data_8PWI
# 
_entry.id   8PWI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8PWI         pdb_00008pwi 10.2210/pdb8pwi/pdb 
WWPDB D_1292131770 ?            ?                   
# 
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 2025-02-05 ? 
2 'Structure model' 1 1 2025-04-23 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8PWI 
_pdbx_database_status.recvd_initial_deposition_date   2023-07-20 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8PWQ unspecified 
PDB . 8PWG unspecified 
PDB . 8PWJ unspecified 
PDB . 8PWP unspecified 
PDB . 7Q88 unspecified 
PDB . 7PNC unspecified 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
4 richard.neutze@gu.se Richard Neutze  ? 'principal investigator/group leader' 0000-0003-0986-6153 
5 gisela.branden@gu.se Gisela  Branden ? 'principal investigator/group leader' 0000-0001-5615-7187 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bosman, R.'   1 0000-0002-9939-602X 
'Ortolani, G.' 2 0000-0001-6373-9919 
'Branden, G.'  3 0000-0001-5615-7187 
'Neutze, R.'   4 0000-0003-0986-6153 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3460 
_citation.page_last                 3460 
_citation.title                     
'Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58263-x 
_citation.pdbx_database_id_PubMed   40216733 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Bosman, R.'         1  ?                   
primary 'Ortolani, G.'       2  0000-0001-6373-9919 
primary 'Ghosh, S.'          3  ?                   
primary 'James, D.'          4  0000-0002-8348-6661 
primary 'Norder, P.'         5  0000-0002-7193-640X 
primary 'Hammarin, G.'       6  0000-0001-5037-6039 
primary 'Ulfarsdottir, T.B.' 7  ?                   
primary 'Ostojic, L.'        8  ?                   
primary 'Weinert, T.'        9  0000-0002-0339-3722 
primary 'Dworkowski, F.'     10 0000-0001-5004-8684 
primary 'Tomizaki, T.'       11 0000-0003-0011-0990 
primary 'Standfuss, J.'      12 0000-0001-8825-386X 
primary 'Branden, G.'        13 0000-0001-5615-7187 
primary 'Neutze, R.'         14 0000-0003-0986-6153 
# 
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 'Sensory rhodopsin-2' 26666.137 1  ? ? ? ? 
2 non-polymer syn RETINAL               284.436   1  ? ? ? ? 
3 non-polymer nat 'CHLORIDE ION'        35.453    1  ? ? ? ? 
4 water       nat water                 18.015    15 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Sensory rhodopsin II,SR-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MVGLTTLFWLGAIGMLVGTLAFAWAGRDAGSGERRYYVTLVGISGIAAVAYVVMALGVGWVPVAERTVFAPRYIDWILTT
PLIVYFLGLLAGLDSREFGIVITLNTVVMLAGFAGAMVPGIERYALFGMGAVAFLGLVYYLVGPMTESASQRSSGIKSLY
VRLRNLTVILWAIYPFIWLLGPPGVALLTPTVDVALIVYLDLVTKVGFGFIALDAAATLRAEHGESLAGVDTDAPAVADE
NSHHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVGLTTLFWLGAIGMLVGTLAFAWAGRDAGSGERRYYVTLVGISGIAAVAYVVMALGVGWVPVAERTVFAPRYIDWILTT
PLIVYFLGLLAGLDSREFGIVITLNTVVMLAGFAGAMVPGIERYALFGMGAVAFLGLVYYLVGPMTESASQRSSGIKSLY
VRLRNLTVILWAIYPFIWLLGPPGVALLTPTVDVALIVYLDLVTKVGFGFIALDAAATLRAEHGESLAGVDTDAPAVADE
NSHHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 RETINAL        RET 
3 'CHLORIDE ION' CL  
4 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   VAL n 
1 3   GLY n 
1 4   LEU n 
1 5   THR n 
1 6   THR n 
1 7   LEU n 
1 8   PHE n 
1 9   TRP n 
1 10  LEU n 
1 11  GLY n 
1 12  ALA n 
1 13  ILE n 
1 14  GLY n 
1 15  MET n 
1 16  LEU n 
1 17  VAL n 
1 18  GLY n 
1 19  THR n 
1 20  LEU n 
1 21  ALA n 
1 22  PHE n 
1 23  ALA n 
1 24  TRP n 
1 25  ALA n 
1 26  GLY n 
1 27  ARG n 
1 28  ASP n 
1 29  ALA n 
1 30  GLY n 
1 31  SER n 
1 32  GLY n 
1 33  GLU n 
1 34  ARG n 
1 35  ARG n 
1 36  TYR n 
1 37  TYR n 
1 38  VAL n 
1 39  THR n 
1 40  LEU n 
1 41  VAL n 
1 42  GLY n 
1 43  ILE n 
1 44  SER n 
1 45  GLY n 
1 46  ILE n 
1 47  ALA n 
1 48  ALA n 
1 49  VAL n 
1 50  ALA n 
1 51  TYR n 
1 52  VAL n 
1 53  VAL n 
1 54  MET n 
1 55  ALA n 
1 56  LEU n 
1 57  GLY n 
1 58  VAL n 
1 59  GLY n 
1 60  TRP n 
1 61  VAL n 
1 62  PRO n 
1 63  VAL n 
1 64  ALA n 
1 65  GLU n 
1 66  ARG n 
1 67  THR n 
1 68  VAL n 
1 69  PHE n 
1 70  ALA n 
1 71  PRO n 
1 72  ARG n 
1 73  TYR n 
1 74  ILE n 
1 75  ASP n 
1 76  TRP n 
1 77  ILE n 
1 78  LEU n 
1 79  THR n 
1 80  THR n 
1 81  PRO n 
1 82  LEU n 
1 83  ILE n 
1 84  VAL n 
1 85  TYR n 
1 86  PHE n 
1 87  LEU n 
1 88  GLY n 
1 89  LEU n 
1 90  LEU n 
1 91  ALA n 
1 92  GLY n 
1 93  LEU n 
1 94  ASP n 
1 95  SER n 
1 96  ARG n 
1 97  GLU n 
1 98  PHE n 
1 99  GLY n 
1 100 ILE n 
1 101 VAL n 
1 102 ILE n 
1 103 THR n 
1 104 LEU n 
1 105 ASN n 
1 106 THR n 
1 107 VAL n 
1 108 VAL n 
1 109 MET n 
1 110 LEU n 
1 111 ALA n 
1 112 GLY n 
1 113 PHE n 
1 114 ALA n 
1 115 GLY n 
1 116 ALA n 
1 117 MET n 
1 118 VAL n 
1 119 PRO n 
1 120 GLY n 
1 121 ILE n 
1 122 GLU n 
1 123 ARG n 
1 124 TYR n 
1 125 ALA n 
1 126 LEU n 
1 127 PHE n 
1 128 GLY n 
1 129 MET n 
1 130 GLY n 
1 131 ALA n 
1 132 VAL n 
1 133 ALA n 
1 134 PHE n 
1 135 LEU n 
1 136 GLY n 
1 137 LEU n 
1 138 VAL n 
1 139 TYR n 
1 140 TYR n 
1 141 LEU n 
1 142 VAL n 
1 143 GLY n 
1 144 PRO n 
1 145 MET n 
1 146 THR n 
1 147 GLU n 
1 148 SER n 
1 149 ALA n 
1 150 SER n 
1 151 GLN n 
1 152 ARG n 
1 153 SER n 
1 154 SER n 
1 155 GLY n 
1 156 ILE n 
1 157 LYS n 
1 158 SER n 
1 159 LEU n 
1 160 TYR n 
1 161 VAL n 
1 162 ARG n 
1 163 LEU n 
1 164 ARG n 
1 165 ASN n 
1 166 LEU n 
1 167 THR n 
1 168 VAL n 
1 169 ILE n 
1 170 LEU n 
1 171 TRP n 
1 172 ALA n 
1 173 ILE n 
1 174 TYR n 
1 175 PRO n 
1 176 PHE n 
1 177 ILE n 
1 178 TRP n 
1 179 LEU n 
1 180 LEU n 
1 181 GLY n 
1 182 PRO n 
1 183 PRO n 
1 184 GLY n 
1 185 VAL n 
1 186 ALA n 
1 187 LEU n 
1 188 LEU n 
1 189 THR n 
1 190 PRO n 
1 191 THR n 
1 192 VAL n 
1 193 ASP n 
1 194 VAL n 
1 195 ALA n 
1 196 LEU n 
1 197 ILE n 
1 198 VAL n 
1 199 TYR n 
1 200 LEU n 
1 201 ASP n 
1 202 LEU n 
1 203 VAL n 
1 204 THR n 
1 205 LYS n 
1 206 VAL n 
1 207 GLY n 
1 208 PHE n 
1 209 GLY n 
1 210 PHE n 
1 211 ILE n 
1 212 ALA n 
1 213 LEU n 
1 214 ASP n 
1 215 ALA n 
1 216 ALA n 
1 217 ALA n 
1 218 THR n 
1 219 LEU n 
1 220 ARG n 
1 221 ALA n 
1 222 GLU n 
1 223 HIS n 
1 224 GLY n 
1 225 GLU n 
1 226 SER n 
1 227 LEU n 
1 228 ALA n 
1 229 GLY n 
1 230 VAL n 
1 231 ASP n 
1 232 THR n 
1 233 ASP n 
1 234 ALA n 
1 235 PRO n 
1 236 ALA n 
1 237 VAL n 
1 238 ALA n 
1 239 ASP n 
1 240 GLU n 
1 241 ASN n 
1 242 SER n 
1 243 HIS n 
1 244 HIS n 
1 245 HIS n 
1 246 HIS n 
1 247 HIS n 
1 248 HIS n 
1 249 HIS 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                   249 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'sop2, sopII' 
_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      'Natronomonas pharaonis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2257 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CL  non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'          35.453  
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
RET non-polymer         . RETINAL         ? 'C20 H28 O'      284.436 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  MET 15  15  15  MET MET A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  TRP 24  24  24  TRP TRP A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ARG 27  27  ?   ?   ?   A . n 
A 1 28  ASP 28  28  ?   ?   ?   A . n 
A 1 29  ALA 29  29  ?   ?   ?   A . n 
A 1 30  GLY 30  30  ?   ?   ?   A . n 
A 1 31  SER 31  31  ?   ?   ?   A . n 
A 1 32  GLY 32  32  ?   ?   ?   A . n 
A 1 33  GLU 33  33  ?   ?   ?   A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  MET 54  54  54  MET MET A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  TRP 60  60  60  TRP TRP A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  PHE 69  69  69  PHE PHE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  ARG 72  72  72  ARG ARG A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  TRP 76  76  76  TRP TRP A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  PHE 86  86  86  PHE PHE A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  SER 95  95  95  SER SER A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 PHE 113 113 113 PHE PHE A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 TYR 124 124 124 TYR TYR A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 MET 129 129 129 MET MET A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 TYR 139 139 139 TYR TYR A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 PRO 144 144 144 PRO PRO A . n 
A 1 145 MET 145 145 145 MET MET A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 TYR 160 160 160 TYR TYR A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ARG 162 162 162 ARG ARG A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 TRP 171 171 171 TRP TRP A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 TYR 174 174 174 TYR TYR A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 TRP 178 178 178 TRP TRP A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 PRO 183 183 183 PRO PRO A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 ASP 193 193 193 ASP ASP A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ALA 217 217 ?   ?   ?   A . n 
A 1 218 THR 218 218 ?   ?   ?   A . n 
A 1 219 LEU 219 219 ?   ?   ?   A . n 
A 1 220 ARG 220 220 ?   ?   ?   A . n 
A 1 221 ALA 221 221 ?   ?   ?   A . n 
A 1 222 GLU 222 222 ?   ?   ?   A . n 
A 1 223 HIS 223 223 ?   ?   ?   A . n 
A 1 224 GLY 224 224 ?   ?   ?   A . n 
A 1 225 GLU 225 225 ?   ?   ?   A . n 
A 1 226 SER 226 226 ?   ?   ?   A . n 
A 1 227 LEU 227 227 ?   ?   ?   A . n 
A 1 228 ALA 228 228 ?   ?   ?   A . n 
A 1 229 GLY 229 229 ?   ?   ?   A . n 
A 1 230 VAL 230 230 ?   ?   ?   A . n 
A 1 231 ASP 231 231 ?   ?   ?   A . n 
A 1 232 THR 232 232 ?   ?   ?   A . n 
A 1 233 ASP 233 233 ?   ?   ?   A . n 
A 1 234 ALA 234 234 ?   ?   ?   A . n 
A 1 235 PRO 235 235 ?   ?   ?   A . n 
A 1 236 ALA 236 236 ?   ?   ?   A . n 
A 1 237 VAL 237 237 ?   ?   ?   A . n 
A 1 238 ALA 238 238 ?   ?   ?   A . n 
A 1 239 ASP 239 239 ?   ?   ?   A . n 
A 1 240 GLU 240 240 ?   ?   ?   A . n 
A 1 241 ASN 241 241 ?   ?   ?   A . n 
A 1 242 SER 242 242 ?   ?   ?   A . n 
A 1 243 HIS 243 243 ?   ?   ?   A . n 
A 1 244 HIS 244 244 ?   ?   ?   A . n 
A 1 245 HIS 245 245 ?   ?   ?   A . n 
A 1 246 HIS 246 246 ?   ?   ?   A . n 
A 1 247 HIS 247 247 ?   ?   ?   A . n 
A 1 248 HIS 248 248 ?   ?   ?   A . n 
A 1 249 HIS 249 249 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 RET ? ? RET ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 RET 1  301 300 RET RET A . 
C 3 CL  1  302 1   CL  CL  A . 
D 4 HOH 1  401 17  HOH HOH A . 
D 4 HOH 2  402 5   HOH HOH A . 
D 4 HOH 3  403 2   HOH HOH A . 
D 4 HOH 4  404 7   HOH HOH A . 
D 4 HOH 5  405 19  HOH HOH A . 
D 4 HOH 6  406 1   HOH HOH A . 
D 4 HOH 7  407 4   HOH HOH A . 
D 4 HOH 8  408 8   HOH HOH A . 
D 4 HOH 9  409 25  HOH HOH A . 
D 4 HOH 10 410 9   HOH HOH A . 
D 4 HOH 11 411 26  HOH HOH A . 
D 4 HOH 12 412 33  HOH HOH A . 
D 4 HOH 13 413 38  HOH HOH A . 
D 4 HOH 14 414 37  HOH HOH A . 
D 4 HOH 15 415 49  HOH HOH A . 
# 
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 GLU 97 ? CG  ? A GLU 97 CG  
2 1 Y 1 A GLU 97 ? CD  ? A GLU 97 CD  
3 1 Y 1 A GLU 97 ? OE1 ? A GLU 97 OE1 
4 1 Y 1 A GLU 97 ? OE2 ? A GLU 97 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8PWI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     89.750 
_cell.length_a_esd                 ? 
_cell.length_b                     131.700 
_cell.length_b_esd                 ? 
_cell.length_c                     51.000 
_cell.length_c_esd                 ? 
_cell.volume                       602823.825 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8PWI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8PWI 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.47 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'LIPIDIC CUBIC PHASE' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'CaCl2 150mM, Glycine 100 mM, 38% (v/v) PEG 400, pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296.0 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-05-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000342 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0000342 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          37.06 
_reflns.entry_id                                       8PWI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.96 
_reflns.d_resolution_low                               44.9 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     4429 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.53 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                72.06 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.22 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.983 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.50 
_reflns_shell.d_res_low                                     44.0 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             12660 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.983 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.18 
_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                                 8PWI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.96 
_refine.ls_d_res_low                             44.88 
_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                     4429 
_refine.ls_number_reflns_R_free                  617 
_refine.ls_number_reflns_R_work                  12043 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    57.09 
_refine.ls_percent_reflns_R_free                 4.87 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2462 
_refine.ls_R_factor_R_free                       0.2763 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2446 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 41.7450 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3019 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.96 
_refine_hist.d_res_low                        44.88 
_refine_hist.number_atoms_solvent             15 
_refine_hist.number_atoms_total               1611 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1575 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         21 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0218  ? 3272 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.7937  ? 4482 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0753  ? 542  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0140  ? 534  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.7323 ? 1086 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.96 2.16  . . 1   25   0.48  . . . . 0.4405 . . . . . . . . . . . 0.1548 
'X-RAY DIFFRACTION' 2.16 2.47  . . 58  1421 27.17 . . . . 0.4084 . . . . . . . . . . . 0.4179 
'X-RAY DIFFRACTION' 2.47 3.11  . . 280 5150 98.30 . . . . 0.2876 . . . . . . . . . . . 0.3388 
'X-RAY DIFFRACTION' 3.11 44.88 . . 278 5447 99.93 . . . . 0.2123 . . . . . . . . . . . 0.2411 
# 
_struct.entry_id                     8PWI 
_struct.title                        
'Light structure of sensory rhodopsin-II solved by serial millisecond crystallography 60-90 milliseconds time-bin' 
_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        8PWI 
_struct_keywords.text            
;SRII, serial millisecond crystallography, sensory rhodopsin, sensory rhodopsin II, SMX, SSX, Time-resolved crystallography, TRX, SIGNALING PROTEIN
;
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BACS2_NATPH 
_struct_ref.pdbx_db_accession          P42196 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MVGLTTLFWLGAIGMLVGTLAFAWAGRDAGSGERRYYVTLVGISGIAAVAYVVMALGVGWVPVAERTVFAPRYIDWILTT
PLIVYFLGLLAGLDSREFGIVITLNTVVMLAGFAGAMVPGIERYALFGMGAVAFLGLVYYLVGPMTESASQRSSGIKSLY
VRLRNLTVILWAIYPFIWLLGPPGVALLTPTVDVALIVYLDLVTKVGFGFIALDAAATLRAEHGESLAGVDTDAPAVAD
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8PWI 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 239 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P42196 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  239 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       239 
# 
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 8PWI GLU A 240 ? UNP P42196 ? ? 'expression tag' 240 1  
1 8PWI ASN A 241 ? UNP P42196 ? ? 'expression tag' 241 2  
1 8PWI SER A 242 ? UNP P42196 ? ? 'expression tag' 242 3  
1 8PWI HIS A 243 ? UNP P42196 ? ? 'expression tag' 243 4  
1 8PWI HIS A 244 ? UNP P42196 ? ? 'expression tag' 244 5  
1 8PWI HIS A 245 ? UNP P42196 ? ? 'expression tag' 245 6  
1 8PWI HIS A 246 ? UNP P42196 ? ? 'expression tag' 246 7  
1 8PWI HIS A 247 ? UNP P42196 ? ? 'expression tag' 247 8  
1 8PWI HIS A 248 ? UNP P42196 ? ? 'expression tag' 248 9  
1 8PWI HIS A 249 ? UNP P42196 ? ? 'expression tag' 249 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 910  ? 
1 MORE         -14  ? 
1 'SSA (A^2)'  9510 ? 
# 
_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 3   ? GLY A 26  ? GLY A 3   GLY A 26  1 ? 24 
HELX_P HELX_P2 AA2 ARG A 35  ? LEU A 56  ? ARG A 35  LEU A 56  1 ? 22 
HELX_P HELX_P3 AA3 ALA A 70  ? GLY A 92  ? ALA A 70  GLY A 92  1 ? 23 
HELX_P HELX_P4 AA4 ASP A 94  ? VAL A 118 ? ASP A 94  VAL A 118 1 ? 25 
HELX_P HELX_P5 AA5 ILE A 121 ? GLY A 143 ? ILE A 121 GLY A 143 1 ? 23 
HELX_P HELX_P6 AA6 GLY A 143 ? SER A 150 ? GLY A 143 SER A 150 1 ? 8  
HELX_P HELX_P7 AA7 SER A 153 ? ALA A 172 ? SER A 153 ALA A 172 1 ? 20 
HELX_P HELX_P8 AA8 ILE A 173 ? GLY A 181 ? ILE A 173 GLY A 181 1 ? 9  
HELX_P HELX_P9 AA9 THR A 189 ? ALA A 216 ? THR A 189 ALA A 216 1 ? 28 
# 
_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 
covale1 covale one ? A LYS 205 NZ A ? ? 1_555 B RET . C15 A ? A LYS 205 A RET 301 1_555 ? ? ? ? ? ? ? 1.435 ? ? 
covale2 covale one ? A LYS 205 NZ B ? ? 1_555 B RET . C15 B ? A LYS 205 A RET 301 1_555 ? ? ? ? ? ? ? 1.268 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 RET B . A LYS A 205 A RET A 301 ? 1_555 LYS A 205 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like 
2 RET B . B LYS A 205 B RET A 301 ? 1_555 LYS A 205 ? 1_555 C15 NZ LYS 1 RET Retinoylation Lipid/lipid-like 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TRP A 60 ? VAL A 63 ? TRP A 60 VAL A 63 
AA1 2 ARG A 66 ? PHE A 69 ? ARG A 66 PHE A 69 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   VAL 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    61 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    VAL 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     61 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   VAL 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    68 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    VAL 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     68 
# 
_pdbx_entry_details.entry_id                   8PWI 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG  A TYR 73  ? A CD1 A TYR 73  ? ? 2.236 1.387 0.849  0.013 N 
2 1 CD1 A TYR 73  ? ? CE1 A TYR 73  ? A 0.895 1.389 -0.494 0.015 N 
3 1 CB  A PHE 176 ? B CG  A PHE 176 ? B 1.404 1.509 -0.105 0.017 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA  A LEU 7   ? B CB  A LEU 7   ? B CG  A LEU 7   ? B 98.88  115.30 -16.42 2.30 N 
2 1 CD1 A TYR 73  ? ? CG  A TYR 73  ? A CD2 A TYR 73  ? A 110.30 117.90 -7.60  1.10 N 
3 1 CB  A TYR 73  ? A CG  A TYR 73  ? A CD1 A TYR 73  ? ? 128.73 121.00 7.73   0.60 N 
4 1 CG  A TYR 73  ? A CD1 A TYR 73  ? ? CE1 A TYR 73  ? A 90.22  121.30 -31.08 0.80 N 
5 1 CD1 A TYR 73  ? ? CE1 A TYR 73  ? A CZ  A TYR 73  ? A 156.77 119.80 36.97  0.90 N 
6 1 CA  A MET 129 ? B CB  A MET 129 ? B CG  A MET 129 ? B 98.49  113.30 -14.81 1.70 N 
7 1 CA  A LEU 159 ? B CB  A LEU 159 ? B CG  A LEU 159 ? B 131.39 115.30 16.09  2.30 N 
8 1 CA  A LEU 200 ? B CB  A LEU 200 ? B CG  A LEU 200 ? B 132.06 115.30 16.76  2.30 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 LEU A 20  ? B -37.62 -84.25  
2  1 ALA A 21  ? B -34.77 -37.41  
3  1 LEU A 56  ? B -67.92 40.05   
4  1 ALA A 64  ? A 55.36  -106.96 
5  1 ALA A 64  ? B 60.54  -117.05 
6  1 ASP A 75  ? B -21.58 -69.34  
7  1 LEU A 87  ? B -58.45 -82.77  
8  1 PHE A 113 ? B -28.83 -77.76  
9  1 PRO A 144 ? B -12.13 -62.35  
10 1 GLU A 147 ? B -29.31 -76.58  
11 1 SER A 148 ? B -47.66 -19.81  
12 1 SER A 150 ? B -55.92 19.31   
13 1 ARG A 162 ? B -63.11 -72.08  
14 1 LEU A 166 ? B -39.89 -72.39  
15 1 LEU A 187 ? B -48.76 -97.81  
16 1 LEU A 188 ? B -29.52 127.53  
17 1 ASP A 214 ? B -29.95 -52.80  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 LEU A 10  ? B GLY A 11  ? B 142.91 
2 1 THR A 19  ? B LEU A 20  ? B 149.93 
3 1 VAL A 185 ? B ALA A 186 ? B 148.97 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     72 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    A 
_pdbx_validate_planes.rmsd            0.094 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
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 1   ? A MET 1   
2  1 Y 1 A ARG 27  ? A ARG 27  
3  1 Y 1 A ASP 28  ? A ASP 28  
4  1 Y 1 A ALA 29  ? A ALA 29  
5  1 Y 1 A GLY 30  ? A GLY 30  
6  1 Y 1 A SER 31  ? A SER 31  
7  1 Y 1 A GLY 32  ? A GLY 32  
8  1 Y 1 A GLU 33  ? A GLU 33  
9  1 Y 1 A ALA 217 ? A ALA 217 
10 1 Y 1 A THR 218 ? A THR 218 
11 1 Y 1 A LEU 219 ? A LEU 219 
12 1 Y 1 A ARG 220 ? A ARG 220 
13 1 Y 1 A ALA 221 ? A ALA 221 
14 1 Y 1 A GLU 222 ? A GLU 222 
15 1 Y 1 A HIS 223 ? A HIS 223 
16 1 Y 1 A GLY 224 ? A GLY 224 
17 1 Y 1 A GLU 225 ? A GLU 225 
18 1 Y 1 A SER 226 ? A SER 226 
19 1 Y 1 A LEU 227 ? A LEU 227 
20 1 Y 1 A ALA 228 ? A ALA 228 
21 1 Y 1 A GLY 229 ? A GLY 229 
22 1 Y 1 A VAL 230 ? A VAL 230 
23 1 Y 1 A ASP 231 ? A ASP 231 
24 1 Y 1 A THR 232 ? A THR 232 
25 1 Y 1 A ASP 233 ? A ASP 233 
26 1 Y 1 A ALA 234 ? A ALA 234 
27 1 Y 1 A PRO 235 ? A PRO 235 
28 1 Y 1 A ALA 236 ? A ALA 236 
29 1 Y 1 A VAL 237 ? A VAL 237 
30 1 Y 1 A ALA 238 ? A ALA 238 
31 1 Y 1 A ASP 239 ? A ASP 239 
32 1 Y 1 A GLU 240 ? A GLU 240 
33 1 Y 1 A ASN 241 ? A ASN 241 
34 1 Y 1 A SER 242 ? A SER 242 
35 1 Y 1 A HIS 243 ? A HIS 243 
36 1 Y 1 A HIS 244 ? A HIS 244 
37 1 Y 1 A HIS 245 ? A HIS 245 
38 1 Y 1 A HIS 246 ? A HIS 246 
39 1 Y 1 A HIS 247 ? A HIS 247 
40 1 Y 1 A HIS 248 ? A HIS 248 
41 1 Y 1 A HIS 249 ? A HIS 249 
# 
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  
CL  CL   CL N N 74  
GLN N    N  N N 75  
GLN CA   C  N S 76  
GLN C    C  N N 77  
GLN O    O  N N 78  
GLN CB   C  N N 79  
GLN CG   C  N N 80  
GLN CD   C  N N 81  
GLN OE1  O  N N 82  
GLN NE2  N  N N 83  
GLN OXT  O  N N 84  
GLN H    H  N N 85  
GLN H2   H  N N 86  
GLN HA   H  N N 87  
GLN HB2  H  N N 88  
GLN HB3  H  N N 89  
GLN HG2  H  N N 90  
GLN HG3  H  N N 91  
GLN HE21 H  N N 92  
GLN HE22 H  N N 93  
GLN HXT  H  N N 94  
GLU N    N  N N 95  
GLU CA   C  N S 96  
GLU C    C  N N 97  
GLU O    O  N N 98  
GLU CB   C  N N 99  
GLU CG   C  N N 100 
GLU CD   C  N N 101 
GLU OE1  O  N N 102 
GLU OE2  O  N N 103 
GLU OXT  O  N N 104 
GLU H    H  N N 105 
GLU H2   H  N N 106 
GLU HA   H  N N 107 
GLU HB2  H  N N 108 
GLU HB3  H  N N 109 
GLU HG2  H  N N 110 
GLU HG3  H  N N 111 
GLU HE2  H  N N 112 
GLU HXT  H  N N 113 
GLY N    N  N N 114 
GLY CA   C  N N 115 
GLY C    C  N N 116 
GLY O    O  N N 117 
GLY OXT  O  N N 118 
GLY H    H  N N 119 
GLY H2   H  N N 120 
GLY HA2  H  N N 121 
GLY HA3  H  N N 122 
GLY HXT  H  N N 123 
HIS N    N  N N 124 
HIS CA   C  N S 125 
HIS C    C  N N 126 
HIS O    O  N N 127 
HIS CB   C  N N 128 
HIS CG   C  Y N 129 
HIS ND1  N  Y N 130 
HIS CD2  C  Y N 131 
HIS CE1  C  Y N 132 
HIS NE2  N  Y N 133 
HIS OXT  O  N N 134 
HIS H    H  N N 135 
HIS H2   H  N N 136 
HIS HA   H  N N 137 
HIS HB2  H  N N 138 
HIS HB3  H  N N 139 
HIS HD1  H  N N 140 
HIS HD2  H  N N 141 
HIS HE1  H  N N 142 
HIS HE2  H  N N 143 
HIS HXT  H  N N 144 
HOH O    O  N N 145 
HOH H1   H  N N 146 
HOH H2   H  N N 147 
ILE N    N  N N 148 
ILE CA   C  N S 149 
ILE C    C  N N 150 
ILE O    O  N N 151 
ILE CB   C  N S 152 
ILE CG1  C  N N 153 
ILE CG2  C  N N 154 
ILE CD1  C  N N 155 
ILE OXT  O  N N 156 
ILE H    H  N N 157 
ILE H2   H  N N 158 
ILE HA   H  N N 159 
ILE HB   H  N N 160 
ILE HG12 H  N N 161 
ILE HG13 H  N N 162 
ILE HG21 H  N N 163 
ILE HG22 H  N N 164 
ILE HG23 H  N N 165 
ILE HD11 H  N N 166 
ILE HD12 H  N N 167 
ILE HD13 H  N N 168 
ILE HXT  H  N N 169 
LEU N    N  N N 170 
LEU CA   C  N S 171 
LEU C    C  N N 172 
LEU O    O  N N 173 
LEU CB   C  N N 174 
LEU CG   C  N N 175 
LEU CD1  C  N N 176 
LEU CD2  C  N N 177 
LEU OXT  O  N N 178 
LEU H    H  N N 179 
LEU H2   H  N N 180 
LEU HA   H  N N 181 
LEU HB2  H  N N 182 
LEU HB3  H  N N 183 
LEU HG   H  N N 184 
LEU HD11 H  N N 185 
LEU HD12 H  N N 186 
LEU HD13 H  N N 187 
LEU HD21 H  N N 188 
LEU HD22 H  N N 189 
LEU HD23 H  N N 190 
LEU HXT  H  N N 191 
LYS N    N  N N 192 
LYS CA   C  N S 193 
LYS C    C  N N 194 
LYS O    O  N N 195 
LYS CB   C  N N 196 
LYS CG   C  N N 197 
LYS CD   C  N N 198 
LYS CE   C  N N 199 
LYS NZ   N  N N 200 
LYS OXT  O  N N 201 
LYS H    H  N N 202 
LYS H2   H  N N 203 
LYS HA   H  N N 204 
LYS HB2  H  N N 205 
LYS HB3  H  N N 206 
LYS HG2  H  N N 207 
LYS HG3  H  N N 208 
LYS HD2  H  N N 209 
LYS HD3  H  N N 210 
LYS HE2  H  N N 211 
LYS HE3  H  N N 212 
LYS HZ1  H  N N 213 
LYS HZ2  H  N N 214 
LYS HZ3  H  N N 215 
LYS HXT  H  N N 216 
MET N    N  N N 217 
MET CA   C  N S 218 
MET C    C  N N 219 
MET O    O  N N 220 
MET CB   C  N N 221 
MET CG   C  N N 222 
MET SD   S  N N 223 
MET CE   C  N N 224 
MET OXT  O  N N 225 
MET H    H  N N 226 
MET H2   H  N N 227 
MET HA   H  N N 228 
MET HB2  H  N N 229 
MET HB3  H  N N 230 
MET HG2  H  N N 231 
MET HG3  H  N N 232 
MET HE1  H  N N 233 
MET HE2  H  N N 234 
MET HE3  H  N N 235 
MET HXT  H  N N 236 
PHE N    N  N N 237 
PHE CA   C  N S 238 
PHE C    C  N N 239 
PHE O    O  N N 240 
PHE CB   C  N N 241 
PHE CG   C  Y N 242 
PHE CD1  C  Y N 243 
PHE CD2  C  Y N 244 
PHE CE1  C  Y N 245 
PHE CE2  C  Y N 246 
PHE CZ   C  Y N 247 
PHE OXT  O  N N 248 
PHE H    H  N N 249 
PHE H2   H  N N 250 
PHE HA   H  N N 251 
PHE HB2  H  N N 252 
PHE HB3  H  N N 253 
PHE HD1  H  N N 254 
PHE HD2  H  N N 255 
PHE HE1  H  N N 256 
PHE HE2  H  N N 257 
PHE HZ   H  N N 258 
PHE HXT  H  N N 259 
PRO N    N  N N 260 
PRO CA   C  N S 261 
PRO C    C  N N 262 
PRO O    O  N N 263 
PRO CB   C  N N 264 
PRO CG   C  N N 265 
PRO CD   C  N N 266 
PRO OXT  O  N N 267 
PRO H    H  N N 268 
PRO HA   H  N N 269 
PRO HB2  H  N N 270 
PRO HB3  H  N N 271 
PRO HG2  H  N N 272 
PRO HG3  H  N N 273 
PRO HD2  H  N N 274 
PRO HD3  H  N N 275 
PRO HXT  H  N N 276 
RET C1   C  N N 277 
RET C2   C  N N 278 
RET C3   C  N N 279 
RET C4   C  N N 280 
RET C5   C  N N 281 
RET C6   C  N N 282 
RET C7   C  N N 283 
RET C8   C  N N 284 
RET C9   C  N N 285 
RET C10  C  N N 286 
RET C11  C  N N 287 
RET C12  C  N N 288 
RET C13  C  N N 289 
RET C14  C  N N 290 
RET C15  C  N N 291 
RET O1   O  N N 292 
RET C16  C  N N 293 
RET C17  C  N N 294 
RET C18  C  N N 295 
RET C19  C  N N 296 
RET C20  C  N N 297 
RET H21  H  N N 298 
RET H22  H  N N 299 
RET H31  H  N N 300 
RET H32  H  N N 301 
RET H41  H  N N 302 
RET H42  H  N N 303 
RET H7   H  N N 304 
RET H8   H  N N 305 
RET H10  H  N N 306 
RET H11  H  N N 307 
RET H12  H  N N 308 
RET H14  H  N N 309 
RET H15  H  N N 310 
RET H161 H  N N 311 
RET H162 H  N N 312 
RET H163 H  N N 313 
RET H171 H  N N 314 
RET H172 H  N N 315 
RET H173 H  N N 316 
RET H181 H  N N 317 
RET H182 H  N N 318 
RET H183 H  N N 319 
RET H191 H  N N 320 
RET H192 H  N N 321 
RET H193 H  N N 322 
RET H201 H  N N 323 
RET H202 H  N N 324 
RET H203 H  N N 325 
SER N    N  N N 326 
SER CA   C  N S 327 
SER C    C  N N 328 
SER O    O  N N 329 
SER CB   C  N N 330 
SER OG   O  N N 331 
SER OXT  O  N N 332 
SER H    H  N N 333 
SER H2   H  N N 334 
SER HA   H  N N 335 
SER HB2  H  N N 336 
SER HB3  H  N N 337 
SER HG   H  N N 338 
SER HXT  H  N N 339 
THR N    N  N N 340 
THR CA   C  N S 341 
THR C    C  N N 342 
THR O    O  N N 343 
THR CB   C  N R 344 
THR OG1  O  N N 345 
THR CG2  C  N N 346 
THR OXT  O  N N 347 
THR H    H  N N 348 
THR H2   H  N N 349 
THR HA   H  N N 350 
THR HB   H  N N 351 
THR HG1  H  N N 352 
THR HG21 H  N N 353 
THR HG22 H  N N 354 
THR HG23 H  N N 355 
THR HXT  H  N N 356 
TRP N    N  N N 357 
TRP CA   C  N S 358 
TRP C    C  N N 359 
TRP O    O  N N 360 
TRP CB   C  N N 361 
TRP CG   C  Y N 362 
TRP CD1  C  Y N 363 
TRP CD2  C  Y N 364 
TRP NE1  N  Y N 365 
TRP CE2  C  Y N 366 
TRP CE3  C  Y N 367 
TRP CZ2  C  Y N 368 
TRP CZ3  C  Y N 369 
TRP CH2  C  Y N 370 
TRP OXT  O  N N 371 
TRP H    H  N N 372 
TRP H2   H  N N 373 
TRP HA   H  N N 374 
TRP HB2  H  N N 375 
TRP HB3  H  N N 376 
TRP HD1  H  N N 377 
TRP HE1  H  N N 378 
TRP HE3  H  N N 379 
TRP HZ2  H  N N 380 
TRP HZ3  H  N N 381 
TRP HH2  H  N N 382 
TRP HXT  H  N N 383 
TYR N    N  N N 384 
TYR CA   C  N S 385 
TYR C    C  N N 386 
TYR O    O  N N 387 
TYR CB   C  N N 388 
TYR CG   C  Y N 389 
TYR CD1  C  Y N 390 
TYR CD2  C  Y N 391 
TYR CE1  C  Y N 392 
TYR CE2  C  Y N 393 
TYR CZ   C  Y N 394 
TYR OH   O  N N 395 
TYR OXT  O  N N 396 
TYR H    H  N N 397 
TYR H2   H  N N 398 
TYR HA   H  N N 399 
TYR HB2  H  N N 400 
TYR HB3  H  N N 401 
TYR HD1  H  N N 402 
TYR HD2  H  N N 403 
TYR HE1  H  N N 404 
TYR HE2  H  N N 405 
TYR HH   H  N N 406 
TYR HXT  H  N N 407 
VAL N    N  N N 408 
VAL CA   C  N S 409 
VAL C    C  N N 410 
VAL O    O  N N 411 
VAL CB   C  N N 412 
VAL CG1  C  N N 413 
VAL CG2  C  N N 414 
VAL OXT  O  N N 415 
VAL H    H  N N 416 
VAL H2   H  N N 417 
VAL HA   H  N N 418 
VAL HB   H  N N 419 
VAL HG11 H  N N 420 
VAL HG12 H  N N 421 
VAL HG13 H  N N 422 
VAL HG21 H  N N 423 
VAL HG22 H  N N 424 
VAL HG23 H  N N 425 
VAL HXT  H  N N 426 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
RET C1  C2   sing N N 264 
RET C1  C6   sing N N 265 
RET C1  C16  sing N N 266 
RET C1  C17  sing N N 267 
RET C2  C3   sing N N 268 
RET C2  H21  sing N N 269 
RET C2  H22  sing N N 270 
RET C3  C4   sing N N 271 
RET C3  H31  sing N N 272 
RET C3  H32  sing N N 273 
RET C4  C5   sing N N 274 
RET C4  H41  sing N N 275 
RET C4  H42  sing N N 276 
RET C5  C6   doub N N 277 
RET C5  C18  sing N N 278 
RET C6  C7   sing N N 279 
RET C7  C8   doub N E 280 
RET C7  H7   sing N N 281 
RET C8  C9   sing N N 282 
RET C8  H8   sing N N 283 
RET C9  C10  doub N E 284 
RET C9  C19  sing N N 285 
RET C10 C11  sing N N 286 
RET C10 H10  sing N N 287 
RET C11 C12  doub N E 288 
RET C11 H11  sing N N 289 
RET C12 C13  sing N N 290 
RET C12 H12  sing N N 291 
RET C13 C14  doub N E 292 
RET C13 C20  sing N N 293 
RET C14 C15  sing N N 294 
RET C14 H14  sing N N 295 
RET C15 O1   doub N N 296 
RET C15 H15  sing N N 297 
RET C16 H161 sing N N 298 
RET C16 H162 sing N N 299 
RET C16 H163 sing N N 300 
RET C17 H171 sing N N 301 
RET C17 H172 sing N N 302 
RET C17 H173 sing N N 303 
RET C18 H181 sing N N 304 
RET C18 H182 sing N N 305 
RET C18 H183 sing N N 306 
RET C19 H191 sing N N 307 
RET C19 H192 sing N N 308 
RET C19 H193 sing N N 309 
RET C20 H201 sing N N 310 
RET C20 H202 sing N N 311 
RET C20 H203 sing N N 312 
SER N   CA   sing N N 313 
SER N   H    sing N N 314 
SER N   H2   sing N N 315 
SER CA  C    sing N N 316 
SER CA  CB   sing N N 317 
SER CA  HA   sing N N 318 
SER C   O    doub N N 319 
SER C   OXT  sing N N 320 
SER CB  OG   sing N N 321 
SER CB  HB2  sing N N 322 
SER CB  HB3  sing N N 323 
SER OG  HG   sing N N 324 
SER OXT HXT  sing N N 325 
THR N   CA   sing N N 326 
THR N   H    sing N N 327 
THR N   H2   sing N N 328 
THR CA  C    sing N N 329 
THR CA  CB   sing N N 330 
THR CA  HA   sing N N 331 
THR C   O    doub N N 332 
THR C   OXT  sing N N 333 
THR CB  OG1  sing N N 334 
THR CB  CG2  sing N N 335 
THR CB  HB   sing N N 336 
THR OG1 HG1  sing N N 337 
THR CG2 HG21 sing N N 338 
THR CG2 HG22 sing N N 339 
THR CG2 HG23 sing N N 340 
THR OXT HXT  sing N N 341 
TRP N   CA   sing N N 342 
TRP N   H    sing N N 343 
TRP N   H2   sing N N 344 
TRP CA  C    sing N N 345 
TRP CA  CB   sing N N 346 
TRP CA  HA   sing N N 347 
TRP C   O    doub N N 348 
TRP C   OXT  sing N N 349 
TRP CB  CG   sing N N 350 
TRP CB  HB2  sing N N 351 
TRP CB  HB3  sing N N 352 
TRP CG  CD1  doub Y N 353 
TRP CG  CD2  sing Y N 354 
TRP CD1 NE1  sing Y N 355 
TRP CD1 HD1  sing N N 356 
TRP CD2 CE2  doub Y N 357 
TRP CD2 CE3  sing Y N 358 
TRP NE1 CE2  sing Y N 359 
TRP NE1 HE1  sing N N 360 
TRP CE2 CZ2  sing Y N 361 
TRP CE3 CZ3  doub Y N 362 
TRP CE3 HE3  sing N N 363 
TRP CZ2 CH2  doub Y N 364 
TRP CZ2 HZ2  sing N N 365 
TRP CZ3 CH2  sing Y N 366 
TRP CZ3 HZ3  sing N N 367 
TRP CH2 HH2  sing N N 368 
TRP OXT HXT  sing N N 369 
TYR N   CA   sing N N 370 
TYR N   H    sing N N 371 
TYR N   H2   sing N N 372 
TYR CA  C    sing N N 373 
TYR CA  CB   sing N N 374 
TYR CA  HA   sing N N 375 
TYR C   O    doub N N 376 
TYR C   OXT  sing N N 377 
TYR CB  CG   sing N N 378 
TYR CB  HB2  sing N N 379 
TYR CB  HB3  sing N N 380 
TYR CG  CD1  doub Y N 381 
TYR CG  CD2  sing Y N 382 
TYR CD1 CE1  sing Y N 383 
TYR CD1 HD1  sing N N 384 
TYR CD2 CE2  doub Y N 385 
TYR CD2 HD2  sing N N 386 
TYR CE1 CZ   doub Y N 387 
TYR CE1 HE1  sing N N 388 
TYR CE2 CZ   sing Y N 389 
TYR CE2 HE2  sing N N 390 
TYR CZ  OH   sing N N 391 
TYR OH  HH   sing N N 392 
TYR OXT HXT  sing N N 393 
VAL N   CA   sing N N 394 
VAL N   H    sing N N 395 
VAL N   H2   sing N N 396 
VAL CA  C    sing N N 397 
VAL CA  CB   sing N N 398 
VAL CA  HA   sing N N 399 
VAL C   O    doub N N 400 
VAL C   OXT  sing N N 401 
VAL CB  CG1  sing N N 402 
VAL CB  CG2  sing N N 403 
VAL CB  HB   sing N N 404 
VAL CG1 HG11 sing N N 405 
VAL CG1 HG12 sing N N 406 
VAL CG1 HG13 sing N N 407 
VAL CG2 HG21 sing N N 408 
VAL CG2 HG22 sing N N 409 
VAL CG2 HG23 sing N N 410 
VAL OXT HXT  sing N N 411 
# 
_pdbx_audit_support.funding_organization   'H2020 Marie Curie Actions of the European Commission' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           637295 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1H68 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8PWI 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.011142 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007593 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.019608 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL  ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
N   ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   A VAL A 1 2   ? 36.66800 18.65400 -14.11200 0.670 106.77000 ?  2   VAL A N   1 
ATOM   2    N  N   B VAL A 1 2   ? 36.51000 18.66500 -14.03600 0.330 106.77000 ?  2   VAL A N   1 
ATOM   3    C  CA  A VAL A 1 2   ? 36.86200 19.80200 -13.23400 0.670 98.77000  ?  2   VAL A CA  1 
ATOM   4    C  CA  B VAL A 1 2   ? 36.76900 19.74100 -13.08900 0.330 98.29000  ?  2   VAL A CA  1 
ATOM   5    C  C   A VAL A 1 2   ? 36.65600 19.32200 -11.80300 0.670 87.39000  ?  2   VAL A C   1 
ATOM   6    C  C   B VAL A 1 2   ? 36.51300 19.29200 -11.62000 0.330 86.81000  ?  2   VAL A C   1 
ATOM   7    O  O   A VAL A 1 2   ? 35.53000 19.00100 -11.40300 0.670 89.06000  ?  2   VAL A O   1 
ATOM   8    O  O   B VAL A 1 2   ? 35.40900 18.88700 -11.29200 0.330 88.94000  ?  2   VAL A O   1 
ATOM   9    C  CB  A VAL A 1 2   ? 35.91100 20.96000 -13.57800 0.670 98.34000  ?  2   VAL A CB  1 
ATOM   10   C  CB  B VAL A 1 2   ? 35.93000 21.00400 -13.47900 0.330 98.19000  ?  2   VAL A CB  1 
ATOM   11   C  CG1 A VAL A 1 2   ? 34.45400 20.56800 -13.35600 0.670 96.66000  ?  2   VAL A CG1 1 
ATOM   12   C  CG1 B VAL A 1 2   ? 34.44400 20.68600 -13.58200 0.330 97.13000  ?  2   VAL A CG1 1 
ATOM   13   C  CG2 A VAL A 1 2   ? 36.26600 22.20300 -12.76800 0.670 88.64000  ?  2   VAL A CG2 1 
ATOM   14   C  CG2 B VAL A 1 2   ? 36.17400 22.14700 -12.51200 0.330 88.64000  ?  2   VAL A CG2 1 
ATOM   15   N  N   A GLY A 1 3   ? 37.74400 19.26100 -11.03500 0.670 83.82000  ?  3   GLY A N   1 
ATOM   16   N  N   B GLY A 1 3   ? 37.56800 19.31800 -10.76800 0.330 80.39000  ?  3   GLY A N   1 
ATOM   17   C  CA  A GLY A 1 3   ? 37.69300 18.80200 -9.66700  0.670 56.42000  ?  3   GLY A CA  1 
ATOM   18   C  CA  B GLY A 1 3   ? 37.47300 18.97100 -9.36500  0.330 59.73000  ?  3   GLY A CA  1 
ATOM   19   C  C   A GLY A 1 3   ? 37.58900 19.94900 -8.67400  0.670 59.40000  ?  3   GLY A C   1 
ATOM   20   C  C   B GLY A 1 3   ? 37.72600 20.17000 -8.44900  0.330 58.22000  ?  3   GLY A C   1 
ATOM   21   O  O   A GLY A 1 3   ? 37.79600 21.11500 -8.99900  0.670 60.00000  ?  3   GLY A O   1 
ATOM   22   O  O   B GLY A 1 3   ? 38.15700 21.24000 -8.87300  0.330 56.28000  ?  3   GLY A O   1 
ATOM   23   N  N   A LEU A 1 4   ? 37.25400 19.58400 -7.43400  0.670 55.23000  ?  4   LEU A N   1 
ATOM   24   N  N   B LEU A 1 4   ? 37.45800 19.96800 -7.15500  0.330 52.34000  ?  4   LEU A N   1 
ATOM   25   C  CA  A LEU A 1 4   ? 37.14800 20.58400 -6.37800  0.670 45.68000  ?  4   LEU A CA  1 
ATOM   26   C  CA  B LEU A 1 4   ? 37.38100 21.10000 -6.22700  0.330 42.69000  ?  4   LEU A CA  1 
ATOM   27   C  C   A LEU A 1 4   ? 38.43900 21.38000 -6.24400  0.670 41.87000  ?  4   LEU A C   1 
ATOM   28   C  C   B LEU A 1 4   ? 38.69500 21.86800 -6.13100  0.330 43.67000  ?  4   LEU A C   1 
ATOM   29   O  O   A LEU A 1 4   ? 38.41100 22.60800 -6.09900  0.670 42.99000  ?  4   LEU A O   1 
ATOM   30   O  O   B LEU A 1 4   ? 38.69800 23.09500 -5.93100  0.330 41.51000  ?  4   LEU A O   1 
ATOM   31   C  CB  A LEU A 1 4   ? 36.81100 19.91300 -5.04900  0.670 42.91000  ?  4   LEU A CB  1 
ATOM   32   C  CB  B LEU A 1 4   ? 36.98200 20.62500 -4.81700  0.330 40.89000  ?  4   LEU A CB  1 
ATOM   33   C  CG  A LEU A 1 4   ? 35.45600 19.22400 -4.92000  0.670 39.60000  ?  4   LEU A CG  1 
ATOM   34   C  CG  B LEU A 1 4   ? 35.58900 20.08500 -4.40400  0.330 43.29000  ?  4   LEU A CG  1 
ATOM   35   C  CD1 A LEU A 1 4   ? 35.32700 18.59800 -3.53700  0.670 44.95000  ?  4   LEU A CD1 1 
ATOM   36   C  CD1 B LEU A 1 4   ? 35.54900 19.81100 -2.95500  0.330 44.80000  ?  4   LEU A CD1 1 
ATOM   37   C  CD2 A LEU A 1 4   ? 34.32700 20.20100 -5.17600  0.670 51.69000  ?  4   LEU A CD2 1 
ATOM   38   C  CD2 B LEU A 1 4   ? 34.43900 21.02900 -4.72900  0.330 49.01000  ?  4   LEU A CD2 1 
ATOM   39   N  N   A THR A 1 5   ? 39.58500 20.69600 -6.28200  0.670 44.38000  ?  5   THR A N   1 
ATOM   40   N  N   B THR A 1 5   ? 39.82700 21.17300 -6.24800  0.330 47.38000  ?  5   THR A N   1 
ATOM   41   C  CA  A THR A 1 5   ? 40.85600 21.39100 -6.10900  0.670 45.53000  ?  5   THR A CA  1 
ATOM   42   C  CA  B THR A 1 5   ? 41.10800 21.84500 -6.05100  0.330 43.79000  ?  5   THR A CA  1 
ATOM   43   C  C   A THR A 1 5   ? 41.07400 22.41800 -7.21300  0.670 46.98000  ?  5   THR A C   1 
ATOM   44   C  C   B THR A 1 5   ? 41.47800 22.74900 -7.22200  0.330 45.42000  ?  5   THR A C   1 
ATOM   45   O  O   A THR A 1 5   ? 41.55100 23.52900 -6.95200  0.670 47.41000  ?  5   THR A O   1 
ATOM   46   O  O   B THR A 1 5   ? 42.19500 23.73300 -7.00900  0.330 43.32000  ?  5   THR A O   1 
ATOM   47   C  CB  A THR A 1 5   ? 42.01200 20.38900 -6.07300  0.670 47.84000  ?  5   THR A CB  1 
ATOM   48   C  CB  B THR A 1 5   ? 42.22800 20.83000 -5.82200  0.330 45.70000  ?  5   THR A CB  1 
ATOM   49   O  OG1 A THR A 1 5   ? 41.77500 19.33200 -7.01100  0.670 60.43000  ?  5   THR A OG1 1 
ATOM   50   O  OG1 B THR A 1 5   ? 42.07200 19.73300 -6.73100  0.330 56.44000  ?  5   THR A OG1 1 
ATOM   51   C  CG2 A THR A 1 5   ? 42.16200 19.79700 -4.67500  0.670 42.10000  ?  5   THR A CG2 1 
ATOM   52   C  CG2 B THR A 1 5   ? 42.18400 20.29400 -4.39600  0.330 43.27000  ?  5   THR A CG2 1 
ATOM   53   N  N   A THR A 1 6   ? 40.72100 22.07100 -8.45400  0.670 37.98000  ?  6   THR A N   1 
ATOM   54   N  N   B THR A 1 6   ? 41.02900 22.46600 -8.45800  0.330 40.11000  ?  6   THR A N   1 
ATOM   55   C  CA  A THR A 1 6   ? 40.86300 23.02900 -9.54700  0.670 42.04000  ?  6   THR A CA  1 
ATOM   56   C  CA  B THR A 1 6   ? 41.19700 23.50100 -9.47300  0.330 40.04000  ?  6   THR A CA  1 
ATOM   57   C  C   A THR A 1 6   ? 40.05300 24.29100 -9.27400  0.670 40.93000  ?  6   THR A C   1 
ATOM   58   C  C   B THR A 1 6   ? 40.28100 24.65600 -9.11800  0.330 41.60000  ?  6   THR A C   1 
ATOM   59   O  O   A THR A 1 6   ? 40.52200 25.40700 -9.52600  0.670 39.36000  ?  6   THR A O   1 
ATOM   60   O  O   B THR A 1 6   ? 40.74000 25.80500 -9.00700  0.330 39.76000  ?  6   THR A O   1 
ATOM   61   C  CB  A THR A 1 6   ? 40.42300 22.40200 -10.87100 0.670 45.91000  ?  6   THR A CB  1 
ATOM   62   C  CB  B THR A 1 6   ? 40.86700 23.04600 -10.89500 0.330 42.69000  ?  6   THR A CB  1 
ATOM   63   O  OG1 A THR A 1 6   ? 41.09700 21.15500 -11.07100 0.670 48.49000  ?  6   THR A OG1 1 
ATOM   64   O  OG1 B THR A 1 6   ? 41.05800 21.63600 -11.05800 0.330 48.28000  ?  6   THR A OG1 1 
ATOM   65   C  CG2 A THR A 1 6   ? 40.74400 23.34200 -12.03100 0.670 35.10000  ?  6   THR A CG2 1 
ATOM   66   C  CG2 B THR A 1 6   ? 41.83900 23.72900 -11.79100 0.330 31.26000  ?  6   THR A CG2 1 
ATOM   67   N  N   A LEU A 1 7   ? 38.83000 24.13100 -8.76400  0.670 39.91000  ?  7   LEU A N   1 
ATOM   68   N  N   B LEU A 1 7   ? 39.00200 24.34400 -8.79200  0.330 39.19000  ?  7   LEU A N   1 
ATOM   69   C  CA  A LEU A 1 7   ? 37.99400 25.28900 -8.47100  0.670 38.02000  ?  7   LEU A CA  1 
ATOM   70   C  CA  B LEU A 1 7   ? 38.07400 25.38500 -8.32600  0.330 38.78000  ?  7   LEU A CA  1 
ATOM   71   C  C   A LEU A 1 7   ? 38.59100 26.12600 -7.34800  0.670 35.74000  ?  7   LEU A C   1 
ATOM   72   C  C   B LEU A 1 7   ? 38.64100 26.14400 -7.12800  0.330 36.57000  ?  7   LEU A C   1 
ATOM   73   O  O   A LEU A 1 7   ? 38.56100 27.36100 -7.40300  0.670 43.14000  ?  7   LEU A O   1 
ATOM   74   O  O   B LEU A 1 7   ? 38.55100 27.36700 -7.04500  0.330 39.74000  ?  7   LEU A O   1 
ATOM   75   C  CB  A LEU A 1 7   ? 36.58100 24.82900 -8.11300  0.670 30.54000  ?  7   LEU A CB  1 
ATOM   76   C  CB  B LEU A 1 7   ? 36.73300 24.79100 -7.97500  0.330 31.35000  ?  7   LEU A CB  1 
ATOM   77   C  CG  A LEU A 1 7   ? 35.81200 24.19300 -9.27100  0.670 40.72000  ?  7   LEU A CG  1 
ATOM   78   C  CG  B LEU A 1 7   ? 36.32100 24.32400 -9.34300  0.330 40.77000  ?  7   LEU A CG  1 
ATOM   79   C  CD1 A LEU A 1 7   ? 34.49900 23.59500 -8.81400  0.670 39.72000  ?  7   LEU A CD1 1 
ATOM   80   C  CD1 B LEU A 1 7   ? 35.15400 23.47300 -9.12900  0.330 38.39000  ?  7   LEU A CD1 1 
ATOM   81   C  CD2 A LEU A 1 7   ? 35.58100 25.23200 -10.36600 0.670 25.67000  ?  7   LEU A CD2 1 
ATOM   82   C  CD2 B LEU A 1 7   ? 36.02100 25.49100 -10.27000 0.330 29.23000  ?  7   LEU A CD2 1 
ATOM   83   N  N   A PHE A 1 8   ? 39.14100 25.47200 -6.32200  0.670 32.63000  ?  8   PHE A N   1 
ATOM   84   N  N   B PHE A 1 8   ? 39.26400 25.47100 -6.19300  0.330 34.67000  ?  8   PHE A N   1 
ATOM   85   C  CA  A PHE A 1 8   ? 39.78400 26.21100 -5.24200  0.670 41.53000  ?  8   PHE A CA  1 
ATOM   86   C  CA  B PHE A 1 8   ? 39.76500 26.33800 -5.13600  0.330 41.34000  ?  8   PHE A CA  1 
ATOM   87   C  C   A PHE A 1 8   ? 40.99300 26.98900 -5.75600  0.670 39.47000  ?  8   PHE A C   1 
ATOM   88   C  C   B PHE A 1 8   ? 40.99400 27.09500 -5.60500  0.330 39.52000  ?  8   PHE A C   1 
ATOM   89   O  O   A PHE A 1 8   ? 41.18100 28.15900 -5.40200  0.670 41.40000  ?  8   PHE A O   1 
ATOM   90   O  O   B PHE A 1 8   ? 41.26400 28.20700 -5.13800  0.330 40.26000  ?  8   PHE A O   1 
ATOM   91   C  CB  A PHE A 1 8   ? 40.17800 25.25300 -4.11500  0.670 41.84000  ?  8   PHE A CB  1 
ATOM   92   C  CB  B PHE A 1 8   ? 40.00600 25.53300 -3.87900  0.330 39.75000  ?  8   PHE A CB  1 
ATOM   93   C  CG  A PHE A 1 8   ? 39.00100 24.72000 -3.32800  0.670 38.67000  ?  8   PHE A CG  1 
ATOM   94   C  CG  B PHE A 1 8   ? 38.76300 25.02900 -3.29300  0.330 40.19000  ?  8   PHE A CG  1 
ATOM   95   C  CD1 A PHE A 1 8   ? 37.92600 25.53900 -3.01300  0.670 45.18000  ?  8   PHE A CD1 1 
ATOM   96   C  CD1 B PHE A 1 8   ? 37.69800 25.87700 -3.05800  0.330 44.03000  ?  8   PHE A CD1 1 
ATOM   97   C  CD2 A PHE A 1 8   ? 38.97200 23.39900 -2.90500  0.670 32.04000  ?  8   PHE A CD2 1 
ATOM   98   C  CD2 B PHE A 1 8   ? 38.61600 23.70200 -3.02000  0.330 33.43000  ?  8   PHE A CD2 1 
ATOM   99   C  CE1 A PHE A 1 8   ? 36.84600 25.05400 -2.29600  0.670 39.73000  ?  8   PHE A CE1 1 
ATOM   100  C  CE1 B PHE A 1 8   ? 36.53700 25.39700 -2.51300  0.330 40.46000  ?  8   PHE A CE1 1 
ATOM   101  C  CE2 A PHE A 1 8   ? 37.89300 22.90900 -2.18500  0.670 27.73000  ?  8   PHE A CE2 1 
ATOM   102  C  CE2 B PHE A 1 8   ? 37.46200 23.23200 -2.50000  0.330 32.87000  ?  8   PHE A CE2 1 
ATOM   103  C  CZ  A PHE A 1 8   ? 36.82900 23.74000 -1.88100  0.670 38.42000  ?  8   PHE A CZ  1 
ATOM   104  C  CZ  B PHE A 1 8   ? 36.41500 24.07100 -2.26900  0.330 39.01000  ?  8   PHE A CZ  1 
ATOM   105  N  N   A TRP A 1 9   ? 41.81400 26.36900 -6.61000  0.670 40.05000  ?  9   TRP A N   1 
ATOM   106  N  N   B TRP A 1 9   ? 41.72700 26.55300 -6.56700  0.330 39.30000  ?  9   TRP A N   1 
ATOM   107  C  CA  A TRP A 1 9   ? 42.96100 27.08700 -7.15900  0.670 33.35000  ?  9   TRP A CA  1 
ATOM   108  C  CA  B TRP A 1 9   ? 42.90200 27.28600 -7.01400  0.330 34.49000  ?  9   TRP A CA  1 
ATOM   109  C  C   A TRP A 1 9   ? 42.51000 28.30600 -7.95500  0.670 37.15000  ?  9   TRP A C   1 
ATOM   110  C  C   B TRP A 1 9   ? 42.52500 28.56600 -7.77700  0.330 36.96000  ?  9   TRP A C   1 
ATOM   111  O  O   A TRP A 1 9   ? 43.13600 29.37000 -7.88200  0.670 33.02000  ?  9   TRP A O   1 
ATOM   112  O  O   B TRP A 1 9   ? 43.09300 29.65500 -7.50700  0.330 34.23000  ?  9   TRP A O   1 
ATOM   113  C  CB  A TRP A 1 9   ? 43.80800 26.15400 -8.02700  0.670 42.74000  ?  9   TRP A CB  1 
ATOM   114  C  CB  B TRP A 1 9   ? 43.77000 26.37800 -7.85400  0.330 41.00000  ?  9   TRP A CB  1 
ATOM   115  C  CG  A TRP A 1 9   ? 44.73200 25.28100 -7.22600  0.670 41.81000  ?  9   TRP A CG  1 
ATOM   116  C  CG  B TRP A 1 9   ? 44.71700 25.64300 -7.04000  0.330 41.92000  ?  9   TRP A CG  1 
ATOM   117  C  CD1 A TRP A 1 9   ? 44.70800 23.91800 -7.14700  0.670 45.12000  ?  9   TRP A CD1 1 
ATOM   118  C  CD1 B TRP A 1 9   ? 44.85000 24.29400 -6.96600  0.330 43.23000  ?  9   TRP A CD1 1 
ATOM   119  C  CD2 A TRP A 1 9   ? 45.81500 25.71100 -6.38500  0.670 43.55000  ?  9   TRP A CD2 1 
ATOM   120  C  CD2 B TRP A 1 9   ? 45.68300 26.19200 -6.14600  0.330 41.73000  ?  9   TRP A CD2 1 
ATOM   121  N  NE1 A TRP A 1 9   ? 45.70600 23.47300 -6.31200  0.670 50.16000  ?  9   TRP A NE1 1 
ATOM   122  N  NE1 B TRP A 1 9   ? 45.82700 23.95900 -6.08200  0.330 45.89000  ?  9   TRP A NE1 1 
ATOM   123  C  CE2 A TRP A 1 9   ? 46.40000 24.55300 -5.83300  0.670 40.79000  ?  9   TRP A CE2 1 
ATOM   124  C  CE2 B TRP A 1 9   ? 46.36600 25.10300 -5.56400  0.330 42.20000  ?  9   TRP A CE2 1 
ATOM   125  C  CE3 A TRP A 1 9   ? 46.34500 26.96100 -6.04600  0.670 34.88000  ?  9   TRP A CE3 1 
ATOM   126  C  CE3 B TRP A 1 9   ? 46.04700 27.48400 -5.78600  0.330 35.81000  ?  9   TRP A CE3 1 
ATOM   127  C  CZ2 A TRP A 1 9   ? 47.48500 24.60700 -4.96000  0.670 47.16000  ?  9   TRP A CZ2 1 
ATOM   128  C  CZ2 B TRP A 1 9   ? 47.38000 25.26400 -4.62800  0.330 46.03000  ?  9   TRP A CZ2 1 
ATOM   129  C  CZ3 A TRP A 1 9   ? 47.42400 27.01200 -5.18000  0.670 52.87000  ?  9   TRP A CZ3 1 
ATOM   130  C  CZ3 B TRP A 1 9   ? 47.06200 27.64000 -4.85300  0.330 50.27000  ?  9   TRP A CZ3 1 
ATOM   131  C  CH2 A TRP A 1 9   ? 47.98200 25.84300 -4.64700  0.670 51.31000  ?  9   TRP A CH2 1 
ATOM   132  C  CH2 B TRP A 1 9   ? 47.72000 26.53400 -4.28500  0.330 47.03000  ?  9   TRP A CH2 1 
ATOM   133  N  N   A LEU A 1 10  ? 41.41800 28.17500 -8.71200  0.670 34.03000  ?  10  LEU A N   1 
ATOM   134  N  N   B LEU A 1 10  ? 41.58200 28.46400 -8.74000  0.330 35.87000  ?  10  LEU A N   1 
ATOM   135  C  CA  A LEU A 1 10  ? 40.90800 29.30700 -9.48100  0.670 32.57000  ?  10  LEU A CA  1 
ATOM   136  C  CA  B LEU A 1 10  ? 41.19000 29.67200 -9.43700  0.330 34.64000  ?  10  LEU A CA  1 
ATOM   137  C  C   A LEU A 1 10  ? 40.53300 30.46300 -8.56500  0.670 38.82000  ?  10  LEU A C   1 
ATOM   138  C  C   B LEU A 1 10  ? 40.78000 30.66200 -8.41100  0.330 38.60000  ?  10  LEU A C   1 
ATOM   139  O  O   A LEU A 1 10  ? 40.84000 31.62700 -8.85000  0.670 30.05000  ?  10  LEU A O   1 
ATOM   140  O  O   B LEU A 1 10  ? 41.22100 31.82300 -8.44600  0.330 33.71000  ?  10  LEU A O   1 
ATOM   141  C  CB  A LEU A 1 10  ? 39.69600 28.87900 -10.30600 0.670 37.87000  ?  10  LEU A CB  1 
ATOM   142  C  CB  B LEU A 1 10  ? 40.06800 29.39400 -10.41800 0.330 35.13000  ?  10  LEU A CB  1 
ATOM   143  C  CG  A LEU A 1 10  ? 39.96600 27.93000 -11.46900 0.670 47.95000  ?  10  LEU A CG  1 
ATOM   144  C  CG  B LEU A 1 10  ? 40.63500 28.63300 -11.58900 0.330 44.45000  ?  10  LEU A CG  1 
ATOM   145  C  CD1 A LEU A 1 10  ? 38.67100 27.44600 -12.09100 0.670 46.88000  ?  10  LEU A CD1 1 
ATOM   146  C  CD1 B LEU A 1 10  ? 39.52100 27.97300 -12.31900 0.330 48.32000  ?  10  LEU A CD1 1 
ATOM   147  C  CD2 A LEU A 1 10  ? 40.84500 28.62000 -12.50400 0.670 52.44000  ?  10  LEU A CD2 1 
ATOM   148  C  CD2 B LEU A 1 10  ? 41.31800 29.56800 -12.54900 0.330 41.57000  ?  10  LEU A CD2 1 
ATOM   149  N  N   A GLY A 1 11  ? 39.84100 30.16100 -7.46600  0.670 45.55000  ?  11  GLY A N   1 
ATOM   150  N  N   B GLY A 1 11  ? 39.93500 30.18500 -7.47700  0.330 43.93000  ?  11  GLY A N   1 
ATOM   151  C  CA  A GLY A 1 11  ? 39.52000 31.20200 -6.50700  0.670 34.71000  ?  11  GLY A CA  1 
ATOM   152  C  CA  B GLY A 1 11  ? 39.92400 30.52400 -6.06800  0.330 27.45000  ?  11  GLY A CA  1 
ATOM   153  C  C   A GLY A 1 11  ? 40.76300 31.81400 -5.89600  0.670 30.67000  ?  11  GLY A C   1 
ATOM   154  C  C   B GLY A 1 11  ? 41.07100 31.44200 -5.80700  0.330 31.30000  ?  11  GLY A C   1 
ATOM   155  O  O   A GLY A 1 11  ? 40.84700 33.03200 -5.72400  0.670 35.34000  ?  11  GLY A O   1 
ATOM   156  O  O   B GLY A 1 11  ? 40.89800 32.67000 -5.92600  0.330 36.40000  ?  11  GLY A O   1 
ATOM   157  N  N   A ALA A 1 12  ? 41.75400 30.97800 -5.57800  0.670 31.32000  ?  12  ALA A N   1 
ATOM   158  N  N   B ALA A 1 12  ? 42.27800 30.93400 -5.51100  0.330 35.03000  ?  12  ALA A N   1 
ATOM   159  C  CA  A ALA A 1 12  ? 43.01500 31.48500 -5.05000  0.670 39.60000  ?  12  ALA A CA  1 
ATOM   160  C  CA  B ALA A 1 12  ? 43.21300 31.92800 -4.95700  0.330 37.40000  ?  12  ALA A CA  1 
ATOM   161  C  C   A ALA A 1 12  ? 43.65400 32.47300 -6.01700  0.670 32.43000  ?  12  ALA A C   1 
ATOM   162  C  C   B ALA A 1 12  ? 43.80300 32.80900 -6.02900  0.330 34.44000  ?  12  ALA A C   1 
ATOM   163  O  O   A ALA A 1 12  ? 44.07200 33.56700 -5.61900  0.670 36.84000  ?  12  ALA A O   1 
ATOM   164  O  O   B ALA A 1 12  ? 44.30200 33.89600 -5.71100  0.330 36.63000  ?  12  ALA A O   1 
ATOM   165  C  CB  A ALA A 1 12  ? 43.96300 30.32000 -4.76800  0.670 40.46000  ?  12  ALA A CB  1 
ATOM   166  C  CB  B ALA A 1 12  ? 44.30600 31.29000 -4.14800  0.330 34.74000  ?  12  ALA A CB  1 
ATOM   167  N  N   A ILE A 1 13  ? 43.73400 32.10500 -7.29800  0.670 40.34000  ?  13  ILE A N   1 
ATOM   168  N  N   B ILE A 1 13  ? 43.73400 32.36400 -7.28900  0.330 38.67000  ?  13  ILE A N   1 
ATOM   169  C  CA  A ILE A 1 13  ? 44.37300 32.97700 -8.28200  0.670 36.79000  ?  13  ILE A CA  1 
ATOM   170  C  CA  B ILE A 1 13  ? 44.25600 33.17200 -8.38700  0.330 36.30000  ?  13  ILE A CA  1 
ATOM   171  C  C   A ILE A 1 13  ? 43.60500 34.28400 -8.40300  0.670 36.86000  ?  13  ILE A C   1 
ATOM   172  C  C   B ILE A 1 13  ? 43.52900 34.49600 -8.43100  0.330 36.56000  ?  13  ILE A C   1 
ATOM   173  O  O   A ILE A 1 13  ? 44.19100 35.37200 -8.45700  0.670 38.20000  ?  13  ILE A O   1 
ATOM   174  O  O   B ILE A 1 13  ? 44.14900 35.55900 -8.28100  0.330 38.27000  ?  13  ILE A O   1 
ATOM   175  C  CB  A ILE A 1 13  ? 44.47400 32.27300 -9.64600  0.670 35.53000  ?  13  ILE A CB  1 
ATOM   176  C  CB  B ILE A 1 13  ? 44.12800 32.46000 -9.74300  0.330 35.27000  ?  13  ILE A CB  1 
ATOM   177  C  CG1 A ILE A 1 13  ? 45.46900 31.11600 -9.59400  0.670 30.59000  ?  13  ILE A CG1 1 
ATOM   178  C  CG1 B ILE A 1 13  ? 44.96600 31.22100 -9.78500  0.330 32.34000  ?  13  ILE A CG1 1 
ATOM   179  C  CG2 A ILE A 1 13  ? 44.88200 33.27700 -10.72100 0.670 28.72000  ?  13  ILE A CG2 1 
ATOM   180  C  CG2 B ILE A 1 13  ? 44.65600 33.37700 -10.79900 0.330 28.72000  ?  13  ILE A CG2 1 
ATOM   181  C  CD1 A ILE A 1 13  ? 45.26300 30.10300 -10.69500 0.670 40.03000  ?  13  ILE A CD1 1 
ATOM   182  C  CD1 B ILE A 1 13  ? 44.51600 30.31400 -10.90700 0.330 37.03000  ?  13  ILE A CD1 1 
ATOM   183  N  N   A GLY A 1 14  ? 42.27700 34.19200 -8.47400  0.670 34.00000  ?  14  GLY A N   1 
ATOM   184  N  N   B GLY A 1 14  ? 42.19100 34.44500 -8.60700  0.330 33.90000  ?  14  GLY A N   1 
ATOM   185  C  CA  A GLY A 1 14  ? 41.47000 35.39200 -8.57200  0.670 27.21000  ?  14  GLY A CA  1 
ATOM   186  C  CA  B GLY A 1 14  ? 41.40200 35.66800 -8.53900  0.330 28.24000  ?  14  GLY A CA  1 
ATOM   187  C  C   A GLY A 1 14  ? 41.64800 36.31200 -7.38300  0.670 38.07000  ?  14  GLY A C   1 
ATOM   188  C  C   B GLY A 1 14  ? 41.76700 36.44400 -7.29500  0.330 38.45000  ?  14  GLY A C   1 
ATOM   189  O  O   A GLY A 1 14  ? 41.73700 37.53100 -7.53900  0.670 39.93000  ?  14  GLY A O   1 
ATOM   190  O  O   B GLY A 1 14  ? 42.03500 37.65100 -7.33900  0.330 38.60000  ?  14  GLY A O   1 
ATOM   191  N  N   A MET A 1 15  ? 41.69000 35.74800 -6.17500  0.670 36.45000  ?  15  MET A N   1 
ATOM   192  N  N   B MET A 1 15  ? 41.89800 35.73200 -6.18300  0.330 36.18000  ?  15  MET A N   1 
ATOM   193  C  CA  A MET A 1 15  ? 41.88600 36.59000 -5.00200  0.670 41.15000  ?  15  MET A CA  1 
ATOM   194  C  CA  B MET A 1 15  ? 42.09200 36.42000 -4.91700  0.330 41.36000  ?  15  MET A CA  1 
ATOM   195  C  C   A MET A 1 15  ? 43.28000 37.20500 -5.00200  0.670 43.79000  ?  15  MET A C   1 
ATOM   196  C  C   B MET A 1 15  ? 43.49000 37.08000 -4.84800  0.330 42.80000  ?  15  MET A C   1 
ATOM   197  O  O   A MET A 1 15  ? 43.44700 38.37500 -4.64000  0.670 37.51000  ?  15  MET A O   1 
ATOM   198  O  O   B MET A 1 15  ? 43.61300 38.26300 -4.47400  0.330 39.19000  ?  15  MET A O   1 
ATOM   199  C  CB  A MET A 1 15  ? 41.63500 35.77900 -3.73300  0.670 37.80000  ?  15  MET A CB  1 
ATOM   200  C  CB  B MET A 1 15  ? 41.81100 35.43000 -3.76300  0.330 36.54000  ?  15  MET A CB  1 
ATOM   201  C  CG  A MET A 1 15  ? 40.19000 35.27700 -3.61300  0.670 36.26000  ?  15  MET A CG  1 
ATOM   202  C  CG  B MET A 1 15  ? 40.37300 34.71000 -3.68100  0.330 37.05000  ?  15  MET A CG  1 
ATOM   203  S  SD  A MET A 1 15  ? 38.98900 36.62000 -3.46600  0.670 35.42000  ?  15  MET A SD  1 
ATOM   204  S  SD  B MET A 1 15  ? 38.95400 35.84300 -3.77800  0.330 32.88000  ?  15  MET A SD  1 
ATOM   205  C  CE  A MET A 1 15  ? 37.44100 35.72900 -3.50800  0.670 28.70000  ?  15  MET A CE  1 
ATOM   206  C  CE  B MET A 1 15  ? 37.45600 34.85700 -3.59300  0.330 36.57000  ?  15  MET A CE  1 
ATOM   207  N  N   A LEU A 1 16  ? 44.28800 36.44700 -5.44000  0.670 40.99000  ?  16  LEU A N   1 
ATOM   208  N  N   B LEU A 1 16  ? 44.55300 36.35300 -5.22400  0.330 40.39000  ?  16  LEU A N   1 
ATOM   209  C  CA  A LEU A 1 16  ? 45.65200 36.96700 -5.46300  0.670 42.76000  ?  16  LEU A CA  1 
ATOM   210  C  CA  B LEU A 1 16  ? 45.80600 37.05000 -5.51000  0.330 42.57000  ?  16  LEU A CA  1 
ATOM   211  C  C   A LEU A 1 16  ? 45.77300 38.15600 -6.41000  0.670 42.46000  ?  16  LEU A C   1 
ATOM   212  C  C   B LEU A 1 16  ? 45.56400 38.28400 -6.33800  0.330 43.28000  ?  16  LEU A C   1 
ATOM   213  O  O   A LEU A 1 16  ? 46.37500 39.18000 -6.06800  0.670 46.83000  ?  16  LEU A O   1 
ATOM   214  O  O   B LEU A 1 16  ? 45.63700 39.39800 -5.84300  0.330 45.03000  ?  16  LEU A O   1 
ATOM   215  C  CB  A LEU A 1 16  ? 46.62500 35.85900 -5.86900  0.670 45.51000  ?  16  LEU A CB  1 
ATOM   216  C  CB  B LEU A 1 16  ? 46.78000 36.14600 -6.26100  0.330 40.97000  ?  16  LEU A CB  1 
ATOM   217  C  CG  A LEU A 1 16  ? 46.98700 34.86100 -4.76800  0.670 55.12000  ?  16  LEU A CG  1 
ATOM   218  C  CG  B LEU A 1 16  ? 47.58400 35.34400 -5.24600  0.330 53.53000  ?  16  LEU A CG  1 
ATOM   219  C  CD1 A LEU A 1 16  ? 47.11100 33.44600 -5.31200  0.670 51.49000  ?  16  LEU A CD1 1 
ATOM   220  C  CD1 B LEU A 1 16  ? 48.08700 33.96500 -5.68200  0.330 50.27000  ?  16  LEU A CD1 1 
ATOM   221  C  CD2 A LEU A 1 16  ? 48.27300 35.28000 -4.06400  0.670 65.84000  ?  16  LEU A CD2 1 
ATOM   222  C  CD2 B LEU A 1 16  ? 48.70400 36.25300 -4.77600  0.330 58.26000  ?  16  LEU A CD2 1 
ATOM   223  N  N   A VAL A 1 17  ? 45.20800 38.03500 -7.61300  0.670 38.19000  ?  17  VAL A N   1 
ATOM   224  N  N   B VAL A 1 17  ? 45.17300 38.07000 -7.59600  0.330 37.29000  ?  17  VAL A N   1 
ATOM   225  C  CA  A VAL A 1 17  ? 45.26400 39.13300 -8.57500  0.670 40.31000  ?  17  VAL A CA  1 
ATOM   226  C  CA  B VAL A 1 17  ? 45.24500 39.12800 -8.60300  0.330 40.41000  ?  17  VAL A CA  1 
ATOM   227  C  C   A VAL A 1 17  ? 44.59000 40.37000 -7.99700  0.670 45.45000  ?  17  VAL A C   1 
ATOM   228  C  C   B VAL A 1 17  ? 44.50900 40.34800 -8.08700  0.330 44.27000  ?  17  VAL A C   1 
ATOM   229  O  O   A VAL A 1 17  ? 45.11000 41.48900 -8.09700  0.670 52.99000  ?  17  VAL A O   1 
ATOM   230  O  O   B VAL A 1 17  ? 45.03300 41.47700 -8.10500  0.330 49.55000  ?  17  VAL A O   1 
ATOM   231  C  CB  A VAL A 1 17  ? 44.61500 38.71300 -9.90600  0.670 39.94000  ?  17  VAL A CB  1 
ATOM   232  C  CB  B VAL A 1 17  ? 44.68500 38.66900 -9.97400  0.330 39.83000  ?  17  VAL A CB  1 
ATOM   233  C  CG1 A VAL A 1 17  ? 44.42900 39.92900 -10.80800 0.670 42.60000  ?  17  VAL A CG1 1 
ATOM   234  C  CG1 B VAL A 1 17  ? 44.73500 39.75600 -10.95600 0.330 42.17000  ?  17  VAL A CG1 1 
ATOM   235  C  CG2 A VAL A 1 17  ? 45.44900 37.65200 -10.60100 0.670 31.97000  ?  17  VAL A CG2 1 
ATOM   236  C  CG2 B VAL A 1 17  ? 45.41600 37.43300 -10.54400 0.330 32.31000  ?  17  VAL A CG2 1 
ATOM   237  N  N   A GLY A 1 18  ? 43.41700 40.18900 -7.38900  0.670 40.45000  ?  18  GLY A N   1 
ATOM   238  N  N   B GLY A 1 18  ? 43.30300 40.12900 -7.54800  0.330 40.16000  ?  18  GLY A N   1 
ATOM   239  C  CA  A GLY A 1 18  ? 42.77000 41.30600 -6.72400  0.670 39.27000  ?  18  GLY A CA  1 
ATOM   240  C  CA  B GLY A 1 18  ? 42.62000 41.23400 -6.91400  0.330 40.62000  ?  18  GLY A CA  1 
ATOM   241  C  C   A GLY A 1 18  ? 43.65300 41.91500 -5.65400  0.670 41.08000  ?  18  GLY A C   1 
ATOM   242  C  C   B GLY A 1 18  ? 43.49600 41.88700 -5.86400  0.330 42.26000  ?  18  GLY A C   1 
ATOM   243  O  O   A GLY A 1 18  ? 43.79900 43.13600 -5.57000  0.670 44.97000  ?  18  GLY A O   1 
ATOM   244  O  O   B GLY A 1 18  ? 43.54500 43.10400 -5.77700  0.330 45.65000  ?  18  GLY A O   1 
ATOM   245  N  N   A THR A 1 19  ? 44.27400 41.06300 -4.83700  0.670 37.24000  ?  19  THR A N   1 
ATOM   246  N  N   B THR A 1 19  ? 44.17900 41.08000 -5.03400  0.330 37.91000  ?  19  THR A N   1 
ATOM   247  C  CA  A THR A 1 19  ? 45.10100 41.54500 -3.73600  0.670 45.65000  ?  19  THR A CA  1 
ATOM   248  C  CA  B THR A 1 19  ? 44.92100 41.60800 -3.87700  0.330 45.05000  ?  19  THR A CA  1 
ATOM   249  C  C   A THR A 1 19  ? 46.23800 42.42600 -4.24200  0.670 45.34000  ?  19  THR A C   1 
ATOM   250  C  C   B THR A 1 19  ? 46.21900 42.32800 -4.26500  0.330 45.40000  ?  19  THR A C   1 
ATOM   251  O  O   A THR A 1 19  ? 46.47100 43.52200 -3.71800  0.670 47.24000  ?  19  THR A O   1 
ATOM   252  O  O   B THR A 1 19  ? 46.51400 43.41700 -3.75600  0.330 48.31000  ?  19  THR A O   1 
ATOM   253  C  CB  A THR A 1 19  ? 45.66100 40.35900 -2.94900  0.670 35.70000  ?  19  THR A CB  1 
ATOM   254  C  CB  B THR A 1 19  ? 45.21300 40.48600 -2.89400  0.330 39.93000  ?  19  THR A CB  1 
ATOM   255  O  OG1 A THR A 1 19  ? 44.59000 39.61300 -2.35700  0.670 38.11000  ?  19  THR A OG1 1 
ATOM   256  O  OG1 B THR A 1 19  ? 43.96700 39.87400 -2.51300  0.330 37.66000  ?  19  THR A OG1 1 
ATOM   257  C  CG2 A THR A 1 19  ? 46.60900 40.84300 -1.86000  0.670 49.96000  ?  19  THR A CG2 1 
ATOM   258  C  CG2 B THR A 1 19  ? 45.82100 41.08800 -1.76300  0.330 42.96000  ?  19  THR A CG2 1 
ATOM   259  N  N   A LEU A 1 20  ? 46.96900 41.95500 -5.25500  0.670 49.63000  ?  20  LEU A N   1 
ATOM   260  N  N   B LEU A 1 20  ? 47.03300 41.71900 -5.10900  0.330 48.30000  ?  20  LEU A N   1 
ATOM   261  C  CA  A LEU A 1 20  ? 48.08500 42.73500 -5.78000  0.670 59.29000  ?  20  LEU A CA  1 
ATOM   262  C  CA  B LEU A 1 20  ? 47.85400 42.54800 -5.98400  0.330 57.20000  ?  20  LEU A CA  1 
ATOM   263  C  C   A LEU A 1 20  ? 47.59800 44.02700 -6.42100  0.670 60.37000  ?  20  LEU A C   1 
ATOM   264  C  C   B LEU A 1 20  ? 47.05100 43.77100 -6.43800  0.330 56.86000  ?  20  LEU A C   1 
ATOM   265  O  O   A LEU A 1 20  ? 48.24500 45.07400 -6.29700  0.670 54.95000  ?  20  LEU A O   1 
ATOM   266  O  O   B LEU A 1 20  ? 47.15200 44.82600 -5.79100  0.330 55.63000  ?  20  LEU A O   1 
ATOM   267  C  CB  A LEU A 1 20  ? 48.87200 41.90400 -6.79000  0.670 52.38000  ?  20  LEU A CB  1 
ATOM   268  C  CB  B LEU A 1 20  ? 48.37600 41.75400 -7.18900  0.330 50.07000  ?  20  LEU A CB  1 
ATOM   269  C  CG  A LEU A 1 20  ? 49.45800 40.59500 -6.26300  0.670 48.38000  ?  20  LEU A CG  1 
ATOM   270  C  CG  B LEU A 1 20  ? 49.31200 40.60600 -6.80400  0.330 50.63000  ?  20  LEU A CG  1 
ATOM   271  C  CD1 A LEU A 1 20  ? 50.16200 39.83700 -7.38000  0.670 57.54000  ?  20  LEU A CD1 1 
ATOM   272  C  CD1 B LEU A 1 20  ? 49.69300 39.80000 -8.01900  0.330 54.04000  ?  20  LEU A CD1 1 
ATOM   273  C  CD2 A LEU A 1 20  ? 50.41000 40.86100 -5.10900  0.670 53.69000  ?  20  LEU A CD2 1 
ATOM   274  C  CD2 B LEU A 1 20  ? 50.57300 41.13200 -6.14400  0.330 50.62000  ?  20  LEU A CD2 1 
ATOM   275  N  N   A ALA A 1 21  ? 46.46100 43.97200 -7.11700  0.670 56.98000  ?  21  ALA A N   1 
ATOM   276  N  N   B ALA A 1 21  ? 46.23100 43.63800 -7.50500  0.330 49.38000  ?  21  ALA A N   1 
ATOM   277  C  CA  A ALA A 1 21  ? 45.91400 45.17700 -7.73200  0.670 48.15000  ?  21  ALA A CA  1 
ATOM   278  C  CA  B ALA A 1 21  ? 45.56000 44.78900 -8.13200  0.330 47.18000  ?  21  ALA A CA  1 
ATOM   279  C  C   A ALA A 1 21  ? 45.58600 46.22500 -6.67600  0.670 56.29000  ?  21  ALA A C   1 
ATOM   280  C  C   B ALA A 1 21  ? 45.13900 45.89400 -7.16300  0.330 52.80000  ?  21  ALA A C   1 
ATOM   281  O  O   A ALA A 1 21  ? 45.93000 47.40300 -6.82500  0.670 53.70000  ?  21  ALA A O   1 
ATOM   282  O  O   B ALA A 1 21  ? 45.24400 47.08400 -7.45800  0.330 51.31000  ?  21  ALA A O   1 
ATOM   283  C  CB  A ALA A 1 21  ? 44.67100 44.83100 -8.55200  0.670 39.79000  ?  21  ALA A CB  1 
ATOM   284  C  CB  B ALA A 1 21  ? 44.33200 44.33200 -8.88900  0.330 45.26000  ?  21  ALA A CB  1 
ATOM   285  N  N   A PHE A 1 22  ? 44.91500 45.81400 -5.59500  0.670 60.21000  ?  22  PHE A N   1 
ATOM   286  N  N   B PHE A 1 22  ? 44.68900 45.52300 -5.97500  0.330 58.16000  ?  22  PHE A N   1 
ATOM   287  C  CA  A PHE A 1 22  ? 44.55000 46.77200 -4.55600  0.670 53.34000  ?  22  PHE A CA  1 
ATOM   288  C  CA  B PHE A 1 22  ? 44.40700 46.56600 -5.00600  0.330 53.47000  ?  22  PHE A CA  1 
ATOM   289  C  C   A PHE A 1 22  ? 45.79000 47.31900 -3.85400  0.670 54.69000  ?  22  PHE A C   1 
ATOM   290  C  C   B PHE A 1 22  ? 45.66100 47.01900 -4.27500  0.330 54.73000  ?  22  PHE A C   1 
ATOM   291  O  O   A PHE A 1 22  ? 45.87300 48.52300 -3.58500  0.670 68.92000  ?  22  PHE A O   1 
ATOM   292  O  O   B PHE A 1 22  ? 45.77300 48.20100 -3.93600  0.330 64.74000  ?  22  PHE A O   1 
ATOM   293  C  CB  A PHE A 1 22  ? 43.59500 46.13100 -3.54400  0.670 55.40000  ?  22  PHE A CB  1 
ATOM   294  C  CB  B PHE A 1 22  ? 43.36600 46.08900 -4.01500  0.330 52.12000  ?  22  PHE A CB  1 
ATOM   295  C  CG  A PHE A 1 22  ? 42.37300 45.50700 -4.16900  0.670 50.01000  ?  22  PHE A CG  1 
ATOM   296  C  CG  B PHE A 1 22  ? 42.09600 45.67300 -4.64700  0.330 49.47000  ?  22  PHE A CG  1 
ATOM   297  C  CD1 A PHE A 1 22  ? 41.72300 46.12400 -5.22900  0.670 49.70000  ?  22  PHE A CD1 1 
ATOM   298  C  CD1 B PHE A 1 22  ? 41.54900 46.42900 -5.66600  0.330 50.06000  ?  22  PHE A CD1 1 
ATOM   299  C  CD2 A PHE A 1 22  ? 41.87800 44.29900 -3.70100  0.670 49.77000  ?  22  PHE A CD2 1 
ATOM   300  C  CD2 B PHE A 1 22  ? 41.43000 44.53600 -4.21700  0.330 48.24000  ?  22  PHE A CD2 1 
ATOM   301  C  CE1 A PHE A 1 22  ? 40.60500 45.54900 -5.80700  0.670 51.89000  ?  22  PHE A CE1 1 
ATOM   302  C  CE1 B PHE A 1 22  ? 40.35500 46.03400 -6.27300  0.330 51.76000  ?  22  PHE A CE1 1 
ATOM   303  C  CE2 A PHE A 1 22  ? 40.76100 43.72000 -4.27600  0.670 47.58000  ?  22  PHE A CE2 1 
ATOM   304  C  CE2 B PHE A 1 22  ? 40.24300 44.13100 -4.80800  0.330 43.94000  ?  22  PHE A CE2 1 
ATOM   305  C  CZ  A PHE A 1 22  ? 40.12600 44.34500 -5.33100  0.670 44.48000  ?  22  PHE A CZ  1 
ATOM   306  C  CZ  B PHE A 1 22  ? 39.69700 44.87800 -5.83400  0.330 44.18000  ?  22  PHE A CZ  1 
ATOM   307  N  N   A ALA A 1 23  ? 46.76600 46.45700 -3.55600  0.670 57.20000  ?  23  ALA A N   1 
ATOM   308  N  N   B ALA A 1 23  ? 46.62300 46.12700 -4.02700  0.330 53.75000  ?  23  ALA A N   1 
ATOM   309  C  CA  A ALA A 1 23  ? 47.97800 46.92500 -2.88800  0.670 62.88000  ?  23  ALA A CA  1 
ATOM   310  C  CA  B ALA A 1 23  ? 47.86600 46.62200 -3.44500  0.330 60.31000  ?  23  ALA A CA  1 
ATOM   311  C  C   A ALA A 1 23  ? 48.69900 47.96000 -3.73900  0.670 70.28000  ?  23  ALA A C   1 
ATOM   312  C  C   B ALA A 1 23  ? 48.43200 47.74300 -4.30400  0.330 66.29000  ?  23  ALA A C   1 
ATOM   313  O  O   A ALA A 1 23  ? 49.19000 48.97500 -3.22400  0.670 74.55000  ?  23  ALA A O   1 
ATOM   314  O  O   B ALA A 1 23  ? 48.95100 48.74100 -3.78800  0.330 69.96000  ?  23  ALA A O   1 
ATOM   315  C  CB  A ALA A 1 23  ? 48.89900 45.74300 -2.58400  0.670 54.90000  ?  23  ALA A CB  1 
ATOM   316  C  CB  B ALA A 1 23  ? 48.88700 45.49700 -3.27900  0.330 56.39000  ?  23  ALA A CB  1 
ATOM   317  N  N   A TRP A 1 24  ? 48.76400 47.72200 -5.04900  0.670 67.58000  ?  24  TRP A N   1 
ATOM   318  N  N   B TRP A 1 24  ? 48.25800 47.64600 -5.61800  0.330 65.31000  ?  24  TRP A N   1 
ATOM   319  C  CA  A TRP A 1 24  ? 49.41500 48.66800 -5.94700  0.670 73.01000  ?  24  TRP A CA  1 
ATOM   320  C  CA  B TRP A 1 24  ? 49.02100 48.55500 -6.45400  0.330 69.37000  ?  24  TRP A CA  1 
ATOM   321  C  C   A TRP A 1 24  ? 48.71200 50.02000 -5.93600  0.670 70.59000  ?  24  TRP A C   1 
ATOM   322  C  C   B TRP A 1 24  ? 48.41200 49.94700 -6.50000  0.330 69.21000  ?  24  TRP A C   1 
ATOM   323  O  O   A TRP A 1 24  ? 49.34600 51.06500 -5.78100  0.670 82.39000  ?  24  TRP A O   1 
ATOM   324  O  O   B TRP A 1 24  ? 49.12700 50.94300 -6.36900  0.330 76.57000  ?  24  TRP A O   1 
ATOM   325  C  CB  A TRP A 1 24  ? 49.41600 48.12500 -7.36700  0.670 68.55000  ?  24  TRP A CB  1 
ATOM   326  C  CB  B TRP A 1 24  ? 49.18800 48.00400 -7.86200  0.330 68.06000  ?  24  TRP A CB  1 
ATOM   327  C  CG  A TRP A 1 24  ? 50.41600 48.79300 -8.22600  0.670 82.26000  ?  24  TRP A CG  1 
ATOM   328  C  CG  B TRP A 1 24  ? 50.35800 48.69200 -8.50300  0.330 81.46000  ?  24  TRP A CG  1 
ATOM   329  C  CD1 A TRP A 1 24  ? 50.19000 49.48300 -9.37600  0.670 81.50000  ?  24  TRP A CD1 1 
ATOM   330  C  CD1 B TRP A 1 24  ? 50.32700 49.56400 -9.56100  0.330 81.52000  ?  24  TRP A CD1 1 
ATOM   331  C  CD2 A TRP A 1 24  ? 51.82100 48.85500 -7.98800  0.670 93.77000  ?  24  TRP A CD2 1 
ATOM   332  C  CD2 B TRP A 1 24  ? 51.73600 48.63000 -8.06800  0.330 91.69000  ?  24  TRP A CD2 1 
ATOM   333  N  NE1 A TRP A 1 24  ? 51.37700 49.94700 -9.89000  0.670 88.62000  ?  24  TRP A NE1 1 
ATOM   334  N  NE1 B TRP A 1 24  ? 51.59600 50.04000 -9.82200  0.330 87.78000  ?  24  TRP A NE1 1 
ATOM   335  C  CE2 A TRP A 1 24  ? 52.39300 49.58500 -9.04500  0.670 94.87000  ?  24  TRP A CE2 1 
ATOM   336  C  CE2 B TRP A 1 24  ? 52.48300 49.48300 -8.93200  0.330 93.86000  ?  24  TRP A CE2 1 
ATOM   337  C  CE3 A TRP A 1 24  ? 52.65200 48.36300 -6.97900  0.670 98.78000  ?  24  TRP A CE3 1 
ATOM   338  C  CE3 B TRP A 1 24  ? 52.41300 47.92400 -7.04200  0.330 91.11000  ?  24  TRP A CE3 1 
ATOM   339  C  CZ2 A TRP A 1 24  ? 53.76000 49.83200 -9.12400  0.670 93.11000  ?  24  TRP A CZ2 1 
ATOM   340  C  CZ2 B TRP A 1 24  ? 53.88800 49.65600 -8.80300  0.330 93.12000  ?  24  TRP A CZ2 1 
ATOM   341  C  CZ3 A TRP A 1 24  ? 54.00700 48.60900 -7.05800  0.670 104.60000 ?  24  TRP A CZ3 1 
ATOM   342  C  CZ3 B TRP A 1 24  ? 53.80700 48.09600 -6.90800  0.330 97.85000  ?  24  TRP A CZ3 1 
ATOM   343  C  CH2 A TRP A 1 24  ? 54.54900 49.33600 -8.12300  0.670 95.22000  ?  24  TRP A CH2 1 
ATOM   344  C  CH2 B TRP A 1 24  ? 54.52900 48.96200 -7.79100  0.330 95.41000  ?  24  TRP A CH2 1 
ATOM   345  N  N   A ALA A 1 25  ? 47.39200 50.01700 -6.10900  0.670 61.08000  ?  25  ALA A N   1 
ATOM   346  N  N   B ALA A 1 25  ? 47.10400 50.05700 -6.65500  0.330 61.45000  ?  25  ALA A N   1 
ATOM   347  C  CA  A ALA A 1 25  ? 46.63900 51.26400 -6.13400  0.670 58.99000  ?  25  ALA A CA  1 
ATOM   348  C  CA  B ALA A 1 25  ? 46.57600 51.40100 -6.75700  0.330 60.88000  ?  25  ALA A CA  1 
ATOM   349  C  C   A ALA A 1 25  ? 46.74100 52.01200 -4.81700  0.670 73.67000  ?  25  ALA A C   1 
ATOM   350  C  C   B ALA A 1 25  ? 46.79200 52.19400 -5.47500  0.330 73.56000  ?  25  ALA A C   1 
ATOM   351  O  O   A ALA A 1 25  ? 46.56500 53.23300 -4.79400  0.670 78.03000  ?  25  ALA A O   1 
ATOM   352  O  O   B ALA A 1 25  ? 46.57800 53.40700 -5.47200  0.330 81.51000  ?  25  ALA A O   1 
ATOM   353  C  CB  A ALA A 1 25  ? 45.17300 50.97100 -6.46100  0.670 54.46000  ?  25  ALA A CB  1 
ATOM   354  C  CB  B ALA A 1 25  ? 45.10200 51.36300 -7.11700  0.330 52.88000  ?  25  ALA A CB  1 
ATOM   355  N  N   A GLY A 1 26  ? 47.01500 51.30900 -3.72200  0.670 76.22000  ?  26  GLY A N   1 
ATOM   356  N  N   B GLY A 1 26  ? 47.25800 51.55100 -4.40900  0.330 75.59000  ?  26  GLY A N   1 
ATOM   357  C  CA  A GLY A 1 26  ? 47.15100 51.95500 -2.43100  0.670 90.38000  ?  26  GLY A CA  1 
ATOM   358  C  CA  B GLY A 1 26  ? 47.30200 52.12700 -3.08000  0.330 86.89000  ?  26  GLY A CA  1 
ATOM   359  C  C   A GLY A 1 26  ? 48.48700 52.60700 -2.16400  0.670 109.57000 ?  26  GLY A C   1 
ATOM   360  C  C   B GLY A 1 26  ? 48.64200 52.63400 -2.59600  0.330 108.98000 ?  26  GLY A C   1 
ATOM   361  O  O   A GLY A 1 26  ? 48.60400 53.36200 -1.19400  0.670 121.73000 ?  26  GLY A O   1 
ATOM   362  O  O   B GLY A 1 26  ? 48.77900 52.92200 -1.39900  0.330 117.55000 ?  26  GLY A O   1 
ATOM   363  N  N   A ARG A 1 34  ? 44.34400 55.76300 2.70100   0.670 90.73000  ?  34  ARG A N   1 
ATOM   364  N  N   B ARG A 1 34  ? 44.27700 56.24700 2.27900   0.330 90.20000  ?  34  ARG A N   1 
ATOM   365  C  CA  A ARG A 1 34  ? 45.02700 54.48700 2.88300   0.670 87.50000  ?  34  ARG A CA  1 
ATOM   366  C  CA  B ARG A 1 34  ? 44.96000 54.95700 2.34000   0.330 85.77000  ?  34  ARG A CA  1 
ATOM   367  C  C   A ARG A 1 34  ? 44.11200 53.44500 3.51100   0.670 77.99000  ?  34  ARG A C   1 
ATOM   368  C  C   B ARG A 1 34  ? 44.03100 53.88500 2.94800   0.330 79.22000  ?  34  ARG A C   1 
ATOM   369  O  O   A ARG A 1 34  ? 44.22600 52.25200 3.20600   0.670 63.26000  ?  34  ARG A O   1 
ATOM   370  O  O   B ARG A 1 34  ? 44.18300 52.68100 2.68200   0.330 70.76000  ?  34  ARG A O   1 
ATOM   371  C  CB  A ARG A 1 34  ? 46.26900 54.69000 3.75600   0.670 93.32000  ?  34  ARG A CB  1 
ATOM   372  C  CB  B ARG A 1 34  ? 46.27000 55.17200 3.13500   0.330 93.03000  ?  34  ARG A CB  1 
ATOM   373  C  CG  A ARG A 1 34  ? 47.52100 53.97400 3.27700   0.670 107.60000 ?  34  ARG A CG  1 
ATOM   374  C  CG  B ARG A 1 34  ? 47.66900 54.92900 2.42200   0.330 100.74000 ?  34  ARG A CG  1 
ATOM   375  C  CD  A ARG A 1 34  ? 48.51800 53.77600 4.42000   0.670 118.14000 ?  34  ARG A CD  1 
ATOM   376  C  CD  B ARG A 1 34  ? 48.75800 54.72100 3.49700   0.330 113.68000 ?  34  ARG A CD  1 
ATOM   377  N  NE  A ARG A 1 34  ? 48.83600 55.02700 5.10800   0.670 125.27000 ?  34  ARG A NE  1 
ATOM   378  N  NE  B ARG A 1 34  ? 48.83600 55.82700 4.46100   0.330 120.01000 ?  34  ARG A NE  1 
ATOM   379  C  CZ  A ARG A 1 34  ? 49.69500 55.13100 6.11900   0.670 122.13000 ?  34  ARG A CZ  1 
ATOM   380  C  CZ  B ARG A 1 34  ? 49.51800 55.79100 5.60700   0.330 122.54000 ?  34  ARG A CZ  1 
ATOM   381  N  NH1 A ARG A 1 34  ? 50.32900 54.05700 6.57000   0.670 126.50000 ?  34  ARG A NH1 1 
ATOM   382  N  NH1 B ARG A 1 34  ? 50.08000 54.67500 6.04700   0.330 124.50000 ?  34  ARG A NH1 1 
ATOM   383  N  NH2 A ARG A 1 34  ? 49.92000 56.31100 6.68100   0.670 114.45000 ?  34  ARG A NH2 1 
ATOM   384  N  NH2 B ARG A 1 34  ? 49.59200 56.88800 6.36100   0.330 117.69000 ?  34  ARG A NH2 1 
ATOM   385  N  N   A ARG A 1 35  ? 43.19400 53.87700 4.38000   0.670 75.50000  ?  35  ARG A N   1 
ATOM   386  N  N   B ARG A 1 35  ? 43.01700 54.30300 3.71800   0.330 74.79000  ?  35  ARG A N   1 
ATOM   387  C  CA  A ARG A 1 35  ? 42.33400 52.93500 5.09100   0.670 77.14000  ?  35  ARG A CA  1 
ATOM   388  C  CA  B ARG A 1 35  ? 42.16900 53.32300 4.39800   0.330 71.16000  ?  35  ARG A CA  1 
ATOM   389  C  C   A ARG A 1 35  ? 41.56700 52.04500 4.12100   0.670 63.58000  ?  35  ARG A C   1 
ATOM   390  C  C   B ARG A 1 35  ? 41.35800 52.48600 3.43500   0.330 61.89000  ?  35  ARG A C   1 
ATOM   391  O  O   A ARG A 1 35  ? 41.52100 50.82000 4.28600   0.670 54.85000  ?  35  ARG A O   1 
ATOM   392  O  O   B ARG A 1 35  ? 41.10900 51.30000 3.69400   0.330 59.25000  ?  35  ARG A O   1 
ATOM   393  C  CB  A ARG A 1 35  ? 41.35900 53.69400 5.99000   0.670 74.82000  ?  35  ARG A CB  1 
ATOM   394  C  CB  B ARG A 1 35  ? 41.21300 53.98500 5.38600   0.330 76.81000  ?  35  ARG A CB  1 
ATOM   395  C  CG  A ARG A 1 35  ? 41.81700 53.86500 7.42500   0.670 86.12000  ?  35  ARG A CG  1 
ATOM   396  C  CG  B ARG A 1 35  ? 41.49900 53.66600 6.85000   0.330 81.03000  ?  35  ARG A CG  1 
ATOM   397  C  CD  A ARG A 1 35  ? 40.88600 54.80200 8.18900   0.670 96.17000  ?  35  ARG A CD  1 
ATOM   398  C  CD  B ARG A 1 35  ? 40.58700 54.50200 7.71600   0.330 91.68000  ?  35  ARG A CD  1 
ATOM   399  N  NE  A ARG A 1 35  ? 40.48600 55.95800 7.38700   0.670 105.60000 ?  35  ARG A NE  1 
ATOM   400  N  NE  B ARG A 1 35  ? 40.31900 55.73200 6.97600   0.330 98.66000  ?  35  ARG A NE  1 
ATOM   401  C  CZ  A ARG A 1 35  ? 39.52600 56.81300 7.72300   0.670 103.29000 ?  35  ARG A CZ  1 
ATOM   402  C  CZ  B ARG A 1 35  ? 39.50700 56.71100 7.35700   0.330 101.32000 ?  35  ARG A CZ  1 
ATOM   403  N  NH1 A ARG A 1 35  ? 38.85600 56.65100 8.85500   0.670 103.90000 ?  35  ARG A NH1 1 
ATOM   404  N  NH1 B ARG A 1 35  ? 38.91500 56.70400 8.54600   0.330 103.48000 ?  35  ARG A NH1 1 
ATOM   405  N  NH2 A ARG A 1 35  ? 39.23700 57.83100 6.92400   0.670 96.74000  ?  35  ARG A NH2 1 
ATOM   406  N  NH2 B ARG A 1 35  ? 39.31600 57.74500 6.53900   0.330 97.00000  ?  35  ARG A NH2 1 
ATOM   407  N  N   A TYR A 1 36  ? 40.94000 52.65000 3.11100   0.670 60.87000  ?  36  TYR A N   1 
ATOM   408  N  N   B TYR A 1 36  ? 40.86300 53.08500 2.36300   0.330 64.15000  ?  36  TYR A N   1 
ATOM   409  C  CA  A TYR A 1 36  ? 40.12900 51.88000 2.17500   0.670 65.91000  ?  36  TYR A CA  1 
ATOM   410  C  CA  B TYR A 1 36  ? 40.05500 52.28000 1.45900   0.330 60.81000  ?  36  TYR A CA  1 
ATOM   411  C  C   A TYR A 1 36  ? 40.97400 50.84000 1.45000   0.670 59.28000  ?  36  TYR A C   1 
ATOM   412  C  C   B TYR A 1 36  ? 40.89700 51.15400 0.89100   0.330 58.61000  ?  36  TYR A C   1 
ATOM   413  O  O   A TYR A 1 36  ? 40.60200 49.66300 1.37200   0.670 57.93000  ?  36  TYR A O   1 
ATOM   414  O  O   B TYR A 1 36  ? 40.63200 49.97200 1.14300   0.330 58.25000  ?  36  TYR A O   1 
ATOM   415  C  CB  A TYR A 1 36  ? 39.45700 52.81800 1.17200   0.670 60.18000  ?  36  TYR A CB  1 
ATOM   416  C  CB  B TYR A 1 36  ? 39.43300 53.13400 0.34900   0.330 63.32000  ?  36  TYR A CB  1 
ATOM   417  C  CG  A TYR A 1 36  ? 38.56800 53.86300 1.80400   0.670 56.00000  ?  36  TYR A CG  1 
ATOM   418  C  CG  B TYR A 1 36  ? 38.44600 54.18200 0.86800   0.330 61.82000  ?  36  TYR A CG  1 
ATOM   419  C  CD1 A TYR A 1 36  ? 37.22700 53.60500 2.05000   0.670 57.79000  ?  36  TYR A CD1 1 
ATOM   420  C  CD1 B TYR A 1 36  ? 38.87700 55.44900 1.25900   0.330 65.93000  ?  36  TYR A CD1 1 
ATOM   421  C  CD2 A TYR A 1 36  ? 39.07000 55.11000 2.15400   0.670 64.12000  ?  36  TYR A CD2 1 
ATOM   422  C  CD2 B TYR A 1 36  ? 37.08400 53.89900 0.95600   0.330 60.88000  ?  36  TYR A CD2 1 
ATOM   423  C  CE1 A TYR A 1 36  ? 36.41000 54.55600 2.62800   0.670 70.73000  ?  36  TYR A CE1 1 
ATOM   424  C  CE1 B TYR A 1 36  ? 37.98200 56.41000 1.71500   0.330 60.91000  ?  36  TYR A CE1 1 
ATOM   425  C  CE2 A TYR A 1 36  ? 38.26000 56.06900 2.73300   0.670 70.25000  ?  36  TYR A CE2 1 
ATOM   426  C  CE2 B TYR A 1 36  ? 36.17600 54.84900 1.42800   0.330 60.56000  ?  36  TYR A CE2 1 
ATOM   427  C  CZ  A TYR A 1 36  ? 36.93100 55.78600 2.96700   0.670 67.73000  ?  36  TYR A CZ  1 
ATOM   428  C  CZ  B TYR A 1 36  ? 36.64100 56.10200 1.80400   0.330 57.62000  ?  36  TYR A CZ  1 
ATOM   429  O  OH  A TYR A 1 36  ? 36.11500 56.73200 3.54200   0.670 70.01000  ?  36  TYR A OH  1 
ATOM   430  O  OH  B TYR A 1 36  ? 35.75600 57.04800 2.27600   0.330 64.82000  ?  36  TYR A OH  1 
ATOM   431  N  N   A TYR A 1 37  ? 42.12100 51.25800 0.91100   0.670 57.41000  ?  37  TYR A N   1 
ATOM   432  N  N   B TYR A 1 37  ? 41.98800 51.52200 0.22700   0.330 60.58000  ?  37  TYR A N   1 
ATOM   433  C  CA  A TYR A 1 37  ? 42.95500 50.33300 0.15300   0.670 62.22000  ?  37  TYR A CA  1 
ATOM   434  C  CA  B TYR A 1 37  ? 42.74600 50.59600 -0.60100  0.330 59.37000  ?  37  TYR A CA  1 
ATOM   435  C  C   A TYR A 1 37  ? 43.48500 49.21200 1.03900   0.670 63.01000  ?  37  TYR A C   1 
ATOM   436  C  C   B TYR A 1 37  ? 43.29300 49.41200 0.21100   0.330 59.64000  ?  37  TYR A C   1 
ATOM   437  O  O   A TYR A 1 37  ? 43.57600 48.05800 0.60400   0.670 58.30000  ?  37  TYR A O   1 
ATOM   438  O  O   B TYR A 1 37  ? 43.43500 48.30000 -0.33200  0.330 52.24000  ?  37  TYR A O   1 
ATOM   439  C  CB  A TYR A 1 37  ? 44.10600 51.09200 -0.50600  0.670 63.19000  ?  37  TYR A CB  1 
ATOM   440  C  CB  B TYR A 1 37  ? 43.88500 51.37300 -1.27700  0.330 65.57000  ?  37  TYR A CB  1 
ATOM   441  C  CG  A TYR A 1 37  ? 43.67500 52.01300 -1.62600  0.670 69.07000  ?  37  TYR A CG  1 
ATOM   442  C  CG  B TYR A 1 37  ? 43.52000 52.54000 -2.22600  0.330 66.45000  ?  37  TYR A CG  1 
ATOM   443  C  CD1 A TYR A 1 37  ? 43.49100 51.53000 -2.91500  0.670 62.86000  ?  37  TYR A CD1 1 
ATOM   444  C  CD1 B TYR A 1 37  ? 43.30400 52.32600 -3.55900  0.330 61.36000  ?  37  TYR A CD1 1 
ATOM   445  C  CD2 A TYR A 1 37  ? 43.45300 53.36300 -1.39500  0.670 68.98000  ?  37  TYR A CD2 1 
ATOM   446  C  CD2 B TYR A 1 37  ? 43.44400 53.85600 -1.77300  0.330 66.83000  ?  37  TYR A CD2 1 
ATOM   447  C  CE1 A TYR A 1 37  ? 43.09900 52.36700 -3.94200  0.670 61.70000  ?  37  TYR A CE1 1 
ATOM   448  C  CE1 B TYR A 1 37  ? 43.01700 53.36600 -4.42400  0.330 63.22000  ?  37  TYR A CE1 1 
ATOM   449  C  CE2 A TYR A 1 37  ? 43.06100 54.20900 -2.41500  0.670 65.17000  ?  37  TYR A CE2 1 
ATOM   450  C  CE2 B TYR A 1 37  ? 43.15300 54.91100 -2.64200  0.330 66.51000  ?  37  TYR A CE2 1 
ATOM   451  C  CZ  A TYR A 1 37  ? 42.88600 53.70500 -3.68700  0.670 59.47000  ?  37  TYR A CZ  1 
ATOM   452  C  CZ  B TYR A 1 37  ? 42.93400 54.65100 -3.97300  0.330 65.30000  ?  37  TYR A CZ  1 
ATOM   453  O  OH  A TYR A 1 37  ? 42.49400 54.54200 -4.70700  0.670 60.61000  ?  37  TYR A OH  1 
ATOM   454  O  OH  B TYR A 1 37  ? 42.63300 55.66000 -4.87600  0.330 65.09000  ?  37  TYR A OH  1 
ATOM   455  N  N   A VAL A 1 38  ? 43.83700 49.52700 2.28600   0.670 50.46000  ?  38  VAL A N   1 
ATOM   456  N  N   B VAL A 1 38  ? 43.60400 49.62900 1.50800   0.330 59.63000  ?  38  VAL A N   1 
ATOM   457  C  CA  A VAL A 1 38  ? 44.33500 48.49300 3.18800   0.670 53.33000  ?  38  VAL A CA  1 
ATOM   458  C  CA  B VAL A 1 38  ? 44.08900 48.54000 2.36200   0.330 52.41000  ?  38  VAL A CA  1 
ATOM   459  C  C   A VAL A 1 38  ? 43.23000 47.49700 3.51700   0.670 53.08000  ?  38  VAL A C   1 
ATOM   460  C  C   B VAL A 1 38  ? 42.95000 47.58400 2.72400   0.330 50.75000  ?  38  VAL A C   1 
ATOM   461  O  O   A VAL A 1 38  ? 43.48200 46.29600 3.66700   0.670 48.73000  ?  38  VAL A O   1 
ATOM   462  O  O   B VAL A 1 38  ? 43.13900 46.35800 2.76600   0.330 44.28000  ?  38  VAL A O   1 
ATOM   463  C  CB  A VAL A 1 38  ? 44.92400 49.13000 4.46000   0.670 60.02000  ?  38  VAL A CB  1 
ATOM   464  C  CB  B VAL A 1 38  ? 44.76700 49.11400 3.61600   0.330 55.75000  ?  38  VAL A CB  1 
ATOM   465  C  CG1 A VAL A 1 38  ? 45.22100 48.06300 5.50300   0.670 46.76000  ?  38  VAL A CG1 1 
ATOM   466  C  CG1 B VAL A 1 38  ? 45.09900 48.00500 4.61600   0.330 54.73000  ?  38  VAL A CG1 1 
ATOM   467  C  CG2 A VAL A 1 38  ? 46.17700 49.92500 4.11700   0.670 59.74000  ?  38  VAL A CG2 1 
ATOM   468  C  CG2 B VAL A 1 38  ? 45.99700 49.87400 3.25400   0.330 53.86000  ?  38  VAL A CG2 1 
ATOM   469  N  N   A THR A 1 39  ? 41.98900 47.97700 3.63800   0.670 45.58000  ?  39  THR A N   1 
ATOM   470  N  N   B THR A 1 39  ? 41.74600 48.13200 2.96200   0.330 48.17000  ?  39  THR A N   1 
ATOM   471  C  CA  A THR A 1 39  ? 40.87700 47.07300 3.91300   0.670 49.56000  ?  39  THR A CA  1 
ATOM   472  C  CA  B THR A 1 39  ? 40.55800 47.32000 3.21400   0.330 47.15000  ?  39  THR A CA  1 
ATOM   473  C  C   A THR A 1 39  ? 40.64800 46.12000 2.74700   0.670 45.45000  ?  39  THR A C   1 
ATOM   474  C  C   B THR A 1 39  ? 40.33000 46.31200 2.10400   0.330 44.26000  ?  39  THR A C   1 
ATOM   475  O  O   A THR A 1 39  ? 40.44200 44.91900 2.95000   0.670 41.23000  ?  39  THR A O   1 
ATOM   476  O  O   B THR A 1 39  ? 40.06800 45.12500 2.36500   0.330 41.66000  ?  39  THR A O   1 
ATOM   477  C  CB  A THR A 1 39  ? 39.60800 47.87500 4.20700   0.670 43.10000  ?  39  THR A CB  1 
ATOM   478  C  CB  B THR A 1 39  ? 39.33600 48.21900 3.35500   0.330 44.18000  ?  39  THR A CB  1 
ATOM   479  O  OG1 A THR A 1 39  ? 39.87300 48.82200 5.25000   0.670 47.66000  ?  39  THR A OG1 1 
ATOM   480  O  OG1 B THR A 1 39  ? 39.69100 49.40200 4.08700   0.330 40.70000  ?  39  THR A OG1 1 
ATOM   481  C  CG2 A THR A 1 39  ? 38.47000 46.95600 4.63600   0.670 46.41000  ?  39  THR A CG2 1 
ATOM   482  C  CG2 B THR A 1 39  ? 38.25500 47.49900 4.11800   0.330 43.91000  ?  39  THR A CG2 1 
ATOM   483  N  N   A LEU A 1 40  ? 40.69700 46.63200 1.51800   0.670 45.58000  ?  40  LEU A N   1 
ATOM   484  N  N   B LEU A 1 40  ? 40.47100 46.75700 0.85300   0.330 45.26000  ?  40  LEU A N   1 
ATOM   485  C  CA  A LEU A 1 40  ? 40.48200 45.77000 0.36100   0.670 42.66000  ?  40  LEU A CA  1 
ATOM   486  C  CA  B LEU A 1 40  ? 40.36900 45.83700 -0.26800  0.330 40.05000  ?  40  LEU A CA  1 
ATOM   487  C  C   A LEU A 1 40  ? 41.58100 44.72000 0.24900   0.670 40.99000  ?  40  LEU A C   1 
ATOM   488  C  C   B LEU A 1 40  ? 41.46400 44.79100 -0.23600  0.330 39.56000  ?  40  LEU A C   1 
ATOM   489  O  O   A LEU A 1 40  ? 41.32000 43.57600 -0.14600  0.670 43.33000  ?  40  LEU A O   1 
ATOM   490  O  O   B LEU A 1 40  ? 41.18000 43.59900 -0.42900  0.330 41.93000  ?  40  LEU A O   1 
ATOM   491  C  CB  A LEU A 1 40  ? 40.39200 46.62000 -0.90500  0.670 42.41000  ?  40  LEU A CB  1 
ATOM   492  C  CB  B LEU A 1 40  ? 40.39100 46.62200 -1.55700  0.330 43.55000  ?  40  LEU A CB  1 
ATOM   493  C  CG  A LEU A 1 40  ? 39.10200 47.44700 -0.94200  0.670 34.12000  ?  40  LEU A CG  1 
ATOM   494  C  CG  B LEU A 1 40  ? 39.07900 47.37600 -1.51700  0.330 40.40000  ?  40  LEU A CG  1 
ATOM   495  C  CD1 A LEU A 1 40  ? 39.22500 48.54900 -1.97600  0.670 46.57000  ?  40  LEU A CD1 1 
ATOM   496  C  CD1 B LEU A 1 40  ? 39.11400 48.36900 -2.65800  0.330 39.12000  ?  40  LEU A CD1 1 
ATOM   497  C  CD2 A LEU A 1 40  ? 37.89800 46.55900 -1.21400  0.670 39.06000  ?  40  LEU A CD2 1 
ATOM   498  C  CD2 B LEU A 1 40  ? 37.85100 46.41400 -1.62300  0.330 37.83000  ?  40  LEU A CD2 1 
ATOM   499  N  N   A VAL A 1 41  ? 42.81900 45.08200 0.58900   0.670 35.88000  ?  41  VAL A N   1 
ATOM   500  N  N   B VAL A 1 41  ? 42.71900 45.20000 0.00700   0.330 39.29000  ?  41  VAL A N   1 
ATOM   501  C  CA  A VAL A 1 41  ? 43.88300 44.08100 0.59500   0.670 34.60000  ?  41  VAL A CA  1 
ATOM   502  C  CA  B VAL A 1 41  ? 43.80800 44.22500 -0.05300  0.330 40.72000  ?  41  VAL A CA  1 
ATOM   503  C  C   A VAL A 1 41  ? 43.56000 42.97900 1.59800   0.670 43.69000  ?  41  VAL A C   1 
ATOM   504  C  C   B VAL A 1 41  ? 43.57000 43.12300 0.95400   0.330 40.80000  ?  41  VAL A C   1 
ATOM   505  O  O   A VAL A 1 41  ? 43.76400 41.78900 1.32700   0.670 42.75000  ?  41  VAL A O   1 
ATOM   506  O  O   B VAL A 1 41  ? 43.95100 41.96300 0.72000   0.330 37.55000  ?  41  VAL A O   1 
ATOM   507  C  CB  A VAL A 1 41  ? 45.24900 44.73000 0.88900   0.670 34.96000  ?  41  VAL A CB  1 
ATOM   508  C  CB  B VAL A 1 41  ? 45.18000 44.87200 0.17800   0.330 43.19000  ?  41  VAL A CB  1 
ATOM   509  C  CG1 A VAL A 1 41  ? 46.30800 43.65500 1.13200   0.670 38.67000  ?  41  VAL A CG1 1 
ATOM   510  C  CG1 B VAL A 1 41  ? 46.24300 43.78800 0.17200   0.330 41.71000  ?  41  VAL A CG1 1 
ATOM   511  C  CG2 A VAL A 1 41  ? 45.66100 45.63500 -0.26000  0.670 43.66000  ?  41  VAL A CG2 1 
ATOM   512  C  CG2 B VAL A 1 41  ? 45.49600 45.92300 -0.88200  0.330 42.62000  ?  41  VAL A CG2 1 
ATOM   513  N  N   A GLY A 1 42  ? 43.04400 43.35600 2.76900   0.670 35.87000  ?  42  GLY A N   1 
ATOM   514  N  N   B GLY A 1 42  ? 42.88600 43.46300 2.06600   0.330 40.41000  ?  42  GLY A N   1 
ATOM   515  C  CA  A GLY A 1 42  ? 42.67900 42.35600 3.75800   0.670 38.02000  ?  42  GLY A CA  1 
ATOM   516  C  CA  B GLY A 1 42  ? 42.54000 42.53400 3.12200   0.330 38.75000  ?  42  GLY A CA  1 
ATOM   517  C  C   A GLY A 1 42  ? 41.53700 41.47100 3.29800   0.670 42.92000  ?  42  GLY A C   1 
ATOM   518  C  C   B GLY A 1 42  ? 41.33500 41.68900 2.75300   0.330 42.22000  ?  42  GLY A C   1 
ATOM   519  O  O   A GLY A 1 42  ? 41.55500 40.25500 3.51300   0.670 43.48000  ?  42  GLY A O   1 
ATOM   520  O  O   B GLY A 1 42  ? 41.33700 40.45600 2.93700   0.330 42.89000  ?  42  GLY A O   1 
ATOM   521  N  N   A ILE A 1 43  ? 40.53900 42.06600 2.64000   0.670 42.39000  ?  43  ILE A N   1 
ATOM   522  N  N   B ILE A 1 43  ? 40.29800 42.34600 2.21200   0.330 40.39000  ?  43  ILE A N   1 
ATOM   523  C  CA  A ILE A 1 43  ? 39.37700 41.30400 2.19000   0.670 41.80000  ?  43  ILE A CA  1 
ATOM   524  C  CA  B ILE A 1 43  ? 39.09700 41.60900 1.81700   0.330 42.22000  ?  43  ILE A CA  1 
ATOM   525  C  C   A ILE A 1 43  ? 39.79800 40.20100 1.22800   0.670 34.52000  ?  43  ILE A C   1 
ATOM   526  C  C   B ILE A 1 43  ? 39.48900 40.38300 1.01800   0.330 35.68000  ?  43  ILE A C   1 
ATOM   527  O  O   A ILE A 1 43  ? 39.42700 39.03500 1.39300   0.670 40.86000  ?  43  ILE A O   1 
ATOM   528  O  O   B ILE A 1 43  ? 39.05400 39.26500 1.30100   0.330 40.01000  ?  43  ILE A O   1 
ATOM   529  C  CB  A ILE A 1 43  ? 38.33900 42.24000 1.54500   0.670 43.91000  ?  43  ILE A CB  1 
ATOM   530  C  CB  B ILE A 1 43  ? 38.11900 42.50300 1.02600   0.330 40.44000  ?  43  ILE A CB  1 
ATOM   531  C  CG1 A ILE A 1 43  ? 37.66500 43.10100 2.61100   0.670 34.47000  ?  43  ILE A CG1 1 
ATOM   532  C  CG1 B ILE A 1 43  ? 37.35200 43.43800 1.96800   0.330 35.13000  ?  43  ILE A CG1 1 
ATOM   533  C  CG2 A ILE A 1 43  ? 37.31600 41.44000 0.75800   0.670 32.70000  ?  43  ILE A CG2 1 
ATOM   534  C  CG2 B ILE A 1 43  ? 37.15100 41.62200 0.22700   0.330 35.68000  ?  43  ILE A CG2 1 
ATOM   535  C  CD1 A ILE A 1 43  ? 37.05800 44.37300 2.07100   0.670 32.20000  ?  43  ILE A CD1 1 
ATOM   536  C  CD1 B ILE A 1 43  ? 36.73100 44.60000 1.33300   0.330 25.92000  ?  43  ILE A CD1 1 
ATOM   537  N  N   A SER A 1 44  ? 40.54500 40.55200 0.18600   0.670 35.36000  ?  44  SER A N   1 
ATOM   538  N  N   B SER A 1 44  ? 40.39100 40.56300 0.07200   0.330 36.02000  ?  44  SER A N   1 
ATOM   539  C  CA  A SER A 1 44  ? 40.93600 39.54700 -0.79500  0.670 39.96000  ?  44  SER A CA  1 
ATOM   540  C  CA  B SER A 1 44  ? 40.75400 39.48100 -0.82500  0.330 39.26000  ?  44  SER A CA  1 
ATOM   541  C  C   A SER A 1 44  ? 42.17700 38.77300 -0.37800  0.670 43.38000  ?  44  SER A C   1 
ATOM   542  C  C   B SER A 1 44  ? 42.08800 38.85900 -0.48800  0.330 39.71000  ?  44  SER A C   1 
ATOM   543  O  O   A SER A 1 44  ? 42.32100 37.60100 -0.74800  0.670 39.86000  ?  44  SER A O   1 
ATOM   544  O  O   B SER A 1 44  ? 42.24500 37.65200 -0.70700  0.330 40.04000  ?  44  SER A O   1 
ATOM   545  C  CB  A SER A 1 44  ? 41.16800 40.19500 -2.16200  0.670 38.96000  ?  44  SER A CB  1 
ATOM   546  C  CB  B SER A 1 44  ? 40.68600 39.96400 -2.28700  0.330 39.18000  ?  44  SER A CB  1 
ATOM   547  O  OG  A SER A 1 44  ? 42.02900 41.31200 -2.06600  0.670 47.21000  ?  44  SER A OG  1 
ATOM   548  O  OG  B SER A 1 44  ? 40.73300 41.37500 -2.36300  0.330 40.54000  ?  44  SER A OG  1 
ATOM   549  N  N   A GLY A 1 45  ? 43.05900 39.39100 0.40900   0.670 36.55000  ?  45  GLY A N   1 
ATOM   550  N  N   B GLY A 1 45  ? 43.02200 39.60900 0.09700   0.330 36.36000  ?  45  GLY A N   1 
ATOM   551  C  CA  A GLY A 1 45  ? 44.24200 38.68600 0.86800   0.670 32.17000  ?  45  GLY A CA  1 
ATOM   552  C  CA  B GLY A 1 45  ? 44.17100 38.94000 0.67800   0.330 33.50000  ?  45  GLY A CA  1 
ATOM   553  C  C   A GLY A 1 45  ? 43.91300 37.52600 1.78500   0.670 36.99000  ?  45  GLY A C   1 
ATOM   554  C  C   B GLY A 1 45  ? 43.69300 37.91000 1.67600   0.330 35.79000  ?  45  GLY A C   1 
ATOM   555  O  O   A GLY A 1 45  ? 44.49900 36.44800 1.67000   0.670 39.36000  ?  45  GLY A O   1 
ATOM   556  O  O   B GLY A 1 45  ? 44.07200 36.72700 1.61500   0.330 37.49000  ?  45  GLY A O   1 
ATOM   557  N  N   A ILE A 1 46  ? 42.97700 37.73100 2.71400   0.670 34.88000  ?  46  ILE A N   1 
ATOM   558  N  N   B ILE A 1 46  ? 42.80500 38.32800 2.58000   0.330 31.81000  ?  46  ILE A N   1 
ATOM   559  C  CA  A ILE A 1 46  ? 42.57400 36.64400 3.59700   0.670 34.64000  ?  46  ILE A CA  1 
ATOM   560  C  CA  B ILE A 1 46  ? 42.39500 37.33000 3.54800   0.330 37.43000  ?  46  ILE A CA  1 
ATOM   561  C  C   A ILE A 1 46  ? 41.90200 35.53600 2.79600   0.670 39.28000  ?  46  ILE A C   1 
ATOM   562  C  C   B ILE A 1 46  ? 41.72800 36.22500 2.79200   0.330 36.68000  ?  46  ILE A C   1 
ATOM   563  O  O   A ILE A 1 46  ? 42.18500 34.34900 2.99500   0.670 46.55000  ?  46  ILE A O   1 
ATOM   564  O  O   B ILE A 1 46  ? 41.79800 35.06100 3.19700   0.330 41.14000  ?  46  ILE A O   1 
ATOM   565  C  CB  A ILE A 1 46  ? 41.65600 37.17700 4.71200   0.670 33.22000  ?  46  ILE A CB  1 
ATOM   566  C  CB  B ILE A 1 46  ? 41.49500 37.93800 4.62700   0.330 35.14000  ?  46  ILE A CB  1 
ATOM   567  C  CG1 A ILE A 1 46  ? 42.45700 38.03800 5.69300   0.670 31.59000  ?  46  ILE A CG1 1 
ATOM   568  C  CG1 B ILE A 1 46  ? 42.35500 38.88200 5.42300   0.330 36.03000  ?  46  ILE A CG1 1 
ATOM   569  C  CG2 A ILE A 1 46  ? 40.98600 36.02400 5.44700   0.670 30.41000  ?  46  ILE A CG2 1 
ATOM   570  C  CG2 B ILE A 1 46  ? 40.85100 36.85900 5.47100   0.330 31.87000  ?  46  ILE A CG2 1 
ATOM   571  C  CD1 A ILE A 1 46  ? 41.61500 38.95800 6.55400   0.670 35.95000  ?  46  ILE A CD1 1 
ATOM   572  C  CD1 B ILE A 1 46  ? 41.57200 39.99800 6.18000   0.330 36.08000  ?  46  ILE A CD1 1 
ATOM   573  N  N   A ALA A 1 47  ? 41.01400 35.90400 1.86900   0.670 33.95000  ?  47  ALA A N   1 
ATOM   574  N  N   B ALA A 1 47  ? 41.14600 36.57100 1.63300   0.330 32.92000  ?  47  ALA A N   1 
ATOM   575  C  CA  A ALA A 1 47  ? 40.34600 34.89600 1.05200   0.670 29.80000  ?  47  ALA A CA  1 
ATOM   576  C  CA  B ALA A 1 47  ? 40.47600 35.61900 0.76200   0.330 33.92000  ?  47  ALA A CA  1 
ATOM   577  C  C   A ALA A 1 47  ? 41.35100 34.11700 0.21100   0.670 35.31000  ?  47  ALA A C   1 
ATOM   578  C  C   B ALA A 1 47  ? 41.43700 34.90200 -0.15900  0.330 34.11000  ?  47  ALA A C   1 
ATOM   579  O  O   A ALA A 1 47  ? 41.22100 32.89800 0.05200   0.670 33.93000  ?  47  ALA A O   1 
ATOM   580  O  O   B ALA A 1 47  ? 41.10000 33.82500 -0.65000  0.330 31.14000  ?  47  ALA A O   1 
ATOM   581  C  CB  A ALA A 1 47  ? 39.28900 35.55700 0.16700   0.670 26.56000  ?  47  ALA A CB  1 
ATOM   582  C  CB  B ALA A 1 47  ? 39.40200 36.33000 -0.06300  0.330 33.89000  ?  47  ALA A CB  1 
ATOM   583  N  N   A ALA A 1 48  ? 42.36400 34.79800 -0.33100  0.670 29.79000  ?  48  ALA A N   1 
ATOM   584  N  N   B ALA A 1 48  ? 42.61700 35.45100 -0.43700  0.330 30.11000  ?  48  ALA A N   1 
ATOM   585  C  CA  A ALA A 1 48  ? 43.40900 34.09000 -1.06400  0.670 35.32000  ?  48  ALA A CA  1 
ATOM   586  C  CA  B ALA A 1 48  ? 43.53000 34.62900 -1.23800  0.330 40.48000  ?  48  ALA A CA  1 
ATOM   587  C  C   A ALA A 1 48  ? 43.96600 32.94200 -0.22900  0.670 41.10000  ?  48  ALA A C   1 
ATOM   588  C  C   B ALA A 1 48  ? 43.98800 33.44000 -0.42000  0.330 37.51000  ?  48  ALA A C   1 
ATOM   589  O  O   A ALA A 1 48  ? 44.02600 31.79400 -0.68400  0.670 39.14000  ?  48  ALA A O   1 
ATOM   590  O  O   B ALA A 1 48  ? 43.84300 32.28300 -0.85100  0.330 37.55000  ?  48  ALA A O   1 
ATOM   591  C  CB  A ALA A 1 48  ? 44.52800 35.05500 -1.45900  0.670 45.50000  ?  48  ALA A CB  1 
ATOM   592  C  CB  B ALA A 1 48  ? 44.70800 35.45600 -1.77300  0.330 42.44000  ?  48  ALA A CB  1 
ATOM   593  N  N   A VAL A 1 49  ? 44.35900 33.23400 1.01200   0.670 41.96000  ?  49  VAL A N   1 
ATOM   594  N  N   B VAL A 1 49  ? 44.41600 33.72300 0.83300   0.330 39.27000  ?  49  VAL A N   1 
ATOM   595  C  CA  A VAL A 1 49  ? 44.95600 32.21000 1.86500   0.670 32.70000  ?  49  VAL A CA  1 
ATOM   596  C  CA  B VAL A 1 49  ? 44.83200 32.76900 1.86400   0.330 37.23000  ?  49  VAL A CA  1 
ATOM   597  C  C   A VAL A 1 49  ? 43.97500 31.06500 2.09400   0.670 41.74000  ?  49  VAL A C   1 
ATOM   598  C  C   B VAL A 1 49  ? 43.91300 31.56200 1.98300   0.330 40.11000  ?  49  VAL A C   1 
ATOM   599  O  O   A VAL A 1 49  ? 44.33500 29.88700 1.99300   0.670 46.98000  ?  49  VAL A O   1 
ATOM   600  O  O   B VAL A 1 49  ? 44.34600 30.42700 1.75500   0.330 41.57000  ?  49  VAL A O   1 
ATOM   601  C  CB  A VAL A 1 49  ? 45.42500 32.82800 3.19600   0.670 40.29000  ?  49  VAL A CB  1 
ATOM   602  C  CB  B VAL A 1 49  ? 44.90800 33.44400 3.23500   0.330 39.65000  ?  49  VAL A CB  1 
ATOM   603  C  CG1 A VAL A 1 49  ? 45.82000 31.73600 4.18300   0.670 30.45000  ?  49  VAL A CG1 1 
ATOM   604  C  CG1 B VAL A 1 49  ? 45.22200 32.35900 4.30800   0.330 31.88000  ?  49  VAL A CG1 1 
ATOM   605  C  CG2 A VAL A 1 49  ? 46.58300 33.78700 2.95300   0.670 39.66000  ?  49  VAL A CG2 1 
ATOM   606  C  CG2 B VAL A 1 49  ? 45.92300 34.58300 3.20700   0.330 36.54000  ?  49  VAL A CG2 1 
ATOM   607  N  N   A ALA A 1 50  ? 42.72000 31.39200 2.41000   0.670 39.29000  ?  50  ALA A N   1 
ATOM   608  N  N   B ALA A 1 50  ? 42.65000 31.79200 2.39500   0.330 37.11000  ?  50  ALA A N   1 
ATOM   609  C  CA  A ALA A 1 50  ? 41.73900 30.33900 2.66000   0.670 24.88000  ?  50  ALA A CA  1 
ATOM   610  C  CA  B ALA A 1 50  ? 41.68600 30.69700 2.46500   0.330 32.69000  ?  50  ALA A CA  1 
ATOM   611  C  C   A ALA A 1 50  ? 41.60500 29.41600 1.45600   0.670 41.51000  ?  50  ALA A C   1 
ATOM   612  C  C   B ALA A 1 50  ? 41.68200 29.87000 1.17900   0.330 40.80000  ?  50  ALA A C   1 
ATOM   613  O  O   A ALA A 1 50  ? 41.52800 28.19200 1.60500   0.670 41.75000  ?  50  ALA A O   1 
ATOM   614  O  O   B ALA A 1 50  ? 41.59700 28.63700 1.24400   0.330 42.44000  ?  50  ALA A O   1 
ATOM   615  C  CB  A ALA A 1 50  ? 40.38600 30.95200 3.02000   0.670 35.59000  ?  50  ALA A CB  1 
ATOM   616  C  CB  B ALA A 1 50  ? 40.27700 31.24200 2.73000   0.330 36.38000  ?  50  ALA A CB  1 
ATOM   617  N  N   A TYR A 1 51  ? 41.59300 29.98000 0.24900   0.670 35.73000  ?  51  TYR A N   1 
ATOM   618  N  N   B TYR A 1 51  ? 41.83000 30.52200 0.00400   0.330 31.97000  ?  51  TYR A N   1 
ATOM   619  C  CA  A TYR A 1 51  ? 41.41100 29.15100 -0.93800  0.670 32.68000  ?  51  TYR A CA  1 
ATOM   620  C  CA  B TYR A 1 51  ? 41.58800 29.78600 -1.22400  0.330 37.70000  ?  51  TYR A CA  1 
ATOM   621  C  C   A TYR A 1 51  ? 42.63500 28.28500 -1.21500  0.670 36.90000  ?  51  TYR A C   1 
ATOM   622  C  C   B TYR A 1 51  ? 42.68800 28.78200 -1.47300  0.330 37.45000  ?  51  TYR A C   1 
ATOM   623  O  O   A TYR A 1 51  ? 42.49700 27.12500 -1.62100  0.670 32.21000  ?  51  TYR A O   1 
ATOM   624  O  O   B TYR A 1 51  ? 42.40000 27.65900 -1.89500  0.330 33.87000  ?  51  TYR A O   1 
ATOM   625  C  CB  A TYR A 1 51  ? 41.07200 30.03600 -2.13300  0.670 37.75000  ?  51  TYR A CB  1 
ATOM   626  C  CB  B TYR A 1 51  ? 41.31500 30.75100 -2.39800  0.330 36.14000  ?  51  TYR A CB  1 
ATOM   627  C  CG  A TYR A 1 51  ? 39.58200 30.22800 -2.28600  0.670 31.92000  ?  51  TYR A CG  1 
ATOM   628  C  CG  B TYR A 1 51  ? 39.79800 30.85800 -2.43600  0.330 32.52000  ?  51  TYR A CG  1 
ATOM   629  C  CD1 A TYR A 1 51  ? 38.78400 29.20800 -2.78500  0.670 37.54000  ?  51  TYR A CD1 1 
ATOM   630  C  CD1 B TYR A 1 51  ? 39.08700 29.78200 -2.89900  0.330 33.69000  ?  51  TYR A CD1 1 
ATOM   631  C  CD2 A TYR A 1 51  ? 38.96800 31.41500 -1.91000  0.670 32.47000  ?  51  TYR A CD2 1 
ATOM   632  C  CD2 B TYR A 1 51  ? 39.07600 31.94200 -1.85800  0.330 32.29000  ?  51  TYR A CD2 1 
ATOM   633  C  CE1 A TYR A 1 51  ? 37.42300 29.36800 -2.91600  0.670 28.52000  ?  51  TYR A CE1 1 
ATOM   634  C  CE1 B TYR A 1 51  ? 37.73900 29.76700 -2.90000  0.330 32.24000  ?  51  TYR A CE1 1 
ATOM   635  C  CE2 A TYR A 1 51  ? 37.60200 31.58400 -2.04200  0.670 35.43000  ?  51  TYR A CE2 1 
ATOM   636  C  CE2 B TYR A 1 51  ? 37.68300 31.94100 -1.85000  0.330 33.58000  ?  51  TYR A CE2 1 
ATOM   637  C  CZ  A TYR A 1 51  ? 36.83600 30.55500 -2.54400  0.670 32.25000  ?  51  TYR A CZ  1 
ATOM   638  C  CZ  B TYR A 1 51  ? 37.04100 30.81500 -2.40500  0.330 33.85000  ?  51  TYR A CZ  1 
ATOM   639  O  OH  A TYR A 1 51  ? 35.47600 30.70700 -2.68200  0.670 36.95000  ?  51  TYR A OH  1 
ATOM   640  O  OH  B TYR A 1 51  ? 35.69100 30.63000 -2.46200  0.330 34.39000  ?  51  TYR A OH  1 
ATOM   641  N  N   A VAL A 1 52  ? 43.83900 28.81200 -0.98700  0.670 45.34000  ?  52  VAL A N   1 
ATOM   642  N  N   B VAL A 1 52  ? 43.93400 29.11600 -1.10900  0.330 43.37000  ?  52  VAL A N   1 
ATOM   643  C  CA  A VAL A 1 52  ? 45.03700 27.99100 -1.15800  0.670 42.11000  ?  52  VAL A CA  1 
ATOM   644  C  CA  B VAL A 1 52  ? 45.02000 28.11700 -1.14900  0.330 41.95000  ?  52  VAL A CA  1 
ATOM   645  C  C   A VAL A 1 52  ? 45.00000 26.80600 -0.20000  0.670 47.67000  ?  52  VAL A C   1 
ATOM   646  C  C   B VAL A 1 52  ? 44.90200 27.11600 0.00200   0.330 45.23000  ?  52  VAL A C   1 
ATOM   647  O  O   A VAL A 1 52  ? 45.21900 25.65500 -0.59700  0.670 48.17000  ?  52  VAL A O   1 
ATOM   648  O  O   B VAL A 1 52  ? 45.06100 25.89500 -0.20700  0.330 48.38000  ?  52  VAL A O   1 
ATOM   649  C  CB  A VAL A 1 52  ? 46.30800 28.83500 -0.95500  0.670 38.87000  ?  52  VAL A CB  1 
ATOM   650  C  CB  B VAL A 1 52  ? 46.39800 28.77200 -1.08300  0.330 39.15000  ?  52  VAL A CB  1 
ATOM   651  C  CG1 A VAL A 1 52  ? 47.53300 27.92600 -0.90800  0.670 34.05000  ?  52  VAL A CG1 1 
ATOM   652  C  CG1 B VAL A 1 52  ? 47.46500 27.66500 -1.13300  0.330 35.17000  ?  52  VAL A CG1 1 
ATOM   653  C  CG2 A VAL A 1 52  ? 46.45200 29.87100 -2.05400  0.670 34.13000  ?  52  VAL A CG2 1 
ATOM   654  C  CG2 B VAL A 1 52  ? 46.53100 29.84400 -2.16500  0.330 38.33000  ?  52  VAL A CG2 1 
ATOM   655  N  N   A VAL A 1 53  ? 44.71800 27.07200 1.07700   0.670 39.21000  ?  53  VAL A N   1 
ATOM   656  N  N   B VAL A 1 53  ? 44.71700 27.61600 1.24700   0.330 35.98000  ?  53  VAL A N   1 
ATOM   657  C  CA  A VAL A 1 53  ? 44.63900 26.00100 2.06900   0.670 35.72000  ?  53  VAL A CA  1 
ATOM   658  C  CA  B VAL A 1 53  ? 44.36200 26.73200 2.35400   0.330 39.16000  ?  53  VAL A CA  1 
ATOM   659  C  C   A VAL A 1 53  ? 43.66400 24.92900 1.60300   0.670 38.68000  ?  53  VAL A C   1 
ATOM   660  C  C   B VAL A 1 53  ? 43.42100 25.63500 1.87400   0.330 39.79000  ?  53  VAL A C   1 
ATOM   661  O  O   A VAL A 1 53  ? 43.94800 23.72700 1.66700   0.670 40.67000  ?  53  VAL A O   1 
ATOM   662  O  O   B VAL A 1 53  ? 43.76900 24.45700 1.88800   0.330 38.40000  ?  53  VAL A O   1 
ATOM   663  C  CB  A VAL A 1 53  ? 44.23300 26.57400 3.43900   0.670 43.72000  ?  53  VAL A CB  1 
ATOM   664  C  CB  B VAL A 1 53  ? 43.70800 27.51100 3.50200   0.330 41.95000  ?  53  VAL A CB  1 
ATOM   665  C  CG1 A VAL A 1 53  ? 43.90400 25.45900 4.41700   0.670 51.22000  ?  53  VAL A CG1 1 
ATOM   666  C  CG1 B VAL A 1 53  ? 42.90300 26.56800 4.33200   0.330 41.88000  ?  53  VAL A CG1 1 
ATOM   667  C  CG2 A VAL A 1 53  ? 45.33900 27.45900 3.98700   0.670 49.51000  ?  53  VAL A CG2 1 
ATOM   668  C  CG2 B VAL A 1 53  ? 44.76500 28.18400 4.37000   0.330 40.09000  ?  53  VAL A CG2 1 
ATOM   669  N  N   A MET A 1 54  ? 42.49100 25.35500 1.13400   0.670 37.23000  ?  54  MET A N   1 
ATOM   670  N  N   B MET A 1 54  ? 42.23800 26.00600 1.38800   0.330 36.49000  ?  54  MET A N   1 
ATOM   671  C  CA  A MET A 1 54  ? 41.50400 24.40000 0.64700   0.670 44.06000  ?  54  MET A CA  1 
ATOM   672  C  CA  B MET A 1 54  ? 41.34300 24.97300 0.88400   0.330 42.08000  ?  54  MET A CA  1 
ATOM   673  C  C   A MET A 1 54  ? 41.99800 23.70100 -0.61400  0.670 47.42000  ?  54  MET A C   1 
ATOM   674  C  C   B MET A 1 54  ? 41.96200 24.24300 -0.28800  0.330 45.79000  ?  54  MET A C   1 
ATOM   675  O  O   A MET A 1 54  ? 41.81700 22.48700 -0.76500  0.670 42.67000  ?  54  MET A O   1 
ATOM   676  O  O   B MET A 1 54  ? 41.82500 23.01500 -0.41800  0.330 45.46000  ?  54  MET A O   1 
ATOM   677  C  CB  A MET A 1 54  ? 40.17400 25.11300 0.40200   0.670 43.73000  ?  54  MET A CB  1 
ATOM   678  C  CB  B MET A 1 54  ? 40.00200 25.56300 0.44600   0.330 45.92000  ?  54  MET A CB  1 
ATOM   679  C  CG  A MET A 1 54  ? 39.44100 25.45000 1.68700   0.670 55.26000  ?  54  MET A CG  1 
ATOM   680  C  CG  B MET A 1 54  ? 38.97800 25.68400 1.55300   0.330 50.86000  ?  54  MET A CG  1 
ATOM   681  S  SD  A MET A 1 54  ? 37.71600 25.91700 1.45500   0.670 42.67000  ?  54  MET A SD  1 
ATOM   682  S  SD  B MET A 1 54  ? 37.35000 26.31400 1.03700   0.330 39.12000  ?  54  MET A SD  1 
ATOM   683  C  CE  A MET A 1 54  ? 37.88500 27.65600 1.00900   0.670 41.68000  ?  54  MET A CE  1 
ATOM   684  C  CE  B MET A 1 54  ? 37.67300 28.08700 1.16300   0.330 40.73000  ?  54  MET A CE  1 
ATOM   685  N  N   A ALA A 1 55  ? 42.63900 24.44300 -1.52000  0.670 40.82000  ?  55  ALA A N   1 
ATOM   686  N  N   B ALA A 1 55  ? 42.61400 25.00700 -1.16500  0.330 39.83000  ?  55  ALA A N   1 
ATOM   687  C  CA  A ALA A 1 55  ? 43.18200 23.82400 -2.72500  0.670 44.01000  ?  55  ALA A CA  1 
ATOM   688  C  CA  B ALA A 1 55  ? 43.14200 24.45100 -2.39800  0.330 44.13000  ?  55  ALA A CA  1 
ATOM   689  C  C   A ALA A 1 55  ? 44.16800 22.71800 -2.37600  0.670 48.42000  ?  55  ALA A C   1 
ATOM   690  C  C   B ALA A 1 55  ? 44.04900 23.29000 -2.09000  0.330 47.62000  ?  55  ALA A C   1 
ATOM   691  O  O   A ALA A 1 55  ? 44.23200 21.69100 -3.06200  0.670 53.36000  ?  55  ALA A O   1 
ATOM   692  O  O   B ALA A 1 55  ? 43.79800 22.16300 -2.53900  0.330 47.19000  ?  55  ALA A O   1 
ATOM   693  C  CB  A ALA A 1 55  ? 43.85600 24.88000 -3.60100  0.670 39.97000  ?  55  ALA A CB  1 
ATOM   694  C  CB  B ALA A 1 55  ? 43.89500 25.50800 -3.21600  0.330 41.42000  ?  55  ALA A CB  1 
ATOM   695  N  N   A LEU A 1 56  ? 44.94300 22.90500 -1.31100  0.670 49.65000  ?  56  LEU A N   1 
ATOM   696  N  N   B LEU A 1 56  ? 45.03600 23.52200 -1.22800  0.330 46.88000  ?  56  LEU A N   1 
ATOM   697  C  CA  A LEU A 1 56  ? 45.90000 21.89700 -0.87800  0.670 48.93000  ?  56  LEU A CA  1 
ATOM   698  C  CA  B LEU A 1 56  ? 45.83500 22.43000 -0.69300  0.330 50.18000  ?  56  LEU A CA  1 
ATOM   699  C  C   A LEU A 1 56  ? 45.24600 20.73700 -0.13900  0.670 47.96000  ?  56  LEU A C   1 
ATOM   700  C  C   B LEU A 1 56  ? 45.05800 21.52200 0.22200   0.330 45.54000  ?  56  LEU A C   1 
ATOM   701  O  O   A LEU A 1 56  ? 45.95600 19.82400 0.29500   0.670 57.21000  ?  56  LEU A O   1 
ATOM   702  O  O   B LEU A 1 56  ? 45.59300 21.11900 1.23600   0.330 50.47000  ?  56  LEU A O   1 
ATOM   703  C  CB  A LEU A 1 56  ? 46.96600 22.53800 0.01400   0.670 51.35000  ?  56  LEU A CB  1 
ATOM   704  C  CB  B LEU A 1 56  ? 47.04500 23.00200 0.04000   0.330 51.12000  ?  56  LEU A CB  1 
ATOM   705  C  CG  A LEU A 1 56  ? 47.90400 23.51500 -0.69600  0.670 43.93000  ?  56  LEU A CG  1 
ATOM   706  C  CG  B LEU A 1 56  ? 47.92100 23.68200 -1.00000  0.330 44.34000  ?  56  LEU A CG  1 
ATOM   707  C  CD1 A LEU A 1 56  ? 48.75800 24.28500 0.29800   0.670 42.94000  ?  56  LEU A CD1 1 
ATOM   708  C  CD1 B LEU A 1 56  ? 49.04500 24.49400 -0.40100  0.330 42.36000  ?  56  LEU A CD1 1 
ATOM   709  C  CD2 A LEU A 1 56  ? 48.78300 22.77400 -1.70000  0.670 58.17000  ?  56  LEU A CD2 1 
ATOM   710  C  CD2 B LEU A 1 56  ? 48.41900 22.49000 -1.78600  0.330 55.06000  ?  56  LEU A CD2 1 
ATOM   711  N  N   A GLY A 1 57  ? 43.92500 20.74400 0.01500   0.670 44.69000  ?  57  GLY A N   1 
ATOM   712  N  N   B GLY A 1 57  ? 43.81600 21.19300 -0.07200  0.330 44.88000  ?  57  GLY A N   1 
ATOM   713  C  CA  A GLY A 1 57  ? 43.24200 19.67500 0.70900   0.670 50.91000  ?  57  GLY A CA  1 
ATOM   714  C  CA  B GLY A 1 57  ? 43.07900 20.23000 0.71800   0.330 50.51000  ?  57  GLY A CA  1 
ATOM   715  C  C   A GLY A 1 57  ? 43.20600 19.80700 2.21100   0.670 61.57000  ?  57  GLY A C   1 
ATOM   716  C  C   B GLY A 1 57  ? 43.11100 20.41100 2.23800   0.330 56.27000  ?  57  GLY A C   1 
ATOM   717  O  O   A GLY A 1 57  ? 42.89900 18.82400 2.89600   0.670 57.41000  ?  57  GLY A O   1 
ATOM   718  O  O   B GLY A 1 57  ? 42.47800 19.64900 2.99200   0.330 53.64000  ?  57  GLY A O   1 
ATOM   719  N  N   A VAL A 1 58  ? 43.50100 20.97300 2.74500   0.670 51.74000  ?  58  VAL A N   1 
ATOM   720  N  N   B VAL A 1 58  ? 43.88000 21.38500 2.72600   0.330 49.72000  ?  58  VAL A N   1 
ATOM   721  C  CA  A VAL A 1 58  ? 43.53100 21.18000 4.18600   0.670 56.04000  ?  58  VAL A CA  1 
ATOM   722  C  CA  B VAL A 1 58  ? 43.90600 21.62000 4.16300   0.330 55.64000  ?  58  VAL A CA  1 
ATOM   723  C  C   A VAL A 1 58  ? 42.18600 21.73200 4.63400   0.670 60.46000  ?  58  VAL A C   1 
ATOM   724  C  C   B VAL A 1 58  ? 42.51300 22.08600 4.57900   0.330 58.55000  ?  58  VAL A C   1 
ATOM   725  O  O   A VAL A 1 58  ? 41.59600 22.59400 3.97200   0.670 53.24000  ?  58  VAL A O   1 
ATOM   726  O  O   B VAL A 1 58  ? 41.98600 23.07500 4.04700   0.330 50.19000  ?  58  VAL A O   1 
ATOM   727  C  CB  A VAL A 1 58  ? 44.68400 22.12200 4.57900   0.670 54.28000  ?  58  VAL A CB  1 
ATOM   728  C  CB  B VAL A 1 58  ? 44.97800 22.66400 4.53500   0.330 52.22000  ?  58  VAL A CB  1 
ATOM   729  C  CG1 A VAL A 1 58  ? 44.53400 22.55700 6.02800   0.670 52.03000  ?  58  VAL A CG1 1 
ATOM   730  C  CG1 B VAL A 1 58  ? 44.94000 22.95000 6.03700   0.330 52.72000  ?  58  VAL A CG1 1 
ATOM   731  C  CG2 A VAL A 1 58  ? 46.02600 21.43700 4.35100   0.670 55.96000  ?  58  VAL A CG2 1 
ATOM   732  C  CG2 B VAL A 1 58  ? 46.37500 22.22600 4.11300   0.330 53.71000  ?  58  VAL A CG2 1 
ATOM   733  N  N   A GLY A 1 59  ? 41.69300 21.22000 5.75700   0.670 56.23000  ?  59  GLY A N   1 
ATOM   734  N  N   B GLY A 1 59  ? 41.87600 21.35100 5.48400   0.330 56.64000  ?  59  GLY A N   1 
ATOM   735  C  CA  A GLY A 1 59  ? 40.46900 21.73200 6.33600   0.670 49.14000  ?  59  GLY A CA  1 
ATOM   736  C  CA  B GLY A 1 59  ? 40.67400 21.85700 6.11800   0.330 49.49000  ?  59  GLY A CA  1 
ATOM   737  C  C   A GLY A 1 59  ? 39.19300 21.15700 5.77300   0.670 56.81000  ?  59  GLY A C   1 
ATOM   738  C  C   B GLY A 1 59  ? 39.33800 21.24500 5.72900   0.330 56.14000  ?  59  GLY A C   1 
ATOM   739  O  O   A GLY A 1 59  ? 38.13100 21.76500 5.93700   0.670 58.56000  ?  59  GLY A O   1 
ATOM   740  O  O   B GLY A 1 59  ? 38.30400 21.75400 6.18300   0.330 58.07000  ?  59  GLY A O   1 
ATOM   741  N  N   A TRP A 1 60  ? 39.25800 20.00700 5.11100   0.670 50.06000  ?  60  TRP A N   1 
ATOM   742  N  N   B TRP A 1 60  ? 39.29300 20.19100 4.91800   0.330 50.11000  ?  60  TRP A N   1 
ATOM   743  C  CA  A TRP A 1 60  ? 38.06200 19.33400 4.61000   0.670 52.09000  ?  60  TRP A CA  1 
ATOM   744  C  CA  B TRP A 1 60  ? 37.99800 19.66600 4.48600   0.330 51.08000  ?  60  TRP A CA  1 
ATOM   745  C  C   A TRP A 1 60  ? 37.57000 18.42800 5.73200   0.670 55.53000  ?  60  TRP A C   1 
ATOM   746  C  C   B TRP A 1 60  ? 37.42000 18.73800 5.55800   0.330 54.47000  ?  60  TRP A C   1 
ATOM   747  O  O   A TRP A 1 60  ? 38.13100 17.35700 5.96100   0.670 51.48000  ?  60  TRP A O   1 
ATOM   748  O  O   B TRP A 1 60  ? 37.98000 17.66600 5.82200   0.330 53.65000  ?  60  TRP A O   1 
ATOM   749  C  CB  A TRP A 1 60  ? 38.36500 18.52700 3.35500   0.670 52.87000  ?  60  TRP A CB  1 
ATOM   750  C  CB  B TRP A 1 60  ? 38.15100 18.92300 3.16700   0.330 52.60000  ?  60  TRP A CB  1 
ATOM   751  C  CG  A TRP A 1 60  ? 38.89200 19.30600 2.18700   0.670 57.67000  ?  60  TRP A CG  1 
ATOM   752  C  CG  B TRP A 1 60  ? 38.81600 19.71100 2.03100   0.330 55.09000  ?  60  TRP A CG  1 
ATOM   753  C  CD1 A TRP A 1 60  ? 39.54100 20.50600 2.21400   0.670 55.96000  ?  60  TRP A CD1 1 
ATOM   754  C  CD1 B TRP A 1 60  ? 39.69400 20.79900 2.12500   0.330 54.24000  ?  60  TRP A CD1 1 
ATOM   755  C  CD2 A TRP A 1 60  ? 38.81700 18.92200 0.80900   0.670 47.37000  ?  60  TRP A CD2 1 
ATOM   756  C  CD2 B TRP A 1 60  ? 38.74400 19.38600 0.65700   0.330 47.44000  ?  60  TRP A CD2 1 
ATOM   757  N  NE1 A TRP A 1 60  ? 39.87500 20.89300 0.93800   0.670 50.77000  ?  60  TRP A NE1 1 
ATOM   758  N  NE1 B TRP A 1 60  ? 40.11100 21.18700 0.86700   0.330 49.65000  ?  60  TRP A NE1 1 
ATOM   759  C  CE2 A TRP A 1 60  ? 39.44100 19.93700 0.05700   0.670 47.37000  ?  60  TRP A CE2 1 
ATOM   760  C  CE2 B TRP A 1 60  ? 39.56100 20.33000 -0.05200  0.330 46.33000  ?  60  TRP A CE2 1 
ATOM   761  C  CE3 A TRP A 1 60  ? 38.28200 17.81800 0.13900   0.670 38.16000  ?  60  TRP A CE3 1 
ATOM   762  C  CE3 B TRP A 1 60  ? 38.08300 18.38300 -0.05700  0.330 44.31000  ?  60  TRP A CE3 1 
ATOM   763  C  CZ2 A TRP A 1 60  ? 39.54400 19.88100 -1.33100  0.670 40.91000  ?  60  TRP A CZ2 1 
ATOM   764  C  CZ2 B TRP A 1 60  ? 39.69500 20.30700 -1.43500  0.330 41.30000  ?  60  TRP A CZ2 1 
ATOM   765  C  CZ3 A TRP A 1 60  ? 38.38300 17.76300 -1.23700  0.670 48.20000  ?  60  TRP A CZ3 1 
ATOM   766  C  CZ3 B TRP A 1 60  ? 38.22500 18.35700 -1.43900  0.330 48.14000  ?  60  TRP A CZ3 1 
ATOM   767  C  CH2 A TRP A 1 60  ? 39.01000 18.78800 -1.95900  0.670 50.23000  ?  60  TRP A CH2 1 
ATOM   768  C  CH2 B TRP A 1 60  ? 39.02700 19.31400 -2.11500  0.330 49.94000  ?  60  TRP A CH2 1 
ATOM   769  N  N   A VAL A 1 61  ? 36.53200 18.84600 6.45000   0.670 51.50000  ?  61  VAL A N   1 
ATOM   770  N  N   B VAL A 1 61  ? 36.26500 19.10000 6.11400   0.330 50.80000  ?  61  VAL A N   1 
ATOM   771  C  CA  A VAL A 1 61  ? 36.08300 18.15200 7.65500   0.670 55.79000  ?  61  VAL A CA  1 
ATOM   772  C  CA  B VAL A 1 61  ? 35.67200 18.44300 7.29700   0.330 51.30000  ?  61  VAL A CA  1 
ATOM   773  C  C   A VAL A 1 61  ? 34.86300 17.29400 7.31000   0.670 48.51000  ?  61  VAL A C   1 
ATOM   774  C  C   B VAL A 1 61  ? 34.49300 17.58300 6.90100   0.330 52.00000  ?  61  VAL A C   1 
ATOM   775  O  O   A VAL A 1 61  ? 33.83700 17.84700 6.89300   0.670 54.36000  ?  61  VAL A O   1 
ATOM   776  O  O   B VAL A 1 61  ? 33.49400 18.10900 6.36700   0.330 55.36000  ?  61  VAL A O   1 
ATOM   777  C  CB  A VAL A 1 61  ? 35.76000 19.12200 8.80300   0.670 43.97000  ?  61  VAL A CB  1 
ATOM   778  C  CB  B VAL A 1 61  ? 35.23000 19.48800 8.34000   0.330 46.94000  ?  61  VAL A CB  1 
ATOM   779  C  CG1 A VAL A 1 61  ? 35.42700 18.30300 10.05200  0.670 61.96000  ?  61  VAL A CG1 1 
ATOM   780  C  CG1 B VAL A 1 61  ? 34.65500 18.83000 9.57800   0.330 57.68000  ?  61  VAL A CG1 1 
ATOM   781  C  CG2 A VAL A 1 61  ? 36.92700 20.04400 9.05000   0.670 41.01000  ?  61  VAL A CG2 1 
ATOM   782  C  CG2 B VAL A 1 61  ? 36.36000 20.40600 8.72400   0.330 41.29000  ?  61  VAL A CG2 1 
ATOM   783  N  N   A PRO A 1 62  ? 34.92500 15.97700 7.46700   0.670 56.26000  ?  62  PRO A N   1 
ATOM   784  N  N   B PRO A 1 62  ? 34.47500 16.26500 7.20200   0.330 55.01000  ?  62  PRO A N   1 
ATOM   785  C  CA  A PRO A 1 62  ? 33.73200 15.14800 7.25400   0.670 56.94000  ?  62  PRO A CA  1 
ATOM   786  C  CA  B PRO A 1 62  ? 33.26400 15.47600 6.97500   0.330 57.13000  ?  62  PRO A CA  1 
ATOM   787  C  C   A PRO A 1 62  ? 32.75800 15.30200 8.41100   0.670 54.30000  ?  62  PRO A C   1 
ATOM   788  C  C   B PRO A 1 62  ? 32.32100 15.67700 8.13200   0.330 56.06000  ?  62  PRO A C   1 
ATOM   789  O  O   A PRO A 1 62  ? 33.14700 15.30500 9.58200   0.670 53.51000  ?  62  PRO A O   1 
ATOM   790  O  O   B PRO A 1 62  ? 32.73800 15.79900 9.28000   0.330 53.74000  ?  62  PRO A O   1 
ATOM   791  C  CB  A PRO A 1 62  ? 34.30400 13.72900 7.18900   0.670 48.44000  ?  62  PRO A CB  1 
ATOM   792  C  CB  B PRO A 1 62  ? 33.76700 14.02600 6.90300   0.330 52.97000  ?  62  PRO A CB  1 
ATOM   793  C  CG  A PRO A 1 62  ? 35.48700 13.78700 8.12800   0.670 66.50000  ?  62  PRO A CG  1 
ATOM   794  C  CG  B PRO A 1 62  ? 34.85900 14.02100 7.83700   0.330 58.66000  ?  62  PRO A CG  1 
ATOM   795  C  CD  A PRO A 1 62  ? 36.03800 15.20200 8.03900   0.670 67.38000  ?  62  PRO A CD  1 
ATOM   796  C  CD  B PRO A 1 62  ? 35.50800 15.43100 7.84600   0.330 61.97000  ?  62  PRO A CD  1 
ATOM   797  N  N   A VAL A 1 63  ? 31.48100 15.44000 8.07000   0.670 54.72000  ?  63  VAL A N   1 
ATOM   798  N  N   B VAL A 1 63  ? 31.05100 15.75700 7.80600   0.330 57.07000  ?  63  VAL A N   1 
ATOM   799  C  CA  A VAL A 1 63  ? 30.42500 15.63300 9.05500   0.670 57.69000  ?  63  VAL A CA  1 
ATOM   800  C  CA  B VAL A 1 63  ? 30.02700 16.07500 8.77400   0.330 58.75000  ?  63  VAL A CA  1 
ATOM   801  C  C   A VAL A 1 63  ? 29.23000 14.80100 8.60900   0.670 60.17000  ?  63  VAL A C   1 
ATOM   802  C  C   B VAL A 1 63  ? 28.86300 15.16900 8.44500   0.330 60.91000  ?  63  VAL A C   1 
ATOM   803  O  O   A VAL A 1 63  ? 28.60200 15.11200 7.58900   0.670 55.51000  ?  63  VAL A O   1 
ATOM   804  O  O   B VAL A 1 63  ? 28.07100 15.42800 7.53700   0.330 61.78000  ?  63  VAL A O   1 
ATOM   805  C  CB  A VAL A 1 63  ? 30.03500 17.10900 9.21000   0.670 54.23000  ?  63  VAL A CB  1 
ATOM   806  C  CB  B VAL A 1 63  ? 29.64900 17.56200 8.74500   0.330 53.86000  ?  63  VAL A CB  1 
ATOM   807  C  CG1 A VAL A 1 63  ? 28.88200 17.25000 10.18600  0.670 57.64000  ?  63  VAL A CG1 1 
ATOM   808  C  CG1 B VAL A 1 63  ? 28.31800 17.77500 9.39900   0.330 58.37000  ?  63  VAL A CG1 1 
ATOM   809  C  CG2 A VAL A 1 63  ? 31.23700 17.92700 9.67000   0.670 46.38000  ?  63  VAL A CG2 1 
ATOM   810  C  CG2 B VAL A 1 63  ? 30.64400 18.36000 9.54300   0.330 47.26000  ?  63  VAL A CG2 1 
ATOM   811  N  N   A ALA A 1 64  ? 28.91300 13.75000 9.37200   0.670 76.08000  ?  64  ALA A N   1 
ATOM   812  N  N   B ALA A 1 64  ? 28.76500 14.09400 9.19800   0.330 72.25000  ?  64  ALA A N   1 
ATOM   813  C  CA  A ALA A 1 64  ? 27.87000 12.80600 8.99000   0.670 74.38000  ?  64  ALA A CA  1 
ATOM   814  C  CA  B ALA A 1 64  ? 27.90400 13.01400 8.79400   0.330 73.67000  ?  64  ALA A CA  1 
ATOM   815  C  C   A ALA A 1 64  ? 28.18200 12.25500 7.60400   0.670 76.70000  ?  64  ALA A C   1 
ATOM   816  C  C   B ALA A 1 64  ? 28.44400 12.55800 7.47300   0.330 75.71000  ?  64  ALA A C   1 
ATOM   817  O  O   A ALA A 1 64  ? 29.10700 11.45100 7.44700   0.670 86.68000  ?  64  ALA A O   1 
ATOM   818  O  O   B ALA A 1 64  ? 29.61200 12.16700 7.33100   0.330 75.00000  ?  64  ALA A O   1 
ATOM   819  C  CB  A ALA A 1 64  ? 26.49800 13.47500 9.03200   0.670 75.18000  ?  64  ALA A CB  1 
ATOM   820  C  CB  B ALA A 1 64  ? 26.45800 13.47300 8.62800   0.330 72.54000  ?  64  ALA A CB  1 
ATOM   821  N  N   A GLU A 1 65  ? 27.42800 12.68500 6.59000   0.670 75.12000  ?  65  GLU A N   1 
ATOM   822  N  N   B GLU A 1 65  ? 27.59000 12.72300 6.49500   0.330 75.29000  ?  65  GLU A N   1 
ATOM   823  C  CA  A GLU A 1 65  ? 27.61500 12.19600 5.22800   0.670 79.49000  ?  65  GLU A CA  1 
ATOM   824  C  CA  B GLU A 1 65  ? 27.81800 12.21000 5.17500   0.330 79.25000  ?  65  GLU A CA  1 
ATOM   825  C  C   A GLU A 1 65  ? 28.06000 13.29100 4.26300   0.670 79.42000  ?  65  GLU A C   1 
ATOM   826  C  C   B GLU A 1 65  ? 28.40400 13.25900 4.24500   0.330 79.21000  ?  65  GLU A C   1 
ATOM   827  O  O   A GLU A 1 65  ? 28.14600 13.04200 3.05300   0.670 83.63000  ?  65  GLU A O   1 
ATOM   828  O  O   B GLU A 1 65  ? 28.78500 12.92100 3.12100   0.330 82.23000  ?  65  GLU A O   1 
ATOM   829  C  CB  A GLU A 1 65  ? 26.32300 11.55300 4.71600   0.670 89.03000  ?  65  GLU A CB  1 
ATOM   830  C  CB  B GLU A 1 65  ? 26.48900 11.67800 4.63500   0.330 88.46000  ?  65  GLU A CB  1 
ATOM   831  C  CG  A GLU A 1 65  ? 26.03500 10.18500 5.29600   0.670 94.11000  ?  65  GLU A CG  1 
ATOM   832  C  CG  B GLU A 1 65  ? 25.88900 10.64400 5.56900   0.330 93.33000  ?  65  GLU A CG  1 
ATOM   833  C  CD  A GLU A 1 65  ? 26.59600 9.05900  4.44200   0.670 115.63000 ?  65  GLU A CD  1 
ATOM   834  C  CD  B GLU A 1 65  ? 26.52700 9.27900  5.43000   0.330 104.30000 ?  65  GLU A CD  1 
ATOM   835  O  OE1 A GLU A 1 65  ? 27.34500 9.34200  3.48300   0.670 123.57000 ?  65  GLU A OE1 1 
ATOM   836  O  OE1 B GLU A 1 65  ? 27.64400 9.18700  4.88200   0.330 111.10000 ?  65  GLU A OE1 1 
ATOM   837  O  OE2 A GLU A 1 65  ? 26.28500 7.88400  4.73200   0.670 121.38000 -1 65  GLU A OE2 1 
ATOM   838  O  OE2 B GLU A 1 65  ? 25.89900 8.29700  5.85600   0.330 110.67000 -1 65  GLU A OE2 1 
ATOM   839  N  N   A ARG A 1 66  ? 28.35300 14.48500 4.76200   0.670 75.23000  ?  66  ARG A N   1 
ATOM   840  N  N   B ARG A 1 66  ? 28.53300 14.50300 4.71300   0.330 74.08000  ?  66  ARG A N   1 
ATOM   841  C  CA  A ARG A 1 66  ? 28.75700 15.61600 3.94100   0.670 64.09000  ?  66  ARG A CA  1 
ATOM   842  C  CA  B ARG A 1 66  ? 28.88600 15.66400 3.91400   0.330 64.28000  ?  66  ARG A CA  1 
ATOM   843  C  C   A ARG A 1 66  ? 30.21800 15.95500 4.20600   0.670 62.75000  ?  66  ARG A C   1 
ATOM   844  C  C   B ARG A 1 66  ? 30.32800 16.06300 4.13600   0.330 62.81000  ?  66  ARG A C   1 
ATOM   845  O  O   A ARG A 1 66  ? 30.83500 15.47300 5.15800   0.670 58.21000  ?  66  ARG A O   1 
ATOM   846  O  O   B ARG A 1 66  ? 31.01200 15.58100 5.04100   0.330 58.61000  ?  66  ARG A O   1 
ATOM   847  C  CB  A ARG A 1 66  ? 27.87200 16.83600 4.22800   0.670 64.92000  ?  66  ARG A CB  1 
ATOM   848  C  CB  B ARG A 1 66  ? 28.07000 16.90400 4.26700   0.330 64.55000  ?  66  ARG A CB  1 
ATOM   849  C  CG  A ARG A 1 66  ? 26.38800 16.59700 4.05100   0.670 76.07000  ?  66  ARG A CG  1 
ATOM   850  C  CG  B ARG A 1 66  ? 26.58800 16.80800 4.16800   0.330 74.79000  ?  66  ARG A CG  1 
ATOM   851  C  CD  A ARG A 1 66  ? 25.61000 16.80000 5.34900   0.670 81.60000  ?  66  ARG A CD  1 
ATOM   852  C  CD  B ARG A 1 66  ? 25.97200 17.43000 5.43300   0.330 70.54000  ?  66  ARG A CD  1 
ATOM   853  N  NE  A ARG A 1 66  ? 26.06300 17.95900 6.11500   0.670 61.41000  ?  66  ARG A NE  1 
ATOM   854  N  NE  B ARG A 1 66  ? 26.75900 18.58200 5.86100   0.330 59.44000  ?  66  ARG A NE  1 
ATOM   855  C  CZ  A ARG A 1 66  ? 25.70200 18.22000 7.36700   0.670 75.35000  ?  66  ARG A CZ  1 
ATOM   856  C  CZ  B ARG A 1 66  ? 26.53300 19.30200 6.95100   0.330 61.76000  ?  66  ARG A CZ  1 
ATOM   857  N  NH1 A ARG A 1 66  ? 24.86900 17.40800 8.00100   0.670 76.61000  ?  66  ARG A NH1 1 
ATOM   858  N  NH1 B ARG A 1 66  ? 25.45100 19.12700 7.69400   0.330 70.70000  ?  66  ARG A NH1 1 
ATOM   859  N  NH2 A ARG A 1 66  ? 26.16900 19.29600 7.98500   0.670 66.55000  ?  66  ARG A NH2 1 
ATOM   860  N  NH2 B ARG A 1 66  ? 27.37500 20.27100 7.27100   0.330 61.18000  ?  66  ARG A NH2 1 
ATOM   861  N  N   A THR A 1 67  ? 30.77200 16.79800 3.34200   0.670 62.78000  ?  67  THR A N   1 
ATOM   862  N  N   B THR A 1 67  ? 30.75700 17.03000 3.32800   0.330 61.80000  ?  67  THR A N   1 
ATOM   863  C  CA  A THR A 1 67  ? 32.09800 17.36700 3.54100   0.670 57.36000  ?  67  THR A CA  1 
ATOM   864  C  CA  B THR A 1 67  ? 31.98000 17.79200 3.53200   0.330 56.25000  ?  67  THR A CA  1 
ATOM   865  C  C   A THR A 1 67  ? 31.95000 18.86800 3.74700   0.670 51.28000  ?  67  THR A C   1 
ATOM   866  C  C   B THR A 1 67  ? 31.58400 19.24300 3.84600   0.330 50.00000  ?  67  THR A C   1 
ATOM   867  O  O   A THR A 1 67  ? 31.31300 19.54800 2.93700   0.670 49.21000  ?  67  THR A O   1 
ATOM   868  O  O   B THR A 1 67  ? 30.56400 19.73700 3.36000   0.330 48.20000  ?  67  THR A O   1 
ATOM   869  C  CB  A THR A 1 67  ? 33.02000 17.07800 2.35700   0.670 55.34000  ?  67  THR A CB  1 
ATOM   870  C  CB  B THR A 1 67  ? 32.90000 17.67900 2.28700   0.330 54.24000  ?  67  THR A CB  1 
ATOM   871  O  OG1 A THR A 1 67  ? 33.08500 15.66400 2.14000   0.670 63.53000  ?  67  THR A OG1 1 
ATOM   872  O  OG1 B THR A 1 67  ? 32.98400 16.31000 1.84600   0.330 61.84000  ?  67  THR A OG1 1 
ATOM   873  C  CG2 A THR A 1 67  ? 34.42000 17.60700 2.64000   0.670 46.93000  ?  67  THR A CG2 1 
ATOM   874  C  CG2 B THR A 1 67  ? 34.29300 18.13500 2.57000   0.330 48.16000  ?  67  THR A CG2 1 
ATOM   875  N  N   A VAL A 1 68  ? 32.52700 19.37500 4.83300   0.670 49.40000  ?  68  VAL A N   1 
ATOM   876  N  N   B VAL A 1 68  ? 32.34400 19.89500 4.72400   0.330 46.38000  ?  68  VAL A N   1 
ATOM   877  C  CA  A VAL A 1 68  ? 32.45000 20.78700 5.19600   0.670 42.67000  ?  68  VAL A CA  1 
ATOM   878  C  CA  B VAL A 1 68  ? 32.13000 21.28200 5.12800   0.330 44.19000  ?  68  VAL A CA  1 
ATOM   879  C  C   A VAL A 1 68  ? 33.83800 21.40200 5.06000   0.670 47.42000  ?  68  VAL A C   1 
ATOM   880  C  C   B VAL A 1 68  ? 33.45300 21.99800 4.96700   0.330 46.31000  ?  68  VAL A C   1 
ATOM   881  O  O   A VAL A 1 68  ? 34.83700 20.80600 5.47500   0.670 53.29000  ?  68  VAL A O   1 
ATOM   882  O  O   B VAL A 1 68  ? 34.49500 21.47800 5.37800   0.330 49.73000  ?  68  VAL A O   1 
ATOM   883  C  CB  A VAL A 1 68  ? 31.90900 20.98500 6.62500   0.670 48.63000  ?  68  VAL A CB  1 
ATOM   884  C  CB  B VAL A 1 68  ? 31.65100 21.42700 6.58600   0.330 45.63000  ?  68  VAL A CB  1 
ATOM   885  C  CG1 A VAL A 1 68  ? 32.42200 22.29900 7.20300   0.670 43.97000  ?  68  VAL A CG1 1 
ATOM   886  C  CG1 B VAL A 1 68  ? 31.92700 22.83600 7.09000   0.330 43.97000  ?  68  VAL A CG1 1 
ATOM   887  C  CG2 A VAL A 1 68  ? 30.39200 20.95800 6.61600   0.670 51.87000  ?  68  VAL A CG2 1 
ATOM   888  C  CG2 B VAL A 1 68  ? 30.19100 21.07400 6.70000   0.330 51.96000  ?  68  VAL A CG2 1 
ATOM   889  N  N   A PHE A 1 69  ? 33.89400 22.60000 4.48600   0.670 43.93000  ?  69  PHE A N   1 
ATOM   890  N  N   B PHE A 1 69  ? 33.42100 23.19700 4.40500   0.330 41.77000  ?  69  PHE A N   1 
ATOM   891  C  CA  A PHE A 1 69  ? 35.14800 23.29300 4.19100   0.670 43.28000  ?  69  PHE A CA  1 
ATOM   892  C  CA  B PHE A 1 69  ? 34.67700 23.86700 4.11500   0.330 42.27000  ?  69  PHE A CA  1 
ATOM   893  C  C   A PHE A 1 69  ? 35.34800 24.37500 5.24300   0.670 42.03000  ?  69  PHE A C   1 
ATOM   894  C  C   B PHE A 1 69  ? 34.89600 24.93100 5.15900   0.330 45.62000  ?  69  PHE A C   1 
ATOM   895  O  O   A PHE A 1 69  ? 34.79500 25.47300 5.14000   0.670 50.85000  ?  69  PHE A O   1 
ATOM   896  O  O   B PHE A 1 69  ? 34.55100 26.10400 4.97400   0.330 45.07000  ?  69  PHE A O   1 
ATOM   897  C  CB  A PHE A 1 69  ? 35.10100 23.86200 2.78000   0.670 46.16000  ?  69  PHE A CB  1 
ATOM   898  C  CB  B PHE A 1 69  ? 34.69100 24.38400 2.68400   0.330 43.98000  ?  69  PHE A CB  1 
ATOM   899  C  CG  A PHE A 1 69  ? 34.87600 22.81700 1.72800   0.670 35.29000  ?  69  PHE A CG  1 
ATOM   900  C  CG  B PHE A 1 69  ? 34.70500 23.28300 1.70000   0.330 37.65000  ?  69  PHE A CG  1 
ATOM   901  C  CD1 A PHE A 1 69  ? 35.90300 21.96900 1.35500   0.670 40.83000  ?  69  PHE A CD1 1 
ATOM   902  C  CD1 B PHE A 1 69  ? 35.89900 22.64700 1.41200   0.330 40.85000  ?  69  PHE A CD1 1 
ATOM   903  C  CD2 A PHE A 1 69  ? 33.63900 22.67100 1.12500   0.670 32.92000  ?  69  PHE A CD2 1 
ATOM   904  C  CD2 B PHE A 1 69  ? 33.56200 22.85200 1.12000   0.330 34.27000  ?  69  PHE A CD2 1 
ATOM   905  C  CE1 A PHE A 1 69  ? 35.70300 20.99700 0.39200   0.670 31.55000  ?  69  PHE A CE1 1 
ATOM   906  C  CE1 B PHE A 1 69  ? 35.95100 21.61800 0.55300   0.330 34.98000  ?  69  PHE A CE1 1 
ATOM   907  C  CE2 A PHE A 1 69  ? 33.43200 21.70400 0.16300   0.670 36.66000  ?  69  PHE A CE2 1 
ATOM   908  C  CE2 B PHE A 1 69  ? 33.61600 21.81700 0.24100   0.330 36.82000  ?  69  PHE A CE2 1 
ATOM   909  C  CZ  A PHE A 1 69  ? 34.46600 20.86400 -0.20400  0.670 40.11000  ?  69  PHE A CZ  1 
ATOM   910  C  CZ  B PHE A 1 69  ? 34.80600 21.19300 -0.00800  0.330 36.74000  ?  69  PHE A CZ  1 
ATOM   911  N  N   A ALA A 1 70  ? 36.15100 24.05900 6.25100   0.670 40.26000  ?  70  ALA A N   1 
ATOM   912  N  N   B ALA A 1 70  ? 35.46600 24.48200 6.28200   0.330 44.10000  ?  70  ALA A N   1 
ATOM   913  C  CA  A ALA A 1 70  ? 36.29500 24.92500 7.40900   0.670 37.71000  ?  70  ALA A CA  1 
ATOM   914  C  CA  B ALA A 1 70  ? 35.81300 25.39300 7.36000   0.330 34.03000  ?  70  ALA A CA  1 
ATOM   915  C  C   A ALA A 1 70  ? 36.98400 26.23800 7.06100   0.670 30.96000  ?  70  ALA A C   1 
ATOM   916  C  C   B ALA A 1 70  ? 36.38100 26.66900 6.80800   0.330 34.71000  ?  70  ALA A C   1 
ATOM   917  O  O   A ALA A 1 70  ? 36.59600 27.28500 7.59300   0.670 39.93000  ?  70  ALA A O   1 
ATOM   918  O  O   B ALA A 1 70  ? 35.76700 27.71600 7.03600   0.330 41.79000  ?  70  ALA A O   1 
ATOM   919  C  CB  A ALA A 1 70  ? 37.06800 24.20400 8.51400   0.670 43.97000  ?  70  ALA A CB  1 
ATOM   920  C  CB  B ALA A 1 70  ? 36.77800 24.71200 8.33400   0.330 43.80000  ?  70  ALA A CB  1 
ATOM   921  N  N   A PRO A 1 71  ? 38.00700 26.24300 6.20100   0.670 31.59000  ?  71  PRO A N   1 
ATOM   922  N  N   B PRO A 1 71  ? 37.46200 26.66500 5.99200   0.330 39.84000  ?  71  PRO A N   1 
ATOM   923  C  CA  A PRO A 1 71  ? 38.64900 27.52900 5.87300   0.670 40.99000  ?  71  PRO A CA  1 
ATOM   924  C  CA  B PRO A 1 71  ? 38.05700 27.94300 5.49700   0.330 43.01000  ?  71  PRO A CA  1 
ATOM   925  C  C   A PRO A 1 71  ? 37.68300 28.54100 5.28200   0.670 42.55000  ?  71  PRO A C   1 
ATOM   926  C  C   B PRO A 1 71  ? 37.12500 28.92900 4.77600   0.330 35.51000  ?  71  PRO A C   1 
ATOM   927  O  O   A PRO A 1 71  ? 37.85100 29.74900 5.49800   0.670 34.20000  ?  71  PRO A O   1 
ATOM   928  O  O   B PRO A 1 71  ? 37.29500 30.14600 4.86200   0.330 33.04000  ?  71  PRO A O   1 
ATOM   929  C  CB  A PRO A 1 71  ? 39.74900 27.13200 4.87800   0.670 48.45000  ?  71  PRO A CB  1 
ATOM   930  C  CB  B PRO A 1 71  ? 39.12300 27.45000 4.50300   0.330 44.28000  ?  71  PRO A CB  1 
ATOM   931  C  CG  A PRO A 1 71  ? 40.07500 25.71100 5.24300   0.670 46.82000  ?  71  PRO A CG  1 
ATOM   932  C  CG  B PRO A 1 71  ? 39.31300 25.99500 4.84900   0.330 42.39000  ?  71  PRO A CG  1 
ATOM   933  C  CD  A PRO A 1 71  ? 38.74200 25.09900 5.62400   0.670 35.46000  ?  71  PRO A CD  1 
ATOM   934  C  CD  B PRO A 1 71  ? 38.04100 25.50500 5.28300   0.330 37.96000  ?  71  PRO A CD  1 
ATOM   935  N  N   A ARG A 1 72  ? 36.66300 28.07900 4.55600   0.670 34.37000  ?  72  ARG A N   1 
ATOM   936  N  N   B ARG A 1 72  ? 36.18600 28.37800 4.00800   0.330 35.83000  ?  72  ARG A N   1 
ATOM   937  C  CA  A ARG A 1 72  ? 35.67900 28.99800 3.99600   0.670 37.29000  ?  72  ARG A CA  1 
ATOM   938  C  CA  B ARG A 1 72  ? 35.11800 29.14500 3.37100   0.330 38.00000  ?  72  ARG A CA  1 
ATOM   939  C  C   A ARG A 1 72  ? 35.02800 29.84300 5.08400   0.670 38.11000  ?  72  ARG A C   1 
ATOM   940  C  C   B ARG A 1 72  ? 34.21700 29.88100 4.36400   0.330 35.20000  ?  72  ARG A C   1 
ATOM   941  O  O   A ARG A 1 72  ? 34.82100 31.04800 4.90200   0.670 35.95000  ?  72  ARG A O   1 
ATOM   942  O  O   B ARG A 1 72  ? 33.67800 30.92500 4.00600   0.330 36.83000  ?  72  ARG A O   1 
ATOM   943  C  CB  A ARG A 1 72  ? 34.62300 28.21300 3.21500   0.670 38.70000  ?  72  ARG A CB  1 
ATOM   944  C  CB  B ARG A 1 72  ? 34.29300 28.22700 2.47700   0.330 32.82000  ?  72  ARG A CB  1 
ATOM   945  C  CG  A ARG A 1 72  ? 33.29000 28.91800 3.06800   0.670 30.02000  ?  72  ARG A CG  1 
ATOM   946  C  CG  B ARG A 1 72  ? 32.86400 28.46800 2.61900   0.330 35.15000  ?  72  ARG A CG  1 
ATOM   947  C  CD  A ARG A 1 72  ? 32.22300 27.96400 2.53700   0.670 37.58000  ?  72  ARG A CD  1 
ATOM   948  C  CD  B ARG A 1 72  ? 32.01300 27.34900 2.11200   0.330 37.42000  ?  72  ARG A CD  1 
ATOM   949  N  NE  A ARG A 1 72  ? 32.43400 27.64800 1.12300   0.670 31.62000  ?  72  ARG A NE  1 
ATOM   950  N  NE  B ARG A 1 72  ? 32.10600 27.29300 0.65700   0.330 35.68000  ?  72  ARG A NE  1 
ATOM   951  C  CZ  A ARG A 1 72  ? 31.81300 26.67200 0.46700   0.670 40.88000  ?  72  ARG A CZ  1 
ATOM   952  C  CZ  B ARG A 1 72  ? 31.33200 26.50700 -0.08100  0.330 41.02000  ?  72  ARG A CZ  1 
ATOM   953  N  NH1 A ARG A 1 72  ? 30.93500 25.90300 1.09300   0.670 36.95000  ?  72  ARG A NH1 1 
ATOM   954  N  NH1 B ARG A 1 72  ? 30.19500 26.03000 0.37700   0.330 33.10000  ?  72  ARG A NH1 1 
ATOM   955  N  NH2 A ARG A 1 72  ? 32.07500 26.46600 -0.81500  0.670 45.53000  ?  72  ARG A NH2 1 
ATOM   956  N  NH2 B ARG A 1 72  ? 31.68000 26.21700 -1.32600  0.330 40.13000  ?  72  ARG A NH2 1 
ATOM   957  N  N   A TYR A 1 73  ? 34.66900 29.22900 6.21200   0.670 40.58000  ?  73  TYR A N   1 
ATOM   958  N  N   B TYR A 1 73  ? 34.07800 29.41900 5.61500   0.330 36.26000  ?  73  TYR A N   1 
ATOM   959  C  CA  A TYR A 1 73  ? 33.93600 29.97100 7.23200   0.670 31.17000  ?  73  TYR A CA  1 
ATOM   960  C  CA  B TYR A 1 73  ? 33.32000 30.19100 6.60800   0.330 30.16000  ?  73  TYR A CA  1 
ATOM   961  C  C   A TYR A 1 73  ? 34.85100 30.87900 8.04300   0.670 34.45000  ?  73  TYR A C   1 
ATOM   962  C  C   B TYR A 1 73  ? 34.22000 31.13400 7.40800   0.330 31.76000  ?  73  TYR A C   1 
ATOM   963  O  O   A TYR A 1 73  ? 34.44200 31.98000 8.42500   0.670 34.20000  ?  73  TYR A O   1 
ATOM   964  O  O   B TYR A 1 73  ? 33.75800 32.16100 7.89900   0.330 32.62000  ?  73  TYR A O   1 
ATOM   965  C  CB  A TYR A 1 73  ? 33.18000 29.00100 8.13500   0.670 36.69000  ?  73  TYR A CB  1 
ATOM   966  C  CB  B TYR A 1 73  ? 32.54000 29.25800 7.56200   0.330 36.66000  ?  73  TYR A CB  1 
ATOM   967  C  CG  A TYR A 1 73  ? 32.10800 28.25500 7.38000   0.670 34.79000  ?  73  TYR A CG  1 
ATOM   968  C  CG  B TYR A 1 73  ? 31.37700 28.44400 6.92600   0.330 36.50000  ?  73  TYR A CG  1 
ATOM   969  C  CD1 . TYR A 1 73  ? 30.08200 28.96700 6.75800   1.000 39.99000  ?  73  TYR A CD1 1 
ATOM   970  C  CD2 A TYR A 1 73  ? 32.34500 26.98400 6.88100   0.670 36.95000  ?  73  TYR A CD2 1 
ATOM   971  C  CD2 B TYR A 1 73  ? 31.60300 27.19500 6.41200   0.330 36.48000  ?  73  TYR A CD2 1 
ATOM   972  C  CE1 A TYR A 1 73  ? 29.89100 28.15400 6.43700   0.670 36.00000  ?  73  TYR A CE1 1 
ATOM   973  C  CE1 B TYR A 1 73  ? 29.03200 28.21000 6.17100   0.330 33.10000  ?  73  TYR A CE1 1 
ATOM   974  C  CE2 A TYR A 1 73  ? 31.37500 26.30000 6.17700   0.670 39.66000  ?  73  TYR A CE2 1 
ATOM   975  C  CE2 B TYR A 1 73  ? 30.58500 26.46000 5.79700   0.330 35.72000  ?  73  TYR A CE2 1 
ATOM   976  C  CZ  A TYR A 1 73  ? 30.15100 26.89000 5.95900   0.670 34.12000  ?  73  TYR A CZ  1 
ATOM   977  C  CZ  B TYR A 1 73  ? 29.30700 26.98300 5.69000   0.330 39.70000  ?  73  TYR A CZ  1 
ATOM   978  O  OH  A TYR A 1 73  ? 29.18300 26.20900 5.25700   0.670 51.40000  ?  73  TYR A OH  1 
ATOM   979  O  OH  B TYR A 1 73  ? 28.28600 26.25900 5.11900   0.330 45.15000  ?  73  TYR A OH  1 
ATOM   980  N  N   A ILE A 1 74  ? 36.09100 30.46000 8.30100   0.670 30.22000  ?  74  ILE A N   1 
ATOM   981  N  N   B ILE A 1 74  ? 35.49600 30.83200 7.58200   0.330 28.62000  ?  74  ILE A N   1 
ATOM   982  C  CA  A ILE A 1 74  ? 37.04400 31.37400 8.92600   0.670 37.72000  ?  74  ILE A CA  1 
ATOM   983  C  CA  B ILE A 1 74  ? 36.33400 31.74100 8.34900   0.330 31.48000  ?  74  ILE A CA  1 
ATOM   984  C  C   A ILE A 1 74  ? 37.24000 32.60000 8.04000   0.670 35.50000  ?  74  ILE A C   1 
ATOM   985  C  C   B ILE A 1 74  ? 36.28800 33.06100 7.63700   0.330 30.96000  ?  74  ILE A C   1 
ATOM   986  O  O   A ILE A 1 74  ? 37.22300 33.74200 8.51200   0.670 41.36000  ?  74  ILE A O   1 
ATOM   987  O  O   B ILE A 1 74  ? 35.91200 34.10400 8.19500   0.330 28.69000  ?  74  ILE A O   1 
ATOM   988  C  CB  A ILE A 1 74  ? 38.37700 30.66000 9.20500   0.670 42.80000  ?  74  ILE A CB  1 
ATOM   989  C  CB  B ILE A 1 74  ? 37.79600 31.27000 8.45800   0.330 38.02000  ?  74  ILE A CB  1 
ATOM   990  C  CG1 A ILE A 1 74  ? 38.22500 29.67300 10.36500  0.670 44.06000  ?  74  ILE A CG1 1 
ATOM   991  C  CG1 B ILE A 1 74  ? 37.90700 30.12600 9.44100   0.330 44.56000  ?  74  ILE A CG1 1 
ATOM   992  C  CG2 A ILE A 1 74  ? 39.45800 31.67200 9.55200   0.670 31.00000  ?  74  ILE A CG2 1 
ATOM   993  C  CG2 B ILE A 1 74  ? 38.69100 32.37500 9.03200   0.330 38.07000  ?  74  ILE A CG2 1 
ATOM   994  C  CD1 A ILE A 1 74  ? 37.63700 28.34600 9.97000   0.670 39.89000  ?  74  ILE A CD1 1 
ATOM   995  C  CD1 B ILE A 1 74  ? 37.51900 28.81600 8.89000   0.330 39.24000  ?  74  ILE A CD1 1 
ATOM   996  N  N   A ASP A 1 75  ? 37.43000 32.37200 6.73800   0.670 29.32000  ?  75  ASP A N   1 
ATOM   997  N  N   B ASP A 1 75  ? 36.78300 32.99400 6.41800   0.330 33.27000  ?  75  ASP A N   1 
ATOM   998  C  CA  A ASP A 1 75  ? 37.48100 33.45200 5.75600   0.670 33.24000  ?  75  ASP A CA  1 
ATOM   999  C  CA  B ASP A 1 75  ? 36.73600 33.99200 5.37200   0.330 29.53000  ?  75  ASP A CA  1 
ATOM   1000 C  C   A ASP A 1 75  ? 36.29000 34.38800 5.91100   0.670 32.82000  ?  75  ASP A C   1 
ATOM   1001 C  C   B ASP A 1 75  ? 35.59400 34.95000 5.64400   0.330 30.23000  ?  75  ASP A C   1 
ATOM   1002 O  O   A ASP A 1 75  ? 36.45400 35.59400 6.12600   0.670 34.36000  ?  75  ASP A O   1 
ATOM   1003 O  O   B ASP A 1 75  ? 35.78400 36.08700 6.10300   0.330 28.00000  ?  75  ASP A O   1 
ATOM   1004 C  CB  A ASP A 1 75  ? 37.54300 32.82400 4.35500   0.670 34.00000  ?  75  ASP A CB  1 
ATOM   1005 C  CB  B ASP A 1 75  ? 36.57400 33.23600 4.04300   0.330 35.52000  ?  75  ASP A CB  1 
ATOM   1006 C  CG  A ASP A 1 75  ? 37.21300 33.79700 3.22100   0.670 42.35000  ?  75  ASP A CG  1 
ATOM   1007 C  CG  B ASP A 1 75  ? 36.94300 34.06900 2.79500   0.330 39.46000  ?  75  ASP A CG  1 
ATOM   1008 O  OD1 A ASP A 1 75  ? 36.92900 34.98800 3.46200   0.670 42.30000  ?  75  ASP A OD1 1 
ATOM   1009 O  OD1 B ASP A 1 75  ? 37.56300 35.16000 2.93600   0.330 35.88000  ?  75  ASP A OD1 1 
ATOM   1010 O  OD2 A ASP A 1 75  ? 37.24200 33.34600 2.05200   0.670 34.42000  -1 75  ASP A OD2 1 
ATOM   1011 O  OD2 B ASP A 1 75  ? 36.67400 33.56300 1.66800   0.330 35.48000  -1 75  ASP A OD2 1 
ATOM   1012 N  N   A TRP A 1 76  ? 35.07600 33.84300 5.81400   0.670 31.04000  ?  76  TRP A N   1 
ATOM   1013 N  N   B TRP A 1 76  ? 34.40300 34.40000 5.49200   0.330 27.40000  ?  76  TRP A N   1 
ATOM   1014 C  CA  A TRP A 1 76  ? 33.88800 34.68900 5.84900   0.670 24.22000  ?  76  TRP A CA  1 
ATOM   1015 C  CA  B TRP A 1 76  ? 33.19500 35.15800 5.72000   0.330 27.97000  ?  76  TRP A CA  1 
ATOM   1016 C  C   A TRP A 1 76  ? 33.81800 35.49200 7.14400   0.670 32.86000  ?  76  TRP A C   1 
ATOM   1017 C  C   B TRP A 1 76  ? 33.24800 35.88800 7.05500   0.330 30.98000  ?  76  TRP A C   1 
ATOM   1018 O  O   A TRP A 1 76  ? 33.44500 36.67000 7.13100   0.670 28.42000  ?  76  TRP A O   1 
ATOM   1019 O  O   B TRP A 1 76  ? 33.36600 37.11800 7.05900   0.330 29.65000  ?  76  TRP A O   1 
ATOM   1020 C  CB  A TRP A 1 76  ? 32.63400 33.83000 5.67500   0.670 21.80000  ?  76  TRP A CB  1 
ATOM   1021 C  CB  B TRP A 1 76  ? 32.01800 34.21700 5.60600   0.330 27.86000  ?  76  TRP A CB  1 
ATOM   1022 C  CG  A TRP A 1 76  ? 32.44500 33.27600 4.28100   0.670 35.56000  ?  76  TRP A CG  1 
ATOM   1023 C  CG  B TRP A 1 76  ? 31.87900 33.66600 4.15900   0.330 32.23000  ?  76  TRP A CG  1 
ATOM   1024 C  CD1 A TRP A 1 76  ? 33.23900 33.49400 3.19500   0.670 35.77000  ?  76  TRP A CD1 1 
ATOM   1025 C  CD1 B TRP A 1 76  ? 32.68200 33.94300 3.09000   0.330 32.77000  ?  76  TRP A CD1 1 
ATOM   1026 C  CD2 A TRP A 1 76  ? 31.39100 32.41200 3.83900   0.670 23.27000  ?  76  TRP A CD2 1 
ATOM   1027 C  CD2 B TRP A 1 76  ? 30.92300 32.72800 3.70300   0.330 27.11000  ?  76  TRP A CD2 1 
ATOM   1028 N  NE1 A TRP A 1 76  ? 32.74300 32.82600 2.10200   0.670 33.77000  ?  76  TRP A NE1 1 
ATOM   1029 N  NE1 B TRP A 1 76  ? 32.27100 33.23700 1.98400   0.330 34.77000  ?  76  TRP A NE1 1 
ATOM   1030 C  CE2 A TRP A 1 76  ? 31.61000 32.14900 2.47200   0.670 30.86000  ?  76  TRP A CE2 1 
ATOM   1031 C  CE2 B TRP A 1 76  ? 31.17100 32.49800 2.33200   0.330 30.61000  ?  76  TRP A CE2 1 
ATOM   1032 C  CE3 A TRP A 1 76  ? 30.28300 31.83300 4.46700   0.670 33.23000  ?  76  TRP A CE3 1 
ATOM   1033 C  CE3 B TRP A 1 76  ? 29.86200 32.06400 4.32500   0.330 32.72000  ?  76  TRP A CE3 1 
ATOM   1034 C  CZ2 A TRP A 1 76  ? 30.76100 31.33400 1.72200   0.670 30.35000  ?  76  TRP A CZ2 1 
ATOM   1035 C  CZ2 B TRP A 1 76  ? 30.39600 31.64600 1.57000   0.330 30.74000  ?  76  TRP A CZ2 1 
ATOM   1036 C  CZ3 A TRP A 1 76  ? 29.44200 31.02300 3.72000   0.670 37.66000  ?  76  TRP A CZ3 1 
ATOM   1037 C  CZ3 B TRP A 1 76  ? 29.09000 31.21700 3.59100   0.330 36.47000  ?  76  TRP A CZ3 1 
ATOM   1038 C  CH2 A TRP A 1 76  ? 29.68600 30.78200 2.36400   0.670 36.21000  ?  76  TRP A CH2 1 
ATOM   1039 C  CH2 B TRP A 1 76  ? 29.34000 31.03100 2.19000   0.330 34.26000  ?  76  TRP A CH2 1 
ATOM   1040 N  N   A ILE A 1 77  ? 34.17600 34.87300 8.27200   0.670 30.07000  ?  77  ILE A N   1 
ATOM   1041 N  N   B ILE A 1 77  ? 33.26500 35.14300 8.19400   0.330 31.86000  ?  77  ILE A N   1 
ATOM   1042 C  CA  A ILE A 1 77  ? 34.04600 35.54200 9.56500   0.670 32.23000  ?  77  ILE A CA  1 
ATOM   1043 C  CA  B ILE A 1 77  ? 33.44400 35.76000 9.52300   0.330 28.91000  ?  77  ILE A CA  1 
ATOM   1044 C  C   A ILE A 1 77  ? 34.96800 36.74900 9.65500   0.670 25.44000  ?  77  ILE A C   1 
ATOM   1045 C  C   B ILE A 1 77  ? 34.36300 36.95400 9.44700   0.330 28.66000  ?  77  ILE A C   1 
ATOM   1046 O  O   A ILE A 1 77  ? 34.66900 37.71900 10.36500  0.670 33.37000  ?  77  ILE A O   1 
ATOM   1047 O  O   B ILE A 1 77  ? 34.01400 38.05400 9.86000   0.330 25.52000  ?  77  ILE A O   1 
ATOM   1048 C  CB  A ILE A 1 77  ? 34.34100 34.55300 10.71200  0.670 25.94000  ?  77  ILE A CB  1 
ATOM   1049 C  CB  B ILE A 1 77  ? 34.02900 34.75000 10.52300  0.330 30.33000  ?  77  ILE A CB  1 
ATOM   1050 C  CG1 A ILE A 1 77  ? 33.25200 33.48500 10.82700  0.670 28.34000  ?  77  ILE A CG1 1 
ATOM   1051 C  CG1 B ILE A 1 77  ? 33.09200 33.58100 10.68800  0.330 28.30000  ?  77  ILE A CG1 1 
ATOM   1052 C  CG2 A ILE A 1 77  ? 34.48500 35.30100 12.04300  0.670 34.00000  ?  77  ILE A CG2 1 
ATOM   1053 C  CG2 B ILE A 1 77  ? 34.44600 35.48200 11.77700  0.330 33.37000  ?  77  ILE A CG2 1 
ATOM   1054 C  CD1 A ILE A 1 77  ? 33.66200 32.27300 11.66000  0.670 38.90000  ?  77  ILE A CD1 1 
ATOM   1055 C  CD1 B ILE A 1 77  ? 33.78200 32.40200 11.09800  0.330 35.52000  ?  77  ILE A CD1 1 
ATOM   1056 N  N   A LEU A 1 78  ? 36.10700 36.70600 8.96700   0.670 27.96000  ?  78  LEU A N   1 
ATOM   1057 N  N   B LEU A 1 78  ? 35.56300 36.73800 8.90700   0.330 28.75000  ?  78  LEU A N   1 
ATOM   1058 C  CA  A LEU A 1 78  ? 37.06000 37.80400 9.03000   0.670 39.15000  ?  78  LEU A CA  1 
ATOM   1059 C  CA  B LEU A 1 78  ? 36.52600 37.82400 8.75400   0.330 34.64000  ?  78  LEU A CA  1 
ATOM   1060 C  C   A LEU A 1 78  ? 36.87200 38.81000 7.91000   0.670 34.98000  ?  78  LEU A C   1 
ATOM   1061 C  C   B LEU A 1 78  ? 36.09200 38.85600 7.72400   0.330 34.40000  ?  78  LEU A C   1 
ATOM   1062 O  O   A LEU A 1 78  ? 37.12500 40.00400 8.11300   0.670 39.64000  ?  78  LEU A O   1 
ATOM   1063 O  O   B LEU A 1 78  ? 35.90600 40.02600 8.05400   0.330 38.99000  ?  78  LEU A O   1 
ATOM   1064 C  CB  A LEU A 1 78  ? 38.49000 37.26600 8.97400   0.670 40.28000  ?  78  LEU A CB  1 
ATOM   1065 C  CB  B LEU A 1 78  ? 37.92000 37.28000 8.37200   0.330 36.72000  ?  78  LEU A CB  1 
ATOM   1066 C  CG  A LEU A 1 78  ? 38.90800 36.33500 10.11100  0.670 41.88000  ?  78  LEU A CG  1 
ATOM   1067 C  CG  B LEU A 1 78  ? 38.63700 36.49900 9.46500   0.330 38.98000  ?  78  LEU A CG  1 
ATOM   1068 C  CD1 A LEU A 1 78  ? 40.23100 35.67100 9.76900   0.670 30.73000  ?  78  LEU A CD1 1 
ATOM   1069 C  CD1 B LEU A 1 78  ? 40.11000 36.06400 9.14100   0.330 35.27000  ?  78  LEU A CD1 1 
ATOM   1070 C  CD2 A LEU A 1 78  ? 38.98800 37.10000 11.41200  0.670 34.86000  ?  78  LEU A CD2 1 
ATOM   1071 C  CD2 B LEU A 1 78  ? 38.52400 37.21800 10.87300  0.330 33.80000  ?  78  LEU A CD2 1 
ATOM   1072 N  N   A THR A 1 79  ? 36.44300 38.35900 6.73200   0.670 33.49000  ?  79  THR A N   1 
ATOM   1073 N  N   B THR A 1 79  ? 36.03100 38.49000 6.45100   0.330 32.06000  ?  79  THR A N   1 
ATOM   1074 C  CA  A THR A 1 79  ? 36.37400 39.24600 5.57900   0.670 33.75000  ?  79  THR A CA  1 
ATOM   1075 C  CA  B THR A 1 79  ? 36.08700 39.60200 5.49500   0.330 33.27000  ?  79  THR A CA  1 
ATOM   1076 C  C   A THR A 1 79  ? 35.04700 39.99000 5.48900   0.670 30.21000  ?  79  THR A C   1 
ATOM   1077 C  C   B THR A 1 79  ? 34.77600 40.35500 5.42600   0.330 34.31000  ?  79  THR A C   1 
ATOM   1078 O  O   A THR A 1 79  ? 35.02800 41.16300 5.09800   0.670 40.11000  ?  79  THR A O   1 
ATOM   1079 O  O   B THR A 1 79  ? 34.78700 41.55900 5.15300   0.330 40.17000  ?  79  THR A O   1 
ATOM   1080 C  CB  A THR A 1 79  ? 36.61300 38.46800 4.27700   0.670 32.94000  ?  79  THR A CB  1 
ATOM   1081 C  CB  B THR A 1 79  ? 36.47600 39.16100 4.09400   0.330 30.84000  ?  79  THR A CB  1 
ATOM   1082 O  OG1 A THR A 1 79  ? 35.61000 37.46200 4.10700   0.670 29.01000  ?  79  THR A OG1 1 
ATOM   1083 O  OG1 B THR A 1 79  ? 35.31000 38.70700 3.40700   0.330 33.13000  ?  79  THR A OG1 1 
ATOM   1084 C  CG2 A THR A 1 79  ? 37.98900 37.81800 4.28400   0.670 31.63000  ?  79  THR A CG2 1 
ATOM   1085 C  CG2 B THR A 1 79  ? 37.40000 37.97100 4.18800   0.330 31.98000  ?  79  THR A CG2 1 
ATOM   1086 N  N   A THR A 1 80  ? 33.93100 39.35000 5.84400   0.670 34.36000  ?  80  THR A N   1 
ATOM   1087 N  N   B THR A 1 80  ? 33.64700 39.69800 5.69300   0.330 35.54000  ?  80  THR A N   1 
ATOM   1088 C  CA  A THR A 1 80  ? 32.65200 40.04700 5.73700   0.670 36.88000  ?  80  THR A CA  1 
ATOM   1089 C  CA  B THR A 1 80  ? 32.34300 40.38600 5.70400   0.330 35.28000  ?  80  THR A CA  1 
ATOM   1090 C  C   A THR A 1 80  ? 32.55800 41.25500 6.66400   0.670 37.08000  ?  80  THR A C   1 
ATOM   1091 C  C   B THR A 1 80  ? 32.16600 41.53800 6.71400   0.330 37.72000  ?  80  THR A C   1 
ATOM   1092 O  O   A THR A 1 80  ? 31.98900 42.27500 6.23600   0.670 35.73000  ?  80  THR A O   1 
ATOM   1093 O  O   B THR A 1 80  ? 31.32000 42.40300 6.47700   0.330 37.07000  ?  80  THR A O   1 
ATOM   1094 C  CB  A THR A 1 80  ? 31.47500 39.08800 5.98000   0.670 31.08000  ?  80  THR A CB  1 
ATOM   1095 C  CB  B THR A 1 80  ? 31.19900 39.34500 5.85100   0.330 32.44000  ?  80  THR A CB  1 
ATOM   1096 O  OG1 A THR A 1 80  ? 31.57900 38.47200 7.27100   0.670 39.00000  ?  80  THR A OG1 1 
ATOM   1097 O  OG1 B THR A 1 80  ? 31.44200 38.46700 6.94400   0.330 36.06000  ?  80  THR A OG1 1 
ATOM   1098 C  CG2 A THR A 1 80  ? 31.42100 38.02100 4.89000   0.670 33.31000  ?  80  THR A CG2 1 
ATOM   1099 C  CG2 B THR A 1 80  ? 31.00500 38.49700 4.58400   0.330 33.20000  ?  80  THR A CG2 1 
ATOM   1100 N  N   A PRO A 1 81  ? 33.06400 41.23400 7.90700   0.670 37.81000  ?  81  PRO A N   1 
ATOM   1101 N  N   B PRO A 1 81  ? 32.88000 41.60700 7.84200   0.330 37.58000  ?  81  PRO A N   1 
ATOM   1102 C  CA  A PRO A 1 81  ? 33.03500 42.47900 8.69800   0.670 32.15000  ?  81  PRO A CA  1 
ATOM   1103 C  CA  B PRO A 1 81  ? 32.97800 42.91000 8.53600   0.330 33.14000  ?  81  PRO A CA  1 
ATOM   1104 C  C   A PRO A 1 81  ? 33.88400 43.57800 8.08400   0.670 34.84000  ?  81  PRO A C   1 
ATOM   1105 C  C   B PRO A 1 81  ? 33.81600 43.91500 7.81100   0.330 36.04000  ?  81  PRO A C   1 
ATOM   1106 O  O   A PRO A 1 81  ? 33.57700 44.76200 8.26700   0.670 37.42000  ?  81  PRO A O   1 
ATOM   1107 O  O   B PRO A 1 81  ? 33.44800 45.11200 7.77200   0.330 34.79000  ?  81  PRO A O   1 
ATOM   1108 C  CB  A PRO A 1 81  ? 33.55900 42.05200 10.07800  0.670 35.86000  ?  81  PRO A CB  1 
ATOM   1109 C  CB  B PRO A 1 81  ? 33.61500 42.57800 9.87300   0.330 35.27000  ?  81  PRO A CB  1 
ATOM   1110 C  CG  A PRO A 1 81  ? 34.34100 40.80500 9.82500   0.670 37.53000  ?  81  PRO A CG  1 
ATOM   1111 C  CG  B PRO A 1 81  ? 34.12500 41.20500 9.75500   0.330 36.29000  ?  81  PRO A CG  1 
ATOM   1112 C  CD  A PRO A 1 81  ? 33.66900 40.11500 8.65700   0.670 35.33000  ?  81  PRO A CD  1 
ATOM   1113 C  CD  B PRO A 1 81  ? 33.15600 40.51400 8.76000   0.330 35.86000  ?  81  PRO A CD  1 
ATOM   1114 N  N   A LEU A 1 82  ? 34.93700 43.21600 7.34800   0.670 38.44000  ?  82  LEU A N   1 
ATOM   1115 N  N   B LEU A 1 82  ? 34.93700 43.46100 7.22800   0.330 38.56000  ?  82  LEU A N   1 
ATOM   1116 C  CA  A LEU A 1 82  ? 35.74900 44.21600 6.66600   0.670 35.16000  ?  82  LEU A CA  1 
ATOM   1117 C  CA  B LEU A 1 82  ? 35.74600 44.31500 6.34600   0.330 34.45000  ?  82  LEU A CA  1 
ATOM   1118 C  C   A LEU A 1 82  ? 34.98200 44.85200 5.51400   0.670 36.19000  ?  82  LEU A C   1 
ATOM   1119 C  C   B LEU A 1 82  ? 34.92800 45.01300 5.25600   0.330 37.15000  ?  82  LEU A C   1 
ATOM   1120 O  O   A LEU A 1 82  ? 35.15500 46.04300 5.22800   0.670 38.95000  ?  82  LEU A O   1 
ATOM   1121 O  O   B LEU A 1 82  ? 35.19300 46.17100 4.89700   0.330 39.44000  ?  82  LEU A O   1 
ATOM   1122 C  CB  A LEU A 1 82  ? 37.03800 43.57300 6.16100   0.670 34.98000  ?  82  LEU A CB  1 
ATOM   1123 C  CB  B LEU A 1 82  ? 36.85000 43.48900 5.70200   0.330 34.95000  ?  82  LEU A CB  1 
ATOM   1124 C  CG  A LEU A 1 82  ? 38.07600 43.18700 7.21900   0.670 34.65000  ?  82  LEU A CG  1 
ATOM   1125 C  CG  B LEU A 1 82  ? 37.99300 43.17200 6.65600   0.330 35.32000  ?  82  LEU A CG  1 
ATOM   1126 C  CD1 A LEU A 1 82  ? 39.19300 42.38500 6.57000   0.670 32.35000  ?  82  LEU A CD1 1 
ATOM   1127 C  CD1 B LEU A 1 82  ? 39.24100 42.69000 5.88500   0.330 30.49000  ?  82  LEU A CD1 1 
ATOM   1128 C  CD2 A LEU A 1 82  ? 38.61100 44.42300 7.91000   0.670 33.76000  ?  82  LEU A CD2 1 
ATOM   1129 C  CD2 B LEU A 1 82  ? 38.21600 44.48100 7.37300   0.330 32.36000  ?  82  LEU A CD2 1 
ATOM   1130 N  N   A ILE A 1 83  ? 34.13800 44.07400 4.83700   0.670 41.11000  ?  83  ILE A N   1 
ATOM   1131 N  N   B ILE A 1 83  ? 33.94800 44.30300 4.69000   0.330 40.34000  ?  83  ILE A N   1 
ATOM   1132 C  CA  A ILE A 1 83  ? 33.28700 44.63900 3.79700   0.670 40.72000  ?  83  ILE A CA  1 
ATOM   1133 C  CA  B ILE A 1 83  ? 33.16000 44.82900 3.57500   0.330 39.70000  ?  83  ILE A CA  1 
ATOM   1134 C  C   A ILE A 1 83  ? 32.27200 45.59500 4.41000   0.670 42.59000  ?  83  ILE A C   1 
ATOM   1135 C  C   B ILE A 1 83  ? 32.07200 45.74200 4.11000   0.330 41.79000  ?  83  ILE A C   1 
ATOM   1136 O  O   A ILE A 1 83  ? 32.01700 46.68100 3.87500   0.670 39.71000  ?  83  ILE A O   1 
ATOM   1137 O  O   B ILE A 1 83  ? 31.82400 46.81700 3.56200   0.330 39.49000  ?  83  ILE A O   1 
ATOM   1138 C  CB  A ILE A 1 83  ? 32.59100 43.51600 3.00800   0.670 37.56000  ?  83  ILE A CB  1 
ATOM   1139 C  CB  B ILE A 1 83  ? 32.58400 43.65800 2.72900   0.330 36.87000  ?  83  ILE A CB  1 
ATOM   1140 C  CG1 A ILE A 1 83  ? 33.61300 42.68600 2.23200   0.670 43.51000  ?  83  ILE A CG1 1 
ATOM   1141 C  CG1 B ILE A 1 83  ? 33.73200 42.88700 2.05500   0.330 41.91000  ?  83  ILE A CG1 1 
ATOM   1142 C  CG2 A ILE A 1 83  ? 31.55600 44.10400 2.06200   0.670 32.02000  ?  83  ILE A CG2 1 
ATOM   1143 C  CG2 B ILE A 1 83  ? 31.54500 44.13700 1.69500   0.330 32.48000  ?  83  ILE A CG2 1 
ATOM   1144 C  CD1 A ILE A 1 83  ? 33.03300 41.43900 1.58600   0.670 35.61000  ?  83  ILE A CD1 1 
ATOM   1145 C  CD1 B ILE A 1 83  ? 33.40400 41.48600 1.49500   0.330 35.74000  ?  83  ILE A CD1 1 
ATOM   1146 N  N   A VAL A 1 84  ? 31.66900 45.20200 5.53500   0.670 42.39000  ?  84  VAL A N   1 
ATOM   1147 N  N   B VAL A 1 84  ? 31.36700 45.31400 5.16500   0.330 41.15000  ?  84  VAL A N   1 
ATOM   1148 C  CA  A VAL A 1 84  ? 30.72500 46.07900 6.22100   0.670 38.80000  ?  84  VAL A CA  1 
ATOM   1149 C  CA  B VAL A 1 84  ? 30.44600 46.24500 5.80800   0.330 37.93000  ?  84  VAL A CA  1 
ATOM   1150 C  C   A VAL A 1 84  ? 31.44100 47.31400 6.74900   0.670 42.88000  ?  84  VAL A C   1 
ATOM   1151 C  C   B VAL A 1 84  ? 31.22700 47.44300 6.36600   0.330 41.64000  ?  84  VAL A C   1 
ATOM   1152 O  O   A VAL A 1 84  ? 30.89700 48.42500 6.72300   0.670 42.58000  ?  84  VAL A O   1 
ATOM   1153 O  O   B VAL A 1 84  ? 30.74900 48.57900 6.36100   0.330 43.49000  ?  84  VAL A O   1 
ATOM   1154 C  CB  A VAL A 1 84  ? 30.01000 45.30700 7.34600   0.670 43.28000  ?  84  VAL A CB  1 
ATOM   1155 C  CB  B VAL A 1 84  ? 29.64200 45.54000 6.91700   0.330 42.29000  ?  84  VAL A CB  1 
ATOM   1156 C  CG1 A VAL A 1 84  ? 29.25100 46.25400 8.25600   0.670 45.36000  ?  84  VAL A CG1 1 
ATOM   1157 C  CG1 B VAL A 1 84  ? 28.68700 46.53500 7.62900   0.330 39.17000  ?  84  VAL A CG1 1 
ATOM   1158 C  CG2 A VAL A 1 84  ? 29.08200 44.25300 6.75100   0.670 34.19000  ?  84  VAL A CG2 1 
ATOM   1159 C  CG2 B VAL A 1 84  ? 28.92600 44.28900 6.37100   0.330 35.18000  ?  84  VAL A CG2 1 
ATOM   1160 N  N   A TYR A 1 85  ? 32.67400 47.14600 7.22500   0.670 46.48000  ?  85  TYR A N   1 
ATOM   1161 N  N   B TYR A 1 85  ? 32.42500 47.21800 6.89500   0.330 44.45000  ?  85  TYR A N   1 
ATOM   1162 C  CA  A TYR A 1 85  ? 33.46200 48.29500 7.65800   0.670 48.08000  ?  85  TYR A CA  1 
ATOM   1163 C  CA  B TYR A 1 85  ? 33.22500 48.38300 7.24400   0.330 45.45000  ?  85  TYR A CA  1 
ATOM   1164 C  C   A TYR A 1 85  ? 33.69000 49.26400 6.50400   0.670 40.88000  ?  85  TYR A C   1 
ATOM   1165 C  C   B TYR A 1 85  ? 33.24100 49.31900 6.06800   0.330 41.10000  ?  85  TYR A C   1 
ATOM   1166 O  O   A TYR A 1 85  ? 33.49100 50.47600 6.64600   0.670 34.32000  ?  85  TYR A O   1 
ATOM   1167 O  O   B TYR A 1 85  ? 32.74100 50.45200 6.13200   0.330 31.68000  ?  85  TYR A O   1 
ATOM   1168 C  CB  A TYR A 1 85  ? 34.79100 47.81400 8.24000   0.670 45.65000  ?  85  TYR A CB  1 
ATOM   1169 C  CB  B TYR A 1 85  ? 34.66100 47.98700 7.62100   0.330 44.79000  ?  85  TYR A CB  1 
ATOM   1170 C  CG  A TYR A 1 85  ? 35.72500 48.92400 8.64700   0.670 49.47000  ?  85  TYR A CG  1 
ATOM   1171 C  CG  B TYR A 1 85  ? 35.58600 49.14100 7.96400   0.330 39.47000  ?  85  TYR A CG  1 
ATOM   1172 C  CD1 A TYR A 1 85  ? 35.36500 49.83700 9.62700   0.670 60.24000  ?  85  TYR A CD1 1 
ATOM   1173 C  CD1 B TYR A 1 85  ? 35.26000 50.08500 8.97200   0.330 59.54000  ?  85  TYR A CD1 1 
ATOM   1174 C  CD2 A TYR A 1 85  ? 36.97100 49.05800 8.05000   0.670 55.21000  ?  85  TYR A CD2 1 
ATOM   1175 C  CD2 B TYR A 1 85  ? 36.83000 49.23900 7.38500   0.330 49.93000  ?  85  TYR A CD2 1 
ATOM   1176 C  CE1 A TYR A 1 85  ? 36.22000 50.85400 10.00100  0.670 53.15000  ?  85  TYR A CE1 1 
ATOM   1177 C  CE1 B TYR A 1 85  ? 36.15200 51.15900 9.32200   0.330 54.72000  ?  85  TYR A CE1 1 
ATOM   1178 C  CE2 A TYR A 1 85  ? 37.83000 50.06800 8.41500   0.670 62.76000  ?  85  TYR A CE2 1 
ATOM   1179 C  CE2 B TYR A 1 85  ? 37.72600 50.28300 7.73300   0.330 56.49000  ?  85  TYR A CE2 1 
ATOM   1180 C  CZ  A TYR A 1 85  ? 37.45300 50.96500 9.39100   0.670 50.11000  ?  85  TYR A CZ  1 
ATOM   1181 C  CZ  B TYR A 1 85  ? 37.37700 51.22300 8.69000   0.330 54.31000  ?  85  TYR A CZ  1 
ATOM   1182 O  OH  A TYR A 1 85  ? 38.31300 51.97600 9.75700   0.670 67.76000  ?  85  TYR A OH  1 
ATOM   1183 O  OH  B TYR A 1 85  ? 38.28600 52.19500 8.96300   0.330 65.27000  ?  85  TYR A OH  1 
ATOM   1184 N  N   A PHE A 1 86  ? 34.09900 48.74500 5.34400   0.670 45.96000  ?  86  PHE A N   1 
ATOM   1185 N  N   B PHE A 1 86  ? 33.78200 48.80000 4.96200   0.330 44.13000  ?  86  PHE A N   1 
ATOM   1186 C  CA  A PHE A 1 86  ? 34.29000 49.59200 4.17000   0.670 42.48000  ?  86  PHE A CA  1 
ATOM   1187 C  CA  B PHE A 1 86  ? 33.92100 49.59200 3.74600   0.330 42.05000  ?  86  PHE A CA  1 
ATOM   1188 C  C   A PHE A 1 86  ? 33.02800 50.38900 3.86200   0.670 45.39000  ?  86  PHE A C   1 
ATOM   1189 C  C   B PHE A 1 86  ? 32.68900 50.42300 3.44700   0.330 43.24000  ?  86  PHE A C   1 
ATOM   1190 O  O   A PHE A 1 86  ? 33.07900 51.60700 3.65500   0.670 46.01000  ?  86  PHE A O   1 
ATOM   1191 O  O   B PHE A 1 86  ? 32.79300 51.62100 3.20800   0.330 44.81000  ?  86  PHE A O   1 
ATOM   1192 C  CB  A PHE A 1 86  ? 34.69700 48.72200 2.97600   0.670 43.93000  ?  86  PHE A CB  1 
ATOM   1193 C  CB  B PHE A 1 86  ? 34.22100 48.68700 2.56600   0.330 40.16000  ?  86  PHE A CB  1 
ATOM   1194 C  CG  A PHE A 1 86  ? 35.12400 49.50100 1.76300   0.670 34.42000  ?  86  PHE A CG  1 
ATOM   1195 C  CG  B PHE A 1 86  ? 34.57800 49.43300 1.33000   0.330 37.59000  ?  86  PHE A CG  1 
ATOM   1196 C  CD1 A PHE A 1 86  ? 34.18600 50.12800 0.96100   0.670 38.63000  ?  86  PHE A CD1 1 
ATOM   1197 C  CD1 B PHE A 1 86  ? 35.87900 49.84800 1.17300   0.330 39.01000  ?  86  PHE A CD1 1 
ATOM   1198 C  CD2 A PHE A 1 86  ? 36.46300 49.58800 1.41200   0.670 35.11000  ?  86  PHE A CD2 1 
ATOM   1199 C  CD2 B PHE A 1 86  ? 33.61400 49.82100 0.39100   0.330 38.49000  ?  86  PHE A CD2 1 
ATOM   1200 C  CE1 A PHE A 1 86  ? 34.57400 50.84000 -0.15600  0.670 46.89000  ?  86  PHE A CE1 1 
ATOM   1201 C  CE1 B PHE A 1 86  ? 36.25400 50.54700 0.05700   0.330 44.89000  ?  86  PHE A CE1 1 
ATOM   1202 C  CE2 A PHE A 1 86  ? 36.85400 50.29600 0.29500   0.670 45.79000  ?  86  PHE A CE2 1 
ATOM   1203 C  CE2 B PHE A 1 86  ? 33.96900 50.52200 -0.72500  0.330 42.23000  ?  86  PHE A CE2 1 
ATOM   1204 C  CZ  A PHE A 1 86  ? 35.90900 50.92100 -0.49000  0.670 44.27000  ?  86  PHE A CZ  1 
ATOM   1205 C  CZ  B PHE A 1 86  ? 35.30700 50.89400 -0.90100  0.330 46.54000  ?  86  PHE A CZ  1 
ATOM   1206 N  N   A LEU A 1 87  ? 31.87700 49.71100 3.83500   0.670 39.31000  ?  87  LEU A N   1 
ATOM   1207 N  N   B LEU A 1 87  ? 31.51200 49.81000 3.46700   0.330 33.00000  ?  87  LEU A N   1 
ATOM   1208 C  CA  A LEU A 1 87  ? 30.62100 50.40700 3.58100   0.670 33.88000  ?  87  LEU A CA  1 
ATOM   1209 C  CA  B LEU A 1 87  ? 30.30900 50.58300 3.21900   0.330 39.56000  ?  87  LEU A CA  1 
ATOM   1210 C  C   A LEU A 1 87  ? 30.31400 51.42700 4.66900   0.670 46.96000  ?  87  LEU A C   1 
ATOM   1211 C  C   B LEU A 1 87  ? 30.15800 51.71200 4.21500   0.330 45.82000  ?  87  LEU A C   1 
ATOM   1212 O  O   A LEU A 1 87  ? 29.75100 52.49000 4.38500   0.670 47.13000  ?  87  LEU A O   1 
ATOM   1213 O  O   B LEU A 1 87  ? 30.42700 52.87200 3.89300   0.330 46.52000  ?  87  LEU A O   1 
ATOM   1214 C  CB  A LEU A 1 87  ? 29.47500 49.40300 3.48100   0.670 42.58000  ?  87  LEU A CB  1 
ATOM   1215 C  CB  B LEU A 1 87  ? 29.06500 49.70000 3.25400   0.330 41.98000  ?  87  LEU A CB  1 
ATOM   1216 C  CG  A LEU A 1 87  ? 29.61000 48.33300 2.40200   0.670 47.08000  ?  87  LEU A CG  1 
ATOM   1217 C  CG  B LEU A 1 87  ? 28.97600 48.57300 2.26200   0.330 42.09000  ?  87  LEU A CG  1 
ATOM   1218 C  CD1 A LEU A 1 87  ? 28.65400 47.18200 2.66200   0.670 50.90000  ?  87  LEU A CD1 1 
ATOM   1219 C  CD1 B LEU A 1 87  ? 27.59400 47.85200 2.41500   0.330 39.38000  ?  87  LEU A CD1 1 
ATOM   1220 C  CD2 A LEU A 1 87  ? 29.35100 48.94600 1.03300   0.670 34.44000  ?  87  LEU A CD2 1 
ATOM   1221 C  CD2 B LEU A 1 87  ? 29.29000 49.09500 0.87600   0.330 37.23000  ?  87  LEU A CD2 1 
ATOM   1222 N  N   A GLY A 1 88  ? 30.65900 51.11800 5.91900   0.670 51.81000  ?  88  GLY A N   1 
ATOM   1223 N  N   B GLY A 1 88  ? 29.61600 51.39300 5.39500   0.330 46.43000  ?  88  GLY A N   1 
ATOM   1224 C  CA  A GLY A 1 88  ? 30.39000 52.04300 7.00300   0.670 51.60000  ?  88  GLY A CA  1 
ATOM   1225 C  CA  B GLY A 1 88  ? 29.59000 52.33600 6.50200   0.330 49.85000  ?  88  GLY A CA  1 
ATOM   1226 C  C   A GLY A 1 88  ? 31.21800 53.30400 6.93000   0.670 54.53000  ?  88  GLY A C   1 
ATOM   1227 C  C   B GLY A 1 88  ? 30.58300 53.48100 6.40400   0.330 56.16000  ?  88  GLY A C   1 
ATOM   1228 O  O   A GLY A 1 88  ? 30.74800 54.37700 7.31900   0.670 53.48000  ?  88  GLY A O   1 
ATOM   1229 O  O   B GLY A 1 88  ? 30.21000 54.62500 6.66700   0.330 55.09000  ?  88  GLY A O   1 
ATOM   1230 N  N   A LEU A 1 89  ? 32.45300 53.19900 6.43900   0.670 47.24000  ?  89  LEU A N   1 
ATOM   1231 N  N   B LEU A 1 89  ? 31.85800 53.19100 6.03400   0.330 50.88000  ?  89  LEU A N   1 
ATOM   1232 C  CA  A LEU A 1 89  ? 33.26100 54.39200 6.22700   0.670 43.74000  ?  89  LEU A CA  1 
ATOM   1233 C  CA  B LEU A 1 89  ? 32.85000 54.23800 5.74500   0.330 50.97000  ?  89  LEU A CA  1 
ATOM   1234 C  C   A LEU A 1 89  ? 32.64300 55.27900 5.15400   0.670 58.54000  ?  89  LEU A C   1 
ATOM   1235 C  C   B LEU A 1 89  ? 32.48500 55.11400 4.56100   0.330 57.94000  ?  89  LEU A C   1 
ATOM   1236 O  O   A LEU A 1 89  ? 32.54300 56.49900 5.32400   0.670 65.06000  ?  89  LEU A O   1 
ATOM   1237 O  O   B LEU A 1 89  ? 33.09200 56.17700 4.39100   0.330 62.51000  ?  89  LEU A O   1 
ATOM   1238 C  CB  A LEU A 1 89  ? 34.68500 53.99900 5.84000   0.670 40.82000  ?  89  LEU A CB  1 
ATOM   1239 C  CB  B LEU A 1 89  ? 34.20800 53.68900 5.40000   0.330 46.08000  ?  89  LEU A CB  1 
ATOM   1240 C  CG  A LEU A 1 89  ? 35.56200 53.36000 6.91700   0.670 57.17000  ?  89  LEU A CG  1 
ATOM   1241 C  CG  B LEU A 1 89  ? 35.21900 53.27200 6.42100   0.330 53.38000  ?  89  LEU A CG  1 
ATOM   1242 C  CD1 A LEU A 1 89  ? 36.88100 52.90100 6.29400   0.670 60.89000  ?  89  LEU A CD1 1 
ATOM   1243 C  CD1 B LEU A 1 89  ? 36.49100 52.66400 5.71500   0.330 55.78000  ?  89  LEU A CD1 1 
ATOM   1244 C  CD2 A LEU A 1 89  ? 35.81200 54.31400 8.06600   0.670 66.61000  ?  89  LEU A CD2 1 
ATOM   1245 C  CD2 B LEU A 1 89  ? 35.53400 54.55100 7.12800   0.330 57.44000  ?  89  LEU A CD2 1 
ATOM   1246 N  N   A LEU A 1 90  ? 32.23200 54.68000 4.03300   0.670 56.62000  ?  90  LEU A N   1 
ATOM   1247 N  N   B LEU A 1 90  ? 31.60200 54.64800 3.68500   0.330 54.01000  ?  90  LEU A N   1 
ATOM   1248 C  CA  A LEU A 1 90  ? 31.59300 55.45500 2.97600   0.670 60.22000  ?  90  LEU A CA  1 
ATOM   1249 C  CA  B LEU A 1 90  ? 31.01200 55.48000 2.64700   0.330 59.31000  ?  90  LEU A CA  1 
ATOM   1250 C  C   A LEU A 1 90  ? 30.37600 56.20000 3.50500   0.670 56.76000  ?  90  LEU A C   1 
ATOM   1251 C  C   B LEU A 1 90  ? 29.70200 56.05400 3.13800   0.330 57.18000  ?  90  LEU A C   1 
ATOM   1252 O  O   A LEU A 1 90  ? 30.16800 57.37600 3.18400   0.670 59.14000  ?  90  LEU A O   1 
ATOM   1253 O  O   B LEU A 1 90  ? 29.25700 57.09600 2.63700   0.330 55.78000  ?  90  LEU A O   1 
ATOM   1254 C  CB  A LEU A 1 90  ? 31.18100 54.54000 1.82700   0.670 52.23000  ?  90  LEU A CB  1 
ATOM   1255 C  CB  B LEU A 1 90  ? 30.76700 54.64200 1.38800   0.330 48.64000  ?  90  LEU A CB  1 
ATOM   1256 C  CG  A LEU A 1 90  ? 32.19100 54.20100 0.73300   0.670 57.61000  ?  90  LEU A CG  1 
ATOM   1257 C  CG  B LEU A 1 90  ? 32.01300 54.43600 0.58400   0.330 56.86000  ?  90  LEU A CG  1 
ATOM   1258 C  CD1 A LEU A 1 90  ? 31.49800 53.32300 -0.31300  0.670 51.50000  ?  90  LEU A CD1 1 
ATOM   1259 C  CD1 B LEU A 1 90  ? 31.69900 53.42300 -0.46700  0.330 52.00000  ?  90  LEU A CD1 1 
ATOM   1260 C  CD2 A LEU A 1 90  ? 32.77400 55.43600 0.09800   0.670 57.91000  ?  90  LEU A CD2 1 
ATOM   1261 C  CD2 B LEU A 1 90  ? 32.37400 55.73300 -0.04500  0.330 57.53000  ?  90  LEU A CD2 1 
ATOM   1262 N  N   A ALA A 1 91  ? 29.55400 55.52800 4.31000   0.670 50.66000  ?  91  ALA A N   1 
ATOM   1263 N  N   B ALA A 1 91  ? 29.07900 55.36500 4.11100   0.330 51.23000  ?  91  ALA A N   1 
ATOM   1264 C  CA  A ALA A 1 91  ? 28.33500 56.12700 4.83200   0.670 56.96000  ?  91  ALA A CA  1 
ATOM   1265 C  CA  B ALA A 1 91  ? 27.83500 55.83500 4.68900   0.330 54.96000  ?  91  ALA A CA  1 
ATOM   1266 C  C   A ALA A 1 91  ? 28.59100 57.09000 5.98200   0.670 62.02000  ?  91  ALA A C   1 
ATOM   1267 C  C   B ALA A 1 91  ? 28.10800 56.84800 5.77800   0.330 60.35000  ?  91  ALA A C   1 
ATOM   1268 O  O   A ALA A 1 91  ? 27.69100 57.86200 6.33100   0.670 60.33000  ?  91  ALA A O   1 
ATOM   1269 O  O   B ALA A 1 91  ? 27.43300 57.87500 5.84900   0.330 60.17000  ?  91  ALA A O   1 
ATOM   1270 C  CB  A ALA A 1 91  ? 27.37200 55.02800 5.28900   0.670 59.13000  ?  91  ALA A CB  1 
ATOM   1271 C  CB  B ALA A 1 91  ? 27.03700 54.65600 5.24700   0.330 58.01000  ?  91  ALA A CB  1 
ATOM   1272 N  N   A GLY A 1 92  ? 29.78200 57.06600 6.57400   0.670 61.80000  ?  92  GLY A N   1 
ATOM   1273 N  N   B GLY A 1 92  ? 29.13200 56.59600 6.58700   0.330 60.97000  ?  92  GLY A N   1 
ATOM   1274 C  CA  A GLY A 1 92  ? 30.10000 57.96300 7.66600   0.670 68.51000  ?  92  GLY A CA  1 
ATOM   1275 C  CA  B GLY A 1 92  ? 29.44000 57.46000 7.69800   0.330 63.25000  ?  92  GLY A CA  1 
ATOM   1276 C  C   A GLY A 1 92  ? 29.41300 57.60300 8.96500   0.670 69.67000  ?  92  GLY A C   1 
ATOM   1277 C  C   B GLY A 1 92  ? 28.54700 57.08100 8.84500   0.330 64.59000  ?  92  GLY A C   1 
ATOM   1278 O  O   A GLY A 1 92  ? 28.80900 58.46200 9.61600   0.670 86.99000  ?  92  GLY A O   1 
ATOM   1279 O  O   B GLY A 1 92  ? 27.52600 57.72300 9.09400   0.330 70.42000  ?  92  GLY A O   1 
ATOM   1280 N  N   A LEU A 1 93  ? 29.50100 56.33800 9.36000   0.670 63.96000  ?  93  LEU A N   1 
ATOM   1281 N  N   B LEU A 1 93  ? 28.89400 56.00500 9.52400   0.330 67.63000  ?  93  LEU A N   1 
ATOM   1282 C  CA  A LEU A 1 93  ? 28.88000 55.89300 10.59700  0.670 71.95000  ?  93  LEU A CA  1 
ATOM   1283 C  CA  B LEU A 1 93  ? 28.17600 55.59100 10.71500  0.330 69.60000  ?  93  LEU A CA  1 
ATOM   1284 C  C   A LEU A 1 93  ? 29.70400 56.32600 11.80200  0.670 76.50000  ?  93  LEU A C   1 
ATOM   1285 C  C   B LEU A 1 93  ? 29.03000 55.88900 11.93200  0.330 72.43000  ?  93  LEU A C   1 
ATOM   1286 O  O   A LEU A 1 93  ? 30.93800 56.33900 11.75900  0.670 80.13000  ?  93  LEU A O   1 
ATOM   1287 O  O   B LEU A 1 93  ? 30.24400 55.65400 11.91000  0.330 75.41000  ?  93  LEU A O   1 
ATOM   1288 C  CB  A LEU A 1 93  ? 28.73600 54.37400 10.60400  0.670 67.64000  ?  93  LEU A CB  1 
ATOM   1289 C  CB  B LEU A 1 93  ? 27.83400 54.10700 10.65800  0.330 67.97000  ?  93  LEU A CB  1 
ATOM   1290 C  CG  A LEU A 1 93  ? 27.61900 53.76200 9.76300   0.670 60.70000  ?  93  LEU A CG  1 
ATOM   1291 C  CG  B LEU A 1 93  ? 26.62300 53.74200 9.80200   0.330 62.39000  ?  93  LEU A CG  1 
ATOM   1292 C  CD1 A LEU A 1 93  ? 27.63300 52.24800 9.94800   0.670 63.45000  ?  93  LEU A CD1 1 
ATOM   1293 C  CD1 B LEU A 1 93  ? 26.43600 52.24700 9.81000   0.330 59.51000  ?  93  LEU A CD1 1 
ATOM   1294 C  CD2 A LEU A 1 93  ? 26.27200 54.34400 10.12900  0.670 64.42000  ?  93  LEU A CD2 1 
ATOM   1295 C  CD2 B LEU A 1 93  ? 25.36900 54.40700 10.31400  0.330 59.51000  ?  93  LEU A CD2 1 
ATOM   1296 N  N   A ASP A 1 94  ? 29.01400 56.67900 12.88200  0.670 78.44000  ?  94  ASP A N   1 
ATOM   1297 N  N   B ASP A 1 94  ? 28.40400 56.45800 12.95800  0.330 75.75000  ?  94  ASP A N   1 
ATOM   1298 C  CA  A ASP A 1 94  ? 29.68600 56.87000 14.15600  0.670 78.15000  ?  94  ASP A CA  1 
ATOM   1299 C  CA  B ASP A 1 94  ? 29.05500 56.65100 14.24800  0.330 79.08000  ?  94  ASP A CA  1 
ATOM   1300 C  C   A ASP A 1 94  ? 30.08900 55.51400 14.73100  0.670 79.12000  ?  94  ASP A C   1 
ATOM   1301 C  C   B ASP A 1 94  ? 29.65500 55.34500 14.71900  0.330 79.25000  ?  94  ASP A C   1 
ATOM   1302 O  O   A ASP A 1 94  ? 29.50500 54.47200 14.41100  0.670 81.44000  ?  94  ASP A O   1 
ATOM   1303 O  O   B ASP A 1 94  ? 29.02000 54.29600 14.59400  0.330 79.38000  ?  94  ASP A O   1 
ATOM   1304 C  CB  A ASP A 1 94  ? 28.78600 57.62500 15.13300  0.670 76.83000  ?  94  ASP A CB  1 
ATOM   1305 C  CB  B ASP A 1 94  ? 28.01100 57.13400 15.22700  0.330 83.04000  ?  94  ASP A CB  1 
ATOM   1306 C  CG  A ASP A 1 94  ? 27.55500 56.83800 15.51900  0.670 85.58000  ?  94  ASP A CG  1 
ATOM   1307 C  CG  B ASP A 1 94  ? 26.73500 56.32200 15.10200  0.330 85.96000  ?  94  ASP A CG  1 
ATOM   1308 O  OD1 A ASP A 1 94  ? 26.80700 56.41200 14.61500  0.670 88.73000  ?  94  ASP A OD1 1 
ATOM   1309 O  OD1 B ASP A 1 94  ? 26.21900 56.25000 13.95000  0.330 84.68000  ?  94  ASP A OD1 1 
ATOM   1310 O  OD2 A ASP A 1 94  ? 27.33600 56.64700 16.73200  0.670 100.76000 -1 94  ASP A OD2 1 
ATOM   1311 O  OD2 B ASP A 1 94  ? 26.27200 55.74200 16.10200  0.330 87.07000  -1 94  ASP A OD2 1 
ATOM   1312 N  N   A SER A 1 95  ? 31.10500 55.53800 15.59700  0.670 86.10000  ?  95  SER A N   1 
ATOM   1313 N  N   B SER A 1 95  ? 30.86500 55.40400 15.29300  0.330 84.00000  ?  95  SER A N   1 
ATOM   1314 C  CA  A SER A 1 95  ? 31.67300 54.30100 16.12200  0.670 76.80000  ?  95  SER A CA  1 
ATOM   1315 C  CA  B SER A 1 95  ? 31.57100 54.17700 15.65700  0.330 78.94000  ?  95  SER A CA  1 
ATOM   1316 C  C   A SER A 1 95  ? 30.64000 53.40700 16.79500  0.670 78.72000  ?  95  SER A C   1 
ATOM   1317 C  C   B SER A 1 95  ? 30.66000 53.26700 16.47700  0.330 77.74000  ?  95  SER A C   1 
ATOM   1318 O  O   A SER A 1 95  ? 30.90700 52.21800 17.00100  0.670 78.96000  ?  95  SER A O   1 
ATOM   1319 O  O   B SER A 1 95  ? 30.96000 52.08300 16.66100  0.330 76.39000  ?  95  SER A O   1 
ATOM   1320 C  CB  A SER A 1 95  ? 32.77800 54.62100 17.12800  0.670 83.12000  ?  95  SER A CB  1 
ATOM   1321 C  CB  B SER A 1 95  ? 32.87000 54.49200 16.39600  0.330 82.46000  ?  95  SER A CB  1 
ATOM   1322 O  OG  A SER A 1 95  ? 32.29100 54.54100 18.46100  0.670 102.94000 ?  95  SER A OG  1 
ATOM   1323 O  OG  B SER A 1 95  ? 32.71800 54.36300 17.79300  0.330 91.33000  ?  95  SER A OG  1 
ATOM   1324 N  N   A ARG A 1 96  ? 29.46400 53.93800 17.12700  0.670 78.17000  ?  96  ARG A N   1 
ATOM   1325 N  N   B ARG A 1 96  ? 29.50500 53.79200 16.90300  0.330 77.57000  ?  96  ARG A N   1 
ATOM   1326 C  CA  A ARG A 1 96  ? 28.44300 53.13400 17.78900  0.670 79.59000  ?  96  ARG A CA  1 
ATOM   1327 C  CA  B ARG A 1 96  ? 28.47900 53.01200 17.57700  0.330 78.98000  ?  96  ARG A CA  1 
ATOM   1328 C  C   A ARG A 1 96  ? 27.61400 52.35200 16.77900  0.670 71.87000  ?  96  ARG A C   1 
ATOM   1329 C  C   B ARG A 1 96  ? 27.51500 52.35500 16.61000  0.330 72.82000  ?  96  ARG A C   1 
ATOM   1330 O  O   A ARG A 1 96  ? 27.29500 51.18000 17.00600  0.670 66.82000  ?  96  ARG A O   1 
ATOM   1331 O  O   B ARG A 1 96  ? 27.10900 51.21800 16.86300  0.330 67.87000  ?  96  ARG A O   1 
ATOM   1332 C  CB  A ARG A 1 96  ? 27.54800 54.03700 18.63700  0.670 95.13000  ?  96  ARG A CB  1 
ATOM   1333 C  CB  B ARG A 1 96  ? 27.69900 53.89100 18.56600  0.330 93.88000  ?  96  ARG A CB  1 
ATOM   1334 C  CG  A ARG A 1 96  ? 26.32900 53.35400 19.23100  0.670 97.83000  ?  96  ARG A CG  1 
ATOM   1335 C  CG  B ARG A 1 96  ? 26.53700 53.17800 19.29200  0.330 97.29000  ?  96  ARG A CG  1 
ATOM   1336 C  CD  A ARG A 1 96  ? 25.40300 54.38400 19.88100  0.670 115.39000 ?  96  ARG A CD  1 
ATOM   1337 C  CD  B ARG A 1 96  ? 25.75400 54.09100 20.26500  0.330 110.83000 ?  96  ARG A CD  1 
ATOM   1338 N  NE  A ARG A 1 96  ? 26.13200 55.33800 20.71700  0.670 119.69000 ?  96  ARG A NE  1 
ATOM   1339 N  NE  B ARG A 1 96  ? 26.57700 54.88600 21.18200  0.330 115.97000 ?  96  ARG A NE  1 
ATOM   1340 C  CZ  A ARG A 1 96  ? 26.49300 56.55900 20.33100  0.670 126.90000 ?  96  ARG A CZ  1 
ATOM   1341 C  CZ  B ARG A 1 96  ? 26.86800 56.17000 20.99900  0.330 123.39000 ?  96  ARG A CZ  1 
ATOM   1342 N  NH1 A ARG A 1 96  ? 26.19700 56.99700 19.11400  0.670 127.07000 ?  96  ARG A NH1 1 
ATOM   1343 N  NH1 B ARG A 1 96  ? 26.46100 56.82400 19.92000  0.330 126.64000 ?  96  ARG A NH1 1 
ATOM   1344 N  NH2 A ARG A 1 96  ? 27.15300 57.34700 21.16800  0.670 129.06000 ?  96  ARG A NH2 1 
ATOM   1345 N  NH2 B ARG A 1 96  ? 27.58600 56.81700 21.91600  0.330 127.58000 ?  96  ARG A NH2 1 
ATOM   1346 N  N   A GLU A 1 97  ? 27.24600 52.98900 15.66500  0.670 81.94000  ?  97  GLU A N   1 
ATOM   1347 N  N   B GLU A 1 97  ? 27.12300 53.04200 15.51300  0.330 80.39000  ?  97  GLU A N   1 
ATOM   1348 C  CA  A GLU A 1 97  ? 26.50900 52.28300 14.62200  0.670 70.27000  ?  97  GLU A CA  1 
ATOM   1349 C  CA  B GLU A 1 97  ? 26.17700 52.43900 14.56600  0.330 68.16000  ?  97  GLU A CA  1 
ATOM   1350 C  C   A GLU A 1 97  ? 27.33800 51.14300 14.04400  0.670 58.51000  ?  97  GLU A C   1 
ATOM   1351 C  C   B GLU A 1 97  ? 26.82900 51.29700 13.78900  0.330 58.87000  ?  97  GLU A C   1 
ATOM   1352 O  O   A GLU A 1 97  ? 26.80000 50.07900 13.71000  0.670 54.46000  ?  97  GLU A O   1 
ATOM   1353 O  O   B GLU A 1 97  ? 26.13000 50.39500 13.31300  0.330 55.45000  ?  97  GLU A O   1 
ATOM   1354 C  CB  A GLU A 1 97  ? 26.10100 53.25800 13.51800  0.670 67.84000  ?  97  GLU A CB  1 
ATOM   1355 C  CB  B GLU A 1 97  ? 25.61700 53.48300 13.61000  0.330 68.08000  ?  97  GLU A CB  1 
ATOM   1356 N  N   A PHE A 1 98  ? 28.65200 51.34800 13.91900  0.670 61.19000  ?  98  PHE A N   1 
ATOM   1357 N  N   B PHE A 1 98  ? 28.16500 51.30100 13.69400  0.330 59.48000  ?  98  PHE A N   1 
ATOM   1358 C  CA  A PHE A 1 98  ? 29.54300 50.27100 13.50100  0.670 52.24000  ?  98  PHE A CA  1 
ATOM   1359 C  CA  B PHE A 1 98  ? 28.90600 50.16100 13.16500  0.330 53.15000  ?  98  PHE A CA  1 
ATOM   1360 C  C   A PHE A 1 98  ? 29.32500 49.02600 14.35600  0.670 52.45000  ?  98  PHE A C   1 
ATOM   1361 C  C   B PHE A 1 98  ? 28.62600 48.91900 13.96300  0.330 48.24000  ?  98  PHE A C   1 
ATOM   1362 O  O   A PHE A 1 98  ? 29.25400 47.90300 13.84500  0.670 46.54000  ?  98  PHE A O   1 
ATOM   1363 O  O   B PHE A 1 98  ? 28.40900 47.84000 13.40500  0.330 40.53000  ?  98  PHE A O   1 
ATOM   1364 C  CB  A PHE A 1 98  ? 31.00000 50.73100 13.60800  0.670 68.21000  ?  98  PHE A CB  1 
ATOM   1365 C  CB  B PHE A 1 98  ? 30.40100 50.44500 13.21700  0.330 59.73000  ?  98  PHE A CB  1 
ATOM   1366 C  CG  A PHE A 1 98  ? 31.52200 51.42200 12.37900  0.670 61.15000  ?  98  PHE A CG  1 
ATOM   1367 C  CG  B PHE A 1 98  ? 30.89800 51.23000 12.06700  0.330 62.61000  ?  98  PHE A CG  1 
ATOM   1368 C  CD1 A PHE A 1 98  ? 31.68100 50.73200 11.19000  0.670 70.78000  ?  98  PHE A CD1 1 
ATOM   1369 C  CD1 B PHE A 1 98  ? 30.99200 50.66900 10.81600  0.330 66.91000  ?  98  PHE A CD1 1 
ATOM   1370 C  CD2 A PHE A 1 98  ? 31.86800 52.76300 12.42100  0.670 71.53000  ?  98  PHE A CD2 1 
ATOM   1371 C  CD2 B PHE A 1 98  ? 31.26700 52.54700 12.23900  0.330 68.84000  ?  98  PHE A CD2 1 
ATOM   1372 C  CE1 A PHE A 1 98  ? 32.16600 51.36900 10.06300  0.670 62.06000  ?  98  PHE A CE1 1 
ATOM   1373 C  CE1 B PHE A 1 98  ? 31.43700 51.41000 9.75200   0.330 60.71000  ?  98  PHE A CE1 1 
ATOM   1374 C  CE2 A PHE A 1 98  ? 32.35200 53.40600 11.30000  0.670 72.00000  ?  98  PHE A CE2 1 
ATOM   1375 C  CE2 B PHE A 1 98  ? 31.71300 53.29000 11.18300  0.330 68.26000  ?  98  PHE A CE2 1 
ATOM   1376 C  CZ  A PHE A 1 98  ? 32.50100 52.70700 10.11700  0.670 64.43000  ?  98  PHE A CZ  1 
ATOM   1377 C  CZ  B PHE A 1 98  ? 31.80000 52.72600 9.93700   0.330 62.78000  ?  98  PHE A CZ  1 
ATOM   1378 N  N   A GLY A 1 99  ? 29.22100 49.21300 15.67200  0.670 63.20000  ?  99  GLY A N   1 
ATOM   1379 N  N   B GLY A 1 99  ? 28.64800 49.06000 15.29000  0.330 58.00000  ?  99  GLY A N   1 
ATOM   1380 C  CA  A GLY A 1 99  ? 29.11000 48.06900 16.56400  0.670 37.18000  ?  99  GLY A CA  1 
ATOM   1381 C  CA  B GLY A 1 99  ? 28.76500 47.90200 16.17000  0.330 43.65000  ?  99  GLY A CA  1 
ATOM   1382 C  C   A GLY A 1 99  ? 27.88900 47.21700 16.28100  0.670 42.73000  ?  99  GLY A C   1 
ATOM   1383 C  C   B GLY A 1 99  ? 27.46300 47.12100 16.27100  0.330 43.90000  ?  99  GLY A C   1 
ATOM   1384 O  O   A GLY A 1 99  ? 27.96100 45.98500 16.29600  0.670 41.99000  ?  99  GLY A O   1 
ATOM   1385 O  O   B GLY A 1 99  ? 27.44000 45.94300 16.64400  0.330 42.79000  ?  99  GLY A O   1 
ATOM   1386 N  N   A ILE A 1 100 ? 26.75300 47.86100 16.01600  0.670 41.98000  ?  100 ILE A N   1 
ATOM   1387 N  N   B ILE A 1 100 ? 26.35200 47.78600 16.01000  0.330 45.18000  ?  100 ILE A N   1 
ATOM   1388 C  CA  A ILE A 1 100 ? 25.52600 47.11900 15.74900  0.670 39.92000  ?  100 ILE A CA  1 
ATOM   1389 C  CA  B ILE A 1 100 ? 25.15700 47.08200 15.59500  0.330 46.05000  ?  100 ILE A CA  1 
ATOM   1390 C  C   A ILE A 1 100 ? 25.68900 46.25100 14.50700  0.670 52.11000  ?  100 ILE A C   1 
ATOM   1391 C  C   B ILE A 1 100 ? 25.51800 46.18800 14.42100  0.330 51.18000  ?  100 ILE A C   1 
ATOM   1392 O  O   A ILE A 1 100 ? 25.45900 45.03700 14.54400  0.670 50.43000  ?  100 ILE A O   1 
ATOM   1393 O  O   B ILE A 1 100 ? 25.56100 44.95000 14.54600  0.330 50.30000  ?  100 ILE A O   1 
ATOM   1394 C  CB  A ILE A 1 100 ? 24.33400 48.08300 15.60700  0.670 60.23000  ?  100 ILE A CB  1 
ATOM   1395 C  CB  B ILE A 1 100 ? 24.07700 48.11700 15.24200  0.330 57.95000  ?  100 ILE A CB  1 
ATOM   1396 C  CG1 A ILE A 1 100 ? 24.03600 48.77100 16.94100  0.670 72.27000  ?  100 ILE A CG1 1 
ATOM   1397 C  CG1 B ILE A 1 100 ? 23.89800 49.01700 16.49800  0.330 68.26000  ?  100 ILE A CG1 1 
ATOM   1398 C  CG2 A ILE A 1 100 ? 23.10800 47.33500 15.10100  0.670 51.27000  ?  100 ILE A CG2 1 
ATOM   1399 C  CG2 B ILE A 1 100 ? 22.75500 47.47100 14.84700  0.330 50.45000  ?  100 ILE A CG2 1 
ATOM   1400 C  CD1 A ILE A 1 100 ? 23.79700 50.26600 16.82300  0.670 70.26000  ?  100 ILE A CD1 1 
ATOM   1401 C  CD1 B ILE A 1 100 ? 24.07400 50.49800 16.30200  0.330 64.47000  ?  100 ILE A CD1 1 
ATOM   1402 N  N   A VAL A 1 101 ? 26.08700 46.85600 13.38500  0.670 44.90000  ?  101 VAL A N   1 
ATOM   1403 N  N   B VAL A 1 101 ? 25.92200 46.81200 13.30100  0.330 44.82000  ?  101 VAL A N   1 
ATOM   1404 C  CA  A VAL A 1 101 ? 26.09800 46.10900 12.12900  0.670 41.98000  ?  101 VAL A CA  1 
ATOM   1405 C  CA  B VAL A 1 101 ? 25.89000 46.03600 12.07800  0.330 42.55000  ?  101 VAL A CA  1 
ATOM   1406 C  C   A VAL A 1 101 ? 27.17000 45.02700 12.15600  0.670 32.35000  ?  101 VAL A C   1 
ATOM   1407 C  C   B VAL A 1 101 ? 27.06800 45.06700 11.97000  0.330 34.92000  ?  101 VAL A C   1 
ATOM   1408 O  O   A VAL A 1 101 ? 26.95700 43.91500 11.65900  0.670 39.54000  ?  101 VAL A O   1 
ATOM   1409 O  O   B VAL A 1 101 ? 26.91800 44.03000 11.31300  0.330 39.42000  ?  101 VAL A O   1 
ATOM   1410 C  CB  A VAL A 1 101 ? 26.27700 47.05500 10.92500  0.670 46.55000  ?  101 VAL A CB  1 
ATOM   1411 C  CB  B VAL A 1 101 ? 25.71400 46.94900 10.84100  0.330 44.87000  ?  101 VAL A CB  1 
ATOM   1412 C  CG1 A VAL A 1 101 ? 25.12100 48.04700 10.86000  0.670 51.57000  ?  101 VAL A CG1 1 
ATOM   1413 C  CG1 B VAL A 1 101 ? 24.50300 47.89700 11.05800  0.330 48.08000  ?  101 VAL A CG1 1 
ATOM   1414 C  CG2 A VAL A 1 101 ? 27.61500 47.77100 10.96900  0.670 47.17000  ?  101 VAL A CG2 1 
ATOM   1415 C  CG2 B VAL A 1 101 ? 26.98700 47.66900 10.43300  0.330 36.56000  ?  101 VAL A CG2 1 
ATOM   1416 N  N   A ILE A 1 102 ? 28.33500 45.32300 12.73800  0.670 35.49000  ?  102 ILE A N   1 
ATOM   1417 N  N   B ILE A 1 102 ? 28.21400 45.28600 12.63500  0.330 36.16000  ?  102 ILE A N   1 
ATOM   1418 C  CA  A ILE A 1 102 ? 29.37700 44.30500 12.81000  0.670 39.43000  ?  102 ILE A CA  1 
ATOM   1419 C  CA  B ILE A 1 102 ? 29.21800 44.18400 12.55300  0.330 39.25000  ?  102 ILE A CA  1 
ATOM   1420 C  C   A ILE A 1 102 ? 28.95900 43.18400 13.75400  0.670 39.18000  ?  102 ILE A C   1 
ATOM   1421 C  C   B ILE A 1 102 ? 28.87500 42.95100 13.41900  0.330 39.90000  ?  102 ILE A C   1 
ATOM   1422 O  O   A ILE A 1 102 ? 29.30200 42.01700 13.52900  0.670 40.03000  ?  102 ILE A O   1 
ATOM   1423 O  O   B ILE A 1 102 ? 29.23800 41.82500 13.05400  0.330 39.33000  ?  102 ILE A O   1 
ATOM   1424 C  CB  A ILE A 1 102 ? 30.71900 44.94100 13.22000  0.670 37.57000  ?  102 ILE A CB  1 
ATOM   1425 C  CB  B ILE A 1 102 ? 30.66900 44.63600 12.82400  0.330 38.61000  ?  102 ILE A CB  1 
ATOM   1426 C  CG1 A ILE A 1 102 ? 31.36000 45.62900 12.01000  0.670 45.83000  ?  102 ILE A CG1 1 
ATOM   1427 C  CG1 B ILE A 1 102 ? 31.29800 45.06300 11.49900  0.330 39.04000  ?  102 ILE A CG1 1 
ATOM   1428 C  CG2 A ILE A 1 102 ? 31.66400 43.89300 13.78400  0.670 31.17000  ?  102 ILE A CG2 1 
ATOM   1429 C  CG2 B ILE A 1 102 ? 31.53900 43.51400 13.44900  0.330 31.09000  ?  102 ILE A CG2 1 
ATOM   1430 C  CD1 A ILE A 1 102 ? 32.12300 46.89000 12.32800  0.670 52.77000  ?  102 ILE A CD1 1 
ATOM   1431 C  CD1 B ILE A 1 102 ? 32.29100 46.24900 11.54200  0.330 44.62000  ?  102 ILE A CD1 1 
ATOM   1432 N  N   A THR A 1 103 ? 28.20500 43.50100 14.81100  0.670 44.91000  ?  103 THR A N   1 
ATOM   1433 N  N   B THR A 1 103 ? 28.13700 43.11100 14.51800  0.330 42.60000  ?  103 THR A N   1 
ATOM   1434 C  CA  A THR A 1 103 ? 27.68500 42.44800 15.67900  0.670 41.14000  ?  103 THR A CA  1 
ATOM   1435 C  CA  B THR A 1 103 ? 27.66100 41.98900 15.33200  0.330 35.68000  ?  103 THR A CA  1 
ATOM   1436 C  C   A THR A 1 103 ? 26.68300 41.57700 14.93000  0.670 35.65000  ?  103 THR A C   1 
ATOM   1437 C  C   B THR A 1 103 ? 26.39000 41.36700 14.72900  0.330 36.14000  ?  103 THR A C   1 
ATOM   1438 O  O   A THR A 1 103 ? 26.77000 40.34300 14.96100  0.670 35.58000  ?  103 THR A O   1 
ATOM   1439 O  O   B THR A 1 103 ? 26.16700 40.14100 14.81600  0.330 33.20000  ?  103 THR A O   1 
ATOM   1440 C  CB  A THR A 1 103 ? 27.03900 43.05600 16.92600  0.670 41.82000  ?  103 THR A CB  1 
ATOM   1441 C  CB  B THR A 1 103 ? 27.38000 42.51100 16.75700  0.330 41.48000  ?  103 THR A CB  1 
ATOM   1442 O  OG1 A THR A 1 103 ? 28.04400 43.66900 17.74300  0.670 36.00000  ?  103 THR A OG1 1 
ATOM   1443 O  OG1 B THR A 1 103 ? 28.55900 43.15500 17.31600  0.330 40.28000  ?  103 THR A OG1 1 
ATOM   1444 C  CG2 A THR A 1 103 ? 26.31800 41.98100 17.73600  0.670 28.59000  ?  103 THR A CG2 1 
ATOM   1445 C  CG2 B THR A 1 103 ? 26.96000 41.37300 17.67800  0.330 30.59000  ?  103 THR A CG2 1 
ATOM   1446 N  N   A LEU A 1 104 ? 25.72500 42.20600 14.24000  0.670 32.23000  ?  104 LEU A N   1 
ATOM   1447 N  N   B LEU A 1 104 ? 25.52500 42.20000 14.13700  0.330 34.02000  ?  104 LEU A N   1 
ATOM   1448 C  CA  A LEU A 1 104 ? 24.76400 41.45000 13.44000  0.670 37.43000  ?  104 LEU A CA  1 
ATOM   1449 C  CA  B LEU A 1 104 ? 24.61400 41.68500 13.10700  0.330 38.16000  ?  104 LEU A CA  1 
ATOM   1450 C  C   A LEU A 1 104 ? 25.46700 40.58400 12.40200  0.670 37.48000  ?  104 LEU A C   1 
ATOM   1451 C  C   B LEU A 1 104 ? 25.31100 40.81100 12.05100  0.330 36.22000  ?  104 LEU A C   1 
ATOM   1452 O  O   A LEU A 1 104 ? 25.09500 39.42300 12.19400  0.670 32.01000  ?  104 LEU A O   1 
ATOM   1453 O  O   B LEU A 1 104 ? 24.94800 39.63300 11.88800  0.330 33.34000  ?  104 LEU A O   1 
ATOM   1454 C  CB  A LEU A 1 104 ? 23.78900 42.40200 12.74500  0.670 37.61000  ?  104 LEU A CB  1 
ATOM   1455 C  CB  B LEU A 1 104 ? 23.82500 42.81800 12.44400  0.330 37.68000  ?  104 LEU A CB  1 
ATOM   1456 C  CG  A LEU A 1 104 ? 22.61900 42.97900 13.53800  0.670 38.05000  ?  104 LEU A CG  1 
ATOM   1457 C  CG  B LEU A 1 104 ? 22.47700 42.71300 13.06300  0.330 37.95000  ?  104 LEU A CG  1 
ATOM   1458 C  CD1 A LEU A 1 104 ? 21.79200 43.92400 12.66200  0.670 44.43000  ?  104 LEU A CD1 1 
ATOM   1459 C  CD1 B LEU A 1 104 ? 21.41700 43.34100 12.14500  0.330 36.78000  ?  104 LEU A CD1 1 
ATOM   1460 C  CD2 A LEU A 1 104 ? 21.73700 41.87700 14.09200  0.670 34.83000  ?  104 LEU A CD2 1 
ATOM   1461 C  CD2 B LEU A 1 104 ? 22.21200 41.23400 13.36400  0.330 32.12000  ?  104 LEU A CD2 1 
ATOM   1462 N  N   A ASN A 1 105 ? 26.48200 41.13300 11.73200  0.670 32.90000  ?  105 ASN A N   1 
ATOM   1463 N  N   B ASN A 1 105 ? 26.27200 41.38100 11.28900  0.330 36.20000  ?  105 ASN A N   1 
ATOM   1464 C  CA  A ASN A 1 105 ? 27.20800 40.35400 10.73500  0.670 39.60000  ?  105 ASN A CA  1 
ATOM   1465 C  CA  B ASN A 1 105 ? 27.06800 40.55200 10.38200  0.330 39.91000  ?  105 ASN A CA  1 
ATOM   1466 C  C   A ASN A 1 105 ? 27.84100 39.11700 11.36100  0.670 37.98000  ?  105 ASN A C   1 
ATOM   1467 C  C   B ASN A 1 105 ? 27.52800 39.30700 11.10100  0.330 37.55000  ?  105 ASN A C   1 
ATOM   1468 O  O   A ASN A 1 105 ? 27.75300 38.01300 10.81000  0.670 39.43000  ?  105 ASN A O   1 
ATOM   1469 O  O   B ASN A 1 105 ? 27.27100 38.19500 10.65200  0.330 38.35000  ?  105 ASN A O   1 
ATOM   1470 C  CB  A ASN A 1 105 ? 28.27700 41.21900 10.06500  0.670 42.87000  ?  105 ASN A CB  1 
ATOM   1471 C  CB  B ASN A 1 105 ? 28.31100 41.30000 9.88100   0.330 42.15000  ?  105 ASN A CB  1 
ATOM   1472 C  CG  A ASN A 1 105 ? 28.93000 40.52500 8.88900   0.670 46.43000  ?  105 ASN A CG  1 
ATOM   1473 C  CG  B ASN A 1 105 ? 29.26600 40.42600 8.93200   0.330 44.99000  ?  105 ASN A CG  1 
ATOM   1474 O  OD1 A ASN A 1 105 ? 28.44000 40.59800 7.76200   0.670 39.41000  ?  105 ASN A OD1 1 
ATOM   1475 O  OD1 B ASN A 1 105 ? 29.29100 40.60800 7.72600   0.330 38.11000  ?  105 ASN A OD1 1 
ATOM   1476 N  ND2 A ASN A 1 105 ? 30.04000 39.84000 9.14600   0.670 46.13000  ?  105 ASN A ND2 1 
ATOM   1477 N  ND2 B ASN A 1 105 ? 30.03400 39.47700 9.52600   0.330 45.39000  ?  105 ASN A ND2 1 
ATOM   1478 N  N   A THR A 1 106 ? 28.47700 39.27800 12.52400  0.670 40.48000  ?  106 THR A N   1 
ATOM   1479 N  N   B THR A 1 106 ? 28.14000 39.47800 12.28100  0.330 39.68000  ?  106 THR A N   1 
ATOM   1480 C  CA  A THR A 1 106 ? 29.16800 38.14900 13.14200  0.670 35.39000  ?  106 THR A CA  1 
ATOM   1481 C  CA  B THR A 1 106 ? 28.86200 38.37100 12.89800  0.330 36.07000  ?  106 THR A CA  1 
ATOM   1482 C  C   A THR A 1 106 ? 28.18800 37.04500 13.52700  0.670 30.28000  ?  106 THR A C   1 
ATOM   1483 C  C   B THR A 1 106 ? 27.91400 37.26900 13.35200  0.330 32.06000  ?  106 THR A C   1 
ATOM   1484 O  O   A THR A 1 106 ? 28.51800 35.85400 13.45700  0.670 25.38000  ?  106 THR A O   1 
ATOM   1485 O  O   B THR A 1 106 ? 28.21100 36.08900 13.17100  0.330 28.04000  ?  106 THR A O   1 
ATOM   1486 C  CB  A THR A 1 106 ? 29.95900 38.61700 14.36400  0.670 36.20000  ?  106 THR A CB  1 
ATOM   1487 C  CB  B THR A 1 106 ? 29.68500 38.88600 14.05100  0.330 35.80000  ?  106 THR A CB  1 
ATOM   1488 O  OG1 A THR A 1 106 ? 30.91900 39.60300 13.96400  0.670 37.47000  ?  106 THR A OG1 1 
ATOM   1489 O  OG1 B THR A 1 106 ? 30.26900 40.11900 13.64200  0.330 36.22000  ?  106 THR A OG1 1 
ATOM   1490 C  CG2 A THR A 1 106 ? 30.67800 37.44200 15.01700  0.670 26.02000  ?  106 THR A CG2 1 
ATOM   1491 C  CG2 B THR A 1 106 ? 30.81200 37.92900 14.30000  0.330 33.24000  ?  106 THR A CG2 1 
ATOM   1492 N  N   A VAL A 1 107 ? 26.97200 37.41800 13.93200  0.670 33.86000  ?  107 VAL A N   1 
ATOM   1493 N  N   B VAL A 1 107 ? 26.75400 37.61900 13.92100  0.330 34.11000  ?  107 VAL A N   1 
ATOM   1494 C  CA  A VAL A 1 107 ? 25.97300 36.40900 14.27500  0.670 26.21000  ?  107 VAL A CA  1 
ATOM   1495 C  CA  B VAL A 1 107 ? 25.77300 36.57600 14.21100  0.330 28.03000  ?  107 VAL A CA  1 
ATOM   1496 C  C   A VAL A 1 107 ? 25.63200 35.56700 13.05300  0.670 33.32000  ?  107 VAL A C   1 
ATOM   1497 C  C   B VAL A 1 107 ? 25.45800 35.75600 12.95400  0.330 33.82000  ?  107 VAL A C   1 
ATOM   1498 O  O   A VAL A 1 107 ? 25.48600 34.34200 13.14400  0.670 29.20000  ?  107 VAL A O   1 
ATOM   1499 O  O   B VAL A 1 107 ? 25.33500 34.52600 13.03400  0.330 29.15000  ?  107 VAL A O   1 
ATOM   1500 C  CB  A VAL A 1 107 ? 24.71400 37.07300 14.86800  0.670 33.23000  ?  107 VAL A CB  1 
ATOM   1501 C  CB  B VAL A 1 107 ? 24.48100 37.16300 14.79300  0.330 32.87000  ?  107 VAL A CB  1 
ATOM   1502 C  CG1 A VAL A 1 107 ? 23.63200 36.02700 15.11300  0.670 31.34000  ?  107 VAL A CG1 1 
ATOM   1503 C  CG1 B VAL A 1 107 ? 23.38200 36.02900 14.95200  0.330 30.72000  ?  107 VAL A CG1 1 
ATOM   1504 C  CG2 A VAL A 1 107 ? 25.04900 37.82000 16.14000  0.670 37.80000  ?  107 VAL A CG2 1 
ATOM   1505 C  CG2 B VAL A 1 107 ? 24.71800 37.90900 16.15200  0.330 37.34000  ?  107 VAL A CG2 1 
ATOM   1506 N  N   A VAL A 1 108 ? 25.48700 36.21100 11.89300  0.670 33.29000  ?  108 VAL A N   1 
ATOM   1507 N  N   B VAL A 1 108 ? 25.24800 36.42300 11.78000  0.330 31.70000  ?  108 VAL A N   1 
ATOM   1508 C  CA  A VAL A 1 108 ? 25.21100 35.47600 10.66100  0.670 26.03000  ?  108 VAL A CA  1 
ATOM   1509 C  CA  B VAL A 1 108 ? 24.79900 35.66700 10.60400  0.330 25.93000  ?  108 VAL A CA  1 
ATOM   1510 C  C   A VAL A 1 108 ? 26.32100 34.47300 10.39200  0.670 31.57000  ?  108 VAL A C   1 
ATOM   1511 C  C   B VAL A 1 108 ? 25.84100 34.63700 10.22200  0.330 30.62000  ?  108 VAL A C   1 
ATOM   1512 O  O   A VAL A 1 108 ? 26.07500 33.28000 10.16300  0.670 24.23000  ?  108 VAL A O   1 
ATOM   1513 O  O   B VAL A 1 108 ? 25.50500 33.48100 9.92400   0.330 24.63000  ?  108 VAL A O   1 
ATOM   1514 C  CB  A VAL A 1 108 ? 25.05800 36.45300 9.48100   0.670 31.55000  ?  108 VAL A CB  1 
ATOM   1515 C  CB  B VAL A 1 108 ? 24.47700 36.55200 9.38400   0.330 30.85000  ?  108 VAL A CB  1 
ATOM   1516 C  CG1 A VAL A 1 108 ? 24.88000 35.68200 8.18200   0.670 22.18000  ?  108 VAL A CG1 1 
ATOM   1517 C  CG1 B VAL A 1 108 ? 24.03500 35.61600 8.21900   0.330 27.17000  ?  108 VAL A CG1 1 
ATOM   1518 C  CG2 A VAL A 1 108 ? 23.90900 37.41600 9.71600   0.670 27.55000  ?  108 VAL A CG2 1 
ATOM   1519 C  CG2 B VAL A 1 108 ? 23.38400 37.58200 9.64800   0.330 24.19000  ?  108 VAL A CG2 1 
ATOM   1520 N  N   A MET A 1 109 ? 27.56600 34.95100 10.41800  0.670 29.00000  ?  109 MET A N   1 
ATOM   1521 N  N   B MET A 1 109 ? 27.12600 35.03400 10.25100  0.330 30.94000  ?  109 MET A N   1 
ATOM   1522 C  CA  A MET A 1 109 ? 28.71100 34.12200 10.06300  0.670 29.92000  ?  109 MET A CA  1 
ATOM   1523 C  CA  B MET A 1 109 ? 28.20300 34.18300 9.72500   0.330 31.92000  ?  109 MET A CA  1 
ATOM   1524 C  C   A MET A 1 109 ? 28.90900 32.97700 11.05000  0.670 36.81000  ?  109 MET A C   1 
ATOM   1525 C  C   B MET A 1 109 ? 28.50500 33.03500 10.63900  0.330 33.24000  ?  109 MET A C   1 
ATOM   1526 O  O   A MET A 1 109 ? 29.12500 31.83300 10.64500  0.670 40.75000  ?  109 MET A O   1 
ATOM   1527 O  O   B MET A 1 109 ? 28.55500 31.87200 10.21100  0.330 34.25000  ?  109 MET A O   1 
ATOM   1528 C  CB  A MET A 1 109 ? 29.96200 34.99200 10.02200  0.670 25.38000  ?  109 MET A CB  1 
ATOM   1529 C  CB  B MET A 1 109 ? 29.46600 34.99100 9.53000   0.330 30.22000  ?  109 MET A CB  1 
ATOM   1530 C  CG  A MET A 1 109 ? 29.95100 36.01300 8.90500   0.670 37.40000  ?  109 MET A CG  1 
ATOM   1531 C  CG  B MET A 1 109 ? 29.25400 36.03600 8.47400   0.330 38.34000  ?  109 MET A CG  1 
ATOM   1532 S  SD  A MET A 1 109 ? 29.72500 35.17500 7.32300   0.670 53.63000  ?  109 MET A SD  1 
ATOM   1533 S  SD  B MET A 1 109 ? 28.43100 35.26700 7.07400   0.330 28.13000  ?  109 MET A SD  1 
ATOM   1534 C  CE  A MET A 1 109 ? 28.38000 36.06300 6.56500   0.670 22.62000  ?  109 MET A CE  1 
ATOM   1535 C  CE  B MET A 1 109 ? 27.27800 36.50300 6.73300   0.330 31.20000  ?  109 MET A CE  1 
ATOM   1536 N  N   A LEU A 1 110 ? 28.81900 33.25700 12.34900  0.670 39.12000  ?  110 LEU A N   1 
ATOM   1537 N  N   B LEU A 1 110 ? 28.82200 33.37900 11.89000  0.330 37.34000  ?  110 LEU A N   1 
ATOM   1538 C  CA  A LEU A 1 110 ? 28.99800 32.20600 13.34400  0.670 33.77000  ?  110 LEU A CA  1 
ATOM   1539 C  CA  B LEU A 1 110 ? 28.83200 32.53000 13.08100  0.330 35.36000  ?  110 LEU A CA  1 
ATOM   1540 C  C   A LEU A 1 110 ? 27.89400 31.16200 13.24700  0.670 31.70000  ?  110 LEU A C   1 
ATOM   1541 C  C   B LEU A 1 110 ? 27.76800 31.42600 13.10400  0.330 32.12000  ?  110 LEU A C   1 
ATOM   1542 O  O   A LEU A 1 110 ? 28.16200 29.95900 13.32900  0.670 30.49000  ?  110 LEU A O   1 
ATOM   1543 O  O   B LEU A 1 110 ? 28.06900 30.28400 13.48700  0.330 30.77000  ?  110 LEU A O   1 
ATOM   1544 C  CB  A LEU A 1 110 ? 29.03500 32.83000 14.73700  0.670 31.53000  ?  110 LEU A CB  1 
ATOM   1545 C  CB  B LEU A 1 110 ? 28.66800 33.44300 14.29400  0.330 28.17000  ?  110 LEU A CB  1 
ATOM   1546 C  CG  A LEU A 1 110 ? 30.29500 33.64000 15.05000  0.670 39.94000  ?  110 LEU A CG  1 
ATOM   1547 C  CG  B LEU A 1 110 ? 29.95300 34.24000 14.44300  0.330 33.89000  ?  110 LEU A CG  1 
ATOM   1548 C  CD1 A LEU A 1 110 ? 30.26100 34.13300 16.48900  0.670 27.23000  ?  110 LEU A CD1 1 
ATOM   1549 C  CD1 B LEU A 1 110 ? 30.02700 35.00700 15.73600  0.330 27.38000  ?  110 LEU A CD1 1 
ATOM   1550 C  CD2 A LEU A 1 110 ? 31.55900 32.83600 14.79200  0.670 31.18000  ?  110 LEU A CD2 1 
ATOM   1551 C  CD2 B LEU A 1 110 ? 31.16400 33.31900 14.25200  0.330 34.80000  ?  110 LEU A CD2 1 
ATOM   1552 N  N   A ALA A 1 111 ? 26.64500 31.60200 13.06700  0.670 26.47000  ?  111 ALA A N   1 
ATOM   1553 N  N   B ALA A 1 111 ? 26.53900 31.77100 12.67300  0.330 28.52000  ?  111 ALA A N   1 
ATOM   1554 C  CA  A ALA A 1 111 ? 25.54500 30.65000 12.95300  0.670 32.22000  ?  111 ALA A CA  1 
ATOM   1555 C  CA  B ALA A 1 111 ? 25.38100 30.86800 12.62400  0.330 33.02000  ?  111 ALA A CA  1 
ATOM   1556 C  C   A ALA A 1 111 ? 25.74000 29.72700 11.75800  0.670 28.99000  ?  111 ALA A C   1 
ATOM   1557 C  C   B ALA A 1 111 ? 25.43900 29.88400 11.46900  0.330 29.58000  ?  111 ALA A C   1 
ATOM   1558 O  O   A ALA A 1 111 ? 25.49200 28.51900 11.85300  0.670 42.45000  ?  111 ALA A O   1 
ATOM   1559 O  O   B ALA A 1 111 ? 24.83900 28.81000 11.54900  0.330 36.20000  ?  111 ALA A O   1 
ATOM   1560 C  CB  A ALA A 1 111 ? 24.21200 31.38800 12.84200  0.670 35.18000  ?  111 ALA A CB  1 
ATOM   1561 C  CB  B ALA A 1 111 ? 24.08800 31.67900 12.46600  0.330 32.74000  ?  111 ALA A CB  1 
ATOM   1562 N  N   A GLY A 1 112 ? 26.17000 30.27400 10.62200  0.670 29.10000  ?  112 GLY A N   1 
ATOM   1563 N  N   B GLY A 1 112 ? 26.04100 30.27400 10.33800  0.330 31.23000  ?  112 GLY A N   1 
ATOM   1564 C  CA  A GLY A 1 112 ? 26.43200 29.42800 9.47000   0.670 33.02000  ?  112 GLY A CA  1 
ATOM   1565 C  CA  B GLY A 1 112 ? 26.02800 29.37900 9.18500   0.330 31.90000  ?  112 GLY A CA  1 
ATOM   1566 C  C   A GLY A 1 112 ? 27.54500 28.43400 9.73200   0.670 27.58000  ?  112 GLY A C   1 
ATOM   1567 C  C   B GLY A 1 112 ? 26.88600 28.17500 9.47600   0.330 31.76000  ?  112 GLY A C   1 
ATOM   1568 O  O   A GLY A 1 112 ? 27.43200 27.25300 9.39300   0.670 25.89000  ?  112 GLY A O   1 
ATOM   1569 O  O   B GLY A 1 112 ? 26.42200 27.04500 9.48800   0.330 41.63000  ?  112 GLY A O   1 
ATOM   1570 N  N   A PHE A 1 113 ? 28.63200 28.89900 10.34900  0.670 27.36000  ?  113 PHE A N   1 
ATOM   1571 N  N   B PHE A 1 113 ? 28.12900 28.43200 9.78700   0.330 28.87000  ?  113 PHE A N   1 
ATOM   1572 C  CA  A PHE A 1 113 ? 29.75000 28.02000 10.66800  0.670 41.03000  ?  113 PHE A CA  1 
ATOM   1573 C  CA  B PHE A 1 113 ? 29.12900 27.50900 10.27300  0.330 36.98000  ?  113 PHE A CA  1 
ATOM   1574 C  C   A PHE A 1 113 ? 29.32100 26.90200 11.60400  0.670 35.04000  ?  113 PHE A C   1 
ATOM   1575 C  C   B PHE A 1 113 ? 28.49200 26.35700 11.05800  0.330 39.53000  ?  113 PHE A C   1 
ATOM   1576 O  O   A PHE A 1 113 ? 29.70000 25.74200 11.41000  0.670 39.92000  ?  113 PHE A O   1 
ATOM   1577 O  O   B PHE A 1 113 ? 28.27400 25.26400 10.50200  0.330 34.89000  ?  113 PHE A O   1 
ATOM   1578 C  CB  A PHE A 1 113 ? 30.87600 28.84400 11.29000  0.670 41.10000  ?  113 PHE A CB  1 
ATOM   1579 C  CB  B PHE A 1 113 ? 30.09900 28.37100 11.11400  0.330 39.97000  ?  113 PHE A CB  1 
ATOM   1580 C  CG  A PHE A 1 113 ? 32.18000 28.10900 11.42700  0.670 39.67000  ?  113 PHE A CG  1 
ATOM   1581 C  CG  B PHE A 1 113 ? 31.49900 27.86800 11.20200  0.330 39.49000  ?  113 PHE A CG  1 
ATOM   1582 C  CD1 A PHE A 1 113 ? 32.41900 26.93700 10.73000  0.670 40.57000  ?  113 PHE A CD1 1 
ATOM   1583 C  CD1 B PHE A 1 113 ? 31.93700 26.84300 10.37000  0.330 40.87000  ?  113 PHE A CD1 1 
ATOM   1584 C  CD2 A PHE A 1 113 ? 33.17600 28.60400 12.25400  0.670 45.26000  ?  113 PHE A CD2 1 
ATOM   1585 C  CD2 B PHE A 1 113 ? 32.41800 28.52800 12.02800  0.330 39.03000  ?  113 PHE A CD2 1 
ATOM   1586 C  CE1 A PHE A 1 113 ? 33.62400 26.27000 10.85900  0.670 46.57000  ?  113 PHE A CE1 1 
ATOM   1587 C  CE1 B PHE A 1 113 ? 33.25000 26.40100 10.44700  0.330 41.99000  ?  113 PHE A CE1 1 
ATOM   1588 C  CE2 A PHE A 1 113 ? 34.37900 27.94400 12.38600  0.670 49.51000  ?  113 PHE A CE2 1 
ATOM   1589 C  CE2 B PHE A 1 113 ? 33.74500 28.11100 12.11000  0.330 49.52000  ?  113 PHE A CE2 1 
ATOM   1590 C  CZ  A PHE A 1 113 ? 34.60400 26.77500 11.68900  0.670 48.46000  ?  113 PHE A CZ  1 
ATOM   1591 C  CZ  B PHE A 1 113 ? 34.17800 27.05200 11.31400  0.330 46.29000  ?  113 PHE A CZ  1 
ATOM   1592 N  N   A ALA A 1 114 ? 28.52300 27.23000 12.62300  0.670 35.25000  ?  114 ALA A N   1 
ATOM   1593 N  N   B ALA A 1 114 ? 28.10300 26.62900 12.32200  0.330 39.41000  ?  114 ALA A N   1 
ATOM   1594 C  CA  A ALA A 1 114 ? 28.08800 26.21600 13.57600  0.670 31.29000  ?  114 ALA A CA  1 
ATOM   1595 C  CA  B ALA A 1 114 ? 27.61600 25.56200 13.20000  0.330 33.99000  ?  114 ALA A CA  1 
ATOM   1596 C  C   A ALA A 1 114 ? 27.10800 25.24300 12.93600  0.670 33.19000  ?  114 ALA A C   1 
ATOM   1597 C  C   B ALA A 1 114 ? 26.32700 24.94700 12.66400  0.330 36.29000  ?  114 ALA A C   1 
ATOM   1598 O  O   A ALA A 1 114 ? 27.20400 24.02800 13.14800  0.670 35.97000  ?  114 ALA A O   1 
ATOM   1599 O  O   B ALA A 1 114 ? 26.09600 23.75900 12.84200  0.330 40.52000  ?  114 ALA A O   1 
ATOM   1600 C  CB  A ALA A 1 114 ? 27.46100 26.88500 14.79700  0.670 30.98000  ?  114 ALA A CB  1 
ATOM   1601 C  CB  B ALA A 1 114 ? 27.46500 26.10000 14.60900  0.330 33.33000  ?  114 ALA A CB  1 
ATOM   1602 N  N   A GLY A 1 115 ? 26.16400 25.75600 12.14300  0.670 28.53000  ?  115 GLY A N   1 
ATOM   1603 N  N   B GLY A 1 115 ? 25.50800 25.70200 11.95400  0.330 34.21000  ?  115 GLY A N   1 
ATOM   1604 C  CA  A GLY A 1 115 ? 25.21300 24.87900 11.48200  0.670 33.49000  ?  115 GLY A CA  1 
ATOM   1605 C  CA  B GLY A 1 115 ? 24.52600 25.05900 11.09800  0.330 37.70000  ?  115 GLY A CA  1 
ATOM   1606 C  C   A GLY A 1 115 ? 25.88500 23.90800 10.53300  0.670 44.51000  ?  115 GLY A C   1 
ATOM   1607 C  C   B GLY A 1 115 ? 25.13100 23.92700 10.29600  0.330 41.44000  ?  115 GLY A C   1 
ATOM   1608 O  O   A GLY A 1 115 ? 25.50800 22.73700 10.45600  0.670 47.54000  ?  115 GLY A O   1 
ATOM   1609 O  O   B GLY A 1 115 ? 24.74900 22.77800 10.47700  0.330 48.03000  ?  115 GLY A O   1 
ATOM   1610 N  N   A ALA A 1 116 ? 26.88800 24.38100 9.79400   0.670 44.01000  ?  116 ALA A N   1 
ATOM   1611 N  N   B ALA A 1 116 ? 26.12300 24.22800 9.45600   0.330 44.15000  ?  116 ALA A N   1 
ATOM   1612 C  CA  A ALA A 1 116 ? 27.61700 23.49200 8.89900   0.670 46.12000  ?  116 ALA A CA  1 
ATOM   1613 C  CA  B ALA A 1 116 ? 26.80100 23.19800 8.66300   0.330 47.14000  ?  116 ALA A CA  1 
ATOM   1614 C  C   A ALA A 1 116 ? 28.31200 22.37200 9.66300   0.670 58.15000  ?  116 ALA A C   1 
ATOM   1615 C  C   B ALA A 1 116 ? 27.47200 22.12900 9.53700   0.330 51.56000  ?  116 ALA A C   1 
ATOM   1616 O  O   A ALA A 1 116 ? 28.43600 21.25500 9.14900   0.670 46.20000  ?  116 ALA A O   1 
ATOM   1617 O  O   B ALA A 1 116 ? 27.31000 20.91900 9.28600   0.330 42.71000  ?  116 ALA A O   1 
ATOM   1618 C  CB  A ALA A 1 116 ? 28.64100 24.28800 8.08800   0.670 35.15000  ?  116 ALA A CB  1 
ATOM   1619 C  CB  B ALA A 1 116 ? 27.82900 23.86000 7.74300   0.330 41.18000  ?  116 ALA A CB  1 
ATOM   1620 N  N   A MET A 1 117 ? 28.76200 22.64200 10.88800  0.670 39.29000  ?  117 MET A N   1 
ATOM   1621 N  N   B MET A 1 117 ? 28.25700 22.55500 10.56500  0.330 48.06000  ?  117 MET A N   1 
ATOM   1622 C  CA  A MET A 1 117 ? 29.54600 21.68000 11.65200  0.670 49.39000  ?  117 MET A CA  1 
ATOM   1623 C  CA  B MET A 1 117 ? 28.95500 21.55700 11.37700  0.330 49.72000  ?  117 MET A CA  1 
ATOM   1624 C  C   A MET A 1 117 ? 28.69700 20.75400 12.51600  0.670 45.97000  ?  117 MET A C   1 
ATOM   1625 C  C   B MET A 1 117 ? 27.96500 20.69900 12.17500  0.330 49.92000  ?  117 MET A C   1 
ATOM   1626 O  O   A MET A 1 117 ? 29.25600 19.88800 13.19700  0.670 55.85000  ?  117 MET A O   1 
ATOM   1627 O  O   B MET A 1 117 ? 28.36300 19.65000 12.69700  0.330 50.76000  ?  117 MET A O   1 
ATOM   1628 C  CB  A MET A 1 117 ? 30.55300 22.41500 12.54600  0.670 49.89000  ?  117 MET A CB  1 
ATOM   1629 C  CB  B MET A 1 117 ? 29.96700 22.21200 12.32800  0.330 51.40000  ?  117 MET A CB  1 
ATOM   1630 C  CG  A MET A 1 117 ? 31.67800 23.10700 11.79600  0.670 51.92000  ?  117 MET A CG  1 
ATOM   1631 C  CG  B MET A 1 117 ? 31.16300 22.91900 11.67000  0.330 53.56000  ?  117 MET A CG  1 
ATOM   1632 S  SD  A MET A 1 117 ? 32.83500 21.94400 11.05100  0.670 73.10000  ?  117 MET A SD  1 
ATOM   1633 S  SD  B MET A 1 117 ? 32.51600 21.96000 10.99100  0.330 68.66000  ?  117 MET A SD  1 
ATOM   1634 C  CE  A MET A 1 117 ? 33.63400 21.27000 12.51100  0.670 67.53000  ?  117 MET A CE  1 
ATOM   1635 C  CE  B MET A 1 117 ? 33.41800 21.54000 12.51800  0.330 67.61000  ?  117 MET A CE  1 
ATOM   1636 N  N   A VAL A 1 118 ? 27.38100 20.90700 12.50700  0.670 50.49000  ?  118 VAL A N   1 
ATOM   1637 N  N   B VAL A 1 118 ? 26.68700 21.07600 12.21700  0.330 52.94000  ?  118 VAL A N   1 
ATOM   1638 C  CA  A VAL A 1 118 ? 26.47900 20.10400 13.33200  0.670 61.66000  ?  118 VAL A CA  1 
ATOM   1639 C  CA  B VAL A 1 118 ? 25.66000 20.35100 12.96800  0.330 60.27000  ?  118 VAL A CA  1 
ATOM   1640 C  C   A VAL A 1 118 ? 25.81700 19.06200 12.44400  0.670 57.78000  ?  118 VAL A C   1 
ATOM   1641 C  C   B VAL A 1 118 ? 24.96400 19.36700 12.00300  0.330 58.07000  ?  118 VAL A C   1 
ATOM   1642 O  O   A VAL A 1 118 ? 25.21000 19.42800 11.42600  0.670 56.22000  ?  118 VAL A O   1 
ATOM   1643 O  O   B VAL A 1 118 ? 24.29100 19.84100 11.07800  0.330 54.65000  ?  118 VAL A O   1 
ATOM   1644 C  CB  A VAL A 1 118 ? 25.41800 20.98200 14.02300  0.670 54.51000  ?  118 VAL A CB  1 
ATOM   1645 C  CB  B VAL A 1 118 ? 24.61700 21.26400 13.62500  0.330 50.56000  ?  118 VAL A CB  1 
ATOM   1646 C  CG1 A VAL A 1 118 ? 24.24900 20.13100 14.49200  0.670 52.78000  ?  118 VAL A CG1 1 
ATOM   1647 C  CG1 B VAL A 1 118 ? 23.32500 20.49800 13.84500  0.330 55.59000  ?  118 VAL A CG1 1 
ATOM   1648 C  CG2 A VAL A 1 118 ? 26.03700 21.75100 15.18200  0.670 46.31000  ?  118 VAL A CG2 1 
ATOM   1649 C  CG2 B VAL A 1 118 ? 25.08300 21.78100 14.94300  0.330 44.13000  ?  118 VAL A CG2 1 
ATOM   1650 N  N   A PRO A 1 119 ? 25.87800 17.76800 12.79300  0.670 59.96000  ?  119 PRO A N   1 
ATOM   1651 N  N   B PRO A 1 119 ? 25.01300 18.07300 12.25800  0.330 63.18000  ?  119 PRO A N   1 
ATOM   1652 C  CA  A PRO A 1 119 ? 25.33800 16.74200 11.88800  0.670 54.10000  ?  119 PRO A CA  1 
ATOM   1653 C  CA  B PRO A 1 119 ? 24.53100 17.11800 11.23700  0.330 58.17000  ?  119 PRO A CA  1 
ATOM   1654 C  C   A PRO A 1 119 ? 23.81800 16.65600 11.88400  0.670 52.27000  ?  119 PRO A C   1 
ATOM   1655 C  C   B PRO A 1 119 ? 23.01800 17.04500 11.08400  0.330 61.96000  ?  119 PRO A C   1 
ATOM   1656 O  O   A PRO A 1 119 ? 23.21700 16.35600 10.84800  0.670 60.20000  ?  119 PRO A O   1 
ATOM   1657 O  O   B PRO A 1 119 ? 22.48900 17.09200 9.94600   0.330 48.61000  ?  119 PRO A O   1 
ATOM   1658 C  CB  A PRO A 1 119 ? 25.96100 15.43400 12.40300  0.670 54.49000  ?  119 PRO A CB  1 
ATOM   1659 C  CB  B PRO A 1 119 ? 25.10500 15.78300 11.72200  0.330 56.91000  ?  119 PRO A CB  1 
ATOM   1660 C  CG  A PRO A 1 119 ? 26.64800 15.75800 13.70300  0.670 65.72000  ?  119 PRO A CG  1 
ATOM   1661 C  CG  B PRO A 1 119 ? 25.72700 16.00800 13.03700  0.330 57.36000  ?  119 PRO A CG  1 
ATOM   1662 C  CD  A PRO A 1 119 ? 26.41900 17.20000 14.04200  0.670 67.21000  ?  119 PRO A CD  1 
ATOM   1663 C  CD  B PRO A 1 119 ? 25.49900 17.40700 13.47400  0.330 61.30000  ?  119 PRO A CD  1 
ATOM   1664 N  N   A GLY A 1 120 ? 23.18500 16.90700 13.02900  0.670 61.85000  ?  120 GLY A N   1 
ATOM   1665 N  N   B GLY A 1 120 ? 22.29800 16.89800 12.19300  0.330 69.17000  ?  120 GLY A N   1 
ATOM   1666 C  CA  A GLY A 1 120 ? 21.75200 16.74600 13.15500  0.670 70.92000  ?  120 GLY A CA  1 
ATOM   1667 C  CA  B GLY A 1 120 ? 20.88600 16.61500 12.08500  0.330 68.24000  ?  120 GLY A CA  1 
ATOM   1668 C  C   A GLY A 1 120 ? 20.96100 17.91500 12.60200  0.670 66.47000  ?  120 GLY A C   1 
ATOM   1669 C  C   B GLY A 1 120 ? 20.06900 17.79900 11.61400  0.330 65.94000  ?  120 GLY A C   1 
ATOM   1670 O  O   A GLY A 1 120 ? 21.50000 18.91300 12.12300  0.670 73.51000  ?  120 GLY A O   1 
ATOM   1671 O  O   B GLY A 1 120 ? 20.56600 18.83600 11.17800  0.330 66.03000  ?  120 GLY A O   1 
ATOM   1672 N  N   A ILE A 1 121 ? 19.63400 17.78300 12.70000  0.670 69.14000  ?  121 ILE A N   1 
ATOM   1673 N  N   B ILE A 1 121 ? 18.76000 17.62500 11.71400  0.330 65.50000  ?  121 ILE A N   1 
ATOM   1674 C  CA  A ILE A 1 121 ? 18.73100 18.82400 12.22700  0.670 68.51000  ?  121 ILE A CA  1 
ATOM   1675 C  CA  B ILE A 1 121 ? 17.87600 18.66300 11.23900  0.330 65.82000  ?  121 ILE A CA  1 
ATOM   1676 C  C   A ILE A 1 121 ? 18.82600 20.09900 13.04100  0.670 63.46000  ?  121 ILE A C   1 
ATOM   1677 C  C   B ILE A 1 121 ? 17.97600 19.94500 12.05000  0.330 62.18000  ?  121 ILE A C   1 
ATOM   1678 O  O   A ILE A 1 121 ? 18.32000 21.14100 12.60500  0.670 51.25000  ?  121 ILE A O   1 
ATOM   1679 O  O   B ILE A 1 121 ? 17.59100 21.01300 11.55700  0.330 52.59000  ?  121 ILE A O   1 
ATOM   1680 C  CB  A ILE A 1 121 ? 17.27800 18.33300 12.25900  0.670 72.97000  ?  121 ILE A CB  1 
ATOM   1681 C  CB  B ILE A 1 121 ? 16.43400 18.17000 11.25500  0.330 72.45000  ?  121 ILE A CB  1 
ATOM   1682 C  CG1 A ILE A 1 121 ? 16.35700 19.25200 11.47300  0.670 75.69000  ?  121 ILE A CG1 1 
ATOM   1683 C  CG1 B ILE A 1 121 ? 15.63700 19.06200 10.32700  0.330 76.83000  ?  121 ILE A CG1 1 
ATOM   1684 C  CG2 A ILE A 1 121 ? 16.76400 18.34900 13.69700  0.670 67.29000  ?  121 ILE A CG2 1 
ATOM   1685 C  CG2 B ILE A 1 121 ? 15.87900 18.32800 12.64900  0.330 74.05000  ?  121 ILE A CG2 1 
ATOM   1686 C  CD1 A ILE A 1 121 ? 15.32800 18.51600 10.64500  0.670 76.39000  ?  121 ILE A CD1 1 
ATOM   1687 C  CD1 B ILE A 1 121 ? 14.75300 18.35500 9.40600   0.330 76.85000  ?  121 ILE A CD1 1 
ATOM   1688 N  N   A GLU A 1 122 ? 19.41800 20.05000 14.24000  0.670 65.00000  ?  122 GLU A N   1 
ATOM   1689 N  N   B GLU A 1 122 ? 18.43500 19.86200 13.30400  0.330 64.16000  ?  122 GLU A N   1 
ATOM   1690 C  CA  A GLU A 1 122 ? 19.62400 21.30300 14.95800  0.670 67.17000  ?  122 GLU A CA  1 
ATOM   1691 C  CA  B GLU A 1 122 ? 18.59800 21.08200 14.07000  0.330 59.44000  ?  122 GLU A CA  1 
ATOM   1692 C  C   A GLU A 1 122 ? 20.32600 22.32200 14.06600  0.670 50.68000  ?  122 GLU A C   1 
ATOM   1693 C  C   B GLU A 1 122 ? 19.37600 22.10300 13.30000  0.330 47.68000  ?  122 GLU A C   1 
ATOM   1694 O  O   A GLU A 1 122 ? 20.24700 23.53000 14.31900  0.670 44.70000  ?  122 GLU A O   1 
ATOM   1695 O  O   B GLU A 1 122 ? 19.19200 23.29200 13.53500  0.330 46.21000  ?  122 GLU A O   1 
ATOM   1696 C  CB  A GLU A 1 122 ? 20.46500 21.13400 16.23000  0.670 57.68000  ?  122 GLU A CB  1 
ATOM   1697 C  CB  B GLU A 1 122 ? 19.32500 20.87300 15.38900  0.330 62.85000  ?  122 GLU A CB  1 
ATOM   1698 C  CG  A GLU A 1 122 ? 20.20400 19.89900 17.03600  0.670 62.26000  ?  122 GLU A CG  1 
ATOM   1699 C  CG  B GLU A 1 122 ? 19.20100 19.53300 16.04700  0.330 63.73000  ?  122 GLU A CG  1 
ATOM   1700 C  CD  A GLU A 1 122 ? 21.21100 18.81500 16.72000  0.670 69.04000  ?  122 GLU A CD  1 
ATOM   1701 C  CD  B GLU A 1 122 ? 20.51100 18.75600 16.01900  0.330 70.51000  ?  122 GLU A CD  1 
ATOM   1702 O  OE1 A GLU A 1 122 ? 22.42300 19.12800 16.60500  0.670 56.52000  ?  122 GLU A OE1 1 
ATOM   1703 O  OE1 B GLU A 1 122 ? 21.60300 19.35300 16.27400  0.330 64.51000  ?  122 GLU A OE1 1 
ATOM   1704 O  OE2 A GLU A 1 122 ? 20.78700 17.64700 16.59100  0.670 70.65000  -1 122 GLU A OE2 1 
ATOM   1705 O  OE2 B GLU A 1 122 ? 20.44700 17.53700 15.73700  0.330 75.09000  -1 122 GLU A OE2 1 
ATOM   1706 N  N   A ARG A 1 123 ? 21.04500 21.85100 13.04000  0.670 41.98000  ?  123 ARG A N   1 
ATOM   1707 N  N   B ARG A 1 123 ? 20.25300 21.66400 12.40200  0.330 46.31000  ?  123 ARG A N   1 
ATOM   1708 C  CA  A ARG A 1 123 ? 21.76700 22.75700 12.15500  0.670 55.61000  ?  123 ARG A CA  1 
ATOM   1709 C  CA  B ARG A 1 123 ? 21.07200 22.62500 11.68400  0.330 49.66000  ?  123 ARG A CA  1 
ATOM   1710 C  C   A ARG A 1 123 ? 20.82000 23.67600 11.39700  0.670 45.53000  ?  123 ARG A C   1 
ATOM   1711 C  C   B ARG A 1 123 ? 20.20600 23.70300 11.05700  0.330 40.15000  ?  123 ARG A C   1 
ATOM   1712 O  O   A ARG A 1 123 ? 21.20700 24.78800 11.02400  0.670 39.23000  ?  123 ARG A O   1 
ATOM   1713 O  O   B ARG A 1 123 ? 20.60700 24.87500 11.03600  0.330 39.34000  ?  123 ARG A O   1 
ATOM   1714 C  CB  A ARG A 1 123 ? 22.63000 21.95800 11.17700  0.670 44.72000  ?  123 ARG A CB  1 
ATOM   1715 C  CB  B ARG A 1 123 ? 21.96000 21.92400 10.64000  0.330 51.00000  ?  123 ARG A CB  1 
ATOM   1716 C  CG  A ARG A 1 123 ? 21.86200 21.28700 10.04100  0.670 55.19000  ?  123 ARG A CG  1 
ATOM   1717 C  CG  B ARG A 1 123 ? 21.29100 21.51600 9.32900   0.330 52.79000  ?  123 ARG A CG  1 
ATOM   1718 C  CD  A ARG A 1 123 ? 22.76500 20.31500 9.28700   0.670 64.28000  ?  123 ARG A CD  1 
ATOM   1719 C  CD  B ARG A 1 123 ? 22.23400 20.62100 8.45000   0.330 61.20000  ?  123 ARG A CD  1 
ATOM   1720 N  NE  A ARG A 1 123 ? 22.18100 19.83800 8.03600   0.670 60.77000  ?  123 ARG A NE  1 
ATOM   1721 N  NE  B ARG A 1 123 ? 21.54700 20.32300 7.19900   0.330 58.18000  ?  123 ARG A NE  1 
ATOM   1722 C  CZ  A ARG A 1 123 ? 21.27900 18.86600 7.95100   0.670 65.71000  ?  123 ARG A CZ  1 
ATOM   1723 C  CZ  B ARG A 1 123 ? 20.54400 19.45800 7.08800   0.330 57.17000  ?  123 ARG A CZ  1 
ATOM   1724 N  NH1 A ARG A 1 123 ? 20.84400 18.26300 9.04800   0.670 72.58000  ?  123 ARG A NH1 1 
ATOM   1725 N  NH1 B ARG A 1 123 ? 20.19100 18.67900 8.09200   0.330 65.53000  ?  123 ARG A NH1 1 
ATOM   1726 N  NH2 A ARG A 1 123 ? 20.80900 18.49800 6.76700   0.670 51.88000  ?  123 ARG A NH2 1 
ATOM   1727 N  NH2 B ARG A 1 123 ? 19.84600 19.40900 5.96100   0.330 49.82000  ?  123 ARG A NH2 1 
ATOM   1728 N  N   A TYR A 1 124 ? 19.58300 23.24000 11.15400  0.670 32.17000  ?  124 TYR A N   1 
ATOM   1729 N  N   B TYR A 1 124 ? 18.98700 23.35200 10.65300  0.330 32.82000  ?  124 TYR A N   1 
ATOM   1730 C  CA  A TYR A 1 124 ? 18.62300 24.13900 10.52300  0.670 32.56000  ?  124 TYR A CA  1 
ATOM   1731 C  CA  B TYR A 1 124 ? 18.09100 24.36100 10.12100  0.330 36.09000  ?  124 TYR A CA  1 
ATOM   1732 C  C   A TYR A 1 124 ? 18.16400 25.21400 11.49900  0.670 45.04000  ?  124 TYR A C   1 
ATOM   1733 C  C   B TYR A 1 124 ? 17.68200 25.40800 11.18600  0.330 41.02000  ?  124 TYR A C   1 
ATOM   1734 O  O   A TYR A 1 124 ? 17.84500 26.33400 11.08300  0.670 34.61000  ?  124 TYR A O   1 
ATOM   1735 O  O   B TYR A 1 124 ? 17.54200 26.60100 10.86400  0.330 35.06000  ?  124 TYR A O   1 
ATOM   1736 C  CB  A TYR A 1 124 ? 17.43400 23.34900 9.98300   0.670 27.00000  ?  124 TYR A CB  1 
ATOM   1737 C  CB  B TYR A 1 124 ? 16.88900 23.68000 9.52400   0.330 36.19000  ?  124 TYR A CB  1 
ATOM   1738 C  CG  A TYR A 1 124 ? 17.75400 22.53900 8.74100   0.670 48.25000  ?  124 TYR A CG  1 
ATOM   1739 C  CG  B TYR A 1 124 ? 17.09200 22.89500 8.24000   0.330 44.95000  ?  124 TYR A CG  1 
ATOM   1740 C  CD1 A TYR A 1 124 ? 18.05900 23.16100 7.53400   0.670 44.02000  ?  124 TYR A CD1 1 
ATOM   1741 C  CD1 B TYR A 1 124 ? 17.16500 23.52300 7.00300   0.330 48.23000  ?  124 TYR A CD1 1 
ATOM   1742 C  CD2 A TYR A 1 124 ? 17.74900 21.15200 8.77700   0.670 55.12000  ?  124 TYR A CD2 1 
ATOM   1743 C  CD2 B TYR A 1 124 ? 17.22400 21.51400 8.26800   0.330 55.96000  ?  124 TYR A CD2 1 
ATOM   1744 C  CE1 A TYR A 1 124 ? 18.35100 22.41800 6.39900   0.670 46.79000  ?  124 TYR A CE1 1 
ATOM   1745 C  CE1 B TYR A 1 124 ? 17.31100 22.81000 5.83500   0.330 45.46000  ?  124 TYR A CE1 1 
ATOM   1746 C  CE2 A TYR A 1 124 ? 18.03800 20.40500 7.65100   0.670 53.91000  ?  124 TYR A CE2 1 
ATOM   1747 C  CE2 B TYR A 1 124 ? 17.38900 20.79200 7.09500   0.330 60.35000  ?  124 TYR A CE2 1 
ATOM   1748 C  CZ  A TYR A 1 124 ? 18.33800 21.04100 6.46700   0.670 65.46000  ?  124 TYR A CZ  1 
ATOM   1749 C  CZ  B TYR A 1 124 ? 17.43900 21.45300 5.87400   0.330 53.52000  ?  124 TYR A CZ  1 
ATOM   1750 O  OH  A TYR A 1 124 ? 18.62400 20.28900 5.35100   0.670 51.31000  ?  124 TYR A OH  1 
ATOM   1751 O  OH  B TYR A 1 124 ? 17.61400 20.70000 4.72300   0.330 51.63000  ?  124 TYR A OH  1 
ATOM   1752 N  N   A ALA A 1 125 ? 18.13700 24.89900 12.79600  0.670 42.51000  ?  125 ALA A N   1 
ATOM   1753 N  N   B ALA A 1 125 ? 17.51600 24.99800 12.45500  0.330 41.53000  ?  125 ALA A N   1 
ATOM   1754 C  CA  A ALA A 1 125 ? 17.84200 25.91800 13.79800  0.670 36.44000  ?  125 ALA A CA  1 
ATOM   1755 C  CA  B ALA A 1 125 ? 17.20900 25.96200 13.49800  0.330 33.80000  ?  125 ALA A CA  1 
ATOM   1756 C  C   A ALA A 1 125 ? 18.92200 26.99300 13.81500  0.670 38.70000  ?  125 ALA A C   1 
ATOM   1757 C  C   B ALA A 1 125 ? 18.28100 27.02100 13.48700  0.330 35.32000  ?  125 ALA A C   1 
ATOM   1758 O  O   A ALA A 1 125 ? 18.62500 28.18400 13.96600  0.670 36.84000  ?  125 ALA A O   1 
ATOM   1759 O  O   B ALA A 1 125 ? 18.00100 28.20300 13.23700  0.330 26.58000  ?  125 ALA A O   1 
ATOM   1760 C  CB  A ALA A 1 125 ? 17.70700 25.27200 15.17600  0.670 32.81000  ?  125 ALA A CB  1 
ATOM   1761 C  CB  B ALA A 1 125 ? 17.12700 25.27200 14.86900  0.330 36.29000  ?  125 ALA A CB  1 
ATOM   1762 N  N   A LEU A 1 126 ? 20.18700 26.59200 13.67500  0.670 33.22000  ?  126 LEU A N   1 
ATOM   1763 N  N   B LEU A 1 126 ? 19.53200 26.58500 13.74400  0.330 36.88000  ?  126 LEU A N   1 
ATOM   1764 C  CA  A LEU A 1 126 ? 21.26200 27.57600 13.59500  0.670 32.42000  ?  126 LEU A CA  1 
ATOM   1765 C  CA  B LEU A 1 126 ? 20.72700 27.37400 13.47500  0.330 34.38000  ?  126 LEU A CA  1 
ATOM   1766 C  C   A LEU A 1 126 ? 21.16700 28.38400 12.30500  0.670 33.58000  ?  126 LEU A C   1 
ATOM   1767 C  C   B LEU A 1 126 ? 20.65200 28.10700 12.14100  0.330 33.87000  ?  126 LEU A C   1 
ATOM   1768 O  O   A LEU A 1 126 ? 21.35200 29.60700 12.31500  0.670 36.17000  ?  126 LEU A O   1 
ATOM   1769 O  O   B LEU A 1 126 ? 20.63000 29.33700 12.11400  0.330 27.18000  ?  126 LEU A O   1 
ATOM   1770 C  CB  A LEU A 1 126 ? 22.61800 26.87700 13.70100  0.670 36.06000  ?  126 LEU A CB  1 
ATOM   1771 C  CB  B LEU A 1 126 ? 21.96500 26.48900 13.49900  0.330 36.30000  ?  126 LEU A CB  1 
ATOM   1772 C  CG  A LEU A 1 126 ? 22.87500 26.20500 15.05100  0.670 47.81000  ?  126 LEU A CG  1 
ATOM   1773 C  CG  B LEU A 1 126 ? 22.42400 26.12300 14.88900  0.330 45.33000  ?  126 LEU A CG  1 
ATOM   1774 C  CD1 A LEU A 1 126 ? 23.98500 25.17100 14.99200  0.670 33.30000  ?  126 LEU A CD1 1 
ATOM   1775 C  CD1 B LEU A 1 126 ? 23.47600 25.00600 14.86500  0.330 38.37000  ?  126 LEU A CD1 1 
ATOM   1776 C  CD2 A LEU A 1 126 ? 23.18500 27.26700 16.11500  0.670 38.17000  ?  126 LEU A CD2 1 
ATOM   1777 C  CD2 B LEU A 1 126 ? 23.05700 27.40700 15.46100  0.330 37.41000  ?  126 LEU A CD2 1 
ATOM   1778 N  N   A PHE A 1 127 ? 20.85500 27.72100 11.18900  0.670 37.61000  ?  127 PHE A N   1 
ATOM   1779 N  N   B PHE A 1 127 ? 20.64600 27.37900 11.02300  0.330 37.18000  ?  127 PHE A N   1 
ATOM   1780 C  CA  A PHE A 1 127 ? 20.69500 28.43900 9.93000   0.670 36.22000  ?  127 PHE A CA  1 
ATOM   1781 C  CA  B PHE A 1 127 ? 20.51500 28.10700 9.77500   0.330 36.29000  ?  127 PHE A CA  1 
ATOM   1782 C  C   A PHE A 1 127 ? 19.59300 29.48800 10.02900  0.670 31.60000  ?  127 PHE A C   1 
ATOM   1783 C  C   B PHE A 1 127 ? 19.42100 29.13400 9.91500   0.330 32.18000  ?  127 PHE A C   1 
ATOM   1784 O  O   A PHE A 1 127 ? 19.75100 30.61500 9.54500   0.670 31.18000  ?  127 PHE A O   1 
ATOM   1785 O  O   B PHE A 1 127 ? 19.61300 30.30300 9.59100   0.330 31.72000  ?  127 PHE A O   1 
ATOM   1786 C  CB  A PHE A 1 127 ? 20.39400 27.45800 8.79900   0.670 35.56000  ?  127 PHE A CB  1 
ATOM   1787 C  CB  B PHE A 1 127 ? 20.16200 27.24800 8.58200   0.330 34.82000  ?  127 PHE A CB  1 
ATOM   1788 C  CG  A PHE A 1 127 ? 19.94500 28.12300 7.53400   0.670 29.72000  ?  127 PHE A CG  1 
ATOM   1789 C  CG  B PHE A 1 127 ? 19.82100 28.11600 7.37700   0.330 30.79000  ?  127 PHE A CG  1 
ATOM   1790 C  CD1 A PHE A 1 127 ? 20.87200 28.62200 6.63200   0.670 37.63000  ?  127 PHE A CD1 1 
ATOM   1791 C  CD1 B PHE A 1 127 ? 20.82800 28.62200 6.58100   0.330 37.64000  ?  127 PHE A CD1 1 
ATOM   1792 C  CD2 A PHE A 1 127 ? 18.59800 28.25800 7.24600   0.670 35.25000  ?  127 PHE A CD2 1 
ATOM   1793 C  CD2 B PHE A 1 127 ? 18.51300 28.49900 7.09300   0.330 35.51000  ?  127 PHE A CD2 1 
ATOM   1794 C  CE1 A PHE A 1 127 ? 20.46400 29.24000 5.46900   0.670 40.76000  ?  127 PHE A CE1 1 
ATOM   1795 C  CE1 B PHE A 1 127 ? 20.55500 29.46700 5.47400   0.330 39.89000  ?  127 PHE A CE1 1 
ATOM   1796 C  CE2 A PHE A 1 127 ? 18.18400 28.87700 6.07800   0.670 41.69000  ?  127 PHE A CE2 1 
ATOM   1797 C  CE2 B PHE A 1 127 ? 18.22200 29.33000 6.01900   0.330 41.20000  ?  127 PHE A CE2 1 
ATOM   1798 C  CZ  A PHE A 1 127 ? 19.11700 29.36600 5.19300   0.670 45.81000  ?  127 PHE A CZ  1 
ATOM   1799 C  CZ  B PHE A 1 127 ? 19.27700 29.83200 5.19000   0.330 41.06000  ?  127 PHE A CZ  1 
ATOM   1800 N  N   A GLY A 1 128 ? 18.47100 29.13500 10.65800  0.670 29.58000  ?  128 GLY A N   1 
ATOM   1801 N  N   B GLY A 1 128 ? 18.26900 28.71500 10.42000  0.330 27.08000  ?  128 GLY A N   1 
ATOM   1802 C  CA  A GLY A 1 128 ? 17.38700 30.09100 10.81100  0.670 24.92000  ?  128 GLY A CA  1 
ATOM   1803 C  CA  B GLY A 1 128 ? 17.19200 29.64800 10.65800  0.330 27.20000  ?  128 GLY A CA  1 
ATOM   1804 C  C   A GLY A 1 128 ? 17.79200 31.31600 11.60300  0.670 34.16000  ?  128 GLY A C   1 
ATOM   1805 C  C   B GLY A 1 128 ? 17.56000 30.76900 11.61400  0.330 31.22000  ?  128 GLY A C   1 
ATOM   1806 O  O   A GLY A 1 128 ? 17.36900 32.43400 11.29500  0.670 32.44000  ?  128 GLY A O   1 
ATOM   1807 O  O   B GLY A 1 128 ? 17.01800 31.85000 11.45200  0.330 33.50000  ?  128 GLY A O   1 
ATOM   1808 N  N   A MET A 1 129 ? 18.61300 31.12900 12.63800  0.670 22.46000  ?  129 MET A N   1 
ATOM   1809 N  N   B MET A 1 129 ? 18.43700 30.61300 12.60800  0.330 23.71000  ?  129 MET A N   1 
ATOM   1810 C  CA  A MET A 1 129 ? 19.03400 32.27700 13.43200  0.670 24.24000  ?  129 MET A CA  1 
ATOM   1811 C  CA  B MET A 1 129 ? 18.77200 31.83500 13.32500  0.330 25.80000  ?  129 MET A CA  1 
ATOM   1812 C  C   A MET A 1 129 ? 19.90000 33.22600 12.61700  0.670 29.47000  ?  129 MET A C   1 
ATOM   1813 C  C   B MET A 1 129 ? 19.43300 32.84900 12.40500  0.330 30.25000  ?  129 MET A C   1 
ATOM   1814 O  O   A MET A 1 129 ? 19.76500 34.45000 12.72600  0.670 21.69000  ?  129 MET A O   1 
ATOM   1815 O  O   B MET A 1 129 ? 18.91100 33.95700 12.24300  0.330 27.74000  ?  129 MET A O   1 
ATOM   1816 C  CB  A MET A 1 129 ? 19.79800 31.82700 14.67000  0.670 30.93000  ?  129 MET A CB  1 
ATOM   1817 C  CB  B MET A 1 129 ? 19.64300 31.61000 14.53700  0.330 31.43000  ?  129 MET A CB  1 
ATOM   1818 C  CG  A MET A 1 129 ? 19.46700 32.67900 15.86300  0.670 45.53000  ?  129 MET A CG  1 
ATOM   1819 C  CG  B MET A 1 129 ? 19.34300 32.86700 15.25800  0.330 40.87000  ?  129 MET A CG  1 
ATOM   1820 S  SD  A MET A 1 129 ? 20.42500 32.32800 17.35100  0.670 54.47000  ?  129 MET A SD  1 
ATOM   1821 S  SD  B MET A 1 129 ? 20.25900 33.26000 16.68300  0.330 44.14000  ?  129 MET A SD  1 
ATOM   1822 C  CE  A MET A 1 129 ? 22.04800 32.94500 16.86700  0.670 42.02000  ?  129 MET A CE  1 
ATOM   1823 C  CE  B MET A 1 129 ? 21.83300 32.90500 15.89700  0.330 41.27000  ?  129 MET A CE  1 
ATOM   1824 N  N   A GLY A 1 130 ? 20.80900 32.68000 11.81100  0.670 21.81000  ?  130 GLY A N   1 
ATOM   1825 N  N   B GLY A 1 130 ? 20.54300 32.47000 11.74800  0.330 26.01000  ?  130 GLY A N   1 
ATOM   1826 C  CA  A GLY A 1 130 ? 21.58200 33.52300 10.91700  0.670 27.49000  ?  130 GLY A CA  1 
ATOM   1827 C  CA  B GLY A 1 130 ? 21.12200 33.21500 10.62500  0.330 28.31000  ?  130 GLY A CA  1 
ATOM   1828 C  C   A GLY A 1 130 ? 20.70500 34.25200 9.92000   0.670 33.86000  ?  130 GLY A C   1 
ATOM   1829 C  C   B GLY A 1 130 ? 20.19600 34.17900 9.87100   0.330 32.04000  ?  130 GLY A C   1 
ATOM   1830 O  O   A GLY A 1 130 ? 20.96000 35.41200 9.58700   0.670 33.73000  ?  130 GLY A O   1 
ATOM   1831 O  O   B GLY A 1 130 ? 20.38700 35.42000 9.90000   0.330 30.79000  ?  130 GLY A O   1 
ATOM   1832 N  N   A ALA A 1 131 ? 19.65700 33.58500 9.43100   0.670 24.42000  ?  131 ALA A N   1 
ATOM   1833 N  N   B ALA A 1 131 ? 19.17500 33.63400 9.21200   0.330 25.23000  ?  131 ALA A N   1 
ATOM   1834 C  CA  A ALA A 1 131 ? 18.74100 34.24300 8.50600   0.670 21.36000  ?  131 ALA A CA  1 
ATOM   1835 C  CA  B ALA A 1 131 ? 18.26700 34.47800 8.44600   0.330 25.26000  ?  131 ALA A CA  1 
ATOM   1836 C  C   A ALA A 1 131 ? 18.06700 35.43900 9.16300   0.670 29.23000  ?  131 ALA A C   1 
ATOM   1837 C  C   B ALA A 1 131 ? 17.78700 35.74000 9.18200   0.330 30.34000  ?  131 ALA A C   1 
ATOM   1838 O  O   A ALA A 1 131 ? 17.94200 36.50600 8.55200   0.670 37.04000  ?  131 ALA A O   1 
ATOM   1839 O  O   B ALA A 1 131 ? 17.89500 36.85000 8.64100   0.330 34.79000  ?  131 ALA A O   1 
ATOM   1840 C  CB  A ALA A 1 131 ? 17.69000 33.25400 8.00700   0.670 24.57000  ?  131 ALA A CB  1 
ATOM   1841 C  CB  B ALA A 1 131 ? 17.05200 33.67000 7.99700   0.330 19.76000  ?  131 ALA A CB  1 
ATOM   1842 N  N   A VAL A 1 132 ? 17.62200 35.28000 10.41000  0.670 40.20000  ?  132 VAL A N   1 
ATOM   1843 N  N   B VAL A 1 132 ? 17.21200 35.60200 10.37400  0.330 37.26000  ?  132 VAL A N   1 
ATOM   1844 C  CA  A VAL A 1 132 ? 16.95800 36.38200 11.09900  0.670 32.64000  ?  132 VAL A CA  1 
ATOM   1845 C  CA  B VAL A 1 132 ? 16.70800 36.77900 11.07500  0.330 31.83000  ?  132 VAL A CA  1 
ATOM   1846 C  C   A VAL A 1 132 ? 17.91600 37.55700 11.25900  0.670 28.10000  ?  132 VAL A C   1 
ATOM   1847 C  C   B VAL A 1 132 ? 17.80000 37.82200 11.21000  0.330 29.90000  ?  132 VAL A C   1 
ATOM   1848 O  O   A VAL A 1 132 ? 17.56600 38.71100 10.98400  0.670 29.87000  ?  132 VAL A O   1 
ATOM   1849 O  O   B VAL A 1 132 ? 17.63200 38.98300 10.80600  0.330 29.40000  ?  132 VAL A O   1 
ATOM   1850 C  CB  A VAL A 1 132 ? 16.40600 35.91400 12.45700  0.670 39.07000  ?  132 VAL A CB  1 
ATOM   1851 C  CB  B VAL A 1 132 ? 16.15100 36.35600 12.44400  0.330 38.91000  ?  132 VAL A CB  1 
ATOM   1852 C  CG1 A VAL A 1 132 ? 15.95100 37.11100 13.27500  0.670 37.84000  ?  132 VAL A CG1 1 
ATOM   1853 C  CG1 B VAL A 1 132 ? 15.56000 37.55500 13.23100  0.330 34.93000  ?  132 VAL A CG1 1 
ATOM   1854 C  CG2 A VAL A 1 132 ? 15.26400 34.93300 12.25500  0.670 37.48000  ?  132 VAL A CG2 1 
ATOM   1855 C  CG2 B VAL A 1 132 ? 15.17200 35.19800 12.25700  0.330 37.27000  ?  132 VAL A CG2 1 
ATOM   1856 N  N   A ALA A 1 133 ? 19.14500 37.27600 11.70000  0.670 25.00000  ?  133 ALA A N   1 
ATOM   1857 N  N   B ALA A 1 133 ? 18.95000 37.41100 11.74600  0.330 26.10000  ?  133 ALA A N   1 
ATOM   1858 C  CA  A ALA A 1 133 ? 20.12800 38.33900 11.87800  0.670 31.03000  ?  133 ALA A CA  1 
ATOM   1859 C  CA  B ALA A 1 133 ? 20.09300 38.31500 11.85800  0.330 31.73000  ?  133 ALA A CA  1 
ATOM   1860 C  C   A ALA A 1 133 ? 20.50700 38.98000 10.55100  0.670 31.89000  ?  133 ALA A C   1 
ATOM   1861 C  C   B ALA A 1 133 ? 20.43600 39.00100 10.52600  0.330 32.25000  ?  133 ALA A C   1 
ATOM   1862 O  O   A ALA A 1 133 ? 20.81000 40.17700 10.50800  0.670 30.83000  ?  133 ALA A O   1 
ATOM   1863 O  O   B ALA A 1 133 ? 20.91500 40.14500 10.51600  0.330 30.27000  ?  133 ALA A O   1 
ATOM   1864 C  CB  A ALA A 1 133 ? 21.37500 37.79300 12.57400  0.670 25.03000  ?  133 ALA A CB  1 
ATOM   1865 C  CB  B ALA A 1 133 ? 21.29500 37.53700 12.39600  0.330 26.57000  ?  133 ALA A CB  1 
ATOM   1866 N  N   A PHE A 1 134 ? 20.50200 38.20300 9.46700   0.670 28.45000  ?  134 PHE A N   1 
ATOM   1867 N  N   B PHE A 1 134 ? 20.18800 38.30800 9.40100   0.330 29.10000  ?  134 PHE A N   1 
ATOM   1868 C  CA  A PHE A 1 134 ? 20.79900 38.76300 8.15500   0.670 31.61000  ?  134 PHE A CA  1 
ATOM   1869 C  CA  B PHE A 1 134 ? 20.48900 38.74500 8.04000   0.330 31.30000  ?  134 PHE A CA  1 
ATOM   1870 C  C   A PHE A 1 134 ? 19.75000 39.79100 7.75100   0.670 32.23000  ?  134 PHE A C   1 
ATOM   1871 C  C   B PHE A 1 134 ? 19.42000 39.65400 7.50200   0.330 31.58000  ?  134 PHE A C   1 
ATOM   1872 O  O   A PHE A 1 134 ? 20.08500 40.84500 7.19600   0.670 23.16000  ?  134 PHE A O   1 
ATOM   1873 O  O   B PHE A 1 134 ? 19.72800 40.63100 6.79400   0.330 26.20000  ?  134 PHE A O   1 
ATOM   1874 C  CB  A PHE A 1 134 ? 20.88500 37.63800 7.12400   0.670 28.87000  ?  134 PHE A CB  1 
ATOM   1875 C  CB  B PHE A 1 134 ? 20.58200 37.55200 7.08700   0.330 29.06000  ?  134 PHE A CB  1 
ATOM   1876 C  CG  A PHE A 1 134 ? 21.23500 38.10600 5.74600   0.670 30.66000  ?  134 PHE A CG  1 
ATOM   1877 C  CG  B PHE A 1 134 ? 21.01200 37.91500 5.73700   0.330 30.20000  ?  134 PHE A CG  1 
ATOM   1878 C  CD1 A PHE A 1 134 ? 22.49400 38.60900 5.47100   0.670 31.05000  ?  134 PHE A CD1 1 
ATOM   1879 C  CD1 B PHE A 1 134 ? 22.34400 38.07500 5.44400   0.330 30.91000  ?  134 PHE A CD1 1 
ATOM   1880 C  CD2 A PHE A 1 134 ? 20.30100 38.04900 4.72400   0.670 30.40000  ?  134 PHE A CD2 1 
ATOM   1881 C  CD2 B PHE A 1 134 ? 20.09300 38.14900 4.75800   0.330 29.65000  ?  134 PHE A CD2 1 
ATOM   1882 C  CE1 A PHE A 1 134 ? 22.81600 39.04300 4.19500   0.670 37.23000  ?  134 PHE A CE1 1 
ATOM   1883 C  CE1 B PHE A 1 134 ? 22.75700 38.38200 4.15500   0.330 34.32000  ?  134 PHE A CE1 1 
ATOM   1884 C  CE2 A PHE A 1 134 ? 20.61900 38.48100 3.45300   0.670 30.82000  ?  134 PHE A CE2 1 
ATOM   1885 C  CE2 B PHE A 1 134 ? 20.49200 38.48100 3.43600   0.330 31.03000  ?  134 PHE A CE2 1 
ATOM   1886 C  CZ  A PHE A 1 134 ? 21.87800 38.97800 3.19100   0.670 35.17000  ?  134 PHE A CZ  1 
ATOM   1887 C  CZ  B PHE A 1 134 ? 21.81500 38.60200 3.13500   0.330 33.20000  ?  134 PHE A CZ  1 
ATOM   1888 N  N   A LEU A 1 135 ? 18.47400 39.51000 8.02400   0.670 26.77000  ?  135 LEU A N   1 
ATOM   1889 N  N   B LEU A 1 135 ? 18.16400 39.30300 7.79100   0.330 28.78000  ?  135 LEU A N   1 
ATOM   1890 C  CA  A LEU A 1 135 ? 17.43400 40.48100 7.70300   0.670 33.80000  ?  135 LEU A CA  1 
ATOM   1891 C  CA  B LEU A 1 135 ? 17.06700 40.24600 7.55600   0.330 34.05000  ?  135 LEU A CA  1 
ATOM   1892 C  C   A LEU A 1 135 ? 17.66300 41.78900 8.45000   0.670 33.78000  ?  135 LEU A C   1 
ATOM   1893 C  C   B LEU A 1 135 ? 17.26000 41.49000 8.38000   0.330 32.42000  ?  135 LEU A C   1 
ATOM   1894 O  O   A LEU A 1 135 ? 17.44800 42.87400 7.89800   0.670 39.10000  ?  135 LEU A O   1 
ATOM   1895 O  O   B LEU A 1 135 ? 17.05800 42.61600 7.90900   0.330 37.08000  ?  135 LEU A O   1 
ATOM   1896 C  CB  A LEU A 1 135 ? 16.05700 39.90700 8.02700   0.670 28.62000  ?  135 LEU A CB  1 
ATOM   1897 C  CB  B LEU A 1 135 ? 15.73000 39.63200 7.92100   0.330 32.19000  ?  135 LEU A CB  1 
ATOM   1898 C  CG  A LEU A 1 135 ? 15.62300 38.76600 7.10700   0.670 37.99000  ?  135 LEU A CG  1 
ATOM   1899 C  CG  B LEU A 1 135 ? 15.13500 38.50700 7.05300   0.330 36.01000  ?  135 LEU A CG  1 
ATOM   1900 C  CD1 A LEU A 1 135 ? 14.36800 38.09500 7.63500   0.670 32.10000  ?  135 LEU A CD1 1 
ATOM   1901 C  CD1 B LEU A 1 135 ? 13.90200 38.08800 7.85200   0.330 31.57000  ?  135 LEU A CD1 1 
ATOM   1902 C  CD2 A LEU A 1 135 ? 15.40800 39.26500 5.68300   0.670 37.02000  ?  135 LEU A CD2 1 
ATOM   1903 C  CD2 B LEU A 1 135 ? 14.77100 39.04200 5.68300   0.330 36.15000  ?  135 LEU A CD2 1 
ATOM   1904 N  N   A GLY A 1 136 ? 18.10200 41.70700 9.70700   0.670 36.79000  ?  136 GLY A N   1 
ATOM   1905 N  N   B GLY A 1 136 ? 17.69200 41.29600 9.61500   0.330 36.38000  ?  136 GLY A N   1 
ATOM   1906 C  CA  A GLY A 1 136 ? 18.43000 42.91900 10.44000  0.670 35.58000  ?  136 GLY A CA  1 
ATOM   1907 C  CA  B GLY A 1 136 ? 18.18700 42.40900 10.38500  0.330 33.94000  ?  136 GLY A CA  1 
ATOM   1908 C  C   A GLY A 1 136 ? 19.60500 43.65800 9.83100   0.670 35.20000  ?  136 GLY A C   1 
ATOM   1909 C  C   B GLY A 1 136 ? 19.24000 43.20100 9.63000   0.330 33.92000  ?  136 GLY A C   1 
ATOM   1910 O  O   A GLY A 1 136 ? 19.62300 44.89100 9.79200   0.670 31.91000  ?  136 GLY A O   1 
ATOM   1911 O  O   B GLY A 1 136 ? 19.13800 44.42200 9.50700   0.330 33.89000  ?  136 GLY A O   1 
ATOM   1912 N  N   A LEU A 1 137 ? 20.60200 42.91600 9.34700   0.670 37.40000  ?  137 LEU A N   1 
ATOM   1913 N  N   B LEU A 1 137 ? 20.29000 42.52500 9.14200   0.330 33.16000  ?  137 LEU A N   1 
ATOM   1914 C  CA  A LEU A 1 137 ? 21.73600 43.54700 8.68200   0.670 38.24000  ?  137 LEU A CA  1 
ATOM   1915 C  CA  B LEU A 1 137 ? 21.36200 43.25000 8.43700   0.330 38.37000  ?  137 LEU A CA  1 
ATOM   1916 C  C   A LEU A 1 137 ? 21.29700 44.26300 7.41300   0.670 42.17000  ?  137 LEU A C   1 
ATOM   1917 C  C   B LEU A 1 137 ? 20.84300 43.84200 7.14400   0.330 40.01000  ?  137 LEU A C   1 
ATOM   1918 O  O   A LEU A 1 137 ? 21.74000 45.38500 7.13900   0.670 44.24000  ?  137 LEU A O   1 
ATOM   1919 O  O   B LEU A 1 137 ? 21.27600 44.92700 6.71500   0.330 43.02000  ?  137 LEU A O   1 
ATOM   1920 C  CB  A LEU A 1 137 ? 22.79800 42.49800 8.36500   0.670 32.32000  ?  137 LEU A CB  1 
ATOM   1921 C  CB  B LEU A 1 137 ? 22.53100 42.34500 8.07500   0.330 32.50000  ?  137 LEU A CB  1 
ATOM   1922 C  CG  A LEU A 1 137 ? 24.06100 42.99000 7.66300   0.670 43.79000  ?  137 LEU A CG  1 
ATOM   1923 C  CG  B LEU A 1 137 ? 23.75100 43.09000 7.60700   0.330 40.39000  ?  137 LEU A CG  1 
ATOM   1924 C  CD1 A LEU A 1 137 ? 24.82700 43.94500 8.56200   0.670 39.85000  ?  137 LEU A CD1 1 
ATOM   1925 C  CD1 B LEU A 1 137 ? 24.38600 43.63300 8.85400   0.330 40.03000  ?  137 LEU A CD1 1 
ATOM   1926 C  CD2 A LEU A 1 137 ? 24.93700 41.81800 7.25700   0.670 34.60000  ?  137 LEU A CD2 1 
ATOM   1927 C  CD2 B LEU A 1 137 ? 24.71900 42.18200 6.78400   0.330 34.54000  ?  137 LEU A CD2 1 
ATOM   1928 N  N   A VAL A 1 138 ? 20.42800 43.62800 6.62300   0.670 39.14000  ?  138 VAL A N   1 
ATOM   1929 N  N   B VAL A 1 138 ? 19.99000 43.08800 6.44700   0.330 35.12000  ?  138 VAL A N   1 
ATOM   1930 C  CA  A VAL A 1 138 ? 19.94100 44.25700 5.39800   0.670 37.46000  ?  138 VAL A CA  1 
ATOM   1931 C  CA  B VAL A 1 138 ? 19.32200 43.70000 5.32400   0.330 38.63000  ?  138 VAL A CA  1 
ATOM   1932 C  C   A VAL A 1 138 ? 19.19500 45.54000 5.72500   0.670 40.34000  ?  138 VAL A C   1 
ATOM   1933 C  C   B VAL A 1 138 ? 18.71300 45.01400 5.79600   0.330 38.04000  ?  138 VAL A C   1 
ATOM   1934 O  O   A VAL A 1 138 ? 19.30900 46.54400 5.00900   0.670 43.79000  ?  138 VAL A O   1 
ATOM   1935 O  O   B VAL A 1 138 ? 19.08800 46.08400 5.29400   0.330 41.66000  ?  138 VAL A O   1 
ATOM   1936 C  CB  A VAL A 1 138 ? 19.05200 43.27700 4.60800   0.670 36.54000  ?  138 VAL A CB  1 
ATOM   1937 C  CB  B VAL A 1 138 ? 18.29900 42.73300 4.70100   0.330 36.19000  ?  138 VAL A CB  1 
ATOM   1938 C  CG1 A VAL A 1 138 ? 18.30600 44.00400 3.49500   0.670 34.55000  ?  138 VAL A CG1 1 
ATOM   1939 C  CG1 B VAL A 1 138 ? 17.42500 43.42900 3.72200   0.330 32.59000  ?  138 VAL A CG1 1 
ATOM   1940 C  CG2 A VAL A 1 138 ? 19.88900 42.14000 4.05000   0.670 35.03000  ?  138 VAL A CG2 1 
ATOM   1941 C  CG2 B VAL A 1 138 ? 18.98800 41.62400 4.00500   0.330 35.05000  ?  138 VAL A CG2 1 
ATOM   1942 N  N   A TYR A 1 139 ? 18.40800 45.52900 6.80300   0.670 40.11000  ?  139 TYR A N   1 
ATOM   1943 N  N   B TYR A 1 139 ? 17.90600 44.97700 6.87700   0.330 34.36000  ?  139 TYR A N   1 
ATOM   1944 C  CA  A TYR A 1 139 ? 17.69300 46.73900 7.18700   0.670 46.02000  ?  139 TYR A CA  1 
ATOM   1945 C  CA  B TYR A 1 139 ? 17.34400 46.24700 7.35200   0.330 45.46000  ?  139 TYR A CA  1 
ATOM   1946 C  C   A TYR A 1 139 ? 18.66200 47.88500 7.44600   0.670 45.85000  ?  139 TYR A C   1 
ATOM   1947 C  C   B TYR A 1 139 ? 18.37600 47.34800 7.59800   0.330 44.38000  ?  139 TYR A C   1 
ATOM   1948 O  O   A TYR A 1 139 ? 18.41400 49.02300 7.03600   0.670 54.21000  ?  139 TYR A O   1 
ATOM   1949 O  O   B TYR A 1 139 ? 18.28200 48.40800 6.97100   0.330 50.46000  ?  139 TYR A O   1 
ATOM   1950 C  CB  A TYR A 1 139 ? 16.83200 46.49800 8.42700   0.670 48.15000  ?  139 TYR A CB  1 
ATOM   1951 C  CB  B TYR A 1 139 ? 16.53500 46.15200 8.64300   0.330 47.04000  ?  139 TYR A CB  1 
ATOM   1952 C  CG  A TYR A 1 139 ? 16.31500 47.79100 9.02900   0.670 56.88000  ?  139 TYR A CG  1 
ATOM   1953 C  CG  B TYR A 1 139 ? 16.26100 47.57900 9.12800   0.330 55.81000  ?  139 TYR A CG  1 
ATOM   1954 C  CD1 A TYR A 1 139 ? 15.16600 48.39700 8.53800   0.670 62.61000  ?  139 TYR A CD1 1 
ATOM   1955 C  CD1 B TYR A 1 139 ? 15.33400 48.36400 8.44200   0.330 61.97000  ?  139 TYR A CD1 1 
ATOM   1956 C  CD2 A TYR A 1 139 ? 16.98900 48.41700 10.07200  0.670 57.08000  ?  139 TYR A CD2 1 
ATOM   1957 C  CD2 B TYR A 1 139 ? 16.95400 48.16300 10.20600  0.330 56.47000  ?  139 TYR A CD2 1 
ATOM   1958 C  CE1 A TYR A 1 139 ? 14.69400 49.58400 9.07600   0.670 60.41000  ?  139 TYR A CE1 1 
ATOM   1959 C  CE1 B TYR A 1 139 ? 15.07700 49.67000 8.77400   0.330 60.20000  ?  139 TYR A CE1 1 
ATOM   1960 C  CE2 A TYR A 1 139 ? 16.52500 49.60600 10.61400  0.670 65.32000  ?  139 TYR A CE2 1 
ATOM   1961 C  CE2 B TYR A 1 139 ? 16.70100 49.50600 10.56300  0.330 64.25000  ?  139 TYR A CE2 1 
ATOM   1962 C  CZ  A TYR A 1 139 ? 15.37700 50.18300 10.11300  0.670 76.07000  ?  139 TYR A CZ  1 
ATOM   1963 C  CZ  B TYR A 1 139 ? 15.74200 50.25600 9.83200   0.330 71.34000  ?  139 TYR A CZ  1 
ATOM   1964 O  OH  A TYR A 1 139 ? 14.91000 51.36300 10.64800  0.670 86.93000  ?  139 TYR A OH  1 
ATOM   1965 O  OH  B TYR A 1 139 ? 15.44000 51.59500 10.12100  0.330 76.81000  ?  139 TYR A OH  1 
ATOM   1966 N  N   A TYR A 1 140 ? 19.77200 47.60900 8.13400   0.670 37.65000  ?  140 TYR A N   1 
ATOM   1967 N  N   B TYR A 1 140 ? 19.33900 47.15000 8.51100   0.330 38.63000  ?  140 TYR A N   1 
ATOM   1968 C  CA  A TYR A 1 140 ? 20.70600 48.68200 8.45800   0.670 43.24000  ?  140 TYR A CA  1 
ATOM   1969 C  CA  B TYR A 1 140 ? 20.27900 48.23200 8.74700   0.330 43.88000  ?  140 TYR A CA  1 
ATOM   1970 C  C   A TYR A 1 140 ? 21.41100 49.19200 7.20900   0.670 49.16000  ?  140 TYR A C   1 
ATOM   1971 C  C   B TYR A 1 140 ? 20.86200 48.72500 7.44400   0.330 44.90000  ?  140 TYR A C   1 
ATOM   1972 O  O   A TYR A 1 140 ? 21.65600 50.39600 7.07800   0.670 50.28000  ?  140 TYR A O   1 
ATOM   1973 O  O   B TYR A 1 140 ? 20.83100 49.93000 7.20700   0.330 45.85000  ?  140 TYR A O   1 
ATOM   1974 C  CB  A TYR A 1 140 ? 21.70600 48.20400 9.50900   0.670 42.72000  ?  140 TYR A CB  1 
ATOM   1975 C  CB  B TYR A 1 140 ? 21.34800 47.85800 9.76700   0.330 47.52000  ?  140 TYR A CB  1 
ATOM   1976 C  CG  A TYR A 1 140 ? 21.18300 48.41400 10.91300  0.670 58.95000  ?  140 TYR A CG  1 
ATOM   1977 C  CG  B TYR A 1 140 ? 20.74800 48.15200 11.12700  0.330 57.33000  ?  140 TYR A CG  1 
ATOM   1978 C  CD1 A TYR A 1 140 ? 20.41800 47.44100 11.54100  0.670 56.75000  ?  140 TYR A CD1 1 
ATOM   1979 C  CD1 B TYR A 1 140 ? 20.61700 49.48000 11.59600  0.330 55.52000  ?  140 TYR A CD1 1 
ATOM   1980 C  CD2 A TYR A 1 140 ? 21.42400 49.60000 11.59500  0.670 49.40000  ?  140 TYR A CD2 1 
ATOM   1981 C  CD2 B TYR A 1 140 ? 20.14500 47.13600 11.86700  0.330 54.88000  ?  140 TYR A CD2 1 
ATOM   1982 C  CE1 A TYR A 1 140 ? 19.92400 47.63400 12.81800  0.670 65.96000  ?  140 TYR A CE1 1 
ATOM   1983 C  CE1 B TYR A 1 140 ? 19.97100 49.76800 12.83200  0.330 59.99000  ?  140 TYR A CE1 1 
ATOM   1984 C  CE2 A TYR A 1 140 ? 20.93400 49.80200 12.87300  0.670 61.51000  ?  140 TYR A CE2 1 
ATOM   1985 C  CE2 B TYR A 1 140 ? 19.52800 47.40100 13.11200  0.330 61.43000  ?  140 TYR A CE2 1 
ATOM   1986 C  CZ  A TYR A 1 140 ? 20.18400 48.81600 13.48000  0.670 67.82000  ?  140 TYR A CZ  1 
ATOM   1987 C  CZ  B TYR A 1 140 ? 19.43500 48.71100 13.59100  0.330 63.64000  ?  140 TYR A CZ  1 
ATOM   1988 O  OH  A TYR A 1 140 ? 19.69100 49.01000 14.75200  0.670 67.38000  ?  140 TYR A OH  1 
ATOM   1989 O  OH  B TYR A 1 140 ? 18.78000 48.94200 14.78800  0.330 56.73000  ?  140 TYR A OH  1 
ATOM   1990 N  N   A LEU A 1 141 ? 21.72100 48.30100 6.26800   0.670 41.12000  ?  141 LEU A N   1 
ATOM   1991 N  N   B LEU A 1 141 ? 21.23400 47.81300 6.52200   0.330 41.97000  ?  141 LEU A N   1 
ATOM   1992 C  CA  A LEU A 1 141 ? 22.34900 48.73700 5.02600   0.670 41.11000  ?  141 LEU A CA  1 
ATOM   1993 C  CA  B LEU A 1 141 ? 21.64300 48.22300 5.17000   0.330 42.53000  ?  141 LEU A CA  1 
ATOM   1994 C  C   A LEU A 1 141 ? 21.40700 49.61500 4.21400   0.670 39.96000  ?  141 LEU A C   1 
ATOM   1995 C  C   B LEU A 1 141 ? 20.61900 49.15300 4.49600   0.330 42.03000  ?  141 LEU A C   1 
ATOM   1996 O  O   A LEU A 1 141 ? 21.80100 50.67500 3.71300   0.670 43.23000  ?  141 LEU A O   1 
ATOM   1997 O  O   B LEU A 1 141 ? 20.93800 50.28700 4.13100   0.330 41.48000  ?  141 LEU A O   1 
ATOM   1998 C  CB  A LEU A 1 141 ? 22.77800 47.52100 4.20900   0.670 43.79000  ?  141 LEU A CB  1 
ATOM   1999 C  CB  B LEU A 1 141 ? 21.89200 47.00900 4.27000   0.330 37.96000  ?  141 LEU A CB  1 
ATOM   2000 C  CG  A LEU A 1 141 ? 24.00500 46.76700 4.71800   0.670 40.81000  ?  141 LEU A CG  1 
ATOM   2001 C  CG  B LEU A 1 141 ? 23.30300 46.45700 4.25400   0.330 38.06000  ?  141 LEU A CG  1 
ATOM   2002 C  CD1 A LEU A 1 141 ? 24.03600 45.37900 4.10500   0.670 41.70000  ?  141 LEU A CD1 1 
ATOM   2003 C  CD1 B LEU A 1 141 ? 23.34000 45.16500 3.53500   0.330 35.29000  ?  141 LEU A CD1 1 
ATOM   2004 C  CD2 A LEU A 1 141 ? 25.26200 47.54900 4.40400   0.670 47.18000  ?  141 LEU A CD2 1 
ATOM   2005 C  CD2 B LEU A 1 141 ? 24.30400 47.41600 3.63800   0.330 46.80000  ?  141 LEU A CD2 1 
ATOM   2006 N  N   A VAL A 1 142 ? 20.15200 49.18800 4.07400   0.670 43.30000  ?  142 VAL A N   1 
ATOM   2007 N  N   B VAL A 1 142 ? 19.39200 48.67300 4.28400   0.330 44.40000  ?  142 VAL A N   1 
ATOM   2008 C  CA  A VAL A 1 142 ? 19.20400 49.90100 3.22800   0.670 47.16000  ?  142 VAL A CA  1 
ATOM   2009 C  CA  B VAL A 1 142 ? 18.34900 49.51000 3.68400   0.330 42.41000  ?  142 VAL A CA  1 
ATOM   2010 C  C   A VAL A 1 142 ? 18.62000 51.12700 3.90900   0.670 43.40000  ?  142 VAL A C   1 
ATOM   2011 C  C   B VAL A 1 142 ? 18.10300 50.77600 4.48500   0.330 46.59000  ?  142 VAL A C   1 
ATOM   2012 O  O   A VAL A 1 142 ? 18.18500 52.05500 3.21600   0.670 54.51000  ?  142 VAL A O   1 
ATOM   2013 O  O   B VAL A 1 142 ? 17.88300 51.84300 3.90200   0.330 52.41000  ?  142 VAL A O   1 
ATOM   2014 C  CB  A VAL A 1 142 ? 18.08600 48.93600 2.79900   0.670 39.59000  ?  142 VAL A CB  1 
ATOM   2015 C  CB  B VAL A 1 142 ? 17.04900 48.71800 3.54300   0.330 35.44000  ?  142 VAL A CB  1 
ATOM   2016 C  CG1 A VAL A 1 142 ? 16.89500 49.68700 2.24500   0.670 47.38000  ?  142 VAL A CG1 1 
ATOM   2017 C  CG1 B VAL A 1 142 ? 15.88600 49.67100 3.43800   0.330 42.68000  ?  142 VAL A CG1 1 
ATOM   2018 C  CG2 A VAL A 1 142 ? 18.62300 47.93800 1.77700   0.670 39.06000  ?  142 VAL A CG2 1 
ATOM   2019 C  CG2 B VAL A 1 142 ? 17.14400 47.91200 2.34500   0.330 35.47000  ?  142 VAL A CG2 1 
ATOM   2020 N  N   A GLY A 1 143 ? 18.61500 51.16900 5.23800   0.670 48.43000  ?  143 GLY A N   1 
ATOM   2021 N  N   B GLY A 1 143 ? 18.00900 50.66500 5.82400   0.330 44.13000  ?  143 GLY A N   1 
ATOM   2022 C  CA  A GLY A 1 143 ? 17.99600 52.25300 5.95900   0.670 49.72000  ?  143 GLY A CA  1 
ATOM   2023 C  CA  B GLY A 1 143 ? 17.44200 51.73900 6.60800   0.330 44.47000  ?  143 GLY A CA  1 
ATOM   2024 C  C   A GLY A 1 143 ? 18.99200 53.17800 6.62400   0.670 50.89000  ?  143 GLY A C   1 
ATOM   2025 C  C   B GLY A 1 143 ? 18.46600 52.80300 6.94100   0.330 49.59000  ?  143 GLY A C   1 
ATOM   2026 O  O   A GLY A 1 143 ? 19.54400 54.09000 5.99900   0.670 57.85000  ?  143 GLY A O   1 
ATOM   2027 O  O   B GLY A 1 143 ? 19.04300 53.46300 6.07300   0.330 51.74000  ?  143 GLY A O   1 
ATOM   2028 N  N   A PRO A 1 144 ? 19.23100 52.96100 7.92200   0.670 44.52000  ?  144 PRO A N   1 
ATOM   2029 N  N   B PRO A 1 144 ? 18.70800 52.95200 8.21900   0.330 46.07000  ?  144 PRO A N   1 
ATOM   2030 C  CA  A PRO A 1 144 ? 20.10700 53.88500 8.66600   0.670 53.08000  ?  144 PRO A CA  1 
ATOM   2031 C  CA  B PRO A 1 144 ? 19.85200 53.70400 8.75100   0.330 51.99000  ?  144 PRO A CA  1 
ATOM   2032 C  C   A PRO A 1 144 ? 21.41200 54.22200 7.96000   0.670 53.04000  ?  144 PRO A C   1 
ATOM   2033 C  C   B PRO A 1 144 ? 20.96700 54.11600 7.81000   0.330 53.37000  ?  144 PRO A C   1 
ATOM   2034 O  O   A PRO A 1 144 ? 21.80500 55.39500 7.93500   0.670 56.74000  ?  144 PRO A O   1 
ATOM   2035 O  O   B PRO A 1 144 ? 21.24900 55.30900 7.65200   0.330 56.09000  ?  144 PRO A O   1 
ATOM   2036 C  CB  A PRO A 1 144 ? 20.35200 53.13900 9.98500   0.670 44.58000  ?  144 PRO A CB  1 
ATOM   2037 C  CB  B PRO A 1 144 ? 20.40200 52.72700 9.79400   0.330 43.28000  ?  144 PRO A CB  1 
ATOM   2038 C  CG  A PRO A 1 144 ? 19.11600 52.31200 10.18200  0.670 48.39000  ?  144 PRO A CG  1 
ATOM   2039 C  CG  B PRO A 1 144 ? 19.20400 52.10500 10.28200  0.330 49.01000  ?  144 PRO A CG  1 
ATOM   2040 C  CD  A PRO A 1 144 ? 18.61400 51.94500 8.80300   0.670 44.62000  ?  144 PRO A CD  1 
ATOM   2041 C  CD  B PRO A 1 144 ? 18.18500 52.03300 9.21400   0.330 45.71000  ?  144 PRO A CD  1 
ATOM   2042 N  N   A MET A 1 145 ? 22.10400 53.23300 7.39200   0.670 53.89000  ?  145 MET A N   1 
ATOM   2043 N  N   B MET A 1 145 ? 21.64300 53.14000 7.21800   0.330 52.00000  ?  145 MET A N   1 
ATOM   2044 C  CA  A MET A 1 145 ? 23.36700 53.52600 6.72300   0.670 52.45000  ?  145 MET A CA  1 
ATOM   2045 C  CA  B MET A 1 145 ? 22.82900 53.48700 6.47100   0.330 51.98000  ?  145 MET A CA  1 
ATOM   2046 C  C   A MET A 1 145 ? 23.15000 54.35400 5.46500   0.670 53.52000  ?  145 MET A C   1 
ATOM   2047 C  C   B MET A 1 145 ? 22.44600 54.23400 5.21600   0.330 50.06000  ?  145 MET A C   1 
ATOM   2048 O  O   A MET A 1 145 ? 24.00200 55.17800 5.11300   0.670 52.18000  ?  145 MET A O   1 
ATOM   2049 O  O   B MET A 1 145 ? 23.25100 55.01900 4.70900   0.330 52.42000  ?  145 MET A O   1 
ATOM   2050 C  CB  A MET A 1 145 ? 24.09800 52.22200 6.40500   0.670 42.74000  ?  145 MET A CB  1 
ATOM   2051 C  CB  B MET A 1 145 ? 23.59300 52.22800 6.13500   0.330 46.79000  ?  145 MET A CB  1 
ATOM   2052 C  CG  A MET A 1 145 ? 24.49200 51.45400 7.66000   0.670 48.13000  ?  145 MET A CG  1 
ATOM   2053 C  CG  B MET A 1 145 ? 23.56900 51.20600 7.20400   0.330 39.34000  ?  145 MET A CG  1 
ATOM   2054 S  SD  A MET A 1 145 ? 25.43000 49.94200 7.37200   0.670 47.03000  ?  145 MET A SD  1 
ATOM   2055 S  SD  B MET A 1 145 ? 24.65300 50.10100 6.43900   0.330 49.93000  ?  145 MET A SD  1 
ATOM   2056 C  CE  A MET A 1 145 ? 26.77800 50.56000 6.37300   0.670 39.78000  ?  145 MET A CE  1 
ATOM   2057 C  CE  B MET A 1 145 ? 26.05500 51.17600 6.25800   0.330 47.24000  ?  145 MET A CE  1 
ATOM   2058 N  N   A THR A 1 146 ? 22.01700 54.16700 4.78400   0.670 47.97000  ?  146 THR A N   1 
ATOM   2059 N  N   B THR A 1 146 ? 21.20800 54.05100 4.74700   0.330 49.37000  ?  146 THR A N   1 
ATOM   2060 C  CA  A THR A 1 146 ? 21.73500 54.97700 3.60400   0.670 57.48000  ?  146 THR A CA  1 
ATOM   2061 C  CA  B THR A 1 146 ? 20.75200 54.74800 3.55300   0.330 54.89000  ?  146 THR A CA  1 
ATOM   2062 C  C   A THR A 1 146 ? 21.37000 56.40500 3.99400   0.670 57.89000  ?  146 THR A C   1 
ATOM   2063 C  C   B THR A 1 146 ? 20.64200 56.22400 3.84300   0.330 55.93000  ?  146 THR A C   1 
ATOM   2064 O  O   A THR A 1 146 ? 21.80400 57.36200 3.34300   0.670 67.90000  ?  146 THR A O   1 
ATOM   2065 O  O   B THR A 1 146 ? 21.32300 57.04700 3.21800   0.330 63.67000  ?  146 THR A O   1 
ATOM   2066 C  CB  A THR A 1 146 ? 20.62000 54.33800 2.77800   0.670 55.80000  ?  146 THR A CB  1 
ATOM   2067 C  CB  B THR A 1 146 ? 19.39900 54.22300 3.10700   0.330 52.60000  ?  146 THR A CB  1 
ATOM   2068 O  OG1 A THR A 1 146 ? 21.03700 53.03300 2.35700   0.670 37.33000  ?  146 THR A OG1 1 
ATOM   2069 O  OG1 B THR A 1 146 ? 19.51200 52.83800 2.76900   0.330 44.87000  ?  146 THR A OG1 1 
ATOM   2070 C  CG2 A THR A 1 146 ? 20.30300 55.19200 1.55600   0.670 42.00000  ?  146 THR A CG2 1 
ATOM   2071 C  CG2 B THR A 1 146 ? 18.91500 55.00200 1.87900   0.330 46.50000  ?  146 THR A CG2 1 
ATOM   2072 N  N   A GLU A 1 147 ? 20.57500 56.57300 5.05500   0.670 58.88000  ?  147 GLU A N   1 
ATOM   2073 N  N   B GLU A 1 147 ? 19.74100 56.55700 4.76600   0.330 57.76000  ?  147 GLU A N   1 
ATOM   2074 C  CA  A GLU A 1 147 ? 20.33500 57.91300 5.58100   0.670 60.19000  ?  147 GLU A CA  1 
ATOM   2075 C  CA  B GLU A 1 147 ? 19.78400 57.77300 5.55900   0.330 60.19000  ?  147 GLU A CA  1 
ATOM   2076 C  C   A GLU A 1 147 ? 21.65800 58.60600 5.87700   0.670 55.80000  ?  147 GLU A C   1 
ATOM   2077 C  C   B GLU A 1 147 ? 21.21900 58.21300 5.74800   0.330 58.64000  ?  147 GLU A C   1 
ATOM   2078 O  O   A GLU A 1 147 ? 21.86500 59.77100 5.51200   0.670 60.90000  ?  147 GLU A O   1 
ATOM   2079 O  O   B GLU A 1 147 ? 21.71800 59.12100 5.07400   0.330 59.38000  ?  147 GLU A O   1 
ATOM   2080 C  CB  A GLU A 1 147 ? 19.45800 57.84800 6.83900   0.670 59.75000  ?  147 GLU A CB  1 
ATOM   2081 C  CB  B GLU A 1 147 ? 19.15600 57.48300 6.91700   0.330 62.04000  ?  147 GLU A CB  1 
ATOM   2082 C  CG  A GLU A 1 147 ? 18.07900 57.22000 6.63600   0.670 69.31000  ?  147 GLU A CG  1 
ATOM   2083 C  CG  B GLU A 1 147 ? 17.82500 56.74700 6.77400   0.330 68.24000  ?  147 GLU A CG  1 
ATOM   2084 C  CD  A GLU A 1 147 ? 16.99900 57.87700 7.48400   0.670 94.23000  ?  147 GLU A CD  1 
ATOM   2085 C  CD  B GLU A 1 147 ? 16.87400 56.97600 7.94400   0.330 83.82000  ?  147 GLU A CD  1 
ATOM   2086 O  OE1 A GLU A 1 147 ? 16.49500 58.94500 7.08000   0.670 107.97000 ?  147 GLU A OE1 1 
ATOM   2087 O  OE1 B GLU A 1 147 ? 16.34300 58.10300 8.09600   0.330 100.17000 ?  147 GLU A OE1 1 
ATOM   2088 O  OE2 A GLU A 1 147 ? 16.65500 57.32900 8.55300   0.670 91.93000  -1 147 GLU A OE2 1 
ATOM   2089 O  OE2 B GLU A 1 147 ? 16.61400 55.99300 8.68300   0.330 76.85000  -1 147 GLU A OE2 1 
ATOM   2090 N  N   A SER A 1 148 ? 22.57200 57.89400 6.54400   0.670 51.49000  ?  148 SER A N   1 
ATOM   2091 N  N   B SER A 1 148 ? 21.89500 57.50800 6.65000   0.330 56.13000  ?  148 SER A N   1 
ATOM   2092 C  CA  A SER A 1 148 ? 23.84000 58.49700 6.94200   0.670 52.17000  ?  148 SER A CA  1 
ATOM   2093 C  CA  B SER A 1 148 ? 23.19100 57.94700 7.12500   0.330 54.22000  ?  148 SER A CA  1 
ATOM   2094 C  C   A SER A 1 148 ? 24.68400 58.86200 5.72300   0.670 61.95000  ?  148 SER A C   1 
ATOM   2095 C  C   B SER A 1 148 ? 24.07600 58.33400 5.96200   0.330 58.15000  ?  148 SER A C   1 
ATOM   2096 O  O   A SER A 1 148 ? 25.23700 59.96600 5.64500   0.670 57.33000  ?  148 SER A O   1 
ATOM   2097 O  O   B SER A 1 148 ? 24.99800 59.13500 6.13000   0.330 62.25000  ?  148 SER A O   1 
ATOM   2098 C  CB  A SER A 1 148 ? 24.59800 57.54600 7.87100   0.670 43.08000  ?  148 SER A CB  1 
ATOM   2099 C  CB  B SER A 1 148 ? 23.80400 56.86500 8.00300   0.330 50.18000  ?  148 SER A CB  1 
ATOM   2100 O  OG  A SER A 1 148 ? 25.98200 57.84700 7.90800   0.670 72.47000  ?  148 SER A OG  1 
ATOM   2101 O  OG  B SER A 1 148 ? 25.15000 57.09300 8.30600   0.330 53.53000  ?  148 SER A OG  1 
ATOM   2102 N  N   A ALA A 1 149 ? 24.79400 57.94700 4.75700   0.670 63.12000  ?  149 ALA A N   1 
ATOM   2103 N  N   B ALA A 1 149 ? 23.75500 57.86300 4.75700   0.330 55.86000  ?  149 ALA A N   1 
ATOM   2104 C  CA  A ALA A 1 149 ? 25.55800 58.23700 3.54800   0.670 60.82000  ?  149 ALA A CA  1 
ATOM   2105 C  CA  B ALA A 1 149 ? 24.55300 58.19500 3.58800   0.330 58.97000  ?  149 ALA A CA  1 
ATOM   2106 C  C   A ALA A 1 149 ? 25.01600 59.44800 2.80100   0.670 60.91000  ?  149 ALA A C   1 
ATOM   2107 C  C   B ALA A 1 149 ? 23.89100 59.18700 2.63800   0.330 62.73000  ?  149 ALA A C   1 
ATOM   2108 O  O   A ALA A 1 149 ? 25.74400 60.05000 2.00300   0.670 63.59000  ?  149 ALA A O   1 
ATOM   2109 O  O   B ALA A 1 149 ? 24.60100 59.92900 1.94600   0.330 60.10000  ?  149 ALA A O   1 
ATOM   2110 C  CB  A ALA A 1 149 ? 25.55800 57.02300 2.61600   0.670 52.10000  ?  149 ALA A CB  1 
ATOM   2111 C  CB  B ALA A 1 149 ? 24.91800 56.93200 2.81900   0.330 56.00000  ?  149 ALA A CB  1 
ATOM   2112 N  N   A SER A 1 150 ? 23.75600 59.81600 3.03700   0.670 63.28000  ?  150 SER A N   1 
ATOM   2113 N  N   B SER A 1 150 ? 22.56900 59.26100 2.59500   0.330 58.11000  ?  150 SER A N   1 
ATOM   2114 C  CA  A SER A 1 150 ? 23.17200 60.94300 2.32100   0.670 68.17000  ?  150 SER A CA  1 
ATOM   2115 C  CA  B SER A 1 150 ? 21.97600 60.45900 2.03800   0.330 60.59000  ?  150 SER A CA  1 
ATOM   2116 C  C   A SER A 1 150 ? 23.86100 62.25400 2.67200   0.670 72.06000  ?  150 SER A C   1 
ATOM   2117 C  C   B SER A 1 150 ? 22.46400 61.73900 2.75900   0.330 68.02000  ?  150 SER A C   1 
ATOM   2118 O  O   A SER A 1 150 ? 23.88000 63.18000 1.85200   0.670 84.45000  ?  150 SER A O   1 
ATOM   2119 O  O   B SER A 1 150 ? 21.81400 62.78500 2.64900   0.330 68.81000  ?  150 SER A O   1 
ATOM   2120 C  CB  A SER A 1 150 ? 21.67700 61.03600 2.62600   0.670 65.08000  ?  150 SER A CB  1 
ATOM   2121 C  CB  B SER A 1 150 ? 20.45600 60.32000 2.08600   0.330 60.45000  ?  150 SER A CB  1 
ATOM   2122 O  OG  A SER A 1 150 ? 21.43800 61.91600 3.71100   0.670 64.63000  ?  150 SER A OG  1 
ATOM   2123 O  OG  B SER A 1 150 ? 19.94500 60.76000 3.33600   0.330 57.55000  ?  150 SER A OG  1 
ATOM   2124 N  N   A GLN A 1 151 ? 24.43200 62.35500 3.87300   0.670 67.36000  ?  151 GLN A N   1 
ATOM   2125 N  N   B GLN A 1 151 ? 23.61700 61.67100 3.48900   0.330 68.38000  ?  151 GLN A N   1 
ATOM   2126 C  CA  A GLN A 1 151 ? 25.08000 63.59000 4.29700   0.670 72.08000  ?  151 GLN A CA  1 
ATOM   2127 C  CA  B GLN A 1 151 ? 24.33800 62.82000 4.07400   0.330 68.98000  ?  151 GLN A CA  1 
ATOM   2128 C  C   A GLN A 1 151 ? 26.40200 63.84600 3.58200   0.670 68.56000  ?  151 GLN A C   1 
ATOM   2129 C  C   B GLN A 1 151 ? 25.55600 63.30600 3.27200   0.330 66.63000  ?  151 GLN A C   1 
ATOM   2130 O  O   A GLN A 1 151 ? 27.01200 64.89600 3.80200   0.670 65.71000  ?  151 GLN A O   1 
ATOM   2131 O  O   B GLN A 1 151 ? 25.88500 64.49200 3.37700   0.330 70.11000  ?  151 GLN A O   1 
ATOM   2132 C  CB  A GLN A 1 151 ? 25.32100 63.56700 5.80900   0.670 73.92000  ?  151 GLN A CB  1 
ATOM   2133 C  CB  B GLN A 1 151 ? 24.92000 62.53400 5.48800   0.330 75.38000  ?  151 GLN A CB  1 
ATOM   2134 C  CG  A GLN A 1 151 ? 24.12000 63.13900 6.64200   0.670 68.27000  ?  151 GLN A CG  1 
ATOM   2135 C  CG  B GLN A 1 151 ? 24.03800 62.06900 6.67200   0.330 72.69000  ?  151 GLN A CG  1 
ATOM   2136 C  CD  A GLN A 1 151 ? 22.90300 64.01100 6.40700   0.670 87.64000  ?  151 GLN A CD  1 
ATOM   2137 C  CD  B GLN A 1 151 ? 23.11600 63.12200 7.23400   0.330 83.67000  ?  151 GLN A CD  1 
ATOM   2138 O  OE1 A GLN A 1 151 ? 22.36500 64.05800 5.30100   0.670 93.71000  ?  151 GLN A OE1 1 
ATOM   2139 O  OE1 B GLN A 1 151 ? 22.27100 63.66100 6.52300   0.330 89.92000  ?  151 GLN A OE1 1 
ATOM   2140 N  NE2 A GLN A 1 151 ? 22.45800 64.70400 7.45000   0.670 94.50000  ?  151 GLN A NE2 1 
ATOM   2141 N  NE2 B GLN A 1 151 ? 23.22600 63.37100 8.55200   0.330 85.16000  ?  151 GLN A NE2 1 
ATOM   2142 N  N   A ARG A 1 152 ? 26.86600 62.93400 2.74100   0.670 60.51000  ?  152 ARG A N   1 
ATOM   2143 N  N   B ARG A 1 152 ? 26.29700 62.43100 2.56400   0.330 60.84000  ?  152 ARG A N   1 
ATOM   2144 C  CA  A ARG A 1 152 ? 28.15700 63.07500 2.08800   0.670 70.68000  ?  152 ARG A CA  1 
ATOM   2145 C  CA  B ARG A 1 152 ? 27.62000 62.77200 2.02400   0.330 67.80000  ?  152 ARG A CA  1 
ATOM   2146 C  C   A ARG A 1 152 ? 27.98000 63.64000 0.68200   0.670 69.49000  ?  152 ARG A C   1 
ATOM   2147 C  C   B ARG A 1 152 ? 27.54200 63.50200 0.66600   0.330 69.11000  ?  152 ARG A C   1 
ATOM   2148 O  O   A ARG A 1 152 ? 26.86500 63.82300 0.18900   0.670 68.33000  ?  152 ARG A O   1 
ATOM   2149 O  O   B ARG A 1 152 ? 26.45700 63.82500 0.15700   0.330 67.92000  ?  152 ARG A O   1 
ATOM   2150 C  CB  A ARG A 1 152 ? 28.88400 61.72600 2.04600   0.670 72.46000  ?  152 ARG A CB  1 
ATOM   2151 C  CB  B ARG A 1 152 ? 28.49700 61.51700 1.89900   0.330 70.71000  ?  152 ARG A CB  1 
ATOM   2152 C  CG  A ARG A 1 152 ? 28.89900 60.99300 3.38300   0.670 62.62000  ?  152 ARG A CG  1 
ATOM   2153 C  CG  B ARG A 1 152 ? 28.69500 60.69600 3.12800   0.330 64.41000  ?  152 ARG A CG  1 
ATOM   2154 C  CD  A ARG A 1 152 ? 30.18000 61.26600 4.16700   0.670 70.98000  ?  152 ARG A CD  1 
ATOM   2155 C  CD  B ARG A 1 152 ? 30.03300 60.92600 3.79800   0.330 68.78000  ?  152 ARG A CD  1 
ATOM   2156 N  NE  A ARG A 1 152 ? 31.22200 60.28700 3.86500   0.670 79.35000  ?  152 ARG A NE  1 
ATOM   2157 N  NE  B ARG A 1 152 ? 31.02700 59.94700 3.35700   0.330 75.83000  ?  152 ARG A NE  1 
ATOM   2158 C  CZ  A ARG A 1 152 ? 32.47900 60.37100 4.28700   0.670 87.06000  ?  152 ARG A CZ  1 
ATOM   2159 C  CZ  B ARG A 1 152 ? 32.27600 59.87000 3.81400   0.330 81.82000  ?  152 ARG A CZ  1 
ATOM   2160 N  NH1 A ARG A 1 152 ? 32.86500 61.39200 5.03900   0.670 94.44000  ?  152 ARG A NH1 1 
ATOM   2161 N  NH1 B ARG A 1 152 ? 32.70700 60.64900 4.79800   0.330 88.32000  ?  152 ARG A NH1 1 
ATOM   2162 N  NH2 A ARG A 1 152 ? 33.35300 59.43100 3.95500   0.670 86.61000  ?  152 ARG A NH2 1 
ATOM   2163 N  NH2 B ARG A 1 152 ? 33.10500 58.95800 3.30000   0.330 80.91000  ?  152 ARG A NH2 1 
ATOM   2164 N  N   A SER A 1 153 ? 29.11200 63.93100 0.04100   0.670 60.19000  ?  153 SER A N   1 
ATOM   2165 N  N   B SER A 1 153 ? 28.71500 63.77500 0.06100   0.330 64.80000  ?  153 SER A N   1 
ATOM   2166 C  CA  A SER A 1 153 ? 29.10800 64.46600 -1.31500  0.670 67.53000  ?  153 SER A CA  1 
ATOM   2167 C  CA  B SER A 1 153 ? 28.73400 64.30900 -1.29800  0.330 67.67000  ?  153 SER A CA  1 
ATOM   2168 C  C   A SER A 1 153 ? 28.27400 63.57200 -2.22300  0.670 63.64000  ?  153 SER A C   1 
ATOM   2169 C  C   B SER A 1 153 ? 27.98500 63.35100 -2.21900  0.330 65.72000  ?  153 SER A C   1 
ATOM   2170 O  O   A SER A 1 153 ? 28.02400 62.41000 -1.89700  0.670 74.20000  ?  153 SER A O   1 
ATOM   2171 O  O   B SER A 1 153 ? 28.02500 62.12400 -2.05600  0.330 72.88000  ?  153 SER A O   1 
ATOM   2172 C  CB  A SER A 1 153 ? 30.53300 64.58300 -1.85100  0.670 69.89000  ?  153 SER A CB  1 
ATOM   2173 C  CB  B SER A 1 153 ? 30.17400 64.52500 -1.79600  0.330 69.56000  ?  153 SER A CB  1 
ATOM   2174 O  OG  A SER A 1 153 ? 31.02300 63.31700 -2.25600  0.670 71.36000  ?  153 SER A OG  1 
ATOM   2175 O  OG  B SER A 1 153 ? 30.73600 63.38900 -2.44300  0.330 71.58000  ?  153 SER A OG  1 
ATOM   2176 N  N   A SER A 1 154 ? 27.83600 64.09700 -3.36600  0.670 76.37000  ?  154 SER A N   1 
ATOM   2177 N  N   B SER A 1 154 ? 27.25000 63.91500 -3.16800  0.330 73.25000  ?  154 SER A N   1 
ATOM   2178 C  CA  A SER A 1 154 ? 26.99000 63.30400 -4.24900  0.670 74.45000  ?  154 SER A CA  1 
ATOM   2179 C  CA  B SER A 1 154 ? 26.33300 63.09300 -3.95400  0.330 69.19000  ?  154 SER A CA  1 
ATOM   2180 C  C   A SER A 1 154 ? 27.75800 62.13000 -4.83900  0.670 75.09000  ?  154 SER A C   1 
ATOM   2181 C  C   B SER A 1 154 ? 27.06700 62.02700 -4.78100  0.330 71.32000  ?  154 SER A C   1 
ATOM   2182 O  O   A SER A 1 154 ? 27.15900 61.08300 -5.12600  0.670 59.37000  ?  154 SER A O   1 
ATOM   2183 O  O   B SER A 1 154 ? 26.53500 60.92800 -4.98700  0.330 62.59000  ?  154 SER A O   1 
ATOM   2184 C  CB  A SER A 1 154 ? 26.39900 64.19700 -5.34300  0.670 68.14000  ?  154 SER A CB  1 
ATOM   2185 C  CB  B SER A 1 154 ? 25.48500 63.99100 -4.83500  0.330 74.28000  ?  154 SER A CB  1 
ATOM   2186 O  OG  A SER A 1 154 ? 25.17900 63.65100 -5.82300  0.670 82.66000  ?  154 SER A OG  1 
ATOM   2187 O  OG  B SER A 1 154 ? 24.22200 63.41200 -5.04100  0.330 79.50000  ?  154 SER A OG  1 
ATOM   2188 N  N   A GLY A 1 155 ? 29.07100 62.27900 -5.03400  0.670 72.61000  ?  155 GLY A N   1 
ATOM   2189 N  N   B GLY A 1 155 ? 28.28400 62.31600 -5.25100  0.330 72.88000  ?  155 GLY A N   1 
ATOM   2190 C  CA  A GLY A 1 155 ? 29.84400 61.18100 -5.59100  0.670 69.07000  ?  155 GLY A CA  1 
ATOM   2191 C  CA  B GLY A 1 155 ? 29.14700 61.23400 -5.69100  0.330 67.96000  ?  155 GLY A CA  1 
ATOM   2192 C  C   A GLY A 1 155 ? 30.07000 60.05300 -4.59600  0.670 71.54000  ?  155 GLY A C   1 
ATOM   2193 C  C   B GLY A 1 155 ? 29.13700 60.08600 -4.70600  0.330 65.29000  ?  155 GLY A C   1 
ATOM   2194 O  O   A GLY A 1 155 ? 30.03200 58.87400 -4.95800  0.670 73.48000  ?  155 GLY A O   1 
ATOM   2195 O  O   B GLY A 1 155 ? 28.57000 59.02700 -4.98400  0.330 62.91000  ?  155 GLY A O   1 
ATOM   2196 N  N   A ILE A 1 156 ? 30.32400 60.39700 -3.33200  0.670 68.03000  ?  156 ILE A N   1 
ATOM   2197 N  N   B ILE A 1 156 ? 29.69700 60.32000 -3.51000  0.330 68.16000  ?  156 ILE A N   1 
ATOM   2198 C  CA  A ILE A 1 156 ? 30.46500 59.37500 -2.29700  0.670 65.73000  ?  156 ILE A CA  1 
ATOM   2199 C  CA  B ILE A 1 156 ? 29.76200 59.30900 -2.45500  0.330 65.90000  ?  156 ILE A CA  1 
ATOM   2200 C  C   A ILE A 1 156 ? 29.14500 58.64000 -2.09900  0.670 62.89000  ?  156 ILE A C   1 
ATOM   2201 C  C   B ILE A 1 156 ? 28.36800 58.77100 -2.11800  0.330 60.43000  ?  156 ILE A C   1 
ATOM   2202 O  O   A ILE A 1 156 ? 29.10600 57.40700 -2.02100  0.670 61.83000  ?  156 ILE A O   1 
ATOM   2203 O  O   B ILE A 1 156 ? 28.20800 57.57600 -1.86400  0.330 56.20000  ?  156 ILE A O   1 
ATOM   2204 C  CB  A ILE A 1 156 ? 30.95800 60.00900 -0.98400  0.670 69.69000  ?  156 ILE A CB  1 
ATOM   2205 C  CB  B ILE A 1 156 ? 30.49200 59.89100 -1.22700  0.330 66.87000  ?  156 ILE A CB  1 
ATOM   2206 C  CG1 A ILE A 1 156 ? 32.39200 60.52200 -1.14600  0.670 75.30000  ?  156 ILE A CG1 1 
ATOM   2207 C  CG1 B ILE A 1 156 ? 31.99900 60.05400 -1.51500  0.330 69.92000  ?  156 ILE A CG1 1 
ATOM   2208 C  CG2 A ILE A 1 156 ? 30.86100 59.01000 0.16300   0.670 64.36000  ?  156 ILE A CG2 1 
ATOM   2209 C  CG2 B ILE A 1 156 ? 30.30900 59.00500 -0.01500  0.330 63.98000  ?  156 ILE A CG2 1 
ATOM   2210 C  CD1 A ILE A 1 156 ? 33.45900 59.50500 -0.79400  0.670 75.53000  ?  156 ILE A CD1 1 
ATOM   2211 C  CD1 B ILE A 1 156 ? 32.95700 59.01300 -0.85700  0.330 70.38000  ?  156 ILE A CD1 1 
ATOM   2212 N  N   A LYS A 1 157 ? 28.04400 59.38900 -2.01200  0.670 58.34000  ?  157 LYS A N   1 
ATOM   2213 N  N   B LYS A 1 157 ? 27.32500 59.58300 -2.17800  0.330 56.54000  ?  157 LYS A N   1 
ATOM   2214 C  CA  A LYS A 1 157 ? 26.73500 58.76100 -1.87400  0.670 55.56000  ?  157 LYS A CA  1 
ATOM   2215 C  CA  B LYS A 1 157 ? 26.04900 58.96400 -1.88300  0.330 56.27000  ?  157 LYS A CA  1 
ATOM   2216 C  C   A LYS A 1 157 ? 26.46800 57.80400 -3.02700  0.670 57.34000  ?  157 LYS A C   1 
ATOM   2217 C  C   B LYS A 1 157 ? 25.53800 58.07700 -3.02300  0.330 59.34000  ?  157 LYS A C   1 
ATOM   2218 O  O   A LYS A 1 157 ? 25.94500 56.70300 -2.82200  0.670 51.28000  ?  157 LYS A O   1 
ATOM   2219 O  O   B LYS A 1 157 ? 24.77300 57.13800 -2.77100  0.330 52.97000  ?  157 LYS A O   1 
ATOM   2220 C  CB  A LYS A 1 157 ? 25.65300 59.83700 -1.79700  0.670 49.49000  ?  157 LYS A CB  1 
ATOM   2221 C  CB  B LYS A 1 157 ? 25.00700 60.00300 -1.53800  0.330 60.00000  ?  157 LYS A CB  1 
ATOM   2222 C  CG  A LYS A 1 157 ? 24.23400 59.30200 -1.73800  0.670 59.16000  ?  157 LYS A CG  1 
ATOM   2223 C  CG  B LYS A 1 157 ? 23.80000 59.28500 -0.91500  0.330 63.41000  ?  157 LYS A CG  1 
ATOM   2224 C  CD  A LYS A 1 157 ? 23.30200 60.11600 -2.63200  0.670 70.87000  ?  157 LYS A CD  1 
ATOM   2225 C  CD  B LYS A 1 157 ? 22.58000 59.52700 -1.68900  0.330 63.04000  ?  157 LYS A CD  1 
ATOM   2226 C  CE  A LYS A 1 157 ? 23.07600 61.51800 -2.08200  0.670 82.46000  ?  157 LYS A CE  1 
ATOM   2227 C  CE  B LYS A 1 157 ? 22.50400 61.00200 -1.85600  0.330 80.05000  ?  157 LYS A CE  1 
ATOM   2228 N  NZ  A LYS A 1 157 ? 21.70800 62.02300 -2.39000  0.670 98.64000  ?  157 LYS A NZ  1 
ATOM   2229 N  NZ  B LYS A 1 157 ? 21.11300 61.44400 -1.92300  0.330 92.12000  ?  157 LYS A NZ  1 
ATOM   2230 N  N   A SER A 1 158 ? 26.83000 58.20400 -4.24900  0.670 69.62000  ?  158 SER A N   1 
ATOM   2231 N  N   B SER A 1 158 ? 25.95500 58.32300 -4.27400  0.330 66.75000  ?  158 SER A N   1 
ATOM   2232 C  CA  A SER A 1 158 ? 26.60100 57.35000 -5.41000  0.670 57.94000  ?  158 SER A CA  1 
ATOM   2233 C  CA  B SER A 1 158 ? 25.52200 57.45000 -5.37300  0.330 56.97000  ?  158 SER A CA  1 
ATOM   2234 C  C   A SER A 1 158 ? 27.42000 56.06800 -5.32200  0.670 51.97000  ?  158 SER A C   1 
ATOM   2235 C  C   B SER A 1 158 ? 26.29800 56.15600 -5.38500  0.330 50.24000  ?  158 SER A C   1 
ATOM   2236 O  O   A SER A 1 158 ? 26.92000 54.97800 -5.62500  0.670 42.86000  ?  158 SER A O   1 
ATOM   2237 O  O   B SER A 1 158 ? 25.69300 55.08100 -5.55000  0.330 38.51000  ?  158 SER A O   1 
ATOM   2238 C  CB  A SER A 1 158 ? 26.93900 58.11900 -6.68800  0.670 52.91000  ?  158 SER A CB  1 
ATOM   2239 C  CB  B SER A 1 158 ? 25.65400 58.14000 -6.73700  0.330 56.77000  ?  158 SER A CB  1 
ATOM   2240 O  OG  A SER A 1 158 ? 26.76800 57.31300 -7.84100  0.670 64.44000  ?  158 SER A OG  1 
ATOM   2241 O  OG  B SER A 1 158 ? 25.21800 57.27100 -7.77200  0.330 59.26000  ?  158 SER A OG  1 
ATOM   2242 N  N   A LEU A 1 159 ? 28.68500 56.17900 -4.91100  0.670 45.18000  ?  159 LEU A N   1 
ATOM   2243 N  N   B LEU A 1 159 ? 27.63300 56.27000 -5.25800  0.330 53.11000  ?  159 LEU A N   1 
ATOM   2244 C  CA  A LEU A 1 159 ? 29.51400 54.99200 -4.73900  0.670 47.56000  ?  159 LEU A CA  1 
ATOM   2245 C  CA  B LEU A 1 159 ? 28.45700 55.10200 -4.98700  0.330 48.99000  ?  159 LEU A CA  1 
ATOM   2246 C  C   A LEU A 1 159 ? 28.93900 54.07200 -3.67200  0.670 49.68000  ?  159 LEU A C   1 
ATOM   2247 C  C   B LEU A 1 159 ? 27.87000 54.27100 -3.82700  0.330 54.01000  ?  159 LEU A C   1 
ATOM   2248 O  O   A LEU A 1 159 ? 28.90400 52.84900 -3.85200  0.670 47.61000  ?  159 LEU A O   1 
ATOM   2249 O  O   B LEU A 1 159 ? 27.79200 53.04000 -3.94000  0.330 47.44000  ?  159 LEU A O   1 
ATOM   2250 C  CB  A LEU A 1 159 ? 30.94100 55.40200 -4.38000  0.670 51.14000  ?  159 LEU A CB  1 
ATOM   2251 C  CB  B LEU A 1 159 ? 29.92200 55.54700 -4.75700  0.330 49.66000  ?  159 LEU A CB  1 
ATOM   2252 C  CG  A LEU A 1 159 ? 31.96400 54.28300 -4.19400  0.670 49.84000  ?  159 LEU A CG  1 
ATOM   2253 C  CG  B LEU A 1 159 ? 31.21800 54.72300 -4.38800  0.330 50.47000  ?  159 LEU A CG  1 
ATOM   2254 C  CD1 A LEU A 1 159 ? 31.97600 53.37300 -5.41400  0.670 57.15000  ?  159 LEU A CD1 1 
ATOM   2255 C  CD1 B LEU A 1 159 ? 31.64800 53.51100 -5.27400  0.330 54.67000  ?  159 LEU A CD1 1 
ATOM   2256 C  CD2 A LEU A 1 159 ? 33.34700 54.86200 -3.93600  0.670 41.87000  ?  159 LEU A CD2 1 
ATOM   2257 C  CD2 B LEU A 1 159 ? 32.48100 55.61000 -4.13000  0.330 53.15000  ?  159 LEU A CD2 1 
ATOM   2258 N  N   A TYR A 1 160 ? 28.47900 54.63800 -2.55400  0.670 50.54000  ?  160 TYR A N   1 
ATOM   2259 N  N   B TYR A 1 160 ? 27.36000 54.91500 -2.74000  0.330 51.78000  ?  160 TYR A N   1 
ATOM   2260 C  CA  A TYR A 1 160 ? 27.90700 53.80400 -1.50300  0.670 49.93000  ?  160 TYR A CA  1 
ATOM   2261 C  CA  B TYR A 1 160 ? 26.78300 54.09700 -1.66200  0.330 46.05000  ?  160 TYR A CA  1 
ATOM   2262 C  C   A TYR A 1 160 ? 26.70400 53.02300 -2.02100  0.670 46.47000  ?  160 TYR A C   1 
ATOM   2263 C  C   B TYR A 1 160 ? 25.55200 53.34100 -2.11600  0.330 47.21000  ?  160 TYR A C   1 
ATOM   2264 O  O   A TYR A 1 160 ? 26.58100 51.81500 -1.78400  0.670 46.25000  ?  160 TYR A O   1 
ATOM   2265 O  O   B TYR A 1 160 ? 25.33300 52.20500 -1.67100  0.330 44.61000  ?  160 TYR A O   1 
ATOM   2266 C  CB  A TYR A 1 160 ? 27.49500 54.64900 -0.29800  0.670 51.60000  ?  160 TYR A CB  1 
ATOM   2267 C  CB  B TYR A 1 160 ? 26.38500 54.85800 -0.36700  0.330 51.84000  ?  160 TYR A CB  1 
ATOM   2268 C  CG  A TYR A 1 160 ? 26.69000 53.82800 0.68500   0.670 44.62000  ?  160 TYR A CG  1 
ATOM   2269 C  CG  B TYR A 1 160 ? 25.73000 53.86200 0.67900   0.330 43.22000  ?  160 TYR A CG  1 
ATOM   2270 C  CD1 A TYR A 1 160 ? 27.32300 52.97600 1.57800   0.670 40.27000  ?  160 TYR A CD1 1 
ATOM   2271 C  CD1 B TYR A 1 160 ? 26.53100 52.90600 1.34300   0.330 43.59000  ?  160 TYR A CD1 1 
ATOM   2272 C  CD2 A TYR A 1 160 ? 25.29900 53.86500 0.68900   0.670 42.21000  ?  160 TYR A CD2 1 
ATOM   2273 C  CD2 B TYR A 1 160 ? 24.34300 53.84100 0.98000   0.330 44.65000  ?  160 TYR A CD2 1 
ATOM   2274 C  CE1 A TYR A 1 160 ? 26.60500 52.20400 2.46200   0.670 34.72000  ?  160 TYR A CE1 1 
ATOM   2275 C  CE1 B TYR A 1 160 ? 25.99400 51.94800 2.25700   0.330 40.59000  ?  160 TYR A CE1 1 
ATOM   2276 C  CE2 A TYR A 1 160 ? 24.56800 53.08900 1.57600   0.670 48.27000  ?  160 TYR A CE2 1 
ATOM   2277 C  CE2 B TYR A 1 160 ? 23.78900 52.86600 1.92900   0.330 45.68000  ?  160 TYR A CE2 1 
ATOM   2278 C  CZ  A TYR A 1 160 ? 25.23200 52.26000 2.45900   0.670 43.24000  ?  160 TYR A CZ  1 
ATOM   2279 C  CZ  B TYR A 1 160 ? 24.65200 51.92200 2.54900   0.330 44.28000  ?  160 TYR A CZ  1 
ATOM   2280 O  OH  A TYR A 1 160 ? 24.53900 51.47900 3.35300   0.670 42.72000  ?  160 TYR A OH  1 
ATOM   2281 O  OH  B TYR A 1 160 ? 24.24100 50.93800 3.46800   0.330 40.05000  ?  160 TYR A OH  1 
ATOM   2282 N  N   A VAL A 1 161 ? 25.79800 53.70400 -2.72700  0.670 44.02000  ?  161 VAL A N   1 
ATOM   2283 N  N   B VAL A 1 161 ? 24.68400 53.95100 -2.92500  0.330 48.99000  ?  161 VAL A N   1 
ATOM   2284 C  CA  A VAL A 1 161 ? 24.58000 53.05200 -3.19900  0.670 52.14000  ?  161 VAL A CA  1 
ATOM   2285 C  CA  B VAL A 1 161 ? 23.54100 53.13900 -3.34400  0.330 52.88000  ?  161 VAL A CA  1 
ATOM   2286 C  C   A VAL A 1 161 ? 24.91800 51.90600 -4.14200  0.670 52.29000  ?  161 VAL A C   1 
ATOM   2287 C  C   B VAL A 1 161 ? 23.91700 52.21600 -4.50000  0.330 52.53000  ?  161 VAL A C   1 
ATOM   2288 O  O   A VAL A 1 161 ? 24.26500 50.85600 -4.12500  0.670 54.10000  ?  161 VAL A O   1 
ATOM   2289 O  O   B VAL A 1 161 ? 23.25500 51.19100 -4.73100  0.330 54.30000  ?  161 VAL A O   1 
ATOM   2290 C  CB  A VAL A 1 161 ? 23.65200 54.08300 -3.87000  0.670 53.86000  ?  161 VAL A CB  1 
ATOM   2291 C  CB  B VAL A 1 161 ? 22.31000 54.04400 -3.54800  0.330 50.13000  ?  161 VAL A CB  1 
ATOM   2292 C  CG1 A VAL A 1 161 ? 22.58900 53.38600 -4.70900  0.670 40.63000  ?  161 VAL A CG1 1 
ATOM   2293 C  CG1 B VAL A 1 161 ? 21.27900 53.34700 -4.33200  0.330 48.38000  ?  161 VAL A CG1 1 
ATOM   2294 C  CG2 A VAL A 1 161 ? 23.01100 54.98300 -2.82100  0.670 59.18000  ?  161 VAL A CG2 1 
ATOM   2295 C  CG2 B VAL A 1 161 ? 21.72700 54.34100 -2.16500  0.330 50.63000  ?  161 VAL A CG2 1 
ATOM   2296 N  N   A ARG A 1 162 ? 25.93600 52.08300 -4.98300  0.670 45.95000  ?  162 ARG A N   1 
ATOM   2297 N  N   B ARG A 1 162 ? 25.03400 52.46000 -5.16900  0.330 53.49000  ?  162 ARG A N   1 
ATOM   2298 C  CA  A ARG A 1 162 ? 26.26800 51.03300 -5.94000  0.670 58.25000  ?  162 ARG A CA  1 
ATOM   2299 C  CA  B ARG A 1 162 ? 25.53400 51.37500 -6.00300  0.330 56.10000  ?  162 ARG A CA  1 
ATOM   2300 C  C   A ARG A 1 162 ? 26.91700 49.83900 -5.24400  0.670 55.13000  ?  162 ARG A C   1 
ATOM   2301 C  C   B ARG A 1 162 ? 25.89700 50.17800 -5.12400  0.330 49.18000  ?  162 ARG A C   1 
ATOM   2302 O  O   A ARG A 1 162 ? 26.57800 48.68700 -5.53700  0.670 47.85000  ?  162 ARG A O   1 
ATOM   2303 O  O   B ARG A 1 162 ? 25.13700 49.19000 -5.06800  0.330 44.65000  ?  162 ARG A O   1 
ATOM   2304 C  CB  A ARG A 1 162 ? 27.15100 51.60900 -7.04800  0.670 62.36000  ?  162 ARG A CB  1 
ATOM   2305 C  CB  B ARG A 1 162 ? 26.70700 51.85500 -6.88500  0.330 63.24000  ?  162 ARG A CB  1 
ATOM   2306 C  CG  A ARG A 1 162 ? 26.37300 52.51800 -7.99900  0.670 68.97000  ?  162 ARG A CG  1 
ATOM   2307 C  CG  B ARG A 1 162 ? 26.22400 52.90000 -7.93300  0.330 68.90000  ?  162 ARG A CG  1 
ATOM   2308 C  CD  A ARG A 1 162 ? 26.81200 52.35500 -9.46200  0.670 87.85000  ?  162 ARG A CD  1 
ATOM   2309 C  CD  B ARG A 1 162 ? 26.57700 52.63100 -9.40900  0.330 87.77000  ?  162 ARG A CD  1 
ATOM   2310 N  NE  A ARG A 1 162 ? 26.31100 51.10900 -10.02300 0.670 103.52000 ?  162 ARG A NE  1 
ATOM   2311 N  NE  B ARG A 1 162 ? 25.87200 51.46200 -9.92800  0.330 98.44000  ?  162 ARG A NE  1 
ATOM   2312 C  CZ  A ARG A 1 162 ? 27.08200 50.17400 -10.56600 0.670 104.04000 ?  162 ARG A CZ  1 
ATOM   2313 C  CZ  B ARG A 1 162 ? 26.43200 50.47100 -10.61100 0.330 99.87000  ?  162 ARG A CZ  1 
ATOM   2314 N  NH1 A ARG A 1 162 ? 28.39100 50.34400 -10.64800 0.670 110.30000 ?  162 ARG A NH1 1 
ATOM   2315 N  NH1 B ARG A 1 162 ? 27.64000 50.58600 -11.12300 0.330 103.76000 ?  162 ARG A NH1 1 
ATOM   2316 N  NH2 A ARG A 1 162 ? 26.54500 49.06600 -11.03700 0.670 100.11000 ?  162 ARG A NH2 1 
ATOM   2317 N  NH2 B ARG A 1 162 ? 25.76100 49.33400 -10.78400 0.330 100.11000 ?  162 ARG A NH2 1 
ATOM   2318 N  N   A LEU A 1 163 ? 27.81200 50.08400 -4.28500  0.670 40.67000  ?  163 LEU A N   1 
ATOM   2319 N  N   B LEU A 1 163 ? 27.00600 50.30100 -4.36200  0.330 48.40000  ?  163 LEU A N   1 
ATOM   2320 C  CA  A LEU A 1 163 ? 28.38800 48.96800 -3.53800  0.670 40.83000  ?  163 LEU A CA  1 
ATOM   2321 C  CA  B LEU A 1 163 ? 27.53100 49.18800 -3.58000  0.330 43.96000  ?  163 LEU A CA  1 
ATOM   2322 C  C   A LEU A 1 163 ? 27.34600 48.31700 -2.63500  0.670 43.36000  ?  163 LEU A C   1 
ATOM   2323 C  C   B LEU A 1 163 ? 26.44300 48.52800 -2.71200  0.330 37.30000  ?  163 LEU A C   1 
ATOM   2324 O  O   A LEU A 1 163 ? 27.32400 47.08900 -2.48200  0.670 44.36000  ?  163 LEU A O   1 
ATOM   2325 O  O   B LEU A 1 163 ? 26.45600 47.30200 -2.54200  0.330 36.31000  ?  163 LEU A O   1 
ATOM   2326 C  CB  A LEU A 1 163 ? 29.58600 49.44600 -2.72300  0.670 42.68000  ?  163 LEU A CB  1 
ATOM   2327 C  CB  B LEU A 1 163 ? 28.73700 49.66700 -2.78000  0.330 43.07000  ?  163 LEU A CB  1 
ATOM   2328 C  CG  A LEU A 1 163 ? 30.81900 49.82400 -3.54500  0.670 45.81000  ?  163 LEU A CG  1 
ATOM   2329 C  CG  B LEU A 1 163 ? 29.92800 50.06600 -3.63300  0.330 40.90000  ?  163 LEU A CG  1 
ATOM   2330 C  CD1 A LEU A 1 163 ? 31.90000 50.42800 -2.66300  0.670 50.31000  ?  163 LEU A CD1 1 
ATOM   2331 C  CD1 B LEU A 1 163 ? 30.94700 50.71300 -2.76700  0.330 43.52000  ?  163 LEU A CD1 1 
ATOM   2332 C  CD2 A LEU A 1 163 ? 31.36000 48.62100 -4.30800  0.670 35.96000  ?  163 LEU A CD2 1 
ATOM   2333 C  CD2 B LEU A 1 163 ? 30.59800 48.89700 -4.29400  0.330 41.95000  ?  163 LEU A CD2 1 
ATOM   2334 N  N   A ARG A 1 164 ? 26.46800 49.12400 -2.03600  0.670 37.76000  ?  164 ARG A N   1 
ATOM   2335 N  N   B ARG A 1 164 ? 25.45300 49.28700 -2.26100  0.330 37.69000  ?  164 ARG A N   1 
ATOM   2336 C  CA  A ARG A 1 164 ? 25.41400 48.57500 -1.19100  0.670 40.76000  ?  164 ARG A CA  1 
ATOM   2337 C  CA  B ARG A 1 164 ? 24.38200 48.75500 -1.43400  0.330 40.67000  ?  164 ARG A CA  1 
ATOM   2338 C  C   A ARG A 1 164 ? 24.52200 47.61400 -1.97100  0.670 36.56000  ?  164 ARG A C   1 
ATOM   2339 C  C   B ARG A 1 164 ? 23.51500 47.76400 -2.21100  0.330 41.05000  ?  164 ARG A C   1 
ATOM   2340 O  O   A ARG A 1 164 ? 24.20900 46.52200 -1.49500  0.670 40.43000  ?  164 ARG A O   1 
ATOM   2341 O  O   B ARG A 1 164 ? 23.26900 46.63100 -1.75300  0.330 34.13000  ?  164 ARG A O   1 
ATOM   2342 C  CB  A ARG A 1 164 ? 24.58500 49.70900 -0.58700  0.670 37.16000  ?  164 ARG A CB  1 
ATOM   2343 C  CB  B ARG A 1 164 ? 23.52200 49.90400 -0.90200  0.330 44.30000  ?  164 ARG A CB  1 
ATOM   2344 C  CG  A ARG A 1 164 ? 23.36700 49.26000 0.21000   0.670 41.16000  ?  164 ARG A CG  1 
ATOM   2345 C  CG  B ARG A 1 164 ? 22.44400 49.52700 0.08400   0.330 38.11000  ?  164 ARG A CG  1 
ATOM   2346 C  CD  A ARG A 1 164 ? 22.30200 50.35500 0.21400   0.670 35.66000  ?  164 ARG A CD  1 
ATOM   2347 C  CD  B ARG A 1 164 ? 21.30100 50.53300 0.14000   0.330 48.06000  ?  164 ARG A CD  1 
ATOM   2348 N  NE  A ARG A 1 164 ? 21.58700 50.41500 -1.05800  0.670 58.89000  ?  164 ARG A NE  1 
ATOM   2349 N  NE  B ARG A 1 164 ? 20.33100 50.39700 -0.95600  0.330 55.79000  ?  164 ARG A NE  1 
ATOM   2350 C  CZ  A ARG A 1 164 ? 20.59000 51.25300 -1.32100  0.670 66.24000  ?  164 ARG A CZ  1 
ATOM   2351 C  CZ  B ARG A 1 164 ? 19.24100 51.14800 -1.12000  0.330 55.53000  ?  164 ARG A CZ  1 
ATOM   2352 N  NH1 A ARG A 1 164 ? 20.18000 52.11200 -0.39800  0.670 53.44000  ?  164 ARG A NH1 1 
ATOM   2353 N  NH1 B ARG A 1 164 ? 18.96900 52.17600 -0.32200  0.330 48.76000  ?  164 ARG A NH1 1 
ATOM   2354 N  NH2 A ARG A 1 164 ? 20.00000 51.23100 -2.50800  0.670 56.79000  ?  164 ARG A NH2 1 
ATOM   2355 N  NH2 B ARG A 1 164 ? 18.39800 50.86200 -2.11000  0.330 53.88000  ?  164 ARG A NH2 1 
ATOM   2356 N  N   A ASN A 1 165 ? 24.08500 48.00500 -3.16500  0.670 38.70000  ?  165 ASN A N   1 
ATOM   2357 N  N   B ASN A 1 165 ? 23.04000 48.13700 -3.39900  0.330 43.80000  ?  165 ASN A N   1 
ATOM   2358 C  CA  A ASN A 1 165 ? 23.17900 47.12800 -3.89800  0.670 42.18000  ?  165 ASN A CA  1 
ATOM   2359 C  CA  B ASN A 1 165 ? 22.13300 47.22000 -4.07500  0.330 44.91000  ?  165 ASN A CA  1 
ATOM   2360 C  C   A ASN A 1 165 ? 23.90600 45.88700 -4.38000  0.670 36.84000  ?  165 ASN A C   1 
ATOM   2361 C  C   B ASN A 1 165 ? 22.86500 45.96600 -4.48800  0.330 35.88000  ?  165 ASN A C   1 
ATOM   2362 O  O   A ASN A 1 165 ? 23.34000 44.78200 -4.31200  0.670 38.09000  ?  165 ASN A O   1 
ATOM   2363 O  O   B ASN A 1 165 ? 22.44900 44.86700 -4.11300  0.330 35.59000  ?  165 ASN A O   1 
ATOM   2364 C  CB  A ASN A 1 165 ? 22.47900 47.91400 -5.01000  0.670 51.22000  ?  165 ASN A CB  1 
ATOM   2365 C  CB  B ASN A 1 165 ? 21.43700 47.90100 -5.25200  0.330 54.00000  ?  165 ASN A CB  1 
ATOM   2366 C  CG  A ASN A 1 165 ? 21.53100 48.97900 -4.43500  0.670 53.88000  ?  165 ASN A CG  1 
ATOM   2367 C  CG  B ASN A 1 165 ? 20.30900 48.81700 -4.79900  0.330 52.01000  ?  165 ASN A CG  1 
ATOM   2368 O  OD1 A ASN A 1 165 ? 20.98000 48.83800 -3.33500  0.670 53.29000  ?  165 ASN A OD1 1 
ATOM   2369 O  OD1 B ASN A 1 165 ? 19.50200 48.42800 -3.94400  0.330 39.13000  ?  165 ASN A OD1 1 
ATOM   2370 N  ND2 A ASN A 1 165 ? 21.36600 50.05600 -5.17300  0.670 49.63000  ?  165 ASN A ND2 1 
ATOM   2371 N  ND2 B ASN A 1 165 ? 20.28700 50.03500 -5.30500  0.330 52.67000  ?  165 ASN A ND2 1 
ATOM   2372 N  N   A LEU A 1 166 ? 25.14300 46.03700 -4.87500  0.670 41.33000  ?  166 LEU A N   1 
ATOM   2373 N  N   B LEU A 1 166 ? 23.99000 46.11000 -5.20300  0.330 36.71000  ?  166 LEU A N   1 
ATOM   2374 C  CA  A LEU A 1 166 ? 25.93100 44.84700 -5.17000  0.670 37.49000  ?  166 LEU A CA  1 
ATOM   2375 C  CA  B LEU A 1 166 ? 24.85400 44.96300 -5.52500  0.330 40.53000  ?  166 LEU A CA  1 
ATOM   2376 C  C   A LEU A 1 166 ? 25.95400 43.91200 -3.95900  0.670 40.59000  ?  166 LEU A C   1 
ATOM   2377 C  C   B LEU A 1 166 ? 24.96000 44.00800 -4.32000  0.330 39.70000  ?  166 LEU A C   1 
ATOM   2378 O  O   A LEU A 1 166 ? 25.75200 42.69700 -4.08100  0.670 29.20000  ?  166 LEU A O   1 
ATOM   2379 O  O   B LEU A 1 166 ? 24.32600 42.93500 -4.29800  0.330 34.40000  ?  166 LEU A O   1 
ATOM   2380 C  CB  A LEU A 1 166 ? 27.35700 45.21500 -5.57800  0.670 45.48000  ?  166 LEU A CB  1 
ATOM   2381 C  CB  B LEU A 1 166 ? 26.26100 45.41800 -5.96500  0.330 40.58000  ?  166 LEU A CB  1 
ATOM   2382 C  CG  A LEU A 1 166 ? 28.28000 44.04200 -5.93000  0.670 46.91000  ?  166 LEU A CG  1 
ATOM   2383 C  CG  B LEU A 1 166 ? 27.35800 44.41600 -6.33700  0.330 37.04000  ?  166 LEU A CG  1 
ATOM   2384 C  CD1 A LEU A 1 166 ? 27.99000 43.56200 -7.34700  0.670 53.38000  ?  166 LEU A CD1 1 
ATOM   2385 C  CD1 B LEU A 1 166 ? 27.60600 44.13000 -7.77100  0.330 54.15000  ?  166 LEU A CD1 1 
ATOM   2386 C  CD2 A LEU A 1 166 ? 29.74400 44.42500 -5.78700  0.670 49.82000  ?  166 LEU A CD2 1 
ATOM   2387 C  CD2 B LEU A 1 166 ? 28.67400 44.76400 -5.67200  0.330 47.69000  ?  166 LEU A CD2 1 
ATOM   2388 N  N   A THR A 1 167 ? 26.19100 44.47400 -2.77300  0.670 32.71000  ?  167 THR A N   1 
ATOM   2389 N  N   B THR A 1 167 ? 25.69900 44.44900 -3.28500  0.330 35.81000  ?  167 THR A N   1 
ATOM   2390 C  CA  A THR A 1 167 ? 26.33900 43.65700 -1.57200  0.670 35.96000  ?  167 THR A CA  1 
ATOM   2391 C  CA  B THR A 1 167 ? 25.87400 43.72700 -2.02700  0.330 36.12000  ?  167 THR A CA  1 
ATOM   2392 C  C   A THR A 1 167 ? 25.02500 42.98100 -1.19400  0.670 37.73000  ?  167 THR A C   1 
ATOM   2393 C  C   B THR A 1 167 ? 24.61600 43.00500 -1.56600  0.330 34.75000  ?  167 THR A C   1 
ATOM   2394 O  O   A THR A 1 167 ? 24.98100 41.76600 -0.96500  0.670 27.06000  ?  167 THR A O   1 
ATOM   2395 O  O   B THR A 1 167 ? 24.61600 41.77400 -1.38000  0.330 31.57000  ?  167 THR A O   1 
ATOM   2396 C  CB  A THR A 1 167 ? 26.85600 44.52600 -0.42200  0.670 26.81000  ?  167 THR A CB  1 
ATOM   2397 C  CB  B THR A 1 167 ? 26.35400 44.72100 -0.96900  0.330 30.70000  ?  167 THR A CB  1 
ATOM   2398 O  OG1 A THR A 1 167 ? 28.23000 44.86600 -0.65700  0.670 43.20000  ?  167 THR A OG1 1 
ATOM   2399 O  OG1 B THR A 1 167 ? 27.72700 45.06400 -1.23300  0.330 30.42000  ?  167 THR A OG1 1 
ATOM   2400 C  CG2 A THR A 1 167 ? 26.73400 43.79600 0.90600   0.670 35.77000  ?  167 THR A CG2 1 
ATOM   2401 C  CG2 B THR A 1 167 ? 26.05600 44.24700 0.43100   0.330 25.19000  ?  167 THR A CG2 1 
ATOM   2402 N  N   A VAL A 1 168 ? 23.93900 43.75500 -1.13000  0.670 29.68000  ?  168 VAL A N   1 
ATOM   2403 N  N   B VAL A 1 168 ? 23.52700 43.74700 -1.42300  0.330 29.62000  ?  168 VAL A N   1 
ATOM   2404 C  CA  A VAL A 1 168 ? 22.66700 43.21500 -0.65700  0.670 27.54000  ?  168 VAL A CA  1 
ATOM   2405 C  CA  B VAL A 1 168 ? 22.31900 43.13600 -0.87800  0.330 30.23000  ?  168 VAL A CA  1 
ATOM   2406 C  C   A VAL A 1 168 ? 22.16300 42.12200 -1.59000  0.670 35.70000  ?  168 VAL A C   1 
ATOM   2407 C  C   B VAL A 1 168 ? 21.81200 42.05400 -1.81500  0.330 35.81000  ?  168 VAL A C   1 
ATOM   2408 O  O   A VAL A 1 168 ? 21.71100 41.06300 -1.14000  0.670 39.43000  ?  168 VAL A O   1 
ATOM   2409 O  O   B VAL A 1 168 ? 21.47500 40.93700 -1.39700  0.330 37.01000  ?  168 VAL A O   1 
ATOM   2410 C  CB  A VAL A 1 168 ? 21.63400 44.34800 -0.50700  0.670 42.56000  ?  168 VAL A CB  1 
ATOM   2411 C  CB  B VAL A 1 168 ? 21.25300 44.21600 -0.66100  0.330 39.69000  ?  168 VAL A CB  1 
ATOM   2412 C  CG1 A VAL A 1 168 ? 20.22500 43.77700 -0.38800  0.670 33.20000  ?  168 VAL A CG1 1 
ATOM   2413 C  CG1 B VAL A 1 168 ? 19.88500 43.58400 -0.23000  0.330 31.40000  ?  168 VAL A CG1 1 
ATOM   2414 C  CG2 A VAL A 1 168 ? 21.96700 45.22800 0.69000   0.670 35.42000  ?  168 VAL A CG2 1 
ATOM   2415 C  CG2 B VAL A 1 168 ? 21.77500 45.27400 0.34100   0.330 37.53000  ?  168 VAL A CG2 1 
ATOM   2416 N  N   A ILE A 1 169 ? 22.23300 42.35500 -2.90100  0.670 36.23000  ?  169 ILE A N   1 
ATOM   2417 N  N   B ILE A 1 169 ? 21.73300 42.40100 -3.10100  0.330 35.73000  ?  169 ILE A N   1 
ATOM   2418 C  CA  A ILE A 1 169 ? 21.66600 41.40100 -3.84800  0.670 29.55000  ?  169 ILE A CA  1 
ATOM   2419 C  CA  B ILE A 1 169 ? 21.49100 41.46100 -4.17700  0.330 31.02000  ?  169 ILE A CA  1 
ATOM   2420 C  C   A ILE A 1 169 ? 22.45300 40.09600 -3.82500  0.670 28.76000  ?  169 ILE A C   1 
ATOM   2421 C  C   B ILE A 1 169 ? 22.41900 40.26800 -4.04700  0.330 28.58000  ?  169 ILE A C   1 
ATOM   2422 O  O   A ILE A 1 169 ? 21.87300 39.00600 -3.75500  0.670 32.38000  ?  169 ILE A O   1 
ATOM   2423 O  O   B ILE A 1 169 ? 21.96600 39.11600 -4.01500  0.330 32.06000  ?  169 ILE A O   1 
ATOM   2424 C  CB  A ILE A 1 169 ? 21.61200 42.01400 -5.25900  0.670 40.98000  ?  169 ILE A CB  1 
ATOM   2425 C  CB  B ILE A 1 169 ? 21.66200 42.22100 -5.50300  0.330 38.38000  ?  169 ILE A CB  1 
ATOM   2426 C  CG1 A ILE A 1 169 ? 20.54600 43.11300 -5.30200  0.670 36.49000  ?  169 ILE A CG1 1 
ATOM   2427 C  CG1 B ILE A 1 169 ? 20.45700 43.18300 -5.66500  0.330 36.20000  ?  169 ILE A CG1 1 
ATOM   2428 C  CG2 A ILE A 1 169 ? 21.32600 40.94700 -6.29500  0.670 23.37000  ?  169 ILE A CG2 1 
ATOM   2429 C  CG2 B ILE A 1 169 ? 22.04900 41.33100 -6.61700  0.330 22.16000  ?  169 ILE A CG2 1 
ATOM   2430 C  CD1 A ILE A 1 169 ? 20.67600 44.05600 -6.46700  0.670 41.38000  ?  169 ILE A CD1 1 
ATOM   2431 C  CD1 B ILE A 1 169 ? 20.79500 44.44300 -6.55000  0.330 40.65000  ?  169 ILE A CD1 1 
ATOM   2432 N  N   A LEU A 1 170 ? 23.78600 40.18600 -3.85300  0.670 25.49000  ?  170 LEU A N   1 
ATOM   2433 N  N   B LEU A 1 170 ? 23.73400 40.52100 -3.96500  0.330 27.10000  ?  170 LEU A N   1 
ATOM   2434 C  CA  A LEU A 1 170 ? 24.59400 38.97300 -3.92600  0.670 24.81000  ?  170 LEU A CA  1 
ATOM   2435 C  CA  B LEU A 1 170 ? 24.70400 39.43100 -3.82000  0.330 27.03000  ?  170 LEU A CA  1 
ATOM   2436 C  C   A LEU A 1 170 ? 24.65000 38.25300 -2.58300  0.670 31.85000  ?  170 LEU A C   1 
ATOM   2437 C  C   B LEU A 1 170 ? 24.43900 38.67700 -2.54700  0.330 32.32000  ?  170 LEU A C   1 
ATOM   2438 O  O   A LEU A 1 170 ? 24.59200 37.02000 -2.53800  0.670 30.72000  ?  170 LEU A O   1 
ATOM   2439 O  O   B LEU A 1 170 ? 24.00500 37.50900 -2.56600  0.330 32.33000  ?  170 LEU A O   1 
ATOM   2440 C  CB  A LEU A 1 170 ? 26.00300 39.30400 -4.41600  0.670 29.94000  ?  170 LEU A CB  1 
ATOM   2441 C  CB  B LEU A 1 170 ? 26.11700 39.97100 -3.73700  0.330 26.11000  ?  170 LEU A CB  1 
ATOM   2442 C  CG  A LEU A 1 170 ? 26.05300 39.83600 -5.84500  0.670 24.85000  ?  170 LEU A CG  1 
ATOM   2443 C  CG  B LEU A 1 170 ? 26.63500 40.71500 -4.94500  0.330 29.99000  ?  170 LEU A CG  1 
ATOM   2444 C  CD1 A LEU A 1 170 ? 27.48300 40.01200 -6.31800  0.670 27.59000  ?  170 LEU A CD1 1 
ATOM   2445 C  CD1 B LEU A 1 170 ? 28.05500 41.22800 -4.71100  0.330 28.26000  ?  170 LEU A CD1 1 
ATOM   2446 C  CD2 A LEU A 1 170 ? 25.29900 38.90800 -6.79300  0.670 29.98000  ?  170 LEU A CD2 1 
ATOM   2447 C  CD2 B LEU A 1 170 ? 26.61000 39.77800 -6.14600  0.330 25.72000  ?  170 LEU A CD2 1 
ATOM   2448 N  N   A TRP A 1 171 ? 24.78100 38.99100 -1.47800  0.670 31.72000  ?  171 TRP A N   1 
ATOM   2449 N  N   B TRP A 1 171 ? 24.59900 39.39500 -1.41900  0.330 29.73000  ?  171 TRP A N   1 
ATOM   2450 C  CA  A TRP A 1 171 ? 24.82300 38.32200 -0.18000  0.670 28.59000  ?  171 TRP A CA  1 
ATOM   2451 C  CA  B TRP A 1 171 ? 24.64000 38.76100 -0.11600  0.330 30.07000  ?  171 TRP A CA  1 
ATOM   2452 C  C   A TRP A 1 171 ? 23.54600 37.52700 0.06700   0.670 29.11000  ?  171 TRP A C   1 
ATOM   2453 C  C   B TRP A 1 171 ? 23.45500 37.87600 0.09100   0.330 29.90000  ?  171 TRP A C   1 
ATOM   2454 O  O   A TRP A 1 171 ? 23.58400 36.47000 0.70900   0.670 25.52000  ?  171 TRP A O   1 
ATOM   2455 O  O   B TRP A 1 171 ? 23.53600 36.98400 0.92300   0.330 25.93000  ?  171 TRP A O   1 
ATOM   2456 C  CB  A TRP A 1 171 ? 25.03900 39.33600 0.94500   0.670 26.28000  ?  171 TRP A CB  1 
ATOM   2457 C  CB  B TRP A 1 171 ? 24.64600 39.75300 1.05500   0.330 27.91000  ?  171 TRP A CB  1 
ATOM   2458 C  CG  A TRP A 1 171 ? 26.44100 39.86000 1.04400   0.670 27.40000  ?  171 TRP A CG  1 
ATOM   2459 C  CG  B TRP A 1 171 ? 25.92300 40.48600 1.27800   0.330 29.59000  ?  171 TRP A CG  1 
ATOM   2460 C  CD1 A TRP A 1 171 ? 27.30800 40.08300 0.01300   0.670 30.51000  ?  171 TRP A CD1 1 
ATOM   2461 C  CD1 B TRP A 1 171 ? 26.70800 41.17000 0.36000   0.330 33.48000  ?  171 TRP A CD1 1 
ATOM   2462 C  CD2 A TRP A 1 171 ? 27.13700 40.23700 2.24000   0.670 36.14000  ?  171 TRP A CD2 1 
ATOM   2463 C  CD2 B TRP A 1 171 ? 26.59600 40.57200 2.49800   0.330 35.05000  ?  171 TRP A CD2 1 
ATOM   2464 N  NE1 A TRP A 1 171 ? 28.49700 40.57400 0.49100   0.670 23.49000  ?  171 TRP A NE1 1 
ATOM   2465 N  NE1 B TRP A 1 171 ? 27.80800 41.69900 0.98200   0.330 28.73000  ?  171 TRP A NE1 1 
ATOM   2466 C  CE2 A TRP A 1 171 ? 28.41900 40.67800 1.85400   0.670 24.55000  ?  171 TRP A CE2 1 
ATOM   2467 C  CE2 B TRP A 1 171 ? 27.75900 41.34400 2.29300   0.330 30.20000  ?  171 TRP A CE2 1 
ATOM   2468 C  CE3 A TRP A 1 171 ? 26.80300 40.24200 3.60000   0.670 29.84000  ?  171 TRP A CE3 1 
ATOM   2469 C  CE3 B TRP A 1 171 ? 26.34300 40.04800 3.76800   0.330 28.42000  ?  171 TRP A CE3 1 
ATOM   2470 C  CZ2 A TRP A 1 171 ? 29.36600 41.12100 2.77800   0.670 33.36000  ?  171 TRP A CZ2 1 
ATOM   2471 C  CZ2 B TRP A 1 171 ? 28.62700 41.62000 3.30400   0.330 31.37000  ?  171 TRP A CZ2 1 
ATOM   2472 C  CZ3 A TRP A 1 171 ? 27.74500 40.68200 4.51400   0.670 31.24000  ?  171 TRP A CZ3 1 
ATOM   2473 C  CZ3 B TRP A 1 171 ? 27.20600 40.29600 4.73700   0.330 26.76000  ?  171 TRP A CZ3 1 
ATOM   2474 C  CH2 A TRP A 1 171 ? 29.01000 41.11400 4.10000   0.670 35.42000  ?  171 TRP A CH2 1 
ATOM   2475 C  CH2 B TRP A 1 171 ? 28.33100 41.09800 4.51600   0.330 34.89000  ?  171 TRP A CH2 1 
ATOM   2476 N  N   A ALA A 1 172 ? 22.41100 38.01000 -0.44700  0.670 22.79000  ?  172 ALA A N   1 
ATOM   2477 N  N   B ALA A 1 172 ? 22.35800 38.12600 -0.63500  0.330 21.70000  ?  172 ALA A N   1 
ATOM   2478 C  CA  A ALA A 1 172 ? 21.13700 37.32700 -0.25400  0.670 31.22000  ?  172 ALA A CA  1 
ATOM   2479 C  CA  B ALA A 1 172 ? 21.15600 37.29300 -0.49800  0.330 31.41000  ?  172 ALA A CA  1 
ATOM   2480 C  C   A ALA A 1 172 ? 21.08200 35.98800 -0.97200  0.670 35.97000  ?  172 ALA A C   1 
ATOM   2481 C  C   B ALA A 1 172 ? 21.28700 35.92500 -1.15500  0.330 34.94000  ?  172 ALA A C   1 
ATOM   2482 O  O   A ALA A 1 172 ? 20.21100 35.16900 -0.66100  0.670 40.96000  ?  172 ALA A O   1 
ATOM   2483 O  O   B ALA A 1 172 ? 20.62000 34.97800 -0.73200  0.330 38.02000  ?  172 ALA A O   1 
ATOM   2484 C  CB  A ALA A 1 172 ? 19.98900 38.21600 -0.73600  0.670 28.01000  ?  172 ALA A CB  1 
ATOM   2485 C  CB  B ALA A 1 172 ? 19.92900 37.96100 -1.10100  0.330 28.08000  ?  172 ALA A CB  1 
ATOM   2486 N  N   A ILE A 1 173 ? 21.99000 35.74800 -1.91600  0.670 28.54000  ?  173 ILE A N   1 
ATOM   2487 N  N   B ILE A 1 173 ? 22.09700 35.80100 -2.19900  0.330 29.27000  ?  173 ILE A N   1 
ATOM   2488 C  CA  A ILE A 1 173 ? 21.99800 34.48700 -2.64500  0.670 25.84000  ?  173 ILE A CA  1 
ATOM   2489 C  CA  B ILE A 1 173 ? 22.17700 34.54000 -2.91100  0.330 27.91000  ?  173 ILE A CA  1 
ATOM   2490 C  C   A ILE A 1 173 ? 22.70500 33.39800 -1.85100  0.670 32.49000  ?  173 ILE A C   1 
ATOM   2491 C  C   B ILE A 1 173 ? 22.80000 33.46300 -2.04300  0.330 31.38000  ?  173 ILE A C   1 
ATOM   2492 O  O   A ILE A 1 173 ? 22.33900 32.22000 -1.94800  0.670 27.43000  ?  173 ILE A O   1 
ATOM   2493 O  O   B ILE A 1 173 ? 22.34400 32.30800 -2.01800  0.330 29.37000  ?  173 ILE A O   1 
ATOM   2494 C  CB  A ILE A 1 173 ? 22.65700 34.69000 -4.02000  0.670 34.76000  ?  173 ILE A CB  1 
ATOM   2495 C  CB  B ILE A 1 173 ? 22.99000 34.73800 -4.19600  0.330 32.79000  ?  173 ILE A CB  1 
ATOM   2496 C  CG1 A ILE A 1 173 ? 21.79900 35.61000 -4.89400  0.670 32.13000  ?  173 ILE A CG1 1 
ATOM   2497 C  CG1 B ILE A 1 173 ? 22.18900 35.57500 -5.16100  0.330 31.62000  ?  173 ILE A CG1 1 
ATOM   2498 C  CG2 A ILE A 1 173 ? 22.89000 33.35100 -4.70800  0.670 25.35000  ?  173 ILE A CG2 1 
ATOM   2499 C  CG2 B ILE A 1 173 ? 23.38500 33.39200 -4.72600  0.330 26.11000  ?  173 ILE A CG2 1 
ATOM   2500 C  CD1 A ILE A 1 173 ? 22.54600 36.22500 -6.05500  0.670 33.39000  ?  173 ILE A CD1 1 
ATOM   2501 C  CD1 B ILE A 1 173 ? 23.02400 36.29000 -6.09800  0.330 33.01000  ?  173 ILE A CD1 1 
ATOM   2502 N  N   A TYR A 1 174 ? 23.70800 33.76000 -1.05500  0.670 25.60000  ?  174 TYR A N   1 
ATOM   2503 N  N   B TYR A 1 174 ? 23.89400 33.81500 -1.37400  0.330 25.41000  ?  174 TYR A N   1 
ATOM   2504 C  CA  A TYR A 1 174 ? 24.47000 32.75600 -0.31500  0.670 27.20000  ?  174 TYR A CA  1 
ATOM   2505 C  CA  B TYR A 1 174 ? 24.57200 32.85900 -0.51800  0.330 27.06000  ?  174 TYR A CA  1 
ATOM   2506 C  C   A TYR A 1 174 ? 23.60000 31.82600 0.52000   0.670 32.26000  ?  174 TYR A C   1 
ATOM   2507 C  C   B TYR A 1 174 ? 23.61200 32.02100 0.30900   0.330 31.15000  ?  174 TYR A C   1 
ATOM   2508 O  O   A TYR A 1 174 ? 23.81700 30.60400 0.46400   0.670 36.72000  ?  174 TYR A O   1 
ATOM   2509 O  O   B TYR A 1 174 ? 23.67700 30.78500 0.20400   0.330 36.17000  ?  174 TYR A O   1 
ATOM   2510 C  CB  A TYR A 1 174 ? 25.48600 33.43700 0.61100   0.670 22.53000  ?  174 TYR A CB  1 
ATOM   2511 C  CB  B TYR A 1 174 ? 25.54200 33.61700 0.39900   0.330 25.29000  ?  174 TYR A CB  1 
ATOM   2512 C  CG  A TYR A 1 174 ? 26.76800 33.90500 -0.03400  0.670 27.47000  ?  174 TYR A CG  1 
ATOM   2513 C  CG  B TYR A 1 174 ? 26.81100 34.10400 -0.23600  0.330 26.03000  ?  174 TYR A CG  1 
ATOM   2514 C  CD1 A TYR A 1 174 ? 26.82700 35.12600 -0.68800  0.670 29.31000  ?  174 TYR A CD1 1 
ATOM   2515 C  CD1 B TYR A 1 174 ? 26.85300 35.32600 -0.86400  0.330 28.67000  ?  174 TYR A CD1 1 
ATOM   2516 C  CD2 A TYR A 1 174 ? 27.93000 33.14700 0.04800   0.670 29.72000  ?  174 TYR A CD2 1 
ATOM   2517 C  CD2 B TYR A 1 174 ? 27.96100 33.41100 -0.10400  0.330 28.23000  ?  174 TYR A CD2 1 
ATOM   2518 C  CE1 A TYR A 1 174 ? 27.99700 35.57200 -1.26500  0.670 28.34000  ?  174 TYR A CE1 1 
ATOM   2519 C  CE1 B TYR A 1 174 ? 28.01600 35.82200 -1.37200  0.330 28.99000  ?  174 TYR A CE1 1 
ATOM   2520 C  CE2 A TYR A 1 174 ? 29.10900 33.58400 -0.52400  0.670 27.86000  ?  174 TYR A CE2 1 
ATOM   2521 C  CE2 B TYR A 1 174 ? 29.10800 33.87200 -0.61400  0.330 27.18000  ?  174 TYR A CE2 1 
ATOM   2522 C  CZ  A TYR A 1 174 ? 29.13500 34.80000 -1.17900  0.670 24.29000  ?  174 TYR A CZ  1 
ATOM   2523 C  CZ  B TYR A 1 174 ? 29.13500 35.06500 -1.25500  0.330 25.61000  ?  174 TYR A CZ  1 
ATOM   2524 O  OH  A TYR A 1 174 ? 30.29800 35.25500 -1.75700  0.670 25.24000  ?  174 TYR A OH  1 
ATOM   2525 O  OH  B TYR A 1 174 ? 30.32300 35.52500 -1.72800  0.330 25.53000  ?  174 TYR A OH  1 
ATOM   2526 N  N   A PRO A 1 175 ? 22.65700 32.31000 1.33800   0.670 26.73000  ?  175 PRO A N   1 
ATOM   2527 N  N   B PRO A 1 175 ? 22.72800 32.60000 1.14400   0.330 28.20000  ?  175 PRO A N   1 
ATOM   2528 C  CA  A PRO A 1 175 ? 21.86900 31.36000 2.14400   0.670 32.99000  ?  175 PRO A CA  1 
ATOM   2529 C  CA  B PRO A 1 175 ? 21.76900 31.76900 1.85900   0.330 32.30000  ?  175 PRO A CA  1 
ATOM   2530 C  C   A PRO A 1 175 ? 21.11800 30.35200 1.29500   0.670 34.84000  ?  175 PRO A C   1 
ATOM   2531 C  C   B PRO A 1 175 ? 21.03300 30.82900 0.96100   0.330 35.40000  ?  175 PRO A C   1 
ATOM   2532 O  O   A PRO A 1 175 ? 20.90700 29.21500 1.73400   0.670 37.14000  ?  175 PRO A O   1 
ATOM   2533 O  O   B PRO A 1 175 ? 20.82900 29.68200 1.37200   0.330 35.21000  ?  175 PRO A O   1 
ATOM   2534 C  CB  A PRO A 1 175 ? 20.91500 32.26000 2.94700   0.670 30.14000  ?  175 PRO A CB  1 
ATOM   2535 C  CB  B PRO A 1 175 ? 20.80000 32.77100 2.50600   0.330 32.99000  ?  175 PRO A CB  1 
ATOM   2536 C  CG  A PRO A 1 175 ? 20.96600 33.60300 2.29900   0.670 34.91000  ?  175 PRO A CG  1 
ATOM   2537 C  CG  B PRO A 1 175 ? 21.12000 34.04800 1.92300   0.330 32.82000  ?  175 PRO A CG  1 
ATOM   2538 C  CD  A PRO A 1 175 ? 22.30000 33.71600 1.61800   0.670 29.04000  ?  175 PRO A CD  1 
ATOM   2539 C  CD  B PRO A 1 175 ? 22.53000 34.00800 1.50400   0.330 29.60000  ?  175 PRO A CD  1 
ATOM   2540 N  N   A PHE A 1 176 ? 20.72600 30.72400 0.07700   0.670 38.25000  ?  176 PHE A N   1 
ATOM   2541 N  N   B PHE A 1 176 ? 20.68000 31.21000 -0.27300  0.330 34.74000  ?  176 PHE A N   1 
ATOM   2542 C  CA  A PHE A 1 176 ? 20.05800 29.76700 -0.79600  0.670 33.40000  ?  176 PHE A CA  1 
ATOM   2543 C  CA  B PHE A 1 176 ? 19.99000 30.21500 -1.10000  0.330 34.27000  ?  176 PHE A CA  1 
ATOM   2544 C  C   A PHE A 1 176 ? 21.03300 28.71800 -1.31500  0.670 41.10000  ?  176 PHE A C   1 
ATOM   2545 C  C   B PHE A 1 176 ? 20.85600 29.04700 -1.45000  0.330 39.04000  ?  176 PHE A C   1 
ATOM   2546 O  O   A PHE A 1 176 ? 20.70000 27.52800 -1.36200  0.670 40.19000  ?  176 PHE A O   1 
ATOM   2547 O  O   B PHE A 1 176 ? 20.38600 27.90100 -1.40000  0.330 35.99000  ?  176 PHE A O   1 
ATOM   2548 C  CB  A PHE A 1 176 ? 19.37700 30.50600 -1.94400  0.670 32.56000  ?  176 PHE A CB  1 
ATOM   2549 C  CB  B PHE A 1 176 ? 19.42300 30.78700 -2.36000  0.330 33.14000  ?  176 PHE A CB  1 
ATOM   2550 C  CG  A PHE A 1 176 ? 18.28300 31.42500 -1.49200  0.670 34.31000  ?  176 PHE A CG  1 
ATOM   2551 C  CG  B PHE A 1 176 ? 18.25300 31.51000 -2.07700  0.330 33.92000  ?  176 PHE A CG  1 
ATOM   2552 C  CD1 A PHE A 1 176 ? 17.00300 30.94400 -1.26900  0.670 42.65000  ?  176 PHE A CD1 1 
ATOM   2553 C  CD1 B PHE A 1 176 ? 17.13100 30.80600 -1.75400  0.330 39.30000  ?  176 PHE A CD1 1 
ATOM   2554 C  CD2 A PHE A 1 176 ? 18.53900 32.76500 -1.26600  0.670 37.69000  ?  176 PHE A CD2 1 
ATOM   2555 C  CD2 B PHE A 1 176 ? 18.26100 32.87000 -1.97000  0.330 37.28000  ?  176 PHE A CD2 1 
ATOM   2556 C  CE1 A PHE A 1 176 ? 15.99800 31.78700 -0.84300  0.670 35.02000  ?  176 PHE A CE1 1 
ATOM   2557 C  CE1 B PHE A 1 176 ? 15.98900 31.47500 -1.39800  0.330 35.95000  ?  176 PHE A CE1 1 
ATOM   2558 C  CE2 A PHE A 1 176 ? 17.53400 33.61300 -0.83700  0.670 39.01000  ?  176 PHE A CE2 1 
ATOM   2559 C  CE2 B PHE A 1 176 ? 17.13000 33.54800 -1.67200  0.330 35.55000  ?  176 PHE A CE2 1 
ATOM   2560 C  CZ  A PHE A 1 176 ? 16.26500 33.12400 -0.62600  0.670 38.71000  ?  176 PHE A CZ  1 
ATOM   2561 C  CZ  B PHE A 1 176 ? 15.98100 32.84400 -1.36600  0.330 35.21000  ?  176 PHE A CZ  1 
ATOM   2562 N  N   A ILE A 1 177 ? 22.24600 29.12900 -1.69500  0.670 28.69000  ?  177 ILE A N   1 
ATOM   2563 N  N   B ILE A 1 177 ? 22.12500 29.30400 -1.77700  0.330 28.76000  ?  177 ILE A N   1 
ATOM   2564 C  CA  A ILE A 1 177 ? 23.23600 28.15700 -2.15200  0.670 35.61000  ?  177 ILE A CA  1 
ATOM   2565 C  CA  B ILE A 1 177 ? 22.96200 28.19200 -2.20200  0.330 36.61000  ?  177 ILE A CA  1 
ATOM   2566 C  C   A ILE A 1 177 ? 23.59900 27.20000 -1.02100  0.670 43.90000  ?  177 ILE A C   1 
ATOM   2567 C  C   B ILE A 1 177 ? 23.28800 27.30400 -1.01800  0.330 42.10000  ?  177 ILE A C   1 
ATOM   2568 O  O   A ILE A 1 177 ? 23.74900 25.98900 -1.22900  0.670 48.74000  ?  177 ILE A O   1 
ATOM   2569 O  O   B ILE A 1 177 ? 23.24700 26.07600 -1.12800  0.330 45.95000  ?  177 ILE A O   1 
ATOM   2570 C  CB  A ILE A 1 177 ? 24.48800 28.87000 -2.69400  0.670 34.91000  ?  177 ILE A CB  1 
ATOM   2571 C  CB  B ILE A 1 177 ? 24.23200 28.67600 -2.89200  0.330 34.18000  ?  177 ILE A CB  1 
ATOM   2572 C  CG1 A ILE A 1 177 ? 24.12700 29.88400 -3.78000  0.670 32.82000  ?  177 ILE A CG1 1 
ATOM   2573 C  CG1 B ILE A 1 177 ? 23.93100 29.70100 -4.00600  0.330 33.09000  ?  177 ILE A CG1 1 
ATOM   2574 C  CG2 A ILE A 1 177 ? 25.48200 27.83800 -3.22700  0.670 44.25000  ?  177 ILE A CG2 1 
ATOM   2575 C  CG2 B ILE A 1 177 ? 24.97100 27.49500 -3.32700  0.330 41.06000  ?  177 ILE A CG2 1 
ATOM   2576 C  CD1 A ILE A 1 177 ? 23.09000 29.40700 -4.76600  0.670 29.69000  ?  177 ILE A CD1 1 
ATOM   2577 C  CD1 B ILE A 1 177 ? 22.79300 29.38000 -4.85200  0.330 30.47000  ?  177 ILE A CD1 1 
ATOM   2578 N  N   A TRP A 1 178 ? 23.78900 27.73800 0.18600   0.670 41.19000  ?  178 TRP A N   1 
ATOM   2579 N  N   B TRP A 1 178 ? 23.62100 27.90600 0.13100   0.330 40.54000  ?  178 TRP A N   1 
ATOM   2580 C  CA  A TRP A 1 178 ? 24.08400 26.91100 1.35400   0.670 35.42000  ?  178 TRP A CA  1 
ATOM   2581 C  CA  B TRP A 1 178 ? 23.83100 27.11500 1.33600   0.330 38.27000  ?  178 TRP A CA  1 
ATOM   2582 C  C   A TRP A 1 178 ? 22.98400 25.88300 1.57900   0.670 46.19000  ?  178 TRP A C   1 
ATOM   2583 C  C   B TRP A 1 178 ? 22.69100 26.18200 1.49800   0.330 44.95000  ?  178 TRP A C   1 
ATOM   2584 O  O   A TRP A 1 178 ? 23.25300 24.68400 1.71900   0.670 50.18000  ?  178 TRP A O   1 
ATOM   2585 O  O   B TRP A 1 178 ? 22.87400 24.97500 1.71600   0.330 49.57000  ?  178 TRP A O   1 
ATOM   2586 C  CB  A TRP A 1 178 ? 24.25000 27.82700 2.57200   0.670 45.91000  ?  178 TRP A CB  1 
ATOM   2587 C  CB  B TRP A 1 178 ? 23.89200 28.00600 2.57300   0.330 44.12000  ?  178 TRP A CB  1 
ATOM   2588 C  CG  A TRP A 1 178 ? 24.74800 27.21300 3.85400   0.670 39.12000  ?  178 TRP A CG  1 
ATOM   2589 C  CG  B TRP A 1 178 ? 24.30300 27.36200 3.85200   0.330 38.72000  ?  178 TRP A CG  1 
ATOM   2590 C  CD1 A TRP A 1 178 ? 26.02500 27.24900 4.34000   0.670 41.28000  ?  178 TRP A CD1 1 
ATOM   2591 C  CD1 B TRP A 1 178 ? 25.51000 27.50300 4.42200   0.330 40.61000  ?  178 TRP A CD1 1 
ATOM   2592 C  CD2 A TRP A 1 178 ? 23.96600 26.52600 4.83800   0.670 32.10000  ?  178 TRP A CD2 1 
ATOM   2593 C  CD2 B TRP A 1 178 ? 23.52500 26.57700 4.76700   0.330 36.79000  ?  178 TRP A CD2 1 
ATOM   2594 N  NE1 A TRP A 1 178 ? 26.08900 26.61200 5.55500   0.670 41.78000  ?  178 TRP A NE1 1 
ATOM   2595 N  NE1 B TRP A 1 178 ? 25.58300 26.84100 5.60500   0.330 40.51000  ?  178 TRP A NE1 1 
ATOM   2596 C  CE2 A TRP A 1 178 ? 24.83800 26.15900 5.88400   0.670 44.90000  ?  178 TRP A CE2 1 
ATOM   2597 C  CE2 B TRP A 1 178 ? 24.36100 26.28900 5.87400   0.330 41.45000  ?  178 TRP A CE2 1 
ATOM   2598 C  CE3 A TRP A 1 178 ? 22.61500 26.18200 4.93400   0.670 46.74000  ?  178 TRP A CE3 1 
ATOM   2599 C  CE3 B TRP A 1 178 ? 22.20200 26.09200 4.78400   0.330 46.13000  ?  178 TRP A CE3 1 
ATOM   2600 C  CZ2 A TRP A 1 178 ? 24.40200 25.45900 7.00800   0.670 44.00000  ?  178 TRP A CZ2 1 
ATOM   2601 C  CZ2 B TRP A 1 178 ? 23.93600 25.49400 6.98900   0.330 45.55000  ?  178 TRP A CZ2 1 
ATOM   2602 C  CZ3 A TRP A 1 178 ? 22.18700 25.48400 6.04800   0.670 47.05000  ?  178 TRP A CZ3 1 
ATOM   2603 C  CZ3 B TRP A 1 178 ? 21.75100 25.29600 5.93400   0.330 42.38000  ?  178 TRP A CZ3 1 
ATOM   2604 C  CH2 A TRP A 1 178 ? 23.07700 25.13200 7.07100   0.670 47.67000  ?  178 TRP A CH2 1 
ATOM   2605 C  CH2 B TRP A 1 178 ? 22.62600 25.00800 6.99600   0.330 44.70000  ?  178 TRP A CH2 1 
ATOM   2606 N  N   A LEU A 1 179 ? 21.73000 26.33400 1.57200   0.670 46.41000  ?  179 LEU A N   1 
ATOM   2607 N  N   B LEU A 1 179 ? 21.49400 26.75900 1.42500   0.330 42.58000  ?  179 LEU A N   1 
ATOM   2608 C  CA  A LEU A 1 179 ? 20.61700 25.44600 1.88900   0.670 38.73000  ?  179 LEU A CA  1 
ATOM   2609 C  CA  B LEU A 1 179 ? 20.29100 25.97600 1.60100   0.330 41.05000  ?  179 LEU A CA  1 
ATOM   2610 C  C   A LEU A 1 179 ? 20.41700 24.38900 0.81200   0.670 42.58000  ?  179 LEU A C   1 
ATOM   2611 C  C   B LEU A 1 179 ? 20.10500 24.92500 0.49600   0.330 44.08000  ?  179 LEU A C   1 
ATOM   2612 O  O   A LEU A 1 179 ? 20.05700 23.24800 1.12000   0.670 45.36000  ?  179 LEU A O   1 
ATOM   2613 O  O   B LEU A 1 179 ? 19.59400 23.83100 0.76600   0.330 43.75000  ?  179 LEU A O   1 
ATOM   2614 C  CB  A LEU A 1 179 ? 19.34700 26.26900 2.07400   0.670 40.12000  ?  179 LEU A CB  1 
ATOM   2615 C  CB  B LEU A 1 179 ? 19.12500 26.93800 1.69300   0.330 38.52000  ?  179 LEU A CB  1 
ATOM   2616 C  CG  A LEU A 1 179 ? 18.25900 25.69900 2.97900   0.670 50.61000  ?  179 LEU A CG  1 
ATOM   2617 C  CG  B LEU A 1 179 ? 17.97000 26.41500 2.47900   0.330 44.49000  ?  179 LEU A CG  1 
ATOM   2618 C  CD1 A LEU A 1 179 ? 18.77900 25.45300 4.37600   0.670 45.17000  ?  179 LEU A CD1 1 
ATOM   2619 C  CD1 B LEU A 1 179 ? 18.52000 25.72900 3.71400   0.330 48.13000  ?  179 LEU A CD1 1 
ATOM   2620 C  CD2 A LEU A 1 179 ? 17.07400 26.65700 2.99000   0.670 39.72000  ?  179 LEU A CD2 1 
ATOM   2621 C  CD2 B LEU A 1 179 ? 17.26100 27.63000 2.90900   0.330 39.72000  ?  179 LEU A CD2 1 
ATOM   2622 N  N   A LEU A 1 180 ? 20.63200 24.74300 -0.45400  0.670 43.92000  ?  180 LEU A N   1 
ATOM   2623 N  N   B LEU A 1 180 ? 20.50100 25.22000 -0.75300  0.330 44.27000  ?  180 LEU A N   1 
ATOM   2624 C  CA  A LEU A 1 180 ? 20.45800 23.77800 -1.53200  0.670 45.17000  ?  180 LEU A CA  1 
ATOM   2625 C  CA  B LEU A 1 180 ? 20.22600 24.29700 -1.86900  0.330 44.85000  ?  180 LEU A CA  1 
ATOM   2626 C  C   A LEU A 1 180 ? 21.66300 22.86400 -1.70400  0.670 45.99000  ?  180 LEU A C   1 
ATOM   2627 C  C   B LEU A 1 180 ? 21.27500 23.22200 -2.03500  0.330 42.80000  ?  180 LEU A C   1 
ATOM   2628 O  O   A LEU A 1 180 ? 21.56100 21.85800 -2.41500  0.670 53.25000  ?  180 LEU A O   1 
ATOM   2629 O  O   B LEU A 1 180 ? 20.92500 22.08600 -2.33400  0.330 48.74000  ?  180 LEU A O   1 
ATOM   2630 C  CB  A LEU A 1 180 ? 20.18100 24.50200 -2.84900  0.670 42.71000  ?  180 LEU A CB  1 
ATOM   2631 C  CB  B LEU A 1 180 ? 20.12000 25.02400 -3.21000  0.330 40.42000  ?  180 LEU A CB  1 
ATOM   2632 C  CG  A LEU A 1 180 ? 18.79600 25.13600 -2.98800  0.670 42.78000  ?  180 LEU A CG  1 
ATOM   2633 C  CG  B LEU A 1 180 ? 18.82500 25.56500 -3.78400  0.330 40.59000  ?  180 LEU A CG  1 
ATOM   2634 C  CD1 A LEU A 1 180 ? 18.73700 26.06700 -4.18900  0.670 41.16000  ?  180 LEU A CD1 1 
ATOM   2635 C  CD1 B LEU A 1 180 ? 19.14500 26.50600 -4.92600  0.330 38.26000  ?  180 LEU A CD1 1 
ATOM   2636 C  CD2 A LEU A 1 180 ? 17.72300 24.06100 -3.10000  0.670 47.61000  ?  180 LEU A CD2 1 
ATOM   2637 C  CD2 B LEU A 1 180 ? 17.95400 24.46900 -4.27000  0.330 36.50000  ?  180 LEU A CD2 1 
ATOM   2638 N  N   A GLY A 1 181 ? 22.78400 23.18100 -1.06500  0.670 48.72000  ?  181 GLY A N   1 
ATOM   2639 N  N   B GLY A 1 181 ? 22.54200 23.56900 -1.85000  0.330 46.21000  ?  181 GLY A N   1 
ATOM   2640 C  CA  A GLY A 1 181 ? 23.99400 22.41400 -1.21400  0.670 43.13000  ?  181 GLY A CA  1 
ATOM   2641 C  CA  B GLY A 1 181 ? 23.63100 22.62900 -1.85100  0.330 45.49000  ?  181 GLY A CA  1 
ATOM   2642 C  C   A GLY A 1 181 ? 24.15500 21.36300 -0.13800  0.670 48.14000  ?  181 GLY A C   1 
ATOM   2643 C  C   B GLY A 1 181 ? 23.58400 21.63600 -0.72500  0.330 46.12000  ?  181 GLY A C   1 
ATOM   2644 O  O   A GLY A 1 181 ? 23.21500 21.02800 0.58900   0.670 52.72000  ?  181 GLY A O   1 
ATOM   2645 O  O   B GLY A 1 181 ? 22.52100 21.24900 -0.24000  0.330 42.80000  ?  181 GLY A O   1 
ATOM   2646 N  N   A PRO A 1 182 ? 25.36600 20.82400 -0.01900  0.670 56.70000  ?  182 PRO A N   1 
ATOM   2647 N  N   B PRO A 1 182 ? 24.75700 21.14600 -0.34900  0.330 50.74000  ?  182 PRO A N   1 
ATOM   2648 C  CA  A PRO A 1 182 ? 25.61700 19.74300 0.94800   0.670 56.97000  ?  182 PRO A CA  1 
ATOM   2649 C  CA  B PRO A 1 182 ? 24.84100 20.05600 0.64000   0.330 54.24000  ?  182 PRO A CA  1 
ATOM   2650 C  C   A PRO A 1 182 ? 25.25100 20.13300 2.36900   0.670 59.01000  ?  182 PRO A C   1 
ATOM   2651 C  C   B PRO A 1 182 ? 24.32100 20.42400 2.02200   0.330 52.54000  ?  182 PRO A C   1 
ATOM   2652 O  O   A PRO A 1 182 ? 24.70500 19.30400 3.11500   0.670 50.40000  ?  182 PRO A O   1 
ATOM   2653 O  O   B PRO A 1 182 ? 23.61800 19.59400 2.62100   0.330 49.14000  ?  182 PRO A O   1 
ATOM   2654 C  CB  A PRO A 1 182 ? 27.12700 19.49000 0.80900   0.670 55.60000  ?  182 PRO A CB  1 
ATOM   2655 C  CB  B PRO A 1 182 ? 26.34100 19.71200 0.65000   0.330 56.23000  ?  182 PRO A CB  1 
ATOM   2656 C  CG  A PRO A 1 182 ? 27.43400 19.88100 -0.60900  0.670 53.17000  ?  182 PRO A CG  1 
ATOM   2657 C  CG  B PRO A 1 182 ? 26.75900 19.95500 -0.80100  0.330 53.89000  ?  182 PRO A CG  1 
ATOM   2658 C  CD  A PRO A 1 182 ? 26.51400 21.04300 -0.92200  0.670 53.56000  ?  182 PRO A CD  1 
ATOM   2659 C  CD  B PRO A 1 182 ? 25.91800 21.14800 -1.26700  0.330 50.06000  ?  182 PRO A CD  1 
ATOM   2660 N  N   A PRO A 1 183 ? 25.54700 21.36500 2.80400   0.670 55.50000  ?  183 PRO A N   1 
ATOM   2661 N  N   B PRO A 1 183 ? 24.62400 21.61600 2.58000   0.330 49.83000  ?  183 PRO A N   1 
ATOM   2662 C  CA  A PRO A 1 183 ? 25.22400 21.71600 4.20100   0.670 57.96000  ?  183 PRO A CA  1 
ATOM   2663 C  CA  B PRO A 1 183 ? 24.15800 21.85200 3.95700   0.330 50.52000  ?  183 PRO A CA  1 
ATOM   2664 C  C   A PRO A 1 183 ? 23.74900 21.57400 4.53000   0.670 49.07000  ?  183 PRO A C   1 
ATOM   2665 C  C   B PRO A 1 183 ? 22.65700 21.84200 4.03000   0.330 50.13000  ?  183 PRO A C   1 
ATOM   2666 O  O   A PRO A 1 183 ? 23.40200 21.28800 5.68300   0.670 51.37000  ?  183 PRO A O   1 
ATOM   2667 O  O   B PRO A 1 183 ? 22.06600 21.41800 5.03800   0.330 52.23000  ?  183 PRO A O   1 
ATOM   2668 C  CB  A PRO A 1 183 ? 25.68500 23.17600 4.32400   0.670 54.16000  ?  183 PRO A CB  1 
ATOM   2669 C  CB  B PRO A 1 183 ? 24.74500 23.23200 4.32300   0.330 50.67000  ?  183 PRO A CB  1 
ATOM   2670 C  CG  A PRO A 1 183 ? 26.67300 23.37000 3.22100   0.670 47.32000  ?  183 PRO A CG  1 
ATOM   2671 C  CG  B PRO A 1 183 ? 25.83500 23.49600 3.34800   0.330 47.73000  ?  183 PRO A CG  1 
ATOM   2672 C  CD  A PRO A 1 183 ? 26.21900 22.47400 2.09900   0.670 50.97000  ?  183 PRO A CD  1 
ATOM   2673 C  CD  B PRO A 1 183 ? 25.33800 22.80300 2.06900   0.330 48.92000  ?  183 PRO A CD  1 
ATOM   2674 N  N   A GLY A 1 184 ? 22.87100 21.77400 3.55000   0.670 47.58000  ?  184 GLY A N   1 
ATOM   2675 N  N   B GLY A 1 184 ? 22.01600 22.27000 2.96200   0.330 44.97000  ?  184 GLY A N   1 
ATOM   2676 C  CA  A GLY A 1 184 ? 21.44100 21.71300 3.77500   0.670 50.70000  ?  184 GLY A CA  1 
ATOM   2677 C  CA  B GLY A 1 184 ? 20.58700 22.28900 3.00500   0.330 47.64000  ?  184 GLY A CA  1 
ATOM   2678 C  C   A GLY A 1 184 ? 20.81400 20.45700 3.21300   0.670 49.69000  ?  184 GLY A C   1 
ATOM   2679 C  C   B GLY A 1 184 ? 19.96700 21.03900 2.45200   0.330 47.48000  ?  184 GLY A C   1 
ATOM   2680 O  O   A GLY A 1 184 ? 21.18000 19.34800 3.60900   0.670 49.51000  ?  184 GLY A O   1 
ATOM   2681 O  O   B GLY A 1 184 ? 20.16100 19.94100 2.97000   0.330 51.44000  ?  184 GLY A O   1 
ATOM   2682 N  N   A VAL A 1 185 ? 19.89400 20.60500 2.26300   0.670 42.92000  ?  185 VAL A N   1 
ATOM   2683 N  N   B VAL A 1 185 ? 19.21600 21.19900 1.37600   0.330 51.45000  ?  185 VAL A N   1 
ATOM   2684 C  CA  A VAL A 1 185 ? 19.16600 19.45100 1.74200   0.670 55.95000  ?  185 VAL A CA  1 
ATOM   2685 C  CA  B VAL A 1 185 ? 18.42100 20.08900 0.88000   0.330 55.01000  ?  185 VAL A CA  1 
ATOM   2686 C  C   A VAL A 1 185 ? 20.06800 18.58100 0.87000   0.670 72.64000  ?  185 VAL A C   1 
ATOM   2687 C  C   B VAL A 1 185 ? 19.22400 19.28900 -0.12100  0.330 52.54000  ?  185 VAL A C   1 
ATOM   2688 O  O   A VAL A 1 185 ? 19.64100 17.53500 0.36600   0.670 74.86000  ?  185 VAL A O   1 
ATOM   2689 O  O   B VAL A 1 185 ? 18.68200 18.43600 -0.82000  0.330 57.80000  ?  185 VAL A O   1 
ATOM   2690 C  CB  A VAL A 1 185 ? 17.91700 19.87800 0.94600   0.670 56.61000  ?  185 VAL A CB  1 
ATOM   2691 C  CB  B VAL A 1 185 ? 17.08600 20.53400 0.26700   0.330 50.94000  ?  185 VAL A CB  1 
ATOM   2692 C  CG1 A VAL A 1 185 ? 16.88600 20.51700 1.85200   0.670 61.47000  ?  185 VAL A CG1 1 
ATOM   2693 C  CG1 B VAL A 1 185 ? 16.40800 21.43900 1.23400   0.330 55.72000  ?  185 VAL A CG1 1 
ATOM   2694 C  CG2 A VAL A 1 185 ? 18.30600 20.82300 -0.19200  0.670 54.36000  ?  185 VAL A CG2 1 
ATOM   2695 C  CG2 B VAL A 1 185 ? 17.22600 21.17700 -1.07400  0.330 48.26000  ?  185 VAL A CG2 1 
ATOM   2696 N  N   A ALA A 1 186 ? 21.31400 19.00500 0.66700   0.670 72.52000  ?  186 ALA A N   1 
ATOM   2697 N  N   B ALA A 1 186 ? 20.52500 19.55300 -0.19500  0.330 55.02000  ?  186 ALA A N   1 
ATOM   2698 C  CA  A ALA A 1 186 ? 22.28600 18.21200 -0.09400  0.670 61.14000  ?  186 ALA A CA  1 
ATOM   2699 C  CA  B ALA A 1 186 ? 21.47200 18.50100 -0.55300  0.330 59.57000  ?  186 ALA A CA  1 
ATOM   2700 C  C   A ALA A 1 186 ? 21.77400 17.90200 -1.50100  0.670 62.53000  ?  186 ALA A C   1 
ATOM   2701 C  C   B ALA A 1 186 ? 21.28200 18.06800 -1.99800  0.330 62.66000  ?  186 ALA A C   1 
ATOM   2702 O  O   A ALA A 1 186 ? 22.02100 16.82600 -2.05400  0.670 69.04000  ?  186 ALA A O   1 
ATOM   2703 O  O   B ALA A 1 186 ? 21.89800 17.10600 -2.46300  0.330 66.10000  ?  186 ALA A O   1 
ATOM   2704 C  CB  A ALA A 1 186 ? 22.63600 16.91700 0.64400   0.670 74.84000  ?  186 ALA A CB  1 
ATOM   2705 C  CB  B ALA A 1 186 ? 21.32100 17.32200 0.40600   0.330 65.05000  ?  186 ALA A CB  1 
ATOM   2706 N  N   A LEU A 1 187 ? 21.04100 18.85100 -2.08000  0.670 62.19000  ?  187 LEU A N   1 
ATOM   2707 N  N   B LEU A 1 187 ? 20.36300 18.74600 -2.67500  0.330 55.78000  ?  187 LEU A N   1 
ATOM   2708 C  CA  A LEU A 1 187 ? 20.52600 18.69000 -3.43900  0.670 50.79000  ?  187 LEU A CA  1 
ATOM   2709 C  CA  B LEU A 1 187 ? 20.22900 18.76300 -4.11300  0.330 59.12000  ?  187 LEU A CA  1 
ATOM   2710 C  C   A LEU A 1 187 ? 21.63800 18.94100 -4.45300  0.670 69.46000  ?  187 LEU A C   1 
ATOM   2711 C  C   B LEU A 1 187 ? 21.61600 19.03700 -4.67100  0.330 67.80000  ?  187 LEU A C   1 
ATOM   2712 O  O   A LEU A 1 187 ? 22.10400 18.01600 -5.12400  0.670 75.58000  ?  187 LEU A O   1 
ATOM   2713 O  O   B LEU A 1 187 ? 22.45300 18.11300 -4.74300  0.330 67.80000  ?  187 LEU A O   1 
ATOM   2714 C  CB  A LEU A 1 187 ? 19.34500 19.64100 -3.65200  0.670 52.65000  ?  187 LEU A CB  1 
ATOM   2715 C  CB  B LEU A 1 187 ? 19.25100 19.85700 -4.50200  0.330 50.16000  ?  187 LEU A CB  1 
ATOM   2716 C  CG  A LEU A 1 187 ? 18.35900 19.38700 -4.79000  0.670 45.53000  ?  187 LEU A CG  1 
ATOM   2717 C  CG  B LEU A 1 187 ? 18.44800 19.93600 -5.75000  0.330 44.28000  ?  187 LEU A CG  1 
ATOM   2718 C  CD1 A LEU A 1 187 ? 17.92600 17.94500 -4.89000  0.670 62.21000  ?  187 LEU A CD1 1 
ATOM   2719 C  CD1 B LEU A 1 187 ? 17.91000 18.60900 -6.04600  0.330 52.32000  ?  187 LEU A CD1 1 
ATOM   2720 C  CD2 A LEU A 1 187 ? 17.13500 20.30000 -4.60600  0.670 39.84000  ?  187 LEU A CD2 1 
ATOM   2721 C  CD2 B LEU A 1 187 ? 17.31700 20.81900 -5.40200  0.330 40.60000  ?  187 LEU A CD2 1 
ATOM   2722 N  N   A LEU A 1 188 ? 22.08200 20.19200 -4.56500  0.670 56.97000  ?  188 LEU A N   1 
ATOM   2723 N  N   B LEU A 1 188 ? 21.86200 20.32400 -5.00300  0.330 56.99000  ?  188 LEU A N   1 
ATOM   2724 C  CA  A LEU A 1 188 ? 23.22000 20.50300 -5.41700  0.670 51.10000  ?  188 LEU A CA  1 
ATOM   2725 C  CA  B LEU A 1 188 ? 23.12300 20.78200 -5.56000  0.330 51.87000  ?  188 LEU A CA  1 
ATOM   2726 C  C   A LEU A 1 188 ? 24.43300 19.68400 -4.99500  0.670 53.80000  ?  188 LEU A C   1 
ATOM   2727 C  C   B LEU A 1 188 ? 24.27900 19.94100 -5.08900  0.330 53.67000  ?  188 LEU A C   1 
ATOM   2728 O  O   A LEU A 1 188 ? 24.66100 19.44700 -3.80500  0.670 52.39000  ?  188 LEU A O   1 
ATOM   2729 O  O   B LEU A 1 188 ? 24.50100 19.77400 -3.89100  0.330 50.85000  ?  188 LEU A O   1 
ATOM   2730 C  CB  A LEU A 1 188 ? 23.55100 21.99100 -5.33900  0.670 49.15000  ?  188 LEU A CB  1 
ATOM   2731 C  CB  B LEU A 1 188 ? 23.42400 22.20800 -5.16700  0.330 49.23000  ?  188 LEU A CB  1 
ATOM   2732 C  CG  A LEU A 1 188 ? 22.54500 22.95800 -5.95300  0.670 45.75000  ?  188 LEU A CG  1 
ATOM   2733 C  CG  B LEU A 1 188 ? 22.57400 23.27900 -5.71200  0.330 46.85000  ?  188 LEU A CG  1 
ATOM   2734 C  CD1 A LEU A 1 188 ? 22.91000 24.38600 -5.58400  0.670 40.60000  ?  188 LEU A CD1 1 
ATOM   2735 C  CD1 B LEU A 1 188 ? 23.26800 24.53300 -5.19400  0.330 40.26000  ?  188 LEU A CD1 1 
ATOM   2736 C  CD2 A LEU A 1 188 ? 22.50100 22.79200 -7.46000  0.670 56.30000  ?  188 LEU A CD2 1 
ATOM   2737 C  CD2 B LEU A 1 188 ? 22.55300 23.16300 -7.20600  0.330 54.18000  ?  188 LEU A CD2 1 
ATOM   2738 N  N   A THR A 1 189 ? 25.21900 19.25600 -5.97700  0.670 47.40000  ?  189 THR A N   1 
ATOM   2739 N  N   B THR A 1 189 ? 25.02400 19.47700 -6.04500  0.330 48.65000  ?  189 THR A N   1 
ATOM   2740 C  CA  A THR A 1 189 ? 26.41200 18.47400 -5.70000  0.670 42.13000  ?  189 THR A CA  1 
ATOM   2741 C  CA  B THR A 1 189 ? 26.19100 18.65400 -5.98200  0.330 45.52000  ?  189 THR A CA  1 
ATOM   2742 C  C   A THR A 1 189 ? 27.53200 19.37400 -5.19300  0.670 42.68000  ?  189 THR A C   1 
ATOM   2743 C  C   B THR A 1 189 ? 27.38600 19.52200 -5.58800  0.330 43.98000  ?  189 THR A C   1 
ATOM   2744 O  O   A THR A 1 189 ? 27.52300 20.58600 -5.42400  0.670 43.63000  ?  189 THR A O   1 
ATOM   2745 O  O   B THR A 1 189 ? 27.53700 20.63700 -6.08700  0.330 43.39000  ?  189 THR A O   1 
ATOM   2746 C  CB  A THR A 1 189 ? 26.86500 17.74000 -6.95700  0.670 53.25000  ?  189 THR A CB  1 
ATOM   2747 C  CB  B THR A 1 189 ? 26.40100 18.01800 -7.34000  0.330 51.40000  ?  189 THR A CB  1 
ATOM   2748 O  OG1 A THR A 1 189 ? 27.19300 18.69400 -7.97500  0.670 52.35000  ?  189 THR A OG1 1 
ATOM   2749 O  OG1 B THR A 1 189 ? 26.93600 18.98300 -8.22600  0.330 51.12000  ?  189 THR A OG1 1 
ATOM   2750 C  CG2 A THR A 1 189 ? 25.76600 16.81600 -7.46100  0.670 63.56000  ?  189 THR A CG2 1 
ATOM   2751 C  CG2 B THR A 1 189 ? 25.03500 17.69300 -7.95300  0.330 51.35000  ?  189 THR A CG2 1 
ATOM   2752 N  N   A PRO A 1 190 ? 28.51800 18.80200 -4.49600  0.670 43.36000  ?  190 PRO A N   1 
ATOM   2753 N  N   B PRO A 1 190 ? 28.23300 19.02900 -4.70000  0.330 41.98000  ?  190 PRO A N   1 
ATOM   2754 C  CA  A PRO A 1 190 ? 29.61400 19.64500 -3.98300  0.670 36.30000  ?  190 PRO A CA  1 
ATOM   2755 C  CA  B PRO A 1 190 ? 29.34900 19.84300 -4.17000  0.330 38.21000  ?  190 PRO A CA  1 
ATOM   2756 C  C   A PRO A 1 190 ? 30.30700 20.44400 -5.07300  0.670 45.51000  ?  190 PRO A C   1 
ATOM   2757 C  C   B PRO A 1 190 ? 30.33100 20.40300 -5.20300  0.330 44.44000  ?  190 PRO A C   1 
ATOM   2758 O  O   A PRO A 1 190 ? 30.63500 21.61900 -4.86600  0.670 40.47000  ?  190 PRO A O   1 
ATOM   2759 O  O   B PRO A 1 190 ? 31.13400 21.28600 -4.84100  0.330 39.14000  ?  190 PRO A O   1 
ATOM   2760 C  CB  A PRO A 1 190 ? 30.56100 18.63000 -3.32200  0.670 38.62000  ?  190 PRO A CB  1 
ATOM   2761 C  CB  B PRO A 1 190 ? 30.07500 18.86500 -3.23400  0.330 40.33000  ?  190 PRO A CB  1 
ATOM   2762 C  CG  A PRO A 1 190 ? 29.70200 17.42700 -3.03000  0.670 36.20000  ?  190 PRO A CG  1 
ATOM   2763 C  CG  B PRO A 1 190 ? 29.07500 17.79300 -2.93300  0.330 42.18000  ?  190 PRO A CG  1 
ATOM   2764 C  CD  A PRO A 1 190 ? 28.68500 17.38000 -4.14100  0.670 44.26000  ?  190 PRO A CD  1 
ATOM   2765 C  CD  B PRO A 1 190 ? 28.19700 17.66800 -4.16200  0.330 43.87000  ?  190 PRO A CD  1 
ATOM   2766 N  N   A THR A 1 191 ? 30.52800 19.84200 -6.24200  0.670 40.25000  ?  191 THR A N   1 
ATOM   2767 N  N   B THR A 1 191 ? 30.38500 19.87000 -6.43400  0.330 40.42000  ?  191 THR A N   1 
ATOM   2768 C  CA  A THR A 1 191 ? 31.27000 20.52900 -7.29400  0.670 40.09000  ?  191 THR A CA  1 
ATOM   2769 C  CA  B THR A 1 191 ? 31.12400 20.58600 -7.47700  0.330 40.99000  ?  191 THR A CA  1 
ATOM   2770 C  C   A THR A 1 191 ? 30.51100 21.75200 -7.79400  0.670 40.84000  ?  191 THR A C   1 
ATOM   2771 C  C   B THR A 1 191 ? 30.35500 21.83800 -7.83700  0.330 40.96000  ?  191 THR A C   1 
ATOM   2772 O  O   A THR A 1 191 ? 31.08600 22.83800 -7.93400  0.670 41.08000  ?  191 THR A O   1 
ATOM   2773 O  O   B THR A 1 191 ? 30.88200 22.96400 -7.79800  0.330 40.67000  ?  191 THR A O   1 
ATOM   2774 C  CB  A THR A 1 191 ? 31.55800 19.57000 -8.44900  0.670 52.61000  ?  191 THR A CB  1 
ATOM   2775 C  CB  B THR A 1 191 ? 31.28500 19.74700 -8.76000  0.330 49.58000  ?  191 THR A CB  1 
ATOM   2776 O  OG1 A THR A 1 191 ? 32.44200 18.53500 -8.00100  0.670 52.01000  ?  191 THR A OG1 1 
ATOM   2777 O  OG1 B THR A 1 191 ? 31.83600 18.45400 -8.47400  0.330 39.99000  ?  191 THR A OG1 1 
ATOM   2778 C  CG2 A THR A 1 191 ? 32.19300 20.31800 -9.60900  0.670 41.95000  ?  191 THR A CG2 1 
ATOM   2779 C  CG2 B THR A 1 191 ? 32.24700 20.39900 -9.65200  0.330 43.96000  ?  191 THR A CG2 1 
ATOM   2780 N  N   A VAL A 1 192 ? 29.22000 21.59100 -8.08500  0.670 41.58000  ?  192 VAL A N   1 
ATOM   2781 N  N   B VAL A 1 192 ? 29.06700 21.62600 -8.13400  0.330 41.22000  ?  192 VAL A N   1 
ATOM   2782 C  CA  A VAL A 1 192 ? 28.42400 22.72800 -8.53100  0.670 32.31000  ?  192 VAL A CA  1 
ATOM   2783 C  CA  B VAL A 1 192 ? 28.09200 22.63800 -8.52400  0.330 34.98000  ?  192 VAL A CA  1 
ATOM   2784 C  C   A VAL A 1 192 ? 28.30000 23.75700 -7.41600  0.670 34.17000  ?  192 VAL A C   1 
ATOM   2785 C  C   B VAL A 1 192 ? 27.79100 23.56100 -7.37100  0.330 35.94000  ?  192 VAL A C   1 
ATOM   2786 O  O   A VAL A 1 192 ? 28.43200 24.96500 -7.64800  0.670 34.82000  ?  192 VAL A O   1 
ATOM   2787 O  O   B VAL A 1 192 ? 27.56600 24.76500 -7.55900  0.330 36.39000  ?  192 VAL A O   1 
ATOM   2788 C  CB  A VAL A 1 192 ? 27.04300 22.25300 -9.02200  0.670 41.38000  ?  192 VAL A CB  1 
ATOM   2789 C  CB  B VAL A 1 192 ? 26.81900 21.91700 -9.00800  0.330 40.91000  ?  192 VAL A CB  1 
ATOM   2790 C  CG1 A VAL A 1 192 ? 26.18400 23.44100 -9.42700  0.670 33.82000  ?  192 VAL A CG1 1 
ATOM   2791 C  CG1 B VAL A 1 192 ? 25.60400 22.85400 -9.10800  0.330 35.97000  ?  192 VAL A CG1 1 
ATOM   2792 C  CG2 A VAL A 1 192 ? 27.20200 21.27300 -10.17400 0.670 41.43000  ?  192 VAL A CG2 1 
ATOM   2793 C  CG2 B VAL A 1 192 ? 27.11600 21.13400 -10.26600 0.330 41.24000  ?  192 VAL A CG2 1 
ATOM   2794 N  N   A ASP A 1 193 ? 28.05100 23.29900 -6.18700  0.670 42.48000  ?  193 ASP A N   1 
ATOM   2795 N  N   B ASP A 1 193 ? 27.73800 23.01300 -6.15500  0.330 42.43000  ?  193 ASP A N   1 
ATOM   2796 C  CA  A ASP A 1 193 ? 27.89200 24.23100 -5.07600  0.670 32.78000  ?  193 ASP A CA  1 
ATOM   2797 C  CA  B ASP A 1 193 ? 27.79000 23.89300 -5.02100  0.330 34.17000  ?  193 ASP A CA  1 
ATOM   2798 C  C   A ASP A 1 193 ? 29.15500 25.05500 -4.86300  0.670 32.62000  ?  193 ASP A C   1 
ATOM   2799 C  C   B ASP A 1 193 ? 29.03000 24.76000 -5.06400  0.330 33.09000  ?  193 ASP A C   1 
ATOM   2800 O  O   A ASP A 1 193 ? 29.08600 26.27100 -4.64600  0.670 34.82000  ?  193 ASP A O   1 
ATOM   2801 O  O   B ASP A 1 193 ? 28.93300 25.98600 -5.01500  0.330 35.12000  ?  193 ASP A O   1 
ATOM   2802 C  CB  A ASP A 1 193 ? 27.53400 23.47000 -3.80400  0.670 42.04000  ?  193 ASP A CB  1 
ATOM   2803 C  CB  B ASP A 1 193 ? 27.74700 23.15400 -3.69600  0.330 40.94000  ?  193 ASP A CB  1 
ATOM   2804 C  CG  A ASP A 1 193 ? 26.88200 24.35400 -2.77200  0.670 44.20000  ?  193 ASP A CG  1 
ATOM   2805 C  CG  B ASP A 1 193 ? 27.62600 24.14100 -2.53800  0.330 41.32000  ?  193 ASP A CG  1 
ATOM   2806 O  OD1 A ASP A 1 193 ? 25.71000 24.73100 -2.97700  0.670 47.18000  ?  193 ASP A OD1 1 
ATOM   2807 O  OD1 B ASP A 1 193 ? 26.52300 24.69900 -2.36300  0.330 44.60000  ?  193 ASP A OD1 1 
ATOM   2808 O  OD2 A ASP A 1 193 ? 27.54100 24.68000 -1.76500  0.670 49.91000  -1 193 ASP A OD2 1 
ATOM   2809 O  OD2 B ASP A 1 193 ? 28.67300 24.46500 -1.92300  0.330 40.57000  -1 193 ASP A OD2 1 
ATOM   2810 N  N   A VAL A 1 194 ? 30.31800 24.40600 -4.92500  0.670 31.75000  ?  194 VAL A N   1 
ATOM   2811 N  N   B VAL A 1 194 ? 30.20300 24.15400 -5.14400  0.330 32.92000  ?  194 VAL A N   1 
ATOM   2812 C  CA  A VAL A 1 194 ? 31.58400 25.11500 -4.77200  0.670 29.09000  ?  194 VAL A CA  1 
ATOM   2813 C  CA  B VAL A 1 194 ? 31.41000 24.93500 -4.87900  0.330 30.64000  ?  194 VAL A CA  1 
ATOM   2814 C  C   A VAL A 1 194 ? 31.78100 26.09800 -5.91800  0.670 33.36000  ?  194 VAL A C   1 
ATOM   2815 C  C   B VAL A 1 194 ? 31.70300 25.89600 -6.01400  0.330 33.33000  ?  194 VAL A C   1 
ATOM   2816 O  O   A VAL A 1 194 ? 32.17500 27.25100 -5.70800  0.670 23.80000  ?  194 VAL A O   1 
ATOM   2817 O  O   B VAL A 1 194 ? 32.21700 27.00700 -5.74900  0.330 26.94000  ?  194 VAL A O   1 
ATOM   2818 C  CB  A VAL A 1 194 ? 32.74400 24.10800 -4.67900  0.670 34.22000  ?  194 VAL A CB  1 
ATOM   2819 C  CB  B VAL A 1 194 ? 32.60400 24.00900 -4.56300  0.330 34.51000  ?  194 VAL A CB  1 
ATOM   2820 C  CG1 A VAL A 1 194 ? 34.06700 24.77000 -4.99400  0.670 36.26000  ?  194 VAL A CG1 1 
ATOM   2821 C  CG1 B VAL A 1 194 ? 33.92000 24.72200 -4.73600  0.330 35.83000  ?  194 VAL A CG1 1 
ATOM   2822 C  CG2 A VAL A 1 194 ? 32.77100 23.46000 -3.29600  0.670 34.19000  ?  194 VAL A CG2 1 
ATOM   2823 C  CG2 B VAL A 1 194 ? 32.46200 23.43400 -3.15300  0.330 34.02000  ?  194 VAL A CG2 1 
ATOM   2824 N  N   A ALA A 1 195 ? 31.50600 25.65800 -7.14900  0.670 28.31000  ?  195 ALA A N   1 
ATOM   2825 N  N   B ALA A 1 195 ? 31.31600 25.58100 -7.27800  0.330 28.12000  ?  195 ALA A N   1 
ATOM   2826 C  CA  A ALA A 1 195 ? 31.66500 26.54500 -8.29800  0.670 32.82000  ?  195 ALA A CA  1 
ATOM   2827 C  CA  B ALA A 1 195 ? 31.52500 26.59800 -8.35100  0.330 32.70000  ?  195 ALA A CA  1 
ATOM   2828 C  C   A ALA A 1 195 ? 30.84200 27.81400 -8.13000  0.670 29.18000  ?  195 ALA A C   1 
ATOM   2829 C  C   B ALA A 1 195 ? 30.73100 27.88100 -8.08000  0.330 29.14000  ?  195 ALA A C   1 
ATOM   2830 O  O   A ALA A 1 195 ? 31.32100 28.91800 -8.41500  0.670 28.90000  ?  195 ALA A O   1 
ATOM   2831 O  O   B ALA A 1 195 ? 31.28100 28.99400 -8.18600  0.330 29.70000  ?  195 ALA A O   1 
ATOM   2832 C  CB  A ALA A 1 195 ? 31.26800 25.81800 -9.58300  0.670 28.91000  ?  195 ALA A CB  1 
ATOM   2833 C  CB  B ALA A 1 195 ? 31.15800 26.08300 -9.75400  0.330 27.28000  ?  195 ALA A CB  1 
ATOM   2834 N  N   A LEU A 1 196 ? 29.60000 27.68100 -7.66200  0.670 26.97000  ?  196 LEU A N   1 
ATOM   2835 N  N   B LEU A 1 196 ? 29.45200 27.73800 -7.66500  0.330 26.71000  ?  196 LEU A N   1 
ATOM   2836 C  CA  A LEU A 1 196 ? 28.76200 28.85900 -7.47500  0.670 26.44000  ?  196 LEU A CA  1 
ATOM   2837 C  CA  B LEU A 1 196 ? 28.62600 28.90800 -7.41400  0.330 26.82000  ?  196 LEU A CA  1 
ATOM   2838 C  C   A LEU A 1 196 ? 29.32600 29.77300 -6.39100  0.670 24.24000  ?  196 LEU A C   1 
ATOM   2839 C  C   B LEU A 1 196 ? 29.01600 29.63900 -6.17000  0.330 26.78000  ?  196 LEU A C   1 
ATOM   2840 O  O   A LEU A 1 196 ? 29.28400 31.00000 -6.52700  0.670 28.01000  ?  196 LEU A O   1 
ATOM   2841 O  O   B LEU A 1 196 ? 28.67900 30.80300 -6.06000  0.330 31.29000  ?  196 LEU A O   1 
ATOM   2842 C  CB  A LEU A 1 196 ? 27.33100 28.43400 -7.14600  0.670 28.07000  ?  196 LEU A CB  1 
ATOM   2843 C  CB  B LEU A 1 196 ? 27.15000 28.57700 -7.30800  0.330 29.02000  ?  196 LEU A CB  1 
ATOM   2844 C  CG  A LEU A 1 196 ? 26.56900 27.79000 -8.30800  0.670 30.01000  ?  196 LEU A CG  1 
ATOM   2845 C  CG  B LEU A 1 196 ? 26.50600 28.00700 -8.57200  0.330 29.53000  ?  196 LEU A CG  1 
ATOM   2846 C  CD1 A LEU A 1 196 ? 25.26800 27.16800 -7.82900  0.670 26.77000  ?  196 LEU A CD1 1 
ATOM   2847 C  CD1 B LEU A 1 196 ? 25.04400 27.80400 -8.28300  0.330 25.10000  ?  196 LEU A CD1 1 
ATOM   2848 C  CD2 A LEU A 1 196 ? 26.30300 28.81300 -9.40600  0.670 35.23000  ?  196 LEU A CD2 1 
ATOM   2849 C  CD2 B LEU A 1 196 ? 26.81300 28.89200 -9.85800  0.330 31.46000  ?  196 LEU A CD2 1 
ATOM   2850 N  N   A ILE A 1 197 ? 29.88000 29.20400 -5.31900  0.670 26.07000  ?  197 ILE A N   1 
ATOM   2851 N  N   B ILE A 1 197 ? 29.67800 29.01800 -5.21000  0.330 27.23000  ?  197 ILE A N   1 
ATOM   2852 C  CA  A ILE A 1 197 ? 30.37700 30.04800 -4.23600  0.670 29.30000  ?  197 ILE A CA  1 
ATOM   2853 C  CA  B ILE A 1 197 ? 30.21500 29.87500 -4.15800  0.330 29.01000  ?  197 ILE A CA  1 
ATOM   2854 C  C   A ILE A 1 197 ? 31.70500 30.69700 -4.61700  0.670 32.29000  ?  197 ILE A C   1 
ATOM   2855 C  C   B ILE A 1 197 ? 31.54200 30.53600 -4.56400  0.330 31.12000  ?  197 ILE A C   1 
ATOM   2856 O  O   A ILE A 1 197 ? 31.97600 31.84100 -4.23400  0.670 33.14000  ?  197 ILE A O   1 
ATOM   2857 O  O   B ILE A 1 197 ? 31.77500 31.71100 -4.22300  0.330 32.56000  ?  197 ILE A O   1 
ATOM   2858 C  CB  A ILE A 1 197 ? 30.48600 29.24300 -2.92800  0.670 30.55000  ?  197 ILE A CB  1 
ATOM   2859 C  CB  B ILE A 1 197 ? 30.30000 29.13100 -2.80700  0.330 31.06000  ?  197 ILE A CB  1 
ATOM   2860 C  CG1 A ILE A 1 197 ? 29.08900 29.01700 -2.34500  0.670 31.27000  ?  197 ILE A CG1 1 
ATOM   2861 C  CG1 B ILE A 1 197 ? 28.97400 29.39000 -2.11000  0.330 30.03000  ?  197 ILE A CG1 1 
ATOM   2862 C  CG2 A ILE A 1 197 ? 31.35600 29.98300 -1.91500  0.670 20.88000  ?  197 ILE A CG2 1 
ATOM   2863 C  CG2 B ILE A 1 197 ? 31.56100 29.50400 -2.08800  0.330 24.81000  ?  197 ILE A CG2 1 
ATOM   2864 C  CD1 A ILE A 1 197 ? 28.93500 27.72300 -1.58600  0.670 47.31000  ?  197 ILE A CD1 1 
ATOM   2865 C  CD1 B ILE A 1 197 ? 28.46400 28.36300 -1.29900  0.330 41.82000  ?  197 ILE A CD1 1 
ATOM   2866 N  N   A VAL A 1 198 ? 32.55900 29.99500 -5.36600  0.670 26.98000  ?  198 VAL A N   1 
ATOM   2867 N  N   B VAL A 1 198 ? 32.41200 29.82900 -5.31500  0.330 27.47000  ?  198 VAL A N   1 
ATOM   2868 C  CA  A VAL A 1 198 ? 33.77900 30.64500 -5.84100  0.670 30.38000  ?  198 VAL A CA  1 
ATOM   2869 C  CA  B VAL A 1 198 ? 33.68800 30.41000 -5.77600  0.330 31.07000  ?  198 VAL A CA  1 
ATOM   2870 C  C   A VAL A 1 198 ? 33.42200 31.87200 -6.67000  0.670 26.99000  ?  198 VAL A C   1 
ATOM   2871 C  C   B VAL A 1 198 ? 33.41700 31.67900 -6.56500  0.330 27.49000  ?  198 VAL A C   1 
ATOM   2872 O  O   A VAL A 1 198 ? 34.05800 32.92800 -6.55500  0.670 29.42000  ?  198 VAL A O   1 
ATOM   2873 O  O   B VAL A 1 198 ? 33.93200 32.76500 -6.26300  0.330 29.46000  ?  198 VAL A O   1 
ATOM   2874 C  CB  A VAL A 1 198 ? 34.66100 29.67000 -6.64400  0.670 33.62000  ?  198 VAL A CB  1 
ATOM   2875 C  CB  B VAL A 1 198 ? 34.46000 29.40200 -6.64100  0.330 33.03000  ?  198 VAL A CB  1 
ATOM   2876 C  CG1 A VAL A 1 198 ? 35.76000 30.44600 -7.36900  0.670 32.68000  ?  198 VAL A CG1 1 
ATOM   2877 C  CG1 B VAL A 1 198 ? 35.55000 30.09300 -7.42800  0.330 32.38000  ?  198 VAL A CG1 1 
ATOM   2878 C  CG2 A VAL A 1 198 ? 35.25800 28.61500 -5.73900  0.670 37.14000  ?  198 VAL A CG2 1 
ATOM   2879 C  CG2 B VAL A 1 198 ? 35.01200 28.29300 -5.78700  0.330 34.48000  ?  198 VAL A CG2 1 
ATOM   2880 N  N   A TYR A 1 199 ? 32.40200 31.75300 -7.52300  0.670 25.62000  ?  199 TYR A N   1 
ATOM   2881 N  N   B TYR A 1 199 ? 32.53500 31.55900 -7.54200  0.330 25.20000  ?  199 TYR A N   1 
ATOM   2882 C  CA  A TYR A 1 199 ? 31.98300 32.89700 -8.32300  0.670 29.37000  ?  199 TYR A CA  1 
ATOM   2883 C  CA  B TYR A 1 199 ? 32.01600 32.69900 -8.28000  0.330 29.47000  ?  199 TYR A CA  1 
ATOM   2884 C  C   A TYR A 1 199 ? 31.51800 34.04200 -7.43300  0.670 28.65000  ?  199 TYR A C   1 
ATOM   2885 C  C   B TYR A 1 199 ? 31.49100 33.81400 -7.35600  0.330 28.08000  ?  199 TYR A C   1 
ATOM   2886 O  O   A TYR A 1 199 ? 31.89400 35.20100 -7.64000  0.670 36.47000  ?  199 TYR A O   1 
ATOM   2887 O  O   B TYR A 1 199 ? 32.05100 34.92400 -7.35100  0.330 34.18000  ?  199 TYR A O   1 
ATOM   2888 C  CB  A TYR A 1 199 ? 30.86600 32.50200 -9.28600  0.670 30.39000  ?  199 TYR A CB  1 
ATOM   2889 C  CB  B TYR A 1 199 ? 30.94500 32.17900 -9.26100  0.330 29.63000  ?  199 TYR A CB  1 
ATOM   2890 C  CG  A TYR A 1 199 ? 30.30500 33.70200 -10.02200 0.670 27.69000  ?  199 TYR A CG  1 
ATOM   2891 C  CG  B TYR A 1 199 ? 30.29700 33.27100 -9.96000  0.330 26.07000  ?  199 TYR A CG  1 
ATOM   2892 C  CD1 A TYR A 1 199 ? 30.95400 34.21600 -11.13700 0.670 22.30000  ?  199 TYR A CD1 1 
ATOM   2893 C  CD1 B TYR A 1 199 ? 30.93900 33.84800 -11.02300 0.330 24.40000  ?  199 TYR A CD1 1 
ATOM   2894 C  CD2 A TYR A 1 199 ? 29.14600 34.33700 -9.58700  0.670 27.76000  ?  199 TYR A CD2 1 
ATOM   2895 C  CD2 B TYR A 1 199 ? 29.06700 33.78900 -9.54400  0.330 26.00000  ?  199 TYR A CD2 1 
ATOM   2896 C  CE1 A TYR A 1 199 ? 30.46400 35.31300 -11.80800 0.670 23.32000  ?  199 TYR A CE1 1 
ATOM   2897 C  CE1 B TYR A 1 199 ? 30.39400 34.90400 -11.69700 0.330 25.03000  ?  199 TYR A CE1 1 
ATOM   2898 C  CE2 A TYR A 1 199 ? 28.64500 35.44200 -10.25300 0.670 30.07000  ?  199 TYR A CE2 1 
ATOM   2899 C  CE2 B TYR A 1 199 ? 28.53200 34.86900 -10.21500 0.330 29.58000  ?  199 TYR A CE2 1 
ATOM   2900 C  CZ  A TYR A 1 199 ? 29.30900 35.92500 -11.36700 0.670 27.04000  ?  199 TYR A CZ  1 
ATOM   2901 C  CZ  B TYR A 1 199 ? 29.20400 35.39000 -11.31800 0.330 27.13000  ?  199 TYR A CZ  1 
ATOM   2902 O  OH  A TYR A 1 199 ? 28.83200 37.02500 -12.04800 0.670 25.31000  ?  199 TYR A OH  1 
ATOM   2903 O  OH  B TYR A 1 199 ? 28.69700 36.45400 -12.03500 0.330 27.69000  ?  199 TYR A OH  1 
ATOM   2904 N  N   A LEU A 1 200 ? 30.69500 33.73200 -6.42700  0.670 24.28000  ?  200 LEU A N   1 
ATOM   2905 N  N   B LEU A 1 200 ? 30.40200 33.54900 -6.57800  0.330 24.09000  ?  200 LEU A N   1 
ATOM   2906 C  CA  A LEU A 1 200 ? 30.15300 34.78000 -5.56400  0.670 26.18000  ?  200 LEU A CA  1 
ATOM   2907 C  CA  B LEU A 1 200 ? 29.84900 34.55100 -5.65400  0.330 25.06000  ?  200 LEU A CA  1 
ATOM   2908 C  C   A LEU A 1 200 ? 31.25400 35.43200 -4.73200  0.670 23.01000  ?  200 LEU A C   1 
ATOM   2909 C  C   B LEU A 1 200 ? 30.94300 35.25900 -4.84600  0.330 24.38000  ?  200 LEU A C   1 
ATOM   2910 O  O   A LEU A 1 200 ? 31.30300 36.66200 -4.60200  0.670 28.80000  ?  200 LEU A O   1 
ATOM   2911 O  O   B LEU A 1 200 ? 30.79300 36.42900 -4.51900  0.330 26.22000  ?  200 LEU A O   1 
ATOM   2912 C  CB  A LEU A 1 200 ? 29.06200 34.20600 -4.65600  0.670 29.16000  ?  200 LEU A CB  1 
ATOM   2913 C  CB  B LEU A 1 200 ? 28.83300 33.93100 -4.68700  0.330 30.72000  ?  200 LEU A CB  1 
ATOM   2914 C  CG  A LEU A 1 200 ? 27.73800 33.83500 -5.32300  0.670 34.46000  ?  200 LEU A CG  1 
ATOM   2915 C  CG  B LEU A 1 200 ? 27.37600 33.49800 -4.86900  0.330 30.97000  ?  200 LEU A CG  1 
ATOM   2916 C  CD1 A LEU A 1 200 ? 26.87000 33.00800 -4.36900  0.670 30.60000  ?  200 LEU A CD1 1 
ATOM   2917 C  CD1 B LEU A 1 200 ? 27.13500 32.68700 -3.61100  0.330 30.19000  ?  200 LEU A CD1 1 
ATOM   2918 C  CD2 A LEU A 1 200 ? 26.97400 35.05900 -5.79400  0.670 27.94000  ?  200 LEU A CD2 1 
ATOM   2919 C  CD2 B LEU A 1 200 ? 26.41000 34.63800 -5.01900  0.330 25.70000  ?  200 LEU A CD2 1 
ATOM   2920 N  N   A ASP A 1 201 ? 32.14400 34.62200 -4.15200  0.670 24.17000  ?  201 ASP A N   1 
ATOM   2921 N  N   B ASP A 1 201 ? 32.07700 34.60500 -4.57600  0.330 25.47000  ?  201 ASP A N   1 
ATOM   2922 C  CA  A ASP A 1 201 ? 33.26200 35.17900 -3.39300  0.670 28.47000  ?  201 ASP A CA  1 
ATOM   2923 C  CA  B ASP A 1 201 ? 33.12600 35.18400 -3.73100  0.330 29.55000  ?  201 ASP A CA  1 
ATOM   2924 C  C   A ASP A 1 201 ? 34.05700 36.16100 -4.24300  0.670 27.81000  ?  201 ASP A C   1 
ATOM   2925 C  C   B ASP A 1 201 ? 34.16800 35.97800 -4.54500  0.330 28.78000  ?  201 ASP A C   1 
ATOM   2926 O  O   A ASP A 1 201 ? 34.37500 37.27100 -3.80300  0.670 30.97000  ?  201 ASP A O   1 
ATOM   2927 O  O   B ASP A 1 201 ? 34.57700 37.06800 -4.15000  0.330 28.88000  ?  201 ASP A O   1 
ATOM   2928 C  CB  A ASP A 1 201 ? 34.17700 34.06100 -2.88800  0.670 26.67000  ?  201 ASP A CB  1 
ATOM   2929 C  CB  B ASP A 1 201 ? 33.79500 34.04300 -2.92300  0.330 27.24000  ?  201 ASP A CB  1 
ATOM   2930 C  CG  A ASP A 1 201 ? 33.61300 33.33700 -1.67700  0.670 30.43000  ?  201 ASP A CG  1 
ATOM   2931 C  CG  B ASP A 1 201 ? 32.95200 33.55300 -1.76400  0.330 32.14000  ?  201 ASP A CG  1 
ATOM   2932 O  OD1 A ASP A 1 201 ? 32.54200 33.74200 -1.17700  0.670 36.62000  ?  201 ASP A OD1 1 
ATOM   2933 O  OD1 B ASP A 1 201 ? 31.97900 34.22000 -1.33900  0.330 29.95000  ?  201 ASP A OD1 1 
ATOM   2934 O  OD2 A ASP A 1 201 ? 34.24900 32.36000 -1.22700  0.670 40.66000  -1 201 ASP A OD2 1 
ATOM   2935 O  OD2 B ASP A 1 201 ? 33.30800 32.49200 -1.26000  0.330 35.17000  -1 201 ASP A OD2 1 
ATOM   2936 N  N   A LEU A 1 202 ? 34.39300 35.76200 -5.47100  0.670 24.32000  ?  202 LEU A N   1 
ATOM   2937 N  N   B LEU A 1 202 ? 34.54600 35.49200 -5.71500  0.330 26.21000  ?  202 LEU A N   1 
ATOM   2938 C  CA  A LEU A 1 202 ? 35.18200 36.63200 -6.33600  0.670 37.27000  ?  202 LEU A CA  1 
ATOM   2939 C  CA  B LEU A 1 202 ? 35.24900 36.37500 -6.64500  0.330 35.87000  ?  202 LEU A CA  1 
ATOM   2940 C  C   A LEU A 1 202 ? 34.45500 37.94200 -6.61800  0.670 32.29000  ?  202 LEU A C   1 
ATOM   2941 C  C   B LEU A 1 202 ? 34.40800 37.61700 -6.95300  0.330 31.75000  ?  202 LEU A C   1 
ATOM   2942 O  O   A LEU A 1 202 ? 35.07400 39.01200 -6.61800  0.670 28.98000  ?  202 LEU A O   1 
ATOM   2943 O  O   B LEU A 1 202 ? 34.91500 38.74300 -6.82000  0.330 30.61000  ?  202 LEU A O   1 
ATOM   2944 C  CB  A LEU A 1 202 ? 35.51700 35.90700 -7.63800  0.670 31.75000  ?  202 LEU A CB  1 
ATOM   2945 C  CB  B LEU A 1 202 ? 35.59500 35.60600 -7.91200  0.330 31.99000  ?  202 LEU A CB  1 
ATOM   2946 C  CG  A LEU A 1 202 ? 36.60500 34.83600 -7.54200  0.670 31.39000  ?  202 LEU A CG  1 
ATOM   2947 C  CG  B LEU A 1 202 ? 36.41700 34.36700 -7.59600  0.330 29.46000  ?  202 LEU A CG  1 
ATOM   2948 C  CD1 A LEU A 1 202 ? 36.70700 34.03400 -8.83300  0.670 38.66000  ?  202 LEU A CD1 1 
ATOM   2949 C  CD1 B LEU A 1 202 ? 35.97000 33.24800 -8.45400  0.330 33.03000  ?  202 LEU A CD1 1 
ATOM   2950 C  CD2 A LEU A 1 202 ? 37.95800 35.44900 -7.18700  0.670 36.94000  ?  202 LEU A CD2 1 
ATOM   2951 C  CD2 B LEU A 1 202 ? 37.88800 34.62200 -7.81700  0.330 34.20000  ?  202 LEU A CD2 1 
ATOM   2952 N  N   A VAL A 1 203 ? 33.14100 37.89000 -6.84700  0.670 28.56000  ?  203 VAL A N   1 
ATOM   2953 N  N   B VAL A 1 203 ? 33.09500 37.44700 -7.29300  0.330 27.01000  ?  203 VAL A N   1 
ATOM   2954 C  CA  A VAL A 1 203 ? 32.42800 39.11500 -7.20300  0.670 32.12000  ?  203 VAL A CA  1 
ATOM   2955 C  CA  B VAL A 1 203 ? 32.16900 38.59200 -7.37500  0.330 30.22000  ?  203 VAL A CA  1 
ATOM   2956 C  C   A VAL A 1 203 ? 32.22500 40.00000 -5.97500  0.670 32.04000  ?  203 VAL A C   1 
ATOM   2957 C  C   B VAL A 1 203 ? 32.26000 39.45600 -6.10800  0.330 32.54000  ?  203 VAL A C   1 
ATOM   2958 O  O   A VAL A 1 203 ? 32.38500 41.22500 -6.04600  0.670 34.04000  ?  203 VAL A O   1 
ATOM   2959 O  O   B VAL A 1 203 ? 32.70400 40.61000 -6.18800  0.330 30.51000  ?  203 VAL A O   1 
ATOM   2960 C  CB  A VAL A 1 203 ? 31.09000 38.79200 -7.89300  0.670 25.68000  ?  203 VAL A CB  1 
ATOM   2961 C  CB  B VAL A 1 203 ? 30.69600 38.21500 -7.59300  0.330 24.94000  ?  203 VAL A CB  1 
ATOM   2962 C  CG1 A VAL A 1 203 ? 30.29200 40.07400 -8.11700  0.670 33.87000  ?  203 VAL A CG1 1 
ATOM   2963 C  CG1 B VAL A 1 203 ? 29.94100 39.46500 -7.39500  0.330 29.05000  ?  203 VAL A CG1 1 
ATOM   2964 C  CG2 A VAL A 1 203 ? 31.32100 38.07800 -9.21700  0.670 32.07000  ?  203 VAL A CG2 1 
ATOM   2965 C  CG2 B VAL A 1 203 ? 30.41500 37.71900 -8.97300  0.330 28.61000  ?  203 VAL A CG2 1 
ATOM   2966 N  N   A THR A 1 204 ? 31.86800 39.40600 -4.83200  0.670 34.02000  ?  204 THR A N   1 
ATOM   2967 N  N   B THR A 1 204 ? 31.78800 38.93400 -4.92900  0.330 31.56000  ?  204 THR A N   1 
ATOM   2968 C  CA  A THR A 1 204 ? 31.61600 40.21700 -3.64400  0.670 31.25000  ?  204 THR A CA  1 
ATOM   2969 C  CA  B THR A 1 204 ? 31.58600 39.82000 -3.77500  0.330 31.48000  ?  204 THR A CA  1 
ATOM   2970 C  C   A THR A 1 204 ? 32.89200 40.77100 -3.02200  0.670 27.03000  ?  204 THR A C   1 
ATOM   2971 C  C   B THR A 1 204 ? 32.88400 40.27400 -3.15700  0.330 27.45000  ?  204 THR A C   1 
ATOM   2972 O  O   A THR A 1 204 ? 32.80400 41.64300 -2.15000  0.670 39.08000  ?  204 THR A O   1 
ATOM   2973 O  O   B THR A 1 204 ? 32.86500 41.29000 -2.47200  0.330 34.16000  ?  204 THR A O   1 
ATOM   2974 C  CB  A THR A 1 204 ? 30.86000 39.42100 -2.57300  0.670 26.56000  ?  204 THR A CB  1 
ATOM   2975 C  CB  B THR A 1 204 ? 30.75400 39.19500 -2.63800  0.330 29.68000  ?  204 THR A CB  1 
ATOM   2976 O  OG1 A THR A 1 204 ? 31.65700 38.30900 -2.14900  0.670 35.22000  ?  204 THR A OG1 1 
ATOM   2977 O  OG1 B THR A 1 204 ? 31.43400 38.06200 -2.10100  0.330 32.25000  ?  204 THR A OG1 1 
ATOM   2978 C  CG2 A THR A 1 204 ? 29.52800 38.92900 -3.10600  0.670 24.95000  ?  204 THR A CG2 1 
ATOM   2979 C  CG2 B THR A 1 204 ? 29.47500 38.67200 -3.11300  0.330 25.48000  ?  204 THR A CG2 1 
ATOM   2980 N  N   A LYS A 1 205 ? 34.06200 40.27900 -3.42400  0.670 24.22000  ?  205 LYS A N   1 
ATOM   2981 N  N   B LYS A 1 205 ? 34.01800 39.63900 -3.45400  0.330 26.14000  ?  205 LYS A N   1 
ATOM   2982 C  CA  A LYS A 1 205 ? 35.33400 40.77600 -2.91600  0.670 32.88000  ?  205 LYS A CA  1 
ATOM   2983 C  CA  B LYS A 1 205 ? 35.25900 40.10600 -2.77600  0.330 31.56000  ?  205 LYS A CA  1 
ATOM   2984 C  C   A LYS A 1 205 ? 36.13000 41.49900 -3.99500  0.670 35.31000  ?  205 LYS A C   1 
ATOM   2985 C  C   B LYS A 1 205 ? 36.10200 40.97200 -3.73300  0.330 35.50000  ?  205 LYS A C   1 
ATOM   2986 O  O   A LYS A 1 205 ? 36.37500 42.70200 -3.87900  0.670 33.58000  ?  205 LYS A O   1 
ATOM   2987 O  O   B LYS A 1 205 ? 36.56600 42.04400 -3.29100  0.330 30.47000  ?  205 LYS A O   1 
ATOM   2988 C  CB  A LYS A 1 205 ? 36.15400 39.61900 -2.32700  0.670 32.33000  ?  205 LYS A CB  1 
ATOM   2989 C  CB  B LYS A 1 205 ? 36.07500 38.92800 -2.23000  0.330 29.06000  ?  205 LYS A CB  1 
ATOM   2990 C  CG  A LYS A 1 205 ? 35.55600 39.01100 -1.06400  0.670 28.23000  ?  205 LYS A CG  1 
ATOM   2991 C  CG  B LYS A 1 205 ? 35.56800 38.35500 -0.91400  0.330 27.95000  ?  205 LYS A CG  1 
ATOM   2992 C  CD  A LYS A 1 205 ? 36.43200 37.89500 -0.51000  0.670 31.44000  ?  205 LYS A CD  1 
ATOM   2993 C  CD  B LYS A 1 205 ? 35.89700 36.87800 -0.73900  0.330 32.43000  ?  205 LYS A CD  1 
ATOM   2994 C  CE  A LYS A 1 205 ? 36.01400 37.51400 0.90200   0.670 32.44000  ?  205 LYS A CE  1 
ATOM   2995 C  CE  B LYS A 1 205 ? 35.30000 36.29000 0.49900   0.330 26.75000  ?  205 LYS A CE  1 
ATOM   2996 N  NZ  A LYS A 1 205 ? 34.86100 36.56600 0.89700   0.670 21.80000  ?  205 LYS A NZ  1 
ATOM   2997 N  NZ  B LYS A 1 205 ? 33.94100 35.80000 0.24700   0.330 23.46000  ?  205 LYS A NZ  1 
ATOM   2998 N  N   A VAL A 1 206 ? 36.54300 40.79600 -5.05200  0.670 35.16000  ?  206 VAL A N   1 
ATOM   2999 N  N   B VAL A 1 206 ? 36.28500 40.53700 -4.98300  0.330 34.25000  ?  206 VAL A N   1 
ATOM   3000 C  CA  A VAL A 1 206 ? 37.37000 41.42300 -6.07900  0.670 34.59000  ?  206 VAL A CA  1 
ATOM   3001 C  CA  B VAL A 1 206 ? 37.17500 41.28100 -5.93000  0.330 34.38000  ?  206 VAL A CA  1 
ATOM   3002 C  C   A VAL A 1 206 ? 36.54200 42.35500 -6.95200  0.670 31.96000  ?  206 VAL A C   1 
ATOM   3003 C  C   B VAL A 1 206 ? 36.35100 42.29500 -6.74300  0.330 33.30000  ?  206 VAL A C   1 
ATOM   3004 O  O   A VAL A 1 206 ? 36.97800 43.46400 -7.27300  0.670 36.02000  ?  206 VAL A O   1 
ATOM   3005 O  O   B VAL A 1 206 ? 36.71700 43.48900 -6.73700  0.330 24.67000  ?  206 VAL A O   1 
ATOM   3006 C  CB  A VAL A 1 206 ? 38.08300 40.34600 -6.91700  0.670 37.58000  ?  206 VAL A CB  1 
ATOM   3007 C  CB  B VAL A 1 206 ? 37.93700 40.30800 -6.85000  0.330 36.93000  ?  206 VAL A CB  1 
ATOM   3008 C  CG1 A VAL A 1 206 ? 38.93500 40.98300 -8.00500  0.670 38.28000  ?  206 VAL A CG1 1 
ATOM   3009 C  CG1 B VAL A 1 206 ? 39.01900 41.02000 -7.65100  0.330 34.05000  ?  206 VAL A CG1 1 
ATOM   3010 C  CG2 A VAL A 1 206 ? 38.92400 39.44800 -6.01300  0.670 31.27000  ?  206 VAL A CG2 1 
ATOM   3011 C  CG2 B VAL A 1 206 ? 38.52800 39.14000 -6.07000  0.330 32.76000  ?  206 VAL A CG2 1 
ATOM   3012 N  N   A GLY A 1 207 ? 35.34600 41.92900 -7.35800  0.670 31.84000  ?  207 GLY A N   1 
ATOM   3013 N  N   B GLY A 1 207 ? 35.29600 41.83700 -7.42100  0.330 34.57000  ?  207 GLY A N   1 
ATOM   3014 C  CA  A GLY A 1 207 ? 34.48300 42.82500 -8.11200  0.670 28.50000  ?  207 GLY A CA  1 
ATOM   3015 C  CA  B GLY A 1 207 ? 34.45200 42.74200 -8.22600  0.330 31.22000  ?  207 GLY A CA  1 
ATOM   3016 C  C   A GLY A 1 207 ? 34.13700 44.07100 -7.32300  0.670 40.81000  ?  207 GLY A C   1 
ATOM   3017 C  C   B GLY A 1 207 ? 34.11800 43.99800 -7.44900  0.330 37.21000  ?  207 GLY A C   1 
ATOM   3018 O  O   A GLY A 1 207 ? 34.28600 45.19400 -7.80900  0.670 40.89000  ?  207 GLY A O   1 
ATOM   3019 O  O   B GLY A 1 207 ? 34.40300 45.10100 -7.95800  0.330 40.55000  ?  207 GLY A O   1 
ATOM   3020 N  N   A PHE A 1 208 ? 33.65400 43.88200 -6.09400  0.670 42.31000  ?  208 PHE A N   1 
ATOM   3021 N  N   B PHE A 1 208 ? 33.54100 43.84300 -6.25500  0.330 37.66000  ?  208 PHE A N   1 
ATOM   3022 C  CA  A PHE A 1 208 ? 33.49600 44.96500 -5.12900  0.670 29.95000  ?  208 PHE A CA  1 
ATOM   3023 C  CA  B PHE A 1 208 ? 33.20700 45.00300 -5.38600  0.330 37.04000  ?  208 PHE A CA  1 
ATOM   3024 C  C   A PHE A 1 208 ? 34.68300 45.91600 -5.16100  0.670 35.21000  ?  208 PHE A C   1 
ATOM   3025 C  C   B PHE A 1 208 ? 34.38200 45.97300 -5.35100  0.330 36.52000  ?  208 PHE A C   1 
ATOM   3026 O  O   A PHE A 1 208 ? 34.52200 47.12600 -5.35500  0.670 37.68000  ?  208 PHE A O   1 
ATOM   3027 O  O   B PHE A 1 208 ? 34.17700 47.18600 -5.56400  0.330 45.01000  ?  208 PHE A O   1 
ATOM   3028 C  CB  A PHE A 1 208 ? 33.31700 44.32400 -3.74500  0.670 38.40000  ?  208 PHE A CB  1 
ATOM   3029 C  CB  B PHE A 1 208 ? 32.88200 44.39900 -4.01900  0.330 37.15000  ?  208 PHE A CB  1 
ATOM   3030 C  CG  A PHE A 1 208 ? 32.99000 45.28000 -2.63600  0.670 35.94000  ?  208 PHE A CG  1 
ATOM   3031 C  CG  B PHE A 1 208 ? 32.61700 45.37300 -2.88000  0.330 32.95000  ?  208 PHE A CG  1 
ATOM   3032 C  CD1 A PHE A 1 208 ? 33.99800 45.91700 -1.93200  0.670 39.59000  ?  208 PHE A CD1 1 
ATOM   3033 C  CD1 B PHE A 1 208 ? 31.33000 45.82300 -2.61300  0.330 36.82000  ?  208 PHE A CD1 1 
ATOM   3034 C  CD2 A PHE A 1 208 ? 31.67600 45.49000 -2.25300  0.670 34.07000  ?  208 PHE A CD2 1 
ATOM   3035 C  CD2 B PHE A 1 208 ? 33.65000 45.80700 -2.05600  0.330 36.97000  ?  208 PHE A CD2 1 
ATOM   3036 C  CE1 A PHE A 1 208 ? 33.70000 46.77700 -0.89300  0.670 36.55000  ?  208 PHE A CE1 1 
ATOM   3037 C  CE1 B PHE A 1 208 ? 31.08700 46.69700 -1.56600  0.330 36.70000  ?  208 PHE A CE1 1 
ATOM   3038 C  CE2 A PHE A 1 208 ? 31.37100 46.34900 -1.21400  0.670 36.27000  ?  208 PHE A CE2 1 
ATOM   3039 C  CE2 B PHE A 1 208 ? 33.40100 46.68200 -1.01200  0.330 38.82000  ?  208 PHE A CE2 1 
ATOM   3040 C  CZ  A PHE A 1 208 ? 32.38500 46.99300 -0.53200  0.670 37.53000  ?  208 PHE A CZ  1 
ATOM   3041 C  CZ  B PHE A 1 208 ? 32.12200 47.12400 -0.77000  0.330 38.63000  ?  208 PHE A CZ  1 
ATOM   3042 N  N   A GLY A 1 209 ? 35.88800 45.37500 -4.99500  0.670 41.48000  ?  209 GLY A N   1 
ATOM   3043 N  N   B GLY A 1 209 ? 35.58500 45.45800 -5.08700  0.330 36.59000  ?  209 GLY A N   1 
ATOM   3044 C  CA  A GLY A 1 209 ? 37.06300 46.22400 -4.93400  0.670 37.70000  ?  209 GLY A CA  1 
ATOM   3045 C  CA  B GLY A 1 209 ? 36.77800 46.32000 -4.98300  0.330 40.40000  ?  209 GLY A CA  1 
ATOM   3046 C  C   A GLY A 1 209 ? 37.27200 47.03700 -6.19600  0.670 42.65000  ?  209 GLY A C   1 
ATOM   3047 C  C   B GLY A 1 209 ? 37.02000 47.11600 -6.25000  0.330 45.06000  ?  209 GLY A C   1 
ATOM   3048 O  O   A GLY A 1 209 ? 37.56800 48.23300 -6.13200  0.670 47.54000  ?  209 GLY A O   1 
ATOM   3049 O  O   B GLY A 1 209 ? 37.36200 48.30900 -6.14100  0.330 46.25000  ?  209 GLY A O   1 
ATOM   3050 N  N   A PHE A 1 210 ? 37.11800 46.40600 -7.36100  0.670 48.18000  ?  210 PHE A N   1 
ATOM   3051 N  N   B PHE A 1 210 ? 36.86600 46.47900 -7.41300  0.330 44.02000  ?  210 PHE A N   1 
ATOM   3052 C  CA  A PHE A 1 210 ? 37.39500 47.11600 -8.60300  0.670 42.53000  ?  210 PHE A CA  1 
ATOM   3053 C  CA  B PHE A 1 210 ? 37.09500 47.17300 -8.71000  0.330 42.33000  ?  210 PHE A CA  1 
ATOM   3054 C  C   A PHE A 1 210 ? 36.36600 48.20600 -8.86900  0.670 46.65000  ?  210 PHE A C   1 
ATOM   3055 C  C   B PHE A 1 210 ? 35.99100 48.21000 -8.91300  0.330 47.29000  ?  210 PHE A C   1 
ATOM   3056 O  O   A PHE A 1 210 ? 36.70500 49.24000 -9.45500  0.670 54.48000  ?  210 PHE A O   1 
ATOM   3057 O  O   B PHE A 1 210 ? 36.29900 49.34000 -9.34500  0.330 51.29000  ?  210 PHE A O   1 
ATOM   3058 C  CB  A PHE A 1 210 ? 37.46400 46.12800 -9.76500  0.670 29.60000  ?  210 PHE A CB  1 
ATOM   3059 C  CB  B PHE A 1 210 ? 37.18400 46.13800 -9.83500  0.330 35.10000  ?  210 PHE A CB  1 
ATOM   3060 C  CG  A PHE A 1 210 ? 38.81200 45.48200 -9.91900  0.670 46.89000  ?  210 PHE A CG  1 
ATOM   3061 C  CG  B PHE A 1 210 ? 38.53400 45.44000 -9.89700  0.330 44.39000  ?  210 PHE A CG  1 
ATOM   3062 C  CD1 A PHE A 1 210 ? 39.94500 46.25100 -10.14300 0.670 52.70000  ?  210 PHE A CD1 1 
ATOM   3063 C  CD1 B PHE A 1 210 ? 39.71400 46.17300 -9.86200  0.330 49.89000  ?  210 PHE A CD1 1 
ATOM   3064 C  CD2 A PHE A 1 210 ? 38.95100 44.11000 -9.82600  0.670 42.80000  ?  210 PHE A CD2 1 
ATOM   3065 C  CD2 B PHE A 1 210 ? 38.62100 44.05600 -9.97800  0.330 42.91000  ?  210 PHE A CD2 1 
ATOM   3066 C  CE1 A PHE A 1 210 ? 41.18400 45.66200 -10.28000 0.670 60.19000  ?  210 PHE A CE1 1 
ATOM   3067 C  CE1 B PHE A 1 210 ? 40.94400 45.53800 -9.91400  0.330 56.66000  ?  210 PHE A CE1 1 
ATOM   3068 C  CE2 A PHE A 1 210 ? 40.19100 43.51400 -9.96200  0.670 38.91000  ?  210 PHE A CE2 1 
ATOM   3069 C  CE2 B PHE A 1 210 ? 39.85500 43.42700 -10.03200 0.330 44.68000  ?  210 PHE A CE2 1 
ATOM   3070 C  CZ  A PHE A 1 210 ? 41.30900 44.29200 -10.18900 0.670 53.57000  ?  210 PHE A CZ  1 
ATOM   3071 C  CZ  B PHE A 1 210 ? 41.01200 44.16800 -9.99900  0.330 51.90000  ?  210 PHE A CZ  1 
ATOM   3072 N  N   A ILE A 1 211 ? 35.11600 48.01000 -8.44400  0.670 46.94000  ?  211 ILE A N   1 
ATOM   3073 N  N   B ILE A 1 211 ? 34.74400 47.84400 -8.60200  0.330 50.31000  ?  211 ILE A N   1 
ATOM   3074 C  CA  A ILE A 1 211 ? 34.14100 49.09000 -8.56000  0.670 51.05000  ?  211 ILE A CA  1 
ATOM   3075 C  CA  B ILE A 1 211 ? 33.61600 48.82000 -8.69600  0.330 46.34000  ?  211 ILE A CA  1 
ATOM   3076 C  C   A ILE A 1 211 ? 34.57000 50.28100 -7.71500  0.670 63.27000  ?  211 ILE A C   1 
ATOM   3077 C  C   B ILE A 1 211 ? 33.93700 49.99900 -7.76600  0.330 54.82000  ?  211 ILE A C   1 
ATOM   3078 O  O   A ILE A 1 211 ? 34.33600 51.43500 -8.09100  0.670 71.40000  ?  211 ILE A O   1 
ATOM   3079 O  O   B ILE A 1 211 ? 33.61200 51.15000 -8.12500  0.330 61.38000  ?  211 ILE A O   1 
ATOM   3080 C  CB  A ILE A 1 211 ? 32.73600 48.60000 -8.16400  0.670 45.39000  ?  211 ILE A CB  1 
ATOM   3081 C  CB  B ILE A 1 211 ? 32.27800 48.15200 -8.33200  0.330 46.98000  ?  211 ILE A CB  1 
ATOM   3082 C  CG1 A ILE A 1 211 ? 32.18400 47.64300 -9.22000  0.670 47.84000  ?  211 ILE A CG1 1 
ATOM   3083 C  CG1 B ILE A 1 211 ? 31.95800 46.99000 -9.27000  0.330 48.98000  ?  211 ILE A CG1 1 
ATOM   3084 C  CG2 A ILE A 1 211 ? 31.79900 49.78600 -7.97800  0.670 46.04000  ?  211 ILE A CG2 1 
ATOM   3085 C  CG2 B ILE A 1 211 ? 31.14200 49.17400 -8.29300  0.330 45.66000  ?  211 ILE A CG2 1 
ATOM   3086 C  CD1 A ILE A 1 211 ? 31.10600 46.71800 -8.69400  0.670 49.77000  ?  211 ILE A CD1 1 
ATOM   3087 C  CD1 B ILE A 1 211 ? 31.02300 45.95500 -8.67200  0.330 49.26000  ?  211 ILE A CD1 1 
ATOM   3088 N  N   A ALA A 1 212 ? 35.20300 50.02800 -6.56600  0.670 65.24000  ?  212 ALA A N   1 
ATOM   3089 N  N   B ALA A 1 212 ? 34.55400 49.71700 -6.61600  0.330 53.40000  ?  212 ALA A N   1 
ATOM   3090 C  CA  A ALA A 1 212 ? 35.68800 51.12400 -5.73600  0.670 65.51000  ?  212 ALA A CA  1 
ATOM   3091 C  CA  B ALA A 1 212 ? 34.95400 50.80000 -5.68900  0.330 60.37000  ?  212 ALA A CA  1 
ATOM   3092 C  C   A ALA A 1 212 ? 36.86400 51.82900 -6.40000  0.670 64.63000  ?  212 ALA A C   1 
ATOM   3093 C  C   B ALA A 1 212 ? 36.06400 51.62900 -6.33600  0.330 61.80000  ?  212 ALA A C   1 
ATOM   3094 O  O   A ALA A 1 212 ? 36.91000 53.06300 -6.45600  0.670 70.86000  ?  212 ALA A O   1 
ATOM   3095 O  O   B ALA A 1 212 ? 35.96500 52.87500 -6.33100  0.330 62.21000  ?  212 ALA A O   1 
ATOM   3096 C  CB  A ALA A 1 212 ? 36.07800 50.60100 -4.35300  0.670 51.81000  ?  212 ALA A CB  1 
ATOM   3097 C  CB  B ALA A 1 212 ? 35.40000 50.21500 -4.37000  0.330 55.87000  ?  212 ALA A CB  1 
ATOM   3098 N  N   A LEU A 1 213 ? 37.82200 51.05800 -6.92200  0.670 56.80000  ?  213 LEU A N   1 
ATOM   3099 N  N   B LEU A 1 213 ? 37.08500 50.96200 -6.88200  0.330 59.71000  ?  213 LEU A N   1 
ATOM   3100 C  CA  A LEU A 1 213 ? 38.95200 51.66100 -7.62200  0.670 59.70000  ?  213 LEU A CA  1 
ATOM   3101 C  CA  B LEU A 1 213 ? 38.21600 51.70000 -7.45200  0.330 59.96000  ?  213 LEU A CA  1 
ATOM   3102 C  C   A LEU A 1 213 ? 38.47200 52.54500 -8.76700  0.670 68.72000  ?  213 LEU A C   1 
ATOM   3103 C  C   B LEU A 1 213 ? 37.77800 52.60000 -8.59700  0.330 68.62000  ?  213 LEU A C   1 
ATOM   3104 O  O   A LEU A 1 213 ? 38.95300 53.67100 -8.94500  0.670 78.36000  ?  213 LEU A O   1 
ATOM   3105 O  O   B LEU A 1 213 ? 38.18900 53.76400 -8.69000  0.330 73.08000  ?  213 LEU A O   1 
ATOM   3106 C  CB  A LEU A 1 213 ? 39.88400 50.57600 -8.15700  0.670 49.57000  ?  213 LEU A CB  1 
ATOM   3107 C  CB  B LEU A 1 213 ? 39.31800 50.73200 -7.92300  0.330 54.14000  ?  213 LEU A CB  1 
ATOM   3108 C  CG  A LEU A 1 213 ? 40.71700 49.75700 -7.17500  0.670 72.13000  ?  213 LEU A CG  1 
ATOM   3109 C  CG  B LEU A 1 213 ? 40.24200 50.06600 -6.87500  0.330 66.28000  ?  213 LEU A CG  1 
ATOM   3110 C  CD1 A LEU A 1 213 ? 41.74000 48.92500 -7.96300  0.670 57.39000  ?  213 LEU A CD1 1 
ATOM   3111 C  CD1 B LEU A 1 213 ? 41.53300 49.40700 -7.49500  0.330 62.49000  ?  213 LEU A CD1 1 
ATOM   3112 C  CD2 A LEU A 1 213 ? 41.41100 50.62200 -6.15400  0.670 60.00000  ?  213 LEU A CD2 1 
ATOM   3113 C  CD2 B LEU A 1 213 ? 40.62100 51.02200 -5.74000  0.330 60.38000  ?  213 LEU A CD2 1 
ATOM   3114 N  N   A ASP A 1 214 ? 37.52600 52.04000 -9.56300  0.670 69.72000  ?  214 ASP A N   1 
ATOM   3115 N  N   B ASP A 1 214 ? 36.90800 52.03700 -9.43700  0.330 70.18000  ?  214 ASP A N   1 
ATOM   3116 C  CA  A ASP A 1 214 ? 37.03500 52.80000 -10.70700 0.670 70.50000  ?  214 ASP A CA  1 
ATOM   3117 C  CA  B ASP A 1 214 ? 36.24000 52.74300 -10.52400 0.330 71.94000  ?  214 ASP A CA  1 
ATOM   3118 C  C   A ASP A 1 214 ? 36.52600 54.17000 -10.28200 0.670 80.20000  ?  214 ASP A C   1 
ATOM   3119 C  C   B ASP A 1 214 ? 36.02900 54.21600 -10.21500 0.330 79.45000  ?  214 ASP A C   1 
ATOM   3120 O  O   A ASP A 1 214 ? 36.76800 55.17200 -10.96600 0.670 93.01000  ?  214 ASP A O   1 
ATOM   3121 O  O   B ASP A 1 214 ? 36.41100 55.08700 -11.00000 0.330 90.58000  ?  214 ASP A O   1 
ATOM   3122 C  CB  A ASP A 1 214 ? 35.93000 52.01600 -11.41500 0.670 75.92000  ?  214 ASP A CB  1 
ATOM   3123 C  CB  B ASP A 1 214 ? 34.89200 52.08500 -10.77300 0.330 72.53000  ?  214 ASP A CB  1 
ATOM   3124 C  CG  A ASP A 1 214 ? 35.55600 52.61800 -12.75200 0.670 78.92000  ?  214 ASP A CG  1 
ATOM   3125 C  CG  B ASP A 1 214 ? 34.34600 52.38600 -12.12000 0.330 78.15000  ?  214 ASP A CG  1 
ATOM   3126 O  OD1 A ASP A 1 214 ? 36.46600 52.86300 -13.56900 0.670 85.34000  ?  214 ASP A OD1 1 
ATOM   3127 O  OD1 B ASP A 1 214 ? 35.00100 52.02300 -13.12400 0.330 79.93000  ?  214 ASP A OD1 1 
ATOM   3128 O  OD2 A ASP A 1 214 ? 34.35000 52.84900 -12.98400 0.670 83.99000  -1 214 ASP A OD2 1 
ATOM   3129 O  OD2 B ASP A 1 214 ? 33.27900 53.01300 -12.15700 0.330 76.53000  -1 214 ASP A OD2 1 
ATOM   3130 N  N   A ALA A 1 215 ? 35.81800 54.23600 -9.15300  0.670 73.84000  ?  215 ALA A N   1 
ATOM   3131 N  N   B ALA A 1 215 ? 35.42000 54.51300 -9.06800  0.330 74.29000  ?  215 ALA A N   1 
ATOM   3132 C  CA  A ALA A 1 215 ? 35.27600 55.51000 -8.69900  0.670 74.71000  ?  215 ALA A CA  1 
ATOM   3133 C  CA  B ALA A 1 215 ? 35.00000 55.87900 -8.77300  0.330 75.36000  ?  215 ALA A CA  1 
ATOM   3134 C  C   A ALA A 1 215 ? 36.36200 56.41100 -8.12500  0.670 84.89000  ?  215 ALA A C   1 
ATOM   3135 C  C   B ALA A 1 215 ? 36.17400 56.87000 -8.84000  0.330 81.12000  ?  215 ALA A C   1 
ATOM   3136 O  O   A ALA A 1 215 ? 36.25600 57.64000 -8.21400  0.670 81.56000  ?  215 ALA A O   1 
ATOM   3137 O  O   B ALA A 1 215 ? 36.11800 57.87300 -9.57200  0.330 78.22000  ?  215 ALA A O   1 
ATOM   3138 C  CB  A ALA A 1 215 ? 34.17700 55.27200 -7.66300  0.670 55.92000  ?  215 ALA A CB  1 
ATOM   3139 C  CB  B ALA A 1 215 ? 34.32300 55.88000 -7.40700  0.330 63.99000  ?  215 ALA A CB  1 
ATOM   3140 N  N   A ALA A 1 216 ? 37.41100 55.82700 -7.54200  0.670 80.42000  ?  216 ALA A N   1 
ATOM   3141 N  N   B ALA A 1 216 ? 37.26400 56.56900 -8.11900  0.330 81.62000  ?  216 ALA A N   1 
ATOM   3142 C  CA  A ALA A 1 216 ? 38.47900 56.63000 -6.95800  0.670 85.89000  ?  216 ALA A CA  1 
ATOM   3143 C  CA  B ALA A 1 216 ? 38.40100 57.48000 -7.91600  0.330 82.70000  ?  216 ALA A CA  1 
ATOM   3144 C  C   A ALA A 1 216 ? 39.26400 57.40400 -8.01000  0.670 82.54000  ?  216 ALA A C   1 
ATOM   3145 C  C   B ALA A 1 216 ? 39.32500 57.59400 -9.13200  0.330 78.29000  ?  216 ALA A C   1 
ATOM   3146 O  O   A ALA A 1 216 ? 39.90500 58.40600 -7.67300  0.670 96.23000  ?  216 ALA A O   1 
ATOM   3147 O  O   B ALA A 1 216 ? 40.55700 57.51200 -8.99100  0.330 82.11000  ?  216 ALA A O   1 
ATOM   3148 C  CB  A ALA A 1 216 ? 39.43100 55.74100 -6.15500  0.670 73.48000  ?  216 ALA A CB  1 
ATOM   3149 C  CB  B ALA A 1 216 ? 39.22600 57.02800 -6.67800  0.330 77.74000  ?  216 ALA A CB  1 
HETATM 3150 C  C1  A RET B 2 .   ? 25.06100 31.73800 5.61700   0.710 39.10000  ?  301 RET A C1  1 
HETATM 3151 C  C1  B RET B 2 .   ? 24.75100 31.79900 5.39700   0.290 34.88000  ?  301 RET A C1  1 
HETATM 3152 C  C2  A RET B 2 .   ? 24.20700 30.70600 6.36900   0.710 26.41000  ?  301 RET A C2  1 
HETATM 3153 C  C2  B RET B 2 .   ? 23.68700 30.82400 5.94400   0.290 31.48000  ?  301 RET A C2  1 
HETATM 3154 C  C3  A RET B 2 .   ? 23.32200 31.28700 7.45900   0.710 30.16000  ?  301 RET A C3  1 
HETATM 3155 C  C3  B RET B 2 .   ? 22.65300 31.46000 6.85200   0.290 29.07000  ?  301 RET A C3  1 
HETATM 3156 C  C4  A RET B 2 .   ? 22.41300 32.36800 6.91000   0.710 29.02000  ?  301 RET A C4  1 
HETATM 3157 C  C4  B RET B 2 .   ? 21.97700 32.60300 6.13800   0.290 28.72000  ?  301 RET A C4  1 
HETATM 3158 C  C5  A RET B 2 .   ? 23.06800 33.26700 5.89500   0.710 31.45000  ?  301 RET A C5  1 
HETATM 3159 C  C5  B RET B 2 .   ? 22.93600 33.55500 5.52000   0.290 30.14000  ?  301 RET A C5  1 
HETATM 3160 C  C6  A RET B 2 .   ? 24.32800 33.07800 5.46400   0.710 35.19000  ?  301 RET A C6  1 
HETATM 3161 C  C6  B RET B 2 .   ? 24.21800 33.24300 5.25100   0.290 31.51000  ?  301 RET A C6  1 
HETATM 3162 C  C7  A RET B 2 .   ? 25.02200 34.13200 4.73900   0.710 23.21000  ?  301 RET A C7  1 
HETATM 3163 C  C7  B RET B 2 .   ? 25.04600 34.25900 4.59800   0.290 26.85000  ?  301 RET A C7  1 
HETATM 3164 C  C8  A RET B 2 .   ? 26.22600 34.09700 4.11300   0.710 24.30000  ?  301 RET A C8  1 
HETATM 3165 C  C8  B RET B 2 .   ? 26.22700 34.33400 3.75600   0.290 27.70000  ?  301 RET A C8  1 
HETATM 3166 C  C9  A RET B 2 .   ? 26.86500 35.20400 3.41500   0.710 24.95000  ?  301 RET A C9  1 
HETATM 3167 C  C9  B RET B 2 .   ? 26.80800 35.59500 3.19400   0.290 24.51000  ?  301 RET A C9  1 
HETATM 3168 C  C10 A RET B 2 .   ? 28.14100 35.05500 2.98000   0.710 29.47000  ?  301 RET A C10 1 
HETATM 3169 C  C10 B RET B 2 .   ? 28.09400 35.60800 2.73700   0.290 25.36000  ?  301 RET A C10 1 
HETATM 3170 C  C11 A RET B 2 .   ? 28.96200 36.03200 2.32100   0.710 23.39000  ?  301 RET A C11 1 
HETATM 3171 C  C11 B RET B 2 .   ? 28.85100 36.71800 2.21300   0.290 23.74000  ?  301 RET A C11 1 
HETATM 3172 C  C12 A RET B 2 .   ? 30.25100 35.80400 2.02800   0.710 30.12000  ?  301 RET A C12 1 
HETATM 3173 C  C12 B RET B 2 .   ? 30.16800 36.62200 1.87800   0.290 27.25000  ?  301 RET A C12 1 
HETATM 3174 C  C13 A RET B 2 .   ? 31.18500 36.73800 1.42300   0.710 30.00000  ?  301 RET A C13 1 
HETATM 3175 C  C13 B RET B 2 .   ? 31.07000 37.65700 1.36000   0.290 26.52000  ?  301 RET A C13 1 
HETATM 3176 C  C14 A RET B 2 .   ? 32.49100 36.39000 1.32400   0.710 19.32000  ?  301 RET A C14 1 
HETATM 3177 C  C14 B RET B 2 .   ? 32.36600 37.34900 1.03600   0.290 25.23000  ?  301 RET A C14 1 
HETATM 3178 C  C15 A RET B 2 .   ? 33.57000 37.18400 0.79500   0.710 21.58000  ?  301 RET A C15 1 
HETATM 3179 C  C15 B RET B 2 .   ? 33.03700 36.07500 1.09200   0.290 25.25000  ?  301 RET A C15 1 
HETATM 3180 C  C16 A RET B 2 .   ? 26.36500 31.92600 6.40300   0.710 35.05000  ?  301 RET A C16 1 
HETATM 3181 C  C16 B RET B 2 .   ? 25.92600 31.75700 6.38000   0.290 34.06000  ?  301 RET A C16 1 
HETATM 3182 C  C17 A RET B 2 .   ? 25.39300 31.14200 4.24200   0.710 32.63000  ?  301 RET A C17 1 
HETATM 3183 C  C17 B RET B 2 .   ? 25.21200 31.24700 4.04200   0.290 32.90000  ?  301 RET A C17 1 
HETATM 3184 C  C18 A RET B 2 .   ? 22.29300 34.53900 5.68700   0.710 31.38000  ?  301 RET A C18 1 
HETATM 3185 C  C18 B RET B 2 .   ? 22.32900 34.90500 5.29400   0.290 31.97000  ?  301 RET A C18 1 
HETATM 3186 C  C19 A RET B 2 .   ? 26.07100 36.46500 3.20800   0.710 14.55000  ?  301 RET A C19 1 
HETATM 3187 C  C19 B RET B 2 .   ? 25.91900 36.80700 3.15900   0.290 22.77000  ?  301 RET A C19 1 
HETATM 3188 C  C20 A RET B 2 .   ? 30.66200 38.08100 0.99400   0.710 25.22000  ?  301 RET A C20 1 
HETATM 3189 C  C20 B RET B 2 .   ? 30.53000 39.05300 1.21400   0.290 29.75000  ?  301 RET A C20 1 
HETATM 3190 CL CL  A CL  C 3 .   ? 30.77200 24.55000 3.41300   0.670 30.00000  ?  302 CL  A CL  1 
HETATM 3191 O  O   A HOH D 4 .   ? 24.66300 55.77400 13.47900  0.670 61.38000  ?  401 HOH A O   1 
HETATM 3192 O  O   B HOH D 4 .   ? 24.69300 56.35300 12.53400  0.330 55.75000  ?  401 HOH A O   1 
HETATM 3193 O  O   A HOH D 4 .   ? 36.99200 31.01200 1.13000   0.670 42.80000  ?  402 HOH A O   1 
HETATM 3194 O  O   B HOH D 4 .   ? 34.53500 31.85300 1.19200   0.330 29.17000  ?  402 HOH A O   1 
HETATM 3195 O  O   A HOH D 4 .   ? 35.95200 34.23200 -0.16400  0.670 44.88000  ?  403 HOH A O   1 
HETATM 3196 O  O   A HOH D 4 .   ? 41.41300 17.93700 5.00500   0.670 45.94000  ?  404 HOH A O   1 
HETATM 3197 O  O   B HOH D 4 .   ? 41.67700 18.37100 4.99500   0.330 48.84000  ?  404 HOH A O   1 
HETATM 3198 O  O   A HOH D 4 .   ? 34.53000 30.05600 0.39700   0.670 38.71000  ?  405 HOH A O   1 
HETATM 3199 O  O   A HOH D 4 .   ? 30.22200 42.51800 -1.17800  0.670 23.89000  ?  406 HOH A O   1 
HETATM 3200 O  O   B HOH D 4 .   ? 31.39000 43.53900 -0.69200  0.330 35.00000  ?  406 HOH A O   1 
HETATM 3201 O  O   A HOH D 4 .   ? 31.97500 38.23800 11.34100  0.670 46.43000  ?  407 HOH A O   1 
HETATM 3202 O  O   B HOH D 4 .   ? 32.15500 39.12500 11.37700  0.330 37.94000  ?  407 HOH A O   1 
HETATM 3203 O  O   A HOH D 4 .   ? 30.34800 16.61500 -7.05300  0.670 39.05000  ?  408 HOH A O   1 
HETATM 3204 O  O   B HOH D 4 .   ? 30.19000 17.05300 -7.21400  0.330 38.75000  ?  408 HOH A O   1 
HETATM 3205 O  O   A HOH D 4 .   ? 34.00600 27.96400 -2.63400  0.670 45.70000  ?  409 HOH A O   1 
HETATM 3206 O  O   B HOH D 4 .   ? 34.52200 27.38000 -3.02700  0.330 40.61000  ?  409 HOH A O   1 
HETATM 3207 O  O   A HOH D 4 .   ? 30.12800 22.12000 1.41500   0.670 49.80000  ?  410 HOH A O   1 
HETATM 3208 O  O   B HOH D 4 .   ? 28.98600 23.07200 1.35000   0.330 45.83000  ?  410 HOH A O   1 
HETATM 3209 O  O   A HOH D 4 .   ? 22.01200 14.41100 -5.08800  0.670 71.21000  ?  411 HOH A O   1 
HETATM 3210 O  O   B HOH D 4 .   ? 22.61400 15.00600 -4.92100  0.330 71.14000  ?  411 HOH A O   1 
HETATM 3211 O  O   A HOH D 4 .   ? 37.24900 55.22800 -2.42100  0.670 55.20000  ?  412 HOH A O   1 
HETATM 3212 O  O   B HOH D 4 .   ? 36.68700 55.22100 -2.31300  0.330 54.55000  ?  412 HOH A O   1 
HETATM 3213 O  O   A HOH D 4 .   ? 36.54300 45.36400 11.93600  0.670 57.29000  ?  413 HOH A O   1 
HETATM 3214 O  O   B HOH D 4 .   ? 37.26400 43.14400 11.75400  0.330 57.29000  ?  413 HOH A O   1 
HETATM 3215 O  O   A HOH D 4 .   ? 17.18600 34.36500 3.65200   0.670 48.05000  ?  414 HOH A O   1 
HETATM 3216 O  O   B HOH D 4 .   ? 17.31300 33.47100 3.49400   0.330 48.05000  ?  414 HOH A O   1 
HETATM 3217 O  O   A HOH D 4 .   ? 35.33100 32.33700 -12.23600 0.670 62.97000  ?  415 HOH A O   1 
HETATM 3218 O  O   B HOH D 4 .   ? 34.26900 30.22500 -11.84400 0.330 62.97000  ?  415 HOH A O   1 
# 
