data_9DRK
# 
_entry.id   9DRK 
# 
_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   9DRK         pdb_00009drk 10.2210/pdb9drk/pdb 
WWPDB D_1000288233 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-09 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DRK 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              don.ronning@unmc.edu 
_pdbx_contact_author.name_first         Donald 
_pdbx_contact_author.name_last          Ronning 
_pdbx_contact_author.name_mi            R 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2583-8849 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'McCue, W.M.'      1 ?                   
'Jayasinghe, Y.P.' 2 0000-0002-9313-8759 
'Aldrich, C.C.'    3 ?                   
'Ronning, D.R.'    4 0000-0003-2583-8849 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                3065 
_citation.page_last                 3087 
_citation.title                     'Metabolically Stable Adenylation Inhibitors of Biotin Protein Ligase as Antibacterial Agents.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02299 
_citation.pdbx_database_id_PubMed   39823202 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, Q.'          1  ?                   
primary 'Engelhart, C.A.'  2  ?                   
primary 'Wallach, J.B.'    3  ?                   
primary 'Tiwari, D.'       4  ?                   
primary 'Ge, P.'           5  0000-0002-2289-5373 
primary 'Manna, A.'        6  ?                   
primary 'Panda, S.'        7  0000-0003-3077-0690 
primary 'McCue, W.M.'      8  ?                   
primary 'Wong, T.Y.'       9  ?                   
primary 'Sharma, S.'       10 ?                   
primary 'Jayasinghe, Y.P.' 11 0000-0002-9313-8759 
primary 'Fuller, J.'       12 0000-0001-7218-2745 
primary 'Ronning, D.R.'    13 0000-0003-2583-8849 
primary 'Bockman, M.R.'    14 ?                   
primary 'Cheung, A.'       15 ?                   
primary 'Dartois, V.'      16 0000-0001-9470-5009 
primary 'Zimmerman, M.D.'  17 ?                   
primary 'Schnappinger, D.' 18 ?                   
primary 'Aldrich, C.C.'    19 0000-0001-9261-594X 
# 
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     man 'Biotin--[acetyl-CoA-carboxylase] ligase'                                                                 
27995.830 2  6.3.4.15 ? ? ? 
2 non-polymer syn "5'-deoxy-5'-({5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl}sulfamamido)adenosine" 
557.647   2  ?        ? ? ? 
3 water       nat water                                                                                                     18.015 
72 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Biotin--[biotin carboxyl-carrier protein] ligase,Biotin--protein ligase,BPL,Biotin-[acetyl-CoA carboxylase] synthetase' 
# 
_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       
;MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARA
QIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVT
QAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDI
DDQGRLCLDVGGRTVVVSAGDVVHL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARA
QIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVT
QAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDI
DDQGRLCLDVGGRTVVVSAGDVVHL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "5'-deoxy-5'-({5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl}sulfamamido)adenosine" A1BGE 
3 water                                                                                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   ASP n 
1 4   ARG n 
1 5   ASP n 
1 6   ARG n 
1 7   LEU n 
1 8   ARG n 
1 9   PRO n 
1 10  PRO n 
1 11  LEU n 
1 12  ASP n 
1 13  GLU n 
1 14  ARG n 
1 15  SER n 
1 16  LEU n 
1 17  ARG n 
1 18  ASP n 
1 19  GLN n 
1 20  LEU n 
1 21  ILE n 
1 22  GLY n 
1 23  ALA n 
1 24  GLY n 
1 25  SER n 
1 26  GLY n 
1 27  TRP n 
1 28  ARG n 
1 29  GLN n 
1 30  LEU n 
1 31  ASP n 
1 32  VAL n 
1 33  VAL n 
1 34  ALA n 
1 35  GLN n 
1 36  THR n 
1 37  GLY n 
1 38  SER n 
1 39  THR n 
1 40  ASN n 
1 41  ALA n 
1 42  ASP n 
1 43  LEU n 
1 44  LEU n 
1 45  ALA n 
1 46  ARG n 
1 47  ALA n 
1 48  ALA n 
1 49  SER n 
1 50  GLY n 
1 51  ALA n 
1 52  ASP n 
1 53  ILE n 
1 54  ASP n 
1 55  GLY n 
1 56  VAL n 
1 57  VAL n 
1 58  LEU n 
1 59  ILE n 
1 60  ALA n 
1 61  GLU n 
1 62  HIS n 
1 63  GLN n 
1 64  THR n 
1 65  ALA n 
1 66  GLY n 
1 67  ARG n 
1 68  GLY n 
1 69  ARG n 
1 70  HIS n 
1 71  GLY n 
1 72  ARG n 
1 73  GLY n 
1 74  TRP n 
1 75  ALA n 
1 76  ALA n 
1 77  THR n 
1 78  ALA n 
1 79  ARG n 
1 80  ALA n 
1 81  GLN n 
1 82  ILE n 
1 83  ILE n 
1 84  LEU n 
1 85  SER n 
1 86  VAL n 
1 87  GLY n 
1 88  VAL n 
1 89  ARG n 
1 90  VAL n 
1 91  VAL n 
1 92  ASP n 
1 93  VAL n 
1 94  PRO n 
1 95  VAL n 
1 96  GLN n 
1 97  ALA n 
1 98  TRP n 
1 99  GLY n 
1 100 TRP n 
1 101 LEU n 
1 102 SER n 
1 103 LEU n 
1 104 ALA n 
1 105 ALA n 
1 106 GLY n 
1 107 LEU n 
1 108 ALA n 
1 109 VAL n 
1 110 LEU n 
1 111 ASP n 
1 112 SER n 
1 113 VAL n 
1 114 ALA n 
1 115 PRO n 
1 116 LEU n 
1 117 ILE n 
1 118 ALA n 
1 119 VAL n 
1 120 PRO n 
1 121 PRO n 
1 122 ALA n 
1 123 GLU n 
1 124 THR n 
1 125 GLY n 
1 126 LEU n 
1 127 LYS n 
1 128 TRP n 
1 129 PRO n 
1 130 ASN n 
1 131 ASP n 
1 132 VAL n 
1 133 LEU n 
1 134 ALA n 
1 135 ARG n 
1 136 GLY n 
1 137 GLY n 
1 138 LYS n 
1 139 LEU n 
1 140 ALA n 
1 141 GLY n 
1 142 ILE n 
1 143 LEU n 
1 144 ALA n 
1 145 GLU n 
1 146 VAL n 
1 147 ALA n 
1 148 GLN n 
1 149 PRO n 
1 150 PHE n 
1 151 VAL n 
1 152 VAL n 
1 153 LEU n 
1 154 GLY n 
1 155 VAL n 
1 156 GLY n 
1 157 LEU n 
1 158 ASN n 
1 159 VAL n 
1 160 THR n 
1 161 GLN n 
1 162 ALA n 
1 163 PRO n 
1 164 GLU n 
1 165 GLU n 
1 166 VAL n 
1 167 ASP n 
1 168 PRO n 
1 169 ASP n 
1 170 ALA n 
1 171 THR n 
1 172 SER n 
1 173 LEU n 
1 174 LEU n 
1 175 ASP n 
1 176 LEU n 
1 177 GLY n 
1 178 VAL n 
1 179 ALA n 
1 180 ALA n 
1 181 PRO n 
1 182 ASP n 
1 183 ARG n 
1 184 ASN n 
1 185 ARG n 
1 186 ILE n 
1 187 ALA n 
1 188 SER n 
1 189 ARG n 
1 190 LEU n 
1 191 LEU n 
1 192 ARG n 
1 193 GLU n 
1 194 LEU n 
1 195 GLU n 
1 196 ALA n 
1 197 ARG n 
1 198 ILE n 
1 199 ILE n 
1 200 GLN n 
1 201 TRP n 
1 202 ARG n 
1 203 ASN n 
1 204 ALA n 
1 205 ASN n 
1 206 PRO n 
1 207 GLN n 
1 208 LEU n 
1 209 ALA n 
1 210 ALA n 
1 211 ASP n 
1 212 TYR n 
1 213 ARG n 
1 214 ALA n 
1 215 ARG n 
1 216 SER n 
1 217 LEU n 
1 218 THR n 
1 219 ILE n 
1 220 GLY n 
1 221 SER n 
1 222 ARG n 
1 223 VAL n 
1 224 ARG n 
1 225 VAL n 
1 226 GLU n 
1 227 LEU n 
1 228 PRO n 
1 229 GLY n 
1 230 GLY n 
1 231 GLN n 
1 232 ASP n 
1 233 VAL n 
1 234 VAL n 
1 235 GLY n 
1 236 ILE n 
1 237 ALA n 
1 238 ARG n 
1 239 ASP n 
1 240 ILE n 
1 241 ASP n 
1 242 ASP n 
1 243 GLN n 
1 244 GLY n 
1 245 ARG n 
1 246 LEU n 
1 247 CYS n 
1 248 LEU n 
1 249 ASP n 
1 250 VAL n 
1 251 GLY n 
1 252 GLY n 
1 253 ARG n 
1 254 THR n 
1 255 VAL n 
1 256 VAL n 
1 257 VAL n 
1 258 SER n 
1 259 ALA n 
1 260 GLY n 
1 261 ASP n 
1 262 VAL n 
1 263 VAL n 
1 264 HIS n 
1 265 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   265 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'birA, Rv3279c' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Mycobacterium tuberculosis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1773 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1BGE non-polymer         . 
"5'-deoxy-5'-({5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl}sulfamamido)adenosine" ? 'C20 H31 N9 O6 S2' 
557.647 
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 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'       75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER ? 'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  PRO 10  10  10  PRO PRO A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  SER 15  15  15  SER SER A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  TRP 27  27  27  TRP TRP A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  ARG 46  46  46  ARG ARG A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  HIS 62  62  62  HIS HIS A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  HIS 70  70  70  HIS HIS A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  TRP 74  74  74  TRP TRP A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  TRP 98  98  98  TRP TRP A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 TRP 100 100 100 TRP TRP A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ASP 111 111 111 ASP ASP A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 ALA 118 118 ?   ?   ?   A . n 
A 1 119 VAL 119 119 ?   ?   ?   A . n 
A 1 120 PRO 120 120 ?   ?   ?   A . n 
A 1 121 PRO 121 121 ?   ?   ?   A . n 
A 1 122 ALA 122 122 ?   ?   ?   A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 TRP 128 128 128 TRP TRP A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 ASN 130 130 130 ASN ASN A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 GLN 148 148 148 GLN GLN A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 PRO 163 163 163 PRO PRO A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 ALA 180 180 180 ALA ALA A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ASN 184 184 184 ASN ASN A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 ARG 189 189 189 ARG ARG A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 GLU 193 193 193 GLU GLU A . n 
A 1 194 LEU 194 194 194 LEU LEU A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ARG 197 197 197 ARG ARG A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 GLN 200 200 200 GLN GLN A . n 
A 1 201 TRP 201 201 201 TRP TRP A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 GLN 207 207 207 GLN GLN A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 TYR 212 212 212 TYR TYR A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 ARG 224 224 224 ARG ARG A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 GLN 231 231 231 GLN GLN A . n 
A 1 232 ASP 232 232 232 ASP ASP A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 ILE 240 240 240 ILE ILE A . n 
A 1 241 ASP 241 241 241 ASP ASP A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 GLN 243 243 243 GLN GLN A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 CYS 247 247 247 CYS CYS A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ASP 249 249 249 ASP ASP A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 LEU 265 265 265 LEU LEU A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   ASP 3   3   ?   ?   ?   B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   ASP 5   5   5   ASP ASP B . n 
B 1 6   ARG 6   6   6   ARG ARG B . n 
B 1 7   LEU 7   7   7   LEU LEU B . n 
B 1 8   ARG 8   8   8   ARG ARG B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  PRO 10  10  10  PRO PRO B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  ARG 14  14  14  ARG ARG B . n 
B 1 15  SER 15  15  15  SER SER B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  ARG 17  17  17  ARG ARG B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  ILE 21  21  21  ILE ILE B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  TRP 27  27  27  TRP TRP B . n 
B 1 28  ARG 28  28  28  ARG ARG B . n 
B 1 29  GLN 29  29  29  GLN GLN B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  GLN 35  35  35  GLN GLN B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  SER 38  38  38  SER SER B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  ASP 42  42  42  ASP ASP B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  ARG 46  46  46  ARG ARG B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  SER 49  49  49  SER SER B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  ASP 54  54  54  ASP ASP B . n 
B 1 55  GLY 55  55  55  GLY GLY B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLU 61  61  61  GLU GLU B . n 
B 1 62  HIS 62  62  62  HIS HIS B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  GLY 66  66  66  GLY GLY B . n 
B 1 67  ARG 67  67  67  ARG ARG B . n 
B 1 68  GLY 68  68  68  GLY GLY B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  HIS 70  70  70  HIS HIS B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ARG 72  72  72  ARG ARG B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  TRP 74  74  74  TRP TRP B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  THR 77  77  77  THR THR B . n 
B 1 78  ALA 78  78  78  ALA ALA B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  GLN 81  81  81  GLN GLN B . n 
B 1 82  ILE 82  82  82  ILE ILE B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  SER 85  85  85  SER SER B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  GLY 87  87  87  GLY GLY B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  VAL 90  90  90  VAL VAL B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  PRO 94  94  94  PRO PRO B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  GLN 96  96  96  GLN GLN B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  TRP 98  98  98  TRP TRP B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 TRP 100 100 100 TRP TRP B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 ALA 104 104 104 ALA ALA B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 GLY 106 106 106 GLY GLY B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 ASP 111 111 111 ASP ASP B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 PRO 115 115 115 PRO PRO B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 ILE 117 117 117 ILE ILE B . n 
B 1 118 ALA 118 118 118 ALA ALA B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 PRO 120 120 120 PRO PRO B . n 
B 1 121 PRO 121 121 121 PRO PRO B . n 
B 1 122 ALA 122 122 122 ALA ALA B . n 
B 1 123 GLU 123 123 123 GLU GLU B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 GLY 125 125 125 GLY GLY B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LYS 127 127 127 LYS LYS B . n 
B 1 128 TRP 128 128 128 TRP TRP B . n 
B 1 129 PRO 129 129 129 PRO PRO B . n 
B 1 130 ASN 130 130 130 ASN ASN B . n 
B 1 131 ASP 131 131 131 ASP ASP B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ARG 135 135 135 ARG ARG B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 GLY 137 137 137 GLY GLY B . n 
B 1 138 LYS 138 138 138 LYS LYS B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 ILE 142 142 142 ILE ILE B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 ALA 144 144 144 ALA ALA B . n 
B 1 145 GLU 145 145 145 GLU GLU B . n 
B 1 146 VAL 146 146 146 VAL VAL B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 GLN 148 148 148 GLN GLN B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 THR 160 160 160 THR THR B . n 
B 1 161 GLN 161 161 161 GLN GLN B . n 
B 1 162 ALA 162 162 162 ALA ALA B . n 
B 1 163 PRO 163 163 163 PRO PRO B . n 
B 1 164 GLU 164 164 164 GLU GLU B . n 
B 1 165 GLU 165 165 165 GLU GLU B . n 
B 1 166 VAL 166 166 166 VAL VAL B . n 
B 1 167 ASP 167 167 167 ASP ASP B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 ASP 169 169 169 ASP ASP B . n 
B 1 170 ALA 170 170 170 ALA ALA B . n 
B 1 171 THR 171 171 171 THR THR B . n 
B 1 172 SER 172 172 172 SER SER B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 ASP 175 175 175 ASP ASP B . n 
B 1 176 LEU 176 176 176 LEU LEU B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 ALA 179 179 179 ALA ALA B . n 
B 1 180 ALA 180 180 180 ALA ALA B . n 
B 1 181 PRO 181 181 181 PRO PRO B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 ARG 183 183 183 ARG ARG B . n 
B 1 184 ASN 184 184 184 ASN ASN B . n 
B 1 185 ARG 185 185 185 ARG ARG B . n 
B 1 186 ILE 186 186 186 ILE ILE B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 SER 188 188 188 SER SER B . n 
B 1 189 ARG 189 189 189 ARG ARG B . n 
B 1 190 LEU 190 190 190 LEU LEU B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 GLU 193 193 193 GLU GLU B . n 
B 1 194 LEU 194 194 194 LEU LEU B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 ARG 197 197 197 ARG ARG B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 ILE 199 199 199 ILE ILE B . n 
B 1 200 GLN 200 200 200 GLN GLN B . n 
B 1 201 TRP 201 201 201 TRP TRP B . n 
B 1 202 ARG 202 202 202 ARG ARG B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 ASN 205 205 205 ASN ASN B . n 
B 1 206 PRO 206 206 206 PRO PRO B . n 
B 1 207 GLN 207 207 207 GLN GLN B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 ALA 209 209 209 ALA ALA B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ASP 211 211 211 ASP ASP B . n 
B 1 212 TYR 212 212 212 TYR TYR B . n 
B 1 213 ARG 213 213 213 ARG ARG B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 ARG 215 215 215 ARG ARG B . n 
B 1 216 SER 216 216 216 SER SER B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 THR 218 218 218 THR THR B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 GLY 220 220 220 GLY GLY B . n 
B 1 221 SER 221 221 221 SER SER B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 VAL 223 223 223 VAL VAL B . n 
B 1 224 ARG 224 224 224 ARG ARG B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 PRO 228 228 228 PRO PRO B . n 
B 1 229 GLY 229 229 229 GLY GLY B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 GLN 231 231 231 GLN GLN B . n 
B 1 232 ASP 232 232 232 ASP ASP B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 VAL 234 234 234 VAL VAL B . n 
B 1 235 GLY 235 235 235 GLY GLY B . n 
B 1 236 ILE 236 236 236 ILE ILE B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 ARG 238 238 238 ARG ARG B . n 
B 1 239 ASP 239 239 239 ASP ASP B . n 
B 1 240 ILE 240 240 240 ILE ILE B . n 
B 1 241 ASP 241 241 241 ASP ASP B . n 
B 1 242 ASP 242 242 242 ASP ASP B . n 
B 1 243 GLN 243 243 243 GLN GLN B . n 
B 1 244 GLY 244 244 244 GLY GLY B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 LEU 246 246 246 LEU LEU B . n 
B 1 247 CYS 247 247 247 CYS CYS B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 ASP 249 249 249 ASP ASP B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 GLY 252 252 252 GLY GLY B . n 
B 1 253 ARG 253 253 253 ARG ARG B . n 
B 1 254 THR 254 254 254 THR THR B . n 
B 1 255 VAL 255 255 255 VAL VAL B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 SER 258 258 258 SER SER B . n 
B 1 259 ALA 259 259 259 ALA ALA B . n 
B 1 260 GLY 260 260 260 GLY GLY B . n 
B 1 261 ASP 261 261 261 ASP ASP B . n 
B 1 262 VAL 262 262 262 VAL VAL B . n 
B 1 263 VAL 263 263 263 VAL VAL B . n 
B 1 264 HIS 264 264 264 HIS HIS B . n 
B 1 265 LEU 265 265 265 LEU LEU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BGE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGE 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BGE 1  301 266 A1BGE BIO A . 
D 2 A1BGE 1  301 266 A1BGE BIO B . 
E 3 HOH   1  401 85  HOH   HOH A . 
E 3 HOH   2  402 77  HOH   HOH A . 
E 3 HOH   3  403 29  HOH   HOH A . 
E 3 HOH   4  404 83  HOH   HOH A . 
E 3 HOH   5  405 33  HOH   HOH A . 
E 3 HOH   6  406 36  HOH   HOH A . 
E 3 HOH   7  407 6   HOH   HOH A . 
E 3 HOH   8  408 72  HOH   HOH A . 
E 3 HOH   9  409 55  HOH   HOH A . 
E 3 HOH   10 410 31  HOH   HOH A . 
E 3 HOH   11 411 67  HOH   HOH A . 
E 3 HOH   12 412 78  HOH   HOH A . 
E 3 HOH   13 413 69  HOH   HOH A . 
E 3 HOH   14 414 13  HOH   HOH A . 
E 3 HOH   15 415 34  HOH   HOH A . 
E 3 HOH   16 416 54  HOH   HOH A . 
E 3 HOH   17 417 60  HOH   HOH A . 
E 3 HOH   18 418 71  HOH   HOH A . 
E 3 HOH   19 419 43  HOH   HOH A . 
E 3 HOH   20 420 86  HOH   HOH A . 
E 3 HOH   21 421 7   HOH   HOH A . 
E 3 HOH   22 422 79  HOH   HOH A . 
E 3 HOH   23 423 8   HOH   HOH A . 
E 3 HOH   24 424 73  HOH   HOH A . 
E 3 HOH   25 425 3   HOH   HOH A . 
E 3 HOH   26 426 52  HOH   HOH A . 
E 3 HOH   27 427 58  HOH   HOH A . 
E 3 HOH   28 428 56  HOH   HOH A . 
E 3 HOH   29 429 40  HOH   HOH A . 
E 3 HOH   30 430 11  HOH   HOH A . 
E 3 HOH   31 431 9   HOH   HOH A . 
E 3 HOH   32 432 35  HOH   HOH A . 
E 3 HOH   33 433 89  HOH   HOH A . 
E 3 HOH   34 434 82  HOH   HOH A . 
E 3 HOH   35 435 64  HOH   HOH A . 
E 3 HOH   36 436 95  HOH   HOH A . 
E 3 HOH   37 437 53  HOH   HOH A . 
E 3 HOH   38 438 49  HOH   HOH A . 
E 3 HOH   39 439 19  HOH   HOH A . 
E 3 HOH   40 440 93  HOH   HOH A . 
E 3 HOH   41 441 17  HOH   HOH A . 
E 3 HOH   42 442 91  HOH   HOH A . 
F 3 HOH   1  401 94  HOH   HOH B . 
F 3 HOH   2  402 48  HOH   HOH B . 
F 3 HOH   3  403 38  HOH   HOH B . 
F 3 HOH   4  404 88  HOH   HOH B . 
F 3 HOH   5  405 61  HOH   HOH B . 
F 3 HOH   6  406 32  HOH   HOH B . 
F 3 HOH   7  407 81  HOH   HOH B . 
F 3 HOH   8  408 44  HOH   HOH B . 
F 3 HOH   9  409 68  HOH   HOH B . 
F 3 HOH   10 410 46  HOH   HOH B . 
F 3 HOH   11 411 92  HOH   HOH B . 
F 3 HOH   12 412 59  HOH   HOH B . 
F 3 HOH   13 413 51  HOH   HOH B . 
F 3 HOH   14 414 30  HOH   HOH B . 
F 3 HOH   15 415 87  HOH   HOH B . 
F 3 HOH   16 416 39  HOH   HOH B . 
F 3 HOH   17 417 75  HOH   HOH B . 
F 3 HOH   18 418 10  HOH   HOH B . 
F 3 HOH   19 419 50  HOH   HOH B . 
F 3 HOH   20 420 12  HOH   HOH B . 
F 3 HOH   21 421 28  HOH   HOH B . 
F 3 HOH   22 422 5   HOH   HOH B . 
F 3 HOH   23 423 45  HOH   HOH B . 
F 3 HOH   24 424 57  HOH   HOH B . 
F 3 HOH   25 425 80  HOH   HOH B . 
F 3 HOH   26 426 70  HOH   HOH B . 
F 3 HOH   27 427 66  HOH   HOH B . 
F 3 HOH   28 428 18  HOH   HOH B . 
F 3 HOH   29 429 37  HOH   HOH B . 
F 3 HOH   30 430 63  HOH   HOH B . 
# 
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 1 A ASP 3   ? CG  ? A ASP 3   CG  
2  1 Y 1 A ASP 3   ? OD1 ? A ASP 3   OD1 
3  1 Y 1 A ASP 3   ? OD2 ? A ASP 3   OD2 
4  1 Y 1 A ARG 14  ? CD  ? A ARG 14  CD  
5  1 Y 1 A ARG 14  ? NE  ? A ARG 14  NE  
6  1 Y 1 A ARG 14  ? CZ  ? A ARG 14  CZ  
7  1 Y 1 A ARG 14  ? NH1 ? A ARG 14  NH1 
8  1 Y 1 A ARG 14  ? NH2 ? A ARG 14  NH2 
9  1 Y 1 A ARG 28  ? CG  ? A ARG 28  CG  
10 1 Y 1 A ARG 28  ? CD  ? A ARG 28  CD  
11 1 Y 1 A ARG 28  ? NE  ? A ARG 28  NE  
12 1 Y 1 A ARG 28  ? CZ  ? A ARG 28  CZ  
13 1 Y 1 A ARG 28  ? NH1 ? A ARG 28  NH1 
14 1 Y 1 A ARG 28  ? NH2 ? A ARG 28  NH2 
15 1 Y 1 A ARG 69  ? CG  ? A ARG 69  CG  
16 1 Y 1 A ARG 69  ? CD  ? A ARG 69  CD  
17 1 Y 1 A ARG 69  ? NE  ? A ARG 69  NE  
18 1 Y 1 A ARG 69  ? CZ  ? A ARG 69  CZ  
19 1 Y 1 A ARG 69  ? NH1 ? A ARG 69  NH1 
20 1 Y 1 A ARG 69  ? NH2 ? A ARG 69  NH2 
21 1 Y 1 A GLN 96  ? CG  ? A GLN 96  CG  
22 1 Y 1 A GLN 96  ? CD  ? A GLN 96  CD  
23 1 Y 1 A GLN 96  ? OE1 ? A GLN 96  OE1 
24 1 Y 1 A GLN 96  ? NE2 ? A GLN 96  NE2 
25 1 Y 1 A ARG 222 ? CG  ? A ARG 222 CG  
26 1 Y 1 A ARG 222 ? CD  ? A ARG 222 CD  
27 1 Y 1 A ARG 222 ? NE  ? A ARG 222 NE  
28 1 Y 1 A ARG 222 ? CZ  ? A ARG 222 CZ  
29 1 Y 1 A ARG 222 ? NH1 ? A ARG 222 NH1 
30 1 Y 1 A ARG 222 ? NH2 ? A ARG 222 NH2 
31 1 Y 1 A ASP 242 ? CG  ? A ASP 242 CG  
32 1 Y 1 A ASP 242 ? OD1 ? A ASP 242 OD1 
33 1 Y 1 A ASP 242 ? OD2 ? A ASP 242 OD2 
34 1 Y 1 B ASP 5   ? CG  ? B ASP 5   CG  
35 1 Y 1 B ASP 5   ? OD1 ? B ASP 5   OD1 
36 1 Y 1 B ASP 5   ? OD2 ? B ASP 5   OD2 
37 1 Y 1 B ARG 6   ? CG  ? B ARG 6   CG  
38 1 Y 1 B ARG 6   ? CD  ? B ARG 6   CD  
39 1 Y 1 B ARG 6   ? NE  ? B ARG 6   NE  
40 1 Y 1 B ARG 6   ? CZ  ? B ARG 6   CZ  
41 1 Y 1 B ARG 6   ? NH1 ? B ARG 6   NH1 
42 1 Y 1 B ARG 6   ? NH2 ? B ARG 6   NH2 
43 1 Y 1 B ARG 14  ? NE  ? B ARG 14  NE  
44 1 Y 1 B ARG 14  ? CZ  ? B ARG 14  CZ  
45 1 Y 1 B ARG 14  ? NH1 ? B ARG 14  NH1 
46 1 Y 1 B ARG 14  ? NH2 ? B ARG 14  NH2 
47 1 Y 1 B ARG 69  ? CG  ? B ARG 69  CG  
48 1 Y 1 B ARG 69  ? CD  ? B ARG 69  CD  
49 1 Y 1 B ARG 69  ? NE  ? B ARG 69  NE  
50 1 Y 1 B ARG 69  ? CZ  ? B ARG 69  CZ  
51 1 Y 1 B ARG 69  ? NH1 ? B ARG 69  NH1 
52 1 Y 1 B ARG 69  ? NH2 ? B ARG 69  NH2 
53 1 Y 1 B GLN 96  ? CD  ? B GLN 96  CD  
54 1 Y 1 B GLN 96  ? OE1 ? B GLN 96  OE1 
55 1 Y 1 B GLN 96  ? NE2 ? B GLN 96  NE2 
56 1 Y 1 B ASN 130 ? CG  ? B ASN 130 CG  
57 1 Y 1 B ASN 130 ? OD1 ? B ASN 130 OD1 
58 1 Y 1 B ASN 130 ? ND2 ? B ASN 130 ND2 
59 1 Y 1 B ASP 131 ? CG  ? B ASP 131 CG  
60 1 Y 1 B ASP 131 ? OD1 ? B ASP 131 OD1 
61 1 Y 1 B ASP 131 ? OD2 ? B ASP 131 OD2 
62 1 Y 1 B ARG 135 ? CG  ? B ARG 135 CG  
63 1 Y 1 B ARG 135 ? CD  ? B ARG 135 CD  
64 1 Y 1 B ARG 135 ? NE  ? B ARG 135 NE  
65 1 Y 1 B ARG 135 ? CZ  ? B ARG 135 CZ  
66 1 Y 1 B ARG 135 ? NH1 ? B ARG 135 NH1 
67 1 Y 1 B ARG 135 ? NH2 ? B ARG 135 NH2 
68 1 Y 1 B ASP 169 ? CG  ? B ASP 169 CG  
69 1 Y 1 B ASP 169 ? OD1 ? B ASP 169 OD1 
70 1 Y 1 B ASP 169 ? OD2 ? B ASP 169 OD2 
71 1 Y 1 B ARG 185 ? CG  ? B ARG 185 CG  
72 1 Y 1 B ARG 185 ? CD  ? B ARG 185 CD  
73 1 Y 1 B ARG 185 ? NE  ? B ARG 185 NE  
74 1 Y 1 B ARG 185 ? CZ  ? B ARG 185 CZ  
75 1 Y 1 B ARG 185 ? NH1 ? B ARG 185 NH1 
76 1 Y 1 B ARG 185 ? NH2 ? B ARG 185 NH2 
77 1 Y 1 B GLN 207 ? CG  ? B GLN 207 CG  
78 1 Y 1 B GLN 207 ? CD  ? B GLN 207 CD  
79 1 Y 1 B GLN 207 ? OE1 ? B GLN 207 OE1 
80 1 Y 1 B GLN 207 ? NE2 ? B GLN 207 NE2 
81 1 Y 1 B GLU 226 ? CG  ? B GLU 226 CG  
82 1 Y 1 B GLU 226 ? CD  ? B GLU 226 CD  
83 1 Y 1 B GLU 226 ? OE1 ? B GLU 226 OE1 
84 1 Y 1 B GLU 226 ? OE2 ? B GLU 226 OE2 
85 1 Y 1 B ASP 261 ? CG  ? B ASP 261 CG  
86 1 Y 1 B ASP 261 ? OD1 ? B ASP 261 OD1 
87 1 Y 1 B ASP 261 ? OD2 ? B ASP 261 OD2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.18.2_3874 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DRK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.651 
_cell.length_a_esd                 ? 
_cell.length_b                     68.705 
_cell.length_b_esd                 ? 
_cell.length_c                     115.134 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DRK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9DRK 
_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             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.19 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% MPEG 2000, 50 mM trimethylamine N-oxide, and 100 mM Tris pH 8.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-06-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_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                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DRK 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.13 
_reflns.d_resolution_low                               42.95 
_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                                     28673 
_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                           94.03 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.23 
_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                                   0.999 
_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                                    2.13 
_reflns_shell.d_res_low                                     2.206 
_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                             2784 
_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                                  0.756 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DRK 
_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                            2.13 
_refine.ls_d_res_low                             42.95 
_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                     26971 
_refine.ls_number_reflns_R_free                  1353 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.08 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1968 
_refine.ls_R_factor_R_free                       0.2620 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1934 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.49 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.28 
_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                       2.13 
_refine_hist.d_res_low                        42.95 
_refine_hist.number_atoms_solvent             72 
_refine_hist.number_atoms_total               3945 
_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        3799 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         74 
_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' ? 0.009  ? 3975 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.070  ? 5443 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 30.623 ? 593  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.063  ? 655  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 707  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.13 2.20  . . 138 2656 99.00  . . . . 0.2474 . . . . . . . . . . . 0.3257 
'X-RAY DIFFRACTION' 2.20 2.29  . . 112 2065 77.00  . . . . 0.2347 . . . . . . . . . . . 0.3009 
'X-RAY DIFFRACTION' 2.29 2.39  . . 129 2691 99.00  . . . . 0.2126 . . . . . . . . . . . 0.2997 
'X-RAY DIFFRACTION' 2.39 2.52  . . 155 2670 100.00 . . . . 0.2045 . . . . . . . . . . . 0.2894 
'X-RAY DIFFRACTION' 2.52 2.64  . . 90  2050 98.00  . . . . 0.2209 . . . . . . . . . . . 0.2991 
'X-RAY DIFFRACTION' 2.69 2.89  . . 135 2458 100.00 . . . . 0.2176 . . . . . . . . . . . 0.3157 
'X-RAY DIFFRACTION' 2.89 3.18  . . 160 2691 100.00 . . . . 0.2084 . . . . . . . . . . . 0.3044 
'X-RAY DIFFRACTION' 3.18 3.63  . . 143 2731 100.00 . . . . 0.1921 . . . . . . . . . . . 0.2762 
'X-RAY DIFFRACTION' 3.63 4.58  . . 139 2730 99.00  . . . . 0.1655 . . . . . . . . . . . 0.2192 
'X-RAY DIFFRACTION' 4.58 42.95 . . 152 2876 99.00  . . . . 0.1826 . . . . . . . . . . . 0.2274 
# 
_struct.entry_id                     9DRK 
_struct.title                        'Crystal structure of Mycobacterium tuberculosis biotin protein ligase in complex with Bio-1' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9DRK 
_struct_keywords.text            'Biotin protein ligase, Adenylation inhibitors, Nucleoside, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BIRA_MYCTU 
_struct_ref.pdbx_db_accession          I6YFP0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARA
QIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVT
QAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDI
DDQGRLCLDVGGRTVVVSAGDVVHL
;
_struct_ref.pdbx_align_begin           1 
# 
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 9DRK A 1 ? 265 ? I6YFP0 1 ? 265 ? 1 265 
2 1 9DRK B 1 ? 265 ? I6YFP0 1 ? 265 ? 1 265 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 MET A 1   ? ARG A 6   ? MET A 1   ARG A 6   1 ? 6  
HELX_P HELX_P2  AA2 ASP A 12  ? ILE A 21  ? ASP A 12  ILE A 21  1 ? 10 
HELX_P HELX_P3  AA3 SER A 38  ? SER A 49  ? SER A 38  SER A 49  1 ? 12 
HELX_P HELX_P4  AA4 ARG A 69  ? GLY A 71  ? ARG A 69  GLY A 71  5 ? 3  
HELX_P HELX_P5  AA5 PRO A 94  ? ALA A 97  ? PRO A 94  ALA A 97  5 ? 4  
HELX_P HELX_P6  AA6 TRP A 98  ? ALA A 114 ? TRP A 98  ALA A 114 1 ? 17 
HELX_P HELX_P7  AA7 PRO A 115 ? ILE A 117 ? PRO A 115 ILE A 117 5 ? 3  
HELX_P HELX_P8  AA8 ALA A 162 ? ASP A 167 ? ALA A 162 ASP A 167 1 ? 6  
HELX_P HELX_P9  AA9 LEU A 173 ? GLY A 177 ? LEU A 173 GLY A 177 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 182 ? ASN A 203 ? ASP A 182 ASN A 203 1 ? 22 
HELX_P HELX_P11 AB2 ASN A 205 ? SER A 216 ? ASN A 205 SER A 216 1 ? 12 
HELX_P HELX_P12 AB3 ARG B 4   ? ARG B 8   ? ARG B 4   ARG B 8   5 ? 5  
HELX_P HELX_P13 AB4 ASP B 12  ? ILE B 21  ? ASP B 12  ILE B 21  1 ? 10 
HELX_P HELX_P14 AB5 SER B 38  ? SER B 49  ? SER B 38  SER B 49  1 ? 12 
HELX_P HELX_P15 AB6 PRO B 94  ? TRP B 98  ? PRO B 94  TRP B 98  5 ? 5  
HELX_P HELX_P16 AB7 GLY B 99  ? ALA B 114 ? GLY B 99  ALA B 114 1 ? 16 
HELX_P HELX_P17 AB8 PRO B 115 ? ILE B 117 ? PRO B 115 ILE B 117 5 ? 3  
HELX_P HELX_P18 AB9 PRO B 120 ? ALA B 122 ? PRO B 120 ALA B 122 5 ? 3  
HELX_P HELX_P19 AC1 ALA B 162 ? ASP B 167 ? ALA B 162 ASP B 167 1 ? 6  
HELX_P HELX_P20 AC2 ASP B 182 ? ASN B 203 ? ASP B 182 ASN B 203 1 ? 22 
HELX_P HELX_P21 AC3 PRO B 206 ? SER B 216 ? PRO B 206 SER B 216 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 TRP 128 A . ? TRP 128 A PRO 129 A ? PRO 129 A 1 6.43 
2 GLN 148 A . ? GLN 148 A PRO 149 A ? PRO 149 A 1 6.62 
3 TRP 128 B . ? TRP 128 B PRO 129 B ? PRO 129 B 1 2.05 
4 GLN 148 B . ? GLN 148 B PRO 149 B ? PRO 149 B 1 1.35 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7  ? 
AA2 ? 2  ? 
AA3 ? 10 ? 
AA4 ? 7  ? 
AA5 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? anti-parallel 
AA1 3 4  ? anti-parallel 
AA1 4 5  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA1 6 7  ? anti-parallel 
AA2 1 2  ? anti-parallel 
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 
AA3 8 9  ? anti-parallel 
AA3 9 10 ? anti-parallel 
AA4 1 2  ? 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 
# 
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 29  ? THR A 36  ? GLN A 29  THR A 36  
AA1 2  VAL A 56  ? GLN A 63  ? VAL A 56  GLN A 63  
AA1 3  GLN A 81  ? ARG A 89  ? GLN A 81  ARG A 89  
AA1 4  PHE A 150 ? ASN A 158 ? PHE A 150 ASN A 158 
AA1 5  GLY A 137 ? ALA A 147 ? GLY A 137 ALA A 147 
AA1 6  ASP A 131 ? ALA A 134 ? ASP A 131 ALA A 134 
AA1 7  GLY A 125 ? LYS A 127 ? GLY A 125 LYS A 127 
AA2 1  GLY A 66  ? ARG A 67  ? GLY A 66  ARG A 67  
AA2 2  GLY A 73  ? TRP A 74  ? GLY A 73  TRP A 74  
AA3 1  ASP A 261 ? HIS A 264 ? ASP A 261 HIS A 264 
AA3 2  ARG A 222 ? LEU A 227 ? ARG A 222 LEU A 227 
AA3 3  GLN A 231 ? ILE A 240 ? GLN A 231 ILE A 240 
AA3 4  LEU A 246 ? VAL A 250 ? LEU A 246 VAL A 250 
AA3 5  ARG A 253 ? VAL A 257 ? ARG A 253 VAL A 257 
AA3 6  ARG B 253 ? VAL B 257 ? ARG B 253 VAL B 257 
AA3 7  LEU B 246 ? VAL B 250 ? LEU B 246 VAL B 250 
AA3 8  GLN B 231 ? ILE B 240 ? GLN B 231 ILE B 240 
AA3 9  ARG B 222 ? LEU B 227 ? ARG B 222 LEU B 227 
AA3 10 ASP B 261 ? HIS B 264 ? ASP B 261 HIS B 264 
AA4 1  GLN B 29  ? VAL B 33  ? GLN B 29  VAL B 33  
AA4 2  VAL B 56  ? ALA B 60  ? VAL B 56  ALA B 60  
AA4 3  GLN B 81  ? ARG B 89  ? GLN B 81  ARG B 89  
AA4 4  PHE B 150 ? ASN B 158 ? PHE B 150 ASN B 158 
AA4 5  GLY B 137 ? ALA B 147 ? GLY B 137 ALA B 147 
AA4 6  ASP B 131 ? ALA B 134 ? ASP B 131 ALA B 134 
AA4 7  THR B 124 ? LYS B 127 ? THR B 124 LYS B 127 
AA5 1  GLY B 66  ? ARG B 67  ? GLY B 66  ARG B 67  
AA5 2  GLY B 73  ? TRP B 74  ? GLY B 73  TRP B 74  
# 
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 29  ? N GLN A 29  O VAL A 57  ? O VAL A 57  
AA1 2 3  N LEU A 58  ? N LEU A 58  O SER A 85  ? O SER A 85  
AA1 3 4  N LEU A 84  ? N LEU A 84  O VAL A 155 ? O VAL A 155 
AA1 4 5  O PHE A 150 ? O PHE A 150 N ALA A 147 ? N ALA A 147 
AA1 5 6  O GLY A 137 ? O GLY A 137 N ALA A 134 ? N ALA A 134 
AA1 6 7  O ASP A 131 ? O ASP A 131 N LYS A 127 ? N LYS A 127 
AA2 1 2  N GLY A 66  ? N GLY A 66  O TRP A 74  ? O TRP A 74  
AA3 1 2  O ASP A 261 ? O ASP A 261 N GLU A 226 ? N GLU A 226 
AA3 2 3  N VAL A 225 ? N VAL A 225 O VAL A 233 ? O VAL A 233 
AA3 3 4  N ARG A 238 ? N ARG A 238 O CYS A 247 ? O CYS A 247 
AA3 4 5  N LEU A 248 ? N LEU A 248 O VAL A 255 ? O VAL A 255 
AA3 5 6  N VAL A 256 ? N VAL A 256 O VAL B 256 ? O VAL B 256 
AA3 6 7  O VAL B 255 ? O VAL B 255 N LEU B 248 ? N LEU B 248 
AA3 7 8  O CYS B 247 ? O CYS B 247 N ASP B 239 ? N ASP B 239 
AA3 8 9  O GLY B 235 ? O GLY B 235 N VAL B 223 ? N VAL B 223 
AA3 9 10 N GLU B 226 ? N GLU B 226 O ASP B 261 ? O ASP B 261 
AA4 1 2  N VAL B 33  ? N VAL B 33  O ILE B 59  ? O ILE B 59  
AA4 2 3  N LEU B 58  ? N LEU B 58  O SER B 85  ? O SER B 85  
AA4 3 4  N LEU B 84  ? N LEU B 84  O VAL B 155 ? O VAL B 155 
AA4 4 5  O PHE B 150 ? O PHE B 150 N ALA B 147 ? N ALA B 147 
AA4 5 6  O LEU B 139 ? O LEU B 139 N VAL B 132 ? N VAL B 132 
AA4 6 7  O ASP B 131 ? O ASP B 131 N LYS B 127 ? N LYS B 127 
AA5 1 2  N GLY B 66  ? N GLY B 66  O TRP B 74  ? O TRP B 74  
# 
_pdbx_entry_details.entry_id                   9DRK 
_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   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 VAL A 166 ? ? -134.74 -38.37 
2 1 ASP A 167 ? ? -174.74 137.01 
3 1 ALA A 179 ? ? -45.35  -73.20 
4 1 ARG B 8   ? ? -116.66 61.80  
5 1 ALA B 23  ? ? -115.38 -95.98 
6 1 PRO B 115 ? ? -67.64  6.10   
7 1 ALA B 147 ? ? -155.88 83.89  
8 1 VAL B 166 ? ? -137.57 -46.43 
9 1 ASP B 167 ? ? -175.60 140.33 
# 
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 ALA 118 ? A ALA 118 
2 1 Y 1 A VAL 119 ? A VAL 119 
3 1 Y 1 A PRO 120 ? A PRO 120 
4 1 Y 1 A PRO 121 ? A PRO 121 
5 1 Y 1 A ALA 122 ? A ALA 122 
6 1 Y 1 B MET 1   ? B MET 1   
7 1 Y 1 B THR 2   ? B THR 2   
8 1 Y 1 B ASP 3   ? B ASP 3   
# 
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 
A1BGE C11  C N R 1   
A1BGE C02  C Y N 2   
A1BGE C04  C Y N 3   
A1BGE C06  C Y N 4   
A1BGE C07  C Y N 5   
A1BGE C09  C Y N 6   
A1BGE C12  C N R 7   
A1BGE C14  C N S 8   
A1BGE C16  C N R 9   
A1BGE C17  C N N 10  
A1BGE C22  C N N 11  
A1BGE C23  C N N 12  
A1BGE C24  C N N 13  
A1BGE C25  C N N 14  
A1BGE C26  C N N 15  
A1BGE C27  C N S 16  
A1BGE C29  C N N 17  
A1BGE C30  C N R 18  
A1BGE C31  C N S 19  
A1BGE C33  C N N 20  
A1BGE N01  N N N 21  
A1BGE N03  N Y N 22  
A1BGE N05  N Y N 23  
A1BGE N08  N Y N 24  
A1BGE N10  N Y N 25  
A1BGE N18  N N N 26  
A1BGE N21  N N N 27  
A1BGE N32  N N N 28  
A1BGE N34  N N N 29  
A1BGE O13  O N N 30  
A1BGE O15  O N N 31  
A1BGE O20  O N N 32  
A1BGE O35  O N N 33  
A1BGE O36  O N N 34  
A1BGE O37  O N N 35  
A1BGE S19  S N N 36  
A1BGE S28  S N N 37  
A1BGE H1   H N N 38  
A1BGE H2   H N N 39  
A1BGE H3   H N N 40  
A1BGE H4   H N N 41  
A1BGE H5   H N N 42  
A1BGE H6   H N N 43  
A1BGE H7   H N N 44  
A1BGE H8   H N N 45  
A1BGE H9   H N N 46  
A1BGE H10  H N N 47  
A1BGE H11  H N N 48  
A1BGE H12  H N N 49  
A1BGE H13  H N N 50  
A1BGE H14  H N N 51  
A1BGE H15  H N N 52  
A1BGE H16  H N N 53  
A1BGE H17  H N N 54  
A1BGE H18  H N N 55  
A1BGE H19  H N N 56  
A1BGE H20  H N N 57  
A1BGE H21  H N N 58  
A1BGE H22  H N N 59  
A1BGE H23  H N N 60  
A1BGE H24  H N N 61  
A1BGE H25  H N N 62  
A1BGE H26  H N N 63  
A1BGE H27  H N N 64  
A1BGE H28  H N N 65  
A1BGE H29  H N N 66  
A1BGE H30  H N N 67  
A1BGE H31  H N N 68  
ALA   N    N N N 69  
ALA   CA   C N S 70  
ALA   C    C N N 71  
ALA   O    O N N 72  
ALA   CB   C N N 73  
ALA   OXT  O N N 74  
ALA   H    H N N 75  
ALA   H2   H N N 76  
ALA   HA   H N N 77  
ALA   HB1  H N N 78  
ALA   HB2  H N N 79  
ALA   HB3  H N N 80  
ALA   HXT  H N N 81  
ARG   N    N N N 82  
ARG   CA   C N S 83  
ARG   C    C N N 84  
ARG   O    O N N 85  
ARG   CB   C N N 86  
ARG   CG   C N N 87  
ARG   CD   C N N 88  
ARG   NE   N N N 89  
ARG   CZ   C N N 90  
ARG   NH1  N N N 91  
ARG   NH2  N N N 92  
ARG   OXT  O N N 93  
ARG   H    H N N 94  
ARG   H2   H N N 95  
ARG   HA   H N N 96  
ARG   HB2  H N N 97  
ARG   HB3  H N N 98  
ARG   HG2  H N N 99  
ARG   HG3  H N N 100 
ARG   HD2  H N N 101 
ARG   HD3  H N N 102 
ARG   HE   H N N 103 
ARG   HH11 H N N 104 
ARG   HH12 H N N 105 
ARG   HH21 H N N 106 
ARG   HH22 H N N 107 
ARG   HXT  H N N 108 
ASN   N    N N N 109 
ASN   CA   C N S 110 
ASN   C    C N N 111 
ASN   O    O N N 112 
ASN   CB   C N N 113 
ASN   CG   C N N 114 
ASN   OD1  O N N 115 
ASN   ND2  N N N 116 
ASN   OXT  O N N 117 
ASN   H    H N N 118 
ASN   H2   H N N 119 
ASN   HA   H N N 120 
ASN   HB2  H N N 121 
ASN   HB3  H N N 122 
ASN   HD21 H N N 123 
ASN   HD22 H N N 124 
ASN   HXT  H N N 125 
ASP   N    N N N 126 
ASP   CA   C N S 127 
ASP   C    C N N 128 
ASP   O    O N N 129 
ASP   CB   C N N 130 
ASP   CG   C N N 131 
ASP   OD1  O N N 132 
ASP   OD2  O N N 133 
ASP   OXT  O N N 134 
ASP   H    H N N 135 
ASP   H2   H N N 136 
ASP   HA   H N N 137 
ASP   HB2  H N N 138 
ASP   HB3  H N N 139 
ASP   HD2  H N N 140 
ASP   HXT  H N N 141 
CYS   N    N N N 142 
CYS   CA   C N R 143 
CYS   C    C N N 144 
CYS   O    O N N 145 
CYS   CB   C N N 146 
CYS   SG   S N N 147 
CYS   OXT  O N N 148 
CYS   H    H N N 149 
CYS   H2   H N N 150 
CYS   HA   H N N 151 
CYS   HB2  H N N 152 
CYS   HB3  H N N 153 
CYS   HG   H N N 154 
CYS   HXT  H N N 155 
GLN   N    N N N 156 
GLN   CA   C N S 157 
GLN   C    C N N 158 
GLN   O    O N N 159 
GLN   CB   C N N 160 
GLN   CG   C N N 161 
GLN   CD   C N N 162 
GLN   OE1  O N N 163 
GLN   NE2  N N N 164 
GLN   OXT  O N N 165 
GLN   H    H N N 166 
GLN   H2   H N N 167 
GLN   HA   H N N 168 
GLN   HB2  H N N 169 
GLN   HB3  H N N 170 
GLN   HG2  H N N 171 
GLN   HG3  H N N 172 
GLN   HE21 H N N 173 
GLN   HE22 H N N 174 
GLN   HXT  H N N 175 
GLU   N    N N N 176 
GLU   CA   C N S 177 
GLU   C    C N N 178 
GLU   O    O N N 179 
GLU   CB   C N N 180 
GLU   CG   C N N 181 
GLU   CD   C N N 182 
GLU   OE1  O N N 183 
GLU   OE2  O N N 184 
GLU   OXT  O N N 185 
GLU   H    H N N 186 
GLU   H2   H N N 187 
GLU   HA   H N N 188 
GLU   HB2  H N N 189 
GLU   HB3  H N N 190 
GLU   HG2  H N N 191 
GLU   HG3  H N N 192 
GLU   HE2  H N N 193 
GLU   HXT  H N N 194 
GLY   N    N N N 195 
GLY   CA   C N N 196 
GLY   C    C N N 197 
GLY   O    O N N 198 
GLY   OXT  O N N 199 
GLY   H    H N N 200 
GLY   H2   H N N 201 
GLY   HA2  H N N 202 
GLY   HA3  H N N 203 
GLY   HXT  H N N 204 
HIS   N    N N N 205 
HIS   CA   C N S 206 
HIS   C    C N N 207 
HIS   O    O N N 208 
HIS   CB   C N N 209 
HIS   CG   C Y N 210 
HIS   ND1  N Y N 211 
HIS   CD2  C Y N 212 
HIS   CE1  C Y N 213 
HIS   NE2  N Y N 214 
HIS   OXT  O N N 215 
HIS   H    H N N 216 
HIS   H2   H N N 217 
HIS   HA   H N N 218 
HIS   HB2  H N N 219 
HIS   HB3  H N N 220 
HIS   HD1  H N N 221 
HIS   HD2  H N N 222 
HIS   HE1  H N N 223 
HIS   HE2  H N N 224 
HIS   HXT  H N N 225 
HOH   O    O N N 226 
HOH   H1   H N N 227 
HOH   H2   H N N 228 
ILE   N    N N N 229 
ILE   CA   C N S 230 
ILE   C    C N N 231 
ILE   O    O N N 232 
ILE   CB   C N S 233 
ILE   CG1  C N N 234 
ILE   CG2  C N N 235 
ILE   CD1  C N N 236 
ILE   OXT  O N N 237 
ILE   H    H N N 238 
ILE   H2   H N N 239 
ILE   HA   H N N 240 
ILE   HB   H N N 241 
ILE   HG12 H N N 242 
ILE   HG13 H N N 243 
ILE   HG21 H N N 244 
ILE   HG22 H N N 245 
ILE   HG23 H N N 246 
ILE   HD11 H N N 247 
ILE   HD12 H N N 248 
ILE   HD13 H N N 249 
ILE   HXT  H N N 250 
LEU   N    N N N 251 
LEU   CA   C N S 252 
LEU   C    C N N 253 
LEU   O    O N N 254 
LEU   CB   C N N 255 
LEU   CG   C N N 256 
LEU   CD1  C N N 257 
LEU   CD2  C N N 258 
LEU   OXT  O N N 259 
LEU   H    H N N 260 
LEU   H2   H N N 261 
LEU   HA   H N N 262 
LEU   HB2  H N N 263 
LEU   HB3  H N N 264 
LEU   HG   H N N 265 
LEU   HD11 H N N 266 
LEU   HD12 H N N 267 
LEU   HD13 H N N 268 
LEU   HD21 H N N 269 
LEU   HD22 H N N 270 
LEU   HD23 H N N 271 
LEU   HXT  H N N 272 
LYS   N    N N N 273 
LYS   CA   C N S 274 
LYS   C    C N N 275 
LYS   O    O N N 276 
LYS   CB   C N N 277 
LYS   CG   C N N 278 
LYS   CD   C N N 279 
LYS   CE   C N N 280 
LYS   NZ   N N N 281 
LYS   OXT  O N N 282 
LYS   H    H N N 283 
LYS   H2   H N N 284 
LYS   HA   H N N 285 
LYS   HB2  H N N 286 
LYS   HB3  H N N 287 
LYS   HG2  H N N 288 
LYS   HG3  H N N 289 
LYS   HD2  H N N 290 
LYS   HD3  H N N 291 
LYS   HE2  H N N 292 
LYS   HE3  H N N 293 
LYS   HZ1  H N N 294 
LYS   HZ2  H N N 295 
LYS   HZ3  H N N 296 
LYS   HXT  H N N 297 
MET   N    N N N 298 
MET   CA   C N S 299 
MET   C    C N N 300 
MET   O    O N N 301 
MET   CB   C N N 302 
MET   CG   C N N 303 
MET   SD   S N N 304 
MET   CE   C N N 305 
MET   OXT  O N N 306 
MET   H    H N N 307 
MET   H2   H N N 308 
MET   HA   H N N 309 
MET   HB2  H N N 310 
MET   HB3  H N N 311 
MET   HG2  H N N 312 
MET   HG3  H N N 313 
MET   HE1  H N N 314 
MET   HE2  H N N 315 
MET   HE3  H N N 316 
MET   HXT  H N N 317 
PHE   N    N N N 318 
PHE   CA   C N S 319 
PHE   C    C N N 320 
PHE   O    O N N 321 
PHE   CB   C N N 322 
PHE   CG   C Y N 323 
PHE   CD1  C Y N 324 
PHE   CD2  C Y N 325 
PHE   CE1  C Y N 326 
PHE   CE2  C Y N 327 
PHE   CZ   C Y N 328 
PHE   OXT  O N N 329 
PHE   H    H N N 330 
PHE   H2   H N N 331 
PHE   HA   H N N 332 
PHE   HB2  H N N 333 
PHE   HB3  H N N 334 
PHE   HD1  H N N 335 
PHE   HD2  H N N 336 
PHE   HE1  H N N 337 
PHE   HE2  H N N 338 
PHE   HZ   H N N 339 
PHE   HXT  H N N 340 
PRO   N    N N N 341 
PRO   CA   C N S 342 
PRO   C    C N N 343 
PRO   O    O N N 344 
PRO   CB   C N N 345 
PRO   CG   C N N 346 
PRO   CD   C N N 347 
PRO   OXT  O N N 348 
PRO   H    H N N 349 
PRO   HA   H N N 350 
PRO   HB2  H N N 351 
PRO   HB3  H N N 352 
PRO   HG2  H N N 353 
PRO   HG3  H N N 354 
PRO   HD2  H N N 355 
PRO   HD3  H N N 356 
PRO   HXT  H N N 357 
SER   N    N N N 358 
SER   CA   C N S 359 
SER   C    C N N 360 
SER   O    O N N 361 
SER   CB   C N N 362 
SER   OG   O N N 363 
SER   OXT  O N N 364 
SER   H    H N N 365 
SER   H2   H N N 366 
SER   HA   H N N 367 
SER   HB2  H N N 368 
SER   HB3  H N N 369 
SER   HG   H N N 370 
SER   HXT  H N N 371 
THR   N    N N N 372 
THR   CA   C N S 373 
THR   C    C N N 374 
THR   O    O N N 375 
THR   CB   C N R 376 
THR   OG1  O N N 377 
THR   CG2  C N N 378 
THR   OXT  O N N 379 
THR   H    H N N 380 
THR   H2   H N N 381 
THR   HA   H N N 382 
THR   HB   H N N 383 
THR   HG1  H N N 384 
THR   HG21 H N N 385 
THR   HG22 H N N 386 
THR   HG23 H N N 387 
THR   HXT  H N N 388 
TRP   N    N N N 389 
TRP   CA   C N S 390 
TRP   C    C N N 391 
TRP   O    O N N 392 
TRP   CB   C N N 393 
TRP   CG   C Y N 394 
TRP   CD1  C Y N 395 
TRP   CD2  C Y N 396 
TRP   NE1  N Y N 397 
TRP   CE2  C Y N 398 
TRP   CE3  C Y N 399 
TRP   CZ2  C Y N 400 
TRP   CZ3  C Y N 401 
TRP   CH2  C Y N 402 
TRP   OXT  O N N 403 
TRP   H    H N N 404 
TRP   H2   H N N 405 
TRP   HA   H N N 406 
TRP   HB2  H N N 407 
TRP   HB3  H N N 408 
TRP   HD1  H N N 409 
TRP   HE1  H N N 410 
TRP   HE3  H N N 411 
TRP   HZ2  H N N 412 
TRP   HZ3  H N N 413 
TRP   HH2  H N N 414 
TRP   HXT  H N N 415 
TYR   N    N N N 416 
TYR   CA   C N S 417 
TYR   C    C N N 418 
TYR   O    O N N 419 
TYR   CB   C N N 420 
TYR   CG   C Y N 421 
TYR   CD1  C Y N 422 
TYR   CD2  C Y N 423 
TYR   CE1  C Y N 424 
TYR   CE2  C Y N 425 
TYR   CZ   C Y N 426 
TYR   OH   O N N 427 
TYR   OXT  O N N 428 
TYR   H    H N N 429 
TYR   H2   H N N 430 
TYR   HA   H N N 431 
TYR   HB2  H N N 432 
TYR   HB3  H N N 433 
TYR   HD1  H N N 434 
TYR   HD2  H N N 435 
TYR   HE1  H N N 436 
TYR   HE2  H N N 437 
TYR   HH   H N N 438 
TYR   HXT  H N N 439 
VAL   N    N N N 440 
VAL   CA   C N S 441 
VAL   C    C N N 442 
VAL   O    O N N 443 
VAL   CB   C N N 444 
VAL   CG1  C N N 445 
VAL   CG2  C N N 446 
VAL   OXT  O N N 447 
VAL   H    H N N 448 
VAL   H2   H N N 449 
VAL   HA   H N N 450 
VAL   HB   H N N 451 
VAL   HG11 H N N 452 
VAL   HG12 H N N 453 
VAL   HG13 H N N 454 
VAL   HG21 H N N 455 
VAL   HG22 H N N 456 
VAL   HG23 H N N 457 
VAL   HXT  H N N 458 
# 
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 
A1BGE O36 S19  doub N N 1   
A1BGE S19 O20  doub N N 2   
A1BGE S19 N18  sing N N 3   
A1BGE S19 N21  sing N N 4   
A1BGE N18 C17  sing N N 5   
A1BGE O15 C14  sing N N 6   
A1BGE N21 C22  sing N N 7   
A1BGE C17 C16  sing N N 8   
A1BGE C16 C14  sing N N 9   
A1BGE C16 O37  sing N N 10  
A1BGE O13 C12  sing N N 11  
A1BGE C14 C12  sing N N 12  
A1BGE C22 C23  sing N N 13  
A1BGE O37 C11  sing N N 14  
A1BGE C12 C11  sing N N 15  
A1BGE C11 N10  sing N N 16  
A1BGE C23 C24  sing N N 17  
A1BGE C24 C25  sing N N 18  
A1BGE N10 C06  sing Y N 19  
A1BGE N10 C09  sing Y N 20  
A1BGE N05 C06  doub Y N 21  
A1BGE N05 C04  sing Y N 22  
A1BGE C06 C07  sing Y N 23  
A1BGE C09 N08  doub Y N 24  
A1BGE C25 C26  sing N N 25  
A1BGE C04 N03  doub Y N 26  
A1BGE C07 N08  sing Y N 27  
A1BGE C07 C02  doub Y N 28  
A1BGE C26 C27  sing N N 29  
A1BGE N32 C31  sing N N 30  
A1BGE N32 C33  sing N N 31  
A1BGE N03 C02  sing Y N 32  
A1BGE C31 C27  sing N N 33  
A1BGE C31 C30  sing N N 34  
A1BGE C27 S28  sing N N 35  
A1BGE C02 N01  sing N N 36  
A1BGE O35 C33  doub N N 37  
A1BGE C33 N34  sing N N 38  
A1BGE C30 N34  sing N N 39  
A1BGE C30 C29  sing N N 40  
A1BGE S28 C29  sing N N 41  
A1BGE C11 H1   sing N N 42  
A1BGE C04 H2   sing N N 43  
A1BGE C09 H3   sing N N 44  
A1BGE C12 H4   sing N N 45  
A1BGE C14 H5   sing N N 46  
A1BGE C16 H6   sing N N 47  
A1BGE C17 H7   sing N N 48  
A1BGE C17 H8   sing N N 49  
A1BGE C22 H9   sing N N 50  
A1BGE C22 H10  sing N N 51  
A1BGE C23 H11  sing N N 52  
A1BGE C23 H12  sing N N 53  
A1BGE C24 H13  sing N N 54  
A1BGE C24 H14  sing N N 55  
A1BGE C25 H15  sing N N 56  
A1BGE C25 H16  sing N N 57  
A1BGE C26 H17  sing N N 58  
A1BGE C26 H18  sing N N 59  
A1BGE C27 H19  sing N N 60  
A1BGE C29 H20  sing N N 61  
A1BGE C29 H21  sing N N 62  
A1BGE C30 H22  sing N N 63  
A1BGE C31 H23  sing N N 64  
A1BGE N01 H24  sing N N 65  
A1BGE N01 H25  sing N N 66  
A1BGE N18 H26  sing N N 67  
A1BGE N21 H27  sing N N 68  
A1BGE N32 H28  sing N N 69  
A1BGE N34 H29  sing N N 70  
A1BGE O13 H30  sing N N 71  
A1BGE O15 H31  sing N N 72  
ALA   N   CA   sing N N 73  
ALA   N   H    sing N N 74  
ALA   N   H2   sing N N 75  
ALA   CA  C    sing N N 76  
ALA   CA  CB   sing N N 77  
ALA   CA  HA   sing N N 78  
ALA   C   O    doub N N 79  
ALA   C   OXT  sing N N 80  
ALA   CB  HB1  sing N N 81  
ALA   CB  HB2  sing N N 82  
ALA   CB  HB3  sing N N 83  
ALA   OXT HXT  sing N N 84  
ARG   N   CA   sing N N 85  
ARG   N   H    sing N N 86  
ARG   N   H2   sing N N 87  
ARG   CA  C    sing N N 88  
ARG   CA  CB   sing N N 89  
ARG   CA  HA   sing N N 90  
ARG   C   O    doub N N 91  
ARG   C   OXT  sing N N 92  
ARG   CB  CG   sing N N 93  
ARG   CB  HB2  sing N N 94  
ARG   CB  HB3  sing N N 95  
ARG   CG  CD   sing N N 96  
ARG   CG  HG2  sing N N 97  
ARG   CG  HG3  sing N N 98  
ARG   CD  NE   sing N N 99  
ARG   CD  HD2  sing N N 100 
ARG   CD  HD3  sing N N 101 
ARG   NE  CZ   sing N N 102 
ARG   NE  HE   sing N N 103 
ARG   CZ  NH1  sing N N 104 
ARG   CZ  NH2  doub N N 105 
ARG   NH1 HH11 sing N N 106 
ARG   NH1 HH12 sing N N 107 
ARG   NH2 HH21 sing N N 108 
ARG   NH2 HH22 sing N N 109 
ARG   OXT HXT  sing N N 110 
ASN   N   CA   sing N N 111 
ASN   N   H    sing N N 112 
ASN   N   H2   sing N N 113 
ASN   CA  C    sing N N 114 
ASN   CA  CB   sing N N 115 
ASN   CA  HA   sing N N 116 
ASN   C   O    doub N N 117 
ASN   C   OXT  sing N N 118 
ASN   CB  CG   sing N N 119 
ASN   CB  HB2  sing N N 120 
ASN   CB  HB3  sing N N 121 
ASN   CG  OD1  doub N N 122 
ASN   CG  ND2  sing N N 123 
ASN   ND2 HD21 sing N N 124 
ASN   ND2 HD22 sing N N 125 
ASN   OXT HXT  sing N N 126 
ASP   N   CA   sing N N 127 
ASP   N   H    sing N N 128 
ASP   N   H2   sing N N 129 
ASP   CA  C    sing N N 130 
ASP   CA  CB   sing N N 131 
ASP   CA  HA   sing N N 132 
ASP   C   O    doub N N 133 
ASP   C   OXT  sing N N 134 
ASP   CB  CG   sing N N 135 
ASP   CB  HB2  sing N N 136 
ASP   CB  HB3  sing N N 137 
ASP   CG  OD1  doub N N 138 
ASP   CG  OD2  sing N N 139 
ASP   OD2 HD2  sing N N 140 
ASP   OXT HXT  sing N N 141 
CYS   N   CA   sing N N 142 
CYS   N   H    sing N N 143 
CYS   N   H2   sing N N 144 
CYS   CA  C    sing N N 145 
CYS   CA  CB   sing N N 146 
CYS   CA  HA   sing N N 147 
CYS   C   O    doub N N 148 
CYS   C   OXT  sing N N 149 
CYS   CB  SG   sing N N 150 
CYS   CB  HB2  sing N N 151 
CYS   CB  HB3  sing N N 152 
CYS   SG  HG   sing N N 153 
CYS   OXT HXT  sing N N 154 
GLN   N   CA   sing N N 155 
GLN   N   H    sing N N 156 
GLN   N   H2   sing N N 157 
GLN   CA  C    sing N N 158 
GLN   CA  CB   sing N N 159 
GLN   CA  HA   sing N N 160 
GLN   C   O    doub N N 161 
GLN   C   OXT  sing N N 162 
GLN   CB  CG   sing N N 163 
GLN   CB  HB2  sing N N 164 
GLN   CB  HB3  sing N N 165 
GLN   CG  CD   sing N N 166 
GLN   CG  HG2  sing N N 167 
GLN   CG  HG3  sing N N 168 
GLN   CD  OE1  doub N N 169 
GLN   CD  NE2  sing N N 170 
GLN   NE2 HE21 sing N N 171 
GLN   NE2 HE22 sing N N 172 
GLN   OXT HXT  sing N N 173 
GLU   N   CA   sing N N 174 
GLU   N   H    sing N N 175 
GLU   N   H2   sing N N 176 
GLU   CA  C    sing N N 177 
GLU   CA  CB   sing N N 178 
GLU   CA  HA   sing N N 179 
GLU   C   O    doub N N 180 
GLU   C   OXT  sing N N 181 
GLU   CB  CG   sing N N 182 
GLU   CB  HB2  sing N N 183 
GLU   CB  HB3  sing N N 184 
GLU   CG  CD   sing N N 185 
GLU   CG  HG2  sing N N 186 
GLU   CG  HG3  sing N N 187 
GLU   CD  OE1  doub N N 188 
GLU   CD  OE2  sing N N 189 
GLU   OE2 HE2  sing N N 190 
GLU   OXT HXT  sing N N 191 
GLY   N   CA   sing N N 192 
GLY   N   H    sing N N 193 
GLY   N   H2   sing N N 194 
GLY   CA  C    sing N N 195 
GLY   CA  HA2  sing N N 196 
GLY   CA  HA3  sing N N 197 
GLY   C   O    doub N N 198 
GLY   C   OXT  sing N N 199 
GLY   OXT HXT  sing N N 200 
HIS   N   CA   sing N N 201 
HIS   N   H    sing N N 202 
HIS   N   H2   sing N N 203 
HIS   CA  C    sing N N 204 
HIS   CA  CB   sing N N 205 
HIS   CA  HA   sing N N 206 
HIS   C   O    doub N N 207 
HIS   C   OXT  sing N N 208 
HIS   CB  CG   sing N N 209 
HIS   CB  HB2  sing N N 210 
HIS   CB  HB3  sing N N 211 
HIS   CG  ND1  sing Y N 212 
HIS   CG  CD2  doub Y N 213 
HIS   ND1 CE1  doub Y N 214 
HIS   ND1 HD1  sing N N 215 
HIS   CD2 NE2  sing Y N 216 
HIS   CD2 HD2  sing N N 217 
HIS   CE1 NE2  sing Y N 218 
HIS   CE1 HE1  sing N N 219 
HIS   NE2 HE2  sing N N 220 
HIS   OXT HXT  sing N N 221 
HOH   O   H1   sing N N 222 
HOH   O   H2   sing N N 223 
ILE   N   CA   sing N N 224 
ILE   N   H    sing N N 225 
ILE   N   H2   sing N N 226 
ILE   CA  C    sing N N 227 
ILE   CA  CB   sing N N 228 
ILE   CA  HA   sing N N 229 
ILE   C   O    doub N N 230 
ILE   C   OXT  sing N N 231 
ILE   CB  CG1  sing N N 232 
ILE   CB  CG2  sing N N 233 
ILE   CB  HB   sing N N 234 
ILE   CG1 CD1  sing N N 235 
ILE   CG1 HG12 sing N N 236 
ILE   CG1 HG13 sing N N 237 
ILE   CG2 HG21 sing N N 238 
ILE   CG2 HG22 sing N N 239 
ILE   CG2 HG23 sing N N 240 
ILE   CD1 HD11 sing N N 241 
ILE   CD1 HD12 sing N N 242 
ILE   CD1 HD13 sing N N 243 
ILE   OXT HXT  sing N N 244 
LEU   N   CA   sing N N 245 
LEU   N   H    sing N N 246 
LEU   N   H2   sing N N 247 
LEU   CA  C    sing N N 248 
LEU   CA  CB   sing N N 249 
LEU   CA  HA   sing N N 250 
LEU   C   O    doub N N 251 
LEU   C   OXT  sing N N 252 
LEU   CB  CG   sing N N 253 
LEU   CB  HB2  sing N N 254 
LEU   CB  HB3  sing N N 255 
LEU   CG  CD1  sing N N 256 
LEU   CG  CD2  sing N N 257 
LEU   CG  HG   sing N N 258 
LEU   CD1 HD11 sing N N 259 
LEU   CD1 HD12 sing N N 260 
LEU   CD1 HD13 sing N N 261 
LEU   CD2 HD21 sing N N 262 
LEU   CD2 HD22 sing N N 263 
LEU   CD2 HD23 sing N N 264 
LEU   OXT HXT  sing N N 265 
LYS   N   CA   sing N N 266 
LYS   N   H    sing N N 267 
LYS   N   H2   sing N N 268 
LYS   CA  C    sing N N 269 
LYS   CA  CB   sing N N 270 
LYS   CA  HA   sing N N 271 
LYS   C   O    doub N N 272 
LYS   C   OXT  sing N N 273 
LYS   CB  CG   sing N N 274 
LYS   CB  HB2  sing N N 275 
LYS   CB  HB3  sing N N 276 
LYS   CG  CD   sing N N 277 
LYS   CG  HG2  sing N N 278 
LYS   CG  HG3  sing N N 279 
LYS   CD  CE   sing N N 280 
LYS   CD  HD2  sing N N 281 
LYS   CD  HD3  sing N N 282 
LYS   CE  NZ   sing N N 283 
LYS   CE  HE2  sing N N 284 
LYS   CE  HE3  sing N N 285 
LYS   NZ  HZ1  sing N N 286 
LYS   NZ  HZ2  sing N N 287 
LYS   NZ  HZ3  sing N N 288 
LYS   OXT HXT  sing N N 289 
MET   N   CA   sing N N 290 
MET   N   H    sing N N 291 
MET   N   H2   sing N N 292 
MET   CA  C    sing N N 293 
MET   CA  CB   sing N N 294 
MET   CA  HA   sing N N 295 
MET   C   O    doub N N 296 
MET   C   OXT  sing N N 297 
MET   CB  CG   sing N N 298 
MET   CB  HB2  sing N N 299 
MET   CB  HB3  sing N N 300 
MET   CG  SD   sing N N 301 
MET   CG  HG2  sing N N 302 
MET   CG  HG3  sing N N 303 
MET   SD  CE   sing N N 304 
MET   CE  HE1  sing N N 305 
MET   CE  HE2  sing N N 306 
MET   CE  HE3  sing N N 307 
MET   OXT HXT  sing N N 308 
PHE   N   CA   sing N N 309 
PHE   N   H    sing N N 310 
PHE   N   H2   sing N N 311 
PHE   CA  C    sing N N 312 
PHE   CA  CB   sing N N 313 
PHE   CA  HA   sing N N 314 
PHE   C   O    doub N N 315 
PHE   C   OXT  sing N N 316 
PHE   CB  CG   sing N N 317 
PHE   CB  HB2  sing N N 318 
PHE   CB  HB3  sing N N 319 
PHE   CG  CD1  doub Y N 320 
PHE   CG  CD2  sing Y N 321 
PHE   CD1 CE1  sing Y N 322 
PHE   CD1 HD1  sing N N 323 
PHE   CD2 CE2  doub Y N 324 
PHE   CD2 HD2  sing N N 325 
PHE   CE1 CZ   doub Y N 326 
PHE   CE1 HE1  sing N N 327 
PHE   CE2 CZ   sing Y N 328 
PHE   CE2 HE2  sing N N 329 
PHE   CZ  HZ   sing N N 330 
PHE   OXT HXT  sing N N 331 
PRO   N   CA   sing N N 332 
PRO   N   CD   sing N N 333 
PRO   N   H    sing N N 334 
PRO   CA  C    sing N N 335 
PRO   CA  CB   sing N N 336 
PRO   CA  HA   sing N N 337 
PRO   C   O    doub N N 338 
PRO   C   OXT  sing N N 339 
PRO   CB  CG   sing N N 340 
PRO   CB  HB2  sing N N 341 
PRO   CB  HB3  sing N N 342 
PRO   CG  CD   sing N N 343 
PRO   CG  HG2  sing N N 344 
PRO   CG  HG3  sing N N 345 
PRO   CD  HD2  sing N N 346 
PRO   CD  HD3  sing N N 347 
PRO   OXT HXT  sing N N 348 
SER   N   CA   sing N N 349 
SER   N   H    sing N N 350 
SER   N   H2   sing N N 351 
SER   CA  C    sing N N 352 
SER   CA  CB   sing N N 353 
SER   CA  HA   sing N N 354 
SER   C   O    doub N N 355 
SER   C   OXT  sing N N 356 
SER   CB  OG   sing N N 357 
SER   CB  HB2  sing N N 358 
SER   CB  HB3  sing N N 359 
SER   OG  HG   sing N N 360 
SER   OXT HXT  sing N N 361 
THR   N   CA   sing N N 362 
THR   N   H    sing N N 363 
THR   N   H2   sing N N 364 
THR   CA  C    sing N N 365 
THR   CA  CB   sing N N 366 
THR   CA  HA   sing N N 367 
THR   C   O    doub N N 368 
THR   C   OXT  sing N N 369 
THR   CB  OG1  sing N N 370 
THR   CB  CG2  sing N N 371 
THR   CB  HB   sing N N 372 
THR   OG1 HG1  sing N N 373 
THR   CG2 HG21 sing N N 374 
THR   CG2 HG22 sing N N 375 
THR   CG2 HG23 sing N N 376 
THR   OXT HXT  sing N N 377 
TRP   N   CA   sing N N 378 
TRP   N   H    sing N N 379 
TRP   N   H2   sing N N 380 
TRP   CA  C    sing N N 381 
TRP   CA  CB   sing N N 382 
TRP   CA  HA   sing N N 383 
TRP   C   O    doub N N 384 
TRP   C   OXT  sing N N 385 
TRP   CB  CG   sing N N 386 
TRP   CB  HB2  sing N N 387 
TRP   CB  HB3  sing N N 388 
TRP   CG  CD1  doub Y N 389 
TRP   CG  CD2  sing Y N 390 
TRP   CD1 NE1  sing Y N 391 
TRP   CD1 HD1  sing N N 392 
TRP   CD2 CE2  doub Y N 393 
TRP   CD2 CE3  sing Y N 394 
TRP   NE1 CE2  sing Y N 395 
TRP   NE1 HE1  sing N N 396 
TRP   CE2 CZ2  sing Y N 397 
TRP   CE3 CZ3  doub Y N 398 
TRP   CE3 HE3  sing N N 399 
TRP   CZ2 CH2  doub Y N 400 
TRP   CZ2 HZ2  sing N N 401 
TRP   CZ3 CH2  sing Y N 402 
TRP   CZ3 HZ3  sing N N 403 
TRP   CH2 HH2  sing N N 404 
TRP   OXT HXT  sing N N 405 
TYR   N   CA   sing N N 406 
TYR   N   H    sing N N 407 
TYR   N   H2   sing N N 408 
TYR   CA  C    sing N N 409 
TYR   CA  CB   sing N N 410 
TYR   CA  HA   sing N N 411 
TYR   C   O    doub N N 412 
TYR   C   OXT  sing N N 413 
TYR   CB  CG   sing N N 414 
TYR   CB  HB2  sing N N 415 
TYR   CB  HB3  sing N N 416 
TYR   CG  CD1  doub Y N 417 
TYR   CG  CD2  sing Y N 418 
TYR   CD1 CE1  sing Y N 419 
TYR   CD1 HD1  sing N N 420 
TYR   CD2 CE2  doub Y N 421 
TYR   CD2 HD2  sing N N 422 
TYR   CE1 CZ   doub Y N 423 
TYR   CE1 HE1  sing N N 424 
TYR   CE2 CZ   sing Y N 425 
TYR   CE2 HE2  sing N N 426 
TYR   CZ  OH   sing N N 427 
TYR   OH  HH   sing N N 428 
TYR   OXT HXT  sing N N 429 
VAL   N   CA   sing N N 430 
VAL   N   H    sing N N 431 
VAL   N   H2   sing N N 432 
VAL   CA  C    sing N N 433 
VAL   CA  CB   sing N N 434 
VAL   CA  HA   sing N N 435 
VAL   C   O    doub N N 436 
VAL   C   OXT  sing N N 437 
VAL   CB  CG1  sing N N 438 
VAL   CB  CG2  sing N N 439 
VAL   CB  HB   sing N N 440 
VAL   CG1 HG11 sing N N 441 
VAL   CG1 HG12 sing N N 442 
VAL   CG1 HG13 sing N N 443 
VAL   CG2 HG21 sing N N 444 
VAL   CG2 HG22 sing N N 445 
VAL   CG2 HG23 sing N N 446 
VAL   OXT HXT  sing N N 447 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           AI143784 
_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   3RUX 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DRK 
_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]   0.015961 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014555 
_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]   0.008686 
_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 
H 
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   . MET   A 1 1   ? -11.002 9.302   25.771  1.00 53.50 ?  1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 1   ? -9.988  8.242   25.904  1.00 60.52 ?  1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 1   ? -9.720  7.829   27.317  1.00 62.90 ?  1   MET   A C   1 
ATOM   4    O O   . MET   A 1 1   ? -9.738  6.637   27.630  1.00 54.96 ?  1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 1   ? -8.653  8.646   25.292  1.00 63.19 ?  1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 1   ? -8.616  8.750   23.785  1.00 63.23 ?  1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 1   ? -9.063  7.240   22.922  1.00 87.24 ?  1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 1   ? -10.858 7.221   23.032  1.00 61.05 ?  1   MET   A CE  1 
ATOM   9    N N   . THR   A 1 2   ? -9.408  8.824   28.145  1.00 51.37 ?  2   THR   A N   1 
ATOM   10   C CA  . THR   A 1 2   ? -9.266  8.586   29.570  1.00 56.55 ?  2   THR   A CA  1 
ATOM   11   C C   . THR   A 1 2   ? -10.503 7.886   30.123  1.00 59.75 ?  2   THR   A C   1 
ATOM   12   O O   . THR   A 1 2   ? -10.395 7.029   31.010  1.00 56.65 ?  2   THR   A O   1 
ATOM   13   C CB  . THR   A 1 2   ? -9.006  9.923   30.276  1.00 59.46 ?  2   THR   A CB  1 
ATOM   14   O OG1 . THR   A 1 2   ? -8.024  10.655  29.531  1.00 63.16 ?  2   THR   A OG1 1 
ATOM   15   C CG2 . THR   A 1 2   ? -8.465  9.702   31.688  1.00 62.31 ?  2   THR   A CG2 1 
ATOM   16   N N   . ASP   A 1 3   ? -11.681 8.202   29.588  1.00 47.22 ?  3   ASP   A N   1 
ATOM   17   C CA  . ASP   A 1 3   ? -12.868 7.505   30.047  1.00 47.77 ?  3   ASP   A CA  1 
ATOM   18   C C   . ASP   A 1 3   ? -12.922 6.086   29.503  1.00 51.01 ?  3   ASP   A C   1 
ATOM   19   O O   . ASP   A 1 3   ? -13.464 5.195   30.163  1.00 45.94 ?  3   ASP   A O   1 
ATOM   20   C CB  . ASP   A 1 3   ? -14.129 8.276   29.650  1.00 52.69 ?  3   ASP   A CB  1 
ATOM   21   N N   . ARG   A 1 4   ? -12.373 5.845   28.310  1.00 48.90 ?  4   ARG   A N   1 
ATOM   22   C CA  . ARG   A 1 4   ? -12.517 4.505   27.756  1.00 48.11 ?  4   ARG   A CA  1 
ATOM   23   C C   . ARG   A 1 4   ? -11.702 3.502   28.550  1.00 45.30 ?  4   ARG   A C   1 
ATOM   24   O O   . ARG   A 1 4   ? -12.106 2.341   28.673  1.00 43.60 ?  4   ARG   A O   1 
ATOM   25   C CB  . ARG   A 1 4   ? -12.140 4.491   26.276  1.00 39.17 ?  4   ARG   A CB  1 
ATOM   26   C CG  . ARG   A 1 4   ? -13.300 4.873   25.400  1.00 43.85 ?  4   ARG   A CG  1 
ATOM   27   C CD  . ARG   A 1 4   ? -12.995 4.754   23.919  1.00 41.52 ?  4   ARG   A CD  1 
ATOM   28   N NE  . ARG   A 1 4   ? -14.011 5.445   23.127  1.00 36.09 ?  4   ARG   A NE  1 
ATOM   29   C CZ  . ARG   A 1 4   ? -14.326 5.133   21.875  1.00 39.13 ?  4   ARG   A CZ  1 
ATOM   30   N NH1 . ARG   A 1 4   ? -13.704 4.133   21.259  1.00 37.77 ?  4   ARG   A NH1 1 
ATOM   31   N NH2 . ARG   A 1 4   ? -15.268 5.815   21.241  1.00 32.62 ?  4   ARG   A NH2 1 
ATOM   32   N N   . ASP   A 1 5   ? -10.602 3.952   29.160  1.00 49.23 ?  5   ASP   A N   1 
ATOM   33   C CA  . ASP   A 1 5   ? -9.820  3.081   30.040  1.00 47.87 ?  5   ASP   A CA  1 
ATOM   34   C C   . ASP   A 1 5   ? -10.685 2.432   31.122  1.00 51.08 ?  5   ASP   A C   1 
ATOM   35   O O   . ASP   A 1 5   ? -10.461 1.270   31.495  1.00 49.04 ?  5   ASP   A O   1 
ATOM   36   C CB  . ASP   A 1 5   ? -8.685  3.867   30.688  1.00 45.58 ?  5   ASP   A CB  1 
ATOM   37   C CG  . ASP   A 1 5   ? -7.565  2.970   31.149  1.00 55.08 ?  5   ASP   A CG  1 
ATOM   38   O OD1 . ASP   A 1 5   ? -6.715  2.601   30.302  1.00 59.80 ?  5   ASP   A OD1 1 
ATOM   39   O OD2 . ASP   A 1 5   ? -7.574  2.597   32.342  1.00 57.30 -1 5   ASP   A OD2 1 
ATOM   40   N N   . ARG   A 1 6   ? -11.685 3.162   31.628  1.00 45.49 ?  6   ARG   A N   1 
ATOM   41   C CA  . ARG   A 1 6   ? -12.607 2.617   32.620  1.00 45.56 ?  6   ARG   A CA  1 
ATOM   42   C C   . ARG   A 1 6   ? -13.535 1.553   32.051  1.00 47.24 ?  6   ARG   A C   1 
ATOM   43   O O   . ARG   A 1 6   ? -14.230 0.885   32.824  1.00 52.16 ?  6   ARG   A O   1 
ATOM   44   C CB  . ARG   A 1 6   ? -13.434 3.744   33.233  1.00 48.98 ?  6   ARG   A CB  1 
ATOM   45   C CG  . ARG   A 1 6   ? -12.588 4.877   33.780  1.00 54.60 ?  6   ARG   A CG  1 
ATOM   46   C CD  . ARG   A 1 6   ? -13.419 5.835   34.611  1.00 58.75 ?  6   ARG   A CD  1 
ATOM   47   N NE  . ARG   A 1 6   ? -12.612 6.975   35.043  1.00 57.48 ?  6   ARG   A NE  1 
ATOM   48   C CZ  . ARG   A 1 6   ? -11.862 6.969   36.139  1.00 55.02 ?  6   ARG   A CZ  1 
ATOM   49   N NH1 . ARG   A 1 6   ? -11.836 5.889   36.918  1.00 52.95 ?  6   ARG   A NH1 1 
ATOM   50   N NH2 . ARG   A 1 6   ? -11.152 8.043   36.462  1.00 61.56 ?  6   ARG   A NH2 1 
ATOM   51   N N   . LEU   A 1 7   ? -13.581 1.389   30.729  1.00 47.98 ?  7   LEU   A N   1 
ATOM   52   C CA  . LEU   A 1 7   ? -14.318 0.299   30.102  1.00 45.44 ?  7   LEU   A CA  1 
ATOM   53   C C   . LEU   A 1 7   ? -13.386 -0.786  29.580  1.00 47.00 ?  7   LEU   A C   1 
ATOM   54   O O   . LEU   A 1 7   ? -13.807 -1.624  28.780  1.00 41.06 ?  7   LEU   A O   1 
ATOM   55   C CB  . LEU   A 1 7   ? -15.200 0.820   28.966  1.00 44.69 ?  7   LEU   A CB  1 
ATOM   56   C CG  . LEU   A 1 7   ? -15.923 2.155   29.173  1.00 52.29 ?  7   LEU   A CG  1 
ATOM   57   C CD1 . LEU   A 1 7   ? -16.747 2.528   27.939  1.00 49.66 ?  7   LEU   A CD1 1 
ATOM   58   C CD2 . LEU   A 1 7   ? -16.800 2.112   30.417  1.00 48.18 ?  7   LEU   A CD2 1 
ATOM   59   N N   . ARG   A 1 8   ? -12.123 -0.789  30.012  1.00 38.42 ?  8   ARG   A N   1 
ATOM   60   C CA  . ARG   A 1 8   ? -11.143 -1.779  29.568  1.00 46.08 ?  8   ARG   A CA  1 
ATOM   61   C C   . ARG   A 1 8   ? -10.588 -2.577  30.751  1.00 32.82 ?  8   ARG   A C   1 
ATOM   62   O O   . ARG   A 1 8   ? -9.404  -2.469  31.084  1.00 39.81 ?  8   ARG   A O   1 
ATOM   63   C CB  . ARG   A 1 8   ? -10.026 -1.094  28.782  1.00 36.85 ?  8   ARG   A CB  1 
ATOM   64   C CG  . ARG   A 1 8   ? -10.572 -0.272  27.624  1.00 37.27 ?  8   ARG   A CG  1 
ATOM   65   C CD  . ARG   A 1 8   ? -9.504  0.585   26.979  1.00 35.03 ?  8   ARG   A CD  1 
ATOM   66   N NE  . ARG   A 1 8   ? -9.999  1.090   25.713  1.00 32.64 ?  8   ARG   A NE  1 
ATOM   67   C CZ  . ARG   A 1 8   ? -9.387  1.995   24.970  1.00 35.31 ?  8   ARG   A CZ  1 
ATOM   68   N NH1 . ARG   A 1 8   ? -9.940  2.391   23.828  1.00 37.94 ?  8   ARG   A NH1 1 
ATOM   69   N NH2 . ARG   A 1 8   ? -8.219  2.487   25.361  1.00 34.93 ?  8   ARG   A NH2 1 
ATOM   70   N N   . PRO   A 1 9   ? -11.415 -3.413  31.387  1.00 39.18 ?  9   PRO   A N   1 
ATOM   71   C CA  . PRO   A 1 9   ? -10.881 -4.327  32.396  1.00 40.63 ?  9   PRO   A CA  1 
ATOM   72   C C   . PRO   A 1 9   ? -10.126 -5.449  31.741  1.00 44.16 ?  9   PRO   A C   1 
ATOM   73   O O   . PRO   A 1 9   ? -10.369 -5.790  30.564  1.00 34.87 ?  9   PRO   A O   1 
ATOM   74   C CB  . PRO   A 1 9   ? -12.151 -4.837  33.104  1.00 40.99 ?  9   PRO   A CB  1 
ATOM   75   C CG  . PRO   A 1 9   ? -13.153 -4.873  31.992  1.00 38.52 ?  9   PRO   A CG  1 
ATOM   76   C CD  . PRO   A 1 9   ? -12.834 -3.690  31.099  1.00 41.63 ?  9   PRO   A CD  1 
ATOM   77   N N   . PRO   A 1 10  ? -9.179  -6.083  32.441  1.00 45.87 ?  10  PRO   A N   1 
ATOM   78   C CA  . PRO   A 1 10  ? -8.386  -7.138  31.815  1.00 39.08 ?  10  PRO   A CA  1 
ATOM   79   C C   . PRO   A 1 10  ? -9.230  -8.381  31.610  1.00 38.95 ?  10  PRO   A C   1 
ATOM   80   O O   . PRO   A 1 10  ? -10.304 -8.540  32.191  1.00 33.64 ?  10  PRO   A O   1 
ATOM   81   C CB  . PRO   A 1 10  ? -7.261  -7.396  32.826  1.00 41.24 ?  10  PRO   A CB  1 
ATOM   82   C CG  . PRO   A 1 10  ? -7.879  -7.068  34.131  1.00 42.17 ?  10  PRO   A CG  1 
ATOM   83   C CD  . PRO   A 1 10  ? -8.905  -5.972  33.887  1.00 39.42 ?  10  PRO   A CD  1 
ATOM   84   N N   . LEU   A 1 11  ? -8.710  -9.270  30.766  1.00 39.38 ?  11  LEU   A N   1 
ATOM   85   C CA  . LEU   A 1 11  ? -9.309  -10.582 30.552  1.00 38.30 ?  11  LEU   A CA  1 
ATOM   86   C C   . LEU   A 1 11  ? -9.073  -11.507 31.741  1.00 40.98 ?  11  LEU   A C   1 
ATOM   87   O O   . LEU   A 1 11  ? -7.984  -11.538 32.319  1.00 41.26 ?  11  LEU   A O   1 
ATOM   88   C CB  . LEU   A 1 11  ? -8.720  -11.211 29.295  1.00 36.51 ?  11  LEU   A CB  1 
ATOM   89   C CG  . LEU   A 1 11  ? -8.920  -10.437 27.992  1.00 40.76 ?  11  LEU   A CG  1 
ATOM   90   C CD1 . LEU   A 1 11  ? -7.864  -10.841 26.990  1.00 42.33 ?  11  LEU   A CD1 1 
ATOM   91   C CD2 . LEU   A 1 11  ? -10.327 -10.680 27.436  1.00 39.46 ?  11  LEU   A CD2 1 
ATOM   92   N N   . ASP   A 1 12  ? -10.094 -12.289 32.087  1.00 43.39 ?  12  ASP   A N   1 
ATOM   93   C CA  . ASP   A 1 12  ? -9.944  -13.382 33.050  1.00 40.54 ?  12  ASP   A CA  1 
ATOM   94   C C   . ASP   A 1 12  ? -9.398  -14.604 32.314  1.00 42.88 ?  12  ASP   A C   1 
ATOM   95   O O   . ASP   A 1 12  ? -10.143 -15.338 31.651  1.00 43.70 ?  12  ASP   A O   1 
ATOM   96   C CB  . ASP   A 1 12  ? -11.274 -13.685 33.732  1.00 39.65 ?  12  ASP   A CB  1 
ATOM   97   C CG  . ASP   A 1 12  ? -11.134 -14.655 34.906  1.00 45.78 ?  12  ASP   A CG  1 
ATOM   98   O OD1 . ASP   A 1 12  ? -10.219 -15.510 34.911  1.00 44.83 ?  12  ASP   A OD1 1 
ATOM   99   O OD2 . ASP   A 1 12  ? -11.940 -14.558 35.855  1.00 49.52 -1 12  ASP   A OD2 1 
ATOM   100  N N   . GLU   A 1 13  ? -8.088  -14.834 32.444  1.00 40.37 ?  13  GLU   A N   1 
ATOM   101  C CA  . GLU   A 1 13  ? -7.462  -15.994 31.818  1.00 32.74 ?  13  GLU   A CA  1 
ATOM   102  C C   . GLU   A 1 13  ? -8.036  -17.302 32.359  1.00 37.94 ?  13  GLU   A C   1 
ATOM   103  O O   . GLU   A 1 13  ? -8.344  -18.227 31.593  1.00 35.14 ?  13  GLU   A O   1 
ATOM   104  C CB  . GLU   A 1 13  ? -5.951  -15.955 32.050  1.00 32.17 ?  13  GLU   A CB  1 
ATOM   105  C CG  . GLU   A 1 13  ? -5.230  -17.144 31.429  1.00 34.19 ?  13  GLU   A CG  1 
ATOM   106  C CD  . GLU   A 1 13  ? -3.771  -17.200 31.825  1.00 45.73 ?  13  GLU   A CD  1 
ATOM   107  O OE1 . GLU   A 1 13  ? -3.506  -17.337 33.038  1.00 53.79 ?  13  GLU   A OE1 1 
ATOM   108  O OE2 . GLU   A 1 13  ? -2.892  -17.094 30.934  1.00 40.30 -1 13  GLU   A OE2 1 
ATOM   109  N N   . ARG   A 1 14  ? -8.133  -17.418 33.685  1.00 36.94 ?  14  ARG   A N   1 
ATOM   110  C CA  . ARG   A 1 14  ? -8.678  -18.628 34.307  1.00 41.29 ?  14  ARG   A CA  1 
ATOM   111  C C   . ARG   A 1 14  ? -10.072 -18.943 33.779  1.00 42.55 ?  14  ARG   A C   1 
ATOM   112  O O   . ARG   A 1 14  ? -10.364 -20.079 33.393  1.00 39.91 ?  14  ARG   A O   1 
ATOM   113  C CB  . ARG   A 1 14  ? -8.719  -18.454 35.829  1.00 33.83 ?  14  ARG   A CB  1 
ATOM   114  C CG  . ARG   A 1 14  ? -9.125  -19.700 36.601  1.00 33.90 ?  14  ARG   A CG  1 
ATOM   115  N N   . SER   A 1 15  ? -10.948 -17.940 33.755  1.00 34.59 ?  15  SER   A N   1 
ATOM   116  C CA  . SER   A 1 15  ? -12.316 -18.165 33.309  1.00 41.79 ?  15  SER   A CA  1 
ATOM   117  C C   . SER   A 1 15  ? -12.371 -18.550 31.837  1.00 39.55 ?  15  SER   A C   1 
ATOM   118  O O   . SER   A 1 15  ? -13.120 -19.463 31.465  1.00 34.77 ?  15  SER   A O   1 
ATOM   119  C CB  . SER   A 1 15  ? -13.165 -16.927 33.574  1.00 39.44 ?  15  SER   A CB  1 
ATOM   120  O OG  . SER   A 1 15  ? -14.509 -17.172 33.251  1.00 43.08 ?  15  SER   A OG  1 
ATOM   121  N N   . LEU   A 1 16  ? -11.580 -17.876 30.991  1.00 31.92 ?  16  LEU   A N   1 
ATOM   122  C CA  . LEU   A 1 16  ? -11.514 -18.226 29.570  1.00 33.27 ?  16  LEU   A CA  1 
ATOM   123  C C   . LEU   A 1 16  ? -11.012 -19.657 29.346  1.00 35.55 ?  16  LEU   A C   1 
ATOM   124  O O   . LEU   A 1 16  ? -11.523 -20.375 28.480  1.00 40.61 ?  16  LEU   A O   1 
ATOM   125  C CB  . LEU   A 1 16  ? -10.611 -17.237 28.833  1.00 34.21 ?  16  LEU   A CB  1 
ATOM   126  C CG  . LEU   A 1 16  ? -11.190 -15.894 28.406  1.00 34.95 ?  16  LEU   A CG  1 
ATOM   127  C CD1 . LEU   A 1 16  ? -10.054 -15.041 27.817  1.00 36.85 ?  16  LEU   A CD1 1 
ATOM   128  C CD2 . LEU   A 1 16  ? -12.323 -16.097 27.404  1.00 36.61 ?  16  LEU   A CD2 1 
ATOM   129  N N   . ARG   A 1 17  ? -9.992  -20.084 30.085  1.00 34.76 ?  17  ARG   A N   1 
ATOM   130  C CA  . ARG   A 1 17  ? -9.542  -21.469 29.965  1.00 37.65 ?  17  ARG   A CA  1 
ATOM   131  C C   . ARG   A 1 17  ? -10.615 -22.445 30.410  1.00 35.78 ?  17  ARG   A C   1 
ATOM   132  O O   . ARG   A 1 17  ? -10.770 -23.524 29.826  1.00 36.15 ?  17  ARG   A O   1 
ATOM   133  C CB  . ARG   A 1 17  ? -8.309  -21.706 30.810  1.00 37.70 ?  17  ARG   A CB  1 
ATOM   134  C CG  . ARG   A 1 17  ? -7.076  -21.056 30.326  1.00 44.87 ?  17  ARG   A CG  1 
ATOM   135  C CD  . ARG   A 1 17  ? -5.996  -21.328 31.346  1.00 41.71 ?  17  ARG   A CD  1 
ATOM   136  N NE  . ARG   A 1 17  ? -4.701  -21.016 30.787  1.00 43.57 ?  17  ARG   A NE  1 
ATOM   137  C CZ  . ARG   A 1 17  ? -3.622  -20.806 31.517  1.00 46.37 ?  17  ARG   A CZ  1 
ATOM   138  N NH1 . ARG   A 1 17  ? -3.695  -20.909 32.842  1.00 44.54 ?  17  ARG   A NH1 1 
ATOM   139  N NH2 . ARG   A 1 17  ? -2.474  -20.520 30.919  1.00 41.75 ?  17  ARG   A NH2 1 
ATOM   140  N N   . ASP   A 1 18  ? -11.348 -22.093 31.458  1.00 35.96 ?  18  ASP   A N   1 
ATOM   141  C CA  . ASP   A 1 18  ? -12.427 -22.953 31.914  1.00 44.31 ?  18  ASP   A CA  1 
ATOM   142  C C   . ASP   A 1 18  ? -13.464 -23.150 30.814  1.00 44.47 ?  18  ASP   A C   1 
ATOM   143  O O   . ASP   A 1 18  ? -14.004 -24.248 30.644  1.00 45.15 ?  18  ASP   A O   1 
ATOM   144  C CB  . ASP   A 1 18  ? -13.056 -22.347 33.170  1.00 43.57 ?  18  ASP   A CB  1 
ATOM   145  C CG  . ASP   A 1 18  ? -12.163 -22.505 34.387  1.00 55.25 ?  18  ASP   A CG  1 
ATOM   146  O OD1 . ASP   A 1 18  ? -11.062 -23.094 34.237  1.00 58.91 ?  18  ASP   A OD1 1 
ATOM   147  O OD2 . ASP   A 1 18  ? -12.544 -22.030 35.483  1.00 64.95 -1 18  ASP   A OD2 1 
ATOM   148  N N   . GLN   A 1 19  ? -13.724 -22.106 30.028  1.00 38.81 ?  19  GLN   A N   1 
ATOM   149  C CA  . GLN   A 1 19  ? -14.752 -22.195 29.003  1.00 40.88 ?  19  GLN   A CA  1 
ATOM   150  C C   . GLN   A 1 19  ? -14.259 -22.873 27.732  1.00 42.03 ?  19  GLN   A C   1 
ATOM   151  O O   . GLN   A 1 19  ? -15.035 -23.548 27.055  1.00 43.44 ?  19  GLN   A O   1 
ATOM   152  C CB  . GLN   A 1 19  ? -15.267 -20.801 28.654  1.00 37.75 ?  19  GLN   A CB  1 
ATOM   153  C CG  . GLN   A 1 19  ? -15.767 -19.995 29.827  1.00 48.60 ?  19  GLN   A CG  1 
ATOM   154  C CD  . GLN   A 1 19  ? -16.015 -18.555 29.426  1.00 51.30 ?  19  GLN   A CD  1 
ATOM   155  O OE1 . GLN   A 1 19  ? -16.851 -18.279 28.563  1.00 41.50 ?  19  GLN   A OE1 1 
ATOM   156  N NE2 . GLN   A 1 19  ? -15.278 -17.629 30.039  1.00 54.35 ?  19  GLN   A NE2 1 
ATOM   157  N N   . LEU   A 1 20  ? -12.987 -22.702 27.380  1.00 38.04 ?  20  LEU   A N   1 
ATOM   158  C CA  . LEU   A 1 20  ? -12.528 -23.032 26.041  1.00 40.89 ?  20  LEU   A CA  1 
ATOM   159  C C   . LEU   A 1 20  ? -11.702 -24.306 25.943  1.00 37.39 ?  20  LEU   A C   1 
ATOM   160  O O   . LEU   A 1 20  ? -11.656 -24.898 24.865  1.00 42.44 ?  20  LEU   A O   1 
ATOM   161  C CB  . LEU   A 1 20  ? -11.728 -21.854 25.467  1.00 39.21 ?  20  LEU   A CB  1 
ATOM   162  C CG  . LEU   A 1 20  ? -12.601 -20.582 25.422  1.00 47.19 ?  20  LEU   A CG  1 
ATOM   163  C CD1 . LEU   A 1 20  ? -11.773 -19.298 25.329  1.00 41.85 ?  20  LEU   A CD1 1 
ATOM   164  C CD2 . LEU   A 1 20  ? -13.638 -20.656 24.294  1.00 39.86 ?  20  LEU   A CD2 1 
ATOM   165  N N   . ILE   A 1 21  ? -11.066 -24.746 27.018  1.00 33.63 ?  21  ILE   A N   1 
ATOM   166  C CA  . ILE   A 1 21  ? -10.200 -25.923 26.998  1.00 33.53 ?  21  ILE   A CA  1 
ATOM   167  C C   . ILE   A 1 21  ? -10.899 -27.044 27.748  1.00 35.58 ?  21  ILE   A C   1 
ATOM   168  O O   . ILE   A 1 21  ? -11.538 -26.805 28.777  1.00 44.59 ?  21  ILE   A O   1 
ATOM   169  C CB  . ILE   A 1 21  ? -8.828  -25.598 27.620  1.00 35.80 ?  21  ILE   A CB  1 
ATOM   170  C CG1 . ILE   A 1 21  ? -8.063  -24.654 26.679  1.00 33.82 ?  21  ILE   A CG1 1 
ATOM   171  C CG2 . ILE   A 1 21  ? -8.010  -26.845 27.854  1.00 37.72 ?  21  ILE   A CG2 1 
ATOM   172  C CD1 . ILE   A 1 21  ? -7.028  -23.830 27.394  1.00 40.75 ?  21  ILE   A CD1 1 
ATOM   173  N N   . GLY   A 1 22  ? -10.803 -28.257 27.223  1.00 48.29 ?  22  GLY   A N   1 
ATOM   174  C CA  . GLY   A 1 22  ? -11.425 -29.415 27.827  1.00 46.87 ?  22  GLY   A CA  1 
ATOM   175  C C   . GLY   A 1 22  ? -12.035 -30.330 26.776  1.00 44.49 ?  22  GLY   A C   1 
ATOM   176  O O   . GLY   A 1 22  ? -11.839 -30.159 25.575  1.00 46.98 ?  22  GLY   A O   1 
ATOM   177  N N   . ALA   A 1 23  ? -12.787 -31.319 27.249  1.00 41.76 ?  23  ALA   A N   1 
ATOM   178  C CA  . ALA   A 1 23  ? -13.332 -32.347 26.374  1.00 52.73 ?  23  ALA   A CA  1 
ATOM   179  C C   . ALA   A 1 23  ? -14.285 -31.737 25.352  1.00 47.90 ?  23  ALA   A C   1 
ATOM   180  O O   . ALA   A 1 23  ? -15.058 -30.828 25.663  1.00 48.80 ?  23  ALA   A O   1 
ATOM   181  C CB  . ALA   A 1 23  ? -14.052 -33.414 27.202  1.00 36.79 ?  23  ALA   A CB  1 
ATOM   182  N N   . GLY   A 1 24  ? -14.224 -32.255 24.123  1.00 47.32 ?  24  GLY   A N   1 
ATOM   183  C CA  . GLY   A 1 24  ? -15.000 -31.746 23.015  1.00 51.13 ?  24  GLY   A CA  1 
ATOM   184  C C   . GLY   A 1 24  ? -14.454 -30.489 22.369  1.00 52.74 ?  24  GLY   A C   1 
ATOM   185  O O   . GLY   A 1 24  ? -14.866 -30.154 21.251  1.00 52.69 ?  24  GLY   A O   1 
ATOM   186  N N   . SER   A 1 25  ? -13.547 -29.777 23.034  1.00 54.02 ?  25  SER   A N   1 
ATOM   187  C CA  . SER   A 1 25  ? -12.998 -28.532 22.510  1.00 50.77 ?  25  SER   A CA  1 
ATOM   188  C C   . SER   A 1 25  ? -11.713 -28.793 21.743  1.00 46.81 ?  25  SER   A C   1 
ATOM   189  O O   . SER   A 1 25  ? -10.826 -29.504 22.227  1.00 50.09 ?  25  SER   A O   1 
ATOM   190  C CB  . SER   A 1 25  ? -12.709 -27.549 23.638  1.00 45.06 ?  25  SER   A CB  1 
ATOM   191  O OG  . SER   A 1 25  ? -11.879 -26.517 23.152  1.00 42.62 ?  25  SER   A OG  1 
ATOM   192  N N   . GLY   A 1 26  ? -11.596 -28.173 20.571  1.00 48.59 ?  26  GLY   A N   1 
ATOM   193  C CA  . GLY   A 1 26  ? -10.362 -28.262 19.817  1.00 55.47 ?  26  GLY   A CA  1 
ATOM   194  C C   . GLY   A 1 26  ? -9.201  -27.491 20.411  1.00 52.88 ?  26  GLY   A C   1 
ATOM   195  O O   . GLY   A 1 26  ? -8.048  -27.820 20.114  1.00 50.55 ?  26  GLY   A O   1 
ATOM   196  N N   . TRP   A 1 27  ? -9.469  -26.480 21.242  1.00 37.89 ?  27  TRP   A N   1 
ATOM   197  C CA  . TRP   A 1 27  ? -8.378  -25.671 21.770  1.00 34.82 ?  27  TRP   A CA  1 
ATOM   198  C C   . TRP   A 1 27  ? -7.630  -26.445 22.847  1.00 40.31 ?  27  TRP   A C   1 
ATOM   199  O O   . TRP   A 1 27  ? -8.228  -26.938 23.804  1.00 36.98 ?  27  TRP   A O   1 
ATOM   200  C CB  . TRP   A 1 27  ? -8.901  -24.344 22.314  1.00 34.12 ?  27  TRP   A CB  1 
ATOM   201  C CG  . TRP   A 1 27  ? -9.692  -23.590 21.294  1.00 34.48 ?  27  TRP   A CG  1 
ATOM   202  C CD1 . TRP   A 1 27  ? -11.007 -23.222 21.375  1.00 39.61 ?  27  TRP   A CD1 1 
ATOM   203  C CD2 . TRP   A 1 27  ? -9.222  -23.127 20.026  1.00 35.43 ?  27  TRP   A CD2 1 
ATOM   204  N NE1 . TRP   A 1 27  ? -11.382 -22.542 20.232  1.00 33.76 ?  27  TRP   A NE1 1 
ATOM   205  C CE2 . TRP   A 1 27  ? -10.307 -22.471 19.389  1.00 32.02 ?  27  TRP   A CE2 1 
ATOM   206  C CE3 . TRP   A 1 27  ? -7.984  -23.191 19.364  1.00 32.35 ?  27  TRP   A CE3 1 
ATOM   207  C CZ2 . TRP   A 1 27  ? -10.195 -21.895 18.127  1.00 29.75 ?  27  TRP   A CZ2 1 
ATOM   208  C CZ3 . TRP   A 1 27  ? -7.872  -22.607 18.106  1.00 31.48 ?  27  TRP   A CZ3 1 
ATOM   209  C CH2 . TRP   A 1 27  ? -8.974  -21.972 17.501  1.00 36.95 ?  27  TRP   A CH2 1 
ATOM   210  N N   . ARG   A 1 28  ? -6.319  -26.557 22.679  1.00 33.04 ?  28  ARG   A N   1 
ATOM   211  C CA  . ARG   A 1 28  ? -5.481  -27.321 23.597  1.00 39.86 ?  28  ARG   A CA  1 
ATOM   212  C C   . ARG   A 1 28  ? -4.830  -26.461 24.669  1.00 39.56 ?  28  ARG   A C   1 
ATOM   213  O O   . ARG   A 1 28  ? -4.524  -26.970 25.750  1.00 38.52 ?  28  ARG   A O   1 
ATOM   214  C CB  . ARG   A 1 28  ? -4.384  -28.060 22.816  1.00 31.80 ?  28  ARG   A CB  1 
ATOM   215  N N   . GLN   A 1 29  ? -4.636  -25.170 24.406  1.00 37.20 ?  29  GLN   A N   1 
ATOM   216  C CA  . GLN   A 1 29  ? -3.875  -24.318 25.298  1.00 33.59 ?  29  GLN   A CA  1 
ATOM   217  C C   . GLN   A 1 29  ? -4.283  -22.875 25.034  1.00 36.56 ?  29  GLN   A C   1 
ATOM   218  O O   . GLN   A 1 29  ? -4.451  -22.474 23.876  1.00 31.84 ?  29  GLN   A O   1 
ATOM   219  C CB  . GLN   A 1 29  ? -2.366  -24.515 25.089  1.00 30.15 ?  29  GLN   A CB  1 
ATOM   220  C CG  . GLN   A 1 29  ? -1.502  -23.672 26.006  1.00 37.03 ?  29  GLN   A CG  1 
ATOM   221  C CD  . GLN   A 1 29  ? -0.020  -23.784 25.686  1.00 45.25 ?  29  GLN   A CD  1 
ATOM   222  O OE1 . GLN   A 1 29  ? 0.432   -24.787 25.116  1.00 45.83 ?  29  GLN   A OE1 1 
ATOM   223  N NE2 . GLN   A 1 29  ? 0.749   -22.756 26.059  1.00 36.38 ?  29  GLN   A NE2 1 
ATOM   224  N N   . LEU   A 1 30  ? -4.479  -22.115 26.109  1.00 30.39 ?  30  LEU   A N   1 
ATOM   225  C CA  . LEU   A 1 30  ? -4.746  -20.688 26.000  1.00 35.25 ?  30  LEU   A CA  1 
ATOM   226  C C   . LEU   A 1 30  ? -3.892  -19.985 27.035  1.00 39.04 ?  30  LEU   A C   1 
ATOM   227  O O   . LEU   A 1 30  ? -3.828  -20.430 28.181  1.00 39.16 ?  30  LEU   A O   1 
ATOM   228  C CB  . LEU   A 1 30  ? -6.226  -20.372 26.221  1.00 31.19 ?  30  LEU   A CB  1 
ATOM   229  C CG  . LEU   A 1 30  ? -6.766  -18.927 26.205  1.00 41.55 ?  30  LEU   A CG  1 
ATOM   230  C CD1 . LEU   A 1 30  ? -8.208  -18.906 25.692  1.00 31.33 ?  30  LEU   A CD1 1 
ATOM   231  C CD2 . LEU   A 1 30  ? -6.717  -18.246 27.592  1.00 37.07 ?  30  LEU   A CD2 1 
ATOM   232  N N   . ASP   A 1 31  ? -3.215  -18.918 26.625  1.00 40.68 ?  31  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31  ? -2.516  -18.043 27.550  1.00 34.15 ?  31  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31  ? -2.848  -16.598 27.216  1.00 33.13 ?  31  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31  ? -2.973  -16.230 26.042  1.00 33.64 ?  31  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31  ? -1.010  -18.256 27.500  1.00 35.51 ?  31  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31  ? -0.632  -19.717 27.615  1.00 44.65 ?  31  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31  ? -0.621  -20.262 28.760  1.00 41.66 ?  31  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31  ? -0.354  -20.310 26.546  1.00 45.20 -1 31  ASP   A OD2 1 
ATOM   240  N N   . VAL   A 1 32  ? -3.027  -15.797 28.256  1.00 36.64 ?  32  VAL   A N   1 
ATOM   241  C CA  . VAL   A 1 32  ? -3.148  -14.348 28.138  1.00 34.16 ?  32  VAL   A CA  1 
ATOM   242  C C   . VAL   A 1 32  ? -1.842  -13.755 28.645  1.00 39.67 ?  32  VAL   A C   1 
ATOM   243  O O   . VAL   A 1 32  ? -1.458  -13.988 29.797  1.00 45.45 ?  32  VAL   A O   1 
ATOM   244  C CB  . VAL   A 1 32  ? -4.349  -13.808 28.932  1.00 36.32 ?  32  VAL   A CB  1 
ATOM   245  C CG1 . VAL   A 1 32  ? -4.346  -12.283 28.942  1.00 38.00 ?  32  VAL   A CG1 1 
ATOM   246  C CG2 . VAL   A 1 32  ? -5.675  -14.328 28.357  1.00 26.87 ?  32  VAL   A CG2 1 
ATOM   247  N N   . VAL   A 1 33  ? -1.144  -13.008 27.795  1.00 39.74 ?  33  VAL   A N   1 
ATOM   248  C CA  . VAL   A 1 33  ? 0.051   -12.287 28.223  1.00 36.12 ?  33  VAL   A CA  1 
ATOM   249  C C   . VAL   A 1 33  ? -0.256  -10.794 28.302  1.00 39.22 ?  33  VAL   A C   1 
ATOM   250  O O   . VAL   A 1 33  ? -1.188  -10.284 27.667  1.00 33.62 ?  33  VAL   A O   1 
ATOM   251  C CB  . VAL   A 1 33  ? 1.252   -12.561 27.300  1.00 28.12 ?  33  VAL   A CB  1 
ATOM   252  C CG1 . VAL   A 1 33  ? 1.586   -14.071 27.331  1.00 38.45 ?  33  VAL   A CG1 1 
ATOM   253  C CG2 . VAL   A 1 33  ? 0.953   -12.121 25.886  1.00 29.00 ?  33  VAL   A CG2 1 
ATOM   254  N N   . ALA   A 1 34  ? 0.529   -10.094 29.120  1.00 33.07 ?  34  ALA   A N   1 
ATOM   255  C CA  . ALA   A 1 34  ? 0.311   -8.670  29.301  1.00 35.90 ?  34  ALA   A CA  1 
ATOM   256  C C   . ALA   A 1 34  ? 0.660   -7.911  28.034  1.00 36.18 ?  34  ALA   A C   1 
ATOM   257  O O   . ALA   A 1 34  ? -0.063  -6.994  27.634  1.00 33.00 ?  34  ALA   A O   1 
ATOM   258  C CB  . ALA   A 1 34  ? 1.135   -8.152  30.480  1.00 36.19 ?  34  ALA   A CB  1 
ATOM   259  N N   . GLN   A 1 35  ? 1.738   -8.306  27.366  1.00 36.57 ?  35  GLN   A N   1 
ATOM   260  C CA  . GLN   A 1 35  ? 2.265   -7.486  26.291  1.00 32.60 ?  35  GLN   A CA  1 
ATOM   261  C C   . GLN   A 1 35  ? 3.135   -8.353  25.410  1.00 39.28 ?  35  GLN   A C   1 
ATOM   262  O O   . GLN   A 1 35  ? 3.846   -9.228  25.904  1.00 37.83 ?  35  GLN   A O   1 
ATOM   263  C CB  . GLN   A 1 35  ? 3.073   -6.318  26.860  1.00 36.94 ?  35  GLN   A CB  1 
ATOM   264  C CG  . GLN   A 1 35  ? 3.484   -5.295  25.860  1.00 41.98 ?  35  GLN   A CG  1 
ATOM   265  C CD  . GLN   A 1 35  ? 4.091   -4.049  26.508  1.00 43.94 ?  35  GLN   A CD  1 
ATOM   266  O OE1 . GLN   A 1 35  ? 3.678   -3.611  27.588  1.00 38.76 ?  35  GLN   A OE1 1 
ATOM   267  N NE2 . GLN   A 1 35  ? 5.086   -3.491  25.853  1.00 40.38 ?  35  GLN   A NE2 1 
ATOM   268  N N   . THR   A 1 36  ? 3.073   -8.112  24.107  1.00 34.72 ?  36  THR   A N   1 
ATOM   269  C CA  . THR   A 1 36  ? 4.048   -8.706  23.217  1.00 33.75 ?  36  THR   A CA  1 
ATOM   270  C C   . THR   A 1 36  ? 4.192   -7.825  21.989  1.00 38.68 ?  36  THR   A C   1 
ATOM   271  O O   . THR   A 1 36  ? 3.402   -6.905  21.765  1.00 35.47 ?  36  THR   A O   1 
ATOM   272  C CB  . THR   A 1 36  ? 3.656   -10.122 22.823  1.00 40.22 ?  36  THR   A CB  1 
ATOM   273  O OG1 . THR   A 1 36  ? 4.726   -10.682 22.050  1.00 43.40 ?  36  THR   A OG1 1 
ATOM   274  C CG2 . THR   A 1 36  ? 2.344   -10.097 21.997  1.00 29.58 ?  36  THR   A CG2 1 
ATOM   275  N N   . GLY   A 1 37  ? 5.226   -8.111  21.195  1.00 34.12 ?  37  GLY   A N   1 
ATOM   276  C CA  . GLY   A 1 37  ? 5.397   -7.385  19.951  1.00 35.95 ?  37  GLY   A CA  1 
ATOM   277  C C   . GLY   A 1 37  ? 4.349   -7.782  18.930  1.00 42.71 ?  37  GLY   A C   1 
ATOM   278  O O   . GLY   A 1 37  ? 3.692   -6.930  18.323  1.00 35.34 ?  37  GLY   A O   1 
ATOM   279  N N   . SER   A 1 38  ? 4.155   -9.085  18.752  1.00 37.33 ?  38  SER   A N   1 
ATOM   280  C CA  . SER   A 1 38  ? 3.128   -9.556  17.841  1.00 31.49 ?  38  SER   A CA  1 
ATOM   281  C C   . SER   A 1 38  ? 2.757   -10.978 18.227  1.00 36.63 ?  38  SER   A C   1 
ATOM   282  O O   . SER   A 1 38  ? 3.630   -11.844 18.322  1.00 35.41 ?  38  SER   A O   1 
ATOM   283  C CB  . SER   A 1 38  ? 3.630   -9.471  16.397  1.00 31.43 ?  38  SER   A CB  1 
ATOM   284  O OG  . SER   A 1 38  ? 2.846   -10.264 15.535  1.00 40.90 ?  38  SER   A OG  1 
ATOM   285  N N   . THR   A 1 39  ? 1.466   -11.226 18.449  1.00 36.76 ?  39  THR   A N   1 
ATOM   286  C CA  . THR   A 1 39  ? 1.065   -12.598 18.772  1.00 33.14 ?  39  THR   A CA  1 
ATOM   287  C C   . THR   A 1 39  ? 1.337   -13.545 17.611  1.00 31.61 ?  39  THR   A C   1 
ATOM   288  O O   . THR   A 1 39  ? 1.623   -14.732 17.826  1.00 35.41 ?  39  THR   A O   1 
ATOM   289  C CB  . THR   A 1 39  ? -0.411  -12.653 19.165  1.00 30.94 ?  39  THR   A CB  1 
ATOM   290  O OG1 . THR   A 1 39  ? -1.214  -12.157 18.088  1.00 29.04 ?  39  THR   A OG1 1 
ATOM   291  C CG2 . THR   A 1 39  ? -0.670  -11.809 20.399  1.00 28.23 ?  39  THR   A CG2 1 
ATOM   292  N N   . ASN   A 1 40  ? 1.255   -13.051 16.378  1.00 28.91 ?  40  ASN   A N   1 
ATOM   293  C CA  . ASN   A 1 40  ? 1.602   -13.888 15.236  1.00 30.79 ?  40  ASN   A CA  1 
ATOM   294  C C   . ASN   A 1 40  ? 3.074   -14.259 15.277  1.00 35.36 ?  40  ASN   A C   1 
ATOM   295  O O   . ASN   A 1 40  ? 3.428   -15.438 15.163  1.00 38.52 ?  40  ASN   A O   1 
ATOM   296  C CB  . ASN   A 1 40  ? 1.271   -13.177 13.926  1.00 33.65 ?  40  ASN   A CB  1 
ATOM   297  C CG  . ASN   A 1 40  ? -0.077  -13.600 13.365  1.00 39.17 ?  40  ASN   A CG  1 
ATOM   298  O OD1 . ASN   A 1 40  ? -0.967  -14.001 14.114  1.00 37.21 ?  40  ASN   A OD1 1 
ATOM   299  N ND2 . ASN   A 1 40  ? -0.241  -13.489 12.055  1.00 31.41 ?  40  ASN   A ND2 1 
ATOM   300  N N   . ALA   A 1 41  ? 3.946   -13.260 15.451  1.00 34.79 ?  41  ALA   A N   1 
ATOM   301  C CA  . ALA   A 1 41  ? 5.376   -13.523 15.546  1.00 38.81 ?  41  ALA   A CA  1 
ATOM   302  C C   . ALA   A 1 41  ? 5.667   -14.532 16.645  1.00 33.79 ?  41  ALA   A C   1 
ATOM   303  O O   . ALA   A 1 41  ? 6.511   -15.418 16.476  1.00 33.60 ?  41  ALA   A O   1 
ATOM   304  C CB  . ALA   A 1 41  ? 6.138   -12.212 15.792  1.00 35.65 ?  41  ALA   A CB  1 
ATOM   305  N N   . ASP   A 1 42  ? 4.927   -14.457 17.754  1.00 36.97 ?  42  ASP   A N   1 
ATOM   306  C CA  . ASP   A 1 42  ? 5.228   -15.306 18.900  1.00 34.54 ?  42  ASP   A CA  1 
ATOM   307  C C   . ASP   A 1 42  ? 4.874   -16.769 18.631  1.00 35.90 ?  42  ASP   A C   1 
ATOM   308  O O   . ASP   A 1 42  ? 5.658   -17.671 18.957  1.00 28.75 ?  42  ASP   A O   1 
ATOM   309  C CB  . ASP   A 1 42  ? 4.484   -14.807 20.129  1.00 33.56 ?  42  ASP   A CB  1 
ATOM   310  C CG  . ASP   A 1 42  ? 5.129   -13.562 20.736  1.00 46.83 ?  42  ASP   A CG  1 
ATOM   311  O OD1 . ASP   A 1 42  ? 6.140   -13.088 20.163  1.00 47.33 ?  42  ASP   A OD1 1 
ATOM   312  O OD2 . ASP   A 1 42  ? 4.640   -13.085 21.796  1.00 44.92 -1 42  ASP   A OD2 1 
ATOM   313  N N   . LEU   A 1 43  ? 3.692   -17.031 18.055  1.00 33.24 ?  43  LEU   A N   1 
ATOM   314  C CA  . LEU   A 1 43  ? 3.330   -18.408 17.731  1.00 33.27 ?  43  LEU   A CA  1 
ATOM   315  C C   . LEU   A 1 43  ? 4.171   -18.935 16.580  1.00 37.29 ?  43  LEU   A C   1 
ATOM   316  O O   . LEU   A 1 43  ? 4.434   -20.141 16.508  1.00 32.48 ?  43  LEU   A O   1 
ATOM   317  C CB  . LEU   A 1 43  ? 1.839   -18.517 17.382  1.00 32.99 ?  43  LEU   A CB  1 
ATOM   318  C CG  . LEU   A 1 43  ? 0.849   -18.456 18.544  1.00 35.64 ?  43  LEU   A CG  1 
ATOM   319  C CD1 . LEU   A 1 43  ? -0.560  -18.917 18.117  1.00 31.60 ?  43  LEU   A CD1 1 
ATOM   320  C CD2 . LEU   A 1 43  ? 1.357   -19.258 19.730  1.00 27.01 ?  43  LEU   A CD2 1 
ATOM   321  N N   . LEU   A 1 44  ? 4.593   -18.057 15.662  1.00 31.20 ?  44  LEU   A N   1 
ATOM   322  C CA  . LEU   A 1 44  ? 5.486   -18.516 14.600  1.00 35.47 ?  44  LEU   A CA  1 
ATOM   323  C C   . LEU   A 1 44  ? 6.838   -18.909 15.171  1.00 33.54 ?  44  LEU   A C   1 
ATOM   324  O O   . LEU   A 1 44  ? 7.438   -19.901 14.732  1.00 32.29 ?  44  LEU   A O   1 
ATOM   325  C CB  . LEU   A 1 44  ? 5.656   -17.439 13.528  1.00 38.63 ?  44  LEU   A CB  1 
ATOM   326  C CG  . LEU   A 1 44  ? 4.443   -17.071 12.667  1.00 39.06 ?  44  LEU   A CG  1 
ATOM   327  C CD1 . LEU   A 1 44  ? 4.601   -15.663 12.122  1.00 34.12 ?  44  LEU   A CD1 1 
ATOM   328  C CD2 . LEU   A 1 44  ? 4.276   -18.065 11.528  1.00 33.72 ?  44  LEU   A CD2 1 
ATOM   329  N N   . ALA   A 1 45  ? 7.326   -18.147 16.158  1.00 32.60 ?  45  ALA   A N   1 
ATOM   330  C CA  . ALA   A 1 45  ? 8.584   -18.487 16.818  1.00 41.01 ?  45  ALA   A CA  1 
ATOM   331  C C   . ALA   A 1 45  ? 8.480   -19.826 17.549  1.00 34.58 ?  45  ALA   A C   1 
ATOM   332  O O   . ALA   A 1 45  ? 9.389   -20.661 17.469  1.00 40.34 ?  45  ALA   A O   1 
ATOM   333  C CB  . ALA   A 1 45  ? 8.992   -17.360 17.777  1.00 30.41 ?  45  ALA   A CB  1 
ATOM   334  N N   . ARG   A 1 46  ? 7.375   -20.054 18.257  1.00 31.26 ?  46  ARG   A N   1 
ATOM   335  C CA  . ARG   A 1 46  ? 7.121   -21.362 18.851  1.00 31.84 ?  46  ARG   A CA  1 
ATOM   336  C C   . ARG   A 1 46  ? 7.235   -22.481 17.829  1.00 37.53 ?  46  ARG   A C   1 
ATOM   337  O O   . ARG   A 1 46  ? 7.908   -23.489 18.077  1.00 32.65 ?  46  ARG   A O   1 
ATOM   338  C CB  . ARG   A 1 46  ? 5.737   -21.390 19.493  1.00 29.97 ?  46  ARG   A CB  1 
ATOM   339  C CG  . ARG   A 1 46  ? 5.688   -20.761 20.847  1.00 33.61 ?  46  ARG   A CG  1 
ATOM   340  C CD  . ARG   A 1 46  ? 4.418   -21.161 21.605  1.00 31.18 ?  46  ARG   A CD  1 
ATOM   341  N NE  . ARG   A 1 46  ? 3.966   -19.997 22.364  1.00 30.98 ?  46  ARG   A NE  1 
ATOM   342  C CZ  . ARG   A 1 46  ? 2.811   -19.907 23.009  1.00 37.79 ?  46  ARG   A CZ  1 
ATOM   343  N NH1 . ARG   A 1 46  ? 2.506   -18.791 23.662  1.00 38.02 ?  46  ARG   A NH1 1 
ATOM   344  N NH2 . ARG   A 1 46  ? 1.950   -20.916 22.980  1.00 35.34 ?  46  ARG   A NH2 1 
ATOM   345  N N   . ALA   A 1 47  ? 6.566   -22.335 16.677  1.00 32.81 ?  47  ALA   A N   1 
ATOM   346  C CA  . ALA   A 1 47  ? 6.570   -23.432 15.710  1.00 35.24 ?  47  ALA   A CA  1 
ATOM   347  C C   . ALA   A 1 47  ? 7.942   -23.610 15.080  1.00 34.70 ?  47  ALA   A C   1 
ATOM   348  O O   . ALA   A 1 47  ? 8.358   -24.738 14.807  1.00 39.64 ?  47  ALA   A O   1 
ATOM   349  C CB  . ALA   A 1 47  ? 5.530   -23.200 14.618  1.00 37.26 ?  47  ALA   A CB  1 
ATOM   350  N N   . ALA   A 1 48  ? 8.662   -22.517 14.849  1.00 29.66 ?  48  ALA   A N   1 
ATOM   351  C CA  . ALA   A 1 48  ? 9.990   -22.643 14.288  1.00 31.13 ?  48  ALA   A CA  1 
ATOM   352  C C   . ALA   A 1 48  ? 10.936  -23.375 15.236  1.00 36.66 ?  48  ALA   A C   1 
ATOM   353  O O   . ALA   A 1 48  ? 11.956  -23.899 14.784  1.00 43.55 ?  48  ALA   A O   1 
ATOM   354  C CB  . ALA   A 1 48  ? 10.529  -21.257 13.921  1.00 26.22 ?  48  ALA   A CB  1 
ATOM   355  N N   . SER   A 1 49  ? 10.615  -23.444 16.530  1.00 40.41 ?  49  SER   A N   1 
ATOM   356  C CA  . SER   A 1 49  ? 11.414  -24.206 17.487  1.00 45.16 ?  49  SER   A CA  1 
ATOM   357  C C   . SER   A 1 49  ? 10.895  -25.611 17.731  1.00 44.24 ?  49  SER   A C   1 
ATOM   358  O O   . SER   A 1 49  ? 11.413  -26.292 18.617  1.00 51.63 ?  49  SER   A O   1 
ATOM   359  C CB  . SER   A 1 49  ? 11.510  -23.473 18.816  1.00 43.85 ?  49  SER   A CB  1 
ATOM   360  O OG  . SER   A 1 49  ? 12.027  -22.185 18.603  1.00 57.81 ?  49  SER   A OG  1 
ATOM   361  N N   . GLY   A 1 50  ? 9.912   -26.069 16.963  1.00 36.25 ?  50  GLY   A N   1 
ATOM   362  C CA  . GLY   A 1 50  ? 9.455   -27.433 17.037  1.00 34.81 ?  50  GLY   A CA  1 
ATOM   363  C C   . GLY   A 1 50  ? 8.173   -27.638 17.814  1.00 39.94 ?  50  GLY   A C   1 
ATOM   364  O O   . GLY   A 1 50  ? 7.646   -28.753 17.807  1.00 40.71 ?  50  GLY   A O   1 
ATOM   365  N N   . ALA   A 1 51  ? 7.655   -26.610 18.475  1.00 37.63 ?  51  ALA   A N   1 
ATOM   366  C CA  . ALA   A 1 51  ? 6.459   -26.787 19.288  1.00 40.09 ?  51  ALA   A CA  1 
ATOM   367  C C   . ALA   A 1 51  ? 5.264   -27.159 18.412  1.00 38.83 ?  51  ALA   A C   1 
ATOM   368  O O   . ALA   A 1 51  ? 5.173   -26.782 17.237  1.00 39.44 ?  51  ALA   A O   1 
ATOM   369  C CB  . ALA   A 1 51  ? 6.161   -25.513 20.096  1.00 33.13 ?  51  ALA   A CB  1 
ATOM   370  N N   . ASP   A 1 52  ? 4.357   -27.951 18.969  1.00 39.05 ?  52  ASP   A N   1 
ATOM   371  C CA  . ASP   A 1 52  ? 3.104   -28.242 18.282  1.00 44.02 ?  52  ASP   A CA  1 
ATOM   372  C C   . ASP   A 1 52  ? 2.104   -27.167 18.694  1.00 40.00 ?  52  ASP   A C   1 
ATOM   373  O O   . ASP   A 1 52  ? 1.659   -27.134 19.846  1.00 46.26 ?  52  ASP   A O   1 
ATOM   374  C CB  . ASP   A 1 52  ? 2.609   -29.644 18.618  1.00 40.86 ?  52  ASP   A CB  1 
ATOM   375  C CG  . ASP   A 1 52  ? 1.361   -30.020 17.845  1.00 51.60 ?  52  ASP   A CG  1 
ATOM   376  O OD1 . ASP   A 1 52  ? 1.018   -29.303 16.880  1.00 52.10 ?  52  ASP   A OD1 1 
ATOM   377  O OD2 . ASP   A 1 52  ? 0.727   -31.042 18.193  1.00 53.60 -1 52  ASP   A OD2 1 
ATOM   378  N N   . ILE   A 1 53  ? 1.786   -26.258 17.774  1.00 40.38 ?  53  ILE   A N   1 
ATOM   379  C CA  . ILE   A 1 53  ? 0.888   -25.149 18.085  1.00 34.93 ?  53  ILE   A CA  1 
ATOM   380  C C   . ILE   A 1 53  ? -0.521  -25.388 17.556  1.00 33.73 ?  53  ILE   A C   1 
ATOM   381  O O   . ILE   A 1 53  ? -1.321  -24.448 17.506  1.00 33.40 ?  53  ILE   A O   1 
ATOM   382  C CB  . ILE   A 1 53  ? 1.441   -23.806 17.567  1.00 34.82 ?  53  ILE   A CB  1 
ATOM   383  C CG1 . ILE   A 1 53  ? 1.530   -23.807 16.043  1.00 34.64 ?  53  ILE   A CG1 1 
ATOM   384  C CG2 . ILE   A 1 53  ? 2.815   -23.491 18.188  1.00 35.47 ?  53  ILE   A CG2 1 
ATOM   385  C CD1 . ILE   A 1 53  ? 1.807   -22.433 15.446  1.00 35.27 ?  53  ILE   A CD1 1 
ATOM   386  N N   . ASP   A 1 54  ? -0.844  -26.610 17.127  1.00 29.95 ?  54  ASP   A N   1 
ATOM   387  C CA  . ASP   A 1 54  ? -2.196  -26.863 16.642  1.00 31.64 ?  54  ASP   A CA  1 
ATOM   388  C C   . ASP   A 1 54  ? -3.187  -26.733 17.800  1.00 30.45 ?  54  ASP   A C   1 
ATOM   389  O O   . ASP   A 1 54  ? -3.047  -27.401 18.830  1.00 32.85 ?  54  ASP   A O   1 
ATOM   390  C CB  . ASP   A 1 54  ? -2.293  -28.236 15.986  1.00 38.59 ?  54  ASP   A CB  1 
ATOM   391  C CG  . ASP   A 1 54  ? -3.664  -28.485 15.357  1.00 47.06 ?  54  ASP   A CG  1 
ATOM   392  O OD1 . ASP   A 1 54  ? -4.043  -27.769 14.387  1.00 45.96 ?  54  ASP   A OD1 1 
ATOM   393  O OD2 . ASP   A 1 54  ? -4.369  -29.391 15.843  1.00 52.49 -1 54  ASP   A OD2 1 
ATOM   394  N N   . GLY   A 1 55  ? -4.155  -25.823 17.664  1.00 32.76 ?  55  GLY   A N   1 
ATOM   395  C CA  . GLY   A 1 55  ? -5.116  -25.597 18.739  1.00 32.20 ?  55  GLY   A CA  1 
ATOM   396  C C   . GLY   A 1 55  ? -4.571  -24.822 19.922  1.00 41.41 ?  55  GLY   A C   1 
ATOM   397  O O   . GLY   A 1 55  ? -5.167  -24.846 21.016  1.00 28.06 ?  55  GLY   A O   1 
ATOM   398  N N   . VAL   A 1 56  ? -3.447  -24.140 19.740  1.00 29.29 ?  56  VAL   A N   1 
ATOM   399  C CA  . VAL   A 1 56  ? -2.894  -23.279 20.768  1.00 32.78 ?  56  VAL   A CA  1 
ATOM   400  C C   . VAL   A 1 56  ? -3.379  -21.855 20.530  1.00 26.11 ?  56  VAL   A C   1 
ATOM   401  O O   . VAL   A 1 56  ? -3.369  -21.357 19.395  1.00 33.52 ?  56  VAL   A O   1 
ATOM   402  C CB  . VAL   A 1 56  ? -1.361  -23.360 20.767  1.00 27.96 ?  56  VAL   A CB  1 
ATOM   403  C CG1 . VAL   A 1 56  ? -0.779  -22.287 21.636  1.00 25.10 ?  56  VAL   A CG1 1 
ATOM   404  C CG2 . VAL   A 1 56  ? -0.941  -24.761 21.228  1.00 29.48 ?  56  VAL   A CG2 1 
ATOM   405  N N   . VAL   A 1 57  ? -3.816  -21.201 21.597  1.00 32.92 ?  57  VAL   A N   1 
ATOM   406  C CA  . VAL   A 1 57  ? -4.332  -19.842 21.542  1.00 28.56 ?  57  VAL   A CA  1 
ATOM   407  C C   . VAL   A 1 57  ? -3.401  -18.945 22.340  1.00 28.04 ?  57  VAL   A C   1 
ATOM   408  O O   . VAL   A 1 57  ? -3.063  -19.257 23.485  1.00 32.43 ?  57  VAL   A O   1 
ATOM   409  C CB  . VAL   A 1 57  ? -5.757  -19.759 22.110  1.00 33.71 ?  57  VAL   A CB  1 
ATOM   410  C CG1 . VAL   A 1 57  ? -6.330  -18.357 21.884  1.00 26.18 ?  57  VAL   A CG1 1 
ATOM   411  C CG2 . VAL   A 1 57  ? -6.630  -20.866 21.495  1.00 33.14 ?  57  VAL   A CG2 1 
ATOM   412  N N   . LEU   A 1 58  ? -3.001  -17.827 21.749  1.00 28.26 ?  58  LEU   A N   1 
ATOM   413  C CA  . LEU   A 1 58  ? -2.257  -16.800 22.464  1.00 27.33 ?  58  LEU   A CA  1 
ATOM   414  C C   . LEU   A 1 58  ? -3.023  -15.490 22.356  1.00 28.24 ?  58  LEU   A C   1 
ATOM   415  O O   . LEU   A 1 58  ? -3.243  -14.989 21.245  1.00 30.93 ?  58  LEU   A O   1 
ATOM   416  C CB  . LEU   A 1 58  ? -0.838  -16.656 21.902  1.00 28.87 ?  58  LEU   A CB  1 
ATOM   417  C CG  . LEU   A 1 58  ? 0.035   -15.532 22.473  1.00 35.22 ?  58  LEU   A CG  1 
ATOM   418  C CD1 . LEU   A 1 58  ? 0.432   -15.799 23.904  1.00 29.78 ?  58  LEU   A CD1 1 
ATOM   419  C CD2 . LEU   A 1 58  ? 1.283   -15.339 21.607  1.00 34.67 ?  58  LEU   A CD2 1 
ATOM   420  N N   . ILE   A 1 59  ? -3.445  -14.960 23.499  1.00 27.57 ?  59  ILE   A N   1 
ATOM   421  C CA  . ILE   A 1 59  ? -4.104  -13.658 23.602  1.00 25.16 ?  59  ILE   A CA  1 
ATOM   422  C C   . ILE   A 1 59  ? -3.125  -12.697 24.270  1.00 34.80 ?  59  ILE   A C   1 
ATOM   423  O O   . ILE   A 1 59  ? -2.417  -13.073 25.219  1.00 32.17 ?  59  ILE   A O   1 
ATOM   424  C CB  . ILE   A 1 59  ? -5.426  -13.749 24.405  1.00 24.01 ?  59  ILE   A CB  1 
ATOM   425  C CG1 . ILE   A 1 59  ? -6.311  -14.866 23.842  1.00 24.36 ?  59  ILE   A CG1 1 
ATOM   426  C CG2 . ILE   A 1 59  ? -6.189  -12.436 24.349  1.00 25.37 ?  59  ILE   A CG2 1 
ATOM   427  C CD1 . ILE   A 1 59  ? -7.266  -15.449 24.817  1.00 24.72 ?  59  ILE   A CD1 1 
ATOM   428  N N   . ALA   A 1 60  ? -3.077  -11.463 23.773  1.00 27.62 ?  60  ALA   A N   1 
ATOM   429  C CA  . ALA   A 1 60  ? -2.237  -10.418 24.344  1.00 26.16 ?  60  ALA   A CA  1 
ATOM   430  C C   . ALA   A 1 60  ? -3.109  -9.236  24.753  1.00 29.92 ?  60  ALA   A C   1 
ATOM   431  O O   . ALA   A 1 60  ? -3.893  -8.732  23.945  1.00 31.92 ?  60  ALA   A O   1 
ATOM   432  C CB  . ALA   A 1 60  ? -1.170  -9.968  23.334  1.00 24.98 ?  60  ALA   A CB  1 
ATOM   433  N N   . GLU   A 1 61  ? -2.966  -8.789  25.998  1.00 30.53 ?  61  GLU   A N   1 
ATOM   434  C CA  . GLU   A 1 61  ? -3.660  -7.585  26.448  1.00 29.32 ?  61  GLU   A CA  1 
ATOM   435  C C   . GLU   A 1 61  ? -3.234  -6.365  25.644  1.00 38.72 ?  61  GLU   A C   1 
ATOM   436  O O   . GLU   A 1 61  ? -4.051  -5.463  25.389  1.00 34.20 ?  61  GLU   A O   1 
ATOM   437  C CB  . GLU   A 1 61  ? -3.395  -7.369  27.939  1.00 33.83 ?  61  GLU   A CB  1 
ATOM   438  C CG  . GLU   A 1 61  ? -4.186  -8.324  28.858  1.00 42.45 ?  61  GLU   A CG  1 
ATOM   439  C CD  . GLU   A 1 61  ? -5.714  -8.110  28.830  1.00 50.37 ?  61  GLU   A CD  1 
ATOM   440  O OE1 . GLU   A 1 61  ? -6.383  -8.615  29.765  1.00 51.21 ?  61  GLU   A OE1 1 
ATOM   441  O OE2 . GLU   A 1 61  ? -6.242  -7.417  27.921  1.00 48.25 -1 61  GLU   A OE2 1 
ATOM   442  N N   . HIS   A 1 62  ? -1.971  -6.328  25.227  1.00 33.09 ?  62  HIS   A N   1 
ATOM   443  C CA  A HIS   A 1 62  ? -1.414  -5.217  24.475  0.80 33.33 ?  62  HIS   A CA  1 
ATOM   444  C CA  B HIS   A 1 62  ? -1.426  -5.219  24.463  0.20 33.39 ?  62  HIS   A CA  1 
ATOM   445  C C   . HIS   A 1 62  ? -0.459  -5.760  23.421  1.00 32.20 ?  62  HIS   A C   1 
ATOM   446  O O   . HIS   A 1 62  ? 0.189   -6.792  23.624  1.00 33.38 ?  62  HIS   A O   1 
ATOM   447  C CB  A HIS   A 1 62  ? -0.695  -4.241  25.426  0.80 35.30 ?  62  HIS   A CB  1 
ATOM   448  C CB  B HIS   A 1 62  ? -0.716  -4.208  25.374  0.20 35.39 ?  62  HIS   A CB  1 
ATOM   449  C CG  A HIS   A 1 62  ? -0.252  -2.971  24.778  0.80 34.67 ?  62  HIS   A CG  1 
ATOM   450  C CG  B HIS   A 1 62  ? -0.173  -3.020  24.646  0.20 34.88 ?  62  HIS   A CG  1 
ATOM   451  N ND1 A HIS   A 1 62  ? -0.773  -2.523  23.583  0.80 35.47 ?  62  HIS   A ND1 1 
ATOM   452  N ND1 B HIS   A 1 62  ? -0.832  -2.431  23.589  0.20 35.43 ?  62  HIS   A ND1 1 
ATOM   453  C CD2 A HIS   A 1 62  ? 0.659   -2.043  25.164  0.80 37.55 ?  62  HIS   A CD2 1 
ATOM   454  C CD2 B HIS   A 1 62  ? 0.972   -2.316  24.816  0.20 36.95 ?  62  HIS   A CD2 1 
ATOM   455  C CE1 A HIS   A 1 62  ? -0.191  -1.383  23.250  0.80 37.78 ?  62  HIS   A CE1 1 
ATOM   456  C CE1 B HIS   A 1 62  ? -0.119  -1.413  23.140  0.20 37.55 ?  62  HIS   A CE1 1 
ATOM   457  N NE2 A HIS   A 1 62  ? 0.673   -1.062  24.198  0.80 37.52 ?  62  HIS   A NE2 1 
ATOM   458  N NE2 B HIS   A 1 62  ? 0.980   -1.321  23.868  0.20 37.11 ?  62  HIS   A NE2 1 
ATOM   459  N N   . GLN   A 1 63  ? -0.371  -5.062  22.292  1.00 31.55 ?  63  GLN   A N   1 
ATOM   460  C CA  . GLN   A 1 63  ? 0.485   -5.499  21.202  1.00 34.05 ?  63  GLN   A CA  1 
ATOM   461  C C   . GLN   A 1 63  ? 1.193   -4.289  20.618  1.00 33.30 ?  63  GLN   A C   1 
ATOM   462  O O   . GLN   A 1 63  ? 0.541   -3.375  20.099  1.00 34.89 ?  63  GLN   A O   1 
ATOM   463  C CB  . GLN   A 1 63  ? -0.318  -6.242  20.133  1.00 29.57 ?  63  GLN   A CB  1 
ATOM   464  C CG  . GLN   A 1 63  ? 0.538   -7.063  19.171  1.00 29.80 ?  63  GLN   A CG  1 
ATOM   465  C CD  . GLN   A 1 63  ? -0.302  -7.755  18.102  1.00 36.96 ?  63  GLN   A CD  1 
ATOM   466  O OE1 . GLN   A 1 63  ? -0.382  -8.982  18.061  1.00 25.89 ?  63  GLN   A OE1 1 
ATOM   467  N NE2 . GLN   A 1 63  ? -0.924  -6.963  17.227  1.00 30.51 ?  63  GLN   A NE2 1 
ATOM   468  N N   . THR   A 1 64  ? 2.526   -4.298  20.683  1.00 35.45 ?  64  THR   A N   1 
ATOM   469  C CA  . THR   A 1 64  ? 3.318   -3.092  20.428  1.00 37.14 ?  64  THR   A CA  1 
ATOM   470  C C   . THR   A 1 64  ? 3.953   -3.064  19.050  1.00 38.67 ?  64  THR   A C   1 
ATOM   471  O O   . THR   A 1 64  ? 4.351   -1.989  18.608  1.00 40.55 ?  64  THR   A O   1 
ATOM   472  C CB  . THR   A 1 64  ? 4.432   -2.920  21.483  1.00 36.00 ?  64  THR   A CB  1 
ATOM   473  O OG1 . THR   A 1 64  ? 5.152   -4.149  21.656  1.00 37.01 ?  64  THR   A OG1 1 
ATOM   474  C CG2 . THR   A 1 64  ? 3.857   -2.483  22.820  1.00 34.66 ?  64  THR   A CG2 1 
ATOM   475  N N   . ALA   A 1 65  ? 4.062   -4.201  18.361  1.00 36.46 ?  65  ALA   A N   1 
ATOM   476  C CA  . ALA   A 1 65  ? 4.613   -4.245  17.003  1.00 37.92 ?  65  ALA   A CA  1 
ATOM   477  C C   . ALA   A 1 65  ? 3.722   -5.084  16.092  1.00 36.84 ?  65  ALA   A C   1 
ATOM   478  O O   . ALA   A 1 65  ? 4.179   -6.002  15.405  1.00 36.30 ?  65  ALA   A O   1 
ATOM   479  C CB  . ALA   A 1 65  ? 6.040   -4.788  17.004  1.00 42.32 ?  65  ALA   A CB  1 
ATOM   480  N N   . GLY   A 1 66  ? 2.425   -4.776  16.079  1.00 34.86 ?  66  GLY   A N   1 
ATOM   481  C CA  . GLY   A 1 66  ? 1.486   -5.607  15.342  1.00 32.82 ?  66  GLY   A CA  1 
ATOM   482  C C   . GLY   A 1 66  ? 1.775   -5.602  13.856  1.00 33.38 ?  66  GLY   A C   1 
ATOM   483  O O   . GLY   A 1 66  ? 2.255   -4.622  13.298  1.00 36.89 ?  66  GLY   A O   1 
ATOM   484  N N   . ARG   A 1 67  ? 1.496   -6.728  13.215  1.00 28.86 ?  67  ARG   A N   1 
ATOM   485  C CA  . ARG   A 1 67  ? 1.711   -6.894  11.788  1.00 39.20 ?  67  ARG   A CA  1 
ATOM   486  C C   . ARG   A 1 67  ? 0.390   -6.832  11.029  1.00 39.33 ?  67  ARG   A C   1 
ATOM   487  O O   . ARG   A 1 67  ? -0.638  -7.337  11.494  1.00 32.23 ?  67  ARG   A O   1 
ATOM   488  C CB  . ARG   A 1 67  ? 2.420   -8.230  11.499  1.00 43.53 ?  67  ARG   A CB  1 
ATOM   489  C CG  . ARG   A 1 67  ? 3.543   -8.540  12.490  1.00 53.26 ?  67  ARG   A CG  1 
ATOM   490  C CD  . ARG   A 1 67  ? 3.793   -10.023 12.656  1.00 49.57 ?  67  ARG   A CD  1 
ATOM   491  N NE  . ARG   A 1 67  ? 4.295   -10.654 11.449  1.00 52.01 ?  67  ARG   A NE  1 
ATOM   492  C CZ  . ARG   A 1 67  ? 5.575   -10.953 11.260  1.00 63.88 ?  67  ARG   A CZ  1 
ATOM   493  N NH1 . ARG   A 1 67  ? 6.465   -10.668 12.205  1.00 57.19 ?  67  ARG   A NH1 1 
ATOM   494  N NH2 . ARG   A 1 67  ? 5.966   -11.531 10.129  1.00 64.71 ?  67  ARG   A NH2 1 
ATOM   495  N N   . GLY   A 1 68  ? 0.429   -6.227  9.842   1.00 37.99 ?  68  GLY   A N   1 
ATOM   496  C CA  . GLY   A 1 68  ? -0.672  -6.277  8.911   1.00 42.50 ?  68  GLY   A CA  1 
ATOM   497  C C   . GLY   A 1 68  ? -0.302  -7.108  7.693   1.00 39.45 ?  68  GLY   A C   1 
ATOM   498  O O   . GLY   A 1 68  ? 0.770   -7.687  7.609   1.00 43.71 ?  68  GLY   A O   1 
ATOM   499  N N   . ARG   A 1 69  ? -1.224  -7.144  6.737   1.00 47.56 ?  69  ARG   A N   1 
ATOM   500  C CA  . ARG   A 1 69  ? -0.927  -7.745  5.449   1.00 48.71 ?  69  ARG   A CA  1 
ATOM   501  C C   . ARG   A 1 69  ? 0.082   -6.891  4.688   1.00 54.87 ?  69  ARG   A C   1 
ATOM   502  O O   . ARG   A 1 69  ? 0.233   -5.695  4.942   1.00 52.08 ?  69  ARG   A O   1 
ATOM   503  C CB  . ARG   A 1 69  ? -2.203  -7.906  4.621   1.00 45.94 ?  69  ARG   A CB  1 
ATOM   504  N N   . HIS   A 1 70  ? 0.802   -7.540  3.760   1.00 63.90 ?  70  HIS   A N   1 
ATOM   505  C CA  . HIS   A 1 70  ? 1.620   -6.862  2.743   1.00 58.78 ?  70  HIS   A CA  1 
ATOM   506  C C   . HIS   A 1 70  ? 2.598   -5.854  3.352   1.00 56.47 ?  70  HIS   A C   1 
ATOM   507  O O   . HIS   A 1 70  ? 2.760   -4.736  2.855   1.00 53.15 ?  70  HIS   A O   1 
ATOM   508  C CB  . HIS   A 1 70  ? 0.735   -6.183  1.693   1.00 55.77 ?  70  HIS   A CB  1 
ATOM   509  C CG  . HIS   A 1 70  ? -0.330  -7.074  1.128   1.00 70.23 ?  70  HIS   A CG  1 
ATOM   510  N ND1 . HIS   A 1 70  ? -1.655  -6.697  1.054   1.00 66.98 ?  70  HIS   A ND1 1 
ATOM   511  C CD2 . HIS   A 1 70  ? -0.261  -8.312  0.580   1.00 71.28 ?  70  HIS   A CD2 1 
ATOM   512  C CE1 . HIS   A 1 70  ? -2.360  -7.671  0.505   1.00 66.76 ?  70  HIS   A CE1 1 
ATOM   513  N NE2 . HIS   A 1 70  ? -1.537  -8.662  0.206   1.00 73.32 ?  70  HIS   A NE2 1 
ATOM   514  N N   . GLY   A 1 71  ? 3.256   -6.253  4.435   1.00 55.59 ?  71  GLY   A N   1 
ATOM   515  C CA  . GLY   A 1 71  ? 4.163   -5.345  5.115   1.00 54.92 ?  71  GLY   A CA  1 
ATOM   516  C C   . GLY   A 1 71  ? 3.515   -4.070  5.616   1.00 55.29 ?  71  GLY   A C   1 
ATOM   517  O O   . GLY   A 1 71  ? 4.083   -2.985  5.449   1.00 63.09 ?  71  GLY   A O   1 
ATOM   518  N N   . ARG   A 1 72  ? 2.327   -4.171  6.207   1.00 53.54 ?  72  ARG   A N   1 
ATOM   519  C CA  . ARG   A 1 72  ? 1.691   -3.062  6.903   1.00 44.93 ?  72  ARG   A CA  1 
ATOM   520  C C   . ARG   A 1 72  ? 1.717   -3.324  8.403   1.00 39.91 ?  72  ARG   A C   1 
ATOM   521  O O   . ARG   A 1 72  ? 2.165   -4.373  8.865   1.00 38.89 ?  72  ARG   A O   1 
ATOM   522  C CB  . ARG   A 1 72  ? 0.261   -2.853  6.423   1.00 45.77 ?  72  ARG   A CB  1 
ATOM   523  C CG  . ARG   A 1 72  ? 0.149   -2.190  5.082   1.00 45.06 ?  72  ARG   A CG  1 
ATOM   524  C CD  . ARG   A 1 72  ? -1.312  -2.089  4.681   1.00 52.05 ?  72  ARG   A CD  1 
ATOM   525  N NE  . ARG   A 1 72  ? -1.794  -3.376  4.194   1.00 58.01 ?  72  ARG   A NE  1 
ATOM   526  C CZ  . ARG   A 1 72  ? -2.411  -3.548  3.031   1.00 60.75 ?  72  ARG   A CZ  1 
ATOM   527  N NH1 . ARG   A 1 72  ? -2.593  -2.512  2.220   1.00 59.75 ?  72  ARG   A NH1 1 
ATOM   528  N NH2 . ARG   A 1 72  ? -2.817  -4.759  2.670   1.00 57.96 ?  72  ARG   A NH2 1 
ATOM   529  N N   . GLY   A 1 73  ? 1.232   -2.351  9.175   1.00 42.92 ?  73  GLY   A N   1 
ATOM   530  C CA  . GLY   A 1 73  ? 1.232   -2.437  10.617  1.00 34.12 ?  73  GLY   A CA  1 
ATOM   531  C C   . GLY   A 1 73  ? -0.174  -2.624  11.164  1.00 38.52 ?  73  GLY   A C   1 
ATOM   532  O O   . GLY   A 1 73  ? -1.170  -2.506  10.457  1.00 36.33 ?  73  GLY   A O   1 
ATOM   533  N N   . TRP   A 1 74  ? -0.234  -2.920  12.462  1.00 35.68 ?  74  TRP   A N   1 
ATOM   534  C CA  . TRP   A 1 74  ? -1.497  -2.992  13.184  1.00 31.61 ?  74  TRP   A CA  1 
ATOM   535  C C   . TRP   A 1 74  ? -1.300  -2.300  14.516  1.00 31.74 ?  74  TRP   A C   1 
ATOM   536  O O   . TRP   A 1 74  ? -0.458  -2.733  15.308  1.00 35.83 ?  74  TRP   A O   1 
ATOM   537  C CB  . TRP   A 1 74  ? -1.959  -4.442  13.410  1.00 33.50 ?  74  TRP   A CB  1 
ATOM   538  C CG  . TRP   A 1 74  ? -3.337  -4.506  13.988  1.00 32.12 ?  74  TRP   A CG  1 
ATOM   539  C CD1 . TRP   A 1 74  ? -3.678  -4.792  15.284  1.00 28.58 ?  74  TRP   A CD1 1 
ATOM   540  C CD2 . TRP   A 1 74  ? -4.564  -4.255  13.294  1.00 29.45 ?  74  TRP   A CD2 1 
ATOM   541  N NE1 . TRP   A 1 74  ? -5.043  -4.738  15.437  1.00 29.50 ?  74  TRP   A NE1 1 
ATOM   542  C CE2 . TRP   A 1 74  ? -5.612  -4.415  14.230  1.00 31.24 ?  74  TRP   A CE2 1 
ATOM   543  C CE3 . TRP   A 1 74  ? -4.878  -3.916  11.969  1.00 29.95 ?  74  TRP   A CE3 1 
ATOM   544  C CZ2 . TRP   A 1 74  ? -6.954  -4.268  13.878  1.00 26.07 ?  74  TRP   A CZ2 1 
ATOM   545  C CZ3 . TRP   A 1 74  ? -6.210  -3.756  11.622  1.00 31.26 ?  74  TRP   A CZ3 1 
ATOM   546  C CH2 . TRP   A 1 74  ? -7.230  -3.926  12.568  1.00 30.78 ?  74  TRP   A CH2 1 
ATOM   547  N N   . ALA   A 1 75  ? -2.071  -1.243  14.764  1.00 26.98 ?  75  ALA   A N   1 
ATOM   548  C CA  . ALA   A 1 75  ? -1.934  -0.458  15.986  1.00 33.05 ?  75  ALA   A CA  1 
ATOM   549  C C   . ALA   A 1 75  ? -2.916  -0.915  17.062  1.00 34.25 ?  75  ALA   A C   1 
ATOM   550  O O   . ALA   A 1 75  ? -4.053  -1.307  16.776  1.00 35.10 ?  75  ALA   A O   1 
ATOM   551  C CB  . ALA   A 1 75  ? -2.155  1.029   15.698  1.00 38.04 ?  75  ALA   A CB  1 
ATOM   552  N N   . ALA   A 1 76  ? -2.475  -0.825  18.313  1.00 32.35 ?  76  ALA   A N   1 
ATOM   553  C CA  . ALA   A 1 76  ? -3.269  -1.235  19.459  1.00 31.38 ?  76  ALA   A CA  1 
ATOM   554  C C   . ALA   A 1 76  ? -2.887  -0.384  20.658  1.00 36.98 ?  76  ALA   A C   1 
ATOM   555  O O   . ALA   A 1 76  ? -1.750  0.073   20.762  1.00 37.72 ?  76  ALA   A O   1 
ATOM   556  C CB  . ALA   A 1 76  ? -3.038  -2.707  19.785  1.00 32.79 ?  76  ALA   A CB  1 
ATOM   557  N N   . THR   A 1 77  ? -3.845  -0.145  21.549  1.00 36.37 ?  77  THR   A N   1 
ATOM   558  C CA  . THR   A 1 77  ? -3.524  0.239   22.916  1.00 38.02 ?  77  THR   A CA  1 
ATOM   559  C C   . THR   A 1 77  ? -4.039  -0.834  23.862  1.00 38.94 ?  77  THR   A C   1 
ATOM   560  O O   . THR   A 1 77  ? -4.823  -1.707  23.481  1.00 39.27 ?  77  THR   A O   1 
ATOM   561  C CB  . THR   A 1 77  ? -4.097  1.614   23.298  1.00 42.20 ?  77  THR   A CB  1 
ATOM   562  O OG1 . THR   A 1 77  ? -5.520  1.513   23.487  1.00 40.80 ?  77  THR   A OG1 1 
ATOM   563  C CG2 . THR   A 1 77  ? -3.738  2.665   22.234  1.00 40.25 ?  77  THR   A CG2 1 
ATOM   564  N N   . ALA   A 1 78  ? -3.580  -0.754  25.110  1.00 39.81 ?  78  ALA   A N   1 
ATOM   565  C CA  . ALA   A 1 78  ? -3.780  -1.835  26.062  1.00 30.65 ?  78  ALA   A CA  1 
ATOM   566  C C   . ALA   A 1 78  ? -5.258  -2.020  26.395  1.00 29.52 ?  78  ALA   A C   1 
ATOM   567  O O   . ALA   A 1 78  ? -5.952  -1.060  26.744  1.00 33.87 ?  78  ALA   A O   1 
ATOM   568  C CB  . ALA   A 1 78  ? -2.985  -1.555  27.341  1.00 35.43 ?  78  ALA   A CB  1 
ATOM   569  N N   . ARG   A 1 79  ? -5.727  -3.265  26.294  1.00 31.40 ?  79  ARG   A N   1 
ATOM   570  C CA  . ARG   A 1 79  ? -7.051  -3.729  26.703  1.00 35.57 ?  79  ARG   A CA  1 
ATOM   571  C C   . ARG   A 1 79  ? -8.166  -3.152  25.841  1.00 30.20 ?  79  ARG   A C   1 
ATOM   572  O O   . ARG   A 1 79  ? -9.344  -3.213  26.223  1.00 27.85 ?  79  ARG   A O   1 
ATOM   573  C CB  . ARG   A 1 79  ? -7.310  -3.430  28.185  1.00 32.50 ?  79  ARG   A CB  1 
ATOM   574  C CG  . ARG   A 1 79  ? -6.540  -4.344  29.121  1.00 39.32 ?  79  ARG   A CG  1 
ATOM   575  C CD  . ARG   A 1 79  ? -6.485  -3.808  30.532  1.00 36.83 ?  79  ARG   A CD  1 
ATOM   576  N NE  . ARG   A 1 79  ? -5.614  -2.636  30.615  1.00 45.58 ?  79  ARG   A NE  1 
ATOM   577  C CZ  . ARG   A 1 79  ? -6.054  -1.397  30.832  1.00 43.04 ?  79  ARG   A CZ  1 
ATOM   578  N NH1 . ARG   A 1 79  ? -5.197  -0.397  30.902  1.00 49.04 ?  79  ARG   A NH1 1 
ATOM   579  N NH2 . ARG   A 1 79  ? -7.353  -1.158  31.000  1.00 42.62 ?  79  ARG   A NH2 1 
ATOM   580  N N   . ALA   A 1 80  ? -7.824  -2.573  24.691  1.00 33.69 ?  80  ALA   A N   1 
ATOM   581  C CA  . ALA   A 1 80  ? -8.799  -1.969  23.792  1.00 32.16 ?  80  ALA   A CA  1 
ATOM   582  C C   . ALA   A 1 80  ? -9.307  -2.947  22.745  1.00 33.05 ?  80  ALA   A C   1 
ATOM   583  O O   . ALA   A 1 80  ? -10.290 -2.655  22.044  1.00 29.22 ?  80  ALA   A O   1 
ATOM   584  C CB  . ALA   A 1 80  ? -8.178  -0.742  23.099  1.00 28.41 ?  80  ALA   A CB  1 
ATOM   585  N N   . GLN   A 1 81  ? -8.657  -4.097  22.621  1.00 29.74 ?  81  GLN   A N   1 
ATOM   586  C CA  . GLN   A 1 81  ? -8.913  -4.993  21.513  1.00 30.89 ?  81  GLN   A CA  1 
ATOM   587  C C   . GLN   A 1 81  ? -8.899  -6.426  22.016  1.00 33.55 ?  81  GLN   A C   1 
ATOM   588  O O   . GLN   A 1 81  ? -8.396  -6.727  23.106  1.00 31.58 ?  81  GLN   A O   1 
ATOM   589  C CB  . GLN   A 1 81  ? -7.852  -4.844  20.429  1.00 28.81 ?  81  GLN   A CB  1 
ATOM   590  C CG  . GLN   A 1 81  ? -7.928  -3.621  19.569  1.00 28.68 ?  81  GLN   A CG  1 
ATOM   591  C CD  . GLN   A 1 81  ? -6.875  -3.670  18.489  1.00 32.03 ?  81  GLN   A CD  1 
ATOM   592  O OE1 . GLN   A 1 81  ? -6.638  -4.726  17.881  1.00 25.41 ?  81  GLN   A OE1 1 
ATOM   593  N NE2 . GLN   A 1 81  ? -6.214  -2.535  18.252  1.00 27.25 ?  81  GLN   A NE2 1 
ATOM   594  N N   . ILE   A 1 82  ? -9.415  -7.320  21.189  1.00 27.27 ?  82  ILE   A N   1 
ATOM   595  C CA  . ILE   A 1 82  ? -9.099  -8.728  21.336  1.00 24.55 ?  82  ILE   A CA  1 
ATOM   596  C C   . ILE   A 1 82  ? -8.024  -9.026  20.309  1.00 22.93 ?  82  ILE   A C   1 
ATOM   597  O O   . ILE   A 1 82  ? -8.259  -8.956  19.094  1.00 28.48 ?  82  ILE   A O   1 
ATOM   598  C CB  . ILE   A 1 82  ? -10.336 -9.621  21.187  1.00 29.71 ?  82  ILE   A CB  1 
ATOM   599  C CG1 . ILE   A 1 82  ? -11.202 -9.464  22.426  1.00 29.79 ?  82  ILE   A CG1 1 
ATOM   600  C CG2 . ILE   A 1 82  ? -9.923  -11.112 21.064  1.00 29.64 ?  82  ILE   A CG2 1 
ATOM   601  C CD1 . ILE   A 1 82  ? -12.640 -9.779  22.181  1.00 36.17 ?  82  ILE   A CD1 1 
ATOM   602  N N   . ILE   A 1 83  ? -6.831  -9.332  20.810  1.00 26.46 ?  83  ILE   A N   1 
ATOM   603  C CA  . ILE   A 1 83  ? -5.654  -9.562  19.993  1.00 26.04 ?  83  ILE   A CA  1 
ATOM   604  C C   . ILE   A 1 83  ? -5.247  -11.009 20.201  1.00 23.53 ?  83  ILE   A C   1 
ATOM   605  O O   . ILE   A 1 83  ? -4.823  -11.382 21.295  1.00 25.54 ?  83  ILE   A O   1 
ATOM   606  C CB  . ILE   A 1 83  ? -4.511  -8.623  20.372  1.00 24.42 ?  83  ILE   A CB  1 
ATOM   607  C CG1 . ILE   A 1 83  ? -4.968  -7.162  20.278  1.00 31.77 ?  83  ILE   A CG1 1 
ATOM   608  C CG2 . ILE   A 1 83  ? -3.335  -8.887  19.492  1.00 23.17 ?  83  ILE   A CG2 1 
ATOM   609  C CD1 . ILE   A 1 83  ? -3.912  -6.152  20.799  1.00 29.41 ?  83  ILE   A CD1 1 
ATOM   610  N N   . LEU   A 1 84  ? -5.338  -11.831 19.163  1.00 30.90 ?  84  LEU   A N   1 
ATOM   611  C CA  . LEU   A 1 84  ? -5.022  -13.217 19.441  1.00 31.35 ?  84  LEU   A CA  1 
ATOM   612  C C   . LEU   A 1 84  ? -4.503  -13.898 18.192  1.00 30.36 ?  84  LEU   A C   1 
ATOM   613  O O   . LEU   A 1 84  ? -4.712  -13.430 17.073  1.00 27.79 ?  84  LEU   A O   1 
ATOM   614  C CB  . LEU   A 1 84  ? -6.224  -13.958 20.033  1.00 30.01 ?  84  LEU   A CB  1 
ATOM   615  C CG  . LEU   A 1 84  ? -7.489  -14.153 19.197  1.00 32.72 ?  84  LEU   A CG  1 
ATOM   616  C CD1 . LEU   A 1 84  ? -7.390  -15.374 18.314  1.00 32.88 ?  84  LEU   A CD1 1 
ATOM   617  C CD2 . LEU   A 1 84  ? -8.633  -14.358 20.168  1.00 29.87 ?  84  LEU   A CD2 1 
ATOM   618  N N   . SER   A 1 85  ? -3.782  -15.008 18.416  1.00 25.87 ?  85  SER   A N   1 
ATOM   619  C CA  . SER   A 1 85  ? -3.301  -15.867 17.354  1.00 23.37 ?  85  SER   A CA  1 
ATOM   620  C C   . SER   A 1 85  ? -3.607  -17.301 17.733  1.00 30.81 ?  85  SER   A C   1 
ATOM   621  O O   . SER   A 1 85  ? -3.667  -17.649 18.915  1.00 24.23 ?  85  SER   A O   1 
ATOM   622  C CB  . SER   A 1 85  ? -1.796  -15.708 17.080  1.00 30.02 ?  85  SER   A CB  1 
ATOM   623  O OG  . SER   A 1 85  ? -1.454  -14.383 16.715  1.00 32.99 ?  85  SER   A OG  1 
ATOM   624  N N   . VAL   A 1 86  ? -3.842  -18.122 16.717  1.00 26.74 ?  86  VAL   A N   1 
ATOM   625  C CA  . VAL   A 1 86  ? -4.118  -19.536 16.930  1.00 29.71 ?  86  VAL   A CA  1 
ATOM   626  C C   . VAL   A 1 86  ? -3.277  -20.299 15.929  1.00 23.48 ?  86  VAL   A C   1 
ATOM   627  O O   . VAL   A 1 86  ? -3.029  -19.825 14.815  1.00 26.74 ?  86  VAL   A O   1 
ATOM   628  C CB  . VAL   A 1 86  ? -5.631  -19.905 16.776  1.00 27.73 ?  86  VAL   A CB  1 
ATOM   629  C CG1 . VAL   A 1 86  ? -6.486  -19.076 17.692  1.00 30.39 ?  86  VAL   A CG1 1 
ATOM   630  C CG2 . VAL   A 1 86  ? -6.088  -19.753 15.335  1.00 29.61 ?  86  VAL   A CG2 1 
ATOM   631  N N   . GLY   A 1 87  ? -2.826  -21.483 16.331  1.00 23.38 ?  87  GLY   A N   1 
ATOM   632  C CA  . GLY   A 1 87  ? -2.109  -22.368 15.439  1.00 27.68 ?  87  GLY   A CA  1 
ATOM   633  C C   . GLY   A 1 87  ? -3.064  -23.405 14.875  1.00 32.42 ?  87  GLY   A C   1 
ATOM   634  O O   . GLY   A 1 87  ? -3.860  -23.998 15.609  1.00 28.78 ?  87  GLY   A O   1 
ATOM   635  N N   . VAL   A 1 88  ? -2.974  -23.610 13.564  1.00 23.59 ?  88  VAL   A N   1 
ATOM   636  C CA  . VAL   A 1 88  ? -3.790  -24.568 12.834  1.00 28.06 ?  88  VAL   A CA  1 
ATOM   637  C C   . VAL   A 1 88  ? -2.842  -25.444 12.025  1.00 32.35 ?  88  VAL   A C   1 
ATOM   638  O O   . VAL   A 1 88  ? -2.058  -24.936 11.215  1.00 28.72 ?  88  VAL   A O   1 
ATOM   639  C CB  . VAL   A 1 88  ? -4.812  -23.899 11.892  1.00 32.14 ?  88  VAL   A CB  1 
ATOM   640  C CG1 . VAL   A 1 88  ? -5.717  -24.972 11.250  1.00 32.55 ?  88  VAL   A CG1 1 
ATOM   641  C CG2 . VAL   A 1 88  ? -5.654  -22.827 12.613  1.00 23.69 ?  88  VAL   A CG2 1 
ATOM   642  N N   . ARG   A 1 89  ? -2.910  -26.749 12.237  1.00 30.09 ?  89  ARG   A N   1 
ATOM   643  C CA  . ARG   A 1 89  ? -2.146  -27.653 11.395  1.00 35.44 ?  89  ARG   A CA  1 
ATOM   644  C C   . ARG   A 1 89  ? -2.807  -27.726 10.029  1.00 38.56 ?  89  ARG   A C   1 
ATOM   645  O O   . ARG   A 1 89  ? -4.005  -28.022 9.928   1.00 40.62 ?  89  ARG   A O   1 
ATOM   646  C CB  . ARG   A 1 89  ? -2.063  -29.035 12.032  1.00 40.80 ?  89  ARG   A CB  1 
ATOM   647  C CG  . ARG   A 1 89  ? -1.321  -30.025 11.166  1.00 42.82 ?  89  ARG   A CG  1 
ATOM   648  C CD  . ARG   A 1 89  ? -1.152  -31.347 11.905  1.00 54.73 ?  89  ARG   A CD  1 
ATOM   649  N NE  . ARG   A 1 89  ? -0.670  -32.385 11.008  1.00 55.67 ?  89  ARG   A NE  1 
ATOM   650  C CZ  . ARG   A 1 89  ? 0.553   -32.894 11.067  1.00 63.25 ?  89  ARG   A CZ  1 
ATOM   651  N NH1 . ARG   A 1 89  ? 1.409   -32.434 11.977  1.00 64.26 ?  89  ARG   A NH1 1 
ATOM   652  N NH2 . ARG   A 1 89  ? 0.923   -33.845 10.212  1.00 59.39 ?  89  ARG   A NH2 1 
ATOM   653  N N   . VAL   A 1 90  ? -2.043  -27.438 8.977   1.00 31.49 ?  90  VAL   A N   1 
ATOM   654  C CA  . VAL   A 1 90  ? -2.595  -27.370 7.627   1.00 32.88 ?  90  VAL   A CA  1 
ATOM   655  C C   . VAL   A 1 90  ? -1.955  -28.363 6.678   1.00 38.15 ?  90  VAL   A C   1 
ATOM   656  O O   . VAL   A 1 90  ? -2.433  -28.505 5.543   1.00 33.80 ?  90  VAL   A O   1 
ATOM   657  C CB  . VAL   A 1 90  ? -2.486  -25.945 7.037   1.00 35.57 ?  90  VAL   A CB  1 
ATOM   658  C CG1 . VAL   A 1 90  ? -3.144  -24.948 7.956   1.00 32.65 ?  90  VAL   A CG1 1 
ATOM   659  C CG2 . VAL   A 1 90  ? -1.029  -25.573 6.793   1.00 31.10 ?  90  VAL   A CG2 1 
ATOM   660  N N   . VAL   A 1 91  ? -0.906  -29.067 7.102   1.00 35.98 ?  91  VAL   A N   1 
ATOM   661  C CA  . VAL   A 1 91  ? -0.090  -29.808 6.152   1.00 41.03 ?  91  VAL   A CA  1 
ATOM   662  C C   . VAL   A 1 91  ? -0.869  -30.959 5.531   1.00 44.52 ?  91  VAL   A C   1 
ATOM   663  O O   . VAL   A 1 91  ? -0.503  -31.428 4.452   1.00 47.23 ?  91  VAL   A O   1 
ATOM   664  C CB  . VAL   A 1 91  ? 1.207   -30.273 6.852   1.00 43.83 ?  91  VAL   A CB  1 
ATOM   665  C CG1 . VAL   A 1 91  ? 0.897   -31.313 7.957   1.00 37.75 ?  91  VAL   A CG1 1 
ATOM   666  C CG2 . VAL   A 1 91  ? 2.260   -30.703 5.856   1.00 50.95 ?  91  VAL   A CG2 1 
ATOM   667  N N   . ASP   A 1 92  ? -1.982  -31.381 6.157   1.00 40.11 ?  92  ASP   A N   1 
ATOM   668  C CA  . ASP   A 1 92  ? -2.882  -32.417 5.635   1.00 45.40 ?  92  ASP   A CA  1 
ATOM   669  C C   . ASP   A 1 92  ? -3.787  -31.926 4.506   1.00 47.45 ?  92  ASP   A C   1 
ATOM   670  O O   . ASP   A 1 92  ? -4.464  -32.744 3.870   1.00 39.83 ?  92  ASP   A O   1 
ATOM   671  C CB  . ASP   A 1 92  ? -3.793  -32.939 6.752   1.00 46.92 ?  92  ASP   A CB  1 
ATOM   672  C CG  . ASP   A 1 92  ? -3.035  -33.315 8.013   1.00 61.88 ?  92  ASP   A CG  1 
ATOM   673  O OD1 . ASP   A 1 92  ? -1.975  -33.975 7.893   1.00 70.10 ?  92  ASP   A OD1 1 
ATOM   674  O OD2 . ASP   A 1 92  ? -3.492  -32.927 9.123   1.00 67.29 -1 92  ASP   A OD2 1 
ATOM   675  N N   . VAL   A 1 93  ? -3.856  -30.619 4.271   1.00 41.50 ?  93  VAL   A N   1 
ATOM   676  C CA  . VAL   A 1 93  ? -4.803  -30.053 3.315   1.00 35.39 ?  93  VAL   A CA  1 
ATOM   677  C C   . VAL   A 1 93  ? -4.016  -29.521 2.117   1.00 39.36 ?  93  VAL   A C   1 
ATOM   678  O O   . VAL   A 1 93  ? -2.978  -28.875 2.310   1.00 40.66 ?  93  VAL   A O   1 
ATOM   679  C CB  . VAL   A 1 93  ? -5.657  -28.966 3.991   1.00 32.54 ?  93  VAL   A CB  1 
ATOM   680  C CG1 . VAL   A 1 93  ? -6.673  -28.376 3.029   1.00 31.57 ?  93  VAL   A CG1 1 
ATOM   681  C CG2 . VAL   A 1 93  ? -6.355  -29.539 5.234   1.00 40.02 ?  93  VAL   A CG2 1 
ATOM   682  N N   . PRO   A 1 94  ? -4.462  -29.764 0.872   1.00 38.87 ?  94  PRO   A N   1 
ATOM   683  C CA  . PRO   A 1 94  ? -3.701  -29.286 -0.301  1.00 37.40 ?  94  PRO   A CA  1 
ATOM   684  C C   . PRO   A 1 94  ? -3.499  -27.775 -0.256  1.00 37.94 ?  94  PRO   A C   1 
ATOM   685  O O   . PRO   A 1 94  ? -4.344  -27.031 0.245   1.00 39.40 ?  94  PRO   A O   1 
ATOM   686  C CB  . PRO   A 1 94  ? -4.577  -29.689 -1.493  1.00 30.30 ?  94  PRO   A CB  1 
ATOM   687  C CG  . PRO   A 1 94  ? -5.565  -30.647 -0.984  1.00 43.25 ?  94  PRO   A CG  1 
ATOM   688  C CD  . PRO   A 1 94  ? -5.734  -30.395 0.489   1.00 35.06 ?  94  PRO   A CD  1 
ATOM   689  N N   . VAL   A 1 95  ? -2.368  -27.319 -0.796  1.00 35.98 ?  95  VAL   A N   1 
ATOM   690  C CA  . VAL   A 1 95  ? -1.952  -25.946 -0.531  1.00 37.94 ?  95  VAL   A CA  1 
ATOM   691  C C   . VAL   A 1 95  ? -2.921  -24.953 -1.159  1.00 34.22 ?  95  VAL   A C   1 
ATOM   692  O O   . VAL   A 1 95  ? -3.118  -23.849 -0.639  1.00 32.53 ?  95  VAL   A O   1 
ATOM   693  C CB  . VAL   A 1 95  ? -0.521  -25.701 -1.022  1.00 42.63 ?  95  VAL   A CB  1 
ATOM   694  C CG1 . VAL   A 1 95  ? 0.433   -26.659 -0.334  1.00 56.20 ?  95  VAL   A CG1 1 
ATOM   695  C CG2 . VAL   A 1 95  ? -0.434  -25.771 -2.547  1.00 43.35 ?  95  VAL   A CG2 1 
ATOM   696  N N   . GLN   A 1 96  ? -3.545  -25.320 -2.276  1.00 32.41 ?  96  GLN   A N   1 
ATOM   697  C CA  . GLN   A 1 96  ? -4.492  -24.437 -2.969  1.00 43.90 ?  96  GLN   A CA  1 
ATOM   698  C C   . GLN   A 1 96  ? -5.701  -24.097 -2.106  1.00 42.72 ?  96  GLN   A C   1 
ATOM   699  O O   . GLN   A 1 96  ? -6.465  -23.200 -2.465  1.00 38.59 ?  96  GLN   A O   1 
ATOM   700  C CB  . GLN   A 1 96  ? -4.939  -25.096 -4.279  1.00 40.76 ?  96  GLN   A CB  1 
ATOM   701  N N   . ALA   A 1 97  ? -5.892  -24.793 -0.984  1.00 38.25 ?  97  ALA   A N   1 
ATOM   702  C CA  . ALA   A 1 97  ? -7.030  -24.569 -0.108  1.00 34.33 ?  97  ALA   A CA  1 
ATOM   703  C C   . ALA   A 1 97  ? -6.706  -23.672 1.074   1.00 31.29 ?  97  ALA   A C   1 
ATOM   704  O O   . ALA   A 1 97  ? -7.611  -23.328 1.833   1.00 32.96 ?  97  ALA   A O   1 
ATOM   705  C CB  . ALA   A 1 97  ? -7.559  -25.904 0.415   1.00 37.77 ?  97  ALA   A CB  1 
ATOM   706  N N   . TRP   A 1 98  ? -5.449  -23.286 1.258   1.00 29.27 ?  98  TRP   A N   1 
ATOM   707  C CA  . TRP   A 1 98  ? -5.085  -22.660 2.520   1.00 32.28 ?  98  TRP   A CA  1 
ATOM   708  C C   . TRP   A 1 98  ? -5.602  -21.238 2.642   1.00 33.02 ?  98  TRP   A C   1 
ATOM   709  O O   . TRP   A 1 98  ? -5.768  -20.756 3.765   1.00 30.53 ?  98  TRP   A O   1 
ATOM   710  C CB  . TRP   A 1 98  ? -3.579  -22.651 2.715   1.00 31.60 ?  98  TRP   A CB  1 
ATOM   711  C CG  . TRP   A 1 98  ? -2.974  -23.993 2.913   1.00 37.37 ?  98  TRP   A CG  1 
ATOM   712  C CD1 . TRP   A 1 98  ? -3.613  -25.219 2.890   1.00 30.34 ?  98  TRP   A CD1 1 
ATOM   713  C CD2 . TRP   A 1 98  ? -1.589  -24.261 3.150   1.00 36.83 ?  98  TRP   A CD2 1 
ATOM   714  N NE1 . TRP   A 1 98  ? -2.686  -26.233 3.107   1.00 30.78 ?  98  TRP   A NE1 1 
ATOM   715  C CE2 . TRP   A 1 98  ? -1.443  -25.670 3.268   1.00 36.44 ?  98  TRP   A CE2 1 
ATOM   716  C CE3 . TRP   A 1 98  ? -0.450  -23.446 3.272   1.00 42.63 ?  98  TRP   A CE3 1 
ATOM   717  C CZ2 . TRP   A 1 98  ? -0.206  -26.272 3.515   1.00 32.53 ?  98  TRP   A CZ2 1 
ATOM   718  C CZ3 . TRP   A 1 98  ? 0.780   -24.049 3.503   1.00 40.54 ?  98  TRP   A CZ3 1 
ATOM   719  C CH2 . TRP   A 1 98  ? 0.893   -25.451 3.616   1.00 35.80 ?  98  TRP   A CH2 1 
ATOM   720  N N   . GLY   A 1 99  ? -5.862  -20.561 1.528   1.00 31.18 ?  99  GLY   A N   1 
ATOM   721  C CA  . GLY   A 1 99  ? -6.412  -19.212 1.612   1.00 36.62 ?  99  GLY   A CA  1 
ATOM   722  C C   . GLY   A 1 99  ? -7.805  -19.169 2.199   1.00 33.51 ?  99  GLY   A C   1 
ATOM   723  O O   . GLY   A 1 99  ? -8.213  -18.135 2.732   1.00 33.93 ?  99  GLY   A O   1 
ATOM   724  N N   . TRP   A 1 100 ? -8.548  -20.279 2.124   1.00 36.52 ?  100 TRP   A N   1 
ATOM   725  C CA  . TRP   A 1 100 ? -9.863  -20.328 2.759   1.00 36.52 ?  100 TRP   A CA  1 
ATOM   726  C C   . TRP   A 1 100 ? -9.776  -20.105 4.257   1.00 39.19 ?  100 TRP   A C   1 
ATOM   727  O O   . TRP   A 1 100 ? -10.708 -19.545 4.853   1.00 31.52 ?  100 TRP   A O   1 
ATOM   728  C CB  . TRP   A 1 100 ? -10.543 -21.660 2.468   1.00 30.47 ?  100 TRP   A CB  1 
ATOM   729  C CG  . TRP   A 1 100 ? -11.244 -21.580 1.197   1.00 32.51 ?  100 TRP   A CG  1 
ATOM   730  C CD1 . TRP   A 1 100 ? -10.836 -22.083 0.002   1.00 37.11 ?  100 TRP   A CD1 1 
ATOM   731  C CD2 . TRP   A 1 100 ? -12.454 -20.884 0.954   1.00 34.70 ?  100 TRP   A CD2 1 
ATOM   732  N NE1 . TRP   A 1 100 ? -11.734 -21.758 -0.976  1.00 35.45 ?  100 TRP   A NE1 1 
ATOM   733  C CE2 . TRP   A 1 100 ? -12.747 -21.028 -0.411  1.00 39.21 ?  100 TRP   A CE2 1 
ATOM   734  C CE3 . TRP   A 1 100 ? -13.326 -20.154 1.761   1.00 34.50 ?  100 TRP   A CE3 1 
ATOM   735  C CZ2 . TRP   A 1 100 ? -13.882 -20.481 -0.987  1.00 43.76 ?  100 TRP   A CZ2 1 
ATOM   736  C CZ3 . TRP   A 1 100 ? -14.459 -19.615 1.185   1.00 39.34 ?  100 TRP   A CZ3 1 
ATOM   737  C CH2 . TRP   A 1 100 ? -14.723 -19.778 -0.170  1.00 42.45 ?  100 TRP   A CH2 1 
ATOM   738  N N   . LEU   A 1 101 ? -8.657  -20.508 4.874   1.00 36.84 ?  101 LEU   A N   1 
ATOM   739  C CA  . LEU   A 1 101 ? -8.537  -20.416 6.325   1.00 39.45 ?  101 LEU   A CA  1 
ATOM   740  C C   . LEU   A 1 101 ? -8.650  -18.977 6.786   1.00 38.39 ?  101 LEU   A C   1 
ATOM   741  O O   . LEU   A 1 101 ? -9.291  -18.691 7.800   1.00 36.89 ?  101 LEU   A O   1 
ATOM   742  C CB  . LEU   A 1 101 ? -7.210  -21.025 6.767   1.00 35.53 ?  101 LEU   A CB  1 
ATOM   743  C CG  . LEU   A 1 101 ? -7.095  -21.542 8.180   1.00 40.64 ?  101 LEU   A CG  1 
ATOM   744  C CD1 . LEU   A 1 101 ? -8.358  -22.344 8.527   1.00 26.51 ?  101 LEU   A CD1 1 
ATOM   745  C CD2 . LEU   A 1 101 ? -5.837  -22.451 8.224   1.00 32.91 ?  101 LEU   A CD2 1 
ATOM   746  N N   . SER   A 1 102 ? -8.062  -18.053 6.022   1.00 34.76 ?  102 SER   A N   1 
ATOM   747  C CA  . SER   A 1 102 ? -8.169  -16.633 6.340   1.00 36.21 ?  102 SER   A CA  1 
ATOM   748  C C   . SER   A 1 102 ? -9.584  -16.101 6.101   1.00 35.25 ?  102 SER   A C   1 
ATOM   749  O O   . SER   A 1 102 ? -10.075 -15.280 6.881   1.00 34.35 ?  102 SER   A O   1 
ATOM   750  C CB  . SER   A 1 102 ? -7.156  -15.843 5.507   1.00 37.67 ?  102 SER   A CB  1 
ATOM   751  O OG  . SER   A 1 102 ? -7.368  -14.454 5.651   1.00 56.50 ?  102 SER   A OG  1 
ATOM   752  N N   . LEU   A 1 103 ? -10.241 -16.523 5.011   1.00 34.39 ?  103 LEU   A N   1 
ATOM   753  C CA  . LEU   A 1 103 ? -11.644 -16.159 4.818   1.00 33.32 ?  103 LEU   A CA  1 
ATOM   754  C C   . LEU   A 1 103 ? -12.500 -16.686 5.964   1.00 30.82 ?  103 LEU   A C   1 
ATOM   755  O O   . LEU   A 1 103 ? -13.315 -15.954 6.525   1.00 30.33 ?  103 LEU   A O   1 
ATOM   756  C CB  . LEU   A 1 103 ? -12.177 -16.678 3.476   1.00 28.23 ?  103 LEU   A CB  1 
ATOM   757  C CG  . LEU   A 1 103 ? -11.438 -16.393 2.158   1.00 39.46 ?  103 LEU   A CG  1 
ATOM   758  C CD1 . LEU   A 1 103 ? -12.356 -16.628 0.975   1.00 38.64 ?  103 LEU   A CD1 1 
ATOM   759  C CD2 . LEU   A 1 103 ? -10.862 -15.007 2.102   1.00 41.94 ?  103 LEU   A CD2 1 
ATOM   760  N N   . ALA   A 1 104 ? -12.304 -17.946 6.347   1.00 30.55 ?  104 ALA   A N   1 
ATOM   761  C CA  . ALA   A 1 104 ? -13.035 -18.503 7.483   1.00 34.21 ?  104 ALA   A CA  1 
ATOM   762  C C   . ALA   A 1 104 ? -12.778 -17.720 8.778   1.00 32.40 ?  104 ALA   A C   1 
ATOM   763  O O   . ALA   A 1 104 ? -13.698 -17.504 9.571   1.00 38.54 ?  104 ALA   A O   1 
ATOM   764  C CB  . ALA   A 1 104 ? -12.668 -19.982 7.652   1.00 37.55 ?  104 ALA   A CB  1 
ATOM   765  N N   . ALA   A 1 105 ? -11.543 -17.288 9.022   1.00 28.22 ?  105 ALA   A N   1 
ATOM   766  C CA  . ALA   A 1 105 ? -11.288 -16.507 10.229  1.00 32.54 ?  105 ALA   A CA  1 
ATOM   767  C C   . ALA   A 1 105 ? -12.143 -15.235 10.275  1.00 34.59 ?  105 ALA   A C   1 
ATOM   768  O O   . ALA   A 1 105 ? -12.727 -14.911 11.314  1.00 32.71 ?  105 ALA   A O   1 
ATOM   769  C CB  . ALA   A 1 105 ? -9.807  -16.158 10.320  1.00 29.65 ?  105 ALA   A CB  1 
ATOM   770  N N   . GLY   A 1 106 ? -12.220 -14.492 9.165   1.00 31.67 ?  106 GLY   A N   1 
ATOM   771  C CA  . GLY   A 1 106 ? -12.984 -13.252 9.176   1.00 32.14 ?  106 GLY   A CA  1 
ATOM   772  C C   . GLY   A 1 106 ? -14.460 -13.512 9.381   1.00 31.60 ?  106 GLY   A C   1 
ATOM   773  O O   . GLY   A 1 106 ? -15.151 -12.761 10.071  1.00 31.89 ?  106 GLY   A O   1 
ATOM   774  N N   . LEU   A 1 107 ? -14.957 -14.590 8.795   1.00 29.85 ?  107 LEU   A N   1 
ATOM   775  C CA  . LEU   A 1 107 ? -16.335 -14.987 9.040   1.00 32.54 ?  107 LEU   A CA  1 
ATOM   776  C C   . LEU   A 1 107 ? -16.561 -15.293 10.522  1.00 34.01 ?  107 LEU   A C   1 
ATOM   777  O O   . LEU   A 1 107 ? -17.577 -14.889 11.107  1.00 32.84 ?  107 LEU   A O   1 
ATOM   778  C CB  . LEU   A 1 107 ? -16.636 -16.187 8.143   1.00 33.36 ?  107 LEU   A CB  1 
ATOM   779  C CG  . LEU   A 1 107 ? -17.987 -16.842 7.939   1.00 37.77 ?  107 LEU   A CG  1 
ATOM   780  C CD1 . LEU   A 1 107 ? -18.986 -15.869 7.315   1.00 39.28 ?  107 LEU   A CD1 1 
ATOM   781  C CD2 . LEU   A 1 107 ? -17.787 -18.083 7.046   1.00 30.54 ?  107 LEU   A CD2 1 
ATOM   782  N N   . ALA   A 1 108 ? -15.613 -15.998 11.153  1.00 31.83 ?  108 ALA   A N   1 
ATOM   783  C CA  . ALA   A 1 108 ? -15.733 -16.296 12.578  1.00 32.29 ?  108 ALA   A CA  1 
ATOM   784  C C   . ALA   A 1 108 ? -15.815 -15.019 13.392  1.00 33.67 ?  108 ALA   A C   1 
ATOM   785  O O   . ALA   A 1 108 ? -16.660 -14.888 14.285  1.00 30.73 ?  108 ALA   A O   1 
ATOM   786  C CB  . ALA   A 1 108 ? -14.548 -17.131 13.047  1.00 29.77 ?  108 ALA   A CB  1 
ATOM   787  N N   . VAL   A 1 109 ? -14.920 -14.069 13.101  1.00 31.05 ?  109 VAL   A N   1 
ATOM   788  C CA  . VAL   A 1 109 ? -14.922 -12.795 13.809  1.00 26.45 ?  109 VAL   A CA  1 
ATOM   789  C C   . VAL   A 1 109 ? -16.233 -12.058 13.577  1.00 30.44 ?  109 VAL   A C   1 
ATOM   790  O O   . VAL   A 1 109 ? -16.870 -11.575 14.522  1.00 29.41 ?  109 VAL   A O   1 
ATOM   791  C CB  . VAL   A 1 109 ? -13.716 -11.953 13.368  1.00 32.03 ?  109 VAL   A CB  1 
ATOM   792  C CG1 . VAL   A 1 109 ? -13.714 -10.613 14.086  1.00 36.56 ?  109 VAL   A CG1 1 
ATOM   793  C CG2 . VAL   A 1 109 ? -12.412 -12.743 13.599  1.00 36.99 ?  109 VAL   A CG2 1 
ATOM   794  N N   . LEU   A 1 110 ? -16.651 -11.940 12.313  1.00 29.99 ?  110 LEU   A N   1 
ATOM   795  C CA  . LEU   A 1 110 ? -17.866 -11.178 12.042  1.00 33.69 ?  110 LEU   A CA  1 
ATOM   796  C C   . LEU   A 1 110 ? -19.051 -11.779 12.785  1.00 39.07 ?  110 LEU   A C   1 
ATOM   797  O O   . LEU   A 1 110 ? -19.820 -11.054 13.423  1.00 30.59 ?  110 LEU   A O   1 
ATOM   798  C CB  . LEU   A 1 110 ? -18.150 -11.119 10.543  1.00 27.89 ?  110 LEU   A CB  1 
ATOM   799  C CG  . LEU   A 1 110 ? -19.493 -10.465 10.192  1.00 30.39 ?  110 LEU   A CG  1 
ATOM   800  C CD1 . LEU   A 1 110 ? -19.547 -9.030  10.671  1.00 34.41 ?  110 LEU   A CD1 1 
ATOM   801  C CD2 . LEU   A 1 110 ? -19.729 -10.539 8.705   1.00 33.88 ?  110 LEU   A CD2 1 
ATOM   802  N N   . ASP   A 1 111 ? -19.178 -13.115 12.758  1.00 30.31 ?  111 ASP   A N   1 
ATOM   803  C CA  . ASP   A 1 111 ? -20.336 -13.762 13.364  1.00 31.26 ?  111 ASP   A CA  1 
ATOM   804  C C   . ASP   A 1 111 ? -20.370 -13.575 14.881  1.00 35.20 ?  111 ASP   A C   1 
ATOM   805  O O   . ASP   A 1 111 ? -21.457 -13.499 15.465  1.00 34.86 ?  111 ASP   A O   1 
ATOM   806  C CB  . ASP   A 1 111 ? -20.337 -15.261 13.029  1.00 32.46 ?  111 ASP   A CB  1 
ATOM   807  C CG  . ASP   A 1 111 ? -20.809 -15.564 11.601  1.00 48.42 ?  111 ASP   A CG  1 
ATOM   808  O OD1 . ASP   A 1 111 ? -21.580 -14.768 11.004  1.00 46.27 ?  111 ASP   A OD1 1 
ATOM   809  O OD2 . ASP   A 1 111 ? -20.410 -16.625 11.069  1.00 46.34 -1 111 ASP   A OD2 1 
ATOM   810  N N   . SER   A 1 112 ? -19.204 -13.504 15.539  1.00 28.24 ?  112 SER   A N   1 
ATOM   811  C CA  . SER   A 1 112 ? -19.180 -13.482 16.992  1.00 29.94 ?  112 SER   A CA  1 
ATOM   812  C C   . SER   A 1 112 ? -19.537 -12.099 17.544  1.00 35.06 ?  112 SER   A C   1 
ATOM   813  O O   . SER   A 1 112 ? -19.805 -11.980 18.742  1.00 39.86 ?  112 SER   A O   1 
ATOM   814  C CB  . SER   A 1 112 ? -17.786 -13.870 17.505  1.00 35.77 ?  112 SER   A CB  1 
ATOM   815  O OG  . SER   A 1 112 ? -16.867 -12.822 17.196  1.00 41.98 ?  112 SER   A OG  1 
ATOM   816  N N   . VAL   A 1 113 ? -19.508 -11.050 16.713  1.00 27.09 ?  113 VAL   A N   1 
ATOM   817  C CA  . VAL   A 1 113 ? -19.864 -9.704  17.149  1.00 33.97 ?  113 VAL   A CA  1 
ATOM   818  C C   . VAL   A 1 113 ? -21.108 -9.161  16.458  1.00 38.67 ?  113 VAL   A C   1 
ATOM   819  O O   . VAL   A 1 113 ? -21.684 -8.183  16.950  1.00 34.89 ?  113 VAL   A O   1 
ATOM   820  C CB  . VAL   A 1 113 ? -18.683 -8.729  16.939  1.00 31.13 ?  113 VAL   A CB  1 
ATOM   821  C CG1 . VAL   A 1 113 ? -17.432 -9.246  17.654  1.00 34.11 ?  113 VAL   A CG1 1 
ATOM   822  C CG2 . VAL   A 1 113 ? -18.439 -8.549  15.457  1.00 34.74 ?  113 VAL   A CG2 1 
ATOM   823  N N   . ALA   A 1 114 ? -21.529 -9.755  15.341  1.00 42.17 ?  114 ALA   A N   1 
ATOM   824  C CA  . ALA   A 1 114 ? -22.686 -9.272  14.592  1.00 41.55 ?  114 ALA   A CA  1 
ATOM   825  C C   . ALA   A 1 114 ? -23.922 -9.022  15.451  1.00 41.20 ?  114 ALA   A C   1 
ATOM   826  O O   . ALA   A 1 114 ? -24.567 -7.978  15.253  1.00 43.24 ?  114 ALA   A O   1 
ATOM   827  C CB  . ALA   A 1 114 ? -23.022 -10.262 13.463  1.00 42.79 ?  114 ALA   A CB  1 
ATOM   828  N N   . PRO   A 1 115 ? -24.301 -9.892  16.397  1.00 36.06 ?  115 PRO   A N   1 
ATOM   829  C CA  . PRO   A 1 115 ? -25.506 -9.610  17.188  1.00 50.04 ?  115 PRO   A CA  1 
ATOM   830  C C   . PRO   A 1 115 ? -25.406 -8.339  18.022  1.00 51.75 ?  115 PRO   A C   1 
ATOM   831  O O   . PRO   A 1 115 ? -26.431 -7.691  18.258  1.00 42.55 ?  115 PRO   A O   1 
ATOM   832  C CB  . PRO   A 1 115 ? -25.644 -10.866 18.066  1.00 46.28 ?  115 PRO   A CB  1 
ATOM   833  C CG  . PRO   A 1 115 ? -24.892 -11.920 17.327  1.00 42.12 ?  115 PRO   A CG  1 
ATOM   834  C CD  . PRO   A 1 115 ? -23.736 -11.208 16.741  1.00 38.69 ?  115 PRO   A CD  1 
ATOM   835  N N   . LEU   A 1 116 ? -24.207 -7.949  18.465  1.00 45.96 ?  116 LEU   A N   1 
ATOM   836  C CA  . LEU   A 1 116 ? -24.080 -6.746  19.285  1.00 44.25 ?  116 LEU   A CA  1 
ATOM   837  C C   . LEU   A 1 116 ? -24.337 -5.457  18.505  1.00 49.71 ?  116 LEU   A C   1 
ATOM   838  O O   . LEU   A 1 116 ? -24.698 -4.441  19.114  1.00 49.14 ?  116 LEU   A O   1 
ATOM   839  C CB  . LEU   A 1 116 ? -22.696 -6.704  19.933  1.00 36.36 ?  116 LEU   A CB  1 
ATOM   840  C CG  . LEU   A 1 116 ? -22.307 -8.085  20.480  1.00 45.31 ?  116 LEU   A CG  1 
ATOM   841  C CD1 . LEU   A 1 116 ? -20.852 -8.145  20.956  1.00 35.94 ?  116 LEU   A CD1 1 
ATOM   842  C CD2 . LEU   A 1 116 ? -23.285 -8.453  21.591  1.00 49.21 ?  116 LEU   A CD2 1 
ATOM   843  N N   . ILE   A 1 117 ? -24.172 -5.471  17.188  1.00 45.76 ?  117 ILE   A N   1 
ATOM   844  C CA  . ILE   A 1 117 ? -24.294 -4.258  16.395  1.00 50.35 ?  117 ILE   A CA  1 
ATOM   845  C C   . ILE   A 1 117 ? -25.677 -4.123  15.761  1.00 55.79 ?  117 ILE   A C   1 
ATOM   846  O O   . ILE   A 1 117 ? -26.155 -3.006  15.535  1.00 55.63 ?  117 ILE   A O   1 
ATOM   847  C CB  . ILE   A 1 117 ? -23.206 -4.203  15.319  1.00 47.83 ?  117 ILE   A CB  1 
ATOM   848  C CG1 . ILE   A 1 117 ? -21.846 -4.559  15.921  1.00 50.22 ?  117 ILE   A CG1 1 
ATOM   849  C CG2 . ILE   A 1 117 ? -23.130 -2.815  14.730  1.00 59.80 ?  117 ILE   A CG2 1 
ATOM   850  C CD1 . ILE   A 1 117 ? -20.853 -5.045  14.897  1.00 43.46 ?  117 ILE   A CD1 1 
ATOM   851  N N   . GLU   A 1 123 ? -23.505 -2.378  5.102   1.00 61.33 ?  123 GLU   A N   1 
ATOM   852  C CA  . GLU   A 1 123 ? -22.332 -1.587  5.470   1.00 53.59 ?  123 GLU   A CA  1 
ATOM   853  C C   . GLU   A 1 123 ? -21.403 -2.410  6.372   1.00 48.16 ?  123 GLU   A C   1 
ATOM   854  O O   . GLU   A 1 123 ? -20.238 -2.054  6.577   1.00 44.19 ?  123 GLU   A O   1 
ATOM   855  C CB  . GLU   A 1 123 ? -22.749 -0.318  6.202   1.00 53.08 ?  123 GLU   A CB  1 
ATOM   856  C CG  . GLU   A 1 123 ? -23.467 -0.650  7.485   1.00 54.39 ?  123 GLU   A CG  1 
ATOM   857  C CD  . GLU   A 1 123 ? -24.951 -0.638  7.298   1.00 57.10 ?  123 GLU   A CD  1 
ATOM   858  O OE1 . GLU   A 1 123 ? -25.391 -1.068  6.215   1.00 58.74 ?  123 GLU   A OE1 1 
ATOM   859  O OE2 . GLU   A 1 123 ? -25.676 -0.262  8.243   1.00 78.74 -1 123 GLU   A OE2 1 
ATOM   860  N N   . THR   A 1 124 ? -21.967 -3.484  6.919   1.00 47.77 ?  124 THR   A N   1 
ATOM   861  C CA  . THR   A 1 124 ? -21.292 -4.395  7.833   1.00 46.82 ?  124 THR   A CA  1 
ATOM   862  C C   . THR   A 1 124 ? -21.094 -5.733  7.135   1.00 46.38 ?  124 THR   A C   1 
ATOM   863  O O   . THR   A 1 124 ? -22.018 -6.245  6.497   1.00 45.96 ?  124 THR   A O   1 
ATOM   864  C CB  . THR   A 1 124 ? -22.099 -4.583  9.128   1.00 49.47 ?  124 THR   A CB  1 
ATOM   865  O OG1 . THR   A 1 124 ? -21.292 -5.250  10.108  1.00 48.01 ?  124 THR   A OG1 1 
ATOM   866  C CG2 . THR   A 1 124 ? -23.374 -5.396  8.891   1.00 45.35 ?  124 THR   A CG2 1 
ATOM   867  N N   . GLY   A 1 125 ? -19.887 -6.279  7.227   1.00 39.39 ?  125 GLY   A N   1 
ATOM   868  C CA  . GLY   A 1 125 ? -19.621 -7.564  6.607   1.00 37.47 ?  125 GLY   A CA  1 
ATOM   869  C C   . GLY   A 1 125 ? -18.138 -7.733  6.341   1.00 30.66 ?  125 GLY   A C   1 
ATOM   870  O O   . GLY   A 1 125 ? -17.305 -7.085  6.957   1.00 34.33 ?  125 GLY   A O   1 
ATOM   871  N N   . LEU   A 1 126 ? -17.841 -8.612  5.412   1.00 30.14 ?  126 LEU   A N   1 
ATOM   872  C CA  . LEU   A 1 126 ? -16.471 -8.966  5.105   1.00 37.00 ?  126 LEU   A CA  1 
ATOM   873  C C   . LEU   A 1 126 ? -16.021 -8.246  3.839   1.00 31.40 ?  126 LEU   A C   1 
ATOM   874  O O   . LEU   A 1 126 ? -16.661 -8.367  2.792   1.00 30.13 ?  126 LEU   A O   1 
ATOM   875  C CB  . LEU   A 1 126 ? -16.341 -10.481 4.953   1.00 29.34 ?  126 LEU   A CB  1 
ATOM   876  C CG  . LEU   A 1 126 ? -16.884 -11.294 6.137   1.00 30.25 ?  126 LEU   A CG  1 
ATOM   877  C CD1 . LEU   A 1 126 ? -16.720 -12.783 5.889   1.00 27.77 ?  126 LEU   A CD1 1 
ATOM   878  C CD2 . LEU   A 1 126 ? -16.195 -10.864 7.411   1.00 35.30 ?  126 LEU   A CD2 1 
ATOM   879  N N   . LYS   A 1 127 ? -14.934 -7.491  3.945   1.00 30.98 ?  127 LYS   A N   1 
ATOM   880  C CA  . LYS   A 1 127 ? -14.190 -7.035  2.775   1.00 32.37 ?  127 LYS   A CA  1 
ATOM   881  C C   . LYS   A 1 127 ? -13.213 -8.129  2.369   1.00 33.09 ?  127 LYS   A C   1 
ATOM   882  O O   . LYS   A 1 127 ? -12.436 -8.615  3.201   1.00 32.71 ?  127 LYS   A O   1 
ATOM   883  C CB  . LYS   A 1 127 ? -13.413 -5.742  3.051   1.00 41.71 ?  127 LYS   A CB  1 
ATOM   884  C CG  . LYS   A 1 127 ? -12.939 -5.029  1.769   1.00 41.55 ?  127 LYS   A CG  1 
ATOM   885  C CD  . LYS   A 1 127 ? -11.927 -3.890  2.002   1.00 44.85 ?  127 LYS   A CD  1 
ATOM   886  C CE  . LYS   A 1 127 ? -12.489 -2.728  2.806   1.00 61.53 ?  127 LYS   A CE  1 
ATOM   887  N NZ  . LYS   A 1 127 ? -11.918 -1.381  2.396   1.00 55.41 ?  127 LYS   A NZ  1 
ATOM   888  N N   . TRP   A 1 128 ? -13.246 -8.511  1.105   1.00 29.28 ?  128 TRP   A N   1 
ATOM   889  C CA  . TRP   A 1 128 ? -12.280 -9.489  0.630   1.00 32.30 ?  128 TRP   A CA  1 
ATOM   890  C C   . TRP   A 1 128 ? -10.863 -8.921  0.766   1.00 29.85 ?  128 TRP   A C   1 
ATOM   891  O O   . TRP   A 1 128 ? -10.608 -7.799  0.325   1.00 30.39 ?  128 TRP   A O   1 
ATOM   892  C CB  . TRP   A 1 128 ? -12.572 -9.877  -0.824  1.00 25.59 ?  128 TRP   A CB  1 
ATOM   893  C CG  . TRP   A 1 128 ? -11.682 -11.002 -1.328  1.00 35.69 ?  128 TRP   A CG  1 
ATOM   894  C CD1 . TRP   A 1 128 ? -11.945 -12.362 -1.299  1.00 34.72 ?  128 TRP   A CD1 1 
ATOM   895  C CD2 . TRP   A 1 128 ? -10.372 -10.862 -1.905  1.00 24.92 ?  128 TRP   A CD2 1 
ATOM   896  N NE1 . TRP   A 1 128 ? -10.871 -13.063 -1.834  1.00 27.58 ?  128 TRP   A NE1 1 
ATOM   897  C CE2 . TRP   A 1 128 ? -9.903  -12.165 -2.214  1.00 30.80 ?  128 TRP   A CE2 1 
ATOM   898  C CE3 . TRP   A 1 128 ? -9.562  -9.765  -2.199  1.00 28.56 ?  128 TRP   A CE3 1 
ATOM   899  C CZ2 . TRP   A 1 128 ? -8.663  -12.386 -2.804  1.00 30.59 ?  128 TRP   A CZ2 1 
ATOM   900  C CZ3 . TRP   A 1 128 ? -8.333  -9.987  -2.789  1.00 34.41 ?  128 TRP   A CZ3 1 
ATOM   901  C CH2 . TRP   A 1 128 ? -7.897  -11.292 -3.090  1.00 32.59 ?  128 TRP   A CH2 1 
ATOM   902  N N   . PRO   A 1 129 ? -9.909  -9.685  1.295   1.00 29.44 ?  129 PRO   A N   1 
ATOM   903  C CA  . PRO   A 1 129 ? -10.107 -11.095 1.633   1.00 34.01 ?  129 PRO   A CA  1 
ATOM   904  C C   . PRO   A 1 129 ? -10.799 -11.362 2.982   1.00 48.38 ?  129 PRO   A C   1 
ATOM   905  O O   . PRO   A 1 129 ? -11.839 -12.046 3.029   1.00 48.70 ?  129 PRO   A O   1 
ATOM   906  C CB  . PRO   A 1 129 ? -8.680  -11.640 1.649   1.00 35.98 ?  129 PRO   A CB  1 
ATOM   907  C CG  . PRO   A 1 129 ? -7.821  -10.485 1.896   1.00 35.63 ?  129 PRO   A CG  1 
ATOM   908  C CD  . PRO   A 1 129 ? -8.486  -9.303  1.298   1.00 35.54 ?  129 PRO   A CD  1 
ATOM   909  N N   . ASN   A 1 130 ? -10.256 -10.778 4.049   1.00 38.93 ?  130 ASN   A N   1 
ATOM   910  C CA  . ASN   A 1 130 ? -10.480 -11.251 5.401   1.00 49.37 ?  130 ASN   A CA  1 
ATOM   911  C C   . ASN   A 1 130 ? -10.912 -10.189 6.407   1.00 50.37 ?  130 ASN   A C   1 
ATOM   912  O O   . ASN   A 1 130 ? -11.274 -10.553 7.530   1.00 48.85 ?  130 ASN   A O   1 
ATOM   913  C CB  . ASN   A 1 130 ? -9.201  -11.949 5.896   1.00 47.37 ?  130 ASN   A CB  1 
ATOM   914  C CG  . ASN   A 1 130 ? -8.001  -10.988 5.964   1.00 59.58 ?  130 ASN   A CG  1 
ATOM   915  O OD1 . ASN   A 1 130 ? -8.158  -9.762  5.948   1.00 55.66 ?  130 ASN   A OD1 1 
ATOM   916  N ND2 . ASN   A 1 130 ? -6.785  -11.557 6.019   1.00 63.63 ?  130 ASN   A ND2 1 
ATOM   917  N N   . ASP   A 1 131 ? -10.889 -8.908  6.058   1.00 48.45 ?  131 ASP   A N   1 
ATOM   918  C CA  . ASP   A 1 131 ? -11.095 -7.872  7.056   1.00 45.05 ?  131 ASP   A CA  1 
ATOM   919  C C   . ASP   A 1 131 ? -12.593 -7.625  7.244   1.00 39.17 ?  131 ASP   A C   1 
ATOM   920  O O   . ASP   A 1 131 ? -13.393 -7.763  6.310   1.00 43.38 ?  131 ASP   A O   1 
ATOM   921  C CB  . ASP   A 1 131 ? -10.349 -6.576  6.681   1.00 48.16 ?  131 ASP   A CB  1 
ATOM   922  C CG  . ASP   A 1 131 ? -8.811  -6.618  7.037   1.00 58.21 ?  131 ASP   A CG  1 
ATOM   923  O OD1 . ASP   A 1 131 ? -8.091  -5.643  6.687   1.00 56.70 ?  131 ASP   A OD1 1 
ATOM   924  O OD2 . ASP   A 1 131 ? -8.309  -7.608  7.650   1.00 48.52 -1 131 ASP   A OD2 1 
ATOM   925  N N   . VAL   A 1 132 ? -12.967 -7.306  8.486   1.00 36.62 ?  132 VAL   A N   1 
ATOM   926  C CA  . VAL   A 1 132 ? -14.354 -7.092  8.878   1.00 28.36 ?  132 VAL   A CA  1 
ATOM   927  C C   . VAL   A 1 132 ? -14.616 -5.593  8.920   1.00 30.36 ?  132 VAL   A C   1 
ATOM   928  O O   . VAL   A 1 132 ? -13.971 -4.859  9.675   1.00 30.90 ?  132 VAL   A O   1 
ATOM   929  C CB  . VAL   A 1 132 ? -14.660 -7.741  10.234  1.00 29.77 ?  132 VAL   A CB  1 
ATOM   930  C CG1 . VAL   A 1 132 ? -16.115 -7.494  10.630  1.00 34.19 ?  132 VAL   A CG1 1 
ATOM   931  C CG2 . VAL   A 1 132 ? -14.356 -9.253  10.203  1.00 33.25 ?  132 VAL   A CG2 1 
ATOM   932  N N   . LEU   A 1 133 ? -15.570 -5.136  8.127   1.00 26.11 ?  133 LEU   A N   1 
ATOM   933  C CA  . LEU   A 1 133 ? -15.978 -3.742  8.125   1.00 30.19 ?  133 LEU   A CA  1 
ATOM   934  C C   . LEU   A 1 133 ? -17.324 -3.587  8.808   1.00 32.97 ?  133 LEU   A C   1 
ATOM   935  O O   . LEU   A 1 133 ? -18.162 -4.487  8.788   1.00 29.36 ?  133 LEU   A O   1 
ATOM   936  C CB  . LEU   A 1 133 ? -16.109 -3.189  6.710   1.00 29.11 ?  133 LEU   A CB  1 
ATOM   937  C CG  . LEU   A 1 133 ? -14.986 -3.310  5.712   1.00 32.43 ?  133 LEU   A CG  1 
ATOM   938  C CD1 . LEU   A 1 133 ? -15.276 -2.277  4.662   1.00 36.55 ?  133 LEU   A CD1 1 
ATOM   939  C CD2 . LEU   A 1 133 ? -13.626 -3.090  6.392   1.00 34.18 ?  133 LEU   A CD2 1 
ATOM   940  N N   . ALA   A 1 134 ? -17.535 -2.415  9.380   1.00 35.19 ?  134 ALA   A N   1 
ATOM   941  C CA  . ALA   A 1 134 ? -18.835 -2.049  9.913   1.00 34.88 ?  134 ALA   A CA  1 
ATOM   942  C C   . ALA   A 1 134 ? -19.001 -0.560  9.686   1.00 38.89 ?  134 ALA   A C   1 
ATOM   943  O O   . ALA   A 1 134 ? -18.136 0.224   10.086  1.00 40.58 ?  134 ALA   A O   1 
ATOM   944  C CB  . ALA   A 1 134 ? -18.944 -2.392  11.399  1.00 33.66 ?  134 ALA   A CB  1 
ATOM   945  N N   . ARG   A 1 135 ? -20.094 -0.181  9.033   1.00 35.87 ?  135 ARG   A N   1 
ATOM   946  C CA  . ARG   A 1 135 ? -20.357 1.210   8.711   1.00 39.51 ?  135 ARG   A CA  1 
ATOM   947  C C   . ARG   A 1 135 ? -19.158 1.811   7.984   1.00 38.85 ?  135 ARG   A C   1 
ATOM   948  O O   . ARG   A 1 135 ? -18.750 2.939   8.246   1.00 38.86 ?  135 ARG   A O   1 
ATOM   949  C CB  . ARG   A 1 135 ? -20.707 2.003   9.975   1.00 40.85 ?  135 ARG   A CB  1 
ATOM   950  C CG  . ARG   A 1 135 ? -21.531 3.258   9.722   1.00 51.68 ?  135 ARG   A CG  1 
ATOM   951  C CD  . ARG   A 1 135 ? -21.911 3.987   11.010  1.00 52.39 ?  135 ARG   A CD  1 
ATOM   952  N NE  . ARG   A 1 135 ? -22.974 3.321   11.767  1.00 51.03 ?  135 ARG   A NE  1 
ATOM   953  C CZ  . ARG   A 1 135 ? -23.026 3.267   13.099  1.00 54.96 ?  135 ARG   A CZ  1 
ATOM   954  N NH1 . ARG   A 1 135 ? -22.076 3.839   13.848  1.00 46.76 ?  135 ARG   A NH1 1 
ATOM   955  N NH2 . ARG   A 1 135 ? -24.035 2.646   13.692  1.00 54.09 ?  135 ARG   A NH2 1 
ATOM   956  N N   . GLY   A 1 136 ? -18.553 1.016   7.095   1.00 37.64 ?  136 GLY   A N   1 
ATOM   957  C CA  . GLY   A 1 136 ? -17.371 1.410   6.355   1.00 32.08 ?  136 GLY   A CA  1 
ATOM   958  C C   . GLY   A 1 136 ? -16.069 1.468   7.136   1.00 38.27 ?  136 GLY   A C   1 
ATOM   959  O O   . GLY   A 1 136 ? -15.006 1.591   6.519   1.00 42.12 ?  136 GLY   A O   1 
ATOM   960  N N   . GLY   A 1 137 ? -16.092 1.382   8.457   1.00 37.14 ?  137 GLY   A N   1 
ATOM   961  C CA  . GLY   A 1 137 ? -14.853 1.385   9.218   1.00 34.02 ?  137 GLY   A CA  1 
ATOM   962  C C   . GLY   A 1 137 ? -14.325 -0.023  9.434   1.00 33.10 ?  137 GLY   A C   1 
ATOM   963  O O   . GLY   A 1 137 ? -15.095 -0.972  9.555   1.00 30.81 ?  137 GLY   A O   1 
ATOM   964  N N   . LYS   A 1 138 ? -12.999 -0.149  9.528   1.00 29.13 ?  138 LYS   A N   1 
ATOM   965  C CA  . LYS   A 1 138 ? -12.383 -1.445  9.801   1.00 36.61 ?  138 LYS   A CA  1 
ATOM   966  C C   . LYS   A 1 138 ? -12.534 -1.783  11.279  1.00 29.18 ?  138 LYS   A C   1 
ATOM   967  O O   . LYS   A 1 138 ? -11.895 -1.172  12.146  1.00 29.23 ?  138 LYS   A O   1 
ATOM   968  C CB  . LYS   A 1 138 ? -10.910 -1.507  9.385   1.00 35.78 ?  138 LYS   A CB  1 
ATOM   969  C CG  . LYS   A 1 138 ? -10.474 -2.993  9.146   1.00 30.43 ?  138 LYS   A CG  1 
ATOM   970  C CD  . LYS   A 1 138 ? -8.985  -3.197  8.801   1.00 42.30 ?  138 LYS   A CD  1 
ATOM   971  C CE  . LYS   A 1 138 ? -8.526  -2.353  7.630   1.00 41.24 ?  138 LYS   A CE  1 
ATOM   972  N NZ  . LYS   A 1 138 ? -9.314  -2.622  6.388   1.00 58.01 ?  138 LYS   A NZ  1 
ATOM   973  N N   . LEU   A 1 139 ? -13.365 -2.785  11.549  1.00 28.29 ?  139 LEU   A N   1 
ATOM   974  C CA  . LEU   A 1 139 ? -13.687 -3.320  12.864  1.00 25.29 ?  139 LEU   A CA  1 
ATOM   975  C C   . LEU   A 1 139 ? -12.699 -4.394  13.326  1.00 26.92 ?  139 LEU   A C   1 
ATOM   976  O O   . LEU   A 1 139 ? -12.403 -4.489  14.519  1.00 30.94 ?  139 LEU   A O   1 
ATOM   977  C CB  . LEU   A 1 139 ? -15.112 -3.894  12.829  1.00 23.75 ?  139 LEU   A CB  1 
ATOM   978  C CG  . LEU   A 1 139 ? -15.576 -4.611  14.087  1.00 24.26 ?  139 LEU   A CG  1 
ATOM   979  C CD1 . LEU   A 1 139 ? -15.449 -3.626  15.245  1.00 30.05 ?  139 LEU   A CD1 1 
ATOM   980  C CD2 . LEU   A 1 139 ? -17.001 -5.066  13.949  1.00 26.40 ?  139 LEU   A CD2 1 
ATOM   981  N N   . ALA   A 1 140 ? -12.205 -5.230  12.416  1.00 23.01 ?  140 ALA   A N   1 
ATOM   982  C CA  . ALA   A 1 140 ? -11.230 -6.257  12.768  1.00 29.53 ?  140 ALA   A CA  1 
ATOM   983  C C   . ALA   A 1 140 ? -10.304 -6.517  11.582  1.00 29.04 ?  140 ALA   A C   1 
ATOM   984  O O   . ALA   A 1 140 ? -10.694 -6.388  10.423  1.00 36.31 ?  140 ALA   A O   1 
ATOM   985  C CB  . ALA   A 1 140 ? -11.904 -7.572  13.191  1.00 21.38 ?  140 ALA   A CB  1 
ATOM   986  N N   . GLY   A 1 141 ? -9.071  -6.871  11.885  1.00 32.70 ?  141 GLY   A N   1 
ATOM   987  C CA  . GLY   A 1 141 ? -8.106  -7.271  10.873  1.00 28.71 ?  141 GLY   A CA  1 
ATOM   988  C C   . GLY   A 1 141 ? -7.745  -8.724  11.103  1.00 32.22 ?  141 GLY   A C   1 
ATOM   989  O O   . GLY   A 1 141 ? -7.616  -9.162  12.256  1.00 33.61 ?  141 GLY   A O   1 
ATOM   990  N N   . ILE   A 1 142 ? -7.619  -9.473  10.007  1.00 35.20 ?  142 ILE   A N   1 
ATOM   991  C CA  . ILE   A 1 142 ? -7.203  -10.873 10.022  1.00 35.81 ?  142 ILE   A CA  1 
ATOM   992  C C   . ILE   A 1 142 ? -5.871  -10.992 9.287   1.00 37.87 ?  142 ILE   A C   1 
ATOM   993  O O   . ILE   A 1 142 ? -5.705  -10.425 8.206   1.00 35.84 ?  142 ILE   A O   1 
ATOM   994  C CB  . ILE   A 1 142 ? -8.234  -11.809 9.354   1.00 37.12 ?  142 ILE   A CB  1 
ATOM   995  C CG1 . ILE   A 1 142 ? -9.660  -11.640 9.925   1.00 40.33 ?  142 ILE   A CG1 1 
ATOM   996  C CG2 . ILE   A 1 142 ? -7.728  -13.248 9.356   1.00 36.33 ?  142 ILE   A CG2 1 
ATOM   997  C CD1 . ILE   A 1 142 ? -9.745  -11.525 11.406  1.00 39.86 ?  142 ILE   A CD1 1 
ATOM   998  N N   . LEU   A 1 143 ? -4.949  -11.783 9.837   1.00 37.20 ?  143 LEU   A N   1 
ATOM   999  C CA  . LEU   A 1 143 ? -3.667  -12.040 9.188   1.00 37.96 ?  143 LEU   A CA  1 
ATOM   1000 C C   . LEU   A 1 143 ? -3.250  -13.474 9.461   1.00 30.10 ?  143 LEU   A C   1 
ATOM   1001 O O   . LEU   A 1 143 ? -2.991  -13.832 10.613  1.00 34.90 ?  143 LEU   A O   1 
ATOM   1002 C CB  . LEU   A 1 143 ? -2.581  -11.077 9.672   1.00 30.22 ?  143 LEU   A CB  1 
ATOM   1003 C CG  . LEU   A 1 143 ? -1.184  -11.339 9.098   1.00 39.87 ?  143 LEU   A CG  1 
ATOM   1004 C CD1 . LEU   A 1 143 ? -1.035  -10.818 7.667   1.00 38.01 ?  143 LEU   A CD1 1 
ATOM   1005 C CD2 . LEU   A 1 143 ? -0.162  -10.667 9.999   1.00 44.40 ?  143 LEU   A CD2 1 
ATOM   1006 N N   . ALA   A 1 144 ? -3.173  -14.276 8.406   1.00 29.89 ?  144 ALA   A N   1 
ATOM   1007 C CA  . ALA   A 1 144 ? -2.701  -15.655 8.480   1.00 37.92 ?  144 ALA   A CA  1 
ATOM   1008 C C   . ALA   A 1 144 ? -1.311  -15.707 7.885   1.00 30.90 ?  144 ALA   A C   1 
ATOM   1009 O O   . ALA   A 1 144 ? -1.077  -15.141 6.820   1.00 32.92 ?  144 ALA   A O   1 
ATOM   1010 C CB  . ALA   A 1 144 ? -3.613  -16.620 7.719   1.00 36.89 ?  144 ALA   A CB  1 
ATOM   1011 N N   . GLU   A 1 145 ? -0.397  -16.379 8.571   1.00 30.73 ?  145 GLU   A N   1 
ATOM   1012 C CA  . GLU   A 1 145 ? 0.952   -16.572 8.084   1.00 27.65 ?  145 GLU   A CA  1 
ATOM   1013 C C   . GLU   A 1 145 ? 1.281   -18.052 8.198   1.00 35.61 ?  145 GLU   A C   1 
ATOM   1014 O O   . GLU   A 1 145 ? 0.586   -18.805 8.880   1.00 35.33 ?  145 GLU   A O   1 
ATOM   1015 C CB  . GLU   A 1 145 ? 1.954   -15.708 8.868   1.00 29.13 ?  145 GLU   A CB  1 
ATOM   1016 C CG  . GLU   A 1 145 ? 1.441   -14.265 9.072   1.00 37.10 ?  145 GLU   A CG  1 
ATOM   1017 C CD  . GLU   A 1 145 ? 2.485   -13.324 9.650   1.00 43.58 ?  145 GLU   A CD  1 
ATOM   1018 O OE1 . GLU   A 1 145 ? 2.315   -12.886 10.805  1.00 44.83 ?  145 GLU   A OE1 1 
ATOM   1019 O OE2 . GLU   A 1 145 ? 3.478   -13.022 8.945   1.00 48.05 -1 145 GLU   A OE2 1 
ATOM   1020 N N   . VAL   A 1 146 ? 2.340   -18.466 7.513   1.00 38.04 ?  146 VAL   A N   1 
ATOM   1021 C CA  . VAL   A 1 146 ? 2.655   -19.876 7.304   1.00 36.65 ?  146 VAL   A CA  1 
ATOM   1022 C C   . VAL   A 1 146 ? 3.895   -20.232 8.099   1.00 36.76 ?  146 VAL   A C   1 
ATOM   1023 O O   . VAL   A 1 146 ? 4.885   -19.500 8.066   1.00 36.11 ?  146 VAL   A O   1 
ATOM   1024 C CB  . VAL   A 1 146 ? 2.877   -20.180 5.811   1.00 39.17 ?  146 VAL   A CB  1 
ATOM   1025 C CG1 . VAL   A 1 146 ? 3.112   -21.685 5.599   1.00 38.05 ?  146 VAL   A CG1 1 
ATOM   1026 C CG2 . VAL   A 1 146 ? 1.715   -19.655 4.986   1.00 28.75 ?  146 VAL   A CG2 1 
ATOM   1027 N N   . ALA   A 1 147 ? 3.848   -21.373 8.802   1.00 38.91 ?  147 ALA   A N   1 
ATOM   1028 C CA  . ALA   A 1 147 ? 5.023   -21.912 9.505   1.00 39.97 ?  147 ALA   A CA  1 
ATOM   1029 C C   . ALA   A 1 147 ? 4.872   -23.432 9.494   1.00 44.39 ?  147 ALA   A C   1 
ATOM   1030 O O   . ALA   A 1 147 ? 4.468   -24.022 10.504  1.00 43.68 ?  147 ALA   A O   1 
ATOM   1031 C CB  . ALA   A 1 147 ? 5.154   -21.381 10.931  1.00 37.64 ?  147 ALA   A CB  1 
ATOM   1032 N N   . GLN   A 1 148 ? 5.197   -24.034 8.337   1.00 38.42 ?  148 GLN   A N   1 
ATOM   1033 C CA  . GLN   A 1 148 ? 4.900   -25.437 8.067   1.00 37.24 ?  148 GLN   A CA  1 
ATOM   1034 C C   . GLN   A 1 148 ? 5.316   -26.304 9.252   1.00 33.27 ?  148 GLN   A C   1 
ATOM   1035 O O   . GLN   A 1 148 ? 6.421   -26.127 9.777   1.00 39.68 ?  148 GLN   A O   1 
ATOM   1036 C CB  . GLN   A 1 148 ? 5.616   -25.910 6.798   1.00 40.31 ?  148 GLN   A CB  1 
ATOM   1037 C CG  . GLN   A 1 148 ? 5.083   -25.284 5.513   1.00 47.80 ?  148 GLN   A CG  1 
ATOM   1038 C CD  . GLN   A 1 148 ? 6.054   -25.411 4.335   1.00 53.99 ?  148 GLN   A CD  1 
ATOM   1039 O OE1 . GLN   A 1 148 ? 6.063   -26.419 3.628   1.00 52.78 ?  148 GLN   A OE1 1 
ATOM   1040 N NE2 . GLN   A 1 148 ? 6.868   -24.370 4.116   1.00 43.62 ?  148 GLN   A NE2 1 
ATOM   1041 N N   . PRO   A 1 149 ? 4.470   -27.259 9.693   1.00 30.51 ?  149 PRO   A N   1 
ATOM   1042 C CA  . PRO   A 1 149 ? 3.211   -27.639 9.036   1.00 38.24 ?  149 PRO   A CA  1 
ATOM   1043 C C   . PRO   A 1 149 ? 1.977   -26.788 9.423   1.00 36.01 ?  149 PRO   A C   1 
ATOM   1044 O O   . PRO   A 1 149 ? 0.845   -27.252 9.261   1.00 32.34 ?  149 PRO   A O   1 
ATOM   1045 C CB  . PRO   A 1 149 ? 3.015   -29.085 9.512   1.00 36.22 ?  149 PRO   A CB  1 
ATOM   1046 C CG  . PRO   A 1 149 ? 3.545   -29.091 10.896  1.00 27.15 ?  149 PRO   A CG  1 
ATOM   1047 C CD  . PRO   A 1 149 ? 4.700   -28.064 10.908  1.00 35.23 ?  149 PRO   A CD  1 
ATOM   1048 N N   . PHE   A 1 150 ? 2.182   -25.559 9.896   1.00 30.25 ?  150 PHE   A N   1 
ATOM   1049 C CA  . PHE   A 1 150 ? 1.113   -24.798 10.520  1.00 31.81 ?  150 PHE   A CA  1 
ATOM   1050 C C   . PHE   A 1 150 ? 0.809   -23.526 9.742   1.00 36.50 ?  150 PHE   A C   1 
ATOM   1051 O O   . PHE   A 1 150 ? 1.659   -22.981 9.042   1.00 32.73 ?  150 PHE   A O   1 
ATOM   1052 C CB  . PHE   A 1 150 ? 1.467   -24.382 11.955  1.00 32.06 ?  150 PHE   A CB  1 
ATOM   1053 C CG  . PHE   A 1 150 ? 1.746   -25.527 12.884  1.00 36.25 ?  150 PHE   A CG  1 
ATOM   1054 C CD1 . PHE   A 1 150 ? 0.719   -26.355 13.321  1.00 30.72 ?  150 PHE   A CD1 1 
ATOM   1055 C CD2 . PHE   A 1 150 ? 3.039   -25.757 13.337  1.00 33.12 ?  150 PHE   A CD2 1 
ATOM   1056 C CE1 . PHE   A 1 150 ? 0.983   -27.393 14.191  1.00 31.78 ?  150 PHE   A CE1 1 
ATOM   1057 C CE2 . PHE   A 1 150 ? 3.313   -26.801 14.204  1.00 37.41 ?  150 PHE   A CE2 1 
ATOM   1058 C CZ  . PHE   A 1 150 ? 2.285   -27.620 14.635  1.00 35.58 ?  150 PHE   A CZ  1 
ATOM   1059 N N   . VAL   A 1 151 ? -0.417  -23.038 9.919   1.00 30.66 ?  151 VAL   A N   1 
ATOM   1060 C CA  . VAL   A 1 151 ? -0.764  -21.649 9.658   1.00 29.75 ?  151 VAL   A CA  1 
ATOM   1061 C C   . VAL   A 1 151 ? -1.031  -21.012 11.010  1.00 27.71 ?  151 VAL   A C   1 
ATOM   1062 O O   . VAL   A 1 151 ? -1.628  -21.643 11.894  1.00 33.20 ?  151 VAL   A O   1 
ATOM   1063 C CB  . VAL   A 1 151 ? -1.967  -21.535 8.703   1.00 29.87 ?  151 VAL   A CB  1 
ATOM   1064 C CG1 . VAL   A 1 151 ? -2.656  -20.146 8.803   1.00 30.91 ?  151 VAL   A CG1 1 
ATOM   1065 C CG2 . VAL   A 1 151 ? -1.498  -21.794 7.296   1.00 35.50 ?  151 VAL   A CG2 1 
ATOM   1066 N N   . VAL   A 1 152 ? -0.509  -19.810 11.204  1.00 31.91 ?  152 VAL   A N   1 
ATOM   1067 C CA  . VAL   A 1 152 ? -0.801  -18.991 12.375  1.00 28.63 ?  152 VAL   A CA  1 
ATOM   1068 C C   . VAL   A 1 152 ? -1.822  -17.947 11.958  1.00 30.13 ?  152 VAL   A C   1 
ATOM   1069 O O   . VAL   A 1 152 ? -1.591  -17.173 11.024  1.00 34.86 ?  152 VAL   A O   1 
ATOM   1070 C CB  . VAL   A 1 152 ? 0.465   -18.336 12.950  1.00 32.33 ?  152 VAL   A CB  1 
ATOM   1071 C CG1 . VAL   A 1 152 ? 0.092   -17.381 14.068  1.00 29.20 ?  152 VAL   A CG1 1 
ATOM   1072 C CG2 . VAL   A 1 152 ? 1.429   -19.409 13.465  1.00 23.71 ?  152 VAL   A CG2 1 
ATOM   1073 N N   . LEU   A 1 153 ? -2.935  -17.917 12.663  1.00 30.44 ?  153 LEU   A N   1 
ATOM   1074 C CA  . LEU   A 1 153 ? -4.106  -17.154 12.279  1.00 32.12 ?  153 LEU   A CA  1 
ATOM   1075 C C   . LEU   A 1 153 ? -4.288  -16.072 13.339  1.00 35.67 ?  153 LEU   A C   1 
ATOM   1076 O O   . LEU   A 1 153 ? -4.587  -16.380 14.494  1.00 30.40 ?  153 LEU   A O   1 
ATOM   1077 C CB  . LEU   A 1 153 ? -5.295  -18.101 12.205  1.00 30.48 ?  153 LEU   A CB  1 
ATOM   1078 C CG  . LEU   A 1 153 ? -6.543  -17.803 11.419  1.00 43.21 ?  153 LEU   A CG  1 
ATOM   1079 C CD1 . LEU   A 1 153 ? -6.124  -17.677 9.985   1.00 41.95 ?  153 LEU   A CD1 1 
ATOM   1080 C CD2 . LEU   A 1 153 ? -7.495  -19.003 11.590  1.00 34.36 ?  153 LEU   A CD2 1 
ATOM   1081 N N   . GLY   A 1 154 ? -4.093  -14.816 12.954  1.00 32.86 ?  154 GLY   A N   1 
ATOM   1082 C CA  . GLY   A 1 154 ? -4.130  -13.692 13.881  1.00 26.56 ?  154 GLY   A CA  1 
ATOM   1083 C C   . GLY   A 1 154 ? -5.399  -12.884 13.685  1.00 28.10 ?  154 GLY   A C   1 
ATOM   1084 O O   . GLY   A 1 154 ? -5.839  -12.677 12.551  1.00 33.10 ?  154 GLY   A O   1 
ATOM   1085 N N   . VAL   A 1 155 ? -5.980  -12.433 14.799  1.00 24.73 ?  155 VAL   A N   1 
ATOM   1086 C CA  . VAL   A 1 155 ? -7.154  -11.571 14.797  1.00 27.58 ?  155 VAL   A CA  1 
ATOM   1087 C C   . VAL   A 1 155 ? -6.896  -10.369 15.700  1.00 25.34 ?  155 VAL   A C   1 
ATOM   1088 O O   . VAL   A 1 155 ? -6.448  -10.517 16.841  1.00 26.58 ?  155 VAL   A O   1 
ATOM   1089 C CB  . VAL   A 1 155 ? -8.416  -12.313 15.276  1.00 32.22 ?  155 VAL   A CB  1 
ATOM   1090 C CG1 . VAL   A 1 155 ? -9.546  -11.315 15.486  1.00 28.22 ?  155 VAL   A CG1 1 
ATOM   1091 C CG2 . VAL   A 1 155 ? -8.812  -13.406 14.285  1.00 31.38 ?  155 VAL   A CG2 1 
ATOM   1092 N N   . GLY   A 1 156 ? -7.208  -9.193  15.206  1.00 25.02 ?  156 GLY   A N   1 
ATOM   1093 C CA  . GLY   A 1 156 ? -7.186  -8.005  16.038  1.00 27.98 ?  156 GLY   A CA  1 
ATOM   1094 C C   . GLY   A 1 156 ? -8.559  -7.378  15.943  1.00 29.77 ?  156 GLY   A C   1 
ATOM   1095 O O   . GLY   A 1 156 ? -8.931  -6.903  14.870  1.00 27.23 ?  156 GLY   A O   1 
ATOM   1096 N N   . LEU   A 1 157 ? -9.346  -7.428  17.014  1.00 30.53 ?  157 LEU   A N   1 
ATOM   1097 C CA  . LEU   A 1 157 ? -10.736 -6.970  16.984  1.00 25.09 ?  157 LEU   A CA  1 
ATOM   1098 C C   . LEU   A 1 157 ? -10.884 -5.735  17.866  1.00 24.28 ?  157 LEU   A C   1 
ATOM   1099 O O   . LEU   A 1 157 ? -10.640 -5.801  19.070  1.00 24.87 ?  157 LEU   A O   1 
ATOM   1100 C CB  . LEU   A 1 157 ? -11.676 -8.081  17.449  1.00 21.63 ?  157 LEU   A CB  1 
ATOM   1101 C CG  . LEU   A 1 157 ? -13.145 -7.686  17.636  1.00 25.62 ?  157 LEU   A CG  1 
ATOM   1102 C CD1 . LEU   A 1 157 ? -13.787 -7.275  16.284  1.00 18.27 ?  157 LEU   A CD1 1 
ATOM   1103 C CD2 . LEU   A 1 157 ? -13.912 -8.829  18.321  1.00 25.14 ?  157 LEU   A CD2 1 
ATOM   1104 N N   . ASN   A 1 158 ? -11.285 -4.617  17.272  1.00 23.81 ?  158 ASN   A N   1 
ATOM   1105 C CA  . ASN   A 1 158 ? -11.396 -3.357  18.012  1.00 26.89 ?  158 ASN   A CA  1 
ATOM   1106 C C   . ASN   A 1 158 ? -12.662 -3.398  18.866  1.00 30.46 ?  158 ASN   A C   1 
ATOM   1107 O O   . ASN   A 1 158 ? -13.772 -3.281  18.341  1.00 29.96 ?  158 ASN   A O   1 
ATOM   1108 C CB  . ASN   A 1 158 ? -11.465 -2.164  17.059  1.00 24.02 ?  158 ASN   A CB  1 
ATOM   1109 C CG  . ASN   A 1 158 ? -10.202 -1.949  16.258  1.00 27.80 ?  158 ASN   A CG  1 
ATOM   1110 O OD1 . ASN   A 1 158 ? -10.279 -1.637  15.080  1.00 33.38 ?  158 ASN   A OD1 1 
ATOM   1111 N ND2 . ASN   A 1 158 ? -9.041  -2.073  16.887  1.00 25.25 ?  158 ASN   A ND2 1 
ATOM   1112 N N   . VAL   A 1 159 ? -12.511 -3.527  20.179  1.00 31.54 ?  159 VAL   A N   1 
ATOM   1113 C CA  . VAL   A 1 159 ? -13.664 -3.653  21.062  1.00 30.04 ?  159 VAL   A CA  1 
ATOM   1114 C C   . VAL   A 1 159 ? -14.055 -2.282  21.613  1.00 32.63 ?  159 VAL   A C   1 
ATOM   1115 O O   . VAL   A 1 159 ? -15.181 -1.813  21.409  1.00 28.85 ?  159 VAL   A O   1 
ATOM   1116 C CB  . VAL   A 1 159 ? -13.375 -4.669  22.182  1.00 26.91 ?  159 VAL   A CB  1 
ATOM   1117 C CG1 . VAL   A 1 159 ? -14.503 -4.706  23.173  1.00 27.90 ?  159 VAL   A CG1 1 
ATOM   1118 C CG2 . VAL   A 1 159 ? -13.208 -6.040  21.566  1.00 29.61 ?  159 VAL   A CG2 1 
ATOM   1119 N N   . THR   A 1 160 ? -13.132 -1.616  22.297  1.00 33.54 ?  160 THR   A N   1 
ATOM   1120 C CA  . THR   A 1 160 ? -13.336 -0.223  22.677  1.00 32.13 ?  160 THR   A CA  1 
ATOM   1121 C C   . THR   A 1 160 ? -12.270 0.666   22.068  1.00 33.43 ?  160 THR   A C   1 
ATOM   1122 O O   . THR   A 1 160 ? -12.067 1.800   22.528  1.00 37.76 ?  160 THR   A O   1 
ATOM   1123 C CB  . THR   A 1 160 ? -13.344 -0.044  24.202  1.00 35.63 ?  160 THR   A CB  1 
ATOM   1124 O OG1 . THR   A 1 160 ? -12.061 -0.411  24.718  1.00 32.79 ?  160 THR   A OG1 1 
ATOM   1125 C CG2 . THR   A 1 160 ? -14.457 -0.868  24.887  1.00 30.86 ?  160 THR   A CG2 1 
ATOM   1126 N N   . GLN   A 1 161 ? -11.563 0.171   21.062  1.00 32.67 ?  161 GLN   A N   1 
ATOM   1127 C CA  . GLN   A 1 161 ? -10.449 0.923   20.510  1.00 29.10 ?  161 GLN   A CA  1 
ATOM   1128 C C   . GLN   A 1 161 ? -10.950 2.124   19.720  1.00 41.83 ?  161 GLN   A C   1 
ATOM   1129 O O   . GLN   A 1 161 ? -11.830 1.995   18.859  1.00 35.91 ?  161 GLN   A O   1 
ATOM   1130 C CB  . GLN   A 1 161 ? -9.601  0.041   19.615  1.00 29.30 ?  161 GLN   A CB  1 
ATOM   1131 C CG  . GLN   A 1 161 ? -8.359  0.758   19.160  1.00 36.04 ?  161 GLN   A CG  1 
ATOM   1132 C CD  . GLN   A 1 161 ? -7.229  0.577   20.148  1.00 35.51 ?  161 GLN   A CD  1 
ATOM   1133 O OE1 . GLN   A 1 161 ? -6.608  -0.478  20.195  1.00 33.79 ?  161 GLN   A OE1 1 
ATOM   1134 N NE2 . GLN   A 1 161 ? -6.994  1.581   20.972  1.00 38.13 ?  161 GLN   A NE2 1 
ATOM   1135 N N   . ALA   A 1 162 ? -10.372 3.291   20.000  1.00 37.83 ?  162 ALA   A N   1 
ATOM   1136 C CA  . ALA   A 1 162 ? -10.856 4.485   19.327  1.00 42.94 ?  162 ALA   A CA  1 
ATOM   1137 C C   . ALA   A 1 162 ? -10.045 4.767   18.083  1.00 39.51 ?  162 ALA   A C   1 
ATOM   1138 O O   . ALA   A 1 162 ? -8.814  4.583   18.089  1.00 37.10 ?  162 ALA   A O   1 
ATOM   1139 C CB  . ALA   A 1 162 ? -10.773 5.701   20.235  1.00 36.81 ?  162 ALA   A CB  1 
ATOM   1140 N N   . PRO   A 1 163 ? -10.751 5.218   17.037  1.00 33.88 ?  163 PRO   A N   1 
ATOM   1141 C CA  . PRO   A 1 163 ? -10.058 5.549   15.789  1.00 35.05 ?  163 PRO   A CA  1 
ATOM   1142 C C   . PRO   A 1 163 ? -8.871  6.462   16.020  1.00 38.32 ?  163 PRO   A C   1 
ATOM   1143 O O   . PRO   A 1 163 ? -7.790  6.214   15.466  1.00 37.43 ?  163 PRO   A O   1 
ATOM   1144 C CB  . PRO   A 1 163 ? -11.159 6.210   14.946  1.00 37.37 ?  163 PRO   A CB  1 
ATOM   1145 C CG  . PRO   A 1 163 ? -12.433 5.601   15.460  1.00 38.40 ?  163 PRO   A CG  1 
ATOM   1146 C CD  . PRO   A 1 163 ? -12.217 5.327   16.918  1.00 38.50 ?  163 PRO   A CD  1 
ATOM   1147 N N   . GLU   A 1 164 ? -9.032  7.498   16.856  1.00 35.99 ?  164 GLU   A N   1 
ATOM   1148 C CA  . GLU   A 1 164 ? -7.931  8.418   17.123  1.00 39.74 ?  164 GLU   A CA  1 
ATOM   1149 C C   . GLU   A 1 164 ? -6.753  7.735   17.802  1.00 43.21 ?  164 GLU   A C   1 
ATOM   1150 O O   . GLU   A 1 164 ? -5.664  8.318   17.842  1.00 41.67 ?  164 GLU   A O   1 
ATOM   1151 C CB  . GLU   A 1 164 ? -8.405  9.596   17.980  1.00 36.26 ?  164 GLU   A CB  1 
ATOM   1152 C CG  . GLU   A 1 164 ? -8.952  9.193   19.332  1.00 41.44 ?  164 GLU   A CG  1 
ATOM   1153 C CD  . GLU   A 1 164 ? -9.680  10.327  20.046  1.00 47.84 ?  164 GLU   A CD  1 
ATOM   1154 O OE1 . GLU   A 1 164 ? -9.287  10.653  21.189  1.00 45.15 ?  164 GLU   A OE1 1 
ATOM   1155 O OE2 . GLU   A 1 164 ? -10.642 10.885  19.468  1.00 51.96 -1 164 GLU   A OE2 1 
ATOM   1156 N N   . GLU   A 1 165 ? -6.931  6.522   18.332  1.00 44.44 ?  165 GLU   A N   1 
ATOM   1157 C CA  . GLU   A 1 165 ? -5.815  5.799   18.932  1.00 37.63 ?  165 GLU   A CA  1 
ATOM   1158 C C   . GLU   A 1 165 ? -5.008  4.986   17.927  1.00 38.14 ?  165 GLU   A C   1 
ATOM   1159 O O   . GLU   A 1 165 ? -3.836  4.702   18.191  1.00 40.99 ?  165 GLU   A O   1 
ATOM   1160 C CB  . GLU   A 1 165 ? -6.307  4.851   20.021  1.00 39.39 ?  165 GLU   A CB  1 
ATOM   1161 C CG  . GLU   A 1 165 ? -6.414  5.433   21.410  1.00 43.67 ?  165 GLU   A CG  1 
ATOM   1162 C CD  . GLU   A 1 165 ? -7.215  4.519   22.327  1.00 42.31 ?  165 GLU   A CD  1 
ATOM   1163 O OE1 . GLU   A 1 165 ? -8.309  4.069   21.894  1.00 39.38 ?  165 GLU   A OE1 1 
ATOM   1164 O OE2 . GLU   A 1 165 ? -6.767  4.248   23.467  1.00 41.84 -1 165 GLU   A OE2 1 
ATOM   1165 N N   . VAL   A 1 166 ? -5.587  4.583   16.794  1.00 39.73 ?  166 VAL   A N   1 
ATOM   1166 C CA  . VAL   A 1 166 ? -4.918  3.572   15.978  1.00 33.53 ?  166 VAL   A CA  1 
ATOM   1167 C C   . VAL   A 1 166 ? -4.908  3.915   14.494  1.00 34.17 ?  166 VAL   A C   1 
ATOM   1168 O O   . VAL   A 1 166 ? -3.930  3.631   13.801  1.00 42.38 ?  166 VAL   A O   1 
ATOM   1169 C CB  . VAL   A 1 166 ? -5.563  2.184   16.191  1.00 33.64 ?  166 VAL   A CB  1 
ATOM   1170 C CG1 . VAL   A 1 166 ? -5.287  1.667   17.578  1.00 29.42 ?  166 VAL   A CG1 1 
ATOM   1171 C CG2 . VAL   A 1 166 ? -7.087  2.209   15.874  1.00 29.69 ?  166 VAL   A CG2 1 
ATOM   1172 N N   . ASP   A 1 167 ? -6.002  4.489   13.979  1.00 38.25 ?  167 ASP   A N   1 
ATOM   1173 C CA  . ASP   A 1 167 ? -6.166  4.651   12.537  1.00 34.92 ?  167 ASP   A CA  1 
ATOM   1174 C C   . ASP   A 1 167 ? -7.426  5.443   12.210  1.00 43.10 ?  167 ASP   A C   1 
ATOM   1175 O O   . ASP   A 1 167 ? -8.488  5.192   12.795  1.00 38.98 ?  167 ASP   A O   1 
ATOM   1176 C CB  . ASP   A 1 167 ? -6.228  3.287   11.850  1.00 35.18 ?  167 ASP   A CB  1 
ATOM   1177 C CG  . ASP   A 1 167 ? -6.166  3.387   10.341  1.00 43.72 ?  167 ASP   A CG  1 
ATOM   1178 O OD1 . ASP   A 1 167 ? -5.036  3.456   9.788   1.00 43.25 ?  167 ASP   A OD1 1 
ATOM   1179 O OD2 . ASP   A 1 167 ? -7.248  3.376   9.705   1.00 43.32 -1 167 ASP   A OD2 1 
ATOM   1180 N N   . PRO   A 1 168 ? -7.354  6.382   11.263  1.00 45.72 ?  168 PRO   A N   1 
ATOM   1181 C CA  . PRO   A 1 168 ? -8.546  7.190   10.934  1.00 47.48 ?  168 PRO   A CA  1 
ATOM   1182 C C   . PRO   A 1 168 ? -9.723  6.374   10.403  1.00 47.05 ?  168 PRO   A C   1 
ATOM   1183 O O   . PRO   A 1 168 ? -10.876 6.719   10.690  1.00 51.64 ?  168 PRO   A O   1 
ATOM   1184 C CB  . PRO   A 1 168 ? -8.026  8.176   9.873   1.00 38.06 ?  168 PRO   A CB  1 
ATOM   1185 C CG  . PRO   A 1 168 ? -6.719  7.613   9.407   1.00 45.30 ?  168 PRO   A CG  1 
ATOM   1186 C CD  . PRO   A 1 168 ? -6.160  6.796   10.512  1.00 39.79 ?  168 PRO   A CD  1 
ATOM   1187 N N   . ASP   A 1 169 ? -9.473  5.293   9.665   1.00 42.46 ?  169 ASP   A N   1 
ATOM   1188 C CA  . ASP   A 1 169 ? -10.530 4.462   9.098   1.00 42.30 ?  169 ASP   A CA  1 
ATOM   1189 C C   . ASP   A 1 169 ? -11.020 3.360   10.033  1.00 46.54 ?  169 ASP   A C   1 
ATOM   1190 O O   . ASP   A 1 169 ? -11.812 2.517   9.600   1.00 43.34 ?  169 ASP   A O   1 
ATOM   1191 C CB  . ASP   A 1 169 ? -10.075 3.830   7.782   1.00 46.34 ?  169 ASP   A CB  1 
ATOM   1192 C CG  . ASP   A 1 169 ? -10.027 4.823   6.638   1.00 66.22 ?  169 ASP   A CG  1 
ATOM   1193 O OD1 . ASP   A 1 169 ? -8.920  5.122   6.144   1.00 65.51 ?  169 ASP   A OD1 1 
ATOM   1194 O OD2 . ASP   A 1 169 ? -11.111 5.301   6.232   1.00 73.71 -1 169 ASP   A OD2 1 
ATOM   1195 N N   . ALA   A 1 170 ? -10.572 3.335   11.285  1.00 39.37 ?  170 ALA   A N   1 
ATOM   1196 C CA  . ALA   A 1 170 ? -10.972 2.269   12.198  1.00 34.28 ?  170 ALA   A CA  1 
ATOM   1197 C C   . ALA   A 1 170 ? -12.361 2.528   12.778  1.00 40.47 ?  170 ALA   A C   1 
ATOM   1198 O O   . ALA   A 1 170 ? -12.821 3.673   12.865  1.00 37.28 ?  170 ALA   A O   1 
ATOM   1199 C CB  . ALA   A 1 170 ? -9.960  2.138   13.333  1.00 31.93 ?  170 ALA   A CB  1 
ATOM   1200 N N   . THR   A 1 171 ? -13.035 1.447   13.167  1.00 30.03 ?  171 THR   A N   1 
ATOM   1201 C CA  . THR   A 1 171 ? -14.184 1.534   14.059  1.00 34.73 ?  171 THR   A CA  1 
ATOM   1202 C C   . THR   A 1 171 ? -14.053 0.438   15.112  1.00 39.99 ?  171 THR   A C   1 
ATOM   1203 O O   . THR   A 1 171 ? -13.123 -0.379  15.080  1.00 35.77 ?  171 THR   A O   1 
ATOM   1204 C CB  . THR   A 1 171 ? -15.533 1.427   13.314  1.00 36.09 ?  171 THR   A CB  1 
ATOM   1205 O OG1 . THR   A 1 171 ? -16.611 1.699   14.235  1.00 38.38 ?  171 THR   A OG1 1 
ATOM   1206 C CG2 . THR   A 1 171 ? -15.718 0.034   12.710  1.00 35.27 ?  171 THR   A CG2 1 
ATOM   1207 N N   . SER   A 1 172 ? -14.973 0.448   16.077  1.00 33.74 ?  172 SER   A N   1 
ATOM   1208 C CA  . SER   A 1 172 ? -14.947 -0.524  17.159  1.00 31.99 ?  172 SER   A CA  1 
ATOM   1209 C C   . SER   A 1 172 ? -16.373 -0.770  17.610  1.00 38.64 ?  172 SER   A C   1 
ATOM   1210 O O   . SER   A 1 172 ? -17.309 -0.062  17.215  1.00 28.43 ?  172 SER   A O   1 
ATOM   1211 C CB  . SER   A 1 172 ? -14.089 -0.050  18.347  1.00 40.48 ?  172 SER   A CB  1 
ATOM   1212 O OG  . SER   A 1 172 ? -14.740 0.957   19.129  1.00 33.37 ?  172 SER   A OG  1 
ATOM   1213 N N   . LEU   A 1 173 ? -16.530 -1.784  18.459  1.00 32.52 ?  173 LEU   A N   1 
ATOM   1214 C CA  . LEU   A 1 173 ? -17.859 -2.089  18.963  1.00 33.64 ?  173 LEU   A CA  1 
ATOM   1215 C C   . LEU   A 1 173 ? -18.439 -0.890  19.690  1.00 37.92 ?  173 LEU   A C   1 
ATOM   1216 O O   . LEU   A 1 173 ? -19.623 -0.566  19.525  1.00 35.89 ?  173 LEU   A O   1 
ATOM   1217 C CB  . LEU   A 1 173 ? -17.812 -3.309  19.872  1.00 32.04 ?  173 LEU   A CB  1 
ATOM   1218 C CG  . LEU   A 1 173 ? -17.413 -4.562  19.097  1.00 30.04 ?  173 LEU   A CG  1 
ATOM   1219 C CD1 . LEU   A 1 173 ? -17.308 -5.739  20.042  1.00 32.74 ?  173 LEU   A CD1 1 
ATOM   1220 C CD2 . LEU   A 1 173 ? -18.447 -4.806  17.984  1.00 32.29 ?  173 LEU   A CD2 1 
ATOM   1221 N N   . LEU   A 1 174 ? -17.604 -0.197  20.467  1.00 34.53 ?  174 LEU   A N   1 
ATOM   1222 C CA  . LEU   A 1 174 ? -18.086 0.928   21.257  1.00 39.32 ?  174 LEU   A CA  1 
ATOM   1223 C C   . LEU   A 1 174 ? -18.513 2.086   20.360  1.00 39.44 ?  174 LEU   A C   1 
ATOM   1224 O O   . LEU   A 1 174 ? -19.516 2.752   20.643  1.00 36.15 ?  174 LEU   A O   1 
ATOM   1225 C CB  . LEU   A 1 174 ? -16.999 1.354   22.246  1.00 30.25 ?  174 LEU   A CB  1 
ATOM   1226 C CG  . LEU   A 1 174 ? -17.241 2.481   23.248  1.00 38.03 ?  174 LEU   A CG  1 
ATOM   1227 C CD1 . LEU   A 1 174 ? -18.464 2.204   24.073  1.00 43.96 ?  174 LEU   A CD1 1 
ATOM   1228 C CD2 . LEU   A 1 174 ? -16.028 2.654   24.159  1.00 37.94 ?  174 LEU   A CD2 1 
ATOM   1229 N N   . ASP   A 1 175 ? -17.770 2.331   19.266  1.00 36.66 ?  175 ASP   A N   1 
ATOM   1230 C CA  . ASP   A 1 175 ? -18.107 3.384   18.300  1.00 40.77 ?  175 ASP   A CA  1 
ATOM   1231 C C   . ASP   A 1 175 ? -19.296 3.025   17.411  1.00 44.23 ?  175 ASP   A C   1 
ATOM   1232 O O   . ASP   A 1 175 ? -19.837 3.899   16.717  1.00 36.75 ?  175 ASP   A O   1 
ATOM   1233 C CB  . ASP   A 1 175 ? -16.912 3.689   17.404  1.00 35.03 ?  175 ASP   A CB  1 
ATOM   1234 C CG  . ASP   A 1 175 ? -15.722 4.235   18.184  1.00 54.73 ?  175 ASP   A CG  1 
ATOM   1235 O OD1 . ASP   A 1 175 ? -15.677 5.467   18.392  1.00 44.52 ?  175 ASP   A OD1 1 
ATOM   1236 O OD2 . ASP   A 1 175 ? -14.835 3.430   18.580  1.00 45.99 -1 175 ASP   A OD2 1 
ATOM   1237 N N   . LEU   A 1 176 ? -19.671 1.760   17.366  1.00 35.57 ?  176 LEU   A N   1 
ATOM   1238 C CA  . LEU   A 1 176 ? -20.900 1.333   16.736  1.00 32.92 ?  176 LEU   A CA  1 
ATOM   1239 C C   . LEU   A 1 176 ? -22.040 1.327   17.731  1.00 34.96 ?  176 LEU   A C   1 
ATOM   1240 O O   . LEU   A 1 176 ? -23.125 0.836   17.418  1.00 42.84 ?  176 LEU   A O   1 
ATOM   1241 C CB  . LEU   A 1 176 ? -20.711 -0.059  16.115  1.00 34.01 ?  176 LEU   A CB  1 
ATOM   1242 C CG  . LEU   A 1 176 ? -19.651 -0.138  15.004  1.00 42.41 ?  176 LEU   A CG  1 
ATOM   1243 C CD1 . LEU   A 1 176 ? -19.074 -1.565  14.838  1.00 34.09 ?  176 LEU   A CD1 1 
ATOM   1244 C CD2 . LEU   A 1 176 ? -20.182 0.419   13.664  1.00 38.47 ?  176 LEU   A CD2 1 
ATOM   1245 N N   . GLY   A 1 177 ? -21.800 1.830   18.942  1.00 42.33 ?  177 GLY   A N   1 
ATOM   1246 C CA  . GLY   A 1 177 ? -22.825 1.986   19.947  1.00 43.88 ?  177 GLY   A CA  1 
ATOM   1247 C C   . GLY   A 1 177 ? -22.995 0.827   20.910  1.00 45.18 ?  177 GLY   A C   1 
ATOM   1248 O O   . GLY   A 1 177 ? -23.910 0.873   21.743  1.00 38.97 ?  177 GLY   A O   1 
ATOM   1249 N N   . VAL   A 1 178 ? -22.165 -0.214  20.831  1.00 45.16 ?  178 VAL   A N   1 
ATOM   1250 C CA  . VAL   A 1 178 ? -22.240 -1.274  21.837  1.00 38.60 ?  178 VAL   A CA  1 
ATOM   1251 C C   . VAL   A 1 178 ? -21.814 -0.706  23.182  1.00 43.51 ?  178 VAL   A C   1 
ATOM   1252 O O   . VAL   A 1 178 ? -20.671 -0.259  23.358  1.00 45.27 ?  178 VAL   A O   1 
ATOM   1253 C CB  . VAL   A 1 178 ? -21.395 -2.489  21.435  1.00 43.11 ?  178 VAL   A CB  1 
ATOM   1254 C CG1 . VAL   A 1 178 ? -21.379 -3.531  22.560  1.00 33.38 ?  178 VAL   A CG1 1 
ATOM   1255 C CG2 . VAL   A 1 178 ? -21.968 -3.108  20.158  1.00 36.26 ?  178 VAL   A CG2 1 
ATOM   1256 N N   . ALA   A 1 179 ? -22.739 -0.738  24.141  1.00 53.65 ?  179 ALA   A N   1 
ATOM   1257 C CA  . ALA   A 1 179 ? -22.675 -0.019  25.410  1.00 47.92 ?  179 ALA   A CA  1 
ATOM   1258 C C   . ALA   A 1 179 ? -21.325 -0.113  26.107  1.00 48.34 ?  179 ALA   A C   1 
ATOM   1259 O O   . ALA   A 1 179 ? -20.573 0.864   26.175  1.00 60.39 ?  179 ALA   A O   1 
ATOM   1260 C CB  . ALA   A 1 179 ? -23.774 -0.550  26.334  1.00 45.83 ?  179 ALA   A CB  1 
ATOM   1261 N N   . ALA   A 1 180 ? -21.038 -1.282  26.665  1.00 41.62 ?  180 ALA   A N   1 
ATOM   1262 C CA  . ALA   A 1 180 ? -19.785 -1.550  27.360  1.00 50.49 ?  180 ALA   A CA  1 
ATOM   1263 C C   . ALA   A 1 180 ? -19.429 -2.994  27.027  1.00 43.50 ?  180 ALA   A C   1 
ATOM   1264 O O   . ALA   A 1 180 ? -19.865 -3.932  27.707  1.00 52.67 ?  180 ALA   A O   1 
ATOM   1265 C CB  . ALA   A 1 180 ? -19.926 -1.327  28.866  1.00 46.05 ?  180 ALA   A CB  1 
ATOM   1266 N N   . PRO   A 1 181 ? -18.665 -3.214  25.960  1.00 47.42 ?  181 PRO   A N   1 
ATOM   1267 C CA  . PRO   A 1 181 ? -18.498 -4.580  25.451  1.00 42.45 ?  181 PRO   A CA  1 
ATOM   1268 C C   . PRO   A 1 181 ? -17.643 -5.410  26.387  1.00 44.66 ?  181 PRO   A C   1 
ATOM   1269 O O   . PRO   A 1 181 ? -16.671 -4.920  26.962  1.00 47.80 ?  181 PRO   A O   1 
ATOM   1270 C CB  . PRO   A 1 181 ? -17.817 -4.381  24.092  1.00 42.90 ?  181 PRO   A CB  1 
ATOM   1271 C CG  . PRO   A 1 181 ? -17.753 -2.845  23.872  1.00 49.72 ?  181 PRO   A CG  1 
ATOM   1272 C CD  . PRO   A 1 181 ? -17.829 -2.244  25.235  1.00 48.43 ?  181 PRO   A CD  1 
ATOM   1273 N N   . ASP   A 1 182 ? -18.009 -6.683  26.533  1.00 41.03 ?  182 ASP   A N   1 
ATOM   1274 C CA  . ASP   A 1 182 ? -17.381 -7.577  27.507  1.00 36.78 ?  182 ASP   A CA  1 
ATOM   1275 C C   . ASP   A 1 182 ? -16.432 -8.513  26.763  1.00 38.49 ?  182 ASP   A C   1 
ATOM   1276 O O   . ASP   A 1 182 ? -16.864 -9.486  26.134  1.00 38.11 ?  182 ASP   A O   1 
ATOM   1277 C CB  . ASP   A 1 182 ? -18.455 -8.322  28.295  1.00 43.74 ?  182 ASP   A CB  1 
ATOM   1278 C CG  . ASP   A 1 182 ? -17.886 -9.213  29.406  1.00 50.02 ?  182 ASP   A CG  1 
ATOM   1279 O OD1 . ASP   A 1 182 ? -18.687 -9.651  30.273  1.00 55.92 ?  182 ASP   A OD1 1 
ATOM   1280 O OD2 . ASP   A 1 182 ? -16.665 -9.519  29.391  1.00 51.15 -1 182 ASP   A OD2 1 
ATOM   1281 N N   . ARG   A 1 183 ? -15.125 -8.228  26.879  1.00 36.76 ?  183 ARG   A N   1 
ATOM   1282 C CA  . ARG   A 1 183 ? -14.111 -8.927  26.096  1.00 36.96 ?  183 ARG   A CA  1 
ATOM   1283 C C   . ARG   A 1 183 ? -14.022 -10.409 26.453  1.00 33.63 ?  183 ARG   A C   1 
ATOM   1284 O O   . ARG   A 1 183 ? -13.640 -11.225 25.611  1.00 37.19 ?  183 ARG   A O   1 
ATOM   1285 C CB  . ARG   A 1 183 ? -12.749 -8.246  26.284  1.00 29.27 ?  183 ARG   A CB  1 
ATOM   1286 C CG  . ARG   A 1 183 ? -12.654 -6.860  25.630  1.00 40.20 ?  183 ARG   A CG  1 
ATOM   1287 C CD  . ARG   A 1 183 ? -11.200 -6.383  25.463  1.00 28.89 ?  183 ARG   A CD  1 
ATOM   1288 N NE  . ARG   A 1 183 ? -10.497 -6.427  26.746  1.00 33.48 ?  183 ARG   A NE  1 
ATOM   1289 C CZ  . ARG   A 1 183 ? -9.228  -6.800  26.922  1.00 33.50 ?  183 ARG   A CZ  1 
ATOM   1290 N NH1 . ARG   A 1 183 ? -8.472  -7.167  25.888  1.00 35.78 ?  183 ARG   A NH1 1 
ATOM   1291 N NH2 . ARG   A 1 183 ? -8.715  -6.806  28.147  1.00 42.33 ?  183 ARG   A NH2 1 
ATOM   1292 N N   . ASN   A 1 184 ? -14.350 -10.775 27.687  1.00 34.98 ?  184 ASN   A N   1 
ATOM   1293 C CA  . ASN   A 1 184 ? -14.393 -12.187 28.038  1.00 42.53 ?  184 ASN   A CA  1 
ATOM   1294 C C   . ASN   A 1 184 ? -15.493 -12.899 27.273  1.00 41.31 ?  184 ASN   A C   1 
ATOM   1295 O O   . ASN   A 1 184 ? -15.254 -13.959 26.684  1.00 41.21 ?  184 ASN   A O   1 
ATOM   1296 C CB  . ASN   A 1 184 ? -14.598 -12.360 29.542  1.00 42.06 ?  184 ASN   A CB  1 
ATOM   1297 C CG  . ASN   A 1 184 ? -13.442 -11.815 30.340  1.00 42.81 ?  184 ASN   A CG  1 
ATOM   1298 O OD1 . ASN   A 1 184 ? -12.372 -12.420 30.389  1.00 41.47 ?  184 ASN   A OD1 1 
ATOM   1299 N ND2 . ASN   A 1 184 ? -13.640 -10.657 30.953  1.00 43.62 ?  184 ASN   A ND2 1 
ATOM   1300 N N   . ARG   A 1 185 ? -16.709 -12.334 27.277  1.00 34.62 ?  185 ARG   A N   1 
ATOM   1301 C CA  . ARG   A 1 185 ? -17.799 -12.939 26.519  1.00 37.15 ?  185 ARG   A CA  1 
ATOM   1302 C C   . ARG   A 1 185 ? -17.438 -13.007 25.044  1.00 31.68 ?  185 ARG   A C   1 
ATOM   1303 O O   . ARG   A 1 185 ? -17.555 -14.060 24.409  1.00 35.53 ?  185 ARG   A O   1 
ATOM   1304 C CB  . ARG   A 1 185 ? -19.109 -12.154 26.710  1.00 35.10 ?  185 ARG   A CB  1 
ATOM   1305 C CG  . ARG   A 1 185 ? -19.754 -12.234 28.107  1.00 48.86 ?  185 ARG   A CG  1 
ATOM   1306 C CD  . ARG   A 1 185 ? -21.104 -11.479 28.130  1.00 52.53 ?  185 ARG   A CD  1 
ATOM   1307 N NE  . ARG   A 1 185 ? -21.853 -11.535 29.397  1.00 50.73 ?  185 ARG   A NE  1 
ATOM   1308 C CZ  . ARG   A 1 185 ? -22.507 -12.591 29.888  1.00 45.85 ?  185 ARG   A CZ  1 
ATOM   1309 N NH1 . ARG   A 1 185 ? -22.559 -13.750 29.245  1.00 33.19 ?  185 ARG   A NH1 1 
ATOM   1310 N NH2 . ARG   A 1 185 ? -23.139 -12.474 31.049  1.00 52.88 ?  185 ARG   A NH2 1 
ATOM   1311 N N   . ILE   A 1 186 ? -16.959 -11.891 24.494  1.00 34.41 ?  186 ILE   A N   1 
ATOM   1312 C CA  . ILE   A 1 186 ? -16.652 -11.819 23.073  1.00 27.64 ?  186 ILE   A CA  1 
ATOM   1313 C C   . ILE   A 1 186 ? -15.549 -12.801 22.714  1.00 27.36 ?  186 ILE   A C   1 
ATOM   1314 O O   . ILE   A 1 186 ? -15.624 -13.481 21.690  1.00 30.98 ?  186 ILE   A O   1 
ATOM   1315 C CB  . ILE   A 1 186 ? -16.287 -10.372 22.687  1.00 34.74 ?  186 ILE   A CB  1 
ATOM   1316 C CG1 . ILE   A 1 186 ? -17.483 -9.447  22.964  1.00 31.26 ?  186 ILE   A CG1 1 
ATOM   1317 C CG2 . ILE   A 1 186 ? -15.902 -10.281 21.207  1.00 35.41 ?  186 ILE   A CG2 1 
ATOM   1318 C CD1 . ILE   A 1 186 ? -17.156 -7.970  22.873  1.00 34.62 ?  186 ILE   A CD1 1 
ATOM   1319 N N   . ALA   A 1 187 ? -14.514 -12.910 23.552  1.00 31.59 ?  187 ALA   A N   1 
ATOM   1320 C CA  . ALA   A 1 187 ? -13.398 -13.776 23.189  1.00 29.52 ?  187 ALA   A CA  1 
ATOM   1321 C C   . ALA   A 1 187 ? -13.821 -15.239 23.187  1.00 30.62 ?  187 ALA   A C   1 
ATOM   1322 O O   . ALA   A 1 187 ? -13.354 -16.020 22.351  1.00 32.90 ?  187 ALA   A O   1 
ATOM   1323 C CB  . ALA   A 1 187 ? -12.223 -13.553 24.141  1.00 28.52 ?  187 ALA   A CB  1 
ATOM   1324 N N   . SER   A 1 188 ? -14.733 -15.604 24.083  1.00 28.27 ?  188 SER   A N   1 
ATOM   1325 C CA  . SER   A 1 188 ? -15.268 -16.955 24.123  1.00 36.68 ?  188 SER   A CA  1 
ATOM   1326 C C   . SER   A 1 188 ? -16.138 -17.230 22.903  1.00 33.89 ?  188 SER   A C   1 
ATOM   1327 O O   . SER   A 1 188 ? -15.973 -18.252 22.233  1.00 31.64 ?  188 SER   A O   1 
ATOM   1328 C CB  . SER   A 1 188 ? -16.052 -17.152 25.429  1.00 37.48 ?  188 SER   A CB  1 
ATOM   1329 O OG  . SER   A 1 188 ? -16.803 -18.358 25.421  1.00 46.08 ?  188 SER   A OG  1 
ATOM   1330 N N   . ARG   A 1 189 ? -17.067 -16.318 22.586  1.00 39.21 ?  189 ARG   A N   1 
ATOM   1331 C CA  . ARG   A 1 189 ? -17.828 -16.460 21.345  1.00 38.73 ?  189 ARG   A CA  1 
ATOM   1332 C C   . ARG   A 1 189 ? -16.904 -16.491 20.140  1.00 35.21 ?  189 ARG   A C   1 
ATOM   1333 O O   . ARG   A 1 189 ? -17.084 -17.316 19.231  1.00 28.21 ?  189 ARG   A O   1 
ATOM   1334 C CB  . ARG   A 1 189 ? -18.842 -15.327 21.193  1.00 37.76 ?  189 ARG   A CB  1 
ATOM   1335 C CG  . ARG   A 1 189 ? -19.954 -15.350 22.229  1.00 39.46 ?  189 ARG   A CG  1 
ATOM   1336 C CD  . ARG   A 1 189 ? -21.035 -14.326 21.904  1.00 39.31 ?  189 ARG   A CD  1 
ATOM   1337 N NE  . ARG   A 1 189 ? -22.062 -14.316 22.944  1.00 43.30 ?  189 ARG   A NE  1 
ATOM   1338 C CZ  . ARG   A 1 189 ? -22.971 -13.356 23.086  1.00 46.21 ?  189 ARG   A CZ  1 
ATOM   1339 N NH1 . ARG   A 1 189 ? -23.869 -13.429 24.066  1.00 40.35 ?  189 ARG   A NH1 1 
ATOM   1340 N NH2 . ARG   A 1 189 ? -22.984 -12.324 22.240  1.00 50.60 ?  189 ARG   A NH2 1 
ATOM   1341 N N   . LEU   A 1 190 ? -15.904 -15.608 20.120  1.00 24.90 ?  190 LEU   A N   1 
ATOM   1342 C CA  . LEU   A 1 190 ? -14.954 -15.593 19.010  1.00 28.63 ?  190 LEU   A CA  1 
ATOM   1343 C C   . LEU   A 1 190 ? -14.261 -16.946 18.844  1.00 31.27 ?  190 LEU   A C   1 
ATOM   1344 O O   . LEU   A 1 190 ? -14.225 -17.504 17.742  1.00 26.68 ?  190 LEU   A O   1 
ATOM   1345 C CB  . LEU   A 1 190 ? -13.921 -14.476 19.211  1.00 30.49 ?  190 LEU   A CB  1 
ATOM   1346 C CG  . LEU   A 1 190 ? -12.814 -14.336 18.157  1.00 37.13 ?  190 LEU   A CG  1 
ATOM   1347 C CD1 . LEU   A 1 190 ? -13.390 -14.357 16.754  1.00 33.49 ?  190 LEU   A CD1 1 
ATOM   1348 C CD2 . LEU   A 1 190 ? -12.077 -13.010 18.381  1.00 39.56 ?  190 LEU   A CD2 1 
ATOM   1349 N N   . LEU   A 1 191 ? -13.689 -17.488 19.926  1.00 29.10 ?  191 LEU   A N   1 
ATOM   1350 C CA  . LEU   A 1 191 ? -12.900 -18.708 19.786  1.00 35.44 ?  191 LEU   A CA  1 
ATOM   1351 C C   . LEU   A 1 191 ? -13.782 -19.943 19.562  1.00 32.85 ?  191 LEU   A C   1 
ATOM   1352 O O   . LEU   A 1 191 ? -13.335 -20.912 18.946  1.00 27.14 ?  191 LEU   A O   1 
ATOM   1353 C CB  . LEU   A 1 191 ? -11.993 -18.872 21.013  1.00 37.90 ?  191 LEU   A CB  1 
ATOM   1354 C CG  . LEU   A 1 191 ? -10.812 -17.884 21.083  1.00 33.61 ?  191 LEU   A CG  1 
ATOM   1355 C CD1 . LEU   A 1 191 ? -10.083 -17.945 22.441  1.00 29.52 ?  191 LEU   A CD1 1 
ATOM   1356 C CD2 . LEU   A 1 191 ? -9.846  -18.176 19.936  1.00 31.17 ?  191 LEU   A CD2 1 
ATOM   1357 N N   . ARG   A 1 192 ? -15.031 -19.928 20.038  1.00 23.85 ?  192 ARG   A N   1 
ATOM   1358 C CA  . ARG   A 1 192 ? -15.952 -20.999 19.678  1.00 32.07 ?  192 ARG   A CA  1 
ATOM   1359 C C   . ARG   A 1 192 ? -16.341 -20.928 18.204  1.00 30.07 ?  192 ARG   A C   1 
ATOM   1360 O O   . ARG   A 1 192 ? -16.346 -21.955 17.523  1.00 27.53 ?  192 ARG   A O   1 
ATOM   1361 C CB  . ARG   A 1 192 ? -17.182 -20.955 20.579  1.00 37.93 ?  192 ARG   A CB  1 
ATOM   1362 C CG  . ARG   A 1 192 ? -17.066 -21.898 21.751  1.00 42.33 ?  192 ARG   A CG  1 
ATOM   1363 C CD  . ARG   A 1 192 ? -18.270 -21.776 22.648  1.00 43.33 ?  192 ARG   A CD  1 
ATOM   1364 N NE  . ARG   A 1 192 ? -18.397 -20.426 23.175  1.00 49.09 ?  192 ARG   A NE  1 
ATOM   1365 C CZ  . ARG   A 1 192 ? -19.565 -19.790 23.303  1.00 54.50 ?  192 ARG   A CZ  1 
ATOM   1366 N NH1 . ARG   A 1 192 ? -19.611 -18.552 23.789  1.00 45.50 ?  192 ARG   A NH1 1 
ATOM   1367 N NH2 . ARG   A 1 192 ? -20.693 -20.394 22.937  1.00 43.39 ?  192 ARG   A NH2 1 
ATOM   1368 N N   . GLU   A 1 193 ? -16.585 -19.746 17.655  1.00 31.46 ?  193 GLU   A N   1 
ATOM   1369 C CA  . GLU   A 1 193 ? -16.883 -19.587 16.211  1.00 28.32 ?  193 GLU   A CA  1 
ATOM   1370 C C   . GLU   A 1 193 ? -15.685 -20.029 15.354  1.00 27.24 ?  193 GLU   A C   1 
ATOM   1371 O O   . GLU   A 1 193 ? -15.913 -20.708 14.374  1.00 25.82 ?  193 GLU   A O   1 
ATOM   1372 C CB  . GLU   A 1 193 ? -17.331 -18.159 15.889  1.00 24.83 ?  193 GLU   A CB  1 
ATOM   1373 C CG  . GLU   A 1 193 ? -18.664 -17.770 16.489  1.00 38.50 ?  193 GLU   A CG  1 
ATOM   1374 C CD  . GLU   A 1 193 ? -19.893 -18.114 15.667  1.00 42.26 ?  193 GLU   A CD  1 
ATOM   1375 O OE1 . GLU   A 1 193 ? -21.003 -17.847 16.142  1.00 33.68 ?  193 GLU   A OE1 1 
ATOM   1376 O OE2 . GLU   A 1 193 ? -19.734 -18.643 14.559  1.00 46.43 -1 193 GLU   A OE2 1 
ATOM   1377 N N   . LEU   A 1 194 ? -14.468 -19.674 15.741  1.00 25.44 ?  194 LEU   A N   1 
ATOM   1378 C CA  . LEU   A 1 194 ? -13.262 -20.015 14.950  1.00 28.22 ?  194 LEU   A CA  1 
ATOM   1379 C C   . LEU   A 1 194 ? -13.076 -21.528 14.908  1.00 29.60 ?  194 LEU   A C   1 
ATOM   1380 O O   . LEU   A 1 194 ? -12.723 -22.046 13.869  1.00 30.98 ?  194 LEU   A O   1 
ATOM   1381 C CB  . LEU   A 1 194 ? -12.047 -19.350 15.582  1.00 28.75 ?  194 LEU   A CB  1 
ATOM   1382 C CG  . LEU   A 1 194 ? -10.832 -19.161 14.684  1.00 39.61 ?  194 LEU   A CG  1 
ATOM   1383 C CD1 . LEU   A 1 194 ? -11.239 -18.587 13.339  1.00 41.23 ?  194 LEU   A CD1 1 
ATOM   1384 C CD2 . LEU   A 1 194 ? -9.816  -18.263 15.365  1.00 37.25 ?  194 LEU   A CD2 1 
ATOM   1385 N N   . GLU   A 1 195 ? -13.372 -22.177 16.016  1.00 30.69 ?  195 GLU   A N   1 
ATOM   1386 C CA  . GLU   A 1 195 ? -13.199 -23.630 16.092  1.00 29.97 ?  195 GLU   A CA  1 
ATOM   1387 C C   . GLU   A 1 195 ? -14.053 -24.363 15.072  1.00 26.85 ?  195 GLU   A C   1 
ATOM   1388 O O   . GLU   A 1 195 ? -13.569 -25.245 14.349  1.00 29.23 ?  195 GLU   A O   1 
ATOM   1389 C CB  . GLU   A 1 195 ? -13.547 -24.105 17.500  1.00 33.48 ?  195 GLU   A CB  1 
ATOM   1390 C CG  . GLU   A 1 195 ? -13.348 -25.572 17.752  1.00 46.50 ?  195 GLU   A CG  1 
ATOM   1391 C CD  . GLU   A 1 195 ? -13.676 -25.940 19.198  1.00 55.08 ?  195 GLU   A CD  1 
ATOM   1392 O OE1 . GLU   A 1 195 ? -14.094 -25.045 19.986  1.00 53.47 ?  195 GLU   A OE1 1 
ATOM   1393 O OE2 . GLU   A 1 195 ? -13.537 -27.136 19.532  1.00 61.74 -1 195 GLU   A OE2 1 
ATOM   1394 N N   . ALA   A 1 196 ? -15.295 -23.969 15.072  1.00 30.91 ?  196 ALA   A N   1 
ATOM   1395 C CA  . ALA   A 1 196 ? -16.172 -24.596 14.087  1.00 32.71 ?  196 ALA   A CA  1 
ATOM   1396 C C   . ALA   A 1 196 ? -15.756 -24.218 12.666  1.00 31.22 ?  196 ALA   A C   1 
ATOM   1397 O O   . ALA   A 1 196 ? -15.815 -25.048 11.753  1.00 31.11 ?  196 ALA   A O   1 
ATOM   1398 C CB  . ALA   A 1 196 ? -17.640 -24.215 14.357  1.00 26.71 ?  196 ALA   A CB  1 
ATOM   1399 N N   . ARG   A 1 197 ? -15.350 -22.967 12.449  1.00 29.56 ?  197 ARG   A N   1 
ATOM   1400 C CA  . ARG   A 1 197 ? -14.964 -22.574 11.096  1.00 28.75 ?  197 ARG   A CA  1 
ATOM   1401 C C   . ARG   A 1 197 ? -13.713 -23.320 10.648  1.00 27.65 ?  197 ARG   A C   1 
ATOM   1402 O O   . ARG   A 1 197 ? -13.620 -23.727 9.488   1.00 29.98 ?  197 ARG   A O   1 
ATOM   1403 C CB  . ARG   A 1 197 ? -14.751 -21.065 11.020  1.00 32.90 ?  197 ARG   A CB  1 
ATOM   1404 C CG  . ARG   A 1 197 ? -16.034 -20.249 11.138  1.00 30.78 ?  197 ARG   A CG  1 
ATOM   1405 C CD  . ARG   A 1 197 ? -17.122 -20.818 10.251  1.00 33.68 ?  197 ARG   A CD  1 
ATOM   1406 N NE  . ARG   A 1 197 ? -18.289 -19.957 10.205  1.00 34.49 ?  197 ARG   A NE  1 
ATOM   1407 C CZ  . ARG   A 1 197 ? -19.366 -20.181 9.459   1.00 34.01 ?  197 ARG   A CZ  1 
ATOM   1408 N NH1 . ARG   A 1 197 ? -19.445 -21.246 8.673   1.00 29.58 ?  197 ARG   A NH1 1 
ATOM   1409 N NH2 . ARG   A 1 197 ? -20.372 -19.326 9.505   1.00 34.61 ?  197 ARG   A NH2 1 
ATOM   1410 N N   . ILE   A 1 198 ? -12.762 -23.542 11.562  1.00 27.02 ?  198 ILE   A N   1 
ATOM   1411 C CA  . ILE   A 1 198 ? -11.546 -24.279 11.217  1.00 28.74 ?  198 ILE   A CA  1 
ATOM   1412 C C   . ILE   A 1 198 ? -11.880 -25.725 10.882  1.00 27.83 ?  198 ILE   A C   1 
ATOM   1413 O O   . ILE   A 1 198 ? -11.374 -26.287 9.903   1.00 29.61 ?  198 ILE   A O   1 
ATOM   1414 C CB  . ILE   A 1 198 ? -10.523 -24.194 12.366  1.00 27.26 ?  198 ILE   A CB  1 
ATOM   1415 C CG1 . ILE   A 1 198 ? -9.913  -22.799 12.466  1.00 28.07 ?  198 ILE   A CG1 1 
ATOM   1416 C CG2 . ILE   A 1 198 ? -9.419  -25.241 12.207  1.00 27.58 ?  198 ILE   A CG2 1 
ATOM   1417 C CD1 . ILE   A 1 198 ? -9.426  -22.466 13.902  1.00 24.02 ?  198 ILE   A CD1 1 
ATOM   1418 N N   . ILE   A 1 199 ? -12.742 -26.348 11.684  1.00 28.90 ?  199 ILE   A N   1 
ATOM   1419 C CA  . ILE   A 1 199 ? -13.168 -27.720 11.401  1.00 31.13 ?  199 ILE   A CA  1 
ATOM   1420 C C   . ILE   A 1 199 ? -13.844 -27.791 10.039  1.00 28.35 ?  199 ILE   A C   1 
ATOM   1421 O O   . ILE   A 1 199 ? -13.576 -28.699 9.243   1.00 29.35 ?  199 ILE   A O   1 
ATOM   1422 C CB  . ILE   A 1 199 ? -14.097 -28.221 12.521  1.00 28.52 ?  199 ILE   A CB  1 
ATOM   1423 C CG1 . ILE   A 1 199 ? -13.308 -28.529 13.780  1.00 29.61 ?  199 ILE   A CG1 1 
ATOM   1424 C CG2 . ILE   A 1 199 ? -14.856 -29.445 12.086  1.00 34.35 ?  199 ILE   A CG2 1 
ATOM   1425 C CD1 . ILE   A 1 199 ? -14.211 -28.624 15.018  1.00 31.11 ?  199 ILE   A CD1 1 
ATOM   1426 N N   . GLN   A 1 200 ? -14.708 -26.807 9.743   1.00 25.36 ?  200 GLN   A N   1 
ATOM   1427 C CA  . GLN   A 1 200 ? -15.350 -26.709 8.435   1.00 32.72 ?  200 GLN   A CA  1 
ATOM   1428 C C   . GLN   A 1 200 ? -14.317 -26.629 7.313   1.00 32.24 ?  200 GLN   A C   1 
ATOM   1429 O O   . GLN   A 1 200 ? -14.416 -27.341 6.307   1.00 32.88 ?  200 GLN   A O   1 
ATOM   1430 C CB  . GLN   A 1 200 ? -16.277 -25.481 8.399   1.00 29.41 ?  200 GLN   A CB  1 
ATOM   1431 C CG  . GLN   A 1 200 ? -17.643 -25.775 8.982   1.00 35.77 ?  200 GLN   A CG  1 
ATOM   1432 C CD  . GLN   A 1 200 ? -18.524 -24.559 9.030   1.00 35.34 ?  200 GLN   A CD  1 
ATOM   1433 O OE1 . GLN   A 1 200 ? -18.492 -23.729 8.129   1.00 38.40 ?  200 GLN   A OE1 1 
ATOM   1434 N NE2 . GLN   A 1 200 ? -19.314 -24.441 10.089  1.00 35.76 ?  200 GLN   A NE2 1 
ATOM   1435 N N   . TRP   A 1 201 ? -13.326 -25.754 7.466   1.00 27.41 ?  201 TRP   A N   1 
ATOM   1436 C CA  . TRP   A 1 201 ? -12.273 -25.637 6.459   1.00 31.34 ?  201 TRP   A CA  1 
ATOM   1437 C C   . TRP   A 1 201 ? -11.547 -26.951 6.275   1.00 32.90 ?  201 TRP   A C   1 
ATOM   1438 O O   . TRP   A 1 201 ? -11.340 -27.403 5.141   1.00 31.78 ?  201 TRP   A O   1 
ATOM   1439 C CB  . TRP   A 1 201 ? -11.268 -24.565 6.855   1.00 26.06 ?  201 TRP   A CB  1 
ATOM   1440 C CG  . TRP   A 1 201 ? -10.008 -24.624 6.035   1.00 35.37 ?  201 TRP   A CG  1 
ATOM   1441 C CD1 . TRP   A 1 201 ? -9.826  -24.117 4.774   1.00 36.49 ?  201 TRP   A CD1 1 
ATOM   1442 C CD2 . TRP   A 1 201 ? -8.757  -25.222 6.408   1.00 32.60 ?  201 TRP   A CD2 1 
ATOM   1443 N NE1 . TRP   A 1 201 ? -8.542  -24.362 4.347   1.00 34.11 ?  201 TRP   A NE1 1 
ATOM   1444 C CE2 . TRP   A 1 201 ? -7.869  -25.048 5.320   1.00 35.02 ?  201 TRP   A CE2 1 
ATOM   1445 C CE3 . TRP   A 1 201 ? -8.309  -25.908 7.538   1.00 35.29 ?  201 TRP   A CE3 1 
ATOM   1446 C CZ2 . TRP   A 1 201 ? -6.555  -25.515 5.342   1.00 34.82 ?  201 TRP   A CZ2 1 
ATOM   1447 C CZ3 . TRP   A 1 201 ? -6.992  -26.367 7.561   1.00 40.33 ?  201 TRP   A CZ3 1 
ATOM   1448 C CH2 . TRP   A 1 201 ? -6.133  -26.161 6.475   1.00 34.94 ?  201 TRP   A CH2 1 
ATOM   1449 N N   . ARG   A 1 202 ? -11.125 -27.571 7.387   1.00 30.53 ?  202 ARG   A N   1 
ATOM   1450 C CA  . ARG   A 1 202 ? -10.380 -28.822 7.281   1.00 34.36 ?  202 ARG   A CA  1 
ATOM   1451 C C   . ARG   A 1 202 ? -11.152 -29.860 6.478   1.00 36.21 ?  202 ARG   A C   1 
ATOM   1452 O O   . ARG   A 1 202 ? -10.550 -30.679 5.774   1.00 37.21 ?  202 ARG   A O   1 
ATOM   1453 C CB  . ARG   A 1 202 ? -10.060 -29.362 8.672   1.00 37.85 ?  202 ARG   A CB  1 
ATOM   1454 C CG  . ARG   A 1 202 ? -8.898  -30.318 8.699   1.00 42.22 ?  202 ARG   A CG  1 
ATOM   1455 C CD  . ARG   A 1 202 ? -8.648  -30.802 10.120  1.00 49.13 ?  202 ARG   A CD  1 
ATOM   1456 N NE  . ARG   A 1 202 ? -7.974  -29.774 10.916  1.00 59.52 ?  202 ARG   A NE  1 
ATOM   1457 C CZ  . ARG   A 1 202 ? -6.691  -29.443 10.783  1.00 49.95 ?  202 ARG   A CZ  1 
ATOM   1458 N NH1 . ARG   A 1 202 ? -5.930  -30.064 9.884   1.00 59.16 ?  202 ARG   A NH1 1 
ATOM   1459 N NH2 . ARG   A 1 202 ? -6.172  -28.493 11.550  1.00 43.42 ?  202 ARG   A NH2 1 
ATOM   1460 N N   . ASN   A 1 203 ? -12.481 -29.812 6.531   1.00 32.82 ?  203 ASN   A N   1 
ATOM   1461 C CA  . ASN   A 1 203 ? -13.318 -30.849 5.943   1.00 37.07 ?  203 ASN   A CA  1 
ATOM   1462 C C   . ASN   A 1 203 ? -13.999 -30.381 4.662   1.00 38.25 ?  203 ASN   A C   1 
ATOM   1463 O O   . ASN   A 1 203 ? -14.942 -31.029 4.197   1.00 36.76 ?  203 ASN   A O   1 
ATOM   1464 C CB  . ASN   A 1 203 ? -14.352 -31.323 6.969   1.00 32.54 ?  203 ASN   A CB  1 
ATOM   1465 C CG  . ASN   A 1 203 ? -13.729 -32.150 8.082   1.00 41.39 ?  203 ASN   A CG  1 
ATOM   1466 O OD1 . ASN   A 1 203 ? -13.593 -33.357 7.934   1.00 43.79 ?  203 ASN   A OD1 1 
ATOM   1467 N ND2 . ASN   A 1 203 ? -13.361 -31.506 9.209   1.00 30.39 ?  203 ASN   A ND2 1 
ATOM   1468 N N   . ALA   A 1 204 ? -13.528 -29.270 4.085   1.00 31.34 ?  204 ALA   A N   1 
ATOM   1469 C CA  . ALA   A 1 204 ? -14.021 -28.743 2.805   1.00 34.03 ?  204 ALA   A CA  1 
ATOM   1470 C C   . ALA   A 1 204 ? -15.537 -28.592 2.802   1.00 34.52 ?  204 ALA   A C   1 
ATOM   1471 O O   . ALA   A 1 204 ? -16.210 -28.924 1.831   1.00 45.90 ?  204 ALA   A O   1 
ATOM   1472 C CB  . ALA   A 1 204 ? -13.561 -29.605 1.623   1.00 33.68 ?  204 ALA   A CB  1 
ATOM   1473 N N   . ASN   A 1 205 ? -16.075 -28.074 3.896   1.00 40.18 ?  205 ASN   A N   1 
ATOM   1474 C CA  . ASN   A 1 205 ? -17.526 -27.990 4.068   1.00 38.16 ?  205 ASN   A CA  1 
ATOM   1475 C C   . ASN   A 1 205 ? -18.091 -26.888 3.184   1.00 39.61 ?  205 ASN   A C   1 
ATOM   1476 O O   . ASN   A 1 205 ? -17.752 -25.715 3.390   1.00 37.89 ?  205 ASN   A O   1 
ATOM   1477 C CB  . ASN   A 1 205 ? -17.883 -27.732 5.542   1.00 35.55 ?  205 ASN   A CB  1 
ATOM   1478 C CG  . ASN   A 1 205 ? -19.332 -28.056 5.858   1.00 42.86 ?  205 ASN   A CG  1 
ATOM   1479 O OD1 . ASN   A 1 205 ? -20.241 -27.600 5.158   1.00 39.32 ?  205 ASN   A OD1 1 
ATOM   1480 N ND2 . ASN   A 1 205 ? -19.559 -28.848 6.906   1.00 41.65 ?  205 ASN   A ND2 1 
ATOM   1481 N N   . PRO   A 1 206 ? -18.957 -27.197 2.206   1.00 41.77 ?  206 PRO   A N   1 
ATOM   1482 C CA  . PRO   A 1 206 ? -19.473 -26.139 1.314   1.00 32.21 ?  206 PRO   A CA  1 
ATOM   1483 C C   . PRO   A 1 206 ? -20.184 -25.008 2.052   1.00 35.26 ?  206 PRO   A C   1 
ATOM   1484 O O   . PRO   A 1 206 ? -20.310 -23.900 1.521   1.00 33.98 ?  206 PRO   A O   1 
ATOM   1485 C CB  . PRO   A 1 206 ? -20.433 -26.893 0.378   1.00 39.81 ?  206 PRO   A CB  1 
ATOM   1486 C CG  . PRO   A 1 206 ? -20.673 -28.228 1.013   1.00 48.88 ?  206 PRO   A CG  1 
ATOM   1487 C CD  . PRO   A 1 206 ? -19.430 -28.538 1.817   1.00 42.69 ?  206 PRO   A CD  1 
ATOM   1488 N N   . GLN   A 1 207 ? -20.659 -25.260 3.260   1.00 38.89 ?  207 GLN   A N   1 
ATOM   1489 C CA  . GLN   A 1 207 ? -21.321 -24.228 4.041   1.00 42.13 ?  207 GLN   A CA  1 
ATOM   1490 C C   . GLN   A 1 207 ? -20.377 -23.054 4.301   1.00 36.82 ?  207 GLN   A C   1 
ATOM   1491 O O   . GLN   A 1 207 ? -20.817 -21.906 4.415   1.00 36.89 ?  207 GLN   A O   1 
ATOM   1492 C CB  . GLN   A 1 207 ? -21.807 -24.895 5.322   1.00 37.48 ?  207 GLN   A CB  1 
ATOM   1493 C CG  . GLN   A 1 207 ? -22.607 -24.139 6.311   1.00 48.00 ?  207 GLN   A CG  1 
ATOM   1494 C CD  . GLN   A 1 207 ? -23.327 -25.126 7.219   1.00 50.03 ?  207 GLN   A CD  1 
ATOM   1495 O OE1 . GLN   A 1 207 ? -23.494 -26.308 6.873   1.00 56.37 ?  207 GLN   A OE1 1 
ATOM   1496 N NE2 . GLN   A 1 207 ? -23.687 -24.676 8.399   1.00 49.08 ?  207 GLN   A NE2 1 
ATOM   1497 N N   . LEU   A 1 208 ? -19.074 -23.318 4.348   1.00 31.79 ?  208 LEU   A N   1 
ATOM   1498 C CA  . LEU   A 1 208 ? -18.105 -22.244 4.535   1.00 40.89 ?  208 LEU   A CA  1 
ATOM   1499 C C   . LEU   A 1 208 ? -18.190 -21.225 3.392   1.00 35.42 ?  208 LEU   A C   1 
ATOM   1500 O O   . LEU   A 1 208 ? -18.320 -20.017 3.623   1.00 36.52 ?  208 LEU   A O   1 
ATOM   1501 C CB  . LEU   A 1 208 ? -16.707 -22.852 4.653   1.00 32.71 ?  208 LEU   A CB  1 
ATOM   1502 C CG  . LEU   A 1 208 ? -15.611 -21.999 5.262   1.00 39.22 ?  208 LEU   A CG  1 
ATOM   1503 C CD1 . LEU   A 1 208 ? -16.028 -21.545 6.669   1.00 37.45 ?  208 LEU   A CD1 1 
ATOM   1504 C CD2 . LEU   A 1 208 ? -14.330 -22.824 5.300   1.00 38.74 ?  208 LEU   A CD2 1 
ATOM   1505 N N   . ALA   A 1 209 ? -18.178 -21.704 2.151   1.00 34.92 ?  209 ALA   A N   1 
ATOM   1506 C CA  . ALA   A 1 209 ? -18.210 -20.795 1.011   1.00 37.55 ?  209 ALA   A CA  1 
ATOM   1507 C C   . ALA   A 1 209 ? -19.554 -20.093 0.906   1.00 39.20 ?  209 ALA   A C   1 
ATOM   1508 O O   . ALA   A 1 209 ? -19.617 -18.912 0.533   1.00 33.46 ?  209 ALA   A O   1 
ATOM   1509 C CB  . ALA   A 1 209 ? -17.912 -21.556 -0.284  1.00 31.30 ?  209 ALA   A CB  1 
ATOM   1510 N N   . ALA   A 1 210 ? -20.645 -20.816 1.201   1.00 32.75 ?  210 ALA   A N   1 
ATOM   1511 C CA  . ALA   A 1 210 ? -21.962 -20.196 1.134   1.00 33.76 ?  210 ALA   A CA  1 
ATOM   1512 C C   . ALA   A 1 210 ? -22.115 -19.138 2.216   1.00 31.32 ?  210 ALA   A C   1 
ATOM   1513 O O   . ALA   A 1 210 ? -22.694 -18.075 1.968   1.00 32.73 ?  210 ALA   A O   1 
ATOM   1514 C CB  . ALA   A 1 210 ? -23.061 -21.260 1.243   1.00 34.50 ?  210 ALA   A CB  1 
ATOM   1515 N N   . ASP   A 1 211 ? -21.597 -19.407 3.422   1.00 30.18 ?  211 ASP   A N   1 
ATOM   1516 C CA  . ASP   A 1 211 ? -21.694 -18.424 4.503   1.00 34.15 ?  211 ASP   A CA  1 
ATOM   1517 C C   . ASP   A 1 211 ? -20.795 -17.222 4.249   1.00 33.91 ?  211 ASP   A C   1 
ATOM   1518 O O   . ASP   A 1 211 ? -21.154 -16.097 4.621   1.00 29.98 ?  211 ASP   A O   1 
ATOM   1519 C CB  . ASP   A 1 211 ? -21.348 -19.057 5.857   1.00 31.42 ?  211 ASP   A CB  1 
ATOM   1520 C CG  . ASP   A 1 211 ? -22.515 -19.876 6.461   1.00 46.85 ?  211 ASP   A CG  1 
ATOM   1521 O OD1 . ASP   A 1 211 ? -23.610 -19.921 5.851   1.00 49.96 ?  211 ASP   A OD1 1 
ATOM   1522 O OD2 . ASP   A 1 211 ? -22.336 -20.471 7.557   1.00 43.61 -1 211 ASP   A OD2 1 
ATOM   1523 N N   . TYR   A 1 212 ? -19.629 -17.434 3.624   1.00 32.93 ?  212 TYR   A N   1 
ATOM   1524 C CA  . TYR   A 1 212 ? -18.771 -16.304 3.264   1.00 27.91 ?  212 TYR   A CA  1 
ATOM   1525 C C   . TYR   A 1 212 ? -19.473 -15.411 2.260   1.00 30.00 ?  212 TYR   A C   1 
ATOM   1526 O O   . TYR   A 1 212 ? -19.535 -14.184 2.432   1.00 27.33 ?  212 TYR   A O   1 
ATOM   1527 C CB  . TYR   A 1 212 ? -17.429 -16.784 2.685   1.00 27.36 ?  212 TYR   A CB  1 
ATOM   1528 C CG  . TYR   A 1 212 ? -16.496 -15.624 2.377   1.00 29.73 ?  212 TYR   A CG  1 
ATOM   1529 C CD1 . TYR   A 1 212 ? -15.544 -15.214 3.302   1.00 30.75 ?  212 TYR   A CD1 1 
ATOM   1530 C CD2 . TYR   A 1 212 ? -16.598 -14.913 1.175   1.00 32.41 ?  212 TYR   A CD2 1 
ATOM   1531 C CE1 . TYR   A 1 212 ? -14.711 -14.130 3.045   1.00 30.11 ?  212 TYR   A CE1 1 
ATOM   1532 C CE2 . TYR   A 1 212 ? -15.780 -13.819 0.909   1.00 32.22 ?  212 TYR   A CE2 1 
ATOM   1533 C CZ  . TYR   A 1 212 ? -14.834 -13.435 1.852   1.00 29.63 ?  212 TYR   A CZ  1 
ATOM   1534 O OH  . TYR   A 1 212 ? -14.006 -12.361 1.618   1.00 37.05 ?  212 TYR   A OH  1 
ATOM   1535 N N   . ARG   A 1 213 ? -19.987 -16.011 1.180   1.00 29.61 ?  213 ARG   A N   1 
ATOM   1536 C CA  . ARG   A 1 213 ? -20.719 -15.239 0.184   1.00 37.96 ?  213 ARG   A CA  1 
ATOM   1537 C C   . ARG   A 1 213 ? -21.895 -14.500 0.804   1.00 35.19 ?  213 ARG   A C   1 
ATOM   1538 O O   . ARG   A 1 213 ? -22.196 -13.364 0.420   1.00 29.68 ?  213 ARG   A O   1 
ATOM   1539 C CB  . ARG   A 1 213 ? -21.200 -16.152 -0.941  1.00 35.28 ?  213 ARG   A CB  1 
ATOM   1540 C CG  . ARG   A 1 213 ? -20.066 -16.751 -1.724  1.00 42.57 ?  213 ARG   A CG  1 
ATOM   1541 C CD  . ARG   A 1 213 ? -20.581 -17.832 -2.637  1.00 44.29 ?  213 ARG   A CD  1 
ATOM   1542 N NE  . ARG   A 1 213 ? -19.598 -18.132 -3.664  1.00 43.05 ?  213 ARG   A NE  1 
ATOM   1543 C CZ  . ARG   A 1 213 ? -19.001 -19.304 -3.802  1.00 49.95 ?  213 ARG   A CZ  1 
ATOM   1544 N NH1 . ARG   A 1 213 ? -19.296 -20.300 -2.977  1.00 47.54 ?  213 ARG   A NH1 1 
ATOM   1545 N NH2 . ARG   A 1 213 ? -18.112 -19.474 -4.770  1.00 48.36 ?  213 ARG   A NH2 1 
ATOM   1546 N N   . ALA   A 1 214 ? -22.581 -15.124 1.761   1.00 30.48 ?  214 ALA   A N   1 
ATOM   1547 C CA  . ALA   A 1 214 ? -23.714 -14.428 2.369   1.00 39.70 ?  214 ALA   A CA  1 
ATOM   1548 C C   . ALA   A 1 214 ? -23.284 -13.241 3.228   1.00 32.61 ?  214 ALA   A C   1 
ATOM   1549 O O   . ALA   A 1 214 ? -24.097 -12.339 3.446   1.00 33.42 ?  214 ALA   A O   1 
ATOM   1550 C CB  . ALA   A 1 214 ? -24.558 -15.398 3.201   1.00 31.07 ?  214 ALA   A CB  1 
ATOM   1551 N N   . ARG   A 1 215 ? -22.039 -13.216 3.724   1.00 32.46 ?  215 ARG   A N   1 
ATOM   1552 C CA  . ARG   A 1 215 ? -21.545 -12.128 4.573   1.00 30.88 ?  215 ARG   A CA  1 
ATOM   1553 C C   . ARG   A 1 215 ? -20.645 -11.123 3.822   1.00 30.53 ?  215 ARG   A C   1 
ATOM   1554 O O   . ARG   A 1 215 ? -20.098 -10.208 4.448   1.00 28.54 ?  215 ARG   A O   1 
ATOM   1555 C CB  . ARG   A 1 215 ? -20.772 -12.696 5.778   1.00 27.51 ?  215 ARG   A CB  1 
ATOM   1556 C CG  . ARG   A 1 215 ? -21.529 -13.564 6.791   1.00 37.40 ?  215 ARG   A CG  1 
ATOM   1557 C CD  . ARG   A 1 215 ? -22.931 -13.076 7.096   1.00 49.20 ?  215 ARG   A CD  1 
ATOM   1558 N NE  . ARG   A 1 215 ? -23.000 -12.075 8.166   1.00 62.69 ?  215 ARG   A NE  1 
ATOM   1559 C CZ  . ARG   A 1 215 ? -23.128 -12.368 9.459   1.00 59.95 ?  215 ARG   A CZ  1 
ATOM   1560 N NH1 . ARG   A 1 215 ? -23.173 -13.634 9.849   1.00 54.83 ?  215 ARG   A NH1 1 
ATOM   1561 N NH2 . ARG   A 1 215 ? -23.204 -11.399 10.358  1.00 60.09 ?  215 ARG   A NH2 1 
ATOM   1562 N N   . SER   A 1 216 ? -20.452 -11.279 2.517   1.00 30.38 ?  216 SER   A N   1 
ATOM   1563 C CA  . SER   A 1 216 ? -19.454 -10.481 1.801   1.00 30.27 ?  216 SER   A CA  1 
ATOM   1564 C C   . SER   A 1 216 ? -19.974 -9.086  1.488   1.00 30.38 ?  216 SER   A C   1 
ATOM   1565 O O   . SER   A 1 216 ? -21.019 -8.939  0.856   1.00 33.18 ?  216 SER   A O   1 
ATOM   1566 C CB  . SER   A 1 216 ? -19.055 -11.167 0.499   1.00 25.40 ?  216 SER   A CB  1 
ATOM   1567 O OG  . SER   A 1 216 ? -18.339 -10.275 -0.334  1.00 34.49 ?  216 SER   A OG  1 
ATOM   1568 N N   . LEU   A 1 217 ? -19.229 -8.055  1.892   1.00 33.75 ?  217 LEU   A N   1 
ATOM   1569 C CA  . LEU   A 1 217 ? -19.544 -6.714  1.397   1.00 33.92 ?  217 LEU   A CA  1 
ATOM   1570 C C   . LEU   A 1 217 ? -18.977 -6.455  0.008   1.00 35.11 ?  217 LEU   A C   1 
ATOM   1571 O O   . LEU   A 1 217 ? -19.383 -5.494  -0.645  1.00 35.03 ?  217 LEU   A O   1 
ATOM   1572 C CB  . LEU   A 1 217 ? -19.008 -5.635  2.338   1.00 38.82 ?  217 LEU   A CB  1 
ATOM   1573 C CG  . LEU   A 1 217 ? -19.629 -5.483  3.717   1.00 45.97 ?  217 LEU   A CG  1 
ATOM   1574 C CD1 . LEU   A 1 217 ? -18.847 -4.442  4.558   1.00 42.37 ?  217 LEU   A CD1 1 
ATOM   1575 C CD2 . LEU   A 1 217 ? -21.097 -5.109  3.573   1.00 45.89 ?  217 LEU   A CD2 1 
ATOM   1576 N N   . THR   A 1 218 ? -18.051 -7.283  -0.454  1.00 36.57 ?  218 THR   A N   1 
ATOM   1577 C CA  . THR   A 1 218 ? -17.305 -6.992  -1.670  1.00 35.07 ?  218 THR   A CA  1 
ATOM   1578 C C   . THR   A 1 218 ? -17.995 -7.532  -2.925  1.00 34.67 ?  218 THR   A C   1 
ATOM   1579 O O   . THR   A 1 218 ? -18.047 -6.837  -3.948  1.00 30.79 ?  218 THR   A O   1 
ATOM   1580 C CB  . THR   A 1 218 ? -15.904 -7.573  -1.517  1.00 27.68 ?  218 THR   A CB  1 
ATOM   1581 O OG1 . THR   A 1 218 ? -15.314 -7.037  -0.328  1.00 31.71 ?  218 THR   A OG1 1 
ATOM   1582 C CG2 . THR   A 1 218 ? -15.032 -7.280  -2.707  1.00 29.80 ?  218 THR   A CG2 1 
ATOM   1583 N N   . ILE   A 1 219 ? -18.538 -8.755  -2.856  1.00 33.90 ?  219 ILE   A N   1 
ATOM   1584 C CA  . ILE   A 1 219 ? -19.238 -9.333  -3.996  1.00 32.20 ?  219 ILE   A CA  1 
ATOM   1585 C C   . ILE   A 1 219 ? -20.413 -8.445  -4.360  1.00 31.38 ?  219 ILE   A C   1 
ATOM   1586 O O   . ILE   A 1 219 ? -21.177 -8.013  -3.490  1.00 36.25 ?  219 ILE   A O   1 
ATOM   1587 C CB  . ILE   A 1 219 ? -19.682 -10.773 -3.684  1.00 25.28 ?  219 ILE   A CB  1 
ATOM   1588 C CG1 . ILE   A 1 219 ? -18.480 -11.710 -3.776  1.00 33.23 ?  219 ILE   A CG1 1 
ATOM   1589 C CG2 . ILE   A 1 219 ? -20.766 -11.228 -4.656  1.00 29.00 ?  219 ILE   A CG2 1 
ATOM   1590 C CD1 . ILE   A 1 219 ? -18.660 -13.012 -3.024  1.00 33.99 ?  219 ILE   A CD1 1 
ATOM   1591 N N   . GLY   A 1 220 ? -20.553 -8.154  -5.654  1.00 31.83 ?  220 GLY   A N   1 
ATOM   1592 C CA  . GLY   A 1 220 ? -21.575 -7.259  -6.135  1.00 34.57 ?  220 GLY   A CA  1 
ATOM   1593 C C   . GLY   A 1 220 ? -21.155 -5.805  -6.244  1.00 41.08 ?  220 GLY   A C   1 
ATOM   1594 O O   . GLY   A 1 220 ? -21.757 -5.057  -7.018  1.00 40.50 ?  220 GLY   A O   1 
ATOM   1595 N N   . SER   A 1 221 ? -20.129 -5.383  -5.527  1.00 41.34 ?  221 SER   A N   1 
ATOM   1596 C CA  . SER   A 1 221 ? -19.774 -3.973  -5.524  1.00 30.59 ?  221 SER   A CA  1 
ATOM   1597 C C   . SER   A 1 221 ? -18.711 -3.666  -6.574  1.00 42.11 ?  221 SER   A C   1 
ATOM   1598 O O   . SER   A 1 221 ? -17.890 -4.516  -6.944  1.00 38.55 ?  221 SER   A O   1 
ATOM   1599 C CB  . SER   A 1 221 ? -19.303 -3.546  -4.128  1.00 36.16 ?  221 SER   A CB  1 
ATOM   1600 O OG  . SER   A 1 221 ? -17.978 -3.955  -3.883  1.00 46.10 ?  221 SER   A OG  1 
ATOM   1601 N N   . ARG   A 1 222 ? -18.779 -2.442  -7.094  1.00 49.54 ?  222 ARG   A N   1 
ATOM   1602 C CA  . ARG   A 1 222 ? -17.663 -1.880  -7.835  1.00 38.23 ?  222 ARG   A CA  1 
ATOM   1603 C C   . ARG   A 1 222 ? -16.501 -1.713  -6.882  1.00 37.95 ?  222 ARG   A C   1 
ATOM   1604 O O   . ARG   A 1 222 ? -16.676 -1.260  -5.749  1.00 38.61 ?  222 ARG   A O   1 
ATOM   1605 C CB  . ARG   A 1 222 ? -18.047 -0.535  -8.458  1.00 42.54 ?  222 ARG   A CB  1 
ATOM   1606 N N   . VAL   A 1 223 ? -15.314 -2.119  -7.320  1.00 33.18 ?  223 VAL   A N   1 
ATOM   1607 C CA  . VAL   A 1 223 ? -14.133 -2.046  -6.474  1.00 41.17 ?  223 VAL   A CA  1 
ATOM   1608 C C   . VAL   A 1 223 ? -12.943 -1.576  -7.299  1.00 36.66 ?  223 VAL   A C   1 
ATOM   1609 O O   . VAL   A 1 223 ? -12.908 -1.702  -8.526  1.00 36.83 ?  223 VAL   A O   1 
ATOM   1610 C CB  . VAL   A 1 223 ? -13.787 -3.400  -5.807  1.00 32.07 ?  223 VAL   A CB  1 
ATOM   1611 C CG1 . VAL   A 1 223 ? -14.949 -3.925  -5.010  1.00 36.49 ?  223 VAL   A CG1 1 
ATOM   1612 C CG2 . VAL   A 1 223 ? -13.383 -4.398  -6.865  1.00 39.16 ?  223 VAL   A CG2 1 
ATOM   1613 N N   . ARG   A 1 224 ? -11.963 -1.034  -6.596  1.00 34.13 ?  224 ARG   A N   1 
ATOM   1614 C CA  . ARG   A 1 224 ? -10.614 -0.870  -7.107  1.00 43.90 ?  224 ARG   A CA  1 
ATOM   1615 C C   . ARG   A 1 224 ? -9.718  -1.780  -6.284  1.00 35.84 ?  224 ARG   A C   1 
ATOM   1616 O O   . ARG   A 1 224 ? -9.750  -1.730  -5.058  1.00 34.53 ?  224 ARG   A O   1 
ATOM   1617 C CB  . ARG   A 1 224 ? -10.150 0.584   -7.013  1.00 41.65 ?  224 ARG   A CB  1 
ATOM   1618 C CG  . ARG   A 1 224 ? -8.687  0.788   -7.433  1.00 44.00 ?  224 ARG   A CG  1 
ATOM   1619 C CD  . ARG   A 1 224 ? -8.327  2.269   -7.524  1.00 46.93 ?  224 ARG   A CD  1 
ATOM   1620 N NE  . ARG   A 1 224 ? -8.262  2.891   -6.206  1.00 53.09 ?  224 ARG   A NE  1 
ATOM   1621 C CZ  . ARG   A 1 224 ? -9.105  3.826   -5.776  1.00 55.49 ?  224 ARG   A CZ  1 
ATOM   1622 N NH1 . ARG   A 1 224 ? -8.963  4.321   -4.555  1.00 52.09 ?  224 ARG   A NH1 1 
ATOM   1623 N NH2 . ARG   A 1 224 ? -10.089 4.263   -6.558  1.00 55.30 ?  224 ARG   A NH2 1 
ATOM   1624 N N   . VAL   A 1 225 ? -8.947  -2.636  -6.945  1.00 43.88 ?  225 VAL   A N   1 
ATOM   1625 C CA  . VAL   A 1 225 ? -8.132  -3.622  -6.243  1.00 41.73 ?  225 VAL   A CA  1 
ATOM   1626 C C   . VAL   A 1 225 ? -6.667  -3.248  -6.416  1.00 41.44 ?  225 VAL   A C   1 
ATOM   1627 O O   . VAL   A 1 225 ? -6.169  -3.150  -7.543  1.00 37.23 ?  225 VAL   A O   1 
ATOM   1628 C CB  . VAL   A 1 225 ? -8.404  -5.047  -6.736  1.00 40.55 ?  225 VAL   A CB  1 
ATOM   1629 C CG1 . VAL   A 1 225 ? -7.566  -6.053  -5.942  1.00 40.68 ?  225 VAL   A CG1 1 
ATOM   1630 C CG2 . VAL   A 1 225 ? -9.880  -5.359  -6.604  1.00 46.29 ?  225 VAL   A CG2 1 
ATOM   1631 N N   . GLU   A 1 226 ? -5.995  -3.042  -5.292  1.00 41.47 ?  226 GLU   A N   1 
ATOM   1632 C CA  . GLU   A 1 226 ? -4.603  -2.616  -5.235  1.00 52.75 ?  226 GLU   A CA  1 
ATOM   1633 C C   . GLU   A 1 226 ? -3.751  -3.880  -5.233  1.00 43.13 ?  226 GLU   A C   1 
ATOM   1634 O O   . GLU   A 1 226 ? -3.641  -4.578  -4.220  1.00 43.38 ?  226 GLU   A O   1 
ATOM   1635 C CB  . GLU   A 1 226 ? -4.385  -1.757  -3.990  1.00 52.93 ?  226 GLU   A CB  1 
ATOM   1636 C CG  . GLU   A 1 226 ? -3.167  -0.854  -3.972  1.00 69.73 ?  226 GLU   A CG  1 
ATOM   1637 C CD  . GLU   A 1 226 ? -2.961  -0.203  -2.592  1.00 78.44 ?  226 GLU   A CD  1 
ATOM   1638 O OE1 . GLU   A 1 226 ? -3.129  -0.897  -1.558  1.00 69.23 ?  226 GLU   A OE1 1 
ATOM   1639 O OE2 . GLU   A 1 226 ? -2.654  1.010   -2.539  1.00 80.39 -1 226 GLU   A OE2 1 
ATOM   1640 N N   . LEU   A 1 227 ? -3.176  -4.177  -6.355  1.00 38.85 ?  227 LEU   A N   1 
ATOM   1641 C CA  . LEU   A 1 227 ? -2.438  -5.412  -6.514  1.00 38.19 ?  227 LEU   A CA  1 
ATOM   1642 C C   . LEU   A 1 227 ? -1.072  -5.324  -5.841  1.00 46.51 ?  227 LEU   A C   1 
ATOM   1643 O O   . LEU   A 1 227 ? -0.478  -4.242  -5.771  1.00 44.88 ?  227 LEU   A O   1 
ATOM   1644 C CB  . LEU   A 1 227 ? -2.257  -5.718  -7.991  1.00 40.17 ?  227 LEU   A CB  1 
ATOM   1645 C CG  . LEU   A 1 227 ? -3.576  -5.959  -8.711  1.00 40.39 ?  227 LEU   A CG  1 
ATOM   1646 C CD1 . LEU   A 1 227 ? -3.328  -6.289  -10.176 1.00 41.23 ?  227 LEU   A CD1 1 
ATOM   1647 C CD2 . LEU   A 1 227 ? -4.297  -7.105  -8.016  1.00 46.04 ?  227 LEU   A CD2 1 
ATOM   1648 N N   . PRO   A 1 228 ? -0.563  -6.462  -5.322  1.00 50.26 ?  228 PRO   A N   1 
ATOM   1649 C CA  . PRO   A 1 228 ? 0.844   -6.525  -4.896  1.00 52.83 ?  228 PRO   A CA  1 
ATOM   1650 C C   . PRO   A 1 228 ? 1.749   -6.023  -5.999  1.00 42.70 ?  228 PRO   A C   1 
ATOM   1651 O O   . PRO   A 1 228 ? 1.753   -6.597  -7.087  1.00 45.84 ?  228 PRO   A O   1 
ATOM   1652 C CB  . PRO   A 1 228 ? 1.079   -8.023  -4.634  1.00 55.20 ?  228 PRO   A CB  1 
ATOM   1653 C CG  . PRO   A 1 228 ? -0.281  -8.629  -4.496  1.00 49.05 ?  228 PRO   A CG  1 
ATOM   1654 C CD  . PRO   A 1 228 ? -1.207  -7.790  -5.329  1.00 49.46 ?  228 PRO   A CD  1 
ATOM   1655 N N   . GLY   A 1 229 ? 2.506   -4.958  -5.747  1.00 50.09 ?  229 GLY   A N   1 
ATOM   1656 C CA  . GLY   A 1 229 ? 3.302   -4.317  -6.775  1.00 39.46 ?  229 GLY   A CA  1 
ATOM   1657 C C   . GLY   A 1 229 ? 2.807   -2.948  -7.184  1.00 54.70 ?  229 GLY   A C   1 
ATOM   1658 O O   . GLY   A 1 229 ? 3.435   -2.311  -8.043  1.00 51.17 ?  229 GLY   A O   1 
ATOM   1659 N N   . GLY   A 1 230 ? 1.691   -2.483  -6.619  1.00 52.51 ?  230 GLY   A N   1 
ATOM   1660 C CA  . GLY   A 1 230 ? 1.226   -1.133  -6.872  1.00 47.59 ?  230 GLY   A CA  1 
ATOM   1661 C C   . GLY   A 1 230 ? 0.540   -0.902  -8.197  1.00 51.64 ?  230 GLY   A C   1 
ATOM   1662 O O   . GLY   A 1 230 ? 0.575   0.218   -8.720  1.00 65.33 ?  230 GLY   A O   1 
ATOM   1663 N N   . GLN   A 1 231 ? -0.061  -1.924  -8.778  1.00 42.26 ?  231 GLN   A N   1 
ATOM   1664 C CA  . GLN   A 1 231 ? -0.978  -1.703  -9.878  1.00 43.29 ?  231 GLN   A CA  1 
ATOM   1665 C C   . GLN   A 1 231 ? -2.396  -1.821  -9.349  1.00 41.80 ?  231 GLN   A C   1 
ATOM   1666 O O   . GLN   A 1 231 ? -2.656  -2.554  -8.393  1.00 48.06 ?  231 GLN   A O   1 
ATOM   1667 C CB  . GLN   A 1 231 ? -0.752  -2.700  -11.003 1.00 40.73 ?  231 GLN   A CB  1 
ATOM   1668 C CG  . GLN   A 1 231 ? 0.653   -2.683  -11.531 1.00 41.24 ?  231 GLN   A CG  1 
ATOM   1669 C CD  . GLN   A 1 231 ? 0.883   -3.827  -12.466 1.00 41.23 ?  231 GLN   A CD  1 
ATOM   1670 O OE1 . GLN   A 1 231 ? 0.291   -3.885  -13.523 1.00 46.68 ?  231 GLN   A OE1 1 
ATOM   1671 N NE2 . GLN   A 1 231 ? 1.737   -4.743  -12.082 1.00 43.04 ?  231 GLN   A NE2 1 
ATOM   1672 N N   . ASP   A 1 232 ? -3.300  -1.080  -9.971  1.00 40.51 ?  232 ASP   A N   1 
ATOM   1673 C CA  . ASP   A 1 232 ? -4.699  -1.022  -9.584  1.00 42.66 ?  232 ASP   A CA  1 
ATOM   1674 C C   . ASP   A 1 232 ? -5.528  -1.533  -10.739 1.00 45.77 ?  232 ASP   A C   1 
ATOM   1675 O O   . ASP   A 1 232 ? -5.197  -1.290  -11.904 1.00 48.62 ?  232 ASP   A O   1 
ATOM   1676 C CB  . ASP   A 1 232 ? -5.176  0.403   -9.252  1.00 44.57 ?  232 ASP   A CB  1 
ATOM   1677 C CG  . ASP   A 1 232 ? -4.374  1.055   -8.154  1.00 60.22 ?  232 ASP   A CG  1 
ATOM   1678 O OD1 . ASP   A 1 232 ? -4.156  2.280   -8.244  1.00 65.66 ?  232 ASP   A OD1 1 
ATOM   1679 O OD2 . ASP   A 1 232 ? -3.957  0.353   -7.206  1.00 67.58 -1 232 ASP   A OD2 1 
ATOM   1680 N N   . VAL   A 1 233 ? -6.605  -2.235  -10.408 1.00 42.70 ?  233 VAL   A N   1 
ATOM   1681 C CA  . VAL   A 1 233 ? -7.595  -2.674  -11.376 1.00 37.01 ?  233 VAL   A CA  1 
ATOM   1682 C C   . VAL   A 1 233 ? -8.956  -2.288  -10.815 1.00 34.73 ?  233 VAL   A C   1 
ATOM   1683 O O   . VAL   A 1 233 ? -9.215  -2.453  -9.619  1.00 41.04 ?  233 VAL   A O   1 
ATOM   1684 C CB  . VAL   A 1 233 ? -7.506  -4.192  -11.649 1.00 37.26 ?  233 VAL   A CB  1 
ATOM   1685 C CG1 . VAL   A 1 233 ? -8.354  -4.595  -12.839 1.00 40.01 ?  233 VAL   A CG1 1 
ATOM   1686 C CG2 . VAL   A 1 233 ? -6.073  -4.592  -11.877 1.00 47.84 ?  233 VAL   A CG2 1 
ATOM   1687 N N   . VAL   A 1 234 ? -9.816  -1.763  -11.675 1.00 36.45 ?  234 VAL   A N   1 
ATOM   1688 C CA  . VAL   A 1 234 ? -11.142 -1.310  -11.296 1.00 40.67 ?  234 VAL   A CA  1 
ATOM   1689 C C   . VAL   A 1 234 ? -12.141 -2.140  -12.085 1.00 37.34 ?  234 VAL   A C   1 
ATOM   1690 O O   . VAL   A 1 234 ? -12.163 -2.088  -13.322 1.00 44.92 ?  234 VAL   A O   1 
ATOM   1691 C CB  . VAL   A 1 234 ? -11.321 0.192   -11.561 1.00 42.80 ?  234 VAL   A CB  1 
ATOM   1692 C CG1 . VAL   A 1 234 ? -12.734 0.638   -11.245 1.00 34.57 ?  234 VAL   A CG1 1 
ATOM   1693 C CG2 . VAL   A 1 234 ? -10.313 0.978   -10.736 1.00 41.50 ?  234 VAL   A CG2 1 
ATOM   1694 N N   . GLY   A 1 235 ? -12.940 -2.927  -11.374 1.00 38.76 ?  235 GLY   A N   1 
ATOM   1695 C CA  . GLY   A 1 235 ? -13.985 -3.725  -11.979 1.00 35.57 ?  235 GLY   A CA  1 
ATOM   1696 C C   . GLY   A 1 235 ? -15.098 -3.981  -10.988 1.00 39.00 ?  235 GLY   A C   1 
ATOM   1697 O O   . GLY   A 1 235 ? -15.183 -3.309  -9.957  1.00 36.95 ?  235 GLY   A O   1 
ATOM   1698 N N   . ILE   A 1 236 ? -15.950 -4.962  -11.254 1.00 36.44 ?  236 ILE   A N   1 
ATOM   1699 C CA  . ILE   A 1 236 ? -17.013 -5.314  -10.322 1.00 38.07 ?  236 ILE   A CA  1 
ATOM   1700 C C   . ILE   A 1 236 ? -16.701 -6.700  -9.768  1.00 34.94 ?  236 ILE   A C   1 
ATOM   1701 O O   . ILE   A 1 236 ? -16.537 -7.655  -10.533 1.00 34.87 ?  236 ILE   A O   1 
ATOM   1702 C CB  . ILE   A 1 236 ? -18.383 -5.288  -11.007 1.00 37.26 ?  236 ILE   A CB  1 
ATOM   1703 C CG1 . ILE   A 1 236 ? -18.774 -3.851  -11.307 1.00 35.94 ?  236 ILE   A CG1 1 
ATOM   1704 C CG2 . ILE   A 1 236 ? -19.429 -5.916  -10.100 1.00 33.59 ?  236 ILE   A CG2 1 
ATOM   1705 C CD1 . ILE   A 1 236 ? -19.810 -3.761  -12.374 1.00 46.64 ?  236 ILE   A CD1 1 
ATOM   1706 N N   . ALA   A 1 237 ? -16.620 -6.814  -8.450  1.00 32.00 ?  237 ALA   A N   1 
ATOM   1707 C CA  . ALA   A 1 237 ? -16.369 -8.112  -7.836  1.00 36.74 ?  237 ALA   A CA  1 
ATOM   1708 C C   . ALA   A 1 237 ? -17.603 -8.995  -8.004  1.00 36.27 ?  237 ALA   A C   1 
ATOM   1709 O O   . ALA   A 1 237 ? -18.705 -8.593  -7.632  1.00 34.10 ?  237 ALA   A O   1 
ATOM   1710 C CB  . ALA   A 1 237 ? -16.016 -7.941  -6.353  1.00 29.24 ?  237 ALA   A CB  1 
ATOM   1711 N N   . ARG   A 1 238 ? -17.434 -10.180 -8.599  1.00 31.11 ?  238 ARG   A N   1 
ATOM   1712 C CA  . ARG   A 1 238 ? -18.570 -11.061 -8.898  1.00 31.53 ?  238 ARG   A CA  1 
ATOM   1713 C C   . ARG   A 1 238 ? -18.693 -12.234 -7.945  1.00 39.44 ?  238 ARG   A C   1 
ATOM   1714 O O   . ARG   A 1 238 ? -19.809 -12.646 -7.626  1.00 36.19 ?  238 ARG   A O   1 
ATOM   1715 C CB  . ARG   A 1 238 ? -18.470 -11.635 -10.324 1.00 27.82 ?  238 ARG   A CB  1 
ATOM   1716 C CG  . ARG   A 1 238 ? -18.665 -10.666 -11.465 1.00 27.21 ?  238 ARG   A CG  1 
ATOM   1717 C CD  . ARG   A 1 238 ? -19.854 -9.739  -11.210 1.00 32.95 ?  238 ARG   A CD  1 
ATOM   1718 N NE  . ARG   A 1 238 ? -20.054 -8.837  -12.350 1.00 37.11 ?  238 ARG   A NE  1 
ATOM   1719 C CZ  . ARG   A 1 238 ? -21.010 -7.913  -12.417 1.00 38.21 ?  238 ARG   A CZ  1 
ATOM   1720 N NH1 . ARG   A 1 238 ? -21.117 -7.151  -13.496 1.00 32.95 ?  238 ARG   A NH1 1 
ATOM   1721 N NH2 . ARG   A 1 238 ? -21.850 -7.744  -11.398 1.00 35.79 ?  238 ARG   A NH2 1 
ATOM   1722 N N   . ASP   A 1 239 ? -17.571 -12.814 -7.517  1.00 28.55 ?  239 ASP   A N   1 
ATOM   1723 C CA  . ASP   A 1 239 ? -17.609 -14.019 -6.707  1.00 31.64 ?  239 ASP   A CA  1 
ATOM   1724 C C   . ASP   A 1 239 ? -16.204 -14.305 -6.204  1.00 32.07 ?  239 ASP   A C   1 
ATOM   1725 O O   . ASP   A 1 239 ? -15.245 -13.594 -6.518  1.00 32.59 ?  239 ASP   A O   1 
ATOM   1726 C CB  . ASP   A 1 239 ? -18.154 -15.204 -7.512  1.00 37.18 ?  239 ASP   A CB  1 
ATOM   1727 C CG  . ASP   A 1 239 ? -18.702 -16.332 -6.619  1.00 44.18 ?  239 ASP   A CG  1 
ATOM   1728 O OD1 . ASP   A 1 239 ? -18.843 -16.156 -5.377  1.00 33.80 ?  239 ASP   A OD1 1 
ATOM   1729 O OD2 . ASP   A 1 239 ? -18.976 -17.413 -7.174  1.00 54.05 -1 239 ASP   A OD2 1 
ATOM   1730 N N   . ILE   A 1 240 ? -16.098 -15.355 -5.411  1.00 34.65 ?  240 ILE   A N   1 
ATOM   1731 C CA  . ILE   A 1 240 ? -14.826 -15.975 -5.086  1.00 33.54 ?  240 ILE   A CA  1 
ATOM   1732 C C   . ILE   A 1 240 ? -14.819 -17.348 -5.749  1.00 40.17 ?  240 ILE   A C   1 
ATOM   1733 O O   . ILE   A 1 240 ? -15.876 -17.948 -5.983  1.00 39.29 ?  240 ILE   A O   1 
ATOM   1734 C CB  . ILE   A 1 240 ? -14.623 -16.096 -3.565  1.00 41.13 ?  240 ILE   A CB  1 
ATOM   1735 C CG1 . ILE   A 1 240 ? -15.801 -16.849 -2.957  1.00 42.06 ?  240 ILE   A CG1 1 
ATOM   1736 C CG2 . ILE   A 1 240 ? -14.491 -14.713 -2.907  1.00 30.32 ?  240 ILE   A CG2 1 
ATOM   1737 C CD1 . ILE   A 1 240 ? -15.753 -16.860 -1.479  1.00 47.06 ?  240 ILE   A CD1 1 
ATOM   1738 N N   . ASP   A 1 241 ? -13.632 -17.854 -6.062  1.00 32.58 ?  241 ASP   A N   1 
ATOM   1739 C CA  . ASP   A 1 241 ? -13.562 -19.158 -6.691  1.00 31.16 ?  241 ASP   A CA  1 
ATOM   1740 C C   . ASP   A 1 241 ? -13.286 -20.227 -5.622  1.00 36.28 ?  241 ASP   A C   1 
ATOM   1741 O O   . ASP   A 1 241 ? -13.334 -19.966 -4.413  1.00 31.89 ?  241 ASP   A O   1 
ATOM   1742 C CB  . ASP   A 1 241 ? -12.525 -19.130 -7.820  1.00 31.30 ?  241 ASP   A CB  1 
ATOM   1743 C CG  . ASP   A 1 241 ? -11.093 -18.990 -7.308  1.00 31.53 ?  241 ASP   A CG  1 
ATOM   1744 O OD1 . ASP   A 1 241 ? -10.884 -18.874 -6.080  1.00 31.33 ?  241 ASP   A OD1 1 
ATOM   1745 O OD2 . ASP   A 1 241 ? -10.162 -18.983 -8.145  1.00 37.98 -1 241 ASP   A OD2 1 
ATOM   1746 N N   . ASP   A 1 242 ? -12.996 -21.451 -6.065  1.00 36.41 ?  242 ASP   A N   1 
ATOM   1747 C CA  . ASP   A 1 242 ? -12.761 -22.556 -5.133  1.00 37.37 ?  242 ASP   A CA  1 
ATOM   1748 C C   . ASP   A 1 242 ? -11.504 -22.376 -4.290  1.00 38.55 ?  242 ASP   A C   1 
ATOM   1749 O O   . ASP   A 1 242 ? -11.316 -23.130 -3.334  1.00 40.50 ?  242 ASP   A O   1 
ATOM   1750 C CB  . ASP   A 1 242 ? -12.667 -23.885 -5.895  1.00 41.01 ?  242 ASP   A CB  1 
ATOM   1751 N N   . GLN   A 1 243 ? -10.623 -21.433 -4.621  1.00 35.59 ?  243 GLN   A N   1 
ATOM   1752 C CA  . GLN   A 1 243 ? -9.492  -21.127 -3.755  1.00 34.54 ?  243 GLN   A CA  1 
ATOM   1753 C C   . GLN   A 1 243 ? -9.705  -19.851 -2.952  1.00 35.99 ?  243 GLN   A C   1 
ATOM   1754 O O   . GLN   A 1 243 ? -8.750  -19.342 -2.355  1.00 34.07 ?  243 GLN   A O   1 
ATOM   1755 C CB  . GLN   A 1 243 ? -8.200  -21.014 -4.569  1.00 34.52 ?  243 GLN   A CB  1 
ATOM   1756 C CG  . GLN   A 1 243 ? -7.925  -22.180 -5.476  1.00 40.89 ?  243 GLN   A CG  1 
ATOM   1757 C CD  . GLN   A 1 243 ? -6.674  -21.968 -6.329  1.00 48.72 ?  243 GLN   A CD  1 
ATOM   1758 O OE1 . GLN   A 1 243 ? -5.741  -21.268 -5.931  1.00 42.49 ?  243 GLN   A OE1 1 
ATOM   1759 N NE2 . GLN   A 1 243 ? -6.657  -22.571 -7.509  1.00 50.21 ?  243 GLN   A NE2 1 
ATOM   1760 N N   . GLY   A 1 244 ? -10.931 -19.328 -2.912  1.00 30.45 ?  244 GLY   A N   1 
ATOM   1761 C CA  . GLY   A 1 244 ? -11.160 -18.062 -2.245  1.00 34.27 ?  244 GLY   A CA  1 
ATOM   1762 C C   . GLY   A 1 244 ? -10.550 -16.849 -2.930  1.00 37.68 ?  244 GLY   A C   1 
ATOM   1763 O O   . GLY   A 1 244 ? -10.381 -15.800 -2.293  1.00 32.00 ?  244 GLY   A O   1 
ATOM   1764 N N   . ARG   A 1 245 ? -10.200 -16.968 -4.203  1.00 29.85 ?  245 ARG   A N   1 
ATOM   1765 C CA  . ARG   A 1 245 ? -9.687  -15.843 -4.959  1.00 29.21 ?  245 ARG   A CA  1 
ATOM   1766 C C   . ARG   A 1 245 ? -10.838 -14.981 -5.457  1.00 32.75 ?  245 ARG   A C   1 
ATOM   1767 O O   . ARG   A 1 245 ? -11.922 -15.476 -5.775  1.00 27.35 ?  245 ARG   A O   1 
ATOM   1768 C CB  . ARG   A 1 245 ? -8.822  -16.331 -6.124  1.00 28.53 ?  245 ARG   A CB  1 
ATOM   1769 C CG  . ARG   A 1 245 ? -7.718  -17.294 -5.659  1.00 33.31 ?  245 ARG   A CG  1 
ATOM   1770 C CD  . ARG   A 1 245 ? -6.779  -17.746 -6.771  1.00 32.71 ?  245 ARG   A CD  1 
ATOM   1771 N NE  . ARG   A 1 245 ? -7.496  -18.496 -7.775  1.00 30.90 ?  245 ARG   A NE  1 
ATOM   1772 C CZ  . ARG   A 1 245 ? -6.926  -19.041 -8.841  1.00 35.33 ?  245 ARG   A CZ  1 
ATOM   1773 N NH1 . ARG   A 1 245 ? -7.675  -19.716 -9.704  1.00 34.21 ?  245 ARG   A NH1 1 
ATOM   1774 N NH2 . ARG   A 1 245 ? -5.616  -18.935 -9.026  1.00 32.99 ?  245 ARG   A NH2 1 
ATOM   1775 N N   . LEU   A 1 246 ? -10.598 -13.670 -5.498  1.00 24.28 ?  246 LEU   A N   1 
ATOM   1776 C CA  . LEU   A 1 246 ? -11.636 -12.724 -5.876  1.00 29.06 ?  246 LEU   A CA  1 
ATOM   1777 C C   . LEU   A 1 246 ? -11.769 -12.669 -7.398  1.00 33.70 ?  246 LEU   A C   1 
ATOM   1778 O O   . LEU   A 1 246 ? -10.780 -12.424 -8.113  1.00 31.60 ?  246 LEU   A O   1 
ATOM   1779 C CB  . LEU   A 1 246 ? -11.303 -11.352 -5.294  1.00 29.58 ?  246 LEU   A CB  1 
ATOM   1780 C CG  . LEU   A 1 246 ? -12.317 -10.227 -5.490  1.00 32.02 ?  246 LEU   A CG  1 
ATOM   1781 C CD1 . LEU   A 1 246 ? -13.577 -10.445 -4.658  1.00 29.82 ?  246 LEU   A CD1 1 
ATOM   1782 C CD2 . LEU   A 1 246 ? -11.658 -8.911  -5.107  1.00 39.11 ?  246 LEU   A CD2 1 
ATOM   1783 N N   . CYS   A 1 247 ? -12.995 -12.911 -7.895  1.00 23.97 ?  247 CYS   A N   1 
ATOM   1784 C CA  . CYS   A 1 247 ? -13.299 -12.880 -9.322  1.00 27.37 ?  247 CYS   A CA  1 
ATOM   1785 C C   . CYS   A 1 247 ? -13.866 -11.512 -9.695  1.00 30.41 ?  247 CYS   A C   1 
ATOM   1786 O O   . CYS   A 1 247 ? -14.978 -11.161 -9.285  1.00 33.46 ?  247 CYS   A O   1 
ATOM   1787 C CB  . CYS   A 1 247 ? -14.270 -14.001 -9.694  1.00 34.79 ?  247 CYS   A CB  1 
ATOM   1788 S SG  . CYS   A 1 247 ? -13.596 -15.645 -9.208  1.00 49.51 ?  247 CYS   A SG  1 
ATOM   1789 N N   . LEU   A 1 248 ? -13.098 -10.757 -10.486 1.00 27.21 ?  248 LEU   A N   1 
ATOM   1790 C CA  . LEU   A 1 248 ? -13.450 -9.421  -10.959 1.00 32.41 ?  248 LEU   A CA  1 
ATOM   1791 C C   . LEU   A 1 248 ? -13.974 -9.459  -12.383 1.00 35.91 ?  248 LEU   A C   1 
ATOM   1792 O O   . LEU   A 1 248 ? -13.403 -10.131 -13.247 1.00 40.49 ?  248 LEU   A O   1 
ATOM   1793 C CB  . LEU   A 1 248 ? -12.234 -8.498  -10.959 1.00 31.63 ?  248 LEU   A CB  1 
ATOM   1794 C CG  . LEU   A 1 248 ? -11.984 -7.556  -9.794  1.00 48.04 ?  248 LEU   A CG  1 
ATOM   1795 C CD1 . LEU   A 1 248 ? -13.080 -6.483  -9.772  1.00 43.62 ?  248 LEU   A CD1 1 
ATOM   1796 C CD2 . LEU   A 1 248 ? -11.977 -8.335  -8.522  1.00 45.46 ?  248 LEU   A CD2 1 
ATOM   1797 N N   . ASP   A 1 249 ? -15.029 -8.704  -12.644 1.00 34.16 ?  249 ASP   A N   1 
ATOM   1798 C CA  . ASP   A 1 249 ? -15.448 -8.410  -14.013 1.00 35.56 ?  249 ASP   A CA  1 
ATOM   1799 C C   . ASP   A 1 249 ? -14.901 -7.032  -14.364 1.00 35.97 ?  249 ASP   A C   1 
ATOM   1800 O O   . ASP   A 1 249 ? -15.304 -6.027  -13.772 1.00 35.58 ?  249 ASP   A O   1 
ATOM   1801 C CB  . ASP   A 1 249 ? -16.968 -8.475  -14.158 1.00 39.90 ?  249 ASP   A CB  1 
ATOM   1802 C CG  . ASP   A 1 249 ? -17.480 -7.817  -15.442 1.00 41.37 ?  249 ASP   A CG  1 
ATOM   1803 O OD1 . ASP   A 1 249 ? -16.958 -8.120  -16.533 1.00 48.90 ?  249 ASP   A OD1 1 
ATOM   1804 O OD2 . ASP   A 1 249 ? -18.468 -7.047  -15.375 1.00 41.81 -1 249 ASP   A OD2 1 
ATOM   1805 N N   . VAL   A 1 250 ? -13.958 -6.994  -15.301 1.00 39.53 ?  250 VAL   A N   1 
ATOM   1806 C CA  . VAL   A 1 250 ? -13.364 -5.753  -15.783 1.00 43.35 ?  250 VAL   A CA  1 
ATOM   1807 C C   . VAL   A 1 250 ? -13.923 -5.525  -17.180 1.00 40.84 ?  250 VAL   A C   1 
ATOM   1808 O O   . VAL   A 1 250 ? -13.433 -6.102  -18.157 1.00 42.55 ?  250 VAL   A O   1 
ATOM   1809 C CB  . VAL   A 1 250 ? -11.832 -5.811  -15.780 1.00 44.67 ?  250 VAL   A CB  1 
ATOM   1810 C CG1 . VAL   A 1 250 ? -11.239 -4.426  -16.033 1.00 45.90 ?  250 VAL   A CG1 1 
ATOM   1811 C CG2 . VAL   A 1 250 ? -11.349 -6.345  -14.445 1.00 37.20 ?  250 VAL   A CG2 1 
ATOM   1812 N N   . GLY   A 1 251 ? -14.979 -4.722  -17.261 1.00 38.79 ?  251 GLY   A N   1 
ATOM   1813 C CA  . GLY   A 1 251 ? -15.616 -4.419  -18.538 1.00 42.81 ?  251 GLY   A CA  1 
ATOM   1814 C C   . GLY   A 1 251 ? -15.841 -5.617  -19.432 1.00 40.35 ?  251 GLY   A C   1 
ATOM   1815 O O   . GLY   A 1 251 ? -15.630 -5.536  -20.648 1.00 50.43 ?  251 GLY   A O   1 
ATOM   1816 N N   . GLY   A 1 252 ? -16.237 -6.750  -18.851 1.00 42.67 ?  252 GLY   A N   1 
ATOM   1817 C CA  . GLY   A 1 252 ? -16.512 -7.956  -19.602 1.00 42.99 ?  252 GLY   A CA  1 
ATOM   1818 C C   . GLY   A 1 252 ? -15.498 -9.060  -19.392 1.00 43.82 ?  252 GLY   A C   1 
ATOM   1819 O O   . GLY   A 1 252 ? -15.843 -10.235 -19.557 1.00 52.54 ?  252 GLY   A O   1 
ATOM   1820 N N   . ARG   A 1 253 ? -14.253 -8.717  -19.058 1.00 37.92 ?  253 ARG   A N   1 
ATOM   1821 C CA  . ARG   A 1 253 ? -13.211 -9.728  -18.879 1.00 46.61 ?  253 ARG   A CA  1 
ATOM   1822 C C   . ARG   A 1 253 ? -13.115 -10.151 -17.422 1.00 46.39 ?  253 ARG   A C   1 
ATOM   1823 O O   . ARG   A 1 253 ? -13.180 -9.313  -16.515 1.00 41.43 ?  253 ARG   A O   1 
ATOM   1824 C CB  . ARG   A 1 253 ? -11.824 -9.189  -19.256 1.00 52.54 ?  253 ARG   A CB  1 
ATOM   1825 C CG  . ARG   A 1 253 ? -11.399 -9.212  -20.686 1.00 53.13 ?  253 ARG   A CG  1 
ATOM   1826 C CD  . ARG   A 1 253 ? -12.154 -8.210  -21.535 1.00 56.79 ?  253 ARG   A CD  1 
ATOM   1827 N NE  . ARG   A 1 253 ? -11.532 -8.117  -22.858 1.00 64.47 ?  253 ARG   A NE  1 
ATOM   1828 C CZ  . ARG   A 1 253 ? -12.038 -7.466  -23.897 1.00 71.34 ?  253 ARG   A CZ  1 
ATOM   1829 N NH1 . ARG   A 1 253 ? -13.251 -6.929  -23.820 1.00 69.87 ?  253 ARG   A NH1 1 
ATOM   1830 N NH2 . ARG   A 1 253 ? -11.368 -7.432  -25.045 1.00 66.46 ?  253 ARG   A NH2 1 
ATOM   1831 N N   . THR   A 1 254 ? -12.906 -11.438 -17.207 1.00 41.68 ?  254 THR   A N   1 
ATOM   1832 C CA  . THR   A 1 254 ? -12.742 -11.993 -15.867 1.00 41.06 ?  254 THR   A CA  1 
ATOM   1833 C C   . THR   A 1 254 ? -11.286 -11.863 -15.436 1.00 36.82 ?  254 THR   A C   1 
ATOM   1834 O O   . THR   A 1 254 ? -10.384 -12.324 -16.139 1.00 29.31 ?  254 THR   A O   1 
ATOM   1835 C CB  . THR   A 1 254 ? -13.189 -13.455 -15.846 1.00 41.51 ?  254 THR   A CB  1 
ATOM   1836 O OG1 . THR   A 1 254 ? -14.565 -13.525 -16.248 1.00 55.33 ?  254 THR   A OG1 1 
ATOM   1837 C CG2 . THR   A 1 254 ? -13.031 -14.069 -14.466 1.00 48.12 ?  254 THR   A CG2 1 
ATOM   1838 N N   . VAL   A 1 255 ? -11.055 -11.217 -14.296 1.00 33.87 ?  255 VAL   A N   1 
ATOM   1839 C CA  . VAL   A 1 255 ? -9.734  -11.147 -13.685 1.00 33.05 ?  255 VAL   A CA  1 
ATOM   1840 C C   . VAL   A 1 255 ? -9.859  -11.762 -12.305 1.00 29.78 ?  255 VAL   A C   1 
ATOM   1841 O O   . VAL   A 1 255 ? -10.656 -11.285 -11.487 1.00 37.29 ?  255 VAL   A O   1 
ATOM   1842 C CB  . VAL   A 1 255 ? -9.214  -9.703  -13.601 1.00 34.36 ?  255 VAL   A CB  1 
ATOM   1843 C CG1 . VAL   A 1 255 ? -7.946  -9.641  -12.781 1.00 33.36 ?  255 VAL   A CG1 1 
ATOM   1844 C CG2 . VAL   A 1 255 ? -8.987  -9.151  -14.990 1.00 36.81 ?  255 VAL   A CG2 1 
ATOM   1845 N N   . VAL   A 1 256 ? -9.082  -12.807 -12.044 1.00 22.98 ?  256 VAL   A N   1 
ATOM   1846 C CA  . VAL   A 1 256 ? -9.120  -13.527 -10.775 1.00 22.80 ?  256 VAL   A CA  1 
ATOM   1847 C C   . VAL   A 1 256 ? -7.907  -13.126 -9.939  1.00 30.16 ?  256 VAL   A C   1 
ATOM   1848 O O   . VAL   A 1 256 ? -6.756  -13.316 -10.348 1.00 32.52 ?  256 VAL   A O   1 
ATOM   1849 C CB  . VAL   A 1 256 ? -9.165  -15.043 -10.999 1.00 28.69 ?  256 VAL   A CB  1 
ATOM   1850 C CG1 . VAL   A 1 256 ? -9.006  -15.769 -9.671  1.00 31.57 ?  256 VAL   A CG1 1 
ATOM   1851 C CG2 . VAL   A 1 256 ? -10.470 -15.433 -11.686 1.00 31.68 ?  256 VAL   A CG2 1 
ATOM   1852 N N   . VAL   A 1 257 ? -8.143  -12.571 -8.764  1.00 30.16 ?  257 VAL   A N   1 
ATOM   1853 C CA  . VAL   A 1 257 ? -7.071  -11.969 -7.982  1.00 32.12 ?  257 VAL   A CA  1 
ATOM   1854 C C   . VAL   A 1 257 ? -6.816  -12.824 -6.741  1.00 32.02 ?  257 VAL   A C   1 
ATOM   1855 O O   . VAL   A 1 257 ? -7.732  -13.070 -5.951  1.00 28.11 ?  257 VAL   A O   1 
ATOM   1856 C CB  . VAL   A 1 257 ? -7.418  -10.522 -7.624  1.00 38.16 ?  257 VAL   A CB  1 
ATOM   1857 C CG1 . VAL   A 1 257 ? -6.592  -10.067 -6.473  1.00 38.18 ?  257 VAL   A CG1 1 
ATOM   1858 C CG2 . VAL   A 1 257 ? -7.196  -9.624  -8.862  1.00 35.54 ?  257 VAL   A CG2 1 
ATOM   1859 N N   . SER   A 1 258 ? -5.566  -13.286 -6.575  1.00 30.60 ?  258 SER   A N   1 
ATOM   1860 C CA  A SER   A 1 258 ? -5.193  -14.085 -5.413  0.90 32.47 ?  258 SER   A CA  1 
ATOM   1861 C CA  B SER   A 1 258 ? -5.174  -14.086 -5.419  0.10 32.79 ?  258 SER   A CA  1 
ATOM   1862 C C   . SER   A 1 258 ? -4.815  -13.251 -4.195  1.00 34.79 ?  258 SER   A C   1 
ATOM   1863 O O   . SER   A 1 258 ? -4.943  -13.742 -3.074  1.00 33.69 ?  258 SER   A O   1 
ATOM   1864 C CB  A SER   A 1 258 ? -4.033  -15.015 -5.752  0.90 33.81 ?  258 SER   A CB  1 
ATOM   1865 C CB  B SER   A 1 258 ? -3.983  -14.982 -5.772  0.10 33.71 ?  258 SER   A CB  1 
ATOM   1866 O OG  A SER   A 1 258 ? -2.817  -14.311 -5.766  0.90 35.92 ?  258 SER   A OG  1 
ATOM   1867 O OG  B SER   A 1 258 ? -4.166  -15.614 -7.027  0.10 34.42 ?  258 SER   A OG  1 
ATOM   1868 N N   . ALA   A 1 259 ? -4.363  -12.008 -4.377  1.00 34.65 ?  259 ALA   A N   1 
ATOM   1869 C CA  . ALA   A 1 259 ? -3.947  -11.165 -3.258  1.00 37.04 ?  259 ALA   A CA  1 
ATOM   1870 C C   . ALA   A 1 259 ? -4.207  -9.715  -3.627  1.00 35.98 ?  259 ALA   A C   1 
ATOM   1871 O O   . ALA   A 1 259 ? -4.066  -9.344  -4.789  1.00 37.27 ?  259 ALA   A O   1 
ATOM   1872 C CB  . ALA   A 1 259 ? -2.458  -11.341 -2.920  1.00 37.82 ?  259 ALA   A CB  1 
ATOM   1873 N N   . GLY   A 1 260 ? -4.578  -8.897  -2.653  1.00 38.36 ?  260 GLY   A N   1 
ATOM   1874 C CA  . GLY   A 1 260 ? -4.753  -7.490  -2.959  1.00 47.09 ?  260 GLY   A CA  1 
ATOM   1875 C C   . GLY   A 1 260 ? -5.465  -6.744  -1.852  1.00 50.05 ?  260 GLY   A C   1 
ATOM   1876 O O   . GLY   A 1 260 ? -5.916  -7.324  -0.856  1.00 48.01 ?  260 GLY   A O   1 
ATOM   1877 N N   . ASP   A 1 261 ? -5.549  -5.431  -2.054  1.00 43.74 ?  261 ASP   A N   1 
ATOM   1878 C CA  . ASP   A 1 261 ? -6.263  -4.518  -1.171  1.00 48.26 ?  261 ASP   A CA  1 
ATOM   1879 C C   . ASP   A 1 261 ? -7.475  -3.963  -1.889  1.00 41.89 ?  261 ASP   A C   1 
ATOM   1880 O O   . ASP   A 1 261 ? -7.347  -3.259  -2.895  1.00 51.86 ?  261 ASP   A O   1 
ATOM   1881 C CB  . ASP   A 1 261 ? -5.369  -3.382  -0.704  1.00 49.72 ?  261 ASP   A CB  1 
ATOM   1882 C CG  . ASP   A 1 261 ? -4.161  -3.885  -0.008  1.00 66.56 ?  261 ASP   A CG  1 
ATOM   1883 O OD1 . ASP   A 1 261 ? -4.358  -4.588  1.007   1.00 74.03 ?  261 ASP   A OD1 1 
ATOM   1884 O OD2 . ASP   A 1 261 ? -3.030  -3.586  -0.455  1.00 77.71 -1 261 ASP   A OD2 1 
ATOM   1885 N N   . VAL   A 1 262 ? -8.630  -4.254  -1.359  1.00 39.84 ?  262 VAL   A N   1 
ATOM   1886 C CA  . VAL   A 1 262 ? -9.871  -3.854  -1.982  1.00 35.78 ?  262 VAL   A CA  1 
ATOM   1887 C C   . VAL   A 1 262 ? -10.301 -2.507  -1.429  1.00 37.19 ?  262 VAL   A C   1 
ATOM   1888 O O   . VAL   A 1 262 ? -10.288 -2.282  -0.221  1.00 38.96 ?  262 VAL   A O   1 
ATOM   1889 C CB  . VAL   A 1 262 ? -10.954 -4.908  -1.757  1.00 30.70 ?  262 VAL   A CB  1 
ATOM   1890 C CG1 . VAL   A 1 262 ? -12.274 -4.382  -2.274  1.00 28.36 ?  262 VAL   A CG1 1 
ATOM   1891 C CG2 . VAL   A 1 262 ? -10.526 -6.201  -2.453  1.00 36.48 ?  262 VAL   A CG2 1 
ATOM   1892 N N   . VAL   A 1 263 ? -10.680 -1.612  -2.322  1.00 38.89 ?  263 VAL   A N   1 
ATOM   1893 C CA  . VAL   A 1 263 ? -11.448 -0.437  -1.970  1.00 46.61 ?  263 VAL   A CA  1 
ATOM   1894 C C   . VAL   A 1 263 ? -12.802 -0.603  -2.628  1.00 35.59 ?  263 VAL   A C   1 
ATOM   1895 O O   . VAL   A 1 263 ? -12.876 -0.926  -3.820  1.00 38.75 ?  263 VAL   A O   1 
ATOM   1896 C CB  . VAL   A 1 263 ? -10.749 0.852   -2.438  1.00 48.06 ?  263 VAL   A CB  1 
ATOM   1897 C CG1 . VAL   A 1 263 ? -11.757 2.001   -2.506  1.00 45.23 ?  263 VAL   A CG1 1 
ATOM   1898 C CG2 . VAL   A 1 263 ? -9.607  1.182   -1.515  1.00 41.45 ?  263 VAL   A CG2 1 
ATOM   1899 N N   . HIS   A 1 264 ? -13.870 -0.408  -1.855  1.00 39.72 ?  264 HIS   A N   1 
ATOM   1900 C CA  . HIS   A 1 264 ? -15.218 -0.402  -2.411  1.00 38.58 ?  264 HIS   A CA  1 
ATOM   1901 C C   . HIS   A 1 264 ? -15.553 0.991   -2.922  1.00 41.48 ?  264 HIS   A C   1 
ATOM   1902 O O   . HIS   A 1 264 ? -15.287 1.987   -2.249  1.00 41.97 ?  264 HIS   A O   1 
ATOM   1903 C CB  . HIS   A 1 264 ? -16.245 -0.840  -1.367  1.00 38.63 ?  264 HIS   A CB  1 
ATOM   1904 C CG  . HIS   A 1 264 ? -16.041 -2.241  -0.879  1.00 42.14 ?  264 HIS   A CG  1 
ATOM   1905 N ND1 . HIS   A 1 264 ? -16.354 -2.642  0.399   1.00 41.25 ?  264 HIS   A ND1 1 
ATOM   1906 C CD2 . HIS   A 1 264 ? -15.546 -3.335  -1.503  1.00 44.14 ?  264 HIS   A CD2 1 
ATOM   1907 C CE1 . HIS   A 1 264 ? -16.073 -3.926  0.540   1.00 47.80 ?  264 HIS   A CE1 1 
ATOM   1908 N NE2 . HIS   A 1 264 ? -15.583 -4.370  -0.602  1.00 34.84 ?  264 HIS   A NE2 1 
ATOM   1909 N N   . LEU   A 1 265 ? -16.134 1.048   -4.113  1.00 39.42 ?  265 LEU   A N   1 
ATOM   1910 C CA  . LEU   A 1 265 ? -16.447 2.310   -4.763  1.00 48.67 ?  265 LEU   A CA  1 
ATOM   1911 C C   . LEU   A 1 265 ? -17.960 2.458   -4.853  1.00 45.06 ?  265 LEU   A C   1 
ATOM   1912 O O   . LEU   A 1 265 ? -18.502 3.522   -4.550  1.00 52.98 ?  265 LEU   A O   1 
ATOM   1913 C CB  . LEU   A 1 265 ? -15.808 2.387   -6.168  1.00 41.41 ?  265 LEU   A CB  1 
ATOM   1914 C CG  . LEU   A 1 265 ? -14.297 2.107   -6.312  1.00 42.44 ?  265 LEU   A CG  1 
ATOM   1915 C CD1 . LEU   A 1 265 ? -13.864 2.166   -7.768  1.00 35.27 ?  265 LEU   A CD1 1 
ATOM   1916 C CD2 . LEU   A 1 265 ? -13.482 3.064   -5.466  1.00 47.82 ?  265 LEU   A CD2 1 
ATOM   1917 N N   . ARG   B 1 4   ? 1.068   -9.567  -57.420 1.00 63.33 ?  4   ARG   B N   1 
ATOM   1918 C CA  . ARG   B 1 4   ? 1.116   -10.671 -56.463 1.00 60.03 ?  4   ARG   B CA  1 
ATOM   1919 C C   . ARG   B 1 4   ? -0.057  -11.642 -56.691 1.00 59.16 ?  4   ARG   B C   1 
ATOM   1920 O O   . ARG   B 1 4   ? -0.036  -12.792 -56.215 1.00 47.43 ?  4   ARG   B O   1 
ATOM   1921 C CB  . ARG   B 1 4   ? 1.113   -10.133 -55.023 1.00 62.36 ?  4   ARG   B CB  1 
ATOM   1922 C CG  . ARG   B 1 4   ? 1.537   -11.145 -53.936 1.00 54.63 ?  4   ARG   B CG  1 
ATOM   1923 C CD  . ARG   B 1 4   ? 1.330   -10.563 -52.522 1.00 52.70 ?  4   ARG   B CD  1 
ATOM   1924 N NE  . ARG   B 1 4   ? 2.459   -9.792  -51.997 1.00 45.66 ?  4   ARG   B NE  1 
ATOM   1925 C CZ  . ARG   B 1 4   ? 3.114   -10.057 -50.866 1.00 50.84 ?  4   ARG   B CZ  1 
ATOM   1926 N NH1 . ARG   B 1 4   ? 2.747   -11.064 -50.083 1.00 53.69 ?  4   ARG   B NH1 1 
ATOM   1927 N NH2 . ARG   B 1 4   ? 4.128   -9.290  -50.491 1.00 47.38 ?  4   ARG   B NH2 1 
ATOM   1928 N N   . ASP   B 1 5   ? -1.067  -11.201 -57.452 1.00 53.28 ?  5   ASP   B N   1 
ATOM   1929 C CA  . ASP   B 1 5   ? -2.161  -12.110 -57.801 1.00 55.35 ?  5   ASP   B CA  1 
ATOM   1930 C C   . ASP   B 1 5   ? -1.675  -13.310 -58.609 1.00 58.26 ?  5   ASP   B C   1 
ATOM   1931 O O   . ASP   B 1 5   ? -2.361  -14.340 -58.651 1.00 57.61 ?  5   ASP   B O   1 
ATOM   1932 C CB  . ASP   B 1 5   ? -3.257  -11.366 -58.573 1.00 54.62 ?  5   ASP   B CB  1 
ATOM   1933 N N   . ARG   B 1 6   ? -0.497  -13.206 -59.230 1.00 62.92 ?  6   ARG   B N   1 
ATOM   1934 C CA  . ARG   B 1 6   ? 0.044   -14.293 -60.036 1.00 52.77 ?  6   ARG   B CA  1 
ATOM   1935 C C   . ARG   B 1 6   ? 0.356   -15.531 -59.217 1.00 54.41 ?  6   ARG   B C   1 
ATOM   1936 O O   . ARG   B 1 6   ? 0.538   -16.601 -59.800 1.00 54.79 ?  6   ARG   B O   1 
ATOM   1937 C CB  . ARG   B 1 6   ? 1.317   -13.845 -60.760 1.00 51.32 ?  6   ARG   B CB  1 
ATOM   1938 N N   . LEU   B 1 7   ? 0.469   -15.417 -57.893 1.00 58.47 ?  7   LEU   B N   1 
ATOM   1939 C CA  . LEU   B 1 7   ? 0.712   -16.592 -57.064 1.00 57.95 ?  7   LEU   B CA  1 
ATOM   1940 C C   . LEU   B 1 7   ? -0.504  -16.998 -56.237 1.00 48.17 ?  7   LEU   B C   1 
ATOM   1941 O O   . LEU   B 1 7   ? -0.359  -17.728 -55.253 1.00 41.04 ?  7   LEU   B O   1 
ATOM   1942 C CB  . LEU   B 1 7   ? 1.932   -16.396 -56.162 1.00 51.75 ?  7   LEU   B CB  1 
ATOM   1943 C CG  . LEU   B 1 7   ? 3.253   -16.367 -56.932 1.00 53.48 ?  7   LEU   B CG  1 
ATOM   1944 C CD1 . LEU   B 1 7   ? 4.423   -16.649 -56.000 1.00 47.02 ?  7   LEU   B CD1 1 
ATOM   1945 C CD2 . LEU   B 1 7   ? 3.227   -17.341 -58.114 1.00 59.18 ?  7   LEU   B CD2 1 
ATOM   1946 N N   . ARG   B 1 8   ? -1.705  -16.605 -56.657 1.00 49.64 ?  8   ARG   B N   1 
ATOM   1947 C CA  . ARG   B 1 8   ? -2.941  -16.965 -55.964 1.00 43.88 ?  8   ARG   B CA  1 
ATOM   1948 C C   . ARG   B 1 8   ? -3.867  -17.830 -56.826 1.00 44.25 ?  8   ARG   B C   1 
ATOM   1949 O O   . ARG   B 1 8   ? -5.006  -17.441 -57.114 1.00 42.97 ?  8   ARG   B O   1 
ATOM   1950 C CB  . ARG   B 1 8   ? -3.630  -15.688 -55.497 1.00 48.11 ?  8   ARG   B CB  1 
ATOM   1951 C CG  . ARG   B 1 8   ? -2.699  -14.835 -54.628 1.00 51.00 ?  8   ARG   B CG  1 
ATOM   1952 C CD  . ARG   B 1 8   ? -3.314  -13.502 -54.184 1.00 42.45 ?  8   ARG   B CD  1 
ATOM   1953 N NE  . ARG   B 1 8   ? -2.469  -12.857 -53.182 1.00 47.31 ?  8   ARG   B NE  1 
ATOM   1954 C CZ  . ARG   B 1 8   ? -2.615  -11.604 -52.758 1.00 40.50 ?  8   ARG   B CZ  1 
ATOM   1955 N NH1 . ARG   B 1 8   ? -1.806  -11.120 -51.825 1.00 46.23 ?  8   ARG   B NH1 1 
ATOM   1956 N NH2 . ARG   B 1 8   ? -3.566  -10.843 -53.252 1.00 35.61 ?  8   ARG   B NH2 1 
ATOM   1957 N N   . PRO   B 1 9   ? -3.425  -19.025 -57.229 1.00 39.26 ?  9   PRO   B N   1 
ATOM   1958 C CA  . PRO   B 1 9   ? -4.331  -19.919 -57.945 1.00 45.66 ?  9   PRO   B CA  1 
ATOM   1959 C C   . PRO   B 1 9   ? -5.465  -20.346 -57.047 1.00 52.25 ?  9   PRO   B C   1 
ATOM   1960 O O   . PRO   B 1 9   ? -5.322  -20.396 -55.808 1.00 50.66 ?  9   PRO   B O   1 
ATOM   1961 C CB  . PRO   B 1 9   ? -3.432  -21.107 -58.322 1.00 33.64 ?  9   PRO   B CB  1 
ATOM   1962 C CG  . PRO   B 1 9   ? -2.336  -21.089 -57.324 1.00 42.53 ?  9   PRO   B CG  1 
ATOM   1963 C CD  . PRO   B 1 9   ? -2.095  -19.633 -57.052 1.00 38.81 ?  9   PRO   B CD  1 
ATOM   1964 N N   . PRO   B 1 10  ? -6.624  -20.665 -57.615 1.00 50.38 ?  10  PRO   B N   1 
ATOM   1965 C CA  . PRO   B 1 10  ? -7.753  -21.098 -56.789 1.00 48.49 ?  10  PRO   B CA  1 
ATOM   1966 C C   . PRO   B 1 10  ? -7.506  -22.474 -56.174 1.00 54.76 ?  10  PRO   B C   1 
ATOM   1967 O O   . PRO   B 1 10  ? -6.629  -23.236 -56.593 1.00 52.10 ?  10  PRO   B O   1 
ATOM   1968 C CB  . PRO   B 1 10  ? -8.926  -21.122 -57.774 1.00 50.55 ?  10  PRO   B CB  1 
ATOM   1969 C CG  . PRO   B 1 10  ? -8.290  -21.326 -59.103 1.00 48.20 ?  10  PRO   B CG  1 
ATOM   1970 C CD  . PRO   B 1 10  ? -6.940  -20.673 -59.055 1.00 49.32 ?  10  PRO   B CD  1 
ATOM   1971 N N   . LEU   B 1 11  ? -8.292  -22.776 -55.144 1.00 50.35 ?  11  LEU   B N   1 
ATOM   1972 C CA  . LEU   B 1 11  ? -8.255  -24.085 -54.508 1.00 51.08 ?  11  LEU   B CA  1 
ATOM   1973 C C   . LEU   B 1 11  ? -9.009  -25.112 -55.338 1.00 52.33 ?  11  LEU   B C   1 
ATOM   1974 O O   . LEU   B 1 11  ? -9.957  -24.785 -56.061 1.00 51.78 ?  11  LEU   B O   1 
ATOM   1975 C CB  . LEU   B 1 11  ? -8.881  -24.037 -53.118 1.00 43.64 ?  11  LEU   B CB  1 
ATOM   1976 C CG  . LEU   B 1 11  ? -8.113  -23.243 -52.078 1.00 52.93 ?  11  LEU   B CG  1 
ATOM   1977 C CD1 . LEU   B 1 11  ? -9.038  -22.953 -50.903 1.00 43.31 ?  11  LEU   B CD1 1 
ATOM   1978 C CD2 . LEU   B 1 11  ? -6.852  -23.992 -51.653 1.00 42.20 ?  11  LEU   B CD2 1 
ATOM   1979 N N   . ASP   B 1 12  ? -8.608  -26.372 -55.179 1.00 50.93 ?  12  ASP   B N   1 
ATOM   1980 C CA  . ASP   B 1 12  ? -9.199  -27.515 -55.876 1.00 46.90 ?  12  ASP   B CA  1 
ATOM   1981 C C   . ASP   B 1 12  ? -10.044 -28.292 -54.873 1.00 43.80 ?  12  ASP   B C   1 
ATOM   1982 O O   . ASP   B 1 12  ? -9.523  -29.131 -54.131 1.00 44.08 ?  12  ASP   B O   1 
ATOM   1983 C CB  . ASP   B 1 12  ? -8.094  -28.376 -56.484 1.00 53.46 ?  12  ASP   B CB  1 
ATOM   1984 C CG  . ASP   B 1 12  ? -8.625  -29.538 -57.306 1.00 47.57 ?  12  ASP   B CG  1 
ATOM   1985 O OD1 . ASP   B 1 12  ? -9.852  -29.751 -57.364 1.00 49.16 ?  12  ASP   B OD1 1 
ATOM   1986 O OD2 . ASP   B 1 12  ? -7.789  -30.240 -57.910 1.00 65.24 -1 12  ASP   B OD2 1 
ATOM   1987 N N   . GLU   B 1 13  ? -11.352 -28.019 -54.875 1.00 36.65 ?  13  GLU   B N   1 
ATOM   1988 C CA  . GLU   B 1 13  ? -12.259 -28.629 -53.908 1.00 41.95 ?  13  GLU   B CA  1 
ATOM   1989 C C   . GLU   B 1 13  ? -12.282 -30.144 -54.034 1.00 44.28 ?  13  GLU   B C   1 
ATOM   1990 O O   . GLU   B 1 13  ? -12.273 -30.853 -53.024 1.00 46.36 ?  13  GLU   B O   1 
ATOM   1991 C CB  . GLU   B 1 13  ? -13.668 -28.082 -54.101 1.00 34.15 ?  13  GLU   B CB  1 
ATOM   1992 C CG  . GLU   B 1 13  ? -14.661 -28.433 -53.018 1.00 45.90 ?  13  GLU   B CG  1 
ATOM   1993 C CD  . GLU   B 1 13  ? -16.005 -27.748 -53.267 1.00 52.12 ?  13  GLU   B CD  1 
ATOM   1994 O OE1 . GLU   B 1 13  ? -16.197 -27.258 -54.397 1.00 57.38 ?  13  GLU   B OE1 1 
ATOM   1995 O OE2 . GLU   B 1 13  ? -16.854 -27.668 -52.350 1.00 45.88 -1 13  GLU   B OE2 1 
ATOM   1996 N N   . ARG   B 1 14  ? -12.361 -30.660 -55.262 1.00 42.38 ?  14  ARG   B N   1 
ATOM   1997 C CA  . ARG   B 1 14  ? -12.418 -32.109 -55.435 1.00 41.85 ?  14  ARG   B CA  1 
ATOM   1998 C C   . ARG   B 1 14  ? -11.155 -32.770 -54.889 1.00 40.77 ?  14  ARG   B C   1 
ATOM   1999 O O   . ARG   B 1 14  ? -11.231 -33.779 -54.188 1.00 38.33 ?  14  ARG   B O   1 
ATOM   2000 C CB  . ARG   B 1 14  ? -12.629 -32.450 -56.912 1.00 46.86 ?  14  ARG   B CB  1 
ATOM   2001 C CG  . ARG   B 1 14  ? -12.553 -33.934 -57.252 1.00 56.42 ?  14  ARG   B CG  1 
ATOM   2002 C CD  . ARG   B 1 14  ? -12.522 -34.137 -58.760 1.00 46.08 ?  14  ARG   B CD  1 
ATOM   2003 N N   . SER   B 1 15  ? -9.988  -32.179 -55.157 1.00 45.64 ?  15  SER   B N   1 
ATOM   2004 C CA  . SER   B 1 15  ? -8.727  -32.753 -54.695 1.00 38.19 ?  15  SER   B CA  1 
ATOM   2005 C C   . SER   B 1 15  ? -8.616  -32.725 -53.170 1.00 39.37 ?  15  SER   B C   1 
ATOM   2006 O O   . SER   B 1 15  ? -8.213  -33.717 -52.553 1.00 37.57 ?  15  SER   B O   1 
ATOM   2007 C CB  . SER   B 1 15  ? -7.559  -32.007 -55.344 1.00 49.98 ?  15  SER   B CB  1 
ATOM   2008 O OG  . SER   B 1 15  ? -6.318  -32.399 -54.798 1.00 53.43 ?  15  SER   B OG  1 
ATOM   2009 N N   . LEU   B 1 16  ? -8.952  -31.594 -52.538 1.00 42.62 ?  16  LEU   B N   1 
ATOM   2010 C CA  . LEU   B 1 16  ? -8.992  -31.558 -51.077 1.00 42.08 ?  16  LEU   B CA  1 
ATOM   2011 C C   . LEU   B 1 16  ? -9.908  -32.642 -50.534 1.00 36.27 ?  16  LEU   B C   1 
ATOM   2012 O O   . LEU   B 1 16  ? -9.548  -33.368 -49.602 1.00 37.05 ?  16  LEU   B O   1 
ATOM   2013 C CB  . LEU   B 1 16  ? -9.454  -30.185 -50.569 1.00 44.15 ?  16  LEU   B CB  1 
ATOM   2014 C CG  . LEU   B 1 16  ? -8.376  -29.104 -50.466 1.00 48.22 ?  16  LEU   B CG  1 
ATOM   2015 C CD1 . LEU   B 1 16  ? -8.951  -27.752 -50.060 1.00 45.23 ?  16  LEU   B CD1 1 
ATOM   2016 C CD2 . LEU   B 1 16  ? -7.313  -29.571 -49.480 1.00 43.29 ?  16  LEU   B CD2 1 
ATOM   2017 N N   . ARG   B 1 17  ? -11.112 -32.748 -51.096 1.00 36.88 ?  17  ARG   B N   1 
ATOM   2018 C CA  . ARG   B 1 17  ? -12.058 -33.753 -50.638 1.00 33.90 ?  17  ARG   B CA  1 
ATOM   2019 C C   . ARG   B 1 17  ? -11.462 -35.147 -50.743 1.00 35.54 ?  17  ARG   B C   1 
ATOM   2020 O O   . ARG   B 1 17  ? -11.571 -35.957 -49.816 1.00 34.77 ?  17  ARG   B O   1 
ATOM   2021 C CB  . ARG   B 1 17  ? -13.323 -33.690 -51.477 1.00 38.80 ?  17  ARG   B CB  1 
ATOM   2022 C CG  . ARG   B 1 17  ? -14.380 -32.859 -50.950 1.00 42.58 ?  17  ARG   B CG  1 
ATOM   2023 C CD  . ARG   B 1 17  ? -15.685 -33.323 -51.518 1.00 42.32 ?  17  ARG   B CD  1 
ATOM   2024 N NE  . ARG   B 1 17  ? -16.645 -32.269 -51.295 1.00 38.87 ?  17  ARG   B NE  1 
ATOM   2025 C CZ  . ARG   B 1 17  ? -16.939 -31.364 -52.207 1.00 46.75 ?  17  ARG   B CZ  1 
ATOM   2026 N NH1 . ARG   B 1 17  ? -16.352 -31.434 -53.390 1.00 55.81 ?  17  ARG   B NH1 1 
ATOM   2027 N NH2 . ARG   B 1 17  ? -17.809 -30.396 -51.929 1.00 49.63 ?  17  ARG   B NH2 1 
ATOM   2028 N N   . ASP   B 1 18  ? -10.856 -35.452 -51.892 1.00 36.17 ?  18  ASP   B N   1 
ATOM   2029 C CA  . ASP   B 1 18  ? -10.320 -36.789 -52.116 1.00 38.81 ?  18  ASP   B CA  1 
ATOM   2030 C C   . ASP   B 1 18  ? -9.257  -37.131 -51.082 1.00 45.09 ?  18  ASP   B C   1 
ATOM   2031 O O   . ASP   B 1 18  ? -9.163  -38.281 -50.630 1.00 47.14 ?  18  ASP   B O   1 
ATOM   2032 C CB  . ASP   B 1 18  ? -9.753  -36.881 -53.534 1.00 45.96 ?  18  ASP   B CB  1 
ATOM   2033 C CG  . ASP   B 1 18  ? -10.848 -36.909 -54.605 1.00 52.35 ?  18  ASP   B CG  1 
ATOM   2034 O OD1 . ASP   B 1 18  ? -12.041 -37.067 -54.239 1.00 54.04 ?  18  ASP   B OD1 1 
ATOM   2035 O OD2 . ASP   B 1 18  ? -10.519 -36.778 -55.814 1.00 58.63 -1 18  ASP   B OD2 1 
ATOM   2036 N N   . GLN   B 1 19  ? -8.467  -36.133 -50.673 1.00 40.00 ?  19  GLN   B N   1 
ATOM   2037 C CA  . GLN   B 1 19  ? -7.355  -36.358 -49.756 1.00 36.83 ?  19  GLN   B CA  1 
ATOM   2038 C C   . GLN   B 1 19  ? -7.827  -36.500 -48.327 1.00 36.25 ?  19  GLN   B C   1 
ATOM   2039 O O   . GLN   B 1 19  ? -7.243  -37.271 -47.556 1.00 38.92 ?  19  GLN   B O   1 
ATOM   2040 C CB  . GLN   B 1 19  ? -6.360  -35.195 -49.826 1.00 37.90 ?  19  GLN   B CB  1 
ATOM   2041 C CG  . GLN   B 1 19  ? -5.767  -34.966 -51.199 1.00 49.11 ?  19  GLN   B CG  1 
ATOM   2042 C CD  . GLN   B 1 19  ? -4.799  -33.798 -51.215 1.00 51.61 ?  19  GLN   B CD  1 
ATOM   2043 O OE1 . GLN   B 1 19  ? -4.638  -33.092 -50.216 1.00 42.60 ?  19  GLN   B OE1 1 
ATOM   2044 N NE2 . GLN   B 1 19  ? -4.142  -33.595 -52.350 1.00 58.36 ?  19  GLN   B NE2 1 
ATOM   2045 N N   . LEU   B 1 20  ? -8.852  -35.733 -47.946 1.00 32.19 ?  20  LEU   B N   1 
ATOM   2046 C CA  . LEU   B 1 20  ? -9.229  -35.555 -46.546 1.00 33.29 ?  20  LEU   B CA  1 
ATOM   2047 C C   . LEU   B 1 20  ? -10.499 -36.276 -46.139 1.00 35.20 ?  20  LEU   B C   1 
ATOM   2048 O O   . LEU   B 1 20  ? -10.542 -36.861 -45.050 1.00 38.07 ?  20  LEU   B O   1 
ATOM   2049 C CB  . LEU   B 1 20  ? -9.405  -34.066 -46.226 1.00 34.23 ?  20  LEU   B CB  1 
ATOM   2050 C CG  . LEU   B 1 20  ? -8.108  -33.275 -46.325 1.00 40.29 ?  20  LEU   B CG  1 
ATOM   2051 C CD1 . LEU   B 1 20  ? -8.417  -31.792 -46.303 1.00 42.08 ?  20  LEU   B CD1 1 
ATOM   2052 C CD2 . LEU   B 1 20  ? -7.178  -33.683 -45.192 1.00 41.20 ?  20  LEU   B CD2 1 
ATOM   2053 N N   . ILE   B 1 21  ? -11.547 -36.227 -46.955 1.00 32.89 ?  21  ILE   B N   1 
ATOM   2054 C CA  . ILE   B 1 21  ? -12.886 -36.574 -46.478 1.00 37.90 ?  21  ILE   B CA  1 
ATOM   2055 C C   . ILE   B 1 21  ? -13.052 -38.093 -46.494 1.00 38.62 ?  21  ILE   B C   1 
ATOM   2056 O O   . ILE   B 1 21  ? -13.161 -38.707 -47.559 1.00 40.70 ?  21  ILE   B O   1 
ATOM   2057 C CB  . ILE   B 1 21  ? -13.972 -35.880 -47.302 1.00 27.86 ?  21  ILE   B CB  1 
ATOM   2058 C CG1 . ILE   B 1 21  ? -13.692 -34.374 -47.321 1.00 38.32 ?  21  ILE   B CG1 1 
ATOM   2059 C CG2 . ILE   B 1 21  ? -15.351 -36.159 -46.689 1.00 26.93 ?  21  ILE   B CG2 1 
ATOM   2060 C CD1 . ILE   B 1 21  ? -13.398 -33.789 -45.901 1.00 35.74 ?  21  ILE   B CD1 1 
ATOM   2061 N N   . GLY   B 1 22  ? -13.076 -38.696 -45.303 1.00 40.02 ?  22  GLY   B N   1 
ATOM   2062 C CA  . GLY   B 1 22  ? -13.124 -40.133 -45.163 1.00 40.77 ?  22  GLY   B CA  1 
ATOM   2063 C C   . GLY   B 1 22  ? -11.850 -40.861 -45.527 1.00 50.94 ?  22  GLY   B C   1 
ATOM   2064 O O   . GLY   B 1 22  ? -11.827 -42.094 -45.442 1.00 46.46 ?  22  GLY   B O   1 
ATOM   2065 N N   . ALA   B 1 23  ? -10.776 -40.145 -45.923 1.00 43.86 ?  23  ALA   B N   1 
ATOM   2066 C CA  . ALA   B 1 23  ? -9.544  -40.790 -46.364 1.00 37.33 ?  23  ALA   B CA  1 
ATOM   2067 C C   . ALA   B 1 23  ? -8.438  -40.433 -45.376 1.00 37.93 ?  23  ALA   B C   1 
ATOM   2068 O O   . ALA   B 1 23  ? -8.315  -41.098 -44.327 1.00 39.45 ?  23  ALA   B O   1 
ATOM   2069 C CB  . ALA   B 1 23  ? -9.229  -40.400 -47.810 1.00 41.86 ?  23  ALA   B CB  1 
ATOM   2070 N N   . GLY   B 1 24  ? -7.623  -39.417 -45.643 1.00 36.26 ?  24  GLY   B N   1 
ATOM   2071 C CA  . GLY   B 1 24  ? -6.550  -39.030 -44.738 1.00 35.42 ?  24  GLY   B CA  1 
ATOM   2072 C C   . GLY   B 1 24  ? -6.954  -38.297 -43.474 1.00 41.11 ?  24  GLY   B C   1 
ATOM   2073 O O   . GLY   B 1 24  ? -6.080  -37.819 -42.739 1.00 38.01 ?  24  GLY   B O   1 
ATOM   2074 N N   . SER   B 1 25  ? -8.251  -38.185 -43.179 1.00 35.02 ?  25  SER   B N   1 
ATOM   2075 C CA  . SER   B 1 25  ? -8.692  -37.516 -41.957 1.00 34.88 ?  25  SER   B CA  1 
ATOM   2076 C C   . SER   B 1 25  ? -10.051 -38.059 -41.543 1.00 31.77 ?  25  SER   B C   1 
ATOM   2077 O O   . SER   B 1 25  ? -10.716 -38.753 -42.309 1.00 36.55 ?  25  SER   B O   1 
ATOM   2078 C CB  . SER   B 1 25  ? -8.809  -35.995 -42.140 1.00 31.90 ?  25  SER   B CB  1 
ATOM   2079 O OG  . SER   B 1 25  ? -10.049 -35.682 -42.769 1.00 25.72 ?  25  SER   B OG  1 
ATOM   2080 N N   . GLY   B 1 26  ? -10.477 -37.691 -40.332 1.00 33.95 ?  26  GLY   B N   1 
ATOM   2081 C CA  . GLY   B 1 26  ? -11.813 -37.932 -39.824 1.00 30.19 ?  26  GLY   B CA  1 
ATOM   2082 C C   . GLY   B 1 26  ? -12.838 -36.878 -40.185 1.00 31.94 ?  26  GLY   B C   1 
ATOM   2083 O O   . GLY   B 1 26  ? -13.994 -36.978 -39.767 1.00 34.45 ?  26  GLY   B O   1 
ATOM   2084 N N   . TRP   B 1 27  ? -12.444 -35.847 -40.933 1.00 30.88 ?  27  TRP   B N   1 
ATOM   2085 C CA  . TRP   B 1 27  ? -13.403 -34.840 -41.362 1.00 32.08 ?  27  TRP   B CA  1 
ATOM   2086 C C   . TRP   B 1 27  ? -14.441 -35.488 -42.269 1.00 37.66 ?  27  TRP   B C   1 
ATOM   2087 O O   . TRP   B 1 27  ? -14.121 -36.369 -43.071 1.00 27.74 ?  27  TRP   B O   1 
ATOM   2088 C CB  . TRP   B 1 27  ? -12.688 -33.699 -42.075 1.00 24.79 ?  27  TRP   B CB  1 
ATOM   2089 C CG  . TRP   B 1 27  ? -11.756 -32.993 -41.154 1.00 27.62 ?  27  TRP   B CG  1 
ATOM   2090 C CD1 . TRP   B 1 27  ? -10.396 -32.961 -41.219 1.00 26.99 ?  27  TRP   B CD1 1 
ATOM   2091 C CD2 . TRP   B 1 27  ? -12.127 -32.206 -40.011 1.00 30.23 ?  27  TRP   B CD2 1 
ATOM   2092 N NE1 . TRP   B 1 27  ? -9.888  -32.198 -40.180 1.00 28.74 ?  27  TRP   B NE1 1 
ATOM   2093 C CE2 . TRP   B 1 27  ? -10.932 -31.731 -39.423 1.00 26.01 ?  27  TRP   B CE2 1 
ATOM   2094 C CE3 . TRP   B 1 27  ? -13.351 -31.874 -39.419 1.00 26.18 ?  27  TRP   B CE3 1 
ATOM   2095 C CZ2 . TRP   B 1 27  ? -10.929 -30.940 -38.276 1.00 24.65 ?  27  TRP   B CZ2 1 
ATOM   2096 C CZ3 . TRP   B 1 27  ? -13.347 -31.075 -38.262 1.00 28.67 ?  27  TRP   B CZ3 1 
ATOM   2097 C CH2 . TRP   B 1 27  ? -12.146 -30.616 -37.714 1.00 26.98 ?  27  TRP   B CH2 1 
ATOM   2098 N N   . ARG   B 1 28  ? -15.686 -35.038 -42.128 1.00 29.09 ?  28  ARG   B N   1 
ATOM   2099 C CA  . ARG   B 1 28  ? -16.843 -35.687 -42.723 1.00 33.76 ?  28  ARG   B CA  1 
ATOM   2100 C C   . ARG   B 1 28  ? -17.395 -34.975 -43.942 1.00 35.74 ?  28  ARG   B C   1 
ATOM   2101 O O   . ARG   B 1 28  ? -18.103 -35.602 -44.738 1.00 34.97 ?  28  ARG   B O   1 
ATOM   2102 C CB  . ARG   B 1 28  ? -17.956 -35.825 -41.679 1.00 34.66 ?  28  ARG   B CB  1 
ATOM   2103 C CG  . ARG   B 1 28  ? -17.551 -36.691 -40.515 1.00 45.29 ?  28  ARG   B CG  1 
ATOM   2104 C CD  . ARG   B 1 28  ? -18.704 -36.997 -39.558 1.00 53.50 ?  28  ARG   B CD  1 
ATOM   2105 N NE  . ARG   B 1 28  ? -19.911 -37.320 -40.317 1.00 66.47 ?  28  ARG   B NE  1 
ATOM   2106 C CZ  . ARG   B 1 28  ? -20.314 -38.557 -40.621 1.00 62.03 ?  28  ARG   B CZ  1 
ATOM   2107 N NH1 . ARG   B 1 28  ? -21.438 -38.743 -41.308 1.00 53.63 ?  28  ARG   B NH1 1 
ATOM   2108 N NH2 . ARG   B 1 28  ? -19.534 -39.585 -40.331 1.00 55.87 ?  28  ARG   B NH2 1 
ATOM   2109 N N   . GLN   B 1 29  ? -17.099 -33.688 -44.109 1.00 34.70 ?  29  GLN   B N   1 
ATOM   2110 C CA  . GLN   B 1 29  ? -17.626 -32.931 -45.233 1.00 32.16 ?  29  GLN   B CA  1 
ATOM   2111 C C   . GLN   B 1 29  ? -16.756 -31.706 -45.420 1.00 32.86 ?  29  GLN   B C   1 
ATOM   2112 O O   . GLN   B 1 29  ? -16.269 -31.127 -44.443 1.00 36.04 ?  29  GLN   B O   1 
ATOM   2113 C CB  . GLN   B 1 29  ? -19.082 -32.517 -45.008 1.00 33.32 ?  29  GLN   B CB  1 
ATOM   2114 C CG  . GLN   B 1 29  ? -19.600 -31.515 -46.019 1.00 30.51 ?  29  GLN   B CG  1 
ATOM   2115 C CD  . GLN   B 1 29  ? -20.935 -30.902 -45.605 1.00 44.27 ?  29  GLN   B CD  1 
ATOM   2116 O OE1 . GLN   B 1 29  ? -21.526 -31.309 -44.600 1.00 40.90 ?  29  GLN   B OE1 1 
ATOM   2117 N NE2 . GLN   B 1 29  ? -21.423 -29.924 -46.388 1.00 33.21 ?  29  GLN   B NE2 1 
ATOM   2118 N N   . LEU   B 1 30  ? -16.573 -31.316 -46.680 1.00 30.11 ?  30  LEU   B N   1 
ATOM   2119 C CA  . LEU   B 1 30  ? -15.728 -30.188 -47.023 1.00 33.38 ?  30  LEU   B CA  1 
ATOM   2120 C C   . LEU   B 1 30  ? -16.348 -29.471 -48.202 1.00 40.68 ?  30  LEU   B C   1 
ATOM   2121 O O   . LEU   B 1 30  ? -16.721 -30.111 -49.190 1.00 35.15 ?  30  LEU   B O   1 
ATOM   2122 C CB  . LEU   B 1 30  ? -14.303 -30.623 -47.373 1.00 30.58 ?  30  LEU   B CB  1 
ATOM   2123 C CG  . LEU   B 1 30  ? -13.271 -29.507 -47.513 1.00 35.58 ?  30  LEU   B CG  1 
ATOM   2124 C CD1 . LEU   B 1 30  ? -11.948 -29.951 -46.895 1.00 35.81 ?  30  LEU   B CD1 1 
ATOM   2125 C CD2 . LEU   B 1 30  ? -13.072 -29.150 -48.972 1.00 36.76 ?  30  LEU   B CD2 1 
ATOM   2126 N N   . ASP   B 1 31  ? -16.479 -28.150 -48.084 1.00 28.80 ?  31  ASP   B N   1 
ATOM   2127 C CA  . ASP   B 1 31  ? -16.947 -27.324 -49.182 1.00 30.15 ?  31  ASP   B CA  1 
ATOM   2128 C C   . ASP   B 1 31  ? -16.033 -26.111 -49.274 1.00 35.91 ?  31  ASP   B C   1 
ATOM   2129 O O   . ASP   B 1 31  ? -15.589 -25.579 -48.252 1.00 33.06 ?  31  ASP   B O   1 
ATOM   2130 C CB  . ASP   B 1 31  ? -18.402 -26.889 -48.981 1.00 36.26 ?  31  ASP   B CB  1 
ATOM   2131 C CG  . ASP   B 1 31  ? -19.371 -28.071 -48.919 1.00 39.80 ?  31  ASP   B CG  1 
ATOM   2132 O OD1 . ASP   B 1 31  ? -19.431 -28.848 -49.909 1.00 39.90 ?  31  ASP   B OD1 1 
ATOM   2133 O OD2 . ASP   B 1 31  ? -20.073 -28.223 -47.878 1.00 41.68 -1 31  ASP   B OD2 1 
ATOM   2134 N N   . VAL   B 1 32  ? -15.713 -25.720 -50.501 1.00 37.30 ?  32  VAL   B N   1 
ATOM   2135 C CA  . VAL   B 1 32  ? -15.046 -24.462 -50.791 1.00 37.17 ?  32  VAL   B CA  1 
ATOM   2136 C C   . VAL   B 1 32  ? -16.089 -23.532 -51.405 1.00 41.47 ?  32  VAL   B C   1 
ATOM   2137 O O   . VAL   B 1 32  ? -16.704 -23.863 -52.426 1.00 40.77 ?  32  VAL   B O   1 
ATOM   2138 C CB  . VAL   B 1 32  ? -13.844 -24.664 -51.723 1.00 32.75 ?  32  VAL   B CB  1 
ATOM   2139 C CG1 . VAL   B 1 32  ? -13.263 -23.341 -52.148 1.00 32.96 ?  32  VAL   B CG1 1 
ATOM   2140 C CG2 . VAL   B 1 32  ? -12.755 -25.526 -51.033 1.00 35.51 ?  32  VAL   B CG2 1 
ATOM   2141 N N   . VAL   B 1 33  ? -16.328 -22.400 -50.762 1.00 36.84 ?  33  VAL   B N   1 
ATOM   2142 C CA  . VAL   B 1 33  ? -17.128 -21.333 -51.350 1.00 35.23 ?  33  VAL   B CA  1 
ATOM   2143 C C   . VAL   B 1 33  ? -16.196 -20.227 -51.829 1.00 38.20 ?  33  VAL   B C   1 
ATOM   2144 O O   . VAL   B 1 33  ? -15.102 -20.015 -51.285 1.00 40.71 ?  33  VAL   B O   1 
ATOM   2145 C CB  . VAL   B 1 33  ? -18.181 -20.802 -50.361 1.00 34.16 ?  33  VAL   B CB  1 
ATOM   2146 C CG1 . VAL   B 1 33  ? -19.029 -21.951 -49.870 1.00 39.07 ?  33  VAL   B CG1 1 
ATOM   2147 C CG2 . VAL   B 1 33  ? -17.514 -20.117 -49.199 1.00 36.84 ?  33  VAL   B CG2 1 
ATOM   2148 N N   . ALA   B 1 34  ? -16.614 -19.535 -52.887 1.00 37.61 ?  34  ALA   B N   1 
ATOM   2149 C CA  . ALA   B 1 34  ? -15.759 -18.514 -53.476 1.00 43.45 ?  34  ALA   B CA  1 
ATOM   2150 C C   . ALA   B 1 34  ? -15.754 -17.258 -52.617 1.00 36.95 ?  34  ALA   B C   1 
ATOM   2151 O O   . ALA   B 1 34  ? -14.719 -16.596 -52.462 1.00 42.27 ?  34  ALA   B O   1 
ATOM   2152 C CB  . ALA   B 1 34  ? -16.225 -18.197 -54.902 1.00 45.33 ?  34  ALA   B CB  1 
ATOM   2153 N N   . GLN   B 1 35  ? -16.893 -16.942 -52.019 1.00 39.59 ?  35  GLN   B N   1 
ATOM   2154 C CA  . GLN   B 1 35  ? -17.018 -15.719 -51.256 1.00 36.60 ?  35  GLN   B CA  1 
ATOM   2155 C C   . GLN   B 1 35  ? -18.125 -15.912 -50.242 1.00 42.23 ?  35  GLN   B C   1 
ATOM   2156 O O   . GLN   B 1 35  ? -19.197 -16.424 -50.580 1.00 39.47 ?  35  GLN   B O   1 
ATOM   2157 C CB  . GLN   B 1 35  ? -17.325 -14.538 -52.182 1.00 42.54 ?  35  GLN   B CB  1 
ATOM   2158 C CG  . GLN   B 1 35  ? -17.201 -13.200 -51.516 1.00 45.68 ?  35  GLN   B CG  1 
ATOM   2159 C CD  . GLN   B 1 35  ? -17.315 -12.057 -52.496 1.00 47.53 ?  35  GLN   B CD  1 
ATOM   2160 O OE1 . GLN   B 1 35  ? -16.444 -11.862 -53.347 1.00 48.96 ?  35  GLN   B OE1 1 
ATOM   2161 N NE2 . GLN   B 1 35  ? -18.397 -11.295 -52.384 1.00 36.90 ?  35  GLN   B NE2 1 
ATOM   2162 N N   . THR   B 1 36  ? -17.853 -15.534 -49.002 1.00 37.02 ?  36  THR   B N   1 
ATOM   2163 C CA  . THR   B 1 36  ? -18.899 -15.409 -48.009 1.00 39.22 ?  36  THR   B CA  1 
ATOM   2164 C C   . THR   B 1 36  ? -18.508 -14.279 -47.075 1.00 36.38 ?  36  THR   B C   1 
ATOM   2165 O O   . THR   B 1 36  ? -17.422 -13.703 -47.189 1.00 37.68 ?  36  THR   B O   1 
ATOM   2166 C CB  . THR   B 1 36  ? -19.111 -16.711 -47.237 1.00 42.15 ?  36  THR   B CB  1 
ATOM   2167 O OG1 . THR   B 1 36  ? -20.328 -16.616 -46.485 1.00 37.45 ?  36  THR   B OG1 1 
ATOM   2168 C CG2 . THR   B 1 36  ? -17.944 -16.967 -46.281 1.00 33.34 ?  36  THR   B CG2 1 
ATOM   2169 N N   . GLY   B 1 37  ? -19.399 -13.978 -46.134 1.00 38.84 ?  37  GLY   B N   1 
ATOM   2170 C CA  . GLY   B 1 37  ? -19.149 -12.930 -45.165 1.00 42.79 ?  37  GLY   B CA  1 
ATOM   2171 C C   . GLY   B 1 37  ? -18.249 -13.425 -44.057 1.00 45.00 ?  37  GLY   B C   1 
ATOM   2172 O O   . GLY   B 1 37  ? -17.276 -12.760 -43.694 1.00 37.26 ?  37  GLY   B O   1 
ATOM   2173 N N   . SER   B 1 38  ? -18.568 -14.603 -43.519 1.00 34.63 ?  38  SER   B N   1 
ATOM   2174 C CA  . SER   B 1 38  ? -17.755 -15.198 -42.465 1.00 37.04 ?  38  SER   B CA  1 
ATOM   2175 C C   . SER   B 1 38  ? -18.009 -16.696 -42.487 1.00 34.13 ?  38  SER   B C   1 
ATOM   2176 O O   . SER   B 1 38  ? -19.165 -17.124 -42.435 1.00 40.51 ?  38  SER   B O   1 
ATOM   2177 C CB  . SER   B 1 38  ? -18.104 -14.591 -41.083 1.00 31.35 ?  38  SER   B CB  1 
ATOM   2178 O OG  . SER   B 1 38  ? -17.667 -15.392 -39.992 1.00 29.53 ?  38  SER   B OG  1 
ATOM   2179 N N   . THR   B 1 39  ? -16.943 -17.491 -42.585 1.00 34.03 ?  39  THR   B N   1 
ATOM   2180 C CA  . THR   B 1 39  ? -17.139 -18.937 -42.530 1.00 33.35 ?  39  THR   B CA  1 
ATOM   2181 C C   . THR   B 1 39  ? -17.579 -19.386 -41.140 1.00 36.77 ?  39  THR   B C   1 
ATOM   2182 O O   . THR   B 1 39  ? -18.282 -20.403 -41.010 1.00 31.99 ?  39  THR   B O   1 
ATOM   2183 C CB  . THR   B 1 39  ? -15.869 -19.666 -42.961 1.00 29.20 ?  39  THR   B CB  1 
ATOM   2184 O OG1 . THR   B 1 39  ? -14.785 -19.309 -42.096 1.00 32.12 ?  39  THR   B OG1 1 
ATOM   2185 C CG2 . THR   B 1 39  ? -15.513 -19.281 -44.380 1.00 30.24 ?  39  THR   B CG2 1 
ATOM   2186 N N   . ASN   B 1 40  ? -17.197 -18.640 -40.095 1.00 34.51 ?  40  ASN   B N   1 
ATOM   2187 C CA  . ASN   B 1 40  ? -17.711 -18.933 -38.760 1.00 33.59 ?  40  ASN   B CA  1 
ATOM   2188 C C   . ASN   B 1 40  ? -19.217 -18.692 -38.721 1.00 34.52 ?  40  ASN   B C   1 
ATOM   2189 O O   . ASN   B 1 40  ? -19.992 -19.563 -38.303 1.00 32.92 ?  40  ASN   B O   1 
ATOM   2190 C CB  . ASN   B 1 40  ? -16.991 -18.085 -37.704 1.00 31.78 ?  40  ASN   B CB  1 
ATOM   2191 C CG  . ASN   B 1 40  ? -15.731 -18.752 -37.130 1.00 35.77 ?  40  ASN   B CG  1 
ATOM   2192 O OD1 . ASN   B 1 40  ? -15.115 -19.631 -37.749 1.00 31.84 ?  40  ASN   B OD1 1 
ATOM   2193 N ND2 . ASN   B 1 40  ? -15.341 -18.320 -35.930 1.00 34.62 ?  40  ASN   B ND2 1 
ATOM   2194 N N   . ALA   B 1 41  ? -19.648 -17.536 -39.218 1.00 33.14 ?  41  ALA   B N   1 
ATOM   2195 C CA  . ALA   B 1 41  ? -21.073 -17.227 -39.286 1.00 43.48 ?  41  ALA   B CA  1 
ATOM   2196 C C   . ALA   B 1 41  ? -21.839 -18.309 -40.038 1.00 35.49 ?  41  ALA   B C   1 
ATOM   2197 O O   . ALA   B 1 41  ? -22.869 -18.798 -39.565 1.00 38.92 ?  41  ALA   B O   1 
ATOM   2198 C CB  . ALA   B 1 41  ? -21.278 -15.863 -39.956 1.00 39.52 ?  41  ALA   B CB  1 
ATOM   2199 N N   . ASP   B 1 42  ? -21.319 -18.716 -41.197 1.00 32.87 ?  42  ASP   B N   1 
ATOM   2200 C CA  . ASP   B 1 42  ? -22.022 -19.662 -42.057 1.00 33.42 ?  42  ASP   B CA  1 
ATOM   2201 C C   . ASP   B 1 42  ? -22.233 -21.014 -41.375 1.00 37.74 ?  42  ASP   B C   1 
ATOM   2202 O O   . ASP   B 1 42  ? -23.301 -21.629 -41.513 1.00 40.80 ?  42  ASP   B O   1 
ATOM   2203 C CB  . ASP   B 1 42  ? -21.232 -19.826 -43.344 1.00 40.13 ?  42  ASP   B CB  1 
ATOM   2204 C CG  . ASP   B 1 42  ? -21.339 -18.618 -44.233 1.00 48.71 ?  42  ASP   B CG  1 
ATOM   2205 O OD1 . ASP   B 1 42  ? -21.912 -17.609 -43.758 1.00 55.50 ?  42  ASP   B OD1 1 
ATOM   2206 O OD2 . ASP   B 1 42  ? -20.818 -18.654 -45.378 1.00 51.66 -1 42  ASP   B OD2 1 
ATOM   2207 N N   . LEU   B 1 43  ? -21.229 -21.506 -40.646 1.00 27.27 ?  43  LEU   B N   1 
ATOM   2208 C CA  . LEU   B 1 43  ? -21.419 -22.770 -39.945 1.00 29.18 ?  43  LEU   B CA  1 
ATOM   2209 C C   . LEU   B 1 43  ? -22.303 -22.617 -38.711 1.00 32.98 ?  43  LEU   B C   1 
ATOM   2210 O O   . LEU   B 1 43  ? -23.051 -23.533 -38.378 1.00 32.98 ?  43  LEU   B O   1 
ATOM   2211 C CB  . LEU   B 1 43  ? -20.076 -23.382 -39.547 1.00 29.53 ?  43  LEU   B CB  1 
ATOM   2212 C CG  . LEU   B 1 43  ? -19.229 -24.040 -40.645 1.00 35.27 ?  43  LEU   B CG  1 
ATOM   2213 C CD1 . LEU   B 1 43  ? -18.024 -24.754 -39.992 1.00 36.43 ?  43  LEU   B CD1 1 
ATOM   2214 C CD2 . LEU   B 1 43  ? -20.067 -25.022 -41.402 1.00 27.89 ?  43  LEU   B CD2 1 
ATOM   2215 N N   . LEU   B 1 44  ? -22.227 -21.494 -38.004 1.00 33.65 ?  44  LEU   B N   1 
ATOM   2216 C CA  . LEU   B 1 44  ? -23.156 -21.300 -36.897 1.00 41.72 ?  44  LEU   B CA  1 
ATOM   2217 C C   . LEU   B 1 44  ? -24.593 -21.216 -37.405 1.00 36.42 ?  44  LEU   B C   1 
ATOM   2218 O O   . LEU   B 1 44  ? -25.511 -21.743 -36.769 1.00 43.49 ?  44  LEU   B O   1 
ATOM   2219 C CB  . LEU   B 1 44  ? -22.779 -20.055 -36.093 1.00 40.75 ?  44  LEU   B CB  1 
ATOM   2220 C CG  . LEU   B 1 44  ? -21.427 -20.106 -35.374 1.00 41.32 ?  44  LEU   B CG  1 
ATOM   2221 C CD1 . LEU   B 1 44  ? -20.877 -18.689 -35.160 1.00 40.68 ?  44  LEU   B CD1 1 
ATOM   2222 C CD2 . LEU   B 1 44  ? -21.483 -20.881 -34.048 1.00 31.69 ?  44  LEU   B CD2 1 
ATOM   2223 N N   . ALA   B 1 45  ? -24.805 -20.580 -38.560 1.00 34.76 ?  45  ALA   B N   1 
ATOM   2224 C CA  . ALA   B 1 45  ? -26.149 -20.534 -39.125 1.00 39.54 ?  45  ALA   B CA  1 
ATOM   2225 C C   . ALA   B 1 45  ? -26.602 -21.928 -39.526 1.00 45.39 ?  45  ALA   B C   1 
ATOM   2226 O O   . ALA   B 1 45  ? -27.740 -22.322 -39.255 1.00 43.36 ?  45  ALA   B O   1 
ATOM   2227 C CB  . ALA   B 1 45  ? -26.198 -19.584 -40.321 1.00 38.32 ?  45  ALA   B CB  1 
ATOM   2228 N N   . ARG   B 1 46  ? -25.707 -22.704 -40.141 1.00 41.40 ?  46  ARG   B N   1 
ATOM   2229 C CA  . ARG   B 1 46  ? -26.027 -24.092 -40.442 1.00 44.60 ?  46  ARG   B CA  1 
ATOM   2230 C C   . ARG   B 1 46  ? -26.510 -24.832 -39.201 1.00 44.81 ?  46  ARG   B C   1 
ATOM   2231 O O   . ARG   B 1 46  ? -27.525 -25.537 -39.242 1.00 48.13 ?  46  ARG   B O   1 
ATOM   2232 C CB  . ARG   B 1 46  ? -24.804 -24.784 -41.023 1.00 37.65 ?  46  ARG   B CB  1 
ATOM   2233 C CG  . ARG   B 1 46  ? -24.579 -24.471 -42.443 1.00 35.34 ?  46  ARG   B CG  1 
ATOM   2234 C CD  . ARG   B 1 46  ? -23.887 -25.627 -43.076 1.00 37.11 ?  46  ARG   B CD  1 
ATOM   2235 N NE  . ARG   B 1 46  ? -22.989 -25.175 -44.119 1.00 46.90 ?  46  ARG   B NE  1 
ATOM   2236 C CZ  . ARG   B 1 46  ? -21.891 -25.825 -44.473 1.00 37.83 ?  46  ARG   B CZ  1 
ATOM   2237 N NH1 . ARG   B 1 46  ? -21.125 -25.351 -45.436 1.00 42.15 ?  46  ARG   B NH1 1 
ATOM   2238 N NH2 . ARG   B 1 46  ? -21.575 -26.950 -43.866 1.00 37.09 ?  46  ARG   B NH2 1 
ATOM   2239 N N   . ALA   B 1 47  ? -25.795 -24.673 -38.084 1.00 42.08 ?  47  ALA   B N   1 
ATOM   2240 C CA  . ALA   B 1 47  ? -26.136 -25.405 -36.868 1.00 40.81 ?  47  ALA   B CA  1 
ATOM   2241 C C   . ALA   B 1 47  ? -27.447 -24.915 -36.265 1.00 47.48 ?  47  ALA   B C   1 
ATOM   2242 O O   . ALA   B 1 47  ? -28.229 -25.712 -35.725 1.00 40.53 ?  47  ALA   B O   1 
ATOM   2243 C CB  . ALA   B 1 47  ? -25.006 -25.268 -35.851 1.00 45.71 ?  47  ALA   B CB  1 
ATOM   2244 N N   . ALA   B 1 48  ? -27.684 -23.602 -36.313 1.00 44.25 ?  48  ALA   B N   1 
ATOM   2245 C CA  . ALA   B 1 48  ? -28.927 -23.040 -35.804 1.00 48.56 ?  48  ALA   B CA  1 
ATOM   2246 C C   . ALA   B 1 48  ? -30.117 -23.472 -36.645 1.00 51.78 ?  48  ALA   B C   1 
ATOM   2247 O O   . ALA   B 1 48  ? -31.248 -23.448 -36.158 1.00 50.50 ?  48  ALA   B O   1 
ATOM   2248 C CB  . ALA   B 1 48  ? -28.839 -21.514 -35.762 1.00 41.52 ?  48  ALA   B CB  1 
ATOM   2249 N N   . SER   B 1 49  ? -29.881 -23.863 -37.894 1.00 52.52 ?  49  SER   B N   1 
ATOM   2250 C CA  . SER   B 1 49  ? -30.921 -24.395 -38.755 1.00 50.49 ?  49  SER   B CA  1 
ATOM   2251 C C   . SER   B 1 49  ? -31.196 -25.871 -38.499 1.00 52.15 ?  49  SER   B C   1 
ATOM   2252 O O   . SER   B 1 49  ? -31.998 -26.469 -39.227 1.00 51.34 ?  49  SER   B O   1 
ATOM   2253 C CB  . SER   B 1 49  ? -30.536 -24.184 -40.215 1.00 48.23 ?  49  SER   B CB  1 
ATOM   2254 O OG  . SER   B 1 49  ? -29.749 -25.269 -40.679 1.00 64.04 ?  49  SER   B OG  1 
ATOM   2255 N N   . GLY   B 1 50  ? -30.555 -26.469 -37.492 1.00 52.77 ?  50  GLY   B N   1 
ATOM   2256 C CA  . GLY   B 1 50  ? -30.791 -27.844 -37.108 1.00 50.37 ?  50  GLY   B CA  1 
ATOM   2257 C C   . GLY   B 1 50  ? -29.774 -28.849 -37.622 1.00 57.63 ?  50  GLY   B C   1 
ATOM   2258 O O   . GLY   B 1 50  ? -29.722 -29.972 -37.098 1.00 60.91 ?  50  GLY   B O   1 
ATOM   2259 N N   . ALA   B 1 51  ? -28.967 -28.480 -38.620 1.00 48.44 ?  51  ALA   B N   1 
ATOM   2260 C CA  . ALA   B 1 51  ? -27.991 -29.401 -39.200 1.00 46.79 ?  51  ALA   B CA  1 
ATOM   2261 C C   . ALA   B 1 51  ? -26.890 -29.779 -38.204 1.00 49.47 ?  51  ALA   B C   1 
ATOM   2262 O O   . ALA   B 1 51  ? -26.535 -29.008 -37.306 1.00 47.59 ?  51  ALA   B O   1 
ATOM   2263 C CB  . ALA   B 1 51  ? -27.352 -28.773 -40.440 1.00 43.77 ?  51  ALA   B CB  1 
ATOM   2264 N N   . ASP   B 1 52  ? -26.327 -30.978 -38.390 1.00 47.82 ?  52  ASP   B N   1 
ATOM   2265 C CA  . ASP   B 1 52  ? -25.172 -31.436 -37.625 1.00 39.88 ?  52  ASP   B CA  1 
ATOM   2266 C C   . ASP   B 1 52  ? -23.920 -30.934 -38.324 1.00 43.38 ?  52  ASP   B C   1 
ATOM   2267 O O   . ASP   B 1 52  ? -23.686 -31.271 -39.492 1.00 43.41 ?  52  ASP   B O   1 
ATOM   2268 C CB  . ASP   B 1 52  ? -25.138 -32.963 -37.532 1.00 46.88 ?  52  ASP   B CB  1 
ATOM   2269 C CG  . ASP   B 1 52  ? -24.237 -33.469 -36.411 1.00 54.71 ?  52  ASP   B CG  1 
ATOM   2270 O OD1 . ASP   B 1 52  ? -24.661 -34.373 -35.666 1.00 64.72 ?  52  ASP   B OD1 1 
ATOM   2271 O OD2 . ASP   B 1 52  ? -23.112 -32.962 -36.251 1.00 53.36 -1 52  ASP   B OD2 1 
ATOM   2272 N N   . ILE   B 1 53  ? -23.110 -30.140 -37.620 1.00 35.35 ?  53  ILE   B N   1 
ATOM   2273 C CA  . ILE   B 1 53  ? -21.869 -29.619 -38.196 1.00 34.28 ?  53  ILE   B CA  1 
ATOM   2274 C C   . ILE   B 1 53  ? -20.633 -30.263 -37.592 1.00 33.84 ?  53  ILE   B C   1 
ATOM   2275 O O   . ILE   B 1 53  ? -19.513 -29.792 -37.841 1.00 28.00 ?  53  ILE   B O   1 
ATOM   2276 C CB  . ILE   B 1 53  ? -21.786 -28.089 -38.066 1.00 38.84 ?  53  ILE   B CB  1 
ATOM   2277 C CG1 . ILE   B 1 53  ? -21.737 -27.709 -36.576 1.00 32.85 ?  53  ILE   B CG1 1 
ATOM   2278 C CG2 . ILE   B 1 53  ? -22.921 -27.432 -38.888 1.00 32.48 ?  53  ILE   B CG2 1 
ATOM   2279 C CD1 . ILE   B 1 53  ? -21.202 -26.297 -36.293 1.00 33.05 ?  53  ILE   B CD1 1 
ATOM   2280 N N   . ASP   B 1 54  ? -20.790 -31.311 -36.785 1.00 29.91 ?  54  ASP   B N   1 
ATOM   2281 C CA  . ASP   B 1 54  ? -19.608 -31.973 -36.244 1.00 34.61 ?  54  ASP   B CA  1 
ATOM   2282 C C   . ASP   B 1 54  ? -18.831 -32.614 -37.386 1.00 31.47 ?  54  ASP   B C   1 
ATOM   2283 O O   . ASP   B 1 54  ? -19.390 -33.381 -38.175 1.00 34.56 ?  54  ASP   B O   1 
ATOM   2284 C CB  . ASP   B 1 54  ? -19.988 -33.024 -35.196 1.00 29.18 ?  54  ASP   B CB  1 
ATOM   2285 C CG  . ASP   B 1 54  ? -18.774 -33.742 -34.633 1.00 40.47 ?  54  ASP   B CG  1 
ATOM   2286 O OD1 . ASP   B 1 54  ? -17.962 -33.113 -33.909 1.00 39.00 ?  54  ASP   B OD1 1 
ATOM   2287 O OD2 . ASP   B 1 54  ? -18.606 -34.941 -34.935 1.00 51.61 -1 54  ASP   B OD2 1 
ATOM   2288 N N   . GLY   B 1 55  ? -17.553 -32.265 -37.502 1.00 30.02 ?  55  GLY   B N   1 
ATOM   2289 C CA  . GLY   B 1 55  ? -16.728 -32.806 -38.567 1.00 25.77 ?  55  GLY   B CA  1 
ATOM   2290 C C   . GLY   B 1 55  ? -16.938 -32.167 -39.919 1.00 35.45 ?  55  GLY   B C   1 
ATOM   2291 O O   . GLY   B 1 55  ? -16.523 -32.736 -40.931 1.00 28.73 ?  55  GLY   B O   1 
ATOM   2292 N N   . VAL   B 1 56  ? -17.562 -30.992 -39.972 1.00 29.37 ?  56  VAL   B N   1 
ATOM   2293 C CA  . VAL   B 1 56  ? -17.868 -30.313 -41.221 1.00 27.76 ?  56  VAL   B CA  1 
ATOM   2294 C C   . VAL   B 1 56  ? -16.856 -29.185 -41.433 1.00 30.95 ?  56  VAL   B C   1 
ATOM   2295 O O   . VAL   B 1 56  ? -16.606 -28.391 -40.515 1.00 30.45 ?  56  VAL   B O   1 
ATOM   2296 C CB  . VAL   B 1 56  ? -19.303 -29.772 -41.200 1.00 29.91 ?  56  VAL   B CB  1 
ATOM   2297 C CG1 . VAL   B 1 56  ? -19.480 -28.718 -42.250 1.00 33.41 ?  56  VAL   B CG1 1 
ATOM   2298 C CG2 . VAL   B 1 56  ? -20.309 -30.916 -41.368 1.00 30.79 ?  56  VAL   B CG2 1 
ATOM   2299 N N   . VAL   B 1 57  ? -16.285 -29.105 -42.643 1.00 29.06 ?  57  VAL   B N   1 
ATOM   2300 C CA  . VAL   B 1 57  ? -15.289 -28.091 -43.009 1.00 34.99 ?  57  VAL   B CA  1 
ATOM   2301 C C   . VAL   B 1 57  ? -15.891 -27.157 -44.052 1.00 30.52 ?  57  VAL   B C   1 
ATOM   2302 O O   . VAL   B 1 57  ? -16.455 -27.621 -45.050 1.00 35.63 ?  57  VAL   B O   1 
ATOM   2303 C CB  . VAL   B 1 57  ? -13.997 -28.733 -43.560 1.00 26.45 ?  57  VAL   B CB  1 
ATOM   2304 C CG1 . VAL   B 1 57  ? -12.923 -27.698 -43.775 1.00 21.58 ?  57  VAL   B CG1 1 
ATOM   2305 C CG2 . VAL   B 1 57  ? -13.486 -29.844 -42.642 1.00 33.36 ?  57  VAL   B CG2 1 
ATOM   2306 N N   . LEU   B 1 58  ? -15.752 -25.848 -43.834 1.00 32.18 ?  58  LEU   B N   1 
ATOM   2307 C CA  . LEU   B 1 58  ? -16.082 -24.813 -44.819 1.00 27.36 ?  58  LEU   B CA  1 
ATOM   2308 C C   . LEU   B 1 58  ? -14.840 -23.975 -45.082 1.00 25.32 ?  58  LEU   B C   1 
ATOM   2309 O O   . LEU   B 1 58  ? -14.202 -23.497 -44.143 1.00 33.01 ?  58  LEU   B O   1 
ATOM   2310 C CB  . LEU   B 1 58  ? -17.211 -23.909 -44.333 1.00 28.68 ?  58  LEU   B CB  1 
ATOM   2311 C CG  . LEU   B 1 58  ? -17.670 -22.823 -45.309 1.00 38.17 ?  58  LEU   B CG  1 
ATOM   2312 C CD1 . LEU   B 1 58  ? -18.382 -23.442 -46.529 1.00 36.10 ?  58  LEU   B CD1 1 
ATOM   2313 C CD2 . LEU   B 1 58  ? -18.575 -21.811 -44.611 1.00 33.99 ?  58  LEU   B CD2 1 
ATOM   2314 N N   . ILE   B 1 59  ? -14.458 -23.850 -46.345 1.00 27.41 ?  59  ILE   B N   1 
ATOM   2315 C CA  . ILE   B 1 59  ? -13.328 -23.028 -46.756 1.00 29.65 ?  59  ILE   B CA  1 
ATOM   2316 C C   . ILE   B 1 59  ? -13.854 -21.951 -47.699 1.00 33.43 ?  59  ILE   B C   1 
ATOM   2317 O O   . ILE   B 1 59  ? -14.698 -22.239 -48.553 1.00 34.67 ?  59  ILE   B O   1 
ATOM   2318 C CB  . ILE   B 1 59  ? -12.239 -23.874 -47.445 1.00 29.20 ?  59  ILE   B CB  1 
ATOM   2319 C CG1 . ILE   B 1 59  ? -11.712 -24.971 -46.514 1.00 33.81 ?  59  ILE   B CG1 1 
ATOM   2320 C CG2 . ILE   B 1 59  ? -11.095 -23.002 -47.864 1.00 27.44 ?  59  ILE   B CG2 1 
ATOM   2321 C CD1 . ILE   B 1 59  ? -10.983 -26.095 -47.263 1.00 28.26 ?  59  ILE   B CD1 1 
ATOM   2322 N N   . ALA   B 1 60  ? -13.362 -20.720 -47.559 1.00 33.12 ?  60  ALA   B N   1 
ATOM   2323 C CA  . ALA   B 1 60  ? -13.790 -19.614 -48.412 1.00 29.98 ?  60  ALA   B CA  1 
ATOM   2324 C C   . ALA   B 1 60  ? -12.598 -18.993 -49.129 1.00 31.55 ?  60  ALA   B C   1 
ATOM   2325 O O   . ALA   B 1 60  ? -11.598 -18.635 -48.497 1.00 30.72 ?  60  ALA   B O   1 
ATOM   2326 C CB  . ALA   B 1 60  ? -14.538 -18.548 -47.603 1.00 30.73 ?  60  ALA   B CB  1 
ATOM   2327 N N   . GLU   B 1 61  ? -12.699 -18.868 -50.453 1.00 35.54 ?  61  GLU   B N   1 
ATOM   2328 C CA  . GLU   B 1 61  ? -11.626 -18.197 -51.179 1.00 38.41 ?  61  GLU   B CA  1 
ATOM   2329 C C   . GLU   B 1 61  ? -11.545 -16.721 -50.816 1.00 40.64 ?  61  GLU   B C   1 
ATOM   2330 O O   . GLU   B 1 61  ? -10.471 -16.120 -50.914 1.00 36.91 ?  61  GLU   B O   1 
ATOM   2331 C CB  . GLU   B 1 61  ? -11.823 -18.360 -52.685 1.00 40.67 ?  61  GLU   B CB  1 
ATOM   2332 C CG  . GLU   B 1 61  ? -11.653 -19.783 -53.146 1.00 46.94 ?  61  GLU   B CG  1 
ATOM   2333 C CD  . GLU   B 1 61  ? -10.192 -20.181 -53.307 1.00 57.11 ?  61  GLU   B CD  1 
ATOM   2334 O OE1 . GLU   B 1 61  ? -9.339  -19.790 -52.465 1.00 53.69 ?  61  GLU   B OE1 1 
ATOM   2335 O OE2 . GLU   B 1 61  ? -9.904  -20.909 -54.282 1.00 61.43 -1 61  GLU   B OE2 1 
ATOM   2336 N N   . HIS   B 1 62  ? -12.645 -16.137 -50.373 1.00 34.43 ?  62  HIS   B N   1 
ATOM   2337 C CA  . HIS   B 1 62  ? -12.634 -14.741 -49.986 1.00 39.58 ?  62  HIS   B CA  1 
ATOM   2338 C C   . HIS   B 1 62  ? -13.655 -14.557 -48.882 1.00 41.58 ?  62  HIS   B C   1 
ATOM   2339 O O   . HIS   B 1 62  ? -14.725 -15.180 -48.906 1.00 41.47 ?  62  HIS   B O   1 
ATOM   2340 C CB  . HIS   B 1 62  ? -12.943 -13.837 -51.184 1.00 42.00 ?  62  HIS   B CB  1 
ATOM   2341 C CG  . HIS   B 1 62  ? -12.903 -12.382 -50.859 1.00 49.44 ?  62  HIS   B CG  1 
ATOM   2342 N ND1 . HIS   B 1 62  ? -11.952 -11.834 -50.023 1.00 46.27 ?  62  HIS   B ND1 1 
ATOM   2343 C CD2 . HIS   B 1 62  ? -13.699 -11.359 -51.249 1.00 51.05 ?  62  HIS   B CD2 1 
ATOM   2344 C CE1 . HIS   B 1 62  ? -12.169 -10.537 -49.906 1.00 46.26 ?  62  HIS   B CE1 1 
ATOM   2345 N NE2 . HIS   B 1 62  ? -13.223 -10.223 -50.640 1.00 49.23 ?  62  HIS   B NE2 1 
ATOM   2346 N N   . GLN   B 1 63  ? -13.309 -13.718 -47.908 1.00 34.58 ?  63  GLN   B N   1 
ATOM   2347 C CA  . GLN   B 1 63  ? -14.181 -13.428 -46.778 1.00 43.74 ?  63  GLN   B CA  1 
ATOM   2348 C C   . GLN   B 1 63  ? -14.240 -11.917 -46.584 1.00 38.80 ?  63  GLN   B C   1 
ATOM   2349 O O   . GLN   B 1 63  ? -13.212 -11.278 -46.355 1.00 39.51 ?  63  GLN   B O   1 
ATOM   2350 C CB  . GLN   B 1 63  ? -13.671 -14.126 -45.514 1.00 38.73 ?  63  GLN   B CB  1 
ATOM   2351 C CG  . GLN   B 1 63  ? -14.679 -14.276 -44.417 1.00 33.46 ?  63  GLN   B CG  1 
ATOM   2352 C CD  . GLN   B 1 63  ? -14.116 -15.079 -43.256 1.00 33.09 ?  63  GLN   B CD  1 
ATOM   2353 O OE1 . GLN   B 1 63  ? -14.568 -16.193 -42.970 1.00 31.90 ?  63  GLN   B OE1 1 
ATOM   2354 N NE2 . GLN   B 1 63  ? -13.094 -14.534 -42.605 1.00 31.74 ?  63  GLN   B NE2 1 
ATOM   2355 N N   . THR   B 1 64  ? -15.445 -11.357 -46.634 1.00 42.14 ?  64  THR   B N   1 
ATOM   2356 C CA  . THR   B 1 64  ? -15.622 -9.913  -46.656 1.00 36.48 ?  64  THR   B CA  1 
ATOM   2357 C C   . THR   B 1 64  ? -16.133 -9.317  -45.350 1.00 38.75 ?  64  THR   B C   1 
ATOM   2358 O O   . THR   B 1 64  ? -16.145 -8.086  -45.215 1.00 45.47 ?  64  THR   B O   1 
ATOM   2359 C CB  . THR   B 1 64  ? -16.593 -9.539  -47.777 1.00 32.16 ?  64  THR   B CB  1 
ATOM   2360 O OG1 . THR   B 1 64  ? -17.897 -10.022 -47.438 1.00 41.80 ?  64  THR   B OG1 1 
ATOM   2361 C CG2 . THR   B 1 64  ? -16.161 -10.149 -49.059 1.00 33.65 ?  64  THR   B CG2 1 
ATOM   2362 N N   . ALA   B 1 65  ? -16.580 -10.133 -44.401 1.00 40.91 ?  65  ALA   B N   1 
ATOM   2363 C CA  . ALA   B 1 65  ? -17.068 -9.646  -43.112 1.00 40.57 ?  65  ALA   B CA  1 
ATOM   2364 C C   . ALA   B 1 65  ? -16.475 -10.478 -41.979 1.00 40.07 ?  65  ALA   B C   1 
ATOM   2365 O O   . ALA   B 1 65  ? -17.177 -10.934 -41.072 1.00 36.98 ?  65  ALA   B O   1 
ATOM   2366 C CB  . ALA   B 1 65  ? -18.597 -9.655  -43.060 1.00 36.82 ?  65  ALA   B CB  1 
ATOM   2367 N N   . GLY   B 1 66  ? -15.155 -10.669 -42.025 1.00 40.35 ?  66  GLY   B N   1 
ATOM   2368 C CA  . GLY   B 1 66  ? -14.505 -11.572 -41.089 1.00 36.62 ?  66  GLY   B CA  1 
ATOM   2369 C C   . GLY   B 1 66  ? -14.583 -11.098 -39.649 1.00 38.00 ?  66  GLY   B C   1 
ATOM   2370 O O   . GLY   B 1 66  ? -14.574 -9.907  -39.355 1.00 38.89 ?  66  GLY   B O   1 
ATOM   2371 N N   . ARG   B 1 67  ? -14.656 -12.061 -38.735 1.00 29.32 ?  67  ARG   B N   1 
ATOM   2372 C CA  . ARG   B 1 67  ? -14.773 -11.796 -37.307 1.00 37.57 ?  67  ARG   B CA  1 
ATOM   2373 C C   . ARG   B 1 67  ? -13.450 -12.085 -36.615 1.00 35.89 ?  67  ARG   B C   1 
ATOM   2374 O O   . ARG   B 1 67  ? -12.784 -13.077 -36.924 1.00 30.38 ?  67  ARG   B O   1 
ATOM   2375 C CB  . ARG   B 1 67  ? -15.866 -12.660 -36.664 1.00 37.19 ?  67  ARG   B CB  1 
ATOM   2376 C CG  . ARG   B 1 67  ? -17.230 -12.538 -37.313 1.00 39.13 ?  67  ARG   B CG  1 
ATOM   2377 C CD  . ARG   B 1 67  ? -18.138 -13.588 -36.761 1.00 39.10 ?  67  ARG   B CD  1 
ATOM   2378 N NE  . ARG   B 1 67  ? -19.533 -13.313 -37.064 1.00 50.79 ?  67  ARG   B NE  1 
ATOM   2379 C CZ  . ARG   B 1 67  ? -20.534 -14.116 -36.701 1.00 55.15 ?  67  ARG   B CZ  1 
ATOM   2380 N NH1 . ARG   B 1 67  ? -20.274 -15.246 -36.031 1.00 41.27 ?  67  ARG   B NH1 1 
ATOM   2381 N NH2 . ARG   B 1 67  ? -21.786 -13.799 -37.015 1.00 42.11 ?  67  ARG   B NH2 1 
ATOM   2382 N N   . GLY   B 1 68  ? -13.062 -11.206 -35.694 1.00 30.59 ?  68  GLY   B N   1 
ATOM   2383 C CA  . GLY   B 1 68  ? -12.001 -11.483 -34.753 1.00 36.76 ?  68  GLY   B CA  1 
ATOM   2384 C C   . GLY   B 1 68  ? -12.543 -11.731 -33.363 1.00 33.10 ?  68  GLY   B C   1 
ATOM   2385 O O   . GLY   B 1 68  ? -13.728 -12.033 -33.173 1.00 42.37 ?  68  GLY   B O   1 
ATOM   2386 N N   . ARG   B 1 69  ? -11.668 -11.589 -32.372 1.00 33.22 ?  69  ARG   B N   1 
ATOM   2387 C CA  . ARG   B 1 69  ? -12.071 -11.725 -30.983 1.00 31.90 ?  69  ARG   B CA  1 
ATOM   2388 C C   . ARG   B 1 69  ? -12.340 -10.345 -30.393 1.00 45.44 ?  69  ARG   B C   1 
ATOM   2389 O O   . ARG   B 1 69  ? -11.847 -9.326  -30.885 1.00 37.06 ?  69  ARG   B O   1 
ATOM   2390 C CB  . ARG   B 1 69  ? -10.999 -12.455 -30.163 1.00 42.54 ?  69  ARG   B CB  1 
ATOM   2391 N N   . HIS   B 1 70  ? -13.147 -10.324 -29.329 1.00 49.67 ?  70  HIS   B N   1 
ATOM   2392 C CA  . HIS   B 1 70  ? -13.430 -9.092  -28.585 1.00 51.02 ?  70  HIS   B CA  1 
ATOM   2393 C C   . HIS   B 1 70  ? -14.080 -8.025  -29.451 1.00 41.82 ?  70  HIS   B C   1 
ATOM   2394 O O   . HIS   B 1 70  ? -13.832 -6.834  -29.266 1.00 49.48 ?  70  HIS   B O   1 
ATOM   2395 C CB  . HIS   B 1 70  ? -12.167 -8.518  -27.952 1.00 51.23 ?  70  HIS   B CB  1 
ATOM   2396 C CG  . HIS   B 1 70  ? -11.426 -9.489  -27.094 1.00 54.18 ?  70  HIS   B CG  1 
ATOM   2397 N ND1 . HIS   B 1 70  ? -10.050 -9.491  -26.999 1.00 53.14 ?  70  HIS   B ND1 1 
ATOM   2398 C CD2 . HIS   B 1 70  ? -11.866 -10.482 -26.284 1.00 53.18 ?  70  HIS   B CD2 1 
ATOM   2399 C CE1 . HIS   B 1 70  ? -9.674  -10.446 -26.165 1.00 64.58 ?  70  HIS   B CE1 1 
ATOM   2400 N NE2 . HIS   B 1 70  ? -10.756 -11.063 -25.720 1.00 65.07 ?  70  HIS   B NE2 1 
ATOM   2401 N N   . GLY   B 1 71  ? -14.906 -8.435  -30.401 1.00 39.84 ?  71  GLY   B N   1 
ATOM   2402 C CA  . GLY   B 1 71  ? -15.549 -7.503  -31.288 1.00 39.71 ?  71  GLY   B CA  1 
ATOM   2403 C C   . GLY   B 1 71  ? -14.701 -7.014  -32.440 1.00 41.22 ?  71  GLY   B C   1 
ATOM   2404 O O   . GLY   B 1 71  ? -15.198 -6.226  -33.256 1.00 38.90 ?  71  GLY   B O   1 
ATOM   2405 N N   . ARG   B 1 72  ? -13.444 -7.437  -32.543 1.00 33.20 ?  72  ARG   B N   1 
ATOM   2406 C CA  . ARG   B 1 72  ? -12.646 -6.987  -33.674 1.00 37.75 ?  72  ARG   B CA  1 
ATOM   2407 C C   . ARG   B 1 72  ? -12.999 -7.796  -34.937 1.00 34.77 ?  72  ARG   B C   1 
ATOM   2408 O O   . ARG   B 1 72  ? -13.708 -8.801  -34.881 1.00 32.87 ?  72  ARG   B O   1 
ATOM   2409 C CB  . ARG   B 1 72  ? -11.159 -7.065  -33.331 1.00 37.67 ?  72  ARG   B CB  1 
ATOM   2410 C CG  . ARG   B 1 72  ? -10.689 -5.848  -32.540 1.00 45.00 ?  72  ARG   B CG  1 
ATOM   2411 C CD  . ARG   B 1 72  ? -9.260  -5.985  -32.054 1.00 44.50 ?  72  ARG   B CD  1 
ATOM   2412 N NE  . ARG   B 1 72  ? -9.025  -7.254  -31.376 1.00 49.43 ?  72  ARG   B NE  1 
ATOM   2413 C CZ  . ARG   B 1 72  ? -8.421  -7.372  -30.196 1.00 58.85 ?  72  ARG   B CZ  1 
ATOM   2414 N NH1 . ARG   B 1 72  ? -8.006  -6.285  -29.552 1.00 54.94 ?  72  ARG   B NH1 1 
ATOM   2415 N NH2 . ARG   B 1 72  ? -8.243  -8.576  -29.658 1.00 63.71 ?  72  ARG   B NH2 1 
ATOM   2416 N N   . GLY   B 1 73  ? -12.546 -7.298  -36.094 1.00 34.13 ?  73  GLY   B N   1 
ATOM   2417 C CA  . GLY   B 1 73  ? -12.748 -7.958  -37.365 1.00 34.14 ?  73  GLY   B CA  1 
ATOM   2418 C C   . GLY   B 1 73  ? -11.488 -8.664  -37.851 1.00 41.41 ?  73  GLY   B C   1 
ATOM   2419 O O   . GLY   B 1 73  ? -10.495 -8.802  -37.139 1.00 36.71 ?  73  GLY   B O   1 
ATOM   2420 N N   . TRP   B 1 74  ? -11.550 -9.126  -39.099 1.00 43.18 ?  74  TRP   B N   1 
ATOM   2421 C CA  . TRP   B 1 74  ? -10.451 -9.821  -39.760 1.00 37.66 ?  74  TRP   B CA  1 
ATOM   2422 C C   . TRP   B 1 74  ? -10.575 -9.540  -41.248 1.00 39.16 ?  74  TRP   B C   1 
ATOM   2423 O O   . TRP   B 1 74  ? -11.637 -9.787  -41.828 1.00 39.63 ?  74  TRP   B O   1 
ATOM   2424 C CB  . TRP   B 1 74  ? -10.502 -11.338 -39.509 1.00 33.52 ?  74  TRP   B CB  1 
ATOM   2425 C CG  . TRP   B 1 74  ? -9.309  -12.113 -40.046 1.00 34.08 ?  74  TRP   B CG  1 
ATOM   2426 C CD1 . TRP   B 1 74  ? -9.271  -12.899 -41.172 1.00 36.64 ?  74  TRP   B CD1 1 
ATOM   2427 C CD2 . TRP   B 1 74  ? -7.988  -12.170 -39.478 1.00 34.91 ?  74  TRP   B CD2 1 
ATOM   2428 N NE1 . TRP   B 1 74  ? -8.015  -13.445 -41.329 1.00 29.90 ?  74  TRP   B NE1 1 
ATOM   2429 C CE2 . TRP   B 1 74  ? -7.211  -13.017 -40.305 1.00 34.21 ?  74  TRP   B CE2 1 
ATOM   2430 C CE3 . TRP   B 1 74  ? -7.392  -11.595 -38.348 1.00 34.06 ?  74  TRP   B CE3 1 
ATOM   2431 C CZ2 . TRP   B 1 74  ? -5.863  -13.296 -40.039 1.00 34.99 ?  74  TRP   B CZ2 1 
ATOM   2432 C CZ3 . TRP   B 1 74  ? -6.065  -11.884 -38.075 1.00 32.95 ?  74  TRP   B CZ3 1 
ATOM   2433 C CH2 . TRP   B 1 74  ? -5.310  -12.725 -38.924 1.00 33.37 ?  74  TRP   B CH2 1 
ATOM   2434 N N   . ALA   B 1 75  ? -9.506  -9.040  -41.860 1.00 33.14 ?  75  ALA   B N   1 
ATOM   2435 C CA  . ALA   B 1 75  ? -9.549  -8.672  -43.265 1.00 39.22 ?  75  ALA   B CA  1 
ATOM   2436 C C   . ALA   B 1 75  ? -8.822  -9.707  -44.114 1.00 34.69 ?  75  ALA   B C   1 
ATOM   2437 O O   . ALA   B 1 75  ? -7.905  -10.397 -43.654 1.00 37.34 ?  75  ALA   B O   1 
ATOM   2438 C CB  . ALA   B 1 75  ? -8.939  -7.280  -43.500 1.00 30.16 ?  75  ALA   B CB  1 
ATOM   2439 N N   . ALA   B 1 76  ? -9.245  -9.794  -45.370 1.00 33.22 ?  76  ALA   B N   1 
ATOM   2440 C CA  . ALA   B 1 76  ? -8.675  -10.711 -46.340 1.00 41.02 ?  76  ALA   B CA  1 
ATOM   2441 C C   . ALA   B 1 76  ? -8.917  -10.152 -47.734 1.00 45.29 ?  76  ALA   B C   1 
ATOM   2442 O O   . ALA   B 1 76  ? -9.843  -9.369  -47.956 1.00 41.65 ?  76  ALA   B O   1 
ATOM   2443 C CB  . ALA   B 1 76  ? -9.300  -12.106 -46.214 1.00 33.16 ?  76  ALA   B CB  1 
ATOM   2444 N N   . THR   B 1 77  ? -8.084  -10.589 -48.673 1.00 41.50 ?  77  THR   B N   1 
ATOM   2445 C CA  . THR   B 1 77  ? -8.340  -10.472 -50.098 1.00 45.99 ?  77  THR   B CA  1 
ATOM   2446 C C   . THR   B 1 77  ? -8.432  -11.872 -50.696 1.00 46.89 ?  77  THR   B C   1 
ATOM   2447 O O   . THR   B 1 77  ? -7.906  -12.839 -50.133 1.00 46.99 ?  77  THR   B O   1 
ATOM   2448 C CB  . THR   B 1 77  ? -7.237  -9.671  -50.789 1.00 36.62 ?  77  THR   B CB  1 
ATOM   2449 O OG1 . THR   B 1 77  ? -5.997  -10.376 -50.656 1.00 46.68 ?  77  THR   B OG1 1 
ATOM   2450 C CG2 . THR   B 1 77  ? -7.091  -8.296  -50.123 1.00 51.24 ?  77  THR   B CG2 1 
ATOM   2451 N N   . ALA   B 1 78  ? -9.090  -11.972 -51.856 1.00 46.80 ?  78  ALA   B N   1 
ATOM   2452 C CA  . ALA   B 1 78  ? -9.400  -13.274 -52.449 1.00 44.97 ?  78  ALA   B CA  1 
ATOM   2453 C C   . ALA   B 1 78  ? -8.142  -14.090 -52.729 1.00 43.60 ?  78  ALA   B C   1 
ATOM   2454 O O   . ALA   B 1 78  ? -7.160  -13.574 -53.278 1.00 37.99 ?  78  ALA   B O   1 
ATOM   2455 C CB  . ALA   B 1 78  ? -10.190 -13.083 -53.739 1.00 43.91 ?  78  ALA   B CB  1 
ATOM   2456 N N   . ARG   B 1 79  ? -8.170  -15.368 -52.326 1.00 39.76 ?  79  ARG   B N   1 
ATOM   2457 C CA  . ARG   B 1 79  ? -7.147  -16.377 -52.616 1.00 40.92 ?  79  ARG   B CA  1 
ATOM   2458 C C   . ARG   B 1 79  ? -5.826  -16.111 -51.905 1.00 40.95 ?  79  ARG   B C   1 
ATOM   2459 O O   . ARG   B 1 79  ? -4.849  -16.832 -52.139 1.00 47.44 ?  79  ARG   B O   1 
ATOM   2460 C CB  . ARG   B 1 79  ? -6.895  -16.518 -54.130 1.00 40.47 ?  79  ARG   B CB  1 
ATOM   2461 C CG  . ARG   B 1 79  ? -8.115  -17.007 -54.914 1.00 46.31 ?  79  ARG   B CG  1 
ATOM   2462 C CD  . ARG   B 1 79  ? -7.995  -16.885 -56.453 1.00 47.17 ?  79  ARG   B CD  1 
ATOM   2463 N NE  . ARG   B 1 79  ? -7.189  -15.747 -56.906 1.00 53.42 ?  79  ARG   B NE  1 
ATOM   2464 C CZ  . ARG   B 1 79  ? -7.680  -14.564 -57.271 1.00 50.11 ?  79  ARG   B CZ  1 
ATOM   2465 N NH1 . ARG   B 1 79  ? -6.855  -13.590 -57.657 1.00 52.90 ?  79  ARG   B NH1 1 
ATOM   2466 N NH2 . ARG   B 1 79  ? -8.988  -14.346 -57.245 1.00 51.58 ?  79  ARG   B NH2 1 
ATOM   2467 N N   . ALA   B 1 80  ? -5.765  -15.118 -51.024 1.00 40.58 ?  80  ALA   B N   1 
ATOM   2468 C CA  . ALA   B 1 80  ? -4.511  -14.756 -50.373 1.00 38.55 ?  80  ALA   B CA  1 
ATOM   2469 C C   . ALA   B 1 80  ? -4.298  -15.494 -49.057 1.00 33.37 ?  80  ALA   B C   1 
ATOM   2470 O O   . ALA   B 1 80  ? -3.158  -15.619 -48.589 1.00 32.86 ?  80  ALA   B O   1 
ATOM   2471 C CB  . ALA   B 1 80  ? -4.482  -13.250 -50.122 1.00 37.75 ?  80  ALA   B CB  1 
ATOM   2472 N N   . GLN   B 1 81  ? -5.370  -15.984 -48.465 1.00 36.93 ?  81  GLN   B N   1 
ATOM   2473 C CA  . GLN   B 1 81  ? -5.352  -16.645 -47.180 1.00 37.49 ?  81  GLN   B CA  1 
ATOM   2474 C C   . GLN   B 1 81  ? -5.919  -18.048 -47.300 1.00 37.81 ?  81  GLN   B C   1 
ATOM   2475 O O   . GLN   B 1 81  ? -6.662  -18.363 -48.233 1.00 33.78 ?  81  GLN   B O   1 
ATOM   2476 C CB  . GLN   B 1 81  ? -6.202  -15.873 -46.179 1.00 37.65 ?  81  GLN   B CB  1 
ATOM   2477 C CG  . GLN   B 1 81  ? -5.598  -14.596 -45.714 1.00 32.72 ?  81  GLN   B CG  1 
ATOM   2478 C CD  . GLN   B 1 81  ? -6.456  -13.968 -44.655 1.00 40.07 ?  81  GLN   B CD  1 
ATOM   2479 O OE1 . GLN   B 1 81  ? -6.994  -14.661 -43.777 1.00 32.68 ?  81  GLN   B OE1 1 
ATOM   2480 N NE2 . GLN   B 1 81  ? -6.617  -12.658 -44.736 1.00 36.48 ?  81  GLN   B NE2 1 
ATOM   2481 N N   . ILE   B 1 82  ? -5.620  -18.875 -46.307 1.00 38.07 ?  82  ILE   B N   1 
ATOM   2482 C CA  . ILE   B 1 82  ? -6.439  -20.046 -46.052 1.00 29.72 ?  82  ILE   B CA  1 
ATOM   2483 C C   . ILE   B 1 82  ? -7.426  -19.658 -44.955 1.00 33.20 ?  82  ILE   B C   1 
ATOM   2484 O O   . ILE   B 1 82  ? -7.039  -19.413 -43.807 1.00 32.64 ?  82  ILE   B O   1 
ATOM   2485 C CB  . ILE   B 1 82  ? -5.583  -21.268 -45.705 1.00 38.17 ?  82  ILE   B CB  1 
ATOM   2486 C CG1 . ILE   B 1 82  ? -4.913  -21.765 -46.996 1.00 35.55 ?  82  ILE   B CG1 1 
ATOM   2487 C CG2 . ILE   B 1 82  ? -6.429  -22.342 -45.092 1.00 27.10 ?  82  ILE   B CG2 1 
ATOM   2488 C CD1 . ILE   B 1 82  ? -3.958  -22.897 -46.801 1.00 35.48 ?  82  ILE   B CD1 1 
ATOM   2489 N N   . ILE   B 1 83  ? -8.700  -19.558 -45.346 1.00 33.22 ?  83  ILE   B N   1 
ATOM   2490 C CA  . ILE   B 1 83  ? -9.808  -19.090 -44.523 1.00 32.40 ?  83  ILE   B CA  1 
ATOM   2491 C C   . ILE   B 1 83  ? -10.744 -20.273 -44.346 1.00 30.33 ?  83  ILE   B C   1 
ATOM   2492 O O   . ILE   B 1 83  ? -11.482 -20.624 -45.271 1.00 31.21 ?  83  ILE   B O   1 
ATOM   2493 C CB  . ILE   B 1 83  ? -10.571 -17.925 -45.185 1.00 29.23 ?  83  ILE   B CB  1 
ATOM   2494 C CG1 . ILE   B 1 83  ? -9.650  -16.789 -45.624 1.00 32.02 ?  83  ILE   B CG1 1 
ATOM   2495 C CG2 . ILE   B 1 83  ? -11.713 -17.426 -44.280 1.00 27.33 ?  83  ILE   B CG2 1 
ATOM   2496 C CD1 . ILE   B 1 83  ? -10.383 -15.747 -46.437 1.00 37.08 ?  83  ILE   B CD1 1 
ATOM   2497 N N   . LEU   B 1 84  ? -10.754 -20.886 -43.174 1.00 32.97 ?  84  LEU   B N   1 
ATOM   2498 C CA  . LEU   B 1 84  ? -11.655 -22.007 -42.982 1.00 32.23 ?  84  LEU   B CA  1 
ATOM   2499 C C   . LEU   B 1 84  ? -12.240 -21.970 -41.589 1.00 30.06 ?  84  LEU   B C   1 
ATOM   2500 O O   . LEU   B 1 84  ? -11.667 -21.370 -40.675 1.00 29.04 ?  84  LEU   B O   1 
ATOM   2501 C CB  . LEU   B 1 84  ? -10.959 -23.356 -43.222 1.00 38.38 ?  84  LEU   B CB  1 
ATOM   2502 C CG  . LEU   B 1 84  ? -9.789  -23.758 -42.330 1.00 33.04 ?  84  LEU   B CG  1 
ATOM   2503 C CD1 . LEU   B 1 84  ? -10.227 -24.445 -41.054 1.00 39.16 ?  84  LEU   B CD1 1 
ATOM   2504 C CD2 . LEU   B 1 84  ? -8.914  -24.692 -43.141 1.00 36.72 ?  84  LEU   B CD2 1 
ATOM   2505 N N   . SER   B 1 85  ? -13.401 -22.636 -41.452 1.00 27.52 ?  85  SER   B N   1 
ATOM   2506 C CA  . SER   B 1 85  ? -14.011 -22.971 -40.177 1.00 24.16 ?  85  SER   B CA  1 
ATOM   2507 C C   . SER   B 1 85  ? -14.350 -24.456 -40.151 1.00 27.45 ?  85  SER   B C   1 
ATOM   2508 O O   . SER   B 1 85  ? -14.631 -25.048 -41.188 1.00 26.54 ?  85  SER   B O   1 
ATOM   2509 C CB  . SER   B 1 85  ? -15.284 -22.171 -39.929 1.00 25.11 ?  85  SER   B CB  1 
ATOM   2510 O OG  . SER   B 1 85  ? -14.990 -20.782 -39.898 1.00 37.61 ?  85  SER   B OG  1 
ATOM   2511 N N   . VAL   B 1 86  ? -14.350 -25.056 -38.956 1.00 20.33 ?  86  VAL   B N   1 
ATOM   2512 C CA  . VAL   B 1 86  ? -14.791 -26.439 -38.802 1.00 24.18 ?  86  VAL   B CA  1 
ATOM   2513 C C   . VAL   B 1 86  ? -15.755 -26.517 -37.621 1.00 27.10 ?  86  VAL   B C   1 
ATOM   2514 O O   . VAL   B 1 86  ? -15.666 -25.735 -36.672 1.00 24.85 ?  86  VAL   B O   1 
ATOM   2515 C CB  . VAL   B 1 86  ? -13.594 -27.414 -38.612 1.00 28.34 ?  86  VAL   B CB  1 
ATOM   2516 C CG1 . VAL   B 1 86  ? -12.666 -27.377 -39.837 1.00 27.83 ?  86  VAL   B CG1 1 
ATOM   2517 C CG2 . VAL   B 1 86  ? -12.783 -27.070 -37.364 1.00 24.05 ?  86  VAL   B CG2 1 
ATOM   2518 N N   . GLY   B 1 87  ? -16.681 -27.469 -37.679 1.00 22.90 ?  87  GLY   B N   1 
ATOM   2519 C CA  . GLY   B 1 87  ? -17.579 -27.732 -36.574 1.00 23.45 ?  87  GLY   B CA  1 
ATOM   2520 C C   . GLY   B 1 87  ? -17.075 -28.870 -35.702 1.00 34.19 ?  87  GLY   B C   1 
ATOM   2521 O O   . GLY   B 1 87  ? -16.616 -29.893 -36.205 1.00 31.84 ?  87  GLY   B O   1 
ATOM   2522 N N   . VAL   B 1 88  ? -17.163 -28.668 -34.387 1.00 26.76 ?  88  VAL   B N   1 
ATOM   2523 C CA  . VAL   B 1 88  ? -16.751 -29.640 -33.383 1.00 29.88 ?  88  VAL   B CA  1 
ATOM   2524 C C   . VAL   B 1 88  ? -17.869 -29.752 -32.342 1.00 37.67 ?  88  VAL   B C   1 
ATOM   2525 O O   . VAL   B 1 88  ? -18.239 -28.755 -31.705 1.00 31.61 ?  88  VAL   B O   1 
ATOM   2526 C CB  . VAL   B 1 88  ? -15.422 -29.243 -32.712 1.00 31.03 ?  88  VAL   B CB  1 
ATOM   2527 C CG1 . VAL   B 1 88  ? -14.974 -30.329 -31.757 1.00 38.96 ?  88  VAL   B CG1 1 
ATOM   2528 C CG2 . VAL   B 1 88  ? -14.346 -28.961 -33.769 1.00 30.79 ?  88  VAL   B CG2 1 
ATOM   2529 N N   . ARG   B 1 89  ? -18.422 -30.953 -32.190 1.00 36.72 ?  89  ARG   B N   1 
ATOM   2530 C CA  . ARG   B 1 89  ? -19.341 -31.223 -31.087 1.00 41.73 ?  89  ARG   B CA  1 
ATOM   2531 C C   . ARG   B 1 89  ? -18.559 -31.281 -29.777 1.00 43.90 ?  89  ARG   B C   1 
ATOM   2532 O O   . ARG   B 1 89  ? -17.608 -32.063 -29.654 1.00 39.58 ?  89  ARG   B O   1 
ATOM   2533 C CB  . ARG   B 1 89  ? -20.091 -32.533 -31.333 1.00 45.02 ?  89  ARG   B CB  1 
ATOM   2534 C CG  . ARG   B 1 89  ? -20.928 -32.985 -30.153 1.00 46.34 ?  89  ARG   B CG  1 
ATOM   2535 C CD  . ARG   B 1 89  ? -21.798 -34.164 -30.546 1.00 50.16 ?  89  ARG   B CD  1 
ATOM   2536 N NE  . ARG   B 1 89  ? -22.884 -33.756 -31.433 1.00 58.74 ?  89  ARG   B NE  1 
ATOM   2537 C CZ  . ARG   B 1 89  ? -24.102 -33.415 -31.015 1.00 58.90 ?  89  ARG   B CZ  1 
ATOM   2538 N NH1 . ARG   B 1 89  ? -24.388 -33.427 -29.713 1.00 56.95 ?  89  ARG   B NH1 1 
ATOM   2539 N NH2 . ARG   B 1 89  ? -25.035 -33.064 -31.901 1.00 58.37 ?  89  ARG   B NH2 1 
ATOM   2540 N N   . VAL   B 1 90  ? -18.960 -30.467 -28.797 1.00 41.31 ?  90  VAL   B N   1 
ATOM   2541 C CA  . VAL   B 1 90  ? -18.152 -30.236 -27.602 1.00 42.56 ?  90  VAL   B CA  1 
ATOM   2542 C C   . VAL   B 1 90  ? -18.821 -30.684 -26.311 1.00 44.89 ?  90  VAL   B C   1 
ATOM   2543 O O   . VAL   B 1 90  ? -18.126 -30.785 -25.285 1.00 43.10 ?  90  VAL   B O   1 
ATOM   2544 C CB  . VAL   B 1 90  ? -17.728 -28.752 -27.472 1.00 46.11 ?  90  VAL   B CB  1 
ATOM   2545 C CG1 . VAL   B 1 90  ? -16.666 -28.399 -28.509 1.00 33.74 ?  90  VAL   B CG1 1 
ATOM   2546 C CG2 . VAL   B 1 90  ? -18.943 -27.813 -27.567 1.00 43.73 ?  90  VAL   B CG2 1 
ATOM   2547 N N   . VAL   B 1 91  ? -20.127 -30.974 -26.307 1.00 43.62 ?  91  VAL   B N   1 
ATOM   2548 C CA  . VAL   B 1 91  ? -20.829 -31.187 -25.034 1.00 49.51 ?  91  VAL   B CA  1 
ATOM   2549 C C   . VAL   B 1 91  ? -20.310 -32.380 -24.254 1.00 48.15 ?  91  VAL   B C   1 
ATOM   2550 O O   . VAL   B 1 91  ? -20.526 -32.460 -23.045 1.00 53.14 ?  91  VAL   B O   1 
ATOM   2551 C CB  . VAL   B 1 91  ? -22.345 -31.297 -25.275 1.00 48.44 ?  91  VAL   B CB  1 
ATOM   2552 C CG1 . VAL   B 1 91  ? -22.856 -29.983 -25.787 1.00 49.60 ?  91  VAL   B CG1 1 
ATOM   2553 C CG2 . VAL   B 1 91  ? -22.614 -32.369 -26.336 1.00 49.44 ?  91  VAL   B CG2 1 
ATOM   2554 N N   . ASP   B 1 92  ? -19.603 -33.292 -24.911 1.00 49.98 ?  92  ASP   B N   1 
ATOM   2555 C CA  . ASP   B 1 92  ? -18.986 -34.414 -24.228 1.00 40.91 ?  92  ASP   B CA  1 
ATOM   2556 C C   . ASP   B 1 92  ? -17.868 -33.996 -23.272 1.00 57.19 ?  92  ASP   B C   1 
ATOM   2557 O O   . ASP   B 1 92  ? -17.526 -34.774 -22.371 1.00 58.36 ?  92  ASP   B O   1 
ATOM   2558 C CB  . ASP   B 1 92  ? -18.486 -35.399 -25.303 1.00 56.63 ?  92  ASP   B CB  1 
ATOM   2559 C CG  . ASP   B 1 92  ? -17.419 -34.781 -26.230 1.00 61.56 ?  92  ASP   B CG  1 
ATOM   2560 O OD1 . ASP   B 1 92  ? -17.796 -33.894 -27.045 1.00 52.90 ?  92  ASP   B OD1 1 
ATOM   2561 O OD2 . ASP   B 1 92  ? -16.249 -35.254 -26.230 1.00 55.51 -1 92  ASP   B OD2 1 
ATOM   2562 N N   . VAL   B 1 93  ? -17.308 -32.796 -23.424 1.00 51.68 ?  93  VAL   B N   1 
ATOM   2563 C CA  . VAL   B 1 93  ? -16.142 -32.344 -22.650 1.00 50.35 ?  93  VAL   B CA  1 
ATOM   2564 C C   . VAL   B 1 93  ? -16.557 -31.307 -21.610 1.00 42.96 ?  93  VAL   B C   1 
ATOM   2565 O O   . VAL   B 1 93  ? -17.336 -30.396 -21.932 1.00 42.77 ?  93  VAL   B O   1 
ATOM   2566 C CB  . VAL   B 1 93  ? -15.061 -31.762 -23.576 1.00 47.37 ?  93  VAL   B CB  1 
ATOM   2567 C CG1 . VAL   B 1 93  ? -13.936 -31.125 -22.765 1.00 44.64 ?  93  VAL   B CG1 1 
ATOM   2568 C CG2 . VAL   B 1 93  ? -14.533 -32.841 -24.487 1.00 46.04 ?  93  VAL   B CG2 1 
ATOM   2569 N N   . PRO   B 1 94  ? -16.068 -31.399 -20.369 1.00 49.24 ?  94  PRO   B N   1 
ATOM   2570 C CA  . PRO   B 1 94  ? -16.474 -30.433 -19.337 1.00 44.19 ?  94  PRO   B CA  1 
ATOM   2571 C C   . PRO   B 1 94  ? -16.235 -28.994 -19.785 1.00 48.10 ?  94  PRO   B C   1 
ATOM   2572 O O   . PRO   B 1 94  ? -15.255 -28.687 -20.473 1.00 44.90 ?  94  PRO   B O   1 
ATOM   2573 C CB  . PRO   B 1 94  ? -15.599 -30.810 -18.136 1.00 49.73 ?  94  PRO   B CB  1 
ATOM   2574 C CG  . PRO   B 1 94  ? -15.242 -32.245 -18.361 1.00 55.10 ?  94  PRO   B CG  1 
ATOM   2575 C CD  . PRO   B 1 94  ? -15.178 -32.453 -19.837 1.00 48.57 ?  94  PRO   B CD  1 
ATOM   2576 N N   . VAL   B 1 95  ? -17.160 -28.108 -19.405 1.00 50.38 ?  95  VAL   B N   1 
ATOM   2577 C CA  . VAL   B 1 95  ? -17.146 -26.754 -19.953 1.00 42.26 ?  95  VAL   B CA  1 
ATOM   2578 C C   . VAL   B 1 95  ? -15.865 -26.021 -19.568 1.00 37.72 ?  95  VAL   B C   1 
ATOM   2579 O O   . VAL   B 1 95  ? -15.390 -25.167 -20.322 1.00 50.01 ?  95  VAL   B O   1 
ATOM   2580 C CB  . VAL   B 1 95  ? -18.415 -25.982 -19.525 1.00 46.34 ?  95  VAL   B CB  1 
ATOM   2581 C CG1 . VAL   B 1 95  ? -18.455 -25.778 -18.015 1.00 48.74 ?  95  VAL   B CG1 1 
ATOM   2582 C CG2 . VAL   B 1 95  ? -18.526 -24.647 -20.280 1.00 40.87 ?  95  VAL   B CG2 1 
ATOM   2583 N N   . GLN   B 1 96  ? -15.269 -26.360 -18.418 1.00 40.11 ?  96  GLN   B N   1 
ATOM   2584 C CA  . GLN   B 1 96  ? -13.986 -25.775 -18.017 1.00 47.30 ?  96  GLN   B CA  1 
ATOM   2585 C C   . GLN   B 1 96  ? -12.933 -25.900 -19.118 1.00 49.37 ?  96  GLN   B C   1 
ATOM   2586 O O   . GLN   B 1 96  ? -12.124 -24.989 -19.321 1.00 54.21 ?  96  GLN   B O   1 
ATOM   2587 C CB  . GLN   B 1 96  ? -13.473 -26.444 -16.733 1.00 49.86 ?  96  GLN   B CB  1 
ATOM   2588 C CG  . GLN   B 1 96  ? -13.730 -25.670 -15.449 1.00 48.08 ?  96  GLN   B CG  1 
ATOM   2589 N N   . ALA   B 1 97  ? -12.931 -27.016 -19.844 1.00 42.45 ?  97  ALA   B N   1 
ATOM   2590 C CA  . ALA   B 1 97  ? -11.886 -27.293 -20.816 1.00 40.55 ?  97  ALA   B CA  1 
ATOM   2591 C C   . ALA   B 1 97  ? -12.090 -26.593 -22.158 1.00 40.97 ?  97  ALA   B C   1 
ATOM   2592 O O   . ALA   B 1 97  ? -11.170 -26.605 -22.979 1.00 43.32 ?  97  ALA   B O   1 
ATOM   2593 C CB  . ALA   B 1 97  ? -11.770 -28.815 -21.033 1.00 37.72 ?  97  ALA   B CB  1 
ATOM   2594 N N   . TRP   B 1 98  ? -13.246 -25.973 -22.412 1.00 38.91 ?  98  TRP   B N   1 
ATOM   2595 C CA  . TRP   B 1 98  ? -13.530 -25.536 -23.775 1.00 40.90 ?  98  TRP   B CA  1 
ATOM   2596 C C   . TRP   B 1 98  ? -12.594 -24.423 -24.234 1.00 38.48 ?  98  TRP   B C   1 
ATOM   2597 O O   . TRP   B 1 98  ? -12.365 -24.268 -25.438 1.00 30.89 ?  98  TRP   B O   1 
ATOM   2598 C CB  . TRP   B 1 98  ? -14.969 -25.067 -23.899 1.00 36.40 ?  98  TRP   B CB  1 
ATOM   2599 C CG  . TRP   B 1 98  ? -15.985 -26.140 -23.746 1.00 39.73 ?  98  TRP   B CG  1 
ATOM   2600 C CD1 . TRP   B 1 98  ? -15.771 -27.476 -23.495 1.00 44.76 ?  98  TRP   B CD1 1 
ATOM   2601 C CD2 . TRP   B 1 98  ? -17.393 -25.968 -23.833 1.00 39.45 ?  98  TRP   B CD2 1 
ATOM   2602 N NE1 . TRP   B 1 98  ? -16.978 -28.144 -23.428 1.00 39.55 ?  98  TRP   B NE1 1 
ATOM   2603 C CE2 . TRP   B 1 98  ? -17.988 -27.234 -23.628 1.00 47.32 ?  98  TRP   B CE2 1 
ATOM   2604 C CE3 . TRP   B 1 98  ? -18.215 -24.861 -24.063 1.00 42.35 ?  98  TRP   B CE3 1 
ATOM   2605 C CZ2 . TRP   B 1 98  ? -19.367 -27.414 -23.642 1.00 42.38 ?  98  TRP   B CZ2 1 
ATOM   2606 C CZ3 . TRP   B 1 98  ? -19.565 -25.039 -24.084 1.00 42.75 ?  98  TRP   B CZ3 1 
ATOM   2607 C CH2 . TRP   B 1 98  ? -20.138 -26.310 -23.878 1.00 46.46 ?  98  TRP   B CH2 1 
ATOM   2608 N N   . GLY   B 1 99  ? -12.047 -23.648 -23.301 1.00 31.34 ?  99  GLY   B N   1 
ATOM   2609 C CA  . GLY   B 1 99  ? -11.077 -22.619 -23.657 1.00 41.68 ?  99  GLY   B CA  1 
ATOM   2610 C C   . GLY   B 1 99  ? -9.835  -23.170 -24.333 1.00 33.40 ?  99  GLY   B C   1 
ATOM   2611 O O   . GLY   B 1 99  ? -9.173  -22.452 -25.084 1.00 32.30 ?  99  GLY   B O   1 
ATOM   2612 N N   . TRP   B 1 100 ? -9.532  -24.443 -24.113 1.00 37.58 ?  100 TRP   B N   1 
ATOM   2613 C CA  . TRP   B 1 100 ? -8.354  -25.047 -24.707 1.00 38.84 ?  100 TRP   B CA  1 
ATOM   2614 C C   . TRP   B 1 100 ? -8.511  -25.332 -26.191 1.00 35.77 ?  100 TRP   B C   1 
ATOM   2615 O O   . TRP   B 1 100 ? -7.496  -25.609 -26.840 1.00 35.52 ?  100 TRP   B O   1 
ATOM   2616 C CB  . TRP   B 1 100 ? -7.994  -26.325 -23.952 1.00 34.65 ?  100 TRP   B CB  1 
ATOM   2617 C CG  . TRP   B 1 100 ? -7.141  -26.009 -22.799 1.00 46.14 ?  100 TRP   B CG  1 
ATOM   2618 C CD1 . TRP   B 1 100 ? -7.538  -25.749 -21.514 1.00 40.67 ?  100 TRP   B CD1 1 
ATOM   2619 C CD2 . TRP   B 1 100 ? -5.720  -25.837 -22.827 1.00 36.00 ?  100 TRP   B CD2 1 
ATOM   2620 N NE1 . TRP   B 1 100 ? -6.441  -25.452 -20.742 1.00 42.67 ?  100 TRP   B NE1 1 
ATOM   2621 C CE2 . TRP   B 1 100 ? -5.315  -25.503 -21.524 1.00 38.16 ?  100 TRP   B CE2 1 
ATOM   2622 C CE3 . TRP   B 1 100 ? -4.749  -25.961 -23.828 1.00 40.25 ?  100 TRP   B CE3 1 
ATOM   2623 C CZ2 . TRP   B 1 100 ? -3.982  -25.293 -21.193 1.00 41.17 ?  100 TRP   B CZ2 1 
ATOM   2624 C CZ3 . TRP   B 1 100 ? -3.424  -25.743 -23.499 1.00 36.56 ?  100 TRP   B CZ3 1 
ATOM   2625 C CH2 . TRP   B 1 100 ? -3.055  -25.408 -22.196 1.00 45.66 ?  100 TRP   B CH2 1 
ATOM   2626 N N   . LEU   B 1 101 ? -9.732  -25.240 -26.750 1.00 40.14 ?  101 LEU   B N   1 
ATOM   2627 C CA  . LEU   B 1 101 ? -9.904  -25.478 -28.183 1.00 38.45 ?  101 LEU   B CA  1 
ATOM   2628 C C   . LEU   B 1 101 ? -9.203  -24.429 -29.020 1.00 35.44 ?  101 LEU   B C   1 
ATOM   2629 O O   . LEU   B 1 101 ? -8.488  -24.772 -29.967 1.00 35.35 ?  101 LEU   B O   1 
ATOM   2630 C CB  . LEU   B 1 101 ? -11.372 -25.551 -28.598 1.00 45.01 ?  101 LEU   B CB  1 
ATOM   2631 C CG  . LEU   B 1 101 ? -11.928 -26.968 -28.706 1.00 32.72 ?  101 LEU   B CG  1 
ATOM   2632 C CD1 . LEU   B 1 101 ? -13.374 -26.971 -29.160 1.00 34.85 ?  101 LEU   B CD1 1 
ATOM   2633 C CD2 . LEU   B 1 101 ? -11.095 -27.760 -29.681 1.00 31.77 ?  101 LEU   B CD2 1 
ATOM   2634 N N   . SER   B 1 102 ? -9.432  -23.141 -28.730 1.00 30.72 ?  102 SER   B N   1 
ATOM   2635 C CA  . SER   B 1 102 ? -8.707  -22.091 -29.437 1.00 32.82 ?  102 SER   B CA  1 
ATOM   2636 C C   . SER   B 1 102 ? -7.203  -22.293 -29.332 1.00 31.66 ?  102 SER   B C   1 
ATOM   2637 O O   . SER   B 1 102 ? -6.489  -22.261 -30.341 1.00 33.95 ?  102 SER   B O   1 
ATOM   2638 C CB  . SER   B 1 102 ? -9.074  -20.720 -28.869 1.00 43.25 ?  102 SER   B CB  1 
ATOM   2639 O OG  . SER   B 1 102 ? -10.313 -20.296 -29.372 1.00 50.29 ?  102 SER   B OG  1 
ATOM   2640 N N   . LEU   B 1 103 ? -6.699  -22.449 -28.103 1.00 32.60 ?  103 LEU   B N   1 
ATOM   2641 C CA  . LEU   B 1 103 ? -5.276  -22.720 -27.913 1.00 27.40 ?  103 LEU   B CA  1 
ATOM   2642 C C   . LEU   B 1 103 ? -4.850  -23.912 -28.752 1.00 33.31 ?  103 LEU   B C   1 
ATOM   2643 O O   . LEU   B 1 103 ? -3.827  -23.867 -29.435 1.00 28.84 ?  103 LEU   B O   1 
ATOM   2644 C CB  . LEU   B 1 103 ? -4.962  -22.973 -26.438 1.00 22.62 ?  103 LEU   B CB  1 
ATOM   2645 C CG  . LEU   B 1 103 ? -5.494  -21.945 -25.438 1.00 34.54 ?  103 LEU   B CG  1 
ATOM   2646 C CD1 . LEU   B 1 103 ? -4.975  -22.207 -24.030 1.00 32.28 ?  103 LEU   B CD1 1 
ATOM   2647 C CD2 . LEU   B 1 103 ? -5.129  -20.568 -25.894 1.00 32.67 ?  103 LEU   B CD2 1 
ATOM   2648 N N   . ALA   B 1 104 ? -5.645  -24.986 -28.727 1.00 33.03 ?  104 ALA   B N   1 
ATOM   2649 C CA  . ALA   B 1 104 ? -5.309  -26.166 -29.512 1.00 27.63 ?  104 ALA   B CA  1 
ATOM   2650 C C   . ALA   B 1 104 ? -5.254  -25.840 -30.996 1.00 32.93 ?  104 ALA   B C   1 
ATOM   2651 O O   . ALA   B 1 104 ? -4.404  -26.369 -31.727 1.00 30.09 ?  104 ALA   B O   1 
ATOM   2652 C CB  . ALA   B 1 104 ? -6.319  -27.283 -29.247 1.00 27.27 ?  104 ALA   B CB  1 
ATOM   2653 N N   . ALA   B 1 105 ? -6.155  -24.970 -31.475 1.00 31.40 ?  105 ALA   B N   1 
ATOM   2654 C CA  . ALA   B 1 105 ? -6.131  -24.676 -32.904 1.00 27.61 ?  105 ALA   B CA  1 
ATOM   2655 C C   . ALA   B 1 105 ? -4.918  -23.831 -33.264 1.00 32.82 ?  105 ALA   B C   1 
ATOM   2656 O O   . ALA   B 1 105 ? -4.384  -23.952 -34.377 1.00 31.20 ?  105 ALA   B O   1 
ATOM   2657 C CB  . ALA   B 1 105 ? -7.423  -23.988 -33.338 1.00 33.12 ?  105 ALA   B CB  1 
ATOM   2658 N N   . GLY   B 1 106 ? -4.471  -22.973 -32.338 1.00 29.37 ?  106 GLY   B N   1 
ATOM   2659 C CA  . GLY   B 1 106 ? -3.273  -22.200 -32.598 1.00 29.22 ?  106 GLY   B CA  1 
ATOM   2660 C C   . GLY   B 1 106 ? -2.073  -23.104 -32.756 1.00 30.80 ?  106 GLY   B C   1 
ATOM   2661 O O   . GLY   B 1 106 ? -1.232  -22.885 -33.624 1.00 29.59 ?  106 GLY   B O   1 
ATOM   2662 N N   . LEU   B 1 107 ? -2.001  -24.157 -31.933 1.00 26.03 ?  107 LEU   B N   1 
ATOM   2663 C CA  . LEU   B 1 107 ? -0.932  -25.141 -32.062 1.00 31.86 ?  107 LEU   B CA  1 
ATOM   2664 C C   . LEU   B 1 107 ? -0.970  -25.816 -33.417 1.00 31.40 ?  107 LEU   B C   1 
ATOM   2665 O O   . LEU   B 1 107 ? 0.074   -25.986 -34.057 1.00 31.09 ?  107 LEU   B O   1 
ATOM   2666 C CB  . LEU   B 1 107 ? -1.047  -26.205 -30.971 1.00 35.93 ?  107 LEU   B CB  1 
ATOM   2667 C CG  . LEU   B 1 107 ? -0.224  -26.202 -29.698 1.00 34.34 ?  107 LEU   B CG  1 
ATOM   2668 C CD1 . LEU   B 1 107 ? -0.688  -27.385 -28.829 1.00 32.72 ?  107 LEU   B CD1 1 
ATOM   2669 C CD2 . LEU   B 1 107 ? 1.257   -26.316 -30.038 1.00 32.86 ?  107 LEU   B CD2 1 
ATOM   2670 N N   . ALA   B 1 108 ? -2.170  -26.221 -33.863 1.00 28.34 ?  108 ALA   B N   1 
ATOM   2671 C CA  . ALA   B 1 108 ? -2.313  -26.879 -35.164 1.00 28.79 ?  108 ALA   B CA  1 
ATOM   2672 C C   . ALA   B 1 108 ? -1.865  -25.978 -36.295 1.00 30.77 ?  108 ALA   B C   1 
ATOM   2673 O O   . ALA   B 1 108 ? -1.227  -26.444 -37.245 1.00 26.36 ?  108 ALA   B O   1 
ATOM   2674 C CB  . ALA   B 1 108 ? -3.760  -27.300 -35.413 1.00 32.48 ?  108 ALA   B CB  1 
ATOM   2675 N N   . VAL   B 1 109 ? -2.229  -24.690 -36.242 1.00 30.28 ?  109 VAL   B N   1 
ATOM   2676 C CA  . VAL   B 1 109 ? -1.798  -23.795 -37.315 1.00 29.75 ?  109 VAL   B CA  1 
ATOM   2677 C C   . VAL   B 1 109 ? -0.286  -23.638 -37.300 1.00 28.04 ?  109 VAL   B C   1 
ATOM   2678 O O   . VAL   B 1 109 ? 0.357   -23.633 -38.354 1.00 37.10 ?  109 VAL   B O   1 
ATOM   2679 C CB  . VAL   B 1 109 ? -2.483  -22.425 -37.226 1.00 28.49 ?  109 VAL   B CB  1 
ATOM   2680 C CG1 . VAL   B 1 109 ? -1.877  -21.517 -38.298 1.00 35.98 ?  109 VAL   B CG1 1 
ATOM   2681 C CG2 . VAL   B 1 109 ? -3.969  -22.550 -37.428 1.00 29.51 ?  109 VAL   B CG2 1 
ATOM   2682 N N   . LEU   B 1 110 ? 0.301   -23.517 -36.111 1.00 31.61 ?  110 LEU   B N   1 
ATOM   2683 C CA  . LEU   B 1 110 ? 1.750   -23.371 -36.019 1.00 40.22 ?  110 LEU   B CA  1 
ATOM   2684 C C   . LEU   B 1 110 ? 2.471   -24.634 -36.492 1.00 38.33 ?  110 LEU   B C   1 
ATOM   2685 O O   . LEU   B 1 110 ? 3.436   -24.552 -37.259 1.00 37.58 ?  110 LEU   B O   1 
ATOM   2686 C CB  . LEU   B 1 110 ? 2.145   -23.017 -34.587 1.00 30.21 ?  110 LEU   B CB  1 
ATOM   2687 C CG  . LEU   B 1 110 ? 3.650   -22.985 -34.349 1.00 35.37 ?  110 LEU   B CG  1 
ATOM   2688 C CD1 . LEU   B 1 110 ? 4.260   -21.843 -35.122 1.00 40.23 ?  110 LEU   B CD1 1 
ATOM   2689 C CD2 . LEU   B 1 110 ? 3.937   -22.850 -32.860 1.00 41.72 ?  110 LEU   B CD2 1 
ATOM   2690 N N   . ASP   B 1 111 ? 1.998   -25.811 -36.077 1.00 40.85 ?  111 ASP   B N   1 
ATOM   2691 C CA  . ASP   B 1 111 ? 2.668   -27.048 -36.467 1.00 30.37 ?  111 ASP   B CA  1 
ATOM   2692 C C   . ASP   B 1 111 ? 2.594   -27.281 -37.972 1.00 42.87 ?  111 ASP   B C   1 
ATOM   2693 O O   . ASP   B 1 111 ? 3.491   -27.907 -38.548 1.00 54.51 ?  111 ASP   B O   1 
ATOM   2694 C CB  . ASP   B 1 111 ? 2.061   -28.245 -35.726 1.00 31.65 ?  111 ASP   B CB  1 
ATOM   2695 C CG  . ASP   B 1 111 ? 2.512   -28.329 -34.261 1.00 55.48 ?  111 ASP   B CG  1 
ATOM   2696 O OD1 . ASP   B 1 111 ? 3.317   -27.469 -33.807 1.00 55.49 ?  111 ASP   B OD1 1 
ATOM   2697 O OD2 . ASP   B 1 111 ? 2.044   -29.257 -33.555 1.00 61.20 -1 111 ASP   B OD2 1 
ATOM   2698 N N   . SER   B 1 112 ? 1.553   -26.782 -38.634 1.00 39.89 ?  112 SER   B N   1 
ATOM   2699 C CA  . SER   B 1 112 ? 1.423   -27.080 -40.056 1.00 44.99 ?  112 SER   B CA  1 
ATOM   2700 C C   . SER   B 1 112 ? 2.350   -26.216 -40.908 1.00 49.60 ?  112 SER   B C   1 
ATOM   2701 O O   . SER   B 1 112 ? 2.821   -26.675 -41.956 1.00 50.70 ?  112 SER   B O   1 
ATOM   2702 C CB  . SER   B 1 112 ? -0.042  -26.927 -40.491 1.00 37.61 ?  112 SER   B CB  1 
ATOM   2703 O OG  . SER   B 1 112 ? -0.423  -25.567 -40.528 1.00 43.58 ?  112 SER   B OG  1 
ATOM   2704 N N   . VAL   B 1 113 ? 2.643   -24.983 -40.468 1.00 44.18 ?  113 VAL   B N   1 
ATOM   2705 C CA  . VAL   B 1 113 ? 3.529   -24.079 -41.199 1.00 46.40 ?  113 VAL   B CA  1 
ATOM   2706 C C   . VAL   B 1 113 ? 4.969   -24.108 -40.686 1.00 54.46 ?  113 VAL   B C   1 
ATOM   2707 O O   . VAL   B 1 113 ? 5.863   -23.561 -41.356 1.00 47.78 ?  113 VAL   B O   1 
ATOM   2708 C CB  . VAL   B 1 113 ? 3.001   -22.630 -41.147 1.00 44.79 ?  113 VAL   B CB  1 
ATOM   2709 C CG1 . VAL   B 1 113 ? 1.522   -22.593 -41.578 1.00 43.57 ?  113 VAL   B CG1 1 
ATOM   2710 C CG2 . VAL   B 1 113 ? 3.184   -22.060 -39.756 1.00 37.19 ?  113 VAL   B CG2 1 
ATOM   2711 N N   . ALA   B 1 114 ? 5.225   -24.717 -39.526 1.00 48.37 ?  114 ALA   B N   1 
ATOM   2712 C CA  . ALA   B 1 114 ? 6.581   -24.713 -38.979 1.00 52.83 ?  114 ALA   B CA  1 
ATOM   2713 C C   . ALA   B 1 114 ? 7.571   -25.404 -39.905 1.00 53.90 ?  114 ALA   B C   1 
ATOM   2714 O O   . ALA   B 1 114 ? 8.611   -24.799 -40.218 1.00 52.28 ?  114 ALA   B O   1 
ATOM   2715 C CB  . ALA   B 1 114 ? 6.588   -25.330 -37.574 1.00 48.68 ?  114 ALA   B CB  1 
ATOM   2716 N N   . PRO   B 1 115 ? 7.312   -26.619 -40.420 1.00 57.34 ?  115 PRO   B N   1 
ATOM   2717 C CA  . PRO   B 1 115 ? 8.270   -27.230 -41.348 1.00 53.43 ?  115 PRO   B CA  1 
ATOM   2718 C C   . PRO   B 1 115 ? 8.377   -26.514 -42.684 1.00 54.82 ?  115 PRO   B C   1 
ATOM   2719 O O   . PRO   B 1 115 ? 9.074   -27.006 -43.575 1.00 54.45 ?  115 PRO   B O   1 
ATOM   2720 C CB  . PRO   B 1 115 ? 7.718   -28.650 -41.545 1.00 64.51 ?  115 PRO   B CB  1 
ATOM   2721 C CG  . PRO   B 1 115 ? 6.719   -28.854 -40.443 1.00 62.83 ?  115 PRO   B CG  1 
ATOM   2722 C CD  . PRO   B 1 115 ? 6.163   -27.512 -40.171 1.00 54.65 ?  115 PRO   B CD  1 
ATOM   2723 N N   . LEU   B 1 116 ? 7.715   -25.364 -42.848 1.00 56.42 ?  116 LEU   B N   1 
ATOM   2724 C CA  . LEU   B 1 116 ? 7.628   -24.723 -44.153 1.00 46.25 ?  116 LEU   B CA  1 
ATOM   2725 C C   . LEU   B 1 116 ? 8.434   -23.446 -44.282 1.00 50.86 ?  116 LEU   B C   1 
ATOM   2726 O O   . LEU   B 1 116 ? 8.776   -23.068 -45.406 1.00 57.71 ?  116 LEU   B O   1 
ATOM   2727 C CB  . LEU   B 1 116 ? 6.167   -24.400 -44.494 1.00 49.18 ?  116 LEU   B CB  1 
ATOM   2728 C CG  . LEU   B 1 116 ? 5.356   -25.440 -45.264 1.00 48.04 ?  116 LEU   B CG  1 
ATOM   2729 C CD1 . LEU   B 1 116 ? 5.273   -26.751 -44.509 1.00 51.86 ?  116 LEU   B CD1 1 
ATOM   2730 C CD2 . LEU   B 1 116 ? 3.962   -24.882 -45.520 1.00 51.44 ?  116 LEU   B CD2 1 
ATOM   2731 N N   . ILE   B 1 117 ? 8.732   -22.769 -43.186 1.00 48.25 ?  117 ILE   B N   1 
ATOM   2732 C CA  . ILE   B 1 117 ? 9.326   -21.445 -43.227 1.00 53.72 ?  117 ILE   B CA  1 
ATOM   2733 C C   . ILE   B 1 117 ? 10.755  -21.523 -42.717 1.00 56.70 ?  117 ILE   B C   1 
ATOM   2734 O O   . ILE   B 1 117 ? 11.066  -22.272 -41.784 1.00 55.76 ?  117 ILE   B O   1 
ATOM   2735 C CB  . ILE   B 1 117 ? 8.503   -20.441 -42.396 1.00 60.39 ?  117 ILE   B CB  1 
ATOM   2736 C CG1 . ILE   B 1 117 ? 8.358   -20.941 -40.958 1.00 55.29 ?  117 ILE   B CG1 1 
ATOM   2737 C CG2 . ILE   B 1 117 ? 7.130   -20.216 -43.035 1.00 59.25 ?  117 ILE   B CG2 1 
ATOM   2738 C CD1 . ILE   B 1 117 ? 7.864   -19.880 -39.997 1.00 57.18 ?  117 ILE   B CD1 1 
ATOM   2739 N N   . ALA   B 1 118 ? 11.628  -20.721 -43.332 1.00 57.25 ?  118 ALA   B N   1 
ATOM   2740 C CA  . ALA   B 1 118 ? 13.052  -20.703 -43.013 1.00 61.31 ?  118 ALA   B CA  1 
ATOM   2741 C C   . ALA   B 1 118 ? 13.381  -19.794 -41.831 1.00 62.23 ?  118 ALA   B C   1 
ATOM   2742 O O   . ALA   B 1 118 ? 14.481  -19.243 -41.766 1.00 74.89 ?  118 ALA   B O   1 
ATOM   2743 C CB  . ALA   B 1 118 ? 13.856  -20.287 -44.247 1.00 72.21 ?  118 ALA   B CB  1 
ATOM   2744 N N   . VAL   B 1 119 ? 12.447  -19.620 -40.904 1.00 64.98 ?  119 VAL   B N   1 
ATOM   2745 C CA  . VAL   B 1 119 ? 12.646  -18.791 -39.721 1.00 58.80 ?  119 VAL   B CA  1 
ATOM   2746 C C   . VAL   B 1 119 ? 13.102  -19.698 -38.583 1.00 60.60 ?  119 VAL   B C   1 
ATOM   2747 O O   . VAL   B 1 119 ? 12.596  -20.827 -38.459 1.00 55.27 ?  119 VAL   B O   1 
ATOM   2748 C CB  . VAL   B 1 119 ? 11.352  -18.042 -39.351 1.00 59.85 ?  119 VAL   B CB  1 
ATOM   2749 C CG1 . VAL   B 1 119 ? 11.449  -17.392 -37.968 1.00 50.86 ?  119 VAL   B CG1 1 
ATOM   2750 C CG2 . VAL   B 1 119 ? 11.010  -17.020 -40.421 1.00 58.02 ?  119 VAL   B CG2 1 
ATOM   2751 N N   . PRO   B 1 120 ? 14.055  -19.272 -37.752 1.00 60.12 ?  120 PRO   B N   1 
ATOM   2752 C CA  . PRO   B 1 120 ? 14.407  -20.051 -36.556 1.00 59.12 ?  120 PRO   B CA  1 
ATOM   2753 C C   . PRO   B 1 120 ? 13.162  -20.434 -35.776 1.00 58.98 ?  120 PRO   B C   1 
ATOM   2754 O O   . PRO   B 1 120 ? 12.327  -19.568 -35.469 1.00 50.78 ?  120 PRO   B O   1 
ATOM   2755 C CB  . PRO   B 1 120 ? 15.289  -19.085 -35.752 1.00 57.31 ?  120 PRO   B CB  1 
ATOM   2756 C CG  . PRO   B 1 120 ? 15.899  -18.198 -36.778 1.00 63.41 ?  120 PRO   B CG  1 
ATOM   2757 C CD  . PRO   B 1 120 ? 14.916  -18.086 -37.922 1.00 56.34 ?  120 PRO   B CD  1 
ATOM   2758 N N   . PRO   B 1 121 ? 12.983  -21.725 -35.471 1.00 53.85 ?  121 PRO   B N   1 
ATOM   2759 C CA  . PRO   B 1 121 ? 11.776  -22.143 -34.728 1.00 61.01 ?  121 PRO   B CA  1 
ATOM   2760 C C   . PRO   B 1 121 ? 11.536  -21.369 -33.441 1.00 59.14 ?  121 PRO   B C   1 
ATOM   2761 O O   . PRO   B 1 121 ? 10.381  -21.021 -33.157 1.00 54.69 ?  121 PRO   B O   1 
ATOM   2762 C CB  . PRO   B 1 121 ? 12.020  -23.644 -34.472 1.00 52.86 ?  121 PRO   B CB  1 
ATOM   2763 C CG  . PRO   B 1 121 ? 13.432  -23.912 -34.901 1.00 53.29 ?  121 PRO   B CG  1 
ATOM   2764 C CD  . PRO   B 1 121 ? 13.753  -22.883 -35.942 1.00 56.54 ?  121 PRO   B CD  1 
ATOM   2765 N N   . ALA   B 1 122 ? 12.587  -21.043 -32.679 1.00 54.02 ?  122 ALA   B N   1 
ATOM   2766 C CA  . ALA   B 1 122 ? 12.407  -20.259 -31.459 1.00 51.72 ?  122 ALA   B CA  1 
ATOM   2767 C C   . ALA   B 1 122 ? 11.876  -18.848 -31.705 1.00 44.08 ?  122 ALA   B C   1 
ATOM   2768 O O   . ALA   B 1 122 ? 11.517  -18.172 -30.734 1.00 49.83 ?  122 ALA   B O   1 
ATOM   2769 C CB  . ALA   B 1 122 ? 13.723  -20.164 -30.683 1.00 46.62 ?  122 ALA   B CB  1 
ATOM   2770 N N   . GLU   B 1 123 ? 11.831  -18.380 -32.953 1.00 45.27 ?  123 GLU   B N   1 
ATOM   2771 C CA  . GLU   B 1 123 ? 11.344  -17.044 -33.280 1.00 49.17 ?  123 GLU   B CA  1 
ATOM   2772 C C   . GLU   B 1 123 ? 9.870   -17.043 -33.680 1.00 50.23 ?  123 GLU   B C   1 
ATOM   2773 O O   . GLU   B 1 123 ? 9.335   -16.007 -34.104 1.00 40.20 ?  123 GLU   B O   1 
ATOM   2774 C CB  . GLU   B 1 123 ? 12.205  -16.425 -34.390 1.00 45.51 ?  123 GLU   B CB  1 
ATOM   2775 C CG  . GLU   B 1 123 ? 13.489  -15.773 -33.867 1.00 50.83 ?  123 GLU   B CG  1 
ATOM   2776 C CD  . GLU   B 1 123 ? 14.395  -15.275 -34.981 1.00 65.93 ?  123 GLU   B CD  1 
ATOM   2777 O OE1 . GLU   B 1 123 ? 13.866  -14.793 -36.010 1.00 62.16 ?  123 GLU   B OE1 1 
ATOM   2778 O OE2 . GLU   B 1 123 ? 15.636  -15.338 -34.812 1.00 62.02 -1 123 GLU   B OE2 1 
ATOM   2779 N N   . THR   B 1 124 ? 9.211   -18.188 -33.553 1.00 49.26 ?  124 THR   B N   1 
ATOM   2780 C CA  . THR   B 1 124 ? 7.817   -18.364 -33.914 1.00 39.09 ?  124 THR   B CA  1 
ATOM   2781 C C   . THR   B 1 124 ? 7.105   -18.967 -32.719 1.00 39.70 ?  124 THR   B C   1 
ATOM   2782 O O   . THR   B 1 124 ? 7.727   -19.565 -31.840 1.00 39.73 ?  124 THR   B O   1 
ATOM   2783 C CB  . THR   B 1 124 ? 7.652   -19.308 -35.097 1.00 37.26 ?  124 THR   B CB  1 
ATOM   2784 O OG1 . THR   B 1 124 ? 8.149   -20.590 -34.712 1.00 46.12 ?  124 THR   B OG1 1 
ATOM   2785 C CG2 . THR   B 1 124 ? 8.412   -18.810 -36.310 1.00 36.98 ?  124 THR   B CG2 1 
ATOM   2786 N N   . GLY   B 1 125 ? 5.790   -18.846 -32.706 1.00 32.92 ?  125 GLY   B N   1 
ATOM   2787 C CA  . GLY   B 1 125 ? 5.062   -19.437 -31.609 1.00 31.95 ?  125 GLY   B CA  1 
ATOM   2788 C C   . GLY   B 1 125 ? 3.709   -18.780 -31.464 1.00 33.12 ?  125 GLY   B C   1 
ATOM   2789 O O   . GLY   B 1 125 ? 3.236   -18.093 -32.366 1.00 30.87 ?  125 GLY   B O   1 
ATOM   2790 N N   . LEU   B 1 126 ? 3.099   -19.030 -30.315 1.00 30.36 ?  126 LEU   B N   1 
ATOM   2791 C CA  . LEU   B 1 126 ? 1.724   -18.651 -30.071 1.00 30.65 ?  126 LEU   B CA  1 
ATOM   2792 C C   . LEU   B 1 126 ? 1.722   -17.458 -29.142 1.00 35.91 ?  126 LEU   B C   1 
ATOM   2793 O O   . LEU   B 1 126 ? 2.379   -17.490 -28.103 1.00 33.71 ?  126 LEU   B O   1 
ATOM   2794 C CB  . LEU   B 1 126 ? 0.937   -19.817 -29.472 1.00 28.31 ?  126 LEU   B CB  1 
ATOM   2795 C CG  . LEU   B 1 126 ? 0.985   -21.005 -30.434 1.00 35.01 ?  126 LEU   B CG  1 
ATOM   2796 C CD1 . LEU   B 1 126 ? 0.406   -22.243 -29.808 1.00 33.69 ?  126 LEU   B CD1 1 
ATOM   2797 C CD2 . LEU   B 1 126 ? 0.282   -20.655 -31.745 1.00 32.29 ?  126 LEU   B CD2 1 
ATOM   2798 N N   . LYS   B 1 127 ? 1.011   -16.405 -29.509 1.00 29.08 ?  127 LYS   B N   1 
ATOM   2799 C CA  . LYS   B 1 127 ? 0.716   -15.375 -28.532 1.00 38.05 ?  127 LYS   B CA  1 
ATOM   2800 C C   . LYS   B 1 127 ? -0.657  -15.668 -27.959 1.00 35.38 ?  127 LYS   B C   1 
ATOM   2801 O O   . LYS   B 1 127 ? -1.619  -15.864 -28.705 1.00 39.46 ?  127 LYS   B O   1 
ATOM   2802 C CB  . LYS   B 1 127 ? 0.772   -13.988 -29.142 1.00 36.24 ?  127 LYS   B CB  1 
ATOM   2803 C CG  . LYS   B 1 127 ? 0.634   -12.934 -28.129 1.00 50.36 ?  127 LYS   B CG  1 
ATOM   2804 C CD  . LYS   B 1 127 ? 1.008   -11.654 -28.828 1.00 42.02 ?  127 LYS   B CD  1 
ATOM   2805 C CE  . LYS   B 1 127 ? -0.004  -11.319 -29.854 1.00 48.91 ?  127 LYS   B CE  1 
ATOM   2806 N NZ  . LYS   B 1 127 ? -1.292  -11.004 -29.144 1.00 60.29 ?  127 LYS   B NZ  1 
ATOM   2807 N N   . TRP   B 1 128 ? -0.744  -15.642 -26.653 1.00 36.75 ?  128 TRP   B N   1 
ATOM   2808 C CA  . TRP   B 1 128 ? -1.975  -16.003 -25.996 1.00 37.40 ?  128 TRP   B CA  1 
ATOM   2809 C C   . TRP   B 1 128 ? -3.043  -14.956 -26.280 1.00 33.03 ?  128 TRP   B C   1 
ATOM   2810 O O   . TRP   B 1 128 ? -2.772  -13.750 -26.207 1.00 35.10 ?  128 TRP   B O   1 
ATOM   2811 C CB  . TRP   B 1 128 ? -1.744  -16.136 -24.496 1.00 36.57 ?  128 TRP   B CB  1 
ATOM   2812 C CG  . TRP   B 1 128 ? -2.963  -16.527 -23.724 1.00 32.61 ?  128 TRP   B CG  1 
ATOM   2813 C CD1 . TRP   B 1 128 ? -3.401  -17.800 -23.457 1.00 33.89 ?  128 TRP   B CD1 1 
ATOM   2814 C CD2 . TRP   B 1 128 ? -3.927  -15.640 -23.136 1.00 31.37 ?  128 TRP   B CD2 1 
ATOM   2815 N NE1 . TRP   B 1 128 ? -4.572  -17.750 -22.736 1.00 35.93 ?  128 TRP   B NE1 1 
ATOM   2816 C CE2 . TRP   B 1 128 ? -4.913  -16.442 -22.519 1.00 33.29 ?  128 TRP   B CE2 1 
ATOM   2817 C CE3 . TRP   B 1 128 ? -4.046  -14.245 -23.061 1.00 33.87 ?  128 TRP   B CE3 1 
ATOM   2818 C CZ2 . TRP   B 1 128 ? -6.004  -15.899 -21.837 1.00 31.30 ?  128 TRP   B CZ2 1 
ATOM   2819 C CZ3 . TRP   B 1 128 ? -5.123  -13.706 -22.370 1.00 38.51 ?  128 TRP   B CZ3 1 
ATOM   2820 C CH2 . TRP   B 1 128 ? -6.088  -14.538 -21.765 1.00 32.45 ?  128 TRP   B CH2 1 
ATOM   2821 N N   . PRO   B 1 129 ? -4.273  -15.380 -26.579 1.00 29.90 ?  129 PRO   B N   1 
ATOM   2822 C CA  . PRO   B 1 129 ? -4.624  -16.807 -26.596 1.00 46.44 ?  129 PRO   B CA  1 
ATOM   2823 C C   . PRO   B 1 129 ? -4.412  -17.509 -27.959 1.00 54.58 ?  129 PRO   B C   1 
ATOM   2824 O O   . PRO   B 1 129 ? -3.636  -18.482 -28.028 1.00 55.08 ?  129 PRO   B O   1 
ATOM   2825 C CB  . PRO   B 1 129 ? -6.100  -16.794 -26.193 1.00 40.47 ?  129 PRO   B CB  1 
ATOM   2826 C CG  . PRO   B 1 129 ? -6.624  -15.486 -26.709 1.00 35.54 ?  129 PRO   B CG  1 
ATOM   2827 C CD  . PRO   B 1 129 ? -5.443  -14.510 -26.754 1.00 36.11 ?  129 PRO   B CD  1 
ATOM   2828 N N   . ASN   B 1 130 ? -5.052  -17.019 -29.027 1.00 52.63 ?  130 ASN   B N   1 
ATOM   2829 C CA  . ASN   B 1 130 ? -4.977  -17.670 -30.342 1.00 59.72 ?  130 ASN   B CA  1 
ATOM   2830 C C   . ASN   B 1 130 ? -4.540  -16.653 -31.414 1.00 61.44 ?  130 ASN   B C   1 
ATOM   2831 O O   . ASN   B 1 130 ? -5.345  -16.151 -32.213 1.00 56.25 ?  130 ASN   B O   1 
ATOM   2832 C CB  . ASN   B 1 130 ? -6.314  -18.332 -30.675 1.00 41.19 ?  130 ASN   B CB  1 
ATOM   2833 N N   . ASP   B 1 131 ? -3.242  -16.345 -31.419 1.00 48.50 ?  131 ASP   B N   1 
ATOM   2834 C CA  . ASP   B 1 131 ? -2.602  -15.645 -32.522 1.00 42.88 ?  131 ASP   B CA  1 
ATOM   2835 C C   . ASP   B 1 131 ? -1.265  -16.325 -32.786 1.00 37.71 ?  131 ASP   B C   1 
ATOM   2836 O O   . ASP   B 1 131 ? -0.547  -16.658 -31.850 1.00 41.47 ?  131 ASP   B O   1 
ATOM   2837 C CB  . ASP   B 1 131 ? -2.385  -14.164 -32.220 1.00 44.49 ?  131 ASP   B CB  1 
ATOM   2838 N N   . VAL   B 1 132 ? -0.939  -16.547 -34.052 1.00 36.09 ?  132 VAL   B N   1 
ATOM   2839 C CA  . VAL   B 1 132 ? 0.316   -17.187 -34.432 1.00 26.37 ?  132 VAL   B CA  1 
ATOM   2840 C C   . VAL   B 1 132 ? 1.258   -16.116 -34.942 1.00 29.39 ?  132 VAL   B C   1 
ATOM   2841 O O   . VAL   B 1 132 ? 0.908   -15.354 -35.853 1.00 34.83 ?  132 VAL   B O   1 
ATOM   2842 C CB  . VAL   B 1 132 ? 0.091   -18.263 -35.504 1.00 36.21 ?  132 VAL   B CB  1 
ATOM   2843 C CG1 . VAL   B 1 132 ? 1.418   -18.740 -36.056 1.00 33.32 ?  132 VAL   B CG1 1 
ATOM   2844 C CG2 . VAL   B 1 132 ? -0.746  -19.405 -34.936 1.00 33.31 ?  132 VAL   B CG2 1 
ATOM   2845 N N   . LEU   B 1 133 ? 2.449   -16.054 -34.360 1.00 29.70 ?  133 LEU   B N   1 
ATOM   2846 C CA  . LEU   B 1 133 ? 3.437   -15.035 -34.685 1.00 34.22 ?  133 LEU   B CA  1 
ATOM   2847 C C   . LEU   B 1 133 ? 4.658   -15.684 -35.316 1.00 31.66 ?  133 LEU   B C   1 
ATOM   2848 O O   . LEU   B 1 133 ? 5.069   -16.776 -34.923 1.00 39.35 ?  133 LEU   B O   1 
ATOM   2849 C CB  . LEU   B 1 133 ? 3.875   -14.253 -33.434 1.00 32.64 ?  133 LEU   B CB  1 
ATOM   2850 C CG  . LEU   B 1 133 ? 2.785   -13.490 -32.692 1.00 32.87 ?  133 LEU   B CG  1 
ATOM   2851 C CD1 . LEU   B 1 133 ? 3.434   -12.538 -31.682 1.00 36.11 ?  133 LEU   B CD1 1 
ATOM   2852 C CD2 . LEU   B 1 133 ? 1.945   -12.722 -33.696 1.00 38.98 ?  133 LEU   B CD2 1 
ATOM   2853 N N   . ALA   B 1 134 ? 5.234   -15.004 -36.290 1.00 36.17 ?  134 ALA   B N   1 
ATOM   2854 C CA  . ALA   B 1 134 ? 6.508   -15.406 -36.865 1.00 37.63 ?  134 ALA   B CA  1 
ATOM   2855 C C   . ALA   B 1 134 ? 7.370   -14.157 -37.019 1.00 39.65 ?  134 ALA   B C   1 
ATOM   2856 O O   . ALA   B 1 134 ? 6.985   -13.225 -37.731 1.00 41.40 ?  134 ALA   B O   1 
ATOM   2857 C CB  . ALA   B 1 134 ? 6.274   -16.105 -38.198 1.00 34.47 ?  134 ALA   B CB  1 
ATOM   2858 N N   . ARG   B 1 135 ? 8.501   -14.116 -36.319 1.00 46.29 ?  135 ARG   B N   1 
ATOM   2859 C CA  . ARG   B 1 135 ? 9.337   -12.911 -36.232 1.00 46.66 ?  135 ARG   B CA  1 
ATOM   2860 C C   . ARG   B 1 135 ? 8.484   -11.659 -35.978 1.00 40.77 ?  135 ARG   B C   1 
ATOM   2861 O O   . ARG   B 1 135 ? 8.557   -10.655 -36.687 1.00 39.99 ?  135 ARG   B O   1 
ATOM   2862 C CB  . ARG   B 1 135 ? 10.206  -12.760 -37.487 1.00 39.96 ?  135 ARG   B CB  1 
ATOM   2863 N N   . GLY   B 1 136 ? 7.642   -11.728 -34.950 1.00 43.51 ?  136 GLY   B N   1 
ATOM   2864 C CA  . GLY   B 1 136 ? 6.870   -10.573 -34.516 1.00 42.78 ?  136 GLY   B CA  1 
ATOM   2865 C C   . GLY   B 1 136 ? 5.615   -10.257 -35.307 1.00 39.22 ?  136 GLY   B C   1 
ATOM   2866 O O   . GLY   B 1 136 ? 4.754   -9.526  -34.799 1.00 49.29 ?  136 GLY   B O   1 
ATOM   2867 N N   . GLY   B 1 137 ? 5.479   -10.768 -36.537 1.00 41.47 ?  137 GLY   B N   1 
ATOM   2868 C CA  . GLY   B 1 137 ? 4.307   -10.506 -37.353 1.00 44.33 ?  137 GLY   B CA  1 
ATOM   2869 C C   . GLY   B 1 137 ? 3.212   -11.551 -37.172 1.00 40.43 ?  137 GLY   B C   1 
ATOM   2870 O O   . GLY   B 1 137 ? 3.483   -12.722 -36.906 1.00 38.24 ?  137 GLY   B O   1 
ATOM   2871 N N   . LYS   B 1 138 ? 1.961   -11.115 -37.338 1.00 34.96 ?  138 LYS   B N   1 
ATOM   2872 C CA  . LYS   B 1 138 ? 0.814   -11.992 -37.099 1.00 41.96 ?  138 LYS   B CA  1 
ATOM   2873 C C   . LYS   B 1 138 ? 0.557   -12.810 -38.359 1.00 33.10 ?  138 LYS   B C   1 
ATOM   2874 O O   . LYS   B 1 138 ? 0.067   -12.296 -39.367 1.00 34.10 ?  138 LYS   B O   1 
ATOM   2875 C CB  . LYS   B 1 138 ? -0.421  -11.190 -36.678 1.00 39.93 ?  138 LYS   B CB  1 
ATOM   2876 C CG  . LYS   B 1 138 ? -1.718  -12.015 -36.653 1.00 38.31 ?  138 LYS   B CG  1 
ATOM   2877 C CD  . LYS   B 1 138 ? -2.665  -11.653 -35.485 0.89 51.06 ?  138 LYS   B CD  1 
ATOM   2878 C CE  . LYS   B 1 138 ? -3.739  -12.756 -35.281 0.53 42.97 ?  138 LYS   B CE  1 
ATOM   2879 N NZ  . LYS   B 1 138 ? -4.505  -12.731 -33.978 1.00 55.69 ?  138 LYS   B NZ  1 
ATOM   2880 N N   . LEU   B 1 139 ? 0.917   -14.081 -38.303 1.00 38.89 ?  139 LEU   B N   1 
ATOM   2881 C CA  . LEU   B 1 139 ? 0.815   -14.970 -39.453 1.00 37.35 ?  139 LEU   B CA  1 
ATOM   2882 C C   . LEU   B 1 139 ? -0.605  -15.499 -39.635 1.00 31.00 ?  139 LEU   B C   1 
ATOM   2883 O O   . LEU   B 1 139 ? -1.065  -15.658 -40.767 1.00 36.26 ?  139 LEU   B O   1 
ATOM   2884 C CB  . LEU   B 1 139 ? 1.822   -16.118 -39.278 1.00 35.02 ?  139 LEU   B CB  1 
ATOM   2885 C CG  . LEU   B 1 139 ? 1.937   -17.240 -40.306 1.00 36.11 ?  139 LEU   B CG  1 
ATOM   2886 C CD1 . LEU   B 1 139 ? 2.204   -16.728 -41.720 1.00 35.74 ?  139 LEU   B CD1 1 
ATOM   2887 C CD2 . LEU   B 1 139 ? 3.024   -18.240 -39.874 1.00 38.50 ?  139 LEU   B CD2 1 
ATOM   2888 N N   . ALA   B 1 140 ? -1.312  -15.758 -38.542 1.00 32.93 ?  140 ALA   B N   1 
ATOM   2889 C CA  . ALA   B 1 140 ? -2.675  -16.254 -38.610 1.00 40.96 ?  140 ALA   B CA  1 
ATOM   2890 C C   . ALA   B 1 140 ? -3.438  -15.830 -37.368 1.00 40.18 ?  140 ALA   B C   1 
ATOM   2891 O O   . ALA   B 1 140 ? -2.854  -15.545 -36.318 1.00 35.08 ?  140 ALA   B O   1 
ATOM   2892 C CB  . ALA   B 1 140 ? -2.724  -17.778 -38.733 1.00 28.94 ?  140 ALA   B CB  1 
ATOM   2893 N N   . GLY   B 1 141 ? -4.758  -15.815 -37.502 1.00 35.27 ?  141 GLY   B N   1 
ATOM   2894 C CA  . GLY   B 1 141 ? -5.644  -15.612 -36.374 1.00 33.43 ?  141 GLY   B CA  1 
ATOM   2895 C C   . GLY   B 1 141 ? -6.647  -16.736 -36.256 1.00 34.18 ?  141 GLY   B C   1 
ATOM   2896 O O   . GLY   B 1 141 ? -7.113  -17.278 -37.260 1.00 32.34 ?  141 GLY   B O   1 
ATOM   2897 N N   . ILE   B 1 142 ? -6.952  -17.097 -35.013 1.00 32.90 ?  142 ILE   B N   1 
ATOM   2898 C CA  . ILE   B 1 142 ? -7.867  -18.175 -34.677 1.00 29.92 ?  142 ILE   B CA  1 
ATOM   2899 C C   . ILE   B 1 142 ? -9.011  -17.625 -33.844 1.00 30.40 ?  142 ILE   B C   1 
ATOM   2900 O O   . ILE   B 1 142 ? -8.799  -16.774 -32.974 1.00 32.65 ?  142 ILE   B O   1 
ATOM   2901 C CB  . ILE   B 1 142 ? -7.123  -19.308 -33.937 1.00 37.13 ?  142 ILE   B CB  1 
ATOM   2902 C CG1 . ILE   B 1 142 ? -6.131  -20.004 -34.882 1.00 39.68 ?  142 ILE   B CG1 1 
ATOM   2903 C CG2 . ILE   B 1 142 ? -8.079  -20.249 -33.217 1.00 28.64 ?  142 ILE   B CG2 1 
ATOM   2904 C CD1 . ILE   B 1 142 ? -4.766  -19.403 -34.914 1.00 41.87 ?  142 ILE   B CD1 1 
ATOM   2905 N N   . LEU   B 1 143 ? -10.223 -18.116 -34.102 1.00 28.40 ?  143 LEU   B N   1 
ATOM   2906 C CA  . LEU   B 1 143 ? -11.407 -17.657 -33.376 1.00 34.99 ?  143 LEU   B CA  1 
ATOM   2907 C C   . LEU   B 1 143 ? -12.382 -18.809 -33.169 1.00 35.26 ?  143 LEU   B C   1 
ATOM   2908 O O   . LEU   B 1 143 ? -12.883 -19.384 -34.141 1.00 34.10 ?  143 LEU   B O   1 
ATOM   2909 C CB  . LEU   B 1 143 ? -12.101 -16.517 -34.128 1.00 32.38 ?  143 LEU   B CB  1 
ATOM   2910 C CG  . LEU   B 1 143 ? -13.453 -16.150 -33.521 1.00 33.63 ?  143 LEU   B CG  1 
ATOM   2911 C CD1 . LEU   B 1 143 ? -13.213 -15.614 -32.127 1.00 29.24 ?  143 LEU   B CD1 1 
ATOM   2912 C CD2 . LEU   B 1 143 ? -14.197 -15.141 -34.374 1.00 37.80 ?  143 LEU   B CD2 1 
ATOM   2913 N N   . ALA   B 1 144 ? -12.685 -19.123 -31.910 1.00 30.66 ?  144 ALA   B N   1 
ATOM   2914 C CA  . ALA   B 1 144 ? -13.655 -20.158 -31.597 1.00 37.13 ?  144 ALA   B CA  1 
ATOM   2915 C C   . ALA   B 1 144 ? -14.958 -19.498 -31.178 1.00 37.31 ?  144 ALA   B C   1 
ATOM   2916 O O   . ALA   B 1 144 ? -14.951 -18.501 -30.451 1.00 38.54 ?  144 ALA   B O   1 
ATOM   2917 C CB  . ALA   B 1 144 ? -13.151 -21.092 -30.491 1.00 37.14 ?  144 ALA   B CB  1 
ATOM   2918 N N   . GLU   B 1 145 ? -16.072 -20.035 -31.668 1.00 29.13 ?  145 GLU   B N   1 
ATOM   2919 C CA  . GLU   B 1 145 ? -17.388 -19.539 -31.294 1.00 38.05 ?  145 GLU   B CA  1 
ATOM   2920 C C   . GLU   B 1 145 ? -18.283 -20.711 -30.935 1.00 43.48 ?  145 GLU   B C   1 
ATOM   2921 O O   . GLU   B 1 145 ? -18.234 -21.766 -31.578 1.00 39.50 ?  145 GLU   B O   1 
ATOM   2922 C CB  . GLU   B 1 145 ? -18.009 -18.717 -32.417 1.00 30.29 ?  145 GLU   B CB  1 
ATOM   2923 C CG  . GLU   B 1 145 ? -17.226 -17.450 -32.713 1.00 45.93 ?  145 GLU   B CG  1 
ATOM   2924 C CD  . GLU   B 1 145 ? -17.950 -16.550 -33.688 1.00 42.14 ?  145 GLU   B CD  1 
ATOM   2925 O OE1 . GLU   B 1 145 ? -18.683 -15.651 -33.225 1.00 53.29 ?  145 GLU   B OE1 1 
ATOM   2926 O OE2 . GLU   B 1 145 ? -17.796 -16.752 -34.910 1.00 44.35 -1 145 GLU   B OE2 1 
ATOM   2927 N N   . VAL   B 1 146 ? -19.102 -20.514 -29.908 1.00 38.05 ?  146 VAL   B N   1 
ATOM   2928 C CA  . VAL   B 1 146 ? -19.829 -21.591 -29.254 1.00 37.83 ?  146 VAL   B CA  1 
ATOM   2929 C C   . VAL   B 1 146 ? -21.279 -21.534 -29.701 1.00 46.93 ?  146 VAL   B C   1 
ATOM   2930 O O   . VAL   B 1 146 ? -21.859 -20.450 -29.822 1.00 45.67 ?  146 VAL   B O   1 
ATOM   2931 C CB  . VAL   B 1 146 ? -19.702 -21.469 -27.723 1.00 36.08 ?  146 VAL   B CB  1 
ATOM   2932 C CG1 . VAL   B 1 146 ? -20.595 -22.461 -27.027 1.00 46.07 ?  146 VAL   B CG1 1 
ATOM   2933 C CG2 . VAL   B 1 146 ? -18.235 -21.654 -27.291 1.00 43.80 ?  146 VAL   B CG2 1 
ATOM   2934 N N   . ALA   B 1 147 ? -21.860 -22.706 -29.985 1.00 42.01 ?  147 ALA   B N   1 
ATOM   2935 C CA  . ALA   B 1 147 ? -23.290 -22.847 -30.300 1.00 35.50 ?  147 ALA   B CA  1 
ATOM   2936 C C   . ALA   B 1 147 ? -23.645 -24.295 -29.955 1.00 43.68 ?  147 ALA   B C   1 
ATOM   2937 O O   . ALA   B 1 147 ? -23.616 -25.181 -30.816 1.00 44.37 ?  147 ALA   B O   1 
ATOM   2938 C CB  . ALA   B 1 147 ? -23.603 -22.528 -31.761 1.00 35.32 ?  147 ALA   B CB  1 
ATOM   2939 N N   . GLN   B 1 148 ? -23.934 -24.524 -28.682 1.00 41.55 ?  148 GLN   B N   1 
ATOM   2940 C CA  . GLN   B 1 148 ? -24.023 -25.883 -28.180 1.00 37.86 ?  148 GLN   B CA  1 
ATOM   2941 C C   . GLN   B 1 148 ? -25.000 -26.685 -29.035 1.00 39.65 ?  148 GLN   B C   1 
ATOM   2942 O O   . GLN   B 1 148 ? -25.979 -26.127 -29.546 1.00 36.86 ?  148 GLN   B O   1 
ATOM   2943 C CB  . GLN   B 1 148 ? -24.449 -25.883 -26.712 1.00 42.50 ?  148 GLN   B CB  1 
ATOM   2944 C CG  . GLN   B 1 148 ? -23.482 -25.130 -25.834 1.00 45.06 ?  148 GLN   B CG  1 
ATOM   2945 C CD  . GLN   B 1 148 ? -23.682 -25.422 -24.369 1.00 48.47 ?  148 GLN   B CD  1 
ATOM   2946 O OE1 . GLN   B 1 148 ? -23.669 -26.590 -23.946 1.00 47.93 ?  148 GLN   B OE1 1 
ATOM   2947 N NE2 . GLN   B 1 148 ? -23.849 -24.367 -23.573 1.00 45.84 ?  148 GLN   B NE2 1 
ATOM   2948 N N   . PRO   B 1 149 ? -24.738 -27.973 -29.271 1.00 39.67 ?  149 PRO   B N   1 
ATOM   2949 C CA  . PRO   B 1 149 ? -23.613 -28.776 -28.788 1.00 40.98 ?  149 PRO   B CA  1 
ATOM   2950 C C   . PRO   B 1 149 ? -22.233 -28.536 -29.468 1.00 43.00 ?  149 PRO   B C   1 
ATOM   2951 O O   . PRO   B 1 149 ? -21.291 -29.309 -29.249 1.00 38.88 ?  149 PRO   B O   1 
ATOM   2952 C CB  . PRO   B 1 149 ? -24.093 -30.198 -29.058 1.00 45.25 ?  149 PRO   B CB  1 
ATOM   2953 C CG  . PRO   B 1 149 ? -24.964 -30.060 -30.265 1.00 37.82 ?  149 PRO   B CG  1 
ATOM   2954 C CD  . PRO   B 1 149 ? -25.660 -28.752 -30.117 1.00 35.16 ?  149 PRO   B CD  1 
ATOM   2955 N N   . PHE   B 1 150 ? -22.110 -27.463 -30.239 1.00 34.52 ?  150 PHE   B N   1 
ATOM   2956 C CA  . PHE   B 1 150 ? -20.969 -27.260 -31.112 1.00 38.78 ?  150 PHE   B CA  1 
ATOM   2957 C C   . PHE   B 1 150 ? -20.137 -26.058 -30.698 1.00 40.34 ?  150 PHE   B C   1 
ATOM   2958 O O   . PHE   B 1 150 ? -20.625 -25.106 -30.077 1.00 38.72 ?  150 PHE   B O   1 
ATOM   2959 C CB  . PHE   B 1 150 ? -21.414 -27.070 -32.566 1.00 38.67 ?  150 PHE   B CB  1 
ATOM   2960 C CG  . PHE   B 1 150 ? -22.282 -28.181 -33.076 1.00 40.54 ?  150 PHE   B CG  1 
ATOM   2961 C CD1 . PHE   B 1 150 ? -21.750 -29.432 -33.318 1.00 39.88 ?  150 PHE   B CD1 1 
ATOM   2962 C CD2 . PHE   B 1 150 ? -23.639 -27.974 -33.300 1.00 42.55 ?  150 PHE   B CD2 1 
ATOM   2963 C CE1 . PHE   B 1 150 ? -22.547 -30.468 -33.793 1.00 39.31 ?  150 PHE   B CE1 1 
ATOM   2964 C CE2 . PHE   B 1 150 ? -24.442 -29.001 -33.770 1.00 41.20 ?  150 PHE   B CE2 1 
ATOM   2965 C CZ  . PHE   B 1 150 ? -23.890 -30.249 -34.018 1.00 40.85 ?  150 PHE   B CZ  1 
ATOM   2966 N N   . VAL   B 1 151 ? -18.858 -26.144 -31.034 1.00 38.73 ?  151 VAL   B N   1 
ATOM   2967 C CA  . VAL   B 1 151 ? -17.997 -24.987 -31.217 1.00 33.80 ?  151 VAL   B CA  1 
ATOM   2968 C C   . VAL   B 1 151 ? -17.632 -24.946 -32.693 1.00 34.14 ?  151 VAL   B C   1 
ATOM   2969 O O   . VAL   B 1 151 ? -17.514 -25.994 -33.347 1.00 34.44 ?  151 VAL   B O   1 
ATOM   2970 C CB  . VAL   B 1 151 ? -16.742 -25.048 -30.325 1.00 42.20 ?  151 VAL   B CB  1 
ATOM   2971 C CG1 . VAL   B 1 151 ? -15.787 -23.953 -30.703 1.00 39.02 ?  151 VAL   B CG1 1 
ATOM   2972 C CG2 . VAL   B 1 151 ? -17.126 -24.925 -28.850 1.00 39.49 ?  151 VAL   B CG2 1 
ATOM   2973 N N   . VAL   B 1 152 ? -17.534 -23.744 -33.238 1.00 36.43 ?  152 VAL   B N   1 
ATOM   2974 C CA  . VAL   B 1 152 ? -17.021 -23.535 -34.581 1.00 35.73 ?  152 VAL   B CA  1 
ATOM   2975 C C   . VAL   B 1 152 ? -15.628 -22.940 -34.442 1.00 32.78 ?  152 VAL   B C   1 
ATOM   2976 O O   . VAL   B 1 152 ? -15.476 -21.854 -33.872 1.00 34.94 ?  152 VAL   B O   1 
ATOM   2977 C CB  . VAL   B 1 152 ? -17.934 -22.620 -35.409 1.00 35.57 ?  152 VAL   B CB  1 
ATOM   2978 C CG1 . VAL   B 1 152 ? -17.243 -22.260 -36.737 1.00 30.11 ?  152 VAL   B CG1 1 
ATOM   2979 C CG2 . VAL   B 1 152 ? -19.258 -23.308 -35.687 1.00 36.16 ?  152 VAL   B CG2 1 
ATOM   2980 N N   . LEU   B 1 153 ? -14.615 -23.650 -34.949 1.00 37.07 ?  153 LEU   B N   1 
ATOM   2981 C CA  . LEU   B 1 153 ? -13.236 -23.170 -34.946 1.00 28.28 ?  153 LEU   B CA  1 
ATOM   2982 C C   . LEU   B 1 153 ? -12.892 -22.561 -36.291 1.00 29.26 ?  153 LEU   B C   1 
ATOM   2983 O O   . LEU   B 1 153 ? -12.919 -23.258 -37.306 1.00 30.38 ?  153 LEU   B O   1 
ATOM   2984 C CB  . LEU   B 1 153 ? -12.222 -24.272 -34.647 1.00 26.25 ?  153 LEU   B CB  1 
ATOM   2985 C CG  . LEU   B 1 153 ? -11.682 -24.422 -33.243 1.00 42.02 ?  153 LEU   B CG  1 
ATOM   2986 C CD1 . LEU   B 1 153 ? -10.804 -23.202 -32.977 1.00 47.78 ?  153 LEU   B CD1 1 
ATOM   2987 C CD2 . LEU   B 1 153 ? -12.777 -24.501 -32.237 1.00 42.46 ?  153 LEU   B CD2 1 
ATOM   2988 N N   . GLY   B 1 154 ? -12.468 -21.301 -36.283 1.00 30.30 ?  154 GLY   B N   1 
ATOM   2989 C CA  . GLY   B 1 154 ? -12.119 -20.582 -37.504 1.00 27.10 ?  154 GLY   B CA  1 
ATOM   2990 C C   . GLY   B 1 154 ? -10.644 -20.220 -37.528 1.00 30.63 ?  154 GLY   B C   1 
ATOM   2991 O O   . GLY   B 1 154 ? -10.088 -19.766 -36.523 1.00 29.73 ?  154 GLY   B O   1 
ATOM   2992 N N   . VAL   B 1 155 ? -10.031 -20.405 -38.694 1.00 32.66 ?  155 VAL   B N   1 
ATOM   2993 C CA  . VAL   B 1 155 ? -8.629  -20.096 -38.929 1.00 33.64 ?  155 VAL   B CA  1 
ATOM   2994 C C   . VAL   B 1 155 ? -8.526  -19.166 -40.136 1.00 30.60 ?  155 VAL   B C   1 
ATOM   2995 O O   . VAL   B 1 155 ? -9.099  -19.439 -41.197 1.00 29.50 ?  155 VAL   B O   1 
ATOM   2996 C CB  . VAL   B 1 155 ? -7.795  -21.368 -39.170 1.00 26.68 ?  155 VAL   B CB  1 
ATOM   2997 C CG1 . VAL   B 1 155 ? -6.416  -20.995 -39.683 1.00 35.43 ?  155 VAL   B CG1 1 
ATOM   2998 C CG2 . VAL   B 1 155 ? -7.711  -22.201 -37.892 1.00 28.17 ?  155 VAL   B CG2 1 
ATOM   2999 N N   . GLY   B 1 156 ? -7.783  -18.087 -39.978 1.00 25.81 ?  156 GLY   B N   1 
ATOM   3000 C CA  . GLY   B 1 156 ? -7.380  -17.289 -41.118 1.00 31.83 ?  156 GLY   B CA  1 
ATOM   3001 C C   . GLY   B 1 156 ? -5.867  -17.238 -41.181 1.00 33.16 ?  156 GLY   B C   1 
ATOM   3002 O O   . GLY   B 1 156 ? -5.240  -16.610 -40.325 1.00 34.25 ?  156 GLY   B O   1 
ATOM   3003 N N   . LEU   B 1 157 ? -5.280  -17.918 -42.170 1.00 29.71 ?  157 LEU   B N   1 
ATOM   3004 C CA  . LEU   B 1 157 ? -3.842  -18.104 -42.308 1.00 28.17 ?  157 LEU   B CA  1 
ATOM   3005 C C   . LEU   B 1 157 ? -3.356  -17.290 -43.512 1.00 29.92 ?  157 LEU   B C   1 
ATOM   3006 O O   . LEU   B 1 157 ? -3.790  -17.536 -44.640 1.00 32.23 ?  157 LEU   B O   1 
ATOM   3007 C CB  . LEU   B 1 157 ? -3.525  -19.598 -42.487 1.00 26.19 ?  157 LEU   B CB  1 
ATOM   3008 C CG  . LEU   B 1 157 ? -2.065  -19.984 -42.791 1.00 27.66 ?  157 LEU   B CG  1 
ATOM   3009 C CD1 . LEU   B 1 157 ? -1.134  -19.453 -41.721 1.00 26.66 ?  157 LEU   B CD1 1 
ATOM   3010 C CD2 . LEU   B 1 157 ? -1.878  -21.512 -42.929 1.00 30.23 ?  157 LEU   B CD2 1 
ATOM   3011 N N   . ASN   B 1 158 ? -2.485  -16.303 -43.273 1.00 33.07 ?  158 ASN   B N   1 
ATOM   3012 C CA  . ASN   B 1 158 ? -1.971  -15.473 -44.369 1.00 33.92 ?  158 ASN   B CA  1 
ATOM   3013 C C   . ASN   B 1 158 ? -0.975  -16.281 -45.200 1.00 30.02 ?  158 ASN   B C   1 
ATOM   3014 O O   . ASN   B 1 158 ? 0.094   -16.654 -44.714 1.00 36.48 ?  158 ASN   B O   1 
ATOM   3015 C CB  . ASN   B 1 158 ? -1.320  -14.204 -43.829 1.00 29.63 ?  158 ASN   B CB  1 
ATOM   3016 C CG  . ASN   B 1 158 ? -2.295  -13.327 -43.028 1.00 38.22 ?  158 ASN   B CG  1 
ATOM   3017 O OD1 . ASN   B 1 158 ? -1.985  -12.880 -41.922 1.00 37.54 ?  158 ASN   B OD1 1 
ATOM   3018 N ND2 . ASN   B 1 158 ? -3.469  -13.079 -43.589 1.00 30.26 ?  158 ASN   B ND2 1 
ATOM   3019 N N   . VAL   B 1 159 ? -1.326  -16.593 -46.442 1.00 32.89 ?  159 VAL   B N   1 
ATOM   3020 C CA  . VAL   B 1 159 ? -0.459  -17.460 -47.237 1.00 36.45 ?  159 VAL   B CA  1 
ATOM   3021 C C   . VAL   B 1 159 ? 0.420   -16.595 -48.146 1.00 34.47 ?  159 VAL   B C   1 
ATOM   3022 O O   . VAL   B 1 159 ? 1.654   -16.673 -48.077 1.00 37.81 ?  159 VAL   B O   1 
ATOM   3023 C CB  . VAL   B 1 159 ? -1.294  -18.489 -48.025 1.00 38.43 ?  159 VAL   B CB  1 
ATOM   3024 C CG1 . VAL   B 1 159 ? -0.401  -19.358 -48.900 1.00 29.07 ?  159 VAL   B CG1 1 
ATOM   3025 C CG2 . VAL   B 1 159 ? -2.127  -19.360 -47.045 1.00 36.50 ?  159 VAL   B CG2 1 
ATOM   3026 N N   . THR   B 1 160 ? -0.207  -15.765 -48.996 1.00 30.62 ?  160 THR   B N   1 
ATOM   3027 C CA  . THR   B 1 160 ? 0.492   -14.737 -49.773 1.00 47.70 ?  160 THR   B CA  1 
ATOM   3028 C C   . THR   B 1 160 ? -0.046  -13.342 -49.478 1.00 41.42 ?  160 THR   B C   1 
ATOM   3029 O O   . THR   B 1 160 ? 0.186   -12.418 -50.267 1.00 50.80 ?  160 THR   B O   1 
ATOM   3030 C CB  . THR   B 1 160 ? 0.392   -14.963 -51.291 1.00 41.59 ?  160 THR   B CB  1 
ATOM   3031 O OG1 . THR   B 1 160 ? -0.973  -14.811 -51.696 1.00 39.04 ?  160 THR   B OG1 1 
ATOM   3032 C CG2 . THR   B 1 160 ? 0.938   -16.324 -51.721 1.00 34.05 ?  160 THR   B CG2 1 
ATOM   3033 N N   . GLN   B 1 161 ? -0.808  -13.191 -48.400 1.00 34.65 ?  161 GLN   B N   1 
ATOM   3034 C CA  . GLN   B 1 161 ? -1.417  -11.914 -48.064 1.00 41.14 ?  161 GLN   B CA  1 
ATOM   3035 C C   . GLN   B 1 161 ? -0.351  -10.862 -47.762 1.00 44.26 ?  161 GLN   B C   1 
ATOM   3036 O O   . GLN   B 1 161 ? 0.611   -11.123 -47.035 1.00 46.14 ?  161 GLN   B O   1 
ATOM   3037 C CB  . GLN   B 1 161 ? -2.347  -12.084 -46.863 1.00 33.20 ?  161 GLN   B CB  1 
ATOM   3038 C CG  . GLN   B 1 161 ? -3.202  -10.865 -46.598 1.00 39.13 ?  161 GLN   B CG  1 
ATOM   3039 C CD  . GLN   B 1 161 ? -4.480  -10.883 -47.396 1.00 39.20 ?  161 GLN   B CD  1 
ATOM   3040 O OE1 . GLN   B 1 161 ? -5.408  -11.619 -47.080 1.00 38.75 ?  161 GLN   B OE1 1 
ATOM   3041 N NE2 . GLN   B 1 161 ? -4.529  -10.088 -48.448 1.00 49.47 ?  161 GLN   B NE2 1 
ATOM   3042 N N   . ALA   B 1 162 ? -0.515  -9.693  -48.325 1.00 45.74 ?  162 ALA   B N   1 
ATOM   3043 C CA  . ALA   B 1 162 ? 0.419   -8.627  -47.992 1.00 46.29 ?  162 ALA   B CA  1 
ATOM   3044 C C   . ALA   B 1 162 ? -0.068  -7.841  -46.781 1.00 45.65 ?  162 ALA   B C   1 
ATOM   3045 O O   . ALA   B 1 162 ? -1.281  -7.730  -46.546 1.00 48.64 ?  162 ALA   B O   1 
ATOM   3046 C CB  . ALA   B 1 162 ? 0.590   -7.678  -49.177 1.00 46.87 ?  162 ALA   B CB  1 
ATOM   3047 N N   . PRO   B 1 163 ? 0.849   -7.296  -45.984 1.00 46.49 ?  163 PRO   B N   1 
ATOM   3048 C CA  . PRO   B 1 163 ? 0.418   -6.364  -44.933 1.00 47.59 ?  163 PRO   B CA  1 
ATOM   3049 C C   . PRO   B 1 163 ? -0.412  -5.206  -45.443 1.00 48.76 ?  163 PRO   B C   1 
ATOM   3050 O O   . PRO   B 1 163 ? -1.260  -4.711  -44.687 1.00 47.22 ?  163 PRO   B O   1 
ATOM   3051 C CB  . PRO   B 1 163 ? 1.739   -5.880  -44.321 1.00 45.80 ?  163 PRO   B CB  1 
ATOM   3052 C CG  . PRO   B 1 163 ? 2.710   -6.977  -44.595 1.00 51.25 ?  163 PRO   B CG  1 
ATOM   3053 C CD  . PRO   B 1 163 ? 2.272   -7.667  -45.861 1.00 47.85 ?  163 PRO   B CD  1 
ATOM   3054 N N   . GLU   B 1 164 ? -0.239  -4.771  -46.696 1.00 52.45 ?  164 GLU   B N   1 
ATOM   3055 C CA  . GLU   B 1 164 ? -0.901  -3.526  -47.065 1.00 51.07 ?  164 GLU   B CA  1 
ATOM   3056 C C   . GLU   B 1 164 ? -2.373  -3.767  -47.362 1.00 57.04 ?  164 GLU   B C   1 
ATOM   3057 O O   . GLU   B 1 164 ? -3.136  -2.805  -47.523 1.00 57.21 ?  164 GLU   B O   1 
ATOM   3058 C CB  . GLU   B 1 164 ? -0.262  -2.902  -48.309 1.00 54.32 ?  164 GLU   B CB  1 
ATOM   3059 C CG  . GLU   B 1 164 ? 1.224   -2.736  -48.118 1.00 62.85 ?  164 GLU   B CG  1 
ATOM   3060 C CD  . GLU   B 1 164 ? 1.858   -4.014  -48.614 1.00 66.91 ?  164 GLU   B CD  1 
ATOM   3061 O OE1 . GLU   B 1 164 ? 1.075   -4.774  -49.256 1.00 78.12 ?  164 GLU   B OE1 1 
ATOM   3062 O OE2 . GLU   B 1 164 ? 3.036   -4.311  -48.281 1.00 64.97 -1 164 GLU   B OE2 1 
ATOM   3063 N N   . GLU   B 1 165 ? -2.767  -5.039  -47.469 1.00 50.35 ?  165 GLU   B N   1 
ATOM   3064 C CA  . GLU   B 1 165 ? -4.128  -5.424  -47.789 1.00 43.62 ?  165 GLU   B CA  1 
ATOM   3065 C C   . GLU   B 1 165 ? -4.979  -5.708  -46.560 1.00 45.97 ?  165 GLU   B C   1 
ATOM   3066 O O   . GLU   B 1 165 ? -6.209  -5.736  -46.680 1.00 51.44 ?  165 GLU   B O   1 
ATOM   3067 C CB  . GLU   B 1 165 ? -4.101  -6.662  -48.688 1.00 45.68 ?  165 GLU   B CB  1 
ATOM   3068 C CG  . GLU   B 1 165 ? -2.997  -6.630  -49.738 1.00 52.35 ?  165 GLU   B CG  1 
ATOM   3069 C CD  . GLU   B 1 165 ? -2.756  -7.977  -50.387 1.00 52.61 ?  165 GLU   B CD  1 
ATOM   3070 O OE1 . GLU   B 1 165 ? -2.291  -8.893  -49.688 1.00 58.60 ?  165 GLU   B OE1 1 
ATOM   3071 O OE2 . GLU   B 1 165 ? -3.035  -8.135  -51.594 1.00 57.33 -1 165 GLU   B OE2 1 
ATOM   3072 N N   . VAL   B 1 166 ? -4.374  -5.925  -45.386 1.00 48.37 ?  166 VAL   B N   1 
ATOM   3073 C CA  . VAL   B 1 166 ? -5.135  -6.453  -44.251 1.00 43.69 ?  166 VAL   B CA  1 
ATOM   3074 C C   . VAL   B 1 166 ? -4.807  -5.769  -42.926 1.00 41.63 ?  166 VAL   B C   1 
ATOM   3075 O O   . VAL   B 1 166 ? -5.715  -5.426  -42.155 1.00 47.13 ?  166 VAL   B O   1 
ATOM   3076 C CB  . VAL   B 1 166 ? -4.936  -7.978  -44.126 1.00 34.24 ?  166 VAL   B CB  1 
ATOM   3077 C CG1 . VAL   B 1 166 ? -5.631  -8.676  -45.265 1.00 35.12 ?  166 VAL   B CG1 1 
ATOM   3078 C CG2 . VAL   B 1 166 ? -3.459  -8.353  -44.060 1.00 31.38 ?  166 VAL   B CG2 1 
ATOM   3079 N N   . ASP   B 1 167 ? -3.522  -5.596  -42.638 1.00 40.36 ?  167 ASP   B N   1 
ATOM   3080 C CA  . ASP   B 1 167 ? -3.056  -5.062  -41.365 1.00 41.01 ?  167 ASP   B CA  1 
ATOM   3081 C C   . ASP   B 1 167 ? -1.547  -4.891  -41.400 1.00 49.79 ?  167 ASP   B C   1 
ATOM   3082 O O   . ASP   B 1 167 ? -0.844  -5.752  -41.944 1.00 50.30 ?  167 ASP   B O   1 
ATOM   3083 C CB  . ASP   B 1 167 ? -3.433  -5.975  -40.198 1.00 43.37 ?  167 ASP   B CB  1 
ATOM   3084 C CG  . ASP   B 1 167 ? -3.170  -5.328  -38.841 1.00 51.60 ?  167 ASP   B CG  1 
ATOM   3085 O OD1 . ASP   B 1 167 ? -2.063  -5.514  -38.256 1.00 51.71 ?  167 ASP   B OD1 1 
ATOM   3086 O OD2 . ASP   B 1 167 ? -4.082  -4.620  -38.365 1.00 50.49 -1 167 ASP   B OD2 1 
ATOM   3087 N N   . PRO   B 1 168 ? -1.009  -3.807  -40.830 1.00 51.11 ?  168 PRO   B N   1 
ATOM   3088 C CA  . PRO   B 1 168 ? 0.447   -3.597  -40.888 1.00 44.00 ?  168 PRO   B CA  1 
ATOM   3089 C C   . PRO   B 1 168 ? 1.227   -4.535  -39.983 1.00 51.14 ?  168 PRO   B C   1 
ATOM   3090 O O   . PRO   B 1 168 ? 2.425   -4.726  -40.213 1.00 48.92 ?  168 PRO   B O   1 
ATOM   3091 C CB  . PRO   B 1 168 ? 0.618   -2.132  -40.451 1.00 49.34 ?  168 PRO   B CB  1 
ATOM   3092 C CG  . PRO   B 1 168 ? -0.764  -1.539  -40.460 1.00 50.89 ?  168 PRO   B CG  1 
ATOM   3093 C CD  . PRO   B 1 168 ? -1.710  -2.668  -40.214 1.00 50.62 ?  168 PRO   B CD  1 
ATOM   3094 N N   . ASP   B 1 169 ? 0.594   -5.128  -38.968 1.00 55.98 ?  169 ASP   B N   1 
ATOM   3095 C CA  . ASP   B 1 169 ? 1.251   -6.121  -38.129 1.00 39.77 ?  169 ASP   B CA  1 
ATOM   3096 C C   . ASP   B 1 169 ? 1.287   -7.502  -38.776 1.00 47.04 ?  169 ASP   B C   1 
ATOM   3097 O O   . ASP   B 1 169 ? 1.864   -8.437  -38.199 1.00 40.54 ?  169 ASP   B O   1 
ATOM   3098 C CB  . ASP   B 1 169 ? 0.548   -6.197  -36.772 1.00 50.14 ?  169 ASP   B CB  1 
ATOM   3099 N N   . ALA   B 1 170 ? 0.702   -7.641  -39.963 1.00 40.74 ?  170 ALA   B N   1 
ATOM   3100 C CA  . ALA   B 1 170 ? 0.563   -8.935  -40.610 1.00 40.88 ?  170 ALA   B CA  1 
ATOM   3101 C C   . ALA   B 1 170 ? 1.862   -9.394  -41.255 1.00 47.20 ?  170 ALA   B C   1 
ATOM   3102 O O   . ALA   B 1 170 ? 2.683   -8.591  -41.708 1.00 42.10 ?  170 ALA   B O   1 
ATOM   3103 C CB  . ALA   B 1 170 ? -0.526  -8.880  -41.680 1.00 36.59 ?  170 ALA   B CB  1 
ATOM   3104 N N   . THR   B 1 171 ? 2.032   -10.711 -41.291 1.00 42.60 ?  171 THR   B N   1 
ATOM   3105 C CA  . THR   B 1 171 ? 3.015   -11.383 -42.122 1.00 40.11 ?  171 THR   B CA  1 
ATOM   3106 C C   . THR   B 1 171 ? 2.327   -12.547 -42.839 1.00 41.01 ?  171 THR   B C   1 
ATOM   3107 O O   . THR   B 1 171 ? 1.160   -12.864 -42.583 1.00 44.76 ?  171 THR   B O   1 
ATOM   3108 C CB  . THR   B 1 171 ? 4.213   -11.863 -41.288 1.00 43.32 ?  171 THR   B CB  1 
ATOM   3109 O OG1 . THR   B 1 171 ? 5.285   -12.242 -42.157 1.00 42.82 ?  171 THR   B OG1 1 
ATOM   3110 C CG2 . THR   B 1 171 ? 3.822   -13.052 -40.403 1.00 42.31 ?  171 THR   B CG2 1 
ATOM   3111 N N   . SER   B 1 172 ? 3.051   -13.181 -43.754 1.00 39.20 ?  172 SER   B N   1 
ATOM   3112 C CA  . SER   B 1 172 ? 2.509   -14.293 -44.516 1.00 34.47 ?  172 SER   B CA  1 
ATOM   3113 C C   . SER   B 1 172 ? 3.628   -15.287 -44.783 1.00 38.56 ?  172 SER   B C   1 
ATOM   3114 O O   . SER   B 1 172 ? 4.810   -14.997 -44.579 1.00 37.68 ?  172 SER   B O   1 
ATOM   3115 C CB  . SER   B 1 172 ? 1.841   -13.805 -45.809 1.00 43.55 ?  172 SER   B CB  1 
ATOM   3116 O OG  . SER   B 1 172 ? 2.786   -13.494 -46.817 1.00 48.91 ?  172 SER   B OG  1 
ATOM   3117 N N   . LEU   B 1 173 ? 3.233   -16.491 -45.199 1.00 34.86 ?  173 LEU   B N   1 
ATOM   3118 C CA  . LEU   B 1 173 ? 4.214   -17.512 -45.540 1.00 39.29 ?  173 LEU   B CA  1 
ATOM   3119 C C   . LEU   B 1 173 ? 5.151   -17.019 -46.634 1.00 43.70 ?  173 LEU   B C   1 
ATOM   3120 O O   . LEU   B 1 173 ? 6.367   -17.228 -46.557 1.00 53.45 ?  173 LEU   B O   1 
ATOM   3121 C CB  . LEU   B 1 173 ? 3.506   -18.799 -45.971 1.00 40.51 ?  173 LEU   B CB  1 
ATOM   3122 C CG  . LEU   B 1 173 ? 2.685   -19.531 -44.900 1.00 37.96 ?  173 LEU   B CG  1 
ATOM   3123 C CD1 . LEU   B 1 173 ? 2.258   -20.905 -45.371 1.00 39.16 ?  173 LEU   B CD1 1 
ATOM   3124 C CD2 . LEU   B 1 173 ? 3.493   -19.651 -43.626 1.00 39.55 ?  173 LEU   B CD2 1 
ATOM   3125 N N   . LEU   B 1 174 ? 4.601   -16.360 -47.659 1.00 40.66 ?  174 LEU   B N   1 
ATOM   3126 C CA  . LEU   B 1 174 ? 5.420   -15.756 -48.704 1.00 50.16 ?  174 LEU   B CA  1 
ATOM   3127 C C   . LEU   B 1 174 ? 6.495   -14.866 -48.093 1.00 53.40 ?  174 LEU   B C   1 
ATOM   3128 O O   . LEU   B 1 174 ? 7.698   -15.126 -48.227 1.00 52.90 ?  174 LEU   B O   1 
ATOM   3129 C CB  . LEU   B 1 174 ? 4.533   -14.951 -49.658 1.00 45.92 ?  174 LEU   B CB  1 
ATOM   3130 C CG  . LEU   B 1 174 ? 5.196   -14.364 -50.913 1.00 45.61 ?  174 LEU   B CG  1 
ATOM   3131 C CD1 . LEU   B 1 174 ? 5.934   -15.435 -51.711 1.00 44.41 ?  174 LEU   B CD1 1 
ATOM   3132 C CD2 . LEU   B 1 174 ? 4.171   -13.648 -51.785 1.00 37.42 ?  174 LEU   B CD2 1 
ATOM   3133 N N   . ASP   B 1 175 ? 6.062   -13.832 -47.367 1.00 53.54 ?  175 ASP   B N   1 
ATOM   3134 C CA  . ASP   B 1 175 ? 6.974   -12.898 -46.715 1.00 47.93 ?  175 ASP   B CA  1 
ATOM   3135 C C   . ASP   B 1 175 ? 7.956   -13.582 -45.766 1.00 56.44 ?  175 ASP   B C   1 
ATOM   3136 O O   . ASP   B 1 175 ? 9.041   -13.042 -45.523 1.00 63.12 ?  175 ASP   B O   1 
ATOM   3137 C CB  . ASP   B 1 175 ? 6.149   -11.834 -45.990 1.00 55.29 ?  175 ASP   B CB  1 
ATOM   3138 C CG  . ASP   B 1 175 ? 5.328   -10.981 -46.959 1.00 59.51 ?  175 ASP   B CG  1 
ATOM   3139 O OD1 . ASP   B 1 175 ? 5.961   -10.306 -47.801 1.00 62.75 ?  175 ASP   B OD1 1 
ATOM   3140 O OD2 . ASP   B 1 175 ? 4.067   -10.987 -46.889 1.00 54.95 -1 175 ASP   B OD2 1 
ATOM   3141 N N   . LEU   B 1 176 ? 7.631   -14.763 -45.242 1.00 49.59 ?  176 LEU   B N   1 
ATOM   3142 C CA  . LEU   B 1 176 ? 8.597   -15.535 -44.475 1.00 51.07 ?  176 LEU   B CA  1 
ATOM   3143 C C   . LEU   B 1 176 ? 9.399   -16.490 -45.341 1.00 55.86 ?  176 LEU   B C   1 
ATOM   3144 O O   . LEU   B 1 176 ? 9.950   -17.469 -44.821 1.00 61.83 ?  176 LEU   B O   1 
ATOM   3145 C CB  . LEU   B 1 176 ? 7.899   -16.320 -43.370 1.00 49.14 ?  176 LEU   B CB  1 
ATOM   3146 C CG  . LEU   B 1 176 ? 7.079   -15.453 -42.433 1.00 46.94 ?  176 LEU   B CG  1 
ATOM   3147 C CD1 . LEU   B 1 176 ? 6.300   -16.383 -41.567 1.00 45.95 ?  176 LEU   B CD1 1 
ATOM   3148 C CD2 . LEU   B 1 176 ? 7.990   -14.554 -41.608 1.00 49.01 ?  176 LEU   B CD2 1 
ATOM   3149 N N   . GLY   B 1 177 ? 9.469   -16.246 -46.645 1.00 58.09 ?  177 GLY   B N   1 
ATOM   3150 C CA  . GLY   B 1 177 ? 10.302  -17.072 -47.496 1.00 54.29 ?  177 GLY   B CA  1 
ATOM   3151 C C   . GLY   B 1 177 ? 9.707   -18.426 -47.832 1.00 62.44 ?  177 GLY   B C   1 
ATOM   3152 O O   . GLY   B 1 177 ? 10.384  -19.454 -47.731 1.00 61.60 ?  177 GLY   B O   1 
ATOM   3153 N N   . VAL   B 1 178 ? 8.432   -18.450 -48.204 1.00 55.35 ?  178 VAL   B N   1 
ATOM   3154 C CA  . VAL   B 1 178 ? 7.864   -19.568 -48.944 1.00 56.96 ?  178 VAL   B CA  1 
ATOM   3155 C C   . VAL   B 1 178 ? 7.616   -19.048 -50.353 1.00 51.31 ?  178 VAL   B C   1 
ATOM   3156 O O   . VAL   B 1 178 ? 6.720   -18.225 -50.574 1.00 54.83 ?  178 VAL   B O   1 
ATOM   3157 C CB  . VAL   B 1 178 ? 6.586   -20.115 -48.298 1.00 55.29 ?  178 VAL   B CB  1 
ATOM   3158 C CG1 . VAL   B 1 178 ? 6.059   -21.284 -49.114 1.00 47.04 ?  178 VAL   B CG1 1 
ATOM   3159 C CG2 . VAL   B 1 178 ? 6.856   -20.542 -46.851 1.00 51.69 ?  178 VAL   B CG2 1 
ATOM   3160 N N   . ALA   B 1 179 ? 8.424   -19.524 -51.303 1.00 58.05 ?  179 ALA   B N   1 
ATOM   3161 C CA  . ALA   B 1 179 ? 8.541   -18.868 -52.604 1.00 52.51 ?  179 ALA   B CA  1 
ATOM   3162 C C   . ALA   B 1 179 ? 7.231   -18.910 -53.378 1.00 54.17 ?  179 ALA   B C   1 
ATOM   3163 O O   . ALA   B 1 179 ? 6.774   -17.885 -53.896 1.00 51.74 ?  179 ALA   B O   1 
ATOM   3164 C CB  . ALA   B 1 179 ? 9.666   -19.517 -53.413 1.00 60.06 ?  179 ALA   B CB  1 
ATOM   3165 N N   . ALA   B 1 180 ? 6.614   -20.088 -53.477 1.00 57.37 ?  180 ALA   B N   1 
ATOM   3166 C CA  . ALA   B 1 180 ? 5.338   -20.252 -54.179 1.00 57.94 ?  180 ALA   B CA  1 
ATOM   3167 C C   . ALA   B 1 180 ? 4.460   -21.190 -53.367 1.00 57.62 ?  180 ALA   B C   1 
ATOM   3168 O O   . ALA   B 1 180 ? 4.298   -22.366 -53.705 1.00 52.59 ?  180 ALA   B O   1 
ATOM   3169 C CB  . ALA   B 1 180 ? 5.548   -20.780 -55.599 1.00 57.32 ?  180 ALA   B CB  1 
ATOM   3170 N N   . PRO   B 1 181 ? 3.866   -20.693 -52.287 1.00 49.84 ?  181 PRO   B N   1 
ATOM   3171 C CA  . PRO   B 1 181 ? 3.123   -21.571 -51.371 1.00 44.91 ?  181 PRO   B CA  1 
ATOM   3172 C C   . PRO   B 1 181 ? 1.967   -22.272 -52.070 1.00 47.11 ?  181 PRO   B C   1 
ATOM   3173 O O   . PRO   B 1 181 ? 1.267   -21.677 -52.889 1.00 43.07 ?  181 PRO   B O   1 
ATOM   3174 C CB  . PRO   B 1 181 ? 2.607   -20.606 -50.291 1.00 53.91 ?  181 PRO   B CB  1 
ATOM   3175 C CG  . PRO   B 1 181 ? 3.348   -19.317 -50.483 1.00 47.00 ?  181 PRO   B CG  1 
ATOM   3176 C CD  . PRO   B 1 181 ? 3.778   -19.272 -51.918 1.00 47.52 ?  181 PRO   B CD  1 
ATOM   3177 N N   . ASP   B 1 182 ? 1.748   -23.544 -51.719 1.00 48.51 ?  182 ASP   B N   1 
ATOM   3178 C CA  . ASP   B 1 182 ? 0.632   -24.320 -52.262 1.00 52.46 ?  182 ASP   B CA  1 
ATOM   3179 C C   . ASP   B 1 182 ? -0.491  -24.391 -51.229 1.00 44.03 ?  182 ASP   B C   1 
ATOM   3180 O O   . ASP   B 1 182 ? -0.389  -25.129 -50.238 1.00 43.82 ?  182 ASP   B O   1 
ATOM   3181 C CB  . ASP   B 1 182 ? 1.075   -25.724 -52.668 1.00 53.16 ?  182 ASP   B CB  1 
ATOM   3182 C CG  . ASP   B 1 182 ? -0.048  -26.528 -53.309 1.00 51.93 ?  182 ASP   B CG  1 
ATOM   3183 O OD1 . ASP   B 1 182 ? -1.139  -25.966 -53.549 1.00 52.16 ?  182 ASP   B OD1 1 
ATOM   3184 O OD2 . ASP   B 1 182 ? 0.160   -27.732 -53.569 1.00 63.59 -1 182 ASP   B OD2 1 
ATOM   3185 N N   . ARG   B 1 183 ? -1.581  -23.663 -51.492 1.00 40.04 ?  183 ARG   B N   1 
ATOM   3186 C CA  . ARG   B 1 183 ? -2.703  -23.633 -50.561 1.00 38.97 ?  183 ARG   B CA  1 
ATOM   3187 C C   . ARG   B 1 183 ? -3.399  -24.984 -50.453 1.00 40.74 ?  183 ARG   B C   1 
ATOM   3188 O O   . ARG   B 1 183 ? -3.903  -25.328 -49.379 1.00 41.87 ?  183 ARG   B O   1 
ATOM   3189 C CB  . ARG   B 1 183 ? -3.693  -22.540 -50.963 1.00 40.22 ?  183 ARG   B CB  1 
ATOM   3190 C CG  . ARG   B 1 183 ? -3.158  -21.122 -50.755 1.00 39.23 ?  183 ARG   B CG  1 
ATOM   3191 C CD  . ARG   B 1 183 ? -4.276  -20.109 -50.757 1.00 38.17 ?  183 ARG   B CD  1 
ATOM   3192 N NE  . ARG   B 1 183 ? -5.009  -20.180 -52.012 1.00 42.92 ?  183 ARG   B NE  1 
ATOM   3193 C CZ  . ARG   B 1 183 ? -6.330  -20.086 -52.099 1.00 40.77 ?  183 ARG   B CZ  1 
ATOM   3194 N NH1 . ARG   B 1 183 ? -7.060  -19.909 -51.004 1.00 46.65 ?  183 ARG   B NH1 1 
ATOM   3195 N NH2 . ARG   B 1 183 ? -6.925  -20.172 -53.280 1.00 45.08 ?  183 ARG   B NH2 1 
ATOM   3196 N N   . ASN   B 1 184 ? -3.419  -25.777 -51.522 1.00 40.40 ?  184 ASN   B N   1 
ATOM   3197 C CA  . ASN   B 1 184 ? -4.010  -27.109 -51.414 1.00 39.61 ?  184 ASN   B CA  1 
ATOM   3198 C C   . ASN   B 1 184 ? -3.229  -27.960 -50.428 1.00 37.65 ?  184 ASN   B C   1 
ATOM   3199 O O   . ASN   B 1 184 ? -3.810  -28.580 -49.528 1.00 34.00 ?  184 ASN   B O   1 
ATOM   3200 C CB  . ASN   B 1 184 ? -4.058  -27.788 -52.780 1.00 45.30 ?  184 ASN   B CB  1 
ATOM   3201 C CG  . ASN   B 1 184 ? -5.225  -27.316 -53.631 1.00 48.12 ?  184 ASN   B CG  1 
ATOM   3202 O OD1 . ASN   B 1 184 ? -6.368  -27.713 -53.426 1.00 55.82 ?  184 ASN   B OD1 1 
ATOM   3203 N ND2 . ASN   B 1 184 ? -4.930  -26.469 -54.602 1.00 58.93 ?  184 ASN   B ND2 1 
ATOM   3204 N N   . ARG   B 1 185 ? -1.900  -27.979 -50.574 1.00 35.80 ?  185 ARG   B N   1 
ATOM   3205 C CA  . ARG   B 1 185 ? -1.046  -28.748 -49.675 1.00 36.62 ?  185 ARG   B CA  1 
ATOM   3206 C C   . ARG   B 1 185 ? -1.082  -28.194 -48.259 1.00 31.62 ?  185 ARG   B C   1 
ATOM   3207 O O   . ARG   B 1 185 ? -1.031  -28.954 -47.286 1.00 35.06 ?  185 ARG   B O   1 
ATOM   3208 C CB  . ARG   B 1 185 ? 0.394   -28.762 -50.201 1.00 39.83 ?  185 ARG   B CB  1 
ATOM   3209 N N   . ILE   B 1 186 ? -1.171  -26.873 -48.116 1.00 34.34 ?  186 ILE   B N   1 
ATOM   3210 C CA  . ILE   B 1 186 ? -1.165  -26.287 -46.785 1.00 29.39 ?  186 ILE   B CA  1 
ATOM   3211 C C   . ILE   B 1 186 ? -2.505  -26.514 -46.102 1.00 30.00 ?  186 ILE   B C   1 
ATOM   3212 O O   . ILE   B 1 186 ? -2.566  -26.899 -44.926 1.00 32.40 ?  186 ILE   B O   1 
ATOM   3213 C CB  . ILE   B 1 186 ? -0.805  -24.795 -46.855 1.00 31.28 ?  186 ILE   B CB  1 
ATOM   3214 C CG1 . ILE   B 1 186 ? 0.648   -24.660 -47.288 1.00 38.57 ?  186 ILE   B CG1 1 
ATOM   3215 C CG2 . ILE   B 1 186 ? -0.982  -24.138 -45.509 1.00 33.13 ?  186 ILE   B CG2 1 
ATOM   3216 C CD1 . ILE   B 1 186 ? 1.018   -23.260 -47.741 1.00 44.58 ?  186 ILE   B CD1 1 
ATOM   3217 N N   . ALA   B 1 187 ? -3.598  -26.286 -46.826 1.00 29.95 ?  187 ALA   B N   1 
ATOM   3218 C CA  . ALA   B 1 187 ? -4.916  -26.540 -46.261 1.00 26.93 ?  187 ALA   B CA  1 
ATOM   3219 C C   . ALA   B 1 187 ? -5.033  -27.978 -45.758 1.00 32.32 ?  187 ALA   B C   1 
ATOM   3220 O O   . ALA   B 1 187 ? -5.493  -28.218 -44.644 1.00 31.02 ?  187 ALA   B O   1 
ATOM   3221 C CB  . ALA   B 1 187 ? -5.991  -26.244 -47.308 1.00 30.39 ?  187 ALA   B CB  1 
ATOM   3222 N N   . SER   B 1 188 ? -4.616  -28.957 -46.566 1.00 30.14 ?  188 SER   B N   1 
ATOM   3223 C CA  . SER   B 1 188 ? -4.821  -30.338 -46.151 1.00 31.88 ?  188 SER   B CA  1 
ATOM   3224 C C   . SER   B 1 188 ? -3.962  -30.669 -44.935 1.00 35.58 ?  188 SER   B C   1 
ATOM   3225 O O   . SER   B 1 188 ? -4.405  -31.383 -44.025 1.00 36.61 ?  188 SER   B O   1 
ATOM   3226 C CB  . SER   B 1 188 ? -4.517  -31.292 -47.303 1.00 33.50 ?  188 SER   B CB  1 
ATOM   3227 O OG  . SER   B 1 188 ? -3.205  -31.061 -47.761 1.00 42.99 ?  188 SER   B OG  1 
ATOM   3228 N N   . ARG   B 1 189 ? -2.731  -30.157 -44.909 1.00 30.56 ?  189 ARG   B N   1 
ATOM   3229 C CA  . ARG   B 1 189 ? -1.881  -30.297 -43.740 1.00 32.69 ?  189 ARG   B CA  1 
ATOM   3230 C C   . ARG   B 1 189 ? -2.518  -29.656 -42.505 1.00 29.44 ?  189 ARG   B C   1 
ATOM   3231 O O   . ARG   B 1 189 ? -2.480  -30.221 -41.405 1.00 24.97 ?  189 ARG   B O   1 
ATOM   3232 C CB  . ARG   B 1 189 ? -0.517  -29.671 -44.043 1.00 37.80 ?  189 ARG   B CB  1 
ATOM   3233 C CG  . ARG   B 1 189 ? 0.388   -29.637 -42.860 1.00 44.91 ?  189 ARG   B CG  1 
ATOM   3234 C CD  . ARG   B 1 189 ? 1.857   -29.766 -43.266 1.00 54.03 ?  189 ARG   B CD  1 
ATOM   3235 N NE  . ARG   B 1 189 ? 2.720   -29.664 -42.090 1.00 53.37 ?  189 ARG   B NE  1 
ATOM   3236 C CZ  . ARG   B 1 189 ? 2.822   -30.600 -41.146 1.00 61.02 ?  189 ARG   B CZ  1 
ATOM   3237 N NH1 . ARG   B 1 189 ? 2.133   -31.735 -41.239 1.00 60.53 ?  189 ARG   B NH1 1 
ATOM   3238 N NH2 . ARG   B 1 189 ? 3.623   -30.405 -40.106 1.00 58.52 ?  189 ARG   B NH2 1 
ATOM   3239 N N   . LEU   B 1 190 ? -3.097  -28.467 -42.665 1.00 26.48 ?  190 LEU   B N   1 
ATOM   3240 C CA  . LEU   B 1 190 ? -3.713  -27.792 -41.530 1.00 27.71 ?  190 LEU   B CA  1 
ATOM   3241 C C   . LEU   B 1 190 ? -4.897  -28.599 -40.991 1.00 28.34 ?  190 LEU   B C   1 
ATOM   3242 O O   . LEU   B 1 190 ? -5.038  -28.790 -39.779 1.00 26.49 ?  190 LEU   B O   1 
ATOM   3243 C CB  . LEU   B 1 190 ? -4.147  -26.391 -41.949 1.00 27.77 ?  190 LEU   B CB  1 
ATOM   3244 C CG  . LEU   B 1 190 ? -4.997  -25.643 -40.919 1.00 29.28 ?  190 LEU   B CG  1 
ATOM   3245 C CD1 . LEU   B 1 190 ? -4.244  -25.447 -39.612 1.00 32.96 ?  190 LEU   B CD1 1 
ATOM   3246 C CD2 . LEU   B 1 190 ? -5.454  -24.300 -41.492 1.00 34.10 ?  190 LEU   B CD2 1 
ATOM   3247 N N   . LEU   B 1 191 ? -5.747  -29.098 -41.884 1.00 24.82 ?  191 LEU   B N   1 
ATOM   3248 C CA  . LEU   B 1 191 ? -6.905  -29.875 -41.448 1.00 26.82 ?  191 LEU   B CA  1 
ATOM   3249 C C   . LEU   B 1 191 ? -6.488  -31.173 -40.755 1.00 27.39 ?  191 LEU   B C   1 
ATOM   3250 O O   . LEU   B 1 191 ? -7.133  -31.607 -39.794 1.00 27.96 ?  191 LEU   B O   1 
ATOM   3251 C CB  . LEU   B 1 191 ? -7.803  -30.148 -42.647 1.00 23.85 ?  191 LEU   B CB  1 
ATOM   3252 C CG  . LEU   B 1 191 ? -8.613  -28.870 -42.972 1.00 29.60 ?  191 LEU   B CG  1 
ATOM   3253 C CD1 . LEU   B 1 191 ? -9.201  -28.942 -44.378 1.00 26.14 ?  191 LEU   B CD1 1 
ATOM   3254 C CD2 . LEU   B 1 191 ? -9.730  -28.692 -41.965 1.00 29.37 ?  191 LEU   B CD2 1 
ATOM   3255 N N   . ARG   B 1 192 ? -5.405  -31.798 -41.203 1.00 25.25 ?  192 ARG   B N   1 
ATOM   3256 C CA  A ARG   B 1 192 ? -4.923  -32.978 -40.493 0.42 35.01 ?  192 ARG   B CA  1 
ATOM   3257 C CA  B ARG   B 1 192 ? -4.911  -32.978 -40.493 0.58 34.75 ?  192 ARG   B CA  1 
ATOM   3258 C C   . ARG   B 1 192 ? -4.406  -32.607 -39.102 1.00 30.38 ?  192 ARG   B C   1 
ATOM   3259 O O   . ARG   B 1 192 ? -4.726  -33.286 -38.117 1.00 25.85 ?  192 ARG   B O   1 
ATOM   3260 C CB  A ARG   B 1 192 ? -3.857  -33.691 -41.329 0.42 32.14 ?  192 ARG   B CB  1 
ATOM   3261 C CB  B ARG   B 1 192 ? -3.812  -33.670 -41.304 0.58 32.21 ?  192 ARG   B CB  1 
ATOM   3262 C CG  A ARG   B 1 192 ? -4.445  -34.368 -42.582 0.42 36.27 ?  192 ARG   B CG  1 
ATOM   3263 C CG  B ARG   B 1 192 ? -4.347  -34.679 -42.324 0.58 36.69 ?  192 ARG   B CG  1 
ATOM   3264 C CD  A ARG   B 1 192 ? -3.406  -35.182 -43.370 0.42 36.27 ?  192 ARG   B CD  1 
ATOM   3265 C CD  B ARG   B 1 192 ? -3.217  -35.520 -42.938 0.58 35.27 ?  192 ARG   B CD  1 
ATOM   3266 N NE  A ARG   B 1 192 ? -4.016  -35.997 -44.423 0.42 36.83 ?  192 ARG   B NE  1 
ATOM   3267 N NE  B ARG   B 1 192 ? -2.141  -34.675 -43.450 0.58 35.48 ?  192 ARG   B NE  1 
ATOM   3268 C CZ  A ARG   B 1 192 ? -4.002  -35.686 -45.718 0.42 39.08 ?  192 ARG   B CZ  1 
ATOM   3269 C CZ  B ARG   B 1 192 ? -2.170  -34.056 -44.626 0.58 33.52 ?  192 ARG   B CZ  1 
ATOM   3270 N NH1 A ARG   B 1 192 ? -3.407  -34.573 -46.129 0.42 39.05 ?  192 ARG   B NH1 1 
ATOM   3271 N NH1 B ARG   B 1 192 ? -3.213  -34.196 -45.423 0.58 36.63 ?  192 ARG   B NH1 1 
ATOM   3272 N NH2 A ARG   B 1 192 ? -4.578  -36.488 -46.605 0.42 33.63 ?  192 ARG   B NH2 1 
ATOM   3273 N NH2 B ARG   B 1 192 ? -1.154  -33.297 -45.004 0.58 32.24 ?  192 ARG   B NH2 1 
ATOM   3274 N N   . GLU   B 1 193 ? -3.652  -31.506 -38.998 1.00 27.21 ?  193 GLU   B N   1 
ATOM   3275 C CA  . GLU   B 1 193 ? -3.141  -31.046 -37.704 1.00 30.10 ?  193 GLU   B CA  1 
ATOM   3276 C C   . GLU   B 1 193 ? -4.275  -30.644 -36.762 1.00 27.62 ?  193 GLU   B C   1 
ATOM   3277 O O   . GLU   B 1 193 ? -4.269  -30.995 -35.575 1.00 26.88 ?  193 GLU   B O   1 
ATOM   3278 C CB  . GLU   B 1 193 ? -2.199  -29.843 -37.882 1.00 31.63 ?  193 GLU   B CB  1 
ATOM   3279 C CG  . GLU   B 1 193 ? -0.883  -30.066 -38.559 1.00 43.23 ?  193 GLU   B CG  1 
ATOM   3280 C CD  . GLU   B 1 193 ? -0.106  -31.215 -37.958 1.00 48.72 ?  193 GLU   B CD  1 
ATOM   3281 O OE1 . GLU   B 1 193 ? 0.383   -31.095 -36.815 1.00 41.28 ?  193 GLU   B OE1 1 
ATOM   3282 O OE2 . GLU   B 1 193 ? 0.081   -32.217 -38.679 1.00 59.61 -1 193 GLU   B OE2 1 
ATOM   3283 N N   . LEU   B 1 194 ? -5.216  -29.835 -37.252 1.00 29.74 ?  194 LEU   B N   1 
ATOM   3284 C CA  . LEU   B 1 194 ? -6.396  -29.514 -36.452 1.00 32.21 ?  194 LEU   B CA  1 
ATOM   3285 C C   . LEU   B 1 194 ? -7.060  -30.789 -35.930 1.00 30.32 ?  194 LEU   B C   1 
ATOM   3286 O O   . LEU   B 1 194 ? -7.365  -30.901 -34.737 1.00 29.70 ?  194 LEU   B O   1 
ATOM   3287 C CB  . LEU   B 1 194 ? -7.393  -28.695 -37.270 1.00 27.01 ?  194 LEU   B CB  1 
ATOM   3288 C CG  . LEU   B 1 194 ? -7.281  -27.173 -37.407 1.00 36.65 ?  194 LEU   B CG  1 
ATOM   3289 C CD1 . LEU   B 1 194 ? -8.323  -26.667 -38.404 1.00 32.53 ?  194 LEU   B CD1 1 
ATOM   3290 C CD2 . LEU   B 1 194 ? -7.449  -26.483 -36.049 1.00 40.71 ?  194 LEU   B CD2 1 
ATOM   3291 N N   . GLU   B 1 195 ? -7.273  -31.777 -36.803 1.00 27.57 ?  195 GLU   B N   1 
ATOM   3292 C CA  . GLU   B 1 195 ? -7.884  -33.020 -36.322 1.00 31.20 ?  195 GLU   B CA  1 
ATOM   3293 C C   . GLU   B 1 195 ? -7.087  -33.610 -35.169 1.00 27.18 ?  195 GLU   B C   1 
ATOM   3294 O O   . GLU   B 1 195 ? -7.657  -33.986 -34.140 1.00 34.52 ?  195 GLU   B O   1 
ATOM   3295 C CB  . GLU   B 1 195 ? -8.014  -34.070 -37.432 1.00 31.39 ?  195 GLU   B CB  1 
ATOM   3296 C CG  . GLU   B 1 195 ? -8.453  -35.444 -36.825 1.00 35.96 ?  195 GLU   B CG  1 
ATOM   3297 C CD  . GLU   B 1 195 ? -8.761  -36.534 -37.865 1.00 34.86 ?  195 GLU   B CD  1 
ATOM   3298 O OE1 . GLU   B 1 195 ? -8.136  -36.555 -38.944 1.00 39.56 ?  195 GLU   B OE1 1 
ATOM   3299 O OE2 . GLU   B 1 195 ? -9.614  -37.394 -37.572 1.00 41.78 -1 195 GLU   B OE2 1 
ATOM   3300 N N   . ALA   B 1 196 ? -5.756  -33.665 -35.308 1.00 23.12 ?  196 ALA   B N   1 
ATOM   3301 C CA  . ALA   B 1 196 ? -4.934  -34.235 -34.247 1.00 28.39 ?  196 ALA   B CA  1 
ATOM   3302 C C   . ALA   B 1 196 ? -5.121  -33.473 -32.943 1.00 31.53 ?  196 ALA   B C   1 
ATOM   3303 O O   . ALA   B 1 196 ? -5.336  -34.076 -31.885 1.00 29.15 ?  196 ALA   B O   1 
ATOM   3304 C CB  . ALA   B 1 196 ? -3.461  -34.256 -34.659 1.00 25.60 ?  196 ALA   B CB  1 
ATOM   3305 N N   . ARG   B 1 197 ? -5.075  -32.137 -32.997 1.00 27.62 ?  197 ARG   B N   1 
ATOM   3306 C CA  . ARG   B 1 197 ? -5.147  -31.383 -31.748 1.00 29.70 ?  197 ARG   B CA  1 
ATOM   3307 C C   . ARG   B 1 197 ? -6.550  -31.454 -31.134 1.00 29.51 ?  197 ARG   B C   1 
ATOM   3308 O O   . ARG   B 1 197 ? -6.691  -31.499 -29.911 1.00 30.89 ?  197 ARG   B O   1 
ATOM   3309 C CB  . ARG   B 1 197 ? -4.711  -29.929 -31.966 1.00 28.42 ?  197 ARG   B CB  1 
ATOM   3310 C CG  . ARG   B 1 197 ? -3.284  -29.788 -32.441 1.00 29.08 ?  197 ARG   B CG  1 
ATOM   3311 C CD  . ARG   B 1 197 ? -2.367  -30.448 -31.444 1.00 28.12 ?  197 ARG   B CD  1 
ATOM   3312 N NE  . ARG   B 1 197 ? -0.965  -30.161 -31.710 1.00 36.92 ?  197 ARG   B NE  1 
ATOM   3313 C CZ  . ARG   B 1 197 ? 0.005   -30.332 -30.815 1.00 37.07 ?  197 ARG   B CZ  1 
ATOM   3314 N NH1 . ARG   B 1 197 ? -0.284  -30.800 -29.607 1.00 38.82 ?  197 ARG   B NH1 1 
ATOM   3315 N NH2 . ARG   B 1 197 ? 1.262   -30.034 -31.126 1.00 38.32 ?  197 ARG   B NH2 1 
ATOM   3316 N N   . ILE   B 1 198 ? -7.595  -31.450 -31.958 1.00 27.75 ?  198 ILE   B N   1 
ATOM   3317 C CA  . ILE   B 1 198 ? -8.947  -31.593 -31.429 1.00 28.40 ?  198 ILE   B CA  1 
ATOM   3318 C C   . ILE   B 1 198 ? -9.074  -32.904 -30.677 1.00 33.21 ?  198 ILE   B C   1 
ATOM   3319 O O   . ILE   B 1 198 ? -9.598  -32.957 -29.554 1.00 33.63 ?  198 ILE   B O   1 
ATOM   3320 C CB  . ILE   B 1 198 ? -9.989  -31.496 -32.552 1.00 32.76 ?  198 ILE   B CB  1 
ATOM   3321 C CG1 . ILE   B 1 198 ? -10.026 -30.079 -33.125 1.00 25.08 ?  198 ILE   B CG1 1 
ATOM   3322 C CG2 . ILE   B 1 198 ? -11.381 -31.875 -32.014 1.00 30.74 ?  198 ILE   B CG2 1 
ATOM   3323 C CD1 . ILE   B 1 198 ? -10.768 -30.012 -34.413 1.00 24.66 ?  198 ILE   B CD1 1 
ATOM   3324 N N   . ILE   B 1 199 ? -8.540  -33.974 -31.258 1.00 32.17 ?  199 ILE   B N   1 
ATOM   3325 C CA  . ILE   B 1 199 ? -8.713  -35.287 -30.657 1.00 35.63 ?  199 ILE   B CA  1 
ATOM   3326 C C   . ILE   B 1 199 ? -8.017  -35.335 -29.308 1.00 43.81 ?  199 ILE   B C   1 
ATOM   3327 O O   . ILE   B 1 199 ? -8.574  -35.846 -28.329 1.00 38.35 ?  199 ILE   B O   1 
ATOM   3328 C CB  . ILE   B 1 199 ? -8.232  -36.387 -31.624 1.00 38.06 ?  199 ILE   B CB  1 
ATOM   3329 C CG1 . ILE   B 1 199 ? -9.389  -36.715 -32.586 1.00 38.66 ?  199 ILE   B CG1 1 
ATOM   3330 C CG2 . ILE   B 1 199 ? -7.768  -37.620 -30.845 1.00 37.77 ?  199 ILE   B CG2 1 
ATOM   3331 C CD1 . ILE   B 1 199 ? -9.017  -37.494 -33.833 1.00 35.53 ?  199 ILE   B CD1 1 
ATOM   3332 N N   . GLN   B 1 200 ? -6.823  -34.743 -29.205 1.00 38.64 ?  200 GLN   B N   1 
ATOM   3333 C CA  . GLN   B 1 200 ? -6.166  -34.795 -27.905 1.00 43.79 ?  200 GLN   B CA  1 
ATOM   3334 C C   . GLN   B 1 200 ? -6.830  -33.855 -26.910 1.00 37.96 ?  200 GLN   B C   1 
ATOM   3335 O O   . GLN   B 1 200 ? -6.829  -34.129 -25.705 1.00 37.38 ?  200 GLN   B O   1 
ATOM   3336 C CB  . GLN   B 1 200 ? -4.664  -34.522 -28.025 1.00 45.53 ?  200 GLN   B CB  1 
ATOM   3337 C CG  . GLN   B 1 200 ? -4.245  -33.313 -28.735 1.00 44.31 ?  200 GLN   B CG  1 
ATOM   3338 C CD  . GLN   B 1 200 ? -2.741  -33.249 -28.811 1.00 51.05 ?  200 GLN   B CD  1 
ATOM   3339 O OE1 . GLN   B 1 200 ? -2.124  -32.302 -28.330 1.00 49.48 ?  200 GLN   B OE1 1 
ATOM   3340 N NE2 . GLN   B 1 200 ? -2.137  -34.276 -29.396 1.00 47.55 ?  200 GLN   B NE2 1 
ATOM   3341 N N   . TRP   B 1 201 ? -7.453  -32.786 -27.389 1.00 34.47 ?  201 TRP   B N   1 
ATOM   3342 C CA  . TRP   B 1 201 ? -8.263  -31.963 -26.503 1.00 38.13 ?  201 TRP   B CA  1 
ATOM   3343 C C   . TRP   B 1 201 ? -9.434  -32.770 -25.949 1.00 40.08 ?  201 TRP   B C   1 
ATOM   3344 O O   . TRP   B 1 201 ? -9.670  -32.802 -24.733 1.00 40.93 ?  201 TRP   B O   1 
ATOM   3345 C CB  . TRP   B 1 201 ? -8.754  -30.726 -27.257 1.00 30.97 ?  201 TRP   B CB  1 
ATOM   3346 C CG  . TRP   B 1 201 ? -9.808  -30.007 -26.539 1.00 31.98 ?  201 TRP   B CG  1 
ATOM   3347 C CD1 . TRP   B 1 201 ? -9.645  -29.086 -25.524 1.00 42.04 ?  201 TRP   B CD1 1 
ATOM   3348 C CD2 . TRP   B 1 201 ? -11.209 -30.117 -26.757 1.00 37.08 ?  201 TRP   B CD2 1 
ATOM   3349 N NE1 . TRP   B 1 201 ? -10.872 -28.630 -25.104 1.00 35.23 ?  201 TRP   B NE1 1 
ATOM   3350 C CE2 . TRP   B 1 201 ? -11.847 -29.247 -25.842 1.00 33.54 ?  201 TRP   B CE2 1 
ATOM   3351 C CE3 . TRP   B 1 201 ? -11.996 -30.874 -27.631 1.00 39.30 ?  201 TRP   B CE3 1 
ATOM   3352 C CZ2 . TRP   B 1 201 ? -13.223 -29.128 -25.774 1.00 43.27 ?  201 TRP   B CZ2 1 
ATOM   3353 C CZ3 . TRP   B 1 201 ? -13.374 -30.738 -27.564 1.00 40.45 ?  201 TRP   B CZ3 1 
ATOM   3354 C CH2 . TRP   B 1 201 ? -13.968 -29.869 -26.653 1.00 40.30 ?  201 TRP   B CH2 1 
ATOM   3355 N N   . ARG   B 1 202 ? -10.170 -33.439 -26.839 1.00 37.61 ?  202 ARG   B N   1 
ATOM   3356 C CA  . ARG   B 1 202 ? -11.304 -34.270 -26.439 1.00 46.77 ?  202 ARG   B CA  1 
ATOM   3357 C C   . ARG   B 1 202 ? -10.908 -35.299 -25.395 1.00 46.61 ?  202 ARG   B C   1 
ATOM   3358 O O   . ARG   B 1 202 ? -11.702 -35.628 -24.508 1.00 51.25 ?  202 ARG   B O   1 
ATOM   3359 C CB  . ARG   B 1 202 ? -11.879 -34.998 -27.656 1.00 42.62 ?  202 ARG   B CB  1 
ATOM   3360 C CG  . ARG   B 1 202 ? -12.716 -34.141 -28.562 1.00 47.98 ?  202 ARG   B CG  1 
ATOM   3361 C CD  . ARG   B 1 202 ? -13.871 -34.926 -29.165 1.00 50.68 ?  202 ARG   B CD  1 
ATOM   3362 N NE  . ARG   B 1 202 ? -13.474 -35.761 -30.294 1.00 56.99 ?  202 ARG   B NE  1 
ATOM   3363 C CZ  . ARG   B 1 202 ? -13.626 -35.418 -31.575 1.00 62.46 ?  202 ARG   B CZ  1 
ATOM   3364 N NH1 . ARG   B 1 202 ? -14.143 -34.231 -31.900 1.00 52.01 ?  202 ARG   B NH1 1 
ATOM   3365 N NH2 . ARG   B 1 202 ? -13.246 -36.263 -32.533 1.00 57.80 ?  202 ARG   B NH2 1 
ATOM   3366 N N   . ASN   B 1 203 ? -9.697  -35.828 -25.496 1.00 43.24 ?  203 ASN   B N   1 
ATOM   3367 C CA  . ASN   B 1 203 ? -9.253  -36.937 -24.667 1.00 45.21 ?  203 ASN   B CA  1 
ATOM   3368 C C   . ASN   B 1 203 ? -8.511  -36.474 -23.426 1.00 44.63 ?  203 ASN   B C   1 
ATOM   3369 O O   . ASN   B 1 203 ? -7.974  -37.314 -22.697 1.00 48.74 ?  203 ASN   B O   1 
ATOM   3370 C CB  . ASN   B 1 203 ? -8.341  -37.869 -25.477 1.00 49.03 ?  203 ASN   B CB  1 
ATOM   3371 C CG  . ASN   B 1 203 ? -9.087  -38.677 -26.506 1.00 54.16 ?  203 ASN   B CG  1 
ATOM   3372 O OD1 . ASN   B 1 203 ? -10.316 -38.683 -26.545 1.00 56.35 ?  203 ASN   B OD1 1 
ATOM   3373 N ND2 . ASN   B 1 203 ? -8.340  -39.341 -27.382 1.00 62.32 ?  203 ASN   B ND2 1 
ATOM   3374 N N   . ALA   B 1 204 ? -8.446  -35.166 -23.183 1.00 39.76 ?  204 ALA   B N   1 
ATOM   3375 C CA  . ALA   B 1 204 ? -7.654  -34.629 -22.085 1.00 44.42 ?  204 ALA   B CA  1 
ATOM   3376 C C   . ALA   B 1 204 ? -6.211  -35.128 -22.164 1.00 49.87 ?  204 ALA   B C   1 
ATOM   3377 O O   . ALA   B 1 204 ? -5.570  -35.411 -21.152 1.00 59.71 ?  204 ALA   B O   1 
ATOM   3378 C CB  . ALA   B 1 204 ? -8.294  -34.967 -20.732 1.00 48.28 ?  204 ALA   B CB  1 
ATOM   3379 N N   . ASN   B 1 205 ? -5.700  -35.258 -23.382 1.00 45.20 ?  205 ASN   B N   1 
ATOM   3380 C CA  . ASN   B 1 205 ? -4.331  -35.705 -23.568 1.00 46.99 ?  205 ASN   B CA  1 
ATOM   3381 C C   . ASN   B 1 205 ? -3.401  -34.592 -23.089 1.00 54.91 ?  205 ASN   B C   1 
ATOM   3382 O O   . ASN   B 1 205 ? -3.483  -33.463 -23.594 1.00 45.79 ?  205 ASN   B O   1 
ATOM   3383 C CB  . ASN   B 1 205 ? -4.098  -36.073 -25.037 1.00 47.07 ?  205 ASN   B CB  1 
ATOM   3384 C CG  . ASN   B 1 205 ? -2.650  -36.462 -25.351 1.00 46.30 ?  205 ASN   B CG  1 
ATOM   3385 O OD1 . ASN   B 1 205 ? -1.735  -36.264 -24.552 1.00 55.75 ?  205 ASN   B OD1 1 
ATOM   3386 N ND2 . ASN   B 1 205 ? -2.443  -37.023 -26.539 1.00 48.66 ?  205 ASN   B ND2 1 
ATOM   3387 N N   . PRO   B 1 206 ? -2.534  -34.851 -22.104 1.00 57.27 ?  206 PRO   B N   1 
ATOM   3388 C CA  . PRO   B 1 206 ? -1.725  -33.762 -21.530 1.00 56.07 ?  206 PRO   B CA  1 
ATOM   3389 C C   . PRO   B 1 206 ? -0.677  -33.207 -22.478 1.00 48.17 ?  206 PRO   B C   1 
ATOM   3390 O O   . PRO   B 1 206 ? -0.175  -32.105 -22.224 1.00 52.90 ?  206 PRO   B O   1 
ATOM   3391 C CB  . PRO   B 1 206 ? -1.080  -34.418 -20.302 1.00 54.73 ?  206 PRO   B CB  1 
ATOM   3392 C CG  . PRO   B 1 206 ? -1.072  -35.881 -20.620 1.00 58.97 ?  206 PRO   B CG  1 
ATOM   3393 C CD  . PRO   B 1 206 ? -2.328  -36.127 -21.397 1.00 53.08 ?  206 PRO   B CD  1 
ATOM   3394 N N   . GLN   B 1 207 ? -0.340  -33.921 -23.561 1.00 49.61 ?  207 GLN   B N   1 
ATOM   3395 C CA  . GLN   B 1 207 ? 0.582   -33.387 -24.560 1.00 52.58 ?  207 GLN   B CA  1 
ATOM   3396 C C   . GLN   B 1 207 ? 0.060   -32.105 -25.206 1.00 54.04 ?  207 GLN   B C   1 
ATOM   3397 O O   . GLN   B 1 207 ? 0.850   -31.375 -25.819 1.00 40.78 ?  207 GLN   B O   1 
ATOM   3398 C CB  . GLN   B 1 207 ? 0.871   -34.430 -25.644 1.00 47.95 ?  207 GLN   B CB  1 
ATOM   3399 N N   . LEU   B 1 208 ? -1.244  -31.817 -25.078 1.00 51.10 ?  208 LEU   B N   1 
ATOM   3400 C CA  . LEU   B 1 208 ? -1.794  -30.549 -25.561 1.00 43.77 ?  208 LEU   B CA  1 
ATOM   3401 C C   . LEU   B 1 208 ? -1.259  -29.381 -24.745 1.00 39.27 ?  208 LEU   B C   1 
ATOM   3402 O O   . LEU   B 1 208 ? -0.664  -28.443 -25.285 1.00 30.65 ?  208 LEU   B O   1 
ATOM   3403 C CB  . LEU   B 1 208 ? -3.326  -30.569 -25.495 1.00 36.20 ?  208 LEU   B CB  1 
ATOM   3404 C CG  . LEU   B 1 208 ? -4.018  -29.293 -25.977 1.00 37.56 ?  208 LEU   B CG  1 
ATOM   3405 C CD1 . LEU   B 1 208 ? -3.729  -29.092 -27.449 1.00 34.71 ?  208 LEU   B CD1 1 
ATOM   3406 C CD2 . LEU   B 1 208 ? -5.512  -29.375 -25.765 1.00 44.66 ?  208 LEU   B CD2 1 
ATOM   3407 N N   . ALA   B 1 209 ? -1.495  -29.405 -23.440 1.00 39.51 ?  209 ALA   B N   1 
ATOM   3408 C CA  . ALA   B 1 209 ? -1.040  -28.301 -22.609 1.00 34.46 ?  209 ALA   B CA  1 
ATOM   3409 C C   . ALA   B 1 209 ? 0.478   -28.240 -22.590 1.00 35.18 ?  209 ALA   B C   1 
ATOM   3410 O O   . ALA   B 1 209 ? 1.063   -27.152 -22.597 1.00 41.30 ?  209 ALA   B O   1 
ATOM   3411 C CB  . ALA   B 1 209 ? -1.622  -28.444 -21.202 1.00 40.32 ?  209 ALA   B CB  1 
ATOM   3412 N N   . ALA   B 1 210 ? 1.131   -29.405 -22.613 1.00 43.53 ?  210 ALA   B N   1 
ATOM   3413 C CA  . ALA   B 1 210 ? 2.588   -29.440 -22.692 1.00 43.23 ?  210 ALA   B CA  1 
ATOM   3414 C C   . ALA   B 1 210 ? 3.084   -28.733 -23.943 1.00 35.94 ?  210 ALA   B C   1 
ATOM   3415 O O   . ALA   B 1 210 ? 3.951   -27.859 -23.872 1.00 38.97 ?  210 ALA   B O   1 
ATOM   3416 C CB  . ALA   B 1 210 ? 3.089   -30.887 -22.672 1.00 43.32 ?  210 ALA   B CB  1 
ATOM   3417 N N   . ASP   B 1 211 ? 2.546   -29.105 -25.102 1.00 38.97 ?  211 ASP   B N   1 
ATOM   3418 C CA  . ASP   B 1 211 ? 3.044   -28.543 -26.349 1.00 35.99 ?  211 ASP   B CA  1 
ATOM   3419 C C   . ASP   B 1 211 ? 2.736   -27.060 -26.446 1.00 29.58 ?  211 ASP   B C   1 
ATOM   3420 O O   . ASP   B 1 211 ? 3.552   -26.288 -26.948 1.00 36.41 ?  211 ASP   B O   1 
ATOM   3421 C CB  . ASP   B 1 211 ? 2.450   -29.304 -27.530 1.00 46.02 ?  211 ASP   B CB  1 
ATOM   3422 C CG  . ASP   B 1 211 ? 3.110   -30.658 -27.730 1.00 56.02 ?  211 ASP   B CG  1 
ATOM   3423 O OD1 . ASP   B 1 211 ? 3.622   -31.210 -26.725 1.00 45.07 ?  211 ASP   B OD1 1 
ATOM   3424 O OD2 . ASP   B 1 211 ? 3.117   -31.159 -28.881 1.00 60.43 -1 211 ASP   B OD2 1 
ATOM   3425 N N   . TYR   B 1 212 ? 1.575   -26.642 -25.954 1.00 26.43 ?  212 TYR   B N   1 
ATOM   3426 C CA  . TYR   B 1 212 ? 1.229   -25.226 -26.019 1.00 36.23 ?  212 TYR   B CA  1 
ATOM   3427 C C   . TYR   B 1 212 ? 2.198   -24.393 -25.189 1.00 33.03 ?  212 TYR   B C   1 
ATOM   3428 O O   . TYR   B 1 212 ? 2.647   -23.328 -25.623 1.00 34.36 ?  212 TYR   B O   1 
ATOM   3429 C CB  . TYR   B 1 212 ? -0.204  -24.997 -25.542 1.00 26.25 ?  212 TYR   B CB  1 
ATOM   3430 C CG  . TYR   B 1 212 ? -0.591  -23.541 -25.665 1.00 29.91 ?  212 TYR   B CG  1 
ATOM   3431 C CD1 . TYR   B 1 212 ? -1.149  -23.052 -26.836 1.00 27.94 ?  212 TYR   B CD1 1 
ATOM   3432 C CD2 . TYR   B 1 212 ? -0.335  -22.639 -24.624 1.00 25.78 ?  212 TYR   B CD2 1 
ATOM   3433 C CE1 . TYR   B 1 212 ? -1.469  -21.703 -26.971 1.00 34.69 ?  212 TYR   B CE1 1 
ATOM   3434 C CE2 . TYR   B 1 212 ? -0.636  -21.292 -24.757 1.00 29.73 ?  212 TYR   B CE2 1 
ATOM   3435 C CZ  . TYR   B 1 212 ? -1.211  -20.831 -25.913 1.00 32.44 ?  212 TYR   B CZ  1 
ATOM   3436 O OH  . TYR   B 1 212 ? -1.534  -19.498 -26.025 1.00 37.22 ?  212 TYR   B OH  1 
ATOM   3437 N N   . ARG   B 1 213 ? 2.519   -24.862 -23.984 1.00 37.65 ?  213 ARG   B N   1 
ATOM   3438 C CA  . ARG   B 1 213 ? 3.448   -24.133 -23.130 1.00 41.33 ?  213 ARG   B CA  1 
ATOM   3439 C C   . ARG   B 1 213 ? 4.833   -24.067 -23.757 1.00 39.98 ?  213 ARG   B C   1 
ATOM   3440 O O   . ARG   B 1 213 ? 5.538   -23.058 -23.615 1.00 41.94 ?  213 ARG   B O   1 
ATOM   3441 C CB  . ARG   B 1 213 ? 3.501   -24.792 -21.747 1.00 44.31 ?  213 ARG   B CB  1 
ATOM   3442 C CG  . ARG   B 1 213 ? 2.334   -24.365 -20.863 1.00 49.81 ?  213 ARG   B CG  1 
ATOM   3443 C CD  . ARG   B 1 213 ? 2.431   -24.942 -19.465 1.00 54.71 ?  213 ARG   B CD  1 
ATOM   3444 N NE  . ARG   B 1 213 ? 1.980   -26.328 -19.395 1.00 43.00 ?  213 ARG   B NE  1 
ATOM   3445 C CZ  . ARG   B 1 213 ? 0.832   -26.713 -18.842 1.00 55.84 ?  213 ARG   B CZ  1 
ATOM   3446 N NH1 . ARG   B 1 213 ? 0.019   -25.807 -18.313 1.00 45.96 ?  213 ARG   B NH1 1 
ATOM   3447 N NH2 . ARG   B 1 213 ? 0.491   -28.007 -18.821 1.00 48.12 ?  213 ARG   B NH2 1 
ATOM   3448 N N   . ALA   B 1 214 ? 5.230   -25.124 -24.473 1.00 33.11 ?  214 ALA   B N   1 
ATOM   3449 C CA  . ALA   B 1 214 ? 6.551   -25.145 -25.093 1.00 43.84 ?  214 ALA   B CA  1 
ATOM   3450 C C   . ALA   B 1 214 ? 6.640   -24.166 -26.263 1.00 45.10 ?  214 ALA   B C   1 
ATOM   3451 O O   . ALA   B 1 214 ? 7.687   -23.550 -26.472 1.00 39.53 ?  214 ALA   B O   1 
ATOM   3452 C CB  . ALA   B 1 214 ? 6.897   -26.563 -25.545 1.00 35.61 ?  214 ALA   B CB  1 
ATOM   3453 N N   . ARG   B 1 215 ? 5.560   -23.998 -27.031 1.00 38.55 ?  215 ARG   B N   1 
ATOM   3454 C CA  . ARG   B 1 215 ? 5.577   -23.110 -28.193 1.00 39.32 ?  215 ARG   B CA  1 
ATOM   3455 C C   . ARG   B 1 215 ? 4.955   -21.745 -27.913 1.00 32.40 ?  215 ARG   B C   1 
ATOM   3456 O O   . ARG   B 1 215 ? 4.798   -20.935 -28.842 1.00 30.89 ?  215 ARG   B O   1 
ATOM   3457 C CB  . ARG   B 1 215 ? 4.868   -23.764 -29.381 1.00 38.00 ?  215 ARG   B CB  1 
ATOM   3458 C CG  . ARG   B 1 215 ? 5.649   -24.932 -30.033 1.00 45.83 ?  215 ARG   B CG  1 
ATOM   3459 C CD  . ARG   B 1 215 ? 4.690   -25.687 -30.925 1.00 51.36 ?  215 ARG   B CD  1 
ATOM   3460 N NE  . ARG   B 1 215 ? 5.148   -26.976 -31.429 1.00 65.76 ?  215 ARG   B NE  1 
ATOM   3461 C CZ  . ARG   B 1 215 ? 5.300   -28.063 -30.677 1.00 65.04 ?  215 ARG   B CZ  1 
ATOM   3462 N NH1 . ARG   B 1 215 ? 5.067   -28.006 -29.370 1.00 60.53 ?  215 ARG   B NH1 1 
ATOM   3463 N NH2 . ARG   B 1 215 ? 5.692   -29.206 -31.231 1.00 71.70 ?  215 ARG   B NH2 1 
ATOM   3464 N N   . SER   B 1 216 ? 4.595   -21.471 -26.670 1.00 33.17 ?  216 SER   B N   1 
ATOM   3465 C CA  . SER   B 1 216 ? 4.044   -20.169 -26.331 1.00 34.84 ?  216 SER   B CA  1 
ATOM   3466 C C   . SER   B 1 216 ? 5.136   -19.109 -26.376 1.00 34.41 ?  216 SER   B C   1 
ATOM   3467 O O   . SER   B 1 216 ? 6.238   -19.314 -25.854 1.00 34.49 ?  216 SER   B O   1 
ATOM   3468 C CB  . SER   B 1 216 ? 3.418   -20.202 -24.938 1.00 32.52 ?  216 SER   B CB  1 
ATOM   3469 O OG  . SER   B 1 216 ? 3.120   -18.883 -24.493 1.00 38.87 ?  216 SER   B OG  1 
ATOM   3470 N N   . LEU   B 1 217 ? 4.832   -17.974 -26.995 1.00 30.38 ?  217 LEU   B N   1 
ATOM   3471 C CA  . LEU   B 1 217 ? 5.718   -16.823 -26.891 1.00 31.48 ?  217 LEU   B CA  1 
ATOM   3472 C C   . LEU   B 1 217 ? 5.332   -15.905 -25.740 1.00 39.38 ?  217 LEU   B C   1 
ATOM   3473 O O   . LEU   B 1 217 ? 6.151   -15.078 -25.312 1.00 34.22 ?  217 LEU   B O   1 
ATOM   3474 C CB  . LEU   B 1 217 ? 5.729   -16.043 -28.204 1.00 32.30 ?  217 LEU   B CB  1 
ATOM   3475 C CG  . LEU   B 1 217 ? 6.228   -16.756 -29.468 1.00 36.34 ?  217 LEU   B CG  1 
ATOM   3476 C CD1 . LEU   B 1 217 ? 5.938   -15.921 -30.688 1.00 34.83 ?  217 LEU   B CD1 1 
ATOM   3477 C CD2 . LEU   B 1 217 ? 7.724   -17.116 -29.405 1.00 36.88 ?  217 LEU   B CD2 1 
ATOM   3478 N N   . THR   B 1 218 ? 4.115   -16.049 -25.215 1.00 33.37 ?  218 THR   B N   1 
ATOM   3479 C CA  . THR   B 1 218 ? 3.691   -15.271 -24.057 1.00 33.32 ?  218 THR   B CA  1 
ATOM   3480 C C   . THR   B 1 218 ? 4.329   -15.794 -22.764 1.00 31.26 ?  218 THR   B C   1 
ATOM   3481 O O   . THR   B 1 218 ? 4.860   -15.015 -21.963 1.00 33.59 ?  218 THR   B O   1 
ATOM   3482 C CB  . THR   B 1 218 ? 2.159   -15.294 -23.991 1.00 36.87 ?  218 THR   B CB  1 
ATOM   3483 O OG1 . THR   B 1 218 ? 1.644   -14.937 -25.284 1.00 32.67 ?  218 THR   B OG1 1 
ATOM   3484 C CG2 . THR   B 1 218 ? 1.617   -14.326 -22.927 1.00 32.69 ?  218 THR   B CG2 1 
ATOM   3485 N N   . ILE   B 1 219 ? 4.323   -17.109 -22.564 1.00 27.85 ?  219 ILE   B N   1 
ATOM   3486 C CA  . ILE   B 1 219 ? 4.820   -17.689 -21.317 1.00 31.99 ?  219 ILE   B CA  1 
ATOM   3487 C C   . ILE   B 1 219 ? 6.307   -17.407 -21.156 1.00 28.91 ?  219 ILE   B C   1 
ATOM   3488 O O   . ILE   B 1 219 ? 7.095   -17.594 -22.087 1.00 37.33 ?  219 ILE   B O   1 
ATOM   3489 C CB  . ILE   B 1 219 ? 4.536   -19.198 -21.291 1.00 32.49 ?  219 ILE   B CB  1 
ATOM   3490 C CG1 . ILE   B 1 219 ? 3.057   -19.435 -21.010 1.00 39.50 ?  219 ILE   B CG1 1 
ATOM   3491 C CG2 . ILE   B 1 219 ? 5.388   -19.890 -20.243 1.00 31.67 ?  219 ILE   B CG2 1 
ATOM   3492 C CD1 . ILE   B 1 219 ? 2.696   -20.864 -21.010 1.00 44.39 ?  219 ILE   B CD1 1 
ATOM   3493 N N   . GLY   B 1 220 ? 6.698   -16.961 -19.965 1.00 32.73 ?  220 GLY   B N   1 
ATOM   3494 C CA  . GLY   B 1 220 ? 8.063   -16.561 -19.685 1.00 25.18 ?  220 GLY   B CA  1 
ATOM   3495 C C   . GLY   B 1 220 ? 8.370   -15.123 -20.030 1.00 39.52 ?  220 GLY   B C   1 
ATOM   3496 O O   . GLY   B 1 220 ? 9.498   -14.670 -19.807 1.00 48.07 ?  220 GLY   B O   1 
ATOM   3497 N N   . SER   B 1 221 ? 7.419   -14.400 -20.596 1.00 31.43 ?  221 SER   B N   1 
ATOM   3498 C CA  . SER   B 1 221 ? 7.632   -13.020 -20.990 1.00 38.20 ?  221 SER   B CA  1 
ATOM   3499 C C   . SER   B 1 221 ? 6.961   -12.085 -20.001 1.00 33.94 ?  221 SER   B C   1 
ATOM   3500 O O   . SER   B 1 221 ? 5.896   -12.395 -19.451 1.00 31.10 ?  221 SER   B O   1 
ATOM   3501 C CB  . SER   B 1 221 ? 7.065   -12.747 -22.392 1.00 36.41 ?  221 SER   B CB  1 
ATOM   3502 O OG  . SER   B 1 221 ? 7.565   -13.677 -23.332 1.00 45.20 ?  221 SER   B OG  1 
ATOM   3503 N N   A ARG   B 1 222 ? 7.600   -10.946 -19.758 0.55 32.88 ?  222 ARG   B N   1 
ATOM   3504 N N   B ARG   B 1 222 ? 7.597   -10.940 -19.781 0.45 32.67 ?  222 ARG   B N   1 
ATOM   3505 C CA  A ARG   B 1 222 ? 6.880   -9.836  -19.163 0.55 31.09 ?  222 ARG   B CA  1 
ATOM   3506 C CA  B ARG   B 1 222 ? 6.916   -9.800  -19.193 0.45 31.22 ?  222 ARG   B CA  1 
ATOM   3507 C C   A ARG   B 1 222 ? 5.858   -9.361  -20.184 0.55 30.62 ?  222 ARG   B C   1 
ATOM   3508 C C   B ARG   B 1 222 ? 5.863   -9.329  -20.192 0.45 31.23 ?  222 ARG   B C   1 
ATOM   3509 O O   A ARG   B 1 222 ? 6.194   -9.133  -21.349 0.55 32.92 ?  222 ARG   B O   1 
ATOM   3510 O O   B ARG   B 1 222 ? 6.184   -9.067  -21.354 0.45 32.60 ?  222 ARG   B O   1 
ATOM   3511 C CB  A ARG   B 1 222 ? 7.828   -8.704  -18.765 0.55 34.06 ?  222 ARG   B CB  1 
ATOM   3512 C CB  B ARG   B 1 222 ? 7.929   -8.699  -18.882 0.45 34.03 ?  222 ARG   B CB  1 
ATOM   3513 C CG  A ARG   B 1 222 ? 7.102   -7.519  -18.123 0.55 30.86 ?  222 ARG   B CG  1 
ATOM   3514 C CG  B ARG   B 1 222 ? 7.442   -7.595  -17.952 0.45 31.05 ?  222 ARG   B CG  1 
ATOM   3515 C CD  A ARG   B 1 222 ? 8.042   -6.518  -17.491 0.55 34.44 ?  222 ARG   B CD  1 
ATOM   3516 C CD  B ARG   B 1 222 ? 8.411   -6.416  -17.924 0.45 35.19 ?  222 ARG   B CD  1 
ATOM   3517 N NE  A ARG   B 1 222 ? 8.776   -7.076  -16.365 0.55 28.11 ?  222 ARG   B NE  1 
ATOM   3518 N NE  B ARG   B 1 222 ? 9.810   -6.820  -18.061 0.45 32.78 ?  222 ARG   B NE  1 
ATOM   3519 C CZ  A ARG   B 1 222 ? 10.087  -7.286  -16.375 0.55 32.23 ?  222 ARG   B CZ  1 
ATOM   3520 C CZ  B ARG   B 1 222 ? 10.614  -6.409  -19.037 0.45 36.01 ?  222 ARG   B CZ  1 
ATOM   3521 N NH1 A ARG   B 1 222 ? 10.791  -6.963  -17.453 0.55 28.40 ?  222 ARG   B NH1 1 
ATOM   3522 N NH1 B ARG   B 1 222 ? 10.162  -5.575  -19.970 0.45 31.11 ?  222 ARG   B NH1 1 
ATOM   3523 N NH2 A ARG   B 1 222 ? 10.695  -7.797  -15.308 0.55 30.63 ?  222 ARG   B NH2 1 
ATOM   3524 N NH2 B ARG   B 1 222 ? 11.875  -6.828  -19.080 0.45 34.97 ?  222 ARG   B NH2 1 
ATOM   3525 N N   . VAL   B 1 223 ? 4.599   -9.276  -19.772 1.00 29.26 ?  223 VAL   B N   1 
ATOM   3526 C CA  . VAL   B 1 223 ? 3.515   -8.950  -20.685 1.00 27.93 ?  223 VAL   B CA  1 
ATOM   3527 C C   . VAL   B 1 223 ? 2.611   -7.903  -20.069 1.00 28.93 ?  223 VAL   B C   1 
ATOM   3528 O O   . VAL   B 1 223 ? 2.568   -7.697  -18.860 1.00 31.94 ?  223 VAL   B O   1 
ATOM   3529 C CB  . VAL   B 1 223 ? 2.668   -10.167 -21.111 1.00 32.08 ?  223 VAL   B CB  1 
ATOM   3530 C CG1 . VAL   B 1 223 ? 3.523   -11.184 -21.829 1.00 25.20 ?  223 VAL   B CG1 1 
ATOM   3531 C CG2 . VAL   B 1 223 ? 1.964   -10.783 -19.930 1.00 28.69 ?  223 VAL   B CG2 1 
ATOM   3532 N N   . ARG   B 1 224 ? 1.888   -7.241  -20.940 1.00 29.92 ?  224 ARG   B N   1 
ATOM   3533 C CA  . ARG   B 1 224 ? 0.954   -6.203  -20.574 1.00 32.65 ?  224 ARG   B CA  1 
ATOM   3534 C C   . ARG   B 1 224 ? -0.390  -6.665  -21.092 1.00 32.63 ?  224 ARG   B C   1 
ATOM   3535 O O   . ARG   B 1 224 ? -0.536  -6.929  -22.288 1.00 40.24 ?  224 ARG   B O   1 
ATOM   3536 C CB  . ARG   B 1 224 ? 1.378   -4.893  -21.203 1.00 29.46 ?  224 ARG   B CB  1 
ATOM   3537 C CG  . ARG   B 1 224 ? 0.447   -3.802  -20.984 1.00 43.92 ?  224 ARG   B CG  1 
ATOM   3538 C CD  . ARG   B 1 224 ? 1.221   -2.549  -21.133 1.00 42.00 ?  224 ARG   B CD  1 
ATOM   3539 N NE  . ARG   B 1 224 ? 0.303   -1.448  -21.229 1.00 44.94 ?  224 ARG   B NE  1 
ATOM   3540 C CZ  . ARG   B 1 224 ? 0.174   -0.552  -20.272 1.00 46.58 ?  224 ARG   B CZ  1 
ATOM   3541 N NH1 . ARG   B 1 224 ? 0.926   -0.647  -19.168 1.00 47.43 ?  224 ARG   B NH1 1 
ATOM   3542 N NH2 . ARG   B 1 224 ? -0.697  0.429   -20.428 1.00 57.40 ?  224 ARG   B NH2 1 
ATOM   3543 N N   . VAL   B 1 225 ? -1.331  -6.865  -20.195 1.00 33.89 ?  225 VAL   B N   1 
ATOM   3544 C CA  . VAL   B 1 225 ? -2.645  -7.354  -20.576 1.00 36.37 ?  225 VAL   B CA  1 
ATOM   3545 C C   . VAL   B 1 225 ? -3.560  -6.144  -20.624 1.00 42.32 ?  225 VAL   B C   1 
ATOM   3546 O O   . VAL   B 1 225 ? -3.774  -5.462  -19.617 1.00 46.69 ?  225 VAL   B O   1 
ATOM   3547 C CB  . VAL   B 1 225 ? -3.153  -8.453  -19.638 1.00 46.31 ?  225 VAL   B CB  1 
ATOM   3548 C CG1 . VAL   B 1 225 ? -4.612  -8.778  -19.965 1.00 54.15 ?  225 VAL   B CG1 1 
ATOM   3549 C CG2 . VAL   B 1 225 ? -2.298  -9.713  -19.828 1.00 37.23 ?  225 VAL   B CG2 1 
ATOM   3550 N N   . GLU   B 1 226 ? -4.013  -5.836  -21.832 1.00 45.01 ?  226 GLU   B N   1 
ATOM   3551 C CA  . GLU   B 1 226 ? -4.888  -4.705  -22.070 1.00 53.73 ?  226 GLU   B CA  1 
ATOM   3552 C C   . GLU   B 1 226 ? -6.314  -5.121  -21.728 1.00 50.57 ?  226 GLU   B C   1 
ATOM   3553 O O   . GLU   B 1 226 ? -6.832  -6.098  -22.280 1.00 52.33 ?  226 GLU   B O   1 
ATOM   3554 C CB  . GLU   B 1 226 ? -4.763  -4.252  -23.524 1.00 41.65 ?  226 GLU   B CB  1 
ATOM   3555 N N   . LEU   B 1 227 ? -6.920  -4.402  -20.790 1.00 56.41 ?  227 LEU   B N   1 
ATOM   3556 C CA  . LEU   B 1 227 ? -8.270  -4.571  -20.284 1.00 57.71 ?  227 LEU   B CA  1 
ATOM   3557 C C   . LEU   B 1 227 ? -9.095  -3.330  -20.593 1.00 54.25 ?  227 LEU   B C   1 
ATOM   3558 O O   . LEU   B 1 227 ? -8.548  -2.228  -20.692 1.00 50.03 ?  227 LEU   B O   1 
ATOM   3559 C CB  . LEU   B 1 227 ? -8.264  -4.800  -18.769 1.00 54.46 ?  227 LEU   B CB  1 
ATOM   3560 C CG  . LEU   B 1 227 ? -7.573  -6.069  -18.293 1.00 42.60 ?  227 LEU   B CG  1 
ATOM   3561 C CD1 . LEU   B 1 227 ? -7.388  -5.979  -16.800 1.00 41.13 ?  227 LEU   B CD1 1 
ATOM   3562 C CD2 . LEU   B 1 227 ? -8.387  -7.268  -18.675 1.00 46.06 ?  227 LEU   B CD2 1 
ATOM   3563 N N   . PRO   B 1 228 ? -10.414 -3.471  -20.722 1.00 63.45 ?  228 PRO   B N   1 
ATOM   3564 C CA  . PRO   B 1 228 ? -11.248 -2.308  -21.068 1.00 58.20 ?  228 PRO   B CA  1 
ATOM   3565 C C   . PRO   B 1 228 ? -11.139 -1.201  -20.030 1.00 53.57 ?  228 PRO   B C   1 
ATOM   3566 O O   . PRO   B 1 228 ? -10.913 -1.448  -18.844 1.00 41.48 ?  228 PRO   B O   1 
ATOM   3567 C CB  . PRO   B 1 228 ? -12.667 -2.890  -21.119 1.00 59.06 ?  228 PRO   B CB  1 
ATOM   3568 C CG  . PRO   B 1 228 ? -12.467 -4.375  -21.339 1.00 60.00 ?  228 PRO   B CG  1 
ATOM   3569 C CD  . PRO   B 1 228 ? -11.196 -4.717  -20.621 1.00 57.59 ?  228 PRO   B CD  1 
ATOM   3570 N N   . GLY   B 1 229 ? -11.270 0.039   -20.499 1.00 58.29 ?  229 GLY   B N   1 
ATOM   3571 C CA  . GLY   B 1 229 ? -11.333 1.177   -19.603 1.00 49.51 ?  229 GLY   B CA  1 
ATOM   3572 C C   . GLY   B 1 229 ? -10.006 1.749   -19.162 1.00 59.22 ?  229 GLY   B C   1 
ATOM   3573 O O   . GLY   B 1 229 ? -9.914  2.286   -18.048 1.00 56.09 ?  229 GLY   B O   1 
ATOM   3574 N N   . GLY   B 1 230 ? -8.972  1.667   -19.998 1.00 56.67 ?  230 GLY   B N   1 
ATOM   3575 C CA  . GLY   B 1 230 ? -7.657  2.100   -19.565 1.00 63.33 ?  230 GLY   B CA  1 
ATOM   3576 C C   . GLY   B 1 230 ? -7.006  1.211   -18.530 1.00 56.64 ?  230 GLY   B C   1 
ATOM   3577 O O   . GLY   B 1 230 ? -5.937  1.557   -18.017 1.00 63.48 ?  230 GLY   B O   1 
ATOM   3578 N N   . GLN   B 1 231 ? -7.623  0.082   -18.197 1.00 54.79 ?  231 GLN   B N   1 
ATOM   3579 C CA  . GLN   B 1 231 ? -7.057  -0.833  -17.217 1.00 61.80 ?  231 GLN   B CA  1 
ATOM   3580 C C   . GLN   B 1 231 ? -5.964  -1.651  -17.895 1.00 63.81 ?  231 GLN   B C   1 
ATOM   3581 O O   . GLN   B 1 231 ? -6.206  -2.278  -18.939 1.00 59.14 ?  231 GLN   B O   1 
ATOM   3582 C CB  . GLN   B 1 231 ? -8.140  -1.746  -16.637 1.00 61.79 ?  231 GLN   B CB  1 
ATOM   3583 C CG  . GLN   B 1 231 ? -9.368  -1.041  -16.033 1.00 56.17 ?  231 GLN   B CG  1 
ATOM   3584 C CD  . GLN   B 1 231 ? -9.023  -0.175  -14.833 1.00 56.87 ?  231 GLN   B CD  1 
ATOM   3585 O OE1 . GLN   B 1 231 ? -8.844  -0.676  -13.718 1.00 51.73 ?  231 GLN   B OE1 1 
ATOM   3586 N NE2 . GLN   B 1 231 ? -8.926  1.134   -15.056 1.00 49.96 ?  231 GLN   B NE2 1 
ATOM   3587 N N   . ASP   B 1 232 ? -4.759  -1.624  -17.327 1.00 59.36 ?  232 ASP   B N   1 
ATOM   3588 C CA  . ASP   B 1 232 ? -3.672  -2.474  -17.797 1.00 55.87 ?  232 ASP   B CA  1 
ATOM   3589 C C   . ASP   B 1 232 ? -2.983  -3.129  -16.609 1.00 53.99 ?  232 ASP   B C   1 
ATOM   3590 O O   . ASP   B 1 232 ? -2.696  -2.471  -15.603 1.00 58.22 ?  232 ASP   B O   1 
ATOM   3591 C CB  . ASP   B 1 232 ? -2.642  -1.698  -18.625 1.00 53.04 ?  232 ASP   B CB  1 
ATOM   3592 C CG  . ASP   B 1 232 ? -3.193  -1.224  -19.962 1.00 62.86 ?  232 ASP   B CG  1 
ATOM   3593 O OD1 . ASP   B 1 232 ? -3.615  -0.039  -20.051 1.00 71.92 ?  232 ASP   B OD1 1 
ATOM   3594 O OD2 . ASP   B 1 232 ? -3.233  -2.029  -20.917 1.00 73.46 -1 232 ASP   B OD2 1 
ATOM   3595 N N   . VAL   B 1 233 ? -2.706  -4.424  -16.742 1.00 54.12 ?  233 VAL   B N   1 
ATOM   3596 C CA  . VAL   B 1 233 ? -1.988  -5.195  -15.733 1.00 46.31 ?  233 VAL   B CA  1 
ATOM   3597 C C   . VAL   B 1 233 ? -0.713  -5.723  -16.373 1.00 37.87 ?  233 VAL   B C   1 
ATOM   3598 O O   . VAL   B 1 233 ? -0.771  -6.394  -17.413 1.00 42.44 ?  233 VAL   B O   1 
ATOM   3599 C CB  . VAL   B 1 233 ? -2.852  -6.343  -15.181 1.00 51.51 ?  233 VAL   B CB  1 
ATOM   3600 C CG1 . VAL   B 1 233 ? -2.031  -7.274  -14.298 1.00 45.66 ?  233 VAL   B CG1 1 
ATOM   3601 C CG2 . VAL   B 1 233 ? -4.014  -5.767  -14.403 1.00 41.73 ?  233 VAL   B CG2 1 
ATOM   3602 N N   . VAL   B 1 234 ? 0.430   -5.417  -15.765 1.00 31.61 ?  234 VAL   B N   1 
ATOM   3603 C CA  . VAL   B 1 234 ? 1.731   -5.883  -16.234 1.00 39.57 ?  234 VAL   B CA  1 
ATOM   3604 C C   . VAL   B 1 234 ? 2.232   -6.966  -15.280 1.00 38.37 ?  234 VAL   B C   1 
ATOM   3605 O O   . VAL   B 1 234 ? 2.275   -6.753  -14.064 1.00 36.14 ?  234 VAL   B O   1 
ATOM   3606 C CB  . VAL   B 1 234 ? 2.748   -4.734  -16.325 1.00 38.42 ?  234 VAL   B CB  1 
ATOM   3607 C CG1 . VAL   B 1 234 ? 4.070   -5.273  -16.809 1.00 29.82 ?  234 VAL   B CG1 1 
ATOM   3608 C CG2 . VAL   B 1 234 ? 2.238   -3.594  -17.244 1.00 33.61 ?  234 VAL   B CG2 1 
ATOM   3609 N N   . GLY   B 1 235 ? 2.607   -8.123  -15.824 1.00 31.56 ?  235 GLY   B N   1 
ATOM   3610 C CA  . GLY   B 1 235 ? 3.222   -9.166  -15.030 1.00 29.48 ?  235 GLY   B CA  1 
ATOM   3611 C C   . GLY   B 1 235 ? 4.034   -10.062 -15.933 1.00 31.53 ?  235 GLY   B C   1 
ATOM   3612 O O   . GLY   B 1 235 ? 4.149   -9.798  -17.129 1.00 37.25 ?  235 GLY   B O   1 
ATOM   3613 N N   . ILE   B 1 236 ? 4.630   -11.109 -15.350 1.00 29.92 ?  236 ILE   B N   1 
ATOM   3614 C CA  . ILE   B 1 236 ? 5.306   -12.164 -16.110 1.00 29.29 ?  236 ILE   B CA  1 
ATOM   3615 C C   . ILE   B 1 236 ? 4.285   -13.267 -16.318 1.00 30.14 ?  236 ILE   B C   1 
ATOM   3616 O O   . ILE   B 1 236 ? 3.713   -13.774 -15.346 1.00 30.41 ?  236 ILE   B O   1 
ATOM   3617 C CB  . ILE   B 1 236 ? 6.548   -12.739 -15.393 1.00 33.74 ?  236 ILE   B CB  1 
ATOM   3618 C CG1 . ILE   B 1 236 ? 7.529   -11.684 -14.882 1.00 35.76 ?  236 ILE   B CG1 1 
ATOM   3619 C CG2 . ILE   B 1 236 ? 7.256   -13.734 -16.288 1.00 29.55 ?  236 ILE   B CG2 1 
ATOM   3620 C CD1 . ILE   B 1 236 ? 7.866   -10.656 -15.839 1.00 37.01 ?  236 ILE   B CD1 1 
ATOM   3621 N N   . ALA   B 1 237 ? 4.043   -13.631 -17.571 1.00 30.13 ?  237 ALA   B N   1 
ATOM   3622 C CA  . ALA   B 1 237 ? 3.165   -14.757 -17.850 1.00 39.15 ?  237 ALA   B CA  1 
ATOM   3623 C C   . ALA   B 1 237 ? 3.878   -16.042 -17.429 1.00 34.54 ?  237 ALA   B C   1 
ATOM   3624 O O   . ALA   B 1 237 ? 4.890   -16.427 -18.025 1.00 34.83 ?  237 ALA   B O   1 
ATOM   3625 C CB  . ALA   B 1 237 ? 2.788   -14.779 -19.326 1.00 31.06 ?  237 ALA   B CB  1 
ATOM   3626 N N   . ARG   B 1 238 ? 3.373   -16.685 -16.377 1.00 35.36 ?  238 ARG   B N   1 
ATOM   3627 C CA  . ARG   B 1 238 ? 3.976   -17.912 -15.852 1.00 41.42 ?  238 ARG   B CA  1 
ATOM   3628 C C   . ARG   B 1 238 ? 3.356   -19.174 -16.424 1.00 36.06 ?  238 ARG   B C   1 
ATOM   3629 O O   . ARG   B 1 238 ? 4.070   -20.152 -16.657 1.00 39.66 ?  238 ARG   B O   1 
ATOM   3630 C CB  . ARG   B 1 238 ? 3.849   -17.963 -14.328 1.00 48.50 ?  238 ARG   B CB  1 
ATOM   3631 C CG  . ARG   B 1 238 ? 4.557   -16.840 -13.644 1.00 45.51 ?  238 ARG   B CG  1 
ATOM   3632 C CD  . ARG   B 1 238 ? 6.017   -17.147 -13.630 1.00 46.35 ?  238 ARG   B CD  1 
ATOM   3633 N NE  . ARG   B 1 238 ? 6.754   -16.209 -12.800 1.00 38.78 ?  238 ARG   B NE  1 
ATOM   3634 C CZ  . ARG   B 1 238 ? 8.007   -15.869 -13.056 1.00 48.61 ?  238 ARG   B CZ  1 
ATOM   3635 N NH1 . ARG   B 1 238 ? 8.645   -14.990 -12.279 1.00 50.07 ?  238 ARG   B NH1 1 
ATOM   3636 N NH2 . ARG   B 1 238 ? 8.611   -16.418 -14.108 1.00 44.31 ?  238 ARG   B NH2 1 
ATOM   3637 N N   . ASP   B 1 239 ? 2.048   -19.195 -16.645 1.00 32.18 ?  239 ASP   B N   1 
ATOM   3638 C CA  . ASP   B 1 239 ? 1.439   -20.455 -17.056 1.00 42.66 ?  239 ASP   B CA  1 
ATOM   3639 C C   . ASP   B 1 239 ? 0.037   -20.187 -17.604 1.00 40.56 ?  239 ASP   B C   1 
ATOM   3640 O O   . ASP   B 1 239 ? -0.457  -19.055 -17.627 1.00 33.47 ?  239 ASP   B O   1 
ATOM   3641 C CB  . ASP   B 1 239 ? 1.442   -21.449 -15.881 1.00 44.08 ?  239 ASP   B CB  1 
ATOM   3642 C CG  . ASP   B 1 239 ? 1.527   -22.932 -16.337 1.00 55.22 ?  239 ASP   B CG  1 
ATOM   3643 O OD1 . ASP   B 1 239 ? 1.051   -23.289 -17.438 1.00 52.10 ?  239 ASP   B OD1 1 
ATOM   3644 O OD2 . ASP   B 1 239 ? 2.163   -23.733 -15.621 1.00 55.10 -1 239 ASP   B OD2 1 
ATOM   3645 N N   . ILE   B 1 240 ? -0.566  -21.245 -18.113 1.00 38.27 ?  240 ILE   B N   1 
ATOM   3646 C CA  . ILE   B 1 240 ? -1.947  -21.270 -18.557 1.00 41.29 ?  240 ILE   B CA  1 
ATOM   3647 C C   . ILE   B 1 240 ? -2.646  -22.230 -17.622 1.00 48.74 ?  240 ILE   B C   1 
ATOM   3648 O O   . ILE   B 1 240 ? -2.098  -23.294 -17.308 1.00 51.02 ?  240 ILE   B O   1 
ATOM   3649 C CB  . ILE   B 1 240 ? -2.085  -21.754 -20.017 1.00 46.40 ?  240 ILE   B CB  1 
ATOM   3650 C CG1 . ILE   B 1 240 ? -1.135  -21.001 -20.936 1.00 41.25 ?  240 ILE   B CG1 1 
ATOM   3651 C CG2 . ILE   B 1 240 ? -3.512  -21.610 -20.485 1.00 46.09 ?  240 ILE   B CG2 1 
ATOM   3652 C CD1 . ILE   B 1 240 ? -1.621  -19.628 -21.249 1.00 39.36 ?  240 ILE   B CD1 1 
ATOM   3653 N N   . ASP   B 1 241 ? -3.831  -21.866 -17.158 1.00 40.65 ?  241 ASP   B N   1 
ATOM   3654 C CA  . ASP   B 1 241 ? -4.454  -22.735 -16.178 1.00 47.57 ?  241 ASP   B CA  1 
ATOM   3655 C C   . ASP   B 1 241 ? -5.288  -23.790 -16.900 1.00 52.30 ?  241 ASP   B C   1 
ATOM   3656 O O   . ASP   B 1 241 ? -5.295  -23.880 -18.129 1.00 54.09 ?  241 ASP   B O   1 
ATOM   3657 C CB  . ASP   B 1 241 ? -5.245  -21.925 -15.138 1.00 43.19 ?  241 ASP   B CB  1 
ATOM   3658 C CG  . ASP   B 1 241 ? -6.545  -21.330 -15.668 1.00 45.83 ?  241 ASP   B CG  1 
ATOM   3659 O OD1 . ASP   B 1 241 ? -7.023  -21.652 -16.789 1.00 47.25 ?  241 ASP   B OD1 1 
ATOM   3660 O OD2 . ASP   B 1 241 ? -7.117  -20.517 -14.926 1.00 47.87 -1 241 ASP   B OD2 1 
ATOM   3661 N N   . ASP   B 1 242 ? -6.009  -24.591 -16.124 1.00 52.98 ?  242 ASP   B N   1 
ATOM   3662 C CA  . ASP   B 1 242 ? -6.830  -25.687 -16.621 1.00 53.69 ?  242 ASP   B CA  1 
ATOM   3663 C C   . ASP   B 1 242 ? -7.999  -25.230 -17.488 1.00 53.28 ?  242 ASP   B C   1 
ATOM   3664 O O   . ASP   B 1 242 ? -8.534  -26.039 -18.250 1.00 60.10 ?  242 ASP   B O   1 
ATOM   3665 C CB  . ASP   B 1 242 ? -7.281  -26.512 -15.405 1.00 59.16 ?  242 ASP   B CB  1 
ATOM   3666 C CG  . ASP   B 1 242 ? -8.146  -25.720 -14.404 1.00 72.96 ?  242 ASP   B CG  1 
ATOM   3667 O OD1 . ASP   B 1 242 ? -8.623  -24.606 -14.715 1.00 76.72 ?  242 ASP   B OD1 1 
ATOM   3668 O OD2 . ASP   B 1 242 ? -8.246  -26.191 -13.236 1.00 90.95 -1 242 ASP   B OD2 1 
ATOM   3669 N N   . GLN   B 1 243 ? -8.412  -23.966 -17.395 1.00 53.86 ?  243 GLN   B N   1 
ATOM   3670 C CA  . GLN   B 1 243 ? -9.454  -23.447 -18.265 1.00 47.24 ?  243 GLN   B CA  1 
ATOM   3671 C C   . GLN   B 1 243 ? -8.898  -22.751 -19.498 1.00 44.83 ?  243 GLN   B C   1 
ATOM   3672 O O   . GLN   B 1 243 ? -9.677  -22.244 -20.310 1.00 45.72 ?  243 GLN   B O   1 
ATOM   3673 C CB  . GLN   B 1 243 ? -10.354 -22.494 -17.490 1.00 51.59 ?  243 GLN   B CB  1 
ATOM   3674 C CG  . GLN   B 1 243 ? -11.478 -23.183 -16.735 1.00 53.50 ?  243 GLN   B CG  1 
ATOM   3675 C CD  . GLN   B 1 243 ? -12.230 -22.221 -15.845 1.00 55.77 ?  243 GLN   B CD  1 
ATOM   3676 O OE1 . GLN   B 1 243 ? -12.972 -21.362 -16.324 1.00 53.54 ?  243 GLN   B OE1 1 
ATOM   3677 N NE2 . GLN   B 1 243 ? -12.029 -22.364 -14.545 1.00 63.21 ?  243 GLN   B NE2 1 
ATOM   3678 N N   . GLY   B 1 244 ? -7.584  -22.741 -19.674 1.00 41.01 ?  244 GLY   B N   1 
ATOM   3679 C CA  . GLY   B 1 244 ? -6.981  -21.991 -20.748 1.00 43.90 ?  244 GLY   B CA  1 
ATOM   3680 C C   . GLY   B 1 244 ? -6.707  -20.537 -20.435 1.00 50.62 ?  244 GLY   B C   1 
ATOM   3681 O O   . GLY   B 1 244 ? -6.394  -19.770 -21.358 1.00 39.66 ?  244 GLY   B O   1 
ATOM   3682 N N   . ARG   B 1 245 ? -6.789  -20.131 -19.169 1.00 38.65 ?  245 ARG   B N   1 
ATOM   3683 C CA  . ARG   B 1 245 ? -6.637  -18.728 -18.815 1.00 36.28 ?  245 ARG   B CA  1 
ATOM   3684 C C   . ARG   B 1 245 ? -5.171  -18.403 -18.529 1.00 36.49 ?  245 ARG   B C   1 
ATOM   3685 O O   . ARG   B 1 245 ? -4.376  -19.270 -18.163 1.00 35.96 ?  245 ARG   B O   1 
ATOM   3686 C CB  . ARG   B 1 245 ? -7.538  -18.382 -17.624 1.00 35.99 ?  245 ARG   B CB  1 
ATOM   3687 C CG  . ARG   B 1 245 ? -9.058  -18.452 -17.954 1.00 36.49 ?  245 ARG   B CG  1 
ATOM   3688 C CD  . ARG   B 1 245 ? -9.962  -18.309 -16.712 1.00 38.07 ?  245 ARG   B CD  1 
ATOM   3689 N NE  . ARG   B 1 245 ? -9.445  -19.078 -15.582 1.00 46.01 ?  245 ARG   B NE  1 
ATOM   3690 C CZ  . ARG   B 1 245 ? -9.963  -19.065 -14.357 1.00 44.56 ?  245 ARG   B CZ  1 
ATOM   3691 N NH1 . ARG   B 1 245 ? -9.410  -19.795 -13.399 1.00 41.45 ?  245 ARG   B NH1 1 
ATOM   3692 N NH2 . ARG   B 1 245 ? -11.027 -18.328 -14.087 1.00 34.38 ?  245 ARG   B NH2 1 
ATOM   3693 N N   . LEU   B 1 246 ? -4.806  -17.144 -18.728 1.00 28.89 ?  246 LEU   B N   1 
ATOM   3694 C CA  . LEU   B 1 246 ? -3.411  -16.760 -18.574 1.00 27.97 ?  246 LEU   B CA  1 
ATOM   3695 C C   . LEU   B 1 246 ? -3.097  -16.464 -17.112 1.00 32.12 ?  246 LEU   B C   1 
ATOM   3696 O O   . LEU   B 1 246 ? -3.778  -15.661 -16.465 1.00 32.45 ?  246 LEU   B O   1 
ATOM   3697 C CB  . LEU   B 1 246 ? -3.088  -15.551 -19.452 1.00 30.16 ?  246 LEU   B CB  1 
ATOM   3698 C CG  . LEU   B 1 246 ? -1.600  -15.164 -19.487 1.00 35.69 ?  246 LEU   B CG  1 
ATOM   3699 C CD1 . LEU   B 1 246 ? -0.759  -16.272 -20.176 1.00 32.60 ?  246 LEU   B CD1 1 
ATOM   3700 C CD2 . LEU   B 1 246 ? -1.396  -13.792 -20.142 1.00 26.64 ?  246 LEU   B CD2 1 
ATOM   3701 N N   . CYS   B 1 247 ? -2.035  -17.079 -16.603 1.00 31.23 ?  247 CYS   B N   1 
ATOM   3702 C CA  . CYS   B 1 247 ? -1.630  -16.906 -15.211 1.00 32.90 ?  247 CYS   B CA  1 
ATOM   3703 C C   . CYS   B 1 247 ? -0.439  -15.961 -15.168 1.00 35.31 ?  247 CYS   B C   1 
ATOM   3704 O O   . CYS   B 1 247 ? 0.653   -16.307 -15.625 1.00 34.39 ?  247 CYS   B O   1 
ATOM   3705 C CB  . CYS   B 1 247 ? -1.293  -18.250 -14.569 1.00 38.82 ?  247 CYS   B CB  1 
ATOM   3706 S SG  . CYS   B 1 247 ? -2.701  -19.354 -14.581 1.00 48.56 ?  247 CYS   B SG  1 
ATOM   3707 N N   . LEU   B 1 248 ? -0.659  -14.779 -14.605 1.00 32.51 ?  248 LEU   B N   1 
ATOM   3708 C CA  . LEU   B 1 248 ? 0.339   -13.729 -14.486 1.00 32.69 ?  248 LEU   B CA  1 
ATOM   3709 C C   . LEU   B 1 248 ? 0.937   -13.719 -13.089 1.00 36.62 ?  248 LEU   B C   1 
ATOM   3710 O O   . LEU   B 1 248 ? 0.200   -13.730 -12.103 1.00 36.54 ?  248 LEU   B O   1 
ATOM   3711 C CB  . LEU   B 1 248 ? -0.304  -12.367 -14.743 1.00 27.77 ?  248 LEU   B CB  1 
ATOM   3712 C CG  . LEU   B 1 248 ? -0.560  -11.856 -16.140 1.00 40.51 ?  248 LEU   B CG  1 
ATOM   3713 C CD1 . LEU   B 1 248 ? -1.332  -10.535 -16.003 1.00 41.84 ?  248 LEU   B CD1 1 
ATOM   3714 C CD2 . LEU   B 1 248 ? 0.775   -11.607 -16.806 1.00 40.12 ?  248 LEU   B CD2 1 
ATOM   3715 N N   . ASP   B 1 249 ? 2.260   -13.650 -13.004 1.00 28.64 ?  249 ASP   B N   1 
ATOM   3716 C CA  . ASP   B 1 249 ? 2.927   -13.274 -11.760 1.00 32.15 ?  249 ASP   B CA  1 
ATOM   3717 C C   . ASP   B 1 249 ? 2.903   -11.748 -11.670 1.00 32.20 ?  249 ASP   B C   1 
ATOM   3718 O O   . ASP   B 1 249 ? 3.533   -11.074 -12.487 1.00 36.44 ?  249 ASP   B O   1 
ATOM   3719 C CB  . ASP   B 1 249 ? 4.359   -13.808 -11.776 1.00 32.04 ?  249 ASP   B CB  1 
ATOM   3720 C CG  . ASP   B 1 249 ? 5.168   -13.420 -10.531 1.00 54.89 ?  249 ASP   B CG  1 
ATOM   3721 O OD1 . ASP   B 1 249 ? 5.221   -12.216 -10.175 1.00 60.89 ?  249 ASP   B OD1 1 
ATOM   3722 O OD2 . ASP   B 1 249 ? 5.835   -14.327 -9.960  1.00 68.50 -1 249 ASP   B OD2 1 
ATOM   3723 N N   . VAL   B 1 250 ? 2.173   -11.195 -10.708 1.00 29.42 ?  250 VAL   B N   1 
ATOM   3724 C CA  . VAL   B 1 250 ? 2.143   -9.756  -10.464 1.00 32.64 ?  250 VAL   B CA  1 
ATOM   3725 C C   . VAL   B 1 250 ? 2.592   -9.539  -9.028  1.00 42.23 ?  250 VAL   B C   1 
ATOM   3726 O O   . VAL   B 1 250 ? 1.893   -9.944  -8.086  1.00 34.87 ?  250 VAL   B O   1 
ATOM   3727 C CB  . VAL   B 1 250 ? 0.752   -9.139  -10.677 1.00 36.66 ?  250 VAL   B CB  1 
ATOM   3728 C CG1 . VAL   B 1 250 ? 0.805   -7.616  -10.407 1.00 34.62 ?  250 VAL   B CG1 1 
ATOM   3729 C CG2 . VAL   B 1 250 ? 0.224   -9.431  -12.056 1.00 27.44 ?  250 VAL   B CG2 1 
ATOM   3730 N N   . GLY   B 1 251 ? 3.747   -8.900  -8.848  1.00 38.68 ?  251 GLY   B N   1 
ATOM   3731 C CA  . GLY   B 1 251 ? 4.216   -8.671  -7.495  1.00 33.87 ?  251 GLY   B CA  1 
ATOM   3732 C C   . GLY   B 1 251 ? 4.559   -9.922  -6.723  1.00 42.48 ?  251 GLY   B C   1 
ATOM   3733 O O   . GLY   B 1 251 ? 4.777   -9.840  -5.513  1.00 52.31 ?  251 GLY   B O   1 
ATOM   3734 N N   . GLY   B 1 252 ? 4.622   -11.078 -7.377  1.00 36.58 ?  252 GLY   B N   1 
ATOM   3735 C CA  . GLY   B 1 252 ? 4.851   -12.330 -6.689  1.00 48.68 ?  252 GLY   B CA  1 
ATOM   3736 C C   . GLY   B 1 252 ? 3.608   -13.145 -6.414  1.00 52.55 ?  252 GLY   B C   1 
ATOM   3737 O O   . GLY   B 1 252 ? 3.716   -14.224 -5.817  1.00 53.46 ?  252 GLY   B O   1 
ATOM   3738 N N   . ARG   B 1 253 ? 2.432   -12.663 -6.811  1.00 48.20 ?  253 ARG   B N   1 
ATOM   3739 C CA  . ARG   B 1 253 ? 1.182   -13.384 -6.619  1.00 40.33 ?  253 ARG   B CA  1 
ATOM   3740 C C   . ARG   B 1 253 ? 0.493   -13.569 -7.961  1.00 37.78 ?  253 ARG   B C   1 
ATOM   3741 O O   . ARG   B 1 253 ? 0.699   -12.802 -8.898  1.00 34.78 ?  253 ARG   B O   1 
ATOM   3742 C CB  . ARG   B 1 253 ? 0.247   -12.640 -5.659  1.00 38.93 ?  253 ARG   B CB  1 
ATOM   3743 C CG  . ARG   B 1 253 ? 0.890   -12.352 -4.319  1.00 52.55 ?  253 ARG   B CG  1 
ATOM   3744 C CD  . ARG   B 1 253 ? 1.432   -13.639 -3.700  1.00 47.26 ?  253 ARG   B CD  1 
ATOM   3745 N NE  . ARG   B 1 253 ? 0.366   -14.592 -3.417  1.00 47.59 ?  253 ARG   B NE  1 
ATOM   3746 C CZ  . ARG   B 1 253 ? -0.389  -14.549 -2.326  1.00 46.07 ?  253 ARG   B CZ  1 
ATOM   3747 N NH1 . ARG   B 1 253 ? -0.184  -13.604 -1.406  1.00 49.31 ?  253 ARG   B NH1 1 
ATOM   3748 N NH2 . ARG   B 1 253 ? -1.333  -15.456 -2.151  1.00 44.45 ?  253 ARG   B NH2 1 
ATOM   3749 N N   . THR   B 1 254 ? -0.342  -14.591 -8.036  1.00 36.26 ?  254 THR   B N   1 
ATOM   3750 C CA  . THR   B 1 254 ? -1.020  -14.943 -9.270  1.00 31.30 ?  254 THR   B CA  1 
ATOM   3751 C C   . THR   B 1 254 ? -2.195  -14.025 -9.553  1.00 31.78 ?  254 THR   B C   1 
ATOM   3752 O O   . THR   B 1 254 ? -3.076  -13.845 -8.708  1.00 38.07 ?  254 THR   B O   1 
ATOM   3753 C CB  . THR   B 1 254 ? -1.521  -16.376 -9.198  1.00 40.66 ?  254 THR   B CB  1 
ATOM   3754 O OG1 . THR   B 1 254 ? -0.459  -17.215 -8.739  1.00 46.21 ?  254 THR   B OG1 1 
ATOM   3755 C CG2 . THR   B 1 254 ? -2.028  -16.840 -10.575 1.00 36.86 ?  254 THR   B CG2 1 
ATOM   3756 N N   . VAL   B 1 255 ? -2.213  -13.463 -10.754 1.00 34.14 ?  255 VAL   B N   1 
ATOM   3757 C CA  . VAL   B 1 255 ? -3.415  -12.895 -11.345 1.00 30.93 ?  255 VAL   B CA  1 
ATOM   3758 C C   . VAL   B 1 255 ? -3.730  -13.721 -12.568 1.00 31.30 ?  255 VAL   B C   1 
ATOM   3759 O O   . VAL   B 1 255 ? -2.829  -14.037 -13.358 1.00 31.39 ?  255 VAL   B O   1 
ATOM   3760 C CB  . VAL   B 1 255 ? -3.239  -11.416 -11.708 1.00 32.51 ?  255 VAL   B CB  1 
ATOM   3761 C CG1 . VAL   B 1 255 ? -4.506  -10.910 -12.293 1.00 27.71 ?  255 VAL   B CG1 1 
ATOM   3762 C CG2 . VAL   B 1 255 ? -2.875  -10.625 -10.457 1.00 29.85 ?  255 VAL   B CG2 1 
ATOM   3763 N N   . VAL   B 1 256 ? -4.994  -14.092 -12.706 1.00 26.04 ?  256 VAL   B N   1 
ATOM   3764 C CA  . VAL   B 1 256 ? -5.475  -14.949 -13.783 1.00 31.48 ?  256 VAL   B CA  1 
ATOM   3765 C C   . VAL   B 1 256 ? -6.347  -14.084 -14.667 1.00 33.26 ?  256 VAL   B C   1 
ATOM   3766 O O   . VAL   B 1 256 ? -7.224  -13.368 -14.161 1.00 27.29 ?  256 VAL   B O   1 
ATOM   3767 C CB  . VAL   B 1 256 ? -6.265  -16.147 -13.224 1.00 28.13 ?  256 VAL   B CB  1 
ATOM   3768 C CG1 . VAL   B 1 256 ? -6.746  -17.031 -14.331 1.00 31.86 ?  256 VAL   B CG1 1 
ATOM   3769 C CG2 . VAL   B 1 256 ? -5.412  -16.922 -12.239 1.00 30.65 ?  256 VAL   B CG2 1 
ATOM   3770 N N   . VAL   B 1 257 ? -6.070  -14.080 -15.969 1.00 30.04 ?  257 VAL   B N   1 
ATOM   3771 C CA  . VAL   B 1 257 ? -6.851  -13.276 -16.907 1.00 36.02 ?  257 VAL   B CA  1 
ATOM   3772 C C   . VAL   B 1 257 ? -7.504  -14.225 -17.899 1.00 35.80 ?  257 VAL   B C   1 
ATOM   3773 O O   . VAL   B 1 257 ? -6.843  -15.116 -18.444 1.00 33.17 ?  257 VAL   B O   1 
ATOM   3774 C CB  . VAL   B 1 257 ? -6.003  -12.200 -17.621 1.00 35.97 ?  257 VAL   B CB  1 
ATOM   3775 C CG1 . VAL   B 1 257 ? -5.533  -11.161 -16.601 1.00 38.91 ?  257 VAL   B CG1 1 
ATOM   3776 C CG2 . VAL   B 1 257 ? -4.808  -12.802 -18.319 1.00 38.96 ?  257 VAL   B CG2 1 
ATOM   3777 N N   . SER   B 1 258 ? -8.810  -14.059 -18.096 1.00 37.44 ?  258 SER   B N   1 
ATOM   3778 C CA  . SER   B 1 258 ? -9.562  -14.966 -18.952 1.00 42.33 ?  258 SER   B CA  1 
ATOM   3779 C C   . SER   B 1 258 ? -9.501  -14.553 -20.413 1.00 43.28 ?  258 SER   B C   1 
ATOM   3780 O O   . SER   B 1 258 ? -9.622  -15.400 -21.301 1.00 50.25 ?  258 SER   B O   1 
ATOM   3781 C CB  . SER   B 1 258 ? -11.026 -15.022 -18.506 1.00 41.71 ?  258 SER   B CB  1 
ATOM   3782 O OG  . SER   B 1 258 ? -11.715 -13.877 -19.006 1.00 46.12 ?  258 SER   B OG  1 
ATOM   3783 N N   . ALA   B 1 259 ? -9.302  -13.271 -20.679 1.00 44.76 ?  259 ALA   B N   1 
ATOM   3784 C CA  . ALA   B 1 259 ? -9.339  -12.759 -22.036 1.00 50.63 ?  259 ALA   B CA  1 
ATOM   3785 C C   . ALA   B 1 259 ? -8.688  -11.393 -22.017 1.00 55.72 ?  259 ALA   B C   1 
ATOM   3786 O O   . ALA   B 1 259 ? -8.583  -10.752 -20.969 1.00 57.80 ?  259 ALA   B O   1 
ATOM   3787 C CB  . ALA   B 1 259 ? -10.769 -12.666 -22.572 1.00 52.22 ?  259 ALA   B CB  1 
ATOM   3788 N N   . GLY   B 1 260 ? -8.257  -10.957 -23.182 1.00 54.03 ?  260 GLY   B N   1 
ATOM   3789 C CA  . GLY   B 1 260 ? -7.638  -9.654  -23.300 1.00 59.65 ?  260 GLY   B CA  1 
ATOM   3790 C C   . GLY   B 1 260 ? -6.618  -9.651  -24.416 1.00 58.32 ?  260 GLY   B C   1 
ATOM   3791 O O   . GLY   B 1 260 ? -6.237  -10.692 -24.954 1.00 49.44 ?  260 GLY   B O   1 
ATOM   3792 N N   . ASP   B 1 261 ? -6.194  -8.442  -24.769 1.00 50.86 ?  261 ASP   B N   1 
ATOM   3793 C CA  . ASP   B 1 261 ? -5.120  -8.243  -25.724 1.00 49.71 ?  261 ASP   B CA  1 
ATOM   3794 C C   . ASP   B 1 261 ? -3.800  -8.259  -24.957 1.00 42.88 ?  261 ASP   B C   1 
ATOM   3795 O O   . ASP   B 1 261 ? -3.578  -7.441  -24.054 1.00 49.34 ?  261 ASP   B O   1 
ATOM   3796 C CB  . ASP   B 1 261 ? -5.325  -6.932  -26.489 1.00 47.58 ?  261 ASP   B CB  1 
ATOM   3797 N N   . VAL   B 1 262 ? -2.939  -9.199  -25.285 1.00 45.51 ?  262 VAL   B N   1 
ATOM   3798 C CA  . VAL   B 1 262 ? -1.655  -9.321  -24.612 1.00 43.65 ?  262 VAL   B CA  1 
ATOM   3799 C C   . VAL   B 1 262 ? -0.614  -8.610  -25.453 1.00 38.48 ?  262 VAL   B C   1 
ATOM   3800 O O   . VAL   B 1 262 ? -0.525  -8.837  -26.666 1.00 47.21 ?  262 VAL   B O   1 
ATOM   3801 C CB  . VAL   B 1 262 ? -1.283  -10.794 -24.375 1.00 46.04 ?  262 VAL   B CB  1 
ATOM   3802 C CG1 . VAL   B 1 262 ? 0.179   -10.926 -24.054 1.00 45.41 ?  262 VAL   B CG1 1 
ATOM   3803 C CG2 . VAL   B 1 262 ? -2.129  -11.356 -23.247 1.00 51.05 ?  262 VAL   B CG2 1 
ATOM   3804 N N   . VAL   B 1 263 ? 0.137   -7.712  -24.816 1.00 36.42 ?  263 VAL   B N   1 
ATOM   3805 C CA  . VAL   B 1 263 ? 1.319   -7.082  -25.394 1.00 37.99 ?  263 VAL   B CA  1 
ATOM   3806 C C   . VAL   B 1 263 ? 2.553   -7.739  -24.783 1.00 34.79 ?  263 VAL   B C   1 
ATOM   3807 O O   . VAL   B 1 263 ? 2.658   -7.865  -23.558 1.00 35.03 ?  263 VAL   B O   1 
ATOM   3808 C CB  . VAL   B 1 263 ? 1.319   -5.563  -25.131 1.00 42.03 ?  263 VAL   B CB  1 
ATOM   3809 C CG1 . VAL   B 1 263 ? 2.548   -4.907  -25.727 1.00 33.41 ?  263 VAL   B CG1 1 
ATOM   3810 C CG2 . VAL   B 1 263 ? 0.035   -4.916  -25.663 1.00 47.18 ?  263 VAL   B CG2 1 
ATOM   3811 N N   . HIS   B 1 264 ? 3.490   -8.150  -25.623 1.00 29.90 ?  264 HIS   B N   1 
ATOM   3812 C CA  . HIS   B 1 264 ? 4.758   -8.687  -25.150 1.00 32.04 ?  264 HIS   B CA  1 
ATOM   3813 C C   . HIS   B 1 264 ? 5.736   -7.529  -24.944 1.00 34.48 ?  264 HIS   B C   1 
ATOM   3814 O O   . HIS   B 1 264 ? 6.045   -6.803  -25.891 1.00 34.10 ?  264 HIS   B O   1 
ATOM   3815 C CB  . HIS   B 1 264 ? 5.316   -9.695  -26.152 1.00 29.56 ?  264 HIS   B CB  1 
ATOM   3816 C CG  . HIS   B 1 264 ? 4.487   -10.934 -26.293 1.00 41.05 ?  264 HIS   B CG  1 
ATOM   3817 N ND1 . HIS   B 1 264 ? 4.719   -11.875 -27.273 1.00 40.93 ?  264 HIS   B ND1 1 
ATOM   3818 C CD2 . HIS   B 1 264 ? 3.439   -11.395 -25.571 1.00 38.61 ?  264 HIS   B CD2 1 
ATOM   3819 C CE1 . HIS   B 1 264 ? 3.854   -12.865 -27.146 1.00 40.17 ?  264 HIS   B CE1 1 
ATOM   3820 N NE2 . HIS   B 1 264 ? 3.068   -12.600 -26.120 1.00 43.10 ?  264 HIS   B NE2 1 
ATOM   3821 N N   . LEU   B 1 265 ? 6.204   -7.351  -23.704 1.00 28.89 ?  265 LEU   B N   1 
ATOM   3822 C CA  . LEU   B 1 265 ? 7.202   -6.340  -23.361 1.00 38.05 ?  265 LEU   B CA  1 
ATOM   3823 C C   . LEU   B 1 265 ? 8.592   -6.933  -23.549 1.00 36.68 ?  265 LEU   B C   1 
ATOM   3824 O O   . LEU   B 1 265 ? 9.207   -6.737  -24.600 1.00 44.77 ?  265 LEU   B O   1 
ATOM   3825 C CB  . LEU   B 1 265 ? 6.971   -5.817  -21.937 1.00 28.40 ?  265 LEU   B CB  1 
ATOM   3826 C CG  . LEU   B 1 265 ? 5.582   -5.168  -21.731 1.00 33.72 ?  265 LEU   B CG  1 
ATOM   3827 C CD1 . LEU   B 1 265 ? 5.329   -4.626  -20.326 1.00 27.63 ?  265 LEU   B CD1 1 
ATOM   3828 C CD2 . LEU   B 1 265 ? 5.404   -4.050  -22.726 1.00 29.38 ?  265 LEU   B CD2 1 
HETATM 3829 C C11 . A1BGE C 2 .   ? -5.000  0.189   9.567   1.00 37.03 ?  301 A1BGE A C11 1 
HETATM 3830 C C02 . A1BGE C 2 .   ? -6.695  -0.886  14.086  1.00 27.56 ?  301 A1BGE A C02 1 
HETATM 3831 C C04 . A1BGE C 2 .   ? -8.313  -0.626  12.403  1.00 30.46 ?  301 A1BGE A C04 1 
HETATM 3832 C C06 . A1BGE C 2 .   ? -6.171  -0.356  11.772  1.00 34.03 ?  301 A1BGE A C06 1 
HETATM 3833 C C07 . A1BGE C 2 .   ? -5.725  -0.613  13.095  1.00 29.25 ?  301 A1BGE A C07 1 
HETATM 3834 C C09 . A1BGE C 2 .   ? -3.954  -0.251  11.884  1.00 31.90 ?  301 A1BGE A C09 1 
HETATM 3835 C C12 . A1BGE C 2 .   ? -3.669  0.882   9.048   1.00 40.82 ?  301 A1BGE A C12 1 
HETATM 3836 C C14 . A1BGE C 2 .   ? -2.847  -0.298  8.505   1.00 38.46 ?  301 A1BGE A C14 1 
HETATM 3837 C C16 . A1BGE C 2 .   ? -3.984  -1.178  7.957   1.00 42.20 ?  301 A1BGE A C16 1 
HETATM 3838 C C17 . A1BGE C 2 .   ? -3.535  -2.636  7.856   1.00 33.29 ?  301 A1BGE A C17 1 
HETATM 3839 C C22 . A1BGE C 2 .   ? -4.632  -6.944  8.525   1.00 45.62 ?  301 A1BGE A C22 1 
HETATM 3840 C C23 . A1BGE C 2 .   ? -4.486  -6.729  10.018  1.00 36.20 ?  301 A1BGE A C23 1 
HETATM 3841 C C24 . A1BGE C 2 .   ? -3.755  -7.839  10.727  1.00 43.31 ?  301 A1BGE A C24 1 
HETATM 3842 C C25 . A1BGE C 2 .   ? -4.461  -8.286  11.943  1.00 33.88 ?  301 A1BGE A C25 1 
HETATM 3843 C C26 . A1BGE C 2 .   ? -3.647  -8.035  13.202  1.00 32.16 ?  301 A1BGE A C26 1 
HETATM 3844 C C27 . A1BGE C 2 .   ? -3.647  -9.278  14.069  1.00 33.60 ?  301 A1BGE A C27 1 
HETATM 3845 C C29 . A1BGE C 2 .   ? -3.203  -10.511 16.220  1.00 29.26 ?  301 A1BGE A C29 1 
HETATM 3846 C C30 . A1BGE C 2 .   ? -2.082  -10.928 15.258  1.00 33.68 ?  301 A1BGE A C30 1 
HETATM 3847 C C31 . A1BGE C 2 .   ? -2.447  -10.236 13.890  1.00 30.37 ?  301 A1BGE A C31 1 
HETATM 3848 C C33 . A1BGE C 2 .   ? -0.237  -9.538  14.620  1.00 39.54 ?  301 A1BGE A C33 1 
HETATM 3849 N N01 . A1BGE C 2 .   ? -6.424  -1.154  15.398  1.00 27.79 ?  301 A1BGE A N01 1 
HETATM 3850 N N03 . A1BGE C 2 .   ? -8.023  -0.894  13.702  1.00 31.02 ?  301 A1BGE A N03 1 
HETATM 3851 N N05 . A1BGE C 2 .   ? -7.483  -0.353  11.389  1.00 34.75 ?  301 A1BGE A N05 1 
HETATM 3852 N N08 . A1BGE C 2 .   ? -4.324  -0.540  13.129  1.00 32.23 ?  301 A1BGE A N08 1 
HETATM 3853 N N10 . A1BGE C 2 .   ? -5.057  -0.127  10.993  1.00 38.64 ?  301 A1BGE A N10 1 
HETATM 3854 N N18 . A1BGE C 2 .   ? -4.504  -3.366  7.134   1.00 27.36 ?  301 A1BGE A N18 1 
HETATM 3855 N N21 . A1BGE C 2 .   ? -5.146  -5.822  7.742   1.00 36.96 ?  301 A1BGE A N21 1 
HETATM 3856 N N32 . A1BGE C 2 .   ? -1.246  -9.463  13.603  1.00 35.35 ?  301 A1BGE A N32 1 
HETATM 3857 N N34 . A1BGE C 2 .   ? -0.740  -10.424 15.624  1.00 34.43 ?  301 A1BGE A N34 1 
HETATM 3858 O O13 . A1BGE C 2 .   ? -4.017  1.743   7.983   1.00 37.34 ?  301 A1BGE A O13 1 
HETATM 3859 O O15 . A1BGE C 2 .   ? -1.970  0.025   7.510   1.00 38.97 ?  301 A1BGE A O15 1 
HETATM 3860 O O20 . A1BGE C 2 .   ? -2.875  -5.097  6.720   1.00 41.63 ?  301 A1BGE A O20 1 
HETATM 3861 O O35 . A1BGE C 2 .   ? 0.840   -8.983  14.612  1.00 36.60 ?  301 A1BGE A O35 1 
HETATM 3862 O O36 . A1BGE C 2 .   ? -4.818  -5.145  5.345   1.00 44.59 ?  301 A1BGE A O36 1 
HETATM 3863 O O37 . A1BGE C 2 .   ? -5.066  -0.996  8.848   1.00 37.50 ?  301 A1BGE A O37 1 
HETATM 3864 S S19 . A1BGE C 2 .   ? -4.275  -4.906  6.628   1.00 43.59 ?  301 A1BGE A S19 1 
HETATM 3865 S S28 . A1BGE C 2 .   ? -3.578  -8.776  15.808  1.00 28.96 ?  301 A1BGE A S28 1 
HETATM 3866 C C11 . A1BGE D 2 .   ? -5.575  -7.505  -37.423 1.00 41.96 ?  301 A1BGE B C11 1 
HETATM 3867 C C02 . A1BGE D 2 .   ? -4.985  -10.352 -41.485 1.00 34.11 ?  301 A1BGE B C02 1 
HETATM 3868 C C04 . A1BGE D 2 .   ? -3.162  -10.286 -40.021 1.00 29.24 ?  301 A1BGE B C04 1 
HETATM 3869 C C06 . A1BGE D 2 .   ? -4.962  -9.047  -39.428 1.00 33.72 ?  301 A1BGE B C06 1 
HETATM 3870 C C07 . A1BGE D 2 .   ? -5.660  -9.474  -40.577 1.00 37.70 ?  301 A1BGE B C07 1 
HETATM 3871 C C09 . A1BGE D 2 .   ? -7.006  -8.148  -39.488 1.00 33.43 ?  301 A1BGE B C09 1 
HETATM 3872 C C12 . A1BGE D 2 .   ? -6.517  -6.226  -37.115 1.00 39.44 ?  301 A1BGE B C12 1 
HETATM 3873 C C14 . A1BGE D 2 .   ? -7.717  -6.874  -36.429 1.00 35.53 ?  301 A1BGE B C14 1 
HETATM 3874 C C16 . A1BGE D 2 .   ? -6.949  -7.902  -35.569 1.00 33.85 ?  301 A1BGE B C16 1 
HETATM 3875 C C17 . A1BGE D 2 .   ? -7.851  -8.990  -35.034 1.00 33.70 ?  301 A1BGE B C17 1 
HETATM 3876 C C22 . A1BGE D 2 .   ? -8.530  -13.245 -34.265 1.00 46.22 ?  301 A1BGE B C22 1 
HETATM 3877 C C23 . A1BGE D 2 .   ? -8.520  -13.503 -35.781 1.00 45.09 ?  301 A1BGE B C23 1 
HETATM 3878 C C24 . A1BGE D 2 .   ? -9.871  -13.989 -36.374 1.00 38.44 ?  301 A1BGE B C24 1 
HETATM 3879 C C25 . A1BGE D 2 .   ? -9.787  -15.287 -37.155 1.00 28.59 ?  301 A1BGE B C25 1 
HETATM 3880 C C26 . A1BGE D 2 .   ? -10.368 -15.203 -38.585 1.00 35.79 ?  301 A1BGE B C26 1 
HETATM 3881 C C27 . A1BGE D 2 .   ? -10.944 -16.550 -38.977 1.00 30.29 ?  301 A1BGE B C27 1 
HETATM 3882 C C29 . A1BGE D 2 .   ? -12.193 -18.036 -40.649 1.00 26.25 ?  301 A1BGE B C29 1 
HETATM 3883 C C30 . A1BGE D 2 .   ? -13.183 -17.724 -39.545 1.00 31.19 ?  301 A1BGE B C30 1 
HETATM 3884 C C31 . A1BGE D 2 .   ? -12.373 -16.853 -38.473 1.00 30.76 ?  301 A1BGE B C31 1 
HETATM 3885 C C33 . A1BGE D 2 .   ? -14.187 -15.574 -39.391 1.00 32.18 ?  301 A1BGE B C33 1 
HETATM 3886 N N01 . A1BGE D 2 .   ? -5.526  -10.832 -42.613 1.00 35.42 ?  301 A1BGE B N01 1 
HETATM 3887 N N03 . A1BGE D 2 .   ? -3.710  -10.754 -41.184 1.00 33.35 ?  301 A1BGE B N03 1 
HETATM 3888 N N05 . A1BGE D 2 .   ? -3.693  -9.444  -39.125 1.00 35.69 ?  301 A1BGE B N05 1 
HETATM 3889 N N08 . A1BGE D 2 .   ? -6.941  -8.879  -40.591 1.00 38.22 ?  301 A1BGE B N08 1 
HETATM 3890 N N10 . A1BGE D 2 .   ? -5.812  -8.205  -38.715 1.00 38.43 ?  301 A1BGE B N10 1 
HETATM 3891 N N18 . A1BGE D 2 .   ? -7.102  -9.750  -34.071 1.00 36.23 ?  301 A1BGE B N18 1 
HETATM 3892 N N21 . A1BGE D 2 .   ? -7.498  -12.366 -33.727 1.00 39.46 ?  301 A1BGE B N21 1 
HETATM 3893 N N32 . A1BGE D 2 .   ? -13.102 -15.614 -38.455 1.00 30.99 ?  301 A1BGE B N32 1 
HETATM 3894 N N34 . A1BGE D 2 .   ? -14.258 -16.847 -40.025 1.00 29.74 ?  301 A1BGE B N34 1 
HETATM 3895 O O13 . A1BGE D 2 .   ? -5.895  -5.424  -36.168 1.00 43.34 ?  301 A1BGE B O13 1 
HETATM 3896 O O15 . A1BGE D 2 .   ? -8.437  -6.016  -35.662 1.00 37.80 ?  301 A1BGE B O15 1 
HETATM 3897 O O20 . A1BGE D 2 .   ? -9.172  -10.491 -33.098 1.00 37.15 ?  301 A1BGE B O20 1 
HETATM 3898 O O35 . A1BGE D 2 .   ? -14.938 -14.653 -39.592 1.00 31.93 ?  301 A1BGE B O35 1 
HETATM 3899 O O36 . A1BGE D 2 .   ? -7.170  -10.830 -31.787 1.00 42.59 ?  301 A1BGE B O36 1 
HETATM 3900 O O37 . A1BGE D 2 .   ? -5.906  -8.395  -36.389 1.00 32.35 ?  301 A1BGE B O37 1 
HETATM 3901 S S19 . A1BGE D 2 .   ? -7.783  -10.848 -33.063 1.00 42.69 ?  301 A1BGE B S19 1 
HETATM 3902 S S28 . A1BGE D 2 .   ? -11.059 -16.633 -40.759 1.00 33.18 ?  301 A1BGE B S28 1 
HETATM 3903 O O   . HOH   E 3 .   ? -10.628 4.014   -8.720  1.00 51.25 ?  401 HOH   A O   1 
HETATM 3904 O O   . HOH   E 3 .   ? -13.386 0.024   1.281   1.00 46.30 ?  402 HOH   A O   1 
HETATM 3905 O O   . HOH   E 3 .   ? -18.929 -18.124 12.228  1.00 39.10 ?  403 HOH   A O   1 
HETATM 3906 O O   . HOH   E 3 .   ? -11.422 9.058   11.196  1.00 49.16 ?  404 HOH   A O   1 
HETATM 3907 O O   . HOH   E 3 .   ? -0.431  -19.760 24.146  1.00 34.71 ?  405 HOH   A O   1 
HETATM 3908 O O   . HOH   E 3 .   ? -11.633 11.900  17.452  1.00 37.91 ?  406 HOH   A O   1 
HETATM 3909 O O   . HOH   E 3 .   ? -11.651 -3.214  25.244  1.00 34.15 ?  407 HOH   A O   1 
HETATM 3910 O O   . HOH   E 3 .   ? -19.614 6.442   16.599  1.00 43.81 ?  408 HOH   A O   1 
HETATM 3911 O O   . HOH   E 3 .   ? -22.241 -8.596  -8.996  1.00 40.00 ?  409 HOH   A O   1 
HETATM 3912 O O   . HOH   E 3 .   ? -0.740  -4.130  17.501  1.00 36.46 ?  410 HOH   A O   1 
HETATM 3913 O O   . HOH   E 3 .   ? -9.593  -28.888 24.901  1.00 46.06 ?  411 HOH   A O   1 
HETATM 3914 O O   . HOH   E 3 .   ? -21.603 -21.057 -1.935  1.00 41.79 ?  412 HOH   A O   1 
HETATM 3915 O O   . HOH   E 3 .   ? -24.739 -17.880 0.292   1.00 42.78 ?  413 HOH   A O   1 
HETATM 3916 O O   . HOH   E 3 .   ? -6.519  -9.071  23.797  1.00 26.70 ?  414 HOH   A O   1 
HETATM 3917 O O   . HOH   E 3 .   ? -8.552  1.101   9.101   1.00 36.11 ?  415 HOH   A O   1 
HETATM 3918 O O   . HOH   E 3 .   ? 6.684   -26.847 14.757  1.00 36.59 ?  416 HOH   A O   1 
HETATM 3919 O O   . HOH   E 3 .   ? 6.465   -10.406 19.806  1.00 46.88 ?  417 HOH   A O   1 
HETATM 3920 O O   . HOH   E 3 .   ? -7.431  -21.199 -0.632  1.00 44.90 ?  418 HOH   A O   1 
HETATM 3921 O O   . HOH   E 3 .   ? -21.352 -23.952 -1.021  1.00 43.35 ?  419 HOH   A O   1 
HETATM 3922 O O   . HOH   E 3 .   ? -23.324 -5.513  -13.406 1.00 47.14 ?  420 HOH   A O   1 
HETATM 3923 O O   . HOH   E 3 .   ? -13.446 -35.966 8.800   1.00 35.70 ?  421 HOH   A O   1 
HETATM 3924 O O   . HOH   E 3 .   ? -14.278 7.856   18.418  1.00 36.93 ?  422 HOH   A O   1 
HETATM 3925 O O   . HOH   E 3 .   ? -15.687 -10.140 0.877   1.00 30.14 ?  423 HOH   A O   1 
HETATM 3926 O O   . HOH   E 3 .   ? -6.052  -8.330  4.766   1.00 43.67 ?  424 HOH   A O   1 
HETATM 3927 O O   . HOH   E 3 .   ? 0.702   -1.042  18.536  1.00 31.94 ?  425 HOH   A O   1 
HETATM 3928 O O   . HOH   E 3 .   ? -5.891  -4.431  23.043  1.00 37.49 ?  426 HOH   A O   1 
HETATM 3929 O O   . HOH   E 3 .   ? 6.958   -22.792 6.454   1.00 38.43 ?  427 HOH   A O   1 
HETATM 3930 O O   . HOH   E 3 .   ? -1.670  1.187   25.948  1.00 39.83 ?  428 HOH   A O   1 
HETATM 3931 O O   . HOH   E 3 .   ? 1.927   -1.865  16.785  1.00 39.77 ?  429 HOH   A O   1 
HETATM 3932 O O   . HOH   E 3 .   ? -4.301  -13.228 5.903   1.00 37.95 ?  430 HOH   A O   1 
HETATM 3933 O O   . HOH   E 3 .   ? -11.347 -19.001 -10.842 1.00 41.17 ?  431 HOH   A O   1 
HETATM 3934 O O   . HOH   E 3 .   ? -3.941  -23.564 28.746  1.00 37.38 ?  432 HOH   A O   1 
HETATM 3935 O O   . HOH   E 3 .   ? 7.571   -27.793 1.351   1.00 49.92 ?  433 HOH   A O   1 
HETATM 3936 O O   . HOH   E 3 .   ? -20.623 -22.099 11.815  1.00 38.37 ?  434 HOH   A O   1 
HETATM 3937 O O   . HOH   E 3 .   ? -3.388  -20.356 -10.996 1.00 51.64 ?  435 HOH   A O   1 
HETATM 3938 O O   . HOH   E 3 .   ? -8.247  -1.211  34.196  1.00 50.45 ?  436 HOH   A O   1 
HETATM 3939 O O   . HOH   E 3 .   ? -0.728  0.710   11.881  1.00 40.38 ?  437 HOH   A O   1 
HETATM 3940 O O   . HOH   E 3 .   ? -15.976 -24.814 23.717  1.00 46.89 ?  438 HOH   A O   1 
HETATM 3941 O O   . HOH   E 3 .   ? -15.416 -27.234 27.357  1.00 49.45 ?  439 HOH   A O   1 
HETATM 3942 O O   . HOH   E 3 .   ? 6.366   -4.103  12.817  1.00 51.20 ?  440 HOH   A O   1 
HETATM 3943 O O   . HOH   E 3 .   ? 5.417   -3.344  10.760  1.00 39.70 ?  441 HOH   A O   1 
HETATM 3944 O O   . HOH   E 3 .   ? 4.506   -30.993 15.521  1.00 50.93 ?  442 HOH   A O   1 
HETATM 3945 O O   . HOH   F 3 .   ? -5.981  -36.467 -39.898 1.00 36.46 ?  401 HOH   B O   1 
HETATM 3946 O O   . HOH   F 3 .   ? -19.205 -27.664 -52.000 1.00 31.69 ?  402 HOH   B O   1 
HETATM 3947 O O   . HOH   F 3 .   ? 0.890   -18.286 -25.513 1.00 36.25 ?  403 HOH   B O   1 
HETATM 3948 O O   . HOH   F 3 .   ? 8.394   -16.570 -24.021 1.00 40.91 ?  404 HOH   B O   1 
HETATM 3949 O O   . HOH   F 3 .   ? 10.302  -9.572  -13.499 1.00 41.12 ?  405 HOH   B O   1 
HETATM 3950 O O   . HOH   F 3 .   ? -19.011 -27.280 -45.738 1.00 33.20 ?  406 HOH   B O   1 
HETATM 3951 O O   . HOH   F 3 .   ? -10.697 -5.345  -36.698 1.00 44.55 ?  407 HOH   B O   1 
HETATM 3952 O O   . HOH   F 3 .   ? 7.774   -14.065 -33.400 1.00 40.13 ?  408 HOH   B O   1 
HETATM 3953 O O   . HOH   F 3 .   ? -12.027 -9.051  -45.582 1.00 39.16 ?  409 HOH   B O   1 
HETATM 3954 O O   . HOH   F 3 .   ? -3.665  -11.281 -26.773 1.00 40.23 ?  410 HOH   B O   1 
HETATM 3955 O O   . HOH   F 3 .   ? -3.895  -35.816 -38.164 1.00 36.07 ?  411 HOH   B O   1 
HETATM 3956 O O   . HOH   F 3 .   ? -14.136 -7.598  -40.760 1.00 35.32 ?  412 HOH   B O   1 
HETATM 3957 O O   . HOH   F 3 .   ? -0.517  -29.722 -34.428 1.00 47.76 ?  413 HOH   B O   1 
HETATM 3958 O O   . HOH   F 3 .   ? -25.398 -28.727 -23.864 1.00 39.64 ?  414 HOH   B O   1 
HETATM 3959 O O   . HOH   F 3 .   ? -21.533 -14.880 -43.877 1.00 42.43 ?  415 HOH   B O   1 
HETATM 3960 O O   . HOH   F 3 .   ? -12.152 -11.923 -43.507 1.00 36.04 ?  416 HOH   B O   1 
HETATM 3961 O O   . HOH   F 3 .   ? -9.116  -19.872 -48.353 1.00 36.45 ?  417 HOH   B O   1 
HETATM 3962 O O   . HOH   F 3 .   ? -24.712 -17.148 -38.017 1.00 36.24 ?  418 HOH   B O   1 
HETATM 3963 O O   . HOH   F 3 .   ? -8.477  -15.532 -48.833 1.00 36.83 ?  419 HOH   B O   1 
HETATM 3964 O O   . HOH   F 3 .   ? -27.323 -32.549 -40.725 1.00 44.95 ?  420 HOH   B O   1 
HETATM 3965 O O   . HOH   F 3 .   ? 6.536   -28.922 -22.799 1.00 42.87 ?  421 HOH   B O   1 
HETATM 3966 O O   . HOH   F 3 .   ? -3.316  2.086   -22.337 1.00 51.26 ?  422 HOH   B O   1 
HETATM 3967 O O   . HOH   F 3 .   ? -9.854  -6.425  -39.491 1.00 37.98 ?  423 HOH   B O   1 
HETATM 3968 O O   . HOH   F 3 .   ? -14.831 -33.140 -35.103 1.00 50.49 ?  424 HOH   B O   1 
HETATM 3969 O O   . HOH   F 3 .   ? -21.837 -25.445 -48.954 1.00 59.26 ?  425 HOH   B O   1 
HETATM 3970 O O   . HOH   F 3 .   ? -12.688 -38.863 -34.824 1.00 50.83 ?  426 HOH   B O   1 
HETATM 3971 O O   . HOH   F 3 .   ? -2.193  -21.235 -54.011 1.00 45.04 ?  427 HOH   B O   1 
HETATM 3972 O O   . HOH   F 3 .   ? -23.584 -27.118 -48.350 1.00 58.01 ?  428 HOH   B O   1 
HETATM 3973 O O   . HOH   F 3 .   ? -7.637  -14.117 -30.110 1.00 49.65 ?  429 HOH   B O   1 
HETATM 3974 O O   . HOH   F 3 .   ? -24.940 -15.323 -39.661 1.00 46.09 ?  430 HOH   B O   1 
# 
