data_9FT7
# 
_entry.id   9FT7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9FT7         pdb_00009ft7 10.2210/pdb9ft7/pdb 
WWPDB D_1292139584 ?            ?                   
EMDB  EMD-50741    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'EM metadata'     1 0 2025-03-05 ? 
3 FSC               1 0 2025-03-05 ? 
4 'Half map'        1 0 2025-03-05 1 
5 'Half map'        1 0 2025-03-05 2 
6 Image             1 0 2025-03-05 ? 
7 Mask              1 0 2025-03-05 1 
8 Mask              1 0 2025-03-05 2 
9 'Primary map'     1 0 2025-03-05 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 Mask              repository 'Initial release' ? ? 
8 8 Mask              repository 'Initial release' ? ? 
9 9 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FT7 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        
'Structure of the human two pore domain potassium ion channel THIK-1 (K2P13.1) in a closed conformation' 
_pdbx_database_related.db_id          EMD-50741 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              stephen.tucker@physics.ox.ac.uk 
_pdbx_contact_author.name_first         Tucker 
_pdbx_contact_author.name_last          Stephen 
_pdbx_contact_author.name_mi            J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8996-2000 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rodstrom, K.E.J.' 1 0000-0002-2952-0400 
'Tucker, S.J.'     2 0000-0001-8996-2000 
# 
_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            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Cryo-EM structure of the human THIK-1 K2P K + channel reveals a lower Y gate regulated by lipids and anesthetics.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-025-01497-6 
_citation.pdbx_database_id_PubMed   40011745 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rodstrom, K.E.J.'    1  ?                   
primary 'Eymsh, B.'           2  ?                   
primary 'Proks, P.'           3  ?                   
primary 'Hayre, M.S.'         4  0000-0002-4067-8233 
primary 'Cordeiro, S.'        5  ?                   
primary 'Mendez-Otalvaro, E.' 6  ?                   
primary 'Madry, C.'           7  ?                   
primary 'Rowland, A.'         8  ?                   
primary 'Kopec, W.'           9  0000-0001-8801-9563 
primary 'Newstead, S.'        10 0000-0001-7432-2270 
primary 'Baukrowitz, T.'      11 0000-0003-4562-0505 
primary 'Schewe, M.'          12 0000-0002-6192-5651 
primary 'Tucker, S.J.'        13 0000-0001-8996-2000 
# 
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 'Potassium channel subfamily K member 13' 33637.980 2 ? ? ? 'K2P13.1 residues G9-G297' 
2 non-polymer syn 'LINOLEIC ACID'                           280.445   2 ? ? ? ?                          
3 non-polymer syn 'POTASSIUM ION'                           39.098    2 ? ? ? ?                          
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Tandem pore domain halothane-inhibited potassium channel 1,THIK-1' 
# 
_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       
;MGPGHLNEDNARFLLLAALIVLYLLGGAAVFSALELAHERQAKQRWEERLANFSRGHNLSRDELRGFLRHYEEATRAGIR
VDNVRPRWDFTGAFYFVGTVVSTIGFGMTTPATVGGKIFLIFYGLVGCSSTILFFNLFLERLITIIAYIMKSCHQRQLRR
RGALPQESLKDAGQCEVDSLAGWKPSVYYVMLILCTASILISCCASAMYTPIEGWSYFDSLYFCFVAFSTIGFGDLVSSQ
NAHYESQGLYRFANFVFILMGVCCIYSLFNVISILIKQSLNWILRKMDSGAELEVLFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGPGHLNEDNARFLLLAALIVLYLLGGAAVFSALELAHERQAKQRWEERLANFSRGHNLSRDELRGFLRHYEEATRAGIR
VDNVRPRWDFTGAFYFVGTVVSTIGFGMTTPATVGGKIFLIFYGLVGCSSTILFFNLFLERLITIIAYIMKSCHQRQLRR
RGALPQESLKDAGQCEVDSLAGWKPSVYYVMLILCTASILISCCASAMYTPIEGWSYFDSLYFCFVAFSTIGFGDLVSSQ
NAHYESQGLYRFANFVFILMGVCCIYSLFNVISILIKQSLNWILRKMDSGAELEVLFQ
;
_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 'LINOLEIC ACID' EIC 
3 'POTASSIUM ION' K   
# 
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   GLY n 
1 3   PRO n 
1 4   GLY n 
1 5   HIS n 
1 6   LEU n 
1 7   ASN n 
1 8   GLU n 
1 9   ASP n 
1 10  ASN n 
1 11  ALA n 
1 12  ARG n 
1 13  PHE n 
1 14  LEU n 
1 15  LEU n 
1 16  LEU n 
1 17  ALA n 
1 18  ALA n 
1 19  LEU n 
1 20  ILE n 
1 21  VAL n 
1 22  LEU n 
1 23  TYR n 
1 24  LEU n 
1 25  LEU n 
1 26  GLY n 
1 27  GLY n 
1 28  ALA n 
1 29  ALA n 
1 30  VAL n 
1 31  PHE n 
1 32  SER n 
1 33  ALA n 
1 34  LEU n 
1 35  GLU n 
1 36  LEU n 
1 37  ALA n 
1 38  HIS n 
1 39  GLU n 
1 40  ARG n 
1 41  GLN n 
1 42  ALA n 
1 43  LYS n 
1 44  GLN n 
1 45  ARG n 
1 46  TRP n 
1 47  GLU n 
1 48  GLU n 
1 49  ARG n 
1 50  LEU n 
1 51  ALA n 
1 52  ASN n 
1 53  PHE n 
1 54  SER n 
1 55  ARG n 
1 56  GLY n 
1 57  HIS n 
1 58  ASN n 
1 59  LEU n 
1 60  SER n 
1 61  ARG n 
1 62  ASP n 
1 63  GLU n 
1 64  LEU n 
1 65  ARG n 
1 66  GLY n 
1 67  PHE n 
1 68  LEU n 
1 69  ARG n 
1 70  HIS n 
1 71  TYR n 
1 72  GLU n 
1 73  GLU n 
1 74  ALA n 
1 75  THR n 
1 76  ARG n 
1 77  ALA n 
1 78  GLY n 
1 79  ILE n 
1 80  ARG n 
1 81  VAL n 
1 82  ASP n 
1 83  ASN n 
1 84  VAL n 
1 85  ARG n 
1 86  PRO n 
1 87  ARG n 
1 88  TRP n 
1 89  ASP n 
1 90  PHE n 
1 91  THR n 
1 92  GLY n 
1 93  ALA n 
1 94  PHE n 
1 95  TYR n 
1 96  PHE n 
1 97  VAL n 
1 98  GLY n 
1 99  THR n 
1 100 VAL n 
1 101 VAL n 
1 102 SER n 
1 103 THR n 
1 104 ILE n 
1 105 GLY n 
1 106 PHE n 
1 107 GLY n 
1 108 MET n 
1 109 THR n 
1 110 THR n 
1 111 PRO n 
1 112 ALA n 
1 113 THR n 
1 114 VAL n 
1 115 GLY n 
1 116 GLY n 
1 117 LYS n 
1 118 ILE n 
1 119 PHE n 
1 120 LEU n 
1 121 ILE n 
1 122 PHE n 
1 123 TYR n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 CYS n 
1 129 SER n 
1 130 SER n 
1 131 THR n 
1 132 ILE n 
1 133 LEU n 
1 134 PHE n 
1 135 PHE n 
1 136 ASN n 
1 137 LEU n 
1 138 PHE n 
1 139 LEU n 
1 140 GLU n 
1 141 ARG n 
1 142 LEU n 
1 143 ILE n 
1 144 THR n 
1 145 ILE n 
1 146 ILE n 
1 147 ALA n 
1 148 TYR n 
1 149 ILE n 
1 150 MET n 
1 151 LYS n 
1 152 SER n 
1 153 CYS n 
1 154 HIS n 
1 155 GLN n 
1 156 ARG n 
1 157 GLN n 
1 158 LEU n 
1 159 ARG n 
1 160 ARG n 
1 161 ARG n 
1 162 GLY n 
1 163 ALA n 
1 164 LEU n 
1 165 PRO n 
1 166 GLN n 
1 167 GLU n 
1 168 SER n 
1 169 LEU n 
1 170 LYS n 
1 171 ASP n 
1 172 ALA n 
1 173 GLY n 
1 174 GLN n 
1 175 CYS n 
1 176 GLU n 
1 177 VAL n 
1 178 ASP n 
1 179 SER n 
1 180 LEU n 
1 181 ALA n 
1 182 GLY n 
1 183 TRP n 
1 184 LYS n 
1 185 PRO n 
1 186 SER n 
1 187 VAL n 
1 188 TYR n 
1 189 TYR n 
1 190 VAL n 
1 191 MET n 
1 192 LEU n 
1 193 ILE n 
1 194 LEU n 
1 195 CYS n 
1 196 THR n 
1 197 ALA n 
1 198 SER n 
1 199 ILE n 
1 200 LEU n 
1 201 ILE n 
1 202 SER n 
1 203 CYS n 
1 204 CYS n 
1 205 ALA n 
1 206 SER n 
1 207 ALA n 
1 208 MET n 
1 209 TYR n 
1 210 THR n 
1 211 PRO n 
1 212 ILE n 
1 213 GLU n 
1 214 GLY n 
1 215 TRP n 
1 216 SER n 
1 217 TYR n 
1 218 PHE n 
1 219 ASP n 
1 220 SER n 
1 221 LEU n 
1 222 TYR n 
1 223 PHE n 
1 224 CYS n 
1 225 PHE n 
1 226 VAL n 
1 227 ALA n 
1 228 PHE n 
1 229 SER n 
1 230 THR n 
1 231 ILE n 
1 232 GLY n 
1 233 PHE n 
1 234 GLY n 
1 235 ASP n 
1 236 LEU n 
1 237 VAL n 
1 238 SER n 
1 239 SER n 
1 240 GLN n 
1 241 ASN n 
1 242 ALA n 
1 243 HIS n 
1 244 TYR n 
1 245 GLU n 
1 246 SER n 
1 247 GLN n 
1 248 GLY n 
1 249 LEU n 
1 250 TYR n 
1 251 ARG n 
1 252 PHE n 
1 253 ALA n 
1 254 ASN n 
1 255 PHE n 
1 256 VAL n 
1 257 PHE n 
1 258 ILE n 
1 259 LEU n 
1 260 MET n 
1 261 GLY n 
1 262 VAL n 
1 263 CYS n 
1 264 CYS n 
1 265 ILE n 
1 266 TYR n 
1 267 SER n 
1 268 LEU n 
1 269 PHE n 
1 270 ASN n 
1 271 VAL n 
1 272 ILE n 
1 273 SER n 
1 274 ILE n 
1 275 LEU n 
1 276 ILE n 
1 277 LYS n 
1 278 GLN n 
1 279 SER n 
1 280 LEU n 
1 281 ASN n 
1 282 TRP n 
1 283 ILE n 
1 284 LEU n 
1 285 ARG n 
1 286 LYS n 
1 287 MET n 
1 288 ASP n 
1 289 SER n 
1 290 GLY n 
1 291 ALA n 
1 292 GLU n 
1 293 LEU n 
1 294 GLU n 
1 295 VAL n 
1 296 LEU n 
1 297 PHE n 
1 298 GLN 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                   298 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 KCNK13 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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            Sf9 
_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          Baculovirus 
_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 
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 
EIC non-polymer         . 'LINOLEIC ACID' '9,12-LINOLEIC ACID' 'C18 H32 O2'     280.445 
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 
ILE 'L-peptide linking' y ISOLEUCINE      ?                    'C6 H13 N O2'    131.173 
K   non-polymer         . 'POTASSIUM ION' ?                    'K 1'            39.098  
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   8   ?   ?   ?   A . n 
A 1 2   GLY 2   9   ?   ?   ?   A . n 
A 1 3   PRO 3   10  ?   ?   ?   A . n 
A 1 4   GLY 4   11  ?   ?   ?   A . n 
A 1 5   HIS 5   12  ?   ?   ?   A . n 
A 1 6   LEU 6   13  ?   ?   ?   A . n 
A 1 7   ASN 7   14  14  ASN ASN A . n 
A 1 8   GLU 8   15  15  GLU GLU A . n 
A 1 9   ASP 9   16  16  ASP ASP A . n 
A 1 10  ASN 10  17  17  ASN ASN A . n 
A 1 11  ALA 11  18  18  ALA ALA A . n 
A 1 12  ARG 12  19  19  ARG ARG A . n 
A 1 13  PHE 13  20  20  PHE PHE A . n 
A 1 14  LEU 14  21  21  LEU LEU A . n 
A 1 15  LEU 15  22  22  LEU LEU A . n 
A 1 16  LEU 16  23  23  LEU LEU A . n 
A 1 17  ALA 17  24  24  ALA ALA A . n 
A 1 18  ALA 18  25  25  ALA ALA A . n 
A 1 19  LEU 19  26  26  LEU LEU A . n 
A 1 20  ILE 20  27  27  ILE ILE A . n 
A 1 21  VAL 21  28  28  VAL VAL A . n 
A 1 22  LEU 22  29  29  LEU LEU A . n 
A 1 23  TYR 23  30  30  TYR TYR A . n 
A 1 24  LEU 24  31  31  LEU LEU A . n 
A 1 25  LEU 25  32  32  LEU LEU A . n 
A 1 26  GLY 26  33  33  GLY GLY A . n 
A 1 27  GLY 27  34  34  GLY GLY A . n 
A 1 28  ALA 28  35  35  ALA ALA A . n 
A 1 29  ALA 29  36  36  ALA ALA A . n 
A 1 30  VAL 30  37  37  VAL VAL A . n 
A 1 31  PHE 31  38  38  PHE PHE A . n 
A 1 32  SER 32  39  39  SER SER A . n 
A 1 33  ALA 33  40  40  ALA ALA A . n 
A 1 34  LEU 34  41  41  LEU LEU A . n 
A 1 35  GLU 35  42  42  GLU GLU A . n 
A 1 36  LEU 36  43  43  LEU LEU A . n 
A 1 37  ALA 37  44  44  ALA ALA A . n 
A 1 38  HIS 38  45  45  HIS HIS A . n 
A 1 39  GLU 39  46  46  GLU GLU A . n 
A 1 40  ARG 40  47  47  ARG ARG A . n 
A 1 41  GLN 41  48  48  GLN GLN A . n 
A 1 42  ALA 42  49  49  ALA ALA A . n 
A 1 43  LYS 43  50  50  LYS LYS A . n 
A 1 44  GLN 44  51  51  GLN GLN A . n 
A 1 45  ARG 45  52  52  ARG ARG A . n 
A 1 46  TRP 46  53  53  TRP TRP A . n 
A 1 47  GLU 47  54  54  GLU GLU A . n 
A 1 48  GLU 48  55  55  GLU GLU A . n 
A 1 49  ARG 49  56  56  ARG ARG A . n 
A 1 50  LEU 50  57  57  LEU LEU A . n 
A 1 51  ALA 51  58  58  ALA ALA A . n 
A 1 52  ASN 52  59  59  ASN ASN A . n 
A 1 53  PHE 53  60  60  PHE PHE A . n 
A 1 54  SER 54  61  61  SER SER A . n 
A 1 55  ARG 55  62  62  ARG ARG A . n 
A 1 56  GLY 56  63  63  GLY GLY A . n 
A 1 57  HIS 57  64  64  HIS HIS A . n 
A 1 58  ASN 58  65  65  ASN ASN A . n 
A 1 59  LEU 59  66  66  LEU LEU A . n 
A 1 60  SER 60  67  67  SER SER A . n 
A 1 61  ARG 61  68  68  ARG ARG A . n 
A 1 62  ASP 62  69  69  ASP ASP A . n 
A 1 63  GLU 63  70  70  GLU GLU A . n 
A 1 64  LEU 64  71  71  LEU LEU A . n 
A 1 65  ARG 65  72  72  ARG ARG A . n 
A 1 66  GLY 66  73  73  GLY GLY A . n 
A 1 67  PHE 67  74  74  PHE PHE A . n 
A 1 68  LEU 68  75  75  LEU LEU A . n 
A 1 69  ARG 69  76  76  ARG ARG A . n 
A 1 70  HIS 70  77  77  HIS HIS A . n 
A 1 71  TYR 71  78  78  TYR TYR A . n 
A 1 72  GLU 72  79  79  GLU GLU A . n 
A 1 73  GLU 73  80  80  GLU GLU A . n 
A 1 74  ALA 74  81  81  ALA ALA A . n 
A 1 75  THR 75  82  82  THR THR A . n 
A 1 76  ARG 76  83  83  ARG ARG A . n 
A 1 77  ALA 77  84  84  ALA ALA A . n 
A 1 78  GLY 78  85  85  GLY GLY A . n 
A 1 79  ILE 79  86  86  ILE ILE A . n 
A 1 80  ARG 80  87  87  ARG ARG A . n 
A 1 81  VAL 81  88  88  VAL VAL A . n 
A 1 82  ASP 82  89  89  ASP ASP A . n 
A 1 83  ASN 83  90  90  ASN ASN A . n 
A 1 84  VAL 84  91  91  VAL VAL A . n 
A 1 85  ARG 85  92  92  ARG ARG A . n 
A 1 86  PRO 86  93  93  PRO PRO A . n 
A 1 87  ARG 87  94  94  ARG ARG A . n 
A 1 88  TRP 88  95  95  TRP TRP A . n 
A 1 89  ASP 89  96  96  ASP ASP A . n 
A 1 90  PHE 90  97  97  PHE PHE A . n 
A 1 91  THR 91  98  98  THR THR A . n 
A 1 92  GLY 92  99  99  GLY GLY A . n 
A 1 93  ALA 93  100 100 ALA ALA A . n 
A 1 94  PHE 94  101 101 PHE PHE A . n 
A 1 95  TYR 95  102 102 TYR TYR A . n 
A 1 96  PHE 96  103 103 PHE PHE A . n 
A 1 97  VAL 97  104 104 VAL VAL A . n 
A 1 98  GLY 98  105 105 GLY GLY A . n 
A 1 99  THR 99  106 106 THR THR A . n 
A 1 100 VAL 100 107 107 VAL VAL A . n 
A 1 101 VAL 101 108 108 VAL VAL A . n 
A 1 102 SER 102 109 109 SER SER A . n 
A 1 103 THR 103 110 110 THR THR A . n 
A 1 104 ILE 104 111 111 ILE ILE A . n 
A 1 105 GLY 105 112 112 GLY GLY A . n 
A 1 106 PHE 106 113 113 PHE PHE A . n 
A 1 107 GLY 107 114 114 GLY GLY A . n 
A 1 108 MET 108 115 115 MET MET A . n 
A 1 109 THR 109 116 116 THR THR A . n 
A 1 110 THR 110 117 117 THR THR A . n 
A 1 111 PRO 111 118 118 PRO PRO A . n 
A 1 112 ALA 112 119 119 ALA ALA A . n 
A 1 113 THR 113 120 120 THR THR A . n 
A 1 114 VAL 114 121 121 VAL VAL A . n 
A 1 115 GLY 115 122 122 GLY GLY A . n 
A 1 116 GLY 116 123 123 GLY GLY A . n 
A 1 117 LYS 117 124 124 LYS LYS A . n 
A 1 118 ILE 118 125 125 ILE ILE A . n 
A 1 119 PHE 119 126 126 PHE PHE A . n 
A 1 120 LEU 120 127 127 LEU LEU A . n 
A 1 121 ILE 121 128 128 ILE ILE A . n 
A 1 122 PHE 122 129 129 PHE PHE A . n 
A 1 123 TYR 123 130 130 TYR TYR A . n 
A 1 124 GLY 124 131 131 GLY GLY A . n 
A 1 125 LEU 125 132 132 LEU LEU A . n 
A 1 126 VAL 126 133 133 VAL VAL A . n 
A 1 127 GLY 127 134 134 GLY GLY A . n 
A 1 128 CYS 128 135 135 CYS CYS A . n 
A 1 129 SER 129 136 136 SER SER A . n 
A 1 130 SER 130 137 137 SER SER A . n 
A 1 131 THR 131 138 138 THR THR A . n 
A 1 132 ILE 132 139 139 ILE ILE A . n 
A 1 133 LEU 133 140 140 LEU LEU A . n 
A 1 134 PHE 134 141 141 PHE PHE A . n 
A 1 135 PHE 135 142 142 PHE PHE A . n 
A 1 136 ASN 136 143 143 ASN ASN A . n 
A 1 137 LEU 137 144 144 LEU LEU A . n 
A 1 138 PHE 138 145 145 PHE PHE A . n 
A 1 139 LEU 139 146 146 LEU LEU A . n 
A 1 140 GLU 140 147 147 GLU GLU A . n 
A 1 141 ARG 141 148 148 ARG ARG A . n 
A 1 142 LEU 142 149 149 LEU LEU A . n 
A 1 143 ILE 143 150 150 ILE ILE A . n 
A 1 144 THR 144 151 151 THR THR A . n 
A 1 145 ILE 145 152 152 ILE ILE A . n 
A 1 146 ILE 146 153 153 ILE ILE A . n 
A 1 147 ALA 147 154 154 ALA ALA A . n 
A 1 148 TYR 148 155 155 TYR TYR A . n 
A 1 149 ILE 149 156 156 ILE ILE A . n 
A 1 150 MET 150 157 157 MET MET A . n 
A 1 151 LYS 151 158 158 LYS LYS A . n 
A 1 152 SER 152 159 159 SER SER A . n 
A 1 153 CYS 153 160 160 CYS CYS A . n 
A 1 154 HIS 154 161 161 HIS HIS A . n 
A 1 155 GLN 155 162 162 GLN GLN A . n 
A 1 156 ARG 156 163 163 ARG ARG A . n 
A 1 157 GLN 157 164 164 GLN GLN A . n 
A 1 158 LEU 158 165 165 LEU LEU A . n 
A 1 159 ARG 159 166 ?   ?   ?   A . n 
A 1 160 ARG 160 167 ?   ?   ?   A . n 
A 1 161 ARG 161 168 ?   ?   ?   A . n 
A 1 162 GLY 162 169 ?   ?   ?   A . n 
A 1 163 ALA 163 170 ?   ?   ?   A . n 
A 1 164 LEU 164 171 ?   ?   ?   A . n 
A 1 165 PRO 165 172 ?   ?   ?   A . n 
A 1 166 GLN 166 173 ?   ?   ?   A . n 
A 1 167 GLU 167 174 ?   ?   ?   A . n 
A 1 168 SER 168 175 ?   ?   ?   A . n 
A 1 169 LEU 169 176 ?   ?   ?   A . n 
A 1 170 LYS 170 177 ?   ?   ?   A . n 
A 1 171 ASP 171 178 ?   ?   ?   A . n 
A 1 172 ALA 172 179 ?   ?   ?   A . n 
A 1 173 GLY 173 180 ?   ?   ?   A . n 
A 1 174 GLN 174 181 ?   ?   ?   A . n 
A 1 175 CYS 175 182 ?   ?   ?   A . n 
A 1 176 GLU 176 183 ?   ?   ?   A . n 
A 1 177 VAL 177 184 ?   ?   ?   A . n 
A 1 178 ASP 178 185 ?   ?   ?   A . n 
A 1 179 SER 179 186 ?   ?   ?   A . n 
A 1 180 LEU 180 187 ?   ?   ?   A . n 
A 1 181 ALA 181 188 ?   ?   ?   A . n 
A 1 182 GLY 182 189 ?   ?   ?   A . n 
A 1 183 TRP 183 190 190 TRP TRP A . n 
A 1 184 LYS 184 191 191 LYS LYS A . n 
A 1 185 PRO 185 192 192 PRO PRO A . n 
A 1 186 SER 186 193 193 SER SER A . n 
A 1 187 VAL 187 194 194 VAL VAL A . n 
A 1 188 TYR 188 195 195 TYR TYR A . n 
A 1 189 TYR 189 196 196 TYR TYR A . n 
A 1 190 VAL 190 197 197 VAL VAL A . n 
A 1 191 MET 191 198 198 MET MET A . n 
A 1 192 LEU 192 199 199 LEU LEU A . n 
A 1 193 ILE 193 200 200 ILE ILE A . n 
A 1 194 LEU 194 201 201 LEU LEU A . n 
A 1 195 CYS 195 202 202 CYS CYS A . n 
A 1 196 THR 196 203 203 THR THR A . n 
A 1 197 ALA 197 204 204 ALA ALA A . n 
A 1 198 SER 198 205 205 SER SER A . n 
A 1 199 ILE 199 206 206 ILE ILE A . n 
A 1 200 LEU 200 207 207 LEU LEU A . n 
A 1 201 ILE 201 208 208 ILE ILE A . n 
A 1 202 SER 202 209 209 SER SER A . n 
A 1 203 CYS 203 210 210 CYS CYS A . n 
A 1 204 CYS 204 211 211 CYS CYS A . n 
A 1 205 ALA 205 212 212 ALA ALA A . n 
A 1 206 SER 206 213 213 SER SER A . n 
A 1 207 ALA 207 214 214 ALA ALA A . n 
A 1 208 MET 208 215 215 MET MET A . n 
A 1 209 TYR 209 216 216 TYR TYR A . n 
A 1 210 THR 210 217 217 THR THR A . n 
A 1 211 PRO 211 218 218 PRO PRO A . n 
A 1 212 ILE 212 219 219 ILE ILE A . n 
A 1 213 GLU 213 220 220 GLU GLU A . n 
A 1 214 GLY 214 221 221 GLY GLY A . n 
A 1 215 TRP 215 222 222 TRP TRP A . n 
A 1 216 SER 216 223 223 SER SER A . n 
A 1 217 TYR 217 224 224 TYR TYR A . n 
A 1 218 PHE 218 225 225 PHE PHE A . n 
A 1 219 ASP 219 226 226 ASP ASP A . n 
A 1 220 SER 220 227 227 SER SER A . n 
A 1 221 LEU 221 228 228 LEU LEU A . n 
A 1 222 TYR 222 229 229 TYR TYR A . n 
A 1 223 PHE 223 230 230 PHE PHE A . n 
A 1 224 CYS 224 231 231 CYS CYS A . n 
A 1 225 PHE 225 232 232 PHE PHE A . n 
A 1 226 VAL 226 233 233 VAL VAL A . n 
A 1 227 ALA 227 234 234 ALA ALA A . n 
A 1 228 PHE 228 235 235 PHE PHE A . n 
A 1 229 SER 229 236 236 SER SER A . n 
A 1 230 THR 230 237 237 THR THR A . n 
A 1 231 ILE 231 238 238 ILE ILE A . n 
A 1 232 GLY 232 239 239 GLY GLY A . n 
A 1 233 PHE 233 240 240 PHE PHE A . n 
A 1 234 GLY 234 241 241 GLY GLY A . n 
A 1 235 ASP 235 242 242 ASP ASP A . n 
A 1 236 LEU 236 243 243 LEU LEU A . n 
A 1 237 VAL 237 244 244 VAL VAL A . n 
A 1 238 SER 238 245 245 SER SER A . n 
A 1 239 SER 239 246 246 SER SER A . n 
A 1 240 GLN 240 247 247 GLN GLN A . n 
A 1 241 ASN 241 248 248 ASN ASN A . n 
A 1 242 ALA 242 249 249 ALA ALA A . n 
A 1 243 HIS 243 250 250 HIS HIS A . n 
A 1 244 TYR 244 251 251 TYR TYR A . n 
A 1 245 GLU 245 252 252 GLU GLU A . n 
A 1 246 SER 246 253 253 SER SER A . n 
A 1 247 GLN 247 254 254 GLN GLN A . n 
A 1 248 GLY 248 255 255 GLY GLY A . n 
A 1 249 LEU 249 256 256 LEU LEU A . n 
A 1 250 TYR 250 257 257 TYR TYR A . n 
A 1 251 ARG 251 258 258 ARG ARG A . n 
A 1 252 PHE 252 259 259 PHE PHE A . n 
A 1 253 ALA 253 260 260 ALA ALA A . n 
A 1 254 ASN 254 261 261 ASN ASN A . n 
A 1 255 PHE 255 262 262 PHE PHE A . n 
A 1 256 VAL 256 263 263 VAL VAL A . n 
A 1 257 PHE 257 264 264 PHE PHE A . n 
A 1 258 ILE 258 265 265 ILE ILE A . n 
A 1 259 LEU 259 266 266 LEU LEU A . n 
A 1 260 MET 260 267 267 MET MET A . n 
A 1 261 GLY 261 268 268 GLY GLY A . n 
A 1 262 VAL 262 269 269 VAL VAL A . n 
A 1 263 CYS 263 270 270 CYS CYS A . n 
A 1 264 CYS 264 271 271 CYS CYS A . n 
A 1 265 ILE 265 272 272 ILE ILE A . n 
A 1 266 TYR 266 273 273 TYR TYR A . n 
A 1 267 SER 267 274 274 SER SER A . n 
A 1 268 LEU 268 275 275 LEU LEU A . n 
A 1 269 PHE 269 276 276 PHE PHE A . n 
A 1 270 ASN 270 277 277 ASN ASN A . n 
A 1 271 VAL 271 278 278 VAL VAL A . n 
A 1 272 ILE 272 279 279 ILE ILE A . n 
A 1 273 SER 273 280 280 SER SER A . n 
A 1 274 ILE 274 281 281 ILE ILE A . n 
A 1 275 LEU 275 282 282 LEU LEU A . n 
A 1 276 ILE 276 283 283 ILE ILE A . n 
A 1 277 LYS 277 284 284 LYS LYS A . n 
A 1 278 GLN 278 285 285 GLN GLN A . n 
A 1 279 SER 279 286 286 SER SER A . n 
A 1 280 LEU 280 287 287 LEU LEU A . n 
A 1 281 ASN 281 288 288 ASN ASN A . n 
A 1 282 TRP 282 289 289 TRP TRP A . n 
A 1 283 ILE 283 290 290 ILE ILE A . n 
A 1 284 LEU 284 291 291 LEU LEU A . n 
A 1 285 ARG 285 292 292 ARG ARG A . n 
A 1 286 LYS 286 293 293 LYS LYS A . n 
A 1 287 MET 287 294 294 MET MET A . n 
A 1 288 ASP 288 295 295 ASP ASP A . n 
A 1 289 SER 289 296 ?   ?   ?   A . n 
A 1 290 GLY 290 297 ?   ?   ?   A . n 
A 1 291 ALA 291 298 ?   ?   ?   A . n 
A 1 292 GLU 292 299 ?   ?   ?   A . n 
A 1 293 LEU 293 300 ?   ?   ?   A . n 
A 1 294 GLU 294 301 ?   ?   ?   A . n 
A 1 295 VAL 295 302 ?   ?   ?   A . n 
A 1 296 LEU 296 303 ?   ?   ?   A . n 
A 1 297 PHE 297 304 ?   ?   ?   A . n 
A 1 298 GLN 298 305 ?   ?   ?   A . n 
B 1 1   MET 1   8   ?   ?   ?   B . n 
B 1 2   GLY 2   9   ?   ?   ?   B . n 
B 1 3   PRO 3   10  ?   ?   ?   B . n 
B 1 4   GLY 4   11  ?   ?   ?   B . n 
B 1 5   HIS 5   12  ?   ?   ?   B . n 
B 1 6   LEU 6   13  ?   ?   ?   B . n 
B 1 7   ASN 7   14  14  ASN ASN B . n 
B 1 8   GLU 8   15  15  GLU GLU B . n 
B 1 9   ASP 9   16  16  ASP ASP B . n 
B 1 10  ASN 10  17  17  ASN ASN B . n 
B 1 11  ALA 11  18  18  ALA ALA B . n 
B 1 12  ARG 12  19  19  ARG ARG B . n 
B 1 13  PHE 13  20  20  PHE PHE B . n 
B 1 14  LEU 14  21  21  LEU LEU B . n 
B 1 15  LEU 15  22  22  LEU LEU B . n 
B 1 16  LEU 16  23  23  LEU LEU B . n 
B 1 17  ALA 17  24  24  ALA ALA B . n 
B 1 18  ALA 18  25  25  ALA ALA B . n 
B 1 19  LEU 19  26  26  LEU LEU B . n 
B 1 20  ILE 20  27  27  ILE ILE B . n 
B 1 21  VAL 21  28  28  VAL VAL B . n 
B 1 22  LEU 22  29  29  LEU LEU B . n 
B 1 23  TYR 23  30  30  TYR TYR B . n 
B 1 24  LEU 24  31  31  LEU LEU B . n 
B 1 25  LEU 25  32  32  LEU LEU B . n 
B 1 26  GLY 26  33  33  GLY GLY B . n 
B 1 27  GLY 27  34  34  GLY GLY B . n 
B 1 28  ALA 28  35  35  ALA ALA B . n 
B 1 29  ALA 29  36  36  ALA ALA B . n 
B 1 30  VAL 30  37  37  VAL VAL B . n 
B 1 31  PHE 31  38  38  PHE PHE B . n 
B 1 32  SER 32  39  39  SER SER B . n 
B 1 33  ALA 33  40  40  ALA ALA B . n 
B 1 34  LEU 34  41  41  LEU LEU B . n 
B 1 35  GLU 35  42  42  GLU GLU B . n 
B 1 36  LEU 36  43  43  LEU LEU B . n 
B 1 37  ALA 37  44  44  ALA ALA B . n 
B 1 38  HIS 38  45  45  HIS HIS B . n 
B 1 39  GLU 39  46  46  GLU GLU B . n 
B 1 40  ARG 40  47  47  ARG ARG B . n 
B 1 41  GLN 41  48  48  GLN GLN B . n 
B 1 42  ALA 42  49  49  ALA ALA B . n 
B 1 43  LYS 43  50  50  LYS LYS B . n 
B 1 44  GLN 44  51  51  GLN GLN B . n 
B 1 45  ARG 45  52  52  ARG ARG B . n 
B 1 46  TRP 46  53  53  TRP TRP B . n 
B 1 47  GLU 47  54  54  GLU GLU B . n 
B 1 48  GLU 48  55  55  GLU GLU B . n 
B 1 49  ARG 49  56  56  ARG ARG B . n 
B 1 50  LEU 50  57  57  LEU LEU B . n 
B 1 51  ALA 51  58  58  ALA ALA B . n 
B 1 52  ASN 52  59  59  ASN ASN B . n 
B 1 53  PHE 53  60  60  PHE PHE B . n 
B 1 54  SER 54  61  61  SER SER B . n 
B 1 55  ARG 55  62  62  ARG ARG B . n 
B 1 56  GLY 56  63  63  GLY GLY B . n 
B 1 57  HIS 57  64  64  HIS HIS B . n 
B 1 58  ASN 58  65  65  ASN ASN B . n 
B 1 59  LEU 59  66  66  LEU LEU B . n 
B 1 60  SER 60  67  67  SER SER B . n 
B 1 61  ARG 61  68  68  ARG ARG B . n 
B 1 62  ASP 62  69  69  ASP ASP B . n 
B 1 63  GLU 63  70  70  GLU GLU B . n 
B 1 64  LEU 64  71  71  LEU LEU B . n 
B 1 65  ARG 65  72  72  ARG ARG B . n 
B 1 66  GLY 66  73  73  GLY GLY B . n 
B 1 67  PHE 67  74  74  PHE PHE B . n 
B 1 68  LEU 68  75  75  LEU LEU B . n 
B 1 69  ARG 69  76  76  ARG ARG B . n 
B 1 70  HIS 70  77  77  HIS HIS B . n 
B 1 71  TYR 71  78  78  TYR TYR B . n 
B 1 72  GLU 72  79  79  GLU GLU B . n 
B 1 73  GLU 73  80  80  GLU GLU B . n 
B 1 74  ALA 74  81  81  ALA ALA B . n 
B 1 75  THR 75  82  82  THR THR B . n 
B 1 76  ARG 76  83  83  ARG ARG B . n 
B 1 77  ALA 77  84  84  ALA ALA B . n 
B 1 78  GLY 78  85  85  GLY GLY B . n 
B 1 79  ILE 79  86  86  ILE ILE B . n 
B 1 80  ARG 80  87  87  ARG ARG B . n 
B 1 81  VAL 81  88  88  VAL VAL B . n 
B 1 82  ASP 82  89  89  ASP ASP B . n 
B 1 83  ASN 83  90  90  ASN ASN B . n 
B 1 84  VAL 84  91  91  VAL VAL B . n 
B 1 85  ARG 85  92  92  ARG ARG B . n 
B 1 86  PRO 86  93  93  PRO PRO B . n 
B 1 87  ARG 87  94  94  ARG ARG B . n 
B 1 88  TRP 88  95  95  TRP TRP B . n 
B 1 89  ASP 89  96  96  ASP ASP B . n 
B 1 90  PHE 90  97  97  PHE PHE B . n 
B 1 91  THR 91  98  98  THR THR B . n 
B 1 92  GLY 92  99  99  GLY GLY B . n 
B 1 93  ALA 93  100 100 ALA ALA B . n 
B 1 94  PHE 94  101 101 PHE PHE B . n 
B 1 95  TYR 95  102 102 TYR TYR B . n 
B 1 96  PHE 96  103 103 PHE PHE B . n 
B 1 97  VAL 97  104 104 VAL VAL B . n 
B 1 98  GLY 98  105 105 GLY GLY B . n 
B 1 99  THR 99  106 106 THR THR B . n 
B 1 100 VAL 100 107 107 VAL VAL B . n 
B 1 101 VAL 101 108 108 VAL VAL B . n 
B 1 102 SER 102 109 109 SER SER B . n 
B 1 103 THR 103 110 110 THR THR B . n 
B 1 104 ILE 104 111 111 ILE ILE B . n 
B 1 105 GLY 105 112 112 GLY GLY B . n 
B 1 106 PHE 106 113 113 PHE PHE B . n 
B 1 107 GLY 107 114 114 GLY GLY B . n 
B 1 108 MET 108 115 115 MET MET B . n 
B 1 109 THR 109 116 116 THR THR B . n 
B 1 110 THR 110 117 117 THR THR B . n 
B 1 111 PRO 111 118 118 PRO PRO B . n 
B 1 112 ALA 112 119 119 ALA ALA B . n 
B 1 113 THR 113 120 120 THR THR B . n 
B 1 114 VAL 114 121 121 VAL VAL B . n 
B 1 115 GLY 115 122 122 GLY GLY B . n 
B 1 116 GLY 116 123 123 GLY GLY B . n 
B 1 117 LYS 117 124 124 LYS LYS B . n 
B 1 118 ILE 118 125 125 ILE ILE B . n 
B 1 119 PHE 119 126 126 PHE PHE B . n 
B 1 120 LEU 120 127 127 LEU LEU B . n 
B 1 121 ILE 121 128 128 ILE ILE B . n 
B 1 122 PHE 122 129 129 PHE PHE B . n 
B 1 123 TYR 123 130 130 TYR TYR B . n 
B 1 124 GLY 124 131 131 GLY GLY B . n 
B 1 125 LEU 125 132 132 LEU LEU B . n 
B 1 126 VAL 126 133 133 VAL VAL B . n 
B 1 127 GLY 127 134 134 GLY GLY B . n 
B 1 128 CYS 128 135 135 CYS CYS B . n 
B 1 129 SER 129 136 136 SER SER B . n 
B 1 130 SER 130 137 137 SER SER B . n 
B 1 131 THR 131 138 138 THR THR B . n 
B 1 132 ILE 132 139 139 ILE ILE B . n 
B 1 133 LEU 133 140 140 LEU LEU B . n 
B 1 134 PHE 134 141 141 PHE PHE B . n 
B 1 135 PHE 135 142 142 PHE PHE B . n 
B 1 136 ASN 136 143 143 ASN ASN B . n 
B 1 137 LEU 137 144 144 LEU LEU B . n 
B 1 138 PHE 138 145 145 PHE PHE B . n 
B 1 139 LEU 139 146 146 LEU LEU B . n 
B 1 140 GLU 140 147 147 GLU GLU B . n 
B 1 141 ARG 141 148 148 ARG ARG B . n 
B 1 142 LEU 142 149 149 LEU LEU B . n 
B 1 143 ILE 143 150 150 ILE ILE B . n 
B 1 144 THR 144 151 151 THR THR B . n 
B 1 145 ILE 145 152 152 ILE ILE B . n 
B 1 146 ILE 146 153 153 ILE ILE B . n 
B 1 147 ALA 147 154 154 ALA ALA B . n 
B 1 148 TYR 148 155 155 TYR TYR B . n 
B 1 149 ILE 149 156 156 ILE ILE B . n 
B 1 150 MET 150 157 157 MET MET B . n 
B 1 151 LYS 151 158 158 LYS LYS B . n 
B 1 152 SER 152 159 159 SER SER B . n 
B 1 153 CYS 153 160 160 CYS CYS B . n 
B 1 154 HIS 154 161 161 HIS HIS B . n 
B 1 155 GLN 155 162 162 GLN GLN B . n 
B 1 156 ARG 156 163 163 ARG ARG B . n 
B 1 157 GLN 157 164 164 GLN GLN B . n 
B 1 158 LEU 158 165 165 LEU LEU B . n 
B 1 159 ARG 159 166 ?   ?   ?   B . n 
B 1 160 ARG 160 167 ?   ?   ?   B . n 
B 1 161 ARG 161 168 ?   ?   ?   B . n 
B 1 162 GLY 162 169 ?   ?   ?   B . n 
B 1 163 ALA 163 170 ?   ?   ?   B . n 
B 1 164 LEU 164 171 ?   ?   ?   B . n 
B 1 165 PRO 165 172 ?   ?   ?   B . n 
B 1 166 GLN 166 173 ?   ?   ?   B . n 
B 1 167 GLU 167 174 ?   ?   ?   B . n 
B 1 168 SER 168 175 ?   ?   ?   B . n 
B 1 169 LEU 169 176 ?   ?   ?   B . n 
B 1 170 LYS 170 177 ?   ?   ?   B . n 
B 1 171 ASP 171 178 ?   ?   ?   B . n 
B 1 172 ALA 172 179 ?   ?   ?   B . n 
B 1 173 GLY 173 180 ?   ?   ?   B . n 
B 1 174 GLN 174 181 ?   ?   ?   B . n 
B 1 175 CYS 175 182 ?   ?   ?   B . n 
B 1 176 GLU 176 183 ?   ?   ?   B . n 
B 1 177 VAL 177 184 ?   ?   ?   B . n 
B 1 178 ASP 178 185 ?   ?   ?   B . n 
B 1 179 SER 179 186 ?   ?   ?   B . n 
B 1 180 LEU 180 187 ?   ?   ?   B . n 
B 1 181 ALA 181 188 ?   ?   ?   B . n 
B 1 182 GLY 182 189 ?   ?   ?   B . n 
B 1 183 TRP 183 190 190 TRP TRP B . n 
B 1 184 LYS 184 191 191 LYS LYS B . n 
B 1 185 PRO 185 192 192 PRO PRO B . n 
B 1 186 SER 186 193 193 SER SER B . n 
B 1 187 VAL 187 194 194 VAL VAL B . n 
B 1 188 TYR 188 195 195 TYR TYR B . n 
B 1 189 TYR 189 196 196 TYR TYR B . n 
B 1 190 VAL 190 197 197 VAL VAL B . n 
B 1 191 MET 191 198 198 MET MET B . n 
B 1 192 LEU 192 199 199 LEU LEU B . n 
B 1 193 ILE 193 200 200 ILE ILE B . n 
B 1 194 LEU 194 201 201 LEU LEU B . n 
B 1 195 CYS 195 202 202 CYS CYS B . n 
B 1 196 THR 196 203 203 THR THR B . n 
B 1 197 ALA 197 204 204 ALA ALA B . n 
B 1 198 SER 198 205 205 SER SER B . n 
B 1 199 ILE 199 206 206 ILE ILE B . n 
B 1 200 LEU 200 207 207 LEU LEU B . n 
B 1 201 ILE 201 208 208 ILE ILE B . n 
B 1 202 SER 202 209 209 SER SER B . n 
B 1 203 CYS 203 210 210 CYS CYS B . n 
B 1 204 CYS 204 211 211 CYS CYS B . n 
B 1 205 ALA 205 212 212 ALA ALA B . n 
B 1 206 SER 206 213 213 SER SER B . n 
B 1 207 ALA 207 214 214 ALA ALA B . n 
B 1 208 MET 208 215 215 MET MET B . n 
B 1 209 TYR 209 216 216 TYR TYR B . n 
B 1 210 THR 210 217 217 THR THR B . n 
B 1 211 PRO 211 218 218 PRO PRO B . n 
B 1 212 ILE 212 219 219 ILE ILE B . n 
B 1 213 GLU 213 220 220 GLU GLU B . n 
B 1 214 GLY 214 221 221 GLY GLY B . n 
B 1 215 TRP 215 222 222 TRP TRP B . n 
B 1 216 SER 216 223 223 SER SER B . n 
B 1 217 TYR 217 224 224 TYR TYR B . n 
B 1 218 PHE 218 225 225 PHE PHE B . n 
B 1 219 ASP 219 226 226 ASP ASP B . n 
B 1 220 SER 220 227 227 SER SER B . n 
B 1 221 LEU 221 228 228 LEU LEU B . n 
B 1 222 TYR 222 229 229 TYR TYR B . n 
B 1 223 PHE 223 230 230 PHE PHE B . n 
B 1 224 CYS 224 231 231 CYS CYS B . n 
B 1 225 PHE 225 232 232 PHE PHE B . n 
B 1 226 VAL 226 233 233 VAL VAL B . n 
B 1 227 ALA 227 234 234 ALA ALA B . n 
B 1 228 PHE 228 235 235 PHE PHE B . n 
B 1 229 SER 229 236 236 SER SER B . n 
B 1 230 THR 230 237 237 THR THR B . n 
B 1 231 ILE 231 238 238 ILE ILE B . n 
B 1 232 GLY 232 239 239 GLY GLY B . n 
B 1 233 PHE 233 240 240 PHE PHE B . n 
B 1 234 GLY 234 241 241 GLY GLY B . n 
B 1 235 ASP 235 242 242 ASP ASP B . n 
B 1 236 LEU 236 243 243 LEU LEU B . n 
B 1 237 VAL 237 244 244 VAL VAL B . n 
B 1 238 SER 238 245 245 SER SER B . n 
B 1 239 SER 239 246 246 SER SER B . n 
B 1 240 GLN 240 247 247 GLN GLN B . n 
B 1 241 ASN 241 248 248 ASN ASN B . n 
B 1 242 ALA 242 249 249 ALA ALA B . n 
B 1 243 HIS 243 250 250 HIS HIS B . n 
B 1 244 TYR 244 251 251 TYR TYR B . n 
B 1 245 GLU 245 252 252 GLU GLU B . n 
B 1 246 SER 246 253 253 SER SER B . n 
B 1 247 GLN 247 254 254 GLN GLN B . n 
B 1 248 GLY 248 255 255 GLY GLY B . n 
B 1 249 LEU 249 256 256 LEU LEU B . n 
B 1 250 TYR 250 257 257 TYR TYR B . n 
B 1 251 ARG 251 258 258 ARG ARG B . n 
B 1 252 PHE 252 259 259 PHE PHE B . n 
B 1 253 ALA 253 260 260 ALA ALA B . n 
B 1 254 ASN 254 261 261 ASN ASN B . n 
B 1 255 PHE 255 262 262 PHE PHE B . n 
B 1 256 VAL 256 263 263 VAL VAL B . n 
B 1 257 PHE 257 264 264 PHE PHE B . n 
B 1 258 ILE 258 265 265 ILE ILE B . n 
B 1 259 LEU 259 266 266 LEU LEU B . n 
B 1 260 MET 260 267 267 MET MET B . n 
B 1 261 GLY 261 268 268 GLY GLY B . n 
B 1 262 VAL 262 269 269 VAL VAL B . n 
B 1 263 CYS 263 270 270 CYS CYS B . n 
B 1 264 CYS 264 271 271 CYS CYS B . n 
B 1 265 ILE 265 272 272 ILE ILE B . n 
B 1 266 TYR 266 273 273 TYR TYR B . n 
B 1 267 SER 267 274 274 SER SER B . n 
B 1 268 LEU 268 275 275 LEU LEU B . n 
B 1 269 PHE 269 276 276 PHE PHE B . n 
B 1 270 ASN 270 277 277 ASN ASN B . n 
B 1 271 VAL 271 278 278 VAL VAL B . n 
B 1 272 ILE 272 279 279 ILE ILE B . n 
B 1 273 SER 273 280 280 SER SER B . n 
B 1 274 ILE 274 281 281 ILE ILE B . n 
B 1 275 LEU 275 282 282 LEU LEU B . n 
B 1 276 ILE 276 283 283 ILE ILE B . n 
B 1 277 LYS 277 284 284 LYS LYS B . n 
B 1 278 GLN 278 285 285 GLN GLN B . n 
B 1 279 SER 279 286 286 SER SER B . n 
B 1 280 LEU 280 287 287 LEU LEU B . n 
B 1 281 ASN 281 288 288 ASN ASN B . n 
B 1 282 TRP 282 289 289 TRP TRP B . n 
B 1 283 ILE 283 290 290 ILE ILE B . n 
B 1 284 LEU 284 291 291 LEU LEU B . n 
B 1 285 ARG 285 292 292 ARG ARG B . n 
B 1 286 LYS 286 293 293 LYS LYS B . n 
B 1 287 MET 287 294 294 MET MET B . n 
B 1 288 ASP 288 295 295 ASP ASP B . n 
B 1 289 SER 289 296 ?   ?   ?   B . n 
B 1 290 GLY 290 297 ?   ?   ?   B . n 
B 1 291 ALA 291 298 ?   ?   ?   B . n 
B 1 292 GLU 292 299 ?   ?   ?   B . n 
B 1 293 LEU 293 300 ?   ?   ?   B . n 
B 1 294 GLU 294 301 ?   ?   ?   B . n 
B 1 295 VAL 295 302 ?   ?   ?   B . n 
B 1 296 LEU 296 303 ?   ?   ?   B . n 
B 1 297 PHE 297 304 ?   ?   ?   B . n 
B 1 298 GLN 298 305 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 EIC 1 401 301 EIC EIC A . 
D 3 K   1 402 401 K   K   A . 
E 3 K   1 403 402 K   K   A . 
F 2 EIC 1 401 301 EIC EIC 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 ASN 14  ? CG  ? A ASN 7   CG  
2   1 Y 1 A ASN 14  ? OD1 ? A ASN 7   OD1 
3   1 Y 1 A ASN 14  ? ND2 ? A ASN 7   ND2 
4   1 Y 1 A GLU 15  ? CG  ? A GLU 8   CG  
5   1 Y 1 A GLU 15  ? CD  ? A GLU 8   CD  
6   1 Y 1 A GLU 15  ? OE1 ? A GLU 8   OE1 
7   1 Y 1 A GLU 15  ? OE2 ? A GLU 8   OE2 
8   1 Y 1 A ASP 69  ? CG  ? A ASP 62  CG  
9   1 Y 1 A ASP 69  ? OD1 ? A ASP 62  OD1 
10  1 Y 1 A ASP 69  ? OD2 ? A ASP 62  OD2 
11  1 Y 1 A ARG 72  ? CG  ? A ARG 65  CG  
12  1 Y 1 A ARG 72  ? CD  ? A ARG 65  CD  
13  1 Y 1 A ARG 72  ? NE  ? A ARG 65  NE  
14  1 Y 1 A ARG 72  ? CZ  ? A ARG 65  CZ  
15  1 Y 1 A ARG 72  ? NH1 ? A ARG 65  NH1 
16  1 Y 1 A ARG 72  ? NH2 ? A ARG 65  NH2 
17  1 Y 1 A ASP 89  ? CG  ? A ASP 82  CG  
18  1 Y 1 A ASP 89  ? OD1 ? A ASP 82  OD1 
19  1 Y 1 A ASP 89  ? OD2 ? A ASP 82  OD2 
20  1 Y 1 A GLU 147 ? CG  ? A GLU 140 CG  
21  1 Y 1 A GLU 147 ? CD  ? A GLU 140 CD  
22  1 Y 1 A GLU 147 ? OE1 ? A GLU 140 OE1 
23  1 Y 1 A GLU 147 ? OE2 ? A GLU 140 OE2 
24  1 Y 1 A MET 157 ? CG  ? A MET 150 CG  
25  1 Y 1 A MET 157 ? SD  ? A MET 150 SD  
26  1 Y 1 A MET 157 ? CE  ? A MET 150 CE  
27  1 Y 1 A LYS 158 ? CG  ? A LYS 151 CG  
28  1 Y 1 A LYS 158 ? CD  ? A LYS 151 CD  
29  1 Y 1 A LYS 158 ? CE  ? A LYS 151 CE  
30  1 Y 1 A LYS 158 ? NZ  ? A LYS 151 NZ  
31  1 Y 1 A SER 159 ? OG  ? A SER 152 OG  
32  1 Y 1 A CYS 160 ? SG  ? A CYS 153 SG  
33  1 Y 1 A HIS 161 ? CG  ? A HIS 154 CG  
34  1 Y 1 A HIS 161 ? ND1 ? A HIS 154 ND1 
35  1 Y 1 A HIS 161 ? CD2 ? A HIS 154 CD2 
36  1 Y 1 A HIS 161 ? CE1 ? A HIS 154 CE1 
37  1 Y 1 A HIS 161 ? NE2 ? A HIS 154 NE2 
38  1 Y 1 A GLN 162 ? CG  ? A GLN 155 CG  
39  1 Y 1 A GLN 162 ? CD  ? A GLN 155 CD  
40  1 Y 1 A GLN 162 ? OE1 ? A GLN 155 OE1 
41  1 Y 1 A GLN 162 ? NE2 ? A GLN 155 NE2 
42  1 Y 1 A ARG 163 ? CG  ? A ARG 156 CG  
43  1 Y 1 A ARG 163 ? CD  ? A ARG 156 CD  
44  1 Y 1 A ARG 163 ? NE  ? A ARG 156 NE  
45  1 Y 1 A ARG 163 ? CZ  ? A ARG 156 CZ  
46  1 Y 1 A ARG 163 ? NH1 ? A ARG 156 NH1 
47  1 Y 1 A ARG 163 ? NH2 ? A ARG 156 NH2 
48  1 Y 1 A GLN 164 ? CG  ? A GLN 157 CG  
49  1 Y 1 A GLN 164 ? CD  ? A GLN 157 CD  
50  1 Y 1 A GLN 164 ? OE1 ? A GLN 157 OE1 
51  1 Y 1 A GLN 164 ? NE2 ? A GLN 157 NE2 
52  1 Y 1 A LEU 165 ? CG  ? A LEU 158 CG  
53  1 Y 1 A LEU 165 ? CD1 ? A LEU 158 CD1 
54  1 Y 1 A LEU 165 ? CD2 ? A LEU 158 CD2 
55  1 Y 1 A TRP 190 ? CG  ? A TRP 183 CG  
56  1 Y 1 A TRP 190 ? CD1 ? A TRP 183 CD1 
57  1 Y 1 A TRP 190 ? CD2 ? A TRP 183 CD2 
58  1 Y 1 A TRP 190 ? NE1 ? A TRP 183 NE1 
59  1 Y 1 A TRP 190 ? CE2 ? A TRP 183 CE2 
60  1 Y 1 A TRP 190 ? CE3 ? A TRP 183 CE3 
61  1 Y 1 A TRP 190 ? CZ2 ? A TRP 183 CZ2 
62  1 Y 1 A TRP 190 ? CZ3 ? A TRP 183 CZ3 
63  1 Y 1 A TRP 190 ? CH2 ? A TRP 183 CH2 
64  1 Y 1 A LYS 191 ? CG  ? A LYS 184 CG  
65  1 Y 1 A LYS 191 ? CD  ? A LYS 184 CD  
66  1 Y 1 A LYS 191 ? CE  ? A LYS 184 CE  
67  1 Y 1 A LYS 191 ? NZ  ? A LYS 184 NZ  
68  1 Y 1 A GLU 252 ? CG  ? A GLU 245 CG  
69  1 Y 1 A GLU 252 ? CD  ? A GLU 245 CD  
70  1 Y 1 A GLU 252 ? OE1 ? A GLU 245 OE1 
71  1 Y 1 A GLU 252 ? OE2 ? A GLU 245 OE2 
72  1 Y 1 A ARG 292 ? CG  ? A ARG 285 CG  
73  1 Y 1 A ARG 292 ? CD  ? A ARG 285 CD  
74  1 Y 1 A ARG 292 ? NE  ? A ARG 285 NE  
75  1 Y 1 A ARG 292 ? CZ  ? A ARG 285 CZ  
76  1 Y 1 A ARG 292 ? NH1 ? A ARG 285 NH1 
77  1 Y 1 A ARG 292 ? NH2 ? A ARG 285 NH2 
78  1 Y 1 A LYS 293 ? CG  ? A LYS 286 CG  
79  1 Y 1 A LYS 293 ? CD  ? A LYS 286 CD  
80  1 Y 1 A LYS 293 ? CE  ? A LYS 286 CE  
81  1 Y 1 A LYS 293 ? NZ  ? A LYS 286 NZ  
82  1 Y 1 A MET 294 ? CG  ? A MET 287 CG  
83  1 Y 1 A MET 294 ? SD  ? A MET 287 SD  
84  1 Y 1 A MET 294 ? CE  ? A MET 287 CE  
85  1 Y 1 A ASP 295 ? CG  ? A ASP 288 CG  
86  1 Y 1 A ASP 295 ? OD1 ? A ASP 288 OD1 
87  1 Y 1 A ASP 295 ? OD2 ? A ASP 288 OD2 
88  1 Y 1 B ASN 14  ? CG  ? B ASN 7   CG  
89  1 Y 1 B ASN 14  ? OD1 ? B ASN 7   OD1 
90  1 Y 1 B ASN 14  ? ND2 ? B ASN 7   ND2 
91  1 Y 1 B GLU 15  ? CG  ? B GLU 8   CG  
92  1 Y 1 B GLU 15  ? CD  ? B GLU 8   CD  
93  1 Y 1 B GLU 15  ? OE1 ? B GLU 8   OE1 
94  1 Y 1 B GLU 15  ? OE2 ? B GLU 8   OE2 
95  1 Y 1 B ASP 69  ? CG  ? B ASP 62  CG  
96  1 Y 1 B ASP 69  ? OD1 ? B ASP 62  OD1 
97  1 Y 1 B ASP 69  ? OD2 ? B ASP 62  OD2 
98  1 Y 1 B ARG 72  ? CG  ? B ARG 65  CG  
99  1 Y 1 B ARG 72  ? CD  ? B ARG 65  CD  
100 1 Y 1 B ARG 72  ? NE  ? B ARG 65  NE  
101 1 Y 1 B ARG 72  ? CZ  ? B ARG 65  CZ  
102 1 Y 1 B ARG 72  ? NH1 ? B ARG 65  NH1 
103 1 Y 1 B ARG 72  ? NH2 ? B ARG 65  NH2 
104 1 Y 1 B ASP 89  ? CG  ? B ASP 82  CG  
105 1 Y 1 B ASP 89  ? OD1 ? B ASP 82  OD1 
106 1 Y 1 B ASP 89  ? OD2 ? B ASP 82  OD2 
107 1 Y 1 B GLU 147 ? CG  ? B GLU 140 CG  
108 1 Y 1 B GLU 147 ? CD  ? B GLU 140 CD  
109 1 Y 1 B GLU 147 ? OE1 ? B GLU 140 OE1 
110 1 Y 1 B GLU 147 ? OE2 ? B GLU 140 OE2 
111 1 Y 1 B MET 157 ? CG  ? B MET 150 CG  
112 1 Y 1 B MET 157 ? SD  ? B MET 150 SD  
113 1 Y 1 B MET 157 ? CE  ? B MET 150 CE  
114 1 Y 1 B LYS 158 ? CG  ? B LYS 151 CG  
115 1 Y 1 B LYS 158 ? CD  ? B LYS 151 CD  
116 1 Y 1 B LYS 158 ? CE  ? B LYS 151 CE  
117 1 Y 1 B LYS 158 ? NZ  ? B LYS 151 NZ  
118 1 Y 1 B SER 159 ? OG  ? B SER 152 OG  
119 1 Y 1 B CYS 160 ? SG  ? B CYS 153 SG  
120 1 Y 1 B HIS 161 ? CG  ? B HIS 154 CG  
121 1 Y 1 B HIS 161 ? ND1 ? B HIS 154 ND1 
122 1 Y 1 B HIS 161 ? CD2 ? B HIS 154 CD2 
123 1 Y 1 B HIS 161 ? CE1 ? B HIS 154 CE1 
124 1 Y 1 B HIS 161 ? NE2 ? B HIS 154 NE2 
125 1 Y 1 B GLN 162 ? CG  ? B GLN 155 CG  
126 1 Y 1 B GLN 162 ? CD  ? B GLN 155 CD  
127 1 Y 1 B GLN 162 ? OE1 ? B GLN 155 OE1 
128 1 Y 1 B GLN 162 ? NE2 ? B GLN 155 NE2 
129 1 Y 1 B ARG 163 ? CG  ? B ARG 156 CG  
130 1 Y 1 B ARG 163 ? CD  ? B ARG 156 CD  
131 1 Y 1 B ARG 163 ? NE  ? B ARG 156 NE  
132 1 Y 1 B ARG 163 ? CZ  ? B ARG 156 CZ  
133 1 Y 1 B ARG 163 ? NH1 ? B ARG 156 NH1 
134 1 Y 1 B ARG 163 ? NH2 ? B ARG 156 NH2 
135 1 Y 1 B GLN 164 ? CG  ? B GLN 157 CG  
136 1 Y 1 B GLN 164 ? CD  ? B GLN 157 CD  
137 1 Y 1 B GLN 164 ? OE1 ? B GLN 157 OE1 
138 1 Y 1 B GLN 164 ? NE2 ? B GLN 157 NE2 
139 1 Y 1 B LEU 165 ? CG  ? B LEU 158 CG  
140 1 Y 1 B LEU 165 ? CD1 ? B LEU 158 CD1 
141 1 Y 1 B LEU 165 ? CD2 ? B LEU 158 CD2 
142 1 Y 1 B TRP 190 ? CG  ? B TRP 183 CG  
143 1 Y 1 B TRP 190 ? CD1 ? B TRP 183 CD1 
144 1 Y 1 B TRP 190 ? CD2 ? B TRP 183 CD2 
145 1 Y 1 B TRP 190 ? NE1 ? B TRP 183 NE1 
146 1 Y 1 B TRP 190 ? CE2 ? B TRP 183 CE2 
147 1 Y 1 B TRP 190 ? CE3 ? B TRP 183 CE3 
148 1 Y 1 B TRP 190 ? CZ2 ? B TRP 183 CZ2 
149 1 Y 1 B TRP 190 ? CZ3 ? B TRP 183 CZ3 
150 1 Y 1 B TRP 190 ? CH2 ? B TRP 183 CH2 
151 1 Y 1 B LYS 191 ? CG  ? B LYS 184 CG  
152 1 Y 1 B LYS 191 ? CD  ? B LYS 184 CD  
153 1 Y 1 B LYS 191 ? CE  ? B LYS 184 CE  
154 1 Y 1 B LYS 191 ? NZ  ? B LYS 184 NZ  
155 1 Y 1 B GLU 252 ? CG  ? B GLU 245 CG  
156 1 Y 1 B GLU 252 ? CD  ? B GLU 245 CD  
157 1 Y 1 B GLU 252 ? OE1 ? B GLU 245 OE1 
158 1 Y 1 B GLU 252 ? OE2 ? B GLU 245 OE2 
159 1 Y 1 B ARG 292 ? CG  ? B ARG 285 CG  
160 1 Y 1 B ARG 292 ? CD  ? B ARG 285 CD  
161 1 Y 1 B ARG 292 ? NE  ? B ARG 285 NE  
162 1 Y 1 B ARG 292 ? CZ  ? B ARG 285 CZ  
163 1 Y 1 B ARG 292 ? NH1 ? B ARG 285 NH1 
164 1 Y 1 B ARG 292 ? NH2 ? B ARG 285 NH2 
165 1 Y 1 B LYS 293 ? CG  ? B LYS 286 CG  
166 1 Y 1 B LYS 293 ? CD  ? B LYS 286 CD  
167 1 Y 1 B LYS 293 ? CE  ? B LYS 286 CE  
168 1 Y 1 B LYS 293 ? NZ  ? B LYS 286 NZ  
169 1 Y 1 B MET 294 ? CG  ? B MET 287 CG  
170 1 Y 1 B MET 294 ? SD  ? B MET 287 SD  
171 1 Y 1 B MET 294 ? CE  ? B MET 287 CE  
172 1 Y 1 B ASP 295 ? CG  ? B ASP 288 CG  
173 1 Y 1 B ASP 295 ? OD1 ? B ASP 288 OD1 
174 1 Y 1 B ASP 295 ? OD2 ? B ASP 288 OD2 
# 
_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                     9FT7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9FT7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   9FT7 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_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                                 9FT7 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_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                            . 
_refine.ls_d_res_low                             ? 
_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                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               NONE 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_struct.entry_id                     9FT7 
_struct.title                        
'Structure of the human two pore domain potassium ion channel THIK-1 (K2P13.1) in a closed conformation' 
_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        9FT7 
_struct_keywords.text            'Potassium channel, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    KCNKD_HUMAN 
_struct_ref.pdbx_db_accession          Q9HB14 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GPGHLNEDNARFLLLAALIVLYLLGGAAVFSALELAHERQAKQRWEERLANFSRGHNLSRDELRGFLRHYEEATRAGIRV
DNVRPRWDFTGAFYFVGTVVSTIGFGMTTPATVGGKIFLIFYGLVGCSSTILFFNLFLERLITIIAYIMKSCHQRQLRRR
GALPQESLKDAGQCEVDSLAGWKPSVYYVMLILCTASILISCCASAMYTPIEGWSYFDSLYFCFVAFSTIGFGDLVSSQN
AHYESQGLYRFANFVFILMGVCCIYSLFNVISILIKQSLNWILRKMDSG
;
_struct_ref.pdbx_align_begin           9 
# 
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 9FT7 A 2 ? 290 ? Q9HB14 9 ? 297 ? 9 297 
2 1 9FT7 B 2 ? 290 ? Q9HB14 9 ? 297 ? 9 297 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9FT7 MET A 1   ? UNP Q9HB14 ? ? 'initiating methionine' 8   1  
1 9FT7 ALA A 291 ? UNP Q9HB14 ? ? 'expression tag'        298 2  
1 9FT7 GLU A 292 ? UNP Q9HB14 ? ? 'expression tag'        299 3  
1 9FT7 LEU A 293 ? UNP Q9HB14 ? ? 'expression tag'        300 4  
1 9FT7 GLU A 294 ? UNP Q9HB14 ? ? 'expression tag'        301 5  
1 9FT7 VAL A 295 ? UNP Q9HB14 ? ? 'expression tag'        302 6  
1 9FT7 LEU A 296 ? UNP Q9HB14 ? ? 'expression tag'        303 7  
1 9FT7 PHE A 297 ? UNP Q9HB14 ? ? 'expression tag'        304 8  
1 9FT7 GLN A 298 ? UNP Q9HB14 ? ? 'expression tag'        305 9  
2 9FT7 MET B 1   ? UNP Q9HB14 ? ? 'initiating methionine' 8   10 
2 9FT7 ALA B 291 ? UNP Q9HB14 ? ? 'expression tag'        298 11 
2 9FT7 GLU B 292 ? UNP Q9HB14 ? ? 'expression tag'        299 12 
2 9FT7 LEU B 293 ? UNP Q9HB14 ? ? 'expression tag'        300 13 
2 9FT7 GLU B 294 ? UNP Q9HB14 ? ? 'expression tag'        301 14 
2 9FT7 VAL B 295 ? UNP Q9HB14 ? ? 'expression tag'        302 15 
2 9FT7 LEU B 296 ? UNP Q9HB14 ? ? 'expression tag'        303 16 
2 9FT7 PHE B 297 ? UNP Q9HB14 ? ? 'expression tag'        304 17 
2 9FT7 GLN B 298 ? UNP Q9HB14 ? ? 'expression tag'        305 18 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 7   ? HIS A 57  ? ASN A 14  HIS A 64  1 ? 51 
HELX_P HELX_P2  AA2 SER A 60  ? ALA A 77  ? SER A 67  ALA A 84  1 ? 18 
HELX_P HELX_P3  AA3 ASP A 89  ? SER A 102 ? ASP A 96  SER A 109 1 ? 14 
HELX_P HELX_P4  AA4 THR A 113 ? GLN A 157 ? THR A 120 GLN A 164 1 ? 45 
HELX_P HELX_P5  AA5 SER A 186 ? GLY A 214 ? SER A 193 GLY A 221 1 ? 29 
HELX_P HELX_P6  AA6 SER A 216 ? SER A 229 ? SER A 223 SER A 236 1 ? 14 
HELX_P HELX_P7  AA7 SER A 246 ? MET A 287 ? SER A 253 MET A 294 1 ? 42 
HELX_P HELX_P8  AA8 GLU B 8   ? HIS B 57  ? GLU B 15  HIS B 64  1 ? 50 
HELX_P HELX_P9  AA9 SER B 60  ? ALA B 77  ? SER B 67  ALA B 84  1 ? 18 
HELX_P HELX_P10 AB1 ASP B 89  ? SER B 102 ? ASP B 96  SER B 109 1 ? 14 
HELX_P HELX_P11 AB2 THR B 113 ? GLN B 157 ? THR B 120 GLN B 164 1 ? 45 
HELX_P HELX_P12 AB3 SER B 186 ? GLY B 214 ? SER B 193 GLY B 221 1 ? 29 
HELX_P HELX_P13 AB4 SER B 216 ? SER B 229 ? SER B 223 SER B 236 1 ? 14 
HELX_P HELX_P14 AB5 SER B 246 ? MET B 287 ? SER B 253 MET B 294 1 ? 42 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A THR 103 O ? ? ? 1_555 E K   .   K ? ? A THR 110 A K   403 1_555 ? ? ? ? ? ? ? 2.838 ? ? 
metalc2  metalc ? ? A ILE 104 O ? ? ? 1_555 E K   .   K ? ? A ILE 111 A K   403 1_555 ? ? ? ? ? ? ? 3.013 ? ? 
metalc3  metalc ? ? A GLY 105 O ? ? ? 1_555 D K   .   K ? ? A GLY 112 A K   402 1_555 ? ? ? ? ? ? ? 3.032 ? ? 
metalc4  metalc ? ? A PHE 106 O ? ? ? 1_555 D K   .   K ? ? A PHE 113 A K   402 1_555 ? ? ? ? ? ? ? 3.157 ? ? 
metalc5  metalc ? ? A THR 230 O ? ? ? 1_555 E K   .   K ? ? A THR 237 A K   403 1_555 ? ? ? ? ? ? ? 2.806 ? ? 
metalc6  metalc ? ? A ILE 231 O ? ? ? 1_555 E K   .   K ? ? A ILE 238 A K   403 1_555 ? ? ? ? ? ? ? 2.928 ? ? 
metalc7  metalc ? ? A GLY 232 O ? ? ? 1_555 D K   .   K ? ? A GLY 239 A K   402 1_555 ? ? ? ? ? ? ? 3.022 ? ? 
metalc8  metalc ? ? A PHE 233 O ? ? ? 1_555 D K   .   K ? ? A PHE 240 A K   402 1_555 ? ? ? ? ? ? ? 2.790 ? ? 
metalc9  metalc ? ? D K   .   K ? ? ? 1_555 B GLY 105 O ? ? A K   402 B GLY 112 1_555 ? ? ? ? ? ? ? 3.030 ? ? 
metalc10 metalc ? ? D K   .   K ? ? ? 1_555 B PHE 106 O ? ? A K   402 B PHE 113 1_555 ? ? ? ? ? ? ? 3.155 ? ? 
metalc11 metalc ? ? D K   .   K ? ? ? 1_555 B GLY 232 O ? ? A K   402 B GLY 239 1_555 ? ? ? ? ? ? ? 3.022 ? ? 
metalc12 metalc ? ? D K   .   K ? ? ? 1_555 B PHE 233 O ? ? A K   402 B PHE 240 1_555 ? ? ? ? ? ? ? 2.790 ? ? 
metalc13 metalc ? ? E K   .   K ? ? ? 1_555 B THR 103 O ? ? A K   403 B THR 110 1_555 ? ? ? ? ? ? ? 2.838 ? ? 
metalc14 metalc ? ? E K   .   K ? ? ? 1_555 B ILE 104 O ? ? A K   403 B ILE 111 1_555 ? ? ? ? ? ? ? 3.013 ? ? 
metalc15 metalc ? ? E K   .   K ? ? ? 1_555 B THR 230 O ? ? A K   403 B THR 237 1_555 ? ? ? ? ? ? ? 2.806 ? ? 
metalc16 metalc ? ? E K   .   K ? ? ? 1_555 B ILE 231 O ? ? A K   403 B ILE 238 1_555 ? ? ? ? ? ? ? 2.928 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? A THR 103 ? A THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? A ILE 104 ? A ILE 111 ? 1_555 66.5  ? 
2  O ? A THR 103 ? A THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? A THR 230 ? A THR 237 ? 1_555 74.9  ? 
3  O ? A ILE 104 ? A ILE 111 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? A THR 230 ? A THR 237 ? 1_555 82.5  ? 
4  O ? A THR 103 ? A THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? A ILE 231 ? A ILE 238 ? 1_555 125.9 ? 
5  O ? A ILE 104 ? A ILE 111 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? A ILE 231 ? A ILE 238 ? 1_555 71.6  ? 
6  O ? A THR 230 ? A THR 237 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? A ILE 231 ? A ILE 238 ? 1_555 67.1  ? 
7  O ? A THR 103 ? A THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 103 ? B THR 110 ? 1_555 123.1 ? 
8  O ? A ILE 104 ? A ILE 111 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 103 ? B THR 110 ? 1_555 153.8 ? 
9  O ? A THR 230 ? A THR 237 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 103 ? B THR 110 ? 1_555 77.6  ? 
10 O ? A ILE 231 ? A ILE 238 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 103 ? B THR 110 ? 1_555 85.0  ? 
11 O ? A THR 103 ? A THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 104 ? B ILE 111 ? 1_555 153.8 ? 
12 O ? A ILE 104 ? A ILE 111 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 104 ? B ILE 111 ? 1_555 117.0 ? 
13 O ? A THR 230 ? A THR 237 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 104 ? B ILE 111 ? 1_555 130.6 ? 
14 O ? A ILE 231 ? A ILE 238 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 104 ? B ILE 111 ? 1_555 76.7  ? 
15 O ? B THR 103 ? B THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 104 ? B ILE 111 ? 1_555 66.5  ? 
16 O ? A THR 103 ? A THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 230 ? B THR 237 ? 1_555 77.6  ? 
17 O ? A ILE 104 ? A ILE 111 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 230 ? B THR 237 ? 1_555 130.6 ? 
18 O ? A THR 230 ? A THR 237 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 230 ? B THR 237 ? 1_555 120.2 ? 
19 O ? A ILE 231 ? A ILE 238 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 230 ? B THR 237 ? 1_555 155.5 ? 
20 O ? B THR 103 ? B THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 230 ? B THR 237 ? 1_555 74.9  ? 
21 O ? B ILE 104 ? B ILE 111 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B THR 230 ? B THR 237 ? 1_555 82.5  ? 
22 O ? A THR 103 ? A THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 231 ? B ILE 238 ? 1_555 85.0  ? 
23 O ? A ILE 104 ? A ILE 111 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 231 ? B ILE 238 ? 1_555 76.7  ? 
24 O ? A THR 230 ? A THR 237 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 231 ? B ILE 238 ? 1_555 155.5 ? 
25 O ? A ILE 231 ? A ILE 238 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 231 ? B ILE 238 ? 1_555 116.9 ? 
26 O ? B THR 103 ? B THR 110 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 231 ? B ILE 238 ? 1_555 125.9 ? 
27 O ? B ILE 104 ? B ILE 111 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 231 ? B ILE 238 ? 1_555 71.6  ? 
28 O ? B THR 230 ? B THR 237 ? 1_555 K ? E K . ? A K 403 ? 1_555 O ? B ILE 231 ? B ILE 238 ? 1_555 67.1  ? 
29 O ? A GLY 105 ? A GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? A PHE 106 ? A PHE 113 ? 1_555 66.6  ? 
30 O ? A GLY 105 ? A GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? A GLY 232 ? A GLY 239 ? 1_555 69.0  ? 
31 O ? A PHE 106 ? A PHE 113 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? A GLY 232 ? A GLY 239 ? 1_555 88.3  ? 
32 O ? A GLY 105 ? A GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? A PHE 233 ? A PHE 240 ? 1_555 119.7 ? 
33 O ? A PHE 106 ? A PHE 113 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? A PHE 233 ? A PHE 240 ? 1_555 68.9  ? 
34 O ? A GLY 232 ? A GLY 239 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? A PHE 233 ? A PHE 240 ? 1_555 71.0  ? 
35 O ? A GLY 105 ? A GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 105 ? B GLY 112 ? 1_555 110.6 ? 
36 O ? A PHE 106 ? A PHE 113 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 105 ? B GLY 112 ? 1_555 157.6 ? 
37 O ? A GLY 232 ? A GLY 239 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 105 ? B GLY 112 ? 1_555 70.6  ? 
38 O ? A PHE 233 ? A PHE 240 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 105 ? B GLY 112 ? 1_555 96.0  ? 
39 O ? A GLY 105 ? A GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 106 ? B PHE 113 ? 1_555 157.5 ? 
40 O ? A PHE 106 ? A PHE 113 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 106 ? B PHE 113 ? 1_555 124.7 ? 
41 O ? A GLY 232 ? A GLY 239 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 106 ? B PHE 113 ? 1_555 126.3 ? 
42 O ? A PHE 233 ? A PHE 240 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 106 ? B PHE 113 ? 1_555 82.6  ? 
43 O ? B GLY 105 ? B GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 106 ? B PHE 113 ? 1_555 66.7  ? 
44 O ? A GLY 105 ? A GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 232 ? B GLY 239 ? 1_555 70.6  ? 
45 O ? A PHE 106 ? A PHE 113 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 232 ? B GLY 239 ? 1_555 126.2 ? 
46 O ? A GLY 232 ? A GLY 239 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 232 ? B GLY 239 ? 1_555 105.4 ? 
47 O ? A PHE 233 ? A PHE 240 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 232 ? B GLY 239 ? 1_555 164.8 ? 
48 O ? B GLY 105 ? B GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 232 ? B GLY 239 ? 1_555 69.0  ? 
49 O ? B PHE 106 ? B PHE 113 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B GLY 232 ? B GLY 239 ? 1_555 88.3  ? 
50 O ? A GLY 105 ? A GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 233 ? B PHE 240 ? 1_555 96.0  ? 
51 O ? A PHE 106 ? A PHE 113 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 233 ? B PHE 240 ? 1_555 82.5  ? 
52 O ? A GLY 232 ? A GLY 239 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 233 ? B PHE 240 ? 1_555 164.7 ? 
53 O ? A PHE 233 ? A PHE 240 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 233 ? B PHE 240 ? 1_555 116.4 ? 
54 O ? B GLY 105 ? B GLY 112 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 233 ? B PHE 240 ? 1_555 119.7 ? 
55 O ? B PHE 106 ? B PHE 113 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 233 ? B PHE 240 ? 1_555 68.9  ? 
56 O ? B GLY 232 ? B GLY 239 ? 1_555 K ? D K . ? A K 402 ? 1_555 O ? B PHE 233 ? B PHE 240 ? 1_555 71.0  ? 
# 
_pdbx_entry_details.entry_id                   9FT7 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 GLU A 42  ? ? -144.86 24.98  
2 1 THR A 110 ? ? 58.65   14.09  
3 1 GLN A 247 ? ? -136.68 -30.72 
4 1 GLU B 42  ? ? -144.86 24.98  
5 1 THR B 110 ? ? 58.58   14.15  
6 1 GLN B 247 ? ? -136.66 -30.75 
# 
_space_group_symop.id              1 
_space_group_symop.operation_xyz   x,y,z 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9FT7 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           'An initial model was built manually in COOT' 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_reconstruction.entry_id                    9FT7 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.16 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               302189 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       
'20 mM HEPES pH 7.5, 200 mM KCl, 0.12% w/v OGNG, 0.012% w/v CHS, pH was adjusted using potassium hydroxide' 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'K2P13.1 homodimer' 
_em_entity_assembly.details              
'Protein generated by removal of the 10xHis and FLAG purification tags with HRV 3C protease cleavage' 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9FT7 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             2300 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             'COMA FREE' 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Au-flat 1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9FT7 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               'Grid blotted for 4 seconds' 
# 
_em_experiment.entry_id                9FT7 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9FT7 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C2 
# 
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 MET 8   ? A MET 1   
2  1 Y 1 A GLY 9   ? A GLY 2   
3  1 Y 1 A PRO 10  ? A PRO 3   
4  1 Y 1 A GLY 11  ? A GLY 4   
5  1 Y 1 A HIS 12  ? A HIS 5   
6  1 Y 1 A LEU 13  ? A LEU 6   
7  1 Y 1 A ARG 166 ? A ARG 159 
8  1 Y 1 A ARG 167 ? A ARG 160 
9  1 Y 1 A ARG 168 ? A ARG 161 
10 1 Y 1 A GLY 169 ? A GLY 162 
11 1 Y 1 A ALA 170 ? A ALA 163 
12 1 Y 1 A LEU 171 ? A LEU 164 
13 1 Y 1 A PRO 172 ? A PRO 165 
14 1 Y 1 A GLN 173 ? A GLN 166 
15 1 Y 1 A GLU 174 ? A GLU 167 
16 1 Y 1 A SER 175 ? A SER 168 
17 1 Y 1 A LEU 176 ? A LEU 169 
18 1 Y 1 A LYS 177 ? A LYS 170 
19 1 Y 1 A ASP 178 ? A ASP 171 
20 1 Y 1 A ALA 179 ? A ALA 172 
21 1 Y 1 A GLY 180 ? A GLY 173 
22 1 Y 1 A GLN 181 ? A GLN 174 
23 1 Y 1 A CYS 182 ? A CYS 175 
24 1 Y 1 A GLU 183 ? A GLU 176 
25 1 Y 1 A VAL 184 ? A VAL 177 
26 1 Y 1 A ASP 185 ? A ASP 178 
27 1 Y 1 A SER 186 ? A SER 179 
28 1 Y 1 A LEU 187 ? A LEU 180 
29 1 Y 1 A ALA 188 ? A ALA 181 
30 1 Y 1 A GLY 189 ? A GLY 182 
31 1 Y 1 A SER 296 ? A SER 289 
32 1 Y 1 A GLY 297 ? A GLY 290 
33 1 Y 1 A ALA 298 ? A ALA 291 
34 1 Y 1 A GLU 299 ? A GLU 292 
35 1 Y 1 A LEU 300 ? A LEU 293 
36 1 Y 1 A GLU 301 ? A GLU 294 
37 1 Y 1 A VAL 302 ? A VAL 295 
38 1 Y 1 A LEU 303 ? A LEU 296 
39 1 Y 1 A PHE 304 ? A PHE 297 
40 1 Y 1 A GLN 305 ? A GLN 298 
41 1 Y 1 B MET 8   ? B MET 1   
42 1 Y 1 B GLY 9   ? B GLY 2   
43 1 Y 1 B PRO 10  ? B PRO 3   
44 1 Y 1 B GLY 11  ? B GLY 4   
45 1 Y 1 B HIS 12  ? B HIS 5   
46 1 Y 1 B LEU 13  ? B LEU 6   
47 1 Y 1 B ARG 166 ? B ARG 159 
48 1 Y 1 B ARG 167 ? B ARG 160 
49 1 Y 1 B ARG 168 ? B ARG 161 
50 1 Y 1 B GLY 169 ? B GLY 162 
51 1 Y 1 B ALA 170 ? B ALA 163 
52 1 Y 1 B LEU 171 ? B LEU 164 
53 1 Y 1 B PRO 172 ? B PRO 165 
54 1 Y 1 B GLN 173 ? B GLN 166 
55 1 Y 1 B GLU 174 ? B GLU 167 
56 1 Y 1 B SER 175 ? B SER 168 
57 1 Y 1 B LEU 176 ? B LEU 169 
58 1 Y 1 B LYS 177 ? B LYS 170 
59 1 Y 1 B ASP 178 ? B ASP 171 
60 1 Y 1 B ALA 179 ? B ALA 172 
61 1 Y 1 B GLY 180 ? B GLY 173 
62 1 Y 1 B GLN 181 ? B GLN 174 
63 1 Y 1 B CYS 182 ? B CYS 175 
64 1 Y 1 B GLU 183 ? B GLU 176 
65 1 Y 1 B VAL 184 ? B VAL 177 
66 1 Y 1 B ASP 185 ? B ASP 178 
67 1 Y 1 B SER 186 ? B SER 179 
68 1 Y 1 B LEU 187 ? B LEU 180 
69 1 Y 1 B ALA 188 ? B ALA 181 
70 1 Y 1 B GLY 189 ? B GLY 182 
71 1 Y 1 B SER 296 ? B SER 289 
72 1 Y 1 B GLY 297 ? B GLY 290 
73 1 Y 1 B ALA 298 ? B ALA 291 
74 1 Y 1 B GLU 299 ? B GLU 292 
75 1 Y 1 B LEU 300 ? B LEU 293 
76 1 Y 1 B GLU 301 ? B GLU 294 
77 1 Y 1 B VAL 302 ? B VAL 295 
78 1 Y 1 B LEU 303 ? B LEU 296 
79 1 Y 1 B PHE 304 ? B PHE 297 
80 1 Y 1 B GLN 305 ? B GLN 298 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EIC C1   C N N 88  
EIC C2   C N N 89  
EIC C3   C N N 90  
EIC C4   C N N 91  
EIC C5   C N N 92  
EIC C6   C N N 93  
EIC C7   C N N 94  
EIC C8   C N N 95  
EIC C9   C N N 96  
EIC C10  C N N 97  
EIC C11  C N N 98  
EIC C12  C N N 99  
EIC C13  C N N 100 
EIC C14  C N N 101 
EIC C15  C N N 102 
EIC C16  C N N 103 
EIC C17  C N N 104 
EIC C18  C N N 105 
EIC O1   O N N 106 
EIC O2   O N N 107 
EIC H21  H N N 108 
EIC H22  H N N 109 
EIC H31  H N N 110 
EIC H32  H N N 111 
EIC H41  H N N 112 
EIC H42  H N N 113 
EIC H51  H N N 114 
EIC H52  H N N 115 
EIC H61  H N N 116 
EIC H62  H N N 117 
EIC H71  H N N 118 
EIC H72  H N N 119 
EIC H81  H N N 120 
EIC H82  H N N 121 
EIC H91  H N N 122 
EIC H1O1 H N N 123 
EIC H111 H N N 124 
EIC H112 H N N 125 
EIC H121 H N N 126 
EIC H131 H N N 127 
EIC H141 H N N 128 
EIC H142 H N N 129 
EIC H151 H N N 130 
EIC H152 H N N 131 
EIC H161 H N N 132 
EIC H162 H N N 133 
EIC H171 H N N 134 
EIC H172 H N N 135 
EIC H181 H N N 136 
EIC H182 H N N 137 
EIC H183 H N N 138 
EIC HO2  H N N 139 
GLN N    N N N 140 
GLN CA   C N S 141 
GLN C    C N N 142 
GLN O    O N N 143 
GLN CB   C N N 144 
GLN CG   C N N 145 
GLN CD   C N N 146 
GLN OE1  O N N 147 
GLN NE2  N N N 148 
GLN OXT  O N N 149 
GLN H    H N N 150 
GLN H2   H N N 151 
GLN HA   H N N 152 
GLN HB2  H N N 153 
GLN HB3  H N N 154 
GLN HG2  H N N 155 
GLN HG3  H N N 156 
GLN HE21 H N N 157 
GLN HE22 H N N 158 
GLN HXT  H N N 159 
GLU N    N N N 160 
GLU CA   C N S 161 
GLU C    C N N 162 
GLU O    O N N 163 
GLU CB   C N N 164 
GLU CG   C N N 165 
GLU CD   C N N 166 
GLU OE1  O N N 167 
GLU OE2  O N N 168 
GLU OXT  O N N 169 
GLU H    H N N 170 
GLU H2   H N N 171 
GLU HA   H N N 172 
GLU HB2  H N N 173 
GLU HB3  H N N 174 
GLU HG2  H N N 175 
GLU HG3  H N N 176 
GLU HE2  H N N 177 
GLU HXT  H N N 178 
GLY N    N N N 179 
GLY CA   C N N 180 
GLY C    C N N 181 
GLY O    O N N 182 
GLY OXT  O N N 183 
GLY H    H N N 184 
GLY H2   H N N 185 
GLY HA2  H N N 186 
GLY HA3  H N N 187 
GLY HXT  H N N 188 
HIS N    N N N 189 
HIS CA   C N S 190 
HIS C    C N N 191 
HIS O    O N N 192 
HIS CB   C N N 193 
HIS CG   C Y N 194 
HIS ND1  N Y N 195 
HIS CD2  C Y N 196 
HIS CE1  C Y N 197 
HIS NE2  N Y N 198 
HIS OXT  O N N 199 
HIS H    H N N 200 
HIS H2   H N N 201 
HIS HA   H N N 202 
HIS HB2  H N N 203 
HIS HB3  H N N 204 
HIS HD1  H N N 205 
HIS HD2  H N N 206 
HIS HE1  H N N 207 
HIS HE2  H N N 208 
HIS HXT  H N N 209 
ILE N    N N N 210 
ILE CA   C N S 211 
ILE C    C N N 212 
ILE O    O N N 213 
ILE CB   C N S 214 
ILE CG1  C N N 215 
ILE CG2  C N N 216 
ILE CD1  C N N 217 
ILE OXT  O N N 218 
ILE H    H N N 219 
ILE H2   H N N 220 
ILE HA   H N N 221 
ILE HB   H N N 222 
ILE HG12 H N N 223 
ILE HG13 H N N 224 
ILE HG21 H N N 225 
ILE HG22 H N N 226 
ILE HG23 H N N 227 
ILE HD11 H N N 228 
ILE HD12 H N N 229 
ILE HD13 H N N 230 
ILE HXT  H N N 231 
K   K    K N N 232 
LEU N    N N N 233 
LEU CA   C N S 234 
LEU C    C N N 235 
LEU O    O N N 236 
LEU CB   C N N 237 
LEU CG   C N N 238 
LEU CD1  C N N 239 
LEU CD2  C N N 240 
LEU OXT  O N N 241 
LEU H    H N N 242 
LEU H2   H N N 243 
LEU HA   H N N 244 
LEU HB2  H N N 245 
LEU HB3  H N N 246 
LEU HG   H N N 247 
LEU HD11 H N N 248 
LEU HD12 H N N 249 
LEU HD13 H N N 250 
LEU HD21 H N N 251 
LEU HD22 H N N 252 
LEU HD23 H N N 253 
LEU HXT  H N N 254 
LYS N    N N N 255 
LYS CA   C N S 256 
LYS C    C N N 257 
LYS O    O N N 258 
LYS CB   C N N 259 
LYS CG   C N N 260 
LYS CD   C N N 261 
LYS CE   C N N 262 
LYS NZ   N N N 263 
LYS OXT  O N N 264 
LYS H    H N N 265 
LYS H2   H N N 266 
LYS HA   H N N 267 
LYS HB2  H N N 268 
LYS HB3  H N N 269 
LYS HG2  H N N 270 
LYS HG3  H N N 271 
LYS HD2  H N N 272 
LYS HD3  H N N 273 
LYS HE2  H N N 274 
LYS HE3  H N N 275 
LYS HZ1  H N N 276 
LYS HZ2  H N N 277 
LYS HZ3  H N N 278 
LYS HXT  H N N 279 
MET N    N N N 280 
MET CA   C N S 281 
MET C    C N N 282 
MET O    O N N 283 
MET CB   C N N 284 
MET CG   C N N 285 
MET SD   S N N 286 
MET CE   C N N 287 
MET OXT  O N N 288 
MET H    H N N 289 
MET H2   H N N 290 
MET HA   H N N 291 
MET HB2  H N N 292 
MET HB3  H N N 293 
MET HG2  H N N 294 
MET HG3  H N N 295 
MET HE1  H N N 296 
MET HE2  H N N 297 
MET HE3  H N N 298 
MET HXT  H N N 299 
PHE N    N N N 300 
PHE CA   C N S 301 
PHE C    C N N 302 
PHE O    O N N 303 
PHE CB   C N N 304 
PHE CG   C Y N 305 
PHE CD1  C Y N 306 
PHE CD2  C Y N 307 
PHE CE1  C Y N 308 
PHE CE2  C Y N 309 
PHE CZ   C Y N 310 
PHE OXT  O N N 311 
PHE H    H N N 312 
PHE H2   H N N 313 
PHE HA   H N N 314 
PHE HB2  H N N 315 
PHE HB3  H N N 316 
PHE HD1  H N N 317 
PHE HD2  H N N 318 
PHE HE1  H N N 319 
PHE HE2  H N N 320 
PHE HZ   H N N 321 
PHE HXT  H N N 322 
PRO N    N N N 323 
PRO CA   C N S 324 
PRO C    C N N 325 
PRO O    O N N 326 
PRO CB   C N N 327 
PRO CG   C N N 328 
PRO CD   C N N 329 
PRO OXT  O N N 330 
PRO H    H N N 331 
PRO HA   H N N 332 
PRO HB2  H N N 333 
PRO HB3  H N N 334 
PRO HG2  H N N 335 
PRO HG3  H N N 336 
PRO HD2  H N N 337 
PRO HD3  H N N 338 
PRO HXT  H N N 339 
SER N    N N N 340 
SER CA   C N S 341 
SER C    C N N 342 
SER O    O N N 343 
SER CB   C N N 344 
SER OG   O N N 345 
SER OXT  O N N 346 
SER H    H N N 347 
SER H2   H N N 348 
SER HA   H N N 349 
SER HB2  H N N 350 
SER HB3  H N N 351 
SER HG   H N N 352 
SER HXT  H N N 353 
THR N    N N N 354 
THR CA   C N S 355 
THR C    C N N 356 
THR O    O N N 357 
THR CB   C N R 358 
THR OG1  O N N 359 
THR CG2  C N N 360 
THR OXT  O N N 361 
THR H    H N N 362 
THR H2   H N N 363 
THR HA   H N N 364 
THR HB   H N N 365 
THR HG1  H N N 366 
THR HG21 H N N 367 
THR HG22 H N N 368 
THR HG23 H N N 369 
THR HXT  H N N 370 
TRP N    N N N 371 
TRP CA   C N S 372 
TRP C    C N N 373 
TRP O    O N N 374 
TRP CB   C N N 375 
TRP CG   C Y N 376 
TRP CD1  C Y N 377 
TRP CD2  C Y N 378 
TRP NE1  N Y N 379 
TRP CE2  C Y N 380 
TRP CE3  C Y N 381 
TRP CZ2  C Y N 382 
TRP CZ3  C Y N 383 
TRP CH2  C Y N 384 
TRP OXT  O N N 385 
TRP H    H N N 386 
TRP H2   H N N 387 
TRP HA   H N N 388 
TRP HB2  H N N 389 
TRP HB3  H N N 390 
TRP HD1  H N N 391 
TRP HE1  H N N 392 
TRP HE3  H N N 393 
TRP HZ2  H N N 394 
TRP HZ3  H N N 395 
TRP HH2  H N N 396 
TRP HXT  H N N 397 
TYR N    N N N 398 
TYR CA   C N S 399 
TYR C    C N N 400 
TYR O    O N N 401 
TYR CB   C N N 402 
TYR CG   C Y N 403 
TYR CD1  C Y N 404 
TYR CD2  C Y N 405 
TYR CE1  C Y N 406 
TYR CE2  C Y N 407 
TYR CZ   C Y N 408 
TYR OH   O N N 409 
TYR OXT  O N N 410 
TYR H    H N N 411 
TYR H2   H N N 412 
TYR HA   H N N 413 
TYR HB2  H N N 414 
TYR HB3  H N N 415 
TYR HD1  H N N 416 
TYR HD2  H N N 417 
TYR HE1  H N N 418 
TYR HE2  H N N 419 
TYR HH   H N N 420 
TYR HXT  H N N 421 
VAL N    N N N 422 
VAL CA   C N S 423 
VAL C    C N N 424 
VAL O    O N N 425 
VAL CB   C N N 426 
VAL CG1  C N N 427 
VAL CG2  C N N 428 
VAL OXT  O N N 429 
VAL H    H N N 430 
VAL H2   H N N 431 
VAL HA   H N N 432 
VAL HB   H N N 433 
VAL HG11 H N N 434 
VAL HG12 H N N 435 
VAL HG13 H N N 436 
VAL HG21 H N N 437 
VAL HG22 H N N 438 
VAL HG23 H N N 439 
VAL HXT  H N N 440 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EIC C1  C2   sing N N 83  
EIC C1  O1   doub N N 84  
EIC C1  O2   sing N N 85  
EIC C2  C3   sing N N 86  
EIC C2  H21  sing N N 87  
EIC C2  H22  sing N N 88  
EIC C3  C4   sing N N 89  
EIC C3  H31  sing N N 90  
EIC C3  H32  sing N N 91  
EIC C4  C5   sing N N 92  
EIC C4  H41  sing N N 93  
EIC C4  H42  sing N N 94  
EIC C5  C6   sing N N 95  
EIC C5  H51  sing N N 96  
EIC C5  H52  sing N N 97  
EIC C6  C7   sing N N 98  
EIC C6  H61  sing N N 99  
EIC C6  H62  sing N N 100 
EIC C7  C8   sing N N 101 
EIC C7  H71  sing N N 102 
EIC C7  H72  sing N N 103 
EIC C8  C9   sing N N 104 
EIC C8  H81  sing N N 105 
EIC C8  H82  sing N N 106 
EIC C9  C10  doub N Z 107 
EIC C9  H91  sing N N 108 
EIC C10 C11  sing N N 109 
EIC C10 H1O1 sing N N 110 
EIC C11 C12  sing N N 111 
EIC C11 H111 sing N N 112 
EIC C11 H112 sing N N 113 
EIC C12 C13  doub N Z 114 
EIC C12 H121 sing N N 115 
EIC C13 C14  sing N N 116 
EIC C13 H131 sing N N 117 
EIC C14 C15  sing N N 118 
EIC C14 H141 sing N N 119 
EIC C14 H142 sing N N 120 
EIC C15 C16  sing N N 121 
EIC C15 H151 sing N N 122 
EIC C15 H152 sing N N 123 
EIC C16 C17  sing N N 124 
EIC C16 H161 sing N N 125 
EIC C16 H162 sing N N 126 
EIC C17 C18  sing N N 127 
EIC C17 H171 sing N N 128 
EIC C17 H172 sing N N 129 
EIC C18 H181 sing N N 130 
EIC C18 H182 sing N N 131 
EIC C18 H183 sing N N 132 
EIC O2  HO2  sing N N 133 
GLN N   CA   sing N N 134 
GLN N   H    sing N N 135 
GLN N   H2   sing N N 136 
GLN CA  C    sing N N 137 
GLN CA  CB   sing N N 138 
GLN CA  HA   sing N N 139 
GLN C   O    doub N N 140 
GLN C   OXT  sing N N 141 
GLN CB  CG   sing N N 142 
GLN CB  HB2  sing N N 143 
GLN CB  HB3  sing N N 144 
GLN CG  CD   sing N N 145 
GLN CG  HG2  sing N N 146 
GLN CG  HG3  sing N N 147 
GLN CD  OE1  doub N N 148 
GLN CD  NE2  sing N N 149 
GLN NE2 HE21 sing N N 150 
GLN NE2 HE22 sing N N 151 
GLN OXT HXT  sing N N 152 
GLU N   CA   sing N N 153 
GLU N   H    sing N N 154 
GLU N   H2   sing N N 155 
GLU CA  C    sing N N 156 
GLU CA  CB   sing N N 157 
GLU CA  HA   sing N N 158 
GLU C   O    doub N N 159 
GLU C   OXT  sing N N 160 
GLU CB  CG   sing N N 161 
GLU CB  HB2  sing N N 162 
GLU CB  HB3  sing N N 163 
GLU CG  CD   sing N N 164 
GLU CG  HG2  sing N N 165 
GLU CG  HG3  sing N N 166 
GLU CD  OE1  doub N N 167 
GLU CD  OE2  sing N N 168 
GLU OE2 HE2  sing N N 169 
GLU OXT HXT  sing N N 170 
GLY N   CA   sing N N 171 
GLY N   H    sing N N 172 
GLY N   H2   sing N N 173 
GLY CA  C    sing N N 174 
GLY CA  HA2  sing N N 175 
GLY CA  HA3  sing N N 176 
GLY C   O    doub N N 177 
GLY C   OXT  sing N N 178 
GLY OXT HXT  sing N N 179 
HIS N   CA   sing N N 180 
HIS N   H    sing N N 181 
HIS N   H2   sing N N 182 
HIS CA  C    sing N N 183 
HIS CA  CB   sing N N 184 
HIS CA  HA   sing N N 185 
HIS C   O    doub N N 186 
HIS C   OXT  sing N N 187 
HIS CB  CG   sing N N 188 
HIS CB  HB2  sing N N 189 
HIS CB  HB3  sing N N 190 
HIS CG  ND1  sing Y N 191 
HIS CG  CD2  doub Y N 192 
HIS ND1 CE1  doub Y N 193 
HIS ND1 HD1  sing N N 194 
HIS CD2 NE2  sing Y N 195 
HIS CD2 HD2  sing N N 196 
HIS CE1 NE2  sing Y N 197 
HIS CE1 HE1  sing N N 198 
HIS NE2 HE2  sing N N 199 
HIS OXT HXT  sing N N 200 
ILE N   CA   sing N N 201 
ILE N   H    sing N N 202 
ILE N   H2   sing N N 203 
ILE CA  C    sing N N 204 
ILE CA  CB   sing N N 205 
ILE CA  HA   sing N N 206 
ILE C   O    doub N N 207 
ILE C   OXT  sing N N 208 
ILE CB  CG1  sing N N 209 
ILE CB  CG2  sing N N 210 
ILE CB  HB   sing N N 211 
ILE CG1 CD1  sing N N 212 
ILE CG1 HG12 sing N N 213 
ILE CG1 HG13 sing N N 214 
ILE CG2 HG21 sing N N 215 
ILE CG2 HG22 sing N N 216 
ILE CG2 HG23 sing N N 217 
ILE CD1 HD11 sing N N 218 
ILE CD1 HD12 sing N N 219 
ILE CD1 HD13 sing N N 220 
ILE OXT HXT  sing N N 221 
LEU N   CA   sing N N 222 
LEU N   H    sing N N 223 
LEU N   H2   sing N N 224 
LEU CA  C    sing N N 225 
LEU CA  CB   sing N N 226 
LEU CA  HA   sing N N 227 
LEU C   O    doub N N 228 
LEU C   OXT  sing N N 229 
LEU CB  CG   sing N N 230 
LEU CB  HB2  sing N N 231 
LEU CB  HB3  sing N N 232 
LEU CG  CD1  sing N N 233 
LEU CG  CD2  sing N N 234 
LEU CG  HG   sing N N 235 
LEU CD1 HD11 sing N N 236 
LEU CD1 HD12 sing N N 237 
LEU CD1 HD13 sing N N 238 
LEU CD2 HD21 sing N N 239 
LEU CD2 HD22 sing N N 240 
LEU CD2 HD23 sing N N 241 
LEU OXT HXT  sing N N 242 
LYS N   CA   sing N N 243 
LYS N   H    sing N N 244 
LYS N   H2   sing N N 245 
LYS CA  C    sing N N 246 
LYS CA  CB   sing N N 247 
LYS CA  HA   sing N N 248 
LYS C   O    doub N N 249 
LYS C   OXT  sing N N 250 
LYS CB  CG   sing N N 251 
LYS CB  HB2  sing N N 252 
LYS CB  HB3  sing N N 253 
LYS CG  CD   sing N N 254 
LYS CG  HG2  sing N N 255 
LYS CG  HG3  sing N N 256 
LYS CD  CE   sing N N 257 
LYS CD  HD2  sing N N 258 
LYS CD  HD3  sing N N 259 
LYS CE  NZ   sing N N 260 
LYS CE  HE2  sing N N 261 
LYS CE  HE3  sing N N 262 
LYS NZ  HZ1  sing N N 263 
LYS NZ  HZ2  sing N N 264 
LYS NZ  HZ3  sing N N 265 
LYS OXT HXT  sing N N 266 
MET N   CA   sing N N 267 
MET N   H    sing N N 268 
MET N   H2   sing N N 269 
MET CA  C    sing N N 270 
MET CA  CB   sing N N 271 
MET CA  HA   sing N N 272 
MET C   O    doub N N 273 
MET C   OXT  sing N N 274 
MET CB  CG   sing N N 275 
MET CB  HB2  sing N N 276 
MET CB  HB3  sing N N 277 
MET CG  SD   sing N N 278 
MET CG  HG2  sing N N 279 
MET CG  HG3  sing N N 280 
MET SD  CE   sing N N 281 
MET CE  HE1  sing N N 282 
MET CE  HE2  sing N N 283 
MET CE  HE3  sing N N 284 
MET OXT HXT  sing N N 285 
PHE N   CA   sing N N 286 
PHE N   H    sing N N 287 
PHE N   H2   sing N N 288 
PHE CA  C    sing N N 289 
PHE CA  CB   sing N N 290 
PHE CA  HA   sing N N 291 
PHE C   O    doub N N 292 
PHE C   OXT  sing N N 293 
PHE CB  CG   sing N N 294 
PHE CB  HB2  sing N N 295 
PHE CB  HB3  sing N N 296 
PHE CG  CD1  doub Y N 297 
PHE CG  CD2  sing Y N 298 
PHE CD1 CE1  sing Y N 299 
PHE CD1 HD1  sing N N 300 
PHE CD2 CE2  doub Y N 301 
PHE CD2 HD2  sing N N 302 
PHE CE1 CZ   doub Y N 303 
PHE CE1 HE1  sing N N 304 
PHE CE2 CZ   sing Y N 305 
PHE CE2 HE2  sing N N 306 
PHE CZ  HZ   sing N N 307 
PHE OXT HXT  sing N N 308 
PRO N   CA   sing N N 309 
PRO N   CD   sing N N 310 
PRO N   H    sing N N 311 
PRO CA  C    sing N N 312 
PRO CA  CB   sing N N 313 
PRO CA  HA   sing N N 314 
PRO C   O    doub N N 315 
PRO C   OXT  sing N N 316 
PRO CB  CG   sing N N 317 
PRO CB  HB2  sing N N 318 
PRO CB  HB3  sing N N 319 
PRO CG  CD   sing N N 320 
PRO CG  HG2  sing N N 321 
PRO CG  HG3  sing N N 322 
PRO CD  HD2  sing N N 323 
PRO CD  HD3  sing N N 324 
PRO OXT HXT  sing N N 325 
SER N   CA   sing N N 326 
SER N   H    sing N N 327 
SER N   H2   sing N N 328 
SER CA  C    sing N N 329 
SER CA  CB   sing N N 330 
SER CA  HA   sing N N 331 
SER C   O    doub N N 332 
SER C   OXT  sing N N 333 
SER CB  OG   sing N N 334 
SER CB  HB2  sing N N 335 
SER CB  HB3  sing N N 336 
SER OG  HG   sing N N 337 
SER OXT HXT  sing N N 338 
THR N   CA   sing N N 339 
THR N   H    sing N N 340 
THR N   H2   sing N N 341 
THR CA  C    sing N N 342 
THR CA  CB   sing N N 343 
THR CA  HA   sing N N 344 
THR C   O    doub N N 345 
THR C   OXT  sing N N 346 
THR CB  OG1  sing N N 347 
THR CB  CG2  sing N N 348 
THR CB  HB   sing N N 349 
THR OG1 HG1  sing N N 350 
THR CG2 HG21 sing N N 351 
THR CG2 HG22 sing N N 352 
THR CG2 HG23 sing N N 353 
THR OXT HXT  sing N N 354 
TRP N   CA   sing N N 355 
TRP N   H    sing N N 356 
TRP N   H2   sing N N 357 
TRP CA  C    sing N N 358 
TRP CA  CB   sing N N 359 
TRP CA  HA   sing N N 360 
TRP C   O    doub N N 361 
TRP C   OXT  sing N N 362 
TRP CB  CG   sing N N 363 
TRP CB  HB2  sing N N 364 
TRP CB  HB3  sing N N 365 
TRP CG  CD1  doub Y N 366 
TRP CG  CD2  sing Y N 367 
TRP CD1 NE1  sing Y N 368 
TRP CD1 HD1  sing N N 369 
TRP CD2 CE2  doub Y N 370 
TRP CD2 CE3  sing Y N 371 
TRP NE1 CE2  sing Y N 372 
TRP NE1 HE1  sing N N 373 
TRP CE2 CZ2  sing Y N 374 
TRP CE3 CZ3  doub Y N 375 
TRP CE3 HE3  sing N N 376 
TRP CZ2 CH2  doub Y N 377 
TRP CZ2 HZ2  sing N N 378 
TRP CZ3 CH2  sing Y N 379 
TRP CZ3 HZ3  sing N N 380 
TRP CH2 HH2  sing N N 381 
TRP OXT HXT  sing N N 382 
TYR N   CA   sing N N 383 
TYR N   H    sing N N 384 
TYR N   H2   sing N N 385 
TYR CA  C    sing N N 386 
TYR CA  CB   sing N N 387 
TYR CA  HA   sing N N 388 
TYR C   O    doub N N 389 
TYR C   OXT  sing N N 390 
TYR CB  CG   sing N N 391 
TYR CB  HB2  sing N N 392 
TYR CB  HB3  sing N N 393 
TYR CG  CD1  doub Y N 394 
TYR CG  CD2  sing Y N 395 
TYR CD1 CE1  sing Y N 396 
TYR CD1 HD1  sing N N 397 
TYR CD2 CE2  doub Y N 398 
TYR CD2 HD2  sing N N 399 
TYR CE1 CZ   doub Y N 400 
TYR CE1 HE1  sing N N 401 
TYR CE2 CZ   sing Y N 402 
TYR CE2 HE2  sing N N 403 
TYR CZ  OH   sing N N 404 
TYR OH  HH   sing N N 405 
TYR OXT HXT  sing N N 406 
VAL N   CA   sing N N 407 
VAL N   H    sing N N 408 
VAL N   H2   sing N N 409 
VAL CA  C    sing N N 410 
VAL CA  CB   sing N N 411 
VAL CA  HA   sing N N 412 
VAL C   O    doub N N 413 
VAL C   OXT  sing N N 414 
VAL CB  CG1  sing N N 415 
VAL CB  CG2  sing N N 416 
VAL CB  HB   sing N N 417 
VAL CG1 HG11 sing N N 418 
VAL CG1 HG12 sing N N 419 
VAL CG1 HG13 sing N N 420 
VAL CG2 HG21 sing N N 421 
VAL CG2 HG22 sing N N 422 
VAL CG2 HG23 sing N N 423 
VAL OXT HXT  sing N N 424 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-06-24 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           9FT7 
_em_admin.last_update        2025-03-05 
_em_admin.map_release_date   2025-03-05 
_em_admin.title              
'Structure of the human two pore domain potassium ion channel THIK-1 (K2P13.1) in a closed conformation' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20    mM      C8H18N2O4S       1 '4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acid' 
1 200   mM      KCl              2 'potassium chloride'                                 
1 0.12  '% w/v' C27H52O12        3 'octyl glucose neopentyl glycol'                     
1 0.012 '% w/v' C31H50O4C4H11NO3 4 'cholesteryl hemisuccinate tris salt'                
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.67 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               Sf9 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         42.54 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    1 
_em_image_recording.num_real_images                     21171 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          'GIF Bioquantum' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? cryoSPARC 4.2.1       
'IMAGE ACQUISITION'        ? 2  ? ? 1 EPU       ?           
MASKING                    ? 3  ? ? ? ?         ?           
'CTF CORRECTION'           ? 4  1 ? ? cryoSPARC 4.2.1       
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ?           
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ?           
'MODEL FITTING'            ? 7  ? 1 ? ?         ?           
OTHER                      ? 8  ? ? ? ?         ?           
'MODEL REFINEMENT'         ? 9  ? 1 ? PHENIX    1.20.1-4487 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? cryoSPARC 4.4.0       
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? cryoSPARC 4.4.0       
CLASSIFICATION             ? 12 1 ? ? ?         ?           
RECONSTRUCTION             ? 13 1 ? ? cryoSPARC 4.4.0       
# 
_em_specimen.concentration           4 
_em_specimen.details                 'Monodisperse sample.' 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/T002018/1  1 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' BB/S008608/1  2 
'Medical Research Council (MRC, United Kingdom)'                 'United Kingdom' MR/W017741/1  3 
'Wellcome Trust'                                                 'United Kingdom' WT084655MA    4 
'Wellcome Trust'                                                 'United Kingdom' 102161/B/13/Z 5 
# 
_space_group.crystal_system   triclinic 
_space_group.name_H-M_alt     'P 1' 
_space_group.IT_number        1 
_space_group.name_Hall        'P 1' 
_space_group.id               1 
# 
_atom_sites.entry_id                    9FT7 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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 
K 
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   . ASN A 1 7   ? 95.21900  124.98600 131.01100 1.000 87.81890  ? 14  ASN A N   1 
ATOM   2    C CA  . ASN A 1 7   ? 96.18700  124.04900 131.56500 1.000 88.26924  ? 14  ASN A CA  1 
ATOM   3    C C   . ASN A 1 7   ? 97.43800  123.99600 130.70100 1.000 85.16741  ? 14  ASN A C   1 
ATOM   4    O O   . ASN A 1 7   ? 97.36300  124.15400 129.48500 1.000 85.56467  ? 14  ASN A O   1 
ATOM   5    C CB  . ASN A 1 7   ? 95.57400  122.65500 131.69200 1.000 85.61518  ? 14  ASN A CB  1 
ATOM   6    N N   . GLU A 1 8   ? 98.59000  123.78400 131.34200 1.000 82.70436  ? 15  GLU A N   1 
ATOM   7    C CA  . GLU A 1 8   ? 99.86500  123.90200 130.64300 1.000 83.32995  ? 15  GLU A CA  1 
ATOM   8    C C   . GLU A 1 8   ? 99.99400  122.89100 129.51100 1.000 86.65883  ? 15  GLU A C   1 
ATOM   9    O O   . GLU A 1 8   ? 100.68300 123.15600 128.52200 1.000 89.38988  ? 15  GLU A O   1 
ATOM   10   C CB  . GLU A 1 8   ? 101.02200 123.74100 131.62700 1.000 81.82936  ? 15  GLU A CB  1 
ATOM   11   N N   . ASP A 1 9   ? 99.34100  121.73400 129.63200 1.000 85.65033  ? 16  ASP A N   1 
ATOM   12   C CA  . ASP A 1 9   ? 99.39700  120.74200 128.56300 1.000 82.71240  ? 16  ASP A CA  1 
ATOM   13   C C   . ASP A 1 9   ? 98.66700  121.21100 127.30900 1.000 84.65277  ? 16  ASP A C   1 
ATOM   14   O O   . ASP A 1 9   ? 99.14500  120.99600 126.18700 1.000 88.43550  ? 16  ASP A O   1 
ATOM   15   C CB  . ASP A 1 9   ? 98.81200  119.42000 129.05100 1.000 81.12377  ? 16  ASP A CB  1 
ATOM   16   C CG  . ASP A 1 9   ? 99.61700  118.80700 130.17500 1.000 86.24990  ? 16  ASP A CG  1 
ATOM   17   O OD1 . ASP A 1 9   ? 100.85900 118.91500 130.14200 1.000 87.06780  ? 16  ASP A OD1 1 
ATOM   18   O OD2 . ASP A 1 9   ? 99.00900  118.21400 131.08900 1.000 88.29638  ? 16  ASP A OD2 1 
ATOM   19   N N   . ASN A 1 10  ? 97.55700  121.92900 127.47400 1.000 76.08611  ? 17  ASN A N   1 
ATOM   20   C CA  . ASN A 1 10  ? 96.89600  122.51100 126.31300 1.000 74.52542  ? 17  ASN A CA  1 
ATOM   21   C C   . ASN A 1 10  ? 97.71500  123.64300 125.71400 1.000 72.72662  ? 17  ASN A C   1 
ATOM   22   O O   . ASN A 1 10  ? 97.75900  123.79900 124.48800 1.000 72.97372  ? 17  ASN A O   1 
ATOM   23   C CB  . ASN A 1 10  ? 95.50400  123.00500 126.69800 1.000 78.82149  ? 17  ASN A CB  1 
ATOM   24   C CG  . ASN A 1 10  ? 94.54200  121.87000 126.97400 1.000 82.36661  ? 17  ASN A CG  1 
ATOM   25   O OD1 . ASN A 1 10  ? 94.91300  120.69900 126.91500 1.000 82.44957  ? 17  ASN A OD1 1 
ATOM   26   N ND2 . ASN A 1 10  ? 93.29700  122.21200 127.27800 1.000 82.75437  ? 17  ASN A ND2 1 
ATOM   27   N N   . ALA A 1 11  ? 98.35400  124.45400 126.55300 1.000 67.11800  ? 18  ALA A N   1 
ATOM   28   C CA  . ALA A 1 11  ? 99.19100  125.52000 126.02100 1.000 67.38551  ? 18  ALA A CA  1 
ATOM   29   C C   . ALA A 1 11  ? 100.35300 124.95400 125.22100 1.000 67.50475  ? 18  ALA A C   1 
ATOM   30   O O   . ALA A 1 11  ? 100.66800 125.45100 124.13600 1.000 74.79622  ? 18  ALA A O   1 
ATOM   31   C CB  . ALA A 1 11  ? 99.70200  126.40600 127.15400 1.000 72.18495  ? 18  ALA A CB  1 
ATOM   32   N N   . ARG A 1 12  ? 100.97600 123.88500 125.72200 1.000 69.64241  ? 19  ARG A N   1 
ATOM   33   C CA  . ARG A 1 12  ? 102.03300 123.21000 124.97300 1.000 68.58924  ? 19  ARG A CA  1 
ATOM   34   C C   . ARG A 1 12  ? 101.52800 122.63300 123.65800 1.000 67.86701  ? 19  ARG A C   1 
ATOM   35   O O   . ARG A 1 12  ? 102.18800 122.76700 122.62300 1.000 67.03667  ? 19  ARG A O   1 
ATOM   36   C CB  . ARG A 1 12  ? 102.65300 122.10300 125.81900 1.000 67.09535  ? 19  ARG A CB  1 
ATOM   37   C CG  . ARG A 1 12  ? 103.92200 121.54000 125.22400 1.000 71.83036  ? 19  ARG A CG  1 
ATOM   38   C CD  . ARG A 1 12  ? 104.37300 120.26900 125.92200 1.000 74.52296  ? 19  ARG A CD  1 
ATOM   39   N NE  . ARG A 1 12  ? 104.62000 120.46000 127.34500 1.000 72.41148  ? 19  ARG A NE  1 
ATOM   40   C CZ  . ARG A 1 12  ? 103.83400 120.00000 128.30600 1.000 74.11989  ? 19  ARG A CZ  1 
ATOM   41   N NH1 . ARG A 1 12  ? 102.74200 119.30800 128.03200 1.000 74.65471  ? 19  ARG A NH1 1 
ATOM   42   N NH2 . ARG A 1 12  ? 104.15600 120.23500 129.57400 1.000 75.06736  ? 19  ARG A NH2 1 
ATOM   43   N N   . PHE A 1 13  ? 100.35300 122.00600 123.67000 1.000 64.23815  ? 20  PHE A N   1 
ATOM   44   C CA  . PHE A 1 13  ? 99.82100  121.41400 122.44600 1.000 59.64659  ? 20  PHE A CA  1 
ATOM   45   C C   . PHE A 1 13  ? 99.50100  122.46400 121.38500 1.000 63.06004  ? 20  PHE A C   1 
ATOM   46   O O   . PHE A 1 13  ? 99.88500  122.31800 120.21600 1.000 66.62571  ? 20  PHE A O   1 
ATOM   47   C CB  . PHE A 1 13  ? 98.57900  120.59800 122.78500 1.000 57.26760  ? 20  PHE A CB  1 
ATOM   48   C CG  . PHE A 1 13  ? 97.95900  119.92000 121.61200 1.000 58.32008  ? 20  PHE A CG  1 
ATOM   49   C CD1 . PHE A 1 13  ? 98.63800  118.93200 120.93500 1.000 59.89346  ? 20  PHE A CD1 1 
ATOM   50   C CD2 . PHE A 1 13  ? 96.69000  120.25600 121.19500 1.000 63.34499  ? 20  PHE A CD2 1 
ATOM   51   C CE1 . PHE A 1 13  ? 98.06500  118.29700 119.86500 1.000 59.78041  ? 20  PHE A CE1 1 
ATOM   52   C CE2 . PHE A 1 13  ? 96.11300  119.62400 120.12100 1.000 64.91825  ? 20  PHE A CE2 1 
ATOM   53   C CZ  . PHE A 1 13  ? 96.80300  118.64400 119.45500 1.000 64.00536  ? 20  PHE A CZ  1 
ATOM   54   N N   . LEU A 1 14  ? 98.82700  123.54800 121.77300 1.000 62.07530  ? 21  LEU A N   1 
ATOM   55   C CA  . LEU A 1 14  ? 98.53800  124.62000 120.82100 1.000 57.75089  ? 21  LEU A CA  1 
ATOM   56   C C   . LEU A 1 14  ? 99.79900  125.33900 120.34700 1.000 56.62008  ? 21  LEU A C   1 
ATOM   57   O O   . LEU A 1 14  ? 99.91300  125.67700 119.16100 1.000 61.48561  ? 21  LEU A O   1 
ATOM   58   C CB  . LEU A 1 14  ? 97.56200  125.61900 121.43800 1.000 60.66752  ? 21  LEU A CB  1 
ATOM   59   C CG  . LEU A 1 14  ? 96.06500  125.39400 121.21100 1.000 60.79015  ? 21  LEU A CG  1 
ATOM   60   C CD1 . LEU A 1 14  ? 95.62200  124.02000 121.67300 1.000 59.45192  ? 21  LEU A CD1 1 
ATOM   61   C CD2 . LEU A 1 14  ? 95.26600  126.47200 121.91800 1.000 56.85591  ? 21  LEU A CD2 1 
ATOM   62   N N   . LEU A 1 15  ? 100.76400 125.56600 121.23900 1.000 52.01189  ? 22  LEU A N   1 
ATOM   63   C CA  . LEU A 1 15  ? 102.01900 126.17700 120.82100 1.000 51.05435  ? 22  LEU A CA  1 
ATOM   64   C C   . LEU A 1 15  ? 102.75900 125.30800 119.81800 1.000 55.59250  ? 22  LEU A C   1 
ATOM   65   O O   . LEU A 1 15  ? 103.29600 125.81600 118.82700 1.000 65.80307  ? 22  LEU A O   1 
ATOM   66   C CB  . LEU A 1 15  ? 102.89500 126.45700 122.03800 1.000 52.21260  ? 22  LEU A CB  1 
ATOM   67   C CG  . LEU A 1 15  ? 104.28300 127.02400 121.75700 1.000 50.91294  ? 22  LEU A CG  1 
ATOM   68   C CD1 . LEU A 1 15  ? 104.17100 128.36200 121.07100 1.000 52.58188  ? 22  LEU A CD1 1 
ATOM   69   C CD2 . LEU A 1 15  ? 105.05900 127.16300 123.04400 1.000 56.07412  ? 22  LEU A CD2 1 
ATOM   70   N N   . LEU A 1 16  ? 102.81000 123.99900 120.05200 1.000 44.07037  ? 23  LEU A N   1 
ATOM   71   C CA  . LEU A 1 16  ? 103.48500 123.12700 119.10000 1.000 42.69970  ? 23  LEU A CA  1 
ATOM   72   C C   . LEU A 1 16  ? 102.75700 123.07400 117.76200 1.000 50.79727  ? 23  LEU A C   1 
ATOM   73   O O   . LEU A 1 16  ? 103.40000 123.04700 116.70900 1.000 56.77475  ? 23  LEU A O   1 
ATOM   74   C CB  . LEU A 1 16  ? 103.63700 121.72600 119.67600 1.000 49.08820  ? 23  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 16  ? 104.39200 120.77800 118.75700 1.000 50.13493  ? 23  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 16  ? 105.78200 121.30300 118.51800 1.000 51.61106  ? 23  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 16  ? 104.44900 119.41500 119.37900 1.000 49.96115  ? 23  LEU A CD2 1 
ATOM   78   N N   . ALA A 1 17  ? 101.42300 123.04000 117.77100 1.000 46.18349  ? 24  ALA A N   1 
ATOM   79   C CA  . ALA A 1 17  ? 100.69400 123.09900 116.50600 1.000 38.73037  ? 24  ALA A CA  1 
ATOM   80   C C   . ALA A 1 17  ? 100.99300 124.37800 115.72700 1.000 41.94962  ? 24  ALA A C   1 
ATOM   81   O O   . ALA A 1 17  ? 101.21700 124.33400 114.51000 1.000 48.38189  ? 24  ALA A O   1 
ATOM   82   C CB  . ALA A 1 17  ? 99.19600  122.96800 116.75700 1.000 46.93357  ? 24  ALA A CB  1 
ATOM   83   N N   . ALA A 1 18  ? 101.02400 125.52500 116.40900 1.000 39.22671  ? 25  ALA A N   1 
ATOM   84   C CA  . ALA A 1 18  ? 101.36800 126.77800 115.73700 1.000 37.04018  ? 25  ALA A CA  1 
ATOM   85   C C   . ALA A 1 18  ? 102.78900 126.77100 115.18300 1.000 40.25664  ? 25  ALA A C   1 
ATOM   86   O O   . ALA A 1 18  ? 103.02600 127.21800 114.05200 1.000 55.20207  ? 25  ALA A O   1 
ATOM   87   C CB  . ALA A 1 18  ? 101.18600 127.95400 116.69400 1.000 39.32342  ? 25  ALA A CB  1 
ATOM   88   N N   . LEU A 1 19  ? 103.74600 126.25700 115.95300 1.000 34.62692  ? 26  LEU A N   1 
ATOM   89   C CA  . LEU A 1 19  ? 105.12000 126.19700 115.46500 1.000 38.16264  ? 26  LEU A CA  1 
ATOM   90   C C   . LEU A 1 19  ? 105.26700 125.25600 114.27500 1.000 39.36534  ? 26  LEU A C   1 
ATOM   91   O O   . LEU A 1 19  ? 106.00700 125.55600 113.33500 1.000 39.40419  ? 26  LEU A O   1 
ATOM   92   C CB  . LEU A 1 19  ? 106.06200 125.78800 116.59100 1.000 43.15697  ? 26  LEU A CB  1 
ATOM   93   C CG  . LEU A 1 19  ? 106.26500 126.84800 117.66900 1.000 42.31277  ? 26  LEU A CG  1 
ATOM   94   C CD1 . LEU A 1 19  ? 107.05500 126.27900 118.82400 1.000 42.42294  ? 26  LEU A CD1 1 
ATOM   95   C CD2 . LEU A 1 19  ? 106.96000 128.05800 117.09200 1.000 39.64805  ? 26  LEU A CD2 1 
ATOM   96   N N   . ILE A 1 20  ? 104.56500 124.12600 114.27800 1.000 33.98046  ? 27  ILE A N   1 
ATOM   97   C CA  . ILE A 1 20  ? 104.62500 123.23300 113.12500 1.000 31.80655  ? 27  ILE A CA  1 
ATOM   98   C C   . ILE A 1 20  ? 104.00000 123.87500 111.88900 1.000 38.93312  ? 27  ILE A C   1 
ATOM   99   O O   . ILE A 1 20  ? 104.51200 123.71800 110.77700 1.000 42.22663  ? 27  ILE A O   1 
ATOM   100  C CB  . ILE A 1 20  ? 103.97200 121.88300 113.45500 1.000 34.60758  ? 27  ILE A CB  1 
ATOM   101  C CG1 . ILE A 1 20  ? 104.81300 121.13500 114.47600 1.000 42.82401  ? 27  ILE A CG1 1 
ATOM   102  C CG2 . ILE A 1 20  ? 103.85800 121.03700 112.22400 1.000 39.98275  ? 27  ILE A CG2 1 
ATOM   103  C CD1 . ILE A 1 20  ? 104.13200 119.92400 115.02600 1.000 45.42739  ? 27  ILE A CD1 1 
ATOM   104  N N   . VAL A 1 21  ? 102.86300 124.55700 112.04000 1.000 44.27104  ? 28  VAL A N   1 
ATOM   105  C CA  . VAL A 1 21  ? 102.26500 125.23000 110.88400 1.000 37.03284  ? 28  VAL A CA  1 
ATOM   106  C C   . VAL A 1 21  ? 103.18900 126.30400 110.31200 1.000 43.47160  ? 28  VAL A C   1 
ATOM   107  O O   . VAL A 1 21  ? 103.33000 126.43200 109.08700 1.000 54.07205  ? 28  VAL A O   1 
ATOM   108  C CB  . VAL A 1 21  ? 100.89000 125.80700 111.25400 1.000 36.06487  ? 28  VAL A CB  1 
ATOM   109  C CG1 . VAL A 1 21  ? 100.41300 126.74400 110.17800 1.000 37.67918  ? 28  VAL A CG1 1 
ATOM   110  C CG2 . VAL A 1 21  ? 99.89900  124.68400 111.42100 1.000 44.74007  ? 28  VAL A CG2 1 
ATOM   111  N N   . LEU A 1 22  ? 103.86300 127.06900 111.17500 1.000 36.57387  ? 29  LEU A N   1 
ATOM   112  C CA  . LEU A 1 22  ? 104.86800 128.00000 110.65900 1.000 33.49539  ? 29  LEU A CA  1 
ATOM   113  C C   . LEU A 1 22  ? 106.07200 127.29200 110.04700 1.000 44.88613  ? 29  LEU A C   1 
ATOM   114  O O   . LEU A 1 22  ? 106.66500 127.80100 109.09100 1.000 54.49979  ? 29  LEU A O   1 
ATOM   115  C CB  . LEU A 1 22  ? 105.32600 128.95300 111.75600 1.000 31.59092  ? 29  LEU A CB  1 
ATOM   116  C CG  . LEU A 1 22  ? 104.25200 129.90400 112.26700 1.000 36.79748  ? 29  LEU A CG  1 
ATOM   117  C CD1 . LEU A 1 22  ? 104.78100 130.71300 113.43000 1.000 42.04393  ? 29  LEU A CD1 1 
ATOM   118  C CD2 . LEU A 1 22  ? 103.78200 130.80900 111.15200 1.000 40.28125  ? 29  LEU A CD2 1 
ATOM   119  N N   . TYR A 1 23  ? 106.40000 126.09300 110.52100 1.000 37.57126  ? 30  TYR A N   1 
ATOM   120  C CA  . TYR A 1 23  ? 107.48300 125.32600 109.91600 1.000 35.57708  ? 30  TYR A CA  1 
ATOM   121  C C   . TYR A 1 23  ? 107.12200 124.83300 108.52300 1.000 37.73328  ? 30  TYR A C   1 
ATOM   122  O O   . TYR A 1 23  ? 107.95200 124.87200 107.61100 1.000 43.70486  ? 30  TYR A O   1 
ATOM   123  C CB  . TYR A 1 23  ? 107.82100 124.14000 110.81500 1.000 44.62927  ? 30  TYR A CB  1 
ATOM   124  C CG  . TYR A 1 23  ? 109.22900 123.62600 110.70300 1.000 46.34052  ? 30  TYR A CG  1 
ATOM   125  C CD1 . TYR A 1 23  ? 110.30200 124.40200 111.09000 1.000 49.77285  ? 30  TYR A CD1 1 
ATOM   126  C CD2 . TYR A 1 23  ? 109.48100 122.35400 110.22300 1.000 39.10795  ? 30  TYR A CD2 1 
ATOM   127  C CE1 . TYR A 1 23  ? 111.58200 123.92800 111.00400 1.000 43.03826  ? 30  TYR A CE1 1 
ATOM   128  C CE2 . TYR A 1 23  ? 110.75600 121.87800 110.12400 1.000 39.38884  ? 30  TYR A CE2 1 
ATOM   129  C CZ  . TYR A 1 23  ? 111.80400 122.66900 110.51800 1.000 43.39460  ? 30  TYR A CZ  1 
ATOM   130  O OH  . TYR A 1 23  ? 113.09000 122.20900 110.41500 1.000 50.69180  ? 30  TYR A OH  1 
ATOM   131  N N   . LEU A 1 24  ? 105.87100 124.43300 108.32400 1.000 36.30808  ? 31  LEU A N   1 
ATOM   132  C CA  . LEU A 1 24  ? 105.42100 124.03600 106.99400 1.000 35.56682  ? 31  LEU A CA  1 
ATOM   133  C C   . LEU A 1 24  ? 105.37000 125.22100 106.03800 1.000 41.48217  ? 31  LEU A C   1 
ATOM   134  O O   . LEU A 1 24  ? 105.79600 125.10800 104.88500 1.000 47.49372  ? 31  LEU A O   1 
ATOM   135  C CB  . LEU A 1 24  ? 104.06100 123.34800 107.07100 1.000 37.14170  ? 31  LEU A CB  1 
ATOM   136  C CG  . LEU A 1 24  ? 103.96600 122.11700 107.96700 1.000 37.42800  ? 31  LEU A CG  1 
ATOM   137  C CD1 . LEU A 1 24  ? 102.61700 121.45900 107.81400 1.000 42.98075  ? 31  LEU A CD1 1 
ATOM   138  C CD2 . LEU A 1 24  ? 105.06200 121.14700 107.64400 1.000 41.07253  ? 31  LEU A CD2 1 
ATOM   139  N N   . LEU A 1 25  ? 104.82500 126.35700 106.47500 1.000 41.36346  ? 32  LEU A N   1 
ATOM   140  C CA  . LEU A 1 25  ? 104.82100 127.53000 105.59900 1.000 40.75838  ? 32  LEU A CA  1 
ATOM   141  C C   . LEU A 1 25  ? 106.23400 128.00600 105.25300 1.000 41.13178  ? 32  LEU A C   1 
ATOM   142  O O   . LEU A 1 25  ? 106.50900 128.35900 104.09700 1.000 50.85994  ? 32  LEU A O   1 
ATOM   143  C CB  . LEU A 1 25  ? 104.02400 128.66700 106.23300 1.000 37.77464  ? 32  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 25  ? 102.51900 128.46400 106.35400 1.000 32.98242  ? 32  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 25  ? 101.91600 129.55200 107.20500 1.000 39.78558  ? 32  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 25  ? 101.88600 128.45400 104.99400 1.000 37.37158  ? 32  LEU A CD2 1 
ATOM   147  N N   . GLY A 1 26  ? 107.16900 127.93300 106.19800 1.000 26.46055  ? 33  GLY A N   1 
ATOM   148  C CA  . GLY A 1 26  ? 108.54100 128.28700 105.87100 1.000 30.94228  ? 33  GLY A CA  1 
ATOM   149  C C   . GLY A 1 26  ? 109.21300 127.30100 104.93500 1.000 41.72220  ? 33  GLY A C   1 
ATOM   150  O O   . GLY A 1 26  ? 109.92900 127.70100 104.01000 1.000 47.34411  ? 33  GLY A O   1 
ATOM   151  N N   . GLY A 1 27  ? 108.97200 126.00600 105.13100 1.000 40.41970  ? 34  GLY A N   1 
ATOM   152  C CA  . GLY A 1 27  ? 109.54300 125.02900 104.22200 1.000 34.67365  ? 34  GLY A CA  1 
ATOM   153  C C   . GLY A 1 27  ? 108.98900 125.15800 102.81800 1.000 36.12309  ? 34  GLY A C   1 
ATOM   154  O O   . GLY A 1 27  ? 109.73300 125.07700 101.84000 1.000 37.64421  ? 34  GLY A O   1 
ATOM   155  N N   . ALA A 1 28  ? 107.67600 125.34800 102.69600 1.000 36.01888  ? 35  ALA A N   1 
ATOM   156  C CA  . ALA A 1 28  ? 107.08100 125.55900 101.38300 1.000 38.07870  ? 35  ALA A CA  1 
ATOM   157  C C   . ALA A 1 28  ? 107.65700 126.79100 100.70400 1.000 36.65035  ? 35  ALA A C   1 
ATOM   158  O O   . ALA A 1 28  ? 107.89800 126.78400 99.49400  1.000 42.18659  ? 35  ALA A O   1 
ATOM   159  C CB  . ALA A 1 28  ? 105.56800 125.68600 101.50600 1.000 36.95309  ? 35  ALA A CB  1 
ATOM   160  N N   . ALA A 1 29  ? 107.88200 127.86300 101.46300 1.000 40.79255  ? 36  ALA A N   1 
ATOM   161  C CA  . ALA A 1 29  ? 108.49500 129.04800 100.87300 1.000 36.99368  ? 36  ALA A CA  1 
ATOM   162  C C   . ALA A 1 29  ? 109.93600 128.81100 100.43600 1.000 37.98504  ? 36  ALA A C   1 
ATOM   163  O O   . ALA A 1 29  ? 110.38900 129.42900 99.46900  1.000 43.19801  ? 36  ALA A O   1 
ATOM   164  C CB  . ALA A 1 29  ? 108.43400 130.21500 101.85500 1.000 40.81965  ? 36  ALA A CB  1 
ATOM   165  N N   . VAL A 1 30  ? 110.67200 127.94100 101.12900 1.000 44.21637  ? 37  VAL A N   1 
ATOM   166  C CA  . VAL A 1 30  ? 112.05300 127.65400 100.73200 1.000 40.88534  ? 37  VAL A CA  1 
ATOM   167  C C   . VAL A 1 30  ? 112.13200 126.69800 99.54100  1.000 46.59097  ? 37  VAL A C   1 
ATOM   168  O O   . VAL A 1 30  ? 112.83000 126.98000 98.56200  1.000 50.76378  ? 37  VAL A O   1 
ATOM   169  C CB  . VAL A 1 30  ? 112.85600 127.12100 101.92900 1.000 41.27981  ? 37  VAL A CB  1 
ATOM   170  C CG1 . VAL A 1 30  ? 114.23900 126.74000 101.48200 1.000 45.16084  ? 37  VAL A CG1 1 
ATOM   171  C CG2 . VAL A 1 30  ? 112.94900 128.17600 102.99900 1.000 41.85537  ? 37  VAL A CG2 1 
ATOM   172  N N   . PHE A 1 31  ? 111.44400 125.55300 99.59900  1.000 47.80804  ? 38  PHE A N   1 
ATOM   173  C CA  . PHE A 1 31  ? 111.54100 124.57100 98.51500  1.000 38.22574  ? 38  PHE A CA  1 
ATOM   174  C C   . PHE A 1 31  ? 111.06000 125.10500 97.17100  1.000 49.62469  ? 38  PHE A C   1 
ATOM   175  O O   . PHE A 1 31  ? 111.68400 124.83700 96.14100  1.000 60.65208  ? 38  PHE A O   1 
ATOM   176  C CB  . PHE A 1 31  ? 110.75800 123.30800 98.85300  1.000 36.11228  ? 38  PHE A CB  1 
ATOM   177  C CG  . PHE A 1 31  ? 111.47700 122.36200 99.75500  1.000 41.41463  ? 38  PHE A CG  1 
ATOM   178  C CD1 . PHE A 1 31  ? 112.51400 121.59800 99.27600  1.000 41.02049  ? 38  PHE A CD1 1 
ATOM   179  C CD2 . PHE A 1 31  ? 111.07600 122.18300 101.05700 1.000 46.93000  ? 38  PHE A CD2 1 
ATOM   180  C CE1 . PHE A 1 31  ? 113.15900 120.70900 100.08900 1.000 45.92574  ? 38  PHE A CE1 1 
ATOM   181  C CE2 . PHE A 1 31  ? 111.72300 121.29000 101.87100 1.000 44.71165  ? 38  PHE A CE2 1 
ATOM   182  C CZ  . PHE A 1 31  ? 112.76200 120.55500 101.38700 1.000 41.59184  ? 38  PHE A CZ  1 
ATOM   183  N N   . SER A 1 32  ? 109.96700 125.86000 97.14800  1.000 46.22325  ? 39  SER A N   1 
ATOM   184  C CA  . SER A 1 32  ? 109.54000 126.46200 95.89100  1.000 44.08143  ? 39  SER A CA  1 
ATOM   185  C C   . SER A 1 32  ? 110.53300 127.47700 95.34200  1.000 48.85084  ? 39  SER A C   1 
ATOM   186  O O   . SER A 1 32  ? 110.46600 127.80400 94.15600  1.000 55.51650  ? 39  SER A O   1 
ATOM   187  C CB  . SER A 1 32  ? 108.18100 127.12900 96.06000  1.000 47.63262  ? 39  SER A CB  1 
ATOM   188  O OG  . SER A 1 32  ? 108.24400 128.15400 97.03100  1.000 57.75429  ? 39  SER A OG  1 
ATOM   189  N N   . ALA A 1 33  ? 111.43300 127.99800 96.16800  1.000 44.86184  ? 40  ALA A N   1 
ATOM   190  C CA  . ALA A 1 33  ? 112.49000 128.87700 95.68300  1.000 45.04870  ? 40  ALA A CA  1 
ATOM   191  C C   . ALA A 1 33  ? 113.71200 128.13000 95.16600  1.000 46.59838  ? 40  ALA A C   1 
ATOM   192  O O   . ALA A 1 33  ? 114.32700 128.55900 94.18600  1.000 53.51346  ? 40  ALA A O   1 
ATOM   193  C CB  . ALA A 1 33  ? 112.91700 129.83800 96.79200  1.000 49.28799  ? 40  ALA A CB  1 
ATOM   194  N N   . LEU A 1 34  ? 114.08000 127.02300 95.80800  1.000 54.15507  ? 41  LEU A N   1 
ATOM   195  C CA  . LEU A 1 34  ? 115.26100 126.26800 95.39500  1.000 56.67966  ? 41  LEU A CA  1 
ATOM   196  C C   . LEU A 1 34  ? 115.11700 125.66500 94.00300  1.000 62.69025  ? 41  LEU A C   1 
ATOM   197  O O   . LEU A 1 34  ? 116.06000 125.71200 93.20600  1.000 63.12385  ? 41  LEU A O   1 
ATOM   198  C CB  . LEU A 1 34  ? 115.55200 125.16200 96.40800  1.000 53.37359  ? 41  LEU A CB  1 
ATOM   199  C CG  . LEU A 1 34  ? 116.06900 125.59200 97.77500  1.000 55.29479  ? 41  LEU A CG  1 
ATOM   200  C CD1 . LEU A 1 34  ? 116.12000 124.40700 98.71100  1.000 54.87838  ? 41  LEU A CD1 1 
ATOM   201  C CD2 . LEU A 1 34  ? 117.43100 126.22500 97.63800  1.000 58.98187  ? 41  LEU A CD2 1 
ATOM   202  N N   . GLU A 1 35  ? 113.95300 125.08800 93.68300  1.000 62.31883  ? 42  GLU A N   1 
ATOM   203  C CA  . GLU A 1 35  ? 113.89500 124.23300 92.50200  1.000 63.51566  ? 42  GLU A CA  1 
ATOM   204  C C   . GLU A 1 35  ? 112.58900 124.28200 91.71600  1.000 62.19571  ? 42  GLU A C   1 
ATOM   205  O O   . GLU A 1 35  ? 112.26300 123.30000 91.04300  1.000 70.73867  ? 42  GLU A O   1 
ATOM   206  C CB  . GLU A 1 35  ? 114.18400 122.80000 92.91500  1.000 64.32950  ? 42  GLU A CB  1 
ATOM   207  C CG  . GLU A 1 35  ? 113.18600 122.21400 93.86500  1.000 56.31894  ? 42  GLU A CG  1 
ATOM   208  C CD  . GLU A 1 35  ? 113.76500 121.04400 94.61800  1.000 66.67317  ? 42  GLU A CD  1 
ATOM   209  O OE1 . GLU A 1 35  ? 114.66100 120.36900 94.07400  1.000 64.83165  ? 42  GLU A OE1 1 
ATOM   210  O OE2 . GLU A 1 35  ? 113.33100 120.79900 95.75700  1.000 71.99572  ? 42  GLU A OE2 1 
ATOM   211  N N   . LEU A 1 36  ? 111.81900 125.36400 91.78600  1.000 61.91298  ? 43  LEU A N   1 
ATOM   212  C CA  . LEU A 1 36  ? 110.85100 125.63000 90.72700  1.000 60.89581  ? 43  LEU A CA  1 
ATOM   213  C C   . LEU A 1 36  ? 111.50100 125.88800 89.36900  1.000 65.37872  ? 43  LEU A C   1 
ATOM   214  O O   . LEU A 1 36  ? 110.93100 125.51900 88.33800  1.000 72.88794  ? 43  LEU A O   1 
ATOM   215  C CB  . LEU A 1 36  ? 109.97800 126.81800 91.11700  1.000 61.26072  ? 43  LEU A CB  1 
ATOM   216  C CG  . LEU A 1 36  ? 108.92100 127.24700 90.10600  1.000 63.54057  ? 43  LEU A CG  1 
ATOM   217  C CD1 . LEU A 1 36  ? 107.93600 126.12200 89.88100  1.000 63.25911  ? 43  LEU A CD1 1 
ATOM   218  C CD2 . LEU A 1 36  ? 108.21100 128.49400 90.58700  1.000 68.62124  ? 43  LEU A CD2 1 
ATOM   219  N N   . ALA A 1 37  ? 112.67800 126.51700 89.33200  1.000 72.89671  ? 44  ALA A N   1 
ATOM   220  C CA  . ALA A 1 37  ? 113.37600 126.71800 88.06000  1.000 75.21535  ? 44  ALA A CA  1 
ATOM   221  C C   . ALA A 1 37  ? 113.79800 125.41200 87.39100  1.000 77.82882  ? 44  ALA A C   1 
ATOM   222  O O   . ALA A 1 37  ? 113.74500 125.29700 86.15600  1.000 79.55883  ? 44  ALA A O   1 
ATOM   223  C CB  . ALA A 1 37  ? 114.59600 127.60800 88.27400  1.000 76.17272  ? 44  ALA A CB  1 
ATOM   224  N N   . HIS A 1 38  ? 114.11000 124.39000 88.18100  1.000 78.74454  ? 45  HIS A N   1 
ATOM   225  C CA  . HIS A 1 38  ? 114.50600 123.10300 87.62100  1.000 76.64088  ? 45  HIS A CA  1 
ATOM   226  C C   . HIS A 1 38  ? 113.31600 122.34900 87.04800  1.000 76.90020  ? 45  HIS A C   1 
ATOM   227  O O   . HIS A 1 38  ? 113.42800 121.73600 85.98100  1.000 82.53359  ? 45  HIS A O   1 
ATOM   228  C CB  . HIS A 1 38  ? 115.21400 122.27500 88.69100  1.000 77.04036  ? 45  HIS A CB  1 
ATOM   229  C CG  . HIS A 1 38  ? 115.77900 120.98500 88.18800  1.000 81.18899  ? 45  HIS A CG  1 
ATOM   230  N ND1 . HIS A 1 38  ? 115.00700 119.86500 87.97700  1.000 82.99224  ? 45  HIS A ND1 1 
ATOM   231  C CD2 . HIS A 1 38  ? 117.04500 120.63600 87.86200  1.000 82.22024  ? 45  HIS A CD2 1 
ATOM   232  C CE1 . HIS A 1 38  ? 115.77200 118.88100 87.53900  1.000 81.45954  ? 45  HIS A CE1 1 
ATOM   233  N NE2 . HIS A 1 38  ? 117.01300 119.32300 87.46100  1.000 81.31840  ? 45  HIS A NE2 1 
ATOM   234  N N   . GLU A 1 39  ? 112.18300 122.35800 87.74900  1.000 66.57798  ? 46  GLU A N   1 
ATOM   235  C CA  . GLU A 1 39  ? 110.97200 121.77100 87.19300  1.000 66.11874  ? 46  GLU A CA  1 
ATOM   236  C C   . GLU A 1 39  ? 110.65500 122.36000 85.82600  1.000 70.51175  ? 46  GLU A C   1 
ATOM   237  O O   . GLU A 1 39  ? 110.40500 121.62600 84.86600  1.000 78.52329  ? 46  GLU A O   1 
ATOM   238  C CB  . GLU A 1 39  ? 109.80000 122.00500 88.14000  1.000 66.85474  ? 46  GLU A CB  1 
ATOM   239  C CG  . GLU A 1 39  ? 108.46600 121.62300 87.54900  1.000 68.27700  ? 46  GLU A CG  1 
ATOM   240  C CD  . GLU A 1 39  ? 107.32100 121.88400 88.49400  1.000 72.96842  ? 46  GLU A CD  1 
ATOM   241  O OE1 . GLU A 1 39  ? 107.52300 122.62000 89.47900  1.000 73.52626  ? 46  GLU A OE1 1 
ATOM   242  O OE2 . GLU A 1 39  ? 106.21400 121.36600 88.24800  1.000 74.21110  ? 46  GLU A OE2 1 
ATOM   243  N N   . ARG A 1 40  ? 110.60300 123.68800 85.73400  1.000 73.30572  ? 47  ARG A N   1 
ATOM   244  C CA  . ARG A 1 40  ? 110.21000 124.32700 84.48300  1.000 75.45777  ? 47  ARG A CA  1 
ATOM   245  C C   . ARG A 1 40  ? 111.23200 124.11000 83.37500  1.000 77.06751  ? 47  ARG A C   1 
ATOM   246  O O   . ARG A 1 40  ? 110.84700 123.93700 82.21100  1.000 80.52251  ? 47  ARG A O   1 
ATOM   247  C CB  . ARG A 1 40  ? 109.96200 125.81500 84.70900  1.000 78.21553  ? 47  ARG A CB  1 
ATOM   248  C CG  . ARG A 1 40  ? 108.75300 126.07800 85.58800  1.000 80.68564  ? 47  ARG A CG  1 
ATOM   249  C CD  . ARG A 1 40  ? 108.35800 127.54100 85.60200  1.000 80.63936  ? 47  ARG A CD  1 
ATOM   250  N NE  . ARG A 1 40  ? 109.36300 128.37000 86.25200  1.000 81.96674  ? 47  ARG A NE  1 
ATOM   251  C CZ  . ARG A 1 40  ? 109.14600 129.60500 86.68000  1.000 82.97046  ? 47  ARG A CZ  1 
ATOM   252  N NH1 . ARG A 1 40  ? 107.96600 130.18600 86.54200  1.000 81.10689  ? 47  ARG A NH1 1 
ATOM   253  N NH2 . ARG A 1 40  ? 110.13600 130.27300 87.26500  1.000 82.84663  ? 47  ARG A NH2 1 
ATOM   254  N N   . GLN A 1 41  ? 112.51600 123.97800 83.71800  1.000 82.15360  ? 48  GLN A N   1 
ATOM   255  C CA  . GLN A 1 41  ? 113.49200 123.61500 82.69200  1.000 84.69134  ? 48  GLN A CA  1 
ATOM   256  C C   . GLN A 1 41  ? 113.28400 122.18900 82.19600  1.000 87.22980  ? 48  GLN A C   1 
ATOM   257  O O   . GLN A 1 41  ? 113.30500 121.93900 80.98600  1.000 88.96436  ? 48  GLN A O   1 
ATOM   258  C CB  . GLN A 1 41  ? 114.91500 123.79700 83.21500  1.000 85.42832  ? 48  GLN A CB  1 
ATOM   259  C CG  . GLN A 1 41  ? 115.33800 125.24500 83.35000  1.000 86.55642  ? 48  GLN A CG  1 
ATOM   260  C CD  . GLN A 1 41  ? 116.70500 125.39400 83.98000  1.000 91.34943  ? 48  GLN A CD  1 
ATOM   261  O OE1 . GLN A 1 41  ? 117.40100 124.40900 84.22100  1.000 93.80561  ? 48  GLN A OE1 1 
ATOM   262  N NE2 . GLN A 1 41  ? 117.09900 126.63200 84.24900  1.000 89.70990  ? 48  GLN A NE2 1 
ATOM   263  N N   . ALA A 1 42  ? 113.10900 121.23600 83.11000  1.000 83.63396  ? 49  ALA A N   1 
ATOM   264  C CA  . ALA A 1 42  ? 112.93600 119.84800 82.69200  1.000 80.91986  ? 49  ALA A CA  1 
ATOM   265  C C   . ALA A 1 42  ? 111.64800 119.64600 81.90000  1.000 82.19777  ? 49  ALA A C   1 
ATOM   266  O O   . ALA A 1 42  ? 111.62800 118.88500 80.92800  1.000 88.60736  ? 49  ALA A O   1 
ATOM   267  C CB  . ALA A 1 42  ? 112.96000 118.92600 83.90700  1.000 79.28591  ? 49  ALA A CB  1 
ATOM   268  N N   . LYS A 1 43  ? 110.56900 120.33100 82.27900  1.000 77.73262  ? 50  LYS A N   1 
ATOM   269  C CA  . LYS A 1 43  ? 109.33800 120.26400 81.49400  1.000 78.50583  ? 50  LYS A CA  1 
ATOM   270  C C   . LYS A 1 43  ? 109.48300 120.90100 80.11600  1.000 80.36693  ? 50  LYS A C   1 
ATOM   271  O O   . LYS A 1 43  ? 108.95800 120.36700 79.13000  1.000 83.75291  ? 50  LYS A O   1 
ATOM   272  C CB  . LYS A 1 43  ? 108.18500 120.91000 82.25900  1.000 81.29368  ? 50  LYS A CB  1 
ATOM   273  C CG  . LYS A 1 43  ? 107.74900 120.12400 83.48000  1.000 80.21712  ? 50  LYS A CG  1 
ATOM   274  C CD  . LYS A 1 43  ? 106.45000 120.66000 84.05800  1.000 81.70104  ? 50  LYS A CD  1 
ATOM   275  C CE  . LYS A 1 43  ? 105.85100 119.67700 85.04900  1.000 80.99321  ? 50  LYS A CE  1 
ATOM   276  N NZ  . LYS A 1 43  ? 104.63800 120.20700 85.72000  1.000 79.22633  ? 50  LYS A NZ  1 
ATOM   277  N N   . GLN A 1 44  ? 110.19000 122.02900 80.00500  1.000 86.82618  ? 51  GLN A N   1 
ATOM   278  C CA  . GLN A 1 44  ? 110.45400 122.56700 78.67300  1.000 89.18661  ? 51  GLN A CA  1 
ATOM   279  C C   . GLN A 1 44  ? 111.27600 121.60100 77.82500  1.000 89.70451  ? 51  GLN A C   1 
ATOM   280  O O   . GLN A 1 44  ? 110.98600 121.40500 76.63700  1.000 92.49656  ? 51  GLN A O   1 
ATOM   281  C CB  . GLN A 1 44  ? 111.16100 123.91500 78.78100  1.000 91.71355  ? 51  GLN A CB  1 
ATOM   282  C CG  . GLN A 1 44  ? 111.56000 124.50300 77.44200  1.000 92.32526  ? 51  GLN A CG  1 
ATOM   283  C CD  . GLN A 1 44  ? 112.25100 125.84400 77.57900  1.000 94.14610  ? 51  GLN A CD  1 
ATOM   284  O OE1 . GLN A 1 44  ? 112.14000 126.51000 78.60800  1.000 93.05936  ? 51  GLN A OE1 1 
ATOM   285  N NE2 . GLN A 1 44  ? 112.96600 126.25000 76.53700  1.000 94.08576  ? 51  GLN A NE2 1 
ATOM   286  N N   . ARG A 1 45  ? 112.31700 121.00700 78.40800  1.000 86.01568  ? 52  ARG A N   1 
ATOM   287  C CA  . ARG A 1 45  ? 113.14600 120.06100 77.66400  1.000 85.68015  ? 52  ARG A CA  1 
ATOM   288  C C   . ARG A 1 45  ? 112.36000 118.82500 77.23600  1.000 86.17135  ? 52  ARG A C   1 
ATOM   289  O O   . ARG A 1 45  ? 112.56500 118.30000 76.13500  1.000 89.90262  ? 52  ARG A O   1 
ATOM   290  C CB  . ARG A 1 45  ? 114.36300 119.67800 78.50200  1.000 86.37153  ? 52  ARG A CB  1 
ATOM   291  C CG  . ARG A 1 45  ? 115.43600 118.93800 77.74100  1.000 88.12860  ? 52  ARG A CG  1 
ATOM   292  C CD  . ARG A 1 45  ? 116.72500 118.87400 78.54500  1.000 88.87110  ? 52  ARG A CD  1 
ATOM   293  N NE  . ARG A 1 45  ? 116.60100 118.05900 79.74600  1.000 91.41836  ? 52  ARG A NE  1 
ATOM   294  C CZ  . ARG A 1 45  ? 116.99400 118.44500 80.95200  1.000 93.50320  ? 52  ARG A CZ  1 
ATOM   295  N NH1 . ARG A 1 45  ? 117.54100 119.63200 81.15400  1.000 92.48355  ? 52  ARG A NH1 1 
ATOM   296  N NH2 . ARG A 1 45  ? 116.83700 117.61800 81.98200  1.000 92.28672  ? 52  ARG A NH2 1 
ATOM   297  N N   . TRP A 1 46  ? 111.42000 118.37400 78.06800  1.000 83.58070  ? 53  TRP A N   1 
ATOM   298  C CA  . TRP A 1 46  ? 110.50900 117.31100 77.64900  1.000 82.71856  ? 53  TRP A CA  1 
ATOM   299  C C   . TRP A 1 46  ? 109.62600 117.72800 76.48400  1.000 81.96019  ? 53  TRP A C   1 
ATOM   300  O O   . TRP A 1 46  ? 109.42100 116.94900 75.54900  1.000 83.36012  ? 53  TRP A O   1 
ATOM   301  C CB  . TRP A 1 46  ? 109.64900 116.83600 78.81500  1.000 80.11073  ? 53  TRP A CB  1 
ATOM   302  C CG  . TRP A 1 46  ? 108.50600 115.98700 78.35200  1.000 80.28759  ? 53  TRP A CG  1 
ATOM   303  C CD1 . TRP A 1 46  ? 107.18700 116.30200 78.42900  1.000 82.50995  ? 53  TRP A CD1 1 
ATOM   304  C CD2 . TRP A 1 46  ? 108.57800 114.74800 77.63800  1.000 82.43790  ? 53  TRP A CD2 1 
ATOM   305  N NE1 . TRP A 1 46  ? 106.42700 115.31000 77.86800  1.000 83.80913  ? 53  TRP A NE1 1 
ATOM   306  C CE2 . TRP A 1 46  ? 107.25900 114.34600 77.36700  1.000 81.99037  ? 53  TRP A CE2 1 
ATOM   307  C CE3 . TRP A 1 46  ? 109.62700 113.92500 77.22500  1.000 86.27136  ? 53  TRP A CE3 1 
ATOM   308  C CZ2 . TRP A 1 46  ? 106.96000 113.16300 76.70500  1.000 80.00531  ? 53  TRP A CZ2 1 
ATOM   309  C CZ3 . TRP A 1 46  ? 109.32600 112.74800 76.56700  1.000 84.51329  ? 53  TRP A CZ3 1 
ATOM   310  C CH2 . TRP A 1 46  ? 108.00500 112.37900 76.31300  1.000 80.29985  ? 53  TRP A CH2 1 
ATOM   311  N N   . GLU A 1 47  ? 109.01900 118.90800 76.55800  1.000 90.63445  ? 54  GLU A N   1 
ATOM   312  C CA  . GLU A 1 47  ? 108.18100 119.34400 75.44500  1.000 90.22692  ? 54  GLU A CA  1 
ATOM   313  C C   . GLU A 1 47  ? 108.97900 119.44000 74.14900  1.000 90.95539  ? 54  GLU A C   1 
ATOM   314  O O   . GLU A 1 47  ? 108.48500 119.07100 73.07600  1.000 94.06242  ? 54  GLU A O   1 
ATOM   315  C CB  . GLU A 1 47  ? 107.52200 120.68000 75.77400  1.000 93.18229  ? 54  GLU A CB  1 
ATOM   316  C CG  . GLU A 1 47  ? 106.43900 120.58300 76.83600  1.000 94.00640  ? 54  GLU A CG  1 
ATOM   317  C CD  . GLU A 1 47  ? 105.23400 119.79000 76.37500  1.000 96.73147  ? 54  GLU A CD  1 
ATOM   318  O OE1 . GLU A 1 47  ? 105.02500 119.67600 75.14900  1.000 96.62302  ? 54  GLU A OE1 1 
ATOM   319  O OE2 . GLU A 1 47  ? 104.49600 119.27700 77.24200  1.000 93.99469  ? 54  GLU A OE2 1 
ATOM   320  N N   . GLU A 1 48  ? 110.24000 119.86500 74.23900  1.000 92.46708  ? 55  GLU A N   1 
ATOM   321  C CA  . GLU A 1 48  ? 111.10900 119.88500 73.06300  1.000 91.71392  ? 55  GLU A CA  1 
ATOM   322  C C   . GLU A 1 48  ? 111.42100 118.48400 72.54100  1.000 93.83576  ? 55  GLU A C   1 
ATOM   323  O O   . GLU A 1 48  ? 111.40500 118.25600 71.32600  1.000 93.25339  ? 55  GLU A O   1 
ATOM   324  C CB  . GLU A 1 48  ? 112.40400 120.62400 73.38900  1.000 92.12581  ? 55  GLU A CB  1 
ATOM   325  C CG  . GLU A 1 48  ? 112.22000 122.10600 73.64000  1.000 95.71063  ? 55  GLU A CG  1 
ATOM   326  C CD  . GLU A 1 48  ? 113.48400 122.76900 74.14800  1.000 97.11980  ? 55  GLU A CD  1 
ATOM   327  O OE1 . GLU A 1 48  ? 114.53500 122.09500 74.18600  1.000 97.13160  ? 55  GLU A OE1 1 
ATOM   328  O OE2 . GLU A 1 48  ? 113.42600 123.96200 74.51100  1.000 96.28231  ? 55  GLU A OE2 1 
ATOM   329  N N   . ARG A 1 49  ? 111.68700 117.53000 73.43600  1.000 91.13882  ? 56  ARG A N   1 
ATOM   330  C CA  . ARG A 1 49  ? 111.92600 116.15600 72.99500  1.000 87.77033  ? 56  ARG A CA  1 
ATOM   331  C C   . ARG A 1 49  ? 110.69200 115.53900 72.35000  1.000 87.59977  ? 56  ARG A C   1 
ATOM   332  O O   . ARG A 1 49  ? 110.79600 114.85900 71.32300  1.000 89.07061  ? 56  ARG A O   1 
ATOM   333  C CB  . ARG A 1 49  ? 112.38800 115.30200 74.17300  1.000 85.28407  ? 56  ARG A CB  1 
ATOM   334  C CG  . ARG A 1 49  ? 113.82400 115.54700 74.58700  1.000 87.06017  ? 56  ARG A CG  1 
ATOM   335  C CD  . ARG A 1 49  ? 114.17300 114.77100 75.83900  1.000 85.32766  ? 56  ARG A CD  1 
ATOM   336  N NE  . ARG A 1 49  ? 115.57300 114.93000 76.20600  1.000 85.55225  ? 56  ARG A NE  1 
ATOM   337  C CZ  . ARG A 1 49  ? 116.04500 114.78000 77.43500  1.000 88.72873  ? 56  ARG A CZ  1 
ATOM   338  N NH1 . ARG A 1 49  ? 115.24700 114.49500 78.45100  1.000 88.76383  ? 56  ARG A NH1 1 
ATOM   339  N NH2 . ARG A 1 49  ? 117.34800 114.92500 77.65200  1.000 88.89325  ? 56  ARG A NH2 1 
ATOM   340  N N   . LEU A 1 50  ? 109.52000 115.74600 72.94500  1.000 88.40300  ? 57  LEU A N   1 
ATOM   341  C CA  . LEU A 1 50  ? 108.28700 115.22300 72.36600  1.000 87.33407  ? 57  LEU A CA  1 
ATOM   342  C C   . LEU A 1 50  ? 107.99300 115.84500 71.00700  1.000 89.15072  ? 57  LEU A C   1 
ATOM   343  O O   . LEU A 1 50  ? 107.54600 115.15200 70.08700  1.000 89.84002  ? 57  LEU A O   1 
ATOM   344  C CB  . LEU A 1 50  ? 107.12100 115.45100 73.32200  1.000 88.17225  ? 57  LEU A CB  1 
ATOM   345  C CG  . LEU A 1 50  ? 105.76400 114.95800 72.83200  1.000 88.29904  ? 57  LEU A CG  1 
ATOM   346  C CD1 . LEU A 1 50  ? 105.80200 113.46300 72.65100  1.000 89.98840  ? 57  LEU A CD1 1 
ATOM   347  C CD2 . LEU A 1 50  ? 104.67500 115.34200 73.80900  1.000 87.95579  ? 57  LEU A CD2 1 
ATOM   348  N N   . ALA A 1 51  ? 108.24600 117.14600 70.85300  1.000 97.29967  ? 58  ALA A N   1 
ATOM   349  C CA  . ALA A 1 51  ? 108.10100 117.78200 69.54600  1.000 96.05991  ? 58  ALA A CA  1 
ATOM   350  C C   . ALA A 1 51  ? 109.06600 117.20000 68.51800  1.000 97.09836  ? 58  ALA A C   1 
ATOM   351  O O   . ALA A 1 51  ? 108.67700 116.92400 67.37600  1.000 96.33075  ? 58  ALA A O   1 
ATOM   352  C CB  . ALA A 1 51  ? 108.30400 119.29000 69.67600  1.000 97.26545  ? 58  ALA A CB  1 
ATOM   353  N N   . ASN A 1 52  ? 110.33500 117.02800 68.89300  1.000 100.15855 ? 59  ASN A N   1 
ATOM   354  C CA  . ASN A 1 52  ? 111.29800 116.42400 67.97500  1.000 99.32355  ? 59  ASN A CA  1 
ATOM   355  C C   . ASN A 1 52  ? 110.89600 115.01200 67.56500  1.000 99.61056  ? 59  ASN A C   1 
ATOM   356  O O   . ASN A 1 52  ? 111.02700 114.64200 66.39400  1.000 100.36280 ? 59  ASN A O   1 
ATOM   357  C CB  . ASN A 1 52  ? 112.69200 116.41000 68.60100  1.000 99.46509  ? 59  ASN A CB  1 
ATOM   358  C CG  . ASN A 1 52  ? 113.35600 117.76900 68.57700  1.000 100.74340 ? 59  ASN A CG  1 
ATOM   359  O OD1 . ASN A 1 52  ? 112.90400 118.68100 67.88800  1.000 100.90045 ? 59  ASN A OD1 1 
ATOM   360  N ND2 . ASN A 1 52  ? 114.44700 117.90700 69.32000  1.000 100.17624 ? 59  ASN A ND2 1 
ATOM   361  N N   . PHE A 1 53  ? 110.39700 114.21200 68.50600  1.000 97.08558  ? 60  PHE A N   1 
ATOM   362  C CA  . PHE A 1 53  ? 109.95000 112.86600 68.15300  1.000 96.80720  ? 60  PHE A CA  1 
ATOM   363  C C   . PHE A 1 53  ? 108.71800 112.89400 67.25400  1.000 97.91180  ? 60  PHE A C   1 
ATOM   364  O O   . PHE A 1 53  ? 108.63800 112.13200 66.28500  1.000 98.12812  ? 60  PHE A O   1 
ATOM   365  C CB  . PHE A 1 53  ? 109.67200 112.05900 69.41900  1.000 96.10490  ? 60  PHE A CB  1 
ATOM   366  C CG  . PHE A 1 53  ? 109.58200 110.57900 69.18700  1.000 97.39129  ? 60  PHE A CG  1 
ATOM   367  C CD1 . PHE A 1 53  ? 110.72000 109.79500 69.20200  1.000 96.15524  ? 60  PHE A CD1 1 
ATOM   368  C CD2 . PHE A 1 53  ? 108.36400 109.97100 68.95900  1.000 97.62029  ? 60  PHE A CD2 1 
ATOM   369  C CE1 . PHE A 1 53  ? 110.64300 108.43800 68.99300  1.000 93.95728  ? 60  PHE A CE1 1 
ATOM   370  C CE2 . PHE A 1 53  ? 108.28400 108.61200 68.75000  1.000 96.44467  ? 60  PHE A CE2 1 
ATOM   371  C CZ  . PHE A 1 53  ? 109.42400 107.84700 68.76700  1.000 94.58278  ? 60  PHE A CZ  1 
ATOM   372  N N   . SER A 1 54  ? 107.74600 113.75400 67.56300  1.000 104.87500 ? 61  SER A N   1 
ATOM   373  C CA  . SER A 1 54  ? 106.56100 113.89200 66.72000  1.000 103.75852 ? 61  SER A CA  1 
ATOM   374  C C   . SER A 1 54  ? 106.92900 114.26200 65.28900  1.000 104.21747 ? 61  SER A C   1 
ATOM   375  O O   . SER A 1 54  ? 106.44500 113.64900 64.33100  1.000 104.28365 ? 61  SER A O   1 
ATOM   376  C CB  . SER A 1 54  ? 105.62000 114.93900 67.31200  1.000 106.20335 ? 61  SER A CB  1 
ATOM   377  O OG  . SER A 1 54  ? 105.23300 114.59700 68.62800  1.000 107.48915 ? 61  SER A OG  1 
ATOM   378  N N   . ARG A 1 55  ? 107.78300 115.27300 65.12600  1.000 111.19693 ? 62  ARG A N   1 
ATOM   379  C CA  . ARG A 1 55  ? 108.18800 115.70600 63.79200  1.000 112.01570 ? 62  ARG A CA  1 
ATOM   380  C C   . ARG A 1 55  ? 109.02500 114.65500 63.07300  1.000 112.50126 ? 62  ARG A C   1 
ATOM   381  O O   . ARG A 1 55  ? 108.84300 114.43100 61.87100  1.000 111.41770 ? 62  ARG A O   1 
ATOM   382  C CB  . ARG A 1 55  ? 108.95200 117.02600 63.88200  1.000 111.42722 ? 62  ARG A CB  1 
ATOM   383  C CG  . ARG A 1 55  ? 109.22700 117.66600 62.53300  1.000 112.48384 ? 62  ARG A CG  1 
ATOM   384  C CD  . ARG A 1 55  ? 109.93000 119.00300 62.68000  1.000 112.69339 ? 62  ARG A CD  1 
ATOM   385  N NE  . ARG A 1 55  ? 111.28400 118.85700 63.19600  1.000 114.75836 ? 62  ARG A NE  1 
ATOM   386  C CZ  . ARG A 1 55  ? 111.64400 119.14700 64.43900  1.000 113.83616 ? 62  ARG A CZ  1 
ATOM   387  N NH1 . ARG A 1 55  ? 110.77400 119.61700 65.31700  1.000 111.25361 ? 62  ARG A NH1 1 
ATOM   388  N NH2 . ARG A 1 55  ? 112.90800 118.96400 64.80800  1.000 112.86371 ? 62  ARG A NH2 1 
ATOM   389  N N   . GLY A 1 56  ? 109.94600 114.00300 63.78100  1.000 113.05883 ? 63  GLY A N   1 
ATOM   390  C CA  . GLY A 1 56  ? 110.87300 113.10200 63.11500  1.000 112.51932 ? 63  GLY A CA  1 
ATOM   391  C C   . GLY A 1 56  ? 110.23000 111.85100 62.54500  1.000 114.26139 ? 63  GLY A C   1 
ATOM   392  O O   . GLY A 1 56  ? 110.64500 111.36100 61.49100  1.000 115.18401 ? 63  GLY A O   1 
ATOM   393  N N   . HIS A 1 57  ? 109.21800 111.31100 63.22200  1.000 110.19964 ? 64  HIS A N   1 
ATOM   394  C CA  . HIS A 1 57  ? 108.61500 110.05100 62.80500  1.000 110.33978 ? 64  HIS A CA  1 
ATOM   395  C C   . HIS A 1 57  ? 107.21200 110.20100 62.22600  1.000 110.33570 ? 64  HIS A C   1 
ATOM   396  O O   . HIS A 1 57  ? 106.52100 109.19300 62.04600  1.000 109.54895 ? 64  HIS A O   1 
ATOM   397  C CB  . HIS A 1 57  ? 108.60300 109.07000 63.97600  1.000 109.29759 ? 64  HIS A CB  1 
ATOM   398  C CG  . HIS A 1 57  ? 109.96100 108.81000 64.54800  1.000 108.52969 ? 64  HIS A CG  1 
ATOM   399  N ND1 . HIS A 1 57  ? 110.93900 108.13100 63.85700  1.000 108.90021 ? 64  HIS A ND1 1 
ATOM   400  C CD2 . HIS A 1 57  ? 110.51000 109.15600 65.73500  1.000 108.49216 ? 64  HIS A CD2 1 
ATOM   401  C CE1 . HIS A 1 57  ? 112.03000 108.06000 64.59800  1.000 109.19268 ? 64  HIS A CE1 1 
ATOM   402  N NE2 . HIS A 1 57  ? 111.79600 108.67500 65.74300  1.000 109.62241 ? 64  HIS A NE2 1 
ATOM   403  N N   . ASN A 1 58  ? 106.77800 111.42500 61.92600  1.000 113.95328 ? 65  ASN A N   1 
ATOM   404  C CA  . ASN A 1 58  ? 105.43100 111.68700 61.41500  1.000 114.37171 ? 65  ASN A CA  1 
ATOM   405  C C   . ASN A 1 58  ? 104.35500 111.09500 62.32500  1.000 112.45079 ? 65  ASN A C   1 
ATOM   406  O O   . ASN A 1 58  ? 103.41200 110.43900 61.87800  1.000 110.88244 ? 65  ASN A O   1 
ATOM   407  C CB  . ASN A 1 58  ? 105.28800 111.16900 59.98100  1.000 114.71527 ? 65  ASN A CB  1 
ATOM   408  C CG  . ASN A 1 58  ? 104.02400 111.66200 59.30600  1.000 115.87957 ? 65  ASN A CG  1 
ATOM   409  O OD1 . ASN A 1 58  ? 103.52100 112.74100 59.61700  1.000 116.06564 ? 65  ASN A OD1 1 
ATOM   410  N ND2 . ASN A 1 58  ? 103.50300 110.87200 58.37500  1.000 114.13536 ? 65  ASN A ND2 1 
ATOM   411  N N   . LEU A 1 59  ? 104.50800 111.32400 63.62500  1.000 109.75348 ? 66  LEU A N   1 
ATOM   412  C CA  . LEU A 1 59  ? 103.57200 110.83400 64.62800  1.000 110.79571 ? 66  LEU A CA  1 
ATOM   413  C C   . LEU A 1 59  ? 102.82500 112.00900 65.24200  1.000 110.96927 ? 66  LEU A C   1 
ATOM   414  O O   . LEU A 1 59  ? 103.44300 113.00200 65.63900  1.000 109.18706 ? 66  LEU A O   1 
ATOM   415  C CB  . LEU A 1 59  ? 104.29600 110.04500 65.71700  1.000 110.66313 ? 66  LEU A CB  1 
ATOM   416  C CG  . LEU A 1 59  ? 104.52900 108.56600 65.43100  1.000 108.88960 ? 66  LEU A CG  1 
ATOM   417  C CD1 . LEU A 1 59  ? 105.51800 108.00700 66.42400  1.000 107.80426 ? 66  LEU A CD1 1 
ATOM   418  C CD2 . LEU A 1 59  ? 103.21900 107.80600 65.49300  1.000 108.90959 ? 66  LEU A CD2 1 
ATOM   419  N N   . SER A 1 60  ? 101.50300 111.89100 65.32200  1.000 108.40914 ? 67  SER A N   1 
ATOM   420  C CA  . SER A 1 60  ? 100.69900 112.90100 65.98900  1.000 105.38316 ? 67  SER A CA  1 
ATOM   421  C C   . SER A 1 60  ? 100.78800 112.75000 67.50200  1.000 105.01774 ? 67  SER A C   1 
ATOM   422  O O   . SER A 1 60  ? 100.99700 111.65600 68.02900  1.000 105.74518 ? 67  SER A O   1 
ATOM   423  C CB  . SER A 1 60  ? 99.24000  112.80500 65.54600  1.000 105.35978 ? 67  SER A CB  1 
ATOM   424  O OG  . SER A 1 60  ? 98.45400  113.80000 66.17400  1.000 105.52222 ? 67  SER A OG  1 
ATOM   425  N N   . ARG A 1 61  ? 100.62000 113.87500 68.19800  1.000 108.91552 ? 68  ARG A N   1 
ATOM   426  C CA  . ARG A 1 61  ? 100.55200 113.87100 69.65500  1.000 109.77359 ? 68  ARG A CA  1 
ATOM   427  C C   . ARG A 1 61  ? 99.40100  113.03500 70.20200  1.000 109.48263 ? 68  ARG A C   1 
ATOM   428  O O   . ARG A 1 61  ? 99.45000  112.63000 71.36600  1.000 110.09250 ? 68  ARG A O   1 
ATOM   429  C CB  . ARG A 1 61  ? 100.44900 115.30600 70.16700  1.000 108.70593 ? 68  ARG A CB  1 
ATOM   430  C CG  . ARG A 1 61  ? 101.76600 116.06300 70.13100  1.000 107.52804 ? 68  ARG A CG  1 
ATOM   431  C CD  . ARG A 1 61  ? 101.59000 117.48700 70.61800  1.000 108.19073 ? 68  ARG A CD  1 
ATOM   432  N NE  . ARG A 1 61  ? 102.86100 118.18300 70.77400  1.000 110.43373 ? 68  ARG A NE  1 
ATOM   433  C CZ  . ARG A 1 61  ? 103.35900 118.57700 71.93800  1.000 110.89138 ? 68  ARG A CZ  1 
ATOM   434  N NH1 . ARG A 1 61  ? 102.72200 118.34800 73.07500  1.000 108.15829 ? 68  ARG A NH1 1 
ATOM   435  N NH2 . ARG A 1 61  ? 104.52200 119.22100 71.96100  1.000 109.66024 ? 68  ARG A NH2 1 
ATOM   436  N N   . ASP A 1 62  ? 98.37500  112.75700 69.39800  1.000 102.40983 ? 69  ASP A N   1 
ATOM   437  C CA  . ASP A 1 62  ? 97.32100  111.83900 69.82300  1.000 101.37067 ? 69  ASP A CA  1 
ATOM   438  C C   . ASP A 1 62  ? 97.83800  110.41200 69.97700  1.000 102.58273 ? 69  ASP A C   1 
ATOM   439  O O   . ASP A 1 62  ? 97.65500  109.78200 71.02700  1.000 102.83648 ? 69  ASP A O   1 
ATOM   440  C CB  . ASP A 1 62  ? 96.15800  111.88400 68.83300  1.000 101.14918 ? 69  ASP A CB  1 
ATOM   441  N N   . GLU A 1 63  ? 98.48700  109.88400 68.93700  1.000 102.22886 ? 70  GLU A N   1 
ATOM   442  C CA  . GLU A 1 63  ? 99.05000  108.54000 69.02000  1.000 100.61468 ? 70  GLU A CA  1 
ATOM   443  C C   . GLU A 1 63  ? 100.10000 108.44200 70.11700  1.000 100.18294 ? 70  GLU A C   1 
ATOM   444  O O   . GLU A 1 63  ? 100.14600 107.45000 70.85500  1.000 102.13923 ? 70  GLU A O   1 
ATOM   445  C CB  . GLU A 1 63  ? 99.66000  108.14500 67.67600  1.000 100.60822 ? 70  GLU A CB  1 
ATOM   446  C CG  . GLU A 1 63  ? 98.69000  107.50500 66.69900  1.000 100.83065 ? 70  GLU A CG  1 
ATOM   447  C CD  . GLU A 1 63  ? 97.53300  108.41200 66.34300  1.000 102.59290 ? 70  GLU A CD  1 
ATOM   448  O OE1 . GLU A 1 63  ? 97.77700  109.60300 66.05800  1.000 102.72046 ? 70  GLU A OE1 1 
ATOM   449  O OE2 . GLU A 1 63  ? 96.37900  107.93500 66.34500  1.000 102.60106 ? 70  GLU A OE2 1 
ATOM   450  N N   . LEU A 1 64  ? 100.95800 109.45300 70.23300  1.000 95.07119  ? 71  LEU A N   1 
ATOM   451  C CA  . LEU A 1 64  ? 101.97700 109.43800 71.27500  1.000 95.09618  ? 71  LEU A CA  1 
ATOM   452  C C   . LEU A 1 64  ? 101.36900 109.51300 72.66900  1.000 94.58569  ? 71  LEU A C   1 
ATOM   453  O O   . LEU A 1 64  ? 101.84700 108.84400 73.58700  1.000 96.06922  ? 71  LEU A O   1 
ATOM   454  C CB  . LEU A 1 64  ? 102.97000 110.57300 71.06000  1.000 94.82016  ? 71  LEU A CB  1 
ATOM   455  C CG  . LEU A 1 64  ? 103.84900 110.39000 69.82700  1.000 96.61681  ? 71  LEU A CG  1 
ATOM   456  C CD1 . LEU A 1 64  ? 104.57500 111.67100 69.50200  1.000 97.51881  ? 71  LEU A CD1 1 
ATOM   457  C CD2 . LEU A 1 64  ? 104.82900 109.26000 70.04600  1.000 97.06764  ? 71  LEU A CD2 1 
ATOM   458  N N   . ARG A 1 65  ? 100.34000 110.34000 72.86400  1.000 89.22343  ? 72  ARG A N   1 
ATOM   459  C CA  . ARG A 1 65  ? 99.65600  110.36000 74.15300  1.000 89.39064  ? 72  ARG A CA  1 
ATOM   460  C C   . ARG A 1 65  ? 99.00800  109.01900 74.47700  1.000 93.00899  ? 72  ARG A C   1 
ATOM   461  O O   . ARG A 1 65  ? 99.03700  108.57600 75.62900  1.000 95.83738  ? 72  ARG A O   1 
ATOM   462  C CB  . ARG A 1 65  ? 98.61100  111.47400 74.17300  1.000 89.97696  ? 72  ARG A CB  1 
ATOM   463  N N   . GLY A 1 66  ? 98.45500  108.33800 73.47500  1.000 90.56598  ? 73  GLY A N   1 
ATOM   464  C CA  . GLY A 1 66  ? 97.94500  106.99200 73.70800  1.000 89.42648  ? 73  GLY A CA  1 
ATOM   465  C C   . GLY A 1 66  ? 99.02400  106.00900 74.12700  1.000 88.23562  ? 73  GLY A C   1 
ATOM   466  O O   . GLY A 1 66  ? 98.87200  105.26200 75.10300  1.000 89.87444  ? 73  GLY A O   1 
ATOM   467  N N   . PHE A 1 67  ? 100.13800 106.00800 73.39900  1.000 84.00836  ? 74  PHE A N   1 
ATOM   468  C CA  . PHE A 1 67  ? 101.25000 105.12200 73.72400  1.000 81.79937  ? 74  PHE A CA  1 
ATOM   469  C C   . PHE A 1 67  ? 101.79800 105.40900 75.11700  1.000 83.07271  ? 74  PHE A C   1 
ATOM   470  O O   . PHE A 1 67  ? 102.06900 104.48600 75.89300  1.000 86.25787  ? 74  PHE A O   1 
ATOM   471  C CB  . PHE A 1 67  ? 102.33200 105.26200 72.65600  1.000 83.98209  ? 74  PHE A CB  1 
ATOM   472  C CG  . PHE A 1 67  ? 103.53200 104.40100 72.88300  1.000 85.36611  ? 74  PHE A CG  1 
ATOM   473  C CD1 . PHE A 1 67  ? 103.43800 103.02800 72.78700  1.000 83.51131  ? 74  PHE A CD1 1 
ATOM   474  C CD2 . PHE A 1 67  ? 104.76500 104.96500 73.14300  1.000 88.05486  ? 74  PHE A CD2 1 
ATOM   475  C CE1 . PHE A 1 67  ? 104.54200 102.23500 72.98000  1.000 84.11256  ? 74  PHE A CE1 1 
ATOM   476  C CE2 . PHE A 1 67  ? 105.87300 104.17600 73.33400  1.000 85.37265  ? 74  PHE A CE2 1 
ATOM   477  C CZ  . PHE A 1 67  ? 105.76100 102.80900 73.25300  1.000 85.45642  ? 74  PHE A CZ  1 
ATOM   478  N N   . LEU A 1 68  ? 101.99000 106.68400 75.45000  1.000 77.76402  ? 75  LEU A N   1 
ATOM   479  C CA  . LEU A 1 68  ? 102.46600 107.02600 76.78300  1.000 74.97721  ? 75  LEU A CA  1 
ATOM   480  C C   . LEU A 1 68  ? 101.44900 106.69000 77.86800  1.000 78.35192  ? 75  LEU A C   1 
ATOM   481  O O   . LEU A 1 68  ? 101.84100 106.39900 78.99800  1.000 82.36531  ? 75  LEU A O   1 
ATOM   482  C CB  . LEU A 1 68  ? 102.83600 108.50200 76.84100  1.000 75.43260  ? 75  LEU A CB  1 
ATOM   483  C CG  . LEU A 1 68  ? 104.01000 108.86800 75.94100  1.000 78.26054  ? 75  LEU A CG  1 
ATOM   484  C CD1 . LEU A 1 68  ? 104.24500 110.36200 75.94700  1.000 80.07647  ? 75  LEU A CD1 1 
ATOM   485  C CD2 . LEU A 1 68  ? 105.24800 108.12400 76.38200  1.000 77.09894  ? 75  LEU A CD2 1 
ATOM   486  N N   . ARG A 1 69  ? 100.15000 106.75000 77.57300  1.000 81.37802  ? 76  ARG A N   1 
ATOM   487  C CA  . ARG A 1 69  ? 99.16500  106.28400 78.54500  1.000 80.82020  ? 76  ARG A CA  1 
ATOM   488  C C   . ARG A 1 69  ? 99.29900  104.78700 78.80000  1.000 84.01310  ? 76  ARG A C   1 
ATOM   489  O O   . ARG A 1 69  ? 99.21600  104.32600 79.95000  1.000 85.72480  ? 76  ARG A O   1 
ATOM   490  C CB  . ARG A 1 69  ? 97.75800  106.61800 78.05800  1.000 80.33965  ? 76  ARG A CB  1 
ATOM   491  C CG  . ARG A 1 69  ? 96.69600  106.53600 79.13100  1.000 82.38466  ? 76  ARG A CG  1 
ATOM   492  C CD  . ARG A 1 69  ? 95.32100  106.77800 78.54000  1.000 83.67488  ? 76  ARG A CD  1 
ATOM   493  N NE  . ARG A 1 69  ? 95.24400  108.07000 77.87000  1.000 87.18064  ? 76  ARG A NE  1 
ATOM   494  C CZ  . ARG A 1 69  ? 94.99100  109.21800 78.48300  1.000 86.84552  ? 76  ARG A CZ  1 
ATOM   495  N NH1 . ARG A 1 69  ? 94.78800  109.27300 79.78800  1.000 84.44042  ? 76  ARG A NH1 1 
ATOM   496  N NH2 . ARG A 1 69  ? 94.94400  110.33800 77.76800  1.000 84.28606  ? 76  ARG A NH2 1 
ATOM   497  N N   . HIS A 1 70  ? 99.60200  104.02100 77.75100  1.000 81.78913  ? 77  HIS A N   1 
ATOM   498  C CA  . HIS A 1 70  ? 99.88500  102.60500 77.96300  1.000 74.34912  ? 77  HIS A CA  1 
ATOM   499  C C   . HIS A 1 70  ? 101.17600 102.39100 78.74000  1.000 74.93847  ? 77  HIS A C   1 
ATOM   500  O O   . HIS A 1 70  ? 101.26800 101.44700 79.52700  1.000 79.70053  ? 77  HIS A O   1 
ATOM   501  C CB  . HIS A 1 70  ? 99.95200  101.86200 76.63200  1.000 78.00008  ? 77  HIS A CB  1 
ATOM   502  C CG  . HIS A 1 70  ? 98.70000  101.96000 75.82100  1.000 81.64154  ? 77  HIS A CG  1 
ATOM   503  N ND1 . HIS A 1 70  ? 97.45000  101.74000 76.35500  1.000 81.54216  ? 77  HIS A ND1 1 
ATOM   504  C CD2 . HIS A 1 70  ? 98.50700  102.23200 74.51000  1.000 81.17267  ? 77  HIS A CD2 1 
ATOM   505  C CE1 . HIS A 1 70  ? 96.53900  101.88700 75.41100  1.000 81.81981  ? 77  HIS A CE1 1 
ATOM   506  N NE2 . HIS A 1 70  ? 97.15400  102.18500 74.28100  1.000 82.00560  ? 77  HIS A NE2 1 
ATOM   507  N N   . TYR A 1 71  ? 102.17800 103.24200 78.53600  1.000 71.97743  ? 78  TYR A N   1 
ATOM   508  C CA  . TYR A 1 71  ? 103.39800 103.11900 79.33000  1.000 71.09221  ? 78  TYR A CA  1 
ATOM   509  C C   . TYR A 1 71  ? 103.20300 103.53000 80.78300  1.000 68.22314  ? 78  TYR A C   1 
ATOM   510  O O   . TYR A 1 71  ? 103.84800 102.96600 81.67000  1.000 73.70216  ? 78  TYR A O   1 
ATOM   511  C CB  . TYR A 1 71  ? 104.51800 103.95300 78.72100  1.000 72.16737  ? 78  TYR A CB  1 
ATOM   512  C CG  . TYR A 1 71  ? 105.87600 103.61400 79.27400  1.000 71.13434  ? 78  TYR A CG  1 
ATOM   513  C CD1 . TYR A 1 71  ? 106.44500 102.37100 79.07600  1.000 72.16219  ? 78  TYR A CD1 1 
ATOM   514  C CD2 . TYR A 1 71  ? 106.57900 104.54100 80.02400  1.000 69.95556  ? 78  TYR A CD2 1 
ATOM   515  C CE1 . TYR A 1 71  ? 107.68900 102.07400 79.58500  1.000 72.25702  ? 78  TYR A CE1 1 
ATOM   516  C CE2 . TYR A 1 71  ? 107.81100 104.25000 80.54100  1.000 64.84249  ? 78  TYR A CE2 1 
ATOM   517  C CZ  . TYR A 1 71  ? 108.36300 103.01900 80.31900  1.000 68.34642  ? 78  TYR A CZ  1 
ATOM   518  O OH  . TYR A 1 71  ? 109.59200 102.72900 80.85200  1.000 75.77928  ? 78  TYR A OH  1 
ATOM   519  N N   . GLU A 1 72  ? 102.32800 104.49400 81.05200  1.000 66.63930  ? 79  GLU A N   1 
ATOM   520  C CA  . GLU A 1 72  ? 101.97300 104.80500 82.43300  1.000 69.29479  ? 79  GLU A CA  1 
ATOM   521  C C   . GLU A 1 72  ? 101.25300 103.64500 83.09700  1.000 73.82619  ? 79  GLU A C   1 
ATOM   522  O O   . GLU A 1 72  ? 101.41700 103.40900 84.29800  1.000 77.61555  ? 79  GLU A O   1 
ATOM   523  C CB  . GLU A 1 72  ? 101.12300 106.07000 82.50100  1.000 74.52835  ? 79  GLU A CB  1 
ATOM   524  C CG  . GLU A 1 72  ? 101.89600 107.33800 82.23200  1.000 75.87294  ? 79  GLU A CG  1 
ATOM   525  C CD  . GLU A 1 72  ? 101.05700 108.57300 82.43200  1.000 75.61693  ? 79  GLU A CD  1 
ATOM   526  O OE1 . GLU A 1 72  ? 99.92900  108.44700 82.94900  1.000 75.75037  ? 79  GLU A OE1 1 
ATOM   527  O OE2 . GLU A 1 72  ? 101.52700 109.67100 82.08000  1.000 76.48691  ? 79  GLU A OE2 1 
ATOM   528  N N   . GLU A 1 73  ? 100.44000 102.91700 82.33700  1.000 76.61194  ? 80  GLU A N   1 
ATOM   529  C CA  . GLU A 1 73  ? 99.84000  101.70200 82.88100  1.000 75.40513  ? 80  GLU A CA  1 
ATOM   530  C C   . GLU A 1 73  ? 100.87700 100.60500 83.11800  1.000 76.02273  ? 80  GLU A C   1 
ATOM   531  O O   . GLU A 1 73  ? 100.84600 99.93000  84.15100  1.000 73.40151  ? 80  GLU A O   1 
ATOM   532  C CB  . GLU A 1 73  ? 98.73900  101.21200 81.94500  1.000 76.03207  ? 80  GLU A CB  1 
ATOM   533  C CG  . GLU A 1 73  ? 98.01700  99.97400  82.41800  1.000 79.25638  ? 80  GLU A CG  1 
ATOM   534  C CD  . GLU A 1 73  ? 96.89500  99.57900  81.48200  1.000 84.39136  ? 80  GLU A CD  1 
ATOM   535  O OE1 . GLU A 1 73  ? 96.02600  100.43200 81.20600  1.000 83.68868  ? 80  GLU A OE1 1 
ATOM   536  O OE2 . GLU A 1 73  ? 96.88600  98.42200  81.01500  1.000 82.62928  ? 80  GLU A OE2 1 
ATOM   537  N N   . ALA A 1 74  ? 101.79400 100.40500 82.17000  1.000 77.33419  ? 81  ALA A N   1 
ATOM   538  C CA  . ALA A 1 74  ? 102.82100 99.37200  82.30100  1.000 69.82313  ? 81  ALA A CA  1 
ATOM   539  C C   . ALA A 1 74  ? 103.81000 99.65000  83.42900  1.000 67.53041  ? 81  ALA A C   1 
ATOM   540  O O   . ALA A 1 74  ? 104.24600 98.71700  84.11000  1.000 74.60574  ? 81  ALA A O   1 
ATOM   541  C CB  . ALA A 1 74  ? 103.56800 99.21000  80.98100  1.000 71.02890  ? 81  ALA A CB  1 
ATOM   542  N N   . THR A 1 75  ? 104.19000 100.91200 83.64100  1.000 69.88376  ? 82  THR A N   1 
ATOM   543  C CA  . THR A 1 75  ? 105.11600 101.23600 84.72700  1.000 69.06260  ? 82  THR A CA  1 
ATOM   544  C C   . THR A 1 75  ? 104.51000 101.02500 86.10600  1.000 71.13729  ? 82  THR A C   1 
ATOM   545  O O   . THR A 1 75  ? 105.23400 100.69400 87.04900  1.000 74.51997  ? 82  THR A O   1 
ATOM   546  C CB  . THR A 1 75  ? 105.61300 102.67400 84.61600  1.000 68.30828  ? 82  THR A CB  1 
ATOM   547  O OG1 . THR A 1 75  ? 104.50100 103.55300 84.42100  1.000 73.56489  ? 82  THR A OG1 1 
ATOM   548  C CG2 . THR A 1 75  ? 106.58700 102.81600 83.47100  1.000 71.25278  ? 82  THR A CG2 1 
ATOM   549  N N   . ARG A 1 76  ? 103.20300 101.21600 86.25900  1.000 69.94290  ? 83  ARG A N   1 
ATOM   550  C CA  . ARG A 1 76  ? 102.57800 100.85900 87.52500  1.000 69.10776  ? 83  ARG A CA  1 
ATOM   551  C C   . ARG A 1 76  ? 102.59700 99.35500  87.76400  1.000 72.66375  ? 83  ARG A C   1 
ATOM   552  O O   . ARG A 1 76  ? 102.69800 98.91900  88.91500  1.000 78.46208  ? 83  ARG A O   1 
ATOM   553  C CB  . ARG A 1 76  ? 101.14400 101.38300 87.55900  1.000 70.11833  ? 83  ARG A CB  1 
ATOM   554  C CG  . ARG A 1 76  ? 100.41000 101.18000 88.87400  1.000 71.57588  ? 83  ARG A CG  1 
ATOM   555  C CD  . ARG A 1 76  ? 101.24500 101.54200 90.09700  1.000 73.16320  ? 83  ARG A CD  1 
ATOM   556  N NE  . ARG A 1 76  ? 101.85700 102.86200 90.00000  1.000 78.07244  ? 83  ARG A NE  1 
ATOM   557  C CZ  . ARG A 1 76  ? 102.89500 103.26100 90.72200  1.000 77.25175  ? 83  ARG A CZ  1 
ATOM   558  N NH1 . ARG A 1 76  ? 103.45700 102.47000 91.62100  1.000 68.97437  ? 83  ARG A NH1 1 
ATOM   559  N NH2 . ARG A 1 76  ? 103.37900 104.48600 90.54100  1.000 75.62178  ? 83  ARG A NH2 1 
ATOM   560  N N   . ALA A 1 77  ? 102.51500 98.54900  86.70800  1.000 71.61108  ? 84  ALA A N   1 
ATOM   561  C CA  . ALA A 1 77  ? 102.76200 97.11600  86.83800  1.000 71.49274  ? 84  ALA A CA  1 
ATOM   562  C C   . ALA A 1 77  ? 104.23100 96.76200  87.01300  1.000 71.88562  ? 84  ALA A C   1 
ATOM   563  O O   . ALA A 1 77  ? 104.53800 95.57500  87.14600  1.000 73.41766  ? 84  ALA A O   1 
ATOM   564  C CB  . ALA A 1 77  ? 102.20400 96.37100  85.62700  1.000 72.38827  ? 84  ALA A CB  1 
ATOM   565  N N   . GLY A 1 78  ? 105.14200 97.73000  87.01000  1.000 69.33321  ? 85  GLY A N   1 
ATOM   566  C CA  . GLY A 1 78  ? 106.52800 97.46400  87.32700  1.000 65.28158  ? 85  GLY A CA  1 
ATOM   567  C C   . GLY A 1 78  ? 107.46800 97.27500  86.15700  1.000 67.67278  ? 85  GLY A C   1 
ATOM   568  O O   . GLY A 1 78  ? 108.58700 96.79800  86.36400  1.000 71.58084  ? 85  GLY A O   1 
ATOM   569  N N   . ILE A 1 79  ? 107.05100 97.61900  84.93900  1.000 70.34792  ? 86  ILE A N   1 
ATOM   570  C CA  . ILE A 1 79  ? 107.98700 97.70300  83.82400  1.000 67.93429  ? 86  ILE A CA  1 
ATOM   571  C C   . ILE A 1 79  ? 108.92200 98.89100  84.02000  1.000 70.93795  ? 86  ILE A C   1 
ATOM   572  O O   . ILE A 1 79  ? 108.55700 99.90800  84.61800  1.000 74.49928  ? 86  ILE A O   1 
ATOM   573  C CB  . ILE A 1 79  ? 107.20800 97.81000  82.50000  1.000 66.75035  ? 86  ILE A CB  1 
ATOM   574  C CG1 . ILE A 1 79  ? 106.42900 96.52800  82.24300  1.000 72.29460  ? 86  ILE A CG1 1 
ATOM   575  C CG2 . ILE A 1 79  ? 108.13400 98.05500  81.33000  1.000 67.79846  ? 86  ILE A CG2 1 
ATOM   576  C CD1 . ILE A 1 79  ? 107.31000 95.35300  81.94200  1.000 73.39301  ? 86  ILE A CD1 1 
ATOM   577  N N   . ARG A 1 80  ? 110.14200 98.76500  83.50000  1.000 68.80888  ? 87  ARG A N   1 
ATOM   578  C CA  . ARG A 1 80  ? 111.05600 99.88600  83.35100  1.000 65.39788  ? 87  ARG A CA  1 
ATOM   579  C C   . ARG A 1 80  ? 111.86400 99.65500  82.08400  1.000 74.06756  ? 87  ARG A C   1 
ATOM   580  O O   . ARG A 1 80  ? 111.96800 98.52900  81.59400  1.000 74.97094  ? 87  ARG A O   1 
ATOM   581  C CB  . ARG A 1 80  ? 112.01600 100.02500 84.53600  1.000 64.41507  ? 87  ARG A CB  1 
ATOM   582  C CG  . ARG A 1 80  ? 111.40200 100.35400 85.88400  1.000 71.25622  ? 87  ARG A CG  1 
ATOM   583  C CD  . ARG A 1 80  ? 110.70900 101.69300 85.90900  1.000 74.72520  ? 87  ARG A CD  1 
ATOM   584  N NE  . ARG A 1 80  ? 110.24500 102.02000 87.25100  1.000 71.10663  ? 87  ARG A NE  1 
ATOM   585  C CZ  . ARG A 1 80  ? 109.09900 101.60200 87.76700  1.000 71.95781  ? 87  ARG A CZ  1 
ATOM   586  N NH1 . ARG A 1 80  ? 108.30700 100.77400 87.11100  1.000 75.93884  ? 87  ARG A NH1 1 
ATOM   587  N NH2 . ARG A 1 80  ? 108.74400 102.01600 88.97800  1.000 73.17734  ? 87  ARG A NH2 1 
ATOM   588  N N   . VAL A 1 81  ? 112.43700 100.73500 81.55100  1.000 81.24570  ? 88  VAL A N   1 
ATOM   589  C CA  . VAL A 1 81  ? 113.33400 100.57800 80.41000  1.000 81.36978  ? 88  VAL A CA  1 
ATOM   590  C C   . VAL A 1 81  ? 114.60600 99.84500  80.81700  1.000 84.29844  ? 88  VAL A C   1 
ATOM   591  O O   . VAL A 1 81  ? 115.14300 99.04100  80.04500  1.000 80.36599  ? 88  VAL A O   1 
ATOM   592  C CB  . VAL A 1 81  ? 113.64100 101.95000 79.78500  1.000 74.77504  ? 88  VAL A CB  1 
ATOM   593  C CG1 . VAL A 1 81  ? 114.73300 101.83200 78.74400  1.000 76.75292  ? 88  VAL A CG1 1 
ATOM   594  C CG2 . VAL A 1 81  ? 112.39600 102.51600 79.15100  1.000 76.98309  ? 88  VAL A CG2 1 
ATOM   595  N N   . ASP A 1 82  ? 115.09300 100.08200 82.03000  1.000 90.05334  ? 89  ASP A N   1 
ATOM   596  C CA  . ASP A 1 82  ? 116.16500 99.26800  82.57500  1.000 86.78685  ? 89  ASP A CA  1 
ATOM   597  C C   . ASP A 1 82  ? 115.65100 97.87800  82.93900  1.000 86.57561  ? 89  ASP A C   1 
ATOM   598  O O   . ASP A 1 82  ? 114.46000 97.66600  83.17400  1.000 89.21256  ? 89  ASP A O   1 
ATOM   599  C CB  . ASP A 1 82  ? 116.78200 99.94300  83.79900  1.000 85.99687  ? 89  ASP A CB  1 
ATOM   600  N N   . ASN A 1 83  ? 116.57000 96.92000  82.97000  1.000 86.30037  ? 90  ASN A N   1 
ATOM   601  C CA  . ASN A 1 83  ? 116.24800 95.55500  83.37100  1.000 87.59552  ? 90  ASN A CA  1 
ATOM   602  C C   . ASN A 1 83  ? 115.99400 95.52600  84.87100  1.000 83.61810  ? 90  ASN A C   1 
ATOM   603  O O   . ASN A 1 83  ? 116.92000 95.71100  85.66500  1.000 86.97210  ? 90  ASN A O   1 
ATOM   604  C CB  . ASN A 1 83  ? 117.38100 94.61100  82.98500  1.000 87.39597  ? 90  ASN A CB  1 
ATOM   605  C CG  . ASN A 1 83  ? 117.55600 94.49600  81.48600  1.000 86.57581  ? 90  ASN A CG  1 
ATOM   606  O OD1 . ASN A 1 83  ? 116.60800 94.19500  80.76100  1.000 87.10672  ? 90  ASN A OD1 1 
ATOM   607  N ND2 . ASN A 1 83  ? 118.77100 94.74300  81.01100  1.000 85.69285  ? 90  ASN A ND2 1 
ATOM   608  N N   . VAL A 1 84  ? 114.74300 95.30500  85.26500  1.000 67.11722  ? 91  VAL A N   1 
ATOM   609  C CA  . VAL A 1 84  ? 114.32600 95.37900  86.66000  1.000 73.46466  ? 91  VAL A CA  1 
ATOM   610  C C   . VAL A 1 84  ? 113.82100 94.01500  87.11700  1.000 78.00539  ? 91  VAL A C   1 
ATOM   611  O O   . VAL A 1 84  ? 113.21100 93.27200  86.34200  1.000 76.09737  ? 91  VAL A O   1 
ATOM   612  C CB  . VAL A 1 84  ? 113.25500 96.47300  86.85100  1.000 69.75668  ? 91  VAL A CB  1 
ATOM   613  C CG1 . VAL A 1 84  ? 112.60100 96.36900  88.20300  1.000 67.30647  ? 91  VAL A CG1 1 
ATOM   614  C CG2 . VAL A 1 84  ? 113.89000 97.83100  86.70500  1.000 70.64181  ? 91  VAL A CG2 1 
ATOM   615  N N   . ARG A 1 85  ? 114.10100 93.68800  88.37800  1.000 75.83082  ? 92  ARG A N   1 
ATOM   616  C CA  . ARG A 1 85  ? 113.72000 92.41400  88.96600  1.000 72.46993  ? 92  ARG A CA  1 
ATOM   617  C C   . ARG A 1 85  ? 112.20000 92.25300  88.97500  1.000 77.05448  ? 92  ARG A C   1 
ATOM   618  O O   . ARG A 1 85  ? 111.47100 93.23800  89.11300  1.000 78.61755  ? 92  ARG A O   1 
ATOM   619  C CB  . ARG A 1 85  ? 114.24500 92.34800  90.39900  1.000 70.71496  ? 92  ARG A CB  1 
ATOM   620  C CG  . ARG A 1 85  ? 114.19100 90.99100  91.05600  1.000 72.77538  ? 92  ARG A CG  1 
ATOM   621  C CD  . ARG A 1 85  ? 114.88000 91.01300  92.40200  1.000 73.21193  ? 92  ARG A CD  1 
ATOM   622  N NE  . ARG A 1 85  ? 114.14100 91.83500  93.35100  1.000 73.22494  ? 92  ARG A NE  1 
ATOM   623  C CZ  . ARG A 1 85  ? 114.69800 92.52900  94.33100  1.000 74.93444  ? 92  ARG A CZ  1 
ATOM   624  N NH1 . ARG A 1 85  ? 116.00200 92.50300  94.54100  1.000 74.06516  ? 92  ARG A NH1 1 
ATOM   625  N NH2 . ARG A 1 85  ? 113.92700 93.26300  95.12500  1.000 74.47813  ? 92  ARG A NH2 1 
ATOM   626  N N   . PRO A 1 86  ? 111.69300 91.03000  88.79800  1.000 70.46316  ? 93  PRO A N   1 
ATOM   627  C CA  . PRO A 1 86  ? 110.25300 90.79800  88.95600  1.000 67.80381  ? 93  PRO A CA  1 
ATOM   628  C C   . PRO A 1 86  ? 109.75500 91.31300  90.29800  1.000 68.54165  ? 93  PRO A C   1 
ATOM   629  O O   . PRO A 1 86  ? 110.43600 91.20400  91.31700  1.000 67.47416  ? 93  PRO A O   1 
ATOM   630  C CB  . PRO A 1 86  ? 110.12700 89.27600  88.84800  1.000 65.35169  ? 93  PRO A CB  1 
ATOM   631  C CG  . PRO A 1 86  ? 111.27600 88.88100  88.01300  1.000 66.63523  ? 93  PRO A CG  1 
ATOM   632  C CD  . PRO A 1 86  ? 112.39600 89.80000  88.40300  1.000 66.13034  ? 93  PRO A CD  1 
ATOM   633  N N   . ARG A 1 87  ? 108.54400 91.86700  90.29500  1.000 61.49420  ? 94  ARG A N   1 
ATOM   634  C CA  . ARG A 1 87  ? 108.02500 92.52000  91.49200  1.000 55.99795  ? 94  ARG A CA  1 
ATOM   635  C C   . ARG A 1 87  ? 107.47100 91.53800  92.51400  1.000 57.65767  ? 94  ARG A C   1 
ATOM   636  O O   . ARG A 1 87  ? 107.61600 91.75800  93.71900  1.000 61.48236  ? 94  ARG A O   1 
ATOM   637  C CB  . ARG A 1 87  ? 106.96100 93.54600  91.10900  1.000 56.78812  ? 94  ARG A CB  1 
ATOM   638  C CG  . ARG A 1 87  ? 107.52100 94.69800  90.31800  1.000 62.41086  ? 94  ARG A CG  1 
ATOM   639  C CD  . ARG A 1 87  ? 108.83900 95.10100  90.92700  1.000 57.87429  ? 94  ARG A CD  1 
ATOM   640  N NE  . ARG A 1 87  ? 109.31400 96.39600  90.47200  1.000 58.81632  ? 94  ARG A NE  1 
ATOM   641  C CZ  . ARG A 1 87  ? 110.45700 96.93300  90.86500  1.000 63.54370  ? 94  ARG A CZ  1 
ATOM   642  N NH1 . ARG A 1 87  ? 111.25800 96.30500  91.70700  1.000 67.33069  ? 94  ARG A NH1 1 
ATOM   643  N NH2 . ARG A 1 87  ? 110.80500 98.13000  90.40400  1.000 65.26773  ? 94  ARG A NH2 1 
ATOM   644  N N   . TRP A 1 88  ? 106.85200 90.44800  92.07000  1.000 52.55241  ? 95  TRP A N   1 
ATOM   645  C CA  . TRP A 1 88  ? 106.12400 89.56600  92.97400  1.000 50.81468  ? 95  TRP A CA  1 
ATOM   646  C C   . TRP A 1 88  ? 106.65200 88.13800  92.99600  1.000 54.78347  ? 95  TRP A C   1 
ATOM   647  O O   . TRP A 1 88  ? 105.91100 87.22200  93.35500  1.000 57.35494  ? 95  TRP A O   1 
ATOM   648  C CB  . TRP A 1 88  ? 104.63600 89.56700  92.63300  1.000 51.62458  ? 95  TRP A CB  1 
ATOM   649  C CG  . TRP A 1 88  ? 103.93900 90.87200  92.83400  1.000 48.51283  ? 95  TRP A CG  1 
ATOM   650  C CD1 . TRP A 1 88  ? 103.29500 91.60900  91.89200  1.000 57.48466  ? 95  TRP A CD1 1 
ATOM   651  C CD2 . TRP A 1 88  ? 103.73100 91.54600  94.07800  1.000 46.82694  ? 95  TRP A CD2 1 
ATOM   652  N NE1 . TRP A 1 88  ? 102.73800 92.72400  92.46200  1.000 62.19383  ? 95  TRP A NE1 1 
ATOM   653  C CE2 . TRP A 1 88  ? 102.98900 92.70300  93.80700  1.000 46.36247  ? 95  TRP A CE2 1 
ATOM   654  C CE3 . TRP A 1 88  ? 104.11700 91.29100  95.39200  1.000 55.15556  ? 95  TRP A CE3 1 
ATOM   655  C CZ2 . TRP A 1 88  ? 102.62500 93.59600  94.79600  1.000 43.59457  ? 95  TRP A CZ2 1 
ATOM   656  C CZ3 . TRP A 1 88  ? 103.75800 92.18200  96.36800  1.000 47.79262  ? 95  TRP A CZ3 1 
ATOM   657  C CH2 . TRP A 1 88  ? 103.02100 93.31800  96.06900  1.000 46.64283  ? 95  TRP A CH2 1 
ATOM   658  N N   . ASP A 1 89  ? 107.90700 87.91500  92.62700  1.000 56.99113  ? 96  ASP A N   1 
ATOM   659  C CA  . ASP A 1 89  ? 108.55900 86.71700  93.12300  1.000 52.82195  ? 96  ASP A CA  1 
ATOM   660  C C   . ASP A 1 89  ? 108.72300 86.81500  94.64200  1.000 59.93098  ? 96  ASP A C   1 
ATOM   661  O O   . ASP A 1 89  ? 108.49500 87.86400  95.24800  1.000 62.40595  ? 96  ASP A O   1 
ATOM   662  C CB  . ASP A 1 89  ? 109.88400 86.48600  92.39000  1.000 58.04232  ? 96  ASP A CB  1 
ATOM   663  C CG  . ASP A 1 89  ? 110.95700 87.51300  92.73400  1.000 64.52149  ? 96  ASP A CG  1 
ATOM   664  O OD1 . ASP A 1 89  ? 110.74400 88.38300  93.60000  1.000 67.34979  ? 96  ASP A OD1 1 
ATOM   665  O OD2 . ASP A 1 89  ? 112.04200 87.44500  92.12000  1.000 66.09960  ? 96  ASP A OD2 1 
ATOM   666  N N   . PHE A 1 90  ? 109.10800 85.70100  95.26900  1.000 54.05657  ? 97  PHE A N   1 
ATOM   667  C CA  . PHE A 1 90  ? 109.17500 85.67500  96.72800  1.000 47.70753  ? 97  PHE A CA  1 
ATOM   668  C C   . PHE A 1 90  ? 110.14500 86.71800  97.27100  1.000 48.08361  ? 97  PHE A C   1 
ATOM   669  O O   . PHE A 1 90  ? 109.89200 87.31900  98.31800  1.000 52.86546  ? 97  PHE A O   1 
ATOM   670  C CB  . PHE A 1 90  ? 109.56500 84.28200  97.21800  1.000 46.49110  ? 97  PHE A CB  1 
ATOM   671  C CG  . PHE A 1 90  ? 109.49400 84.12300  98.71400  1.000 50.12390  ? 97  PHE A CG  1 
ATOM   672  C CD1 . PHE A 1 90  ? 110.54900 84.49800  99.52200  1.000 53.63025  ? 97  PHE A CD1 1 
ATOM   673  C CD2 . PHE A 1 90  ? 108.37400 83.58300  99.30900  1.000 51.36695  ? 97  PHE A CD2 1 
ATOM   674  C CE1 . PHE A 1 90  ? 110.47700 84.35200  100.88600 1.000 51.12772  ? 97  PHE A CE1 1 
ATOM   675  C CE2 . PHE A 1 90  ? 108.30400 83.43200  100.67300 1.000 45.21104  ? 97  PHE A CE2 1 
ATOM   676  C CZ  . PHE A 1 90  ? 109.35600 83.81600  101.45900 1.000 45.50490  ? 97  PHE A CZ  1 
ATOM   677  N N   . THR A 1 91  ? 111.25000 86.96100  96.56900  1.000 51.29267  ? 98  THR A N   1 
ATOM   678  C CA  . THR A 1 91  ? 112.18800 87.99300  97.00400  1.000 54.63900  ? 98  THR A CA  1 
ATOM   679  C C   . THR A 1 91  ? 111.60200 89.39400  96.86000  1.000 55.73528  ? 98  THR A C   1 
ATOM   680  O O   . THR A 1 91  ? 111.73800 90.23000  97.76300  1.000 62.47791  ? 98  THR A O   1 
ATOM   681  C CB  . THR A 1 91  ? 113.48700 87.87600  96.21800  1.000 54.36379  ? 98  THR A CB  1 
ATOM   682  O OG1 . THR A 1 91  ? 114.12600 86.63900  96.54600  1.000 55.19299  ? 98  THR A OG1 1 
ATOM   683  C CG2 . THR A 1 91  ? 114.41300 89.01700  96.57300  1.000 52.89367  ? 98  THR A CG2 1 
ATOM   684  N N   . GLY A 1 92  ? 110.93700 89.66600  95.73900  1.000 49.62908  ? 99  GLY A N   1 
ATOM   685  C CA  . GLY A 1 92  ? 110.28100 90.95200  95.57600  1.000 48.75236  ? 99  GLY A CA  1 
ATOM   686  C C   . GLY A 1 92  ? 109.15200 91.17100  96.56200  1.000 53.00198  ? 99  GLY A C   1 
ATOM   687  O O   . GLY A 1 92  ? 108.97200 92.27700  97.07200  1.000 58.65459  ? 99  GLY A O   1 
ATOM   688  N N   . ALA A 1 93  ? 108.38300 90.12200  96.85500  1.000 48.04468  ? 100 ALA A N   1 
ATOM   689  C CA  . ALA A 1 93  ? 107.33300 90.23600  97.86000  1.000 43.82470  ? 100 ALA A CA  1 
ATOM   690  C C   . ALA A 1 93  ? 107.90500 90.42600  99.25800  1.000 46.44181  ? 100 ALA A C   1 
ATOM   691  O O   . ALA A 1 93  ? 107.31800 91.14000  100.07700 1.000 50.43234  ? 100 ALA A O   1 
ATOM   692  C CB  . ALA A 1 93  ? 106.42900 89.01000  97.81500  1.000 44.82461  ? 100 ALA A CB  1 
ATOM   693  N N   . PHE A 1 94  ? 109.04000 89.79500  99.55700  1.000 42.05509  ? 101 PHE A N   1 
ATOM   694  C CA  . PHE A 1 94  ? 109.69000 90.02600  100.84500 1.000 38.65585  ? 101 PHE A CA  1 
ATOM   695  C C   . PHE A 1 94  ? 110.20200 91.45500  100.96700 1.000 39.65521  ? 101 PHE A C   1 
ATOM   696  O O   . PHE A 1 94  ? 110.08400 92.07300  102.02900 1.000 48.11627  ? 101 PHE A O   1 
ATOM   697  C CB  . PHE A 1 94  ? 110.83400 89.03500  101.04200 1.000 40.45439  ? 101 PHE A CB  1 
ATOM   698  C CG  . PHE A 1 94  ? 111.42700 89.06200  102.41800 1.000 45.73538  ? 101 PHE A CG  1 
ATOM   699  C CD1 . PHE A 1 94  ? 112.40100 89.98000  102.74900 1.000 44.90262  ? 101 PHE A CD1 1 
ATOM   700  C CD2 . PHE A 1 94  ? 111.01600 88.16300  103.37600 1.000 51.66962  ? 101 PHE A CD2 1 
ATOM   701  C CE1 . PHE A 1 94  ? 112.94200 90.00500  104.00700 1.000 47.31780  ? 101 PHE A CE1 1 
ATOM   702  C CE2 . PHE A 1 94  ? 111.55700 88.18500  104.63800 1.000 43.03145  ? 101 PHE A CE2 1 
ATOM   703  C CZ  . PHE A 1 94  ? 112.52000 89.10500  104.95200 1.000 44.59498  ? 101 PHE A CZ  1 
ATOM   704  N N   . TYR A 1 95  ? 110.72200 92.01700  99.87900  1.000 41.34011  ? 102 TYR A N   1 
ATOM   705  C CA  . TYR A 1 95  ? 111.09100 93.42800  99.89500  1.000 43.68254  ? 102 TYR A CA  1 
ATOM   706  C C   . TYR A 1 95  ? 109.86400 94.31300  100.08600 1.000 38.59951  ? 102 TYR A C   1 
ATOM   707  O O   . TYR A 1 95  ? 109.89800 95.27500  100.86300 1.000 42.14518  ? 102 TYR A O   1 
ATOM   708  C CB  . TYR A 1 95  ? 111.82500 93.77100  98.60100  1.000 48.61651  ? 102 TYR A CB  1 
ATOM   709  C CG  . TYR A 1 95  ? 112.61800 95.05600  98.61600  1.000 45.26464  ? 102 TYR A CG  1 
ATOM   710  C CD1 . TYR A 1 95  ? 112.74900 95.80400  99.76700  1.000 44.35293  ? 102 TYR A CD1 1 
ATOM   711  C CD2 . TYR A 1 95  ? 113.29800 95.47700  97.48900  1.000 46.71913  ? 102 TYR A CD2 1 
ATOM   712  C CE1 . TYR A 1 95  ? 113.46200 96.97700  99.77200  1.000 44.12670  ? 102 TYR A CE1 1 
ATOM   713  C CE2 . TYR A 1 95  ? 114.04000 96.62900  97.49700  1.000 49.85507  ? 102 TYR A CE2 1 
ATOM   714  C CZ  . TYR A 1 95  ? 114.11300 97.37800  98.63900  1.000 50.81986  ? 102 TYR A CZ  1 
ATOM   715  O OH  . TYR A 1 95  ? 114.87900 98.51300  98.66200  1.000 54.87690  ? 102 TYR A OH  1 
ATOM   716  N N   . PHE A 1 96  ? 108.78000 94.01600  99.37300  1.000 33.49244  ? 103 PHE A N   1 
ATOM   717  C CA  . PHE A 1 96  ? 107.54700 94.77800  99.54000  1.000 23.33729  ? 103 PHE A CA  1 
ATOM   718  C C   . PHE A 1 96  ? 107.06700 94.78000  100.98400 1.000 37.08007  ? 103 PHE A C   1 
ATOM   719  O O   . PHE A 1 96  ? 106.77900 95.84000  101.54300 1.000 49.72589  ? 103 PHE A O   1 
ATOM   720  C CB  . PHE A 1 96  ? 106.45200 94.24700  98.62700  1.000 35.25569  ? 103 PHE A CB  1 
ATOM   721  C CG  . PHE A 1 96  ? 105.12200 94.87000  98.88800  1.000 36.09489  ? 103 PHE A CG  1 
ATOM   722  C CD1 . PHE A 1 96  ? 104.89500 96.19100  98.58000  1.000 42.20759  ? 103 PHE A CD1 1 
ATOM   723  C CD2 . PHE A 1 96  ? 104.10000 94.13800  99.43800  1.000 35.23603  ? 103 PHE A CD2 1 
ATOM   724  C CE1 . PHE A 1 96  ? 103.67800 96.76500  98.82600  1.000 39.49905  ? 103 PHE A CE1 1 
ATOM   725  C CE2 . PHE A 1 96  ? 102.88100 94.70900  99.68000  1.000 36.28037  ? 103 PHE A CE2 1 
ATOM   726  C CZ  . PHE A 1 96  ? 102.67000 96.02100  99.37300  1.000 38.18752  ? 103 PHE A CZ  1 
ATOM   727  N N   . VAL A 1 97  ? 106.90700 93.59800  101.58500 1.000 39.77606  ? 104 VAL A N   1 
ATOM   728  C CA  . VAL A 1 97  ? 106.44100 93.54500  102.96900 1.000 26.72294  ? 104 VAL A CA  1 
ATOM   729  C C   . VAL A 1 97  ? 107.43200 94.20600  103.91500 1.000 29.51870  ? 104 VAL A C   1 
ATOM   730  O O   . VAL A 1 97  ? 107.03100 94.77200  104.93400 1.000 42.10982  ? 104 VAL A O   1 
ATOM   731  C CB  . VAL A 1 97  ? 106.12400 92.10100  103.40000 1.000 27.06208  ? 104 VAL A CB  1 
ATOM   732  C CG1 . VAL A 1 97  ? 105.04100 91.52400  102.53100 1.000 32.64357  ? 104 VAL A CG1 1 
ATOM   733  C CG2 . VAL A 1 97  ? 107.34500 91.24300  103.34800 1.000 35.77683  ? 104 VAL A CG2 1 
ATOM   734  N N   . GLY A 1 98  ? 108.72900 94.13600  103.62600 1.000 32.93955  ? 105 GLY A N   1 
ATOM   735  C CA  . GLY A 1 98  ? 109.68100 94.91100  104.40400 1.000 27.33046  ? 105 GLY A CA  1 
ATOM   736  C C   . GLY A 1 98  ? 109.43000 96.40700  104.35600 1.000 27.52197  ? 105 GLY A C   1 
ATOM   737  O O   . GLY A 1 98  ? 109.56300 97.09800  105.36500 1.000 34.69505  ? 105 GLY A O   1 
ATOM   738  N N   . THR A 1 99  ? 109.07200 96.93000  103.18400 1.000 27.57667  ? 106 THR A N   1 
ATOM   739  C CA  . THR A 1 99  ? 108.75600 98.35400  103.08500 1.000 25.40287  ? 106 THR A CA  1 
ATOM   740  C C   . THR A 1 99  ? 107.38200 98.71400  103.64200 1.000 25.23860  ? 106 THR A C   1 
ATOM   741  O O   . THR A 1 99  ? 107.17400 99.85600  104.05800 1.000 32.77055  ? 106 THR A O   1 
ATOM   742  C CB  . THR A 1 99  ? 108.85500 98.83400  101.63800 1.000 31.79317  ? 106 THR A CB  1 
ATOM   743  O OG1 . THR A 1 99  ? 107.81000 98.24900  100.85800 1.000 40.14285  ? 106 THR A OG1 1 
ATOM   744  C CG2 . THR A 1 99  ? 110.19500 98.47200  101.04500 1.000 35.42733  ? 106 THR A CG2 1 
ATOM   745  N N   . VAL A 1 100 ? 106.43100 97.78600  103.64000 1.000 25.06658  ? 107 VAL A N   1 
ATOM   746  C CA  . VAL A 1 100 ? 105.14900 98.02800  104.30300 1.000 20.42464  ? 107 VAL A CA  1 
ATOM   747  C C   . VAL A 1 100 ? 105.31700 98.06300  105.81700 1.000 34.84734  ? 107 VAL A C   1 
ATOM   748  O O   . VAL A 1 100 ? 104.90000 99.01500  106.48300 1.000 41.82803  ? 107 VAL A O   1 
ATOM   749  C CB  . VAL A 1 100 ? 104.11800 96.96800  103.88300 1.000 22.82553  ? 107 VAL A CB  1 
ATOM   750  C CG1 . VAL A 1 100 ? 102.97700 96.92900  104.86200 1.000 17.66010  ? 107 VAL A CG1 1 
ATOM   751  C CG2 . VAL A 1 100 ? 103.59300 97.27400  102.51600 1.000 33.98118  ? 107 VAL A CG2 1 
ATOM   752  N N   . VAL A 1 101 ? 105.91900 97.01800  106.38200 1.000 37.91131  ? 108 VAL A N   1 
ATOM   753  C CA  . VAL A 1 101 ? 105.96500 96.83400  107.82800 1.000 22.85858  ? 108 VAL A CA  1 
ATOM   754  C C   . VAL A 1 101 ? 106.83500 97.88100  108.51800 1.000 32.10978  ? 108 VAL A C   1 
ATOM   755  O O   . VAL A 1 101 ? 106.54500 98.28100  109.64900 1.000 36.31507  ? 108 VAL A O   1 
ATOM   756  C CB  . VAL A 1 101 ? 106.43500 95.39900  108.11800 1.000 29.96104  ? 108 VAL A CB  1 
ATOM   757  C CG1 . VAL A 1 101 ? 106.78300 95.22300  109.55000 1.000 37.29144  ? 108 VAL A CG1 1 
ATOM   758  C CG2 . VAL A 1 101 ? 105.34600 94.42800  107.74700 1.000 34.69701  ? 108 VAL A CG2 1 
ATOM   759  N N   . SER A 1 102 ? 107.88900 98.35900  107.86700 1.000 36.62029  ? 109 SER A N   1 
ATOM   760  C CA  . SER A 1 102 ? 108.64500 99.49300  108.38800 1.000 24.61483  ? 109 SER A CA  1 
ATOM   761  C C   . SER A 1 102 ? 108.01100 100.84000 108.07300 1.000 33.47176  ? 109 SER A C   1 
ATOM   762  O O   . SER A 1 102 ? 108.55900 101.86600 108.48200 1.000 41.39810  ? 109 SER A O   1 
ATOM   763  C CB  . SER A 1 102 ? 110.07600 99.46000  107.86200 1.000 29.82328  ? 109 SER A CB  1 
ATOM   764  O OG  . SER A 1 102 ? 110.09100 99.50100  106.45500 1.000 38.25033  ? 109 SER A OG  1 
ATOM   765  N N   . THR A 1 103 ? 106.88900 100.86200 107.35800 1.000 36.87531  ? 110 THR A N   1 
ATOM   766  C CA  . THR A 1 103 ? 106.23200 102.04600 106.80800 1.000 27.28372  ? 110 THR A CA  1 
ATOM   767  C C   . THR A 1 103 ? 107.09800 102.86200 105.85700 1.000 22.06926  ? 110 THR A C   1 
ATOM   768  O O   . THR A 1 103 ? 106.76100 104.01500 105.57700 1.000 30.17741  ? 110 THR A O   1 
ATOM   769  C CB  . THR A 1 103 ? 105.70800 102.97600 107.90700 1.000 31.17429  ? 110 THR A CB  1 
ATOM   770  O OG1 . THR A 1 103 ? 106.81100 103.60600 108.56100 1.000 34.11651  ? 110 THR A OG1 1 
ATOM   771  C CG2 . THR A 1 103 ? 104.90100 102.20800 108.92300 1.000 24.78474  ? 110 THR A CG2 1 
ATOM   772  N N   . ILE A 1 104 ? 108.22300 102.33200 105.37600 1.000 25.74493  ? 111 ILE A N   1 
ATOM   773  C CA  . ILE A 1 104 ? 108.99600 103.07500 104.38100 1.000 15.00497  ? 111 ILE A CA  1 
ATOM   774  C C   . ILE A 1 104 ? 108.16500 103.29400 103.12600 1.000 22.03549  ? 111 ILE A C   1 
ATOM   775  O O   . ILE A 1 104 ? 108.01300 104.42300 102.65000 1.000 37.08018  ? 111 ILE A O   1 
ATOM   776  C CB  . ILE A 1 104 ? 110.32200 102.36800 104.06500 1.000 16.39840  ? 111 ILE A CB  1 
ATOM   777  C CG1 . ILE A 1 104 ? 111.19500 102.28000 105.30600 1.000 30.39282  ? 111 ILE A CG1 1 
ATOM   778  C CG2 . ILE A 1 104 ? 111.06200 103.12300 103.01500 1.000 22.32080  ? 111 ILE A CG2 1 
ATOM   779  C CD1 . ILE A 1 104 ? 112.34100 101.33000 105.15600 1.000 23.37161  ? 111 ILE A CD1 1 
ATOM   780  N N   . GLY A 1 105 ? 107.58800 102.22600 102.59200 1.000 29.33534  ? 112 GLY A N   1 
ATOM   781  C CA  . GLY A 1 105 ? 106.68900 102.34800 101.46500 1.000 25.55357  ? 112 GLY A CA  1 
ATOM   782  C C   . GLY A 1 105 ? 107.24700 103.01000 100.22400 1.000 23.98963  ? 112 GLY A C   1 
ATOM   783  O O   . GLY A 1 105 ? 106.69600 104.01200 99.76600  1.000 30.95393  ? 112 GLY A O   1 
ATOM   784  N N   . PHE A 1 106 ? 108.36700 102.50500 99.70200  1.000 31.83940  ? 113 PHE A N   1 
ATOM   785  C CA  . PHE A 1 106 ? 108.93700 103.07600 98.48500  1.000 28.29747  ? 113 PHE A CA  1 
ATOM   786  C C   . PHE A 1 106 ? 107.91500 103.11500 97.36300  1.000 30.50866  ? 113 PHE A C   1 
ATOM   787  O O   . PHE A 1 106 ? 107.87700 104.06500 96.57700  1.000 44.45142  ? 113 PHE A O   1 
ATOM   788  C CB  . PHE A 1 106 ? 110.15500 102.27800 98.02800  1.000 32.58156  ? 113 PHE A CB  1 
ATOM   789  C CG  . PHE A 1 106 ? 111.34200 102.39200 98.92700  1.000 36.29745  ? 113 PHE A CG  1 
ATOM   790  C CD1 . PHE A 1 106 ? 111.83000 103.62400 99.29400  1.000 34.15369  ? 113 PHE A CD1 1 
ATOM   791  C CD2 . PHE A 1 106 ? 111.98800 101.26400 99.38100  1.000 33.90740  ? 113 PHE A CD2 1 
ATOM   792  C CE1 . PHE A 1 106 ? 112.92700 103.72500 100.10100 1.000 41.19210  ? 113 PHE A CE1 1 
ATOM   793  C CE2 . PHE A 1 106 ? 113.08300 101.36300 100.19100 1.000 30.93755  ? 113 PHE A CE2 1 
ATOM   794  C CZ  . PHE A 1 106 ? 113.55400 102.59300 100.55000 1.000 37.95640  ? 113 PHE A CZ  1 
ATOM   795  N N   . GLY A 1 107 ? 107.07600 102.09200 97.27400  1.000 35.85254  ? 114 GLY A N   1 
ATOM   796  C CA  . GLY A 1 107 ? 106.00500 102.09200 96.30500  1.000 34.77039  ? 114 GLY A CA  1 
ATOM   797  C C   . GLY A 1 107 ? 106.44600 101.78000 94.90200  1.000 37.19810  ? 114 GLY A C   1 
ATOM   798  O O   . GLY A 1 107 ? 105.73200 102.10600 93.95200  1.000 48.48424  ? 114 GLY A O   1 
ATOM   799  N N   . MET A 1 108 ? 107.62000 101.17100 94.74300  1.000 39.31894  ? 115 MET A N   1 
ATOM   800  C CA  . MET A 1 108 ? 108.00700 100.60300 93.45800  1.000 48.83082  ? 115 MET A CA  1 
ATOM   801  C C   . MET A 1 108 ? 107.20400 99.34400  93.16300  1.000 53.98044  ? 115 MET A C   1 
ATOM   802  O O   . MET A 1 108 ? 106.82100 99.09700  92.01400  1.000 56.03513  ? 115 MET A O   1 
ATOM   803  C CB  . MET A 1 108 ? 109.50900 100.32000 93.44700  1.000 46.27741  ? 115 MET A CB  1 
ATOM   804  C CG  . MET A 1 108 ? 109.91600 99.06500  94.20000  1.000 52.37639  ? 115 MET A CG  1 
ATOM   805  S SD  . MET A 1 108 ? 109.68300 99.18200  95.98100  1.000 64.20467  ? 115 MET A SD  1 
ATOM   806  C CE  . MET A 1 108 ? 110.50700 97.69700  96.53000  1.000 45.34197  ? 115 MET A CE  1 
ATOM   807  N N   . THR A 1 109 ? 106.94100 98.54200  94.19200  1.000 50.33003  ? 116 THR A N   1 
ATOM   808  C CA  . THR A 1 109 ? 105.98500 97.44500  94.15800  1.000 45.80371  ? 116 THR A CA  1 
ATOM   809  C C   . THR A 1 109 ? 104.75800 97.84400  94.96400  1.000 40.61496  ? 116 THR A C   1 
ATOM   810  O O   . THR A 1 109 ? 104.88400 98.27700  96.11300  1.000 38.31190  ? 116 THR A O   1 
ATOM   811  C CB  . THR A 1 109 ? 106.60600 96.17800  94.74500  1.000 48.10637  ? 116 THR A CB  1 
ATOM   812  O OG1 . THR A 1 109 ? 107.77000 95.81800  93.99800  1.000 58.45325  ? 116 THR A OG1 1 
ATOM   813  C CG2 . THR A 1 109 ? 105.64600 95.05200  94.67400  1.000 51.48808  ? 116 THR A CG2 1 
ATOM   814  N N   . THR A 1 110 ? 103.57500 97.68700  94.36900  1.000 48.58707  ? 117 THR A N   1 
ATOM   815  C CA  . THR A 1 110 ? 102.32400 97.99800  95.04200  1.000 49.60227  ? 117 THR A CA  1 
ATOM   816  C C   . THR A 1 110 ? 101.26500 96.97300  94.66500  1.000 56.29365  ? 117 THR A C   1 
ATOM   817  O O   . THR A 1 110 ? 101.23100 96.51000  93.51700  1.000 58.41984  ? 117 THR A O   1 
ATOM   818  C CB  . THR A 1 110 ? 101.81800 99.39500  94.66300  1.000 56.25646  ? 117 THR A CB  1 
ATOM   819  O OG1 . THR A 1 110 ? 101.85600 99.54400  93.24100  1.000 62.30503  ? 117 THR A OG1 1 
ATOM   820  C CG2 . THR A 1 110 ? 102.68000 100.46600 95.28000  1.000 59.25659  ? 117 THR A CG2 1 
ATOM   821  N N   . PRO A 1 111 ? 100.38900 96.61100  95.59700  1.000 52.00143  ? 118 PRO A N   1 
ATOM   822  C CA  . PRO A 1 111 ? 99.35000  95.62400  95.29400  1.000 48.82815  ? 118 PRO A CA  1 
ATOM   823  C C   . PRO A 1 111 ? 98.35000  96.16500  94.28800  1.000 53.49785  ? 118 PRO A C   1 
ATOM   824  O O   . PRO A 1 111 ? 98.06200  97.36200  94.24600  1.000 52.15278  ? 118 PRO A O   1 
ATOM   825  C CB  . PRO A 1 111 ? 98.69700  95.37000  96.65400  1.000 43.76565  ? 118 PRO A CB  1 
ATOM   826  C CG  . PRO A 1 111 ? 98.91500  96.61800  97.39600  1.000 48.65652  ? 118 PRO A CG  1 
ATOM   827  C CD  . PRO A 1 111 ? 100.25100 97.14200  96.96000  1.000 48.75449  ? 118 PRO A CD  1 
ATOM   828  N N   . ALA A 1 112 ? 97.81800  95.26600  93.46400  1.000 58.30243  ? 119 ALA A N   1 
ATOM   829  C CA  . ALA A 1 112 ? 96.99000  95.69200  92.34400  1.000 61.76630  ? 119 ALA A CA  1 
ATOM   830  C C   . ALA A 1 112 ? 95.64900  94.97100  92.30200  1.000 64.62654  ? 119 ALA A C   1 
ATOM   831  O O   . ALA A 1 112 ? 94.65500  95.53800  91.84100  1.000 65.84334  ? 119 ALA A O   1 
ATOM   832  C CB  . ALA A 1 112 ? 97.73900  95.48000  91.03000  1.000 62.11594  ? 119 ALA A CB  1 
ATOM   833  N N   . THR A 1 113 ? 95.60100  93.73200  92.77300  1.000 60.05650  ? 120 THR A N   1 
ATOM   834  C CA  . THR A 1 113 ? 94.33000  93.04100  92.91700  1.000 60.65542  ? 120 THR A CA  1 
ATOM   835  C C   . THR A 1 113 ? 93.57000  93.56400  94.13100  1.000 62.59455  ? 120 THR A C   1 
ATOM   836  O O   . THR A 1 113 ? 94.15800  94.08500  95.08100  1.000 63.25239  ? 120 THR A O   1 
ATOM   837  C CB  . THR A 1 113 ? 94.54600  91.53600  93.04500  1.000 59.38832  ? 120 THR A CB  1 
ATOM   838  O OG1 . THR A 1 113 ? 95.37500  91.27000  94.18000  1.000 61.50389  ? 120 THR A OG1 1 
ATOM   839  C CG2 . THR A 1 113 ? 95.21100  90.98600  91.80000  1.000 55.82923  ? 120 THR A CG2 1 
ATOM   840  N N   . VAL A 1 114 ? 92.24200  93.43200  94.08500  1.000 57.43347  ? 121 VAL A N   1 
ATOM   841  C CA  . VAL A 1 114 ? 91.41700  93.77900  95.24000  1.000 51.56789  ? 121 VAL A CA  1 
ATOM   842  C C   . VAL A 1 114 ? 91.72300  92.88900  96.43700  1.000 53.17567  ? 121 VAL A C   1 
ATOM   843  O O   . VAL A 1 114 ? 91.64500  93.34000  97.58500  1.000 57.05736  ? 121 VAL A O   1 
ATOM   844  C CB  . VAL A 1 114 ? 89.92300  93.72700  94.87000  1.000 53.59770  ? 121 VAL A CB  1 
ATOM   845  C CG1 . VAL A 1 114 ? 89.61700  94.75300  93.80100  1.000 59.13803  ? 121 VAL A CG1 1 
ATOM   846  C CG2 . VAL A 1 114 ? 89.53500  92.34100  94.40000  1.000 56.06874  ? 121 VAL A CG2 1 
ATOM   847  N N   . GLY A 1 115 ? 92.06900  91.62300  96.20700  1.000 48.73347  ? 122 GLY A N   1 
ATOM   848  C CA  . GLY A 1 115 ? 92.48900  90.77800  97.31200  1.000 43.83007  ? 122 GLY A CA  1 
ATOM   849  C C   . GLY A 1 115 ? 93.76500  91.26100  97.97200  1.000 44.89898  ? 122 GLY A C   1 
ATOM   850  O O   . GLY A 1 115 ? 93.87900  91.26100  99.19900  1.000 52.32953  ? 122 GLY A O   1 
ATOM   851  N N   . GLY A 1 116 ? 94.72100  91.72500  97.17200  1.000 35.67406  ? 123 GLY A N   1 
ATOM   852  C CA  . GLY A 1 116 ? 95.92200  92.31400  97.73700  1.000 38.19498  ? 123 GLY A CA  1 
ATOM   853  C C   . GLY A 1 116 ? 95.65300  93.59700  98.49600  1.000 44.34102  ? 123 GLY A C   1 
ATOM   854  O O   . GLY A 1 116 ? 96.20700  93.81700  99.57400  1.000 50.01596  ? 123 GLY A O   1 
ATOM   855  N N   . LYS A 1 117 ? 94.79800  94.45800  97.94800  1.000 48.24067  ? 124 LYS A N   1 
ATOM   856  C CA  . LYS A 1 117 ? 94.43900  95.69400  98.63500  1.000 45.08013  ? 124 LYS A CA  1 
ATOM   857  C C   . LYS A 1 117 ? 93.73500  95.43100  99.96200  1.000 48.67650  ? 124 LYS A C   1 
ATOM   858  O O   . LYS A 1 117 ? 94.01700  96.10300  100.95800 1.000 56.27960  ? 124 LYS A O   1 
ATOM   859  C CB  . LYS A 1 117 ? 93.56500  96.55200  97.72500  1.000 47.11491  ? 124 LYS A CB  1 
ATOM   860  C CG  . LYS A 1 117 ? 94.33000  97.21000  96.59700  1.000 50.76447  ? 124 LYS A CG  1 
ATOM   861  C CD  . LYS A 1 117 ? 93.42000  98.00300  95.68700  1.000 49.04817  ? 124 LYS A CD  1 
ATOM   862  C CE  . LYS A 1 117 ? 94.22600  98.83600  94.71400  1.000 47.78851  ? 124 LYS A CE  1 
ATOM   863  N NZ  . LYS A 1 117 ? 93.37700  99.40000  93.63800  1.000 46.84547  ? 124 LYS A NZ  1 
ATOM   864  N N   . ILE A 1 118 ? 92.81000  94.46900  100.00100 1.000 39.42243  ? 125 ILE A N   1 
ATOM   865  C CA  . ILE A 1 118 ? 92.17300  94.11000  101.26800 1.000 31.17600  ? 125 ILE A CA  1 
ATOM   866  C C   . ILE A 1 118 ? 93.19600  93.56500  102.25400 1.000 37.32334  ? 125 ILE A C   1 
ATOM   867  O O   . ILE A 1 118 ? 93.25700  93.99400  103.40900 1.000 45.24874  ? 125 ILE A O   1 
ATOM   868  C CB  . ILE A 1 118 ? 91.04000  93.09600  101.04300 1.000 32.22679  ? 125 ILE A CB  1 
ATOM   869  C CG1 . ILE A 1 118 ? 89.87600  93.72400  100.29200 1.000 39.88209  ? 125 ILE A CG1 1 
ATOM   870  C CG2 . ILE A 1 118 ? 90.55800  92.55400  102.36200 1.000 32.47475  ? 125 ILE A CG2 1 
ATOM   871  C CD1 . ILE A 1 118 ? 88.88500  92.71100  99.78700  1.000 44.71451  ? 125 ILE A CD1 1 
ATOM   872  N N   . PHE A 1 119 ? 94.00900  92.60100  101.81600 1.000 42.06577  ? 126 PHE A N   1 
ATOM   873  C CA  . PHE A 1 119 ? 94.96300  91.96100  102.71600 1.000 36.32814  ? 126 PHE A CA  1 
ATOM   874  C C   . PHE A 1 119 ? 95.97700  92.94900  103.27500 1.000 35.90183  ? 126 PHE A C   1 
ATOM   875  O O   . PHE A 1 119 ? 96.42500  92.80100  104.41500 1.000 46.05176  ? 126 PHE A O   1 
ATOM   876  C CB  . PHE A 1 119 ? 95.67800  90.82400  101.99300 1.000 37.76421  ? 126 PHE A CB  1 
ATOM   877  C CG  . PHE A 1 119 ? 96.65100  90.07700  102.85100 1.000 36.28821  ? 126 PHE A CG  1 
ATOM   878  C CD1 . PHE A 1 119 ? 96.22900  89.42100  103.98400 1.000 42.39649  ? 126 PHE A CD1 1 
ATOM   879  C CD2 . PHE A 1 119 ? 97.98600  90.02000  102.51800 1.000 39.52021  ? 126 PHE A CD2 1 
ATOM   880  C CE1 . PHE A 1 119 ? 97.12100  88.73000  104.77000 1.000 43.96911  ? 126 PHE A CE1 1 
ATOM   881  C CE2 . PHE A 1 119 ? 98.87800  89.33200  103.30200 1.000 38.51161  ? 126 PHE A CE2 1 
ATOM   882  C CZ  . PHE A 1 119 ? 98.44600  88.68800  104.42700 1.000 40.80310  ? 126 PHE A CZ  1 
ATOM   883  N N   . LEU A 1 120 ? 96.37300  93.94300  102.48000 1.000 33.66288  ? 127 LEU A N   1 
ATOM   884  C CA  . LEU A 1 120 ? 97.26800  94.98300  102.97800 1.000 33.37872  ? 127 LEU A CA  1 
ATOM   885  C C   . LEU A 1 120 ? 96.69800  95.72400  104.18000 1.000 42.23353  ? 127 LEU A C   1 
ATOM   886  O O   . LEU A 1 120 ? 97.43300  96.03700  105.11500 1.000 49.77427  ? 127 LEU A O   1 
ATOM   887  C CB  . LEU A 1 120 ? 97.60300  95.97000  101.86800 1.000 36.19995  ? 127 LEU A CB  1 
ATOM   888  C CG  . LEU A 1 120 ? 98.51900  97.08800  102.34600 1.000 33.65728  ? 127 LEU A CG  1 
ATOM   889  C CD1 . LEU A 1 120 ? 99.87500  96.53000  102.65600 1.000 38.91315  ? 127 LEU A CD1 1 
ATOM   890  C CD2 . LEU A 1 120 ? 98.62400  98.16100  101.30100 1.000 43.70962  ? 127 LEU A CD2 1 
ATOM   891  N N   . ILE A 1 121 ? 95.39500  95.99900  104.19400 1.000 42.82866  ? 128 ILE A N   1 
ATOM   892  C CA  . ILE A 1 121 ? 94.84400  96.82300  105.27100 1.000 40.94371  ? 128 ILE A CA  1 
ATOM   893  C C   . ILE A 1 121 ? 94.92100  96.11800  106.62300 1.000 41.04687  ? 128 ILE A C   1 
ATOM   894  O O   . ILE A 1 121 ? 95.04300  96.77600  107.66100 1.000 49.25848  ? 128 ILE A O   1 
ATOM   895  C CB  . ILE A 1 121 ? 93.40900  97.25600  104.91900 1.000 39.72283  ? 128 ILE A CB  1 
ATOM   896  C CG1 . ILE A 1 121 ? 93.42600  98.20100  103.71800 1.000 36.52619  ? 128 ILE A CG1 1 
ATOM   897  C CG2 . ILE A 1 121 ? 92.74300  97.94500  106.08300 1.000 40.63601  ? 128 ILE A CG2 1 
ATOM   898  C CD1 . ILE A 1 121 ? 92.07600  98.43500  103.11300 1.000 37.49644  ? 128 ILE A CD1 1 
ATOM   899  N N   . PHE A 1 122 ? 94.87600  94.79100  106.65000 1.000 38.68727  ? 129 PHE A N   1 
ATOM   900  C CA  . PHE A 1 122 ? 95.07100  94.05500  107.89600 1.000 39.10113  ? 129 PHE A CA  1 
ATOM   901  C C   . PHE A 1 122 ? 96.53200  93.72100  108.17400 1.000 42.14519  ? 129 PHE A C   1 
ATOM   902  O O   . PHE A 1 122 ? 96.99300  93.82700  109.32300 1.000 55.70055  ? 129 PHE A O   1 
ATOM   903  C CB  . PHE A 1 122 ? 94.25100  92.76700  107.87400 1.000 38.27563  ? 129 PHE A CB  1 
ATOM   904  C CG  . PHE A 1 122 ? 92.78900  92.99300  107.66200 1.000 42.67662  ? 129 PHE A CG  1 
ATOM   905  C CD1 . PHE A 1 122 ? 92.08300  93.83900  108.49100 1.000 44.12897  ? 129 PHE A CD1 1 
ATOM   906  C CD2 . PHE A 1 122 ? 92.12000  92.36000  106.63600 1.000 45.57199  ? 129 PHE A CD2 1 
ATOM   907  C CE1 . PHE A 1 122 ? 90.74100  94.05000  108.29900 1.000 45.55006  ? 129 PHE A CE1 1 
ATOM   908  C CE2 . PHE A 1 122 ? 90.77700  92.56900  106.44000 1.000 50.57788  ? 129 PHE A CE2 1 
ATOM   909  C CZ  . PHE A 1 122 ? 90.08700  93.41500  107.27300 1.000 47.55327  ? 129 PHE A CZ  1 
ATOM   910  N N   . TYR A 1 123 ? 97.28600  93.36300  107.13600 1.000 39.40856  ? 130 TYR A N   1 
ATOM   911  C CA  . TYR A 1 123 ? 98.68400  93.02100  107.33300 1.000 36.88891  ? 130 TYR A CA  1 
ATOM   912  C C   . TYR A 1 123 ? 99.49100  94.22500  107.78400 1.000 38.76248  ? 130 TYR A C   1 
ATOM   913  O O   . TYR A 1 123 ? 100.27600 94.12300  108.72600 1.000 53.01347  ? 130 TYR A O   1 
ATOM   914  C CB  . TYR A 1 123 ? 99.24900  92.45900  106.03300 1.000 44.97718  ? 130 TYR A CB  1 
ATOM   915  C CG  . TYR A 1 123 ? 100.67400 91.99500  106.11000 1.000 47.26383  ? 130 TYR A CG  1 
ATOM   916  C CD1 . TYR A 1 123 ? 100.97500 90.70000  106.48100 1.000 47.03629  ? 130 TYR A CD1 1 
ATOM   917  C CD2 . TYR A 1 123 ? 101.71800 92.85300  105.81700 1.000 46.63759  ? 130 TYR A CD2 1 
ATOM   918  C CE1 . TYR A 1 123 ? 102.26800 90.27100  106.54400 1.000 45.81986  ? 130 TYR A CE1 1 
ATOM   919  C CE2 . TYR A 1 123 ? 103.01400 92.43300  105.88800 1.000 43.14752  ? 130 TYR A CE2 1 
ATOM   920  C CZ  . TYR A 1 123 ? 103.28300 91.14100  106.25000 1.000 47.56123  ? 130 TYR A CZ  1 
ATOM   921  O OH  . TYR A 1 123 ? 104.58000 90.71300  106.32800 1.000 56.44613  ? 130 TYR A OH  1 
ATOM   922  N N   . GLY A 1 124 ? 99.30100  95.37800  107.14900 1.000 29.62981  ? 131 GLY A N   1 
ATOM   923  C CA  . GLY A 1 124 ? 99.99800  96.57000  107.58000 1.000 34.37981  ? 131 GLY A CA  1 
ATOM   924  C C   . GLY A 1 124 ? 99.54600  97.03600  108.94200 1.000 38.75007  ? 131 GLY A C   1 
ATOM   925  O O   . GLY A 1 124 ? 100.35400 97.52400  109.72900 1.000 43.25632  ? 131 GLY A O   1 
ATOM   926  N N   . LEU A 1 125 ? 98.27200  96.82400  109.26400 1.000 37.40642  ? 132 LEU A N   1 
ATOM   927  C CA  . LEU A 1 125 ? 97.73400  97.23200  110.55800 1.000 39.12601  ? 132 LEU A CA  1 
ATOM   928  C C   . LEU A 1 125 ? 98.39900  96.48800  111.70800 1.000 40.03866  ? 132 LEU A C   1 
ATOM   929  O O   . LEU A 1 125 ? 98.76700  97.09600  112.71800 1.000 42.53208  ? 132 LEU A O   1 
ATOM   930  C CB  . LEU A 1 125 ? 96.22500  97.00500  110.58400 1.000 42.70367  ? 132 LEU A CB  1 
ATOM   931  C CG  . LEU A 1 125 ? 95.49000  97.27900  111.88800 1.000 40.85427  ? 132 LEU A CG  1 
ATOM   932  C CD1 . LEU A 1 125 ? 95.63700  98.73300  112.26100 1.000 40.35911  ? 132 LEU A CD1 1 
ATOM   933  C CD2 . LEU A 1 125 ? 94.03500  96.90800  111.74700 1.000 42.57947  ? 132 LEU A CD2 1 
ATOM   934  N N   . VAL A 1 126 ? 98.54000  95.16900  111.59400 1.000 34.14451  ? 133 VAL A N   1 
ATOM   935  C CA  . VAL A 1 126 ? 99.22300  94.45200  112.67200 1.000 32.15040  ? 133 VAL A CA  1 
ATOM   936  C C   . VAL A 1 126 ? 100.74700 94.56900  112.57200 1.000 42.80322  ? 133 VAL A C   1 
ATOM   937  O O   . VAL A 1 126 ? 101.43600 94.68800  113.59400 1.000 52.23591  ? 133 VAL A O   1 
ATOM   938  C CB  . VAL A 1 126 ? 98.77500  92.98400  112.70200 1.000 36.11456  ? 133 VAL A CB  1 
ATOM   939  C CG1 . VAL A 1 126 ? 99.43100  92.27000  113.85700 1.000 41.14059  ? 133 VAL A CG1 1 
ATOM   940  C CG2 . VAL A 1 126 ? 97.27400  92.90000  112.82300 1.000 38.67246  ? 133 VAL A CG2 1 
ATOM   941  N N   . GLY A 1 127 ? 101.30100 94.57200  111.35800 1.000 42.16556  ? 134 GLY A N   1 
ATOM   942  C CA  . GLY A 1 127 ? 102.74300 94.68500  111.19400 1.000 35.61601  ? 134 GLY A CA  1 
ATOM   943  C C   . GLY A 1 127 ? 103.33300 95.99700  111.67200 1.000 35.57320  ? 134 GLY A C   1 
ATOM   944  O O   . GLY A 1 127 ? 104.37100 96.01200  112.33200 1.000 46.05969  ? 134 GLY A O   1 
ATOM   945  N N   . CYS A 1 128 ? 102.69600 97.11700  111.33400 1.000 30.55775  ? 135 CYS A N   1 
ATOM   946  C CA  . CYS A 1 128 ? 103.21100 98.41400  111.75500 1.000 27.41861  ? 135 CYS A CA  1 
ATOM   947  C C   . CYS A 1 128 ? 103.14600 98.59300  113.26600 1.000 40.86351  ? 135 CYS A C   1 
ATOM   948  O O   . CYS A 1 128 ? 104.05700 99.17700  113.86000 1.000 50.82199  ? 135 CYS A O   1 
ATOM   949  C CB  . CYS A 1 128 ? 102.44500 99.53000  111.05200 1.000 37.71433  ? 135 CYS A CB  1 
ATOM   950  S SG  . CYS A 1 128 ? 102.60400 99.54100  109.25800 1.000 58.13659  ? 135 CYS A SG  1 
ATOM   951  N N   . SER A 1 129 ? 102.06900 98.13800  113.90400 1.000 38.27338  ? 136 SER A N   1 
ATOM   952  C CA  . SER A 1 129 ? 102.01800 98.15900  115.36200 1.000 33.33643  ? 136 SER A CA  1 
ATOM   953  C C   . SER A 1 129 ? 103.10500 97.29200  115.98700 1.000 43.21855  ? 136 SER A C   1 
ATOM   954  O O   . SER A 1 129 ? 103.79900 97.72400  116.92000 1.000 52.09635  ? 136 SER A O   1 
ATOM   955  C CB  . SER A 1 129 ? 100.64800 97.68800  115.82300 1.000 40.90393  ? 136 SER A CB  1 
ATOM   956  O OG  . SER A 1 129 ? 99.65400  98.63100  115.48800 1.000 51.46587  ? 136 SER A OG  1 
ATOM   957  N N   . SER A 1 130 ? 103.29200 96.07700  115.46500 1.000 43.68635  ? 137 SER A N   1 
ATOM   958  C CA  . SER A 1 130 ? 104.35500 95.20100  115.94900 1.000 33.75543  ? 137 SER A CA  1 
ATOM   959  C C   . SER A 1 130 ? 105.73400 95.82800  115.79000 1.000 45.67928  ? 137 SER A C   1 
ATOM   960  O O   . SER A 1 130 ? 106.58800 95.70800  116.67300 1.000 54.39469  ? 137 SER A O   1 
ATOM   961  C CB  . SER A 1 130 ? 104.29000 93.86800  115.21200 1.000 36.24876  ? 137 SER A CB  1 
ATOM   962  O OG  . SER A 1 130 ? 105.18100 92.93300  115.77900 1.000 55.69063  ? 137 SER A OG  1 
ATOM   963  N N   . THR A 1 131 ? 105.95600 96.54700  114.69600 1.000 43.43554  ? 138 THR A N   1 
ATOM   964  C CA  . THR A 1 131 ? 107.23900 97.20400  114.48100 1.000 31.79219  ? 138 THR A CA  1 
ATOM   965  C C   . THR A 1 131 ? 107.43600 98.44800  115.34000 1.000 38.93506  ? 138 THR A C   1 
ATOM   966  O O   . THR A 1 131 ? 108.55800 98.71800  115.77400 1.000 52.20944  ? 138 THR A O   1 
ATOM   967  C CB  . THR A 1 131 ? 107.39100 97.53800  113.00800 1.000 32.59653  ? 138 THR A CB  1 
ATOM   968  O OG1 . THR A 1 131 ? 107.39100 96.31800  112.27200 1.000 47.41658  ? 138 THR A OG1 1 
ATOM   969  C CG2 . THR A 1 131 ? 108.68100 98.22400  112.75700 1.000 38.96395  ? 138 THR A CG2 1 
ATOM   970  N N   . ILE A 1 132 ? 106.40400 99.26200  115.55600 1.000 40.95621  ? 139 ILE A N   1 
ATOM   971  C CA  . ILE A 1 132 ? 106.58900 100.38900 116.46900 1.000 40.70287  ? 139 ILE A CA  1 
ATOM   972  C C   . ILE A 1 132 ? 106.87100 99.89500  117.88200 1.000 51.27232  ? 139 ILE A C   1 
ATOM   973  O O   . ILE A 1 132 ? 107.71300 100.46300 118.59900 1.000 60.70328  ? 139 ILE A O   1 
ATOM   974  C CB  . ILE A 1 132 ? 105.36200 101.31500 116.43000 1.000 42.75451  ? 139 ILE A CB  1 
ATOM   975  C CG1 . ILE A 1 132 ? 105.36000 102.14300 115.15000 1.000 44.71002  ? 139 ILE A CG1 1 
ATOM   976  C CG2 . ILE A 1 132 ? 105.34200 102.22500 117.63100 1.000 52.13058  ? 139 ILE A CG2 1 
ATOM   977  C CD1 . ILE A 1 132 ? 104.03400 102.78800 114.85700 1.000 50.05222  ? 139 ILE A CD1 1 
ATOM   978  N N   . LEU A 1 133 ? 106.29900 98.74800  118.24700 1.000 47.13572  ? 140 LEU A N   1 
ATOM   979  C CA  . LEU A 1 133 ? 106.73500 98.06400  119.46000 1.000 36.85916  ? 140 LEU A CA  1 
ATOM   980  C C   . LEU A 1 133 ? 108.20800 97.68500  119.38400 1.000 44.64591  ? 140 LEU A C   1 
ATOM   981  O O   . LEU A 1 133 ? 108.95500 97.86900  120.35100 1.000 57.82953  ? 140 LEU A O   1 
ATOM   982  C CB  . LEU A 1 133 ? 105.87500 96.83100  119.70700 1.000 40.83749  ? 140 LEU A CB  1 
ATOM   983  C CG  . LEU A 1 133 ? 106.29800 96.03200  120.92800 1.000 43.58888  ? 140 LEU A CG  1 
ATOM   984  C CD1 . LEU A 1 133 ? 106.18800 96.90900  122.13400 1.000 46.32835  ? 140 LEU A CD1 1 
ATOM   985  C CD2 . LEU A 1 133 ? 105.42100 94.82600  121.08900 1.000 47.69195  ? 140 LEU A CD2 1 
ATOM   986  N N   . PHE A 1 134 ? 108.62200 97.07200  118.27600 1.000 45.44404  ? 141 PHE A N   1 
ATOM   987  C CA  . PHE A 1 134 ? 110.01200 96.64900  118.14400 1.000 42.99851  ? 141 PHE A CA  1 
ATOM   988  C C   . PHE A 1 134 ? 110.98600 97.81300  118.28300 1.000 39.74467  ? 141 PHE A C   1 
ATOM   989  O O   . PHE A 1 134 ? 112.01800 97.68100  118.94100 1.000 50.00453  ? 141 PHE A O   1 
ATOM   990  C CB  . PHE A 1 134 ? 110.22600 95.94700  116.80800 1.000 41.92830  ? 141 PHE A CB  1 
ATOM   991  C CG  . PHE A 1 134 ? 111.62000 95.44600  116.61300 1.000 47.41124  ? 141 PHE A CG  1 
ATOM   992  C CD1 . PHE A 1 134 ? 112.04900 94.29900  117.24300 1.000 52.79823  ? 141 PHE A CD1 1 
ATOM   993  C CD2 . PHE A 1 134 ? 112.50400 96.12500  115.80100 1.000 43.84312  ? 141 PHE A CD2 1 
ATOM   994  C CE1 . PHE A 1 134 ? 113.32900 93.83800  117.06400 1.000 47.83639  ? 141 PHE A CE1 1 
ATOM   995  C CE2 . PHE A 1 134 ? 113.78500 95.66800  115.62000 1.000 45.40204  ? 141 PHE A CE2 1 
ATOM   996  C CZ  . PHE A 1 134 ? 114.19900 94.52500  116.25300 1.000 48.21003  ? 141 PHE A CZ  1 
ATOM   997  N N   . PHE A 1 135 ? 110.70000 98.95000  117.65100 1.000 37.71099  ? 142 PHE A N   1 
ATOM   998  C CA  . PHE A 1 135 ? 111.58100 100.10700 117.81000 1.000 46.96111  ? 142 PHE A CA  1 
ATOM   999  C C   . PHE A 1 135 ? 111.54800 100.69600 119.21400 1.000 55.78255  ? 142 PHE A C   1 
ATOM   1000 O O   . PHE A 1 135 ? 112.57000 101.21700 119.67700 1.000 62.74157  ? 142 PHE A O   1 
ATOM   1001 C CB  . PHE A 1 135 ? 111.25600 101.20300 116.79400 1.000 47.62815  ? 142 PHE A CB  1 
ATOM   1002 C CG  . PHE A 1 135 ? 111.33400 100.76300 115.36400 1.000 48.63207  ? 142 PHE A CG  1 
ATOM   1003 C CD1 . PHE A 1 135 ? 112.14700 99.71000  114.99000 1.000 49.73580  ? 142 PHE A CD1 1 
ATOM   1004 C CD2 . PHE A 1 135 ? 110.62300 101.42700 114.38500 1.000 42.61121  ? 142 PHE A CD2 1 
ATOM   1005 C CE1 . PHE A 1 135 ? 112.22800 99.31600  113.67500 1.000 48.46120  ? 142 PHE A CE1 1 
ATOM   1006 C CE2 . PHE A 1 135 ? 110.70400 101.03700 113.07300 1.000 43.10191  ? 142 PHE A CE2 1 
ATOM   1007 C CZ  . PHE A 1 135 ? 111.51100 99.98200  112.71800 1.000 42.89618  ? 142 PHE A CZ  1 
ATOM   1008 N N   . ASN A 1 136 ? 110.45100 100.53000 119.95800 1.000 57.60584  ? 143 ASN A N   1 
ATOM   1009 C CA  . ASN A 1 136 ? 110.49900 101.00800 121.34000 1.000 52.15155  ? 143 ASN A CA  1 
ATOM   1010 C C   . ASN A 1 136 ? 111.26300 100.06400 122.26300 1.000 48.04161  ? 143 ASN A C   1 
ATOM   1011 O O   . ASN A 1 136 ? 112.00000 100.52600 123.14700 1.000 57.75739  ? 143 ASN A O   1 
ATOM   1012 C CB  . ASN A 1 136 ? 109.08700 101.22800 121.87500 1.000 56.37000  ? 143 ASN A CB  1 
ATOM   1013 C CG  . ASN A 1 136 ? 108.40500 102.41500 121.23300 1.000 61.35332  ? 143 ASN A CG  1 
ATOM   1014 O OD1 . ASN A 1 136 ? 109.03800 103.20400 120.53600 1.000 56.65389  ? 143 ASN A OD1 1 
ATOM   1015 N ND2 . ASN A 1 136 ? 107.10700 102.55000 121.46700 1.000 61.49449  ? 143 ASN A ND2 1 
ATOM   1016 N N   . LEU A 1 137 ? 111.18900 98.75900  122.01500 1.000 45.00843  ? 144 LEU A N   1 
ATOM   1017 C CA  . LEU A 1 137 ? 112.04400 97.83200  122.75000 1.000 48.13495  ? 144 LEU A CA  1 
ATOM   1018 C C   . LEU A 1 137 ? 113.50900 98.01300  122.37900 1.000 53.75040  ? 144 LEU A C   1 
ATOM   1019 O O   . LEU A 1 137 ? 114.38600 97.96200  123.24900 1.000 55.12748  ? 144 LEU A O   1 
ATOM   1020 C CB  . LEU A 1 137 ? 111.60500 96.39800  122.48400 1.000 45.03084  ? 144 LEU A CB  1 
ATOM   1021 C CG  . LEU A 1 137 ? 110.21800 96.03300  122.99000 1.000 44.56128  ? 144 LEU A CG  1 
ATOM   1022 C CD1 . LEU A 1 137 ? 109.92800 94.57800  122.72100 1.000 46.29796  ? 144 LEU A CD1 1 
ATOM   1023 C CD2 . LEU A 1 137 ? 110.13800 96.32500  124.46600 1.000 53.70287  ? 144 LEU A CD2 1 
ATOM   1024 N N   . PHE A 1 138 ? 113.79500 98.21500  121.09500 1.000 58.48410  ? 145 PHE A N   1 
ATOM   1025 C CA  . PHE A 1 138 ? 115.15400 98.52100  120.67100 1.000 56.08905  ? 145 PHE A CA  1 
ATOM   1026 C C   . PHE A 1 138 ? 115.70200 99.73700  121.40100 1.000 59.93009  ? 145 PHE A C   1 
ATOM   1027 O O   . PHE A 1 138 ? 116.82500 99.70800  121.90700 1.000 62.14488  ? 145 PHE A O   1 
ATOM   1028 C CB  . PHE A 1 138 ? 115.21100 98.74900  119.16500 1.000 52.60738  ? 145 PHE A CB  1 
ATOM   1029 C CG  . PHE A 1 138 ? 116.55600 99.20000  118.68300 1.000 53.71647  ? 145 PHE A CG  1 
ATOM   1030 C CD1 . PHE A 1 138 ? 117.52600 98.27900  118.35500 1.000 60.33149  ? 145 PHE A CD1 1 
ATOM   1031 C CD2 . PHE A 1 138 ? 116.85600 100.54300 118.57300 1.000 57.57175  ? 145 PHE A CD2 1 
ATOM   1032 C CE1 . PHE A 1 138 ? 118.76400 98.68800  117.91800 1.000 63.56092  ? 145 PHE A CE1 1 
ATOM   1033 C CE2 . PHE A 1 138 ? 118.09300 100.95500 118.14200 1.000 60.34602  ? 145 PHE A CE2 1 
ATOM   1034 C CZ  . PHE A 1 138 ? 119.04700 100.02800 117.81300 1.000 59.46093  ? 145 PHE A CZ  1 
ATOM   1035 N N   . LEU A 1 139 ? 114.95200 100.84100 121.40000 1.000 61.61630  ? 146 LEU A N   1 
ATOM   1036 C CA  . LEU A 1 139 ? 115.41800 102.04400 122.08200 1.000 56.71175  ? 146 LEU A CA  1 
ATOM   1037 C C   . LEU A 1 139 ? 115.65800 101.81400 123.57100 1.000 60.06476  ? 146 LEU A C   1 
ATOM   1038 O O   . LEU A 1 139 ? 116.66100 102.28700 124.11600 1.000 64.99404  ? 146 LEU A O   1 
ATOM   1039 C CB  . LEU A 1 139 ? 114.42000 103.17900 121.87100 1.000 56.10840  ? 146 LEU A CB  1 
ATOM   1040 C CG  . LEU A 1 139 ? 114.76800 104.50200 122.54600 1.000 57.19383  ? 146 LEU A CG  1 
ATOM   1041 C CD1 . LEU A 1 139 ? 116.10400 105.00800 122.05800 1.000 60.04448  ? 146 LEU A CD1 1 
ATOM   1042 C CD2 . LEU A 1 139 ? 113.68300 105.52500 122.28300 1.000 59.24149  ? 146 LEU A CD2 1 
ATOM   1043 N N   . GLU A 1 140 ? 114.74700 101.11600 124.25700 1.000 65.92665  ? 147 GLU A N   1 
ATOM   1044 C CA  . GLU A 1 140 ? 114.98200 100.81700 125.67200 1.000 62.23393  ? 147 GLU A CA  1 
ATOM   1045 C C   . GLU A 1 140 ? 116.23300 99.96600  125.89500 1.000 65.76738  ? 147 GLU A C   1 
ATOM   1046 O O   . GLU A 1 140 ? 117.01800 100.23300 126.81800 1.000 66.36983  ? 147 GLU A O   1 
ATOM   1047 C CB  . GLU A 1 140 ? 113.75900 100.12500 126.27000 1.000 58.99034  ? 147 GLU A CB  1 
ATOM   1048 N N   . ARG A 1 141 ? 116.50400 99.01800  124.99500 1.000 70.23976  ? 148 ARG A N   1 
ATOM   1049 C CA  . ARG A 1 141 ? 117.74400 98.24600  125.08500 1.000 71.89782  ? 148 ARG A CA  1 
ATOM   1050 C C   . ARG A 1 141 ? 118.97500 99.09700  124.81600 1.000 74.92970  ? 148 ARG A C   1 
ATOM   1051 O O   . ARG A 1 141 ? 120.00400 98.93400  125.48000 1.000 75.63234  ? 148 ARG A O   1 
ATOM   1052 C CB  . ARG A 1 141 ? 117.70000 97.06300  124.12000 1.000 69.19318  ? 148 ARG A CB  1 
ATOM   1053 C CG  . ARG A 1 141 ? 116.67100 95.98800  124.44400 1.000 69.68751  ? 148 ARG A CG  1 
ATOM   1054 C CD  . ARG A 1 141 ? 116.94600 95.29000  125.76800 1.000 71.07505  ? 148 ARG A CD  1 
ATOM   1055 N NE  . ARG A 1 141 ? 116.49000 96.04400  126.92800 1.000 73.16107  ? 148 ARG A NE  1 
ATOM   1056 C CZ  . ARG A 1 141 ? 116.93400 95.85200  128.16200 1.000 71.41269  ? 148 ARG A CZ  1 
ATOM   1057 N NH1 . ARG A 1 141 ? 117.85500 94.94200  128.43000 1.000 72.00890  ? 148 ARG A NH1 1 
ATOM   1058 N NH2 . ARG A 1 141 ? 116.44400 96.59300  129.15100 1.000 70.38194  ? 148 ARG A NH2 1 
ATOM   1059 N N   . LEU A 1 142 ? 118.91000 99.97800  123.82600 1.000 74.75044  ? 149 LEU A N   1 
ATOM   1060 C CA  . LEU A 1 142 ? 120.05400 100.82500 123.51600 1.000 69.90724  ? 149 LEU A CA  1 
ATOM   1061 C C   . LEU A 1 142 ? 120.37100 101.77500 124.66300 1.000 72.48630  ? 149 LEU A C   1 
ATOM   1062 O O   . LEU A 1 142 ? 121.54300 101.98900 124.99500 1.000 74.27850  ? 149 LEU A O   1 
ATOM   1063 C CB  . LEU A 1 142 ? 119.78900 101.59800 122.22900 1.000 65.89134  ? 149 LEU A CB  1 
ATOM   1064 C CG  . LEU A 1 142 ? 120.90600 102.51600 121.76100 1.000 71.12074  ? 149 LEU A CG  1 
ATOM   1065 C CD1 . LEU A 1 142 ? 122.17000 101.71800 121.57300 1.000 74.60796  ? 149 LEU A CD1 1 
ATOM   1066 C CD2 . LEU A 1 142 ? 120.49800 103.16800 120.46700 1.000 69.67268  ? 149 LEU A CD2 1 
ATOM   1067 N N   . ILE A 1 143 ? 119.34200 102.37100 125.27000 1.000 75.49840  ? 150 ILE A N   1 
ATOM   1068 C CA  . ILE A 1 143 ? 119.55600 103.19500 126.45800 1.000 71.18575  ? 150 ILE A CA  1 
ATOM   1069 C C   . ILE A 1 143 ? 120.17700 102.38300 127.58700 1.000 75.04335  ? 150 ILE A C   1 
ATOM   1070 O O   . ILE A 1 143 ? 121.08400 102.85700 128.28000 1.000 80.81635  ? 150 ILE A O   1 
ATOM   1071 C CB  . ILE A 1 143 ? 118.23500 103.84900 126.90200 1.000 73.07315  ? 150 ILE A CB  1 
ATOM   1072 C CG1 . ILE A 1 143 ? 117.70000 104.77700 125.81700 1.000 73.71499  ? 150 ILE A CG1 1 
ATOM   1073 C CG2 . ILE A 1 143 ? 118.43700 104.62400 128.18500 1.000 74.34377  ? 150 ILE A CG2 1 
ATOM   1074 C CD1 . ILE A 1 143 ? 118.58900 105.94500 125.53300 1.000 74.94440  ? 150 ILE A CD1 1 
ATOM   1075 N N   . THR A 1 144 ? 119.72300 101.14000 127.78000 1.000 79.25182  ? 151 THR A N   1 
ATOM   1076 C CA  . THR A 1 144 ? 120.31600 100.31000 128.82800 1.000 81.01620  ? 151 THR A CA  1 
ATOM   1077 C C   . THR A 1 144 ? 121.78100 99.98400  128.54800 1.000 81.53470  ? 151 THR A C   1 
ATOM   1078 O O   . THR A 1 144 ? 122.61600 100.00900 129.46000 1.000 80.04065  ? 151 THR A O   1 
ATOM   1079 C CB  . THR A 1 144 ? 119.51200 99.02300  128.99500 1.000 81.24684  ? 151 THR A CB  1 
ATOM   1080 O OG1 . THR A 1 144 ? 118.16100 99.34600  129.34500 1.000 82.36733  ? 151 THR A OG1 1 
ATOM   1081 C CG2 . THR A 1 144 ? 120.11500 98.15900  130.08400 1.000 80.80389  ? 151 THR A CG2 1 
ATOM   1082 N N   . ILE A 1 145 ? 122.11600 99.70100  127.29000 1.000 86.38557  ? 152 ILE A N   1 
ATOM   1083 C CA  . ILE A 1 145 ? 123.50500 99.43900  126.91800 1.000 86.09741  ? 152 ILE A CA  1 
ATOM   1084 C C   . ILE A 1 145 ? 124.38200 100.67100 127.11500 1.000 84.61270  ? 152 ILE A C   1 
ATOM   1085 O O   . ILE A 1 145 ? 125.50300 100.57000 127.62600 1.000 85.52824  ? 152 ILE A O   1 
ATOM   1086 C CB  . ILE A 1 145 ? 123.57900 98.92200  125.47100 1.000 85.44189  ? 152 ILE A CB  1 
ATOM   1087 C CG1 . ILE A 1 145 ? 123.00800 97.51000  125.38100 1.000 84.38963  ? 152 ILE A CG1 1 
ATOM   1088 C CG2 . ILE A 1 145 ? 125.00700 98.93500  124.97300 1.000 86.11556  ? 152 ILE A CG2 1 
ATOM   1089 C CD1 . ILE A 1 145 ? 122.65600 97.09500  123.98000 1.000 84.79239  ? 152 ILE A CD1 1 
ATOM   1090 N N   . ILE A 1 146 ? 123.90600 101.84600 126.69700 1.000 87.61368  ? 153 ILE A N   1 
ATOM   1091 C CA  . ILE A 1 146 ? 124.67600 103.07100 126.90600 1.000 89.16965  ? 153 ILE A CA  1 
ATOM   1092 C C   . ILE A 1 146 ? 124.86900 103.35500 128.39100 1.000 89.28251  ? 153 ILE A C   1 
ATOM   1093 O O   . ILE A 1 146 ? 125.95300 103.76800 128.81900 1.000 89.62530  ? 153 ILE A O   1 
ATOM   1094 C CB  . ILE A 1 146 ? 124.01000 104.25800 126.18600 1.000 86.98994  ? 153 ILE A CB  1 
ATOM   1095 C CG1 . ILE A 1 146 ? 123.99800 104.03000 124.67700 1.000 87.56748  ? 153 ILE A CG1 1 
ATOM   1096 C CG2 . ILE A 1 146 ? 124.72700 105.55100 126.51100 1.000 85.53042  ? 153 ILE A CG2 1 
ATOM   1097 C CD1 . ILE A 1 146 ? 123.04100 104.92600 123.93700 1.000 85.29660  ? 153 ILE A CD1 1 
ATOM   1098 N N   . ALA A 1 147 ? 123.83600 103.12900 129.20300 1.000 98.85444  ? 154 ALA A N   1 
ATOM   1099 C CA  . ALA A 1 147 ? 123.98100 103.29900 130.64600 1.000 100.08282 ? 154 ALA A CA  1 
ATOM   1100 C C   . ALA A 1 147 ? 125.00600 102.33700 131.23500 1.000 99.69914  ? 154 ALA A C   1 
ATOM   1101 O O   . ALA A 1 147 ? 125.84200 102.73600 132.05600 1.000 101.22993 ? 154 ALA A O   1 
ATOM   1102 C CB  . ALA A 1 147 ? 122.62800 103.12100 131.33300 1.000 100.30404 ? 154 ALA A CB  1 
ATOM   1103 N N   . TYR A 1 148 ? 124.97100 101.07100 130.81700 1.000 102.68975 ? 155 TYR A N   1 
ATOM   1104 C CA  . TYR A 1 148 ? 125.95700 100.10200 131.28900 1.000 104.76200 ? 155 TYR A CA  1 
ATOM   1105 C C   . TYR A 1 148 ? 127.37500 100.49300 130.88900 1.000 106.39287 ? 155 TYR A C   1 
ATOM   1106 O O   . TYR A 1 148 ? 128.30100 100.42000 131.70200 1.000 107.68482 ? 155 TYR A O   1 
ATOM   1107 C CB  . TYR A 1 148 ? 125.61700 98.71000  130.75600 1.000 107.03365 ? 155 TYR A CB  1 
ATOM   1108 C CG  . TYR A 1 148 ? 126.66900 97.66700  131.05500 1.000 107.83831 ? 155 TYR A CG  1 
ATOM   1109 C CD1 . TYR A 1 148 ? 126.71200 97.03200  132.28800 1.000 106.49965 ? 155 TYR A CD1 1 
ATOM   1110 C CD2 . TYR A 1 148 ? 127.61800 97.31600  130.10400 1.000 106.45932 ? 155 TYR A CD2 1 
ATOM   1111 C CE1 . TYR A 1 148 ? 127.67000 96.07700  132.56500 1.000 106.77401 ? 155 TYR A CE1 1 
ATOM   1112 C CE2 . TYR A 1 148 ? 128.58000 96.36400  130.37300 1.000 106.16197 ? 155 TYR A CE2 1 
ATOM   1113 C CZ  . TYR A 1 148 ? 128.60200 95.74800  131.60400 1.000 107.91488 ? 155 TYR A CZ  1 
ATOM   1114 O OH  . TYR A 1 148 ? 129.56000 94.79900  131.87500 1.000 109.16649 ? 155 TYR A OH  1 
ATOM   1115 N N   . ILE A 1 149 ? 127.57000 100.88400 129.63100 1.000 107.39299 ? 156 ILE A N   1 
ATOM   1116 C CA  . ILE A 1 149 ? 128.89800 101.28600 129.17400 1.000 107.60664 ? 156 ILE A CA  1 
ATOM   1117 C C   . ILE A 1 149 ? 129.39100 102.51800 129.92700 1.000 109.55535 ? 156 ILE A C   1 
ATOM   1118 O O   . ILE A 1 149 ? 130.55900 102.58900 130.32500 1.000 109.46241 ? 156 ILE A O   1 
ATOM   1119 C CB  . ILE A 1 149 ? 128.89200 101.51600 127.65200 1.000 107.53821 ? 156 ILE A CB  1 
ATOM   1120 C CG1 . ILE A 1 149 ? 128.77400 100.18100 126.91800 1.000 106.47466 ? 156 ILE A CG1 1 
ATOM   1121 C CG2 . ILE A 1 149 ? 130.14600 102.25100 127.21600 1.000 107.70399 ? 156 ILE A CG2 1 
ATOM   1122 C CD1 . ILE A 1 149 ? 128.54400 100.32200 125.43200 1.000 107.16947 ? 156 ILE A CD1 1 
ATOM   1123 N N   . MET A 1 150 ? 128.52700 103.51900 130.10700 1.000 117.41790 ? 157 MET A N   1 
ATOM   1124 C CA  . MET A 1 150 ? 128.91600 104.71200 130.85400 1.000 117.13884 ? 157 MET A CA  1 
ATOM   1125 C C   . MET A 1 150 ? 129.26400 104.39400 132.30500 1.000 118.93436 ? 157 MET A C   1 
ATOM   1126 O O   . MET A 1 150 ? 130.21000 104.96300 132.86000 1.000 118.96953 ? 157 MET A O   1 
ATOM   1127 C CB  . MET A 1 150 ? 127.80200 105.75700 130.78800 1.000 114.02821 ? 157 MET A CB  1 
ATOM   1128 N N   . LYS A 1 151 ? 128.52200 103.48000 132.93600 1.000 121.52173 ? 158 LYS A N   1 
ATOM   1129 C CA  . LYS A 1 151 ? 128.87600 103.04300 134.28600 1.000 120.68876 ? 158 LYS A CA  1 
ATOM   1130 C C   . LYS A 1 151 ? 130.19800 102.28200 134.32100 1.000 122.38906 ? 158 LYS A C   1 
ATOM   1131 O O   . LYS A 1 151 ? 130.98400 102.43900 135.26200 1.000 123.15635 ? 158 LYS A O   1 
ATOM   1132 C CB  . LYS A 1 151 ? 127.75400 102.18400 134.86800 1.000 119.93424 ? 158 LYS A CB  1 
ATOM   1133 N N   . SER A 1 152 ? 130.46100 101.44900 133.31400 1.000 126.36261 ? 159 SER A N   1 
ATOM   1134 C CA  . SER A 1 152 ? 131.75100 100.77000 133.22600 1.000 127.15575 ? 159 SER A CA  1 
ATOM   1135 C C   . SER A 1 152 ? 132.90100 101.75300 133.03400 1.000 128.16127 ? 159 SER A C   1 
ATOM   1136 O O   . SER A 1 152 ? 133.98800 101.56300 133.59200 1.000 128.09734 ? 159 SER A O   1 
ATOM   1137 C CB  . SER A 1 152 ? 131.72900 99.75000  132.08800 1.000 125.81517 ? 159 SER A CB  1 
ATOM   1138 N N   . CYS A 1 153 ? 132.68000 102.80900 132.25100 1.000 131.83749 ? 160 CYS A N   1 
ATOM   1139 C CA  . CYS A 1 153 ? 133.67400 103.87300 132.12900 1.000 131.80212 ? 160 CYS A CA  1 
ATOM   1140 C C   . CYS A 1 153 ? 133.86400 104.62600 133.44100 1.000 132.42546 ? 160 CYS A C   1 
ATOM   1141 O O   . CYS A 1 153 ? 134.99400 104.97600 133.80100 1.000 132.18402 ? 160 CYS A O   1 
ATOM   1142 C CB  . CYS A 1 153 ? 133.27400 104.83700 131.01100 1.000 130.38609 ? 160 CYS A CB  1 
ATOM   1143 N N   . HIS A 1 154 ? 132.77400 104.89600 134.16100 1.000 136.11540 ? 161 HIS A N   1 
ATOM   1144 C CA  . HIS A 1 154 ? 132.89400 105.52100 135.47500 1.000 136.95859 ? 161 HIS A CA  1 
ATOM   1145 C C   . HIS A 1 154 ? 133.70300 104.64900 136.42700 1.000 138.32189 ? 161 HIS A C   1 
ATOM   1146 O O   . HIS A 1 154 ? 134.50100 105.15800 137.22200 1.000 137.73142 ? 161 HIS A O   1 
ATOM   1147 C CB  . HIS A 1 154 ? 131.50700 105.80400 136.05200 1.000 135.88424 ? 161 HIS A CB  1 
ATOM   1148 N N   . GLN A 1 155 ? 133.50700 103.33100 136.36100 1.000 139.52862 ? 162 GLN A N   1 
ATOM   1149 C CA  . GLN A 1 155 ? 134.34500 102.41900 137.13200 1.000 138.45446 ? 162 GLN A CA  1 
ATOM   1150 C C   . GLN A 1 155 ? 135.75600 102.34900 136.56000 1.000 139.45896 ? 162 GLN A C   1 
ATOM   1151 O O   . GLN A 1 155 ? 136.73400 102.27500 137.31400 1.000 138.97927 ? 162 GLN A O   1 
ATOM   1152 C CB  . GLN A 1 155 ? 133.71100 101.02900 137.17300 1.000 137.36549 ? 162 GLN A CB  1 
ATOM   1153 N N   . ARG A 1 156 ? 135.88200 102.35800 135.23100 1.000 144.36647 ? 163 ARG A N   1 
ATOM   1154 C CA  . ARG A 1 156 ? 137.20000 102.37200 134.60300 1.000 144.51996 ? 163 ARG A CA  1 
ATOM   1155 C C   . ARG A 1 156 ? 137.98400 103.64000 134.91500 1.000 144.63671 ? 163 ARG A C   1 
ATOM   1156 O O   . ARG A 1 156 ? 139.21400 103.63600 134.80400 1.000 144.03235 ? 163 ARG A O   1 
ATOM   1157 C CB  . ARG A 1 156 ? 137.06400 102.21000 133.08800 1.000 143.50922 ? 163 ARG A CB  1 
ATOM   1158 N N   . GLN A 1 157 ? 137.30500 104.72300 135.29900 1.000 144.84348 ? 164 GLN A N   1 
ATOM   1159 C CA  . GLN A 1 157 ? 137.99500 105.92800 135.74300 1.000 144.59777 ? 164 GLN A CA  1 
ATOM   1160 C C   . GLN A 1 157 ? 138.66500 105.76900 137.10300 1.000 145.23776 ? 164 GLN A C   1 
ATOM   1161 O O   . GLN A 1 157 ? 139.45800 106.63800 137.48300 1.000 145.31561 ? 164 GLN A O   1 
ATOM   1162 C CB  . GLN A 1 157 ? 137.01600 107.10300 135.78700 1.000 143.65480 ? 164 GLN A CB  1 
ATOM   1163 N N   . LEU A 1 158 ? 138.36900 104.70200 137.83900 1.000 145.20733 ? 165 LEU A N   1 
ATOM   1164 C CA  . LEU A 1 158 ? 138.95600 104.49700 139.16000 1.000 144.61605 ? 165 LEU A CA  1 
ATOM   1165 C C   . LEU A 1 158 ? 140.46600 104.30000 139.07100 1.000 144.64487 ? 165 LEU A C   1 
ATOM   1166 O O   . LEU A 1 158 ? 140.95100 103.17000 139.00700 1.000 144.25839 ? 165 LEU A O   1 
ATOM   1167 C CB  . LEU A 1 158 ? 138.31100 103.29700 139.85600 1.000 144.19734 ? 165 LEU A CB  1 
ATOM   1168 N N   . TRP A 1 183 ? 123.45500 105.97800 137.33000 1.000 132.96148 ? 190 TRP A N   1 
ATOM   1169 C CA  . TRP A 1 183 ? 122.27200 106.63500 136.78700 1.000 133.97066 ? 190 TRP A CA  1 
ATOM   1170 C C   . TRP A 1 183 ? 122.22600 106.51100 135.26900 1.000 134.92370 ? 190 TRP A C   1 
ATOM   1171 O O   . TRP A 1 183 ? 123.23400 106.21100 134.63000 1.000 134.04350 ? 190 TRP A O   1 
ATOM   1172 C CB  . TRP A 1 183 ? 122.24300 108.10900 137.19500 1.000 132.55576 ? 190 TRP A CB  1 
ATOM   1173 N N   . LYS A 1 184 ? 121.04600 106.74300 134.70000 1.000 133.88162 ? 191 LYS A N   1 
ATOM   1174 C CA  . LYS A 1 184 ? 120.87700 106.69400 133.26000 1.000 132.88715 ? 191 LYS A CA  1 
ATOM   1175 C C   . LYS A 1 184 ? 121.59300 107.87100 132.59600 1.000 132.95717 ? 191 LYS A C   1 
ATOM   1176 O O   . LYS A 1 184 ? 121.86700 108.88700 133.23900 1.000 133.14415 ? 191 LYS A O   1 
ATOM   1177 C CB  . LYS A 1 184 ? 119.39000 106.70900 132.91200 1.000 131.24575 ? 191 LYS A CB  1 
ATOM   1178 N N   . PRO A 1 185 ? 121.91100 107.75700 131.30700 1.000 122.46971 ? 192 PRO A N   1 
ATOM   1179 C CA  . PRO A 1 185 ? 122.56700 108.86900 130.61500 1.000 121.45519 ? 192 PRO A CA  1 
ATOM   1180 C C   . PRO A 1 185 ? 121.61400 110.03300 130.39800 1.000 121.38165 ? 192 PRO A C   1 
ATOM   1181 O O   . PRO A 1 185 ? 120.39900 109.85800 130.27700 1.000 121.93406 ? 192 PRO A O   1 
ATOM   1182 C CB  . PRO A 1 185 ? 123.00200 108.24400 129.28700 1.000 122.00032 ? 192 PRO A CB  1 
ATOM   1183 C CG  . PRO A 1 185 ? 121.97700 107.20400 129.03800 1.000 120.39136 ? 192 PRO A CG  1 
ATOM   1184 C CD  . PRO A 1 185 ? 121.68200 106.62000 130.39800 1.000 120.94777 ? 192 PRO A CD  1 
ATOM   1185 N N   . SER A 1 186 ? 122.18100 111.23500 130.34300 1.000 108.95068 ? 193 SER A N   1 
ATOM   1186 C CA  . SER A 1 186 ? 121.39300 112.40200 129.98100 1.000 108.78821 ? 193 SER A CA  1 
ATOM   1187 C C   . SER A 1 186 ? 121.09100 112.41100 128.48700 1.000 107.50359 ? 193 SER A C   1 
ATOM   1188 O O   . SER A 1 186 ? 121.86300 111.90800 127.66800 1.000 106.94924 ? 193 SER A O   1 
ATOM   1189 C CB  . SER A 1 186 ? 122.12300 113.68400 130.37200 1.000 108.13039 ? 193 SER A CB  1 
ATOM   1190 O OG  . SER A 1 186 ? 123.29300 113.85700 129.59600 1.000 107.58074 ? 193 SER A OG  1 
ATOM   1191 N N   . VAL A 1 187 ? 119.94500 113.00300 128.14200 1.000 97.60783  ? 194 VAL A N   1 
ATOM   1192 C CA  . VAL A 1 187 ? 119.39400 112.89200 126.79400 1.000 95.62684  ? 194 VAL A CA  1 
ATOM   1193 C C   . VAL A 1 187 ? 120.31500 113.50700 125.75200 1.000 95.54993  ? 194 VAL A C   1 
ATOM   1194 O O   . VAL A 1 187 ? 120.38800 113.02400 124.61800 1.000 100.30849 ? 194 VAL A O   1 
ATOM   1195 C CB  . VAL A 1 187 ? 117.99200 113.52500 126.74200 1.000 94.41502  ? 194 VAL A CB  1 
ATOM   1196 C CG1 . VAL A 1 187 ? 117.36300 113.29400 125.38800 1.000 89.92573  ? 194 VAL A CG1 1 
ATOM   1197 C CG2 . VAL A 1 187 ? 117.11500 112.94600 127.83400 1.000 96.82175  ? 194 VAL A CG2 1 
ATOM   1198 N N   . TYR A 1 188 ? 121.02000 114.58300 126.10300 1.000 100.18125 ? 195 TYR A N   1 
ATOM   1199 C CA  . TYR A 1 188 ? 121.92600 115.22300 125.15300 1.000 102.23006 ? 195 TYR A CA  1 
ATOM   1200 C C   . TYR A 1 188 ? 123.05100 114.29100 124.70500 1.000 102.22152 ? 195 TYR A C   1 
ATOM   1201 O O   . TYR A 1 188 ? 123.37300 114.22300 123.51100 1.000 106.19921 ? 195 TYR A O   1 
ATOM   1202 C CB  . TYR A 1 188 ? 122.48500 116.50300 125.77100 1.000 102.36440 ? 195 TYR A CB  1 
ATOM   1203 C CG  . TYR A 1 188 ? 123.39700 117.28800 124.86500 1.000 104.10051 ? 195 TYR A CG  1 
ATOM   1204 C CD1 . TYR A 1 188 ? 122.88500 118.02300 123.80700 1.000 102.05198 ? 195 TYR A CD1 1 
ATOM   1205 C CD2 . TYR A 1 188 ? 124.76600 117.32600 125.08800 1.000 104.12158 ? 195 TYR A CD2 1 
ATOM   1206 C CE1 . TYR A 1 188 ? 123.71200 118.75300 122.97800 1.000 104.31373 ? 195 TYR A CE1 1 
ATOM   1207 C CE2 . TYR A 1 188 ? 125.60200 118.05800 124.26900 1.000 104.22085 ? 195 TYR A CE2 1 
ATOM   1208 C CZ  . TYR A 1 188 ? 125.07000 118.76800 123.21400 1.000 105.65081 ? 195 TYR A CZ  1 
ATOM   1209 O OH  . TYR A 1 188 ? 125.89900 119.49900 122.39300 1.000 102.58959 ? 195 TYR A OH  1 
ATOM   1210 N N   . TYR A 1 189 ? 123.65700 113.55500 125.63600 1.000 98.03598  ? 196 TYR A N   1 
ATOM   1211 C CA  . TYR A 1 189 ? 124.70200 112.61700 125.23800 1.000 98.96744  ? 196 TYR A CA  1 
ATOM   1212 C C   . TYR A 1 189 ? 124.15100 111.41500 124.48100 1.000 99.59844  ? 196 TYR A C   1 
ATOM   1213 O O   . TYR A 1 189 ? 124.82900 110.88700 123.59300 1.000 102.29538 ? 196 TYR A O   1 
ATOM   1214 C CB  . TYR A 1 189 ? 125.49800 112.16100 126.45700 1.000 102.60444 ? 196 TYR A CB  1 
ATOM   1215 C CG  . TYR A 1 189 ? 126.28600 113.27400 127.10700 1.000 104.81455 ? 196 TYR A CG  1 
ATOM   1216 C CD1 . TYR A 1 189 ? 127.20900 114.01000 126.37800 1.000 104.68335 ? 196 TYR A CD1 1 
ATOM   1217 C CD2 . TYR A 1 189 ? 126.11200 113.58800 128.44700 1.000 103.36752 ? 196 TYR A CD2 1 
ATOM   1218 C CE1 . TYR A 1 189 ? 127.93200 115.02900 126.96300 1.000 103.01638 ? 196 TYR A CE1 1 
ATOM   1219 C CE2 . TYR A 1 189 ? 126.83100 114.60600 129.04100 1.000 103.34837 ? 196 TYR A CE2 1 
ATOM   1220 C CZ  . TYR A 1 189 ? 127.74000 115.32300 128.29400 1.000 104.31949 ? 196 TYR A CZ  1 
ATOM   1221 O OH  . TYR A 1 189 ? 128.46200 116.33600 128.88200 1.000 105.91822 ? 196 TYR A OH  1 
ATOM   1222 N N   . VAL A 1 190 ? 122.92100 110.99100 124.77300 1.000 81.39768  ? 197 VAL A N   1 
ATOM   1223 C CA  . VAL A 1 190 ? 122.30000 109.96500 123.94100 1.000 79.46397  ? 197 VAL A CA  1 
ATOM   1224 C C   . VAL A 1 190 ? 122.08300 110.47900 122.52500 1.000 80.60201  ? 197 VAL A C   1 
ATOM   1225 O O   . VAL A 1 190 ? 122.27800 109.74800 121.54800 1.000 85.64405  ? 197 VAL A O   1 
ATOM   1226 C CB  . VAL A 1 190 ? 120.98500 109.48100 124.57300 1.000 80.10798  ? 197 VAL A CB  1 
ATOM   1227 C CG1 . VAL A 1 190 ? 120.29700 108.49200 123.65700 1.000 79.63318  ? 197 VAL A CG1 1 
ATOM   1228 C CG2 . VAL A 1 190 ? 121.25800 108.84800 125.91500 1.000 82.42431  ? 197 VAL A CG2 1 
ATOM   1229 N N   . MET A 1 191 ? 121.66000 111.73400 122.38700 1.000 79.85113  ? 198 MET A N   1 
ATOM   1230 C CA  . MET A 1 191 ? 121.49900 112.30600 121.05600 1.000 77.07940  ? 198 MET A CA  1 
ATOM   1231 C C   . MET A 1 191 ? 122.82300 112.36000 120.31000 1.000 79.73389  ? 198 MET A C   1 
ATOM   1232 O O   . MET A 1 191 ? 122.88300 112.05100 119.11700 1.000 84.31086  ? 198 MET A O   1 
ATOM   1233 C CB  . MET A 1 191 ? 120.89000 113.70100 121.13800 1.000 76.65951  ? 198 MET A CB  1 
ATOM   1234 C CG  . MET A 1 191 ? 120.57000 114.28100 119.77900 1.000 79.87391  ? 198 MET A CG  1 
ATOM   1235 S SD  . MET A 1 191 ? 120.13600 116.02100 119.83900 1.000 91.69908  ? 198 MET A SD  1 
ATOM   1236 C CE  . MET A 1 191 ? 121.70200 116.73100 120.32500 1.000 83.56439  ? 198 MET A CE  1 
ATOM   1237 N N   . LEU A 1 192 ? 123.89700 112.75700 120.99400 1.000 79.29775  ? 199 LEU A N   1 
ATOM   1238 C CA  . LEU A 1 192 ? 125.20200 112.79300 120.33800 1.000 78.61666  ? 199 LEU A CA  1 
ATOM   1239 C C   . LEU A 1 192 ? 125.71800 111.40600 119.97300 1.000 82.32172  ? 199 LEU A C   1 
ATOM   1240 O O   . LEU A 1 192 ? 126.44000 111.26300 118.98300 1.000 85.62694  ? 199 LEU A O   1 
ATOM   1241 C CB  . LEU A 1 192 ? 126.22400 113.50600 121.21800 1.000 81.33779  ? 199 LEU A CB  1 
ATOM   1242 C CG  . LEU A 1 192 ? 125.94200 114.97400 121.51900 1.000 86.78859  ? 199 LEU A CG  1 
ATOM   1243 C CD1 . LEU A 1 192 ? 127.07600 115.56000 122.33800 1.000 86.86167  ? 199 LEU A CD1 1 
ATOM   1244 C CD2 . LEU A 1 192 ? 125.73900 115.75500 120.23500 1.000 85.09703  ? 199 LEU A CD2 1 
ATOM   1245 N N   . ILE A 1 193 ? 125.38900 110.38300 120.76000 1.000 75.55354  ? 200 ILE A N   1 
ATOM   1246 C CA  . ILE A 1 193 ? 125.72100 109.01300 120.37000 1.000 71.94353  ? 200 ILE A CA  1 
ATOM   1247 C C   . ILE A 1 193 ? 124.92600 108.57400 119.14400 1.000 68.55412  ? 200 ILE A C   1 
ATOM   1248 O O   . ILE A 1 193 ? 125.48900 108.04700 118.18000 1.000 71.95735  ? 200 ILE A O   1 
ATOM   1249 C CB  . ILE A 1 193 ? 125.51400 108.05100 121.55000 1.000 71.18280  ? 200 ILE A CB  1 
ATOM   1250 C CG1 . ILE A 1 193 ? 126.58500 108.29500 122.61000 1.000 73.43448  ? 200 ILE A CG1 1 
ATOM   1251 C CG2 . ILE A 1 193 ? 125.54500 106.61800 121.07500 1.000 72.20029  ? 200 ILE A CG2 1 
ATOM   1252 C CD1 . ILE A 1 193 ? 126.25600 107.70800 123.95100 1.000 74.34687  ? 200 ILE A CD1 1 
ATOM   1253 N N   . LEU A 1 194 ? 123.61000 108.78400 119.15800 1.000 58.01443  ? 201 LEU A N   1 
ATOM   1254 C CA  . LEU A 1 194 ? 122.77400 108.37400 118.03100 1.000 59.38507  ? 201 LEU A CA  1 
ATOM   1255 C C   . LEU A 1 194 ? 123.06700 109.13900 116.74300 1.000 67.24263  ? 201 LEU A C   1 
ATOM   1256 O O   . LEU A 1 194 ? 122.90900 108.57800 115.65400 1.000 71.71221  ? 201 LEU A O   1 
ATOM   1257 C CB  . LEU A 1 194 ? 121.30100 108.50800 118.40100 1.000 61.03167  ? 201 LEU A CB  1 
ATOM   1258 C CG  . LEU A 1 194 ? 120.79300 107.38200 119.29300 1.000 61.56292  ? 201 LEU A CG  1 
ATOM   1259 C CD1 . LEU A 1 194 ? 119.43300 107.70800 119.85600 1.000 67.65782  ? 201 LEU A CD1 1 
ATOM   1260 C CD2 . LEU A 1 194 ? 120.73200 106.11200 118.49400 1.000 58.99805  ? 201 LEU A CD2 1 
ATOM   1261 N N   . CYS A 1 195 ? 123.47900 110.40300 116.82600 1.000 70.17361  ? 202 CYS A N   1 
ATOM   1262 C CA  . CYS A 1 195 ? 123.97400 111.08700 115.63300 1.000 65.96114  ? 202 CYS A CA  1 
ATOM   1263 C C   . CYS A 1 195 ? 125.19800 110.38700 115.05500 1.000 66.90717  ? 202 CYS A C   1 
ATOM   1264 O O   . CYS A 1 195 ? 125.29700 110.19400 113.83900 1.000 67.42588  ? 202 CYS A O   1 
ATOM   1265 C CB  . CYS A 1 195 ? 124.28900 112.54900 115.94600 1.000 67.31357  ? 202 CYS A CB  1 
ATOM   1266 S SG  . CYS A 1 195 ? 122.84000 113.55700 116.30300 1.000 80.88933  ? 202 CYS A SG  1 
ATOM   1267 N N   . THR A 1 196 ? 126.14800 110.01000 115.90900 1.000 67.74923  ? 203 THR A N   1 
ATOM   1268 C CA  . THR A 1 196 ? 127.35300 109.33400 115.43500 1.000 64.88385  ? 203 THR A CA  1 
ATOM   1269 C C   . THR A 1 196 ? 127.03400 107.98300 114.80600 1.000 66.83688  ? 203 THR A C   1 
ATOM   1270 O O   . THR A 1 196 ? 127.56800 107.63900 113.74800 1.000 69.82580  ? 203 THR A O   1 
ATOM   1271 C CB  . THR A 1 196 ? 128.34800 109.16800 116.57700 1.000 62.28517  ? 203 THR A CB  1 
ATOM   1272 O OG1 . THR A 1 196 ? 128.62300 110.44700 117.15700 1.000 70.66338  ? 203 THR A OG1 1 
ATOM   1273 C CG2 . THR A 1 196 ? 129.63800 108.57600 116.05900 1.000 65.52832  ? 203 THR A CG2 1 
ATOM   1274 N N   . ALA A 1 197 ? 126.17700 107.19300 115.45200 1.000 66.70271  ? 204 ALA A N   1 
ATOM   1275 C CA  . ALA A 1 197 ? 125.76000 105.92100 114.86900 1.000 62.85727  ? 204 ALA A CA  1 
ATOM   1276 C C   . ALA A 1 197 ? 125.07500 106.10600 113.52000 1.000 69.40649  ? 204 ALA A C   1 
ATOM   1277 O O   . ALA A 1 197 ? 125.34300 105.35500 112.57700 1.000 77.05384  ? 204 ALA A O   1 
ATOM   1278 C CB  . ALA A 1 197 ? 124.83800 105.17700 115.83200 1.000 59.83138  ? 204 ALA A CB  1 
ATOM   1279 N N   . SER A 1 198 ? 124.18200 107.09100 113.40900 1.000 62.03339  ? 205 SER A N   1 
ATOM   1280 C CA  . SER A 1 198 ? 123.47700 107.32500 112.14900 1.000 55.58852  ? 205 SER A CA  1 
ATOM   1281 C C   . SER A 1 198 ? 124.42100 107.74400 111.03000 1.000 55.61307  ? 205 SER A C   1 
ATOM   1282 O O   . SER A 1 198 ? 124.23900 107.34100 109.87700 1.000 60.47257  ? 205 SER A O   1 
ATOM   1283 C CB  . SER A 1 198 ? 122.39400 108.37800 112.34600 1.000 57.21748  ? 205 SER A CB  1 
ATOM   1284 O OG  . SER A 1 198 ? 121.50100 107.98000 113.36600 1.000 63.75204  ? 205 SER A OG  1 
ATOM   1285 N N   . ILE A 1 199 ? 125.41800 108.56900 111.33800 1.000 53.63451  ? 206 ILE A N   1 
ATOM   1286 C CA  . ILE A 1 199 ? 126.40600 108.95600 110.33500 1.000 56.26055  ? 206 ILE A CA  1 
ATOM   1287 C C   . ILE A 1 199 ? 127.27800 107.77200 109.92600 1.000 61.18801  ? 206 ILE A C   1 
ATOM   1288 O O   . ILE A 1 199 ? 127.54700 107.57000 108.73800 1.000 67.24236  ? 206 ILE A O   1 
ATOM   1289 C CB  . ILE A 1 199 ? 127.25500 110.13000 110.84800 1.000 57.27146  ? 206 ILE A CB  1 
ATOM   1290 C CG1 . ILE A 1 199 ? 126.41800 111.40300 110.89800 1.000 61.63302  ? 206 ILE A CG1 1 
ATOM   1291 C CG2 . ILE A 1 199 ? 128.46100 110.33900 109.96500 1.000 55.75914  ? 206 ILE A CG2 1 
ATOM   1292 C CD1 . ILE A 1 199 ? 127.05100 112.50100 111.69800 1.000 62.75765  ? 206 ILE A CD1 1 
ATOM   1293 N N   . LEU A 1 200 ? 127.74000 106.97700 110.89300 1.000 58.84748  ? 207 LEU A N   1 
ATOM   1294 C CA  . LEU A 1 200 ? 128.60000 105.84300 110.55600 1.000 58.56099  ? 207 LEU A CA  1 
ATOM   1295 C C   . LEU A 1 200 ? 127.87700 104.78200 109.73300 1.000 60.65234  ? 207 LEU A C   1 
ATOM   1296 O O   . LEU A 1 200 ? 128.46200 104.21200 108.80700 1.000 65.05476  ? 207 LEU A O   1 
ATOM   1297 C CB  . LEU A 1 200 ? 129.17900 105.22000 111.82100 1.000 57.69443  ? 207 LEU A CB  1 
ATOM   1298 C CG  . LEU A 1 200 ? 130.18800 106.07900 112.57600 1.000 61.86996  ? 207 LEU A CG  1 
ATOM   1299 C CD1 . LEU A 1 200 ? 130.61000 105.39000 113.85900 1.000 62.19678  ? 207 LEU A CD1 1 
ATOM   1300 C CD2 . LEU A 1 200 ? 131.38800 106.38100 111.70100 1.000 62.33520  ? 207 LEU A CD2 1 
ATOM   1301 N N   . ILE A 1 201 ? 126.62100 104.48300 110.05500 1.000 52.34263  ? 208 ILE A N   1 
ATOM   1302 C CA  . ILE A 1 201 ? 125.85200 103.55600 109.22800 1.000 53.24768  ? 208 ILE A CA  1 
ATOM   1303 C C   . ILE A 1 201 ? 125.61500 104.13600 107.83900 1.000 56.26118  ? 208 ILE A C   1 
ATOM   1304 O O   . ILE A 1 201 ? 125.79700 103.45700 106.82400 1.000 57.60368  ? 208 ILE A O   1 
ATOM   1305 C CB  . ILE A 1 201 ? 124.52400 103.19500 109.91200 1.000 47.90357  ? 208 ILE A CB  1 
ATOM   1306 C CG1 . ILE A 1 201 ? 124.78400 102.40600 111.18400 1.000 51.19490  ? 208 ILE A CG1 1 
ATOM   1307 C CG2 . ILE A 1 201 ? 123.65200 102.39500 108.98300 1.000 51.93498  ? 208 ILE A CG2 1 
ATOM   1308 C CD1 . ILE A 1 201 ? 123.62400 102.40900 112.11500 1.000 53.24627  ? 208 ILE A CD1 1 
ATOM   1309 N N   . SER A 1 202 ? 125.21200 105.40300 107.77600 1.000 53.65115  ? 209 SER A N   1 
ATOM   1310 C CA  . SER A 1 202 ? 124.93300 106.04500 106.49600 1.000 48.15377  ? 209 SER A CA  1 
ATOM   1311 C C   . SER A 1 202 ? 126.15700 106.10000 105.58800 1.000 50.75095  ? 209 SER A C   1 
ATOM   1312 O O   . SER A 1 202 ? 126.03900 105.89800 104.37600 1.000 56.73266  ? 209 SER A O   1 
ATOM   1313 C CB  . SER A 1 202 ? 124.38600 107.44700 106.73900 1.000 51.17423  ? 209 SER A CB  1 
ATOM   1314 O OG  . SER A 1 202 ? 124.04700 108.07500 105.52300 1.000 58.76398  ? 209 SER A OG  1 
ATOM   1315 N N   . CYS A 1 203 ? 127.34100 106.35600 106.14400 1.000 57.15272  ? 210 CYS A N   1 
ATOM   1316 C CA  . CYS A 1 203 ? 128.55100 106.34000 105.32300 1.000 59.04781  ? 210 CYS A CA  1 
ATOM   1317 C C   . CYS A 1 203 ? 128.93500 104.93500 104.86100 1.000 63.06904  ? 210 CYS A C   1 
ATOM   1318 O O   . CYS A 1 203 ? 129.37000 104.76000 103.71900 1.000 66.87051  ? 210 CYS A O   1 
ATOM   1319 C CB  . CYS A 1 203 ? 129.70600 106.98500 106.08200 1.000 57.86386  ? 210 CYS A CB  1 
ATOM   1320 S SG  . CYS A 1 203 ? 129.44000 108.72600 106.46800 1.000 74.57911  ? 210 CYS A SG  1 
ATOM   1321 N N   . CYS A 1 204 ? 128.76600 103.92000 105.70900 1.000 60.90298  ? 211 CYS A N   1 
ATOM   1322 C CA  . CYS A 1 204 ? 129.01600 102.54600 105.27200 1.000 59.43149  ? 211 CYS A CA  1 
ATOM   1323 C C   . CYS A 1 204 ? 128.03000 102.10600 104.19200 1.000 65.24126  ? 211 CYS A C   1 
ATOM   1324 O O   . CYS A 1 204 ? 128.41900 101.51500 103.17400 1.000 68.91838  ? 211 CYS A O   1 
ATOM   1325 C CB  . CYS A 1 204 ? 128.96300 101.59900 106.46600 1.000 64.53046  ? 211 CYS A CB  1 
ATOM   1326 S SG  . CYS A 1 204 ? 130.30800 101.82100 107.64500 1.000 82.81035  ? 211 CYS A SG  1 
ATOM   1327 N N   . ALA A 1 205 ? 126.74600 102.39700 104.38700 1.000 61.08324  ? 212 ALA A N   1 
ATOM   1328 C CA  . ALA A 1 205 ? 125.75700 102.08300 103.36400 1.000 56.31735  ? 212 ALA A CA  1 
ATOM   1329 C C   . ALA A 1 205 ? 126.05500 102.80900 102.05900 1.000 52.16173  ? 212 ALA A C   1 
ATOM   1330 O O   . ALA A 1 205 ? 125.90800 102.23400 100.97700 1.000 55.62576  ? 212 ALA A O   1 
ATOM   1331 C CB  . ALA A 1 205 ? 124.35900 102.42900 103.86800 1.000 52.86854  ? 212 ALA A CB  1 
ATOM   1332 N N   . SER A 1 206 ? 126.39300 104.09600 102.13100 1.000 48.17225  ? 213 SER A N   1 
ATOM   1333 C CA  . SER A 1 206 ? 126.77100 104.81900 100.92200 1.000 48.80706  ? 213 SER A CA  1 
ATOM   1334 C C   . SER A 1 206 ? 127.98700 104.20200 100.24400 1.000 56.07303  ? 213 SER A C   1 
ATOM   1335 O O   . SER A 1 206 ? 128.02700 104.08800 99.01500  1.000 61.88453  ? 213 SER A O   1 
ATOM   1336 C CB  . SER A 1 206 ? 127.04200 106.28100 101.25400 1.000 50.56010  ? 213 SER A CB  1 
ATOM   1337 O OG  . SER A 1 206 ? 125.87900 106.90300 101.75700 1.000 55.88785  ? 213 SER A OG  1 
ATOM   1338 N N   . ALA A 1 207 ? 128.97300 103.76400 101.02700 1.000 55.32159  ? 214 ALA A N   1 
ATOM   1339 C CA  . ALA A 1 207 ? 130.14100 103.09800 100.46200 1.000 51.43876  ? 214 ALA A CA  1 
ATOM   1340 C C   . ALA A 1 207 ? 129.81400 101.74300 99.86500  1.000 54.82723  ? 214 ALA A C   1 
ATOM   1341 O O   . ALA A 1 207 ? 130.61900 101.21100 99.09600  1.000 56.42614  ? 214 ALA A O   1 
ATOM   1342 C CB  . ALA A 1 207 ? 131.22500 102.94100 101.52500 1.000 55.92317  ? 214 ALA A CB  1 
ATOM   1343 N N   . MET A 1 208 ? 128.66800 101.16500 100.20900 1.000 57.13247  ? 215 MET A N   1 
ATOM   1344 C CA  . MET A 1 208 ? 128.25200 99.94600  99.52100  1.000 56.37960  ? 215 MET A CA  1 
ATOM   1345 C C   . MET A 1 208 ? 127.42900 100.22900 98.26600  1.000 56.82261  ? 215 MET A C   1 
ATOM   1346 O O   . MET A 1 208 ? 127.68300 99.63900  97.21300  1.000 57.04001  ? 215 MET A O   1 
ATOM   1347 C CB  . MET A 1 208 ? 127.46100 99.03800  100.46200 1.000 55.04462  ? 215 MET A CB  1 
ATOM   1348 C CG  . MET A 1 208 ? 127.03000 97.74200  99.80800  1.000 58.46769  ? 215 MET A CG  1 
ATOM   1349 S SD  . MET A 1 208 ? 126.06000 96.68100  100.88100 1.000 75.73389  ? 215 MET A SD  1 
ATOM   1350 C CE  . MET A 1 208 ? 124.58100 97.66100  101.04800 1.000 60.90330  ? 215 MET A CE  1 
ATOM   1351 N N   . TYR A 1 209 ? 126.42600 101.10500 98.36500  1.000 56.55254  ? 216 TYR A N   1 
ATOM   1352 C CA  . TYR A 1 209 ? 125.57200 101.41300 97.21800  1.000 53.42411  ? 216 TYR A CA  1 
ATOM   1353 C C   . TYR A 1 209 ? 126.30500 102.13600 96.09300  1.000 53.60009  ? 216 TYR A C   1 
ATOM   1354 O O   . TYR A 1 209 ? 125.96800 101.93200 94.92400  1.000 60.70348  ? 216 TYR A O   1 
ATOM   1355 C CB  . TYR A 1 209 ? 124.37100 102.25600 97.64100  1.000 53.03645  ? 216 TYR A CB  1 
ATOM   1356 C CG  . TYR A 1 209 ? 123.45200 101.61800 98.64900  1.000 52.30440  ? 216 TYR A CG  1 
ATOM   1357 C CD1 . TYR A 1 209 ? 123.05600 100.30200 98.52200  1.000 50.64110  ? 216 TYR A CD1 1 
ATOM   1358 C CD2 . TYR A 1 209 ? 122.95000 102.34800 99.70700  1.000 53.76591  ? 216 TYR A CD2 1 
ATOM   1359 C CE1 . TYR A 1 209 ? 122.21100 99.72800  99.43600  1.000 48.46736  ? 216 TYR A CE1 1 
ATOM   1360 C CE2 . TYR A 1 209 ? 122.10400 101.78300 100.62200 1.000 52.62692  ? 216 TYR A CE2 1 
ATOM   1361 C CZ  . TYR A 1 209 ? 121.73900 100.47500 100.48300 1.000 50.30995  ? 216 TYR A CZ  1 
ATOM   1362 O OH  . TYR A 1 209 ? 120.88800 99.91700  101.40000 1.000 57.52342  ? 216 TYR A OH  1 
ATOM   1363 N N   . THR A 1 210 ? 127.28200 102.98700 96.40400  1.000 49.80406  ? 217 THR A N   1 
ATOM   1364 C CA  . THR A 1 210 ? 127.98700 103.71900 95.35300  1.000 49.44108  ? 217 THR A CA  1 
ATOM   1365 C C   . THR A 1 210 ? 128.62500 102.83900 94.28300  1.000 55.16894  ? 217 THR A C   1 
ATOM   1366 O O   . THR A 1 210 ? 128.36800 103.08300 93.09300  1.000 60.27010  ? 217 THR A O   1 
ATOM   1367 C CB  . THR A 1 210 ? 129.01800 104.65700 95.98200  1.000 56.68356  ? 217 THR A CB  1 
ATOM   1368 O OG1 . THR A 1 210 ? 128.34400 105.63900 96.77200  1.000 63.20131  ? 217 THR A OG1 1 
ATOM   1369 C CG2 . THR A 1 210 ? 129.82600 105.34200 94.90200  1.000 55.38436  ? 217 THR A CG2 1 
ATOM   1370 N N   . PRO A 1 211 ? 129.45400 101.83800 94.59800  1.000 55.04922  ? 218 PRO A N   1 
ATOM   1371 C CA  . PRO A 1 211 ? 130.00200 101.01000 93.51300  1.000 57.44640  ? 218 PRO A CA  1 
ATOM   1372 C C   . PRO A 1 211 ? 129.00200 100.05200 92.89100  1.000 56.91863  ? 218 PRO A C   1 
ATOM   1373 O O   . PRO A 1 211 ? 129.12800 99.74600  91.70000  1.000 56.15805  ? 218 PRO A O   1 
ATOM   1374 C CB  . PRO A 1 211 ? 131.14500 100.24800 94.19500  1.000 56.39014  ? 218 PRO A CB  1 
ATOM   1375 C CG  . PRO A 1 211 ? 130.76000 100.19700 95.60300  1.000 52.95621  ? 218 PRO A CG  1 
ATOM   1376 C CD  . PRO A 1 211 ? 130.07100 101.49000 95.88800  1.000 53.46377  ? 218 PRO A CD  1 
ATOM   1377 N N   . ILE A 1 212 ? 128.02100 99.56500  93.64300  1.000 57.69575  ? 219 ILE A N   1 
ATOM   1378 C CA  . ILE A 1 212 ? 127.14600 98.50200  93.15300  1.000 54.87462  ? 219 ILE A CA  1 
ATOM   1379 C C   . ILE A 1 212 ? 125.98800 99.05300  92.33300  1.000 55.65024  ? 219 ILE A C   1 
ATOM   1380 O O   . ILE A 1 212 ? 125.68100 98.53700  91.25600  1.000 57.78095  ? 219 ILE A O   1 
ATOM   1381 C CB  . ILE A 1 212 ? 126.64100 97.65000  94.33200  1.000 52.24123  ? 219 ILE A CB  1 
ATOM   1382 C CG1 . ILE A 1 212 ? 127.81000 96.95200  95.01500  1.000 57.52938  ? 219 ILE A CG1 1 
ATOM   1383 C CG2 . ILE A 1 212 ? 125.65300 96.62800  93.85000  1.000 56.34153  ? 219 ILE A CG2 1 
ATOM   1384 C CD1 . ILE A 1 212 ? 127.39800 96.09700  96.17700  1.000 58.53398  ? 219 ILE A CD1 1 
ATOM   1385 N N   . GLU A 1 213 ? 125.32600 100.10200 92.80900  1.000 57.75983  ? 220 GLU A N   1 
ATOM   1386 C CA  . GLU A 1 213 ? 124.18900 100.67000 92.09700  1.000 58.17003  ? 220 GLU A CA  1 
ATOM   1387 C C   . GLU A 1 213 ? 124.58200 101.72100 91.07000  1.000 63.58700  ? 220 GLU A C   1 
ATOM   1388 O O   . GLU A 1 213 ? 123.75600 102.07500 90.22500  1.000 67.80141  ? 220 GLU A O   1 
ATOM   1389 C CB  . GLU A 1 213 ? 123.20300 101.29100 93.08900  1.000 51.81707  ? 220 GLU A CB  1 
ATOM   1390 C CG  . GLU A 1 213 ? 122.65800 100.35000 94.14600  1.000 52.57649  ? 220 GLU A CG  1 
ATOM   1391 C CD  . GLU A 1 213 ? 121.69700 99.32300  93.59600  1.000 57.20278  ? 220 GLU A CD  1 
ATOM   1392 O OE1 . GLU A 1 213 ? 121.45100 99.31100  92.37600  1.000 54.82163  ? 220 GLU A OE1 1 
ATOM   1393 O OE2 . GLU A 1 213 ? 121.17600 98.52300  94.39400  1.000 63.55005  ? 220 GLU A OE2 1 
ATOM   1394 N N   . GLY A 1 214 ? 125.80900 102.22500 91.11900  1.000 63.11255  ? 221 GLY A N   1 
ATOM   1395 C CA  . GLY A 1 214 ? 126.23500 103.26700 90.21200  1.000 60.74563  ? 221 GLY A CA  1 
ATOM   1396 C C   . GLY A 1 214 ? 125.72500 104.64900 90.53900  1.000 63.90397  ? 221 GLY A C   1 
ATOM   1397 O O   . GLY A 1 214 ? 125.93900 105.57200 89.74800  1.000 68.32065  ? 221 GLY A O   1 
ATOM   1398 N N   . TRP A 1 215 ? 125.05700 104.82300 91.67500  1.000 51.64602  ? 222 TRP A N   1 
ATOM   1399 C CA  . TRP A 1 215 ? 124.68300 106.15000 92.13500  1.000 50.31386  ? 222 TRP A CA  1 
ATOM   1400 C C   . TRP A 1 215 ? 125.91800 106.98200 92.44900  1.000 53.10605  ? 222 TRP A C   1 
ATOM   1401 O O   . TRP A 1 215 ? 127.00600 106.46200 92.70300  1.000 54.70011  ? 222 TRP A O   1 
ATOM   1402 C CB  . TRP A 1 215 ? 123.82300 106.06100 93.38900  1.000 46.50256  ? 222 TRP A CB  1 
ATOM   1403 C CG  . TRP A 1 215 ? 122.55700 105.33500 93.21200  1.000 46.73247  ? 222 TRP A CG  1 
ATOM   1404 C CD1 . TRP A 1 215 ? 121.89600 105.11900 92.05000  1.000 50.20084  ? 222 TRP A CD1 1 
ATOM   1405 C CD2 . TRP A 1 215 ? 121.79600 104.70000 94.23500  1.000 44.70230  ? 222 TRP A CD2 1 
ATOM   1406 N NE1 . TRP A 1 215 ? 120.75500 104.40100 92.28600  1.000 53.81046  ? 222 TRP A NE1 1 
ATOM   1407 C CE2 . TRP A 1 215 ? 120.67400 104.13000 93.62400  1.000 45.96534  ? 222 TRP A CE2 1 
ATOM   1408 C CE3 . TRP A 1 215 ? 121.95200 104.56400 95.61200  1.000 51.07692  ? 222 TRP A CE3 1 
ATOM   1409 C CZ2 . TRP A 1 215 ? 119.71700 103.43400 94.34000  1.000 46.71581  ? 222 TRP A CZ2 1 
ATOM   1410 C CZ3 . TRP A 1 215 ? 121.00400 103.87700 96.31700  1.000 48.66549  ? 222 TRP A CZ3 1 
ATOM   1411 C CH2 . TRP A 1 215 ? 119.90100 103.31900 95.68400  1.000 47.85926  ? 222 TRP A CH2 1 
ATOM   1412 N N   . SER A 1 216 ? 125.73900 108.29600 92.43200  1.000 54.76785  ? 223 SER A N   1 
ATOM   1413 C CA  . SER A 1 216 ? 126.74000 109.16100 93.02400  1.000 52.93191  ? 223 SER A CA  1 
ATOM   1414 C C   . SER A 1 216 ? 126.71000 108.99100 94.53700  1.000 56.07665  ? 223 SER A C   1 
ATOM   1415 O O   . SER A 1 216 ? 125.72300 108.53000 95.11400  1.000 59.84396  ? 223 SER A O   1 
ATOM   1416 C CB  . SER A 1 216 ? 126.49900 110.61600 92.63400  1.000 58.32755  ? 223 SER A CB  1 
ATOM   1417 O OG  . SER A 1 216 ? 125.43000 111.16900 93.37200  1.000 64.85480  ? 223 SER A OG  1 
ATOM   1418 N N   . TYR A 1 217 ? 127.81800 109.34600 95.18300  1.000 59.83219  ? 224 TYR A N   1 
ATOM   1419 C CA  . TYR A 1 217 ? 127.90400 109.18000 96.62900  1.000 56.15024  ? 224 TYR A CA  1 
ATOM   1420 C C   . TYR A 1 217 ? 126.85000 110.00700 97.35700  1.000 58.36515  ? 224 TYR A C   1 
ATOM   1421 O O   . TYR A 1 217 ? 126.21500 109.52400 98.30200  1.000 65.29141  ? 224 TYR A O   1 
ATOM   1422 C CB  . TYR A 1 217 ? 129.30400 109.55300 97.10900  1.000 55.99651  ? 224 TYR A CB  1 
ATOM   1423 C CG  . TYR A 1 217 ? 129.60300 109.12100 98.52000  1.000 56.47356  ? 224 TYR A CG  1 
ATOM   1424 C CD1 . TYR A 1 217 ? 130.13400 107.87100 98.77900  1.000 60.65004  ? 224 TYR A CD1 1 
ATOM   1425 C CD2 . TYR A 1 217 ? 129.36400 109.96300 99.59200  1.000 60.54828  ? 224 TYR A CD2 1 
ATOM   1426 C CE1 . TYR A 1 217 ? 130.40700 107.46600 100.06400 1.000 59.03329  ? 224 TYR A CE1 1 
ATOM   1427 C CE2 . TYR A 1 217 ? 129.64000 109.56800 100.88100 1.000 62.47165  ? 224 TYR A CE2 1 
ATOM   1428 C CZ  . TYR A 1 217 ? 130.16000 108.31800 101.11000 1.000 60.79336  ? 224 TYR A CZ  1 
ATOM   1429 O OH  . TYR A 1 217 ? 130.44600 107.91700 102.39000 1.000 65.48812  ? 224 TYR A OH  1 
ATOM   1430 N N   . PHE A 1 218 ? 126.63900 111.25000 96.92600  1.000 58.17640  ? 225 PHE A N   1 
ATOM   1431 C CA  . PHE A 1 218 ? 125.63000 112.09000 97.56200  1.000 55.56921  ? 225 PHE A CA  1 
ATOM   1432 C C   . PHE A 1 218 ? 124.20900 111.59300 97.32200  1.000 57.42333  ? 225 PHE A C   1 
ATOM   1433 O O   . PHE A 1 218 ? 123.35800 111.69200 98.21300  1.000 66.38047  ? 225 PHE A O   1 
ATOM   1434 C CB  . PHE A 1 218 ? 125.76500 113.52700 97.07900  1.000 60.24481  ? 225 PHE A CB  1 
ATOM   1435 C CG  . PHE A 1 218 ? 124.78200 114.45400 97.70700  1.000 62.22795  ? 225 PHE A CG  1 
ATOM   1436 C CD1 . PHE A 1 218 ? 124.68400 114.54600 99.08000  1.000 61.55035  ? 225 PHE A CD1 1 
ATOM   1437 C CD2 . PHE A 1 218 ? 123.94700 115.22400 96.92700  1.000 56.97205  ? 225 PHE A CD2 1 
ATOM   1438 C CE1 . PHE A 1 218 ? 123.77500 115.38700 99.66200  1.000 57.63814  ? 225 PHE A CE1 1 
ATOM   1439 C CE2 . PHE A 1 218 ? 123.03900 116.07000 97.50500  1.000 58.48378  ? 225 PHE A CE2 1 
ATOM   1440 C CZ  . PHE A 1 218 ? 122.95200 116.15000 98.87400  1.000 62.35019  ? 225 PHE A CZ  1 
ATOM   1441 N N   . ASP A 1 219 ? 123.92400 111.05800 96.13600  1.000 49.56168  ? 226 ASP A N   1 
ATOM   1442 C CA  . ASP A 1 219 ? 122.62500 110.42800 95.92100  1.000 44.52804  ? 226 ASP A CA  1 
ATOM   1443 C C   . ASP A 1 219 ? 122.42000 109.23300 96.83700  1.000 49.32432  ? 226 ASP A C   1 
ATOM   1444 O O   . ASP A 1 219 ? 121.30600 108.99400 97.31100  1.000 57.39525  ? 226 ASP A O   1 
ATOM   1445 C CB  . ASP A 1 219 ? 122.46700 110.01600 94.46100  1.000 49.43600  ? 226 ASP A CB  1 
ATOM   1446 C CG  . ASP A 1 219 ? 122.37800 111.20300 93.52700  1.000 59.22524  ? 226 ASP A CG  1 
ATOM   1447 O OD1 . ASP A 1 219 ? 121.62700 112.14800 93.83900  1.000 65.58712  ? 226 ASP A OD1 1 
ATOM   1448 O OD2 . ASP A 1 219 ? 123.05300 111.19100 92.47800  1.000 55.12375  ? 226 ASP A OD2 1 
ATOM   1449 N N   . SER A 1 220 ? 123.47800 108.47400 97.11200  1.000 46.63474  ? 227 SER A N   1 
ATOM   1450 C CA  . SER A 1 220 ? 123.34500 107.35400 98.03600  1.000 47.08967  ? 227 SER A CA  1 
ATOM   1451 C C   . SER A 1 220 ? 123.18600 107.79400 99.48800  1.000 48.98454  ? 227 SER A C   1 
ATOM   1452 O O   . SER A 1 220 ? 122.43800 107.16000 100.23400 1.000 53.89379  ? 227 SER A O   1 
ATOM   1453 C CB  . SER A 1 220 ? 124.54200 106.42600 97.89300  1.000 52.36175  ? 227 SER A CB  1 
ATOM   1454 O OG  . SER A 1 220 ? 125.66500 106.96700 98.55000  1.000 60.88852  ? 227 SER A OG  1 
ATOM   1455 N N   . LEU A 1 221 ? 123.83200 108.88500 99.90700  1.000 46.65695  ? 228 LEU A N   1 
ATOM   1456 C CA  . LEU A 1 221 ? 123.53900 109.45400 101.22600 1.000 39.36852  ? 228 LEU A CA  1 
ATOM   1457 C C   . LEU A 1 221 ? 122.10200 109.94800 101.33700 1.000 44.02629  ? 228 LEU A C   1 
ATOM   1458 O O   . LEU A 1 221 ? 121.44000 109.73700 102.36300 1.000 50.49012  ? 228 LEU A O   1 
ATOM   1459 C CB  . LEU A 1 221 ? 124.50000 110.59600 101.54500 1.000 40.15573  ? 228 LEU A CB  1 
ATOM   1460 C CG  . LEU A 1 221 ? 125.92000 110.27500 101.99200 1.000 45.34135  ? 228 LEU A CG  1 
ATOM   1461 C CD1 . LEU A 1 221 ? 126.75400 111.53300 102.00000 1.000 49.94271  ? 228 LEU A CD1 1 
ATOM   1462 C CD2 . LEU A 1 221 ? 125.88300 109.68600 103.37200 1.000 49.86577  ? 228 LEU A CD2 1 
ATOM   1463 N N   . TYR A 1 222 ? 121.60800 110.63100 100.30700 1.000 43.49581  ? 229 TYR A N   1 
ATOM   1464 C CA  . TYR A 1 222 ? 120.21900 111.07400 100.30900 1.000 44.65601  ? 229 TYR A CA  1 
ATOM   1465 C C   . TYR A 1 222 ? 119.24500 109.90000 100.34100 1.000 44.62497  ? 229 TYR A C   1 
ATOM   1466 O O   . TYR A 1 222 ? 118.24700 109.94000 101.06900 1.000 43.28813  ? 229 TYR A O   1 
ATOM   1467 C CB  . TYR A 1 222 ? 119.97200 111.96900 99.09700  1.000 46.98061  ? 229 TYR A CB  1 
ATOM   1468 C CG  . TYR A 1 222 ? 118.53100 112.14100 98.69200  1.000 47.21043  ? 229 TYR A CG  1 
ATOM   1469 C CD1 . TYR A 1 222 ? 117.74100 113.11100 99.28100  1.000 42.49258  ? 229 TYR A CD1 1 
ATOM   1470 C CD2 . TYR A 1 222 ? 117.97500 111.36900 97.68800  1.000 48.79016  ? 229 TYR A CD2 1 
ATOM   1471 C CE1 . TYR A 1 222 ? 116.43400 113.28100 98.90900  1.000 40.81074  ? 229 TYR A CE1 1 
ATOM   1472 C CE2 . TYR A 1 222 ? 116.66700 111.53700 97.30500  1.000 48.27062  ? 229 TYR A CE2 1 
ATOM   1473 C CZ  . TYR A 1 222 ? 115.90200 112.49300 97.92000  1.000 49.80571  ? 229 TYR A CZ  1 
ATOM   1474 O OH  . TYR A 1 222 ? 114.59700 112.66600 97.53300  1.000 51.23040  ? 229 TYR A OH  1 
ATOM   1475 N N   . PHE A 1 223 ? 119.51100 108.84600 99.56600  1.000 43.09975  ? 230 PHE A N   1 
ATOM   1476 C CA  . PHE A 1 223 ? 118.72800 107.62000 99.69600  1.000 36.18648  ? 230 PHE A CA  1 
ATOM   1477 C C   . PHE A 1 223 ? 118.78400 107.03500 101.09500 1.000 37.57670  ? 230 PHE A C   1 
ATOM   1478 O O   . PHE A 1 223 ? 117.77000 106.56000 101.61100 1.000 40.47212  ? 230 PHE A O   1 
ATOM   1479 C CB  . PHE A 1 223 ? 119.18400 106.55700 98.70600  1.000 33.69305  ? 230 PHE A CB  1 
ATOM   1480 C CG  . PHE A 1 223 ? 118.56200 105.21800 98.96500  1.000 38.46043  ? 230 PHE A CG  1 
ATOM   1481 C CD1 . PHE A 1 223 ? 117.22800 104.99600 98.71700  1.000 45.30100  ? 230 PHE A CD1 1 
ATOM   1482 C CD2 . PHE A 1 223 ? 119.31000 104.18800 99.49100  1.000 39.88448  ? 230 PHE A CD2 1 
ATOM   1483 C CE1 . PHE A 1 223 ? 116.66100 103.77000 98.97600  1.000 40.04413  ? 230 PHE A CE1 1 
ATOM   1484 C CE2 . PHE A 1 223 ? 118.74300 102.96400 99.74700  1.000 39.38595  ? 230 PHE A CE2 1 
ATOM   1485 C CZ  . PHE A 1 223 ? 117.42100 102.75700 99.48900  1.000 38.13203  ? 230 PHE A CZ  1 
ATOM   1486 N N   . CYS A 1 224 ? 119.96300 107.01400 101.71200 1.000 42.89066  ? 231 CYS A N   1 
ATOM   1487 C CA  . CYS A 1 224 ? 120.06000 106.48700 103.06700 1.000 37.76518  ? 231 CYS A CA  1 
ATOM   1488 C C   . CYS A 1 224 ? 119.18100 107.26600 104.03300 1.000 40.81888  ? 231 CYS A C   1 
ATOM   1489 O O   . CYS A 1 224 ? 118.45900 106.67000 104.83400 1.000 54.56469  ? 231 CYS A O   1 
ATOM   1490 C CB  . CYS A 1 224 ? 121.51200 106.47300 103.53500 1.000 35.75913  ? 231 CYS A CB  1 
ATOM   1491 S SG  . CYS A 1 224 ? 122.54600 105.29500 102.65700 1.000 49.40348  ? 231 CYS A SG  1 
ATOM   1492 N N   . PHE A 1 225 ? 119.22000 108.59400 103.98200 1.000 28.91900  ? 232 PHE A N   1 
ATOM   1493 C CA  . PHE A 1 225 ? 118.32900 109.35500 104.85700 1.000 29.20803  ? 232 PHE A CA  1 
ATOM   1494 C C   . PHE A 1 225 ? 116.85900 109.10400 104.54100 1.000 32.83881  ? 232 PHE A C   1 
ATOM   1495 O O   . PHE A 1 225 ? 116.04700 108.90700 105.44900 1.000 33.85907  ? 232 PHE A O   1 
ATOM   1496 C CB  . PHE A 1 225 ? 118.60900 110.84700 104.79200 1.000 32.68770  ? 232 PHE A CB  1 
ATOM   1497 C CG  . PHE A 1 225 ? 117.66300 111.65100 105.63200 1.000 33.88863  ? 232 PHE A CG  1 
ATOM   1498 C CD1 . PHE A 1 225 ? 117.80100 111.68500 107.00600 1.000 38.25709  ? 232 PHE A CD1 1 
ATOM   1499 C CD2 . PHE A 1 225 ? 116.61500 112.34000 105.05800 1.000 35.69795  ? 232 PHE A CD2 1 
ATOM   1500 C CE1 . PHE A 1 225 ? 116.92900 112.40500 107.78400 1.000 31.56050  ? 232 PHE A CE1 1 
ATOM   1501 C CE2 . PHE A 1 225 ? 115.74100 113.06100 105.83600 1.000 37.12465  ? 232 PHE A CE2 1 
ATOM   1502 C CZ  . PHE A 1 225 ? 115.90000 113.09200 107.19900 1.000 36.05110  ? 232 PHE A CZ  1 
ATOM   1503 N N   . VAL A 1 226 ? 116.48800 109.13500 103.26100 1.000 40.65118  ? 233 VAL A N   1 
ATOM   1504 C CA  . VAL A 1 226 ? 115.08700 108.96200 102.87400 1.000 28.69897  ? 233 VAL A CA  1 
ATOM   1505 C C   . VAL A 1 226 ? 114.54800 107.58900 103.25700 1.000 26.92967  ? 233 VAL A C   1 
ATOM   1506 O O   . VAL A 1 226 ? 113.37200 107.45500 103.60700 1.000 35.80620  ? 233 VAL A O   1 
ATOM   1507 C CB  . VAL A 1 226 ? 114.93400 109.24100 101.36800 1.000 30.87092  ? 233 VAL A CB  1 
ATOM   1508 C CG1 . VAL A 1 226 ? 113.62500 108.73500 100.86100 1.000 30.03905  ? 233 VAL A CG1 1 
ATOM   1509 C CG2 . VAL A 1 226 ? 115.02500 110.71900 101.11700 1.000 31.39246  ? 233 VAL A CG2 1 
ATOM   1510 N N   . ALA A 1 227 ? 115.38300 106.55600 103.21900 1.000 30.75973  ? 234 ALA A N   1 
ATOM   1511 C CA  . ALA A 1 227 ? 114.96600 105.24300 103.69600 1.000 23.82868  ? 234 ALA A CA  1 
ATOM   1512 C C   . ALA A 1 227 ? 114.93700 105.16100 105.21700 1.000 38.46935  ? 234 ALA A C   1 
ATOM   1513 O O   . ALA A 1 227 ? 113.95900 104.67900 105.79500 1.000 45.12650  ? 234 ALA A O   1 
ATOM   1514 C CB  . ALA A 1 227 ? 115.88500 104.16600 103.13100 1.000 26.14498  ? 234 ALA A CB  1 
ATOM   1515 N N   . PHE A 1 228 ? 116.00700 105.59100 105.88400 1.000 37.65846  ? 235 PHE A N   1 
ATOM   1516 C CA  . PHE A 1 228 ? 116.10600 105.42300 107.32900 1.000 21.31672  ? 235 PHE A CA  1 
ATOM   1517 C C   . PHE A 1 228 ? 115.10300 106.27900 108.09200 1.000 28.98480  ? 235 PHE A C   1 
ATOM   1518 O O   . PHE A 1 228 ? 114.64300 105.87400 109.16100 1.000 47.92733  ? 235 PHE A O   1 
ATOM   1519 C CB  . PHE A 1 228 ? 117.51800 105.76600 107.80000 1.000 29.33092  ? 235 PHE A CB  1 
ATOM   1520 C CG  . PHE A 1 228 ? 118.59500 104.87000 107.25100 1.000 28.16519  ? 235 PHE A CG  1 
ATOM   1521 C CD1 . PHE A 1 228 ? 118.30000 103.81600 106.41300 1.000 31.40224  ? 235 PHE A CD1 1 
ATOM   1522 C CD2 . PHE A 1 228 ? 119.91400 105.10700 107.56500 1.000 31.26079  ? 235 PHE A CD2 1 
ATOM   1523 C CE1 . PHE A 1 228 ? 119.29500 103.01600 105.91400 1.000 36.28688  ? 235 PHE A CE1 1 
ATOM   1524 C CE2 . PHE A 1 228 ? 120.90800 104.30600 107.06900 1.000 35.12228  ? 235 PHE A CE2 1 
ATOM   1525 C CZ  . PHE A 1 228 ? 120.59800 103.26100 106.24200 1.000 32.77052  ? 235 PHE A CZ  1 
ATOM   1526 N N   . SER A 1 229 ? 114.74700 107.45100 107.57800 1.000 27.14654  ? 236 SER A N   1 
ATOM   1527 C CA  . SER A 1 229 ? 113.68400 108.23200 108.20000 1.000 28.30485  ? 236 SER A CA  1 
ATOM   1528 C C   . SER A 1 229 ? 112.30000 107.65600 107.96800 1.000 39.68424  ? 236 SER A C   1 
ATOM   1529 O O   . SER A 1 229 ? 111.33300 108.20700 108.49700 1.000 46.46656  ? 236 SER A O   1 
ATOM   1530 C CB  . SER A 1 229 ? 113.73200 109.67100 107.70600 1.000 25.24047  ? 236 SER A CB  1 
ATOM   1531 O OG  . SER A 1 229 ? 113.56700 109.71500 106.30900 1.000 41.13277  ? 236 SER A OG  1 
ATOM   1532 N N   . THR A 1 230 ? 112.18100 106.58400 107.19100 1.000 33.67288  ? 237 THR A N   1 
ATOM   1533 C CA  . THR A 1 230 ? 110.92600 106.00500 106.72200 1.000 20.11054  ? 237 THR A CA  1 
ATOM   1534 C C   . THR A 1 230 ? 110.10600 106.94400 105.84800 1.000 21.69769  ? 237 THR A C   1 
ATOM   1535 O O   . THR A 1 230 ? 108.92200 106.68000 105.62200 1.000 38.34526  ? 237 THR A O   1 
ATOM   1536 C CB  . THR A 1 230 ? 110.05300 105.51000 107.87900 1.000 28.03879  ? 237 THR A CB  1 
ATOM   1537 O OG1 . THR A 1 230 ? 109.46800 106.63200 108.54200 1.000 38.01704  ? 237 THR A OG1 1 
ATOM   1538 C CG2 . THR A 1 230 ? 110.87000 104.71300 108.86900 1.000 25.11843  ? 237 THR A CG2 1 
ATOM   1539 N N   . ILE A 1 231 ? 110.67500 108.05000 105.36600 1.000 21.19362  ? 238 ILE A N   1 
ATOM   1540 C CA  . ILE A 1 231 ? 109.94800 108.86800 104.39800 1.000 19.78626  ? 238 ILE A CA  1 
ATOM   1541 C C   . ILE A 1 231 ? 109.72900 108.07800 103.11600 1.000 22.36315  ? 238 ILE A C   1 
ATOM   1542 O O   . ILE A 1 231 ? 108.59300 107.84800 102.69200 1.000 40.60212  ? 238 ILE A O   1 
ATOM   1543 C CB  . ILE A 1 231 ? 110.68400 110.18800 104.12500 1.000 18.57494  ? 238 ILE A CB  1 
ATOM   1544 C CG1 . ILE A 1 231 ? 110.78600 111.02700 105.38800 1.000 29.06626  ? 238 ILE A CG1 1 
ATOM   1545 C CG2 . ILE A 1 231 ? 109.94000 110.97700 103.10700 1.000 20.15605  ? 238 ILE A CG2 1 
ATOM   1546 C CD1 . ILE A 1 231 ? 111.79800 112.12600 105.28600 1.000 27.32536  ? 238 ILE A CD1 1 
ATOM   1547 N N   . GLY A 1 232 ? 110.81300 107.61700 102.50400 1.000 16.21014  ? 239 GLY A N   1 
ATOM   1548 C CA  . GLY A 1 232 ? 110.71800 106.69300 101.39400 1.000 14.83267  ? 239 GLY A CA  1 
ATOM   1549 C C   . GLY A 1 232 ? 109.96600 107.17100 100.17100 1.000 25.34261  ? 239 GLY A C   1 
ATOM   1550 O O   . GLY A 1 232 ? 108.89600 106.64100 99.87100  1.000 38.89045  ? 239 GLY A O   1 
ATOM   1551 N N   . PHE A 1 233 ? 110.47400 108.18900 99.47400  1.000 19.38350  ? 240 PHE A N   1 
ATOM   1552 C CA  . PHE A 1 233 ? 109.79000 108.64500 98.26900  1.000 23.03147  ? 240 PHE A CA  1 
ATOM   1553 C C   . PHE A 1 233 ? 109.74600 107.55200 97.21200  1.000 40.66271  ? 240 PHE A C   1 
ATOM   1554 O O   . PHE A 1 233 ? 108.71200 107.33900 96.57000  1.000 47.53034  ? 240 PHE A O   1 
ATOM   1555 C CB  . PHE A 1 233 ? 110.46200 109.88800 97.69100  1.000 19.67561  ? 240 PHE A CB  1 
ATOM   1556 C CG  . PHE A 1 233 ? 110.54400 111.03900 98.63500  1.000 24.44901  ? 240 PHE A CG  1 
ATOM   1557 C CD1 . PHE A 1 233 ? 109.41200 111.52500 99.24700  1.000 30.90803  ? 240 PHE A CD1 1 
ATOM   1558 C CD2 . PHE A 1 233 ? 111.74400 111.66300 98.87600  1.000 31.52344  ? 240 PHE A CD2 1 
ATOM   1559 C CE1 . PHE A 1 233 ? 109.48300 112.59200 100.09600 1.000 35.18042  ? 240 PHE A CE1 1 
ATOM   1560 C CE2 . PHE A 1 233 ? 111.81700 112.72900 99.72700  1.000 32.60117  ? 240 PHE A CE2 1 
ATOM   1561 C CZ  . PHE A 1 233 ? 110.68700 113.19300 100.33800 1.000 32.95018  ? 240 PHE A CZ  1 
ATOM   1562 N N   . GLY A 1 234 ? 110.84700 106.83700 97.03000  1.000 45.94908  ? 241 GLY A N   1 
ATOM   1563 C CA  . GLY A 1 234 ? 110.92900 105.82900 95.99600  1.000 39.34678  ? 241 GLY A CA  1 
ATOM   1564 C C   . GLY A 1 234 ? 111.41600 106.32500 94.65900  1.000 40.61207  ? 241 GLY A C   1 
ATOM   1565 O O   . GLY A 1 234 ? 111.23000 105.63100 93.65400  1.000 51.53139  ? 241 GLY A O   1 
ATOM   1566 N N   . ASP A 1 235 ? 112.03000 107.50700 94.61100  1.000 44.13748  ? 242 ASP A N   1 
ATOM   1567 C CA  . ASP A 1 235 ? 112.75900 107.92800 93.42000  1.000 51.55146  ? 242 ASP A CA  1 
ATOM   1568 C C   . ASP A 1 235 ? 114.02700 107.10300 93.23500  1.000 54.38382  ? 242 ASP A C   1 
ATOM   1569 O O   . ASP A 1 235 ? 114.34400 106.67400 92.12100  1.000 60.23577  ? 242 ASP A O   1 
ATOM   1570 C CB  . ASP A 1 235 ? 113.07800 109.42100 93.49300  1.000 49.14782  ? 242 ASP A CB  1 
ATOM   1571 C CG  . ASP A 1 235 ? 113.78100 109.80800 94.77200  1.000 55.78247  ? 242 ASP A CG  1 
ATOM   1572 O OD1 . ASP A 1 235 ? 113.86100 108.96500 95.68500  1.000 57.82997  ? 242 ASP A OD1 1 
ATOM   1573 O OD2 . ASP A 1 235 ? 114.25000 110.96000 94.86700  1.000 55.51733  ? 242 ASP A OD2 1 
ATOM   1574 N N   . LEU A 1 236 ? 114.76600 106.87800 94.31700  1.000 48.26308  ? 243 LEU A N   1 
ATOM   1575 C CA  . LEU A 1 236 ? 115.85400 105.91100 94.35900  1.000 49.50441  ? 243 LEU A CA  1 
ATOM   1576 C C   . LEU A 1 236 ? 115.42300 104.72300 95.20500  1.000 46.43669  ? 243 LEU A C   1 
ATOM   1577 O O   . LEU A 1 236 ? 114.91100 104.90300 96.31300  1.000 46.76618  ? 243 LEU A O   1 
ATOM   1578 C CB  . LEU A 1 236 ? 117.11000 106.54300 94.96000  1.000 44.26635  ? 243 LEU A CB  1 
ATOM   1579 C CG  . LEU A 1 236 ? 117.64200 107.83500 94.34700  1.000 43.44613  ? 243 LEU A CG  1 
ATOM   1580 C CD1 . LEU A 1 236 ? 118.85100 108.30900 95.11100  1.000 41.18896  ? 243 LEU A CD1 1 
ATOM   1581 C CD2 . LEU A 1 236 ? 117.98800 107.63200 92.89400  1.000 45.16623  ? 243 LEU A CD2 1 
ATOM   1582 N N   . VAL A 1 237 ? 115.63900 103.51500 94.69000  1.000 42.52684  ? 244 VAL A N   1 
ATOM   1583 C CA  . VAL A 1 237 ? 115.44900 102.29000 95.46000  1.000 37.87889  ? 244 VAL A CA  1 
ATOM   1584 C C   . VAL A 1 237 ? 116.62500 101.36400 95.19200  1.000 42.98882  ? 244 VAL A C   1 
ATOM   1585 O O   . VAL A 1 237 ? 116.97900 101.12200 94.03400  1.000 45.64965  ? 244 VAL A O   1 
ATOM   1586 C CB  . VAL A 1 237 ? 114.13000 101.58000 95.10200  1.000 41.24174  ? 244 VAL A CB  1 
ATOM   1587 C CG1 . VAL A 1 237 ? 113.94500 100.35900 95.96400  1.000 35.17157  ? 244 VAL A CG1 1 
ATOM   1588 C CG2 . VAL A 1 237 ? 112.95700 102.51100 95.26500  1.000 47.51273  ? 244 VAL A CG2 1 
ATOM   1589 N N   . SER A 1 238 ? 117.24000 100.86400 96.25800  1.000 40.54509  ? 245 SER A N   1 
ATOM   1590 C CA  . SER A 1 238 ? 118.32500 99.90500  96.15000  1.000 36.54596  ? 245 SER A CA  1 
ATOM   1591 C C   . SER A 1 238 ? 117.79700 98.50200  95.89200  1.000 43.11401  ? 245 SER A C   1 
ATOM   1592 O O   . SER A 1 238 ? 116.64200 98.18400  96.17700  1.000 51.58021  ? 245 SER A O   1 
ATOM   1593 C CB  . SER A 1 238 ? 119.15100 99.88700  97.42600  1.000 47.96610  ? 245 SER A CB  1 
ATOM   1594 O OG  . SER A 1 238 ? 118.35700 99.45000  98.51100  1.000 50.36125  ? 245 SER A OG  1 
ATOM   1595 N N   . SER A 1 239 ? 118.67900 97.65100  95.36500  1.000 58.57880  ? 246 SER A N   1 
ATOM   1596 C CA  . SER A 1 239 ? 118.40200 96.23200  95.13800  1.000 57.82638  ? 246 SER A CA  1 
ATOM   1597 C C   . SER A 1 239 ? 117.21600 96.04600  94.18900  1.000 60.11779  ? 246 SER A C   1 
ATOM   1598 O O   . SER A 1 239 ? 116.14600 95.56700  94.55800  1.000 63.78879  ? 246 SER A O   1 
ATOM   1599 C CB  . SER A 1 239 ? 118.17000 95.50000  96.46200  1.000 53.35641  ? 246 SER A CB  1 
ATOM   1600 O OG  . SER A 1 239 ? 117.92900 94.12500  96.23900  1.000 55.55263  ? 246 SER A OG  1 
ATOM   1601 N N   . GLN A 1 240 ? 117.44300 96.44700  92.94600  1.000 54.78307  ? 247 GLN A N   1 
ATOM   1602 C CA  . GLN A 1 240 ? 116.38700 96.46600  91.94000  1.000 50.74566  ? 247 GLN A CA  1 
ATOM   1603 C C   . GLN A 1 240 ? 116.81800 95.93200  90.58400  1.000 58.30087  ? 247 GLN A C   1 
ATOM   1604 O O   . GLN A 1 240 ? 115.97200 95.37900  89.87600  1.000 64.11765  ? 247 GLN A O   1 
ATOM   1605 C CB  . GLN A 1 240 ? 115.82800 97.87500  91.76300  1.000 54.41426  ? 247 GLN A CB  1 
ATOM   1606 C CG  . GLN A 1 240 ? 115.07400 98.36800  92.97100  1.000 58.59799  ? 247 GLN A CG  1 
ATOM   1607 C CD  . GLN A 1 240 ? 113.77600 97.63300  93.18200  1.000 51.49457  ? 247 GLN A CD  1 
ATOM   1608 O OE1 . GLN A 1 240 ? 112.76900 97.94300  92.55500  1.000 57.62937  ? 247 GLN A OE1 1 
ATOM   1609 N NE2 . GLN A 1 240 ? 113.78900 96.65500  94.07300  1.000 49.81307  ? 247 GLN A NE2 1 
ATOM   1610 N N   . ASN A 1 241 ? 118.08000 96.07500  90.19100  1.000 67.44404  ? 248 ASN A N   1 
ATOM   1611 C CA  . ASN A 1 241 ? 118.51600 95.57700  88.89700  1.000 64.48809  ? 248 ASN A CA  1 
ATOM   1612 C C   . ASN A 1 241 ? 118.30600 94.07200  88.81600  1.000 65.80026  ? 248 ASN A C   1 
ATOM   1613 O O   . ASN A 1 241 ? 118.27700 93.36900  89.82800  1.000 70.38313  ? 248 ASN A O   1 
ATOM   1614 C CB  . ASN A 1 241 ? 119.98500 95.91500  88.66100  1.000 64.42798  ? 248 ASN A CB  1 
ATOM   1615 C CG  . ASN A 1 241 ? 120.22600 97.39900  88.53900  1.000 70.67972  ? 248 ASN A CG  1 
ATOM   1616 O OD1 . ASN A 1 241 ? 119.29000 98.17900  88.38400  1.000 73.24112  ? 248 ASN A OD1 1 
ATOM   1617 N ND2 . ASN A 1 241 ? 121.48800 97.80100  88.60600  1.000 70.20272  ? 248 ASN A ND2 1 
ATOM   1618 N N   . ALA A 1 242 ? 118.14300 93.58100  87.59000  1.000 68.27163  ? 249 ALA A N   1 
ATOM   1619 C CA  . ALA A 1 242 ? 117.90100 92.16200  87.37800  1.000 71.50368  ? 249 ALA A CA  1 
ATOM   1620 C C   . ALA A 1 242 ? 119.05900 91.27900  87.81600  1.000 75.84469  ? 249 ALA A C   1 
ATOM   1621 O O   . ALA A 1 242 ? 118.83700 90.09900  88.10300  1.000 77.79506  ? 249 ALA A O   1 
ATOM   1622 C CB  . ALA A 1 242 ? 117.58900 91.90200  85.90600  1.000 75.59870  ? 249 ALA A CB  1 
ATOM   1623 N N   . HIS A 1 243 ? 120.28100 91.80200  87.88600  1.000 81.46063  ? 250 HIS A N   1 
ATOM   1624 C CA  . HIS A 1 243 ? 121.38900 90.95900  88.30700  1.000 77.68007  ? 250 HIS A CA  1 
ATOM   1625 C C   . HIS A 1 243 ? 122.43600 91.77300  89.05400  1.000 78.08441  ? 250 HIS A C   1 
ATOM   1626 O O   . HIS A 1 243 ? 122.68500 92.93800  88.73700  1.000 80.17326  ? 250 HIS A O   1 
ATOM   1627 C CB  . HIS A 1 243 ? 122.01000 90.26300  87.08900  1.000 74.59756  ? 250 HIS A CB  1 
ATOM   1628 C CG  . HIS A 1 243 ? 123.07900 89.27300  87.42900  1.000 79.30286  ? 250 HIS A CG  1 
ATOM   1629 N ND1 . HIS A 1 243 ? 124.38500 89.64000  87.66700  1.000 83.24454  ? 250 HIS A ND1 1 
ATOM   1630 C CD2 . HIS A 1 243 ? 123.03500 87.92700  87.56300  1.000 83.14018  ? 250 HIS A CD2 1 
ATOM   1631 C CE1 . HIS A 1 243 ? 125.10000 88.56300  87.93700  1.000 81.45538  ? 250 HIS A CE1 1 
ATOM   1632 N NE2 . HIS A 1 243 ? 124.30400 87.51000  87.88100  1.000 83.93655  ? 250 HIS A NE2 1 
ATOM   1633 N N   . TYR A 1 244 ? 123.05900 91.13000  90.04100  1.000 69.31354  ? 251 TYR A N   1 
ATOM   1634 C CA  . TYR A 1 244 ? 124.22000 91.66100  90.73800  1.000 69.33980  ? 251 TYR A CA  1 
ATOM   1635 C C   . TYR A 1 244 ? 125.20300 90.52700  90.98400  1.000 75.04413  ? 251 TYR A C   1 
ATOM   1636 O O   . TYR A 1 244 ? 124.84100 89.34900  90.96500  1.000 75.79007  ? 251 TYR A O   1 
ATOM   1637 C CB  . TYR A 1 244 ? 123.88100 92.29400  92.09600  1.000 68.59871  ? 251 TYR A CB  1 
ATOM   1638 C CG  . TYR A 1 244 ? 122.94800 93.47100  92.06600  1.000 69.54371  ? 251 TYR A CG  1 
ATOM   1639 C CD1 . TYR A 1 244 ? 123.41500 94.73200  91.74600  1.000 72.60252  ? 251 TYR A CD1 1 
ATOM   1640 C CD2 . TYR A 1 244 ? 121.61900 93.33700  92.41700  1.000 68.11525  ? 251 TYR A CD2 1 
ATOM   1641 C CE1 . TYR A 1 244 ? 122.58200 95.81700  91.74700  1.000 68.36047  ? 251 TYR A CE1 1 
ATOM   1642 C CE2 . TYR A 1 244 ? 120.77400 94.41700  92.41100  1.000 69.65892  ? 251 TYR A CE2 1 
ATOM   1643 C CZ  . TYR A 1 244 ? 121.26400 95.65600  92.07700  1.000 69.17356  ? 251 TYR A CZ  1 
ATOM   1644 O OH  . TYR A 1 244 ? 120.42900 96.74400  92.05100  1.000 71.00935  ? 251 TYR A OH  1 
ATOM   1645 N N   . GLU A 1 245 ? 126.46100 90.89500  91.19900  1.000 83.45228  ? 252 GLU A N   1 
ATOM   1646 C CA  . GLU A 1 245 ? 127.42200 89.95000  91.74700  1.000 82.44322  ? 252 GLU A CA  1 
ATOM   1647 C C   . GLU A 1 245 ? 127.06400 89.61900  93.19200  1.000 83.49296  ? 252 GLU A C   1 
ATOM   1648 O O   . GLU A 1 245 ? 126.79200 90.51800  93.99300  1.000 83.46334  ? 252 GLU A O   1 
ATOM   1649 C CB  . GLU A 1 245 ? 128.83500 90.52400  91.66300  1.000 80.41018  ? 252 GLU A CB  1 
ATOM   1650 N N   . SER A 1 246 ? 127.07400 88.32600  93.52500  1.000 79.85847  ? 253 SER A N   1 
ATOM   1651 C CA  . SER A 1 246 ? 126.79200 87.85100  94.88200  1.000 79.11358  ? 253 SER A CA  1 
ATOM   1652 C C   . SER A 1 246 ? 125.43700 88.34000  95.39700  1.000 78.78383  ? 253 SER A C   1 
ATOM   1653 O O   . SER A 1 246 ? 125.34300 88.94100  96.46800  1.000 79.97381  ? 253 SER A O   1 
ATOM   1654 C CB  . SER A 1 246 ? 127.91400 88.25400  95.83900  1.000 79.23514  ? 253 SER A CB  1 
ATOM   1655 O OG  . SER A 1 246 ? 129.16500 87.76800  95.39100  1.000 81.34854  ? 253 SER A OG  1 
ATOM   1656 N N   . GLN A 1 247 ? 124.38500 88.09300  94.61000  1.000 77.28863  ? 254 GLN A N   1 
ATOM   1657 C CA  . GLN A 1 247 ? 123.06500 88.65200  94.90200  1.000 73.77588  ? 254 GLN A CA  1 
ATOM   1658 C C   . GLN A 1 247 ? 122.64000 88.40600  96.34300  1.000 74.64450  ? 254 GLN A C   1 
ATOM   1659 O O   . GLN A 1 247 ? 122.10600 89.30100  97.00300  1.000 75.32876  ? 254 GLN A O   1 
ATOM   1660 C CB  . GLN A 1 247 ? 122.01900 88.06700  93.95600  1.000 71.08369  ? 254 GLN A CB  1 
ATOM   1661 C CG  . GLN A 1 247 ? 122.17600 88.46300  92.51200  1.000 76.22765  ? 254 GLN A CG  1 
ATOM   1662 C CD  . GLN A 1 247 ? 120.86400 88.41700  91.76300  1.000 79.21044  ? 254 GLN A CD  1 
ATOM   1663 O OE1 . GLN A 1 247 ? 119.86700 88.98500  92.20400  1.000 79.31682  ? 254 GLN A OE1 1 
ATOM   1664 N NE2 . GLN A 1 247 ? 120.85400 87.73300  90.62700  1.000 77.56767  ? 254 GLN A NE2 1 
ATOM   1665 N N   . GLY A 1 248 ? 122.82600 87.18200  96.83200  1.000 75.94893  ? 255 GLY A N   1 
ATOM   1666 C CA  . GLY A 1 248 ? 122.38100 86.85700  98.17900  1.000 74.07661  ? 255 GLY A CA  1 
ATOM   1667 C C   . GLY A 1 248 ? 123.05900 87.68300  99.25600  1.000 72.19624  ? 255 GLY A C   1 
ATOM   1668 O O   . GLY A 1 248 ? 122.40300 88.22200  100.15100 1.000 73.68500  ? 255 GLY A O   1 
ATOM   1669 N N   . LEU A 1 249 ? 124.38100 87.81900  99.16500  1.000 70.22842  ? 256 LEU A N   1 
ATOM   1670 C CA  . LEU A 1 249 ? 125.10700 88.65500  100.11500 1.000 71.83908  ? 256 LEU A CA  1 
ATOM   1671 C C   . LEU A 1 249 ? 124.68400 90.11500  100.02300 1.000 70.72201  ? 256 LEU A C   1 
ATOM   1672 O O   . LEU A 1 249 ? 124.54200 90.78900  101.04800 1.000 69.39317  ? 256 LEU A O   1 
ATOM   1673 C CB  . LEU A 1 249 ? 126.61000 88.51800  99.88900  1.000 68.90389  ? 256 LEU A CB  1 
ATOM   1674 C CG  . LEU A 1 249 ? 127.50200 89.40000  100.76100 1.000 67.86883  ? 256 LEU A CG  1 
ATOM   1675 C CD1 . LEU A 1 249 ? 127.29000 89.08200  102.22300 1.000 70.14534  ? 256 LEU A CD1 1 
ATOM   1676 C CD2 . LEU A 1 249 ? 128.95700 89.21300  100.38300 1.000 69.00698  ? 256 LEU A CD2 1 
ATOM   1677 N N   . TYR A 1 250 ? 124.48400 90.62500  98.81000  1.000 67.32848  ? 257 TYR A N   1 
ATOM   1678 C CA  . TYR A 1 250 ? 124.05900 92.01200  98.66900  1.000 59.92020  ? 257 TYR A CA  1 
ATOM   1679 C C   . TYR A 1 250 ? 122.66600 92.24700  99.23700  1.000 62.07328  ? 257 TYR A C   1 
ATOM   1680 O O   . TYR A 1 250 ? 122.43900 93.24900  99.91800  1.000 74.28217  ? 257 TYR A O   1 
ATOM   1681 C CB  . TYR A 1 250 ? 124.10300 92.43800  97.20700  1.000 61.30715  ? 257 TYR A CB  1 
ATOM   1682 C CG  . TYR A 1 250 ? 123.66900 93.86500  97.00400  1.000 65.83341  ? 257 TYR A CG  1 
ATOM   1683 C CD1 . TYR A 1 250 ? 124.30100 94.90000  97.66100  1.000 66.50879  ? 257 TYR A CD1 1 
ATOM   1684 C CD2 . TYR A 1 250 ? 122.60900 94.17200  96.17400  1.000 66.60126  ? 257 TYR A CD2 1 
ATOM   1685 C CE1 . TYR A 1 250 ? 123.90900 96.20000  97.47400  1.000 62.81858  ? 257 TYR A CE1 1 
ATOM   1686 C CE2 . TYR A 1 250 ? 122.20500 95.46900  95.99100  1.000 61.46943  ? 257 TYR A CE2 1 
ATOM   1687 C CZ  . TYR A 1 250 ? 122.85900 96.47800  96.64000  1.000 61.61457  ? 257 TYR A CZ  1 
ATOM   1688 O OH  . TYR A 1 250 ? 122.44600 97.77300  96.46400  1.000 67.67430  ? 257 TYR A OH  1 
ATOM   1689 N N   . ARG A 1 251 ? 121.71500 91.35700  98.95500  1.000 59.12261  ? 258 ARG A N   1 
ATOM   1690 C CA  . ARG A 1 251 ? 120.38900 91.47700  99.55400  1.000 64.74800  ? 258 ARG A CA  1 
ATOM   1691 C C   . ARG A 1 251 ? 120.42800 91.39600  101.07500 1.000 67.22216  ? 258 ARG A C   1 
ATOM   1692 O O   . ARG A 1 251 ? 119.74000 92.16200  101.76100 1.000 65.02776  ? 258 ARG A O   1 
ATOM   1693 C CB  . ARG A 1 251 ? 119.45100 90.41600  98.99100  1.000 63.96608  ? 258 ARG A CB  1 
ATOM   1694 C CG  . ARG A 1 251 ? 119.09100 90.62100  97.53900  1.000 63.03845  ? 258 ARG A CG  1 
ATOM   1695 C CD  . ARG A 1 251 ? 118.20800 89.49900  97.04200  1.000 67.33435  ? 258 ARG A CD  1 
ATOM   1696 N NE  . ARG A 1 251 ? 118.14500 89.45200  95.58800  1.000 72.13267  ? 258 ARG A NE  1 
ATOM   1697 C CZ  . ARG A 1 251 ? 117.65800 88.43300  94.89600  1.000 72.23082  ? 258 ARG A CZ  1 
ATOM   1698 N NH1 . ARG A 1 251 ? 117.19300 87.35000  95.49600  1.000 71.33352  ? 258 ARG A NH1 1 
ATOM   1699 N NH2 . ARG A 1 251 ? 117.63600 88.50100  93.56800  1.000 66.95162  ? 258 ARG A NH2 1 
ATOM   1700 N N   . PHE A 1 252 ? 121.22800 90.48500  101.62700 1.000 64.60213  ? 259 PHE A N   1 
ATOM   1701 C CA  . PHE A 1 252 ? 121.34900 90.40600  103.08000 1.000 60.21842  ? 259 PHE A CA  1 
ATOM   1702 C C   . PHE A 1 252 ? 121.94400 91.67900  103.67100 1.000 61.52165  ? 259 PHE A C   1 
ATOM   1703 O O   . PHE A 1 252 ? 121.45700 92.19400  104.68500 1.000 64.56965  ? 259 PHE A O   1 
ATOM   1704 C CB  . PHE A 1 252 ? 122.19100 89.19300  103.46700 1.000 60.19917  ? 259 PHE A CB  1 
ATOM   1705 C CG  . PHE A 1 252 ? 122.43100 89.07400  104.93800 1.000 63.96423  ? 259 PHE A CG  1 
ATOM   1706 C CD1 . PHE A 1 252 ? 121.42200 88.65400  105.78100 1.000 63.62856  ? 259 PHE A CD1 1 
ATOM   1707 C CD2 . PHE A 1 252 ? 123.66300 89.38100  105.47800 1.000 64.48409  ? 259 PHE A CD2 1 
ATOM   1708 C CE1 . PHE A 1 252 ? 121.63600 88.54300  107.13300 1.000 65.25437  ? 259 PHE A CE1 1 
ATOM   1709 C CE2 . PHE A 1 252 ? 123.88300 89.27200  106.83000 1.000 63.11451  ? 259 PHE A CE2 1 
ATOM   1710 C CZ  . PHE A 1 252 ? 122.86800 88.85200  107.65800 1.000 65.52309  ? 259 PHE A CZ  1 
ATOM   1711 N N   . ALA A 1 253 ? 123.01300 92.19200  103.06300 1.000 54.76844  ? 260 ALA A N   1 
ATOM   1712 C CA  . ALA A 1 253 ? 123.60200 93.44200  103.52700 1.000 51.51544  ? 260 ALA A CA  1 
ATOM   1713 C C   . ALA A 1 253 ? 122.63800 94.61400  103.41000 1.000 51.12210  ? 260 ALA A C   1 
ATOM   1714 O O   . ALA A 1 253 ? 122.59400 95.47300  104.29300 1.000 55.02691  ? 260 ALA A O   1 
ATOM   1715 C CB  . ALA A 1 253 ? 124.88400 93.73000  102.75100 1.000 49.75301  ? 260 ALA A CB  1 
ATOM   1716 N N   . ASN A 1 254 ? 121.85200 94.66900  102.33700 1.000 49.82078  ? 261 ASN A N   1 
ATOM   1717 C CA  . ASN A 1 254 ? 120.84000 95.71400  102.21800 1.000 48.14482  ? 261 ASN A CA  1 
ATOM   1718 C C   . ASN A 1 254 ? 119.77200 95.61700  103.30000 1.000 54.43854  ? 261 ASN A C   1 
ATOM   1719 O O   . ASN A 1 254 ? 119.38900 96.63300  103.89100 1.000 57.64407  ? 261 ASN A O   1 
ATOM   1720 C CB  . ASN A 1 254 ? 120.19800 95.65700  100.83700 1.000 47.90741  ? 261 ASN A CB  1 
ATOM   1721 C CG  . ASN A 1 254 ? 119.29800 96.83200  100.57300 1.000 56.20384  ? 261 ASN A CG  1 
ATOM   1722 O OD1 . ASN A 1 254 ? 119.70100 97.98000  100.72100 1.000 60.22643  ? 261 ASN A OD1 1 
ATOM   1723 N ND2 . ASN A 1 254 ? 118.06800 96.55300  100.17900 1.000 61.23511  ? 261 ASN A ND2 1 
ATOM   1724 N N   . PHE A 1 255 ? 119.31100 94.40500  103.60700 1.000 47.21232  ? 262 PHE A N   1 
ATOM   1725 C CA  . PHE A 1 255 ? 118.35800 94.22700  104.70000 1.000 46.00222  ? 262 PHE A CA  1 
ATOM   1726 C C   . PHE A 1 255 ? 118.93600 94.68300  106.03400 1.000 52.40935  ? 262 PHE A C   1 
ATOM   1727 O O   . PHE A 1 255 ? 118.29900 95.44500  106.77200 1.000 55.04063  ? 262 PHE A O   1 
ATOM   1728 C CB  . PHE A 1 255 ? 117.92300 92.76500  104.77300 1.000 54.22347  ? 262 PHE A CB  1 
ATOM   1729 C CG  . PHE A 1 255 ? 117.00100 92.45500  105.91700 1.000 55.99199  ? 262 PHE A CG  1 
ATOM   1730 C CD1 . PHE A 1 255 ? 115.89300 93.23600  106.16400 1.000 49.03954  ? 262 PHE A CD1 1 
ATOM   1731 C CD2 . PHE A 1 255 ? 117.23000 91.36200  106.72800 1.000 55.75546  ? 262 PHE A CD2 1 
ATOM   1732 C CE1 . PHE A 1 255 ? 115.04200 92.94400  107.20400 1.000 48.74489  ? 262 PHE A CE1 1 
ATOM   1733 C CE2 . PHE A 1 255 ? 116.38200 91.07000  107.76900 1.000 55.00539  ? 262 PHE A CE2 1 
ATOM   1734 C CZ  . PHE A 1 255 ? 115.28700 91.86300  108.00600 1.000 53.30905  ? 262 PHE A CZ  1 
ATOM   1735 N N   . VAL A 1 256 ? 120.15300 94.24200  106.34900 1.000 48.59643  ? 263 VAL A N   1 
ATOM   1736 C CA  . VAL A 1 256 ? 120.79400 94.61200  107.61000 1.000 35.43897  ? 263 VAL A CA  1 
ATOM   1737 C C   . VAL A 1 256 ? 121.00600 96.12000  107.71000 1.000 39.47650  ? 263 VAL A C   1 
ATOM   1738 O O   . VAL A 1 256 ? 120.72800 96.73000  108.74900 1.000 49.72112  ? 263 VAL A O   1 
ATOM   1739 C CB  . VAL A 1 256 ? 122.11800 93.85100  107.77600 1.000 38.36639  ? 263 VAL A CB  1 
ATOM   1740 C CG1 . VAL A 1 256 ? 122.88000 94.39000  108.95400 1.000 45.19067  ? 263 VAL A CG1 1 
ATOM   1741 C CG2 . VAL A 1 256 ? 121.85100 92.38000  107.95800 1.000 44.51269  ? 263 VAL A CG2 1 
ATOM   1742 N N   . PHE A 1 257 ? 121.51100 96.74700  106.64600 1.000 40.93014  ? 264 PHE A N   1 
ATOM   1743 C CA  . PHE A 1 257 ? 121.75200 98.18500  106.70300 1.000 38.61909  ? 264 PHE A CA  1 
ATOM   1744 C C   . PHE A 1 257 ? 120.46600 98.99000  106.80800 1.000 42.36788  ? 264 PHE A C   1 
ATOM   1745 O O   . PHE A 1 257 ? 120.40700 99.94700  107.58500 1.000 49.16325  ? 264 PHE A O   1 
ATOM   1746 C CB  . PHE A 1 257 ? 122.56500 98.65100  105.49800 1.000 44.36001  ? 264 PHE A CB  1 
ATOM   1747 C CG  . PHE A 1 257 ? 124.02900 98.36000  105.61300 1.000 49.96282  ? 264 PHE A CG  1 
ATOM   1748 C CD1 . PHE A 1 257 ? 124.76600 98.89600  106.64900 1.000 45.72830  ? 264 PHE A CD1 1 
ATOM   1749 C CD2 . PHE A 1 257 ? 124.67400 97.57900  104.68000 1.000 44.89749  ? 264 PHE A CD2 1 
ATOM   1750 C CE1 . PHE A 1 257 ? 126.10800 98.63800  106.76500 1.000 40.94995  ? 264 PHE A CE1 1 
ATOM   1751 C CE2 . PHE A 1 257 ? 126.01900 97.32000  104.79200 1.000 42.61347  ? 264 PHE A CE2 1 
ATOM   1752 C CZ  . PHE A 1 257 ? 126.73500 97.85100  105.83400 1.000 46.17192  ? 264 PHE A CZ  1 
ATOM   1753 N N   . ILE A 1 258 ? 119.41400 98.61700  106.07800 1.000 41.26416  ? 265 ILE A N   1 
ATOM   1754 C CA  . ILE A 1 258 ? 118.16300 99.36000  106.21700 1.000 33.02192  ? 265 ILE A CA  1 
ATOM   1755 C C   . ILE A 1 258 ? 117.56300 99.17600  107.60500 1.000 35.39180  ? 265 ILE A C   1 
ATOM   1756 O O   . ILE A 1 258 ? 117.05200 100.13100 108.19800 1.000 42.37047  ? 265 ILE A O   1 
ATOM   1757 C CB  . ILE A 1 258 ? 117.16200 98.97500  105.11700 1.000 40.04823  ? 265 ILE A CB  1 
ATOM   1758 C CG1 . ILE A 1 258 ? 117.74100 99.26500  103.73500 1.000 40.12297  ? 265 ILE A CG1 1 
ATOM   1759 C CG2 . ILE A 1 258 ? 115.87900 99.75000  105.29500 1.000 45.60524  ? 265 ILE A CG2 1 
ATOM   1760 C CD1 . ILE A 1 258 ? 117.69300 100.71400 103.35300 1.000 41.14216  ? 265 ILE A CD1 1 
ATOM   1761 N N   . LEU A 1 259 ? 117.63600 97.96800  108.16400 1.000 36.63721  ? 266 LEU A N   1 
ATOM   1762 C CA  . LEU A 1 259 ? 117.12300 97.76100  109.51500 1.000 34.79553  ? 266 LEU A CA  1 
ATOM   1763 C C   . LEU A 1 259 ? 117.88600 98.57900  110.55400 1.000 41.79334  ? 266 LEU A C   1 
ATOM   1764 O O   . LEU A 1 259 ? 117.27900 99.27900  111.37800 1.000 50.95732  ? 266 LEU A O   1 
ATOM   1765 C CB  . LEU A 1 259 ? 117.17600 96.27900  109.86300 1.000 34.32510  ? 266 LEU A CB  1 
ATOM   1766 C CG  . LEU A 1 259 ? 116.76500 95.95100  111.28500 1.000 34.24761  ? 266 LEU A CG  1 
ATOM   1767 C CD1 . LEU A 1 259 ? 115.34300 96.38000  111.50000 1.000 37.04558  ? 266 LEU A CD1 1 
ATOM   1768 C CD2 . LEU A 1 259 ? 116.92200 94.47200  111.52800 1.000 39.54128  ? 266 LEU A CD2 1 
ATOM   1769 N N   . MET A 1 260 ? 119.21900 98.51900  110.52500 1.000 50.10386  ? 267 MET A N   1 
ATOM   1770 C CA  . MET A 1 260 ? 120.00600 99.28200  111.48800 1.000 46.07372  ? 267 MET A CA  1 
ATOM   1771 C C   . MET A 1 260 ? 119.78100 100.77600 111.32900 1.000 48.03389  ? 267 MET A C   1 
ATOM   1772 O O   . MET A 1 260 ? 119.64700 101.50200 112.32200 1.000 58.34968  ? 267 MET A O   1 
ATOM   1773 C CB  . MET A 1 260 ? 121.48500 98.95400  111.31900 1.000 48.76735  ? 267 MET A CB  1 
ATOM   1774 C CG  . MET A 1 260 ? 121.88300 97.57600  111.79300 1.000 51.70485  ? 267 MET A CG  1 
ATOM   1775 S SD  . MET A 1 260 ? 123.58300 97.19700  111.34200 1.000 73.13117  ? 267 MET A SD  1 
ATOM   1776 C CE  . MET A 1 260 ? 124.46400 98.43000  112.28700 1.000 57.90445  ? 267 MET A CE  1 
ATOM   1777 N N   . GLY A 1 261 ? 119.69900 101.24800 110.09000 1.000 38.10336  ? 268 GLY A N   1 
ATOM   1778 C CA  . GLY A 1 261 ? 119.46700 102.66000 109.86100 1.000 38.05335  ? 268 GLY A CA  1 
ATOM   1779 C C   . GLY A 1 261 ? 118.12200 103.13400 110.36600 1.000 30.61045  ? 268 GLY A C   1 
ATOM   1780 O O   . GLY A 1 261 ? 118.02300 104.18300 111.00200 1.000 34.70617  ? 268 GLY A O   1 
ATOM   1781 N N   . VAL A 1 262 ? 117.06100 102.38600 110.06000 1.000 24.27628  ? 269 VAL A N   1 
ATOM   1782 C CA  . VAL A 1 262 ? 115.73800 102.77300 110.53600 1.000 20.31005  ? 269 VAL A CA  1 
ATOM   1783 C C   . VAL A 1 262 ? 115.69300 102.81000 112.05500 1.000 34.07774  ? 269 VAL A C   1 
ATOM   1784 O O   . VAL A 1 262 ? 115.19100 103.77200 112.64200 1.000 47.13475  ? 269 VAL A O   1 
ATOM   1785 C CB  . VAL A 1 262 ? 114.66200 101.83200 109.96900 1.000 18.39141  ? 269 VAL A CB  1 
ATOM   1786 C CG1 . VAL A 1 262 ? 113.33900 102.13700 110.59800 1.000 27.90750  ? 269 VAL A CG1 1 
ATOM   1787 C CG2 . VAL A 1 262 ? 114.55200 102.00000 108.48300 1.000 37.63447  ? 269 VAL A CG2 1 
ATOM   1788 N N   . CYS A 1 263 ? 116.24300 101.79300 112.72000 1.000 47.80971  ? 270 CYS A N   1 
ATOM   1789 C CA  . CYS A 1 263 ? 116.20900 101.79900 114.18200 1.000 37.97883  ? 270 CYS A CA  1 
ATOM   1790 C C   . CYS A 1 263 ? 117.01900 102.94500 114.78800 1.000 44.82931  ? 270 CYS A C   1 
ATOM   1791 O O   . CYS A 1 263 ? 116.53900 103.62700 115.70400 1.000 53.50559  ? 270 CYS A O   1 
ATOM   1792 C CB  . CYS A 1 263 ? 116.69900 100.45900 114.71800 1.000 42.23643  ? 270 CYS A CB  1 
ATOM   1793 S SG  . CYS A 1 263 ? 115.69100 99.05600  114.20700 1.000 60.74859  ? 270 CYS A SG  1 
ATOM   1794 N N   . CYS A 1 264 ? 118.17200 103.27600 114.20200 1.000 50.48661  ? 271 CYS A N   1 
ATOM   1795 C CA  . CYS A 1 264 ? 118.97000 104.38600 114.72600 1.000 42.72016  ? 271 CYS A CA  1 
ATOM   1796 C C   . CYS A 1 264 ? 118.33000 105.74600 114.47500 1.000 49.63689  ? 271 CYS A C   1 
ATOM   1797 O O   . CYS A 1 264 ? 118.26400 106.57900 115.38400 1.000 61.03012  ? 271 CYS A O   1 
ATOM   1798 C CB  . CYS A 1 264 ? 120.38100 104.34500 114.15000 1.000 48.88126  ? 271 CYS A CB  1 
ATOM   1799 S SG  . CYS A 1 264 ? 121.35000 102.95400 114.74900 1.000 70.55971  ? 271 CYS A SG  1 
ATOM   1800 N N   . ILE A 1 265 ? 117.86000 106.01000 113.25900 1.000 45.81183  ? 272 ILE A N   1 
ATOM   1801 C CA  . ILE A 1 265 ? 117.28200 107.32600 112.99600 1.000 40.10160  ? 272 ILE A CA  1 
ATOM   1802 C C   . ILE A 1 265 ? 115.92100 107.49300 113.66900 1.000 41.10278  ? 272 ILE A C   1 
ATOM   1803 O O   . ILE A 1 265 ? 115.58300 108.59300 114.11300 1.000 56.52598  ? 272 ILE A O   1 
ATOM   1804 C CB  . ILE A 1 265 ? 117.23700 107.62500 111.49000 1.000 35.39772  ? 272 ILE A CB  1 
ATOM   1805 C CG1 . ILE A 1 265 ? 118.66000 107.80800 110.97500 1.000 41.22393  ? 272 ILE A CG1 1 
ATOM   1806 C CG2 . ILE A 1 265 ? 116.46700 108.87800 111.21500 1.000 39.82460  ? 272 ILE A CG2 1 
ATOM   1807 C CD1 . ILE A 1 265 ? 118.74900 108.50400 109.64900 1.000 37.06581  ? 272 ILE A CD1 1 
ATOM   1808 N N   . TYR A 1 266 ? 115.11100 106.44100 113.76300 1.000 40.57747  ? 273 TYR A N   1 
ATOM   1809 C CA  . TYR A 1 266 ? 113.88600 106.56400 114.54900 1.000 44.14311  ? 273 TYR A CA  1 
ATOM   1810 C C   . TYR A 1 266 ? 114.17500 106.80500 116.03300 1.000 48.81508  ? 273 TYR A C   1 
ATOM   1811 O O   . TYR A 1 266 ? 113.46900 107.58400 116.69200 1.000 56.03203  ? 273 TYR A O   1 
ATOM   1812 C CB  . TYR A 1 266 ? 113.03200 105.31600 114.36300 1.000 49.63431  ? 273 TYR A CB  1 
ATOM   1813 C CG  . TYR A 1 266 ? 111.67400 105.39400 115.00700 1.000 52.66618  ? 273 TYR A CG  1 
ATOM   1814 C CD1 . TYR A 1 266 ? 110.60400 105.97200 114.34300 1.000 55.69227  ? 273 TYR A CD1 1 
ATOM   1815 C CD2 . TYR A 1 266 ? 111.45800 104.88100 116.27700 1.000 53.63699  ? 273 TYR A CD2 1 
ATOM   1816 C CE1 . TYR A 1 266 ? 109.35800 106.04300 114.93000 1.000 55.21340  ? 273 TYR A CE1 1 
ATOM   1817 C CE2 . TYR A 1 266 ? 110.21700 104.94600 116.87000 1.000 54.45822  ? 273 TYR A CE2 1 
ATOM   1818 C CZ  . TYR A 1 266 ? 109.17100 105.52800 116.19400 1.000 61.02922  ? 273 TYR A CZ  1 
ATOM   1819 O OH  . TYR A 1 266 ? 107.93200 105.59300 116.78300 1.000 65.17307  ? 273 TYR A OH  1 
ATOM   1820 N N   . SER A 1 267 ? 115.24100 106.20100 116.56800 1.000 45.50383  ? 274 SER A N   1 
ATOM   1821 C CA  . SER A 1 267 ? 115.66800 106.55500 117.91900 1.000 43.16155  ? 274 SER A CA  1 
ATOM   1822 C C   . SER A 1 267 ? 116.09200 108.01500 118.01600 1.000 49.40526  ? 274 SER A C   1 
ATOM   1823 O O   . SER A 1 267 ? 115.77900 108.70000 119.00000 1.000 55.98756  ? 274 SER A O   1 
ATOM   1824 C CB  . SER A 1 267 ? 116.80700 105.64200 118.35700 1.000 44.82596  ? 274 SER A CB  1 
ATOM   1825 O OG  . SER A 1 267 ? 116.36500 104.30100 118.42800 1.000 51.30956  ? 274 SER A OG  1 
ATOM   1826 N N   . LEU A 1 268 ? 116.80800 108.50900 117.00700 1.000 41.97340  ? 275 LEU A N   1 
ATOM   1827 C CA  . LEU A 1 268 ? 117.20100 109.91400 116.99000 1.000 38.35382  ? 275 LEU A CA  1 
ATOM   1828 C C   . LEU A 1 268 ? 115.99200 110.84000 116.94100 1.000 47.54650  ? 275 LEU A C   1 
ATOM   1829 O O   . LEU A 1 268 ? 115.98300 111.89400 117.58400 1.000 61.48204  ? 275 LEU A O   1 
ATOM   1830 C CB  . LEU A 1 268 ? 118.11800 110.17200 115.80000 1.000 29.87441  ? 275 LEU A CB  1 
ATOM   1831 C CG  . LEU A 1 268 ? 118.65400 111.58500 115.65000 1.000 41.53198  ? 275 LEU A CG  1 
ATOM   1832 C CD1 . LEU A 1 268 ? 119.48800 111.94000 116.85100 1.000 46.57179  ? 275 LEU A CD1 1 
ATOM   1833 C CD2 . LEU A 1 268 ? 119.47000 111.69200 114.38700 1.000 47.32717  ? 275 LEU A CD2 1 
ATOM   1834 N N   . PHE A 1 269 ? 114.96300 110.46400 116.18400 1.000 37.99036  ? 276 PHE A N   1 
ATOM   1835 C CA  . PHE A 1 269 ? 113.73300 111.24900 116.14700 1.000 30.61611  ? 276 PHE A CA  1 
ATOM   1836 C C   . PHE A 1 269 ? 113.05400 111.30300 117.50700 1.000 37.02266  ? 276 PHE A C   1 
ATOM   1837 O O   . PHE A 1 269 ? 112.61700 112.36900 117.94600 1.000 48.17146  ? 276 PHE A O   1 
ATOM   1838 C CB  . PHE A 1 269 ? 112.76800 110.70200 115.09800 1.000 36.73543  ? 276 PHE A CB  1 
ATOM   1839 C CG  . PHE A 1 269 ? 113.19500 110.95300 113.68700 1.000 36.07326  ? 276 PHE A CG  1 
ATOM   1840 C CD1 . PHE A 1 269 ? 114.33200 111.68100 113.41000 1.000 36.32868  ? 276 PHE A CD1 1 
ATOM   1841 C CD2 . PHE A 1 269 ? 112.44400 110.47600 112.63700 1.000 32.21695  ? 276 PHE A CD2 1 
ATOM   1842 C CE1 . PHE A 1 269 ? 114.71400 111.91500 112.11700 1.000 36.72462  ? 276 PHE A CE1 1 
ATOM   1843 C CE2 . PHE A 1 269 ? 112.82500 110.71000 111.34600 1.000 39.14827  ? 276 PHE A CE2 1 
ATOM   1844 C CZ  . PHE A 1 269 ? 113.96100 111.42900 111.08600 1.000 38.63245  ? 276 PHE A CZ  1 
ATOM   1845 N N   . ASN A 1 270 ? 112.96100 110.16800 118.19700 1.000 44.41244  ? 277 ASN A N   1 
ATOM   1846 C CA  . ASN A 1 270 ? 112.40800 110.19000 119.55300 1.000 44.43977  ? 277 ASN A CA  1 
ATOM   1847 C C   . ASN A 1 270 ? 113.21200 111.08900 120.49400 1.000 45.51921  ? 277 ASN A C   1 
ATOM   1848 O O   . ASN A 1 270 ? 112.64200 111.90100 121.24000 1.000 52.28608  ? 277 ASN A O   1 
ATOM   1849 C CB  . ASN A 1 270 ? 112.32800 108.77300 120.10800 1.000 44.31752  ? 277 ASN A CB  1 
ATOM   1850 C CG  . ASN A 1 270 ? 111.13300 108.01800 119.58700 1.000 50.16151  ? 277 ASN A CG  1 
ATOM   1851 O OD1 . ASN A 1 270 ? 110.38300 108.52100 118.75600 1.000 50.07866  ? 277 ASN A OD1 1 
ATOM   1852 N ND2 . ASN A 1 270 ? 110.94300 106.80300 120.07600 1.000 54.09601  ? 277 ASN A ND2 1 
ATOM   1853 N N   . VAL A 1 271 ? 114.53700 110.95800 120.48300 1.000 42.21164  ? 278 VAL A N   1 
ATOM   1854 C CA  . VAL A 1 271 ? 115.36600 111.75200 121.39100 1.000 42.96367  ? 278 VAL A CA  1 
ATOM   1855 C C   . VAL A 1 271 ? 115.25900 113.25000 121.09700 1.000 52.75321  ? 278 VAL A C   1 
ATOM   1856 O O   . VAL A 1 271 ? 115.11500 114.07400 122.01800 1.000 63.78548  ? 278 VAL A O   1 
ATOM   1857 C CB  . VAL A 1 271 ? 116.82100 111.26600 121.32100 1.000 46.30151  ? 278 VAL A CB  1 
ATOM   1858 C CG1 . VAL A 1 271 ? 117.73800 112.28400 121.93000 1.000 52.50526  ? 278 VAL A CG1 1 
ATOM   1859 C CG2 . VAL A 1 271 ? 116.96000 109.93700 122.02200 1.000 51.99868  ? 278 VAL A CG2 1 
ATOM   1860 N N   . ILE A 1 272 ? 115.29500 113.63500 119.82000 1.000 41.40766  ? 279 ILE A N   1 
ATOM   1861 C CA  . ILE A 1 272 ? 115.08800 115.04200 119.49200 1.000 37.18385  ? 279 ILE A CA  1 
ATOM   1862 C C   . ILE A 1 272 ? 113.69000 115.49600 119.89300 1.000 40.67105  ? 279 ILE A C   1 
ATOM   1863 O O   . ILE A 1 272 ? 113.49800 116.64400 120.30000 1.000 43.08480  ? 279 ILE A O   1 
ATOM   1864 C CB  . ILE A 1 272 ? 115.36700 115.30200 118.00200 1.000 33.52473  ? 279 ILE A CB  1 
ATOM   1865 C CG1 . ILE A 1 272 ? 116.84500 115.11500 117.70100 1.000 38.66663  ? 279 ILE A CG1 1 
ATOM   1866 C CG2 . ILE A 1 272 ? 115.02300 116.71700 117.63300 1.000 40.83910  ? 279 ILE A CG2 1 
ATOM   1867 C CD1 . ILE A 1 272 ? 117.16200 115.17100 116.23700 1.000 37.24532  ? 279 ILE A CD1 1 
ATOM   1868 N N   . SER A 1 273 ? 112.68200 114.63300 119.74500 1.000 44.20699  ? 280 SER A N   1 
ATOM   1869 C CA  . SER A 1 273 ? 111.34300 115.03300 120.15900 1.000 41.74359  ? 280 SER A CA  1 
ATOM   1870 C C   . SER A 1 273 ? 111.28200 115.32300 121.65000 1.000 46.26413  ? 280 SER A C   1 
ATOM   1871 O O   . SER A 1 273 ? 110.57000 116.23800 122.07900 1.000 55.28637  ? 280 SER A O   1 
ATOM   1872 C CB  . SER A 1 273 ? 110.33400 113.95000 119.79700 1.000 43.54010  ? 280 SER A CB  1 
ATOM   1873 O OG  . SER A 1 273 ? 110.25700 112.98100 120.82100 1.000 53.97001  ? 280 SER A OG  1 
ATOM   1874 N N   . ILE A 1 274 ? 112.07500 114.60800 122.44600 1.000 52.63271  ? 281 ILE A N   1 
ATOM   1875 C CA  . ILE A 1 274 ? 112.12600 114.91000 123.87600 1.000 52.65994  ? 281 ILE A CA  1 
ATOM   1876 C C   . ILE A 1 274 ? 112.81500 116.24600 124.13200 1.000 58.24578  ? 281 ILE A C   1 
ATOM   1877 O O   . ILE A 1 274 ? 112.37500 117.03800 124.97900 1.000 64.71933  ? 281 ILE A O   1 
ATOM   1878 C CB  . ILE A 1 274 ? 112.81100 113.76900 124.64600 1.000 53.18330  ? 281 ILE A CB  1 
ATOM   1879 C CG1 . ILE A 1 274 ? 111.96400 112.50200 124.58100 1.000 56.08738  ? 281 ILE A CG1 1 
ATOM   1880 C CG2 . ILE A 1 274 ? 113.04600 114.16500 126.08400 1.000 51.67005  ? 281 ILE A CG2 1 
ATOM   1881 C CD1 . ILE A 1 274 ? 112.71300 111.25200 124.96600 1.000 57.61869  ? 281 ILE A CD1 1 
ATOM   1882 N N   . LEU A 1 275 ? 113.89100 116.53100 123.39900 1.000 57.64230  ? 282 LEU A N   1 
ATOM   1883 C CA  . LEU A 1 275 ? 114.52800 117.83900 123.56500 1.000 56.24601  ? 282 LEU A CA  1 
ATOM   1884 C C   . LEU A 1 275 ? 113.64000 118.99400 123.10200 1.000 59.15158  ? 282 LEU A C   1 
ATOM   1885 O O   . LEU A 1 275 ? 113.64800 120.06900 123.71600 1.000 65.99173  ? 282 LEU A O   1 
ATOM   1886 C CB  . LEU A 1 275 ? 115.86000 117.88200 122.82800 1.000 52.19178  ? 282 LEU A CB  1 
ATOM   1887 C CG  . LEU A 1 275 ? 116.86400 116.84500 123.30500 1.000 55.96840  ? 282 LEU A CG  1 
ATOM   1888 C CD1 . LEU A 1 275 ? 118.11700 116.93300 122.48300 1.000 59.45500  ? 282 LEU A CD1 1 
ATOM   1889 C CD2 . LEU A 1 275 ? 117.17100 117.06900 124.76500 1.000 61.07681  ? 282 LEU A CD2 1 
ATOM   1890 N N   . ILE A 1 276 ? 112.81900 118.77600 122.07900 1.000 54.40148  ? 283 ILE A N   1 
ATOM   1891 C CA  . ILE A 1 276 ? 111.82200 119.77200 121.69400 1.000 54.32202  ? 283 ILE A CA  1 
ATOM   1892 C C   . ILE A 1 276 ? 110.79400 119.96900 122.80000 1.000 56.85307  ? 283 ILE A C   1 
ATOM   1893 O O   . ILE A 1 276 ? 110.38800 121.10000 123.08200 1.000 56.36663  ? 283 ILE A O   1 
ATOM   1894 C CB  . ILE A 1 276 ? 111.16000 119.39500 120.35800 1.000 50.44756  ? 283 ILE A CB  1 
ATOM   1895 C CG1 . ILE A 1 276 ? 112.20000 119.37700 119.24800 1.000 51.64535  ? 283 ILE A CG1 1 
ATOM   1896 C CG2 . ILE A 1 276 ? 110.11200 120.40700 119.99200 1.000 48.98486  ? 283 ILE A CG2 1 
ATOM   1897 C CD1 . ILE A 1 276 ? 111.69200 118.80000 117.96800 1.000 52.06588  ? 283 ILE A CD1 1 
ATOM   1898 N N   . LYS A 1 277 ? 110.28100 118.87900 123.37400 1.000 60.24242  ? 284 LYS A N   1 
ATOM   1899 C CA  . LYS A 1 277 ? 109.30900 119.02500 124.45700 1.000 55.84049  ? 284 LYS A CA  1 
ATOM   1900 C C   . LYS A 1 277 ? 109.87600 119.83400 125.61900 1.000 59.84353  ? 284 LYS A C   1 
ATOM   1901 O O   . LYS A 1 277 ? 109.19000 120.70100 126.17800 1.000 70.13846  ? 284 LYS A O   1 
ATOM   1902 C CB  . LYS A 1 277 ? 108.85000 117.65800 124.96000 1.000 60.26816  ? 284 LYS A CB  1 
ATOM   1903 C CG  . LYS A 1 277 ? 107.60100 117.72900 125.82200 1.000 62.45077  ? 284 LYS A CG  1 
ATOM   1904 C CD  . LYS A 1 277 ? 107.30600 116.41200 126.51800 1.000 64.35459  ? 284 LYS A CD  1 
ATOM   1905 C CE  . LYS A 1 277 ? 106.99900 115.30400 125.53400 1.000 67.07227  ? 284 LYS A CE  1 
ATOM   1906 N NZ  . LYS A 1 277 ? 106.68500 114.01800 126.21500 1.000 68.52407  ? 284 LYS A NZ  1 
ATOM   1907 N N   . GLN A 1 278 ? 111.13000 119.57700 125.99000 1.000 65.44444  ? 285 GLN A N   1 
ATOM   1908 C CA  . GLN A 1 278 ? 111.76100 120.39100 127.02900 1.000 67.43171  ? 285 GLN A CA  1 
ATOM   1909 C C   . GLN A 1 278 ? 111.92800 121.84900 126.60600 1.000 71.23360  ? 285 GLN A C   1 
ATOM   1910 O O   . GLN A 1 278 ? 111.76100 122.76200 127.42500 1.000 70.08396  ? 285 GLN A O   1 
ATOM   1911 C CB  . GLN A 1 278 ? 113.11400 119.79600 127.41200 1.000 68.71745  ? 285 GLN A CB  1 
ATOM   1912 C CG  . GLN A 1 278 ? 113.02200 118.46200 128.12400 1.000 72.89509  ? 285 GLN A CG  1 
ATOM   1913 C CD  . GLN A 1 278 ? 114.38100 117.87400 128.42900 1.000 76.22506  ? 285 GLN A CD  1 
ATOM   1914 O OE1 . GLN A 1 278 ? 115.41100 118.49200 128.16600 1.000 76.66196  ? 285 GLN A OE1 1 
ATOM   1915 N NE2 . GLN A 1 278 ? 114.39200 116.66800 128.98200 1.000 75.07458  ? 285 GLN A NE2 1 
ATOM   1916 N N   . SER A 1 279 ? 112.20700 122.09800 125.32500 1.000 75.36075  ? 286 SER A N   1 
ATOM   1917 C CA  . SER A 1 279 ? 112.29700 123.48200 124.86300 1.000 73.49780  ? 286 SER A CA  1 
ATOM   1918 C C   . SER A 1 279 ? 110.94800 124.19600 124.89900 1.000 74.95099  ? 286 SER A C   1 
ATOM   1919 O O   . SER A 1 279 ? 110.88000 125.38300 125.23600 1.000 75.17735  ? 286 SER A O   1 
ATOM   1920 C CB  . SER A 1 279 ? 112.87600 123.52000 123.45400 1.000 71.16360  ? 286 SER A CB  1 
ATOM   1921 O OG  . SER A 1 279 ? 114.12900 122.86500 123.41300 1.000 78.32898  ? 286 SER A OG  1 
ATOM   1922 N N   . LEU A 1 280 ? 109.86800 123.50000 124.55100 1.000 71.06813  ? 287 LEU A N   1 
ATOM   1923 C CA  . LEU A 1 280 ? 108.53800 124.09200 124.68200 1.000 65.30624  ? 287 LEU A CA  1 
ATOM   1924 C C   . LEU A 1 280 ? 108.19700 124.39700 126.13100 1.000 65.65598  ? 287 LEU A C   1 
ATOM   1925 O O   . LEU A 1 280 ? 107.61400 125.44600 126.42800 1.000 71.07921  ? 287 LEU A O   1 
ATOM   1926 C CB  . LEU A 1 280 ? 107.47400 123.17600 124.08700 1.000 60.08231  ? 287 LEU A CB  1 
ATOM   1927 C CG  . LEU A 1 280 ? 107.54600 122.84100 122.60800 1.000 63.10965  ? 287 LEU A CG  1 
ATOM   1928 C CD1 . LEU A 1 280 ? 106.44900 121.86500 122.27700 1.000 66.01197  ? 287 LEU A CD1 1 
ATOM   1929 C CD2 . LEU A 1 280 ? 107.40000 124.09900 121.79700 1.000 68.39096  ? 287 LEU A CD2 1 
ATOM   1930 N N   . ASN A 1 281 ? 108.50700 123.47700 127.04500 1.000 75.35853  ? 288 ASN A N   1 
ATOM   1931 C CA  . ASN A 1 281 ? 108.27700 123.76200 128.45800 1.000 77.93476  ? 288 ASN A CA  1 
ATOM   1932 C C   . ASN A 1 281 ? 109.07700 124.97200 128.92800 1.000 80.87605  ? 288 ASN A C   1 
ATOM   1933 O O   . ASN A 1 281 ? 108.57400 125.79100 129.70600 1.000 80.03577  ? 288 ASN A O   1 
ATOM   1934 C CB  . ASN A 1 281 ? 108.60800 122.53800 129.30900 1.000 75.97762  ? 288 ASN A CB  1 
ATOM   1935 C CG  . ASN A 1 281 ? 107.59900 121.42800 129.14300 1.000 76.36301  ? 288 ASN A CG  1 
ATOM   1936 O OD1 . ASN A 1 281 ? 106.51600 121.63600 128.60000 1.000 76.78351  ? 288 ASN A OD1 1 
ATOM   1937 N ND2 . ASN A 1 281 ? 107.94600 120.23800 129.61400 1.000 78.29223  ? 288 ASN A ND2 1 
ATOM   1938 N N   . TRP A 1 282 ? 110.29800 125.14000 128.41900 1.000 86.00786  ? 289 TRP A N   1 
ATOM   1939 C CA  . TRP A 1 282 ? 111.06000 126.34000 128.75700 1.000 86.85198  ? 289 TRP A CA  1 
ATOM   1940 C C   . TRP A 1 282 ? 110.43700 127.60700 128.18100 1.000 87.99856  ? 289 TRP A C   1 
ATOM   1941 O O   . TRP A 1 282 ? 110.38600 128.63600 128.86200 1.000 89.69162  ? 289 TRP A O   1 
ATOM   1942 C CB  . TRP A 1 282 ? 112.50300 126.21500 128.28200 1.000 88.95233  ? 289 TRP A CB  1 
ATOM   1943 C CG  . TRP A 1 282 ? 113.28600 127.47000 128.51700 1.000 90.69519  ? 289 TRP A CG  1 
ATOM   1944 C CD1 . TRP A 1 282 ? 113.77000 127.92100 129.70900 1.000 90.65493  ? 289 TRP A CD1 1 
ATOM   1945 C CD2 . TRP A 1 282 ? 113.66600 128.44300 127.53700 1.000 90.44993  ? 289 TRP A CD2 1 
ATOM   1946 N NE1 . TRP A 1 282 ? 114.43200 129.11000 129.53300 1.000 90.77191  ? 289 TRP A NE1 1 
ATOM   1947 C CE2 . TRP A 1 282 ? 114.38300 129.45200 128.20800 1.000 90.58323  ? 289 TRP A CE2 1 
ATOM   1948 C CE3 . TRP A 1 282 ? 113.47500 128.55600 126.15800 1.000 89.39753  ? 289 TRP A CE3 1 
ATOM   1949 C CZ2 . TRP A 1 282 ? 114.90600 130.55900 127.54800 1.000 90.60873  ? 289 TRP A CZ2 1 
ATOM   1950 C CZ3 . TRP A 1 282 ? 113.99600 129.65700 125.50500 1.000 90.85875  ? 289 TRP A CZ3 1 
ATOM   1951 C CH2 . TRP A 1 282 ? 114.70200 130.64300 126.19900 1.000 92.13814  ? 289 TRP A CH2 1 
ATOM   1952 N N   . ILE A 1 283 ? 109.98600 127.57000 126.92700 1.000 84.46783  ? 290 ILE A N   1 
ATOM   1953 C CA  . ILE A 1 283 ? 109.33500 128.74400 126.34300 1.000 84.70673  ? 290 ILE A CA  1 
ATOM   1954 C C   . ILE A 1 283 ? 108.07500 129.12000 127.11700 1.000 85.01287  ? 290 ILE A C   1 
ATOM   1955 O O   . ILE A 1 283 ? 107.83800 130.30000 127.40300 1.000 86.46381  ? 290 ILE A O   1 
ATOM   1956 C CB  . ILE A 1 283 ? 109.03000 128.51400 124.85100 1.000 82.31411  ? 290 ILE A CB  1 
ATOM   1957 C CG1 . ILE A 1 283 ? 110.32300 128.45100 124.04100 1.000 84.93542  ? 290 ILE A CG1 1 
ATOM   1958 C CG2 . ILE A 1 283 ? 108.14000 129.61300 124.31400 1.000 82.89318  ? 290 ILE A CG2 1 
ATOM   1959 C CD1 . ILE A 1 283 ? 110.12300 127.99800 122.61400 1.000 84.94947  ? 290 ILE A CD1 1 
ATOM   1960 N N   . LEU A 1 284 ? 107.25400 128.13400 127.47600 1.000 84.49511  ? 291 LEU A N   1 
ATOM   1961 C CA  . LEU A 1 284 ? 106.06300 128.42900 128.26900 1.000 83.54593  ? 291 LEU A CA  1 
ATOM   1962 C C   . LEU A 1 284 ? 106.40400 128.94300 129.66200 1.000 84.87974  ? 291 LEU A C   1 
ATOM   1963 O O   . LEU A 1 284 ? 105.67500 129.78300 130.19900 1.000 86.80285  ? 291 LEU A O   1 
ATOM   1964 C CB  . LEU A 1 284 ? 105.16600 127.19800 128.36800 1.000 85.12768  ? 291 LEU A CB  1 
ATOM   1965 C CG  . LEU A 1 284 ? 104.51700 126.73600 127.06600 1.000 82.99153  ? 291 LEU A CG  1 
ATOM   1966 C CD1 . LEU A 1 284 ? 103.80300 125.42000 127.27200 1.000 82.27178  ? 291 LEU A CD1 1 
ATOM   1967 C CD2 . LEU A 1 284 ? 103.55600 127.78700 126.56800 1.000 82.16467  ? 291 LEU A CD2 1 
ATOM   1968 N N   . ARG A 1 285 ? 107.49000 128.46000 130.26700 1.000 88.64779  ? 292 ARG A N   1 
ATOM   1969 C CA  . ARG A 1 285 ? 107.91300 129.02400 131.54600 1.000 90.76765  ? 292 ARG A CA  1 
ATOM   1970 C C   . ARG A 1 285 ? 108.36400 130.47300 131.39800 1.000 92.46044  ? 292 ARG A C   1 
ATOM   1971 O O   . ARG A 1 285 ? 108.00100 131.32700 132.21400 1.000 89.64880  ? 292 ARG A O   1 
ATOM   1972 C CB  . ARG A 1 285 ? 109.02800 128.17400 132.15200 1.000 89.64698  ? 292 ARG A CB  1 
ATOM   1973 N N   . LYS A 1 286 ? 109.15900 130.76900 130.36900 1.000 100.77500 ? 293 LYS A N   1 
ATOM   1974 C CA  . LYS A 1 286 ? 109.58800 132.14300 130.12600 1.000 99.96490  ? 293 LYS A CA  1 
ATOM   1975 C C   . LYS A 1 286 ? 108.43700 133.04300 129.69600 1.000 99.82963  ? 293 LYS A C   1 
ATOM   1976 O O   . LYS A 1 286 ? 108.49800 134.26000 129.90100 1.000 102.21986 ? 293 LYS A O   1 
ATOM   1977 C CB  . LYS A 1 286 ? 110.69600 132.17000 129.07400 1.000 98.78489  ? 293 LYS A CB  1 
ATOM   1978 N N   . MET A 1 287 ? 107.38700 132.47900 129.09900 1.000 96.42848  ? 294 MET A N   1 
ATOM   1979 C CA  . MET A 1 287 ? 106.20000 133.27000 128.79400 1.000 95.98642  ? 294 MET A CA  1 
ATOM   1980 C C   . MET A 1 287 ? 105.35600 133.58700 130.02100 1.000 98.68943  ? 294 MET A C   1 
ATOM   1981 O O   . MET A 1 287 ? 104.39100 134.35000 129.89900 1.000 100.31916 ? 294 MET A O   1 
ATOM   1982 C CB  . MET A 1 287 ? 105.34000 132.54800 127.75600 1.000 96.16898  ? 294 MET A CB  1 
ATOM   1983 N N   . ASP A 1 288 ? 105.67700 133.02700 131.18300 1.000 101.15503 ? 295 ASP A N   1 
ATOM   1984 C CA  . ASP A 1 288 ? 104.90500 133.29000 132.39500 1.000 101.99485 ? 295 ASP A CA  1 
ATOM   1985 C C   . ASP A 1 288 ? 104.99600 134.75700 132.80100 1.000 101.54152 ? 295 ASP A C   1 
ATOM   1986 O O   . ASP A 1 288 ? 106.08600 135.32600 132.86600 1.000 100.68163 ? 295 ASP A O   1 
ATOM   1987 C CB  . ASP A 1 288 ? 105.37900 132.39900 133.54400 1.000 99.57282  ? 295 ASP A CB  1 
ATOM   1988 N N   . ASN B 1 7   ? 117.77300 88.00600  131.01100 1.000 87.97233  ? 14  ASN B N   1 
ATOM   1989 C CA  . ASN B 1 7   ? 116.80500 88.94300  131.56500 1.000 88.48029  ? 14  ASN B CA  1 
ATOM   1990 C C   . ASN B 1 7   ? 115.55400 88.99600  130.70100 1.000 85.21849  ? 14  ASN B C   1 
ATOM   1991 O O   . ASN B 1 7   ? 115.62900 88.83800  129.48500 1.000 85.38149  ? 14  ASN B O   1 
ATOM   1992 C CB  . ASN B 1 7   ? 117.41800 90.33700  131.69200 1.000 85.55160  ? 14  ASN B CB  1 
ATOM   1993 N N   . GLU B 1 8   ? 114.40200 89.20800  131.34200 1.000 82.35458  ? 15  GLU B N   1 
ATOM   1994 C CA  . GLU B 1 8   ? 113.12700 89.09000  130.64300 1.000 82.97530  ? 15  GLU B CA  1 
ATOM   1995 C C   . GLU B 1 8   ? 112.99800 90.10100  129.51100 1.000 86.12485  ? 15  GLU B C   1 
ATOM   1996 O O   . GLU B 1 8   ? 112.30900 89.83600  128.52200 1.000 88.90985  ? 15  GLU B O   1 
ATOM   1997 C CB  . GLU B 1 8   ? 111.97000 89.25100  131.62700 1.000 81.36846  ? 15  GLU B CB  1 
ATOM   1998 N N   . ASP B 1 9   ? 113.65100 91.25800  129.63100 1.000 85.46680  ? 16  ASP B N   1 
ATOM   1999 C CA  . ASP B 1 9   ? 113.59500 92.25000  128.56300 1.000 82.43143  ? 16  ASP B CA  1 
ATOM   2000 C C   . ASP B 1 9   ? 114.32500 91.78100  127.30900 1.000 84.25950  ? 16  ASP B C   1 
ATOM   2001 O O   . ASP B 1 9   ? 113.84700 91.99600  126.18700 1.000 88.09446  ? 16  ASP B O   1 
ATOM   2002 C CB  . ASP B 1 9   ? 114.18000 93.57200  129.05100 1.000 80.67531  ? 16  ASP B CB  1 
ATOM   2003 C CG  . ASP B 1 9   ? 113.37500 94.18500  130.17400 1.000 85.86161  ? 16  ASP B CG  1 
ATOM   2004 O OD1 . ASP B 1 9   ? 112.13300 94.07700  130.14200 1.000 86.51395  ? 16  ASP B OD1 1 
ATOM   2005 O OD2 . ASP B 1 9   ? 113.98300 94.77800  131.08900 1.000 88.04866  ? 16  ASP B OD2 1 
ATOM   2006 N N   . ASN B 1 10  ? 115.43500 91.06300  127.47400 1.000 75.57658  ? 17  ASN B N   1 
ATOM   2007 C CA  . ASN B 1 10  ? 116.09600 90.48100  126.31300 1.000 73.93741  ? 17  ASN B CA  1 
ATOM   2008 C C   . ASN B 1 10  ? 115.27700 89.34900  125.71400 1.000 72.20289  ? 17  ASN B C   1 
ATOM   2009 O O   . ASN B 1 10  ? 115.23300 89.19300  124.48800 1.000 72.43695  ? 17  ASN B O   1 
ATOM   2010 C CB  . ASN B 1 10  ? 117.48800 89.98700  126.69800 1.000 78.29659  ? 17  ASN B CB  1 
ATOM   2011 C CG  . ASN B 1 10  ? 118.45000 91.12200  126.97300 1.000 81.89883  ? 17  ASN B CG  1 
ATOM   2012 O OD1 . ASN B 1 10  ? 118.07900 92.29300  126.91500 1.000 82.05860  ? 17  ASN B OD1 1 
ATOM   2013 N ND2 . ASN B 1 10  ? 119.69500 90.78000  127.27800 1.000 82.30892  ? 17  ASN B ND2 1 
ATOM   2014 N N   . ALA B 1 11  ? 114.63800 88.53800  126.55300 1.000 66.65047  ? 18  ALA B N   1 
ATOM   2015 C CA  . ALA B 1 11  ? 113.80100 87.47200  126.02100 1.000 66.89642  ? 18  ALA B CA  1 
ATOM   2016 C C   . ALA B 1 11  ? 112.63900 88.03800  125.22100 1.000 67.07853  ? 18  ALA B C   1 
ATOM   2017 O O   . ALA B 1 11  ? 112.32400 87.54100  124.13600 1.000 74.59619  ? 18  ALA B O   1 
ATOM   2018 C CB  . ALA B 1 11  ? 113.29000 86.58600  127.15400 1.000 71.69364  ? 18  ALA B CB  1 
ATOM   2019 N N   . ARG B 1 12  ? 112.01600 89.10700  125.72200 1.000 69.33304  ? 19  ARG B N   1 
ATOM   2020 C CA  . ARG B 1 12  ? 110.95900 89.78200  124.97300 1.000 68.19912  ? 19  ARG B CA  1 
ATOM   2021 C C   . ARG B 1 12  ? 111.46400 90.35900  123.65800 1.000 67.73489  ? 19  ARG B C   1 
ATOM   2022 O O   . ARG B 1 12  ? 110.80400 90.22500  122.62300 1.000 67.09595  ? 19  ARG B O   1 
ATOM   2023 C CB  . ARG B 1 12  ? 110.33900 90.88900  125.81900 1.000 66.81251  ? 19  ARG B CB  1 
ATOM   2024 C CG  . ARG B 1 12  ? 109.07000 91.45200  125.22400 1.000 71.09105  ? 19  ARG B CG  1 
ATOM   2025 C CD  . ARG B 1 12  ? 108.61900 92.72300  125.92200 1.000 74.00220  ? 19  ARG B CD  1 
ATOM   2026 N NE  . ARG B 1 12  ? 108.37200 92.53200  127.34500 1.000 72.27762  ? 19  ARG B NE  1 
ATOM   2027 C CZ  . ARG B 1 12  ? 109.15800 92.99200  128.30600 1.000 74.07813  ? 19  ARG B CZ  1 
ATOM   2028 N NH1 . ARG B 1 12  ? 110.25000 93.68400  128.03200 1.000 74.62622  ? 19  ARG B NH1 1 
ATOM   2029 N NH2 . ARG B 1 12  ? 108.83600 92.75700  129.57400 1.000 74.74374  ? 19  ARG B NH2 1 
ATOM   2030 N N   . PHE B 1 13  ? 112.63900 90.98600  123.67000 1.000 64.40882  ? 20  PHE B N   1 
ATOM   2031 C CA  . PHE B 1 13  ? 113.17100 91.57800  122.44600 1.000 59.76008  ? 20  PHE B CA  1 
ATOM   2032 C C   . PHE B 1 13  ? 113.49100 90.52800  121.38500 1.000 63.06584  ? 20  PHE B C   1 
ATOM   2033 O O   . PHE B 1 13  ? 113.10700 90.67400  120.21600 1.000 66.63114  ? 20  PHE B O   1 
ATOM   2034 C CB  . PHE B 1 13  ? 114.41300 92.39400  122.78500 1.000 57.12185  ? 20  PHE B CB  1 
ATOM   2035 C CG  . PHE B 1 13  ? 115.03300 93.07200  121.61100 1.000 58.01473  ? 20  PHE B CG  1 
ATOM   2036 C CD1 . PHE B 1 13  ? 114.35400 94.06000  120.93500 1.000 59.67634  ? 20  PHE B CD1 1 
ATOM   2037 C CD2 . PHE B 1 13  ? 116.30200 92.73600  121.19500 1.000 62.91325  ? 20  PHE B CD2 1 
ATOM   2038 C CE1 . PHE B 1 13  ? 114.92700 94.69500  119.86500 1.000 59.87074  ? 20  PHE B CE1 1 
ATOM   2039 C CE2 . PHE B 1 13  ? 116.87900 93.36800  120.12100 1.000 64.41968  ? 20  PHE B CE2 1 
ATOM   2040 C CZ  . PHE B 1 13  ? 116.18900 94.34800  119.45500 1.000 63.86717  ? 20  PHE B CZ  1 
ATOM   2041 N N   . LEU B 1 14  ? 114.16500 89.44400  121.77300 1.000 61.64937  ? 21  LEU B N   1 
ATOM   2042 C CA  . LEU B 1 14  ? 114.45400 88.37200  120.82100 1.000 57.11311  ? 21  LEU B CA  1 
ATOM   2043 C C   . LEU B 1 14  ? 113.19300 87.65300  120.34700 1.000 56.12774  ? 21  LEU B C   1 
ATOM   2044 O O   . LEU B 1 14  ? 113.07900 87.31500  119.16100 1.000 61.55553  ? 21  LEU B O   1 
ATOM   2045 C CB  . LEU B 1 14  ? 115.43000 87.37300  121.43800 1.000 60.36555  ? 21  LEU B CB  1 
ATOM   2046 C CG  . LEU B 1 14  ? 116.92700 87.59800  121.21100 1.000 60.67422  ? 21  LEU B CG  1 
ATOM   2047 C CD1 . LEU B 1 14  ? 117.37000 88.97200  121.67300 1.000 59.32524  ? 21  LEU B CD1 1 
ATOM   2048 C CD2 . LEU B 1 14  ? 117.72600 86.52000  121.91800 1.000 56.78843  ? 21  LEU B CD2 1 
ATOM   2049 N N   . LEU B 1 15  ? 112.22800 87.42600  121.23900 1.000 51.66100  ? 22  LEU B N   1 
ATOM   2050 C CA  . LEU B 1 15  ? 110.97300 86.81500  120.82100 1.000 50.87814  ? 22  LEU B CA  1 
ATOM   2051 C C   . LEU B 1 15  ? 110.23300 87.68400  119.81800 1.000 55.44286  ? 22  LEU B C   1 
ATOM   2052 O O   . LEU B 1 15  ? 109.69600 87.17600  118.82700 1.000 65.61344  ? 22  LEU B O   1 
ATOM   2053 C CB  . LEU B 1 15  ? 110.09700 86.53500  122.03800 1.000 51.92409  ? 22  LEU B CB  1 
ATOM   2054 C CG  . LEU B 1 15  ? 108.70900 85.96800  121.75700 1.000 50.68880  ? 22  LEU B CG  1 
ATOM   2055 C CD1 . LEU B 1 15  ? 108.82100 84.63000  121.07100 1.000 52.21095  ? 22  LEU B CD1 1 
ATOM   2056 C CD2 . LEU B 1 15  ? 107.93300 85.82900  123.04400 1.000 55.80745  ? 22  LEU B CD2 1 
ATOM   2057 N N   . LEU B 1 16  ? 110.18200 88.99300  120.05200 1.000 43.95035  ? 23  LEU B N   1 
ATOM   2058 C CA  . LEU B 1 16  ? 109.50700 89.86500  119.10000 1.000 42.50376  ? 23  LEU B CA  1 
ATOM   2059 C C   . LEU B 1 16  ? 110.23500 89.91800  117.76200 1.000 50.64884  ? 23  LEU B C   1 
ATOM   2060 O O   . LEU B 1 16  ? 109.59200 89.94500  116.70900 1.000 56.51706  ? 23  LEU B O   1 
ATOM   2061 C CB  . LEU B 1 16  ? 109.35500 91.26600  119.67600 1.000 48.71235  ? 23  LEU B CB  1 
ATOM   2062 C CG  . LEU B 1 16  ? 108.60000 92.21400  118.75600 1.000 49.78625  ? 23  LEU B CG  1 
ATOM   2063 C CD1 . LEU B 1 16  ? 107.21000 91.68900  118.51800 1.000 51.47673  ? 23  LEU B CD1 1 
ATOM   2064 C CD2 . LEU B 1 16  ? 108.54300 93.57700  119.37900 1.000 50.04260  ? 23  LEU B CD2 1 
ATOM   2065 N N   . ALA B 1 17  ? 111.56900 89.95200  117.77100 1.000 46.11401  ? 24  ALA B N   1 
ATOM   2066 C CA  . ALA B 1 17  ? 112.29800 89.89300  116.50600 1.000 38.17578  ? 24  ALA B CA  1 
ATOM   2067 C C   . ALA B 1 17  ? 111.99900 88.61400  115.72700 1.000 41.35670  ? 24  ALA B C   1 
ATOM   2068 O O   . ALA B 1 17  ? 111.77500 88.65800  114.51000 1.000 48.16793  ? 24  ALA B O   1 
ATOM   2069 C CB  . ALA B 1 17  ? 113.79600 90.02400  116.75700 1.000 46.51528  ? 24  ALA B CB  1 
ATOM   2070 N N   . ALA B 1 18  ? 111.96800 87.46700  116.40900 1.000 38.91561  ? 25  ALA B N   1 
ATOM   2071 C CA  . ALA B 1 18  ? 111.62400 86.21400  115.73700 1.000 36.88165  ? 25  ALA B CA  1 
ATOM   2072 C C   . ALA B 1 18  ? 110.20300 86.22100  115.18300 1.000 39.92372  ? 25  ALA B C   1 
ATOM   2073 O O   . ALA B 1 18  ? 109.96600 85.77400  114.05200 1.000 54.98783  ? 25  ALA B O   1 
ATOM   2074 C CB  . ALA B 1 18  ? 111.80600 85.03800  116.69400 1.000 39.20940  ? 25  ALA B CB  1 
ATOM   2075 N N   . LEU B 1 19  ? 109.24600 86.73500  115.95300 1.000 33.86958  ? 26  LEU B N   1 
ATOM   2076 C CA  . LEU B 1 19  ? 107.87200 86.79500  115.46500 1.000 37.74030  ? 26  LEU B CA  1 
ATOM   2077 C C   . LEU B 1 19  ? 107.72500 87.73600  114.27500 1.000 39.09361  ? 26  LEU B C   1 
ATOM   2078 O O   . LEU B 1 19  ? 106.98500 87.43600  113.33500 1.000 39.24306  ? 26  LEU B O   1 
ATOM   2079 C CB  . LEU B 1 19  ? 106.93000 87.20400  116.59100 1.000 43.08619  ? 26  LEU B CB  1 
ATOM   2080 C CG  . LEU B 1 19  ? 106.72700 86.14400  117.66900 1.000 42.13706  ? 26  LEU B CG  1 
ATOM   2081 C CD1 . LEU B 1 19  ? 105.93700 86.71300  118.82400 1.000 42.10605  ? 26  LEU B CD1 1 
ATOM   2082 C CD2 . LEU B 1 19  ? 106.03200 84.93400  117.09200 1.000 39.30557  ? 26  LEU B CD2 1 
ATOM   2083 N N   . ILE B 1 20  ? 108.42700 88.86600  114.27800 1.000 33.57542  ? 27  ILE B N   1 
ATOM   2084 C CA  . ILE B 1 20  ? 108.36700 89.75900  113.12500 1.000 31.32242  ? 27  ILE B CA  1 
ATOM   2085 C C   . ILE B 1 20  ? 108.99200 89.11700  111.88900 1.000 38.50313  ? 27  ILE B C   1 
ATOM   2086 O O   . ILE B 1 20  ? 108.48000 89.27400  110.77700 1.000 41.89832  ? 27  ILE B O   1 
ATOM   2087 C CB  . ILE B 1 20  ? 109.02000 91.10900  113.45500 1.000 34.33263  ? 27  ILE B CB  1 
ATOM   2088 C CG1 . ILE B 1 20  ? 108.17900 91.85700  114.47600 1.000 42.29939  ? 27  ILE B CG1 1 
ATOM   2089 C CG2 . ILE B 1 20  ? 109.13400 91.95500  112.22400 1.000 39.44332  ? 27  ILE B CG2 1 
ATOM   2090 C CD1 . ILE B 1 20  ? 108.86000 93.06800  115.02600 1.000 44.93440  ? 27  ILE B CD1 1 
ATOM   2091 N N   . VAL B 1 21  ? 110.12900 88.43500  112.04000 1.000 44.19757  ? 28  VAL B N   1 
ATOM   2092 C CA  . VAL B 1 21  ? 110.72700 87.76200  110.88400 1.000 36.90814  ? 28  VAL B CA  1 
ATOM   2093 C C   . VAL B 1 21  ? 109.80300 86.68800  110.31200 1.000 43.35521  ? 28  VAL B C   1 
ATOM   2094 O O   . VAL B 1 21  ? 109.66200 86.56000  109.08700 1.000 54.09212  ? 28  VAL B O   1 
ATOM   2095 C CB  . VAL B 1 21  ? 112.10200 87.18500  111.25400 1.000 36.01860  ? 28  VAL B CB  1 
ATOM   2096 C CG1 . VAL B 1 21  ? 112.57900 86.24800  110.17800 1.000 37.70897  ? 28  VAL B CG1 1 
ATOM   2097 C CG2 . VAL B 1 21  ? 113.09300 88.30800  111.42100 1.000 44.49182  ? 28  VAL B CG2 1 
ATOM   2098 N N   . LEU B 1 22  ? 109.12900 85.92300  111.17500 1.000 36.06165  ? 29  LEU B N   1 
ATOM   2099 C CA  . LEU B 1 22  ? 108.12400 84.99200  110.65900 1.000 32.82633  ? 29  LEU B CA  1 
ATOM   2100 C C   . LEU B 1 22  ? 106.92000 85.70000  110.04700 1.000 43.96479  ? 29  LEU B C   1 
ATOM   2101 O O   . LEU B 1 22  ? 106.32700 85.19100  109.09100 1.000 53.95826  ? 29  LEU B O   1 
ATOM   2102 C CB  . LEU B 1 22  ? 107.66600 84.03900  111.75600 1.000 31.14859  ? 29  LEU B CB  1 
ATOM   2103 C CG  . LEU B 1 22  ? 108.74000 83.08800  112.26700 1.000 36.29214  ? 29  LEU B CG  1 
ATOM   2104 C CD1 . LEU B 1 22  ? 108.21100 82.27900  113.43000 1.000 41.38795  ? 29  LEU B CD1 1 
ATOM   2105 C CD2 . LEU B 1 22  ? 109.21000 82.18300  111.15100 1.000 39.94313  ? 29  LEU B CD2 1 
ATOM   2106 N N   . TYR B 1 23  ? 106.59200 86.89900  110.52100 1.000 37.02960  ? 30  TYR B N   1 
ATOM   2107 C CA  . TYR B 1 23  ? 105.50900 87.66600  109.91600 1.000 35.40570  ? 30  TYR B CA  1 
ATOM   2108 C C   . TYR B 1 23  ? 105.87000 88.15900  108.52300 1.000 37.84076  ? 30  TYR B C   1 
ATOM   2109 O O   . TYR B 1 23  ? 105.04000 88.12000  107.61100 1.000 43.93058  ? 30  TYR B O   1 
ATOM   2110 C CB  . TYR B 1 23  ? 105.17100 88.85200  110.81500 1.000 44.63645  ? 30  TYR B CB  1 
ATOM   2111 C CG  . TYR B 1 23  ? 103.76300 89.36600  110.70300 1.000 46.16041  ? 30  TYR B CG  1 
ATOM   2112 C CD1 . TYR B 1 23  ? 102.69000 88.59000  111.09000 1.000 49.76257  ? 30  TYR B CD1 1 
ATOM   2113 C CD2 . TYR B 1 23  ? 103.51100 90.63800  110.22300 1.000 38.58301  ? 30  TYR B CD2 1 
ATOM   2114 C CE1 . TYR B 1 23  ? 101.41000 89.06400  111.00400 1.000 42.69427  ? 30  TYR B CE1 1 
ATOM   2115 C CE2 . TYR B 1 23  ? 102.23600 91.11400  110.12400 1.000 39.31155  ? 30  TYR B CE2 1 
ATOM   2116 C CZ  . TYR B 1 23  ? 101.18800 90.32300  110.51800 1.000 43.16462  ? 30  TYR B CZ  1 
ATOM   2117 O OH  . TYR B 1 23  ? 99.90200  90.78300  110.41500 1.000 50.51461  ? 30  TYR B OH  1 
ATOM   2118 N N   . LEU B 1 24  ? 107.12100 88.55900  108.32400 1.000 36.68806  ? 31  LEU B N   1 
ATOM   2119 C CA  . LEU B 1 24  ? 107.57100 88.95600  106.99400 1.000 35.61117  ? 31  LEU B CA  1 
ATOM   2120 C C   . LEU B 1 24  ? 107.62200 87.77100  106.03800 1.000 41.18579  ? 31  LEU B C   1 
ATOM   2121 O O   . LEU B 1 24  ? 107.19600 87.88400  104.88500 1.000 47.47830  ? 31  LEU B O   1 
ATOM   2122 C CB  . LEU B 1 24  ? 108.93100 89.64400  107.07100 1.000 37.10714  ? 31  LEU B CB  1 
ATOM   2123 C CG  . LEU B 1 24  ? 109.02600 90.87500  107.96700 1.000 37.49253  ? 31  LEU B CG  1 
ATOM   2124 C CD1 . LEU B 1 24  ? 110.37500 91.53300  107.81400 1.000 42.98715  ? 31  LEU B CD1 1 
ATOM   2125 C CD2 . LEU B 1 24  ? 107.93000 91.84500  107.64400 1.000 40.81481  ? 31  LEU B CD2 1 
ATOM   2126 N N   . LEU B 1 25  ? 108.16700 86.63500  106.47500 1.000 40.79712  ? 32  LEU B N   1 
ATOM   2127 C CA  . LEU B 1 25  ? 108.17100 85.46200  105.59900 1.000 40.35241  ? 32  LEU B CA  1 
ATOM   2128 C C   . LEU B 1 25  ? 106.75800 84.98600  105.25200 1.000 40.88707  ? 32  LEU B C   1 
ATOM   2129 O O   . LEU B 1 25  ? 106.48300 84.63300  104.09700 1.000 50.59842  ? 32  LEU B O   1 
ATOM   2130 C CB  . LEU B 1 25  ? 108.96800 84.32500  106.23300 1.000 37.22573  ? 32  LEU B CB  1 
ATOM   2131 C CG  . LEU B 1 25  ? 110.47300 84.52800  106.35400 1.000 32.30362  ? 32  LEU B CG  1 
ATOM   2132 C CD1 . LEU B 1 25  ? 111.07600 83.44000  107.20500 1.000 39.22404  ? 32  LEU B CD1 1 
ATOM   2133 C CD2 . LEU B 1 25  ? 111.10600 84.53800  104.99400 1.000 36.99549  ? 32  LEU B CD2 1 
ATOM   2134 N N   . GLY B 1 26  ? 105.82300 85.05900  106.19800 1.000 26.75545  ? 33  GLY B N   1 
ATOM   2135 C CA  . GLY B 1 26  ? 104.45100 84.70500  105.87100 1.000 30.50731  ? 33  GLY B CA  1 
ATOM   2136 C C   . GLY B 1 26  ? 103.77900 85.69100  104.93500 1.000 41.37198  ? 33  GLY B C   1 
ATOM   2137 O O   . GLY B 1 26  ? 103.06300 85.29100  104.01000 1.000 47.40516  ? 33  GLY B O   1 
ATOM   2138 N N   . GLY B 1 27  ? 104.02000 86.98600  105.13100 1.000 40.46779  ? 34  GLY B N   1 
ATOM   2139 C CA  . GLY B 1 27  ? 103.44900 87.96300  104.22200 1.000 34.86742  ? 34  GLY B CA  1 
ATOM   2140 C C   . GLY B 1 27  ? 104.00300 87.83400  102.81800 1.000 36.23043  ? 34  GLY B C   1 
ATOM   2141 O O   . GLY B 1 27  ? 103.25900 87.91500  101.84000 1.000 37.43060  ? 34  GLY B O   1 
ATOM   2142 N N   . ALA B 1 28  ? 105.31600 87.64400  102.69600 1.000 36.13268  ? 35  ALA B N   1 
ATOM   2143 C CA  . ALA B 1 28  ? 105.91100 87.43300  101.38300 1.000 38.33129  ? 35  ALA B CA  1 
ATOM   2144 C C   . ALA B 1 28  ? 105.33500 86.20100  100.70400 1.000 36.65954  ? 35  ALA B C   1 
ATOM   2145 O O   . ALA B 1 28  ? 105.09400 86.20800  99.49400  1.000 42.36620  ? 35  ALA B O   1 
ATOM   2146 C CB  . ALA B 1 28  ? 107.42400 87.30600  101.50600 1.000 37.01814  ? 35  ALA B CB  1 
ATOM   2147 N N   . ALA B 1 29  ? 105.11000 85.12900  101.46200 1.000 40.39899  ? 36  ALA B N   1 
ATOM   2148 C CA  . ALA B 1 29  ? 104.49700 83.94400  100.87300 1.000 36.82494  ? 36  ALA B CA  1 
ATOM   2149 C C   . ALA B 1 29  ? 103.05600 84.18100  100.43600 1.000 37.83580  ? 36  ALA B C   1 
ATOM   2150 O O   . ALA B 1 29  ? 102.60300 83.56300  99.46900  1.000 43.17376  ? 36  ALA B O   1 
ATOM   2151 C CB  . ALA B 1 29  ? 104.55800 82.77700  101.85500 1.000 40.72058  ? 36  ALA B CB  1 
ATOM   2152 N N   . VAL B 1 30  ? 102.31900 85.05100  101.12900 1.000 43.84663  ? 37  VAL B N   1 
ATOM   2153 C CA  . VAL B 1 30  ? 100.93900 85.33800  100.73200 1.000 40.39701  ? 37  VAL B CA  1 
ATOM   2154 C C   . VAL B 1 30  ? 100.86000 86.29400  99.54100  1.000 46.22400  ? 37  VAL B C   1 
ATOM   2155 O O   . VAL B 1 30  ? 100.16200 86.01200  98.56200  1.000 50.27532  ? 37  VAL B O   1 
ATOM   2156 C CB  . VAL B 1 30  ? 100.13600 85.87100  101.92900 1.000 40.88285  ? 37  VAL B CB  1 
ATOM   2157 C CG1 . VAL B 1 30  ? 98.75300  86.25200  101.48200 1.000 44.95826  ? 37  VAL B CG1 1 
ATOM   2158 C CG2 . VAL B 1 30  ? 100.04300 84.81600  102.99900 1.000 41.64856  ? 37  VAL B CG2 1 
ATOM   2159 N N   . PHE B 1 31  ? 101.54800 87.43800  99.59800  1.000 47.92727  ? 38  PHE B N   1 
ATOM   2160 C CA  . PHE B 1 31  ? 101.45100 88.42100  98.51500  1.000 38.27201  ? 38  PHE B CA  1 
ATOM   2161 C C   . PHE B 1 31  ? 101.93200 87.88700  97.17100  1.000 49.46040  ? 38  PHE B C   1 
ATOM   2162 O O   . PHE B 1 31  ? 101.30800 88.15500  96.14100  1.000 60.44960  ? 38  PHE B O   1 
ATOM   2163 C CB  . PHE B 1 31  ? 102.23400 89.68400  98.85300  1.000 36.20531  ? 38  PHE B CB  1 
ATOM   2164 C CG  . PHE B 1 31  ? 101.51500 90.63000  99.75500  1.000 41.52284  ? 38  PHE B CG  1 
ATOM   2165 C CD1 . PHE B 1 31  ? 100.47800 91.39400  99.27600  1.000 41.22921  ? 38  PHE B CD1 1 
ATOM   2166 C CD2 . PHE B 1 31  ? 101.91600 90.80900  101.05700 1.000 46.88715  ? 38  PHE B CD2 1 
ATOM   2167 C CE1 . PHE B 1 31  ? 99.83300  92.28300  100.08800 1.000 45.73209  ? 38  PHE B CE1 1 
ATOM   2168 C CE2 . PHE B 1 31  ? 101.26900 91.70200  101.87100 1.000 44.71983  ? 38  PHE B CE2 1 
ATOM   2169 C CZ  . PHE B 1 31  ? 100.23000 92.43700  101.38700 1.000 41.46364  ? 38  PHE B CZ  1 
ATOM   2170 N N   . SER B 1 32  ? 103.02500 87.13200  97.14800  1.000 46.04937  ? 39  SER B N   1 
ATOM   2171 C CA  . SER B 1 32  ? 103.45200 86.53000  95.89100  1.000 43.77681  ? 39  SER B CA  1 
ATOM   2172 C C   . SER B 1 32  ? 102.45900 85.51500  95.34200  1.000 48.25286  ? 39  SER B C   1 
ATOM   2173 O O   . SER B 1 32  ? 102.52600 85.18800  94.15600  1.000 55.00593  ? 39  SER B O   1 
ATOM   2174 C CB  . SER B 1 32  ? 104.81100 85.86300  96.06000  1.000 47.14246  ? 39  SER B CB  1 
ATOM   2175 O OG  . SER B 1 32  ? 104.74800 84.83800  97.03100  1.000 57.18906  ? 39  SER B OG  1 
ATOM   2176 N N   . ALA B 1 33  ? 101.55900 84.99400  96.16800  1.000 44.24922  ? 40  ALA B N   1 
ATOM   2177 C CA  . ALA B 1 33  ? 100.50200 84.11500  95.68300  1.000 44.30001  ? 40  ALA B CA  1 
ATOM   2178 C C   . ALA B 1 33  ? 99.28000  84.86200  95.16600  1.000 45.76790  ? 40  ALA B C   1 
ATOM   2179 O O   . ALA B 1 33  ? 98.66500  84.43200  94.18600  1.000 52.67793  ? 40  ALA B O   1 
ATOM   2180 C CB  . ALA B 1 33  ? 100.07500 83.15400  96.79200  1.000 48.64367  ? 40  ALA B CB  1 
ATOM   2181 N N   . LEU B 1 34  ? 98.91200  85.96900  95.80800  1.000 53.73462  ? 41  LEU B N   1 
ATOM   2182 C CA  . LEU B 1 34  ? 97.73100  86.72400  95.39500  1.000 56.49012  ? 41  LEU B CA  1 
ATOM   2183 C C   . LEU B 1 34  ? 97.87500  87.32700  94.00300  1.000 62.53286  ? 41  LEU B C   1 
ATOM   2184 O O   . LEU B 1 34  ? 96.93200  87.28000  93.20600  1.000 63.04944  ? 41  LEU B O   1 
ATOM   2185 C CB  . LEU B 1 34  ? 97.44000  87.83000  96.40800  1.000 53.35360  ? 41  LEU B CB  1 
ATOM   2186 C CG  . LEU B 1 34  ? 96.92300  87.40000  97.77500  1.000 55.38543  ? 41  LEU B CG  1 
ATOM   2187 C CD1 . LEU B 1 34  ? 96.87200  88.58500  98.71100  1.000 54.69910  ? 41  LEU B CD1 1 
ATOM   2188 C CD2 . LEU B 1 34  ? 95.56100  86.76700  97.63800  1.000 58.97561  ? 41  LEU B CD2 1 
ATOM   2189 N N   . GLU B 1 35  ? 99.03900  87.90400  93.68300  1.000 62.52159  ? 42  GLU B N   1 
ATOM   2190 C CA  . GLU B 1 35  ? 99.09700  88.75900  92.50200  1.000 63.53280  ? 42  GLU B CA  1 
ATOM   2191 C C   . GLU B 1 35  ? 100.40300 88.71000  91.71600  1.000 62.20171  ? 42  GLU B C   1 
ATOM   2192 O O   . GLU B 1 35  ? 100.72900 89.69200  91.04300  1.000 70.85604  ? 42  GLU B O   1 
ATOM   2193 C CB  . GLU B 1 35  ? 98.80800  90.19200  92.91500  1.000 64.46263  ? 42  GLU B CB  1 
ATOM   2194 C CG  . GLU B 1 35  ? 99.80600  90.77800  93.86500  1.000 56.76732  ? 42  GLU B CG  1 
ATOM   2195 C CD  . GLU B 1 35  ? 99.22700  91.94800  94.61800  1.000 67.12682  ? 42  GLU B CD  1 
ATOM   2196 O OE1 . GLU B 1 35  ? 98.33000  92.62300  94.07400  1.000 65.36334  ? 42  GLU B OE1 1 
ATOM   2197 O OE2 . GLU B 1 35  ? 99.66100  92.19300  95.75700  1.000 72.19302  ? 42  GLU B OE2 1 
ATOM   2198 N N   . LEU B 1 36  ? 101.17300 87.62800  91.78600  1.000 62.00596  ? 43  LEU B N   1 
ATOM   2199 C CA  . LEU B 1 36  ? 102.14100 87.36200  90.72700  1.000 60.93720  ? 43  LEU B CA  1 
ATOM   2200 C C   . LEU B 1 36  ? 101.49100 87.10400  89.36900  1.000 65.45069  ? 43  LEU B C   1 
ATOM   2201 O O   . LEU B 1 36  ? 102.06100 87.47300  88.33800  1.000 73.03485  ? 43  LEU B O   1 
ATOM   2202 C CB  . LEU B 1 36  ? 103.01400 86.17400  91.11700  1.000 61.12580  ? 43  LEU B CB  1 
ATOM   2203 C CG  . LEU B 1 36  ? 104.07100 85.74500  90.10600  1.000 63.13085  ? 43  LEU B CG  1 
ATOM   2204 C CD1 . LEU B 1 36  ? 105.05600 86.87000  89.88000  1.000 63.20375  ? 43  LEU B CD1 1 
ATOM   2205 C CD2 . LEU B 1 36  ? 104.78100 84.49800  90.58700  1.000 68.46795  ? 43  LEU B CD2 1 
ATOM   2206 N N   . ALA B 1 37  ? 100.31400 86.47500  89.33200  1.000 73.06015  ? 44  ALA B N   1 
ATOM   2207 C CA  . ALA B 1 37  ? 99.61600  86.27400  88.06000  1.000 75.42437  ? 44  ALA B CA  1 
ATOM   2208 C C   . ALA B 1 37  ? 99.19400  87.58000  87.39100  1.000 77.79192  ? 44  ALA B C   1 
ATOM   2209 O O   . ALA B 1 37  ? 99.24700  87.69500  86.15600  1.000 79.57933  ? 44  ALA B O   1 
ATOM   2210 C CB  . ALA B 1 37  ? 98.39600  85.38400  88.27400  1.000 76.16953  ? 44  ALA B CB  1 
ATOM   2211 N N   . HIS B 1 38  ? 98.88200  88.60200  88.18100  1.000 78.81190  ? 45  HIS B N   1 
ATOM   2212 C CA  . HIS B 1 38  ? 98.48600  89.88900  87.62100  1.000 76.94451  ? 45  HIS B CA  1 
ATOM   2213 C C   . HIS B 1 38  ? 99.67600  90.64300  87.04800  1.000 77.33006  ? 45  HIS B C   1 
ATOM   2214 O O   . HIS B 1 38  ? 99.56400  91.25600  85.98000  1.000 83.18261  ? 45  HIS B O   1 
ATOM   2215 C CB  . HIS B 1 38  ? 97.77800  90.71700  88.69100  1.000 77.45406  ? 45  HIS B CB  1 
ATOM   2216 C CG  . HIS B 1 38  ? 97.21300  92.00700  88.18800  1.000 81.32896  ? 45  HIS B CG  1 
ATOM   2217 N ND1 . HIS B 1 38  ? 97.98500  93.12700  87.97700  1.000 83.42321  ? 45  HIS B ND1 1 
ATOM   2218 C CD2 . HIS B 1 38  ? 95.94700  92.35600  87.86200  1.000 82.32401  ? 45  HIS B CD2 1 
ATOM   2219 C CE1 . HIS B 1 38  ? 97.22000  94.11100  87.53900  1.000 81.99687  ? 45  HIS B CE1 1 
ATOM   2220 N NE2 . HIS B 1 38  ? 95.97900  93.66900  87.46100  1.000 81.72590  ? 45  HIS B NE2 1 
ATOM   2221 N N   . GLU B 1 39  ? 100.80900 90.63400  87.74900  1.000 66.51443  ? 46  GLU B N   1 
ATOM   2222 C CA  . GLU B 1 39  ? 102.02000 91.22100  87.19300  1.000 65.85753  ? 46  GLU B CA  1 
ATOM   2223 C C   . GLU B 1 39  ? 102.33700 90.63200  85.82600  1.000 70.24439  ? 46  GLU B C   1 
ATOM   2224 O O   . GLU B 1 39  ? 102.58700 91.36600  84.86600  1.000 78.71081  ? 46  GLU B O   1 
ATOM   2225 C CB  . GLU B 1 39  ? 103.19200 90.98700  88.14000  1.000 66.47647  ? 46  GLU B CB  1 
ATOM   2226 C CG  . GLU B 1 39  ? 104.52600 91.36900  87.54900  1.000 67.72618  ? 46  GLU B CG  1 
ATOM   2227 C CD  . GLU B 1 39  ? 105.67100 91.10800  88.49400  1.000 72.40357  ? 46  GLU B CD  1 
ATOM   2228 O OE1 . GLU B 1 39  ? 105.46900 90.37200  89.47800  1.000 73.06411  ? 46  GLU B OE1 1 
ATOM   2229 O OE2 . GLU B 1 39  ? 106.77800 91.62600  88.24700  1.000 73.75580  ? 46  GLU B OE2 1 
ATOM   2230 N N   . ARG B 1 40  ? 102.38900 89.30400  85.73400  1.000 72.50863  ? 47  ARG B N   1 
ATOM   2231 C CA  . ARG B 1 40  ? 102.78200 88.66500  84.48300  1.000 74.88419  ? 47  ARG B CA  1 
ATOM   2232 C C   . ARG B 1 40  ? 101.76000 88.88200  83.37500  1.000 76.46377  ? 47  ARG B C   1 
ATOM   2233 O O   . ARG B 1 40  ? 102.14500 89.05500  82.21100  1.000 79.81094  ? 47  ARG B O   1 
ATOM   2234 C CB  . ARG B 1 40  ? 103.03000 87.17700  84.70900  1.000 77.86095  ? 47  ARG B CB  1 
ATOM   2235 C CG  . ARG B 1 40  ? 104.23900 86.91400  85.58800  1.000 80.08972  ? 47  ARG B CG  1 
ATOM   2236 C CD  . ARG B 1 40  ? 104.63400 85.45100  85.60200  1.000 79.97235  ? 47  ARG B CD  1 
ATOM   2237 N NE  . ARG B 1 40  ? 103.62900 84.62200  86.25200  1.000 81.41687  ? 47  ARG B NE  1 
ATOM   2238 C CZ  . ARG B 1 40  ? 103.84600 83.38700  86.68000  1.000 82.56028  ? 47  ARG B CZ  1 
ATOM   2239 N NH1 . ARG B 1 40  ? 105.02600 82.80600  86.54200  1.000 80.73036  ? 47  ARG B NH1 1 
ATOM   2240 N NH2 . ARG B 1 40  ? 102.85600 82.71900  87.26500  1.000 82.33538  ? 47  ARG B NH2 1 
ATOM   2241 N N   . GLN B 1 41  ? 100.47600 89.01400  83.71800  1.000 81.58812  ? 48  GLN B N   1 
ATOM   2242 C CA  . GLN B 1 41  ? 99.50000  89.37700  82.69200  1.000 84.35595  ? 48  GLN B CA  1 
ATOM   2243 C C   . GLN B 1 41  ? 99.70800  90.80300  82.19600  1.000 86.93146  ? 48  GLN B C   1 
ATOM   2244 O O   . GLN B 1 41  ? 99.68700  91.05300  80.98600  1.000 88.58062  ? 48  GLN B O   1 
ATOM   2245 C CB  . GLN B 1 41  ? 98.07700  89.19500  83.21500  1.000 85.17307  ? 48  GLN B CB  1 
ATOM   2246 C CG  . GLN B 1 41  ? 97.65400  87.74700  83.35000  1.000 86.09290  ? 48  GLN B CG  1 
ATOM   2247 C CD  . GLN B 1 41  ? 96.28700  87.59800  83.98000  1.000 90.94031  ? 48  GLN B CD  1 
ATOM   2248 O OE1 . GLN B 1 41  ? 95.59100  88.58300  84.22100  1.000 93.35207  ? 48  GLN B OE1 1 
ATOM   2249 N NE2 . GLN B 1 41  ? 95.89300  86.36000  84.24900  1.000 89.43448  ? 48  GLN B NE2 1 
ATOM   2250 N N   . ALA B 1 42  ? 99.88300  91.75600  83.11000  1.000 83.09016  ? 49  ALA B N   1 
ATOM   2251 C CA  . ALA B 1 42  ? 100.05600 93.14400  82.69200  1.000 80.10225  ? 49  ALA B CA  1 
ATOM   2252 C C   . ALA B 1 42  ? 101.34400 93.34600  81.90000  1.000 81.42895  ? 49  ALA B C   1 
ATOM   2253 O O   . ALA B 1 42  ? 101.36400 94.10700  80.92800  1.000 87.87637  ? 49  ALA B O   1 
ATOM   2254 C CB  . ALA B 1 42  ? 100.03100 94.06600  83.90700  1.000 78.46432  ? 49  ALA B CB  1 
ATOM   2255 N N   . LYS B 1 43  ? 102.42300 92.66100  82.27900  1.000 77.78893  ? 50  LYS B N   1 
ATOM   2256 C CA  . LYS B 1 43  ? 103.65400 92.72800  81.49400  1.000 78.75812  ? 50  LYS B CA  1 
ATOM   2257 C C   . LYS B 1 43  ? 103.50900 92.09100  80.11600  1.000 80.93335  ? 50  LYS B C   1 
ATOM   2258 O O   . LYS B 1 43  ? 104.03400 92.62500  79.13000  1.000 84.39576  ? 50  LYS B O   1 
ATOM   2259 C CB  . LYS B 1 43  ? 104.80600 92.08200  82.25900  1.000 81.47714  ? 50  LYS B CB  1 
ATOM   2260 C CG  . LYS B 1 43  ? 105.24300 92.86800  83.48000  1.000 80.55597  ? 50  LYS B CG  1 
ATOM   2261 C CD  . LYS B 1 43  ? 106.54200 92.33200  84.05800  1.000 81.82721  ? 50  LYS B CD  1 
ATOM   2262 C CE  . LYS B 1 43  ? 107.14100 93.31500  85.04900  1.000 81.24949  ? 50  LYS B CE  1 
ATOM   2263 N NZ  . LYS B 1 43  ? 108.35400 92.78500  85.72000  1.000 79.28451  ? 50  LYS B NZ  1 
ATOM   2264 N N   . GLN B 1 44  ? 102.80100 90.96300  80.00500  1.000 87.63639  ? 51  GLN B N   1 
ATOM   2265 C CA  . GLN B 1 44  ? 102.53800 90.42500  78.67300  1.000 89.71588  ? 51  GLN B CA  1 
ATOM   2266 C C   . GLN B 1 44  ? 101.71600 91.39100  77.82500  1.000 90.20460  ? 51  GLN B C   1 
ATOM   2267 O O   . GLN B 1 44  ? 102.00600 91.58700  76.63700  1.000 93.16720  ? 51  GLN B O   1 
ATOM   2268 C CB  . GLN B 1 44  ? 101.83100 89.07700  78.78100  1.000 92.18747  ? 51  GLN B CB  1 
ATOM   2269 C CG  . GLN B 1 44  ? 101.43200 88.48900  77.44200  1.000 92.87474  ? 51  GLN B CG  1 
ATOM   2270 C CD  . GLN B 1 44  ? 100.74100 87.14800  77.57900  1.000 94.80237  ? 51  GLN B CD  1 
ATOM   2271 O OE1 . GLN B 1 44  ? 100.85200 86.48200  78.60800  1.000 93.64461  ? 51  GLN B OE1 1 
ATOM   2272 N NE2 . GLN B 1 44  ? 100.02600 86.74200  76.53700  1.000 94.63644  ? 51  GLN B NE2 1 
ATOM   2273 N N   . ARG B 1 45  ? 100.67500 91.98500  78.40800  1.000 86.14951  ? 52  ARG B N   1 
ATOM   2274 C CA  . ARG B 1 45  ? 99.84600  92.93100  77.66400  1.000 85.81894  ? 52  ARG B CA  1 
ATOM   2275 C C   . ARG B 1 45  ? 100.63200 94.16700  77.23600  1.000 86.34191  ? 52  ARG B C   1 
ATOM   2276 O O   . ARG B 1 45  ? 100.42700 94.69200  76.13500  1.000 90.16816  ? 52  ARG B O   1 
ATOM   2277 C CB  . ARG B 1 45  ? 98.62900  93.31400  78.50200  1.000 86.62887  ? 52  ARG B CB  1 
ATOM   2278 C CG  . ARG B 1 45  ? 97.55600  94.05400  77.74100  1.000 88.36737  ? 52  ARG B CG  1 
ATOM   2279 C CD  . ARG B 1 45  ? 96.26700  94.11800  78.54500  1.000 89.11182  ? 52  ARG B CD  1 
ATOM   2280 N NE  . ARG B 1 45  ? 96.39100  94.93300  79.74600  1.000 91.54689  ? 52  ARG B NE  1 
ATOM   2281 C CZ  . ARG B 1 45  ? 95.99800  94.54700  80.95200  1.000 93.69781  ? 52  ARG B CZ  1 
ATOM   2282 N NH1 . ARG B 1 45  ? 95.45100  93.36000  81.15400  1.000 92.72671  ? 52  ARG B NH1 1 
ATOM   2283 N NH2 . ARG B 1 45  ? 96.15500  95.37400  81.98200  1.000 92.42876  ? 52  ARG B NH2 1 
ATOM   2284 N N   . TRP B 1 46  ? 101.57200 94.61800  78.06800  1.000 83.51596  ? 53  TRP B N   1 
ATOM   2285 C CA  . TRP B 1 46  ? 102.48300 95.68100  77.64800  1.000 82.73579  ? 53  TRP B CA  1 
ATOM   2286 C C   . TRP B 1 46  ? 103.36600 95.26400  76.48400  1.000 81.80539  ? 53  TRP B C   1 
ATOM   2287 O O   . TRP B 1 46  ? 103.57100 96.04300  75.54900  1.000 83.39706  ? 53  TRP B O   1 
ATOM   2288 C CB  . TRP B 1 46  ? 103.34300 96.15600  78.81500  1.000 80.13653  ? 53  TRP B CB  1 
ATOM   2289 C CG  . TRP B 1 46  ? 104.48500 97.00500  78.35200  1.000 80.52472  ? 53  TRP B CG  1 
ATOM   2290 C CD1 . TRP B 1 46  ? 105.80500 96.69000  78.42900  1.000 82.47454  ? 53  TRP B CD1 1 
ATOM   2291 C CD2 . TRP B 1 46  ? 104.41400 98.24400  77.63800  1.000 82.69320  ? 53  TRP B CD2 1 
ATOM   2292 N NE1 . TRP B 1 46  ? 106.56500 97.68200  77.86800  1.000 84.06115  ? 53  TRP B NE1 1 
ATOM   2293 C CE2 . TRP B 1 46  ? 105.73300 98.64600  77.36700  1.000 82.27513  ? 53  TRP B CE2 1 
ATOM   2294 C CE3 . TRP B 1 46  ? 103.36500 99.06700  77.22500  1.000 86.22063  ? 53  TRP B CE3 1 
ATOM   2295 C CZ2 . TRP B 1 46  ? 106.03200 99.82900  76.70500  1.000 80.04149  ? 53  TRP B CZ2 1 
ATOM   2296 C CZ3 . TRP B 1 46  ? 103.66600 100.24400 76.56600  1.000 84.34827  ? 53  TRP B CZ3 1 
ATOM   2297 C CH2 . TRP B 1 46  ? 104.98700 100.61200 76.31300  1.000 80.13357  ? 53  TRP B CH2 1 
ATOM   2298 N N   . GLU B 1 47  ? 103.97300 94.08400  76.55800  1.000 90.91390  ? 54  GLU B N   1 
ATOM   2299 C CA  . GLU B 1 47  ? 104.81100 93.64800  75.44500  1.000 90.74937  ? 54  GLU B CA  1 
ATOM   2300 C C   . GLU B 1 47  ? 104.01300 93.55200  74.14900  1.000 91.24511  ? 54  GLU B C   1 
ATOM   2301 O O   . GLU B 1 47  ? 104.50700 93.92100  73.07600  1.000 94.23383  ? 54  GLU B O   1 
ATOM   2302 C CB  . GLU B 1 47  ? 105.47000 92.31200  75.77400  1.000 93.62968  ? 54  GLU B CB  1 
ATOM   2303 C CG  . GLU B 1 47  ? 106.55300 92.40900  76.83600  1.000 94.38718  ? 54  GLU B CG  1 
ATOM   2304 C CD  . GLU B 1 47  ? 107.75800 93.20200  76.37500  1.000 97.10358  ? 54  GLU B CD  1 
ATOM   2305 O OE1 . GLU B 1 47  ? 107.96700 93.31600  75.14900  1.000 97.07181  ? 54  GLU B OE1 1 
ATOM   2306 O OE2 . GLU B 1 47  ? 108.49600 93.71500  77.24100  1.000 94.29327  ? 54  GLU B OE2 1 
ATOM   2307 N N   . GLU B 1 48  ? 102.75200 93.12700  74.23900  1.000 92.51434  ? 55  GLU B N   1 
ATOM   2308 C CA  . GLU B 1 48  ? 101.88300 93.10700  73.06300  1.000 91.62433  ? 55  GLU B CA  1 
ATOM   2309 C C   . GLU B 1 48  ? 101.57100 94.50800  72.54100  1.000 93.61394  ? 55  GLU B C   1 
ATOM   2310 O O   . GLU B 1 48  ? 101.58700 94.73600  71.32600  1.000 92.94465  ? 55  GLU B O   1 
ATOM   2311 C CB  . GLU B 1 48  ? 100.58800 92.36800  73.38900  1.000 91.97571  ? 55  GLU B CB  1 
ATOM   2312 C CG  . GLU B 1 48  ? 100.77200 90.88600  73.64000  1.000 95.72756  ? 55  GLU B CG  1 
ATOM   2313 C CD  . GLU B 1 48  ? 99.50800  90.22300  74.14800  1.000 97.07328  ? 55  GLU B CD  1 
ATOM   2314 O OE1 . GLU B 1 48  ? 98.45700  90.89700  74.18600  1.000 97.02625  ? 55  GLU B OE1 1 
ATOM   2315 O OE2 . GLU B 1 48  ? 99.56600  89.02900  74.51100  1.000 96.10375  ? 55  GLU B OE2 1 
ATOM   2316 N N   . ARG B 1 49  ? 101.30500 95.46200  73.43600  1.000 91.35567  ? 56  ARG B N   1 
ATOM   2317 C CA  . ARG B 1 49  ? 101.06500 96.83600  72.99500  1.000 88.13686  ? 56  ARG B CA  1 
ATOM   2318 C C   . ARG B 1 49  ? 102.30000 97.45300  72.35000  1.000 88.11820  ? 56  ARG B C   1 
ATOM   2319 O O   . ARG B 1 49  ? 102.19600 98.13300  71.32300  1.000 89.35812  ? 56  ARG B O   1 
ATOM   2320 C CB  . ARG B 1 49  ? 100.60300 97.69000  74.17300  1.000 85.39481  ? 56  ARG B CB  1 
ATOM   2321 C CG  . ARG B 1 49  ? 99.16800  97.44500  74.58700  1.000 87.22006  ? 56  ARG B CG  1 
ATOM   2322 C CD  . ARG B 1 49  ? 98.81900  98.22100  75.83900  1.000 85.50560  ? 56  ARG B CD  1 
ATOM   2323 N NE  . ARG B 1 49  ? 97.41800  98.06200  76.20600  1.000 85.86574  ? 56  ARG B NE  1 
ATOM   2324 C CZ  . ARG B 1 49  ? 96.94700  98.21200  77.43500  1.000 89.04893  ? 56  ARG B CZ  1 
ATOM   2325 N NH1 . ARG B 1 49  ? 97.74500  98.49700  78.45100  1.000 89.01513  ? 56  ARG B NH1 1 
ATOM   2326 N NH2 . ARG B 1 49  ? 95.64400  98.06700  77.65200  1.000 89.23494  ? 56  ARG B NH2 1 
ATOM   2327 N N   . LEU B 1 50  ? 103.47200 97.24600  72.94400  1.000 88.79787  ? 57  LEU B N   1 
ATOM   2328 C CA  . LEU B 1 50  ? 104.70400 97.76900  72.36500  1.000 87.39111  ? 57  LEU B CA  1 
ATOM   2329 C C   . LEU B 1 50  ? 104.99900 97.14700  71.00700  1.000 89.09216  ? 57  LEU B C   1 
ATOM   2330 O O   . LEU B 1 50  ? 105.44600 97.84000  70.08700  1.000 90.00499  ? 57  LEU B O   1 
ATOM   2331 C CB  . LEU B 1 50  ? 105.87100 97.54100  73.32200  1.000 88.04304  ? 57  LEU B CB  1 
ATOM   2332 C CG  . LEU B 1 50  ? 107.22800 98.03400  72.83200  1.000 87.94788  ? 57  LEU B CG  1 
ATOM   2333 C CD1 . LEU B 1 50  ? 107.19000 99.52900  72.65000  1.000 89.94263  ? 57  LEU B CD1 1 
ATOM   2334 C CD2 . LEU B 1 50  ? 108.31700 97.65000  73.80900  1.000 87.60600  ? 57  LEU B CD2 1 
ATOM   2335 N N   . ALA B 1 51  ? 104.74600 95.84600  70.85300  1.000 96.85396  ? 58  ALA B N   1 
ATOM   2336 C CA  . ALA B 1 51  ? 104.89100 95.21000  69.54600  1.000 95.61715  ? 58  ALA B CA  1 
ATOM   2337 C C   . ALA B 1 51  ? 103.92600 95.79200  68.51800  1.000 96.63344  ? 58  ALA B C   1 
ATOM   2338 O O   . ALA B 1 51  ? 104.31500 96.06800  67.37600  1.000 95.86287  ? 58  ALA B O   1 
ATOM   2339 C CB  . ALA B 1 51  ? 104.68800 93.70200  69.67600  1.000 97.07062  ? 58  ALA B CB  1 
ATOM   2340 N N   . ASN B 1 52  ? 102.65700 95.96400  68.89300  1.000 100.26186 ? 59  ASN B N   1 
ATOM   2341 C CA  . ASN B 1 52  ? 101.69400 96.56800  67.97500  1.000 99.61096  ? 59  ASN B CA  1 
ATOM   2342 C C   . ASN B 1 52  ? 102.09600 97.98000  67.56500  1.000 99.74284  ? 59  ASN B C   1 
ATOM   2343 O O   . ASN B 1 52  ? 101.96500 98.35000  66.39400  1.000 100.26432 ? 59  ASN B O   1 
ATOM   2344 C CB  . ASN B 1 52  ? 100.30000 96.58100  68.60100  1.000 99.67443  ? 59  ASN B CB  1 
ATOM   2345 C CG  . ASN B 1 52  ? 99.63600  95.22300  68.57700  1.000 100.88963 ? 59  ASN B CG  1 
ATOM   2346 O OD1 . ASN B 1 52  ? 100.08800 94.31100  67.88800  1.000 100.96943 ? 59  ASN B OD1 1 
ATOM   2347 N ND2 . ASN B 1 52  ? 98.54500  95.08500  69.32000  1.000 100.32618 ? 59  ASN B ND2 1 
ATOM   2348 N N   . PHE B 1 53  ? 102.59500 98.78000  68.50600  1.000 96.92804  ? 60  PHE B N   1 
ATOM   2349 C CA  . PHE B 1 53  ? 103.04200 100.12600 68.15300  1.000 96.52242  ? 60  PHE B CA  1 
ATOM   2350 C C   . PHE B 1 53  ? 104.27400 100.09800 67.25400  1.000 97.69975  ? 60  PHE B C   1 
ATOM   2351 O O   . PHE B 1 53  ? 104.35400 100.86000 66.28500  1.000 97.82535  ? 60  PHE B O   1 
ATOM   2352 C CB  . PHE B 1 53  ? 103.32000 100.93300 69.41900  1.000 95.81447  ? 60  PHE B CB  1 
ATOM   2353 C CG  . PHE B 1 53  ? 103.41000 102.41300 69.18700  1.000 97.37363  ? 60  PHE B CG  1 
ATOM   2354 C CD1 . PHE B 1 53  ? 102.27200 103.19700 69.20200  1.000 96.14320  ? 60  PHE B CD1 1 
ATOM   2355 C CD2 . PHE B 1 53  ? 104.62800 103.02100 68.95900  1.000 97.53246  ? 60  PHE B CD2 1 
ATOM   2356 C CE1 . PHE B 1 53  ? 102.34900 104.55400 68.99300  1.000 93.73600  ? 60  PHE B CE1 1 
ATOM   2357 C CE2 . PHE B 1 53  ? 104.70800 104.38000 68.75000  1.000 96.26283  ? 60  PHE B CE2 1 
ATOM   2358 C CZ  . PHE B 1 53  ? 103.56800 105.14500 68.76700  1.000 94.39728  ? 60  PHE B CZ  1 
ATOM   2359 N N   . SER B 1 54  ? 105.24500 99.23800  67.56300  1.000 105.16631 ? 61  SER B N   1 
ATOM   2360 C CA  . SER B 1 54  ? 106.43100 99.10000  66.72000  1.000 104.03978 ? 61  SER B CA  1 
ATOM   2361 C C   . SER B 1 54  ? 106.06200 98.73000  65.28900  1.000 104.60679 ? 61  SER B C   1 
ATOM   2362 O O   . SER B 1 54  ? 106.54700 99.34300  64.33100  1.000 104.74157 ? 61  SER B O   1 
ATOM   2363 C CB  . SER B 1 54  ? 107.37200 98.05300  67.31200  1.000 106.15268 ? 61  SER B CB  1 
ATOM   2364 O OG  . SER B 1 54  ? 107.75900 98.39500  68.62800  1.000 107.63522 ? 61  SER B OG  1 
ATOM   2365 N N   . ARG B 1 55  ? 105.20800 97.71900  65.12600  1.000 111.34222 ? 62  ARG B N   1 
ATOM   2366 C CA  . ARG B 1 55  ? 104.80400 97.28600  63.79200  1.000 112.00661 ? 62  ARG B CA  1 
ATOM   2367 C C   . ARG B 1 55  ? 103.96700 98.33700  63.07300  1.000 112.35880 ? 62  ARG B C   1 
ATOM   2368 O O   . ARG B 1 55  ? 104.14900 98.56100  61.87100  1.000 111.16274 ? 62  ARG B O   1 
ATOM   2369 C CB  . ARG B 1 55  ? 104.04000 95.96600  63.88200  1.000 111.21973 ? 62  ARG B CB  1 
ATOM   2370 C CG  . ARG B 1 55  ? 103.76500 95.32600  62.53300  1.000 112.19081 ? 62  ARG B CG  1 
ATOM   2371 C CD  . ARG B 1 55  ? 103.06200 93.98900  62.68000  1.000 112.49950 ? 62  ARG B CD  1 
ATOM   2372 N NE  . ARG B 1 55  ? 101.70800 94.13500  63.19600  1.000 114.52349 ? 62  ARG B NE  1 
ATOM   2373 C CZ  . ARG B 1 55  ? 101.34800 93.84500  64.43900  1.000 113.60119 ? 62  ARG B CZ  1 
ATOM   2374 N NH1 . ARG B 1 55  ? 102.21800 93.37500  65.31700  1.000 111.01886 ? 62  ARG B NH1 1 
ATOM   2375 N NH2 . ARG B 1 55  ? 100.08400 94.02800  64.80800  1.000 112.67276 ? 62  ARG B NH2 1 
ATOM   2376 N N   . GLY B 1 56  ? 103.04600 98.98900  63.78100  1.000 112.76055 ? 63  GLY B N   1 
ATOM   2377 C CA  . GLY B 1 56  ? 102.11900 99.89000  63.11500  1.000 112.29937 ? 63  GLY B CA  1 
ATOM   2378 C C   . GLY B 1 56  ? 102.76100 101.14100 62.54500  1.000 114.20755 ? 63  GLY B C   1 
ATOM   2379 O O   . GLY B 1 56  ? 102.34700 101.63100 61.49100  1.000 115.35162 ? 63  GLY B O   1 
ATOM   2380 N N   . HIS B 1 57  ? 103.77400 101.68100 63.22200  1.000 110.31582 ? 64  HIS B N   1 
ATOM   2381 C CA  . HIS B 1 57  ? 104.37700 102.94100 62.80400  1.000 110.49790 ? 64  HIS B CA  1 
ATOM   2382 C C   . HIS B 1 57  ? 105.78000 102.79100 62.22600  1.000 110.46430 ? 64  HIS B C   1 
ATOM   2383 O O   . HIS B 1 57  ? 106.47100 103.79900 62.04600  1.000 109.70201 ? 64  HIS B O   1 
ATOM   2384 C CB  . HIS B 1 57  ? 104.38900 103.92200 63.97600  1.000 109.38882 ? 64  HIS B CB  1 
ATOM   2385 C CG  . HIS B 1 57  ? 103.03100 104.18200 64.54800  1.000 108.58502 ? 64  HIS B CG  1 
ATOM   2386 N ND1 . HIS B 1 57  ? 102.05200 104.86100 63.85700  1.000 108.90761 ? 64  HIS B ND1 1 
ATOM   2387 C CD2 . HIS B 1 57  ? 102.48200 103.83600 65.73500  1.000 108.60960 ? 64  HIS B CD2 1 
ATOM   2388 C CE1 . HIS B 1 57  ? 100.96200 104.93200 64.59800  1.000 109.28508 ? 64  HIS B CE1 1 
ATOM   2389 N NE2 . HIS B 1 57  ? 101.19600 104.31700 65.74300  1.000 109.70600 ? 64  HIS B NE2 1 
ATOM   2390 N N   . ASN B 1 58  ? 106.21400 101.56700 61.92600  1.000 113.80202 ? 65  ASN B N   1 
ATOM   2391 C CA  . ASN B 1 58  ? 107.56100 101.30500 61.41500  1.000 114.28704 ? 65  ASN B CA  1 
ATOM   2392 C C   . ASN B 1 58  ? 108.63700 101.89600 62.32500  1.000 112.33105 ? 65  ASN B C   1 
ATOM   2393 O O   . ASN B 1 58  ? 109.58000 102.55300 61.87800  1.000 110.73493 ? 65  ASN B O   1 
ATOM   2394 C CB  . ASN B 1 58  ? 107.70400 101.82300 59.98100  1.000 114.65370 ? 65  ASN B CB  1 
ATOM   2395 C CG  . ASN B 1 58  ? 108.96800 101.33000 59.30600  1.000 115.63232 ? 65  ASN B CG  1 
ATOM   2396 O OD1 . ASN B 1 58  ? 109.47100 100.25100 59.61700  1.000 115.81752 ? 65  ASN B OD1 1 
ATOM   2397 N ND2 . ASN B 1 58  ? 109.48900 102.12000 58.37500  1.000 113.76145 ? 65  ASN B ND2 1 
ATOM   2398 N N   . LEU B 1 59  ? 108.48400 101.66800 63.62500  1.000 109.79929 ? 66  LEU B N   1 
ATOM   2399 C CA  . LEU B 1 59  ? 109.42000 102.15700 64.62800  1.000 111.04168 ? 66  LEU B CA  1 
ATOM   2400 C C   . LEU B 1 59  ? 110.16700 100.98300 65.24200  1.000 111.20603 ? 66  LEU B C   1 
ATOM   2401 O O   . LEU B 1 59  ? 109.54900 99.99000  65.63900  1.000 109.37395 ? 66  LEU B O   1 
ATOM   2402 C CB  . LEU B 1 59  ? 108.69600 102.94700 65.71700  1.000 110.92201 ? 66  LEU B CB  1 
ATOM   2403 C CG  . LEU B 1 59  ? 108.46300 104.42600 65.43100  1.000 109.11955 ? 66  LEU B CG  1 
ATOM   2404 C CD1 . LEU B 1 59  ? 107.47400 104.98500 66.42400  1.000 108.06032 ? 66  LEU B CD1 1 
ATOM   2405 C CD2 . LEU B 1 59  ? 109.77200 105.18600 65.49300  1.000 109.21416 ? 66  LEU B CD2 1 
ATOM   2406 N N   . SER B 1 60  ? 111.48900 101.10100 65.32200  1.000 108.69618 ? 67  SER B N   1 
ATOM   2407 C CA  . SER B 1 60  ? 112.29300 100.09100 65.98900  1.000 105.73280 ? 67  SER B CA  1 
ATOM   2408 C C   . SER B 1 60  ? 112.20400 100.24200 67.50100  1.000 105.38823 ? 67  SER B C   1 
ATOM   2409 O O   . SER B 1 60  ? 111.99500 101.33600 68.02900  1.000 106.05726 ? 67  SER B O   1 
ATOM   2410 C CB  . SER B 1 60  ? 113.75100 100.18700 65.54600  1.000 105.62930 ? 67  SER B CB  1 
ATOM   2411 O OG  . SER B 1 60  ? 114.53800 99.19200  66.17400  1.000 105.70894 ? 67  SER B OG  1 
ATOM   2412 N N   . ARG B 1 61  ? 112.37100 99.11700  68.19800  1.000 108.92879 ? 68  ARG B N   1 
ATOM   2413 C CA  . ARG B 1 61  ? 112.44000 99.12100  69.65500  1.000 109.71230 ? 68  ARG B CA  1 
ATOM   2414 C C   . ARG B 1 61  ? 113.59100 99.95700  70.20200  1.000 109.39192 ? 68  ARG B C   1 
ATOM   2415 O O   . ARG B 1 61  ? 113.54200 100.36200 71.36600  1.000 110.00495 ? 68  ARG B O   1 
ATOM   2416 C CB  . ARG B 1 61  ? 112.54300 97.68600  70.16700  1.000 108.59439 ? 68  ARG B CB  1 
ATOM   2417 C CG  . ARG B 1 61  ? 111.22600 96.92900  70.13100  1.000 107.39876 ? 68  ARG B CG  1 
ATOM   2418 C CD  . ARG B 1 61  ? 111.40200 95.50500  70.61800  1.000 108.18761 ? 68  ARG B CD  1 
ATOM   2419 N NE  . ARG B 1 61  ? 110.13100 94.80900  70.77400  1.000 110.45628 ? 68  ARG B NE  1 
ATOM   2420 C CZ  . ARG B 1 61  ? 109.63300 94.41500  71.93800  1.000 110.91949 ? 68  ARG B CZ  1 
ATOM   2421 N NH1 . ARG B 1 61  ? 110.27000 94.64400  73.07500  1.000 108.29163 ? 68  ARG B NH1 1 
ATOM   2422 N NH2 . ARG B 1 61  ? 108.47000 93.77100  71.96100  1.000 109.60381 ? 68  ARG B NH2 1 
ATOM   2423 N N   . ASP B 1 62  ? 114.61700 100.23500 69.39800  1.000 102.63539 ? 69  ASP B N   1 
ATOM   2424 C CA  . ASP B 1 62  ? 115.67100 101.15300 69.82300  1.000 101.59843 ? 69  ASP B CA  1 
ATOM   2425 C C   . ASP B 1 62  ? 115.15400 102.58000 69.97700  1.000 102.64857 ? 69  ASP B C   1 
ATOM   2426 O O   . ASP B 1 62  ? 115.33700 103.21000 71.02700  1.000 102.87870 ? 69  ASP B O   1 
ATOM   2427 C CB  . ASP B 1 62  ? 116.83400 101.10800 68.83200  1.000 101.51082 ? 69  ASP B CB  1 
ATOM   2428 N N   . GLU B 1 63  ? 114.50400 103.10800 68.93700  1.000 102.53827 ? 70  GLU B N   1 
ATOM   2429 C CA  . GLU B 1 63  ? 113.94100 104.45200 69.02000  1.000 101.13956 ? 70  GLU B CA  1 
ATOM   2430 C C   . GLU B 1 63  ? 112.89200 104.55000 70.11700  1.000 100.59682 ? 70  GLU B C   1 
ATOM   2431 O O   . GLU B 1 63  ? 112.84600 105.54200 70.85500  1.000 102.45458 ? 70  GLU B O   1 
ATOM   2432 C CB  . GLU B 1 63  ? 113.33200 104.84700 67.67500  1.000 101.18316 ? 70  GLU B CB  1 
ATOM   2433 C CG  . GLU B 1 63  ? 114.30200 105.48700 66.69900  1.000 101.26483 ? 70  GLU B CG  1 
ATOM   2434 C CD  . GLU B 1 63  ? 115.45900 104.58000 66.34300  1.000 103.05776 ? 70  GLU B CD  1 
ATOM   2435 O OE1 . GLU B 1 63  ? 115.21500 103.38900 66.05800  1.000 102.92415 ? 70  GLU B OE1 1 
ATOM   2436 O OE2 . GLU B 1 63  ? 116.61300 105.05700 66.34500  1.000 103.15406 ? 70  GLU B OE2 1 
ATOM   2437 N N   . LEU B 1 64  ? 112.03400 103.53900 70.23300  1.000 95.47080  ? 71  LEU B N   1 
ATOM   2438 C CA  . LEU B 1 64  ? 111.01500 103.55400 71.27500  1.000 95.67167  ? 71  LEU B CA  1 
ATOM   2439 C C   . LEU B 1 64  ? 111.62300 103.47900 72.66900  1.000 95.10963  ? 71  LEU B C   1 
ATOM   2440 O O   . LEU B 1 64  ? 111.14500 104.14800 73.58600  1.000 96.72811  ? 71  LEU B O   1 
ATOM   2441 C CB  . LEU B 1 64  ? 110.02100 102.41900 71.06000  1.000 95.34429  ? 71  LEU B CB  1 
ATOM   2442 C CG  . LEU B 1 64  ? 109.14300 102.60200 69.82700  1.000 97.05668  ? 71  LEU B CG  1 
ATOM   2443 C CD1 . LEU B 1 64  ? 108.41600 101.32100 69.50200  1.000 97.89715  ? 71  LEU B CD1 1 
ATOM   2444 C CD2 . LEU B 1 64  ? 108.16300 103.73200 70.04600  1.000 97.62462  ? 71  LEU B CD2 1 
ATOM   2445 N N   . ARG B 1 65  ? 112.65200 102.65200 72.86400  1.000 89.22755  ? 72  ARG B N   1 
ATOM   2446 C CA  . ARG B 1 65  ? 113.33600 102.63200 74.15300  1.000 89.36704  ? 72  ARG B CA  1 
ATOM   2447 C C   . ARG B 1 65  ? 113.98400 103.97300 74.47700  1.000 93.03617  ? 72  ARG B C   1 
ATOM   2448 O O   . ARG B 1 65  ? 113.95500 104.41600 75.62900  1.000 95.98716  ? 72  ARG B O   1 
ATOM   2449 C CB  . ARG B 1 65  ? 114.38100 101.51800 74.17300  1.000 89.98411  ? 72  ARG B CB  1 
ATOM   2450 N N   . GLY B 1 66  ? 114.53700 104.65400 73.47500  1.000 90.53167  ? 73  GLY B N   1 
ATOM   2451 C CA  . GLY B 1 66  ? 115.04700 106.00000 73.70700  1.000 89.50671  ? 73  GLY B CA  1 
ATOM   2452 C C   . GLY B 1 66  ? 113.96800 106.98300 74.12700  1.000 88.12237  ? 73  GLY B C   1 
ATOM   2453 O O   . GLY B 1 66  ? 114.12000 107.73000 75.10300  1.000 89.64589  ? 73  GLY B O   1 
ATOM   2454 N N   . PHE B 1 67  ? 112.85400 106.98400 73.39900  1.000 83.94147  ? 74  PHE B N   1 
ATOM   2455 C CA  . PHE B 1 67  ? 111.74200 107.87000 73.72400  1.000 81.90843  ? 74  PHE B CA  1 
ATOM   2456 C C   . PHE B 1 67  ? 111.19400 107.58300 75.11700  1.000 83.23079  ? 74  PHE B C   1 
ATOM   2457 O O   . PHE B 1 67  ? 110.92200 108.50600 75.89300  1.000 86.54337  ? 74  PHE B O   1 
ATOM   2458 C CB  . PHE B 1 67  ? 110.66000 107.73000 72.65600  1.000 84.08866  ? 74  PHE B CB  1 
ATOM   2459 C CG  . PHE B 1 67  ? 109.46000 108.59100 72.88300  1.000 85.52422  ? 74  PHE B CG  1 
ATOM   2460 C CD1 . PHE B 1 67  ? 109.55300 109.96400 72.78700  1.000 83.67154  ? 74  PHE B CD1 1 
ATOM   2461 C CD2 . PHE B 1 67  ? 108.22700 108.02700 73.14300  1.000 88.31329  ? 74  PHE B CD2 1 
ATOM   2462 C CE1 . PHE B 1 67  ? 108.45000 110.75700 72.98000  1.000 84.24996  ? 74  PHE B CE1 1 
ATOM   2463 C CE2 . PHE B 1 67  ? 107.11900 108.81600 73.33400  1.000 85.70409  ? 74  PHE B CE2 1 
ATOM   2464 C CZ  . PHE B 1 67  ? 107.23100 110.18300 73.25300  1.000 85.54563  ? 74  PHE B CZ  1 
ATOM   2465 N N   . LEU B 1 68  ? 111.00200 106.30800 75.45000  1.000 77.83740  ? 75  LEU B N   1 
ATOM   2466 C CA  . LEU B 1 68  ? 110.52600 105.96600 76.78300  1.000 75.03919  ? 75  LEU B CA  1 
ATOM   2467 C C   . LEU B 1 68  ? 111.54300 106.30100 77.86800  1.000 78.29145  ? 75  LEU B C   1 
ATOM   2468 O O   . LEU B 1 68  ? 111.15100 106.59300 78.99800  1.000 82.24826  ? 75  LEU B O   1 
ATOM   2469 C CB  . LEU B 1 68  ? 110.15600 104.49000 76.84100  1.000 75.42055  ? 75  LEU B CB  1 
ATOM   2470 C CG  . LEU B 1 68  ? 108.98100 104.12400 75.94100  1.000 78.30696  ? 75  LEU B CG  1 
ATOM   2471 C CD1 . LEU B 1 68  ? 108.74700 102.63000 75.94700  1.000 79.92843  ? 75  LEU B CD1 1 
ATOM   2472 C CD2 . LEU B 1 68  ? 107.74400 104.86800 76.38200  1.000 77.06832  ? 75  LEU B CD2 1 
ATOM   2473 N N   . ARG B 1 69  ? 112.84200 106.24200 77.57300  1.000 81.52753  ? 76  ARG B N   1 
ATOM   2474 C CA  . ARG B 1 69  ? 113.82700 106.70800 78.54400  1.000 80.98840  ? 76  ARG B CA  1 
ATOM   2475 C C   . ARG B 1 69  ? 113.69300 108.20500 78.80000  1.000 84.30555  ? 76  ARG B C   1 
ATOM   2476 O O   . ARG B 1 69  ? 113.77600 108.66600 79.95000  1.000 86.17161  ? 76  ARG B O   1 
ATOM   2477 C CB  . ARG B 1 69  ? 115.23400 106.37400 78.05800  1.000 80.79482  ? 76  ARG B CB  1 
ATOM   2478 C CG  . ARG B 1 69  ? 116.29600 106.45600 79.13100  1.000 83.00065  ? 76  ARG B CG  1 
ATOM   2479 C CD  . ARG B 1 69  ? 117.67100 106.21400 78.54000  1.000 84.31927  ? 76  ARG B CD  1 
ATOM   2480 N NE  . ARG B 1 69  ? 117.74800 104.92200 77.87000  1.000 87.55156  ? 76  ARG B NE  1 
ATOM   2481 C CZ  . ARG B 1 69  ? 118.00000 103.77400 78.48300  1.000 87.20774  ? 76  ARG B CZ  1 
ATOM   2482 N NH1 . ARG B 1 69  ? 118.20400 103.71900 79.78800  1.000 84.79633  ? 76  ARG B NH1 1 
ATOM   2483 N NH2 . ARG B 1 69  ? 118.04700 102.65400 77.76800  1.000 84.83515  ? 76  ARG B NH2 1 
ATOM   2484 N N   . HIS B 1 70  ? 113.38900 108.97100 77.75100  1.000 82.32795  ? 77  HIS B N   1 
ATOM   2485 C CA  . HIS B 1 70  ? 113.10700 110.38700 77.96300  1.000 74.81795  ? 77  HIS B CA  1 
ATOM   2486 C C   . HIS B 1 70  ? 111.81600 110.60100 78.74000  1.000 75.23100  ? 77  HIS B C   1 
ATOM   2487 O O   . HIS B 1 70  ? 111.72400 111.54500 79.52700  1.000 79.72743  ? 77  HIS B O   1 
ATOM   2488 C CB  . HIS B 1 70  ? 113.04000 111.13000 76.63200  1.000 78.45033  ? 77  HIS B CB  1 
ATOM   2489 C CG  . HIS B 1 70  ? 114.29100 111.03200 75.82100  1.000 82.27496  ? 77  HIS B CG  1 
ATOM   2490 N ND1 . HIS B 1 70  ? 115.54200 111.25200 76.35500  1.000 82.33572  ? 77  HIS B ND1 1 
ATOM   2491 C CD2 . HIS B 1 70  ? 114.48500 110.76000 74.50900  1.000 81.79188  ? 77  HIS B CD2 1 
ATOM   2492 C CE1 . HIS B 1 70  ? 116.45300 111.10500 75.41100  1.000 82.55284  ? 77  HIS B CE1 1 
ATOM   2493 N NE2 . HIS B 1 70  ? 115.83800 110.80700 74.28100  1.000 82.77248  ? 77  HIS B NE2 1 
ATOM   2494 N N   . TYR B 1 71  ? 110.81400 109.75000 78.53600  1.000 72.48613  ? 78  TYR B N   1 
ATOM   2495 C CA  . TYR B 1 71  ? 109.59400 109.87300 79.33000  1.000 71.48229  ? 78  TYR B CA  1 
ATOM   2496 C C   . TYR B 1 71  ? 109.78900 109.46200 80.78300  1.000 68.56121  ? 78  TYR B C   1 
ATOM   2497 O O   . TYR B 1 71  ? 109.14400 110.02600 81.67000  1.000 73.61141  ? 78  TYR B O   1 
ATOM   2498 C CB  . TYR B 1 71  ? 108.47400 109.03900 78.72100  1.000 72.43785  ? 78  TYR B CB  1 
ATOM   2499 C CG  . TYR B 1 71  ? 107.11600 109.37800 79.27400  1.000 71.30989  ? 78  TYR B CG  1 
ATOM   2500 C CD1 . TYR B 1 71  ? 106.54700 110.62100 79.07500  1.000 72.39892  ? 78  TYR B CD1 1 
ATOM   2501 C CD2 . TYR B 1 71  ? 106.41300 108.45100 80.02400  1.000 70.24568  ? 78  TYR B CD2 1 
ATOM   2502 C CE1 . TYR B 1 71  ? 105.30300 110.91800 79.58500  1.000 72.48003  ? 78  TYR B CE1 1 
ATOM   2503 C CE2 . TYR B 1 71  ? 105.18100 108.74200 80.54100  1.000 65.20796  ? 78  TYR B CE2 1 
ATOM   2504 C CZ  . TYR B 1 71  ? 104.62900 109.97300 80.31900  1.000 68.69849  ? 78  TYR B CZ  1 
ATOM   2505 O OH  . TYR B 1 71  ? 103.40000 110.26300 80.85200  1.000 76.06926  ? 78  TYR B OH  1 
ATOM   2506 N N   . GLU B 1 72  ? 110.66400 108.49800 81.05200  1.000 67.30648  ? 79  GLU B N   1 
ATOM   2507 C CA  . GLU B 1 72  ? 111.01900 108.18700 82.43300  1.000 69.87722  ? 79  GLU B CA  1 
ATOM   2508 C C   . GLU B 1 72  ? 111.73900 109.34700 83.09700  1.000 74.47961  ? 79  GLU B C   1 
ATOM   2509 O O   . GLU B 1 72  ? 111.57500 109.58300 84.29800  1.000 78.53185  ? 79  GLU B O   1 
ATOM   2510 C CB  . GLU B 1 72  ? 111.86900 106.92200 82.50100  1.000 74.71305  ? 79  GLU B CB  1 
ATOM   2511 C CG  . GLU B 1 72  ? 111.09600 105.65400 82.23200  1.000 76.28484  ? 79  GLU B CG  1 
ATOM   2512 C CD  . GLU B 1 72  ? 111.93500 104.41900 82.43200  1.000 76.11376  ? 79  GLU B CD  1 
ATOM   2513 O OE1 . GLU B 1 72  ? 113.06300 104.54500 82.94900  1.000 76.42320  ? 79  GLU B OE1 1 
ATOM   2514 O OE2 . GLU B 1 72  ? 111.46500 103.32100 82.08000  1.000 76.78494  ? 79  GLU B OE2 1 
ATOM   2515 N N   . GLU B 1 73  ? 112.55200 110.07500 82.33700  1.000 77.09231  ? 80  GLU B N   1 
ATOM   2516 C CA  . GLU B 1 73  ? 113.15200 111.29000 82.88000  1.000 75.80317  ? 80  GLU B CA  1 
ATOM   2517 C C   . GLU B 1 73  ? 112.11500 112.38700 83.11800  1.000 76.33793  ? 80  GLU B C   1 
ATOM   2518 O O   . GLU B 1 73  ? 112.14600 113.06200 84.15100  1.000 73.89504  ? 80  GLU B O   1 
ATOM   2519 C CB  . GLU B 1 73  ? 114.25300 111.78000 81.94500  1.000 76.49949  ? 80  GLU B CB  1 
ATOM   2520 C CG  . GLU B 1 73  ? 114.97500 113.01800 82.41800  1.000 79.67598  ? 80  GLU B CG  1 
ATOM   2521 C CD  . GLU B 1 73  ? 116.09700 113.41300 81.48200  1.000 84.44724  ? 80  GLU B CD  1 
ATOM   2522 O OE1 . GLU B 1 73  ? 116.96600 112.56000 81.20600  1.000 83.90209  ? 80  GLU B OE1 1 
ATOM   2523 O OE2 . GLU B 1 73  ? 116.10600 114.57000 81.01500  1.000 82.62929  ? 80  GLU B OE2 1 
ATOM   2524 N N   . ALA B 1 74  ? 111.19800 112.58700 82.17000  1.000 77.69990  ? 81  ALA B N   1 
ATOM   2525 C CA  . ALA B 1 74  ? 110.17100 113.62000 82.30100  1.000 70.68806  ? 81  ALA B CA  1 
ATOM   2526 C C   . ALA B 1 74  ? 109.18200 113.34200 83.42900  1.000 68.48070  ? 81  ALA B C   1 
ATOM   2527 O O   . ALA B 1 74  ? 108.74600 114.27500 84.11000  1.000 75.34082  ? 81  ALA B O   1 
ATOM   2528 C CB  . ALA B 1 74  ? 109.42400 113.78200 80.98100  1.000 71.97838  ? 81  ALA B CB  1 
ATOM   2529 N N   . THR B 1 75  ? 108.80200 112.08000 83.64100  1.000 70.50533  ? 82  THR B N   1 
ATOM   2530 C CA  . THR B 1 75  ? 107.87600 111.75600 84.72700  1.000 69.92524  ? 82  THR B CA  1 
ATOM   2531 C C   . THR B 1 75  ? 108.48200 111.96700 86.10600  1.000 71.73939  ? 82  THR B C   1 
ATOM   2532 O O   . THR B 1 75  ? 107.75800 112.29800 87.04900  1.000 75.08145  ? 82  THR B O   1 
ATOM   2533 C CB  . THR B 1 75  ? 107.37900 110.31800 84.61600  1.000 69.04611  ? 82  THR B CB  1 
ATOM   2534 O OG1 . THR B 1 75  ? 108.49100 109.43900 84.42100  1.000 74.11705  ? 82  THR B OG1 1 
ATOM   2535 C CG2 . THR B 1 75  ? 106.40500 110.17600 83.47100  1.000 72.04913  ? 82  THR B CG2 1 
ATOM   2536 N N   . ARG B 1 76  ? 109.78900 111.77600 86.25900  1.000 70.07184  ? 83  ARG B N   1 
ATOM   2537 C CA  . ARG B 1 76  ? 110.41400 112.13300 87.52500  1.000 69.42858  ? 83  ARG B CA  1 
ATOM   2538 C C   . ARG B 1 76  ? 110.39500 113.63700 87.76400  1.000 73.33679  ? 83  ARG B C   1 
ATOM   2539 O O   . ARG B 1 76  ? 110.29400 114.07300 88.91500  1.000 79.20417  ? 83  ARG B O   1 
ATOM   2540 C CB  . ARG B 1 76  ? 111.84800 111.60900 87.55900  1.000 70.24647  ? 83  ARG B CB  1 
ATOM   2541 C CG  . ARG B 1 76  ? 112.58200 111.81200 88.87300  1.000 71.82553  ? 83  ARG B CG  1 
ATOM   2542 C CD  . ARG B 1 76  ? 111.74700 111.45000 90.09700  1.000 73.26258  ? 83  ARG B CD  1 
ATOM   2543 N NE  . ARG B 1 76  ? 111.13500 110.13000 90.00000  1.000 78.11447  ? 83  ARG B NE  1 
ATOM   2544 C CZ  . ARG B 1 76  ? 110.09700 109.73100 90.72200  1.000 77.30651  ? 83  ARG B CZ  1 
ATOM   2545 N NH1 . ARG B 1 76  ? 109.53500 110.52200 91.62100  1.000 68.83231  ? 83  ARG B NH1 1 
ATOM   2546 N NH2 . ARG B 1 76  ? 109.61300 108.50600 90.54100  1.000 75.84857  ? 83  ARG B NH2 1 
ATOM   2547 N N   . ALA B 1 77  ? 110.47700 114.44300 86.70800  1.000 71.97081  ? 84  ALA B N   1 
ATOM   2548 C CA  . ALA B 1 77  ? 110.23000 115.87600 86.83700  1.000 71.42767  ? 84  ALA B CA  1 
ATOM   2549 C C   . ALA B 1 77  ? 108.76100 116.23000 87.01300  1.000 71.98741  ? 84  ALA B C   1 
ATOM   2550 O O   . ALA B 1 77  ? 108.45400 117.41700 87.14600  1.000 73.96081  ? 84  ALA B O   1 
ATOM   2551 C CB  . ALA B 1 77  ? 110.78800 116.62100 85.62700  1.000 72.52709  ? 84  ALA B CB  1 
ATOM   2552 N N   . GLY B 1 78  ? 107.85000 115.26200 87.01000  1.000 69.20415  ? 85  GLY B N   1 
ATOM   2553 C CA  . GLY B 1 78  ? 106.46300 115.52800 87.32700  1.000 65.67755  ? 85  GLY B CA  1 
ATOM   2554 C C   . GLY B 1 78  ? 105.52400 115.71700 86.15700  1.000 68.20257  ? 85  GLY B C   1 
ATOM   2555 O O   . GLY B 1 78  ? 104.40500 116.19400 86.36300  1.000 71.94929  ? 85  GLY B O   1 
ATOM   2556 N N   . ILE B 1 79  ? 105.94100 115.37300 84.93900  1.000 70.79587  ? 86  ILE B N   1 
ATOM   2557 C CA  . ILE B 1 79  ? 105.00500 115.28900 83.82400  1.000 68.46104  ? 86  ILE B CA  1 
ATOM   2558 C C   . ILE B 1 79  ? 104.07000 114.10100 84.02000  1.000 71.26566  ? 86  ILE B C   1 
ATOM   2559 O O   . ILE B 1 79  ? 104.43500 113.08400 84.61800  1.000 74.80820  ? 86  ILE B O   1 
ATOM   2560 C CB  . ILE B 1 79  ? 105.78400 115.18200 82.50000  1.000 67.28723  ? 86  ILE B CB  1 
ATOM   2561 C CG1 . ILE B 1 79  ? 106.56300 116.46400 82.24300  1.000 72.95960  ? 86  ILE B CG1 1 
ATOM   2562 C CG2 . ILE B 1 79  ? 104.85800 114.93700 81.33000  1.000 68.47695  ? 86  ILE B CG2 1 
ATOM   2563 C CD1 . ILE B 1 79  ? 105.68200 117.63900 81.94200  1.000 73.75081  ? 86  ILE B CD1 1 
ATOM   2564 N N   . ARG B 1 80  ? 102.85000 114.22700 83.50000  1.000 69.07580  ? 87  ARG B N   1 
ATOM   2565 C CA  . ARG B 1 80  ? 101.93600 113.10600 83.35100  1.000 65.55705  ? 87  ARG B CA  1 
ATOM   2566 C C   . ARG B 1 80  ? 101.12800 113.33700 82.08400  1.000 74.17150  ? 87  ARG B C   1 
ATOM   2567 O O   . ARG B 1 80  ? 101.02400 114.46300 81.59400  1.000 75.19833  ? 87  ARG B O   1 
ATOM   2568 C CB  . ARG B 1 80  ? 100.97600 112.96700 84.53600  1.000 64.54248  ? 87  ARG B CB  1 
ATOM   2569 C CG  . ARG B 1 80  ? 101.59000 112.63800 85.88300  1.000 71.56083  ? 87  ARG B CG  1 
ATOM   2570 C CD  . ARG B 1 80  ? 102.28200 111.29900 85.90900  1.000 75.22026  ? 87  ARG B CD  1 
ATOM   2571 N NE  . ARG B 1 80  ? 102.74700 110.97200 87.25100  1.000 71.70768  ? 87  ARG B NE  1 
ATOM   2572 C CZ  . ARG B 1 80  ? 103.89300 111.39000 87.76700  1.000 72.43618  ? 87  ARG B CZ  1 
ATOM   2573 N NH1 . ARG B 1 80  ? 104.68500 112.21800 87.11100  1.000 76.46927  ? 87  ARG B NH1 1 
ATOM   2574 N NH2 . ARG B 1 80  ? 104.24800 110.97600 88.97800  1.000 73.42889  ? 87  ARG B NH2 1 
ATOM   2575 N N   . VAL B 1 81  ? 100.55500 112.25700 81.55100  1.000 81.48401  ? 88  VAL B N   1 
ATOM   2576 C CA  . VAL B 1 81  ? 99.65800  112.41400 80.41000  1.000 81.55519  ? 88  VAL B CA  1 
ATOM   2577 C C   . VAL B 1 81  ? 98.38600  113.14700 80.81700  1.000 84.58325  ? 88  VAL B C   1 
ATOM   2578 O O   . VAL B 1 81  ? 97.84900  113.95100 80.04500  1.000 80.85645  ? 88  VAL B O   1 
ATOM   2579 C CB  . VAL B 1 81  ? 99.35100  111.04200 79.78500  1.000 75.24981  ? 88  VAL B CB  1 
ATOM   2580 C CG1 . VAL B 1 81  ? 98.25900  111.16000 78.74400  1.000 77.16258  ? 88  VAL B CG1 1 
ATOM   2581 C CG2 . VAL B 1 81  ? 100.59600 110.47600 79.15100  1.000 77.49561  ? 88  VAL B CG2 1 
ATOM   2582 N N   . ASP B 1 82  ? 97.89900  112.91000 82.03000  1.000 90.15581  ? 89  ASP B N   1 
ATOM   2583 C CA  . ASP B 1 82  ? 96.82700  113.72400 82.57500  1.000 86.95332  ? 89  ASP B CA  1 
ATOM   2584 C C   . ASP B 1 82  ? 97.34100  115.11400 82.93900  1.000 86.69456  ? 89  ASP B C   1 
ATOM   2585 O O   . ASP B 1 82  ? 98.53200  115.32600 83.17400  1.000 89.29944  ? 89  ASP B O   1 
ATOM   2586 C CB  . ASP B 1 82  ? 96.21000  113.04900 83.79900  1.000 86.07230  ? 89  ASP B CB  1 
ATOM   2587 N N   . ASN B 1 83  ? 96.42200  116.07200 82.97000  1.000 86.15270  ? 90  ASN B N   1 
ATOM   2588 C CA  . ASN B 1 83  ? 96.74400  117.43700 83.37100  1.000 87.51961  ? 90  ASN B CA  1 
ATOM   2589 C C   . ASN B 1 83  ? 96.99800  117.46600 84.87100  1.000 83.54254  ? 90  ASN B C   1 
ATOM   2590 O O   . ASN B 1 83  ? 96.07200  117.28100 85.66500  1.000 86.76748  ? 90  ASN B O   1 
ATOM   2591 C CB  . ASN B 1 83  ? 95.61100  118.38100 82.98500  1.000 87.49680  ? 90  ASN B CB  1 
ATOM   2592 C CG  . ASN B 1 83  ? 95.43600  118.49600 81.48600  1.000 86.59812  ? 90  ASN B CG  1 
ATOM   2593 O OD1 . ASN B 1 83  ? 96.38300  118.79700 80.76100  1.000 87.23563  ? 90  ASN B OD1 1 
ATOM   2594 N ND2 . ASN B 1 83  ? 94.22100  118.24900 81.01100  1.000 85.67680  ? 90  ASN B ND2 1 
ATOM   2595 N N   . VAL B 1 84  ? 98.24900  117.68700 85.26500  1.000 66.94450  ? 91  VAL B N   1 
ATOM   2596 C CA  . VAL B 1 84  ? 98.66600  117.61300 86.66000  1.000 73.11678  ? 91  VAL B CA  1 
ATOM   2597 C C   . VAL B 1 84  ? 99.17100  118.97700 87.11700  1.000 77.66752  ? 91  VAL B C   1 
ATOM   2598 O O   . VAL B 1 84  ? 99.78100  119.72000 86.34200  1.000 75.70061  ? 91  VAL B O   1 
ATOM   2599 C CB  . VAL B 1 84  ? 99.73600  116.51900 86.85100  1.000 69.59105  ? 91  VAL B CB  1 
ATOM   2600 C CG1 . VAL B 1 84  ? 100.39100 116.62300 88.20300  1.000 66.99924  ? 91  VAL B CG1 1 
ATOM   2601 C CG2 . VAL B 1 84  ? 99.10200  115.16100 86.70500  1.000 70.47044  ? 91  VAL B CG2 1 
ATOM   2602 N N   . ARG B 1 85  ? 98.89100  119.30400 88.37800  1.000 75.59801  ? 92  ARG B N   1 
ATOM   2603 C CA  . ARG B 1 85  ? 99.27200  120.57800 88.96600  1.000 72.23330  ? 92  ARG B CA  1 
ATOM   2604 C C   . ARG B 1 85  ? 100.79200 120.73900 88.97500  1.000 76.72254  ? 92  ARG B C   1 
ATOM   2605 O O   . ARG B 1 85  ? 101.52100 119.75400 89.11300  1.000 78.49005  ? 92  ARG B O   1 
ATOM   2606 C CB  . ARG B 1 85  ? 98.74700  120.64400 90.39900  1.000 70.46816  ? 92  ARG B CB  1 
ATOM   2607 C CG  . ARG B 1 85  ? 98.80100  122.00100 91.05600  1.000 72.57102  ? 92  ARG B CG  1 
ATOM   2608 C CD  . ARG B 1 85  ? 98.11200  121.97900 92.40200  1.000 73.05411  ? 92  ARG B CD  1 
ATOM   2609 N NE  . ARG B 1 85  ? 98.85100  121.15700 93.35100  1.000 72.77216  ? 92  ARG B NE  1 
ATOM   2610 C CZ  . ARG B 1 85  ? 98.29400  120.46300 94.33100  1.000 74.58330  ? 92  ARG B CZ  1 
ATOM   2611 N NH1 . ARG B 1 85  ? 96.99000  120.48900 94.54100  1.000 73.85909  ? 92  ARG B NH1 1 
ATOM   2612 N NH2 . ARG B 1 85  ? 99.06500  119.72900 95.12400  1.000 74.02377  ? 92  ARG B NH2 1 
ATOM   2613 N N   . PRO B 1 86  ? 101.29900 121.96200 88.79800  1.000 69.77680  ? 93  PRO B N   1 
ATOM   2614 C CA  . PRO B 1 86  ? 102.73900 122.19400 88.95600  1.000 67.04974  ? 93  PRO B CA  1 
ATOM   2615 C C   . PRO B 1 86  ? 103.23700 121.67900 90.29800  1.000 67.87379  ? 93  PRO B C   1 
ATOM   2616 O O   . PRO B 1 86  ? 102.55500 121.78800 91.31700  1.000 66.85559  ? 93  PRO B O   1 
ATOM   2617 C CB  . PRO B 1 86  ? 102.86500 123.71600 88.84800  1.000 64.99598  ? 93  PRO B CB  1 
ATOM   2618 C CG  . PRO B 1 86  ? 101.71600 124.11100 88.01300  1.000 66.24195  ? 93  PRO B CG  1 
ATOM   2619 C CD  . PRO B 1 86  ? 100.59600 123.19200 88.40300  1.000 65.64521  ? 93  PRO B CD  1 
ATOM   2620 N N   . ARG B 1 87  ? 104.44800 121.12500 90.29500  1.000 61.08988  ? 94  ARG B N   1 
ATOM   2621 C CA  . ARG B 1 87  ? 104.96700 120.47200 91.49200  1.000 55.53749  ? 94  ARG B CA  1 
ATOM   2622 C C   . ARG B 1 87  ? 105.52100 121.45400 92.51400  1.000 57.15510  ? 94  ARG B C   1 
ATOM   2623 O O   . ARG B 1 87  ? 105.37600 121.23400 93.71900  1.000 61.25113  ? 94  ARG B O   1 
ATOM   2624 C CB  . ARG B 1 87  ? 106.03100 119.44600 91.10900  1.000 56.22322  ? 94  ARG B CB  1 
ATOM   2625 C CG  . ARG B 1 87  ? 105.47100 118.29400 90.31800  1.000 62.12375  ? 94  ARG B CG  1 
ATOM   2626 C CD  . ARG B 1 87  ? 104.15300 117.89100 90.92700  1.000 57.41843  ? 94  ARG B CD  1 
ATOM   2627 N NE  . ARG B 1 87  ? 103.67800 116.59600 90.47200  1.000 58.49293  ? 94  ARG B NE  1 
ATOM   2628 C CZ  . ARG B 1 87  ? 102.53500 116.05900 90.86500  1.000 63.25269  ? 94  ARG B CZ  1 
ATOM   2629 N NH1 . ARG B 1 87  ? 101.73400 116.68700 91.70700  1.000 66.82931  ? 94  ARG B NH1 1 
ATOM   2630 N NH2 . ARG B 1 87  ? 102.18700 114.86200 90.40400  1.000 64.97129  ? 94  ARG B NH2 1 
ATOM   2631 N N   . TRP B 1 88  ? 106.14000 122.54400 92.07000  1.000 52.24657  ? 95  TRP B N   1 
ATOM   2632 C CA  . TRP B 1 88  ? 106.86800 123.42600 92.97300  1.000 50.42655  ? 95  TRP B CA  1 
ATOM   2633 C C   . TRP B 1 88  ? 106.34000 124.85400 92.99600  1.000 54.56753  ? 95  TRP B C   1 
ATOM   2634 O O   . TRP B 1 88  ? 107.08100 125.77000 93.35500  1.000 57.22373  ? 95  TRP B O   1 
ATOM   2635 C CB  . TRP B 1 88  ? 108.35600 123.42500 92.63300  1.000 51.60370  ? 95  TRP B CB  1 
ATOM   2636 C CG  . TRP B 1 88  ? 109.05300 122.12000 92.83400  1.000 48.75863  ? 95  TRP B CG  1 
ATOM   2637 C CD1 . TRP B 1 88  ? 109.69700 121.38300 91.89200  1.000 57.52999  ? 95  TRP B CD1 1 
ATOM   2638 C CD2 . TRP B 1 88  ? 109.26100 121.44600 94.07800  1.000 46.51898  ? 95  TRP B CD2 1 
ATOM   2639 N NE1 . TRP B 1 88  ? 110.25400 120.26800 92.46200  1.000 61.94751  ? 95  TRP B NE1 1 
ATOM   2640 C CE2 . TRP B 1 88  ? 110.00300 120.28900 93.80700  1.000 45.90484  ? 95  TRP B CE2 1 
ATOM   2641 C CE3 . TRP B 1 88  ? 108.87500 121.70100 95.39200  1.000 54.68806  ? 95  TRP B CE3 1 
ATOM   2642 C CZ2 . TRP B 1 88  ? 110.36700 119.39600 94.79600  1.000 43.39532  ? 95  TRP B CZ2 1 
ATOM   2643 C CZ3 . TRP B 1 88  ? 109.23400 120.81000 96.36800  1.000 47.15648  ? 95  TRP B CZ3 1 
ATOM   2644 C CH2 . TRP B 1 88  ? 109.97100 119.67400 96.06900  1.000 46.14598  ? 95  TRP B CH2 1 
ATOM   2645 N N   . ASP B 1 89  ? 105.08500 125.07700 92.62700  1.000 56.79299  ? 96  ASP B N   1 
ATOM   2646 C CA  . ASP B 1 89  ? 104.43300 126.27500 93.12300  1.000 52.50508  ? 96  ASP B CA  1 
ATOM   2647 C C   . ASP B 1 89  ? 104.26900 126.17700 94.64200  1.000 60.02643  ? 96  ASP B C   1 
ATOM   2648 O O   . ASP B 1 89  ? 104.49700 125.12800 95.24800  1.000 62.62013  ? 96  ASP B O   1 
ATOM   2649 C CB  . ASP B 1 89  ? 103.10800 126.50600 92.39000  1.000 57.61892  ? 96  ASP B CB  1 
ATOM   2650 C CG  . ASP B 1 89  ? 102.03500 125.47900 92.73400  1.000 64.40459  ? 96  ASP B CG  1 
ATOM   2651 O OD1 . ASP B 1 89  ? 102.24800 124.60900 93.60000  1.000 67.36561  ? 96  ASP B OD1 1 
ATOM   2652 O OD2 . ASP B 1 89  ? 100.95000 125.54700 92.12000  1.000 65.87027  ? 96  ASP B OD2 1 
ATOM   2653 N N   . PHE B 1 90  ? 103.88400 127.29100 95.26800  1.000 54.01831  ? 97  PHE B N   1 
ATOM   2654 C CA  . PHE B 1 90  ? 103.81700 127.31700 96.72800  1.000 47.34282  ? 97  PHE B CA  1 
ATOM   2655 C C   . PHE B 1 90  ? 102.84700 126.27400 97.27100  1.000 47.64791  ? 97  PHE B C   1 
ATOM   2656 O O   . PHE B 1 90  ? 103.10000 125.67300 98.31800  1.000 52.81764  ? 97  PHE B O   1 
ATOM   2657 C CB  . PHE B 1 90  ? 103.42700 128.71000 97.21800  1.000 45.91765  ? 97  PHE B CB  1 
ATOM   2658 C CG  . PHE B 1 90  ? 103.49800 128.86900 98.71400  1.000 49.83706  ? 97  PHE B CG  1 
ATOM   2659 C CD1 . PHE B 1 90  ? 102.44300 128.49400 99.52200  1.000 53.56314  ? 97  PHE B CD1 1 
ATOM   2660 C CD2 . PHE B 1 90  ? 104.61800 129.40900 99.30900  1.000 51.20499  ? 97  PHE B CD2 1 
ATOM   2661 C CE1 . PHE B 1 90  ? 102.51500 128.64000 100.88600 1.000 50.93482  ? 97  PHE B CE1 1 
ATOM   2662 C CE2 . PHE B 1 90  ? 104.68800 129.56000 100.67300 1.000 45.02453  ? 97  PHE B CE2 1 
ATOM   2663 C CZ  . PHE B 1 90  ? 103.63600 129.17600 101.45900 1.000 45.56153  ? 97  PHE B CZ  1 
ATOM   2664 N N   . THR B 1 91  ? 101.74200 126.03100 96.56900  1.000 50.44754  ? 98  THR B N   1 
ATOM   2665 C CA  . THR B 1 91  ? 100.80400 124.99900 97.00400  1.000 54.28755  ? 98  THR B CA  1 
ATOM   2666 C C   . THR B 1 91  ? 101.39000 123.59800 96.86000  1.000 55.21409  ? 98  THR B C   1 
ATOM   2667 O O   . THR B 1 91  ? 101.25400 122.76200 97.76300  1.000 61.91423  ? 98  THR B O   1 
ATOM   2668 C CB  . THR B 1 91  ? 99.50500  125.11600 96.21800  1.000 54.08683  ? 98  THR B CB  1 
ATOM   2669 O OG1 . THR B 1 91  ? 98.86600  126.35300 96.54600  1.000 54.75662  ? 98  THR B OG1 1 
ATOM   2670 C CG2 . THR B 1 91  ? 98.57900  123.97500 96.57300  1.000 52.58714  ? 98  THR B CG2 1 
ATOM   2671 N N   . GLY B 1 92  ? 102.05500 123.32600 95.73900  1.000 49.29423  ? 99  GLY B N   1 
ATOM   2672 C CA  . GLY B 1 92  ? 102.71100 122.04000 95.57600  1.000 48.52118  ? 99  GLY B CA  1 
ATOM   2673 C C   . GLY B 1 92  ? 103.84000 121.82100 96.56200  1.000 52.93912  ? 99  GLY B C   1 
ATOM   2674 O O   . GLY B 1 92  ? 104.02000 120.71500 97.07200  1.000 58.78090  ? 99  GLY B O   1 
ATOM   2675 N N   . ALA B 1 93  ? 104.60900 122.87000 96.85500  1.000 48.02808  ? 100 ALA B N   1 
ATOM   2676 C CA  . ALA B 1 93  ? 105.65900 122.75600 97.86000  1.000 43.85834  ? 100 ALA B CA  1 
ATOM   2677 C C   . ALA B 1 93  ? 105.08700 122.56600 99.25700  1.000 46.58745  ? 100 ALA B C   1 
ATOM   2678 O O   . ALA B 1 93  ? 105.67400 121.85200 100.07700 1.000 50.54343  ? 100 ALA B O   1 
ATOM   2679 C CB  . ALA B 1 93  ? 106.56300 123.98200 97.81500  1.000 44.50717  ? 100 ALA B CB  1 
ATOM   2680 N N   . PHE B 1 94  ? 103.95200 123.19700 99.55700  1.000 42.52160  ? 101 PHE B N   1 
ATOM   2681 C CA  . PHE B 1 94  ? 103.30200 122.96600 100.84500 1.000 38.92130  ? 101 PHE B CA  1 
ATOM   2682 C C   . PHE B 1 94  ? 102.79000 121.53700 100.96700 1.000 40.03599  ? 101 PHE B C   1 
ATOM   2683 O O   . PHE B 1 94  ? 102.90800 120.91900 102.02900 1.000 49.06670  ? 101 PHE B O   1 
ATOM   2684 C CB  . PHE B 1 94  ? 102.15800 123.95700 101.04200 1.000 40.69481  ? 101 PHE B CB  1 
ATOM   2685 C CG  . PHE B 1 94  ? 101.56500 123.93000 102.41800 1.000 46.10626  ? 101 PHE B CG  1 
ATOM   2686 C CD1 . PHE B 1 94  ? 100.59100 123.01200 102.74900 1.000 45.04834  ? 101 PHE B CD1 1 
ATOM   2687 C CD2 . PHE B 1 94  ? 101.97600 124.82900 103.37600 1.000 52.10744  ? 101 PHE B CD2 1 
ATOM   2688 C CE1 . PHE B 1 94  ? 100.05000 122.98700 104.00700 1.000 47.64904  ? 101 PHE B CE1 1 
ATOM   2689 C CE2 . PHE B 1 94  ? 101.43500 124.80700 104.63800 1.000 43.49199  ? 101 PHE B CE2 1 
ATOM   2690 C CZ  . PHE B 1 94  ? 100.47200 123.88700 104.95200 1.000 45.19487  ? 101 PHE B CZ  1 
ATOM   2691 N N   . TYR B 1 95  ? 102.27000 120.97500 99.87900  1.000 41.09768  ? 102 TYR B N   1 
ATOM   2692 C CA  . TYR B 1 95  ? 101.90100 119.56400 99.89500  1.000 43.56926  ? 102 TYR B CA  1 
ATOM   2693 C C   . TYR B 1 95  ? 103.12800 118.67900 100.08600 1.000 38.63695  ? 102 TYR B C   1 
ATOM   2694 O O   . TYR B 1 95  ? 103.09400 117.71700 100.86300 1.000 41.91505  ? 102 TYR B O   1 
ATOM   2695 C CB  . TYR B 1 95  ? 101.16700 119.22100 98.60100  1.000 48.61008  ? 102 TYR B CB  1 
ATOM   2696 C CG  . TYR B 1 95  ? 100.37400 117.93600 98.61600  1.000 45.07759  ? 102 TYR B CG  1 
ATOM   2697 C CD1 . TYR B 1 95  ? 100.24300 117.18800 99.76700  1.000 44.43417  ? 102 TYR B CD1 1 
ATOM   2698 C CD2 . TYR B 1 95  ? 99.69400  117.51500 97.48900  1.000 46.51822  ? 102 TYR B CD2 1 
ATOM   2699 C CE1 . TYR B 1 95  ? 99.53000  116.01500 99.77100  1.000 44.50258  ? 102 TYR B CE1 1 
ATOM   2700 C CE2 . TYR B 1 95  ? 98.95200  116.36300 97.49700  1.000 49.91649  ? 102 TYR B CE2 1 
ATOM   2701 C CZ  . TYR B 1 95  ? 98.87900  115.61400 98.63900  1.000 51.17814  ? 102 TYR B CZ  1 
ATOM   2702 O OH  . TYR B 1 95  ? 98.11300  114.47900 98.66200  1.000 55.10156  ? 102 TYR B OH  1 
ATOM   2703 N N   . PHE B 1 96  ? 104.21200 118.97600 99.37300  1.000 33.39705  ? 103 PHE B N   1 
ATOM   2704 C CA  . PHE B 1 96  ? 105.44500 118.21400 99.54000  1.000 22.93172  ? 103 PHE B CA  1 
ATOM   2705 C C   . PHE B 1 96  ? 105.92500 118.21200 100.98400 1.000 37.12506  ? 103 PHE B C   1 
ATOM   2706 O O   . PHE B 1 96  ? 106.21300 117.15200 101.54300 1.000 50.30626  ? 103 PHE B O   1 
ATOM   2707 C CB  . PHE B 1 96  ? 106.54000 118.74500 98.62700  1.000 35.05963  ? 103 PHE B CB  1 
ATOM   2708 C CG  . PHE B 1 96  ? 107.87000 118.12200 98.88800  1.000 36.10986  ? 103 PHE B CG  1 
ATOM   2709 C CD1 . PHE B 1 96  ? 108.09700 116.80100 98.58000  1.000 42.31180  ? 103 PHE B CD1 1 
ATOM   2710 C CD2 . PHE B 1 96  ? 108.89200 118.85400 99.43800  1.000 35.17208  ? 103 PHE B CD2 1 
ATOM   2711 C CE1 . PHE B 1 96  ? 109.31400 116.22700 98.82600  1.000 39.42594  ? 103 PHE B CE1 1 
ATOM   2712 C CE2 . PHE B 1 96  ? 110.11100 118.28300 99.68000  1.000 36.37846  ? 103 PHE B CE2 1 
ATOM   2713 C CZ  . PHE B 1 96  ? 110.32200 116.97100 99.37300  1.000 38.29929  ? 103 PHE B CZ  1 
ATOM   2714 N N   . VAL B 1 97  ? 106.08500 119.39400 101.58500 1.000 39.52080  ? 104 VAL B N   1 
ATOM   2715 C CA  . VAL B 1 97  ? 106.55100 119.44700 102.96900 1.000 26.55727  ? 104 VAL B CA  1 
ATOM   2716 C C   . VAL B 1 97  ? 105.56000 118.78600 103.91500 1.000 29.31683  ? 104 VAL B C   1 
ATOM   2717 O O   . VAL B 1 97  ? 105.96100 118.22000 104.93400 1.000 42.26627  ? 104 VAL B O   1 
ATOM   2718 C CB  . VAL B 1 97  ? 106.86800 120.89100 103.40000 1.000 27.23735  ? 104 VAL B CB  1 
ATOM   2719 C CG1 . VAL B 1 97  ? 107.95100 121.46800 102.53100 1.000 32.70862  ? 104 VAL B CG1 1 
ATOM   2720 C CG2 . VAL B 1 97  ? 105.64700 121.74900 103.34800 1.000 35.90173  ? 104 VAL B CG2 1 
ATOM   2721 N N   . GLY B 1 98  ? 104.26300 118.85600 103.62600 1.000 32.79776  ? 105 GLY B N   1 
ATOM   2722 C CA  . GLY B 1 98  ? 103.31100 118.08100 104.40400 1.000 27.15370  ? 105 GLY B CA  1 
ATOM   2723 C C   . GLY B 1 98  ? 103.56200 116.58500 104.35600 1.000 27.93967  ? 105 GLY B C   1 
ATOM   2724 O O   . GLY B 1 98  ? 103.42900 115.89400 105.36500 1.000 35.38165  ? 105 GLY B O   1 
ATOM   2725 N N   . THR B 1 99  ? 103.92000 116.06200 103.18400 1.000 28.25935  ? 106 THR B N   1 
ATOM   2726 C CA  . THR B 1 99  ? 104.23600 114.63800 103.08500 1.000 26.23012  ? 106 THR B CA  1 
ATOM   2727 C C   . THR B 1 99  ? 105.61000 114.27800 103.64200 1.000 25.17022  ? 106 THR B C   1 
ATOM   2728 O O   . THR B 1 99  ? 105.81800 113.13600 104.05800 1.000 32.81498  ? 106 THR B O   1 
ATOM   2729 C CB  . THR B 1 99  ? 104.13700 114.15800 101.63700 1.000 31.69724  ? 106 THR B CB  1 
ATOM   2730 O OG1 . THR B 1 99  ? 105.18200 114.74300 100.85700 1.000 40.18221  ? 106 THR B OG1 1 
ATOM   2731 C CG2 . THR B 1 99  ? 102.79700 114.52000 101.04500 1.000 35.60114  ? 106 THR B CG2 1 
ATOM   2732 N N   . VAL B 1 100 ? 106.56100 115.20600 103.64000 1.000 24.54465  ? 107 VAL B N   1 
ATOM   2733 C CA  . VAL B 1 100 ? 107.84300 114.96400 104.30300 1.000 19.90832  ? 107 VAL B CA  1 
ATOM   2734 C C   . VAL B 1 100 ? 107.67500 114.92900 105.81700 1.000 34.51247  ? 107 VAL B C   1 
ATOM   2735 O O   . VAL B 1 100 ? 108.09200 113.97700 106.48300 1.000 41.78133  ? 107 VAL B O   1 
ATOM   2736 C CB  . VAL B 1 100 ? 108.87400 116.02400 103.88300 1.000 22.58258  ? 107 VAL B CB  1 
ATOM   2737 C CG1 . VAL B 1 100 ? 110.01500 116.06300 104.86200 1.000 16.87986  ? 107 VAL B CG1 1 
ATOM   2738 C CG2 . VAL B 1 100 ? 109.39900 115.71800 102.51600 1.000 33.95967  ? 107 VAL B CG2 1 
ATOM   2739 N N   . VAL B 1 101 ? 107.07300 115.97400 106.38200 1.000 37.74239  ? 108 VAL B N   1 
ATOM   2740 C CA  . VAL B 1 101 ? 107.02700 116.15800 107.82800 1.000 22.40631  ? 108 VAL B CA  1 
ATOM   2741 C C   . VAL B 1 101 ? 106.15700 115.11100 108.51800 1.000 32.33849  ? 108 VAL B C   1 
ATOM   2742 O O   . VAL B 1 101 ? 106.44700 114.71100 109.64900 1.000 36.09620  ? 108 VAL B O   1 
ATOM   2743 C CB  . VAL B 1 101 ? 106.55700 117.59300 108.11800 1.000 29.95393  ? 108 VAL B CB  1 
ATOM   2744 C CG1 . VAL B 1 101 ? 106.20900 117.76900 109.55000 1.000 37.34591  ? 108 VAL B CG1 1 
ATOM   2745 C CG2 . VAL B 1 101 ? 107.64600 118.56400 107.74700 1.000 34.58137  ? 108 VAL B CG2 1 
ATOM   2746 N N   . SER B 1 102 ? 105.10300 114.63300 107.86700 1.000 36.86581  ? 109 SER B N   1 
ATOM   2747 C CA  . SER B 1 102 ? 104.34700 113.49900 108.38800 1.000 25.45987  ? 109 SER B CA  1 
ATOM   2748 C C   . SER B 1 102 ? 104.98100 112.15200 108.07300 1.000 33.82700  ? 109 SER B C   1 
ATOM   2749 O O   . SER B 1 102 ? 104.43300 111.12600 108.48200 1.000 41.54400  ? 109 SER B O   1 
ATOM   2750 C CB  . SER B 1 102 ? 102.91600 113.53200 107.86200 1.000 30.07199  ? 109 SER B CB  1 
ATOM   2751 O OG  . SER B 1 102 ? 102.90100 113.49100 106.45500 1.000 38.04027  ? 109 SER B OG  1 
ATOM   2752 N N   . THR B 1 103 ? 106.10300 112.13000 107.35800 1.000 36.79081  ? 110 THR B N   1 
ATOM   2753 C CA  . THR B 1 103 ? 106.76000 110.94600 106.80700 1.000 26.91300  ? 110 THR B CA  1 
ATOM   2754 C C   . THR B 1 103 ? 105.89400 110.13000 105.85700 1.000 22.18345  ? 110 THR B C   1 
ATOM   2755 O O   . THR B 1 103 ? 106.23100 108.97700 105.57700 1.000 30.54492  ? 110 THR B O   1 
ATOM   2756 C CB  . THR B 1 103 ? 107.28400 110.01600 107.90700 1.000 31.33773  ? 110 THR B CB  1 
ATOM   2757 O OG1 . THR B 1 103 ? 106.18100 109.38600 108.56100 1.000 34.29368  ? 110 THR B OG1 1 
ATOM   2758 C CG2 . THR B 1 103 ? 108.09100 110.78400 108.92200 1.000 24.77204  ? 110 THR B CG2 1 
ATOM   2759 N N   . ILE B 1 104 ? 104.76900 110.66000 105.37600 1.000 26.17532  ? 111 ILE B N   1 
ATOM   2760 C CA  . ILE B 1 104 ? 103.99600 109.91700 104.38100 1.000 14.15219  ? 111 ILE B CA  1 
ATOM   2761 C C   . ILE B 1 104 ? 104.82700 109.69800 103.12600 1.000 21.20581  ? 111 ILE B C   1 
ATOM   2762 O O   . ILE B 1 104 ? 104.97900 108.56900 102.65000 1.000 36.87128  ? 111 ILE B O   1 
ATOM   2763 C CB  . ILE B 1 104 ? 102.67000 110.62400 104.06500 1.000 17.34208  ? 111 ILE B CB  1 
ATOM   2764 C CG1 . ILE B 1 104 ? 101.79700 110.71200 105.30600 1.000 30.55393  ? 111 ILE B CG1 1 
ATOM   2765 C CG2 . ILE B 1 104 ? 101.93000 109.86900 103.01500 1.000 21.36629  ? 111 ILE B CG2 1 
ATOM   2766 C CD1 . ILE B 1 104 ? 100.65100 111.66200 105.15600 1.000 23.43427  ? 111 ILE B CD1 1 
ATOM   2767 N N   . GLY B 1 105 ? 105.40400 110.76600 102.59200 1.000 29.23945  ? 112 GLY B N   1 
ATOM   2768 C CA  . GLY B 1 105 ? 106.30300 110.64400 101.46500 1.000 25.32073  ? 112 GLY B CA  1 
ATOM   2769 C C   . GLY B 1 105 ? 105.74500 109.98200 100.22400 1.000 24.25798  ? 112 GLY B C   1 
ATOM   2770 O O   . GLY B 1 105 ? 106.29600 108.98000 99.76600  1.000 30.81475  ? 112 GLY B O   1 
ATOM   2771 N N   . PHE B 1 106 ? 104.62500 110.48700 99.70200  1.000 32.23094  ? 113 PHE B N   1 
ATOM   2772 C CA  . PHE B 1 106 ? 104.05500 109.91600 98.48500  1.000 28.09239  ? 113 PHE B CA  1 
ATOM   2773 C C   . PHE B 1 106 ? 105.07700 109.87700 97.36300  1.000 30.73934  ? 113 PHE B C   1 
ATOM   2774 O O   . PHE B 1 106 ? 105.11500 108.92700 96.57700  1.000 44.92635  ? 113 PHE B O   1 
ATOM   2775 C CB  . PHE B 1 106 ? 102.83700 110.71400 98.02800  1.000 32.48217  ? 113 PHE B CB  1 
ATOM   2776 C CG  . PHE B 1 106 ? 101.65000 110.60000 98.92700  1.000 36.31137  ? 113 PHE B CG  1 
ATOM   2777 C CD1 . PHE B 1 106 ? 101.16200 109.36800 99.29400  1.000 34.04904  ? 113 PHE B CD1 1 
ATOM   2778 C CD2 . PHE B 1 106 ? 101.00400 111.72800 99.38100  1.000 34.13585  ? 113 PHE B CD2 1 
ATOM   2779 C CE1 . PHE B 1 106 ? 100.06500 109.26700 100.10100 1.000 41.28694  ? 113 PHE B CE1 1 
ATOM   2780 C CE2 . PHE B 1 106 ? 99.90900  111.62900 100.19100 1.000 31.32367  ? 113 PHE B CE2 1 
ATOM   2781 C CZ  . PHE B 1 106 ? 99.43800  110.39900 100.55000 1.000 38.07199  ? 113 PHE B CZ  1 
ATOM   2782 N N   . GLY B 1 107 ? 105.91500 110.90000 97.27400  1.000 36.11497  ? 114 GLY B N   1 
ATOM   2783 C CA  . GLY B 1 107 ? 106.98700 110.90000 96.30500  1.000 34.26867  ? 114 GLY B CA  1 
ATOM   2784 C C   . GLY B 1 107 ? 106.54600 111.21200 94.90200  1.000 36.99970  ? 114 GLY B C   1 
ATOM   2785 O O   . GLY B 1 107 ? 107.26000 110.88600 93.95200  1.000 48.27200  ? 114 GLY B O   1 
ATOM   2786 N N   . MET B 1 108 ? 105.37200 111.82100 94.74300  1.000 39.16211  ? 115 MET B N   1 
ATOM   2787 C CA  . MET B 1 108 ? 104.98500 112.38900 93.45800  1.000 48.85216  ? 115 MET B CA  1 
ATOM   2788 C C   . MET B 1 108 ? 105.78800 113.64800 93.16300  1.000 53.73670  ? 115 MET B C   1 
ATOM   2789 O O   . MET B 1 108 ? 106.17100 113.89500 92.01400  1.000 55.42728  ? 115 MET B O   1 
ATOM   2790 C CB  . MET B 1 108 ? 103.48300 112.67200 93.44700  1.000 45.91210  ? 115 MET B CB  1 
ATOM   2791 C CG  . MET B 1 108 ? 103.07600 113.92700 94.20000  1.000 52.21325  ? 115 MET B CG  1 
ATOM   2792 S SD  . MET B 1 108 ? 103.30900 113.81000 95.98100  1.000 63.66158  ? 115 MET B SD  1 
ATOM   2793 C CE  . MET B 1 108 ? 102.48500 115.29500 96.53000  1.000 44.90539  ? 115 MET B CE  1 
ATOM   2794 N N   . THR B 1 109 ? 106.05100 114.45000 94.19200  1.000 50.12517  ? 116 THR B N   1 
ATOM   2795 C CA  . THR B 1 109 ? 107.00700 115.54700 94.15800  1.000 45.55933  ? 116 THR B CA  1 
ATOM   2796 C C   . THR B 1 109 ? 108.23400 115.14800 94.96400  1.000 39.94225  ? 116 THR B C   1 
ATOM   2797 O O   . THR B 1 109 ? 108.10800 114.71500 96.11200  1.000 37.17086  ? 116 THR B O   1 
ATOM   2798 C CB  . THR B 1 109 ? 106.38600 116.81400 94.74500  1.000 48.34642  ? 116 THR B CB  1 
ATOM   2799 O OG1 . THR B 1 109 ? 105.22200 117.17400 93.99800  1.000 58.30677  ? 116 THR B OG1 1 
ATOM   2800 C CG2 . THR B 1 109 ? 107.34600 117.94000 94.67400  1.000 51.47343  ? 116 THR B CG2 1 
ATOM   2801 N N   . THR B 1 110 ? 109.41700 115.30500 94.36900  1.000 48.34041  ? 117 THR B N   1 
ATOM   2802 C CA  . THR B 1 110 ? 110.66800 114.99400 95.04200  1.000 49.10850  ? 117 THR B CA  1 
ATOM   2803 C C   . THR B 1 110 ? 111.72700 116.01900 94.66500  1.000 55.74773  ? 117 THR B C   1 
ATOM   2804 O O   . THR B 1 110 ? 111.76100 116.48200 93.51600  1.000 57.93471  ? 117 THR B O   1 
ATOM   2805 C CB  . THR B 1 110 ? 111.17300 113.59700 94.66300  1.000 56.30921  ? 117 THR B CB  1 
ATOM   2806 O OG1 . THR B 1 110 ? 111.13600 113.44800 93.24100  1.000 62.56442  ? 117 THR B OG1 1 
ATOM   2807 C CG2 . THR B 1 110 ? 110.31200 112.52600 95.28000  1.000 59.56782  ? 117 THR B CG2 1 
ATOM   2808 N N   . PRO B 1 111 ? 112.60300 116.38100 95.59700  1.000 51.23386  ? 118 PRO B N   1 
ATOM   2809 C CA  . PRO B 1 111 ? 113.64200 117.36800 95.29400  1.000 48.07743  ? 118 PRO B CA  1 
ATOM   2810 C C   . PRO B 1 111 ? 114.64200 116.82700 94.28800  1.000 53.08672  ? 118 PRO B C   1 
ATOM   2811 O O   . PRO B 1 111 ? 114.93000 115.63000 94.24500  1.000 52.19907  ? 118 PRO B O   1 
ATOM   2812 C CB  . PRO B 1 111 ? 114.29500 117.62200 96.65400  1.000 42.85436  ? 118 PRO B CB  1 
ATOM   2813 C CG  . PRO B 1 111 ? 114.07700 116.37400 97.39600  1.000 48.27139  ? 118 PRO B CG  1 
ATOM   2814 C CD  . PRO B 1 111 ? 112.74100 115.85000 96.96000  1.000 48.44146  ? 118 PRO B CD  1 
ATOM   2815 N N   . ALA B 1 112 ? 115.17400 117.72600 93.46400  1.000 57.48431  ? 119 ALA B N   1 
ATOM   2816 C CA  . ALA B 1 112 ? 116.00200 117.30000 92.34400  1.000 61.24154  ? 119 ALA B CA  1 
ATOM   2817 C C   . ALA B 1 112 ? 117.34300 118.02100 92.30200  1.000 64.11000  ? 119 ALA B C   1 
ATOM   2818 O O   . ALA B 1 112 ? 118.33700 117.45400 91.84000  1.000 65.38889  ? 119 ALA B O   1 
ATOM   2819 C CB  . ALA B 1 112 ? 115.25300 117.51200 91.03000  1.000 61.44656  ? 119 ALA B CB  1 
ATOM   2820 N N   . THR B 1 113 ? 117.39100 119.26000 92.77300  1.000 59.45609  ? 120 THR B N   1 
ATOM   2821 C CA  . THR B 1 113 ? 118.66200 119.95100 92.91700  1.000 60.04911  ? 120 THR B CA  1 
ATOM   2822 C C   . THR B 1 113 ? 119.42200 119.42800 94.13100  1.000 61.94883  ? 120 THR B C   1 
ATOM   2823 O O   . THR B 1 113 ? 118.83400 118.90700 95.08000  1.000 62.68505  ? 120 THR B O   1 
ATOM   2824 C CB  . THR B 1 113 ? 118.44600 121.45600 93.04500  1.000 58.60253  ? 120 THR B CB  1 
ATOM   2825 O OG1 . THR B 1 113 ? 117.61700 121.72200 94.18000  1.000 60.60957  ? 120 THR B OG1 1 
ATOM   2826 C CG2 . THR B 1 113 ? 117.78100 122.00600 91.80000  1.000 55.20561  ? 120 THR B CG2 1 
ATOM   2827 N N   . VAL B 1 114 ? 120.75000 119.56000 94.08400  1.000 56.62283  ? 121 VAL B N   1 
ATOM   2828 C CA  . VAL B 1 114 ? 121.57500 119.21300 95.24000  1.000 50.66080  ? 121 VAL B CA  1 
ATOM   2829 C C   . VAL B 1 114 ? 121.26900 120.10300 96.43700  1.000 52.63272  ? 121 VAL B C   1 
ATOM   2830 O O   . VAL B 1 114 ? 121.34700 119.65200 97.58500  1.000 56.25680  ? 121 VAL B O   1 
ATOM   2831 C CB  . VAL B 1 114 ? 123.06900 119.26500 94.87000  1.000 52.73428  ? 121 VAL B CB  1 
ATOM   2832 C CG1 . VAL B 1 114 ? 123.37500 118.23900 93.80100  1.000 58.32264  ? 121 VAL B CG1 1 
ATOM   2833 C CG2 . VAL B 1 114 ? 123.45700 120.65100 94.40000  1.000 55.68822  ? 121 VAL B CG2 1 
ATOM   2834 N N   . GLY B 1 115 ? 120.92300 121.36900 96.20700  1.000 48.72384  ? 122 GLY B N   1 
ATOM   2835 C CA  . GLY B 1 115 ? 120.50300 122.21400 97.31200  1.000 43.62183  ? 122 GLY B CA  1 
ATOM   2836 C C   . GLY B 1 115 ? 119.22700 121.73100 97.97200  1.000 44.66980  ? 122 GLY B C   1 
ATOM   2837 O O   . GLY B 1 115 ? 119.11300 121.73100 99.19900  1.000 51.98639  ? 122 GLY B O   1 
ATOM   2838 N N   . GLY B 1 116 ? 118.27100 121.26700 97.17200  1.000 35.89241  ? 123 GLY B N   1 
ATOM   2839 C CA  . GLY B 1 116 ? 117.07000 120.67800 97.73600  1.000 38.35398  ? 123 GLY B CA  1 
ATOM   2840 C C   . GLY B 1 116 ? 117.33900 119.39500 98.49600  1.000 44.17756  ? 123 GLY B C   1 
ATOM   2841 O O   . GLY B 1 116 ? 116.78500 119.17500 99.57400  1.000 50.06034  ? 123 GLY B O   1 
ATOM   2842 N N   . LYS B 1 117 ? 118.19400 118.53400 97.94800  1.000 47.80171  ? 124 LYS B N   1 
ATOM   2843 C CA  . LYS B 1 117 ? 118.55300 117.29800 98.63500  1.000 45.11241  ? 124 LYS B CA  1 
ATOM   2844 C C   . LYS B 1 117 ? 119.25700 117.56100 99.96200  1.000 48.56197  ? 124 LYS B C   1 
ATOM   2845 O O   . LYS B 1 117 ? 118.97500 116.88900 100.95800 1.000 55.92562  ? 124 LYS B O   1 
ATOM   2846 C CB  . LYS B 1 117 ? 119.42700 116.44000 97.72500  1.000 47.44169  ? 124 LYS B CB  1 
ATOM   2847 C CG  . LYS B 1 117 ? 118.66200 115.78200 96.59700  1.000 50.92653  ? 124 LYS B CG  1 
ATOM   2848 C CD  . LYS B 1 117 ? 119.57200 114.98900 95.68700  1.000 49.20796  ? 124 LYS B CD  1 
ATOM   2849 C CE  . LYS B 1 117 ? 118.76600 114.15600 94.71400  1.000 47.84726  ? 124 LYS B CE  1 
ATOM   2850 N NZ  . LYS B 1 117 ? 119.61500 113.59200 93.63800  1.000 47.05068  ? 124 LYS B NZ  1 
ATOM   2851 N N   . ILE B 1 118 ? 120.18200 118.52300 100.00100 1.000 39.40949  ? 125 ILE B N   1 
ATOM   2852 C CA  . ILE B 1 118 ? 120.81900 118.88200 101.26800 1.000 31.53254  ? 125 ILE B CA  1 
ATOM   2853 C C   . ILE B 1 118 ? 119.79600 119.42700 102.25300 1.000 37.40596  ? 125 ILE B C   1 
ATOM   2854 O O   . ILE B 1 118 ? 119.73500 118.99800 103.40900 1.000 45.39698  ? 125 ILE B O   1 
ATOM   2855 C CB  . ILE B 1 118 ? 121.95200 119.89600 101.04300 1.000 32.55675  ? 125 ILE B CB  1 
ATOM   2856 C CG1 . ILE B 1 118 ? 123.11600 119.26800 100.29200 1.000 39.60814  ? 125 ILE B CG1 1 
ATOM   2857 C CG2 . ILE B 1 118 ? 122.43400 120.43800 102.36200 1.000 32.57267  ? 125 ILE B CG2 1 
ATOM   2858 C CD1 . ILE B 1 118 ? 124.10700 120.28100 99.78700  1.000 44.81213  ? 125 ILE B CD1 1 
ATOM   2859 N N   . PHE B 1 119 ? 118.98300 120.39100 101.81600 1.000 41.80455  ? 126 PHE B N   1 
ATOM   2860 C CA  . PHE B 1 119 ? 118.02900 121.03100 102.71600 1.000 36.18654  ? 126 PHE B CA  1 
ATOM   2861 C C   . PHE B 1 119 ? 117.01500 120.04300 103.27400 1.000 35.63043  ? 126 PHE B C   1 
ATOM   2862 O O   . PHE B 1 119 ? 116.56700 120.19100 104.41500 1.000 45.98145  ? 126 PHE B O   1 
ATOM   2863 C CB  . PHE B 1 119 ? 117.31400 122.16800 101.99300 1.000 37.67260  ? 126 PHE B CB  1 
ATOM   2864 C CG  . PHE B 1 119 ? 116.34100 122.91500 102.85100 1.000 35.95930  ? 126 PHE B CG  1 
ATOM   2865 C CD1 . PHE B 1 119 ? 116.76300 123.57100 103.98400 1.000 42.08017  ? 126 PHE B CD1 1 
ATOM   2866 C CD2 . PHE B 1 119 ? 115.00600 122.97200 102.51800 1.000 39.20516  ? 126 PHE B CD2 1 
ATOM   2867 C CE1 . PHE B 1 119 ? 115.87100 124.26200 104.77000 1.000 43.84059  ? 126 PHE B CE1 1 
ATOM   2868 C CE2 . PHE B 1 119 ? 114.11400 123.66000 103.30200 1.000 38.17336  ? 126 PHE B CE2 1 
ATOM   2869 C CZ  . PHE B 1 119 ? 114.54600 124.30400 104.42600 1.000 40.61787  ? 126 PHE B CZ  1 
ATOM   2870 N N   . LEU B 1 120 ? 116.61900 119.04900 102.48000 1.000 33.38259  ? 127 LEU B N   1 
ATOM   2871 C CA  . LEU B 1 120 ? 115.72400 118.00900 102.97700 1.000 32.94028  ? 127 LEU B CA  1 
ATOM   2872 C C   . LEU B 1 120 ? 116.29400 117.26800 104.18000 1.000 42.44173  ? 127 LEU B C   1 
ATOM   2873 O O   . LEU B 1 120 ? 115.55900 116.95500 105.11500 1.000 49.92331  ? 127 LEU B O   1 
ATOM   2874 C CB  . LEU B 1 120 ? 115.38900 117.02200 101.86700 1.000 35.87422  ? 127 LEU B CB  1 
ATOM   2875 C CG  . LEU B 1 120 ? 114.47300 115.90400 102.34600 1.000 33.15331  ? 127 LEU B CG  1 
ATOM   2876 C CD1 . LEU B 1 120 ? 113.11700 116.46200 102.65600 1.000 38.49691  ? 127 LEU B CD1 1 
ATOM   2877 C CD2 . LEU B 1 120 ? 114.36800 114.83100 101.30100 1.000 43.59219  ? 127 LEU B CD2 1 
ATOM   2878 N N   . ILE B 1 121 ? 117.59700 116.99300 104.19400 1.000 43.19079  ? 128 ILE B N   1 
ATOM   2879 C CA  . ILE B 1 121 ? 118.14800 116.16900 105.27000 1.000 40.86397  ? 128 ILE B CA  1 
ATOM   2880 C C   . ILE B 1 121 ? 118.07100 116.87400 106.62300 1.000 40.99016  ? 128 ILE B C   1 
ATOM   2881 O O   . ILE B 1 121 ? 117.94900 116.21600 107.66100 1.000 49.42497  ? 128 ILE B O   1 
ATOM   2882 C CB  . ILE B 1 121 ? 119.58300 115.73600 104.91900 1.000 39.50204  ? 128 ILE B CB  1 
ATOM   2883 C CG1 . ILE B 1 121 ? 119.56600 114.79100 103.71800 1.000 36.37291  ? 128 ILE B CG1 1 
ATOM   2884 C CG2 . ILE B 1 121 ? 120.24900 115.04700 106.08300 1.000 40.33684  ? 128 ILE B CG2 1 
ATOM   2885 C CD1 . ILE B 1 121 ? 120.91600 114.55700 103.11300 1.000 37.37881  ? 128 ILE B CD1 1 
ATOM   2886 N N   . PHE B 1 122 ? 118.11600 118.20100 106.65000 1.000 38.13578  ? 129 PHE B N   1 
ATOM   2887 C CA  . PHE B 1 122 ? 117.92100 118.93700 107.89600 1.000 38.49941  ? 129 PHE B CA  1 
ATOM   2888 C C   . PHE B 1 122 ? 116.46000 119.27100 108.17400 1.000 41.56687  ? 129 PHE B C   1 
ATOM   2889 O O   . PHE B 1 122 ? 115.99900 119.16500 109.32300 1.000 55.32637  ? 129 PHE B O   1 
ATOM   2890 C CB  . PHE B 1 122 ? 118.74100 120.22500 107.87400 1.000 37.76580  ? 129 PHE B CB  1 
ATOM   2891 C CG  . PHE B 1 122 ? 120.20300 119.99900 107.66200 1.000 42.05236  ? 129 PHE B CG  1 
ATOM   2892 C CD1 . PHE B 1 122 ? 120.90900 119.15300 108.49100 1.000 43.60805  ? 129 PHE B CD1 1 
ATOM   2893 C CD2 . PHE B 1 122 ? 120.87200 120.63200 106.63600 1.000 45.15904  ? 129 PHE B CD2 1 
ATOM   2894 C CE1 . PHE B 1 122 ? 122.25100 118.94200 108.29900 1.000 45.12268  ? 129 PHE B CE1 1 
ATOM   2895 C CE2 . PHE B 1 122 ? 122.21500 120.42300 106.44000 1.000 50.23273  ? 129 PHE B CE2 1 
ATOM   2896 C CZ  . PHE B 1 122 ? 122.90500 119.57700 107.27300 1.000 47.14043  ? 129 PHE B CZ  1 
ATOM   2897 N N   . TYR B 1 123 ? 115.70600 119.62900 107.13600 1.000 39.16456  ? 130 TYR B N   1 
ATOM   2898 C CA  . TYR B 1 123 ? 114.30800 119.97100 107.33300 1.000 36.85811  ? 130 TYR B CA  1 
ATOM   2899 C C   . TYR B 1 123 ? 113.50100 118.76700 107.78400 1.000 38.70440  ? 130 TYR B C   1 
ATOM   2900 O O   . TYR B 1 123 ? 112.71600 118.86900 108.72600 1.000 53.05250  ? 130 TYR B O   1 
ATOM   2901 C CB  . TYR B 1 123 ? 113.74300 120.53300 106.03300 1.000 44.94931  ? 130 TYR B CB  1 
ATOM   2902 C CG  . TYR B 1 123 ? 112.31800 120.99700 106.11000 1.000 47.03411  ? 130 TYR B CG  1 
ATOM   2903 C CD1 . TYR B 1 123 ? 112.01700 122.29200 106.48100 1.000 46.54472  ? 130 TYR B CD1 1 
ATOM   2904 C CD2 . TYR B 1 123 ? 111.27400 120.13900 105.81700 1.000 46.64564  ? 130 TYR B CD2 1 
ATOM   2905 C CE1 . TYR B 1 123 ? 110.72400 122.72100 106.54400 1.000 45.61971  ? 130 TYR B CE1 1 
ATOM   2906 C CE2 . TYR B 1 123 ? 109.97800 120.55900 105.88800 1.000 42.98161  ? 130 TYR B CE2 1 
ATOM   2907 C CZ  . TYR B 1 123 ? 109.70900 121.85100 106.25000 1.000 47.32663  ? 130 TYR B CZ  1 
ATOM   2908 O OH  . TYR B 1 123 ? 108.41200 122.27900 106.32800 1.000 56.29730  ? 130 TYR B OH  1 
ATOM   2909 N N   . GLY B 1 124 ? 113.69100 117.61400 107.14900 1.000 29.23519  ? 131 GLY B N   1 
ATOM   2910 C CA  . GLY B 1 124 ? 112.99400 116.42200 107.58000 1.000 34.07684  ? 131 GLY B CA  1 
ATOM   2911 C C   . GLY B 1 124 ? 113.44600 115.95600 108.94200 1.000 38.68313  ? 131 GLY B C   1 
ATOM   2912 O O   . GLY B 1 124 ? 112.63800 115.46800 109.72800 1.000 43.10862  ? 131 GLY B O   1 
ATOM   2913 N N   . LEU B 1 125 ? 114.72000 116.16800 109.26400 1.000 37.54341  ? 132 LEU B N   1 
ATOM   2914 C CA  . LEU B 1 125 ? 115.25800 115.76000 110.55800 1.000 39.49995  ? 132 LEU B CA  1 
ATOM   2915 C C   . LEU B 1 125 ? 114.59300 116.50400 111.70800 1.000 40.14547  ? 132 LEU B C   1 
ATOM   2916 O O   . LEU B 1 125 ? 114.22500 115.89600 112.71800 1.000 42.50543  ? 132 LEU B O   1 
ATOM   2917 C CB  . LEU B 1 125 ? 116.76700 115.98700 110.58400 1.000 43.11930  ? 132 LEU B CB  1 
ATOM   2918 C CG  . LEU B 1 125 ? 117.50200 115.71300 111.88800 1.000 40.80423  ? 132 LEU B CG  1 
ATOM   2919 C CD1 . LEU B 1 125 ? 117.35500 114.25900 112.26100 1.000 40.08250  ? 132 LEU B CD1 1 
ATOM   2920 C CD2 . LEU B 1 125 ? 118.95700 116.08400 111.74700 1.000 42.45116  ? 132 LEU B CD2 1 
ATOM   2921 N N   . VAL B 1 126 ? 114.45200 117.82300 111.59400 1.000 34.34777  ? 133 VAL B N   1 
ATOM   2922 C CA  . VAL B 1 126 ? 113.76900 118.54000 112.67200 1.000 32.51961  ? 133 VAL B CA  1 
ATOM   2923 C C   . VAL B 1 126 ? 112.24500 118.42300 112.57200 1.000 43.17268  ? 133 VAL B C   1 
ATOM   2924 O O   . VAL B 1 126 ? 111.55600 118.30400 113.59400 1.000 53.13823  ? 133 VAL B O   1 
ATOM   2925 C CB  . VAL B 1 126 ? 114.21700 120.00800 112.70200 1.000 36.58155  ? 133 VAL B CB  1 
ATOM   2926 C CG1 . VAL B 1 126 ? 113.56100 120.72200 113.85700 1.000 41.50539  ? 133 VAL B CG1 1 
ATOM   2927 C CG2 . VAL B 1 126 ? 115.71800 120.09200 112.82300 1.000 38.96962  ? 133 VAL B CG2 1 
ATOM   2928 N N   . GLY B 1 127 ? 111.69100 118.42000 111.35800 1.000 42.34781  ? 134 GLY B N   1 
ATOM   2929 C CA  . GLY B 1 127 ? 110.24900 118.30700 111.19400 1.000 35.86473  ? 134 GLY B CA  1 
ATOM   2930 C C   . GLY B 1 127 ? 109.65900 116.99500 111.67200 1.000 35.81170  ? 134 GLY B C   1 
ATOM   2931 O O   . GLY B 1 127 ? 108.62100 116.98000 112.33200 1.000 46.42421  ? 134 GLY B O   1 
ATOM   2932 N N   . CYS B 1 128 ? 110.29600 115.87500 111.33400 1.000 30.34804  ? 135 CYS B N   1 
ATOM   2933 C CA  . CYS B 1 128 ? 109.78100 114.57800 111.75500 1.000 27.59586  ? 135 CYS B CA  1 
ATOM   2934 C C   . CYS B 1 128 ? 109.84600 114.39900 113.26600 1.000 40.95463  ? 135 CYS B C   1 
ATOM   2935 O O   . CYS B 1 128 ? 108.93500 113.81500 113.86000 1.000 51.14004  ? 135 CYS B O   1 
ATOM   2936 C CB  . CYS B 1 128 ? 110.54700 113.46200 111.05200 1.000 38.04532  ? 135 CYS B CB  1 
ATOM   2937 S SG  . CYS B 1 128 ? 110.38800 113.45100 109.25800 1.000 59.34286  ? 135 CYS B SG  1 
ATOM   2938 N N   . SER B 1 129 ? 110.92300 114.85400 113.90300 1.000 38.25259  ? 136 SER B N   1 
ATOM   2939 C CA  . SER B 1 129 ? 110.97400 114.83300 115.36200 1.000 33.43568  ? 136 SER B CA  1 
ATOM   2940 C C   . SER B 1 129 ? 109.88700 115.70000 115.98700 1.000 42.92835  ? 136 SER B C   1 
ATOM   2941 O O   . SER B 1 129 ? 109.19300 115.26800 116.91900 1.000 51.96611  ? 136 SER B O   1 
ATOM   2942 C CB  . SER B 1 129 ? 112.34400 115.30400 115.82300 1.000 41.34227  ? 136 SER B CB  1 
ATOM   2943 O OG  . SER B 1 129 ? 113.33800 114.36100 115.48800 1.000 51.83742  ? 136 SER B OG  1 
ATOM   2944 N N   . SER B 1 130 ? 109.70000 116.91500 115.46500 1.000 43.53227  ? 137 SER B N   1 
ATOM   2945 C CA  . SER B 1 130 ? 108.63700 117.79100 115.94900 1.000 34.14888  ? 137 SER B CA  1 
ATOM   2946 C C   . SER B 1 130 ? 107.25800 117.16400 115.79000 1.000 45.86043  ? 137 SER B C   1 
ATOM   2947 O O   . SER B 1 130 ? 106.40400 117.28400 116.67300 1.000 54.61259  ? 137 SER B O   1 
ATOM   2948 C CB  . SER B 1 130 ? 108.70200 119.12400 115.21200 1.000 36.50548  ? 137 SER B CB  1 
ATOM   2949 O OG  . SER B 1 130 ? 107.81100 120.05900 115.77900 1.000 55.57472  ? 137 SER B OG  1 
ATOM   2950 N N   . THR B 1 131 ? 107.03600 116.44500 114.69600 1.000 43.51546  ? 138 THR B N   1 
ATOM   2951 C CA  . THR B 1 131 ? 105.75300 115.78800 114.48100 1.000 31.96928  ? 138 THR B CA  1 
ATOM   2952 C C   . THR B 1 131 ? 105.55600 114.54400 115.34000 1.000 38.84030  ? 138 THR B C   1 
ATOM   2953 O O   . THR B 1 131 ? 104.43400 114.27400 115.77300 1.000 52.41263  ? 138 THR B O   1 
ATOM   2954 C CB  . THR B 1 131 ? 105.60100 115.45400 113.00700 1.000 32.84699  ? 138 THR B CB  1 
ATOM   2955 O OG1 . THR B 1 131 ? 105.60100 116.67400 112.27200 1.000 47.63527  ? 138 THR B OG1 1 
ATOM   2956 C CG2 . THR B 1 131 ? 104.31100 114.76800 112.75700 1.000 38.90147  ? 138 THR B CG2 1 
ATOM   2957 N N   . ILE B 1 132 ? 106.58800 113.73000 115.55600 1.000 40.55343  ? 139 ILE B N   1 
ATOM   2958 C CA  . ILE B 1 132 ? 106.40300 112.60300 116.46900 1.000 40.58677  ? 139 ILE B CA  1 
ATOM   2959 C C   . ILE B 1 132 ? 106.12100 113.09700 117.88200 1.000 51.17229  ? 139 ILE B C   1 
ATOM   2960 O O   . ILE B 1 132 ? 105.27900 112.52900 118.59900 1.000 60.99130  ? 139 ILE B O   1 
ATOM   2961 C CB  . ILE B 1 132 ? 107.63000 111.67700 116.43000 1.000 42.65272  ? 139 ILE B CB  1 
ATOM   2962 C CG1 . ILE B 1 132 ? 107.63200 110.84900 115.14900 1.000 44.65731  ? 139 ILE B CG1 1 
ATOM   2963 C CG2 . ILE B 1 132 ? 107.65000 110.76700 117.63000 1.000 51.91426  ? 139 ILE B CG2 1 
ATOM   2964 C CD1 . ILE B 1 132 ? 108.95800 110.20400 114.85700 1.000 49.91134  ? 139 ILE B CD1 1 
ATOM   2965 N N   . LEU B 1 133 ? 106.69300 114.24400 118.24700 1.000 46.56947  ? 140 LEU B N   1 
ATOM   2966 C CA  . LEU B 1 133 ? 106.25700 114.92800 119.46000 1.000 36.27614  ? 140 LEU B CA  1 
ATOM   2967 C C   . LEU B 1 133 ? 104.78400 115.30700 119.38400 1.000 44.48894  ? 140 LEU B C   1 
ATOM   2968 O O   . LEU B 1 133 ? 104.03700 115.12300 120.35100 1.000 57.71241  ? 140 LEU B O   1 
ATOM   2969 C CB  . LEU B 1 133 ? 107.11700 116.16100 119.70700 1.000 40.64522  ? 140 LEU B CB  1 
ATOM   2970 C CG  . LEU B 1 133 ? 106.69500 116.96000 120.92800 1.000 43.93630  ? 140 LEU B CG  1 
ATOM   2971 C CD1 . LEU B 1 133 ? 106.80400 116.08300 122.13400 1.000 46.30561  ? 140 LEU B CD1 1 
ATOM   2972 C CD2 . LEU B 1 133 ? 107.57100 118.16600 121.08900 1.000 47.98278  ? 140 LEU B CD2 1 
ATOM   2973 N N   . PHE B 1 134 ? 104.37000 115.92000 118.27600 1.000 45.41269  ? 141 PHE B N   1 
ATOM   2974 C CA  . PHE B 1 134 ? 102.98000 116.34300 118.14400 1.000 42.66334  ? 141 PHE B CA  1 
ATOM   2975 C C   . PHE B 1 134 ? 102.00600 115.17900 118.28300 1.000 39.64569  ? 141 PHE B C   1 
ATOM   2976 O O   . PHE B 1 134 ? 100.97400 115.31100 118.94100 1.000 50.02236  ? 141 PHE B O   1 
ATOM   2977 C CB  . PHE B 1 134 ? 102.76600 117.04500 116.80800 1.000 41.37671  ? 141 PHE B CB  1 
ATOM   2978 C CG  . PHE B 1 134 ? 101.37200 117.54600 116.61300 1.000 46.96572  ? 141 PHE B CG  1 
ATOM   2979 C CD1 . PHE B 1 134 ? 100.94300 118.69300 117.24300 1.000 52.60341  ? 141 PHE B CD1 1 
ATOM   2980 C CD2 . PHE B 1 134 ? 100.48800 116.86700 115.80000 1.000 43.67734  ? 141 PHE B CD2 1 
ATOM   2981 C CE1 . PHE B 1 134 ? 99.66300  119.15400 117.06400 1.000 47.90009  ? 141 PHE B CE1 1 
ATOM   2982 C CE2 . PHE B 1 134 ? 99.20700  117.32400 115.62000 1.000 45.30161  ? 141 PHE B CE2 1 
ATOM   2983 C CZ  . PHE B 1 134 ? 98.79300  118.46700 116.25300 1.000 48.25408  ? 141 PHE B CZ  1 
ATOM   2984 N N   . PHE B 1 135 ? 102.29200 114.04200 117.65100 1.000 37.30792  ? 142 PHE B N   1 
ATOM   2985 C CA  . PHE B 1 135 ? 101.41100 112.88500 117.81000 1.000 46.27983  ? 142 PHE B CA  1 
ATOM   2986 C C   . PHE B 1 135 ? 101.44500 112.29600 119.21400 1.000 55.19862  ? 142 PHE B C   1 
ATOM   2987 O O   . PHE B 1 135 ? 100.42200 111.77500 119.67700 1.000 62.21921  ? 142 PHE B O   1 
ATOM   2988 C CB  . PHE B 1 135 ? 101.73600 111.78900 116.79400 1.000 47.01288  ? 142 PHE B CB  1 
ATOM   2989 C CG  . PHE B 1 135 ? 101.65800 112.22900 115.36400 1.000 48.16098  ? 142 PHE B CG  1 
ATOM   2990 C CD1 . PHE B 1 135 ? 100.84500 113.28200 114.99000 1.000 49.41180  ? 142 PHE B CD1 1 
ATOM   2991 C CD2 . PHE B 1 135 ? 102.36900 111.56500 114.38500 1.000 42.47948  ? 142 PHE B CD2 1 
ATOM   2992 C CE1 . PHE B 1 135 ? 100.76400 113.67600 113.67500 1.000 48.13989  ? 142 PHE B CE1 1 
ATOM   2993 C CE2 . PHE B 1 135 ? 102.28800 111.95500 113.07300 1.000 43.14560  ? 142 PHE B CE2 1 
ATOM   2994 C CZ  . PHE B 1 135 ? 101.48100 113.01000 112.71800 1.000 42.72774  ? 142 PHE B CZ  1 
ATOM   2995 N N   . ASN B 1 136 ? 102.54100 112.46200 119.95800 1.000 57.29237  ? 143 ASN B N   1 
ATOM   2996 C CA  . ASN B 1 136 ? 102.49300 111.98400 121.34000 1.000 51.89753  ? 143 ASN B CA  1 
ATOM   2997 C C   . ASN B 1 136 ? 101.72900 112.92800 122.26300 1.000 47.46150  ? 143 ASN B C   1 
ATOM   2998 O O   . ASN B 1 136 ? 100.99200 112.46600 123.14700 1.000 57.19974  ? 143 ASN B O   1 
ATOM   2999 C CB  . ASN B 1 136 ? 103.90500 111.76400 121.87500 1.000 56.29634  ? 143 ASN B CB  1 
ATOM   3000 C CG  . ASN B 1 136 ? 104.58700 110.57700 121.23300 1.000 61.12870  ? 143 ASN B CG  1 
ATOM   3001 O OD1 . ASN B 1 136 ? 103.95400 109.78800 120.53600 1.000 56.01683  ? 143 ASN B OD1 1 
ATOM   3002 N ND2 . ASN B 1 136 ? 105.88500 110.44200 121.46700 1.000 61.18441  ? 143 ASN B ND2 1 
ATOM   3003 N N   . LEU B 1 137 ? 101.80300 114.23300 122.01500 1.000 44.79895  ? 144 LEU B N   1 
ATOM   3004 C CA  . LEU B 1 137 ? 100.94800 115.16000 122.75000 1.000 48.18601  ? 144 LEU B CA  1 
ATOM   3005 C C   . LEU B 1 137 ? 99.48300  114.97900 122.37900 1.000 53.83953  ? 144 LEU B C   1 
ATOM   3006 O O   . LEU B 1 137 ? 98.60600  115.03000 123.24900 1.000 55.47117  ? 144 LEU B O   1 
ATOM   3007 C CB  . LEU B 1 137 ? 101.38700 116.59400 122.48400 1.000 44.74818  ? 144 LEU B CB  1 
ATOM   3008 C CG  . LEU B 1 137 ? 102.77400 116.95900 122.99000 1.000 44.11786  ? 144 LEU B CG  1 
ATOM   3009 C CD1 . LEU B 1 137 ? 103.06400 118.41500 122.72100 1.000 45.82170  ? 144 LEU B CD1 1 
ATOM   3010 C CD2 . LEU B 1 137 ? 102.85400 116.66700 124.46600 1.000 53.54019  ? 144 LEU B CD2 1 
ATOM   3011 N N   . PHE B 1 138 ? 99.19700  114.77700 121.09500 1.000 58.63693  ? 145 PHE B N   1 
ATOM   3012 C CA  . PHE B 1 138 ? 97.83800  114.47100 120.67100 1.000 56.26104  ? 145 PHE B CA  1 
ATOM   3013 C C   . PHE B 1 138 ? 97.29000  113.25500 121.40100 1.000 59.98542  ? 145 PHE B C   1 
ATOM   3014 O O   . PHE B 1 138 ? 96.16700  113.28400 121.90700 1.000 61.95122  ? 145 PHE B O   1 
ATOM   3015 C CB  . PHE B 1 138 ? 97.78100  114.24300 119.16500 1.000 52.76497  ? 145 PHE B CB  1 
ATOM   3016 C CG  . PHE B 1 138 ? 96.43600  113.79200 118.68200 1.000 53.77920  ? 145 PHE B CG  1 
ATOM   3017 C CD1 . PHE B 1 138 ? 95.46600  114.71300 118.35500 1.000 60.52970  ? 145 PHE B CD1 1 
ATOM   3018 C CD2 . PHE B 1 138 ? 96.13600  112.44900 118.57300 1.000 57.47157  ? 145 PHE B CD2 1 
ATOM   3019 C CE1 . PHE B 1 138 ? 94.22800  114.30400 117.91800 1.000 63.62792  ? 145 PHE B CE1 1 
ATOM   3020 C CE2 . PHE B 1 138 ? 94.89900  112.03700 118.14200 1.000 60.40395  ? 145 PHE B CE2 1 
ATOM   3021 C CZ  . PHE B 1 138 ? 93.94500  112.96400 117.81200 1.000 59.48142  ? 145 PHE B CZ  1 
ATOM   3022 N N   . LEU B 1 139 ? 98.04000  112.15100 121.40000 1.000 61.34175  ? 146 LEU B N   1 
ATOM   3023 C CA  . LEU B 1 139 ? 97.57400  110.94800 122.08200 1.000 56.54635  ? 146 LEU B CA  1 
ATOM   3024 C C   . LEU B 1 139 ? 97.33500  111.17800 123.57100 1.000 60.00255  ? 146 LEU B C   1 
ATOM   3025 O O   . LEU B 1 139 ? 96.33100  110.70500 124.11600 1.000 64.81891  ? 146 LEU B O   1 
ATOM   3026 C CB  . LEU B 1 139 ? 98.57200  109.81300 121.87100 1.000 55.98960  ? 146 LEU B CB  1 
ATOM   3027 C CG  . LEU B 1 139 ? 98.22400  108.49100 122.54600 1.000 56.67821  ? 146 LEU B CG  1 
ATOM   3028 C CD1 . LEU B 1 139 ? 96.88800  107.98400 122.05800 1.000 59.51596  ? 146 LEU B CD1 1 
ATOM   3029 C CD2 . LEU B 1 139 ? 99.30900  107.46700 122.28300 1.000 58.75520  ? 146 LEU B CD2 1 
ATOM   3030 N N   . GLU B 1 140 ? 98.24500  111.87600 124.25700 1.000 65.71725  ? 147 GLU B N   1 
ATOM   3031 C CA  . GLU B 1 140 ? 98.01000  112.17500 125.67200 1.000 62.00497  ? 147 GLU B CA  1 
ATOM   3032 C C   . GLU B 1 140 ? 96.75900  113.02600 125.89500 1.000 65.86739  ? 147 GLU B C   1 
ATOM   3033 O O   . GLU B 1 140 ? 95.97500  112.75900 126.81800 1.000 66.49241  ? 147 GLU B O   1 
ATOM   3034 C CB  . GLU B 1 140 ? 99.23300  112.86700 126.27000 1.000 58.59770  ? 147 GLU B CB  1 
ATOM   3035 N N   . ARG B 1 141 ? 96.48800  113.97400 124.99500 1.000 70.25990  ? 148 ARG B N   1 
ATOM   3036 C CA  . ARG B 1 141 ? 95.24800  114.74600 125.08500 1.000 71.71407  ? 148 ARG B CA  1 
ATOM   3037 C C   . ARG B 1 141 ? 94.01700  113.89500 124.81600 1.000 74.98271  ? 148 ARG B C   1 
ATOM   3038 O O   . ARG B 1 141 ? 92.98800  114.05800 125.48000 1.000 75.70254  ? 148 ARG B O   1 
ATOM   3039 C CB  . ARG B 1 141 ? 95.29200  115.92900 124.12000 1.000 68.96762  ? 148 ARG B CB  1 
ATOM   3040 C CG  . ARG B 1 141 ? 96.32100  117.00400 124.44400 1.000 69.51672  ? 148 ARG B CG  1 
ATOM   3041 C CD  . ARG B 1 141 ? 96.04600  117.70200 125.76800 1.000 70.97510  ? 148 ARG B CD  1 
ATOM   3042 N NE  . ARG B 1 141 ? 96.50200  116.94900 126.92800 1.000 72.90938  ? 148 ARG B NE  1 
ATOM   3043 C CZ  . ARG B 1 141 ? 96.05800  117.14000 128.16200 1.000 71.37043  ? 148 ARG B CZ  1 
ATOM   3044 N NH1 . ARG B 1 141 ? 95.13700  118.05000 128.43000 1.000 72.23136  ? 148 ARG B NH1 1 
ATOM   3045 N NH2 . ARG B 1 141 ? 96.54800  116.39900 129.15100 1.000 70.19141  ? 148 ARG B NH2 1 
ATOM   3046 N N   . LEU B 1 142 ? 94.08300  113.01400 123.82600 1.000 74.67704  ? 149 LEU B N   1 
ATOM   3047 C CA  . LEU B 1 142 ? 92.93800  112.16700 123.51600 1.000 69.84810  ? 149 LEU B CA  1 
ATOM   3048 C C   . LEU B 1 142 ? 92.62100  111.21700 124.66300 1.000 72.14405  ? 149 LEU B C   1 
ATOM   3049 O O   . LEU B 1 142 ? 91.44900  111.00300 124.99500 1.000 73.66398  ? 149 LEU B O   1 
ATOM   3050 C CB  . LEU B 1 142 ? 93.20300  111.39400 122.22900 1.000 65.76263  ? 149 LEU B CB  1 
ATOM   3051 C CG  . LEU B 1 142 ? 92.08600  110.47600 121.76100 1.000 70.92147  ? 149 LEU B CG  1 
ATOM   3052 C CD1 . LEU B 1 142 ? 90.82200  111.27400 121.57300 1.000 74.40070  ? 149 LEU B CD1 1 
ATOM   3053 C CD2 . LEU B 1 142 ? 92.49400  109.82400 120.46700 1.000 69.57890  ? 149 LEU B CD2 1 
ATOM   3054 N N   . ILE B 1 143 ? 93.65000  110.62100 125.27000 1.000 75.19850  ? 150 ILE B N   1 
ATOM   3055 C CA  . ILE B 1 143 ? 93.43600  109.79700 126.45800 1.000 71.24166  ? 150 ILE B CA  1 
ATOM   3056 C C   . ILE B 1 143 ? 92.81500  110.60900 127.58700 1.000 74.79114  ? 150 ILE B C   1 
ATOM   3057 O O   . ILE B 1 143 ? 91.90800  110.13500 128.28000 1.000 80.62334  ? 150 ILE B O   1 
ATOM   3058 C CB  . ILE B 1 143 ? 94.75700  109.14300 126.90200 1.000 73.30017  ? 150 ILE B CB  1 
ATOM   3059 C CG1 . ILE B 1 143 ? 95.29200  108.21500 125.81700 1.000 73.90770  ? 150 ILE B CG1 1 
ATOM   3060 C CG2 . ILE B 1 143 ? 94.55500  108.36800 128.18500 1.000 74.37410  ? 150 ILE B CG2 1 
ATOM   3061 C CD1 . ILE B 1 143 ? 94.40300  107.04700 125.53300 1.000 74.77975  ? 150 ILE B CD1 1 
ATOM   3062 N N   . THR B 1 144 ? 93.26900  111.85200 127.78000 1.000 79.07762  ? 151 THR B N   1 
ATOM   3063 C CA  . THR B 1 144 ? 92.67600  112.68200 128.82800 1.000 81.19072  ? 151 THR B CA  1 
ATOM   3064 C C   . THR B 1 144 ? 91.21100  113.00800 128.54800 1.000 81.79385  ? 151 THR B C   1 
ATOM   3065 O O   . THR B 1 144 ? 90.37600  112.98300 129.46000 1.000 80.09293  ? 151 THR B O   1 
ATOM   3066 C CB  . THR B 1 144 ? 93.48000  113.96900 128.99500 1.000 81.26308  ? 151 THR B CB  1 
ATOM   3067 O OG1 . THR B 1 144 ? 94.83100  113.64700 129.34500 1.000 82.57371  ? 151 THR B OG1 1 
ATOM   3068 C CG2 . THR B 1 144 ? 92.87800  114.83300 130.08400 1.000 80.68293  ? 151 THR B CG2 1 
ATOM   3069 N N   . ILE B 1 145 ? 90.87600  113.29100 127.29000 1.000 86.31360  ? 152 ILE B N   1 
ATOM   3070 C CA  . ILE B 1 145 ? 89.48700  113.55300 126.91800 1.000 85.74957  ? 152 ILE B CA  1 
ATOM   3071 C C   . ILE B 1 145 ? 88.61000  112.32100 127.11500 1.000 84.53648  ? 152 ILE B C   1 
ATOM   3072 O O   . ILE B 1 145 ? 87.48900  112.42200 127.62600 1.000 85.46891  ? 152 ILE B O   1 
ATOM   3073 C CB  . ILE B 1 145 ? 89.41300  114.07000 125.47100 1.000 84.93529  ? 152 ILE B CB  1 
ATOM   3074 C CG1 . ILE B 1 145 ? 89.98400  115.48200 125.38100 1.000 83.82336  ? 152 ILE B CG1 1 
ATOM   3075 C CG2 . ILE B 1 145 ? 87.98500  114.05700 124.97300 1.000 85.82192  ? 152 ILE B CG2 1 
ATOM   3076 C CD1 . ILE B 1 145 ? 90.33600  115.89700 123.98000 1.000 84.53211  ? 152 ILE B CD1 1 
ATOM   3077 N N   . ILE B 1 146 ? 89.08600  111.14700 126.69700 1.000 87.18894  ? 153 ILE B N   1 
ATOM   3078 C CA  . ILE B 1 146 ? 88.31600  109.92100 126.90600 1.000 88.57713  ? 153 ILE B CA  1 
ATOM   3079 C C   . ILE B 1 146 ? 88.12300  109.63700 128.39100 1.000 88.85752  ? 153 ILE B C   1 
ATOM   3080 O O   . ILE B 1 146 ? 87.03900  109.22400 128.81900 1.000 89.11154  ? 153 ILE B O   1 
ATOM   3081 C CB  . ILE B 1 146 ? 88.98200  108.73400 126.18600 1.000 86.31673  ? 153 ILE B CB  1 
ATOM   3082 C CG1 . ILE B 1 146 ? 88.99400  108.96200 124.67700 1.000 87.03460  ? 153 ILE B CG1 1 
ATOM   3083 C CG2 . ILE B 1 146 ? 88.26500  107.44100 126.51100 1.000 85.10380  ? 153 ILE B CG2 1 
ATOM   3084 C CD1 . ILE B 1 146 ? 89.95100  108.06600 123.93700 1.000 84.85520  ? 153 ILE B CD1 1 
ATOM   3085 N N   . ALA B 1 147 ? 89.15600  109.86300 129.20300 1.000 98.42725  ? 154 ALA B N   1 
ATOM   3086 C CA  . ALA B 1 147 ? 89.01100  109.69300 130.64600 1.000 99.62045  ? 154 ALA B CA  1 
ATOM   3087 C C   . ALA B 1 147 ? 87.98600  110.65500 131.23500 1.000 99.32469  ? 154 ALA B C   1 
ATOM   3088 O O   . ALA B 1 147 ? 87.15100  110.25600 132.05600 1.000 100.82026 ? 154 ALA B O   1 
ATOM   3089 C CB  . ALA B 1 147 ? 90.36400  109.87100 131.33300 1.000 99.84542  ? 154 ALA B CB  1 
ATOM   3090 N N   . TYR B 1 148 ? 88.02100  111.92100 130.81700 1.000 102.74252 ? 155 TYR B N   1 
ATOM   3091 C CA  . TYR B 1 148 ? 87.03500  112.89000 131.28900 1.000 104.90799 ? 155 TYR B CA  1 
ATOM   3092 C C   . TYR B 1 148 ? 85.61800  112.49900 130.88900 1.000 106.56291 ? 155 TYR B C   1 
ATOM   3093 O O   . TYR B 1 148 ? 84.69100  112.57200 131.70200 1.000 107.66922 ? 155 TYR B O   1 
ATOM   3094 C CB  . TYR B 1 148 ? 87.37500  114.28200 130.75600 1.000 107.09267 ? 155 TYR B CB  1 
ATOM   3095 C CG  . TYR B 1 148 ? 86.32300  115.32500 131.05500 1.000 108.01145 ? 155 TYR B CG  1 
ATOM   3096 C CD1 . TYR B 1 148 ? 86.28100  115.96000 132.28800 1.000 106.63310 ? 155 TYR B CD1 1 
ATOM   3097 C CD2 . TYR B 1 148 ? 85.37400  115.67600 130.10400 1.000 106.55640 ? 155 TYR B CD2 1 
ATOM   3098 C CE1 . TYR B 1 148 ? 85.32200  116.91500 132.56500 1.000 106.87056 ? 155 TYR B CE1 1 
ATOM   3099 C CE2 . TYR B 1 148 ? 84.41200  116.62800 130.37300 1.000 106.17148 ? 155 TYR B CE2 1 
ATOM   3100 C CZ  . TYR B 1 148 ? 84.39000  117.24400 131.60400 1.000 107.94348 ? 155 TYR B CZ  1 
ATOM   3101 O OH  . TYR B 1 148 ? 83.43200  118.19300 131.87500 1.000 109.21814 ? 155 TYR B OH  1 
ATOM   3102 N N   . ILE B 1 149 ? 85.42200  112.10800 129.63100 1.000 107.67383 ? 156 ILE B N   1 
ATOM   3103 C CA  . ILE B 1 149 ? 84.09400  111.70600 129.17400 1.000 107.78644 ? 156 ILE B CA  1 
ATOM   3104 C C   . ILE B 1 149 ? 83.60100  110.47400 129.92700 1.000 109.84537 ? 156 ILE B C   1 
ATOM   3105 O O   . ILE B 1 149 ? 82.43300  110.40300 130.32500 1.000 109.69870 ? 156 ILE B O   1 
ATOM   3106 C CB  . ILE B 1 149 ? 84.10000  111.47600 127.65200 1.000 107.71501 ? 156 ILE B CB  1 
ATOM   3107 C CG1 . ILE B 1 149 ? 84.21800  112.81100 126.91800 1.000 106.55949 ? 156 ILE B CG1 1 
ATOM   3108 C CG2 . ILE B 1 149 ? 82.84600  110.74100 127.21600 1.000 107.95644 ? 156 ILE B CG2 1 
ATOM   3109 C CD1 . ILE B 1 149 ? 84.44800  112.67000 125.43200 1.000 107.21389 ? 156 ILE B CD1 1 
ATOM   3110 N N   . MET B 1 150 ? 84.46500  109.47300 130.10700 1.000 117.39763 ? 157 MET B N   1 
ATOM   3111 C CA  . MET B 1 150 ? 84.07600  108.28000 130.85400 1.000 117.01975 ? 157 MET B CA  1 
ATOM   3112 C C   . MET B 1 150 ? 83.72800  108.59800 132.30500 1.000 118.87754 ? 157 MET B C   1 
ATOM   3113 O O   . MET B 1 150 ? 82.78300  108.02900 132.86000 1.000 118.87039 ? 157 MET B O   1 
ATOM   3114 C CB  . MET B 1 150 ? 85.19000  107.23500 130.78800 1.000 113.83181 ? 157 MET B CB  1 
ATOM   3115 N N   . LYS B 1 151 ? 84.47000  109.51200 132.93600 1.000 121.62411 ? 158 LYS B N   1 
ATOM   3116 C CA  . LYS B 1 151 ? 84.11600  109.94900 134.28600 1.000 120.85177 ? 158 LYS B CA  1 
ATOM   3117 C C   . LYS B 1 151 ? 82.79400  110.71000 134.32100 1.000 122.53886 ? 158 LYS B C   1 
ATOM   3118 O O   . LYS B 1 151 ? 82.00800  110.55300 135.26200 1.000 123.36688 ? 158 LYS B O   1 
ATOM   3119 C CB  . LYS B 1 151 ? 85.23800  110.80800 134.86800 1.000 120.03809 ? 158 LYS B CB  1 
ATOM   3120 N N   . SER B 1 152 ? 82.53100  111.54300 133.31400 1.000 126.25364 ? 159 SER B N   1 
ATOM   3121 C CA  . SER B 1 152 ? 81.24100  112.22200 133.22600 1.000 127.05163 ? 159 SER B CA  1 
ATOM   3122 C C   . SER B 1 152 ? 80.09100  111.23900 133.03400 1.000 128.06977 ? 159 SER B C   1 
ATOM   3123 O O   . SER B 1 152 ? 79.00400  111.42900 133.59200 1.000 128.03381 ? 159 SER B O   1 
ATOM   3124 C CB  . SER B 1 152 ? 81.26300  113.24200 132.08800 1.000 125.74619 ? 159 SER B CB  1 
ATOM   3125 N N   . CYS B 1 153 ? 80.31200  110.18300 132.25100 1.000 131.67628 ? 160 CYS B N   1 
ATOM   3126 C CA  . CYS B 1 153 ? 79.31800  109.11900 132.12900 1.000 131.73269 ? 160 CYS B CA  1 
ATOM   3127 C C   . CYS B 1 153 ? 79.12800  108.36600 133.44100 1.000 132.34595 ? 160 CYS B C   1 
ATOM   3128 O O   . CYS B 1 153 ? 77.99800  108.01600 133.80100 1.000 132.11935 ? 160 CYS B O   1 
ATOM   3129 C CB  . CYS B 1 153 ? 79.71800  108.15500 131.01100 1.000 130.26688 ? 160 CYS B CB  1 
ATOM   3130 N N   . HIS B 1 154 ? 80.21800  108.09600 134.16100 1.000 135.81647 ? 161 HIS B N   1 
ATOM   3131 C CA  . HIS B 1 154 ? 80.09800  107.47100 135.47500 1.000 136.64269 ? 161 HIS B CA  1 
ATOM   3132 C C   . HIS B 1 154 ? 79.29000  108.34300 136.42700 1.000 138.02293 ? 161 HIS B C   1 
ATOM   3133 O O   . HIS B 1 154 ? 78.49100  107.83400 137.22200 1.000 137.42000 ? 161 HIS B O   1 
ATOM   3134 C CB  . HIS B 1 154 ? 81.48500  107.18800 136.05200 1.000 135.56406 ? 161 HIS B CB  1 
ATOM   3135 N N   . GLN B 1 155 ? 79.48500  109.66100 136.36100 1.000 139.16124 ? 162 GLN B N   1 
ATOM   3136 C CA  . GLN B 1 155 ? 78.64700  110.57300 137.13200 1.000 138.00308 ? 162 GLN B CA  1 
ATOM   3137 C C   . GLN B 1 155 ? 77.23600  110.64300 136.56000 1.000 139.01626 ? 162 GLN B C   1 
ATOM   3138 O O   . GLN B 1 155 ? 76.25800  110.71700 137.31400 1.000 138.59006 ? 162 GLN B O   1 
ATOM   3139 C CB  . GLN B 1 155 ? 79.28100  111.96300 137.17300 1.000 136.95968 ? 162 GLN B CB  1 
ATOM   3140 N N   . ARG B 1 156 ? 77.11000  110.63400 135.23100 1.000 144.03472 ? 163 ARG B N   1 
ATOM   3141 C CA  . ARG B 1 156 ? 75.79300  110.62000 134.60300 1.000 144.28409 ? 163 ARG B CA  1 
ATOM   3142 C C   . ARG B 1 156 ? 75.00800  109.35200 134.91500 1.000 144.38020 ? 163 ARG B C   1 
ATOM   3143 O O   . ARG B 1 156 ? 73.77800  109.35600 134.80400 1.000 143.70756 ? 163 ARG B O   1 
ATOM   3144 C CB  . ARG B 1 156 ? 75.92800  110.78200 133.08800 1.000 143.22424 ? 163 ARG B CB  1 
ATOM   3145 N N   . GLN B 1 157 ? 75.68700  108.26900 135.29900 1.000 144.40227 ? 164 GLN B N   1 
ATOM   3146 C CA  . GLN B 1 157 ? 74.99700  107.06400 135.74300 1.000 144.14231 ? 164 GLN B CA  1 
ATOM   3147 C C   . GLN B 1 157 ? 74.32700  107.22300 137.10300 1.000 144.76408 ? 164 GLN B C   1 
ATOM   3148 O O   . GLN B 1 157 ? 73.53400  106.35400 137.48300 1.000 144.77359 ? 164 GLN B O   1 
ATOM   3149 C CB  . GLN B 1 157 ? 75.97600  105.88900 135.78700 1.000 143.18568 ? 164 GLN B CB  1 
ATOM   3150 N N   . LEU B 1 158 ? 74.62300  108.29000 137.83900 1.000 144.74113 ? 165 LEU B N   1 
ATOM   3151 C CA  . LEU B 1 158 ? 74.03600  108.49500 139.16000 1.000 144.09523 ? 165 LEU B CA  1 
ATOM   3152 C C   . LEU B 1 158 ? 72.52600  108.69200 139.07100 1.000 144.08408 ? 165 LEU B C   1 
ATOM   3153 O O   . LEU B 1 158 ? 72.04100  109.82200 139.00700 1.000 143.64329 ? 165 LEU B O   1 
ATOM   3154 C CB  . LEU B 1 158 ? 74.68200  109.69500 139.85600 1.000 143.67476 ? 165 LEU B CB  1 
ATOM   3155 N N   . TRP B 1 183 ? 89.53700  107.01400 137.33000 1.000 130.88915 ? 190 TRP B N   1 
ATOM   3156 C CA  . TRP B 1 183 ? 90.72000  106.35700 136.78700 1.000 131.88576 ? 190 TRP B CA  1 
ATOM   3157 C C   . TRP B 1 183 ? 90.76600  106.48200 135.26900 1.000 132.90808 ? 190 TRP B C   1 
ATOM   3158 O O   . TRP B 1 183 ? 89.75800  106.78100 134.63000 1.000 132.08160 ? 190 TRP B O   1 
ATOM   3159 C CB  . TRP B 1 183 ? 90.74900  104.88300 137.19500 1.000 130.45057 ? 190 TRP B CB  1 
ATOM   3160 N N   . LYS B 1 184 ? 91.94600  106.24900 134.70000 1.000 131.98148 ? 191 LYS B N   1 
ATOM   3161 C CA  . LYS B 1 184 ? 92.11500  106.29800 133.26000 1.000 130.93604 ? 191 LYS B CA  1 
ATOM   3162 C C   . LYS B 1 184 ? 91.39900  105.12100 132.59600 1.000 130.98811 ? 191 LYS B C   1 
ATOM   3163 O O   . LYS B 1 184 ? 91.12500  104.10500 133.23900 1.000 131.24487 ? 191 LYS B O   1 
ATOM   3164 C CB  . LYS B 1 184 ? 93.60200  106.28300 132.91200 1.000 129.28190 ? 191 LYS B CB  1 
ATOM   3165 N N   . PRO B 1 185 ? 91.08100  105.23500 131.30700 1.000 121.26548 ? 192 PRO B N   1 
ATOM   3166 C CA  . PRO B 1 185 ? 90.42500  104.12300 130.61500 1.000 120.43687 ? 192 PRO B CA  1 
ATOM   3167 C C   . PRO B 1 185 ? 91.37900  102.95900 130.39800 1.000 120.50314 ? 192 PRO B C   1 
ATOM   3168 O O   . PRO B 1 185 ? 92.59300  103.13400 130.27700 1.000 121.01720 ? 192 PRO B O   1 
ATOM   3169 C CB  . PRO B 1 185 ? 89.99000  104.74800 129.28700 1.000 120.79500 ? 192 PRO B CB  1 
ATOM   3170 C CG  . PRO B 1 185 ? 91.01500  105.78800 129.03800 1.000 119.14585 ? 192 PRO B CG  1 
ATOM   3171 C CD  . PRO B 1 185 ? 91.31000  106.37200 130.39800 1.000 119.66741 ? 192 PRO B CD  1 
ATOM   3172 N N   . SER B 1 186 ? 90.81100  101.75700 130.34300 1.000 107.95879 ? 193 SER B N   1 
ATOM   3173 C CA  . SER B 1 186 ? 91.59900  100.59000 129.98100 1.000 107.59173 ? 193 SER B CA  1 
ATOM   3174 C C   . SER B 1 186 ? 91.90200  100.58100 128.48700 1.000 106.18494 ? 193 SER B C   1 
ATOM   3175 O O   . SER B 1 186 ? 91.12900  101.08400 127.66800 1.000 105.62990 ? 193 SER B O   1 
ATOM   3176 C CB  . SER B 1 186 ? 90.86900  99.30800  130.37200 1.000 107.12023 ? 193 SER B CB  1 
ATOM   3177 O OG  . SER B 1 186 ? 89.69900  99.13500  129.59600 1.000 106.53673 ? 193 SER B OG  1 
ATOM   3178 N N   . VAL B 1 187 ? 93.04700  99.98900  128.14200 1.000 96.83772  ? 194 VAL B N   1 
ATOM   3179 C CA  . VAL B 1 187 ? 93.59800  100.10000 126.79400 1.000 94.92826  ? 194 VAL B CA  1 
ATOM   3180 C C   . VAL B 1 187 ? 92.67700  99.48500  125.75200 1.000 94.78932  ? 194 VAL B C   1 
ATOM   3181 O O   . VAL B 1 187 ? 92.60400  99.96800  124.61800 1.000 99.42365  ? 194 VAL B O   1 
ATOM   3182 C CB  . VAL B 1 187 ? 95.00000  99.46700  126.74200 1.000 93.83944  ? 194 VAL B CB  1 
ATOM   3183 C CG1 . VAL B 1 187 ? 95.62900  99.69800  125.38800 1.000 89.30653  ? 194 VAL B CG1 1 
ATOM   3184 C CG2 . VAL B 1 187 ? 95.87700  100.04600 127.83400 1.000 96.24187  ? 194 VAL B CG2 1 
ATOM   3185 N N   . TYR B 1 188 ? 91.97200  98.40900  126.10300 1.000 99.34827  ? 195 TYR B N   1 
ATOM   3186 C CA  . TYR B 1 188 ? 91.06600  97.76900  125.15300 1.000 101.44583 ? 195 TYR B CA  1 
ATOM   3187 C C   . TYR B 1 188 ? 89.94100  98.70100  124.70500 1.000 101.49691 ? 195 TYR B C   1 
ATOM   3188 O O   . TYR B 1 188 ? 89.61900  98.76900  123.51100 1.000 105.55463 ? 195 TYR B O   1 
ATOM   3189 C CB  . TYR B 1 188 ? 90.50700  96.48900  125.77100 1.000 101.47916 ? 195 TYR B CB  1 
ATOM   3190 C CG  . TYR B 1 188 ? 89.59500  95.70400  124.86500 1.000 103.18818 ? 195 TYR B CG  1 
ATOM   3191 C CD1 . TYR B 1 188 ? 90.10700  94.96900  123.80700 1.000 101.07927 ? 195 TYR B CD1 1 
ATOM   3192 C CD2 . TYR B 1 188 ? 88.22600  95.66600  125.08800 1.000 103.25975 ? 195 TYR B CD2 1 
ATOM   3193 C CE1 . TYR B 1 188 ? 89.28000  94.23900  122.97800 1.000 103.56231 ? 195 TYR B CE1 1 
ATOM   3194 C CE2 . TYR B 1 188 ? 87.39000  94.93400  124.26900 1.000 103.29371 ? 195 TYR B CE2 1 
ATOM   3195 C CZ  . TYR B 1 188 ? 87.92200  94.22400  123.21400 1.000 104.93266 ? 195 TYR B CZ  1 
ATOM   3196 O OH  . TYR B 1 188 ? 87.09300  93.49300  122.39300 1.000 101.96879 ? 195 TYR B OH  1 
ATOM   3197 N N   . TYR B 1 189 ? 89.33500  99.43700  125.63600 1.000 97.25283  ? 196 TYR B N   1 
ATOM   3198 C CA  . TYR B 1 189 ? 88.29000  100.37500 125.23800 1.000 98.07373  ? 196 TYR B CA  1 
ATOM   3199 C C   . TYR B 1 189 ? 88.84100  101.57700 124.48100 1.000 98.81228  ? 196 TYR B C   1 
ATOM   3200 O O   . TYR B 1 189 ? 88.16300  102.10500 123.59300 1.000 101.50091 ? 196 TYR B O   1 
ATOM   3201 C CB  . TYR B 1 189 ? 87.49400  100.83100 126.45700 1.000 101.82404 ? 196 TYR B CB  1 
ATOM   3202 C CG  . TYR B 1 189 ? 86.70600  99.71800  127.10700 1.000 103.90458 ? 196 TYR B CG  1 
ATOM   3203 C CD1 . TYR B 1 189 ? 85.78300  98.98200  126.37800 1.000 103.91257 ? 196 TYR B CD1 1 
ATOM   3204 C CD2 . TYR B 1 189 ? 86.88000  99.40400  128.44700 1.000 102.46384 ? 196 TYR B CD2 1 
ATOM   3205 C CE1 . TYR B 1 189 ? 85.06000  97.96300  126.96300 1.000 102.24674 ? 196 TYR B CE1 1 
ATOM   3206 C CE2 . TYR B 1 189 ? 86.16100  98.38600  129.04100 1.000 102.47611 ? 196 TYR B CE2 1 
ATOM   3207 C CZ  . TYR B 1 189 ? 85.25200  97.66900  128.29400 1.000 103.47904 ? 196 TYR B CZ  1 
ATOM   3208 O OH  . TYR B 1 189 ? 84.53100  96.65600  128.88200 1.000 105.21075 ? 196 TYR B OH  1 
ATOM   3209 N N   . VAL B 1 190 ? 90.07100  102.00100 124.77300 1.000 81.11869  ? 197 VAL B N   1 
ATOM   3210 C CA  . VAL B 1 190 ? 90.69200  103.02700 123.94100 1.000 79.16977  ? 197 VAL B CA  1 
ATOM   3211 C C   . VAL B 1 190 ? 90.90900  102.51300 122.52500 1.000 80.43283  ? 197 VAL B C   1 
ATOM   3212 O O   . VAL B 1 190 ? 90.71400  103.24400 121.54800 1.000 85.76821  ? 197 VAL B O   1 
ATOM   3213 C CB  . VAL B 1 190 ? 92.00700  103.51100 124.57300 1.000 79.96621  ? 197 VAL B CB  1 
ATOM   3214 C CG1 . VAL B 1 190 ? 92.69500  104.50000 123.65700 1.000 79.46023  ? 197 VAL B CG1 1 
ATOM   3215 C CG2 . VAL B 1 190 ? 91.73500  104.14400 125.91500 1.000 82.08590  ? 197 VAL B CG2 1 
ATOM   3216 N N   . MET B 1 191 ? 91.33200  101.25800 122.38700 1.000 79.40879  ? 198 MET B N   1 
ATOM   3217 C CA  . MET B 1 191 ? 91.49300  100.68600 121.05600 1.000 76.64245  ? 198 MET B CA  1 
ATOM   3218 C C   . MET B 1 191 ? 90.16900  100.63200 120.31000 1.000 79.50423  ? 198 MET B C   1 
ATOM   3219 O O   . MET B 1 191 ? 90.10900  100.94100 119.11700 1.000 84.19840  ? 198 MET B O   1 
ATOM   3220 C CB  . MET B 1 191 ? 92.10200  99.29100  121.13800 1.000 76.43298  ? 198 MET B CB  1 
ATOM   3221 C CG  . MET B 1 191 ? 92.42200  98.71100  119.77900 1.000 79.63765  ? 198 MET B CG  1 
ATOM   3222 S SD  . MET B 1 191 ? 92.85600  96.97100  119.83900 1.000 91.38137  ? 198 MET B SD  1 
ATOM   3223 C CE  . MET B 1 191 ? 91.29000  96.26100  120.32500 1.000 83.20956  ? 198 MET B CE  1 
ATOM   3224 N N   . LEU B 1 192 ? 89.09500  100.23500 120.99400 1.000 79.11367  ? 199 LEU B N   1 
ATOM   3225 C CA  . LEU B 1 192 ? 87.79000  100.19900 120.33800 1.000 78.49144  ? 199 LEU B CA  1 
ATOM   3226 C C   . LEU B 1 192 ? 87.27400  101.58600 119.97300 1.000 82.22586  ? 199 LEU B C   1 
ATOM   3227 O O   . LEU B 1 192 ? 86.55200  101.72900 118.98300 1.000 85.46359  ? 199 LEU B O   1 
ATOM   3228 C CB  . LEU B 1 192 ? 86.76800  99.48600  121.21800 1.000 81.11069  ? 199 LEU B CB  1 
ATOM   3229 C CG  . LEU B 1 192 ? 87.05000  98.01800  121.51900 1.000 86.45130  ? 199 LEU B CG  1 
ATOM   3230 C CD1 . LEU B 1 192 ? 85.91600  97.43200  122.33800 1.000 86.53640  ? 199 LEU B CD1 1 
ATOM   3231 C CD2 . LEU B 1 192 ? 87.25300  97.23700  120.23500 1.000 84.84305  ? 199 LEU B CD2 1 
ATOM   3232 N N   . ILE B 1 193 ? 87.60300  102.60900 120.76000 1.000 75.13797  ? 200 ILE B N   1 
ATOM   3233 C CA  . ILE B 1 193 ? 87.27100  103.97900 120.37000 1.000 71.33202  ? 200 ILE B CA  1 
ATOM   3234 C C   . ILE B 1 193 ? 88.06600  104.41800 119.14400 1.000 67.91905  ? 200 ILE B C   1 
ATOM   3235 O O   . ILE B 1 193 ? 87.50300  104.94500 118.18000 1.000 71.50509  ? 200 ILE B O   1 
ATOM   3236 C CB  . ILE B 1 193 ? 87.47800  104.94100 121.55000 1.000 70.53063  ? 200 ILE B CB  1 
ATOM   3237 C CG1 . ILE B 1 193 ? 86.40700  104.69700 122.61000 1.000 72.91967  ? 200 ILE B CG1 1 
ATOM   3238 C CG2 . ILE B 1 193 ? 87.44700  106.37400 121.07500 1.000 71.94208  ? 200 ILE B CG2 1 
ATOM   3239 C CD1 . ILE B 1 193 ? 86.73600  105.28400 123.95100 1.000 73.98213  ? 200 ILE B CD1 1 
ATOM   3240 N N   . LEU B 1 194 ? 89.38200  104.20800 119.15800 1.000 57.39935  ? 201 LEU B N   1 
ATOM   3241 C CA  . LEU B 1 194 ? 90.21800  104.61900 118.03100 1.000 58.90207  ? 201 LEU B CA  1 
ATOM   3242 C C   . LEU B 1 194 ? 89.92500  103.85300 116.74300 1.000 66.97516  ? 201 LEU B C   1 
ATOM   3243 O O   . LEU B 1 194 ? 90.08300  104.41400 115.65400 1.000 71.34089  ? 201 LEU B O   1 
ATOM   3244 C CB  . LEU B 1 194 ? 91.69100  104.48400 118.40100 1.000 60.60133  ? 201 LEU B CB  1 
ATOM   3245 C CG  . LEU B 1 194 ? 92.19900  105.61000 119.29300 1.000 61.02787  ? 201 LEU B CG  1 
ATOM   3246 C CD1 . LEU B 1 194 ? 93.55900  105.28400 119.85600 1.000 67.21966  ? 201 LEU B CD1 1 
ATOM   3247 C CD2 . LEU B 1 194 ? 92.26000  106.88000 118.49400 1.000 58.87002  ? 201 LEU B CD2 1 
ATOM   3248 N N   . CYS B 1 195 ? 89.51300  102.58900 116.82600 1.000 70.56794  ? 202 CYS B N   1 
ATOM   3249 C CA  . CYS B 1 195 ? 89.01800  101.90500 115.63300 1.000 66.20157  ? 202 CYS B CA  1 
ATOM   3250 C C   . CYS B 1 195 ? 87.79400  102.60500 115.05500 1.000 67.16018  ? 202 CYS B C   1 
ATOM   3251 O O   . CYS B 1 195 ? 87.69500  102.79800 113.83900 1.000 67.76217  ? 202 CYS B O   1 
ATOM   3252 C CB  . CYS B 1 195 ? 88.70300  100.44300 115.94600 1.000 67.46082  ? 202 CYS B CB  1 
ATOM   3253 S SG  . CYS B 1 195 ? 90.15200  99.43500  116.30300 1.000 80.97756  ? 202 CYS B SG  1 
ATOM   3254 N N   . THR B 1 196 ? 86.84400  102.98200 115.90900 1.000 67.91020  ? 203 THR B N   1 
ATOM   3255 C CA  . THR B 1 196 ? 85.63900  103.65800 115.43500 1.000 65.08872  ? 203 THR B CA  1 
ATOM   3256 C C   . THR B 1 196 ? 85.95900  105.00900 114.80600 1.000 67.05469  ? 203 THR B C   1 
ATOM   3257 O O   . THR B 1 196 ? 85.42400  105.35300 113.74800 1.000 69.96207  ? 203 THR B O   1 
ATOM   3258 C CB  . THR B 1 196 ? 84.64400  103.82400 116.57700 1.000 62.48728  ? 203 THR B CB  1 
ATOM   3259 O OG1 . THR B 1 196 ? 84.36900  102.54500 117.15700 1.000 70.64941  ? 203 THR B OG1 1 
ATOM   3260 C CG2 . THR B 1 196 ? 83.35400  104.41600 116.05900 1.000 65.68553  ? 203 THR B CG2 1 
ATOM   3261 N N   . ALA B 1 197 ? 86.81500  105.79900 115.45200 1.000 66.71547  ? 204 ALA B N   1 
ATOM   3262 C CA  . ALA B 1 197 ? 87.23200  107.07100 114.86900 1.000 62.85319  ? 204 ALA B CA  1 
ATOM   3263 C C   . ALA B 1 197 ? 87.91700  106.88600 113.52000 1.000 69.39431  ? 204 ALA B C   1 
ATOM   3264 O O   . ALA B 1 197 ? 87.64900  107.63700 112.57700 1.000 77.15838  ? 204 ALA B O   1 
ATOM   3265 C CB  . ALA B 1 197 ? 88.15400  107.81500 115.83200 1.000 59.76891  ? 204 ALA B CB  1 
ATOM   3266 N N   . SER B 1 198 ? 88.81000  105.90100 113.40900 1.000 61.66770  ? 205 SER B N   1 
ATOM   3267 C CA  . SER B 1 198 ? 89.51500  105.66700 112.14900 1.000 54.97388  ? 205 SER B CA  1 
ATOM   3268 C C   . SER B 1 198 ? 88.57100  105.24800 111.03000 1.000 55.17074  ? 205 SER B C   1 
ATOM   3269 O O   . SER B 1 198 ? 88.75300  105.65100 109.87700 1.000 60.20252  ? 205 SER B O   1 
ATOM   3270 C CB  . SER B 1 198 ? 90.59800  104.61400 112.34600 1.000 56.63455  ? 205 SER B CB  1 
ATOM   3271 O OG  . SER B 1 198 ? 91.49100  105.01200 113.36600 1.000 63.18605  ? 205 SER B OG  1 
ATOM   3272 N N   . ILE B 1 199 ? 87.57400  104.42300 111.33800 1.000 53.13944  ? 206 ILE B N   1 
ATOM   3273 C CA  . ILE B 1 199 ? 86.58600  104.03600 110.33500 1.000 55.83415  ? 206 ILE B CA  1 
ATOM   3274 C C   . ILE B 1 199 ? 85.71400  105.22000 109.92600 1.000 60.95919  ? 206 ILE B C   1 
ATOM   3275 O O   . ILE B 1 199 ? 85.44500  105.42200 108.73800 1.000 66.91524  ? 206 ILE B O   1 
ATOM   3276 C CB  . ILE B 1 199 ? 85.73700  102.86200 110.84800 1.000 56.67515  ? 206 ILE B CB  1 
ATOM   3277 C CG1 . ILE B 1 199 ? 86.57400  101.58900 110.89800 1.000 61.03678  ? 206 ILE B CG1 1 
ATOM   3278 C CG2 . ILE B 1 199 ? 84.53100  102.65300 109.96500 1.000 55.24272  ? 206 ILE B CG2 1 
ATOM   3279 C CD1 . ILE B 1 199 ? 85.94100  100.49100 111.69800 1.000 62.33618  ? 206 ILE B CD1 1 
ATOM   3280 N N   . LEU B 1 200 ? 85.25200  106.01500 110.89300 1.000 58.70243  ? 207 LEU B N   1 
ATOM   3281 C CA  . LEU B 1 200 ? 84.39200  107.14900 110.55600 1.000 58.16790  ? 207 LEU B CA  1 
ATOM   3282 C C   . LEU B 1 200 ? 85.11500  108.21000 109.73300 1.000 60.06474  ? 207 LEU B C   1 
ATOM   3283 O O   . LEU B 1 200 ? 84.53000  108.78000 108.80700 1.000 64.47607  ? 207 LEU B O   1 
ATOM   3284 C CB  . LEU B 1 200 ? 83.81300  107.77200 111.82100 1.000 57.22887  ? 207 LEU B CB  1 
ATOM   3285 C CG  . LEU B 1 200 ? 82.80400  106.91300 112.57600 1.000 61.36482  ? 207 LEU B CG  1 
ATOM   3286 C CD1 . LEU B 1 200 ? 82.38200  107.60200 113.85900 1.000 61.80929  ? 207 LEU B CD1 1 
ATOM   3287 C CD2 . LEU B 1 200 ? 81.60400  106.61100 111.70100 1.000 61.90624  ? 207 LEU B CD2 1 
ATOM   3288 N N   . ILE B 1 201 ? 86.37100  108.50900 110.05500 1.000 51.80149  ? 208 ILE B N   1 
ATOM   3289 C CA  . ILE B 1 201 ? 87.14000  109.43600 109.22800 1.000 52.72020  ? 208 ILE B CA  1 
ATOM   3290 C C   . ILE B 1 201 ? 87.37700  108.85600 107.83900 1.000 56.12675  ? 208 ILE B C   1 
ATOM   3291 O O   . ILE B 1 201 ? 87.19500  109.53500 106.82400 1.000 57.76687  ? 208 ILE B O   1 
ATOM   3292 C CB  . ILE B 1 201 ? 88.46800  109.79700 109.91200 1.000 47.49786  ? 208 ILE B CB  1 
ATOM   3293 C CG1 . ILE B 1 201 ? 88.20800  110.58600 111.18400 1.000 50.81516  ? 208 ILE B CG1 1 
ATOM   3294 C CG2 . ILE B 1 201 ? 89.34000  110.59700 108.98300 1.000 51.44328  ? 208 ILE B CG2 1 
ATOM   3295 C CD1 . ILE B 1 201 ? 89.36800  110.58300 112.11500 1.000 52.80926  ? 208 ILE B CD1 1 
ATOM   3296 N N   . SER B 1 202 ? 87.78000  107.58900 107.77600 1.000 53.60871  ? 209 SER B N   1 
ATOM   3297 C CA  . SER B 1 202 ? 88.05900  106.94700 106.49600 1.000 47.99211  ? 209 SER B CA  1 
ATOM   3298 C C   . SER B 1 202 ? 86.83500  106.89200 105.58800 1.000 50.89821  ? 209 SER B C   1 
ATOM   3299 O O   . SER B 1 202 ? 86.95300  107.09400 104.37600 1.000 56.55753  ? 209 SER B O   1 
ATOM   3300 C CB  . SER B 1 202 ? 88.60600  105.54500 106.73900 1.000 50.88423  ? 209 SER B CB  1 
ATOM   3301 O OG  . SER B 1 202 ? 88.94500  104.91700 105.52300 1.000 58.59703  ? 209 SER B OG  1 
ATOM   3302 N N   . CYS B 1 203 ? 85.65100  106.63600 106.14400 1.000 57.27509  ? 210 CYS B N   1 
ATOM   3303 C CA  . CYS B 1 203 ? 84.44100  106.65200 105.32300 1.000 58.78132  ? 210 CYS B CA  1 
ATOM   3304 C C   . CYS B 1 203 ? 84.05700  108.05700 104.86100 1.000 62.66508  ? 210 CYS B C   1 
ATOM   3305 O O   . CYS B 1 203 ? 83.62200  108.23200 103.71900 1.000 66.43603  ? 210 CYS B O   1 
ATOM   3306 C CB  . CYS B 1 203 ? 83.28600  106.00700 106.08200 1.000 57.46524  ? 210 CYS B CB  1 
ATOM   3307 S SG  . CYS B 1 203 ? 83.55200  104.26600 106.46800 1.000 74.73942  ? 210 CYS B SG  1 
ATOM   3308 N N   . CYS B 1 204 ? 84.22600  109.07200 105.70900 1.000 60.88637  ? 211 CYS B N   1 
ATOM   3309 C CA  . CYS B 1 204 ? 83.97600  110.44600 105.27200 1.000 59.38355  ? 211 CYS B CA  1 
ATOM   3310 C C   . CYS B 1 204 ? 84.96200  110.88600 104.19200 1.000 65.21805  ? 211 CYS B C   1 
ATOM   3311 O O   . CYS B 1 204 ? 84.57300  111.47700 103.17400 1.000 69.03106  ? 211 CYS B O   1 
ATOM   3312 C CB  . CYS B 1 204 ? 84.02900  111.39300 106.46600 1.000 64.42859  ? 211 CYS B CB  1 
ATOM   3313 S SG  . CYS B 1 204 ? 82.68400  111.17100 107.64500 1.000 83.10995  ? 211 CYS B SG  1 
ATOM   3314 N N   . ALA B 1 205 ? 86.24600  110.59500 104.38700 1.000 61.12560  ? 212 ALA B N   1 
ATOM   3315 C CA  . ALA B 1 205 ? 87.23500  110.90900 103.36400 1.000 56.42734  ? 212 ALA B CA  1 
ATOM   3316 C C   . ALA B 1 205 ? 86.93700  110.18300 102.05900 1.000 52.37531  ? 212 ALA B C   1 
ATOM   3317 O O   . ALA B 1 205 ? 87.08400  110.75800 100.97700 1.000 55.92283  ? 212 ALA B O   1 
ATOM   3318 C CB  . ALA B 1 205 ? 88.63300  110.56300 103.86800 1.000 52.68598  ? 212 ALA B CB  1 
ATOM   3319 N N   . SER B 1 206 ? 86.59900  108.89600 102.13100 1.000 48.28990  ? 213 SER B N   1 
ATOM   3320 C CA  . SER B 1 206 ? 86.22100  108.17300 100.92200 1.000 48.85410  ? 213 SER B CA  1 
ATOM   3321 C C   . SER B 1 206 ? 85.00500  108.79000 100.24400 1.000 56.04922  ? 213 SER B C   1 
ATOM   3322 O O   . SER B 1 206 ? 84.96500  108.90400 99.01500  1.000 61.82017  ? 213 SER B O   1 
ATOM   3323 C CB  . SER B 1 206 ? 85.94900  106.71100 101.25400 1.000 50.86692  ? 213 SER B CB  1 
ATOM   3324 O OG  . SER B 1 206 ? 87.11300  106.08900 101.75700 1.000 56.12201  ? 213 SER B OG  1 
ATOM   3325 N N   . ALA B 1 207 ? 84.01900  109.22800 101.02700 1.000 55.30025  ? 214 ALA B N   1 
ATOM   3326 C CA  . ALA B 1 207 ? 82.85100  109.89400 100.46200 1.000 51.68147  ? 214 ALA B CA  1 
ATOM   3327 C C   . ALA B 1 207 ? 83.17800  111.24900 99.86500  1.000 54.63871  ? 214 ALA B C   1 
ATOM   3328 O O   . ALA B 1 207 ? 82.37300  111.78100 99.09600  1.000 56.06389  ? 214 ALA B O   1 
ATOM   3329 C CB  . ALA B 1 207 ? 81.76700  110.05100 101.52500 1.000 55.92412  ? 214 ALA B CB  1 
ATOM   3330 N N   . MET B 1 208 ? 84.32400  111.82700 100.20900 1.000 56.73089  ? 215 MET B N   1 
ATOM   3331 C CA  . MET B 1 208 ? 84.74000  113.04600 99.52100  1.000 56.21801  ? 215 MET B CA  1 
ATOM   3332 C C   . MET B 1 208 ? 85.56300  112.76300 98.26600  1.000 56.65465  ? 215 MET B C   1 
ATOM   3333 O O   . MET B 1 208 ? 85.30900  113.35300 97.21300  1.000 57.02363  ? 215 MET B O   1 
ATOM   3334 C CB  . MET B 1 208 ? 85.53100  113.95400 100.46200 1.000 54.90933  ? 215 MET B CB  1 
ATOM   3335 C CG  . MET B 1 208 ? 85.96200  115.25000 99.80800  1.000 58.40828  ? 215 MET B CG  1 
ATOM   3336 S SD  . MET B 1 208 ? 86.93200  116.31100 100.88100 1.000 75.66301  ? 215 MET B SD  1 
ATOM   3337 C CE  . MET B 1 208 ? 88.41100  115.33100 101.04800 1.000 60.62919  ? 215 MET B CE  1 
ATOM   3338 N N   . TYR B 1 209 ? 86.56600  111.88700 98.36500  1.000 56.66516  ? 216 TYR B N   1 
ATOM   3339 C CA  . TYR B 1 209 ? 87.42000  111.57900 97.21800  1.000 53.74068  ? 216 TYR B CA  1 
ATOM   3340 C C   . TYR B 1 209 ? 86.68700  110.85600 96.09300  1.000 53.76945  ? 216 TYR B C   1 
ATOM   3341 O O   . TYR B 1 209 ? 87.02400  111.06000 94.92400  1.000 60.83006  ? 216 TYR B O   1 
ATOM   3342 C CB  . TYR B 1 209 ? 88.62100  110.73600 97.64100  1.000 53.32314  ? 216 TYR B CB  1 
ATOM   3343 C CG  . TYR B 1 209 ? 89.54000  111.37400 98.64900  1.000 52.49231  ? 216 TYR B CG  1 
ATOM   3344 C CD1 . TYR B 1 209 ? 89.93600  112.69000 98.52200  1.000 51.02336  ? 216 TYR B CD1 1 
ATOM   3345 C CD2 . TYR B 1 209 ? 90.04200  110.64400 99.70700  1.000 53.67209  ? 216 TYR B CD2 1 
ATOM   3346 C CE1 . TYR B 1 209 ? 90.78100  113.26400 99.43600  1.000 48.71196  ? 216 TYR B CE1 1 
ATOM   3347 C CE2 . TYR B 1 209 ? 90.88800  111.20900 100.62200 1.000 52.63854  ? 216 TYR B CE2 1 
ATOM   3348 C CZ  . TYR B 1 209 ? 91.25300  112.51700 100.48300 1.000 50.22639  ? 216 TYR B CZ  1 
ATOM   3349 O OH  . TYR B 1 209 ? 92.10400  113.07500 101.40000 1.000 57.67747  ? 216 TYR B OH  1 
ATOM   3350 N N   . THR B 1 210 ? 85.71000  110.00500 96.40400  1.000 49.65751  ? 217 THR B N   1 
ATOM   3351 C CA  . THR B 1 210 ? 85.00500  109.27300 95.35300  1.000 49.14096  ? 217 THR B CA  1 
ATOM   3352 C C   . THR B 1 210 ? 84.36700  110.15300 94.28300  1.000 55.36843  ? 217 THR B C   1 
ATOM   3353 O O   . THR B 1 210 ? 84.62400  109.90900 93.09300  1.000 60.55212  ? 217 THR B O   1 
ATOM   3354 C CB  . THR B 1 210 ? 83.97400  108.33500 95.98200  1.000 56.48108  ? 217 THR B CB  1 
ATOM   3355 O OG1 . THR B 1 210 ? 84.64800  107.35300 96.77200  1.000 63.05185  ? 217 THR B OG1 1 
ATOM   3356 C CG2 . THR B 1 210 ? 83.16600  107.65000 94.90200  1.000 55.08679  ? 217 THR B CG2 1 
ATOM   3357 N N   . PRO B 1 211 ? 83.53800  111.15400 94.59800  1.000 54.73738  ? 218 PRO B N   1 
ATOM   3358 C CA  . PRO B 1 211 ? 82.99000  111.98200 93.51300  1.000 56.73988  ? 218 PRO B CA  1 
ATOM   3359 C C   . PRO B 1 211 ? 83.99000  112.94000 92.89100  1.000 56.28625  ? 218 PRO B C   1 
ATOM   3360 O O   . PRO B 1 211 ? 83.86400  113.24600 91.69900  1.000 55.62242  ? 218 PRO B O   1 
ATOM   3361 C CB  . PRO B 1 211 ? 81.84700  112.74400 94.19500  1.000 55.54519  ? 218 PRO B CB  1 
ATOM   3362 C CG  . PRO B 1 211 ? 82.23200  112.79500 95.60300  1.000 52.23627  ? 218 PRO B CG  1 
ATOM   3363 C CD  . PRO B 1 211 ? 82.92100  111.50200 95.88800  1.000 52.87450  ? 218 PRO B CD  1 
ATOM   3364 N N   . ILE B 1 212 ? 84.97100  113.42700 93.64300  1.000 57.44725  ? 219 ILE B N   1 
ATOM   3365 C CA  . ILE B 1 212 ? 85.84600  114.49000 93.15300  1.000 54.84294  ? 219 ILE B CA  1 
ATOM   3366 C C   . ILE B 1 212 ? 87.00400  113.93900 92.33300  1.000 55.73953  ? 219 ILE B C   1 
ATOM   3367 O O   . ILE B 1 212 ? 87.31100  114.45500 91.25600  1.000 57.79604  ? 219 ILE B O   1 
ATOM   3368 C CB  . ILE B 1 212 ? 86.35100  115.34200 94.33200  1.000 52.14894  ? 219 ILE B CB  1 
ATOM   3369 C CG1 . ILE B 1 212 ? 85.18200  116.04000 95.01500  1.000 57.51413  ? 219 ILE B CG1 1 
ATOM   3370 C CG2 . ILE B 1 212 ? 87.33900  116.36300 93.85000  1.000 56.41440  ? 219 ILE B CG2 1 
ATOM   3371 C CD1 . ILE B 1 212 ? 85.59400  116.89500 96.17700  1.000 58.66235  ? 219 ILE B CD1 1 
ATOM   3372 N N   . GLU B 1 213 ? 87.66600  112.89000 92.80900  1.000 57.93073  ? 220 GLU B N   1 
ATOM   3373 C CA  . GLU B 1 213 ? 88.80300  112.32200 92.09700  1.000 58.18571  ? 220 GLU B CA  1 
ATOM   3374 C C   . GLU B 1 213 ? 88.41000  111.27100 91.07000  1.000 63.64150  ? 220 GLU B C   1 
ATOM   3375 O O   . GLU B 1 213 ? 89.23600  110.91700 90.22500  1.000 68.00880  ? 220 GLU B O   1 
ATOM   3376 C CB  . GLU B 1 213 ? 89.78900  111.70100 93.08900  1.000 52.00579  ? 220 GLU B CB  1 
ATOM   3377 C CG  . GLU B 1 213 ? 90.33400  112.64200 94.14600  1.000 52.74947  ? 220 GLU B CG  1 
ATOM   3378 C CD  . GLU B 1 213 ? 91.29500  113.66900 93.59600  1.000 57.23342  ? 220 GLU B CD  1 
ATOM   3379 O OE1 . GLU B 1 213 ? 91.54100  113.68100 92.37600  1.000 54.92587  ? 220 GLU B OE1 1 
ATOM   3380 O OE2 . GLU B 1 213 ? 91.81600  114.46900 94.39400  1.000 63.42728  ? 220 GLU B OE2 1 
ATOM   3381 N N   . GLY B 1 214 ? 87.18300  110.76700 91.11900  1.000 63.31132  ? 221 GLY B N   1 
ATOM   3382 C CA  . GLY B 1 214 ? 86.75700  109.72500 90.21200  1.000 61.14358  ? 221 GLY B CA  1 
ATOM   3383 C C   . GLY B 1 214 ? 87.26700  108.34300 90.53900  1.000 64.38209  ? 221 GLY B C   1 
ATOM   3384 O O   . GLY B 1 214 ? 87.05300  107.41900 89.74800  1.000 68.66300  ? 221 GLY B O   1 
ATOM   3385 N N   . TRP B 1 215 ? 87.93500  108.16900 91.67500  1.000 52.19258  ? 222 TRP B N   1 
ATOM   3386 C CA  . TRP B 1 215 ? 88.30900  106.84200 92.13500  1.000 50.74482  ? 222 TRP B CA  1 
ATOM   3387 C C   . TRP B 1 215 ? 87.07400  106.01000 92.44900  1.000 53.32151  ? 222 TRP B C   1 
ATOM   3388 O O   . TRP B 1 215 ? 85.98600  106.53000 92.70200  1.000 54.93341  ? 222 TRP B O   1 
ATOM   3389 C CB  . TRP B 1 215 ? 89.16900  106.93100 93.38900  1.000 46.91792  ? 222 TRP B CB  1 
ATOM   3390 C CG  . TRP B 1 215 ? 90.43500  107.65700 93.21200  1.000 46.94829  ? 222 TRP B CG  1 
ATOM   3391 C CD1 . TRP B 1 215 ? 91.09600  107.87300 92.05000  1.000 50.72152  ? 222 TRP B CD1 1 
ATOM   3392 C CD2 . TRP B 1 215 ? 91.19600  108.29200 94.23500  1.000 44.84062  ? 222 TRP B CD2 1 
ATOM   3393 N NE1 . TRP B 1 215 ? 92.23700  108.59100 92.28600  1.000 54.23422  ? 222 TRP B NE1 1 
ATOM   3394 C CE2 . TRP B 1 215 ? 92.31800  108.86200 93.62400  1.000 46.30114  ? 222 TRP B CE2 1 
ATOM   3395 C CE3 . TRP B 1 215 ? 91.04000  108.42800 95.61200  1.000 51.34238  ? 222 TRP B CE3 1 
ATOM   3396 C CZ2 . TRP B 1 215 ? 93.27500  109.55800 94.33900  1.000 47.26612  ? 222 TRP B CZ2 1 
ATOM   3397 C CZ3 . TRP B 1 215 ? 91.98800  109.11500 96.31700  1.000 49.09268  ? 222 TRP B CZ3 1 
ATOM   3398 C CH2 . TRP B 1 215 ? 93.09100  109.67300 95.68400  1.000 48.37279  ? 222 TRP B CH2 1 
ATOM   3399 N N   . SER B 1 216 ? 87.25300  104.69600 92.43200  1.000 54.53038  ? 223 SER B N   1 
ATOM   3400 C CA  . SER B 1 216 ? 86.25200  103.83100 93.02400  1.000 52.77637  ? 223 SER B CA  1 
ATOM   3401 C C   . SER B 1 216 ? 86.28200  104.00100 94.53700  1.000 55.94451  ? 223 SER B C   1 
ATOM   3402 O O   . SER B 1 216 ? 87.26800  104.46200 95.11400  1.000 59.92761  ? 223 SER B O   1 
ATOM   3403 C CB  . SER B 1 216 ? 86.49300  102.37600 92.63400  1.000 58.40876  ? 223 SER B CB  1 
ATOM   3404 O OG  . SER B 1 216 ? 87.56200  101.82300 93.37200  1.000 64.99474  ? 223 SER B OG  1 
ATOM   3405 N N   . TYR B 1 217 ? 85.17400  103.64600 95.18300  1.000 59.51103  ? 224 TYR B N   1 
ATOM   3406 C CA  . TYR B 1 217 ? 85.08800  103.81200 96.62900  1.000 56.09465  ? 224 TYR B CA  1 
ATOM   3407 C C   . TYR B 1 217 ? 86.14200  102.98500 97.35700  1.000 58.18435  ? 224 TYR B C   1 
ATOM   3408 O O   . TYR B 1 217 ? 86.77700  103.46800 98.30200  1.000 65.04054  ? 224 TYR B O   1 
ATOM   3409 C CB  . TYR B 1 217 ? 83.68800  103.43900 97.10900  1.000 55.88927  ? 224 TYR B CB  1 
ATOM   3410 C CG  . TYR B 1 217 ? 83.38900  103.87100 98.52000  1.000 56.29645  ? 224 TYR B CG  1 
ATOM   3411 C CD1 . TYR B 1 217 ? 82.85800  105.12100 98.77900  1.000 60.35948  ? 224 TYR B CD1 1 
ATOM   3412 C CD2 . TYR B 1 217 ? 83.62800  103.02900 99.59200  1.000 60.27195  ? 224 TYR B CD2 1 
ATOM   3413 C CE1 . TYR B 1 217 ? 82.58500  105.52600 100.06400 1.000 58.84224  ? 224 TYR B CE1 1 
ATOM   3414 C CE2 . TYR B 1 217 ? 83.35200  103.42400 100.88100 1.000 62.38080  ? 224 TYR B CE2 1 
ATOM   3415 C CZ  . TYR B 1 217 ? 82.83200  104.67400 101.11000 1.000 60.66079  ? 224 TYR B CZ  1 
ATOM   3416 O OH  . TYR B 1 217 ? 82.54600  105.07500 102.39000 1.000 65.35440  ? 224 TYR B OH  1 
ATOM   3417 N N   . PHE B 1 218 ? 86.35300  101.74200 96.92600  1.000 58.16224  ? 225 PHE B N   1 
ATOM   3418 C CA  . PHE B 1 218 ? 87.36200  100.90200 97.56200  1.000 55.41811  ? 225 PHE B CA  1 
ATOM   3419 C C   . PHE B 1 218 ? 88.78300  101.39900 97.32200  1.000 57.38323  ? 225 PHE B C   1 
ATOM   3420 O O   . PHE B 1 218 ? 89.63400  101.30000 98.21300  1.000 66.43938  ? 225 PHE B O   1 
ATOM   3421 C CB  . PHE B 1 218 ? 87.22700  99.46500  97.07900  1.000 59.93092  ? 225 PHE B CB  1 
ATOM   3422 C CG  . PHE B 1 218 ? 88.21000  98.53800  97.70700  1.000 61.96699  ? 225 PHE B CG  1 
ATOM   3423 C CD1 . PHE B 1 218 ? 88.30800  98.44600  99.08000  1.000 61.56439  ? 225 PHE B CD1 1 
ATOM   3424 C CD2 . PHE B 1 218 ? 89.04500  97.76800  96.92700  1.000 56.86258  ? 225 PHE B CD2 1 
ATOM   3425 C CE1 . PHE B 1 218 ? 89.21700  97.60500  99.66200  1.000 58.00640  ? 225 PHE B CE1 1 
ATOM   3426 C CE2 . PHE B 1 218 ? 89.95300  96.92200  97.50500  1.000 58.32691  ? 225 PHE B CE2 1 
ATOM   3427 C CZ  . PHE B 1 218 ? 90.04000  96.84200  98.87400  1.000 62.58267  ? 225 PHE B CZ  1 
ATOM   3428 N N   . ASP B 1 219 ? 89.06800  101.93400 96.13600  1.000 49.24112  ? 226 ASP B N   1 
ATOM   3429 C CA  . ASP B 1 219 ? 90.36700  102.56400 95.92100  1.000 44.15263  ? 226 ASP B CA  1 
ATOM   3430 C C   . ASP B 1 219 ? 90.57200  103.75900 96.83700  1.000 49.26966  ? 226 ASP B C   1 
ATOM   3431 O O   . ASP B 1 219 ? 91.68600  103.99800 97.31100  1.000 57.71851  ? 226 ASP B O   1 
ATOM   3432 C CB  . ASP B 1 219 ? 90.52500  102.97600 94.46000  1.000 49.00910  ? 226 ASP B CB  1 
ATOM   3433 C CG  . ASP B 1 219 ? 90.61400  101.78900 93.52700  1.000 58.90906  ? 226 ASP B CG  1 
ATOM   3434 O OD1 . ASP B 1 219 ? 91.36500  100.84400 93.83900  1.000 65.17326  ? 226 ASP B OD1 1 
ATOM   3435 O OD2 . ASP B 1 219 ? 89.93900  101.80100 92.47800  1.000 55.09016  ? 226 ASP B OD2 1 
ATOM   3436 N N   . SER B 1 220 ? 89.51400  104.51800 97.11200  1.000 46.29771  ? 227 SER B N   1 
ATOM   3437 C CA  . SER B 1 220 ? 89.64700  105.63800 98.03600  1.000 46.59656  ? 227 SER B CA  1 
ATOM   3438 C C   . SER B 1 220 ? 89.80600  105.19800 99.48800  1.000 48.59323  ? 227 SER B C   1 
ATOM   3439 O O   . SER B 1 220 ? 90.55400  105.83200 100.23400 1.000 53.58895  ? 227 SER B O   1 
ATOM   3440 C CB  . SER B 1 220 ? 88.45000  106.56600 97.89300  1.000 52.11253  ? 227 SER B CB  1 
ATOM   3441 O OG  . SER B 1 220 ? 87.32700  106.02500 98.55000  1.000 60.63771  ? 227 SER B OG  1 
ATOM   3442 N N   . LEU B 1 221 ? 89.16000  104.10700 99.90700  1.000 46.58761  ? 228 LEU B N   1 
ATOM   3443 C CA  . LEU B 1 221 ? 89.45300  103.53800 101.22600 1.000 39.44453  ? 228 LEU B CA  1 
ATOM   3444 C C   . LEU B 1 221 ? 90.89000  103.04400 101.33700 1.000 44.00647  ? 228 LEU B C   1 
ATOM   3445 O O   . LEU B 1 221 ? 91.55200  103.25500 102.36300 1.000 50.44345  ? 228 LEU B O   1 
ATOM   3446 C CB  . LEU B 1 221 ? 88.49200  102.39600 101.54500 1.000 40.28994  ? 228 LEU B CB  1 
ATOM   3447 C CG  . LEU B 1 221 ? 87.07200  102.71700 101.99200 1.000 45.10760  ? 228 LEU B CG  1 
ATOM   3448 C CD1 . LEU B 1 221 ? 86.23800  101.45900 102.00000 1.000 49.90585  ? 228 LEU B CD1 1 
ATOM   3449 C CD2 . LEU B 1 221 ? 87.10900  103.30600 103.37200 1.000 49.58211  ? 228 LEU B CD2 1 
ATOM   3450 N N   . TYR B 1 222 ? 91.38400  102.36100 100.30700 1.000 43.84575  ? 229 TYR B N   1 
ATOM   3451 C CA  . TYR B 1 222 ? 92.77300  101.91800 100.30900 1.000 45.02771  ? 229 TYR B CA  1 
ATOM   3452 C C   . TYR B 1 222 ? 93.74700  103.09200 100.34100 1.000 45.10248  ? 229 TYR B C   1 
ATOM   3453 O O   . TYR B 1 222 ? 94.74500  103.05200 101.06900 1.000 43.70531  ? 229 TYR B O   1 
ATOM   3454 C CB  . TYR B 1 222 ? 93.02000  101.02300 99.09700  1.000 46.78877  ? 229 TYR B CB  1 
ATOM   3455 C CG  . TYR B 1 222 ? 94.46100  100.85100 98.69200  1.000 47.30948  ? 229 TYR B CG  1 
ATOM   3456 C CD1 . TYR B 1 222 ? 95.25100  99.88100  99.28100  1.000 43.10595  ? 229 TYR B CD1 1 
ATOM   3457 C CD2 . TYR B 1 222 ? 95.01700  101.62300 97.68800  1.000 48.61853  ? 229 TYR B CD2 1 
ATOM   3458 C CE1 . TYR B 1 222 ? 96.55800  99.71100  98.90900  1.000 41.38391  ? 229 TYR B CE1 1 
ATOM   3459 C CE2 . TYR B 1 222 ? 96.32500  101.45500 97.30500  1.000 48.22523  ? 229 TYR B CE2 1 
ATOM   3460 C CZ  . TYR B 1 222 ? 97.09000  100.49900 97.92000  1.000 50.09387  ? 229 TYR B CZ  1 
ATOM   3461 O OH  . TYR B 1 222 ? 98.39500  100.32600 97.53300  1.000 51.20757  ? 229 TYR B OH  1 
ATOM   3462 N N   . PHE B 1 223 ? 93.48100  104.14600 99.56600  1.000 43.24701  ? 230 PHE B N   1 
ATOM   3463 C CA  . PHE B 1 223 ? 94.26400  105.37200 99.69600  1.000 36.18913  ? 230 PHE B CA  1 
ATOM   3464 C C   . PHE B 1 223 ? 94.20800  105.95700 101.09500 1.000 37.58058  ? 230 PHE B C   1 
ATOM   3465 O O   . PHE B 1 223 ? 95.22200  106.43200 101.61100 1.000 40.41480  ? 230 PHE B O   1 
ATOM   3466 C CB  . PHE B 1 223 ? 93.80800  106.43500 98.70600  1.000 33.52209  ? 230 PHE B CB  1 
ATOM   3467 C CG  . PHE B 1 223 ? 94.43000  107.77400 98.96500  1.000 38.56793  ? 230 PHE B CG  1 
ATOM   3468 C CD1 . PHE B 1 223 ? 95.76400  107.99600 98.71700  1.000 45.39530  ? 230 PHE B CD1 1 
ATOM   3469 C CD2 . PHE B 1 223 ? 93.68200  108.80400 99.49100  1.000 39.96455  ? 230 PHE B CD2 1 
ATOM   3470 C CE1 . PHE B 1 223 ? 96.33100  109.22200 98.97600  1.000 40.13092  ? 230 PHE B CE1 1 
ATOM   3471 C CE2 . PHE B 1 223 ? 94.24900  110.02800 99.74700  1.000 39.42668  ? 230 PHE B CE2 1 
ATOM   3472 C CZ  . PHE B 1 223 ? 95.57100  110.23500 99.48900  1.000 38.30512  ? 230 PHE B CZ  1 
ATOM   3473 N N   . CYS B 1 224 ? 93.02900  105.97800 101.71200 1.000 42.48147  ? 231 CYS B N   1 
ATOM   3474 C CA  . CYS B 1 224 ? 92.93200  106.50500 103.06700 1.000 37.57629  ? 231 CYS B CA  1 
ATOM   3475 C C   . CYS B 1 224 ? 93.81100  105.72600 104.03300 1.000 40.69907  ? 231 CYS B C   1 
ATOM   3476 O O   . CYS B 1 224 ? 94.53300  106.32200 104.83400 1.000 54.28142  ? 231 CYS B O   1 
ATOM   3477 C CB  . CYS B 1 224 ? 91.48000  106.51900 103.53500 1.000 35.58834  ? 231 CYS B CB  1 
ATOM   3478 S SG  . CYS B 1 224 ? 90.44600  107.69700 102.65700 1.000 49.14950  ? 231 CYS B SG  1 
ATOM   3479 N N   . PHE B 1 225 ? 93.77200  104.39700 103.98200 1.000 28.56132  ? 232 PHE B N   1 
ATOM   3480 C CA  . PHE B 1 225 ? 94.66300  103.63700 104.85700 1.000 29.07923  ? 232 PHE B CA  1 
ATOM   3481 C C   . PHE B 1 225 ? 96.13300  103.88800 104.54100 1.000 32.86172  ? 232 PHE B C   1 
ATOM   3482 O O   . PHE B 1 225 ? 96.94500  104.08500 105.44900 1.000 34.04589  ? 232 PHE B O   1 
ATOM   3483 C CB  . PHE B 1 225 ? 94.38300  102.14500 104.79200 1.000 32.63531  ? 232 PHE B CB  1 
ATOM   3484 C CG  . PHE B 1 225 ? 95.32900  101.34100 105.63200 1.000 33.29112  ? 232 PHE B CG  1 
ATOM   3485 C CD1 . PHE B 1 225 ? 95.19100  101.30700 107.00600 1.000 37.67507  ? 232 PHE B CD1 1 
ATOM   3486 C CD2 . PHE B 1 225 ? 96.37700  100.65200 105.05800 1.000 35.87117  ? 232 PHE B CD2 1 
ATOM   3487 C CE1 . PHE B 1 225 ? 96.06300  100.58700 107.78400 1.000 30.97478  ? 232 PHE B CE1 1 
ATOM   3488 C CE2 . PHE B 1 225 ? 97.25100  99.93100  105.83600 1.000 37.11162  ? 232 PHE B CE2 1 
ATOM   3489 C CZ  . PHE B 1 225 ? 97.09200  99.90000  107.19900 1.000 35.33912  ? 232 PHE B CZ  1 
ATOM   3490 N N   . VAL B 1 226 ? 96.50400  103.85700 103.26100 1.000 40.64678  ? 233 VAL B N   1 
ATOM   3491 C CA  . VAL B 1 226 ? 97.90500  104.03000 102.87400 1.000 28.29495  ? 233 VAL B CA  1 
ATOM   3492 C C   . VAL B 1 226 ? 98.44400  105.40300 103.25700 1.000 27.53885  ? 233 VAL B C   1 
ATOM   3493 O O   . VAL B 1 226 ? 99.62000  105.53700 103.60700 1.000 36.22154  ? 233 VAL B O   1 
ATOM   3494 C CB  . VAL B 1 226 ? 98.05800  103.75100 101.36800 1.000 30.87767  ? 233 VAL B CB  1 
ATOM   3495 C CG1 . VAL B 1 226 ? 99.36700  104.25700 100.86000 1.000 30.12582  ? 233 VAL B CG1 1 
ATOM   3496 C CG2 . VAL B 1 226 ? 97.96700  102.27300 101.11700 1.000 31.36195  ? 233 VAL B CG2 1 
ATOM   3497 N N   . ALA B 1 227 ? 97.60900  106.43600 103.21900 1.000 29.97538  ? 234 ALA B N   1 
ATOM   3498 C CA  . ALA B 1 227 ? 98.02600  107.74900 103.69600 1.000 22.84788  ? 234 ALA B CA  1 
ATOM   3499 C C   . ALA B 1 227 ? 98.05500  107.83100 105.21700 1.000 38.19803  ? 234 ALA B C   1 
ATOM   3500 O O   . ALA B 1 227 ? 99.03300  108.31300 105.79500 1.000 45.28404  ? 234 ALA B O   1 
ATOM   3501 C CB  . ALA B 1 227 ? 97.10700  108.82600 103.13100 1.000 25.63239  ? 234 ALA B CB  1 
ATOM   3502 N N   . PHE B 1 228 ? 96.98500  107.40100 105.88400 1.000 37.14546  ? 235 PHE B N   1 
ATOM   3503 C CA  . PHE B 1 228 ? 96.88600  107.56900 107.32900 1.000 20.46933  ? 235 PHE B CA  1 
ATOM   3504 C C   . PHE B 1 228 ? 97.88900  106.71300 108.09200 1.000 28.83628  ? 235 PHE B C   1 
ATOM   3505 O O   . PHE B 1 228 ? 98.34900  107.11800 109.16100 1.000 47.49365  ? 235 PHE B O   1 
ATOM   3506 C CB  . PHE B 1 228 ? 95.47400  107.22600 107.80000 1.000 28.92775  ? 235 PHE B CB  1 
ATOM   3507 C CG  . PHE B 1 228 ? 94.39700  108.12200 107.25100 1.000 27.96172  ? 235 PHE B CG  1 
ATOM   3508 C CD1 . PHE B 1 228 ? 94.69200  109.17600 106.41300 1.000 31.15238  ? 235 PHE B CD1 1 
ATOM   3509 C CD2 . PHE B 1 228 ? 93.07800  107.88500 107.56500 1.000 31.11865  ? 235 PHE B CD2 1 
ATOM   3510 C CE1 . PHE B 1 228 ? 93.69700  109.97600 105.91400 1.000 36.11368  ? 235 PHE B CE1 1 
ATOM   3511 C CE2 . PHE B 1 228 ? 92.08400  108.68600 107.06900 1.000 35.14993  ? 235 PHE B CE2 1 
ATOM   3512 C CZ  . PHE B 1 228 ? 92.39400  109.73100 106.24200 1.000 32.58035  ? 235 PHE B CZ  1 
ATOM   3513 N N   . SER B 1 229 ? 98.24500  105.54100 107.57800 1.000 27.08135  ? 236 SER B N   1 
ATOM   3514 C CA  . SER B 1 229 ? 99.30800  104.76000 108.20000 1.000 27.56968  ? 236 SER B CA  1 
ATOM   3515 C C   . SER B 1 229 ? 100.69200 105.33600 107.96800 1.000 39.23904  ? 236 SER B C   1 
ATOM   3516 O O   . SER B 1 229 ? 101.65900 104.78500 108.49700 1.000 45.73579  ? 236 SER B O   1 
ATOM   3517 C CB  . SER B 1 229 ? 99.26000  103.32100 107.70600 1.000 24.60144  ? 236 SER B CB  1 
ATOM   3518 O OG  . SER B 1 229 ? 99.42500  103.27700 106.30900 1.000 40.58053  ? 236 SER B OG  1 
ATOM   3519 N N   . THR B 1 230 ? 100.81100 106.40800 107.19100 1.000 33.29836  ? 237 THR B N   1 
ATOM   3520 C CA  . THR B 1 230 ? 102.06600 106.98700 106.72200 1.000 18.80508  ? 237 THR B CA  1 
ATOM   3521 C C   . THR B 1 230 ? 102.88600 106.04800 105.84800 1.000 21.55036  ? 237 THR B C   1 
ATOM   3522 O O   . THR B 1 230 ? 104.07000 106.31200 105.62200 1.000 38.38487  ? 237 THR B O   1 
ATOM   3523 C CB  . THR B 1 230 ? 102.93900 107.48200 107.87900 1.000 28.14072  ? 237 THR B CB  1 
ATOM   3524 O OG1 . THR B 1 230 ? 103.52400 106.36000 108.54200 1.000 37.38591  ? 237 THR B OG1 1 
ATOM   3525 C CG2 . THR B 1 230 ? 102.12200 108.27900 108.86900 1.000 25.13189  ? 237 THR B CG2 1 
ATOM   3526 N N   . ILE B 1 231 ? 102.31700 104.94200 105.36600 1.000 20.89266  ? 238 ILE B N   1 
ATOM   3527 C CA  . ILE B 1 231 ? 103.04400 104.12400 104.39800 1.000 18.96622  ? 238 ILE B CA  1 
ATOM   3528 C C   . ILE B 1 231 ? 103.26300 104.91400 103.11600 1.000 21.50636  ? 238 ILE B C   1 
ATOM   3529 O O   . ILE B 1 231 ? 104.39900 105.14400 102.69200 1.000 40.57352  ? 238 ILE B O   1 
ATOM   3530 C CB  . ILE B 1 231 ? 102.30800 102.80400 104.12400 1.000 18.59243  ? 238 ILE B CB  1 
ATOM   3531 C CG1 . ILE B 1 231 ? 102.20600 101.96500 105.38800 1.000 28.77250  ? 238 ILE B CG1 1 
ATOM   3532 C CG2 . ILE B 1 231 ? 103.05200 102.01500 103.10700 1.000 20.70747  ? 238 ILE B CG2 1 
ATOM   3533 C CD1 . ILE B 1 231 ? 101.19400 100.86600 105.28600 1.000 27.67108  ? 238 ILE B CD1 1 
ATOM   3534 N N   . GLY B 1 232 ? 102.17900 105.37500 102.50400 1.000 14.25593  ? 239 GLY B N   1 
ATOM   3535 C CA  . GLY B 1 232 ? 102.27400 106.29900 101.39400 1.000 14.17802  ? 239 GLY B CA  1 
ATOM   3536 C C   . GLY B 1 232 ? 103.02600 105.82100 100.17100 1.000 25.00654  ? 239 GLY B C   1 
ATOM   3537 O O   . GLY B 1 232 ? 104.09600 106.35100 99.87100  1.000 39.07493  ? 239 GLY B O   1 
ATOM   3538 N N   . PHE B 1 233 ? 102.51800 104.80300 99.47400  1.000 19.16508  ? 240 PHE B N   1 
ATOM   3539 C CA  . PHE B 1 233 ? 103.20200 104.34700 98.26800  1.000 22.38865  ? 240 PHE B CA  1 
ATOM   3540 C C   . PHE B 1 233 ? 103.24600 105.44000 97.21200  1.000 40.86075  ? 240 PHE B C   1 
ATOM   3541 O O   . PHE B 1 233 ? 104.28000 105.65300 96.57000  1.000 47.79482  ? 240 PHE B O   1 
ATOM   3542 C CB  . PHE B 1 233 ? 102.53000 103.10400 97.69100  1.000 20.33996  ? 240 PHE B CB  1 
ATOM   3543 C CG  . PHE B 1 233 ? 102.44800 101.95300 98.63500  1.000 24.75392  ? 240 PHE B CG  1 
ATOM   3544 C CD1 . PHE B 1 233 ? 103.58000 101.46700 99.24700  1.000 30.53892  ? 240 PHE B CD1 1 
ATOM   3545 C CD2 . PHE B 1 233 ? 101.24800 101.32900 98.87600  1.000 32.04550  ? 240 PHE B CD2 1 
ATOM   3546 C CE1 . PHE B 1 233 ? 103.50900 100.39900 100.09600 1.000 34.77843  ? 240 PHE B CE1 1 
ATOM   3547 C CE2 . PHE B 1 233 ? 101.17500 100.26300 99.72700  1.000 32.84106  ? 240 PHE B CE2 1 
ATOM   3548 C CZ  . PHE B 1 233 ? 102.30500 99.79900  100.33800 1.000 32.68604  ? 240 PHE B CZ  1 
ATOM   3549 N N   . GLY B 1 234 ? 102.14500 106.15500 97.03000  1.000 46.35243  ? 241 GLY B N   1 
ATOM   3550 C CA  . GLY B 1 234 ? 102.06300 107.16300 95.99600  1.000 39.33651  ? 241 GLY B CA  1 
ATOM   3551 C C   . GLY B 1 234 ? 101.57600 106.66700 94.65900  1.000 40.86997  ? 241 GLY B C   1 
ATOM   3552 O O   . GLY B 1 234 ? 101.76200 107.36100 93.65400  1.000 51.89454  ? 241 GLY B O   1 
ATOM   3553 N N   . ASP B 1 235 ? 100.96200 105.48500 94.61100  1.000 44.13661  ? 242 ASP B N   1 
ATOM   3554 C CA  . ASP B 1 235 ? 100.23200 105.06400 93.42000  1.000 51.58701  ? 242 ASP B CA  1 
ATOM   3555 C C   . ASP B 1 235 ? 98.96500  105.88900 93.23500  1.000 54.82458  ? 242 ASP B C   1 
ATOM   3556 O O   . ASP B 1 235 ? 98.64800  106.31800 92.12100  1.000 60.68109  ? 242 ASP B O   1 
ATOM   3557 C CB  . ASP B 1 235 ? 99.91400  103.57100 93.49300  1.000 48.88213  ? 242 ASP B CB  1 
ATOM   3558 C CG  . ASP B 1 235 ? 99.21100  103.18400 94.77200  1.000 55.48261  ? 242 ASP B CG  1 
ATOM   3559 O OD1 . ASP B 1 235 ? 99.13100  104.02700 95.68500  1.000 57.64750  ? 242 ASP B OD1 1 
ATOM   3560 O OD2 . ASP B 1 235 ? 98.74200  102.03200 94.86700  1.000 55.28431  ? 242 ASP B OD2 1 
ATOM   3561 N N   . LEU B 1 236 ? 98.22600  106.11400 94.31700  1.000 48.21517  ? 243 LEU B N   1 
ATOM   3562 C CA  . LEU B 1 236 ? 97.13800  107.08100 94.35900  1.000 49.02097  ? 243 LEU B CA  1 
ATOM   3563 C C   . LEU B 1 236 ? 97.56900  108.26900 95.20500  1.000 45.94660  ? 243 LEU B C   1 
ATOM   3564 O O   . LEU B 1 236 ? 98.08100  108.08900 96.31300  1.000 46.40145  ? 243 LEU B O   1 
ATOM   3565 C CB  . LEU B 1 236 ? 95.88200  106.44900 94.96000  1.000 43.63915  ? 243 LEU B CB  1 
ATOM   3566 C CG  . LEU B 1 236 ? 95.35000  105.15700 94.34700  1.000 42.80080  ? 243 LEU B CG  1 
ATOM   3567 C CD1 . LEU B 1 236 ? 94.14100  104.68300 95.11100  1.000 41.03623  ? 243 LEU B CD1 1 
ATOM   3568 C CD2 . LEU B 1 236 ? 95.00400  105.36000 92.89400  1.000 44.57935  ? 243 LEU B CD2 1 
ATOM   3569 N N   . VAL B 1 237 ? 97.35300  109.47700 94.69000  1.000 42.47268  ? 244 VAL B N   1 
ATOM   3570 C CA  . VAL B 1 237 ? 97.54300  110.70200 95.46000  1.000 37.81235  ? 244 VAL B CA  1 
ATOM   3571 C C   . VAL B 1 237 ? 96.36700  111.62800 95.19200  1.000 42.62535  ? 244 VAL B C   1 
ATOM   3572 O O   . VAL B 1 237 ? 96.01300  111.87000 94.03400  1.000 45.28716  ? 244 VAL B O   1 
ATOM   3573 C CB  . VAL B 1 237 ? 98.86200  111.41200 95.10200  1.000 41.28765  ? 244 VAL B CB  1 
ATOM   3574 C CG1 . VAL B 1 237 ? 99.04700  112.63300 95.96300  1.000 34.85514  ? 244 VAL B CG1 1 
ATOM   3575 C CG2 . VAL B 1 237 ? 100.03500 110.48100 95.26500  1.000 47.90582  ? 244 VAL B CG2 1 
ATOM   3576 N N   . SER B 1 238 ? 95.75200  112.12800 96.25800  1.000 39.97516  ? 245 SER B N   1 
ATOM   3577 C CA  . SER B 1 238 ? 94.66700  113.08700 96.15000  1.000 36.34448  ? 245 SER B CA  1 
ATOM   3578 C C   . SER B 1 238 ? 95.19500  114.49000 95.89200  1.000 43.13973  ? 245 SER B C   1 
ATOM   3579 O O   . SER B 1 238 ? 96.35000  114.80800 96.17700  1.000 51.44859  ? 245 SER B O   1 
ATOM   3580 C CB  . SER B 1 238 ? 93.84100  113.10500 97.42600  1.000 48.07841  ? 245 SER B CB  1 
ATOM   3581 O OG  . SER B 1 238 ? 94.63500  113.54200 98.51100  1.000 50.66918  ? 245 SER B OG  1 
ATOM   3582 N N   . SER B 1 239 ? 94.31300  115.34100 95.36500  1.000 58.26803  ? 246 SER B N   1 
ATOM   3583 C CA  . SER B 1 239 ? 94.59000  116.76000 95.13800  1.000 57.25627  ? 246 SER B CA  1 
ATOM   3584 C C   . SER B 1 239 ? 95.77600  116.94600 94.18900  1.000 59.65395  ? 246 SER B C   1 
ATOM   3585 O O   . SER B 1 239 ? 96.84600  117.42500 94.55800  1.000 63.25886  ? 246 SER B O   1 
ATOM   3586 C CB  . SER B 1 239 ? 94.82200  117.49200 96.46200  1.000 52.92531  ? 246 SER B CB  1 
ATOM   3587 O OG  . SER B 1 239 ? 95.06300  118.86700 96.23900  1.000 55.37826  ? 246 SER B OG  1 
ATOM   3588 N N   . GLN B 1 240 ? 95.54900  116.54500 92.94600  1.000 54.39908  ? 247 GLN B N   1 
ATOM   3589 C CA  . GLN B 1 240 ? 96.60400  116.52600 91.94000  1.000 50.33441  ? 247 GLN B CA  1 
ATOM   3590 C C   . GLN B 1 240 ? 96.17400  117.06000 90.58400  1.000 58.21803  ? 247 GLN B C   1 
ATOM   3591 O O   . GLN B 1 240 ? 97.02000  117.61300 89.87600  1.000 64.21638  ? 247 GLN B O   1 
ATOM   3592 C CB  . GLN B 1 240 ? 97.16400  115.11700 91.76300  1.000 53.95203  ? 247 GLN B CB  1 
ATOM   3593 C CG  . GLN B 1 240 ? 97.91800  114.62400 92.97100  1.000 58.41807  ? 247 GLN B CG  1 
ATOM   3594 C CD  . GLN B 1 240 ? 99.21600  115.35900 93.18200  1.000 51.25249  ? 247 GLN B CD  1 
ATOM   3595 O OE1 . GLN B 1 240 ? 100.22300 115.04900 92.55500  1.000 57.47668  ? 247 GLN B OE1 1 
ATOM   3596 N NE2 . GLN B 1 240 ? 99.20300  116.33700 94.07300  1.000 49.59598  ? 247 GLN B NE2 1 
ATOM   3597 N N   . ASN B 1 241 ? 94.91200  116.91700 90.19000  1.000 67.00799  ? 248 ASN B N   1 
ATOM   3598 C CA  . ASN B 1 241 ? 94.47600  117.41500 88.89700  1.000 63.95249  ? 248 ASN B CA  1 
ATOM   3599 C C   . ASN B 1 241 ? 94.68600  118.92000 88.81600  1.000 65.16855  ? 248 ASN B C   1 
ATOM   3600 O O   . ASN B 1 241 ? 94.71500  119.62300 89.82800  1.000 69.30772  ? 248 ASN B O   1 
ATOM   3601 C CB  . ASN B 1 241 ? 93.00700  117.07700 88.66100  1.000 63.92661  ? 248 ASN B CB  1 
ATOM   3602 C CG  . ASN B 1 241 ? 92.76600  115.59300 88.53900  1.000 70.08624  ? 248 ASN B CG  1 
ATOM   3603 O OD1 . ASN B 1 241 ? 93.70200  114.81300 88.38400  1.000 72.70107  ? 248 ASN B OD1 1 
ATOM   3604 N ND2 . ASN B 1 241 ? 91.50400  115.19100 88.60600  1.000 69.68864  ? 248 ASN B ND2 1 
ATOM   3605 N N   . ALA B 1 242 ? 94.84900  119.41100 87.59000  1.000 68.24384  ? 249 ALA B N   1 
ATOM   3606 C CA  . ALA B 1 242 ? 95.09100  120.83000 87.37800  1.000 71.35698  ? 249 ALA B CA  1 
ATOM   3607 C C   . ALA B 1 242 ? 93.93300  121.71300 87.81600  1.000 75.64448  ? 249 ALA B C   1 
ATOM   3608 O O   . ALA B 1 242 ? 94.15500  122.89300 88.10300  1.000 77.64483  ? 249 ALA B O   1 
ATOM   3609 C CB  . ALA B 1 242 ? 95.40300  121.09000 85.90600  1.000 75.29753  ? 249 ALA B CB  1 
ATOM   3610 N N   . HIS B 1 243 ? 92.71100  121.19000 87.88600  1.000 81.16429  ? 250 HIS B N   1 
ATOM   3611 C CA  . HIS B 1 243 ? 91.60300  122.03300 88.30700  1.000 77.31267  ? 250 HIS B CA  1 
ATOM   3612 C C   . HIS B 1 243 ? 90.55600  121.21900 89.05400  1.000 77.76614  ? 250 HIS B C   1 
ATOM   3613 O O   . HIS B 1 243 ? 90.30700  120.05400 88.73700  1.000 79.66088  ? 250 HIS B O   1 
ATOM   3614 C CB  . HIS B 1 243 ? 90.98200  122.72900 87.08900  1.000 74.06477  ? 250 HIS B CB  1 
ATOM   3615 C CG  . HIS B 1 243 ? 89.91300  123.71900 87.42900  1.000 78.70586  ? 250 HIS B CG  1 
ATOM   3616 N ND1 . HIS B 1 243 ? 88.60700  123.35200 87.66700  1.000 82.55822  ? 250 HIS B ND1 1 
ATOM   3617 C CD2 . HIS B 1 243 ? 89.95700  125.06500 87.56300  1.000 82.78487  ? 250 HIS B CD2 1 
ATOM   3618 C CE1 . HIS B 1 243 ? 87.89200  124.42900 87.93700  1.000 80.84354  ? 250 HIS B CE1 1 
ATOM   3619 N NE2 . HIS B 1 243 ? 88.68700  125.48200 87.88100  1.000 83.36976  ? 250 HIS B NE2 1 
ATOM   3620 N N   . TYR B 1 244 ? 89.93300  121.86200 90.04100  1.000 69.13019  ? 251 TYR B N   1 
ATOM   3621 C CA  . TYR B 1 244 ? 88.77200  121.33100 90.73800  1.000 69.43309  ? 251 TYR B CA  1 
ATOM   3622 C C   . TYR B 1 244 ? 87.78900  122.46500 90.98400  1.000 74.86493  ? 251 TYR B C   1 
ATOM   3623 O O   . TYR B 1 244 ? 88.15100  123.64300 90.96500  1.000 75.52272  ? 251 TYR B O   1 
ATOM   3624 C CB  . TYR B 1 244 ? 89.11100  120.69800 92.09600  1.000 68.61146  ? 251 TYR B CB  1 
ATOM   3625 C CG  . TYR B 1 244 ? 90.04400  119.52100 92.06600  1.000 69.13975  ? 251 TYR B CG  1 
ATOM   3626 C CD1 . TYR B 1 244 ? 89.57700  118.26000 91.74600  1.000 72.28891  ? 251 TYR B CD1 1 
ATOM   3627 C CD2 . TYR B 1 244 ? 91.37300  119.65500 92.41700  1.000 67.59526  ? 251 TYR B CD2 1 
ATOM   3628 C CE1 . TYR B 1 244 ? 90.41000  117.17500 91.74700  1.000 68.32548  ? 251 TYR B CE1 1 
ATOM   3629 C CE2 . TYR B 1 244 ? 92.21700  118.57500 92.41100  1.000 69.42792  ? 251 TYR B CE2 1 
ATOM   3630 C CZ  . TYR B 1 244 ? 91.72800  117.33600 92.07700  1.000 69.15815  ? 251 TYR B CZ  1 
ATOM   3631 O OH  . TYR B 1 244 ? 92.56300  116.24800 92.05100  1.000 70.76392  ? 251 TYR B OH  1 
ATOM   3632 N N   . GLU B 1 245 ? 86.53100  122.09700 91.19900  1.000 83.36191  ? 252 GLU B N   1 
ATOM   3633 C CA  . GLU B 1 245 ? 85.57000  123.04200 91.74700  1.000 82.24468  ? 252 GLU B CA  1 
ATOM   3634 C C   . GLU B 1 245 ? 85.92800  123.37300 93.19200  1.000 83.24147  ? 252 GLU B C   1 
ATOM   3635 O O   . GLU B 1 245 ? 86.20000  122.47400 93.99300  1.000 83.08459  ? 252 GLU B O   1 
ATOM   3636 C CB  . GLU B 1 245 ? 84.15700  122.46800 91.66300  1.000 80.33040  ? 252 GLU B CB  1 
ATOM   3637 N N   . SER B 1 246 ? 85.91800  124.66600 93.52500  1.000 79.97381  ? 253 SER B N   1 
ATOM   3638 C CA  . SER B 1 246 ? 86.20000  125.14100 94.88200  1.000 79.37947  ? 253 SER B CA  1 
ATOM   3639 C C   . SER B 1 246 ? 87.55400  124.65200 95.39700  1.000 79.01585  ? 253 SER B C   1 
ATOM   3640 O O   . SER B 1 246 ? 87.64900  124.05100 96.46800  1.000 80.08520  ? 253 SER B O   1 
ATOM   3641 C CB  . SER B 1 246 ? 85.07800  124.73800 95.83900  1.000 79.44684  ? 253 SER B CB  1 
ATOM   3642 O OG  . SER B 1 246 ? 83.82700  125.22400 95.39100  1.000 81.47791  ? 253 SER B OG  1 
ATOM   3643 N N   . GLN B 1 247 ? 88.60700  124.89900 94.61000  1.000 77.46795  ? 254 GLN B N   1 
ATOM   3644 C CA  . GLN B 1 247 ? 89.92700  124.34000 94.90200  1.000 73.78556  ? 254 GLN B CA  1 
ATOM   3645 C C   . GLN B 1 247 ? 90.35200  124.58600 96.34300  1.000 74.35543  ? 254 GLN B C   1 
ATOM   3646 O O   . GLN B 1 247 ? 90.88600  123.69100 97.00300  1.000 74.79699  ? 254 GLN B O   1 
ATOM   3647 C CB  . GLN B 1 247 ? 90.97300  124.92500 93.95500  1.000 71.12790  ? 254 GLN B CB  1 
ATOM   3648 C CG  . GLN B 1 247 ? 90.81600  124.52900 92.51200  1.000 76.01643  ? 254 GLN B CG  1 
ATOM   3649 C CD  . GLN B 1 247 ? 92.12800  124.57500 91.76300  1.000 79.05016  ? 254 GLN B CD  1 
ATOM   3650 O OE1 . GLN B 1 247 ? 93.12500  124.00700 92.20400  1.000 79.53701  ? 254 GLN B OE1 1 
ATOM   3651 N NE2 . GLN B 1 247 ? 92.13800  125.25900 90.62700  1.000 77.27330  ? 254 GLN B NE2 1 
ATOM   3652 N N   . GLY B 1 248 ? 90.16500  125.81000 96.83200  1.000 76.27517  ? 255 GLY B N   1 
ATOM   3653 C CA  . GLY B 1 248 ? 90.61100  126.13500 98.17900  1.000 74.53888  ? 255 GLY B CA  1 
ATOM   3654 C C   . GLY B 1 248 ? 89.93300  125.30900 99.25600  1.000 72.56312  ? 255 GLY B C   1 
ATOM   3655 O O   . GLY B 1 248 ? 90.58900  124.77000 100.15100 1.000 73.96032  ? 255 GLY B O   1 
ATOM   3656 N N   . LEU B 1 249 ? 88.61100  125.17300 99.16500  1.000 70.71108  ? 256 LEU B N   1 
ATOM   3657 C CA  . LEU B 1 249 ? 87.88500  124.33700 100.11500 1.000 72.26479  ? 256 LEU B CA  1 
ATOM   3658 C C   . LEU B 1 249 ? 88.30800  122.87700 100.02300 1.000 71.03148  ? 256 LEU B C   1 
ATOM   3659 O O   . LEU B 1 249 ? 88.45000  122.20300 101.04800 1.000 69.51994  ? 256 LEU B O   1 
ATOM   3660 C CB  . LEU B 1 249 ? 86.38200  124.47400 99.88900  1.000 69.48265  ? 256 LEU B CB  1 
ATOM   3661 C CG  . LEU B 1 249 ? 85.49000  123.59200 100.76100 1.000 68.17223  ? 256 LEU B CG  1 
ATOM   3662 C CD1 . LEU B 1 249 ? 85.70200  123.91000 102.22300 1.000 70.49688  ? 256 LEU B CD1 1 
ATOM   3663 C CD2 . LEU B 1 249 ? 84.03500  123.77900 100.38300 1.000 69.35805  ? 256 LEU B CD2 1 
ATOM   3664 N N   . TYR B 1 250 ? 88.50800  122.36700 98.81000  1.000 67.75795  ? 257 TYR B N   1 
ATOM   3665 C CA  . TYR B 1 250 ? 88.93200  120.98000 98.66900  1.000 60.48394  ? 257 TYR B CA  1 
ATOM   3666 C C   . TYR B 1 250 ? 90.32600  120.74500 99.23700  1.000 62.50428  ? 257 TYR B C   1 
ATOM   3667 O O   . TYR B 1 250 ? 90.55300  119.74300 99.91800  1.000 74.32293  ? 257 TYR B O   1 
ATOM   3668 C CB  . TYR B 1 250 ? 88.88800  120.55400 97.20700  1.000 61.68325  ? 257 TYR B CB  1 
ATOM   3669 C CG  . TYR B 1 250 ? 89.32300  119.12700 97.00400  1.000 65.98484  ? 257 TYR B CG  1 
ATOM   3670 C CD1 . TYR B 1 250 ? 88.69000  118.09100 97.66100  1.000 66.79007  ? 257 TYR B CD1 1 
ATOM   3671 C CD2 . TYR B 1 250 ? 90.38300  118.82000 96.17400  1.000 66.82834  ? 257 TYR B CD2 1 
ATOM   3672 C CE1 . TYR B 1 250 ? 89.08300  116.79100 97.47400  1.000 63.34289  ? 257 TYR B CE1 1 
ATOM   3673 C CE2 . TYR B 1 250 ? 90.78700  117.52300 95.99100  1.000 62.03385  ? 257 TYR B CE2 1 
ATOM   3674 C CZ  . TYR B 1 250 ? 90.13300  116.51400 96.64000  1.000 62.21028  ? 257 TYR B CZ  1 
ATOM   3675 O OH  . TYR B 1 250 ? 90.54600  115.21900 96.46400  1.000 67.94473  ? 257 TYR B OH  1 
ATOM   3676 N N   . ARG B 1 251 ? 91.27700  121.63500 98.95500  1.000 59.42322  ? 258 ARG B N   1 
ATOM   3677 C CA  . ARG B 1 251 ? 92.60300  121.51500 99.55400  1.000 64.79476  ? 258 ARG B CA  1 
ATOM   3678 C C   . ARG B 1 251 ? 92.56400  121.59600 101.07500 1.000 67.23073  ? 258 ARG B C   1 
ATOM   3679 O O   . ARG B 1 251 ? 93.25200  120.83000 101.76100 1.000 64.85647  ? 258 ARG B O   1 
ATOM   3680 C CB  . ARG B 1 251 ? 93.54100  122.57600 98.99100  1.000 64.11919  ? 258 ARG B CB  1 
ATOM   3681 C CG  . ARG B 1 251 ? 93.90000  122.37100 97.53900  1.000 63.31047  ? 258 ARG B CG  1 
ATOM   3682 C CD  . ARG B 1 251 ? 94.78400  123.49300 97.04200  1.000 67.71458  ? 258 ARG B CD  1 
ATOM   3683 N NE  . ARG B 1 251 ? 94.84700  123.54000 95.58800  1.000 72.13852  ? 258 ARG B NE  1 
ATOM   3684 C CZ  . ARG B 1 251 ? 95.33400  124.55900 94.89600  1.000 72.27656  ? 258 ARG B CZ  1 
ATOM   3685 N NH1 . ARG B 1 251 ? 95.79900  125.64200 95.49600  1.000 71.23759  ? 258 ARG B NH1 1 
ATOM   3686 N NH2 . ARG B 1 251 ? 95.35600  124.49100 93.56800  1.000 66.90018  ? 258 ARG B NH2 1 
ATOM   3687 N N   . PHE B 1 252 ? 91.76400  122.50700 101.62700 1.000 65.16144  ? 259 PHE B N   1 
ATOM   3688 C CA  . PHE B 1 252 ? 91.64300  122.58600 103.08000 1.000 60.90573  ? 259 PHE B CA  1 
ATOM   3689 C C   . PHE B 1 252 ? 91.04800  121.31300 103.67100 1.000 62.15398  ? 259 PHE B C   1 
ATOM   3690 O O   . PHE B 1 252 ? 91.53500  120.79800 104.68500 1.000 65.05393  ? 259 PHE B O   1 
ATOM   3691 C CB  . PHE B 1 252 ? 90.80100  123.79900 103.46700 1.000 60.56567  ? 259 PHE B CB  1 
ATOM   3692 C CG  . PHE B 1 252 ? 90.56100  123.91800 104.93800 1.000 64.22790  ? 259 PHE B CG  1 
ATOM   3693 C CD1 . PHE B 1 252 ? 91.57000  124.33800 105.78100 1.000 63.80616  ? 259 PHE B CD1 1 
ATOM   3694 C CD2 . PHE B 1 252 ? 89.32900  123.61100 105.47800 1.000 64.85445  ? 259 PHE B CD2 1 
ATOM   3695 C CE1 . PHE B 1 252 ? 91.35600  124.44900 107.13300 1.000 65.60950  ? 259 PHE B CE1 1 
ATOM   3696 C CE2 . PHE B 1 252 ? 89.10900  123.72000 106.83000 1.000 63.55450  ? 259 PHE B CE2 1 
ATOM   3697 C CZ  . PHE B 1 252 ? 90.12400  124.14000 107.65800 1.000 66.01859  ? 259 PHE B CZ  1 
ATOM   3698 N N   . ALA B 1 253 ? 89.97900  120.80000 103.06300 1.000 54.84694  ? 260 ALA B N   1 
ATOM   3699 C CA  . ALA B 1 253 ? 89.39000  119.55000 103.52700 1.000 51.34409  ? 260 ALA B CA  1 
ATOM   3700 C C   . ALA B 1 253 ? 90.35400  118.37800 103.41000 1.000 51.09385  ? 260 ALA B C   1 
ATOM   3701 O O   . ALA B 1 253 ? 90.39800  117.51900 104.29300 1.000 55.29145  ? 260 ALA B O   1 
ATOM   3702 C CB  . ALA B 1 253 ? 88.10800  119.26200 102.75100 1.000 49.81570  ? 260 ALA B CB  1 
ATOM   3703 N N   . ASN B 1 254 ? 91.14000  118.32300 102.33700 1.000 49.63075  ? 261 ASN B N   1 
ATOM   3704 C CA  . ASN B 1 254 ? 92.15200  117.27800 102.21800 1.000 48.02223  ? 261 ASN B CA  1 
ATOM   3705 C C   . ASN B 1 254 ? 93.22000  117.37500 103.30000 1.000 54.11959  ? 261 ASN B C   1 
ATOM   3706 O O   . ASN B 1 254 ? 93.60300  116.35900 103.89100 1.000 57.18189  ? 261 ASN B O   1 
ATOM   3707 C CB  . ASN B 1 254 ? 92.79400  117.33500 100.83700 1.000 47.79153  ? 261 ASN B CB  1 
ATOM   3708 C CG  . ASN B 1 254 ? 93.69400  116.16000 100.57300 1.000 55.94743  ? 261 ASN B CG  1 
ATOM   3709 O OD1 . ASN B 1 254 ? 93.29100  115.01200 100.72100 1.000 60.06081  ? 261 ASN B OD1 1 
ATOM   3710 N ND2 . ASN B 1 254 ? 94.92400  116.43900 100.17900 1.000 60.90566  ? 261 ASN B ND2 1 
ATOM   3711 N N   . PHE B 1 255 ? 93.68100  118.58700 103.60700 1.000 47.11306  ? 262 PHE B N   1 
ATOM   3712 C CA  . PHE B 1 255 ? 94.63400  118.76500 104.70000 1.000 45.89034  ? 262 PHE B CA  1 
ATOM   3713 C C   . PHE B 1 255 ? 94.05600  118.30900 106.03400 1.000 52.32948  ? 262 PHE B C   1 
ATOM   3714 O O   . PHE B 1 255 ? 94.69300  117.54700 106.77200 1.000 55.00627  ? 262 PHE B O   1 
ATOM   3715 C CB  . PHE B 1 255 ? 95.06900  120.22700 104.77300 1.000 53.85947  ? 262 PHE B CB  1 
ATOM   3716 C CG  . PHE B 1 255 ? 95.99100  120.53700 105.91700 1.000 55.79259  ? 262 PHE B CG  1 
ATOM   3717 C CD1 . PHE B 1 255 ? 97.09900  119.75600 106.16400 1.000 49.21088  ? 262 PHE B CD1 1 
ATOM   3718 C CD2 . PHE B 1 255 ? 95.76200  121.63000 106.72800 1.000 55.45029  ? 262 PHE B CD2 1 
ATOM   3719 C CE1 . PHE B 1 255 ? 97.95000  120.04800 107.20400 1.000 48.93017  ? 262 PHE B CE1 1 
ATOM   3720 C CE2 . PHE B 1 255 ? 96.61000  121.92200 107.76900 1.000 54.65112  ? 262 PHE B CE2 1 
ATOM   3721 C CZ  . PHE B 1 255 ? 97.70500  121.12900 108.00600 1.000 52.83309  ? 262 PHE B CZ  1 
ATOM   3722 N N   . VAL B 1 256 ? 92.83900  118.75000 106.34900 1.000 48.43235  ? 263 VAL B N   1 
ATOM   3723 C CA  . VAL B 1 256 ? 92.19800  118.38000 107.61000 1.000 35.38938  ? 263 VAL B CA  1 
ATOM   3724 C C   . VAL B 1 256 ? 91.98600  116.87200 107.70900 1.000 39.51630  ? 263 VAL B C   1 
ATOM   3725 O O   . VAL B 1 256 ? 92.26400  116.26200 108.74900 1.000 49.77057  ? 263 VAL B O   1 
ATOM   3726 C CB  . VAL B 1 256 ? 90.87400  119.14100 107.77600 1.000 38.19892  ? 263 VAL B CB  1 
ATOM   3727 C CG1 . VAL B 1 256 ? 90.11200  118.60200 108.95400 1.000 45.27937  ? 263 VAL B CG1 1 
ATOM   3728 C CG2 . VAL B 1 256 ? 91.14100  120.61200 107.95800 1.000 44.38554  ? 263 VAL B CG2 1 
ATOM   3729 N N   . PHE B 1 257 ? 91.48100  116.24500 106.64600 1.000 40.89721  ? 264 PHE B N   1 
ATOM   3730 C CA  . PHE B 1 257 ? 91.24000  114.80700 106.70300 1.000 38.49658  ? 264 PHE B CA  1 
ATOM   3731 C C   . PHE B 1 257 ? 92.52600  114.00200 106.80800 1.000 42.51057  ? 264 PHE B C   1 
ATOM   3732 O O   . PHE B 1 257 ? 92.58500  113.04500 107.58400 1.000 49.35678  ? 264 PHE B O   1 
ATOM   3733 C CB  . PHE B 1 257 ? 90.42700  114.34100 105.49800 1.000 44.10211  ? 264 PHE B CB  1 
ATOM   3734 C CG  . PHE B 1 257 ? 88.96300  114.63200 105.61300 1.000 49.74088  ? 264 PHE B CG  1 
ATOM   3735 C CD1 . PHE B 1 257 ? 88.22600  114.09600 106.64900 1.000 45.47401  ? 264 PHE B CD1 1 
ATOM   3736 C CD2 . PHE B 1 257 ? 88.31800  115.41300 104.68000 1.000 45.14798  ? 264 PHE B CD2 1 
ATOM   3737 C CE1 . PHE B 1 257 ? 86.88400  114.35400 106.76500 1.000 41.08399  ? 264 PHE B CE1 1 
ATOM   3738 C CE2 . PHE B 1 257 ? 86.97300  115.67200 104.79200 1.000 42.89415  ? 264 PHE B CE2 1 
ATOM   3739 C CZ  . PHE B 1 257 ? 86.25700  115.14100 105.83400 1.000 46.24558  ? 264 PHE B CZ  1 
ATOM   3740 N N   . ILE B 1 258 ? 93.57800  114.37500 106.07800 1.000 40.92216  ? 265 ILE B N   1 
ATOM   3741 C CA  . ILE B 1 258 ? 94.82900  113.63200 106.21700 1.000 32.59618  ? 265 ILE B CA  1 
ATOM   3742 C C   . ILE B 1 258 ? 95.42900  113.81600 107.60500 1.000 35.26470  ? 265 ILE B C   1 
ATOM   3743 O O   . ILE B 1 258 ? 95.94000  112.86100 108.19800 1.000 42.01723  ? 265 ILE B O   1 
ATOM   3744 C CB  . ILE B 1 258 ? 95.83000  114.01700 105.11700 1.000 39.51915  ? 265 ILE B CB  1 
ATOM   3745 C CG1 . ILE B 1 258 ? 95.25100  113.72700 103.73500 1.000 39.72261  ? 265 ILE B CG1 1 
ATOM   3746 C CG2 . ILE B 1 258 ? 97.11300  113.24200 105.29500 1.000 44.96748  ? 265 ILE B CG2 1 
ATOM   3747 C CD1 . ILE B 1 258 ? 95.29900  112.27800 103.35300 1.000 40.81864  ? 265 ILE B CD1 1 
ATOM   3748 N N   . LEU B 1 259 ? 95.35600  115.02400 108.16400 1.000 36.90918  ? 266 LEU B N   1 
ATOM   3749 C CA  . LEU B 1 259 ? 95.86900  115.23100 109.51500 1.000 35.05941  ? 266 LEU B CA  1 
ATOM   3750 C C   . LEU B 1 259 ? 95.10600  114.41300 110.55400 1.000 41.99504  ? 266 LEU B C   1 
ATOM   3751 O O   . LEU B 1 259 ? 95.71300  113.71300 111.37800 1.000 51.29712  ? 266 LEU B O   1 
ATOM   3752 C CB  . LEU B 1 259 ? 95.81600  116.71300 109.86300 1.000 34.11735  ? 266 LEU B CB  1 
ATOM   3753 C CG  . LEU B 1 259 ? 96.22700  117.04100 111.28500 1.000 34.17760  ? 266 LEU B CG  1 
ATOM   3754 C CD1 . LEU B 1 259 ? 97.64900  116.61200 111.50000 1.000 37.70429  ? 266 LEU B CD1 1 
ATOM   3755 C CD2 . LEU B 1 259 ? 96.07000  118.52000 111.52800 1.000 39.56757  ? 266 LEU B CD2 1 
ATOM   3756 N N   . MET B 1 260 ? 93.77300  114.47300 110.52500 1.000 50.31256  ? 267 MET B N   1 
ATOM   3757 C CA  . MET B 1 260 ? 92.98600  113.71000 111.48800 1.000 46.34273  ? 267 MET B CA  1 
ATOM   3758 C C   . MET B 1 260 ? 93.21100  112.21600 111.32900 1.000 47.86343  ? 267 MET B C   1 
ATOM   3759 O O   . MET B 1 260 ? 93.34500  111.49000 112.32200 1.000 58.36129  ? 267 MET B O   1 
ATOM   3760 C CB  . MET B 1 260 ? 91.50700  114.03800 111.31900 1.000 48.89584  ? 267 MET B CB  1 
ATOM   3761 C CG  . MET B 1 260 ? 91.10900  115.41600 111.79300 1.000 51.57166  ? 267 MET B CG  1 
ATOM   3762 S SD  . MET B 1 260 ? 89.40900  115.79500 111.34200 1.000 73.03339  ? 267 MET B SD  1 
ATOM   3763 C CE  . MET B 1 260 ? 88.52800  114.56200 112.28700 1.000 58.00890  ? 267 MET B CE  1 
ATOM   3764 N N   . GLY B 1 261 ? 93.29300  111.74400 110.09000 1.000 37.82416  ? 268 GLY B N   1 
ATOM   3765 C CA  . GLY B 1 261 ? 93.52500  110.33200 109.86100 1.000 38.18866  ? 268 GLY B CA  1 
ATOM   3766 C C   . GLY B 1 261 ? 94.87000  109.85800 110.36600 1.000 30.80688  ? 268 GLY B C   1 
ATOM   3767 O O   . GLY B 1 261 ? 94.96900  108.80900 111.00200 1.000 34.84796  ? 268 GLY B O   1 
ATOM   3768 N N   . VAL B 1 262 ? 95.93100  110.60600 110.06000 1.000 24.87072  ? 269 VAL B N   1 
ATOM   3769 C CA  . VAL B 1 262 ? 97.25400  110.21900 110.53600 1.000 21.41582  ? 269 VAL B CA  1 
ATOM   3770 C C   . VAL B 1 262 ? 97.29900  110.18200 112.05400 1.000 34.76559  ? 269 VAL B C   1 
ATOM   3771 O O   . VAL B 1 262 ? 97.80100  109.22000 112.64200 1.000 47.52327  ? 269 VAL B O   1 
ATOM   3772 C CB  . VAL B 1 262 ? 98.33000  111.16000 109.96900 1.000 19.18090  ? 269 VAL B CB  1 
ATOM   3773 C CG1 . VAL B 1 262 ? 99.65300  110.85500 110.59800 1.000 28.91455  ? 269 VAL B CG1 1 
ATOM   3774 C CG2 . VAL B 1 262 ? 98.44000  110.99200 108.48300 1.000 37.99724  ? 269 VAL B CG2 1 
ATOM   3775 N N   . CYS B 1 263 ? 96.74900  111.19900 112.72000 1.000 47.98800  ? 270 CYS B N   1 
ATOM   3776 C CA  . CYS B 1 263 ? 96.78300  111.19300 114.18200 1.000 37.77658  ? 270 CYS B CA  1 
ATOM   3777 C C   . CYS B 1 263 ? 95.97300  110.04700 114.78800 1.000 45.15389  ? 270 CYS B C   1 
ATOM   3778 O O   . CYS B 1 263 ? 96.45300  109.36500 115.70400 1.000 53.73747  ? 270 CYS B O   1 
ATOM   3779 C CB  . CYS B 1 263 ? 96.29300  112.53300 114.71800 1.000 42.39082  ? 270 CYS B CB  1 
ATOM   3780 S SG  . CYS B 1 263 ? 97.30100  113.93600 114.20700 1.000 60.80049  ? 270 CYS B SG  1 
ATOM   3781 N N   . CYS B 1 264 ? 94.82000  109.71600 114.20200 1.000 51.74202  ? 271 CYS B N   1 
ATOM   3782 C CA  . CYS B 1 264 ? 94.02200  108.60600 114.72600 1.000 44.10970  ? 271 CYS B CA  1 
ATOM   3783 C C   . CYS B 1 264 ? 94.66200  107.24600 114.47500 1.000 50.57757  ? 271 CYS B C   1 
ATOM   3784 O O   . CYS B 1 264 ? 94.72800  106.41300 115.38400 1.000 61.46067  ? 271 CYS B O   1 
ATOM   3785 C CB  . CYS B 1 264 ? 92.61100  108.64700 114.15000 1.000 49.80911  ? 271 CYS B CB  1 
ATOM   3786 S SG  . CYS B 1 264 ? 91.64200  110.03800 114.74900 1.000 71.16534  ? 271 CYS B SG  1 
ATOM   3787 N N   . ILE B 1 265 ? 95.13200  106.98200 113.25900 1.000 45.71733  ? 272 ILE B N   1 
ATOM   3788 C CA  . ILE B 1 265 ? 95.71000  105.66600 112.99600 1.000 40.11054  ? 272 ILE B CA  1 
ATOM   3789 C C   . ILE B 1 265 ? 97.07100  105.49900 113.66900 1.000 41.20687  ? 272 ILE B C   1 
ATOM   3790 O O   . ILE B 1 265 ? 97.40900  104.39900 114.11300 1.000 56.39820  ? 272 ILE B O   1 
ATOM   3791 C CB  . ILE B 1 265 ? 95.75500  105.36700 111.49000 1.000 35.59164  ? 272 ILE B CB  1 
ATOM   3792 C CG1 . ILE B 1 265 ? 94.33200  105.18400 110.97500 1.000 41.40680  ? 272 ILE B CG1 1 
ATOM   3793 C CG2 . ILE B 1 265 ? 96.52500  104.11400 111.21500 1.000 40.18644  ? 272 ILE B CG2 1 
ATOM   3794 C CD1 . ILE B 1 265 ? 94.24300  104.48800 109.64900 1.000 37.06773  ? 272 ILE B CD1 1 
ATOM   3795 N N   . TYR B 1 266 ? 97.88100  106.55100 113.76300 1.000 41.00006  ? 273 TYR B N   1 
ATOM   3796 C CA  . TYR B 1 266 ? 99.10600  106.42800 114.54900 1.000 44.53459  ? 273 TYR B CA  1 
ATOM   3797 C C   . TYR B 1 266 ? 98.81700  106.18700 116.03300 1.000 49.36215  ? 273 TYR B C   1 
ATOM   3798 O O   . TYR B 1 266 ? 99.52300  105.40800 116.69200 1.000 56.76268  ? 273 TYR B O   1 
ATOM   3799 C CB  . TYR B 1 266 ? 99.96000  107.67600 114.36300 1.000 49.92655  ? 273 TYR B CB  1 
ATOM   3800 C CG  . TYR B 1 266 ? 101.31800 107.59800 115.00700 1.000 53.08752  ? 273 TYR B CG  1 
ATOM   3801 C CD1 . TYR B 1 266 ? 102.38800 107.02000 114.34300 1.000 56.28498  ? 273 TYR B CD1 1 
ATOM   3802 C CD2 . TYR B 1 266 ? 101.53400 108.11100 116.27700 1.000 53.87018  ? 273 TYR B CD2 1 
ATOM   3803 C CE1 . TYR B 1 266 ? 103.63400 106.94900 114.93000 1.000 55.64161  ? 273 TYR B CE1 1 
ATOM   3804 C CE2 . TYR B 1 266 ? 102.77500 108.04600 116.87000 1.000 54.82956  ? 273 TYR B CE2 1 
ATOM   3805 C CZ  . TYR B 1 266 ? 103.82100 107.46400 116.19300 1.000 61.40362  ? 273 TYR B CZ  1 
ATOM   3806 O OH  . TYR B 1 266 ? 105.06000 107.39900 116.78300 1.000 65.14430  ? 273 TYR B OH  1 
ATOM   3807 N N   . SER B 1 267 ? 97.75100  106.79100 116.56800 1.000 45.49419  ? 274 SER B N   1 
ATOM   3808 C CA  . SER B 1 267 ? 97.32400  106.43700 117.91900 1.000 42.83065  ? 274 SER B CA  1 
ATOM   3809 C C   . SER B 1 267 ? 96.90000  104.97700 118.01600 1.000 49.63885  ? 274 SER B C   1 
ATOM   3810 O O   . SER B 1 267 ? 97.21300  104.29200 119.00000 1.000 56.25291  ? 274 SER B O   1 
ATOM   3811 C CB  . SER B 1 267 ? 96.18500  107.35000 118.35700 1.000 44.48384  ? 274 SER B CB  1 
ATOM   3812 O OG  . SER B 1 267 ? 96.62700  108.69100 118.42700 1.000 51.61110  ? 274 SER B OG  1 
ATOM   3813 N N   . LEU B 1 268 ? 96.18400  104.48300 117.00700 1.000 42.30056  ? 275 LEU B N   1 
ATOM   3814 C CA  . LEU B 1 268 ? 95.79100  103.07800 116.99000 1.000 38.53234  ? 275 LEU B CA  1 
ATOM   3815 C C   . LEU B 1 268 ? 97.00000  102.15200 116.94100 1.000 47.25816  ? 275 LEU B C   1 
ATOM   3816 O O   . LEU B 1 268 ? 97.00900  101.09800 117.58400 1.000 61.08550  ? 275 LEU B O   1 
ATOM   3817 C CB  . LEU B 1 268 ? 94.87400  102.82000 115.80000 1.000 29.97666  ? 275 LEU B CB  1 
ATOM   3818 C CG  . LEU B 1 268 ? 94.33800  101.40700 115.65000 1.000 41.62199  ? 275 LEU B CG  1 
ATOM   3819 C CD1 . LEU B 1 268 ? 93.50400  101.05200 116.85100 1.000 46.48411  ? 275 LEU B CD1 1 
ATOM   3820 C CD2 . LEU B 1 268 ? 93.52200  101.30000 114.38700 1.000 47.33322  ? 275 LEU B CD2 1 
ATOM   3821 N N   . PHE B 1 269 ? 98.02900  102.52800 116.18400 1.000 37.82793  ? 276 PHE B N   1 
ATOM   3822 C CA  . PHE B 1 269 ? 99.25900  101.74300 116.14700 1.000 30.62337  ? 276 PHE B CA  1 
ATOM   3823 C C   . PHE B 1 269 ? 99.93800  101.68900 117.50700 1.000 37.09957  ? 276 PHE B C   1 
ATOM   3824 O O   . PHE B 1 269 ? 100.37500 100.62300 117.94600 1.000 48.67215  ? 276 PHE B O   1 
ATOM   3825 C CB  . PHE B 1 269 ? 100.22400 102.29000 115.09800 1.000 36.85267  ? 276 PHE B CB  1 
ATOM   3826 C CG  . PHE B 1 269 ? 99.79700  102.03900 113.68700 1.000 36.33439  ? 276 PHE B CG  1 
ATOM   3827 C CD1 . PHE B 1 269 ? 98.66000  101.31100 113.41000 1.000 36.63108  ? 276 PHE B CD1 1 
ATOM   3828 C CD2 . PHE B 1 269 ? 100.54800 102.51600 112.63700 1.000 32.22908  ? 276 PHE B CD2 1 
ATOM   3829 C CE1 . PHE B 1 269 ? 98.27800  101.07700 112.11600 1.000 36.62663  ? 276 PHE B CE1 1 
ATOM   3830 C CE2 . PHE B 1 269 ? 100.16700 102.28200 111.34600 1.000 39.19723  ? 276 PHE B CE2 1 
ATOM   3831 C CZ  . PHE B 1 269 ? 99.03100  101.56300 111.08500 1.000 38.54690  ? 276 PHE B CZ  1 
ATOM   3832 N N   . ASN B 1 270 ? 100.03100 102.82400 118.19700 1.000 43.82745  ? 277 ASN B N   1 
ATOM   3833 C CA  . ASN B 1 270 ? 100.58400 102.80200 119.55300 1.000 43.79046  ? 277 ASN B CA  1 
ATOM   3834 C C   . ASN B 1 270 ? 99.78000  101.90300 120.49400 1.000 45.29705  ? 277 ASN B C   1 
ATOM   3835 O O   . ASN B 1 270 ? 100.35000 101.09100 121.24000 1.000 52.50296  ? 277 ASN B O   1 
ATOM   3836 C CB  . ASN B 1 270 ? 100.66400 104.21900 120.10800 1.000 43.65993  ? 277 ASN B CB  1 
ATOM   3837 C CG  . ASN B 1 270 ? 101.85900 104.97400 119.58600 1.000 49.66857  ? 277 ASN B CG  1 
ATOM   3838 O OD1 . ASN B 1 270 ? 102.60900 104.47100 118.75600 1.000 49.77664  ? 277 ASN B OD1 1 
ATOM   3839 N ND2 . ASN B 1 270 ? 102.04900 106.18900 120.07600 1.000 53.98831  ? 277 ASN B ND2 1 
ATOM   3840 N N   . VAL B 1 271 ? 98.45500  102.03500 120.48300 1.000 41.41627  ? 278 VAL B N   1 
ATOM   3841 C CA  . VAL B 1 271 ? 97.62600  101.24000 121.39100 1.000 42.36670  ? 278 VAL B CA  1 
ATOM   3842 C C   . VAL B 1 271 ? 97.73300  99.74200  121.09700 1.000 52.30278  ? 278 VAL B C   1 
ATOM   3843 O O   . VAL B 1 271 ? 97.87700  98.91800  122.01800 1.000 63.16313  ? 278 VAL B O   1 
ATOM   3844 C CB  . VAL B 1 271 ? 96.17100  101.72600 121.32100 1.000 45.89478  ? 278 VAL B CB  1 
ATOM   3845 C CG1 . VAL B 1 271 ? 95.25400  100.70800 121.93000 1.000 52.27785  ? 278 VAL B CG1 1 
ATOM   3846 C CG2 . VAL B 1 271 ? 96.03200  103.05500 122.02200 1.000 51.58197  ? 278 VAL B CG2 1 
ATOM   3847 N N   . ILE B 1 272 ? 97.69700  99.35700  119.82000 1.000 41.07983  ? 279 ILE B N   1 
ATOM   3848 C CA  . ILE B 1 272 ? 97.90400  97.95000  119.49200 1.000 36.82612  ? 279 ILE B CA  1 
ATOM   3849 C C   . ILE B 1 272 ? 99.30200  97.49600  119.89300 1.000 40.56517  ? 279 ILE B C   1 
ATOM   3850 O O   . ILE B 1 272 ? 99.49400  96.34800  120.30000 1.000 42.83900  ? 279 ILE B O   1 
ATOM   3851 C CB  . ILE B 1 272 ? 97.62500  97.69000  118.00200 1.000 33.38891  ? 279 ILE B CB  1 
ATOM   3852 C CG1 . ILE B 1 272 ? 96.14700  97.87700  117.70100 1.000 38.74351  ? 279 ILE B CG1 1 
ATOM   3853 C CG2 . ILE B 1 272 ? 97.96900  96.27500  117.63300 1.000 40.40221  ? 279 ILE B CG2 1 
ATOM   3854 C CD1 . ILE B 1 272 ? 95.83000  97.82100  116.23700 1.000 36.67746  ? 279 ILE B CD1 1 
ATOM   3855 N N   . SER B 1 273 ? 100.31000 98.35900  119.74500 1.000 44.01716  ? 280 SER B N   1 
ATOM   3856 C CA  . SER B 1 273 ? 101.64900 97.95900  120.15900 1.000 41.06319  ? 280 SER B CA  1 
ATOM   3857 C C   . SER B 1 273 ? 101.71000 97.66900  121.65000 1.000 45.65195  ? 280 SER B C   1 
ATOM   3858 O O   . SER B 1 273 ? 102.42200 96.75400  122.07900 1.000 55.15720  ? 280 SER B O   1 
ATOM   3859 C CB  . SER B 1 273 ? 102.65800 99.04200  119.79700 1.000 42.74246  ? 280 SER B CB  1 
ATOM   3860 O OG  . SER B 1 273 ? 102.73500 100.01100 120.82000 1.000 53.25070  ? 280 SER B OG  1 
ATOM   3861 N N   . ILE B 1 274 ? 100.91700 98.38400  122.44600 1.000 51.94382  ? 281 ILE B N   1 
ATOM   3862 C CA  . ILE B 1 274 ? 100.86600 98.08200  123.87600 1.000 52.29884  ? 281 ILE B CA  1 
ATOM   3863 C C   . ILE B 1 274 ? 100.17700 96.74600  124.13200 1.000 58.07322  ? 281 ILE B C   1 
ATOM   3864 O O   . ILE B 1 274 ? 100.61700 95.95400  124.97900 1.000 64.79336  ? 281 ILE B O   1 
ATOM   3865 C CB  . ILE B 1 274 ? 100.18100 99.22300  124.64600 1.000 52.61131  ? 281 ILE B CB  1 
ATOM   3866 C CG1 . ILE B 1 274 ? 101.02800 100.49000 124.58100 1.000 55.60814  ? 281 ILE B CG1 1 
ATOM   3867 C CG2 . ILE B 1 274 ? 99.94600  98.82700  126.08400 1.000 50.99516  ? 281 ILE B CG2 1 
ATOM   3868 C CD1 . ILE B 1 274 ? 100.27900 101.74000 124.96600 1.000 57.31965  ? 281 ILE B CD1 1 
ATOM   3869 N N   . LEU B 1 275 ? 99.10100  96.46100  123.39900 1.000 57.29572  ? 282 LEU B N   1 
ATOM   3870 C CA  . LEU B 1 275 ? 98.46400  95.15300  123.56500 1.000 55.70368  ? 282 LEU B CA  1 
ATOM   3871 C C   . LEU B 1 275 ? 99.35200  93.99800  123.10200 1.000 58.34137  ? 282 LEU B C   1 
ATOM   3872 O O   . LEU B 1 275 ? 99.34400  92.92300  123.71600 1.000 65.50569  ? 282 LEU B O   1 
ATOM   3873 C CB  . LEU B 1 275 ? 97.13200  95.11000  122.82800 1.000 51.85135  ? 282 LEU B CB  1 
ATOM   3874 C CG  . LEU B 1 275 ? 96.12800  96.14700  123.30500 1.000 55.26857  ? 282 LEU B CG  1 
ATOM   3875 C CD1 . LEU B 1 275 ? 94.87500  96.05900  122.48300 1.000 58.70288  ? 282 LEU B CD1 1 
ATOM   3876 C CD2 . LEU B 1 275 ? 95.82100  95.92300  124.76400 1.000 60.28696  ? 282 LEU B CD2 1 
ATOM   3877 N N   . ILE B 1 276 ? 100.17400 94.21600  122.07900 1.000 53.41668  ? 283 ILE B N   1 
ATOM   3878 C CA  . ILE B 1 276 ? 101.17000 93.22000  121.69400 1.000 53.82078  ? 283 ILE B CA  1 
ATOM   3879 C C   . ILE B 1 276 ? 102.19800 93.02300  122.80000 1.000 56.46059  ? 283 ILE B C   1 
ATOM   3880 O O   . ILE B 1 276 ? 102.60400 91.89200  123.08200 1.000 56.02995  ? 283 ILE B O   1 
ATOM   3881 C CB  . ILE B 1 276 ? 101.83200 93.59700  120.35800 1.000 49.86282  ? 283 ILE B CB  1 
ATOM   3882 C CG1 . ILE B 1 276 ? 100.79200 93.61500  119.24700 1.000 50.98354  ? 283 ILE B CG1 1 
ATOM   3883 C CG2 . ILE B 1 276 ? 102.88000 92.58500  119.99200 1.000 48.35791  ? 283 ILE B CG2 1 
ATOM   3884 C CD1 . ILE B 1 276 ? 101.30000 94.19200  117.96800 1.000 51.37525  ? 283 ILE B CD1 1 
ATOM   3885 N N   . LYS B 1 277 ? 102.71100 94.11300  123.37400 1.000 59.43546  ? 284 LYS B N   1 
ATOM   3886 C CA  . LYS B 1 277 ? 103.68300 93.96700  124.45700 1.000 55.12725  ? 284 LYS B CA  1 
ATOM   3887 C C   . LYS B 1 277 ? 103.11700 93.15800  125.61900 1.000 59.36951  ? 284 LYS B C   1 
ATOM   3888 O O   . LYS B 1 277 ? 103.80200 92.29100  126.17800 1.000 69.98200  ? 284 LYS B O   1 
ATOM   3889 C CB  . LYS B 1 277 ? 104.14200 95.33400  124.96000 1.000 59.38153  ? 284 LYS B CB  1 
ATOM   3890 C CG  . LYS B 1 277 ? 105.39100 95.26300  125.82200 1.000 61.51060  ? 284 LYS B CG  1 
ATOM   3891 C CD  . LYS B 1 277 ? 105.68600 96.58000  126.51800 1.000 63.47047  ? 284 LYS B CD  1 
ATOM   3892 C CE  . LYS B 1 277 ? 105.99300 97.68800  125.53400 1.000 66.75424  ? 284 LYS B CE  1 
ATOM   3893 N NZ  . LYS B 1 277 ? 106.30700 98.97400  126.21500 1.000 68.53427  ? 284 LYS B NZ  1 
ATOM   3894 N N   . GLN B 1 278 ? 101.86200 93.41500  125.98900 1.000 64.81017  ? 285 GLN B N   1 
ATOM   3895 C CA  . GLN B 1 278 ? 101.23100 92.60100  127.02900 1.000 67.06983  ? 285 GLN B CA  1 
ATOM   3896 C C   . GLN B 1 278 ? 101.06400 91.14300  126.60600 1.000 70.94898  ? 285 GLN B C   1 
ATOM   3897 O O   . GLN B 1 278 ? 101.23100 90.23000  127.42500 1.000 69.56456  ? 285 GLN B O   1 
ATOM   3898 C CB  . GLN B 1 278 ? 99.87800  93.19600  127.41200 1.000 68.26985  ? 285 GLN B CB  1 
ATOM   3899 C CG  . GLN B 1 278 ? 99.97000  94.53000  128.12400 1.000 72.35640  ? 285 GLN B CG  1 
ATOM   3900 C CD  . GLN B 1 278 ? 98.61100  95.11800  128.42900 1.000 75.90216  ? 285 GLN B CD  1 
ATOM   3901 O OE1 . GLN B 1 278 ? 97.58100  94.50000  128.16600 1.000 76.36159  ? 285 GLN B OE1 1 
ATOM   3902 N NE2 . GLN B 1 278 ? 98.60000  96.32400  128.98200 1.000 74.77921  ? 285 GLN B NE2 1 
ATOM   3903 N N   . SER B 1 279 ? 100.78600 90.89400  125.32500 1.000 74.98594  ? 286 SER B N   1 
ATOM   3904 C CA  . SER B 1 279 ? 100.69500 89.51000  124.86300 1.000 72.89136  ? 286 SER B CA  1 
ATOM   3905 C C   . SER B 1 279 ? 102.04400 88.79600  124.89900 1.000 74.25298  ? 286 SER B C   1 
ATOM   3906 O O   . SER B 1 279 ? 102.11200 87.60900  125.23600 1.000 74.53764  ? 286 SER B O   1 
ATOM   3907 C CB  . SER B 1 279 ? 100.11600 89.47200  123.45400 1.000 70.46153  ? 286 SER B CB  1 
ATOM   3908 O OG  . SER B 1 279 ? 98.86300  90.12700  123.41300 1.000 77.96751  ? 286 SER B OG  1 
ATOM   3909 N N   . LEU B 1 280 ? 103.12400 89.49200  124.55100 1.000 70.19834  ? 287 LEU B N   1 
ATOM   3910 C CA  . LEU B 1 280 ? 104.45400 88.90000  124.68200 1.000 64.73911  ? 287 LEU B CA  1 
ATOM   3911 C C   . LEU B 1 280 ? 104.79500 88.59500  126.13100 1.000 65.28447  ? 287 LEU B C   1 
ATOM   3912 O O   . LEU B 1 280 ? 105.37800 87.54600  126.42800 1.000 70.71687  ? 287 LEU B O   1 
ATOM   3913 C CB  . LEU B 1 280 ? 105.51800 89.81600  124.08700 1.000 59.35344  ? 287 LEU B CB  1 
ATOM   3914 C CG  . LEU B 1 280 ? 105.44700 90.15100  122.60800 1.000 62.59350  ? 287 LEU B CG  1 
ATOM   3915 C CD1 . LEU B 1 280 ? 106.54300 91.12700  122.27700 1.000 65.37815  ? 287 LEU B CD1 1 
ATOM   3916 C CD2 . LEU B 1 280 ? 105.59200 88.89300  121.79700 1.000 67.90933  ? 287 LEU B CD2 1 
ATOM   3917 N N   . ASN B 1 281 ? 104.48500 89.51500  127.04500 1.000 74.89650  ? 288 ASN B N   1 
ATOM   3918 C CA  . ASN B 1 281 ? 104.71500 89.23000  128.45800 1.000 77.39462  ? 288 ASN B CA  1 
ATOM   3919 C C   . ASN B 1 281 ? 103.91500 88.02000  128.92800 1.000 80.51595  ? 288 ASN B C   1 
ATOM   3920 O O   . ASN B 1 281 ? 104.41800 87.20100  129.70600 1.000 79.48948  ? 288 ASN B O   1 
ATOM   3921 C CB  . ASN B 1 281 ? 104.38400 90.45400  129.30900 1.000 75.23509  ? 288 ASN B CB  1 
ATOM   3922 C CG  . ASN B 1 281 ? 105.39300 91.56400  129.14200 1.000 75.76456  ? 288 ASN B CG  1 
ATOM   3923 O OD1 . ASN B 1 281 ? 106.47600 91.35600  128.60000 1.000 75.99598  ? 288 ASN B OD1 1 
ATOM   3924 N ND2 . ASN B 1 281 ? 105.04700 92.75400  129.61400 1.000 78.15657  ? 288 ASN B ND2 1 
ATOM   3925 N N   . TRP B 1 282 ? 102.69400 87.85200  128.41900 1.000 85.93480  ? 289 TRP B N   1 
ATOM   3926 C CA  . TRP B 1 282 ? 101.93200 86.65200  128.75700 1.000 86.58881  ? 289 TRP B CA  1 
ATOM   3927 C C   . TRP B 1 282 ? 102.55500 85.38500  128.18100 1.000 87.56926  ? 289 TRP B C   1 
ATOM   3928 O O   . TRP B 1 282 ? 102.60600 84.35600  128.86200 1.000 89.21068  ? 289 TRP B O   1 
ATOM   3929 C CB  . TRP B 1 282 ? 100.48900 86.77700  128.28200 1.000 88.55851  ? 289 TRP B CB  1 
ATOM   3930 C CG  . TRP B 1 282 ? 99.70600  85.52200  128.51700 1.000 90.17257  ? 289 TRP B CG  1 
ATOM   3931 C CD1 . TRP B 1 282 ? 99.22200  85.07200  129.70900 1.000 90.23552  ? 289 TRP B CD1 1 
ATOM   3932 C CD2 . TRP B 1 282 ? 99.32600  84.54900  127.53700 1.000 89.96177  ? 289 TRP B CD2 1 
ATOM   3933 N NE1 . TRP B 1 282 ? 98.56000  83.88200  129.53300 1.000 90.22693  ? 289 TRP B NE1 1 
ATOM   3934 C CE2 . TRP B 1 282 ? 98.60900  83.54000  128.20800 1.000 90.09252  ? 289 TRP B CE2 1 
ATOM   3935 C CE3 . TRP B 1 282 ? 99.51700  84.43600  126.15800 1.000 89.08640  ? 289 TRP B CE3 1 
ATOM   3936 C CZ2 . TRP B 1 282 ? 98.08600  82.43300  127.54800 1.000 90.36757  ? 289 TRP B CZ2 1 
ATOM   3937 C CZ3 . TRP B 1 282 ? 98.99600  83.33500  125.50500 1.000 90.55362  ? 289 TRP B CZ3 1 
ATOM   3938 C CH2 . TRP B 1 282 ? 98.29000  82.34900  126.19900 1.000 91.96115  ? 289 TRP B CH2 1 
ATOM   3939 N N   . ILE B 1 283 ? 103.00600 85.42200  126.92700 1.000 84.05489  ? 290 ILE B N   1 
ATOM   3940 C CA  . ILE B 1 283 ? 103.65700 84.24800  126.34300 1.000 84.40305  ? 290 ILE B CA  1 
ATOM   3941 C C   . ILE B 1 283 ? 104.91700 83.87200  127.11700 1.000 84.77217  ? 290 ILE B C   1 
ATOM   3942 O O   . ILE B 1 283 ? 105.15400 82.69200  127.40300 1.000 86.26723  ? 290 ILE B O   1 
ATOM   3943 C CB  . ILE B 1 283 ? 103.96200 84.47800  124.85100 1.000 81.76494  ? 290 ILE B CB  1 
ATOM   3944 C CG1 . ILE B 1 283 ? 102.66900 84.54100  124.04100 1.000 84.30561  ? 290 ILE B CG1 1 
ATOM   3945 C CG2 . ILE B 1 283 ? 104.85200 83.37900  124.31400 1.000 82.52502  ? 290 ILE B CG2 1 
ATOM   3946 C CD1 . ILE B 1 283 ? 102.86900 84.99400  122.61400 1.000 84.56164  ? 290 ILE B CD1 1 
ATOM   3947 N N   . LEU B 1 284 ? 105.73800 84.85800  127.47600 1.000 84.12641  ? 291 LEU B N   1 
ATOM   3948 C CA  . LEU B 1 284 ? 106.92900 84.56300  128.26900 1.000 83.26909  ? 291 LEU B CA  1 
ATOM   3949 C C   . LEU B 1 284 ? 106.58800 84.04900  129.66200 1.000 84.59884  ? 291 LEU B C   1 
ATOM   3950 O O   . LEU B 1 284 ? 107.31700 83.20900  130.19900 1.000 86.53728  ? 291 LEU B O   1 
ATOM   3951 C CB  . LEU B 1 284 ? 107.82600 85.79400  128.36800 1.000 84.73307  ? 291 LEU B CB  1 
ATOM   3952 C CG  . LEU B 1 284 ? 108.47500 86.25600  127.06600 1.000 82.46834  ? 291 LEU B CG  1 
ATOM   3953 C CD1 . LEU B 1 284 ? 109.18900 87.57200  127.27100 1.000 81.80009  ? 291 LEU B CD1 1 
ATOM   3954 C CD2 . LEU B 1 284 ? 109.43600 85.20500  126.56800 1.000 81.72659  ? 291 LEU B CD2 1 
ATOM   3955 N N   . ARG B 1 285 ? 105.50200 84.53200  130.26700 1.000 88.10629  ? 292 ARG B N   1 
ATOM   3956 C CA  . ARG B 1 285 ? 105.07900 83.96800  131.54600 1.000 90.51119  ? 292 ARG B CA  1 
ATOM   3957 C C   . ARG B 1 285 ? 104.62800 82.51900  131.39800 1.000 92.04519  ? 292 ARG B C   1 
ATOM   3958 O O   . ARG B 1 285 ? 104.99100 81.66500  132.21400 1.000 89.34065  ? 292 ARG B O   1 
ATOM   3959 C CB  . ARG B 1 285 ? 103.96400 84.81800  132.15200 1.000 89.38261  ? 292 ARG B CB  1 
ATOM   3960 N N   . LYS B 1 286 ? 103.83400 82.22300  130.36900 1.000 99.98291  ? 293 LYS B N   1 
ATOM   3961 C CA  . LYS B 1 286 ? 103.40400 80.84900  130.12600 1.000 99.32400  ? 293 LYS B CA  1 
ATOM   3962 C C   . LYS B 1 286 ? 104.55500 79.94900  129.69600 1.000 99.31451  ? 293 LYS B C   1 
ATOM   3963 O O   . LYS B 1 286 ? 104.49400 78.73200  129.90100 1.000 101.65433 ? 293 LYS B O   1 
ATOM   3964 C CB  . LYS B 1 286 ? 102.29600 80.82200  129.07400 1.000 98.03284  ? 293 LYS B CB  1 
ATOM   3965 N N   . MET B 1 287 ? 105.60500 80.51300  129.09900 1.000 96.05096  ? 294 MET B N   1 
ATOM   3966 C CA  . MET B 1 287 ? 106.79200 79.72200  128.79400 1.000 95.53445  ? 294 MET B CA  1 
ATOM   3967 C C   . MET B 1 287 ? 107.63700 79.40500  130.02100 1.000 98.31094  ? 294 MET B C   1 
ATOM   3968 O O   . MET B 1 287 ? 108.60100 78.64200  129.89900 1.000 99.93056  ? 294 MET B O   1 
ATOM   3969 C CB  . MET B 1 287 ? 107.65200 80.44400  127.75600 1.000 95.74783  ? 294 MET B CB  1 
ATOM   3970 N N   . ASP B 1 288 ? 107.31500 79.96600  131.18300 1.000 100.75406 ? 295 ASP B N   1 
ATOM   3971 C CA  . ASP B 1 288 ? 108.08700 79.70200  132.39500 1.000 101.47542 ? 295 ASP B CA  1 
ATOM   3972 C C   . ASP B 1 288 ? 107.99600 78.23500  132.80100 1.000 101.00466 ? 295 ASP B C   1 
ATOM   3973 O O   . ASP B 1 288 ? 106.90700 77.66600  132.86600 1.000 100.05560 ? 295 ASP B O   1 
ATOM   3974 C CB  . ASP B 1 288 ? 107.61300 80.59300  133.54400 1.000 99.02919  ? 295 ASP B CB  1 
HETATM 3975 C C1  . EIC C 2 .   ? 116.03100 92.98500  100.17500 1.000 54.81116  ? 401 EIC A C1  1 
HETATM 3976 C C2  . EIC C 2 .   ? 115.84800 93.96100  101.32100 1.000 51.67922  ? 401 EIC A C2  1 
HETATM 3977 C C3  . EIC C 2 .   ? 114.67200 93.63900  102.22900 1.000 52.91951  ? 401 EIC A C3  1 
HETATM 3978 C C4  . EIC C 2 .   ? 114.52900 94.60700  103.38900 1.000 48.55105  ? 401 EIC A C4  1 
HETATM 3979 C C5  . EIC C 2 .   ? 114.21600 96.03200  102.98400 1.000 43.62671  ? 401 EIC A C5  1 
HETATM 3980 C C6  . EIC C 2 .   ? 113.98200 96.96600  104.15400 1.000 44.96678  ? 401 EIC A C6  1 
HETATM 3981 C C7  . EIC C 2 .   ? 112.90900 96.48700  105.11200 1.000 50.53743  ? 401 EIC A C7  1 
HETATM 3982 C C8  . EIC C 2 .   ? 113.43700 95.98400  106.45100 1.000 46.49003  ? 401 EIC A C8  1 
HETATM 3983 C C9  . EIC C 2 .   ? 113.35800 97.00600  107.53500 1.000 42.21860  ? 401 EIC A C9  1 
HETATM 3984 C C10 . EIC C 2 .   ? 112.58800 96.93000  108.59700 1.000 41.87588  ? 401 EIC A C10 1 
HETATM 3985 C C11 . EIC C 2 .   ? 111.64100 95.82000  108.93100 1.000 40.93893  ? 401 EIC A C11 1 
HETATM 3986 C C12 . EIC C 2 .   ? 111.22600 95.87000  110.36800 1.000 47.61198  ? 401 EIC A C12 1 
HETATM 3987 C C13 . EIC C 2 .   ? 111.45400 94.95500  111.28200 1.000 50.59374  ? 401 EIC A C13 1 
HETATM 3988 C C14 . EIC C 2 .   ? 112.19600 93.67700  111.07100 1.000 49.09874  ? 401 EIC A C14 1 
HETATM 3989 C C15 . EIC C 2 .   ? 112.93500 93.21100  112.31600 1.000 42.30455  ? 401 EIC A C15 1 
HETATM 3990 C C16 . EIC C 2 .   ? 113.83200 92.01200  112.07900 1.000 45.53489  ? 401 EIC A C16 1 
HETATM 3991 C C17 . EIC C 2 .   ? 114.62400 91.58900  113.30100 1.000 53.81442  ? 401 EIC A C17 1 
HETATM 3992 C C18 . EIC C 2 .   ? 115.67200 90.54400  112.99400 1.000 49.98110  ? 401 EIC A C18 1 
HETATM 3993 O O1  . EIC C 2 .   ? 115.49100 91.86400  100.26200 1.000 55.68436  ? 401 EIC A O1  1 
HETATM 3994 O O2  . EIC C 2 .   ? 116.72000 93.36800  99.19900  1.000 57.06298  ? 401 EIC A O2  1 
HETATM 3995 K K   . K   D 3 .   ? 106.49600 106.49700 98.04100  1.000 20.56621  ? 402 K   A K   1 
HETATM 3996 K K   . K   E 3 .   ? 106.49600 106.49600 104.22400 1.000 26.69094  ? 403 K   A K   1 
HETATM 3997 C C1  . EIC F 2 .   ? 96.96100  120.00700 100.17500 1.000 54.78548  ? 401 EIC B C1  1 
HETATM 3998 C C2  . EIC F 2 .   ? 97.14400  119.03100 101.32100 1.000 51.68925  ? 401 EIC B C2  1 
HETATM 3999 C C3  . EIC F 2 .   ? 98.32000  119.35300 102.22900 1.000 52.99779  ? 401 EIC B C3  1 
HETATM 4000 C C4  . EIC F 2 .   ? 98.46300  118.38500 103.38900 1.000 48.38712  ? 401 EIC B C4  1 
HETATM 4001 C C5  . EIC F 2 .   ? 98.77600  116.96000 102.98400 1.000 43.37802  ? 401 EIC B C5  1 
HETATM 4002 C C6  . EIC F 2 .   ? 99.01000  116.02600 104.15400 1.000 45.07467  ? 401 EIC B C6  1 
HETATM 4003 C C7  . EIC F 2 .   ? 100.08300 116.50500 105.11200 1.000 50.53731  ? 401 EIC B C7  1 
HETATM 4004 C C8  . EIC F 2 .   ? 99.55500  117.00800 106.45100 1.000 46.18765  ? 401 EIC B C8  1 
HETATM 4005 C C9  . EIC F 2 .   ? 99.63400  115.98600 107.53500 1.000 41.89975  ? 401 EIC B C9  1 
HETATM 4006 C C10 . EIC F 2 .   ? 100.40400 116.06200 108.59700 1.000 41.52997  ? 401 EIC B C10 1 
HETATM 4007 C C11 . EIC F 2 .   ? 101.35100 117.17200 108.93100 1.000 40.68450  ? 401 EIC B C11 1 
HETATM 4008 C C12 . EIC F 2 .   ? 101.76600 117.12200 110.36700 1.000 47.47781  ? 401 EIC B C12 1 
HETATM 4009 C C13 . EIC F 2 .   ? 101.53800 118.03700 111.28200 1.000 50.33452  ? 401 EIC B C13 1 
HETATM 4010 C C14 . EIC F 2 .   ? 100.79600 119.31500 111.07100 1.000 48.99252  ? 401 EIC B C14 1 
HETATM 4011 C C15 . EIC F 2 .   ? 100.05700 119.78100 112.31600 1.000 41.65519  ? 401 EIC B C15 1 
HETATM 4012 C C16 . EIC F 2 .   ? 99.16000  120.98000 112.07900 1.000 45.28491  ? 401 EIC B C16 1 
HETATM 4013 C C17 . EIC F 2 .   ? 98.36800  121.40300 113.30100 1.000 53.50901  ? 401 EIC B C17 1 
HETATM 4014 C C18 . EIC F 2 .   ? 97.32000  122.44800 112.99400 1.000 50.01503  ? 401 EIC B C18 1 
HETATM 4015 O O1  . EIC F 2 .   ? 97.50100  121.12800 100.26200 1.000 55.51747  ? 401 EIC B O1  1 
HETATM 4016 O O2  . EIC F 2 .   ? 96.27200  119.62400 99.19900  1.000 57.04667  ? 401 EIC B O2  1 
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