOM   3699 C CG  . ARG B  1 223 ? 8.955  -16.962 99.786  1.00 36.07  ? 238 ARG B CG  1 
ATOM   3700 C CD  . ARG B  1 223 ? 9.646  -18.308 99.899  1.00 35.46  ? 238 ARG B CD  1 
ATOM   3701 N NE  . ARG B  1 223 ? 9.445  -19.124 98.714  1.00 36.79  ? 238 ARG B NE  1 
ATOM   3702 C CZ  . ARG B  1 223 ? 8.442  -19.983 98.497  1.00 37.12  ? 238 ARG B CZ  1 
ATOM   3703 N NH1 . ARG B  1 223 ? 7.470  -20.171 99.382  1.00 34.54  ? 238 ARG B NH1 1 
ATOM   3704 N NH2 . ARG B  1 223 ? 8.421  -20.655 97.359  1.00 36.66  ? 238 ARG B NH2 1 
ATOM   3705 N N   . PRO B  1 224 ? 8.849  -15.886 104.709 1.00 38.87  ? 239 PRO B N   1 
ATOM   3706 C CA  . PRO B  1 224 ? 9.275  -15.062 105.836 1.00 37.79  ? 239 PRO B CA  1 
ATOM   3707 C C   . PRO B  1 224 ? 10.803 -15.036 106.001 1.00 36.36  ? 239 PRO B C   1 
ATOM   3708 O O   . PRO B  1 224 ? 11.483 -15.911 105.476 1.00 37.38  ? 239 PRO B O   1 
ATOM   3709 C CB  . PRO B  1 224 ? 8.566  -15.674 107.045 1.00 38.47  ? 239 PRO B CB  1 
ATOM   3710 C CG  . PRO B  1 224 ? 8.220  -17.085 106.627 1.00 38.82  ? 239 PRO B CG  1 
ATOM   3711 C CD  . PRO B  1 224 ? 8.101  -17.084 105.123 1.00 38.34  ? 239 PRO B CD  1 
ATOM   3712 N N   . GLY B  1 225 ? 11.300 -13.996 106.672 1.00 33.10  ? 240 GLY B N   1 
ATOM   3713 C CA  . GLY B  1 225 ? 12.729 -13.809 106.972 1.00 32.05  ? 240 GLY B CA  1 
ATOM   3714 C C   . GLY B  1 225 ? 13.269 -14.967 107.785 1.00 30.45  ? 240 GLY B C   1 
ATOM   3715 O O   . GLY B  1 225 ? 12.563 -15.442 108.680 1.00 29.72  ? 240 GLY B O   1 
ATOM   3716 N N   . ILE B  1 226 ? 14.470 -15.427 107.453 1.00 30.76  ? 241 ILE B N   1 
ATOM   3717 C CA  . ILE B  1 226 ? 15.213 -16.477 108.201 1.00 30.91  ? 241 ILE B CA  1 
ATOM   3718 C C   . ILE B  1 226 ? 16.348 -15.789 108.957 1.00 31.07  ? 241 ILE B C   1 
ATOM   3719 O O   . ILE B  1 226 ? 17.035 -14.924 108.369 1.00 32.74  ? 241 ILE B O   1 
ATOM   3720 C CB  . ILE B  1 226 ? 15.728 -17.586 107.270 1.00 32.02  ? 241 ILE B CB  1 
ATOM   3721 C CG1 . ILE B  1 226 ? 14.675 -18.015 106.241 1.00 35.63  ? 241 ILE B CG1 1 
ATOM   3722 C CG2 . ILE B  1 226 ? 16.221 -18.770 108.080 1.00 32.98  ? 241 ILE B CG2 1 
ATOM   3723 C CD1 . ILE B  1 226 ? 13.376 -18.482 106.840 1.00 36.66  ? 241 ILE B CD1 1 
ATOM   3724 N N   . TYR B  1 227 ? 16.516 -16.183 110.213 1.00 30.69  ? 242 TYR B N   1 
ATOM   3725 C CA  . TYR B  1 227 ? 17.501 -15.640 111.175 1.00 32.07  ? 242 TYR B CA  1 
ATOM   3726 C C   . TYR B  1 227 ? 18.307 -16.810 111.724 1.00 32.00  ? 242 TYR B C   1 
ATOM   3727 O O   . TYR B  1 227 ? 17.717 -17.897 111.884 1.00 33.43  ? 242 TYR B O   1 
ATOM   3728 C CB  . TYR B  1 227 ? 16.779 -14.905 112.305 1.00 31.27  ? 242 TYR B CB  1 
ATOM   3729 C CG  . TYR B  1 227 ? 15.966 -13.717 111.866 1.00 31.29  ? 242 TYR B CG  1 
ATOM   3730 C CD1 . TYR B  1 227 ? 14.747 -13.869 111.220 1.00 30.32  ? 242 TYR B CD1 1 
ATOM   3731 C CD2 . TYR B  1 227 ? 16.413 -12.430 112.114 1.00 31.29  ? 242 TYR B CD2 1 
ATOM   3732 C CE1 . TYR B  1 227 ? 14.000 -12.773 110.817 1.00 31.60  ? 242 TYR B CE1 1 
ATOM   3733 C CE2 . TYR B  1 227 ? 15.675 -11.324 111.724 1.00 31.30  ? 242 TYR B CE2 1 
ATOM   3734 C CZ  . TYR B  1 227 ? 14.465 -11.494 111.076 1.00 32.07  ? 242 TYR B CZ  1 
ATOM   3735 O OH  . TYR B  1 227 ? 13.758 -10.394 110.693 1.00 33.16  ? 242 TYR B OH  1 
ATOM   3736 N N   . THR B  1 228 ? 19.592 -16.606 111.998 1.00 31.68  ? 243 THR B N   1 
ATOM   3737 C CA  . THR B  1 228 ? 20.401 -17.563 112.789 1.00 32.47  ? 243 THR B CA  1 
ATOM   3738 C C   . THR B  1 228 ? 19.835 -17.580 114.211 1.00 33.10  ? 243 THR B C   1 
ATOM   3739 O O   . THR B  1 228 ? 19.656 -16.491 114.774 1.00 32.86  ? 243 THR B O   1 
ATOM   3740 C CB  . THR B  1 228 ? 21.895 -17.216 112.768 1.00 30.64  ? 243 THR B CB  1 
ATOM   3741 O OG1 . THR B  1 228 ? 22.257 -17.005 111.407 1.00 29.86  ? 243 THR B OG1 1 
ATOM   3742 C CG2 . THR B  1 228 ? 22.751 -18.310 113.366 1.00 32.01  ? 243 THR B CG2 1 
ATOM   3743 N N   . ARG B  1 229 ? 19.540 -18.767 114.747 1.00 32.81  ? 244 ARG B N   1 
ATOM   3744 C CA  . ARG B  1 229 ? 19.029 -18.958 116.127 1.00 33.52  ? 244 ARG B CA  1 
ATOM   3745 C C   . ARG B  1 229 ? 20.217 -18.848 117.088 1.00 32.80  ? 244 ARG B C   1 
ATOM   3746 O O   . ARG B  1 229 ? 21.077 -19.759 117.073 1.00 31.25  ? 244 ARG B O   1 
ATOM   3747 C CB  . ARG B  1 229 ? 18.303 -20.304 116.220 1.00 34.33  ? 244 ARG B CB  1 
ATOM   3748 C CG  . ARG B  1 229 ? 17.590 -20.559 117.537 1.00 35.38  ? 244 ARG B CG  1 
ATOM   3749 C CD  . ARG B  1 229 ? 16.842 -21.875 117.466 1.00 35.55  ? 244 ARG B CD  1 
ATOM   3750 N NE  . ARG B  1 229 ? 15.604 -21.746 116.708 1.00 36.59  ? 244 ARG B NE  1 
ATOM   3751 C CZ  . ARG B  1 229 ? 14.460 -21.232 117.162 1.00 35.91  ? 244 ARG B CZ  1 
ATOM   3752 N NH1 . ARG B  1 229 ? 14.360 -20.778 118.402 1.00 37.48  ? 244 ARG B NH1 1 
ATOM   3753 N NH2 . ARG B  1 229 ? 13.406 -21.179 116.362 1.00 37.77  ? 244 ARG B NH2 1 
ATOM   3754 N N   . VAL B  1 230 ? 20.282 -17.777 117.887 1.00 31.27  ? 245 VAL B N   1 
ATOM   3755 C CA  . VAL B  1 230 ? 21.462 -17.471 118.752 1.00 31.97  ? 245 VAL B CA  1 
ATOM   3756 C C   . VAL B  1 230 ? 21.651 -18.582 119.801 1.00 32.26  ? 245 VAL B C   1 
ATOM   3757 O O   . VAL B  1 230 ? 22.830 -18.944 120.055 1.00 32.86  ? 245 VAL B O   1 
ATOM   3758 C CB  . VAL B  1 230 ? 21.355 -16.079 119.406 1.00 32.83  ? 245 VAL B CB  1 
ATOM   3759 C CG1 . VAL B  1 230 ? 22.468 -15.841 120.420 1.00 34.25  ? 245 VAL B CG1 1 
ATOM   3760 C CG2 . VAL B  1 230 ? 21.355 -14.961 118.367 1.00 32.96  ? 245 VAL B CG2 1 
ATOM   3761 N N   . THR B  1 231 ? 20.571 -19.120 120.384 1.00 32.19  ? 246 THR B N   1 
ATOM   3762 C CA  . THR B  1 231 ? 20.649 -20.162 121.451 1.00 33.37  ? 246 THR B CA  1 
ATOM   3763 C C   . THR B  1 231 ? 21.457 -21.368 120.962 1.00 32.77  ? 246 THR B C   1 
ATOM   3764 O O   . THR B  1 231 ? 22.176 -21.956 121.777 1.00 34.52  ? 246 THR B O   1 
ATOM   3765 C CB  . THR B  1 231 ? 19.274 -20.608 121.961 1.00 34.63  ? 246 THR B CB  1 
ATOM   3766 O OG1 . THR B  1 231 ? 18.480 -21.030 120.851 1.00 36.38  ? 246 THR B OG1 1 
ATOM   3767 C CG2 . THR B  1 231 ? 18.585 -19.519 122.755 1.00 35.00  ? 246 THR B CG2 1 
ATOM   3768 N N   . TYR B  1 232 ? 21.367 -21.692 119.674 1.00 35.28  ? 247 TYR B N   1 
ATOM   3769 C CA  . TYR B  1 232 ? 22.066 -22.842 119.042 1.00 35.04  ? 247 TYR B CA  1 
ATOM   3770 C C   . TYR B  1 232 ? 23.592 -22.684 119.121 1.00 34.94  ? 247 TYR B C   1 
ATOM   3771 O O   . TYR B  1 232 ? 24.297 -23.712 119.174 1.00 35.58  ? 247 TYR B O   1 
ATOM   3772 C CB  . TYR B  1 232 ? 21.599 -23.000 117.597 1.00 35.73  ? 247 TYR B CB  1 
ATOM   3773 C CG  . TYR B  1 232 ? 21.902 -24.351 117.010 1.00 36.13  ? 247 TYR B CG  1 
ATOM   3774 C CD1 . TYR B  1 232 ? 23.144 -24.619 116.460 1.00 36.66  ? 247 TYR B CD1 1 
ATOM   3775 C CD2 . TYR B  1 232 ? 20.950 -25.363 117.006 1.00 34.57  ? 247 TYR B CD2 1 
ATOM   3776 C CE1 . TYR B  1 232 ? 23.438 -25.860 115.915 1.00 37.94  ? 247 TYR B CE1 1 
ATOM   3777 C CE2 . TYR B  1 232 ? 21.225 -26.606 116.461 1.00 36.19  ? 247 TYR B CE2 1 
ATOM   3778 C CZ  . TYR B  1 232 ? 22.475 -26.855 115.918 1.00 38.65  ? 247 TYR B CZ  1 
ATOM   3779 O OH  . TYR B  1 232 ? 22.754 -28.074 115.374 1.00 42.09  ? 247 TYR B OH  1 
ATOM   3780 N N   . TYR B  1 233 ? 24.104 -21.448 119.121 1.00 34.70  ? 248 TYR B N   1 
ATOM   3781 C CA  . TYR B  1 233 ? 25.550 -21.119 118.987 1.00 35.24  ? 248 TYR B CA  1 
ATOM   3782 C C   . TYR B  1 233 ? 26.128 -20.463 120.256 1.00 36.29  ? 248 TYR B C   1 
ATOM   3783 O O   . TYR B  1 233 ? 27.276 -19.983 120.175 1.00 36.90  ? 248 TYR B O   1 
ATOM   3784 C CB  . TYR B  1 233 ? 25.743 -20.274 117.720 1.00 34.33  ? 248 TYR B CB  1 
ATOM   3785 C CG  . TYR B  1 233 ? 25.429 -21.051 116.465 1.00 32.42  ? 248 TYR B CG  1 
ATOM   3786 C CD1 . TYR B  1 233 ? 26.251 -22.093 116.069 1.00 32.25  ? 248 TYR B CD1 1 
ATOM   3787 C CD2 . TYR B  1 233 ? 24.270 -20.828 115.735 1.00 31.82  ? 248 TYR B CD2 1 
ATOM   3788 C CE1 . TYR B  1 233 ? 25.963 -22.867 114.961 1.00 31.94  ? 248 TYR B CE1 1 
ATOM   3789 C CE2 . TYR B  1 233 ? 23.967 -21.590 114.616 1.00 32.64  ? 248 TYR B CE2 1 
ATOM   3790 C CZ  . TYR B  1 233 ? 24.814 -22.619 114.236 1.00 31.55  ? 248 TYR B CZ  1 
ATOM   3791 O OH  . TYR B  1 233 ? 24.570 -23.402 113.156 1.00 29.97  ? 248 TYR B OH  1 
ATOM   3792 N N   . LEU B  1 234 ? 25.427 -20.505 121.397 1.00 37.42  ? 249 LEU B N   1 
ATOM   3793 C CA  . LEU B  1 234 ? 25.888 -19.881 122.674 1.00 38.37  ? 249 LEU B CA  1 
ATOM   3794 C C   . LEU B  1 234 ? 27.252 -20.443 123.094 1.00 39.80  ? 249 LEU B C   1 
ATOM   3795 O O   . LEU B  1 234 ? 28.122 -19.626 123.457 1.00 35.45  ? 249 LEU B O   1 
ATOM   3796 C CB  . LEU B  1 234 ? 24.861 -20.084 123.794 1.00 39.02  ? 249 LEU B CB  1 
ATOM   3797 C CG  . LEU B  1 234 ? 23.594 -19.228 123.707 1.00 38.58  ? 249 LEU B CG  1 
ATOM   3798 C CD1 . LEU B  1 234 ? 22.530 -19.732 124.675 1.00 38.85  ? 249 LEU B CD1 1 
ATOM   3799 C CD2 . LEU B  1 234 ? 23.893 -17.756 123.959 1.00 37.70  ? 249 LEU B CD2 1 
ATOM   3800 N N   . ASP B  1 235 ? 27.440 -21.767 123.045 1.00 41.31  ? 250 ASP B N   1 
ATOM   3801 C CA  . ASP B  1 235 ? 28.717 -22.426 123.451 1.00 42.24  ? 250 ASP B CA  1 
ATOM   3802 C C   . ASP B  1 235 ? 29.872 -21.922 122.583 1.00 40.02  ? 250 ASP B C   1 
ATOM   3803 O O   . ASP B  1 235 ? 30.967 -21.667 123.146 1.00 40.14  ? 250 ASP B O   1 
ATOM   3804 C CB  . ASP B  1 235 ? 28.658 -23.954 123.371 1.00 45.72  ? 250 ASP B CB  1 
ATOM   3805 C CG  . ASP B  1 235 ? 27.707 -24.602 124.361 1.00 49.17  ? 250 ASP B CG  1 
ATOM   3806 O OD1 . ASP B  1 235 ? 27.278 -23.912 125.305 1.00 50.51  ? 250 ASP B OD1 1 
ATOM   3807 O OD2 . ASP B  1 235 ? 27.410 -25.800 124.179 1.00 54.47  ? 250 ASP B OD2 1 
ATOM   3808 N N   . TRP B  1 236 ? 29.646 -21.776 121.274 1.00 36.85  ? 251 TRP B N   1 
ATOM   3809 C CA  . TRP B  1 236 ? 30.665 -21.255 120.325 1.00 35.42  ? 251 TRP B CA  1 
ATOM   3810 C C   . TRP B  1 236 ? 30.966 -19.785 120.652 1.00 34.28  ? 251 TRP B C   1 
ATOM   3811 O O   . TRP B  1 236 ? 32.151 -19.424 120.680 1.00 34.63  ? 251 TRP B O   1 
ATOM   3812 C CB  . TRP B  1 236 ? 30.223 -21.446 118.869 1.00 35.61  ? 251 TRP B CB  1 
ATOM   3813 C CG  . TRP B  1 236 ? 31.177 -20.871 117.869 1.00 34.22  ? 251 TRP B CG  1 
ATOM   3814 C CD1 . TRP B  1 236 ? 32.316 -21.448 117.392 1.00 33.53  ? 251 TRP B CD1 1 
ATOM   3815 C CD2 . TRP B  1 236 ? 31.097 -19.571 117.256 1.00 35.27  ? 251 TRP B CD2 1 
ATOM   3816 N NE1 . TRP B  1 236 ? 32.940 -20.609 116.511 1.00 33.57  ? 251 TRP B NE1 1 
ATOM   3817 C CE2 . TRP B  1 236 ? 32.217 -19.449 116.407 1.00 34.02  ? 251 TRP B CE2 1 
ATOM   3818 C CE3 . TRP B  1 236 ? 30.185 -18.509 117.329 1.00 36.13  ? 251 TRP B CE3 1 
ATOM   3819 C CZ2 . TRP B  1 236 ? 32.447 -18.310 115.637 1.00 34.22  ? 251 TRP B CZ2 1 
ATOM   3820 C CZ3 . TRP B  1 236 ? 30.408 -17.385 116.559 1.00 35.92  ? 251 TRP B CZ3 1 
ATOM   3821 C CH2 . TRP B  1 236 ? 31.525 -17.290 115.723 1.00 34.45  ? 251 TRP B CH2 1 
ATOM   3822 N N   . ILE B  1 237 ? 29.942 -18.966 120.893 1.00 34.63  ? 252 ILE B N   1 
ATOM   3823 C CA  . ILE B  1 237 ? 30.114 -17.528 121.270 1.00 35.74  ? 252 ILE B CA  1 
ATOM   3824 C C   . ILE B  1 237 ? 30.946 -17.458 122.563 1.00 37.38  ? 252 ILE B C   1 
ATOM   3825 O O   . ILE B  1 237 ? 31.933 -16.695 122.581 1.00 37.06  ? 252 ILE B O   1 
ATOM   3826 C CB  . ILE B  1 237 ? 28.753 -16.811 121.398 1.00 35.81  ? 252 ILE B CB  1 
ATOM   3827 C CG1 . ILE B  1 237 ? 28.034 -16.692 120.053 1.00 34.84  ? 252 ILE B CG1 1 
ATOM   3828 C CG2 . ILE B  1 237 ? 28.914 -15.446 122.052 1.00 37.88  ? 252 ILE B CG2 1 
ATOM   3829 C CD1 . ILE B  1 237 ? 26.560 -16.328 120.165 1.00 34.50  ? 252 ILE B CD1 1 
ATOM   3830 N N   . HIS B  1 238 ? 30.583 -18.247 123.584 1.00 37.59  ? 253 HIS B N   1 
ATOM   3831 C CA  . HIS B  1 238 ? 31.230 -18.265 124.927 1.00 38.92  ? 253 HIS B CA  1 
ATOM   3832 C C   . HIS B  1 238 ? 32.654 -18.829 124.865 1.00 38.19  ? 253 HIS B C   1 
ATOM   3833 O O   . HIS B  1 238 ? 33.397 -18.602 125.831 1.00 39.11  ? 253 HIS B O   1 
ATOM   3834 C CB  . HIS B  1 238 ? 30.375 -19.026 125.949 1.00 38.56  ? 253 HIS B CB  1 
ATOM   3835 C CG  . HIS B  1 238 ? 29.093 -18.342 126.279 1.00 41.93  ? 253 HIS B CG  1 
ATOM   3836 N ND1 . HIS B  1 238 ? 27.967 -19.043 126.665 1.00 44.92  ? 253 HIS B ND1 1 
ATOM   3837 C CD2 . HIS B  1 238 ? 28.734 -17.041 126.235 1.00 44.81  ? 253 HIS B CD2 1 
ATOM   3838 C CE1 . HIS B  1 238 ? 26.980 -18.198 126.873 1.00 44.75  ? 253 HIS B CE1 1 
ATOM   3839 N NE2 . HIS B  1 238 ? 27.422 -16.964 126.614 1.00 44.60  ? 253 HIS B NE2 1 
ATOM   3840 N N   . HIS B  1 239 ? 33.039 -19.508 123.784 1.00 38.37  ? 254 HIS B N   1 
ATOM   3841 C CA  . HIS B  1 239 ? 34.450 -19.904 123.532 1.00 39.73  ? 254 HIS B CA  1 
ATOM   3842 C C   . HIS B  1 239 ? 35.336 -18.655 123.373 1.00 41.09  ? 254 HIS B C   1 
ATOM   3843 O O   . HIS B  1 239 ? 36.509 -18.734 123.755 1.00 42.11  ? 254 HIS B O   1 
ATOM   3844 C CB  . HIS B  1 239 ? 34.556 -20.836 122.325 1.00 41.34  ? 254 HIS B CB  1 
ATOM   3845 C CG  . HIS B  1 239 ? 35.927 -21.376 122.110 1.00 43.49  ? 254 HIS B CG  1 
ATOM   3846 N ND1 . HIS B  1 239 ? 36.319 -22.604 122.602 1.00 47.13  ? 254 HIS B ND1 1 
ATOM   3847 C CD2 . HIS B  1 239 ? 36.998 -20.858 121.469 1.00 44.35  ? 254 HIS B CD2 1 
ATOM   3848 C CE1 . HIS B  1 239 ? 37.573 -22.829 122.258 1.00 47.84  ? 254 HIS B CE1 1 
ATOM   3849 N NE2 . HIS B  1 239 ? 38.017 -21.765 121.570 1.00 47.92  ? 254 HIS B NE2 1 
ATOM   3850 N N   . TYR B  1 240 ? 34.801 -17.558 122.828 1.00 40.86  ? 255 TYR B N   1 
ATOM   3851 C CA  . TYR B  1 240 ? 35.572 -16.344 122.438 1.00 39.21  ? 255 TYR B CA  1 
ATOM   3852 C C   . TYR B  1 240 ? 35.229 -15.150 123.325 1.00 37.27  ? 255 TYR B C   1 
ATOM   3853 O O   . TYR B  1 240 ? 36.155 -14.418 123.682 1.00 36.94  ? 255 TYR B O   1 
ATOM   3854 C CB  . TYR B  1 240 ? 35.326 -16.021 120.964 1.00 38.05  ? 255 TYR B CB  1 
ATOM   3855 C CG  . TYR B  1 240 ? 35.831 -17.094 120.039 1.00 39.22  ? 255 TYR B CG  1 
ATOM   3856 C CD1 . TYR B  1 240 ? 37.189 -17.241 119.800 1.00 39.06  ? 255 TYR B CD1 1 
ATOM   3857 C CD2 . TYR B  1 240 ? 34.962 -17.996 119.446 1.00 37.90  ? 255 TYR B CD2 1 
ATOM   3858 C CE1 . TYR B  1 240 ? 37.670 -18.237 118.967 1.00 39.87  ? 255 TYR B CE1 1 
ATOM   3859 C CE2 . TYR B  1 240 ? 35.428 -19.001 118.615 1.00 37.71  ? 255 TYR B CE2 1 
ATOM   3860 C CZ  . TYR B  1 240 ? 36.784 -19.122 118.375 1.00 39.26  ? 255 TYR B CZ  1 
ATOM   3861 O OH  . TYR B  1 240 ? 37.240 -20.105 117.546 1.00 40.99  ? 255 TYR B OH  1 
ATOM   3862 N N   . VAL B  1 241 ? 33.950 -14.948 123.643 1.00 39.06  ? 256 VAL B N   1 
ATOM   3863 C CA  . VAL B  1 241 ? 33.450 -13.708 124.304 1.00 39.99  ? 256 VAL B CA  1 
ATOM   3864 C C   . VAL B  1 241 ? 33.382 -13.967 125.806 1.00 40.96  ? 256 VAL B C   1 
ATOM   3865 O O   . VAL B  1 241 ? 32.650 -14.854 126.231 1.00 42.35  ? 256 VAL B O   1 
ATOM   3866 C CB  . VAL B  1 241 ? 32.089 -13.264 123.737 1.00 39.31  ? 256 VAL B CB  1 
ATOM   3867 C CG1 . VAL B  1 241 ? 31.622 -11.957 124.360 1.00 39.16  ? 256 VAL B CG1 1 
ATOM   3868 C CG2 . VAL B  1 241 ? 32.125 -13.138 122.221 1.00 39.47  ? 256 VAL B CG2 1 
ATOM   3869 N N   . PRO B  1 242 ? 34.131 -13.210 126.644 1.00 43.99  ? 257 PRO B N   1 
ATOM   3870 C CA  . PRO B  1 242 ? 34.082 -13.390 128.094 1.00 45.81  ? 257 PRO B CA  1 
ATOM   3871 C C   . PRO B  1 242 ? 32.681 -13.134 128.672 1.00 47.68  ? 257 PRO B C   1 
ATOM   3872 O O   . PRO B  1 242 ? 31.989 -12.256 128.176 1.00 49.99  ? 257 PRO B O   1 
ATOM   3873 C CB  . PRO B  1 242 ? 35.071 -12.346 128.650 1.00 44.63  ? 257 PRO B CB  1 
ATOM   3874 C CG  . PRO B  1 242 ? 35.944 -11.970 127.476 1.00 46.84  ? 257 PRO B CG  1 
ATOM   3875 C CD  . PRO B  1 242 ? 35.064 -12.138 126.255 1.00 46.43  ? 257 PRO B CD  1 
ATOM   3876 N N   . LYS B  1 243 ? 32.313 -13.867 129.728 1.00 51.83  ? 258 LYS B N   1 
ATOM   3877 C CA  . LYS B  1 243 ? 31.131 -13.561 130.582 1.00 58.53  ? 258 LYS B CA  1 
ATOM   3878 C C   . LYS B  1 243 ? 31.369 -12.220 131.298 1.00 60.72  ? 258 LYS B C   1 
ATOM   3879 O O   . LYS B  1 243 ? 32.550 -11.830 131.464 1.00 62.35  ? 258 LYS B O   1 
ATOM   3880 C CB  . LYS B  1 243 ? 30.860 -14.702 131.572 1.00 58.19  ? 258 LYS B CB  1 
ATOM   3881 C CG  . LYS B  1 243 ? 30.437 -16.014 130.923 0.00 59.42  ? 258 LYS B CG  1 
ATOM   3882 C CD  . LYS B  1 243 ? 30.143 -17.112 131.923 0.00 59.43  ? 258 LYS B CD  1 
ATOM   3883 C CE  . LYS B  1 243 ? 29.714 -18.409 131.271 0.00 59.36  ? 258 LYS B CE  1 
ATOM   3884 N NZ  . LYS B  1 243 ? 29.465 -19.471 132.275 0.00 59.33  ? 258 LYS B NZ  1 
ATOM   3885 N N   . LYS B  1 244 ? 30.283 -11.537 131.679 1.00 64.64  ? 259 LYS B N   1 
ATOM   3886 C CA  . LYS B  1 244 ? 30.285 -10.183 132.301 1.00 63.44  ? 259 LYS B CA  1 
ATOM   3887 C C   . LYS B  1 244 ? 30.962 -10.242 133.678 1.00 62.56  ? 259 LYS B C   1 
ATOM   3888 O O   . LYS B  1 244 ? 31.961 -9.554  133.914 1.00 59.98  ? 259 LYS B O   1 
ATOM   3889 C CB  . LYS B  1 244 ? 28.849 -9.659  132.426 1.00 62.49  ? 259 LYS B CB  1 
ATOM   3890 C CG  . LYS B  1 244 ? 28.639 -8.277  132.932 0.00 64.09  ? 259 LYS B CG  1 
ATOM   3891 C CD  . LYS B  1 244 ? 27.217 -7.792  132.734 0.00 64.00  ? 259 LYS B CD  1 
ATOM   3892 C CE  . LYS B  1 244 ? 26.887 -6.553  133.535 0.00 63.94  ? 259 LYS B CE  1 
ATOM   3893 N NZ  . LYS B  1 244 ? 25.534 -6.034  133.226 0.00 63.92  ? 259 LYS B NZ  1 
ATOM   3894 N N   . ILE C  1 1   ? 31.939 -19.261 78.825  1.00 38.68  ? 16  ILE C N   1 
ATOM   3895 C CA  . ILE C  1 1   ? 33.191 -20.086 78.817  1.00 36.95  ? 16  ILE C CA  1 
ATOM   3896 C C   . ILE C  1 1   ? 34.393 -19.139 78.918  1.00 36.51  ? 16  ILE C C   1 
ATOM   3897 O O   . ILE C  1 1   ? 34.488 -18.217 78.075  1.00 38.08  ? 16  ILE C O   1 
ATOM   3898 C CB  . ILE C  1 1   ? 33.269 -20.991 77.566  1.00 36.92  ? 16  ILE C CB  1 
ATOM   3899 C CG1 . ILE C  1 1   ? 32.104 -21.986 77.488  1.00 35.76  ? 16  ILE C CG1 1 
ATOM   3900 C CG2 . ILE C  1 1   ? 34.618 -21.699 77.472  1.00 36.72  ? 16  ILE C CG2 1 
ATOM   3901 C CD1 . ILE C  1 1   ? 32.096 -23.047 78.568  1.00 36.16  ? 16  ILE C CD1 1 
ATOM   3902 N N   . VAL C  1 2   ? 35.283 -19.376 79.889  1.00 36.07  ? 17  VAL C N   1 
ATOM   3903 C CA  . VAL C  1 2   ? 36.531 -18.578 80.097  1.00 37.73  ? 17  VAL C CA  1 
ATOM   3904 C C   . VAL C  1 2   ? 37.701 -19.329 79.453  1.00 38.77  ? 17  VAL C C   1 
ATOM   3905 O O   . VAL C  1 2   ? 37.847 -20.532 79.727  1.00 35.22  ? 17  VAL C O   1 
ATOM   3906 C CB  . VAL C  1 2   ? 36.798 -18.305 81.589  1.00 37.58  ? 17  VAL C CB  1 
ATOM   3907 C CG1 . VAL C  1 2   ? 38.030 -17.435 81.798  1.00 38.07  ? 17  VAL C CG1 1 
ATOM   3908 C CG2 . VAL C  1 2   ? 35.592 -17.683 82.267  1.00 38.84  ? 17  VAL C CG2 1 
ATOM   3909 N N   . GLY C  1 3   ? 38.507 -18.622 78.650  1.00 40.82  ? 18  GLY C N   1 
ATOM   3910 C CA  . GLY C  1 3   ? 39.735 -19.137 78.008  1.00 40.41  ? 18  GLY C CA  1 
ATOM   3911 C C   . GLY C  1 3   ? 39.439 -20.155 76.922  1.00 40.49  ? 18  GLY C C   1 
ATOM   3912 O O   . GLY C  1 3   ? 40.333 -20.959 76.615  1.00 41.14  ? 18  GLY C O   1 
ATOM   3913 N N   . GLY C  1 4   ? 38.227 -20.140 76.371  1.00 40.65  ? 19  GLY C N   1 
ATOM   3914 C CA  . GLY C  1 4   ? 37.798 -21.086 75.333  1.00 43.75  ? 19  GLY C CA  1 
ATOM   3915 C C   . GLY C  1 4   ? 38.066 -20.543 73.943  1.00 45.47  ? 19  GLY C C   1 
ATOM   3916 O O   . GLY C  1 4   ? 38.677 -19.460 73.819  1.00 48.46  ? 19  GLY C O   1 
ATOM   3917 N N   . GLN C  1 5   ? 37.619 -21.286 72.935  1.00 44.08  ? 20  GLN C N   1 
ATOM   3918 C CA  . GLN C  1 5   ? 37.568 -20.873 71.513  1.00 44.70  ? 20  GLN C CA  1 
ATOM   3919 C C   . GLN C  1 5   ? 36.167 -21.168 70.986  1.00 42.60  ? 20  GLN C C   1 
ATOM   3920 O O   . GLN C  1 5   ? 35.448 -21.940 71.646  1.00 40.23  ? 20  GLN C O   1 
ATOM   3921 C CB  . GLN C  1 5   ? 38.620 -21.639 70.713  1.00 45.33  ? 20  GLN C CB  1 
ATOM   3922 C CG  . GLN C  1 5   ? 40.037 -21.246 71.095  1.00 48.66  ? 20  GLN C CG  1 
ATOM   3923 C CD  . GLN C  1 5   ? 41.067 -22.271 70.698  1.00 48.47  ? 20  GLN C CD  1 
ATOM   3924 O OE1 . GLN C  1 5   ? 40.776 -23.453 70.528  1.00 55.50  ? 20  GLN C OE1 1 
ATOM   3925 N NE2 . GLN C  1 5   ? 42.302 -21.822 70.585  1.00 46.59  ? 20  GLN C NE2 1 
ATOM   3926 N N   . GLU C  1 6   ? 35.809 -20.576 69.849  1.00 40.87  ? 21  GLU C N   1 
ATOM   3927 C CA  . GLU C  1 6   ? 34.556 -20.894 69.118  1.00 42.50  ? 21  GLU C CA  1 
ATOM   3928 C C   . GLU C  1 6   ? 34.608 -22.377 68.742  1.00 40.35  ? 21  GLU C C   1 
ATOM   3929 O O   . GLU C  1 6   ? 35.669 -22.831 68.266  1.00 40.63  ? 21  GLU C O   1 
ATOM   3930 C CB  . GLU C  1 6   ? 34.377 -19.995 67.888  1.00 43.11  ? 21  GLU C CB  1 
ATOM   3931 C CG  . GLU C  1 6   ? 33.137 -20.334 67.065  1.00 45.64  ? 21  GLU C CG  1 
ATOM   3932 C CD  . GLU C  1 6   ? 32.662 -19.296 66.053  1.00 45.18  ? 21  GLU C CD  1 
ATOM   3933 O OE1 . GLU C  1 6   ? 31.646 -19.572 65.367  1.00 42.11  ? 21  GLU C OE1 1 
ATOM   3934 O OE2 . GLU C  1 6   ? 33.291 -18.215 65.957  1.00 40.66  ? 21  GLU C OE2 1 
ATOM   3935 N N   . ALA C  1 7   ? 33.523 -23.108 68.998  1.00 39.75  ? 22  ALA C N   1 
ATOM   3936 C CA  . ALA C  1 7   ? 33.366 -24.534 68.634  1.00 39.80  ? 22  ALA C CA  1 
ATOM   3937 C C   . ALA C  1 7   ? 33.306 -24.653 67.114  1.00 42.17  ? 22  ALA C C   1 
ATOM   3938 O O   . ALA C  1 7   ? 32.656 -23.835 66.467  1.00 42.05  ? 22  ALA C O   1 
ATOM   3939 C CB  . ALA C  1 7   ? 32.112 -25.095 69.259  1.00 39.44  ? 22  ALA C CB  1 
ATOM   3940 N N   . PRO C  1 8   ? 33.955 -25.663 66.487  1.00 41.80  ? 23  PRO C N   1 
ATOM   3941 C CA  . PRO C  1 8   ? 33.637 -26.015 65.104  1.00 42.73  ? 23  PRO C CA  1 
ATOM   3942 C C   . PRO C  1 8   ? 32.162 -26.432 64.984  1.00 42.52  ? 23  PRO C C   1 
ATOM   3943 O O   . PRO C  1 8   ? 31.625 -26.990 65.942  1.00 43.95  ? 23  PRO C O   1 
ATOM   3944 C CB  . PRO C  1 8   ? 34.592 -27.170 64.756  1.00 41.73  ? 23  PRO C CB  1 
ATOM   3945 C CG  . PRO C  1 8   ? 35.656 -27.150 65.840  1.00 41.53  ? 23  PRO C CG  1 
ATOM   3946 C CD  . PRO C  1 8   ? 35.015 -26.509 67.055  1.00 41.54  ? 23  PRO C CD  1 
ATOM   3947 N N   . ARG C  1 9   ? 31.557 -26.165 63.822  1.00 41.69  ? 24  ARG C N   1 
ATOM   3948 C CA  . ARG C  1 9   ? 30.129 -26.451 63.499  1.00 42.53  ? 24  ARG C CA  1 
ATOM   3949 C C   . ARG C  1 9   ? 29.792 -27.934 63.715  1.00 40.34  ? 24  ARG C C   1 
ATOM   3950 O O   . ARG C  1 9   ? 28.629 -28.210 64.061  1.00 39.35  ? 24  ARG C O   1 
ATOM   3951 C CB  . ARG C  1 9   ? 29.824 -26.073 62.046  1.00 47.68  ? 24  ARG C CB  1 
ATOM   3952 C CG  . ARG C  1 9   ? 29.862 -24.578 61.781  1.00 52.43  ? 24  ARG C CG  1 
ATOM   3953 C CD  . ARG C  1 9   ? 29.214 -24.185 60.465  1.00 53.50  ? 24  ARG C CD  1 
ATOM   3954 N NE  . ARG C  1 9   ? 28.971 -22.750 60.498  1.00 58.43  ? 24  ARG C NE  1 
ATOM   3955 C CZ  . ARG C  1 9   ? 27.848 -22.151 60.905  1.00 56.51  ? 24  ARG C CZ  1 
ATOM   3956 N NH1 . ARG C  1 9   ? 26.792 -22.851 61.295  1.00 54.22  ? 24  ARG C NH1 1 
ATOM   3957 N NH2 . ARG C  1 9   ? 27.781 -20.828 60.897  1.00 56.65  ? 24  ARG C NH2 1 
ATOM   3958 N N   . SER C  1 10  ? 30.747 -28.848 63.501  1.00 40.84  ? 25  SER C N   1 
ATOM   3959 C CA  . SER C  1 10  ? 30.539 -30.322 63.594  1.00 44.40  ? 25  SER C CA  1 
ATOM   3960 C C   . SER C  1 10  ? 30.529 -30.809 65.051  1.00 43.51  ? 25  SER C C   1 
ATOM   3961 O O   . SER C  1 10  ? 30.058 -31.939 65.264  1.00 47.39  ? 25  SER C O   1 
ATOM   3962 C CB  . SER C  1 10  ? 31.572 -31.074 62.790  1.00 46.10  ? 25  SER C CB  1 
ATOM   3963 O OG  . SER C  1 10  ? 32.883 -30.777 63.253  1.00 47.53  ? 25  SER C OG  1 
ATOM   3964 N N   . LYS C  1 11  ? 31.003 -30.006 66.017  1.00 42.67  ? 26  LYS C N   1 
ATOM   3965 C CA  . LYS C  1 11  ? 31.222 -30.450 67.423  1.00 41.94  ? 26  LYS C CA  1 
ATOM   3966 C C   . LYS C  1 11  ? 30.006 -30.120 68.296  1.00 40.61  ? 26  LYS C C   1 
ATOM   3967 O O   . LYS C  1 11  ? 29.339 -29.097 68.043  1.00 38.73  ? 26  LYS C O   1 
ATOM   3968 C CB  . LYS C  1 11  ? 32.471 -29.799 68.025  1.00 43.09  ? 26  LYS C CB  1 
ATOM   3969 C CG  . LYS C  1 11  ? 33.757 -29.961 67.224  1.00 45.57  ? 26  LYS C CG  1 
ATOM   3970 C CD  . LYS C  1 11  ? 34.040 -31.373 66.760  1.00 47.64  ? 26  LYS C CD  1 
ATOM   3971 C CE  . LYS C  1 11  ? 35.434 -31.547 66.192  1.00 49.90  ? 26  LYS C CE  1 
ATOM   3972 N NZ  . LYS C  1 11  ? 35.621 -32.913 65.651  1.00 50.21  ? 26  LYS C NZ  1 
ATOM   3973 N N   . TRP C  1 12  ? 29.760 -30.967 69.299  1.00 37.98  ? 27  TRP C N   1 
ATOM   3974 C CA  . TRP C  1 12  ? 28.772 -30.782 70.397  1.00 36.45  ? 27  TRP C CA  1 
ATOM   3975 C C   . TRP C  1 12  ? 27.351 -30.709 69.837  1.00 36.56  ? 27  TRP C C   1 
ATOM   3976 O O   . TRP C  1 12  ? 26.640 -29.730 70.062  1.00 37.38  ? 27  TRP C O   1 
ATOM   3977 C CB  . TRP C  1 12  ? 29.129 -29.544 71.233  1.00 36.65  ? 27  TRP C CB  1 
ATOM   3978 C CG  . TRP C  1 12  ? 30.594 -29.243 71.315  1.00 36.29  ? 27  TRP C CG  1 
ATOM   3979 C CD1 . TRP C  1 12  ? 31.201 -28.089 70.919  1.00 36.88  ? 27  TRP C CD1 1 
ATOM   3980 C CD2 . TRP C  1 12  ? 31.644 -30.102 71.800  1.00 36.81  ? 27  TRP C CD2 1 
ATOM   3981 N NE1 . TRP C  1 12  ? 32.548 -28.158 71.144  1.00 37.25  ? 27  TRP C NE1 1 
ATOM   3982 C CE2 . TRP C  1 12  ? 32.852 -29.378 71.686  1.00 35.95  ? 27  TRP C CE2 1 
ATOM   3983 C CE3 . TRP C  1 12  ? 31.684 -31.396 72.340  1.00 35.78  ? 27  TRP C CE3 1 
ATOM   3984 C CZ2 . TRP C  1 12  ? 34.081 -29.909 72.080  1.00 35.59  ? 27  TRP C CZ2 1 
ATOM   3985 C CZ3 . TRP C  1 12  ? 32.900 -31.923 72.723  1.00 36.07  ? 27  TRP C CZ3 1 
ATOM   3986 C CH2 . TRP C  1 12  ? 34.080 -31.188 72.595  1.00 36.09  ? 27  TRP C CH2 1 
ATOM   3987 N N   . PRO C  1 13  ? 26.882 -31.740 69.094  1.00 36.34  ? 28  PRO C N   1 
ATOM   3988 C CA  . PRO C  1 13  ? 25.535 -31.726 68.511  1.00 35.50  ? 28  PRO C CA  1 
ATOM   3989 C C   . PRO C  1 13  ? 24.383 -31.854 69.526  1.00 36.03  ? 28  PRO C C   1 
ATOM   3990 O O   . PRO C  1 13  ? 23.232 -31.704 69.132  1.00 36.83  ? 28  PRO C O   1 
ATOM   3991 C CB  . PRO C  1 13  ? 25.575 -32.922 67.544  1.00 37.40  ? 28  PRO C CB  1 
ATOM   3992 C CG  . PRO C  1 13  ? 26.571 -33.879 68.176  1.00 37.17  ? 28  PRO C CG  1 
ATOM   3993 C CD  . PRO C  1 13  ? 27.625 -32.971 68.771  1.00 38.04  ? 28  PRO C CD  1 
ATOM   3994 N N   . TRP C  1 14  ? 24.711 -32.086 70.801  1.00 34.77  ? 29  TRP C N   1 
ATOM   3995 C CA  . TRP C  1 14  ? 23.762 -32.264 71.938  1.00 35.63  ? 29  TRP C CA  1 
ATOM   3996 C C   . TRP C  1 14  ? 23.566 -30.957 72.723  1.00 35.24  ? 29  TRP C C   1 
ATOM   3997 O O   . TRP C  1 14  ? 22.634 -30.923 73.555  1.00 35.91  ? 29  TRP C O   1 
ATOM   3998 C CB  . TRP C  1 14  ? 24.255 -33.378 72.875  1.00 34.90  ? 29  TRP C CB  1 
ATOM   3999 C CG  . TRP C  1 14  ? 25.711 -33.273 73.190  1.00 35.34  ? 29  TRP C CG  1 
ATOM   4000 C CD1 . TRP C  1 14  ? 26.314 -32.366 74.011  1.00 36.07  ? 29  TRP C CD1 1 
ATOM   4001 C CD2 . TRP C  1 14  ? 26.763 -34.091 72.649  1.00 35.41  ? 29  TRP C CD2 1 
ATOM   4002 N NE1 . TRP C  1 14  ? 27.669 -32.572 74.024  1.00 37.72  ? 29  TRP C NE1 1 
ATOM   4003 C CE2 . TRP C  1 14  ? 27.973 -33.625 73.202  1.00 35.41  ? 29  TRP C CE2 1 
ATOM   4004 C CE3 . TRP C  1 14  ? 26.798 -35.166 71.755  1.00 35.31  ? 29  TRP C CE3 1 
ATOM   4005 C CZ2 . TRP C  1 14  ? 29.201 -34.205 72.894  1.00 36.86  ? 29  TRP C CZ2 1 
ATOM   4006 C CZ3 . TRP C  1 14  ? 28.013 -35.736 71.447  1.00 35.78  ? 29  TRP C CZ3 1 
ATOM   4007 C CH2 . TRP C  1 14  ? 29.197 -35.262 72.011  1.00 36.84  ? 29  TRP C CH2 1 
ATOM   4008 N N   . GLN C  1 15  ? 24.410 -29.936 72.514  1.00 35.39  ? 30  GLN C N   1 
ATOM   4009 C CA  . GLN C  1 15  ? 24.330 -28.633 73.240  1.00 35.64  ? 30  GLN C CA  1 
ATOM   4010 C C   . GLN C  1 15  ? 22.977 -27.987 72.928  1.00 35.53  ? 30  GLN C C   1 
ATOM   4011 O O   . GLN C  1 15  ? 22.615 -27.946 71.735  1.00 39.27  ? 30  GLN C O   1 
ATOM   4012 C CB  . GLN C  1 15  ? 25.477 -27.701 72.839  1.00 35.56  ? 30  GLN C CB  1 
ATOM   4013 C CG  . GLN C  1 15  ? 25.458 -26.345 73.544  1.00 36.54  ? 30  GLN C CG  1 
ATOM   4014 C CD  . GLN C  1 15  ? 25.858 -26.410 75.002  1.00 35.72  ? 30  GLN C CD  1 
ATOM   4015 O OE1 . GLN C  1 15  ? 26.884 -26.980 75.359  1.00 36.10  ? 30  GLN C OE1 1 
ATOM   4016 N NE2 . GLN C  1 15  ? 25.065 -25.797 75.867  1.00 35.25  ? 30  GLN C NE2 1 
ATOM   4017 N N   . VAL C  1 16  ? 22.247 -27.543 73.958  1.00 35.07  ? 31  VAL C N   1 
ATOM   4018 C CA  . VAL C  1 16  ? 20.987 -26.760 73.784  1.00 35.68  ? 31  VAL C CA  1 
ATOM   4019 C C   . VAL C  1 16  ? 21.100 -25.463 74.592  1.00 34.31  ? 31  VAL C C   1 
ATOM   4020 O O   . VAL C  1 16  ? 21.921 -25.402 75.522  1.00 35.18  ? 31  VAL C O   1 
ATOM   4021 C CB  . VAL C  1 16  ? 19.720 -27.570 74.127  1.00 37.30  ? 31  VAL C CB  1 
ATOM   4022 C CG1 . VAL C  1 16  ? 19.787 -28.992 73.579  1.00 38.00  ? 31  VAL C CG1 1 
ATOM   4023 C CG2 . VAL C  1 16  ? 19.408 -27.594 75.609  1.00 38.09  ? 31  VAL C CG2 1 
ATOM   4024 N N   . SER C  1 17  ? 20.319 -24.463 74.190  1.00 32.88  ? 32  SER C N   1 
ATOM   4025 C CA  . SER C  1 17  ? 20.140 -23.156 74.863  1.00 33.62  ? 32  SER C CA  1 
ATOM   4026 C C   . SER C  1 17  ? 18.730 -23.121 75.466  1.00 32.51  ? 32  SER C C   1 
ATOM   4027 O O   . SER C  1 17  ? 17.780 -23.457 74.739  1.00 32.76  ? 32  SER C O   1 
ATOM   4028 C CB  . SER C  1 17  ? 20.383 -22.033 73.871  1.00 33.91  ? 32  SER C CB  1 
ATOM   4029 O OG  . SER C  1 17  ? 19.920 -20.790 74.368  1.00 33.81  ? 32  SER C OG  1 
ATOM   4030 N N   . LEU C  1 18  ? 18.600 -22.763 76.747  1.00 31.88  ? 33  LEU C N   1 
ATOM   4031 C CA  . LEU C  1 18  ? 17.288 -22.539 77.412  1.00 32.55  ? 33  LEU C CA  1 
ATOM   4032 C C   . LEU C  1 18  ? 16.955 -21.054 77.288  1.00 31.42  ? 33  LEU C C   1 
ATOM   4033 O O   . LEU C  1 18  ? 17.838 -20.228 77.585  1.00 29.72  ? 33  LEU C O   1 
ATOM   4034 C CB  . LEU C  1 18  ? 17.323 -22.979 78.881  1.00 32.74  ? 33  LEU C CB  1 
ATOM   4035 C CG  . LEU C  1 18  ? 17.829 -24.395 79.177  1.00 35.47  ? 33  LEU C CG  1 
ATOM   4036 C CD1 . LEU C  1 18  ? 17.451 -24.807 80.605  1.00 36.31  ? 33  LEU C CD1 1 
ATOM   4037 C CD2 . LEU C  1 18  ? 17.295 -25.410 78.179  1.00 36.14  ? 33  LEU C CD2 1 
ATOM   4038 N N   . ARG C  1 19  ? 15.718 -20.745 76.893  1.00 31.58  ? 34  ARG C N   1 
ATOM   4039 C CA  . ARG C  1 19  ? 15.254 -19.369 76.592  1.00 33.22  ? 34  ARG C CA  1 
ATOM   4040 C C   . ARG C  1 19  ? 14.077 -19.023 77.499  1.00 33.05  ? 34  ARG C C   1 
ATOM   4041 O O   . ARG C  1 19  ? 13.193 -19.884 77.688  1.00 32.82  ? 34  ARG C O   1 
ATOM   4042 C CB  . ARG C  1 19  ? 14.857 -19.232 75.122  1.00 33.58  ? 34  ARG C CB  1 
ATOM   4043 C CG  . ARG C  1 19  ? 15.934 -19.664 74.140  1.00 33.51  ? 34  ARG C CG  1 
ATOM   4044 C CD  . ARG C  1 19  ? 17.225 -18.871 74.275  1.00 33.45  ? 34  ARG C CD  1 
ATOM   4045 N NE  . ARG C  1 19  ? 18.084 -19.130 73.133  1.00 34.33  ? 34  ARG C NE  1 
ATOM   4046 C CZ  . ARG C  1 19  ? 17.895 -18.660 71.892  1.00 32.99  ? 34  ARG C CZ  1 
ATOM   4047 N NH1 . ARG C  1 19  ? 16.882 -17.848 71.616  1.00 32.40  ? 34  ARG C NH1 1 
ATOM   4048 N NH2 . ARG C  1 19  ? 18.736 -19.011 70.932  1.00 30.29  ? 34  ARG C NH2 1 
ATOM   4049 N N   . VAL C  1 20  ? 14.101 -17.805 78.044  1.00 34.72  ? 35  VAL C N   1 
ATOM   4050 C CA  . VAL C  1 20  ? 13.051 -17.242 78.940  1.00 35.12  ? 35  VAL C CA  1 
ATOM   4051 C C   . VAL C  1 20  ? 12.341 -16.122 78.171  1.00 37.43  ? 35  VAL C C   1 
ATOM   4052 O O   . VAL C  1 20  ? 13.035 -15.350 77.473  1.00 35.56  ? 35  VAL C O   1 
ATOM   4053 C CB  . VAL C  1 20  ? 13.629 -16.765 80.290  1.00 34.57  ? 35  VAL C CB  1 
ATOM   4054 C CG1 . VAL C  1 20  ? 14.701 -15.689 80.155  1.00 34.08  ? 35  VAL C CG1 1 
ATOM   4055 C CG2 . VAL C  1 20  ? 12.533 -16.291 81.233  1.00 36.96  ? 35  VAL C CG2 1 
ATOM   4056 N N   . HIS C  1 21  ? 11.012 -16.044 78.291  1.00 41.97  ? 36  HIS C N   1 
ATOM   4057 C CA  . HIS C  1 21  ? 10.171 -15.025 77.606  1.00 46.84  ? 36  HIS C CA  1 
ATOM   4058 C C   . HIS C  1 21  ? 10.463 -13.643 78.199  1.00 46.20  ? 36  HIS C C   1 
ATOM   4059 O O   . HIS C  1 21  ? 10.457 -13.520 79.429  1.00 50.15  ? 36  HIS C O   1 
ATOM   4060 C CB  . HIS C  1 21  ? 8.674  -15.370 77.702  1.00 49.10  ? 36  HIS C CB  1 
ATOM   4061 C CG  . HIS C  1 21  ? 7.782  -14.392 77.011  1.00 52.72  ? 36  HIS C CG  1 
ATOM   4062 N ND1 . HIS C  1 21  ? 7.661  -14.339 75.632  1.00 55.14  ? 36  HIS C ND1 1 
ATOM   4063 C CD2 . HIS C  1 21  ? 6.970  -13.427 77.499  1.00 56.27  ? 36  HIS C CD2 1 
ATOM   4064 C CE1 . HIS C  1 21  ? 6.811  -13.391 75.303  1.00 56.13  ? 36  HIS C CE1 1 
ATOM   4065 N NE2 . HIS C  1 21  ? 6.374  -12.812 76.431  1.00 58.25  ? 36  HIS C NE2 1 
ATOM   4066 N N   . GLY C  1 22  ? 10.720 -12.656 77.345  1.00 48.08  ? 37  GLY C N   1 
ATOM   4067 C CA  . GLY C  1 22  ? 10.852 -11.239 77.731  1.00 48.13  ? 37  GLY C CA  1 
ATOM   4068 C C   . GLY C  1 22  ? 10.682 -10.341 76.512  1.00 47.79  ? 37  GLY C C   1 
ATOM   4069 O O   . GLY C  1 22  ? 9.905  -10.671 75.618  1.00 48.02  ? 37  GLY C O   1 
ATOM   4070 N N   . PRO C  1 23  ? 11.397 -9.195  76.436  1.00 46.32  ? 38  PRO C N   1 
ATOM   4071 C CA  . PRO C  1 23  ? 11.497 -8.424  75.194  1.00 44.53  ? 38  PRO C CA  1 
ATOM   4072 C C   . PRO C  1 23  ? 11.899 -9.296  73.994  1.00 44.64  ? 38  PRO C C   1 
ATOM   4073 O O   . PRO C  1 23  ? 11.441 -9.035  72.891  1.00 47.32  ? 38  PRO C O   1 
ATOM   4074 C CB  . PRO C  1 23  ? 12.589 -7.395  75.519  1.00 45.10  ? 38  PRO C CB  1 
ATOM   4075 C CG  . PRO C  1 23  ? 12.476 -7.200  77.010  1.00 45.37  ? 38  PRO C CG  1 
ATOM   4076 C CD  . PRO C  1 23  ? 12.136 -8.573  77.547  1.00 46.54  ? 38  PRO C CD  1 
ATOM   4077 N N   . TYR C  1 24  ? 12.752 -10.299 74.237  1.00 40.50  ? 39  TYR C N   1 
ATOM   4078 C CA  . TYR C  1 24  ? 13.067 -11.410 73.303  1.00 37.03  ? 39  TYR C CA  1 
ATOM   4079 C C   . TYR C  1 24  ? 13.258 -12.712 74.099  1.00 36.81  ? 39  TYR C C   1 
ATOM   4080 O O   . TYR C  1 24  ? 13.267 -12.673 75.339  1.00 36.71  ? 39  TYR C O   1 
ATOM   4081 C CB  . TYR C  1 24  ? 14.297 -11.067 72.462  1.00 36.56  ? 39  TYR C CB  1 
ATOM   4082 C CG  . TYR C  1 24  ? 15.583 -10.902 73.232  1.00 36.25  ? 39  TYR C CG  1 
ATOM   4083 C CD1 . TYR C  1 24  ? 15.853 -9.744  73.949  1.00 36.08  ? 39  TYR C CD1 1 
ATOM   4084 C CD2 . TYR C  1 24  ? 16.548 -11.898 73.225  1.00 36.49  ? 39  TYR C CD2 1 
ATOM   4085 C CE1 . TYR C  1 24  ? 17.045 -9.581  74.641  1.00 34.62  ? 39  TYR C CE1 1 
ATOM   4086 C CE2 . TYR C  1 24  ? 17.741 -11.754 73.915  1.00 35.41  ? 39  TYR C CE2 1 
ATOM   4087 C CZ  . TYR C  1 24  ? 17.990 -10.594 74.627  1.00 35.63  ? 39  TYR C CZ  1 
ATOM   4088 O OH  . TYR C  1 24  ? 19.172 -10.463 75.292  1.00 36.55  ? 39  TYR C OH  1 
ATOM   4089 N N   . TRP C  1 25  ? 13.383 -13.835 73.390  1.00 35.91  ? 40  TRP C N   1 
ATOM   4090 C CA  . TRP C  1 25  ? 13.608 -15.180 73.981  1.00 35.87  ? 40  TRP C CA  1 
ATOM   4091 C C   . TRP C  1 25  ? 15.087 -15.302 74.340  1.00 34.29  ? 40  TRP C C   1 
ATOM   4092 O O   . TRP C  1 25  ? 15.868 -15.770 73.501  1.00 34.41  ? 40  TRP C O   1 
ATOM   4093 C CB  . TRP C  1 25  ? 13.132 -16.288 73.037  1.00 37.09  ? 40  TRP C CB  1 
ATOM   4094 C CG  . TRP C  1 25  ? 11.643 -16.414 73.030  1.00 38.87  ? 40  TRP C CG  1 
ATOM   4095 C CD1 . TRP C  1 25  ? 10.776 -15.881 72.123  1.00 39.43  ? 40  TRP C CD1 1 
ATOM   4096 C CD2 . TRP C  1 25  ? 10.838 -17.117 73.991  1.00 39.72  ? 40  TRP C CD2 1 
ATOM   4097 N NE1 . TRP C  1 25  ? 9.489  -16.215 72.443  1.00 38.72  ? 40  TRP C NE1 1 
ATOM   4098 C CE2 . TRP C  1 25  ? 9.493  -16.971 73.585  1.00 40.77  ? 40  TRP C CE2 1 
ATOM   4099 C CE3 . TRP C  1 25  ? 11.122 -17.864 75.142  1.00 39.17  ? 40  TRP C CE3 1 
ATOM   4100 C CZ2 . TRP C  1 25  ? 8.435  -17.538 74.298  1.00 40.92  ? 40  TRP C CZ2 1 
ATOM   4101 C CZ3 . TRP C  1 25  ? 10.078 -18.425 75.844  1.00 40.31  ? 40  TRP C CZ3 1 
ATOM   4102 C CH2 . TRP C  1 25  ? 8.755  -18.266 75.425  1.00 42.67  ? 40  TRP C CH2 1 
ATOM   4103 N N   . MET C  1 26  ? 15.434 -14.867 75.551  1.00 34.61  ? 41  MET C N   1 
ATOM   4104 C CA  . MET C  1 26  ? 16.829 -14.658 75.999  1.00 33.75  ? 41  MET C CA  1 
ATOM   4105 C C   . MET C  1 26  ? 17.399 -15.972 76.549  1.00 31.70  ? 41  MET C C   1 
ATOM   4106 O O   . MET C  1 26  ? 16.716 -16.638 77.342  1.00 29.50  ? 41  MET C O   1 
ATOM   4107 C CB  . MET C  1 26  ? 16.875 -13.574 77.079  1.00 35.76  ? 41  MET C CB  1 
ATOM   4108 C CG  . MET C  1 26  ? 18.279 -13.127 77.431  1.00 40.39  ? 41  MET C CG  1 
ATOM   4109 S SD  . MET C  1 26  ? 18.309 -11.690 78.533  1.00 46.20  ? 41  MET C SD  1 
ATOM   4110 C CE  . MET C  1 26  ? 17.487 -12.345 79.985  1.00 45.92  ? 41  MET C CE  1 
ATOM   4111 N N   . HIS C  1 27  ? 18.619 -16.306 76.136  1.00 31.88  ? 42  HIS C N   1 
ATOM   4112 C CA  . HIS C  1 27  ? 19.461 -17.372 76.729  1.00 32.96  ? 42  HIS C CA  1 
ATOM   4113 C C   . HIS C  1 27  ? 19.727 -17.045 78.204  1.00 36.16  ? 42  HIS C C   1 
ATOM   4114 O O   . HIS C  1 27  ? 20.160 -15.915 78.484  1.00 36.72  ? 42  HIS C O   1 
ATOM   4115 C CB  . HIS C  1 27  ? 20.769 -17.526 75.945  1.00 33.69  ? 42  HIS C CB  1 
ATOM   4116 C CG  . HIS C  1 27  ? 21.712 -18.483 76.590  1.00 33.86  ? 42  HIS C CG  1 
ATOM   4117 N ND1 . HIS C  1 27  ? 21.710 -19.831 76.302  1.00 32.10  ? 42  HIS C ND1 1 
ATOM   4118 C CD2 . HIS C  1 27  ? 22.635 -18.295 77.559  1.00 33.50  ? 42  HIS C CD2 1 
ATOM   4119 C CE1 . HIS C  1 27  ? 22.625 -20.430 77.034  1.00 31.73  ? 42  HIS C CE1 1 
ATOM   4120 N NE2 . HIS C  1 27  ? 23.205 -19.507 77.821  1.00 31.54  ? 42  HIS C NE2 1 
ATOM   4121 N N   . PHE C  1 28  ? 19.448 -17.989 79.107  1.00 35.46  ? 43  PHE C N   1 
ATOM   4122 C CA  . PHE C  1 28  ? 19.797 -17.910 80.551  1.00 35.64  ? 43  PHE C CA  1 
ATOM   4123 C C   . PHE C  1 28  ? 20.633 -19.125 80.995  1.00 35.59  ? 43  PHE C C   1 
ATOM   4124 O O   . PHE C  1 28  ? 21.391 -18.969 81.962  1.00 37.46  ? 43  PHE C O   1 
ATOM   4125 C CB  . PHE C  1 28  ? 18.537 -17.733 81.408  1.00 33.86  ? 43  PHE C CB  1 
ATOM   4126 C CG  . PHE C  1 28  ? 17.577 -18.897 81.398  1.00 34.48  ? 43  PHE C CG  1 
ATOM   4127 C CD1 . PHE C  1 28  ? 17.707 -19.934 82.312  1.00 34.33  ? 43  PHE C CD1 1 
ATOM   4128 C CD2 . PHE C  1 28  ? 16.531 -18.948 80.486  1.00 32.68  ? 43  PHE C CD2 1 
ATOM   4129 C CE1 . PHE C  1 28  ? 16.829 -21.008 82.296  1.00 34.57  ? 43  PHE C CE1 1 
ATOM   4130 C CE2 . PHE C  1 28  ? 15.645 -20.015 80.483  1.00 32.99  ? 43  PHE C CE2 1 
ATOM   4131 C CZ  . PHE C  1 28  ? 15.803 -21.050 81.380  1.00 34.18  ? 43  PHE C CZ  1 
ATOM   4132 N N   . CYS C  1 29  ? 20.508 -20.292 80.352  1.00 36.34  ? 44  CYS C N   1 
ATOM   4133 C CA  . CYS C  1 29  ? 21.196 -21.545 80.778  1.00 37.40  ? 44  CYS C CA  1 
ATOM   4134 C C   . CYS C  1 29  ? 21.405 -22.480 79.584  1.00 34.39  ? 44  CYS C C   1 
ATOM   4135 O O   . CYS C  1 29  ? 20.705 -22.339 78.573  1.00 37.26  ? 44  CYS C O   1 
ATOM   4136 C CB  . CYS C  1 29  ? 20.411 -22.285 81.862  1.00 36.78  ? 44  CYS C CB  1 
ATOM   4137 S SG  . CYS C  1 29  ? 20.821 -21.780 83.555  1.00 44.16  ? 44  CYS C SG  1 
ATOM   4138 N N   . GLY C  1 30  ? 22.352 -23.397 79.730  1.00 34.56  ? 45  GLY C N   1 
ATOM   4139 C CA  . GLY C  1 30  ? 22.611 -24.490 78.784  1.00 33.14  ? 45  GLY C CA  1 
ATOM   4140 C C   . GLY C  1 30  ? 21.889 -25.756 79.196  1.00 31.17  ? 45  GLY C C   1 
ATOM   4141 O O   . GLY C  1 30  ? 21.195 -25.761 80.225  1.00 32.94  ? 45  GLY C O   1 
ATOM   4142 N N   . GLY C  1 31  ? 22.061 -26.791 78.386  1.00 31.37  ? 46  GLY C N   1 
ATOM   4143 C CA  . GLY C  1 31  ? 21.479 -28.132 78.555  1.00 30.82  ? 46  GLY C CA  1 
ATOM   4144 C C   . GLY C  1 31  ? 22.152 -29.106 77.610  1.00 30.17  ? 46  GLY C C   1 
ATOM   4145 O O   . GLY C  1 31  ? 22.973 -28.664 76.786  1.00 30.08  ? 46  GLY C O   1 
ATOM   4146 N N   . SER C  1 32  ? 21.817 -30.385 77.720  1.00 31.53  ? 47  SER C N   1 
ATOM   4147 C CA  . SER C  1 32  ? 22.264 -31.439 76.784  1.00 32.03  ? 47  SER C CA  1 
ATOM   4148 C C   . SER C  1 32  ? 21.056 -32.281 76.374  1.00 33.20  ? 47  SER C C   1 
ATOM   4149 O O   . SER C  1 32  ? 20.200 -32.556 77.233  1.00 34.86  ? 47  SER C O   1 
ATOM   4150 C CB  . SER C  1 32  ? 23.362 -32.268 77.381  1.00 31.98  ? 47  SER C CB  1 
ATOM   4151 O OG  . SER C  1 32  ? 22.959 -32.821 78.619  1.00 33.50  ? 47  SER C OG  1 
ATOM   4152 N N   . LEU C  1 33  ? 20.981 -32.633 75.092  1.00 33.91  ? 48  LEU C N   1 
ATOM   4153 C CA  . LEU C  1 33  ? 19.990 -33.606 74.577  1.00 36.82  ? 48  LEU C CA  1 
ATOM   4154 C C   . LEU C  1 33  ? 20.514 -35.011 74.907  1.00 34.71  ? 48  LEU C C   1 
ATOM   4155 O O   . LEU C  1 33  ? 21.557 -35.388 74.365  1.00 36.04  ? 48  LEU C O   1 
ATOM   4156 C CB  . LEU C  1 33  ? 19.807 -33.376 73.076  1.00 37.34  ? 48  LEU C CB  1 
ATOM   4157 C CG  . LEU C  1 33  ? 18.650 -34.136 72.437  1.00 37.94  ? 48  LEU C CG  1 
ATOM   4158 C CD1 . LEU C  1 33  ? 17.322 -33.487 72.795  1.00 37.84  ? 48  LEU C CD1 1 
ATOM   4159 C CD2 . LEU C  1 33  ? 18.838 -34.212 70.929  1.00 38.31  ? 48  LEU C CD2 1 
ATOM   4160 N N   . ILE C  1 34  ? 19.849 -35.718 75.820  1.00 35.63  ? 49  ILE C N   1 
ATOM   4161 C CA  . ILE C  1 34  ? 20.245 -37.089 76.276  1.00 36.57  ? 49  ILE C CA  1 
ATOM   4162 C C   . ILE C  1 34  ? 19.301 -38.145 75.675  1.00 36.78  ? 49  ILE C C   1 
ATOM   4163 O O   . ILE C  1 34  ? 19.555 -39.349 75.854  1.00 39.40  ? 49  ILE C O   1 
ATOM   4164 C CB  . ILE C  1 34  ? 20.300 -37.153 77.816  1.00 33.24  ? 49  ILE C CB  1 
ATOM   4165 C CG1 . ILE C  1 34  ? 18.984 -36.748 78.481  1.00 33.89  ? 49  ILE C CG1 1 
ATOM   4166 C CG2 . ILE C  1 34  ? 21.461 -36.320 78.336  1.00 35.06  ? 49  ILE C CG2 1 
ATOM   4167 C CD1 . ILE C  1 34  ? 18.795 -37.340 79.848  1.00 34.66  ? 49  ILE C CD1 1 
ATOM   4168 N N   . HIS C  1 35  ? 18.251 -37.704 74.991  1.00 37.52  ? 50  HIS C N   1 
ATOM   4169 C CA  . HIS C  1 35  ? 17.200 -38.538 74.357  1.00 40.07  ? 50  HIS C CA  1 
ATOM   4170 C C   . HIS C  1 35  ? 16.466 -37.607 73.400  1.00 39.77  ? 50  HIS C C   1 
ATOM   4171 O O   . HIS C  1 35  ? 16.407 -36.407 73.673  1.00 40.64  ? 50  HIS C O   1 
ATOM   4172 C CB  . HIS C  1 35  ? 16.308 -39.163 75.443  1.00 40.48  ? 50  HIS C CB  1 
ATOM   4173 C CG  . HIS C  1 35  ? 15.190 -40.031 74.963  1.00 41.11  ? 50  HIS C CG  1 
ATOM   4174 N ND1 . HIS C  1 35  ? 13.990 -39.517 74.496  1.00 42.54  ? 50  HIS C ND1 1 
ATOM   4175 C CD2 . HIS C  1 35  ? 15.063 -41.374 74.919  1.00 41.11  ? 50  HIS C CD2 1 
ATOM   4176 C CE1 . HIS C  1 35  ? 13.179 -40.504 74.172  1.00 40.03  ? 50  HIS C CE1 1 
ATOM   4177 N NE2 . HIS C  1 35  ? 13.811 -41.655 74.432  1.00 42.04  ? 50  HIS C NE2 1 
ATOM   4178 N N   . PRO C  1 36  ? 15.906 -38.095 72.268  1.00 40.75  ? 51  PRO C N   1 
ATOM   4179 C CA  . PRO C  1 36  ? 15.131 -37.242 71.364  1.00 39.67  ? 51  PRO C CA  1 
ATOM   4180 C C   . PRO C  1 36  ? 14.095 -36.305 72.003  1.00 38.38  ? 51  PRO C C   1 
ATOM   4181 O O   . PRO C  1 36  ? 13.842 -35.276 71.407  1.00 37.17  ? 51  PRO C O   1 
ATOM   4182 C CB  . PRO C  1 36  ? 14.415 -38.263 70.466  1.00 40.37  ? 51  PRO C CB  1 
ATOM   4183 C CG  . PRO C  1 36  ? 15.404 -39.405 70.382  1.00 41.55  ? 51  PRO C CG  1 
ATOM   4184 C CD  . PRO C  1 36  ? 16.012 -39.478 71.765  1.00 40.77  ? 51  PRO C CD  1 
ATOM   4185 N N   . GLN C  1 37  ? 13.552 -36.644 73.180  1.00 38.58  ? 52  GLN C N   1 
ATOM   4186 C CA  . GLN C  1 37  ? 12.477 -35.849 73.836  1.00 38.49  ? 52  GLN C CA  1 
ATOM   4187 C C   . GLN C  1 37  ? 12.909 -35.338 75.221  1.00 36.20  ? 52  GLN C C   1 
ATOM   4188 O O   . GLN C  1 37  ? 12.042 -34.794 75.937  1.00 36.28  ? 52  GLN C O   1 
ATOM   4189 C CB  . GLN C  1 37  ? 11.207 -36.696 73.898  1.00 38.67  ? 52  GLN C CB  1 
ATOM   4190 C CG  . GLN C  1 37  ? 9.930  -35.871 73.975  1.00 40.66  ? 52  GLN C CG  1 
ATOM   4191 C CD  . GLN C  1 37  ? 8.696  -36.616 73.520  1.00 40.75  ? 52  GLN C CD  1 
ATOM   4192 O OE1 . GLN C  1 37  ? 8.762  -37.754 73.069  1.00 44.00  ? 52  GLN C OE1 1 
ATOM   4193 N NE2 . GLN C  1 37  ? 7.546  -35.974 73.638  1.00 40.28  ? 52  GLN C NE2 1 
ATOM   4194 N N   . TRP C  1 38  ? 14.189 -35.450 75.594  1.00 37.60  ? 53  TRP C N   1 
ATOM   4195 C CA  . TRP C  1 38  ? 14.650 -35.065 76.957  1.00 35.46  ? 53  TRP C CA  1 
ATOM   4196 C C   . TRP C  1 38  ? 15.938 -34.240 76.901  1.00 33.22  ? 53  TRP C C   1 
ATOM   4197 O O   . TRP C  1 38  ? 16.922 -34.669 76.252  1.00 31.04  ? 53  TRP C O   1 
ATOM   4198 C CB  . TRP C  1 38  ? 14.805 -36.291 77.862  1.00 36.08  ? 53  TRP C CB  1 
ATOM   4199 C CG  . TRP C  1 38  ? 13.509 -36.972 78.176  1.00 36.16  ? 53  TRP C CG  1 
ATOM   4200 C CD1 . TRP C  1 38  ? 12.913 -37.963 77.453  1.00 37.27  ? 53  TRP C CD1 1 
ATOM   4201 C CD2 . TRP C  1 38  ? 12.631 -36.707 79.285  1.00 37.39  ? 53  TRP C CD2 1 
ATOM   4202 N NE1 . TRP C  1 38  ? 11.735 -38.338 78.038  1.00 38.08  ? 53  TRP C NE1 1 
ATOM   4203 C CE2 . TRP C  1 38  ? 11.535 -37.591 79.167  1.00 39.22  ? 53  TRP C CE2 1 
ATOM   4204 C CE3 . TRP C  1 38  ? 12.674 -35.835 80.378  1.00 38.35  ? 53  TRP C CE3 1 
ATOM   4205 C CZ2 . TRP C  1 38  ? 10.482 -37.603 80.083  1.00 39.82  ? 53  TRP C CZ2 1 
ATOM   4206 C CZ3 . TRP C  1 38  ? 11.640 -35.852 81.291  1.00 37.88  ? 53  TRP C CZ3 1 
ATOM   4207 C CH2 . TRP C  1 38  ? 10.565 -36.734 81.149  1.00 40.63  ? 53  TRP C CH2 1 
ATOM   4208 N N   . VAL C  1 39  ? 15.920 -33.115 77.620  1.00 35.20  ? 54  VAL C N   1 
ATOM   4209 C CA  . VAL C  1 39  ? 17.099 -32.247 77.896  1.00 32.85  ? 54  VAL C CA  1 
ATOM   4210 C C   . VAL C  1 39  ? 17.487 -32.407 79.372  1.00 32.86  ? 54  VAL C C   1 
ATOM   4211 O O   . VAL C  1 39  ? 16.602 -32.297 80.244  1.00 31.52  ? 54  VAL C O   1 
ATOM   4212 C CB  . VAL C  1 39  ? 16.801 -30.780 77.529  1.00 33.66  ? 54  VAL C CB  1 
ATOM   4213 C CG1 . VAL C  1 39  ? 17.879 -29.815 78.005  1.00 33.67  ? 54  VAL C CG1 1 
ATOM   4214 C CG2 . VAL C  1 39  ? 16.573 -30.635 76.033  1.00 34.76  ? 54  VAL C CG2 1 
ATOM   4215 N N   . LEU C  1 40  ? 18.770 -32.660 79.625  1.00 31.88  ? 55  LEU C N   1 
ATOM   4216 C CA  . LEU C  1 40  ? 19.379 -32.630 80.977  1.00 31.68  ? 55  LEU C CA  1 
ATOM   4217 C C   . LEU C  1 40  ? 19.931 -31.220 81.229  1.00 32.70  ? 55  LEU C C   1 
ATOM   4218 O O   . LEU C  1 40  ? 20.639 -30.700 80.337  1.00 35.11  ? 55  LEU C O   1 
ATOM   4219 C CB  . LEU C  1 40  ? 20.487 -33.685 81.036  1.00 31.07  ? 55  LEU C CB  1 
ATOM   4220 C CG  . LEU C  1 40  ? 21.158 -33.865 82.394  1.00 29.45  ? 55  LEU C CG  1 
ATOM   4221 C CD1 . LEU C  1 40  ? 20.177 -34.397 83.425  1.00 31.29  ? 55  LEU C CD1 1 
ATOM   4222 C CD2 . LEU C  1 40  ? 22.344 -34.801 82.274  1.00 30.33  ? 55  LEU C CD2 1 
ATOM   4223 N N   . THR C  1 41  ? 19.609 -30.633 82.385  1.00 33.62  ? 56  THR C N   1 
ATOM   4224 C CA  . THR C  1 41  ? 20.066 -29.276 82.797  1.00 33.09  ? 56  THR C CA  1 
ATOM   4225 C C   . THR C  1 41  ? 20.307 -29.250 84.313  1.00 32.19  ? 56  THR C C   1 
ATOM   4226 O O   . THR C  1 41  ? 20.208 -30.308 84.976  1.00 28.11  ? 56  THR C O   1 
ATOM   4227 C CB  . THR C  1 41  ? 19.086 -28.207 82.285  1.00 32.19  ? 56  THR C CB  1 
ATOM   4228 O OG1 . THR C  1 41  ? 19.707 -26.927 82.397  1.00 33.12  ? 56  THR C OG1 1 
ATOM   4229 C CG2 . THR C  1 41  ? 17.770 -28.169 83.030  1.00 32.02  ? 56  THR C CG2 1 
ATOM   4230 N N   . ALA C  1 42  ? 20.654 -28.076 84.839  1.00 32.74  ? 57  ALA C N   1 
ATOM   4231 C CA  . ALA C  1 42  ? 20.832 -27.816 86.282  1.00 32.30  ? 57  ALA C CA  1 
ATOM   4232 C C   . ALA C  1 42  ? 19.474 -27.394 86.843  1.00 30.80  ? 57  ALA C C   1 
ATOM   4233 O O   . ALA C  1 42  ? 18.785 -26.616 86.173  1.00 31.50  ? 57  ALA C O   1 
ATOM   4234 C CB  . ALA C  1 42  ? 21.889 -26.760 86.502  1.00 33.02  ? 57  ALA C CB  1 
ATOM   4235 N N   . ALA C  1 43  ? 19.103 -27.919 88.008  1.00 29.52  ? 58  ALA C N   1 
ATOM   4236 C CA  . ALA C  1 43  ? 17.899 -27.533 88.783  1.00 30.00  ? 58  ALA C CA  1 
ATOM   4237 C C   . ALA C  1 43  ? 17.859 -26.024 89.057  1.00 30.01  ? 58  ALA C C   1 
ATOM   4238 O O   . ALA C  1 43  ? 16.757 -25.460 88.980  1.00 28.92  ? 58  ALA C O   1 
ATOM   4239 C CB  . ALA C  1 43  ? 17.848 -28.315 90.070  1.00 30.62  ? 58  ALA C CB  1 
ATOM   4240 N N   . HIS C  1 44  ? 18.997 -25.386 89.361  1.00 30.92  ? 59  HIS C N   1 
ATOM   4241 C CA  . HIS C  1 44  ? 19.058 -23.944 89.741  1.00 31.72  ? 59  HIS C CA  1 
ATOM   4242 C C   . HIS C  1 44  ? 18.650 -23.054 88.553  1.00 33.19  ? 59  HIS C C   1 
ATOM   4243 O O   . HIS C  1 44  ? 18.267 -21.903 88.794  1.00 34.46  ? 59  HIS C O   1 
ATOM   4244 C CB  . HIS C  1 44  ? 20.422 -23.578 90.358  1.00 32.33  ? 59  HIS C CB  1 
ATOM   4245 C CG  . HIS C  1 44  ? 21.487 -23.239 89.373  1.00 34.54  ? 59  HIS C CG  1 
ATOM   4246 N ND1 . HIS C  1 44  ? 22.443 -24.153 88.973  1.00 33.97  ? 59  HIS C ND1 1 
ATOM   4247 C CD2 . HIS C  1 44  ? 21.741 -22.098 88.699  1.00 33.94  ? 59  HIS C CD2 1 
ATOM   4248 C CE1 . HIS C  1 44  ? 23.236 -23.587 88.092  1.00 32.64  ? 59  HIS C CE1 1 
ATOM   4249 N NE2 . HIS C  1 44  ? 22.832 -22.331 87.919  1.00 32.07  ? 59  HIS C NE2 1 
ATOM   4250 N N   . CYS C  1 45  ? 18.724 -23.558 87.319  1.00 34.39  ? 60  CYS C N   1 
ATOM   4251 C CA  . CYS C  1 45  ? 18.270 -22.851 86.090  1.00 35.14  ? 60  CYS C CA  1 
ATOM   4252 C C   . CYS C  1 45  ? 16.744 -22.697 86.081  1.00 34.45  ? 60  CYS C C   1 
ATOM   4253 O O   . CYS C  1 45  ? 16.267 -21.685 85.534  1.00 32.41  ? 60  CYS C O   1 
ATOM   4254 C CB  . CYS C  1 45  ? 18.721 -23.578 84.832  1.00 35.84  ? 60  CYS C CB  1 
ATOM   4255 S SG  . CYS C  1 45  ? 20.515 -23.549 84.615  1.00 40.47  ? 60  CYS C SG  1 
ATOM   4256 N N   . VAL C  1 46  ? 16.013 -23.658 86.650  1.00 34.01  ? 61  VAL C N   1 
ATOM   4257 C CA  . VAL C  1 46  ? 14.524 -23.748 86.536  1.00 35.54  ? 61  VAL C CA  1 
ATOM   4258 C C   . VAL C  1 46  ? 13.861 -23.890 87.916  1.00 37.66  ? 61  VAL C C   1 
ATOM   4259 O O   . VAL C  1 46  ? 12.632 -24.076 87.941  1.00 44.37  ? 61  VAL C O   1 
ATOM   4260 C CB  . VAL C  1 46  ? 14.124 -24.900 85.588  1.00 35.05  ? 61  VAL C CB  1 
ATOM   4261 C CG1 . VAL C  1 46  ? 14.551 -24.613 84.161  1.00 35.20  ? 61  VAL C CG1 1 
ATOM   4262 C CG2 . VAL C  1 46  ? 14.668 -26.252 86.036  1.00 35.54  ? 61  VAL C CG2 1 
ATOM   4263 N N   . GLY C  1 47  ? 14.611 -23.776 89.019  1.00 35.80  ? 62  GLY C N   1 
ATOM   4264 C CA  . GLY C  1 47  ? 14.091 -23.933 90.390  1.00 35.20  ? 62  GLY C CA  1 
ATOM   4265 C C   . GLY C  1 47  ? 14.969 -23.224 91.421  1.00 36.06  ? 62  GLY C C   1 
ATOM   4266 O O   . GLY C  1 47  ? 15.901 -22.522 91.047  1.00 35.28  ? 62  GLY C O   1 
ATOM   4267 N N   . PRO C  1 48  ? 14.723 -23.384 92.745  1.00 36.47  ? 63  PRO C N   1 
ATOM   4268 C CA  . PRO C  1 48  ? 13.731 -24.333 93.263  1.00 36.27  ? 63  PRO C CA  1 
ATOM   4269 C C   . PRO C  1 48  ? 12.260 -23.906 93.149  1.00 35.83  ? 63  PRO C C   1 
ATOM   4270 O O   . PRO C  1 48  ? 11.424 -24.755 93.323  1.00 35.19  ? 63  PRO C O   1 
ATOM   4271 C CB  . PRO C  1 48  ? 14.106 -24.434 94.752  1.00 36.62  ? 63  PRO C CB  1 
ATOM   4272 C CG  . PRO C  1 48  ? 14.653 -23.058 95.075  1.00 36.52  ? 63  PRO C CG  1 
ATOM   4273 C CD  . PRO C  1 48  ? 15.407 -22.648 93.823  1.00 35.10  ? 63  PRO C CD  1 
ATOM   4274 N N   . ASP C  1 49  ? 11.976 -22.630 92.870  1.00 36.34  ? 64  ASP C N   1 
ATOM   4275 C CA  . ASP C  1 49  ? 10.589 -22.108 92.742  1.00 38.76  ? 64  ASP C CA  1 
ATOM   4276 C C   . ASP C  1 49  ? 10.000 -22.534 91.393  1.00 36.39  ? 64  ASP C C   1 
ATOM   4277 O O   . ASP C  1 49  ? 10.728 -22.508 90.384  1.00 36.96  ? 64  ASP C O   1 
ATOM   4278 C CB  . ASP C  1 49  ? 10.527 -20.589 92.876  1.00 40.34  ? 64  ASP C CB  1 
ATOM   4279 C CG  . ASP C  1 49  ? 10.980 -20.076 94.234  1.00 45.28  ? 64  ASP C CG  1 
ATOM   4280 O OD1 . ASP C  1 49  ? 10.660 -20.718 95.261  1.00 42.04  ? 64  ASP C OD1 1 
ATOM   4281 O OD2 . ASP C  1 49  ? 11.670 -19.044 94.248  1.00 54.07  ? 64  ASP C OD2 1 
ATOM   4282 N N   . VAL C  1 50  ? 8.720  -22.899 91.397  1.00 37.95  ? 65  VAL C N   1 
ATOM   4283 C CA  . VAL C  1 50  ? 7.977  -23.423 90.214  1.00 40.69  ? 65  VAL C CA  1 
ATOM   4284 C C   . VAL C  1 50  ? 7.841  -22.291 89.187  1.00 42.99  ? 65  VAL C C   1 
ATOM   4285 O O   . VAL C  1 50  ? 7.419  -21.192 89.585  1.00 42.88  ? 65  VAL C O   1 
ATOM   4286 C CB  . VAL C  1 50  ? 6.615  -24.007 90.638  1.00 43.26  ? 65  VAL C CB  1 
ATOM   4287 C CG1 . VAL C  1 50  ? 5.744  -24.382 89.447  1.00 45.66  ? 65  VAL C CG1 1 
ATOM   4288 C CG2 . VAL C  1 50  ? 6.792  -25.216 91.553  1.00 41.55  ? 65  VAL C CG2 1 
ATOM   4289 N N   . LYS C  1 51  ? 8.191  -22.563 87.923  1.00 43.72  ? 66  LYS C N   1 
ATOM   4290 C CA  . LYS C  1 51  ? 8.180  -21.598 86.788  1.00 48.01  ? 66  LYS C CA  1 
ATOM   4291 C C   . LYS C  1 51  ? 7.004  -21.942 85.854  1.00 46.65  ? 66  LYS C C   1 
ATOM   4292 O O   . LYS C  1 51  ? 6.587  -23.121 85.813  1.00 43.86  ? 66  LYS C O   1 
ATOM   4293 C CB  . LYS C  1 51  ? 9.499  -21.631 85.989  1.00 52.54  ? 66  LYS C CB  1 
ATOM   4294 C CG  . LYS C  1 51  ? 10.805 -21.677 86.773  1.00 54.19  ? 66  LYS C CG  1 
ATOM   4295 C CD  . LYS C  1 51  ? 11.141 -20.402 87.501  1.00 54.91  ? 66  LYS C CD  1 
ATOM   4296 C CE  . LYS C  1 51  ? 12.453 -20.502 88.252  1.00 56.87  ? 66  LYS C CE  1 
ATOM   4297 N NZ  . LYS C  1 51  ? 12.466 -19.619 89.440  1.00 58.44  ? 66  LYS C NZ  1 
ATOM   4298 N N   . ASP C  1 52  ? 6.500  -20.945 85.122  1.00 46.88  ? 67  ASP C N   1 
ATOM   4299 C CA  . ASP C  1 52  ? 5.474  -21.095 84.058  1.00 46.40  ? 67  ASP C CA  1 
ATOM   4300 C C   . ASP C  1 52  ? 6.137  -21.753 82.840  1.00 45.93  ? 67  ASP C C   1 
ATOM   4301 O O   . ASP C  1 52  ? 7.105  -21.156 82.311  1.00 48.31  ? 67  ASP C O   1 
ATOM   4302 C CB  . ASP C  1 52  ? 4.867  -19.725 83.732  1.00 48.77  ? 67  ASP C CB  1 
ATOM   4303 C CG  . ASP C  1 52  ? 3.835  -19.721 82.617  1.00 50.43  ? 67  ASP C CG  1 
ATOM   4304 O OD1 . ASP C  1 52  ? 3.187  -20.766 82.397  1.00 53.25  ? 67  ASP C OD1 1 
ATOM   4305 O OD2 . ASP C  1 52  ? 3.693  -18.666 81.973  1.00 57.96  ? 67  ASP C OD2 1 
ATOM   4306 N N   . LEU C  1 53  ? 5.631  -22.909 82.393  1.00 45.18  ? 68  LEU C N   1 
ATOM   4307 C CA  . LEU C  1 53  ? 6.157  -23.649 81.206  1.00 46.13  ? 68  LEU C CA  1 
ATOM   4308 C C   . LEU C  1 53  ? 6.044  -22.802 79.932  1.00 42.96  ? 68  LEU C C   1 
ATOM   4309 O O   . LEU C  1 53  ? 6.928  -22.937 79.058  1.00 41.16  ? 68  LEU C O   1 
ATOM   4310 C CB  . LEU C  1 53  ? 5.398  -24.966 81.024  1.00 48.97  ? 68  LEU C CB  1 
ATOM   4311 C CG  . LEU C  1 53  ? 5.814  -26.098 81.960  1.00 52.10  ? 68  LEU C CG  1 
ATOM   4312 C CD1 . LEU C  1 53  ? 4.758  -27.184 81.960  1.00 55.31  ? 68  LEU C CD1 1 
ATOM   4313 C CD2 . LEU C  1 53  ? 7.160  -26.686 81.570  1.00 53.71  ? 68  LEU C CD2 1 
ATOM   4314 N N   . ALA C  1 54  ? 4.997  -21.979 79.825  1.00 42.07  ? 69  ALA C N   1 
ATOM   4315 C CA  . ALA C  1 54  ? 4.706  -21.119 78.649  1.00 42.73  ? 69  ALA C CA  1 
ATOM   4316 C C   . ALA C  1 54  ? 5.839  -20.110 78.415  1.00 43.38  ? 69  ALA C C   1 
ATOM   4317 O O   . ALA C  1 54  ? 6.029  -19.718 77.251  1.00 47.12  ? 69  ALA C O   1 
ATOM   4318 C CB  . ALA C  1 54  ? 3.383  -20.412 78.823  1.00 41.66  ? 69  ALA C CB  1 
ATOM   4319 N N   . ALA C  1 55  ? 6.575  -19.730 79.466  1.00 41.46  ? 70  ALA C N   1 
ATOM   4320 C CA  . ALA C  1 55  ? 7.664  -18.728 79.417  1.00 40.26  ? 70  ALA C CA  1 
ATOM   4321 C C   . ALA C  1 55  ? 9.029  -19.401 79.192  1.00 38.70  ? 70  ALA C C   1 
ATOM   4322 O O   . ALA C  1 55  ? 10.042 -18.679 79.258  1.00 39.50  ? 70  ALA C O   1 
ATOM   4323 C CB  . ALA C  1 55  ? 7.643  -17.919 80.696  1.00 39.61  ? 70  ALA C CB  1 
ATOM   4324 N N   . LEU C  1 56  ? 9.072  -20.712 78.924  1.00 38.29  ? 71  LEU C N   1 
ATOM   4325 C CA  . LEU C  1 56  ? 10.327 -21.477 78.697  1.00 38.14  ? 71  LEU C CA  1 
ATOM   4326 C C   . LEU C  1 56  ? 10.310 -22.082 77.289  1.00 38.79  ? 71  LEU C C   1 
ATOM   4327 O O   . LEU C  1 56  ? 9.274  -22.645 76.896  1.00 39.55  ? 71  LEU C O   1 
ATOM   4328 C CB  . LEU C  1 56  ? 10.438 -22.572 79.761  1.00 36.42  ? 71  LEU C CB  1 
ATOM   4329 C CG  . LEU C  1 56  ? 11.665 -23.479 79.662  1.00 37.78  ? 71  LEU C CG  1 
ATOM   4330 C CD1 . LEU C  1 56  ? 12.950 -22.697 79.883  1.00 39.06  ? 71  LEU C CD1 1 
ATOM   4331 C CD2 . LEU C  1 56  ? 11.577 -24.621 80.665  1.00 38.81  ? 71  LEU C CD2 1 
ATOM   4332 N N   . ARG C  1 57  ? 11.431 -21.983 76.572  1.00 37.98  ? 72  ARG C N   1 
ATOM   4333 C CA  . ARG C  1 57  ? 11.653 -22.674 75.279  1.00 37.69  ? 72  ARG C CA  1 
ATOM   4334 C C   . ARG C  1 57  ? 13.057 -23.277 75.260  1.00 35.22  ? 72  ARG C C   1 
ATOM   4335 O O   . ARG C  1 57  ? 13.959 -22.758 75.969  1.00 33.85  ? 72  ARG C O   1 
ATOM   4336 C CB  . ARG C  1 57  ? 11.473 -21.717 74.098  1.00 39.84  ? 72  ARG C CB  1 
ATOM   4337 C CG  . ARG C  1 57  ? 10.059 -21.181 73.928  1.00 41.55  ? 72  ARG C CG  1 
ATOM   4338 C CD  . ARG C  1 57  ? 9.134  -22.132 73.207  1.00 41.24  ? 72  ARG C CD  1 
ATOM   4339 N NE  . ARG C  1 57  ? 7.938  -21.395 72.833  1.00 43.84  ? 72  ARG C NE  1 
ATOM   4340 C CZ  . ARG C  1 57  ? 6.906  -21.119 73.632  1.00 45.03  ? 72  ARG C CZ  1 
ATOM   4341 N NH1 . ARG C  1 57  ? 6.876  -21.537 74.888  1.00 47.79  ? 72  ARG C NH1 1 
ATOM   4342 N NH2 . ARG C  1 57  ? 5.894  -20.411 73.161  1.00 46.20  ? 72  ARG C NH2 1 
ATOM   4343 N N   . VAL C  1 58  ? 13.228 -24.323 74.449  1.00 34.90  ? 73  VAL C N   1 
ATOM   4344 C CA  . VAL C  1 58  ? 14.545 -24.951 74.148  1.00 34.81  ? 73  VAL C CA  1 
ATOM   4345 C C   . VAL C  1 58  ? 14.919 -24.603 72.704  1.00 34.97  ? 73  VAL C C   1 
ATOM   4346 O O   . VAL C  1 58  ? 14.048 -24.668 71.813  1.00 35.98  ? 73  VAL C O   1 
ATOM   4347 C CB  . VAL C  1 58  ? 14.520 -26.471 74.397  1.00 36.23  ? 73  VAL C CB  1 
ATOM   4348 C CG1 . VAL C  1 58  ? 15.781 -27.165 73.899  1.00 37.76  ? 73  VAL C CG1 1 
ATOM   4349 C CG2 . VAL C  1 58  ? 14.299 -26.777 75.867  1.00 36.83  ? 73  VAL C CG2 1 
ATOM   4350 N N   . GLN C  1 59  ? 16.186 -24.248 72.506  1.00 34.59  ? 74  GLN C N   1 
ATOM   4351 C CA  . GLN C  1 59  ? 16.826 -24.063 71.185  1.00 34.34  ? 74  GLN C CA  1 
ATOM   4352 C C   . GLN C  1 59  ? 17.923 -25.119 71.060  1.00 34.73  ? 74  GLN C C   1 
ATOM   4353 O O   . GLN C  1 59  ? 18.812 -25.125 71.915  1.00 34.93  ? 74  GLN C O   1 
ATOM   4354 C CB  . GLN C  1 59  ? 17.386 -22.639 71.087  1.00 34.76  ? 74  GLN C CB  1 
ATOM   4355 C CG  . GLN C  1 59  ? 18.218 -22.374 69.839  1.00 35.19  ? 74  GLN C CG  1 
ATOM   4356 C CD  . GLN C  1 59  ? 17.421 -22.618 68.581  1.00 36.24  ? 74  GLN C CD  1 
ATOM   4357 O OE1 . GLN C  1 59  ? 16.308 -22.119 68.435  1.00 37.78  ? 74  GLN C OE1 1 
ATOM   4358 N NE2 . GLN C  1 59  ? 17.967 -23.416 67.677  1.00 36.53  ? 74  GLN C NE2 1 
ATOM   4359 N N   . LEU C  1 60  ? 17.856 -25.969 70.034  1.00 35.86  ? 75  LEU C N   1 
ATOM   4360 C CA  . LEU C  1 60  ? 18.880 -27.005 69.740  1.00 38.16  ? 75  LEU C CA  1 
ATOM   4361 C C   . LEU C  1 60  ? 20.138 -26.320 69.206  1.00 38.55  ? 75  LEU C C   1 
ATOM   4362 O O   . LEU C  1 60  ? 20.101 -25.089 68.970  1.00 39.85  ? 75  LEU C O   1 
ATOM   4363 C CB  . LEU C  1 60  ? 18.316 -28.019 68.739  1.00 40.09  ? 75  LEU C CB  1 
ATOM   4364 C CG  . LEU C  1 60  ? 17.078 -28.783 69.217  1.00 42.84  ? 75  LEU C CG  1 
ATOM   4365 C CD1 . LEU C  1 60  ? 16.493 -29.640 68.100  1.00 41.67  ? 75  LEU C CD1 1 
ATOM   4366 C CD2 . LEU C  1 60  ? 17.394 -29.629 70.445  1.00 42.71  ? 75  LEU C CD2 1 
ATOM   4367 N N   . ARG C  1 61  ? 21.209 -27.090 69.027  1.00 38.04  ? 76  ARG C N   1 
ATOM   4368 C CA  . ARG C  1 61  ? 22.549 -26.534 68.734  1.00 39.29  ? 76  ARG C CA  1 
ATOM   4369 C C   . ARG C  1 61  ? 22.449 -25.521 67.589  1.00 40.56  ? 76  ARG C C   1 
ATOM   4370 O O   . ARG C  1 61  ? 21.903 -25.866 66.535  1.00 42.79  ? 76  ARG C O   1 
ATOM   4371 C CB  . ARG C  1 61  ? 23.538 -27.629 68.358  1.00 40.11  ? 76  ARG C CB  1 
ATOM   4372 C CG  . ARG C  1 61  ? 24.976 -27.150 68.449  1.00 39.59  ? 76  ARG C CG  1 
ATOM   4373 C CD  . ARG C  1 61  ? 25.818 -27.818 67.400  1.00 38.49  ? 76  ARG C CD  1 
ATOM   4374 N NE  . ARG C  1 61  ? 27.229 -27.511 67.538  1.00 38.11  ? 76  ARG C NE  1 
ATOM   4375 C CZ  . ARG C  1 61  ? 27.831 -26.402 67.113  1.00 37.70  ? 76  ARG C CZ  1 
ATOM   4376 N NH1 . ARG C  1 61  ? 27.139 -25.432 66.536  1.00 39.53  ? 76  ARG C NH1 1 
ATOM   4377 N NH2 . ARG C  1 61  ? 29.140 -26.277 67.268  1.00 36.84  ? 76  ARG C NH2 1 
ATOM   4378 N N   . GLU C  1 62  ? 22.904 -24.295 67.823  1.00 40.33  ? 77  GLU C N   1 
ATOM   4379 C CA  . GLU C  1 62  ? 23.139 -23.278 66.764  1.00 41.55  ? 77  GLU C CA  1 
ATOM   4380 C C   . GLU C  1 62  ? 24.526 -22.683 67.013  1.00 40.62  ? 77  GLU C C   1 
ATOM   4381 O O   . GLU C  1 62  ? 24.941 -22.599 68.187  1.00 42.84  ? 77  GLU C O   1 
ATOM   4382 C CB  . GLU C  1 62  ? 21.998 -22.252 66.693  1.00 42.65  ? 77  GLU C CB  1 
ATOM   4383 C CG  . GLU C  1 62  ? 21.522 -21.723 68.024  1.00 41.79  ? 77  GLU C CG  1 
ATOM   4384 C CD  . GLU C  1 62  ? 20.488 -20.615 67.950  1.00 41.83  ? 77  GLU C CD  1 
ATOM   4385 O OE1 . GLU C  1 62  ? 19.755 -20.533 66.956  1.00 45.61  ? 77  GLU C OE1 1 
ATOM   4386 O OE2 . GLU C  1 62  ? 20.401 -19.853 68.913  1.00 40.95  ? 77  GLU C OE2 1 
ATOM   4387 N N   . GLN C  1 63  ? 25.234 -22.348 65.939  1.00 37.49  ? 78  GLN C N   1 
ATOM   4388 C CA  . GLN C  1 63  ? 26.636 -21.858 65.991  1.00 39.43  ? 78  GLN C CA  1 
ATOM   4389 C C   . GLN C  1 63  ? 26.655 -20.460 66.627  1.00 39.52  ? 78  GLN C C   1 
ATOM   4390 O O   . GLN C  1 63  ? 27.594 -20.173 67.381  1.00 38.46  ? 78  GLN C O   1 
ATOM   4391 C CB  . GLN C  1 63  ? 27.252 -21.879 64.589  1.00 38.82  ? 78  GLN C CB  1 
ATOM   4392 C CG  . GLN C  1 63  ? 28.759 -21.659 64.554  1.00 39.24  ? 78  GLN C CG  1 
ATOM   4393 C CD  . GLN C  1 63  ? 29.535 -22.728 65.282  1.00 42.28  ? 78  GLN C CD  1 
ATOM   4394 O OE1 . GLN C  1 63  ? 29.057 -23.842 65.497  1.00 38.93  ? 78  GLN C OE1 1 
ATOM   4395 N NE2 . GLN C  1 63  ? 30.737 -22.377 65.702  1.00 45.82  ? 78  GLN C NE2 1 
ATOM   4396 N N   . HIS C  1 64  ? 25.638 -19.644 66.343  1.00 39.00  ? 79  HIS C N   1 
ATOM   4397 C CA  . HIS C  1 64  ? 25.482 -18.252 66.835  1.00 37.79  ? 79  HIS C CA  1 
ATOM   4398 C C   . HIS C  1 64  ? 24.085 -18.102 67.441  1.00 37.27  ? 79  HIS C C   1 
ATOM   4399 O O   . HIS C  1 64  ? 23.105 -18.284 66.683  1.00 40.25  ? 79  HIS C O   1 
ATOM   4400 C CB  . HIS C  1 64  ? 25.724 -17.277 65.681  1.00 38.68  ? 79  HIS C CB  1 
ATOM   4401 C CG  . HIS C  1 64  ? 27.111 -17.335 65.142  1.00 37.72  ? 79  HIS C CG  1 
ATOM   4402 N ND1 . HIS C  1 64  ? 27.420 -17.970 63.953  1.00 40.27  ? 79  HIS C ND1 1 
ATOM   4403 C CD2 . HIS C  1 64  ? 28.272 -16.852 65.629  1.00 36.75  ? 79  HIS C CD2 1 
ATOM   4404 C CE1 . HIS C  1 64  ? 28.715 -17.872 63.728  1.00 38.72  ? 79  HIS C CE1 1 
ATOM   4405 N NE2 . HIS C  1 64  ? 29.259 -17.177 64.737  1.00 38.48  ? 79  HIS C NE2 1 
ATOM   4406 N N   . LEU C  1 65  ? 23.993 -17.788 68.739  1.00 37.01  ? 80  LEU C N   1 
ATOM   4407 C CA  . LEU C  1 65  ? 22.689 -17.587 69.436  1.00 37.31  ? 80  LEU C CA  1 
ATOM   4408 C C   . LEU C  1 65  ? 21.852 -16.563 68.669  1.00 36.27  ? 80  LEU C C   1 
ATOM   4409 O O   . LEU C  1 65  ? 22.421 -15.535 68.278  1.00 35.71  ? 80  LEU C O   1 
ATOM   4410 C CB  . LEU C  1 65  ? 22.864 -17.081 70.874  1.00 38.85  ? 80  LEU C CB  1 
ATOM   4411 C CG  . LEU C  1 65  ? 23.060 -18.111 71.982  1.00 41.13  ? 80  LEU C CG  1 
ATOM   4412 C CD1 . LEU C  1 65  ? 23.204 -17.394 73.311  1.00 42.36  ? 80  LEU C CD1 1 
ATOM   4413 C CD2 . LEU C  1 65  ? 21.928 -19.121 72.049  1.00 40.97  ? 80  LEU C CD2 1 
ATOM   4414 N N   . TYR C  1 66  ? 20.555 -16.845 68.515  1.00 36.02  ? 81  TYR C N   1 
ATOM   4415 C CA  . TYR C  1 66  ? 19.464 -15.901 68.141  1.00 37.37  ? 81  TYR C CA  1 
ATOM   4416 C C   . TYR C  1 66  ? 19.308 -15.755 66.620  1.00 38.23  ? 81  TYR C C   1 
ATOM   4417 O O   . TYR C  1 66  ? 18.223 -15.294 66.210  1.00 41.19  ? 81  TYR C O   1 
ATOM   4418 C CB  . TYR C  1 66  ? 19.659 -14.516 68.770  1.00 34.70  ? 81  TYR C CB  1 
ATOM   4419 C CG  . TYR C  1 66  ? 19.827 -14.517 70.268  1.00 33.68  ? 81  TYR C CG  1 
ATOM   4420 C CD1 . TYR C  1 66  ? 18.823 -15.001 71.097  1.00 32.28  ? 81  TYR C CD1 1 
ATOM   4421 C CD2 . TYR C  1 66  ? 20.977 -14.023 70.864  1.00 32.82  ? 81  TYR C CD2 1 
ATOM   4422 C CE1 . TYR C  1 66  ? 18.970 -15.013 72.473  1.00 32.31  ? 81  TYR C CE1 1 
ATOM   4423 C CE2 . TYR C  1 66  ? 21.133 -14.020 72.243  1.00 32.40  ? 81  TYR C CE2 1 
ATOM   4424 C CZ  . TYR C  1 66  ? 20.122 -14.515 73.051  1.00 32.28  ? 81  TYR C CZ  1 
ATOM   4425 O OH  . TYR C  1 66  ? 20.240 -14.527 74.408  1.00 31.40  ? 81  TYR C OH  1 
ATOM   4426 N N   . TYR C  1 67  ? 20.296 -16.144 65.805  1.00 41.27  ? 82  TYR C N   1 
ATOM   4427 C CA  A TYR C  1 67  ? 20.300 -15.836 64.349  0.50 42.43  ? 82  TYR C CA  1 
ATOM   4428 C CA  B TYR C  1 67  ? 20.325 -15.857 64.345  0.50 43.95  ? 82  TYR C CA  1 
ATOM   4429 C C   . TYR C  1 67  ? 19.375 -16.803 63.600  1.00 43.84  ? 82  TYR C C   1 
ATOM   4430 O O   . TYR C  1 67  ? 18.666 -16.321 62.704  1.00 46.85  ? 82  TYR C O   1 
ATOM   4431 C CB  A TYR C  1 67  ? 21.730 -15.770 63.811  0.50 42.34  ? 82  TYR C CB  1 
ATOM   4432 C CB  B TYR C  1 67  ? 21.745 -15.949 63.774  0.50 45.87  ? 82  TYR C CB  1 
ATOM   4433 C CG  A TYR C  1 67  ? 22.457 -14.532 64.285  0.50 41.20  ? 82  TYR C CG  1 
ATOM   4434 C CG  B TYR C  1 67  ? 21.818 -15.770 62.277  0.50 47.32  ? 82  TYR C CG  1 
ATOM   4435 C CD1 A TYR C  1 67  ? 22.337 -13.323 63.615  0.50 40.78  ? 82  TYR C CD1 1 
ATOM   4436 C CD1 B TYR C  1 67  ? 21.159 -14.722 61.653  0.50 47.83  ? 82  TYR C CD1 1 
ATOM   4437 C CD2 A TYR C  1 67  ? 23.210 -14.549 65.446  0.50 40.65  ? 82  TYR C CD2 1 
ATOM   4438 C CD2 B TYR C  1 67  ? 22.537 -16.646 61.481  0.50 49.05  ? 82  TYR C CD2 1 
ATOM   4439 C CE1 A TYR C  1 67  ? 22.977 -12.179 64.067  0.50 40.09  ? 82  TYR C CE1 1 
ATOM   4440 C CE1 B TYR C  1 67  ? 21.211 -14.550 60.280  0.50 46.68  ? 82  TYR C CE1 1 
ATOM   4441 C CE2 A TYR C  1 67  ? 23.852 -13.416 65.914  0.50 40.51  ? 82  TYR C CE2 1 
ATOM   4442 C CE2 B TYR C  1 67  ? 22.599 -16.488 60.105  0.50 48.30  ? 82  TYR C CE2 1 
ATOM   4443 C CZ  A TYR C  1 67  ? 23.734 -12.224 65.224  0.50 40.82  ? 82  TYR C CZ  1 
ATOM   4444 C CZ  B TYR C  1 67  ? 21.935 -15.435 59.504  0.50 46.86  ? 82  TYR C CZ  1 
ATOM   4445 O OH  A TYR C  1 67  ? 24.368 -11.106 65.685  0.50 39.98  ? 82  TYR C OH  1 
ATOM   4446 O OH  B TYR C  1 67  ? 21.989 -15.267 58.152  0.50 48.40  ? 82  TYR C OH  1 
ATOM   4447 N N   . GLN C  1 68  ? 19.372 -18.089 63.952  1.00 45.34  ? 83  GLN C N   1 
ATOM   4448 C CA  . GLN C  1 68  ? 18.541 -19.101 63.242  1.00 53.33  ? 83  GLN C CA  1 
ATOM   4449 C C   . GLN C  1 68  ? 17.669 -19.848 64.251  1.00 49.15  ? 83  GLN C C   1 
ATOM   4450 O O   . GLN C  1 68  ? 17.729 -21.081 64.266  1.00 52.95  ? 83  GLN C O   1 
ATOM   4451 C CB  . GLN C  1 68  ? 19.446 -20.037 62.437  1.00 58.89  ? 83  GLN C CB  1 
ATOM   4452 C CG  . GLN C  1 68  ? 20.159 -19.366 61.271  1.00 64.32  ? 83  GLN C CG  1 
ATOM   4453 C CD  . GLN C  1 68  ? 19.250 -19.098 60.096  1.00 68.93  ? 83  GLN C CD  1 
ATOM   4454 O OE1 . GLN C  1 68  ? 19.204 -19.864 59.136  1.00 68.65  ? 83  GLN C OE1 1 
ATOM   4455 N NE2 . GLN C  1 68  ? 18.508 -18.003 60.165  1.00 72.10  ? 83  GLN C NE2 1 
ATOM   4456 N N   . ASP C  1 69  ? 16.875 -19.121 65.040  1.00 46.08  ? 84  ASP C N   1 
ATOM   4457 C CA  . ASP C  1 69  ? 16.106 -19.711 66.168  1.00 44.64  ? 84  ASP C CA  1 
ATOM   4458 C C   . ASP C  1 69  ? 14.952 -20.557 65.622  1.00 43.71  ? 84  ASP C C   1 
ATOM   4459 O O   . ASP C  1 69  ? 14.225 -20.070 64.743  1.00 44.44  ? 84  ASP C O   1 
ATOM   4460 C CB  . ASP C  1 69  ? 15.586 -18.656 67.150  1.00 41.72  ? 84  ASP C CB  1 
ATOM   4461 C CG  . ASP C  1 69  ? 16.611 -18.146 68.146  1.00 39.47  ? 84  ASP C CG  1 
ATOM   4462 O OD1 . ASP C  1 69  ? 17.760 -18.625 68.124  1.00 38.76  ? 84  ASP C OD1 1 
ATOM   4463 O OD2 . ASP C  1 69  ? 16.250 -17.271 68.951  1.00 38.70  ? 84  ASP C OD2 1 
ATOM   4464 N N   . GLN C  1 70  ? 14.814 -21.781 66.138  1.00 45.00  ? 85  GLN C N   1 
ATOM   4465 C CA  . GLN C  1 70  ? 13.615 -22.649 65.998  1.00 47.54  ? 85  GLN C CA  1 
ATOM   4466 C C   . GLN C  1 70  ? 13.242 -23.127 67.405  1.00 44.83  ? 85  GLN C C   1 
ATOM   4467 O O   . GLN C  1 70  ? 13.726 -24.191 67.831  1.00 44.30  ? 85  GLN C O   1 
ATOM   4468 C CB  . GLN C  1 70  ? 13.905 -23.783 65.014  1.00 49.86  ? 85  GLN C CB  1 
ATOM   4469 C CG  . GLN C  1 70  ? 14.129 -23.281 63.596  1.00 54.71  ? 85  GLN C CG  1 
ATOM   4470 C CD  . GLN C  1 70  ? 14.461 -24.388 62.629  1.00 58.48  ? 85  GLN C CD  1 
ATOM   4471 O OE1 . GLN C  1 70  ? 15.351 -25.196 62.878  1.00 61.16  ? 85  GLN C OE1 1 
ATOM   4472 N NE2 . GLN C  1 70  ? 13.758 -24.426 61.508  1.00 61.90  ? 85  GLN C NE2 1 
ATOM   4473 N N   . LEU C  1 71  ? 12.458 -22.324 68.120  1.00 41.24  ? 86  LEU C N   1 
ATOM   4474 C CA  . LEU C  1 71  ? 12.209 -22.512 69.572  1.00 40.23  ? 86  LEU C CA  1 
ATOM   4475 C C   . LEU C  1 71  ? 11.214 -23.656 69.776  1.00 40.25  ? 86  LEU C C   1 
ATOM   4476 O O   . LEU C  1 71  ? 10.181 -23.671 69.089  1.00 40.80  ? 86  LEU C O   1 
ATOM   4477 C CB  . LEU C  1 71  ? 11.709 -21.200 70.180  1.00 38.27  ? 86  LEU C CB  1 
ATOM   4478 C CG  . LEU C  1 71  ? 12.691 -20.033 70.090  1.00 40.49  ? 86  LEU C CG  1 
ATOM   4479 C CD1 . LEU C  1 71  ? 12.106 -18.802 70.751  1.00 40.86  ? 86  LEU C CD1 1 
ATOM   4480 C CD2 . LEU C  1 71  ? 14.042 -20.374 70.697  1.00 39.65  ? 86  LEU C CD2 1 
ATOM   4481 N N   . LEU C  1 72  ? 11.553 -24.587 70.673  1.00 39.24  ? 87  LEU C N   1 
ATOM   4482 C CA  . LEU C  1 72  ? 10.761 -25.811 70.968  1.00 38.73  ? 87  LEU C CA  1 
ATOM   4483 C C   . LEU C  1 72  ? 10.080 -25.646 72.321  1.00 39.51  ? 87  LEU C C   1 
ATOM   4484 O O   . LEU C  1 72  ? 10.735 -25.292 73.305  1.00 40.80  ? 87  LEU C O   1 
ATOM   4485 C CB  . LEU C  1 72  ? 11.687 -27.032 70.954  1.00 36.70  ? 87  LEU C CB  1 
ATOM   4486 C CG  . LEU C  1 72  ? 12.490 -27.236 69.669  1.00 37.19  ? 87  LEU C CG  1 
ATOM   4487 C CD1 . LEU C  1 72  ? 13.441 -28.412 69.809  1.00 38.11  ? 87  LEU C CD1 1 
ATOM   4488 C CD2 . LEU C  1 72  ? 11.574 -27.436 68.465  1.00 38.33  ? 87  LEU C CD2 1 
ATOM   4489 N N   . PRO C  1 73  ? 8.751  -25.888 72.419  1.00 41.19  ? 88  PRO C N   1 
ATOM   4490 C CA  . PRO C  1 73  ? 8.064  -25.830 73.705  1.00 40.96  ? 88  PRO C CA  1 
ATOM   4491 C C   . PRO C  1 73  ? 8.407  -27.053 74.571  1.00 40.51  ? 88  PRO C C   1 
ATOM   4492 O O   . PRO C  1 73  ? 8.806  -28.077 74.046  1.00 40.77  ? 88  PRO C O   1 
ATOM   4493 C CB  . PRO C  1 73  ? 6.584  -25.759 73.309  1.00 43.20  ? 88  PRO C CB  1 
ATOM   4494 C CG  . PRO C  1 73  ? 6.524  -26.521 72.000  1.00 43.36  ? 88  PRO C CG  1 
ATOM   4495 C CD  . PRO C  1 73  ? 7.843  -26.233 71.309  1.00 42.56  ? 88  PRO C CD  1 
ATOM   4496 N N   . VAL C  1 74  ? 8.325  -26.870 75.891  1.00 41.29  ? 89  VAL C N   1 
ATOM   4497 C CA  . VAL C  1 74  ? 8.591  -27.901 76.939  1.00 39.30  ? 89  VAL C CA  1 
ATOM   4498 C C   . VAL C  1 74  ? 7.235  -28.335 77.505  1.00 39.21  ? 89  VAL C C   1 
ATOM   4499 O O   . VAL C  1 74  ? 6.433  -27.443 77.831  1.00 37.98  ? 89  VAL C O   1 
ATOM   4500 C CB  . VAL C  1 74  ? 9.519  -27.343 78.038  1.00 39.73  ? 89  VAL C CB  1 
ATOM   4501 C CG1 . VAL C  1 74  ? 9.714  -28.317 79.199  1.00 40.30  ? 89  VAL C CG1 1 
ATOM   4502 C CG2 . VAL C  1 74  ? 10.865 -26.922 77.467  1.00 40.89  ? 89  VAL C CG2 1 
ATOM   4503 N N   . SER C  1 75  ? 6.995  -29.644 77.611  1.00 40.22  ? 90  SER C N   1 
ATOM   4504 C CA  . SER C  1 75  ? 5.762  -30.229 78.194  1.00 42.78  ? 90  SER C CA  1 
ATOM   4505 C C   . SER C  1 75  ? 5.899  -30.359 79.715  1.00 42.63  ? 90  SER C C   1 
ATOM   4506 O O   . SER C  1 75  ? 4.886  -30.181 80.383  1.00 45.19  ? 90  SER C O   1 
ATOM   4507 C CB  . SER C  1 75  ? 5.425  -31.549 77.564  1.00 43.49  ? 90  SER C CB  1 
ATOM   4508 O OG  . SER C  1 75  ? 6.455  -32.495 77.781  1.00 48.70  ? 90  SER C OG  1 
ATOM   4509 N N   . ARG C  1 76  ? 7.097  -30.650 80.237  1.00 40.37  ? 91  ARG C N   1 
ATOM   4510 C CA  . ARG C  1 76  ? 7.314  -30.909 81.685  1.00 40.89  ? 91  ARG C CA  1 
ATOM   4511 C C   . ARG C  1 76  ? 8.717  -30.471 82.121  1.00 37.60  ? 91  ARG C C   1 
ATOM   4512 O O   . ARG C  1 76  ? 9.684  -30.814 81.430  1.00 37.51  ? 91  ARG C O   1 
ATOM   4513 C CB  . ARG C  1 76  ? 7.122  -32.398 81.986  1.00 42.68  ? 91  ARG C CB  1 
ATOM   4514 C CG  . ARG C  1 76  ? 6.961  -32.719 83.464  1.00 43.64  ? 91  ARG C CG  1 
ATOM   4515 C CD  . ARG C  1 76  ? 6.722  -34.198 83.680  1.00 45.45  ? 91  ARG C CD  1 
ATOM   4516 N NE  . ARG C  1 76  ? 6.723  -34.570 85.088  1.00 50.07  ? 91  ARG C NE  1 
ATOM   4517 C CZ  . ARG C  1 76  ? 6.553  -35.806 85.557  1.00 51.19  ? 91  ARG C CZ  1 
ATOM   4518 N NH1 . ARG C  1 76  ? 6.374  -36.826 84.731  1.00 53.33  ? 91  ARG C NH1 1 
ATOM   4519 N NH2 . ARG C  1 76  ? 6.565  -36.017 86.862  1.00 51.44  ? 91  ARG C NH2 1 
ATOM   4520 N N   . ILE C  1 77  ? 8.799  -29.784 83.264  1.00 36.06  ? 92  ILE C N   1 
ATOM   4521 C CA  . ILE C  1 77  ? 10.048 -29.557 84.049  1.00 37.53  ? 92  ILE C CA  1 
ATOM   4522 C C   . ILE C  1 77  ? 10.037 -30.541 85.231  1.00 36.03  ? 92  ILE C C   1 
ATOM   4523 O O   . ILE C  1 77  ? 9.106  -30.464 86.044  1.00 35.53  ? 92  ILE C O   1 
ATOM   4524 C CB  . ILE C  1 77  ? 10.155 -28.095 84.529  1.00 36.81  ? 92  ILE C CB  1 
ATOM   4525 C CG1 . ILE C  1 77  ? 10.207 -27.098 83.368  1.00 39.85  ? 92  ILE C CG1 1 
ATOM   4526 C CG2 . ILE C  1 77  ? 11.354 -27.926 85.448  1.00 38.25  ? 92  ILE C CG2 1 
ATOM   4527 C CD1 . ILE C  1 77  ? 9.819  -25.684 83.754  1.00 40.04  ? 92  ILE C CD1 1 
ATOM   4528 N N   . ILE C  1 78  ? 11.028 -31.436 85.311  1.00 35.38  ? 93  ILE C N   1 
ATOM   4529 C CA  . ILE C  1 78  ? 11.252 -32.340 86.480  1.00 35.79  ? 93  ILE C CA  1 
ATOM   4530 C C   . ILE C  1 78  ? 12.548 -31.900 87.169  1.00 34.73  ? 93  ILE C C   1 
ATOM   4531 O O   . ILE C  1 78  ? 13.628 -32.106 86.591  1.00 35.05  ? 93  ILE C O   1 
ATOM   4532 C CB  . ILE C  1 78  ? 11.295 -33.832 86.081  1.00 35.77  ? 93  ILE C CB  1 
ATOM   4533 C CG1 . ILE C  1 78  ? 10.209 -34.194 85.060  1.00 37.91  ? 93  ILE C CG1 1 
ATOM   4534 C CG2 . ILE C  1 78  ? 11.237 -34.681 87.345  1.00 36.58  ? 93  ILE C CG2 1 
ATOM   4535 C CD1 . ILE C  1 78  ? 10.115 -35.677 84.720  1.00 39.13  ? 93  ILE C CD1 1 
ATOM   4536 N N   . VAL C  1 79  ? 12.428 -31.266 88.340  1.00 35.58  ? 94  VAL C N   1 
ATOM   4537 C CA  . VAL C  1 79  ? 13.578 -30.858 89.196  1.00 36.25  ? 94  VAL C CA  1 
ATOM   4538 C C   . VAL C  1 79  ? 13.744 -31.928 90.272  1.00 35.13  ? 94  VAL C C   1 
ATOM   4539 O O   . VAL C  1 79  ? 12.728 -32.361 90.826  1.00 37.59  ? 94  VAL C O   1 
ATOM   4540 C CB  . VAL C  1 79  ? 13.358 -29.454 89.789  1.00 35.48  ? 94  VAL C CB  1 
ATOM   4541 C CG1 . VAL C  1 79  ? 14.385 -29.099 90.854  1.00 37.01  ? 94  VAL C CG1 1 
ATOM   4542 C CG2 . VAL C  1 79  ? 13.343 -28.411 88.690  1.00 35.58  ? 94  VAL C CG2 1 
ATOM   4543 N N   . HIS C  1 80  ? 14.980 -32.339 90.542  1.00 35.95  ? 95  HIS C N   1 
ATOM   4544 C CA  . HIS C  1 80  ? 15.282 -33.329 91.607  1.00 35.11  ? 95  HIS C CA  1 
ATOM   4545 C C   . HIS C  1 80  ? 14.634 -32.837 92.903  1.00 36.57  ? 95  HIS C C   1 
ATOM   4546 O O   . HIS C  1 80  ? 14.880 -31.702 93.321  1.00 35.59  ? 95  HIS C O   1 
ATOM   4547 C CB  . HIS C  1 80  ? 16.789 -33.568 91.754  1.00 34.06  ? 95  HIS C CB  1 
ATOM   4548 C CG  . HIS C  1 80  ? 17.096 -34.877 92.396  1.00 35.10  ? 95  HIS C CG  1 
ATOM   4549 N ND1 . HIS C  1 80  ? 16.802 -35.143 93.721  1.00 34.88  ? 95  HIS C ND1 1 
ATOM   4550 C CD2 . HIS C  1 80  ? 17.636 -36.007 91.891  1.00 35.42  ? 95  HIS C CD2 1 
ATOM   4551 C CE1 . HIS C  1 80  ? 17.158 -36.379 94.007  1.00 34.45  ? 95  HIS C CE1 1 
ATOM   4552 N NE2 . HIS C  1 80  ? 17.688 -36.928 92.906  1.00 35.46  ? 95  HIS C NE2 1 
ATOM   4553 N N   . PRO C  1 81  ? 13.782 -33.649 93.575  1.00 37.11  ? 96  PRO C N   1 
ATOM   4554 C CA  . PRO C  1 81  ? 13.075 -33.188 94.771  1.00 35.57  ? 96  PRO C CA  1 
ATOM   4555 C C   . PRO C  1 81  ? 13.988 -32.861 95.966  1.00 34.17  ? 96  PRO C C   1 
ATOM   4556 O O   . PRO C  1 81  ? 13.539 -32.176 96.845  1.00 35.27  ? 96  PRO C O   1 
ATOM   4557 C CB  . PRO C  1 81  ? 12.105 -34.339 95.091  1.00 36.23  ? 96  PRO C CB  1 
ATOM   4558 C CG  . PRO C  1 81  ? 12.734 -35.559 94.458  1.00 36.74  ? 96  PRO C CG  1 
ATOM   4559 C CD  . PRO C  1 81  ? 13.450 -35.041 93.229  1.00 37.78  ? 96  PRO C CD  1 
ATOM   4560 N N   . GLN C  1 82  ? 15.246 -33.302 95.947  1.00 34.82  ? 97  GLN C N   1 
ATOM   4561 C CA  . GLN C  1 82  ? 16.241 -33.017 97.011  1.00 36.28  ? 97  GLN C CA  1 
ATOM   4562 C C   . GLN C  1 82  ? 16.890 -31.646 96.776  1.00 36.54  ? 97  GLN C C   1 
ATOM   4563 O O   . GLN C  1 82  ? 17.574 -31.197 97.697  1.00 38.08  ? 97  GLN C O   1 
ATOM   4564 C CB  . GLN C  1 82  ? 17.243 -34.173 97.120  1.00 37.89  ? 97  GLN C CB  1 
ATOM   4565 C CG  . GLN C  1 82  ? 16.575 -35.480 97.567  1.00 38.73  ? 97  GLN C CG  1 
ATOM   4566 C CD  . GLN C  1 82  ? 17.418 -36.737 97.590  1.00 41.77  ? 97  GLN C CD  1 
ATOM   4567 O OE1 . GLN C  1 82  ? 16.936 -37.798 97.971  1.00 45.76  ? 97  GLN C OE1 1 
ATOM   4568 N NE2 . GLN C  1 82  ? 18.678 -36.660 97.198  1.00 43.21  ? 97  GLN C NE2 1 
ATOM   4569 N N   . PHE C  1 83  ? 16.655 -30.976 95.638  1.00 34.31  ? 98  PHE C N   1 
ATOM   4570 C CA  . PHE C  1 83  ? 17.323 -29.686 95.310  1.00 32.32  ? 98  PHE C CA  1 
ATOM   4571 C C   . PHE C  1 83  ? 16.692 -28.511 96.066  1.00 31.33  ? 98  PHE C C   1 
ATOM   4572 O O   . PHE C  1 83  ? 15.455 -28.331 96.019  1.00 29.60  ? 98  PHE C O   1 
ATOM   4573 C CB  . PHE C  1 83  ? 17.245 -29.360 93.821  1.00 31.09  ? 98  PHE C CB  1 
ATOM   4574 C CG  . PHE C  1 83  ? 17.822 -28.011 93.478  1.00 30.12  ? 98  PHE C CG  1 
ATOM   4575 C CD1 . PHE C  1 83  ? 19.192 -27.793 93.511  1.00 29.18  ? 98  PHE C CD1 1 
ATOM   4576 C CD2 . PHE C  1 83  ? 16.989 -26.944 93.175  1.00 30.06  ? 98  PHE C CD2 1 
ATOM   4577 C CE1 . PHE C  1 83  ? 19.720 -26.547 93.210  1.00 27.90  ? 98  PHE C CE1 1 
ATOM   4578 C CE2 . PHE C  1 83  ? 17.520 -25.700 92.862  1.00 29.05  ? 98  PHE C CE2 1 
ATOM   4579 C CZ  . PHE C  1 83  ? 18.882 -25.504 92.886  1.00 28.73  ? 98  PHE C CZ  1 
ATOM   4580 N N   . TYR C  1 84  ? 17.537 -27.678 96.680  1.00 30.69  ? 99  TYR C N   1 
ATOM   4581 C CA  . TYR C  1 84  ? 17.162 -26.313 97.123  1.00 32.53  ? 99  TYR C CA  1 
ATOM   4582 C C   . TYR C  1 84  ? 18.217 -25.294 96.651  1.00 31.59  ? 99  TYR C C   1 
ATOM   4583 O O   . TYR C  1 84  ? 17.798 -24.270 96.111  1.00 29.07  ? 99  TYR C O   1 
ATOM   4584 C CB  . TYR C  1 84  ? 16.871 -26.263 98.630  1.00 32.24  ? 99  TYR C CB  1 
ATOM   4585 C CG  . TYR C  1 84  ? 16.305 -24.924 99.014  1.00 31.97  ? 99  TYR C CG  1 
ATOM   4586 C CD1 . TYR C  1 84  ? 15.064 -24.526 98.546  1.00 33.05  ? 99  TYR C CD1 1 
ATOM   4587 C CD2 . TYR C  1 84  ? 17.050 -24.011 99.740  1.00 34.06  ? 99  TYR C CD2 1 
ATOM   4588 C CE1 . TYR C  1 84  ? 14.557 -23.266 98.818  1.00 33.00  ? 99  TYR C CE1 1 
ATOM   4589 C CE2 . TYR C  1 84  ? 16.555 -22.749 100.029 1.00 34.42  ? 99  TYR C CE2 1 
ATOM   4590 C CZ  . TYR C  1 84  ? 15.305 -22.376 99.566  1.00 34.37  ? 99  TYR C CZ  1 
ATOM   4591 O OH  . TYR C  1 84  ? 14.804 -21.134 99.827  1.00 37.19  ? 99  TYR C OH  1 
ATOM   4592 N N   . THR C  1 85  ? 19.514 -25.545 96.858  1.00 30.82  ? 100 THR C N   1 
ATOM   4593 C CA  . THR C  1 85  ? 20.625 -24.703 96.327  1.00 31.48  ? 100 THR C CA  1 
ATOM   4594 C C   . THR C  1 85  ? 21.699 -25.603 95.719  1.00 30.46  ? 100 THR C C   1 
ATOM   4595 O O   . THR C  1 85  ? 21.801 -26.771 96.139  1.00 30.29  ? 100 THR C O   1 
ATOM   4596 C CB  . THR C  1 85  ? 21.253 -23.786 97.392  1.00 31.80  ? 100 THR C CB  1 
ATOM   4597 O OG1 . THR C  1 85  ? 22.101 -24.557 98.245  1.00 32.72  ? 100 THR C OG1 1 
ATOM   4598 C CG2 . THR C  1 85  ? 20.232 -23.061 98.240  1.00 31.62  ? 100 THR C CG2 1 
ATOM   4599 N N   . ALA C  1 86  ? 22.487 -25.055 94.791  1.00 31.19  ? 101 ALA C N   1 
ATOM   4600 C CA  . ALA C  1 86  ? 23.596 -25.756 94.098  1.00 32.67  ? 101 ALA C CA  1 
ATOM   4601 C C   . ALA C  1 86  ? 24.654 -26.219 95.108  1.00 32.79  ? 101 ALA C C   1 
ATOM   4602 O O   . ALA C  1 86  ? 25.202 -27.320 94.911  1.00 36.68  ? 101 ALA C O   1 
ATOM   4603 C CB  . ALA C  1 86  ? 24.203 -24.866 93.041  1.00 34.45  ? 101 ALA C CB  1 
ATOM   4604 N N   . GLN C  1 87  ? 24.904 -25.439 96.164  1.00 33.00  ? 102 GLN C N   1 
ATOM   4605 C CA  . GLN C  1 87  ? 25.976 -25.714 97.166  1.00 32.48  ? 102 GLN C CA  1 
ATOM   4606 C C   . GLN C  1 87  ? 25.557 -26.887 98.062  1.00 31.95  ? 102 GLN C C   1 
ATOM   4607 O O   . GLN C  1 87  ? 26.447 -27.604 98.529  1.00 30.45  ? 102 GLN C O   1 
ATOM   4608 C CB  . GLN C  1 87  ? 26.305 -24.495 98.030  1.00 33.33  ? 102 GLN C CB  1 
ATOM   4609 C CG  . GLN C  1 87  ? 26.947 -23.337 97.279  1.00 33.12  ? 102 GLN C CG  1 
ATOM   4610 C CD  . GLN C  1 87  ? 26.004 -22.492 96.454  1.00 35.30  ? 102 GLN C CD  1 
ATOM   4611 O OE1 . GLN C  1 87  ? 26.375 -22.007 95.388  1.00 41.51  ? 102 GLN C OE1 1 
ATOM   4612 N NE2 . GLN C  1 87  ? 24.780 -22.298 96.920  1.00 34.17  ? 102 GLN C NE2 1 
ATOM   4613 N N   . ILE C  1 88  ? 24.257 -27.076 98.299  1.00 31.82  ? 103 ILE C N   1 
ATOM   4614 C CA  . ILE C  1 88  ? 23.716 -28.248 99.048  1.00 33.52  ? 103 ILE C CA  1 
ATOM   4615 C C   . ILE C  1 88  ? 23.773 -29.479 98.133  1.00 33.24  ? 103 ILE C C   1 
ATOM   4616 O O   . ILE C  1 88  ? 24.157 -30.554 98.620  1.00 34.15  ? 103 ILE C O   1 
ATOM   4617 C CB  . ILE C  1 88  ? 22.304 -27.950 99.599  1.00 34.38  ? 103 ILE C CB  1 
ATOM   4618 C CG1 . ILE C  1 88  ? 22.356 -26.837 100.650 1.00 35.08  ? 103 ILE C CG1 1 
ATOM   4619 C CG2 . ILE C  1 88  ? 21.651 -29.213 100.156 1.00 33.66  ? 103 ILE C CG2 1 
ATOM   4620 C CD1 . ILE C  1 88  ? 21.024 -26.188 100.957 1.00 36.04  ? 103 ILE C CD1 1 
ATOM   4621 N N   . GLY C  1 89  ? 23.376 -29.334 96.868  1.00 33.63  ? 104 GLY C N   1 
ATOM   4622 C CA  . GLY C  1 89  ? 23.531 -30.358 95.816  1.00 33.33  ? 104 GLY C CA  1 
ATOM   4623 C C   . GLY C  1 89  ? 22.201 -30.783 95.226  1.00 31.72  ? 104 GLY C C   1 
ATOM   4624 O O   . GLY C  1 89  ? 21.204 -30.050 95.413  1.00 32.78  ? 104 GLY C O   1 
ATOM   4625 N N   . ALA C  1 90  ? 22.196 -31.934 94.545  1.00 32.20  ? 105 ALA C N   1 
ATOM   4626 C CA  . ALA C  1 90  ? 21.096 -32.457 93.701  1.00 31.97  ? 105 ALA C CA  1 
ATOM   4627 C C   . ALA C  1 90  ? 20.735 -31.427 92.617  1.00 32.32  ? 105 ALA C C   1 
ATOM   4628 O O   . ALA C  1 90  ? 19.536 -31.289 92.289  1.00 32.44  ? 105 ALA C O   1 
ATOM   4629 C CB  . ALA C  1 90  ? 19.923 -32.840 94.579  1.00 32.15  ? 105 ALA C CB  1 
ATOM   4630 N N   . ASP C  1 91  ? 21.747 -30.752 92.061  1.00 31.65  ? 106 ASP C N   1 
ATOM   4631 C CA  . ASP C  1 91  ? 21.564 -29.656 91.078  1.00 31.57  ? 106 ASP C CA  1 
ATOM   4632 C C   . ASP C  1 91  ? 21.414 -30.296 89.694  1.00 33.04  ? 106 ASP C C   1 
ATOM   4633 O O   . ASP C  1 91  ? 22.373 -30.281 88.892  1.00 31.13  ? 106 ASP C O   1 
ATOM   4634 C CB  . ASP C  1 91  ? 22.675 -28.608 91.166  1.00 31.84  ? 106 ASP C CB  1 
ATOM   4635 C CG  . ASP C  1 91  ? 22.365 -27.354 90.365  1.00 31.92  ? 106 ASP C CG  1 
ATOM   4636 O OD1 . ASP C  1 91  ? 21.186 -27.161 90.003  1.00 30.49  ? 106 ASP C OD1 1 
ATOM   4637 O OD2 . ASP C  1 91  ? 23.299 -26.585 90.103  1.00 33.33  ? 106 ASP C OD2 1 
ATOM   4638 N N   . ILE C  1 92  ? 20.234 -30.861 89.446  1.00 31.64  ? 107 ILE C N   1 
ATOM   4639 C CA  . ILE C  1 92  ? 19.934 -31.643 88.215  1.00 31.03  ? 107 ILE C CA  1 
ATOM   4640 C C   . ILE C  1 92  ? 18.430 -31.552 87.955  1.00 30.58  ? 107 ILE C C   1 
ATOM   4641 O O   . ILE C  1 92  ? 17.644 -31.638 88.922  1.00 28.76  ? 107 ILE C O   1 
ATOM   4642 C CB  . ILE C  1 92  ? 20.457 -33.090 88.339  1.00 32.66  ? 107 ILE C CB  1 
ATOM   4643 C CG1 . ILE C  1 92  ? 20.497 -33.805 86.984  1.00 32.22  ? 107 ILE C CG1 1 
ATOM   4644 C CG2 . ILE C  1 92  ? 19.684 -33.888 89.389  1.00 33.45  ? 107 ILE C CG2 1 
ATOM   4645 C CD1 . ILE C  1 92  ? 21.386 -35.025 86.976  1.00 32.88  ? 107 ILE C CD1 1 
ATOM   4646 N N   . ALA C  1 93  ? 18.071 -31.323 86.692  1.00 31.71  ? 108 ALA C N   1 
ATOM   4647 C CA  . ALA C  1 93  ? 16.680 -31.243 86.215  1.00 30.98  ? 108 ALA C CA  1 
ATOM   4648 C C   . ALA C  1 93  ? 16.577 -31.858 84.820  1.00 31.52  ? 108 ALA C C   1 
ATOM   4649 O O   . ALA C  1 93  ? 17.613 -31.978 84.120  1.00 31.35  ? 108 ALA C O   1 
ATOM   4650 C CB  . ALA C  1 93  ? 16.212 -29.811 86.237  1.00 32.82  ? 108 ALA C CB  1 
ATOM   4651 N N   . LEU C  1 94  ? 15.357 -32.254 84.461  1.00 31.83  ? 109 LEU C N   1 
ATOM   4652 C CA  . LEU C  1 94  ? 14.993 -32.798 83.135  1.00 32.58  ? 109 LEU C CA  1 
ATOM   4653 C C   . LEU C  1 94  ? 13.923 -31.898 82.521  1.00 32.55  ? 109 LEU C C   1 
ATOM   4654 O O   . LEU C  1 94  ? 12.987 -31.516 83.245  1.00 34.95  ? 109 LEU C O   1 
ATOM   4655 C CB  . LEU C  1 94  ? 14.492 -34.234 83.314  1.00 33.20  ? 109 LEU C CB  1 
ATOM   4656 C CG  . LEU C  1 94  ? 15.570 -35.265 83.652  1.00 35.33  ? 109 LEU C CG  1 
ATOM   4657 C CD1 . LEU C  1 94  ? 14.946 -36.578 84.098  1.00 35.50  ? 109 LEU C CD1 1 
ATOM   4658 C CD2 . LEU C  1 94  ? 16.508 -35.504 82.477  1.00 36.46  ? 109 LEU C CD2 1 
ATOM   4659 N N   . LEU C  1 95  ? 14.084 -31.548 81.243  1.00 33.96  ? 110 LEU C N   1 
ATOM   4660 C CA  . LEU C  1 95  ? 13.007 -30.932 80.428  1.00 34.80  ? 110 LEU C CA  1 
ATOM   4661 C C   . LEU C  1 95  ? 12.479 -31.987 79.450  1.00 34.64  ? 110 LEU C C   1 
ATOM   4662 O O   . LEU C  1 95  ? 13.284 -32.529 78.675  1.00 34.77  ? 110 LEU C O   1 
ATOM   4663 C CB  . LEU C  1 95  ? 13.550 -29.703 79.690  1.00 34.25  ? 110 LEU C CB  1 
ATOM   4664 C CG  . LEU C  1 95  ? 14.346 -28.699 80.527  1.00 34.69  ? 110 LEU C CG  1 
ATOM   4665 C CD1 . LEU C  1 95  ? 14.723 -27.491 79.679  1.00 34.39  ? 110 LEU C CD1 1 
ATOM   4666 C CD2 . LEU C  1 95  ? 13.578 -28.255 81.766  1.00 35.06  ? 110 LEU C CD2 1 
ATOM   4667 N N   . GLU C  1 96  ? 11.184 -32.288 79.515  1.00 35.75  ? 111 GLU C N   1 
ATOM   4668 C CA  . GLU C  1 96  ? 10.495 -33.134 78.506  1.00 37.57  ? 111 GLU C CA  1 
ATOM   4669 C C   . GLU C  1 96  ? 9.979  -32.215 77.396  1.00 35.67  ? 111 GLU C C   1 
ATOM   4670 O O   . GLU C  1 96  ? 9.186  -31.315 77.700  1.00 37.56  ? 111 GLU C O   1 
ATOM   4671 C CB  . GLU C  1 96  ? 9.345  -33.916 79.143  1.00 38.65  ? 111 GLU C CB  1 
ATOM   4672 C CG  . GLU C  1 96  ? 8.814  -35.020 78.252  1.00 41.33  ? 111 GLU C CG  1 
ATOM   4673 C CD  . GLU C  1 96  ? 7.710  -35.863 78.871  1.00 44.48  ? 111 GLU C CD  1 
ATOM   4674 O OE1 . GLU C  1 96  ? 6.977  -35.352 79.748  1.00 45.72  ? 111 GLU C OE1 1 
ATOM   4675 O OE2 . GLU C  1 96  ? 7.543  -37.011 78.435  1.00 49.85  ? 111 GLU C OE2 1 
ATOM   4676 N N   . LEU C  1 97  ? 10.434 -32.411 76.161  1.00 35.80  ? 112 LEU C N   1 
ATOM   4677 C CA  . LEU C  1 97  ? 9.965  -31.624 74.986  1.00 38.77  ? 112 LEU C CA  1 
ATOM   4678 C C   . LEU C  1 97  ? 8.561  -32.123 74.611  1.00 39.90  ? 112 LEU C C   1 
ATOM   4679 O O   . LEU C  1 97  ? 8.243  -33.276 74.948  1.00 37.06  ? 112 LEU C O   1 
ATOM   4680 C CB  . LEU C  1 97  ? 10.973 -31.774 73.841  1.00 38.26  ? 112 LEU C CB  1 
ATOM   4681 C CG  . LEU C  1 97  ? 12.423 -31.393 74.176  1.00 39.83  ? 112 LEU C CG  1 
ATOM   4682 C CD1 . LEU C  1 97  ? 13.343 -31.624 72.995  1.00 39.89  ? 112 LEU C CD1 1 
ATOM   4683 C CD2 . LEU C  1 97  ? 12.533 -29.951 74.642  1.00 41.02  ? 112 LEU C CD2 1 
ATOM   4684 N N   . GLU C  1 98  ? 7.739  -31.276 73.983  1.00 43.06  ? 113 GLU C N   1 
ATOM   4685 C CA  . GLU C  1 98  ? 6.383  -31.655 73.494  1.00 48.75  ? 113 GLU C CA  1 
ATOM   4686 C C   . GLU C  1 98  ? 6.494  -32.680 72.364  1.00 46.82  ? 113 GLU C C   1 
ATOM   4687 O O   . GLU C  1 98  ? 5.566  -33.483 72.226  1.00 48.46  ? 113 GLU C O   1 
ATOM   4688 C CB  . GLU C  1 98  ? 5.601  -30.446 72.992  1.00 54.16  ? 113 GLU C CB  1 
ATOM   4689 C CG  . GLU C  1 98  ? 5.115  -29.564 74.117  1.00 60.48  ? 113 GLU C CG  1 
ATOM   4690 C CD  . GLU C  1 98  ? 4.083  -28.533 73.700  1.00 67.34  ? 113 GLU C CD  1 
ATOM   4691 O OE1 . GLU C  1 98  ? 3.533  -27.860 74.593  1.00 75.03  ? 113 GLU C OE1 1 
ATOM   4692 O OE2 . GLU C  1 98  ? 3.835  -28.402 72.484  1.00 71.54  ? 113 GLU C OE2 1 
ATOM   4693 N N   . GLU C  1 99  ? 7.583  -32.638 71.591  1.00 46.70  ? 114 GLU C N   1 
ATOM   4694 C CA  . GLU C  1 99  ? 7.846  -33.576 70.469  1.00 48.91  ? 114 GLU C CA  1 
ATOM   4695 C C   . GLU C  1 99  ? 9.255  -34.132 70.599  1.00 45.62  ? 114 GLU C C   1 
ATOM   4696 O O   . GLU C  1 99  ? 10.143 -33.459 71.109  1.00 42.25  ? 114 GLU C O   1 
ATOM   4697 C CB  . GLU C  1 99  ? 7.718  -32.869 69.119  1.00 50.08  ? 114 GLU C CB  1 
ATOM   4698 C CG  . GLU C  1 99  ? 6.355  -32.259 68.884  1.00 51.85  ? 114 GLU C CG  1 
ATOM   4699 C CD  . GLU C  1 99  ? 5.252  -33.248 68.547  1.00 55.83  ? 114 GLU C CD  1 
ATOM   4700 O OE1 . GLU C  1 99  ? 4.154  -32.784 68.191  1.00 65.12  ? 114 GLU C OE1 1 
ATOM   4701 O OE2 . GLU C  1 99  ? 5.487  -34.470 68.610  1.00 53.48  ? 114 GLU C OE2 1 
ATOM   4702 N N   . PRO C  1 100 ? 9.501  -35.371 70.123  1.00 45.50  ? 115 PRO C N   1 
ATOM   4703 C CA  . PRO C  1 100 ? 10.865 -35.862 69.954  1.00 47.41  ? 115 PRO C CA  1 
ATOM   4704 C C   . PRO C  1 100 ? 11.501 -35.107 68.779  1.00 48.12  ? 115 PRO C C   1 
ATOM   4705 O O   . PRO C  1 100 ? 10.785 -34.770 67.854  1.00 49.38  ? 115 PRO C O   1 
ATOM   4706 C CB  . PRO C  1 100 ? 10.682 -37.356 69.672  1.00 46.92  ? 115 PRO C CB  1 
ATOM   4707 C CG  . PRO C  1 100 ? 9.321  -37.437 69.029  1.00 47.31  ? 115 PRO C CG  1 
ATOM   4708 C CD  . PRO C  1 100 ? 8.495  -36.359 69.703  1.00 47.16  ? 115 PRO C CD  1 
ATOM   4709 N N   . VAL C  1 101 ? 12.802 -34.830 68.847  1.00 48.45  ? 116 VAL C N   1 
ATOM   4710 C CA  . VAL C  1 101 ? 13.532 -34.146 67.743  1.00 50.42  ? 116 VAL C CA  1 
ATOM   4711 C C   . VAL C  1 101 ? 13.891 -35.215 66.706  1.00 53.59  ? 116 VAL C C   1 
ATOM   4712 O O   . VAL C  1 101 ? 14.117 -36.386 67.109  1.00 54.39  ? 116 VAL C O   1 
ATOM   4713 C CB  . VAL C  1 101 ? 14.763 -33.361 68.242  1.00 49.50  ? 116 VAL C CB  1 
ATOM   4714 C CG1 . VAL C  1 101 ? 14.416 -32.455 69.417  1.00 49.89  ? 116 VAL C CG1 1 
ATOM   4715 C CG2 . VAL C  1 101 ? 15.938 -34.253 68.604  1.00 49.95  ? 116 VAL C CG2 1 
ATOM   4716 N N   . LYS C  1 102 ? 13.889 -34.835 65.426  1.00 57.14  ? 117 LYS C N   1 
ATOM   4717 C CA  . LYS C  1 102 ? 14.431 -35.668 64.315  1.00 57.53  ? 117 LYS C CA  1 
ATOM   4718 C C   . LYS C  1 102 ? 15.952 -35.486 64.324  1.00 57.99  ? 117 LYS C C   1 
ATOM   4719 O O   . LYS C  1 102 ? 16.389 -34.353 64.072  1.00 68.22  ? 117 LYS C O   1 
ATOM   4720 C CB  . LYS C  1 102 ? 13.792 -35.274 62.977  1.00 55.43  ? 117 LYS C CB  1 
ATOM   4721 C CG  . LYS C  1 102 ? 12.304 -35.475 62.867  0.00 56.94  ? 117 LYS C CG  1 
ATOM   4722 C CD  . LYS C  1 102 ? 11.745 -35.082 61.516  0.00 56.84  ? 117 LYS C CD  1 
ATOM   4723 C CE  . LYS C  1 102 ? 10.274 -35.403 61.362  0.00 56.78  ? 117 LYS C CE  1 
ATOM   4724 N NZ  . LYS C  1 102 ? 9.758  -34.979 60.039  0.00 56.75  ? 117 LYS C NZ  1 
ATOM   4725 N N   . VAL C  1 103 ? 16.715 -36.530 64.674  1.00 59.40  ? 118 VAL C N   1 
ATOM   4726 C CA  . VAL C  1 103 ? 18.184 -36.437 64.932  1.00 57.94  ? 118 VAL C CA  1 
ATOM   4727 C C   . VAL C  1 103 ? 18.933 -36.491 63.593  1.00 60.54  ? 118 VAL C C   1 
ATOM   4728 O O   . VAL C  1 103 ? 18.374 -37.021 62.606  1.00 61.31  ? 118 VAL C O   1 
ATOM   4729 C CB  . VAL C  1 103 ? 18.685 -37.511 65.925  1.00 55.72  ? 118 VAL C CB  1 
ATOM   4730 C CG1 . VAL C  1 103 ? 17.996 -37.390 67.276  1.00 56.83  ? 118 VAL C CG1 1 
ATOM   4731 C CG2 . VAL C  1 103 ? 18.565 -38.937 65.402  1.00 55.42  ? 118 VAL C CG2 1 
ATOM   4732 N N   . SER C  1 104 ? 20.139 -35.925 63.573  1.00 60.65  ? 119 SER C N   1 
ATOM   4733 C CA  . SER C  1 104 ? 21.045 -35.845 62.399  1.00 62.97  ? 119 SER C CA  1 
ATOM   4734 C C   . SER C  1 104 ? 22.495 -35.842 62.893  1.00 64.85  ? 119 SER C C   1 
ATOM   4735 O O   . SER C  1 104 ? 22.694 -35.917 64.117  1.00 69.53  ? 119 SER C O   1 
ATOM   4736 C CB  . SER C  1 104 ? 20.727 -34.628 61.571  1.00 60.82  ? 119 SER C CB  1 
ATOM   4737 O OG  . SER C  1 104 ? 20.847 -33.439 62.336  1.00 57.48  ? 119 SER C OG  1 
ATOM   4738 N N   . SER C  1 105 ? 23.472 -35.761 61.987  1.00 67.31  ? 120 SER C N   1 
ATOM   4739 C CA  . SER C  1 105 ? 24.915 -35.625 62.328  1.00 67.61  ? 120 SER C CA  1 
ATOM   4740 C C   . SER C  1 105 ? 25.154 -34.305 63.080  1.00 65.64  ? 120 SER C C   1 
ATOM   4741 O O   . SER C  1 105 ? 26.043 -34.286 63.961  1.00 71.20  ? 120 SER C O   1 
ATOM   4742 C CB  . SER C  1 105 ? 25.783 -35.735 61.096  1.00 69.50  ? 120 SER C CB  1 
ATOM   4743 O OG  . SER C  1 105 ? 25.603 -34.612 60.248  1.00 71.27  ? 120 SER C OG  1 
ATOM   4744 N N   . HIS C  1 106 ? 24.384 -33.253 62.756  1.00 61.70  ? 121 HIS C N   1 
ATOM   4745 C CA  . HIS C  1 106 ? 24.512 -31.875 63.313  1.00 61.12  ? 121 HIS C CA  1 
ATOM   4746 C C   . HIS C  1 106 ? 23.752 -31.721 64.642  1.00 60.67  ? 121 HIS C C   1 
ATOM   4747 O O   . HIS C  1 106 ? 24.164 -30.862 65.446  1.00 63.69  ? 121 HIS C O   1 
ATOM   4748 C CB  . HIS C  1 106 ? 24.050 -30.833 62.282  1.00 61.56  ? 121 HIS C CB  1 
ATOM   4749 C CG  . HIS C  1 106 ? 24.388 -29.422 62.628  0.00 62.56  ? 121 HIS C CG  1 
ATOM   4750 N ND1 . HIS C  1 106 ? 25.657 -28.901 62.458  0.00 62.51  ? 121 HIS C ND1 1 
ATOM   4751 C CD2 . HIS C  1 106 ? 23.629 -28.417 63.116  0.00 62.58  ? 121 HIS C CD2 1 
ATOM   4752 C CE1 . HIS C  1 106 ? 25.667 -27.640 62.838  0.00 62.51  ? 121 HIS C CE1 1 
ATOM   4753 N NE2 . HIS C  1 106 ? 24.434 -27.318 63.246  0.00 62.54  ? 121 HIS C NE2 1 
ATOM   4754 N N   . VAL C  1 107 ? 22.674 -32.485 64.859  1.00 57.67  ? 122 VAL C N   1 
ATOM   4755 C CA  . VAL C  1 107 ? 21.841 -32.448 66.100  1.00 55.02  ? 122 VAL C CA  1 
ATOM   4756 C C   . VAL C  1 107 ? 21.535 -33.887 66.533  1.00 54.81  ? 122 VAL C C   1 
ATOM   4757 O O   . VAL C  1 107 ? 20.713 -34.542 65.855  1.00 54.59  ? 122 VAL C O   1 
ATOM   4758 C CB  . VAL C  1 107 ? 20.548 -31.639 65.879  1.00 57.20  ? 122 VAL C CB  1 
ATOM   4759 C CG1 . VAL C  1 107 ? 19.592 -31.727 67.059  1.00 56.54  ? 122 VAL C CG1 1 
ATOM   4760 C CG2 . VAL C  1 107 ? 20.850 -30.183 65.560  1.00 59.74  ? 122 VAL C CG2 1 
ATOM   4761 N N   . HIS C  1 108 ? 22.143 -34.355 67.627  1.00 52.19  ? 123 HIS C N   1 
ATOM   4762 C CA  . HIS C  1 108 ? 21.874 -35.704 68.194  1.00 52.43  ? 123 HIS C CA  1 
ATOM   4763 C C   . HIS C  1 108 ? 22.295 -35.780 69.667  1.00 47.11  ? 123 HIS C C   1 
ATOM   4764 O O   . HIS C  1 108 ? 22.906 -34.820 70.168  1.00 44.13  ? 123 HIS C O   1 
ATOM   4765 C CB  . HIS C  1 108 ? 22.474 -36.810 67.309  1.00 54.98  ? 123 HIS C CB  1 
ATOM   4766 C CG  . HIS C  1 108 ? 23.961 -36.901 67.265  1.00 56.82  ? 123 HIS C CG  1 
ATOM   4767 N ND1 . HIS C  1 108 ? 24.689 -36.484 66.163  1.00 61.94  ? 123 HIS C ND1 1 
ATOM   4768 C CD2 . HIS C  1 108 ? 24.850 -37.432 68.133  1.00 59.73  ? 123 HIS C CD2 1 
ATOM   4769 C CE1 . HIS C  1 108 ? 25.968 -36.723 66.370  1.00 63.52  ? 123 HIS C CE1 1 
ATOM   4770 N NE2 . HIS C  1 108 ? 26.096 -37.297 67.578  1.00 62.56  ? 123 HIS C NE2 1 
ATOM   4771 N N   . THR C  1 109 ? 21.941 -36.885 70.329  1.00 41.65  ? 124 THR C N   1 
ATOM   4772 C CA  . THR C  1 109 ? 22.021 -37.046 71.802  1.00 39.23  ? 124 THR C CA  1 
ATOM   4773 C C   . THR C  1 109 ? 23.472 -37.277 72.227  1.00 37.60  ? 124 THR C C   1 
ATOM   4774 O O   . THR C  1 109 ? 24.271 -37.776 71.401  1.00 37.12  ? 124 THR C O   1 
ATOM   4775 C CB  . THR C  1 109 ? 21.137 -38.192 72.306  1.00 39.34  ? 124 THR C CB  1 
ATOM   4776 O OG1 . THR C  1 109 ? 21.632 -39.404 71.743  1.00 43.81  ? 124 THR C OG1 1 
ATOM   4777 C CG2 . THR C  1 109 ? 19.678 -38.030 71.952  1.00 38.53  ? 124 THR C CG2 1 
ATOM   4778 N N   . VAL C  1 110 ? 23.795 -36.908 73.469  1.00 35.54  ? 125 VAL C N   1 
ATOM   4779 C CA  . VAL C  1 110 ? 25.039 -37.333 74.175  1.00 35.76  ? 125 VAL C CA  1 
ATOM   4780 C C   . VAL C  1 110 ? 24.740 -38.661 74.887  1.00 35.93  ? 125 VAL C C   1 
ATOM   4781 O O   . VAL C  1 110 ? 23.585 -38.862 75.300  1.00 35.99  ? 125 VAL C O   1 
ATOM   4782 C CB  . VAL C  1 110 ? 25.546 -36.250 75.152  1.00 34.91  ? 125 VAL C CB  1 
ATOM   4783 C CG1 . VAL C  1 110 ? 24.652 -36.072 76.374  1.00 35.26  ? 125 VAL C CG1 1 
ATOM   4784 C CG2 . VAL C  1 110 ? 26.985 -36.503 75.572  1.00 35.61  ? 125 VAL C CG2 1 
ATOM   4785 N N   . THR C  1 111 ? 25.747 -39.519 75.028  1.00 37.52  ? 126 THR C N   1 
ATOM   4786 C CA  . THR C  1 111 ? 25.663 -40.803 75.775  1.00 39.37  ? 126 THR C CA  1 
ATOM   4787 C C   . THR C  1 111 ? 25.925 -40.521 77.259  1.00 38.88  ? 126 THR C C   1 
ATOM   4788 O O   . THR C  1 111 ? 26.890 -39.791 77.559  1.00 37.42  ? 126 THR C O   1 
ATOM   4789 C CB  . THR C  1 111 ? 26.633 -41.839 75.193  1.00 41.11  ? 126 THR C CB  1 
ATOM   4790 O OG1 . THR C  1 111 ? 26.330 -41.955 73.800  1.00 44.38  ? 126 THR C OG1 1 
ATOM   4791 C CG2 . THR C  1 111 ? 26.530 -43.204 75.844  1.00 41.74  ? 126 THR C CG2 1 
ATOM   4792 N N   . LEU C  1 112 ? 25.093 -41.065 78.147  1.00 36.92  ? 127 LEU C N   1 
ATOM   4793 C CA  . LEU C  1 112 ? 25.334 -41.022 79.614  1.00 40.40  ? 127 LEU C CA  1 
ATOM   4794 C C   . LEU C  1 112 ? 26.299 -42.141 79.985  1.00 39.57  ? 127 LEU C C   1 
ATOM   4795 O O   . LEU C  1 112 ? 26.270 -43.213 79.386  1.00 38.79  ? 127 LEU C O   1 
ATOM   4796 C CB  . LEU C  1 112 ? 24.007 -41.129 80.372  1.00 39.66  ? 127 LEU C CB  1 
ATOM   4797 C CG  . LEU C  1 112 ? 22.997 -40.029 80.051  1.00 42.76  ? 127 LEU C CG  1 
ATOM   4798 C CD1 . LEU C  1 112 ? 21.750 -40.160 80.909  1.00 45.34  ? 127 LEU C CD1 1 
ATOM   4799 C CD2 . LEU C  1 112 ? 23.612 -38.646 80.217  1.00 42.48  ? 127 LEU C CD2 1 
ATOM   4800 N N   . PRO C  1 113 ? 27.187 -41.925 80.980  1.00 38.97  ? 128 PRO C N   1 
ATOM   4801 C CA  . PRO C  1 113 ? 28.128 -42.957 81.410  1.00 41.38  ? 128 PRO C CA  1 
ATOM   4802 C C   . PRO C  1 113 ? 27.407 -44.072 82.162  1.00 40.96  ? 128 PRO C C   1 
ATOM   4803 O O   . PRO C  1 113 ? 26.314 -43.857 82.680  1.00 40.91  ? 128 PRO C O   1 
ATOM   4804 C CB  . PRO C  1 113 ? 29.111 -42.218 82.327  1.00 40.11  ? 128 PRO C CB  1 
ATOM   4805 C CG  . PRO C  1 113 ? 28.328 -41.024 82.835  1.00 39.49  ? 128 PRO C CG  1 
ATOM   4806 C CD  . PRO C  1 113 ? 27.335 -40.684 81.748  1.00 39.80  ? 128 PRO C CD  1 
ATOM   4807 N N   . PRO C  1 114 ? 27.982 -45.293 82.234  1.00 44.77  ? 129 PRO C N   1 
ATOM   4808 C CA  . PRO C  1 114 ? 27.462 -46.322 83.135  1.00 45.94  ? 129 PRO C CA  1 
ATOM   4809 C C   . PRO C  1 114 ? 27.735 -45.911 84.591  1.00 47.83  ? 129 PRO C C   1 
ATOM   4810 O O   . PRO C  1 114 ? 28.637 -45.118 84.812  1.00 49.74  ? 129 PRO C O   1 
ATOM   4811 C CB  . PRO C  1 114 ? 28.232 -47.586 82.728  1.00 47.37  ? 129 PRO C CB  1 
ATOM   4812 C CG  . PRO C  1 114 ? 29.526 -47.063 82.134  1.00 48.39  ? 129 PRO C CG  1 
ATOM   4813 C CD  . PRO C  1 114 ? 29.157 -45.749 81.473  1.00 46.75  ? 129 PRO C CD  1 
ATOM   4814 N N   . ALA C  1 115 ? 26.969 -46.464 85.536  1.00 49.52  ? 130 ALA C N   1 
ATOM   4815 C CA  . ALA C  1 115 ? 27.089 -46.232 86.999  1.00 51.68  ? 130 ALA C CA  1 
ATOM   4816 C C   . ALA C  1 115 ? 28.519 -46.503 87.482  1.00 52.63  ? 130 ALA C C   1 
ATOM   4817 O O   . ALA C  1 115 ? 28.984 -45.759 88.357  1.00 56.21  ? 130 ALA C O   1 
ATOM   4818 C CB  . ALA C  1 115 ? 26.087 -47.085 87.737  1.00 52.26  ? 130 ALA C CB  1 
ATOM   4819 N N   . SER C  1 116 ? 29.204 -47.494 86.903  1.00 55.03  ? 131 SER C N   1 
ATOM   4820 C CA  . SER C  1 116 ? 30.569 -47.935 87.308  1.00 58.91  ? 131 SER C CA  1 
ATOM   4821 C C   . SER C  1 116 ? 31.654 -46.928 86.886  1.00 58.64  ? 131 SER C C   1 
ATOM   4822 O O   . SER C  1 116 ? 32.755 -47.001 87.451  1.00 59.17  ? 131 SER C O   1 
ATOM   4823 C CB  . SER C  1 116 ? 30.866 -49.309 86.758  1.00 59.56  ? 131 SER C CB  1 
ATOM   4824 O OG  . SER C  1 116 ? 30.711 -49.330 85.349  1.00 60.15  ? 131 SER C OG  1 
ATOM   4825 N N   . GLU C  1 117 ? 31.373 -46.036 85.929  1.00 59.21  ? 132 GLU C N   1 
ATOM   4826 C CA  . GLU C  1 117 ? 32.349 -45.112 85.292  1.00 56.41  ? 132 GLU C CA  1 
ATOM   4827 C C   . GLU C  1 117 ? 32.916 -44.133 86.328  1.00 58.69  ? 132 GLU C C   1 
ATOM   4828 O O   . GLU C  1 117 ? 32.115 -43.428 86.982  1.00 60.27  ? 132 GLU C O   1 
ATOM   4829 C CB  . GLU C  1 117 ? 31.672 -44.331 84.166  1.00 56.65  ? 132 GLU C CB  1 
ATOM   4830 C CG  . GLU C  1 117 ? 32.663 -43.666 83.238  1.00 57.16  ? 132 GLU C CG  1 
ATOM   4831 C CD  . GLU C  1 117 ? 33.376 -44.621 82.294  1.00 57.92  ? 132 GLU C CD  1 
ATOM   4832 O OE1 . GLU C  1 117 ? 32.726 -45.555 81.770  1.00 59.08  ? 132 GLU C OE1 1 
ATOM   4833 O OE2 . GLU C  1 117 ? 34.574 -44.414 82.053  1.00 55.36  ? 132 GLU C OE2 1 
ATOM   4834 N N   . THR C  1 118 ? 34.238 -44.146 86.513  1.00 61.89  ? 133 THR C N   1 
ATOM   4835 C CA  . THR C  1 118 ? 34.987 -43.212 87.392  1.00 65.07  ? 133 THR C CA  1 
ATOM   4836 C C   . THR C  1 118 ? 36.004 -42.504 86.494  1.00 62.84  ? 133 THR C C   1 
ATOM   4837 O O   . THR C  1 118 ? 37.073 -43.080 86.203  1.00 71.14  ? 133 THR C O   1 
ATOM   4838 C CB  . THR C  1 118 ? 35.588 -43.921 88.617  1.00 68.92  ? 133 THR C CB  1 
ATOM   4839 O OG1 . THR C  1 118 ? 36.513 -44.892 88.128  1.00 74.85  ? 133 THR C OG1 1 
ATOM   4840 C CG2 . THR C  1 118 ? 34.551 -44.580 89.502  1.00 70.52  ? 133 THR C CG2 1 
ATOM   4841 N N   . PHE C  1 119 ? 35.644 -41.303 86.040  1.00 56.31  ? 134 PHE C N   1 
ATOM   4842 C CA  . PHE C  1 119 ? 36.467 -40.394 85.203  1.00 50.26  ? 134 PHE C CA  1 
ATOM   4843 C C   . PHE C  1 119 ? 37.682 -39.990 86.026  1.00 49.22  ? 134 PHE C C   1 
ATOM   4844 O O   . PHE C  1 119 ? 37.536 -39.192 86.948  1.00 49.33  ? 134 PHE C O   1 
ATOM   4845 C CB  . PHE C  1 119 ? 35.667 -39.153 84.803  1.00 47.39  ? 134 PHE C CB  1 
ATOM   4846 C CG  . PHE C  1 119 ? 34.422 -39.437 84.003  1.00 45.12  ? 134 PHE C CG  1 
ATOM   4847 C CD1 . PHE C  1 119 ? 34.502 -39.641 82.635  1.00 45.30  ? 134 PHE C CD1 1 
ATOM   4848 C CD2 . PHE C  1 119 ? 33.175 -39.499 84.611  1.00 44.38  ? 134 PHE C CD2 1 
ATOM   4849 C CE1 . PHE C  1 119 ? 33.361 -39.899 81.890  1.00 45.77  ? 134 PHE C CE1 1 
ATOM   4850 C CE2 . PHE C  1 119 ? 32.038 -39.769 83.865  1.00 44.09  ? 134 PHE C CE2 1 
ATOM   4851 C CZ  . PHE C  1 119 ? 32.133 -39.967 82.507  1.00 43.64  ? 134 PHE C CZ  1 
ATOM   4852 N N   . PRO C  1 120 ? 38.896 -40.518 85.748  1.00 46.20  ? 135 PRO C N   1 
ATOM   4853 C CA  . PRO C  1 120 ? 40.026 -40.330 86.654  1.00 46.82  ? 135 PRO C CA  1 
ATOM   4854 C C   . PRO C  1 120 ? 40.533 -38.891 86.631  1.00 45.52  ? 135 PRO C C   1 
ATOM   4855 O O   . PRO C  1 120 ? 40.377 -38.192 85.635  1.00 43.75  ? 135 PRO C O   1 
ATOM   4856 C CB  . PRO C  1 120 ? 41.096 -41.298 86.133  1.00 48.10  ? 135 PRO C CB  1 
ATOM   4857 C CG  . PRO C  1 120 ? 40.771 -41.431 84.659  1.00 48.85  ? 135 PRO C CG  1 
ATOM   4858 C CD  . PRO C  1 120 ? 39.259 -41.314 84.566  1.00 48.83  ? 135 PRO C CD  1 
ATOM   4859 N N   . PRO C  1 121 ? 41.111 -38.394 87.743  1.00 45.16  ? 136 PRO C N   1 
ATOM   4860 C CA  . PRO C  1 121 ? 41.792 -37.097 87.755  1.00 45.11  ? 136 PRO C CA  1 
ATOM   4861 C C   . PRO C  1 121 ? 42.802 -36.915 86.617  1.00 43.71  ? 136 PRO C C   1 
ATOM   4862 O O   . PRO C  1 121 ? 43.491 -37.857 86.295  1.00 43.56  ? 136 PRO C O   1 
ATOM   4863 C CB  . PRO C  1 121 ? 42.514 -37.103 89.104  1.00 44.77  ? 136 PRO C CB  1 
ATOM   4864 C CG  . PRO C  1 121 ? 41.591 -37.928 89.981  1.00 46.62  ? 136 PRO C CG  1 
ATOM   4865 C CD  . PRO C  1 121 ? 41.105 -39.032 89.070  1.00 46.24  ? 136 PRO C CD  1 
ATOM   4866 N N   . GLY C  1 122 ? 42.810 -35.728 86.011  1.00 44.98  ? 137 GLY C N   1 
ATOM   4867 C CA  . GLY C  1 122 ? 43.716 -35.352 84.911  1.00 46.51  ? 137 GLY C CA  1 
ATOM   4868 C C   . GLY C  1 122 ? 43.165 -35.676 83.529  1.00 47.26  ? 137 GLY C C   1 
ATOM   4869 O O   . GLY C  1 122 ? 43.788 -35.234 82.549  1.00 49.93  ? 137 GLY C O   1 
ATOM   4870 N N   . MET C  1 123 ? 42.058 -36.425 83.431  1.00 47.74  ? 138 MET C N   1 
ATOM   4871 C CA  . MET C  1 123 ? 41.407 -36.783 82.142  1.00 51.69  ? 138 MET C CA  1 
ATOM   4872 C C   . MET C  1 123 ? 40.993 -35.491 81.435  1.00 51.11  ? 138 MET C C   1 
ATOM   4873 O O   . MET C  1 123 ? 40.357 -34.641 82.054  1.00 47.08  ? 138 MET C O   1 
ATOM   4874 C CB  . MET C  1 123 ? 40.175 -37.680 82.341  1.00 55.86  ? 138 MET C CB  1 
ATOM   4875 C CG  . MET C  1 123 ? 39.386 -37.964 81.056  1.00 61.18  ? 138 MET C CG  1 
ATOM   4876 S SD  . MET C  1 123 ? 38.298 -39.383 81.153  1.00 70.43  ? 138 MET C SD  1 
ATOM   4877 C CE  . MET C  1 123 ? 39.509 -40.686 80.935  1.00 70.82  ? 138 MET C CE  1 
ATOM   4878 N N   . PRO C  1 124 ? 41.347 -35.302 80.140  1.00 51.85  ? 139 PRO C N   1 
ATOM   4879 C CA  . PRO C  1 124 ? 40.890 -34.136 79.386  1.00 50.51  ? 139 PRO C CA  1 
ATOM   4880 C C   . PRO C  1 124 ? 39.397 -34.257 79.051  1.00 47.21  ? 139 PRO C C   1 
ATOM   4881 O O   . PRO C  1 124 ? 39.024 -35.194 78.387  1.00 50.62  ? 139 PRO C O   1 
ATOM   4882 C CB  . PRO C  1 124 ? 41.758 -34.167 78.120  1.00 53.05  ? 139 PRO C CB  1 
ATOM   4883 C CG  . PRO C  1 124 ? 42.089 -35.628 77.922  1.00 54.33  ? 139 PRO C CG  1 
ATOM   4884 C CD  . PRO C  1 124 ? 42.197 -36.189 79.323  1.00 53.34  ? 139 PRO C CD  1 
ATOM   4885 N N   . CYS C  1 125 ? 38.588 -33.334 79.565  1.00 44.72  ? 140 CYS C N   1 
ATOM   4886 C CA  . CYS C  1 125 ? 37.133 -33.214 79.282  1.00 42.29  ? 140 CYS C CA  1 
ATOM   4887 C C   . CYS C  1 125 ? 36.877 -31.838 78.664  1.00 38.74  ? 140 CYS C C   1 
ATOM   4888 O O   . CYS C  1 125 ? 37.775 -30.987 78.740  1.00 36.26  ? 140 CYS C O   1 
ATOM   4889 C CB  . CYS C  1 125 ? 36.337 -33.429 80.563  1.00 44.49  ? 140 CYS C CB  1 
ATOM   4890 S SG  . CYS C  1 125 ? 36.645 -35.056 81.302  1.00 49.00  ? 140 CYS C SG  1 
ATOM   4891 N N   . TRP C  1 126 ? 35.709 -31.643 78.054  1.00 36.72  ? 141 TRP C N   1 
ATOM   4892 C CA  . TRP C  1 126 ? 35.308 -30.375 77.400  1.00 36.48  ? 141 TRP C CA  1 
ATOM   4893 C C   . TRP C  1 126 ? 34.014 -29.869 78.027  1.00 35.32  ? 141 TRP C C   1 
ATOM   4894 O O   . TRP C  1 126 ? 33.096 -30.681 78.255  1.00 33.79  ? 141 TRP C O   1 
ATOM   4895 C CB  . TRP C  1 126 ? 35.183 -30.572 75.892  1.00 37.17  ? 141 TRP C CB  1 
ATOM   4896 C CG  . TRP C  1 126 ? 36.504 -30.844 75.244  1.00 38.98  ? 141 TRP C CG  1 
ATOM   4897 C CD1 . TRP C  1 126 ? 37.188 -32.027 75.223  1.00 39.35  ? 141 TRP C CD1 1 
ATOM   4898 C CD2 . TRP C  1 126 ? 37.319 -29.894 74.538  1.00 39.54  ? 141 TRP C CD2 1 
ATOM   4899 N NE1 . TRP C  1 126 ? 38.371 -31.877 74.550  1.00 41.04  ? 141 TRP C NE1 1 
ATOM   4900 C CE2 . TRP C  1 126 ? 38.477 -30.582 74.111  1.00 41.96  ? 141 TRP C CE2 1 
ATOM   4901 C CE3 . TRP C  1 126 ? 37.184 -28.535 74.232  1.00 40.08  ? 141 TRP C CE3 1 
ATOM   4902 C CZ2 . TRP C  1 126 ? 39.483 -29.953 73.376  1.00 42.14  ? 141 TRP C CZ2 1 
ATOM   4903 C CZ3 . TRP C  1 126 ? 38.178 -27.914 73.507  1.00 41.58  ? 141 TRP C CZ3 1 
ATOM   4904 C CH2 . TRP C  1 126 ? 39.308 -28.618 73.079  1.00 43.10  ? 141 TRP C CH2 1 
ATOM   4905 N N   . VAL C  1 127 ? 33.965 -28.564 78.284  1.00 34.34  ? 142 VAL C N   1 
ATOM   4906 C CA  . VAL C  1 127 ? 32.716 -27.854 78.665  1.00 33.78  ? 142 VAL C CA  1 
ATOM   4907 C C   . VAL C  1 127 ? 32.425 -26.828 77.568  1.00 33.47  ? 142 VAL C C   1 
ATOM   4908 O O   . VAL C  1 127 ? 33.384 -26.246 77.013  1.00 34.07  ? 142 VAL C O   1 
ATOM   4909 C CB  . VAL C  1 127 ? 32.783 -27.253 80.083  1.00 33.39  ? 142 VAL C CB  1 
ATOM   4910 C CG1 . VAL C  1 127 ? 33.832 -26.161 80.219  1.00 35.53  ? 142 VAL C CG1 1 
ATOM   4911 C CG2 . VAL C  1 127 ? 31.414 -26.753 80.534  1.00 33.86  ? 142 VAL C CG2 1 
ATOM   4912 N N   . THR C  1 128 ? 31.142 -26.675 77.241  1.00 32.56  ? 143 THR C N   1 
ATOM   4913 C CA  . THR C  1 128 ? 30.644 -25.871 76.102  1.00 32.54  ? 143 THR C CA  1 
ATOM   4914 C C   . THR C  1 128 ? 29.508 -24.968 76.588  1.00 31.25  ? 143 THR C C   1 
ATOM   4915 O O   . THR C  1 128 ? 28.804 -25.354 77.548  1.00 30.12  ? 143 THR C O   1 
ATOM   4916 C CB  . THR C  1 128 ? 30.231 -26.788 74.942  1.00 33.02  ? 143 THR C CB  1 
ATOM   4917 O OG1 . THR C  1 128 ? 29.275 -27.745 75.389  1.00 33.49  ? 143 THR C OG1 1 
ATOM   4918 C CG2 . THR C  1 128 ? 31.394 -27.564 74.368  1.00 33.36  ? 143 THR C CG2 1 
ATOM   4919 N N   . GLY C  1 129 ? 29.349 -23.798 75.964  1.00 30.77  ? 144 GLY C N   1 
ATOM   4920 C CA  . GLY C  1 129 ? 28.154 -22.961 76.180  1.00 31.95  ? 144 GLY C CA  1 
ATOM   4921 C C   . GLY C  1 129 ? 28.303 -21.548 75.662  1.00 31.61  ? 144 GLY C C   1 
ATOM   4922 O O   . GLY C  1 129 ? 29.367 -21.223 75.083  1.00 31.70  ? 144 GLY C O   1 
ATOM   4923 N N   . TRP C  1 130 ? 27.268 -20.737 75.893  1.00 32.81  ? 145 TRP C N   1 
ATOM   4924 C CA  . TRP C  1 130 ? 27.185 -19.324 75.446  1.00 34.99  ? 145 TRP C CA  1 
ATOM   4925 C C   . TRP C  1 130 ? 27.299 -18.379 76.645  1.00 37.22  ? 145 TRP C C   1 
ATOM   4926 O O   . TRP C  1 130 ? 26.826 -17.228 76.538  1.00 38.99  ? 145 TRP C O   1 
ATOM   4927 C CB  . TRP C  1 130 ? 25.886 -19.103 74.675  1.00 34.19  ? 145 TRP C CB  1 
ATOM   4928 C CG  . TRP C  1 130 ? 25.758 -19.899 73.412  1.00 34.32  ? 145 TRP C CG  1 
ATOM   4929 C CD1 . TRP C  1 130 ? 26.208 -19.558 72.171  1.00 34.99  ? 145 TRP C CD1 1 
ATOM   4930 C CD2 . TRP C  1 130 ? 25.068 -21.150 73.255  1.00 33.45  ? 145 TRP C CD2 1 
ATOM   4931 N NE1 . TRP C  1 130 ? 25.853 -20.510 71.254  1.00 34.99  ? 145 TRP C NE1 1 
ATOM   4932 C CE2 . TRP C  1 130 ? 25.150 -21.499 71.888  1.00 33.91  ? 145 TRP C CE2 1 
ATOM   4933 C CE3 . TRP C  1 130 ? 24.404 -22.012 74.135  1.00 33.01  ? 145 TRP C CE3 1 
ATOM   4934 C CZ2 . TRP C  1 130 ? 24.587 -22.674 71.388  1.00 33.14  ? 145 TRP C CZ2 1 
ATOM   4935 C CZ3 . TRP C  1 130 ? 23.851 -23.173 73.639  1.00 34.92  ? 145 TRP C CZ3 1 
ATOM   4936 C CH2 . TRP C  1 130 ? 23.935 -23.494 72.282  1.00 35.18  ? 145 TRP C CH2 1 
ATOM   4937 N N   . GLY C  1 131 ? 27.925 -18.835 77.733  1.00 35.24  ? 146 GLY C N   1 
ATOM   4938 C CA  . GLY C  1 131 ? 28.064 -18.052 78.970  1.00 35.87  ? 146 GLY C CA  1 
ATOM   4939 C C   . GLY C  1 131 ? 29.158 -17.001 78.864  1.00 36.66  ? 146 GLY C C   1 
ATOM   4940 O O   . GLY C  1 131 ? 29.819 -16.901 77.795  1.00 34.52  ? 146 GLY C O   1 
ATOM   4941 N N   . ASP C  1 132 ? 29.355 -16.266 79.959  1.00 36.49  ? 147 ASP C N   1 
ATOM   4942 C CA  . ASP C  1 132 ? 30.300 -15.129 80.072  1.00 36.92  ? 147 ASP C CA  1 
ATOM   4943 C C   . ASP C  1 132 ? 31.718 -15.610 79.743  1.00 37.71  ? 147 ASP C C   1 
ATOM   4944 O O   . ASP C  1 132 ? 32.042 -16.770 80.053  1.00 35.30  ? 147 ASP C O   1 
ATOM   4945 C CB  . ASP C  1 132 ? 30.190 -14.491 81.460  1.00 37.39  ? 147 ASP C CB  1 
ATOM   4946 C CG  . ASP C  1 132 ? 28.923 -13.676 81.675  1.00 38.48  ? 147 ASP C CG  1 
ATOM   4947 O OD1 . ASP C  1 132 ? 28.034 -13.689 80.798  1.00 40.13  ? 147 ASP C OD1 1 
ATOM   4948 O OD2 . ASP C  1 132 ? 28.826 -13.040 82.733  1.00 45.81  ? 147 ASP C OD2 1 
ATOM   4949 N N   . VAL C  1 133 ? 32.516 -14.746 79.111  1.00 37.32  ? 148 VAL C N   1 
ATOM   4950 C CA  . VAL C  1 133 ? 33.918 -15.047 78.702  1.00 38.05  ? 148 VAL C CA  1 
ATOM   4951 C C   . VAL C  1 133 ? 34.875 -14.681 79.843  1.00 39.25  ? 148 VAL C C   1 
ATOM   4952 O O   . VAL C  1 133 ? 36.053 -15.054 79.745  1.00 39.05  ? 148 VAL C O   1 
ATOM   4953 C CB  . VAL C  1 133 ? 34.295 -14.363 77.372  1.00 38.56  ? 148 VAL C CB  1 
ATOM   4954 C CG1 . VAL C  1 133 ? 33.423 -14.874 76.235  1.00 39.59  ? 148 VAL C CG1 1 
ATOM   4955 C CG2 . VAL C  1 133 ? 34.254 -12.841 77.442  1.00 38.43  ? 148 VAL C CG2 1 
ATOM   4956 N N   . ASP C  1 134 ? 34.384 -13.992 80.880  1.00 42.27  ? 149 ASP C N   1 
ATOM   4957 C CA  . ASP C  1 134 ? 35.116 -13.723 82.148  1.00 43.60  ? 149 ASP C CA  1 
ATOM   4958 C C   . ASP C  1 134 ? 34.116 -13.227 83.201  1.00 44.43  ? 149 ASP C C   1 
ATOM   4959 O O   . ASP C  1 134 ? 32.919 -13.111 82.867  1.00 43.47  ? 149 ASP C O   1 
ATOM   4960 C CB  . ASP C  1 134 ? 36.242 -12.706 81.930  1.00 47.91  ? 149 ASP C CB  1 
ATOM   4961 C CG  . ASP C  1 134 ? 37.500 -12.975 82.738  1.00 51.67  ? 149 ASP C CG  1 
ATOM   4962 O OD1 . ASP C  1 134 ? 37.381 -13.505 83.871  1.00 56.13  ? 149 ASP C OD1 1 
ATOM   4963 O OD2 . ASP C  1 134 ? 38.588 -12.640 82.237  1.00 58.45  ? 149 ASP C OD2 1 
ATOM   4964 N N   . ASN C  1 135 ? 34.581 -12.940 84.420  1.00 44.67  ? 150 ASN C N   1 
ATOM   4965 C CA  . ASN C  1 135 ? 33.732 -12.377 85.507  1.00 46.69  ? 150 ASN C CA  1 
ATOM   4966 C C   . ASN C  1 135 ? 33.107 -11.064 85.021  1.00 46.76  ? 150 ASN C C   1 
ATOM   4967 O O   . ASN C  1 135 ? 33.863 -10.170 84.608  1.00 45.66  ? 150 ASN C O   1 
ATOM   4968 C CB  . ASN C  1 135 ? 34.515 -12.199 86.811  1.00 46.29  ? 150 ASN C CB  1 
ATOM   4969 C CG  . ASN C  1 135 ? 34.998 -13.521 87.375  1.00 48.55  ? 150 ASN C CG  1 
ATOM   4970 O OD1 . ASN C  1 135 ? 34.201 -14.334 87.839  1.00 50.37  ? 150 ASN C OD1 1 
ATOM   4971 N ND2 . ASN C  1 135 ? 36.293 -13.771 87.302  1.00 51.51  ? 150 ASN C ND2 1 
ATOM   4972 N N   . ASP C  1 136 ? 31.773 -10.995 85.008  1.00 48.92  ? 151 ASP C N   1 
ATOM   4973 C CA  . ASP C  1 136 ? 30.971 -9.803  84.610  1.00 53.90  ? 151 ASP C CA  1 
ATOM   4974 C C   . ASP C  1 136 ? 31.318 -9.359  83.179  1.00 51.90  ? 151 ASP C C   1 
ATOM   4975 O O   . ASP C  1 136 ? 31.210 -8.154  82.904  1.00 52.46  ? 151 ASP C O   1 
ATOM   4976 C CB  . ASP C  1 136 ? 31.171 -8.660  85.610  1.00 58.10  ? 151 ASP C CB  1 
ATOM   4977 C CG  . ASP C  1 136 ? 30.964 -9.070  87.057  1.00 61.27  ? 151 ASP C CG  1 
ATOM   4978 O OD1 . ASP C  1 136 ? 29.842 -9.506  87.387  1.00 63.81  ? 151 ASP C OD1 1 
ATOM   4979 O OD2 . ASP C  1 136 ? 31.932 -8.967  87.838  1.00 67.83  ? 151 ASP C OD2 1 
ATOM   4980 N N   . GLU C  1 137 ? 31.692 -10.294 82.296  1.00 49.86  ? 152 GLU C N   1 
ATOM   4981 C CA  . GLU C  1 137 ? 32.024 -10.034 80.868  1.00 47.02  ? 152 GLU C CA  1 
ATOM   4982 C C   . GLU C  1 137 ? 31.177 -10.965 79.995  1.00 43.01  ? 152 GLU C C   1 
ATOM   4983 O O   . GLU C  1 137 ? 31.553 -12.145 79.830  1.00 38.61  ? 152 GLU C O   1 
ATOM   4984 C CB  . GLU C  1 137 ? 33.519 -10.225 80.613  1.00 51.37  ? 152 GLU C CB  1 
ATOM   4985 C CG  . GLU C  1 137 ? 34.378 -9.073  81.118  1.00 56.87  ? 152 GLU C CG  1 
ATOM   4986 C CD  . GLU C  1 137 ? 35.871 -9.204  80.848  1.00 59.17  ? 152 GLU C CD  1 
ATOM   4987 O OE1 . GLU C  1 137 ? 36.654 -8.531  81.551  1.00 60.90  ? 152 GLU C OE1 1 
ATOM   4988 O OE2 . GLU C  1 137 ? 36.251 -9.974  79.936  1.00 59.12  ? 152 GLU C OE2 1 
ATOM   4989 N N   . ARG C  1 138 ? 30.073 -10.449 79.450  1.00 40.54  ? 153 ARG C N   1 
ATOM   4990 C CA  . ARG C  1 138 ? 29.130 -11.214 78.591  1.00 43.29  ? 153 ARG C CA  1 
ATOM   4991 C C   . ARG C  1 138 ? 29.844 -11.668 77.311  1.00 40.44  ? 153 ARG C C   1 
ATOM   4992 O O   . ARG C  1 138 ? 30.826 -11.013 76.892  1.00 40.29  ? 153 ARG C O   1 
ATOM   4993 C CB  . ARG C  1 138 ? 27.877 -10.387 78.274  1.00 46.95  ? 153 ARG C CB  1 
ATOM   4994 C CG  . ARG C  1 138 ? 26.976 -10.143 79.477  1.00 48.83  ? 153 ARG C CG  1 
ATOM   4995 C CD  . ARG C  1 138 ? 25.717 -9.383  79.102  1.00 50.59  ? 153 ARG C CD  1 
ATOM   4996 N NE  . ARG C  1 138 ? 24.985 -8.953  80.306  0.00 50.00  ? 153 ARG C NE  1 
ATOM   4997 C CZ  . ARG C  1 138 ? 23.926 -8.143  80.322  0.00 50.02  ? 153 ARG C CZ  1 
ATOM   4998 N NH1 . ARG C  1 138 ? 23.444 -7.618  79.207  0.00 50.01  ? 153 ARG C NH1 1 
ATOM   4999 N NH2 . ARG C  1 138 ? 23.345 -7.858  81.474  0.00 50.00  ? 153 ARG C NH2 1 
ATOM   5000 N N   . LEU C  1 139 ? 29.402 -12.797 76.757  1.00 36.44  ? 154 LEU C N   1 
ATOM   5001 C CA  . LEU C  1 139 ? 29.777 -13.259 75.399  1.00 35.92  ? 154 LEU C CA  1 
ATOM   5002 C C   . LEU C  1 139 ? 29.353 -12.174 74.409  1.00 35.93  ? 154 LEU C C   1 
ATOM   5003 O O   . LEU C  1 139 ? 28.170 -11.839 74.347  1.00 35.55  ? 154 LEU C O   1 
ATOM   5004 C CB  . LEU C  1 139 ? 29.073 -14.589 75.110  1.00 34.04  ? 154 LEU C CB  1 
ATOM   5005 C CG  . LEU C  1 139 ? 29.431 -15.273 73.794  1.00 34.68  ? 154 LEU C CG  1 
ATOM   5006 C CD1 . LEU C  1 139 ? 30.878 -15.755 73.787  1.00 35.79  ? 154 LEU C CD1 1 
ATOM   5007 C CD2 . LEU C  1 139 ? 28.490 -16.434 73.532  1.00 33.24  ? 154 LEU C CD2 1 
ATOM   5008 N N   . PRO C  1 140 ? 30.282 -11.574 73.627  1.00 36.37  ? 155 PRO C N   1 
ATOM   5009 C CA  . PRO C  1 140 ? 29.902 -10.575 72.629  1.00 35.91  ? 155 PRO C CA  1 
ATOM   5010 C C   . PRO C  1 140 ? 29.091 -11.148 71.469  1.00 36.51  ? 155 PRO C C   1 
ATOM   5011 O O   . PRO C  1 140 ? 29.234 -12.327 71.133  1.00 34.92  ? 155 PRO C O   1 
ATOM   5012 C CB  . PRO C  1 140 ? 31.233 -10.038 72.073  1.00 36.15  ? 155 PRO C CB  1 
ATOM   5013 C CG  . PRO C  1 140 ? 32.310 -10.568 72.996  1.00 37.87  ? 155 PRO C CG  1 
ATOM   5014 C CD  . PRO C  1 140 ? 31.735 -11.801 73.662  1.00 37.04  ? 155 PRO C CD  1 
ATOM   5015 N N   . PRO C  1 141 ? 28.227 -10.340 70.808  1.00 37.08  ? 156 PRO C N   1 
ATOM   5016 C CA  . PRO C  1 141 ? 27.627 -10.753 69.539  1.00 36.67  ? 156 PRO C CA  1 
ATOM   5017 C C   . PRO C  1 141 ? 28.739 -11.031 68.523  1.00 36.19  ? 156 PRO C C   1 
ATOM   5018 O O   . PRO C  1 141 ? 29.784 -10.390 68.587  1.00 37.91  ? 156 PRO C O   1 
ATOM   5019 C CB  . PRO C  1 141 ? 26.722 -9.590  69.118  1.00 36.85  ? 156 PRO C CB  1 
ATOM   5020 C CG  . PRO C  1 141 ? 27.165 -8.416  69.974  1.00 36.87  ? 156 PRO C CG  1 
ATOM   5021 C CD  . PRO C  1 141 ? 27.790 -8.999  71.224  1.00 37.18  ? 156 PRO C CD  1 
ATOM   5022 N N   . PRO C  1 142 ? 28.581 -11.976 67.567  1.00 36.26  ? 157 PRO C N   1 
ATOM   5023 C CA  . PRO C  1 142 ? 27.327 -12.701 67.331  1.00 35.31  ? 157 PRO C CA  1 
ATOM   5024 C C   . PRO C  1 142 ? 27.108 -13.984 68.158  1.00 34.61  ? 157 PRO C C   1 
ATOM   5025 O O   . PRO C  1 142 ? 26.382 -14.855 67.712  1.00 35.18  ? 157 PRO C O   1 
ATOM   5026 C CB  . PRO C  1 142 ? 27.475 -13.036 65.840  1.00 35.48  ? 157 PRO C CB  1 
ATOM   5027 C CG  . PRO C  1 142 ? 28.947 -13.344 65.686  1.00 36.03  ? 157 PRO C CG  1 
ATOM   5028 C CD  . PRO C  1 142 ? 29.645 -12.398 66.641  1.00 36.96  ? 157 PRO C CD  1 
ATOM   5029 N N   . PHE C  1 143 ? 27.696 -14.072 69.352  1.00 34.53  ? 158 PHE C N   1 
ATOM   5030 C CA  . PHE C  1 143 ? 27.373 -15.088 70.394  1.00 33.88  ? 158 PHE C CA  1 
ATOM   5031 C C   . PHE C  1 143 ? 27.720 -16.488 69.888  1.00 33.16  ? 158 PHE C C   1 
ATOM   5032 O O   . PHE C  1 143 ? 26.845 -17.351 69.781  1.00 30.08  ? 158 PHE C O   1 
ATOM   5033 C CB  . PHE C  1 143 ? 25.894 -15.007 70.791  1.00 33.42  ? 158 PHE C CB  1 
ATOM   5034 C CG  . PHE C  1 143 ? 25.367 -13.620 71.051  1.00 33.95  ? 158 PHE C CG  1 
ATOM   5035 C CD1 . PHE C  1 143 ? 25.751 -12.924 72.186  1.00 34.79  ? 158 PHE C CD1 1 
ATOM   5036 C CD2 . PHE C  1 143 ? 24.480 -13.014 70.167  1.00 35.05  ? 158 PHE C CD2 1 
ATOM   5037 C CE1 . PHE C  1 143 ? 25.265 -11.649 72.435  1.00 34.87  ? 158 PHE C CE1 1 
ATOM   5038 C CE2 . PHE C  1 143 ? 23.988 -11.742 70.420  1.00 34.84  ? 158 PHE C CE2 1 
ATOM   5039 C CZ  . PHE C  1 143 ? 24.377 -11.065 71.556  1.00 35.29  ? 158 PHE C CZ  1 
ATOM   5040 N N   . PRO C  1 144 ? 29.006 -16.762 69.562  1.00 32.83  ? 159 PRO C N   1 
ATOM   5041 C CA  . PRO C  1 144 ? 29.395 -18.082 69.076  1.00 34.06  ? 159 PRO C CA  1 
ATOM   5042 C C   . PRO C  1 144 ? 29.388 -19.100 70.228  1.00 33.97  ? 159 PRO C C   1 
ATOM   5043 O O   . PRO C  1 144 ? 29.746 -18.727 71.346  1.00 34.76  ? 159 PRO C O   1 
ATOM   5044 C CB  . PRO C  1 144 ? 30.817 -17.851 68.543  1.00 34.82  ? 159 PRO C CB  1 
ATOM   5045 C CG  . PRO C  1 144 ? 31.354 -16.733 69.419  1.00 34.41  ? 159 PRO C CG  1 
ATOM   5046 C CD  . PRO C  1 144 ? 30.153 -15.840 69.665  1.00 34.18  ? 159 PRO C CD  1 
ATOM   5047 N N   . LEU C  1 145 ? 28.982 -20.344 69.959  1.00 34.67  ? 160 LEU C N   1 
ATOM   5048 C CA  . LEU C  1 145 ? 29.136 -21.461 70.931  1.00 34.39  ? 160 LEU C CA  1 
ATOM   5049 C C   . LEU C  1 145 ? 30.633 -21.625 71.203  1.00 34.45  ? 160 LEU C C   1 
ATOM   5050 O O   . LEU C  1 145 ? 31.398 -21.761 70.231  1.00 36.83  ? 160 LEU C O   1 
ATOM   5051 C CB  . LEU C  1 145 ? 28.512 -22.755 70.392  1.00 36.10  ? 160 LEU C CB  1 
ATOM   5052 C CG  . LEU C  1 145 ? 28.704 -23.997 71.272  1.00 36.65  ? 160 LEU C CG  1 
ATOM   5053 C CD1 . LEU C  1 145 ? 28.037 -23.815 72.625  1.00 37.17  ? 160 LEU C CD1 1 
ATOM   5054 C CD2 . LEU C  1 145 ? 28.175 -25.249 70.587  1.00 36.12  ? 160 LEU C CD2 1 
ATOM   5055 N N   . LYS C  1 146 ? 31.033 -21.571 72.473  1.00 35.54  ? 161 LYS C N   1 
ATOM   5056 C CA  . LYS C  1 146 ? 32.457 -21.695 72.880  1.00 34.24  ? 161 LYS C CA  1 
ATOM   5057 C C   . LYS C  1 146 ? 32.670 -23.053 73.549  1.00 34.94  ? 161 LYS C C   1 
ATOM   5058 O O   . LYS C  1 146 ? 31.695 -23.653 74.037  1.00 34.80  ? 161 LYS C O   1 
ATOM   5059 C CB  . LYS C  1 146 ? 32.900 -20.522 73.754  1.00 34.80  ? 161 LYS C CB  1 
ATOM   5060 C CG  . LYS C  1 146 ? 32.775 -19.151 73.099  1.00 37.68  ? 161 LYS C CG  1 
ATOM   5061 C CD  . LYS C  1 146 ? 33.661 -18.099 73.695  1.00 40.42  ? 161 LYS C CD  1 
ATOM   5062 C CE  . LYS C  1 146 ? 35.065 -18.136 73.140  1.00 43.87  ? 161 LYS C CE  1 
ATOM   5063 N NZ  . LYS C  1 146 ? 35.719 -16.808 73.252  1.00 47.02  ? 161 LYS C NZ  1 
ATOM   5064 N N   . GLN C  1 147 ? 33.915 -23.519 73.508  1.00 34.91  ? 162 GLN C N   1 
ATOM   5065 C CA  . GLN C  1 147 ? 34.390 -24.810 74.053  1.00 34.39  ? 162 GLN C CA  1 
ATOM   5066 C C   . GLN C  1 147 ? 35.678 -24.519 74.820  1.00 35.84  ? 162 GLN C C   1 
ATOM   5067 O O   . GLN C  1 147 ? 36.398 -23.572 74.432  1.00 35.25  ? 162 GLN C O   1 
ATOM   5068 C CB  . GLN C  1 147 ? 34.625 -25.804 72.912  1.00 35.83  ? 162 GLN C CB  1 
ATOM   5069 C CG  . GLN C  1 147 ? 35.652 -25.337 71.879  1.00 35.88  ? 162 GLN C CG  1 
ATOM   5070 C CD  . GLN C  1 147 ? 36.019 -26.380 70.851  1.00 35.97  ? 162 GLN C CD  1 
ATOM   5071 O OE1 . GLN C  1 147 ? 35.175 -27.106 70.347  1.00 34.04  ? 162 GLN C OE1 1 
ATOM   5072 N NE2 . GLN C  1 147 ? 37.293 -26.446 70.501  1.00 37.37  ? 162 GLN C NE2 1 
ATOM   5073 N N   . VAL C  1 148 ? 35.961 -25.296 75.861  1.00 35.48  ? 163 VAL C N   1 
ATOM   5074 C CA  . VAL C  1 148 ? 37.281 -25.255 76.545  1.00 35.91  ? 163 VAL C CA  1 
ATOM   5075 C C   . VAL C  1 148 ? 37.578 -26.647 77.111  1.00 36.04  ? 163 VAL C C   1 
ATOM   5076 O O   . VAL C  1 148 ? 36.656 -27.307 77.619  1.00 37.32  ? 163 VAL C O   1 
ATOM   5077 C CB  . VAL C  1 148 ? 37.340 -24.128 77.596  1.00 35.95  ? 163 VAL C CB  1 
ATOM   5078 C CG1 . VAL C  1 148 ? 36.400 -24.354 78.765  1.00 36.90  ? 163 VAL C CG1 1 
ATOM   5079 C CG2 . VAL C  1 148 ? 38.758 -23.885 78.081  1.00 36.01  ? 163 VAL C CG2 1 
ATOM   5080 N N   . LYS C  1 149 ? 38.819 -27.087 76.938  1.00 37.02  ? 164 LYS C N   1 
ATOM   5081 C CA  . LYS C  1 149 ? 39.365 -28.333 77.524  1.00 38.08  ? 164 LYS C CA  1 
ATOM   5082 C C   . LYS C  1 149 ? 39.698 -28.039 78.987  1.00 36.89  ? 164 LYS C C   1 
ATOM   5083 O O   . LYS C  1 149 ? 40.445 -27.084 79.230  1.00 36.16  ? 164 LYS C O   1 
ATOM   5084 C CB  . LYS C  1 149 ? 40.582 -28.766 76.703  1.00 39.98  ? 164 LYS C CB  1 
ATOM   5085 C CG  . LYS C  1 149 ? 41.247 -30.081 77.077  1.00 41.97  ? 164 LYS C CG  1 
ATOM   5086 C CD  . LYS C  1 149 ? 42.509 -30.283 76.253  1.00 44.50  ? 164 LYS C CD  1 
ATOM   5087 C CE  . LYS C  1 149 ? 43.222 -31.587 76.521  1.00 48.59  ? 164 LYS C CE  1 
ATOM   5088 N NZ  . LYS C  1 149 ? 44.501 -31.687 75.808  0.00 47.00  ? 164 LYS C NZ  1 
ATOM   5089 N N   . VAL C  1 150 ? 39.144 -28.811 79.926  1.00 36.50  ? 165 VAL C N   1 
ATOM   5090 C CA  . VAL C  1 150 ? 39.355 -28.636 81.395  1.00 37.66  ? 165 VAL C CA  1 
ATOM   5091 C C   . VAL C  1 150 ? 39.739 -29.991 81.985  1.00 38.88  ? 165 VAL C C   1 
ATOM   5092 O O   . VAL C  1 150 ? 39.094 -31.001 81.702  1.00 41.16  ? 165 VAL C O   1 
ATOM   5093 C CB  . VAL C  1 150 ? 38.126 -28.018 82.094  1.00 37.32  ? 165 VAL C CB  1 
ATOM   5094 C CG1 . VAL C  1 150 ? 37.966 -26.543 81.750  1.00 38.03  ? 165 VAL C CG1 1 
ATOM   5095 C CG2 . VAL C  1 150 ? 36.828 -28.751 81.802  1.00 38.19  ? 165 VAL C CG2 1 
ATOM   5096 N N   . PRO C  1 151 ? 40.809 -30.069 82.806  1.00 42.53  ? 166 PRO C N   1 
ATOM   5097 C CA  . PRO C  1 151 ? 41.178 -31.326 83.458  1.00 44.81  ? 166 PRO C CA  1 
ATOM   5098 C C   . PRO C  1 151 ? 40.223 -31.614 84.624  1.00 43.16  ? 166 PRO C C   1 
ATOM   5099 O O   . PRO C  1 151 ? 40.018 -30.729 85.443  1.00 43.39  ? 166 PRO C O   1 
ATOM   5100 C CB  . PRO C  1 151 ? 42.605 -31.072 83.958  1.00 46.19  ? 166 PRO C CB  1 
ATOM   5101 C CG  . PRO C  1 151 ? 42.643 -29.571 84.204  1.00 47.86  ? 166 PRO C CG  1 
ATOM   5102 C CD  . PRO C  1 151 ? 41.716 -28.966 83.168  1.00 45.74  ? 166 PRO C CD  1 
ATOM   5103 N N   . ILE C  1 152 ? 39.670 -32.829 84.680  1.00 44.70  ? 167 ILE C N   1 
ATOM   5104 C CA  . ILE C  1 152 ? 38.953 -33.342 85.887  1.00 44.67  ? 167 ILE C CA  1 
ATOM   5105 C C   . ILE C  1 152 ? 39.959 -33.415 87.041  1.00 44.21  ? 167 ILE C C   1 
ATOM   5106 O O   . ILE C  1 152 ? 41.127 -33.780 86.814  1.00 42.96  ? 167 ILE C O   1 
ATOM   5107 C CB  . ILE C  1 152 ? 38.238 -34.686 85.627  1.00 46.61  ? 167 ILE C CB  1 
ATOM   5108 C CG1 . ILE C  1 152 ? 36.897 -34.438 84.934  1.00 47.83  ? 167 ILE C CG1 1 
ATOM   5109 C CG2 . ILE C  1 152 ? 38.062 -35.492 86.913  1.00 48.53  ? 167 ILE C CG2 1 
ATOM   5110 C CD1 . ILE C  1 152 ? 36.096 -35.689 84.638  1.00 50.08  ? 167 ILE C CD1 1 
ATOM   5111 N N   . MET C  1 153 ? 39.516 -33.005 88.222  1.00 44.61  ? 168 MET C N   1 
ATOM   5112 C CA  . MET C  1 153 ? 40.314 -33.031 89.468  1.00 47.72  ? 168 MET C CA  1 
ATOM   5113 C C   . MET C  1 153 ? 39.528 -33.817 90.518  1.00 43.97  ? 168 MET C C   1 
ATOM   5114 O O   . MET C  1 153 ? 38.278 -33.768 90.479  1.00 44.03  ? 168 MET C O   1 
ATOM   5115 C CB  . MET C  1 153 ? 40.600 -31.603 89.935  1.00 50.94  ? 168 MET C CB  1 
ATOM   5116 C CG  . MET C  1 153 ? 41.542 -30.848 89.009  1.00 55.63  ? 168 MET C CG  1 
ATOM   5117 S SD  . MET C  1 153 ? 42.458 -29.521 89.837  1.00 66.61  ? 168 MET C SD  1 
ATOM   5118 C CE  . MET C  1 153 ? 41.114 -28.609 90.593  1.00 64.71  ? 168 MET C CE  1 
ATOM   5119 N N   . GLU C  1 154 ? 40.237 -34.542 91.388  1.00 42.70  ? 169 GLU C N   1 
ATOM   5120 C CA  . GLU C  1 154 ? 39.655 -35.358 92.486  1.00 45.11  ? 169 GLU C CA  1 
ATOM   5121 C C   . GLU C  1 154 ? 38.817 -34.450 93.394  1.00 41.82  ? 169 GLU C C   1 
ATOM   5122 O O   . GLU C  1 154 ? 39.237 -33.309 93.647  1.00 41.18  ? 169 GLU C O   1 
ATOM   5123 C CB  . GLU C  1 154 ? 40.765 -36.062 93.269  1.00 48.18  ? 169 GLU C CB  1 
ATOM   5124 C CG  . GLU C  1 154 ? 40.288 -37.210 94.137  1.00 52.47  ? 169 GLU C CG  1 
ATOM   5125 C CD  . GLU C  1 154 ? 41.402 -37.791 94.989  1.00 57.07  ? 169 GLU C CD  1 
ATOM   5126 O OE1 . GLU C  1 154 ? 41.884 -38.889 94.660  1.00 59.96  ? 169 GLU C OE1 1 
ATOM   5127 O OE2 . GLU C  1 154 ? 41.802 -37.128 95.962  1.00 61.67  ? 169 GLU C OE2 1 
ATOM   5128 N N   . ASN C  1 155 ? 37.667 -34.943 93.850  1.00 41.31  ? 170 ASN C N   1 
ATOM   5129 C CA  . ASN C  1 155 ? 36.746 -34.210 94.761  1.00 42.53  ? 170 ASN C CA  1 
ATOM   5130 C C   . ASN C  1 155 ? 37.485 -33.754 96.016  1.00 42.35  ? 170 ASN C C   1 
ATOM   5131 O O   . ASN C  1 155 ? 37.264 -32.614 96.421  1.00 42.05  ? 170 ASN C O   1 
ATOM   5132 C CB  . ASN C  1 155 ? 35.516 -35.036 95.140  1.00 43.36  ? 170 ASN C CB  1 
ATOM   5133 C CG  . ASN C  1 155 ? 34.353 -34.768 94.218  1.00 45.17  ? 170 ASN C CG  1 
ATOM   5134 O OD1 . ASN C  1 155 ? 34.543 -34.377 93.065  1.00 51.58  ? 170 ASN C OD1 1 
ATOM   5135 N ND2 . ASN C  1 155 ? 33.147 -34.989 94.707  1.00 41.30  ? 170 ASN C ND2 1 
ATOM   5136 N N   . HIS C  1 156 ? 38.336 -34.605 96.591  1.00 44.42  ? 171 HIS C N   1 
ATOM   5137 C CA  . HIS C  1 156 ? 39.079 -34.307 97.840  1.00 44.72  ? 171 HIS C CA  1 
ATOM   5138 C C   . HIS C  1 156 ? 40.036 -33.126 97.605  1.00 42.51  ? 171 HIS C C   1 
ATOM   5139 O O   . HIS C  1 156 ? 40.076 -32.250 98.477  1.00 40.52  ? 171 HIS C O   1 
ATOM   5140 C CB  . HIS C  1 156 ? 39.768 -35.572 98.379  1.00 48.70  ? 171 HIS C CB  1 
ATOM   5141 C CG  . HIS C  1 156 ? 40.554 -35.343 99.626  1.00 51.78  ? 171 HIS C CG  1 
ATOM   5142 N ND1 . HIS C  1 156 ? 40.033 -35.578 100.883 1.00 55.96  ? 171 HIS C ND1 1 
ATOM   5143 C CD2 . HIS C  1 156 ? 41.818 -34.910 99.817  1.00 54.82  ? 171 HIS C CD2 1 
ATOM   5144 C CE1 . HIS C  1 156 ? 40.938 -35.286 101.793 1.00 55.52  ? 171 HIS C CE1 1 
ATOM   5145 N NE2 . HIS C  1 156 ? 42.043 -34.874 101.165 1.00 54.73  ? 171 HIS C NE2 1 
ATOM   5146 N N   . ILE C  1 157 ? 40.712 -33.067 96.450  1.00 39.46  ? 172 ILE C N   1 
ATOM   5147 C CA  . ILE C  1 157 ? 41.654 -31.968 96.079  1.00 40.16  ? 172 ILE C CA  1 
ATOM   5148 C C   . ILE C  1 157 ? 40.874 -30.662 95.895  1.00 39.64  ? 172 ILE C C   1 
ATOM   5149 O O   . ILE C  1 157 ? 41.361 -29.610 96.335  1.00 39.68  ? 172 ILE C O   1 
ATOM   5150 C CB  . ILE C  1 157 ? 42.448 -32.339 94.809  1.00 42.51  ? 172 ILE C CB  1 
ATOM   5151 C CG1 . ILE C  1 157 ? 43.366 -33.544 95.045  1.00 43.05  ? 172 ILE C CG1 1 
ATOM   5152 C CG2 . ILE C  1 157 ? 43.222 -31.145 94.257  1.00 42.93  ? 172 ILE C CG2 1 
ATOM   5153 C CD1 . ILE C  1 157 ? 44.384 -33.368 96.157  1.00 44.52  ? 172 ILE C CD1 1 
ATOM   5154 N N   . CYS C  1 158 ? 39.728 -30.735 95.234  1.00 39.33  ? 173 CYS C N   1 
ATOM   5155 C CA  A CYS C  1 158 ? 38.853 -29.572 94.930  0.50 40.92  ? 173 CYS C CA  1 
ATOM   5156 C CA  B CYS C  1 158 ? 38.867 -29.562 94.938  0.50 41.55  ? 173 CYS C CA  1 
ATOM   5157 C C   . CYS C  1 158 ? 38.239 -29.030 96.230  1.00 39.53  ? 173 CYS C C   1 
ATOM   5158 O O   . CYS C  1 158 ? 38.202 -27.794 96.383  1.00 36.09  ? 173 CYS C O   1 
ATOM   5159 C CB  A CYS C  1 158 ? 37.793 -29.979 93.914  0.50 42.27  ? 173 CYS C CB  1 
ATOM   5160 C CB  B CYS C  1 158 ? 37.817 -29.917 93.899  0.50 43.57  ? 173 CYS C CB  1 
ATOM   5161 S SG  A CYS C  1 158 ? 36.601 -28.685 93.492  0.50 44.91  ? 173 CYS C SG  1 
ATOM   5162 S SG  B CYS C  1 158 ? 38.568 -30.204 92.279  0.50 48.05  ? 173 CYS C SG  1 
ATOM   5163 N N   . ASP C  1 159 ? 37.798 -29.929 97.118  1.00 37.77  ? 174 ASP C N   1 
ATOM   5164 C CA  . ASP C  1 159 ? 37.287 -29.573 98.469  1.00 38.34  ? 174 ASP C CA  1 
ATOM   5165 C C   . ASP C  1 159 ? 38.381 -28.806 99.227  1.00 37.30  ? 174 ASP C C   1 
ATOM   5166 O O   . ASP C  1 159 ? 38.076 -27.742 99.761  1.00 37.84  ? 174 ASP C O   1 
ATOM   5167 C CB  . ASP C  1 159 ? 36.846 -30.809 99.252  1.00 39.73  ? 174 ASP C CB  1 
ATOM   5168 C CG  . ASP C  1 159 ? 36.099 -30.469 100.528 1.00 40.51  ? 174 ASP C CG  1 
ATOM   5169 O OD1 . ASP C  1 159 ? 35.111 -29.707 100.446 1.00 40.84  ? 174 ASP C OD1 1 
ATOM   5170 O OD2 . ASP C  1 159 ? 36.532 -30.930 101.594 1.00 43.71  ? 174 ASP C OD2 1 
ATOM   5171 N N   . ALA C  1 160 ? 39.617 -29.316 99.219  1.00 35.90  ? 175 ALA C N   1 
ATOM   5172 C CA  . ALA C  1 160 ? 40.795 -28.708 99.877  1.00 36.43  ? 175 ALA C CA  1 
ATOM   5173 C C   . ALA C  1 160 ? 41.058 -27.308 99.307  1.00 37.83  ? 175 ALA C C   1 
ATOM   5174 O O   . ALA C  1 160 ? 41.327 -26.400 100.103 1.00 42.15  ? 175 ALA C O   1 
ATOM   5175 C CB  . ALA C  1 160 ? 41.994 -29.615 99.733  1.00 36.10  ? 175 ALA C CB  1 
ATOM   5176 N N   . LYS C  1 161 ? 40.968 -27.123 97.984  1.00 39.33  ? 176 LYS C N   1 
ATOM   5177 C CA  . LYS C  1 161 ? 41.192 -25.805 97.324  1.00 38.28  ? 176 LYS C CA  1 
ATOM   5178 C C   . LYS C  1 161 ? 40.155 -24.785 97.813  1.00 36.72  ? 176 LYS C C   1 
ATOM   5179 O O   . LYS C  1 161 ? 40.554 -23.649 98.122  1.00 35.73  ? 176 LYS C O   1 
ATOM   5180 C CB  . LYS C  1 161 ? 41.199 -25.937 95.798  1.00 40.79  ? 176 LYS C CB  1 
ATOM   5181 C CG  . LYS C  1 161 ? 42.487 -26.529 95.246  1.00 42.74  ? 176 LYS C CG  1 
ATOM   5182 C CD  . LYS C  1 161 ? 42.517 -26.708 93.748  1.00 45.95  ? 176 LYS C CD  1 
ATOM   5183 C CE  . LYS C  1 161 ? 43.931 -26.944 93.260  1.00 47.76  ? 176 LYS C CE  1 
ATOM   5184 N NZ  . LYS C  1 161 ? 43.965 -27.417 91.860  1.00 53.13  ? 176 LYS C NZ  1 
ATOM   5185 N N   . TYR C  1 162 ? 38.884 -25.176 97.926  1.00 33.82  ? 177 TYR C N   1 
ATOM   5186 C CA  . TYR C  1 162 ? 37.782 -24.276 98.363  1.00 33.74  ? 177 TYR C CA  1 
ATOM   5187 C C   . TYR C  1 162 ? 37.969 -23.838 99.823  1.00 33.48  ? 177 TYR C C   1 
ATOM   5188 O O   . TYR C  1 162 ? 37.397 -22.795 100.190 1.00 33.64  ? 177 TYR C O   1 
ATOM   5189 C CB  . TYR C  1 162 ? 36.410 -24.911 98.104  1.00 32.40  ? 177 TYR C CB  1 
ATOM   5190 C CG  . TYR C  1 162 ? 35.822 -24.450 96.801  1.00 32.39  ? 177 TYR C CG  1 
ATOM   5191 C CD1 . TYR C  1 162 ? 36.226 -25.025 95.605  1.00 31.61  ? 177 TYR C CD1 1 
ATOM   5192 C CD2 . TYR C  1 162 ? 34.941 -23.381 96.746  1.00 31.60  ? 177 TYR C CD2 1 
ATOM   5193 C CE1 . TYR C  1 162 ? 35.727 -24.586 94.391  1.00 32.02  ? 177 TYR C CE1 1 
ATOM   5194 C CE2 . TYR C  1 162 ? 34.430 -22.931 95.538  1.00 33.17  ? 177 TYR C CE2 1 
ATOM   5195 C CZ  . TYR C  1 162 ? 34.827 -23.533 94.356  1.00 33.73  ? 177 TYR C CZ  1 
ATOM   5196 O OH  . TYR C  1 162 ? 34.343 -23.100 93.157  1.00 33.72  ? 177 TYR C OH  1 
ATOM   5197 N N   . HIS C  1 163 ? 38.744 -24.586 100.615 1.00 34.48  ? 178 HIS C N   1 
ATOM   5198 C CA  . HIS C  1 163 ? 39.087 -24.272 102.027 1.00 33.84  ? 178 HIS C CA  1 
ATOM   5199 C C   . HIS C  1 163 ? 40.267 -23.295 102.125 1.00 36.27  ? 178 HIS C C   1 
ATOM   5200 O O   . HIS C  1 163 ? 40.354 -22.620 103.162 1.00 36.84  ? 178 HIS C O   1 
ATOM   5201 C CB  . HIS C  1 163 ? 39.340 -25.562 102.815 1.00 34.38  ? 178 HIS C CB  1 
ATOM   5202 C CG  . HIS C  1 163 ? 38.087 -26.295 103.154 1.00 32.81  ? 178 HIS C CG  1 
ATOM   5203 N ND1 . HIS C  1 163 ? 37.503 -27.204 102.299 1.00 34.04  ? 178 HIS C ND1 1 
ATOM   5204 C CD2 . HIS C  1 163 ? 37.293 -26.242 104.236 1.00 33.53  ? 178 HIS C CD2 1 
ATOM   5205 C CE1 . HIS C  1 163 ? 36.420 -27.695 102.852 1.00 33.28  ? 178 HIS C CE1 1 
ATOM   5206 N NE2 . HIS C  1 163 ? 36.272 -27.123 104.042 1.00 34.34  ? 178 HIS C NE2 1 
ATOM   5207 N N   . LEU C  1 164 ? 41.135 -23.211 101.111 1.00 36.72  ? 179 LEU C N   1 
ATOM   5208 C CA  . LEU C  1 164 ? 42.269 -22.244 101.088 1.00 38.07  ? 179 LEU C CA  1 
ATOM   5209 C C   . LEU C  1 164 ? 41.705 -20.822 100.972 1.00 36.12  ? 179 LEU C C   1 
ATOM   5210 O O   . LEU C  1 164 ? 40.912 -20.580 100.060 1.00 35.92  ? 179 LEU C O   1 
ATOM   5211 C CB  . LEU C  1 164 ? 43.219 -22.559 99.926  1.00 40.42  ? 179 LEU C CB  1 
ATOM   5212 C CG  . LEU C  1 164 ? 43.969 -23.890 100.015 1.00 43.89  ? 179 LEU C CG  1 
ATOM   5213 C CD1 . LEU C  1 164 ? 44.667 -24.199 98.703  1.00 45.96  ? 179 LEU C CD1 1 
ATOM   5214 C CD2 . LEU C  1 164 ? 44.976 -23.884 101.158 1.00 43.77  ? 179 LEU C CD2 1 
ATOM   5215 N N   . GLY C  1 165 ? 42.100 -19.926 101.880 1.00 36.10  ? 180 GLY C N   1 
ATOM   5216 C CA  . GLY C  1 165 ? 41.622 -18.532 101.939 1.00 35.25  ? 180 GLY C CA  1 
ATOM   5217 C C   . GLY C  1 165 ? 40.179 -18.446 102.416 1.00 35.22  ? 180 GLY C C   1 
ATOM   5218 O O   . GLY C  1 165 ? 39.533 -17.427 102.117 1.00 35.97  ? 180 GLY C O   1 
ATOM   5219 N N   . ALA C  1 166 ? 39.701 -19.453 103.157 1.00 34.11  ? 181 ALA C N   1 
ATOM   5220 C CA  . ALA C  1 166 ? 38.319 -19.542 103.683 1.00 34.82  ? 181 ALA C CA  1 
ATOM   5221 C C   . ALA C  1 166 ? 38.345 -19.830 105.187 1.00 34.11  ? 181 ALA C C   1 
ATOM   5222 O O   . ALA C  1 166 ? 39.300 -20.457 105.667 1.00 34.79  ? 181 ALA C O   1 
ATOM   5223 C CB  . ALA C  1 166 ? 37.536 -20.600 102.941 1.00 33.57  ? 181 ALA C CB  1 
ATOM   5224 N N   . TYR C  1 167 ? 37.309 -19.389 105.895 1.00 35.82  ? 182 TYR C N   1 
ATOM   5225 C CA  . TYR C  1 167 ? 37.122 -19.612 107.354 1.00 35.29  ? 182 TYR C CA  1 
ATOM   5226 C C   . TYR C  1 167 ? 36.561 -21.017 107.609 1.00 35.51  ? 182 TYR C C   1 
ATOM   5227 O O   . TYR C  1 167 ? 36.697 -21.494 108.748 1.00 37.41  ? 182 TYR C O   1 
ATOM   5228 C CB  . TYR C  1 167 ? 36.192 -18.552 107.945 1.00 34.71  ? 182 TYR C CB  1 
ATOM   5229 C CG  . TYR C  1 167 ? 36.744 -17.150 107.905 1.00 35.52  ? 182 TYR C CG  1 
ATOM   5230 C CD1 . TYR C  1 167 ? 37.756 -16.757 108.770 1.00 37.39  ? 182 TYR C CD1 1 
ATOM   5231 C CD2 . TYR C  1 167 ? 36.248 -16.208 107.017 1.00 35.06  ? 182 TYR C CD2 1 
ATOM   5232 C CE1 . TYR C  1 167 ? 38.254 -15.462 108.761 1.00 37.10  ? 182 TYR C CE1 1 
ATOM   5233 C CE2 . TYR C  1 167 ? 36.742 -14.913 106.989 1.00 35.77  ? 182 TYR C CE2 1 
ATOM   5234 C CZ  . TYR C  1 167 ? 37.746 -14.536 107.863 1.00 37.31  ? 182 TYR C CZ  1 
ATOM   5235 O OH  . TYR C  1 167 ? 38.239 -13.263 107.813 1.00 39.85  ? 182 TYR C OH  1 
ATOM   5236 N N   . THR C  1 168 ? 35.915 -21.639 106.612 1.00 36.33  ? 183 THR C N   1 
ATOM   5237 C CA  . THR C  1 168 ? 35.248 -22.964 106.735 1.00 33.58  ? 183 THR C CA  1 
ATOM   5238 C C   . THR C  1 168 ? 36.269 -23.981 107.253 1.00 35.24  ? 183 THR C C   1 
ATOM   5239 O O   . THR C  1 168 ? 37.391 -24.017 106.703 1.00 34.19  ? 183 THR C O   1 
ATOM   5240 C CB  . THR C  1 168 ? 34.623 -23.425 105.409 1.00 32.19  ? 183 THR C CB  1 
ATOM   5241 O OG1 . THR C  1 168 ? 33.927 -22.339 104.792 1.00 31.85  ? 183 THR C OG1 1 
ATOM   5242 C CG2 . THR C  1 168 ? 33.670 -24.586 105.596 1.00 30.33  ? 183 THR C CG2 1 
ATOM   5243 N N   . GLY C  1 169 ? 35.900 -24.745 108.285 1.00 37.80  ? 184 GLY C N   1 
ATOM   5244 C CA  . GLY C  1 169 ? 36.736 -25.804 108.876 1.00 38.01  ? 184 GLY C CA  1 
ATOM   5245 C C   . GLY C  1 169 ? 37.091 -26.846 107.835 1.00 39.17  ? 184 GLY C C   1 
ATOM   5246 O O   . GLY C  1 169 ? 36.202 -27.198 107.040 1.00 41.35  ? 184 GLY C O   1 
ATOM   5247 N N   . ASP C  1 170 ? 38.340 -27.320 107.835 1.00 40.50  ? 185 ASP C N   1 
ATOM   5248 C CA  . ASP C  1 170 ? 38.887 -28.271 106.826 1.00 45.24  ? 185 ASP C CA  1 
ATOM   5249 C C   . ASP C  1 170 ? 38.073 -29.574 106.783 1.00 44.29  ? 185 ASP C C   1 
ATOM   5250 O O   . ASP C  1 170 ? 38.002 -30.168 105.694 1.00 48.35  ? 185 ASP C O   1 
ATOM   5251 C CB  . ASP C  1 170 ? 40.371 -28.549 107.080 1.00 47.46  ? 185 ASP C CB  1 
ATOM   5252 C CG  . ASP C  1 170 ? 41.290 -27.394 106.712 1.00 48.92  ? 185 ASP C CG  1 
ATOM   5253 O OD1 . ASP C  1 170 ? 40.869 -26.519 105.925 1.00 50.73  ? 185 ASP C OD1 1 
ATOM   5254 O OD2 . ASP C  1 170 ? 42.427 -27.378 107.213 1.00 54.59  ? 185 ASP C OD2 1 
ATOM   5255 N N   . ASP C  1 171 ? 37.470 -29.987 107.903 1.00 44.69  ? 186 ASP C N   1 
ATOM   5256 C CA  . ASP C  1 171 ? 36.649 -31.226 108.046 1.00 46.18  ? 186 ASP C CA  1 
ATOM   5257 C C   . ASP C  1 171 ? 35.187 -30.997 107.629 1.00 43.63  ? 186 ASP C C   1 
ATOM   5258 O O   . ASP C  1 171 ? 34.414 -31.967 107.667 1.00 41.88  ? 186 ASP C O   1 
ATOM   5259 C CB  . ASP C  1 171 ? 36.691 -31.760 109.481 1.00 52.49  ? 186 ASP C CB  1 
ATOM   5260 C CG  . ASP C  1 171 ? 36.052 -30.831 110.504 1.00 57.10  ? 186 ASP C CG  1 
ATOM   5261 O OD1 . ASP C  1 171 ? 36.247 -29.600 110.388 1.00 57.01  ? 186 ASP C OD1 1 
ATOM   5262 O OD2 . ASP C  1 171 ? 35.349 -31.342 111.399 1.00 65.82  ? 186 ASP C OD2 1 
ATOM   5263 N N   . VAL C  1 172 ? 34.805 -29.771 107.267 1.00 41.95  ? 187 VAL C N   1 
ATOM   5264 C CA  . VAL C  1 172 ? 33.422 -29.420 106.824 1.00 40.94  ? 187 VAL C CA  1 
ATOM   5265 C C   . VAL C  1 172 ? 33.429 -29.431 105.296 1.00 39.55  ? 187 VAL C C   1 
ATOM   5266 O O   . VAL C  1 172 ? 34.086 -28.563 104.710 1.00 39.00  ? 187 VAL C O   1 
ATOM   5267 C CB  . VAL C  1 172 ? 32.975 -28.065 107.406 1.00 40.53  ? 187 VAL C CB  1 
ATOM   5268 C CG1 . VAL C  1 172 ? 31.574 -27.671 106.960 1.00 41.81  ? 187 VAL C CG1 1 
ATOM   5269 C CG2 . VAL C  1 172 ? 33.078 -28.062 108.921 1.00 41.35  ? 187 VAL C CG2 1 
ATOM   5270 N N   . ARG C  1 173 ? 32.718 -30.379 104.679 1.00 39.73  ? 188 ARG C N   1 
ATOM   5271 C CA  . ARG C  1 173 ? 32.680 -30.585 103.206 1.00 40.75  ? 188 ARG C CA  1 
ATOM   5272 C C   . ARG C  1 173 ? 32.048 -29.357 102.534 1.00 38.73  ? 188 ARG C C   1 
ATOM   5273 O O   . ARG C  1 173 ? 30.979 -28.901 102.995 1.00 36.47  ? 188 ARG C O   1 
ATOM   5274 C CB  . ARG C  1 173 ? 31.892 -31.851 102.828 1.00 44.15  ? 188 ARG C CB  1 
ATOM   5275 C CG  . ARG C  1 173 ? 32.513 -33.164 103.288 1.00 48.88  ? 188 ARG C CG  1 
ATOM   5276 C CD  . ARG C  1 173 ? 33.806 -33.535 102.582 1.00 50.64  ? 188 ARG C CD  1 
ATOM   5277 N NE  . ARG C  1 173 ? 33.643 -33.768 101.156 1.00 54.21  ? 188 ARG C NE  1 
ATOM   5278 C CZ  . ARG C  1 173 ? 33.146 -34.843 100.551 0.00 52.83  ? 188 ARG C CZ  1 
ATOM   5279 N NH1 . ARG C  1 173 ? 32.690 -35.861 101.265 0.00 52.85  ? 188 ARG C NH1 1 
ATOM   5280 N NH2 . ARG C  1 173 ? 33.079 -34.907 99.232  0.00 52.90  ? 188 ARG C NH2 1 
ATOM   5281 N N   . ILE C  1 174 ? 32.721 -28.816 101.517 1.00 38.43  ? 189 ILE C N   1 
ATOM   5282 C CA  . ILE C  1 174 ? 32.170 -27.788 100.586 1.00 37.91  ? 189 ILE C CA  1 
ATOM   5283 C C   . ILE C  1 174 ? 31.760 -28.509 99.294  1.00 36.73  ? 189 ILE C C   1 
ATOM   5284 O O   . ILE C  1 174 ? 30.593 -28.393 98.892  1.00 37.71  ? 189 ILE C O   1 
ATOM   5285 C CB  . ILE C  1 174 ? 33.191 -26.655 100.361 1.00 35.50  ? 189 ILE C CB  1 
ATOM   5286 C CG1 . ILE C  1 174 ? 33.433 -25.869 101.653 1.00 36.01  ? 189 ILE C CG1 1 
ATOM   5287 C CG2 . ILE C  1 174 ? 32.743 -25.746 99.223  1.00 37.48  ? 189 ILE C CG2 1 
ATOM   5288 C CD1 . ILE C  1 174 ? 34.650 -24.963 101.638 1.00 36.92  ? 189 ILE C CD1 1 
ATOM   5289 N N   . VAL C  1 175 ? 32.698 -29.229 98.677  1.00 36.44  ? 190 VAL C N   1 
ATOM   5290 C CA  . VAL C  1 175 ? 32.470 -30.061 97.461  1.00 35.85  ? 190 VAL C CA  1 
ATOM   5291 C C   . VAL C  1 175 ? 32.007 -31.441 97.927  1.00 37.16  ? 190 VAL C C   1 
ATOM   5292 O O   . VAL C  1 175 ? 32.815 -32.154 98.559  1.00 37.61  ? 190 VAL C O   1 
ATOM   5293 C CB  . VAL C  1 175 ? 33.721 -30.164 96.570  1.00 36.00  ? 190 VAL C CB  1 
ATOM   5294 C CG1 . VAL C  1 175 ? 33.393 -30.880 95.271  1.00 35.38  ? 190 VAL C CG1 1 
ATOM   5295 C CG2 . VAL C  1 175 ? 34.342 -28.805 96.283  1.00 36.32  ? 190 VAL C CG2 1 
ATOM   5296 N N   . ARG C  1 176 ? 30.766 -31.803 97.615  1.00 36.37  ? 191 ARG C N   1 
ATOM   5297 C CA  . ARG C  1 176 ? 30.100 -33.024 98.145  1.00 38.99  ? 191 ARG C CA  1 
ATOM   5298 C C   . ARG C  1 176 ? 30.242 -34.168 97.129  1.00 38.96  ? 191 ARG C C   1 
ATOM   5299 O O   . ARG C  1 176 ? 30.752 -33.914 96.025  1.00 36.87  ? 191 ARG C O   1 
ATOM   5300 C CB  . ARG C  1 176 ? 28.652 -32.677 98.506  1.00 40.61  ? 191 ARG C CB  1 
ATOM   5301 C CG  . ARG C  1 176 ? 28.540 -31.496 99.458  1.00 44.56  ? 191 ARG C CG  1 
ATOM   5302 C CD  . ARG C  1 176 ? 27.184 -31.337 100.112 1.00 50.69  ? 191 ARG C CD  1 
ATOM   5303 N NE  . ARG C  1 176 ? 27.186 -30.201 101.033 1.00 55.58  ? 191 ARG C NE  1 
ATOM   5304 C CZ  . ARG C  1 176 ? 26.197 -29.873 101.867 1.00 61.45  ? 191 ARG C CZ  1 
ATOM   5305 N NH1 . ARG C  1 176 ? 25.077 -30.581 101.917 1.00 63.51  ? 191 ARG C NH1 1 
ATOM   5306 N NH2 . ARG C  1 176 ? 26.336 -28.821 102.657 1.00 67.38  ? 191 ARG C NH2 1 
ATOM   5307 N N   . ASP C  1 177 ? 29.827 -35.383 97.507  1.00 38.53  ? 192 ASP C N   1 
ATOM   5308 C CA  . ASP C  1 177 ? 30.070 -36.639 96.745  1.00 40.16  ? 192 ASP C CA  1 
ATOM   5309 C C   . ASP C  1 177 ? 29.225 -36.679 95.461  1.00 37.39  ? 192 ASP C C   1 
ATOM   5310 O O   . ASP C  1 177 ? 29.635 -37.373 94.526  1.00 39.12  ? 192 ASP C O   1 
ATOM   5311 C CB  . ASP C  1 177 ? 29.822 -37.859 97.640  1.00 41.58  ? 192 ASP C CB  1 
ATOM   5312 C CG  . ASP C  1 177 ? 30.781 -37.960 98.814  1.00 43.91  ? 192 ASP C CG  1 
ATOM   5313 O OD1 . ASP C  1 177 ? 31.886 -37.409 98.714  1.00 47.63  ? 192 ASP C OD1 1 
ATOM   5314 O OD2 . ASP C  1 177 ? 30.417 -38.594 99.821  1.00 48.97  ? 192 ASP C OD2 1 
ATOM   5315 N N   . ASP C  1 178 ? 28.110 -35.947 95.400  1.00 35.47  ? 193 ASP C N   1 
ATOM   5316 C CA  . ASP C  1 178 ? 27.256 -35.838 94.181  1.00 35.45  ? 193 ASP C CA  1 
ATOM   5317 C C   . ASP C  1 178 ? 27.774 -34.736 93.241  1.00 34.95  ? 193 ASP C C   1 
ATOM   5318 O O   . ASP C  1 178 ? 27.054 -34.406 92.286  1.00 36.33  ? 193 ASP C O   1 
ATOM   5319 C CB  . ASP C  1 178 ? 25.792 -35.601 94.552  1.00 34.52  ? 193 ASP C CB  1 
ATOM   5320 C CG  . ASP C  1 178 ? 25.508 -34.260 95.209  1.00 34.77  ? 193 ASP C CG  1 
ATOM   5321 O OD1 . ASP C  1 178 ? 26.422 -33.711 95.859  1.00 34.55  ? 193 ASP C OD1 1 
ATOM   5322 O OD2 . ASP C  1 178 ? 24.355 -33.803 95.129  1.00 35.61  ? 193 ASP C OD2 1 
ATOM   5323 N N   . MET C  1 179 ? 28.951 -34.168 93.516  1.00 34.33  ? 194 MET C N   1 
ATOM   5324 C CA  . MET C  1 179 ? 29.563 -33.087 92.705  1.00 33.82  ? 194 MET C CA  1 
ATOM   5325 C C   . MET C  1 179 ? 30.868 -33.591 92.091  1.00 36.07  ? 194 MET C C   1 
ATOM   5326 O O   . MET C  1 179 ? 31.432 -34.592 92.572  1.00 36.94  ? 194 MET C O   1 
ATOM   5327 C CB  . MET C  1 179 ? 29.834 -31.838 93.545  1.00 32.83  ? 194 MET C CB  1 
ATOM   5328 C CG  . MET C  1 179 ? 28.560 -31.240 94.108  1.00 33.95  ? 194 MET C CG  1 
ATOM   5329 S SD  . MET C  1 179 ? 28.816 -29.950 95.332  1.00 34.40  ? 194 MET C SD  1 
ATOM   5330 C CE  . MET C  1 179 ? 27.168 -29.905 96.027  1.00 34.07  ? 194 MET C CE  1 
ATOM   5331 N N   . LEU C  1 180 ? 31.271 -32.934 91.012  1.00 38.13  ? 195 LEU C N   1 
ATOM   5332 C CA  . LEU C  1 180 ? 32.482 -33.208 90.204  1.00 39.49  ? 195 LEU C CA  1 
ATOM   5333 C C   . LEU C  1 180 ? 33.161 -31.857 89.971  1.00 41.58  ? 195 LEU C C   1 
ATOM   5334 O O   . LEU C  1 180 ? 32.436 -30.841 89.923  1.00 41.73  ? 195 LEU C O   1 
ATOM   5335 C CB  . LEU C  1 180 ? 32.016 -33.875 88.906  1.00 42.68  ? 195 LEU C CB  1 
ATOM   5336 C CG  . LEU C  1 180 ? 33.106 -34.326 87.939  1.00 45.00  ? 195 LEU C CG  1 
ATOM   5337 C CD1 . LEU C  1 180 ? 32.662 -35.561 87.171  1.00 46.58  ? 195 LEU C CD1 1 
ATOM   5338 C CD2 . LEU C  1 180 ? 33.464 -33.214 86.970  1.00 47.22  ? 195 LEU C CD2 1 
ATOM   5339 N N   . CYS C  1 181 ? 34.483 -31.833 89.820  1.00 40.31  ? 196 CYS C N   1 
ATOM   5340 C CA  A CYS C  1 181 ? 35.302 -30.587 89.787  0.50 41.58  ? 196 CYS C CA  1 
ATOM   5341 C CA  B CYS C  1 181 ? 35.256 -30.575 89.752  0.50 41.73  ? 196 CYS C CA  1 
ATOM   5342 C C   . CYS C  1 181 ? 36.230 -30.580 88.565  1.00 40.10  ? 196 CYS C C   1 
ATOM   5343 O O   . CYS C  1 181 ? 36.837 -31.622 88.301  1.00 40.05  ? 196 CYS C O   1 
ATOM   5344 C CB  A CYS C  1 181 ? 36.123 -30.456 91.066  0.50 43.82  ? 196 CYS C CB  1 
ATOM   5345 C CB  B CYS C  1 181 ? 35.938 -30.388 91.094  0.50 44.33  ? 196 CYS C CB  1 
ATOM   5346 S SG  A CYS C  1 181 ? 35.200 -29.717 92.435  0.50 45.27  ? 196 CYS C SG  1 
ATOM   5347 S SG  B CYS C  1 181 ? 37.328 -29.245 91.040  0.50 46.08  ? 196 CYS C SG  1 
ATOM   5348 N N   . ALA C  1 182 ? 36.347 -29.430 87.888  1.00 40.02  ? 197 ALA C N   1 
ATOM   5349 C CA  . ALA C  1 182 ? 37.245 -29.217 86.729  1.00 39.43  ? 197 ALA C CA  1 
ATOM   5350 C C   . ALA C  1 182 ? 37.524 -27.722 86.530  1.00 40.17  ? 197 ALA C C   1 
ATOM   5351 O O   . ALA C  1 182 ? 36.642 -26.887 86.859  1.00 37.93  ? 197 ALA C O   1 
ATOM   5352 C CB  . ALA C  1 182 ? 36.630 -29.814 85.485  1.00 39.04  ? 197 ALA C CB  1 
ATOM   5353 N N   . GLY C  1 183 ? 38.698 -27.404 85.976  1.00 40.11  ? 198 GLY C N   1 
ATOM   5354 C CA  . GLY C  1 183 ? 39.069 -26.049 85.526  1.00 41.05  ? 198 GLY C CA  1 
ATOM   5355 C C   . GLY C  1 183 ? 40.183 -25.450 86.364  1.00 43.21  ? 198 GLY C C   1 
ATOM   5356 O O   . GLY C  1 183 ? 40.550 -26.045 87.397  1.00 43.53  ? 198 GLY C O   1 
ATOM   5357 N N   . ASN C  1 184 ? 40.683 -24.293 85.930  1.00 42.48  ? 199 ASN C N   1 
ATOM   5358 C CA  . ASN C  1 184 ? 41.855 -23.599 86.519  1.00 44.16  ? 199 ASN C CA  1 
ATOM   5359 C C   . ASN C  1 184 ? 41.663 -22.098 86.285  1.00 43.14  ? 199 ASN C C   1 
ATOM   5360 O O   . ASN C  1 184 ? 40.547 -21.703 85.873  1.00 41.76  ? 199 ASN C O   1 
ATOM   5361 C CB  . ASN C  1 184 ? 43.161 -24.187 85.967  1.00 44.40  ? 199 ASN C CB  1 
ATOM   5362 C CG  . ASN C  1 184 ? 43.257 -24.133 84.455  1.00 45.26  ? 199 ASN C CG  1 
ATOM   5363 O OD1 . ASN C  1 184 ? 42.867 -23.146 83.839  1.00 45.07  ? 199 ASN C OD1 1 
ATOM   5364 N ND2 . ASN C  1 184 ? 43.763 -25.189 83.842  1.00 44.92  ? 199 ASN C ND2 1 
ATOM   5365 N N   . THR C  1 185 ? 42.709 -21.297 86.508  1.00 45.57  ? 200 THR C N   1 
ATOM   5366 C CA  . THR C  1 185 ? 42.666 -19.813 86.417  1.00 45.15  ? 200 THR C CA  1 
ATOM   5367 C C   . THR C  1 185 ? 42.684 -19.338 84.959  1.00 44.35  ? 200 THR C C   1 
ATOM   5368 O O   . THR C  1 185 ? 42.505 -18.122 84.748  1.00 46.05  ? 200 THR C O   1 
ATOM   5369 C CB  . THR C  1 185 ? 43.798 -19.179 87.238  1.00 46.26  ? 200 THR C CB  1 
ATOM   5370 O OG1 . THR C  1 185 ? 45.042 -19.746 86.827  1.00 44.15  ? 200 THR C OG1 1 
ATOM   5371 C CG2 . THR C  1 185 ? 43.611 -19.389 88.723  1.00 47.77  ? 200 THR C CG2 1 
ATOM   5372 N N   . ARG C  1 186 ? 42.867 -20.238 83.985  1.00 46.12  ? 201 ARG C N   1 
ATOM   5373 C CA  . ARG C  1 186 ? 42.800 -19.912 82.533  1.00 46.46  ? 201 ARG C CA  1 
ATOM   5374 C C   . ARG C  1 186 ? 41.531 -20.498 81.893  1.00 43.60  ? 201 ARG C C   1 
ATOM   5375 O O   . ARG C  1 186 ? 41.094 -19.934 80.879  1.00 43.41  ? 201 ARG C O   1 
ATOM   5376 C CB  . ARG C  1 186 ? 44.062 -20.427 81.828  1.00 48.64  ? 201 ARG C CB  1 
ATOM   5377 C CG  . ARG C  1 186 ? 45.355 -19.776 82.306  1.00 49.85  ? 201 ARG C CG  1 
ATOM   5378 C CD  . ARG C  1 186 ? 46.592 -20.333 81.627  1.00 53.06  ? 201 ARG C CD  1 
ATOM   5379 N NE  . ARG C  1 186 ? 47.828 -19.812 82.193  0.00 52.29  ? 201 ARG C NE  1 
ATOM   5380 C CZ  . ARG C  1 186 ? 48.350 -18.606 81.966  0.00 52.33  ? 201 ARG C CZ  1 
ATOM   5381 N NH1 . ARG C  1 186 ? 47.762 -17.732 81.164  0.00 52.31  ? 201 ARG C NH1 1 
ATOM   5382 N NH2 . ARG C  1 186 ? 49.484 -18.274 82.557  0.00 52.28  ? 201 ARG C NH2 1 
ATOM   5383 N N   . ARG C  1 187 ? 40.970 -21.585 82.437  1.00 42.28  ? 202 ARG C N   1 
ATOM   5384 C CA  . ARG C  1 187 ? 39.991 -22.458 81.730  1.00 42.98  ? 202 ARG C CA  1 
ATOM   5385 C C   . ARG C  1 187 ? 38.851 -22.808 82.695  1.00 41.28  ? 202 ARG C C   1 
ATOM   5386 O O   . ARG C  1 187 ? 39.115 -23.492 83.707  1.00 39.86  ? 202 ARG C O   1 
ATOM   5387 C CB  . ARG C  1 187 ? 40.669 -23.729 81.197  1.00 46.52  ? 202 ARG C CB  1 
ATOM   5388 C CG  . ARG C  1 187 ? 41.978 -23.512 80.441  1.00 49.94  ? 202 ARG C CG  1 
ATOM   5389 C CD  . ARG C  1 187 ? 42.105 -24.211 79.103  1.00 54.50  ? 202 ARG C CD  1 
ATOM   5390 N NE  . ARG C  1 187 ? 43.384 -23.916 78.468  1.00 58.27  ? 202 ARG C NE  1 
ATOM   5391 C CZ  . ARG C  1 187 ? 43.713 -22.765 77.869  1.00 62.07  ? 202 ARG C CZ  1 
ATOM   5392 N NH1 . ARG C  1 187 ? 42.862 -21.751 77.800  1.00 60.14  ? 202 ARG C NH1 1 
ATOM   5393 N NH2 . ARG C  1 187 ? 44.919 -22.630 77.340  1.00 65.09  ? 202 ARG C NH2 1 
ATOM   5394 N N   . ASP C  1 188 ? 37.626 -22.363 82.405  1.00 38.17  ? 203 ASP C N   1 
ATOM   5395 C CA  . ASP C  1 188 ? 36.464 -22.572 83.308  1.00 38.28  ? 203 ASP C CA  1 
ATOM   5396 C C   . ASP C  1 188 ? 35.157 -22.314 82.551  1.00 37.11  ? 203 ASP C C   1 
ATOM   5397 O O   . ASP C  1 188 ? 35.177 -21.696 81.471  1.00 35.84  ? 203 ASP C O   1 
ATOM   5398 C CB  . ASP C  1 188 ? 36.580 -21.679 84.555  1.00 39.09  ? 203 ASP C CB  1 
ATOM   5399 C CG  . ASP C  1 188 ? 35.810 -22.137 85.787  1.00 39.97  ? 203 ASP C CG  1 
ATOM   5400 O OD1 . ASP C  1 188 ? 35.134 -23.181 85.718  1.00 40.35  ? 203 ASP C OD1 1 
ATOM   5401 O OD2 . ASP C  1 188 ? 35.893 -21.435 86.821  1.00 41.08  ? 203 ASP C OD2 1 
ATOM   5402 N N   . SER C  1 189 ? 34.061 -22.796 83.125  1.00 36.91  ? 204 SER C N   1 
ATOM   5403 C CA  . SER C  1 189 ? 32.672 -22.404 82.786  1.00 37.52  ? 204 SER C CA  1 
ATOM   5404 C C   . SER C  1 189 ? 32.340 -21.137 83.579  1.00 36.41  ? 204 SER C C   1 
ATOM   5405 O O   . SER C  1 189 ? 33.084 -20.824 84.533  1.00 39.04  ? 204 SER C O   1 
ATOM   5406 C CB  . SER C  1 189 ? 31.724 -23.531 83.083  1.00 38.05  ? 204 SER C CB  1 
ATOM   5407 O OG  . SER C  1 189 ? 31.792 -23.891 84.458  1.00 37.92  ? 204 SER C OG  1 
ATOM   5408 N N   . CYS C  1 190 ? 31.277 -20.431 83.209  1.00 36.05  ? 205 CYS C N   1 
ATOM   5409 C CA  . CYS C  1 190 ? 30.895 -19.136 83.831  1.00 37.35  ? 205 CYS C CA  1 
ATOM   5410 C C   . CYS C  1 190 ? 29.375 -18.954 83.775  1.00 37.28  ? 205 CYS C C   1 
ATOM   5411 O O   . CYS C  1 190 ? 28.680 -19.896 83.357  1.00 35.45  ? 205 CYS C O   1 
ATOM   5412 C CB  . CYS C  1 190 ? 31.637 -17.987 83.151  1.00 40.49  ? 205 CYS C CB  1 
ATOM   5413 S SG  . CYS C  1 190 ? 31.820 -16.493 84.171  1.00 45.87  ? 205 CYS C SG  1 
ATOM   5414 N N   . GLN C  1 191 ? 28.889 -17.806 84.259  1.00 36.91  ? 206 GLN C N   1 
ATOM   5415 C CA  A GLN C  1 191 ? 27.449 -17.431 84.275  0.50 36.01  ? 206 GLN C CA  1 
ATOM   5416 C CA  B GLN C  1 191 ? 27.452 -17.417 84.269  0.50 35.55  ? 206 GLN C CA  1 
ATOM   5417 C C   . GLN C  1 191 ? 26.898 -17.555 82.846  1.00 34.86  ? 206 GLN C C   1 
ATOM   5418 O O   . GLN C  1 191 ? 27.524 -17.004 81.927  1.00 35.77  ? 206 GLN C O   1 
ATOM   5419 C CB  A GLN C  1 191 ? 27.256 -16.022 84.849  0.50 36.34  ? 206 GLN C CB  1 
ATOM   5420 C CB  B GLN C  1 191 ? 27.309 -15.990 84.810  0.50 35.29  ? 206 GLN C CB  1 
ATOM   5421 C CG  A GLN C  1 191 ? 27.361 -15.939 86.371  0.50 36.68  ? 206 GLN C CG  1 
ATOM   5422 C CG  B GLN C  1 191 ? 25.886 -15.449 84.812  0.50 34.79  ? 206 GLN C CG  1 
ATOM   5423 C CD  A GLN C  1 191 ? 28.784 -15.960 86.884  0.50 36.90  ? 206 GLN C CD  1 
ATOM   5424 C CD  B GLN C  1 191 ? 25.776 -14.133 85.541  0.00 34.83  ? 206 GLN C CD  1 
ATOM   5425 O OE1 A GLN C  1 191 ? 29.709 -15.485 86.233  0.50 36.47  ? 206 GLN C OE1 1 
ATOM   5426 O OE1 B GLN C  1 191 ? 26.595 -13.813 86.400  0.00 34.76  ? 206 GLN C OE1 1 
ATOM   5427 N NE2 A GLN C  1 191 ? 28.976 -16.506 88.072  0.50 37.50  ? 206 GLN C NE2 1 
ATOM   5428 N NE2 B GLN C  1 191 ? 24.752 -13.362 85.214  0.00 34.77  ? 206 GLN C NE2 1 
ATOM   5429 N N   . GLY C  1 192 ? 25.789 -18.285 82.682  1.00 32.03  ? 207 GLY C N   1 
ATOM   5430 C CA  . GLY C  1 192 ? 25.168 -18.578 81.377  1.00 32.19  ? 207 GLY C CA  1 
ATOM   5431 C C   . GLY C  1 192 ? 25.555 -19.939 80.813  1.00 31.84  ? 207 GLY C C   1 
ATOM   5432 O O   . GLY C  1 192 ? 24.887 -20.385 79.866  1.00 34.02  ? 207 GLY C O   1 
ATOM   5433 N N   . ASP C  1 193 ? 26.601 -20.580 81.340  1.00 32.03  ? 208 ASP C N   1 
ATOM   5434 C CA  . ASP C  1 193 ? 27.003 -21.960 80.964  1.00 32.38  ? 208 ASP C CA  1 
ATOM   5435 C C   . ASP C  1 193 ? 26.278 -22.983 81.836  1.00 33.87  ? 208 ASP C C   1 
ATOM   5436 O O   . ASP C  1 193 ? 26.306 -24.166 81.463  1.00 32.62  ? 208 ASP C O   1 
ATOM   5437 C CB  . ASP C  1 193 ? 28.513 -22.163 81.067  1.00 33.43  ? 208 ASP C CB  1 
ATOM   5438 C CG  . ASP C  1 193 ? 29.293 -21.324 80.085  1.00 32.35  ? 208 ASP C CG  1 
ATOM   5439 O OD1 . ASP C  1 193 ? 28.850 -21.228 78.922  1.00 31.48  ? 208 ASP C OD1 1 
ATOM   5440 O OD2 . ASP C  1 193 ? 30.340 -20.787 80.488  1.00 33.47  ? 208 ASP C OD2 1 
ATOM   5441 N N   . SER C  1 194 ? 25.664 -22.543 82.940  1.00 35.51  ? 209 SER C N   1 
ATOM   5442 C CA  . SER C  1 194 ? 24.915 -23.379 83.912  1.00 35.18  ? 209 SER C CA  1 
ATOM   5443 C C   . SER C  1 194 ? 23.962 -24.319 83.181  1.00 33.16  ? 209 SER C C   1 
ATOM   5444 O O   . SER C  1 194 ? 23.286 -23.861 82.231  1.00 33.78  ? 209 SER C O   1 
ATOM   5445 C CB  . SER C  1 194 ? 24.169 -22.539 84.902  1.00 37.48  ? 209 SER C CB  1 
ATOM   5446 O OG  . SER C  1 194 ? 25.051 -22.091 85.914  1.00 37.56  ? 209 SER C OG  1 
ATOM   5447 N N   . GLY C  1 195 ? 23.934 -25.582 83.612  1.00 32.07  ? 210 GLY C N   1 
ATOM   5448 C CA  . GLY C  1 195 ? 23.069 -26.626 83.039  1.00 31.50  ? 210 GLY C CA  1 
ATOM   5449 C C   . GLY C  1 195 ? 23.681 -27.298 81.830  1.00 31.68  ? 210 GLY C C   1 
ATOM   5450 O O   . GLY C  1 195 ? 23.173 -28.360 81.441  1.00 32.56  ? 210 GLY C O   1 
ATOM   5451 N N   . GLY C  1 196 ? 24.743 -26.722 81.261  1.00 32.18  ? 211 GLY C N   1 
ATOM   5452 C CA  . GLY C  1 196 ? 25.441 -27.255 80.082  1.00 32.16  ? 211 GLY C CA  1 
ATOM   5453 C C   . GLY C  1 196 ? 26.274 -28.480 80.435  1.00 34.10  ? 211 GLY C C   1 
ATOM   5454 O O   . GLY C  1 196 ? 26.510 -28.757 81.605  1.00 32.87  ? 211 GLY C O   1 
ATOM   5455 N N   . PRO C  1 197 ? 26.735 -29.247 79.427  1.00 36.79  ? 212 PRO C N   1 
ATOM   5456 C CA  . PRO C  1 197 ? 27.444 -30.500 79.670  1.00 35.76  ? 212 PRO C CA  1 
ATOM   5457 C C   . PRO C  1 197 ? 28.963 -30.344 79.833  1.00 36.29  ? 212 PRO C C   1 
ATOM   5458 O O   . PRO C  1 197 ? 29.558 -29.523 79.153  1.00 36.62  ? 212 PRO C O   1 
ATOM   5459 C CB  . PRO C  1 197 ? 27.098 -31.285 78.403  1.00 36.24  ? 212 PRO C CB  1 
ATOM   5460 C CG  . PRO C  1 197 ? 27.056 -30.230 77.316  1.00 37.15  ? 212 PRO C CG  1 
ATOM   5461 C CD  . PRO C  1 197 ? 26.589 -28.954 77.993  1.00 36.75  ? 212 PRO C CD  1 
ATOM   5462 N N   . LEU C  1 198 ? 29.527 -31.115 80.769  1.00 36.13  ? 213 LEU C N   1 
ATOM   5463 C CA  . LEU C  1 198 ? 30.954 -31.518 80.798  1.00 35.61  ? 213 LEU C CA  1 
ATOM   5464 C C   . LEU C  1 198 ? 31.035 -32.925 80.200  1.00 35.41  ? 213 LEU C C   1 
ATOM   5465 O O   . LEU C  1 198 ? 30.391 -33.838 80.752  1.00 36.38  ? 213 LEU C O   1 
ATOM   5466 C CB  . LEU C  1 198 ? 31.476 -31.490 82.235  1.00 35.26  ? 213 LEU C CB  1 
ATOM   5467 C CG  . LEU C  1 198 ? 32.973 -31.749 82.393  1.00 36.21  ? 213 LEU C CG  1 
ATOM   5468 C CD1 . LEU C  1 198 ? 33.802 -30.603 81.833  1.00 36.75  ? 213 LEU C CD1 1 
ATOM   5469 C CD2 . LEU C  1 198 ? 33.321 -31.966 83.851  1.00 37.64  ? 213 LEU C CD2 1 
ATOM   5470 N N   . VAL C  1 199 ? 31.740 -33.067 79.080  1.00 34.74  ? 214 VAL C N   1 
ATOM   5471 C CA  . VAL C  1 199 ? 31.802 -34.319 78.271  1.00 36.16  ? 214 VAL C CA  1 
ATOM   5472 C C   . VAL C  1 199 ? 33.262 -34.776 78.191  1.00 38.51  ? 214 VAL C C   1 
ATOM   5473 O O   . VAL C  1 199 ? 34.154 -33.913 78.063  1.00 36.52  ? 214 VAL C O   1 
ATOM   5474 C CB  . VAL C  1 199 ? 31.160 -34.140 76.881  1.00 36.32  ? 214 VAL C CB  1 
ATOM   5475 C CG1 . VAL C  1 199 ? 29.665 -33.912 76.998  1.00 34.45  ? 214 VAL C CG1 1 
ATOM   5476 C CG2 . VAL C  1 199 ? 31.805 -33.036 76.051  1.00 37.76  ? 214 VAL C CG2 1 
ATOM   5477 N N   . CYS C  1 200 ? 33.490 -36.085 78.311  1.00 40.75  ? 215 CYS C N   1 
ATOM   5478 C CA  . CYS C  1 200 ? 34.828 -36.730 78.246  1.00 42.75  ? 215 CYS C CA  1 
ATOM   5479 C C   . CYS C  1 200 ? 34.760 -37.867 77.217  1.00 41.33  ? 215 CYS C C   1 
ATOM   5480 O O   . CYS C  1 200 ? 33.750 -38.601 77.214  1.00 40.09  ? 215 CYS C O   1 
ATOM   5481 C CB  . CYS C  1 200 ? 35.271 -37.253 79.613  1.00 46.02  ? 215 CYS C CB  1 
ATOM   5482 S SG  . CYS C  1 200 ? 34.935 -36.137 81.008  1.00 48.60  ? 215 CYS C SG  1 
ATOM   5483 N N   . LYS C  1 201 ? 35.766 -37.983 76.353  1.00 41.89  ? 216 LYS C N   1 
ATOM   5484 C CA  . LYS C  1 201 ? 35.816 -39.032 75.301  1.00 46.30  ? 216 LYS C CA  1 
ATOM   5485 C C   . LYS C  1 201 ? 36.497 -40.264 75.902  1.00 46.46  ? 216 LYS C C   1 
ATOM   5486 O O   . LYS C  1 201 ? 37.688 -40.166 76.228  1.00 46.40  ? 216 LYS C O   1 
ATOM   5487 C CB  . LYS C  1 201 ? 36.511 -38.539 74.030  1.00 48.46  ? 216 LYS C CB  1 
ATOM   5488 C CG  . LYS C  1 201 ? 36.156 -39.342 72.787  1.00 48.48  ? 216 LYS C CG  1 
ATOM   5489 C CD  . LYS C  1 201 ? 36.773 -38.817 71.516  1.00 49.58  ? 216 LYS C CD  1 
ATOM   5490 C CE  . LYS C  1 201 ? 36.146 -39.446 70.292  1.00 50.05  ? 216 LYS C CE  1 
ATOM   5491 N NZ  . LYS C  1 201 ? 36.773 -38.947 69.048  1.00 51.38  ? 216 LYS C NZ  1 
ATOM   5492 N N   . VAL C  1 202 ? 35.753 -41.366 76.042  1.00 50.03  ? 217 VAL C N   1 
ATOM   5493 C CA  . VAL C  1 202 ? 36.203 -42.648 76.664  1.00 52.38  ? 217 VAL C CA  1 
ATOM   5494 C C   . VAL C  1 202 ? 35.905 -43.786 75.678  1.00 53.23  ? 217 VAL C C   1 
ATOM   5495 O O   . VAL C  1 202 ? 34.716 -44.031 75.405  1.00 51.56  ? 217 VAL C O   1 
ATOM   5496 C CB  . VAL C  1 202 ? 35.505 -42.894 78.020  1.00 54.17  ? 217 VAL C CB  1 
ATOM   5497 C CG1 . VAL C  1 202 ? 36.031 -44.141 78.719  1.00 55.07  ? 217 VAL C CG1 1 
ATOM   5498 C CG2 . VAL C  1 202 ? 35.612 -41.694 78.951  1.00 54.23  ? 217 VAL C CG2 1 
ATOM   5499 N N   . ASN C  1 203 ? 36.947 -44.458 75.180  1.00 58.35  ? 218 ASN C N   1 
ATOM   5500 C CA  . ASN C  1 203 ? 36.860 -45.619 74.247  1.00 60.61  ? 218 ASN C CA  1 
ATOM   5501 C C   . ASN C  1 203 ? 36.060 -45.209 73.007  1.00 59.68  ? 218 ASN C C   1 
ATOM   5502 O O   . ASN C  1 203 ? 35.105 -45.933 72.638  1.00 58.64  ? 218 ASN C O   1 
ATOM   5503 C CB  . ASN C  1 203 ? 36.256 -46.856 74.922  1.00 64.38  ? 218 ASN C CB  1 
ATOM   5504 C CG  . ASN C  1 203 ? 37.027 -47.305 76.144  1.00 69.45  ? 218 ASN C CG  1 
ATOM   5505 O OD1 . ASN C  1 203 ? 38.186 -46.934 76.329  1.00 71.84  ? 218 ASN C OD1 1 
ATOM   5506 N ND2 . ASN C  1 203 ? 36.397 -48.114 76.982  1.00 71.76  ? 218 ASN C ND2 1 
ATOM   5507 N N   . GLY C  1 204 ? 36.408 -44.052 72.430  1.00 60.33  ? 219 GLY C N   1 
ATOM   5508 C CA  . GLY C  1 204 ? 35.811 -43.506 71.195  1.00 57.91  ? 219 GLY C CA  1 
ATOM   5509 C C   . GLY C  1 204 ? 34.419 -42.917 71.381  1.00 56.83  ? 219 GLY C C   1 
ATOM   5510 O O   . GLY C  1 204 ? 33.848 -42.484 70.361  1.00 54.27  ? 219 GLY C O   1 
ATOM   5511 N N   . THR C  1 205 ? 33.876 -42.895 72.606  1.00 52.69  ? 220 THR C N   1 
ATOM   5512 C CA  . THR C  1 205 ? 32.504 -42.404 72.900  1.00 52.38  ? 220 THR C CA  1 
ATOM   5513 C C   . THR C  1 205 ? 32.607 -41.172 73.803  1.00 46.94  ? 220 THR C C   1 
ATOM   5514 O O   . THR C  1 205 ? 33.295 -41.241 74.836  1.00 42.44  ? 220 THR C O   1 
ATOM   5515 C CB  . THR C  1 205 ? 31.619 -43.504 73.501  1.00 54.33  ? 220 THR C CB  1 
ATOM   5516 O OG1 . THR C  1 205 ? 31.620 -44.601 72.589  1.00 59.65  ? 220 THR C OG1 1 
ATOM   5517 C CG2 . THR C  1 205 ? 30.197 -43.050 73.755  1.00 54.50  ? 220 THR C CG2 1 
ATOM   5518 N N   . TRP C  1 206 ? 31.939 -40.085 73.410  1.00 44.51  ? 221 TRP C N   1 
ATOM   5519 C CA  . TRP C  1 206 ? 31.692 -38.900 74.270  1.00 41.18  ? 221 TRP C CA  1 
ATOM   5520 C C   . TRP C  1 206 ? 30.667 -39.276 75.345  1.00 39.11  ? 221 TRP C C   1 
ATOM   5521 O O   . TRP C  1 206 ? 29.565 -39.711 74.975  1.00 42.09  ? 221 TRP C O   1 
ATOM   5522 C CB  . TRP C  1 206 ? 31.236 -37.700 73.434  1.00 40.76  ? 221 TRP C CB  1 
ATOM   5523 C CG  . TRP C  1 206 ? 32.349 -37.134 72.610  1.00 39.90  ? 221 TRP C CG  1 
ATOM   5524 C CD1 . TRP C  1 206 ? 32.578 -37.350 71.283  1.00 39.51  ? 221 TRP C CD1 1 
ATOM   5525 C CD2 . TRP C  1 206 ? 33.421 -36.295 73.073  1.00 38.20  ? 221 TRP C CD2 1 
ATOM   5526 N NE1 . TRP C  1 206 ? 33.711 -36.694 70.886  1.00 41.40  ? 221 TRP C NE1 1 
ATOM   5527 C CE2 . TRP C  1 206 ? 34.244 -36.027 71.956  1.00 39.28  ? 221 TRP C CE2 1 
ATOM   5528 C CE3 . TRP C  1 206 ? 33.753 -35.722 74.307  1.00 36.89  ? 221 TRP C CE3 1 
ATOM   5529 C CZ2 . TRP C  1 206 ? 35.383 -35.228 72.044  1.00 39.59  ? 221 TRP C CZ2 1 
ATOM   5530 C CZ3 . TRP C  1 206 ? 34.883 -34.937 74.394  1.00 36.51  ? 221 TRP C CZ3 1 
ATOM   5531 C CH2 . TRP C  1 206 ? 35.685 -34.693 73.277  1.00 37.68  ? 221 TRP C CH2 1 
ATOM   5532 N N   . LEU C  1 207 ? 31.051 -39.164 76.618  1.00 38.22  ? 222 LEU C N   1 
ATOM   5533 C CA  . LEU C  1 207 ? 30.188 -39.432 77.796  1.00 38.97  ? 222 LEU C CA  1 
ATOM   5534 C C   . LEU C  1 207 ? 30.016 -38.130 78.584  1.00 36.40  ? 222 LEU C C   1 
ATOM   5535 O O   . LEU C  1 207 ? 31.024 -37.439 78.811  1.00 39.16  ? 222 LEU C O   1 
ATOM   5536 C CB  . LEU C  1 207 ? 30.828 -40.530 78.656  1.00 41.14  ? 222 LEU C CB  1 
ATOM   5537 C CG  . LEU C  1 207 ? 31.001 -41.888 77.976  1.00 41.13  ? 222 LEU C CG  1 
ATOM   5538 C CD1 . LEU C  1 207 ? 31.786 -42.839 78.865  1.00 43.67  ? 222 LEU C CD1 1 
ATOM   5539 C CD2 . LEU C  1 207 ? 29.650 -42.491 77.610  1.00 41.29  ? 222 LEU C CD2 1 
ATOM   5540 N N   . GLN C  1 208 ? 28.792 -37.815 79.002  1.00 34.38  ? 223 GLN C N   1 
ATOM   5541 C CA  . GLN C  1 208 ? 28.530 -36.635 79.859  1.00 35.60  ? 223 GLN C CA  1 
ATOM   5542 C C   . GLN C  1 208 ? 28.888 -36.978 81.314  1.00 34.65  ? 223 GLN C C   1 
ATOM   5543 O O   . GLN C  1 208 ? 28.108 -37.679 81.974  1.00 32.74  ? 223 GLN C O   1 
ATOM   5544 C CB  . GLN C  1 208 ? 27.096 -36.125 79.725  1.00 35.42  ? 223 GLN C CB  1 
ATOM   5545 C CG  . GLN C  1 208 ? 26.937 -34.789 80.435  1.00 36.12  ? 223 GLN C CG  1 
ATOM   5546 C CD  . GLN C  1 208 ? 25.632 -34.079 80.183  1.00 37.20  ? 223 GLN C CD  1 
ATOM   5547 O OE1 . GLN C  1 208 ? 24.883 -34.390 79.257  1.00 36.93  ? 223 GLN C OE1 1 
ATOM   5548 N NE2 . GLN C  1 208 ? 25.365 -33.092 81.022  1.00 39.01  ? 223 GLN C NE2 1 
ATOM   5549 N N   . ALA C  1 209 ? 30.029 -36.474 81.786  1.00 34.01  ? 224 ALA C N   1 
ATOM   5550 C CA  . ALA C  1 209 ? 30.519 -36.624 83.176  1.00 34.47  ? 224 ALA C CA  1 
ATOM   5551 C C   . ALA C  1 209 ? 29.756 -35.688 84.126  1.00 35.73  ? 224 ALA C C   1 
ATOM   5552 O O   . ALA C  1 209 ? 29.510 -36.107 85.281  1.00 32.57  ? 224 ALA C O   1 
ATOM   5553 C CB  . ALA C  1 209 ? 32.002 -36.359 83.230  1.00 33.62  ? 224 ALA C CB  1 
ATOM   5554 N N   . GLY C  1 210 ? 29.398 -34.476 83.668  1.00 34.01  ? 225 GLY C N   1 
ATOM   5555 C CA  . GLY C  1 210 ? 28.951 -33.385 84.554  1.00 34.81  ? 225 GLY C CA  1 
ATOM   5556 C C   . GLY C  1 210 ? 27.902 -32.465 83.947  1.00 34.30  ? 225 GLY C C   1 
ATOM   5557 O O   . GLY C  1 210 ? 27.759 -32.417 82.709  1.00 36.34  ? 225 GLY C O   1 
ATOM   5558 N N   . VAL C  1 211 ? 27.173 -31.777 84.824  1.00 33.11  ? 226 VAL C N   1 
ATOM   5559 C CA  . VAL C  1 211 ? 26.285 -30.629 84.505  1.00 32.96  ? 226 VAL C CA  1 
ATOM   5560 C C   . VAL C  1 211 ? 26.883 -29.406 85.204  1.00 31.97  ? 226 VAL C C   1 
ATOM   5561 O O   . VAL C  1 211 ? 27.085 -29.484 86.414  1.00 34.47  ? 226 VAL C O   1 
ATOM   5562 C CB  . VAL C  1 211 ? 24.839 -30.913 84.946  1.00 32.48  ? 226 VAL C CB  1 
ATOM   5563 C CG1 . VAL C  1 211 ? 23.922 -29.721 84.716  1.00 32.83  ? 226 VAL C CG1 1 
ATOM   5564 C CG2 . VAL C  1 211 ? 24.286 -32.145 84.242  1.00 32.70  ? 226 VAL C CG2 1 
ATOM   5565 N N   . VAL C  1 212 ? 27.125 -28.313 84.475  1.00 32.62  ? 227 VAL C N   1 
ATOM   5566 C CA  . VAL C  1 212 ? 27.654 -27.032 85.041  1.00 32.13  ? 227 VAL C CA  1 
ATOM   5567 C C   . VAL C  1 212 ? 26.707 -26.607 86.170  1.00 31.07  ? 227 VAL C C   1 
ATOM   5568 O O   . VAL C  1 212 ? 25.497 -26.477 85.896  1.00 33.99  ? 227 VAL C O   1 
ATOM   5569 C CB  . VAL C  1 212 ? 27.800 -25.923 83.982  1.00 29.86  ? 227 VAL C CB  1 
ATOM   5570 C CG1 . VAL C  1 212 ? 28.287 -24.612 84.596  1.00 30.68  ? 227 VAL C CG1 1 
ATOM   5571 C CG2 . VAL C  1 212 ? 28.737 -26.315 82.856  1.00 30.77  ? 227 VAL C CG2 1 
ATOM   5572 N N   . SER C  1 213 ? 27.230 -26.453 87.390  1.00 29.27  ? 228 SER C N   1 
ATOM   5573 C CA  . SER C  1 213 ? 26.432 -26.224 88.624  1.00 30.00  ? 228 SER C CA  1 
ATOM   5574 C C   . SER C  1 213 ? 26.784 -24.878 89.267  1.00 30.75  ? 228 SER C C   1 
ATOM   5575 O O   . SER C  1 213 ? 25.925 -23.987 89.256  1.00 33.07  ? 228 SER C O   1 
ATOM   5576 C CB  . SER C  1 213 ? 26.583 -27.362 89.596  1.00 29.44  ? 228 SER C CB  1 
ATOM   5577 O OG  . SER C  1 213 ? 25.701 -27.196 90.704  1.00 29.92  ? 228 SER C OG  1 
ATOM   5578 N N   . TRP C  1 214 ? 27.972 -24.741 89.849  1.00 31.77  ? 229 TRP C N   1 
ATOM   5579 C CA  . TRP C  1 214 ? 28.334 -23.538 90.642  1.00 31.71  ? 229 TRP C CA  1 
ATOM   5580 C C   . TRP C  1 214 ? 29.846 -23.378 90.747  1.00 31.61  ? 229 TRP C C   1 
ATOM   5581 O O   . TRP C  1 214 ? 30.600 -24.261 90.308  1.00 32.45  ? 229 TRP C O   1 
ATOM   5582 C CB  . TRP C  1 214 ? 27.653 -23.547 92.018  1.00 31.50  ? 229 TRP C CB  1 
ATOM   5583 C CG  . TRP C  1 214 ? 28.110 -24.616 92.961  1.00 33.21  ? 229 TRP C CG  1 
ATOM   5584 C CD1 . TRP C  1 214 ? 27.717 -25.922 92.976  1.00 33.32  ? 229 TRP C CD1 1 
ATOM   5585 C CD2 . TRP C  1 214 ? 29.030 -24.461 94.054  1.00 33.59  ? 229 TRP C CD2 1 
ATOM   5586 N NE1 . TRP C  1 214 ? 28.334 -26.595 93.993  1.00 33.78  ? 229 TRP C NE1 1 
ATOM   5587 C CE2 . TRP C  1 214 ? 29.142 -25.723 94.678  1.00 33.47  ? 229 TRP C CE2 1 
ATOM   5588 C CE3 . TRP C  1 214 ? 29.766 -23.382 94.563  1.00 35.08  ? 229 TRP C CE3 1 
ATOM   5589 C CZ2 . TRP C  1 214 ? 29.956 -25.927 95.793  1.00 33.37  ? 229 TRP C CZ2 1 
ATOM   5590 C CZ3 . TRP C  1 214 ? 30.571 -23.587 95.662  1.00 36.65  ? 229 TRP C CZ3 1 
ATOM   5591 C CH2 . TRP C  1 214 ? 30.668 -24.845 96.264  1.00 35.68  ? 229 TRP C CH2 1 
ATOM   5592 N N   . GLY C  1 215 ? 30.248 -22.241 91.298  1.00 33.32  ? 230 GLY C N   1 
ATOM   5593 C CA  . GLY C  1 215 ? 31.638 -21.940 91.662  1.00 33.89  ? 230 GLY C CA  1 
ATOM   5594 C C   . GLY C  1 215 ? 31.711 -20.554 92.249  1.00 35.64  ? 230 GLY C C   1 
ATOM   5595 O O   . GLY C  1 215 ? 30.700 -19.834 92.167  1.00 40.54  ? 230 GLY C O   1 
ATOM   5596 N N   . GLU C  1 216 ? 32.840 -20.202 92.853  1.00 37.38  ? 231 GLU C N   1 
ATOM   5597 C CA  . GLU C  1 216 ? 33.093 -18.820 93.326  1.00 39.73  ? 231 GLU C CA  1 
ATOM   5598 C C   . GLU C  1 216 ? 33.701 -18.046 92.156  1.00 39.29  ? 231 GLU C C   1 
ATOM   5599 O O   . GLU C  1 216 ? 34.901 -18.222 91.885  1.00 40.45  ? 231 GLU C O   1 
ATOM   5600 C CB  . GLU C  1 216 ? 33.980 -18.829 94.559  1.00 43.01  ? 231 GLU C CB  1 
ATOM   5601 C CG  . GLU C  1 216 ? 34.140 -17.455 95.166  1.00 46.92  ? 231 GLU C CG  1 
ATOM   5602 C CD  . GLU C  1 216 ? 35.274 -17.440 96.162  1.00 50.23  ? 231 GLU C CD  1 
ATOM   5603 O OE1 . GLU C  1 216 ? 36.187 -16.607 96.004  1.00 53.98  ? 231 GLU C OE1 1 
ATOM   5604 O OE2 . GLU C  1 216 ? 35.250 -18.299 97.069  1.00 51.24  ? 231 GLU C OE2 1 
ATOM   5605 N N   . GLY C  1 217 ? 32.870 -17.279 91.452  1.00 39.06  ? 232 GLY C N   1 
ATOM   5606 C CA  . GLY C  1 217 ? 33.243 -16.602 90.204  1.00 41.33  ? 232 GLY C CA  1 
ATOM   5607 C C   . GLY C  1 217 ? 33.698 -17.600 89.154  1.00 43.87  ? 232 GLY C C   1 
ATOM   5608 O O   . GLY C  1 217 ? 33.284 -18.786 89.216  1.00 40.06  ? 232 GLY C O   1 
ATOM   5609 N N   . CYS C  1 218 ? 34.511 -17.130 88.212  1.00 42.75  ? 233 CYS C N   1 
ATOM   5610 C CA  . CYS C  1 218 ? 34.979 -17.896 87.028  1.00 43.66  ? 233 CYS C CA  1 
ATOM   5611 C C   . CYS C  1 218 ? 36.500 -17.764 86.961  1.00 42.45  ? 233 CYS C C   1 
ATOM   5612 O O   . CYS C  1 218 ? 36.990 -16.628 87.039  1.00 41.60  ? 233 CYS C O   1 
ATOM   5613 C CB  . CYS C  1 218 ? 34.300 -17.397 85.756  1.00 45.55  ? 233 CYS C CB  1 
ATOM   5614 S SG  . CYS C  1 218 ? 32.508 -17.171 85.962  1.00 52.36  ? 233 CYS C SG  1 
ATOM   5615 N N   . ALA C  1 219 ? 37.198 -18.898 86.920  1.00 42.55  ? 234 ALA C N   1 
ATOM   5616 C CA  . ALA C  1 219 ? 38.667 -19.014 86.777  1.00 43.40  ? 234 ALA C CA  1 
ATOM   5617 C C   . ALA C  1 219 ? 39.387 -18.203 87.866  1.00 42.19  ? 234 ALA C C   1 
ATOM   5618 O O   . ALA C  1 219 ? 40.432 -17.618 87.566  1.00 41.46  ? 234 ALA C O   1 
ATOM   5619 C CB  . ALA C  1 219 ? 39.055 -18.580 85.382  1.00 42.61  ? 234 ALA C CB  1 
ATOM   5620 N N   . GLN C  1 220 ? 38.862 -18.197 89.099  1.00 43.39  ? 235 GLN C N   1 
ATOM   5621 C CA  . GLN C  1 220 ? 39.502 -17.576 90.295  1.00 42.52  ? 235 GLN C CA  1 
ATOM   5622 C C   . GLN C  1 220 ? 40.483 -18.581 90.907  1.00 40.44  ? 235 GLN C C   1 
ATOM   5623 O O   . GLN C  1 220 ? 40.232 -19.784 90.851  1.00 37.08  ? 235 GLN C O   1 
ATOM   5624 C CB  . GLN C  1 220 ? 38.457 -17.152 91.330  1.00 44.50  ? 235 GLN C CB  1 
ATOM   5625 C CG  . GLN C  1 220 ? 37.451 -16.123 90.828  1.00 49.13  ? 235 GLN C CG  1 
ATOM   5626 C CD  . GLN C  1 220 ? 38.074 -14.769 90.588  1.00 55.34  ? 235 GLN C CD  1 
ATOM   5627 O OE1 . GLN C  1 220 ? 38.798 -14.552 89.617  1.00 61.52  ? 235 GLN C OE1 1 
ATOM   5628 N NE2 . GLN C  1 220 ? 37.788 -13.829 91.473  1.00 59.85  ? 235 GLN C NE2 1 
ATOM   5629 N N   . PRO C  1 221 ? 41.625 -18.131 91.482  1.00 38.59  ? 236 PRO C N   1 
ATOM   5630 C CA  . PRO C  1 221 ? 42.576 -19.032 92.139  1.00 40.51  ? 236 PRO C CA  1 
ATOM   5631 C C   . PRO C  1 221 ? 41.938 -19.922 93.216  1.00 38.54  ? 236 PRO C C   1 
ATOM   5632 O O   . PRO C  1 221 ? 41.206 -19.408 94.033  1.00 37.86  ? 236 PRO C O   1 
ATOM   5633 C CB  . PRO C  1 221 ? 43.603 -18.084 92.788  1.00 39.47  ? 236 PRO C CB  1 
ATOM   5634 C CG  . PRO C  1 221 ? 43.531 -16.830 91.949  1.00 39.97  ? 236 PRO C CG  1 
ATOM   5635 C CD  . PRO C  1 221 ? 42.083 -16.731 91.516  1.00 40.31  ? 236 PRO C CD  1 
ATOM   5636 N N   . ASN C  1 222 ? 42.197 -21.231 93.152  1.00 37.66  ? 237 ASN C N   1 
ATOM   5637 C CA  . ASN C  1 222 ? 41.756 -22.250 94.143  1.00 37.75  ? 237 ASN C CA  1 
ATOM   5638 C C   . ASN C  1 222 ? 40.222 -22.354 94.172  1.00 36.28  ? 237 ASN C C   1 
ATOM   5639 O O   . ASN C  1 222 ? 39.686 -22.787 95.207  1.00 34.24  ? 237 ASN C O   1 
ATOM   5640 C CB  . ASN C  1 222 ? 42.323 -21.953 95.537  1.00 38.83  ? 237 ASN C CB  1 
ATOM   5641 C CG  . ASN C  1 222 ? 43.837 -21.983 95.552  1.00 40.60  ? 237 ASN C CG  1 
ATOM   5642 O OD1 . ASN C  1 222 ? 44.430 -22.925 95.042  1.00 45.85  ? 237 ASN C OD1 1 
ATOM   5643 N ND2 . ASN C  1 222 ? 44.465 -20.946 96.082  1.00 39.38  ? 237 ASN C ND2 1 
ATOM   5644 N N   . ARG C  1 223 ? 39.546 -21.993 93.079  1.00 34.67  ? 238 ARG C N   1 
ATOM   5645 C CA  . ARG C  1 223 ? 38.060 -22.029 92.972  1.00 36.20  ? 238 ARG C CA  1 
ATOM   5646 C C   . ARG C  1 223 ? 37.684 -22.629 91.623  1.00 34.05  ? 238 ARG C C   1 
ATOM   5647 O O   . ARG C  1 223 ? 37.129 -21.954 90.758  1.00 35.88  ? 238 ARG C O   1 
ATOM   5648 C CB  . ARG C  1 223 ? 37.473 -20.634 93.195  1.00 37.07  ? 238 ARG C CB  1 
ATOM   5649 C CG  . ARG C  1 223 ? 37.818 -20.013 94.542  1.00 37.44  ? 238 ARG C CG  1 
ATOM   5650 C CD  . ARG C  1 223 ? 37.195 -20.710 95.738  1.00 37.93  ? 238 ARG C CD  1 
ATOM   5651 N NE  . ARG C  1 223 ? 37.478 -19.963 96.963  1.00 37.58  ? 238 ARG C NE  1 
ATOM   5652 C CZ  . ARG C  1 223 ? 38.527 -20.135 97.778  1.00 37.38  ? 238 ARG C CZ  1 
ATOM   5653 N NH1 . ARG C  1 223 ? 39.440 -21.071 97.547  1.00 36.63  ? 238 ARG C NH1 1 
ATOM   5654 N NH2 . ARG C  1 223 ? 38.648 -19.357 98.845  1.00 35.84  ? 238 ARG C NH2 1 
ATOM   5655 N N   . PRO C  1 224 ? 37.975 -23.930 91.397  1.00 35.26  ? 239 PRO C N   1 
ATOM   5656 C CA  . PRO C  1 224 ? 37.575 -24.586 90.155  1.00 35.58  ? 239 PRO C CA  1 
ATOM   5657 C C   . PRO C  1 224 ? 36.048 -24.701 90.018  1.00 35.40  ? 239 PRO C C   1 
ATOM   5658 O O   . PRO C  1 224 ? 35.346 -24.625 91.021  1.00 35.51  ? 239 PRO C O   1 
ATOM   5659 C CB  . PRO C  1 224 ? 38.257 -25.958 90.211  1.00 36.39  ? 239 PRO C CB  1 
ATOM   5660 C CG  . PRO C  1 224 ? 38.527 -26.196 91.684  1.00 36.07  ? 239 PRO C CG  1 
ATOM   5661 C CD  . PRO C  1 224 ? 38.705 -24.830 92.306  1.00 34.77  ? 239 PRO C CD  1 
ATOM   5662 N N   . GLY C  1 225 ? 35.579 -24.854 88.775  1.00 33.34  ? 240 GLY C N   1 
ATOM   5663 C CA  . GLY C  1 225 ? 34.166 -25.105 88.446  1.00 33.00  ? 240 GLY C CA  1 
ATOM   5664 C C   . GLY C  1 225 ? 33.662 -26.352 89.148  1.00 33.81  ? 240 GLY C C   1 
ATOM   5665 O O   . GLY C  1 225 ? 34.407 -27.345 89.173  1.00 30.86  ? 240 GLY C O   1 
ATOM   5666 N N   . ILE C  1 226 ? 32.481 -26.267 89.767  1.00 34.43  ? 241 ILE C N   1 
ATOM   5667 C CA  . ILE C  1 226 ? 31.760 -27.418 90.380  1.00 34.38  ? 241 ILE C CA  1 
ATOM   5668 C C   . ILE C  1 226 ? 30.630 -27.812 89.430  1.00 33.42  ? 241 ILE C C   1 
ATOM   5669 O O   . ILE C  1 226 ? 29.930 -26.913 88.916  1.00 32.94  ? 241 ILE C O   1 
ATOM   5670 C CB  . ILE C  1 226 ? 31.211 -27.094 91.783  1.00 35.92  ? 241 ILE C CB  1 
ATOM   5671 C CG1 . ILE C  1 226 ? 32.202 -26.292 92.630  1.00 36.81  ? 241 ILE C CG1 1 
ATOM   5672 C CG2 . ILE C  1 226 ? 30.764 -28.374 92.485  1.00 35.40  ? 241 ILE C CG2 1 
ATOM   5673 C CD1 . ILE C  1 226 ? 33.522 -26.968 92.828  1.00 37.75  ? 241 ILE C CD1 1 
ATOM   5674 N N   . TYR C  1 227 ? 30.482 -29.115 89.218  1.00 31.62  ? 242 TYR C N   1 
ATOM   5675 C CA  . TYR C  1 227 ? 29.516 -29.749 88.296  1.00 32.96  ? 242 TYR C CA  1 
ATOM   5676 C C   . TYR C  1 227 ? 28.718 -30.782 89.085  1.00 33.24  ? 242 TYR C C   1 
ATOM   5677 O O   . TYR C  1 227 ? 29.283 -31.368 90.015  1.00 33.77  ? 242 TYR C O   1 
ATOM   5678 C CB  . TYR C  1 227 ? 30.268 -30.413 87.142  1.00 32.72  ? 242 TYR C CB  1 
ATOM   5679 C CG  . TYR C  1 227 ? 31.063 -29.469 86.281  1.00 33.48  ? 242 TYR C CG  1 
ATOM   5680 C CD1 . TYR C  1 227 ? 32.275 -28.944 86.712  1.00 34.18  ? 242 TYR C CD1 1 
ATOM   5681 C CD2 . TYR C  1 227 ? 30.601 -29.095 85.030  1.00 33.62  ? 242 TYR C CD2 1 
ATOM   5682 C CE1 . TYR C  1 227 ? 33.002 -28.067 85.922  1.00 35.96  ? 242 TYR C CE1 1 
ATOM   5683 C CE2 . TYR C  1 227 ? 31.331 -28.245 84.215  1.00 34.86  ? 242 TYR C CE2 1 
ATOM   5684 C CZ  . TYR C  1 227 ? 32.525 -27.714 84.669  1.00 34.86  ? 242 TYR C CZ  1 
ATOM   5685 O OH  . TYR C  1 227 ? 33.227 -26.872 83.864  1.00 35.92  ? 242 TYR C OH  1 
ATOM   5686 N N   . THR C  1 228 ? 27.449 -30.997 88.739  1.00 32.81  ? 243 THR C N   1 
ATOM   5687 C CA  . THR C  1 228 ? 26.683 -32.161 89.250  1.00 34.56  ? 243 THR C CA  1 
ATOM   5688 C C   . THR C  1 228 ? 27.309 -33.415 88.631  1.00 34.31  ? 243 THR C C   1 
ATOM   5689 O O   . THR C  1 228 ? 27.500 -33.413 87.407  1.00 36.54  ? 243 THR C O   1 
ATOM   5690 C CB  . THR C  1 228 ? 25.189 -32.036 88.951  1.00 33.74  ? 243 THR C CB  1 
ATOM   5691 O OG1 . THR C  1 228 ? 24.798 -30.741 89.402  1.00 33.54  ? 243 THR C OG1 1 
ATOM   5692 C CG2 . THR C  1 228 ? 24.367 -33.111 89.624  1.00 34.40  ? 243 THR C CG2 1 
ATOM   5693 N N   . ARG C  1 229 ? 27.651 -34.409 89.453  1.00 34.44  ? 244 ARG C N   1 
ATOM   5694 C CA  . ARG C  1 229 ? 28.214 -35.711 89.007  1.00 36.17  ? 244 ARG C CA  1 
ATOM   5695 C C   . ARG C  1 229 ? 27.078 -36.551 88.405  1.00 35.97  ? 244 ARG C C   1 
ATOM   5696 O O   . ARG C  1 229 ? 26.177 -36.940 89.161  1.00 36.80  ? 244 ARG C O   1 
ATOM   5697 C CB  . ARG C  1 229 ? 28.896 -36.401 90.190  1.00 38.80  ? 244 ARG C CB  1 
ATOM   5698 C CG  . ARG C  1 229 ? 29.632 -37.683 89.831  1.00 41.28  ? 244 ARG C CG  1 
ATOM   5699 C CD  . ARG C  1 229 ? 30.283 -38.322 91.042  1.00 41.98  ? 244 ARG C CD  1 
ATOM   5700 N NE  . ARG C  1 229 ? 31.454 -37.580 91.487  1.00 44.01  ? 244 ARG C NE  1 
ATOM   5701 C CZ  . ARG C  1 229 ? 32.660 -37.608 90.908  1.00 47.80  ? 244 ARG C CZ  1 
ATOM   5702 N NH1 . ARG C  1 229 ? 32.894 -38.344 89.831  1.00 49.95  ? 244 ARG C NH1 1 
ATOM   5703 N NH2 . ARG C  1 229 ? 33.644 -36.889 91.420  1.00 48.59  ? 244 ARG C NH2 1 
ATOM   5704 N N   . VAL C  1 230 ? 27.093 -36.784 87.088  1.00 35.62  ? 245 VAL C N   1 
ATOM   5705 C CA  . VAL C  1 230 ? 25.951 -37.436 86.371  1.00 36.95  ? 245 VAL C CA  1 
ATOM   5706 C C   . VAL C  1 230 ? 25.787 -38.877 86.878  1.00 36.35  ? 245 VAL C C   1 
ATOM   5707 O O   . VAL C  1 230 ? 24.630 -39.283 87.078  1.00 35.03  ? 245 VAL C O   1 
ATOM   5708 C CB  . VAL C  1 230 ? 26.093 -37.374 84.839  1.00 36.52  ? 245 VAL C CB  1 
ATOM   5709 C CG1 . VAL C  1 230 ? 25.049 -38.230 84.130  1.00 36.69  ? 245 VAL C CG1 1 
ATOM   5710 C CG2 . VAL C  1 230 ? 26.027 -35.935 84.343  1.00 37.67  ? 245 VAL C CG2 1 
ATOM   5711 N N   . THR C  1 231 ? 26.882 -39.609 87.106  1.00 36.01  ? 246 THR C N   1 
ATOM   5712 C CA  . THR C  1 231 ? 26.836 -41.034 87.552  1.00 37.46  ? 246 THR C CA  1 
ATOM   5713 C C   . THR C  1 231 ? 26.033 -41.146 88.854  1.00 38.64  ? 246 THR C C   1 
ATOM   5714 O O   . THR C  1 231 ? 25.318 -42.150 89.015  1.00 40.01  ? 246 THR C O   1 
ATOM   5715 C CB  . THR C  1 231 ? 28.227 -41.655 87.722  1.00 35.77  ? 246 THR C CB  1 
ATOM   5716 O OG1 . THR C  1 231 ? 29.012 -40.836 88.586  1.00 36.00  ? 246 THR C OG1 1 
ATOM   5717 C CG2 . THR C  1 231 ? 28.950 -41.833 86.405  1.00 37.30  ? 246 THR C CG2 1 
ATOM   5718 N N   . TYR C  1 232 ? 26.113 -40.133 89.724  1.00 39.37  ? 247 TYR C N   1 
ATOM   5719 C CA  . TYR C  1 232 ? 25.407 -40.079 91.032  1.00 37.32  ? 247 TYR C CA  1 
ATOM   5720 C C   . TYR C  1 232 ? 23.887 -40.149 90.834  1.00 35.50  ? 247 TYR C C   1 
ATOM   5721 O O   . TYR C  1 232 ? 23.230 -40.761 91.701  1.00 33.86  ? 247 TYR C O   1 
ATOM   5722 C CB  . TYR C  1 232 ? 25.808 -38.838 91.839  1.00 36.26  ? 247 TYR C CB  1 
ATOM   5723 C CG  . TYR C  1 232 ? 25.439 -38.913 93.296  1.00 35.12  ? 247 TYR C CG  1 
ATOM   5724 C CD1 . TYR C  1 232 ? 24.154 -38.611 93.722  1.00 36.98  ? 247 TYR C CD1 1 
ATOM   5725 C CD2 . TYR C  1 232 ? 26.359 -39.325 94.247  1.00 35.45  ? 247 TYR C CD2 1 
ATOM   5726 C CE1 . TYR C  1 232 ? 23.792 -38.706 95.054  1.00 36.53  ? 247 TYR C CE1 1 
ATOM   5727 C CE2 . TYR C  1 232 ? 26.017 -39.420 95.586  1.00 36.17  ? 247 TYR C CE2 1 
ATOM   5728 C CZ  . TYR C  1 232 ? 24.729 -39.107 95.989  1.00 37.09  ? 247 TYR C CZ  1 
ATOM   5729 O OH  . TYR C  1 232 ? 24.368 -39.202 97.297  1.00 37.75  ? 247 TYR C OH  1 
ATOM   5730 N N   . TYR C  1 233 ? 23.354 -39.563 89.755  1.00 36.48  ? 248 TYR C N   1 
ATOM   5731 C CA  . TYR C  1 233 ? 21.893 -39.391 89.538  1.00 35.50  ? 248 TYR C CA  1 
ATOM   5732 C C   . TYR C  1 233 ? 21.384 -40.224 88.346  1.00 36.83  ? 248 TYR C C   1 
ATOM   5733 O O   . TYR C  1 233 ? 20.245 -39.965 87.928  1.00 36.29  ? 248 TYR C O   1 
ATOM   5734 C CB  . TYR C  1 233 ? 21.587 -37.895 89.417  1.00 35.29  ? 248 TYR C CB  1 
ATOM   5735 C CG  . TYR C  1 233 ? 21.804 -37.156 90.710  1.00 34.07  ? 248 TYR C CG  1 
ATOM   5736 C CD1 . TYR C  1 233 ? 20.952 -37.350 91.788  1.00 35.42  ? 248 TYR C CD1 1 
ATOM   5737 C CD2 . TYR C  1 233 ? 22.888 -36.310 90.883  1.00 34.13  ? 248 TYR C CD2 1 
ATOM   5738 C CE1 . TYR C  1 233 ? 21.153 -36.700 92.995  1.00 33.57  ? 248 TYR C CE1 1 
ATOM   5739 C CE2 . TYR C  1 233 ? 23.097 -35.643 92.082  1.00 33.68  ? 248 TYR C CE2 1 
ATOM   5740 C CZ  . TYR C  1 233 ? 22.232 -35.846 93.146  1.00 33.76  ? 248 TYR C CZ  1 
ATOM   5741 O OH  . TYR C  1 233 ? 22.433 -35.222 94.344  1.00 34.06  ? 248 TYR C OH  1 
ATOM   5742 N N   . LEU C  1 234 ? 22.131 -41.234 87.868  1.00 39.64  ? 249 LEU C N   1 
ATOM   5743 C CA  . LEU C  1 234 ? 21.717 -42.095 86.715  1.00 40.76  ? 249 LEU C CA  1 
ATOM   5744 C C   . LEU C  1 234 ? 20.369 -42.763 86.994  1.00 41.81  ? 249 LEU C C   1 
ATOM   5745 O O   . LEU C  1 234 ? 19.516 -42.726 86.087  1.00 45.05  ? 249 LEU C O   1 
ATOM   5746 C CB  . LEU C  1 234 ? 22.775 -43.162 86.427  1.00 42.87  ? 249 LEU C CB  1 
ATOM   5747 C CG  . LEU C  1 234 ? 23.978 -42.679 85.628  1.00 45.04  ? 249 LEU C CG  1 
ATOM   5748 C CD1 . LEU C  1 234 ? 25.101 -43.690 85.726  1.00 45.07  ? 249 LEU C CD1 1 
ATOM   5749 C CD2 . LEU C  1 234 ? 23.612 -42.420 84.172  1.00 45.16  ? 249 LEU C CD2 1 
ATOM   5750 N N   . ASP C  1 235 ? 20.177 -43.341 88.187  1.00 42.10  ? 250 ASP C N   1 
ATOM   5751 C CA  . ASP C  1 235 ? 18.918 -44.037 88.568  1.00 42.50  ? 250 ASP C CA  1 
ATOM   5752 C C   . ASP C  1 235 ? 17.742 -43.060 88.497  1.00 42.54  ? 250 ASP C C   1 
ATOM   5753 O O   . ASP C  1 235 ? 16.679 -43.472 88.007  1.00 44.81  ? 250 ASP C O   1 
ATOM   5754 C CB  . ASP C  1 235 ? 18.998 -44.654 89.966  1.00 44.36  ? 250 ASP C CB  1 
ATOM   5755 C CG  . ASP C  1 235 ? 19.930 -45.848 90.073  1.00 47.23  ? 250 ASP C CG  1 
ATOM   5756 O OD1 . ASP C  1 235 ? 20.399 -46.336 89.033  1.00 52.06  ? 250 ASP C OD1 1 
ATOM   5757 O OD2 . ASP C  1 235 ? 20.177 -46.285 91.212  1.00 55.57  ? 250 ASP C OD2 1 
ATOM   5758 N N   . TRP C  1 236 ? 17.922 -41.828 88.979  1.00 39.26  ? 251 TRP C N   1 
ATOM   5759 C CA  . TRP C  1 236 ? 16.879 -40.766 88.935  1.00 38.01  ? 251 TRP C CA  1 
ATOM   5760 C C   . TRP C  1 236 ? 16.584 -40.388 87.478  1.00 36.02  ? 251 TRP C C   1 
ATOM   5761 O O   . TRP C  1 236 ? 15.405 -40.306 87.132  1.00 34.77  ? 251 TRP C O   1 
ATOM   5762 C CB  . TRP C  1 236 ? 17.284 -39.545 89.775  1.00 35.86  ? 251 TRP C CB  1 
ATOM   5763 C CG  . TRP C  1 236 ? 16.270 -38.447 89.744  1.00 34.67  ? 251 TRP C CG  1 
ATOM   5764 C CD1 . TRP C  1 236 ? 15.146 -38.346 90.505  1.00 34.72  ? 251 TRP C CD1 1 
ATOM   5765 C CD2 . TRP C  1 236 ? 16.272 -37.297 88.878  1.00 34.56  ? 251 TRP C CD2 1 
ATOM   5766 N NE1 . TRP C  1 236 ? 14.453 -37.214 90.174  1.00 35.05  ? 251 TRP C NE1 1 
ATOM   5767 C CE2 . TRP C  1 236 ? 15.120 -36.548 89.186  1.00 32.65  ? 251 TRP C CE2 1 
ATOM   5768 C CE3 . TRP C  1 236 ? 17.138 -36.822 87.884  1.00 32.63  ? 251 TRP C CE3 1 
ATOM   5769 C CZ2 . TRP C  1 236 ? 14.812 -35.350 88.541  1.00 33.96  ? 251 TRP C CZ2 1 
ATOM   5770 C CZ3 . TRP C  1 236 ? 16.832 -35.641 87.246  1.00 32.87  ? 251 TRP C CZ3 1 
ATOM   5771 C CH2 . TRP C  1 236 ? 15.686 -34.913 87.573  1.00 32.69  ? 251 TRP C CH2 1 
ATOM   5772 N N   . ILE C  1 237 ? 17.615 -40.195 86.652  1.00 38.18  ? 252 ILE C N   1 
ATOM   5773 C CA  . ILE C  1 237 ? 17.452 -39.870 85.201  1.00 41.14  ? 252 ILE C CA  1 
ATOM   5774 C C   . ILE C  1 237 ? 16.665 -41.007 84.527  1.00 42.81  ? 252 ILE C C   1 
ATOM   5775 O O   . ILE C  1 237 ? 15.662 -40.709 83.840  1.00 42.55  ? 252 ILE C O   1 
ATOM   5776 C CB  . ILE C  1 237 ? 18.813 -39.616 84.516  1.00 40.47  ? 252 ILE C CB  1 
ATOM   5777 C CG1 . ILE C  1 237 ? 19.495 -38.354 85.049  1.00 39.52  ? 252 ILE C CG1 1 
ATOM   5778 C CG2 . ILE C  1 237 ? 18.656 -39.560 82.998  1.00 40.42  ? 252 ILE C CG2 1 
ATOM   5779 C CD1 . ILE C  1 237 ? 20.960 -38.256 84.692  1.00 39.68  ? 252 ILE C CD1 1 
ATOM   5780 N N   . HIS C  1 238 ? 17.085 -42.258 84.741  1.00 42.95  ? 253 HIS C N   1 
ATOM   5781 C CA  . HIS C  1 238 ? 16.508 -43.474 84.094  1.00 44.70  ? 253 HIS C CA  1 
ATOM   5782 C C   . HIS C  1 238 ? 15.103 -43.775 84.621  1.00 42.92  ? 253 HIS C C   1 
ATOM   5783 O O   . HIS C  1 238 ? 14.406 -44.566 83.977  1.00 46.71  ? 253 HIS C O   1 
ATOM   5784 C CB  . HIS C  1 238 ? 17.438 -44.683 84.253  1.00 44.10  ? 253 HIS C CB  1 
ATOM   5785 C CG  . HIS C  1 238 ? 18.705 -44.544 83.484  1.00 46.17  ? 253 HIS C CG  1 
ATOM   5786 N ND1 . HIS C  1 238 ? 18.742 -43.952 82.237  1.00 48.69  ? 253 HIS C ND1 1 
ATOM   5787 C CD2 . HIS C  1 238 ? 19.970 -44.924 83.766  1.00 47.69  ? 253 HIS C CD2 1 
ATOM   5788 C CE1 . HIS C  1 238 ? 19.980 -43.973 81.783  1.00 48.64  ? 253 HIS C CE1 1 
ATOM   5789 N NE2 . HIS C  1 238 ? 20.753 -44.560 82.705  1.00 47.09  ? 253 HIS C NE2 1 
ATOM   5790 N N   . HIS C  1 239 ? 14.687 -43.164 85.731  1.00 44.60  ? 254 HIS C N   1 
ATOM   5791 C CA  . HIS C  1 239 ? 13.292 -43.234 86.232  1.00 44.84  ? 254 HIS C CA  1 
ATOM   5792 C C   . HIS C  1 239 ? 12.335 -42.551 85.246  1.00 45.76  ? 254 HIS C C   1 
ATOM   5793 O O   . HIS C  1 239 ? 11.162 -42.967 85.193  1.00 48.39  ? 254 HIS C O   1 
ATOM   5794 C CB  . HIS C  1 239 ? 13.200 -42.630 87.635  1.00 46.18  ? 254 HIS C CB  1 
ATOM   5795 C CG  . HIS C  1 239 ? 11.868 -42.822 88.272  1.00 47.99  ? 254 HIS C CG  1 
ATOM   5796 N ND1 . HIS C  1 239 ? 11.584 -43.895 89.096  1.00 49.91  ? 254 HIS C ND1 1 
ATOM   5797 C CD2 . HIS C  1 239 ? 10.738 -42.092 88.192  1.00 49.86  ? 254 HIS C CD2 1 
ATOM   5798 C CE1 . HIS C  1 239 ? 10.336 -43.807 89.508  1.00 48.92  ? 254 HIS C CE1 1 
ATOM   5799 N NE2 . HIS C  1 239 ? 9.795  -42.711 88.965  1.00 50.12  ? 254 HIS C NE2 1 
ATOM   5800 N N   . TYR C  1 240 ? 12.805 -41.548 84.492  1.00 44.63  ? 255 TYR C N   1 
ATOM   5801 C CA  . TYR C  1 240 ? 11.982 -40.722 83.568  1.00 42.96  ? 255 TYR C CA  1 
ATOM   5802 C C   . TYR C  1 240 ? 12.375 -40.944 82.102  1.00 42.37  ? 255 TYR C C   1 
ATOM   5803 O O   . TYR C  1 240 ? 11.473 -40.989 81.257  1.00 44.18  ? 255 TYR C O   1 
ATOM   5804 C CB  . TYR C  1 240 ? 12.105 -39.246 83.948  1.00 42.87  ? 255 TYR C CB  1 
ATOM   5805 C CG  . TYR C  1 240 ? 11.622 -38.948 85.343  1.00 39.24  ? 255 TYR C CG  1 
ATOM   5806 C CD1 . TYR C  1 240 ? 10.267 -38.928 85.632  1.00 39.05  ? 255 TYR C CD1 1 
ATOM   5807 C CD2 . TYR C  1 240 ? 12.515 -38.736 86.383  1.00 39.49  ? 255 TYR C CD2 1 
ATOM   5808 C CE1 . TYR C  1 240 ? 9.808  -38.684 86.913  1.00 40.14  ? 255 TYR C CE1 1 
ATOM   5809 C CE2 . TYR C  1 240 ? 12.074 -38.485 87.673  1.00 38.77  ? 255 TYR C CE2 1 
ATOM   5810 C CZ  . TYR C  1 240 ? 10.716 -38.451 87.935  1.00 39.61  ? 255 TYR C CZ  1 
ATOM   5811 O OH  . TYR C  1 240 ? 10.264 -38.209 89.194  1.00 43.08  ? 255 TYR C OH  1 
ATOM   5812 N N   . VAL C  1 241 ? 13.669 -41.051 81.804  1.00 44.67  ? 256 VAL C N   1 
ATOM   5813 C CA  . VAL C  1 241 ? 14.223 -41.078 80.417  1.00 45.93  ? 256 VAL C CA  1 
ATOM   5814 C C   . VAL C  1 241 ? 14.373 -42.532 79.980  1.00 48.77  ? 256 VAL C C   1 
ATOM   5815 O O   . VAL C  1 241 ? 15.090 -43.287 80.630  1.00 48.53  ? 256 VAL C O   1 
ATOM   5816 C CB  . VAL C  1 241 ? 15.569 -40.333 80.333  1.00 44.93  ? 256 VAL C CB  1 
ATOM   5817 C CG1 . VAL C  1 241 ? 16.151 -40.326 78.924  1.00 44.47  ? 256 VAL C CG1 1 
ATOM   5818 C CG2 . VAL C  1 241 ? 15.438 -38.910 80.854  1.00 45.57  ? 256 VAL C CG2 1 
ATOM   5819 N N   . PRO C  1 242 ? 13.720 -42.965 78.872  1.00 53.75  ? 257 PRO C N   1 
ATOM   5820 C CA  . PRO C  1 242 ? 13.930 -44.310 78.331  1.00 56.13  ? 257 PRO C CA  1 
ATOM   5821 C C   . PRO C  1 242 ? 15.393 -44.606 77.963  1.00 59.51  ? 257 PRO C C   1 
ATOM   5822 O O   . PRO C  1 242 ? 16.072 -43.702 77.493  1.00 61.19  ? 257 PRO C O   1 
ATOM   5823 C CB  . PRO C  1 242 ? 13.060 -44.340 77.063  1.00 55.41  ? 257 PRO C CB  1 
ATOM   5824 C CG  . PRO C  1 242 ? 12.010 -43.276 77.303  1.00 56.71  ? 257 PRO C CG  1 
ATOM   5825 C CD  . PRO C  1 242 ? 12.728 -42.203 78.095  1.00 54.09  ? 257 PRO C CD  1 
ATOM   5826 N N   . LYS C  1 243 ? 15.824 -45.857 78.173  1.00 64.87  ? 258 LYS C N   1 
ATOM   5827 C CA  . LYS C  1 243 ? 17.145 -46.400 77.745  1.00 68.62  ? 258 LYS C CA  1 
ATOM   5828 C C   . LYS C  1 243 ? 17.058 -46.828 76.275  1.00 68.73  ? 258 LYS C C   1 
ATOM   5829 O O   . LYS C  1 243 ? 17.570 -46.140 75.388  1.00 72.46  ? 258 LYS C O   1 
ATOM   5830 C CB  . LYS C  1 243 ? 17.556 -47.586 78.624  1.00 69.82  ? 258 LYS C CB  1 
ATOM   5831 C CG  . LYS C  1 243 ? 17.783 -47.301 80.078  0.00 71.11  ? 258 LYS C CG  1 
ATOM   5832 C CD  . LYS C  1 243 ? 18.163 -48.528 80.881  0.00 71.13  ? 258 LYS C CD  1 
ATOM   5833 C CE  . LYS C  1 243 ? 18.435 -48.226 82.339  0.00 71.05  ? 258 LYS C CE  1 
ATOM   5834 N NZ  . LYS C  1 243 ? 18.779 -49.452 83.096  0.00 71.02  ? 258 LYS C NZ  1 
ATOM   5835 N N   . ILE D  1 1   ? 14.931 2.376   65.625  1.00 34.72  ? 16  ILE D N   1 
ATOM   5836 C CA  . ILE D  1 1   ? 13.714 2.750   64.842  1.00 34.25  ? 16  ILE D CA  1 
ATOM   5837 C C   . ILE D  1 1   ? 12.467 2.413   65.674  1.00 34.32  ? 16  ILE D C   1 
ATOM   5838 O O   . ILE D  1 1   ? 12.344 1.254   66.121  1.00 32.49  ? 16  ILE D O   1 
ATOM   5839 C CB  . ILE D  1 1   ? 13.707 2.058   63.461  1.00 35.02  ? 16  ILE D CB  1 
ATOM   5840 C CG1 . ILE D  1 1   ? 14.903 2.470   62.590  1.00 36.05  ? 16  ILE D CG1 1 
ATOM   5841 C CG2 . ILE D  1 1   ? 12.392 2.281   62.730  1.00 34.84  ? 16  ILE D CG2 1 
ATOM   5842 C CD1 . ILE D  1 1   ? 14.908 3.922   62.149  1.00 35.60  ? 16  ILE D CD1 1 
ATOM   5843 N N   . VAL D  1 2   ? 11.573 3.390   65.850  1.00 35.04  ? 17  VAL D N   1 
ATOM   5844 C CA  . VAL D  1 2   ? 10.296 3.248   66.607  1.00 35.79  ? 17  VAL D CA  1 
ATOM   5845 C C   . VAL D  1 2   ? 9.164  3.025   65.600  1.00 36.40  ? 17  VAL D C   1 
ATOM   5846 O O   . VAL D  1 2   ? 9.063  3.815   64.637  1.00 37.07  ? 17  VAL D O   1 
ATOM   5847 C CB  . VAL D  1 2   ? 10.019 4.476   67.493  1.00 36.44  ? 17  VAL D CB  1 
ATOM   5848 C CG1 . VAL D  1 2   ? 8.764  4.289   68.331  1.00 36.68  ? 17  VAL D CG1 1 
ATOM   5849 C CG2 . VAL D  1 2   ? 11.206 4.828   68.378  1.00 36.87  ? 17  VAL D CG2 1 
ATOM   5850 N N   . GLY D  1 3   ? 8.332  2.009   65.846  1.00 37.81  ? 18  GLY D N   1 
ATOM   5851 C CA  . GLY D  1 3   ? 7.115  1.698   65.072  1.00 37.83  ? 18  GLY D CA  1 
ATOM   5852 C C   . GLY D  1 3   ? 7.430  1.176   63.688  1.00 40.59  ? 18  GLY D C   1 
ATOM   5853 O O   . GLY D  1 3   ? 6.562  1.301   62.804  1.00 48.04  ? 18  GLY D O   1 
ATOM   5854 N N   . GLY D  1 4   ? 8.620  0.611   63.495  1.00 40.76  ? 19  GLY D N   1 
ATOM   5855 C CA  . GLY D  1 4   ? 9.082  0.157   62.174  1.00 45.79  ? 19  GLY D CA  1 
ATOM   5856 C C   . GLY D  1 4   ? 8.690  -1.281  61.873  1.00 46.63  ? 19  GLY D C   1 
ATOM   5857 O O   . GLY D  1 4   ? 7.903  -1.868  62.638  1.00 49.90  ? 19  GLY D O   1 
ATOM   5858 N N   . GLN D  1 5   ? 9.248  -1.816  60.793  1.00 42.25  ? 20  GLN D N   1 
ATOM   5859 C CA  . GLN D  1 5   ? 9.286  -3.265  60.477  1.00 43.13  ? 20  GLN D CA  1 
ATOM   5860 C C   . GLN D  1 5   ? 10.736 -3.609  60.130  1.00 41.52  ? 20  GLN D C   1 
ATOM   5861 O O   . GLN D  1 5   ? 11.521 -2.667  59.841  1.00 38.53  ? 20  GLN D O   1 
ATOM   5862 C CB  . GLN D  1 5   ? 8.366  -3.596  59.302  1.00 46.85  ? 20  GLN D CB  1 
ATOM   5863 C CG  . GLN D  1 5   ? 6.904  -3.197  59.491  1.00 50.24  ? 20  GLN D CG  1 
ATOM   5864 C CD  . GLN D  1 5   ? 6.028  -3.574  58.320  0.00 49.13  ? 20  GLN D CD  1 
ATOM   5865 O OE1 . GLN D  1 5   ? 6.492  -3.729  57.192  0.00 49.32  ? 20  GLN D OE1 1 
ATOM   5866 N NE2 . GLN D  1 5   ? 4.738  -3.717  58.578  0.00 49.22  ? 20  GLN D NE2 1 
ATOM   5867 N N   . GLU D  1 6   ? 11.081 -4.894  60.151  1.00 38.99  ? 21  GLU D N   1 
ATOM   5868 C CA  . GLU D  1 6   ? 12.372 -5.391  59.607  1.00 41.56  ? 21  GLU D CA  1 
ATOM   5869 C C   . GLU D  1 6   ? 12.402 -5.044  58.114  1.00 38.35  ? 21  GLU D C   1 
ATOM   5870 O O   . GLU D  1 6   ? 11.387 -5.282  57.438  1.00 40.74  ? 21  GLU D O   1 
ATOM   5871 C CB  . GLU D  1 6   ? 12.536 -6.891  59.866  1.00 42.10  ? 21  GLU D CB  1 
ATOM   5872 C CG  . GLU D  1 6   ? 13.763 -7.502  59.200  1.00 45.92  ? 21  GLU D CG  1 
ATOM   5873 C CD  . GLU D  1 6   ? 14.173 -8.881  59.697  1.00 47.23  ? 21  GLU D CD  1 
ATOM   5874 O OE1 . GLU D  1 6   ? 13.472 -9.430  60.583  1.00 44.32  ? 21  GLU D OE1 1 
ATOM   5875 O OE2 . GLU D  1 6   ? 15.201 -9.404  59.197  1.00 48.15  ? 21  GLU D OE2 1 
ATOM   5876 N N   . ALA D  1 7   ? 13.507 -4.477  57.640  1.00 36.83  ? 22  ALA D N   1 
ATOM   5877 C CA  . ALA D  1 7   ? 13.717 -4.127  56.216  1.00 37.06  ? 22  ALA D CA  1 
ATOM   5878 C C   . ALA D  1 7   ? 13.841 -5.417  55.410  1.00 36.86  ? 22  ALA D C   1 
ATOM   5879 O O   . ALA D  1 7   ? 14.516 -6.341  55.854  1.00 36.25  ? 22  ALA D O   1 
ATOM   5880 C CB  . ALA D  1 7   ? 14.948 -3.270  56.056  1.00 37.60  ? 22  ALA D CB  1 
ATOM   5881 N N   . PRO D  1 8   ? 13.192 -5.541  54.231  1.00 38.90  ? 23  PRO D N   1 
ATOM   5882 C CA  . PRO D  1 8   ? 13.518 -6.623  53.300  1.00 37.58  ? 23  PRO D CA  1 
ATOM   5883 C C   . PRO D  1 8   ? 14.991 -6.529  52.862  1.00 38.97  ? 23  PRO D C   1 
ATOM   5884 O O   . PRO D  1 8   ? 15.513 -5.414  52.786  1.00 37.11  ? 23  PRO D O   1 
ATOM   5885 C CB  . PRO D  1 8   ? 12.560 -6.427  52.111  1.00 37.80  ? 23  PRO D CB  1 
ATOM   5886 C CG  . PRO D  1 8   ? 11.465 -5.506  52.634  1.00 38.59  ? 23  PRO D CG  1 
ATOM   5887 C CD  . PRO D  1 8   ? 12.110 -4.676  53.728  1.00 38.14  ? 23  PRO D CD  1 
ATOM   5888 N N   . ARG D  1 9   ? 15.606 -7.685  52.572  1.00 38.65  ? 24  ARG D N   1 
ATOM   5889 C CA  . ARG D  1 9   ? 17.034 -7.845  52.180  1.00 41.00  ? 24  ARG D CA  1 
ATOM   5890 C C   . ARG D  1 9   ? 17.398 -6.964  50.981  1.00 39.89  ? 24  ARG D C   1 
ATOM   5891 O O   . ARG D  1 9   ? 18.551 -6.523  50.923  1.00 44.49  ? 24  ARG D O   1 
ATOM   5892 C CB  . ARG D  1 9   ? 17.344 -9.309  51.864  1.00 44.19  ? 24  ARG D CB  1 
ATOM   5893 C CG  . ARG D  1 9   ? 17.321 -10.208 53.089  1.00 49.61  ? 24  ARG D CG  1 
ATOM   5894 C CD  . ARG D  1 9   ? 17.889 -11.594 52.831  1.00 53.79  ? 24  ARG D CD  1 
ATOM   5895 N NE  . ARG D  1 9   ? 18.367 -12.198 54.070  1.00 55.10  ? 24  ARG D NE  1 
ATOM   5896 C CZ  . ARG D  1 9   ? 19.574 -12.021 54.615  1.00 55.58  ? 24  ARG D CZ  1 
ATOM   5897 N NH1 . ARG D  1 9   ? 20.491 -11.254 54.042  1.00 55.46  ? 24  ARG D NH1 1 
ATOM   5898 N NH2 . ARG D  1 9   ? 19.864 -12.628 55.754  1.00 59.53  ? 24  ARG D NH2 1 
ATOM   5899 N N   . SER D  1 10  ? 16.461 -6.734  50.060  1.00 39.59  ? 25  SER D N   1 
ATOM   5900 C CA  . SER D  1 10  ? 16.653 -5.973  48.798  1.00 41.30  ? 25  SER D CA  1 
ATOM   5901 C C   . SER D  1 10  ? 16.680 -4.449  49.023  1.00 40.42  ? 25  SER D C   1 
ATOM   5902 O O   . SER D  1 10  ? 17.052 -3.735  48.061  1.00 42.87  ? 25  SER D O   1 
ATOM   5903 C CB  . SER D  1 10  ? 15.572 -6.346  47.808  1.00 40.92  ? 25  SER D CB  1 
ATOM   5904 O OG  . SER D  1 10  ? 14.282 -6.052  48.334  1.00 41.42  ? 25  SER D OG  1 
ATOM   5905 N N   . LYS D  1 11  ? 16.266 -3.950  50.195  1.00 41.34  ? 26  LYS D N   1 
ATOM   5906 C CA  . LYS D  1 11  ? 16.072 -2.491  50.433  1.00 38.16  ? 26  LYS D CA  1 
ATOM   5907 C C   . LYS D  1 11  ? 17.269 -1.891  51.168  1.00 35.20  ? 26  LYS D C   1 
ATOM   5908 O O   . LYS D  1 11  ? 17.891 -2.582  51.993  1.00 35.68  ? 26  LYS D O   1 
ATOM   5909 C CB  . LYS D  1 11  ? 14.778 -2.222  51.200  1.00 37.82  ? 26  LYS D CB  1 
ATOM   5910 C CG  . LYS D  1 11  ? 13.516 -2.811  50.585  1.00 40.86  ? 26  LYS D CG  1 
ATOM   5911 C CD  . LYS D  1 11  ? 13.345 -2.547  49.107  1.00 43.74  ? 26  LYS D CD  1 
ATOM   5912 C CE  . LYS D  1 11  ? 11.975 -2.962  48.586  0.00 42.55  ? 26  LYS D CE  1 
ATOM   5913 N NZ  . LYS D  1 11  ? 11.897 -2.861  47.110  0.00 42.60  ? 26  LYS D NZ  1 
ATOM   5914 N N   . TRP D  1 12  ? 17.530 -0.608  50.896  1.00 35.30  ? 27  TRP D N   1 
ATOM   5915 C CA  . TRP D  1 12  ? 18.500 0.271   51.601  1.00 32.77  ? 27  TRP D CA  1 
ATOM   5916 C C   . TRP D  1 12  ? 19.922 -0.266  51.456  1.00 31.90  ? 27  TRP D C   1 
ATOM   5917 O O   . TRP D  1 12  ? 20.597 -0.511  52.451  1.00 33.56  ? 27  TRP D O   1 
ATOM   5918 C CB  . TRP D  1 12  ? 18.094 0.446   53.070  1.00 33.57  ? 27  TRP D CB  1 
ATOM   5919 C CG  . TRP D  1 12  ? 16.616 0.413   53.313  1.00 32.38  ? 27  TRP D CG  1 
ATOM   5920 C CD1 . TRP D  1 12  ? 15.960 -0.454  54.128  1.00 32.44  ? 27  TRP D CD1 1 
ATOM   5921 C CD2 . TRP D  1 12  ? 15.607 1.259   52.730  1.00 34.56  ? 27  TRP D CD2 1 
ATOM   5922 N NE1 . TRP D  1 12  ? 14.619 -0.197  54.111  1.00 33.74  ? 27  TRP D NE1 1 
ATOM   5923 C CE2 . TRP D  1 12  ? 14.366 0.842   53.257  1.00 33.05  ? 27  TRP D CE2 1 
ATOM   5924 C CE3 . TRP D  1 12  ? 15.629 2.332   51.828  1.00 33.54  ? 27  TRP D CE3 1 
ATOM   5925 C CZ2 . TRP D  1 12  ? 13.164 1.470   52.924  1.00 33.65  ? 27  TRP D CZ2 1 
ATOM   5926 C CZ3 . TRP D  1 12  ? 14.440 2.939   51.482  1.00 35.18  ? 27  TRP D CZ3 1 
ATOM   5927 C CH2 . TRP D  1 12  ? 13.224 2.515   52.028  1.00 34.63  ? 27  TRP D CH2 1 
ATOM   5928 N N   . PRO D  1 13  ? 20.431 -0.446  50.219  1.00 31.37  ? 28  PRO D N   1 
ATOM   5929 C CA  . PRO D  1 13  ? 21.778 -0.994  50.011  1.00 32.17  ? 28  PRO D CA  1 
ATOM   5930 C C   . PRO D  1 13  ? 22.929 -0.042  50.392  1.00 32.41  ? 28  PRO D C   1 
ATOM   5931 O O   . PRO D  1 13  ? 24.063 -0.466  50.390  1.00 32.83  ? 28  PRO D O   1 
ATOM   5932 C CB  . PRO D  1 13  ? 21.770 -1.311  48.507  1.00 32.24  ? 28  PRO D CB  1 
ATOM   5933 C CG  . PRO D  1 13  ? 20.818 -0.290  47.913  1.00 32.34  ? 28  PRO D CG  1 
ATOM   5934 C CD  . PRO D  1 13  ? 19.741 -0.130  48.958  1.00 31.86  ? 28  PRO D CD  1 
ATOM   5935 N N   . TRP D  1 14  ? 22.598 1.196   50.766  1.00 31.70  ? 29  TRP D N   1 
ATOM   5936 C CA  . TRP D  1 14  ? 23.532 2.280   51.169  1.00 30.14  ? 29  TRP D CA  1 
ATOM   5937 C C   . TRP D  1 14  ? 23.697 2.358   52.692  1.00 30.90  ? 29  TRP D C   1 
ATOM   5938 O O   . TRP D  1 14  ? 24.628 3.061   53.120  1.00 30.29  ? 29  TRP D O   1 
ATOM   5939 C CB  . TRP D  1 14  ? 23.038 3.616   50.604  1.00 30.81  ? 29  TRP D CB  1 
ATOM   5940 C CG  . TRP D  1 14  ? 21.582 3.861   50.846  1.00 29.76  ? 29  TRP D CG  1 
ATOM   5941 C CD1 . TRP D  1 14  ? 20.979 4.172   52.029  1.00 30.89  ? 29  TRP D CD1 1 
ATOM   5942 C CD2 . TRP D  1 14  ? 20.533 3.775   49.869  1.00 30.91  ? 29  TRP D CD2 1 
ATOM   5943 N NE1 . TRP D  1 14  ? 19.627 4.294   51.853  1.00 31.37  ? 29  TRP D NE1 1 
ATOM   5944 C CE2 . TRP D  1 14  ? 19.324 4.071   50.538  1.00 31.49  ? 29  TRP D CE2 1 
ATOM   5945 C CE3 . TRP D  1 14  ? 20.496 3.492   48.498  1.00 31.24  ? 29  TRP D CE3 1 
ATOM   5946 C CZ2 . TRP D  1 14  ? 18.097 4.090   49.879  1.00 32.35  ? 29  TRP D CZ2 1 
ATOM   5947 C CZ3 . TRP D  1 14  ? 19.281 3.512   47.849  1.00 31.99  ? 29  TRP D CZ3 1 
ATOM   5948 C CH2 . TRP D  1 14  ? 18.098 3.797   48.536  1.00 31.75  ? 29  TRP D CH2 1 
ATOM   5949 N N   . GLN D  1 15  ? 22.837 1.694   53.477  1.00 32.09  ? 30  GLN D N   1 
ATOM   5950 C CA  . GLN D  1 15  ? 22.878 1.714   54.963  1.00 33.51  ? 30  GLN D CA  1 
ATOM   5951 C C   . GLN D  1 15  ? 24.216 1.131   55.421  1.00 33.96  ? 30  GLN D C   1 
ATOM   5952 O O   . GLN D  1 15  ? 24.588 0.058   54.914  1.00 36.11  ? 30  GLN D O   1 
ATOM   5953 C CB  . GLN D  1 15  ? 21.712 0.927   55.571  1.00 33.95  ? 30  GLN D CB  1 
ATOM   5954 C CG  . GLN D  1 15  ? 21.686 0.931   57.095  1.00 34.30  ? 30  GLN D CG  1 
ATOM   5955 C CD  . GLN D  1 15  ? 21.244 2.254   57.676  1.00 33.53  ? 30  GLN D CD  1 
ATOM   5956 O OE1 . GLN D  1 15  ? 20.175 2.758   57.352  1.00 36.54  ? 30  GLN D OE1 1 
ATOM   5957 N NE2 . GLN D  1 15  ? 22.067 2.834   58.534  1.00 33.89  ? 30  GLN D NE2 1 
ATOM   5958 N N   . VAL D  1 16  ? 24.919 1.839   56.307  1.00 32.58  ? 31  VAL D N   1 
ATOM   5959 C CA  . VAL D  1 16  ? 26.171 1.361   56.952  1.00 33.05  ? 31  VAL D CA  1 
ATOM   5960 C C   . VAL D  1 16  ? 26.022 1.495   58.469  1.00 32.39  ? 31  VAL D C   1 
ATOM   5961 O O   . VAL D  1 16  ? 25.179 2.287   58.941  1.00 32.04  ? 31  VAL D O   1 
ATOM   5962 C CB  . VAL D  1 16  ? 27.434 2.069   56.420  1.00 34.76  ? 31  VAL D CB  1 
ATOM   5963 C CG1 . VAL D  1 16  ? 27.414 2.206   54.910  1.00 35.64  ? 31  VAL D CG1 1 
ATOM   5964 C CG2 . VAL D  1 16  ? 27.691 3.415   57.064  1.00 35.90  ? 31  VAL D CG2 1 
ATOM   5965 N N   . SER D  1 17  ? 26.804 0.690   59.186  1.00 31.45  ? 32  SER D N   1 
ATOM   5966 C CA  . SER D  1 17  ? 26.931 0.672   60.658  1.00 30.26  ? 32  SER D CA  1 
ATOM   5967 C C   . SER D  1 17  ? 28.324 1.192   61.008  1.00 31.18  ? 32  SER D C   1 
ATOM   5968 O O   . SER D  1 17  ? 29.304 0.693   60.396  1.00 31.76  ? 32  SER D O   1 
ATOM   5969 C CB  . SER D  1 17  ? 26.678 -0.730  61.168  1.00 29.86  ? 32  SER D CB  1 
ATOM   5970 O OG  . SER D  1 17  ? 27.069 -0.861  62.521  1.00 30.38  ? 32  SER D OG  1 
ATOM   5971 N N   . LEU D  1 18  ? 28.413 2.184   61.904  1.00 31.53  ? 33  LEU D N   1 
ATOM   5972 C CA  . LEU D  1 18  ? 29.708 2.674   62.450  1.00 31.56  ? 33  LEU D CA  1 
ATOM   5973 C C   . LEU D  1 18  ? 30.022 1.884   63.722  1.00 31.63  ? 33  LEU D C   1 
ATOM   5974 O O   . LEU D  1 18  ? 29.106 1.725   64.550  1.00 31.26  ? 33  LEU D O   1 
ATOM   5975 C CB  . LEU D  1 18  ? 29.628 4.175   62.741  1.00 34.92  ? 33  LEU D CB  1 
ATOM   5976 C CG  . LEU D  1 18  ? 29.243 5.092   61.576  1.00 36.31  ? 33  LEU D CG  1 
ATOM   5977 C CD1 . LEU D  1 18  ? 29.511 6.544   61.935  1.00 37.21  ? 33  LEU D CD1 1 
ATOM   5978 C CD2 . LEU D  1 18  ? 29.971 4.730   60.291  1.00 37.94  ? 33  LEU D CD2 1 
ATOM   5979 N N   . ARG D  1 19  ? 31.255 1.386   63.849  1.00 29.84  ? 34  ARG D N   1 
ATOM   5980 C CA  . ARG D  1 19  ? 31.687 0.496   64.958  1.00 31.14  ? 34  ARG D CA  1 
ATOM   5981 C C   . ARG D  1 19  ? 32.831 1.158   65.727  1.00 32.23  ? 34  ARG D C   1 
ATOM   5982 O O   . ARG D  1 19  ? 33.734 1.723   65.082  1.00 32.35  ? 34  ARG D O   1 
ATOM   5983 C CB  . ARG D  1 19  ? 32.120 -0.876  64.436  1.00 29.98  ? 34  ARG D CB  1 
ATOM   5984 C CG  . ARG D  1 19  ? 31.088 -1.568  63.559  1.00 29.10  ? 34  ARG D CG  1 
ATOM   5985 C CD  . ARG D  1 19  ? 29.755 -1.799  64.239  1.00 29.11  ? 34  ARG D CD  1 
ATOM   5986 N NE  . ARG D  1 19  ? 28.932 -2.695  63.440  1.00 29.71  ? 34  ARG D NE  1 
ATOM   5987 C CZ  . ARG D  1 19  ? 29.112 -4.011  63.324  1.00 28.94  ? 34  ARG D CZ  1 
ATOM   5988 N NH1 . ARG D  1 19  ? 30.072 -4.629  63.991  1.00 29.59  ? 34  ARG D NH1 1 
ATOM   5989 N NH2 . ARG D  1 19  ? 28.320 -4.707  62.531  1.00 31.17  ? 34  ARG D NH2 1 
ATOM   5990 N N   . VAL D  1 20  ? 32.775 1.075   67.059  1.00 33.63  ? 35  VAL D N   1 
ATOM   5991 C CA  . VAL D  1 20  ? 33.808 1.598   67.996  1.00 35.04  ? 35  VAL D CA  1 
ATOM   5992 C C   . VAL D  1 20  ? 34.480 0.385   68.652  1.00 36.06  ? 35  VAL D C   1 
ATOM   5993 O O   . VAL D  1 20  ? 33.773 -0.578  68.992  1.00 34.05  ? 35  VAL D O   1 
ATOM   5994 C CB  . VAL D  1 20  ? 33.218 2.586   69.027  1.00 34.43  ? 35  VAL D CB  1 
ATOM   5995 C CG1 . VAL D  1 20  ? 32.128 1.982   69.904  1.00 33.67  ? 35  VAL D CG1 1 
ATOM   5996 C CG2 . VAL D  1 20  ? 34.305 3.195   69.897  1.00 35.31  ? 35  VAL D CG2 1 
ATOM   5997 N N   . HIS D  1 21  ? 35.801 0.440   68.813  1.00 40.24  ? 36  HIS D N   1 
ATOM   5998 C CA  . HIS D  1 21  ? 36.625 -0.635  69.422  1.00 43.34  ? 36  HIS D CA  1 
ATOM   5999 C C   . HIS D  1 21  ? 36.307 -0.705  70.915  1.00 42.72  ? 36  HIS D C   1 
ATOM   6000 O O   . HIS D  1 21  ? 36.305 0.344   71.573  1.00 45.25  ? 36  HIS D O   1 
ATOM   6001 C CB  . HIS D  1 21  ? 38.126 -0.399  69.189  1.00 48.18  ? 36  HIS D CB  1 
ATOM   6002 C CG  . HIS D  1 21  ? 38.963 -1.632  69.285  1.00 53.75  ? 36  HIS D CG  1 
ATOM   6003 N ND1 . HIS D  1 21  ? 38.567 -2.765  69.972  1.00 58.94  ? 36  HIS D ND1 1 
ATOM   6004 C CD2 . HIS D  1 21  ? 40.183 -1.913  68.775  1.00 59.03  ? 36  HIS D CD2 1 
ATOM   6005 C CE1 . HIS D  1 21  ? 39.500 -3.690  69.874  1.00 59.09  ? 36  HIS D CE1 1 
ATOM   6006 N NE2 . HIS D  1 21  ? 40.501 -3.191  69.144  1.00 60.65  ? 36  HIS D NE2 1 
ATOM   6007 N N   . GLY D  1 22  ? 35.994 -1.896  71.412  1.00 43.69  ? 37  GLY D N   1 
ATOM   6008 C CA  . GLY D  1 22  ? 35.821 -2.171  72.849  1.00 45.66  ? 37  GLY D CA  1 
ATOM   6009 C C   . GLY D  1 22  ? 35.994 -3.657  73.116  1.00 44.89  ? 37  GLY D C   1 
ATOM   6010 O O   . GLY D  1 22  ? 36.831 -4.289  72.474  1.00 47.89  ? 37  GLY D O   1 
ATOM   6011 N N   . PRO D  1 23  ? 35.211 -4.253  74.045  1.00 45.64  ? 38  PRO D N   1 
ATOM   6012 C CA  . PRO D  1 23  ? 35.149 -5.709  74.185  1.00 46.41  ? 38  PRO D CA  1 
ATOM   6013 C C   . PRO D  1 23  ? 34.851 -6.393  72.841  1.00 45.32  ? 38  PRO D C   1 
ATOM   6014 O O   . PRO D  1 23  ? 35.377 -7.460  72.595  1.00 49.57  ? 38  PRO D O   1 
ATOM   6015 C CB  . PRO D  1 23  ? 33.999 -5.933  75.181  1.00 47.59  ? 38  PRO D CB  1 
ATOM   6016 C CG  . PRO D  1 23  ? 33.940 -4.654  75.979  1.00 47.89  ? 38  PRO D CG  1 
ATOM   6017 C CD  . PRO D  1 23  ? 34.339 -3.562  75.007  1.00 47.58  ? 38  PRO D CD  1 
ATOM   6018 N N   . TYR D  1 24  ? 34.016 -5.750  72.015  1.00 41.63  ? 39  TYR D N   1 
ATOM   6019 C CA  . TYR D  1 24  ? 33.761 -6.098  70.593  1.00 38.58  ? 39  TYR D CA  1 
ATOM   6020 C C   . TYR D  1 24  ? 33.567 -4.811  69.780  1.00 37.34  ? 39  TYR D C   1 
ATOM   6021 O O   . TYR D  1 24  ? 33.526 -3.714  70.378  1.00 36.01  ? 39  TYR D O   1 
ATOM   6022 C CB  . TYR D  1 24  ? 32.562 -7.042  70.484  1.00 36.67  ? 39  TYR D CB  1 
ATOM   6023 C CG  . TYR D  1 24  ? 31.237 -6.458  70.904  1.00 37.54  ? 39  TYR D CG  1 
ATOM   6024 C CD1 . TYR D  1 24  ? 30.904 -6.289  72.243  1.00 37.19  ? 39  TYR D CD1 1 
ATOM   6025 C CD2 . TYR D  1 24  ? 30.301 -6.082  69.952  1.00 37.29  ? 39  TYR D CD2 1 
ATOM   6026 C CE1 . TYR D  1 24  ? 29.678 -5.762  72.621  1.00 37.08  ? 39  TYR D CE1 1 
ATOM   6027 C CE2 . TYR D  1 24  ? 29.077 -5.543  70.316  1.00 36.65  ? 39  TYR D CE2 1 
ATOM   6028 C CZ  . TYR D  1 24  ? 28.762 -5.386  71.652  1.00 36.14  ? 39  TYR D CZ  1 
ATOM   6029 O OH  . TYR D  1 24  ? 27.549 -4.863  71.988  1.00 37.56  ? 39  TYR D OH  1 
ATOM   6030 N N   . TRP D  1 25  ? 33.472 -4.946  68.455  1.00 34.75  ? 40  TRP D N   1 
ATOM   6031 C CA  . TRP D  1 25  ? 33.269 -3.810  67.520  1.00 34.91  ? 40  TRP D CA  1 
ATOM   6032 C C   . TRP D  1 25  ? 31.789 -3.427  67.531  1.00 33.75  ? 40  TRP D C   1 
ATOM   6033 O O   . TRP D  1 25  ? 31.018 -3.982  66.732  1.00 32.06  ? 40  TRP D O   1 
ATOM   6034 C CB  . TRP D  1 25  ? 33.793 -4.153  66.125  1.00 35.77  ? 40  TRP D CB  1 
ATOM   6035 C CG  . TRP D  1 25  ? 35.288 -4.115  66.062  1.00 34.94  ? 40  TRP D CG  1 
ATOM   6036 C CD1 . TRP D  1 25  ? 36.150 -5.165  66.200  1.00 35.03  ? 40  TRP D CD1 1 
ATOM   6037 C CD2 . TRP D  1 25  ? 36.104 -2.941  65.908  1.00 34.60  ? 40  TRP D CD2 1 
ATOM   6038 N NE1 . TRP D  1 25  ? 37.443 -4.731  66.104  1.00 33.47  ? 40  TRP D NE1 1 
ATOM   6039 C CE2 . TRP D  1 25  ? 37.448 -3.372  65.925  1.00 34.68  ? 40  TRP D CE2 1 
ATOM   6040 C CE3 . TRP D  1 25  ? 35.831 -1.580  65.719  1.00 34.05  ? 40  TRP D CE3 1 
ATOM   6041 C CZ2 . TRP D  1 25  ? 38.513 -2.484  65.774  1.00 33.54  ? 40  TRP D CZ2 1 
ATOM   6042 C CZ3 . TRP D  1 25  ? 36.883 -0.703  65.574  1.00 35.19  ? 40  TRP D CZ3 1 
ATOM   6043 C CH2 . TRP D  1 25  ? 38.206 -1.152  65.602  1.00 35.61  ? 40  TRP D CH2 1 
ATOM   6044 N N   . MET D  1 26  ? 31.424 -2.538  68.452  1.00 33.65  ? 41  MET D N   1 
ATOM   6045 C CA  . MET D  1 26  ? 30.019 -2.243  68.818  1.00 35.82  ? 41  MET D CA  1 
ATOM   6046 C C   . MET D  1 26  ? 29.467 -1.141  67.904  1.00 34.35  ? 41  MET D C   1 
ATOM   6047 O O   . MET D  1 26  ? 30.159 -0.123  67.703  1.00 31.49  ? 41  MET D O   1 
ATOM   6048 C CB  . MET D  1 26  ? 29.923 -1.805  70.280  1.00 38.87  ? 41  MET D CB  1 
ATOM   6049 C CG  . MET D  1 26  ? 28.498 -1.738  70.798  1.00 42.59  ? 41  MET D CG  1 
ATOM   6050 S SD  . MET D  1 26  ? 28.407 -1.370  72.561  1.00 46.35  ? 41  MET D SD  1 
ATOM   6051 C CE  . MET D  1 26  ? 29.138 0.267   72.612  1.00 46.71  ? 41  MET D CE  1 
ATOM   6052 N N   . HIS D  1 27  ? 28.254 -1.347  67.388  1.00 32.06  ? 42  HIS D N   1 
ATOM   6053 C CA  . HIS D  1 27  ? 27.440 -0.325  66.682  1.00 32.15  ? 42  HIS D CA  1 
ATOM   6054 C C   . HIS D  1 27  ? 27.159 0.848   67.628  1.00 32.58  ? 42  HIS D C   1 
ATOM   6055 O O   . HIS D  1 27  ? 26.681 0.589   68.737  1.00 32.54  ? 42  HIS D O   1 
ATOM   6056 C CB  . HIS D  1 27  ? 26.138 -0.944  66.152  1.00 31.38  ? 42  HIS D CB  1 
ATOM   6057 C CG  . HIS D  1 27  ? 25.220 0.070   65.564  1.00 30.36  ? 42  HIS D CG  1 
ATOM   6058 N ND1 . HIS D  1 27  ? 25.230 0.370   64.230  1.00 29.21  ? 42  HIS D ND1 1 
ATOM   6059 C CD2 . HIS D  1 27  ? 24.306 0.886   66.133  1.00 29.89  ? 42  HIS D CD2 1 
ATOM   6060 C CE1 . HIS D  1 27  ? 24.327 1.298   63.986  1.00 29.46  ? 42  HIS D CE1 1 
ATOM   6061 N NE2 . HIS D  1 27  ? 23.764 1.648   65.138  1.00 28.48  ? 42  HIS D NE2 1 
ATOM   6062 N N   . PHE D  1 28  ? 27.450 2.083   67.204  1.00 34.53  ? 43  PHE D N   1 
ATOM   6063 C CA  . PHE D  1 28  ? 27.080 3.330   67.931  1.00 35.65  ? 43  PHE D CA  1 
ATOM   6064 C C   . PHE D  1 28  ? 26.289 4.297   67.035  1.00 35.53  ? 43  PHE D C   1 
ATOM   6065 O O   . PHE D  1 28  ? 25.497 5.062   67.593  1.00 37.45  ? 43  PHE D O   1 
ATOM   6066 C CB  . PHE D  1 28  ? 28.315 3.987   68.553  1.00 34.97  ? 43  PHE D CB  1 
ATOM   6067 C CG  . PHE D  1 28  ? 29.317 4.546   67.577  1.00 34.28  ? 43  PHE D CG  1 
ATOM   6068 C CD1 . PHE D  1 28  ? 30.333 3.756   67.056  1.00 32.29  ? 43  PHE D CD1 1 
ATOM   6069 C CD2 . PHE D  1 28  ? 29.263 5.882   67.209  1.00 33.37  ? 43  PHE D CD2 1 
ATOM   6070 C CE1 . PHE D  1 28  ? 31.257 4.286   66.170  1.00 31.22  ? 43  PHE D CE1 1 
ATOM   6071 C CE2 . PHE D  1 28  ? 30.183 6.406   66.317  1.00 32.67  ? 43  PHE D CE2 1 
ATOM   6072 C CZ  . PHE D  1 28  ? 31.176 5.608   65.798  1.00 32.75  ? 43  PHE D CZ  1 
ATOM   6073 N N   . CYS D  1 29  ? 26.472 4.279   65.714  1.00 35.51  ? 44  CYS D N   1 
ATOM   6074 C CA  . CYS D  1 29  ? 25.775 5.207   64.779  1.00 36.05  ? 44  CYS D CA  1 
ATOM   6075 C C   . CYS D  1 29  ? 25.556 4.553   63.411  1.00 33.26  ? 44  CYS D C   1 
ATOM   6076 O O   . CYS D  1 29  ? 26.246 3.575   63.085  1.00 33.86  ? 44  CYS D O   1 
ATOM   6077 C CB  . CYS D  1 29  ? 26.564 6.502   64.610  1.00 36.77  ? 44  CYS D CB  1 
ATOM   6078 S SG  . CYS D  1 29  ? 26.174 7.781   65.838  1.00 39.99  ? 44  CYS D SG  1 
ATOM   6079 N N   . GLY D  1 30  ? 24.613 5.103   62.652  1.00 31.89  ? 45  GLY D N   1 
ATOM   6080 C CA  . GLY D  1 30  ? 24.381 4.769   61.239  1.00 30.66  ? 45  GLY D CA  1 
ATOM   6081 C C   . GLY D  1 30  ? 25.140 5.709   60.320  1.00 29.71  ? 45  GLY D C   1 
ATOM   6082 O O   . GLY D  1 30  ? 25.857 6.626   60.817  1.00 29.59  ? 45  GLY D O   1 
ATOM   6083 N N   . GLY D  1 31  ? 24.995 5.464   59.022  1.00 31.18  ? 46  GLY D N   1 
ATOM   6084 C CA  . GLY D  1 31  ? 25.624 6.228   57.933  1.00 31.35  ? 46  GLY D CA  1 
ATOM   6085 C C   . GLY D  1 31  ? 25.059 5.797   56.597  1.00 32.37  ? 46  GLY D C   1 
ATOM   6086 O O   . GLY D  1 31  ? 24.244 4.850   56.572  1.00 32.66  ? 46  GLY D O   1 
ATOM   6087 N N   . SER D  1 32  ? 25.456 6.473   55.523  1.00 31.65  ? 47  SER D N   1 
ATOM   6088 C CA  . SER D  1 32  ? 25.062 6.122   54.139  1.00 32.37  ? 47  SER D CA  1 
ATOM   6089 C C   . SER D  1 32  ? 26.306 6.144   53.248  1.00 31.27  ? 47  SER D C   1 
ATOM   6090 O O   . SER D  1 32  ? 27.153 7.040   53.426  1.00 29.73  ? 47  SER D O   1 
ATOM   6091 C CB  . SER D  1 32  ? 23.970 7.014   53.633  1.00 31.71  ? 47  SER D CB  1 
ATOM   6092 O OG  . SER D  1 32  ? 24.346 8.373   53.733  1.00 34.06  ? 47  SER D OG  1 
ATOM   6093 N N   . LEU D  1 33  ? 26.422 5.163   52.356  1.00 30.44  ? 48  LEU D N   1 
ATOM   6094 C CA  . LEU D  1 33  ? 27.451 5.149   51.284  1.00 31.53  ? 48  LEU D CA  1 
ATOM   6095 C C   . LEU D  1 33  ? 26.998 6.107   50.178  1.00 30.75  ? 48  LEU D C   1 
ATOM   6096 O O   . LEU D  1 33  ? 25.945 5.863   49.584  1.00 32.46  ? 48  LEU D O   1 
ATOM   6097 C CB  . LEU D  1 33  ? 27.629 3.718   50.769  1.00 31.96  ? 48  LEU D CB  1 
ATOM   6098 C CG  . LEU D  1 33  ? 28.857 3.490   49.886  1.00 32.24  ? 48  LEU D CG  1 
ATOM   6099 C CD1 . LEU D  1 33  ? 30.138 3.497   50.707  1.00 31.56  ? 48  LEU D CD1 1 
ATOM   6100 C CD2 . LEU D  1 33  ? 28.730 2.192   49.106  1.00 33.09  ? 48  LEU D CD2 1 
ATOM   6101 N N   . ILE D  1 34  ? 27.726 7.204   49.973  1.00 31.77  ? 49  ILE D N   1 
ATOM   6102 C CA  . ILE D  1 34  ? 27.390 8.239   48.943  1.00 32.53  ? 49  ILE D CA  1 
ATOM   6103 C C   . ILE D  1 34  ? 28.396 8.168   47.781  1.00 31.32  ? 49  ILE D C   1 
ATOM   6104 O O   . ILE D  1 34  ? 28.211 8.889   46.803  1.00 32.89  ? 49  ILE D O   1 
ATOM   6105 C CB  . ILE D  1 34  ? 27.300 9.640   49.585  1.00 31.27  ? 49  ILE D CB  1 
ATOM   6106 C CG1 . ILE D  1 34  ? 28.595 10.053  50.289  1.00 31.72  ? 49  ILE D CG1 1 
ATOM   6107 C CG2 . ILE D  1 34  ? 26.100 9.716   50.518  1.00 32.11  ? 49  ILE D CG2 1 
ATOM   6108 C CD1 . ILE D  1 34  ? 28.748 11.557  50.435  1.00 33.14  ? 49  ILE D CD1 1 
ATOM   6109 N N   . HIS D  1 35  ? 29.428 7.337   47.904  1.00 33.12  ? 50  HIS D N   1 
ATOM   6110 C CA  . HIS D  1 35  ? 30.514 7.123   46.912  1.00 34.40  ? 50  HIS D CA  1 
ATOM   6111 C C   . HIS D  1 35  ? 31.210 5.835   47.331  1.00 34.86  ? 50  HIS D C   1 
ATOM   6112 O O   . HIS D  1 35  ? 31.222 5.538   48.521  1.00 35.84  ? 50  HIS D O   1 
ATOM   6113 C CB  . HIS D  1 35  ? 31.442 8.351   46.887  1.00 34.75  ? 50  HIS D CB  1 
ATOM   6114 C CG  . HIS D  1 35  ? 32.554 8.290   45.894  1.00 34.79  ? 50  HIS D CG  1 
ATOM   6115 N ND1 . HIS D  1 35  ? 33.744 7.632   46.156  1.00 35.38  ? 50  HIS D ND1 1 
ATOM   6116 C CD2 . HIS D  1 35  ? 32.673 8.809   44.653  1.00 36.18  ? 50  HIS D CD2 1 
ATOM   6117 C CE1 . HIS D  1 35  ? 34.554 7.750   45.120  1.00 35.50  ? 50  HIS D CE1 1 
ATOM   6118 N NE2 . HIS D  1 35  ? 33.918 8.475   44.184  1.00 36.03  ? 50  HIS D NE2 1 
ATOM   6119 N N   . PRO D  1 36  ? 31.789 5.027   46.413  1.00 36.14  ? 51  PRO D N   1 
ATOM   6120 C CA  . PRO D  1 36  ? 32.532 3.826   46.810  1.00 34.11  ? 51  PRO D CA  1 
ATOM   6121 C C   . PRO D  1 36  ? 33.568 3.989   47.935  1.00 33.82  ? 51  PRO D C   1 
ATOM   6122 O O   . PRO D  1 36  ? 33.874 2.994   48.568  1.00 34.28  ? 51  PRO D O   1 
ATOM   6123 C CB  . PRO D  1 36  ? 33.231 3.439   45.500  1.00 36.00  ? 51  PRO D CB  1 
ATOM   6124 C CG  . PRO D  1 36  ? 32.236 3.852   44.447  1.00 35.59  ? 51  PRO D CG  1 
ATOM   6125 C CD  . PRO D  1 36  ? 31.732 5.188   44.948  1.00 36.19  ? 51  PRO D CD  1 
ATOM   6126 N N   . GLN D  1 37  ? 34.087 5.199   48.170  1.00 33.21  ? 52  GLN D N   1 
ATOM   6127 C CA  . GLN D  1 37  ? 35.133 5.460   49.193  1.00 34.63  ? 52  GLN D CA  1 
ATOM   6128 C C   . GLN D  1 37  ? 34.646 6.445   50.269  1.00 32.10  ? 52  GLN D C   1 
ATOM   6129 O O   . GLN D  1 37  ? 35.472 6.804   51.126  1.00 32.58  ? 52  GLN D O   1 
ATOM   6130 C CB  . GLN D  1 37  ? 36.414 5.949   48.508  1.00 36.65  ? 52  GLN D CB  1 
ATOM   6131 C CG  . GLN D  1 37  ? 37.666 5.648   49.319  1.00 39.36  ? 52  GLN D CG  1 
ATOM   6132 C CD  . GLN D  1 37  ? 38.942 5.678   48.515  1.00 41.71  ? 52  GLN D CD  1 
ATOM   6133 O OE1 . GLN D  1 37  ? 38.960 6.102   47.357  1.00 43.41  ? 52  GLN D OE1 1 
ATOM   6134 N NE2 . GLN D  1 37  ? 40.022 5.228   49.142  1.00 39.45  ? 52  GLN D NE2 1 
ATOM   6135 N N   . TRP D  1 38  ? 33.374 6.852   50.277  1.00 31.40  ? 53  TRP D N   1 
ATOM   6136 C CA  . TRP D  1 38  ? 32.881 7.904   51.211  1.00 31.39  ? 53  TRP D CA  1 
ATOM   6137 C C   . TRP D  1 38  ? 31.554 7.521   51.867  1.00 30.73  ? 53  TRP D C   1 
ATOM   6138 O O   . TRP D  1 38  ? 30.610 7.137   51.155  1.00 31.06  ? 53  TRP D O   1 
ATOM   6139 C CB  . TRP D  1 38  ? 32.785 9.265   50.518  1.00 30.45  ? 53  TRP D CB  1 
ATOM   6140 C CG  . TRP D  1 38  ? 34.113 9.828   50.119  1.00 30.63  ? 53  TRP D CG  1 
ATOM   6141 C CD1 . TRP D  1 38  ? 34.772 9.620   48.943  1.00 31.21  ? 53  TRP D CD1 1 
ATOM   6142 C CD2 . TRP D  1 38  ? 34.936 10.729  50.882  1.00 30.26  ? 53  TRP D CD2 1 
ATOM   6143 N NE1 . TRP D  1 38  ? 35.952 10.314  48.926  1.00 30.00  ? 53  TRP D NE1 1 
ATOM   6144 C CE2 . TRP D  1 38  ? 36.078 11.009  50.098  1.00 31.69  ? 53  TRP D CE2 1 
ATOM   6145 C CE3 . TRP D  1 38  ? 34.825 11.324  52.143  1.00 31.61  ? 53  TRP D CE3 1 
ATOM   6146 C CZ2 . TRP D  1 38  ? 37.091 11.866  50.534  1.00 32.18  ? 53  TRP D CZ2 1 
ATOM   6147 C CZ3 . TRP D  1 38  ? 35.837 12.149  52.584  1.00 32.33  ? 53  TRP D CZ3 1 
ATOM   6148 C CH2 . TRP D  1 38  ? 36.952 12.418  51.787  1.00 31.29  ? 53  TRP D CH2 1 
ATOM   6149 N N   . VAL D  1 39  ? 31.495 7.682   53.190  1.00 32.43  ? 54  VAL D N   1 
ATOM   6150 C CA  . VAL D  1 39  ? 30.274 7.499   54.025  1.00 30.77  ? 54  VAL D CA  1 
ATOM   6151 C C   . VAL D  1 39  ? 29.852 8.869   54.563  1.00 29.55  ? 54  VAL D C   1 
ATOM   6152 O O   . VAL D  1 39  ? 30.706 9.588   55.110  1.00 28.61  ? 54  VAL D O   1 
ATOM   6153 C CB  . VAL D  1 39  ? 30.546 6.475   55.140  1.00 30.87  ? 54  VAL D CB  1 
ATOM   6154 C CG1 . VAL D  1 39  ? 29.441 6.429   56.189  1.00 30.47  ? 54  VAL D CG1 1 
ATOM   6155 C CG2 . VAL D  1 39  ? 30.797 5.093   54.546  1.00 31.65  ? 54  VAL D CG2 1 
ATOM   6156 N N   . LEU D  1 40  ? 28.566 9.192   54.424  1.00 29.59  ? 55  LEU D N   1 
ATOM   6157 C CA  . LEU D  1 40  ? 27.911 10.370  55.047  1.00 29.76  ? 55  LEU D CA  1 
ATOM   6158 C C   . LEU D  1 40  ? 27.334 9.944   56.399  1.00 30.55  ? 55  LEU D C   1 
ATOM   6159 O O   . LEU D  1 40  ? 26.650 8.905   56.447  1.00 30.26  ? 55  LEU D O   1 
ATOM   6160 C CB  . LEU D  1 40  ? 26.820 10.887  54.104  1.00 29.93  ? 55  LEU D CB  1 
ATOM   6161 C CG  . LEU D  1 40  ? 26.082 12.146  54.552  1.00 30.91  ? 55  LEU D CG  1 
ATOM   6162 C CD1 . LEU D  1 40  ? 27.026 13.332  54.651  1.00 31.24  ? 55  LEU D CD1 1 
ATOM   6163 C CD2 . LEU D  1 40  ? 24.939 12.464  53.598  1.00 31.29  ? 55  LEU D CD2 1 
ATOM   6164 N N   . THR D  1 41  ? 27.603 10.721  57.453  1.00 29.82  ? 56  THR D N   1 
ATOM   6165 C CA  . THR D  1 41  ? 27.104 10.486  58.831  1.00 30.23  ? 56  THR D CA  1 
ATOM   6166 C C   . THR D  1 41  ? 26.813 11.828  59.521  1.00 29.38  ? 56  THR D C   1 
ATOM   6167 O O   . THR D  1 41  ? 26.921 12.882  58.865  1.00 28.89  ? 56  THR D O   1 
ATOM   6168 C CB  . THR D  1 41  ? 28.084 9.573   59.589  1.00 30.81  ? 56  THR D CB  1 
ATOM   6169 O OG1 . THR D  1 41  ? 27.393 9.073   60.738  1.00 30.97  ? 56  THR D OG1 1 
ATOM   6170 C CG2 . THR D  1 41  ? 29.375 10.260  59.989  1.00 32.93  ? 56  THR D CG2 1 
ATOM   6171 N N   . ALA D  1 42  ? 26.449 11.773  60.803  1.00 30.59  ? 57  ALA D N   1 
ATOM   6172 C CA  . ALA D  1 42  ? 26.252 12.941  61.686  1.00 29.36  ? 57  ALA D CA  1 
ATOM   6173 C C   . ALA D  1 42  ? 27.593 13.254  62.346  1.00 28.73  ? 57  ALA D C   1 
ATOM   6174 O O   . ALA D  1 42  ? 28.280 12.309  62.759  1.00 28.69  ? 57  ALA D O   1 
ATOM   6175 C CB  . ALA D  1 42  ? 25.178 12.653  62.704  1.00 30.61  ? 57  ALA D CB  1 
ATOM   6176 N N   . ALA D  1 43  ? 27.951 14.534  62.425  1.00 28.10  ? 58  ALA D N   1 
ATOM   6177 C CA  . ALA D  1 43  ? 29.139 15.047  63.145  1.00 26.94  ? 58  ALA D CA  1 
ATOM   6178 C C   . ALA D  1 43  ? 29.142 14.605  64.618  1.00 28.49  ? 58  ALA D C   1 
ATOM   6179 O O   . ALA D  1 43  ? 30.235 14.287  65.119  1.00 29.00  ? 58  ALA D O   1 
ATOM   6180 C CB  . ALA D  1 43  ? 29.184 16.545  63.028  1.00 26.31  ? 58  ALA D CB  1 
ATOM   6181 N N   . HIS D  1 44  ? 27.986 14.580  65.295  1.00 29.01  ? 59  HIS D N   1 
ATOM   6182 C CA  . HIS D  1 44  ? 27.892 14.278  66.752  1.00 30.15  ? 59  HIS D CA  1 
ATOM   6183 C C   . HIS D  1 44  ? 28.309 12.823  67.021  1.00 31.00  ? 59  HIS D C   1 
ATOM   6184 O O   . HIS D  1 44  ? 28.690 12.532  68.167  1.00 30.25  ? 59  HIS D O   1 
ATOM   6185 C CB  . HIS D  1 44  ? 26.506 14.651  67.322  1.00 29.32  ? 59  HIS D CB  1 
ATOM   6186 C CG  . HIS D  1 44  ? 25.453 13.604  67.185  1.00 30.17  ? 59  HIS D CG  1 
ATOM   6187 N ND1 . HIS D  1 44  ? 24.443 13.704  66.261  1.00 29.82  ? 59  HIS D ND1 1 
ATOM   6188 C CD2 . HIS D  1 44  ? 25.222 12.459  67.872  1.00 30.99  ? 59  HIS D CD2 1 
ATOM   6189 C CE1 . HIS D  1 44  ? 23.653 12.655  66.357  1.00 30.26  ? 59  HIS D CE1 1 
ATOM   6190 N NE2 . HIS D  1 44  ? 24.107 11.876  67.337  1.00 31.36  ? 59  HIS D NE2 1 
ATOM   6191 N N   . CYS D  1 45  ? 28.239 11.945  66.014  1.00 31.54  ? 60  CYS D N   1 
ATOM   6192 C CA  . CYS D  1 45  ? 28.688 10.533  66.101  1.00 34.62  ? 60  CYS D CA  1 
ATOM   6193 C C   . CYS D  1 45  ? 30.211 10.452  66.257  1.00 32.90  ? 60  CYS D C   1 
ATOM   6194 O O   . CYS D  1 45  ? 30.663 9.512   66.928  1.00 35.68  ? 60  CYS D O   1 
ATOM   6195 C CB  . CYS D  1 45  ? 28.258 9.744   64.872  1.00 34.76  ? 60  CYS D CB  1 
ATOM   6196 S SG  . CYS D  1 45  ? 26.466 9.526   64.777  1.00 37.71  ? 60  CYS D SG  1 
ATOM   6197 N N   . VAL D  1 46  ? 30.959 11.389  65.664  1.00 32.32  ? 61  VAL D N   1 
ATOM   6198 C CA  . VAL D  1 46  ? 32.451 11.319  65.566  1.00 35.78  ? 61  VAL D CA  1 
ATOM   6199 C C   . VAL D  1 46  ? 33.115 12.612  66.071  1.00 36.56  ? 61  VAL D C   1 
ATOM   6200 O O   . VAL D  1 46  ? 34.344 12.686  65.982  1.00 39.72  ? 61  VAL D O   1 
ATOM   6201 C CB  . VAL D  1 46  ? 32.889 10.978  64.129  1.00 35.70  ? 61  VAL D CB  1 
ATOM   6202 C CG1 . VAL D  1 46  ? 32.470 9.563   63.752  1.00 35.64  ? 61  VAL D CG1 1 
ATOM   6203 C CG2 . VAL D  1 46  ? 32.371 11.978  63.098  1.00 36.89  ? 61  VAL D CG2 1 
ATOM   6204 N N   . GLY D  1 47  ? 32.361 13.546  66.652  1.00 34.81  ? 62  GLY D N   1 
ATOM   6205 C CA  . GLY D  1 47  ? 32.883 14.847  67.116  1.00 35.79  ? 62  GLY D CA  1 
ATOM   6206 C C   . GLY D  1 47  ? 32.003 15.461  68.195  1.00 34.25  ? 62  GLY D C   1 
ATOM   6207 O O   . GLY D  1 47  ? 31.065 14.821  68.650  1.00 37.07  ? 62  GLY D O   1 
ATOM   6208 N N   . PRO D  1 48  ? 32.262 16.712  68.644  1.00 36.88  ? 63  PRO D N   1 
ATOM   6209 C CA  . PRO D  1 48  ? 33.254 17.596  68.020  1.00 36.45  ? 63  PRO D CA  1 
ATOM   6210 C C   . PRO D  1 48  ? 34.730 17.302  68.343  1.00 36.27  ? 63  PRO D C   1 
ATOM   6211 O O   . PRO D  1 48  ? 35.572 17.872  67.684  1.00 36.98  ? 63  PRO D O   1 
ATOM   6212 C CB  . PRO D  1 48  ? 32.878 18.971  68.592  1.00 35.90  ? 63  PRO D CB  1 
ATOM   6213 C CG  . PRO D  1 48  ? 32.336 18.658  69.962  1.00 37.01  ? 63  PRO D CG  1 
ATOM   6214 C CD  . PRO D  1 48  ? 31.601 17.340  69.799  1.00 35.96  ? 63  PRO D CD  1 
ATOM   6215 N N   . ASP D  1 49  ? 35.020 16.461  69.337  1.00 37.68  ? 64  ASP D N   1 
ATOM   6216 C CA  . ASP D  1 49  ? 36.417 16.145  69.748  1.00 39.94  ? 64  ASP D CA  1 
ATOM   6217 C C   . ASP D  1 49  ? 37.032 15.147  68.767  1.00 40.17  ? 64  ASP D C   1 
ATOM   6218 O O   . ASP D  1 49  ? 36.322 14.211  68.347  1.00 36.63  ? 64  ASP D O   1 
ATOM   6219 C CB  . ASP D  1 49  ? 36.499 15.588  71.168  1.00 40.39  ? 64  ASP D CB  1 
ATOM   6220 C CG  . ASP D  1 49  ? 36.047 16.574  72.228  1.00 44.62  ? 64  ASP D CG  1 
ATOM   6221 O OD1 . ASP D  1 49  ? 36.336 17.799  72.084  1.00 41.98  ? 64  ASP D OD1 1 
ATOM   6222 O OD2 . ASP D  1 49  ? 35.401 16.109  73.184  1.00 48.05  ? 64  ASP D OD2 1 
ATOM   6223 N N   . VAL D  1 50  ? 38.318 15.331  68.454  1.00 39.37  ? 65  VAL D N   1 
ATOM   6224 C CA  . VAL D  1 50  ? 39.104 14.449  67.549  1.00 40.18  ? 65  VAL D CA  1 
ATOM   6225 C C   . VAL D  1 50  ? 39.261 13.096  68.246  1.00 42.04  ? 65  VAL D C   1 
ATOM   6226 O O   . VAL D  1 50  ? 39.698 13.077  69.412  1.00 48.40  ? 65  VAL D O   1 
ATOM   6227 C CB  . VAL D  1 50  ? 40.457 15.082  67.173  1.00 41.63  ? 65  VAL D CB  1 
ATOM   6228 C CG1 . VAL D  1 50  ? 41.369 14.113  66.425  1.00 42.01  ? 65  VAL D CG1 1 
ATOM   6229 C CG2 . VAL D  1 50  ? 40.249 16.349  66.357  1.00 41.84  ? 65  VAL D CG2 1 
ATOM   6230 N N   . LYS D  1 51  ? 38.894 12.025  67.549  1.00 43.27  ? 66  LYS D N   1 
ATOM   6231 C CA  . LYS D  1 51  ? 38.981 10.625  68.027  1.00 48.88  ? 66  LYS D CA  1 
ATOM   6232 C C   . LYS D  1 51  ? 40.031 9.867   67.220  1.00 47.61  ? 66  LYS D C   1 
ATOM   6233 O O   . LYS D  1 51  ? 40.348 10.299  66.096  1.00 46.72  ? 66  LYS D O   1 
ATOM   6234 C CB  . LYS D  1 51  ? 37.584 10.016  67.950  1.00 53.82  ? 66  LYS D CB  1 
ATOM   6235 C CG  . LYS D  1 51  ? 36.687 10.533  69.069  1.00 57.15  ? 66  LYS D CG  1 
ATOM   6236 C CD  . LYS D  1 51  ? 35.194 10.501  68.816  1.00 59.26  ? 66  LYS D CD  1 
ATOM   6237 C CE  . LYS D  1 51  ? 34.460 11.509  69.680  1.00 58.59  ? 66  LYS D CE  1 
ATOM   6238 N NZ  . LYS D  1 51  ? 32.989 11.414  69.527  1.00 62.25  ? 66  LYS D NZ  1 
ATOM   6239 N N   . ASP D  1 52  ? 40.548 8.777   67.797  1.00 47.23  ? 67  ASP D N   1 
ATOM   6240 C CA  . ASP D  1 52  ? 41.551 7.880   67.159  1.00 46.31  ? 67  ASP D CA  1 
ATOM   6241 C C   . ASP D  1 52  ? 40.863 7.100   66.034  1.00 42.50  ? 67  ASP D C   1 
ATOM   6242 O O   . ASP D  1 52  ? 39.899 6.388   66.327  1.00 43.10  ? 67  ASP D O   1 
ATOM   6243 C CB  . ASP D  1 52  ? 42.192 6.952   68.197  1.00 49.80  ? 67  ASP D CB  1 
ATOM   6244 C CG  . ASP D  1 52  ? 43.224 5.980   67.646  1.00 53.06  ? 67  ASP D CG  1 
ATOM   6245 O OD1 . ASP D  1 52  ? 43.842 6.287   66.604  1.00 54.10  ? 67  ASP D OD1 1 
ATOM   6246 O OD2 . ASP D  1 52  ? 43.395 4.915   68.265  1.00 61.99  ? 67  ASP D OD2 1 
ATOM   6247 N N   . LEU D  1 53  ? 41.334 7.267   64.796  1.00 42.43  ? 68  LEU D N   1 
ATOM   6248 C CA  . LEU D  1 53  ? 40.813 6.587   63.575  1.00 43.93  ? 68  LEU D CA  1 
ATOM   6249 C C   . LEU D  1 53  ? 40.911 5.063   63.733  1.00 43.58  ? 68  LEU D C   1 
ATOM   6250 O O   . LEU D  1 53  ? 40.023 4.379   63.210  1.00 43.38  ? 68  LEU D O   1 
ATOM   6251 C CB  . LEU D  1 53  ? 41.620 7.035   62.351  1.00 45.73  ? 68  LEU D CB  1 
ATOM   6252 C CG  . LEU D  1 53  ? 41.302 8.427   61.806  1.00 49.28  ? 68  LEU D CG  1 
ATOM   6253 C CD1 . LEU D  1 53  ? 42.459 8.970   60.978  1.00 51.21  ? 68  LEU D CD1 1 
ATOM   6254 C CD2 . LEU D  1 53  ? 40.041 8.389   60.975  1.00 51.30  ? 68  LEU D CD2 1 
ATOM   6255 N N   . ALA D  1 54  ? 41.956 4.557   64.403  1.00 41.86  ? 69  ALA D N   1 
ATOM   6256 C CA  . ALA D  1 54  ? 42.219 3.109   64.604  1.00 43.57  ? 69  ALA D CA  1 
ATOM   6257 C C   . ALA D  1 54  ? 41.085 2.450   65.403  1.00 41.51  ? 69  ALA D C   1 
ATOM   6258 O O   . ALA D  1 54  ? 40.904 1.240   65.255  1.00 42.05  ? 69  ALA D O   1 
ATOM   6259 C CB  . ALA D  1 54  ? 43.554 2.912   65.286  1.00 44.84  ? 69  ALA D CB  1 
ATOM   6260 N N   . ALA D  1 55  ? 40.356 3.215   66.224  1.00 40.09  ? 70  ALA D N   1 
ATOM   6261 C CA  . ALA D  1 55  ? 39.233 2.748   67.071  1.00 39.31  ? 70  ALA D CA  1 
ATOM   6262 C C   . ALA D  1 55  ? 37.890 2.799   66.327  1.00 37.62  ? 70  ALA D C   1 
ATOM   6263 O O   . ALA D  1 55  ? 36.887 2.434   66.949  1.00 36.94  ? 70  ALA D O   1 
ATOM   6264 C CB  . ALA D  1 55  ? 39.174 3.579   68.330  1.00 39.98  ? 70  ALA D CB  1 
ATOM   6265 N N   . LEU D  1 56  ? 37.861 3.227   65.062  1.00 37.23  ? 71  LEU D N   1 
ATOM   6266 C CA  . LEU D  1 56  ? 36.623 3.327   64.240  1.00 37.11  ? 71  LEU D CA  1 
ATOM   6267 C C   . LEU D  1 56  ? 36.711 2.346   63.069  1.00 35.49  ? 71  LEU D C   1 
ATOM   6268 O O   . LEU D  1 56  ? 37.749 2.326   62.404  1.00 40.19  ? 71  LEU D O   1 
ATOM   6269 C CB  . LEU D  1 56  ? 36.464 4.771   63.748  1.00 36.56  ? 71  LEU D CB  1 
ATOM   6270 C CG  . LEU D  1 56  ? 35.321 5.048   62.771  1.00 36.96  ? 71  LEU D CG  1 
ATOM   6271 C CD1 . LEU D  1 56  ? 33.968 4.747   63.397  1.00 38.98  ? 71  LEU D CD1 1 
ATOM   6272 C CD2 . LEU D  1 56  ? 35.375 6.494   62.297  1.00 36.63  ? 71  LEU D CD2 1 
ATOM   6273 N N   . ARG D  1 57  ? 35.630 1.613   62.791  1.00 35.51  ? 72  ARG D N   1 
ATOM   6274 C CA  . ARG D  1 57  ? 35.461 0.827   61.538  1.00 35.85  ? 72  ARG D CA  1 
ATOM   6275 C C   . ARG D  1 57  ? 34.047 0.982   60.985  1.00 33.40  ? 72  ARG D C   1 
ATOM   6276 O O   . ARG D  1 57  ? 33.148 1.351   61.738  1.00 30.19  ? 72  ARG D O   1 
ATOM   6277 C CB  . ARG D  1 57  ? 35.848 -0.640  61.750  1.00 39.25  ? 72  ARG D CB  1 
ATOM   6278 C CG  . ARG D  1 57  ? 37.336 -0.842  61.483  1.00 41.66  ? 72  ARG D CG  1 
ATOM   6279 C CD  . ARG D  1 57  ? 37.974 -2.173  61.782  1.00 45.46  ? 72  ARG D CD  1 
ATOM   6280 N NE  . ARG D  1 57  ? 39.402 -2.038  62.069  1.00 46.66  ? 72  ARG D NE  1 
ATOM   6281 C CZ  . ARG D  1 57  ? 40.228 -3.048  62.371  1.00 51.53  ? 72  ARG D CZ  1 
ATOM   6282 N NH1 . ARG D  1 57  ? 39.797 -4.303  62.404  1.00 50.81  ? 72  ARG D NH1 1 
ATOM   6283 N NH2 . ARG D  1 57  ? 41.499 -2.794  62.629  1.00 52.74  ? 72  ARG D NH2 1 
ATOM   6284 N N   . VAL D  1 58  ? 33.900 0.727   59.685  1.00 33.28  ? 73  VAL D N   1 
ATOM   6285 C CA  . VAL D  1 58  ? 32.608 0.784   58.951  1.00 33.41  ? 73  VAL D CA  1 
ATOM   6286 C C   . VAL D  1 58  ? 32.221 -0.640  58.554  1.00 32.35  ? 73  VAL D C   1 
ATOM   6287 O O   . VAL D  1 58  ? 33.098 -1.411  58.126  1.00 31.43  ? 73  VAL D O   1 
ATOM   6288 C CB  . VAL D  1 58  ? 32.694 1.736   57.744  1.00 34.85  ? 73  VAL D CB  1 
ATOM   6289 C CG1 . VAL D  1 58  ? 31.458 1.669   56.861  1.00 35.04  ? 73  VAL D CG1 1 
ATOM   6290 C CG2 . VAL D  1 58  ? 32.941 3.172   58.195  1.00 33.95  ? 73  VAL D CG2 1 
ATOM   6291 N N   . GLN D  1 59  ? 30.940 -0.962  58.707  1.00 32.97  ? 74  GLN D N   1 
ATOM   6292 C CA  . GLN D  1 59  ? 30.309 -2.213  58.226  1.00 32.68  ? 74  GLN D CA  1 
ATOM   6293 C C   . GLN D  1 59  ? 29.255 -1.818  57.192  1.00 33.35  ? 74  GLN D C   1 
ATOM   6294 O O   . GLN D  1 59  ? 28.357 -1.027  57.552  1.00 34.38  ? 74  GLN D O   1 
ATOM   6295 C CB  . GLN D  1 59  ? 29.707 -2.963  59.412  1.00 32.31  ? 74  GLN D CB  1 
ATOM   6296 C CG  . GLN D  1 59  ? 28.857 -4.169  59.041  1.00 32.66  ? 74  GLN D CG  1 
ATOM   6297 C CD  . GLN D  1 59  ? 29.620 -5.195  58.239  1.00 33.51  ? 74  GLN D CD  1 
ATOM   6298 O OE1 . GLN D  1 59  ? 30.738 -5.571  58.588  1.00 35.68  ? 74  GLN D OE1 1 
ATOM   6299 N NE2 . GLN D  1 59  ? 29.027 -5.654  57.147  1.00 33.49  ? 74  GLN D NE2 1 
ATOM   6300 N N   . LEU D  1 60  ? 29.347 -2.376  55.983  1.00 34.45  ? 75  LEU D N   1 
ATOM   6301 C CA  . LEU D  1 60  ? 28.370 -2.154  54.885  1.00 37.01  ? 75  LEU D CA  1 
ATOM   6302 C C   . LEU D  1 60  ? 27.063 -2.887  55.220  1.00 38.16  ? 75  LEU D C   1 
ATOM   6303 O O   . LEU D  1 60  ? 27.036 -3.618  56.220  1.00 36.66  ? 75  LEU D O   1 
ATOM   6304 C CB  . LEU D  1 60  ? 28.972 -2.647  53.564  1.00 38.22  ? 75  LEU D CB  1 
ATOM   6305 C CG  . LEU D  1 60  ? 30.246 -1.932  53.111  1.00 39.94  ? 75  LEU D CG  1 
ATOM   6306 C CD1 . LEU D  1 60  ? 30.850 -2.624  51.897  1.00 39.94  ? 75  LEU D CD1 1 
ATOM   6307 C CD2 . LEU D  1 60  ? 29.976 -0.465  52.815  1.00 39.67  ? 75  LEU D CD2 1 
ATOM   6308 N N   . ARG D  1 61  ? 26.026 -2.711  54.395  1.00 37.70  ? 76  ARG D N   1 
ATOM   6309 C CA  . ARG D  1 61  ? 24.656 -3.256  54.616  1.00 40.82  ? 76  ARG D CA  1 
ATOM   6310 C C   . ARG D  1 61  ? 24.769 -4.706  55.117  1.00 38.69  ? 76  ARG D C   1 
ATOM   6311 O O   . ARG D  1 61  ? 25.368 -5.510  54.400  1.00 40.20  ? 76  ARG D O   1 
ATOM   6312 C CB  . ARG D  1 61  ? 23.853 -3.133  53.309  1.00 40.98  ? 76  ARG D CB  1 
ATOM   6313 C CG  . ARG D  1 61  ? 22.500 -3.839  53.223  1.00 42.96  ? 76  ARG D CG  1 
ATOM   6314 C CD  . ARG D  1 61  ? 21.477 -3.257  54.163  1.00 44.35  ? 76  ARG D CD  1 
ATOM   6315 N NE  . ARG D  1 61  ? 20.085 -3.548  53.805  1.00 45.76  ? 76  ARG D NE  1 
ATOM   6316 C CZ  . ARG D  1 61  ? 19.449 -4.696  54.028  1.00 43.00  ? 76  ARG D CZ  1 
ATOM   6317 N NH1 . ARG D  1 61  ? 20.075 -5.722  54.585  1.00 42.54  ? 76  ARG D NH1 1 
ATOM   6318 N NH2 . ARG D  1 61  ? 18.168 -4.817  53.732  1.00 38.95  ? 76  ARG D NH2 1 
ATOM   6319 N N   . GLU D  1 62  ? 24.228 -5.008  56.300  1.00 38.11  ? 77  GLU D N   1 
ATOM   6320 C CA  . GLU D  1 62  ? 23.940 -6.402  56.734  1.00 39.69  ? 77  GLU D CA  1 
ATOM   6321 C C   . GLU D  1 62  ? 22.506 -6.446  57.268  1.00 38.66  ? 77  GLU D C   1 
ATOM   6322 O O   . GLU D  1 62  ? 22.032 -5.428  57.791  1.00 42.99  ? 77  GLU D O   1 
ATOM   6323 C CB  . GLU D  1 62  ? 24.998 -6.952  57.700  1.00 39.62  ? 77  GLU D CB  1 
ATOM   6324 C CG  . GLU D  1 62  ? 25.451 -6.010  58.782  1.00 41.07  ? 77  GLU D CG  1 
ATOM   6325 C CD  . GLU D  1 62  ? 26.486 -6.574  59.753  1.00 40.05  ? 77  GLU D CD  1 
ATOM   6326 O OE1 . GLU D  1 62  ? 27.192 -7.536  59.415  1.00 41.15  ? 77  GLU D OE1 1 
ATOM   6327 O OE2 . GLU D  1 62  ? 26.594 -6.033  60.848  1.00 40.73  ? 77  GLU D OE2 1 
ATOM   6328 N N   . GLN D  1 63  ? 21.810 -7.556  57.035  1.00 35.19  ? 78  GLN D N   1 
ATOM   6329 C CA  . GLN D  1 63  ? 20.400 -7.757  57.450  1.00 36.01  ? 78  GLN D CA  1 
ATOM   6330 C C   . GLN D  1 63  ? 20.333 -7.854  58.980  1.00 35.59  ? 78  GLN D C   1 
ATOM   6331 O O   . GLN D  1 63  ? 19.348 -7.345  59.557  1.00 34.62  ? 78  GLN D O   1 
ATOM   6332 C CB  . GLN D  1 63  ? 19.832 -8.991  56.744  1.00 35.79  ? 78  GLN D CB  1 
ATOM   6333 C CG  . GLN D  1 63  ? 18.329 -9.167  56.876  1.00 36.62  ? 78  GLN D CG  1 
ATOM   6334 C CD  . GLN D  1 63  ? 17.542 -8.039  56.262  1.00 38.76  ? 78  GLN D CD  1 
ATOM   6335 O OE1 . GLN D  1 63  ? 18.033 -7.290  55.421  1.00 38.18  ? 78  GLN D OE1 1 
ATOM   6336 N NE2 . GLN D  1 63  ? 16.312 -7.887  56.720  1.00 44.19  ? 78  GLN D NE2 1 
ATOM   6337 N N   . HIS D  1 64  ? 21.332 -8.489  59.602  1.00 35.19  ? 79  HIS D N   1 
ATOM   6338 C CA  . HIS D  1 64  ? 21.439 -8.711  61.066  1.00 34.79  ? 79  HIS D CA  1 
ATOM   6339 C C   . HIS D  1 64  ? 22.819 -8.251  61.546  1.00 36.49  ? 79  HIS D C   1 
ATOM   6340 O O   . HIS D  1 64  ? 23.806 -8.857  61.095  1.00 39.31  ? 79  HIS D O   1 
ATOM   6341 C CB  . HIS D  1 64  ? 21.172 -10.187 61.385  1.00 36.69  ? 79  HIS D CB  1 
ATOM   6342 C CG  . HIS D  1 64  ? 19.792 -10.624 61.035  1.00 35.54  ? 79  HIS D CG  1 
ATOM   6343 N ND1 . HIS D  1 64  ? 19.512 -11.370 59.903  1.00 37.86  ? 79  HIS D ND1 1 
ATOM   6344 C CD2 . HIS D  1 64  ? 18.611 -10.399 61.647  1.00 36.40  ? 79  HIS D CD2 1 
ATOM   6345 C CE1 . HIS D  1 64  ? 18.213 -11.595 59.839  1.00 36.07  ? 79  HIS D CE1 1 
ATOM   6346 N NE2 . HIS D  1 64  ? 17.636 -11.013 60.904  1.00 36.18  ? 79  HIS D NE2 1 
ATOM   6347 N N   . LEU D  1 65  ? 22.890 -7.212  62.396  1.00 34.91  ? 80  LEU D N   1 
ATOM   6348 C CA  . LEU D  1 65  ? 24.165 -6.684  62.950  1.00 36.00  ? 80  LEU D CA  1 
ATOM   6349 C C   . LEU D  1 65  ? 24.981 -7.828  63.550  1.00 35.73  ? 80  LEU D C   1 
ATOM   6350 O O   . LEU D  1 65  ? 24.382 -8.651  64.276  1.00 35.99  ? 80  LEU D O   1 
ATOM   6351 C CB  . LEU D  1 65  ? 23.918 -5.658  64.060  1.00 36.56  ? 80  LEU D CB  1 
ATOM   6352 C CG  . LEU D  1 65  ? 23.876 -4.186  63.686  1.00 37.67  ? 80  LEU D CG  1 
ATOM   6353 C CD1 . LEU D  1 65  ? 23.701 -3.369  64.954  1.00 38.01  ? 80  LEU D CD1 1 
ATOM   6354 C CD2 . LEU D  1 65  ? 25.115 -3.717  62.945  1.00 37.02  ? 80  LEU D CD2 1 
ATOM   6355 N N   . TYR D  1 66  ? 26.288 -7.837  63.266  1.00 33.98  ? 81  TYR D N   1 
ATOM   6356 C CA  . TYR D  1 66  ? 27.346 -8.647  63.929  1.00 35.47  ? 81  TYR D CA  1 
ATOM   6357 C C   . TYR D  1 66  ? 27.480 -10.052 63.327  1.00 36.68  ? 81  TYR D C   1 
ATOM   6358 O O   . TYR D  1 66  ? 28.524 -10.666 63.579  1.00 37.06  ? 81  TYR D O   1 
ATOM   6359 C CB  . TYR D  1 66  ? 27.128 -8.741  65.440  1.00 32.16  ? 81  TYR D CB  1 
ATOM   6360 C CG  . TYR D  1 66  ? 26.985 -7.411  66.133  1.00 32.03  ? 81  TYR D CG  1 
ATOM   6361 C CD1 . TYR D  1 66  ? 28.012 -6.481  66.101  1.00 30.67  ? 81  TYR D CD1 1 
ATOM   6362 C CD2 . TYR D  1 66  ? 25.822 -7.077  66.813  1.00 30.19  ? 81  TYR D CD2 1 
ATOM   6363 C CE1 . TYR D  1 66  ? 27.885 -5.246  66.718  1.00 31.69  ? 81  TYR D CE1 1 
ATOM   6364 C CE2 . TYR D  1 66  ? 25.680 -5.848  67.436  1.00 32.25  ? 81  TYR D CE2 1 
ATOM   6365 C CZ  . TYR D  1 66  ? 26.716 -4.929  67.386  1.00 31.11  ? 81  TYR D CZ  1 
ATOM   6366 O OH  . TYR D  1 66  ? 26.604 -3.735  68.023  1.00 30.17  ? 81  TYR D OH  1 
ATOM   6367 N N   . TYR D  1 67  ? 26.511 -10.542 62.550  1.00 39.85  ? 82  TYR D N   1 
ATOM   6368 C CA  A TYR D  1 67  ? 26.455 -11.965 62.108  0.50 44.52  ? 82  TYR D CA  1 
ATOM   6369 C CA  B TYR D  1 67  ? 26.478 -11.971 62.130  0.50 41.57  ? 82  TYR D CA  1 
ATOM   6370 C C   . TYR D  1 67  ? 27.464 -12.218 60.975  1.00 45.62  ? 82  TYR D C   1 
ATOM   6371 O O   . TYR D  1 67  ? 28.114 -13.290 60.994  1.00 50.14  ? 82  TYR D O   1 
ATOM   6372 C CB  A TYR D  1 67  ? 25.033 -12.380 61.709  0.50 45.60  ? 82  TYR D CB  1 
ATOM   6373 C CB  B TYR D  1 67  ? 25.030 -12.419 61.907  0.50 38.89  ? 82  TYR D CB  1 
ATOM   6374 C CG  A TYR D  1 67  ? 24.941 -13.787 61.171  0.50 48.65  ? 82  TYR D CG  1 
ATOM   6375 C CG  B TYR D  1 67  ? 24.304 -12.588 63.219  0.50 37.03  ? 82  TYR D CG  1 
ATOM   6376 C CD1 A TYR D  1 67  ? 25.541 -14.845 61.835  0.50 48.10  ? 82  TYR D CD1 1 
ATOM   6377 C CD1 B TYR D  1 67  ? 24.461 -13.737 63.978  0.50 36.59  ? 82  TYR D CD1 1 
ATOM   6378 C CD2 A TYR D  1 67  ? 24.255 -14.066 59.999  0.50 51.29  ? 82  TYR D CD2 1 
ATOM   6379 C CD2 B TYR D  1 67  ? 23.546 -11.563 63.755  0.50 35.34  ? 82  TYR D CD2 1 
ATOM   6380 C CE1 A TYR D  1 67  ? 25.472 -16.139 61.348  0.50 48.45  ? 82  TYR D CE1 1 
ATOM   6381 C CE1 B TYR D  1 67  ? 23.833 -13.887 65.203  0.50 34.61  ? 82  TYR D CE1 1 
ATOM   6382 C CE2 A TYR D  1 67  ? 24.173 -15.356 59.500  0.50 50.91  ? 82  TYR D CE2 1 
ATOM   6383 C CE2 B TYR D  1 67  ? 22.919 -11.691 64.983  0.50 34.74  ? 82  TYR D CE2 1 
ATOM   6384 C CZ  A TYR D  1 67  ? 24.782 -16.395 60.178  0.50 50.15  ? 82  TYR D CZ  1 
ATOM   6385 C CZ  B TYR D  1 67  ? 23.059 -12.860 65.709  0.50 34.46  ? 82  TYR D CZ  1 
ATOM   6386 O OH  A TYR D  1 67  ? 24.706 -17.669 59.697  0.50 53.33  ? 82  TYR D OH  1 
ATOM   6387 O OH  B TYR D  1 67  ? 22.444 -12.993 66.917  0.50 32.34  ? 82  TYR D OH  1 
ATOM   6388 N N   . GLN D  1 68  ? 27.617 -11.271 60.041  1.00 47.28  ? 83  GLN D N   1 
ATOM   6389 C CA  . GLN D  1 68  ? 28.500 -11.454 58.854  1.00 50.53  ? 83  GLN D CA  1 
ATOM   6390 C C   . GLN D  1 68  ? 29.429 -10.244 58.728  1.00 43.62  ? 83  GLN D C   1 
ATOM   6391 O O   . GLN D  1 68  ? 29.458 -9.645  57.650  1.00 47.28  ? 83  GLN D O   1 
ATOM   6392 C CB  . GLN D  1 68  ? 27.647 -11.642 57.593  1.00 56.29  ? 83  GLN D CB  1 
ATOM   6393 C CG  . GLN D  1 68  ? 26.794 -12.902 57.582  1.00 63.34  ? 83  GLN D CG  1 
ATOM   6394 C CD  . GLN D  1 68  ? 27.572 -14.163 57.305  1.00 66.27  ? 83  GLN D CD  1 
ATOM   6395 O OE1 . GLN D  1 68  ? 28.801 -14.184 57.296  1.00 71.83  ? 83  GLN D OE1 1 
ATOM   6396 N NE2 . GLN D  1 68  ? 26.844 -15.240 57.060  1.00 68.32  ? 83  GLN D NE2 1 
ATOM   6397 N N   . ASP D  1 69  ? 30.159 -9.898  59.791  1.00 41.03  ? 84  ASP D N   1 
ATOM   6398 C CA  . ASP D  1 69  ? 30.955 -8.642  59.846  1.00 39.14  ? 84  ASP D CA  1 
ATOM   6399 C C   . ASP D  1 69  ? 32.168 -8.764  58.915  1.00 38.05  ? 84  ASP D C   1 
ATOM   6400 O O   . ASP D  1 69  ? 32.877 -9.774  58.988  1.00 34.26  ? 84  ASP D O   1 
ATOM   6401 C CB  . ASP D  1 69  ? 31.390 -8.284  61.267  1.00 35.20  ? 84  ASP D CB  1 
ATOM   6402 C CG  . ASP D  1 69  ? 30.331 -7.587  62.106  1.00 35.35  ? 84  ASP D CG  1 
ATOM   6403 O OD1 . ASP D  1 69  ? 29.187 -7.418  61.630  1.00 34.08  ? 84  ASP D OD1 1 
ATOM   6404 O OD2 . ASP D  1 69  ? 30.664 -7.222  63.256  1.00 35.19  ? 84  ASP D OD2 1 
ATOM   6405 N N   . GLN D  1 70  ? 32.336 -7.775  58.041  1.00 38.65  ? 85  GLN D N   1 
ATOM   6406 C CA  . GLN D  1 70  ? 33.570 -7.516  57.259  1.00 38.34  ? 85  GLN D CA  1 
ATOM   6407 C C   . GLN D  1 70  ? 33.914 -6.036  57.465  1.00 36.87  ? 85  GLN D C   1 
ATOM   6408 O O   . GLN D  1 70  ? 33.467 -5.191  56.669  1.00 37.94  ? 85  GLN D O   1 
ATOM   6409 C CB  . GLN D  1 70  ? 33.355 -7.897  55.794  1.00 38.71  ? 85  GLN D CB  1 
ATOM   6410 C CG  . GLN D  1 70  ? 33.082 -9.382  55.585  1.00 42.78  ? 85  GLN D CG  1 
ATOM   6411 C CD  . GLN D  1 70  ? 32.891 -9.762  54.133  0.00 41.10  ? 85  GLN D CD  1 
ATOM   6412 O OE1 . GLN D  1 70  ? 32.258 -9.052  53.353  0.00 41.28  ? 85  GLN D OE1 1 
ATOM   6413 N NE2 . GLN D  1 70  ? 33.435 -10.909 53.760  0.00 41.16  ? 85  GLN D NE2 1 
ATOM   6414 N N   . LEU D  1 71  ? 34.649 -5.737  58.528  1.00 35.84  ? 86  LEU D N   1 
ATOM   6415 C CA  . LEU D  1 71  ? 34.845 -4.344  59.010  1.00 37.14  ? 86  LEU D CA  1 
ATOM   6416 C C   . LEU D  1 71  ? 35.895 -3.652  58.139  1.00 36.91  ? 86  LEU D C   1 
ATOM   6417 O O   . LEU D  1 71  ? 36.948 -4.267  57.879  1.00 36.01  ? 86  LEU D O   1 
ATOM   6418 C CB  . LEU D  1 71  ? 35.244 -4.380  60.488  1.00 36.89  ? 86  LEU D CB  1 
ATOM   6419 C CG  . LEU D  1 71  ? 34.198 -4.985  61.427  1.00 38.07  ? 86  LEU D CG  1 
ATOM   6420 C CD1 . LEU D  1 71  ? 34.670 -4.906  62.864  1.00 37.47  ? 86  LEU D CD1 1 
ATOM   6421 C CD2 . LEU D  1 71  ? 32.839 -4.308  61.280  1.00 37.58  ? 86  LEU D CD2 1 
ATOM   6422 N N   . LEU D  1 72  ? 35.613 -2.413  57.728  1.00 34.69  ? 87  LEU D N   1 
ATOM   6423 C CA  . LEU D  1 72  ? 36.475 -1.615  56.822  1.00 33.67  ? 87  LEU D CA  1 
ATOM   6424 C C   . LEU D  1 72  ? 37.106 -0.482  57.626  1.00 34.80  ? 87  LEU D C   1 
ATOM   6425 O O   . LEU D  1 72  ? 36.401 0.263   58.306  1.00 36.93  ? 87  LEU D O   1 
ATOM   6426 C CB  . LEU D  1 72  ? 35.643 -1.083  55.655  1.00 31.62  ? 87  LEU D CB  1 
ATOM   6427 C CG  . LEU D  1 72  ? 34.885 -2.139  54.851  1.00 32.61  ? 87  LEU D CG  1 
ATOM   6428 C CD1 . LEU D  1 72  ? 34.014 -1.475  53.806  1.00 32.14  ? 87  LEU D CD1 1 
ATOM   6429 C CD2 . LEU D  1 72  ? 35.838 -3.138  54.203  1.00 31.50  ? 87  LEU D CD2 1 
ATOM   6430 N N   . PRO D  1 73  ? 38.448 -0.325  57.576  1.00 32.92  ? 88  PRO D N   1 
ATOM   6431 C CA  . PRO D  1 73  ? 39.108 0.776   58.269  1.00 34.01  ? 88  PRO D CA  1 
ATOM   6432 C C   . PRO D  1 73  ? 38.894 2.117   57.543  1.00 31.81  ? 88  PRO D C   1 
ATOM   6433 O O   . PRO D  1 73  ? 38.582 2.116   56.368  1.00 30.94  ? 88  PRO D O   1 
ATOM   6434 C CB  . PRO D  1 73  ? 40.575 0.312   58.292  1.00 34.21  ? 88  PRO D CB  1 
ATOM   6435 C CG  . PRO D  1 73  ? 40.727 -0.481  57.018  1.00 34.39  ? 88  PRO D CG  1 
ATOM   6436 C CD  . PRO D  1 73  ? 39.401 -1.194  56.862  1.00 32.59  ? 88  PRO D CD  1 
ATOM   6437 N N   . VAL D  1 74  ? 39.054 3.217   58.283  1.00 32.56  ? 89  VAL D N   1 
ATOM   6438 C CA  . VAL D  1 74  ? 38.796 4.613   57.827  1.00 33.84  ? 89  VAL D CA  1 
ATOM   6439 C C   . VAL D  1 74  ? 40.144 5.333   57.733  1.00 32.22  ? 89  VAL D C   1 
ATOM   6440 O O   . VAL D  1 74  ? 40.909 5.257   58.706  1.00 32.46  ? 89  VAL D O   1 
ATOM   6441 C CB  . VAL D  1 74  ? 37.815 5.300   58.797  1.00 34.14  ? 89  VAL D CB  1 
ATOM   6442 C CG1 . VAL D  1 74  ? 37.658 6.787   58.536  1.00 36.55  ? 89  VAL D CG1 1 
ATOM   6443 C CG2 . VAL D  1 74  ? 36.459 4.621   58.748  1.00 34.83  ? 89  VAL D CG2 1 
ATOM   6444 N N   . SER D  1 75  ? 40.392 6.039   56.628  1.00 32.78  ? 90  SER D N   1 
ATOM   6445 C CA  . SER D  1 75  ? 41.615 6.857   56.399  1.00 35.10  ? 90  SER D CA  1 
ATOM   6446 C C   . SER D  1 75  ? 41.429 8.279   56.938  1.00 34.80  ? 90  SER D C   1 
ATOM   6447 O O   . SER D  1 75  ? 42.425 8.842   57.403  1.00 35.50  ? 90  SER D O   1 
ATOM   6448 C CB  . SER D  1 75  ? 42.004 6.886   54.942  1.00 34.13  ? 90  SER D CB  1 
ATOM   6449 O OG  . SER D  1 75  ? 40.950 7.424   54.163  1.00 38.28  ? 90  SER D OG  1 
ATOM   6450 N N   . ARG D  1 76  ? 40.221 8.840   56.864  1.00 35.94  ? 91  ARG D N   1 
ATOM   6451 C CA  . ARG D  1 76  ? 39.958 10.267  57.201  1.00 37.46  ? 91  ARG D CA  1 
ATOM   6452 C C   . ARG D  1 76  ? 38.558 10.448  57.808  1.00 33.85  ? 91  ARG D C   1 
ATOM   6453 O O   . ARG D  1 76  ? 37.608 9.860   57.279  1.00 29.13  ? 91  ARG D O   1 
ATOM   6454 C CB  . ARG D  1 76  ? 40.055 11.124  55.935  1.00 40.55  ? 91  ARG D CB  1 
ATOM   6455 C CG  . ARG D  1 76  ? 41.470 11.417  55.460  1.00 45.98  ? 91  ARG D CG  1 
ATOM   6456 C CD  . ARG D  1 76  ? 41.687 12.895  55.187  1.00 50.99  ? 91  ARG D CD  1 
ATOM   6457 N NE  . ARG D  1 76  ? 40.962 13.381  54.023  1.00 54.63  ? 91  ARG D NE  1 
ATOM   6458 C CZ  . ARG D  1 76  ? 40.852 14.666  53.665  1.00 55.39  ? 91  ARG D CZ  1 
ATOM   6459 N NH1 . ARG D  1 76  ? 41.393 15.628  54.399  1.00 54.03  ? 91  ARG D NH1 1 
ATOM   6460 N NH2 . ARG D  1 76  ? 40.176 14.986  52.574  1.00 54.62  ? 91  ARG D NH2 1 
ATOM   6461 N N   . ILE D  1 77  ? 38.456 11.249  58.872  1.00 36.18  ? 92  ILE D N   1 
ATOM   6462 C CA  . ILE D  1 77  ? 37.173 11.790  59.413  1.00 36.86  ? 92  ILE D CA  1 
ATOM   6463 C C   . ILE D  1 77  ? 37.157 13.288  59.102  1.00 35.95  ? 92  ILE D C   1 
ATOM   6464 O O   . ILE D  1 77  ? 38.071 13.994  59.560  1.00 35.62  ? 92  ILE D O   1 
ATOM   6465 C CB  . ILE D  1 77  ? 37.030 11.508  60.921  1.00 36.68  ? 92  ILE D CB  1 
ATOM   6466 C CG1 . ILE D  1 77  ? 36.963 10.007  61.218  1.00 39.69  ? 92  ILE D CG1 1 
ATOM   6467 C CG2 . ILE D  1 77  ? 35.824 12.237  61.494  1.00 38.86  ? 92  ILE D CG2 1 
ATOM   6468 C CD1 . ILE D  1 77  ? 37.281 9.641   62.658  1.00 40.26  ? 92  ILE D CD1 1 
ATOM   6469 N N   . ILE D  1 78  ? 36.148 13.751  58.370  1.00 35.67  ? 93  ILE D N   1 
ATOM   6470 C CA  . ILE D  1 78  ? 35.957 15.190  58.032  1.00 36.66  ? 93  ILE D CA  1 
ATOM   6471 C C   . ILE D  1 78  ? 34.627 15.638  58.636  1.00 35.99  ? 93  ILE D C   1 
ATOM   6472 O O   . ILE D  1 78  ? 33.567 15.157  58.186  1.00 34.09  ? 93  ILE D O   1 
ATOM   6473 C CB  . ILE D  1 78  ? 36.045 15.429  56.517  1.00 38.34  ? 93  ILE D CB  1 
ATOM   6474 C CG1 . ILE D  1 78  ? 37.311 14.775  55.951  1.00 41.31  ? 93  ILE D CG1 1 
ATOM   6475 C CG2 . ILE D  1 78  ? 35.985 16.921  56.205  1.00 37.49  ? 93  ILE D CG2 1 
ATOM   6476 C CD1 . ILE D  1 78  ? 37.493 14.931  54.476  1.00 43.58  ? 93  ILE D CD1 1 
ATOM   6477 N N   . VAL D  1 79  ? 34.704 16.506  59.638  1.00 34.62  ? 94  VAL D N   1 
ATOM   6478 C CA  . VAL D  1 79  ? 33.524 17.011  60.392  1.00 35.24  ? 94  VAL D CA  1 
ATOM   6479 C C   . VAL D  1 79  ? 33.330 18.465  59.977  1.00 35.24  ? 94  VAL D C   1 
ATOM   6480 O O   . VAL D  1 79  ? 34.342 19.201  59.880  1.00 34.64  ? 94  VAL D O   1 
ATOM   6481 C CB  . VAL D  1 79  ? 33.722 16.856  61.909  1.00 35.22  ? 94  VAL D CB  1 
ATOM   6482 C CG1 . VAL D  1 79  ? 32.575 17.475  62.687  1.00 35.20  ? 94  VAL D CG1 1 
ATOM   6483 C CG2 . VAL D  1 79  ? 33.914 15.398  62.306  1.00 36.38  ? 94  VAL D CG2 1 
ATOM   6484 N N   . HIS D  1 80  ? 32.084 18.863  59.725  1.00 34.14  ? 95  HIS D N   1 
ATOM   6485 C CA  . HIS D  1 80  ? 31.759 20.247  59.307  1.00 32.77  ? 95  HIS D CA  1 
ATOM   6486 C C   . HIS D  1 80  ? 32.359 21.203  60.334  1.00 31.94  ? 95  HIS D C   1 
ATOM   6487 O O   . HIS D  1 80  ? 32.099 21.057  61.525  1.00 31.53  ? 95  HIS D O   1 
ATOM   6488 C CB  . HIS D  1 80  ? 30.255 20.445  59.100  1.00 33.07  ? 95  HIS D CB  1 
ATOM   6489 C CG  . HIS D  1 80  ? 29.965 21.602  58.211  1.00 32.78  ? 95  HIS D CG  1 
ATOM   6490 N ND1 . HIS D  1 80  ? 30.141 22.902  58.633  1.00 33.97  ? 95  HIS D ND1 1 
ATOM   6491 C CD2 . HIS D  1 80  ? 29.573 21.666  56.921  1.00 33.02  ? 95  HIS D CD2 1 
ATOM   6492 C CE1 . HIS D  1 80  ? 29.853 23.724  57.646  1.00 33.60  ? 95  HIS D CE1 1 
ATOM   6493 N NE2 . HIS D  1 80  ? 29.506 22.989  56.582  1.00 33.12  ? 95  HIS D NE2 1 
ATOM   6494 N N   . PRO D  1 81  ? 33.182 22.197  59.920  1.00 30.98  ? 96  PRO D N   1 
ATOM   6495 C CA  . PRO D  1 81  ? 33.852 23.077  60.881  1.00 32.40  ? 96  PRO D CA  1 
ATOM   6496 C C   . PRO D  1 81  ? 32.898 23.973  61.696  1.00 32.36  ? 96  PRO D C   1 
ATOM   6497 O O   . PRO D  1 81  ? 33.326 24.517  62.685  1.00 34.06  ? 96  PRO D O   1 
ATOM   6498 C CB  . PRO D  1 81  ? 34.814 23.902  60.000  1.00 31.28  ? 96  PRO D CB  1 
ATOM   6499 C CG  . PRO D  1 81  ? 34.192 23.883  58.627  1.00 32.31  ? 96  PRO D CG  1 
ATOM   6500 C CD  . PRO D  1 81  ? 33.510 22.532  58.524  1.00 31.99  ? 96  PRO D CD  1 
ATOM   6501 N N   . GLN D  1 82  ? 31.639 24.112  61.274  1.00 34.14  ? 97  GLN D N   1 
ATOM   6502 C CA  . GLN D  1 82  ? 30.592 24.870  62.008  1.00 36.41  ? 97  GLN D CA  1 
ATOM   6503 C C   . GLN D  1 82  ? 29.999 24.024  63.142  1.00 36.30  ? 97  GLN D C   1 
ATOM   6504 O O   . GLN D  1 82  ? 29.275 24.603  63.973  1.00 37.48  ? 97  GLN D O   1 
ATOM   6505 C CB  . GLN D  1 82  ? 29.501 25.329  61.042  1.00 39.00  ? 97  GLN D CB  1 
ATOM   6506 C CG  . GLN D  1 82  ? 29.978 26.377  60.046  1.00 41.86  ? 97  GLN D CG  1 
ATOM   6507 C CD  . GLN D  1 82  ? 30.069 27.766  60.633  1.00 46.15  ? 97  GLN D CD  1 
ATOM   6508 O OE1 . GLN D  1 82  ? 29.379 28.113  61.592  1.00 49.67  ? 97  GLN D OE1 1 
ATOM   6509 N NE2 . GLN D  1 82  ? 30.939 28.583  60.066  1.00 50.87  ? 97  GLN D NE2 1 
ATOM   6510 N N   . PHE D  1 83  ? 30.284 22.718  63.201  1.00 33.90  ? 98  PHE D N   1 
ATOM   6511 C CA  . PHE D  1 83  ? 29.661 21.804  64.184  1.00 33.60  ? 98  PHE D CA  1 
ATOM   6512 C C   . PHE D  1 83  ? 30.311 21.945  65.560  1.00 32.91  ? 98  PHE D C   1 
ATOM   6513 O O   . PHE D  1 83  ? 31.539 21.806  65.688  1.00 33.11  ? 98  PHE D O   1 
ATOM   6514 C CB  . PHE D  1 83  ? 29.731 20.331  63.790  1.00 32.58  ? 98  PHE D CB  1 
ATOM   6515 C CG  . PHE D  1 83  ? 29.134 19.434  64.842  1.00 30.91  ? 98  PHE D CG  1 
ATOM   6516 C CD1 . PHE D  1 83  ? 27.758 19.378  65.027  1.00 31.34  ? 98  PHE D CD1 1 
ATOM   6517 C CD2 . PHE D  1 83  ? 29.947 18.682  65.681  1.00 31.05  ? 98  PHE D CD2 1 
ATOM   6518 C CE1 . PHE D  1 83  ? 27.207 18.560  66.000  1.00 30.41  ? 98  PHE D CE1 1 
ATOM   6519 C CE2 . PHE D  1 83  ? 29.393 17.880  66.666  1.00 31.28  ? 98  PHE D CE2 1 
ATOM   6520 C CZ  . PHE D  1 83  ? 28.026 17.819  66.821  1.00 31.19  ? 98  PHE D CZ  1 
ATOM   6521 N N   . TYR D  1 84  ? 29.465 22.155  66.567  1.00 30.96  ? 99  TYR D N   1 
ATOM   6522 C CA  . TYR D  1 84  ? 29.807 21.924  67.988  1.00 32.10  ? 99  TYR D CA  1 
ATOM   6523 C C   . TYR D  1 84  ? 28.718 21.078  68.662  1.00 31.22  ? 99  TYR D C   1 
ATOM   6524 O O   . TYR D  1 84  ? 29.103 20.111  69.331  1.00 31.03  ? 99  TYR D O   1 
ATOM   6525 C CB  . TYR D  1 84  ? 30.117 23.234  68.719  1.00 32.20  ? 99  TYR D CB  1 
ATOM   6526 C CG  . TYR D  1 84  ? 30.677 22.949  70.085  1.00 33.19  ? 99  TYR D CG  1 
ATOM   6527 C CD1 . TYR D  1 84  ? 31.918 22.342  70.222  1.00 33.06  ? 99  TYR D CD1 1 
ATOM   6528 C CD2 . TYR D  1 84  ? 29.919 23.151  71.230  1.00 32.62  ? 99  TYR D CD2 1 
ATOM   6529 C CE1 . TYR D  1 84  ? 32.414 21.991  71.468  1.00 33.05  ? 99  TYR D CE1 1 
ATOM   6530 C CE2 . TYR D  1 84  ? 30.404 22.812  72.482  1.00 34.14  ? 99  TYR D CE2 1 
ATOM   6531 C CZ  . TYR D  1 84  ? 31.653 22.228  72.601  1.00 34.19  ? 99  TYR D CZ  1 
ATOM   6532 O OH  . TYR D  1 84  ? 32.124 21.903  73.838  1.00 34.04  ? 99  TYR D OH  1 
ATOM   6533 N N   . THR D  1 85  ? 27.427 21.403  68.501  1.00 32.24  ? 100 THR D N   1 
ATOM   6534 C CA  . THR D  1 85  ? 26.296 20.556  68.990  1.00 33.20  ? 100 THR D CA  1 
ATOM   6535 C C   . THR D  1 85  ? 25.229 20.416  67.903  1.00 31.26  ? 100 THR D C   1 
ATOM   6536 O O   . THR D  1 85  ? 25.148 21.302  67.040  1.00 29.56  ? 100 THR D O   1 
ATOM   6537 C CB  . THR D  1 85  ? 25.649 21.088  70.278  1.00 33.57  ? 100 THR D CB  1 
ATOM   6538 O OG1 . THR D  1 85  ? 24.841 22.218  69.957  1.00 34.36  ? 100 THR D OG1 1 
ATOM   6539 C CG2 . THR D  1 85  ? 26.654 21.475  71.337  1.00 33.73  ? 100 THR D CG2 1 
ATOM   6540 N N   . ALA D  1 86  ? 24.437 19.338  67.967  1.00 30.70  ? 101 ALA D N   1 
ATOM   6541 C CA  . ALA D  1 86  ? 23.339 19.037  67.017  1.00 31.06  ? 101 ALA D CA  1 
ATOM   6542 C C   . ALA D  1 86  ? 22.286 20.151  67.052  1.00 31.27  ? 101 ALA D C   1 
ATOM   6543 O O   . ALA D  1 86  ? 21.752 20.468  65.975  1.00 34.65  ? 101 ALA D O   1 
ATOM   6544 C CB  . ALA D  1 86  ? 22.726 17.697  67.328  1.00 30.61  ? 101 ALA D CB  1 
ATOM   6545 N N   . GLN D  1 87  ? 22.019 20.739  68.225  1.00 31.49  ? 102 GLN D N   1 
ATOM   6546 C CA  . GLN D  1 87  ? 20.943 21.754  68.412  1.00 33.49  ? 102 GLN D CA  1 
ATOM   6547 C C   . GLN D  1 87  ? 21.372 23.086  67.784  1.00 34.09  ? 102 GLN D C   1 
ATOM   6548 O O   . GLN D  1 87  ? 20.485 23.834  67.355  1.00 37.47  ? 102 GLN D O   1 
ATOM   6549 C CB  . GLN D  1 87  ? 20.588 21.970  69.885  1.00 33.85  ? 102 GLN D CB  1 
ATOM   6550 C CG  . GLN D  1 87  ? 19.887 20.791  70.539  1.00 35.10  ? 102 GLN D CG  1 
ATOM   6551 C CD  . GLN D  1 87  ? 20.787 19.642  70.929  1.00 37.07  ? 102 GLN D CD  1 
ATOM   6552 O OE1 . GLN D  1 87  ? 20.399 18.479  70.824  1.00 42.34  ? 102 GLN D OE1 1 
ATOM   6553 N NE2 . GLN D  1 87  ? 22.001 19.942  71.363  1.00 34.33  ? 102 GLN D NE2 1 
ATOM   6554 N N   . ILE D  1 88  ? 22.673 23.381  67.736  1.00 34.16  ? 103 ILE D N   1 
ATOM   6555 C CA  . ILE D  1 88  ? 23.210 24.582  67.031  1.00 34.94  ? 103 ILE D CA  1 
ATOM   6556 C C   . ILE D  1 88  ? 23.169 24.314  65.517  1.00 35.37  ? 103 ILE D C   1 
ATOM   6557 O O   . ILE D  1 88  ? 22.762 25.226  64.772  1.00 34.91  ? 103 ILE D O   1 
ATOM   6558 C CB  . ILE D  1 88  ? 24.610 24.954  67.558  1.00 35.71  ? 103 ILE D CB  1 
ATOM   6559 C CG1 . ILE D  1 88  ? 24.545 25.385  69.026  1.00 36.74  ? 103 ILE D CG1 1 
ATOM   6560 C CG2 . ILE D  1 88  ? 25.256 26.025  66.682  1.00 37.90  ? 103 ILE D CG2 1 
ATOM   6561 C CD1 . ILE D  1 88  ? 25.872 25.389  69.756  1.00 36.59  ? 103 ILE D CD1 1 
ATOM   6562 N N   . GLY D  1 89  ? 23.594 23.122  65.083  1.00 34.76  ? 104 GLY D N   1 
ATOM   6563 C CA  . GLY D  1 89  ? 23.458 22.630  63.698  1.00 33.62  ? 104 GLY D CA  1 
ATOM   6564 C C   . GLY D  1 89  ? 24.794 22.275  63.065  1.00 33.12  ? 104 GLY D C   1 
ATOM   6565 O O   . GLY D  1 89  ? 25.775 22.127  63.806  1.00 33.45  ? 104 GLY D O   1 
ATOM   6566 N N   . ALA D  1 90  ? 24.813 22.156  61.732  1.00 33.06  ? 105 ALA D N   1 
ATOM   6567 C CA  . ALA D  1 90  ? 25.926 21.624  60.905  1.00 31.05  ? 105 ALA D CA  1 
ATOM   6568 C C   . ALA D  1 90  ? 26.277 20.203  61.368  1.00 29.21  ? 105 ALA D C   1 
ATOM   6569 O O   . ALA D  1 90  ? 27.475 19.848  61.348  1.00 28.40  ? 105 ALA D O   1 
ATOM   6570 C CB  . ALA D  1 90  ? 27.105 22.567  60.952  1.00 32.93  ? 105 ALA D CB  1 
ATOM   6571 N N   . ASP D  1 91  ? 25.262 19.403  61.724  1.00 27.10  ? 106 ASP D N   1 
ATOM   6572 C CA  . ASP D  1 91  ? 25.445 18.022  62.247  1.00 29.23  ? 106 ASP D CA  1 
ATOM   6573 C C   . ASP D  1 91  ? 25.636 17.082  61.051  1.00 29.20  ? 106 ASP D C   1 
ATOM   6574 O O   . ASP D  1 91  ? 24.702 16.343  60.687  1.00 30.72  ? 106 ASP D O   1 
ATOM   6575 C CB  . ASP D  1 91  ? 24.323 17.622  63.209  1.00 28.98  ? 106 ASP D CB  1 
ATOM   6576 C CG  . ASP D  1 91  ? 24.608 16.333  63.965  1.00 29.33  ? 106 ASP D CG  1 
ATOM   6577 O OD1 . ASP D  1 91  ? 25.777 15.888  63.965  1.00 29.32  ? 106 ASP D OD1 1 
ATOM   6578 O OD2 . ASP D  1 91  ? 23.666 15.790  64.560  1.00 29.82  ? 106 ASP D OD2 1 
ATOM   6579 N N   . ILE D  1 92  ? 26.822 17.145  60.445  1.00 30.04  ? 107 ILE D N   1 
ATOM   6580 C CA  . ILE D  1 92  ? 27.171 16.388  59.209  1.00 30.96  ? 107 ILE D CA  1 
ATOM   6581 C C   . ILE D  1 92  ? 28.674 16.122  59.208  1.00 30.49  ? 107 ILE D C   1 
ATOM   6582 O O   . ILE D  1 92  ? 29.452 17.033  59.596  1.00 29.24  ? 107 ILE D O   1 
ATOM   6583 C CB  . ILE D  1 92  ? 26.666 17.139  57.960  1.00 31.02  ? 107 ILE D CB  1 
ATOM   6584 C CG1 . ILE D  1 92  ? 26.612 16.228  56.733  1.00 32.74  ? 107 ILE D CG1 1 
ATOM   6585 C CG2 . ILE D  1 92  ? 27.457 18.413  57.697  1.00 31.91  ? 107 ILE D CG2 1 
ATOM   6586 C CD1 . ILE D  1 92  ? 25.741 16.755  55.616  1.00 32.23  ? 107 ILE D CD1 1 
ATOM   6587 N N   . ALA D  1 93  ? 29.060 14.898  58.836  1.00 31.03  ? 108 ALA D N   1 
ATOM   6588 C CA  . ALA D  1 93  ? 30.471 14.459  58.738  1.00 30.65  ? 108 ALA D CA  1 
ATOM   6589 C C   . ALA D  1 93  ? 30.631 13.460  57.587  1.00 30.57  ? 108 ALA D C   1 
ATOM   6590 O O   . ALA D  1 93  ? 29.627 12.860  57.150  1.00 30.59  ? 108 ALA D O   1 
ATOM   6591 C CB  . ALA D  1 93  ? 30.919 13.882  60.056  1.00 30.12  ? 108 ALA D CB  1 
ATOM   6592 N N   . LEU D  1 94  ? 31.872 13.300  57.131  1.00 31.90  ? 109 LEU D N   1 
ATOM   6593 C CA  . LEU D  1 94  ? 32.279 12.387  56.038  1.00 31.80  ? 109 LEU D CA  1 
ATOM   6594 C C   . LEU D  1 94  ? 33.349 11.438  56.574  1.00 31.59  ? 109 LEU D C   1 
ATOM   6595 O O   . LEU D  1 94  ? 34.246 11.908  57.298  1.00 30.59  ? 109 LEU D O   1 
ATOM   6596 C CB  . LEU D  1 94  ? 32.797 13.220  54.864  1.00 32.85  ? 109 LEU D CB  1 
ATOM   6597 C CG  . LEU D  1 94  ? 31.752 14.058  54.127  1.00 32.11  ? 109 LEU D CG  1 
ATOM   6598 C CD1 . LEU D  1 94  ? 32.422 15.077  53.218  1.00 33.20  ? 109 LEU D CD1 1 
ATOM   6599 C CD2 . LEU D  1 94  ? 30.799 13.175  53.338  1.00 32.34  ? 109 LEU D CD2 1 
ATOM   6600 N N   . LEU D  1 95  ? 33.224 10.144  56.269  1.00 32.71  ? 110 LEU D N   1 
ATOM   6601 C CA  . LEU D  1 95  ? 34.291 9.138   56.510  1.00 33.47  ? 110 LEU D CA  1 
ATOM   6602 C C   . LEU D  1 95  ? 34.876 8.737   55.159  1.00 32.70  ? 110 LEU D C   1 
ATOM   6603 O O   . LEU D  1 95  ? 34.092 8.295   54.292  1.00 31.64  ? 110 LEU D O   1 
ATOM   6604 C CB  . LEU D  1 95  ? 33.718 7.921   57.245  1.00 33.53  ? 110 LEU D CB  1 
ATOM   6605 C CG  . LEU D  1 95  ? 32.848 8.216   58.466  1.00 34.41  ? 110 LEU D CG  1 
ATOM   6606 C CD1 . LEU D  1 95  ? 32.403 6.915   59.123  1.00 36.28  ? 110 LEU D CD1 1 
ATOM   6607 C CD2 . LEU D  1 95  ? 33.574 9.097   59.474  1.00 33.95  ? 110 LEU D CD2 1 
ATOM   6608 N N   . GLU D  1 96  ? 36.192 8.872   54.989  1.00 32.64  ? 111 GLU D N   1 
ATOM   6609 C CA  . GLU D  1 96  ? 36.887 8.292   53.815  1.00 34.16  ? 111 GLU D CA  1 
ATOM   6610 C C   . GLU D  1 96  ? 37.384 6.898   54.198  1.00 34.26  ? 111 GLU D C   1 
ATOM   6611 O O   . GLU D  1 96  ? 38.178 6.793   55.152  1.00 36.10  ? 111 GLU D O   1 
ATOM   6612 C CB  . GLU D  1 96  ? 38.040 9.145   53.282  1.00 34.58  ? 111 GLU D CB  1 
ATOM   6613 C CG  . GLU D  1 96  ? 38.425 8.709   51.875  1.00 35.79  ? 111 GLU D CG  1 
ATOM   6614 C CD  . GLU D  1 96  ? 39.515 9.491   51.176  1.00 37.51  ? 111 GLU D CD  1 
ATOM   6615 O OE1 . GLU D  1 96  ? 40.218 10.272  51.842  1.00 37.89  ? 111 GLU D OE1 1 
ATOM   6616 O OE2 . GLU D  1 96  ? 39.627 9.320   49.954  1.00 41.79  ? 111 GLU D OE2 1 
ATOM   6617 N N   . LEU D  1 97  ? 36.967 5.884   53.442  1.00 34.40  ? 112 LEU D N   1 
ATOM   6618 C CA  . LEU D  1 97  ? 37.468 4.496   53.600  1.00 34.75  ? 112 LEU D CA  1 
ATOM   6619 C C   . LEU D  1 97  ? 38.886 4.435   53.019  1.00 34.12  ? 112 LEU D C   1 
ATOM   6620 O O   . LEU D  1 97  ? 39.216 5.263   52.150  1.00 36.58  ? 112 LEU D O   1 
ATOM   6621 C CB  . LEU D  1 97  ? 36.519 3.527   52.884  1.00 33.43  ? 112 LEU D CB  1 
ATOM   6622 C CG  . LEU D  1 97  ? 35.058 3.571   53.314  1.00 33.92  ? 112 LEU D CG  1 
ATOM   6623 C CD1 . LEU D  1 97  ? 34.233 2.618   52.467  1.00 34.39  ? 112 LEU D CD1 1 
ATOM   6624 C CD2 . LEU D  1 97  ? 34.903 3.239   54.791  1.00 35.26  ? 112 LEU D CD2 1 
ATOM   6625 N N   . GLU D  1 98  ? 39.703 3.508   53.510  1.00 35.35  ? 113 GLU D N   1 
ATOM   6626 C CA  . GLU D  1 98  ? 41.097 3.287   53.037  1.00 36.25  ? 113 GLU D CA  1 
ATOM   6627 C C   . GLU D  1 98  ? 41.088 2.744   51.608  1.00 34.43  ? 113 GLU D C   1 
ATOM   6628 O O   . GLU D  1 98  ? 42.087 2.968   50.893  1.00 34.86  ? 113 GLU D O   1 
ATOM   6629 C CB  . GLU D  1 98  ? 41.829 2.302   53.946  1.00 35.34  ? 113 GLU D CB  1 
ATOM   6630 C CG  . GLU D  1 98  ? 42.145 2.864   55.315  1.00 35.89  ? 113 GLU D CG  1 
ATOM   6631 C CD  . GLU D  1 98  ? 43.019 1.960   56.162  1.00 34.83  ? 113 GLU D CD  1 
ATOM   6632 O OE1 . GLU D  1 98  ? 43.447 0.905   55.655  1.00 35.81  ? 113 GLU D OE1 1 
ATOM   6633 O OE2 . GLU D  1 98  ? 43.256 2.310   57.331  1.00 36.63  ? 113 GLU D OE2 1 
ATOM   6634 N N   . GLU D  1 99  ? 40.034 2.012   51.237  1.00 33.91  ? 114 GLU D N   1 
ATOM   6635 C CA  . GLU D  1 99  ? 39.847 1.436   49.889  1.00 35.82  ? 114 GLU D CA  1 
ATOM   6636 C C   . GLU D  1 99  ? 38.435 1.746   49.410  1.00 36.38  ? 114 GLU D C   1 
ATOM   6637 O O   . GLU D  1 99  ? 37.506 1.833   50.214  1.00 35.71  ? 114 GLU D O   1 
ATOM   6638 C CB  . GLU D  1 99  ? 40.042 -0.087  49.875  1.00 35.22  ? 114 GLU D CB  1 
ATOM   6639 C CG  . GLU D  1 99  ? 41.343 -0.566  50.498  1.00 34.71  ? 114 GLU D CG  1 
ATOM   6640 C CD  . GLU D  1 99  ? 42.625 -0.175  49.783  1.00 33.65  ? 114 GLU D CD  1 
ATOM   6641 O OE1 . GLU D  1 99  ? 42.545 0.335   48.656  1.00 34.39  ? 114 GLU D OE1 1 
ATOM   6642 O OE2 . GLU D  1 99  ? 43.697 -0.388  50.362  1.00 34.16  ? 114 GLU D OE2 1 
ATOM   6643 N N   . PRO D  1 100 ? 38.237 1.895   48.084  1.00 38.24  ? 115 PRO D N   1 
ATOM   6644 C CA  . PRO D  1 100 ? 36.896 1.961   47.516  1.00 39.57  ? 115 PRO D CA  1 
ATOM   6645 C C   . PRO D  1 100 ? 36.269 0.566   47.624  1.00 40.37  ? 115 PRO D C   1 
ATOM   6646 O O   . PRO D  1 100 ? 36.979 -0.409  47.499  1.00 40.01  ? 115 PRO D O   1 
ATOM   6647 C CB  . PRO D  1 100 ? 37.127 2.387   46.064  1.00 39.39  ? 115 PRO D CB  1 
ATOM   6648 C CG  . PRO D  1 100 ? 38.516 1.863   45.753  1.00 39.57  ? 115 PRO D CG  1 
ATOM   6649 C CD  . PRO D  1 100 ? 39.284 1.979   47.052  1.00 39.77  ? 115 PRO D CD  1 
ATOM   6650 N N   . VAL D  1 101 ? 34.979 0.506   47.932  1.00 38.30  ? 116 VAL D N   1 
ATOM   6651 C CA  . VAL D  1 101 ? 34.231 -0.782  48.009  1.00 39.66  ? 116 VAL D CA  1 
ATOM   6652 C C   . VAL D  1 101 ? 33.811 -1.152  46.583  1.00 37.70  ? 116 VAL D C   1 
ATOM   6653 O O   . VAL D  1 101 ? 33.621 -0.230  45.763  1.00 37.07  ? 116 VAL D O   1 
ATOM   6654 C CB  . VAL D  1 101 ? 33.034 -0.704  48.982  1.00 41.41  ? 116 VAL D CB  1 
ATOM   6655 C CG1 . VAL D  1 101 ? 33.458 -0.177  50.349  1.00 41.76  ? 116 VAL D CG1 1 
ATOM   6656 C CG2 . VAL D  1 101 ? 31.867 0.099   48.423  1.00 40.44  ? 116 VAL D CG2 1 
ATOM   6657 N N   . LYS D  1 102 ? 33.644 -2.448  46.322  1.00 38.21  ? 117 LYS D N   1 
ATOM   6658 C CA  . LYS D  1 102 ? 32.995 -2.995  45.111  1.00 40.17  ? 117 LYS D CA  1 
ATOM   6659 C C   . LYS D  1 102 ? 31.481 -2.894  45.309  1.00 41.16  ? 117 LYS D C   1 
ATOM   6660 O O   . LYS D  1 102 ? 30.971 -3.501  46.257  1.00 41.27  ? 117 LYS D O   1 
ATOM   6661 C CB  . LYS D  1 102 ? 33.437 -4.441  44.869  1.00 42.81  ? 117 LYS D CB  1 
ATOM   6662 C CG  . LYS D  1 102 ? 34.654 -4.599  43.968  1.00 45.75  ? 117 LYS D CG  1 
ATOM   6663 C CD  . LYS D  1 102 ? 35.874 -3.795  44.367  1.00 48.62  ? 117 LYS D CD  1 
ATOM   6664 C CE  . LYS D  1 102 ? 36.940 -3.829  43.294  1.00 52.56  ? 117 LYS D CE  1 
ATOM   6665 N NZ  . LYS D  1 102 ? 38.238 -3.292  43.758  1.00 56.33  ? 117 LYS D NZ  1 
ATOM   6666 N N   . VAL D  1 103 ? 30.797 -2.157  44.440  1.00 41.12  ? 118 VAL D N   1 
ATOM   6667 C CA  . VAL D  1 103 ? 29.318 -1.966  44.504  1.00 40.77  ? 118 VAL D CA  1 
ATOM   6668 C C   . VAL D  1 103 ? 28.630 -3.148  43.814  1.00 41.28  ? 118 VAL D C   1 
ATOM   6669 O O   . VAL D  1 103 ? 29.257 -3.813  42.981  1.00 41.14  ? 118 VAL D O   1 
ATOM   6670 C CB  . VAL D  1 103 ? 28.865 -0.601  43.951  1.00 42.52  ? 118 VAL D CB  1 
ATOM   6671 C CG1 . VAL D  1 103 ? 29.508 0.547   44.723  1.00 44.23  ? 118 VAL D CG1 1 
ATOM   6672 C CG2 . VAL D  1 103 ? 29.096 -0.444  42.457  1.00 43.41  ? 118 VAL D CG2 1 
ATOM   6673 N N   . SER D  1 104 ? 27.373 -3.392  44.188  1.00 41.56  ? 119 SER D N   1 
ATOM   6674 C CA  . SER D  1 104 ? 26.492 -4.481  43.693  1.00 43.20  ? 119 SER D CA  1 
ATOM   6675 C C   . SER D  1 104 ? 25.032 -4.053  43.886  1.00 43.15  ? 119 SER D C   1 
ATOM   6676 O O   . SER D  1 104 ? 24.814 -2.938  44.376  1.00 41.97  ? 119 SER D O   1 
ATOM   6677 C CB  . SER D  1 104 ? 26.786 -5.782  44.400  1.00 42.16  ? 119 SER D CB  1 
ATOM   6678 O OG  . SER D  1 104 ? 26.628 -5.645  45.802  1.00 43.24  ? 119 SER D OG  1 
ATOM   6679 N N   . SER D  1 105 ? 24.073 -4.897  43.506  1.00 43.53  ? 120 SER D N   1 
ATOM   6680 C CA  . SER D  1 105 ? 22.621 -4.652  43.710  1.00 47.37  ? 120 SER D CA  1 
ATOM   6681 C C   . SER D  1 105 ? 22.310 -4.581  45.214  1.00 45.40  ? 120 SER D C   1 
ATOM   6682 O O   . SER D  1 105 ? 21.425 -3.792  45.591  1.00 47.53  ? 120 SER D O   1 
ATOM   6683 C CB  . SER D  1 105 ? 21.785 -5.702  43.011  1.00 48.81  ? 120 SER D CB  1 
ATOM   6684 O OG  . SER D  1 105 ? 21.945 -6.967  43.635  1.00 50.10  ? 120 SER D OG  1 
ATOM   6685 N N   . HIS D  1 106 ? 23.026 -5.363  46.032  1.00 44.79  ? 121 HIS D N   1 
ATOM   6686 C CA  . HIS D  1 106 ? 22.822 -5.512  47.499  1.00 44.14  ? 121 HIS D CA  1 
ATOM   6687 C C   . HIS D  1 106 ? 23.577 -4.427  48.284  1.00 43.06  ? 121 HIS D C   1 
ATOM   6688 O O   . HIS D  1 106 ? 23.137 -4.123  49.405  1.00 45.61  ? 121 HIS D O   1 
ATOM   6689 C CB  . HIS D  1 106 ? 23.230 -6.925  47.949  1.00 45.31  ? 121 HIS D CB  1 
ATOM   6690 C CG  . HIS D  1 106 ? 22.845 -7.279  49.342  0.00 44.83  ? 121 HIS D CG  1 
ATOM   6691 N ND1 . HIS D  1 106 ? 21.557 -7.644  49.682  0.00 44.82  ? 121 HIS D ND1 1 
ATOM   6692 C CD2 . HIS D  1 106 ? 23.569 -7.339  50.481  0.00 44.86  ? 121 HIS D CD2 1 
ATOM   6693 C CE1 . HIS D  1 106 ? 21.501 -7.899  50.974  0.00 44.81  ? 121 HIS D CE1 1 
ATOM   6694 N NE2 . HIS D  1 106 ? 22.723 -7.721  51.487  0.00 44.82  ? 121 HIS D NE2 1 
ATOM   6695 N N   . VAL D  1 107 ? 24.680 -3.894  47.748  1.00 40.31  ? 122 VAL D N   1 
ATOM   6696 C CA  . VAL D  1 107 ? 25.505 -2.827  48.396  1.00 39.53  ? 122 VAL D CA  1 
ATOM   6697 C C   . VAL D  1 107 ? 25.878 -1.779  47.341  1.00 38.00  ? 122 VAL D C   1 
ATOM   6698 O O   . VAL D  1 107 ? 26.718 -2.084  46.490  1.00 36.72  ? 122 VAL D O   1 
ATOM   6699 C CB  . VAL D  1 107 ? 26.764 -3.417  49.062  1.00 44.03  ? 122 VAL D CB  1 
ATOM   6700 C CG1 . VAL D  1 107 ? 27.675 -2.332  49.612  1.00 44.92  ? 122 VAL D CG1 1 
ATOM   6701 C CG2 . VAL D  1 107 ? 26.422 -4.421  50.153  1.00 46.96  ? 122 VAL D CG2 1 
ATOM   6702 N N   . HIS D  1 108 ? 25.306 -0.578  47.414  1.00 35.69  ? 123 HIS D N   1 
ATOM   6703 C CA  . HIS D  1 108 ? 25.628 0.540   46.490  1.00 35.67  ? 123 HIS D CA  1 
ATOM   6704 C C   . HIS D  1 108 ? 25.220 1.887   47.094  1.00 35.16  ? 123 HIS D C   1 
ATOM   6705 O O   . HIS D  1 108 ? 24.572 1.907   48.155  1.00 34.64  ? 123 HIS D O   1 
ATOM   6706 C CB  . HIS D  1 108 ? 25.054 0.290   45.083  1.00 38.49  ? 123 HIS D CB  1 
ATOM   6707 C CG  . HIS D  1 108 ? 23.569 0.312   44.941  1.00 37.90  ? 123 HIS D CG  1 
ATOM   6708 N ND1 . HIS D  1 108 ? 22.836 -0.839  44.714  1.00 40.15  ? 123 HIS D ND1 1 
ATOM   6709 C CD2 . HIS D  1 108 ? 22.689 1.334   44.887  1.00 37.72  ? 123 HIS D CD2 1 
ATOM   6710 C CE1 . HIS D  1 108 ? 21.560 -0.528  44.574  1.00 40.78  ? 123 HIS D CE1 1 
ATOM   6711 N NE2 . HIS D  1 108 ? 21.444 0.802   44.674  1.00 41.90  ? 123 HIS D NE2 1 
ATOM   6712 N N   . THR D  1 109 ? 25.616 2.965   46.423  1.00 33.64  ? 124 THR D N   1 
ATOM   6713 C CA  . THR D  1 109 ? 25.544 4.360   46.921  1.00 34.79  ? 124 THR D CA  1 
ATOM   6714 C C   . THR D  1 109 ? 24.102 4.873   46.867  1.00 33.33  ? 124 THR D C   1 
ATOM   6715 O O   . THR D  1 109 ? 23.316 4.363   46.054  1.00 35.32  ? 124 THR D O   1 
ATOM   6716 C CB  . THR D  1 109 ? 26.464 5.295   46.127  1.00 32.22  ? 124 THR D CB  1 
ATOM   6717 O OG1 . THR D  1 109 ? 25.999 5.303   44.778  1.00 35.25  ? 124 THR D OG1 1 
ATOM   6718 C CG2 . THR D  1 109 ? 27.917 4.887   46.170  1.00 33.25  ? 124 THR D CG2 1 
ATOM   6719 N N   . VAL D  1 110 ? 23.789 5.850   47.716  1.00 34.46  ? 125 VAL D N   1 
ATOM   6720 C CA  . VAL D  1 110 ? 22.524 6.637   47.666  1.00 34.05  ? 125 VAL D CA  1 
ATOM   6721 C C   . VAL D  1 110 ? 22.810 7.901   46.853  1.00 33.93  ? 125 VAL D C   1 
ATOM   6722 O O   . VAL D  1 110 ? 23.947 8.410   46.907  1.00 33.48  ? 125 VAL D O   1 
ATOM   6723 C CB  . VAL D  1 110 ? 21.973 6.951   49.072  1.00 32.72  ? 125 VAL D CB  1 
ATOM   6724 C CG1 . VAL D  1 110 ? 22.821 7.960   49.833  1.00 32.31  ? 125 VAL D CG1 1 
ATOM   6725 C CG2 . VAL D  1 110 ? 20.517 7.401   49.016  1.00 31.14  ? 125 VAL D CG2 1 
ATOM   6726 N N   . THR D  1 111 ? 21.797 8.393   46.146  1.00 33.43  ? 126 THR D N   1 
ATOM   6727 C CA  . THR D  1 111 ? 21.843 9.635   45.340  1.00 34.05  ? 126 THR D CA  1 
ATOM   6728 C C   . THR D  1 111 ? 21.527 10.816  46.262  1.00 35.57  ? 126 THR D C   1 
ATOM   6729 O O   . THR D  1 111 ? 20.540 10.728  47.024  1.00 34.82  ? 126 THR D O   1 
ATOM   6730 C CB  . THR D  1 111 ? 20.870 9.553   44.158  1.00 34.02  ? 126 THR D CB  1 
ATOM   6731 O OG1 . THR D  1 111 ? 21.101 8.332   43.453  1.00 33.51  ? 126 THR D OG1 1 
ATOM   6732 C CG2 . THR D  1 111 ? 20.992 10.729  43.216  1.00 33.05  ? 126 THR D CG2 1 
ATOM   6733 N N   . LEU D  1 112 ? 22.343 11.868  46.204  1.00 34.79  ? 127 LEU D N   1 
ATOM   6734 C CA  . LEU D  1 112 ? 22.099 13.132  46.944  1.00 37.06  ? 127 LEU D CA  1 
ATOM   6735 C C   . LEU D  1 112 ? 21.122 13.994  46.148  1.00 36.78  ? 127 LEU D C   1 
ATOM   6736 O O   . LEU D  1 112 ? 21.115 13.952  44.921  1.00 38.14  ? 127 LEU D O   1 
ATOM   6737 C CB  . LEU D  1 112 ? 23.429 13.851  47.183  1.00 37.03  ? 127 LEU D CB  1 
ATOM   6738 C CG  . LEU D  1 112 ? 24.458 13.071  48.000  1.00 37.34  ? 127 LEU D CG  1 
ATOM   6739 C CD1 . LEU D  1 112 ? 25.671 13.932  48.299  1.00 38.46  ? 127 LEU D CD1 1 
ATOM   6740 C CD2 . LEU D  1 112 ? 23.859 12.548  49.297  1.00 39.38  ? 127 LEU D CD2 1 
ATOM   6741 N N   . PRO D  1 113 ? 20.262 14.790  46.825  1.00 39.18  ? 128 PRO D N   1 
ATOM   6742 C CA  . PRO D  1 113 ? 19.263 15.597  46.133  1.00 39.32  ? 128 PRO D CA  1 
ATOM   6743 C C   . PRO D  1 113 ? 19.905 16.778  45.417  1.00 38.94  ? 128 PRO D C   1 
ATOM   6744 O O   . PRO D  1 113 ? 21.000 17.200  45.783  1.00 40.24  ? 128 PRO D O   1 
ATOM   6745 C CB  . PRO D  1 113 ? 18.326 16.069  47.253  1.00 39.95  ? 128 PRO D CB  1 
ATOM   6746 C CG  . PRO D  1 113 ? 19.184 16.059  48.498  1.00 39.01  ? 128 PRO D CG  1 
ATOM   6747 C CD  . PRO D  1 113 ? 20.207 14.963  48.282  1.00 38.46  ? 128 PRO D CD  1 
ATOM   6748 N N   . PRO D  1 114 ? 19.247 17.349  44.382  1.00 41.56  ? 129 PRO D N   1 
ATOM   6749 C CA  . PRO D  1 114 ? 19.656 18.648  43.850  1.00 42.54  ? 129 PRO D CA  1 
ATOM   6750 C C   . PRO D  1 114 ? 19.355 19.736  44.891  1.00 41.99  ? 129 PRO D C   1 
ATOM   6751 O O   . PRO D  1 114 ? 18.491 19.512  45.734  1.00 43.02  ? 129 PRO D O   1 
ATOM   6752 C CB  . PRO D  1 114 ? 18.807 18.802  42.576  1.00 43.93  ? 129 PRO D CB  1 
ATOM   6753 C CG  . PRO D  1 114 ? 17.581 17.950  42.832  1.00 43.05  ? 129 PRO D CG  1 
ATOM   6754 C CD  . PRO D  1 114 ? 18.075 16.795  43.680  1.00 42.51  ? 129 PRO D CD  1 
ATOM   6755 N N   . ALA D  1 115 ? 20.046 20.875  44.792  1.00 43.75  ? 130 ALA D N   1 
ATOM   6756 C CA  . ALA D  1 115 ? 19.954 22.025  45.727  1.00 45.32  ? 130 ALA D CA  1 
ATOM   6757 C C   . ALA D  1 115 ? 18.503 22.510  45.871  1.00 46.01  ? 130 ALA D C   1 
ATOM   6758 O O   . ALA D  1 115 ? 18.131 22.913  46.987  1.00 48.87  ? 130 ALA D O   1 
ATOM   6759 C CB  . ALA D  1 115 ? 20.862 23.135  45.259  1.00 45.98  ? 130 ALA D CB  1 
ATOM   6760 N N   . SER D  1 116 ? 17.712 22.451  44.798  1.00 48.90  ? 131 SER D N   1 
ATOM   6761 C CA  . SER D  1 116 ? 16.338 23.012  44.724  1.00 50.18  ? 131 SER D CA  1 
ATOM   6762 C C   . SER D  1 116 ? 15.328 22.164  45.511  1.00 48.28  ? 131 SER D C   1 
ATOM   6763 O O   . SER D  1 116 ? 14.260 22.720  45.828  1.00 48.62  ? 131 SER D O   1 
ATOM   6764 C CB  . SER D  1 116 ? 15.909 23.176  43.291  1.00 50.14  ? 131 SER D CB  1 
ATOM   6765 O OG  . SER D  1 116 ? 15.977 21.937  42.602  1.00 53.30  ? 131 SER D OG  1 
ATOM   6766 N N   . GLU D  1 117 ? 15.622 20.890  45.816  1.00 46.83  ? 132 GLU D N   1 
ATOM   6767 C CA  . GLU D  1 117 ? 14.599 19.973  46.408  1.00 48.52  ? 132 GLU D CA  1 
ATOM   6768 C C   . GLU D  1 117 ? 14.355 20.372  47.872  1.00 48.93  ? 132 GLU D C   1 
ATOM   6769 O O   . GLU D  1 117 ? 15.321 20.330  48.651  1.00 49.99  ? 132 GLU D O   1 
ATOM   6770 C CB  . GLU D  1 117 ? 15.013 18.504  46.265  1.00 50.15  ? 132 GLU D CB  1 
ATOM   6771 C CG  . GLU D  1 117 ? 13.994 17.488  46.785  1.00 51.60  ? 132 GLU D CG  1 
ATOM   6772 C CD  . GLU D  1 117 ? 12.572 17.558  46.239  1.00 56.64  ? 132 GLU D CD  1 
ATOM   6773 O OE1 . GLU D  1 117 ? 11.660 17.942  47.011  1.00 57.11  ? 132 GLU D OE1 1 
ATOM   6774 O OE2 . GLU D  1 117 ? 12.374 17.217  45.052  1.00 59.96  ? 132 GLU D OE2 1 
ATOM   6775 N N   . THR D  1 118 ? 13.102 20.679  48.243  1.00 48.12  ? 133 THR D N   1 
ATOM   6776 C CA  . THR D  1 118 ? 12.691 21.133  49.606  1.00 48.90  ? 133 THR D CA  1 
ATOM   6777 C C   . THR D  1 118 ? 12.112 19.997  50.463  1.00 47.95  ? 133 THR D C   1 
ATOM   6778 O O   . THR D  1 118 ? 12.066 20.192  51.695  1.00 47.58  ? 133 THR D O   1 
ATOM   6779 C CB  . THR D  1 118 ? 11.652 22.261  49.549  1.00 49.41  ? 133 THR D CB  1 
ATOM   6780 O OG1 . THR D  1 118 ? 10.505 21.803  48.829  1.00 50.92  ? 133 THR D OG1 1 
ATOM   6781 C CG2 . THR D  1 118 ? 12.196 23.515  48.898  1.00 50.66  ? 133 THR D CG2 1 
ATOM   6782 N N   . PHE D  1 119 ? 11.672 18.898  49.836  1.00 45.82  ? 134 PHE D N   1 
ATOM   6783 C CA  . PHE D  1 119 ? 11.011 17.725  50.468  1.00 45.35  ? 134 PHE D CA  1 
ATOM   6784 C C   . PHE D  1 119 ? 9.770  18.174  51.246  1.00 47.29  ? 134 PHE D C   1 
ATOM   6785 O O   . PHE D  1 119 ? 9.768  18.162  52.476  1.00 45.20  ? 134 PHE D O   1 
ATOM   6786 C CB  . PHE D  1 119 ? 12.021 16.948  51.318  1.00 43.35  ? 134 PHE D CB  1 
ATOM   6787 C CG  . PHE D  1 119 ? 13.171 16.364  50.540  1.00 41.02  ? 134 PHE D CG  1 
ATOM   6788 C CD1 . PHE D  1 119 ? 13.018 15.185  49.823  1.00 39.40  ? 134 PHE D CD1 1 
ATOM   6789 C CD2 . PHE D  1 119 ? 14.404 16.995  50.525  1.00 40.17  ? 134 PHE D CD2 1 
ATOM   6790 C CE1 . PHE D  1 119 ? 14.082 14.647  49.116  1.00 40.28  ? 134 PHE D CE1 1 
ATOM   6791 C CE2 . PHE D  1 119 ? 15.469 16.451  49.820  1.00 39.60  ? 134 PHE D CE2 1 
ATOM   6792 C CZ  . PHE D  1 119 ? 15.302 15.282  49.112  1.00 38.43  ? 134 PHE D CZ  1 
ATOM   6793 N N   . PRO D  1 120 ? 8.671  18.586  50.568  1.00 48.24  ? 135 PRO D N   1 
ATOM   6794 C CA  . PRO D  1 120 ? 7.498  19.107  51.271  1.00 49.42  ? 135 PRO D CA  1 
ATOM   6795 C C   . PRO D  1 120 ? 6.721  18.011  51.998  1.00 48.45  ? 135 PRO D C   1 
ATOM   6796 O O   . PRO D  1 120 ? 6.867  16.834  51.671  1.00 51.36  ? 135 PRO D O   1 
ATOM   6797 C CB  . PRO D  1 120 ? 6.663  19.718  50.133  1.00 49.78  ? 135 PRO D CB  1 
ATOM   6798 C CG  . PRO D  1 120 ? 7.016  18.875  48.929  1.00 51.70  ? 135 PRO D CG  1 
ATOM   6799 C CD  . PRO D  1 120 ? 8.488  18.567  49.108  1.00 48.58  ? 135 PRO D CD  1 
ATOM   6800 N N   . PRO D  1 121 ? 5.852  18.366  52.979  1.00 47.10  ? 136 PRO D N   1 
ATOM   6801 C CA  . PRO D  1 121 ? 4.935  17.410  53.601  1.00 48.34  ? 136 PRO D CA  1 
ATOM   6802 C C   . PRO D  1 121 ? 4.107  16.605  52.587  1.00 51.41  ? 136 PRO D C   1 
ATOM   6803 O O   . PRO D  1 121 ? 3.713  17.169  51.581  1.00 52.21  ? 136 PRO D O   1 
ATOM   6804 C CB  . PRO D  1 121 ? 3.990  18.303  54.428  1.00 49.04  ? 136 PRO D CB  1 
ATOM   6805 C CG  . PRO D  1 121 ? 4.803  19.534  54.735  1.00 48.63  ? 136 PRO D CG  1 
ATOM   6806 C CD  . PRO D  1 121 ? 5.695  19.723  53.528  1.00 49.23  ? 136 PRO D CD  1 
ATOM   6807 N N   . GLY D  1 122 ? 3.849  15.326  52.885  1.00 52.20  ? 137 GLY D N   1 
ATOM   6808 C CA  . GLY D  1 122 ? 3.113  14.398  52.008  1.00 51.89  ? 137 GLY D CA  1 
ATOM   6809 C C   . GLY D  1 122 ? 4.048  13.557  51.157  1.00 52.89  ? 137 GLY D C   1 
ATOM   6810 O O   . GLY D  1 122 ? 3.605  12.496  50.686  1.00 55.81  ? 137 GLY D O   1 
ATOM   6811 N N   . MET D  1 123 ? 5.295  13.991  50.958  1.00 53.41  ? 138 MET D N   1 
ATOM   6812 C CA  . MET D  1 123 ? 6.318  13.193  50.239  1.00 57.81  ? 138 MET D CA  1 
ATOM   6813 C C   . MET D  1 123 ? 6.595  11.909  51.019  1.00 56.07  ? 138 MET D C   1 
ATOM   6814 O O   . MET D  1 123 ? 6.783  11.973  52.233  1.00 55.40  ? 138 MET D O   1 
ATOM   6815 C CB  . MET D  1 123 ? 7.613  13.988  50.092  1.00 61.11  ? 138 MET D CB  1 
ATOM   6816 C CG  . MET D  1 123 ? 8.574  13.318  49.161  1.00 66.14  ? 138 MET D CG  1 
ATOM   6817 S SD  . MET D  1 123 ? 9.595  14.534  48.305  1.00 73.40  ? 138 MET D SD  1 
ATOM   6818 C CE  . MET D  1 123 ? 8.465  15.102  47.035  1.00 73.91  ? 138 MET D CE  1 
ATOM   6819 N N   . PRO D  1 124 ? 6.613  10.714  50.373  1.00 54.68  ? 139 PRO D N   1 
ATOM   6820 C CA  . PRO D  1 124 ? 6.882  9.457   51.075  1.00 53.53  ? 139 PRO D CA  1 
ATOM   6821 C C   . PRO D  1 124 ? 8.369  9.346   51.436  1.00 50.27  ? 139 PRO D C   1 
ATOM   6822 O O   . PRO D  1 124 ? 9.178  9.324   50.524  1.00 51.53  ? 139 PRO D O   1 
ATOM   6823 C CB  . PRO D  1 124 ? 6.453  8.371   50.074  1.00 54.41  ? 139 PRO D CB  1 
ATOM   6824 C CG  . PRO D  1 124 ? 6.643  9.016   48.719  1.00 55.53  ? 139 PRO D CG  1 
ATOM   6825 C CD  . PRO D  1 124 ? 6.348  10.488  48.939  1.00 58.09  ? 139 PRO D CD  1 
ATOM   6826 N N   . CYS D  1 125 ? 8.694  9.310   52.736  1.00 46.19  ? 140 CYS D N   1 
ATOM   6827 C CA  . CYS D  1 125 ? 10.094 9.263   53.238  1.00 44.66  ? 140 CYS D CA  1 
ATOM   6828 C C   . CYS D  1 125 ? 10.256 8.163   54.286  1.00 40.33  ? 140 CYS D C   1 
ATOM   6829 O O   . CYS D  1 125 ? 9.332  7.949   55.110  1.00 39.45  ? 140 CYS D O   1 
ATOM   6830 C CB  . CYS D  1 125 ? 10.559 10.605  53.790  1.00 45.64  ? 140 CYS D CB  1 
ATOM   6831 S SG  . CYS D  1 125 ? 10.365 11.958  52.599  1.00 51.96  ? 140 CYS D SG  1 
ATOM   6832 N N   . TRP D  1 126 ? 11.418 7.515   54.254  1.00 38.16  ? 141 TRP D N   1 
ATOM   6833 C CA  . TRP D  1 126 ? 11.763 6.356   55.118  1.00 37.22  ? 141 TRP D CA  1 
ATOM   6834 C C   . TRP D  1 126 ? 13.057 6.648   55.883  1.00 36.00  ? 141 TRP D C   1 
ATOM   6835 O O   . TRP D  1 126 ? 13.982 7.218   55.284  1.00 33.75  ? 141 TRP D O   1 
ATOM   6836 C CB  . TRP D  1 126 ? 11.893 5.079   54.283  1.00 36.63  ? 141 TRP D CB  1 
ATOM   6837 C CG  . TRP D  1 126 ? 10.606 4.668   53.641  1.00 40.45  ? 141 TRP D CG  1 
ATOM   6838 C CD1 . TRP D  1 126 ? 10.028 5.206   52.525  1.00 40.63  ? 141 TRP D CD1 1 
ATOM   6839 C CD2 . TRP D  1 126 ? 9.726  3.629   54.088  1.00 40.05  ? 141 TRP D CD2 1 
ATOM   6840 N NE1 . TRP D  1 126 ? 8.848  4.577   52.250  1.00 43.06  ? 141 TRP D NE1 1 
ATOM   6841 C CE2 . TRP D  1 126 ? 8.637  3.603   53.190  1.00 42.75  ? 141 TRP D CE2 1 
ATOM   6842 C CE3 . TRP D  1 126 ? 9.758  2.720   55.150  1.00 40.75  ? 141 TRP D CE3 1 
ATOM   6843 C CZ2 . TRP D  1 126 ? 7.579  2.707   53.335  1.00 44.52  ? 141 TRP D CZ2 1 
ATOM   6844 C CZ3 . TRP D  1 126 ? 8.709  1.836   55.294  1.00 44.26  ? 141 TRP D CZ3 1 
ATOM   6845 C CH2 . TRP D  1 126 ? 7.640  1.828   54.394  1.00 45.76  ? 141 TRP D CH2 1 
ATOM   6846 N N   . VAL D  1 127 ? 13.108 6.259   57.156  1.00 36.13  ? 142 VAL D N   1 
ATOM   6847 C CA  . VAL D  1 127 ? 14.345 6.276   57.988  1.00 36.13  ? 142 VAL D CA  1 
ATOM   6848 C C   . VAL D  1 127 ? 14.639 4.829   58.390  1.00 34.94  ? 142 VAL D C   1 
ATOM   6849 O O   . VAL D  1 127 ? 13.686 4.064   58.619  1.00 35.87  ? 142 VAL D O   1 
ATOM   6850 C CB  . VAL D  1 127 ? 14.232 7.241   59.183  1.00 36.06  ? 142 VAL D CB  1 
ATOM   6851 C CG1 . VAL D  1 127 ? 13.150 6.838   60.181  1.00 37.24  ? 142 VAL D CG1 1 
ATOM   6852 C CG2 . VAL D  1 127 ? 15.574 7.419   59.874  1.00 37.04  ? 142 VAL D CG2 1 
ATOM   6853 N N   . THR D  1 128 ? 15.922 4.467   58.416  1.00 34.38  ? 143 THR D N   1 
ATOM   6854 C CA  . THR D  1 128 ? 16.416 3.083   58.608  1.00 33.77  ? 143 THR D CA  1 
ATOM   6855 C C   . THR D  1 128 ? 17.545 3.082   59.641  1.00 31.80  ? 143 THR D C   1 
ATOM   6856 O O   . THR D  1 128 ? 18.273 4.093   59.747  1.00 32.03  ? 143 THR D O   1 
ATOM   6857 C CB  . THR D  1 128 ? 16.829 2.463   57.264  1.00 34.03  ? 143 THR D CB  1 
ATOM   6858 O OG1 . THR D  1 128 ? 17.796 3.298   56.627  1.00 34.91  ? 143 THR D OG1 1 
ATOM   6859 C CG2 . THR D  1 128 ? 15.654 2.267   56.336  1.00 33.65  ? 143 THR D CG2 1 
ATOM   6860 N N   . GLY D  1 129 ? 17.675 1.988   60.386  1.00 31.18  ? 144 GLY D N   1 
ATOM   6861 C CA  . GLY D  1 129 ? 18.839 1.766   61.262  1.00 31.44  ? 144 GLY D CA  1 
ATOM   6862 C C   . GLY D  1 129 ? 18.634 0.633   62.242  1.00 31.26  ? 144 GLY D C   1 
ATOM   6863 O O   . GLY D  1 129 ? 17.570 -0.022  62.200  1.00 31.62  ? 144 GLY D O   1 
ATOM   6864 N N   . TRP D  1 130 ? 19.643 0.422   63.090  1.00 31.60  ? 145 TRP D N   1 
ATOM   6865 C CA  . TRP D  1 130 ? 19.697 -0.630  64.133  1.00 32.57  ? 145 TRP D CA  1 
ATOM   6866 C C   . TRP D  1 130 ? 19.564 0.004   65.520  1.00 32.44  ? 145 TRP D C   1 
ATOM   6867 O O   . TRP D  1 130 ? 20.003 -0.625  66.493  1.00 32.69  ? 145 TRP D O   1 
ATOM   6868 C CB  . TRP D  1 130 ? 21.008 -1.417  64.012  1.00 31.97  ? 145 TRP D CB  1 
ATOM   6869 C CG  . TRP D  1 130 ? 21.178 -2.158  62.726  1.00 31.51  ? 145 TRP D CG  1 
ATOM   6870 C CD1 . TRP D  1 130 ? 20.726 -3.412  62.432  1.00 31.21  ? 145 TRP D CD1 1 
ATOM   6871 C CD2 . TRP D  1 130 ? 21.918 -1.718  61.577  1.00 32.29  ? 145 TRP D CD2 1 
ATOM   6872 N NE1 . TRP D  1 130 ? 21.107 -3.769  61.171  1.00 31.49  ? 145 TRP D NE1 1 
ATOM   6873 C CE2 . TRP D  1 130 ? 21.845 -2.755  60.622  1.00 31.30  ? 145 TRP D CE2 1 
ATOM   6874 C CE3 . TRP D  1 130 ? 22.623 -0.550  61.258  1.00 30.83  ? 145 TRP D CE3 1 
ATOM   6875 C CZ2 . TRP D  1 130 ? 22.446 -2.652  59.369  1.00 31.10  ? 145 TRP D CZ2 1 
ATOM   6876 C CZ3 . TRP D  1 130 ? 23.226 -0.458  60.025  1.00 32.42  ? 145 TRP D CZ3 1 
ATOM   6877 C CH2 . TRP D  1 130 ? 23.142 -1.497  59.094  1.00 32.47  ? 145 TRP D CH2 1 
ATOM   6878 N N   . GLY D  1 131 ? 18.964 1.195   65.612  1.00 33.66  ? 146 GLY D N   1 
ATOM   6879 C CA  . GLY D  1 131 ? 18.801 1.924   66.881  1.00 33.11  ? 146 GLY D CA  1 
ATOM   6880 C C   . GLY D  1 131 ? 17.675 1.355   67.729  1.00 33.58  ? 146 GLY D C   1 
ATOM   6881 O O   . GLY D  1 131 ? 17.009 0.386   67.303  1.00 33.56  ? 146 GLY D O   1 
ATOM   6882 N N   . ASP D  1 132 ? 17.473 1.963   68.896  1.00 35.23  ? 147 ASP D N   1 
ATOM   6883 C CA  . ASP D  1 132 ? 16.483 1.571   69.931  1.00 35.73  ? 147 ASP D CA  1 
ATOM   6884 C C   . ASP D  1 132 ? 15.082 1.544   69.308  1.00 35.46  ? 147 ASP D C   1 
ATOM   6885 O O   . ASP D  1 132 ? 14.797 2.364   68.409  1.00 34.34  ? 147 ASP D O   1 
ATOM   6886 C CB  . ASP D  1 132 ? 16.561 2.516   71.135  1.00 38.18  ? 147 ASP D CB  1 
ATOM   6887 C CG  . ASP D  1 132 ? 17.838 2.438   71.957  1.00 38.39  ? 147 ASP D CG  1 
ATOM   6888 O OD1 . ASP D  1 132 ? 18.697 1.602   71.641  1.00 39.18  ? 147 ASP D OD1 1 
ATOM   6889 O OD2 . ASP D  1 132 ? 17.968 3.244   72.888  1.00 43.41  ? 147 ASP D OD2 1 
ATOM   6890 N N   . VAL D  1 133 ? 14.252 0.600   69.747  1.00 35.62  ? 148 VAL D N   1 
ATOM   6891 C CA  . VAL D  1 133 ? 12.862 0.396   69.243  1.00 37.02  ? 148 VAL D CA  1 
ATOM   6892 C C   . VAL D  1 133 ? 11.881 1.242   70.064  1.00 38.90  ? 148 VAL D C   1 
ATOM   6893 O O   . VAL D  1 133 ? 10.705 1.317   69.663  1.00 39.03  ? 148 VAL D O   1 
ATOM   6894 C CB  . VAL D  1 133 ? 12.472 -1.094  69.209  1.00 37.62  ? 148 VAL D CB  1 
ATOM   6895 C CG1 . VAL D  1 133 ? 13.364 -1.860  68.243  1.00 38.35  ? 148 VAL D CG1 1 
ATOM   6896 C CG2 . VAL D  1 133 ? 12.472 -1.751  70.584  1.00 37.73  ? 148 VAL D CG2 1 
ATOM   6897 N N   . ASP D  1 134 ? 12.350 1.858   71.153  1.00 40.84  ? 149 ASP D N   1 
ATOM   6898 C CA  . ASP D  1 134 ? 11.608 2.874   71.951  1.00 42.82  ? 149 ASP D CA  1 
ATOM   6899 C C   . ASP D  1 134 ? 12.605 3.585   72.874  1.00 41.34  ? 149 ASP D C   1 
ATOM   6900 O O   . ASP D  1 134 ? 13.791 3.200   72.859  1.00 43.56  ? 149 ASP D O   1 
ATOM   6901 C CB  . ASP D  1 134 ? 10.463 2.235   72.746  1.00 44.17  ? 149 ASP D CB  1 
ATOM   6902 C CG  . ASP D  1 134 ? 9.216  3.100   72.839  1.00 49.49  ? 149 ASP D CG  1 
ATOM   6903 O OD1 . ASP D  1 134 ? 9.354  4.337   72.936  1.00 54.82  ? 149 ASP D OD1 1 
ATOM   6904 O OD2 . ASP D  1 134 ? 8.117  2.537   72.783  1.00 57.07  ? 149 ASP D OD2 1 
ATOM   6905 N N   . ASN D  1 135 ? 12.149 4.559   73.666  1.00 39.96  ? 150 ASN D N   1 
ATOM   6906 C CA  . ASN D  1 135 ? 12.998 5.270   74.664  1.00 42.49  ? 150 ASN D CA  1 
ATOM   6907 C C   . ASN D  1 135 ? 13.597 4.234   75.631  1.00 41.97  ? 150 ASN D C   1 
ATOM   6908 O O   . ASN D  1 135 ? 12.819 3.465   76.231  1.00 41.32  ? 150 ASN D O   1 
ATOM   6909 C CB  . ASN D  1 135 ? 12.224 6.355   75.415  1.00 41.77  ? 150 ASN D CB  1 
ATOM   6910 C CG  . ASN D  1 135 ? 11.746 7.466   74.502  1.00 42.49  ? 150 ASN D CG  1 
ATOM   6911 O OD1 . ASN D  1 135 ? 12.542 8.282   74.039  1.00 43.39  ? 150 ASN D OD1 1 
ATOM   6912 N ND2 . ASN D  1 135 ? 10.452 7.510   74.235  1.00 42.24  ? 150 ASN D ND2 1 
ATOM   6913 N N   . ASP D  1 136 ? 14.930 4.172   75.710  1.00 42.79  ? 151 ASP D N   1 
ATOM   6914 C CA  . ASP D  1 136 ? 15.706 3.282   76.620  1.00 44.87  ? 151 ASP D CA  1 
ATOM   6915 C C   . ASP D  1 136 ? 15.350 1.804   76.374  1.00 43.83  ? 151 ASP D C   1 
ATOM   6916 O O   . ASP D  1 136 ? 15.435 1.032   77.329  1.00 44.10  ? 151 ASP D O   1 
ATOM   6917 C CB  . ASP D  1 136 ? 15.470 3.681   78.083  1.00 46.63  ? 151 ASP D CB  1 
ATOM   6918 C CG  . ASP D  1 136 ? 15.716 5.158   78.361  0.00 45.95  ? 151 ASP D CG  1 
ATOM   6919 O OD1 . ASP D  1 136 ? 16.842 5.631   78.101  0.00 45.87  ? 151 ASP D OD1 1 
ATOM   6920 O OD2 . ASP D  1 136 ? 14.774 5.825   78.835  0.00 46.03  ? 151 ASP D OD2 1 
ATOM   6921 N N   . GLU D  1 137 ? 14.979 1.421   75.143  1.00 44.70  ? 152 GLU D N   1 
ATOM   6922 C CA  . GLU D  1 137 ? 14.590 0.033   74.755  1.00 45.84  ? 152 GLU D CA  1 
ATOM   6923 C C   . GLU D  1 137 ? 15.429 -0.399  73.542  1.00 43.34  ? 152 GLU D C   1 
ATOM   6924 O O   . GLU D  1 137 ? 15.093 0.000   72.410  1.00 42.90  ? 152 GLU D O   1 
ATOM   6925 C CB  . GLU D  1 137 ? 13.087 -0.037  74.470  1.00 48.12  ? 152 GLU D CB  1 
ATOM   6926 C CG  . GLU D  1 137 ? 12.549 -1.457  74.435  1.00 53.74  ? 152 GLU D CG  1 
ATOM   6927 C CD  . GLU D  1 137 ? 11.067 -1.593  74.112  1.00 56.84  ? 152 GLU D CD  1 
ATOM   6928 O OE1 . GLU D  1 137 ? 10.307 -0.647  74.386  1.00 58.55  ? 152 GLU D OE1 1 
ATOM   6929 O OE2 . GLU D  1 137 ? 10.676 -2.653  73.587  1.00 60.40  ? 152 GLU D OE2 1 
ATOM   6930 N N   . ARG D  1 138 ? 16.497 -1.161  73.776  1.00 39.26  ? 153 ARG D N   1 
ATOM   6931 C CA  . ARG D  1 138 ? 17.463 -1.570  72.726  1.00 40.37  ? 153 ARG D CA  1 
ATOM   6932 C C   . ARG D  1 138 ? 16.779 -2.491  71.711  1.00 39.57  ? 153 ARG D C   1 
ATOM   6933 O O   . ARG D  1 138 ? 15.782 -3.149  72.061  1.00 38.84  ? 153 ARG D O   1 
ATOM   6934 C CB  . ARG D  1 138 ? 18.700 -2.208  73.363  1.00 44.02  ? 153 ARG D CB  1 
ATOM   6935 C CG  . ARG D  1 138 ? 19.600 -1.194  74.058  1.00 45.31  ? 153 ARG D CG  1 
ATOM   6936 C CD  . ARG D  1 138 ? 20.957 -1.763  74.422  1.00 46.19  ? 153 ARG D CD  1 
ATOM   6937 N NE  . ARG D  1 138 ? 21.643 -0.954  75.435  0.00 45.98  ? 153 ARG D NE  1 
ATOM   6938 C CZ  . ARG D  1 138 ? 22.777 -1.283  76.055  0.00 45.97  ? 153 ARG D CZ  1 
ATOM   6939 N NH1 . ARG D  1 138 ? 23.385 -2.434  75.815  0.00 45.94  ? 153 ARG D NH1 1 
ATOM   6940 N NH2 . ARG D  1 138 ? 23.305 -0.444  76.928  0.00 45.96  ? 153 ARG D NH2 1 
ATOM   6941 N N   . LEU D  1 139 ? 17.276 -2.487  70.473  1.00 38.60  ? 154 LEU D N   1 
ATOM   6942 C CA  . LEU D  1 139 ? 16.931 -3.501  69.445  1.00 36.84  ? 154 LEU D CA  1 
ATOM   6943 C C   . LEU D  1 139 ? 17.357 -4.866  69.986  1.00 37.11  ? 154 LEU D C   1 
ATOM   6944 O O   . LEU D  1 139 ? 18.531 -5.057  70.301  1.00 37.91  ? 154 LEU D O   1 
ATOM   6945 C CB  . LEU D  1 139 ? 17.655 -3.164  68.141  1.00 35.83  ? 154 LEU D CB  1 
ATOM   6946 C CG  . LEU D  1 139 ? 17.319 -4.045  66.938  1.00 34.08  ? 154 LEU D CG  1 
ATOM   6947 C CD1 . LEU D  1 139 ? 15.877 -3.863  66.480  1.00 32.83  ? 154 LEU D CD1 1 
ATOM   6948 C CD2 . LEU D  1 139 ? 18.278 -3.755  65.804  1.00 35.40  ? 154 LEU D CD2 1 
ATOM   6949 N N   . PRO D  1 140 ? 16.441 -5.848  70.134  1.00 36.28  ? 155 PRO D N   1 
ATOM   6950 C CA  . PRO D  1 140 ? 16.834 -7.195  70.551  1.00 36.79  ? 155 PRO D CA  1 
ATOM   6951 C C   . PRO D  1 140 ? 17.672 -7.951  69.519  1.00 35.71  ? 155 PRO D C   1 
ATOM   6952 O O   . PRO D  1 140 ? 17.582 -7.678  68.323  1.00 37.03  ? 155 PRO D O   1 
ATOM   6953 C CB  . PRO D  1 140 ? 15.497 -7.925  70.741  1.00 36.94  ? 155 PRO D CB  1 
ATOM   6954 C CG  . PRO D  1 140 ? 14.477 -6.819  70.873  1.00 36.18  ? 155 PRO D CG  1 
ATOM   6955 C CD  . PRO D  1 140 ? 14.986 -5.738  69.949  1.00 36.66  ? 155 PRO D CD  1 
ATOM   6956 N N   . PRO D  1 141 ? 18.501 -8.938  69.937  1.00 35.44  ? 156 PRO D N   1 
ATOM   6957 C CA  . PRO D  1 141 ? 19.127 -9.857  68.989  1.00 35.40  ? 156 PRO D CA  1 
ATOM   6958 C C   . PRO D  1 141 ? 18.033 -10.606 68.225  1.00 35.68  ? 156 PRO D C   1 
ATOM   6959 O O   . PRO D  1 141 ? 16.956 -10.830 68.778  1.00 36.11  ? 156 PRO D O   1 
ATOM   6960 C CB  . PRO D  1 141 ? 19.976 -10.810 69.850  1.00 36.39  ? 156 PRO D CB  1 
ATOM   6961 C CG  . PRO D  1 141 ? 20.068 -10.149 71.216  1.00 35.91  ? 156 PRO D CG  1 
ATOM   6962 C CD  . PRO D  1 141 ? 18.868 -9.233  71.331  1.00 35.84  ? 156 PRO D CD  1 
ATOM   6963 N N   . PRO D  1 142 ? 18.237 -11.020 66.948  1.00 34.31  ? 157 PRO D N   1 
ATOM   6964 C CA  . PRO D  1 142 ? 19.513 -10.882 66.239  1.00 34.62  ? 157 PRO D CA  1 
ATOM   6965 C C   . PRO D  1 142 ? 19.725 -9.560  65.474  1.00 35.52  ? 157 PRO D C   1 
ATOM   6966 O O   . PRO D  1 142 ? 20.427 -9.565  64.473  1.00 35.83  ? 157 PRO D O   1 
ATOM   6967 C CB  . PRO D  1 142 ? 19.415 -12.079 65.285  1.00 34.41  ? 157 PRO D CB  1 
ATOM   6968 C CG  . PRO D  1 142 ? 17.964 -12.086 64.872  1.00 34.71  ? 157 PRO D CG  1 
ATOM   6969 C CD  . PRO D  1 142 ? 17.210 -11.663 66.115  1.00 34.25  ? 157 PRO D CD  1 
ATOM   6970 N N   . PHE D  1 143 ? 19.124 -8.461  65.940  1.00 36.25  ? 158 PHE D N   1 
ATOM   6971 C CA  . PHE D  1 143 ? 19.447 -7.073  65.511  1.00 34.92  ? 158 PHE D CA  1 
ATOM   6972 C C   . PHE D  1 143 ? 19.136 -6.870  64.029  1.00 33.53  ? 158 PHE D C   1 
ATOM   6973 O O   . PHE D  1 143 ? 20.023 -6.562  63.230  1.00 32.22  ? 158 PHE D O   1 
ATOM   6974 C CB  . PHE D  1 143 ? 20.919 -6.758  65.803  1.00 34.35  ? 158 PHE D CB  1 
ATOM   6975 C CG  . PHE D  1 143 ? 21.411 -7.135  67.177  1.00 35.62  ? 158 PHE D CG  1 
ATOM   6976 C CD1 . PHE D  1 143 ? 20.947 -6.483  68.313  1.00 35.61  ? 158 PHE D CD1 1 
ATOM   6977 C CD2 . PHE D  1 143 ? 22.371 -8.129  67.333  1.00 37.40  ? 158 PHE D CD2 1 
ATOM   6978 C CE1 . PHE D  1 143 ? 21.422 -6.825  69.569  1.00 35.29  ? 158 PHE D CE1 1 
ATOM   6979 C CE2 . PHE D  1 143 ? 22.839 -8.472  68.593  1.00 36.26  ? 158 PHE D CE2 1 
ATOM   6980 C CZ  . PHE D  1 143 ? 22.368 -7.816  69.707  1.00 35.87  ? 158 PHE D CZ  1 
ATOM   6981 N N   . PRO D  1 144 ? 17.866 -7.026  63.597  1.00 34.66  ? 159 PRO D N   1 
ATOM   6982 C CA  . PRO D  1 144 ? 17.509 -6.818  62.196  1.00 34.18  ? 159 PRO D CA  1 
ATOM   6983 C C   . PRO D  1 144 ? 17.536 -5.320  61.854  1.00 33.49  ? 159 PRO D C   1 
ATOM   6984 O O   . PRO D  1 144 ? 17.163 -4.521  62.691  1.00 32.79  ? 159 PRO D O   1 
ATOM   6985 C CB  . PRO D  1 144 ? 16.092 -7.394  62.107  1.00 34.83  ? 159 PRO D CB  1 
ATOM   6986 C CG  . PRO D  1 144 ? 15.530 -7.161  63.490  1.00 35.55  ? 159 PRO D CG  1 
ATOM   6987 C CD  . PRO D  1 144 ? 16.702 -7.386  64.419  1.00 35.98  ? 159 PRO D CD  1 
ATOM   6988 N N   . LEU D  1 145 ? 17.982 -4.974  60.646  1.00 34.64  ? 160 LEU D N   1 
ATOM   6989 C CA  . LEU D  1 145 ? 17.840 -3.596  60.109  1.00 35.48  ? 160 LEU D CA  1 
ATOM   6990 C C   . LEU D  1 145 ? 16.342 -3.278  60.047  1.00 33.80  ? 160 LEU D C   1 
ATOM   6991 O O   . LEU D  1 145 ? 15.585 -4.081  59.464  1.00 34.78  ? 160 LEU D O   1 
ATOM   6992 C CB  . LEU D  1 145 ? 18.495 -3.479  58.729  1.00 34.33  ? 160 LEU D CB  1 
ATOM   6993 C CG  . LEU D  1 145 ? 18.370 -2.113  58.055  1.00 35.16  ? 160 LEU D CG  1 
ATOM   6994 C CD1 . LEU D  1 145 ? 19.049 -1.023  58.872  1.00 33.89  ? 160 LEU D CD1 1 
ATOM   6995 C CD2 . LEU D  1 145 ? 18.949 -2.153  56.648  1.00 36.91  ? 160 LEU D CD2 1 
ATOM   6996 N N   . LYS D  1 146 ? 15.926 -2.188  60.688  1.00 34.75  ? 161 LYS D N   1 
ATOM   6997 C CA  . LYS D  1 146 ? 14.519 -1.732  60.703  1.00 34.79  ? 161 LYS D CA  1 
ATOM   6998 C C   . LYS D  1 146 ? 14.369 -0.512  59.788  1.00 35.39  ? 161 LYS D C   1 
ATOM   6999 O O   . LYS D  1 146 ? 15.370 0.192   59.521  1.00 33.39  ? 161 LYS D O   1 
ATOM   7000 C CB  . LYS D  1 146 ? 14.079 -1.438  62.134  1.00 34.67  ? 161 LYS D CB  1 
ATOM   7001 C CG  . LYS D  1 146 ? 13.849 -2.671  62.993  1.00 36.06  ? 161 LYS D CG  1 
ATOM   7002 C CD  . LYS D  1 146 ? 13.138 -2.360  64.313  1.00 37.27  ? 161 LYS D CD  1 
ATOM   7003 C CE  . LYS D  1 146 ? 11.649 -2.088  64.183  1.00 39.55  ? 161 LYS D CE  1 
ATOM   7004 N NZ  . LYS D  1 146 ? 11.144 -1.146  65.223  1.00 39.30  ? 161 LYS D NZ  1 
ATOM   7005 N N   . GLN D  1 147 ? 13.142 -0.319  59.320  1.00 33.52  ? 162 GLN D N   1 
ATOM   7006 C CA  . GLN D  1 147 ? 12.697 0.786   58.442  1.00 33.97  ? 162 GLN D CA  1 
ATOM   7007 C C   . GLN D  1 147 ? 11.403 1.337   59.040  1.00 34.81  ? 162 GLN D C   1 
ATOM   7008 O O   . GLN D  1 147 ? 10.686 0.559   59.687  1.00 34.90  ? 162 GLN D O   1 
ATOM   7009 C CB  . GLN D  1 147 ? 12.479 0.264   57.020  1.00 35.42  ? 162 GLN D CB  1 
ATOM   7010 C CG  . GLN D  1 147 ? 11.452 -0.864  56.924  1.00 37.27  ? 162 GLN D CG  1 
ATOM   7011 C CD  . GLN D  1 147 ? 11.148 -1.269  55.503  1.00 37.86  ? 162 GLN D CD  1 
ATOM   7012 O OE1 . GLN D  1 147 ? 12.043 -1.469  54.692  1.00 37.45  ? 162 GLN D OE1 1 
ATOM   7013 N NE2 . GLN D  1 147 ? 9.872  -1.416  55.189  1.00 40.17  ? 162 GLN D NE2 1 
ATOM   7014 N N   . VAL D  1 148 ? 11.111 2.619   58.848  1.00 34.84  ? 163 VAL D N   1 
ATOM   7015 C CA  . VAL D  1 148 ? 9.766  3.183   59.166  1.00 35.93  ? 163 VAL D CA  1 
ATOM   7016 C C   . VAL D  1 148 ? 9.498  4.350   58.213  1.00 35.80  ? 163 VAL D C   1 
ATOM   7017 O O   . VAL D  1 148 ? 10.436 5.131   57.942  1.00 34.01  ? 163 VAL D O   1 
ATOM   7018 C CB  . VAL D  1 148 ? 9.638  3.562   60.660  1.00 35.77  ? 163 VAL D CB  1 
ATOM   7019 C CG1 . VAL D  1 148 ? 10.571 4.692   61.071  1.00 34.95  ? 163 VAL D CG1 1 
ATOM   7020 C CG2 . VAL D  1 148 ? 8.199  3.882   61.046  1.00 36.49  ? 163 VAL D CG2 1 
ATOM   7021 N N   . LYS D  1 149 ? 8.269  4.435   57.702  1.00 35.64  ? 164 LYS D N   1 
ATOM   7022 C CA  . LYS D  1 149 ? 7.787  5.578   56.889  1.00 38.93  ? 164 LYS D CA  1 
ATOM   7023 C C   . LYS D  1 149 ? 7.456  6.713   57.863  1.00 36.74  ? 164 LYS D C   1 
ATOM   7024 O O   . LYS D  1 149 ? 6.675  6.465   58.795  1.00 36.46  ? 164 LYS D O   1 
ATOM   7025 C CB  . LYS D  1 149 ? 6.573  5.174   56.047  1.00 42.28  ? 164 LYS D CB  1 
ATOM   7026 C CG  . LYS D  1 149 ? 6.153  6.199   54.999  1.00 45.30  ? 164 LYS D CG  1 
ATOM   7027 C CD  . LYS D  1 149 ? 4.916  5.805   54.230  1.00 49.15  ? 164 LYS D CD  1 
ATOM   7028 C CE  . LYS D  1 149 ? 4.615  6.763   53.099  1.00 53.48  ? 164 LYS D CE  1 
ATOM   7029 N NZ  . LYS D  1 149 ? 3.315  6.452   52.460  1.00 58.87  ? 164 LYS D NZ  1 
ATOM   7030 N N   . VAL D  1 150 ? 8.072  7.881   57.683  1.00 36.43  ? 165 VAL D N   1 
ATOM   7031 C CA  . VAL D  1 150 ? 7.881  9.055   58.587  1.00 37.23  ? 165 VAL D CA  1 
ATOM   7032 C C   . VAL D  1 150 ? 7.274  10.186  57.767  1.00 39.04  ? 165 VAL D C   1 
ATOM   7033 O O   . VAL D  1 150 ? 7.748  10.469  56.661  1.00 38.12  ? 165 VAL D O   1 
ATOM   7034 C CB  . VAL D  1 150 ? 9.176  9.486   59.305  1.00 36.05  ? 165 VAL D CB  1 
ATOM   7035 C CG1 . VAL D  1 150 ? 9.516  8.518   60.421  1.00 37.66  ? 165 VAL D CG1 1 
ATOM   7036 C CG2 . VAL D  1 150 ? 10.351 9.663   58.364  1.00 37.60  ? 165 VAL D CG2 1 
ATOM   7037 N N   . PRO D  1 151 ? 6.210  10.855  58.277  1.00 39.75  ? 166 PRO D N   1 
ATOM   7038 C CA  . PRO D  1 151 ? 5.646  12.014  57.594  1.00 41.59  ? 166 PRO D CA  1 
ATOM   7039 C C   . PRO D  1 151 ? 6.566  13.224  57.816  1.00 42.83  ? 166 PRO D C   1 
ATOM   7040 O O   . PRO D  1 151 ? 6.829  13.556  58.961  1.00 41.62  ? 166 PRO D O   1 
ATOM   7041 C CB  . PRO D  1 151 ? 4.272  12.179  58.261  1.00 40.95  ? 166 PRO D CB  1 
ATOM   7042 C CG  . PRO D  1 151 ? 4.479  11.657  59.668  1.00 41.38  ? 166 PRO D CG  1 
ATOM   7043 C CD  . PRO D  1 151 ? 5.497  10.542  59.528  1.00 41.27  ? 166 PRO D CD  1 
ATOM   7044 N N   . ILE D  1 152 ? 7.060  13.818  56.731  1.00 42.66  ? 167 ILE D N   1 
ATOM   7045 C CA  . ILE D  1 152 ? 7.797  15.111  56.781  1.00 46.67  ? 167 ILE D CA  1 
ATOM   7046 C C   . ILE D  1 152 ? 6.812  16.193  57.232  1.00 48.68  ? 167 ILE D C   1 
ATOM   7047 O O   . ILE D  1 152 ? 5.630  16.149  56.815  1.00 48.75  ? 167 ILE D O   1 
ATOM   7048 C CB  . ILE D  1 152 ? 8.486  15.432  55.438  1.00 48.36  ? 167 ILE D CB  1 
ATOM   7049 C CG1 . ILE D  1 152 ? 9.812  14.667  55.341  1.00 50.92  ? 167 ILE D CG1 1 
ATOM   7050 C CG2 . ILE D  1 152 ? 8.660  16.939  55.250  1.00 49.45  ? 167 ILE D CG2 1 
ATOM   7051 C CD1 . ILE D  1 152 ? 10.686 15.015  54.156  1.00 53.06  ? 167 ILE D CD1 1 
ATOM   7052 N N   A MET D  1 153 ? 7.277  17.120  58.075  0.50 48.88  ? 168 MET D N   1 
ATOM   7053 N N   B MET D  1 153 ? 7.308  17.139  58.040  0.50 48.26  ? 168 MET D N   1 
ATOM   7054 C CA  A MET D  1 153 ? 6.495  18.313  58.491  0.50 50.20  ? 168 MET D CA  1 
ATOM   7055 C CA  B MET D  1 153 ? 6.575  18.305  58.603  0.50 48.91  ? 168 MET D CA  1 
ATOM   7056 C C   A MET D  1 153 ? 7.325  19.568  58.227  0.50 48.89  ? 168 MET D C   1 
ATOM   7057 C C   B MET D  1 153 ? 7.348  19.578  58.236  0.50 48.22  ? 168 MET D C   1 
ATOM   7058 O O   A MET D  1 153 ? 8.559  19.480  58.332  0.50 50.43  ? 168 MET D O   1 
ATOM   7059 O O   B MET D  1 153 ? 8.591  19.523  58.312  0.50 49.64  ? 168 MET D O   1 
ATOM   7060 C CB  A MET D  1 153 ? 6.096  18.201  59.963  0.50 53.30  ? 168 MET D CB  1 
ATOM   7061 C CB  B MET D  1 153 ? 6.499  18.162  60.126  0.50 51.18  ? 168 MET D CB  1 
ATOM   7062 C CG  A MET D  1 153 ? 5.024  17.147  60.167  0.50 55.08  ? 168 MET D CG  1 
ATOM   7063 C CG  B MET D  1 153 ? 5.662  19.212  60.823  0.50 53.28  ? 168 MET D CG  1 
ATOM   7064 S SD  A MET D  1 153 ? 4.939  16.547  61.859  0.50 61.98  ? 168 MET D SD  1 
ATOM   7065 S SD  B MET D  1 153 ? 5.646  18.942  62.616  0.50 55.52  ? 168 MET D SD  1 
ATOM   7066 C CE  A MET D  1 153 ? 4.666  18.091  62.727  0.50 60.88  ? 168 MET D CE  1 
ATOM   7067 C CE  B MET D  1 153 ? 5.148  17.220  62.671  0.50 56.61  ? 168 MET D CE  1 
ATOM   7068 N N   . GLU D  1 154 ? 6.661  20.663  57.841  1.00 46.04  ? 169 GLU D N   1 
ATOM   7069 C CA  . GLU D  1 154 ? 7.302  21.970  57.512  1.00 45.51  ? 169 GLU D CA  1 
ATOM   7070 C C   . GLU D  1 154 ? 8.090  22.471  58.734  1.00 41.28  ? 169 GLU D C   1 
ATOM   7071 O O   . GLU D  1 154 ? 7.617  22.261  59.867  1.00 38.60  ? 169 GLU D O   1 
ATOM   7072 C CB  . GLU D  1 154 ? 6.262  23.009  57.076  1.00 51.19  ? 169 GLU D CB  1 
ATOM   7073 C CG  . GLU D  1 154 ? 6.003  23.030  55.584  1.00 56.97  ? 169 GLU D CG  1 
ATOM   7074 C CD  . GLU D  1 154 ? 5.130  24.187  55.132  1.00 62.07  ? 169 GLU D CD  1 
ATOM   7075 O OE1 . GLU D  1 154 ? 5.518  25.344  55.376  1.00 63.89  ? 169 GLU D OE1 1 
ATOM   7076 O OE2 . GLU D  1 154 ? 4.058  23.924  54.550  1.00 68.43  ? 169 GLU D OE2 1 
ATOM   7077 N N   . ASN D  1 155 ? 9.250  23.088  58.503  1.00 37.15  ? 170 ASN D N   1 
ATOM   7078 C CA  . ASN D  1 155 ? 10.181 23.565  59.559  1.00 37.66  ? 170 ASN D CA  1 
ATOM   7079 C C   . ASN D  1 155 ? 9.438  24.500  60.525  1.00 37.18  ? 170 ASN D C   1 
ATOM   7080 O O   . ASN D  1 155 ? 9.635  24.337  61.736  1.00 36.20  ? 170 ASN D O   1 
ATOM   7081 C CB  . ASN D  1 155 ? 11.421 24.254  58.978  1.00 37.69  ? 170 ASN D CB  1 
ATOM   7082 C CG  . ASN D  1 155 ? 12.574 23.309  58.683  1.00 38.54  ? 170 ASN D CG  1 
ATOM   7083 O OD1 . ASN D  1 155 ? 12.362 22.150  58.341  1.00 37.54  ? 170 ASN D OD1 1 
ATOM   7084 N ND2 . ASN D  1 155 ? 13.803 23.785  58.835  1.00 40.67  ? 170 ASN D ND2 1 
ATOM   7085 N N   . HIS D  1 156 ? 8.602  25.419  60.024  1.00 38.17  ? 171 HIS D N   1 
ATOM   7086 C CA  . HIS D  1 156 ? 7.878  26.414  60.871  1.00 40.10  ? 171 HIS D CA  1 
ATOM   7087 C C   . HIS D  1 156 ? 6.891  25.696  61.812  1.00 37.53  ? 171 HIS D C   1 
ATOM   7088 O O   . HIS D  1 156 ? 6.766  26.123  62.970  1.00 38.42  ? 171 HIS D O   1 
ATOM   7089 C CB  . HIS D  1 156 ? 7.285  27.550  60.017  1.00 41.73  ? 171 HIS D CB  1 
ATOM   7090 C CG  . HIS D  1 156 ? 5.916  27.308  59.482  1.00 46.95  ? 171 HIS D CG  1 
ATOM   7091 N ND1 . HIS D  1 156 ? 5.690  26.787  58.222  1.00 50.55  ? 171 HIS D ND1 1 
ATOM   7092 C CD2 . HIS D  1 156 ? 4.702  27.515  60.034  1.00 49.70  ? 171 HIS D CD2 1 
ATOM   7093 C CE1 . HIS D  1 156 ? 4.387  26.682  58.020  1.00 50.36  ? 171 HIS D CE1 1 
ATOM   7094 N NE2 . HIS D  1 156 ? 3.759  27.125  59.116  1.00 50.78  ? 171 HIS D NE2 1 
ATOM   7095 N N   . ILE D  1 157 ? 6.199  24.662  61.332  1.00 37.03  ? 172 ILE D N   1 
ATOM   7096 C CA  . ILE D  1 157 ? 5.218  23.853  62.128  1.00 38.51  ? 172 ILE D CA  1 
ATOM   7097 C C   . ILE D  1 157 ? 5.967  23.097  63.233  1.00 36.85  ? 172 ILE D C   1 
ATOM   7098 O O   . ILE D  1 157 ? 5.483  23.051  64.375  1.00 37.67  ? 172 ILE D O   1 
ATOM   7099 C CB  . ILE D  1 157 ? 4.424  22.876  61.233  1.00 39.18  ? 172 ILE D CB  1 
ATOM   7100 C CG1 . ILE D  1 157 ? 3.613  23.591  60.143  1.00 42.26  ? 172 ILE D CG1 1 
ATOM   7101 C CG2 . ILE D  1 157 ? 3.548  21.963  62.077  1.00 40.23  ? 172 ILE D CG2 1 
ATOM   7102 C CD1 . ILE D  1 157 ? 2.623  24.612  60.659  1.00 43.90  ? 172 ILE D CD1 1 
ATOM   7103 N N   . CYS D  1 158 ? 7.099  22.494  62.884  1.00 36.70  ? 173 CYS D N   1 
ATOM   7104 C CA  A CYS D  1 158 ? 7.954  21.699  63.803  0.50 36.36  ? 173 CYS D CA  1 
ATOM   7105 C CA  B CYS D  1 158 ? 7.922  21.697  63.831  0.50 38.13  ? 173 CYS D CA  1 
ATOM   7106 C C   . CYS D  1 158 ? 8.588  22.621  64.857  1.00 36.39  ? 173 CYS D C   1 
ATOM   7107 O O   . CYS D  1 158 ? 8.640  22.218  66.024  1.00 36.34  ? 173 CYS D O   1 
ATOM   7108 C CB  A CYS D  1 158 ? 9.003  20.958  62.982  0.50 35.70  ? 173 CYS D CB  1 
ATOM   7109 C CB  B CYS D  1 158 ? 8.946  20.841  63.101  0.50 39.59  ? 173 CYS D CB  1 
ATOM   7110 S SG  A CYS D  1 158 ? 10.157 19.952  63.941  0.50 35.62  ? 173 CYS D SG  1 
ATOM   7111 S SG  B CYS D  1 158 ? 8.187  19.371  62.368  0.50 44.08  ? 173 CYS D SG  1 
ATOM   7112 N N   . ASP D  1 159 ? 9.036  23.814  64.442  1.00 35.56  ? 174 ASP D N   1 
ATOM   7113 C CA  . ASP D  1 159 ? 9.563  24.864  65.354  1.00 35.01  ? 174 ASP D CA  1 
ATOM   7114 C C   . ASP D  1 159 ? 8.483  25.218  66.381  1.00 34.28  ? 174 ASP D C   1 
ATOM   7115 O O   . ASP D  1 159 ? 8.804  25.225  67.581  1.00 31.87  ? 174 ASP D O   1 
ATOM   7116 C CB  . ASP D  1 159 ? 10.025 26.112  64.599  1.00 34.76  ? 174 ASP D CB  1 
ATOM   7117 C CG  . ASP D  1 159 ? 10.802 27.086  65.467  1.00 35.81  ? 174 ASP D CG  1 
ATOM   7118 O OD1 . ASP D  1 159 ? 11.743 26.643  66.137  1.00 35.77  ? 174 ASP D OD1 1 
ATOM   7119 O OD2 . ASP D  1 159 ? 10.449 28.286  65.478  1.00 38.09  ? 174 ASP D OD2 1 
ATOM   7120 N N   . ALA D  1 160 ? 7.248  25.462  65.931  1.00 34.69  ? 175 ALA D N   1 
ATOM   7121 C CA  . ALA D  1 160 ? 6.091  25.798  66.804  1.00 35.40  ? 175 ALA D CA  1 
ATOM   7122 C C   . ALA D  1 160 ? 5.828  24.656  67.799  1.00 35.89  ? 175 ALA D C   1 
ATOM   7123 O O   . ALA D  1 160 ? 5.603  24.957  68.980  1.00 37.53  ? 175 ALA D O   1 
ATOM   7124 C CB  . ALA D  1 160 ? 4.859  26.110  65.982  1.00 34.11  ? 175 ALA D CB  1 
ATOM   7125 N N   . LYS D  1 161 ? 5.886  23.394  67.361  1.00 36.91  ? 176 LYS D N   1 
ATOM   7126 C CA  . LYS D  1 161 ? 5.639  22.224  68.253  1.00 38.63  ? 176 LYS D CA  1 
ATOM   7127 C C   . LYS D  1 161 ? 6.717  22.151  69.349  1.00 34.89  ? 176 LYS D C   1 
ATOM   7128 O O   . LYS D  1 161 ? 6.356  21.912  70.496  1.00 34.47  ? 176 LYS D O   1 
ATOM   7129 C CB  . LYS D  1 161 ? 5.534  20.927  67.450  1.00 41.16  ? 176 LYS D CB  1 
ATOM   7130 C CG  . LYS D  1 161 ? 4.233  20.770  66.676  1.00 44.03  ? 176 LYS D CG  1 
ATOM   7131 C CD  . LYS D  1 161 ? 4.050  19.386  66.110  1.00 49.82  ? 176 LYS D CD  1 
ATOM   7132 C CE  . LYS D  1 161 ? 2.742  19.222  65.364  1.00 52.84  ? 176 LYS D CE  1 
ATOM   7133 N NZ  . LYS D  1 161 ? 2.294  17.808  65.373  1.00 55.86  ? 176 LYS D NZ  1 
ATOM   7134 N N   . TYR D  1 162 ? 7.984  22.412  69.025  1.00 34.36  ? 177 TYR D N   1 
ATOM   7135 C CA  . TYR D  1 162 ? 9.114  22.376  69.994  1.00 34.38  ? 177 TYR D CA  1 
ATOM   7136 C C   . TYR D  1 162 ? 8.957  23.471  71.061  1.00 33.76  ? 177 TYR D C   1 
ATOM   7137 O O   . TYR D  1 162 ? 9.508  23.276  72.155  1.00 33.76  ? 177 TYR D O   1 
ATOM   7138 C CB  . TYR D  1 162 ? 10.466 22.416  69.275  1.00 34.06  ? 177 TYR D CB  1 
ATOM   7139 C CG  . TYR D  1 162 ? 11.044 21.038  69.099  1.00 31.93  ? 177 TYR D CG  1 
ATOM   7140 C CD1 . TYR D  1 162 ? 10.605 20.199  68.085  1.00 32.46  ? 177 TYR D CD1 1 
ATOM   7141 C CD2 . TYR D  1 162 ? 11.960 20.531  70.007  1.00 31.45  ? 177 TYR D CD2 1 
ATOM   7142 C CE1 . TYR D  1 162 ? 11.098 18.909  67.946  1.00 31.30  ? 177 TYR D CE1 1 
ATOM   7143 C CE2 . TYR D  1 162 ? 12.454 19.240  69.888  1.00 33.06  ? 177 TYR D CE2 1 
ATOM   7144 C CZ  . TYR D  1 162 ? 12.025 18.427  68.851  1.00 30.98  ? 177 TYR D CZ  1 
ATOM   7145 O OH  . TYR D  1 162 ? 12.513 17.160  68.720  1.00 33.58  ? 177 TYR D OH  1 
ATOM   7146 N N   . HIS D  1 163 ? 8.204  24.540  70.772  1.00 32.92  ? 178 HIS D N   1 
ATOM   7147 C CA  . HIS D  1 163 ? 7.901  25.658  71.709  1.00 33.46  ? 178 HIS D CA  1 
ATOM   7148 C C   . HIS D  1 163 ? 6.728  25.318  72.647  1.00 32.35  ? 178 HIS D C   1 
ATOM   7149 O O   . HIS D  1 163 ? 6.649  25.947  73.710  1.00 31.62  ? 178 HIS D O   1 
ATOM   7150 C CB  . HIS D  1 163 ? 7.651  26.953  70.923  1.00 32.31  ? 178 HIS D CB  1 
ATOM   7151 C CG  . HIS D  1 163 ? 8.900  27.590  70.425  1.00 32.03  ? 178 HIS D CG  1 
ATOM   7152 N ND1 . HIS D  1 163 ? 9.491  27.234  69.228  1.00 31.85  ? 178 HIS D ND1 1 
ATOM   7153 C CD2 . HIS D  1 163 ? 9.675  28.559  70.963  1.00 33.76  ? 178 HIS D CD2 1 
ATOM   7154 C CE1 . HIS D  1 163 ? 10.583 27.959  69.053  1.00 32.26  ? 178 HIS D CE1 1 
ATOM   7155 N NE2 . HIS D  1 163 ? 10.709 28.784  70.093  1.00 33.11  ? 178 HIS D NE2 1 
ATOM   7156 N N   . LEU D  1 164 ? 5.843  24.393  72.272  1.00 33.41  ? 179 LEU D N   1 
ATOM   7157 C CA  . LEU D  1 164 ? 4.714  23.951  73.132  1.00 35.23  ? 179 LEU D CA  1 
ATOM   7158 C C   . LEU D  1 164 ? 5.275  23.185  74.336  1.00 36.17  ? 179 LEU D C   1 
ATOM   7159 O O   . LEU D  1 164 ? 6.055  22.237  74.124  1.00 33.68  ? 179 LEU D O   1 
ATOM   7160 C CB  . LEU D  1 164 ? 3.748  23.080  72.321  1.00 37.80  ? 179 LEU D CB  1 
ATOM   7161 C CG  . LEU D  1 164 ? 2.971  23.789  71.211  1.00 40.39  ? 179 LEU D CG  1 
ATOM   7162 C CD1 . LEU D  1 164 ? 2.185  22.781  70.385  1.00 41.18  ? 179 LEU D CD1 1 
ATOM   7163 C CD2 . LEU D  1 164 ? 2.031  24.860  71.764  1.00 39.85  ? 179 LEU D CD2 1 
ATOM   7164 N N   . GLY D  1 165 ? 4.900  23.599  75.549  1.00 36.34  ? 180 GLY D N   1 
ATOM   7165 C CA  . GLY D  1 165 ? 5.397  23.019  76.811  1.00 36.13  ? 180 GLY D CA  1 
ATOM   7166 C C   . GLY D  1 165 ? 6.843  23.395  77.080  1.00 35.82  ? 180 GLY D C   1 
ATOM   7167 O O   . GLY D  1 165 ? 7.502  22.659  77.840  1.00 36.54  ? 180 GLY D O   1 
ATOM   7168 N N   . ALA D  1 166 ? 7.319  24.509  76.513  1.00 34.33  ? 181 ALA D N   1 
ATOM   7169 C CA  . ALA D  1 166 ? 8.695  25.026  76.698  1.00 34.52  ? 181 ALA D CA  1 
ATOM   7170 C C   . ALA D  1 166 ? 8.646  26.484  77.155  1.00 35.65  ? 181 ALA D C   1 
ATOM   7171 O O   . ALA D  1 166 ? 7.690  27.188  76.808  1.00 36.17  ? 181 ALA D O   1 
ATOM   7172 C CB  . ALA D  1 166 ? 9.489  24.874  75.427  1.00 34.74  ? 181 ALA D CB  1 
ATOM   7173 N N   . TYR D  1 167 ? 9.669  26.912  77.895  1.00 36.21  ? 182 TYR D N   1 
ATOM   7174 C CA  . TYR D  1 167 ? 9.856  28.313  78.344  1.00 37.04  ? 182 TYR D CA  1 
ATOM   7175 C C   . TYR D  1 167 ? 10.426 29.176  77.209  1.00 35.40  ? 182 TYR D C   1 
ATOM   7176 O O   . TYR D  1 167 ? 10.301 30.406  77.301  1.00 34.82  ? 182 TYR D O   1 
ATOM   7177 C CB  . TYR D  1 167 ? 10.773 28.358  79.567  1.00 37.01  ? 182 TYR D CB  1 
ATOM   7178 C CG  . TYR D  1 167 ? 10.241 27.702  80.817  1.00 37.74  ? 182 TYR D CG  1 
ATOM   7179 C CD1 . TYR D  1 167 ? 9.134  28.209  81.481  1.00 39.49  ? 182 TYR D CD1 1 
ATOM   7180 C CD2 . TYR D  1 167 ? 10.888 26.615  81.388  1.00 37.36  ? 182 TYR D CD2 1 
ATOM   7181 C CE1 . TYR D  1 167 ? 8.667  27.642  82.657  1.00 37.88  ? 182 TYR D CE1 1 
ATOM   7182 C CE2 . TYR D  1 167 ? 10.436 26.036  82.562  1.00 36.74  ? 182 TYR D CE2 1 
ATOM   7183 C CZ  . TYR D  1 167 ? 9.324  26.553  83.202  1.00 37.81  ? 182 TYR D CZ  1 
ATOM   7184 O OH  . TYR D  1 167 ? 8.864  25.981  84.349  1.00 36.87  ? 182 TYR D OH  1 
ATOM   7185 N N   . THR D  1 168 ? 11.072 28.566  76.210  1.00 34.32  ? 183 THR D N   1 
ATOM   7186 C CA  . THR D  1 168 ? 11.769 29.264  75.096  1.00 34.56  ? 183 THR D CA  1 
ATOM   7187 C C   . THR D  1 168 ? 10.773 30.208  74.412  1.00 35.05  ? 183 THR D C   1 
ATOM   7188 O O   . THR D  1 168 ? 9.649  29.754  74.110  1.00 33.95  ? 183 THR D O   1 
ATOM   7189 C CB  . THR D  1 168 ? 12.391 28.273  74.102  1.00 34.50  ? 183 THR D CB  1 
ATOM   7190 O OG1 . THR D  1 168 ? 13.094 27.254  74.819  1.00 34.86  ? 183 THR D OG1 1 
ATOM   7191 C CG2 . THR D  1 168 ? 13.344 28.934  73.132  1.00 34.29  ? 183 THR D CG2 1 
ATOM   7192 N N   . GLY D  1 169 ? 11.165 31.473  74.216  1.00 34.95  ? 184 GLY D N   1 
ATOM   7193 C CA  . GLY D  1 169 ? 10.362 32.495  73.518  1.00 36.65  ? 184 GLY D CA  1 
ATOM   7194 C C   . GLY D  1 169 ? 10.018 32.046  72.107  1.00 35.54  ? 184 GLY D C   1 
ATOM   7195 O O   . GLY D  1 169 ? 10.899 31.455  71.443  1.00 36.95  ? 184 GLY D O   1 
ATOM   7196 N N   . ASP D  1 170 ? 8.788  32.308  71.669  1.00 36.42  ? 185 ASP D N   1 
ATOM   7197 C CA  . ASP D  1 170 ? 8.227  31.855  70.365  1.00 39.25  ? 185 ASP D CA  1 
ATOM   7198 C C   . ASP D  1 170 ? 9.080  32.330  69.182  1.00 37.72  ? 185 ASP D C   1 
ATOM   7199 O O   . ASP D  1 170 ? 9.110  31.589  68.180  1.00 37.26  ? 185 ASP D O   1 
ATOM   7200 C CB  . ASP D  1 170 ? 6.764  32.286  70.218  1.00 40.47  ? 185 ASP D CB  1 
ATOM   7201 C CG  . ASP D  1 170 ? 5.812  31.464  71.074  1.00 44.89  ? 185 ASP D CG  1 
ATOM   7202 O OD1 . ASP D  1 170 ? 6.176  30.321  71.437  1.00 45.29  ? 185 ASP D OD1 1 
ATOM   7203 O OD2 . ASP D  1 170 ? 4.719  31.971  71.382  1.00 52.15  ? 185 ASP D OD2 1 
ATOM   7204 N N   . ASP D  1 171 ? 9.727  33.495  69.291  1.00 37.37  ? 186 ASP D N   1 
ATOM   7205 C CA  . ASP D  1 171 ? 10.559 34.109  68.216  1.00 39.88  ? 186 ASP D CA  1 
ATOM   7206 C C   . ASP D  1 171 ? 12.021 33.665  68.328  1.00 36.77  ? 186 ASP D C   1 
ATOM   7207 O O   . ASP D  1 171 ? 12.833 34.147  67.524  1.00 34.54  ? 186 ASP D O   1 
ATOM   7208 C CB  . ASP D  1 171 ? 10.452 35.639  68.244  1.00 43.69  ? 186 ASP D CB  1 
ATOM   7209 C CG  . ASP D  1 171 ? 9.057  36.178  67.963  1.00 50.00  ? 186 ASP D CG  1 
ATOM   7210 O OD1 . ASP D  1 171 ? 8.101  35.362  67.877  1.00 55.13  ? 186 ASP D OD1 1 
ATOM   7211 O OD2 . ASP D  1 171 ? 8.934  37.413  67.821  1.00 58.92  ? 186 ASP D OD2 1 
ATOM   7212 N N   . VAL D  1 172 ? 12.356 32.782  69.273  1.00 34.53  ? 187 VAL D N   1 
ATOM   7213 C CA  . VAL D  1 172 ? 13.714 32.182  69.389  1.00 33.39  ? 187 VAL D CA  1 
ATOM   7214 C C   . VAL D  1 172 ? 13.658 30.818  68.694  1.00 33.40  ? 187 VAL D C   1 
ATOM   7215 O O   . VAL D  1 172 ? 13.019 29.906  69.243  1.00 33.92  ? 187 VAL D O   1 
ATOM   7216 C CB  . VAL D  1 172 ? 14.170 32.105  70.855  1.00 33.81  ? 187 VAL D CB  1 
ATOM   7217 C CG1 . VAL D  1 172 ? 15.567 31.504  70.977  1.00 32.20  ? 187 VAL D CG1 1 
ATOM   7218 C CG2 . VAL D  1 172 ? 14.123 33.483  71.507  1.00 35.41  ? 187 VAL D CG2 1 
ATOM   7219 N N   . ARG D  1 173 ? 14.241 30.711  67.495  1.00 34.23  ? 188 ARG D N   1 
ATOM   7220 C CA  . ARG D  1 173 ? 14.077 29.517  66.627  1.00 34.19  ? 188 ARG D CA  1 
ATOM   7221 C C   . ARG D  1 173 ? 14.825 28.342  67.266  1.00 33.30  ? 188 ARG D C   1 
ATOM   7222 O O   . ARG D  1 173 ? 15.983 28.523  67.661  1.00 33.34  ? 188 ARG D O   1 
ATOM   7223 C CB  . ARG D  1 173 ? 14.559 29.789  65.200  1.00 35.44  ? 188 ARG D CB  1 
ATOM   7224 C CG  . ARG D  1 173 ? 14.013 28.785  64.197  1.00 37.11  ? 188 ARG D CG  1 
ATOM   7225 C CD  . ARG D  1 173 ? 14.063 29.233  62.760  1.00 38.03  ? 188 ARG D CD  1 
ATOM   7226 N NE  . ARG D  1 173 ? 13.133 30.329  62.512  1.00 39.62  ? 188 ARG D NE  1 
ATOM   7227 C CZ  . ARG D  1 173 ? 12.767 30.769  61.307  1.00 36.89  ? 188 ARG D CZ  1 
ATOM   7228 N NH1 . ARG D  1 173 ? 13.259 30.220  60.206  1.00 37.24  ? 188 ARG D NH1 1 
ATOM   7229 N NH2 . ARG D  1 173 ? 11.896 31.759  61.213  1.00 35.40  ? 188 ARG D NH2 1 
ATOM   7230 N N   . ILE D  1 174 ? 14.158 27.194  67.375  1.00 33.27  ? 189 ILE D N   1 
ATOM   7231 C CA  . ILE D  1 174 ? 14.729 25.915  67.883  1.00 33.95  ? 189 ILE D CA  1 
ATOM   7232 C C   . ILE D  1 174 ? 15.115 25.063  66.670  1.00 33.91  ? 189 ILE D C   1 
ATOM   7233 O O   . ILE D  1 174 ? 16.298 24.661  66.582  1.00 33.59  ? 189 ILE D O   1 
ATOM   7234 C CB  . ILE D  1 174 ? 13.742 25.204  68.835  1.00 33.85  ? 189 ILE D CB  1 
ATOM   7235 C CG1 . ILE D  1 174 ? 13.490 26.035  70.101  1.00 34.20  ? 189 ILE D CG1 1 
ATOM   7236 C CG2 . ILE D  1 174 ? 14.245 23.802  69.171  1.00 33.56  ? 189 ILE D CG2 1 
ATOM   7237 C CD1 . ILE D  1 174 ? 12.298 25.595  70.921  1.00 34.02  ? 189 ILE D CD1 1 
ATOM   7238 N N   . VAL D  1 175 ? 14.154 24.823  65.771  1.00 32.78  ? 190 VAL D N   1 
ATOM   7239 C CA  . VAL D  1 175 ? 14.348 24.041  64.515  1.00 33.93  ? 190 VAL D CA  1 
ATOM   7240 C C   . VAL D  1 175 ? 14.885 24.996  63.447  1.00 35.50  ? 190 VAL D C   1 
ATOM   7241 O O   . VAL D  1 175 ? 14.131 25.875  63.001  1.00 37.70  ? 190 VAL D O   1 
ATOM   7242 C CB  . VAL D  1 175 ? 13.041 23.350  64.081  1.00 33.44  ? 190 VAL D CB  1 
ATOM   7243 C CG1 . VAL D  1 175 ? 13.223 22.545  62.804  1.00 33.30  ? 190 VAL D CG1 1 
ATOM   7244 C CG2 . VAL D  1 175 ? 12.497 22.467  65.190  1.00 33.18  ? 190 VAL D CG2 1 
ATOM   7245 N N   . ARG D  1 176 ? 16.150 24.820  63.063  1.00 36.26  ? 191 ARG D N   1 
ATOM   7246 C CA  . ARG D  1 176 ? 16.906 25.797  62.242  1.00 37.54  ? 191 ARG D CA  1 
ATOM   7247 C C   . ARG D  1 176 ? 16.791 25.418  60.764  1.00 36.53  ? 191 ARG D C   1 
ATOM   7248 O O   . ARG D  1 176 ? 16.236 24.339  60.459  1.00 35.16  ? 191 ARG D O   1 
ATOM   7249 C CB  . ARG D  1 176 ? 18.338 25.873  62.774  1.00 38.48  ? 191 ARG D CB  1 
ATOM   7250 C CG  . ARG D  1 176 ? 18.380 26.289  64.234  1.00 40.08  ? 191 ARG D CG  1 
ATOM   7251 C CD  . ARG D  1 176 ? 19.708 26.873  64.633  1.00 44.66  ? 191 ARG D CD  1 
ATOM   7252 N NE  . ARG D  1 176 ? 19.676 27.378  65.999  1.00 47.20  ? 191 ARG D NE  1 
ATOM   7253 C CZ  . ARG D  1 176 ? 20.665 28.038  66.597  1.00 50.46  ? 191 ARG D CZ  1 
ATOM   7254 N NH1 . ARG D  1 176 ? 21.794 28.304  65.953  1.00 51.43  ? 191 ARG D NH1 1 
ATOM   7255 N NH2 . ARG D  1 176 ? 20.516 28.435  67.851  1.00 51.51  ? 191 ARG D NH2 1 
ATOM   7256 N N   . ASP D  1 177 ? 17.259 26.303  59.884  1.00 36.40  ? 192 ASP D N   1 
ATOM   7257 C CA  . ASP D  1 177 ? 16.984 26.243  58.421  1.00 36.45  ? 192 ASP D CA  1 
ATOM   7258 C C   . ASP D  1 177 ? 17.820 25.126  57.774  1.00 35.58  ? 192 ASP D C   1 
ATOM   7259 O O   . ASP D  1 177 ? 17.404 24.616  56.722  1.00 35.57  ? 192 ASP D O   1 
ATOM   7260 C CB  . ASP D  1 177 ? 17.211 27.604  57.754  1.00 38.79  ? 192 ASP D CB  1 
ATOM   7261 C CG  . ASP D  1 177 ? 16.398 28.745  58.354  1.00 40.59  ? 192 ASP D CG  1 
ATOM   7262 O OD1 . ASP D  1 177 ? 15.447 28.464  59.116  1.00 40.20  ? 192 ASP D OD1 1 
ATOM   7263 O OD2 . ASP D  1 177 ? 16.743 29.906  58.081  1.00 43.58  ? 192 ASP D OD2 1 
ATOM   7264 N N   . ASP D  1 178 ? 18.934 24.733  58.396  1.00 35.29  ? 193 ASP D N   1 
ATOM   7265 C CA  . ASP D  1 178 ? 19.790 23.595  57.962  1.00 35.36  ? 193 ASP D CA  1 
ATOM   7266 C C   . ASP D  1 178 ? 19.265 22.272  58.546  1.00 34.65  ? 193 ASP D C   1 
ATOM   7267 O O   . ASP D  1 178 ? 20.008 21.269  58.483  1.00 33.46  ? 193 ASP D O   1 
ATOM   7268 C CB  . ASP D  1 178 ? 21.251 23.839  58.360  1.00 35.55  ? 193 ASP D CB  1 
ATOM   7269 C CG  . ASP D  1 178 ? 21.515 23.822  59.859  1.00 36.55  ? 193 ASP D CG  1 
ATOM   7270 O OD1 . ASP D  1 178 ? 20.611 24.205  60.619  1.00 37.76  ? 193 ASP D OD1 1 
ATOM   7271 O OD2 . ASP D  1 178 ? 22.615 23.405  60.251  1.00 39.03  ? 193 ASP D OD2 1 
ATOM   7272 N N   . MET D  1 179 ? 18.048 22.252  59.104  1.00 34.66  ? 194 MET D N   1 
ATOM   7273 C CA  . MET D  1 179 ? 17.429 21.041  59.688  1.00 34.88  ? 194 MET D CA  1 
ATOM   7274 C C   . MET D  1 179 ? 16.110 20.735  58.974  1.00 36.05  ? 194 MET D C   1 
ATOM   7275 O O   . MET D  1 179 ? 15.509 21.648  58.341  1.00 38.12  ? 194 MET D O   1 
ATOM   7276 C CB  . MET D  1 179 ? 17.186 21.200  61.191  1.00 33.31  ? 194 MET D CB  1 
ATOM   7277 C CG  . MET D  1 179 ? 18.459 21.437  61.982  1.00 33.41  ? 194 MET D CG  1 
ATOM   7278 S SD  . MET D  1 179 ? 18.110 22.004  63.662  1.00 32.65  ? 194 MET D SD  1 
ATOM   7279 C CE  . MET D  1 179 ? 19.733 22.566  64.163  1.00 32.26  ? 194 MET D CE  1 
ATOM   7280 N N   . LEU D  1 180 ? 15.711 19.474  59.067  1.00 36.24  ? 195 LEU D N   1 
ATOM   7281 C CA  . LEU D  1 180 ? 14.496 18.896  58.448  1.00 36.87  ? 195 LEU D CA  1 
ATOM   7282 C C   . LEU D  1 180 ? 13.810 18.096  59.554  1.00 36.15  ? 195 LEU D C   1 
ATOM   7283 O O   . LEU D  1 180 ? 14.523 17.506  60.387  1.00 37.26  ? 195 LEU D O   1 
ATOM   7284 C CB  . LEU D  1 180 ? 14.914 18.036  57.249  1.00 36.48  ? 195 LEU D CB  1 
ATOM   7285 C CG  . LEU D  1 180 ? 13.788 17.385  56.444  1.00 37.84  ? 195 LEU D CG  1 
ATOM   7286 C CD1 . LEU D  1 180 ? 14.209 17.192  54.998  1.00 39.01  ? 195 LEU D CD1 1 
ATOM   7287 C CD2 . LEU D  1 180 ? 13.356 16.048  57.032  1.00 39.18  ? 195 LEU D CD2 1 
ATOM   7288 N N   . CYS D  1 181 ? 12.482 18.081  59.539  1.00 35.94  ? 196 CYS D N   1 
ATOM   7289 C CA  A CYS D  1 181 ? 11.640 17.493  60.617  0.50 35.54  ? 196 CYS D CA  1 
ATOM   7290 C CA  B CYS D  1 181 ? 11.639 17.499  60.606  0.50 36.79  ? 196 CYS D CA  1 
ATOM   7291 C C   . CYS D  1 181 ? 10.760 16.377  60.038  1.00 35.17  ? 196 CYS D C   1 
ATOM   7292 O O   . CYS D  1 181 ? 10.153 16.590  58.972  1.00 35.74  ? 196 CYS D O   1 
ATOM   7293 C CB  A CYS D  1 181 ? 10.757 18.551  61.277  0.50 36.47  ? 196 CYS D CB  1 
ATOM   7294 C CB  B CYS D  1 181 ? 10.804 18.613  61.210  0.50 39.55  ? 196 CYS D CB  1 
ATOM   7295 S SG  A CYS D  1 181 ? 11.600 19.534  62.544  0.50 36.61  ? 196 CYS D SG  1 
ATOM   7296 S SG  B CYS D  1 181 ? 9.684  18.027  62.496  0.50 42.07  ? 196 CYS D SG  1 
ATOM   7297 N N   . ALA D  1 182 ? 10.697 15.238  60.733  1.00 35.26  ? 197 ALA D N   1 
ATOM   7298 C CA  . ALA D  1 182 ? 9.897  14.061  60.327  1.00 34.63  ? 197 ALA D CA  1 
ATOM   7299 C C   . ALA D  1 182 ? 9.561  13.189  61.536  1.00 35.10  ? 197 ALA D C   1 
ATOM   7300 O O   . ALA D  1 182 ? 10.361 13.143  62.496  1.00 34.50  ? 197 ALA D O   1 
ATOM   7301 C CB  . ALA D  1 182 ? 10.631 13.274  59.273  1.00 35.57  ? 197 ALA D CB  1 
ATOM   7302 N N   . GLY D  1 183 ? 8.410  12.514  61.468  1.00 34.58  ? 198 GLY D N   1 
ATOM   7303 C CA  . GLY D  1 183 ? 7.971  11.521  62.462  1.00 34.64  ? 198 GLY D CA  1 
ATOM   7304 C C   . GLY D  1 183 ? 6.801  12.013  63.287  1.00 35.34  ? 198 GLY D C   1 
ATOM   7305 O O   . GLY D  1 183 ? 6.418  13.186  63.150  1.00 38.00  ? 198 GLY D O   1 
ATOM   7306 N N   . ASN D  1 184 ? 6.262  11.125  64.121  1.00 36.83  ? 199 ASN D N   1 
ATOM   7307 C CA  . ASN D  1 184 ? 5.094  11.369  65.007  1.00 37.72  ? 199 ASN D CA  1 
ATOM   7308 C C   . ASN D  1 184 ? 5.245  10.465  66.239  1.00 38.19  ? 199 ASN D C   1 
ATOM   7309 O O   . ASN D  1 184 ? 6.351  9.942   66.434  1.00 41.16  ? 199 ASN D O   1 
ATOM   7310 C CB  . ASN D  1 184 ? 3.792  11.189  64.219  1.00 36.62  ? 199 ASN D CB  1 
ATOM   7311 C CG  . ASN D  1 184 ? 3.608  9.810   63.616  1.00 35.42  ? 199 ASN D CG  1 
ATOM   7312 O OD1 . ASN D  1 184 ? 4.097  8.800   64.124  1.00 35.72  ? 199 ASN D OD1 1 
ATOM   7313 N ND2 . ASN D  1 184 ? 2.837  9.744   62.545  1.00 36.82  ? 199 ASN D ND2 1 
ATOM   7314 N N   . THR D  1 185 ? 4.176  10.260  67.012  1.00 39.11  ? 200 THR D N   1 
ATOM   7315 C CA  . THR D  1 185 ? 4.174  9.478   68.278  1.00 41.51  ? 200 THR D CA  1 
ATOM   7316 C C   . THR D  1 185 ? 4.187  7.967   67.996  1.00 40.63  ? 200 THR D C   1 
ATOM   7317 O O   . THR D  1 185 ? 4.325  7.211   68.967  1.00 42.23  ? 200 THR D O   1 
ATOM   7318 C CB  . THR D  1 185 ? 2.987  9.887   69.164  1.00 41.61  ? 200 THR D CB  1 
ATOM   7319 O OG1 . THR D  1 185 ? 1.787  9.769   68.401  1.00 43.10  ? 200 THR D OG1 1 
ATOM   7320 C CG2 . THR D  1 185 ? 3.101  11.308  69.675  1.00 42.49  ? 200 THR D CG2 1 
ATOM   7321 N N   . ARG D  1 186 ? 4.045  7.534   66.741  1.00 42.51  ? 201 ARG D N   1 
ATOM   7322 C CA  . ARG D  1 186 ? 4.099  6.096   66.357  1.00 43.89  ? 201 ARG D CA  1 
ATOM   7323 C C   . ARG D  1 186 ? 5.362  5.782   65.542  1.00 42.13  ? 201 ARG D C   1 
ATOM   7324 O O   . ARG D  1 186 ? 5.781  4.625   65.563  1.00 40.81  ? 201 ARG D O   1 
ATOM   7325 C CB  . ARG D  1 186 ? 2.833  5.720   65.585  1.00 45.21  ? 201 ARG D CB  1 
ATOM   7326 C CG  . ARG D  1 186 ? 1.567  5.775   66.427  1.00 49.86  ? 201 ARG D CG  1 
ATOM   7327 C CD  . ARG D  1 186 ? 0.329  5.566   65.579  1.00 52.65  ? 201 ARG D CD  1 
ATOM   7328 N NE  . ARG D  1 186 ? 0.099  6.707   64.697  1.00 57.89  ? 201 ARG D NE  1 
ATOM   7329 C CZ  . ARG D  1 186 ? -0.459 7.870   65.048  1.00 60.70  ? 201 ARG D CZ  1 
ATOM   7330 N NH1 . ARG D  1 186 ? -0.874 8.087   66.287  1.00 62.47  ? 201 ARG D NH1 1 
ATOM   7331 N NH2 . ARG D  1 186 ? -0.608 8.822   64.140  1.00 63.31  ? 201 ARG D NH2 1 
ATOM   7332 N N   . ARG D  1 187 ? 5.944  6.763   64.851  1.00 41.27  ? 202 ARG D N   1 
ATOM   7333 C CA  . ARG D  1 187 ? 6.981  6.554   63.804  1.00 40.18  ? 202 ARG D CA  1 
ATOM   7334 C C   . ARG D  1 187 ? 8.121  7.551   64.020  1.00 39.29  ? 202 ARG D C   1 
ATOM   7335 O O   . ARG D  1 187 ? 7.859  8.769   63.922  1.00 39.46  ? 202 ARG D O   1 
ATOM   7336 C CB  . ARG D  1 187 ? 6.338  6.734   62.429  1.00 41.66  ? 202 ARG D CB  1 
ATOM   7337 C CG  . ARG D  1 187 ? 5.208  5.758   62.145  1.00 45.27  ? 202 ARG D CG  1 
ATOM   7338 C CD  . ARG D  1 187 ? 4.283  6.290   61.071  1.00 48.98  ? 202 ARG D CD  1 
ATOM   7339 N NE  . ARG D  1 187 ? 3.334  5.271   60.644  1.00 52.70  ? 202 ARG D NE  1 
ATOM   7340 C CZ  . ARG D  1 187 ? 3.605  4.246   59.835  1.00 54.91  ? 202 ARG D CZ  1 
ATOM   7341 N NH1 . ARG D  1 187 ? 4.817  4.076   59.326  1.00 57.05  ? 202 ARG D NH1 1 
ATOM   7342 N NH2 . ARG D  1 187 ? 2.648  3.383   59.535  1.00 57.62  ? 202 ARG D NH2 1 
ATOM   7343 N N   . ASP D  1 188 ? 9.326  7.067   64.333  1.00 37.82  ? 203 ASP D N   1 
ATOM   7344 C CA  . ASP D  1 188 ? 10.493 7.949   64.608  1.00 36.62  ? 203 ASP D CA  1 
ATOM   7345 C C   . ASP D  1 188 ? 11.792 7.137   64.555  1.00 37.79  ? 203 ASP D C   1 
ATOM   7346 O O   . ASP D  1 188 ? 11.742 5.890   64.592  1.00 38.38  ? 203 ASP D O   1 
ATOM   7347 C CB  . ASP D  1 188 ? 10.345 8.663   65.960  1.00 36.90  ? 203 ASP D CB  1 
ATOM   7348 C CG  . ASP D  1 188 ? 11.124 9.967   66.120  1.00 38.05  ? 203 ASP D CG  1 
ATOM   7349 O OD1 . ASP D  1 188 ? 11.850 10.357  65.174  1.00 39.77  ? 203 ASP D OD1 1 
ATOM   7350 O OD2 . ASP D  1 188 ? 10.985 10.601  67.193  1.00 39.15  ? 203 ASP D OD2 1 
ATOM   7351 N N   . SER D  1 189 ? 12.910 7.843   64.420  1.00 37.65  ? 204 SER D N   1 
ATOM   7352 C CA  . SER D  1 189 ? 14.275 7.330   64.666  1.00 38.77  ? 204 SER D CA  1 
ATOM   7353 C C   . SER D  1 189 ? 14.561 7.492   66.159  1.00 39.28  ? 204 SER D C   1 
ATOM   7354 O O   . SER D  1 189 ? 13.832 8.256   66.835  1.00 35.51  ? 204 SER D O   1 
ATOM   7355 C CB  . SER D  1 189 ? 15.286 8.049   63.815  1.00 40.15  ? 204 SER D CB  1 
ATOM   7356 O OG  . SER D  1 189 ? 15.249 9.448   64.065  1.00 40.89  ? 204 SER D OG  1 
ATOM   7357 N N   . CYS D  1 190 ? 15.567 6.784   66.661  1.00 36.92  ? 205 CYS D N   1 
ATOM   7358 C CA  . CYS D  1 190 ? 15.916 6.766   68.099  1.00 39.02  ? 205 CYS D CA  1 
ATOM   7359 C C   . CYS D  1 190 ? 17.431 6.606   68.270  1.00 36.69  ? 205 CYS D C   1 
ATOM   7360 O O   . CYS D  1 190 ? 18.153 6.677   67.253  1.00 35.77  ? 205 CYS D O   1 
ATOM   7361 C CB  . CYS D  1 190 ? 15.110 5.682   68.803  1.00 40.59  ? 205 CYS D CB  1 
ATOM   7362 S SG  . CYS D  1 190 ? 14.847 6.000   70.568  1.00 46.29  ? 205 CYS D SG  1 
ATOM   7363 N N   . GLN D  1 191 ? 17.887 6.476   69.519  1.00 39.18  ? 206 GLN D N   1 
ATOM   7364 C CA  . GLN D  1 191 ? 19.321 6.336   69.891  1.00 38.48  ? 206 GLN D CA  1 
ATOM   7365 C C   . GLN D  1 191 ? 19.897 5.134   69.130  1.00 35.19  ? 206 GLN D C   1 
ATOM   7366 O O   . GLN D  1 191 ? 19.273 4.063   69.175  1.00 35.23  ? 206 GLN D O   1 
ATOM   7367 C CB  . GLN D  1 191 ? 19.468 6.164   71.408  1.00 42.65  ? 206 GLN D CB  1 
ATOM   7368 C CG  . GLN D  1 191 ? 19.417 7.465   72.200  1.00 47.76  ? 206 GLN D CG  1 
ATOM   7369 C CD  . GLN D  1 191 ? 18.067 8.146   72.256  1.00 49.66  ? 206 GLN D CD  1 
ATOM   7370 O OE1 . GLN D  1 191 ? 17.937 9.332   71.964  1.00 54.90  ? 206 GLN D OE1 1 
ATOM   7371 N NE2 . GLN D  1 191 ? 17.045 7.413   72.662  1.00 50.44  ? 206 GLN D NE2 1 
ATOM   7372 N N   . GLY D  1 192 ? 21.017 5.321   68.429  1.00 33.99  ? 207 GLY D N   1 
ATOM   7373 C CA  . GLY D  1 192 ? 21.661 4.293   67.585  1.00 33.74  ? 207 GLY D CA  1 
ATOM   7374 C C   . GLY D  1 192 ? 21.335 4.454   66.108  1.00 33.24  ? 207 GLY D C   1 
ATOM   7375 O O   . GLY D  1 192 ? 22.067 3.869   65.294  1.00 34.63  ? 207 GLY D O   1 
ATOM   7376 N N   . ASP D  1 193 ? 20.283 5.210   65.757  1.00 33.73  ? 208 ASP D N   1 
ATOM   7377 C CA  . ASP D  1 193 ? 19.923 5.523   64.351  1.00 33.38  ? 208 ASP D CA  1 
ATOM   7378 C C   . ASP D  1 193 ? 20.676 6.773   63.878  1.00 33.72  ? 208 ASP D C   1 
ATOM   7379 O O   . ASP D  1 193 ? 20.720 6.960   62.653  1.00 34.47  ? 208 ASP D O   1 
ATOM   7380 C CB  . ASP D  1 193 ? 18.419 5.707   64.169  1.00 35.83  ? 208 ASP D CB  1 
ATOM   7381 C CG  . ASP D  1 193 ? 17.618 4.447   64.452  1.00 36.99  ? 208 ASP D CG  1 
ATOM   7382 O OD1 . ASP D  1 193 ? 18.067 3.360   64.040  1.00 35.65  ? 208 ASP D OD1 1 
ATOM   7383 O OD2 . ASP D  1 193 ? 16.556 4.556   65.098  1.00 37.61  ? 208 ASP D OD2 1 
ATOM   7384 N N   . SER D  1 194 ? 21.242 7.568   64.801  1.00 32.88  ? 209 SER D N   1 
ATOM   7385 C CA  . SER D  1 194 ? 22.006 8.815   64.524  1.00 32.62  ? 209 SER D CA  1 
ATOM   7386 C C   . SER D  1 194 ? 23.012 8.596   63.395  1.00 32.03  ? 209 SER D C   1 
ATOM   7387 O O   . SER D  1 194 ? 23.692 7.545   63.396  1.00 33.14  ? 209 SER D O   1 
ATOM   7388 C CB  . SER D  1 194 ? 22.712 9.334   65.746  1.00 34.79  ? 209 SER D CB  1 
ATOM   7389 O OG  . SER D  1 194 ? 21.814 10.043  66.586  1.00 38.90  ? 209 SER D OG  1 
ATOM   7390 N N   . GLY D  1 195 ? 23.104 9.566   62.479  1.00 29.60  ? 210 GLY D N   1 
ATOM   7391 C CA  . GLY D  1 195 ? 24.021 9.538   61.326  1.00 30.20  ? 210 GLY D CA  1 
ATOM   7392 C C   . GLY D  1 195 ? 23.442 8.783   60.141  1.00 29.22  ? 210 GLY D C   1 
ATOM   7393 O O   . GLY D  1 195 ? 23.983 8.940   59.041  1.00 29.35  ? 210 GLY D O   1 
ATOM   7394 N N   . GLY D  1 196 ? 22.384 7.997   60.352  1.00 30.44  ? 211 GLY D N   1 
ATOM   7395 C CA  . GLY D  1 196 ? 21.745 7.175   59.319  1.00 29.14  ? 211 GLY D CA  1 
ATOM   7396 C C   . GLY D  1 196 ? 20.898 8.028   58.384  1.00 31.22  ? 211 GLY D C   1 
ATOM   7397 O O   . GLY D  1 196 ? 20.670 9.213   58.631  1.00 32.04  ? 211 GLY D O   1 
ATOM   7398 N N   . PRO D  1 197 ? 20.407 7.434   57.276  1.00 32.31  ? 212 PRO D N   1 
ATOM   7399 C CA  . PRO D  1 197 ? 19.726 8.190   56.234  1.00 31.81  ? 212 PRO D CA  1 
ATOM   7400 C C   . PRO D  1 197 ? 18.212 8.314   56.429  1.00 33.51  ? 212 PRO D C   1 
ATOM   7401 O O   . PRO D  1 197 ? 17.578 7.360   56.859  1.00 34.88  ? 212 PRO D O   1 
ATOM   7402 C CB  . PRO D  1 197 ? 20.076 7.355   55.000  1.00 31.19  ? 212 PRO D CB  1 
ATOM   7403 C CG  . PRO D  1 197 ? 20.071 5.924   55.506  1.00 31.20  ? 212 PRO D CG  1 
ATOM   7404 C CD  . PRO D  1 197 ? 20.514 6.000   56.950  1.00 32.39  ? 212 PRO D CD  1 
ATOM   7405 N N   . LEU D  1 198 ? 17.693 9.506   56.132  1.00 34.80  ? 213 LEU D N   1 
ATOM   7406 C CA  . LEU D  1 198 ? 16.274 9.744   55.769  1.00 35.43  ? 213 LEU D CA  1 
ATOM   7407 C C   . LEU D  1 198 ? 16.224 9.871   54.245  1.00 34.24  ? 213 LEU D C   1 
ATOM   7408 O O   . LEU D  1 198 ? 16.882 10.795  53.705  1.00 32.81  ? 213 LEU D O   1 
ATOM   7409 C CB  . LEU D  1 198 ? 15.767 11.013  56.461  1.00 35.84  ? 213 LEU D CB  1 
ATOM   7410 C CG  . LEU D  1 198 ? 14.303 11.370  56.205  1.00 36.04  ? 213 LEU D CG  1 
ATOM   7411 C CD1 . LEU D  1 198 ? 13.373 10.351  56.836  1.00 39.31  ? 213 LEU D CD1 1 
ATOM   7412 C CD2 . LEU D  1 198 ? 13.994 12.752  56.740  1.00 38.22  ? 213 LEU D CD2 1 
ATOM   7413 N N   . VAL D  1 199 ? 15.503 8.962   53.586  1.00 33.55  ? 214 VAL D N   1 
ATOM   7414 C CA  . VAL D  1 199 ? 15.461 8.847   52.099  1.00 35.28  ? 214 VAL D CA  1 
ATOM   7415 C C   . VAL D  1 199 ? 14.014 9.032   51.631  1.00 37.34  ? 214 VAL D C   1 
ATOM   7416 O O   . VAL D  1 199 ? 13.101 8.499   52.280  1.00 36.34  ? 214 VAL D O   1 
ATOM   7417 C CB  . VAL D  1 199 ? 16.082 7.527   51.599  1.00 36.12  ? 214 VAL D CB  1 
ATOM   7418 C CG1 . VAL D  1 199 ? 17.574 7.497   51.867  1.00 36.04  ? 214 VAL D CG1 1 
ATOM   7419 C CG2 . VAL D  1 199 ? 15.417 6.284   52.185  1.00 36.43  ? 214 VAL D CG2 1 
ATOM   7420 N N   . CYS D  1 200 ? 13.819 9.824   50.574  1.00 41.40  ? 215 CYS D N   1 
ATOM   7421 C CA  . CYS D  1 200 ? 12.501 10.088  49.939  1.00 43.93  ? 215 CYS D CA  1 
ATOM   7422 C C   . CYS D  1 200 ? 12.580 9.676   48.466  1.00 41.77  ? 215 CYS D C   1 
ATOM   7423 O O   . CYS D  1 200 ? 13.592 9.990   47.812  1.00 38.27  ? 215 CYS D O   1 
ATOM   7424 C CB  . CYS D  1 200 ? 12.088 11.550  50.077  1.00 45.29  ? 215 CYS D CB  1 
ATOM   7425 S SG  . CYS D  1 200 ? 12.220 12.182  51.770  1.00 51.49  ? 215 CYS D SG  1 
ATOM   7426 N N   . LYS D  1 201 ? 11.560 8.961   47.992  1.00 44.06  ? 216 LYS D N   1 
ATOM   7427 C CA  . LYS D  1 201 ? 11.449 8.472   46.597  1.00 46.13  ? 216 LYS D CA  1 
ATOM   7428 C C   . LYS D  1 201 ? 10.838 9.595   45.750  1.00 46.43  ? 216 LYS D C   1 
ATOM   7429 O O   . LYS D  1 201 ? 9.665  9.946   46.004  1.00 48.21  ? 216 LYS D O   1 
ATOM   7430 C CB  . LYS D  1 201 ? 10.611 7.188   46.580  1.00 47.54  ? 216 LYS D CB  1 
ATOM   7431 C CG  . LYS D  1 201 ? 10.735 6.339   45.322  1.00 52.68  ? 216 LYS D CG  1 
ATOM   7432 C CD  . LYS D  1 201 ? 9.885  5.078   45.394  1.00 55.03  ? 216 LYS D CD  1 
ATOM   7433 C CE  . LYS D  1 201 ? 9.866  4.265   44.117  1.00 58.00  ? 216 LYS D CE  1 
ATOM   7434 N NZ  . LYS D  1 201 ? 10.992 3.304   44.049  1.00 59.03  ? 216 LYS D NZ  1 
ATOM   7435 N N   . VAL D  1 202 ? 11.630 10.192  44.850  1.00 44.72  ? 217 VAL D N   1 
ATOM   7436 C CA  . VAL D  1 202 ? 11.248 11.394  44.044  1.00 44.27  ? 217 VAL D CA  1 
ATOM   7437 C C   . VAL D  1 202 ? 11.436 11.049  42.563  1.00 44.39  ? 217 VAL D C   1 
ATOM   7438 O O   . VAL D  1 202 ? 12.603 10.881  42.156  1.00 43.95  ? 217 VAL D O   1 
ATOM   7439 C CB  . VAL D  1 202 ? 12.068 12.631  44.466  1.00 44.27  ? 217 VAL D CB  1 
ATOM   7440 C CG1 . VAL D  1 202 ? 11.675 13.882  43.686  1.00 43.71  ? 217 VAL D CG1 1 
ATOM   7441 C CG2 . VAL D  1 202 ? 11.962 12.886  45.962  1.00 42.16  ? 217 VAL D CG2 1 
ATOM   7442 N N   . ASN D  1 203 ? 10.335 10.923  41.806  1.00 47.39  ? 218 ASN D N   1 
ATOM   7443 C CA  . ASN D  1 203 ? 10.331 10.583  40.354  1.00 51.52  ? 218 ASN D CA  1 
ATOM   7444 C C   . ASN D  1 203 ? 11.101 9.276   40.134  1.00 50.12  ? 218 ASN D C   1 
ATOM   7445 O O   . ASN D  1 203 ? 11.991 9.249   39.259  1.00 49.05  ? 218 ASN D O   1 
ATOM   7446 C CB  . ASN D  1 203 ? 10.888 11.735  39.510  1.00 56.22  ? 218 ASN D CB  1 
ATOM   7447 C CG  . ASN D  1 203 ? 10.108 13.024  39.683  1.00 63.90  ? 218 ASN D CG  1 
ATOM   7448 O OD1 . ASN D  1 203 ? 8.956  13.005  40.111  1.00 70.35  ? 218 ASN D OD1 1 
ATOM   7449 N ND2 . ASN D  1 203 ? 10.723 14.153  39.363  1.00 69.54  ? 218 ASN D ND2 1 
ATOM   7450 N N   . GLY D  1 204 ? 10.794 8.254   40.940  1.00 49.60  ? 219 GLY D N   1 
ATOM   7451 C CA  . GLY D  1 204 ? 11.365 6.900   40.833  1.00 48.79  ? 219 GLY D CA  1 
ATOM   7452 C C   . GLY D  1 204 ? 12.768 6.777   41.409  1.00 50.41  ? 219 GLY D C   1 
ATOM   7453 O O   . GLY D  1 204 ? 13.240 5.629   41.468  1.00 49.65  ? 219 GLY D O   1 
ATOM   7454 N N   . THR D  1 205 ? 13.417 7.865   41.862  1.00 49.54  ? 220 THR D N   1 
ATOM   7455 C CA  . THR D  1 205 ? 14.804 7.841   42.414  1.00 47.81  ? 220 THR D CA  1 
ATOM   7456 C C   . THR D  1 205 ? 14.761 8.104   43.925  1.00 46.04  ? 220 THR D C   1 
ATOM   7457 O O   . THR D  1 205 ? 14.086 9.070   44.345  1.00 43.29  ? 220 THR D O   1 
ATOM   7458 C CB  . THR D  1 205 ? 15.719 8.821   41.667  1.00 48.97  ? 220 THR D CB  1 
ATOM   7459 O OG1 . THR D  1 205 ? 15.749 8.376   40.313  1.00 48.23  ? 220 THR D OG1 1 
ATOM   7460 C CG2 . THR D  1 205 ? 17.143 8.876   42.183  1.00 48.60  ? 220 THR D CG2 1 
ATOM   7461 N N   . TRP D  1 206 ? 15.451 7.261   44.700  1.00 43.33  ? 221 TRP D N   1 
ATOM   7462 C CA  . TRP D  1 206 ? 15.697 7.473   46.147  1.00 38.82  ? 221 TRP D CA  1 
ATOM   7463 C C   . TRP D  1 206 ? 16.714 8.600   46.319  1.00 37.89  ? 221 TRP D C   1 
ATOM   7464 O O   . TRP D  1 206 ? 17.824 8.479   45.764  1.00 35.76  ? 221 TRP D O   1 
ATOM   7465 C CB  . TRP D  1 206 ? 16.160 6.177   46.825  1.00 38.82  ? 221 TRP D CB  1 
ATOM   7466 C CG  . TRP D  1 206 ? 15.052 5.181   46.935  1.00 37.11  ? 221 TRP D CG  1 
ATOM   7467 C CD1 . TRP D  1 206 ? 14.844 4.098   46.134  1.00 38.38  ? 221 TRP D CD1 1 
ATOM   7468 C CD2 . TRP D  1 206 ? 13.956 5.218   47.864  1.00 36.36  ? 221 TRP D CD2 1 
ATOM   7469 N NE1 . TRP D  1 206 ? 13.701 3.451   46.510  1.00 38.71  ? 221 TRP D NE1 1 
ATOM   7470 C CE2 . TRP D  1 206 ? 13.132 4.113   47.566  1.00 37.02  ? 221 TRP D CE2 1 
ATOM   7471 C CE3 . TRP D  1 206 ? 13.591 6.073   48.913  1.00 36.70  ? 221 TRP D CE3 1 
ATOM   7472 C CZ2 . TRP D  1 206 ? 11.973 3.834   48.290  1.00 36.98  ? 221 TRP D CZ2 1 
ATOM   7473 C CZ3 . TRP D  1 206 ? 12.442 5.802   49.622  1.00 37.12  ? 221 TRP D CZ3 1 
ATOM   7474 C CH2 . TRP D  1 206 ? 11.642 4.700   49.309  1.00 37.05  ? 221 TRP D CH2 1 
ATOM   7475 N N   . LEU D  1 207 ? 16.329 9.654   47.044  1.00 36.70  ? 222 LEU D N   1 
ATOM   7476 C CA  . LEU D  1 207 ? 17.218 10.797  47.388  1.00 36.97  ? 222 LEU D CA  1 
ATOM   7477 C C   . LEU D  1 207 ? 17.370 10.857  48.909  1.00 35.41  ? 222 LEU D C   1 
ATOM   7478 O O   . LEU D  1 207 ? 16.346 10.739  49.607  1.00 34.99  ? 222 LEU D O   1 
ATOM   7479 C CB  . LEU D  1 207 ? 16.620 12.097  46.832  1.00 37.09  ? 222 LEU D CB  1 
ATOM   7480 C CG  . LEU D  1 207 ? 16.393 12.152  45.321  1.00 37.44  ? 222 LEU D CG  1 
ATOM   7481 C CD1 . LEU D  1 207 ? 15.765 13.484  44.926  1.00 37.77  ? 222 LEU D CD1 1 
ATOM   7482 C CD2 . LEU D  1 207 ? 17.688 11.935  44.545  1.00 37.45  ? 222 LEU D CD2 1 
ATOM   7483 N N   . GLN D  1 208 ? 18.590 11.064  49.411  1.00 34.17  ? 223 GLN D N   1 
ATOM   7484 C CA  . GLN D  1 208 ? 18.817 11.286  50.861  1.00 34.03  ? 223 GLN D CA  1 
ATOM   7485 C C   . GLN D  1 208 ? 18.458 12.736  51.210  1.00 34.48  ? 223 GLN D C   1 
ATOM   7486 O O   . GLN D  1 208 ? 19.258 13.638  50.922  1.00 36.28  ? 223 GLN D O   1 
ATOM   7487 C CB  . GLN D  1 208 ? 20.238 10.926  51.295  1.00 34.21  ? 223 GLN D CB  1 
ATOM   7488 C CG  . GLN D  1 208 ? 20.376 10.954  52.814  1.00 33.91  ? 223 GLN D CG  1 
ATOM   7489 C CD  . GLN D  1 208 ? 21.617 10.304  53.372  1.00 34.39  ? 223 GLN D CD  1 
ATOM   7490 O OE1 . GLN D  1 208 ? 22.388 9.649   52.671  1.00 33.70  ? 223 GLN D OE1 1 
ATOM   7491 N NE2 . GLN D  1 208 ? 21.813 10.491  54.666  1.00 33.35  ? 223 GLN D NE2 1 
ATOM   7492 N N   . ALA D  1 209 ? 17.301 12.935  51.841  1.00 34.95  ? 224 ALA D N   1 
ATOM   7493 C CA  . ALA D  1 209 ? 16.818 14.237  52.357  1.00 33.96  ? 224 ALA D CA  1 
ATOM   7494 C C   . ALA D  1 209 ? 17.566 14.628  53.642  1.00 33.58  ? 224 ALA D C   1 
ATOM   7495 O O   . ALA D  1 209 ? 17.856 15.825  53.806  1.00 34.22  ? 224 ALA D O   1 
ATOM   7496 C CB  . ALA D  1 209 ? 15.332 14.158  52.601  1.00 34.76  ? 224 ALA D CB  1 
ATOM   7497 N N   . GLY D  1 210 ? 17.882 13.656  54.505  1.00 33.07  ? 225 GLY D N   1 
ATOM   7498 C CA  . GLY D  1 210 ? 18.256 13.910  55.908  1.00 33.36  ? 225 GLY D CA  1 
ATOM   7499 C C   . GLY D  1 210 ? 19.321 12.975  56.449  1.00 31.42  ? 225 GLY D C   1 
ATOM   7500 O O   . GLY D  1 210 ? 19.464 11.849  55.954  1.00 28.15  ? 225 GLY D O   1 
ATOM   7501 N N   . VAL D  1 211 ? 20.042 13.458  57.456  1.00 33.00  ? 226 VAL D N   1 
ATOM   7502 C CA  . VAL D  1 211 ? 20.917 12.663  58.367  1.00 31.83  ? 226 VAL D CA  1 
ATOM   7503 C C   . VAL D  1 211 ? 20.261 12.706  59.748  1.00 31.44  ? 226 VAL D C   1 
ATOM   7504 O O   . VAL D  1 211 ? 19.974 13.829  60.208  1.00 32.73  ? 226 VAL D O   1 
ATOM   7505 C CB  . VAL D  1 211 ? 22.345 13.235  58.399  1.00 31.73  ? 226 VAL D CB  1 
ATOM   7506 C CG1 . VAL D  1 211 ? 23.244 12.461  59.356  1.00 31.57  ? 226 VAL D CG1 1 
ATOM   7507 C CG2 . VAL D  1 211 ? 22.959 13.301  57.009  1.00 31.45  ? 226 VAL D CG2 1 
ATOM   7508 N N   . VAL D  1 212 ? 20.021 11.547  60.370  1.00 31.41  ? 227 VAL D N   1 
ATOM   7509 C CA  . VAL D  1 212 ? 19.407 11.458  61.729  1.00 31.78  ? 227 VAL D CA  1 
ATOM   7510 C C   . VAL D  1 212 ? 20.297 12.274  62.678  1.00 31.11  ? 227 VAL D C   1 
ATOM   7511 O O   . VAL D  1 212 ? 21.497 11.960  62.751  1.00 28.24  ? 227 VAL D O   1 
ATOM   7512 C CB  . VAL D  1 212 ? 19.233 10.003  62.206  1.00 32.38  ? 227 VAL D CB  1 
ATOM   7513 C CG1 . VAL D  1 212 ? 18.672 9.944   63.618  1.00 34.34  ? 227 VAL D CG1 1 
ATOM   7514 C CG2 . VAL D  1 212 ? 18.347 9.185   61.279  1.00 34.31  ? 227 VAL D CG2 1 
ATOM   7515 N N   . SER D  1 213 ? 19.747 13.311  63.326  1.00 29.74  ? 228 SER D N   1 
ATOM   7516 C CA  . SER D  1 213 ? 20.532 14.308  64.103  1.00 29.19  ? 228 SER D CA  1 
ATOM   7517 C C   . SER D  1 213 ? 20.131 14.278  65.579  1.00 29.83  ? 228 SER D C   1 
ATOM   7518 O O   . SER D  1 213 ? 20.963 13.860  66.393  1.00 32.35  ? 228 SER D O   1 
ATOM   7519 C CB  . SER D  1 213 ? 20.404 15.684  63.518  1.00 28.94  ? 228 SER D CB  1 
ATOM   7520 O OG  . SER D  1 213 ? 21.270 16.579  64.195  1.00 29.39  ? 228 SER D OG  1 
ATOM   7521 N N   . TRP D  1 214 ? 18.928 14.746  65.929  1.00 29.06  ? 229 TRP D N   1 
ATOM   7522 C CA  . TRP D  1 214 ? 18.535 14.932  67.349  1.00 29.84  ? 229 TRP D CA  1 
ATOM   7523 C C   . TRP D  1 214 ? 17.016 14.985  67.509  1.00 31.02  ? 229 TRP D C   1 
ATOM   7524 O O   . TRP D  1 214 ? 16.283 14.989  66.503  1.00 32.76  ? 229 TRP D O   1 
ATOM   7525 C CB  . TRP D  1 214 ? 19.224 16.161  67.964  1.00 30.14  ? 229 TRP D CB  1 
ATOM   7526 C CG  . TRP D  1 214 ? 18.800 17.487  67.411  1.00 29.57  ? 229 TRP D CG  1 
ATOM   7527 C CD1 . TRP D  1 214 ? 19.227 18.078  66.261  1.00 29.84  ? 229 TRP D CD1 1 
ATOM   7528 C CD2 . TRP D  1 214 ? 17.897 18.425  68.023  1.00 29.62  ? 229 TRP D CD2 1 
ATOM   7529 N NE1 . TRP D  1 214 ? 18.632 19.299  66.093  1.00 30.76  ? 229 TRP D NE1 1 
ATOM   7530 C CE2 . TRP D  1 214 ? 17.809 19.541  67.160  1.00 30.05  ? 229 TRP D CE2 1 
ATOM   7531 C CE3 . TRP D  1 214 ? 17.144 18.422  69.202  1.00 31.08  ? 229 TRP D CE3 1 
ATOM   7532 C CZ2 . TRP D  1 214 ? 17.007 20.644  67.451  1.00 31.27  ? 229 TRP D CZ2 1 
ATOM   7533 C CZ3 . TRP D  1 214 ? 16.347 19.510  69.486  1.00 32.00  ? 229 TRP D CZ3 1 
ATOM   7534 C CH2 . TRP D  1 214 ? 16.285 20.607  68.624  1.00 31.14  ? 229 TRP D CH2 1 
ATOM   7535 N N   . GLY D  1 215 ? 16.583 15.001  68.764  1.00 34.13  ? 230 GLY D N   1 
ATOM   7536 C CA  . GLY D  1 215 ? 15.188 15.252  69.164  1.00 35.27  ? 230 GLY D CA  1 
ATOM   7537 C C   . GLY D  1 215 ? 15.068 15.166  70.668  1.00 36.33  ? 230 GLY D C   1 
ATOM   7538 O O   . GLY D  1 215 ? 16.060 14.784  71.310  1.00 37.71  ? 230 GLY D O   1 
ATOM   7539 N N   . GLU D  1 216 ? 13.908 15.516  71.217  1.00 37.74  ? 231 GLU D N   1 
ATOM   7540 C CA  . GLU D  1 216 ? 13.599 15.293  72.646  1.00 38.68  ? 231 GLU D CA  1 
ATOM   7541 C C   . GLU D  1 216 ? 13.005 13.889  72.758  1.00 39.98  ? 231 GLU D C   1 
ATOM   7542 O O   . GLU D  1 216 ? 11.814 13.715  72.419  1.00 40.50  ? 231 GLU D O   1 
ATOM   7543 C CB  . GLU D  1 216 ? 12.674 16.378  73.182  1.00 42.49  ? 231 GLU D CB  1 
ATOM   7544 C CG  . GLU D  1 216 ? 12.438 16.253  74.676  1.00 47.71  ? 231 GLU D CG  1 
ATOM   7545 C CD  . GLU D  1 216 ? 11.447 17.257  75.229  1.00 48.61  ? 231 GLU D CD  1 
ATOM   7546 O OE1 . GLU D  1 216 ? 10.613 16.862  76.061  1.00 53.26  ? 231 GLU D OE1 1 
ATOM   7547 O OE2 . GLU D  1 216 ? 11.513 18.426  74.818  1.00 49.66  ? 231 GLU D OE2 1 
ATOM   7548 N N   . GLY D  1 217 ? 13.826 12.923  73.171  1.00 38.56  ? 232 GLY D N   1 
ATOM   7549 C CA  . GLY D  1 217 ? 13.448 11.499  73.208  1.00 39.51  ? 232 GLY D CA  1 
ATOM   7550 C C   . GLY D  1 217 ? 13.073 10.999  71.826  1.00 37.80  ? 232 GLY D C   1 
ATOM   7551 O O   . GLY D  1 217 ? 13.551 11.576  70.823  1.00 37.34  ? 232 GLY D O   1 
ATOM   7552 N N   . CYS D  1 218 ? 12.234 9.967   71.775  1.00 38.22  ? 233 CYS D N   1 
ATOM   7553 C CA  . CYS D  1 218 ? 11.795 9.270   70.539  1.00 38.36  ? 233 CYS D CA  1 
ATOM   7554 C C   . CYS D  1 218 ? 10.271 9.140   70.573  1.00 38.83  ? 233 CYS D C   1 
ATOM   7555 O O   . CYS D  1 218 ? 9.747  8.717   71.623  1.00 37.37  ? 233 CYS D O   1 
ATOM   7556 C CB  . CYS D  1 218 ? 12.460 7.902   70.436  1.00 41.53  ? 233 CYS D CB  1 
ATOM   7557 S SG  . CYS D  1 218 ? 14.249 7.973   70.699  1.00 48.05  ? 233 CYS D SG  1 
ATOM   7558 N N   . ALA D  1 219 ? 9.601  9.552   69.492  1.00 38.33  ? 234 ALA D N   1 
ATOM   7559 C CA  . ALA D  1 219 ? 8.144  9.433   69.276  1.00 39.97  ? 234 ALA D CA  1 
ATOM   7560 C C   . ALA D  1 219 ? 7.366  10.065  70.443  1.00 40.20  ? 234 ALA D C   1 
ATOM   7561 O O   . ALA D  1 219 ? 6.345  9.487   70.835  1.00 41.87  ? 234 ALA D O   1 
ATOM   7562 C CB  . ALA D  1 219 ? 7.806  7.975   69.069  1.00 39.28  ? 234 ALA D CB  1 
ATOM   7563 N N   . GLN D  1 220 ? 7.840  11.200  70.963  1.00 40.76  ? 235 GLN D N   1 
ATOM   7564 C CA  . GLN D  1 220 ? 7.205  11.943  72.081  1.00 42.57  ? 235 GLN D CA  1 
ATOM   7565 C C   . GLN D  1 220 ? 6.257  12.992  71.505  1.00 39.60  ? 235 GLN D C   1 
ATOM   7566 O O   . GLN D  1 220 ? 6.540  13.562  70.451  1.00 38.38  ? 235 GLN D O   1 
ATOM   7567 C CB  . GLN D  1 220 ? 8.260  12.607  72.969  1.00 45.34  ? 235 GLN D CB  1 
ATOM   7568 C CG  . GLN D  1 220 ? 9.205  11.636  73.661  1.00 49.55  ? 235 GLN D CG  1 
ATOM   7569 C CD  . GLN D  1 220 ? 8.510  10.793  74.705  1.00 52.15  ? 235 GLN D CD  1 
ATOM   7570 O OE1 . GLN D  1 220 ? 7.813  9.834   74.386  1.00 51.58  ? 235 GLN D OE1 1 
ATOM   7571 N NE2 . GLN D  1 220 ? 8.695  11.141  75.968  1.00 56.59  ? 235 GLN D NE2 1 
ATOM   7572 N N   . PRO D  1 221 ? 5.115  13.291  72.177  1.00 40.14  ? 236 PRO D N   1 
ATOM   7573 C CA  . PRO D  1 221 ? 4.190  14.333  71.720  1.00 37.87  ? 236 PRO D CA  1 
ATOM   7574 C C   . PRO D  1 221 ? 4.861  15.701  71.494  1.00 37.27  ? 236 PRO D C   1 
ATOM   7575 O O   . PRO D  1 221 ? 5.612  16.126  72.356  1.00 33.89  ? 236 PRO D O   1 
ATOM   7576 C CB  . PRO D  1 221 ? 3.160  14.450  72.858  1.00 38.82  ? 236 PRO D CB  1 
ATOM   7577 C CG  . PRO D  1 221 ? 3.226  13.129  73.594  1.00 39.61  ? 236 PRO D CG  1 
ATOM   7578 C CD  . PRO D  1 221 ? 4.652  12.648  73.422  1.00 40.64  ? 236 PRO D CD  1 
ATOM   7579 N N   . ASN D  1 222 ? 4.599  16.328  70.337  1.00 37.97  ? 237 ASN D N   1 
ATOM   7580 C CA  . ASN D  1 222 ? 5.070  17.691  69.962  1.00 39.35  ? 237 ASN D CA  1 
ATOM   7581 C C   . ASN D  1 222 ? 6.600  17.741  69.841  1.00 38.17  ? 237 ASN D C   1 
ATOM   7582 O O   . ASN D  1 222 ? 7.149  18.871  69.915  1.00 36.41  ? 237 ASN D O   1 
ATOM   7583 C CB  . ASN D  1 222 ? 4.583  18.754  70.957  1.00 38.99  ? 237 ASN D CB  1 
ATOM   7584 C CG  . ASN D  1 222 ? 3.080  18.914  70.975  1.00 41.29  ? 237 ASN D CG  1 
ATOM   7585 O OD1 . ASN D  1 222 ? 2.480  19.047  72.039  1.00 44.76  ? 237 ASN D OD1 1 
ATOM   7586 N ND2 . ASN D  1 222 ? 2.464  18.972  69.808  1.00 40.98  ? 237 ASN D ND2 1 
ATOM   7587 N N   . ARG D  1 223 ? 7.267  16.595  69.642  1.00 38.20  ? 238 ARG D N   1 
ATOM   7588 C CA  . ARG D  1 223 ? 8.750  16.496  69.574  1.00 37.08  ? 238 ARG D CA  1 
ATOM   7589 C C   . ARG D  1 223 ? 9.137  15.564  68.426  1.00 35.73  ? 238 ARG D C   1 
ATOM   7590 O O   . ARG D  1 223 ? 9.687  14.482  68.641  1.00 34.54  ? 238 ARG D O   1 
ATOM   7591 C CB  . ARG D  1 223 ? 9.308  16.048  70.928  1.00 36.60  ? 238 ARG D CB  1 
ATOM   7592 C CG  . ARG D  1 223 ? 9.004  16.998  72.080  1.00 36.91  ? 238 ARG D CG  1 
ATOM   7593 C CD  . ARG D  1 223 ? 9.665  18.364  71.970  1.00 36.29  ? 238 ARG D CD  1 
ATOM   7594 N NE  . ARG D  1 223 ? 9.429  19.151  73.169  1.00 37.20  ? 238 ARG D NE  1 
ATOM   7595 C CZ  . ARG D  1 223 ? 8.417  19.994  73.393  1.00 37.64  ? 238 ARG D CZ  1 
ATOM   7596 N NH1 . ARG D  1 223 ? 7.473  20.209  72.489  1.00 36.84  ? 238 ARG D NH1 1 
ATOM   7597 N NH2 . ARG D  1 223 ? 8.359  20.628  74.554  1.00 36.06  ? 238 ARG D NH2 1 
ATOM   7598 N N   . PRO D  1 224 ? 8.858  15.954  67.162  1.00 35.83  ? 239 PRO D N   1 
ATOM   7599 C CA  . PRO D  1 224 ? 9.269  15.144  66.018  1.00 35.59  ? 239 PRO D CA  1 
ATOM   7600 C C   . PRO D  1 224 ? 10.799 15.065  65.866  1.00 33.42  ? 239 PRO D C   1 
ATOM   7601 O O   . PRO D  1 224 ? 11.499 15.912  66.405  1.00 35.46  ? 239 PRO D O   1 
ATOM   7602 C CB  . PRO D  1 224 ? 8.616  15.794  64.792  1.00 37.23  ? 239 PRO D CB  1 
ATOM   7603 C CG  . PRO D  1 224 ? 7.833  16.999  65.298  1.00 36.93  ? 239 PRO D CG  1 
ATOM   7604 C CD  . PRO D  1 224 ? 8.129  17.171  66.769  1.00 36.54  ? 239 PRO D CD  1 
ATOM   7605 N N   . GLY D  1 225 ? 11.278 14.015  65.195  1.00 32.32  ? 240 GLY D N   1 
ATOM   7606 C CA  . GLY D  1 225 ? 12.711 13.804  64.903  1.00 31.83  ? 240 GLY D CA  1 
ATOM   7607 C C   . GLY D  1 225 ? 13.268 14.952  64.087  1.00 30.42  ? 240 GLY D C   1 
ATOM   7608 O O   . GLY D  1 225 ? 12.562 15.430  63.187  1.00 31.60  ? 240 GLY D O   1 
ATOM   7609 N N   . ILE D  1 226 ? 14.468 15.417  64.425  1.00 31.77  ? 241 ILE D N   1 
ATOM   7610 C CA  . ILE D  1 226 ? 15.208 16.468  63.672  1.00 30.34  ? 241 ILE D CA  1 
ATOM   7611 C C   . ILE D  1 226 ? 16.347 15.782  62.918  1.00 30.89  ? 241 ILE D C   1 
ATOM   7612 O O   . ILE D  1 226 ? 17.042 14.929  63.510  1.00 32.83  ? 241 ILE D O   1 
ATOM   7613 C CB  . ILE D  1 226 ? 15.721 17.579  64.605  1.00 30.74  ? 241 ILE D CB  1 
ATOM   7614 C CG1 . ILE D  1 226 ? 14.672 18.008  65.635  1.00 33.25  ? 241 ILE D CG1 1 
ATOM   7615 C CG2 . ILE D  1 226 ? 16.232 18.759  63.804  1.00 31.10  ? 241 ILE D CG2 1 
ATOM   7616 C CD1 . ILE D  1 226 ? 13.382 18.481  65.038  1.00 34.45  ? 241 ILE D CD1 1 
ATOM   7617 N N   . TYR D  1 227 ? 16.522 16.173  61.661  1.00 31.49  ? 242 TYR D N   1 
ATOM   7618 C CA  . TYR D  1 227 ? 17.517 15.628  60.708  1.00 32.82  ? 242 TYR D CA  1 
ATOM   7619 C C   . TYR D  1 227 ? 18.323 16.798  60.156  1.00 33.38  ? 242 TYR D C   1 
ATOM   7620 O O   . TYR D  1 227 ? 17.732 17.884  60.000  1.00 34.74  ? 242 TYR D O   1 
ATOM   7621 C CB  . TYR D  1 227 ? 16.805 14.879  59.578  1.00 32.23  ? 242 TYR D CB  1 
ATOM   7622 C CG  . TYR D  1 227 ? 15.986 13.695  60.017  1.00 31.24  ? 242 TYR D CG  1 
ATOM   7623 C CD1 . TYR D  1 227 ? 14.761 13.859  60.650  1.00 32.25  ? 242 TYR D CD1 1 
ATOM   7624 C CD2 . TYR D  1 227 ? 16.421 12.401  59.776  1.00 32.89  ? 242 TYR D CD2 1 
ATOM   7625 C CE1 . TYR D  1 227 ? 14.001 12.774  61.054  1.00 32.11  ? 242 TYR D CE1 1 
ATOM   7626 C CE2 . TYR D  1 227 ? 15.673 11.302  60.176  1.00 32.31  ? 242 TYR D CE2 1 
ATOM   7627 C CZ  . TYR D  1 227 ? 14.461 11.489  60.818  1.00 32.91  ? 242 TYR D CZ  1 
ATOM   7628 O OH  . TYR D  1 227 ? 13.720 10.416  61.219  1.00 33.72  ? 242 TYR D OH  1 
ATOM   7629 N N   . THR D  1 228 ? 19.607 16.595  59.873  1.00 32.41  ? 243 THR D N   1 
ATOM   7630 C CA  . THR D  1 228 ? 20.410 17.562  59.088  1.00 33.02  ? 243 THR D CA  1 
ATOM   7631 C C   . THR D  1 228 ? 19.845 17.581  57.664  1.00 32.69  ? 243 THR D C   1 
ATOM   7632 O O   . THR D  1 228 ? 19.673 16.498  57.102  1.00 31.06  ? 243 THR D O   1 
ATOM   7633 C CB  . THR D  1 228 ? 21.907 17.232  59.117  1.00 32.53  ? 243 THR D CB  1 
ATOM   7634 O OG1 . THR D  1 228 ? 22.260 17.025  60.484  1.00 33.60  ? 243 THR D OG1 1 
ATOM   7635 C CG2 . THR D  1 228 ? 22.751 18.332  58.513  1.00 32.87  ? 243 THR D CG2 1 
ATOM   7636 N N   . ARG D  1 229 ? 19.537 18.767  57.132  1.00 32.49  ? 244 ARG D N   1 
ATOM   7637 C CA  . ARG D  1 229 ? 19.026 18.968  55.755  1.00 33.02  ? 244 ARG D CA  1 
ATOM   7638 C C   . ARG D  1 229 ? 20.213 18.851  54.786  1.00 32.25  ? 244 ARG D C   1 
ATOM   7639 O O   . ARG D  1 229 ? 21.086 19.741  54.809  1.00 29.93  ? 244 ARG D O   1 
ATOM   7640 C CB  . ARG D  1 229 ? 18.307 20.321  55.668  1.00 33.59  ? 244 ARG D CB  1 
ATOM   7641 C CG  . ARG D  1 229 ? 17.602 20.585  54.347  1.00 34.54  ? 244 ARG D CG  1 
ATOM   7642 C CD  . ARG D  1 229 ? 16.848 21.902  54.383  1.00 34.27  ? 244 ARG D CD  1 
ATOM   7643 N NE  . ARG D  1 229 ? 15.617 21.794  55.157  1.00 36.19  ? 244 ARG D NE  1 
ATOM   7644 C CZ  . ARG D  1 229 ? 14.472 21.257  54.727  1.00 36.42  ? 244 ARG D CZ  1 
ATOM   7645 N NH1 . ARG D  1 229 ? 14.360 20.768  53.501  1.00 38.25  ? 244 ARG D NH1 1 
ATOM   7646 N NH2 . ARG D  1 229 ? 13.424 21.219  55.534  1.00 37.45  ? 244 ARG D NH2 1 
ATOM   7647 N N   . VAL D  1 230 ? 20.263 17.785  53.981  1.00 31.62  ? 245 VAL D N   1 
ATOM   7648 C CA  . VAL D  1 230 ? 21.438 17.472  53.109  1.00 32.59  ? 245 VAL D CA  1 
ATOM   7649 C C   . VAL D  1 230 ? 21.636 18.584  52.063  1.00 32.99  ? 245 VAL D C   1 
ATOM   7650 O O   . VAL D  1 230 ? 22.820 18.936  51.794  1.00 32.78  ? 245 VAL D O   1 
ATOM   7651 C CB  . VAL D  1 230 ? 21.315 16.084  52.449  1.00 32.52  ? 245 VAL D CB  1 
ATOM   7652 C CG1 . VAL D  1 230 ? 22.405 15.840  51.413  1.00 33.40  ? 245 VAL D CG1 1 
ATOM   7653 C CG2 . VAL D  1 230 ? 21.334 14.971  53.491  1.00 33.99  ? 245 VAL D CG2 1 
ATOM   7654 N N   . THR D  1 231 ? 20.557 19.130  51.488  1.00 33.16  ? 246 THR D N   1 
ATOM   7655 C CA  . THR D  1 231 ? 20.638 20.172  50.420  1.00 34.44  ? 246 THR D CA  1 
ATOM   7656 C C   . THR D  1 231 ? 21.455 21.367  50.909  1.00 34.10  ? 246 THR D C   1 
ATOM   7657 O O   . THR D  1 231 ? 22.192 21.929  50.096  1.00 36.91  ? 246 THR D O   1 
ATOM   7658 C CB  . THR D  1 231 ? 19.268 20.628  49.912  1.00 33.93  ? 246 THR D CB  1 
ATOM   7659 O OG1 . THR D  1 231 ? 18.474 21.048  51.025  1.00 35.86  ? 246 THR D OG1 1 
ATOM   7660 C CG2 . THR D  1 231 ? 18.584 19.542  49.110  1.00 34.18  ? 246 THR D CG2 1 
ATOM   7661 N N   . TYR D  1 232 ? 21.370 21.687  52.201  1.00 36.98  ? 247 TYR D N   1 
ATOM   7662 C CA  . TYR D  1 232 ? 22.069 22.835  52.830  1.00 35.97  ? 247 TYR D CA  1 
ATOM   7663 C C   . TYR D  1 232 ? 23.593 22.676  52.744  1.00 36.13  ? 247 TYR D C   1 
ATOM   7664 O O   . TYR D  1 232 ? 24.286 23.705  52.677  1.00 37.88  ? 247 TYR D O   1 
ATOM   7665 C CB  . TYR D  1 232 ? 21.604 22.990  54.276  1.00 37.65  ? 247 TYR D CB  1 
ATOM   7666 C CG  . TYR D  1 232 ? 21.913 24.338  54.868  1.00 38.40  ? 247 TYR D CG  1 
ATOM   7667 C CD1 . TYR D  1 232 ? 23.162 24.605  55.405  1.00 39.11  ? 247 TYR D CD1 1 
ATOM   7668 C CD2 . TYR D  1 232 ? 20.964 25.352  54.887  1.00 37.23  ? 247 TYR D CD2 1 
ATOM   7669 C CE1 . TYR D  1 232 ? 23.466 25.841  55.952  1.00 40.01  ? 247 TYR D CE1 1 
ATOM   7670 C CE2 . TYR D  1 232 ? 21.248 26.591  55.437  1.00 37.62  ? 247 TYR D CE2 1 
ATOM   7671 C CZ  . TYR D  1 232 ? 22.504 26.838  55.969  1.00 40.20  ? 247 TYR D CZ  1 
ATOM   7672 O OH  . TYR D  1 232 ? 22.801 28.047  56.525  1.00 40.57  ? 247 TYR D OH  1 
ATOM   7673 N N   . TYR D  1 233 ? 24.109 21.439  52.749  1.00 35.19  ? 248 TYR D N   1 
ATOM   7674 C CA  . TYR D  1 233 ? 25.556 21.122  52.889  1.00 35.42  ? 248 TYR D CA  1 
ATOM   7675 C C   . TYR D  1 233 ? 26.147 20.469  51.624  1.00 36.37  ? 248 TYR D C   1 
ATOM   7676 O O   . TYR D  1 233 ? 27.301 19.993  51.704  1.00 36.18  ? 248 TYR D O   1 
ATOM   7677 C CB  . TYR D  1 233 ? 25.749 20.281  54.155  1.00 35.25  ? 248 TYR D CB  1 
ATOM   7678 C CG  . TYR D  1 233 ? 25.433 21.062  55.409  1.00 32.68  ? 248 TYR D CG  1 
ATOM   7679 C CD1 . TYR D  1 233 ? 26.265 22.091  55.807  1.00 30.97  ? 248 TYR D CD1 1 
ATOM   7680 C CD2 . TYR D  1 233 ? 24.267 20.855  56.134  1.00 30.70  ? 248 TYR D CD2 1 
ATOM   7681 C CE1 . TYR D  1 233 ? 25.987 22.867  56.917  1.00 30.78  ? 248 TYR D CE1 1 
ATOM   7682 C CE2 . TYR D  1 233 ? 23.975 21.618  57.257  1.00 32.36  ? 248 TYR D CE2 1 
ATOM   7683 C CZ  . TYR D  1 233 ? 24.835 22.635  57.639  1.00 30.81  ? 248 TYR D CZ  1 
ATOM   7684 O OH  . TYR D  1 233 ? 24.600 23.426  58.717  1.00 31.00  ? 248 TYR D OH  1 
ATOM   7685 N N   . LEU D  1 234 ? 25.440 20.494  50.486  1.00 37.30  ? 249 LEU D N   1 
ATOM   7686 C CA  . LEU D  1 234 ? 25.901 19.875  49.207  1.00 39.45  ? 249 LEU D CA  1 
ATOM   7687 C C   . LEU D  1 234 ? 27.263 20.441  48.783  1.00 38.88  ? 249 LEU D C   1 
ATOM   7688 O O   . LEU D  1 234 ? 28.127 19.630  48.412  1.00 36.46  ? 249 LEU D O   1 
ATOM   7689 C CB  . LEU D  1 234 ? 24.864 20.087  48.096  1.00 40.05  ? 249 LEU D CB  1 
ATOM   7690 C CG  . LEU D  1 234 ? 23.615 19.207  48.176  1.00 38.99  ? 249 LEU D CG  1 
ATOM   7691 C CD1 . LEU D  1 234 ? 22.516 19.730  47.263  1.00 38.25  ? 249 LEU D CD1 1 
ATOM   7692 C CD2 . LEU D  1 234 ? 23.940 17.756  47.850  1.00 38.92  ? 249 LEU D CD2 1 
ATOM   7693 N N   . ASP D  1 235 ? 27.450 21.765  48.831  1.00 41.26  ? 250 ASP D N   1 
ATOM   7694 C CA  . ASP D  1 235 ? 28.722 22.430  48.420  1.00 41.56  ? 250 ASP D CA  1 
ATOM   7695 C C   . ASP D  1 235 ? 29.885 21.922  49.278  1.00 39.08  ? 250 ASP D C   1 
ATOM   7696 O O   . ASP D  1 235 ? 30.974 21.667  48.708  1.00 40.36  ? 250 ASP D O   1 
ATOM   7697 C CB  . ASP D  1 235 ? 28.659 23.958  48.510  1.00 45.59  ? 250 ASP D CB  1 
ATOM   7698 C CG  . ASP D  1 235 ? 27.679 24.611  47.553  1.00 48.28  ? 250 ASP D CG  1 
ATOM   7699 O OD1 . ASP D  1 235 ? 27.246 23.935  46.602  1.00 50.22  ? 250 ASP D OD1 1 
ATOM   7700 O OD2 . ASP D  1 235 ? 27.353 25.795  47.773  1.00 54.72  ? 250 ASP D OD2 1 
ATOM   7701 N N   . TRP D  1 236 ? 29.671 21.775  50.588  1.00 36.94  ? 251 TRP D N   1 
ATOM   7702 C CA  . TRP D  1 236 ? 30.684 21.239  51.534  1.00 35.95  ? 251 TRP D CA  1 
ATOM   7703 C C   . TRP D  1 236 ? 30.980 19.769  51.198  1.00 33.71  ? 251 TRP D C   1 
ATOM   7704 O O   . TRP D  1 236 ? 32.160 19.399  51.170  1.00 32.78  ? 251 TRP D O   1 
ATOM   7705 C CB  . TRP D  1 236 ? 30.234 21.423  52.990  1.00 36.53  ? 251 TRP D CB  1 
ATOM   7706 C CG  . TRP D  1 236 ? 31.175 20.831  53.990  1.00 35.45  ? 251 TRP D CG  1 
ATOM   7707 C CD1 . TRP D  1 236 ? 32.317 21.395  54.476  1.00 35.16  ? 251 TRP D CD1 1 
ATOM   7708 C CD2 . TRP D  1 236 ? 31.077 19.530  54.597  1.00 35.90  ? 251 TRP D CD2 1 
ATOM   7709 N NE1 . TRP D  1 236 ? 32.932 20.538  55.349  1.00 34.42  ? 251 TRP D NE1 1 
ATOM   7710 C CE2 . TRP D  1 236 ? 32.194 19.391  55.448  1.00 34.92  ? 251 TRP D CE2 1 
ATOM   7711 C CE3 . TRP D  1 236 ? 30.154 18.478  54.517  1.00 36.43  ? 251 TRP D CE3 1 
ATOM   7712 C CZ2 . TRP D  1 236 ? 32.406 18.247  56.218  1.00 36.08  ? 251 TRP D CZ2 1 
ATOM   7713 C CZ3 . TRP D  1 236 ? 30.362 17.348  55.284  1.00 36.31  ? 251 TRP D CZ3 1 
ATOM   7714 C CH2 . TRP D  1 236 ? 31.475 17.235  56.119  1.00 35.71  ? 251 TRP D CH2 1 
ATOM   7715 N N   . ILE D  1 237 ? 29.952 18.956  50.957  1.00 34.08  ? 252 ILE D N   1 
ATOM   7716 C CA  . ILE D  1 237 ? 30.110 17.518  50.567  1.00 35.36  ? 252 ILE D CA  1 
ATOM   7717 C C   . ILE D  1 237 ? 30.947 17.447  49.278  1.00 36.99  ? 252 ILE D C   1 
ATOM   7718 O O   . ILE D  1 237 ? 31.927 16.680  49.256  1.00 35.82  ? 252 ILE D O   1 
ATOM   7719 C CB  . ILE D  1 237 ? 28.742 16.813  50.431  1.00 35.10  ? 252 ILE D CB  1 
ATOM   7720 C CG1 . ILE D  1 237 ? 28.043 16.682  51.788  1.00 34.94  ? 252 ILE D CG1 1 
ATOM   7721 C CG2 . ILE D  1 237 ? 28.887 15.457  49.744  1.00 36.62  ? 252 ILE D CG2 1 
ATOM   7722 C CD1 . ILE D  1 237 ? 26.587 16.245  51.722  1.00 34.12  ? 252 ILE D CD1 1 
ATOM   7723 N N   . HIS D  1 238 ? 30.592 18.248  48.266  1.00 37.53  ? 253 HIS D N   1 
ATOM   7724 C CA  . HIS D  1 238 ? 31.235 18.263  46.923  1.00 39.65  ? 253 HIS D CA  1 
ATOM   7725 C C   . HIS D  1 238 ? 32.660 18.822  46.987  1.00 38.11  ? 253 HIS D C   1 
ATOM   7726 O O   . HIS D  1 238 ? 33.395 18.605  46.020  1.00 41.15  ? 253 HIS D O   1 
ATOM   7727 C CB  . HIS D  1 238 ? 30.368 19.020  45.910  1.00 40.43  ? 253 HIS D CB  1 
ATOM   7728 C CG  . HIS D  1 238 ? 29.089 18.327  45.587  1.00 43.28  ? 253 HIS D CG  1 
ATOM   7729 N ND1 . HIS D  1 238 ? 27.952 19.020  45.212  1.00 45.83  ? 253 HIS D ND1 1 
ATOM   7730 C CD2 . HIS D  1 238 ? 28.748 17.020  45.612  1.00 45.08  ? 253 HIS D CD2 1 
ATOM   7731 C CE1 . HIS D  1 238 ? 26.973 18.164  45.001  1.00 47.20  ? 253 HIS D CE1 1 
ATOM   7732 N NE2 . HIS D  1 238 ? 27.436 16.931  45.242  1.00 45.37  ? 253 HIS D NE2 1 
ATOM   7733 N N   . HIS D  1 239 ? 33.046 19.499  48.070  1.00 38.45  ? 254 HIS D N   1 
ATOM   7734 C CA  . HIS D  1 239 ? 34.455 19.894  48.329  1.00 38.62  ? 254 HIS D CA  1 
ATOM   7735 C C   . HIS D  1 239 ? 35.338 18.646  48.482  1.00 40.63  ? 254 HIS D C   1 
ATOM   7736 O O   . HIS D  1 239 ? 36.514 18.729  48.088  1.00 40.84  ? 254 HIS D O   1 
ATOM   7737 C CB  . HIS D  1 239 ? 34.563 20.825  49.539  1.00 40.43  ? 254 HIS D CB  1 
ATOM   7738 C CG  . HIS D  1 239 ? 35.939 21.337  49.784  1.00 43.26  ? 254 HIS D CG  1 
ATOM   7739 N ND1 . HIS D  1 239 ? 36.372 22.550  49.292  1.00 45.35  ? 254 HIS D ND1 1 
ATOM   7740 C CD2 . HIS D  1 239 ? 36.983 20.795  50.447  1.00 45.05  ? 254 HIS D CD2 1 
ATOM   7741 C CE1 . HIS D  1 239 ? 37.624 22.744  49.660  1.00 46.75  ? 254 HIS D CE1 1 
ATOM   7742 N NE2 . HIS D  1 239 ? 38.025 21.674  50.366  1.00 46.70  ? 254 HIS D NE2 1 
ATOM   7743 N N   . TYR D  1 240 ? 34.809 17.556  49.049  1.00 41.48  ? 255 TYR D N   1 
ATOM   7744 C CA  . TYR D  1 240 ? 35.595 16.354  49.440  1.00 40.02  ? 255 TYR D CA  1 
ATOM   7745 C C   . TYR D  1 240 ? 35.253 15.157  48.556  1.00 38.40  ? 255 TYR D C   1 
ATOM   7746 O O   . TYR D  1 240 ? 36.177 14.442  48.177  1.00 38.53  ? 255 TYR D O   1 
ATOM   7747 C CB  . TYR D  1 240 ? 35.358 16.041  50.916  1.00 39.97  ? 255 TYR D CB  1 
ATOM   7748 C CG  . TYR D  1 240 ? 35.869 17.121  51.831  1.00 40.44  ? 255 TYR D CG  1 
ATOM   7749 C CD1 . TYR D  1 240 ? 37.228 17.254  52.076  1.00 39.66  ? 255 TYR D CD1 1 
ATOM   7750 C CD2 . TYR D  1 240 ? 35.007 18.032  52.424  1.00 38.14  ? 255 TYR D CD2 1 
ATOM   7751 C CE1 . TYR D  1 240 ? 37.718 18.247  52.909  1.00 39.09  ? 255 TYR D CE1 1 
ATOM   7752 C CE2 . TYR D  1 240 ? 35.481 19.030  53.257  1.00 37.89  ? 255 TYR D CE2 1 
ATOM   7753 C CZ  . TYR D  1 240 ? 36.839 19.138  53.501  1.00 38.76  ? 255 TYR D CZ  1 
ATOM   7754 O OH  . TYR D  1 240 ? 37.304 20.120  54.323  1.00 40.55  ? 255 TYR D OH  1 
ATOM   7755 N N   . VAL D  1 241 ? 33.970 14.935  48.261  1.00 39.89  ? 256 VAL D N   1 
ATOM   7756 C CA  . VAL D  1 241 ? 33.473 13.688  47.613  1.00 41.07  ? 256 VAL D CA  1 
ATOM   7757 C C   . VAL D  1 241 ? 33.413 13.938  46.109  1.00 42.72  ? 256 VAL D C   1 
ATOM   7758 O O   . VAL D  1 241 ? 32.649 14.794  45.674  1.00 42.49  ? 256 VAL D O   1 
ATOM   7759 C CB  . VAL D  1 241 ? 32.108 13.259  48.188  1.00 40.66  ? 256 VAL D CB  1 
ATOM   7760 C CG1 . VAL D  1 241 ? 31.624 11.955  47.571  1.00 40.11  ? 256 VAL D CG1 1 
ATOM   7761 C CG2 . VAL D  1 241 ? 32.146 13.144  49.703  1.00 40.69  ? 256 VAL D CG2 1 
ATOM   7762 N N   . PRO D  1 242 ? 34.212 13.224  45.277  1.00 47.26  ? 257 PRO D N   1 
ATOM   7763 C CA  . PRO D  1 242 ? 34.169 13.415  43.828  1.00 51.21  ? 257 PRO D CA  1 
ATOM   7764 C C   . PRO D  1 242 ? 32.788 13.071  43.255  1.00 52.84  ? 257 PRO D C   1 
ATOM   7765 O O   . PRO D  1 242 ? 32.168 12.134  43.728  1.00 54.17  ? 257 PRO D O   1 
ATOM   7766 C CB  . PRO D  1 242 ? 35.235 12.477  43.241  1.00 50.08  ? 257 PRO D CB  1 
ATOM   7767 C CG  . PRO D  1 242 ? 35.683 11.583  44.385  1.00 50.09  ? 257 PRO D CG  1 
ATOM   7768 C CD  . PRO D  1 242 ? 35.191 12.204  45.678  1.00 48.88  ? 257 PRO D CD  1 
ATOM   7769 N N   . LYS D  1 243 ? 32.329 13.857  42.279  1.00 57.91  ? 258 LYS D N   1 
ATOM   7770 C CA  . LYS D  1 243 ? 31.085 13.587  41.508  1.00 65.22  ? 258 LYS D CA  1 
ATOM   7771 C C   . LYS D  1 243 ? 31.299 12.312  40.679  1.00 66.44  ? 258 LYS D C   1 
ATOM   7772 O O   . LYS D  1 243 ? 32.473 11.985  40.377  1.00 67.22  ? 258 LYS D O   1 
ATOM   7773 C CB  . LYS D  1 243 ? 30.708 14.807  40.658  1.00 69.09  ? 258 LYS D CB  1 
ATOM   7774 C CG  . LYS D  1 243 ? 30.308 16.039  41.465  1.00 72.52  ? 258 LYS D CG  1 
ATOM   7775 C CD  . LYS D  1 243 ? 29.765 17.183  40.635  1.00 73.80  ? 258 LYS D CD  1 
ATOM   7776 C CE  . LYS D  1 243 ? 29.356 18.379  41.449  0.00 75.02  ? 258 LYS D CE  1 
ATOM   7777 N NZ  . LYS D  1 243 ? 28.783 19.451  40.602  0.00 75.08  ? 258 LYS D NZ  1 
ATOM   7778 N N   . LYS D  1 244 ? 30.212 11.599  40.364  1.00 70.66  ? 259 LYS D N   1 
ATOM   7779 C CA  . LYS D  1 244 ? 30.235 10.322  39.595  1.00 71.61  ? 259 LYS D CA  1 
ATOM   7780 C C   . LYS D  1 244 ? 30.980 10.572  38.280  1.00 71.76  ? 259 LYS D C   1 
ATOM   7781 O O   . LYS D  1 244 ? 30.818 11.642  37.694  1.00 71.56  ? 259 LYS D O   1 
ATOM   7782 C CB  . LYS D  1 244 ? 28.810 9.813   39.350  1.00 71.14  ? 259 LYS D CB  1 
ATOM   7783 C CG  . LYS D  1 244 ? 28.026 9.429   40.599  1.00 71.45  ? 259 LYS D CG  1 
ATOM   7784 C CD  . LYS D  1 244 ? 26.540 9.273   40.386  0.00 73.17  ? 259 LYS D CD  1 
ATOM   7785 C CE  . LYS D  1 244 ? 25.738 9.347   41.669  0.00 73.14  ? 259 LYS D CE  1 
ATOM   7786 N NZ  . LYS D  1 244 ? 24.288 9.165   41.421  0.00 73.11  ? 259 LYS D NZ  1 
ATOM   7787 N N   . PRO D  1 245 ? 31.824 9.636   37.771  1.00 73.02  ? 260 PRO D N   1 
ATOM   7788 C CA  . PRO D  1 245 ? 32.620 9.905   36.569  1.00 75.55  ? 260 PRO D CA  1 
ATOM   7789 C C   . PRO D  1 245 ? 31.754 10.129  35.316  1.00 78.52  ? 260 PRO D C   1 
ATOM   7790 O O   . PRO D  1 245 ? 32.073 10.961  34.461  1.00 76.26  ? 260 PRO D O   1 
ATOM   7791 C CB  . PRO D  1 245 ? 33.503 8.657   36.397  1.00 75.22  ? 260 PRO D CB  1 
ATOM   7792 C CG  . PRO D  1 245 ? 33.436 7.946   37.736  1.00 74.68  ? 260 PRO D CG  1 
ATOM   7793 C CD  . PRO D  1 245 ? 32.072 8.285   38.302  1.00 73.25  ? 260 PRO D CD  1 
ATOM   7794 O OXT . PRO D  1 245 ? 30.715 9.487   35.138  1.00 81.32  ? 260 PRO D OXT 1 
HETATM 7795 C C   . ACT E  2 .   ? 24.167 14.148  96.258  1.00 51.09  ? 301 ACT A C   1 
HETATM 7796 O O   . ACT E  2 .   ? 22.908 13.988  96.371  1.00 45.37  ? 301 ACT A O   1 
HETATM 7797 O OXT . ACT E  2 .   ? 24.789 15.207  96.563  1.00 44.90  ? 301 ACT A OXT 1 
HETATM 7798 C CH3 . ACT E  2 .   ? 24.994 12.979  95.711  1.00 47.87  ? 301 ACT A CH3 1 
HETATM 7799 C C1  . EDO F  3 .   ? 38.400 30.735  102.336 1.00 59.95  ? 302 EDO A C1  1 
HETATM 7800 O O1  . EDO F  3 .   ? 37.281 29.931  102.648 1.00 62.35  ? 302 EDO A O1  1 
HETATM 7801 C C2  . EDO F  3 .   ? 38.098 31.743  101.291 1.00 59.90  ? 302 EDO A C2  1 
HETATM 7802 O O2  . EDO F  3 .   ? 37.514 32.942  101.767 1.00 59.86  ? 302 EDO A O2  1 
HETATM 7803 S S   . SO4 G  4 .   ? 35.883 35.700  103.938 1.00 69.99  ? 303 SO4 A S   1 
HETATM 7804 O O1  . SO4 G  4 .   ? 36.707 36.289  102.921 1.00 72.65  ? 303 SO4 A O1  1 
HETATM 7805 O O2  . SO4 G  4 .   ? 36.608 35.670  105.178 1.00 73.69  ? 303 SO4 A O2  1 
HETATM 7806 O O3  . SO4 G  4 .   ? 34.687 36.485  104.105 1.00 65.76  ? 303 SO4 A O3  1 
HETATM 7807 O O4  . SO4 G  4 .   ? 35.539 34.355  103.552 1.00 68.81  ? 303 SO4 A O4  1 
HETATM 7808 C C1  . EDO H  3 .   ? 14.948 17.871  87.842  1.00 55.08  ? 304 EDO A C1  1 
HETATM 7809 O O1  . EDO H  3 .   ? 15.255 16.677  87.151  1.00 57.48  ? 304 EDO A O1  1 
HETATM 7810 C C2  . EDO H  3 .   ? 13.564 18.343  87.595  1.00 55.88  ? 304 EDO A C2  1 
HETATM 7811 O O2  . EDO H  3 .   ? 13.323 19.685  87.991  1.00 57.57  ? 304 EDO A O2  1 
HETATM 7812 C C1  . GOL I  5 .   ? 22.948 21.793  109.363 1.00 59.33  ? 305 GOL A C1  1 
HETATM 7813 O O1  . GOL I  5 .   ? 23.530 22.698  108.428 1.00 56.33  ? 305 GOL A O1  1 
HETATM 7814 C C2  . GOL I  5 .   ? 23.334 20.356  109.076 1.00 60.93  ? 305 GOL A C2  1 
HETATM 7815 O O2  . GOL I  5 .   ? 22.873 19.981  107.779 1.00 63.28  ? 305 GOL A O2  1 
HETATM 7816 C C3  . GOL I  5 .   ? 24.827 20.107  109.164 1.00 59.80  ? 305 GOL A C3  1 
HETATM 7817 O O3  . GOL I  5 .   ? 25.214 19.343  110.304 1.00 56.51  ? 305 GOL A O3  1 
HETATM 7818 O O1  . MES J  6 .   ? 29.518 21.131  84.335  1.00 85.70  ? 306 MES A O1  1 
HETATM 7819 C C2  . MES J  6 .   ? 29.226 19.890  84.956  1.00 91.76  ? 306 MES A C2  1 
HETATM 7820 C C3  . MES J  6 .   ? 28.054 19.194  84.302  1.00 92.07  ? 306 MES A C3  1 
HETATM 7821 N N4  . MES J  6 .   ? 26.836 20.064  84.349  1.00 89.42  ? 306 MES A N4  1 
HETATM 7822 C C5  . MES J  6 .   ? 27.178 21.415  83.806  1.00 88.21  ? 306 MES A C5  1 
HETATM 7823 C C6  . MES J  6 .   ? 28.401 21.995  84.473  1.00 86.45  ? 306 MES A C6  1 
HETATM 7824 C C7  . MES J  6 .   ? 25.683 19.473  83.583  1.00 87.33  ? 306 MES A C7  1 
HETATM 7825 C C8  . MES J  6 .   ? 25.001 18.308  84.273  1.00 86.46  ? 306 MES A C8  1 
HETATM 7826 S S   . MES J  6 .   ? 23.952 18.831  85.611  1.00 88.93  ? 306 MES A S   1 
HETATM 7827 O O1S . MES J  6 .   ? 23.405 17.631  86.183  1.00 90.07  ? 306 MES A O1S 1 
HETATM 7828 O O2S . MES J  6 .   ? 22.942 19.671  85.035  1.00 83.06  ? 306 MES A O2S 1 
HETATM 7829 O O3S . MES J  6 .   ? 24.803 19.538  86.526  1.00 89.15  ? 306 MES A O3S 1 
HETATM 7830 C C1  . EDO K  3 .   ? 25.858 42.974  78.482  1.00 61.26  ? 307 EDO A C1  1 
HETATM 7831 O O1  . EDO K  3 .   ? 26.943 43.715  77.972  1.00 63.98  ? 307 EDO A O1  1 
HETATM 7832 C C2  . EDO K  3 .   ? 24.535 43.376  77.928  1.00 60.09  ? 307 EDO A C2  1 
HETATM 7833 O O2  . EDO K  3 .   ? 23.588 42.318  77.828  1.00 56.01  ? 307 EDO A O2  1 
HETATM 7834 C C1  . EDO L  3 .   ? 30.501 13.918  84.168  1.00 62.44  ? 308 EDO A C1  1 
HETATM 7835 O O1  . EDO L  3 .   ? 31.770 14.480  83.939  1.00 59.05  ? 308 EDO A O1  1 
HETATM 7836 C C2  . EDO L  3 .   ? 29.628 14.792  84.995  1.00 63.32  ? 308 EDO A C2  1 
HETATM 7837 O O2  . EDO L  3 .   ? 29.435 16.105  84.468  1.00 64.02  ? 308 EDO A O2  1 
HETATM 7838 C C1  . EDO M  3 .   ? 46.358 24.163  92.106  1.00 67.47  ? 309 EDO A C1  1 
HETATM 7839 O O1  . EDO M  3 .   ? 47.454 23.280  92.010  1.00 69.36  ? 309 EDO A O1  1 
HETATM 7840 C C2  . EDO M  3 .   ? 46.138 24.972  90.880  1.00 69.56  ? 309 EDO A C2  1 
HETATM 7841 O O2  . EDO M  3 .   ? 45.858 26.343  91.108  1.00 71.25  ? 309 EDO A O2  1 
HETATM 7842 S S   . SO4 N  4 .   ? 38.993 17.843  103.088 1.00 104.03 ? 310 SO4 A S   1 
HETATM 7843 O O1  . SO4 N  4 .   ? 40.204 18.080  102.343 1.00 101.52 ? 310 SO4 A O1  1 
HETATM 7844 O O2  . SO4 N  4 .   ? 38.275 19.076  103.262 1.00 96.22  ? 310 SO4 A O2  1 
HETATM 7845 O O3  . SO4 N  4 .   ? 38.158 16.913  102.374 1.00 102.46 ? 310 SO4 A O3  1 
HETATM 7846 O O4  . SO4 N  4 .   ? 39.335 17.299  104.375 1.00 106.02 ? 310 SO4 A O4  1 
HETATM 7847 C C   . ACT O  2 .   ? 22.709 2.887   102.856 1.00 64.85  ? 301 ACT B C   1 
HETATM 7848 O O   . ACT O  2 .   ? 22.105 2.660   103.937 1.00 61.59  ? 301 ACT B O   1 
HETATM 7849 O OXT . ACT O  2 .   ? 23.959 2.996   102.751 1.00 58.11  ? 301 ACT B OXT 1 
HETATM 7850 C CH3 . ACT O  2 .   ? 21.863 3.041   101.585 1.00 61.34  ? 301 ACT B CH3 1 
HETATM 7851 C C1  . EDO P  3 .   ? 16.637 -0.183  125.593 1.00 54.94  ? 302 EDO B C1  1 
HETATM 7852 O O1  . EDO P  3 .   ? 17.286 0.935   126.168 1.00 56.43  ? 302 EDO B O1  1 
HETATM 7853 C C2  . EDO P  3 .   ? 16.053 0.197   124.285 1.00 54.95  ? 302 EDO B C2  1 
HETATM 7854 O O2  . EDO P  3 .   ? 15.867 -0.845  123.345 1.00 49.44  ? 302 EDO B O2  1 
HETATM 7855 O OH2 . 1PE Q  7 .   ? 31.596 -6.361  100.853 1.00 57.79  ? 303 1PE B OH2 1 
HETATM 7856 C C12 . 1PE Q  7 .   ? 32.254 -7.177  101.800 1.00 58.90  ? 303 1PE B C12 1 
HETATM 7857 C C22 . 1PE Q  7 .   ? 32.909 -6.369  102.868 1.00 56.99  ? 303 1PE B C22 1 
HETATM 7858 O OH3 . 1PE Q  7 .   ? 33.667 -7.209  103.731 1.00 59.73  ? 303 1PE B OH3 1 
HETATM 7859 C C13 . 1PE Q  7 .   ? 35.885 -6.874  104.612 1.00 66.38  ? 303 1PE B C13 1 
HETATM 7860 C C23 . 1PE Q  7 .   ? 34.435 -6.482  104.690 1.00 65.22  ? 303 1PE B C23 1 
HETATM 7861 O OH4 . 1PE Q  7 .   ? 36.352 -6.803  103.266 1.00 66.35  ? 303 1PE B OH4 1 
HETATM 7862 C C14 . 1PE Q  7 .   ? 38.254 -6.643  101.777 1.00 69.39  ? 303 1PE B C14 1 
HETATM 7863 C C24 . 1PE Q  7 .   ? 37.738 -6.490  103.182 1.00 69.31  ? 303 1PE B C24 1 
HETATM 7864 O OH5 . 1PE Q  7 .   ? 38.893 -7.908  101.621 1.00 71.86  ? 303 1PE B OH5 1 
HETATM 7865 C C15 . 1PE Q  7 .   ? 40.131 -9.335  100.135 1.00 73.25  ? 303 1PE B C15 1 
HETATM 7866 C C25 . 1PE Q  7 .   ? 39.867 -7.924  100.579 1.00 72.78  ? 303 1PE B C25 1 
HETATM 7867 O OH6 . 1PE Q  7 .   ? 40.863 -10.043 101.133 1.00 73.50  ? 303 1PE B OH6 1 
HETATM 7868 C C16 . 1PE Q  7 .   ? 42.949 -10.680 102.137 1.00 73.33  ? 303 1PE B C16 1 
HETATM 7869 C C26 . 1PE Q  7 .   ? 42.278 -9.927  101.013 1.00 74.17  ? 303 1PE B C26 1 
HETATM 7870 O OH7 . 1PE Q  7 .   ? 43.985 -9.941  102.779 1.00 72.55  ? 303 1PE B OH7 1 
HETATM 7871 S S   . SO4 R  4 .   ? 0.330  -6.443  110.306 1.00 83.10  ? 304 SO4 B S   1 
HETATM 7872 O O1  . SO4 R  4 .   ? 1.427  -6.687  109.413 1.00 83.19  ? 304 SO4 B O1  1 
HETATM 7873 O O2  . SO4 R  4 .   ? 0.745  -6.705  111.657 1.00 82.05  ? 304 SO4 B O2  1 
HETATM 7874 O O3  . SO4 R  4 .   ? -0.092 -5.070  110.189 1.00 79.17  ? 304 SO4 B O3  1 
HETATM 7875 O O4  . SO4 R  4 .   ? -0.761 -7.316  109.966 1.00 85.14  ? 304 SO4 B O4  1 
HETATM 7876 S S   . SO4 S  4 .   ? 11.381 -0.371  125.900 1.00 66.26  ? 305 SO4 B S   1 
HETATM 7877 O O1  . SO4 S  4 .   ? 12.380 -1.066  126.658 1.00 61.82  ? 305 SO4 B O1  1 
HETATM 7878 O O2  . SO4 S  4 .   ? 11.243 0.958   126.433 1.00 66.07  ? 305 SO4 B O2  1 
HETATM 7879 O O3  . SO4 S  4 .   ? 11.772 -0.293  124.520 1.00 66.00  ? 305 SO4 B O3  1 
HETATM 7880 O O4  . SO4 S  4 .   ? 10.121 -1.066  125.992 1.00 63.76  ? 305 SO4 B O4  1 
HETATM 7881 C C1  . EDO T  3 .   ? 6.064  -1.278  113.413 1.00 68.27  ? 306 EDO B C1  1 
HETATM 7882 O O1  . EDO T  3 .   ? 6.443  -2.561  113.839 1.00 60.55  ? 306 EDO B O1  1 
HETATM 7883 C C2  . EDO T  3 .   ? 6.140  -0.301  114.516 1.00 70.52  ? 306 EDO B C2  1 
HETATM 7884 O O2  . EDO T  3 .   ? 7.403  0.320   114.652 1.00 74.22  ? 306 EDO B O2  1 
HETATM 7885 O O1  . MES U  6 .   ? 16.951 -10.781 104.100 1.00 77.55  ? 307 MES B O1  1 
HETATM 7886 C C2  . MES U  6 .   ? 17.389 -10.121 102.922 1.00 82.15  ? 307 MES B C2  1 
HETATM 7887 C C3  . MES U  6 .   ? 18.625 -10.766 102.344 1.00 82.55  ? 307 MES B C3  1 
HETATM 7888 N N4  . MES U  6 .   ? 19.734 -10.812 103.347 1.00 82.10  ? 307 MES B N4  1 
HETATM 7889 C C5  . MES U  6 .   ? 19.219 -11.417 104.618 1.00 80.82  ? 307 MES B C5  1 
HETATM 7890 C C6  . MES U  6 .   ? 17.966 -10.723 105.088 1.00 78.68  ? 307 MES B C6  1 
HETATM 7891 C C7  . MES U  6 .   ? 20.924 -11.561 102.806 1.00 82.56  ? 307 MES B C7  1 
HETATM 7892 C C8  . MES U  6 .   ? 21.682 -10.833 101.707 1.00 82.91  ? 307 MES B C8  1 
HETATM 7893 S S   . MES U  6 .   ? 22.395 -9.282  102.233 1.00 85.56  ? 307 MES B S   1 
HETATM 7894 O O1S . MES U  6 .   ? 23.708 -9.587  102.732 1.00 79.61  ? 307 MES B O1S 1 
HETATM 7895 O O2S . MES U  6 .   ? 21.530 -8.755  103.251 1.00 88.33  ? 307 MES B O2S 1 
HETATM 7896 O O3S . MES U  6 .   ? 22.431 -8.446  101.066 1.00 88.62  ? 307 MES B O3S 1 
HETATM 7897 C C1  . EDO V  3 .   ? 8.804  -0.562  121.131 1.00 69.30  ? 308 EDO B C1  1 
HETATM 7898 O O1  . EDO V  3 .   ? 9.909  -0.827  121.973 1.00 70.15  ? 308 EDO B O1  1 
HETATM 7899 C C2  . EDO V  3 .   ? 8.845  0.773   120.486 1.00 67.42  ? 308 EDO B C2  1 
HETATM 7900 O O2  . EDO V  3 .   ? 10.086 1.085   119.880 1.00 65.15  ? 308 EDO B O2  1 
HETATM 7901 C C1  . GOL W  5 .   ? 23.024 10.754  116.149 1.00 59.43  ? 309 GOL B C1  1 
HETATM 7902 O O1  . GOL W  5 .   ? 23.807 9.580   116.330 1.00 54.83  ? 309 GOL B O1  1 
HETATM 7903 C C2  . GOL W  5 .   ? 23.350 11.449  114.844 1.00 60.38  ? 309 GOL B C2  1 
HETATM 7904 O O2  . GOL W  5 .   ? 23.105 10.571  113.742 1.00 59.71  ? 309 GOL B O2  1 
HETATM 7905 C C3  . GOL W  5 .   ? 22.573 12.737  114.665 1.00 57.96  ? 309 GOL B C3  1 
HETATM 7906 O O3  . GOL W  5 .   ? 21.265 12.505  114.153 1.00 55.79  ? 309 GOL B O3  1 
HETATM 7907 O O1  . MES X  6 .   ? 29.911 -21.236 87.249  1.00 84.73  ? 301 MES C O1  1 
HETATM 7908 C C2  . MES X  6 .   ? 28.922 -22.148 86.801  1.00 84.36  ? 301 MES C C2  1 
HETATM 7909 C C3  . MES X  6 .   ? 27.620 -21.947 87.536  1.00 85.60  ? 301 MES C C3  1 
HETATM 7910 N N4  . MES X  6 .   ? 27.118 -20.537 87.439  1.00 87.75  ? 301 MES C N4  1 
HETATM 7911 C C5  . MES X  6 .   ? 28.225 -19.582 87.762  1.00 90.22  ? 301 MES C C5  1 
HETATM 7912 C C6  . MES X  6 .   ? 29.470 -19.916 86.981  1.00 89.70  ? 301 MES C C6  1 
HETATM 7913 C C7  . MES X  6 .   ? 25.941 -20.324 88.354  1.00 86.91  ? 301 MES C C7  1 
HETATM 7914 C C8  . MES X  6 .   ? 25.195 -19.014 88.166  1.00 87.23  ? 301 MES C C8  1 
HETATM 7915 S S   . MES X  6 .   ? 24.197 -18.969 86.690  1.00 89.02  ? 301 MES C S   1 
HETATM 7916 O O1S . MES X  6 .   ? 24.996 -19.532 85.639  1.00 89.65  ? 301 MES C O1S 1 
HETATM 7917 O O2S . MES X  6 .   ? 23.891 -17.584 86.471  1.00 92.12  ? 301 MES C O2S 1 
HETATM 7918 O O3S . MES X  6 .   ? 23.023 -19.746 86.959  1.00 86.20  ? 301 MES C O3S 1 
HETATM 7919 C C   . ACT Y  2 .   ? 24.128 -14.016 75.722  1.00 56.01  ? 302 ACT C C   1 
HETATM 7920 O O   . ACT Y  2 .   ? 22.878 -13.845 75.569  1.00 47.54  ? 302 ACT C O   1 
HETATM 7921 O OXT . ACT Y  2 .   ? 24.751 -15.077 75.412  1.00 51.34  ? 302 ACT C OXT 1 
HETATM 7922 C CH3 . ACT Y  2 .   ? 24.945 -12.856 76.322  1.00 51.44  ? 302 ACT C CH3 1 
HETATM 7923 S S   . SO4 Z  4 .   ? 35.959 -35.649 67.896  1.00 68.42  ? 303 SO4 C S   1 
HETATM 7924 O O1  . SO4 Z  4 .   ? 36.878 -36.186 68.861  1.00 68.41  ? 303 SO4 C O1  1 
HETATM 7925 O O2  . SO4 Z  4 .   ? 35.580 -34.315 68.285  1.00 66.26  ? 303 SO4 C O2  1 
HETATM 7926 O O3  . SO4 Z  4 .   ? 36.597 -35.604 66.608  1.00 73.21  ? 303 SO4 C O3  1 
HETATM 7927 O O4  . SO4 Z  4 .   ? 34.789 -36.488 67.817  1.00 63.04  ? 303 SO4 C O4  1 
HETATM 7928 C C1  . GOL AA 5 .   ? 23.324 -21.659 62.407  1.00 61.33  ? 304 GOL C C1  1 
HETATM 7929 O O1  . GOL AA 5 .   ? 23.600 -22.533 63.500  1.00 57.38  ? 304 GOL C O1  1 
HETATM 7930 C C2  . GOL AA 5 .   ? 23.379 -20.197 62.804  1.00 63.69  ? 304 GOL C C2  1 
HETATM 7931 O O2  . GOL AA 5 .   ? 22.778 -20.010 64.085  1.00 64.27  ? 304 GOL C O2  1 
HETATM 7932 C C3  . GOL AA 5 .   ? 24.773 -19.604 62.828  1.00 63.40  ? 304 GOL C C3  1 
HETATM 7933 O O3  . GOL AA 5 .   ? 25.430 -19.674 61.565  1.00 61.80  ? 304 GOL C O3  1 
HETATM 7934 C C1  . EDO BA 3 .   ? 37.469 -32.136 70.412  1.00 59.06  ? 305 EDO C C1  1 
HETATM 7935 O O1  . EDO BA 3 .   ? 38.004 -33.437 70.288  1.00 57.99  ? 305 EDO C O1  1 
HETATM 7936 C C2  . EDO BA 3 .   ? 38.306 -31.097 69.764  1.00 57.20  ? 305 EDO C C2  1 
HETATM 7937 O O2  . EDO BA 3 .   ? 37.587 -29.934 69.386  1.00 60.70  ? 305 EDO C O2  1 
HETATM 7938 S S   . SO4 CA 4 .   ? 38.460 -17.885 69.044  1.00 98.41  ? 306 SO4 C S   1 
HETATM 7939 O O1  . SO4 CA 4 .   ? 39.872 -18.020 69.302  1.00 98.02  ? 306 SO4 C O1  1 
HETATM 7940 O O2  . SO4 CA 4 .   ? 37.772 -17.553 70.265  1.00 97.28  ? 306 SO4 C O2  1 
HETATM 7941 O O3  . SO4 CA 4 .   ? 38.251 -16.837 68.082  1.00 104.09 ? 306 SO4 C O3  1 
HETATM 7942 O O4  . SO4 CA 4 .   ? 37.945 -19.123 68.525  1.00 93.47  ? 306 SO4 C O4  1 
HETATM 7943 C C1  . EDO DA 3 .   ? 46.322 -23.998 79.944  1.00 67.86  ? 307 EDO C C1  1 
HETATM 7944 O O1  . EDO DA 3 .   ? 47.566 -23.337 79.923  1.00 69.53  ? 307 EDO C O1  1 
HETATM 7945 C C2  . EDO DA 3 .   ? 46.065 -24.766 81.188  1.00 69.14  ? 307 EDO C C2  1 
HETATM 7946 O O2  . EDO DA 3 .   ? 45.976 -26.176 81.032  1.00 70.16  ? 307 EDO C O2  1 
HETATM 7947 C C   . ACT EA 2 .   ? 22.759 -2.978  69.014  1.00 65.25  ? 301 ACT D C   1 
HETATM 7948 O O   . ACT EA 2 .   ? 22.201 -2.689  67.925  1.00 60.85  ? 301 ACT D O   1 
HETATM 7949 O OXT . ACT EA 2 .   ? 24.003 -3.125  69.157  1.00 57.90  ? 301 ACT D OXT 1 
HETATM 7950 C CH3 . ACT EA 2 .   ? 21.862 -3.156  70.244  1.00 61.64  ? 301 ACT D CH3 1 
HETATM 7951 C C1  . EDO FA 3 .   ? 6.602  -0.113  57.380  1.00 64.80  ? 302 EDO D C1  1 
HETATM 7952 O O1  . EDO FA 3 .   ? 7.767  -0.904  57.544  1.00 68.60  ? 302 EDO D O1  1 
HETATM 7953 C C2  . EDO FA 3 .   ? 6.543  1.037   58.323  1.00 61.19  ? 302 EDO D C2  1 
HETATM 7954 O O2  . EDO FA 3 .   ? 6.332  2.311   57.747  1.00 55.25  ? 302 EDO D O2  1 
HETATM 7955 S S   . SO4 GA 4 .   ? 0.248  6.393   61.541  1.00 82.39  ? 303 SO4 D S   1 
HETATM 7956 O O1  . SO4 GA 4 .   ? 1.299  7.221   62.065  1.00 80.37  ? 303 SO4 D O1  1 
HETATM 7957 O O2  . SO4 GA 4 .   ? -1.007 7.074   61.705  1.00 86.47  ? 303 SO4 D O2  1 
HETATM 7958 O O3  . SO4 GA 4 .   ? 0.482  6.142   60.144  1.00 80.23  ? 303 SO4 D O3  1 
HETATM 7959 O O4  . SO4 GA 4 .   ? 0.216  5.140   62.252  1.00 77.11  ? 303 SO4 D O4  1 
HETATM 7960 S S   . SO4 HA 4 .   ? 11.405 0.306   46.048  1.00 68.18  ? 304 SO4 D S   1 
HETATM 7961 O O1  . SO4 HA 4 .   ? 12.671 0.682   45.486  1.00 61.07  ? 304 SO4 D O1  1 
HETATM 7962 O O2  . SO4 HA 4 .   ? 11.533 0.076   47.461  1.00 63.52  ? 304 SO4 D O2  1 
HETATM 7963 O O3  . SO4 HA 4 .   ? 10.441 1.354   45.828  1.00 68.93  ? 304 SO4 D O3  1 
HETATM 7964 O O4  . SO4 HA 4 .   ? 10.961 -0.903  45.412  1.00 70.18  ? 304 SO4 D O4  1 
HETATM 7965 C C1  . EDO IA 3 .   ? 8.999  0.264   51.214  1.00 60.04  ? 305 EDO D C1  1 
HETATM 7966 O O1  . EDO IA 3 .   ? 9.490  -0.874  51.893  1.00 58.67  ? 305 EDO D O1  1 
HETATM 7967 C C2  . EDO IA 3 .   ? 9.699  0.509   49.930  1.00 61.07  ? 305 EDO D C2  1 
HETATM 7968 O O2  . EDO IA 3 .   ? 9.271  1.660   49.223  1.00 61.56  ? 305 EDO D O2  1 
HETATM 7969 O OH2 . 1PE JA 7 .   ? 31.688 6.159   70.881  1.00 57.78  ? 306 1PE D OH2 1 
HETATM 7970 C C12 . 1PE JA 7 .   ? 32.797 6.763   70.248  1.00 62.34  ? 306 1PE D C12 1 
HETATM 7971 C C22 . 1PE JA 7 .   ? 32.531 7.029   68.806  1.00 62.05  ? 306 1PE D C22 1 
HETATM 7972 O OH3 . 1PE JA 7 .   ? 33.747 7.304   68.120  1.00 65.77  ? 306 1PE D OH3 1 
HETATM 7973 C C13 . 1PE JA 7 .   ? 35.864 6.324   67.567  1.00 72.12  ? 306 1PE D C13 1 
HETATM 7974 C C23 . 1PE JA 7 .   ? 34.373 6.150   67.562  1.00 70.78  ? 306 1PE D C23 1 
HETATM 7975 O OH4 . 1PE JA 7 .   ? 36.268 6.935   68.789  1.00 76.56  ? 306 1PE D OH4 1 
HETATM 7976 C C14 . 1PE JA 7 .   ? 37.898 7.206   70.526  1.00 79.19  ? 306 1PE D C14 1 
HETATM 7977 C C24 . 1PE JA 7 .   ? 37.535 6.490   69.260  1.00 78.20  ? 306 1PE D C24 1 
HETATM 7978 O OH5 . 1PE JA 7 .   ? 39.160 7.853   70.368  1.00 78.57  ? 306 1PE D OH5 1 
HETATM 7979 C C15 . 1PE JA 7 .   ? 40.089 9.356   71.989  1.00 82.98  ? 306 1PE D C15 1 
HETATM 7980 C C25 . 1PE JA 7 .   ? 39.943 7.925   71.558  1.00 81.89  ? 306 1PE D C25 1 
HETATM 7981 O OH6 . 1PE JA 7 .   ? 40.776 10.105  70.990  1.00 81.96  ? 306 1PE D OH6 1 
HETATM 7982 C C16 . 1PE JA 7 .   ? 42.816 10.910  70.019  1.00 81.59  ? 306 1PE D C16 1 
HETATM 7983 C C26 . 1PE JA 7 .   ? 42.196 10.037  71.081  1.00 81.22  ? 306 1PE D C26 1 
HETATM 7984 O OH7 . 1PE JA 7 .   ? 43.862 10.273  69.293  1.00 83.32  ? 306 1PE D OH7 1 
HETATM 7985 O O1  . MES KA 6 .   ? 17.071 11.205  67.233  1.00 82.40  ? 307 MES D O1  1 
HETATM 7986 C C2  . MES KA 6 .   ? 17.061 9.955   67.898  1.00 86.29  ? 307 MES D C2  1 
HETATM 7987 C C3  . MES KA 6 .   ? 17.983 9.945   69.096  1.00 88.17  ? 307 MES D C3  1 
HETATM 7988 N N4  . MES KA 6 .   ? 19.377 10.380  68.758  1.00 87.97  ? 307 MES D N4  1 
HETATM 7989 C C5  . MES KA 6 .   ? 19.324 11.639  67.958  1.00 87.53  ? 307 MES D C5  1 
HETATM 7990 C C6  . MES KA 6 .   ? 18.388 11.478  66.789  1.00 86.32  ? 307 MES D C6  1 
HETATM 7991 C C7  . MES KA 6 .   ? 20.189 10.569  70.010  1.00 87.61  ? 307 MES D C7  1 
HETATM 7992 C C8  . MES KA 6 .   ? 21.677 10.767  69.788  1.00 86.37  ? 307 MES D C8  1 
HETATM 7993 S S   . MES KA 6 .   ? 22.557 9.227   69.667  1.00 84.26  ? 307 MES D S   1 
HETATM 7994 O O1S . MES KA 6 .   ? 22.470 8.617   70.964  1.00 90.23  ? 307 MES D O1S 1 
HETATM 7995 O O2S . MES KA 6 .   ? 23.905 9.569   69.303  1.00 81.94  ? 307 MES D O2S 1 
HETATM 7996 O O3S . MES KA 6 .   ? 21.888 8.460   68.654  1.00 87.05  ? 307 MES D O3S 1 
HETATM 7997 C C1  . EDO LA 3 .   ? 16.739 0.059   46.288  1.00 56.15  ? 308 EDO D C1  1 
HETATM 7998 O O1  . EDO LA 3 .   ? 17.234 -1.254  46.464  1.00 58.20  ? 308 EDO D O1  1 
HETATM 7999 C C2  . EDO LA 3 .   ? 15.650 0.399   47.239  1.00 57.42  ? 308 EDO D C2  1 
HETATM 8000 O O2  . EDO LA 3 .   ? 16.087 0.656   48.567  1.00 50.46  ? 308 EDO D O2  1 
HETATM 8001 C C1  . GOL MA 5 .   ? 24.120 -10.361 56.440  1.00 62.73  ? 309 GOL D C1  1 
HETATM 8002 O O1  . GOL MA 5 .   ? 23.089 -10.534 55.471  1.00 63.06  ? 309 GOL D O1  1 
HETATM 8003 C C2  . GOL MA 5 .   ? 23.812 -11.028 57.771  1.00 62.37  ? 309 GOL D C2  1 
HETATM 8004 O O2  . GOL MA 5 .   ? 24.216 -10.169 58.838  1.00 59.71  ? 309 GOL D O2  1 
HETATM 8005 C C3  . GOL MA 5 .   ? 22.363 -11.418 57.987  1.00 58.99  ? 309 GOL D C3  1 
HETATM 8006 O O3  . GOL MA 5 .   ? 21.997 -12.621 57.313  1.00 56.72  ? 309 GOL D O3  1 
HETATM 8007 O O   . HOH NA 8 .   ? 34.444 16.442  104.690 1.00 55.49  ? 401 HOH A O   1 
HETATM 8008 O O   . HOH NA 8 .   ? 34.006 20.133  73.952  1.00 43.14  ? 402 HOH A O   1 
HETATM 8009 O O   . HOH NA 8 .   ? 37.650 35.971  95.378  1.00 45.84  ? 403 HOH A O   1 
HETATM 8010 O O   . HOH NA 8 .   ? 35.880 34.173  80.964  1.00 47.01  ? 404 HOH A O   1 
HETATM 8011 O O   . HOH NA 8 .   ? 36.758 42.868  89.334  1.00 58.80  ? 405 HOH A O   1 
HETATM 8012 O O   . HOH NA 8 .   ? 21.370 36.247  74.885  1.00 41.68  ? 406 HOH A O   1 
HETATM 8013 O O   . HOH NA 8 .   ? 13.081 20.061  73.568  1.00 38.47  ? 407 HOH A O   1 
HETATM 8014 O O   . HOH NA 8 .   ? 35.352 25.772  87.104  1.00 36.34  ? 408 HOH A O   1 
HETATM 8015 O O   . HOH NA 8 .   ? 37.706 15.834  93.932  1.00 36.89  ? 409 HOH A O   1 
HETATM 8016 O O   . HOH NA 8 .   ? 4.716  24.848  85.786  1.00 55.47  ? 410 HOH A O   1 
HETATM 8017 O O   . HOH NA 8 .   ? 36.145 31.214  67.787  1.00 42.68  ? 411 HOH A O   1 
HETATM 8018 O O   . HOH NA 8 .   ? 40.495 21.798  82.622  1.00 40.05  ? 412 HOH A O   1 
HETATM 8019 O O   . HOH NA 8 .   ? 11.542 37.372  80.653  1.00 46.48  ? 413 HOH A O   1 
HETATM 8020 O O   . HOH NA 8 .   ? 15.721 25.905  103.977 1.00 37.98  ? 414 HOH A O   1 
HETATM 8021 O O   . HOH NA 8 .   ? 20.015 28.700  74.631  1.00 31.71  ? 415 HOH A O   1 
HETATM 8022 O O   . HOH NA 8 .   ? 28.591 26.899  72.085  1.00 37.19  ? 416 HOH A O   1 
HETATM 8023 O O   . HOH NA 8 .   ? 26.675 45.573  93.535  1.00 46.77  ? 417 HOH A O   1 
HETATM 8024 O O   . HOH NA 8 .   ? 21.861 40.570  95.632  1.00 51.43  ? 418 HOH A O   1 
HETATM 8025 O O   . HOH NA 8 .   ? 15.671 15.604  106.249 1.00 57.21  ? 419 HOH A O   1 
HETATM 8026 O O   . HOH NA 8 .   ? 19.169 23.158  107.688 1.00 58.41  ? 420 HOH A O   1 
HETATM 8027 O O   . HOH NA 8 .   ? 33.408 38.763  103.979 1.00 62.16  ? 421 HOH A O   1 
HETATM 8028 O O   . HOH NA 8 .   ? 40.047 17.096  77.211  1.00 50.42  ? 422 HOH A O   1 
HETATM 8029 O O   . HOH NA 8 .   ? 30.817 44.025  82.706  1.00 46.21  ? 423 HOH A O   1 
HETATM 8030 O O   . HOH NA 8 .   ? 16.125 45.977  84.485  1.00 38.87  ? 424 HOH A O   1 
HETATM 8031 O O   . HOH NA 8 .   ? 38.360 42.394  98.896  1.00 55.19  ? 425 HOH A O   1 
HETATM 8032 O O   . HOH NA 8 .   ? 8.092  22.261  102.226 1.00 48.58  ? 426 HOH A O   1 
HETATM 8033 O O   . HOH NA 8 .   ? 42.998 26.657  69.723  1.00 49.41  ? 427 HOH A O   1 
HETATM 8034 O O   . HOH NA 8 .   ? 13.560 32.281  106.992 1.00 61.07  ? 428 HOH A O   1 
HETATM 8035 O O   . HOH NA 8 .   ? 23.603 30.829  91.388  1.00 32.47  ? 429 HOH A O   1 
HETATM 8036 O O   . HOH NA 8 .   ? 11.063 31.060  101.583 1.00 47.96  ? 430 HOH A O   1 
HETATM 8037 O O   . HOH NA 8 .   ? 31.712 16.162  106.355 1.00 51.69  ? 431 HOH A O   1 
HETATM 8038 O O   . HOH NA 8 .   ? 13.796 16.166  102.830 1.00 46.17  ? 432 HOH A O   1 
HETATM 8039 O O   . HOH NA 8 .   ? 13.575 28.900  77.731  1.00 46.23  ? 433 HOH A O   1 
HETATM 8040 O O   . HOH NA 8 .   ? 30.596 18.988  82.498  1.00 47.62  ? 434 HOH A O   1 
HETATM 8041 O O   . HOH NA 8 .   ? 37.966 23.677  104.703 1.00 57.29  ? 435 HOH A O   1 
HETATM 8042 O O   . HOH NA 8 .   ? 7.265  24.408  95.248  1.00 39.52  ? 436 HOH A O   1 
HETATM 8043 O O   . HOH NA 8 .   ? 27.611 10.693  88.620  1.00 53.09  ? 437 HOH A O   1 
HETATM 8044 O O   . HOH NA 8 .   ? 25.544 13.714  89.952  1.00 51.76  ? 438 HOH A O   1 
HETATM 8045 O O   . HOH NA 8 .   ? 36.189 18.070  95.894  1.00 40.34  ? 439 HOH A O   1 
HETATM 8046 O O   . HOH NA 8 .   ? 29.738 30.348  96.976  1.00 32.25  ? 440 HOH A O   1 
HETATM 8047 O O   . HOH NA 8 .   ? 31.604 12.961  101.844 1.00 56.44  ? 441 HOH A O   1 
HETATM 8048 O O   . HOH NA 8 .   ? 11.443 9.725   101.633 1.00 53.43  ? 442 HOH A O   1 
HETATM 8049 O O   . HOH NA 8 .   ? 20.015 8.154   95.408  1.00 47.01  ? 443 HOH A O   1 
HETATM 8050 O O   . HOH NA 8 .   ? 24.544 25.577  106.843 1.00 42.85  ? 444 HOH A O   1 
HETATM 8051 O O   . HOH NA 8 .   ? 21.287 29.765  101.644 1.00 37.25  ? 445 HOH A O   1 
HETATM 8052 O O   . HOH NA 8 .   ? 30.781 18.852  95.635  1.00 39.87  ? 446 HOH A O   1 
HETATM 8053 O O   . HOH NA 8 .   ? 40.148 15.544  71.679  1.00 55.49  ? 447 HOH A O   1 
HETATM 8054 O O   . HOH NA 8 .   ? 38.523 22.551  84.446  1.00 45.50  ? 448 HOH A O   1 
HETATM 8055 O O   . HOH NA 8 .   ? 36.315 19.412  82.004  1.00 37.77  ? 449 HOH A O   1 
HETATM 8056 O O   . HOH NA 8 .   ? 32.657 8.992   95.104  1.00 50.11  ? 450 HOH A O   1 
HETATM 8057 O O   . HOH NA 8 .   ? 40.572 12.861  62.721  1.00 46.04  ? 451 HOH A O   1 
HETATM 8058 O O   . HOH NA 8 .   ? 5.001  36.031  90.447  1.00 51.98  ? 452 HOH A O   1 
HETATM 8059 O O   . HOH NA 8 .   ? 29.674 38.605  85.500  1.00 36.15  ? 453 HOH A O   1 
HETATM 8060 O O   . HOH NA 8 .   ? 33.738 33.019  101.983 1.00 53.16  ? 454 HOH A O   1 
HETATM 8061 O O   . HOH NA 8 .   ? 27.761 39.766  99.012  1.00 44.18  ? 455 HOH A O   1 
HETATM 8062 O O   . HOH NA 8 .   ? 43.286 19.580  73.643  1.00 62.33  ? 456 HOH A O   1 
HETATM 8063 O O   . HOH NA 8 .   ? 25.971 28.918  79.058  1.00 31.08  ? 457 HOH A O   1 
HETATM 8064 O O   . HOH NA 8 .   ? 43.050 27.885  92.164  1.00 59.40  ? 458 HOH A O   1 
HETATM 8065 O O   . HOH NA 8 .   ? 29.402 30.124  66.992  1.00 53.76  ? 459 HOH A O   1 
HETATM 8066 O O   . HOH NA 8 .   ? 10.253 40.002  99.423  1.00 44.07  ? 460 HOH A O   1 
HETATM 8067 O O   . HOH NA 8 .   ? 7.810  19.802  101.219 1.00 49.72  ? 461 HOH A O   1 
HETATM 8068 O O   . HOH NA 8 .   ? 20.294 18.997  85.257  1.00 54.75  ? 462 HOH A O   1 
HETATM 8069 O O   . HOH NA 8 .   ? 39.975 23.329  66.050  1.00 41.60  ? 463 HOH A O   1 
HETATM 8070 O O   . HOH NA 8 .   ? 35.749 20.596  71.998  1.00 37.63  ? 464 HOH A O   1 
HETATM 8071 O O   . HOH NA 8 .   ? 31.545 39.906  83.911  1.00 47.14  ? 465 HOH A O   1 
HETATM 8072 O O   . HOH NA 8 .   ? 27.358 14.330  93.653  1.00 41.12  ? 466 HOH A O   1 
HETATM 8073 O O   . HOH NA 8 .   ? 45.699 39.144  84.544  1.00 47.59  ? 467 HOH A O   1 
HETATM 8074 O O   . HOH NA 8 .   ? 22.227 16.549  88.877  1.00 52.62  ? 468 HOH A O   1 
HETATM 8075 O O   . HOH NA 8 .   ? 27.916 49.511  86.544  1.00 62.28  ? 469 HOH A O   1 
HETATM 8076 O O   . HOH NA 8 .   ? 13.619 20.376  79.952  1.00 42.53  ? 470 HOH A O   1 
HETATM 8077 O O   . HOH NA 8 .   ? 23.653 42.083  98.603  1.00 62.20  ? 471 HOH A O   1 
HETATM 8078 O O   . HOH NA 8 .   ? 39.307 25.103  100.032 1.00 54.12  ? 472 HOH A O   1 
HETATM 8079 O O   . HOH NA 8 .   ? 23.082 20.228  75.835  1.00 55.48  ? 473 HOH A O   1 
HETATM 8080 O O   . HOH NA 8 .   ? 29.152 26.841  69.236  1.00 46.93  ? 474 HOH A O   1 
HETATM 8081 O O   . HOH NA 8 .   ? 26.349 24.502  93.359  1.00 30.84  ? 475 HOH A O   1 
HETATM 8082 O O   . HOH NA 8 .   ? 43.029 34.085  80.501  1.00 50.85  ? 476 HOH A O   1 
HETATM 8083 O O   . HOH NA 8 .   ? 42.931 21.023  94.295  1.00 52.59  ? 477 HOH A O   1 
HETATM 8084 O O   . HOH NA 8 .   ? 11.444 20.049  104.978 1.00 44.93  ? 478 HOH A O   1 
HETATM 8085 O O   . HOH NA 8 .   ? 45.510 22.221  83.800  1.00 59.94  ? 479 HOH A O   1 
HETATM 8086 O O   . HOH NA 8 .   ? 38.978 30.009  69.162  1.00 55.66  ? 480 HOH A O   1 
HETATM 8087 O O   . HOH NA 8 .   ? 28.698 41.520  80.558  1.00 53.77  ? 481 HOH A O   1 
HETATM 8088 O O   . HOH NA 8 .   ? 25.332 22.124  94.186  1.00 28.46  ? 482 HOH A O   1 
HETATM 8089 O O   . HOH NA 8 .   ? 7.466  34.537  82.694  1.00 56.03  ? 483 HOH A O   1 
HETATM 8090 O O   . HOH NA 8 .   ? 29.421 7.658   92.102  1.00 52.70  ? 484 HOH A O   1 
HETATM 8091 O O   . HOH NA 8 .   ? 40.712 25.555  96.491  1.00 36.04  ? 485 HOH A O   1 
HETATM 8092 O O   . HOH NA 8 .   ? 7.554  32.655  84.698  1.00 47.57  ? 486 HOH A O   1 
HETATM 8093 O O   . HOH NA 8 .   ? 31.042 31.942  65.466  1.00 48.21  ? 487 HOH A O   1 
HETATM 8094 O O   . HOH NA 8 .   ? 40.749 22.983  97.306  1.00 57.72  ? 488 HOH A O   1 
HETATM 8095 O O   . HOH NA 8 .   ? 30.890 25.096  84.965  1.00 43.78  ? 489 HOH A O   1 
HETATM 8096 O O   . HOH NA 8 .   ? 31.219 33.456  102.638 1.00 42.64  ? 490 HOH A O   1 
HETATM 8097 O O   . HOH NA 8 .   ? 4.970  36.268  99.654  1.00 47.93  ? 491 HOH A O   1 
HETATM 8098 O O   . HOH NA 8 .   ? 42.137 18.708  100.295 1.00 56.10  ? 492 HOH A O   1 
HETATM 8099 O O   . HOH NA 8 .   ? 39.331 14.991  86.454  1.00 46.61  ? 493 HOH A O   1 
HETATM 8100 O O   . HOH NA 8 .   ? 9.744  31.393  82.447  1.00 41.48  ? 494 HOH A O   1 
HETATM 8101 O O   . HOH NA 8 .   ? 20.985 39.426  103.001 1.00 47.76  ? 495 HOH A O   1 
HETATM 8102 O O   . HOH NA 8 .   ? 13.305 39.228  104.821 1.00 52.92  ? 496 HOH A O   1 
HETATM 8103 O O   . HOH NA 8 .   ? 22.749 42.727  94.483  1.00 42.43  ? 497 HOH A O   1 
HETATM 8104 O O   . HOH NA 8 .   ? 9.107  29.714  100.265 1.00 37.77  ? 498 HOH A O   1 
HETATM 8105 O O   . HOH NA 8 .   ? 34.175 21.607  82.574  1.00 46.78  ? 499 HOH A O   1 
HETATM 8106 O O   . HOH NA 8 .   ? 27.315 9.021   97.116  1.00 43.27  ? 500 HOH A O   1 
HETATM 8107 O O   . HOH NA 8 .   ? 21.572 22.379  78.056  1.00 38.50  ? 501 HOH A O   1 
HETATM 8108 O O   . HOH NA 8 .   ? 15.788 25.576  112.641 1.00 61.23  ? 502 HOH A O   1 
HETATM 8109 O O   . HOH NA 8 .   ? 13.316 13.896  101.499 1.00 36.54  ? 503 HOH A O   1 
HETATM 8110 O O   . HOH NA 8 .   ? 32.420 22.172  84.732  1.00 52.06  ? 504 HOH A O   1 
HETATM 8111 O O   . HOH NA 8 .   ? 32.504 31.682  61.351  1.00 65.44  ? 505 HOH A O   1 
HETATM 8112 O O   . HOH NA 8 .   ? 38.092 37.793  71.363  1.00 58.51  ? 506 HOH A O   1 
HETATM 8113 O O   . HOH NA 8 .   ? 33.275 28.485  110.578 1.00 60.65  ? 507 HOH A O   1 
HETATM 8114 O O   . HOH NA 8 .   ? 43.005 24.924  67.467  1.00 50.70  ? 508 HOH A O   1 
HETATM 8115 O O   . HOH NA 8 .   ? 18.477 39.841  78.674  1.00 46.30  ? 509 HOH A O   1 
HETATM 8116 O O   . HOH NA 8 .   ? 22.111 10.738  97.211  1.00 55.12  ? 510 HOH A O   1 
HETATM 8117 O O   . HOH NA 8 .   ? 33.507 22.520  108.012 1.00 49.88  ? 511 HOH A O   1 
HETATM 8118 O O   . HOH NA 8 .   ? 27.748 20.168  80.404  1.00 40.20  ? 512 HOH A O   1 
HETATM 8119 O O   . HOH NA 8 .   ? 18.418 21.479  79.497  1.00 43.15  ? 513 HOH A O   1 
HETATM 8120 O O   . HOH NA 8 .   ? 29.903 16.631  80.194  1.00 51.19  ? 514 HOH A O   1 
HETATM 8121 O O   . HOH NA 8 .   ? 24.687 31.263  79.275  1.00 31.99  ? 515 HOH A O   1 
HETATM 8122 O O   . HOH NA 8 .   ? 24.835 21.474  81.272  1.00 46.79  ? 516 HOH A O   1 
HETATM 8123 O O   . HOH NA 8 .   ? 36.907 37.838  78.802  1.00 51.54  ? 517 HOH A O   1 
HETATM 8124 O O   . HOH NA 8 .   ? 22.644 43.479  81.594  1.00 48.60  ? 518 HOH A O   1 
HETATM 8125 O O   . HOH NA 8 .   ? 33.442 25.237  110.356 1.00 59.90  ? 519 HOH A O   1 
HETATM 8126 O O   . HOH NA 8 .   ? 29.554 35.416  71.273  1.00 41.19  ? 520 HOH A O   1 
HETATM 8127 O O   . HOH NA 8 .   ? 19.860 41.539  80.454  1.00 45.98  ? 521 HOH A O   1 
HETATM 8128 O O   . HOH NA 8 .   ? 30.053 40.493  100.963 1.00 49.84  ? 522 HOH A O   1 
HETATM 8129 O O   . HOH NA 8 .   ? 34.584 27.570  59.695  1.00 48.46  ? 523 HOH A O   1 
HETATM 8130 O O   . HOH NA 8 .   ? 9.710  40.454  95.211  1.00 41.84  ? 524 HOH A O   1 
HETATM 8131 O O   . HOH NA 8 .   ? 6.592  16.079  100.872 1.00 63.15  ? 525 HOH A O   1 
HETATM 8132 O O   . HOH NA 8 .   ? 25.493 48.981  87.705  1.00 62.01  ? 526 HOH A O   1 
HETATM 8133 O O   . HOH NA 8 .   ? 37.574 37.713  75.697  1.00 54.11  ? 527 HOH A O   1 
HETATM 8134 O O   . HOH NA 8 .   ? 17.688 18.831  85.966  1.00 57.83  ? 528 HOH A O   1 
HETATM 8135 O O   . HOH NA 8 .   ? 3.031  24.115  87.907  1.00 44.10  ? 529 HOH A O   1 
HETATM 8136 O O   . HOH NA 8 .   ? 43.830 21.407  67.627  1.00 57.95  ? 530 HOH A O   1 
HETATM 8137 O O   . HOH NA 8 .   ? 30.978 34.917  105.307 1.00 56.56  ? 531 HOH A O   1 
HETATM 8138 O O   . HOH NA 8 .   ? 6.881  38.875  82.798  1.00 59.10  ? 532 HOH A O   1 
HETATM 8139 O O   . HOH NA 8 .   ? 5.162  16.186  94.849  1.00 68.42  ? 533 HOH A O   1 
HETATM 8140 O O   . HOH NA 8 .   ? 33.298 10.837  102.497 1.00 56.99  ? 534 HOH A O   1 
HETATM 8141 O O   . HOH NA 8 .   ? 11.174 31.247  104.468 1.00 45.53  ? 535 HOH A O   1 
HETATM 8142 O O   . HOH NA 8 .   ? 5.991  40.089  85.618  1.00 48.05  ? 536 HOH A O   1 
HETATM 8143 O O   . HOH NA 8 .   ? 14.323 27.508  105.862 1.00 47.05  ? 537 HOH A O   1 
HETATM 8144 O O   . HOH NA 8 .   ? 41.654 17.458  74.319  1.00 63.77  ? 538 HOH A O   1 
HETATM 8145 O O   . HOH NA 8 .   ? 42.779 26.681  97.941  1.00 54.70  ? 539 HOH A O   1 
HETATM 8146 O O   . HOH NA 8 .   ? 23.897 15.816  91.925  1.00 45.68  ? 540 HOH A O   1 
HETATM 8147 O O   . HOH NA 8 .   ? 28.311 33.911  69.433  1.00 45.59  ? 541 HOH A O   1 
HETATM 8148 O O   . HOH NA 8 .   ? 11.628 17.503  104.394 1.00 53.14  ? 542 HOH A O   1 
HETATM 8149 O O   . HOH NA 8 .   ? 12.096 36.234  73.557  1.00 51.12  ? 543 HOH A O   1 
HETATM 8150 O O   . HOH NA 8 .   ? 13.292 30.211  105.731 1.00 53.08  ? 544 HOH A O   1 
HETATM 8151 O O   . HOH NA 8 .   ? 1.321  25.115  89.966  1.00 56.35  ? 545 HOH A O   1 
HETATM 8152 O O   . HOH NA 8 .   ? 41.957 15.518  62.045  1.00 53.82  ? 546 HOH A O   1 
HETATM 8153 O O   . HOH NA 8 .   ? 24.738 46.347  95.918  1.00 58.72  ? 547 HOH A O   1 
HETATM 8154 O O   . HOH OA 8 .   ? 16.659 -5.339  97.946  1.00 46.38  ? 401 HOH B O   1 
HETATM 8155 O O   . HOH OA 8 .   ? 42.220 0.805   107.042 1.00 49.27  ? 402 HOH B O   1 
HETATM 8156 O O   . HOH OA 8 .   ? 16.194 -20.106 120.438 1.00 34.71  ? 403 HOH B O   1 
HETATM 8157 O O   . HOH OA 8 .   ? 18.571 -30.183 115.579 1.00 44.86  ? 404 HOH B O   1 
HETATM 8158 O O   . HOH OA 8 .   ? 10.995 -19.885 113.984 1.00 39.51  ? 405 HOH B O   1 
HETATM 8159 O O   . HOH OA 8 .   ? 14.280 -0.925  128.327 1.00 61.32  ? 406 HOH B O   1 
HETATM 8160 O O   . HOH OA 8 .   ? 35.035 9.466   100.862 1.00 52.20  ? 407 HOH B O   1 
HETATM 8161 O O   . HOH OA 8 .   ? 13.349 -0.609  122.531 1.00 60.18  ? 408 HOH B O   1 
HETATM 8162 O O   . HOH OA 8 .   ? 11.597 -10.661 109.327 1.00 42.83  ? 409 HOH B O   1 
HETATM 8163 O O   . HOH OA 8 .   ? 13.323 3.687   125.923 1.00 63.85  ? 410 HOH B O   1 
HETATM 8164 O O   . HOH OA 8 .   ? 31.549 4.170   116.631 1.00 31.24  ? 411 HOH B O   1 
HETATM 8165 O O   . HOH OA 8 .   ? 18.237 -25.034 103.672 1.00 40.24  ? 412 HOH B O   1 
HETATM 8166 O O   . HOH OA 8 .   ? 6.510  -9.929  117.407 1.00 48.46  ? 413 HOH B O   1 
HETATM 8167 O O   . HOH OA 8 .   ? 4.024  -26.856 102.183 1.00 39.19  ? 414 HOH B O   1 
HETATM 8168 O O   . HOH OA 8 .   ? 35.896 -21.515 115.797 1.00 39.94  ? 415 HOH B O   1 
HETATM 8169 O O   . HOH OA 8 .   ? 25.842 -9.867  125.903 1.00 42.48  ? 416 HOH B O   1 
HETATM 8170 O O   . HOH OA 8 .   ? 10.315 -12.586 101.482 1.00 39.41  ? 417 HOH B O   1 
HETATM 8171 O O   . HOH OA 8 .   ? 39.853 -20.373 117.720 1.00 53.66  ? 418 HOH B O   1 
HETATM 8172 O O   . HOH OA 8 .   ? 15.148 -8.384  97.438  1.00 44.47  ? 419 HOH B O   1 
HETATM 8173 O O   . HOH OA 8 .   ? 39.915 -2.829  110.871 1.00 38.08  ? 420 HOH B O   1 
HETATM 8174 O O   . HOH OA 8 .   ? 10.860 -30.743 105.505 1.00 33.94  ? 421 HOH B O   1 
HETATM 8175 O O   . HOH OA 8 .   ? 34.274 -0.341  128.635 1.00 45.09  ? 422 HOH B O   1 
HETATM 8176 O O   . HOH OA 8 .   ? 44.506 1.536   115.913 1.00 37.42  ? 423 HOH B O   1 
HETATM 8177 O O   . HOH OA 8 .   ? 14.485 -11.159 105.087 1.00 57.80  ? 424 HOH B O   1 
HETATM 8178 O O   . HOH OA 8 .   ? 26.971 -23.185 105.920 1.00 31.95  ? 425 HOH B O   1 
HETATM 8179 O O   . HOH OA 8 .   ? 24.599 -5.062  101.774 1.00 49.36  ? 426 HOH B O   1 
HETATM 8180 O O   . HOH OA 8 .   ? 9.085  -0.043  103.984 1.00 43.99  ? 427 HOH B O   1 
HETATM 8181 O O   . HOH OA 8 .   ? 6.575  -15.483 97.148  1.00 46.22  ? 428 HOH B O   1 
HETATM 8182 O O   . HOH OA 8 .   ? 21.925 -25.936 109.605 1.00 45.01  ? 429 HOH B O   1 
HETATM 8183 O O   . HOH OA 8 .   ? 5.622  -13.381 117.576 1.00 49.79  ? 430 HOH B O   1 
HETATM 8184 O O   . HOH OA 8 .   ? 11.338 -22.068 98.156  1.00 45.98  ? 431 HOH B O   1 
HETATM 8185 O O   . HOH OA 8 .   ? 36.863 -0.037  119.816 1.00 38.28  ? 432 HOH B O   1 
HETATM 8186 O O   . HOH OA 8 .   ? 0.625  -20.269 103.580 1.00 52.72  ? 433 HOH B O   1 
HETATM 8187 O O   . HOH OA 8 .   ? 39.472 4.675   109.388 1.00 51.49  ? 434 HOH B O   1 
HETATM 8188 O O   . HOH OA 8 .   ? 30.608 11.721  109.724 1.00 50.89  ? 435 HOH B O   1 
HETATM 8189 O O   . HOH OA 8 .   ? 7.099  -28.846 97.506  1.00 47.43  ? 436 HOH B O   1 
HETATM 8190 O O   . HOH OA 8 .   ? 13.687 -26.339 111.516 1.00 37.69  ? 437 HOH B O   1 
HETATM 8191 O O   . HOH OA 8 .   ? 36.649 -20.463 111.438 1.00 40.33  ? 438 HOH B O   1 
HETATM 8192 O O   . HOH OA 8 .   ? 39.119 4.062   112.020 1.00 57.66  ? 439 HOH B O   1 
HETATM 8193 O O   . HOH OA 8 .   ? 23.616 -9.152  115.656 1.00 32.43  ? 440 HOH B O   1 
HETATM 8194 O O   . HOH OA 8 .   ? 17.889 -17.839 119.917 1.00 29.75  ? 441 HOH B O   1 
HETATM 8195 O O   . HOH OA 8 .   ? 8.339  -11.790 105.504 1.00 42.63  ? 442 HOH B O   1 
HETATM 8196 O O   . HOH OA 8 .   ? 11.902 -32.113 107.693 1.00 43.04  ? 443 HOH B O   1 
HETATM 8197 O O   . HOH OA 8 .   ? 15.961 0.087   107.043 1.00 34.21  ? 444 HOH B O   1 
HETATM 8198 O O   . HOH OA 8 .   ? 38.700 -0.533  117.770 1.00 34.73  ? 445 HOH B O   1 
HETATM 8199 O O   . HOH OA 8 .   ? 7.426  -29.448 103.949 1.00 46.00  ? 446 HOH B O   1 
HETATM 8200 O O   . HOH OA 8 .   ? 20.975 -19.240 108.219 1.00 32.45  ? 447 HOH B O   1 
HETATM 8201 O O   . HOH OA 8 .   ? 17.548 -3.984  117.894 1.00 34.51  ? 448 HOH B O   1 
HETATM 8202 O O   . HOH OA 8 .   ? 19.617 -6.496  126.789 1.00 42.81  ? 449 HOH B O   1 
HETATM 8203 O O   . HOH OA 8 .   ? 15.046 -24.871 116.567 1.00 59.79  ? 450 HOH B O   1 
HETATM 8204 O O   . HOH OA 8 .   ? 26.630 -2.909  128.318 1.00 33.90  ? 451 HOH B O   1 
HETATM 8205 O O   . HOH OA 8 .   ? 8.872  -8.366  129.035 1.00 55.10  ? 452 HOH B O   1 
HETATM 8206 O O   . HOH OA 8 .   ? 23.319 -17.190 127.634 1.00 47.95  ? 453 HOH B O   1 
HETATM 8207 O O   . HOH OA 8 .   ? 15.124 8.036   104.816 1.00 36.81  ? 454 HOH B O   1 
HETATM 8208 O O   . HOH OA 8 .   ? 32.864 8.094   107.231 1.00 44.84  ? 455 HOH B O   1 
HETATM 8209 O O   . HOH OA 8 .   ? 16.053 -12.433 107.652 1.00 46.11  ? 456 HOH B O   1 
HETATM 8210 O O   . HOH OA 8 .   ? 14.115 4.412   97.972  1.00 49.99  ? 457 HOH B O   1 
HETATM 8211 O O   . HOH OA 8 .   ? 19.746 5.890   99.230  1.00 45.23  ? 458 HOH B O   1 
HETATM 8212 O O   . HOH OA 8 .   ? 6.537  -13.189 104.231 1.00 46.82  ? 459 HOH B O   1 
HETATM 8213 O O   . HOH OA 8 .   ? 6.331  -26.875 86.635  1.00 36.92  ? 460 HOH B O   1 
HETATM 8214 O O   . HOH OA 8 .   ? 18.919 -23.737 120.218 1.00 46.72  ? 461 HOH B O   1 
HETATM 8215 O O   . HOH OA 8 .   ? 26.021 0.579   119.449 1.00 32.42  ? 462 HOH B O   1 
HETATM 8216 O O   . HOH OA 8 .   ? 1.366  -11.862 105.265 1.00 53.08  ? 463 HOH B O   1 
HETATM 8217 O O   . HOH OA 8 .   ? 10.447 -20.658 125.666 1.00 52.40  ? 464 HOH B O   1 
HETATM 8218 O O   . HOH OA 8 .   ? 7.001  -33.541 98.364  1.00 39.87  ? 465 HOH B O   1 
HETATM 8219 O O   . HOH OA 8 .   ? 4.919  -2.798  104.350 1.00 51.63  ? 466 HOH B O   1 
HETATM 8220 O O   . HOH OA 8 .   ? 24.647 -11.878 127.371 1.00 39.46  ? 467 HOH B O   1 
HETATM 8221 O O   . HOH OA 8 .   ? 40.897 -12.365 112.059 1.00 39.13  ? 468 HOH B O   1 
HETATM 8222 O O   . HOH OA 8 .   ? 20.783 -4.550  110.839 1.00 28.70  ? 469 HOH B O   1 
HETATM 8223 O O   . HOH OA 8 .   ? 28.067 -17.781 101.249 1.00 48.27  ? 470 HOH B O   1 
HETATM 8224 O O   . HOH OA 8 .   ? 10.031 -23.217 116.132 1.00 42.97  ? 471 HOH B O   1 
HETATM 8225 O O   . HOH OA 8 .   ? 12.689 -12.659 103.538 1.00 46.73  ? 472 HOH B O   1 
HETATM 8226 O O   . HOH OA 8 .   ? 7.050  -19.854 93.483  1.00 51.07  ? 473 HOH B O   1 
HETATM 8227 O O   . HOH OA 8 .   ? 10.827 -19.733 117.222 1.00 44.60  ? 474 HOH B O   1 
HETATM 8228 O O   . HOH OA 8 .   ? 28.579 5.023   131.457 1.00 48.60  ? 475 HOH B O   1 
HETATM 8229 O O   . HOH OA 8 .   ? 20.046 -14.253 129.602 1.00 42.74  ? 476 HOH B O   1 
HETATM 8230 O O   . HOH OA 8 .   ? 21.617 -2.573  109.139 1.00 30.14  ? 477 HOH B O   1 
HETATM 8231 O O   . HOH OA 8 .   ? 19.447 0.751   102.157 1.00 42.89  ? 478 HOH B O   1 
HETATM 8232 O O   . HOH OA 8 .   ? 25.228 -17.329 101.962 1.00 34.42  ? 479 HOH B O   1 
HETATM 8233 O O   . HOH OA 8 .   ? 22.471 -20.145 110.404 1.00 35.34  ? 480 HOH B O   1 
HETATM 8234 O O   . HOH OA 8 .   ? 35.175 -6.456  100.619 1.00 56.11  ? 481 HOH B O   1 
HETATM 8235 O O   . HOH OA 8 .   ? 29.703 7.154   117.364 1.00 54.11  ? 482 HOH B O   1 
HETATM 8236 O O   . HOH OA 8 .   ? 10.210 -35.314 100.327 1.00 51.53  ? 483 HOH B O   1 
HETATM 8237 O O   . HOH OA 8 .   ? 33.632 7.535   104.815 1.00 34.12  ? 484 HOH B O   1 
HETATM 8238 O O   . HOH OA 8 .   ? 37.305 -17.834 112.082 1.00 50.10  ? 485 HOH B O   1 
HETATM 8239 O O   . HOH OA 8 .   ? 27.619 -23.565 120.102 1.00 39.81  ? 486 HOH B O   1 
HETATM 8240 O O   . HOH OA 8 .   ? 16.608 -12.711 97.708  1.00 59.40  ? 487 HOH B O   1 
HETATM 8241 O O   . HOH OA 8 .   ? 2.426  -15.286 103.312 1.00 46.54  ? 488 HOH B O   1 
HETATM 8242 O O   . HOH OA 8 .   ? 7.752  -11.814 129.137 1.00 62.07  ? 489 HOH B O   1 
HETATM 8243 O O   . HOH OA 8 .   ? 24.550 7.466   129.796 1.00 57.41  ? 490 HOH B O   1 
HETATM 8244 O O   . HOH OA 8 .   ? 17.916 -27.260 102.290 1.00 42.87  ? 491 HOH B O   1 
HETATM 8245 O O   . HOH OA 8 .   ? 13.904 8.781   122.389 1.00 50.96  ? 492 HOH B O   1 
HETATM 8246 O O   . HOH OA 8 .   ? 33.932 4.232   123.217 1.00 49.07  ? 493 HOH B O   1 
HETATM 8247 O O   . HOH OA 8 .   ? 8.886  -26.380 114.679 1.00 43.01  ? 494 HOH B O   1 
HETATM 8248 O O   . HOH OA 8 .   ? 3.770  -2.334  108.967 1.00 56.77  ? 495 HOH B O   1 
HETATM 8249 O O   . HOH OA 8 .   ? 34.821 -9.070  130.486 1.00 48.30  ? 496 HOH B O   1 
HETATM 8250 O O   . HOH OA 8 .   ? 25.295 -23.736 122.017 1.00 42.70  ? 497 HOH B O   1 
HETATM 8251 O O   . HOH OA 8 .   ? 27.970 -13.266 130.778 1.00 58.73  ? 498 HOH B O   1 
HETATM 8252 O O   . HOH OA 8 .   ? 17.036 -4.936  128.329 1.00 47.03  ? 499 HOH B O   1 
HETATM 8253 O O   . HOH OA 8 .   ? 28.746 -24.715 117.655 1.00 40.82  ? 500 HOH B O   1 
HETATM 8254 O O   . HOH OA 8 .   ? 31.934 2.369   99.283  1.00 56.38  ? 501 HOH B O   1 
HETATM 8255 O O   . HOH OA 8 .   ? 35.884 7.911   111.621 1.00 43.18  ? 502 HOH B O   1 
HETATM 8256 O O   . HOH OA 8 .   ? 43.879 -8.865  107.266 1.00 46.94  ? 503 HOH B O   1 
HETATM 8257 O O   . HOH OA 8 .   ? 18.924 -13.818 101.120 1.00 42.49  ? 504 HOH B O   1 
HETATM 8258 O O   . HOH OA 8 .   ? 3.997  -7.681  113.880 1.00 56.60  ? 505 HOH B O   1 
HETATM 8259 O O   . HOH OA 8 .   ? 3.586  -20.199 113.923 1.00 42.16  ? 506 HOH B O   1 
HETATM 8260 O O   . HOH OA 8 .   ? 43.287 -4.087  111.568 1.00 69.59  ? 507 HOH B O   1 
HETATM 8261 O O   . HOH OA 8 .   ? 20.049 4.091   122.242 1.00 56.97  ? 508 HOH B O   1 
HETATM 8262 O O   . HOH OA 8 .   ? 33.205 -14.696 100.787 1.00 50.30  ? 509 HOH B O   1 
HETATM 8263 O O   . HOH OA 8 .   ? 12.818 8.949   115.607 1.00 58.42  ? 510 HOH B O   1 
HETATM 8264 O O   . HOH OA 8 .   ? 3.176  -26.147 96.300  1.00 51.30  ? 511 HOH B O   1 
HETATM 8265 O O   . HOH OA 8 .   ? 37.896 -9.737  125.247 1.00 58.42  ? 512 HOH B O   1 
HETATM 8266 O O   . HOH OA 8 .   ? 8.998  7.119   110.991 1.00 52.39  ? 513 HOH B O   1 
HETATM 8267 O O   . HOH OA 8 .   ? 9.987  -29.081 109.430 1.00 42.48  ? 514 HOH B O   1 
HETATM 8268 O O   . HOH OA 8 .   ? 24.527 -29.964 105.857 1.00 60.97  ? 515 HOH B O   1 
HETATM 8269 O O   . HOH OA 8 .   ? 6.159  -33.371 105.332 1.00 62.80  ? 516 HOH B O   1 
HETATM 8270 O O   . HOH OA 8 .   ? 42.893 1.406   118.436 1.00 49.23  ? 517 HOH B O   1 
HETATM 8271 O O   . HOH OA 8 .   ? 28.432 -6.651  128.787 1.00 59.23  ? 518 HOH B O   1 
HETATM 8272 O O   . HOH OA 8 .   ? 8.639  4.235   124.901 1.00 65.97  ? 519 HOH B O   1 
HETATM 8273 O O   . HOH OA 8 .   ? 9.331  -17.104 128.161 1.00 63.85  ? 520 HOH B O   1 
HETATM 8274 O O   . HOH OA 8 .   ? 11.157 -27.421 110.988 1.00 45.20  ? 521 HOH B O   1 
HETATM 8275 O O   . HOH OA 8 .   ? 4.654  -15.224 104.842 1.00 65.76  ? 522 HOH B O   1 
HETATM 8276 O O   . HOH OA 8 .   ? 36.312 10.700  117.922 1.00 57.37  ? 523 HOH B O   1 
HETATM 8277 O O   . HOH OA 8 .   ? 5.037  -29.217 103.737 1.00 54.57  ? 524 HOH B O   1 
HETATM 8278 O O   . HOH OA 8 .   ? 36.882 2.360   121.155 1.00 36.03  ? 525 HOH B O   1 
HETATM 8279 O O   . HOH OA 8 .   ? 2.505  -12.222 117.217 1.00 68.73  ? 526 HOH B O   1 
HETATM 8280 O O   . HOH OA 8 .   ? 23.902 -14.744 101.856 1.00 45.74  ? 527 HOH B O   1 
HETATM 8281 O O   . HOH OA 8 .   ? 5.364  -14.098 124.836 1.00 61.09  ? 528 HOH B O   1 
HETATM 8282 O O   . HOH OA 8 .   ? 24.969 -26.472 110.262 1.00 59.37  ? 529 HOH B O   1 
HETATM 8283 O O   . HOH OA 8 .   ? 31.282 -17.997 98.203  1.00 55.10  ? 530 HOH B O   1 
HETATM 8284 O O   . HOH OA 8 .   ? 3.933  -9.326  116.698 1.00 57.78  ? 531 HOH B O   1 
HETATM 8285 O O   . HOH OA 8 .   ? 37.292 8.831   106.888 1.00 58.20  ? 532 HOH B O   1 
HETATM 8286 O O   . HOH OA 8 .   ? 40.357 1.738   118.400 1.00 37.85  ? 533 HOH B O   1 
HETATM 8287 O O   . HOH OA 8 .   ? 35.354 8.993   109.231 1.00 53.11  ? 534 HOH B O   1 
HETATM 8288 O O   . HOH OA 8 .   ? 40.453 4.212   117.023 1.00 61.63  ? 535 HOH B O   1 
HETATM 8289 O O   . HOH PA 8 .   ? 21.014 -36.343 97.298  1.00 44.53  ? 401 HOH C O   1 
HETATM 8290 O O   . HOH PA 8 .   ? 36.452 -43.014 82.507  1.00 61.10  ? 402 HOH C O   1 
HETATM 8291 O O   . HOH PA 8 .   ? 33.922 -20.052 98.001  1.00 44.35  ? 403 HOH C O   1 
HETATM 8292 O O   . HOH PA 8 .   ? 40.456 -17.200 94.646  1.00 54.43  ? 404 HOH C O   1 
HETATM 8293 O O   . HOH PA 8 .   ? 13.226 -19.878 98.425  1.00 48.21  ? 405 HOH C O   1 
HETATM 8294 O O   . HOH PA 8 .   ? 34.500 -16.470 67.259  1.00 55.74  ? 406 HOH C O   1 
HETATM 8295 O O   . HOH PA 8 .   ? 35.251 -25.687 84.754  1.00 37.90  ? 407 HOH C O   1 
HETATM 8296 O O   . HOH PA 8 .   ? 37.602 -35.965 76.441  1.00 48.75  ? 408 HOH C O   1 
HETATM 8297 O O   . HOH PA 8 .   ? 30.685 -44.192 89.386  1.00 52.26  ? 409 HOH C O   1 
HETATM 8298 O O   . HOH PA 8 .   ? 30.317 -13.309 85.087  1.00 43.60  ? 410 HOH C O   1 
HETATM 8299 O O   . HOH PA 8 .   ? 18.939 -23.304 64.126  1.00 56.09  ? 411 HOH C O   1 
HETATM 8300 O O   . HOH PA 8 .   ? 15.726 -25.777 67.799  1.00 44.14  ? 412 HOH C O   1 
HETATM 8301 O O   . HOH PA 8 .   ? 35.809 -34.308 90.843  1.00 46.09  ? 413 HOH C O   1 
HETATM 8302 O O   . HOH PA 8 .   ? 4.810  -24.950 86.023  1.00 49.83  ? 414 HOH C O   1 
HETATM 8303 O O   . HOH PA 8 .   ? 36.107 -31.203 104.109 1.00 37.63  ? 415 HOH C O   1 
HETATM 8304 O O   . HOH PA 8 .   ? 30.738 -18.994 89.513  1.00 51.06  ? 416 HOH C O   1 
HETATM 8305 O O   . HOH PA 8 .   ? 11.568 -37.000 91.063  1.00 39.97  ? 417 HOH C O   1 
HETATM 8306 O O   . HOH PA 8 .   ? 21.112 -41.184 73.539  1.00 55.22  ? 418 HOH C O   1 
HETATM 8307 O O   . HOH PA 8 .   ? 21.972 -38.736 98.192  1.00 42.50  ? 419 HOH C O   1 
HETATM 8308 O O   . HOH PA 8 .   ? 20.011 -28.677 97.274  1.00 33.86  ? 420 HOH C O   1 
HETATM 8309 O O   . HOH PA 8 .   ? 37.691 -15.739 77.842  1.00 37.76  ? 421 HOH C O   1 
HETATM 8310 O O   . HOH PA 8 .   ? 28.584 -27.036 99.918  1.00 35.30  ? 422 HOH C O   1 
HETATM 8311 O O   . HOH PA 8 .   ? 39.308 -25.215 71.793  1.00 52.06  ? 423 HOH C O   1 
HETATM 8312 O O   . HOH PA 8 .   ? 24.086 -45.080 81.974  1.00 51.25  ? 424 HOH C O   1 
HETATM 8313 O O   . HOH PA 8 .   ? 40.426 -21.962 89.342  1.00 43.80  ? 425 HOH C O   1 
HETATM 8314 O O   . HOH PA 8 .   ? 19.797 -8.170  76.484  1.00 46.19  ? 426 HOH C O   1 
HETATM 8315 O O   . HOH PA 8 .   ? 31.379 -14.297 87.934  1.00 51.53  ? 427 HOH C O   1 
HETATM 8316 O O   . HOH PA 8 .   ? 20.429 -19.235 86.626  1.00 56.93  ? 428 HOH C O   1 
HETATM 8317 O O   . HOH PA 8 .   ? 31.468 -39.954 88.009  1.00 44.21  ? 429 HOH C O   1 
HETATM 8318 O O   . HOH PA 8 .   ? 29.340 -26.805 102.689 1.00 53.10  ? 430 HOH C O   1 
HETATM 8319 O O   . HOH PA 8 .   ? 10.797 -30.973 70.334  1.00 45.85  ? 431 HOH C O   1 
HETATM 8320 O O   . HOH PA 8 .   ? 15.701 -15.787 65.406  1.00 58.72  ? 432 HOH C O   1 
HETATM 8321 O O   . HOH PA 8 .   ? 39.179 -14.940 85.295  1.00 50.06  ? 433 HOH C O   1 
HETATM 8322 O O   . HOH PA 8 .   ? 27.282 -14.279 78.266  1.00 43.97  ? 434 HOH C O   1 
HETATM 8323 O O   . HOH PA 8 .   ? 7.259  -24.481 76.594  1.00 40.81  ? 435 HOH C O   1 
HETATM 8324 O O   . HOH PA 8 .   ? 35.676 -20.727 99.837  1.00 37.94  ? 436 HOH C O   1 
HETATM 8325 O O   . HOH PA 8 .   ? 27.232 -10.896 83.220  1.00 48.24  ? 437 HOH C O   1 
HETATM 8326 O O   . HOH PA 8 .   ? 25.993 -28.929 92.782  1.00 33.57  ? 438 HOH C O   1 
HETATM 8327 O O   . HOH PA 8 .   ? 31.730 -16.078 65.312  1.00 48.26  ? 439 HOH C O   1 
HETATM 8328 O O   . HOH PA 8 .   ? 23.698 -30.876 80.535  1.00 32.64  ? 440 HOH C O   1 
HETATM 8329 O O   . HOH PA 8 .   ? 26.383 -24.530 78.492  1.00 30.62  ? 441 HOH C O   1 
HETATM 8330 O O   . HOH PA 8 .   ? 32.467 -22.183 87.204  1.00 54.08  ? 442 HOH C O   1 
HETATM 8331 O O   . HOH PA 8 .   ? 45.736 -39.136 87.167  1.00 45.91  ? 443 HOH C O   1 
HETATM 8332 O O   . HOH PA 8 .   ? 26.461 -45.792 78.513  1.00 55.69  ? 444 HOH C O   1 
HETATM 8333 O O   . HOH PA 8 .   ? 29.668 -38.604 86.378  1.00 32.77  ? 445 HOH C O   1 
HETATM 8334 O O   . HOH PA 8 .   ? 40.628 -12.898 109.088 1.00 43.00  ? 446 HOH C O   1 
HETATM 8335 O O   . HOH PA 8 .   ? 29.790 -30.402 74.994  1.00 36.86  ? 447 HOH C O   1 
HETATM 8336 O O   . HOH PA 8 .   ? 36.371 -19.462 89.907  1.00 37.15  ? 448 HOH C O   1 
HETATM 8337 O O   . HOH PA 8 .   ? 39.998 -23.175 105.823 1.00 40.35  ? 449 HOH C O   1 
HETATM 8338 O O   . HOH PA 8 .   ? 42.968 -28.121 79.532  1.00 51.10  ? 450 HOH C O   1 
HETATM 8339 O O   . HOH PA 8 .   ? 24.752 -21.937 90.659  1.00 52.51  ? 451 HOH C O   1 
HETATM 8340 O O   . HOH PA 8 .   ? 36.352 -17.911 76.078  1.00 36.26  ? 452 HOH C O   1 
HETATM 8341 O O   . HOH PA 8 .   ? 30.141 -16.993 91.674  1.00 55.91  ? 453 HOH C O   1 
HETATM 8342 O O   . HOH PA 8 .   ? 33.669 -32.993 69.764  1.00 51.21  ? 454 HOH C O   1 
HETATM 8343 O O   . HOH PA 8 .   ? 33.702 -33.743 63.827  1.00 55.19  ? 455 HOH C O   1 
HETATM 8344 O O   . HOH PA 8 .   ? 38.465 -22.590 87.490  1.00 42.90  ? 456 HOH C O   1 
HETATM 8345 O O   . HOH PA 8 .   ? 5.110  -36.712 81.299  1.00 73.79  ? 457 HOH C O   1 
HETATM 8346 O O   . HOH PA 8 .   ? 23.384 -22.360 99.408  1.00 36.37  ? 458 HOH C O   1 
HETATM 8347 O O   . HOH PA 8 .   ? 27.798 -39.718 72.799  1.00 46.41  ? 459 HOH C O   1 
HETATM 8348 O O   . HOH PA 8 .   ? 30.817 -18.936 76.136  1.00 40.59  ? 460 HOH C O   1 
HETATM 8349 O O   . HOH PA 8 .   ? 21.107 -29.746 69.943  1.00 43.98  ? 461 HOH C O   1 
HETATM 8350 O O   . HOH PA 8 .   ? 35.965 -50.798 77.764  1.00 51.15  ? 462 HOH C O   1 
HETATM 8351 O O   . HOH PA 8 .   ? 7.900  -19.527 70.703  1.00 53.27  ? 463 HOH C O   1 
HETATM 8352 O O   . HOH PA 8 .   ? 34.556 -14.340 72.453  1.00 58.00  ? 464 HOH C O   1 
HETATM 8353 O O   . HOH PA 8 .   ? 28.002 -20.121 91.318  1.00 49.35  ? 465 HOH C O   1 
HETATM 8354 O O   . HOH PA 8 .   ? 28.905 -41.542 91.347  1.00 49.15  ? 466 HOH C O   1 
HETATM 8355 O O   . HOH PA 8 .   ? 31.016 -25.154 86.932  1.00 45.40  ? 467 HOH C O   1 
HETATM 8356 O O   . HOH PA 8 .   ? 13.746 -20.310 91.913  1.00 40.92  ? 468 HOH C O   1 
HETATM 8357 O O   . HOH PA 8 .   ? 33.546 -20.555 107.822 1.00 40.43  ? 469 HOH C O   1 
HETATM 8358 O O   . HOH PA 8 .   ? 38.188 -23.627 67.129  1.00 56.07  ? 470 HOH C O   1 
HETATM 8359 O O   . HOH PA 8 .   ? 25.354 -22.208 77.662  1.00 31.31  ? 471 HOH C O   1 
HETATM 8360 O O   . HOH PA 8 .   ? 39.484 -29.880 103.213 1.00 51.77  ? 472 HOH C O   1 
HETATM 8361 O O   . HOH PA 8 .   ? 9.715  -31.247 89.400  1.00 47.29  ? 473 HOH C O   1 
HETATM 8362 O O   . HOH PA 8 .   ? 5.081  -36.432 72.145  1.00 45.88  ? 474 HOH C O   1 
HETATM 8363 O O   . HOH PA 8 .   ? 21.565 -22.424 93.927  1.00 32.83  ? 475 HOH C O   1 
HETATM 8364 O O   . HOH PA 8 .   ? 31.140 -33.553 69.299  1.00 39.49  ? 476 HOH C O   1 
HETATM 8365 O O   . HOH PA 8 .   ? 4.764  -35.938 81.610  1.00 69.87  ? 477 HOH C O   1 
HETATM 8366 O O   . HOH PA 8 .   ? 40.894 -25.536 75.519  1.00 34.92  ? 478 HOH C O   1 
HETATM 8367 O O   . HOH PA 8 .   ? 28.905 -29.822 104.889 1.00 54.35  ? 479 HOH C O   1 
HETATM 8368 O O   . HOH PA 8 .   ? 40.322 -15.165 100.381 1.00 59.10  ? 480 HOH C O   1 
HETATM 8369 O O   . HOH PA 8 .   ? 33.182 -28.316 61.611  1.00 57.88  ? 481 HOH C O   1 
HETATM 8370 O O   . HOH PA 8 .   ? 22.734 -42.610 77.198  1.00 46.23  ? 482 HOH C O   1 
HETATM 8371 O O   . HOH PA 8 .   ? 11.303 -19.816 66.987  1.00 41.96  ? 483 HOH C O   1 
HETATM 8372 O O   . HOH PA 8 .   ? 25.269 -13.478 81.954  1.00 58.25  ? 484 HOH C O   1 
HETATM 8373 O O   . HOH PA 8 .   ? 24.677 -31.226 92.532  1.00 31.63  ? 485 HOH C O   1 
HETATM 8374 O O   . HOH PA 8 .   ? 7.405  -32.614 87.276  1.00 48.09  ? 486 HOH C O   1 
HETATM 8375 O O   . HOH PA 8 .   ? 9.160  -29.627 71.495  1.00 39.16  ? 487 HOH C O   1 
HETATM 8376 O O   . HOH PA 8 .   ? 37.906 -37.754 89.568  1.00 64.48  ? 488 HOH C O   1 
HETATM 8377 O O   . HOH PA 8 .   ? 37.498 -37.501 96.653  1.00 58.46  ? 489 HOH C O   1 
HETATM 8378 O O   . HOH PA 8 .   ? 18.526 -39.821 93.196  1.00 41.75  ? 490 HOH C O   1 
HETATM 8379 O O   . HOH PA 8 .   ? 18.763 -42.408 78.037  1.00 57.85  ? 491 HOH C O   1 
HETATM 8380 O O   . HOH PA 8 .   ? 21.043 -39.325 68.739  1.00 47.31  ? 492 HOH C O   1 
HETATM 8381 O O   . HOH PA 8 .   ? 23.982 -42.376 94.181  1.00 48.00  ? 493 HOH C O   1 
HETATM 8382 O O   . HOH PA 8 .   ? 11.617 -9.713  69.908  1.00 56.71  ? 494 HOH C O   1 
HETATM 8383 O O   . HOH PA 8 .   ? 7.605  -22.139 69.781  1.00 58.34  ? 495 HOH C O   1 
HETATM 8384 O O   . HOH PA 8 .   ? 45.396 -22.444 88.280  1.00 60.20  ? 496 HOH C O   1 
HETATM 8385 O O   . HOH PA 8 .   ? 22.492 -30.746 103.594 1.00 51.78  ? 497 HOH C O   1 
HETATM 8386 O O   . HOH PA 8 .   ? 40.177 -38.341 76.463  1.00 61.49  ? 498 HOH C O   1 
HETATM 8387 O O   . HOH PA 8 .   ? 44.016 -25.928 89.145  1.00 60.32  ? 499 HOH C O   1 
HETATM 8388 O O   . HOH PA 8 .   ? 39.308 -22.709 109.898 1.00 58.24  ? 500 HOH C O   1 
HETATM 8389 O O   . HOH PA 8 .   ? 12.607 -44.399 73.633  1.00 47.23  ? 501 HOH C O   1 
HETATM 8390 O O   . HOH PA 8 .   ? 19.813 -41.450 91.408  1.00 46.79  ? 502 HOH C O   1 
HETATM 8391 O O   . HOH PA 8 .   ? 28.640 -19.251 94.425  1.00 54.62  ? 503 HOH C O   1 
HETATM 8392 O O   . HOH PA 8 .   ? 29.659 -35.404 100.705 1.00 37.86  ? 504 HOH C O   1 
HETATM 8393 O O   . HOH PA 8 .   ? 13.406 -13.888 70.271  1.00 42.50  ? 505 HOH C O   1 
HETATM 8394 O O   . HOH PA 8 .   ? 9.771  -40.471 76.854  1.00 38.11  ? 506 HOH C O   1 
HETATM 8395 O O   . HOH PA 8 .   ? 42.804 -19.039 97.934  1.00 55.37  ? 507 HOH C O   1 
HETATM 8396 O O   . HOH PA 8 .   ? 34.280 -47.215 79.605  1.00 62.63  ? 508 HOH C O   1 
HETATM 8397 O O   . HOH PA 8 .   ? 33.413 -25.188 61.470  1.00 53.54  ? 509 HOH C O   1 
HETATM 8398 O O   . HOH PA 8 .   ? 22.602 -43.481 90.236  1.00 48.09  ? 510 HOH C O   1 
HETATM 8399 O O   . HOH PA 8 .   ? 31.999 -12.801 69.673  1.00 57.20  ? 511 HOH C O   1 
HETATM 8400 O O   . HOH PA 8 .   ? 30.087 -40.362 70.845  1.00 48.17  ? 512 HOH C O   1 
HETATM 8401 O O   . HOH PA 8 .   ? 17.735 -18.948 86.209  1.00 56.52  ? 513 HOH C O   1 
HETATM 8402 O O   . HOH PA 8 .   ? 36.748 -37.850 92.941  1.00 51.79  ? 514 HOH C O   1 
HETATM 8403 O O   . HOH PA 8 .   ? 34.932 -27.501 112.408 1.00 53.23  ? 515 HOH C O   1 
HETATM 8404 O O   . HOH PA 8 .   ? 33.701 -22.247 63.853  1.00 59.97  ? 516 HOH C O   1 
HETATM 8405 O O   . HOH PA 8 .   ? 42.955 -24.553 104.354 1.00 50.89  ? 517 HOH C O   1 
HETATM 8406 O O   . HOH PA 8 .   ? 7.005  -38.605 89.094  1.00 52.12  ? 518 HOH C O   1 
HETATM 8407 O O   . HOH PA 8 .   ? 2.957  -23.939 84.092  1.00 46.99  ? 519 HOH C O   1 
HETATM 8408 O O   . HOH PA 8 .   ? 27.614 -8.556  74.830  1.00 55.94  ? 520 HOH C O   1 
HETATM 8409 O O   . HOH PA 8 .   ? 6.429  -15.907 71.075  1.00 56.13  ? 521 HOH C O   1 
HETATM 8410 O O   . HOH PA 8 .   ? 27.466 -50.191 85.599  1.00 68.02  ? 522 HOH C O   1 
HETATM 8411 O O   . HOH PA 8 .   ? 43.975 -21.275 104.337 1.00 54.44  ? 523 HOH C O   1 
HETATM 8412 O O   . HOH PA 8 .   ? 46.567 -22.301 84.167  1.00 58.44  ? 524 HOH C O   1 
HETATM 8413 O O   . HOH PA 8 .   ? 6.199  -39.928 86.325  1.00 45.40  ? 525 HOH C O   1 
HETATM 8414 O O   . HOH PA 8 .   ? 10.963 -31.220 67.657  1.00 46.07  ? 526 HOH C O   1 
HETATM 8415 O O   . HOH PA 8 .   ? 30.969 -35.184 66.659  1.00 61.24  ? 527 HOH C O   1 
HETATM 8416 O O   . HOH PA 8 .   ? 42.228 -24.001 90.674  1.00 57.59  ? 528 HOH C O   1 
HETATM 8417 O O   . HOH PA 8 .   ? 20.264 -39.965 96.317  1.00 61.04  ? 529 HOH C O   1 
HETATM 8418 O O   . HOH PA 8 .   ? 14.288 -27.699 65.917  1.00 46.83  ? 530 HOH C O   1 
HETATM 8419 O O   . HOH PA 8 .   ? 8.685  -12.074 72.028  1.00 59.63  ? 531 HOH C O   1 
HETATM 8420 O O   . HOH PA 8 .   ? 28.239 -33.828 102.480 1.00 45.26  ? 532 HOH C O   1 
HETATM 8421 O O   . HOH PA 8 .   ? 8.499  -16.620 68.533  1.00 61.46  ? 533 HOH C O   1 
HETATM 8422 O O   . HOH PA 8 .   ? 20.240 -43.511 94.206  1.00 60.94  ? 534 HOH C O   1 
HETATM 8423 O O   . HOH PA 8 .   ? 21.682 -42.087 96.004  1.00 47.91  ? 535 HOH C O   1 
HETATM 8424 O O   . HOH PA 8 .   ? 23.851 -15.318 80.341  1.00 53.12  ? 536 HOH C O   1 
HETATM 8425 O O   . HOH PA 8 .   ? 20.942 -43.481 78.585  1.00 58.58  ? 537 HOH C O   1 
HETATM 8426 O O   . HOH PA 8 .   ? 28.545 -19.298 97.886  1.00 52.93  ? 538 HOH C O   1 
HETATM 8427 O O   . HOH PA 8 .   ? 6.086  -13.384 70.995  1.00 69.62  ? 539 HOH C O   1 
HETATM 8428 O O   . HOH PA 8 .   ? 11.467 -17.274 67.594  1.00 54.90  ? 540 HOH C O   1 
HETATM 8429 O O   . HOH PA 8 .   ? 43.035 -26.678 73.782  1.00 58.42  ? 541 HOH C O   1 
HETATM 8430 O O   . HOH QA 8 .   ? 16.532 5.312   73.839  1.00 45.81  ? 401 HOH D O   1 
HETATM 8431 O O   . HOH QA 8 .   ? 15.972 11.984  70.436  1.00 44.44  ? 402 HOH D O   1 
HETATM 8432 O O   . HOH QA 8 .   ? 11.602 10.613  62.529  1.00 38.95  ? 403 HOH D O   1 
HETATM 8433 O O   . HOH QA 8 .   ? 11.017 19.821  57.795  1.00 34.24  ? 404 HOH D O   1 
HETATM 8434 O O   . HOH QA 8 .   ? 35.193 -9.360  70.981  1.00 51.21  ? 405 HOH D O   1 
HETATM 8435 O O   . HOH QA 8 .   ? 18.658 30.069  56.432  1.00 46.12  ? 406 HOH D O   1 
HETATM 8436 O O   . HOH QA 8 .   ? 13.175 0.651   49.319  1.00 51.67  ? 407 HOH D O   1 
HETATM 8437 O O   . HOH QA 8 .   ? 14.411 -10.875 68.823  1.00 59.91  ? 408 HOH D O   1 
HETATM 8438 O O   . HOH QA 8 .   ? 18.238 25.064  68.197  1.00 41.47  ? 409 HOH D O   1 
HETATM 8439 O O   . HOH QA 8 .   ? 39.811 15.868  59.434  1.00 51.03  ? 410 HOH D O   1 
HETATM 8440 O O   . HOH QA 8 .   ? 16.107 20.134  51.452  1.00 34.25  ? 411 HOH D O   1 
HETATM 8441 O O   . HOH QA 8 .   ? 25.905 9.881   46.054  1.00 36.37  ? 412 HOH D O   1 
HETATM 8442 O O   . HOH QA 8 .   ? 31.604 -4.158  55.189  1.00 30.84  ? 413 HOH D O   1 
HETATM 8443 O O   . HOH QA 8 .   ? 15.322 8.372   74.352  1.00 47.82  ? 414 HOH D O   1 
HETATM 8444 O O   . HOH QA 8 .   ? 30.504 -11.625 62.195  1.00 47.81  ? 415 HOH D O   1 
HETATM 8445 O O   . HOH QA 8 .   ? 39.918 2.726   61.020  1.00 37.85  ? 416 HOH D O   1 
HETATM 8446 O O   . HOH QA 8 .   ? 4.187  27.014  69.745  1.00 39.30  ? 417 HOH D O   1 
HETATM 8447 O O   . HOH QA 8 .   ? 44.523 -1.478  55.942  1.00 33.95  ? 418 HOH D O   1 
HETATM 8448 O O   . HOH QA 8 .   ? 32.823 -8.036  64.522  1.00 43.92  ? 419 HOH D O   1 
HETATM 8449 O O   . HOH QA 8 .   ? 10.881 30.731  66.353  1.00 33.75  ? 420 HOH D O   1 
HETATM 8450 O O   . HOH QA 8 .   ? 35.858 21.428  56.100  1.00 40.46  ? 421 HOH D O   1 
HETATM 8451 O O   . HOH QA 8 .   ? 19.639 6.650   45.160  1.00 35.45  ? 422 HOH D O   1 
HETATM 8452 O O   . HOH QA 8 .   ? 21.856 25.805  62.323  1.00 42.26  ? 423 HOH D O   1 
HETATM 8453 O O   . HOH QA 8 .   ? 29.763 11.017  44.016  1.00 60.06  ? 424 HOH D O   1 
HETATM 8454 O O   . HOH QA 8 .   ? 36.631 20.375  60.604  1.00 42.09  ? 425 HOH D O   1 
HETATM 8455 O O   . HOH QA 8 .   ? 36.830 -0.043  52.007  1.00 33.34  ? 426 HOH D O   1 
HETATM 8456 O O   . HOH QA 8 .   ? 32.171 22.751  46.561  1.00 53.71  ? 427 HOH D O   1 
HETATM 8457 O O   . HOH QA 8 .   ? 26.966 23.205  65.975  1.00 28.59  ? 428 HOH D O   1 
HETATM 8458 O O   . HOH QA 8 .   ? 28.966 14.807  70.353  1.00 48.41  ? 429 HOH D O   1 
HETATM 8459 O O   . HOH QA 8 .   ? 13.769 26.321  60.358  1.00 36.40  ? 430 HOH D O   1 
HETATM 8460 O O   . HOH QA 8 .   ? 15.401 -11.548 57.560  1.00 60.94  ? 431 HOH D O   1 
HETATM 8461 O O   . HOH QA 8 .   ? 21.009 19.238  63.678  1.00 30.14  ? 432 HOH D O   1 
HETATM 8462 O O   . HOH QA 8 .   ? 6.502  26.854  85.360  1.00 40.22  ? 433 HOH D O   1 
HETATM 8463 O O   . HOH QA 8 .   ? 5.598  13.247  54.320  1.00 48.44  ? 434 HOH D O   1 
HETATM 8464 O O   . HOH QA 8 .   ? 17.723 17.852  51.995  1.00 30.05  ? 435 HOH D O   1 
HETATM 8465 O O   . HOH QA 8 .   ? 23.527 9.076   56.239  1.00 30.80  ? 436 HOH D O   1 
HETATM 8466 O O   . HOH QA 8 .   ? 6.693  15.462  74.766  1.00 52.80  ? 437 HOH D O   1 
HETATM 8467 O O   . HOH QA 8 .   ? 11.276 21.975  73.781  1.00 43.23  ? 438 HOH D O   1 
HETATM 8468 O O   . HOH QA 8 .   ? 19.719 -5.931  72.601  1.00 41.96  ? 439 HOH D O   1 
HETATM 8469 O O   . HOH QA 8 .   ? 20.239 14.277  42.344  1.00 42.44  ? 440 HOH D O   1 
HETATM 8470 O O   . HOH QA 8 .   ? 39.994 20.513  53.970  1.00 47.40  ? 441 HOH D O   1 
HETATM 8471 O O   . HOH QA 8 .   ? 0.585  20.402  68.385  1.00 52.35  ? 442 HOH D O   1 
HETATM 8472 O O   . HOH QA 8 .   ? 13.986 -4.434  73.714  1.00 51.39  ? 443 HOH D O   1 
HETATM 8473 O O   . HOH QA 8 .   ? 9.106  0.042   67.803  1.00 46.45  ? 444 HOH D O   1 
HETATM 8474 O O   . HOH QA 8 .   ? 7.543  29.340  67.817  1.00 45.92  ? 445 HOH D O   1 
HETATM 8475 O O   . HOH QA 8 .   ? 10.356 12.432  70.372  1.00 41.30  ? 446 HOH D O   1 
HETATM 8476 O O   . HOH QA 8 .   ? 7.102  28.706  74.421  1.00 40.24  ? 447 HOH D O   1 
HETATM 8477 O O   . HOH QA 8 .   ? 6.493  13.306  67.686  1.00 46.41  ? 448 HOH D O   1 
HETATM 8478 O O   . HOH QA 8 .   ? 13.878 -8.533  49.519  1.00 49.75  ? 449 HOH D O   1 
HETATM 8479 O O   . HOH QA 8 .   ? 15.955 -0.137  64.766  1.00 37.25  ? 450 HOH D O   1 
HETATM 8480 O O   . HOH QA 8 .   ? 15.928 12.427  64.076  1.00 40.27  ? 451 HOH D O   1 
HETATM 8481 O O   . HOH QA 8 .   ? 17.423 4.083   53.965  1.00 34.58  ? 452 HOH D O   1 
HETATM 8482 O O   . HOH QA 8 .   ? 26.020 -0.643  52.504  1.00 35.07  ? 453 HOH D O   1 
HETATM 8483 O O   . HOH QA 8 .   ? 6.360  9.950   54.268  1.00 42.02  ? 454 HOH D O   1 
HETATM 8484 O O   . HOH QA 8 .   ? 30.701 9.227   32.335  1.00 43.76  ? 455 HOH D O   1 
HETATM 8485 O O   . HOH QA 8 .   ? 24.567 5.123   70.253  1.00 54.65  ? 456 HOH D O   1 
HETATM 8486 O O   . HOH QA 8 .   ? 23.387 22.349  72.371  1.00 38.58  ? 457 HOH D O   1 
HETATM 8487 O O   . HOH QA 8 .   ? 21.607 2.618   62.804  1.00 28.36  ? 458 HOH D O   1 
HETATM 8488 O O   . HOH QA 8 .   ? 8.399  11.889  66.367  1.00 44.69  ? 459 HOH D O   1 
HETATM 8489 O O   . HOH QA 8 .   ? 1.382  12.030  66.753  1.00 49.86  ? 460 HOH D O   1 
HETATM 8490 O O   . HOH QA 8 .   ? 20.761 4.513   61.023  1.00 29.74  ? 461 HOH D O   1 
HETATM 8491 O O   . HOH QA 8 .   ? 7.001  33.519  73.530  1.00 40.35  ? 462 HOH D O   1 
HETATM 8492 O O   . HOH QA 8 .   ? 10.082 35.282  71.484  1.00 55.39  ? 463 HOH D O   1 
HETATM 8493 O O   . HOH QA 8 .   ? 26.828 2.843   43.598  1.00 38.80  ? 464 HOH D O   1 
HETATM 8494 O O   . HOH QA 8 .   ? 19.412 -0.536  69.894  1.00 44.83  ? 465 HOH D O   1 
HETATM 8495 O O   . HOH QA 8 .   ? 45.056 7.784   57.752  1.00 43.11  ? 466 HOH D O   1 
HETATM 8496 O O   . HOH QA 8 .   ? 33.669 -4.260  48.534  1.00 44.53  ? 467 HOH D O   1 
HETATM 8497 O O   . HOH QA 8 .   ? 4.738  2.859   67.576  1.00 47.51  ? 468 HOH D O   1 
HETATM 8498 O O   . HOH QA 8 .   ? 34.557 9.132   41.457  1.00 46.43  ? 469 HOH D O   1 
HETATM 8499 O O   . HOH QA 8 .   ? 33.544 20.494  64.088  1.00 38.20  ? 470 HOH D O   1 
HETATM 8500 O O   . HOH QA 8 .   ? 21.692 13.878  69.183  1.00 39.97  ? 471 HOH D O   1 
HETATM 8501 O O   . HOH QA 8 .   ? 27.931 13.224  41.071  1.00 59.04  ? 472 HOH D O   1 
HETATM 8502 O O   . HOH QA 8 .   ? 25.265 17.344  69.891  1.00 31.39  ? 473 HOH D O   1 
HETATM 8503 O O   . HOH QA 8 .   ? 42.966 9.460   52.293  1.00 52.04  ? 474 HOH D O   1 
HETATM 8504 O O   . HOH QA 8 .   ? 9.094  -6.890  60.856  1.00 45.47  ? 475 HOH D O   1 
HETATM 8505 O O   . HOH QA 8 .   ? 22.442 20.071  61.464  1.00 33.58  ? 476 HOH D O   1 
HETATM 8506 O O   . HOH QA 8 .   ? 39.440 -4.285  59.516  1.00 61.24  ? 477 HOH D O   1 
HETATM 8507 O O   . HOH QA 8 .   ? 15.003 -8.020  67.009  1.00 42.12  ? 478 HOH D O   1 
HETATM 8508 O O   . HOH QA 8 .   ? 3.213  25.979  75.682  1.00 46.38  ? 479 HOH D O   1 
HETATM 8509 O O   . HOH QA 8 .   ? 10.047 23.321  55.695  1.00 44.76  ? 480 HOH D O   1 
HETATM 8510 O O   . HOH QA 8 .   ? 27.685 23.551  51.810  1.00 40.74  ? 481 HOH D O   1 
HETATM 8511 O O   . HOH QA 8 .   ? 17.940 27.426  69.550  1.00 43.75  ? 482 HOH D O   1 
HETATM 8512 O O   . HOH QA 8 .   ? 24.717 11.742  44.483  1.00 40.82  ? 483 HOH D O   1 
HETATM 8513 O O   . HOH QA 8 .   ? 25.987 25.983  59.124  1.00 52.48  ? 484 HOH D O   1 
HETATM 8514 O O   . HOH QA 8 .   ? 14.134 11.338  66.954  1.00 57.79  ? 485 HOH D O   1 
HETATM 8515 O O   . HOH QA 8 .   ? 38.783 0.423   53.952  1.00 35.52  ? 486 HOH D O   1 
HETATM 8516 O O   . HOH QA 8 .   ? 28.796 24.663  54.248  1.00 38.42  ? 487 HOH D O   1 
HETATM 8517 O O   . HOH QA 8 .   ? 25.314 24.007  49.919  1.00 40.15  ? 488 HOH D O   1 
HETATM 8518 O O   . HOH QA 8 .   ? 2.473  15.116  68.658  1.00 44.14  ? 489 HOH D O   1 
HETATM 8519 O O   . HOH QA 8 .   ? 41.009 12.351  59.911  1.00 40.37  ? 490 HOH D O   1 
HETATM 8520 O O   . HOH QA 8 .   ? 12.611 13.142  68.478  1.00 49.91  ? 491 HOH D O   1 
HETATM 8521 O O   . HOH QA 8 .   ? 3.603  9.904   52.149  1.00 59.09  ? 492 HOH D O   1 
HETATM 8522 O O   . HOH QA 8 .   ? 33.321 14.654  71.015  1.00 44.18  ? 493 HOH D O   1 
HETATM 8523 O O   . HOH QA 8 .   ? 10.860 19.886  54.670  1.00 45.99  ? 494 HOH D O   1 
HETATM 8524 O O   . HOH QA 8 .   ? 24.585 -7.265  41.732  1.00 49.42  ? 495 HOH D O   1 
HETATM 8525 O O   . HOH QA 8 .   ? 9.979  28.914  62.552  1.00 39.72  ? 496 HOH D O   1 
HETATM 8526 O O   . HOH QA 8 .   ? 3.659  20.259  57.938  1.00 41.69  ? 497 HOH D O   1 
HETATM 8527 O O   . HOH QA 8 .   ? 8.830  26.270  57.123  1.00 45.08  ? 498 HOH D O   1 
HETATM 8528 O O   . HOH QA 8 .   ? 24.414 29.808  66.367  1.00 55.88  ? 499 HOH D O   1 
HETATM 8529 O O   . HOH QA 8 .   ? 37.467 17.788  59.826  1.00 45.03  ? 500 HOH D O   1 
HETATM 8530 O O   . HOH QA 8 .   ? 14.752 25.059  55.265  1.00 64.23  ? 501 HOH D O   1 
HETATM 8531 O O   . HOH QA 8 .   ? 33.682 -7.667  67.012  1.00 34.38  ? 502 HOH D O   1 
HETATM 8532 O O   . HOH QA 8 .   ? 43.006 -1.289  53.499  1.00 50.61  ? 503 HOH D O   1 
HETATM 8533 O O   . HOH QA 8 .   ? 10.874 27.392  60.823  1.00 47.51  ? 504 HOH D O   1 
HETATM 8534 O O   . HOH QA 8 .   ? 18.936 24.041  51.753  1.00 47.55  ? 505 HOH D O   1 
HETATM 8535 O O   . HOH QA 8 .   ? 18.955 13.803  70.711  1.00 47.44  ? 506 HOH D O   1 
HETATM 8536 O O   . HOH QA 8 .   ? 36.017 -7.947  60.255  1.00 41.48  ? 507 HOH D O   1 
HETATM 8537 O O   . HOH QA 8 .   ? 3.753  7.576   58.129  1.00 58.95  ? 508 HOH D O   1 
HETATM 8538 O O   . HOH QA 8 .   ? 10.516 21.155  45.685  1.00 58.39  ? 509 HOH D O   1 
HETATM 8539 O O   . HOH QA 8 .   ? 40.297 -6.252  66.016  1.00 54.92  ? 510 HOH D O   1 
HETATM 8540 O O   . HOH QA 8 .   ? 22.047 20.812  42.205  1.00 54.89  ? 511 HOH D O   1 
HETATM 8541 O O   . HOH QA 8 .   ? 3.512  2.517   62.880  1.00 55.54  ? 512 HOH D O   1 
HETATM 8542 O O   . HOH QA 8 .   ? 17.401 4.864   43.506  1.00 56.00  ? 513 HOH D O   1 
HETATM 8543 O O   . HOH QA 8 .   ? 4.062  18.532  74.936  1.00 62.78  ? 514 HOH D O   1 
HETATM 8544 O O   . HOH QA 8 .   ? 27.885 17.205  70.459  1.00 51.29  ? 515 HOH D O   1 
HETATM 8545 O O   . HOH QA 8 .   ? 35.001 12.939  74.183  1.00 61.00  ? 516 HOH D O   1 
HETATM 8546 O O   . HOH QA 8 .   ? 41.297 18.036  51.722  1.00 53.09  ? 517 HOH D O   1 
HETATM 8547 O O   . HOH QA 8 .   ? 3.399  2.656   56.140  1.00 51.49  ? 518 HOH D O   1 
HETATM 8548 O O   . HOH QA 8 .   ? 8.804  -4.813  64.236  1.00 56.98  ? 519 HOH D O   1 
HETATM 8549 O O   . HOH QA 8 .   ? 42.920 -5.530  64.437  1.00 58.77  ? 520 HOH D O   1 
HETATM 8550 O O   . HOH QA 8 .   ? 36.921 -2.404  50.725  1.00 37.26  ? 521 HOH D O   1 
HETATM 8551 O O   . HOH QA 8 .   ? 3.980  9.433   55.519  1.00 51.74  ? 522 HOH D O   1 
HETATM 8552 O O   . HOH QA 8 .   ? 25.075 26.544  61.807  1.00 59.53  ? 523 HOH D O   1 
HETATM 8553 O O   . HOH QA 8 .   ? 15.640 -10.385 48.300  1.00 61.15  ? 524 HOH D O   1 
HETATM 8554 O O   . HOH QA 8 .   ? 23.933 14.711  70.362  1.00 46.61  ? 525 HOH D O   1 
HETATM 8555 O O   . HOH QA 8 .   ? 37.486 -8.714  64.662  1.00 61.25  ? 526 HOH D O   1 
HETATM 8556 O O   . HOH QA 8 .   ? 35.159 -8.879  62.642  1.00 50.36  ? 527 HOH D O   1 
HETATM 8557 O O   . HOH QA 8 .   ? 40.273 -1.825  53.483  1.00 36.17  ? 528 HOH D O   1 
HETATM 8558 O O   . HOH QA 8 .   ? 36.531 -8.892  67.510  1.00 63.38  ? 529 HOH D O   1 
HETATM 8559 O O   . HOH QA 8 .   ? 12.740 -5.994  66.821  1.00 56.34  ? 530 HOH D O   1 
HETATM 8560 O O   . HOH QA 8 .   ? 17.728 13.345  41.180  1.00 59.65  ? 531 HOH D O   1 
# 
